data_7I9P
# 
_entry.id   7I9P 
# 
_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   7I9P         pdb_00007i9p 10.2210/pdb7i9p/pdb 
WWPDB D_1001408492 ?            ?                   
# 
_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                        7I9P 
_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    3   ?                           ? ? 
? 
4 non-polymer syn '3-(aminomethyl)-5-chloro-N-[3-(2H-tetrazol-5-yl)phenyl]benzamide' 328.756   1   ?                           ? ? 
? 
5 non-polymer syn 'SULFATE ION'                                                      96.063    1   ?                           ? ? 
? 
6 water       nat water                                                              18.015    116 ?                           ? ? 
? 
# 
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 '3-(aminomethyl)-5-chloro-N-[3-(2H-tetrazol-5-yl)phenyl]benzamide' A1B9N 
5 'SULFATE ION'                                                      SO4   
6 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 
A1B9N non-polymer         . '3-(aminomethyl)-5-chloro-N-[3-(2H-tetrazol-5-yl)phenyl]benzamide' ? 'C15 H13 Cl N6 O' 328.756 
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 
SO4   non-polymer         . 'SULFATE ION'                                                      ? 'O4 S -2'         96.063  
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 3 DMS   1  202 203 DMS   DMS B . 
E 4 A1B9N 1  203 204 A1B9N LIG B . 
F 5 SO4   1  204 205 SO4   SO4 B . 
G 3 DMS   1  205 206 DMS   DMS B . 
H 6 HOH   1  101 149 HOH   HOH A . 
H 6 HOH   2  102 121 HOH   HOH A . 
H 6 HOH   3  103 154 HOH   HOH A . 
H 6 HOH   4  104 98  HOH   HOH A . 
H 6 HOH   5  105 48  HOH   HOH A . 
H 6 HOH   6  106 118 HOH   HOH A . 
H 6 HOH   7  107 49  HOH   HOH A . 
H 6 HOH   8  108 65  HOH   HOH A . 
H 6 HOH   9  109 34  HOH   HOH A . 
H 6 HOH   10 110 117 HOH   HOH A . 
H 6 HOH   11 111 141 HOH   HOH A . 
H 6 HOH   12 112 136 HOH   HOH A . 
H 6 HOH   13 113 28  HOH   HOH A . 
H 6 HOH   14 114 36  HOH   HOH A . 
H 6 HOH   15 115 16  HOH   HOH A . 
H 6 HOH   16 116 137 HOH   HOH A . 
H 6 HOH   17 117 156 HOH   HOH A . 
H 6 HOH   18 118 20  HOH   HOH A . 
H 6 HOH   19 119 50  HOH   HOH A . 
H 6 HOH   20 120 144 HOH   HOH A . 
H 6 HOH   21 121 105 HOH   HOH A . 
H 6 HOH   22 122 120 HOH   HOH A . 
H 6 HOH   23 123 29  HOH   HOH A . 
H 6 HOH   24 124 70  HOH   HOH A . 
H 6 HOH   25 125 151 HOH   HOH A . 
H 6 HOH   26 126 140 HOH   HOH A . 
H 6 HOH   27 127 110 HOH   HOH A . 
H 6 HOH   28 128 126 HOH   HOH A . 
H 6 HOH   29 129 77  HOH   HOH A . 
H 6 HOH   30 130 119 HOH   HOH A . 
H 6 HOH   31 131 27  HOH   HOH A . 
H 6 HOH   32 132 145 HOH   HOH A . 
H 6 HOH   33 133 157 HOH   HOH A . 
I 6 HOH   1  301 127 HOH   HOH B . 
I 6 HOH   2  302 11  HOH   HOH B . 
I 6 HOH   3  303 9   HOH   HOH B . 
I 6 HOH   4  304 46  HOH   HOH B . 
I 6 HOH   5  305 89  HOH   HOH B . 
I 6 HOH   6  306 138 HOH   HOH B . 
I 6 HOH   7  307 129 HOH   HOH B . 
I 6 HOH   8  308 135 HOH   HOH B . 
I 6 HOH   9  309 131 HOH   HOH B . 
I 6 HOH   10 310 100 HOH   HOH B . 
I 6 HOH   11 311 72  HOH   HOH B . 
I 6 HOH   12 312 5   HOH   HOH B . 
I 6 HOH   13 313 90  HOH   HOH B . 
I 6 HOH   14 314 14  HOH   HOH B . 
I 6 HOH   15 315 39  HOH   HOH B . 
I 6 HOH   16 316 54  HOH   HOH B . 
I 6 HOH   17 317 51  HOH   HOH B . 
I 6 HOH   18 318 69  HOH   HOH B . 
I 6 HOH   19 319 153 HOH   HOH B . 
I 6 HOH   20 320 13  HOH   HOH B . 
I 6 HOH   21 321 63  HOH   HOH B . 
I 6 HOH   22 322 128 HOH   HOH B . 
I 6 HOH   23 323 10  HOH   HOH B . 
I 6 HOH   24 324 31  HOH   HOH B . 
I 6 HOH   25 325 4   HOH   HOH B . 
I 6 HOH   26 326 56  HOH   HOH B . 
I 6 HOH   27 327 66  HOH   HOH B . 
I 6 HOH   28 328 24  HOH   HOH B . 
I 6 HOH   29 329 133 HOH   HOH B . 
I 6 HOH   30 330 123 HOH   HOH B . 
I 6 HOH   31 331 1   HOH   HOH B . 
I 6 HOH   32 332 2   HOH   HOH B . 
I 6 HOH   33 333 134 HOH   HOH B . 
I 6 HOH   34 334 81  HOH   HOH B . 
I 6 HOH   35 335 92  HOH   HOH B . 
I 6 HOH   36 336 58  HOH   HOH B . 
I 6 HOH   37 337 32  HOH   HOH B . 
I 6 HOH   38 338 68  HOH   HOH B . 
I 6 HOH   39 339 12  HOH   HOH B . 
I 6 HOH   40 340 115 HOH   HOH B . 
I 6 HOH   41 341 152 HOH   HOH B . 
I 6 HOH   42 342 124 HOH   HOH B . 
I 6 HOH   43 343 30  HOH   HOH B . 
I 6 HOH   44 344 43  HOH   HOH B . 
I 6 HOH   45 345 23  HOH   HOH B . 
I 6 HOH   46 346 130 HOH   HOH B . 
I 6 HOH   47 347 3   HOH   HOH B . 
I 6 HOH   48 348 21  HOH   HOH B . 
I 6 HOH   49 349 108 HOH   HOH B . 
I 6 HOH   50 350 35  HOH   HOH B . 
I 6 HOH   51 351 125 HOH   HOH B . 
I 6 HOH   52 352 116 HOH   HOH B . 
I 6 HOH   53 353 60  HOH   HOH B . 
I 6 HOH   54 354 17  HOH   HOH B . 
I 6 HOH   55 355 82  HOH   HOH B . 
I 6 HOH   56 356 80  HOH   HOH B . 
I 6 HOH   57 357 18  HOH   HOH B . 
I 6 HOH   58 358 73  HOH   HOH B . 
I 6 HOH   59 359 94  HOH   HOH B . 
I 6 HOH   60 360 67  HOH   HOH B . 
I 6 HOH   61 361 62  HOH   HOH B . 
I 6 HOH   62 362 146 HOH   HOH B . 
I 6 HOH   63 363 107 HOH   HOH B . 
I 6 HOH   64 364 64  HOH   HOH B . 
I 6 HOH   65 365 155 HOH   HOH B . 
I 6 HOH   66 366 102 HOH   HOH B . 
I 6 HOH   67 367 150 HOH   HOH B . 
I 6 HOH   68 368 42  HOH   HOH B . 
I 6 HOH   69 369 139 HOH   HOH B . 
I 6 HOH   70 370 61  HOH   HOH B . 
I 6 HOH   71 371 26  HOH   HOH B . 
I 6 HOH   72 372 87  HOH   HOH B . 
I 6 HOH   73 373 112 HOH   HOH B . 
I 6 HOH   74 374 59  HOH   HOH B . 
I 6 HOH   75 375 158 HOH   HOH B . 
I 6 HOH   76 376 75  HOH   HOH B . 
I 6 HOH   77 377 109 HOH   HOH B . 
I 6 HOH   78 378 45  HOH   HOH B . 
I 6 HOH   79 379 148 HOH   HOH B . 
I 6 HOH   80 380 132 HOH   HOH B . 
I 6 HOH   81 381 57  HOH   HOH B . 
I 6 HOH   82 382 147 HOH   HOH B . 
I 6 HOH   83 383 44  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (23-JAN-2024)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.7.15                 02/11/23        program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7I9P 
_cell.length_a           42.735 
_cell.length_b           42.735 
_cell.length_c           217.039 
_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                         7I9P 
_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          7I9P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.080 
_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   42.44 
_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   2024-07-05 
_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                     7I9P 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.260 
_reflns.d_resolution_high            1.540 
_reflns.number_obs                   31371 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.225 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.800 
_reflns.B_iso_Wilson_estimate        28.950 
_reflns.pdbx_redundancy              19.900 
_reflns.pdbx_Rrim_I_all              0.231 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     624381 
_reflns.pdbx_scaling_rejects         714 
_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 1.540 1.620  ? 78019 ? ? ?     ? ? ? 17.600 ? 0.300  ? 4435 ? ? ? ? 100.000 21.766 5.048 0.665 ? 
1 2 4.860 54.260 ? 19470 ? ? 0.072 ? ? ? 16.300 ? 33.200 ? 1197 ? ? ? ? 99.800  0.074  0.018 0.996 ? 
# 
_refine.entry_id                                 7I9P 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.5380 
_refine.ls_d_res_low                             54.2600 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    93.7000 
_refine.ls_number_reflns_obs                     29302 
_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                          0.2224 
_refine.ls_R_factor_R_work                       0.2205 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2590 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.0300 
_refine.ls_number_reflns_R_free                  1474 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               40.6100 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -4.1790 
_refine.aniso_B[2][2]                            -4.1790 
_refine.aniso_B[3][3]                            8.3581 
_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               0.9500 
_refine.correlation_coeff_Fo_to_Fc_free          0.9340 
_refine.overall_SU_R_Cruickshank_DPI             0.0940 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.0970 
_refine.pdbx_overall_SU_R_Blow_DPI               0.0990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1010 
_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                                158.640 
_refine.B_iso_min                                22.260 
_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                        7I9P 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.270 
_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                       1.5380 
_refine_hist.d_res_low                        54.2600 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             116 
_refine_hist.number_atoms_total               1632 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           66.31 
_refine_hist.pdbx_B_iso_mean_solvent          45.73 
_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        535  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              293  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1581 ?      ? 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 196  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1281 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1581 0.010  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2151 1.020  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.900  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    15.520 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.5400 
_refine_ls_shell.d_res_low                        1.5600 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.percent_reflns_obs               50.0400 
_refine_ls_shell.number_reflns_R_work             557 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.4601 
_refine_ls_shell.R_factor_R_free                  0.4788 
_refine_ls_shell.percent_reflns_R_free            5.1100 
_refine_ls_shell.number_reflns_R_free             30 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                587 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7I9P 
_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-0027707-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I9P 
_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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 3 ? 
H N N 6 ? 
I N N 6 ? 
# 
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 7I9P A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I9P 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 7I9P SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I9P MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I9P MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I9P 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)' 4840 ? 
1 MORE         -37  ? 
1 'SSA (A^2)'  9760 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N 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 TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O 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 GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7I9P 
_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 CYS B 80  ? ? 77.41   -11.18 
2 1 LEU B 92  ? ? -130.82 -38.30 
3 1 LYS B 157 ? ? -60.65  31.74  
# 
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 -14.0752 -1.2432 -19.5491 0.0141 -0.0494 -0.1657 0.1036 0.0703 0.0614 2.7154 2.9828 3.3875 -1.7368 
0.6032 0.7053 0.3698 -0.3161 -0.0537 0.3159 0.1860 -0.1928 -0.4436 -0.0202 0.4449 
'X-RAY DIFFRACTION' 2 ? refined -18.6123 1.4721  -15.7460 0.0881 -0.0216 -0.0348 0.1017 0.0027 0.0054 1.0409 1.0563 1.9331 -0.9700 
0.4455 0.0686 0.2615 -0.2467 -0.0148 0.0859 0.0321 0.0697  -0.1842 -0.0015 0.1532 
# 
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 
A1B9N N1   N  N N 1   
A1B9N N3   N  Y N 2   
A1B9N C4   C  Y N 3   
A1B9N C5   C  Y N 4   
A1B9N C6   C  N N 5   
A1B9N C7   C  Y N 6   
A1B9N C8   C  Y N 7   
A1B9N C10  C  Y N 8   
A1B9N C13  C  Y N 9   
A1B9N O    O  N N 10  
A1B9N C3   C  Y N 11  
A1B9N CL   CL N N 12  
A1B9N C2   C  Y N 13  
A1B9N C14  C  Y N 14  
A1B9N C1   C  Y N 15  
A1B9N C    C  N N 16  
A1B9N N    N  N N 17  
A1B9N C11  C  Y N 18  
A1B9N C9   C  Y N 19  
A1B9N C12  C  Y N 20  
A1B9N N5   N  Y N 21  
A1B9N N4   N  Y N 22  
A1B9N N2   N  Y N 23  
A1B9N H7   H  N N 24  
A1B9N H6   H  N N 25  
A1B9N H8   H  N N 26  
A1B9N H10  H  N N 27  
A1B9N H11  H  N N 28  
A1B9N H5   H  N N 29  
A1B9N H12  H  N N 30  
A1B9N H3   H  N N 31  
A1B9N H4   H  N N 32  
A1B9N H1   H  N N 33  
A1B9N H13  H  N N 34  
A1B9N H9   H  N N 35  
A1B9N H    H  N N 36  
ALA   N    N  N N 37  
ALA   CA   C  N S 38  
ALA   C    C  N N 39  
ALA   O    O  N N 40  
ALA   CB   C  N N 41  
ALA   OXT  O  N N 42  
ALA   H    H  N N 43  
ALA   H2   H  N N 44  
ALA   HA   H  N N 45  
ALA   HB1  H  N N 46  
ALA   HB2  H  N N 47  
ALA   HB3  H  N N 48  
ALA   HXT  H  N N 49  
ARG   N    N  N N 50  
ARG   CA   C  N S 51  
ARG   C    C  N N 52  
ARG   O    O  N N 53  
ARG   CB   C  N N 54  
ARG   CG   C  N N 55  
ARG   CD   C  N N 56  
ARG   NE   N  N N 57  
ARG   CZ   C  N N 58  
ARG   NH1  N  N N 59  
ARG   NH2  N  N N 60  
ARG   OXT  O  N N 61  
ARG   H    H  N N 62  
ARG   H2   H  N N 63  
ARG   HA   H  N N 64  
ARG   HB2  H  N N 65  
ARG   HB3  H  N N 66  
ARG   HG2  H  N N 67  
ARG   HG3  H  N N 68  
ARG   HD2  H  N N 69  
ARG   HD3  H  N N 70  
ARG   HE   H  N N 71  
ARG   HH11 H  N N 72  
ARG   HH12 H  N N 73  
ARG   HH21 H  N N 74  
ARG   HH22 H  N N 75  
ARG   HXT  H  N N 76  
ASN   N    N  N N 77  
ASN   CA   C  N S 78  
ASN   C    C  N N 79  
ASN   O    O  N N 80  
ASN   CB   C  N N 81  
ASN   CG   C  N N 82  
ASN   OD1  O  N N 83  
ASN   ND2  N  N N 84  
ASN   OXT  O  N N 85  
ASN   H    H  N N 86  
ASN   H2   H  N N 87  
ASN   HA   H  N N 88  
ASN   HB2  H  N N 89  
ASN   HB3  H  N N 90  
ASN   HD21 H  N N 91  
ASN   HD22 H  N N 92  
ASN   HXT  H  N N 93  
ASP   N    N  N N 94  
ASP   CA   C  N S 95  
ASP   C    C  N N 96  
ASP   O    O  N N 97  
ASP   CB   C  N N 98  
ASP   CG   C  N N 99  
ASP   OD1  O  N N 100 
ASP   OD2  O  N N 101 
ASP   OXT  O  N N 102 
ASP   H    H  N N 103 
ASP   H2   H  N N 104 
ASP   HA   H  N N 105 
ASP   HB2  H  N N 106 
ASP   HB3  H  N N 107 
ASP   HD2  H  N N 108 
ASP   HXT  H  N N 109 
CYS   N    N  N N 110 
CYS   CA   C  N R 111 
CYS   C    C  N N 112 
CYS   O    O  N N 113 
CYS   CB   C  N N 114 
CYS   SG   S  N N 115 
CYS   OXT  O  N N 116 
CYS   H    H  N N 117 
CYS   H2   H  N N 118 
CYS   HA   H  N N 119 
CYS   HB2  H  N N 120 
CYS   HB3  H  N N 121 
CYS   HG   H  N N 122 
CYS   HXT  H  N N 123 
DMS   S    S  N N 124 
DMS   O    O  N N 125 
DMS   C1   C  N N 126 
DMS   C2   C  N N 127 
DMS   H11  H  N N 128 
DMS   H12  H  N N 129 
DMS   H13  H  N N 130 
DMS   H21  H  N N 131 
DMS   H22  H  N N 132 
DMS   H23  H  N N 133 
GLN   N    N  N N 134 
GLN   CA   C  N S 135 
GLN   C    C  N N 136 
GLN   O    O  N N 137 
GLN   CB   C  N N 138 
GLN   CG   C  N N 139 
GLN   CD   C  N N 140 
GLN   OE1  O  N N 141 
GLN   NE2  N  N N 142 
GLN   OXT  O  N N 143 
GLN   H    H  N N 144 
GLN   H2   H  N N 145 
GLN   HA   H  N N 146 
GLN   HB2  H  N N 147 
GLN   HB3  H  N N 148 
GLN   HG2  H  N N 149 
GLN   HG3  H  N N 150 
GLN   HE21 H  N N 151 
GLN   HE22 H  N N 152 
GLN   HXT  H  N N 153 
GLU   N    N  N N 154 
GLU   CA   C  N S 155 
GLU   C    C  N N 156 
GLU   O    O  N N 157 
GLU   CB   C  N N 158 
GLU   CG   C  N N 159 
GLU   CD   C  N N 160 
GLU   OE1  O  N N 161 
GLU   OE2  O  N N 162 
GLU   OXT  O  N N 163 
GLU   H    H  N N 164 
GLU   H2   H  N N 165 
GLU   HA   H  N N 166 
GLU   HB2  H  N N 167 
GLU   HB3  H  N N 168 
GLU   HG2  H  N N 169 
GLU   HG3  H  N N 170 
GLU   HE2  H  N N 171 
GLU   HXT  H  N N 172 
GLY   N    N  N N 173 
GLY   CA   C  N N 174 
GLY   C    C  N N 175 
GLY   O    O  N N 176 
GLY   OXT  O  N N 177 
GLY   H    H  N N 178 
GLY   H2   H  N N 179 
GLY   HA2  H  N N 180 
GLY   HA3  H  N N 181 
GLY   HXT  H  N N 182 
HIS   N    N  N N 183 
HIS   CA   C  N S 184 
HIS   C    C  N N 185 
HIS   O    O  N N 186 
HIS   CB   C  N N 187 
HIS   CG   C  Y N 188 
HIS   ND1  N  Y N 189 
HIS   CD2  C  Y N 190 
HIS   CE1  C  Y N 191 
HIS   NE2  N  Y N 192 
HIS   OXT  O  N N 193 
HIS   H    H  N N 194 
HIS   H2   H  N N 195 
HIS   HA   H  N N 196 
HIS   HB2  H  N N 197 
HIS   HB3  H  N N 198 
HIS   HD1  H  N N 199 
HIS   HD2  H  N N 200 
HIS   HE1  H  N N 201 
HIS   HE2  H  N N 202 
HIS   HXT  H  N N 203 
HOH   O    O  N N 204 
HOH   H1   H  N N 205 
HOH   H2   H  N N 206 
ILE   N    N  N N 207 
ILE   CA   C  N S 208 
ILE   C    C  N N 209 
ILE   O    O  N N 210 
ILE   CB   C  N S 211 
ILE   CG1  C  N N 212 
ILE   CG2  C  N N 213 
ILE   CD1  C  N N 214 
ILE   OXT  O  N N 215 
ILE   H    H  N N 216 
ILE   H2   H  N N 217 
ILE   HA   H  N N 218 
ILE   HB   H  N N 219 
ILE   HG12 H  N N 220 
ILE   HG13 H  N N 221 
ILE   HG21 H  N N 222 
ILE   HG22 H  N N 223 
ILE   HG23 H  N N 224 
ILE   HD11 H  N N 225 
ILE   HD12 H  N N 226 
ILE   HD13 H  N N 227 
ILE   HXT  H  N N 228 
LEU   N    N  N N 229 
LEU   CA   C  N S 230 
LEU   C    C  N N 231 
LEU   O    O  N N 232 
LEU   CB   C  N N 233 
LEU   CG   C  N N 234 
LEU   CD1  C  N N 235 
LEU   CD2  C  N N 236 
LEU   OXT  O  N N 237 
LEU   H    H  N N 238 
LEU   H2   H  N N 239 
LEU   HA   H  N N 240 
LEU   HB2  H  N N 241 
LEU   HB3  H  N N 242 
LEU   HG   H  N N 243 
LEU   HD11 H  N N 244 
LEU   HD12 H  N N 245 
LEU   HD13 H  N N 246 
LEU   HD21 H  N N 247 
LEU   HD22 H  N N 248 
LEU   HD23 H  N N 249 
LEU   HXT  H  N N 250 
LYS   N    N  N N 251 
LYS   CA   C  N S 252 
LYS   C    C  N N 253 
LYS   O    O  N N 254 
LYS   CB   C  N N 255 
LYS   CG   C  N N 256 
LYS   CD   C  N N 257 
LYS   CE   C  N N 258 
LYS   NZ   N  N N 259 
LYS   OXT  O  N N 260 
LYS   H    H  N N 261 
LYS   H2   H  N N 262 
LYS   HA   H  N N 263 
LYS   HB2  H  N N 264 
LYS   HB3  H  N N 265 
LYS   HG2  H  N N 266 
LYS   HG3  H  N N 267 
LYS   HD2  H  N N 268 
LYS   HD3  H  N N 269 
LYS   HE2  H  N N 270 
LYS   HE3  H  N N 271 
LYS   HZ1  H  N N 272 
LYS   HZ2  H  N N 273 
LYS   HZ3  H  N N 274 
LYS   HXT  H  N N 275 
MET   N    N  N N 276 
MET   CA   C  N S 277 
MET   C    C  N N 278 
MET   O    O  N N 279 
MET   CB   C  N N 280 
MET   CG   C  N N 281 
MET   SD   S  N N 282 
MET   CE   C  N N 283 
MET   OXT  O  N N 284 
MET   H    H  N N 285 
MET   H2   H  N N 286 
MET   HA   H  N N 287 
MET   HB2  H  N N 288 
MET   HB3  H  N N 289 
MET   HG2  H  N N 290 
MET   HG3  H  N N 291 
MET   HE1  H  N N 292 
MET   HE2  H  N N 293 
MET   HE3  H  N N 294 
MET   HXT  H  N N 295 
PHE   N    N  N N 296 
PHE   CA   C  N S 297 
PHE   C    C  N N 298 
PHE   O    O  N N 299 
PHE   CB   C  N N 300 
PHE   CG   C  Y N 301 
PHE   CD1  C  Y N 302 
PHE   CD2  C  Y N 303 
PHE   CE1  C  Y N 304 
PHE   CE2  C  Y N 305 
PHE   CZ   C  Y N 306 
PHE   OXT  O  N N 307 
PHE   H    H  N N 308 
PHE   H2   H  N N 309 
PHE   HA   H  N N 310 
PHE   HB2  H  N N 311 
PHE   HB3  H  N N 312 
PHE   HD1  H  N N 313 
PHE   HD2  H  N N 314 
PHE   HE1  H  N N 315 
PHE   HE2  H  N N 316 
PHE   HZ   H  N N 317 
PHE   HXT  H  N N 318 
PRO   N    N  N N 319 
PRO   CA   C  N S 320 
PRO   C    C  N N 321 
PRO   O    O  N N 322 
PRO   CB   C  N N 323 
PRO   CG   C  N N 324 
PRO   CD   C  N N 325 
PRO   OXT  O  N N 326 
PRO   H    H  N N 327 
PRO   HA   H  N N 328 
PRO   HB2  H  N N 329 
PRO   HB3  H  N N 330 
PRO   HG2  H  N N 331 
PRO   HG3  H  N N 332 
PRO   HD2  H  N N 333 
PRO   HD3  H  N N 334 
PRO   HXT  H  N N 335 
SER   N    N  N N 336 
SER   CA   C  N S 337 
SER   C    C  N N 338 
SER   O    O  N N 339 
SER   CB   C  N N 340 
SER   OG   O  N N 341 
SER   OXT  O  N N 342 
SER   H    H  N N 343 
SER   H2   H  N N 344 
SER   HA   H  N N 345 
SER   HB2  H  N N 346 
SER   HB3  H  N N 347 
SER   HG   H  N N 348 
SER   HXT  H  N N 349 
SO4   S    S  N N 350 
SO4   O1   O  N N 351 
SO4   O2   O  N N 352 
SO4   O3   O  N N 353 
SO4   O4   O  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
# 
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 
A1B9N N   C    sing N N 1   
A1B9N C   C1   sing N N 2   
A1B9N C1  C2   sing Y N 3   
A1B9N C2  C3   doub Y N 4   
A1B9N CL  C3   sing N N 5   
A1B9N C3  C4   sing Y N 6   
A1B9N C4  C5   doub Y N 7   
A1B9N C5  C6   sing N N 8   
A1B9N C6  O    doub N N 9   
A1B9N N1  C6   sing N N 10  
A1B9N C7  N1   sing N N 11  
A1B9N C7  C8   doub Y N 12  
A1B9N C8  C9   sing Y N 13  
A1B9N C9  C10  doub Y N 14  
A1B9N C10 C11  sing Y N 15  
A1B9N C12 C11  sing N N 16  
A1B9N C12 N2   sing Y N 17  
A1B9N N2  N3   doub Y N 18  
A1B9N N3  N4   sing Y N 19  
A1B9N N4  N5   sing Y N 20  
A1B9N N5  C12  doub Y N 21  
A1B9N C11 C13  doub Y N 22  
A1B9N C13 C7   sing Y N 23  
A1B9N C14 C5   sing Y N 24  
A1B9N C1  C14  doub Y N 25  
A1B9N N1  H7   sing N N 26  
A1B9N C4  H6   sing N N 27  
A1B9N C8  H8   sing N N 28  
A1B9N C10 H10  sing N N 29  
A1B9N C13 H11  sing N N 30  
A1B9N C2  H5   sing N N 31  
A1B9N C14 H12  sing N N 32  
A1B9N C   H3   sing N N 33  
A1B9N C   H4   sing N N 34  
A1B9N N   H1   sing N N 35  
A1B9N N   H13  sing N N 36  
A1B9N C9  H9   sing N N 37  
A1B9N N4  H    sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
SO4   S   O1   doub N N 337 
SO4   S   O2   doub N N 338 
SO4   S   O3   sing N N 339 
SO4   S   O4   sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7I9P 
_atom_sites.fract_transf_matrix[1][1]   0.023400 
_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]   0.023400 
_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]   0.004607 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -21.257 19.637  -7.531  1.00 47.76  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.548 18.958  -7.651  1.00 47.26  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.685 18.200  -8.991  1.00 44.70  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.759 18.797  -10.075 1.00 45.69  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.698 19.936  -7.448  1.00 50.96  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -25.011 19.244  -7.207  1.00 58.01  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.123 18.522  -6.185  1.00 60.41  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.932 19.425  -8.030  1.00 60.12  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.718 16.887  -8.899  1.00 40.93  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.766 16.043  -10.082 1.00 37.79  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -24.149 15.772  -10.606 1.00 34.59  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -25.091 15.652  -9.835  1.00 34.02  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -22.024 14.736  -9.838  1.00 37.79  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.566 14.946  -9.639  1.00 39.12  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.756 13.373  -9.218  1.00 39.54  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -18.115 13.960  -9.052  1.00 40.57  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -24.278 15.712  -11.935 1.00 32.04  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.558 15.460  -12.577 1.00 32.15  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.404 14.465  -13.721 1.00 31.51  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.301 14.278  -14.237 1.00 31.41  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -26.238 16.766  -13.049 1.00 32.85  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.466 17.517  -14.113 1.00 34.10  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.484 18.440  -13.766 1.00 36.18  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.829 17.433  -15.451 1.00 35.38  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.792 19.161  -14.738 1.00 37.14  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -25.159 18.164  -16.434 1.00 36.72  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -24.152 19.041  -16.071 1.00 38.38  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.441 19.712  -17.047 1.00 41.58  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.493 13.792  -14.099 1.00 30.77  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.430 12.812  -15.200 1.00 29.99  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -27.256 13.274  -16.405 1.00 30.09  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -28.239 14.017  -16.254 1.00 29.70  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.837 11.409  -14.742 1.00 29.98  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.322 11.388  -14.298 1.00 30.69  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.911 10.928  -13.587 1.00 29.58  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.834 9.959   -13.915 1.00 31.17  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.822 12.850  -17.608 1.00 30.17  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.484 13.207  -18.867 1.00 31.18  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.533 11.964  -19.703 1.00 31.72  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.490 11.296  -19.870 1.00 31.46  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.688 14.256  -19.675 1.00 34.98  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.284 15.528  -18.976 1.00 43.68  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.655 16.517  -19.944 1.00 52.49  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.961 16.074  -20.890 1.00 55.52  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.857 17.739  -19.756 1.00 57.24  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.708 11.632  -20.272 1.00 31.59  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.797 10.396  -21.073 1.00 32.40  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.881 10.480  -22.293 1.00 32.59  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.805 11.546  -22.898 1.00 34.09  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -30.251 10.146  -21.508 1.00 35.77  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.470 8.694   -21.931 1.00 39.38  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.943 8.326   -21.999 1.00 43.26  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -32.124 6.890   -22.212 1.00 44.29  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -32.108 6.313   -23.411 1.00 44.19  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.942 7.045   -24.506 1.00 44.03  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -32.239 4.997   -23.524 1.00 41.16  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -27.205 9.396   -22.642 1.00 31.89  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -26.305 9.353   -23.803 1.00 32.90  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.723 8.295   -24.858 1.00 33.83  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -26.201 8.320   -25.972 1.00 34.91  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.870 9.087   -23.355 1.00 33.22  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.583 7.346   -24.488 1.00 33.24  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -28.062 6.362   -25.450 1.00 34.59  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.656 5.117   -24.846 1.00 35.20  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.775 4.992   -23.629 1.00 35.02  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -29.119 4.227   -25.726 1.00 35.70  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.635 2.929   -25.351 1.00 36.13  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.445 1.998   -25.242 1.00 36.24  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -27.439 2.200   -25.935 1.00 37.77  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.520 2.352   -26.471 1.00 38.68  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.867 3.021   -26.644 1.00 45.50  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -32.092 4.071   -26.014 1.00 46.56  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.688 2.513   -27.450 1.00 48.79  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.605 0.913   -24.495 1.00 35.37  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.583 -0.121  -24.377 1.00 35.76  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.972 -1.277  -25.305 1.00 37.45  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.873 -2.069  -25.002 1.00 37.21  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.463 -0.538  -22.904 1.00 36.51  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.965 0.646   -22.067 1.00 37.50  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.549 -1.745  -22.770 1.00 37.04  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -27.135 0.472   -20.555 1.00 38.71  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.320 -1.345  -26.463 0.50 38.32  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -27.323 -1.344  -26.470 0.50 37.89  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.581 -2.385  -27.456 0.50 40.09  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.645 -2.325  -27.506 0.50 39.23  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.293 -2.822  -28.145 0.50 41.95  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.381 -2.759  -28.270 0.50 41.62  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.347 -2.044  -28.261 0.50 42.62  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.533 -1.914  -28.549 0.50 42.35  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.544 -1.888  -28.573 0.50 42.01  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.625 -1.655  -28.513 0.50 39.90  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -28.013 -0.724  -29.214 0.50 43.77  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.786 -1.150  -27.844 0.50 40.26  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.975 -1.662  -28.093 0.50 42.08  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -29.046 -2.574  -29.643 0.50 39.86  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.272 -4.052  -28.645 1.00 42.95  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -25.133 -4.552  -29.426 1.00 45.63  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -25.290 -3.987  -30.844 1.00 49.02  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.405 -4.003  -31.369 1.00 49.89  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -25.198 -6.079  -29.501 1.00 45.40  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -24.105 -6.738  -30.303 1.00 45.64  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -24.125 -7.026  -31.640 1.00 46.54  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.893 -7.305  -29.787 1.00 45.46  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.979 -7.702  -31.994 1.00 46.93  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -22.213 -7.900  -30.869 1.00 46.41  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -22.282 -7.310  -28.526 1.00 45.36  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.964 -8.507  -30.720 1.00 46.93  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -21.085 -7.982  -28.368 1.00 46.73  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.426 -8.552  -29.459 1.00 47.05  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -24.205 -3.473  -31.464 1.00 50.39  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -24.306 -2.931  -32.821 1.00 52.72  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.705 -3.961  -33.769 1.00 55.23  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.540 -4.338  -33.618 1.00 54.10  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.546 -1.596  -32.956 1.00 55.29  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.542 -1.045  -34.381 1.00 61.76  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.503 0.015   -34.699 1.00 67.41  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -21.711 0.367   -33.797 1.00 69.38  ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.475 0.490   -35.857 1.00 68.44  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -24.498 -4.425  -34.738 1.00 57.88  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -24.006 -5.392  -35.714 1.00 60.89  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.987 -4.690  -36.607 1.00 62.90  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -23.191 -3.528  -36.960 1.00 63.83  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -25.173 -5.939  -36.554 1.00 64.84  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -25.781 -7.220  -35.981 1.00 71.96  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -26.639 -7.960  -37.021 1.00 77.82  ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -27.041 -9.340  -36.548 1.00 82.10  ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -27.624 -10.159 -37.648 1.00 84.65  ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.870 -5.353  -36.905 1.00 63.84  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.825 -4.757  -37.738 1.00 64.67  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -20.247 -3.476  -37.114 1.00 63.00  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -20.097 -2.462  -37.789 1.00 63.21  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.288 -4.542  -39.189 1.00 68.95  ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.771 -5.810  -39.863 1.00 77.71  ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -21.117 -6.866  -39.682 1.00 80.83  ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.797 -5.750  -40.575 1.00 80.76  ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.955 -3.517  -35.797 1.00 60.92  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -19.305 -2.392  -35.137 1.00 59.14  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.800 -2.484  -35.463 1.00 58.24  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -17.333 -3.534  -35.906 1.00 58.35  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.515 -2.488  -33.635 1.00 58.93  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -17.029 -1.404  -35.247 1.00 58.03  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.577 -1.432  -35.487 1.00 58.56  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.941 -2.452  -34.517 1.00 57.06  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -15.282 -2.438  -33.343 1.00 55.06  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.977 -0.037  -35.243 1.00 62.98  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -13.478 0.032   -35.491 1.00 70.82  ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -12.753 1.019   -34.592 1.00 80.41  ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -13.407 1.967   -34.099 1.00 82.49  ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -11.531 0.842   -34.380 1.00 83.49  ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -14.123 -3.388  -35.029 1.00 57.24  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.510 -4.441  -34.197 1.00 57.19  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -12.023 -4.158  -33.990 1.00 56.45  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -11.280 -4.147  -34.978 1.00 57.19  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.675 -5.853  -34.834 1.00 58.82  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -13.275 -6.936  -33.850 1.00 59.22  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -15.097 -6.085  -35.333 1.00 60.09  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.562 -3.977  -32.715 1.00 55.23  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -10.144 -3.701  -32.454 1.00 54.68  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.708  -4.094  -31.021 1.00 53.44  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.519 -4.583  -30.262 1.00 52.68  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.804  -2.232  -32.804 1.00 56.65  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.376  -2.148  -32.882 1.00 57.97  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.357 -1.252  -31.783 1.00 56.59  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.433  -3.918  -30.685 1.00 53.23  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.914  -4.246  -29.371 1.00 53.28  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.378  -5.657  -29.344 1.00 53.79  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.903  -6.534  -30.035 1.00 54.83  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.331  -5.882  -28.556 1.00 52.92  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.776  -7.210  -28.404 1.00 52.84  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -6.367  -7.913  -27.150 1.00 50.97  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -7.287  -7.375  -26.512 1.00 49.67  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -4.240  -7.162  -28.452 1.00 56.28  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.642  -6.359  -27.331 1.00 61.69  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -4.082  -5.241  -27.021 1.00 62.99  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.605  -6.901  -26.711 1.00 63.63  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.874  -9.115  -26.794 1.00 49.62  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.404  -9.900  -25.662 1.00 48.94  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -5.259  -10.368 -24.736 1.00 48.87  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.929  -11.557 -24.682 1.00 48.68  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -7.171  -11.114 -26.191 1.00 49.14  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.888  -10.824 -27.382 1.00 50.14  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.623  -9.431  -24.015 1.00 48.02  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.455  -9.814  -23.210 1.00 47.77  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.795  -10.604 -21.963 1.00 46.61  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.794  -10.305 -21.303 1.00 46.10  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.808  -8.468  -22.873 1.00 49.23  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.981  -7.495  -22.829 1.00 49.63  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.888  -7.973  -23.951 1.00 47.79  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.955  -11.581 -21.622 1.00 46.32  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -3.118  -12.365 -20.398 1.00 47.29  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -2.087  -11.831 -19.391 1.00 47.13  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.888  -11.989 -19.594 1.00 46.84  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.920  -13.870 -20.666 1.00 49.88  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -4.087  -14.502 -21.451 1.00 54.39  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.826  -15.990 -21.701 1.00 60.25  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.669  -16.552 -22.765 1.00 64.22  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.785  -17.245 -22.550 1.00 66.17  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -6.209  -17.469 -21.310 1.00 67.33  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -6.485  -17.723 -23.574 1.00 63.45  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.555  -11.133 -18.345 1.00 46.75  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.653  -10.477 -17.406 1.00 46.53  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.815  -10.948 -15.985 1.00 46.41  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.939  -11.094 -15.518 1.00 46.57  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.915  -8.959  -17.446 1.00 46.58  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.861  -8.299  -18.816 1.00 48.23  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.699  -7.027  -18.846 1.00 48.29  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.414  -8.089  -19.271 1.00 49.45  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.695  -11.115 -15.268 1.00 45.87  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.725  -11.480 -13.859 1.00 46.08  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.903  -10.170 -13.099 1.00 44.66  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? -0.068  -9.281  -13.246 1.00 44.80  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.602   -12.139 -13.442 1.00 49.26  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 0.760   -13.590 -13.871 1.00 57.58  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.080   -14.003 -14.824 1.00 59.51  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 1.569   -14.313 -13.244 1.00 61.90  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -2.000  -10.017 -12.326 1.00 42.94  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -2.244  -8.767  -11.607 1.00 41.41  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.596  -8.982  -10.119 1.00 40.36  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.997  -10.079 -9.705  1.00 40.60  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.310  -7.857  -12.314 1.00 41.73  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -3.048  -7.684  -13.806 1.00 42.35  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.722  -8.353  -12.063 1.00 41.75  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.415  -7.926  -9.318  1.00 38.84  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.747  -7.893  -7.897  1.00 38.38  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.742  -6.742  -7.679  1.00 37.50  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.675  -5.735  -8.379  1.00 38.02  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.490  -7.683  -7.051  1.00 38.83  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.701  -6.915  -6.772  1.00 35.92  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.711  -5.898  -6.481  1.00 35.02  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.534  -5.522  -4.993  1.00 35.28  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.637  -6.408  -4.135  1.00 35.75  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -7.109  -6.502  -6.719  1.00 34.43  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.296  -5.654  -6.293  1.00 35.48  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.343  -4.315  -7.039  1.00 34.67  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.604  -6.418  -6.448  1.00 36.92  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.215  -4.252  -4.686  1.00 34.73  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -5.040  -3.852  -3.283  1.00 35.52  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.368  -3.401  -2.625  1.00 34.70  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.405  -3.325  -3.294  1.00 34.86  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.899  -2.822  -3.080  1.00 37.30  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.099  -1.443  -3.686  1.00 39.43  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.271  -1.083  -4.004  1.00 37.90  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.090  -0.705  -3.817  1.00 40.89  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.321  -3.124  -1.305  1.00 34.55  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.476  -2.707  -0.537  1.00 34.75  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -8.063  -1.380  -1.021  1.00 34.99  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.266  -1.180  -0.886  1.00 35.61  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -7.114  -2.672  0.960   1.00 36.83  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.281  -2.365  1.870   1.00 41.88  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.898  -2.543  3.322   1.00 47.76  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.610  -1.519  3.981   1.00 48.18  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.846  -3.705  3.790   1.00 49.14  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.264  -0.529  -1.703  1.00 33.97  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.789  0.734   -2.238  1.00 34.23  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.454  0.590   -3.634  1.00 32.89  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.867  1.596   -4.220  1.00 33.38  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.677  1.772   -2.316  1.00 36.57  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.202  2.048   -1.011  1.00 42.16  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.569  -0.634  -4.143  1.00 30.91  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.198  -0.867  -5.446  1.00 31.48  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.294  -0.582  -6.631  1.00 32.30  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.776  -0.434  -7.760  1.00 32.91  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.983  -0.550  -6.401  1.00 32.18  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -6.030  -0.314  -7.485  1.00 34.23  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.387  -1.619  -7.955  1.00 35.35  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.881  -2.406  -7.150  1.00 36.12  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.956  0.698   -7.054  1.00 37.13  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.529  2.073   -6.782  1.00 44.68  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.452  2.490   -7.520  1.00 46.85  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -5.074  2.723   -5.827  1.00 48.55  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.429  -1.856  -9.270  1.00 35.10  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.777  -3.001  -9.874  1.00 35.53  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.310  -2.657  -10.154 1.00 38.01  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.990  -1.526  -10.530 1.00 38.04  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.461  -3.374  -11.208 1.00 33.87  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.770  -4.106  -11.059 1.00 32.51  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.798  -5.442  -10.685 1.00 33.04  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.977  -3.467  -11.309 1.00 32.45  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -8.008  -6.119  -10.562 1.00 33.36  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -9.181  -4.153  -11.209 1.00 32.58  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -9.194  -5.472  -10.832 1.00 32.50  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.431  -3.646  -10.032 1.00 39.73  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -1.017  -3.490  -10.377 1.00 41.77  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.500  -4.783  -11.025 1.00 44.23  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -1.034  -5.859  -10.753 1.00 43.72  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? -0.176  -3.161  -9.146  1.00 42.36  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.258  -4.202  -8.184  1.00 44.54  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.562   -4.685  -11.849 1.00 46.47  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.146   -5.861  -12.501 1.00 49.34  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.036   -6.645  -11.544 1.00 52.57  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 2.843   -6.048  -10.831 1.00 52.80  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.012   -5.431  -13.691 1.00 49.97  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.291   -4.790  -14.868 1.00 52.14  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.294   -4.382  -15.935 1.00 53.44  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.289   -5.747  -15.477 1.00 52.46  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 1.936   -7.976  -11.559 1.00 54.64  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 2.811   -8.815  -10.741 1.00 57.56  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 3.901   -9.327  -11.670 1.00 60.69  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.588   -9.858  -12.738 1.00 60.81  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.058   -10.003 -10.098 1.00 58.34  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.019   -10.894 -9.307  1.00 59.16  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 0.912   -9.517  -9.221  1.00 58.75  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.170   -9.135  -11.306 1.00 63.20  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.279   -9.623  -12.141 1.00 65.78  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.210   -10.545 -11.354 1.00 67.15  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.221   -10.526 -10.119 1.00 68.04  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.066   -8.453  -12.759 1.00 69.24  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.190   -7.423  -13.465 1.00 75.03  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 5.962   -7.693  -14.938 1.00 83.05  ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 6.764   -8.450  -15.535 1.00 84.90  ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 4.991   -7.138  -15.501 1.00 85.28  ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -36.737 13.278  -12.161 1.00 53.50  ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.595 13.054  -13.041 1.00 53.97  ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.791 11.986  -14.108 1.00 53.94  ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.784 11.245  -14.075 1.00 54.58  ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.852 11.906  -15.080 1.00 52.60  ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.954 10.876  -16.116 1.00 51.36  ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -34.517 9.519   -15.571 1.00 49.65  ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -33.381 9.339   -15.122 1.00 49.83  ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -34.224 11.223  -17.426 1.00 53.43  ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -34.560 10.209  -18.510 1.00 56.84  ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -33.991 10.506  -19.881 1.00 61.92  ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -33.012 11.286  -19.949 1.00 62.50  ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -34.553 10.004  -20.887 1.00 62.80  ? 17  GLU   B OE2 1 
ATOM   325  N  N   A THR   B 2 9   ? -35.441 8.568   -15.582 0.50 48.61  ? 18  THR   B N   1 
ATOM   326  N  N   B THR   B 2 9   ? -35.448 8.567   -15.575 0.50 48.37  ? 18  THR   B N   1 
ATOM   327  C  CA  A THR   B 2 9   ? -35.181 7.234   -15.047 0.50 48.08  ? 18  THR   B CA  1 
ATOM   328  C  CA  B THR   B 2 9   ? -35.216 7.223   -15.058 0.50 47.60  ? 18  THR   B CA  1 
ATOM   329  C  C   A THR   B 2 9   ? -35.241 6.141   -16.119 0.50 46.73  ? 18  THR   B C   1 
ATOM   330  C  C   B THR   B 2 9   ? -35.220 6.144   -16.126 0.50 46.51  ? 18  THR   B C   1 
ATOM   331  O  O   A THR   B 2 9   ? -35.147 4.966   -15.779 0.50 47.19  ? 18  THR   B O   1 
ATOM   332  O  O   B THR   B 2 9   ? -35.090 4.972   -15.788 0.50 46.97  ? 18  THR   B O   1 
ATOM   333  C  CB  A THR   B 2 9   ? -36.093 6.904   -13.830 0.50 49.98  ? 18  THR   B CB  1 
ATOM   334  C  CB  B THR   B 2 9   ? -36.294 6.895   -14.034 0.50 48.83  ? 18  THR   B CB  1 
ATOM   335  O  OG1 A THR   B 2 9   ? -36.881 8.034   -13.412 0.50 51.35  ? 18  THR   B OG1 1 
ATOM   336  O  OG1 B THR   B 2 9   ? -37.571 6.975   -14.679 0.50 49.39  ? 18  THR   B OG1 1 
ATOM   337  C  CG2 A THR   B 2 9   ? -35.303 6.358   -12.645 0.50 50.35  ? 18  THR   B CG2 1 
ATOM   338  C  CG2 B THR   B 2 9   ? -36.244 7.823   -12.834 0.50 49.36  ? 18  THR   B CG2 1 
ATOM   339  N  N   . THR   B 2 10  ? -35.369 6.514   -17.417 1.00 45.12  ? 19  THR   B N   1 
ATOM   340  C  CA  . THR   B 2 10  ? -35.390 5.573   -18.533 1.00 42.48  ? 19  THR   B CA  1 
ATOM   341  C  C   . THR   B 2 10  ? -34.063 4.816   -18.550 1.00 39.40  ? 19  THR   B C   1 
ATOM   342  O  O   . THR   B 2 10  ? -33.007 5.411   -18.272 1.00 39.20  ? 19  THR   B O   1 
ATOM   343  C  CB  . THR   B 2 10  ? -35.553 6.364   -19.869 1.00 43.28  ? 19  THR   B CB  1 
ATOM   344  O  OG1 . THR   B 2 10  ? -36.647 7.284   -19.748 1.00 45.10  ? 19  THR   B OG1 1 
ATOM   345  C  CG2 . THR   B 2 10  ? -35.781 5.467   -21.068 1.00 43.89  ? 19  THR   B CG2 1 
ATOM   346  N  N   . ASP   B 2 11  ? -34.124 3.501   -18.772 1.00 37.10  ? 20  ASP   B N   1 
ATOM   347  C  CA  . ASP   B 2 11  ? -32.969 2.632   -18.906 1.00 36.04  ? 20  ASP   B CA  1 
ATOM   348  C  C   . ASP   B 2 11  ? -32.030 3.203   -19.995 1.00 35.02  ? 20  ASP   B C   1 
ATOM   349  O  O   . ASP   B 2 11  ? -32.489 3.892   -20.920 1.00 35.99  ? 20  ASP   B O   1 
ATOM   350  C  CB  . ASP   B 2 11  ? -33.419 1.219   -19.366 1.00 37.93  ? 20  ASP   B CB  1 
ATOM   351  C  CG  . ASP   B 2 11  ? -33.904 0.266   -18.281 1.00 42.59  ? 20  ASP   B CG  1 
ATOM   352  O  OD1 . ASP   B 2 11  ? -34.064 0.710   -17.131 1.00 40.74  ? 20  ASP   B OD1 1 
ATOM   353  O  OD2 . ASP   B 2 11  ? -34.116 -0.944  -18.594 1.00 44.38  ? 20  ASP   B OD2 1 
ATOM   354  N  N   . GLY   B 2 12  ? -30.755 2.927   -19.870 1.00 32.46  ? 21  GLY   B N   1 
ATOM   355  C  CA  . GLY   B 2 12  ? -29.772 3.369   -20.844 1.00 31.59  ? 21  GLY   B CA  1 
ATOM   356  C  C   . GLY   B 2 12  ? -28.460 3.783   -20.222 1.00 30.83  ? 21  GLY   B C   1 
ATOM   357  O  O   . GLY   B 2 12  ? -28.243 3.618   -19.002 1.00 29.52  ? 21  GLY   B O   1 
ATOM   358  N  N   . VAL   B 2 13  ? -27.577 4.316   -21.081 1.00 30.07  ? 22  VAL   B N   1 
ATOM   359  C  CA  . VAL   B 2 13  ? -26.277 4.813   -20.671 1.00 29.74  ? 22  VAL   B CA  1 
ATOM   360  C  C   . VAL   B 2 13  ? -26.322 6.331   -20.502 1.00 29.36  ? 22  VAL   B C   1 
ATOM   361  O  O   . VAL   B 2 13  ? -26.999 7.049   -21.268 1.00 30.18  ? 22  VAL   B O   1 
ATOM   362  C  CB  . VAL   B 2 13  ? -25.178 4.331   -21.640 1.00 30.41  ? 22  VAL   B CB  1 
ATOM   363  C  CG1 . VAL   B 2 13  ? -25.349 4.923   -23.047 1.00 29.69  ? 22  VAL   B CG1 1 
ATOM   364  C  CG2 . VAL   B 2 13  ? -23.784 4.598   -21.094 1.00 31.37  ? 22  VAL   B CG2 1 
ATOM   365  N  N   . TYR   B 2 14  ? -25.661 6.827   -19.433 1.00 27.73  ? 23  TYR   B N   1 
ATOM   366  C  CA  . TYR   B 2 14  ? -25.686 8.247   -19.082 1.00 27.85  ? 23  TYR   B CA  1 
ATOM   367  C  C   . TYR   B 2 14  ? -24.293 8.765   -18.811 1.00 27.89  ? 23  TYR   B C   1 
ATOM   368  O  O   . TYR   B 2 14  ? -23.470 8.061   -18.235 1.00 28.53  ? 23  TYR   B O   1 
ATOM   369  C  CB  . TYR   B 2 14  ? -26.494 8.479   -17.767 1.00 27.92  ? 23  TYR   B CB  1 
ATOM   370  C  CG  . TYR   B 2 14  ? -27.992 8.301   -17.871 1.00 28.64  ? 23  TYR   B CG  1 
ATOM   371  C  CD1 . TYR   B 2 14  ? -28.554 7.051   -18.113 1.00 29.20  ? 23  TYR   B CD1 1 
ATOM   372  C  CD2 . TYR   B 2 14  ? -28.848 9.373   -17.696 1.00 30.03  ? 23  TYR   B CD2 1 
ATOM   373  C  CE1 . TYR   B 2 14  ? -29.931 6.882   -18.200 1.00 29.94  ? 23  TYR   B CE1 1 
ATOM   374  C  CE2 . TYR   B 2 14  ? -30.225 9.220   -17.794 1.00 31.47  ? 23  TYR   B CE2 1 
ATOM   375  C  CZ  . TYR   B 2 14  ? -30.764 7.965   -17.993 1.00 32.71  ? 23  TYR   B CZ  1 
ATOM   376  O  OH  . TYR   B 2 14  ? -32.125 7.825   -18.107 1.00 36.48  ? 23  TYR   B OH  1 
ATOM   377  N  N   . ARG   B 2 15  ? -24.063 10.037  -19.120 1.00 26.87  ? 24  ARG   B N   1 
ATOM   378  C  CA  . ARG   B 2 15  ? -22.815 10.702  -18.763 1.00 27.24  ? 24  ARG   B CA  1 
ATOM   379  C  C   . ARG   B 2 15  ? -22.973 11.204  -17.321 1.00 27.67  ? 24  ARG   B C   1 
ATOM   380  O  O   . ARG   B 2 15  ? -24.055 11.650  -16.933 1.00 26.58  ? 24  ARG   B O   1 
ATOM   381  C  CB  . ARG   B 2 15  ? -22.602 11.967  -19.632 1.00 28.65  ? 24  ARG   B CB  1 
ATOM   382  C  CG  . ARG   B 2 15  ? -22.565 11.704  -21.139 1.00 29.81  ? 24  ARG   B CG  1 
ATOM   383  C  CD  . ARG   B 2 15  ? -22.486 12.997  -21.958 1.00 29.96  ? 24  ARG   B CD  1 
ATOM   384  N  NE  . ARG   B 2 15  ? -22.733 12.697  -23.368 1.00 32.55  ? 24  ARG   B NE  1 
ATOM   385  C  CZ  . ARG   B 2 15  ? -21.802 12.305  -24.235 1.00 35.37  ? 24  ARG   B CZ  1 
ATOM   386  N  NH1 . ARG   B 2 15  ? -20.532 12.210  -23.860 1.00 31.01  ? 24  ARG   B NH1 1 
ATOM   387  N  NH2 . ARG   B 2 15  ? -22.131 12.027  -25.490 1.00 37.71  ? 24  ARG   B NH2 1 
ATOM   388  N  N   . VAL   B 2 16  ? -21.882 11.251  -16.569 1.00 28.22  ? 25  VAL   B N   1 
ATOM   389  C  CA  . VAL   B 2 16  ? -21.857 11.843  -15.242 1.00 28.81  ? 25  VAL   B CA  1 
ATOM   390  C  C   . VAL   B 2 16  ? -21.036 13.124  -15.346 1.00 29.56  ? 25  VAL   B C   1 
ATOM   391  O  O   . VAL   B 2 16  ? -19.858 13.068  -15.702 1.00 29.99  ? 25  VAL   B O   1 
ATOM   392  C  CB  . VAL   B 2 16  ? -21.218 10.886  -14.222 1.00 28.24  ? 25  VAL   B CB  1 
ATOM   393  C  CG1 . VAL   B 2 16  ? -21.116 11.589  -12.870 1.00 28.88  ? 25  VAL   B CG1 1 
ATOM   394  C  CG2 . VAL   B 2 16  ? -22.030 9.595   -14.119 1.00 26.77  ? 25  VAL   B CG2 1 
ATOM   395  N  N   . MET   B 2 17  ? -21.670 14.269  -15.136 1.00 30.57  ? 26  MET   B N   1 
ATOM   396  C  CA  . MET   B 2 17  ? -21.073 15.578  -15.321 1.00 32.04  ? 26  MET   B CA  1 
ATOM   397  C  C   . MET   B 2 17  ? -20.901 16.378  -14.015 1.00 33.54  ? 26  MET   B C   1 
ATOM   398  O  O   . MET   B 2 17  ? -21.649 16.177  -13.050 1.00 32.39  ? 26  MET   B O   1 
ATOM   399  C  CB  . MET   B 2 17  ? -21.995 16.401  -16.253 1.00 31.57  ? 26  MET   B CB  1 
ATOM   400  C  CG  . MET   B 2 17  ? -22.439 15.712  -17.540 1.00 33.98  ? 26  MET   B CG  1 
ATOM   401  S  SD  . MET   B 2 17  ? -21.086 15.467  -18.699 1.00 33.13  ? 26  MET   B SD  1 
ATOM   402  C  CE  . MET   B 2 17  ? -20.550 17.192  -18.955 1.00 30.55  ? 26  MET   B CE  1 
ATOM   403  N  N   . THR   B 2 18  ? -20.000 17.382  -14.029 1.00 35.75  ? 27  THR   B N   1 
ATOM   404  C  CA  . THR   B 2 18  ? -19.856 18.320  -12.911 1.00 38.29  ? 27  THR   B CA  1 
ATOM   405  C  C   . THR   B 2 18  ? -19.651 19.742  -13.419 1.00 40.06  ? 27  THR   B C   1 
ATOM   406  O  O   . THR   B 2 18  ? -18.989 19.948  -14.437 1.00 38.31  ? 27  THR   B O   1 
ATOM   407  C  CB  . THR   B 2 18  ? -18.736 17.914  -11.943 1.00 40.62  ? 27  THR   B CB  1 
ATOM   408  O  OG1 . THR   B 2 18  ? -18.692 18.886  -10.888 1.00 43.37  ? 27  THR   B OG1 1 
ATOM   409  C  CG2 . THR   B 2 18  ? -17.371 17.822  -12.618 1.00 40.23  ? 27  THR   B CG2 1 
ATOM   410  N  N   . ARG   B 2 19  ? -20.197 20.734  -12.698 1.00 42.88  ? 28  ARG   B N   1 
ATOM   411  C  CA  . ARG   B 2 19  ? -19.948 22.132  -13.028 1.00 46.39  ? 28  ARG   B CA  1 
ATOM   412  C  C   . ARG   B 2 19  ? -18.977 22.795  -12.003 1.00 48.58  ? 28  ARG   B C   1 
ATOM   413  O  O   . ARG   B 2 19  ? -18.817 24.014  -12.016 1.00 48.78  ? 28  ARG   B O   1 
ATOM   414  C  CB  . ARG   B 2 19  ? -21.261 22.934  -13.165 1.00 49.36  ? 28  ARG   B CB  1 
ATOM   415  C  CG  . ARG   B 2 19  ? -21.965 22.717  -14.502 1.00 54.52  ? 28  ARG   B CG  1 
ATOM   416  C  CD  . ARG   B 2 19  ? -23.276 23.473  -14.586 1.00 60.35  ? 28  ARG   B CD  1 
ATOM   417  N  NE  . ARG   B 2 19  ? -24.029 23.139  -15.798 1.00 65.68  ? 28  ARG   B NE  1 
ATOM   418  C  CZ  . ARG   B 2 19  ? -25.202 22.508  -15.803 1.00 70.17  ? 28  ARG   B CZ  1 
ATOM   419  N  NH1 . ARG   B 2 19  ? -25.779 22.148  -14.658 1.00 70.46  ? 28  ARG   B NH1 1 
ATOM   420  N  NH2 . ARG   B 2 19  ? -25.812 22.238  -16.952 1.00 70.72  ? 28  ARG   B NH2 1 
ATOM   421  N  N   . ARG   B 2 20  ? -18.320 21.998  -11.145 1.00 50.59  ? 29  ARG   B N   1 
ATOM   422  C  CA  . ARG   B 2 20  ? -17.390 22.498  -10.132 1.00 53.21  ? 29  ARG   B CA  1 
ATOM   423  C  C   . ARG   B 2 20  ? -16.130 23.064  -10.769 1.00 53.90  ? 29  ARG   B C   1 
ATOM   424  O  O   . ARG   B 2 20  ? -15.634 24.099  -10.329 1.00 54.48  ? 29  ARG   B O   1 
ATOM   425  C  CB  . ARG   B 2 20  ? -17.019 21.379  -9.145  1.00 56.57  ? 29  ARG   B CB  1 
ATOM   426  C  CG  . ARG   B 2 20  ? -16.294 21.889  -7.912  1.00 63.57  ? 29  ARG   B CG  1 
ATOM   427  C  CD  . ARG   B 2 20  ? -15.953 20.770  -6.939  1.00 70.24  ? 29  ARG   B CD  1 
ATOM   428  N  NE  . ARG   B 2 20  ? -15.135 19.721  -7.553  1.00 75.49  ? 29  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   B 2 20  ? -13.811 19.776  -7.679  1.00 79.51  ? 29  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   B 2 20  ? -13.140 20.842  -7.257  1.00 79.66  ? 29  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   B 2 20  ? -13.151 18.773  -8.245  1.00 79.87  ? 29  ARG   B NH2 1 
ATOM   432  N  N   . LEU   B 2 21  ? -15.630 22.402  -11.819 1.00 53.30  ? 30  LEU   B N   1 
ATOM   433  C  CA  . LEU   B 2 21  ? -14.422 22.812  -12.524 1.00 53.33  ? 30  LEU   B CA  1 
ATOM   434  C  C   . LEU   B 2 21  ? -14.754 23.849  -13.652 1.00 51.84  ? 30  LEU   B C   1 
ATOM   435  O  O   . LEU   B 2 21  ? -15.809 24.488  -13.606 1.00 51.39  ? 30  LEU   B O   1 
ATOM   436  C  CB  . LEU   B 2 21  ? -13.743 21.522  -13.073 1.00 54.43  ? 30  LEU   B CB  1 
ATOM   437  C  CG  . LEU   B 2 21  ? -12.599 20.830  -12.281 1.00 57.01  ? 30  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   B 2 21  ? -12.613 21.150  -10.788 1.00 58.17  ? 30  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   B 2 21  ? -12.650 19.322  -12.471 1.00 57.80  ? 30  LEU   B CD2 1 
ATOM   440  N  N   . LEU   B 2 22  ? -13.851 24.039  -14.630 1.00 50.73  ? 31  LEU   B N   1 
ATOM   441  C  CA  . LEU   B 2 22  ? -14.066 24.965  -15.733 1.00 50.15  ? 31  LEU   B CA  1 
ATOM   442  C  C   . LEU   B 2 22  ? -15.161 24.396  -16.645 1.00 48.94  ? 31  LEU   B C   1 
ATOM   443  O  O   . LEU   B 2 22  ? -15.112 23.202  -16.972 1.00 49.44  ? 31  LEU   B O   1 
ATOM   444  C  CB  . LEU   B 2 22  ? -12.749 25.111  -16.500 1.00 50.46  ? 31  LEU   B CB  1 
ATOM   445  C  CG  . LEU   B 2 22  ? -12.658 26.238  -17.494 1.00 51.44  ? 31  LEU   B CG  1 
ATOM   446  C  CD1 . LEU   B 2 22  ? -12.712 27.602  -16.806 1.00 51.33  ? 31  LEU   B CD1 1 
ATOM   447  C  CD2 . LEU   B 2 22  ? -11.397 26.096  -18.331 1.00 52.05  ? 31  LEU   B CD2 1 
ATOM   448  N  N   . GLY   B 2 23  ? -16.161 25.218  -16.993 1.00 46.47  ? 32  GLY   B N   1 
ATOM   449  C  CA  . GLY   B 2 23  ? -17.294 24.791  -17.812 1.00 45.17  ? 32  GLY   B CA  1 
ATOM   450  C  C   . GLY   B 2 23  ? -18.021 23.575  -17.233 1.00 43.48  ? 32  GLY   B C   1 
ATOM   451  O  O   . GLY   B 2 23  ? -18.145 23.445  -16.009 1.00 42.60  ? 32  GLY   B O   1 
ATOM   452  N  N   . SER   B 2 24  ? -18.506 22.680  -18.106 1.00 42.38  ? 33  SER   B N   1 
ATOM   453  C  CA  . SER   B 2 24  ? -19.167 21.446  -17.673 1.00 41.89  ? 33  SER   B CA  1 
ATOM   454  C  C   . SER   B 2 24  ? -18.236 20.330  -18.064 1.00 40.03  ? 33  SER   B C   1 
ATOM   455  O  O   . SER   B 2 24  ? -17.882 20.196  -19.235 1.00 40.75  ? 33  SER   B O   1 
ATOM   456  C  CB  . SER   B 2 24  ? -20.526 21.280  -18.348 1.00 44.07  ? 33  SER   B CB  1 
ATOM   457  O  OG  . SER   B 2 24  ? -21.327 22.437  -18.132 1.00 46.27  ? 33  SER   B OG  1 
ATOM   458  N  N   . THR   B 2 25  ? -17.776 19.570  -17.080 1.00 38.06  ? 34  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 25  ? -16.785 18.515  -17.301 1.00 36.45  ? 34  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 25  ? -17.370 17.135  -17.082 1.00 34.55  ? 34  THR   B C   1 
ATOM   461  O  O   . THR   B 2 25  ? -18.066 16.909  -16.088 1.00 33.49  ? 34  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 25  ? -15.592 18.707  -16.324 1.00 38.46  ? 34  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 25  ? -15.049 20.021  -16.477 1.00 40.82  ? 34  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 25  ? -14.491 17.657  -16.500 1.00 38.64  ? 34  THR   B CG2 1 
ATOM   465  N  N   . GLN   B 2 26  ? -17.089 16.219  -18.002 1.00 32.76  ? 35  GLN   B N   1 
ATOM   466  C  CA  . GLN   B 2 26  ? -17.538 14.841  -17.850 1.00 31.51  ? 35  GLN   B CA  1 
ATOM   467  C  C   . GLN   B 2 26  ? -16.535 14.004  -17.008 1.00 32.02  ? 35  GLN   B C   1 
ATOM   468  O  O   . GLN   B 2 26  ? -15.404 13.723  -17.453 1.00 32.65  ? 35  GLN   B O   1 
ATOM   469  C  CB  . GLN   B 2 26  ? -17.817 14.167  -19.202 1.00 29.25  ? 35  GLN   B CB  1 
ATOM   470  C  CG  . GLN   B 2 26  ? -18.279 12.715  -19.052 1.00 27.14  ? 35  GLN   B CG  1 
ATOM   471  C  CD  . GLN   B 2 26  ? -18.583 12.066  -20.373 1.00 31.25  ? 35  GLN   B CD  1 
ATOM   472  O  OE1 . GLN   B 2 26  ? -19.213 12.671  -21.244 1.00 31.03  ? 35  GLN   B OE1 1 
ATOM   473  N  NE2 . GLN   B 2 26  ? -18.193 10.792  -20.534 1.00 28.46  ? 35  GLN   B NE2 1 
ATOM   474  N  N   . VAL   B 2 27  ? -16.960 13.608  -15.813 1.00 31.74  ? 36  VAL   B N   1 
ATOM   475  C  CA  . VAL   B 2 27  ? -16.092 12.811  -14.941 1.00 31.79  ? 36  VAL   B CA  1 
ATOM   476  C  C   . VAL   B 2 27  ? -16.274 11.304  -15.107 1.00 30.08  ? 36  VAL   B C   1 
ATOM   477  O  O   . VAL   B 2 27  ? -15.410 10.535  -14.665 1.00 29.84  ? 36  VAL   B O   1 
ATOM   478  C  CB  . VAL   B 2 27  ? -16.222 13.233  -13.470 1.00 32.46  ? 36  VAL   B CB  1 
ATOM   479  C  CG1 . VAL   B 2 27  ? -15.726 14.669  -13.295 1.00 34.22  ? 36  VAL   B CG1 1 
ATOM   480  C  CG2 . VAL   B 2 27  ? -17.658 13.093  -13.000 1.00 32.78  ? 36  VAL   B CG2 1 
ATOM   481  N  N   . GLY   B 2 28  ? -17.370 10.880  -15.735 1.00 28.08  ? 37  GLY   B N   1 
ATOM   482  C  CA  . GLY   B 2 28  ? -17.580 9.463   -15.973 1.00 26.69  ? 37  GLY   B CA  1 
ATOM   483  C  C   . GLY   B 2 28  ? -18.882 9.148   -16.658 1.00 27.00  ? 37  GLY   B C   1 
ATOM   484  O  O   . GLY   B 2 28  ? -19.502 10.038  -17.240 1.00 27.94  ? 37  GLY   B O   1 
ATOM   485  N  N   . VAL   B 2 29  ? -19.304 7.888   -16.575 1.00 25.54  ? 38  VAL   B N   1 
ATOM   486  C  CA  . VAL   B 2 29  ? -20.475 7.321   -17.246 1.00 26.28  ? 38  VAL   B CA  1 
ATOM   487  C  C   . VAL   B 2 29  ? -21.124 6.245   -16.337 1.00 26.22  ? 38  VAL   B C   1 
ATOM   488  O  O   . VAL   B 2 29  ? -20.480 5.728   -15.409 1.00 25.96  ? 38  VAL   B O   1 
ATOM   489  C  CB  . VAL   B 2 29  ? -19.955 6.634   -18.564 1.00 27.20  ? 38  VAL   B CB  1 
ATOM   490  C  CG1 . VAL   B 2 29  ? -21.082 5.987   -19.360 1.00 27.03  ? 38  VAL   B CG1 1 
ATOM   491  C  CG2 . VAL   B 2 29  ? -19.234 7.652   -19.447 1.00 27.56  ? 38  VAL   B CG2 1 
ATOM   492  N  N   . GLY   B 2 30  ? -22.393 5.938   -16.579 1.00 25.96  ? 39  GLY   B N   1 
ATOM   493  C  CA  . GLY   B 2 30  ? -23.062 4.885   -15.825 1.00 26.71  ? 39  GLY   B CA  1 
ATOM   494  C  C   . GLY   B 2 30  ? -24.274 4.326   -16.527 1.00 27.59  ? 39  GLY   B C   1 
ATOM   495  O  O   . GLY   B 2 30  ? -24.676 4.808   -17.601 1.00 28.26  ? 39  GLY   B O   1 
ATOM   496  N  N   . VAL   B 2 31  ? -24.842 3.286   -15.929 1.00 25.32  ? 40  VAL   B N   1 
ATOM   497  C  CA  . VAL   B 2 31  ? -25.962 2.531   -16.461 1.00 26.09  ? 40  VAL   B CA  1 
ATOM   498  C  C   . VAL   B 2 31  ? -27.197 2.637   -15.598 1.00 26.20  ? 40  VAL   B C   1 
ATOM   499  O  O   . VAL   B 2 31  ? -27.147 2.278   -14.402 1.00 25.44  ? 40  VAL   B O   1 
ATOM   500  C  CB  . VAL   B 2 31  ? -25.524 1.034   -16.543 1.00 27.57  ? 40  VAL   B CB  1 
ATOM   501  C  CG1 . VAL   B 2 31  ? -26.699 0.131   -16.935 1.00 27.63  ? 40  VAL   B CG1 1 
ATOM   502  C  CG2 . VAL   B 2 31  ? -24.355 0.874   -17.506 1.00 28.44  ? 40  VAL   B CG2 1 
