data_7IA1
# 
_entry.id   7IA1 
# 
_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   7IA1         pdb_00007ia1 10.2210/pdb7ia1/pdb 
WWPDB D_1001408504 ?            ?                   
# 
_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                        7IA1 
_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 'N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrazolo[3,4-c]pyridine-4-carboxamide' 279.297   1  ? ?    ? ? 
5 water       nat water                                                                       18.015    58 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                        DMS   
4 'N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrazolo[3,4-c]pyridine-4-carboxamide' A1B8K 
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 
A1B8K non-polymer         . 'N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrazolo[3,4-c]pyridine-4-carboxamide' ? 'C15 H13 N5 O'   279.297 
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 A1B8K 1  202 203 A1B8K LIG B . 
E 5 HOH   1  101 118 HOH   HOH A . 
E 5 HOH   2  102 34  HOH   HOH A . 
E 5 HOH   3  103 16  HOH   HOH A . 
E 5 HOH   4  104 98  HOH   HOH A . 
E 5 HOH   5  105 129 HOH   HOH A . 
E 5 HOH   6  106 29  HOH   HOH A . 
E 5 HOH   7  107 124 HOH   HOH A . 
E 5 HOH   8  108 50  HOH   HOH A . 
E 5 HOH   9  109 27  HOH   HOH A . 
F 5 HOH   1  301 14  HOH   HOH B . 
F 5 HOH   2  302 11  HOH   HOH B . 
F 5 HOH   3  303 57  HOH   HOH B . 
F 5 HOH   4  304 92  HOH   HOH B . 
F 5 HOH   5  305 9   HOH   HOH B . 
F 5 HOH   6  306 46  HOH   HOH B . 
F 5 HOH   7  307 1   HOH   HOH B . 
F 5 HOH   8  308 90  HOH   HOH B . 
F 5 HOH   9  309 127 HOH   HOH B . 
F 5 HOH   10 310 58  HOH   HOH B . 
F 5 HOH   11 311 4   HOH   HOH B . 
F 5 HOH   12 312 117 HOH   HOH B . 
F 5 HOH   13 313 123 HOH   HOH B . 
F 5 HOH   14 314 100 HOH   HOH B . 
F 5 HOH   15 315 56  HOH   HOH B . 
F 5 HOH   16 316 51  HOH   HOH B . 
F 5 HOH   17 317 36  HOH   HOH B . 
F 5 HOH   18 318 20  HOH   HOH B . 
F 5 HOH   19 319 126 HOH   HOH B . 
F 5 HOH   20 320 116 HOH   HOH B . 
F 5 HOH   21 321 28  HOH   HOH B . 
F 5 HOH   22 322 128 HOH   HOH B . 
F 5 HOH   23 323 115 HOH   HOH B . 
F 5 HOH   24 324 69  HOH   HOH B . 
F 5 HOH   25 325 54  HOH   HOH B . 
F 5 HOH   26 326 68  HOH   HOH B . 
F 5 HOH   27 327 2   HOH   HOH B . 
F 5 HOH   28 328 24  HOH   HOH B . 
F 5 HOH   29 329 61  HOH   HOH B . 
F 5 HOH   30 330 89  HOH   HOH B . 
F 5 HOH   31 331 5   HOH   HOH B . 
F 5 HOH   32 332 3   HOH   HOH B . 
F 5 HOH   33 333 108 HOH   HOH B . 
F 5 HOH   34 334 62  HOH   HOH B . 
F 5 HOH   35 335 107 HOH   HOH B . 
F 5 HOH   36 336 64  HOH   HOH B . 
F 5 HOH   37 337 35  HOH   HOH B . 
F 5 HOH   38 338 125 HOH   HOH B . 
F 5 HOH   39 339 105 HOH   HOH B . 
F 5 HOH   40 340 43  HOH   HOH B . 
F 5 HOH   41 341 102 HOH   HOH B . 
F 5 HOH   42 342 94  HOH   HOH B . 
F 5 HOH   43 343 87  HOH   HOH B . 
F 5 HOH   44 344 49  HOH   HOH B . 
F 5 HOH   45 345 72  HOH   HOH B . 
F 5 HOH   46 346 79  HOH   HOH B . 
F 5 HOH   47 347 44  HOH   HOH B . 
F 5 HOH   48 348 59  HOH   HOH B . 
F 5 HOH   49 349 75  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (23-JAN-2024)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.7.15                 02/11/23        program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7IA1 
_cell.length_a           42.753 
_cell.length_b           42.753 
_cell.length_c           217.159 
_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                         7IA1 
_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          7IA1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.120 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   42.52 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IA1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             217.160 
_reflns.d_resolution_high            2.530 
_reflns.number_obs                   7448 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.387 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.400 
_reflns.B_iso_Wilson_estimate        74.860 
_reflns.pdbx_redundancy              24.500 
_reflns.pdbx_Rrim_I_all              0.395 
_reflns.pdbx_Rpim_I_all              0.079 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     182757 
_reflns.pdbx_scaling_rejects         209 
_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 2.530 2.690   ? 29827 ? ? 5.604 ? ? ? 26.200 ? 0.700  ? 1140 ? ? ? ? 100.000 5.714 1.104 0.533 ? 
1 2 7.600 217.160 ? 6209  ? ? 0.093 ? ? ? 17.100 ? 21.300 ? 363  ? ? ? ? 99.900  0.096 0.023 0.995 ? 
# 
_refine.entry_id                                 7IA1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.5330 
_refine.ls_d_res_low                             54.2900 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6000 
_refine.ls_number_reflns_obs                     7355 
_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                          0.2221 
_refine.ls_R_factor_R_work                       0.2179 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.3034 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.7300 
_refine.ls_number_reflns_R_free                  348 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               68.8300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -5.6710 
_refine.aniso_B[2][2]                            -5.6710 
_refine.aniso_B[3][3]                            11.3420 
_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               0.9380 
_refine.correlation_coeff_Fo_to_Fc_free          0.8800 
_refine.overall_SU_R_Cruickshank_DPI             0.6880 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.3560 
_refine.pdbx_overall_SU_R_Blow_DPI               1.5940 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.3720 
_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                                124.820 
_refine.B_iso_min                                42.670 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7IA1 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.340 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.5330 
_refine_hist.d_res_low                        54.2900 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             58 
_refine_hist.number_atoms_total               1559 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           68.40 
_refine_hist.pdbx_B_iso_mean_solvent          61.52 
_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        534  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              269  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1562 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 194  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1181 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1562 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2126 0.890  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.690  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    17.550 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.5300 
_refine_ls_shell.d_res_low                        2.5900 
_refine_ls_shell.pdbx_total_number_of_bins_used   18 
_refine_ls_shell.percent_reflns_obs               96.4200 
_refine_ls_shell.number_reflns_R_work             417 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3384 
_refine_ls_shell.R_factor_R_free                  0.3755 
_refine_ls_shell.percent_reflns_R_free            3.7000 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                433 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IA1 
_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-0029758-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IA1 
_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 7IA1 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IA1 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 7IA1 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IA1 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IA1 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IA1 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)' 4210 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9730 ? 
# 
_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 ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
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 ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O ILE B 138 ? O ILE B 147 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O 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                   7IA1 
_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 ? ? -114.51 -159.40 
2 1 CYS B 80 ? ? 74.88   -23.43  
3 1 LEU B 92 ? ? -133.08 -35.78  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     347 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.6850 -1.6028 -19.3809 -0.1686 -0.1494 -0.3249 0.1702 0.1670 0.1340 5.2903 6.0791 6.0285 
-2.0649 1.4470 1.6763  0.5100 -0.4708 -0.0392 0.6427 0.3495 -0.5969 -0.6788 -0.1885 0.6321 
'X-RAY DIFFRACTION' 2 ? refined -18.6965 0.8814  -15.6814 0.0916  -0.0432 -0.1662 0.2031 0.0095 0.0261 2.5926 2.9899 3.0242 
-1.1506 1.2674 -0.1001 0.4261 -0.3656 -0.0605 0.1906 0.1102 -0.0284 -0.2323 0.0255  0.1927 
# 
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 
A1B8K N1   N N N 1   
A1B8K N3   N Y N 2   
A1B8K C4   C Y N 3   
A1B8K C5   C Y N 4   
A1B8K C6   C Y N 5   
A1B8K C7   C Y N 6   
A1B8K C8   C N N 7   
A1B8K C10  C Y N 8   
A1B8K C13  C Y N 9   
A1B8K C15  C Y N 10  
A1B8K O1   O N N 11  
A1B8K C1   C N N 12  
A1B8K C2   C Y N 13  
A1B8K C3   C Y N 14  
A1B8K N2   N N N 15  
A1B8K C9   C N N 16  
A1B8K C11  C Y N 17  
A1B8K C12  C Y N 18  
A1B8K N4   N Y N 19  
A1B8K N5   N Y N 20  
A1B8K C14  C Y N 21  
A1B8K H1   H N N 22  
A1B8K H3   H N N 23  
A1B8K H4   H N N 24  
A1B8K H5   H N N 25  
A1B8K H6   H N N 26  
A1B8K H2   H N N 27  
A1B8K H7   H N N 28  
A1B8K H8   H N N 29  
A1B8K H9   H N N 30  
A1B8K H10  H N N 31  
A1B8K H11  H N N 32  
A1B8K H12  H N N 33  
A1B8K H13  H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
DMS   S    S N N 122 
DMS   O    O N N 123 
DMS   C1   C N N 124 
DMS   C2   C N N 125 
DMS   H11  H N N 126 
DMS   H12  H N N 127 
DMS   H13  H N N 128 
DMS   H21  H N N 129 
DMS   H22  H N N 130 
DMS   H23  H N N 131 
GLN   N    N N N 132 
GLN   CA   C N S 133 
GLN   C    C N N 134 
GLN   O    O N N 135 
GLN   CB   C N N 136 
GLN   CG   C N N 137 
GLN   CD   C N N 138 
GLN   OE1  O N N 139 
GLN   NE2  N N N 140 
GLN   OXT  O N N 141 
GLN   H    H N N 142 
GLN   H2   H N N 143 
GLN   HA   H N N 144 
GLN   HB2  H N N 145 
GLN   HB3  H N N 146 
GLN   HG2  H N N 147 
GLN   HG3  H N N 148 
GLN   HE21 H N N 149 
GLN   HE22 H N N 150 
GLN   HXT  H N N 151 
GLU   N    N N N 152 
GLU   CA   C N S 153 
GLU   C    C N N 154 
GLU   O    O N N 155 
GLU   CB   C N N 156 
GLU   CG   C N N 157 
GLU   CD   C N N 158 
GLU   OE1  O N N 159 
GLU   OE2  O N N 160 
GLU   OXT  O N N 161 
GLU   H    H N N 162 
GLU   H2   H N N 163 
GLU   HA   H N N 164 
GLU   HB2  H N N 165 
GLU   HB3  H N N 166 
GLU   HG2  H N N 167 
GLU   HG3  H N N 168 
GLU   HE2  H N N 169 
GLU   HXT  H N N 170 
GLY   N    N N N 171 
GLY   CA   C N N 172 
GLY   C    C N N 173 
GLY   O    O N N 174 
GLY   OXT  O N N 175 
GLY   H    H N N 176 
GLY   H2   H N N 177 
GLY   HA2  H N N 178 
GLY   HA3  H N N 179 
GLY   HXT  H N N 180 
HIS   N    N N N 181 
HIS   CA   C N S 182 
HIS   C    C N N 183 
HIS   O    O N N 184 
HIS   CB   C N N 185 
HIS   CG   C Y N 186 
HIS   ND1  N Y N 187 
HIS   CD2  C Y N 188 
HIS   CE1  C Y N 189 
HIS   NE2  N Y N 190 
HIS   OXT  O N N 191 
HIS   H    H N N 192 
HIS   H2   H N N 193 
HIS   HA   H N N 194 
HIS   HB2  H N N 195 
HIS   HB3  H N N 196 
HIS   HD1  H N N 197 
HIS   HD2  H N N 198 
HIS   HE1  H N N 199 
HIS   HE2  H N N 200 
HIS   HXT  H N N 201 
HOH   O    O N N 202 
HOH   H1   H N N 203 
HOH   H2   H N N 204 
ILE   N    N N N 205 
ILE   CA   C N S 206 
ILE   C    C N N 207 
ILE   O    O N N 208 
ILE   CB   C N S 209 
ILE   CG1  C N N 210 
ILE   CG2  C N N 211 
ILE   CD1  C N N 212 
ILE   OXT  O N N 213 
ILE   H    H N N 214 
ILE   H2   H N N 215 
ILE   HA   H N N 216 
ILE   HB   H N N 217 
ILE   HG12 H N N 218 
ILE   HG13 H N N 219 
ILE   HG21 H N N 220 
ILE   HG22 H N N 221 
ILE   HG23 H N N 222 
ILE   HD11 H N N 223 
ILE   HD12 H N N 224 
ILE   HD13 H N N 225 
ILE   HXT  H N N 226 
LEU   N    N N N 227 
LEU   CA   C N S 228 
LEU   C    C N N 229 
LEU   O    O N N 230 
LEU   CB   C N N 231 
LEU   CG   C N N 232 
LEU   CD1  C N N 233 
LEU   CD2  C N N 234 
LEU   OXT  O N N 235 
LEU   H    H N N 236 
LEU   H2   H N N 237 
LEU   HA   H N N 238 
LEU   HB2  H N N 239 
LEU   HB3  H N N 240 
LEU   HG   H N N 241 
LEU   HD11 H N N 242 
LEU   HD12 H N N 243 
LEU   HD13 H N N 244 
LEU   HD21 H N N 245 
LEU   HD22 H N N 246 
LEU   HD23 H N N 247 
LEU   HXT  H N N 248 
LYS   N    N N N 249 
LYS   CA   C N S 250 
LYS   C    C N N 251 
LYS   O    O N N 252 
LYS   CB   C N N 253 
LYS   CG   C N N 254 
LYS   CD   C N N 255 
LYS   CE   C N N 256 
LYS   NZ   N N N 257 
LYS   OXT  O N N 258 
LYS   H    H N N 259 
LYS   H2   H N N 260 
LYS   HA   H N N 261 
LYS   HB2  H N N 262 
LYS   HB3  H N N 263 
LYS   HG2  H N N 264 
LYS   HG3  H N N 265 
LYS   HD2  H N N 266 
LYS   HD3  H N N 267 
LYS   HE2  H N N 268 
LYS   HE3  H N N 269 
LYS   HZ1  H N N 270 
LYS   HZ2  H N N 271 
LYS   HZ3  H N N 272 
LYS   HXT  H N N 273 
MET   N    N N N 274 
MET   CA   C N S 275 
MET   C    C N N 276 
MET   O    O N N 277 
MET   CB   C N N 278 
MET   CG   C N N 279 
MET   SD   S N N 280 
MET   CE   C N N 281 
MET   OXT  O N N 282 
MET   H    H N N 283 
MET   H2   H N N 284 
MET   HA   H N N 285 
MET   HB2  H N N 286 
MET   HB3  H N N 287 
MET   HG2  H N N 288 
MET   HG3  H N N 289 
MET   HE1  H N N 290 
MET   HE2  H N N 291 
MET   HE3  H N N 292 
MET   HXT  H N N 293 
PHE   N    N N N 294 
PHE   CA   C N S 295 
PHE   C    C N N 296 
PHE   O    O N N 297 
PHE   CB   C N N 298 
PHE   CG   C Y N 299 
PHE   CD1  C Y N 300 
PHE   CD2  C Y N 301 
PHE   CE1  C Y N 302 
PHE   CE2  C Y N 303 
PHE   CZ   C Y N 304 
PHE   OXT  O N N 305 
PHE   H    H N N 306 
PHE   H2   H N N 307 
PHE   HA   H N N 308 
PHE   HB2  H N N 309 
PHE   HB3  H N N 310 
PHE   HD1  H N N 311 
PHE   HD2  H N N 312 
PHE   HE1  H N N 313 
PHE   HE2  H N N 314 
PHE   HZ   H N N 315 
PHE   HXT  H N N 316 
PRO   N    N N N 317 
PRO   CA   C N S 318 
PRO   C    C N N 319 
PRO   O    O N N 320 
PRO   CB   C N N 321 
PRO   CG   C N N 322 
PRO   CD   C N N 323 
PRO   OXT  O N N 324 
PRO   H    H N N 325 
PRO   HA   H N N 326 
PRO   HB2  H N N 327 
PRO   HB3  H N N 328 
PRO   HG2  H N N 329 
PRO   HG3  H N N 330 
PRO   HD2  H N N 331 
PRO   HD3  H N N 332 
PRO   HXT  H N N 333 
SER   N    N N N 334 
SER   CA   C N S 335 
SER   C    C N N 336 
SER   O    O N N 337 
SER   CB   C N N 338 
SER   OG   O N N 339 
SER   OXT  O N N 340 
SER   H    H N N 341 
SER   H2   H N N 342 
SER   HA   H N N 343 
SER   HB2  H N N 344 
SER   HB3  H N N 345 
SER   HG   H N N 346 
SER   HXT  H N N 347 
THR   N    N N N 348 
THR   CA   C N S 349 
THR   C    C N N 350 
THR   O    O N N 351 
THR   CB   C N R 352 
THR   OG1  O N N 353 
THR   CG2  C N N 354 
THR   OXT  O N N 355 
THR   H    H N N 356 
THR   H2   H N N 357 
THR   HA   H N N 358 
THR   HB   H N N 359 
THR   HG1  H N N 360 
THR   HG21 H N N 361 
THR   HG22 H N N 362 
THR   HG23 H N N 363 
THR   HXT  H N N 364 
TRP   N    N N N 365 
TRP   CA   C N S 366 
TRP   C    C N N 367 
TRP   O    O N N 368 
TRP   CB   C N N 369 
TRP   CG   C Y N 370 
TRP   CD1  C Y N 371 
TRP   CD2  C Y N 372 
TRP   NE1  N Y N 373 
TRP   CE2  C Y N 374 
TRP   CE3  C Y N 375 
TRP   CZ2  C Y N 376 
TRP   CZ3  C Y N 377 
TRP   CH2  C Y N 378 
TRP   OXT  O N N 379 
TRP   H    H N N 380 
TRP   H2   H N N 381 
TRP   HA   H N N 382 
TRP   HB2  H N N 383 
TRP   HB3  H N N 384 
TRP   HD1  H N N 385 
TRP   HE1  H N N 386 
TRP   HE3  H N N 387 
TRP   HZ2  H N N 388 
TRP   HZ3  H N N 389 
TRP   HH2  H N N 390 
TRP   HXT  H N N 391 
TYR   N    N N N 392 
TYR   CA   C N S 393 
TYR   C    C N N 394 
TYR   O    O N N 395 
TYR   CB   C N N 396 
TYR   CG   C Y N 397 
TYR   CD1  C Y N 398 
TYR   CD2  C Y N 399 
TYR   CE1  C Y N 400 
TYR   CE2  C Y N 401 
TYR   CZ   C Y N 402 
TYR   OH   O N N 403 
TYR   OXT  O N N 404 
TYR   H    H N N 405 
TYR   H2   H N N 406 
TYR   HA   H N N 407 
TYR   HB2  H N N 408 
TYR   HB3  H N N 409 
TYR   HD1  H N N 410 
TYR   HD2  H N N 411 
TYR   HE1  H N N 412 
TYR   HE2  H N N 413 
TYR   HH   H N N 414 
TYR   HXT  H N N 415 
VAL   N    N N N 416 
VAL   CA   C N S 417 
VAL   C    C N N 418 
VAL   O    O N N 419 
VAL   CB   C N N 420 
VAL   CG1  C N N 421 
VAL   CG2  C N N 422 
VAL   OXT  O N N 423 
VAL   H    H N N 424 
VAL   H2   H N N 425 
VAL   HA   H N N 426 
VAL   HB   H N N 427 
VAL   HG11 H N N 428 
VAL   HG12 H N N 429 
VAL   HG13 H N N 430 
VAL   HG21 H N N 431 
VAL   HG22 H N N 432 
VAL   HG23 H N N 433 
VAL   HXT  H N N 434 
# 
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 
A1B8K O1  C1   doub N N 1   
A1B8K C1  N1   sing N N 2   
A1B8K N1  C2   sing N N 3   
A1B8K C2  C3   doub Y N 4   
A1B8K C3  C4   sing Y N 5   
A1B8K C4  C5   doub Y N 6   
A1B8K C5  C6   sing Y N 7   
A1B8K C6  C7   doub Y N 8   
A1B8K C6  C8   sing N N 9   
A1B8K C8  N2   sing N N 10  
A1B8K N2  C9   sing N N 11  
A1B8K C1  C10  sing N N 12  
A1B8K C10 C11  doub Y N 13  
A1B8K C11 N3   sing Y N 14  
A1B8K N3  C12  doub Y N 15  
A1B8K C12 C13  sing Y N 16  
A1B8K C13 N4   sing Y N 17  
A1B8K N4  N5   sing Y N 18  
A1B8K N5  C14  doub Y N 19  
A1B8K C14 C15  sing Y N 20  
A1B8K C2  C7   sing Y N 21  
A1B8K C10 C15  sing Y N 22  
A1B8K C5  C9   sing N N 23  
A1B8K C13 C15  doub Y N 24  
A1B8K N1  H1   sing N N 25  
A1B8K C4  H3   sing N N 26  
A1B8K C7  H4   sing N N 27  
A1B8K C8  H5   sing N N 28  
A1B8K C8  H6   sing N N 29  
A1B8K C3  H2   sing N N 30  
A1B8K N2  H7   sing N N 31  
A1B8K C9  H8   sing N N 32  
A1B8K C9  H9   sing N N 33  
A1B8K C11 H10  sing N N 34  
A1B8K C12 H11  sing N N 35  
A1B8K N4  H12  sing N N 36  
A1B8K C14 H13  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_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                    7IA1 
_atom_sites.fract_transf_matrix[1][1]   0.023390 
_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]   0.023390 
_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]   0.004605 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -21.732 19.602  -7.289  1.00 72.03  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.674 18.486  -7.357  1.00 72.29  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.710 17.836  -8.743  1.00 70.94  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.860 18.528  -9.754  1.00 71.18  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -24.086 18.925  -6.916  1.00 75.31  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.862 17.866  -6.137  1.00 82.39  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.256 16.829  -5.764  1.00 83.79  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -26.074 18.075  -5.894  1.00 85.15  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.576 16.499  -8.778  1.00 69.12  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.596 15.714  -10.008 1.00 67.80  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -24.014 15.469  -10.515 1.00 66.53  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.965 15.506  -9.731  1.00 66.34  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.881 14.367  -9.806  1.00 68.07  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.386 14.492  -9.669  1.00 69.21  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.594 12.907  -9.323  1.00 69.55  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.925 13.455  -8.978  1.00 67.63  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.148 15.203  -11.837 1.00 65.35  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.426 14.940  -12.488 1.00 64.88  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.311 13.971  -13.654 1.00 64.13  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.248 13.864  -14.258 1.00 64.00  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.116 16.240  -12.932 1.00 65.23  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.372 17.031  -13.984 1.00 66.85  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.448 18.005  -13.626 1.00 68.17  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.662 16.876  -15.334 1.00 68.07  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.783 18.760  -14.588 1.00 69.35  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.006 17.625  -16.306 1.00 69.20  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -24.068 18.569  -15.929 1.00 70.47  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.397 19.292  -16.887 1.00 72.30  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.416 13.284  -14.001 1.00 63.29  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.398 12.341  -15.114 1.00 62.68  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.232 12.814  -16.334 1.00 63.24  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.197 13.570  -16.188 1.00 63.20  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.773 10.907  -14.673 1.00 62.06  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.226 10.810  -14.199 1.00 62.19  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.788 10.380  -13.632 1.00 62.08  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.704 9.413   -14.062 1.00 62.76  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.818 12.383  -17.545 1.00 63.44  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.472 12.705  -18.820 1.00 64.22  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.518 11.453  -19.680 1.00 64.84  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.500 10.772  -19.811 1.00 65.17  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.675 13.750  -19.605 1.00 66.32  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.779 15.166  -19.095 1.00 71.66  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.972 16.158  -19.910 1.00 79.37  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -25.035 15.730  -20.625 1.00 79.56  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -26.279 17.370  -19.831 1.00 83.45  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.655 11.186  -20.334 1.00 64.47  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.782 10.004  -21.171 1.00 64.60  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.810 10.033  -22.328 1.00 65.72  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.600 11.089  -22.918 1.00 66.52  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -30.216 9.854   -21.670 1.00 65.02  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.480 8.501   -22.293 1.00 66.65  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.682 7.796   -21.679 1.00 68.16  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.722 6.365   -21.997 1.00 69.35  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -32.031 5.872   -23.193 1.00 70.82  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -32.299 6.687   -24.204 1.00 70.92  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.030 4.562   -23.398 1.00 70.03  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -27.185 8.896   -22.632 1.00 65.80  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -26.244 8.793   -23.743 1.00 66.79  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.655 7.769   -24.811 1.00 67.83  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -26.016 7.716   -25.856 1.00 68.06  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.843 8.485   -23.236 1.00 67.07  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.676 6.952   -24.546 1.00 68.35  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -28.142 5.980   -25.528 1.00 69.25  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.668 4.670   -24.981 1.00 70.07  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.720 4.472   -23.765 1.00 70.15  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -29.078 3.766   -25.895 1.00 70.28  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.584 2.438   -25.554 1.00 70.93  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.446 1.443   -25.385 1.00 72.01  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.363 1.635   -25.943 1.00 72.01  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.502 1.917   -26.664 1.00 72.07  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.837 2.604   -26.774 1.00 76.88  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -32.073 3.575   -26.015 1.00 77.59  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.639 2.201   -27.644 1.00 78.79  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.703 0.349   -24.660 1.00 72.66  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.702 -0.685  -24.495 1.00 73.79  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -28.065 -1.887  -25.361 1.00 75.68  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.844 -2.757  -24.963 1.00 75.47  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.438 -1.003  -23.018 1.00 73.91  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.887 0.244   -22.309 1.00 74.64  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.472 -2.146  -22.896 1.00 74.27  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.814 0.148   -20.823 1.00 75.77  ? 59  ILE   A CD1 1 
ATOM   82   N N   . THR   A 1 17  ? -27.562 -1.859  -26.610 1.00 77.34  ? 60  THR   A N   1 
ATOM   83   C CA  . THR   A 1 17  ? -27.753 -2.903  -27.616 1.00 79.22  ? 60  THR   A CA  1 
ATOM   84   C C   . THR   A 1 17  ? -26.430 -3.262  -28.283 1.00 80.36  ? 60  THR   A C   1 
ATOM   85   O O   . THR   A 1 17  ? -25.556 -2.410  -28.427 1.00 80.34  ? 60  THR   A O   1 
ATOM   86   C CB  . THR   A 1 17  ? -28.736 -2.452  -28.715 1.00 81.09  ? 60  THR   A CB  1 
ATOM   87   O OG1 . THR   A 1 17  ? -28.164 -1.386  -29.488 1.00 82.53  ? 60  THR   A OG1 1 
ATOM   88   C CG2 . THR   A 1 17  ? -30.106 -2.071  -28.171 1.00 81.41  ? 60  THR   A CG2 1 
ATOM   89   N N   . TRP   A 1 18  ? -26.316 -4.497  -28.755 1.00 81.34  ? 61  TRP   A N   1 
ATOM   90   C CA  . TRP   A 1 18  ? -25.136 -4.936  -29.488 1.00 83.12  ? 61  TRP   A CA  1 
ATOM   91   C C   . TRP   A 1 18  ? -25.252 -4.419  -30.930 1.00 85.26  ? 61  TRP   A C   1 
ATOM   92   O O   . TRP   A 1 18  ? -26.332 -4.473  -31.518 1.00 84.95  ? 61  TRP   A O   1 
ATOM   93   C CB  . TRP   A 1 18  ? -25.075 -6.473  -29.466 1.00 83.09  ? 61  TRP   A CB  1 
ATOM   94   C CG  . TRP   A 1 18  ? -23.987 -7.110  -30.284 1.00 83.92  ? 61  TRP   A CG  1 
ATOM   95   C CD1 . TRP   A 1 18  ? -24.046 -7.447  -31.606 1.00 84.99  ? 61  TRP   A CD1 1 
ATOM   96   C CD2 . TRP   A 1 18  ? -22.761 -7.668  -29.785 1.00 84.05  ? 61  TRP   A CD2 1 
ATOM   97   N NE1 . TRP   A 1 18  ? -22.896 -8.102  -31.981 1.00 85.33  ? 61  TRP   A NE1 1 
ATOM   98   C CE2 . TRP   A 1 18  ? -22.098 -8.267  -30.877 1.00 84.94  ? 61  TRP   A CE2 1 
ATOM   99   C CE3 . TRP   A 1 18  ? -22.132 -7.667  -28.537 1.00 84.33  ? 61  TRP   A CE3 1 
ATOM   100  C CZ2 . TRP   A 1 18  ? -20.848 -8.873  -30.747 1.00 85.41  ? 61  TRP   A CZ2 1 
ATOM   101  C CZ3 . TRP   A 1 18  ? -20.915 -8.302  -28.403 1.00 85.18  ? 61  TRP   A CZ3 1 
ATOM   102  C CH2 . TRP   A 1 18  ? -20.271 -8.868  -29.503 1.00 85.44  ? 61  TRP   A CH2 1 
ATOM   103  N N   . GLU   A 1 19  ? -24.154 -3.910  -31.499 1.00 87.31  ? 62  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 19  ? -24.155 -3.427  -32.877 1.00 89.85  ? 62  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 19  ? -23.483 -4.441  -33.805 1.00 92.20  ? 62  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 19  ? -22.285 -4.675  -33.672 1.00 92.27  ? 62  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 19  ? -23.428 -2.073  -32.998 1.00 92.66  ? 62  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 19  ? -23.386 -1.546  -34.431 1.00 99.14  ? 62  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 19  ? -22.276 -0.571  -34.782 1.00 106.47 ? 62  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 19  ? -21.710 0.043   -33.849 1.00 108.51 ? 62  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 19  ? -21.978 -0.414  -35.990 1.00 108.12 ? 62  GLU   A OE2 1 
ATOM   112  N N   . LYS   A 1 20  ? -24.231 -5.016  -34.756 1.00 94.06  ? 63  LYS   A N   1 
ATOM   113  C CA  . LYS   A 1 20  ? -23.637 -5.936  -35.728 1.00 96.55  ? 63  LYS   A CA  1 
ATOM   114  C C   . LYS   A 1 20  ? -22.764 -5.110  -36.669 1.00 99.09  ? 63  LYS   A C   1 
ATOM   115  O O   . LYS   A 1 20  ? -23.162 -4.008  -37.054 1.00 99.42  ? 63  LYS   A O   1 
ATOM   116  C CB  . LYS   A 1 20  ? -24.717 -6.637  -36.571 1.00 98.65  ? 63  LYS   A CB  1 
ATOM   117  C CG  . LYS   A 1 20  ? -25.778 -7.390  -35.784 1.00 103.08 ? 63  LYS   A CG  1 
ATOM   118  C CD  . LYS   A 1 20  ? -26.760 -8.068  -36.740 1.00 107.42 ? 63  LYS   A CD  1 
ATOM   119  C CE  . LYS   A 1 20  ? -28.005 -8.588  -36.061 1.00 111.17 ? 63  LYS   A CE  1 
ATOM   120  N NZ  . LYS   A 1 20  ? -28.871 -9.333  -37.016 1.00 113.78 ? 63  LYS   A NZ  1 
ATOM   121  N N   . ASP   A 1 21  ? -21.597 -5.643  -37.063 1.00 100.80 ? 64  ASP   A N   1 
ATOM   122  C CA  . ASP   A 1 21  ? -20.682 -4.949  -37.983 1.00 102.69 ? 64  ASP   A CA  1 
ATOM   123  C C   . ASP   A 1 21  ? -20.061 -3.698  -37.359 1.00 103.17 ? 64  ASP   A C   1 
ATOM   124  O O   . ASP   A 1 21  ? -19.928 -2.662  -38.023 1.00 103.55 ? 64  ASP   A O   1 
ATOM   125  C CB  . ASP   A 1 21  ? -21.338 -4.623  -39.344 1.00 105.50 ? 64  ASP   A CB  1 
ATOM   126  C CG  . ASP   A 1 21  ? -21.496 -5.821  -40.258 1.00 112.39 ? 64  ASP   A CG  1 
ATOM   127  O OD1 . ASP   A 1 21  ? -20.554 -6.643  -40.328 1.00 114.39 ? 64  ASP   A OD1 1 
ATOM   128  O OD2 . ASP   A 1 21  ? -22.555 -5.928  -40.919 1.00 114.42 ? 64  ASP   A OD2 1 
ATOM   129  N N   . ALA   A 1 22  ? -19.690 -3.800  -36.082 1.00 102.71 ? 65  ALA   A N   1 
ATOM   130  C CA  . ALA   A 1 22  ? -19.023 -2.715  -35.374 1.00 102.75 ? 65  ALA   A CA  1 
ATOM   131  C C   . ALA   A 1 22  ? -17.492 -2.858  -35.563 1.00 102.96 ? 65  ALA   A C   1 
ATOM   132  O O   . ALA   A 1 22  ? -17.017 -3.910  -36.002 1.00 102.86 ? 65  ALA   A O   1 
ATOM   133  C CB  . ALA   A 1 22  ? -19.393 -2.758  -33.897 1.00 102.52 ? 65  ALA   A CB  1 
ATOM   134  N N   . GLU   A 1 23  ? -16.727 -1.798  -35.256 1.00 102.88 ? 66  GLU   A N   1 
ATOM   135  C CA  . GLU   A 1 23  ? -15.270 -1.784  -35.378 1.00 103.08 ? 66  GLU   A CA  1 
ATOM   136  C C   . GLU   A 1 23  ? -14.595 -2.807  -34.438 1.00 101.87 ? 66  GLU   A C   1 
ATOM   137  O O   . GLU   A 1 23  ? -14.570 -2.588  -33.230 1.00 101.75 ? 66  GLU   A O   1 
ATOM   138  C CB  . GLU   A 1 23  ? -14.755 -0.367  -35.079 1.00 106.66 ? 66  GLU   A CB  1 
ATOM   139  C CG  . GLU   A 1 23  ? -13.264 -0.179  -35.288 1.00 113.45 ? 66  GLU   A CG  1 
ATOM   140  C CD  . GLU   A 1 23  ? -12.657 1.005   -34.557 1.00 121.97 ? 66  GLU   A CD  1 
ATOM   141  O OE1 . GLU   A 1 23  ? -13.405 1.744   -33.872 1.00 123.23 ? 66  GLU   A OE1 1 
ATOM   142  O OE2 . GLU   A 1 23  ? -11.422 1.188   -34.666 1.00 124.82 ? 66  GLU   A OE2 1 
ATOM   143  N N   . VAL   A 1 24  ? -14.049 -3.917  -35.001 1.00 100.62 ? 67  VAL   A N   1 
ATOM   144  C CA  . VAL   A 1 24  ? -13.363 -4.976  -34.244 1.00 99.93  ? 67  VAL   A CA  1 
ATOM   145  C C   . VAL   A 1 24  ? -11.887 -4.636  -34.064 1.00 99.60  ? 67  VAL   A C   1 
ATOM   146  O O   . VAL   A 1 24  ? -11.141 -4.653  -35.034 1.00 99.82  ? 67  VAL   A O   1 
ATOM   147  C CB  . VAL   A 1 24  ? -13.516 -6.397  -34.851 1.00 99.97  ? 67  VAL   A CB  1 
ATOM   148  C CG1 . VAL   A 1 24  ? -13.188 -7.453  -33.809 1.00 100.42 ? 67  VAL   A CG1 1 
ATOM   149  C CG2 . VAL   A 1 24  ? -14.911 -6.630  -35.419 1.00 100.12 ? 67  VAL   A CG2 1 
ATOM   150  N N   . THR   A 1 25  ? -11.459 -4.328  -32.832 1.00 98.83  ? 68  THR   A N   1 
ATOM   151  C CA  . THR   A 1 25  ? -10.064 -3.969  -32.561 1.00 98.55  ? 68  THR   A CA  1 
ATOM   152  C C   . THR   A 1 25  ? -9.632  -4.379  -31.148 1.00 98.03  ? 68  THR   A C   1 
ATOM   153  O O   . THR   A 1 25  ? -10.478 -4.677  -30.315 1.00 98.07  ? 68  THR   A O   1 
ATOM   154  C CB  . THR   A 1 25  ? -9.866  -2.458  -32.761 1.00 99.90  ? 68  THR   A CB  1 
ATOM   155  O OG1 . THR   A 1 25  ? -8.471  -2.175  -32.658 1.00 101.07 ? 68  THR   A OG1 1 
ATOM   156  C CG2 . THR   A 1 25  ? -10.617 -1.642  -31.736 1.00 100.08 ? 68  THR   A CG2 1 
ATOM   157  N N   . GLY   A 1 26  ? -8.326  -4.393  -30.884 1.00 97.33  ? 69  GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 26  ? -7.822  -4.720  -29.557 1.00 96.84  ? 69  GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 26  ? -7.312  -6.134  -29.432 1.00 95.88  ? 69  GLY   A C   1 
ATOM   160  O O   . GLY   A 1 26  ? -7.823  -7.049  -30.081 1.00 95.95  ? 69  GLY   A O   1 
ATOM   161  N N   . ASN   A 1 27  ? -6.299  -6.319  -28.588 1.00 94.76  ? 70  ASN   A N   1 
ATOM   162  C CA  . ASN   A 1 27  ? -5.717  -7.637  -28.382 1.00 94.13  ? 70  ASN   A CA  1 
ATOM   163  C C   . ASN   A 1 27  ? -6.319  -8.370  -27.143 1.00 92.63  ? 70  ASN   A C   1 
ATOM   164  O O   . ASN   A 1 27  ? -7.186  -7.818  -26.465 1.00 92.72  ? 70  ASN   A O   1 
ATOM   165  C CB  . ASN   A 1 27  ? -4.177  -7.561  -28.359 1.00 95.67  ? 70  ASN   A CB  1 
ATOM   166  C CG  . ASN   A 1 27  ? -3.584  -6.658  -27.310 1.00 99.41  ? 70  ASN   A CG  1 
ATOM   167  O OD1 . ASN   A 1 27  ? -4.254  -5.802  -26.729 1.00 100.73 ? 70  ASN   A OD1 1 
ATOM   168  N ND2 . ASN   A 1 27  ? -2.295  -6.821  -27.059 1.00 100.08 ? 70  ASN   A ND2 1 
ATOM   169  N N   . SER   A 1 28  ? -5.922  -9.639  -26.904 1.00 91.14  ? 71  SER   A N   1 
ATOM   170  C CA  . SER   A 1 28  ? -6.402  -10.453 -25.775 1.00 90.06  ? 71  SER   A CA  1 
ATOM   171  C C   . SER   A 1 28  ? -5.201  -10.929 -24.940 1.00 88.61  ? 71  SER   A C   1 
ATOM   172  O O   . SER   A 1 28  ? -4.788  -12.084 -25.050 1.00 88.61  ? 71  SER   A O   1 
ATOM   173  C CB  . SER   A 1 28  ? -7.192  -11.663 -26.277 1.00 91.18  ? 71  SER   A CB  1 
ATOM   174  O OG  . SER   A 1 28  ? -8.024  -11.362 -27.384 1.00 93.24  ? 71  SER   A OG  1 
ATOM   175  N N   . PRO   A 1 29  ? -4.612  -10.053 -24.109 1.00 87.44  ? 72  PRO   A N   1 
ATOM   176  C CA  . PRO   A 1 29  ? -3.421  -10.464 -23.354 1.00 86.98  ? 72  PRO   A CA  1 
ATOM   177  C C   . PRO   A 1 29  ? -3.686  -11.148 -22.017 1.00 86.40  ? 72  PRO   A C   1 
ATOM   178  O O   . PRO   A 1 29  ? -4.679  -10.856 -21.367 1.00 86.39  ? 72  PRO   A O   1 
ATOM   179  C CB  . PRO   A 1 29  ? -2.651  -9.153  -23.185 1.00 87.69  ? 72  PRO   A CB  1 
ATOM   180  C CG  . PRO   A 1 29  ? -3.696  -8.075  -23.242 1.00 88.02  ? 72  PRO   A CG  1 
ATOM   181  C CD  . PRO   A 1 29  ? -4.943  -8.632  -23.876 1.00 86.67  ? 72  PRO   A CD  1 
ATOM   182  N N   . ARG   A 1 30  ? -2.780  -12.039 -21.592 1.00 85.86  ? 73  ARG   A N   1 
ATOM   183  C CA  . ARG   A 1 30  ? -2.910  -12.696 -20.291 1.00 85.63  ? 73  ARG   A CA  1 
ATOM   184  C C   . ARG   A 1 30  ? -1.938  -12.031 -19.324 1.00 83.84  ? 73  ARG   A C   1 
ATOM   185  O O   . ARG   A 1 30  ? -0.732  -12.268 -19.387 1.00 83.91  ? 73  ARG   A O   1 
ATOM   186  C CB  . ARG   A 1 30  ? -2.654  -14.202 -20.395 1.00 88.26  ? 73  ARG   A CB  1 
ATOM   187  C CG  . ARG   A 1 30  ? -3.675  -14.911 -21.274 1.00 93.63  ? 73  ARG   A CG  1 
ATOM   188  C CD  . ARG   A 1 30  ? -3.490  -16.417 -21.237 1.00 99.12  ? 73  ARG   A CD  1 
ATOM   189  N NE  . ARG   A 1 30  ? -4.205  -17.079 -22.332 1.00 103.67 ? 73  ARG   A NE  1 
ATOM   190  C CZ  . ARG   A 1 30  ? -5.470  -17.487 -22.264 1.00 106.56 ? 73  ARG   A CZ  1 
ATOM   191  N NH1 . ARG   A 1 30  ? -6.174  -17.312 -21.151 1.00 106.36 ? 73  ARG   A NH1 1 
ATOM   192  N NH2 . ARG   A 1 30  ? -6.038  -18.080 -23.307 1.00 106.40 ? 73  ARG   A NH2 1 
ATOM   193  N N   . LEU   A 1 31  ? -2.463  -11.156 -18.464 1.00 82.00  ? 74  LEU   A N   1 
ATOM   194  C CA  . LEU   A 1 31  ? -1.655  -10.390 -17.525 1.00 80.78  ? 74  LEU   A CA  1 
ATOM   195  C C   . LEU   A 1 31  ? -1.742  -10.945 -16.107 1.00 79.47  ? 74  LEU   A C   1 
ATOM   196  O O   . LEU   A 1 31  ? -2.828  -11.303 -15.657 1.00 79.79  ? 74  LEU   A O   1 
ATOM   197  C CB  . LEU   A 1 31  ? -2.116  -8.920  -17.536 1.00 80.83  ? 74  LEU   A CB  1 
ATOM   198  C CG  . LEU   A 1 31  ? -2.169  -8.252  -18.914 1.00 82.24  ? 74  LEU   A CG  1 
ATOM   199  C CD1 . LEU   A 1 31  ? -2.751  -6.876  -18.829 1.00 82.61  ? 74  LEU   A CD1 1 
ATOM   200  C CD2 . LEU   A 1 31  ? -0.789  -8.197  -19.545 1.00 83.18  ? 74  LEU   A CD2 1 
ATOM   201  N N   . ASP   A 1 32  ? -0.603  -11.004 -15.393 1.00 77.60  ? 75  ASP   A N   1 
ATOM   202  C CA  . ASP   A 1 32  ? -0.585  -11.452 -14.005 1.00 76.14  ? 75  ASP   A CA  1 
ATOM   203  C C   . ASP   A 1 32  ? -0.723  -10.238 -13.113 1.00 73.81  ? 75  ASP   A C   1 
ATOM   204  O O   . ASP   A 1 32  ? 0.209   -9.435  -13.027 1.00 74.30  ? 75  ASP   A O   1 
ATOM   205  C CB  . ASP   A 1 32  ? 0.714   -12.192 -13.695 1.00 78.34  ? 75  ASP   A CB  1 
ATOM   206  C CG  . ASP   A 1 32  ? 0.720   -13.598 -14.247 1.00 84.25  ? 75  ASP   A CG  1 
ATOM   207  O OD1 . ASP   A 1 32  ? 0.062   -13.829 -15.291 1.00 85.60  ? 75  ASP   A OD1 1 
ATOM   208  O OD2 . ASP   A 1 32  ? 1.382   -14.472 -13.638 1.00 86.63  ? 75  ASP   A OD2 1 
ATOM   209  N N   . VAL   A 1 33  ? -1.888  -10.073 -12.477 1.00 71.19  ? 76  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 33  ? -2.137  -8.885  -11.666 1.00 69.30  ? 76  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 33  ? -2.403  -9.200  -10.177 1.00 67.63  ? 76  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 33  ? -2.625  -10.356 -9.797  1.00 67.61  ? 76  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 33  ? -3.271  -8.009  -12.288 1.00 69.08  ? 76  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 33  ? -2.894  -7.506  -13.674 1.00 69.32  ? 76  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 33  ? -4.585  -8.763  -12.325 1.00 69.09  ? 76  VAL   A CG2 1 