ATOM   503  N  N   . MET   B 2 32  ? -28.348 2.991   -16.208 1.00 25.51  ? 41  MET   B N   1 
ATOM   504  C  CA  . MET   B 2 32  ? -29.624 3.004   -15.500 1.00 26.77  ? 41  MET   B CA  1 
ATOM   505  C  C   . MET   B 2 32  ? -30.324 1.693   -15.940 1.00 28.21  ? 41  MET   B C   1 
ATOM   506  O  O   . MET   B 2 32  ? -30.456 1.403   -17.153 1.00 28.18  ? 41  MET   B O   1 
ATOM   507  C  CB  . MET   B 2 32  ? -30.447 4.252   -15.899 1.00 26.93  ? 41  MET   B CB  1 
ATOM   508  C  CG  . MET   B 2 32  ? -31.710 4.437   -15.112 1.00 29.67  ? 41  MET   B CG  1 
ATOM   509  S  SD  . MET   B 2 32  ? -31.267 5.030   -13.435 1.00 31.54  ? 41  MET   B SD  1 
ATOM   510  C  CE  . MET   B 2 32  ? -30.822 6.684   -13.794 1.00 29.89  ? 41  MET   B CE  1 
ATOM   511  N  N   . GLN   B 2 33  ? -30.703 0.877   -14.962 1.00 27.19  ? 42  GLN   B N   1 
ATOM   512  C  CA  . GLN   B 2 33  ? -31.371 -0.385  -15.224 1.00 28.80  ? 42  GLN   B CA  1 
ATOM   513  C  C   . GLN   B 2 33  ? -32.245 -0.724  -14.036 1.00 29.78  ? 42  GLN   B C   1 
ATOM   514  O  O   . GLN   B 2 33  ? -31.801 -0.613  -12.874 1.00 29.61  ? 42  GLN   B O   1 
ATOM   515  C  CB  . GLN   B 2 33  ? -30.390 -1.527  -15.535 1.00 31.05  ? 42  GLN   B CB  1 
ATOM   516  C  CG  . GLN   B 2 33  ? -31.134 -2.820  -15.870 1.00 35.46  ? 42  GLN   B CG  1 
ATOM   517  C  CD  . GLN   B 2 33  ? -30.237 -3.928  -16.334 1.00 39.07  ? 42  GLN   B CD  1 
ATOM   518  O  OE1 . GLN   B 2 33  ? -30.276 -5.039  -15.800 1.00 44.06  ? 42  GLN   B OE1 1 
ATOM   519  N  NE2 . GLN   B 2 33  ? -29.391 -3.642  -17.323 1.00 35.81  ? 42  GLN   B NE2 1 
ATOM   520  N  N   . GLU   B 2 34  ? -33.516 -1.043  -14.310 1.00 30.71  ? 43  GLU   B N   1 
ATOM   521  C  CA  . GLU   B 2 34  ? -34.503 -1.405  -13.273 1.00 32.26  ? 43  GLU   B CA  1 
ATOM   522  C  C   . GLU   B 2 34  ? -34.624 -0.368  -12.127 1.00 33.70  ? 43  GLU   B C   1 
ATOM   523  O  O   . GLU   B 2 34  ? -34.723 -0.745  -10.948 1.00 35.20  ? 43  GLU   B O   1 
ATOM   524  C  CB  . GLU   B 2 34  ? -34.191 -2.793  -12.697 1.00 34.09  ? 43  GLU   B CB  1 
ATOM   525  C  CG  . GLU   B 2 34  ? -34.227 -3.927  -13.709 1.00 39.27  ? 43  GLU   B CG  1 
ATOM   526  C  CD  . GLU   B 2 34  ? -33.512 -5.182  -13.251 1.00 47.87  ? 43  GLU   B CD  1 
ATOM   527  O  OE1 . GLU   B 2 34  ? -33.816 -5.671  -12.141 1.00 50.04  ? 43  GLU   B OE1 1 
ATOM   528  O  OE2 . GLU   B 2 34  ? -32.634 -5.671  -13.994 1.00 52.39  ? 43  GLU   B OE2 1 
ATOM   529  N  N   . GLY   B 2 35  ? -34.541 0.914   -12.469 1.00 32.64  ? 44  GLY   B N   1 
ATOM   530  C  CA  . GLY   B 2 35  ? -34.651 2.004   -11.512 1.00 32.13  ? 44  GLY   B CA  1 
ATOM   531  C  C   . GLY   B 2 35  ? -33.394 2.320   -10.714 1.00 30.64  ? 44  GLY   B C   1 
ATOM   532  O  O   . GLY   B 2 35  ? -33.442 3.154   -9.801  1.00 31.18  ? 44  GLY   B O   1 
ATOM   533  N  N   . VAL   B 2 36  ? -32.261 1.660   -11.033 1.00 27.98  ? 45  VAL   B N   1 
ATOM   534  C  CA  . VAL   B 2 36  ? -31.004 1.848   -10.284 1.00 26.79  ? 45  VAL   B CA  1 
ATOM   535  C  C   . VAL   B 2 36  ? -29.886 2.377   -11.215 1.00 26.07  ? 45  VAL   B C   1 
ATOM   536  O  O   . VAL   B 2 36  ? -29.755 1.910   -12.360 1.00 25.14  ? 45  VAL   B O   1 
ATOM   537  C  CB  . VAL   B 2 36  ? -30.609 0.467   -9.660  1.00 26.87  ? 45  VAL   B CB  1 
ATOM   538  C  CG1 . VAL   B 2 36  ? -29.213 0.510   -9.037  1.00 26.14  ? 45  VAL   B CG1 1 
ATOM   539  C  CG2 . VAL   B 2 36  ? -31.653 0.033   -8.629  1.00 27.04  ? 45  VAL   B CG2 1 
ATOM   540  N  N   . PHE   B 2 37  ? -29.100 3.351   -10.725 1.00 25.37  ? 46  PHE   B N   1 
ATOM   541  C  CA  . PHE   B 2 37  ? -27.995 3.911   -11.488 1.00 24.79  ? 46  PHE   B CA  1 
ATOM   542  C  C   . PHE   B 2 37  ? -26.690 3.267   -11.000 1.00 24.11  ? 46  PHE   B C   1 
ATOM   543  O  O   . PHE   B 2 37  ? -26.408 3.254   -9.802  1.00 23.61  ? 46  PHE   B O   1 
ATOM   544  C  CB  . PHE   B 2 37  ? -27.929 5.439   -11.342 1.00 24.65  ? 46  PHE   B CB  1 
ATOM   545  C  CG  . PHE   B 2 37  ? -26.949 6.036   -12.330 1.00 24.82  ? 46  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   B 2 37  ? -27.134 5.880   -13.703 1.00 25.99  ? 46  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   B 2 37  ? -25.777 6.630   -11.888 1.00 25.33  ? 46  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   B 2 37  ? -26.215 6.410   -14.608 1.00 26.79  ? 46  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   B 2 37  ? -24.851 7.128   -12.788 1.00 26.48  ? 46  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   B 2 37  ? -25.076 7.029   -14.139 1.00 26.80  ? 46  PHE   B CZ  1 
ATOM   551  N  N   . HIS   B 2 38  ? -25.921 2.733   -11.935 1.00 22.82  ? 47  HIS   B N   1 
ATOM   552  C  CA  . HIS   B 2 38  ? -24.713 1.973   -11.633 1.00 23.53  ? 47  HIS   B CA  1 
ATOM   553  C  C   . HIS   B 2 38  ? -23.515 2.703   -12.239 1.00 24.12  ? 47  HIS   B C   1 
ATOM   554  O  O   . HIS   B 2 38  ? -23.512 2.999   -13.441 1.00 24.99  ? 47  HIS   B O   1 
ATOM   555  C  CB  . HIS   B 2 38  ? -24.792 0.581   -12.306 1.00 23.42  ? 47  HIS   B CB  1 
ATOM   556  C  CG  . HIS   B 2 38  ? -26.012 -0.226  -11.938 1.00 25.23  ? 47  HIS   B CG  1 
ATOM   557  N  ND1 . HIS   B 2 38  ? -27.266 0.037   -12.513 1.00 25.37  ? 47  HIS   B ND1 1 
ATOM   558  C  CD2 . HIS   B 2 38  ? -26.130 -1.289  -11.105 1.00 25.12  ? 47  HIS   B CD2 1 
ATOM   559  C  CE1 . HIS   B 2 38  ? -28.090 -0.863  -12.000 1.00 25.28  ? 47  HIS   B CE1 1 
ATOM   560  N  NE2 . HIS   B 2 38  ? -27.451 -1.690  -11.155 1.00 25.74  ? 47  HIS   B NE2 1 
ATOM   561  N  N   . THR   B 2 39  ? -22.455 2.910   -11.422 1.00 23.51  ? 48  THR   B N   1 
ATOM   562  C  CA  . THR   B 2 39  ? -21.232 3.558   -11.938 1.00 23.55  ? 48  THR   B CA  1 
ATOM   563  C  C   . THR   B 2 39  ? -20.018 3.057   -11.130 1.00 24.51  ? 48  THR   B C   1 
ATOM   564  O  O   . THR   B 2 39  ? -20.169 2.166   -10.273 1.00 24.45  ? 48  THR   B O   1 
ATOM   565  C  CB  . THR   B 2 39  ? -21.384 5.113   -12.016 1.00 23.84  ? 48  THR   B CB  1 
ATOM   566  O  OG1 . THR   B 2 39  ? -20.243 5.657   -12.720 1.00 23.98  ? 48  THR   B OG1 1 
ATOM   567  C  CG2 . THR   B 2 39  ? -21.513 5.769   -10.627 1.00 24.58  ? 48  THR   B CG2 1 
ATOM   568  N  N   . MET   B 2 40  ? -18.821 3.581   -11.429 1.00 24.08  ? 49  MET   B N   1 
ATOM   569  C  CA  . MET   B 2 40  ? -17.639 3.187   -10.669 1.00 23.48  ? 49  MET   B CA  1 
ATOM   570  C  C   . MET   B 2 40  ? -17.454 4.144   -9.504  1.00 23.70  ? 49  MET   B C   1 
ATOM   571  O  O   . MET   B 2 40  ? -17.731 5.365   -9.594  1.00 23.84  ? 49  MET   B O   1 
ATOM   572  C  CB  . MET   B 2 40  ? -16.395 3.128   -11.578 1.00 24.76  ? 49  MET   B CB  1 
ATOM   573  C  CG  . MET   B 2 40  ? -16.630 2.301   -12.868 1.00 25.89  ? 49  MET   B CG  1 
ATOM   574  S  SD  . MET   B 2 40  ? -15.121 1.654   -13.580 1.00 30.74  ? 49  MET   B SD  1 
ATOM   575  C  CE  . MET   B 2 40  ? -14.821 0.209   -12.532 1.00 27.35  ? 49  MET   B CE  1 
ATOM   576  N  N   . TRP   B 2 41  ? -16.987 3.615   -8.359  1.00 23.74  ? 50  TRP   B N   1 
ATOM   577  C  CA  A TRP   B 2 41  ? -16.809 4.457   -7.167  0.50 24.52  ? 50  TRP   B CA  1 
ATOM   578  C  CA  B TRP   B 2 41  ? -16.786 4.441   -7.165  0.50 23.70  ? 50  TRP   B CA  1 
ATOM   579  C  C   . TRP   B 2 41  ? -15.883 5.654   -7.442  1.00 24.55  ? 50  TRP   B C   1 
ATOM   580  O  O   . TRP   B 2 41  ? -16.190 6.755   -7.012  1.00 25.71  ? 50  TRP   B O   1 
ATOM   581  C  CB  A TRP   B 2 41  ? -16.326 3.618   -5.957  0.50 25.21  ? 50  TRP   B CB  1 
ATOM   582  C  CB  B TRP   B 2 41  ? -16.199 3.589   -6.012  0.50 23.16  ? 50  TRP   B CB  1 
ATOM   583  C  CG  A TRP   B 2 41  ? -16.376 4.375   -4.663  0.50 26.85  ? 50  TRP   B CG  1 
ATOM   584  C  CG  B TRP   B 2 41  ? -16.063 4.389   -4.759  0.50 23.08  ? 50  TRP   B CG  1 
ATOM   585  C  CD1 A TRP   B 2 41  ? -17.400 4.399   -3.763  0.50 28.02  ? 50  TRP   B CD1 1 
ATOM   586  C  CD1 B TRP   B 2 41  ? -15.032 5.210   -4.415  0.50 23.52  ? 50  TRP   B CD1 1 
ATOM   587  C  CD2 A TRP   B 2 41  ? -15.359 5.237   -4.140  0.50 27.59  ? 50  TRP   B CD2 1 
ATOM   588  C  CD2 B TRP   B 2 41  ? -17.054 4.538   -3.741  0.50 22.99  ? 50  TRP   B CD2 1 
ATOM   589  N  NE1 A TRP   B 2 41  ? -17.082 5.230   -2.708  0.50 28.47  ? 50  TRP   B NE1 1 
ATOM   590  N  NE1 B TRP   B 2 41  ? -15.303 5.838   -3.224  0.50 23.45  ? 50  TRP   B NE1 1 
ATOM   591  C  CE2 A TRP   B 2 41  ? -15.830 5.749   -2.914  0.50 28.66  ? 50  TRP   B CE2 1 
ATOM   592  C  CE2 B TRP   B 2 41  ? -16.547 5.451   -2.790  0.50 23.72  ? 50  TRP   B CE2 1 
ATOM   593  C  CE3 A TRP   B 2 41  ? -14.084 5.611   -4.581  0.50 28.71  ? 50  TRP   B CE3 1 
ATOM   594  C  CE3 B TRP   B 2 41  ? -18.326 3.989   -3.538  0.50 23.14  ? 50  TRP   B CE3 1 
ATOM   595  C  CZ2 A TRP   B 2 41  ? -15.080 6.624   -2.136  0.50 30.19  ? 50  TRP   B CZ2 1 
ATOM   596  C  CZ2 B TRP   B 2 41  ? -17.259 5.814   -1.651  0.50 24.89  ? 50  TRP   B CZ2 1 
ATOM   597  C  CZ3 A TRP   B 2 41  ? -13.333 6.460   -3.794  0.50 30.04  ? 50  TRP   B CZ3 1 
ATOM   598  C  CZ3 B TRP   B 2 41  ? -19.033 4.360   -2.409  0.50 24.23  ? 50  TRP   B CZ3 1 
ATOM   599  C  CH2 A TRP   B 2 41  ? -13.832 6.959   -2.590  0.50 30.34  ? 50  TRP   B CH2 1 
ATOM   600  C  CH2 B TRP   B 2 41  ? -18.515 5.291   -1.499  0.50 24.64  ? 50  TRP   B CH2 1 
ATOM   601  N  N   . HIS   B 2 42  ? -14.763 5.457   -8.183  1.00 25.21  ? 51  HIS   B N   1 
ATOM   602  C  CA  . HIS   B 2 42  ? -13.826 6.558   -8.425  1.00 26.08  ? 51  HIS   B CA  1 
ATOM   603  C  C   . HIS   B 2 42  ? -14.443 7.713   -9.242  1.00 26.93  ? 51  HIS   B C   1 
ATOM   604  O  O   . HIS   B 2 42  ? -13.908 8.826   -9.208  1.00 28.22  ? 51  HIS   B O   1 
ATOM   605  C  CB  . HIS   B 2 42  ? -12.494 6.066   -9.019  1.00 26.43  ? 51  HIS   B CB  1 
ATOM   606  C  CG  . HIS   B 2 42  ? -12.544 5.786   -10.497 1.00 28.02  ? 51  HIS   B CG  1 
ATOM   607  N  ND1 . HIS   B 2 42  ? -12.685 4.486   -10.983 1.00 29.47  ? 51  HIS   B ND1 1 
ATOM   608  C  CD2 . HIS   B 2 42  ? -12.505 6.647   -11.548 1.00 29.36  ? 51  HIS   B CD2 1 
ATOM   609  C  CE1 . HIS   B 2 42  ? -12.649 4.590   -12.310 1.00 30.00  ? 51  HIS   B CE1 1 
ATOM   610  N  NE2 . HIS   B 2 42  ? -12.544 5.872   -12.705 1.00 29.87  ? 51  HIS   B NE2 1 
ATOM   611  N  N   . VAL   B 2 43  ? -15.585 7.482   -9.914  1.00 25.80  ? 52  VAL   B N   1 
ATOM   612  C  CA  . VAL   B 2 43  ? -16.246 8.555   -10.682 1.00 25.75  ? 52  VAL   B CA  1 
ATOM   613  C  C   . VAL   B 2 43  ? -16.955 9.554   -9.726  1.00 27.26  ? 52  VAL   B C   1 
ATOM   614  O  O   . VAL   B 2 43  ? -16.809 10.791  -9.875  1.00 28.12  ? 52  VAL   B O   1 
ATOM   615  C  CB  . VAL   B 2 43  ? -17.257 7.971   -11.704 1.00 26.22  ? 52  VAL   B CB  1 
ATOM   616  C  CG1 . VAL   B 2 43  ? -18.171 9.071   -12.295 1.00 26.85  ? 52  VAL   B CG1 1 
ATOM   617  C  CG2 . VAL   B 2 43  ? -16.528 7.217   -12.823 1.00 26.32  ? 52  VAL   B CG2 1 
ATOM   618  N  N   . THR   B 2 44  ? -17.733 9.019   -8.747  1.00 24.96  ? 53  THR   B N   1 
ATOM   619  C  CA  . THR   B 2 44  ? -18.498 9.901   -7.866  1.00 25.44  ? 53  THR   B CA  1 
ATOM   620  C  C   . THR   B 2 44  ? -17.942 10.064  -6.453  1.00 26.10  ? 53  THR   B C   1 
ATOM   621  O  O   . THR   B 2 44  ? -18.406 10.945  -5.712  1.00 25.98  ? 53  THR   B O   1 
ATOM   622  C  CB  . THR   B 2 44  ? -19.968 9.420   -7.738  1.00 25.97  ? 53  THR   B CB  1 
ATOM   623  O  OG1 . THR   B 2 44  ? -19.977 8.131   -7.101  1.00 24.88  ? 53  THR   B OG1 1 
ATOM   624  C  CG2 . THR   B 2 44  ? -20.692 9.330   -9.088  1.00 25.50  ? 53  THR   B CG2 1 
ATOM   625  N  N   . LYS   B 2 45  ? -17.043 9.143   -6.043  1.00 26.81  ? 54  LYS   B N   1 
ATOM   626  C  CA  . LYS   B 2 45  ? -16.546 9.085   -4.658  1.00 28.22  ? 54  LYS   B CA  1 
ATOM   627  C  C   . LYS   B 2 45  ? -17.744 8.895   -3.668  1.00 30.20  ? 54  LYS   B C   1 
ATOM   628  O  O   . LYS   B 2 45  ? -17.630 9.250   -2.498  1.00 31.27  ? 54  LYS   B O   1 
ATOM   629  C  CB  . LYS   B 2 45  ? -15.671 10.316  -4.282  1.00 30.37  ? 54  LYS   B CB  1 
ATOM   630  C  CG  . LYS   B 2 45  ? -14.532 10.649  -5.281  1.00 36.57  ? 54  LYS   B CG  1 
ATOM   631  C  CD  . LYS   B 2 45  ? -13.591 9.490   -5.545  1.00 43.52  ? 54  LYS   B CD  1 
ATOM   632  C  CE  . LYS   B 2 45  ? -12.346 9.895   -6.321  1.00 49.53  ? 54  LYS   B CE  1 
ATOM   633  N  NZ  . LYS   B 2 45  ? -12.670 10.755  -7.501  1.00 51.88  ? 54  LYS   B NZ  1 
ATOM   634  N  N   . GLY   B 2 46  ? -18.869 8.344   -4.145  1.00 30.62  ? 55  GLY   B N   1 
ATOM   635  C  CA  . GLY   B 2 46  ? -20.056 8.110   -3.329  1.00 31.16  ? 55  GLY   B CA  1 
ATOM   636  C  C   . GLY   B 2 46  ? -20.920 9.331   -3.082  1.00 31.65  ? 55  GLY   B C   1 
ATOM   637  O  O   . GLY   B 2 46  ? -21.801 9.286   -2.232  1.00 32.56  ? 55  GLY   B O   1 
ATOM   638  N  N   . ALA   B 2 47  ? -20.696 10.437  -3.812  1.00 31.06  ? 56  ALA   B N   1 
ATOM   639  C  CA  . ALA   B 2 47  ? -21.517 11.641  -3.647  1.00 31.57  ? 56  ALA   B CA  1 
ATOM   640  C  C   . ALA   B 2 47  ? -22.931 11.459  -4.232  1.00 31.03  ? 56  ALA   B C   1 
ATOM   641  O  O   . ALA   B 2 47  ? -23.116 10.658  -5.143  1.00 29.94  ? 56  ALA   B O   1 
ATOM   642  C  CB  . ALA   B 2 47  ? -20.851 12.828  -4.334  1.00 33.09  ? 56  ALA   B CB  1 
ATOM   643  N  N   . ALA   B 2 48  ? -23.907 12.257  -3.766  1.00 30.11  ? 57  ALA   B N   1 
ATOM   644  C  CA  . ALA   B 2 48  ? -25.248 12.243  -4.369  1.00 30.01  ? 57  ALA   B CA  1 
ATOM   645  C  C   . ALA   B 2 48  ? -25.194 12.779  -5.803  1.00 30.58  ? 57  ALA   B C   1 
ATOM   646  O  O   . ALA   B 2 48  ? -24.288 13.530  -6.154  1.00 31.53  ? 57  ALA   B O   1 
ATOM   647  C  CB  . ALA   B 2 48  ? -26.214 13.119  -3.556  1.00 29.49  ? 57  ALA   B CB  1 
ATOM   648  N  N   . LEU   B 2 49  ? -26.181 12.419  -6.625  1.00 29.90  ? 58  LEU   B N   1 
ATOM   649  C  CA  . LEU   B 2 49  ? -26.256 12.874  -8.004  1.00 31.01  ? 58  LEU   B CA  1 
ATOM   650  C  C   . LEU   B 2 49  ? -27.592 13.563  -8.266  1.00 33.50  ? 58  LEU   B C   1 
ATOM   651  O  O   . LEU   B 2 49  ? -28.592 13.286  -7.604  1.00 33.86  ? 58  LEU   B O   1 
ATOM   652  C  CB  . LEU   B 2 49  ? -26.148 11.680  -8.991  1.00 30.28  ? 58  LEU   B CB  1 
ATOM   653  C  CG  . LEU   B 2 49  ? -24.899 10.807  -8.897  1.00 32.03  ? 58  LEU   B CG  1 
ATOM   654  C  CD1 . LEU   B 2 49  ? -24.999 9.600   -9.801  1.00 32.31  ? 58  LEU   B CD1 1 
ATOM   655  C  CD2 . LEU   B 2 49  ? -23.655 11.599  -9.214  1.00 33.55  ? 58  LEU   B CD2 1 
ATOM   656  N  N   . ARG   B 2 50  ? -27.610 14.434  -9.252  1.00 34.65  ? 59  ARG   B N   1 
ATOM   657  C  CA  . ARG   B 2 50  ? -28.807 15.115  -9.683  1.00 36.64  ? 59  ARG   B CA  1 
ATOM   658  C  C   . ARG   B 2 50  ? -29.250 14.532  -11.045 1.00 37.69  ? 59  ARG   B C   1 
ATOM   659  O  O   . ARG   B 2 50  ? -28.412 14.174  -11.878 1.00 36.48  ? 59  ARG   B O   1 
ATOM   660  C  CB  . ARG   B 2 50  ? -28.497 16.616  -9.789  1.00 39.49  ? 59  ARG   B CB  1 
ATOM   661  C  CG  . ARG   B 2 50  ? -29.570 17.431  -10.455 1.00 46.86  ? 59  ARG   B CG  1 
ATOM   662  C  CD  . ARG   B 2 50  ? -29.471 18.926  -10.152 1.00 52.13  ? 59  ARG   B CD  1 
ATOM   663  N  NE  . ARG   B 2 50  ? -28.106 19.454  -10.253 1.00 55.81  ? 59  ARG   B NE  1 
ATOM   664  C  CZ  . ARG   B 2 50  ? -27.538 19.862  -11.382 1.00 58.17  ? 59  ARG   B CZ  1 
ATOM   665  N  NH1 . ARG   B 2 50  ? -28.198 19.782  -12.534 1.00 56.80  ? 59  ARG   B NH1 1 
ATOM   666  N  NH2 . ARG   B 2 50  ? -26.300 20.341  -11.371 1.00 58.88  ? 59  ARG   B NH2 1 
ATOM   667  N  N   . SER   B 2 51  ? -30.557 14.437  -11.268 1.00 39.05  ? 60  SER   B N   1 
ATOM   668  C  CA  . SER   B 2 51  ? -31.093 13.988  -12.554 1.00 40.92  ? 60  SER   B CA  1 
ATOM   669  C  C   . SER   B 2 51  ? -32.266 14.934  -12.815 1.00 42.44  ? 60  SER   B C   1 
ATOM   670  O  O   . SER   B 2 51  ? -33.331 14.743  -12.240 1.00 43.07  ? 60  SER   B O   1 
ATOM   671  C  CB  . SER   B 2 51  ? -31.565 12.539  -12.458 1.00 42.33  ? 60  SER   B CB  1 
ATOM   672  O  OG  . SER   B 2 51  ? -32.181 12.142  -13.666 1.00 45.13  ? 60  SER   B OG  1 
ATOM   673  N  N   . GLY   B 2 52  ? -32.028 16.012  -13.564 1.00 43.09  ? 61  GLY   B N   1 
ATOM   674  C  CA  . GLY   B 2 52  ? -33.032 17.053  -13.774 1.00 44.28  ? 61  GLY   B CA  1 
ATOM   675  C  C   . GLY   B 2 52  ? -33.246 17.790  -12.466 1.00 45.71  ? 61  GLY   B C   1 
ATOM   676  O  O   . GLY   B 2 52  ? -32.290 18.273  -11.865 1.00 45.72  ? 61  GLY   B O   1 
ATOM   677  N  N   . GLU   B 2 53  ? -34.485 17.807  -11.964 1.00 46.54  ? 62  GLU   B N   1 
ATOM   678  C  CA  . GLU   B 2 53  ? -34.802 18.393  -10.665 1.00 48.20  ? 62  GLU   B CA  1 
ATOM   679  C  C   . GLU   B 2 53  ? -34.753 17.349  -9.518  1.00 48.13  ? 62  GLU   B C   1 
ATOM   680  O  O   . GLU   B 2 53  ? -34.896 17.728  -8.354  1.00 49.12  ? 62  GLU   B O   1 
ATOM   681  C  CB  . GLU   B 2 53  ? -36.192 19.030  -10.708 1.00 52.61  ? 62  GLU   B CB  1 
ATOM   682  C  CG  . GLU   B 2 53  ? -36.188 20.510  -11.040 1.00 61.96  ? 62  GLU   B CG  1 
ATOM   683  C  CD  . GLU   B 2 53  ? -37.533 21.162  -10.783 1.00 74.60  ? 62  GLU   B CD  1 
ATOM   684  O  OE1 . GLU   B 2 53  ? -38.566 20.507  -11.059 1.00 78.02  ? 62  GLU   B OE1 1 
ATOM   685  O  OE2 . GLU   B 2 53  ? -37.559 22.322  -10.309 1.00 78.64  ? 62  GLU   B OE2 1 
ATOM   686  N  N   . GLY   B 2 54  ? -34.573 16.063  -9.851  1.00 46.52  ? 63  GLY   B N   1 
ATOM   687  C  CA  . GLY   B 2 54  ? -34.536 14.976  -8.886  1.00 45.79  ? 63  GLY   B CA  1 
ATOM   688  C  C   . GLY   B 2 54  ? -33.154 14.671  -8.344  1.00 44.80  ? 63  GLY   B C   1 
ATOM   689  O  O   . GLY   B 2 54  ? -32.134 15.109  -8.895  1.00 44.77  ? 63  GLY   B O   1 
ATOM   690  N  N   . ARG   B 2 55  ? -33.125 13.931  -7.237  1.00 42.84  ? 64  ARG   B N   1 
ATOM   691  C  CA  . ARG   B 2 55  ? -31.901 13.543  -6.563  1.00 41.60  ? 64  ARG   B CA  1 
ATOM   692  C  C   . ARG   B 2 55  ? -31.778 12.001  -6.546  1.00 39.88  ? 64  ARG   B C   1 
ATOM   693  O  O   . ARG   B 2 55  ? -32.785 11.293  -6.404  1.00 41.23  ? 64  ARG   B O   1 
ATOM   694  C  CB  . ARG   B 2 55  ? -31.941 14.081  -5.122  1.00 42.93  ? 64  ARG   B CB  1 
ATOM   695  C  CG  . ARG   B 2 55  ? -30.652 13.915  -4.326  1.00 45.51  ? 64  ARG   B CG  1 
ATOM   696  C  CD  . ARG   B 2 55  ? -30.869 14.389  -2.894  1.00 48.77  ? 64  ARG   B CD  1 
ATOM   697  N  NE  . ARG   B 2 55  ? -29.732 14.073  -2.036  1.00 51.85  ? 64  ARG   B NE  1 
ATOM   698  C  CZ  . ARG   B 2 55  ? -28.978 14.977  -1.416  1.00 54.45  ? 64  ARG   B CZ  1 
ATOM   699  N  NH1 . ARG   B 2 55  ? -29.254 16.271  -1.528  1.00 55.17  ? 64  ARG   B NH1 1 
ATOM   700  N  NH2 . ARG   B 2 55  ? -27.959 14.592  -0.660  1.00 52.49  ? 64  ARG   B NH2 1 
ATOM   701  N  N   . LEU   B 2 56  ? -30.549 11.498  -6.719  1.00 35.57  ? 65  LEU   B N   1 
ATOM   702  C  CA  . LEU   B 2 56  ? -30.220 10.085  -6.643  1.00 32.83  ? 65  LEU   B CA  1 
ATOM   703  C  C   . LEU   B 2 56  ? -29.248 9.952   -5.479  1.00 30.95  ? 65  LEU   B C   1 
ATOM   704  O  O   . LEU   B 2 56  ? -28.180 10.567  -5.490  1.00 30.88  ? 65  LEU   B O   1 
ATOM   705  C  CB  . LEU   B 2 56  ? -29.499 9.573   -7.924  1.00 32.00  ? 65  LEU   B CB  1 
ATOM   706  C  CG  . LEU   B 2 56  ? -30.160 9.706   -9.315  1.00 34.90  ? 65  LEU   B CG  1 
ATOM   707  C  CD1 . LEU   B 2 56  ? -29.562 8.681   -10.289 1.00 34.33  ? 65  LEU   B CD1 1 
ATOM   708  C  CD2 . LEU   B 2 56  ? -31.659 9.487   -9.274  1.00 37.18  ? 65  LEU   B CD2 1 
ATOM   709  N  N   . ASP   B 2 57  ? -29.602 9.151   -4.490  1.00 29.83  ? 66  ASP   B N   1 
ATOM   710  C  CA  . ASP   B 2 57  ? -28.751 8.940   -3.322  1.00 29.42  ? 66  ASP   B CA  1 
ATOM   711  C  C   . ASP   B 2 57  ? -28.045 7.591   -3.430  1.00 28.48  ? 66  ASP   B C   1 
ATOM   712  O  O   . ASP   B 2 57  ? -28.636 6.615   -3.911  1.00 28.71  ? 66  ASP   B O   1 
ATOM   713  C  CB  . ASP   B 2 57  ? -29.606 8.960   -2.026  1.00 32.40  ? 66  ASP   B CB  1 
ATOM   714  C  CG  . ASP   B 2 57  ? -30.284 10.313  -1.826  1.00 39.70  ? 66  ASP   B CG  1 
ATOM   715  O  OD1 . ASP   B 2 57  ? -29.622 11.344  -2.060  1.00 39.77  ? 66  ASP   B OD1 1 
ATOM   716  O  OD2 . ASP   B 2 57  ? -31.492 10.332  -1.485  1.00 42.45  ? 66  ASP   B OD2 1 
ATOM   717  N  N   . PRO   B 2 58  ? -26.786 7.511   -2.979  1.00 27.32  ? 67  PRO   B N   1 
ATOM   718  C  CA  . PRO   B 2 58  ? -26.093 6.212   -2.991  1.00 26.78  ? 67  PRO   B CA  1 
ATOM   719  C  C   . PRO   B 2 58  ? -26.830 5.189   -2.126  1.00 26.52  ? 67  PRO   B C   1 
ATOM   720  O  O   . PRO   B 2 58  ? -27.443 5.531   -1.100  1.00 27.17  ? 67  PRO   B O   1 
ATOM   721  C  CB  . PRO   B 2 58  ? -24.702 6.534   -2.426  1.00 28.12  ? 67  PRO   B CB  1 
ATOM   722  C  CG  . PRO   B 2 58  ? -24.898 7.810   -1.644  1.00 29.76  ? 67  PRO   B CG  1 
ATOM   723  C  CD  . PRO   B 2 58  ? -25.972 8.570   -2.353  1.00 28.56  ? 67  PRO   B CD  1 
ATOM   724  N  N   . TYR   B 2 59  ? -26.767 3.938   -2.534  1.00 25.38  ? 68  TYR   B N   1 
ATOM   725  C  CA  . TYR   B 2 59  ? -27.466 2.863   -1.855  1.00 24.97  ? 68  TYR   B CA  1 
ATOM   726  C  C   . TYR   B 2 59  ? -26.458 1.791   -1.406  1.00 24.82  ? 68  TYR   B C   1 
ATOM   727  O  O   . TYR   B 2 59  ? -26.551 1.263   -0.288  1.00 25.69  ? 68  TYR   B O   1 
ATOM   728  C  CB  . TYR   B 2 59  ? -28.532 2.260   -2.801  1.00 25.00  ? 68  TYR   B CB  1 
ATOM   729  C  CG  . TYR   B 2 59  ? -29.312 1.118   -2.183  1.00 25.39  ? 68  TYR   B CG  1 
ATOM   730  C  CD1 . TYR   B 2 59  ? -28.758 -0.153  -2.077  1.00 26.87  ? 68  TYR   B CD1 1 
ATOM   731  C  CD2 . TYR   B 2 59  ? -30.602 1.313   -1.690  1.00 26.23  ? 68  TYR   B CD2 1 
ATOM   732  C  CE1 . TYR   B 2 59  ? -29.459 -1.201  -1.492  1.00 27.01  ? 68  TYR   B CE1 1 
ATOM   733  C  CE2 . TYR   B 2 59  ? -31.329 0.261   -1.161  1.00 26.28  ? 68  TYR   B CE2 1 
ATOM   734  C  CZ  . TYR   B 2 59  ? -30.756 -0.996  -1.070  1.00 26.61  ? 68  TYR   B CZ  1 
ATOM   735  O  OH  . TYR   B 2 59  ? -31.479 -2.025  -0.530  1.00 28.83  ? 68  TYR   B OH  1 
ATOM   736  N  N   . TRP   B 2 60  ? -25.525 1.456   -2.297  1.00 24.55  ? 69  TRP   B N   1 
ATOM   737  C  CA  . TRP   B 2 60  ? -24.497 0.467   -1.996  1.00 25.13  ? 69  TRP   B CA  1 
ATOM   738  C  C   . TRP   B 2 60  ? -23.219 0.904   -2.692  1.00 24.86  ? 69  TRP   B C   1 
ATOM   739  O  O   . TRP   B 2 60  ? -23.261 1.440   -3.806  1.00 23.35  ? 69  TRP   B O   1 
ATOM   740  C  CB  . TRP   B 2 60  ? -24.908 -0.913  -2.544  1.00 25.38  ? 69  TRP   B CB  1 
ATOM   741  C  CG  . TRP   B 2 60  ? -23.786 -1.909  -2.511  1.00 26.08  ? 69  TRP   B CG  1 
ATOM   742  C  CD1 . TRP   B 2 60  ? -23.343 -2.622  -1.428  1.00 26.27  ? 69  TRP   B CD1 1 
ATOM   743  C  CD2 . TRP   B 2 60  ? -22.875 -2.188  -3.585  1.00 24.47  ? 69  TRP   B CD2 1 
ATOM   744  N  NE1 . TRP   B 2 60  ? -22.248 -3.379  -1.785  1.00 26.30  ? 69  TRP   B NE1 1 
ATOM   745  C  CE2 . TRP   B 2 60  ? -21.900 -3.077  -3.086  1.00 25.44  ? 69  TRP   B CE2 1 
ATOM   746  C  CE3 . TRP   B 2 60  ? -22.769 -1.739  -4.915  1.00 24.53  ? 69  TRP   B CE3 1 
ATOM   747  C  CZ2 . TRP   B 2 60  ? -20.862 -3.572  -3.890  1.00 25.67  ? 69  TRP   B CZ2 1 
ATOM   748  C  CZ3 . TRP   B 2 60  ? -21.714 -2.186  -5.697  1.00 24.58  ? 69  TRP   B CZ3 1 
ATOM   749  C  CH2 . TRP   B 2 60  ? -20.806 -3.134  -5.209  1.00 25.66  ? 69  TRP   B CH2 1 
ATOM   750  N  N   . GLY   B 2 61  ? -22.083 0.602   -2.074  1.00 24.36  ? 70  GLY   B N   1 
ATOM   751  C  CA  . GLY   B 2 61  ? -20.808 0.895   -2.722  1.00 24.32  ? 70  GLY   B CA  1 
ATOM   752  C  C   . GLY   B 2 61  ? -19.662 0.166   -2.051  1.00 24.38  ? 70  GLY   B C   1 
ATOM   753  O  O   . GLY   B 2 61  ? -19.760 -0.210  -0.882  1.00 24.75  ? 70  GLY   B O   1 
ATOM   754  N  N   . ASP   B 2 62  ? -18.554 0.019   -2.790  1.00 24.92  ? 71  ASP   B N   1 
ATOM   755  C  CA  . ASP   B 2 62  ? -17.391 -0.672  -2.239  1.00 24.86  ? 71  ASP   B CA  1 
ATOM   756  C  C   . ASP   B 2 62  ? -16.146 -0.163  -2.984  1.00 24.85  ? 71  ASP   B C   1 
ATOM   757  O  O   . ASP   B 2 62  ? -16.026 -0.325  -4.193  1.00 25.79  ? 71  ASP   B O   1 
ATOM   758  C  CB  . ASP   B 2 62  ? -17.553 -2.196  -2.416  1.00 26.78  ? 71  ASP   B CB  1 
ATOM   759  C  CG  . ASP   B 2 62  ? -16.458 -2.969  -1.695  1.00 33.28  ? 71  ASP   B CG  1 
ATOM   760  O  OD1 . ASP   B 2 62  ? -15.349 -3.082  -2.243  1.00 32.29  ? 71  ASP   B OD1 1 
ATOM   761  O  OD2 . ASP   B 2 62  ? -16.694 -3.399  -0.578  1.00 38.27  ? 71  ASP   B OD2 1 
ATOM   762  N  N   . VAL   B 2 63  ? -15.215 0.475   -2.237  1.00 24.75  ? 72  VAL   B N   1 
ATOM   763  C  CA  . VAL   B 2 63  ? -13.973 1.028   -2.822  1.00 25.06  ? 72  VAL   B CA  1 
ATOM   764  C  C   . VAL   B 2 63  ? -13.107 -0.055  -3.477  1.00 25.83  ? 72  VAL   B C   1 
ATOM   765  O  O   . VAL   B 2 63  ? -12.526 0.208   -4.559  1.00 25.72  ? 72  VAL   B O   1 
ATOM   766  C  CB  . VAL   B 2 63  ? -13.175 1.861   -1.779  1.00 25.24  ? 72  VAL   B CB  1 
ATOM   767  C  CG1 . VAL   B 2 63  ? -11.678 1.991   -2.125  1.00 26.06  ? 72  VAL   B CG1 1 
ATOM   768  C  CG2 . VAL   B 2 63  ? -13.821 3.221   -1.537  1.00 25.38  ? 72  VAL   B CG2 1 
ATOM   769  N  N   . LYS   B 2 64  ? -13.029 -1.258  -2.845  1.00 25.89  ? 73  LYS   B N   1 
ATOM   770  C  CA  . LYS   B 2 64  ? -12.147 -2.290  -3.415  1.00 27.04  ? 73  LYS   B CA  1 
ATOM   771  C  C   . LYS   B 2 64  ? -12.633 -2.820  -4.779  1.00 26.49  ? 73  LYS   B C   1 
ATOM   772  O  O   . LYS   B 2 64  ? -11.847 -2.968  -5.703  1.00 27.91  ? 73  LYS   B O   1 
ATOM   773  C  CB  . LYS   B 2 64  ? -11.912 -3.445  -2.454  1.00 29.05  ? 73  LYS   B CB  1 
ATOM   774  C  CG  . LYS   B 2 64  ? -10.875 -4.445  -3.017  1.00 31.42  ? 73  LYS   B CG  1 
ATOM   775  C  CD  . LYS   B 2 64  ? -10.522 -5.503  -1.983  1.00 32.95  ? 73  LYS   B CD  1 
ATOM   776  C  CE  . LYS   B 2 64  ? -9.647  -6.567  -2.593  1.00 36.38  ? 73  LYS   B CE  1 
ATOM   777  N  NZ  . LYS   B 2 64  ? -9.246  -7.610  -1.604  1.00 38.35  ? 73  LYS   B NZ  1 
ATOM   778  N  N   . GLN   B 2 65  ? -13.943 -3.053  -4.904  1.00 25.93  ? 74  GLN   B N   1 
ATOM   779  C  CA  . GLN   B 2 65  ? -14.536 -3.435  -6.194  1.00 25.60  ? 74  GLN   B CA  1 
ATOM   780  C  C   . GLN   B 2 65  ? -14.584 -2.250  -7.182  1.00 24.91  ? 74  GLN   B C   1 
ATOM   781  O  O   . GLN   B 2 65  ? -14.772 -2.462  -8.392  1.00 24.68  ? 74  GLN   B O   1 
ATOM   782  C  CB  . GLN   B 2 65  ? -15.978 -3.930  -5.985  1.00 27.18  ? 74  GLN   B CB  1 
ATOM   783  C  CG  . GLN   B 2 65  ? -16.056 -5.253  -5.199  1.00 31.20  ? 74  GLN   B CG  1 
ATOM   784  C  CD  . GLN   B 2 65  ? -17.502 -5.710  -5.038  1.00 38.24  ? 74  GLN   B CD  1 
ATOM   785  O  OE1 . GLN   B 2 65  ? -18.269 -5.816  -6.017  1.00 40.21  ? 74  GLN   B OE1 1 
ATOM   786  N  NE2 . GLN   B 2 65  ? -17.914 -6.007  -3.798  1.00 40.57  ? 74  GLN   B NE2 1 
ATOM   787  N  N   . ASP   B 2 66  ? -14.480 -1.007  -6.651  1.00 24.08  ? 75  ASP   B N   1 
ATOM   788  C  CA  . ASP   B 2 66  ? -14.577 0.268   -7.368  1.00 24.77  ? 75  ASP   B CA  1 
ATOM   789  C  C   . ASP   B 2 66  ? -15.975 0.391   -8.044  1.00 24.34  ? 75  ASP   B C   1 
ATOM   790  O  O   . ASP   B 2 66  ? -16.064 0.761   -9.210  1.00 24.29  ? 75  ASP   B O   1 
ATOM   791  C  CB  . ASP   B 2 66  ? -13.427 0.480   -8.407  1.00 23.78  ? 75  ASP   B CB  1 
ATOM   792  C  CG  . ASP   B 2 66  ? -13.360 1.901   -8.960  1.00 26.61  ? 75  ASP   B CG  1 
ATOM   793  O  OD1 . ASP   B 2 66  ? -13.794 2.833   -8.248  1.00 27.09  ? 75  ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   B 2 66  ? -12.840 2.079   -10.085 1.00 28.70  ? 75  ASP   B OD2 1 
ATOM   795  N  N   . LEU   B 2 67  ? -17.059 0.081   -7.292  1.00 24.20  ? 76  LEU   B N   1 
ATOM   796  C  CA  . LEU   B 2 67  ? -18.431 0.153   -7.814  1.00 23.57  ? 76  LEU   B CA  1 
ATOM   797  C  C   . LEU   B 2 67  ? -19.377 0.855   -6.815  1.00 23.13  ? 76  LEU   B C   1 
ATOM   798  O  O   . LEU   B 2 67  ? -19.146 0.828   -5.592  1.00 22.34  ? 76  LEU   B O   1 
ATOM   799  C  CB  . LEU   B 2 67  ? -18.992 -1.263  -8.098  1.00 23.55  ? 76  LEU   B CB  1 
ATOM   800  C  CG  . LEU   B 2 67  ? -18.331 -2.041  -9.239  1.00 23.85  ? 76  LEU   B CG  1 
ATOM   801  C  CD1 . LEU   B 2 67  ? -18.846 -3.494  -9.259  1.00 24.37  ? 76  LEU   B CD1 1 
ATOM   802  C  CD2 . LEU   B 2 67  ? -18.547 -1.302  -10.636 1.00 24.00  ? 76  LEU   B CD2 1 
ATOM   803  N  N   . VAL   B 2 68  ? -20.472 1.438   -7.363  1.00 22.50  ? 77  VAL   B N   1 
ATOM   804  C  CA  . VAL   B 2 68  ? -21.477 2.106   -6.525  1.00 22.52  ? 77  VAL   B CA  1 
ATOM   805  C  C   . VAL   B 2 68  ? -22.830 2.018   -7.250  1.00 22.86  ? 77  VAL   B C   1 
ATOM   806  O  O   . VAL   B 2 68  ? -22.879 2.105   -8.497  1.00 23.01  ? 77  VAL   B O   1 
ATOM   807  C  CB  . VAL   B 2 68  ? -21.057 3.579   -6.167  1.00 23.51  ? 77  VAL   B CB  1 
ATOM   808  C  CG1 . VAL   B 2 68  ? -20.759 4.419   -7.417  1.00 24.80  ? 77  VAL   B CG1 1 
ATOM   809  C  CG2 . VAL   B 2 68  ? -22.074 4.283   -5.246  1.00 24.16  ? 77  VAL   B CG2 1 
ATOM   810  N  N   . SER   B 2 69  ? -23.922 1.840   -6.492  1.00 22.26  ? 78  SER   B N   1 
ATOM   811  C  CA  . SER   B 2 69  ? -25.285 1.858   -7.051  1.00 23.15  ? 78  SER   B CA  1 
ATOM   812  C  C   . SER   B 2 69  ? -26.105 2.966   -6.337  1.00 24.16  ? 78  SER   B C   1 
ATOM   813  O  O   . SER   B 2 69  ? -25.851 3.283   -5.153  1.00 23.50  ? 78  SER   B O   1 
ATOM   814  C  CB  . SER   B 2 69  ? -25.978 0.490   -6.930  1.00 23.93  ? 78  SER   B CB  1 
ATOM   815  O  OG  . SER   B 2 69  ? -26.332 0.142   -5.599  1.00 24.34  ? 78  SER   B OG  1 
ATOM   816  N  N   . TYR   B 2 70  ? -27.097 3.526   -7.045  1.00 22.64  ? 79  TYR   B N   1 
ATOM   817  C  CA  . TYR   B 2 70  ? -27.941 4.636   -6.563  1.00 23.69  ? 79  TYR   B CA  1 
ATOM   818  C  C   . TYR   B 2 70  ? -29.416 4.223   -6.691  1.00 24.90  ? 79  TYR   B C   1 
ATOM   819  O  O   . TYR   B 2 70  ? -29.800 3.645   -7.741  1.00 24.91  ? 79  TYR   B O   1 
ATOM   820  C  CB  . TYR   B 2 70  ? -27.730 5.894   -7.449  1.00 24.07  ? 79  TYR   B CB  1 
ATOM   821  C  CG  . TYR   B 2 70  ? -26.403 6.567   -7.192  1.00 24.68  ? 79  TYR   B CG  1 
ATOM   822  C  CD1 . TYR   B 2 70  ? -25.234 6.097   -7.787  1.00 24.53  ? 79  TYR   B CD1 1 
ATOM   823  C  CD2 . TYR   B 2 70  ? -26.314 7.680   -6.357  1.00 25.47  ? 79  TYR   B CD2 1 
ATOM   824  C  CE1 . TYR   B 2 70  ? -23.997 6.671   -7.497  1.00 24.85  ? 79  TYR   B CE1 1 
ATOM   825  C  CE2 . TYR   B 2 70  ? -25.089 8.277   -6.081  1.00 25.98  ? 79  TYR   B CE2 1 
ATOM   826  C  CZ  . TYR   B 2 70  ? -23.929 7.742   -6.627  1.00 26.01  ? 79  TYR   B CZ  1 
ATOM   827  O  OH  . TYR   B 2 70  ? -22.714 8.303   -6.339  1.00 27.31  ? 79  TYR   B OH  1 
ATOM   828  N  N   . CYS   B 2 71  ? -30.244 4.549   -5.642  1.00 25.71  ? 80  CYS   B N   1 
ATOM   829  C  CA  . CYS   B 2 71  ? -31.699 4.278   -5.597  1.00 27.34  ? 80  CYS   B CA  1 
ATOM   830  C  C   . CYS   B 2 71  ? -32.072 2.842   -5.289  1.00 28.54  ? 80  CYS   B C   1 
ATOM   831  O  O   . CYS   B 2 71  ? -33.256 2.578   -5.055  1.00 30.13  ? 80  CYS   B O   1 
ATOM   832  C  CB  . CYS   B 2 71  ? -32.414 4.737   -6.866  1.00 28.56  ? 80  CYS   B CB  1 
ATOM   833  S  SG  . CYS   B 2 71  ? -31.935 6.394   -7.417  1.00 34.21  ? 80  CYS   B SG  1 
ATOM   834  N  N   . GLY   B 2 72  ? -31.116 1.935   -5.314  1.00 27.30  ? 81  GLY   B N   1 
ATOM   835  C  CA  . GLY   B 2 72  ? -31.376 0.526   -5.068  1.00 26.75  ? 81  GLY   B CA  1 
ATOM   836  C  C   . GLY   B 2 72  ? -30.119 -0.308  -5.183  1.00 25.84  ? 81  GLY   B C   1 
ATOM   837  O  O   . GLY   B 2 72  ? -29.030 0.206   -5.464  1.00 25.52  ? 81  GLY   B O   1 
ATOM   838  N  N   . PRO   B 2 73  ? -30.248 -1.611  -4.867  1.00 25.40  ? 82  PRO   B N   1 
ATOM   839  C  CA  . PRO   B 2 73  ? -29.093 -2.516  -4.919  1.00 25.61  ? 82  PRO   B CA  1 
ATOM   840  C  C   . PRO   B 2 73  ? -28.590 -2.786  -6.341  1.00 25.95  ? 82  PRO   B C   1 
ATOM   841  O  O   . PRO   B 2 73  ? -29.351 -2.589  -7.305  1.00 26.23  ? 82  PRO   B O   1 
ATOM   842  C  CB  . PRO   B 2 73  ? -29.637 -3.803  -4.281  1.00 26.39  ? 82  PRO   B CB  1 
ATOM   843  C  CG  . PRO   B 2 73  ? -31.060 -3.795  -4.619  1.00 26.88  ? 82  PRO   B CG  1 
ATOM   844  C  CD  . PRO   B 2 73  ? -31.486 -2.333  -4.534  1.00 25.57  ? 82  PRO   B CD  1 
ATOM   845  N  N   . TRP   B 2 74  ? -27.317 -3.214  -6.482  1.00 25.72  ? 83  TRP   B N   1 
ATOM   846  C  CA  . TRP   B 2 74  ? -26.699 -3.533  -7.783  1.00 26.10  ? 83  TRP   B CA  1 
ATOM   847  C  C   . TRP   B 2 74  ? -27.569 -4.542  -8.540  1.00 26.48  ? 83  TRP   B C   1 
ATOM   848  O  O   . TRP   B 2 74  ? -27.910 -5.572  -7.967  1.00 26.87  ? 83  TRP   B O   1 
ATOM   849  C  CB  . TRP   B 2 74  ? -25.267 -4.070  -7.567  1.00 25.74  ? 83  TRP   B CB  1 
ATOM   850  C  CG  . TRP   B 2 74  ? -24.491 -4.260  -8.834  1.00 25.32  ? 83  TRP   B CG  1 
ATOM   851  C  CD1 . TRP   B 2 74  ? -24.417 -5.388  -9.601  1.00 25.49  ? 83  TRP   B CD1 1 
ATOM   852  C  CD2 . TRP   B 2 74  ? -23.657 -3.281  -9.469  1.00 24.76  ? 83  TRP   B CD2 1 
ATOM   853  N  NE1 . TRP   B 2 74  ? -23.617 -5.158  -10.698 1.00 25.74  ? 83  TRP   B NE1 1 
ATOM   854  C  CE2 . TRP   B 2 74  ? -23.159 -3.859  -10.656 1.00 25.23  ? 83  TRP   B CE2 1 
ATOM   855  C  CE3 . TRP   B 2 74  ? -23.320 -1.947  -9.171  1.00 23.97  ? 83  TRP   B CE3 1 
ATOM   856  C  CZ2 . TRP   B 2 74  ? -22.380 -3.139  -11.567 1.00 25.70  ? 83  TRP   B CZ2 1 
ATOM   857  C  CZ3 . TRP   B 2 74  ? -22.491 -1.260  -10.036 1.00 25.52  ? 83  TRP   B CZ3 1 
ATOM   858  C  CH2 . TRP   B 2 74  ? -22.044 -1.845  -11.233 1.00 25.52  ? 83  TRP   B CH2 1 