ATOM   216  N N   . ALA   A 1 34  ? -2.331  -8.149  -9.341  1.00 66.02  ? 77  ALA   A N   1 
ATOM   217  C CA  . ALA   A 1 34  ? -2.608  -8.168  -7.912  1.00 64.99  ? 77  ALA   A CA  1 
ATOM   218  C C   . ALA   A 1 34  ? -3.598  -7.053  -7.624  1.00 63.55  ? 77  ALA   A C   1 
ATOM   219  O O   . ALA   A 1 34  ? -3.494  -5.975  -8.209  1.00 63.51  ? 77  ALA   A O   1 
ATOM   220  C CB  . ALA   A 1 34  ? -1.335  -7.919  -7.127  1.00 65.18  ? 77  ALA   A CB  1 
ATOM   221  N N   . LEU   A 1 35  ? -4.558  -7.302  -6.732  1.00 62.19  ? 78  LEU   A N   1 
ATOM   222  C CA  . LEU   A 1 35  ? -5.542  -6.290  -6.370  1.00 61.14  ? 78  LEU   A CA  1 
ATOM   223  C C   . LEU   A 1 35  ? -5.392  -5.931  -4.894  1.00 61.05  ? 78  LEU   A C   1 
ATOM   224  O O   . LEU   A 1 35  ? -5.442  -6.812  -4.027  1.00 60.93  ? 78  LEU   A O   1 
ATOM   225  C CB  . LEU   A 1 35  ? -6.962  -6.777  -6.666  1.00 60.29  ? 78  LEU   A CB  1 
ATOM   226  C CG  . LEU   A 1 35  ? -8.052  -5.776  -6.375  1.00 60.16  ? 78  LEU   A CG  1 
ATOM   227  C CD1 . LEU   A 1 35  ? -8.019  -4.662  -7.365  1.00 60.72  ? 78  LEU   A CD1 1 
ATOM   228  C CD2 . LEU   A 1 35  ? -9.401  -6.430  -6.377  1.00 59.93  ? 78  LEU   A CD2 1 
ATOM   229  N N   . ASP   A 1 36  ? -5.175  -4.641  -4.610  1.00 60.66  ? 79  ASP   A N   1 
ATOM   230  C CA  . ASP   A 1 36  ? -5.026  -4.199  -3.232  1.00 60.62  ? 79  ASP   A CA  1 
ATOM   231  C C   . ASP   A 1 36  ? -6.378  -3.761  -2.622  1.00 60.84  ? 79  ASP   A C   1 
ATOM   232  O O   . ASP   A 1 36  ? -7.382  -3.617  -3.339  1.00 60.76  ? 79  ASP   A O   1 
ATOM   233  C CB  . ASP   A 1 36  ? -3.912  -3.131  -3.084  1.00 61.67  ? 79  ASP   A CB  1 
ATOM   234  C CG  . ASP   A 1 36  ? -4.182  -1.736  -3.631  1.00 65.64  ? 79  ASP   A CG  1 
ATOM   235  O OD1 . ASP   A 1 36  ? -5.346  -1.440  -3.973  1.00 66.03  ? 79  ASP   A OD1 1 
ATOM   236  O OD2 . ASP   A 1 36  ? -3.228  -0.939  -3.707  1.00 67.86  ? 79  ASP   A OD2 1 
ATOM   237  N N   . GLU   A 1 37  ? -6.390  -3.560  -1.293  1.00 60.65  ? 80  GLU   A N   1 
ATOM   238  C CA  . GLU   A 1 37  ? -7.540  -3.133  -0.510  1.00 60.80  ? 80  GLU   A CA  1 
ATOM   239  C C   . GLU   A 1 37  ? -8.155  -1.813  -1.028  1.00 60.62  ? 80  GLU   A C   1 
ATOM   240  O O   . GLU   A 1 37  ? -9.309  -1.549  -0.750  1.00 60.69  ? 80  GLU   A O   1 
ATOM   241  C CB  . GLU   A 1 37  ? -7.131  -2.999  0.962   1.00 63.45  ? 80  GLU   A CB  1 
ATOM   242  C CG  . GLU   A 1 37  ? -8.064  -3.702  1.924   1.00 70.00  ? 80  GLU   A CG  1 
ATOM   243  C CD  . GLU   A 1 37  ? -7.856  -3.292  3.369   1.00 78.95  ? 80  GLU   A CD  1 
ATOM   244  O OE1 . GLU   A 1 37  ? -7.547  -2.102  3.613   1.00 80.67  ? 80  GLU   A OE1 1 
ATOM   245  O OE2 . GLU   A 1 37  ? -7.996  -4.163  4.257   1.00 82.15  ? 80  GLU   A OE2 1 
ATOM   246  N N   . SER   A 1 38  ? -7.410  -1.002  -1.793  1.00 60.16  ? 81  SER   A N   1 
ATOM   247  C CA  . SER   A 1 38  ? -7.948  0.236   -2.360  1.00 60.30  ? 81  SER   A CA  1 
ATOM   248  C C   . SER   A 1 38  ? -8.595  0.052   -3.756  1.00 60.39  ? 81  SER   A C   1 
ATOM   249  O O   . SER   A 1 38  ? -8.983  1.045   -4.388  1.00 60.72  ? 81  SER   A O   1 
ATOM   250  C CB  . SER   A 1 38  ? -6.863  1.301   -2.423  1.00 61.87  ? 81  SER   A CB  1 
ATOM   251  O OG  . SER   A 1 38  ? -6.320  1.499   -1.127  1.00 65.06  ? 81  SER   A OG  1 
ATOM   252  N N   . GLY   A 1 39  ? -8.721  -1.200  -4.211  1.00 59.53  ? 82  GLY   A N   1 
ATOM   253  C CA  . GLY   A 1 39  ? -9.300  -1.532  -5.504  1.00 59.10  ? 82  GLY   A CA  1 
ATOM   254  C C   . GLY   A 1 39  ? -8.404  -1.193  -6.675  1.00 58.79  ? 82  GLY   A C   1 
ATOM   255  O O   . GLY   A 1 39  ? -8.891  -1.040  -7.790  1.00 59.32  ? 82  GLY   A O   1 
ATOM   256  N N   . ASP   A 1 40  ? -7.086  -1.094  -6.442  1.00 58.04  ? 83  ASP   A N   1 
ATOM   257  C CA  . ASP   A 1 40  ? -6.101  -0.759  -7.462  1.00 57.93  ? 83  ASP   A CA  1 
ATOM   258  C C   . ASP   A 1 40  ? -5.345  -1.989  -7.949  1.00 58.28  ? 83  ASP   A C   1 
ATOM   259  O O   . ASP   A 1 40  ? -4.832  -2.759  -7.135  1.00 58.32  ? 83  ASP   A O   1 
ATOM   260  C CB  . ASP   A 1 40  ? -5.110  0.274   -6.911  1.00 58.92  ? 83  ASP   A CB  1 
ATOM   261  C CG  . ASP   A 1 40  ? -5.755  1.598   -6.559  1.00 62.42  ? 83  ASP   A CG  1 
ATOM   262  O OD1 . ASP   A 1 40  ? -6.776  1.936   -7.174  1.00 62.24  ? 83  ASP   A OD1 1 
ATOM   263  O OD2 . ASP   A 1 40  ? -5.233  2.293   -5.667  1.00 65.03  ? 83  ASP   A OD2 1 
ATOM   264  N N   . PHE   A 1 41  ? -5.248  -2.163  -9.274  1.00 58.42  ? 84  PHE   A N   1 
ATOM   265  C CA  . PHE   A 1 41  ? -4.521  -3.291  -9.845  1.00 59.23  ? 84  PHE   A CA  1 
ATOM   266  C C   . PHE   A 1 41  ? -3.044  -2.958  -10.067 1.00 61.89  ? 84  PHE   A C   1 
ATOM   267  O O   . PHE   A 1 41  ? -2.687  -1.799  -10.284 1.00 61.79  ? 84  PHE   A O   1 
ATOM   268  C CB  . PHE   A 1 41  ? -5.155  -3.741  -11.158 1.00 57.93  ? 84  PHE   A CB  1 
ATOM   269  C CG  . PHE   A 1 41  ? -6.460  -4.482  -11.026 1.00 57.44  ? 84  PHE   A CG  1 
ATOM   270  C CD1 . PHE   A 1 41  ? -6.482  -5.842  -10.796 1.00 57.77  ? 84  PHE   A CD1 1 
ATOM   271  C CD2 . PHE   A 1 41  ? -7.666  -3.828  -11.186 1.00 57.62  ? 84  PHE   A CD2 1 
ATOM   272  C CE1 . PHE   A 1 41  ? -7.687  -6.524  -10.700 1.00 58.18  ? 84  PHE   A CE1 1 
ATOM   273  C CE2 . PHE   A 1 41  ? -8.868  -4.515  -11.095 1.00 57.82  ? 84  PHE   A CE2 1 
ATOM   274  C CZ  . PHE   A 1 41  ? -8.871  -5.856  -10.854 1.00 57.58  ? 84  PHE   A CZ  1 
ATOM   275  N N   . SER   A 1 42  ? -2.185  -3.972  -10.003 1.00 64.23  ? 85  SER   A N   1 
ATOM   276  C CA  . SER   A 1 42  ? -0.758  -3.771  -10.228 1.00 67.59  ? 85  SER   A CA  1 
ATOM   277  C C   . SER   A 1 42  ? -0.167  -4.932  -11.004 1.00 70.98  ? 85  SER   A C   1 
ATOM   278  O O   . SER   A 1 42  ? -0.667  -6.055  -10.894 1.00 71.56  ? 85  SER   A O   1 
ATOM   279  C CB  . SER   A 1 42  ? -0.011  -3.520  -8.919  1.00 69.49  ? 85  SER   A CB  1 
ATOM   280  O OG  . SER   A 1 42  ? -0.245  -4.503  -7.922  1.00 72.30  ? 85  SER   A OG  1 
ATOM   281  N N   . LEU   A 1 43  ? 0.864   -4.668  -11.826 1.00 73.02  ? 86  LEU   A N   1 
ATOM   282  C CA  . LEU   A 1 43  ? 1.462   -5.736  -12.614 1.00 75.71  ? 86  LEU   A CA  1 
ATOM   283  C C   . LEU   A 1 43  ? 2.482   -6.547  -11.857 1.00 78.35  ? 86  LEU   A C   1 
ATOM   284  O O   . LEU   A 1 43  ? 3.546   -6.045  -11.498 1.00 78.63  ? 86  LEU   A O   1 
ATOM   285  C CB  . LEU   A 1 43  ? 2.040   -5.234  -13.932 1.00 76.17  ? 86  LEU   A CB  1 
ATOM   286  C CG  . LEU   A 1 43  ? 1.012   -4.979  -15.021 1.00 78.16  ? 86  LEU   A CG  1 
ATOM   287  C CD1 . LEU   A 1 43  ? 1.673   -4.464  -16.279 1.00 78.93  ? 86  LEU   A CD1 1 
ATOM   288  C CD2 . LEU   A 1 43  ? 0.194   -6.228  -15.329 1.00 78.94  ? 86  LEU   A CD2 1 
ATOM   289  N N   . VAL   A 1 44  ? 2.149   -7.812  -11.616 1.00 80.13  ? 87  VAL   A N   1 
ATOM   290  C CA  . VAL   A 1 44  ? 3.027   -8.763  -10.942 1.00 82.44  ? 87  VAL   A CA  1 
ATOM   291  C C   . VAL   A 1 44  ? 3.976   -9.353  -11.988 1.00 84.77  ? 87  VAL   A C   1 
ATOM   292  O O   . VAL   A 1 44  ? 3.569   -9.570  -13.137 1.00 85.10  ? 87  VAL   A O   1 
ATOM   293  C CB  . VAL   A 1 44  ? 2.186   -9.867  -10.249 1.00 83.22  ? 87  VAL   A CB  1 
ATOM   294  C CG1 . VAL   A 1 44  ? 3.035   -11.075 -9.860  1.00 83.83  ? 87  VAL   A CG1 1 
ATOM   295  C CG2 . VAL   A 1 44  ? 1.447   -9.311  -9.042  1.00 83.71  ? 87  VAL   A CG2 1 
ATOM   296  N N   . GLU   A 1 45  ? 5.244   -9.576  -11.612 1.00 86.19  ? 88  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 45  ? 6.232   -10.165 -12.515 1.00 88.27  ? 88  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 45  ? 7.031   -11.262 -11.806 1.00 89.25  ? 88  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 45  ? 7.457   -12.227 -12.441 1.00 89.83  ? 88  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 45  ? 7.180   -9.093  -13.081 1.00 92.00  ? 88  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 45  ? 6.494   -8.045  -13.948 1.00 98.79  ? 88  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 45  ? 6.294   -8.444  -15.397 1.00 105.76 ? 88  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 45  ? 7.242   -9.004  -15.998 1.00 106.62 ? 88  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 45  ? 5.190   -8.186  -15.931 1.00 107.70 ? 88  GLU   A OE2 1 
ATOM   305  N N   . GLY   B 2 7   ? -35.568 11.729  -11.393 1.00 82.15  ? 16  GLY   B N   1 
ATOM   306  C CA  . GLY   B 2 7   ? -36.046 12.310  -12.641 1.00 82.47  ? 16  GLY   B CA  1 
ATOM   307  C C   . GLY   B 2 7   ? -36.159 11.289  -13.757 1.00 82.52  ? 16  GLY   B C   1 
ATOM   308  O O   . GLY   B 2 7   ? -37.163 10.570  -13.842 1.00 83.10  ? 16  GLY   B O   1 
ATOM   309  N N   . GLU   B 2 8   ? -35.132 11.212  -14.633 1.00 81.39  ? 17  GLU   B N   1 
ATOM   310  C CA  . GLU   B 2 8   ? -35.157 10.244  -15.720 1.00 80.59  ? 17  GLU   B CA  1 
ATOM   311  C C   . GLU   B 2 8   ? -34.634 8.892   -15.266 1.00 79.38  ? 17  GLU   B C   1 
ATOM   312  O O   . GLU   B 2 8   ? -33.432 8.730   -15.037 1.00 79.76  ? 17  GLU   B O   1 
ATOM   313  C CB  . GLU   B 2 8   ? -34.378 10.728  -16.947 1.00 82.99  ? 17  GLU   B CB  1 
ATOM   314  C CG  . GLU   B 2 8   ? -34.507 9.764   -18.117 1.00 87.37  ? 17  GLU   B CG  1 
ATOM   315  C CD  . GLU   B 2 8   ? -33.805 10.180  -19.393 1.00 92.45  ? 17  GLU   B CD  1 
ATOM   316  O OE1 . GLU   B 2 8   ? -32.773 10.882  -19.299 1.00 93.27  ? 17  GLU   B OE1 1 
ATOM   317  O OE2 . GLU   B 2 8   ? -34.288 9.807   -20.488 1.00 94.12  ? 17  GLU   B OE2 1 
ATOM   318  N N   A THR   B 2 9   ? -35.530 7.911   -15.133 0.50 78.56  ? 18  THR   B N   1 
ATOM   319  N N   B THR   B 2 9   ? -35.542 7.922   -15.139 0.50 78.55  ? 18  THR   B N   1 
ATOM   320  C CA  A THR   B 2 9   ? -35.124 6.560   -14.725 0.50 78.23  ? 18  THR   B CA  1 
ATOM   321  C CA  B THR   B 2 9   ? -35.206 6.559   -14.726 0.50 78.22  ? 18  THR   B CA  1 
ATOM   322  C C   A THR   B 2 9   ? -35.149 5.551   -15.880 0.50 77.34  ? 18  THR   B C   1 
ATOM   323  C C   B THR   B 2 9   ? -35.228 5.551   -15.881 0.50 77.34  ? 18  THR   B C   1 
ATOM   324  O O   A THR   B 2 9   ? -35.084 4.351   -15.625 0.50 77.66  ? 18  THR   B O   1 
ATOM   325  O O   B THR   B 2 9   ? -35.238 4.349   -15.625 0.50 77.68  ? 18  THR   B O   1 
ATOM   326  C CB  A THR   B 2 9   ? -35.913 6.021   -13.502 0.50 79.81  ? 18  THR   B CB  1 
ATOM   327  C CB  B THR   B 2 9   ? -36.131 6.093   -13.588 0.50 79.80  ? 18  THR   B CB  1 
ATOM   328  O OG1 A THR   B 2 9   ? -36.999 6.885   -13.128 0.50 81.03  ? 18  THR   B OG1 1 
ATOM   329  O OG1 B THR   B 2 9   ? -37.490 6.449   -13.884 0.50 80.85  ? 18  THR   B OG1 1 
ATOM   330  C CG2 A THR   B 2 9   ? -35.011 5.740   -12.302 0.50 80.17  ? 18  THR   B CG2 1 
ATOM   331  C CG2 B THR   B 2 9   ? -35.713 6.650   -12.233 0.50 80.29  ? 18  THR   B CG2 1 
ATOM   332  N N   . THR   B 2 10  ? -35.239 6.023   -17.136 1.00 76.15  ? 19  THR   B N   1 
ATOM   333  C CA  . THR   B 2 10  ? -35.278 5.161   -18.315 1.00 74.29  ? 19  THR   B CA  1 
ATOM   334  C C   . THR   B 2 10  ? -33.996 4.335   -18.433 1.00 71.78  ? 19  THR   B C   1 
ATOM   335  O O   . THR   B 2 10  ? -32.912 4.870   -18.216 1.00 71.75  ? 19  THR   B O   1 
ATOM   336  C CB  . THR   B 2 10  ? -35.503 6.033   -19.575 1.00 75.55  ? 19  THR   B CB  1 
ATOM   337  O OG1 . THR   B 2 10  ? -36.647 6.871   -19.383 1.00 76.51  ? 19  THR   B OG1 1 
ATOM   338  C CG2 . THR   B 2 10  ? -35.671 5.206   -20.850 1.00 75.77  ? 19  THR   B CG2 1 
ATOM   339  N N   . ASP   B 2 11  ? -34.122 3.031   -18.742 1.00 69.48  ? 20  ASP   B N   1 
ATOM   340  C CA  . ASP   B 2 11  ? -32.982 2.139   -18.928 1.00 68.07  ? 20  ASP   B CA  1 
ATOM   341  C C   . ASP   B 2 11  ? -32.081 2.659   -20.051 1.00 66.48  ? 20  ASP   B C   1 
ATOM   342  O O   . ASP   B 2 11  ? -32.583 3.176   -21.045 1.00 67.01  ? 20  ASP   B O   1 
ATOM   343  C CB  . ASP   B 2 11  ? -33.454 0.724   -19.314 1.00 69.93  ? 20  ASP   B CB  1 
ATOM   344  C CG  . ASP   B 2 11  ? -33.961 -0.154  -18.187 1.00 74.84  ? 20  ASP   B CG  1 
ATOM   345  O OD1 . ASP   B 2 11  ? -34.350 0.394   -17.135 1.00 75.70  ? 20  ASP   B OD1 1 
ATOM   346  O OD2 . ASP   B 2 11  ? -33.987 -1.392  -18.368 1.00 76.90  ? 20  ASP   B OD2 1 
ATOM   347  N N   . GLY   B 2 12  ? -30.776 2.493   -19.902 1.00 64.55  ? 21  GLY   B N   1 
ATOM   348  C CA  . GLY   B 2 12  ? -29.814 2.928   -20.902 1.00 63.31  ? 21  GLY   B CA  1 
ATOM   349  C C   . GLY   B 2 12  ? -28.475 3.316   -20.314 1.00 62.26  ? 21  GLY   B C   1 
ATOM   350  O O   . GLY   B 2 12  ? -28.238 3.153   -19.117 1.00 62.56  ? 21  GLY   B O   1 
ATOM   351  N N   . VAL   B 2 13  ? -27.573 3.809   -21.154 1.00 60.97  ? 22  VAL   B N   1 
ATOM   352  C CA  . VAL   B 2 13  ? -26.255 4.249   -20.708 1.00 60.16  ? 22  VAL   B CA  1 
ATOM   353  C C   . VAL   B 2 13  ? -26.293 5.775   -20.495 1.00 59.56  ? 22  VAL   B C   1 
ATOM   354  O O   . VAL   B 2 13  ? -27.020 6.471   -21.201 1.00 60.11  ? 22  VAL   B O   1 
ATOM   355  C CB  . VAL   B 2 13  ? -25.142 3.772   -21.668 1.00 60.40  ? 22  VAL   B CB  1 
ATOM   356  C CG1 . VAL   B 2 13  ? -25.323 4.346   -23.068 1.00 61.09  ? 22  VAL   B CG1 1 
ATOM   357  C CG2 . VAL   B 2 13  ? -23.762 4.084   -21.120 1.00 60.52  ? 22  VAL   B CG2 1 
ATOM   358  N N   . TYR   B 2 14  ? -25.616 6.280   -19.449 1.00 58.25  ? 23  TYR   B N   1 
ATOM   359  C CA  . TYR   B 2 14  ? -25.641 7.702   -19.086 1.00 57.31  ? 23  TYR   B CA  1 
ATOM   360  C C   . TYR   B 2 14  ? -24.247 8.262   -18.820 1.00 56.82  ? 23  TYR   B C   1 
ATOM   361  O O   . TYR   B 2 14  ? -23.402 7.563   -18.292 1.00 56.96  ? 23  TYR   B O   1 
ATOM   362  C CB  . TYR   B 2 14  ? -26.451 7.905   -17.787 1.00 56.49  ? 23  TYR   B CB  1 
ATOM   363  C CG  . TYR   B 2 14  ? -27.945 7.760   -17.941 1.00 56.22  ? 23  TYR   B CG  1 
ATOM   364  C CD1 . TYR   B 2 14  ? -28.517 6.528   -18.219 1.00 56.83  ? 23  TYR   B CD1 1 
ATOM   365  C CD2 . TYR   B 2 14  ? -28.794 8.830   -17.708 1.00 56.40  ? 23  TYR   B CD2 1 
ATOM   366  C CE1 . TYR   B 2 14  ? -29.886 6.390   -18.379 1.00 57.48  ? 23  TYR   B CE1 1 
ATOM   367  C CE2 . TYR   B 2 14  ? -30.170 8.701   -17.848 1.00 57.11  ? 23  TYR   B CE2 1 
ATOM   368  C CZ  . TYR   B 2 14  ? -30.715 7.473   -18.170 1.00 58.06  ? 23  TYR   B CZ  1 
ATOM   369  O OH  . TYR   B 2 14  ? -32.071 7.311   -18.311 1.00 59.41  ? 23  TYR   B OH  1 
ATOM   370  N N   . ARG   B 2 15  ? -24.051 9.547   -19.072 1.00 56.10  ? 24  ARG   B N   1 
ATOM   371  C CA  . ARG   B 2 15  ? -22.807 10.230  -18.752 1.00 55.95  ? 24  ARG   B CA  1 
ATOM   372  C C   . ARG   B 2 15  ? -22.935 10.793  -17.339 1.00 55.64  ? 24  ARG   B C   1 
ATOM   373  O O   . ARG   B 2 15  ? -24.000 11.264  -16.963 1.00 55.14  ? 24  ARG   B O   1 
ATOM   374  C CB  . ARG   B 2 15  ? -22.567 11.418  -19.716 1.00 56.99  ? 24  ARG   B CB  1 
ATOM   375  C CG  . ARG   B 2 15  ? -22.443 11.055  -21.182 1.00 58.79  ? 24  ARG   B CG  1 
ATOM   376  C CD  . ARG   B 2 15  ? -22.304 12.318  -22.021 1.00 61.71  ? 24  ARG   B CD  1 
ATOM   377  N NE  . ARG   B 2 15  ? -22.474 12.051  -23.451 1.00 63.29  ? 24  ARG   B NE  1 
ATOM   378  C CZ  . ARG   B 2 15  ? -21.492 11.676  -24.264 1.00 65.04  ? 24  ARG   B CZ  1 
ATOM   379  N NH1 . ARG   B 2 15  ? -20.253 11.536  -23.802 1.00 64.96  ? 24  ARG   B NH1 1 
ATOM   380  N NH2 . ARG   B 2 15  ? -21.741 11.424  -25.540 1.00 64.43  ? 24  ARG   B NH2 1 
ATOM   381  N N   . VAL   B 2 16  ? -21.840 10.784  -16.585 1.00 55.96  ? 25  VAL   B N   1 
ATOM   382  C CA  . VAL   B 2 16  ? -21.717 11.329  -15.235 1.00 56.89  ? 25  VAL   B CA  1 
ATOM   383  C C   . VAL   B 2 16  ? -20.886 12.605  -15.392 1.00 57.67  ? 25  VAL   B C   1 
ATOM   384  O O   . VAL   B 2 16  ? -19.744 12.547  -15.839 1.00 57.58  ? 25  VAL   B O   1 
ATOM   385  C CB  . VAL   B 2 16  ? -21.048 10.319  -14.267 1.00 57.65  ? 25  VAL   B CB  1 
ATOM   386  C CG1 . VAL   B 2 16  ? -21.027 10.863  -12.844 1.00 58.39  ? 25  VAL   B CG1 1 
ATOM   387  C CG2 . VAL   B 2 16  ? -21.744 8.960   -14.316 1.00 57.79  ? 25  VAL   B CG2 1 
ATOM   388  N N   . MET   B 2 17  ? -21.489 13.754  -15.114 1.00 58.43  ? 26  MET   B N   1 
ATOM   389  C CA  . MET   B 2 17  ? -20.886 15.063  -15.339 1.00 59.88  ? 26  MET   B CA  1 
ATOM   390  C C   . MET   B 2 17  ? -20.722 15.873  -14.051 1.00 62.02  ? 26  MET   B C   1 
ATOM   391  O O   . MET   B 2 17  ? -21.382 15.581  -13.060 1.00 62.34  ? 26  MET   B O   1 
ATOM   392  C CB  . MET   B 2 17  ? -21.825 15.877  -16.259 1.00 60.08  ? 26  MET   B CB  1 
ATOM   393  C CG  . MET   B 2 17  ? -22.250 15.188  -17.530 1.00 61.18  ? 26  MET   B CG  1 
ATOM   394  S SD  . MET   B 2 17  ? -20.969 15.236  -18.802 1.00 63.59  ? 26  MET   B SD  1 
ATOM   395  C CE  . MET   B 2 17  ? -20.654 16.980  -18.895 1.00 61.73  ? 26  MET   B CE  1 
ATOM   396  N N   . THR   B 2 18  ? -19.908 16.943  -14.087 1.00 63.57  ? 27  THR   B N   1 
ATOM   397  C CA  . THR   B 2 18  ? -19.771 17.870  -12.963 1.00 65.84  ? 27  THR   B CA  1 
ATOM   398  C C   . THR   B 2 18  ? -19.535 19.328  -13.422 1.00 68.28  ? 27  THR   B C   1 
ATOM   399  O O   . THR   B 2 18  ? -18.899 19.575  -14.450 1.00 68.31  ? 27  THR   B O   1 
ATOM   400  C CB  . THR   B 2 18  ? -18.719 17.416  -11.937 1.00 66.89  ? 27  THR   B CB  1 
ATOM   401  O OG1 . THR   B 2 18  ? -18.719 18.350  -10.846 1.00 67.96  ? 27  THR   B OG1 1 
ATOM   402  C CG2 . THR   B 2 18  ? -17.325 17.314  -12.529 1.00 66.90  ? 27  THR   B CG2 1 
ATOM   403  N N   . ARG   B 2 19  ? -20.043 20.288  -12.648 1.00 69.97  ? 28  ARG   B N   1 
ATOM   404  C CA  . ARG   B 2 19  ? -19.821 21.702  -12.937 1.00 72.28  ? 28  ARG   B CA  1 
ATOM   405  C C   . ARG   B 2 19  ? -18.853 22.384  -11.922 1.00 73.67  ? 28  ARG   B C   1 
ATOM   406  O O   . ARG   B 2 19  ? -18.616 23.588  -12.007 1.00 73.89  ? 28  ARG   B O   1 
ATOM   407  C CB  . ARG   B 2 19  ? -21.154 22.458  -13.076 1.00 74.58  ? 28  ARG   B CB  1 
ATOM   408  C CG  . ARG   B 2 19  ? -21.841 22.197  -14.409 1.00 79.15  ? 28  ARG   B CG  1 
ATOM   409  C CD  . ARG   B 2 19  ? -22.995 23.143  -14.635 1.00 84.36  ? 28  ARG   B CD  1 
ATOM   410  N NE  . ARG   B 2 19  ? -23.813 22.771  -15.794 1.00 88.96  ? 28  ARG   B NE  1 
ATOM   411  C CZ  . ARG   B 2 19  ? -25.000 22.174  -15.712 1.00 92.05  ? 28  ARG   B CZ  1 
ATOM   412  N NH1 . ARG   B 2 19  ? -25.520 21.869  -14.527 1.00 92.46  ? 28  ARG   B NH1 1 
ATOM   413  N NH2 . ARG   B 2 19  ? -25.677 21.878  -16.815 1.00 91.75  ? 28  ARG   B NH2 1 
ATOM   414  N N   . ARG   B 2 20  ? -18.265 21.593  -11.004 1.00 74.52  ? 29  ARG   B N   1 
ATOM   415  C CA  . ARG   B 2 20  ? -17.313 22.018  -9.969  1.00 75.74  ? 29  ARG   B CA  1 
ATOM   416  C C   . ARG   B 2 20  ? -15.933 22.447  -10.544 1.00 75.57  ? 29  ARG   B C   1 
ATOM   417  O O   . ARG   B 2 20  ? -15.112 23.038  -9.834  1.00 75.89  ? 29  ARG   B O   1 
ATOM   418  C CB  . ARG   B 2 20  ? -17.157 20.888  -8.924  1.00 78.15  ? 29  ARG   B CB  1 
ATOM   419  C CG  . ARG   B 2 20  ? -16.493 21.303  -7.617  1.00 83.04  ? 29  ARG   B CG  1 
ATOM   420  C CD  . ARG   B 2 20  ? -15.993 20.104  -6.838  1.00 88.27  ? 29  ARG   B CD  1 
ATOM   421  N NE  . ARG   B 2 20  ? -15.091 19.253  -7.623  1.00 93.09  ? 29  ARG   B NE  1 
ATOM   422  C CZ  . ARG   B 2 20  ? -13.766 19.377  -7.643  1.00 96.59  ? 29  ARG   B CZ  1 
ATOM   423  N NH1 . ARG   B 2 20  ? -13.170 20.331  -6.934  1.00 96.83  ? 29  ARG   B NH1 1 
ATOM   424  N NH2 . ARG   B 2 20  ? -13.026 18.551  -8.375  1.00 96.51  ? 29  ARG   B NH2 1 
ATOM   425  N N   . LEU   B 2 21  ? -15.689 22.169  -11.827 1.00 74.81  ? 30  LEU   B N   1 
ATOM   426  C CA  . LEU   B 2 21  ? -14.447 22.549  -12.478 1.00 74.63  ? 30  LEU   B CA  1 
ATOM   427  C C   . LEU   B 2 21  ? -14.761 23.606  -13.588 1.00 74.02  ? 30  LEU   B C   1 
ATOM   428  O O   . LEU   B 2 21  ? -15.791 24.297  -13.507 1.00 74.20  ? 30  LEU   B O   1 
ATOM   429  C CB  . LEU   B 2 21  ? -13.751 21.281  -13.020 1.00 74.99  ? 30  LEU   B CB  1 
ATOM   430  C CG  . LEU   B 2 21  ? -13.270 20.289  -11.963 1.00 76.95  ? 30  LEU   B CG  1 
ATOM   431  C CD1 . LEU   B 2 21  ? -14.349 19.286  -11.619 1.00 77.82  ? 30  LEU   B CD1 1 
ATOM   432  C CD2 . LEU   B 2 21  ? -12.056 19.527  -12.446 1.00 77.71  ? 30  LEU   B CD2 1 
ATOM   433  N N   . LEU   B 2 22  ? -13.869 23.783  -14.572 1.00 72.84  ? 31  LEU   B N   1 
ATOM   434  C CA  . LEU   B 2 22  ? -14.113 24.711  -15.662 1.00 72.10  ? 31  LEU   B CA  1 
ATOM   435  C C   . LEU   B 2 22  ? -15.135 24.048  -16.600 1.00 71.88  ? 31  LEU   B C   1 
ATOM   436  O O   . LEU   B 2 22  ? -15.018 22.847  -16.883 1.00 72.19  ? 31  LEU   B O   1 
ATOM   437  C CB  . LEU   B 2 22  ? -12.809 24.957  -16.397 1.00 71.67  ? 31  LEU   B CB  1 
ATOM   438  C CG  . LEU   B 2 22  ? -12.860 26.023  -17.434 1.00 72.20  ? 31  LEU   B CG  1 
ATOM   439  C CD1 . LEU   B 2 22  ? -12.500 27.358  -16.842 1.00 72.54  ? 31  LEU   B CD1 1 
ATOM   440  C CD2 . LEU   B 2 22  ? -11.952 25.672  -18.566 1.00 72.62  ? 31  LEU   B CD2 1 
ATOM   441  N N   . GLY   B 2 23  ? -16.148 24.814  -17.026 1.00 70.80  ? 32  GLY   B N   1 
ATOM   442  C CA  . GLY   B 2 23  ? -17.224 24.320  -17.880 1.00 69.99  ? 32  GLY   B CA  1 
ATOM   443  C C   . GLY   B 2 23  ? -17.927 23.094  -17.318 1.00 68.88  ? 32  GLY   B C   1 
ATOM   444  O O   . GLY   B 2 23  ? -18.062 22.947  -16.101 1.00 68.84  ? 32  GLY   B O   1 
ATOM   445  N N   . SER   B 2 24  ? -18.347 22.181  -18.200 1.00 67.76  ? 33  SER   B N   1 
ATOM   446  C CA  . SER   B 2 24  ? -18.993 20.933  -17.799 1.00 66.95  ? 33  SER   B CA  1 
ATOM   447  C C   . SER   B 2 24  ? -18.006 19.790  -18.073 1.00 65.79  ? 33  SER   B C   1 
ATOM   448  O O   . SER   B 2 24  ? -17.602 19.603  -19.216 1.00 65.93  ? 33  SER   B O   1 
ATOM   449  C CB  . SER   B 2 24  ? -20.287 20.725  -18.583 1.00 67.99  ? 33  SER   B CB  1 
ATOM   450  O OG  . SER   B 2 24  ? -21.200 21.800  -18.418 1.00 69.73  ? 33  SER   B OG  1 
ATOM   451  N N   . THR   B 2 25  ? -17.581 19.060  -17.034 1.00 64.62  ? 34  THR   B N   1 
ATOM   452  C CA  . THR   B 2 25  ? -16.598 17.987  -17.210 1.00 64.12  ? 34  THR   B CA  1 
ATOM   453  C C   . THR   B 2 25  ? -17.154 16.573  -16.959 1.00 62.85  ? 34  THR   B C   1 
ATOM   454  O O   . THR   B 2 25  ? -17.665 16.296  -15.874 1.00 62.58  ? 34  THR   B O   1 
ATOM   455  C CB  . THR   B 2 25  ? -15.352 18.255  -16.342 1.00 65.38  ? 34  THR   B CB  1 
ATOM   456  O OG1 . THR   B 2 25  ? -14.806 19.549  -16.644 1.00 66.19  ? 34  THR   B OG1 1 
ATOM   457  C CG2 . THR   B 2 25  ? -14.291 17.177  -16.504 1.00 65.61  ? 34  THR   B CG2 1 
ATOM   458  N N   . GLN   B 2 26  ? -17.035 15.674  -17.957 1.00 61.63  ? 35  GLN   B N   1 
ATOM   459  C CA  . GLN   B 2 26  ? -17.484 14.292  -17.779 1.00 60.71  ? 35  GLN   B CA  1 
ATOM   460  C C   . GLN   B 2 26  ? -16.467 13.524  -16.934 1.00 60.22  ? 35  GLN   B C   1 
ATOM   461  O O   . GLN   B 2 26  ? -15.327 13.340  -17.357 1.00 60.85  ? 35  GLN   B O   1 
ATOM   462  C CB  . GLN   B 2 26  ? -17.708 13.579  -19.130 1.00 60.77  ? 35  GLN   B CB  1 
ATOM   463  C CG  . GLN   B 2 26  ? -18.045 12.099  -18.982 1.00 61.44  ? 35  GLN   B CG  1 
ATOM   464  C CD  . GLN   B 2 26  ? -18.343 11.417  -20.288 1.00 63.52  ? 35  GLN   B CD  1 
ATOM   465  O OE1 . GLN   B 2 26  ? -18.952 11.987  -21.195 1.00 64.58  ? 35  GLN   B OE1 1 
ATOM   466  N NE2 . GLN   B 2 26  ? -17.941 10.165  -20.406 1.00 63.06  ? 35  GLN   B NE2 1 
ATOM   467  N N   . VAL   B 2 27  ? -16.883 13.065  -15.750 1.00 58.70  ? 36  VAL   B N   1 
ATOM   468  C CA  . VAL   B 2 27  ? -16.020 12.288  -14.864 1.00 57.67  ? 36  VAL   B CA  1 
ATOM   469  C C   . VAL   B 2 27  ? -16.172 10.753  -15.043 1.00 56.89  ? 36  VAL   B C   1 
ATOM   470  O O   . VAL   B 2 27  ? -15.330 9.970   -14.564 1.00 57.39  ? 36  VAL   B O   1 
ATOM   471  C CB  . VAL   B 2 27  ? -16.258 12.709  -13.396 1.00 58.08  ? 36  VAL   B CB  1 
ATOM   472  C CG1 . VAL   B 2 27  ? -15.892 14.167  -13.193 1.00 58.67  ? 36  VAL   B CG1 1 
ATOM   473  C CG2 . VAL   B 2 27  ? -17.700 12.463  -12.986 1.00 58.16  ? 36  VAL   B CG2 1 
ATOM   474  N N   . GLY   B 2 28  ? -17.237 10.334  -15.711 1.00 55.40  ? 37  GLY   B N   1 
ATOM   475  C CA  . GLY   B 2 28  ? -17.501 8.924   -15.913 1.00 54.63  ? 37  GLY   B CA  1 
ATOM   476  C C   . GLY   B 2 28  ? -18.806 8.655   -16.619 1.00 53.50  ? 37  GLY   B C   1 
ATOM   477  O O   . GLY   B 2 28  ? -19.427 9.563   -17.159 1.00 53.17  ? 37  GLY   B O   1 
ATOM   478  N N   . VAL   B 2 29  ? -19.223 7.392   -16.600 1.00 52.82  ? 38  VAL   B N   1 
ATOM   479  C CA  . VAL   B 2 29  ? -20.385 6.812   -17.271 1.00 52.49  ? 38  VAL   B CA  1 
ATOM   480  C C   . VAL   B 2 29  ? -21.080 5.820   -16.305 1.00 51.70  ? 38  VAL   B C   1 
ATOM   481  O O   . VAL   B 2 29  ? -20.472 5.355   -15.342 1.00 51.27  ? 38  VAL   B O   1 
ATOM   482  C CB  . VAL   B 2 29  ? -19.905 6.094   -18.589 1.00 52.78  ? 38  VAL   B CB  1 
ATOM   483  C CG1 . VAL   B 2 29  ? -21.036 5.393   -19.320 1.00 53.01  ? 38  VAL   B CG1 1 
ATOM   484  C CG2 . VAL   B 2 29  ? -19.198 7.053   -19.532 1.00 53.16  ? 38  VAL   B CG2 1 
ATOM   485  N N   . GLY   B 2 30  ? -22.341 5.501   -16.577 1.00 51.25  ? 39  GLY   B N   1 
ATOM   486  C CA  . GLY   B 2 30  ? -23.089 4.547   -15.776 1.00 51.53  ? 39  GLY   B CA  1 
ATOM   487  C C   . GLY   B 2 30  ? -24.234 3.885   -16.513 1.00 51.75  ? 39  GLY   B C   1 
ATOM   488  O O   . GLY   B 2 30  ? -24.638 4.342   -17.577 1.00 52.19  ? 39  GLY   B O   1 
ATOM   489  N N   . VAL   B 2 31  ? -24.769 2.805   -15.953 1.00 51.54  ? 40  VAL   B N   1 
ATOM   490  C CA  . VAL   B 2 31  ? -25.876 2.059   -16.547 1.00 51.81  ? 40  VAL   B CA  1 
ATOM   491  C C   . VAL   B 2 31  ? -27.145 2.183   -15.704 1.00 52.44  ? 40  VAL   B C   1 
ATOM   492  O O   . VAL   B 2 31  ? -27.125 1.898   -14.501 1.00 52.49  ? 40  VAL   B O   1 
ATOM   493  C CB  . VAL   B 2 31  ? -25.481 0.568   -16.715 1.00 51.95  ? 40  VAL   B CB  1 
ATOM   494  C CG1 . VAL   B 2 31  ? -26.675 -0.292  -17.112 1.00 52.14  ? 40  VAL   B CG1 1 
ATOM   495  C CG2 . VAL   B 2 31  ? -24.347 0.418   -17.715 1.00 52.45  ? 40  VAL   B CG2 1 
ATOM   496  N N   . MET   B 2 32  ? -28.256 2.555   -16.336 1.00 52.56  ? 41  MET   B N   1 
ATOM   497  C CA  . MET   B 2 32  ? -29.527 2.590   -15.633 1.00 53.34  ? 41  MET   B CA  1 
ATOM   498  C C   . MET   B 2 32  ? -30.266 1.316   -16.002 1.00 54.17  ? 41  MET   B C   1 
ATOM   499  O O   . MET   B 2 32  ? -30.496 1.079   -17.179 1.00 54.83  ? 41  MET   B O   1 
ATOM   500  C CB  . MET   B 2 32  ? -30.344 3.813   -16.019 1.00 53.58  ? 41  MET   B CB  1 
ATOM   501  C CG  . MET   B 2 32  ? -31.555 3.990   -15.156 1.00 55.44  ? 41  MET   B CG  1 
ATOM   502  S SD  . MET   B 2 32  ? -31.152 4.729   -13.571 1.00 60.67  ? 41  MET   B SD  1 
ATOM   503  C CE  . MET   B 2 32  ? -30.689 6.363   -14.101 1.00 59.19  ? 41  MET   B CE  1 
ATOM   504  N N   . GLN   B 2 33  ? -30.557 0.454   -15.027 1.00 53.97  ? 42  GLN   B N   1 
ATOM   505  C CA  . GLN   B 2 33  ? -31.258 -0.792  -15.295 1.00 54.23  ? 42  GLN   B CA  1 
ATOM   506  C C   . GLN   B 2 33  ? -32.108 -1.127  -14.102 1.00 54.15  ? 42  GLN   B C   1 
ATOM   507  O O   . GLN   B 2 33  ? -31.596 -1.119  -12.982 1.00 54.97  ? 42  GLN   B O   1 
ATOM   508  C CB  . GLN   B 2 33  ? -30.272 -1.920  -15.589 1.00 56.46  ? 42  GLN   B CB  1 
ATOM   509  C CG  . GLN   B 2 33  ? -30.989 -3.191  -16.025 1.00 62.83  ? 42  GLN   B CG  1 
ATOM   510  C CD  . GLN   B 2 33  ? -30.076 -4.191  -16.705 1.00 69.40  ? 42  GLN   B CD  1 
ATOM   511  O OE1 . GLN   B 2 33  ? -29.992 -5.369  -16.306 1.00 71.12  ? 42  GLN   B OE1 1 
ATOM   512  N NE2 . GLN   B 2 33  ? -29.369 -3.746  -17.747 1.00 70.49  ? 42  GLN   B NE2 1 
ATOM   513  N N   . GLU   B 2 34  ? -33.408 -1.363  -14.313 1.00 53.34  ? 43  GLU   B N   1 
ATOM   514  C CA  . GLU   B 2 34  ? -34.360 -1.672  -13.240 1.00 53.46  ? 43  GLU   B CA  1 
ATOM   515  C C   . GLU   B 2 34  ? -34.443 -0.571  -12.132 1.00 53.22  ? 43  GLU   B C   1 
ATOM   516  O O   . GLU   B 2 34  ? -34.631 -0.878  -10.958 1.00 53.67  ? 43  GLU   B O   1 
ATOM   517  C CB  . GLU   B 2 34  ? -34.097 -3.065  -12.636 1.00 55.84  ? 43  GLU   B CB  1 
ATOM   518  C CG  . GLU   B 2 34  ? -34.367 -4.207  -13.607 1.00 60.98  ? 43  GLU   B CG  1 
ATOM   519  C CD  . GLU   B 2 34  ? -33.600 -5.497  -13.361 1.00 67.84  ? 43  GLU   B CD  1 
ATOM   520  O OE1 . GLU   B 2 34  ? -33.881 -6.187  -12.353 1.00 68.08  ? 43  GLU   B OE1 1 
ATOM   521  O OE2 . GLU   B 2 34  ? -32.715 -5.821  -14.185 1.00 71.35  ? 43  GLU   B OE2 1 
ATOM   522  N N   . GLY   B 2 35  ? -34.338 0.695   -12.527 1.00 52.52  ? 44  GLY   B N   1 
ATOM   523  C CA  . GLY   B 2 35  ? -34.399 1.825   -11.605 1.00 52.07  ? 44  GLY   B CA  1 
ATOM   524  C C   . GLY   B 2 35  ? -33.164 1.982   -10.739 1.00 51.63  ? 44  GLY   B C   1 
ATOM   525  O O   . GLY   B 2 35  ? -33.203 2.675   -9.714  1.00 51.32  ? 44  GLY   B O   1 
ATOM   526  N N   . VAL   B 2 36  ? -32.054 1.318   -11.132 1.00 51.19  ? 45  VAL   B N   1 
ATOM   527  C CA  . VAL   B 2 36  ? -30.800 1.354   -10.390 1.00 51.24  ? 45  VAL   B CA  1 
ATOM   528  C C   . VAL   B 2 36  ? -29.686 1.876   -11.290 1.00 51.07  ? 45  VAL   B C   1 
ATOM   529  O O   . VAL   B 2 36  ? -29.553 1.438   -12.433 1.00 51.52  ? 45  VAL   B O   1 
ATOM   530  C CB  . VAL   B 2 36  ? -30.459 -0.016  -9.733  1.00 51.84  ? 45  VAL   B CB  1 
ATOM   531  C CG1 . VAL   B 2 36  ? -29.070 -0.014  -9.102  1.00 52.56  ? 45  VAL   B CG1 1 
ATOM   532  C CG2 . VAL   B 2 36  ? -31.500 -0.398  -8.696  1.00 51.95  ? 45  VAL   B CG2 1 
ATOM   533  N N   . PHE   B 2 37  ? -28.933 2.867   -10.801 1.00 50.22  ? 46  PHE   B N   1 
ATOM   534  C CA  . PHE   B 2 37  ? -27.831 3.421   -11.552 1.00 49.69  ? 46  PHE   B CA  1 
ATOM   535  C C   . PHE   B 2 37  ? -26.583 2.741   -11.064 1.00 49.29  ? 46  PHE   B C   1 
ATOM   536  O O   . PHE   B 2 37  ? -26.300 2.745   -9.873  1.00 49.26  ? 46  PHE   B O   1 
ATOM   537  C CB  . PHE   B 2 37  ? -27.721 4.911   -11.326 1.00 49.64  ? 46  PHE   B CB  1 
ATOM   538  C CG  . PHE   B 2 37  ? -26.768 5.570   -12.286 1.00 50.24  ? 46  PHE   B CG  1 
ATOM   539  C CD1 . PHE   B 2 37  ? -27.111 5.746   -13.614 1.00 50.84  ? 46  PHE   B CD1 1 
ATOM   540  C CD2 . PHE   B 2 37  ? -25.536 6.028   -11.858 1.00 50.92  ? 46  PHE   B CD2 1 
ATOM   541  C CE1 . PHE   B 2 37  ? -26.240 6.361   -14.494 1.00 51.44  ? 46  PHE   B CE1 1 
ATOM   542  C CE2 . PHE   B 2 37  ? -24.670 6.649   -12.741 1.00 51.64  ? 46  PHE   B CE2 1 
ATOM   543  C CZ  . PHE   B 2 37  ? -25.032 6.817   -14.051 1.00 51.40  ? 46  PHE   B CZ  1 
ATOM   544  N N   . HIS   B 2 38  ? -25.858 2.107   -11.978 1.00 48.63  ? 47  HIS   B N   1 
ATOM   545  C CA  . HIS   B 2 38  ? -24.647 1.381   -11.652 1.00 47.87  ? 47  HIS   B CA  1 
ATOM   546  C C   . HIS   B 2 38  ? -23.457 2.141   -12.202 1.00 47.59  ? 47  HIS   B C   1 
ATOM   547  O O   . HIS   B 2 38  ? -23.480 2.525   -13.364 1.00 47.13  ? 47  HIS   B O   1 
ATOM   548  C CB  . HIS   B 2 38  ? -24.691 -0.014  -12.291 1.00 47.40  ? 47  HIS   B CB  1 
ATOM   549  C CG  . HIS   B 2 38  ? -25.950 -0.769  -12.013 1.00 48.43  ? 47  HIS   B CG  1 
ATOM   550  N ND1 . HIS   B 2 38  ? -27.124 -0.487  -12.693 1.00 50.03  ? 47  HIS   B ND1 1 
ATOM   551  C CD2 . HIS   B 2 38  ? -26.176 -1.791  -11.155 1.00 49.46  ? 47  HIS   B CD2 1 
ATOM   552  C CE1 . HIS   B 2 38  ? -28.027 -1.330  -12.214 1.00 50.60  ? 47  HIS   B CE1 1 
ATOM   553  N NE2 . HIS   B 2 38  ? -27.502 -2.131  -11.281 1.00 50.68  ? 47  HIS   B NE2 1 
ATOM   554  N N   . THR   B 2 39  ? -22.416 2.364   -11.385 1.00 47.47  ? 48  THR   B N   1 
ATOM   555  C CA  . THR   B 2 39  ? -21.206 3.018   -11.884 1.00 48.04  ? 48  THR   B CA  1 
ATOM   556  C C   . THR   B 2 39  ? -19.952 2.520   -11.098 1.00 48.70  ? 48  THR   B C   1 
ATOM   557  O O   . THR   B 2 39  ? -20.053 1.649   -10.228 1.00 48.44  ? 48  THR   B O   1 
ATOM   558  C CB  . THR   B 2 39  ? -21.379 4.569   -11.957 1.00 48.74  ? 48  THR   B CB  1 
ATOM   559  O OG1 . THR   B 2 39  ? -20.327 5.087   -12.770 1.00 49.39  ? 48  THR   B OG1 1 
ATOM   560  C CG2 . THR   B 2 39  ? -21.351 5.235   -10.595 1.00 48.78  ? 48  THR   B CG2 1 
ATOM   561  N N   . MET   B 2 40  ? -18.770 3.031   -11.453 1.00 49.12  ? 49  MET   B N   1 
ATOM   562  C CA  . MET   B 2 40  ? -17.546 2.708   -10.760 1.00 49.67  ? 49  MET   B CA  1 
ATOM   563  C C   . MET   B 2 40  ? -17.402 3.654   -9.577  1.00 50.88  ? 49  MET   B C   1 
ATOM   564  O O   . MET   B 2 40  ? -17.710 4.848   -9.684  1.00 51.74  ? 49  MET   B O   1 
ATOM   565  C CB  . MET   B 2 40  ? -16.363 2.810   -11.715 1.00 50.06  ? 49  MET   B CB  1 
ATOM   566  C CG  . MET   B 2 40  ? -16.541 1.932   -12.929 1.00 52.70  ? 49  MET   B CG  1 
ATOM   567  S SD  . MET   B 2 40  ? -15.126 0.858   -13.238 1.00 61.50  ? 49  MET   B SD  1 
ATOM   568  C CE  . MET   B 2 40  ? -15.454 -0.478  -12.149 1.00 53.92  ? 49  MET   B CE  1 
ATOM   569  N N   . TRP   B 2 41  ? -16.954 3.118   -8.435  1.00 50.70  ? 50  TRP   B N   1 
ATOM   570  C CA  A TRP   B 2 41  ? -16.785 3.898   -7.218  0.50 51.10  ? 50  TRP   B CA  1 
ATOM   571  C CA  B TRP   B 2 41  ? -16.774 3.885   -7.210  0.50 51.10  ? 50  TRP   B CA  1 
ATOM   572  C C   . TRP   B 2 41  ? -15.861 5.090   -7.409  1.00 51.24  ? 50  TRP   B C   1 
ATOM   573  O O   . TRP   B 2 41  ? -16.120 6.144   -6.840  1.00 51.30  ? 50  TRP   B O   1 
ATOM   574  C CB  A TRP   B 2 41  ? -16.293 3.024   -6.047  0.50 51.14  ? 50  TRP   B CB  1 
ATOM   575  C CB  B TRP   B 2 41  ? -16.244 2.992   -6.062  0.50 51.15  ? 50  TRP   B CB  1 
ATOM   576  C CG  A TRP   B 2 41  ? -16.505 3.668   -4.708  0.50 51.61  ? 50  TRP   B CG  1 
ATOM   577  C CG  B TRP   B 2 41  ? -16.043 3.744   -4.778  0.50 51.65  ? 50  TRP   B CG  1 
ATOM   578  C CD1 A TRP   B 2 41  ? -17.627 3.600   -3.939  0.50 52.45  ? 50  TRP   B CD1 1 
ATOM   579  C CD1 B TRP   B 2 41  ? -14.962 4.498   -4.429  0.50 52.59  ? 50  TRP   B CD1 1 
ATOM   580  C CD2 A TRP   B 2 41  ? -15.601 4.548   -4.024  0.50 51.83  ? 50  TRP   B CD2 1 
ATOM   581  C CD2 B TRP   B 2 41  ? -16.997 3.901   -3.726  0.50 51.75  ? 50  TRP   B CD2 1 
ATOM   582  N NE1 A TRP   B 2 41  ? -17.472 4.366   -2.809  0.50 52.76  ? 50  TRP   B NE1 1 
ATOM   583  N NE1 B TRP   B 2 41  ? -15.187 5.117   -3.226  0.50 52.93  ? 50  TRP   B NE1 1 
ATOM   584  C CE2 A TRP   B 2 41  ? -16.240 4.964   -2.839  0.50 52.65  ? 50  TRP   B CE2 1 
ATOM   585  C CE2 B TRP   B 2 41  ? -16.426 4.757   -2.765  0.50 52.61  ? 50  TRP   B CE2 1 
ATOM   586  C CE3 A TRP   B 2 41  ? -14.308 5.016   -4.290  0.50 52.46  ? 50  TRP   B CE3 1 
ATOM   587  C CE3 B TRP   B 2 41  ? -18.270 3.381   -3.489  0.50 52.32  ? 50  TRP   B CE3 1 
ATOM   588  C CZ2 A TRP   B 2 41  ? -15.633 5.827   -1.928  0.50 53.49  ? 50  TRP   B CZ2 1 
ATOM   589  C CZ2 B TRP   B 2 41  ? -17.089 5.110   -1.593  0.50 53.26  ? 50  TRP   B CZ2 1 
ATOM   590  C CZ3 A TRP   B 2 41  ? -13.705 5.860   -3.379  0.50 53.44  ? 50  TRP   B CZ3 1 
ATOM   591  C CZ3 B TRP   B 2 41  ? -18.915 3.719   -2.320  0.50 53.25  ? 50  TRP   B CZ3 1 
ATOM   592  C CH2 A TRP   B 2 41  ? -14.360 6.248   -2.208  0.50 53.69  ? 50  TRP   B CH2 1 
ATOM   593  C CH2 B TRP   B 2 41  ? -18.329 4.578   -1.389  0.50 53.35  ? 50  TRP   B CH2 1 
ATOM   594  N N   . HIS   B 2 42  ? -14.774 4.930   -8.176  1.00 51.33  ? 51  HIS   B N   1 
ATOM   595  C CA  . HIS   B 2 42  ? -13.836 6.044   -8.370  1.00 52.16  ? 51  HIS   B CA  1 
ATOM   596  C C   . HIS   B 2 42  ? -14.418 7.216   -9.195  1.00 53.40  ? 51  HIS   B C   1 
ATOM   597  O O   . HIS   B 2 42  ? -13.814 8.280   -9.238  1.00 53.67  ? 51  HIS   B O   1 
ATOM   598  C CB  . HIS   B 2 42  ? -12.488 5.564   -8.936  1.00 52.10  ? 51  HIS   B CB  1 
ATOM   599  C CG  . HIS   B 2 42  ? -12.507 5.199   -10.391 1.00 51.94  ? 51  HIS   B CG  1 
ATOM   600  N ND1 . HIS   B 2 42  ? -12.713 3.898   -10.806 1.00 52.77  ? 51  HIS   B ND1 1 
ATOM   601  C CD2 . HIS   B 2 42  ? -12.305 5.975   -11.476 1.00 52.35  ? 51  HIS   B CD2 1 
ATOM   602  C CE1 . HIS   B 2 42  ? -12.651 3.928   -12.121 1.00 52.84  ? 51  HIS   B CE1 1 
ATOM   603  N NE2 . HIS   B 2 42  ? -12.407 5.157   -12.567 1.00 53.16  ? 51  HIS   B NE2 1 
ATOM   604  N N   . VAL   B 2 43  ? -15.595 7.042   -9.802  1.00 54.18  ? 52  VAL   B N   1 
ATOM   605  C CA  . VAL   B 2 43  ? -16.233 8.093   -10.579 1.00 55.51  ? 52  VAL   B CA  1 
ATOM   606  C C   . VAL   B 2 43  ? -16.920 9.113   -9.655  1.00 56.46  ? 52  VAL   B C   1 
ATOM   607  O O   . VAL   B 2 43  ? -16.651 10.313  -9.740  1.00 56.70  ? 52  VAL   B O   1 
ATOM   608  C CB  . VAL   B 2 43  ? -17.221 7.477   -11.604 1.00 56.52  ? 52  VAL   B CB  1 
ATOM   609  C CG1 . VAL   B 2 43  ? -17.998 8.563   -12.345 1.00 57.17  ? 52  VAL   B CG1 1 
ATOM   610  C CG2 . VAL   B 2 43  ? -16.493 6.558   -12.580 1.00 56.91  ? 52  VAL   B CG2 1 
ATOM   611  N N   . THR   B 2 44  ? -17.752 8.621   -8.730  1.00 56.72  ? 53  THR   B N   1 
ATOM   612  C CA  . THR   B 2 44  ? -18.536 9.449   -7.827  1.00 57.29  ? 53  THR   B CA  1 
ATOM   613  C C   . THR   B 2 44  ? -17.962 9.588   -6.423  1.00 59.05  ? 53  THR   B C   1 
ATOM   614  O O   . THR   B 2 44  ? -18.272 10.569  -5.742  1.00 59.79  ? 53  THR   B O   1 
ATOM   615  C CB  . THR   B 2 44  ? -19.964 8.893   -7.735  1.00 57.57  ? 53  THR   B CB  1 
ATOM   616  O OG1 . THR   B 2 44  ? -19.978 7.701   -6.948  1.00 57.60  ? 53  THR   B OG1 1 
ATOM   617  C CG2 . THR   B 2 44  ? -20.593 8.621   -9.109  1.00 57.86  ? 53  THR   B CG2 1 
ATOM   618  N N   . LYS   B 2 45  ? -17.190 8.588   -5.960  1.00 59.49  ? 54  LYS   B N   1 
ATOM   619  C CA  . LYS   B 2 45  ? -16.629 8.524   -4.599  1.00 60.51  ? 54  LYS   B CA  1 
ATOM   620  C C   . LYS   B 2 45  ? -17.726 8.337   -3.524  1.00 60.71  ? 54  LYS   B C   1 
ATOM   621  O O   . LYS   B 2 45  ? -17.509 8.686   -2.361  1.00 60.93  ? 54  LYS   B O   1 
ATOM   622  C CB  . LYS   B 2 45  ? -15.782 9.765   -4.257  1.00 63.08  ? 54  LYS   B CB  1 
ATOM   623  C CG  . LYS   B 2 45  ? -14.626 10.031  -5.197  1.00 67.84  ? 54  LYS   B CG  1 
ATOM   624  C CD  . LYS   B 2 45  ? -13.518 9.034   -5.017  1.00 73.43  ? 54  LYS   B CD  1 
ATOM   625  C CE  . LYS   B 2 45  ? -12.280 9.486   -5.750  1.00 78.87  ? 54  LYS   B CE  1 
ATOM   626  N NZ  . LYS   B 2 45  ? -12.545 9.714   -7.199  1.00 82.11  ? 54  LYS   B NZ  1 
ATOM   627  N N   . GLY   B 2 46  ? -18.876 7.792   -3.924  1.00 60.28  ? 55  GLY   B N   1 
ATOM   628  C CA  . GLY   B 2 46  ? -20.017 7.587   -3.047  1.00 60.25  ? 55  GLY   B CA  1 
ATOM   629  C C   . GLY   B 2 46  ? -20.948 8.780   -2.934  1.00 60.38  ? 55  GLY   B C   1 
ATOM   630  O O   . GLY   B 2 46  ? -21.963 8.699   -2.247  1.00 60.67  ? 55  GLY   B O   1 
ATOM   631  N N   . ALA   B 2 47  ? -20.624 9.898   -3.588  1.00 60.36  ? 56  ALA   B N   1 
ATOM   632  C CA  . ALA   B 2 47  ? -21.442 11.107  -3.524  1.00 60.92  ? 56  ALA   B CA  1 
ATOM   633  C C   . ALA   B 2 47  ? -22.808 10.951  -4.212  1.00 61.62  ? 56  ALA   B C   1 
ATOM   634  O O   . ALA   B 2 47  ? -22.967 10.102  -5.083  1.00 61.99  ? 56  ALA   B O   1 
ATOM   635  C CB  . ALA   B 2 47  ? -20.680 12.274  -4.138  1.00 60.98  ? 56  ALA   B CB  1 
ATOM   636  N N   . ALA   B 2 48  ? -23.789 11.766  -3.818  1.00 61.77  ? 57  ALA   B N   1 
ATOM   637  C CA  . ALA   B 2 48  ? -25.108 11.736  -4.431  1.00 62.81  ? 57  ALA   B CA  1 
ATOM   638  C C   . ALA   B 2 48  ? -25.047 12.333  -5.830  1.00 63.92  ? 57  ALA   B C   1 
ATOM   639  O O   . ALA   B 2 48  ? -24.213 13.194  -6.104  1.00 64.46  ? 57  ALA   B O   1 
ATOM   640  C CB  . ALA   B 2 48  ? -26.104 12.522  -3.586  1.00 63.12  ? 57  ALA   B CB  1 
ATOM   641  N N   . LEU   B 2 49  ? -25.940 11.877  -6.716  1.00 64.03  ? 58  LEU   B N   1 
ATOM   642  C CA  . LEU   B 2 49  ? -26.036 12.366  -8.089  1.00 64.51  ? 58  LEU   B CA  1 
ATOM   643  C C   . LEU   B 2 49  ? -27.371 13.096  -8.311  1.00 65.81  ? 58  LEU   B C   1 
ATOM   644  O O   . LEU   B 2 49  ? -28.317 12.931  -7.540  1.00 65.85  ? 58  LEU   B O   1 
ATOM   645  C CB  . LEU   B 2 49  ? -25.911 11.202  -9.086  1.00 64.05  ? 58  LEU   B CB  1 
ATOM   646  C CG  . LEU   B 2 49  ? -24.729 10.297  -8.909  1.00 64.77  ? 58  LEU   B CG  1 
ATOM   647  C CD1 . LEU   B 2 49  ? -24.844 9.114   -9.818  1.00 65.19  ? 58  LEU   B CD1 1 
ATOM   648  C CD2 . LEU   B 2 49  ? -23.427 11.045  -9.121  1.00 65.24  ? 58  LEU   B CD2 1 
ATOM   649  N N   . ARG   B 2 50  ? -27.456 13.882  -9.378  1.00 66.89  ? 59  ARG   B N   1 
ATOM   650  C CA  . ARG   B 2 50  ? -28.667 14.615  -9.699  1.00 68.41  ? 59  ARG   B CA  1 
ATOM   651  C C   . ARG   B 2 50  ? -29.188 14.184  -11.075 1.00 69.65  ? 59  ARG   B C   1 
ATOM   652  O O   . ARG   B 2 50  ? -28.397 13.960  -11.990 1.00 69.60  ? 59  ARG   B O   1 
ATOM   653  C CB  . ARG   B 2 50  ? -28.373 16.119  -9.627  1.00 70.32  ? 59  ARG   B CB  1 
ATOM   654  C CG  . ARG   B 2 50  ? -29.470 17.006  -10.174 1.00 74.95  ? 59  ARG   B CG  1 
ATOM   655  C CD  . ARG   B 2 50  ? -29.202 18.483  -9.940  1.00 79.63  ? 59  ARG   B CD  1 
ATOM   656  N NE  . ARG   B 2 50  ? -27.908 18.933  -10.463 1.00 83.56  ? 59  ARG   B NE  1 
ATOM   657  C CZ  . ARG   B 2 50  ? -27.702 19.341  -11.712 1.00 86.56  ? 59  ARG   B CZ  1 
ATOM   658  N NH1 . ARG   B 2 50  ? -28.695 19.332  -12.595 1.00 86.03  ? 59  ARG   B NH1 1 
ATOM   659  N NH2 . ARG   B 2 50  ? -26.497 19.749  -12.091 1.00 87.29  ? 59  ARG   B NH2 1 
ATOM   660  N N   . SER   B 2 51  ? -30.503 13.997  -11.208 1.00 70.74  ? 60  SER   B N   1 
ATOM   661  C CA  . SER   B 2 51  ? -31.086 13.631  -12.500 1.00 72.71  ? 60  SER   B CA  1 
ATOM   662  C C   . SER   B 2 51  ? -32.229 14.587  -12.774 1.00 74.29  ? 60  SER   B C   1 
ATOM   663  O O   . SER   B 2 51  ? -33.371 14.312  -12.408 1.00 74.69  ? 60  SER   B O   1 
ATOM   664  C CB  . SER   B 2 51  ? -31.575 12.189  -12.502 1.00 74.22  ? 60  SER   B CB  1 
ATOM   665  O OG  . SER   B 2 51  ? -32.085 11.870  -13.786 1.00 76.65  ? 60  SER   B OG  1 
ATOM   666  N N   . GLY   B 2 52  ? -31.902 15.732  -13.363 1.00 74.82  ? 61  GLY   B N   1 
ATOM   667  C CA  . GLY   B 2 52  ? -32.872 16.787  -13.607 1.00 75.51  ? 61  GLY   B CA  1 
ATOM   668  C C   . GLY   B 2 52  ? -33.184 17.432  -12.277 1.00 76.16  ? 61  GLY   B C   1 
ATOM   669  O O   . GLY   B 2 52  ? -32.287 17.963  -11.618 1.00 76.50  ? 61  GLY   B O   1 
ATOM   670  N N   . GLU   B 2 53  ? -34.437 17.325  -11.836 1.00 76.04  ? 62  GLU   B N   1 
ATOM   671  C CA  . GLU   B 2 53  ? -34.820 17.821  -10.518 1.00 76.17  ? 62  GLU   B CA  1 
ATOM   672  C C   . GLU   B 2 53  ? -34.679 16.733  -9.423  1.00 75.54  ? 62  GLU   B C   1 
ATOM   673  O O   . GLU   B 2 53  ? -34.581 17.072  -8.240  1.00 75.77  ? 62  GLU   B O   1 
ATOM   674  C CB  . GLU   B 2 53  ? -36.245 18.364  -10.546 1.00 79.10  ? 62  GLU   B CB  1 
ATOM   675  C CG  . GLU   B 2 53  ? -36.314 19.877  -10.587 1.00 85.39  ? 62  GLU   B CG  1 
ATOM   676  C CD  . GLU   B 2 53  ? -37.733 20.400  -10.689 1.00 93.47  ? 62  GLU   B CD  1 
ATOM   677  O OE1 . GLU   B 2 53  ? -38.539 19.772  -11.415 1.00 94.71  ? 62  GLU   B OE1 1 
ATOM   678  O OE2 . GLU   B 2 53  ? -38.042 21.432  -10.047 1.00 96.26  ? 62  GLU   B OE2 1 
ATOM   679  N N   . GLY   B 2 54  ? -34.681 15.454  -9.828  1.00 74.50  ? 63  GLY   B N   1 
ATOM   680  C CA  . GLY   B 2 54  ? -34.585 14.304  -8.937  1.00 73.96  ? 63  GLY   B CA  1 
ATOM   681  C C   . GLY   B 2 54  ? -33.211 14.061  -8.347  1.00 72.95  ? 63  GLY   B C   1 
ATOM   682  O O   . GLY   B 2 54  ? -32.208 14.553  -8.866  1.00 73.32  ? 63  GLY   B O   1 
ATOM   683  N N   . ARG   B 2 55  ? -33.149 13.285  -7.259  1.00 71.49  ? 64  ARG   B N   1 
ATOM   684  C CA  . ARG   B 2 55  ? -31.877 12.994  -6.599  1.00 70.52  ? 64  ARG   B CA  1 
ATOM   685  C C   . ARG   B 2 55  ? -31.612 11.479  -6.487  1.00 68.62  ? 64  ARG   B C   1 
ATOM   686  O O   . ARG   B 2 55  ? -32.507 10.723  -6.109  1.00 68.87  ? 64  ARG   B O   1 
ATOM   687  C CB  . ARG   B 2 55  ? -31.868 13.649  -5.208  1.00 71.99  ? 64  ARG   B CB  1 
ATOM   688  C CG  . ARG   B 2 55  ? -30.549 13.560  -4.462  1.00 75.93  ? 64  ARG   B CG  1 
ATOM   689  C CD  . ARG   B 2 55  ? -30.794 13.757  -2.975  1.00 80.31  ? 64  ARG   B CD  1 
ATOM   690  N NE  . ARG   B 2 55  ? -29.567 13.698  -2.170  1.00 84.03  ? 64  ARG   B NE  1 
ATOM   691  C CZ  . ARG   B 2 55  ? -29.107 14.709  -1.434  1.00 86.25  ? 64  ARG   B CZ  1 
ATOM   692  N NH1 . ARG   B 2 55  ? -29.754 15.873  -1.412  1.00 86.37  ? 64  ARG   B NH1 1 
ATOM   693  N NH2 . ARG   B 2 55  ? -27.998 14.567  -0.717  1.00 85.03  ? 64  ARG   B NH2 1 
ATOM   694  N N   . LEU   B 2 56  ? -30.392 11.037  -6.810  1.00 66.53  ? 65  LEU   B N   1 
ATOM   695  C CA  . LEU   B 2 56  ? -30.034 9.628   -6.680  1.00 65.17  ? 65  LEU   B CA  1 
ATOM   696  C C   . LEU   B 2 56  ? -29.134 9.467   -5.460  1.00 64.21  ? 65  LEU   B C   1 
ATOM   697  O O   . LEU   B 2 56  ? -28.038 10.017  -5.424  1.00 64.02  ? 65  LEU   B O   1 
ATOM   698  C CB  . LEU   B 2 56  ? -29.296 9.115   -7.917  1.00 64.99  ? 65  LEU   B CB  1 
ATOM   699  C CG  . LEU   B 2 56  ? -29.882 9.434   -9.280  1.00 66.01  ? 65  LEU   B CG  1 
ATOM   700  C CD1 . LEU   B 2 56  ? -28.926 9.020   -10.366 1.00 66.43  ? 65  LEU   B CD1 1 
ATOM   701  C CD2 . LEU   B 2 56  ? -31.202 8.734   -9.486  1.00 66.55  ? 65  LEU   B CD2 1 
ATOM   702  N N   . ASP   B 2 57  ? -29.597 8.737   -4.458  1.00 63.51  ? 66  ASP   B N   1 
ATOM   703  C CA  . ASP   B 2 57  ? -28.825 8.502   -3.245  1.00 63.25  ? 66  ASP   B CA  1 
ATOM   704  C C   . ASP   B 2 57  ? -28.202 7.106   -3.314  1.00 61.74  ? 66  ASP   B C   1 
ATOM   705  O O   . ASP   B 2 57  ? -28.865 6.154   -3.735  1.00 62.20  ? 66  ASP   B O   1 
ATOM   706  C CB  . ASP   B 2 57  ? -29.738 8.617   -2.024  1.00 66.76  ? 66  ASP   B CB  1 
ATOM   707  C CG  . ASP   B 2 57  ? -30.332 10.005  -1.834  1.00 74.74  ? 66  ASP   B CG  1 
ATOM   708  O OD1 . ASP   B 2 57  ? -29.556 10.949  -1.523  1.00 76.54  ? 66  ASP   B OD1 1 
ATOM   709  O OD2 . ASP   B 2 57  ? -31.575 10.150  -1.984  1.00 77.23  ? 66  ASP   B OD2 1 
ATOM   710  N N   . PRO   B 2 58  ? -26.924 6.961   -2.931  1.00 59.69  ? 67  PRO   B N   1 
ATOM   711  C CA  . PRO   B 2 58  ? -26.285 5.638   -3.005  1.00 58.45  ? 67  PRO   B CA  1 
ATOM   712  C C   . PRO   B 2 58  ? -26.958 4.563   -2.145  1.00 57.29  ? 67  PRO   B C   1 
ATOM   713  O O   . PRO   B 2 58  ? -27.537 4.854   -1.099  1.00 57.95  ? 67  PRO   B O   1 
ATOM   714  C CB  . PRO   B 2 58  ? -24.840 5.915   -2.577  1.00 59.24  ? 67  PRO   B CB  1 
ATOM   715  C CG  . PRO   B 2 58  ? -24.907 7.180   -1.793  1.00 59.94  ? 67  PRO   B CG  1 
ATOM   716  C CD  . PRO   B 2 58  ? -25.999 7.989   -2.418  1.00 58.69  ? 67  PRO   B CD  1 
ATOM   717  N N   . TYR   B 2 59  ? -26.913 3.317   -2.606  1.00 55.34  ? 68  TYR   B N   1 
ATOM   718  C CA  . TYR   B 2 59  ? -27.539 2.214   -1.894  1.00 53.68  ? 68  TYR   B CA  1 
ATOM   719  C C   . TYR   B 2 59  ? -26.489 1.247   -1.388  1.00 52.87  ? 68  TYR   B C   1 
ATOM   720  O O   . TYR   B 2 59  ? -26.535 0.846   -0.235  1.00 53.53  ? 68  TYR   B O   1 
ATOM   721  C CB  . TYR   B 2 59  ? -28.558 1.519   -2.806  1.00 52.84  ? 68  TYR   B CB  1 
ATOM   722  C CG  . TYR   B 2 59  ? -29.311 0.379   -2.162  1.00 52.58  ? 68  TYR   B CG  1 
ATOM   723  C CD1 . TYR   B 2 59  ? -28.742 -0.882  -2.052  1.00 53.19  ? 68  TYR   B CD1 1 
ATOM   724  C CD2 . TYR   B 2 59  ? -30.623 0.536   -1.748  1.00 53.06  ? 68  TYR   B CD2 1 
ATOM   725  C CE1 . TYR   B 2 59  ? -29.435 -1.940  -1.489  1.00 53.93  ? 68  TYR   B CE1 1 
ATOM   726  C CE2 . TYR   B 2 59  ? -31.336 -0.521  -1.208  1.00 53.98  ? 68  TYR   B CE2 1 
ATOM   727  C CZ  . TYR   B 2 59  ? -30.738 -1.761  -1.081  1.00 55.02  ? 68  TYR   B CZ  1 
ATOM   728  O OH  . TYR   B 2 59  ? -31.437 -2.809  -0.526  1.00 56.61  ? 68  TYR   B OH  1 
ATOM   729  N N   . TRP   B 2 60  ? -25.554 0.872   -2.248  1.00 51.82  ? 69  TRP   B N   1 
ATOM   730  C CA  . TRP   B 2 60  ? -24.481 -0.073  -1.965  1.00 51.49  ? 69  TRP   B CA  1 
ATOM   731  C C   . TRP   B 2 60  ? -23.192 0.401   -2.660  1.00 50.75  ? 69  TRP   B C   1 
ATOM   732  O O   . TRP   B 2 60  ? -23.253 1.008   -3.725  1.00 50.47  ? 69  TRP   B O   1 
ATOM   733  C CB  . TRP   B 2 60  ? -24.884 -1.490  -2.466  1.00 51.70  ? 69  TRP   B CB  1 
ATOM   734  C CG  . TRP   B 2 60  ? -23.746 -2.471  -2.494  1.00 52.29  ? 69  TRP   B CG  1 
ATOM   735  C CD1 . TRP   B 2 60  ? -23.233 -3.160  -1.434  1.00 53.28  ? 69  TRP   B CD1 1 
ATOM   736  C CD2 . TRP   B 2 60  ? -22.872 -2.728  -3.602  1.00 52.31  ? 69  TRP   B CD2 1 
ATOM   737  N NE1 . TRP   B 2 60  ? -22.106 -3.846  -1.819  1.00 53.72  ? 69  TRP   B NE1 1 
ATOM   738  C CE2 . TRP   B 2 60  ? -21.863 -3.600  -3.147  1.00 53.20  ? 69  TRP   B CE2 1 
ATOM   739  C CE3 . TRP   B 2 60  ? -22.841 -2.300  -4.933  1.00 52.84  ? 69  TRP   B CE3 1 
ATOM   740  C CZ2 . TRP   B 2 60  ? -20.854 -4.071  -3.984  1.00 53.69  ? 69  TRP   B CZ2 1 
ATOM   741  C CZ3 . TRP   B 2 60  ? -21.833 -2.757  -5.755  1.00 53.68  ? 69  TRP   B CZ3 1 
ATOM   742  C CH2 . TRP   B 2 60  ? -20.866 -3.648  -5.285  1.00 53.76  ? 69  TRP   B CH2 1 
ATOM   743  N N   . GLY   B 2 61  ? -22.044 0.069   -2.087  1.00 50.53  ? 70  GLY   B N   1 
ATOM   744  C CA  . GLY   B 2 61  ? -20.750 0.406   -2.672  1.00 51.00  ? 70  GLY   B CA  1 
ATOM   745  C C   . GLY   B 2 61  ? -19.603 -0.336  -2.021  1.00 51.32  ? 70  GLY   B C   1 
ATOM   746  O O   . GLY   B 2 61  ? -19.722 -0.766  -0.874  1.00 51.73  ? 70  GLY   B O   1 
ATOM   747  N N   . ASP   B 2 62  ? -18.486 -0.501  -2.737  1.00 51.07  ? 71  ASP   B N   1 
ATOM   748  C CA  . ASP   B 2 62  ? -17.301 -1.205  -2.225  1.00 51.30  ? 71  ASP   B CA  1 
ATOM   749  C C   . ASP   B 2 62  ? -16.072 -0.685  -2.978  1.00 51.39  ? 71  ASP   B C   1 
ATOM   750  O O   . ASP   B 2 62  ? -16.045 -0.707  -4.210  1.00 51.14  ? 71  ASP   B O   1 
ATOM   751  C CB  . ASP   B 2 62  ? -17.449 -2.728  -2.398  1.00 53.03  ? 71  ASP   B CB  1 
ATOM   752  C CG  . ASP   B 2 62  ? -16.342 -3.554  -1.774  1.00 59.08  ? 71  ASP   B CG  1 
ATOM   753  O OD1 . ASP   B 2 62  ? -15.244 -3.622  -2.364  1.00 59.80  ? 71  ASP   B OD1 1 
ATOM   754  O OD2 . ASP   B 2 62  ? -16.583 -4.159  -0.715  1.00 62.35  ? 71  ASP   B OD2 1 
ATOM   755  N N   . VAL   B 2 63  ? -15.067 -0.193  -2.234  1.00 51.25  ? 72  VAL   B N   1 
ATOM   756  C CA  . VAL   B 2 63  ? -13.859 0.391   -2.808  1.00 51.12  ? 72  VAL   B CA  1 
ATOM   757  C C   . VAL   B 2 63  ? -12.969 -0.670  -3.470  1.00 51.54  ? 72  VAL   B C   1 
ATOM   758  O O   . VAL   B 2 63  ? -12.381 -0.380  -4.513  1.00 51.75  ? 72  VAL   B O   1 
ATOM   759  C CB  . VAL   B 2 63  ? -13.122 1.258   -1.757  1.00 51.32  ? 72  VAL   B CB  1 
ATOM   760  C CG1 . VAL   B 2 63  ? -11.648 1.456   -2.090  1.00 51.72  ? 72  VAL   B CG1 1 
ATOM   761  C CG2 . VAL   B 2 63  ? -13.815 2.598   -1.597  1.00 51.77  ? 72  VAL   B CG2 1 
ATOM   762  N N   . LYS   B 2 64  ? -12.904 -1.897  -2.917  1.00 51.62  ? 73  LYS   B N   1 
ATOM   763  C CA  . LYS   B 2 64  ? -12.077 -2.946  -3.524  1.00 52.07  ? 73  LYS   B CA  1 
ATOM   764  C C   . LYS   B 2 64  ? -12.667 -3.429  -4.850  1.00 52.65  ? 73  LYS   B C   1 
ATOM   765  O O   . LYS   B 2 64  ? -11.940 -3.507  -5.829  1.00 52.68  ? 73  LYS   B O   1 
ATOM   766  C CB  . LYS   B 2 64  ? -11.836 -4.111  -2.564  1.00 53.45  ? 73  LYS   B CB  1 
ATOM   767  C CG  . LYS   B 2 64  ? -10.541 -4.859  -2.850  1.00 56.07  ? 73  LYS   B CG  1 
ATOM   768  C CD  . LYS   B 2 64  ? -10.553 -6.195  -2.170  1.00 59.55  ? 73  LYS   B CD  1 
ATOM   769  C CE  . LYS   B 2 64  ? -9.186  -6.796  -2.073  1.00 63.29  ? 73  LYS   B CE  1 
ATOM   770  N NZ  . LYS   B 2 64  ? -9.264  -8.244  -1.747  1.00 65.85  ? 73  LYS   B NZ  1 
ATOM   771  N N   . GLN   B 2 65  ? -13.984 -3.721  -4.902  1.00 52.88  ? 74  GLN   B N   1 
ATOM   772  C CA  . GLN   B 2 65  ? -14.643 -4.100  -6.160  1.00 53.18  ? 74  GLN   B CA  1 
ATOM   773  C C   . GLN   B 2 65  ? -14.702 -2.910  -7.136  1.00 53.08  ? 74  GLN   B C   1 
ATOM   774  O O   . GLN   B 2 65  ? -14.840 -3.116  -8.343  1.00 53.43  ? 74  GLN   B O   1 
ATOM   775  C CB  . GLN   B 2 65  ? -16.082 -4.586  -5.913  1.00 55.63  ? 74  GLN   B CB  1 
ATOM   776  C CG  . GLN   B 2 65  ? -16.217 -5.836  -5.050  1.00 60.83  ? 74  GLN   B CG  1 
ATOM   777  C CD  . GLN   B 2 65  ? -17.657 -6.331  -4.957  1.00 66.46  ? 74  GLN   B CD  1 
ATOM   778  O OE1 . GLN   B 2 65  ? -18.427 -6.332  -5.944  1.00 66.99  ? 74  GLN   B OE1 1 
ATOM   779  N NE2 . GLN   B 2 65  ? -18.044 -6.798  -3.761  1.00 67.77  ? 74  GLN   B NE2 1 
ATOM   780  N N   . ASP   B 2 66  ? -14.646 -1.671  -6.599  1.00 52.52  ? 75  ASP   B N   1 
ATOM   781  C CA  . ASP   B 2 66  ? -14.711 -0.391  -7.297  1.00 52.06  ? 75  ASP   B CA  1 
ATOM   782  C C   . ASP   B 2 66  ? -16.054 -0.218  -7.957  1.00 50.64  ? 75  ASP   B C   1 
ATOM   783  O O   . ASP   B 2 66  ? -16.131 0.296   -9.059  1.00 50.52  ? 75  ASP   B O   1 
ATOM   784  C CB  . ASP   B 2 66  ? -13.556 -0.210  -8.295  1.00 54.32  ? 75  ASP   B CB  1 
ATOM   785  C CG  . ASP   B 2 66  ? -13.442 1.208   -8.801  1.00 59.41  ? 75  ASP   B CG  1 
ATOM   786  O OD1 . ASP   B 2 66  ? -13.559 2.143   -7.980  1.00 61.54  ? 75  ASP   B OD1 1 
ATOM   787  O OD2 . ASP   B 2 66  ? -13.253 1.384   -10.007 1.00 60.85  ? 75  ASP   B OD2 1 
ATOM   788  N N   . LEU   B 2 67  ? -17.131 -0.610  -7.271  1.00 49.42  ? 76  LEU   B N   1 
ATOM   789  C CA  . LEU   B 2 67  ? -18.480 -0.485  -7.814  1.00 48.64  ? 76  LEU   B CA  1 
ATOM   790  C C   . LEU   B 2 67  ? -19.395 0.233   -6.838  1.00 47.94  ? 76  LEU   B C   1 
ATOM   791  O O   . LEU   B 2 67  ? -19.132 0.223   -5.638  1.00 48.37  ? 76  LEU   B O   1 
ATOM   792  C CB  . LEU   B 2 67  ? -19.050 -1.867  -8.142  1.00 48.69  ? 76  LEU   B CB  1 
ATOM   793  C CG  . LEU   B 2 67  ? -18.335 -2.625  -9.246  1.00 49.49  ? 76  LEU   B CG  1 
ATOM   794  C CD1 . LEU   B 2 67  ? -18.782 -4.042  -9.294  1.00 49.45  ? 76  LEU   B CD1 1 
ATOM   795  C CD2 . LEU   B 2 67  ? -18.520 -1.941  -10.591 1.00 50.14  ? 76  LEU   B CD2 1 
ATOM   796  N N   . VAL   B 2 68  ? -20.456 0.878   -7.351  1.00 46.97  ? 77  VAL   B N   1 
ATOM   797  C CA  . VAL   B 2 68  ? -21.432 1.603   -6.540  1.00 46.61  ? 77  VAL   B CA  1 
ATOM   798  C C   . VAL   B 2 68  ? -22.813 1.623   -7.241  1.00 46.88  ? 77  VAL   B C   1 
ATOM   799  O O   . VAL   B 2 68  ? -22.891 1.728   -8.458  1.00 46.98  ? 77  VAL   B O   1 
ATOM   800  C CB  . VAL   B 2 68  ? -20.903 3.010   -6.128  1.00 46.66  ? 77  VAL   B CB  1 
ATOM   801  C CG1 . VAL   B 2 68  ? -20.693 3.909   -7.326  1.00 46.57  ? 77  VAL   B CG1 1 
ATOM   802  C CG2 . VAL   B 2 68  ? -21.788 3.676   -5.087  1.00 46.87  ? 77  VAL   B CG2 1 
ATOM   803  N N   . SER   B 2 69  ? -23.888 1.422   -6.486  1.00 47.13  ? 78  SER   B N   1 
ATOM   804  C CA  . SER   B 2 69  ? -25.245 1.424   -7.030  1.00 47.74  ? 78  SER   B CA  1 
ATOM   805  C C   . SER   B 2 69  ? -26.098 2.519   -6.373  1.00 48.88  ? 78  SER   B C   1 
ATOM   806  O O   . SER   B 2 69  ? -25.855 2.910   -5.235  1.00 48.90  ? 78  SER   B O   1 
ATOM   807  C CB  . SER   B 2 69  ? -25.896 0.042   -6.922  1.00 47.82  ? 78  SER   B CB  1 
ATOM   808  O OG  . SER   B 2 69  ? -26.253 -0.314  -5.599  1.00 48.25  ? 78  SER   B OG  1 
ATOM   809  N N   . TYR   B 2 70  ? -27.049 3.057   -7.120  1.00 49.77  ? 79  TYR   B N   1 
ATOM   810  C CA  . TYR   B 2 70  ? -27.905 4.149   -6.664  1.00 51.14  ? 79  TYR   B CA  1 
ATOM   811  C C   . TYR   B 2 70  ? -29.360 3.725   -6.761  1.00 52.47  ? 79  TYR   B C   1 
ATOM   812  O O   . TYR   B 2 70  ? -29.735 3.021   -7.702  1.00 53.06  ? 79  TYR   B O   1 
ATOM   813  C CB  . TYR   B 2 70  ? -27.665 5.407   -7.527  1.00 51.47  ? 79  TYR   B CB  1 
ATOM   814  C CG  . TYR   B 2 70  ? -26.323 6.050   -7.262  1.00 52.77  ? 79  TYR   B CG  1 
ATOM   815  C CD1 . TYR   B 2 70  ? -25.158 5.532   -7.816  1.00 53.81  ? 79  TYR   B CD1 1 
ATOM   816  C CD2 . TYR   B 2 70  ? -26.211 7.150   -6.421  1.00 54.04  ? 79  TYR   B CD2 1 
ATOM   817  C CE1 . TYR   B 2 70  ? -23.916 6.088   -7.535  1.00 54.90  ? 79  TYR   B CE1 1 
ATOM   818  C CE2 . TYR   B 2 70  ? -24.974 7.709   -6.125  1.00 54.97  ? 79  TYR   B CE2 1 
ATOM   819  C CZ  . TYR   B 2 70  ? -23.828 7.179   -6.689  1.00 55.92  ? 79  TYR   B CZ  1 
ATOM   820  O OH  . TYR   B 2 70  ? -22.609 7.745   -6.414  1.00 57.25  ? 79  TYR   B OH  1 
ATOM   821  N N   . CYS   B 2 71  ? -30.166 4.123   -5.771  1.00 52.74  ? 80  CYS   B N   1 
ATOM   822  C CA  . CYS   B 2 71  ? -31.604 3.853   -5.668  1.00 53.45  ? 80  CYS   B CA  1 
ATOM   823  C C   . CYS   B 2 71  ? -31.947 2.425   -5.270  1.00 52.89  ? 80  CYS   B C   1 
ATOM   824  O O   . CYS   B 2 71  ? -33.028 2.204   -4.720  1.00 53.19  ? 80  CYS   B O   1 
ATOM   825  C CB  . CYS   B 2 71  ? -32.350 4.268   -6.929  1.00 55.35  ? 80  CYS   B CB  1 
ATOM   826  S SG  . CYS   B 2 71  ? -32.263 6.041   -7.281  1.00 62.20  ? 80  CYS   B SG  1 
ATOM   827  N N   . GLY   B 2 72  ? -31.048 1.481   -5.513  1.00 51.89  ? 81  GLY   B N   1 
ATOM   828  C CA  . GLY   B 2 72  ? -31.302 0.097   -5.146  1.00 51.82  ? 81  GLY   B CA  1 
ATOM   829  C C   . GLY   B 2 72  ? -30.086 -0.786  -5.260  1.00 52.10  ? 81  GLY   B C   1 
ATOM   830  O O   . GLY   B 2 72  ? -28.994 -0.334  -5.610  1.00 52.17  ? 81  GLY   B O   1 
ATOM   831  N N   . PRO   B 2 73  ? -30.265 -2.076  -4.955  1.00 52.10  ? 82  PRO   B N   1 
ATOM   832  C CA  . PRO   B 2 73  ? -29.139 -3.019  -5.051  1.00 52.48  ? 82  PRO   B CA  1 
ATOM   833  C C   . PRO   B 2 73  ? -28.682 -3.281  -6.485  1.00 53.04  ? 82  PRO   B C   1 
ATOM   834  O O   . PRO   B 2 73  ? -29.454 -3.090  -7.422  1.00 53.45  ? 82  PRO   B O   1 
ATOM   835  C CB  . PRO   B 2 73  ? -29.714 -4.295  -4.434  1.00 52.87  ? 82  PRO   B CB  1 
ATOM   836  C CG  . PRO   B 2 73  ? -31.187 -4.179  -4.686  1.00 52.83  ? 82  PRO   B CG  1 
ATOM   837  C CD  . PRO   B 2 73  ? -31.493 -2.740  -4.481  1.00 51.13  ? 82  PRO   B CD  1 
ATOM   838  N N   . TRP   B 2 74  ? -27.432 -3.760  -6.648  1.00 52.85  ? 83  TRP   B N   1 
ATOM   839  C CA  . TRP   B 2 74  ? -26.828 -4.095  -7.941  1.00 53.05  ? 83  TRP   B CA  1 
ATOM   840  C C   . TRP   B 2 74  ? -27.719 -5.075  -8.722  1.00 54.52  ? 83  TRP   B C   1 
ATOM   841  O O   . TRP   B 2 74  ? -28.075 -6.131  -8.195  1.00 55.18  ? 83  TRP   B O   1 
ATOM   842  C CB  . TRP   B 2 74  ? -25.429 -4.692  -7.711  1.00 52.30  ? 83  TRP   B CB  1 
ATOM   843  C CG  . TRP   B 2 74  ? -24.633 -4.863  -8.961  1.00 52.02  ? 83  TRP   B CG  1 
ATOM   844  C CD1 . TRP   B 2 74  ? -24.582 -5.968  -9.751  1.00 52.74  ? 83  TRP   B CD1 1 
ATOM   845  C CD2 . TRP   B 2 74  ? -23.769 -3.892  -9.568  1.00 51.85  ? 83  TRP   B CD2 1 
ATOM   846  N NE1 . TRP   B 2 74  ? -23.763 -5.739  -10.832 1.00 53.11  ? 83  TRP   B NE1 1 
ATOM   847  C CE2 . TRP   B 2 74  ? -23.263 -4.464  -10.752 1.00 52.70  ? 83  TRP   B CE2 1 
ATOM   848  C CE3 . TRP   B 2 74  ? -23.389 -2.588  -9.235  1.00 52.14  ? 83  TRP   B CE3 1 
ATOM   849  C CZ2 . TRP   B 2 74  ? -22.401 -3.775  -11.605 1.00 53.03  ? 83  TRP   B CZ2 1 
ATOM   850  C CZ3 . TRP   B 2 74  ? -22.542 -1.905  -10.083 1.00 52.83  ? 83  TRP   B CZ3 1 
ATOM   851  C CH2 . TRP   B 2 74  ? -22.058 -2.497  -11.251 1.00 53.07  ? 83  TRP   B CH2 1 
ATOM   852  N N   . LYS   B 2 75  ? -28.105 -4.717  -9.960  1.00 54.84  ? 84  LYS   B N   1 
ATOM   853  C CA  . LYS   B 2 75  ? -29.001 -5.546  -10.769 1.00 55.38  ? 84  LYS   B CA  1 
ATOM   854  C C   . LYS   B 2 75  ? -28.285 -6.357  -11.850 1.00 57.26  ? 84  LYS   B C   1 
ATOM   855  O O   . LYS   B 2 75  ? -28.836 -7.345  -12.336 1.00 57.65  ? 84  LYS   B O   1 
ATOM   856  C CB  . LYS   B 2 75  ? -30.092 -4.684  -11.435 1.00 55.16  ? 84  LYS   B CB  1 
ATOM   857  C CG  . LYS   B 2 75  ? -30.898 -3.818  -10.485 1.00 56.19  ? 84  LYS   B CG  1 
ATOM   858  C CD  . LYS   B 2 75  ? -31.908 -4.606  -9.693  1.00 57.34  ? 84  LYS   B CD  1 
ATOM   859  C CE  . LYS   B 2 75  ? -32.665 -3.714  -8.746  1.00 58.68  ? 84  LYS   B CE  1 
ATOM   860  N NZ  . LYS   B 2 75  ? -33.822 -4.411  -8.132  1.00 60.23  ? 84  LYS   B NZ  1 
ATOM   861  N N   . LEU   B 2 76  ? -27.101 -5.911  -12.282 1.00 57.95  ? 85  LEU   B N   1 
ATOM   862  C CA  . LEU   B 2 76  ? -26.375 -6.570  -13.368 1.00 58.54  ? 85  LEU   B CA  1 
ATOM   863  C C   . LEU   B 2 76  ? -25.770 -7.897  -12.907 1.00 60.27  ? 85  LEU   B C   1 
ATOM   864  O O   . LEU   B 2 76  ? -25.076 -7.932  -11.902 1.00 60.46  ? 85  LEU   B O   1 
ATOM   865  C CB  . LEU   B 2 76  ? -25.309 -5.632  -13.952 1.00 57.96  ? 85  LEU   B CB  1 
ATOM   866  C CG  . LEU   B 2 76  ? -25.744 -4.180  -14.196 1.00 58.47  ? 85  LEU   B CG  1 
ATOM   867  C CD1 . LEU   B 2 76  ? -24.599 -3.333  -14.673 1.00 58.74  ? 85  LEU   B CD1 1 
ATOM   868  C CD2 . LEU   B 2 76  ? -26.883 -4.097  -15.164 1.00 58.79  ? 85  LEU   B CD2 1 
ATOM   869  N N   . ASP   B 2 77  ? -26.049 -8.994  -13.624 1.00 61.62  ? 86  ASP   B N   1 
ATOM   870  C CA  . ASP   B 2 77  ? -25.571 -10.317 -13.221 1.00 63.32  ? 86  ASP   B CA  1 
ATOM   871  C C   . ASP   B 2 77  ? -25.037 -11.188 -14.370 1.00 64.49  ? 86  ASP   B C   1 
ATOM   872  O O   . ASP   B 2 77  ? -24.665 -12.336 -14.125 1.00 64.94  ? 86  ASP   B O   1 
ATOM   873  C CB  . ASP   B 2 77  ? -26.647 -11.079 -12.420 1.00 65.66  ? 86  ASP   B CB  1 
ATOM   874  C CG  . ASP   B 2 77  ? -27.969 -11.304 -13.142 1.00 73.17  ? 86  ASP   B CG  1 
ATOM   875  O OD1 . ASP   B 2 77  ? -28.364 -10.434 -13.966 1.00 74.61  ? 86  ASP   B OD1 1 
ATOM   876  O OD2 . ASP   B 2 77  ? -28.627 -12.334 -12.867 1.00 76.40  ? 86  ASP   B OD2 1 
ATOM   877  N N   . ALA   B 2 78  ? -24.958 -10.656 -15.598 1.00 64.79  ? 87  ALA   B N   1 
ATOM   878  C CA  . ALA   B 2 78  ? -24.419 -11.429 -16.724 1.00 65.46  ? 87  ALA   B CA  1 
ATOM   879  C C   . ALA   B 2 78  ? -22.895 -11.589 -16.591 1.00 66.36  ? 87  ALA   B C   1 
ATOM   880  O O   . ALA   B 2 78  ? -22.245 -10.806 -15.895 1.00 66.35  ? 87  ALA   B O   1 
ATOM   881  C CB  . ALA   B 2 78  ? -24.774 -10.774 -18.055 1.00 65.11  ? 87  ALA   B CB  1 
ATOM   882  N N   . ALA   B 2 79  ? -22.330 -12.618 -17.235 1.00 66.83  ? 88  ALA   B N   1 
ATOM   883  C CA  . ALA   B 2 79  ? -20.900 -12.857 -17.153 1.00 67.76  ? 88  ALA   B CA  1 
ATOM   884  C C   . ALA   B 2 79  ? -20.311 -13.272 -18.482 1.00 68.62  ? 88  ALA   B C   1 
ATOM   885  O O   . ALA   B 2 79  ? -20.950 -14.014 -19.218 1.00 68.85  ? 88  ALA   B O   1 
ATOM   886  C CB  . ALA   B 2 79  ? -20.623 -13.925 -16.115 1.00 68.09  ? 88  ALA   B CB  1 
ATOM   887  N N   . TRP   B 2 80  ? -19.069 -12.845 -18.774 1.00 69.01  ? 89  TRP   B N   1 
ATOM   888  C CA  . TRP   B 2 80  ? -18.355 -13.238 -19.990 1.00 69.87  ? 89  TRP   B CA  1 
ATOM   889  C C   . TRP   B 2 80  ? -18.159 -14.747 -19.978 1.00 70.82  ? 89  TRP   B C   1 
ATOM   890  O O   . TRP   B 2 80  ? -17.818 -15.302 -18.938 1.00 70.75  ? 89  TRP   B O   1 
ATOM   891  C CB  . TRP   B 2 80  ? -16.987 -12.554 -20.048 1.00 69.90  ? 89  TRP   B CB  1 
ATOM   892  C CG  . TRP   B 2 80  ? -16.169 -12.918 -21.251 1.00 70.58  ? 89  TRP   B CG  1 
ATOM   893  C CD1 . TRP   B 2 80  ? -16.555 -12.856 -22.560 1.00 71.64  ? 89  TRP   B CD1 1 
ATOM   894  C CD2 . TRP   B 2 80  ? -14.789 -13.307 -21.258 1.00 70.65  ? 89  TRP   B CD2 1 
ATOM   895  N NE1 . TRP   B 2 80  ? -15.515 -13.236 -23.378 1.00 71.95  ? 89  TRP   B NE1 1 
ATOM   896  C CE2 . TRP   B 2 80  ? -14.415 -13.506 -22.604 1.00 71.53  ? 89  TRP   B CE2 1 
ATOM   897  C CE3 . TRP   B 2 80  ? -13.837 -13.520 -20.256 1.00 71.09  ? 89  TRP   B CE3 1 
ATOM   898  C CZ2 . TRP   B 2 80  ? -13.127 -13.897 -22.968 1.00 72.02  ? 89  TRP   B CZ2 1 
ATOM   899  C CZ3 . TRP   B 2 80  ? -12.565 -13.917 -20.620 1.00 71.86  ? 89  TRP   B CZ3 1 
ATOM   900  C CH2 . TRP   B 2 80  ? -12.219 -14.095 -21.960 1.00 72.04  ? 89  TRP   B CH2 1 
ATOM   901  N N   . ASP   B 2 81  ? -18.417 -15.415 -21.108 1.00 71.73  ? 90  ASP   B N   1 
ATOM   902  C CA  . ASP   B 2 81  ? -18.305 -16.869 -21.164 1.00 72.95  ? 90  ASP   B CA  1 
ATOM   903  C C   . ASP   B 2 81  ? -16.871 -17.404 -21.324 1.00 74.12  ? 90  ASP   B C   1 
ATOM   904  O O   . ASP   B 2 81  ? -16.688 -18.620 -21.392 1.00 74.37  ? 90  ASP   B O   1 
ATOM   905  C CB  . ASP   B 2 81  ? -19.222 -17.451 -22.245 1.00 74.08  ? 90  ASP   B CB  1 
ATOM   906  C CG  . ASP   B 2 81  ? -18.931 -16.990 -23.657 1.00 78.00  ? 90  ASP   B CG  1 
ATOM   907  O OD1 . ASP   B 2 81  ? -17.987 -16.192 -23.841 1.00 78.85  ? 90  ASP   B OD1 1 
ATOM   908  O OD2 . ASP   B 2 81  ? -19.652 -17.424 -24.584 1.00 79.50  ? 90  ASP   B OD2 1 
ATOM   909  N N   . GLY   B 2 82  ? -15.886 -16.515 -21.396 1.00 74.49  ? 91  GLY   B N   1 
ATOM   910  C CA  . GLY   B 2 82  ? -14.492 -16.912 -21.532 1.00 75.52  ? 91  GLY   B CA  1 
ATOM   911  C C   . GLY   B 2 82  ? -14.065 -17.301 -22.935 1.00 76.29  ? 91  GLY   B C   1 
ATOM   912  O O   . GLY   B 2 82  ? -12.912 -17.689 -23.145 1.00 76.34  ? 91  GLY   B O   1 
ATOM   913  N N   . LEU   B 2 83  ? -14.979 -17.187 -23.917 1.00 76.50  ? 92  LEU   B N   1 
ATOM   914  C CA  . LEU   B 2 83  ? -14.686 -17.574 -25.289 1.00 76.93  ? 92  LEU   B CA  1 
ATOM   915  C C   . LEU   B 2 83  ? -15.112 -16.548 -26.314 1.00 77.30  ? 92  LEU   B C   1 
ATOM   916  O O   . LEU   B 2 83  ? -14.479 -16.444 -27.362 1.00 77.81  ? 92  LEU   B O   1 
ATOM   917  C CB  . LEU   B 2 83  ? -15.424 -18.874 -25.622 1.00 77.37  ? 92  LEU   B CB  1 
ATOM   918  C CG  . LEU   B 2 83  ? -14.987 -20.149 -24.919 1.00 79.52  ? 92  LEU   B CG  1 
ATOM   919  C CD1 . LEU   B 2 83  ? -15.790 -21.320 -25.432 1.00 80.31  ? 92  LEU   B CD1 1 
ATOM   920  C CD2 . LEU   B 2 83  ? -13.517 -20.429 -25.147 1.00 80.35  ? 92  LEU   B CD2 1 
ATOM   921  N N   . SER   B 2 84  ? -16.238 -15.864 -26.080 1.00 76.94  ? 93  SER   B N   1 
ATOM   922  C CA  . SER   B 2 84  ? -16.797 -14.952 -27.073 1.00 76.77  ? 93  SER   B CA  1 
ATOM   923  C C   . SER   B 2 84  ? -16.220 -13.544 -27.061 1.00 76.95  ? 93  SER   B C   1 
ATOM   924  O O   . SER   B 2 84  ? -15.693 -13.080 -26.045 1.00 77.42  ? 93  SER   B O   1 
ATOM   925  C CB  . SER   B 2 84  ? -18.314 -14.866 -26.921 1.00 77.36  ? 93  SER   B CB  1 
ATOM   926  O OG  . SER   B 2 84  ? -18.923 -16.122 -26.694 1.00 78.73  ? 93  SER   B OG  1 
ATOM   927  N N   . GLU   B 2 85  ? -16.350 -12.853 -28.199 1.00 76.34  ? 94  GLU   B N   1 
ATOM   928  C CA  . GLU   B 2 85  ? -15.972 -11.455 -28.320 1.00 75.75  ? 94  GLU   B CA  1 
ATOM   929  C C   . GLU   B 2 85  ? -17.080 -10.637 -27.656 1.00 74.48  ? 94  GLU   B C   1 
ATOM   930  O O   . GLU   B 2 85  ? -18.255 -11.008 -27.684 1.00 74.69  ? 94  GLU   B O   1 
ATOM   931  C CB  . GLU   B 2 85  ? -15.806 -11.038 -29.802 1.00 77.86  ? 94  GLU   B CB  1 
ATOM   932  C CG  . GLU   B 2 85  ? -14.472 -11.458 -30.403 1.00 82.22  ? 94  GLU   B CG  1 
ATOM   933  C CD  . GLU   B 2 85  ? -14.096 -10.846 -31.740 1.00 86.78  ? 94  GLU   B CD  1 
ATOM   934  O OE1 . GLU   B 2 85  ? -14.910 -10.074 -32.294 1.00 87.04  ? 94  GLU   B OE1 1 
ATOM   935  O OE2 . GLU   B 2 85  ? -12.981 -11.131 -32.231 1.00 88.29  ? 94  GLU   B OE2 1 
ATOM   936  N N   . VAL   B 2 86  ? -16.697 -9.552  -27.013 1.00 73.03  ? 95  VAL   B N   1 
ATOM   937  C CA  . VAL   B 2 86  ? -17.627 -8.663  -26.326 1.00 71.63  ? 95  VAL   B CA  1 
ATOM   938  C C   . VAL   B 2 86  ? -17.649 -7.301  -27.061 1.00 70.71  ? 95  VAL   B C   1 
ATOM   939  O O   . VAL   B 2 86  ? -16.908 -7.097  -28.032 1.00 70.89  ? 95  VAL   B O   1 
ATOM   940  C CB  . VAL   B 2 86  ? -17.211 -8.514  -24.836 1.00 71.76  ? 95  VAL   B CB  1 
ATOM   941  C CG1 . VAL   B 2 86  ? -17.046 -9.875  -24.165 1.00 72.34  ? 95  VAL   B CG1 1 
ATOM   942  C CG2 . VAL   B 2 86  ? -15.937 -7.688  -24.716 1.00 71.91  ? 95  VAL   B CG2 1 
ATOM   943  N N   . GLN   B 2 87  ? -18.524 -6.383  -26.630 1.00 69.61  ? 96  GLN   B N   1 
ATOM   944  C CA  . GLN   B 2 87  ? -18.579 -5.052  -27.202 1.00 68.65  ? 96  GLN   B CA  1 
ATOM   945  C C   . GLN   B 2 87  ? -18.568 -4.023  -26.088 1.00 67.34  ? 96  GLN   B C   1 
ATOM   946  O O   . GLN   B 2 87  ? -19.453 -4.022  -25.247 1.00 67.34  ? 96  GLN   B O   1 
ATOM   947  C CB  . GLN   B 2 87  ? -19.790 -4.875  -28.125 1.00 69.56  ? 96  GLN   B CB  1 
ATOM   948  C CG  . GLN   B 2 87  ? -19.372 -4.723  -29.577 1.00 72.21  ? 96  GLN   B CG  1 
ATOM   949  C CD  . GLN   B 2 87  ? -20.534 -4.747  -30.532 1.00 74.94  ? 96  GLN   B CD  1 
ATOM   950  O OE1 . GLN   B 2 87  ? -21.616 -4.243  -30.242 1.00 75.38  ? 96  GLN   B OE1 1 
ATOM   951  N NE2 . GLN   B 2 87  ? -20.325 -5.340  -31.699 1.00 75.45  ? 96  GLN   B NE2 1 
ATOM   952  N N   . LEU   B 2 88  ? -17.541 -3.181  -26.058 1.00 65.92  ? 97  LEU   B N   1 
ATOM   953  C CA  . LEU   B 2 88  ? -17.457 -2.111  -25.087 1.00 65.01  ? 97  LEU   B CA  1 
ATOM   954  C C   . LEU   B 2 88  ? -18.320 -0.963  -25.628 1.00 64.45  ? 97  LEU   B C   1 
ATOM   955  O O   . LEU   B 2 88  ? -18.013 -0.439  -26.700 1.00 64.81  ? 97  LEU   B O   1 
ATOM   956  C CB  . LEU   B 2 88  ? -15.993 -1.645  -24.950 1.00 64.71  ? 97  LEU   B CB  1 
ATOM   957  C CG  . LEU   B 2 88  ? -15.767 -0.319  -24.217 1.00 65.57  ? 97  LEU   B CG  1 
ATOM   958  C CD1 . LEU   B 2 88  ? -16.137 -0.428  -22.751 1.00 65.72  ? 97  LEU   B CD1 1 
ATOM   959  C CD2 . LEU   B 2 88  ? -14.355 0.186   -24.412 1.00 65.98  ? 97  LEU   B CD2 1 
ATOM   960  N N   . LEU   B 2 89  ? -19.394 -0.578  -24.914 1.00 63.26  ? 98  LEU   B N   1 
ATOM   961  C CA  . LEU   B 2 89  ? -20.190 0.561   -25.337 1.00 62.66  ? 98  LEU   B CA  1 
ATOM   962  C C   . LEU   B 2 89  ? -19.444 1.767   -24.796 1.00 62.48  ? 98  LEU   B C   1 
ATOM   963  O O   . LEU   B 2 89  ? -19.758 2.269   -23.718 1.00 62.49  ? 98  LEU   B O   1 
ATOM   964  C CB  . LEU   B 2 89  ? -21.652 0.491   -24.830 1.00 62.53  ? 98  LEU   B CB  1 
ATOM   965  C CG  . LEU   B 2 89  ? -22.674 1.636   -25.197 1.00 63.52  ? 98  LEU   B CG  1 
ATOM   966  C CD1 . LEU   B 2 89  ? -22.256 2.485   -26.383 1.00 64.20  ? 98  LEU   B CD1 1 
ATOM   967  C CD2 . LEU   B 2 89  ? -24.042 1.085   -25.459 1.00 63.83  ? 98  LEU   B CD2 1 
ATOM   968  N N   . ALA   B 2 90  ? -18.410 2.195   -25.528 1.00 62.16  ? 99  ALA   B N   1 
ATOM   969  C CA  . ALA   B 2 90  ? -17.589 3.307   -25.091 1.00 62.63  ? 99  ALA   B CA  1 
ATOM   970  C C   . ALA   B 2 90  ? -18.292 4.624   -25.256 1.00 63.33  ? 99  ALA   B C   1 
ATOM   971  O O   . ALA   B 2 90  ? -18.593 4.995   -26.376 1.00 63.51  ? 99  ALA   B O   1 
ATOM   972  C CB  . ALA   B 2 90  ? -16.279 3.326   -25.848 1.00 62.45  ? 99  ALA   B CB  1 
ATOM   973  N N   . VAL   B 2 91  ? -18.536 5.340   -24.147 1.00 63.71  ? 100 VAL   B N   1 
ATOM   974  C CA  . VAL   B 2 91  ? -19.144 6.665   -24.172 1.00 64.87  ? 100 VAL   B CA  1 
ATOM   975  C C   . VAL   B 2 91  ? -18.025 7.639   -23.768 1.00 66.43  ? 100 VAL   B C   1 
ATOM   976  O O   . VAL   B 2 91  ? -17.839 7.912   -22.584 1.00 66.70  ? 100 VAL   B O   1 
ATOM   977  C CB  . VAL   B 2 91  ? -20.370 6.759   -23.227 1.00 65.14  ? 100 VAL   B CB  1 
ATOM   978  C CG1 . VAL   B 2 91  ? -21.095 8.092   -23.396 1.00 65.67  ? 100 VAL   B CG1 1 
ATOM   979  C CG2 . VAL   B 2 91  ? -21.327 5.597   -23.455 1.00 65.21  ? 100 VAL   B CG2 1 
ATOM   980  N N   . PRO   B 2 92  ? -17.236 8.141   -24.737 1.00 67.23  ? 101 PRO   B N   1 
ATOM   981  C CA  . PRO   B 2 92  ? -16.093 8.996   -24.384 1.00 68.03  ? 101 PRO   B CA  1 
ATOM   982  C C   . PRO   B 2 92  ? -16.461 10.449  -24.120 1.00 69.30  ? 101 PRO   B C   1 
ATOM   983  O O   . PRO   B 2 92  ? -17.468 10.926  -24.636 1.00 69.70  ? 101 PRO   B O   1 
ATOM   984  C CB  . PRO   B 2 92  ? -15.169 8.871   -25.614 1.00 68.53  ? 101 PRO   B CB  1 
ATOM   985  C CG  . PRO   B 2 92  ? -15.827 7.854   -26.537 1.00 68.64  ? 101 PRO   B CG  1 
ATOM   986  C CD  . PRO   B 2 92  ? -17.275 7.887   -26.186 1.00 66.86  ? 101 PRO   B CD  1 
ATOM   987  N N   . PRO   B 2 93  ? -15.638 11.183  -23.355 1.00 69.75  ? 102 PRO   B N   1 
ATOM   988  C CA  . PRO   B 2 93  ? -15.956 12.597  -23.088 1.00 70.08  ? 102 PRO   B CA  1 
ATOM   989  C C   . PRO   B 2 93  ? -16.088 13.431  -24.357 1.00 71.02  ? 102 PRO   B C   1 
ATOM   990  O O   . PRO   B 2 93  ? -15.198 13.402  -25.208 1.00 71.89  ? 102 PRO   B O   1 
ATOM   991  C CB  . PRO   B 2 93  ? -14.772 13.065  -22.241 1.00 70.61  ? 102 PRO   B CB  1 
ATOM   992  C CG  . PRO   B 2 93  ? -14.247 11.811  -21.597 1.00 71.00  ? 102 PRO   B CG  1 
ATOM   993  C CD  . PRO   B 2 93  ? -14.414 10.757  -22.650 1.00 69.35  ? 102 PRO   B CD  1 
ATOM   994  N N   . GLY   B 2 94  ? -17.220 14.118  -24.508 1.00 70.75  ? 103 GLY   B N   1 
ATOM   995  C CA  . GLY   B 2 94  ? -17.501 14.977  -25.662 1.00 70.67  ? 103 GLY   B CA  1 
ATOM   996  C C   . GLY   B 2 94  ? -17.830 14.264  -26.964 1.00 70.57  ? 103 GLY   B C   1 
ATOM   997  O O   . GLY   B 2 94  ? -18.286 14.881  -27.929 1.00 70.39  ? 103 GLY   B O   1 
ATOM   998  N N   . GLU   B 2 95  ? -17.560 12.965  -27.016 1.00 70.64  ? 104 GLU   B N   1 
ATOM   999  C CA  . GLU   B 2 95  ? -17.789 12.154  -28.204 1.00 71.13  ? 104 GLU   B CA  1 
ATOM   1000 C C   . GLU   B 2 95  ? -19.057 11.311  -28.042 1.00 71.21  ? 104 GLU   B C   1 
ATOM   1001 O O   . GLU   B 2 95  ? -19.515 11.089  -26.924 1.00 71.17  ? 104 GLU   B O   1 
ATOM   1002 C CB  . GLU   B 2 95  ? -16.553 11.273  -28.485 1.00 73.37  ? 104 GLU   B CB  1 
ATOM   1003 C CG  . GLU   B 2 95  ? -15.260 12.076  -28.516 1.00 78.45  ? 104 GLU   B CG  1 
ATOM   1004 C CD  . GLU   B 2 95  ? -14.000 11.284  -28.800 1.00 85.86  ? 104 GLU   B CD  1 
ATOM   1005 O OE1 . GLU   B 2 95  ? -14.058 10.034  -28.736 1.00 87.55  ? 104 GLU   B OE1 1 
ATOM   1006 O OE2 . GLU   B 2 95  ? -12.956 11.910  -29.097 1.00 87.99  ? 104 GLU   B OE2 1 
ATOM   1007 N N   . ARG   B 2 96  ? -19.625 10.857  -29.153 1.00 71.15  ? 105 ARG   B N   1 
ATOM   1008 C CA  . ARG   B 2 96  ? -20.842 10.053  -29.173 1.00 71.93  ? 105 ARG   B CA  1 
ATOM   1009 C C   . ARG   B 2 96  ? -20.593 8.616   -28.680 1.00 72.76  ? 105 ARG   B C   1 
ATOM   1010 O O   . ARG   B 2 96  ? -19.467 8.123   -28.786 1.00 73.28  ? 105 ARG   B O   1 
ATOM   1011 C CB  . ARG   B 2 96  ? -21.358 10.039  -30.612 1.00 73.56  ? 105 ARG   B CB  1 
ATOM   1012 C CG  . ARG   B 2 96  ? -22.759 9.503   -30.821 1.00 76.83  ? 105 ARG   B CG  1 
ATOM   1013 C CD  . ARG   B 2 96  ? -23.458 10.229  -31.957 1.00 80.21  ? 105 ARG   B CD  1 
ATOM   1014 N NE  . ARG   B 2 96  ? -22.686 10.227  -33.200 1.00 83.55  ? 105 ARG   B NE  1 
ATOM   1015 C CZ  . ARG   B 2 96  ? -22.378 11.319  -33.897 1.00 86.49  ? 105 ARG   B CZ  1 
ATOM   1016 N NH1 . ARG   B 2 96  ? -22.779 12.517  -33.483 1.00 86.46  ? 105 ARG   B NH1 1 
ATOM   1017 N NH2 . ARG   B 2 96  ? -21.672 11.221  -35.016 1.00 86.18  ? 105 ARG   B NH2 1 
ATOM   1018 N N   . ALA   B 2 97  ? -21.637 7.942   -28.135 1.00 72.62  ? 106 ALA   B N   1 
ATOM   1019 C CA  . ALA   B 2 97  ? -21.547 6.547   -27.688 1.00 72.84  ? 106 ALA   B CA  1 
ATOM   1020 C C   . ALA   B 2 97  ? -21.197 5.665   -28.895 1.00 73.70  ? 106 ALA   B C   1 
ATOM   1021 O O   . ALA   B 2 97  ? -21.694 5.905   -30.004 1.00 73.84  ? 106 ALA   B O   1 
ATOM   1022 C CB  . ALA   B 2 97  ? -22.865 6.104   -27.084 1.00 72.64  ? 106 ALA   B CB  1 
ATOM   1023 N N   . LYS   B 2 98  ? -20.317 4.678   -28.696 1.00 74.02  ? 107 LYS   B N   1 