ATOM   859  N  N   . LYS   B 2 75  ? -27.967 -4.220  -9.793  1.00 26.09  ? 84  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 2 75  ? -28.895 -5.057  -10.591 1.00 27.35  ? 84  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 2 75  ? -28.204 -5.869  -11.694 1.00 29.71  ? 84  LYS   B C   1 
ATOM   862  O  O   . LYS   B 2 75  ? -28.817 -6.792  -12.233 1.00 31.07  ? 84  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 2 75  ? -29.960 -4.166  -11.280 1.00 27.81  ? 84  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 2 75  ? -30.811 -3.308  -10.326 1.00 30.44  ? 84  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 2 75  ? -31.712 -4.181  -9.439  1.00 35.73  ? 84  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 2 75  ? -32.659 -3.328  -8.609  1.00 39.83  ? 84  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 2 75  ? -33.761 -4.121  -8.003  1.00 42.58  ? 84  LYS   B NZ  1 
ATOM   868  N  N   . LEU   B 2 76  ? -26.993 -5.478  -12.096 1.00 29.14  ? 85  LEU   B N   1 
ATOM   869  C  CA  . LEU   B 2 76  ? -26.299 -6.092  -13.230 1.00 29.04  ? 85  LEU   B CA  1 
ATOM   870  C  C   . LEU   B 2 76  ? -25.635 -7.418  -12.842 1.00 30.87  ? 85  LEU   B C   1 
ATOM   871  O  O   . LEU   B 2 76  ? -24.747 -7.418  -11.997 1.00 30.75  ? 85  LEU   B O   1 
ATOM   872  C  CB  . LEU   B 2 76  ? -25.274 -5.095  -13.812 1.00 27.86  ? 85  LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 2 76  ? -25.770 -3.614  -14.064 1.00 28.37  ? 85  LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 2 76  ? -24.690 -2.768  -14.680 1.00 29.01  ? 85  LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 2 76  ? -27.014 -3.550  -14.911 1.00 28.62  ? 85  LEU   B CD2 1 
ATOM   876  N  N   . ASP   B 2 77  ? -26.051 -8.549  -13.460 1.00 32.54  ? 86  ASP   B N   1 
ATOM   877  C  CA  . ASP   B 2 77  ? -25.435 -9.838  -13.094 1.00 34.88  ? 86  ASP   B CA  1 
ATOM   878  C  C   . ASP   B 2 77  ? -24.924 -10.689 -14.261 1.00 34.54  ? 86  ASP   B C   1 
ATOM   879  O  O   . ASP   B 2 77  ? -24.480 -11.828 -14.019 1.00 34.67  ? 86  ASP   B O   1 
ATOM   880  C  CB  . ASP   B 2 77  ? -26.344 -10.699 -12.197 1.00 39.27  ? 86  ASP   B CB  1 
ATOM   881  C  CG  . ASP   B 2 77  ? -27.712 -11.006 -12.758 1.00 48.52  ? 86  ASP   B CG  1 
ATOM   882  O  OD1 . ASP   B 2 77  ? -28.078 -10.419 -13.797 1.00 50.59  ? 86  ASP   B OD1 1 
ATOM   883  O  OD2 . ASP   B 2 77  ? -28.423 -11.835 -12.155 1.00 53.76  ? 86  ASP   B OD2 1 
ATOM   884  N  N   . ALA   B 2 78  ? -24.946 -10.167 -15.488 1.00 33.20  ? 87  ALA   B N   1 
ATOM   885  C  CA  . ALA   B 2 78  ? -24.409 -10.945 -16.612 1.00 32.96  ? 87  ALA   B CA  1 
ATOM   886  C  C   . ALA   B 2 78  ? -22.885 -11.034 -16.507 1.00 33.06  ? 87  ALA   B C   1 
ATOM   887  O  O   . ALA   B 2 78  ? -22.221 -10.155 -15.937 1.00 32.40  ? 87  ALA   B O   1 
ATOM   888  C  CB  . ALA   B 2 78  ? -24.836 -10.353 -17.949 1.00 32.11  ? 87  ALA   B CB  1 
ATOM   889  N  N   . ALA   B 2 79  ? -22.335 -12.139 -17.021 1.00 33.87  ? 88  ALA   B N   1 
ATOM   890  C  CA  . ALA   B 2 79  ? -20.916 -12.382 -16.949 1.00 35.06  ? 88  ALA   B CA  1 
ATOM   891  C  C   . ALA   B 2 79  ? -20.347 -12.703 -18.326 1.00 35.52  ? 88  ALA   B C   1 
ATOM   892  O  O   . ALA   B 2 79  ? -21.009 -13.382 -19.130 1.00 35.40  ? 88  ALA   B O   1 
ATOM   893  C  CB  . ALA   B 2 79  ? -20.667 -13.564 -16.021 1.00 35.86  ? 88  ALA   B CB  1 
ATOM   894  N  N   . TRP   B 2 80  ? -19.087 -12.294 -18.588 1.00 35.38  ? 89  TRP   B N   1 
ATOM   895  C  CA  . TRP   B 2 80  ? -18.399 -12.675 -19.838 1.00 36.21  ? 89  TRP   B CA  1 
ATOM   896  C  C   . TRP   B 2 80  ? -18.287 -14.209 -19.885 1.00 37.11  ? 89  TRP   B C   1 
ATOM   897  O  O   . TRP   B 2 80  ? -18.036 -14.818 -18.855 1.00 36.25  ? 89  TRP   B O   1 
ATOM   898  C  CB  . TRP   B 2 80  ? -16.963 -12.095 -19.880 1.00 36.32  ? 89  TRP   B CB  1 
ATOM   899  C  CG  . TRP   B 2 80  ? -16.196 -12.440 -21.130 1.00 36.59  ? 89  TRP   B CG  1 
ATOM   900  C  CD1 . TRP   B 2 80  ? -16.668 -12.445 -22.413 1.00 37.94  ? 89  TRP   B CD1 1 
ATOM   901  C  CD2 . TRP   B 2 80  ? -14.820 -12.855 -21.204 1.00 36.96  ? 89  TRP   B CD2 1 
ATOM   902  N  NE1 . TRP   B 2 80  ? -15.672 -12.834 -23.284 1.00 38.88  ? 89  TRP   B NE1 1 
ATOM   903  C  CE2 . TRP   B 2 80  ? -14.520 -13.069 -22.569 1.00 38.13  ? 89  TRP   B CE2 1 
ATOM   904  C  CE3 . TRP   B 2 80  ? -13.802 -13.017 -20.257 1.00 37.61  ? 89  TRP   B CE3 1 
ATOM   905  C  CZ2 . TRP   B 2 80  ? -13.254 -13.472 -23.001 1.00 39.00  ? 89  TRP   B CZ2 1 
ATOM   906  C  CZ3 . TRP   B 2 80  ? -12.545 -13.412 -20.689 1.00 38.37  ? 89  TRP   B CZ3 1 
ATOM   907  C  CH2 . TRP   B 2 80  ? -12.284 -13.645 -22.045 1.00 38.21  ? 89  TRP   B CH2 1 
ATOM   908  N  N   . ASP   B 2 81  ? -18.558 -14.816 -21.055 1.00 38.58  ? 90  ASP   B N   1 
ATOM   909  C  CA  . ASP   B 2 81  ? -18.486 -16.277 -21.164 1.00 40.57  ? 90  ASP   B CA  1 
ATOM   910  C  C   . ASP   B 2 81  ? -17.058 -16.835 -21.266 1.00 43.43  ? 90  ASP   B C   1 
ATOM   911  O  O   . ASP   B 2 81  ? -16.895 -18.058 -21.281 1.00 44.77  ? 90  ASP   B O   1 
ATOM   912  C  CB  . ASP   B 2 81  ? -19.362 -16.780 -22.325 1.00 40.86  ? 90  ASP   B CB  1 
ATOM   913  C  CG  . ASP   B 2 81  ? -18.910 -16.382 -23.701 1.00 44.82  ? 90  ASP   B CG  1 
ATOM   914  O  OD1 . ASP   B 2 81  ? -17.792 -15.827 -23.829 1.00 44.78  ? 90  ASP   B OD1 1 
ATOM   915  O  OD2 . ASP   B 2 81  ? -19.657 -16.646 -24.670 1.00 48.62  ? 90  ASP   B OD2 1 
ATOM   916  N  N   . GLY   B 2 82  ? -16.042 -15.974 -21.343 1.00 43.91  ? 91  GLY   B N   1 
ATOM   917  C  CA  . GLY   B 2 82  ? -14.655 -16.444 -21.427 1.00 44.93  ? 91  GLY   B CA  1 
ATOM   918  C  C   . GLY   B 2 82  ? -14.209 -16.844 -22.827 1.00 45.84  ? 91  GLY   B C   1 
ATOM   919  O  O   . GLY   B 2 82  ? -13.065 -17.271 -23.016 1.00 46.56  ? 91  GLY   B O   1 
ATOM   920  N  N   . LEU   B 2 83  ? -15.094 -16.729 -23.820 1.00 46.12  ? 92  LEU   B N   1 
ATOM   921  C  CA  . LEU   B 2 83  ? -14.782 -17.167 -25.188 1.00 47.85  ? 92  LEU   B CA  1 
ATOM   922  C  C   . LEU   B 2 83  ? -15.096 -16.148 -26.288 1.00 48.07  ? 92  LEU   B C   1 
ATOM   923  O  O   . LEU   B 2 83  ? -14.413 -16.112 -27.310 1.00 48.60  ? 92  LEU   B O   1 
ATOM   924  C  CB  . LEU   B 2 83  ? -15.618 -18.413 -25.527 1.00 49.20  ? 92  LEU   B CB  1 
ATOM   925  C  CG  . LEU   B 2 83  ? -15.328 -19.709 -24.832 1.00 53.08  ? 92  LEU   B CG  1 
ATOM   926  C  CD1 . LEU   B 2 83  ? -16.186 -20.803 -25.445 1.00 54.04  ? 92  LEU   B CD1 1 
ATOM   927  C  CD2 . LEU   B 2 83  ? -13.871 -20.097 -25.001 1.00 54.09  ? 92  LEU   B CD2 1 
ATOM   928  N  N   . SER   B 2 84  ? -16.204 -15.429 -26.142 1.00 46.89  ? 93  SER   B N   1 
ATOM   929  C  CA  . SER   B 2 84  ? -16.733 -14.546 -27.152 1.00 46.77  ? 93  SER   B CA  1 
ATOM   930  C  C   . SER   B 2 84  ? -16.244 -13.113 -27.121 1.00 45.09  ? 93  SER   B C   1 
ATOM   931  O  O   . SER   B 2 84  ? -15.861 -12.584 -26.070 1.00 44.56  ? 93  SER   B O   1 
ATOM   932  C  CB  . SER   B 2 84  ? -18.258 -14.535 -27.058 1.00 49.52  ? 93  SER   B CB  1 
ATOM   933  O  OG  . SER   B 2 84  ? -18.780 -15.852 -27.009 1.00 53.08  ? 93  SER   B OG  1 
ATOM   934  N  N   . GLU   B 2 85  ? -16.331 -12.456 -28.283 1.00 43.27  ? 94  GLU   B N   1 
ATOM   935  C  CA  . GLU   B 2 85  ? -16.036 -11.044 -28.365 1.00 41.83  ? 94  GLU   B CA  1 
ATOM   936  C  C   . GLU   B 2 85  ? -17.201 -10.294 -27.644 1.00 40.36  ? 94  GLU   B C   1 
ATOM   937  O  O   . GLU   B 2 85  ? -18.308 -10.825 -27.473 1.00 40.57  ? 94  GLU   B O   1 
ATOM   938  C  CB  . GLU   B 2 85  ? -15.848 -10.583 -29.836 1.00 42.79  ? 94  GLU   B CB  1 
ATOM   939  C  CG  . GLU   B 2 85  ? -14.515 -11.057 -30.417 1.00 45.45  ? 94  GLU   B CG  1 
ATOM   940  C  CD  . GLU   B 2 85  ? -14.093 -10.399 -31.723 1.00 51.98  ? 94  GLU   B CD  1 
ATOM   941  O  OE1 . GLU   B 2 85  ? -14.963 -9.815  -32.406 1.00 51.76  ? 94  GLU   B OE1 1 
ATOM   942  O  OE2 . GLU   B 2 85  ? -12.886 -10.459 -32.053 1.00 54.16  ? 94  GLU   B OE2 1 
ATOM   943  N  N   . VAL   B 2 86  ? -16.905 -9.106  -27.144 1.00 38.18  ? 95  VAL   B N   1 
ATOM   944  C  CA  . VAL   B 2 86  ? -17.865 -8.260  -26.425 1.00 36.36  ? 95  VAL   B CA  1 
ATOM   945  C  C   . VAL   B 2 86  ? -17.825 -6.872  -27.073 1.00 36.32  ? 95  VAL   B C   1 
ATOM   946  O  O   . VAL   B 2 86  ? -17.009 -6.640  -27.968 1.00 37.75  ? 95  VAL   B O   1 
ATOM   947  C  CB  . VAL   B 2 86  ? -17.399 -8.163  -24.925 1.00 34.26  ? 95  VAL   B CB  1 
ATOM   948  C  CG1 . VAL   B 2 86  ? -17.259 -9.543  -24.277 1.00 34.16  ? 95  VAL   B CG1 1 
ATOM   949  C  CG2 . VAL   B 2 86  ? -16.099 -7.385  -24.822 1.00 34.08  ? 95  VAL   B CG2 1 
ATOM   950  N  N   . GLN   B 2 87  ? -18.678 -5.920  -26.620 1.00 34.70  ? 96  GLN   B N   1 
ATOM   951  C  CA  . GLN   B 2 87  ? -18.605 -4.562  -27.100 1.00 34.24  ? 96  GLN   B CA  1 
ATOM   952  C  C   . GLN   B 2 87  ? -18.474 -3.590  -25.943 1.00 33.18  ? 96  GLN   B C   1 
ATOM   953  O  O   . GLN   B 2 87  ? -19.244 -3.669  -24.999 1.00 32.07  ? 96  GLN   B O   1 
ATOM   954  C  CB  . GLN   B 2 87  ? -19.830 -4.206  -27.963 1.00 34.04  ? 96  GLN   B CB  1 
ATOM   955  C  CG  . GLN   B 2 87  ? -19.696 -4.870  -29.339 1.00 34.10  ? 96  GLN   B CG  1 
ATOM   956  C  CD  . GLN   B 2 87  ? -20.736 -4.456  -30.331 1.00 37.00  ? 96  GLN   B CD  1 
ATOM   957  O  OE1 . GLN   B 2 87  ? -21.629 -3.651  -30.070 1.00 36.53  ? 96  GLN   B OE1 1 
ATOM   958  N  NE2 . GLN   B 2 87  ? -20.620 -4.993  -31.561 1.00 38.55  ? 96  GLN   B NE2 1 
ATOM   959  N  N   . LEU   B 2 88  ? -17.545 -2.645  -26.040 1.00 32.99  ? 97  LEU   B N   1 
ATOM   960  C  CA  . LEU   B 2 88  ? -17.492 -1.542  -25.102 1.00 32.68  ? 97  LEU   B CA  1 
ATOM   961  C  C   . LEU   B 2 88  ? -18.395 -0.450  -25.714 1.00 33.43  ? 97  LEU   B C   1 
ATOM   962  O  O   . LEU   B 2 88  ? -18.180 -0.056  -26.870 1.00 34.22  ? 97  LEU   B O   1 
ATOM   963  C  CB  . LEU   B 2 88  ? -16.049 -1.019  -24.942 1.00 32.43  ? 97  LEU   B CB  1 
ATOM   964  C  CG  . LEU   B 2 88  ? -15.933 0.339   -24.250 1.00 34.46  ? 97  LEU   B CG  1 
ATOM   965  C  CD1 . LEU   B 2 88  ? -16.433 0.234   -22.766 1.00 33.03  ? 97  LEU   B CD1 1 
ATOM   966  C  CD2 . LEU   B 2 88  ? -14.522 0.884   -24.367 1.00 35.34  ? 97  LEU   B CD2 1 
ATOM   967  N  N   . LEU   B 2 89  ? -19.420 0.015   -24.986 1.00 32.05  ? 98  LEU   B N   1 
ATOM   968  C  CA  . LEU   B 2 89  ? -20.248 1.097   -25.476 1.00 32.37  ? 98  LEU   B CA  1 
ATOM   969  C  C   . LEU   B 2 89  ? -19.605 2.306   -24.866 1.00 33.03  ? 98  LEU   B C   1 
ATOM   970  O  O   . LEU   B 2 89  ? -19.980 2.734   -23.742 1.00 32.12  ? 98  LEU   B O   1 
ATOM   971  C  CB  . LEU   B 2 89  ? -21.689 0.909   -25.019 1.00 33.27  ? 98  LEU   B CB  1 
ATOM   972  C  CG  . LEU   B 2 89  ? -22.690 2.027   -25.384 1.00 34.96  ? 98  LEU   B CG  1 
ATOM   973  C  CD1 . LEU   B 2 89  ? -22.629 2.397   -26.895 1.00 36.77  ? 98  LEU   B CD1 1 
ATOM   974  C  CD2 . LEU   B 2 89  ? -24.096 1.644   -24.946 1.00 36.09  ? 98  LEU   B CD2 1 
ATOM   975  N  N   . ALA   B 2 90  ? -18.536 2.781   -25.539 1.00 32.16  ? 99  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 90  ? -17.776 3.919   -25.051 1.00 32.94  ? 99  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 90  ? -18.550 5.211   -25.161 1.00 32.47  ? 99  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 90  ? -19.057 5.544   -26.249 1.00 32.99  ? 99  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 90  ? -16.460 4.051   -25.794 1.00 33.40  ? 99  ALA   B CB  1 
ATOM   980  N  N   . VAL   B 2 91  ? -18.581 5.993   -24.068 1.00 30.75  ? 100 VAL   B N   1 
ATOM   981  C  CA  . VAL   B 2 91  ? -19.221 7.311   -24.091 1.00 30.57  ? 100 VAL   B CA  1 
ATOM   982  C  C   . VAL   B 2 91  ? -18.127 8.332   -23.710 1.00 32.22  ? 100 VAL   B C   1 
ATOM   983  O  O   . VAL   B 2 91  ? -17.998 8.695   -22.535 1.00 31.54  ? 100 VAL   B O   1 
ATOM   984  C  CB  . VAL   B 2 91  ? -20.448 7.400   -23.137 1.00 31.28  ? 100 VAL   B CB  1 
ATOM   985  C  CG1 . VAL   B 2 91  ? -21.116 8.777   -23.219 1.00 32.20  ? 100 VAL   B CG1 1 
ATOM   986  C  CG2 . VAL   B 2 91  ? -21.465 6.288   -23.408 1.00 31.34  ? 100 VAL   B CG2 1 
ATOM   987  N  N   . PRO   B 2 92  ? -17.263 8.728   -24.676 1.00 33.29  ? 101 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 92  ? -16.154 9.647   -24.354 1.00 33.56  ? 101 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 92  ? -16.615 11.086  -24.124 1.00 32.44  ? 101 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 92  ? -17.627 11.493  -24.669 1.00 33.29  ? 101 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 92  ? -15.259 9.572   -25.616 1.00 35.07  ? 101 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 92  ? -15.735 8.343   -26.372 1.00 35.72  ? 101 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 92  ? -17.213 8.312   -26.089 1.00 33.48  ? 101 PRO   B CD  1 
ATOM   994  N  N   . PRO   B 2 93  ? -15.867 11.866  -23.323 1.00 32.47  ? 102 PRO   B N   1 
ATOM   995  C  CA  . PRO   B 2 93  ? -16.268 13.260  -23.065 1.00 32.92  ? 102 PRO   B CA  1 
ATOM   996  C  C   . PRO   B 2 93  ? -16.441 14.090  -24.353 1.00 35.11  ? 102 PRO   B C   1 
ATOM   997  O  O   . PRO   B 2 93  ? -15.581 14.047  -25.226 1.00 35.31  ? 102 PRO   B O   1 
ATOM   998  C  CB  . PRO   B 2 93  ? -15.140 13.783  -22.170 1.00 33.25  ? 102 PRO   B CB  1 
ATOM   999  C  CG  . PRO   B 2 93  ? -14.586 12.523  -21.473 1.00 33.85  ? 102 PRO   B CG  1 
ATOM   1000 C  CD  . PRO   B 2 93  ? -14.627 11.509  -22.587 1.00 31.99  ? 102 PRO   B CD  1 
ATOM   1001 N  N   . GLY   B 2 94  ? -17.575 14.774  -24.486 1.00 35.71  ? 103 GLY   B N   1 
ATOM   1002 C  CA  . GLY   B 2 94  ? -17.907 15.608  -25.647 1.00 36.27  ? 103 GLY   B CA  1 
ATOM   1003 C  C   . GLY   B 2 94  ? -18.117 14.891  -26.976 1.00 36.59  ? 103 GLY   B C   1 
ATOM   1004 O  O   . GLY   B 2 94  ? -18.183 15.524  -28.040 1.00 37.10  ? 103 GLY   B O   1 
ATOM   1005 N  N   . GLU   B 2 95  ? -18.183 13.546  -26.940 1.00 36.51  ? 104 GLU   B N   1 
ATOM   1006 C  CA  . GLU   B 2 95  ? -18.316 12.727  -28.150 1.00 37.73  ? 104 GLU   B CA  1 
ATOM   1007 C  C   . GLU   B 2 95  ? -19.500 11.752  -28.055 1.00 37.75  ? 104 GLU   B C   1 
ATOM   1008 O  O   . GLU   B 2 95  ? -19.887 11.347  -26.960 1.00 36.23  ? 104 GLU   B O   1 
ATOM   1009 C  CB  . GLU   B 2 95  ? -16.982 11.957  -28.449 1.00 38.41  ? 104 GLU   B CB  1 
ATOM   1010 C  CG  . GLU   B 2 95  ? -15.755 12.867  -28.446 1.00 40.17  ? 104 GLU   B CG  1 
ATOM   1011 C  CD  . GLU   B 2 95  ? -14.385 12.236  -28.667 1.00 45.99  ? 104 GLU   B CD  1 
ATOM   1012 O  OE1 . GLU   B 2 95  ? -14.287 10.991  -28.595 1.00 42.98  ? 104 GLU   B OE1 1 
ATOM   1013 O  OE2 . GLU   B 2 95  ? -13.413 12.987  -28.933 1.00 47.32  ? 104 GLU   B OE2 1 
ATOM   1014 N  N   . ARG   B 2 96  ? -20.089 11.391  -29.216 1.00 38.25  ? 105 ARG   B N   1 
ATOM   1015 C  CA  . ARG   B 2 96  ? -21.241 10.481  -29.263 1.00 39.17  ? 105 ARG   B CA  1 
ATOM   1016 C  C   . ARG   B 2 96  ? -20.907 9.085   -28.756 1.00 37.69  ? 105 ARG   B C   1 
ATOM   1017 O  O   . ARG   B 2 96  ? -19.774 8.629   -28.937 1.00 36.93  ? 105 ARG   B O   1 
ATOM   1018 C  CB  . ARG   B 2 96  ? -21.705 10.337  -30.719 1.00 43.74  ? 105 ARG   B CB  1 
ATOM   1019 C  CG  . ARG   B 2 96  ? -23.154 9.854   -30.867 1.00 50.19  ? 105 ARG   B CG  1 
ATOM   1020 C  CD  . ARG   B 2 96  ? -23.855 10.440  -32.088 1.00 55.54  ? 105 ARG   B CD  1 
ATOM   1021 N  NE  . ARG   B 2 96  ? -23.043 10.369  -33.301 1.00 60.09  ? 105 ARG   B NE  1 
ATOM   1022 C  CZ  . ARG   B 2 96  ? -22.678 11.425  -34.025 1.00 64.35  ? 105 ARG   B CZ  1 
ATOM   1023 N  NH1 . ARG   B 2 96  ? -23.046 12.649  -33.661 1.00 64.30  ? 105 ARG   B NH1 1 
ATOM   1024 N  NH2 . ARG   B 2 96  ? -21.941 11.264  -35.119 1.00 64.70  ? 105 ARG   B NH2 1 
ATOM   1025 N  N   . ALA   B 2 97  ? -21.912 8.372   -28.166 1.00 37.51  ? 106 ALA   B N   1 
ATOM   1026 C  CA  . ALA   B 2 97  ? -21.754 6.976   -27.726 1.00 38.06  ? 106 ALA   B CA  1 
ATOM   1027 C  C   . ALA   B 2 97  ? -21.392 6.121   -28.958 1.00 39.18  ? 106 ALA   B C   1 
ATOM   1028 O  O   . ALA   B 2 97  ? -21.978 6.308   -30.029 1.00 39.72  ? 106 ALA   B O   1 
ATOM   1029 C  CB  . ALA   B 2 97  ? -23.044 6.466   -27.107 1.00 37.78  ? 106 ALA   B CB  1 
ATOM   1030 N  N   . LYS   B 2 98  ? -20.407 5.229   -28.819 1.00 39.05  ? 107 LYS   B N   1 
ATOM   1031 C  CA  . LYS   B 2 98  ? -19.908 4.429   -29.932 1.00 41.45  ? 107 LYS   B CA  1 
ATOM   1032 C  C   . LYS   B 2 98  ? -19.540 3.044   -29.442 1.00 40.65  ? 107 LYS   B C   1 
ATOM   1033 O  O   . LYS   B 2 98  ? -18.917 2.911   -28.369 1.00 39.34  ? 107 LYS   B O   1 
ATOM   1034 C  CB  . LYS   B 2 98  ? -18.684 5.162   -30.503 1.00 46.00  ? 107 LYS   B CB  1 
ATOM   1035 C  CG  . LYS   B 2 98  ? -18.124 4.685   -31.835 1.00 54.19  ? 107 LYS   B CG  1 
ATOM   1036 C  CD  . LYS   B 2 98  ? -16.686 5.257   -32.026 1.00 61.77  ? 107 LYS   B CD  1 
ATOM   1037 C  CE  . LYS   B 2 98  ? -15.862 5.321   -30.734 1.00 66.97  ? 107 LYS   B CE  1 
ATOM   1038 N  NZ  . LYS   B 2 98  ? -14.393 5.360   -30.982 1.00 69.87  ? 107 LYS   B NZ  1 
ATOM   1039 N  N   . ASN   B 2 99  ? -19.971 2.000   -30.189 1.00 39.84  ? 108 ASN   B N   1 
ATOM   1040 C  CA  . ASN   B 2 99  ? -19.691 0.604   -29.850 1.00 40.06  ? 108 ASN   B CA  1 
ATOM   1041 C  C   . ASN   B 2 99  ? -18.384 0.156   -30.458 1.00 40.12  ? 108 ASN   B C   1 
ATOM   1042 O  O   . ASN   B 2 99  ? -18.150 0.355   -31.663 1.00 40.15  ? 108 ASN   B O   1 
ATOM   1043 C  CB  . ASN   B 2 99  ? -20.796 -0.329  -30.356 1.00 40.60  ? 108 ASN   B CB  1 
ATOM   1044 C  CG  . ASN   B 2 99  ? -22.128 -0.140  -29.706 1.00 43.04  ? 108 ASN   B CG  1 
ATOM   1045 O  OD1 . ASN   B 2 99  ? -22.774 0.910   -29.858 1.00 44.81  ? 108 ASN   B OD1 1 
ATOM   1046 N  ND2 . ASN   B 2 99  ? -22.583 -1.149  -28.966 1.00 42.04  ? 108 ASN   B ND2 1 
ATOM   1047 N  N   . ILE   B 2 100 ? -17.539 -0.487  -29.646 1.00 39.18  ? 109 ILE   B N   1 
ATOM   1048 C  CA  . ILE   B 2 100 ? -16.266 -1.023  -30.087 1.00 39.05  ? 109 ILE   B CA  1 
ATOM   1049 C  C   . ILE   B 2 100 ? -16.221 -2.487  -29.734 1.00 39.15  ? 109 ILE   B C   1 
ATOM   1050 O  O   . ILE   B 2 100 ? -16.341 -2.842  -28.560 1.00 37.51  ? 109 ILE   B O   1 
ATOM   1051 C  CB  . ILE   B 2 100 ? -15.058 -0.284  -29.494 1.00 40.66  ? 109 ILE   B CB  1 
ATOM   1052 C  CG1 . ILE   B 2 100 ? -15.176 1.234   -29.678 1.00 42.67  ? 109 ILE   B CG1 1 
ATOM   1053 C  CG2 . ILE   B 2 100 ? -13.728 -0.850  -30.034 1.00 40.99  ? 109 ILE   B CG2 1 
ATOM   1054 C  CD1 . ILE   B 2 100 ? -14.937 1.745   -31.103 1.00 45.04  ? 109 ILE   B CD1 1 
ATOM   1055 N  N   . GLN   B 2 101 ? -16.050 -3.356  -30.735 1.00 39.83  ? 110 GLN   B N   1 
ATOM   1056 C  CA  . GLN   B 2 101 ? -16.003 -4.795  -30.501 1.00 40.63  ? 110 GLN   B CA  1 
ATOM   1057 C  C   . GLN   B 2 101 ? -14.588 -5.260  -30.266 1.00 41.92  ? 110 GLN   B C   1 
ATOM   1058 O  O   . GLN   B 2 101 ? -13.672 -4.778  -30.924 1.00 44.04  ? 110 GLN   B O   1 
ATOM   1059 C  CB  . GLN   B 2 101 ? -16.592 -5.532  -31.711 1.00 42.94  ? 110 GLN   B CB  1 
ATOM   1060 C  CG  . GLN   B 2 101 ? -16.825 -7.001  -31.446 1.00 42.32  ? 110 GLN   B CG  1 
ATOM   1061 C  CD  . GLN   B 2 101 ? -17.827 -7.549  -32.426 1.00 44.88  ? 110 GLN   B CD  1 
ATOM   1062 O  OE1 . GLN   B 2 101 ? -18.829 -6.902  -32.750 1.00 43.66  ? 110 GLN   B OE1 1 
ATOM   1063 N  NE2 . GLN   B 2 101 ? -17.572 -8.762  -32.912 1.00 47.60  ? 110 GLN   B NE2 1 
ATOM   1064 N  N   . THR   B 2 102 ? -14.388 -6.212  -29.330 1.00 39.41  ? 111 THR   B N   1 
ATOM   1065 C  CA  . THR   B 2 102 ? -13.061 -6.708  -28.968 1.00 38.51  ? 111 THR   B CA  1 
ATOM   1066 C  C   . THR   B 2 102 ? -13.128 -8.089  -28.326 1.00 38.17  ? 111 THR   B C   1 
ATOM   1067 O  O   . THR   B 2 102 ? -14.169 -8.460  -27.795 1.00 39.22  ? 111 THR   B O   1 
ATOM   1068 C  CB  . THR   B 2 102 ? -12.326 -5.684  -28.047 1.00 39.16  ? 111 THR   B CB  1 
ATOM   1069 O  OG1 . THR   B 2 102 ? -10.912 -5.963  -28.020 1.00 41.25  ? 111 THR   B OG1 1 
ATOM   1070 C  CG2 . THR   B 2 102 ? -12.894 -5.641  -26.602 1.00 39.16  ? 111 THR   B CG2 1 
ATOM   1071 N  N   . LEU   B 2 103 ? -12.026 -8.855  -28.360 1.00 36.80  ? 112 LEU   B N   1 
ATOM   1072 C  CA  . LEU   B 2 103 ? -11.972 -10.136 -27.660 1.00 36.74  ? 112 LEU   B CA  1 
ATOM   1073 C  C   . LEU   B 2 103 ? -11.220 -9.836  -26.389 1.00 37.84  ? 112 LEU   B C   1 
ATOM   1074 O  O   . LEU   B 2 103 ? -10.034 -9.475  -26.438 1.00 38.38  ? 112 LEU   B O   1 
ATOM   1075 C  CB  . LEU   B 2 103 ? -11.198 -11.251 -28.429 1.00 37.76  ? 112 LEU   B CB  1 
ATOM   1076 C  CG  . LEU   B 2 103 ? -11.173 -12.557 -27.647 1.00 41.43  ? 112 LEU   B CG  1 
ATOM   1077 C  CD1 . LEU   B 2 103 ? -12.502 -13.263 -27.720 1.00 41.86  ? 112 LEU   B CD1 1 
ATOM   1078 C  CD2 . LEU   B 2 103 ? -10.012 -13.464 -28.057 1.00 43.79  ? 112 LEU   B CD2 1 
ATOM   1079 N  N   . PRO   B 2 104 ? -11.868 -9.991  -25.218 1.00 37.60  ? 113 PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 2 104 ? -11.170 -9.652  -23.980 1.00 37.00  ? 113 PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 2 104 ? -9.972  -10.532 -23.742 1.00 37.36  ? 113 PRO   B C   1 
ATOM   1082 O  O   . PRO   B 2 104 ? -9.949  -11.700 -24.139 1.00 37.99  ? 113 PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 2 104 ? -12.214 -9.927  -22.881 1.00 38.10  ? 113 PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 2 104 ? -13.545 -9.742  -23.577 1.00 37.94  ? 113 PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 2 104 ? -13.274 -10.367 -24.964 1.00 36.90  ? 113 PRO   B CD  1 
ATOM   1086 N  N   . GLY   B 2 105 ? -8.996  -9.956  -23.068 1.00 37.80  ? 114 GLY   B N   1 
ATOM   1087 C  CA  . GLY   B 2 105 ? -7.868  -10.670 -22.506 1.00 38.29  ? 114 GLY   B CA  1 
ATOM   1088 C  C   . GLY   B 2 105 ? -8.240  -11.094 -21.081 1.00 38.91  ? 114 GLY   B C   1 
ATOM   1089 O  O   . GLY   B 2 105 ? -9.424  -11.061 -20.708 1.00 38.42  ? 114 GLY   B O   1 
ATOM   1090 N  N   . ILE   B 2 106 ? -7.250  -11.512 -20.253 1.00 39.51  ? 115 ILE   B N   1 
ATOM   1091 C  CA  . ILE   B 2 106 ? -7.538  -11.962 -18.879 1.00 40.77  ? 115 ILE   B CA  1 
ATOM   1092 C  C   . ILE   B 2 106 ? -6.649  -11.277 -17.859 1.00 40.47  ? 115 ILE   B C   1 
ATOM   1093 O  O   . ILE   B 2 106 ? -5.438  -11.222 -18.065 1.00 42.28  ? 115 ILE   B O   1 
ATOM   1094 C  CB  . ILE   B 2 106 ? -7.251  -13.504 -18.729 1.00 42.95  ? 115 ILE   B CB  1 
ATOM   1095 C  CG1 . ILE   B 2 106 ? -7.863  -14.351 -19.854 1.00 46.42  ? 115 ILE   B CG1 1 
ATOM   1096 C  CG2 . ILE   B 2 106 ? -7.679  -14.030 -17.352 1.00 43.83  ? 115 ILE   B CG2 1 
ATOM   1097 C  CD1 . ILE   B 2 106 ? -9.283  -14.300 -19.919 1.00 48.49  ? 115 ILE   B CD1 1 
ATOM   1098 N  N   . PHE   B 2 107 ? -7.207  -10.890 -16.703 1.00 38.46  ? 116 PHE   B N   1 
ATOM   1099 C  CA  . PHE   B 2 107 ? -6.443  -10.497 -15.514 1.00 38.22  ? 116 PHE   B CA  1 
ATOM   1100 C  C   . PHE   B 2 107 ? -6.399  -11.775 -14.675 1.00 40.74  ? 116 PHE   B C   1 
ATOM   1101 O  O   . PHE   B 2 107 ? -7.447  -12.230 -14.222 1.00 41.20  ? 116 PHE   B O   1 
ATOM   1102 C  CB  . PHE   B 2 107 ? -7.168  -9.400  -14.700 1.00 36.27  ? 116 PHE   B CB  1 
ATOM   1103 C  CG  . PHE   B 2 107 ? -6.901  -7.965  -15.096 1.00 35.55  ? 116 PHE   B CG  1 
ATOM   1104 C  CD1 . PHE   B 2 107 ? -6.153  -7.662  -16.228 1.00 36.03  ? 116 PHE   B CD1 1 
ATOM   1105 C  CD2 . PHE   B 2 107 ? -7.452  -6.916  -14.376 1.00 35.26  ? 116 PHE   B CD2 1 
ATOM   1106 C  CE1 . PHE   B 2 107 ? -5.969  -6.340  -16.629 1.00 36.48  ? 116 PHE   B CE1 1 
ATOM   1107 C  CE2 . PHE   B 2 107 ? -7.252  -5.599  -14.772 1.00 34.95  ? 116 PHE   B CE2 1 
ATOM   1108 C  CZ  . PHE   B 2 107 ? -6.494  -5.317  -15.876 1.00 35.76  ? 116 PHE   B CZ  1 
ATOM   1109 N  N   . LYS   B 2 108 ? -5.197  -12.330 -14.410 1.00 41.90  ? 117 LYS   B N   1 
ATOM   1110 C  CA  . LYS   B 2 108 ? -5.036  -13.509 -13.559 1.00 43.15  ? 117 LYS   B CA  1 
ATOM   1111 C  C   . LYS   B 2 108 ? -4.698  -13.008 -12.165 1.00 43.04  ? 117 LYS   B C   1 
ATOM   1112 O  O   . LYS   B 2 108 ? -3.702  -12.299 -12.006 1.00 43.16  ? 117 LYS   B O   1 
ATOM   1113 C  CB  . LYS   B 2 108 ? -3.879  -14.412 -14.052 1.00 46.25  ? 117 LYS   B CB  1 
ATOM   1114 C  CG  . LYS   B 2 108 ? -4.096  -15.038 -15.417 1.00 53.60  ? 117 LYS   B CG  1 
ATOM   1115 C  CD  . LYS   B 2 108 ? -2.770  -15.581 -15.959 1.00 60.29  ? 117 LYS   B CD  1 
ATOM   1116 C  CE  . LYS   B 2 108 ? -2.928  -16.608 -17.054 1.00 66.05  ? 117 LYS   B CE  1 
ATOM   1117 N  NZ  . LYS   B 2 108 ? -1.808  -17.600 -17.039 1.00 69.06  ? 117 LYS   B NZ  1 
ATOM   1118 N  N   . THR   B 2 109 ? -5.524  -13.337 -11.165 1.00 42.33  ? 118 THR   B N   1 
ATOM   1119 C  CA  . THR   B 2 109 ? -5.267  -12.882 -9.795  1.00 42.92  ? 118 THR   B CA  1 
ATOM   1120 C  C   . THR   B 2 109 ? -5.201  -14.080 -8.830  1.00 44.07  ? 118 THR   B C   1 
ATOM   1121 O  O   . THR   B 2 109 ? -5.666  -15.171 -9.175  1.00 44.02  ? 118 THR   B O   1 
ATOM   1122 C  CB  . THR   B 2 109 ? -6.331  -11.825 -9.326  1.00 42.43  ? 118 THR   B CB  1 
ATOM   1123 O  OG1 . THR   B 2 109 ? -7.499  -12.475 -8.820  1.00 42.58  ? 118 THR   B OG1 1 
ATOM   1124 C  CG2 . THR   B 2 109 ? -6.707  -10.814 -10.405 1.00 41.95  ? 118 THR   B CG2 1 
ATOM   1125 N  N   . LYS   B 2 110 ? -4.707  -13.851 -7.601  1.00 44.86  ? 119 LYS   B N   1 
ATOM   1126 C  CA  . LYS   B 2 110 ? -4.673  -14.899 -6.584  1.00 46.48  ? 119 LYS   B CA  1 
ATOM   1127 C  C   . LYS   B 2 110 ? -6.095  -15.365 -6.183  1.00 47.62  ? 119 LYS   B C   1 
ATOM   1128 O  O   . LYS   B 2 110 ? -6.244  -16.427 -5.581  1.00 48.84  ? 119 LYS   B O   1 
ATOM   1129 C  CB  . LYS   B 2 110 ? -3.901  -14.416 -5.347  1.00 48.04  ? 119 LYS   B CB  1 
ATOM   1130 C  CG  . LYS   B 2 110 ? -4.605  -13.290 -4.588  1.00 51.92  ? 119 LYS   B CG  1 
ATOM   1131 C  CD  . LYS   B 2 110 ? -3.907  -13.033 -3.257  1.00 56.03  ? 119 LYS   B CD  1 
ATOM   1132 C  CE  . LYS   B 2 110 ? -4.874  -12.755 -2.130  1.00 59.57  ? 119 LYS   B CE  1 
ATOM   1133 N  NZ  . LYS   B 2 110 ? -5.342  -11.350 -2.142  1.00 61.86  ? 119 LYS   B NZ  1 
ATOM   1134 N  N   . ASP   B 2 111 ? -7.121  -14.567 -6.492  1.00 46.84  ? 120 ASP   B N   1 
ATOM   1135 C  CA  . ASP   B 2 111 ? -8.504  -14.883 -6.176  1.00 47.34  ? 120 ASP   B CA  1 
ATOM   1136 C  C   . ASP   B 2 111 ? -9.339  -15.247 -7.408  1.00 47.39  ? 120 ASP   B C   1 
ATOM   1137 O  O   . ASP   B 2 111 ? -10.564 -15.203 -7.333  1.00 48.15  ? 120 ASP   B O   1 
ATOM   1138 C  CB  . ASP   B 2 111 ? -9.151  -13.709 -5.432  1.00 48.96  ? 120 ASP   B CB  1 
ATOM   1139 C  CG  . ASP   B 2 111 ? -8.512  -13.472 -4.082  1.00 52.92  ? 120 ASP   B CG  1 
ATOM   1140 O  OD1 . ASP   B 2 111 ? -8.214  -14.465 -3.386  1.00 53.59  ? 120 ASP   B OD1 1 
ATOM   1141 O  OD2 . ASP   B 2 111 ? -8.301  -12.302 -3.728  1.00 54.89  ? 120 ASP   B OD2 1 
ATOM   1142 N  N   . GLY   B 2 112 ? -8.695  -15.598 -8.516  1.00 46.42  ? 121 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 112 ? -9.407  -15.948 -9.732  1.00 46.16  ? 121 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 112 ? -9.119  -15.037 -10.915 1.00 45.37  ? 121 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 112 ? -8.433  -14.012 -10.793 1.00 45.33  ? 121 GLY   B O   1 
ATOM   1146 N  N   . ASP   B 2 113 ? -9.640  -15.425 -12.070 1.00 44.07  ? 122 ASP   B N   1 
ATOM   1147 C  CA  . ASP   B 2 113 ? -9.449  -14.721 -13.333 1.00 43.32  ? 122 ASP   B CA  1 
ATOM   1148 C  C   . ASP   B 2 113 ? -10.621 -13.773 -13.628 1.00 41.95  ? 122 ASP   B C   1 
ATOM   1149 O  O   . ASP   B 2 113 ? -11.766 -14.073 -13.296 1.00 42.22  ? 122 ASP   B O   1 
ATOM   1150 C  CB  . ASP   B 2 113 ? -9.287  -15.737 -14.474 1.00 45.32  ? 122 ASP   B CB  1 
ATOM   1151 C  CG  . ASP   B 2 113 ? -7.963  -16.488 -14.491 1.00 52.14  ? 122 ASP   B CG  1 
ATOM   1152 O  OD1 . ASP   B 2 113 ? -7.134  -16.244 -13.609 1.00 54.04  ? 122 ASP   B OD1 1 
ATOM   1153 O  OD2 . ASP   B 2 113 ? -7.761  -17.310 -15.402 1.00 55.74  ? 122 ASP   B OD2 1 
ATOM   1154 N  N   . ILE   B 2 114 ? -10.319 -12.622 -14.251 1.00 40.15  ? 123 ILE   B N   1 
ATOM   1155 C  CA  . ILE   B 2 114 ? -11.297 -11.605 -14.607 1.00 39.83  ? 123 ILE   B CA  1 
ATOM   1156 C  C   . ILE   B 2 114 ? -11.053 -11.244 -16.087 1.00 37.76  ? 123 ILE   B C   1 
ATOM   1157 O  O   . ILE   B 2 114 ? -9.900  -11.121 -16.488 1.00 36.87  ? 123 ILE   B O   1 
ATOM   1158 C  CB  . ILE   B 2 114 ? -11.084 -10.336 -13.696 1.00 41.29  ? 123 ILE   B CB  1 
ATOM   1159 C  CG1 . ILE   B 2 114 ? -10.941 -10.693 -12.193 1.00 44.03  ? 123 ILE   B CG1 1 
ATOM   1160 C  CG2 . ILE   B 2 114 ? -12.175 -9.298  -13.915 1.00 42.67  ? 123 ILE   B CG2 1 
ATOM   1161 C  CD1 . ILE   B 2 114 ? -10.430 -9.519  -11.292 1.00 46.08  ? 123 ILE   B CD1 1 
ATOM   1162 N  N   . GLY   B 2 115 ? -12.109 -11.022 -16.876 1.00 36.65  ? 124 GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 2 115 ? -11.930 -10.566 -18.255 1.00 35.81  ? 124 GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 2 115 ? -11.343 -9.162  -18.257 1.00 34.82  ? 124 GLY   B C   1 
ATOM   1165 O  O   . GLY   B 2 115 ? -11.523 -8.412  -17.293 1.00 33.76  ? 124 GLY   B O   1 
ATOM   1166 N  N   . ALA   B 2 116 ? -10.603 -8.799  -19.306 1.00 34.38  ? 125 ALA   B N   1 
ATOM   1167 C  CA  . ALA   B 2 116 ? -10.001 -7.473  -19.398 1.00 34.78  ? 125 ALA   B CA  1 
ATOM   1168 C  C   . ALA   B 2 116 ? -10.077 -6.955  -20.837 1.00 36.10  ? 125 ALA   B C   1 
ATOM   1169 O  O   . ALA   B 2 116 ? -9.880  -7.737  -21.760 1.00 37.05  ? 125 ALA   B O   1 
ATOM   1170 C  CB  . ALA   B 2 116 ? -8.560  -7.531  -18.945 1.00 35.22  ? 125 ALA   B CB  1 
ATOM   1171 N  N   . VAL   B 2 117 ? -10.340 -5.644  -21.025 1.00 35.04  ? 126 VAL   B N   1 
ATOM   1172 C  CA  A VAL   B 2 117 ? -10.412 -5.087  -22.369 0.50 35.88  ? 126 VAL   B CA  1 
ATOM   1173 C  CA  B VAL   B 2 117 ? -10.499 -4.991  -22.323 0.50 36.51  ? 126 VAL   B CA  1 
ATOM   1174 C  C   . VAL   B 2 117 ? -9.300  -4.058  -22.624 1.00 36.86  ? 126 VAL   B C   1 
ATOM   1175 O  O   . VAL   B 2 117 ? -9.028  -3.138  -21.844 1.00 36.18  ? 126 VAL   B O   1 
ATOM   1176 C  CB  A VAL   B 2 117 ? -11.804 -4.578  -22.758 0.50 36.04  ? 126 VAL   B CB  1 
ATOM   1177 C  CB  B VAL   B 2 117 ? -11.889 -4.295  -22.313 0.50 38.11  ? 126 VAL   B CB  1 
ATOM   1178 C  CG1 A VAL   B 2 117 ? -12.832 -5.701  -22.636 0.50 36.64  ? 126 VAL   B CG1 1 
ATOM   1179 C  CG1 B VAL   B 2 117 ? -11.941 -3.030  -23.157 0.50 39.10  ? 126 VAL   B CG1 1 
ATOM   1180 C  CG2 A VAL   B 2 117 ? -12.211 -3.357  -21.939 0.50 35.67  ? 126 VAL   B CG2 1 
ATOM   1181 C  CG2 B VAL   B 2 117 ? -12.988 -5.277  -22.712 0.50 39.03  ? 126 VAL   B CG2 1 
ATOM   1182 N  N   . ALA   B 2 118 ? -8.546  -4.320  -23.710 1.00 36.98  ? 127 ALA   B N   1 
ATOM   1183 C  CA  . ALA   B 2 118 ? -7.391  -3.523  -24.049 1.00 38.81  ? 127 ALA   B CA  1 
ATOM   1184 C  C   . ALA   B 2 118 ? -7.747  -2.429  -25.036 1.00 40.52  ? 127 ALA   B C   1 
ATOM   1185 O  O   . ALA   B 2 118 ? -7.354  -2.457  -26.211 1.00 41.13  ? 127 ALA   B O   1 
ATOM   1186 C  CB  . ALA   B 2 118 ? -6.288  -4.418  -24.596 1.00 39.72  ? 127 ALA   B CB  1 
ATOM   1187 N  N   . LEU   B 2 119 ? -8.544  -1.461  -24.543 1.00 40.16  ? 128 LEU   B N   1 
ATOM   1188 C  CA  . LEU   B 2 119 ? -9.003  -0.290  -25.273 1.00 40.74  ? 128 LEU   B CA  1 
ATOM   1189 C  C   . LEU   B 2 119 ? -8.676  0.949   -24.420 1.00 42.00  ? 128 LEU   B C   1 
ATOM   1190 O  O   . LEU   B 2 119 ? -8.885  0.927   -23.192 1.00 42.14  ? 128 LEU   B O   1 
ATOM   1191 C  CB  . LEU   B 2 119 ? -10.526 -0.374  -25.538 1.00 40.40  ? 128 LEU   B CB  1 
ATOM   1192 C  CG  . LEU   B 2 119 ? -10.966 -1.531  -26.425 1.00 42.06  ? 128 LEU   B CG  1 
ATOM   1193 C  CD1 . LEU   B 2 119 ? -12.470 -1.760  -26.348 1.00 42.07  ? 128 LEU   B CD1 1 
ATOM   1194 C  CD2 . LEU   B 2 119 ? -10.468 -1.350  -27.867 1.00 43.39  ? 128 LEU   B CD2 1 
ATOM   1195 N  N   . ASP   B 2 120 ? -8.162  2.014   -25.059 1.00 42.43  ? 129 ASP   B N   1 
ATOM   1196 C  CA  . ASP   B 2 120 ? -7.745  3.203   -24.320 1.00 43.82  ? 129 ASP   B CA  1 
ATOM   1197 C  C   . ASP   B 2 120 ? -8.568  4.442   -24.651 1.00 43.15  ? 129 ASP   B C   1 
ATOM   1198 O  O   . ASP   B 2 120 ? -8.491  4.972   -25.763 1.00 43.91  ? 129 ASP   B O   1 
ATOM   1199 C  CB  . ASP   B 2 120 ? -6.233  3.473   -24.535 1.00 47.35  ? 129 ASP   B CB  1 
ATOM   1200 C  CG  . ASP   B 2 120 ? -5.605  4.427   -23.522 1.00 53.60  ? 129 ASP   B CG  1 
ATOM   1201 O  OD1 . ASP   B 2 120 ? -6.331  4.910   -22.625 1.00 55.40  ? 129 ASP   B OD1 1 
ATOM   1202 O  OD2 . ASP   B 2 120 ? -4.388  4.690   -23.626 1.00 56.25  ? 129 ASP   B OD2 1 
ATOM   1203 N  N   . TYR   B 2 121 ? -9.324  4.934   -23.663 1.00 41.06  ? 130 TYR   B N   1 
ATOM   1204 C  CA  . TYR   B 2 121 ? -10.141 6.125   -23.815 1.00 39.96  ? 130 TYR   B CA  1 
ATOM   1205 C  C   . TYR   B 2 121 ? -9.814  7.147   -22.691 1.00 38.55  ? 130 TYR   B C   1 
ATOM   1206 O  O   . TYR   B 2 121 ? -9.191  6.770   -21.693 1.00 38.67  ? 130 TYR   B O   1 
ATOM   1207 C  CB  . TYR   B 2 121 ? -11.634 5.722   -23.746 1.00 40.40  ? 130 TYR   B CB  1 
ATOM   1208 C  CG  . TYR   B 2 121 ? -12.154 5.191   -25.063 1.00 40.81  ? 130 TYR   B CG  1 
ATOM   1209 C  CD1 . TYR   B 2 121 ? -12.484 6.052   -26.100 1.00 42.21  ? 130 TYR   B CD1 1 
ATOM   1210 C  CD2 . TYR   B 2 121 ? -12.270 3.826   -25.288 1.00 41.81  ? 130 TYR   B CD2 1 
ATOM   1211 C  CE1 . TYR   B 2 121 ? -12.928 5.568   -27.322 1.00 43.95  ? 130 TYR   B CE1 1 
ATOM   1212 C  CE2 . TYR   B 2 121 ? -12.744 3.331   -26.495 1.00 43.12  ? 130 TYR   B CE2 1 
ATOM   1213 C  CZ  . TYR   B 2 121 ? -13.049 4.206   -27.520 1.00 45.31  ? 130 TYR   B CZ  1 
ATOM   1214 O  OH  . TYR   B 2 121 ? -13.485 3.749   -28.742 1.00 48.50  ? 130 TYR   B OH  1 
ATOM   1215 N  N   . PRO   B 2 122 ? -10.230 8.431   -22.821 1.00 37.51  ? 131 PRO   B N   1 
ATOM   1216 C  CA  . PRO   B 2 122 ? -9.975  9.400   -21.736 1.00 36.67  ? 131 PRO   B CA  1 
ATOM   1217 C  C   . PRO   B 2 122 ? -10.578 8.923   -20.396 1.00 34.83  ? 131 PRO   B C   1 
ATOM   1218 O  O   . PRO   B 2 122 ? -11.582 8.226   -20.424 1.00 34.31  ? 131 PRO   B O   1 
ATOM   1219 C  CB  . PRO   B 2 122 ? -10.708 10.657  -22.222 1.00 38.17  ? 131 PRO   B CB  1 
ATOM   1220 C  CG  . PRO   B 2 122 ? -10.695 10.530  -23.727 1.00 39.01  ? 131 PRO   B CG  1 
ATOM   1221 C  CD  . PRO   B 2 122 ? -10.916 9.073   -23.967 1.00 37.42  ? 131 PRO   B CD  1 
ATOM   1222 N  N   . ALA   B 2 123 ? -9.967  9.278   -19.246 1.00 33.63  ? 132 ALA   B N   1 
ATOM   1223 C  CA  . ALA   B 2 123 ? -10.441 8.912   -17.894 1.00 33.07  ? 132 ALA   B CA  1 
ATOM   1224 C  C   . ALA   B 2 123 ? -11.965 9.170   -17.658 1.00 30.95  ? 132 ALA   B C   1 
ATOM   1225 O  O   . ALA   B 2 123 ? -12.634 8.398   -16.950 1.00 30.25  ? 132 ALA   B O   1 
ATOM   1226 C  CB  . ALA   B 2 123 ? -9.620  9.664   -16.837 1.00 34.06  ? 132 ALA   B CB  1 
ATOM   1227 N  N   . GLY   B 2 124 ? -12.491 10.231  -18.269 1.00 30.64  ? 133 GLY   B N   1 
ATOM   1228 C  CA  . GLY   B 2 124 ? -13.907 10.585  -18.183 1.00 30.81  ? 133 GLY   B CA  1 
ATOM   1229 C  C   . GLY   B 2 124 ? -14.863 9.593   -18.834 1.00 29.08  ? 133 GLY   B C   1 
ATOM   1230 O  O   . GLY   B 2 124 ? -16.091 9.725   -18.710 1.00 29.16  ? 133 GLY   B O   1 
ATOM   1231 N  N   . THR   B 2 125 ? -14.314 8.567   -19.499 1.00 27.34  ? 134 THR   B N   1 
ATOM   1232 C  CA  . THR   B 2 125 ? -15.103 7.479   -20.100 1.00 27.45  ? 134 THR   B CA  1 
ATOM   1233 C  C   . THR   B 2 125 ? -15.372 6.368   -19.042 1.00 26.85  ? 134 THR   B C   1 
ATOM   1234 O  O   . THR   B 2 125 ? -16.150 5.446   -19.292 1.00 26.98  ? 134 THR   B O   1 
ATOM   1235 C  CB  . THR   B 2 125 ? -14.373 6.929   -21.353 1.00 29.91  ? 134 THR   B CB  1 
ATOM   1236 O  OG1 . THR   B 2 125 ? -13.901 8.005   -22.172 1.00 30.29  ? 134 THR   B OG1 1 
ATOM   1237 C  CG2 . THR   B 2 125 ? -15.224 6.003   -22.181 1.00 30.96  ? 134 THR   B CG2 1 
ATOM   1238 N  N   . SER   B 2 126 ? -14.711 6.442   -17.851 1.00 24.95  ? 135 SER   B N   1 
ATOM   1239 C  CA  . SER   B 2 126 ? -14.900 5.426   -16.761 1.00 25.61  ? 135 SER   B CA  1 
ATOM   1240 C  C   . SER   B 2 126 ? -16.386 5.214   -16.458 1.00 25.51  ? 135 SER   B C   1 
ATOM   1241 O  O   . SER   B 2 126 ? -17.100 6.187   -16.316 1.00 26.09  ? 135 SER   B O   1 
ATOM   1242 C  CB  . SER   B 2 126 ? -14.266 5.921   -15.470 1.00 28.35  ? 135 SER   B CB  1 
ATOM   1243 O  OG  . SER   B 2 126 ? -12.853 5.982   -15.542 1.00 31.64  ? 135 SER   B OG  1 
ATOM   1244 N  N   . GLY   B 2 127 ? -16.827 3.965   -16.348 1.00 24.22  ? 136 GLY   B N   1 
ATOM   1245 C  CA  . GLY   B 2 127 ? -18.219 3.627   -16.090 1.00 24.80  ? 136 GLY   B CA  1 
ATOM   1246 C  C   . GLY   B 2 127 ? -18.973 3.207   -17.357 1.00 24.94  ? 136 GLY   B C   1 
ATOM   1247 O  O   . GLY   B 2 127 ? -20.118 2.743   -17.280 1.00 24.85  ? 136 GLY   B O   1 
ATOM   1248 N  N   . SER   B 2 128 ? -18.341 3.355   -18.575 1.00 24.54  ? 137 SER   B N   1 
ATOM   1249 C  CA  . SER   B 2 128 ? -19.004 2.887   -19.792 1.00 25.02  ? 137 SER   B CA  1 
ATOM   1250 C  C   . SER   B 2 128 ? -19.236 1.381   -19.697 1.00 25.39  ? 137 SER   B C   1 
ATOM   1251 O  O   . SER   B 2 128 ? -18.365 0.649   -19.236 1.00 25.97  ? 137 SER   B O   1 
ATOM   1252 C  CB  . SER   B 2 128 ? -18.127 3.186   -21.022 1.00 26.60  ? 137 SER   B CB  1 
ATOM   1253 O  OG  . SER   B 2 128 ? -18.147 4.593   -21.213 1.00 29.96  ? 137 SER   B OG  1 
ATOM   1254 N  N   . PRO   B 2 129 ? -20.417 0.915   -20.135 1.00 26.86  ? 138 PRO   B N   1 
ATOM   1255 C  CA  . PRO   B 2 129 ? -20.713 -0.507  -20.012 1.00 27.22  ? 138 PRO   B CA  1 
ATOM   1256 C  C   . PRO   B 2 129 ? -20.091 -1.350  -21.107 1.00 28.27  ? 138 PRO   B C   1 
ATOM   1257 O  O   . PRO   B 2 129 ? -19.993 -0.924  -22.267 1.00 28.17  ? 138 PRO   B O   1 
ATOM   1258 C  CB  . PRO   B 2 129 ? -22.244 -0.544  -20.128 1.00 28.12  ? 138 PRO   B CB  1 
ATOM   1259 C  CG  . PRO   B 2 129 ? -22.581 0.610   -21.029 1.00 29.18  ? 138 PRO   B CG  1 
ATOM   1260 C  CD  . PRO   B 2 129 ? -21.577 1.680   -20.650 1.00 27.89  ? 138 PRO   B CD  1 
ATOM   1261 N  N   . ILE   B 2 130 ? -19.741 -2.582  -20.726 1.00 27.31  ? 139 ILE   B N   1 
ATOM   1262 C  CA  . ILE   B 2 130 ? -19.242 -3.620  -21.645 1.00 29.64  ? 139 ILE   B CA  1 
ATOM   1263 C  C   . ILE   B 2 130 ? -20.412 -4.608  -21.781 1.00 30.05  ? 139 ILE   B C   1 
ATOM   1264 O  O   . ILE   B 2 130 ? -20.998 -4.980  -20.765 1.00 29.87  ? 139 ILE   B O   1 
ATOM   1265 C  CB  . ILE   B 2 130 ? -18.001 -4.284  -21.033 1.00 31.14  ? 139 ILE   B CB  1 
ATOM   1266 C  CG1 . ILE   B 2 130 ? -16.899 -3.235  -20.847 1.00 34.02  ? 139 ILE   B CG1 1 
ATOM   1267 C  CG2 . ILE   B 2 130 ? -17.508 -5.465  -21.887 1.00 31.27  ? 139 ILE   B CG2 1 
ATOM   1268 C  CD1 . ILE   B 2 130 ? -15.802 -3.651  -19.896 1.00 35.81  ? 139 ILE   B CD1 1 
ATOM   1269 N  N   . LEU   B 2 131 ? -20.802 -4.956  -23.030 1.00 31.25  ? 140 LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 131 ? -21.965 -5.790  -23.313 1.00 33.17  ? 140 LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 131 ? -21.636 -7.129  -23.981 1.00 33.60  ? 140 LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 131 ? -20.669 -7.236  -24.740 1.00 33.79  ? 140 LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 131 ? -22.912 -5.061  -24.323 1.00 35.52  ? 140 LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 131 ? -22.987 -3.537  -24.293 1.00 38.76  ? 140 LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 131 ? -23.922 -3.042  -25.371 1.00 40.43  ? 140 LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 131 ? -23.434 -3.041  -22.918 1.00 39.94  ? 140 LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 132 ? -22.501 -8.118  -23.766 1.00 33.40  ? 141 ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 132 ? -22.412 -9.364  -24.505 1.00 35.21  ? 141 ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 132 ? -23.297 -9.238  -25.779 1.00 37.33  ? 141 ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 132 ? -23.972 -8.206  -25.970 1.00 36.38  ? 141 ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 132 ? -22.778 -10.579 -23.640 1.00 35.86  ? 141 ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 132 ? -24.194 -10.613 -23.103 1.00 37.72  ? 141 ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 132 ? -25.059 -9.916  -23.662 1.00 38.87  ? 141 ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 132 ? -24.439 -11.366 -22.155 1.00 38.79  ? 141 ASP   B OD2 1 
ATOM   1285 N  N   . LYS   B 2 133 ? -23.342 -10.297 -26.617 1.00 39.42  ? 142 LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 2 133 ? -24.136 -10.275 -27.861 1.00 41.62  ? 142 LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 2 133 ? -25.634 -10.152 -27.659 1.00 42.91  ? 142 LYS   B C   1 
ATOM   1288 O  O   . LYS   B 2 133 ? -26.369 -9.834  -28.615 1.00 43.86  ? 142 LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 2 133 ? -23.808 -11.522 -28.728 1.00 44.97  ? 142 LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 2 133 ? -22.359 -11.555 -29.129 1.00 52.67  ? 142 LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 2 133 ? -21.947 -12.880 -29.789 1.00 59.67  ? 142 LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 2 133 ? -20.466 -13.135 -29.586 1.00 64.79  ? 142 LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 2 133 ? -20.068 -14.541 -29.927 1.00 68.39  ? 142 LYS   B NZ  1 
ATOM   1294 N  N   . CYS   B 2 134 ? -26.106 -10.410 -26.429 1.00 42.92  ? 143 CYS   B N   1 
ATOM   1295 C  CA  . CYS   B 2 134 ? -27.513 -10.221 -26.087 1.00 43.66  ? 143 CYS   B CA  1 
ATOM   1296 C  C   . CYS   B 2 134 ? -27.825 -8.799  -25.590 1.00 43.06  ? 143 CYS   B C   1 
ATOM   1297 O  O   . CYS   B 2 134 ? -28.971 -8.511  -25.251 1.00 44.00  ? 143 CYS   B O   1 
ATOM   1298 C  CB  . CYS   B 2 134 ? -27.975 -11.264 -25.082 1.00 46.01  ? 143 CYS   B CB  1 
ATOM   1299 S  SG  . CYS   B 2 134 ? -27.919 -12.959 -25.707 1.00 53.97  ? 143 CYS   B SG  1 
ATOM   1300 N  N   . GLY   B 2 135 ? -26.824 -7.919  -25.544 1.00 41.61  ? 144 GLY   B N   1 
ATOM   1301 C  CA  . GLY   B 2 135 ? -27.027 -6.551  -25.072 1.00 39.69  ? 144 GLY   B CA  1 
ATOM   1302 C  C   . GLY   B 2 135 ? -26.990 -6.423  -23.556 1.00 38.66  ? 144 GLY   B C   1 
ATOM   1303 O  O   . GLY   B 2 135 ? -27.224 -5.334  -23.022 1.00 39.38  ? 144 GLY   B O   1 
ATOM   1304 N  N   . ARG   B 2 136 ? -26.667 -7.524  -22.837 1.00 36.04  ? 145 ARG   B N   1 
ATOM   1305 C  CA  . ARG   B 2 136 ? -26.607 -7.471  -21.367 1.00 35.08  ? 145 ARG   B CA  1 
ATOM   1306 C  C   . ARG   B 2 136 ? -25.280 -6.889  -20.885 1.00 32.44  ? 145 ARG   B C   1 
ATOM   1307 O  O   . ARG   B 2 136 ? -24.222 -7.225  -21.428 1.00 31.41  ? 145 ARG   B O   1 
ATOM   1308 C  CB  . ARG   B 2 136 ? -26.810 -8.876  -20.786 1.00 37.84  ? 145 ARG   B CB  1 
ATOM   1309 C  CG  . ARG   B 2 136 ? -28.217 -9.429  -21.041 1.00 42.65  ? 145 ARG   B CG  1 
ATOM   1310 C  CD  . ARG   B 2 136 ? -28.339 -10.829 -20.474 1.00 49.29  ? 145 ARG   B CD  1 
ATOM   1311 N  NE  . ARG   B 2 136 ? -27.625 -11.804 -21.296 1.00 56.59  ? 145 ARG   B NE  1 
ATOM   1312 C  CZ  . ARG   B 2 136 ? -27.316 -13.038 -20.909 1.00 61.61  ? 145 ARG   B CZ  1 
ATOM   1313 N  NH1 . ARG   B 2 136 ? -27.589 -13.443 -19.671 1.00 62.55  ? 145 ARG   B NH1 1 
ATOM   1314 N  NH2 . ARG   B 2 136 ? -26.694 -13.864 -21.741 1.00 61.98  ? 145 ARG   B NH2 1 
ATOM   1315 N  N   . VAL   B 2 137 ? -25.328 -6.070  -19.804 1.00 29.47  ? 146 VAL   B N   1 
ATOM   1316 C  CA  . VAL   B 2 137 ? -24.133 -5.457  -19.291 1.00 28.72  ? 146 VAL   B CA  1 
ATOM   1317 C  C   . VAL   B 2 137 ? -23.366 -6.476  -18.471 1.00 29.22  ? 146 VAL   B C   1 
ATOM   1318 O  O   . VAL   B 2 137 ? -23.852 -6.897  -17.426 1.00 29.12  ? 146 VAL   B O   1 
ATOM   1319 C  CB  . VAL   B 2 137 ? -24.451 -4.158  -18.486 1.00 28.90  ? 146 VAL   B CB  1 
ATOM   1320 C  CG1 . VAL   B 2 137 ? -23.167 -3.551  -17.909 1.00 28.60  ? 146 VAL   B CG1 1 
ATOM   1321 C  CG2 . VAL   B 2 137 ? -25.176 -3.143  -19.391 1.00 29.48  ? 146 VAL   B CG2 1 
ATOM   1322 N  N   . ILE   B 2 138 ? -22.174 -6.863  -18.931 1.00 29.41  ? 147 ILE   B N   1 
ATOM   1323 C  CA  . ILE   B 2 138 ? -21.318 -7.834  -18.221 1.00 29.74  ? 147 ILE   B CA  1 
ATOM   1324 C  C   . ILE   B 2 138 ? -20.292 -7.180  -17.273 1.00 27.81  ? 147 ILE   B C   1 
ATOM   1325 O  O   . ILE   B 2 138 ? -19.589 -7.895  -16.545 1.00 27.88  ? 147 ILE   B O   1 
ATOM   1326 C  CB  . ILE   B 2 138 ? -20.622 -8.823  -19.223 1.00 31.11  ? 147 ILE   B CB  1 
ATOM   1327 C  CG1 . ILE   B 2 138 ? -19.812 -8.067  -20.301 1.00 32.21  ? 147 ILE   B CG1 1 
ATOM   1328 C  CG2 . ILE   B 2 138 ? -21.634 -9.736  -19.868 1.00 31.89  ? 147 ILE   B CG2 1 
ATOM   1329 C  CD1 . ILE   B 2 138 ? -18.815 -8.983  -21.102 1.00 34.21  ? 147 ILE   B CD1 1 
ATOM   1330 N  N   . GLY   B 2 139 ? -20.272 -5.845  -17.227 1.00 27.25  ? 148 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 139 ? -19.400 -5.067  -16.355 1.00 25.90  ? 148 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 139 ? -19.202 -3.646  -16.842 1.00 26.70  ? 148 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 139 ? -19.623 -3.297  -17.953 1.00 28.09  ? 148 GLY   B O   1 
ATOM   1334 N  N   . LEU   B 2 140 ? -18.432 -2.866  -16.077 1.00 25.94  ? 149 LEU   B N   1 
ATOM   1335 C  CA  . LEU   B 2 140 ? -18.106 -1.478  -16.389 1.00 25.68  ? 149 LEU   B CA  1 
ATOM   1336 C  C   . LEU   B 2 140 ? -16.595 -1.321  -16.660 1.00 26.85  ? 149 LEU   B C   1 
ATOM   1337 O  O   . LEU   B 2 140 ? -15.746 -2.039  -16.102 1.00 26.72  ? 149 LEU   B O   1 
ATOM   1338 C  CB  . LEU   B 2 140 ? -18.536 -0.535  -15.245 1.00 24.82  ? 149 LEU   B CB  1 
ATOM   1339 C  CG  . LEU   B 2 140 ? -20.001 -0.551  -14.794 1.00 25.18  ? 149 LEU   B CG  1 
ATOM   1340 C  CD1 . LEU   B 2 140 ? -20.264 0.557   -13.774 1.00 24.75  ? 149 LEU   B CD1 1 
ATOM   1341 C  CD2 . LEU   B 2 140 ? -20.997 -0.464  -15.993 1.00 25.25  ? 149 LEU   B CD2 1 
ATOM   1342 N  N   . TYR   B 2 141 ? -16.280 -0.402  -17.576 1.00 26.36  ? 150 TYR   B N   1 
ATOM   1343 C  CA  . TYR   B 2 141 ? -14.941 -0.145  -18.060 1.00 27.64  ? 150 TYR   B CA  1 
ATOM   1344 C  C   . TYR   B 2 141 ? -14.341 1.016   -17.310 1.00 28.05  ? 150 TYR   B C   1 
ATOM   1345 O  O   . TYR   B 2 141 ? -15.022 2.021   -17.184 1.00 29.19  ? 150 TYR   B O   1 
ATOM   1346 C  CB  . TYR   B 2 141 ? -15.048 0.165   -19.586 1.00 28.92  ? 150 TYR   B CB  1 
ATOM   1347 C  CG  . TYR   B 2 141 ? -13.819 0.796   -20.202 1.00 31.17  ? 150 TYR   B CG  1 
ATOM   1348 C  CD1 . TYR   B 2 141 ? -13.743 2.171   -20.394 1.00 32.41  ? 150 TYR   B CD1 1 
ATOM   1349 C  CD2 . TYR   B 2 141 ? -12.766 0.013   -20.661 1.00 32.54  ? 150 TYR   B CD2 1 
ATOM   1350 C  CE1 . TYR   B 2 141 ? -12.620 2.757   -20.961 1.00 34.11  ? 150 TYR   B CE1 1 
ATOM   1351 C  CE2 . TYR   B 2 141 ? -11.643 0.586   -21.245 1.00 34.41  ? 150 TYR   B CE2 1 
ATOM   1352 C  CZ  . TYR   B 2 141 ? -11.565 1.960   -21.378 1.00 36.08  ? 150 TYR   B CZ  1 
ATOM   1353 O  OH  . TYR   B 2 141 ? -10.461 2.524   -21.971 1.00 39.19  ? 150 TYR   B OH  1 
ATOM   1354 N  N   . GLY   B 2 142 ? -13.071 0.926   -16.897 1.00 28.18  ? 151 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 142 ? -12.442 2.072   -16.246 1.00 29.05  ? 151 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 142 ? -11.533 1.844   -15.059 1.00 29.58  ? 151 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 142 ? -10.976 2.818   -14.530 1.00 30.88  ? 151 GLY   B O   1 
ATOM   1358 N  N   . ASN   B 2 143 ? -11.347 0.580   -14.642 1.00 28.34  ? 152 ASN   B N   1 
ATOM   1359 C  CA  . ASN   B 2 143 ? -10.413 0.306   -13.547 1.00 29.27  ? 152 ASN   B CA  1 
ATOM   1360 C  C   . ASN   B 2 143 ? -9.493  -0.799  -14.049 1.00 30.49  ? 152 ASN   B C   1 
ATOM   1361 O  O   . ASN   B 2 143 ? -9.946  -1.895  -14.365 1.00 30.80  ? 152 ASN   B O   1 
ATOM   1362 C  CB  . ASN   B 2 143 ? -11.107 -0.106  -12.237 1.00 29.52  ? 152 ASN   B CB  1 
ATOM   1363 C  CG  . ASN   B 2 143 ? -10.138 -0.105  -11.065 1.00 30.65  ? 152 ASN   B CG  1 
ATOM   1364 O  OD1 . ASN   B 2 143 ? -9.146  0.641   -11.059 1.00 30.94  ? 152 ASN   B OD1 1 
ATOM   1365 N  ND2 . ASN   B 2 143 ? -10.377 -0.946  -10.066 1.00 29.38  ? 152 ASN   B ND2 1 
ATOM   1366 N  N   . GLY   B 2 144 ? -8.234  -0.463  -14.220 1.00 31.89  ? 153 GLY   B N   1 
ATOM   1367 C  CA  . GLY   B 2 144 ? -7.271  -1.395  -14.781 1.00 32.97  ? 153 GLY   B CA  1 
ATOM   1368 C  C   . GLY   B 2 144 ? -5.835  -1.033  -14.499 1.00 34.81  ? 153 GLY   B C   1 
ATOM   1369 O  O   . GLY   B 2 144 ? -5.518  -0.474  -13.439 1.00 33.64  ? 153 GLY   B O   1 
ATOM   1370 N  N   . VAL   B 2 145 ? -4.958  -1.328  -15.481 1.00 36.66  ? 154 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 145 ? -3.537  -1.140  -15.332 1.00 39.95  ? 154 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 145 ? -2.875  -0.558  -16.610 1.00 43.80  ? 154 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 145 ? -3.462  -0.588  -17.693 1.00 43.23  ? 154 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 145 ? -2.935  -2.514  -14.902 1.00 41.81  ? 154 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 145 ? -2.865  -3.500  -16.073 1.00 42.03  ? 154 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 145 ? -1.588  -2.363  -14.212 1.00 43.45  ? 154 VAL   B CG2 1 
ATOM   1377 N  N   . VAL   B 2 146 ? -1.670  0.016   -16.449 1.00 46.85  ? 155 VAL   B N   1 
ATOM   1378 C  CA  . VAL   B 2 146 ? -0.889  0.562   -17.558 1.00 49.99  ? 155 VAL   B CA  1 
ATOM   1379 C  C   . VAL   B 2 146 ? 0.214   -0.442  -17.781 1.00 53.44  ? 155 VAL   B C   1 
ATOM   1380 O  O   . VAL   B 2 146 ? 0.993   -0.685  -16.860 1.00 53.33  ? 155 VAL   B O   1 
ATOM   1381 C  CB  . VAL   B 2 146 ? -0.310  1.949   -17.217 1.00 50.91  ? 155 VAL   B CB  1 
ATOM   1382 C  CG1 . VAL   B 2 146 ? 0.692   2.403   -18.281 1.00 51.90  ? 155 VAL   B CG1 1 
ATOM   1383 C  CG2 . VAL   B 2 146 ? -1.423  2.973   -17.038 1.00 51.42  ? 155 VAL   B CG2 1 
ATOM   1384 N  N   . ILE   B 2 147 ? 0.258   -1.086  -18.966 1.00 56.27  ? 156 ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 2 147 ? 1.272   -2.121  -19.203 1.00 59.29  ? 156 ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 2 147 ? 2.565   -1.518  -19.846 1.00 61.89  ? 156 ILE   B C   1 
ATOM   1387 O  O   . ILE   B 2 147 ? 2.584   -0.318  -20.139 1.00 61.84  ? 156 ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 2 147 ? 0.668   -3.337  -19.972 1.00 60.46  ? 156 ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 2 147 ? 0.501   -3.056  -21.469 1.00 61.27  ? 156 ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 2 147 ? -0.664  -3.789  -19.341 1.00 61.08  ? 156 ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 2 147 ? 0.099   -4.305  -22.275 1.00 62.65  ? 156 ILE   B CD1 1 
ATOM   1392 N  N   . LYS   B 2 148 ? 3.644   -2.338  -20.013 1.00 63.51  ? 157 LYS   B N   1 
ATOM   1393 C  CA  . LYS   B 2 148 ? 4.990   -1.949  -20.499 1.00 65.84  ? 157 LYS   B CA  1 
ATOM   1394 C  C   . LYS   B 2 148 ? 5.082   -1.346  -21.922 1.00 67.16  ? 157 LYS   B C   1 
ATOM   1395 O  O   . LYS   B 2 148 ? 6.101   -1.501  -22.600 1.00 68.03  ? 157 LYS   B O   1 
ATOM   1396 C  CB  . LYS   B 2 148 ? 6.005   -3.107  -20.376 1.00 69.37  ? 157 LYS   B CB  1 
ATOM   1397 C  CG  . LYS   B 2 148 ? 5.469   -4.511  -20.664 1.00 75.55  ? 157 LYS   B CG  1 
ATOM   1398 C  CD  . LYS   B 2 148 ? 4.949   -5.223  -19.401 1.00 81.39  ? 157 LYS   B CD  1 
ATOM   1399 C  CE  . LYS   B 2 148 ? 5.988   -5.342  -18.310 1.00 86.30  ? 157 LYS   B CE  1 
ATOM   1400 N  NZ  . LYS   B 2 148 ? 5.670   -4.475  -17.138 1.00 88.61  ? 157 LYS   B NZ  1 
ATOM   1401 N  N   . ASN   B 2 149 ? 4.046   -0.632  -22.358 1.00 67.19  ? 158 ASN   B N   1 
ATOM   1402 C  CA  . ASN   B 2 149 ? 3.995   0.096   -23.622 1.00 67.57  ? 158 ASN   B CA  1 
ATOM   1403 C  C   . ASN   B 2 149 ? 3.197   1.423   -23.506 1.00 67.08  ? 158 ASN   B C   1 
ATOM   1404 O  O   . ASN   B 2 149 ? 2.920   2.066   -24.526 1.00 67.70  ? 158 ASN   B O   1 
ATOM   1405 C  CB  . ASN   B 2 149 ? 3.494   -0.774  -24.819 1.00 69.53  ? 158 ASN   B CB  1 
ATOM   1406 C  CG  . ASN   B 2 149 ? 2.927   -2.163  -24.528 1.00 73.07  ? 158 ASN   B CG  1 
ATOM   1407 O  OD1 . ASN   B 2 149 ? 3.484   -2.962  -23.759 1.00 74.35  ? 158 ASN   B OD1 1 
ATOM   1408 N  ND2 . ASN   B 2 149 ? 1.824   -2.507  -25.188 1.00 73.37  ? 158 ASN   B ND2 1 
ATOM   1409 N  N   . GLY   B 2 150 ? 2.830   1.811   -22.275 1.00 65.44  ? 159 GLY   B N   1 
ATOM   1410 C  CA  . GLY   B 2 150 ? 2.041   3.005   -21.982 1.00 63.58  ? 159 GLY   B CA  1 
ATOM   1411 C  C   . GLY   B 2 150 ? 0.553   2.859   -22.261 1.00 60.84  ? 159 GLY   B C   1 
ATOM   1412 O  O   . GLY   B 2 150 ? -0.230  3.771   -21.960 1.00 61.12  ? 159 GLY   B O   1 
ATOM   1413 N  N   . SER   B 2 151 ? 0.139   1.711   -22.842 1.00 57.68  ? 160 SER   B N   1 
ATOM   1414 C  CA  A SER   B 2 151 ? -1.271  1.505   -23.161 0.50 56.42  ? 160 SER   B CA  1 
ATOM   1415 C  CA  B SER   B 2 151 ? -1.263  1.452   -23.175 0.50 56.42  ? 160 SER   B CA  1 
ATOM   1416 C  C   . SER   B 2 151 ? -2.102  1.133   -21.917 1.00 54.41  ? 160 SER   B C   1 
ATOM   1417 O  O   . SER   B 2 151 ? -1.547  0.880   -20.847 1.00 54.75  ? 160 SER   B O   1 
ATOM   1418 C  CB  A SER   B 2 151 ? -1.436  0.476   -24.276 0.50 57.68  ? 160 SER   B CB  1 
ATOM   1419 C  CB  B SER   B 2 151 ? -1.363  0.318   -24.194 0.50 57.63  ? 160 SER   B CB  1 
ATOM   1420 O  OG  A SER   B 2 151 ? -2.678  0.698   -24.923 0.50 59.53  ? 160 SER   B OG  1 
ATOM   1421 O  OG  B SER   B 2 151 ? -0.780  -0.876  -23.698 0.50 59.49  ? 160 SER   B OG  1 
ATOM   1422 N  N   . TYR   B 2 152 ? -3.433  1.145   -22.052 1.00 50.29  ? 161 TYR   B N   1 
ATOM   1423 C  CA  . TYR   B 2 152 ? -4.339  0.864   -20.954 1.00 47.05  ? 161 TYR   B CA  1 
ATOM   1424 C  C   . TYR   B 2 152 ? -5.135  -0.429  -21.137 1.00 42.88  ? 161 TYR   B C   1 
ATOM   1425 O  O   . TYR   B 2 152 ? -5.624  -0.702  -22.225 1.00 42.67  ? 161 TYR   B O   1 
ATOM   1426 C  CB  . TYR   B 2 152 ? -5.287  2.036   -20.834 1.00 47.13  ? 161 TYR   B CB  1 
ATOM   1427 C  CG  . TYR   B 2 152 ? -6.190  1.956   -19.636 1.00 47.70  ? 161 TYR   B CG  1 
ATOM   1428 C  CD1 . TYR   B 2 152 ? -5.699  2.172   -18.359 1.00 48.45  ? 161 TYR   B CD1 1 
ATOM   1429 C  CD2 . TYR   B 2 152 ? -7.547  1.716   -19.783 1.00 48.57  ? 161 TYR   B CD2 1 
ATOM   1430 C  CE1 . TYR   B 2 152 ? -6.530  2.122   -17.253 1.00 49.60  ? 161 TYR   B CE1 1 
ATOM   1431 C  CE2 . TYR   B 2 152 ? -8.386  1.648   -18.683 1.00 49.23  ? 161 TYR   B CE2 1 
ATOM   1432 C  CZ  . TYR   B 2 152 ? -7.874  1.854   -17.418 1.00 50.19  ? 161 TYR   B CZ  1 
ATOM   1433 O  OH  . TYR   B 2 152 ? -8.702  1.810   -16.330 1.00 51.44  ? 161 TYR   B OH  1 
ATOM   1434 N  N   . VAL   B 2 153 ? -5.256  -1.234  -20.072 1.00 39.24  ? 162 VAL   B N   1 
ATOM   1435 C  CA  . VAL   B 2 153 ? -6.071  -2.438  -20.095 1.00 36.05  ? 162 VAL   B CA  1 
ATOM   1436 C  C   . VAL   B 2 153 ? -7.016  -2.394  -18.869 1.00 33.31  ? 162 VAL   B C   1 
ATOM   1437 O  O   . VAL   B 2 153 ? -6.559  -2.362  -17.736 1.00 32.21  ? 162 VAL   B O   1 
ATOM   1438 C  CB  . VAL   B 2 153 ? -5.239  -3.727  -20.103 1.00 36.14  ? 162 VAL   B CB  1 
ATOM   1439 C  CG1 . VAL   B 2 153 ? -6.146  -4.954  -20.130 1.00 35.90  ? 162 VAL   B CG1 1 
ATOM   1440 C  CG2 . VAL   B 2 153 ? -4.268  -3.742  -21.288 1.00 37.30  ? 162 VAL   B CG2 1 
ATOM   1441 N  N   . SER   B 2 154 ? -8.328  -2.353  -19.116 1.00 32.23  ? 163 SER   B N   1 
ATOM   1442 C  CA  . SER   B 2 154 ? -9.308  -2.263  -18.029 1.00 30.94  ? 163 SER   B CA  1 
ATOM   1443 C  C   . SER   B 2 154 ? -9.812  -3.632  -17.659 1.00 29.72  ? 163 SER   B C   1 
ATOM   1444 O  O   . SER   B 2 154 ? -10.109 -4.410  -18.557 1.00 29.76  ? 163 SER   B O   1 
ATOM   1445 C  CB  . SER   B 2 154 ? -10.504 -1.452  -18.519 1.00 31.82  ? 163 SER   B CB  1 
ATOM   1446 O  OG  . SER   B 2 154 ? -11.592 -1.451  -17.605 1.00 32.43  ? 163 SER   B OG  1 
ATOM   1447 N  N   . ALA   B 2 155 ? -10.098 -3.880  -16.360 1.00 29.09  ? 164 ALA   B N   1 
ATOM   1448 C  CA  . ALA   B 2 155 ? -10.808 -5.098  -15.989 1.00 27.81  ? 164 ALA   B CA  1 
ATOM   1449 C  C   . ALA   B 2 155 ? -12.253 -4.922  -16.522 1.00 28.47  ? 164 ALA   B C   1 
ATOM   1450 O  O   . ALA   B 2 155 ? -12.727 -3.781  -16.697 1.00 29.47  ? 164 ALA   B O   1 
ATOM   1451 C  CB  . ALA   B 2 155 ? -10.882 -5.221  -14.457 1.00 28.34  ? 164 ALA   B CB  1 
ATOM   1452 N  N   . ILE   B 2 156 ? -12.949 -6.031  -16.710 1.00 27.35  ? 165 ILE   B N   1 
ATOM   1453 C  CA  . ILE   B 2 156 ? -14.375 -6.029  -16.918 1.00 28.17  ? 165 ILE   B CA  1 
ATOM   1454 C  C   . ILE   B 2 156 ? -14.925 -6.110  -15.473 1.00 27.67  ? 165 ILE   B C   1 
ATOM   1455 O  O   . ILE   B 2 156 ? -14.939 -7.192  -14.863 1.00 28.95  ? 165 ILE   B O   1 
ATOM   1456 C  CB  . ILE   B 2 156 ? -14.834 -7.262  -17.726 1.00 30.12  ? 165 ILE   B CB  1 
ATOM   1457 C  CG1 . ILE   B 2 156 ? -14.187 -7.211  -19.138 1.00 32.61  ? 165 ILE   B CG1 1 
ATOM   1458 C  CG2 . ILE   B 2 156 ? -16.384 -7.177  -17.838 1.00 29.96  ? 165 ILE   B CG2 1 
ATOM   1459 C  CD1 . ILE   B 2 156 ? -14.586 -8.421  -20.033 1.00 34.67  ? 165 ILE   B CD1 1 
ATOM   1460 N  N   . THR   B 2 157 ? -15.296 -4.945  -14.884 1.00 26.68  ? 166 THR   B N   1 
ATOM   1461 C  CA  . THR   B 2 157 ? -15.707 -4.939  -13.468 1.00 25.82  ? 166 THR   B CA  1 
ATOM   1462 C  C   . THR   B 2 157 ? -17.216 -5.177  -13.272 1.00 25.62  ? 166 THR   B C   1 
ATOM   1463 O  O   . THR   B 2 157 ? -18.032 -4.357  -13.717 1.00 26.29  ? 166 THR   B O   1 
ATOM   1464 C  CB  . THR   B 2 157 ? -15.253 -3.651  -12.761 1.00 25.14  ? 166 THR   B CB  1 
ATOM   1465 O  OG1 . THR   B 2 157 ? -13.810 -3.548  -12.796 1.00 25.56  ? 166 THR   B OG1 1 
ATOM   1466 C  CG2 . THR   B 2 157 ? -15.743 -3.622  -11.325 1.00 24.92  ? 166 THR   B CG2 1 
ATOM   1467 N  N   . GLN   B 2 158 ? -17.593 -6.295  -12.631 1.00 24.96  ? 167 GLN   B N   1 
ATOM   1468 C  CA  . GLN   B 2 158 ? -19.019 -6.584  -12.429 1.00 25.16  ? 167 GLN   B CA  1 
ATOM   1469 C  C   . GLN   B 2 158 ? -19.344 -6.726  -10.914 1.00 26.14  ? 167 GLN   B C   1 
ATOM   1470 O  O   . GLN   B 2 158 ? -18.535 -7.270  -10.161 1.00 25.24  ? 167 GLN   B O   1 
ATOM   1471 C  CB  . GLN   B 2 158 ? -19.363 -7.908  -13.129 1.00 26.82  ? 167 GLN   B CB  1 
ATOM   1472 C  CG  . GLN   B 2 158 ? -20.859 -8.280  -13.088 1.00 29.87  ? 167 GLN   B CG  1 
ATOM   1473 C  CD  . GLN   B 2 158 ? -21.798 -7.213  -13.663 1.00 30.03  ? 167 GLN   B CD  1 
ATOM   1474 O  OE1 . GLN   B 2 158 ? -21.943 -6.106  -13.118 1.00 26.18  ? 167 GLN   B OE1 1 
ATOM   1475 N  NE2 . GLN   B 2 158 ? -22.455 -7.518  -14.788 1.00 29.53  ? 167 GLN   B NE2 1 
ATOM   1476 N  N   . GLY   B 2 159 ? -20.522 -6.282  -10.509 1.00 29.36  ? 168 GLY   B N   1 
ATOM   1477 C  CA  . GLY   B 2 159 ? -20.945 -6.393  -9.116  1.00 33.03  ? 168 GLY   B CA  1 
ATOM   1478 C  C   . GLY   B 2 159 ? -21.670 -7.697  -8.861  1.00 38.52  ? 168 GLY   B C   1 
ATOM   1479 O  O   . GLY   B 2 159 ? -21.637 -8.620  -9.681  1.00 39.59  ? 168 GLY   B O   1 
ATOM   1480 N  N   . LYS   B 2 160 ? -22.279 -7.811  -7.684  1.00 41.36  ? 169 LYS   B N   1 
ATOM   1481 C  CA  . LYS   B 2 160 ? -23.053 -8.989  -7.316  1.00 43.67  ? 169 LYS   B CA  1 
ATOM   1482 C  C   . LYS   B 2 160 ? -24.507 -8.550  -7.172  1.00 45.48  ? 169 LYS   B C   1 
ATOM   1483 O  O   . LYS   B 2 160 ? -24.783 -7.509  -6.566  1.00 45.51  ? 169 LYS   B O   1 
ATOM   1484 C  CB  . LYS   B 2 160 ? -22.530 -9.576  -5.986  1.00 46.88  ? 169 LYS   B CB  1 
ATOM   1485 C  CG  . LYS   B 2 160 ? -23.454 -10.601 -5.332  1.00 53.78  ? 169 LYS   B CG  1 
ATOM   1486 C  CD  . LYS   B 2 160 ? -22.910 -11.133 -4.005  1.00 60.51  ? 169 LYS   B CD  1 
ATOM   1487 C  CE  . LYS   B 2 160 ? -23.705 -12.335 -3.544  1.00 66.28  ? 169 LYS   B CE  1 
ATOM   1488 N  NZ  . LYS   B 2 160 ? -23.297 -12.796 -2.184  1.00 70.05  ? 169 LYS   B NZ  1 
ATOM   1489 N  N   . ARG   B 2 161 ? -25.434 -9.330  -7.728  1.00 46.84  ? 170 ARG   B N   1 
ATOM   1490 C  CA  . ARG   B 2 161 ? -26.851 -9.041  -7.570  1.00 49.35  ? 170 ARG   B CA  1 
ATOM   1491 C  C   . ARG   B 2 161 ? -27.356 -9.889  -6.384  1.00 52.01  ? 170 ARG   B C   1 
ATOM   1492 O  O   . ARG   B 2 161 ? -27.390 -11.119 -6.487  1.00 52.34  ? 170 ARG   B O   1 
ATOM   1493 C  CB  . ARG   B 2 161 ? -27.626 -9.372  -8.859  1.00 50.66  ? 170 ARG   B CB  1 
ATOM   1494 C  CG  . ARG   B 2 161 ? -29.019 -8.763  -8.879  1.00 52.71  ? 170 ARG   B CG  1 
ATOM   1495 C  CD  . ARG   B 2 161 ? -29.908 -9.353  -9.960  1.00 54.62  ? 170 ARG   B CD  1 
ATOM   1496 N  NE  . ARG   B 2 161 ? -31.305 -8.965  -9.756  1.00 56.23  ? 170 ARG   B NE  1 
ATOM   1497 C  CZ  . ARG   B 2 161 ? -31.962 -8.080  -10.498 1.00 56.55  ? 170 ARG   B CZ  1 
ATOM   1498 N  NH1 . ARG   B 2 161 ? -31.370 -7.505  -11.537 1.00 54.40  ? 170 ARG   B NH1 1 
ATOM   1499 N  NH2 . ARG   B 2 161 ? -33.228 -7.792  -10.231 1.00 56.68  ? 170 ARG   B NH2 1 
ATOM   1500 N  N   . GLU   B 2 162 ? -27.671 -9.241  -5.246  1.00 53.60  ? 171 GLU   B N   1 
ATOM   1501 C  CA  . GLU   B 2 162 ? -28.170 -9.916  -4.042  1.00 56.00  ? 171 GLU   B CA  1 
ATOM   1502 C  C   . GLU   B 2 162 ? -29.531 -10.570 -4.305  1.00 57.36  ? 171 GLU   B C   1 
ATOM   1503 O  O   . GLU   B 2 162 ? -29.876 -11.563 -3.659  1.00 58.24  ? 171 GLU   B O   1 
ATOM   1504 C  CB  . GLU   B 2 162 ? -28.311 -8.919  -2.879  1.00 59.74  ? 171 GLU   B CB  1 
ATOM   1505 C  CG  . GLU   B 2 162 ? -27.017 -8.233  -2.478  1.00 67.15  ? 171 GLU   B CG  1 
ATOM   1506 C  CD  . GLU   B 2 162 ? -26.132 -9.076  -1.586  1.00 76.33  ? 171 GLU   B CD  1 
ATOM   1507 O  OE1 . GLU   B 2 162 ? -26.643 -9.598  -0.567  1.00 78.84  ? 171 GLU   B OE1 1 
ATOM   1508 O  OE2 . GLU   B 2 162 ? -24.928 -9.216  -1.905  1.00 78.91  ? 171 GLU   B OE2 1 
HETATM 1509 S  S   . DMS   C 3 .   ? -18.920 12.539  -0.345  1.00 67.47  ? 201 DMS   B S   1 
HETATM 1510 O  O   . DMS   C 3 .   ? -19.707 11.261  -0.403  1.00 67.34  ? 201 DMS   B O   1 
HETATM 1511 C  C1  . DMS   C 3 .   ? -19.884 13.917  -1.003  1.00 67.57  ? 201 DMS   B C1  1 
HETATM 1512 C  C2  . DMS   C 3 .   ? -17.717 12.558  -1.708  1.00 67.19  ? 201 DMS   B C2  1 
HETATM 1513 S  S   . DMS   D 3 .   ? -5.759  2.891   -13.381 1.00 68.31  ? 202 DMS   B S   1 
HETATM 1514 O  O   . DMS   D 3 .   ? -7.066  2.755   -14.146 1.00 67.56  ? 202 DMS   B O   1 
HETATM 1515 C  C1  . DMS   D 3 .   ? -5.666  4.498   -12.539 1.00 68.55  ? 202 DMS   B C1  1 
HETATM 1516 C  C2  . DMS   D 3 .   ? -4.376  3.158   -14.535 1.00 68.23  ? 202 DMS   B C2  1 
HETATM 1517 N  N1  . A1B9N E 4 .   ? -9.217  5.085   -13.928 1.00 43.34  ? 203 A1B9N B N1  1 
HETATM 1518 N  N3  . A1B9N E 4 .   ? -9.679  9.822   -9.498  1.00 48.34  ? 203 A1B9N B N3  1 
HETATM 1519 C  C4  . A1B9N E 4 .   ? -9.923  5.224   -16.707 1.00 41.08  ? 203 A1B9N B C4  1 
HETATM 1520 C  C5  . A1B9N E 4 .   ? -8.655  5.542   -16.233 1.00 41.65  ? 203 A1B9N B C5  1 
HETATM 1521 C  C6  . A1B9N E 4 .   ? -8.436  5.795   -14.776 1.00 42.49  ? 203 A1B9N B C6  1 
HETATM 1522 C  C7  . A1B9N E 4 .   ? -9.198  5.156   -12.509 1.00 44.34  ? 203 A1B9N B C7  1 
HETATM 1523 C  C8  . A1B9N E 4 .   ? -9.221  3.993   -11.749 1.00 44.45  ? 203 A1B9N B C8  1 
HETATM 1524 C  C10 . A1B9N E 4 .   ? -9.064  5.300   -9.737  1.00 45.52  ? 203 A1B9N B C10 1 
HETATM 1525 C  C13 . A1B9N E 4 .   ? -9.117  6.394   -11.876 1.00 44.93  ? 203 A1B9N B C13 1 
HETATM 1526 O  O   . A1B9N E 4 .   ? -7.603  6.614   -14.396 1.00 42.27  ? 203 A1B9N B O   1 
HETATM 1527 C  C3  . A1B9N E 4 .   ? -10.113 5.073   -18.065 1.00 40.27  ? 203 A1B9N B C3  1 
HETATM 1528 CL CL  . A1B9N E 4 .   ? -11.727 4.798   -18.670 1.00 39.27  ? 203 A1B9N B CL  1 
HETATM 1529 C  C2  . A1B9N E 4 .   ? -9.070  5.193   -18.961 1.00 40.23  ? 203 A1B9N B C2  1 
HETATM 1530 C  C14 . A1B9N E 4 .   ? -7.596  5.674   -17.129 1.00 41.03  ? 203 A1B9N B C14 1 
HETATM 1531 C  C1  . A1B9N E 4 .   ? -7.794  5.494   -18.493 1.00 40.89  ? 203 A1B9N B C1  1 
HETATM 1532 C  C   . A1B9N E 4 .   ? -6.630  5.609   -19.447 1.00 41.81  ? 203 A1B9N B C   1 
HETATM 1533 N  N   . A1B9N E 4 .   ? -6.753  6.831   -20.248 1.00 42.08  ? 203 A1B9N B N   1 
HETATM 1534 C  C11 . A1B9N E 4 .   ? -9.068  6.475   -10.488 1.00 46.01  ? 203 A1B9N B C11 1 
HETATM 1535 C  C9  . A1B9N E 4 .   ? -9.150  4.070   -10.366 1.00 45.04  ? 203 A1B9N B C9  1 
HETATM 1536 C  C12 . A1B9N E 4 .   ? -9.168  7.793   -9.824  1.00 47.34  ? 203 A1B9N B C12 1 
HETATM 1537 N  N5  . A1B9N E 4 .   ? -9.052  7.939   -8.508  1.00 47.84  ? 203 A1B9N B N5  1 
HETATM 1538 N  N4  . A1B9N E 4 .   ? -9.395  9.214   -8.370  1.00 48.17  ? 203 A1B9N B N4  1 
HETATM 1539 N  N2  . A1B9N E 4 .   ? -9.529  8.930   -10.456 1.00 47.89  ? 203 A1B9N B N2  1 
HETATM 1540 S  S   . SO4   F 5 .   ? -6.713  8.628   -24.993 1.00 158.61 ? 204 SO4   B S   1 
HETATM 1541 O  O1  . SO4   F 5 .   ? -7.377  9.935   -24.919 1.00 158.64 ? 204 SO4   B O1  1 
HETATM 1542 O  O2  . SO4   F 5 .   ? -7.472  7.732   -25.874 1.00 158.59 ? 204 SO4   B O2  1 
HETATM 1543 O  O3  . SO4   F 5 .   ? -5.356  8.805   -25.544 1.00 158.64 ? 204 SO4   B O3  1 
HETATM 1544 O  O4  . SO4   F 5 .   ? -6.600  8.056   -23.636 1.00 158.55 ? 204 SO4   B O4  1 
HETATM 1545 S  S   . DMS   G 3 .   ? -7.404  11.092  -19.662 1.00 77.74  ? 205 DMS   B S   1 
HETATM 1546 O  O   . DMS   G 3 .   ? -6.608  10.208  -18.726 1.00 77.66  ? 205 DMS   B O   1 
HETATM 1547 C  C1  . DMS   G 3 .   ? -7.809  12.656  -18.838 1.00 77.61  ? 205 DMS   B C1  1 
HETATM 1548 C  C2  . DMS   G 3 .   ? -6.257  11.802  -20.887 1.00 77.77  ? 205 DMS   B C2  1 
HETATM 1549 O  O   . HOH   H 6 .   ? -9.295  -8.464  -29.330 1.00 49.95  ? 101 HOH   A O   1 
HETATM 1550 O  O   . HOH   H 6 .   ? -32.309 0.509   -28.946 1.00 46.94  ? 102 HOH   A O   1 
HETATM 1551 O  O   . HOH   H 6 .   ? -3.062  1.816   -4.310  1.00 56.50  ? 103 HOH   A O   1 
HETATM 1552 O  O   . HOH   H 6 .   ? -23.914 19.443  -19.708 1.00 45.68  ? 104 HOH   A O   1 
HETATM 1553 O  O   . HOH   H 6 .   ? -7.984  1.023   3.326   1.00 45.34  ? 105 HOH   A O   1 
HETATM 1554 O  O   . HOH   H 6 .   ? -4.725  -14.002 -25.695 1.00 31.07  ? 106 HOH   A O   1 
HETATM 1555 O  O   . HOH   H 6 .   ? -8.297  -1.343  6.539   1.00 41.46  ? 107 HOH   A O   1 
HETATM 1556 O  O   . HOH   H 6 .   ? -24.544 9.687   -27.585 1.00 35.03  ? 108 HOH   A O   1 
HETATM 1557 O  O   . HOH   H 6 .   ? -2.278  -3.491  -6.518  1.00 40.14  ? 109 HOH   A O   1 
HETATM 1558 O  O   . HOH   H 6 .   ? -9.565  -6.249  -25.545 1.00 36.35  ? 110 HOH   A O   1 
HETATM 1559 O  O   . HOH   H 6 .   ? -25.619 12.837  -23.891 1.00 45.97  ? 111 HOH   A O   1 
HETATM 1560 O  O   . HOH   H 6 .   ? -2.607  -4.422  -24.837 1.00 54.63  ? 112 HOH   A O   1 
HETATM 1561 O  O   . HOH   H 6 .   ? -3.157  -11.332 -7.235  1.00 42.11  ? 113 HOH   A O   1 
HETATM 1562 O  O   . HOH   H 6 .   ? -30.905 13.271  -16.437 1.00 40.85  ? 114 HOH   A O   1 
HETATM 1563 O  O   . HOH   H 6 .   ? -29.417 16.229  -15.021 1.00 40.31  ? 115 HOH   A O   1 