ATOM   1024 C CA  . LYS   B 2 98  ? -19.830 3.873   -29.807 1.00 74.79  ? 107 LYS   B CA  1 
ATOM   1025 C C   . LYS   B 2 98  ? -19.433 2.461   -29.383 1.00 74.11  ? 107 LYS   B C   1 
ATOM   1026 O O   . LYS   B 2 98  ? -18.612 2.303   -28.493 1.00 74.46  ? 107 LYS   B O   1 
ATOM   1027 C CB  . LYS   B 2 98  ? -18.667 4.661   -30.434 1.00 78.20  ? 107 LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 2 98  ? -17.644 3.917   -31.258 1.00 84.12  ? 107 LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 2 98  ? -16.366 4.774   -31.358 1.00 89.91  ? 107 LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 2 98  ? -15.759 5.047   -29.990 1.00 93.93  ? 107 LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 2 98  ? -14.503 5.840   -30.069 1.00 96.55  ? 107 LYS   B NZ  1 
ATOM   1032 N N   . ASN   B 2 99  ? -20.038 1.438   -30.002 1.00 73.34  ? 108 ASN   B N   1 
ATOM   1033 C CA  . ASN   B 2 99  ? -19.772 0.034   -29.681 1.00 73.18  ? 108 ASN   B CA  1 
ATOM   1034 C C   . ASN   B 2 99  ? -18.472 -0.437  -30.318 1.00 73.25  ? 108 ASN   B C   1 
ATOM   1035 O O   . ASN   B 2 99  ? -18.380 -0.478  -31.537 1.00 73.76  ? 108 ASN   B O   1 
ATOM   1036 C CB  . ASN   B 2 99  ? -20.903 -0.869  -30.199 1.00 73.88  ? 108 ASN   B CB  1 
ATOM   1037 C CG  . ASN   B 2 99  ? -22.234 -0.741  -29.499 1.00 76.32  ? 108 ASN   B CG  1 
ATOM   1038 O OD1 . ASN   B 2 99  ? -22.792 0.349   -29.348 1.00 77.88  ? 108 ASN   B OD1 1 
ATOM   1039 N ND2 . ASN   B 2 99  ? -22.801 -1.867  -29.097 1.00 75.95  ? 108 ASN   B ND2 1 
ATOM   1040 N N   . ILE   B 2 100 ? -17.491 -0.838  -29.515 1.00 72.75  ? 109 ILE   B N   1 
ATOM   1041 C CA  . ILE   B 2 100 ? -16.227 -1.354  -30.035 1.00 72.78  ? 109 ILE   B CA  1 
ATOM   1042 C C   . ILE   B 2 100 ? -16.134 -2.854  -29.746 1.00 72.56  ? 109 ILE   B C   1 
ATOM   1043 O O   . ILE   B 2 100 ? -16.106 -3.244  -28.583 1.00 72.41  ? 109 ILE   B O   1 
ATOM   1044 C CB  . ILE   B 2 100 ? -15.040 -0.624  -29.383 1.00 73.33  ? 109 ILE   B CB  1 
ATOM   1045 C CG1 . ILE   B 2 100 ? -15.191 0.900   -29.464 1.00 74.10  ? 109 ILE   B CG1 1 
ATOM   1046 C CG2 . ILE   B 2 100 ? -13.714 -1.122  -29.960 1.00 73.76  ? 109 ILE   B CG2 1 
ATOM   1047 C CD1 . ILE   B 2 100 ? -15.008 1.470   -30.807 1.00 75.19  ? 109 ILE   B CD1 1 
ATOM   1048 N N   . GLN   B 2 101 ? -16.063 -3.689  -30.782 1.00 72.40  ? 110 GLN   B N   1 
ATOM   1049 C CA  . GLN   B 2 101 ? -15.968 -5.138  -30.595 1.00 72.81  ? 110 GLN   B CA  1 
ATOM   1050 C C   . GLN   B 2 101 ? -14.520 -5.588  -30.350 1.00 72.79  ? 110 GLN   B C   1 
ATOM   1051 O O   . GLN   B 2 101 ? -13.605 -5.106  -31.014 1.00 72.85  ? 110 GLN   B O   1 
ATOM   1052 C CB  . GLN   B 2 101 ? -16.566 -5.870  -31.805 1.00 74.35  ? 110 GLN   B CB  1 
ATOM   1053 C CG  . GLN   B 2 101 ? -16.695 -7.376  -31.617 1.00 77.55  ? 110 GLN   B CG  1 
ATOM   1054 C CD  . GLN   B 2 101 ? -17.631 -7.958  -32.641 1.00 81.98  ? 110 GLN   B CD  1 
ATOM   1055 O OE1 . GLN   B 2 101 ? -18.711 -7.418  -32.914 1.00 83.89  ? 110 GLN   B OE1 1 
ATOM   1056 N NE2 . GLN   B 2 101 ? -17.233 -9.062  -33.242 1.00 82.16  ? 110 GLN   B NE2 1 
ATOM   1057 N N   . THR   B 2 102 ? -14.307 -6.507  -29.398 1.00 72.52  ? 111 THR   B N   1 
ATOM   1058 C CA  . THR   B 2 102 ? -12.966 -7.008  -29.080 1.00 72.82  ? 111 THR   B CA  1 
ATOM   1059 C C   . THR   B 2 102 ? -13.033 -8.390  -28.447 1.00 72.86  ? 111 THR   B C   1 
ATOM   1060 O O   . THR   B 2 102 ? -14.092 -8.776  -27.955 1.00 73.08  ? 111 THR   B O   1 
ATOM   1061 C CB  . THR   B 2 102 ? -12.272 -6.041  -28.080 1.00 74.54  ? 111 THR   B CB  1 
ATOM   1062 O OG1 . THR   B 2 102 ? -10.877 -6.339  -28.003 1.00 75.84  ? 111 THR   B OG1 1 
ATOM   1063 C CG2 . THR   B 2 102 ? -12.898 -6.071  -26.692 1.00 74.82  ? 111 THR   B CG2 1 
ATOM   1064 N N   . LEU   B 2 103 ? -11.904 -9.138  -28.430 1.00 72.50  ? 112 LEU   B N   1 
ATOM   1065 C CA  . LEU   B 2 103 ? -11.860 -10.393 -27.685 1.00 72.40  ? 112 LEU   B CA  1 
ATOM   1066 C C   . LEU   B 2 103 ? -11.062 -10.108 -26.415 1.00 72.73  ? 112 LEU   B C   1 
ATOM   1067 O O   . LEU   B 2 103 ? -9.912  -9.658  -26.480 1.00 72.92  ? 112 LEU   B O   1 
ATOM   1068 C CB  . LEU   B 2 103 ? -11.232 -11.574 -28.422 1.00 72.09  ? 112 LEU   B CB  1 
ATOM   1069 C CG  . LEU   B 2 103 ? -11.333 -12.860 -27.596 1.00 73.00  ? 112 LEU   B CG  1 
ATOM   1070 C CD1 . LEU   B 2 103 ? -12.655 -13.526 -27.802 1.00 73.42  ? 112 LEU   B CD1 1 
ATOM   1071 C CD2 . LEU   B 2 103 ? -10.191 -13.800 -27.847 1.00 73.61  ? 112 LEU   B CD2 1 
ATOM   1072 N N   . PRO   B 2 104 ? -11.652 -10.370 -25.249 1.00 72.39  ? 113 PRO   B N   1 
ATOM   1073 C CA  . PRO   B 2 104 ? -10.958 -10.048 -24.009 1.00 72.31  ? 113 PRO   B CA  1 
ATOM   1074 C C   . PRO   B 2 104 ? -9.851  -11.013 -23.619 1.00 72.61  ? 113 PRO   B C   1 
ATOM   1075 O O   . PRO   B 2 104 ? -9.919  -12.221 -23.858 1.00 72.73  ? 113 PRO   B O   1 
ATOM   1076 C CB  . PRO   B 2 104 ? -12.080 -10.007 -22.963 1.00 72.96  ? 113 PRO   B CB  1 
ATOM   1077 C CG  . PRO   B 2 104 ? -13.363 -10.154 -23.725 1.00 73.50  ? 113 PRO   B CG  1 
ATOM   1078 C CD  . PRO   B 2 104 ? -13.017 -10.854 -24.993 1.00 71.92  ? 113 PRO   B CD  1 
ATOM   1079 N N   . GLY   B 2 105 ? -8.841  -10.443 -22.979 1.00 72.17  ? 114 GLY   B N   1 
ATOM   1080 C CA  . GLY   B 2 105 ? -7.735  -11.172 -22.394 1.00 71.85  ? 114 GLY   B CA  1 
ATOM   1081 C C   . GLY   B 2 105 ? -8.110  -11.668 -21.010 1.00 71.14  ? 114 GLY   B C   1 
ATOM   1082 O O   . GLY   B 2 105 ? -9.295  -11.800 -20.688 1.00 71.42  ? 114 GLY   B O   1 
ATOM   1083 N N   . ILE   B 2 106 ? -7.115  -11.949 -20.180 1.00 70.21  ? 115 ILE   B N   1 
ATOM   1084 C CA  . ILE   B 2 106 ? -7.345  -12.512 -18.856 1.00 70.26  ? 115 ILE   B CA  1 
ATOM   1085 C C   . ILE   B 2 106 ? -6.435  -11.850 -17.832 1.00 70.30  ? 115 ILE   B C   1 
ATOM   1086 O O   . ILE   B 2 106 ? -5.239  -11.723 -18.070 1.00 70.64  ? 115 ILE   B O   1 
ATOM   1087 C CB  . ILE   B 2 106 ? -7.025  -14.044 -18.934 1.00 70.91  ? 115 ILE   B CB  1 
ATOM   1088 C CG1 . ILE   B 2 106 ? -8.046  -14.821 -19.776 1.00 72.37  ? 115 ILE   B CG1 1 
ATOM   1089 C CG2 . ILE   B 2 106 ? -6.836  -14.692 -17.579 1.00 71.25  ? 115 ILE   B CG2 1 
ATOM   1090 C CD1 . ILE   B 2 106 ? -9.365  -14.889 -19.206 1.00 74.12  ? 115 ILE   B CD1 1 
ATOM   1091 N N   . PHE   B 2 107 ? -6.985  -11.497 -16.672 1.00 69.72  ? 116 PHE   B N   1 
ATOM   1092 C CA  . PHE   B 2 107 ? -6.241  -11.009 -15.527 1.00 69.64  ? 116 PHE   B CA  1 
ATOM   1093 C C   . PHE   B 2 107 ? -6.147  -12.234 -14.634 1.00 70.28  ? 116 PHE   B C   1 
ATOM   1094 O O   . PHE   B 2 107 ? -7.182  -12.683 -14.153 1.00 70.49  ? 116 PHE   B O   1 
ATOM   1095 C CB  . PHE   B 2 107 ? -7.074  -9.964  -14.769 1.00 69.26  ? 116 PHE   B CB  1 
ATOM   1096 C CG  . PHE   B 2 107 ? -6.876  -8.516  -15.141 1.00 69.37  ? 116 PHE   B CG  1 
ATOM   1097 C CD1 . PHE   B 2 107 ? -6.152  -8.163  -16.266 1.00 70.04  ? 116 PHE   B CD1 1 
ATOM   1098 C CD2 . PHE   B 2 107 ? -7.413  -7.508  -14.363 1.00 69.62  ? 116 PHE   B CD2 1 
ATOM   1099 C CE1 . PHE   B 2 107 ? -5.981  -6.829  -16.606 1.00 70.55  ? 116 PHE   B CE1 1 
ATOM   1100 C CE2 . PHE   B 2 107 ? -7.223  -6.176  -14.699 1.00 70.14  ? 116 PHE   B CE2 1 
ATOM   1101 C CZ  . PHE   B 2 107 ? -6.520  -5.845  -15.821 1.00 70.09  ? 116 PHE   B CZ  1 
ATOM   1102 N N   . LYS   B 2 108 ? -4.954  -12.809 -14.435 1.00 70.56  ? 117 LYS   B N   1 
ATOM   1103 C CA  . LYS   B 2 108 ? -4.807  -13.975 -13.562 1.00 71.30  ? 117 LYS   B CA  1 
ATOM   1104 C C   . LYS   B 2 108 ? -4.435  -13.454 -12.194 1.00 71.29  ? 117 LYS   B C   1 
ATOM   1105 O O   . LYS   B 2 108 ? -3.450  -12.732 -12.084 1.00 71.28  ? 117 LYS   B O   1 
ATOM   1106 C CB  . LYS   B 2 108 ? -3.720  -14.939 -14.087 1.00 74.12  ? 117 LYS   B CB  1 
ATOM   1107 C CG  . LYS   B 2 108 ? -4.113  -15.648 -15.387 1.00 79.94  ? 117 LYS   B CG  1 
ATOM   1108 C CD  . LYS   B 2 108 ? -2.996  -16.516 -16.000 1.00 86.17  ? 117 LYS   B CD  1 
ATOM   1109 C CE  . LYS   B 2 108 ? -3.499  -17.325 -17.189 1.00 91.48  ? 117 LYS   B CE  1 
ATOM   1110 N NZ  . LYS   B 2 108 ? -2.404  -17.784 -18.104 1.00 94.06  ? 117 LYS   B NZ  1 
ATOM   1111 N N   . THR   B 2 109 ? -5.257  -13.744 -11.161 1.00 71.28  ? 118 THR   B N   1 
ATOM   1112 C CA  . THR   B 2 109 ? -5.021  -13.286 -9.779  1.00 71.59  ? 118 THR   B CA  1 
ATOM   1113 C C   . THR   B 2 109 ? -4.930  -14.475 -8.789  1.00 71.63  ? 118 THR   B C   1 
ATOM   1114 O O   . THR   B 2 109 ? -5.239  -15.609 -9.156  1.00 72.01  ? 118 THR   B O   1 
ATOM   1115 C CB  . THR   B 2 109 ? -6.079  -12.214 -9.330  1.00 72.99  ? 118 THR   B CB  1 
ATOM   1116 O OG1 . THR   B 2 109 ? -7.280  -12.832 -8.859  1.00 73.97  ? 118 THR   B OG1 1 
ATOM   1117 C CG2 . THR   B 2 109 ? -6.397  -11.190 -10.404 1.00 73.45  ? 118 THR   B CG2 1 
ATOM   1118 N N   . LYS   B 2 110 ? -4.524  -14.217 -7.535  1.00 71.09  ? 119 LYS   B N   1 
ATOM   1119 C CA  . LYS   B 2 110 ? -4.476  -15.250 -6.499  1.00 71.16  ? 119 LYS   B CA  1 
ATOM   1120 C C   . LYS   B 2 110 ? -5.890  -15.761 -6.101  1.00 71.49  ? 119 LYS   B C   1 
ATOM   1121 O O   . LYS   B 2 110 ? -6.003  -16.762 -5.392  1.00 71.65  ? 119 LYS   B O   1 
ATOM   1122 C CB  . LYS   B 2 110 ? -3.702  -14.746 -5.262  1.00 72.19  ? 119 LYS   B CB  1 
ATOM   1123 C CG  . LYS   B 2 110 ? -4.501  -13.827 -4.344  1.00 75.50  ? 119 LYS   B CG  1 
ATOM   1124 C CD  . LYS   B 2 110 ? -3.596  -13.013 -3.434  1.00 79.62  ? 119 LYS   B CD  1 
ATOM   1125 C CE  . LYS   B 2 110 ? -4.212  -12.702 -2.084  1.00 83.03  ? 119 LYS   B CE  1 
ATOM   1126 N NZ  . LYS   B 2 110 ? -5.470  -11.916 -2.192  1.00 84.66  ? 119 LYS   B NZ  1 
ATOM   1127 N N   . ASP   B 2 111 ? -6.954  -15.063 -6.537  1.00 71.23  ? 120 ASP   B N   1 
ATOM   1128 C CA  . ASP   B 2 111 ? -8.329  -15.438 -6.245  1.00 71.64  ? 120 ASP   B CA  1 
ATOM   1129 C C   . ASP   B 2 111 ? -9.121  -15.865 -7.493  1.00 72.32  ? 120 ASP   B C   1 
ATOM   1130 O O   . ASP   B 2 111 ? -10.345 -15.959 -7.430  1.00 73.16  ? 120 ASP   B O   1 
ATOM   1131 C CB  . ASP   B 2 111 ? -9.045  -14.280 -5.545  1.00 73.06  ? 120 ASP   B CB  1 
ATOM   1132 C CG  . ASP   B 2 111 ? -8.533  -14.003 -4.147  1.00 76.41  ? 120 ASP   B CG  1 
ATOM   1133 O OD1 . ASP   B 2 111 ? -8.192  -14.971 -3.441  1.00 76.76  ? 120 ASP   B OD1 1 
ATOM   1134 O OD2 . ASP   B 2 111 ? -8.493  -12.814 -3.755  1.00 78.02  ? 120 ASP   B OD2 1 
ATOM   1135 N N   . GLY   B 2 112 ? -8.443  -16.113 -8.607  1.00 71.80  ? 121 GLY   B N   1 
ATOM   1136 C CA  . GLY   B 2 112 ? -9.105  -16.535 -9.829  1.00 71.70  ? 121 GLY   B CA  1 
ATOM   1137 C C   . GLY   B 2 112 ? -8.925  -15.576 -10.979 1.00 71.39  ? 121 GLY   B C   1 
ATOM   1138 O O   . GLY   B 2 112 ? -8.470  -14.447 -10.787 1.00 71.48  ? 121 GLY   B O   1 
ATOM   1139 N N   . ASP   B 2 113 ? -9.306  -16.022 -12.184 1.00 70.80  ? 122 ASP   B N   1 
ATOM   1140 C CA  . ASP   B 2 113 ? -9.183  -15.240 -13.406 1.00 71.03  ? 122 ASP   B CA  1 
ATOM   1141 C C   . ASP   B 2 113 ? -10.384 -14.334 -13.712 1.00 70.82  ? 122 ASP   B C   1 
ATOM   1142 O O   . ASP   B 2 113 ? -11.540 -14.699 -13.488 1.00 70.86  ? 122 ASP   B O   1 
ATOM   1143 C CB  . ASP   B 2 113 ? -8.885  -16.162 -14.595 1.00 72.80  ? 122 ASP   B CB  1 
ATOM   1144 C CG  . ASP   B 2 113 ? -7.591  -16.940 -14.485 1.00 78.20  ? 122 ASP   B CG  1 
ATOM   1145 O OD1 . ASP   B 2 113 ? -6.906  -16.824 -13.434 1.00 79.74  ? 122 ASP   B OD1 1 
ATOM   1146 O OD2 . ASP   B 2 113 ? -7.257  -17.667 -15.443 1.00 80.38  ? 122 ASP   B OD2 1 
ATOM   1147 N N   . ILE   B 2 114 ? -10.092 -13.141 -14.230 1.00 70.34  ? 123 ILE   B N   1 
ATOM   1148 C CA  . ILE   B 2 114 ? -11.093 -12.128 -14.576 1.00 70.31  ? 123 ILE   B CA  1 
ATOM   1149 C C   . ILE   B 2 114 ? -10.900 -11.742 -16.038 1.00 70.05  ? 123 ILE   B C   1 
ATOM   1150 O O   . ILE   B 2 114 ? -9.770  -11.746 -16.521 1.00 70.12  ? 123 ILE   B O   1 
ATOM   1151 C CB  . ILE   B 2 114 ? -10.933 -10.866 -13.675 1.00 70.58  ? 123 ILE   B CB  1 
ATOM   1152 C CG1 . ILE   B 2 114 ? -10.804 -11.232 -12.187 1.00 71.78  ? 123 ILE   B CG1 1 
ATOM   1153 C CG2 . ILE   B 2 114 ? -12.052 -9.860  -13.901 1.00 70.75  ? 123 ILE   B CG2 1 
ATOM   1154 C CD1 . ILE   B 2 114 ? -10.271 -10.127 -11.332 1.00 73.31  ? 123 ILE   B CD1 1 
ATOM   1155 N N   . GLY   B 2 115 ? -11.988 -11.406 -16.729 1.00 69.26  ? 124 GLY   B N   1 
ATOM   1156 C CA  . GLY   B 2 115 ? -11.899 -10.948 -18.109 1.00 68.88  ? 124 GLY   B CA  1 
ATOM   1157 C C   . GLY   B 2 115 ? -11.222 -9.593  -18.171 1.00 68.55  ? 124 GLY   B C   1 
ATOM   1158 O O   . GLY   B 2 115 ? -11.189 -8.868  -17.170 1.00 68.57  ? 124 GLY   B O   1 
ATOM   1159 N N   . ALA   B 2 116 ? -10.652 -9.241  -19.326 1.00 68.24  ? 125 ALA   B N   1 
ATOM   1160 C CA  . ALA   B 2 116 ? -9.998  -7.944  -19.466 1.00 68.69  ? 125 ALA   B CA  1 
ATOM   1161 C C   . ALA   B 2 116 ? -10.059 -7.400  -20.879 1.00 69.52  ? 125 ALA   B C   1 
ATOM   1162 O O   . ALA   B 2 116 ? -9.569  -8.038  -21.797 1.00 69.98  ? 125 ALA   B O   1 
ATOM   1163 C CB  . ALA   B 2 116 ? -8.559  -8.016  -18.987 1.00 68.53  ? 125 ALA   B CB  1 
ATOM   1164 N N   . VAL   B 2 117 ? -10.652 -6.222  -21.060 1.00 69.61  ? 126 VAL   B N   1 
ATOM   1165 C CA  A VAL   B 2 117 ? -10.728 -5.603  -22.381 0.50 70.29  ? 126 VAL   B CA  1 
ATOM   1166 C CA  B VAL   B 2 117 ? -10.750 -5.603  -22.370 0.50 70.25  ? 126 VAL   B CA  1 
ATOM   1167 C C   . VAL   B 2 117 ? -9.520  -4.709  -22.614 1.00 71.02  ? 126 VAL   B C   1 
ATOM   1168 O O   . VAL   B 2 117 ? -9.263  -3.787  -21.834 1.00 71.55  ? 126 VAL   B O   1 
ATOM   1169 C CB  A VAL   B 2 117 ? -12.062 -4.884  -22.666 0.50 70.85  ? 126 VAL   B CB  1 
ATOM   1170 C CB  B VAL   B 2 117 ? -12.103 -4.873  -22.497 0.50 70.75  ? 126 VAL   B CB  1 
ATOM   1171 C CG1 A VAL   B 2 117 ? -13.147 -5.888  -23.026 0.50 71.40  ? 126 VAL   B CG1 1 
ATOM   1172 C CG1 B VAL   B 2 117 ? -12.073 -3.808  -23.572 0.50 71.22  ? 126 VAL   B CG1 1 
ATOM   1173 C CG2 A VAL   B 2 117 ? -12.489 -4.022  -21.486 0.50 71.38  ? 126 VAL   B CG2 1 
ATOM   1174 C CG2 B VAL   B 2 117 ? -13.224 -5.868  -22.759 0.50 71.25  ? 126 VAL   B CG2 1 
ATOM   1175 N N   . ALA   B 2 118 ? -8.737  -5.013  -23.665 1.00 70.99  ? 127 ALA   B N   1 
ATOM   1176 C CA  . ALA   B 2 118 ? -7.542  -4.237  -23.956 1.00 71.58  ? 127 ALA   B CA  1 
ATOM   1177 C C   . ALA   B 2 118 ? -7.839  -3.125  -24.944 1.00 72.40  ? 127 ALA   B C   1 
ATOM   1178 O O   . ALA   B 2 118 ? -7.498  -3.217  -26.122 1.00 72.82  ? 127 ALA   B O   1 
ATOM   1179 C CB  . ALA   B 2 118 ? -6.439  -5.138  -24.467 1.00 71.56  ? 127 ALA   B CB  1 
ATOM   1180 N N   . LEU   B 2 119 ? -8.521  -2.078  -24.461 1.00 72.28  ? 128 LEU   B N   1 
ATOM   1181 C CA  . LEU   B 2 119 ? -8.889  -0.912  -25.251 1.00 72.35  ? 128 LEU   B CA  1 
ATOM   1182 C C   . LEU   B 2 119 ? -8.512  0.327   -24.443 1.00 73.02  ? 128 LEU   B C   1 
ATOM   1183 O O   . LEU   B 2 119 ? -8.852  0.395   -23.260 1.00 73.16  ? 128 LEU   B O   1 
ATOM   1184 C CB  . LEU   B 2 119 ? -10.399 -0.923  -25.536 1.00 72.13  ? 128 LEU   B CB  1 
ATOM   1185 C CG  . LEU   B 2 119 ? -10.896 -2.032  -26.459 1.00 73.31  ? 128 LEU   B CG  1 
ATOM   1186 C CD1 . LEU   B 2 119 ? -12.407 -2.026  -26.556 1.00 73.66  ? 128 LEU   B CD1 1 
ATOM   1187 C CD2 . LEU   B 2 119 ? -10.282 -1.920  -27.838 1.00 73.87  ? 128 LEU   B CD2 1 
ATOM   1188 N N   . ASP   B 2 120 ? -7.787  1.291   -25.047 1.00 73.34  ? 129 ASP   B N   1 
ATOM   1189 C CA  . ASP   B 2 120 ? -7.395  2.489   -24.307 1.00 74.23  ? 129 ASP   B CA  1 
ATOM   1190 C C   . ASP   B 2 120 ? -8.358  3.636   -24.518 1.00 73.92  ? 129 ASP   B C   1 
ATOM   1191 O O   . ASP   B 2 120 ? -8.640  4.007   -25.644 1.00 74.24  ? 129 ASP   B O   1 
ATOM   1192 C CB  . ASP   B 2 120 ? -5.953  2.915   -24.592 1.00 77.45  ? 129 ASP   B CB  1 
ATOM   1193 C CG  . ASP   B 2 120 ? -5.332  3.755   -23.481 1.00 85.74  ? 129 ASP   B CG  1 
ATOM   1194 O OD1 . ASP   B 2 120 ? -6.095  4.308   -22.643 1.00 87.48  ? 129 ASP   B OD1 1 
ATOM   1195 O OD2 . ASP   B 2 120 ? -4.086  3.840   -23.429 1.00 89.05  ? 129 ASP   B OD2 1 
ATOM   1196 N N   . TYR   B 2 121 ? -8.851  4.199   -23.416 1.00 73.43  ? 130 TYR   B N   1 
ATOM   1197 C CA  . TYR   B 2 121 ? -9.811  5.297   -23.396 1.00 73.19  ? 130 TYR   B CA  1 
ATOM   1198 C C   . TYR   B 2 121 ? -9.499  6.258   -22.246 1.00 72.48  ? 130 TYR   B C   1 
ATOM   1199 O O   . TYR   B 2 121 ? -8.855  5.864   -21.266 1.00 72.46  ? 130 TYR   B O   1 
ATOM   1200 C CB  . TYR   B 2 121 ? -11.229 4.733   -23.233 1.00 73.40  ? 130 TYR   B CB  1 
ATOM   1201 C CG  . TYR   B 2 121 ? -11.831 4.337   -24.554 1.00 74.31  ? 130 TYR   B CG  1 
ATOM   1202 C CD1 . TYR   B 2 121 ? -12.380 5.288   -25.401 1.00 75.41  ? 130 TYR   B CD1 1 
ATOM   1203 C CD2 . TYR   B 2 121 ? -11.807 3.018   -24.984 1.00 75.29  ? 130 TYR   B CD2 1 
ATOM   1204 C CE1 . TYR   B 2 121 ? -12.913 4.934   -26.632 1.00 76.40  ? 130 TYR   B CE1 1 
ATOM   1205 C CE2 . TYR   B 2 121 ? -12.319 2.655   -26.221 1.00 76.44  ? 130 TYR   B CE2 1 
ATOM   1206 C CZ  . TYR   B 2 121 ? -12.865 3.619   -27.047 1.00 77.52  ? 130 TYR   B CZ  1 
ATOM   1207 O OH  . TYR   B 2 121 ? -13.384 3.272   -28.266 1.00 79.52  ? 130 TYR   B OH  1 
ATOM   1208 N N   . PRO   B 2 122 ? -9.941  7.530   -22.342 1.00 71.46  ? 131 PRO   B N   1 
ATOM   1209 C CA  . PRO   B 2 122 ? -9.675  8.473   -21.242 1.00 70.49  ? 131 PRO   B CA  1 
ATOM   1210 C C   . PRO   B 2 122 ? -10.323 8.031   -19.939 1.00 69.23  ? 131 PRO   B C   1 
ATOM   1211 O O   . PRO   B 2 122 ? -11.292 7.272   -19.961 1.00 69.56  ? 131 PRO   B O   1 
ATOM   1212 C CB  . PRO   B 2 122 ? -10.299 9.794   -21.726 1.00 71.27  ? 131 PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 2 122 ? -10.577 9.617   -23.164 1.00 71.94  ? 131 PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 2 122 ? -10.721 8.157   -23.428 1.00 70.78  ? 131 PRO   B CD  1 
ATOM   1215 N N   . ALA   B 2 123 ? -9.819  8.531   -18.805 1.00 67.72  ? 132 ALA   B N   1 
ATOM   1216 C CA  . ALA   B 2 123 ? -10.391 8.188   -17.501 1.00 66.75  ? 132 ALA   B CA  1 
ATOM   1217 C C   . ALA   B 2 123 ? -11.885 8.548   -17.396 1.00 65.48  ? 132 ALA   B C   1 
ATOM   1218 O O   . ALA   B 2 123 ? -12.617 7.860   -16.693 1.00 65.89  ? 132 ALA   B O   1 
ATOM   1219 C CB  . ALA   B 2 123 ? -9.604  8.851   -16.386 1.00 66.79  ? 132 ALA   B CB  1 
ATOM   1220 N N   . GLY   B 2 124 ? -12.333 9.555   -18.150 1.00 63.72  ? 133 GLY   B N   1 
ATOM   1221 C CA  . GLY   B 2 124 ? -13.733 9.963   -18.187 1.00 62.57  ? 133 GLY   B CA  1 
ATOM   1222 C C   . GLY   B 2 124 ? -14.672 8.947   -18.821 1.00 61.30  ? 133 GLY   B C   1 
ATOM   1223 O O   . GLY   B 2 124 ? -15.889 9.085   -18.716 1.00 61.10  ? 133 GLY   B O   1 
ATOM   1224 N N   . THR   B 2 125 ? -14.125 7.909   -19.486 1.00 60.42  ? 134 THR   B N   1 
ATOM   1225 C CA  . THR   B 2 125 ? -14.929 6.834   -20.083 1.00 59.89  ? 134 THR   B CA  1 
ATOM   1226 C C   . THR   B 2 125 ? -15.376 5.797   -19.019 1.00 59.48  ? 134 THR   B C   1 
ATOM   1227 O O   . THR   B 2 125 ? -16.299 5.033   -19.288 1.00 59.82  ? 134 THR   B O   1 
ATOM   1228 C CB  . THR   B 2 125 ? -14.182 6.193   -21.282 1.00 61.01  ? 134 THR   B CB  1 
ATOM   1229 O OG1 . THR   B 2 125 ? -13.671 7.220   -22.136 1.00 62.10  ? 134 THR   B OG1 1 
ATOM   1230 C CG2 . THR   B 2 125 ? -15.064 5.251   -22.110 1.00 60.95  ? 134 THR   B CG2 1 
ATOM   1231 N N   . SER   B 2 126 ? -14.745 5.794   -17.807 1.00 58.71  ? 135 SER   B N   1 
ATOM   1232 C CA  . SER   B 2 126 ? -15.012 4.876   -16.682 1.00 58.42  ? 135 SER   B CA  1 
ATOM   1233 C C   . SER   B 2 126 ? -16.489 4.651   -16.350 1.00 57.59  ? 135 SER   B C   1 
ATOM   1234 O O   . SER   B 2 126 ? -17.187 5.593   -16.042 1.00 58.11  ? 135 SER   B O   1 
ATOM   1235 C CB  . SER   B 2 126 ? -14.297 5.350   -15.421 1.00 59.60  ? 135 SER   B CB  1 
ATOM   1236 O OG  . SER   B 2 126 ? -12.898 5.445   -15.613 1.00 61.44  ? 135 SER   B OG  1 
ATOM   1237 N N   . GLY   B 2 127 ? -16.915 3.400   -16.324 1.00 56.23  ? 136 GLY   B N   1 
ATOM   1238 C CA  . GLY   B 2 127 ? -18.292 3.022   -16.055 1.00 55.83  ? 136 GLY   B CA  1 
ATOM   1239 C C   . GLY   B 2 127 ? -19.063 2.644   -17.304 1.00 55.69  ? 136 GLY   B C   1 
ATOM   1240 O O   . GLY   B 2 127 ? -20.268 2.397   -17.233 1.00 55.79  ? 136 GLY   B O   1 
ATOM   1241 N N   . SER   B 2 128 ? -18.378 2.599   -18.466 1.00 55.32  ? 137 SER   B N   1 
ATOM   1242 C CA  . SER   B 2 128 ? -18.968 2.231   -19.736 1.00 55.46  ? 137 SER   B CA  1 
ATOM   1243 C C   . SER   B 2 128 ? -19.213 0.725   -19.757 1.00 55.71  ? 137 SER   B C   1 
ATOM   1244 O O   . SER   B 2 128 ? -18.313 -0.061  -19.466 1.00 55.53  ? 137 SER   B O   1 
ATOM   1245 C CB  . SER   B 2 128 ? -18.071 2.662   -20.895 1.00 56.44  ? 137 SER   B CB  1 
ATOM   1246 O OG  . SER   B 2 128 ? -18.249 4.036   -21.204 1.00 57.95  ? 137 SER   B OG  1 
ATOM   1247 N N   . PRO   B 2 129 ? -20.446 0.308   -20.069 1.00 56.01  ? 138 PRO   B N   1 
ATOM   1248 C CA  . PRO   B 2 129 ? -20.756 -1.127  -20.061 1.00 56.25  ? 138 PRO   B CA  1 
ATOM   1249 C C   . PRO   B 2 129 ? -20.064 -1.970  -21.128 1.00 56.47  ? 138 PRO   B C   1 
ATOM   1250 O O   . PRO   B 2 129 ? -19.798 -1.512  -22.237 1.00 56.53  ? 138 PRO   B O   1 
ATOM   1251 C CB  . PRO   B 2 129 ? -22.272 -1.153  -20.266 1.00 57.17  ? 138 PRO   B CB  1 
ATOM   1252 C CG  . PRO   B 2 129 ? -22.571 0.131   -21.027 1.00 57.48  ? 138 PRO   B CG  1 
ATOM   1253 C CD  . PRO   B 2 129 ? -21.631 1.123   -20.409 1.00 55.73  ? 138 PRO   B CD  1 
ATOM   1254 N N   . ILE   B 2 130 ? -19.801 -3.230  -20.785 1.00 56.18  ? 139 ILE   B N   1 
ATOM   1255 C CA  . ILE   B 2 130 ? -19.224 -4.215  -21.684 1.00 56.26  ? 139 ILE   B CA  1 
ATOM   1256 C C   . ILE   B 2 130 ? -20.342 -5.216  -21.934 1.00 57.67  ? 139 ILE   B C   1 
ATOM   1257 O O   . ILE   B 2 130 ? -20.975 -5.690  -20.986 1.00 57.71  ? 139 ILE   B O   1 
ATOM   1258 C CB  . ILE   B 2 130 ? -17.981 -4.829  -21.042 1.00 55.74  ? 139 ILE   B CB  1 
ATOM   1259 C CG1 . ILE   B 2 130 ? -16.895 -3.756  -20.895 1.00 56.42  ? 139 ILE   B CG1 1 
ATOM   1260 C CG2 . ILE   B 2 130 ? -17.494 -6.033  -21.826 1.00 55.64  ? 139 ILE   B CG2 1 
ATOM   1261 C CD1 . ILE   B 2 130 ? -15.851 -4.107  -19.949 1.00 57.85  ? 139 ILE   B CD1 1 
ATOM   1262 N N   . LEU   B 2 131 ? -20.649 -5.476  -23.212 1.00 58.34  ? 140 LEU   B N   1 
ATOM   1263 C CA  . LEU   B 2 131 ? -21.806 -6.279  -23.575 1.00 59.48  ? 140 LEU   B CA  1 
ATOM   1264 C C   . LEU   B 2 131 ? -21.537 -7.611  -24.224 1.00 60.98  ? 140 LEU   B C   1 
ATOM   1265 O O   . LEU   B 2 131 ? -20.556 -7.768  -24.933 1.00 61.20  ? 140 LEU   B O   1 
ATOM   1266 C CB  . LEU   B 2 131 ? -22.709 -5.480  -24.537 1.00 59.75  ? 140 LEU   B CB  1 
ATOM   1267 C CG  . LEU   B 2 131 ? -22.889 -4.002  -24.296 1.00 61.34  ? 140 LEU   B CG  1 
ATOM   1268 C CD1 . LEU   B 2 131 ? -23.770 -3.395  -25.365 1.00 61.77  ? 140 LEU   B CD1 1 
ATOM   1269 C CD2 . LEU   B 2 131 ? -23.429 -3.744  -22.895 1.00 62.13  ? 140 LEU   B CD2 1 
ATOM   1270 N N   . ASP   B 2 132 ? -22.475 -8.547  -24.067 1.00 62.24  ? 141 ASP   B N   1 
ATOM   1271 C CA  . ASP   B 2 132 ? -22.430 -9.824  -24.766 1.00 64.35  ? 141 ASP   B CA  1 
ATOM   1272 C C   . ASP   B 2 132 ? -23.307 -9.746  -26.033 1.00 66.84  ? 141 ASP   B C   1 
ATOM   1273 O O   . ASP   B 2 132 ? -24.029 -8.757  -26.217 1.00 66.81  ? 141 ASP   B O   1 
ATOM   1274 C CB  . ASP   B 2 132 ? -22.848 -10.991 -23.848 1.00 65.82  ? 141 ASP   B CB  1 
ATOM   1275 C CG  . ASP   B 2 132 ? -24.219 -10.923 -23.215 1.00 69.68  ? 141 ASP   B CG  1 
ATOM   1276 O OD1 . ASP   B 2 132 ? -25.091 -10.247 -23.763 1.00 70.35  ? 141 ASP   B OD1 1 
ATOM   1277 O OD2 . ASP   B 2 132 ? -24.420 -11.571 -22.187 1.00 72.66  ? 141 ASP   B OD2 1 
ATOM   1278 N N   . LYS   B 2 133 ? -23.270 -10.782 -26.898 1.00 68.67  ? 142 LYS   B N   1 
ATOM   1279 C CA  . LYS   B 2 133 ? -24.061 -10.805 -28.134 1.00 70.62  ? 142 LYS   B CA  1 
ATOM   1280 C C   . LYS   B 2 133 ? -25.579 -10.642 -27.895 1.00 71.32  ? 142 LYS   B C   1 
ATOM   1281 O O   . LYS   B 2 133 ? -26.300 -10.233 -28.807 1.00 71.65  ? 142 LYS   B O   1 
ATOM   1282 C CB  . LYS   B 2 133 ? -23.742 -12.064 -28.961 1.00 74.46  ? 142 LYS   B CB  1 
ATOM   1283 C CG  . LYS   B 2 133 ? -22.262 -12.161 -29.383 1.00 81.10  ? 142 LYS   B CG  1 
ATOM   1284 C CD  . LYS   B 2 133 ? -21.635 -13.541 -29.114 1.00 87.05  ? 142 LYS   B CD  1 
ATOM   1285 C CE  . LYS   B 2 133 ? -20.337 -13.735 -29.869 1.00 91.80  ? 142 LYS   B CE  1 
ATOM   1286 N NZ  . LYS   B 2 133 ? -19.731 -15.076 -29.610 1.00 94.65  ? 142 LYS   B NZ  1 
ATOM   1287 N N   . CYS   B 2 134 ? -26.047 -10.895 -26.654 1.00 71.48  ? 143 CYS   B N   1 
ATOM   1288 C CA  . CYS   B 2 134 ? -27.448 -10.713 -26.244 1.00 71.97  ? 143 CYS   B CA  1 
ATOM   1289 C C   . CYS   B 2 134 ? -27.803 -9.277  -25.849 1.00 70.81  ? 143 CYS   B C   1 
ATOM   1290 O O   . CYS   B 2 134 ? -28.977 -8.984  -25.641 1.00 71.22  ? 143 CYS   B O   1 
ATOM   1291 C CB  . CYS   B 2 134 ? -27.796 -11.673 -25.113 1.00 74.22  ? 143 CYS   B CB  1 
ATOM   1292 S SG  . CYS   B 2 134 ? -28.536 -13.228 -25.661 1.00 81.25  ? 143 CYS   B SG  1 
ATOM   1293 N N   . GLY   B 2 135 ? -26.804 -8.419  -25.686 1.00 69.27  ? 144 GLY   B N   1 
ATOM   1294 C CA  . GLY   B 2 135 ? -27.010 -7.044  -25.251 1.00 68.31  ? 144 GLY   B CA  1 
ATOM   1295 C C   . GLY   B 2 135 ? -26.904 -6.861  -23.747 1.00 67.03  ? 144 GLY   B C   1 
ATOM   1296 O O   . GLY   B 2 135 ? -27.027 -5.735  -23.247 1.00 67.14  ? 144 GLY   B O   1 
ATOM   1297 N N   . ARG   B 2 136 ? -26.678 -7.966  -23.006 1.00 65.55  ? 145 ARG   B N   1 
ATOM   1298 C CA  . ARG   B 2 136 ? -26.564 -7.953  -21.553 1.00 64.71  ? 145 ARG   B CA  1 
ATOM   1299 C C   . ARG   B 2 136 ? -25.278 -7.316  -21.079 1.00 63.08  ? 145 ARG   B C   1 
ATOM   1300 O O   . ARG   B 2 136 ? -24.266 -7.364  -21.777 1.00 63.35  ? 145 ARG   B O   1 
ATOM   1301 C CB  . ARG   B 2 136 ? -26.732 -9.359  -20.969 1.00 66.14  ? 145 ARG   B CB  1 
ATOM   1302 C CG  . ARG   B 2 136 ? -28.175 -9.834  -21.011 1.00 69.87  ? 145 ARG   B CG  1 
ATOM   1303 C CD  . ARG   B 2 136 ? -28.290 -11.293 -20.654 1.00 73.56  ? 145 ARG   B CD  1 
ATOM   1304 N NE  . ARG   B 2 136 ? -27.808 -12.146 -21.739 1.00 77.02  ? 145 ARG   B NE  1 
ATOM   1305 C CZ  . ARG   B 2 136 ? -27.112 -13.265 -21.564 1.00 79.29  ? 145 ARG   B CZ  1 
ATOM   1306 N NH1 . ARG   B 2 136 ? -26.781 -13.666 -20.339 1.00 78.35  ? 145 ARG   B NH1 1 
ATOM   1307 N NH2 . ARG   B 2 136 ? -26.726 -13.984 -22.612 1.00 79.41  ? 145 ARG   B NH2 1 
ATOM   1308 N N   . VAL   B 2 137 ? -25.327 -6.683  -19.905 1.00 61.16  ? 146 VAL   B N   1 
ATOM   1309 C CA  . VAL   B 2 137 ? -24.155 -6.030  -19.355 1.00 59.66  ? 146 VAL   B CA  1 
ATOM   1310 C C   . VAL   B 2 137 ? -23.381 -7.027  -18.522 1.00 58.32  ? 146 VAL   B C   1 
ATOM   1311 O O   . VAL   B 2 137 ? -23.851 -7.472  -17.478 1.00 58.18  ? 146 VAL   B O   1 
ATOM   1312 C CB  . VAL   B 2 137 ? -24.522 -4.766  -18.569 1.00 60.03  ? 146 VAL   B CB  1 
ATOM   1313 C CG1 . VAL   B 2 137 ? -23.266 -4.060  -18.082 1.00 60.79  ? 146 VAL   B CG1 1 
ATOM   1314 C CG2 . VAL   B 2 137 ? -25.374 -3.832  -19.418 1.00 60.10  ? 146 VAL   B CG2 1 
ATOM   1315 N N   . ILE   B 2 138 ? -22.224 -7.433  -19.034 1.00 56.98  ? 147 ILE   B N   1 
ATOM   1316 C CA  . ILE   B 2 138 ? -21.354 -8.396  -18.379 1.00 55.85  ? 147 ILE   B CA  1 
ATOM   1317 C C   . ILE   B 2 138 ? -20.293 -7.749  -17.468 1.00 55.30  ? 147 ILE   B C   1 
ATOM   1318 O O   . ILE   B 2 138 ? -19.513 -8.470  -16.863 1.00 55.44  ? 147 ILE   B O   1 
ATOM   1319 C CB  . ILE   B 2 138 ? -20.704 -9.356  -19.420 1.00 55.58  ? 147 ILE   B CB  1 
ATOM   1320 C CG1 . ILE   B 2 138 ? -19.748 -8.616  -20.358 1.00 55.65  ? 147 ILE   B CG1 1 
ATOM   1321 C CG2 . ILE   B 2 138 ? -21.750 -10.142 -20.199 1.00 55.81  ? 147 ILE   B CG2 1 
ATOM   1322 C CD1 . ILE   B 2 138 ? -18.869 -9.483  -21.090 1.00 56.25  ? 147 ILE   B CD1 1 
ATOM   1323 N N   . GLY   B 2 139 ? -20.273 -6.424  -17.363 1.00 54.79  ? 148 GLY   B N   1 
ATOM   1324 C CA  . GLY   B 2 139 ? -19.306 -5.732  -16.519 1.00 55.02  ? 148 GLY   B CA  1 
ATOM   1325 C C   . GLY   B 2 139 ? -19.072 -4.292  -16.919 1.00 55.16  ? 148 GLY   B C   1 
ATOM   1326 O O   . GLY   B 2 139 ? -19.642 -3.830  -17.904 1.00 55.30  ? 148 GLY   B O   1 
ATOM   1327 N N   . LEU   B 2 140 ? -18.238 -3.561  -16.160 1.00 55.04  ? 149 LEU   B N   1 
ATOM   1328 C CA  . LEU   B 2 140 ? -17.926 -2.161  -16.465 1.00 55.32  ? 149 LEU   B CA  1 
ATOM   1329 C C   . LEU   B 2 140 ? -16.432 -1.954  -16.725 1.00 56.07  ? 149 LEU   B C   1 
ATOM   1330 O O   . LEU   B 2 140 ? -15.588 -2.633  -16.141 1.00 55.91  ? 149 LEU   B O   1 
ATOM   1331 C CB  . LEU   B 2 140 ? -18.388 -1.197  -15.352 1.00 54.97  ? 149 LEU   B CB  1 
ATOM   1332 C CG  . LEU   B 2 140 ? -19.873 -1.169  -14.992 1.00 55.63  ? 149 LEU   B CG  1 
ATOM   1333 C CD1 . LEU   B 2 140 ? -20.150 -0.114  -13.934 1.00 56.19  ? 149 LEU   B CD1 1 
ATOM   1334 C CD2 . LEU   B 2 140 ? -20.737 -0.935  -16.197 1.00 55.67  ? 149 LEU   B CD2 1 
ATOM   1335 N N   . TYR   B 2 141 ? -16.123 -0.996  -17.601 1.00 56.64  ? 150 TYR   B N   1 
ATOM   1336 C CA  . TYR   B 2 141 ? -14.766 -0.630  -17.987 1.00 57.80  ? 150 TYR   B CA  1 
ATOM   1337 C C   . TYR   B 2 141 ? -14.300 0.525   -17.100 1.00 58.16  ? 150 TYR   B C   1 
ATOM   1338 O O   . TYR   B 2 141 ? -15.073 1.439   -16.873 1.00 57.96  ? 150 TYR   B O   1 
ATOM   1339 C CB  . TYR   B 2 141 ? -14.765 -0.191  -19.475 1.00 58.29  ? 150 TYR   B CB  1 
ATOM   1340 C CG  . TYR   B 2 141 ? -13.461 0.415   -19.964 1.00 60.02  ? 150 TYR   B CG  1 
ATOM   1341 C CD1 . TYR   B 2 141 ? -13.199 1.771   -19.816 1.00 61.47  ? 150 TYR   B CD1 1 
ATOM   1342 C CD2 . TYR   B 2 141 ? -12.532 -0.349  -20.652 1.00 61.50  ? 150 TYR   B CD2 1 
ATOM   1343 C CE1 . TYR   B 2 141 ? -11.991 2.322   -20.222 1.00 62.83  ? 150 TYR   B CE1 1 
ATOM   1344 C CE2 . TYR   B 2 141 ? -11.342 0.200   -21.110 1.00 62.82  ? 150 TYR   B CE2 1 
ATOM   1345 C CZ  . TYR   B 2 141 ? -11.065 1.534   -20.879 1.00 64.16  ? 150 TYR   B CZ  1 
ATOM   1346 O OH  . TYR   B 2 141 ? -9.894  2.085   -21.344 1.00 66.35  ? 150 TYR   B OH  1 
ATOM   1347 N N   . GLY   B 2 142 ? -13.042 0.514   -16.661 1.00 58.43  ? 151 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 142 ? -12.514 1.616   -15.867 1.00 59.24  ? 151 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 142 ? -11.542 1.241   -14.773 1.00 59.88  ? 151 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 142 ? -10.916 2.124   -14.180 1.00 60.10  ? 151 GLY   B O   1 
ATOM   1351 N N   . ASN   B 2 143 ? -11.418 -0.058  -14.475 1.00 59.95  ? 152 ASN   B N   1 
ATOM   1352 C CA  . ASN   B 2 143 ? -10.487 -0.506  -13.439 1.00 60.62  ? 152 ASN   B CA  1 
ATOM   1353 C C   . ASN   B 2 143 ? -9.556  -1.576  -13.965 1.00 61.21  ? 152 ASN   B C   1 
ATOM   1354 O O   . ASN   B 2 143 ? -9.951  -2.724  -14.130 1.00 60.93  ? 152 ASN   B O   1 
ATOM   1355 C CB  . ASN   B 2 143 ? -11.225 -1.006  -12.203 1.00 61.49  ? 152 ASN   B CB  1 
ATOM   1356 C CG  . ASN   B 2 143 ? -10.342 -1.097  -10.985 1.00 63.55  ? 152 ASN   B CG  1 
ATOM   1357 O OD1 . ASN   B 2 143 ? -9.266  -0.484  -10.921 1.00 63.61  ? 152 ASN   B OD1 1 
ATOM   1358 N ND2 . ASN   B 2 143 ? -10.778 -1.872  -9.991  1.00 64.21  ? 152 ASN   B ND2 1 
ATOM   1359 N N   . GLY   B 2 144 ? -8.321  -1.193  -14.213 1.00 62.09  ? 153 GLY   B N   1 
ATOM   1360 C CA  . GLY   B 2 144 ? -7.337  -2.115  -14.738 1.00 63.64  ? 153 GLY   B CA  1 
ATOM   1361 C C   . GLY   B 2 144 ? -5.914  -1.744  -14.426 1.00 65.45  ? 153 GLY   B C   1 
ATOM   1362 O O   . GLY   B 2 144 ? -5.603  -1.282  -13.328 1.00 65.56  ? 153 GLY   B O   1 
ATOM   1363 N N   . VAL   B 2 145 ? -5.040  -1.945  -15.404 1.00 66.86  ? 154 VAL   B N   1 
ATOM   1364 C CA  . VAL   B 2 145 ? -3.622  -1.727  -15.211 1.00 68.64  ? 154 VAL   B CA  1 
ATOM   1365 C C   . VAL   B 2 145 ? -2.952  -1.009  -16.408 1.00 70.95  ? 154 VAL   B C   1 
ATOM   1366 O O   . VAL   B 2 145 ? -3.535  -0.904  -17.490 1.00 70.86  ? 154 VAL   B O   1 
ATOM   1367 C CB  . VAL   B 2 145 ? -2.993  -3.104  -14.877 1.00 68.99  ? 154 VAL   B CB  1 
ATOM   1368 C CG1 . VAL   B 2 145 ? -2.571  -3.864  -16.133 1.00 69.04  ? 154 VAL   B CG1 1 
ATOM   1369 C CG2 . VAL   B 2 145 ? -1.853  -2.970  -13.881 1.00 69.69  ? 154 VAL   B CG2 1 
ATOM   1370 N N   . VAL   B 2 146 ? -1.745  -0.479  -16.192 1.00 72.73  ? 155 VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 146 ? -1.001  0.201   -17.242 1.00 74.95  ? 155 VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 146 ? 0.133   -0.711  -17.698 1.00 77.46  ? 155 VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 146 ? 1.048   -1.000  -16.931 1.00 77.53  ? 155 VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 146 ? -0.489  1.578   -16.777 1.00 75.51  ? 155 VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 146 ? 0.465   2.175   -17.798 1.00 76.28  ? 155 VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 146 ? -1.654  2.521   -16.511 1.00 75.72  ? 155 VAL   B CG2 1 
ATOM   1377 N N   . ILE   B 2 147 ? 0.042   -1.209  -18.931 1.00 79.33  ? 156 ILE   B N   1 
ATOM   1378 C CA  . ILE   B 2 147 ? 1.038   -2.130  -19.469 1.00 81.51  ? 156 ILE   B CA  1 
ATOM   1379 C C   . ILE   B 2 147 ? 2.300   -1.401  -19.950 1.00 83.75  ? 156 ILE   B C   1 
ATOM   1380 O O   . ILE   B 2 147 ? 2.289   -0.177  -20.059 1.00 84.22  ? 156 ILE   B O   1 
ATOM   1381 C CB  . ILE   B 2 147 ? 0.403   -3.037  -20.555 1.00 82.19  ? 156 ILE   B CB  1 
ATOM   1382 C CG1 . ILE   B 2 147 ? -0.317  -2.207  -21.633 1.00 82.96  ? 156 ILE   B CG1 1 
ATOM   1383 C CG2 . ILE   B 2 147 ? -0.538  -4.056  -19.909 1.00 82.86  ? 156 ILE   B CG2 1 
ATOM   1384 C CD1 . ILE   B 2 147 ? -0.889  -3.038  -22.773 1.00 84.10  ? 156 ILE   B CD1 1 
ATOM   1385 N N   . LYS   B 2 148 ? 3.388   -2.153  -20.223 1.00 84.93  ? 157 LYS   B N   1 
ATOM   1386 C CA  . LYS   B 2 148 ? 4.697   -1.649  -20.661 1.00 86.51  ? 157 LYS   B CA  1 
ATOM   1387 C C   . LYS   B 2 148 ? 4.679   -0.547  -21.743 1.00 87.32  ? 157 LYS   B C   1 
ATOM   1388 O O   . LYS   B 2 148 ? 5.610   0.263   -21.796 1.00 87.60  ? 157 LYS   B O   1 
ATOM   1389 C CB  . LYS   B 2 148 ? 5.587   -2.808  -21.130 1.00 89.02  ? 157 LYS   B CB  1 
ATOM   1390 C CG  . LYS   B 2 148 ? 5.728   -3.913  -20.092 1.00 93.92  ? 157 LYS   B CG  1 
ATOM   1391 C CD  . LYS   B 2 148 ? 6.884   -4.847  -20.441 1.00 99.21  ? 157 LYS   B CD  1 
ATOM   1392 C CE  . LYS   B 2 148 ? 8.254   -4.206  -20.294 1.00 103.18 ? 157 LYS   B CE  1 
ATOM   1393 N NZ  . LYS   B 2 148 ? 8.701   -4.139  -18.871 1.00 105.41 ? 157 LYS   B NZ  1 
ATOM   1394 N N   . ASN   B 2 149 ? 3.654   -0.518  -22.604 1.00 87.38  ? 158 ASN   B N   1 
ATOM   1395 C CA  . ASN   B 2 149 ? 3.578   0.506   -23.654 1.00 88.03  ? 158 ASN   B CA  1 
ATOM   1396 C C   . ASN   B 2 149 ? 2.697   1.711   -23.281 1.00 87.17  ? 158 ASN   B C   1 
ATOM   1397 O O   . ASN   B 2 149 ? 2.196   2.408   -24.168 1.00 87.41  ? 158 ASN   B O   1 
ATOM   1398 C CB  . ASN   B 2 149 ? 3.161   -0.083  -25.020 1.00 90.54  ? 158 ASN   B CB  1 
ATOM   1399 C CG  . ASN   B 2 149 ? 2.310   -1.336  -24.971 1.00 95.16  ? 158 ASN   B CG  1 
ATOM   1400 O OD1 . ASN   B 2 149 ? 2.813   -2.460  -24.815 1.00 96.16  ? 158 ASN   B OD1 1 
ATOM   1401 N ND2 . ASN   B 2 149 ? 1.002   -1.165  -25.124 1.00 96.44  ? 158 ASN   B ND2 1 
ATOM   1402 N N   . GLY   B 2 150 ? 2.534   1.945   -21.978 1.00 85.92  ? 159 GLY   B N   1 
ATOM   1403 C CA  . GLY   B 2 150 ? 1.736   3.034   -21.427 1.00 84.95  ? 159 GLY   B CA  1 
ATOM   1404 C C   . GLY   B 2 150 ? 0.235   2.852   -21.542 1.00 83.58  ? 159 GLY   B C   1 
ATOM   1405 O O   . GLY   B 2 150 ? -0.524  3.540   -20.855 1.00 83.63  ? 159 GLY   B O   1 
ATOM   1406 N N   . SER   B 2 151 ? -0.204  1.920   -22.414 1.00 82.08  ? 160 SER   B N   1 
ATOM   1407 C CA  A SER   B 2 151 ? -1.611  1.613   -22.681 0.50 81.65  ? 160 SER   B CA  1 
ATOM   1408 C CA  B SER   B 2 151 ? -1.624  1.668   -22.661 0.50 81.74  ? 160 SER   B CA  1 
ATOM   1409 C C   . SER   B 2 151 ? -2.371  1.098   -21.445 1.00 80.86  ? 160 SER   B C   1 
ATOM   1410 O O   . SER   B 2 151 ? -1.750  0.662   -20.469 1.00 80.95  ? 160 SER   B O   1 
ATOM   1411 C CB  A SER   B 2 151 ? -1.716  0.608   -23.827 0.50 82.86  ? 160 SER   B CB  1 
ATOM   1412 C CB  B SER   B 2 151 ? -1.837  0.802   -23.907 0.50 83.13  ? 160 SER   B CB  1 
ATOM   1413 O OG  A SER   B 2 151 ? -3.057  0.375   -24.225 0.50 84.75  ? 160 SER   B OG  1 
ATOM   1414 O OG  B SER   B 2 151 ? -0.737  -0.032  -24.233 0.50 85.32  ? 160 SER   B OG  1 
ATOM   1415 N N   . TYR   B 2 152 ? -3.714  1.156   -21.487 1.00 78.71  ? 161 TYR   B N   1 
ATOM   1416 C CA  . TYR   B 2 152 ? -4.569  0.685   -20.413 1.00 77.07  ? 161 TYR   B CA  1 
ATOM   1417 C C   . TYR   B 2 152 ? -5.272  -0.598  -20.835 1.00 75.54  ? 161 TYR   B C   1 
ATOM   1418 O O   . TYR   B 2 152 ? -5.725  -0.725  -21.970 1.00 75.64  ? 161 TYR   B O   1 
ATOM   1419 C CB  . TYR   B 2 152 ? -5.621  1.753   -20.042 1.00 76.50  ? 161 TYR   B CB  1 
ATOM   1420 C CG  . TYR   B 2 152 ? -6.069  1.688   -18.596 1.00 76.38  ? 161 TYR   B CG  1 
ATOM   1421 C CD1 . TYR   B 2 152 ? -5.228  2.087   -17.569 1.00 76.89  ? 161 TYR   B CD1 1 
ATOM   1422 C CD2 . TYR   B 2 152 ? -7.339  1.236   -18.257 1.00 76.74  ? 161 TYR   B CD2 1 
ATOM   1423 C CE1 . TYR   B 2 152 ? -5.626  2.013   -16.238 1.00 77.42  ? 161 TYR   B CE1 1 
ATOM   1424 C CE2 . TYR   B 2 152 ? -7.746  1.154   -16.928 1.00 77.23  ? 161 TYR   B CE2 1 
ATOM   1425 C CZ  . TYR   B 2 152 ? -6.887  1.553   -15.921 1.00 77.90  ? 161 TYR   B CZ  1 
ATOM   1426 O OH  . TYR   B 2 152 ? -7.270  1.509   -14.601 1.00 78.76  ? 161 TYR   B OH  1 
ATOM   1427 N N   . VAL   B 2 153 ? -5.346  -1.559  -19.919 1.00 73.66  ? 162 VAL   B N   1 