HETATM 1564 O  O   . HOH   H 6 .   ? -3.257  0.836   -12.078 1.00 48.58  ? 116 HOH   A O   1 
HETATM 1565 O  O   . HOH   H 6 .   ? -28.575 17.934  -18.948 1.00 61.09  ? 117 HOH   A O   1 
HETATM 1566 O  O   . HOH   H 6 .   ? -7.084  -8.684  -3.224  1.00 33.96  ? 118 HOH   A O   1 
HETATM 1567 O  O   . HOH   H 6 .   ? -30.936 0.766   -22.800 1.00 46.67  ? 119 HOH   A O   1 
HETATM 1568 O  O   . HOH   H 6 .   ? -8.363  2.176   0.918   1.00 43.54  ? 120 HOH   A O   1 
HETATM 1569 O  O   . HOH   H 6 .   ? -28.636 -5.651  -28.053 1.00 42.20  ? 121 HOH   A O   1 
HETATM 1570 O  O   . HOH   H 6 .   ? -22.672 -8.753  -34.705 1.00 60.04  ? 122 HOH   A O   1 
HETATM 1571 O  O   . HOH   H 6 .   ? -4.765  -9.655  -5.696  1.00 33.35  ? 123 HOH   A O   1 
HETATM 1572 O  O   . HOH   H 6 .   ? -26.981 -2.928  -35.369 1.00 54.54  ? 124 HOH   A O   1 
HETATM 1573 O  O   . HOH   H 6 .   ? -28.068 2.229   -29.705 1.00 63.29  ? 125 HOH   A O   1 
HETATM 1574 O  O   . HOH   H 6 .   ? 1.724   -1.885  -11.943 1.00 54.29  ? 126 HOH   A O   1 
HETATM 1575 O  O   . HOH   H 6 .   ? -3.888  -4.002  0.279   1.00 55.91  ? 127 HOH   A O   1 
HETATM 1576 O  O   . HOH   H 6 .   ? -6.893  -15.282 -25.550 1.00 43.60  ? 128 HOH   A O   1 
HETATM 1577 O  O   . HOH   H 6 .   ? -9.606  2.936   -7.101  1.00 50.84  ? 129 HOH   A O   1 
HETATM 1578 O  O   . HOH   H 6 .   ? -3.974  -0.311  -0.420  1.00 54.32  ? 130 HOH   A O   1 
HETATM 1579 O  O   . HOH   H 6 .   ? -3.067  -8.531  -3.359  1.00 50.17  ? 131 HOH   A O   1 
HETATM 1580 O  O   . HOH   H 6 .   ? -4.653  -6.570  -0.485  1.00 72.01  ? 132 HOH   A O   1 
HETATM 1581 O  O   . HOH   H 6 .   ? -0.822  -11.718 -5.966  1.00 52.28  ? 133 HOH   A O   1 
HETATM 1582 O  O   . HOH   I 6 .   ? -18.463 -19.917 -21.257 1.00 46.54  ? 301 HOH   B O   1 
HETATM 1583 O  O   . HOH   I 6 .   ? -34.316 2.142   -15.150 1.00 41.96  ? 302 HOH   B O   1 
HETATM 1584 O  O   . HOH   I 6 .   ? -15.419 -4.082  1.435   1.00 34.29  ? 303 HOH   B O   1 
HETATM 1585 O  O   . HOH   I 6 .   ? -16.885 21.327  -14.597 1.00 42.89  ? 304 HOH   B O   1 
HETATM 1586 O  O   . HOH   I 6 .   ? -28.854 -4.025  -21.590 1.00 46.55  ? 305 HOH   B O   1 
HETATM 1587 O  O   . HOH   I 6 .   ? -9.945  9.758   -12.862 1.00 60.43  ? 306 HOH   B O   1 
HETATM 1588 O  O   . HOH   I 6 .   ? -20.589 -6.837  -5.430  1.00 49.58  ? 307 HOH   B O   1 
HETATM 1589 O  O   . HOH   I 6 .   ? -4.828  -0.785  -24.703 1.00 45.94  ? 308 HOH   B O   1 
HETATM 1590 O  O   . HOH   I 6 .   ? -22.972 -10.626 -10.676 1.00 53.05  ? 309 HOH   B O   1 
HETATM 1591 O  O   . HOH   I 6 .   ? -35.527 4.350   -8.777  1.00 52.17  ? 310 HOH   B O   1 
HETATM 1592 O  O   . HOH   I 6 .   ? -17.601 15.453  -30.622 1.00 50.30  ? 311 HOH   B O   1 
HETATM 1593 O  O   . HOH   I 6 .   ? -26.240 -7.539  -16.449 1.00 32.49  ? 312 HOH   B O   1 
HETATM 1594 O  O   . HOH   I 6 .   ? -20.000 -11.689 -25.607 1.00 45.72  ? 313 HOH   B O   1 
HETATM 1595 O  O   . HOH   I 6 .   ? -6.478  0.091   -11.016 1.00 29.02  ? 314 HOH   B O   1 
HETATM 1596 O  O   . HOH   I 6 .   ? -21.713 7.715   -0.055  0.50 31.84  ? 315 HOH   B O   1 
HETATM 1597 O  O   . HOH   I 6 .   ? -35.048 -2.499  -16.607 1.00 53.89  ? 316 HOH   B O   1 
HETATM 1598 O  O   . HOH   I 6 .   ? -31.108 13.092  -19.301 1.00 54.81  ? 317 HOH   B O   1 
HETATM 1599 O  O   . HOH   I 6 .   ? -7.355  -10.338 -5.330  1.00 39.63  ? 318 HOH   B O   1 
HETATM 1600 O  O   . HOH   I 6 .   ? -17.902 8.977   -30.868 1.00 43.07  ? 319 HOH   B O   1 
HETATM 1601 O  O   . HOH   I 6 .   ? -30.345 -0.481  -19.110 1.00 43.38  ? 320 HOH   B O   1 
HETATM 1602 O  O   . HOH   I 6 .   ? -27.720 -6.358  -5.367  1.00 41.55  ? 321 HOH   B O   1 
HETATM 1603 O  O   . HOH   I 6 .   ? -23.589 -5.758  -4.852  1.00 45.17  ? 322 HOH   B O   1 
HETATM 1604 O  O   . HOH   I 6 .   ? -19.376 15.180  -22.320 1.00 29.60  ? 323 HOH   B O   1 
HETATM 1605 O  O   . HOH   I 6 .   ? -12.219 2.615   -5.838  1.00 30.48  ? 324 HOH   B O   1 
HETATM 1606 O  O   . HOH   I 6 .   ? -18.285 -10.314 -16.413 1.00 31.39  ? 325 HOH   B O   1 
HETATM 1607 O  O   . HOH   I 6 .   ? -16.749 -14.603 -16.427 1.00 40.70  ? 326 HOH   B O   1 
HETATM 1608 O  O   . HOH   I 6 .   ? -12.311 -17.731 -28.064 1.00 41.96  ? 327 HOH   B O   1 
HETATM 1609 O  O   . HOH   I 6 .   ? -16.538 -6.633  -8.349  1.00 49.73  ? 328 HOH   B O   1 
HETATM 1610 O  O   . HOH   I 6 .   ? -23.377 7.820   -34.358 1.00 57.27  ? 329 HOH   B O   1 
HETATM 1611 O  O   . HOH   I 6 .   ? -22.478 15.649  -6.107  1.00 38.86  ? 330 HOH   B O   1 
HETATM 1612 O  O   . HOH   I 6 .   ? -13.231 -1.734  -14.871 1.00 23.45  ? 331 HOH   B O   1 
HETATM 1613 O  O   . HOH   I 6 .   ? -28.028 -5.835  -18.390 1.00 38.13  ? 332 HOH   B O   1 
HETATM 1614 O  O   . HOH   I 6 .   ? -21.651 14.912  -34.557 1.00 58.58  ? 333 HOH   B O   1 
HETATM 1615 O  O   . HOH   I 6 .   ? -35.576 -5.070  -9.924  1.00 47.30  ? 334 HOH   B O   1 
HETATM 1616 O  O   . HOH   I 6 .   ? -15.881 -9.809  -15.258 1.00 35.69  ? 335 HOH   B O   1 
HETATM 1617 O  O   . HOH   I 6 .   ? -17.257 13.518  -5.520  1.00 40.35  ? 336 HOH   B O   1 
HETATM 1618 O  O   . HOH   I 6 .   ? -12.696 -2.842  -10.271 1.00 30.72  ? 337 HOH   B O   1 
HETATM 1619 O  O   . HOH   I 6 .   ? -22.252 -13.141 -21.666 1.00 38.91  ? 338 HOH   B O   1 
HETATM 1620 O  O   . HOH   I 6 .   ? -7.617  -6.135  0.230   1.00 46.88  ? 339 HOH   B O   1 
HETATM 1621 O  O   . HOH   I 6 .   ? -15.362 9.814   -0.830  1.00 36.02  ? 340 HOH   B O   1 
HETATM 1622 O  O   . HOH   I 6 .   ? -29.593 -8.123  -14.673 1.00 62.34  ? 341 HOH   B O   1 
HETATM 1623 O  O   . HOH   I 6 .   ? -15.492 -8.063  -11.714 1.00 36.52  ? 342 HOH   B O   1 
HETATM 1624 O  O   . HOH   I 6 .   ? -11.316 12.621  -19.405 1.00 36.00  ? 343 HOH   B O   1 
HETATM 1625 O  O   . HOH   I 6 .   ? -19.339 25.889  -15.008 1.00 56.69  ? 344 HOH   B O   1 
HETATM 1626 O  O   . HOH   I 6 .   ? -32.138 7.746   -4.370  1.00 42.87  ? 345 HOH   B O   1 
HETATM 1627 O  O   . HOH   I 6 .   ? -24.955 -11.818 -9.148  1.00 56.13  ? 346 HOH   B O   1 
HETATM 1628 O  O   . HOH   I 6 .   ? -26.140 -3.985  -3.934  1.00 32.31  ? 347 HOH   B O   1 
HETATM 1629 O  O   . HOH   I 6 .   ? -15.530 16.944  -20.351 1.00 41.56  ? 348 HOH   B O   1 
HETATM 1630 O  O   . HOH   I 6 .   ? -21.838 -11.957 -12.803 1.00 46.71  ? 349 HOH   B O   1 
HETATM 1631 O  O   . HOH   I 6 .   ? -16.432 -14.005 -30.750 1.00 48.49  ? 350 HOH   B O   1 
HETATM 1632 O  O   B HOH   I 6 .   ? -28.623 7.316   0.930   0.50 24.36  ? 351 HOH   B O   1 
HETATM 1633 O  O   . HOH   I 6 .   ? -14.939 -11.860 -16.622 1.00 41.74  ? 352 HOH   B O   1 
HETATM 1634 O  O   . HOH   I 6 .   ? -21.317 6.603   -32.903 1.00 52.36  ? 353 HOH   B O   1 
HETATM 1635 O  O   . HOH   I 6 .   ? -1.163  1.048   -13.717 1.00 52.67  ? 354 HOH   B O   1 
HETATM 1636 O  O   . HOH   I 6 .   ? -11.695 -4.351  -8.367  1.00 34.81  ? 355 HOH   B O   1 
HETATM 1637 O  O   . HOH   I 6 .   ? -32.540 -6.537  -6.682  1.00 44.34  ? 356 HOH   B O   1 
HETATM 1638 O  O   . HOH   I 6 .   ? -19.873 -12.961 -23.045 1.00 34.84  ? 357 HOH   B O   1 
HETATM 1639 O  O   . HOH   I 6 .   ? -11.638 8.538   -14.065 1.00 44.15  ? 358 HOH   B O   1 
HETATM 1640 O  O   . HOH   I 6 .   ? -11.006 -18.163 -12.044 1.00 51.40  ? 359 HOH   B O   1 
HETATM 1641 O  O   . HOH   I 6 .   ? -24.272 -14.403 -17.725 1.00 50.02  ? 360 HOH   B O   1 
HETATM 1642 O  O   . HOH   I 6 .   ? -14.643 -6.010  -1.571  1.00 39.90  ? 361 HOH   B O   1 
HETATM 1643 O  O   . HOH   I 6 .   ? -10.511 -10.206 -3.173  1.00 59.74  ? 362 HOH   B O   1 
HETATM 1644 O  O   . HOH   I 6 .   ? -9.170  -10.209 -7.489  1.00 49.43  ? 363 HOH   B O   1 
HETATM 1645 O  O   . HOH   I 6 .   ? -19.830 -5.130  -0.839  1.00 38.74  ? 364 HOH   B O   1 
HETATM 1646 O  O   . HOH   I 6 .   ? -11.855 9.460   -27.333 1.00 47.70  ? 365 HOH   B O   1 
HETATM 1647 O  O   . HOH   I 6 .   ? -30.893 5.043   -2.316  1.00 40.36  ? 366 HOH   B O   1 
HETATM 1648 O  O   . HOH   I 6 .   ? -20.930 25.443  -17.151 1.00 56.39  ? 367 HOH   B O   1 
HETATM 1649 O  O   . HOH   I 6 .   ? -20.747 -7.093  -2.476  1.00 54.51  ? 368 HOH   B O   1 
HETATM 1650 O  O   . HOH   I 6 .   ? -14.068 11.723  -31.983 1.00 55.67  ? 369 HOH   B O   1 
HETATM 1651 O  O   . HOH   I 6 .   ? -29.716 -5.021  -0.809  1.00 42.69  ? 370 HOH   B O   1 
HETATM 1652 O  O   . HOH   I 6 .   ? -17.601 17.229  -22.005 1.00 43.88  ? 371 HOH   B O   1 
HETATM 1653 O  O   . HOH   I 6 .   ? -1.813  -14.376 -9.913  1.00 62.15  ? 372 HOH   B O   1 
HETATM 1654 O  O   . HOH   I 6 .   ? -30.578 -7.199  -4.928  1.00 46.17  ? 373 HOH   B O   1 
HETATM 1655 O  O   . HOH   I 6 .   ? -19.144 -11.552 -13.736 1.00 37.33  ? 374 HOH   B O   1 
HETATM 1656 O  O   . HOH   I 6 .   ? -30.174 -6.581  -20.214 1.00 55.99  ? 375 HOH   B O   1 
HETATM 1657 O  O   . HOH   I 6 .   ? -11.947 13.144  -15.065 1.00 62.26  ? 376 HOH   B O   1 
HETATM 1658 O  O   . HOH   I 6 .   ? -11.231 -6.568  2.117   1.00 52.00  ? 377 HOH   B O   1 
HETATM 1659 O  O   . HOH   I 6 .   ? -30.214 -12.040 -27.550 0.50 34.50  ? 378 HOH   B O   1 
HETATM 1660 O  O   . HOH   I 6 .   ? -12.826 -6.425  -8.305  1.00 54.52  ? 379 HOH   B O   1 
HETATM 1661 O  O   . HOH   I 6 .   ? -16.806 -10.867 -12.401 1.00 52.90  ? 380 HOH   B O   1 
HETATM 1662 O  O   . HOH   I 6 .   ? -17.761 28.604  -14.050 1.00 47.00  ? 381 HOH   B O   1 
HETATM 1663 O  O   . HOH   I 6 .   ? -13.573 -7.420  -3.325  1.00 45.28  ? 382 HOH   B O   1 
HETATM 1664 O  O   . HOH   I 6 .   ? -21.806 5.038   -0.422  0.50 32.66  ? 383 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 0.7883 0.3834 0.6427 0.0588  -0.0381 -0.0960 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.7768 0.4024 0.6164 0.0813  -0.0333 -0.0970 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.7417 0.3769 0.5798 0.0792  -0.0196 -0.0735 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.7705 0.3682 0.5972 0.0819  -0.0175 -0.0603 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.8391 0.4389 0.6583 0.1075  -0.0444 -0.1129 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.9161 0.5595 0.7283 0.1299  -0.0409 -0.1204 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 0.9302 0.6167 0.7484 0.1308  -0.0385 -0.1304 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 0.9494 0.5845 0.7505 0.1468  -0.0405 -0.1162 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.6754 0.3579 0.5220 0.0758  -0.0110 -0.0686 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.6319 0.3264 0.4776 0.0740  -0.0001 -0.0495 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.5916 0.2975 0.4252 0.0958  -0.0007 -0.0515 51  MET   A C   
12   O  O   . MET   A 8   ? 0.5764 0.3060 0.4103 0.1092  -0.0049 -0.0668 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.6135 0.3477 0.4748 0.0590  0.0080  -0.0428 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.6278 0.3539 0.5046 0.0376  0.0092  -0.0382 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.6118 0.3865 0.5040 0.0257  0.0159  -0.0336 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.6211 0.3845 0.5357 0.0032  0.0145  -0.0317 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.5680 0.2582 0.3911 0.1006  0.0033  -0.0364 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.5691 0.2703 0.3823 0.1223  0.0001  -0.0393 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.5572 0.2713 0.3686 0.1201  0.0071  -0.0238 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.5599 0.2627 0.3709 0.1053  0.0153  -0.0082 52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.5996 0.2575 0.3910 0.1432  -0.0094 -0.0431 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.6390 0.2446 0.4120 0.1385  -0.0058 -0.0237 52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.6777 0.2448 0.4522 0.1223  -0.0050 -0.0198 52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.6670 0.2580 0.4191 0.1528  -0.0044 -0.0106 52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7112 0.2293 0.4706 0.1158  0.0011  0.0006  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7081 0.2487 0.4384 0.1503  0.0014  0.0099  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.7400 0.2437 0.4747 0.1308  0.0055  0.0166  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8026 0.2582 0.5189 0.1246  0.0150  0.0401  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.5386 0.2795 0.3512 0.1349  0.0034  -0.0297 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.5259 0.2782 0.3353 0.1356  0.0068  -0.0186 53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.5416 0.2731 0.3287 0.1600  -0.0014 -0.0174 53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.5405 0.2657 0.3224 0.1786  -0.0111 -0.0298 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.5023 0.3028 0.3338 0.1292  0.0083  -0.0254 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.4981 0.3264 0.3416 0.1441  0.0006  -0.0432 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.4868 0.3035 0.3336 0.1076  0.0161  -0.0243 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.4803 0.3552 0.3488 0.1356  0.0034  -0.0481 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.5516 0.2721 0.3228 0.1625  0.0022  -0.0030 54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.5808 0.2796 0.3244 0.1880  -0.0059 -0.0001 54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.5796 0.3024 0.3231 0.1911  -0.0068 0.0021  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.5742 0.3013 0.3198 0.1753  0.0041  0.0142  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.6581 0.3021 0.3688 0.1909  0.0011  0.0202  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.7810 0.3889 0.4899 0.1826  0.0034  0.0222  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.9228 0.4733 0.5982 0.1865  0.0106  0.0444  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.9670 0.5137 0.6286 0.1834  0.0219  0.0628  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.0018 0.5098 0.6633 0.1935  0.0057  0.0438  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.5732 0.3121 0.3150 0.2127  -0.0210 -0.0108 55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.5757 0.3364 0.3188 0.2163  -0.0252 -0.0121 55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.6014 0.3295 0.3072 0.2235  -0.0181 0.0076  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.6444 0.3333 0.3177 0.2384  -0.0171 0.0183  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.6086 0.3918 0.3587 0.2392  -0.0446 -0.0319 55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.6383 0.4530 0.4050 0.2359  -0.0513 -0.0399 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.6673 0.5169 0.4595 0.2496  -0.0700 -0.0635 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.6626 0.5416 0.4785 0.2402  -0.0763 -0.0722 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.6704 0.5417 0.4667 0.2556  -0.0881 -0.0746 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.6950 0.5324 0.4455 0.2822  -0.0933 -0.0673 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.6168 0.5109 0.4361 0.2454  -0.0948 -0.0838 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.5869 0.3295 0.2952 0.2145  -0.0126 0.0130  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.6194 0.3381 0.2927 0.2228  -0.0037 0.0314  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.6312 0.3634 0.2910 0.2421  -0.0161 0.0231  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.6639 0.3758 0.2867 0.2574  -0.0112 0.0362  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.6188 0.3404 0.3032 0.1971  0.0158  0.0466  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.6023 0.3684 0.2923 0.2400  -0.0308 0.0022  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.6185 0.3959 0.2997 0.2578  -0.0466 -0.0097 57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.5997 0.4142 0.3234 0.2437  -0.0574 -0.0288 57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.5790 0.4132 0.3385 0.2208  -0.0516 -0.0322 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.6053 0.4277 0.3236 0.2592  -0.0747 -0.0422 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.5882 0.4398 0.3447 0.2459  -0.0862 -0.0597 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.5922 0.4395 0.3451 0.2310  -0.0743 -0.0489 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.6311 0.4571 0.3470 0.2414  -0.0642 -0.0339 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.6211 0.4781 0.3705 0.2706  -0.1125 -0.0802 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.6994 0.5695 0.4597 0.2881  -0.1304 -0.0973 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.7116 0.5808 0.4765 0.2856  -0.1216 -0.0914 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.7366 0.6174 0.4996 0.3067  -0.1550 -0.1180 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.5625 0.4298 0.3516 0.2100  -0.0768 -0.0574 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.5695 0.4327 0.3565 0.1984  -0.0696 -0.0506 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.5924 0.4547 0.3757 0.2119  -0.0908 -0.0676 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.5725 0.4507 0.3906 0.2018  -0.1052 -0.0844 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.5614 0.4405 0.3851 0.1679  -0.0585 -0.0472 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.5753 0.4523 0.3973 0.1582  -0.0399 -0.0324 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.5701 0.4443 0.3928 0.1584  -0.0552 -0.0429 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.5732 0.4686 0.4290 0.1330  -0.0312 -0.0320 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.6237 0.4676 0.3648 0.2355  -0.0930 -0.0638 60  THR   A N   
83   N  N   B THR   A 17  ? 0.6183 0.4621 0.3592 0.2356  -0.0931 -0.0639 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.6518 0.4906 0.3809 0.2536  -0.1148 -0.0814 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.6412 0.4799 0.3693 0.2551  -0.1157 -0.0820 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.6940 0.5162 0.3839 0.2673  -0.1059 -0.0706 60  THR   A C   
87   C  C   B THR   A 17  ? 0.6909 0.5124 0.3779 0.2705  -0.1077 -0.0718 60  THR   A C   
88   O  O   A THR   A 17  ? 0.7138 0.5282 0.3775 0.2713  -0.0846 -0.0497 60  THR   A O   
89   O  O   B THR   A 17  ? 0.7137 0.5257 0.3698 0.2788  -0.0884 -0.0519 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.6843 0.5198 0.3922 0.2843  -0.1359 -0.0962 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.6572 0.4935 0.3655 0.2842  -0.1344 -0.0948 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.7280 0.5455 0.3894 0.3051  -0.1226 -0.0783 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.6424 0.4986 0.3886 0.2735  -0.1410 -0.1046 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.6635 0.5217 0.4138 0.2764  -0.1511 -0.1139 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.6634 0.4947 0.3563 0.3083  -0.1619 -0.1172 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.7094 0.5267 0.3960 0.2755  -0.1227 -0.0859 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 0.7610 0.5650 0.4077 0.2947  -0.1172 -0.0797 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 0.8245 0.6168 0.4211 0.3327  -0.1251 -0.0824 61  TRP   A C   
99   O  O   . TRP   A 18  ? 0.8350 0.6274 0.4329 0.3469  -0.1495 -0.1023 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 0.7561 0.5544 0.4145 0.2937  -0.1368 -0.0989 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 0.7767 0.5623 0.3949 0.3169  -0.1347 -0.0973 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 0.8064 0.5801 0.3818 0.3531  -0.1506 -0.1104 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 0.7746 0.5600 0.3929 0.3074  -0.1184 -0.0851 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 0.8226 0.5898 0.3709 0.3670  -0.1430 -0.1061 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 0.8042 0.5792 0.3801 0.3392  -0.1239 -0.0911 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 0.7606 0.5551 0.4079 0.2781  -0.0997 -0.0698 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 0.8139 0.5897 0.3794 0.3420  -0.1109 -0.0827 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 0.7815 0.5749 0.4191 0.2806  -0.0899 -0.0629 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 0.8014 0.5867 0.3997 0.3121  -0.0949 -0.0691 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 0.8592 0.6431 0.4123 0.3498  -0.1043 -0.0623 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 0.9116 0.6816 0.4099 0.3879  -0.1088 -0.0614 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 0.9574 0.7208 0.4202 0.4148  -0.1171 -0.0710 62  GLU   A C   
113  O  O   . GLU   A 19  ? 0.9437 0.7111 0.4009 0.4103  -0.0981 -0.0583 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 0.9558 0.7188 0.4263 0.3900  -0.0778 -0.0302 62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.0651 0.8100 0.4713 0.4309  -0.0781 -0.0242 62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.1512 0.8863 0.5236 0.4344  -0.0432 0.0099  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.1630 0.9074 0.5656 0.4036  -0.0188 0.0282  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.1892 0.9068 0.5046 0.4683  -0.0403 0.0185  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.0018 0.7564 0.4411 0.4445  -0.1469 -0.0955 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.0559 0.8016 0.4560 0.4753  -0.1585 -0.1084 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.1036 0.8434 0.4428 0.5034  -0.1315 -0.0834 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.1259 0.8593 0.4401 0.5131  -0.1202 -0.0672 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.1123 0.8497 0.5015 0.5019  -0.1996 -0.1428 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.1846 0.9244 0.6252 0.4807  -0.2274 -0.1713 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.2682 0.9976 0.6911 0.5123  -0.2695 -0.2080 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.3079 1.0334 0.7780 0.4915  -0.2953 -0.2346 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.3523 1.0640 0.7999 0.5250  -0.3364 -0.2715 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.1218 0.8644 0.4396 0.5145  -0.1188 -0.0783 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.1503 0.8930 0.4138 0.5397  -0.0892 -0.0530 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.1218 0.8717 0.4002 0.5129  -0.0520 -0.0175 64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.1412 0.8817 0.3790 0.5296  -0.0342 0.0035  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.2326 0.9587 0.4286 0.5887  -0.1037 -0.0614 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.3518 1.0698 0.5308 0.6176  -0.1421 -0.0987 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.3861 1.1095 0.5754 0.6156  -0.1440 -0.1084 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.4027 1.1080 0.5579 0.6436  -0.1718 -0.1196 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.0715 0.8354 0.4078 0.4710  -0.0417 -0.0113 65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.0403 0.8117 0.3951 0.4441  -0.0087 0.0191  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.0295 0.8168 0.3665 0.4506  0.0223  0.0394  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.0337 0.8285 0.3549 0.4705  0.0156  0.0269  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.0126 0.7948 0.4318 0.4014  -0.0113 0.0153  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.0231 0.8167 0.3649 0.4341  0.0557  0.0696  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.0246 0.8409 0.3596 0.4362  0.0876  0.0897  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 0.9818 0.8230 0.3631 0.4160  0.0836  0.0776  66  GLU   A C   
144  O  O   . GLU   A 23  ? 0.9404 0.7830 0.3687 0.3842  0.0747  0.0716  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.0766 0.8942 0.4221 0.4133  0.1217  0.1227  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.1662 1.0127 0.5120 0.4122  0.1573  0.1449  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.2678 1.1269 0.6605 0.3717  0.1837  0.1676  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.2975 1.1333 0.7036 0.3517  0.1803  0.1735  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.2873 1.1806 0.7045 0.3612  0.2063  0.1779  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 0.9845 0.8424 0.3479 0.4385  0.0871  0.0718  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 0.9651 0.8428 0.3652 0.4258  0.0808  0.0592  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 0.9378 0.8514 0.3557 0.4162  0.1151  0.0805  67  VAL   A C   
153  O  O   . VAL   A 24  ? 0.9539 0.8822 0.3370 0.4431  0.1346  0.0909  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 0.9981 0.8676 0.3694 0.4594  0.0547  0.0321  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 0.9872 0.8662 0.3966 0.4442  0.0430  0.0179  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.0325 0.8696 0.3812 0.4747  0.0214  0.0102  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 0.8984 0.8294 0.3707 0.3798  0.1221  0.0858  68  THR   A N   
158  C  CA  . THR   A 25  ? 0.8700 0.8401 0.3674 0.3688  0.1522  0.1033  68  THR   A CA  
159  C  C   . THR   A 25  ? 0.8300 0.8182 0.3824 0.3393  0.1457  0.0960  68  THR   A C   
160  O  O   . THR   A 25  ? 0.8223 0.7902 0.3889 0.3279  0.1203  0.0797  68  THR   A O   
161  C  CB  . THR   A 25  ? 0.8941 0.8685 0.3900 0.3559  0.1841  0.1330  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 0.8902 0.9077 0.4047 0.3533  0.2141  0.1482  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 0.8864 0.8449 0.4187 0.3182  0.1815  0.1391  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 0.8043 0.8319 0.3861 0.3288  0.1685  0.1077  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 0.7823 0.8296 0.4125 0.3048  0.1626  0.1010  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 0.7859 0.8469 0.4108 0.3279  0.1493  0.0835  69  GLY   A C   
167  O  O   . GLY   A 26  ? 0.8193 0.8577 0.4062 0.3562  0.1316  0.0687  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.7507 0.8472 0.4129 0.3174  0.1559  0.0834  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.7470 0.8548 0.4057 0.3395  0.1419  0.0666  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.7266 0.8077 0.4022 0.3239  0.1135  0.0515  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.7148 0.7705 0.4018 0.2984  0.1055  0.0535  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.7630 0.9287 0.4469 0.3455  0.1654  0.0740  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.8033 0.9981 0.5427 0.3098  0.1759  0.0831  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.8180 1.0014 0.5738 0.2808  0.1838  0.0954  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.8053 1.0381 0.5742 0.3130  0.1748  0.0758  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.7087 0.7933 0.3833 0.3406  0.0986  0.0371  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.7071 0.7618 0.3908 0.3292  0.0728  0.0249  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.6867 0.7726 0.3974 0.3295  0.0725  0.0219  71  SER   A C   
179  O  O   . SER   A 28  ? 0.6922 0.7694 0.3880 0.3528  0.0570  0.0089  71  SER   A O   
180  C  CB  . SER   A 28  ? 0.7366 0.7478 0.3826 0.3532  0.0476  0.0075  71  SER   A CB  
181  O  OG  . SER   A 28  ? 0.7653 0.7595 0.3801 0.3665  0.0485  0.0069  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.6508 0.7725 0.4012 0.3053  0.0881  0.0327  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.6263 0.7846 0.4040 0.3086  0.0872  0.0284  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.6213 0.7502 0.3997 0.3028  0.0627  0.0188  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.6255 0.7214 0.4049 0.2795  0.0543  0.0212  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.6157 0.8176 0.4372 0.2817  0.1095  0.0417  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.6334 0.8012 0.4513 0.2553  0.1117  0.0509  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.6378 0.7684 0.4098 0.2761  0.1060  0.0481  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.6137 0.7555 0.3909 0.3246  0.0523  0.0089  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.6360 0.7503 0.4106 0.3221  0.0304  0.0020  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.6047 0.7668 0.4193 0.3107  0.0357  0.0037  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.5798 0.7893 0.4105 0.3290  0.0418  -0.0007 73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.6887 0.7766 0.4298 0.3569  0.0114  -0.0111 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.7773 0.8086 0.4805 0.3648  -0.0008 -0.0163 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 0.8722 0.8740 0.5431 0.3997  -0.0212 -0.0308 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 0.9478 0.9077 0.5846 0.4143  -0.0317 -0.0396 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 0.9988 0.8976 0.6177 0.4060  -0.0520 -0.0448 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.0193 0.8908 0.6479 0.3835  -0.0611 -0.0393 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 0.9845 0.8501 0.5761 0.4203  -0.0633 -0.0557 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.5967 0.7501 0.4294 0.2810  0.0336  0.0088  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.5658 0.7639 0.4381 0.2681  0.0370  0.0085  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.5738 0.7493 0.4404 0.2645  0.0173  0.0038  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.5990 0.7261 0.4443 0.2521  0.0090  0.0073  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.5511 0.7657 0.4529 0.2357  0.0546  0.0187  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.5656 0.7970 0.4699 0.2355  0.0772  0.0278  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.5691 0.7836 0.4820 0.2052  0.0879  0.0386  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.5484 0.8451 0.4854 0.2455  0.0935  0.0277  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.5472 0.7609 0.4347 0.2748  0.0106  -0.0037 75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.5579 0.7545 0.4382 0.2740  -0.0079 -0.0078 75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5240 0.7376 0.4354 0.2421  -0.0020 -0.0046 75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.4942 0.7603 0.4477 0.2325  0.0087  -0.0068 75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.5823 0.8168 0.4724 0.3017  -0.0195 -0.0193 75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7096 0.9166 0.5616 0.3376  -0.0320 -0.0247 75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.7539 0.9270 0.5801 0.3427  -0.0278 -0.0212 75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.7624 0.9803 0.6092 0.3621  -0.0477 -0.0336 75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.5231 0.6930 0.4156 0.2250  -0.0080 0.0004  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.4914 0.6730 0.4090 0.1972  -0.0037 0.0016  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.4918 0.6498 0.3917 0.1953  -0.0196 -0.0008 76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.5203 0.6396 0.3828 0.2102  -0.0308 0.0014  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5016 0.6632 0.4208 0.1736  0.0117  0.0112  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5012 0.6799 0.4282 0.1785  0.0279  0.0157  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.5328 0.6379 0.4156 0.1694  0.0060  0.0167  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.4566 0.6369 0.3823 0.1778  -0.0204 -0.0053 77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.4620 0.6249 0.3715 0.1755  -0.0336 -0.0083 77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.4534 0.6015 0.3697 0.1481  -0.0249 -0.0044 77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.4435 0.6108 0.3903 0.1311  -0.0127 -0.0037 77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.4445 0.6522 0.3787 0.1848  -0.0472 -0.0226 77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.4557 0.5678 0.3415 0.1450  -0.0298 -0.0005 78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.4482 0.5458 0.3367 0.1232  -0.0228 0.0019  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.4513 0.5551 0.3342 0.1247  -0.0354 -0.0070 78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.4750 0.5595 0.3238 0.1402  -0.0447 -0.0047 78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.4666 0.5185 0.3230 0.1201  -0.0162 0.0140  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.4865 0.5218 0.3399 0.1021  -0.0099 0.0165  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.4600 0.5120 0.3452 0.0850  -0.0004 0.0137  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.5267 0.5231 0.3530 0.1002  -0.0046 0.0274  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.4257 0.5542 0.3395 0.1104  -0.0367 -0.0173 79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.4361 0.5706 0.3430 0.1140  -0.0511 -0.0289 79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.4449 0.5476 0.3259 0.1051  -0.0465 -0.0247 79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.4566 0.5362 0.3315 0.0941  -0.0325 -0.0138 79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.4284 0.6069 0.3819 0.1064  -0.0604 -0.0465 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.4409 0.6259 0.4311 0.0803  -0.0499 -0.0484 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.4373 0.5909 0.4119 0.0694  -0.0380 -0.0388 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.4323 0.6535 0.4679 0.0707  -0.0539 -0.0597 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.4478 0.5519 0.3131 0.1123  -0.0591 -0.0347 80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.4671 0.5471 0.3061 0.1081  -0.0551 -0.0326 80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.4613 0.5412 0.3270 0.0867  -0.0465 -0.0367 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.4828 0.5401 0.3300 0.0815  -0.0368 -0.0301 80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.4997 0.5854 0.3143 0.1249  -0.0721 -0.0447 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.5826 0.6455 0.3632 0.1256  -0.0669 -0.0420 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.6677 0.7333 0.4138 0.1477  -0.0831 -0.0516 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.6643 0.7455 0.4209 0.1481  -0.0960 -0.0713 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.7031 0.7535 0.4106 0.1658  -0.0843 -0.0400 80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.4258 0.5294 0.3356 0.0740  -0.0480 -0.0453 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.4236 0.5206 0.3563 0.0542  -0.0397 -0.0472 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.4105 0.4921 0.3469 0.0448  -0.0213 -0.0308 81  SER   A C   