ATOM   1428 C CA  . VAL   B 2 153 ? -6.062  -2.802  -20.140 1.00 71.80  ? 162 VAL   B CA  1 
ATOM   1429 C C   . VAL   B 2 153 ? -6.944  -2.912  -18.920 1.00 69.66  ? 162 VAL   B C   1 
ATOM   1430 O O   . VAL   B 2 153 ? -6.451  -3.093  -17.812 1.00 69.56  ? 162 VAL   B O   1 
ATOM   1431 C CB  . VAL   B 2 153 ? -5.125  -4.020  -20.328 1.00 72.07  ? 162 VAL   B CB  1 
ATOM   1432 C CG1 . VAL   B 2 153 ? -5.895  -5.333  -20.215 1.00 72.32  ? 162 VAL   B CG1 1 
ATOM   1433 C CG2 . VAL   B 2 153 ? -4.396  -3.939  -21.664 1.00 72.36  ? 162 VAL   B CG2 1 
ATOM   1434 N N   . SER   B 2 154 ? -8.228  -2.656  -19.100 1.00 67.84  ? 163 SER   B N   1 
ATOM   1435 C CA  . SER   B 2 154 ? -9.176  -2.663  -17.994 1.00 66.52  ? 163 SER   B CA  1 
ATOM   1436 C C   . SER   B 2 154 ? -9.786  -4.039  -17.774 1.00 65.00  ? 163 SER   B C   1 
ATOM   1437 O O   . SER   B 2 154 ? -9.960  -4.786  -18.723 1.00 65.18  ? 163 SER   B O   1 
ATOM   1438 C CB  . SER   B 2 154 ? -10.265 -1.621  -18.247 1.00 67.25  ? 163 SER   B CB  1 
ATOM   1439 O OG  . SER   B 2 154 ? -11.547 -1.953  -17.737 1.00 69.02  ? 163 SER   B OG  1 
ATOM   1440 N N   . ALA   B 2 155 ? -10.171 -4.347  -16.534 1.00 63.32  ? 164 ALA   B N   1 
ATOM   1441 C CA  . ALA   B 2 155 ? -10.852 -5.600  -16.239 1.00 62.05  ? 164 ALA   B CA  1 
ATOM   1442 C C   . ALA   B 2 155 ? -12.357 -5.497  -16.631 1.00 61.18  ? 164 ALA   B C   1 
ATOM   1443 O O   . ALA   B 2 155 ? -12.871 -4.400  -16.882 1.00 60.94  ? 164 ALA   B O   1 
ATOM   1444 C CB  . ALA   B 2 155 ? -10.714 -5.916  -14.758 1.00 61.59  ? 164 ALA   B CB  1 
ATOM   1445 N N   . ILE   B 2 156 ? -13.052 -6.648  -16.713 1.00 60.32  ? 165 ILE   B N   1 
ATOM   1446 C CA  . ILE   B 2 156 ? -14.490 -6.674  -16.930 1.00 59.74  ? 165 ILE   B CA  1 
ATOM   1447 C C   . ILE   B 2 156 ? -15.050 -6.791  -15.510 1.00 58.98  ? 165 ILE   B C   1 
ATOM   1448 O O   . ILE   B 2 156 ? -15.109 -7.899  -14.961 1.00 58.76  ? 165 ILE   B O   1 
ATOM   1449 C CB  . ILE   B 2 156 ? -14.930 -7.849  -17.838 1.00 60.02  ? 165 ILE   B CB  1 
ATOM   1450 C CG1 . ILE   B 2 156 ? -14.219 -7.784  -19.214 1.00 60.86  ? 165 ILE   B CG1 1 
ATOM   1451 C CG2 . ILE   B 2 156 ? -16.456 -7.864  -17.993 1.00 60.22  ? 165 ILE   B CG2 1 
ATOM   1452 C CD1 . ILE   B 2 156 ? -14.586 -8.893  -20.186 1.00 61.67  ? 165 ILE   B CD1 1 
ATOM   1453 N N   . THR   B 2 157 ? -15.357 -5.626  -14.876 1.00 58.12  ? 166 THR   B N   1 
ATOM   1454 C CA  . THR   B 2 157 ? -15.814 -5.561  -13.477 1.00 57.22  ? 166 THR   B CA  1 
ATOM   1455 C C   . THR   B 2 157 ? -17.305 -5.719  -13.307 1.00 56.79  ? 166 THR   B C   1 
ATOM   1456 O O   . THR   B 2 157 ? -18.059 -4.798  -13.609 1.00 56.70  ? 166 THR   B O   1 
ATOM   1457 C CB  . THR   B 2 157 ? -15.337 -4.280  -12.790 1.00 57.31  ? 166 THR   B CB  1 
ATOM   1458 O OG1 . THR   B 2 157 ? -13.961 -4.068  -13.078 1.00 57.92  ? 166 THR   B OG1 1 
ATOM   1459 C CG2 . THR   B 2 157 ? -15.534 -4.321  -11.301 1.00 57.22  ? 166 THR   B CG2 1 
ATOM   1460 N N   . GLN   B 2 158 ? -17.729 -6.866  -12.791 1.00 56.41  ? 167 GLN   B N   1 
ATOM   1461 C CA  . GLN   B 2 158 ? -19.129 -7.147  -12.543 1.00 56.90  ? 167 GLN   B CA  1 
ATOM   1462 C C   . GLN   B 2 158 ? -19.365 -7.267  -11.031 1.00 58.85  ? 167 GLN   B C   1 
ATOM   1463 O O   . GLN   B 2 158 ? -18.504 -7.750  -10.299 1.00 58.99  ? 167 GLN   B O   1 
ATOM   1464 C CB  . GLN   B 2 158 ? -19.533 -8.432  -13.290 1.00 57.17  ? 167 GLN   B CB  1 
ATOM   1465 C CG  . GLN   B 2 158 ? -21.005 -8.837  -13.217 1.00 58.15  ? 167 GLN   B CG  1 
ATOM   1466 C CD  . GLN   B 2 158 ? -21.968 -7.822  -13.791 1.00 59.16  ? 167 GLN   B CD  1 
ATOM   1467 O OE1 . GLN   B 2 158 ? -22.074 -6.689  -13.320 1.00 60.84  ? 167 GLN   B OE1 1 
ATOM   1468 N NE2 . GLN   B 2 158 ? -22.734 -8.219  -14.778 1.00 57.64  ? 167 GLN   B NE2 1 
ATOM   1469 N N   . GLY   B 2 159 ? -20.517 -6.805  -10.572 1.00 60.32  ? 168 GLY   B N   1 
ATOM   1470 C CA  . GLY   B 2 159 ? -20.871 -6.893  -9.168  1.00 62.53  ? 168 GLY   B CA  1 
ATOM   1471 C C   . GLY   B 2 159 ? -21.587 -8.185  -8.845  1.00 65.36  ? 168 GLY   B C   1 
ATOM   1472 O O   . GLY   B 2 159 ? -21.527 -9.152  -9.610  1.00 65.31  ? 168 GLY   B O   1 
ATOM   1473 N N   . LYS   B 2 160 ? -22.272 -8.213  -7.699  1.00 67.62  ? 169 LYS   B N   1 
ATOM   1474 C CA  . LYS   B 2 160 ? -23.035 -9.386  -7.296  1.00 70.19  ? 169 LYS   B CA  1 
ATOM   1475 C C   . LYS   B 2 160 ? -24.524 -9.023  -7.108  1.00 72.78  ? 169 LYS   B C   1 
ATOM   1476 O O   . LYS   B 2 160 ? -24.846 -8.009  -6.480  1.00 73.27  ? 169 LYS   B O   1 
ATOM   1477 C CB  . LYS   B 2 160 ? -22.447 -10.021 -6.025  1.00 72.20  ? 169 LYS   B CB  1 
ATOM   1478 C CG  . LYS   B 2 160 ? -22.861 -11.471 -5.851  1.00 76.79  ? 169 LYS   B CG  1 
ATOM   1479 C CD  . LYS   B 2 160 ? -22.632 -11.980 -4.437  1.00 81.72  ? 169 LYS   B CD  1 
ATOM   1480 C CE  . LYS   B 2 160 ? -23.255 -13.345 -4.235  1.00 85.15  ? 169 LYS   B CE  1 
ATOM   1481 N NZ  . LYS   B 2 160 ? -23.144 -13.799 -2.824  1.00 87.41  ? 169 LYS   B NZ  1 
ATOM   1482 N N   . ARG   B 2 161 ? -25.426 -9.834  -7.688  1.00 74.12  ? 170 ARG   B N   1 
ATOM   1483 C CA  . ARG   B 2 161 ? -26.868 -9.634  -7.555  1.00 75.72  ? 170 ARG   B CA  1 
ATOM   1484 C C   . ARG   B 2 161 ? -27.368 -10.548 -6.425  1.00 77.38  ? 170 ARG   B C   1 
ATOM   1485 O O   . ARG   B 2 161 ? -27.148 -11.759 -6.479  1.00 77.91  ? 170 ARG   B O   1 
ATOM   1486 C CB  . ARG   B 2 161 ? -27.582 -9.953  -8.886  1.00 76.98  ? 170 ARG   B CB  1 
ATOM   1487 C CG  . ARG   B 2 161 ? -29.100 -9.864  -8.791  1.00 79.97  ? 170 ARG   B CG  1 
ATOM   1488 C CD  . ARG   B 2 161 ? -29.807 -9.794  -10.137 1.00 83.33  ? 170 ARG   B CD  1 
ATOM   1489 N NE  . ARG   B 2 161 ? -31.261 -9.730  -9.954  1.00 86.65  ? 170 ARG   B NE  1 
ATOM   1490 C CZ  . ARG   B 2 161 ? -32.076 -8.930  -10.637 1.00 88.47  ? 170 ARG   B CZ  1 
ATOM   1491 N NH1 . ARG   B 2 161 ? -31.596 -8.130  -11.582 1.00 87.85  ? 170 ARG   B NH1 1 
ATOM   1492 N NH2 . ARG   B 2 161 ? -33.378 -8.927  -10.381 1.00 88.19  ? 170 ARG   B NH2 1 
ATOM   1493 N N   . GLU   B 2 162 ? -27.989 -9.979  -5.385  1.00 78.09  ? 171 GLU   B N   1 
ATOM   1494 C CA  . GLU   B 2 162 ? -28.473 -10.778 -4.254  1.00 79.28  ? 171 GLU   B CA  1 
ATOM   1495 C C   . GLU   B 2 162 ? -29.808 -11.466 -4.555  1.00 79.30  ? 171 GLU   B C   1 
ATOM   1496 O O   . GLU   B 2 162 ? -30.206 -12.387 -3.843  1.00 79.23  ? 171 GLU   B O   1 
ATOM   1497 C CB  . GLU   B 2 162 ? -28.572 -9.918  -2.982  1.00 83.04  ? 171 GLU   B CB  1 
ATOM   1498 C CG  . GLU   B 2 162 ? -27.255 -9.275  -2.568  1.00 90.76  ? 171 GLU   B CG  1 
ATOM   1499 C CD  . GLU   B 2 162 ? -26.336 -10.166 -1.750  1.00 100.94 ? 171 GLU   B CD  1 
ATOM   1500 O OE1 . GLU   B 2 162 ? -26.360 -10.057 -0.502  1.00 102.81 ? 171 GLU   B OE1 1 
ATOM   1501 O OE2 . GLU   B 2 162 ? -25.594 -10.976 -2.355  1.00 104.29 ? 171 GLU   B OE2 1 
HETATM 1502 S S   . DMS   C 3 .   ? -18.619 12.006  -0.401  1.00 97.21  ? 201 DMS   B S   1 
HETATM 1503 O O   . DMS   C 3 .   ? -19.459 10.769  -0.464  1.00 97.14  ? 201 DMS   B O   1 
HETATM 1504 C C1  . DMS   C 3 .   ? -19.686 13.422  -0.774  1.00 97.25  ? 201 DMS   B C1  1 
HETATM 1505 C C2  . DMS   C 3 .   ? -17.644 12.125  -1.932  1.00 97.18  ? 201 DMS   B C2  1 
HETATM 1506 N N1  . A1B8K D 4 .   ? -8.998  4.207   -13.269 1.00 62.68  ? 202 A1B8K B N1  1 
HETATM 1507 N N3  . A1B8K D 4 .   ? -10.062 4.461   -17.303 1.00 65.76  ? 202 A1B8K B N3  1 
HETATM 1508 C C4  . A1B8K D 4 .   ? -8.964  5.343   -9.743  1.00 60.24  ? 202 A1B8K B C4  1 
HETATM 1509 C C5  . A1B8K D 4 .   ? -9.229  4.146   -9.090  1.00 59.70  ? 202 A1B8K B C5  1 
HETATM 1510 C C6  . A1B8K D 4 .   ? -9.451  2.981   -9.808  1.00 59.71  ? 202 A1B8K B C6  1 
HETATM 1511 C C7  . A1B8K D 4 .   ? -9.372  2.975   -11.195 1.00 60.51  ? 202 A1B8K B C7  1 
HETATM 1512 C C8  . A1B8K D 4 .   ? -9.768  1.868   -8.850  1.00 59.07  ? 202 A1B8K B C8  1 
HETATM 1513 C C10 . A1B8K D 4 .   ? -8.513  4.932   -15.535 1.00 64.90  ? 202 A1B8K B C10 1 
HETATM 1514 C C13 . A1B8K D 4 .   ? -7.818  4.999   -17.856 1.00 65.78  ? 202 A1B8K B C13 1 
HETATM 1515 C C15 . A1B8K D 4 .   ? -7.489  5.142   -16.497 1.00 65.49  ? 202 A1B8K B C15 1 
HETATM 1516 O O1  . A1B8K D 4 .   ? -7.430  5.824   -13.630 1.00 64.34  ? 202 A1B8K B O1  1 
HETATM 1517 C C1  . A1B8K D 4 .   ? -8.273  5.039   -14.059 1.00 64.04  ? 202 A1B8K B C1  1 
HETATM 1518 C C2  . A1B8K D 4 .   ? -9.099  4.184   -11.852 1.00 61.31  ? 202 A1B8K B C2  1 
HETATM 1519 C C3  . A1B8K D 4 .   ? -8.868  5.349   -11.125 1.00 60.79  ? 202 A1B8K B C3  1 
HETATM 1520 N N2  . A1B8K D 4 .   ? -9.240  2.407   -7.589  1.00 58.84  ? 202 A1B8K B N2  1 
HETATM 1521 C C9  . A1B8K D 4 .   ? -9.403  3.867   -7.625  1.00 59.14  ? 202 A1B8K B C9  1 
HETATM 1522 C C11 . A1B8K D 4 .   ? -9.764  4.548   -15.998 1.00 65.42  ? 202 A1B8K B C11 1 
HETATM 1523 C C12 . A1B8K D 4 .   ? -9.108  4.650   -18.215 1.00 65.76  ? 202 A1B8K B C12 1 
HETATM 1524 N N4  . A1B8K D 4 .   ? -6.694  5.265   -18.561 1.00 65.98  ? 202 A1B8K B N4  1 
HETATM 1525 N N5  . A1B8K D 4 .   ? -5.650  5.545   -17.730 1.00 65.99  ? 202 A1B8K B N5  1 
HETATM 1526 C C14 . A1B8K D 4 .   ? -6.115  5.480   -16.494 1.00 65.74  ? 202 A1B8K B C14 1 
HETATM 1527 O O   . HOH   E 5 .   ? -4.102  -14.632 -25.237 1.00 58.21  ? 101 HOH   A O   1 
HETATM 1528 O O   . HOH   E 5 .   ? -2.229  -3.983  -6.161  1.00 53.22  ? 102 HOH   A O   1 
HETATM 1529 O O   . HOH   E 5 .   ? -29.706 15.597  -15.220 1.00 63.48  ? 103 HOH   A O   1 
HETATM 1530 O O   . HOH   E 5 .   ? -23.775 18.863  -19.935 1.00 65.07  ? 104 HOH   A O   1 
HETATM 1531 O O   . HOH   E 5 .   ? -7.097  4.432   -4.465  1.00 71.64  ? 105 HOH   A O   1 
HETATM 1532 O O   . HOH   E 5 .   ? -4.862  -10.189 -5.595  1.00 49.45  ? 106 HOH   A O   1 
HETATM 1533 O O   . HOH   E 5 .   ? -26.349 1.142   -30.208 1.00 75.18  ? 107 HOH   A O   1 
HETATM 1534 O O   . HOH   E 5 .   ? -31.672 0.451   -23.406 1.00 61.94  ? 108 HOH   A O   1 
HETATM 1535 O O   . HOH   E 5 .   ? -2.531  -8.557  -3.388  1.00 47.40  ? 109 HOH   A O   1 
HETATM 1536 O O   . HOH   F 5 .   ? -6.901  -0.506  -10.997 1.00 49.32  ? 301 HOH   B O   1 
HETATM 1537 O O   . HOH   F 5 .   ? -34.304 2.135   -15.232 1.00 57.55  ? 302 HOH   B O   1 
HETATM 1538 O O   . HOH   F 5 .   ? -16.324 26.452  -12.549 1.00 72.40  ? 303 HOH   B O   1 
HETATM 1539 O O   . HOH   F 5 .   ? -15.846 -10.287 -15.404 1.00 72.71  ? 304 HOH   B O   1 
HETATM 1540 O O   . HOH   F 5 .   ? -15.236 -4.868  1.320   1.00 60.90  ? 305 HOH   B O   1 
HETATM 1541 O O   . HOH   F 5 .   ? -16.798 21.096  -14.731 1.00 92.94  ? 306 HOH   B O   1 
HETATM 1542 O O   . HOH   F 5 .   ? -13.107 -2.370  -14.879 1.00 56.73  ? 307 HOH   B O   1 
HETATM 1543 O O   . HOH   F 5 .   ? -19.681 -12.062 -25.723 1.00 58.11  ? 308 HOH   B O   1 
HETATM 1544 O O   . HOH   F 5 .   ? -15.370 8.679   -30.590 1.00 63.78  ? 309 HOH   B O   1 
HETATM 1545 O O   . HOH   F 5 .   ? -17.208 12.997  -5.520  1.00 57.93  ? 310 HOH   B O   1 
HETATM 1546 O O   . HOH   F 5 .   ? -18.249 -10.789 -16.432 1.00 63.24  ? 311 HOH   B O   1 
HETATM 1547 O O   . HOH   F 5 .   ? -9.652  -6.890  -25.678 1.00 68.29  ? 312 HOH   B O   1 
HETATM 1548 O O   . HOH   F 5 .   ? -5.529  -9.613  -0.664  1.00 66.96  ? 313 HOH   B O   1 
HETATM 1549 O O   . HOH   F 5 .   ? -35.511 4.156   -9.116  1.00 64.74  ? 314 HOH   B O   1 
HETATM 1550 O O   . HOH   F 5 .   ? -16.253 -15.047 -16.614 1.00 67.37  ? 315 HOH   B O   1 
HETATM 1551 O O   . HOH   F 5 .   ? -30.974 13.068  -19.283 1.00 65.52  ? 316 HOH   B O   1 
HETATM 1552 O O   . HOH   F 5 .   ? -31.326 12.499  -16.492 1.00 63.91  ? 317 HOH   B O   1 
HETATM 1553 O O   . HOH   F 5 .   ? -7.073  -9.330  -3.280  1.00 53.85  ? 318 HOH   B O   1 
HETATM 1554 O O   . HOH   F 5 .   ? -20.578 14.403  -33.425 1.00 51.72  ? 319 HOH   B O   1 
HETATM 1555 O O   . HOH   F 5 .   ? -14.653 -12.539 -16.432 1.00 51.74  ? 320 HOH   B O   1 
HETATM 1556 O O   . HOH   F 5 .   ? -3.339  -11.586 -7.078  1.00 45.42  ? 321 HOH   B O   1 
HETATM 1557 O O   . HOH   F 5 .   ? -22.754 7.550   -34.461 1.00 63.43  ? 322 HOH   B O   1 
HETATM 1558 O O   . HOH   F 5 .   ? -15.311 9.458   -0.513  1.00 70.47  ? 323 HOH   B O   1 
HETATM 1559 O O   . HOH   F 5 .   ? -7.267  -10.739 -5.560  1.00 56.81  ? 324 HOH   B O   1 
HETATM 1560 O O   . HOH   F 5 .   ? 6.514   -4.909  -16.902 1.00 62.90  ? 325 HOH   B O   1 
HETATM 1561 O O   . HOH   F 5 .   ? -21.281 -14.203 -22.270 1.00 51.51  ? 326 HOH   B O   1 
HETATM 1562 O O   . HOH   F 5 .   ? -28.180 -6.405  -18.737 1.00 55.04  ? 327 HOH   B O   1 
HETATM 1563 O O   . HOH   F 5 .   ? -16.262 -7.294  -8.233  1.00 67.64  ? 328 HOH   B O   1 
HETATM 1564 O O   . HOH   F 5 .   ? -29.837 -5.392  -1.074  1.00 42.67  ? 329 HOH   B O   1 
HETATM 1565 O O   . HOH   F 5 .   ? -29.261 -3.979  -21.987 1.00 67.40  ? 330 HOH   B O   1 
HETATM 1566 O O   . HOH   F 5 .   ? -26.836 -7.955  -16.734 1.00 58.51  ? 331 HOH   B O   1 
HETATM 1567 O O   . HOH   F 5 .   ? -25.948 -5.145  -4.275  1.00 50.38  ? 332 HOH   B O   1 
HETATM 1568 O O   . HOH   F 5 .   ? -21.733 -12.449 -13.028 1.00 54.70  ? 333 HOH   B O   1 
HETATM 1569 O O   . HOH   F 5 .   ? -14.619 -6.787  -1.786  1.00 58.74  ? 334 HOH   B O   1 
HETATM 1570 O O   . HOH   F 5 .   ? -9.742  -11.175 -7.431  1.00 58.81  ? 335 HOH   B O   1 
HETATM 1571 O O   . HOH   F 5 .   ? -19.324 -6.029  -0.630  1.00 60.84  ? 336 HOH   B O   1 
HETATM 1572 O O   . HOH   F 5 .   ? -16.391 -14.205 -31.252 1.00 61.58  ? 337 HOH   B O   1 
HETATM 1573 O O   . HOH   F 5 .   ? -22.634 -13.913 -25.793 1.00 55.07  ? 338 HOH   B O   1 
HETATM 1574 O O   . HOH   F 5 .   ? -29.534 -6.076  -27.463 1.00 71.25  ? 339 HOH   B O   1 
HETATM 1575 O O   . HOH   F 5 .   ? -18.661 26.061  -14.532 1.00 72.83  ? 340 HOH   B O   1 
HETATM 1576 O O   . HOH   F 5 .   ? -31.152 3.975   -2.080  1.00 59.71  ? 341 HOH   B O   1 
HETATM 1577 O O   . HOH   F 5 .   ? -10.563 22.413  -13.989 1.00 81.51  ? 342 HOH   B O   1 
HETATM 1578 O O   . HOH   F 5 .   ? -1.007  -14.260 -9.730  1.00 55.66  ? 343 HOH   B O   1 
HETATM 1579 O O   . HOH   F 5 .   ? -35.538 -0.304  -7.384  1.00 67.27  ? 344 HOH   B O   1 
HETATM 1580 O O   . HOH   F 5 .   ? -17.984 13.884  -31.589 1.00 59.43  ? 345 HOH   B O   1 
HETATM 1581 O O   . HOH   F 5 .   ? -23.793 -7.134  -2.741  1.00 62.27  ? 346 HOH   B O   1 
HETATM 1582 O O   . HOH   F 5 .   ? -21.377 3.646   -0.000  0.50 63.21  ? 347 HOH   B O   1 
HETATM 1583 O O   . HOH   F 5 .   ? -18.998 -12.160 -13.473 1.00 70.29  ? 348 HOH   B O   1 
HETATM 1584 O O   . HOH   F 5 .   ? -11.804 14.239  -14.545 1.00 58.20  ? 349 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   ? 1.1781 0.5023 1.0563 0.2218  -0.1165 -0.2205 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.1543 0.5727 1.0197 0.2449  -0.0937 -0.2227 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.1336 0.5642 0.9976 0.2381  -0.0724 -0.1718 50  ASP   A C   
4    O O   . ASP   A 7   ? 1.1635 0.5250 1.0161 0.2510  -0.0799 -0.1486 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.1942 0.6246 1.0428 0.2997  -0.1054 -0.2692 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.2473 0.7905 1.0926 0.3135  -0.0834 -0.2931 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.2457 0.8445 1.0932 0.2813  -0.0657 -0.2817 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.2725 0.8483 1.1143 0.3566  -0.0838 -0.3230 50  ASP   A OD2 
9    N N   . MET   A 8   ? 1.0810 0.5946 0.9507 0.2205  -0.0477 -0.1554 51  MET   A N   
10   C CA  . MET   A 8   ? 1.0584 0.5934 0.9245 0.2153  -0.0283 -0.1134 51  MET   A CA  
11   C C   . MET   A 8   ? 1.0353 0.6035 0.8892 0.2571  -0.0280 -0.1248 51  MET   A C   
12   O O   . MET   A 8   ? 1.0179 0.6279 0.8748 0.2829  -0.0325 -0.1653 51  MET   A O   
13   C CB  . MET   A 8   ? 1.0344 0.6391 0.9128 0.1823  -0.0066 -0.0959 51  MET   A CB  
14   C CG  . MET   A 8   ? 1.0505 0.6298 0.9493 0.1414  -0.0058 -0.0754 51  MET   A CG  
15   S SD  . MET   A 8   ? 1.0232 0.6844 0.9348 0.1125  0.0132  -0.0623 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.9974 0.6268 0.9453 0.0720  0.0035  -0.0542 51  MET   A CE  
17   N N   . TYR   A 9   ? 1.0290 0.5840 0.8700 0.2644  -0.0223 -0.0903 52  TYR   A N   
18   C CA  . TYR   A 9   ? 1.0150 0.6018 0.8482 0.3039  -0.0271 -0.0997 52  TYR   A CA  
19   C C   . TYR   A 9   ? 1.0007 0.6123 0.8236 0.2972  -0.0134 -0.0644 52  TYR   A C   
20   O O   . TYR   A 9   ? 1.0144 0.5918 0.8255 0.2709  -0.0021 -0.0257 52  TYR   A O   
21   C CB  . TYR   A 9   ? 1.0506 0.5634 0.8644 0.3472  -0.0540 -0.1105 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 1.1159 0.5259 0.8984 0.3410  -0.0598 -0.0661 52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 1.1597 0.4881 0.9422 0.3174  -0.0661 -0.0574 52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 1.1486 0.5386 0.8990 0.3614  -0.0608 -0.0345 52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.2162 0.4472 0.9716 0.3072  -0.0670 -0.0125 52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.2083 0.5004 0.9204 0.3567  -0.0618 0.0108  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.2496 0.4619 0.9659 0.3273  -0.0624 0.0239  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.3171 0.4320 0.9980 0.3161  -0.0578 0.0736  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.9675 0.6401 0.7971 0.3224  -0.0153 -0.0799 53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.9561 0.6518 0.7738 0.3209  -0.0078 -0.0537 53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.9834 0.6465 0.7730 0.3667  -0.0299 -0.0497 53  ILE   A C   
32   O O   . ILE   A 10  ? 0.9840 0.6392 0.7782 0.4046  -0.0515 -0.0784 53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.9068 0.6966 0.7546 0.3042  0.0070  -0.0688 53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.8766 0.7305 0.7557 0.3307  -0.0014 -0.1118 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.8964 0.7055 0.7569 0.2616  0.0266  -0.0633 53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.8466 0.7831 0.7550 0.3140  0.0121  -0.1204 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 1.0038 0.6467 0.7600 0.3665  -0.0255 -0.0145 54  GLU   A N   
38   C CA  . GLU   A 11  ? 1.0386 0.6475 0.7539 0.4105  -0.0470 -0.0049 54  GLU   A CA  
39   C C   . GLU   A 11  ? 1.0328 0.6912 0.7395 0.4089  -0.0412 0.0043  54  GLU   A C   
40   O O   . GLU   A 11  ? 1.0366 0.7017 0.7379 0.3747  -0.0170 0.0299  54  GLU   A O   
41   C CB  . GLU   A 11  ? 1.1200 0.6215 0.7783 0.4140  -0.0466 0.0397  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.2144 0.6399 0.8684 0.4263  -0.0622 0.0330  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.3685 0.6806 0.9667 0.4230  -0.0588 0.0830  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.3827 0.6855 0.9548 0.3980  -0.0336 0.1250  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.4532 0.6840 1.0336 0.4457  -0.0802 0.0802  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 1.0186 0.7080 0.7230 0.4486  -0.0664 -0.0176 55  ARG   A N   
47   C CA  . ARG   A 12  ? 1.0083 0.7413 0.7048 0.4505  -0.0676 -0.0157 55  ARG   A CA  
48   C C   . ARG   A 12  ? 1.0665 0.7376 0.6927 0.4519  -0.0571 0.0310  55  ARG   A C   
49   O O   . ARG   A 12  ? 1.1211 0.7129 0.6937 0.4740  -0.0635 0.0577  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.9941 0.7704 0.7061 0.4957  -0.1031 -0.0528 55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.9918 0.8263 0.7144 0.4921  -0.1082 -0.0637 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.9522 0.8828 0.7550 0.4907  -0.1207 -0.1135 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.9428 0.9249 0.7671 0.4696  -0.1189 -0.1223 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.9713 0.9530 0.7667 0.4975  -0.1453 -0.1275 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.0086 0.9411 0.7450 0.5488  -0.1741 -0.1208 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.9399 0.9628 0.7581 0.4759  -0.1448 -0.1387 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 1.0573 0.7612 0.6816 0.4283  -0.0389 0.0421  56  ALA   A N   
58   C CA  . ALA   A 13  ? 1.1064 0.7659 0.6653 0.4309  -0.0237 0.0836  56  ALA   A CA  
59   C C   . ALA   A 13  ? 1.1193 0.8094 0.6485 0.4574  -0.0390 0.0734  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.1558 0.8105 0.6195 0.4697  -0.0285 0.1047  56  ALA   A O   
61   C CB  . ALA   A 13  ? 1.1040 0.7654 0.6791 0.3822  0.0144  0.1096  56  ALA   A CB  
62   N N   . GLY   A 14  ? 1.0876 0.8440 0.6655 0.4643  -0.0621 0.0298  57  GLY   A N   
63   C CA  . GLY   A 14  ? 1.0965 0.8811 0.6535 0.4892  -0.0838 0.0126  57  GLY   A CA  
64   C C   . GLY   A 14  ? 1.0577 0.9194 0.6854 0.4658  -0.0903 -0.0258 57  GLY   A C   
65   O O   . GLY   A 14  ? 1.0249 0.9232 0.7173 0.4296  -0.0753 -0.0380 57  GLY   A O   
66   N N   . ASP   A 15  ? 1.0585 0.9415 0.6704 0.4873  -0.1142 -0.0454 58  ASP   A N   
67   C CA  . ASP   A 15  ? 1.0244 0.9706 0.7000 0.4647  -0.1241 -0.0811 58  ASP   A CA  
68   C C   . ASP   A 15  ? 1.0410 0.9840 0.7110 0.4303  -0.0955 -0.0633 58  ASP   A C   
69   O O   . ASP   A 15  ? 1.0757 0.9763 0.6840 0.4363  -0.0752 -0.0294 58  ASP   A O   
70   C CB  . ASP   A 15  ? 1.0373 1.0020 0.6989 0.5047  -0.1687 -0.1144 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 1.0799 1.0706 0.7706 0.5393  -0.2062 -0.1463 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 1.0808 1.0702 0.7970 0.5366  -0.1967 -0.1418 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 1.0981 1.1102 0.7853 0.5730  -0.2481 -0.1786 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 1.0129 1.0009 0.7468 0.3959  -0.0942 -0.0862 59  ILE   A N   
75   C CA  . ILE   A 16  ? 1.0306 1.0128 0.7601 0.3685  -0.0738 -0.0735 59  ILE   A CA  
76   C C   . ILE   A 16  ? 1.0527 1.0458 0.7769 0.3828  -0.1021 -0.1016 59  ILE   A C   
77   O O   . ILE   A 16  ? 1.0175 1.0471 0.8029 0.3621  -0.1181 -0.1324 59  ILE   A O   
78   C CB  . ILE   A 16  ? 1.0056 1.0098 0.7927 0.3193  -0.0480 -0.0688 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 1.0238 1.0084 0.8039 0.3111  -0.0238 -0.0427 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 1.0159 1.0102 0.7959 0.2977  -0.0337 -0.0580 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 1.0139 1.0216 0.8433 0.2708  -0.0035 -0.0427 59  ILE   A CD1 
82   N N   . THR   A 17  ? 1.1102 1.0701 0.7581 0.4207  -0.1097 -0.0921 60  THR   A N   
83   C CA  . THR   A 17  ? 1.1425 1.1023 0.7651 0.4447  -0.1391 -0.1194 60  THR   A CA  
84   C C   . THR   A 17  ? 1.1912 1.1181 0.7440 0.4585  -0.1172 -0.0952 60  THR   A C   
85   O O   . THR   A 17  ? 1.2149 1.1167 0.7207 0.4653  -0.0863 -0.0565 60  THR   A O   
86   C CB  . THR   A 17  ? 1.1784 1.1375 0.7652 0.4953  -0.1813 -0.1433 60  THR   A CB  
87   O OG1 . THR   A 17  ? 1.2412 1.1561 0.7384 0.5321  -0.1687 -0.1082 60  THR   A OG1 
88   C CG2 . THR   A 17  ? 1.1431 1.1456 0.8046 0.4894  -0.2066 -0.1733 60  THR   A CG2 
89   N N   . TRP   A 18  ? 1.2054 1.1330 0.7520 0.4648  -0.1343 -0.1201 61  TRP   A N   
90   C CA  . TRP   A 18  ? 1.2580 1.1620 0.7384 0.4860  -0.1166 -0.1055 61  TRP   A CA  
91   C C   . TRP   A 18  ? 1.3236 1.2061 0.7098 0.5438  -0.1317 -0.1049 61  TRP   A C   
92   O O   . TRP   A 18  ? 1.3205 1.2077 0.6995 0.5712  -0.1755 -0.1381 61  TRP   A O   
93   C CB  . TRP   A 18  ? 1.2480 1.1544 0.7547 0.4765  -0.1357 -0.1385 61  TRP   A CB  
94   C CG  . TRP   A 18  ? 1.2863 1.1736 0.7286 0.5059  -0.1248 -0.1358 61  TRP   A CG  
95   C CD1 . TRP   A 18  ? 1.3288 1.2022 0.6980 0.5569  -0.1486 -0.1585 61  TRP   A CD1 
96   C CD2 . TRP   A 18  ? 1.2859 1.1705 0.7371 0.4882  -0.0930 -0.1178 61  TRP   A CD2 
97   N NE1 . TRP   A 18  ? 1.3495 1.2137 0.6790 0.5731  -0.1280 -0.1537 61  TRP   A NE1 
98   C CE2 . TRP   A 18  ? 1.3237 1.1963 0.7072 0.5316  -0.0951 -0.1297 61  TRP   A CE2 
99   C CE3 . TRP   A 18  ? 1.2684 1.1615 0.7744 0.4444  -0.0639 -0.0936 61  TRP   A CE3 
100  C CZ2 . TRP   A 18  ? 1.3314 1.2049 0.7090 0.5323  -0.0683 -0.1195 61  TRP   A CZ2 
101  C CZ3 . TRP   A 18  ? 1.2820 1.1727 0.7816 0.4447  -0.0423 -0.0838 61  TRP   A CZ3 
102  C CH2 . TRP   A 18  ? 1.3079 1.1915 0.7471 0.4884  -0.0432 -0.0963 61  TRP   A CH2 
103  N N   . GLU   A 19  ? 1.3808 1.2418 0.6949 0.5627  -0.0957 -0.0672 62  GLU   A N   
104  C CA  . GLU   A 19  ? 1.4564 1.2915 0.6659 0.6184  -0.1030 -0.0592 62  GLU   A CA  
105  C C   . GLU   A 19  ? 1.5074 1.3395 0.6563 0.6508  -0.1029 -0.0752 62  GLU   A C   
106  O O   . GLU   A 19  ? 1.5086 1.3460 0.6513 0.6393  -0.0612 -0.0519 62  GLU   A O   
107  C CB  . GLU   A 19  ? 1.5172 1.3263 0.6774 0.6194  -0.0589 -0.0020 62  GLU   A CB  
108  C CG  . GLU   A 19  ? 1.6512 1.4256 0.6901 0.6768  -0.0613 0.0144  62  GLU   A CG  
109  C CD  . GLU   A 19  ? 1.7740 1.5217 0.7497 0.6767  -0.0045 0.0751  62  GLU   A CD  
110  O OE1 . GLU   A 19  ? 1.7795 1.5304 0.8129 0.6305  0.0313  0.1064  62  GLU   A OE1 
111  O OE2 . GLU   A 19  ? 1.8388 1.5627 0.7067 0.7222  0.0044  0.0910  62  GLU   A OE2 
112  N N   . LYS   A 20  ? 1.5477 1.3739 0.6523 0.6944  -0.1506 -0.1174 63  LYS   A N   
113  C CA  . LYS   A 20  ? 1.6047 1.4242 0.6396 0.7339  -0.1541 -0.1377 63  LYS   A CA  
114  C C   . LYS   A 20  ? 1.6804 1.4810 0.6035 0.7711  -0.1117 -0.0924 63  LYS   A C   
115  O O   . LYS   A 20  ? 1.7087 1.4873 0.5813 0.7890  -0.1114 -0.0656 63  LYS   A O   
116  C CB  . LYS   A 20  ? 1.6419 1.4561 0.6501 0.7754  -0.2211 -0.1969 63  LYS   A CB  
117  C CG  . LYS   A 20  ? 1.6542 1.4883 0.7742 0.7385  -0.2665 -0.2436 63  LYS   A CG  
118  C CD  . LYS   A 20  ? 1.7190 1.5496 0.8128 0.7812  -0.3350 -0.3048 63  LYS   A CD  
119  C CE  . LYS   A 20  ? 1.7190 1.5758 0.9291 0.7436  -0.3810 -0.3485 63  LYS   A CE  
120  N NZ  . LYS   A 20  ? 1.7581 1.6134 0.9515 0.7824  -0.4507 -0.4133 63  LYS   A NZ  
121  N N   . ASP   A 21  ? 1.7128 1.5211 0.5961 0.7843  -0.0758 -0.0837 64  ASP   A N   
122  C CA  . ASP   A 21  ? 1.7747 1.5732 0.5536 0.8167  -0.0266 -0.0390 64  ASP   A CA  
123  C C   . ASP   A 21  ? 1.7728 1.5691 0.5779 0.7752  0.0283  0.0250  64  ASP   A C   
124  O O   . ASP   A 21  ? 1.8139 1.5830 0.5378 0.7951  0.0534  0.0676  64  ASP   A O   
125  C CB  . ASP   A 21  ? 1.8628 1.6299 0.5160 0.8827  -0.0564 -0.0475 64  ASP   A CB  
126  C CG  . ASP   A 21  ? 1.9683 1.7373 0.5645 0.9349  -0.0963 -0.1051 64  ASP   A CG  
127  O OD1 . ASP   A 21  ? 1.9866 1.7764 0.5833 0.9391  -0.0709 -0.1159 64  ASP   A OD1 
128  O OD2 . ASP   A 21  ? 2.0155 1.7656 0.5665 0.9748  -0.1556 -0.1424 64  ASP   A OD2 
129  N N   . ALA   A 22  ? 1.7226 1.5422 0.6377 0.7179  0.0445  0.0313  65  ALA   A N   
130  C CA  . ALA   A 22  ? 1.7104 1.5304 0.6634 0.6745  0.0927  0.0846  65  ALA   A CA  
131  C C   . ALA   A 22  ? 1.7066 1.5564 0.6490 0.6696  0.1532  0.1135  65  ALA   A C   
132  O O   . ALA   A 22  ? 1.7036 1.5775 0.6270 0.6959  0.1536  0.0861  65  ALA   A O   
133  C CB  . ALA   A 22  ? 1.6635 1.4972 0.7347 0.6195  0.0784  0.0737  65  ALA   A CB  
134  N N   . GLU   A 23  ? 1.7007 1.5503 0.6581 0.6373  0.2031  0.1662  66  GLU   A N   
135  C CA  . GLU   A 23  ? 1.6883 1.5763 0.6522 0.6259  0.2642  0.1962  66  GLU   A CA  
136  C C   . GLU   A 23  ? 1.6236 1.5616 0.6856 0.5996  0.2644  0.1681  66  GLU   A C   
137  O O   . GLU   A 23  ? 1.5898 1.5342 0.7419 0.5522  0.2597  0.1714  66  GLU   A O   
138  C CB  . GLU   A 23  ? 1.7335 1.6056 0.7133 0.5862  0.3091  0.2554  66  GLU   A CB  
139  C CG  . GLU   A 23  ? 1.8015 1.7176 0.7914 0.5707  0.3772  0.2916  66  GLU   A CG  
140  C CD  . GLU   A 23  ? 1.8882 1.8011 0.9452 0.5124  0.4142  0.3376  66  GLU   A CD  
141  O OE1 . GLU   A 23  ? 1.9093 1.7776 0.9950 0.4871  0.3871  0.3433  66  GLU   A OE1 
142  O OE2 . GLU   A 23  ? 1.8997 1.8580 0.9850 0.4925  0.4697  0.3651  66  GLU   A OE2 
143  N N   . VAL   A 24  ? 1.6053 1.5748 0.6431 0.6347  0.2679  0.1396  67  VAL   A N   
144  C CA  . VAL   A 24  ? 1.5565 1.5669 0.6736 0.6211  0.2646  0.1112  67  VAL   A CA  
145  C C   . VAL   A 24  ? 1.5198 1.5853 0.6792 0.6006  0.3256  0.1438  67  VAL   A C   
146  O O   . VAL   A 24  ? 1.5311 1.6262 0.6354 0.6325  0.3657  0.1551  67  VAL   A O   
147  C CB  . VAL   A 24  ? 1.5692 1.5814 0.6477 0.6708  0.2315  0.0581  67  VAL   A CB  
148  C CG1 . VAL   A 24  ? 1.5396 1.5696 0.7063 0.6507  0.2107  0.0273  67  VAL   A CG1 
149  C CG2 . VAL   A 24  ? 1.6069 1.5702 0.6271 0.6998  0.1756  0.0264  67  VAL   A CG2 
150  N N   . THR   A 25  ? 1.4709 1.5551 0.7289 0.5487  0.3330  0.1570  68  THR   A N   
151  C CA  . THR   A 25  ? 1.4285 1.5718 0.7441 0.5243  0.3859  0.1843  68  THR   A CA  
152  C C   . THR   A 25  ? 1.3767 1.5463 0.8017 0.4866  0.3693  0.1691  68  THR   A C   
153  O O   . THR   A 25  ? 1.3801 1.5140 0.8321 0.4702  0.3240  0.1492  68  THR   A O   
154  C CB  . THR   A 25  ? 1.4535 1.5850 0.7572 0.4940  0.4291  0.2396  68  THR   A CB  
155  O OG1 . THR   A 25  ? 1.4267 1.6242 0.7894 0.4712  0.4832  0.2635  68  THR   A OG1 
156  C CG2 . THR   A 25  ? 1.4564 1.5420 0.8043 0.4496  0.4022  0.2509  68  THR   A CG2 
157  N N   . GLY   A 26  ? 1.3256 1.5603 0.8123 0.4742  0.4059  0.1785  69  GLY   A N   
158  C CA  . GLY   A 26  ? 1.2775 1.5389 0.8630 0.4424  0.3892  0.1656  69  GLY   A CA  
159  C C   . GLY   A 26  ? 1.2481 1.5408 0.8540 0.4759  0.3699  0.1255  69  GLY   A C   
160  O O   . GLY   A 26  ? 1.2779 1.5444 0.8234 0.5190  0.3453  0.0957  69  GLY   A O   
161  N N   . ASN   A 27  ? 1.1878 1.5333 0.8795 0.4582  0.3767  0.1222  70  ASN   A N   
162  C CA  . ASN   A 27  ? 1.1626 1.5355 0.8785 0.4923  0.3557  0.0848  70  ASN   A CA  
163  C C   . ASN   A 27  ? 1.1505 1.4734 0.8955 0.4775  0.2981  0.0624  70  ASN   A C   
164  O O   . ASN   A 27  ? 1.1656 1.4427 0.9147 0.4402  0.2792  0.0753  70  ASN   A O   
165  C CB  . ASN   A 27  ? 1.1264 1.5954 0.9133 0.4949  0.3967  0.0894  70  ASN   A CB  
166  C CG  . ASN   A 27  ? 1.1312 1.6349 1.0109 0.4408  0.4073  0.1121  70  ASN   A CG  
167  O OD1 . ASN   A 27  ? 1.1619 1.6187 1.0468 0.3985  0.3943  0.1315  70  ASN   A OD1 
168  N ND2 . ASN   A 27  ? 1.0847 1.6752 1.0427 0.4432  0.4299  0.1066  70  ASN   A ND2 
169  N N   . SER   A 28  ? 1.1269 1.4527 0.8835 0.5101  0.2703  0.0288  71  SER   A N   
170  C CA  . SER   A 28  ? 1.1245 1.3976 0.8999 0.4991  0.2186  0.0110  71  SER   A CA  
171  C C   . SER   A 28  ? 1.0666 1.3874 0.9128 0.5041  0.2123  0.0016  71  SER   A C   
172  O O   . SER   A 28  ? 1.0686 1.3876 0.9104 0.5456  0.1913  -0.0275 71  SER   A O   
173  C CB  . SER   A 28  ? 1.1796 1.3904 0.8943 0.5360  0.1808  -0.0221 71  SER   A CB  
174  O OG  . SER   A 28  ? 1.2366 1.4229 0.8831 0.5495  0.1883  -0.0223 71  SER   A OG  
175  N N   . PRO   A 29  ? 1.0158 1.3783 0.9281 0.4651  0.2268  0.0232  72  PRO   A N   
176  C CA  . PRO   A 29  ? 0.9683 1.3850 0.9517 0.4736  0.2178  0.0114  72  PRO   A CA  
177  C C   . PRO   A 29  ? 0.9754 1.3386 0.9687 0.4650  0.1659  0.0013  72  PRO   A C   
178  O O   . PRO   A 29  ? 1.0039 1.3053 0.9733 0.4314  0.1470  0.0135  72  PRO   A O   
179  C CB  . PRO   A 29  ? 0.9306 1.4195 0.9818 0.4350  0.2572  0.0372  72  PRO   A CB  
180  C CG  . PRO   A 29  ? 0.9635 1.4018 0.9789 0.3937  0.2672  0.0648  72  PRO   A CG  
181  C CD  . PRO   A 29  ? 1.0005 1.3648 0.9276 0.4155  0.2502  0.0562  72  PRO   A CD  
182  N N   . ARG   A 30  ? 0.9487 1.3375 0.9761 0.4971  0.1439  -0.0202 73  ARG   A N   
183  C CA  . ARG   A 30  ? 0.9624 1.2983 0.9929 0.4924  0.0949  -0.0259 73  ARG   A CA  
184  C C   . ARG   A 30  ? 0.8924 1.2929 1.0005 0.4708  0.0947  -0.0188 73  ARG   A C   
185  O O   . ARG   A 30  ? 0.8488 1.3247 1.0145 0.4989  0.0984  -0.0346 73  ARG   A O   
186  C CB  . ARG   A 30  ? 1.0158 1.3165 1.0211 0.5466  0.0600  -0.0553 73  ARG   A CB  
187  C CG  . ARG   A 30  ? 1.1334 1.3604 1.0637 0.5653  0.0515  -0.0671 73  ARG   A CG  
188  C CD  . ARG   A 30  ? 1.2304 1.4015 1.1341 0.6138  0.0090  -0.0961 73  ARG   A CD  
189  N NE  . ARG   A 30  ? 1.3251 1.4459 1.1679 0.6410  0.0043  -0.1168 73  ARG   A NE  
190  C CZ  . ARG   A 30  ? 1.4095 1.4370 1.2022 0.6207  -0.0207 -0.1156 73  ARG   A CZ  
191  N NH1 . ARG   A 30  ? 1.4241 1.3998 1.2172 0.5733  -0.0382 -0.0922 73  ARG   A NH1 
192  N NH2 . ARG   A 30  ? 1.4368 1.4257 1.1804 0.6483  -0.0286 -0.1401 73  ARG   A NH2 
193  N N   . LEU   A 31  ? 0.8754 1.2519 0.9884 0.4219  0.0904  0.0018  74  LEU   A N   
194  C CA  . LEU   A 31  ? 0.8181 1.2497 1.0017 0.3963  0.0868  0.0064  74  LEU   A CA  
195  C C   . LEU   A 31  ? 0.8223 1.2041 0.9931 0.3961  0.0361  0.0018  74  LEU   A C   
196  O O   . LEU   A 31  ? 0.8769 1.1720 0.9827 0.3848  0.0162  0.0103  74  LEU   A O   
197  C CB  . LEU   A 31  ? 0.8118 1.2509 1.0085 0.3439  0.1168  0.0304  74  LEU   A CB  
198  C CG  . LEU   A 31  ? 0.8192 1.2923 1.0132 0.3400  0.1683  0.0432  74  LEU   A CG  
199  C CD1 . LEU   A 31  ? 0.8299 1.2856 1.0232 0.2913  0.1892  0.0681  74  LEU   A CD1 
200  C CD2 . LEU   A 31  ? 0.7724 1.3495 1.0385 0.3583  0.1988  0.0353  74  LEU   A CD2 
201  N N   . ASP   A 32  ? 0.7588 1.1978 0.9917 0.4084  0.0156  -0.0113 75  ASP   A N   
202  C CA  . ASP   A 32  ? 0.7611 1.1554 0.9764 0.4115  -0.0339 -0.0142 75  ASP   A CA  
203  C C   . ASP   A 32  ? 0.7200 1.1252 0.9594 0.3634  -0.0340 -0.0025 75  ASP   A C   
204  O O   . ASP   A 32  ? 0.6712 1.1598 0.9920 0.3502  -0.0242 -0.0097 75  ASP   A O   
205  C CB  . ASP   A 32  ? 0.7542 1.2026 1.0197 0.4580  -0.0639 -0.0388 75  ASP   A CB  
206  C CG  . ASP   A 32  ? 0.8582 1.2633 1.0796 0.5119  -0.0812 -0.0529 75  ASP   A CG  
207  O OD1 . ASP   A 32  ? 0.9000 1.2729 1.0794 0.5158  -0.0560 -0.0498 75  ASP   A OD1 
208  O OD2 . ASP   A 32  ? 0.8882 1.2882 1.1152 0.5530  -0.1236 -0.0692 75  ASP   A OD2 
209  N N   . VAL   A 33  ? 0.7359 1.0602 0.9090 0.3362  -0.0434 0.0135  76  VAL   A N   
210  C CA  . VAL   A 33  ? 0.7060 1.0341 0.8931 0.2933  -0.0427 0.0215  76  VAL   A CA  
211  C C   . VAL   A 33  ? 0.7185 0.9923 0.8589 0.2924  -0.0859 0.0221  76  VAL   A C   
212  O O   . VAL   A 33  ? 0.7565 0.9720 0.8402 0.3193  -0.1129 0.0239  76  VAL   A O   
213  C CB  . VAL   A 33  ? 0.7220 1.0210 0.8817 0.2573  -0.0057 0.0393  76  VAL   A CB  
214  C CG1 . VAL   A 33  ? 0.6916 1.0476 0.8949 0.2556  0.0377  0.0423  76  VAL   A CG1 
215  C CG2 . VAL   A 33  ? 0.7790 0.9918 0.8544 0.2607  -0.0106 0.0491  76  VAL   A CG2 
216  N N   . ALA   A 34  ? 0.6847 0.9761 0.8477 0.2625  -0.0927 0.0204  77  ALA   A N   
217  C CA  . ALA   A 34  ? 0.7024 0.9495 0.8176 0.2578  -0.1283 0.0205  77  ALA   A CA  
218  C C   . ALA   A 34  ? 0.6999 0.9215 0.7931 0.2160  -0.1085 0.0296  77  ALA   A C   
219  O O   . ALA   A 34  ? 0.6680 0.9301 0.8150 0.1906  -0.0813 0.0282  77  ALA   A O   
220  C CB  . ALA   A 34  ? 0.6649 0.9722 0.8395 0.2702  -0.1639 -0.0014 77  ALA   A CB  
221  N N   . LEU   A 35  ? 0.7319 0.8857 0.7455 0.2096  -0.1205 0.0396  78  LEU   A N   
222  C CA  . LEU   A 35  ? 0.7338 0.8654 0.7239 0.1759  -0.1037 0.0443  78  LEU   A CA  
223  C C   . LEU   A 35  ? 0.7456 0.8667 0.7074 0.1739  -0.1365 0.0339  78  LEU   A C   
224  O O   . LEU   A 35  ? 0.7792 0.8590 0.6770 0.1935  -0.1625 0.0396  78  LEU   A O   
225  C CB  . LEU   A 35  ? 0.7656 0.8359 0.6892 0.1675  -0.0818 0.0628  78  LEU   A CB  
226  C CG  . LEU   A 35  ? 0.7766 0.8299 0.6794 0.1379  -0.0629 0.0650  78  LEU   A CG  
227  C CD1 . LEU   A 35  ? 0.7527 0.8417 0.7128 0.1207  -0.0360 0.0615  78  LEU   A CD1 
228  C CD2 . LEU   A 35  ? 0.8131 0.8120 0.6522 0.1317  -0.0488 0.0803  78  LEU   A CD2 
229  N N   . ASP   A 36  ? 0.7151 0.8690 0.7207 0.1518  -0.1370 0.0184  79  ASP   A N   
230  C CA  . ASP   A 36  ? 0.7266 0.8723 0.7043 0.1520  -0.1707 0.0025  79  ASP   A CA  
231  C C   . ASP   A 36  ? 0.7716 0.8654 0.6749 0.1354  -0.1562 0.0093  79  ASP   A C   
232  O O   . ASP   A 36  ? 0.7810 0.8548 0.6727 0.1199  -0.1203 0.0234  79  ASP   A O   
233  C CB  . ASP   A 36  ? 0.6891 0.8973 0.7566 0.1403  -0.1895 -0.0248 79  ASP   A CB  
234  C CG  . ASP   A 36  ? 0.7175 0.9395 0.8369 0.1041  -0.1621 -0.0296 79  ASP   A CG  
235  O OD1 . ASP   A 36  ? 0.7498 0.9315 0.8274 0.0905  -0.1317 -0.0151 79  ASP   A OD1 
236  O OD2 . ASP   A 36  ? 0.7007 0.9729 0.9049 0.0894  -0.1725 -0.0483 79  ASP   A OD2 
237  N N   . GLU   A 37  ? 0.7918 0.8682 0.6443 0.1422  -0.1854 -0.0031 80  GLU   A N   
238  C CA  . GLU   A 37  ? 0.8312 0.8681 0.6109 0.1320  -0.1745 -0.0020 80  GLU   A CA  
239  C C   . GLU   A 37  ? 0.8118 0.8595 0.6320 0.1046  -0.1475 -0.0126 80  GLU   A C   
240  O O   . GLU   A 37  ? 0.8387 0.8585 0.6087 0.0967  -0.1273 -0.0090 80  GLU   A O   
241  C CB  . GLU   A 37  ? 0.8852 0.9133 0.6121 0.1490  -0.2159 -0.0203 80  GLU   A CB  
242  C CG  . GLU   A 37  ? 1.0252 0.9988 0.6358 0.1586  -0.2100 -0.0019 80  GLU   A CG  
243  C CD  . GLU   A 37  ? 1.1626 1.1270 0.7099 0.1748  -0.2451 -0.0231 80  GLU   A CD  
244  O OE1 . GLU   A 37  ? 1.1613 1.1538 0.7500 0.1674  -0.2610 -0.0566 80  GLU   A OE1 
245  O OE2 . GLU   A 37  ? 1.2483 1.1726 0.7005 0.1956  -0.2582 -0.0061 80  GLU   A OE2 
246  N N   . SER   A 38  ? 0.7630 0.8497 0.6730 0.0907  -0.1455 -0.0242 81  SER   A N   
247  C CA  . SER   A 38  ? 0.7534 0.8390 0.6989 0.0663  -0.1216 -0.0301 81  SER   A CA  
248  C C   . SER   A 38  ? 0.7510 0.8314 0.7122 0.0579  -0.0802 -0.0057 81  SER   A C   
249  O O   . SER   A 38  ? 0.7467 0.8230 0.7373 0.0410  -0.0606 -0.0066 81  SER   A O   
250  C CB  . SER   A 38  ? 0.7332 0.8541 0.7634 0.0509  -0.1401 -0.0528 81  SER   A CB  
251  O OG  . SER   A 38  ? 0.7773 0.9029 0.7918 0.0609  -0.1838 -0.0806 81  SER   A OG  
252  N N   . GLY   A 39  ? 0.7500 0.8248 0.6872 0.0720  -0.0708 0.0144  82  GLY   A N   
253  C CA  . GLY   A 39  ? 0.7437 0.8132 0.6887 0.0695  -0.0382 0.0335  82  GLY   A CA  
254  C C   . GLY   A 39  ? 0.7028 0.8103 0.7209 0.0650  -0.0255 0.0369  82  GLY   A C   
255  O O   . GLY   A 39  ? 0.7085 0.8116 0.7337 0.0608  0.0026  0.0497  82  GLY   A O   