256  O  O   . SER   A 38  ? 0.4139 0.4875 0.3667 0.0305  -0.0138 -0.0302 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.4289 0.5534 0.4071 0.0423  -0.0483 -0.0621 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.4969 0.6334 0.4717 0.0510  -0.0681 -0.0808 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.3937 0.4684 0.3124 0.0546  -0.0158 -0.0186 82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.4059 0.4659 0.3245 0.0492  -0.0015 -0.0055 82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.3993 0.4793 0.3485 0.0438  0.0049  -0.0034 82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.4102 0.4791 0.3609 0.0387  0.0166  0.0057  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.3792 0.4910 0.3524 0.0464  -0.0025 -0.0117 83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.3857 0.5235 0.3914 0.0413  0.0062  -0.0089 83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.3982 0.5495 0.3953 0.0600  0.0058  -0.0050 83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4084 0.5690 0.3950 0.0752  -0.0073 -0.0117 83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.3974 0.5676 0.4457 0.0290  0.0000  -0.0217 83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.4955 0.6481 0.5542 0.0102  0.0006  -0.0258 83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5358 0.6611 0.5830 0.0031  0.0129  -0.0150 83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.5345 0.6991 0.6110 0.0048  -0.0131 -0.0413 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.3954 0.5453 0.3929 0.0616  0.0195  0.0054  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.3986 0.5619 0.3893 0.0808  0.0199  0.0078  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.3991 0.6132 0.4319 0.0800  0.0231  0.0022  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.3826 0.6139 0.4487 0.0612  0.0335  0.0036  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.3916 0.5327 0.3627 0.0852  0.0325  0.0194  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.4017 0.4990 0.3346 0.0902  0.0277  0.0235  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.4221 0.5044 0.3290 0.1077  0.0171  0.0225  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.4125 0.4834 0.3372 0.0774  0.0336  0.0284  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.4494 0.4916 0.3264 0.1087  0.0139  0.0272  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.4348 0.4715 0.3316 0.0805  0.0298  0.0314  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.4459 0.4685 0.3206 0.0942  0.0206  0.0312  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4132 0.6507 0.4455 0.1006  0.0150  -0.0034 85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4066 0.6993 0.4812 0.1034  0.0188  -0.0093 85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4397 0.7432 0.4977 0.1316  0.0188  -0.0083 85  SER   A C   
285  O  O   . SER   A 42  ? 0.4588 0.7277 0.4748 0.1498  0.0080  -0.0075 85  SER   A O   
286  C  CB  . SER   A 42  ? 0.3937 0.7188 0.4970 0.1012  0.0015  -0.0257 85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.4381 0.7474 0.5068 0.1238  -0.0181 -0.0323 85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4407 0.7925 0.5323 0.1357  0.0309  -0.0085 86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.4767 0.8439 0.5543 0.1656  0.0310  -0.0097 86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5074 0.9002 0.5897 0.1875  0.0098  -0.0248 86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.4827 0.9173 0.6062 0.1787  0.0029  -0.0357 86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4564 0.8727 0.5697 0.1638  0.0539  -0.0045 86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.4949 0.8885 0.5976 0.1499  0.0767  0.0120  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.4815 0.9289 0.6199 0.1493  0.1012  0.0185  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.5352 0.8772 0.5809 0.1694  0.0735  0.0172  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5557 0.9236 0.5968 0.2172  -0.0016 -0.0264 87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.5864 0.9751 0.6256 0.2437  -0.0224 -0.0399 87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6030 1.0409 0.6620 0.2672  -0.0149 -0.0447 87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6189 1.0382 0.6535 0.2792  -0.0040 -0.0373 87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6374 0.9632 0.6162 0.2634  -0.0405 -0.0377 87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6439 0.9883 0.6158 0.2951  -0.0625 -0.0507 87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6647 0.9446 0.6229 0.2409  -0.0442 -0.0313 87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5976 1.1013 0.7025 0.2742  -0.0205 -0.0583 88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.6036 1.1636 0.7320 0.2988  -0.0126 -0.0644 88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.6129 1.1987 0.7399 0.3335  -0.0378 -0.0819 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.6288 1.2050 0.7514 0.3334  -0.0596 -0.0904 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.6012 1.2314 0.7984 0.2743  0.0111  -0.0630 88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.6835 1.2860 0.8815 0.2399  0.0350  -0.0449 88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.7943 1.3901 0.9710 0.2503  0.0587  -0.0316 88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.8047 1.4377 0.9835 0.2803  0.0624  -0.0371 88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.8432 1.3975 0.9996 0.2309  0.0728  -0.0167 88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.7337 0.6694 0.6295 0.1730  -0.0092 -0.0823 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.7502 0.6629 0.6375 0.1685  -0.0095 -0.0765 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.7434 0.6640 0.6422 0.1684  -0.0146 -0.0771 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.7369 0.6824 0.6546 0.1682  -0.0183 -0.0816 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.7372 0.6368 0.6245 0.1690  -0.0152 -0.0725 17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.7171 0.6217 0.6126 0.1705  -0.0210 -0.0735 17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.6852 0.6023 0.5990 0.1546  -0.0204 -0.0693 17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.6918 0.5996 0.6021 0.1446  -0.0154 -0.0621 17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.7580 0.6383 0.6338 0.1797  -0.0221 -0.0705 17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 0.7967 0.6836 0.6794 0.1853  -0.0301 -0.0741 17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 0.8748 0.7406 0.7372 0.1978  -0.0316 -0.0717 17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 0.8946 0.7401 0.7398 0.1973  -0.0247 -0.0641 17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 0.8844 0.7540 0.7477 0.2086  -0.0398 -0.0775 17  GLU   B OE2 
325  N  N   A THR   B 9   ? 0.6583 0.5968 0.5919 0.1522  -0.0257 -0.0738 18  THR   B N   
326  N  N   B THR   B 9   ? 0.6551 0.5937 0.5889 0.1521  -0.0257 -0.0738 18  THR   B N   
327  C  CA  A THR   B 9   ? 0.6422 0.5915 0.5932 0.1372  -0.0259 -0.0699 18  THR   B CA  
328  C  CA  B THR   B 9   ? 0.6358 0.5855 0.5872 0.1374  -0.0261 -0.0701 18  THR   B CA  
329  C  C   A THR   B 9   ? 0.6235 0.5716 0.5807 0.1387  -0.0347 -0.0723 18  THR   B C   
330  C  C   B THR   B 9   ? 0.6209 0.5686 0.5778 0.1387  -0.0347 -0.0722 18  THR   B C   
331  O  O   A THR   B 9   ? 0.6221 0.5773 0.5934 0.1272  -0.0366 -0.0699 18  THR   B O   
332  O  O   B THR   B 9   ? 0.6199 0.5743 0.5905 0.1271  -0.0365 -0.0697 18  THR   B O   
333  C  CB  A THR   B 9   ? 0.6508 0.6261 0.6221 0.1284  -0.0232 -0.0709 18  THR   B CB  
334  C  CB  B THR   B 9   ? 0.6355 0.6122 0.6078 0.1305  -0.0249 -0.0725 18  THR   B CB  
335  O  OG1 A THR   B 9   ? 0.6667 0.6504 0.6340 0.1374  -0.0207 -0.0755 18  THR   B OG1 
336  O  OG1 B THR   B 9   ? 0.6344 0.6263 0.6160 0.1402  -0.0319 -0.0812 18  THR   B OG1 
337  C  CG2 A THR   B 9   ? 0.6539 0.6300 0.6294 0.1134  -0.0164 -0.0629 18  THR   B CG2 
338  C  CG2 B THR   B 9   ? 0.6431 0.6228 0.6095 0.1293  -0.0166 -0.0704 18  THR   B CG2 
339  N  N   . THR   B 10  ? 0.6108 0.5480 0.5556 0.1535  -0.0406 -0.0768 19  THR   B N   
340  C  CA  . THR   B 10  ? 0.5779 0.5114 0.5247 0.1582  -0.0502 -0.0802 19  THR   B CA  
341  C  C   . THR   B 10  ? 0.5456 0.4653 0.4861 0.1505  -0.0480 -0.0724 19  THR   B C   
342  O  O   . THR   B 10  ? 0.5519 0.4590 0.4786 0.1486  -0.0397 -0.0651 19  THR   B O   
343  C  CB  . THR   B 10  ? 0.5988 0.5192 0.5264 0.1782  -0.0547 -0.0850 19  THR   B CB  
344  O  OG1 . THR   B 10  ? 0.6179 0.5488 0.5468 0.1870  -0.0552 -0.0916 19  THR   B OG1 
345  C  CG2 . THR   B 10  ? 0.6067 0.5251 0.5356 0.1865  -0.0664 -0.0908 19  THR   B CG2 
346  N  N   . ASP   B 11  ? 0.5115 0.4346 0.4636 0.1449  -0.0556 -0.0738 20  ASP   B N   
347  C  CA  . ASP   B 11  ? 0.5043 0.4150 0.4500 0.1402  -0.0557 -0.0680 20  ASP   B CA  
348  C  C   . ASP   B 11  ? 0.5056 0.3979 0.4272 0.1544  -0.0543 -0.0653 20  ASP   B C   
349  O  O   . ASP   B 11  ? 0.5226 0.4106 0.4341 0.1690  -0.0574 -0.0700 20  ASP   B O   
350  C  CB  . ASP   B 11  ? 0.5232 0.4365 0.4814 0.1378  -0.0680 -0.0731 20  ASP   B CB  
351  C  CG  . ASP   B 11  ? 0.5704 0.4968 0.5510 0.1201  -0.0685 -0.0717 20  ASP   B CG  
352  O  OD1 . ASP   B 11  ? 0.5408 0.4782 0.5288 0.1107  -0.0593 -0.0675 20  ASP   B OD1 
353  O  OD2 . ASP   B 11  ? 0.5909 0.5150 0.5804 0.1161  -0.0785 -0.0745 20  ASP   B OD2 
354  N  N   . GLY   B 12  ? 0.4793 0.3622 0.3918 0.1504  -0.0493 -0.0576 21  GLY   B N   
355  C  CA  . GLY   B 12  ? 0.4802 0.3485 0.3716 0.1622  -0.0466 -0.0533 21  GLY   B CA  
356  C  C   . GLY   B 12  ? 0.4745 0.3382 0.3587 0.1544  -0.0356 -0.0433 21  GLY   B C   
357  O  O   . GLY   B 12  ? 0.4521 0.3227 0.3467 0.1401  -0.0309 -0.0403 21  GLY   B O   
358  N  N   . VAL   B 13  ? 0.4744 0.3272 0.3409 0.1641  -0.0314 -0.0381 22  VAL   B N   
359  C  CA  . VAL   B 13  ? 0.4736 0.3229 0.3336 0.1575  -0.0211 -0.0285 22  VAL   B CA  
360  C  C   . VAL   B 13  ? 0.4734 0.3160 0.3262 0.1575  -0.0134 -0.0257 22  VAL   B C   
361  O  O   . VAL   B 13  ? 0.4893 0.3247 0.3328 0.1694  -0.0151 -0.0288 22  VAL   B O   
362  C  CB  . VAL   B 13  ? 0.4881 0.3322 0.3351 0.1664  -0.0208 -0.0231 22  VAL   B CB  
363  C  CG1 . VAL   B 13  ? 0.4880 0.3222 0.3178 0.1845  -0.0217 -0.0233 22  VAL   B CG1 
364  C  CG2 . VAL   B 13  ? 0.5003 0.3462 0.3455 0.1572  -0.0110 -0.0135 22  VAL   B CG2 
365  N  N   . TYR   B 14  ? 0.4508 0.2949 0.3078 0.1444  -0.0058 -0.0206 23  TYR   B N   
366  C  CA  . TYR   B 14  ? 0.4571 0.2929 0.3080 0.1423  0.0005  -0.0185 23  TYR   B CA  
367  C  C   . TYR   B 14  ? 0.4607 0.2917 0.3072 0.1341  0.0088  -0.0093 23  TYR   B C   
368  O  O   . TYR   B 14  ? 0.4633 0.3031 0.3175 0.1250  0.0102  -0.0062 23  TYR   B O   
369  C  CB  . TYR   B 14  ? 0.4514 0.2950 0.3143 0.1333  0.0000  -0.0239 23  TYR   B CB  
370  C  CG  . TYR   B 14  ? 0.4560 0.3068 0.3253 0.1401  -0.0069 -0.0329 23  TYR   B CG  
371  C  CD1 . TYR   B 14  ? 0.4558 0.3175 0.3361 0.1411  -0.0143 -0.0375 23  TYR   B CD1 
372  C  CD2 . TYR   B 14  ? 0.4762 0.3236 0.3413 0.1453  -0.0065 -0.0372 23  TYR   B CD2 
373  C  CE1 . TYR   B 14  ? 0.4591 0.3303 0.3484 0.1460  -0.0208 -0.0459 23  TYR   B CE1 
374  C  CE2 . TYR   B 14  ? 0.4885 0.3462 0.3609 0.1520  -0.0127 -0.0458 23  TYR   B CE2 
375  C  CZ  . TYR   B 14  ? 0.4950 0.3664 0.3814 0.1512  -0.0196 -0.0500 23  TYR   B CZ  
376  O  OH  . TYR   B 14  ? 0.5352 0.4193 0.4315 0.1569  -0.0261 -0.0586 23  TYR   B OH  
377  N  N   . ARG   B 15  ? 0.4562 0.2735 0.2913 0.1362  0.0141  -0.0051 24  ARG   B N   
378  C  CA  . ARG   B 15  ? 0.4630 0.2757 0.2964 0.1260  0.0218  0.0034  24  ARG   B CA  
379  C  C   . ARG   B 15  ? 0.4651 0.2791 0.3070 0.1136  0.0223  -0.0001 24  ARG   B C   
380  O  O   . ARG   B 15  ? 0.4526 0.2634 0.2940 0.1167  0.0191  -0.0069 24  ARG   B O   
381  C  CB  . ARG   B 15  ? 0.4926 0.2863 0.3096 0.1322  0.0270  0.0095  24  ARG   B CB  
382  C  CG  . ARG   B 15  ? 0.5131 0.3026 0.3171 0.1477  0.0272  0.0132  24  ARG   B CG  
383  C  CD  . ARG   B 15  ? 0.5279 0.2965 0.3138 0.1546  0.0328  0.0197  24  ARG   B CD  
384  N  NE  . ARG   B 15  ? 0.5666 0.3316 0.3384 0.1729  0.0314  0.0211  24  ARG   B NE  
385  C  CZ  . ARG   B 15  ? 0.6031 0.3720 0.3689 0.1779  0.0362  0.0298  24  ARG   B CZ  
386  N  NH1 . ARG   B 15  ? 0.5422 0.3199 0.3161 0.1652  0.0431  0.0384  24  ARG   B NH1 
387  N  NH2 . ARG   B 15  ? 0.6388 0.4040 0.3901 0.1967  0.0339  0.0296  24  ARG   B NH2 
388  N  N   . VAL   B 16  ? 0.4685 0.2869 0.3168 0.1010  0.0262  0.0045  25  VAL   B N   
389  C  CA  . VAL   B 16  ? 0.4744 0.2921 0.3282 0.0902  0.0266  0.0016  25  VAL   B CA  
390  C  C   . VAL   B 16  ? 0.4915 0.2936 0.3380 0.0844  0.0315  0.0077  25  VAL   B C   
391  O  O   . VAL   B 16  ? 0.4954 0.3004 0.3437 0.0790  0.0360  0.0156  25  VAL   B O   
392  C  CB  . VAL   B 16  ? 0.4572 0.2918 0.3240 0.0801  0.0261  0.0013  25  VAL   B CB  
393  C  CG1 . VAL   B 16  ? 0.4647 0.2975 0.3350 0.0704  0.0263  -0.0018 25  VAL   B CG1 
394  C  CG2 . VAL   B 16  ? 0.4320 0.2793 0.3057 0.0845  0.0212  -0.0037 25  VAL   B CG2 
395  N  N   . MET   B 17  ? 0.5129 0.2982 0.3506 0.0864  0.0306  0.0044  26  MET   B N   
396  C  CA  . MET   B 17  ? 0.5413 0.3062 0.3698 0.0816  0.0342  0.0099  26  MET   B CA  
397  C  C   . MET   B 17  ? 0.5619 0.3196 0.3930 0.0710  0.0321  0.0058  26  MET   B C   
398  O  O   . MET   B 17  ? 0.5438 0.3083 0.3785 0.0723  0.0278  -0.0028 26  MET   B O   
399  C  CB  . MET   B 17  ? 0.5481 0.2925 0.3590 0.0952  0.0336  0.0092  26  MET   B CB  
400  C  CG  . MET   B 17  ? 0.5788 0.3280 0.3842 0.1094  0.0336  0.0107  26  MET   B CG  
401  S  SD  . MET   B 17  ? 0.5683 0.3191 0.3712 0.1081  0.0412  0.0242  26  MET   B SD  
402  C  CE  . MET   B 17  ? 0.5504 0.2714 0.3391 0.1025  0.0472  0.0329  26  MET   B CE  
403  N  N   . THR   B 18  ? 0.5963 0.3381 0.4238 0.0615  0.0350  0.0117  27  THR   B N   
404  C  CA  . THR   B 18  ? 0.6330 0.3622 0.4598 0.0527  0.0315  0.0071  27  THR   B CA  
405  C  C   . THR   B 18  ? 0.6703 0.3687 0.4830 0.0508  0.0329  0.0119  27  THR   B C   
406  O  O   . THR   B 18  ? 0.6511 0.3433 0.4610 0.0486  0.0388  0.0224  27  THR   B O   
407  C  CB  . THR   B 18  ? 0.6518 0.3971 0.4946 0.0380  0.0312  0.0075  27  THR   B CB  
408  O  OG1 . THR   B 18  ? 0.6925 0.4231 0.5324 0.0314  0.0263  0.0016  27  THR   B OG1 
409  C  CG2 . THR   B 18  ? 0.6422 0.3935 0.4927 0.0282  0.0372  0.0186  27  THR   B CG2 
410  N  N   . ARG   B 19  ? 0.7162 0.3942 0.5188 0.0518  0.0275  0.0048  28  ARG   B N   
411  C  CA  . ARG   B 19  ? 0.7766 0.4211 0.5648 0.0484  0.0275  0.0090  28  ARG   B CA  
412  C  C   . ARG   B 19  ? 0.8046 0.4408 0.6003 0.0311  0.0240  0.0079  28  ARG   B C   
413  O  O   . ARG   B 19  ? 0.8213 0.4267 0.6053 0.0266  0.0217  0.0093  28  ARG   B O   
414  C  CB  . ARG   B 19  ? 0.8292 0.4502 0.5960 0.0644  0.0230  0.0021  28  ARG   B CB  
415  C  CG  . ARG   B 19  ? 0.8990 0.5177 0.6546 0.0799  0.0267  0.0060  28  ARG   B CG  
416  C  CD  . ARG   B 19  ? 0.9865 0.5851 0.7215 0.0969  0.0216  -0.0020 28  ARG   B CD  
417  N  NE  . ARG   B 19  ? 1.0564 0.6572 0.7821 0.1134  0.0238  -0.0002 28  ARG   B NE  
418  C  CZ  . ARG   B 19  ? 1.1068 0.7255 0.8339 0.1277  0.0202  -0.0091 28  ARG   B CZ  
419  N  NH1 . ARG   B 19  ? 1.1013 0.7376 0.8384 0.1275  0.0155  -0.0192 28  ARG   B NH1 
420  N  NH2 . ARG   B 19  ? 1.1161 0.7360 0.8349 0.1424  0.0212  -0.0079 28  ARG   B NH2 
421  N  N   . ARG   B 20  ? 0.8153 0.4773 0.6295 0.0216  0.0229  0.0053  29  ARG   B N   
422  C  CA  . ARG   B 20  ? 0.8467 0.5053 0.6698 0.0061  0.0184  0.0027  29  ARG   B CA  
423  C  C   . ARG   B 20  ? 0.8561 0.5059 0.6859 -0.0096 0.0230  0.0145  29  ARG   B C   
424  O  O   . ARG   B 20  ? 0.8711 0.4993 0.6994 -0.0209 0.0185  0.0137  29  ARG   B O   
425  C  CB  . ARG   B 20  ? 0.8726 0.5637 0.7130 0.0022  0.0166  -0.0025 29  ARG   B CB  
426  C  CG  . ARG   B 20  ? 0.9602 0.6479 0.8072 -0.0100 0.0095  -0.0088 29  ARG   B CG  
427  C  CD  . ARG   B 20  ? 1.0295 0.7485 0.8910 -0.0118 0.0078  -0.0138 29  ARG   B CD  
428  N  NE  . ARG   B 20  ? 1.0821 0.8274 0.9585 -0.0165 0.0147  -0.0052 29  ARG   B NE  
429  C  CZ  . ARG   B 20  ? 1.1254 0.8798 1.0159 -0.0305 0.0165  0.0010  29  ARG   B CZ  
430  N  NH1 . ARG   B 20  ? 1.1318 0.8701 1.0249 -0.0433 0.0118  -0.0003 29  ARG   B NH1 
431  N  NH2 . ARG   B 20  ? 1.1177 0.8974 1.0197 -0.0317 0.0227  0.0082  29  ARG   B NH2 
432  N  N   . LEU   B 21  ? 0.8408 0.5070 0.6775 -0.0099 0.0318  0.0254  30  LEU   B N   
433  C  CA  . LEU   B 21  ? 0.8392 0.5032 0.6839 -0.0239 0.0385  0.0385  30  LEU   B CA  
434  C  C   . LEU   B 21  ? 0.8378 0.4685 0.6633 -0.0198 0.0430  0.0476  30  LEU   B C   
435  O  O   . LEU   B 21  ? 0.8473 0.4519 0.6533 -0.0087 0.0383  0.0413  30  LEU   B O   
436  C  CB  . LEU   B 21  ? 0.8359 0.5364 0.6959 -0.0235 0.0458  0.0456  30  LEU   B CB  
437  C  CG  . LEU   B 21  ? 0.8506 0.5817 0.7337 -0.0364 0.0447  0.0444  30  LEU   B CG  
438  C  CD1 . LEU   B 21  ? 0.8651 0.5925 0.7528 -0.0434 0.0344  0.0319  30  LEU   B CD1 
439  C  CD2 . LEU   B 21  ? 0.8478 0.6108 0.7374 -0.0264 0.0474  0.0438  30  LEU   B CD2 
440  N  N   . LEU   B 22  ? 0.8221 0.4536 0.6520 -0.0280 0.0522  0.0625  31  LEU   B N   
441  C  CA  . LEU   B 22  ? 0.8312 0.4318 0.6423 -0.0241 0.0579  0.0730  31  LEU   B CA  
442  C  C   . LEU   B 22  ? 0.8211 0.4232 0.6153 -0.0009 0.0607  0.0722  31  LEU   B C   
443  O  O   . LEU   B 22  ? 0.8142 0.4472 0.6172 0.0064  0.0641  0.0726  31  LEU   B O   
444  C  CB  . LEU   B 22  ? 0.8281 0.4376 0.6516 -0.0389 0.0684  0.0901  31  LEU   B CB  
445  C  CG  . LEU   B 22  ? 0.8573 0.4328 0.6642 -0.0412 0.0752  0.1037  31  LEU   B CG  
446  C  CD1 . LEU   B 22  ? 0.8717 0.4075 0.6709 -0.0532 0.0672  0.0999  31  LEU   B CD1 
447  C  CD2 . LEU   B 22  ? 0.8538 0.4485 0.6752 -0.0531 0.0878  0.1217  31  LEU   B CD2 
448  N  N   . GLY   B 23  ? 0.8089 0.3779 0.5788 0.0114  0.0581  0.0697  32  GLY   B N   
449  C  CA  . GLY   B 23  ? 0.7981 0.3668 0.5513 0.0343  0.0589  0.0671  32  GLY   B CA  
450  C  C   . GLY   B 23  ? 0.7636 0.3622 0.5264 0.0443  0.0534  0.0542  32  GLY   B C   
451  O  O   . GLY   B 23  ? 0.7466 0.3530 0.5191 0.0386  0.0463  0.0436  32  GLY   B O   
452  N  N   . SER   B 24  ? 0.7452 0.3601 0.5049 0.0595  0.0564  0.0552  33  SER   B N   
453  C  CA  . SER   B 24  ? 0.7263 0.3693 0.4961 0.0679  0.0516  0.0446  33  SER   B CA  
454  C  C   . SER   B 24  ? 0.6877 0.3602 0.4732 0.0633  0.0572  0.0516  33  SER   B C   
455  O  O   . SER   B 24  ? 0.6986 0.3717 0.4779 0.0692  0.0640  0.0617  33  SER   B O   
456  C  CB  . SER   B 24  ? 0.7609 0.3987 0.5150 0.0893  0.0485  0.0385  33  SER   B CB  
457  O  OG  . SER   B 24  ? 0.8046 0.4128 0.5408 0.0955  0.0441  0.0333  33  SER   B OG  
458  N  N   . THR   B 25  ? 0.6485 0.3447 0.4530 0.0535  0.0544  0.0467  34  THR   B N   
459  C  CA  . THR   B 25  ? 0.6136 0.3381 0.4332 0.0487  0.0589  0.0526  34  THR   B CA  
460  C  C   . THR   B 25  ? 0.5797 0.3273 0.4058 0.0579  0.0545  0.0444  34  THR   B C   
461  O  O   . THR   B 25  ? 0.5638 0.3148 0.3940 0.0578  0.0480  0.0338  34  THR   B O   
462  C  CB  . THR   B 25  ? 0.6301 0.3642 0.4671 0.0288  0.0591  0.0543  34  THR   B CB  
463  O  OG1 . THR   B 25  ? 0.6692 0.3801 0.5017 0.0179  0.0623  0.0618  34  THR   B OG1 
464  C  CG2 . THR   B 25  ? 0.6168 0.3819 0.4695 0.0242  0.0635  0.0602  34  THR   B CG2 
465  N  N   . GLN   B 26  ? 0.5518 0.3146 0.3784 0.0660  0.0579  0.0495  35  GLN   B N   
466  C  CA  . GLN   B 26  ? 0.5271 0.3101 0.3601 0.0736  0.0532  0.0425  35  GLN   B CA  
467  C  C   . GLN   B 26  ? 0.5199 0.3265 0.3702 0.0623  0.0530  0.0425  35  GLN   B C   
468  O  O   . GLN   B 26  ? 0.5219 0.3412 0.3773 0.0588  0.0584  0.0511  35  GLN   B O   
469  C  CB  . GLN   B 26  ? 0.5005 0.2869 0.3238 0.0900  0.0545  0.0457  35  GLN   B CB  
470  C  CG  . GLN   B 26  ? 0.4656 0.2701 0.2955 0.0970  0.0482  0.0381  35  GLN   B CG  
471  C  CD  . GLN   B 26  ? 0.5207 0.3266 0.3401 0.1140  0.0476  0.0396  35  GLN   B CD  
472  O  OE1 . GLN   B 26  ? 0.5278 0.3182 0.3328 0.1252  0.0481  0.0405  35  GLN   B OE1 
473  N  NE2 . GLN   B 26  ? 0.4778 0.3010 0.3026 0.1177  0.0453  0.0390  35  GLN   B NE2 
474  N  N   . VAL   B 27  ? 0.5115 0.3247 0.3699 0.0579  0.0472  0.0333  36  VAL   B N   
475  C  CA  . VAL   B 27  ? 0.5006 0.3344 0.3730 0.0489  0.0463  0.0324  36  VAL   B CA  
476  C  C   . VAL   B 27  ? 0.4723 0.3230 0.3476 0.0572  0.0435  0.0298  36  VAL   B C   
477  O  O   . VAL   B 27  ? 0.4606 0.3284 0.3447 0.0525  0.0435  0.0310  36  VAL   B O   
478  C  CB  . VAL   B 27  ? 0.5075 0.3393 0.3864 0.0388  0.0421  0.0251  36  VAL   B CB  
479  C  CG1 . VAL   B 27  ? 0.5359 0.3512 0.4132 0.0286  0.0440  0.0282  36  VAL   B CG1 
480  C  CG2 . VAL   B 27  ? 0.5153 0.3411 0.3892 0.0464  0.0368  0.0158  36  VAL   B CG2 
481  N  N   . GLY   B 28  ? 0.4513 0.2966 0.3189 0.0696  0.0403  0.0260  37  GLY   B N   
482  C  CA  . GLY   B 28  ? 0.4290 0.2867 0.2985 0.0773  0.0364  0.0234  37  GLY   B CA  
483  C  C   . GLY   B 28  ? 0.4377 0.2881 0.3001 0.0898  0.0317  0.0182  37  GLY   B C   
484  O  O   . GLY   B 28  ? 0.4572 0.2936 0.3107 0.0956  0.0326  0.0181  37  GLY   B O   
485  N  N   . VAL   B 29  ? 0.4150 0.2741 0.2813 0.0941  0.0261  0.0136  38  VAL   B N   
486  C  CA  . VAL   B 29  ? 0.4267 0.2824 0.2893 0.1054  0.0199  0.0079  38  VAL   B CA  
487  C  C   . VAL   B 29  ? 0.4195 0.2840 0.2926 0.1011  0.0139  0.0014  38  VAL   B C   
488  O  O   . VAL   B 29  ? 0.4112 0.2841 0.2911 0.0923  0.0148  0.0026  38  VAL   B O   
489  C  CB  . VAL   B 29  ? 0.4409 0.2978 0.2948 0.1175  0.0192  0.0118  38  VAL   B CB  
490  C  CG1 . VAL   B 29  ? 0.4415 0.2943 0.2911 0.1302  0.0111  0.0051  38  VAL   B CG1 
491  C  CG2 . VAL   B 29  ? 0.4512 0.3012 0.2948 0.1213  0.0268  0.0203  38  VAL   B CG2 
492  N  N   . GLY   B 30  ? 0.4163 0.2790 0.2909 0.1070  0.0081  -0.0051 39  GLY   B N   
493  C  CA  . GLY   B 30  ? 0.4196 0.2904 0.3050 0.1024  0.0028  -0.0099 39  GLY   B CA  
494  C  C   . GLY   B 30  ? 0.4304 0.3004 0.3176 0.1107  -0.0049 -0.0163 39  GLY   B C   
495  O  O   . GLY   B 30  ? 0.4439 0.3070 0.3229 0.1218  -0.0067 -0.0180 39  GLY   B O   
496  N  N   . VAL   B 31  ? 0.3957 0.2726 0.2937 0.1053  -0.0098 -0.0196 40  VAL   B N   
497  C  CA  . VAL   B 31  ? 0.4031 0.2813 0.3069 0.1102  -0.0185 -0.0259 40  VAL   B CA  
498  C  C   . VAL   B 31  ? 0.3966 0.2845 0.3143 0.1034  -0.0191 -0.0302 40  VAL   B C   
499  O  O   . VAL   B 31  ? 0.3819 0.2768 0.3079 0.0924  -0.0161 -0.0281 40  VAL   B O   
500  C  CB  . VAL   B 31  ? 0.4217 0.2989 0.3270 0.1087  -0.0244 -0.0251 40  VAL   B CB  
501  C  CG1 . VAL   B 31  ? 0.4192 0.2972 0.3335 0.1105  -0.0348 -0.0319 40  VAL   B CG1 
502  C  CG2 . VAL   B 31  ? 0.4400 0.3100 0.3307 0.1184  -0.0243 -0.0213 40  VAL   B CG2 
503  N  N   . MET   B 32  ? 0.3864 0.2762 0.3069 0.1108  -0.0237 -0.0366 41  MET   B N   
504  C  CA  . MET   B 32  ? 0.3929 0.2959 0.3284 0.1057  -0.0249 -0.0412 41  MET   B CA  
505  C  C   . MET   B 32  ? 0.4059 0.3130 0.3531 0.1048  -0.0349 -0.0454 41  MET   B C   
506  O  O   . MET   B 32  ? 0.4095 0.3098 0.3514 0.1152  -0.0428 -0.0496 41  MET   B O   
507  C  CB  . MET   B 32  ? 0.3960 0.2999 0.3275 0.1154  -0.0243 -0.0460 41  MET   B CB  
508  C  CG  . MET   B 32  ? 0.4203 0.3408 0.3664 0.1116  -0.0242 -0.0505 41  MET   B CG  
509  S  SD  . MET   B 32  ? 0.4421 0.3676 0.3888 0.1007  -0.0137 -0.0452 41  MET   B SD  
510  C  CE  . MET   B 32  ? 0.4327 0.3430 0.3600 0.1103  -0.0094 -0.0452 41  MET   B CE  
511  N  N   . GLN   B 33  ? 0.3847 0.3016 0.3467 0.0924  -0.0348 -0.0440 42  GLN   B N   
512  C  CA  . GLN   B 33  ? 0.3999 0.3195 0.3748 0.0882  -0.0442 -0.0472 42  GLN   B CA  
513  C  C   . GLN   B 33  ? 0.4005 0.3366 0.3945 0.0750  -0.0410 -0.0458 42  GLN   B C   
514  O  O   . GLN   B 33  ? 0.3973 0.3370 0.3909 0.0668  -0.0323 -0.0395 42  GLN   B O   
515  C  CB  . GLN   B 33  ? 0.4358 0.3411 0.4028 0.0872  -0.0488 -0.0440 42  GLN   B CB  
516  C  CG  . GLN   B 33  ? 0.4879 0.3921 0.4673 0.0831  -0.0604 -0.0482 42  GLN   B CG  
517  C  CD  . GLN   B 33  ? 0.5430 0.4301 0.5115 0.0854  -0.0672 -0.0467 42  GLN   B CD  
518  O  OE1 . GLN   B 33  ? 0.6052 0.4883 0.5805 0.0753  -0.0708 -0.0444 42  GLN   B OE1 
519  N  NE2 . GLN   B 33  ? 0.5114 0.3877 0.4615 0.0994  -0.0688 -0.0475 42  GLN   B NE2 
520  N  N   . GLU   B 34  ? 0.4025 0.3508 0.4134 0.0737  -0.0477 -0.0516 43  GLU   B N   
521  C  CA  . GLU   B 34  ? 0.4084 0.3765 0.4407 0.0610  -0.0447 -0.0498 43  GLU   B CA  
522  C  C   . GLU   B 34  ? 0.4224 0.4039 0.4542 0.0594  -0.0325 -0.0463 43  GLU   B C   
523  O  O   . GLU   B 34  ? 0.4354 0.4265 0.4756 0.0482  -0.0258 -0.0402 43  GLU   B O   
524  C  CB  . GLU   B 34  ? 0.4314 0.3936 0.4703 0.0474  -0.0462 -0.0436 43  GLU   B CB  
525  C  CG  . GLU   B 34  ? 0.5008 0.4495 0.5419 0.0479  -0.0598 -0.0478 43  GLU   B CG  
526  C  CD  . GLU   B 34  ? 0.6159 0.5495 0.6535 0.0382  -0.0613 -0.0412 43  GLU   B CD  
527  O  OE1 . GLU   B 34  ? 0.6368 0.5784 0.6859 0.0245  -0.0557 -0.0346 43  GLU   B OE1 
528  O  OE2 . GLU   B 34  ? 0.6851 0.5987 0.7070 0.0454  -0.0679 -0.0423 43  GLU   B OE2 
529  N  N   . GLY   B 35  ? 0.4137 0.3933 0.4333 0.0712  -0.0297 -0.0498 44  GLY   B N   
530  C  CA  . GLY   B 35  ? 0.4054 0.3942 0.4213 0.0724  -0.0202 -0.0482 44  GLY   B CA  
531  C  C   . GLY   B 35  ? 0.3953 0.3723 0.3964 0.0691  -0.0123 -0.0416 44  GLY   B C   
532  O  O   . GLY   B 35  ? 0.4013 0.3846 0.3988 0.0696  -0.0051 -0.0405 44  GLY   B O   
533  N  N   . VAL   B 36  ? 0.3701 0.3307 0.3623 0.0666  -0.0142 -0.0377 45  VAL   B N   
534  C  CA  . VAL   B 36  ? 0.3622 0.3137 0.3421 0.0630  -0.0076 -0.0317 45  VAL   B CA  
535  C  C   . VAL   B 36  ? 0.3647 0.2985 0.3275 0.0710  -0.0088 -0.0316 45  VAL   B C   
536  O  O   . VAL   B 36  ? 0.3566 0.2822 0.3165 0.0765  -0.0153 -0.0335 45  VAL   B O   
537  C  CB  . VAL   B 36  ? 0.3617 0.3123 0.3470 0.0522  -0.0079 -0.0259 45  VAL   B CB  
538  C  CG1 . VAL   B 36  ? 0.3599 0.3011 0.3321 0.0500  -0.0030 -0.0206 45  VAL   B CG1 
539  C  CG2 . VAL   B 36  ? 0.3524 0.3210 0.3540 0.0434  -0.0045 -0.0239 45  VAL   B CG2 
540  N  N   . PHE   B 37  ? 0.3611 0.2897 0.3131 0.0717  -0.0026 -0.0294 46  PHE   B N   
541  C  CA  . PHE   B 37  ? 0.3634 0.2775 0.3011 0.0771  -0.0020 -0.0277 46  PHE   B CA  
542  C  C   . PHE   B 37  ? 0.3573 0.2678 0.2911 0.0706  0.0003  -0.0220 46  PHE   B C   
543  O  O   . PHE   B 37  ? 0.3486 0.2643 0.2843 0.0635  0.0045  -0.0196 46  PHE   B O   
544  C  CB  . PHE   B 37  ? 0.3662 0.2753 0.2949 0.0813  0.0024  -0.0291 46  PHE   B CB  
545  C  CG  . PHE   B 37  ? 0.3778 0.2720 0.2932 0.0868  0.0030  -0.0265 46  PHE   B CG  
546  C  CD1 . PHE   B 37  ? 0.3964 0.2843 0.3070 0.0963  -0.0014 -0.0279 46  PHE   B CD1 
547  C  CD2 . PHE   B 37  ? 0.3887 0.2765 0.2971 0.0822  0.0079  -0.0222 46  PHE   B CD2 
548  C  CE1 . PHE   B 37  ? 0.4149 0.2905 0.3127 0.1017  0.0005  -0.0241 46  PHE   B CE1 
549  C  CE2 . PHE   B 37  ? 0.4105 0.2870 0.3087 0.0858  0.0095  -0.0185 46  PHE   B CE2 
550  C  CZ  . PHE   B 37  ? 0.4184 0.2890 0.3109 0.0957  0.0065  -0.0188 46  PHE   B CZ  
551  N  N   . HIS   B 38  ? 0.3457 0.2481 0.2733 0.0745  -0.0029 -0.0201 47  HIS   B N   
552  C  CA  . HIS   B 38  ? 0.3566 0.2570 0.2804 0.0706  -0.0021 -0.0153 47  HIS   B CA  
553  C  C   . HIS   B 38  ? 0.3698 0.2639 0.2827 0.0749  0.0011  -0.0122 47  HIS   B C   
554  O  O   . HIS   B 38  ? 0.3850 0.2729 0.2916 0.0836  -0.0008 -0.0127 47  HIS   B O   
555  C  CB  . HIS   B 38  ? 0.3561 0.2528 0.2808 0.0732  -0.0095 -0.0157 47  HIS   B CB  
556  C  CG  . HIS   B 38  ? 0.3733 0.2750 0.3104 0.0681  -0.0138 -0.0183 47  HIS   B CG  
557  N  ND1 . HIS   B 38  ? 0.3713 0.2767 0.3160 0.0717  -0.0177 -0.0237 47  HIS   B ND1 
558  C  CD2 . HIS   B 38  ? 0.3692 0.2730 0.3124 0.0598  -0.0147 -0.0157 47  HIS   B CD2 
559  C  CE1 . HIS   B 38  ? 0.3639 0.2754 0.3213 0.0642  -0.0207 -0.0242 47  HIS   B CE1 
560  N  NE2 . HIS   B 38  ? 0.3708 0.2802 0.3271 0.0567  -0.0188 -0.0189 47  HIS   B NE2 
561  N  N   . THR   B 39  ? 0.3618 0.2585 0.2728 0.0689  0.0057  -0.0085 48  THR   B N   
562  C  CA  . THR   B 39  ? 0.3657 0.2595 0.2694 0.0708  0.0091  -0.0047 48  THR   B CA  
563  C  C   . THR   B 39  ? 0.3756 0.2758 0.2796 0.0651  0.0110  -0.0012 48  THR   B C   
564  O  O   . THR   B 39  ? 0.3725 0.2767 0.2799 0.0612  0.0092  -0.0018 48  THR   B O   
565  C  CB  . THR   B 39  ? 0.3722 0.2604 0.2730 0.0707  0.0132  -0.0052 48  THR   B CB  
566  O  OG1 . THR   B 39  ? 0.3772 0.2620 0.2719 0.0721  0.0167  -0.0001 48  THR   B OG1 
567  C  CG2 . THR   B 39  ? 0.3794 0.2705 0.2840 0.0627  0.0158  -0.0072 48  THR   B CG2 
568  N  N   . MET   B 40  ? 0.3708 0.2727 0.2714 0.0648  0.0144  0.0026  49  MET   B N   
569  C  CA  . MET   B 40  ? 0.3599 0.2705 0.2618 0.0600  0.0158  0.0051  49  MET   B CA  
570  C  C   . MET   B 40  ? 0.3606 0.2735 0.2664 0.0513  0.0188  0.0036  49  MET   B C   
571  O  O   . MET   B 40  ? 0.3645 0.2713 0.2702 0.0493  0.0210  0.0026  49  MET   B O   
572  C  CB  . MET   B 40  ? 0.3758 0.2912 0.2738 0.0644  0.0176  0.0100  49  MET   B CB  
573  C  CG  . MET   B 40  ? 0.3937 0.3049 0.2849 0.0759  0.0140  0.0108  49  MET   B CG  
574  S  SD  . MET   B 40  ? 0.4537 0.3751 0.3392 0.0832  0.0149  0.0161  49  MET   B SD  
575  C  CE  . MET   B 40  ? 0.4095 0.3351 0.2946 0.0821  0.0097  0.0138  49  MET   B CE  
576  N  N   . TRP   B 41  ? 0.3580 0.2782 0.2657 0.0469  0.0182  0.0029  50  TRP   B N   
577  C  CA  A TRP   B 41  ? 0.3662 0.2887 0.2766 0.0400  0.0197  0.0003  50  TRP   B CA  
578  C  CA  B TRP   B 41  ? 0.3559 0.2785 0.2662 0.0400  0.0197  0.0004  50  TRP   B CA  
579  C  C   . TRP   B 41  ? 0.3661 0.2884 0.2782 0.0357  0.0221  0.0018  50  TRP   B C   
580  O  O   . TRP   B 41  ? 0.3830 0.2988 0.2953 0.0318  0.0226  -0.0010 50  TRP   B O   
581  C  CB  A TRP   B 41  ? 0.3723 0.3030 0.2825 0.0379  0.0184  -0.0003 50  TRP   B CB  
582  C  CB  B TRP   B 41  ? 0.3462 0.2775 0.2564 0.0380  0.0184  0.0000  50  TRP   B CB  
583  C  CG  A TRP   B 41  ? 0.3923 0.3245 0.3034 0.0330  0.0189  -0.0041 50  TRP   B CG  
584  C  CG  B TRP   B 41  ? 0.3441 0.2776 0.2555 0.0326  0.0189  -0.0036 50  TRP   B CG  
585  C  CD1 A TRP   B 41  ? 0.4081 0.3385 0.3180 0.0330  0.0192  -0.0070 50  TRP   B CD1 
586  C  CD1 B TRP   B 41  ? 0.3474 0.2850 0.2613 0.0278  0.0188  -0.0047 50  TRP   B CD1 
587  C  CD2 A TRP   B 41  ? 0.3997 0.3358 0.3128 0.0280  0.0187  -0.0059 50  TRP   B CD2 
588  C  CD2 B TRP   B 41  ? 0.3441 0.2754 0.2541 0.0322  0.0190  -0.0070 50  TRP   B CD2 
589  N  NE1 A TRP   B 41  ? 0.4136 0.3456 0.3226 0.0299  0.0189  -0.0108 50  TRP   B NE1 
590  N  NE1 B TRP   B 41  ? 0.3473 0.2836 0.2603 0.0250  0.0179  -0.0095 50  TRP   B NE1 
591  C  CE2 A TRP   B 41  ? 0.4144 0.3490 0.3257 0.0263  0.0179  -0.0106 50  TRP   B CE2 
592  C  CE2 B TRP   B 41  ? 0.3528 0.2857 0.2626 0.0284  0.0185  -0.0108 50  TRP   B CE2 
593  C  CE3 A TRP   B 41  ? 0.4105 0.3527 0.3277 0.0247  0.0190  -0.0038 50  TRP   B CE3 
594  C  CE3 B TRP   B 41  ? 0.3466 0.2761 0.2563 0.0346  0.0196  -0.0072 50  TRP   B CE3 
595  C  CZ2 A TRP   B 41  ? 0.4328 0.3691 0.3452 0.0217  0.0161  -0.0144 50  TRP   B CZ2 
596  C  CZ2 B TRP   B 41  ? 0.3689 0.3010 0.2756 0.0290  0.0185  -0.0148 50  TRP   B CZ2 
597  C  CZ3 A TRP   B 41  ? 0.4249 0.3706 0.3457 0.0184  0.0175  -0.0070 50  TRP   B CZ3 
598  C  CZ3 B TRP   B 41  ? 0.3603 0.2915 0.2688 0.0341  0.0208  -0.0102 50  TRP   B CZ3 
599  C  CH2 A TRP   B 41  ? 0.4311 0.3727 0.3490 0.0171  0.0154  -0.0128 50  TRP   B CH2 
600  C  CH2 B TRP   B 41  ? 0.3662 0.2981 0.2720 0.0323  0.0203  -0.0141 50  TRP   B CH2 
601  N  N   . HIS   B 42  ? 0.3719 0.3010 0.2849 0.0365  0.0234  0.0063  51  HIS   B N   
602  C  CA  . HIS   B 42  ? 0.3811 0.3119 0.2981 0.0304  0.0262  0.0090  51  HIS   B CA  
603  C  C   . HIS   B 42  ? 0.3977 0.3138 0.3117 0.0305  0.0287  0.0103  51  HIS   B C   
604  O  O   . HIS   B 42  ? 0.4144 0.3266 0.3311 0.0234  0.0305  0.0117  51  HIS   B O   
605  C  CB  . HIS   B 42  ? 0.3796 0.3250 0.2997 0.0315  0.0281  0.0144  51  HIS   B CB  
606  C  CG  . HIS   B 42  ? 0.4020 0.3454 0.3171 0.0400  0.0305  0.0197  51  HIS   B CG  
607  N  ND1 . HIS   B 42  ? 0.4214 0.3677 0.3306 0.0500  0.0279  0.0200  51  HIS   B ND1 
608  C  CD2 . HIS   B 42  ? 0.4217 0.3589 0.3352 0.0406  0.0348  0.0246  51  HIS   B CD2 
609  C  CE1 . HIS   B 42  ? 0.4305 0.3744 0.3350 0.0572  0.0304  0.0246  51  HIS   B CE1 
610  N  NE2 . HIS   B 42  ? 0.4298 0.3686 0.3364 0.0521  0.0352  0.0280  51  HIS   B NE2 
611  N  N   . VAL   B 43  ? 0.3885 0.2953 0.2966 0.0383  0.0280  0.0094  52  VAL   B N   
612  C  CA  . VAL   B 43  ? 0.3945 0.2864 0.2973 0.0407  0.0297  0.0100  52  VAL   B CA  