256  N N   . ASP   A 40  ? 0.6613 0.8099 0.7339 0.0669  -0.0455 0.0253  83  ASP   A N   
257  C CA  . ASP   A 40  ? 0.6176 0.8146 0.7687 0.0599  -0.0301 0.0281  83  ASP   A CA  
258  C C   . ASP   A 40  ? 0.6071 0.8351 0.7722 0.0860  -0.0327 0.0327  83  ASP   A C   
259  O O   . ASP   A 40  ? 0.6097 0.8435 0.7626 0.1062  -0.0647 0.0228  83  ASP   A O   
260  C CB  . ASP   A 40  ? 0.5952 0.8278 0.8156 0.0407  -0.0495 0.0080  83  ASP   A CB  
261  C CG  . ASP   A 40  ? 0.6529 0.8513 0.8673 0.0158  -0.0475 0.0003  83  ASP   A CG  
262  O OD1 . ASP   A 40  ? 0.6740 0.8359 0.8550 0.0103  -0.0207 0.0150  83  ASP   A OD1 
263  O OD2 . ASP   A 40  ? 0.6732 0.8806 0.9170 0.0047  -0.0762 -0.0233 83  ASP   A OD2 
264  N N   . PHE   A 41  ? 0.5955 0.8419 0.7823 0.0895  -0.0007 0.0466  84  PHE   A N   
265  C CA  . PHE   A 41  ? 0.5901 0.8683 0.7919 0.1185  -0.0009 0.0471  84  PHE   A CA  
266  C C   . PHE   A 41  ? 0.5658 0.9238 0.8619 0.1168  -0.0006 0.0360  84  PHE   A C   
267  O O   . PHE   A 41  ? 0.5359 0.9227 0.8893 0.0868  0.0158  0.0366  84  PHE   A O   
268  C CB  . PHE   A 41  ? 0.5895 0.8504 0.7613 0.1290  0.0316  0.0630  84  PHE   A CB  
269  C CG  . PHE   A 41  ? 0.6325 0.8266 0.7233 0.1375  0.0268  0.0700  84  PHE   A CG  
270  C CD1 . PHE   A 41  ? 0.6573 0.8270 0.7106 0.1643  0.0069  0.0680  84  PHE   A CD1 
271  C CD2 . PHE   A 41  ? 0.6588 0.8148 0.7156 0.1186  0.0425  0.0783  84  PHE   A CD2 
272  C CE1 . PHE   A 41  ? 0.7047 0.8135 0.6923 0.1656  0.0050  0.0757  84  PHE   A CE1 
273  C CE2 . PHE   A 41  ? 0.6986 0.8043 0.6941 0.1233  0.0400  0.0827  84  PHE   A CE2 
274  C CZ  . PHE   A 41  ? 0.7138 0.7965 0.6773 0.1437  0.0226  0.0822  84  PHE   A CZ  
275  N N   . SER   A 42  ? 0.5768 0.9707 0.8928 0.1485  -0.0192 0.0253  85  SER   A N   
276  C CA  . SER   A 42  ? 0.5563 1.0401 0.9718 0.1508  -0.0187 0.0112  85  SER   A CA  
277  C C   . SER   A 42  ? 0.5840 1.1036 1.0094 0.1914  -0.0115 0.0082  85  SER   A C   
278  O O   . SER   A 42  ? 0.6324 1.0996 0.9871 0.2226  -0.0284 0.0100  85  SER   A O   
279  C CB  . SER   A 42  ? 0.5582 1.0690 1.0132 0.1490  -0.0656 -0.0130 85  SER   A CB  
280  O OG  . SER   A 42  ? 0.6331 1.0966 1.0175 0.1803  -0.1084 -0.0196 85  SER   A OG  
281  N N   . LEU   A 43  ? 0.5518 1.1585 1.0641 0.1908  0.0159  0.0038  86  LEU   A N   
282  C CA  . LEU   A 43  ? 0.5681 1.2163 1.0921 0.2343  0.0250  -0.0035 86  LEU   A CA  
283  C C   . LEU   A 43  ? 0.5724 1.2663 1.1380 0.2711  -0.0201 -0.0307 86  LEU   A C   
284  O O   . LEU   A 43  ? 0.5161 1.2930 1.1785 0.2610  -0.0299 -0.0482 86  LEU   A O   
285  C CB  . LEU   A 43  ? 0.5286 1.2510 1.1143 0.2244  0.0811  0.0054  86  LEU   A CB  
286  C CG  . LEU   A 43  ? 0.5948 1.2635 1.1114 0.2140  0.1238  0.0318  86  LEU   A CG  
287  C CD1 . LEU   A 43  ? 0.5618 1.3045 1.1327 0.2052  0.1808  0.0438  86  LEU   A CD1 
288  C CD2 . LEU   A 43  ? 0.6590 1.2594 1.0809 0.2550  0.1106  0.0305  86  LEU   A CD2 
289  N N   . VAL   A 44  ? 0.6380 1.2749 1.1317 0.3140  -0.0501 -0.0348 87  VAL   A N   
290  C CA  . VAL   A 44  ? 0.6521 1.3143 1.1661 0.3598  -0.0981 -0.0588 87  VAL   A CA  
291  C C   . VAL   A 44  ? 0.6334 1.3786 1.2090 0.3987  -0.0772 -0.0746 87  VAL   A C   
292  O O   . VAL   A 44  ? 0.6504 1.3855 1.1976 0.4053  -0.0367 -0.0640 87  VAL   A O   
293  C CB  . VAL   A 44  ? 0.7376 1.2864 1.1379 0.3870  -0.1378 -0.0513 87  VAL   A CB  
294  C CG1 . VAL   A 44  ? 0.7404 1.2994 1.1454 0.4460  -0.1841 -0.0723 87  VAL   A CG1 
295  C CG2 . VAL   A 44  ? 0.7826 1.2679 1.1300 0.3545  -0.1609 -0.0404 87  VAL   A CG2 
296  N N   . GLU   A 45  ? 0.5932 1.4265 1.2551 0.4263  -0.1045 -0.1026 88  GLU   A N   
297  C CA  . GLU   A 45  ? 0.5666 1.4918 1.2954 0.4692  -0.0865 -0.1231 88  GLU   A CA  
298  C C   . GLU   A 45  ? 0.5707 1.5091 1.3113 0.5311  -0.1472 -0.1528 88  GLU   A C   
299  O O   . GLU   A 45  ? 0.5691 1.5308 1.3132 0.5850  -0.1466 -0.1692 88  GLU   A O   
300  C CB  . GLU   A 45  ? 0.5251 1.5849 1.3855 0.4359  -0.0414 -0.1294 88  GLU   A CB  
301  C CG  . GLU   A 45  ? 0.6205 1.6657 1.4674 0.3802  0.0216  -0.0974 88  GLU   A CG  
302  C CD  . GLU   A 45  ? 0.7153 1.7713 1.5317 0.4004  0.0766  -0.0865 88  GLU   A CD  
303  O OE1 . GLU   A 45  ? 0.6752 1.8237 1.5523 0.4401  0.0917  -0.1076 88  GLU   A OE1 
304  O OE2 . GLU   A 45  ? 0.7950 1.7705 1.5267 0.3791  0.1035  -0.0594 88  GLU   A OE2 
305  N N   . GLY   B 7   ? 1.0783 1.0541 0.9890 0.2977  0.0410  -0.1110 16  GLY   B N   
306  C CA  . GLY   B 7   ? 1.0884 1.0452 0.9998 0.3173  0.0258  -0.1109 16  GLY   B CA  
307  C C   . GLY   B 7   ? 1.0828 1.0480 1.0045 0.3121  0.0133  -0.1012 16  GLY   B C   
308  O O   . GLY   B 7   ? 1.0662 1.0713 1.0200 0.3113  0.0100  -0.1047 16  GLY   B O   
309  N N   . GLU   B 8   ? 1.0896 1.0181 0.9848 0.3090  0.0057  -0.0892 17  GLU   B N   
310  C CA  . GLU   B 8   ? 1.0776 1.0092 0.9754 0.3072  -0.0074 -0.0818 17  GLU   B CA  
311  C C   . GLU   B 8   ? 1.0562 1.0022 0.9576 0.2829  -0.0032 -0.0750 17  GLU   B C   
312  O O   . GLU   B 8   ? 1.0758 1.0005 0.9543 0.2705  0.0031  -0.0666 17  GLU   B O   
313  C CB  . GLU   B 8   ? 1.1325 1.0221 0.9985 0.3184  -0.0165 -0.0717 17  GLU   B CB  
314  C CG  . GLU   B 8   ? 1.1878 1.0798 1.0519 0.3219  -0.0317 -0.0670 17  GLU   B CG  
315  C CD  . GLU   B 8   ? 1.2765 1.1308 1.1055 0.3356  -0.0390 -0.0560 17  GLU   B CD  
316  O OE1 . GLU   B 8   ? 1.3040 1.1302 1.1095 0.3316  -0.0287 -0.0462 17  GLU   B OE1 
317  O OE2 . GLU   B 8   ? 1.2991 1.1527 1.1243 0.3504  -0.0552 -0.0568 17  GLU   B OE2 
318  N N   A THR   B 9   ? 1.0238 1.0054 0.9556 0.2755  -0.0077 -0.0782 18  THR   B N   
319  N N   B THR   B 9   ? 1.0236 1.0054 0.9556 0.2759  -0.0078 -0.0783 18  THR   B N   
320  C CA  A THR   B 9   ? 1.0149 1.0068 0.9506 0.2525  -0.0063 -0.0710 18  THR   B CA  
321  C CA  B THR   B 9   ? 1.0132 1.0074 0.9513 0.2529  -0.0066 -0.0716 18  THR   B CA  
322  C C   A THR   B 9   ? 1.0057 0.9909 0.9419 0.2531  -0.0259 -0.0674 18  THR   B C   
323  C C   B THR   B 9   ? 1.0043 0.9916 0.9428 0.2534  -0.0263 -0.0679 18  THR   B C   
324  O O   A THR   B 9   ? 1.0038 0.9981 0.9488 0.2357  -0.0291 -0.0631 18  THR   B O   
325  O O   B THR   B 9   ? 1.0011 0.9996 0.9507 0.2360  -0.0298 -0.0640 18  THR   B O   
326  C CB  A THR   B 9   ? 1.0107 1.0444 0.9774 0.2368  0.0053  -0.0735 18  THR   B CB  
327  C CB  B THR   B 9   ? 1.0072 1.0454 0.9793 0.2399  0.0039  -0.0753 18  THR   B CB  
328  O OG1 A THR   B 9   ? 1.0108 1.0701 0.9979 0.2501  0.0134  -0.0842 18  THR   B OG1 
329  O OG1 B THR   B 9   ? 0.9991 1.0678 1.0049 0.2540  -0.0019 -0.0848 18  THR   B OG1 
330  C CG2 A THR   B 9   ? 1.0228 1.0511 0.9720 0.2168  0.0199  -0.0666 18  THR   B CG2 
331  C CG2 B THR   B 9   ? 1.0167 1.0571 0.9766 0.2332  0.0246  -0.0766 18  THR   B CG2 
332  N N   . THR   B 10  ? 1.0010 0.9674 0.9248 0.2740  -0.0400 -0.0692 19  THR   B N   
333  C CA  . THR   B 10  ? 0.9827 0.9394 0.9006 0.2798  -0.0607 -0.0684 19  THR   B CA  
334  C C   . THR   B 10  ? 0.9680 0.9016 0.8579 0.2690  -0.0598 -0.0591 19  THR   B C   
335  O O   . THR   B 10  ? 0.9831 0.8962 0.8469 0.2679  -0.0467 -0.0519 19  THR   B O   
336  C CB  . THR   B 10  ? 1.0118 0.9478 0.9111 0.3074  -0.0729 -0.0707 19  THR   B CB  
337  O OG1 . THR   B 10  ? 1.0082 0.9651 0.9337 0.3194  -0.0738 -0.0800 19  THR   B OG1 
338  C CG2 . THR   B 10  ? 1.0212 0.9470 0.9106 0.3181  -0.0968 -0.0725 19  THR   B CG2 
339  N N   . ASP   B 11  ? 0.9352 0.8722 0.8327 0.2611  -0.0747 -0.0599 20  ASP   B N   
340  C CA  . ASP   B 11  ? 0.9331 0.8485 0.8048 0.2547  -0.0770 -0.0533 20  ASP   B CA  
341  C C   . ASP   B 11  ? 0.9362 0.8219 0.7676 0.2755  -0.0784 -0.0489 20  ASP   B C   
342  O O   . ASP   B 11  ? 0.9480 0.8268 0.7713 0.2958  -0.0888 -0.0526 20  ASP   B O   
343  C CB  . ASP   B 11  ? 0.9511 0.8693 0.8366 0.2484  -0.0989 -0.0577 20  ASP   B CB  
344  C CG  . ASP   B 11  ? 0.9944 0.9356 0.9137 0.2220  -0.0966 -0.0561 20  ASP   B CG  
345  O OD1 . ASP   B 11  ? 0.9904 0.9558 0.9301 0.2113  -0.0789 -0.0543 20  ASP   B OD1 
346  O OD2 . ASP   B 11  ? 1.0213 0.9552 0.9452 0.2128  -0.1130 -0.0563 20  ASP   B OD2 
347  N N   . GLY   B 12  ? 0.9252 0.7954 0.7321 0.2707  -0.0683 -0.0403 21  GLY   B N   
348  C CA  . GLY   B 12  ? 0.9292 0.7764 0.6997 0.2881  -0.0657 -0.0332 21  GLY   B CA  
349  C C   . GLY   B 12  ? 0.9225 0.7632 0.6799 0.2783  -0.0461 -0.0222 21  GLY   B C   
350  O O   . GLY   B 12  ? 0.9178 0.7687 0.6903 0.2587  -0.0369 -0.0215 21  GLY   B O   
351  N N   . VAL   B 13  ? 0.9209 0.7456 0.6501 0.2917  -0.0400 -0.0129 22  VAL   B N   
352  C CA  . VAL   B 13  ? 0.9147 0.7356 0.6355 0.2824  -0.0223 -0.0013 22  VAL   B CA  
353  C C   . VAL   B 13  ? 0.9091 0.7221 0.6318 0.2818  -0.0104 0.0044  22  VAL   B C   
354  O O   . VAL   B 13  ? 0.9212 0.7252 0.6376 0.2969  -0.0156 0.0034  22  VAL   B O   
355  C CB  . VAL   B 13  ? 0.9295 0.7428 0.6228 0.2950  -0.0209 0.0071  22  VAL   B CB  
356  C CG1 . VAL   B 13  ? 0.9517 0.7513 0.6183 0.3194  -0.0240 0.0119  22  VAL   B CG1 
357  C CG2 . VAL   B 13  ? 0.9299 0.7464 0.6230 0.2830  -0.0036 0.0189  22  VAL   B CG2 
358  N N   . TYR   B 14  ? 0.8887 0.7033 0.6211 0.2646  0.0025  0.0085  23  TYR   B N   
359  C CA  . TYR   B 14  ? 0.8797 0.6826 0.6152 0.2621  0.0111  0.0117  23  TYR   B CA  
360  C C   . TYR   B 14  ? 0.8777 0.6725 0.6086 0.2508  0.0238  0.0245  23  TYR   B C   
361  O O   . TYR   B 14  ? 0.8744 0.6802 0.6097 0.2388  0.0272  0.0263  23  TYR   B O   
362  C CB  . TYR   B 14  ? 0.8582 0.6722 0.6160 0.2507  0.0117  -0.0010 23  TYR   B CB  
363  C CG  . TYR   B 14  ? 0.8467 0.6719 0.6174 0.2609  0.0016  -0.0129 23  TYR   B CG  
364  C CD1 . TYR   B 14  ? 0.8467 0.6875 0.6252 0.2618  -0.0094 -0.0184 23  TYR   B CD1 
365  C CD2 . TYR   B 14  ? 0.8474 0.6692 0.6264 0.2685  0.0021  -0.0196 23  TYR   B CD2 
366  C CE1 . TYR   B 14  ? 0.8441 0.6991 0.6406 0.2695  -0.0199 -0.0288 23  TYR   B CE1 
367  C CE2 . TYR   B 14  ? 0.8453 0.6833 0.6414 0.2787  -0.0071 -0.0307 23  TYR   B CE2 
368  C CZ  . TYR   B 14  ? 0.8474 0.7042 0.6545 0.2779  -0.0179 -0.0349 23  TYR   B CZ  
369  O OH  . TYR   B 14  ? 0.8500 0.7270 0.6802 0.2859  -0.0283 -0.0454 23  TYR   B OH  
370  N N   . ARG   B 15  ? 0.8768 0.6523 0.6023 0.2533  0.0293  0.0328  24  ARG   B N   
371  C CA  . ARG   B 15  ? 0.8769 0.6442 0.6046 0.2395  0.0398  0.0452  24  ARG   B CA  
372  C C   . ARG   B 15  ? 0.8685 0.6329 0.6126 0.2239  0.0401  0.0346  24  ARG   B C   
373  O O   . ARG   B 15  ? 0.8627 0.6217 0.6107 0.2294  0.0354  0.0226  24  ARG   B O   
374  C CB  . ARG   B 15  ? 0.9029 0.6456 0.6168 0.2481  0.0444  0.0612  24  ARG   B CB  
375  C CG  . ARG   B 15  ? 0.9336 0.6760 0.6240 0.2668  0.0454  0.0732  24  ARG   B CG  
376  C CD  . ARG   B 15  ? 0.9848 0.7000 0.6598 0.2741  0.0505  0.0909  24  ARG   B CD  
377  N NE  . ARG   B 15  ? 1.0157 0.7276 0.6614 0.2969  0.0497  0.1005  24  ARG   B NE  
378  C CZ  . ARG   B 15  ? 1.0398 0.7613 0.6700 0.3013  0.0607  0.1170  24  ARG   B CZ  
379  N NH1 . ARG   B 15  ? 1.0282 0.7657 0.6744 0.2834  0.0732  0.1265  24  ARG   B NH1 
380  N NH2 . ARG   B 15  ? 1.0441 0.7614 0.6425 0.3252  0.0587  0.1234  24  ARG   B NH2 
381  N N   . VAL   B 16  ? 0.8683 0.6369 0.6212 0.2063  0.0450  0.0385  25  VAL   B N   
382  C CA  . VAL   B 16  ? 0.8781 0.6415 0.6419 0.1914  0.0442  0.0288  25  VAL   B CA  
383  C C   . VAL   B 16  ? 0.8953 0.6346 0.6613 0.1837  0.0472  0.0407  25  VAL   B C   
384  O O   . VAL   B 16  ? 0.8913 0.6352 0.6612 0.1760  0.0527  0.0563  25  VAL   B O   
385  C CB  . VAL   B 16  ? 0.8783 0.6627 0.6496 0.1772  0.0441  0.0246  25  VAL   B CB  
386  C CG1 . VAL   B 16  ? 0.8879 0.6660 0.6647 0.1645  0.0418  0.0128  25  VAL   B CG1 
387  C CG2 . VAL   B 16  ? 0.8741 0.6787 0.6430 0.1834  0.0406  0.0176  25  VAL   B CG2 
388  N N   . MET   B 17  ? 0.9140 0.6278 0.6783 0.1870  0.0432  0.0342  26  MET   B N   
389  C CA  . MET   B 17  ? 0.9422 0.6251 0.7079 0.1804  0.0432  0.0457  26  MET   B CA  
390  C C   . MET   B 17  ? 0.9728 0.6375 0.7462 0.1677  0.0365  0.0325  26  MET   B C   
391  O O   . MET   B 17  ? 0.9742 0.6480 0.7466 0.1701  0.0329  0.0128  26  MET   B O   
392  C CB  . MET   B 17  ? 0.9578 0.6152 0.7099 0.1993  0.0405  0.0490  26  MET   B CB  
393  C CG  . MET   B 17  ? 0.9718 0.6421 0.7106 0.2167  0.0433  0.0578  26  MET   B CG  
394  S SD  . MET   B 17  ? 1.0052 0.6744 0.7365 0.2129  0.0545  0.0883  26  MET   B SD  
395  C CE  . MET   B 17  ? 0.9966 0.6203 0.7285 0.2046  0.0533  0.1022  26  MET   B CE  
396  N N   . THR   B 18  ? 0.9994 0.6364 0.7794 0.1553  0.0341  0.0432  27  THR   B N   
397  C CA  . THR   B 18  ? 1.0355 0.6462 0.8201 0.1451  0.0238  0.0295  27  THR   B CA  
398  C C   . THR   B 18  ? 1.0815 0.6463 0.8667 0.1414  0.0180  0.0408  27  THR   B C   
399  O O   . THR   B 18  ? 1.0822 0.6413 0.8718 0.1357  0.0243  0.0656  27  THR   B O   
400  C CB  . THR   B 18  ? 1.0384 0.6664 0.8367 0.1248  0.0209  0.0250  27  THR   B CB  
401  O OG1 . THR   B 18  ? 1.0620 0.6607 0.8594 0.1186  0.0081  0.0081  27  THR   B OG1 
402  C CG2 . THR   B 18  ? 1.0287 0.6676 0.8457 0.1073  0.0260  0.0485  27  THR   B CG2 
403  N N   . ARG   B 19  ? 1.1160 0.6470 0.8954 0.1454  0.0059  0.0229  28  ARG   B N   
404  C CA  . ARG   B 19  ? 1.1623 0.6422 0.9418 0.1409  -0.0033 0.0314  28  ARG   B CA  
405  C C   . ARG   B 19  ? 1.1829 0.6395 0.9766 0.1179  -0.0164 0.0251  28  ARG   B C   
406  O O   . ARG   B 19  ? 1.2006 0.6101 0.9968 0.1109  -0.0275 0.0305  28  ARG   B O   
407  C CB  . ARG   B 19  ? 1.2080 0.6570 0.9687 0.1665  -0.0105 0.0174  28  ARG   B CB  
408  C CG  . ARG   B 19  ? 1.2665 0.7246 1.0161 0.1858  -0.0020 0.0314  28  ARG   B CG  
409  C CD  . ARG   B 19  ? 1.3504 0.7705 1.0845 0.2095  -0.0118 0.0221  28  ARG   B CD  
410  N NE  . ARG   B 19  ? 1.4083 0.8409 1.1308 0.2310  -0.0065 0.0312  28  ARG   B NE  
411  C CZ  . ARG   B 19  ? 1.4393 0.8998 1.1584 0.2525  -0.0061 0.0133  28  ARG   B CZ  
412  N NH1 . ARG   B 19  ? 1.4354 0.9166 1.1611 0.2555  -0.0075 -0.0128 28  ARG   B NH1 
413  N NH2 . ARG   B 19  ? 1.4357 0.9049 1.1453 0.2711  -0.0045 0.0219  28  ARG   B NH2 
414  N N   . ARG   B 20  ? 1.1801 0.6682 0.9832 0.1057  -0.0168 0.0149  29  ARG   B N   
415  C CA  . ARG   B 20  ? 1.1955 0.6699 1.0122 0.0844  -0.0310 0.0064  29  ARG   B CA  
416  C C   . ARG   B 20  ? 1.1859 0.6539 1.0317 0.0574  -0.0317 0.0339  29  ARG   B C   
417  O O   . ARG   B 20  ? 1.1911 0.6391 1.0532 0.0375  -0.0471 0.0296  29  ARG   B O   
418  C CB  . ARG   B 20  ? 1.2132 0.7281 1.0282 0.0824  -0.0299 -0.0101 29  ARG   B CB  
419  C CG  . ARG   B 20  ? 1.2793 0.7779 1.0979 0.0683  -0.0483 -0.0282 29  ARG   B CG  
420  C CD  . ARG   B 20  ? 1.3306 0.8719 1.1513 0.0619  -0.0462 -0.0348 29  ARG   B CD  
421  N NE  . ARG   B 20  ? 1.3712 0.9505 1.2152 0.0496  -0.0345 -0.0102 29  ARG   B NE  
422  C CZ  . ARG   B 20  ? 1.4035 0.9898 1.2766 0.0268  -0.0404 0.0031  29  ARG   B CZ  
423  N NH1 . ARG   B 20  ? 1.4133 0.9684 1.2974 0.0113  -0.0602 -0.0055 29  ARG   B NH1 
424  N NH2 . ARG   B 20  ? 1.3829 1.0083 1.2758 0.0202  -0.0276 0.0242  29  ARG   B NH2 
425  N N   . LEU   B 21  ? 1.1680 0.6538 1.0206 0.0570  -0.0154 0.0620  30  LEU   B N   
426  C CA  . LEU   B 21  ? 1.1560 0.6427 1.0369 0.0330  -0.0112 0.0916  30  LEU   B CA  
427  C C   . LEU   B 21  ? 1.1651 0.6094 1.0379 0.0368  -0.0086 0.1134  30  LEU   B C   
428  O O   . LEU   B 21  ? 1.1886 0.5928 1.0379 0.0545  -0.0178 0.0995  30  LEU   B O   
429  C CB  . LEU   B 21  ? 1.1365 0.6826 1.0302 0.0304  0.0073  0.1079  30  LEU   B CB  
430  C CG  . LEU   B 21  ? 1.1451 0.7292 1.0495 0.0238  0.0029  0.0911  30  LEU   B CG  
431  C CD1 . LEU   B 21  ? 1.1597 0.7612 1.0360 0.0469  0.0056  0.0688  30  LEU   B CD1 
432  C CD2 . LEU   B 21  ? 1.1300 0.7620 1.0605 0.0122  0.0162  0.1128  30  LEU   B CD2 
433  N N   . LEU   B 22  ? 1.1413 0.5932 1.0332 0.0209  0.0033  0.1474  31  LEU   B N   
434  C CA  . LEU   B 22  ? 1.1484 0.5614 1.0295 0.0240  0.0075  0.1722  31  LEU   B CA  
435  C C   . LEU   B 22  ? 1.1514 0.5805 0.9991 0.0553  0.0218  0.1743  31  LEU   B C   
436  O O   . LEU   B 22  ? 1.1388 0.6190 0.9852 0.0630  0.0362  0.1756  31  LEU   B O   
437  C CB  . LEU   B 22  ? 1.1281 0.5549 1.0401 -0.0027 0.0197  0.2098  31  LEU   B CB  
438  C CG  . LEU   B 22  ? 1.1521 0.5351 1.0561 -0.0058 0.0237  0.2404  31  LEU   B CG  
439  C CD1 . LEU   B 22  ? 1.1690 0.4944 1.0928 -0.0303 0.0017  0.2413  31  LEU   B CD1 
440  C CD2 . LEU   B 22  ? 1.1397 0.5621 1.0574 -0.0156 0.0492  0.2793  31  LEU   B CD2 
441  N N   . GLY   B 23  ? 1.1616 0.5458 0.9828 0.0743  0.0150  0.1720  32  GLY   B N   
442  C CA  . GLY   B 23  ? 1.1585 0.5523 0.9484 0.1052  0.0235  0.1713  32  GLY   B CA  
443  C C   . GLY   B 23  ? 1.1325 0.5695 0.9152 0.1223  0.0250  0.1430  32  GLY   B C   
444  O O   . GLY   B 23  ? 1.1273 0.5694 0.9187 0.1179  0.0150  0.1168  32  GLY   B O   
445  N N   . SER   B 24  ? 1.1134 0.5814 0.8797 0.1412  0.0372  0.1490  33  SER   B N   
446  C CA  . SER   B 24  ? 1.0911 0.6001 0.8525 0.1554  0.0388  0.1261  33  SER   B CA  
447  C C   . SER   B 24  ? 1.0563 0.6137 0.8297 0.1453  0.0529  0.1384  33  SER   B C   
448  O O   . SER   B 24  ? 1.0574 0.6250 0.8228 0.1496  0.0653  0.1623  33  SER   B O   
449  C CB  . SER   B 24  ? 1.1138 0.6202 0.8494 0.1854  0.0378  0.1207  33  SER   B CB  
450  O OG  . SER   B 24  ? 1.1538 0.6167 0.8788 0.1979  0.0247  0.1100  33  SER   B OG  
451  N N   . THR   B 25  ? 1.0263 0.6121 0.8168 0.1334  0.0508  0.1229  34  THR   B N   
452  C CA  . THR   B 25  ? 1.0008 0.6312 0.8042 0.1251  0.0620  0.1329  34  THR   B CA  
453  C C   . THR   B 25  ? 0.9760 0.6414 0.7705 0.1391  0.0627  0.1150  34  THR   B C   
454  O O   . THR   B 25  ? 0.9713 0.6392 0.7672 0.1384  0.0537  0.0919  34  THR   B O   
455  C CB  . THR   B 25  ? 1.0045 0.6410 0.8388 0.0973  0.0586  0.1356  34  THR   B CB  
456  O OG1 . THR   B 25  ? 1.0219 0.6249 0.8680 0.0817  0.0571  0.1546  34  THR   B OG1 
457  C CG2 . THR   B 25  ? 0.9858 0.6705 0.8365 0.0904  0.0694  0.1456  34  THR   B CG2 
458  N N   . GLN   B 26  ? 0.9553 0.6468 0.7394 0.1516  0.0730  0.1262  35  GLN   B N   
459  C CA  . GLN   B 26  ? 0.9363 0.6572 0.7132 0.1632  0.0717  0.1108  35  GLN   B CA  
460  C C   . GLN   B 26  ? 0.9137 0.6637 0.7108 0.1474  0.0721  0.1070  35  GLN   B C   
461  O O   . GLN   B 26  ? 0.9111 0.6808 0.7200 0.1406  0.0812  0.1237  35  GLN   B O   
462  C CB  . GLN   B 26  ? 0.9397 0.6738 0.6956 0.1842  0.0789  0.1210  35  GLN   B CB  
463  C CG  . GLN   B 26  ? 0.9409 0.7020 0.6913 0.1943  0.0750  0.1059  35  GLN   B CG  
464  C CD  . GLN   B 26  ? 0.9724 0.7417 0.6993 0.2168  0.0782  0.1124  35  GLN   B CD  
465  O OE1 . GLN   B 26  ? 0.9986 0.7490 0.7063 0.2314  0.0783  0.1195  35  GLN   B OE1 
466  N NE2 . GLN   B 26  ? 0.9586 0.7537 0.6838 0.2219  0.0789  0.1087  35  GLN   B NE2 
467  N N   . VAL   B 27  ? 0.8919 0.6463 0.6923 0.1430  0.0628  0.0858  36  VAL   B N   
468  C CA  . VAL   B 27  ? 0.8657 0.6446 0.6810 0.1302  0.0604  0.0807  36  VAL   B CA  
469  C C   . VAL   B 27  ? 0.8496 0.6559 0.6561 0.1417  0.0612  0.0756  36  VAL   B C   
470  O O   . VAL   B 27  ? 0.8450 0.6733 0.6621 0.1346  0.0601  0.0752  36  VAL   B O   
471  C CB  . VAL   B 27  ? 0.8737 0.6392 0.6940 0.1182  0.0493  0.0621  36  VAL   B CB  
472  C CG1 . VAL   B 27  ? 0.8875 0.6235 0.7182 0.1055  0.0452  0.0665  36  VAL   B CG1 
473  C CG2 . VAL   B 27  ? 0.8827 0.6416 0.6857 0.1310  0.0450  0.0437  36  VAL   B CG2 
474  N N   . GLY   B 28  ? 0.8378 0.6409 0.6261 0.1594  0.0609  0.0710  37  GLY   B N   
475  C CA  . GLY   B 28  ? 0.8247 0.6468 0.6041 0.1701  0.0584  0.0650  37  GLY   B CA  
476  C C   . GLY   B 28  ? 0.8186 0.6332 0.5812 0.1880  0.0547  0.0586  37  GLY   B C   
477  O O   . GLY   B 28  ? 0.8226 0.6192 0.5784 0.1955  0.0556  0.0613  37  GLY   B O   
478  N N   . VAL   B 29  ? 0.8075 0.6347 0.5646 0.1947  0.0486  0.0500  38  VAL   B N   
479  C CA  . VAL   B 29  ? 0.8079 0.6332 0.5531 0.2106  0.0415  0.0427  38  VAL   B CA  
480  C C   . VAL   B 29  ? 0.7926 0.6271 0.5445 0.2037  0.0328  0.0286  38  VAL   B C   
481  O O   . VAL   B 29  ? 0.7822 0.6248 0.5412 0.1904  0.0327  0.0270  38  VAL   B O   
482  C CB  . VAL   B 29  ? 0.8152 0.6462 0.5440 0.2279  0.0422  0.0510  38  VAL   B CB  
483  C CG1 . VAL   B 29  ? 0.8236 0.6510 0.5394 0.2449  0.0307  0.0418  38  VAL   B CG1 
484  C CG2 . VAL   B 29  ? 0.8246 0.6497 0.5456 0.2340  0.0539  0.0684  38  VAL   B CG2 
485  N N   . GLY   B 30  ? 0.7877 0.6214 0.5381 0.2123  0.0252  0.0199  39  GLY   B N   
486  C CA  . GLY   B 30  ? 0.7849 0.6288 0.5441 0.2047  0.0180  0.0096  39  GLY   B CA  
487  C C   . GLY   B 30  ? 0.7872 0.6331 0.5461 0.2165  0.0068  0.0032  39  GLY   B C   
488  O O   . GLY   B 30  ? 0.7980 0.6363 0.5486 0.2323  0.0039  0.0041  39  GLY   B O   
489  N N   . VAL   B 31  ? 0.7784 0.6333 0.5464 0.2082  -0.0010 -0.0028 40  VAL   B N   
490  C CA  . VAL   B 31  ? 0.7789 0.6369 0.5527 0.2155  -0.0147 -0.0095 40  VAL   B CA  
491  C C   . VAL   B 31  ? 0.7740 0.6475 0.5709 0.2055  -0.0141 -0.0166 40  VAL   B C   
492  O O   . VAL   B 31  ? 0.7686 0.6516 0.5741 0.1889  -0.0080 -0.0162 40  VAL   B O   
493  C CB  . VAL   B 31  ? 0.7838 0.6383 0.5518 0.2139  -0.0267 -0.0095 40  VAL   B CB  
494  C CG1 . VAL   B 31  ? 0.7816 0.6382 0.5612 0.2159  -0.0439 -0.0173 40  VAL   B CG1 
495  C CG2 . VAL   B 31  ? 0.8014 0.6450 0.5464 0.2295  -0.0273 -0.0044 40  VAL   B CG2 
496  N N   . MET   B 32  ? 0.7707 0.6489 0.5774 0.2166  -0.0205 -0.0226 41  MET   B N   
497  C CA  . MET   B 32  ? 0.7645 0.6641 0.5979 0.2090  -0.0199 -0.0294 41  MET   B CA  
498  C C   . MET   B 32  ? 0.7674 0.6750 0.6159 0.2055  -0.0367 -0.0324 41  MET   B C   
499  O O   . MET   B 32  ? 0.7809 0.6790 0.6233 0.2202  -0.0517 -0.0358 41  MET   B O   
500  C CB  . MET   B 32  ? 0.7641 0.6672 0.6045 0.2237  -0.0180 -0.0351 41  MET   B CB  
501  C CG  . MET   B 32  ? 0.7688 0.6995 0.6381 0.2173  -0.0131 -0.0423 41  MET   B CG  
502  S SD  . MET   B 32  ? 0.8344 0.7705 0.7004 0.2050  0.0077  -0.0423 41  MET   B SD  
503  C CE  . MET   B 32  ? 0.8305 0.7407 0.6778 0.2230  0.0114  -0.0438 41  MET   B CE  
504  N N   . GLN   B 33  ? 0.7549 0.6761 0.6197 0.1859  -0.0355 -0.0305 42  GLN   B N   
505  C CA  . GLN   B 33  ? 0.7506 0.6767 0.6333 0.1785  -0.0528 -0.0319 42  GLN   B CA  
506  C C   . GLN   B 33  ? 0.7305 0.6841 0.6427 0.1577  -0.0446 -0.0292 42  GLN   B C   
507  O O   . GLN   B 33  ? 0.7425 0.6990 0.6471 0.1446  -0.0298 -0.0229 42  GLN   B O   
508  C CB  . GLN   B 33  ? 0.7938 0.6957 0.6556 0.1763  -0.0642 -0.0278 42  GLN   B CB  
509  C CG  . GLN   B 33  ? 0.8701 0.7689 0.7482 0.1707  -0.0870 -0.0309 42  GLN   B CG  
510  C CD  . GLN   B 33  ? 0.9720 0.8407 0.8243 0.1784  -0.1035 -0.0314 42  GLN   B CD  
511  O OE1 . GLN   B 33  ? 0.9957 0.8543 0.8522 0.1644  -0.1143 -0.0281 42  GLN   B OE1 
512  N NE2 . GLN   B 33  ? 1.0003 0.8536 0.8243 0.2018  -0.1055 -0.0350 42  GLN   B NE2 
513  N N   . GLU   B 34  ? 0.7015 0.6776 0.6474 0.1550  -0.0535 -0.0335 43  GLU   B N   
514  C CA  . GLU   B 34  ? 0.6805 0.6904 0.6602 0.1352  -0.0438 -0.0292 43  GLU   B CA  
515  C C   . GLU   B 34  ? 0.6707 0.7020 0.6496 0.1351  -0.0174 -0.0293 43  GLU   B C   
516  O O   . GLU   B 34  ? 0.6676 0.7174 0.6544 0.1178  -0.0032 -0.0221 43  GLU   B O   
517  C CB  . GLU   B 34  ? 0.7127 0.7148 0.6942 0.1117  -0.0490 -0.0183 43  GLU   B CB  
518  C CG  . GLU   B 34  ? 0.7800 0.7653 0.7718 0.1098  -0.0775 -0.0203 43  GLU   B CG  
519  C CD  . GLU   B 34  ? 0.8818 0.8384 0.8572 0.0955  -0.0881 -0.0116 43  GLU   B CD  
520  O OE1 . GLU   B 34  ? 0.8761 0.8434 0.8672 0.0716  -0.0821 0.0001  43  GLU   B OE1 
521  O OE2 . GLU   B 34  ? 0.9475 0.8705 0.8931 0.1096  -0.1021 -0.0159 43  GLU   B OE2 
522  N N   . GLY   B 35  ? 0.6672 0.6937 0.6345 0.1553  -0.0122 -0.0375 44  GLY   B N   
523  C CA  . GLY   B 35  ? 0.6586 0.6984 0.6216 0.1596  0.0087  -0.0410 44  GLY   B CA  
524  C C   . GLY   B 35  ? 0.6707 0.6903 0.6007 0.1523  0.0208  -0.0358 44  GLY   B C   
525  O O   . GLY   B 35  ? 0.6649 0.6955 0.5896 0.1515  0.0375  -0.0384 44  GLY   B O   
526  N N   . VAL   B 36  ? 0.6823 0.6730 0.5897 0.1483  0.0114  -0.0294 45  VAL   B N   
527  C CA  . VAL   B 36  ? 0.6985 0.6709 0.5776 0.1412  0.0193  -0.0242 45  VAL   B CA  
528  C C   . VAL   B 36  ? 0.7137 0.6572 0.5698 0.1544  0.0136  -0.0246 45  VAL   B C   
529  O O   . VAL   B 36  ? 0.7240 0.6555 0.5779 0.1628  0.0001  -0.0239 45  VAL   B O   
530  C CB  . VAL   B 36  ? 0.7078 0.6783 0.5837 0.1217  0.0161  -0.0140 45  VAL   B CB  
531  C CG1 . VAL   B 36  ? 0.7335 0.6838 0.5799 0.1172  0.0202  -0.0094 45  VAL   B CG1 
532  C CG2 . VAL   B 36  ? 0.6920 0.6931 0.5887 0.1067  0.0266  -0.0101 45  VAL   B CG2 
533  N N   . PHE   B 37  ? 0.7118 0.6449 0.5513 0.1569  0.0236  -0.0260 46  PHE   B N   
534  C CA  . PHE   B 37  ? 0.7190 0.6283 0.5405 0.1661  0.0209  -0.0235 46  PHE   B CA  
535  C C   . PHE   B 37  ? 0.7221 0.6218 0.5288 0.1550  0.0203  -0.0164 46  PHE   B C   
536  O O   . PHE   B 37  ? 0.7222 0.6258 0.5238 0.1437  0.0272  -0.0162 46  PHE   B O   
537  C CB  . PHE   B 37  ? 0.7230 0.6244 0.5389 0.1735  0.0295  -0.0285 46  PHE   B CB  
538  C CG  . PHE   B 37  ? 0.7426 0.6212 0.5451 0.1828  0.0270  -0.0234 46  PHE   B CG  
539  C CD1 . PHE   B 37  ? 0.7528 0.6244 0.5547 0.1981  0.0201  -0.0219 46  PHE   B CD1 
540  C CD2 . PHE   B 37  ? 0.7596 0.6248 0.5504 0.1760  0.0314  -0.0191 46  PHE   B CD2 
541  C CE1 . PHE   B 37  ? 0.7716 0.6238 0.5592 0.2063  0.0204  -0.0143 46  PHE   B CE1 
542  C CE2 . PHE   B 37  ? 0.7772 0.6252 0.5598 0.1823  0.0311  -0.0116 46  PHE   B CE2 
543  C CZ  . PHE   B 37  ? 0.7771 0.6188 0.5570 0.1975  0.0270  -0.0083 46  PHE   B CZ  
544  N N   . HIS   B 38  ? 0.7204 0.6084 0.5191 0.1601  0.0113  -0.0112 47  HIS   B N   
545  C CA  . HIS   B 38  ? 0.7173 0.5977 0.5040 0.1530  0.0088  -0.0049 47  HIS   B CA  
546  C C   . HIS   B 38  ? 0.7206 0.5904 0.4973 0.1607  0.0123  -0.0010 47  HIS   B C   
547  O O   . HIS   B 38  ? 0.7175 0.5816 0.4915 0.1744  0.0109  0.0002  47  HIS   B O   
548  C CB  . HIS   B 38  ? 0.7131 0.5890 0.4989 0.1552  -0.0050 -0.0026 47  HIS   B CB  
549  C CG  . HIS   B 38  ? 0.7177 0.6033 0.5189 0.1469  -0.0108 -0.0047 47  HIS   B CG  
550  N ND1 . HIS   B 38  ? 0.7301 0.6242 0.5466 0.1543  -0.0145 -0.0104 47  HIS   B ND1 
551  C CD2 . HIS   B 38  ? 0.7285 0.6170 0.5336 0.1313  -0.0141 -0.0004 47  HIS   B CD2 
552  C CE1 . HIS   B 38  ? 0.7279 0.6333 0.5614 0.1416  -0.0192 -0.0096 47  HIS   B CE1 
553  N NE2 . HIS   B 38  ? 0.7327 0.6340 0.5590 0.1269  -0.0183 -0.0026 47  HIS   B NE2 
554  N N   . THR   B 39  ? 0.7212 0.5894 0.4929 0.1516  0.0165  0.0018  48  THR   B N   
555  C CA  . THR   B 39  ? 0.7315 0.5939 0.5000 0.1558  0.0198  0.0076  48  THR   B CA  
556  C C   . THR   B 39  ? 0.7397 0.6050 0.5057 0.1461  0.0177  0.0114  48  THR   B C   
557  O O   . THR   B 39  ? 0.7368 0.6045 0.4991 0.1378  0.0129  0.0099  48  THR   B O   
558  C CB  . THR   B 39  ? 0.7416 0.5968 0.5133 0.1577  0.0274  0.0060  48  THR   B CB  
559  O OG1 . THR   B 39  ? 0.7518 0.6020 0.5228 0.1623  0.0306  0.0152  48  THR   B OG1 
560  C CG2 . THR   B 39  ? 0.7424 0.5960 0.5149 0.1457  0.0308  -0.0003 48  THR   B CG2 
561  N N   . MET   B 40  ? 0.7437 0.6098 0.5128 0.1474  0.0207  0.0176  49  MET   B N   
562  C CA  . MET   B 40  ? 0.7479 0.6199 0.5194 0.1393  0.0176  0.0206  49  MET   B CA  
563  C C   . MET   B 40  ? 0.7636 0.6317 0.5378 0.1261  0.0191  0.0158  49  MET   B C   
564  O O   . MET   B 40  ? 0.7759 0.6361 0.5539 0.1253  0.0243  0.0138  49  MET   B O   
565  C CB  . MET   B 40  ? 0.7477 0.6282 0.5263 0.1469  0.0206  0.0299  49  MET   B CB  
566  C CG  . MET   B 40  ? 0.7833 0.6655 0.5535 0.1640  0.0188  0.0324  49  MET   B CG  
567  S SD  . MET   B 40  ? 0.8894 0.7864 0.6610 0.1730  0.0147  0.0377  49  MET   B SD  
568  C CE  . MET   B 40  ? 0.7989 0.6879 0.5619 0.1666  0.0001  0.0306  49  MET   B CE  
569  N N   . TRP   B 41  ? 0.7622 0.6328 0.5316 0.1169  0.0127  0.0133  50  TRP   B N   
570  C CA  A TRP   B 41  ? 0.7699 0.6353 0.5364 0.1060  0.0113  0.0066  50  TRP   B CA  
571  C CA  B TRP   B 41  ? 0.7699 0.6354 0.5364 0.1060  0.0112  0.0066  50  TRP   B CA  
572  C C   . TRP   B 41  ? 0.7677 0.6304 0.5488 0.1016  0.0119  0.0085  50  TRP   B C   
573  O O   . TRP   B 41  ? 0.7730 0.6238 0.5523 0.0966  0.0122  0.0011  50  TRP   B O   
574  C CB  A TRP   B 41  ? 0.7733 0.6413 0.5286 0.0989  0.0025  0.0053  50  TRP   B CB  
575  C CB  B TRP   B 41  ? 0.7731 0.6415 0.5288 0.0990  0.0021  0.0056  50  TRP   B CB  
576  C CG  A TRP   B 41  ? 0.7859 0.6466 0.5286 0.0908  0.0009  -0.0041 50  TRP   B CG  
577  C CG  B TRP   B 41  ? 0.7844 0.6462 0.5317 0.0898  -0.0015 -0.0028 50  TRP   B CG  
578  C CD1 A TRP   B 41  ? 0.8031 0.6609 0.5290 0.0897  0.0055  -0.0102 50  TRP   B CD1 
579  C CD1 B TRP   B 41  ? 0.7936 0.6541 0.5506 0.0835  -0.0082 -0.0048 50  TRP   B CD1 
580  C CD2 A TRP   B 41  ? 0.7891 0.6450 0.5350 0.0837  -0.0059 -0.0093 50  TRP   B CD2 
581  C CD2 B TRP   B 41  ? 0.7942 0.6500 0.5220 0.0872  0.0013  -0.0113 50  TRP   B CD2 
582  N NE1 A TRP   B 41  ? 0.8136 0.6641 0.5271 0.0850  0.0028  -0.0198 50  TRP   B NE1 
583  N NE1 B TRP   B 41  ? 0.8065 0.6564 0.5482 0.0780  -0.0121 -0.0159 50  TRP   B NE1 
584  C CE2 A TRP   B 41  ? 0.8095 0.6563 0.5348 0.0808  -0.0061 -0.0202 50  TRP   B CE2 
585  C CE2 B TRP   B 41  ? 0.8098 0.6576 0.5314 0.0814  -0.0051 -0.0200 50  TRP   B CE2 
586  C CE3 A TRP   B 41  ? 0.7891 0.6491 0.5549 0.0793  -0.0123 -0.0056 50  TRP   B CE3 
587  C CE3 B TRP   B 41  ? 0.8044 0.6630 0.5207 0.0892  0.0086  -0.0123 50  TRP   B CE3 
588  C CZ2 A TRP   B 41  ? 0.8251 0.6620 0.5453 0.0751  -0.0151 -0.0298 50  TRP   B CZ2 
589  C CZ2 B TRP   B 41  ? 0.8280 0.6690 0.5266 0.0806  -0.0036 -0.0307 50  TRP   B CZ2 
590  C CZ3 A TRP   B 41  ? 0.8041 0.6561 0.5703 0.0706  -0.0217 -0.0137 50  TRP   B CZ3 
591  C CZ3 B TRP   B 41  ? 0.8229 0.6796 0.5205 0.0868  0.0125  -0.0205 50  TRP   B CZ3 
592  C CH2 A TRP   B 41  ? 0.8201 0.6583 0.5617 0.0691  -0.0244 -0.0267 50  TRP   B CH2 
593  C CH2 B TRP   B 41  ? 0.8312 0.6785 0.5174 0.0840  0.0068  -0.0302 50  TRP   B CH2 
594  N N   . HIS   B 42  ? 0.7602 0.6340 0.5562 0.1034  0.0118  0.0184  51  HIS   B N   
595  C CA  . HIS   B 42  ? 0.7641 0.6383 0.5796 0.0959  0.0128  0.0233  51  HIS   B CA  
596  C C   . HIS   B 42  ? 0.7834 0.6434 0.6021 0.0988  0.0214  0.0263  51  HIS   B C   
597  O O   . HIS   B 42  ? 0.7842 0.6374 0.6176 0.0900  0.0213  0.0302  51  HIS   B O   
598  C CB  . HIS   B 42  ? 0.7495 0.6461 0.5842 0.0969  0.0125  0.0346  51  HIS   B CB  
599  C CG  . HIS   B 42  ? 0.7436 0.6502 0.5798 0.1112  0.0228  0.0453  51  HIS   B CG  
600  N ND1 . HIS   B 42  ? 0.7558 0.6695 0.5796 0.1247  0.0212  0.0449  51  HIS   B ND1 
601  C CD2 . HIS   B 42  ? 0.7448 0.6534 0.5910 0.1143  0.0336  0.0566  51  HIS   B CD2 
602  C CE1 . HIS   B 42  ? 0.7542 0.6745 0.5788 0.1373  0.0306  0.0538  51  HIS   B CE1 
603  N NE2 . HIS   B 42  ? 0.7547 0.6733 0.5918 0.1316  0.0394  0.0622  51  HIS   B NE2 
604  N N   . VAL   B 43  ? 0.7997 0.6534 0.6055 0.1105  0.0269  0.0246  52  VAL   B N   
605  C CA  . VAL   B 43  ? 0.8217 0.6601 0.6272 0.1160  0.0332  0.0270  52  VAL   B CA  
606  C C   . VAL   B 43  ? 0.8423 0.6605 0.6423 0.1111  0.0299  0.0142  52  VAL   B C   
607  O O   . VAL   B 43  ? 0.8487 0.6497 0.6558 0.1062  0.0294  0.0161  52  VAL   B O   
608  C CB  . VAL   B 43  ? 0.8375 0.6783 0.6318 0.1323  0.0375  0.0285  52  VAL   B CB  
609  C CG1 . VAL   B 43  ? 0.8527 0.6759 0.6437 0.1403  0.0418  0.0298  52  VAL   B CG1 
610  C CG2 . VAL   B 43  ? 0.8365 0.6935 0.6321 0.1406  0.0399  0.0395  52  VAL   B CG2 
611  N N   . THR   B 44  ? 0.8494 0.6695 0.6364 0.1123  0.0275  0.0016  53  THR   B N   
612  C CA  . THR   B 44  ? 0.8646 0.6699 0.6424 0.1122  0.0260  -0.0126 53  THR   B CA  
613  C C   . THR   B 44  ? 0.8902 0.6918 0.6616 0.1013  0.0180  -0.0223 53  THR   B C   
614  O O   . THR   B 44  ? 0.9079 0.6918 0.6720 0.1014  0.0147  -0.0344 53  THR   B O   
615  C CB  . THR   B 44  ? 0.8685 0.6826 0.6365 0.1222  0.0309  -0.0198 53  THR   B CB  
616  O OG1 . THR   B 44  ? 0.8661 0.6960 0.6264 0.1171  0.0296  -0.0212 53  THR   B OG1 
617  C CG2 . THR   B 44  ? 0.8689 0.6874 0.6420 0.1341  0.0352  -0.0121 53  THR   B CG2 
618  N N   . LYS   B 45  ? 0.8911 0.7075 0.6619 0.0945  0.0134  -0.0186 54  LYS   B N   
619  C CA  . LYS   B 45  ? 0.9080 0.7224 0.6687 0.0857  0.0038  -0.0274 54  LYS   B CA  
620  C C   . LYS   B 45  ? 0.9192 0.7325 0.6549 0.0903  0.0066  -0.0401 54  LYS   B C   
621  O O   . LYS   B 45  ? 0.9300 0.7347 0.6503 0.0866  -0.0006 -0.0512 54  LYS   B O   
622  C CB  . LYS   B 45  ? 0.9433 0.7399 0.7137 0.0768  -0.0059 -0.0324 54  LYS   B CB  
623  C CG  . LYS   B 45  ? 0.9923 0.7942 0.7912 0.0692  -0.0074 -0.0178 54  LYS   B CG  
624  C CD  . LYS   B 45  ? 1.0524 0.8770 0.8608 0.0637  -0.0131 -0.0107 54  LYS   B CD  
625  C CE  . LYS   B 45  ? 1.1071 0.9415 0.9479 0.0548  -0.0145 0.0025  54  LYS   B CE  
626  N NZ  . LYS   B 45  ? 1.1441 0.9805 0.9951 0.0615  -0.0004 0.0165  54  LYS   B NZ  
627  N N   . GLY   B 46  ? 0.9116 0.7350 0.6439 0.0983  0.0167  -0.0383 55  GLY   B N   
628  C CA  . GLY   B 46  ? 0.9153 0.7447 0.6294 0.1026  0.0233  -0.0472 55  GLY   B CA  
629  C C   . GLY   B 46  ? 0.9213 0.7409 0.6320 0.1125  0.0286  -0.0601 55  GLY   B C   
630  O O   . GLY   B 46  ? 0.9259 0.7554 0.6241 0.1183  0.0365  -0.0679 55  GLY   B O   
631  N N   . ALA   B 47  ? 0.9238 0.7242 0.6455 0.1149  0.0246  -0.0619 56  ALA   B N   
632  C CA  . ALA   B 47  ? 0.9373 0.7222 0.6550 0.1263  0.0267  -0.0749 56  ALA   B CA  
633  C C   . ALA   B 47  ? 0.9390 0.7382 0.6641 0.1393  0.0374  -0.0744 56  ALA   B C   
634  O O   . ALA   B 47  ? 0.9346 0.7488 0.6719 0.1386  0.0407  -0.0622 56  ALA   B O   
635  C CB  . ALA   B 47  ? 0.9437 0.7005 0.6727 0.1235  0.0180  -0.0733 56  ALA   B CB  
636  N N   . ALA   B 48  ? 0.9446 0.7395 0.6628 0.1525  0.0413  -0.0890 57  ALA   B N   
637  C CA  . ALA   B 48  ? 0.9489 0.7597 0.6780 0.1662  0.0498  -0.0902 57  ALA   B CA  
638  C C   . ALA   B 48  ? 0.9639 0.7575 0.7074 0.1721  0.0453  -0.0824 57  ALA   B C   
639  O O   . ALA   B 48  ? 0.9807 0.7453 0.7232 0.1686  0.0375  -0.0802 57  ALA   B O   
640  C CB  . ALA   B 48  ? 0.9558 0.7683 0.6741 0.1814  0.0551  -0.1091 57  ALA   B CB  
641  N N   . LEU   B 49  ? 0.9549 0.7661 0.7118 0.1808  0.0496  -0.0774 58  LEU   B N   
642  C CA  . LEU   B 49  ? 0.9629 0.7594 0.7289 0.1896  0.0455  -0.0696 58  LEU   B CA  
643  C C   . LEU   B 49  ? 0.9771 0.7751 0.7482 0.2098  0.0468  -0.0809 58  LEU   B C   
644  O O   . LEU   B 49  ? 0.9690 0.7905 0.7427 0.2162  0.0533  -0.0926 58  LEU   B O   
645  C CB  . LEU   B 49  ? 0.9485 0.7616 0.7236 0.1857  0.0453  -0.0549 58  LEU   B CB  
646  C CG  . LEU   B 49  ? 0.9572 0.7747 0.7291 0.1694  0.0441  -0.0447 58  LEU   B CG  
647  C CD1 . LEU   B 49  ? 0.9549 0.7885 0.7335 0.1699  0.0430  -0.0346 58  LEU   B CD1 
648  C CD2 . LEU   B 49  ? 0.9724 0.7653 0.7412 0.1622  0.0400  -0.0376 58  LEU   B CD2 
649  N N   . ARG   B 50  ? 0.9978 0.7729 0.7708 0.2206  0.0411  -0.0763 59  ARG   B N   
650  C CA  . ARG   B 50  ? 1.0157 0.7896 0.7940 0.2421  0.0397  -0.0865 59  ARG   B CA  
651  C C   . ARG   B 50  ? 1.0251 0.8079 0.8135 0.2512  0.0362  -0.0762 59  ARG   B C   
652  O O   . ARG   B 50  ? 1.0305 0.7998 0.8140 0.2451  0.0330  -0.0607 59  ARG   B O   
653  C CB  . ARG   B 50  ? 1.0583 0.7887 0.8248 0.2500  0.0326  -0.0926 59  ARG   B CB  
654  C CG  . ARG   B 50  ? 1.1197 0.8389 0.8891 0.2747  0.0278  -0.1007 59  ARG   B CG  
655  C CD  . ARG   B 50  ? 1.1994 0.8708 0.9552 0.2825  0.0192  -0.1088 59  ARG   B CD  
656  N NE  . ARG   B 50  ? 1.2645 0.8976 1.0128 0.2667  0.0130  -0.0920 59  ARG   B NE  
657  C CZ  . ARG   B 50  ? 1.3111 0.9199 1.0578 0.2702  0.0082  -0.0751 59  ARG   B CZ  
658  N NH1 . ARG   B 50  ? 1.3010 0.9172 1.0505 0.2902  0.0064  -0.0740 59  ARG   B NH1 
659  N NH2 . ARG   B 50  ? 1.3318 0.9105 1.0744 0.2536  0.0052  -0.0582 59  ARG   B NH2 
660  N N   . SER   B 51  ? 1.0253 0.8340 0.8284 0.2660  0.0366  -0.0850 60  SER   B N   
661  C CA  . SER   B 51  ? 1.0448 0.8609 0.8570 0.2768  0.0296  -0.0780 60  SER   B CA  
662  C C   . SER   B 51  ? 1.0634 0.8765 0.8828 0.3014  0.0245  -0.0895 60  SER   B C   
663  O O   . SER   B 51  ? 1.0499 0.8983 0.8897 0.3101  0.0271  -0.1010 60  SER   B O   
664  C CB  . SER   B 51  ? 1.0448 0.9009 0.8743 0.2684  0.0313  -0.0760 60  SER   B CB  
665  O OG  . SER   B 51  ? 1.0724 0.9315 0.9085 0.2800  0.0211  -0.0710 60  SER   B OG  
666  N N   . GLY   B 52  ? 1.0893 0.8606 0.8931 0.3122  0.0175  -0.0859 61  GLY   B N   
667  C CA  . GLY   B 52  ? 1.1013 0.8605 0.9075 0.3377  0.0104  -0.0969 61  GLY   B CA  
668  C C   . GLY   B 52  ? 1.1084 0.8699 0.9154 0.3424  0.0162  -0.1157 61  GLY   B C   
669  O O   . GLY   B 52  ? 1.1280 0.8602 0.9185 0.3319  0.0176  -0.1165 61  GLY   B O   
670  N N   . GLU   B 53  ? 1.0875 0.8872 0.9147 0.3577  0.0197  -0.1313 62  GLU   B N   
671  C CA  . GLU   B 53  ? 1.0859 0.8959 0.9124 0.3652  0.0279  -0.1506 62  GLU   B CA  
672  C C   . GLU   B 53  ? 1.0619 0.9132 0.8949 0.3452  0.0431  -0.1517 62  GLU   B C   
673  O O   . GLU   B 53  ? 1.0679 0.9212 0.8900 0.3466  0.0510  -0.1648 62  GLU   B O   
674  C CB  . GLU   B 53  ? 1.1093 0.9418 0.9544 0.3952  0.0258  -0.1672 62  GLU   B CB  
675  C CG  . GLU   B 53  ? 1.2109 0.9953 1.0380 0.4188  0.0155  -0.1792 62  GLU   B CG  
676  C CD  . GLU   B 53  ? 1.2986 1.1071 1.1456 0.4520  0.0122  -0.1962 62  GLU   B CD  
677  O OE1 . GLU   B 53  ? 1.2928 1.1392 1.1667 0.4577  0.0098  -0.1919 62  GLU   B OE1 
678  O OE2 . GLU   B 53  ? 1.3439 1.1333 1.1803 0.4733  0.0104  -0.2149 62  GLU   B OE2 
679  N N   . GLY   B 54  ? 1.0342 0.9149 0.8817 0.3283  0.0458  -0.1382 63  GLY   B N   
680  C CA  . GLY   B 54  ? 1.0129 0.9303 0.8670 0.3083  0.0585  -0.1354 63  GLY   B CA  
681  C C   . GLY   B 54  ? 1.0163 0.9096 0.8458 0.2865  0.0608  -0.1279 63  GLY   B C   
682  O O   . GLY   B 54  ? 1.0405 0.8921 0.8532 0.2820  0.0522  -0.1205 63  GLY   B O   
683  N N   . ARG   B 55  ? 0.9890 0.9098 0.8173 0.2725  0.0723  -0.1283 64  ARG   B N   
684  C CA  . ARG   B 55  ? 0.9908 0.8922 0.7963 0.2529  0.0732  -0.1223 64  ARG   B CA  
685  C C   . ARG   B 55  ? 0.9558 0.8829 0.7685 0.2314  0.0774  -0.1080 64  ARG   B C   
686  O O   . ARG   B 55  ? 0.9400 0.9070 0.7696 0.2291  0.0864  -0.1076 64  ARG   B O   
687  C CB  . ARG   B 55  ? 1.0172 0.9155 0.8026 0.2585  0.0804  -0.1384 64  ARG   B CB  
688  C CG  . ARG   B 55  ? 1.0838 0.9576 0.8436 0.2413  0.0775  -0.1356 64  ARG   B CG  
689  C CD  . ARG   B 55  ? 1.1423 1.0273 0.8819 0.2467  0.0869  -0.1509 64  ARG   B CD  
690  N NE  . ARG   B 55  ? 1.2060 1.0675 0.9193 0.2321  0.0815  -0.1506 64  ARG   B NE  
691  C CZ  . ARG   B 55  ? 1.2528 1.0827 0.9416 0.2394  0.0743  -0.1666 64  ARG   B CZ  
692  N NH1 . ARG   B 55  ? 1.2606 1.0753 0.9458 0.2620  0.0720  -0.1842 64  ARG   B NH1 
693  N NH2 . ARG   B 55  ? 1.2505 1.0622 0.9182 0.2252  0.0672  -0.1661 64  ARG   B NH2 
694  N N   . LEU   B 56  ? 0.9406 0.8453 0.7420 0.2160  0.0707  -0.0958 65  LEU   B N   
695  C CA  . LEU   B 56  ? 0.9166 0.8385 0.7210 0.1974  0.0722  -0.0831 65  LEU   B CA  
696  C C   . LEU   B 56  ? 0.9146 0.8289 0.6963 0.1847  0.0757  -0.0837 65  LEU   B C   
697  O O   . LEU   B 56  ? 0.9272 0.8116 0.6938 0.1812  0.0690  -0.0838 65  LEU   B O   
698  C CB  . LEU   B 56  ? 0.9189 0.8246 0.7259 0.1920  0.0616  -0.0696 65  LEU   B CB  
699  C CG  . LEU   B 56  ? 0.9288 0.8303 0.7488 0.2066  0.0543  -0.0684 65  LEU   B CG  
700  C CD1 . LEU   B 56  ? 0.9427 0.8253 0.7562 0.2025  0.0458  -0.0554 65  LEU   B CD1 
701  C CD2 . LEU   B 56  ? 0.9159 0.8522 0.7606 0.2105  0.0551  -0.0706 65  LEU   B CD2 
702  N N   . ASP   B 57  ? 0.8973 0.8389 0.6770 0.1776  0.0858  -0.0836 66  ASP   B N   
703  C CA  . ASP   B 57  ? 0.9045 0.8402 0.6587 0.1670  0.0885  -0.0838 66  ASP   B CA  
704  C C   . ASP   B 57  ? 0.8839 0.8238 0.6383 0.1486  0.0847  -0.0674 66  ASP   B C   
705  O O   . ASP   B 57  ? 0.8762 0.8376 0.6494 0.1434  0.0867  -0.0583 66  ASP   B O   
706  C CB  . ASP   B 57  ? 0.9428 0.9051 0.6886 0.1731  0.1035  -0.0932 66  ASP   B CB  
707  C CG  . ASP   B 57  ? 1.0472 1.0036 0.7889 0.1948  0.1065  -0.1124 66  ASP   B CG  
708  O OD1 . ASP   B 57  ? 1.0886 1.0113 0.8084 0.1996  0.0983  -0.1229 66  ASP   B OD1 
709  O OD2 . ASP   B 57  ? 1.0623 1.0479 0.8243 0.2073  0.1157  -0.1176 66  ASP   B OD2 
710  N N   . PRO   B 58  ? 0.8713 0.7901 0.6066 0.1391  0.0771  -0.0637 67  PRO   B N   
711  C CA  . PRO   B 58  ? 0.8554 0.7757 0.5897 0.1244  0.0718  -0.0490 67  PRO   B CA  
712  C C   . PRO   B 58  ? 0.8339 0.7782 0.5645 0.1150  0.0808  -0.0415 67  PRO   B C   
713  O O   . PRO   B 58  ? 0.8417 0.8003 0.5599 0.1176  0.0924  -0.0475 67  PRO   B O   
714  C CB  . PRO   B 58  ? 0.8798 0.7762 0.5951 0.1190  0.0623  -0.0498 67  PRO   B CB  
715  C CG  . PRO   B 58  ? 0.8970 0.7832 0.5972 0.1274  0.0648  -0.0655 67  PRO   B CG  
716  C CD  . PRO   B 58  ? 0.8739 0.7659 0.5899 0.1416  0.0709  -0.0736 67  PRO   B CD  
717  N N   . TYR   B 59  ? 0.8044 0.7528 0.5453 0.1046  0.0755  -0.0279 68  TYR   B N   
718  C CA  . TYR   B 59  ? 0.7772 0.7447 0.5175 0.0925  0.0825  -0.0170 68  TYR   B CA  
719  C C   . TYR   B 59  ? 0.7796 0.7305 0.4989 0.0806  0.0737  -0.0059 68  TYR   B C   
720  O O   . TYR   B 59  ? 0.7926 0.7493 0.4918 0.0730  0.0804  -0.0004 68  TYR   B O   
721  C CB  . TYR   B 59  ? 0.7500 0.7348 0.5227 0.0896  0.0813  -0.0105 68  TYR   B CB  
722  C CG  . TYR   B 59  ? 0.7376 0.7433 0.5170 0.0742  0.0882  0.0031  68  TYR   B CG  
723  C CD1 . TYR   B 59  ? 0.7532 0.7438 0.5239 0.0600  0.0783  0.0174  68  TYR   B CD1 
724  C CD2 . TYR   B 59  ? 0.7258 0.7667 0.5235 0.0739  0.1041  0.0026  68  TYR   B CD2 
725  C CE1 . TYR   B 59  ? 0.7554 0.7610 0.5329 0.0436  0.0837  0.0325  68  TYR   B CE1 
726  C CE2 . TYR   B 59  ? 0.7268 0.7892 0.5352 0.0570  0.1116  0.0182  68  TYR   B CE2 
727  C CZ  . TYR   B 59  ? 0.7502 0.7926 0.5479 0.0408  0.1010  0.0339  68  TYR   B CZ  
728  O OH  . TYR   B 59  ? 0.7610 0.8208 0.5689 0.0219  0.1078  0.0518  68  TYR   B OH  
729  N N   . TRP   B 60  ? 0.7715 0.7028 0.4945 0.0805  0.0590  -0.0024 69  TRP   B N   
730  C CA  . TRP   B 60  ? 0.7782 0.6930 0.4852 0.0724  0.0475  0.0071  69  TRP   B CA  
731  C C   . TRP   B 60  ? 0.7747 0.6718 0.4817 0.0796  0.0362  0.0024  69  TRP   B C   
732  O O   . TRP   B 60  ? 0.7661 0.6620 0.4896 0.0884  0.0354  -0.0025 69  TRP   B O   
733  C CB  . TRP   B 60  ? 0.7767 0.6915 0.4962 0.0638  0.0406  0.0201  69  TRP   B CB  
734  C CG  . TRP   B 60  ? 0.7956 0.6894 0.5019 0.0603  0.0254  0.0283  69  TRP   B CG  
735  C CD1 . TRP   B 60  ? 0.8191 0.7039 0.5015 0.0518  0.0220  0.0369  69  TRP   B CD1 
736  C CD2 . TRP   B 60  ? 0.7981 0.6777 0.5116 0.0684  0.0117  0.0272  69  TRP   B CD2 
737  N NE1 . TRP   B 60  ? 0.8329 0.6986 0.5096 0.0546  0.0057  0.0405  69  TRP   B NE1 
738  C CE2 . TRP   B 60  ? 0.8203 0.6843 0.5166 0.0650  0.0001  0.0343  69  TRP   B CE2 
739  C CE3 . TRP   B 60  ? 0.7993 0.6784 0.5299 0.0800  0.0086  0.0210  69  TRP   B CE3 
740  C CZ2 . TRP   B 60  ? 0.8299 0.6813 0.5286 0.0736  -0.0136 0.0346  69  TRP   B CZ2 
741  C CZ3 . TRP   B 60  ? 0.8144 0.6809 0.5444 0.0878  -0.0035 0.0224  69  TRP   B CZ3 
742  C CH2 . TRP   B 60  ? 0.8241 0.6785 0.5399 0.0850  -0.0141 0.0286  69  TRP   B CH2 
743  N N   . GLY   B 61  ? 0.7817 0.6667 0.4714 0.0759  0.0273  0.0055  70  GLY   B N   
744  C CA  . GLY   B 61  ? 0.7898 0.6639 0.4839 0.0809  0.0172  0.0033  70  GLY   B CA  
745  C C   . GLY   B 61  ? 0.8020 0.6673 0.4807 0.0764  0.0053  0.0089  70  GLY   B C   
746  O O   . GLY   B 61  ? 0.8149 0.6785 0.4720 0.0699  0.0054  0.0120  70  GLY   B O   
747  N N   . ASP   B 62  ? 0.7968 0.6580 0.4857 0.0810  -0.0047 0.0109  71  ASP   B N   
748  C CA  . ASP   B 62  ? 0.8050 0.6604 0.4838 0.0795  -0.0181 0.0153  71  ASP   B CA  
749  C C   . ASP   B 62  ? 0.7982 0.6582 0.4960 0.0857  -0.0237 0.0132  71  ASP   B C   
750  O O   . ASP   B 62  ? 0.7880 0.6522 0.5028 0.0932  -0.0212 0.0153  71  ASP   B O   
751  C CB  . ASP   B 62  ? 0.8314 0.6793 0.5042 0.0792  -0.0259 0.0257  71  ASP   B CB  
752  C CG  . ASP   B 62  ? 0.9154 0.7548 0.5746 0.0795  -0.0410 0.0306  71  ASP   B CG  
753  O OD1 . ASP   B 62  ? 0.9191 0.7617 0.5911 0.0879  -0.0496 0.0298  71  ASP   B OD1 
754  O OD2 . ASP   B 62  ? 0.9675 0.7983 0.6031 0.0725  -0.0440 0.0360  71  ASP   B OD2 
755  N N   . VAL   B 63  ? 0.7971 0.6578 0.4923 0.0824  -0.0313 0.0093  72  VAL   B N   
756  C CA  . VAL   B 63  ? 0.7848 0.6545 0.5031 0.0850  -0.0359 0.0085  72  VAL   B CA  
757  C C   . VAL   B 63  ? 0.7842 0.6615 0.5126 0.0932  -0.0441 0.0160  72  VAL   B C   
758  O O   . VAL   B 63  ? 0.7753 0.6647 0.5263 0.0993  -0.0408 0.0187  72  VAL   B O   
759  C CB  . VAL   B 63  ? 0.7887 0.6569 0.5042 0.0776  -0.0442 0.0007  72  VAL   B CB  
760  C CG1 . VAL   B 63  ? 0.7807 0.6623 0.5221 0.0777  -0.0541 0.0028  72  VAL   B CG1 
761  C CG2 . VAL   B 63  ? 0.7970 0.6579 0.5120 0.0740  -0.0355 -0.0084 72  VAL   B CG2 
762  N N   . LYS   B 64  ? 0.7938 0.6633 0.5043 0.0947  -0.0542 0.0201  73  LYS   B N   
763  C CA  . LYS   B 64  ? 0.7957 0.6694 0.5134 0.1057  -0.0640 0.0254  73  LYS   B CA  
764  C C   . LYS   B 64  ? 0.8013 0.6736 0.5255 0.1158  -0.0575 0.0282  73  LYS   B C   
765  O O   . LYS   B 64  ? 0.7919 0.6769 0.5326 0.1274  -0.0571 0.0293  73  LYS   B O   
766  C CB  . LYS   B 64  ? 0.8253 0.6854 0.5200 0.1056  -0.0791 0.0292  73  LYS   B CB  
767  C CG  . LYS   B 64  ? 0.8522 0.7205 0.5575 0.1180  -0.0932 0.0313  73  LYS   B CG  
768  C CD  . LYS   B 64  ? 0.9120 0.7592 0.5914 0.1205  -0.1086 0.0366  73  LYS   B CD  
769  C CE  . LYS   B 64  ? 0.9538 0.8095 0.6414 0.1333  -0.1254 0.0367  73  LYS   B CE  
770  N NZ  . LYS   B 64  ? 1.0035 0.8328 0.6658 0.1396  -0.1414 0.0430  73  LYS   B NZ  
771  N N   . GLN   B 65  ? 0.8127 0.6718 0.5246 0.1119  -0.0523 0.0289  74  GLN   B N   
772  C CA  . GLN   B 65  ? 0.8156 0.6717 0.5333 0.1211  -0.0487 0.0295  74  GLN   B CA  
773  C C   . GLN   B 65  ? 0.8042 0.6735 0.5392 0.1257  -0.0357 0.0267  74  GLN   B C   
774  O O   . GLN   B 65  ? 0.8065 0.6772 0.5465 0.1380  -0.0338 0.0271  74  GLN   B O   
775  C CB  . GLN   B 65  ? 0.8548 0.6976 0.5615 0.1129  -0.0469 0.0310  74  GLN   B CB  
776  C CG  . GLN   B 65  ? 0.9324 0.7583 0.6208 0.1062  -0.0585 0.0375  74  GLN   B CG  
777  C CD  . GLN   B 65  ? 1.0078 0.8248 0.6927 0.0963  -0.0554 0.0414  74  GLN   B CD  
778  O OE1 . GLN   B 65  ? 1.0102 0.8281 0.7072 0.1004  -0.0530 0.0387  74  GLN   B OE1 
779  N NE2 . GLN   B 65  ? 1.0324 0.8417 0.7008 0.0829  -0.0559 0.0487  74  GLN   B NE2 
780  N N   . ASP   B 66  ? 0.7932 0.6685 0.5339 0.1164  -0.0279 0.0237  75  ASP   B N   
781  C CA  . ASP   B 66  ? 0.7801 0.6625 0.5353 0.1175  -0.0165 0.0222  75  ASP   B CA  
782  C C   . ASP   B 66  ? 0.7652 0.6412 0.5177 0.1209  -0.0090 0.0203  75  ASP   B C   
783  O O   . ASP   B 66  ? 0.7599 0.6389 0.5207 0.1294  -0.0026 0.0218  75  ASP   B O   
784  C CB  . ASP   B 66  ? 0.7980 0.6952 0.5706 0.1270  -0.0147 0.0273  75  ASP   B CB  
785  C CG  . ASP   B 66  ? 0.8559 0.7581 0.6435 0.1239  -0.0038 0.0289  75  ASP   B CG  
786  O OD1 . ASP   B 66  ? 0.8842 0.7807 0.6733 0.1119  -0.0033 0.0245  75  ASP   B OD1 
787  O OD2 . ASP   B 66  ? 0.8692 0.7786 0.6644 0.1341  0.0036  0.0346  75  ASP   B OD2 
788  N N   . LEU   B 67  ? 0.7558 0.6246 0.4973 0.1143  -0.0094 0.0178  76  LEU   B N   
789  C CA  . LEU   B 67  ? 0.7458 0.6128 0.4894 0.1168  -0.0036 0.0154  76  LEU   B CA  
790  C C   . LEU   B 67  ? 0.7376 0.6061 0.4777 0.1077  0.0043  0.0101  76  LEU   B C   
791  O O   . LEU   B 67  ? 0.7471 0.6148 0.4761 0.0990  0.0034  0.0091  76  LEU   B O   
792  C CB  . LEU   B 67  ? 0.7499 0.6109 0.4893 0.1192  -0.0123 0.0183  76  LEU   B CB  
793  C CG  . LEU   B 67  ? 0.7612 0.6185 0.5008 0.1331  -0.0209 0.0205  76  LEU   B CG  
794  C CD1 . LEU   B 67  ? 0.7672 0.6118 0.4998 0.1334  -0.0337 0.0222  76  LEU   B CD1 
795  C CD2 . LEU   B 67  ? 0.7658 0.6269 0.5122 0.1463  -0.0150 0.0187  76  LEU   B CD2 
796  N N   . VAL   B 68  ? 0.7219 0.5932 0.4696 0.1120  0.0116  0.0060  77  VAL   B N   
797  C CA  . VAL   B 68  ? 0.7164 0.5924 0.4624 0.1076  0.0204  -0.0006 77  VAL   B CA  
798  C C   . VAL   B 68  ? 0.7132 0.5967 0.4714 0.1134  0.0243  -0.0030 77  VAL   B C   
799  O O   . VAL   B 68  ? 0.7127 0.5933 0.4790 0.1234  0.0214  -0.0023 77  VAL   B O   
800  C CB  . VAL   B 68  ? 0.7194 0.5900 0.4633 0.1078  0.0244  -0.0072 77  VAL   B CB  
801  C CG1 . VAL   B 68  ? 0.7164 0.5812 0.4719 0.1169  0.0260  -0.0069 77  VAL   B CG1 
802  C CG2 . VAL   B 68  ? 0.7237 0.5975 0.4596 0.1056  0.0321  -0.0163 77  VAL   B CG2 
803  N N   . SER   B 69  ? 0.7120 0.6072 0.4716 0.1075  0.0303  -0.0049 78  SER   B N   
804  C CA  . SER   B 69  ? 0.7097 0.6177 0.4863 0.1118  0.0333  -0.0075 78  SER   B CA  
805  C C   . SER   B 69  ? 0.7192 0.6395 0.4986 0.1152  0.0456  -0.0167 78  SER   B C   
806  O O   . SER   B 69  ? 0.7241 0.6450 0.4889 0.1108  0.0522  -0.0199 78  SER   B O   
807  C CB  . SER   B 69  ? 0.7055 0.6215 0.4898 0.1021  0.0285  0.0000  78  SER   B CB  
808  O OG  . SER   B 69  ? 0.7098 0.6364 0.4870 0.0894  0.0366  0.0040  78  SER   B OG  
809  N N   . TYR   B 70  ? 0.7222 0.6508 0.5182 0.1256  0.0473  -0.0221 79  TYR   B N   
810  C CA  . TYR   B 70  ? 0.7342 0.6742 0.5348 0.1336  0.0576  -0.0326 79  TYR   B CA  
811  C C   . TYR   B 70  ? 0.7334 0.7020 0.5581 0.1342  0.0616  -0.0333 79  TYR   B C   
812  O O   . TYR   B 70  ? 0.7344 0.7061 0.5754 0.1343  0.0522  -0.0290 79  TYR   B O   
813  C CB  . TYR   B 70  ? 0.7445 0.6665 0.5447 0.1484  0.0545  -0.0390 79  TYR   B CB  
814  C CG  . TYR   B 70  ? 0.7750 0.6729 0.5570 0.1459  0.0524  -0.0387 79  TYR   B CG  
815  C CD1 . TYR   B 70  ? 0.7940 0.6793 0.5711 0.1409  0.0449  -0.0293 79  TYR   B CD1 
816  C CD2 . TYR   B 70  ? 0.7976 0.6868 0.5687 0.1486  0.0569  -0.0487 79  TYR   B CD2 
817  C CE1 . TYR   B 70  ? 0.8167 0.6855 0.5837 0.1367  0.0427  -0.0282 79  TYR   B CE1 
818  C CE2 . TYR   B 70  ? 0.8209 0.6883 0.5793 0.1437  0.0523  -0.0487 79  TYR   B CE2 
819  C CZ  . TYR   B 70  ? 0.8354 0.6948 0.5944 0.1367  0.0455  -0.0377 79  TYR   B CZ  
820  O OH  . TYR   B 70  ? 0.8599 0.7027 0.6128 0.1307  0.0406  -0.0370 79  TYR   B OH  
821  N N   . CYS   B 71  ? 0.7285 0.7194 0.5561 0.1347  0.0750  -0.0391 80  CYS   B N   
822  C CA  . CYS   B 71  ? 0.7162 0.7432 0.5716 0.1349  0.0826  -0.0399 80  CYS   B CA  
823  C C   . CYS   B 71  ? 0.6994 0.7442 0.5659 0.1154  0.0836  -0.0262 80  CYS   B C   
824  O O   . CYS   B 71  ? 0.6850 0.7646 0.5715 0.1108  0.0952  -0.0243 80  CYS   B O   
825  C CB  . CYS   B 71  ? 0.7304 0.7620 0.6106 0.1492  0.0741  -0.0458 80  CYS   B CB  
826  S SG  . CYS   B 71  ? 0.8271 0.8397 0.6966 0.1730  0.0746  -0.0608 80  CYS   B SG  
827  N N   . GLY   B 72  ? 0.6983 0.7202 0.5530 0.1044  0.0718  -0.0162 81  GLY   B N   
828  C CA  . GLY   B 72  ? 0.6919 0.7225 0.5546 0.0852  0.0698  -0.0021 81  GLY   B CA  
829  C C   . GLY   B 72  ? 0.7133 0.7122 0.5542 0.0772  0.0566  0.0065  81  GLY   B C   
830  O O   . GLY   B 72  ? 0.7287 0.7032 0.5503 0.0860  0.0503  0.0019  81  GLY   B O   
831  N N   . PRO   B 73  ? 0.7116 0.7109 0.5571 0.0601  0.0518  0.0199  82  PRO   B N   
832  C CA  . PRO   B 73  ? 0.7338 0.7015 0.5586 0.0543  0.0373  0.0277  82  PRO   B CA  
833  C C   . PRO   B 73  ? 0.7463 0.6927 0.5763 0.0650  0.0181  0.0229  82  PRO   B C   
834  O O   . PRO   B 73  ? 0.7409 0.6964 0.5936 0.0721  0.0130  0.0169  82  PRO   B O   
835  C CB  . PRO   B 73  ? 0.7341 0.7077 0.5669 0.0334  0.0365  0.0437  82  PRO   B CB  
836  C CG  . PRO   B 73  ? 0.7099 0.7169 0.5807 0.0295  0.0431  0.0430  82  PRO   B CG  
837  C CD  . PRO   B 73  ? 0.6810 0.7096 0.5521 0.0448  0.0595  0.0296  82  PRO   B CD  
838  N N   . TRP   B 74  ? 0.7602 0.6795 0.5682 0.0675  0.0071  0.0256  83  TRP   B N   
839  C CA  . TRP   B 74  ? 0.7700 0.6690 0.5764 0.0801  -0.0096 0.0215  83  TRP   B CA  
840  C C   . TRP   B 74  ? 0.7826 0.6793 0.6096 0.0764  -0.0248 0.0229  83  TRP   B C   
841  O O   . TRP   B 74  ? 0.7906 0.6834 0.6227 0.0601  -0.0306 0.0326  83  TRP   B O   
842  C CB  . TRP   B 74  ? 0.7764 0.6524 0.5585 0.0810  -0.0179 0.0262  83  TRP   B CB  
843  C CG  . TRP   B 74  ? 0.7802 0.6398 0.5567 0.0977  -0.0307 0.0212  83  TRP   B CG  
844  C CD1 . TRP   B 74  ? 0.7953 0.6371 0.5713 0.1023  -0.0489 0.0215  83  TRP   B CD1 
845  C CD2 . TRP   B 74  ? 0.7803 0.6400 0.5497 0.1130  -0.0257 0.0155  83  TRP   B CD2 
846  N NE1 . TRP   B 74  ? 0.8059 0.6394 0.5726 0.1220  -0.0540 0.0155  83  TRP   B NE1 
847  C CE2 . TRP   B 74  ? 0.7975 0.6433 0.5616 0.1276  -0.0389 0.0133  83  TRP   B CE2 
848  C CE3 . TRP   B 74  ? 0.7818 0.6507 0.5487 0.1155  -0.0119 0.0124  83  TRP   B CE3 
849  C CZ2 . TRP   B 74  ? 0.8039 0.6495 0.5613 0.1439  -0.0355 0.0104  83  TRP   B CZ2 
850  C CZ3 . TRP   B 74  ? 0.7929 0.6582 0.5560 0.1292  -0.0107 0.0100  83  TRP   B CZ3 
851  C CH2 . TRP   B 74  ? 0.8005 0.6566 0.5593 0.1429  -0.0208 0.0102  83  TRP   B CH2 
852  N N   . LYS   B 75  ? 0.7824 0.6802 0.6210 0.0908  -0.0323 0.0136  84  LYS   B N   
853  C CA  . LYS   B 75  ? 0.7830 0.6786 0.6424 0.0891  -0.0499 0.0119  84  LYS   B CA  
854  C C   . LYS   B 75  ? 0.8224 0.6873 0.6661 0.1018  -0.0717 0.0080  84  LYS   B C   
855  O O   . LYS   B 75  ? 0.8269 0.6809 0.6824 0.0975  -0.0911 0.0073  84  LYS   B O   
856  C CB  . LYS   B 75  ? 0.7651 0.6830 0.6479 0.0985  -0.0473 0.0028  84  LYS   B CB  
857  C CG  . LYS   B 75  ? 0.7612 0.7122 0.6613 0.0909  -0.0261 0.0036  84  LYS   B CG  
858  C CD  . LYS   B 75  ? 0.7596 0.7321 0.6870 0.0685  -0.0238 0.0129  84  LYS   B CD  
859  C CE  . LYS   B 75  ? 0.7599 0.7687 0.7010 0.0645  0.0000  0.0132  84  LYS   B CE  
860  N NZ  . LYS   B 75  ? 0.7582 0.7969 0.7334 0.0439  0.0042  0.0231  84  LYS   B NZ  
861  N N   . LEU   B 76  ? 0.8436 0.6960 0.6623 0.1185  -0.0692 0.0048  85  LEU   B N   
862  C CA  . LEU   B 76  ? 0.8651 0.6929 0.6661 0.1357  -0.0868 -0.0002 85  LEU   B CA  
863  C C   . LEU   B 76  ? 0.8985 0.7034 0.6882 0.1277  -0.1000 0.0056  85  LEU   B C   
864  O O   . LEU   B 76  ? 0.9039 0.7091 0.6842 0.1185  -0.0908 0.0134  85  LEU   B O   
865  C CB  . LEU   B 76  ? 0.8642 0.6922 0.6457 0.1554  -0.0766 -0.0032 85  LEU   B CB  
866  C CG  . LEU   B 76  ? 0.8621 0.7083 0.6513 0.1617  -0.0616 -0.0063 85  LEU   B CG  
867  C CD1 . LEU   B 76  ? 0.8722 0.7162 0.6435 0.1767  -0.0514 -0.0053 85  LEU   B CD1 
868  C CD2 . LEU   B 76  ? 0.8612 0.7100 0.6627 0.1706  -0.0726 -0.0138 85  LEU   B CD2 
869  N N   . ASP   B 77  ? 0.9231 0.7056 0.7125 0.1319  -0.1238 0.0013  86  ASP   B N   
870  C CA  . ASP   B 77  ? 0.9573 0.7122 0.7362 0.1249  -0.1400 0.0064  86  ASP   B CA  
871  C C   . ASP   B 77  ? 0.9887 0.7129 0.7487 0.1470  -0.1645 -0.0041 86  ASP   B C   
872  O O   . ASP   B 77  ? 1.0070 0.7029 0.7574 0.1438  -0.1817 -0.0015 86  ASP   B O   
873  C CB  . ASP   B 77  ? 0.9795 0.7334 0.7817 0.0967  -0.1463 0.0163  86  ASP   B CB  
874  C CG  . ASP   B 77  ? 1.0641 0.8220 0.8939 0.0920  -0.1608 0.0103  86  ASP   B CG  
875  O OD1 . ASP   B 77  ? 1.0744 0.8495 0.9109 0.1064  -0.1568 0.0001  86  ASP   B OD1 
876  O OD2 . ASP   B 77  ? 1.1044 0.8481 0.9505 0.0731  -0.1771 0.0166  86  ASP   B OD2 
877  N N   . ALA   B 78  ? 0.9945 0.7218 0.7455 0.1711  -0.1663 -0.0156 87  ALA   B N   
878  C CA  . ALA   B 78  ? 1.0200 0.7197 0.7474 0.1966  -0.1880 -0.0272 87  ALA   B CA  
879  C C   . ALA   B 78  ? 1.0416 0.7356 0.7442 0.2121  -0.1819 -0.0254 87  ALA   B C   
880  O O   . ALA   B 78  ? 1.0337 0.7496 0.7376 0.2067  -0.1594 -0.0171 87  ALA   B O   
881  C CB  . ALA   B 78  ? 1.0158 0.7219 0.7362 0.2193  -0.1901 -0.0388 87  ALA   B CB  
882  N N   . ALA   B 79  ? 1.0643 0.7293 0.7455 0.2319  -0.2033 -0.0343 88  ALA   B N   
883  C CA  . ALA   B 79  ? 1.0838 0.7464 0.7445 0.2492  -0.1992 -0.0337 88  ALA   B CA  
884  C C   . ALA   B 79  ? 1.1084 0.7571 0.7419 0.2856  -0.2119 -0.0481 88  ALA   B C   
885  O O   . ALA   B 79  ? 1.1232 0.7443 0.7484 0.2946  -0.2368 -0.0599 88  ALA   B O   
886  C CB  . ALA   B 79  ? 1.0959 0.7347 0.7566 0.2343  -0.2124 -0.0268 88  ALA   B CB  
887  N N   . TRP   B 80  ? 1.1115 0.7796 0.7310 0.3069  -0.1957 -0.0475 89  TRP   B N   
888  C CA  . TRP   B 80  ? 1.1344 0.7950 0.7251 0.3448  -0.2035 -0.0600 89  TRP   B CA  
889  C C   . TRP   B 80  ? 1.1652 0.7850 0.7405 0.3556  -0.2341 -0.0701 89  TRP   B C   
890  O O   . TRP   B 80  ? 1.1650 0.7744 0.7487 0.3400  -0.2391 -0.0627 89  TRP   B O   
891  C CB  . TRP   B 80  ? 1.1246 0.8196 0.7115 0.3601  -0.1780 -0.0535 89  TRP   B CB  
892  C CG  . TRP   B 80  ? 1.1429 0.8380 0.7007 0.4007  -0.1810 -0.0645 89  TRP   B CG  
893  C CD1 . TRP   B 80  ? 1.1669 0.8549 0.7004 0.4259  -0.1865 -0.0755 89  TRP   B CD1 
894  C CD2 . TRP   B 80  ? 1.1424 0.8502 0.6917 0.4228  -0.1762 -0.0653 89  TRP   B CD2 
895  N NE1 . TRP   B 80  ? 1.1775 0.8715 0.6847 0.4632  -0.1848 -0.0832 89  TRP   B NE1 
896  C CE2 . TRP   B 80  ? 1.1635 0.8720 0.6824 0.4620  -0.1777 -0.0770 89  TRP   B CE2 
897  C CE3 . TRP   B 80  ? 1.1391 0.8589 0.7030 0.4148  -0.1716 -0.0576 89  TRP   B CE3 
898  C CZ2 . TRP   B 80  ? 1.1687 0.8934 0.6744 0.4932  -0.1723 -0.0809 89  TRP   B CZ2 
899  C CZ3 . TRP   B 80  ? 1.1473 0.8824 0.7007 0.4451  -0.1686 -0.0619 89  TRP   B CZ3 
900  C CH2 . TRP   B 80  ? 1.1573 0.8967 0.6833 0.4838  -0.1678 -0.0732 89  TRP   B CH2 
901  N N   . ASP   B 81  ? 1.1939 0.7868 0.7449 0.3821  -0.2567 -0.0871 90  ASP   B N   
902  C CA  . ASP   B 81  ? 1.2302 0.7769 0.7648 0.3936  -0.2901 -0.0990 90  ASP   B CA  
903  C C   . ASP   B 81  ? 1.2526 0.7990 0.7645 0.4259  -0.2901 -0.1048 90  ASP   B C   
904  O O   . ASP   B 81  ? 1.2752 0.7803 0.7700 0.4402  -0.3191 -0.1163 90  ASP   B O   
905  C CB  . ASP   B 81  ? 1.2616 0.7733 0.7797 0.4077  -0.3201 -0.1173 90  ASP   B CB  
906  C CG  . ASP   B 81  ? 1.3176 0.8414 0.8047 0.4467  -0.3146 -0.1308 90  ASP   B CG  
907  O OD1 . ASP   B 81  ? 1.3179 0.8802 0.7980 0.4624  -0.2847 -0.1241 90  ASP   B OD1 
908  O OD2 . ASP   B 81  ? 1.3521 0.8469 0.8218 0.4612  -0.3408 -0.1476 90  ASP   B OD2 
909  N N   . GLY   B 82  ? 1.2415 0.8333 0.7553 0.4373  -0.2592 -0.0971 91  GLY   B N   
910  C CA  . GLY   B 82  ? 1.2558 0.8585 0.7551 0.4677  -0.2555 -0.1013 91  GLY   B CA  
911  C C   . GLY   B 82  ? 1.2798 0.8763 0.7427 0.5147  -0.2632 -0.1200 91  GLY   B C   
912  O O   . GLY   B 82  ? 1.2807 0.8890 0.7307 0.5449  -0.2601 -0.1253 91  GLY   B O   
913  N N   . LEU   B 83  ? 1.2937 0.8740 0.7391 0.5233  -0.2732 -0.1306 92  LEU   B N   
914  C CA  . LEU   B 83  ? 1.3162 0.8863 0.7203 0.5698  -0.2829 -0.1501 92  LEU   B CA  
915  C C   . LEU   B 83  ? 1.3172 0.9119 0.7080 0.5803  -0.2644 -0.1491 92  LEU   B C   
916  O O   . LEU   B 83  ? 1.3292 0.9394 0.6879 0.6196  -0.2545 -0.1568 92  LEU   B O   
917  C CB  . LEU   B 83  ? 1.3503 0.8564 0.7331 0.5789  -0.3284 -0.1713 92  LEU   B CB  
918  C CG  . LEU   B 83  ? 1.3911 0.8574 0.7728 0.5805  -0.3556 -0.1776 92  LEU   B CG  
919  C CD1 . LEU   B 83  ? 1.4309 0.8317 0.7889 0.5916  -0.4015 -0.1997 92  LEU   B CD1 
920  C CD2 . LEU   B 83  ? 1.4008 0.8878 0.7645 0.6194  -0.3446 -0.1828 92  LEU   B CD2 
921  N N   . SER   B 84  ? 1.3054 0.9007 0.7171 0.5483  -0.2621 -0.1407 93  SER   B N   
922  C CA  . SER   B 84  ? 1.3035 0.9137 0.6999 0.5587  -0.2506 -0.1408 93  SER   B CA  
923  C C   . SER   B 84  ? 1.2838 0.9468 0.6932 0.5527  -0.2081 -0.1200 93  SER   B C   
924  O O   . SER   B 84  ? 1.2703 0.9594 0.7121 0.5277  -0.1879 -0.1035 93  SER   B O   
925  C CB  . SER   B 84  ? 1.3131 0.8998 0.7264 0.5311  -0.2705 -0.1434 93  SER   B CB  
926  O OG  . SER   B 84  ? 1.3447 0.8845 0.7620 0.5216  -0.3086 -0.1564 93  SER   B OG  
927  N N   . GLU   B 85  ? 1.2807 0.9564 0.6634 0.5752  -0.1963 -0.1205 94  GLU   B N   
928  C CA  . GLU   B 85  ? 1.2554 0.9744 0.6481 0.5684  -0.1586 -0.0996 94  GLU   B CA  
929  C C   . GLU   B 85  ? 1.2288 0.9467 0.6544 0.5289  -0.1570 -0.0896 94  GLU   B C   
930  O O   . GLU   B 85  ? 1.2407 0.9288 0.6684 0.5193  -0.1833 -0.1007 94  GLU   B O   
931  C CB  . GLU   B 85  ? 1.2942 1.0221 0.6418 0.6070  -0.1482 -0.1023 94  GLU   B CB  
932  C CG  . GLU   B 85  ? 1.3520 1.1000 0.6720 0.6458  -0.1352 -0.1053 94  GLU   B CG  
933  C CD  . GLU   B 85  ? 1.4167 1.1857 0.6947 0.6816  -0.1140 -0.1007 94  GLU   B CD  
934  O OE1 . GLU   B 85  ? 1.4261 1.1896 0.6916 0.6781  -0.1115 -0.0953 94  GLU   B OE1 
935  O OE2 . GLU   B 85  ? 1.4350 1.2276 0.6921 0.7142  -0.0993 -0.1016 94  GLU   B OE2 
936  N N   . VAL   B 86  ? 1.1899 0.9411 0.6439 0.5058  -0.1275 -0.0693 95  VAL   B N   
937  C CA  . VAL   B 86  ? 1.1608 0.9153 0.6456 0.4710  -0.1220 -0.0595 95  VAL   B CA  
938  C C   . VAL   B 86  ? 1.1451 0.9208 0.6205 0.4775  -0.0974 -0.0461 95  VAL   B C   
939  O O   . VAL   B 86  ? 1.1528 0.9418 0.5990 0.5064  -0.0835 -0.0426 95  VAL   B O   
940  C CB  . VAL   B 86  ? 1.1443 0.9137 0.6688 0.4373  -0.1111 -0.0480 95  VAL   B CB  
941  C CG1 . VAL   B 86  ? 1.1578 0.9045 0.6861 0.4341  -0.1344 -0.0584 95  VAL   B CG1 
942  C CG2 . VAL   B 86  ? 1.1307 0.9377 0.6638 0.4388  -0.0798 -0.0316 95  VAL   B CG2 
943  N N   . GLN   B 87  ? 1.1230 0.9007 0.6210 0.4524  -0.0924 -0.0385 96  GLN   B N   
944  C CA  . GLN   B 87  ? 1.1082 0.9008 0.5995 0.4555  -0.0708 -0.0244 96  GLN   B CA  
945  C C   . GLN   B 87  ? 1.0730 0.8826 0.6029 0.4215  -0.0521 -0.0093 96  GLN   B C   
946  O O   . GLN   B 87  ? 1.0676 0.8687 0.6225 0.3976  -0.0624 -0.0136 96  GLN   B O   
947  C CB  . GLN   B 87  ? 1.1339 0.9058 0.6032 0.4693  -0.0878 -0.0335 96  GLN   B CB  
948  C CG  . GLN   B 87  ? 1.1842 0.9549 0.6046 0.5081  -0.0833 -0.0337 96  GLN   B CG  
949  C CD  . GLN   B 87  ? 1.2356 0.9825 0.6293 0.5257  -0.1057 -0.0457 96  GLN   B CD  
950  O OE1 . GLN   B 87  ? 1.2364 0.9769 0.6510 0.5080  -0.1140 -0.0462 96  GLN   B OE1 
951  N NE2 . GLN   B 87  ? 1.2622 0.9965 0.6082 0.5629  -0.1167 -0.0567 96  GLN   B NE2 
952  N N   . LEU   B 88  ? 1.0450 0.8793 0.5804 0.4193  -0.0249 0.0081  97  LEU   B N   
953  C CA  . LEU   B 88  ? 1.0181 0.8654 0.5866 0.3893  -0.0084 0.0216  97  LEU   B CA  
954  C C   . LEU   B 88  ? 1.0163 0.8550 0.5776 0.3895  -0.0037 0.0279  97  LEU   B C   
955  O O   . LEU   B 88  ? 1.0283 0.8703 0.5639 0.4093  0.0080  0.0377  97  LEU   B O   
956  C CB  . LEU   B 88  ? 1.0009 0.8774 0.5803 0.3870  0.0164  0.0381  97  LEU   B CB  
957  C CG  . LEU   B 88  ? 0.9982 0.8864 0.6068 0.3598  0.0345  0.0540  97  LEU   B CG  
958  C CD1 . LEU   B 88  ? 0.9918 0.8747 0.6305 0.3310  0.0252  0.0472  97  LEU   B CD1 
959  C CD2 . LEU   B 88  ? 0.9902 0.9082 0.6083 0.3607  0.0582  0.0720  97  LEU   B CD2 
960  N N   . LEU   B 89  ? 0.9978 0.8261 0.5799 0.3694  -0.0124 0.0229  98  LEU   B N   
961  C CA  . LEU   B 89  ? 0.9941 0.8143 0.5722 0.3701  -0.0087 0.0284  98  LEU   B CA  
962  C C   . LEU   B 89  ? 0.9815 0.8142 0.5781 0.3522  0.0148  0.0464  98  LEU   B C   
963  O O   . LEU   B 89  ? 0.9723 0.8055 0.5965 0.3285  0.0164  0.0458  98  LEU   B O   
964  C CB  . LEU   B 89  ? 0.9907 0.7990 0.5861 0.3585  -0.0273 0.0150  98  LEU   B CB  
965  C CG  . LEU   B 89  ? 1.0064 0.8060 0.6011 0.3611  -0.0278 0.0173  98  LEU   B CG  
966  C CD1 . LEU   B 89  ? 1.0279 0.8216 0.5899 0.3831  -0.0169 0.0305  98  LEU   B CD1 
967  C CD2 . LEU   B 89  ? 1.0121 0.8022 0.6107 0.3661  -0.0526 0.0005  98  LEU   B CD2 
968  N N   . ALA   B 90  ? 0.9789 0.8226 0.5604 0.3636  0.0332  0.0623  99  ALA   B N   
969  C CA  . ALA   B 90  ? 0.9741 0.8297 0.5757 0.3456  0.0544  0.0809  99  ALA   B CA  
970  C C   . ALA   B 90  ? 0.9889 0.8276 0.5897 0.3401  0.0585  0.0895  99  ALA   B C   
971  O O   . ALA   B 90  ? 1.0044 0.8326 0.5761 0.3599  0.0601  0.0963  99  ALA   B O   
972  C CB  . ALA   B 90  ? 0.9686 0.8455 0.5587 0.3583  0.0737  0.0973  99  ALA   B CB  
973  N N   . VAL   B 91  ? 0.9855 0.8200 0.6154 0.3150  0.0593  0.0890  100 VAL   B N   
974  C CA  . VAL   B 91  ? 1.0056 0.8215 0.6374 0.3092  0.0623  0.0962  100 VAL   B CA  
975  C C   . VAL   B 91  ? 1.0170 0.8392 0.6679 0.2901  0.0804  0.1150  100 VAL   B C   
976  O O   . VAL   B 91  ? 1.0105 0.8348 0.6891 0.2677  0.0796  0.1106  100 VAL   B O   
977  C CB  . VAL   B 91  ? 1.0068 0.8119 0.6561 0.2982  0.0478  0.0786  100 VAL   B CB  
978  C CG1 . VAL   B 91  ? 1.0214 0.8051 0.6686 0.2988  0.0484  0.0836  100 VAL   B CG1 
979  C CG2 . VAL   B 91  ? 1.0105 0.8160 0.6514 0.3111  0.0291  0.0603  100 VAL   B CG2 
980  N N   . PRO   B 92  ? 1.0305 0.8568 0.6671 0.2983  0.0964  0.1367  101 PRO   B N   
981  C CA  . PRO   B 92  ? 1.0296 0.8652 0.6901 0.2776  0.1130  0.1563  101 PRO   B CA  
982  C C   . PRO   B 92  ? 1.0522 0.8597 0.7211 0.2632  0.1137  0.1653  101 PRO   B C   
983  O O   . PRO   B 92  ? 1.0729 0.8550 0.7203 0.2761  0.1067  0.1634  101 PRO   B O   
984  C CB  . PRO   B 92  ? 1.0362 0.8905 0.6772 0.2939  0.1313  0.1774  101 PRO   B CB  
985  C CG  . PRO   B 92  ? 1.0510 0.9034 0.6537 0.3254  0.1218  0.1648  101 PRO   B CG  
986  C CD  . PRO   B 92  ? 1.0389 0.8643 0.6370 0.3268  0.1006  0.1449  101 PRO   B CD  
987  N N   . PRO   B 93  ? 1.0468 0.8568 0.7465 0.2376  0.1205  0.1748  102 PRO   B N   
988  C CA  . PRO   B 93  ? 1.0595 0.8370 0.7663 0.2241  0.1187  0.1824  102 PRO   B CA  
989  C C   . PRO   B 93  ? 1.0870 0.8441 0.7674 0.2367  0.1281  0.2056  102 PRO   B C   
990  O O   . PRO   B 93  ? 1.0942 0.8689 0.7682 0.2402  0.1453  0.2284  102 PRO   B O   
991  C CB  . PRO   B 93  ? 1.0498 0.8388 0.7941 0.1954  0.1246  0.1911  102 PRO   B CB  
992  C CG  . PRO   B 93  ? 1.0384 0.8620 0.7973 0.1932  0.1221  0.1770  102 PRO   B CG  
993  C CD  . PRO   B 93  ? 1.0213 0.8618 0.7517 0.2202  0.1266  0.1771  102 PRO   B CD  
994  N N   . GLY   B 94  ? 1.1009 0.8228 0.7643 0.2458  0.1171  0.2001  103 GLY   B N   
995  C CA  . GLY   B 94  ? 1.1188 0.8139 0.7526 0.2596  0.1224  0.2213  103 GLY   B CA  
996  C C   . GLY   B 94  ? 1.1282 0.8318 0.7215 0.2903  0.1251  0.2249  103 GLY   B C   
997  O O   . GLY   B 94  ? 1.1448 0.8233 0.7063 0.3067  0.1256  0.2388  103 GLY   B O   
998  N N   . GLU   B 95  ? 1.1188 0.8552 0.7102 0.2995  0.1256  0.2126  104 GLU   B N   
999  C CA  . GLU   B 95  ? 1.1352 0.8804 0.6871 0.3301  0.1258  0.2123  104 GLU   B CA  
1000 C C   . GLU   B 95  ? 1.1410 0.8809 0.6839 0.3457  0.1022  0.1818  104 GLU   B C   
1001 O O   . GLU   B 95  ? 1.1301 0.8721 0.7017 0.3311  0.0906  0.1618  104 GLU   B O   
1002 C CB  . GLU   B 95  ? 1.1498 0.9342 0.7038 0.3325  0.1423  0.2205  104 GLU   B CB  
1003 C CG  . GLU   B 95  ? 1.2027 1.0007 0.7774 0.3124  0.1660  0.2507  104 GLU   B CG  
1004 C CD  . GLU   B 95  ? 1.2793 1.1221 0.8609 0.3159  0.1842  0.2600  104 GLU   B CD  
1005 O OE1 . GLU   B 95  ? 1.2969 1.1585 0.8711 0.3315  0.1760  0.2392  104 GLU   B OE1 
1006 O OE2 . GLU   B 95  ? 1.2959 1.1555 0.8917 0.3035  0.2062  0.2884  104 GLU   B OE2 
1007 N N   . ARG   B 96  ? 1.1554 0.8891 0.6588 0.3752  0.0949  0.1788  105 ARG   B N   
1008 C CA  . ARG   B 96  ? 1.1695 0.8986 0.6648 0.3909  0.0707  0.1515  105 ARG   B CA  
1009 C C   . ARG   B 96  ? 1.1668 0.9220 0.6757 0.3890  0.0643  0.1323  105 ARG   B C   
1010 O O   . ARG   B 96  ? 1.1663 0.9432 0.6750 0.3878  0.0787  0.1410  105 ARG   B O   
1011 C CB  . ARG   B 96  ? 1.2119 0.9252 0.6576 0.4239  0.0640  0.1562  105 ARG   B CB  
1012 C CG  . ARG   B 96  ? 1.2600 0.9627 0.6964 0.4417  0.0359  0.1309  105 ARG   B CG  
1013 C CD  . ARG   B 96  ? 1.3254 1.0009 0.7212 0.4673  0.0279  0.1396  105 ARG   B CD  
1014 N NE  . ARG   B 96  ? 1.3841 1.0583 0.7320 0.4886  0.0425  0.1606  105 ARG   B NE  
1015 C CZ  . ARG   B 96  ? 1.4368 1.0918 0.7576 0.4944  0.0569  0.1885  105 ARG   B CZ  
1016 N NH1 . ARG   B 96  ? 1.4391 1.0700 0.7761 0.4808  0.0562  0.1977  105 ARG   B NH1 
1017 N NH2 . ARG   B 96  ? 1.4468 1.1053 0.7226 0.5145  0.0723  0.2081  105 ARG   B NH2 
1018 N N   . ALA   B 97  ? 1.1608 0.9148 0.6835 0.3885  0.0429  0.1071  106 ALA   B N   
1019 C CA  . ALA   B 97  ? 1.1541 0.9259 0.6877 0.3867  0.0332  0.0890  106 ALA   B CA  
1020 C C   . ALA   B 97  ? 1.1768 0.9522 0.6712 0.4152  0.0305  0.0883  106 ALA   B C   
1021 O O   . ALA   B 97  ? 1.1955 0.9557 0.6544 0.4394  0.0241  0.0908  106 ALA   B O   
1022 C CB  . ALA   B 97  ? 1.1466 0.9140 0.6993 0.3822  0.0107  0.0660  106 ALA   B CB  
1023 N N   . LYS   B 98  ? 1.1734 0.9677 0.6714 0.4148  0.0347  0.0848  107 LYS   B N   
1024 C CA  . LYS   B 98  ? 1.1946 0.9933 0.6537 0.4440  0.0343  0.0838  107 LYS   B CA  
1025 C C   . LYS   B 98  ? 1.1791 0.9900 0.6469 0.4449  0.0245  0.0671  107 LYS   B C   
1026 O O   . LYS   B 98  ? 1.1678 0.9966 0.6647 0.4256  0.0351  0.0710  107 LYS   B O   
1027 C CB  . LYS   B 98  ? 1.2391 1.0503 0.6819 0.4497  0.0634  0.1116  107 LYS   B CB  
1028 C CG  . LYS   B 98  ? 1.3164 1.1478 0.7321 0.4728  0.0753  0.1162  107 LYS   B CG  
1029 C CD  . LYS   B 98  ? 1.3784 1.2334 0.8042 0.4626  0.1085  0.1464  107 LYS   B CD  
1030 C CE  . LYS   B 98  ? 1.4057 1.2766 0.8866 0.4264  0.1159  0.1498  107 LYS   B CE  
1031 N NZ  . LYS   B 98  ? 1.4251 1.3207 0.9227 0.4138  0.1453  0.1787  107 LYS   B NZ  
1032 N N   . ASN   B 99  ? 1.1820 0.9803 0.6245 0.4673  0.0013  0.0478  108 ASN   B N   
1033 C CA  . ASN   B 99  ? 1.1776 0.9790 0.6240 0.4707  -0.0131 0.0303  108 ASN   B CA  
1034 C C   . ASN   B 99  ? 1.1812 0.9995 0.6024 0.4926  0.0022  0.0370  108 ASN   B C   
1035 O O   . ASN   B 99  ? 1.2039 1.0175 0.5810 0.5238  0.0033  0.0382  108 ASN   B O   
1036 C CB  . ASN   B 99  ? 1.2005 0.9782 0.6282 0.4876  -0.0463 0.0069  108 ASN   B CB  
1037 C CG  . ASN   B 99  ? 1.2246 0.9914 0.6836 0.4667  -0.0652 -0.0037 108 ASN   B CG  
1038 O OD1 . ASN   B 99  ? 1.2404 1.0068 0.7117 0.4563  -0.0582 0.0051  108 ASN   B OD1 
1039 N ND2 . ASN   B 99  ? 1.2187 0.9761 0.6908 0.4614  -0.0903 -0.0226 108 ASN   B ND2 
1040 N N   . ILE   B 100 ? 1.1593 0.9983 0.6065 0.4790  0.0129  0.0401  109 ILE   B N   
1041 C CA  . ILE   B 100 ? 1.1583 1.0192 0.5877 0.5007  0.0275  0.0450  109 ILE   B CA  
1042 C C   . ILE   B 100 ? 1.1588 1.0119 0.5862 0.5105  0.0050  0.0225  109 ILE   B C   
1043 O O   . ILE   B 100 ? 1.1450 0.9989 0.6075 0.4861  -0.0023 0.0173  109 ILE   B O   
1044 C CB  . ILE   B 100 ? 1.1428 1.0368 0.6066 0.4793  0.0566  0.0669  109 ILE   B CB  
1045 C CG1 . ILE   B 100 ? 1.1493 1.0442 0.6220 0.4627  0.0753  0.0893  109 ILE   B CG1 
1046 C CG2 . ILE   B 100 ? 1.1428 1.0671 0.5926 0.5031  0.0738  0.0732  109 ILE   B CG2 
1047 C CD1 . ILE   B 100 ? 1.1759 1.0727 0.6082 0.4880  0.0909  0.1049  109 ILE   B CD1 
1048 N N   . GLN   B 101 ? 1.1746 1.0176 0.5588 0.5470  -0.0066 0.0093  110 GLN   B N   
1049 C CA  . GLN   B 101 ? 1.1864 1.0155 0.5646 0.5594  -0.0308 -0.0132 110 GLN   B CA  
1050 C C   . GLN   B 101 ? 1.1732 1.0325 0.5600 0.5679  -0.0137 -0.0080 110 GLN   B C   
1051 O O   . GLN   B 101 ? 1.1688 1.0578 0.5416 0.5853  0.0132  0.0071  110 GLN   B O   
1052 C CB  . GLN   B 101 ? 1.2325 1.0334 0.5589 0.5969  -0.0549 -0.0330 110 GLN   B CB  
1053 C CG  . GLN   B 101 ? 1.2837 1.0587 0.6039 0.6075  -0.0873 -0.0588 110 GLN   B CG  
1054 C CD  . GLN   B 101 ? 1.3661 1.1053 0.6433 0.6354  -0.1185 -0.0803 110 GLN   B CD  
1055 O OE1 . GLN   B 101 ? 1.3960 1.1206 0.6708 0.6285  -0.1291 -0.0811 110 GLN   B OE1 
1056 N NE2 . GLN   B 101 ? 1.3853 1.1092 0.6272 0.6693  -0.1353 -0.0994 110 GLN   B NE2 
1057 N N   . THR   B 102 ? 1.1638 1.0171 0.5745 0.5560  -0.0292 -0.0193 111 THR   B N   
1058 C CA  . THR   B 102 ? 1.1543 1.0358 0.5767 0.5647  -0.0171 -0.0166 111 THR   B CA  
1059 C C   . THR   B 102 ? 1.1620 1.0181 0.5882 0.5664  -0.0469 -0.0372 111 THR   B C   
1060 O O   . THR   B 102 ? 1.1740 0.9957 0.6071 0.5485  -0.0723 -0.0480 111 THR   B O   
1061 C CB  . THR   B 102 ? 1.1486 1.0643 0.6193 0.5304  0.0083  0.0056  111 THR   B CB  
1062 O OG1 . THR   B 102 ? 1.1491 1.1015 0.6310 0.5430  0.0244  0.0114  111 THR   B OG1 
1063 C CG2 . THR   B 102 ? 1.1459 1.0441 0.6529 0.4919  -0.0068 0.0025  111 THR   B CG2 
1064 N N   . LEU   B 103 ? 1.1525 1.0258 0.5763 0.5873  -0.0439 -0.0415 112 LEU   B N   
1065 C CA  . LEU   B 103 ? 1.1574 1.0053 0.5883 0.5861  -0.0716 -0.0581 112 LEU   B CA  
1066 C C   . LEU   B 103 ? 1.1366 1.0127 0.6139 0.5574  -0.0581 -0.0440 112 LEU   B C   
1067 O O   . LEU   B 103 ? 1.1196 1.0401 0.6111 0.5645  -0.0324 -0.0313 112 LEU   B O   
1068 C CB  . LEU   B 103 ? 1.1683 1.0072 0.5636 0.6310  -0.0853 -0.0770 112 LEU   B CB  
1069 C CG  . LEU   B 103 ? 1.1896 0.9920 0.5920 0.6262  -0.1183 -0.0932 112 LEU   B CG  
1070 C CD1 . LEU   B 103 ? 1.2202 0.9667 0.6026 0.6231  -0.1540 -0.1108 112 LEU   B CD1 
1071 C CD2 . LEU   B 103 ? 1.1997 1.0111 0.5862 0.6639  -0.1220 -0.1047 112 LEU   B CD2 
1072 N N   . PRO   B 104 ? 1.1322 0.9844 0.6337 0.5250  -0.0755 -0.0458 113 PRO   B N   
1073 C CA  . PRO   B 104 ? 1.1099 0.9862 0.6515 0.4977  -0.0647 -0.0332 113 PRO   B CA  
1074 C C   . PRO   B 104 ? 1.1093 0.9943 0.6554 0.5144  -0.0724 -0.0393 113 PRO   B C   
1075 O O   . PRO   B 104 ? 1.1290 0.9834 0.6510 0.5374  -0.0971 -0.0566 113 PRO   B O   
1076 C CB  . PRO   B 104 ? 1.1224 0.9685 0.6811 0.4605  -0.0804 -0.0333 113 PRO   B CB  
1077 C CG  . PRO   B 104 ? 1.1483 0.9617 0.6827 0.4662  -0.0959 -0.0436 113 PRO   B CG  
1078 C CD  . PRO   B 104 ? 1.1436 0.9497 0.6393 0.5094  -0.1037 -0.0572 113 PRO   B CD  
1079 N N   . GLY   B 105 ? 1.0791 1.0049 0.6583 0.5018  -0.0529 -0.0253 114 GLY   B N   
1080 C CA  . GLY   B 105 ? 1.0651 1.0064 0.6585 0.5121  -0.0588 -0.0282 114 GLY   B CA  
1081 C C   . GLY   B 105 ? 1.0610 0.9724 0.6695 0.4833  -0.0806 -0.0299 114 GLY   B C   
1082 O O   . GLY   B 105 ? 1.0802 0.9527 0.6806 0.4632  -0.0955 -0.0332 114 GLY   B O   
1083 N N   . ILE   B 106 ? 1.0354 0.9662 0.6662 0.4814  -0.0825 -0.0270 115 ILE   B N   
1084 C CA  . ILE   B 106 ? 1.0426 0.9446 0.6823 0.4581  -0.1037 -0.0276 115 ILE   B CA  
1085 C C   . ILE   B 106 ? 1.0179 0.9582 0.6948 0.4380  -0.0915 -0.0149 115 ILE   B C   
1086 O O   . ILE   B 106 ? 1.0021 0.9854 0.6965 0.4557  -0.0797 -0.0122 115 ILE   B O   
1087 C CB  . ILE   B 106 ? 1.0689 0.9394 0.6859 0.4872  -0.1318 -0.0432 115 ILE   B CB  
1088 C CG1 . ILE   B 106 ? 1.1159 0.9386 0.6955 0.5043  -0.1514 -0.0583 115 ILE   B CG1 
1089 C CG2 . ILE   B 106 ? 1.0778 0.9254 0.7040 0.4691  -0.1523 -0.0412 115 ILE   B CG2 
1090 C CD1 . ILE   B 106 ? 1.1534 0.9336 0.7290 0.4734  -0.1662 -0.0571 115 ILE   B CD1 
1091 N N   . PHE   B 107 ? 1.0117 0.9366 0.7006 0.4026  -0.0962 -0.0082 116 PHE   B N   
1092 C CA  . PHE   B 107 ? 0.9925 0.9425 0.7111 0.3821  -0.0922 0.0010  116 PHE   B CA  
1093 C C   . PHE   B 107 ? 1.0156 0.9325 0.7222 0.3846  -0.1201 -0.0051 116 PHE   B C   
1094 O O   . PHE   B 107 ? 1.0388 0.9121 0.7273 0.3685  -0.1347 -0.0065 116 PHE   B O   
1095 C CB  . PHE   B 107 ? 0.9864 0.9299 0.7153 0.3444  -0.0837 0.0098  116 PHE   B CB  
1096 C CG  . PHE   B 107 ? 0.9680 0.9479 0.7197 0.3328  -0.0574 0.0199  116 PHE   B CG  
1097 C CD1 . PHE   B 107 ? 0.9621 0.9777 0.7216 0.3541  -0.0394 0.0234  116 PHE   B CD1 
1098 C CD2 . PHE   B 107 ? 0.9682 0.9452 0.7320 0.3012  -0.0506 0.0266  116 PHE   B CD2 
1099 C CE1 . PHE   B 107 ? 0.9517 0.9969 0.7320 0.3412  -0.0157 0.0356  116 PHE   B CE1 
1100 C CE2 . PHE   B 107 ? 0.9588 0.9633 0.7431 0.2903  -0.0290 0.0362  116 PHE   B CE2 
1101 C CZ  . PHE   B 107 ? 0.9444 0.9814 0.7373 0.3090  -0.0119 0.0416  116 PHE   B CZ  
1102 N N   . LYS   B 108 ? 1.0096 0.9458 0.7257 0.4053  -0.1280 -0.0082 117 LYS   B N   
1103 C CA  . LYS   B 108 ? 1.0351 0.9364 0.7375 0.4091  -0.1563 -0.0128 117 LYS   B CA  
1104 C C   . LYS   B 108 ? 1.0235 0.9381 0.7470 0.3818  -0.1572 -0.0031 117 LYS   B C   
1105 O O   . LYS   B 108 ? 0.9967 0.9601 0.7517 0.3818  -0.1442 0.0014  117 LYS   B O   
1106 C CB  . LYS   B 108 ? 1.0681 0.9808 0.7673 0.4503  -0.1674 -0.0231 117 LYS   B CB  
1107 C CG  . LYS   B 108 ? 1.1588 1.0500 0.8286 0.4819  -0.1716 -0.0361 117 LYS   B CG  
1108 C CD  . LYS   B 108 ? 1.2350 1.1397 0.8993 0.5277  -0.1812 -0.0485 117 LYS   B CD  
1109 C CE  . LYS   B 108 ? 1.3253 1.1980 0.9527 0.5596  -0.1904 -0.0642 117 LYS   B CE  
1110 N NZ  . LYS   B 108 ? 1.3485 1.2529 0.9726 0.6084  -0.1873 -0.0762 117 LYS   B NZ  
1111 N N   . THR   B 109 ? 1.0427 0.9159 0.7496 0.3570  -0.1712 0.0008  118 THR   B N   
1112 C CA  . THR   B 109 ? 1.0408 0.9202 0.7590 0.3315  -0.1740 0.0091  118 THR   B CA  
1113 C C   . THR   B 109 ? 1.0622 0.9014 0.7580 0.3334  -0.2023 0.0096  118 THR   B C   
1114 O O   . THR   B 109 ? 1.0879 0.8883 0.7597 0.3493  -0.2196 0.0045  118 THR   B O   
1115 C CB  . THR   B 109 ? 1.0595 0.9347 0.7790 0.2970  -0.1585 0.0162  118 THR   B CB  
1116 O OG1 . THR   B 109 ? 1.0971 0.9243 0.7891 0.2818  -0.1699 0.0184  118 THR   B OG1 
1117 C CG2 . THR   B 109 ? 1.0527 0.9526 0.7854 0.2966  -0.1343 0.0160  118 THR   B CG2 
1118 N N   . LYS   B 110 ? 1.0515 0.8967 0.7529 0.3172  -0.2085 0.0158  119 LYS   B N   
1119 C CA  . LYS   B 110 ? 1.0739 0.8795 0.7505 0.3165  -0.2345 0.0193  119 LYS   B CA  
1120 C C   . LYS   B 110 ? 1.1068 0.8583 0.7510 0.2957  -0.2407 0.0261  119 LYS   B C   
1121 O O   . LYS   B 110 ? 1.1311 0.8413 0.7500 0.2955  -0.2624 0.0312  119 LYS   B O   
1122 C CB  . LYS   B 110 ? 1.0757 0.9031 0.7639 0.3045  -0.2394 0.0241  119 LYS   B CB  
1123 C CG  . LYS   B 110 ? 1.1219 0.9438 0.8031 0.2702  -0.2285 0.0318  119 LYS   B CG  
1124 C CD  . LYS   B 110 ? 1.1561 1.0118 0.8572 0.2616  -0.2296 0.0322  119 LYS   B CD  
1125 C CE  . LYS   B 110 ? 1.2155 1.0480 0.8914 0.2360  -0.2333 0.0390  119 LYS   B CE  
1126 N NZ  . LYS   B 110 ? 1.2404 1.0662 0.9102 0.2130  -0.2118 0.0416  119 LYS   B NZ  
1127 N N   . ASP   B 111 ? 1.1022 0.8552 0.7490 0.2778  -0.2217 0.0275  120 ASP   B N   
1128 C CA  . ASP   B 111 ? 1.1286 0.8402 0.7533 0.2570  -0.2244 0.0342  120 ASP   B CA  
1129 C C   . ASP   B 111 ? 1.1448 0.8377 0.7653 0.2666  -0.2247 0.0274  120 ASP   B C   
1130 O O   . ASP   B 111 ? 1.1669 0.8347 0.7783 0.2474  -0.2236 0.0322  120 ASP   B O   
1131 C CB  . ASP   B 111 ? 1.1395 0.8668 0.7697 0.2269  -0.2047 0.0410  120 ASP   B CB  
1132 C CG  . ASP   B 111 ? 1.1825 0.9147 0.8061 0.2146  -0.2091 0.0478  120 ASP   B CG  
1133 O OD1 . ASP   B 111 ? 1.2037 0.9070 0.8060 0.2184  -0.2296 0.0534  120 ASP   B OD1 
1134 O OD2 . ASP   B 111 ? 1.1882 0.9503 0.8258 0.2017  -0.1935 0.0473  120 ASP   B OD2 
1135 N N   . GLY   B 112 ? 1.1314 0.8380 0.7587 0.2965  -0.2264 0.0161  121 GLY   B N   
1136 C CA  . GLY   B 112 ? 1.1392 0.8269 0.7581 0.3099  -0.2295 0.0072  121 GLY   B CA  
1137 C C   . GLY   B 112 ? 1.1160 0.8448 0.7517 0.3223  -0.2070 0.0003  121 GLY   B C   
1138 O O   . GLY   B 112 ? 1.0960 0.8669 0.7530 0.3136  -0.1865 0.0047  121 GLY   B O   
1139 N N   . ASP   B 113 ? 1.1175 0.8312 0.7415 0.3425  -0.2122 -0.0102 122 ASP   B N   
1140 C CA  . ASP   B 113 ? 1.1064 0.8537 0.7386 0.3584  -0.1924 -0.0163 122 ASP   B CA  
1141 C C   . ASP   B 113 ? 1.1015 0.8511 0.7381 0.3365  -0.1768 -0.0128 122 ASP   B C   
1142 O O   . ASP   B 113 ? 1.1163 0.8321 0.7441 0.3188  -0.1874 -0.0117 122 ASP   B O   
1143 C CB  . ASP   B 113 ? 1.1407 0.8721 0.7531 0.3968  -0.2062 -0.0311 122 ASP   B CB  
1144 C CG  . ASP   B 113 ? 1.2075 0.9457 0.8180 0.4258  -0.2183 -0.0368 122 ASP   B CG  
1145 O OD1 . ASP   B 113 ? 1.2174 0.9699 0.8425 0.4150  -0.2191 -0.0286 122 ASP   B OD1 
1146 O OD2 . ASP   B 113 ? 1.2438 0.9730 0.8373 0.4613  -0.2282 -0.0505 122 ASP   B OD2 
1147 N N   . ILE   B 114 ? 1.0764 0.8675 0.7288 0.3379  -0.1519 -0.0102 123 ILE   B N   
1148 C CA  . ILE   B 114 ? 1.0718 0.8699 0.7298 0.3209  -0.1356 -0.0068 123 ILE   B CA  
1149 C C   . ILE   B 114 ? 1.0640 0.8811 0.7163 0.3467  -0.1234 -0.0124 123 ILE   B C   
1150 O O   . ILE   B 114 ? 1.0546 0.8993 0.7105 0.3697  -0.1160 -0.0135 123 ILE   B O   
1151 C CB  . ILE   B 114 ? 1.0577 0.8852 0.7389 0.2945  -0.1161 0.0043  123 ILE   B CB  
1152 C CG1 . ILE   B 114 ? 1.0764 0.8914 0.7595 0.2746  -0.1270 0.0099  123 ILE   B CG1 
1153 C CG2 . ILE   B 114 ? 1.0576 0.8872 0.7435 0.2770  -0.1019 0.0072  123 ILE   B CG2 
1154 C CD1 . ILE   B 114 ? 1.0792 0.9238 0.7824 0.2562  -0.1123 0.0173  123 ILE   B CD1 
1155 N N   . GLY   B 115 ? 1.0610 0.8659 0.7047 0.3437  -0.1210 -0.0152 124 GLY   B N   
1156 C CA  . GLY   B 115 ? 1.0543 0.8752 0.6877 0.3676  -0.1088 -0.0189 124 GLY   B CA  
1157 C C   . GLY   B 115 ? 1.0285 0.8935 0.6826 0.3612  -0.0800 -0.0067 124 GLY   B C   
1158 O O   . GLY   B 115 ? 1.0176 0.8942 0.6935 0.3341  -0.0715 0.0024  124 GLY   B O   
1159 N N   . ALA   B 116 ? 1.0190 0.9082 0.6658 0.3861  -0.0653 -0.0060 125 ALA   B N   
1160 C CA  . ALA   B 116 ? 1.0039 0.9340 0.6721 0.3787  -0.0377 0.0082  125 ALA   B CA  
1161 C C   . ALA   B 116 ? 1.0159 0.9586 0.6669 0.4000  -0.0217 0.0110  125 ALA   B C   
1162 O O   . ALA   B 116 ? 1.0270 0.9750 0.6571 0.4326  -0.0229 0.0043  125 ALA   B O   
1163 C CB  . ALA   B 116 ? 0.9823 0.9476 0.6738 0.3827  -0.0308 0.0137  125 ALA   B CB  
1164 N N   . VAL   B 117 ? 1.0139 0.9603 0.6708 0.3837  -0.0070 0.0208  126 VAL   B N   
1165 C CA  A VAL   B 117 ? 1.0254 0.9820 0.6633 0.4027  0.0091  0.0265  126 VAL   B CA  
1166 C CA  B VAL   B 117 ? 1.0251 0.9811 0.6631 0.4023  0.0088  0.0264  126 VAL   B CA  
1167 C C   . VAL   B 117 ? 1.0124 1.0143 0.6717 0.4028  0.0369  0.0444  126 VAL   B C   
1168 O O   . VAL   B 117 ? 1.0039 1.0201 0.6946 0.3747  0.0473  0.0564  126 VAL   B O   
1169 C CB  A VAL   B 117 ? 1.0442 0.9763 0.6715 0.3910  0.0075  0.0269  126 VAL   B CB  
1170 C CB  B VAL   B 117 ? 1.0422 0.9733 0.6728 0.3871  0.0065  0.0268  126 VAL   B CB  
1171 C CG1 A VAL   B 117 ? 1.0730 0.9671 0.6730 0.4036  -0.0185 0.0089  126 VAL   B CG1 
1172 C CG1 B VAL   B 117 ? 1.0480 0.9923 0.6659 0.3982  0.0271  0.0390  126 VAL   B CG1 
1173 C CG2 A VAL   B 117 ? 1.0420 0.9717 0.6986 0.3542  0.0105  0.0337  126 VAL   B CG2 
1174 C CG2 B VAL   B 117 ? 1.0694 0.9617 0.6761 0.3958  -0.0202 0.0091  126 VAL   B CG2 
1175 N N   . ALA   B 118 ? 1.0094 1.0352 0.6527 0.4347  0.0484  0.0462  127 ALA   B N   
1176 C CA  . ALA   B 118 ? 0.9927 1.0675 0.6596 0.4354  0.0766  0.0654  127 ALA   B CA  
1177 C C   . ALA   B 118 ? 1.0059 1.0860 0.6590 0.4370  0.0981  0.0814  127 ALA   B C   
1178 O O   . ALA   B 118 ? 1.0142 1.1110 0.6416 0.4667  0.1122  0.0859  127 ALA   B O   
1179 C CB  . ALA   B 118 ? 0.9838 1.0895 0.6456 0.4688  0.0808  0.0608  127 ALA   B CB  
1180 N N   . LEU   B 119 ? 1.0055 1.0686 0.6721 0.4067  0.0998  0.0897  128 LEU   B N   
1181 C CA  . LEU   B 119 ? 1.0109 1.0720 0.6663 0.4039  0.1175  0.1063  128 LEU   B CA  
1182 C C   . LEU   B 119 ? 1.0006 1.0752 0.6988 0.3676  0.1300  0.1237  128 LEU   B C   
1183 O O   . LEU   B 119 ? 1.0005 1.0593 0.7202 0.3425  0.1156  0.1157  128 LEU   B O   
1184 C CB  . LEU   B 119 ? 1.0340 1.0493 0.6576 0.4065  0.1001  0.0942  128 LEU   B CB  
1185 C CG  . LEU   B 119 ? 1.0703 1.0659 0.6494 0.4415  0.0842  0.0761  128 LEU   B CG  
1186 C CD1 . LEU   B 119 ? 1.0954 1.0490 0.6542 0.4383  0.0640  0.0640  128 LEU   B CD1 
1187 C CD2 . LEU   B 119 ? 1.0803 1.0978 0.6286 0.4746  0.1037  0.0860  128 LEU   B CD2 
1188 N N   . ASP   B 120 ? 0.9908 1.0941 0.7015 0.3645  0.1560  0.1477  129 ASP   B N   
1189 C CA  . ASP   B 120 ? 0.9849 1.0975 0.7378 0.3291  0.1652  0.1641  129 ASP   B CA  
1190 C C   . ASP   B 120 ? 0.9964 1.0751 0.7371 0.3152  0.1671  0.1727  129 ASP   B C   
1191 O O   . ASP   B 120 ? 1.0122 1.0852 0.7232 0.3315  0.1793  0.1843  129 ASP   B O   
1192 C CB  . ASP   B 120 ? 0.9971 1.1620 0.7837 0.3257  0.1900  0.1866  129 ASP   B CB  
1193 C CG  . ASP   B 120 ? 1.0799 1.2576 0.9201 0.2878  0.1904  0.1964  129 ASP   B CG  
1194 O OD1 . ASP   B 120 ? 1.1124 1.2541 0.9574 0.2643  0.1755  0.1890  129 ASP   B OD1 
1195 O OD2 . ASP   B 120 ? 1.0934 1.3183 0.9716 0.2824  0.2046  0.2102  129 ASP   B OD2 
1196 N N   . TYR   B 121 ? 0.9909 1.0465 0.7527 0.2867  0.1544  0.1667  130 TYR   B N   
1197 C CA  . TYR   B 121 ? 1.0020 1.0226 0.7563 0.2726  0.1525  0.1713  130 TYR   B CA  
1198 C C   . TYR   B 121 ? 0.9804 0.9982 0.7752 0.2376  0.1504  0.1763  130 TYR   B C   
1199 O O   . TYR   B 121 ? 0.9649 1.0002 0.7883 0.2247  0.1434  0.1691  130 TYR   B O   
1200 C CB  . TYR   B 121 ? 1.0264 1.0105 0.7520 0.2818  0.1312  0.1488  130 TYR   B CB  
1201 C CG  . TYR   B 121 ? 1.0561 1.0296 0.7378 0.3129  0.1320  0.1474  130 TYR   B CG  
1202 C CD1 . TYR   B 121 ? 1.0833 1.0380 0.7438 0.3182  0.1397  0.1602  130 TYR   B CD1 
1203 C CD2 . TYR   B 121 ? 1.0738 1.0539 0.7330 0.3387  0.1236  0.1334  130 TYR   B CD2 
1204 C CE1 . TYR   B 121 ? 1.1139 1.0582 0.7306 0.3485  0.1388  0.1586  130 TYR   B CE1 
1205 C CE2 . TYR   B 121 ? 1.1064 1.0754 0.7226 0.3691  0.1222  0.1305  130 TYR   B CE2 
1206 C CZ  . TYR   B 121 ? 1.1329 1.0852 0.7273 0.3741  0.1300  0.1432  130 TYR   B CZ  
1207 O OH  . TYR   B 121 ? 1.1777 1.1177 0.7261 0.4056  0.1266  0.1397  130 TYR   B OH  
1208 N N   . PRO   B 122 ? 0.9753 0.9685 0.7713 0.2233  0.1546  0.1878  131 PRO   B N   
1209 C CA  . PRO   B 122 ? 0.9540 0.9388 0.7856 0.1914  0.1495  0.1900  131 PRO   B CA  
1210 C C   . PRO   B 122 ? 0.9431 0.9096 0.7776 0.1821  0.1279  0.1645  131 PRO   B C   
1211 O O   . PRO   B 122 ? 0.9612 0.9126 0.7692 0.1972  0.1172  0.1478  131 PRO   B O   
1212 C CB  . PRO   B 122 ? 0.9783 0.9304 0.7993 0.1848  0.1548  0.2040  131 PRO   B CB  
1213 C CG  . PRO   B 122 ? 0.9990 0.9512 0.7833 0.2116  0.1672  0.2152  131 PRO   B CG  
1214 C CD  . PRO   B 122 ? 0.9862 0.9543 0.7488 0.2368  0.1612  0.1980  131 PRO   B CD  
1215 N N   . ALA   B 123 ? 0.9132 0.8805 0.7795 0.1569  0.1210  0.1621  132 ALA   B N   
1216 C CA  . ALA   B 123 ? 0.9064 0.8572 0.7728 0.1478  0.1021  0.1395  132 ALA   B CA  
1217 C C   . ALA   B 123 ? 0.9115 0.8243 0.7520 0.1522  0.0941  0.1274  132 ALA   B C   
1218 O O   . ALA   B 123 ? 0.9231 0.8274 0.7529 0.1546  0.0819  0.1090  132 ALA   B O   
1219 C CB  . ALA   B 123 ? 0.8943 0.8487 0.7950 0.1214  0.0954  0.1396  132 ALA   B CB  
1220 N N   . GLY   B 124 ? 0.8994 0.7920 0.7298 0.1549  0.1015  0.1388  133 GLY   B N   
1221 C CA  . GLY   B 124 ? 0.9031 0.7629 0.7112 0.1622  0.0943  0.1283  133 GLY   B CA  
1222 C C   . GLY   B 124 ? 0.8964 0.7563 0.6764 0.1858  0.0902  0.1179  133 GLY   B C   
1223 O O   . GLY   B 124 ? 0.9052 0.7445 0.6718 0.1917  0.0818  0.1058  133 GLY   B O   
1224 N N   . THR   B 125 ? 0.8800 0.7636 0.6522 0.2002  0.0948  0.1215  134 THR   B N   
1225 C CA  . THR   B 125 ? 0.8826 0.7645 0.6286 0.2225  0.0874  0.1100  134 THR   B CA  
1226 C C   . THR   B 125 ? 0.8753 0.7585 0.6261 0.2172  0.0723  0.0900  134 THR   B C   
1227 O O   . THR   B 125 ? 0.8879 0.7630 0.6219 0.2299  0.0623  0.0784  134 THR   B O   
1228 C CB  . THR   B 125 ? 0.8950 0.7973 0.6258 0.2433  0.0974  0.1206  134 THR   B CB  
1229 O OG1 . THR   B 125 ? 0.9089 0.8129 0.6378 0.2442  0.1142  0.1429  134 THR   B OG1 
1230 C CG2 . THR   B 125 ? 0.9080 0.8011 0.6066 0.2690  0.0876  0.1090  134 THR   B CG2 
1231 N N   . SER   B 126 ? 0.8552 0.7471 0.6285 0.1979  0.0698  0.0869  135 SER   B N   
1232 C CA  . SER   B 126 ? 0.8500 0.7429 0.6266 0.1906  0.0571  0.0716  135 SER   B CA  
1233 C C   . SER   B 126 ? 0.8494 0.7245 0.6144 0.1923  0.0474  0.0577  135 SER   B C   
1234 O O   . SER   B 126 ? 0.8598 0.7210 0.6271 0.1858  0.0482  0.0549  135 SER   B O   
1235 C CB  . SER   B 126 ? 0.8561 0.7537 0.6546 0.1689  0.0556  0.0710  135 SER   B CB  
1236 O OG  . SER   B 126 ? 0.8660 0.7861 0.6824 0.1655  0.0624  0.0829  135 SER   B OG  
1237 N N   . GLY   B 127 ? 0.8347 0.7113 0.5904 0.1998  0.0376  0.0489  136 GLY   B N   
1238 C CA  . GLY   B 127 ? 0.8353 0.7007 0.5851 0.2002  0.0282  0.0373  136 GLY   B CA  
1239 C C   . GLY   B 127 ? 0.8411 0.6998 0.5752 0.2198  0.0231  0.0350  136 GLY   B C   
1240 O O   . GLY   B 127 ? 0.8447 0.6967 0.5783 0.2207  0.0146  0.0260  136 GLY   B O   
1241 N N   . SER   B 128 ? 0.8394 0.7017 0.5608 0.2364  0.0281  0.0432  137 SER   B N   
1242 C CA  . SER   B 128 ? 0.8507 0.7053 0.5511 0.2585  0.0220  0.0407  137 SER   B CA  
1243 C C   . SER   B 128 ? 0.8572 0.7094 0.5502 0.2657  0.0058  0.0294  137 SER   B C   
1244 O O   . SER   B 128 ? 0.8520 0.7118 0.5460 0.2656  0.0044  0.0297  137 SER   B O   
1245 C CB  . SER   B 128 ? 0.8661 0.7268 0.5516 0.2746  0.0346  0.0542  137 SER   B CB  
1246 O OG  . SER   B 128 ? 0.8875 0.7409 0.5736 0.2718  0.0453  0.0648  137 SER   B OG  
1247 N N   . PRO   B 129 ? 0.8666 0.7071 0.5545 0.2715  -0.0084 0.0191  138 PRO   B N   
1248 C CA  . PRO   B 129 ? 0.8735 0.7069 0.5568 0.2756  -0.0269 0.0084  138 PRO   B CA  
1249 C C   . PRO   B 129 ? 0.8859 0.7153 0.5445 0.3000  -0.0331 0.0065  138 PRO   B C   
1250 O O   . PRO   B 129 ? 0.8931 0.7231 0.5317 0.3199  -0.0266 0.0109  138 PRO   B O   
1251 C CB  . PRO   B 129 ? 0.8865 0.7112 0.5746 0.2759  -0.0402 -0.0008 138 PRO   B CB  
1252 C CG  . PRO   B 129 ? 0.8931 0.7173 0.5737 0.2863  -0.0305 0.0045  138 PRO   B CG  
1253 C CD  . PRO   B 129 ? 0.8651 0.6983 0.5541 0.2741  -0.0102 0.0165  138 PRO   B CD  
1254 N N   . ILE   B 130 ? 0.8846 0.7081 0.5420 0.2999  -0.0464 -0.0003 139 ILE   B N   
1255 C CA  . ILE   B 130 ? 0.8961 0.7123 0.5291 0.3248  -0.0565 -0.0062 139 ILE   B CA  
1256 C C   . ILE   B 130 ? 0.9235 0.7165 0.5513 0.3281  -0.0831 -0.0205 139 ILE   B C   
1257 O O   . ILE   B 130 ? 0.9194 0.7061 0.5673 0.3064  -0.0930 -0.0233 139 ILE   B O   
1258 C CB  . ILE   B 130 ? 0.8849 0.7102 0.5228 0.3224  -0.0531 -0.0031 139 ILE   B CB  
1259 C CG1 . ILE   B 130 ? 0.8815 0.7328 0.5296 0.3182  -0.0280 0.0114  139 ILE   B CG1 
1260 C CG2 . ILE   B 130 ? 0.8956 0.7097 0.5088 0.3493  -0.0677 -0.0127 139 ILE   B CG2 
1261 C CD1 . ILE   B 130 ? 0.8903 0.7543 0.5536 0.3081  -0.0252 0.0149  139 ILE   B CD1 
1262 N N   . LEU   B 131 ? 0.9448 0.7255 0.5462 0.3542  -0.0948 -0.0289 140 LEU   B N   
1263 C CA  . LEU   B 131 ? 0.9677 0.7258 0.5663 0.3574  -0.1226 -0.0434 140 LEU   B CA  
1264 C C   . LEU   B 131 ? 1.0027 0.7378 0.5764 0.3792  -0.1460 -0.0570 140 LEU   B C   
1265 O O   . LEU   B 131 ? 1.0140 0.7513 0.5601 0.4049  -0.1400 -0.0577 140 LEU   B O   
1266 C CB  . LEU   B 131 ? 0.9750 0.7319 0.5635 0.3699  -0.1247 -0.0458 140 LEU   B CB  
1267 C CG  . LEU   B 131 ? 0.9844 0.7594 0.5868 0.3588  -0.1020 -0.0332 140 LEU   B CG  
1268 C CD1 . LEU   B 131 ? 0.9974 0.7658 0.5839 0.3765  -0.1090 -0.0369 140 LEU   B CD1 
1269 C CD2 . LEU   B 131 ? 0.9783 0.7631 0.6193 0.3259  -0.0975 -0.0299 140 LEU   B CD2 
1270 N N   . ASP   B 132 ? 1.0229 0.7356 0.6061 0.3705  -0.1736 -0.0685 141 ASP   B N   
1271 C CA  . ASP   B 132 ? 1.0679 0.7504 0.6266 0.3917  -0.2024 -0.0847 141 ASP   B CA  
1272 C C   . ASP   B 132 ? 1.1110 0.7797 0.6489 0.4134  -0.2214 -0.0979 141 ASP   B C   
1273 O O   . ASP   B 132 ? 1.1024 0.7854 0.6506 0.4079  -0.2129 -0.0932 141 ASP   B O   
1274 C CB  . ASP   B 132 ? 1.0865 0.7472 0.6672 0.3685  -0.2249 -0.0886 141 ASP   B CB  
1275 C CG  . ASP   B 132 ? 1.1227 0.7846 0.7405 0.3374  -0.2342 -0.0867 141 ASP   B CG  
1276 O OD1 . ASP   B 132 ? 1.1260 0.7972 0.7497 0.3397  -0.2351 -0.0896 141 ASP   B OD1 
1277 O OD2 . ASP   B 132 ? 1.1552 0.8095 0.7958 0.3118  -0.2409 -0.0819 141 ASP   B OD2 
1278 N N   . LYS   B 133 ? 1.1543 0.7931 0.6618 0.4393  -0.2492 -0.1155 142 LYS   B N   
1279 C CA  . LYS   B 133 ? 1.1929 0.8147 0.6755 0.4630  -0.2719 -0.1307 142 LYS   B CA  
1280 C C   . LYS   B 133 ? 1.1902 0.8110 0.7087 0.4387  -0.2895 -0.1338 142 LYS   B C   
1281 O O   . LYS   B 133 ? 1.1996 0.8179 0.7049 0.4544  -0.3007 -0.1415 142 LYS   B O   
1282 C CB  . LYS   B 133 ? 1.2664 0.8518 0.7109 0.4935  -0.3028 -0.1517 142 LYS   B CB  
1283 C CG  . LYS   B 133 ? 1.3612 0.9535 0.7666 0.5255  -0.2841 -0.1503 142 LYS   B CG  
1284 C CD  . LYS   B 133 ? 1.4493 1.0135 0.8446 0.5345  -0.3046 -0.1625 142 LYS   B CD  
1285 C CE  . LYS   B 133 ? 1.5223 1.0930 0.8728 0.5763  -0.2917 -0.1669 142 LYS   B CE  
1286 N NZ  . LYS   B 133 ? 1.5714 1.1136 0.9112 0.5886  -0.3130 -0.1802 142 LYS   B NZ  
1287 N N   . CYS   B 134 ? 1.1752 0.8016 0.7393 0.4011  -0.2899 -0.1264 143 CYS   B N   
1288 C CA  . CYS   B 134 ? 1.1642 0.7991 0.7711 0.3745  -0.3013 -0.1263 143 CYS   B CA  
1289 C C   . CYS   B 134 ? 1.1302 0.8013 0.7589 0.3621  -0.2717 -0.1124 143 CYS   B C   
1290 O O   . CYS   B 134 ? 1.1202 0.8036 0.7823 0.3461  -0.2793 -0.1134 143 CYS   B O   
1291 C CB  . CYS   B 134 ? 1.1834 0.8093 0.8271 0.3408  -0.3134 -0.1229 143 CYS   B CB  
1292 S SG  . CYS   B 134 ? 1.2873 0.8683 0.9314 0.3430  -0.3651 -0.1431 143 CYS   B SG  
1293 N N   . GLY   B 135 ? 1.1100 0.7982 0.7235 0.3681  -0.2394 -0.0994 144 GLY   B N   
1294 C CA  . GLY   B 135 ? 1.0823 0.7992 0.7139 0.3566  -0.2119 -0.0862 144 GLY   B CA  
1295 C C   . GLY   B 135 ? 1.0481 0.7835 0.7151 0.3232  -0.1927 -0.0737 144 GLY   B C   
1296 O O   . GLY   B 135 ? 1.0372 0.7944 0.7195 0.3128  -0.1703 -0.0639 144 GLY   B O   
1297 N N   . ARG   B 136 ? 1.0298 0.7537 0.7073 0.3074  -0.2026 -0.0741 145 ARG   B N   
1298 C CA  . ARG   B 136 ? 1.0050 0.7431 0.7105 0.2770  -0.1869 -0.0622 145 ARG   B CA  
1299 C C   . ARG   B 136 ? 0.9846 0.7350 0.6773 0.2786  -0.1594 -0.0509 145 ARG   B C   
1300 O O   . ARG   B 136 ? 0.9999 0.7439 0.6632 0.3014  -0.1560 -0.0520 145 ARG   B O   
1301 C CB  . ARG   B 136 ? 1.0259 0.7439 0.7432 0.2604  -0.2079 -0.0643 145 ARG   B CB  
1302 C CG  . ARG   B 136 ? 1.0639 0.7792 0.8115 0.2455  -0.2308 -0.0706 145 ARG   B CG  
1303 C CD  . ARG   B 136 ? 1.1175 0.8050 0.8726 0.2314  -0.2557 -0.0725 145 ARG   B CD  
1304 N NE  . ARG   B 136 ? 1.1844 0.8363 0.9057 0.2586  -0.2824 -0.0874 145 ARG   B NE  
1305 C CZ  . ARG   B 136 ? 1.2290 0.8498 0.9339 0.2610  -0.2973 -0.0894 145 ARG   B CZ  
1306 N NH1 . ARG   B 136 ? 1.2127 0.8333 0.9309 0.2369  -0.2880 -0.0757 145 ARG   B NH1 
1307 N NH2 . ARG   B 136 ? 1.2523 0.8408 0.9242 0.2897  -0.3222 -0.1056 145 ARG   B NH2 
1308 N N   . VAL   B 137 ? 0.9461 0.7161 0.6616 0.2552  -0.1397 -0.0405 146 VAL   B N   
1309 C CA  . VAL   B 137 ? 0.9255 0.7075 0.6337 0.2536  -0.1161 -0.0304 146 VAL   B CA  
1310 C C   . VAL   B 137 ? 0.9122 0.6849 0.6186 0.2437  -0.1204 -0.0270 146 VAL   B C   
1311 O O   . VAL   B 137 ? 0.9046 0.6771 0.6291 0.2205  -0.1231 -0.0232 146 VAL   B O   
1312 C CB  . VAL   B 137 ? 0.9163 0.7203 0.6442 0.2376  -0.0948 -0.0231 146 VAL   B CB  
1313 C CG1 . VAL   B 137 ? 0.9251 0.7387 0.6458 0.2363  -0.0739 -0.0138 146 VAL   B CG1 
1314 C CG2 . VAL   B 137 ? 0.9149 0.7244 0.6444 0.2492  -0.0941 -0.0270 146 VAL   B CG2 
1315 N N   . ILE   B 138 ? 0.9057 0.6705 0.5889 0.2631  -0.1219 -0.0283 147 ILE   B N   
1316 C CA  . ILE   B 138 ? 0.8965 0.6509 0.5747 0.2595  -0.1280 -0.0262 147 ILE   B CA  
1317 C C   . ILE   B 138 ? 0.8811 0.6554 0.5648 0.2503  -0.1066 -0.0154 147 ILE   B C   
1318 O O   . ILE   B 138 ? 0.8860 0.6540 0.5664 0.2478  -0.1115 -0.0131 147 ILE   B O   
1319 C CB  . ILE   B 138 ? 0.9088 0.6432 0.5597 0.2886  -0.1452 -0.0362 147 ILE   B CB  
1320 C CG1 . ILE   B 138 ? 0.9103 0.6618 0.5423 0.3144  -0.1284 -0.0350 147 ILE   B CG1 
1321 C CG2 . ILE   B 138 ? 0.9223 0.6308 0.5674 0.2960  -0.1725 -0.0490 147 ILE   B CG2 
1322 C CD1 . ILE   B 138 ? 0.9302 0.6703 0.5366 0.3426  -0.1387 -0.0428 147 ILE   B CD1 
1323 N N   . GLY   B 139 ? 0.8646 0.6602 0.5569 0.2456  -0.0858 -0.0095 148 GLY   B N   
1324 C CA  . GLY   B 139 ? 0.8592 0.6724 0.5589 0.2357  -0.0681 -0.0005 148 GLY   B CA  
1325 C C   . GLY   B 139 ? 0.8538 0.6847 0.5572 0.2389  -0.0483 0.0049  148 GLY   B C   
1326 O O   . GLY   B 139 ? 0.8585 0.6875 0.5553 0.2510  -0.0474 0.0025  148 GLY   B O   
1327 N N   . LEU   B 140 ? 0.8439 0.6897 0.5575 0.2278  -0.0342 0.0124  149 LEU   B N   
1328 C CA  . LEU   B 140 ? 0.8412 0.7001 0.5604 0.2280  -0.0166 0.0191  149 LEU   B CA  
1329 C C   . LEU   B 140 ? 0.8450 0.7202 0.5654 0.2358  -0.0067 0.0269  149 LEU   B C   
1330 O O   . LEU   B 140 ? 0.8398 0.7206 0.5639 0.2336  -0.0113 0.0272  149 LEU   B O   
1331 C CB  . LEU   B 140 ? 0.8307 0.6927 0.5650 0.2062  -0.0085 0.0206  149 LEU   B CB  
1332 C CG  . LEU   B 140 ? 0.8400 0.6946 0.5790 0.1975  -0.0133 0.0142  149 LEU   B CG  
1333 C CD1 . LEU   B 140 ? 0.8415 0.7014 0.5919 0.1811  -0.0030 0.0147  149 LEU   B CD1 
1334 C CD2 . LEU   B 140 ? 0.8443 0.6934 0.5774 0.2126  -0.0165 0.0107  149 LEU   B CD2 
1335 N N   . TYR   B 141 ? 0.8498 0.7338 0.5686 0.2446  0.0069  0.0345  150 TYR   B N   
1336 C CA  . TYR   B 141 ? 0.8554 0.7606 0.5801 0.2510  0.0200  0.0451  150 TYR   B CA  
1337 C C   . TYR   B 141 ? 0.8491 0.7637 0.5970 0.2286  0.0304  0.0528  150 TYR   B C   
1338 O O   . TYR   B 141 ? 0.8494 0.7527 0.6002 0.2180  0.0334  0.0527  150 TYR   B O   
1339 C CB  . TYR   B 141 ? 0.8663 0.7742 0.5742 0.2719  0.0301  0.0517  150 TYR   B CB  
1340 C CG  . TYR   B 141 ? 0.8766 0.8104 0.5936 0.2763  0.0486  0.0669  150 TYR   B CG  
1341 C CD1 . TYR   B 141 ? 0.8872 0.8271 0.6213 0.2604  0.0629  0.0800  150 TYR   B CD1 
1342 C CD2 . TYR   B 141 ? 0.8920 0.8443 0.6004 0.2977  0.0520  0.0686  150 TYR   B CD2 
1343 C CE1 . TYR   B 141 ? 0.8910 0.8570 0.6391 0.2606  0.0801  0.0963  150 TYR   B CE1 
1344 C CE2 . TYR   B 141 ? 0.8945 0.8771 0.6154 0.3013  0.0713  0.0843  150 TYR   B CE2 
1345 C CZ  . TYR   B 141 ? 0.9014 0.8919 0.6444 0.2809  0.0856  0.0992  150 TYR   B CZ  
1346 O OH  . TYR   B 141 ? 0.9129 0.9352 0.6728 0.2815  0.1052  0.1173  150 TYR   B OH  
1347 N N   . GLY   B 142 ? 0.8401 0.7751 0.6049 0.2231  0.0347  0.0587  151 GLY   B N   
1348 C CA  . GLY   B 142 ? 0.8400 0.7827 0.6282 0.2019  0.0416  0.0653  151 GLY   B CA  
1349 C C   . GLY   B 142 ? 0.8374 0.7943 0.6434 0.1905  0.0350  0.0638  151 GLY   B C   
1350 O O   . GLY   B 142 ? 0.8300 0.7959 0.6576 0.1740  0.0388  0.0690  151 GLY   B O   
1351 N N   . ASN   B 143 ? 0.8416 0.7977 0.6385 0.1989  0.0227  0.0563  152 ASN   B N   
1352 C CA  . ASN   B 143 ? 0.8415 0.8096 0.6523 0.1909  0.0139  0.0546  152 ASN   B CA  
1353 C C   . ASN   B 143 ? 0.8429 0.8290 0.6537 0.2112  0.0104  0.0551  152 ASN   B C   
1354 O O   . ASN   B 143 ? 0.8512 0.8222 0.6416 0.2248  -0.0009 0.0476  152 ASN   B O   
1355 C CB  . ASN   B 143 ? 0.8638 0.8097 0.6628 0.1784  -0.0002 0.0453  152 ASN   B CB  
1356 C CG  . ASN   B 143 ? 0.8828 0.8378 0.6942 0.1667  -0.0091 0.0444  152 ASN   B CG  
1357 O OD1 . ASN   B 143 ? 0.8678 0.8456 0.7033 0.1621  -0.0050 0.0499  152 ASN   B OD1 
1358 N ND2 . ASN   B 143 ? 0.9021 0.8397 0.6979 0.1613  -0.0224 0.0383  152 ASN   B ND2 
1359 N N   . GLY   B 144 ? 0.8351 0.8537 0.6703 0.2133  0.0194  0.0637  153 GLY   B N   
1360 C CA  . GLY   B 144 ? 0.8456 0.8881 0.6842 0.2355  0.0184  0.0641  153 GLY   B CA  
1361 C C   . GLY   B 144 ? 0.8431 0.9253 0.7186 0.2301  0.0232  0.0720  153 GLY   B C   
1362 O O   . GLY   B 144 ? 0.8375 0.9215 0.7321 0.2091  0.0155  0.0714  153 GLY   B O   
1363 N N   . VAL   B 145 ? 0.8460 0.9623 0.7323 0.2500  0.0357  0.0790  154 VAL   B N   
1364 C CA  . VAL   B 145 ? 0.8395 1.0019 0.7664 0.2477  0.0408  0.0871  154 VAL   B CA  
1365 C C   . VAL   B 145 ? 0.8491 1.0509 0.7958 0.2549  0.0671  0.1041  154 VAL   B C   
1366 O O   . VAL   B 145 ? 0.8598 1.0520 0.7807 0.2688  0.0802  0.1081  154 VAL   B O   
1367 C CB  . VAL   B 145 ? 0.8422 1.0133 0.7656 0.2687  0.0244  0.0764  154 VAL   B CB  
1368 C CG1 . VAL   B 145 ? 0.8397 1.0323 0.7512 0.3042  0.0344  0.0763  154 VAL   B CG1 
1369 C CG2 . VAL   B 145 ? 0.8275 1.0294 0.7909 0.2562  0.0154  0.0780  154 VAL   B CG2 
1370 N N   . VAL   B 146 ? 0.8412 1.0877 0.8346 0.2439  0.0745  0.1152  155 VAL   B N   
1371 C CA  . VAL   B 146 ? 0.8465 1.1363 0.8649 0.2476  0.1011  0.1349  155 VAL   B CA  
1372 C C   . VAL   B 146 ? 0.8561 1.1962 0.8908 0.2757  0.1068  0.1351  155 VAL   B C   
1373 O O   . VAL   B 146 ? 0.8353 1.2049 0.9058 0.2714  0.0961  0.1322  155 VAL   B O   
1374 C CB  . VAL   B 146 ? 0.8328 1.1389 0.8972 0.2125  0.1073  0.1500  155 VAL   B CB  
1375 C CG1 . VAL   B 146 ? 0.8136 1.1727 0.9120 0.2145  0.1353  0.1736  155 VAL   B CG1 
1376 C CG2 . VAL   B 146 ? 0.8595 1.1148 0.9028 0.1906  0.1041  0.1495  155 VAL   B CG2 
1377 N N   . ILE   B 147 ? 0.8868 1.2349 0.8924 0.3074  0.1216  0.1365  156 ILE   B N   
1378 C CA  . ILE   B 147 ? 0.8962 1.2904 0.9103 0.3406  0.1280  0.1345  156 ILE   B CA  
1379 C C   . ILE   B 147 ? 0.8838 1.3481 0.9504 0.3359  0.1550  0.1572  156 ILE   B C   
1380 O O   . ILE   B 147 ? 0.8804 1.3505 0.9691 0.3080  0.1700  0.1761  156 ILE   B O   
1381 C CB  . ILE   B 147 ? 0.9314 1.3029 0.8887 0.3794  0.1302  0.1238  156 ILE   B CB  
1382 C CG1 . ILE   B 147 ? 0.9544 1.3130 0.8847 0.3793  0.1520  0.1374  156 ILE   B CG1 
1383 C CG2 . ILE   B 147 ? 0.9726 1.2847 0.8910 0.3847  0.0990  0.1004  156 ILE   B CG2 
1384 C CD1 . ILE   B 147 ? 0.9945 1.3328 0.8682 0.4189  0.1532  0.1264  156 ILE   B CD1 
1385 N N   . LYS   B 148 ? 0.8735 1.3915 0.9618 0.3629  0.1606  0.1557  157 LYS   B N   
1386 C CA  . LYS   B 148 ? 0.8489 1.4448 0.9933 0.3622  0.1867  0.1768  157 LYS   B CA  
1387 C C   . LYS   B 148 ? 0.8516 1.4677 0.9983 0.3540  0.2218  0.2041  157 LYS   B C   
1388 O O   . LYS   B 148 ? 0.8177 1.4895 1.0212 0.3351  0.2413  0.2268  157 LYS   B O   
1389 C CB  . LYS   B 148 ? 0.8634 1.5074 1.0116 0.4057  0.1903  0.1677  157 LYS   B CB  
1390 C CG  . LYS   B 148 ? 0.9321 1.5572 1.0790 0.4159  0.1553  0.1430  157 LYS   B CG  
1391 C CD  . LYS   B 148 ? 0.9728 1.6572 1.1395 0.4559  0.1595  0.1367  157 LYS   B CD  
1392 C CE  . LYS   B 148 ? 0.9679 1.7382 1.2141 0.4429  0.1772  0.1557  157 LYS   B CE  
1393 N NZ  . LYS   B 148 ? 0.9795 1.7536 1.2720 0.4160  0.1488  0.1495  157 LYS   B NZ  
1394 N N   . ASN   B 149 ? 0.8869 1.4589 0.9741 0.3675  0.2289  0.2031  158 ASN   B N   
1395 C CA  . ASN   B 149 ? 0.8930 1.4774 0.9743 0.3615  0.2608  0.2298  158 ASN   B CA  
1396 C C   . ASN   B 149 ? 0.8980 1.4346 0.9796 0.3207  0.2564  0.2402  158 ASN   B C   
1397 O O   . ASN   B 149 ? 0.9142 1.4365 0.9705 0.3195  0.2756  0.2573  158 ASN   B O   
1398 C CB  . ASN   B 149 ? 0.9502 1.5235 0.9665 0.4046  0.2751  0.2262  158 ASN   B CB  
1399 C CG  . ASN   B 149 ? 1.0376 1.5739 1.0041 0.4399  0.2496  0.1939  158 ASN   B CG  
1400 O OD1 . ASN   B 149 ? 1.0366 1.6005 1.0166 0.4621  0.2401  0.1797  158 ASN   B OD1 
1401 N ND2 . ASN   B 149 ? 1.0943 1.5665 1.0035 0.4458  0.2369  0.1821  158 ASN   B ND2 
1402 N N   . GLY   B 150 ? 0.8821 1.3934 0.9890 0.2902  0.2305  0.2294  159 GLY   B N   
1403 C CA  . GLY   B 150 ? 0.8856 1.3489 0.9930 0.2535  0.2217  0.2341  159 GLY   B CA  
1404 C C   . GLY   B 150 ? 0.9125 1.3063 0.9569 0.2619  0.2082  0.2182  159 GLY   B C   
1405 O O   . GLY   B 150 ? 0.9291 1.2784 0.9702 0.2357  0.1940  0.2139  159 GLY   B O   
1406 N N   . SER   B 151 ? 0.9128 1.2982 0.9077 0.2997  0.2117  0.2083  160 SER   B N   
1407 C CA  A SER   B 151 ? 0.9470 1.2724 0.8831 0.3121  0.1986  0.1928  160 SER   B CA  
1408 C CA  B SER   B 151 ? 0.9480 1.2730 0.8848 0.3110  0.1987  0.1932  160 SER   B CA  
1409 C C   . SER   B 151 ? 0.9544 1.2356 0.8823 0.3001  0.1665  0.1684  160 SER   B C   
1410 O O   . SER   B 151 ? 0.9405 1.2372 0.8979 0.2920  0.1525  0.1599  160 SER   B O   
1411 C CB  A SER   B 151 ? 0.9754 1.3069 0.8661 0.3566  0.2055  0.1852  160 SER   B CB  
1412 C CB  B SER   B 151 ? 0.9806 1.3088 0.8691 0.3547  0.2071  0.1873  160 SER   B CB  
1413 O OG  A SER   B 151 ? 1.0357 1.3120 0.8725 0.3682  0.1927  0.1717  160 SER   B OG  
1414 O OG  B SER   B 151 ? 0.9858 1.3667 0.8891 0.3809  0.2169  0.1869  160 SER   B OG  
1415 N N   . TYR   B 152 ? 0.9581 1.1860 0.8465 0.2990  0.1551  0.1582  161 TYR   B N   
1416 C CA  . TYR   B 152 ? 0.9552 1.1413 0.8320 0.2880  0.1281  0.1376  161 TYR   B CA  
1417 C C   . TYR   B 152 ? 0.9588 1.1199 0.7915 0.3178  0.1140  0.1187  161 TYR   B C   
1418 O O   . TYR   B 152 ? 0.9739 1.1270 0.7728 0.3408  0.1220  0.1197  161 TYR   B O   
1419 C CB  . TYR   B 152 ? 0.9633 1.1096 0.8338 0.2627  0.1247  0.1396  161 TYR   B CB  
1420 C CG  . TYR   B 152 ? 0.9674 1.0878 0.8471 0.2401  0.1028  0.1252  161 TYR   B CG  
1421 C CD1 . TYR   B 152 ? 0.9542 1.0935 0.8736 0.2173  0.0982  0.1280  161 TYR   B CD1 
1422 C CD2 . TYR   B 152 ? 0.9962 1.0749 0.8448 0.2417  0.0867  0.1092  161 TYR   B CD2 
1423 C CE1 . TYR   B 152 ? 0.9682 1.0834 0.8899 0.1993  0.0783  0.1145  161 TYR   B CE1 
1424 C CE2 . TYR   B 152 ? 1.0074 1.0654 0.8616 0.2223  0.0693  0.0977  161 TYR   B CE2 
1425 C CZ  . TYR   B 152 ? 0.9989 1.0741 0.8867 0.2021  0.0654  0.1002  161 TYR   B CZ  
1426 O OH  . TYR   B 152 ? 1.0166 1.0711 0.9048 0.1848  0.0488  0.0889  161 TYR   B OH  
1427 N N   . VAL   B 153 ? 0.9400 1.0867 0.7720 0.3175  0.0915  0.1018  162 VAL   B N   
1428 C CA  . VAL   B 153 ? 0.9396 1.0551 0.7333 0.3404  0.0733  0.0834  162 VAL   B CA  
1429 C C   . VAL   B 153 ? 0.9254 1.0033 0.7180 0.3163  0.0527  0.0730  162 VAL   B C   
1430 O O   . VAL   B 153 ? 0.9148 0.9987 0.7295 0.3014  0.0427  0.0706  162 VAL   B O   
1431 C CB  . VAL   B 153 ? 0.9361 1.0739 0.7283 0.3692  0.0672  0.0750  162 VAL   B CB  
1432 C CG1 . VAL   B 153 ? 0.9652 1.0604 0.7222 0.3853  0.0412  0.0547  162 VAL   B CG1 
1433 C CG2 . VAL   B 153 ? 0.9290 1.1049 0.7155 0.3980  0.0902  0.0845  162 VAL   B CG2 
1434 N N   . SER   B 154 ? 0.9219 0.9647 0.6912 0.3108  0.0483  0.0688  163 SER   B N   
1435 C CA  . SER   B 154 ? 0.9162 0.9269 0.6844 0.2880  0.0326  0.0605  163 SER   B CA  
1436 C C   . SER   B 154 ? 0.9143 0.8963 0.6591 0.2990  0.0103  0.0452  163 SER   B C   
1437 O O   . SER   B 154 ? 0.9273 0.9012 0.6481 0.3244  0.0056  0.0386  163 SER   B O   
1438 C CB  . SER   B 154 ? 0.9345 0.9258 0.6951 0.2759  0.0395  0.0642  163 SER   B CB  
1439 O OG  . SER   B 154 ? 0.9729 0.9309 0.7188 0.2677  0.0244  0.0530  163 SER   B OG  
1440 N N   . ALA   B 155 ? 0.8974 0.8613 0.6471 0.2795  -0.0040 0.0399  164 ALA   B N   
1441 C CA  . ALA   B 155 ? 0.8986 0.8313 0.6280 0.2845  -0.0253 0.0284  164 ALA   B CA  
1442 C C   . ALA   B 155 ? 0.9023 0.8071 0.6149 0.2805  -0.0294 0.0236  164 ALA   B C   
1443 O O   . ALA   B 155 ? 0.8964 0.8051 0.6140 0.2714  -0.0166 0.0287  164 ALA   B O   
1444 C CB  . ALA   B 155 ? 0.8920 0.8170 0.6311 0.2643  -0.0369 0.0277  164 ALA   B CB  
1445 N N   . ILE   B 156 ? 0.9071 0.7834 0.6014 0.2878  -0.0488 0.0137  165 ILE   B N   
1446 C CA  . ILE   B 156 ? 0.9108 0.7632 0.5959 0.2812  -0.0562 0.0086  165 ILE   B CA  
1447 C C   . ILE   B 156 ? 0.9012 0.7424 0.5972 0.2534  -0.0626 0.0103  165 ILE   B C   
1448 O O   . ILE   B 156 ? 0.9068 0.7292 0.5965 0.2511  -0.0794 0.0071  165 ILE   B O   
1449 C CB  . ILE   B 156 ? 0.9303 0.7579 0.5922 0.3033  -0.0756 -0.0028 165 ILE   B CB  
1450 C CG1 . ILE   B 156 ? 0.9420 0.7832 0.5873 0.3354  -0.0680 -0.0049 165 ILE   B CG1 
1451 C CG2 . ILE   B 156 ? 0.9411 0.7469 0.6001 0.2935  -0.0854 -0.0080 165 ILE   B CG2 
1452 C CD1 . ILE   B 156 ? 0.9703 0.7853 0.5876 0.3618  -0.0885 -0.0189 165 ILE   B CD1 
1453 N N   . THR   B 157 ? 0.8817 0.7344 0.5922 0.2334  -0.0487 0.0160  166 THR   B N   
1454 C CA  . THR   B 157 ? 0.8697 0.7167 0.5878 0.2087  -0.0508 0.0179  166 THR   B CA  
1455 C C   . THR   B 157 ? 0.8696 0.7013 0.5868 0.1974  -0.0560 0.0148  166 THR   B C   
1456 O O   . THR   B 157 ? 0.8645 0.7020 0.5878 0.1941  -0.0464 0.0141  166 THR   B O   
1457 C CB  . THR   B 157 ? 0.8597 0.7254 0.5923 0.1947  -0.0355 0.0234  166 THR   B CB  
1458 O OG1 . THR   B 157 ? 0.8586 0.7436 0.5987 0.2043  -0.0301 0.0274  166 THR   B OG1 
1459 C CG2 . THR   B 157 ? 0.8598 0.7205 0.5939 0.1741  -0.0387 0.0244  166 THR   B CG2 
1460 N N   . GLN   B 158 ? 0.8730 0.6859 0.5845 0.1908  -0.0713 0.0138  167 GLN   B N   
1461 C CA  . GLN   B 158 ? 0.8813 0.6834 0.5974 0.1771  -0.0768 0.0128  167 GLN   B CA  
1462 C C   . GLN   B 158 ? 0.9052 0.7068 0.6241 0.1540  -0.0744 0.0196  167 GLN   B C   
1463 O O   . GLN   B 158 ? 0.9113 0.7079 0.6221 0.1516  -0.0791 0.0238  167 GLN   B O   
1464 C CB  . GLN   B 158 ? 0.8955 0.6734 0.6031 0.1874  -0.0982 0.0074  167 GLN   B CB  
1465 C CG  . GLN   B 158 ? 0.9079 0.6755 0.6259 0.1732  -0.1072 0.0065  167 GLN   B CG  
1466 C CD  . GLN   B 158 ? 0.9111 0.6947 0.6419 0.1735  -0.0974 0.0026  167 GLN   B CD  
1467 O OE1 . GLN   B 158 ? 0.9229 0.7263 0.6625 0.1652  -0.0792 0.0057  167 GLN   B OE1 
1468 N NE2 . GLN   B 158 ? 0.8950 0.6684 0.6268 0.1832  -0.1113 -0.0050 167 GLN   B NE2 
1469 N N   . GLY   B 159 ? 0.9180 0.7266 0.6472 0.1389  -0.0667 0.0208  168 GLY   B N   
1470 C CA  . GLY   B 159 ? 0.9455 0.7562 0.6744 0.1185  -0.0618 0.0278  168 GLY   B CA  
1471 C C   . GLY   B 159 ? 0.9874 0.7803 0.7157 0.1068  -0.0755 0.0337  168 GLY   B C   
1472 O O   . GLY   B 159 ? 0.9943 0.7675 0.7197 0.1155  -0.0930 0.0313  168 GLY   B O   
1473 N N   . LYS   B 160 ? 1.0133 0.8123 0.7438 0.0870  -0.0677 0.0418  169 LYS   B N   
1474 C CA  . LYS   B 160 ? 1.0498 0.8340 0.7831 0.0713  -0.0783 0.0513  169 LYS   B CA  
1475 C C   . LYS   B 160 ? 1.0680 0.8734 0.8239 0.0565  -0.0669 0.0537  169 LYS   B C   
1476 O O   . LYS   B 160 ? 1.0651 0.8948 0.8240 0.0522  -0.0475 0.0531  169 LYS   B O   
1477 C CB  . LYS   B 160 ? 1.0867 0.8572 0.7994 0.0603  -0.0807 0.0633  169 LYS   B CB  
1478 C CG  . LYS   B 160 ? 1.1543 0.8977 0.8655 0.0475  -0.0978 0.0747  169 LYS   B CG  
1479 C CD  . LYS   B 160 ? 1.2277 0.9598 0.9176 0.0331  -0.0966 0.0903  169 LYS   B CD  
1480 C CE  . LYS   B 160 ? 1.2792 0.9849 0.9711 0.0155  -0.1110 0.1052  169 LYS   B CE  
1481 N NZ  . LYS   B 160 ? 1.3193 1.0144 0.9876 0.0003  -0.1074 0.1235  169 LYS   B NZ  
1482 N N   . ARG   B 161 ? 1.0819 0.8790 0.8555 0.0503  -0.0803 0.0550  170 ARG   B N   
1483 C CA  . ARG   B 161 ? 1.0847 0.9056 0.8866 0.0355  -0.0719 0.0580  170 ARG   B CA  
1484 C C   . ARG   B 161 ? 1.1064 0.9236 0.9100 0.0101  -0.0705 0.0764  170 ARG   B C   
1485 O O   . ARG   B 161 ? 1.1260 0.9118 0.9225 0.0036  -0.0897 0.0841  170 ARG   B O   
1486 C CB  . ARG   B 161 ? 1.0951 0.9109 0.9190 0.0423  -0.0894 0.0487  170 ARG   B CB  
1487 C CG  . ARG   B 161 ? 1.1115 0.9555 0.9716 0.0269  -0.0836 0.0516  170 ARG   B CG  
1488 C CD  . ARG   B 161 ? 1.1463 0.9915 1.0282 0.0380  -0.0997 0.0387  170 ARG   B CD  
1489 N NE  . ARG   B 161 ? 1.1644 1.0410 1.0867 0.0215  -0.0951 0.0424  170 ARG   B NE  
1490 C CZ  . ARG   B 161 ? 1.1713 1.0734 1.1170 0.0314  -0.0929 0.0314  170 ARG   B CZ  
1491 N NH1 . ARG   B 161 ? 1.1709 1.0669 1.1003 0.0572  -0.0951 0.0173  170 ARG   B NH1 
1492 N NH2 . ARG   B 161 ? 1.1431 1.0783 1.1295 0.0158  -0.0884 0.0356  170 ARG   B NH2 
1493 N N   . GLU   B 162 ? 1.1034 0.9505 0.9133 -0.0030 -0.0478 0.0842  171 GLU   B N   
1494 C CA  . GLU   B 162 ? 1.1187 0.9662 0.9273 -0.0273 -0.0422 0.1046  171 GLU   B CA  
1495 C C   . GLU   B 162 ? 1.1021 0.9611 0.9497 -0.0466 -0.0475 0.1132  171 GLU   B C   
1496 O O   . GLU   B 162 ? 1.1033 0.9533 0.9538 -0.0690 -0.0499 0.1327  171 GLU   B O   
1497 C CB  . GLU   B 162 ? 1.1619 1.0376 0.9556 -0.0310 -0.0145 0.1095  171 GLU   B CB  
1498 C CG  . GLU   B 162 ? 1.2758 1.1394 1.0332 -0.0151 -0.0119 0.1016  171 GLU   B CG  
1499 C CD  . GLU   B 162 ? 1.4259 1.2596 1.1498 -0.0214 -0.0209 0.1150  171 GLU   B CD  
1500 O OE1 . GLU   B 162 ? 1.4538 1.2965 1.1560 -0.0294 -0.0061 0.1250  171 GLU   B OE1 
1501 O OE2 . GLU   B 162 ? 1.4815 1.2824 1.1986 -0.0162 -0.0434 0.1150  171 GLU   B OE2 
1502 S S   . DMS   C .   ? 1.4231 1.1672 1.1033 0.1013  -0.0117 -0.1003 201 DMS   B S   
1503 O O   . DMS   C .   ? 1.4146 1.1877 1.0886 0.1059  0.0032  -0.0921 201 DMS   B O   
1504 C C1  . DMS   C .   ? 1.4318 1.1520 1.1112 0.1165  -0.0079 -0.1135 201 DMS   B C1  
1505 C C2  . DMS   C .   ? 1.4100 1.1532 1.1291 0.0904  -0.0141 -0.0799 201 DMS   B C2  
1506 N N1  . A1B8K D .   ? 0.8331 0.8272 0.7212 0.1377  0.0465  0.0849  202 A1B8K B N1  
1507 N N3  . A1B8K D .   ? 0.8888 0.8806 0.7293 0.1880  0.0846  0.1109  202 A1B8K B N3  
1508 C C4  . A1B8K D .   ? 0.8083 0.7703 0.7101 0.0912  0.0130  0.0599  202 A1B8K B C4  
1509 C C5  . A1B8K D .   ? 0.8091 0.7686 0.6908 0.0984  0.0029  0.0506  202 A1B8K B C5  
1510 C C6  . A1B8K D .   ? 0.8118 0.7774 0.6795 0.1163  0.0059  0.0524  202 A1B8K B C6  
1511 C C7  . A1B8K D .   ? 0.8170 0.7940 0.6881 0.1296  0.0192  0.0622  202 A1B8K B C7  
1512 C C8  . A1B8K D .   ? 0.8141 0.7694 0.6609 0.1183  -0.0078 0.0429  202 A1B8K B C8  
1513 C C10 . A1B8K D .   ? 0.8517 0.8686 0.7455 0.1543  0.0759  0.1116  202 A1B8K B C10 
1514 C C13 . A1B8K D .   ? 0.8536 0.9041 0.7416 0.1819  0.1064  0.1382  202 A1B8K B C13 
1515 C C15 . A1B8K D .   ? 0.8423 0.8918 0.7543 0.1604  0.0926  0.1297  202 A1B8K B C15 
1516 O O1  . A1B8K D .   ? 0.8263 0.8511 0.7670 0.1169  0.0604  0.1079  202 A1B8K B O1  
1517 C C1  . A1B8K D .   ? 0.8371 0.8492 0.7468 0.1346  0.0605  0.1011  202 A1B8K B C1  
1518 C C2  . A1B8K D .   ? 0.8194 0.8016 0.7084 0.1231  0.0315  0.0731  202 A1B8K B C2  
1519 C C3  . A1B8K D .   ? 0.8097 0.7841 0.7160 0.1028  0.0281  0.0728  202 A1B8K B C3  
1520 N N2  . A1B8K D .   ? 0.8086 0.7630 0.6640 0.1024  -0.0185 0.0377  202 A1B8K B N2  
1521 C C9  . A1B8K D .   ? 0.8110 0.7574 0.6785 0.0900  -0.0124 0.0382  202 A1B8K B C9  
1522 C C11 . A1B8K D .   ? 0.8781 0.8697 0.7379 0.1687  0.0738  0.1035  202 A1B8K B C11 
1523 C C12 . A1B8K D .   ? 0.8760 0.8955 0.7270 0.1957  0.1006  0.1274  202 A1B8K B C12 
1524 N N4  . A1B8K D .   ? 0.8365 0.9236 0.7468 0.1842  0.1237  0.1569  202 A1B8K B N4  
1525 N N5  . A1B8K D .   ? 0.8145 0.9262 0.7667 0.1642  0.1205  0.1606  202 A1B8K B N5  
1526 C C14 . A1B8K D .   ? 0.8197 0.9071 0.7712 0.1504  0.1006  0.1436  202 A1B8K B C14 
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