613  C  C   . VAL   B 43  ? 0.4174 0.2992 0.3193 0.0363  0.0282  0.0042  52  VAL   B C   
614  O  O   . VAL   B 43  ? 0.4333 0.3029 0.3323 0.0326  0.0296  0.0051  52  VAL   B O   
615  C  CB  . VAL   B 43  ? 0.4041 0.2910 0.3011 0.0518  0.0283  0.0096  52  VAL   B CB  
616  C  CG1 . VAL   B 43  ? 0.4198 0.2907 0.3098 0.0560  0.0290  0.0083  52  VAL   B CG1 
617  C  CG2 . VAL   B 43  ? 0.4041 0.2975 0.2986 0.0583  0.0295  0.0152  52  VAL   B CG2 
618  N  N   . THR   B 44  ? 0.3864 0.2723 0.2897 0.0373  0.0253  -0.0013 53  THR   B N   
619  C  CA  . THR   B 44  ? 0.3960 0.2739 0.2966 0.0361  0.0238  -0.0071 53  THR   B CA  
620  C  C   . THR   B 44  ? 0.4016 0.2850 0.3051 0.0294  0.0221  -0.0106 53  THR   B C   
621  O  O   . THR   B 44  ? 0.4040 0.2795 0.3037 0.0290  0.0204  -0.0157 53  THR   B O   
622  C  CB  . THR   B 44  ? 0.4026 0.2819 0.3021 0.0432  0.0223  -0.0111 53  THR   B CB  
623  O  OG1 . THR   B 44  ? 0.3827 0.2753 0.2874 0.0423  0.0215  -0.0110 53  THR   B OG1 
624  C  CG2 . THR   B 44  ? 0.3996 0.2732 0.2959 0.0513  0.0223  -0.0098 53  THR   B CG2 
625  N  N   . LYS   B 45  ? 0.4044 0.3013 0.3130 0.0263  0.0219  -0.0087 54  LYS   B N   
626  C  CA  . LYS   B 45  ? 0.4193 0.3234 0.3297 0.0220  0.0197  -0.0125 54  LYS   B CA  
627  C  C   . LYS   B 45  ? 0.4456 0.3498 0.3521 0.0264  0.0188  -0.0174 54  LYS   B C   
628  O  O   . LYS   B 45  ? 0.4593 0.3649 0.3638 0.0250  0.0168  -0.0219 54  LYS   B O   
629  C  CB  . LYS   B 45  ? 0.4479 0.3463 0.3599 0.0143  0.0179  -0.0146 54  LYS   B CB  
630  C  CG  . LYS   B 45  ? 0.5240 0.4237 0.4417 0.0085  0.0200  -0.0085 54  LYS   B CG  
631  C  CD  . LYS   B 45  ? 0.6040 0.5218 0.5275 0.0089  0.0214  -0.0041 54  LYS   B CD  
632  C  CE  . LYS   B 45  ? 0.6758 0.5997 0.6066 0.0027  0.0240  0.0019  54  LYS   B CE  
633  N  NZ  . LYS   B 45  ? 0.7114 0.6210 0.6389 0.0026  0.0277  0.0068  54  LYS   B NZ  
634  N  N   . GLY   B 46  ? 0.4511 0.3553 0.3570 0.0320  0.0201  -0.0165 55  GLY   B N   
635  C  CA  . GLY   B 46  ? 0.4573 0.3650 0.3617 0.0359  0.0204  -0.0196 55  GLY   B CA  
636  C  C   . GLY   B 46  ? 0.4680 0.3671 0.3674 0.0394  0.0198  -0.0247 55  GLY   B C   
637  O  O   . GLY   B 46  ? 0.4783 0.3828 0.3761 0.0431  0.0204  -0.0277 55  GLY   B O   
638  N  N   . ALA   B 47  ? 0.4663 0.3517 0.3620 0.0391  0.0189  -0.0255 56  ALA   B N   
639  C  CA  . ALA   B 47  ? 0.4792 0.3530 0.3672 0.0439  0.0174  -0.0307 56  ALA   B CA  
640  C  C   . ALA   B 47  ? 0.4717 0.3479 0.3596 0.0522  0.0186  -0.0316 56  ALA   B C   
641  O  O   . ALA   B 47  ? 0.4545 0.3354 0.3477 0.0531  0.0197  -0.0278 56  ALA   B O   
642  C  CB  . ALA   B 47  ? 0.5062 0.3619 0.3894 0.0407  0.0161  -0.0301 56  ALA   B CB  
643  N  N   . ALA   B 48  ? 0.4633 0.3358 0.3448 0.0590  0.0175  -0.0371 57  ALA   B N   
644  C  CA  . ALA   B 48  ? 0.4608 0.3367 0.3426 0.0676  0.0180  -0.0388 57  ALA   B CA  
645  C  C   . ALA   B 48  ? 0.4746 0.3355 0.3519 0.0704  0.0171  -0.0372 57  ALA   B C   
646  O  O   . ALA   B 48  ? 0.4940 0.3388 0.3652 0.0666  0.0165  -0.0354 57  ALA   B O   
647  C  CB  . ALA   B 48  ? 0.4570 0.3325 0.3310 0.0760  0.0169  -0.0456 57  ALA   B CB  
648  N  N   . LEU   B 49  ? 0.4632 0.3295 0.3434 0.0772  0.0170  -0.0376 58  LEU   B N   
649  C  CA  . LEU   B 49  ? 0.4839 0.3366 0.3579 0.0826  0.0160  -0.0363 58  LEU   B CA  
650  C  C   . LEU   B 49  ? 0.5182 0.3687 0.3860 0.0946  0.0140  -0.0422 58  LEU   B C   
651  O  O   . LEU   B 49  ? 0.5155 0.3820 0.3890 0.0986  0.0138  -0.0464 58  LEU   B O   
652  C  CB  . LEU   B 49  ? 0.4689 0.3301 0.3514 0.0818  0.0162  -0.0320 58  LEU   B CB  
653  C  CG  . LEU   B 49  ? 0.4876 0.3535 0.3760 0.0724  0.0178  -0.0262 58  LEU   B CG  
654  C  CD1 . LEU   B 49  ? 0.4865 0.3599 0.3812 0.0742  0.0165  -0.0236 58  LEU   B CD1 
655  C  CD2 . LEU   B 49  ? 0.5140 0.3654 0.3954 0.0678  0.0194  -0.0222 58  LEU   B CD2 
656  N  N   . ARG   B 50  ? 0.5429 0.3747 0.3990 0.1011  0.0129  -0.0422 59  ARG   B N   
657  C  CA  . ARG   B 50  ? 0.5722 0.3998 0.4200 0.1144  0.0104  -0.0478 59  ARG   B CA  
658  C  C   . ARG   B 50  ? 0.5835 0.4146 0.4341 0.1210  0.0091  -0.0466 59  ARG   B C   
659  O  O   . ARG   B 50  ? 0.5705 0.3949 0.4207 0.1173  0.0104  -0.0406 59  ARG   B O   
660  C  CB  . ARG   B 50  ? 0.6241 0.4233 0.4528 0.1183  0.0093  -0.0488 59  ARG   B CB  
661  C  CG  . ARG   B 50  ? 0.7254 0.5143 0.5409 0.1339  0.0064  -0.0538 59  ARG   B CG  
662  C  CD  . ARG   B 50  ? 0.8081 0.5692 0.6035 0.1386  0.0042  -0.0567 59  ARG   B CD  
663  N  NE  . ARG   B 50  ? 0.8643 0.6026 0.6537 0.1269  0.0058  -0.0501 59  ARG   B NE  
664  C  CZ  . ARG   B 50  ? 0.9038 0.6220 0.6843 0.1265  0.0075  -0.0435 59  ARG   B CZ  
665  N  NH1 . ARG   B 50  ? 0.8890 0.6056 0.6636 0.1383  0.0075  -0.0430 59  ARG   B NH1 
666  N  NH2 . ARG   B 50  ? 0.9194 0.6203 0.6974 0.1143  0.0094  -0.0370 59  ARG   B NH2 
667  N  N   . SER   B 51  ? 0.5957 0.4388 0.4493 0.1315  0.0063  -0.0526 60  SER   B N   
668  C  CA  . SER   B 51  ? 0.6180 0.4639 0.4731 0.1399  0.0033  -0.0535 60  SER   B CA  
669  C  C   . SER   B 51  ? 0.6419 0.4841 0.4865 0.1554  0.0001  -0.0608 60  SER   B C   
670  O  O   . SER   B 51  ? 0.6399 0.5027 0.4940 0.1594  -0.0014 -0.0668 60  SER   B O   
671  C  CB  . SER   B 51  ? 0.6204 0.4919 0.4960 0.1350  0.0018  -0.0542 60  SER   B CB  
672  O  OG  . SER   B 51  ? 0.6544 0.5286 0.5316 0.1441  -0.0029 -0.0569 60  SER   B OG  
673  N  N   . GLY   B 52  ? 0.6656 0.4817 0.4900 0.1638  -0.0004 -0.0599 61  GLY   B N   
674  C  CA  . GLY   B 52  ? 0.6883 0.4960 0.4981 0.1800  -0.0037 -0.0669 61  GLY   B CA  
675  C  C   . GLY   B 52  ? 0.7081 0.5152 0.5136 0.1795  -0.0031 -0.0709 61  GLY   B C   
676  O  O   . GLY   B 52  ? 0.7159 0.5065 0.5147 0.1703  -0.0008 -0.0670 61  GLY   B O   
677  N  N   . GLU   B 53  ? 0.7100 0.5376 0.5208 0.1890  -0.0055 -0.0787 62  GLU   B N   
678  C  CA  . GLU   B 53  ? 0.7308 0.5627 0.5380 0.1907  -0.0050 -0.0832 62  GLU   B CA  
679  C  C   . GLU   B 53  ? 0.7130 0.5738 0.5420 0.1781  -0.0015 -0.0815 62  GLU   B C   
680  O  O   . GLU   B 53  ? 0.7248 0.5906 0.5510 0.1789  -0.0004 -0.0842 62  GLU   B O   
681  C  CB  . GLU   B 53  ? 0.7861 0.6269 0.5860 0.2100  -0.0089 -0.0924 62  GLU   B CB  
682  C  CG  . GLU   B 53  ? 0.9259 0.7320 0.6962 0.2236  -0.0123 -0.0956 62  GLU   B CG  
683  C  CD  . GLU   B 53  ? 1.0851 0.9022 0.8471 0.2435  -0.0162 -0.1057 62  GLU   B CD  
684  O  OE1 . GLU   B 53  ? 1.1126 0.9614 0.8906 0.2501  -0.0173 -0.1099 62  GLU   B OE1 
685  O  OE2 . GLU   B 53  ? 1.1513 0.9459 0.8909 0.2529  -0.0186 -0.1097 62  GLU   B OE2 
686  N  N   . GLY   B 54  ? 0.6804 0.5584 0.5287 0.1680  0.0000  -0.0770 63  GLY   B N   
687  C  CA  . GLY   B 54  ? 0.6561 0.5594 0.5243 0.1560  0.0035  -0.0742 63  GLY   B CA  
688  C  C   . GLY   B 54  ? 0.6474 0.5397 0.5153 0.1414  0.0067  -0.0674 63  GLY   B C   
689  O  O   . GLY   B 54  ? 0.6589 0.5267 0.5157 0.1381  0.0065  -0.0638 63  GLY   B O   
690  N  N   . ARG   B 55  ? 0.6119 0.5235 0.4923 0.1330  0.0101  -0.0655 64  ARG   B N   
691  C  CA  . ARG   B 55  ? 0.5979 0.5036 0.4792 0.1202  0.0128  -0.0600 64  ARG   B CA  
692  C  C   . ARG   B 55  ? 0.5636 0.4879 0.4638 0.1096  0.0148  -0.0546 64  ARG   B C   
693  O  O   . ARG   B 55  ? 0.5684 0.5154 0.4826 0.1105  0.0154  -0.0555 64  ARG   B O   
694  C  CB  . ARG   B 55  ? 0.6155 0.5249 0.4908 0.1217  0.0145  -0.0627 64  ARG   B CB  
695  C  CG  . ARG   B 55  ? 0.6516 0.5529 0.5248 0.1107  0.0160  -0.0588 64  ARG   B CG  
696  C  CD  . ARG   B 55  ? 0.6930 0.6003 0.5596 0.1148  0.0169  -0.0627 64  ARG   B CD  
697  N  NE  . ARG   B 55  ? 0.7331 0.6373 0.5995 0.1050  0.0179  -0.0597 64  ARG   B NE  
698  C  CZ  . ARG   B 55  ? 0.7763 0.6630 0.6295 0.1051  0.0149  -0.0630 64  ARG   B CZ  
699  N  NH1 . ARG   B 55  ? 0.7968 0.6649 0.6347 0.1142  0.0107  -0.0692 64  ARG   B NH1 
700  N  NH2 . ARG   B 55  ? 0.7509 0.6379 0.6057 0.0965  0.0153  -0.0608 64  ARG   B NH2 
701  N  N   . LEU   B 56  ? 0.5123 0.4266 0.4126 0.0998  0.0155  -0.0490 65  LEU   B N   
702  C  CA  . LEU   B 56  ? 0.4690 0.3953 0.3829 0.0901  0.0167  -0.0438 65  LEU   B CA  
703  C  C   . LEU   B 56  ? 0.4464 0.3717 0.3578 0.0821  0.0197  -0.0406 65  LEU   B C   
704  O  O   . LEU   B 56  ? 0.4541 0.3632 0.3558 0.0796  0.0193  -0.0397 65  LEU   B O   
705  C  CB  . LEU   B 56  ? 0.4623 0.3774 0.3760 0.0878  0.0142  -0.0403 65  LEU   B CB  
706  C  CG  . LEU   B 56  ? 0.5009 0.4118 0.4134 0.0968  0.0102  -0.0431 65  LEU   B CG  
707  C  CD1 . LEU   B 56  ? 0.4933 0.4012 0.4098 0.0937  0.0078  -0.0392 65  LEU   B CD1 
708  C  CD2 . LEU   B 56  ? 0.5199 0.4496 0.4432 0.1025  0.0082  -0.0482 65  LEU   B CD2 
709  N  N   . ASP   B 57  ? 0.4235 0.3663 0.3438 0.0779  0.0226  -0.0387 66  ASP   B N   
710  C  CA  . ASP   B 57  ? 0.4191 0.3625 0.3362 0.0720  0.0252  -0.0360 66  ASP   B CA  
711  C  C   . ASP   B 57  ? 0.4038 0.3500 0.3283 0.0630  0.0257  -0.0298 66  ASP   B C   
712  O  O   . ASP   B 57  ? 0.4003 0.3551 0.3356 0.0608  0.0252  -0.0274 66  ASP   B O   
713  C  CB  . ASP   B 57  ? 0.4505 0.4112 0.3693 0.0752  0.0290  -0.0372 66  ASP   B CB  
714  C  CG  . ASP   B 57  ? 0.5473 0.5050 0.4561 0.0863  0.0279  -0.0442 66  ASP   B CG  
715  O  OD1 . ASP   B 57  ? 0.5592 0.4967 0.4553 0.0888  0.0246  -0.0476 66  ASP   B OD1 
716  O  OD2 . ASP   B 57  ? 0.5745 0.5500 0.4886 0.0925  0.0301  -0.0462 66  ASP   B OD2 
717  N  N   . PRO   B 58  ? 0.3935 0.3322 0.3122 0.0581  0.0259  -0.0275 67  PRO   B N   
718  C  CA  . PRO   B 58  ? 0.3842 0.3254 0.3078 0.0513  0.0261  -0.0219 67  PRO   B CA  
719  C  C   . PRO   B 58  ? 0.3735 0.3297 0.3045 0.0485  0.0293  -0.0185 67  PRO   B C   
720  O  O   . PRO   B 58  ? 0.3788 0.3448 0.3089 0.0511  0.0328  -0.0196 67  PRO   B O   
721  C  CB  . PRO   B 58  ? 0.4064 0.3403 0.3219 0.0482  0.0258  -0.0215 67  PRO   B CB  
722  C  CG  . PRO   B 58  ? 0.4305 0.3617 0.3384 0.0524  0.0261  -0.0268 67  PRO   B CG  
723  C  CD  . PRO   B 58  ? 0.4163 0.3449 0.3241 0.0588  0.0253  -0.0305 67  PRO   B CD  
724  N  N   . TYR   B 59  ? 0.3565 0.3137 0.2941 0.0437  0.0282  -0.0139 68  TYR   B N   
725  C  CA  . TYR   B 59  ? 0.3448 0.3136 0.2904 0.0394  0.0312  -0.0092 68  TYR   B CA  
726  C  C   . TYR   B 59  ? 0.3461 0.3096 0.2872 0.0344  0.0312  -0.0037 68  TYR   B C   
727  O  O   . TYR   B 59  ? 0.3554 0.3254 0.2952 0.0320  0.0354  0.0005  68  TYR   B O   
728  C  CB  . TYR   B 59  ? 0.3391 0.3128 0.2979 0.0379  0.0284  -0.0092 68  TYR   B CB  
729  C  CG  . TYR   B 59  ? 0.3366 0.3219 0.3062 0.0311  0.0313  -0.0035 68  TYR   B CG  
730  C  CD1 . TYR   B 59  ? 0.3580 0.3359 0.3270 0.0247  0.0300  0.0024  68  TYR   B CD1 
731  C  CD2 . TYR   B 59  ? 0.3376 0.3414 0.3178 0.0312  0.0354  -0.0035 68  TYR   B CD2 
732  C  CE1 . TYR   B 59  ? 0.3541 0.3399 0.3325 0.0173  0.0329  0.0088  68  TYR   B CE1 
733  C  CE2 . TYR   B 59  ? 0.3304 0.3458 0.3225 0.0234  0.0387  0.0031  68  TYR   B CE2 
734  C  CZ  . TYR   B 59  ? 0.3383 0.3433 0.3294 0.0158  0.0375  0.0095  68  TYR   B CZ  
735  O  OH  . TYR   B 59  ? 0.3597 0.3737 0.3620 0.0071  0.0410  0.0169  68  TYR   B OH  
736  N  N   . TRP   B 60  ? 0.3478 0.2998 0.2854 0.0341  0.0267  -0.0036 69  TRP   B N   
737  C  CA  . TRP   B 60  ? 0.3589 0.3052 0.2906 0.0314  0.0258  0.0008  69  TRP   B CA  
738  C  C   . TRP   B 60  ? 0.3605 0.2986 0.2854 0.0341  0.0226  -0.0014 69  TRP   B C   
739  O  O   . TRP   B 60  ? 0.3425 0.2760 0.2688 0.0369  0.0201  -0.0041 69  TRP   B O   
740  C  CB  . TRP   B 60  ? 0.3615 0.3039 0.2989 0.0278  0.0226  0.0047  69  TRP   B CB  
741  C  CG  . TRP   B 60  ? 0.3763 0.3095 0.3052 0.0275  0.0199  0.0082  69  TRP   B CG  
742  C  CD1 . TRP   B 60  ? 0.3812 0.3139 0.3032 0.0256  0.0224  0.0129  69  TRP   B CD1 
743  C  CD2 . TRP   B 60  ? 0.3608 0.2846 0.2846 0.0312  0.0145  0.0070  69  TRP   B CD2 
744  N  NE1 . TRP   B 60  ? 0.3876 0.3106 0.3009 0.0279  0.0181  0.0142  69  TRP   B NE1 
745  C  CE2 . TRP   B 60  ? 0.3778 0.2965 0.2922 0.0316  0.0135  0.0105  69  TRP   B CE2 
746  C  CE3 . TRP   B 60  ? 0.3624 0.2821 0.2873 0.0355  0.0107  0.0035  69  TRP   B CE3 
747  C  CZ2 . TRP   B 60  ? 0.3856 0.2969 0.2928 0.0363  0.0086  0.0104  69  TRP   B CZ2 
748  C  CZ3 . TRP   B 60  ? 0.3679 0.2805 0.2854 0.0400  0.0066  0.0039  69  TRP   B CZ3 
749  C  CH2 . TRP   B 60  ? 0.3856 0.2946 0.2949 0.0404  0.0054  0.0072  69  TRP   B CH2 
750  N  N   . GLY   B 61  ? 0.3571 0.2940 0.2745 0.0337  0.0227  0.0003  70  GLY   B N   
751  C  CA  . GLY   B 61  ? 0.3595 0.2921 0.2725 0.0356  0.0201  -0.0007 70  GLY   B CA  
752  C  C   . GLY   B 61  ? 0.3623 0.2959 0.2682 0.0357  0.0194  0.0016  70  GLY   B C   
753  O  O   . GLY   B 61  ? 0.3670 0.3039 0.2694 0.0348  0.0215  0.0031  70  GLY   B O   
754  N  N   . ASP   B 62  ? 0.3704 0.3026 0.2738 0.0378  0.0167  0.0019  71  ASP   B N   
755  C  CA  . ASP   B 62  ? 0.3710 0.3060 0.2675 0.0395  0.0153  0.0035  71  ASP   B CA  
756  C  C   . ASP   B 62  ? 0.3693 0.3085 0.2663 0.0412  0.0139  0.0024  71  ASP   B C   
757  O  O   . ASP   B 62  ? 0.3820 0.3183 0.2799 0.0440  0.0124  0.0037  71  ASP   B O   
758  C  CB  . ASP   B 62  ? 0.3994 0.3273 0.2909 0.0417  0.0126  0.0075  71  ASP   B CB  
759  C  CG  . ASP   B 62  ? 0.4843 0.4139 0.3662 0.0451  0.0111  0.0090  71  ASP   B CG  
760  O  OD1 . ASP   B 62  ? 0.4717 0.4047 0.3506 0.0493  0.0085  0.0085  71  ASP   B OD1 
761  O  OD2 . ASP   B 62  ? 0.5494 0.4784 0.4263 0.0442  0.0129  0.0108  71  ASP   B OD2 
762  N  N   . VAL   B 63  ? 0.3655 0.3127 0.2623 0.0395  0.0143  0.0001  72  VAL   B N   
763  C  CA  . VAL   B 63  ? 0.3657 0.3204 0.2659 0.0392  0.0135  -0.0004 72  VAL   B CA  
764  C  C   . VAL   B 63  ? 0.3756 0.3342 0.2715 0.0452  0.0113  0.0027  72  VAL   B C   
765  O  O   . VAL   B 63  ? 0.3719 0.3344 0.2709 0.0467  0.0117  0.0044  72  VAL   B O   
766  C  CB  . VAL   B 63  ? 0.3645 0.3278 0.2668 0.0354  0.0130  -0.0043 72  VAL   B CB  
767  C  CG1 . VAL   B 63  ? 0.3692 0.3452 0.2757 0.0350  0.0116  -0.0041 72  VAL   B CG1 
768  C  CG2 . VAL   B 63  ? 0.3667 0.3246 0.2730 0.0304  0.0143  -0.0079 72  VAL   B CG2 
769  N  N   . LYS   B 64  ? 0.3798 0.3365 0.2674 0.0493  0.0091  0.0038  73  LYS   B N   
770  C  CA  . LYS   B 64  ? 0.3956 0.3550 0.2767 0.0569  0.0060  0.0060  73  LYS   B CA  
771  C  C   . LYS   B 64  ? 0.3925 0.3425 0.2717 0.0614  0.0043  0.0083  73  LYS   B C   
772  O  O   . LYS   B 64  ? 0.4090 0.3648 0.2868 0.0672  0.0033  0.0095  73  LYS   B O   
773  C  CB  . LYS   B 64  ? 0.4259 0.3823 0.2957 0.0614  0.0034  0.0067  73  LYS   B CB  
774  C  CG  . LYS   B 64  ? 0.4576 0.4173 0.3189 0.0711  -0.0006 0.0080  73  LYS   B CG  
775  C  CD  . LYS   B 64  ? 0.4827 0.4386 0.3307 0.0766  -0.0034 0.0085  73  LYS   B CD  
776  C  CE  . LYS   B 64  ? 0.5299 0.4857 0.3668 0.0880  -0.0082 0.0095  73  LYS   B CE  
777  N  NZ  . LYS   B 64  ? 0.5619 0.5120 0.3832 0.0948  -0.0114 0.0100  73  LYS   B NZ  
778  N  N   . GLN   B 65  ? 0.3894 0.3265 0.2691 0.0591  0.0041  0.0087  74  GLN   B N   
779  C  CA  . GLN   B 65  ? 0.3886 0.3164 0.2677 0.0632  0.0014  0.0095  74  GLN   B CA  
780  C  C   . GLN   B 65  ? 0.3763 0.3080 0.2623 0.0625  0.0042  0.0089  74  GLN   B C   
781  O  O   . GLN   B 65  ? 0.3757 0.3024 0.2596 0.0685  0.0021  0.0094  74  GLN   B O   
782  C  CB  . GLN   B 65  ? 0.4122 0.3276 0.2929 0.0595  0.0000  0.0095  74  GLN   B CB  
783  C  CG  . GLN   B 65  ? 0.4687 0.3756 0.3411 0.0600  -0.0029 0.0118  74  GLN   B CG  
784  C  CD  . GLN   B 65  ? 0.5597 0.4564 0.4369 0.0543  -0.0036 0.0129  74  GLN   B CD  
785  O  OE1 . GLN   B 65  ? 0.5852 0.4756 0.4670 0.0548  -0.0069 0.0116  74  GLN   B OE1 
786  N  NE2 . GLN   B 65  ? 0.5897 0.4858 0.4661 0.0490  -0.0006 0.0155  74  GLN   B NE2 
787  N  N   . ASP   B 66  ? 0.3610 0.2997 0.2542 0.0558  0.0086  0.0076  75  ASP   B N   
788  C  CA  . ASP   B 66  ? 0.3676 0.3071 0.2665 0.0535  0.0119  0.0074  75  ASP   B CA  
789  C  C   . ASP   B 66  ? 0.3656 0.2937 0.2655 0.0547  0.0110  0.0062  75  ASP   B C   
790  O  O   . ASP   B 66  ? 0.3663 0.2913 0.2654 0.0590  0.0113  0.0072  75  ASP   B O   
791  C  CB  . ASP   B 66  ? 0.3525 0.3002 0.2509 0.0579  0.0132  0.0106  75  ASP   B CB  
792  C  CG  . ASP   B 66  ? 0.3864 0.3344 0.2903 0.0537  0.0176  0.0118  75  ASP   B CG  
793  O  OD1 . ASP   B 66  ? 0.3921 0.3368 0.3003 0.0464  0.0191  0.0092  75  ASP   B OD1 
794  O  OD2 . ASP   B 66  ? 0.4122 0.3633 0.3149 0.0583  0.0196  0.0155  75  ASP   B OD2 
795  N  N   . LEU   B 67  ? 0.3647 0.2883 0.2664 0.0515  0.0102  0.0044  76  LEU   B N   
796  C  CA  . LEU   B 67  ? 0.3581 0.2745 0.2631 0.0523  0.0090  0.0026  76  LEU   B CA  
797  C  C   . LEU   B 67  ? 0.3501 0.2683 0.2603 0.0466  0.0119  0.0002  76  LEU   B C   
798  O  O   . LEU   B 67  ? 0.3387 0.2616 0.2484 0.0427  0.0139  0.0003  76  LEU   B O   
799  C  CB  . LEU   B 67  ? 0.3606 0.2705 0.2638 0.0550  0.0037  0.0031  76  LEU   B CB  
800  C  CG  . LEU   B 67  ? 0.3682 0.2736 0.2642 0.0634  -0.0010 0.0042  76  LEU   B CG  
801  C  CD1 . LEU   B 67  ? 0.3789 0.2748 0.2721 0.0648  -0.0074 0.0042  76  LEU   B CD1 
802  C  CD2 . LEU   B 67  ? 0.3711 0.2741 0.2668 0.0697  -0.0012 0.0030  76  LEU   B CD2 
803  N  N   . VAL   B 68  ? 0.3419 0.2570 0.2560 0.0479  0.0119  -0.0022 77  VAL   B N   
804  C  CA  . VAL   B 68  ? 0.3396 0.2578 0.2581 0.0448  0.0144  -0.0049 77  VAL   B CA  
805  C  C   . VAL   B 68  ? 0.3426 0.2594 0.2665 0.0476  0.0122  -0.0072 77  VAL   B C   
806  O  O   . VAL   B 68  ? 0.3470 0.2582 0.2692 0.0529  0.0093  -0.0080 77  VAL   B O   
807  C  CB  . VAL   B 68  ? 0.3533 0.2709 0.2692 0.0436  0.0175  -0.0070 77  VAL   B CB  
808  C  CG1 . VAL   B 68  ? 0.3729 0.2833 0.2860 0.0472  0.0173  -0.0070 77  VAL   B CG1 
809  C  CG2 . VAL   B 68  ? 0.3598 0.2805 0.2777 0.0427  0.0196  -0.0105 77  VAL   B CG2 
810  N  N   . SER   B 69  ? 0.3308 0.2540 0.2612 0.0447  0.0134  -0.0081 78  SER   B N   
811  C  CA  . SER   B 69  ? 0.3384 0.2645 0.2767 0.0469  0.0113  -0.0111 78  SER   B CA  
812  C  C   . SER   B 69  ? 0.3481 0.2816 0.2885 0.0477  0.0153  -0.0143 78  SER   B C   
813  O  O   . SER   B 69  ? 0.3391 0.2770 0.2768 0.0450  0.0193  -0.0134 78  SER   B O   
814  C  CB  . SER   B 69  ? 0.3443 0.2738 0.2911 0.0425  0.0085  -0.0090 78  SER   B CB  
815  O  OG  . SER   B 69  ? 0.3453 0.2835 0.2961 0.0364  0.0130  -0.0059 78  SER   B OG  
816  N  N   . TYR   B 70  ? 0.3270 0.2620 0.2710 0.0528  0.0135  -0.0184 79  TYR   B N   
817  C  CA  . TYR   B 70  ? 0.3382 0.2794 0.2824 0.0565  0.0162  -0.0225 79  TYR   B CA  
818  C  C   . TYR   B 70  ? 0.3446 0.2996 0.3018 0.0574  0.0147  -0.0247 79  TYR   B C   
819  O  O   . TYR   B 70  ? 0.3433 0.2968 0.3062 0.0590  0.0095  -0.0261 79  TYR   B O   
820  C  CB  . TYR   B 70  ? 0.3504 0.2794 0.2848 0.0640  0.0148  -0.0260 79  TYR   B CB  
821  C  CG  . TYR   B 70  ? 0.3653 0.2831 0.2892 0.0620  0.0169  -0.0241 79  TYR   B CG  
822  C  CD1 . TYR   B 70  ? 0.3669 0.2776 0.2876 0.0596  0.0159  -0.0201 79  TYR   B CD1 
823  C  CD2 . TYR   B 70  ? 0.3785 0.2934 0.2958 0.0627  0.0191  -0.0266 79  TYR   B CD2 
824  C  CE1 . TYR   B 70  ? 0.3753 0.2795 0.2895 0.0563  0.0179  -0.0181 79  TYR   B CE1 
825  C  CE2 . TYR   B 70  ? 0.3907 0.2959 0.3006 0.0592  0.0200  -0.0252 79  TYR   B CE2 
826  C  CZ  . TYR   B 70  ? 0.3924 0.2939 0.3021 0.0552  0.0196  -0.0207 79  TYR   B CZ  
827  O  OH  . TYR   B 70  ? 0.4123 0.3078 0.3176 0.0507  0.0204  -0.0193 79  TYR   B OH  
828  N  N   . CYS   B 71  ? 0.3485 0.3179 0.3104 0.0572  0.0190  -0.0255 80  CYS   B N   
829  C  CA  . CYS   B 71  ? 0.3581 0.3460 0.3346 0.0577  0.0190  -0.0274 80  CYS   B CA  
830  C  C   . CYS   B 71  ? 0.3652 0.3632 0.3561 0.0478  0.0192  -0.0221 80  CYS   B C   
831  O  O   . CYS   B 71  ? 0.3743 0.3909 0.3798 0.0460  0.0203  -0.0224 80  CYS   B O   
832  C  CB  . CYS   B 71  ? 0.3732 0.3600 0.3521 0.0658  0.0134  -0.0336 80  CYS   B CB  
833  S  SG  . CYS   B 71  ? 0.4570 0.4261 0.4165 0.0774  0.0127  -0.0386 80  CYS   B SG  
834  N  N   . GLY   B 72  ? 0.3546 0.3408 0.3417 0.0418  0.0178  -0.0174 81  GLY   B N   
835  C  CA  . GLY   B 72  ? 0.3427 0.3329 0.3407 0.0322  0.0171  -0.0119 81  GLY   B CA  
836  C  C   . GLY   B 72  ? 0.3402 0.3131 0.3285 0.0289  0.0146  -0.0079 81  GLY   B C   
837  O  O   . GLY   B 72  ? 0.3446 0.3056 0.3196 0.0337  0.0140  -0.0091 81  GLY   B O   
838  N  N   . PRO   B 73  ? 0.3327 0.3048 0.3275 0.0204  0.0138  -0.0023 82  PRO   B N   
839  C  CA  . PRO   B 73  ? 0.3445 0.2999 0.3287 0.0184  0.0109  0.0015  82  PRO   B CA  
840  C  C   . PRO   B 73  ? 0.3553 0.2960 0.3347 0.0237  0.0020  -0.0025 82  PRO   B C   
841  O  O   . PRO   B 73  ? 0.3555 0.2986 0.3427 0.0268  -0.0032 -0.0077 82  PRO   B O   
842  C  CB  . PRO   B 73  ? 0.3508 0.3081 0.3439 0.0082  0.0117  0.0083  82  PRO   B CB  
843  C  CG  . PRO   B 73  ? 0.3458 0.3175 0.3579 0.0046  0.0103  0.0061  82  PRO   B CG  
844  C  CD  . PRO   B 73  ? 0.3244 0.3104 0.3369 0.0123  0.0147  0.0007  82  PRO   B CD  
845  N  N   . TRP   B 74  ? 0.3614 0.2885 0.3273 0.0261  0.0000  -0.0005 83  TRP   B N   
846  C  CA  . TRP   B 74  ? 0.3730 0.2870 0.3318 0.0329  -0.0078 -0.0035 83  TRP   B CA  
847  C  C   . TRP   B 74  ? 0.3764 0.2853 0.3445 0.0305  -0.0165 -0.0055 83  TRP   B C   
848  O  O   . TRP   B 74  ? 0.3803 0.2867 0.3538 0.0222  -0.0176 -0.0013 83  TRP   B O   
849  C  CB  . TRP   B 74  ? 0.3767 0.2804 0.3210 0.0349  -0.0080 0.0001  83  TRP   B CB  
850  C  CG  . TRP   B 74  ? 0.3780 0.2711 0.3129 0.0440  -0.0144 -0.0024 83  TRP   B CG  
851  C  CD1 . TRP   B 74  ? 0.3855 0.2661 0.3167 0.0470  -0.0232 -0.0032 83  TRP   B CD1 
852  C  CD2 . TRP   B 74  ? 0.3733 0.2673 0.3003 0.0517  -0.0124 -0.0041 83  TRP   B CD2 
853  N  NE1 . TRP   B 74  ? 0.3939 0.2693 0.3147 0.0577  -0.0265 -0.0056 83  TRP   B NE1 
854  C  CE2 . TRP   B 74  ? 0.3852 0.2694 0.3042 0.0602  -0.0193 -0.0055 83  TRP   B CE2 
855  C  CE3 . TRP   B 74  ? 0.3611 0.2625 0.2870 0.0523  -0.0056 -0.0045 83  TRP   B CE3 
856  C  CZ2 . TRP   B 74  ? 0.3939 0.2779 0.3048 0.0691  -0.0183 -0.0063 83  TRP   B CZ2 
857  C  CZ3 . TRP   B 74  ? 0.3841 0.2830 0.3024 0.0593  -0.0051 -0.0050 83  TRP   B CZ3 
858  C  CH2 . TRP   B 74  ? 0.3889 0.2804 0.3002 0.0676  -0.0107 -0.0054 83  TRP   B CH2 
859  N  N   . LYS   B 75  ? 0.3714 0.2784 0.3414 0.0377  -0.0229 -0.0117 84  LYS   B N   
860  C  CA  . LYS   B 75  ? 0.3851 0.2885 0.3656 0.0364  -0.0330 -0.0157 84  LYS   B CA  
861  C  C   . LYS   B 75  ? 0.4251 0.3100 0.3938 0.0442  -0.0432 -0.0181 84  LYS   B C   
862  O  O   . LYS   B 75  ? 0.4424 0.3202 0.4177 0.0423  -0.0531 -0.0212 84  LYS   B O   
863  C  CB  . LYS   B 75  ? 0.3837 0.2986 0.3742 0.0412  -0.0348 -0.0225 84  LYS   B CB  
864  C  CG  . LYS   B 75  ? 0.4065 0.3413 0.4087 0.0362  -0.0260 -0.0216 84  LYS   B CG  
865  C  CD  . LYS   B 75  ? 0.4643 0.4095 0.4839 0.0228  -0.0247 -0.0174 84  LYS   B CD  
866  C  CE  . LYS   B 75  ? 0.5046 0.4727 0.5359 0.0202  -0.0163 -0.0171 84  LYS   B CE  
867  N  NZ  . LYS   B 75  ? 0.5277 0.5103 0.5798 0.0079  -0.0155 -0.0135 84  LYS   B NZ  
868  N  N   . LEU   B 76  ? 0.4255 0.3040 0.3776 0.0537  -0.0413 -0.0175 85  LEU   B N   
869  C  CA  . LEU   B 76  ? 0.4336 0.2974 0.3725 0.0645  -0.0501 -0.0200 85  LEU   B CA  
870  C  C   . LEU   B 76  ? 0.4639 0.3141 0.3948 0.0617  -0.0544 -0.0163 85  LEU   B C   
871  O  O   . LEU   B 76  ? 0.4645 0.3158 0.3881 0.0594  -0.0477 -0.0109 85  LEU   B O   
872  C  CB  . LEU   B 76  ? 0.4226 0.2880 0.3481 0.0757  -0.0451 -0.0196 85  LEU   B CB  
873  C  CG  . LEU   B 76  ? 0.4241 0.3000 0.3537 0.0786  -0.0391 -0.0220 85  LEU   B CG  
874  C  CD1 . LEU   B 76  ? 0.4373 0.3118 0.3532 0.0882  -0.0345 -0.0201 85  LEU   B CD1 
875  C  CD2 . LEU   B 76  ? 0.4241 0.3011 0.3621 0.0826  -0.0466 -0.0289 85  LEU   B CD2 
876  N  N   . ASP   B 77  ? 0.4897 0.3257 0.4208 0.0626  -0.0666 -0.0198 86  ASP   B N   
877  C  CA  . ASP   B 77  ? 0.5283 0.3476 0.4493 0.0608  -0.0716 -0.0163 86  ASP   B CA  
878  C  C   . ASP   B 77  ? 0.5354 0.3359 0.4410 0.0741  -0.0845 -0.0211 86  ASP   B C   
879  O  O   . ASP   B 77  ? 0.5461 0.3296 0.4416 0.0737  -0.0905 -0.0191 86  ASP   B O   
880  C  CB  . ASP   B 77  ? 0.5808 0.3962 0.5153 0.0449  -0.0731 -0.0128 86  ASP   B CB  
881  C  CG  . ASP   B 77  ? 0.6920 0.5074 0.6441 0.0390  -0.0821 -0.0183 86  ASP   B CG  
882  O  OD1 . ASP   B 77  ? 0.7156 0.5362 0.6704 0.0478  -0.0868 -0.0256 86  ASP   B OD1 
883  O  OD2 . ASP   B 77  ? 0.7560 0.5668 0.7198 0.0254  -0.0845 -0.0150 86  ASP   B OD2 
884  N  N   . ALA   B 78  ? 0.5194 0.3215 0.4206 0.0869  -0.0889 -0.0272 87  ALA   B N   
885  C  CA  . ALA   B 78  ? 0.5278 0.3128 0.4118 0.1022  -0.1011 -0.0320 87  ALA   B CA  
886  C  C   . ALA   B 78  ? 0.5360 0.3196 0.4004 0.1121  -0.0962 -0.0273 87  ALA   B C   
887  O  O   . ALA   B 78  ? 0.5226 0.3215 0.3871 0.1102  -0.0836 -0.0220 87  ALA   B O   
888  C  CB  . ALA   B 78  ? 0.5165 0.3043 0.3994 0.1150  -0.1066 -0.0394 87  ALA   B CB  
889  N  N   . ALA   B 79  ? 0.5580 0.3232 0.4056 0.1226  -0.1072 -0.0297 88  ALA   B N   
890  C  CA  . ALA   B 79  ? 0.5796 0.3442 0.4084 0.1335  -0.1042 -0.0259 88  ALA   B CA  
891  C  C   . ALA   B 79  ? 0.5944 0.3510 0.4042 0.1551  -0.1134 -0.0311 88  ALA   B C   
892  O  O   . ALA   B 79  ? 0.5994 0.3394 0.4061 0.1610  -0.1274 -0.0383 88  ALA   B O   
893  C  CB  . ALA   B 79  ? 0.5971 0.3457 0.4198 0.1268  -0.1082 -0.0227 88  ALA   B CB  
894  N  N   . TRP   B 80  ? 0.5930 0.3615 0.3898 0.1676  -0.1062 -0.0275 89  TRP   B N   
895  C  CA  . TRP   B 80  ? 0.6123 0.3752 0.3884 0.1904  -0.1139 -0.0312 89  TRP   B CA  
896  C  C   . TRP   B 80  ? 0.6376 0.3745 0.3980 0.1972  -0.1291 -0.0354 89  TRP   B C   
897  O  O   . TRP   B 80  ? 0.6292 0.3593 0.3890 0.1881  -0.1284 -0.0318 89  TRP   B O   
898  C  CB  . TRP   B 80  ? 0.6102 0.3932 0.3767 0.2003  -0.1023 -0.0248 89  TRP   B CB  
899  C  CG  . TRP   B 80  ? 0.6213 0.4028 0.3663 0.2249  -0.1081 -0.0273 89  TRP   B CG  
900  C  CD1 . TRP   B 80  ? 0.6436 0.4175 0.3804 0.2394  -0.1164 -0.0332 89  TRP   B CD1 
901  C  CD2 . TRP   B 80  ? 0.6292 0.4181 0.3571 0.2393  -0.1063 -0.0240 89  TRP   B CD2 
902  N  NE1 . TRP   B 80  ? 0.6623 0.4380 0.3770 0.2625  -0.1194 -0.0335 89  TRP   B NE1 
903  C  CE2 . TRP   B 80  ? 0.6509 0.4373 0.3606 0.2627  -0.1128 -0.0277 89  TRP   B CE2 
904  C  CE3 . TRP   B 80  ? 0.6343 0.4341 0.3606 0.2358  -0.0995 -0.0186 89  TRP   B CE3 
905  C  CZ2 . TRP   B 80  ? 0.6655 0.4606 0.3558 0.2825  -0.1125 -0.0256 89  TRP   B CZ2 
906  C  CZ3 . TRP   B 80  ? 0.6468 0.4558 0.3551 0.2550  -0.0996 -0.0171 89  TRP   B CZ3 
907  C  CH2 . TRP   B 80  ? 0.6514 0.4584 0.3420 0.2780  -0.1058 -0.0203 89  TRP   B CH2 
908  N  N   . ASP   B 81  ? 0.6660 0.3866 0.4134 0.2129  -0.1436 -0.0433 90  ASP   B N   
909  C  CA  . ASP   B 81  ? 0.7063 0.3982 0.4369 0.2203  -0.1601 -0.0483 90  ASP   B CA  
910  C  C   . ASP   B 81  ? 0.7512 0.4423 0.4568 0.2389  -0.1605 -0.0461 90  ASP   B C   
911  O  O   . ASP   B 81  ? 0.7823 0.4479 0.4710 0.2462  -0.1740 -0.0499 90  ASP   B O   
912  C  CB  . ASP   B 81  ? 0.7181 0.3904 0.4441 0.2301  -0.1777 -0.0590 90  ASP   B CB  
913  C  CG  . ASP   B 81  ? 0.7711 0.4508 0.4809 0.2549  -0.1799 -0.0631 90  ASP   B CG  
914  O  OD1 . ASP   B 81  ? 0.7673 0.4667 0.4673 0.2662  -0.1680 -0.0570 90  ASP   B OD1 
915  O  OD2 . ASP   B 81  ? 0.8249 0.4912 0.5313 0.2639  -0.1938 -0.0725 90  ASP   B OD2 
916  N  N   . GLY   B 82  ? 0.7490 0.4673 0.4522 0.2466  -0.1464 -0.0402 91  GLY   B N   
917  C  CA  . GLY   B 82  ? 0.7674 0.4907 0.4490 0.2646  -0.1458 -0.0379 91  GLY   B CA  
918  C  C   . GLY   B 82  ? 0.7885 0.5065 0.4465 0.2927  -0.1556 -0.0435 91  GLY   B C   
919  O  O   . GLY   B 82  ? 0.8022 0.5259 0.4408 0.3107  -0.1559 -0.0422 91  GLY   B O   
920  N  N   . LEU   B 83  ? 0.7953 0.5035 0.4538 0.2982  -0.1641 -0.0503 92  LEU   B N   
921  C  CA  . LEU   B 83  ? 0.8279 0.5282 0.4619 0.3267  -0.1753 -0.0569 92  LEU   B CA  
922  C  C   . LEU   B 83  ? 0.8245 0.5402 0.4615 0.3360  -0.1701 -0.0575 92  LEU   B C   
923  O  O   . LEU   B 83  ? 0.8353 0.5588 0.4526 0.3608  -0.1705 -0.0580 92  LEU   B O   
924  C  CB  . LEU   B 83  ? 0.8614 0.5233 0.4848 0.3307  -0.1984 -0.0681 92  LEU   B CB  
925  C  CG  . LEU   B 83  ? 0.9238 0.5594 0.5338 0.3297  -0.2096 -0.0699 92  LEU   B CG  
926  C  CD1 . LEU   B 83  ? 0.9524 0.5498 0.5511 0.3359  -0.2335 -0.0818 92  LEU   B CD1 
927  C  CD2 . LEU   B 83  ? 0.9422 0.5864 0.5265 0.3530  -0.2075 -0.0672 92  LEU   B CD2 
928  N  N   . SER   B 84  ? 0.8018 0.5190 0.4609 0.3183  -0.1672 -0.0583 93  SER   B N   
929  C  CA  . SER   B 84  ? 0.7966 0.5225 0.4580 0.3262  -0.1649 -0.0604 93  SER   B CA  
930  C  C   . SER   B 84  ? 0.7617 0.5181 0.4332 0.3221  -0.1438 -0.0500 93  SER   B C   
931  O  O   . SER   B 84  ? 0.7449 0.5167 0.4316 0.3042  -0.1302 -0.0418 93  SER   B O   
932  C  CB  . SER   B 84  ? 0.8300 0.5415 0.5098 0.3106  -0.1742 -0.0678 93  SER   B CB  
933  O  OG  . SER   B 84  ? 0.8869 0.5689 0.5610 0.3102  -0.1940 -0.0770 93  SER   B OG  
934  N  N   . GLU   B 85  ? 0.7392 0.5026 0.4022 0.3384  -0.1418 -0.0506 94  GLU   B N   
935  C  CA  . GLU   B 85  ? 0.7098 0.4976 0.3820 0.3339  -0.1229 -0.0409 94  GLU   B CA  
936  C  C   . GLU   B 85  ? 0.6828 0.4699 0.3809 0.3090  -0.1191 -0.0416 94  GLU   B C   
937  O  O   . GLU   B 85  ? 0.6884 0.4581 0.3948 0.3010  -0.1320 -0.0504 94  GLU   B O   
938  C  CB  . GLU   B 85  ? 0.7264 0.5194 0.3798 0.3594  -0.1218 -0.0406 94  GLU   B CB  
939  C  CG  . GLU   B 85  ? 0.7645 0.5675 0.3948 0.3828  -0.1197 -0.0364 94  GLU   B CG  
940  C  CD  . GLU   B 85  ? 0.8487 0.6644 0.4618 0.4064  -0.1125 -0.0317 94  GLU   B CD  
941  O  OE1 . GLU   B 85  ? 0.8482 0.6574 0.4611 0.4101  -0.1144 -0.0349 94  GLU   B OE1 
942  O  OE2 . GLU   B 85  ? 0.8749 0.7083 0.4746 0.4214  -0.1044 -0.0242 94  GLU   B OE2 
943  N  N   . VAL   B 86  ? 0.6443 0.4507 0.3557 0.2961  -0.1016 -0.0322 95  VAL   B N   
944  C  CA  . VAL   B 86  ? 0.6129 0.4216 0.3469 0.2744  -0.0960 -0.0318 95  VAL   B CA  
945  C  C   . VAL   B 86  ? 0.6084 0.4296 0.3419 0.2789  -0.0834 -0.0258 95  VAL   B C   
946  O  O   . VAL   B 86  ? 0.6294 0.4583 0.3467 0.2966  -0.0783 -0.0209 95  VAL   B O   
947  C  CB  . VAL   B 86  ? 0.5779 0.3962 0.3276 0.2525  -0.0864 -0.0254 95  VAL   B CB  
948  C  CG1 . VAL   B 86  ? 0.5821 0.3873 0.3286 0.2497  -0.0973 -0.0293 95  VAL   B CG1 
949  C  CG2 . VAL   B 86  ? 0.5692 0.4090 0.3168 0.2538  -0.0705 -0.0145 95  VAL   B CG2 
950  N  N   . GLN   B 87  ? 0.5815 0.4050 0.3317 0.2635  -0.0778 -0.0255 96  GLN   B N   
951  C  CA  . GLN   B 87  ? 0.5731 0.4057 0.3222 0.2660  -0.0653 -0.0189 96  GLN   B CA  
952  C  C   . GLN   B 87  ? 0.5501 0.3934 0.3173 0.2438  -0.0519 -0.0120 96  GLN   B C   
953  O  O   . GLN   B 87  ? 0.5318 0.3720 0.3148 0.2276  -0.0548 -0.0161 96  GLN   B O   
954  C  CB  . GLN   B 87  ? 0.5750 0.3973 0.3211 0.2751  -0.0729 -0.0266 96  GLN   B CB  
955  C  CG  . GLN   B 87  ? 0.5862 0.4001 0.3094 0.3018  -0.0834 -0.0316 96  GLN   B CG  
956  C  CD  . GLN   B 87  ? 0.6279 0.4333 0.3446 0.3148  -0.0905 -0.0389 96  GLN   B CD  
957  O  OE1 . GLN   B 87  ? 0.6178 0.4234 0.3467 0.3050  -0.0879 -0.0406 96  GLN   B OE1 
958  N  NE2 . GLN   B 87  ? 0.6573 0.4552 0.3521 0.3402  -0.1000 -0.0437 96  GLN   B NE2 
959  N  N   . LEU   B 88  ? 0.5442 0.4001 0.3090 0.2435  -0.0376 -0.0015 97  LEU   B N   
960  C  CA  . LEU   B 88  ? 0.5328 0.3962 0.3128 0.2242  -0.0259 0.0043  97  LEU   B CA  
961  C  C   . LEU   B 88  ? 0.5454 0.4015 0.3234 0.2275  -0.0235 0.0035  97  LEU   B C   
962  O  O   . LEU   B 88  ? 0.5609 0.4156 0.3237 0.2437  -0.0207 0.0070  97  LEU   B O   
963  C  CB  . LEU   B 88  ? 0.5242 0.4040 0.3038 0.2213  -0.0124 0.0159  97  LEU   B CB  
964  C  CG  . LEU   B 88  ? 0.5440 0.4293 0.3361 0.2041  -0.0003 0.0224  97  LEU   B CG  
965  C  CD1 . LEU   B 88  ? 0.5205 0.4046 0.3299 0.1843  -0.0027 0.0176  97  LEU   B CD1 
966  C  CD2 . LEU   B 88  ? 0.5499 0.4516 0.3412 0.2030  0.0123  0.0340  97  LEU   B CD2 
967  N  N   . LEU   B 89  ? 0.5248 0.3765 0.3163 0.2141  -0.0248 -0.0012 98  LEU   B N   
968  C  CA  . LEU   B 89  ? 0.5320 0.3771 0.3210 0.2175  -0.0224 -0.0021 98  LEU   B CA  
969  C  C   . LEU   B 89  ? 0.5367 0.3874 0.3311 0.2047  -0.0083 0.0074  98  LEU   B C   
970  O  O   . LEU   B 89  ? 0.5199 0.3719 0.3285 0.1881  -0.0061 0.0059  98  LEU   B O   
971  C  CB  . LEU   B 89  ? 0.5412 0.3808 0.3422 0.2113  -0.0319 -0.0127 98  LEU   B CB  
972  C  CG  . LEU   B 89  ? 0.5651 0.3988 0.3646 0.2147  -0.0306 -0.0154 98  LEU   B CG  
973  C  CD1 . LEU   B 89  ? 0.5974 0.4238 0.3759 0.2367  -0.0308 -0.0140 98  LEU   B CD1 
974  C  CD2 . LEU   B 89  ? 0.5749 0.4079 0.3882 0.2095  -0.0411 -0.0265 98  LEU   B CD2 
975  N  N   . ALA   B 90  ? 0.5276 0.3829 0.3112 0.2116  0.0012  0.0175  99  ALA   B N   
976  C  CA  . ALA   B 90  ? 0.5341 0.3945 0.3230 0.1988  0.0143  0.0274  99  ALA   B CA  
977  C  C   . ALA   B 90  ? 0.5329 0.3811 0.3197 0.1965  0.0182  0.0279  99  ALA   B C   
978  O  O   . ALA   B 90  ? 0.5476 0.3861 0.3198 0.2120  0.0170  0.0276  99  ALA   B O   
979  C  CB  . ALA   B 90  ? 0.5398 0.4101 0.3193 0.2065  0.0237  0.0389  99  ALA   B CB  
980  N  N   . VAL   B 91  ? 0.5072 0.3550 0.3062 0.1788  0.0229  0.0290  100 VAL   B N   
981  C  CA  . VAL   B 91  ? 0.5105 0.3451 0.3060 0.1764  0.0268  0.0298  100 VAL   B CA  
982  C  C   . VAL   B 91  ? 0.5298 0.3660 0.3285 0.1633  0.0387  0.0410  100 VAL   B C   
983  O  O   . VAL   B 91  ? 0.5162 0.3545 0.3276 0.1469  0.0401  0.0399  100 VAL   B O   
984  C  CB  . VAL   B 91  ? 0.5173 0.3477 0.3234 0.1684  0.0200  0.0193  100 VAL   B CB  
985  C  CG1 . VAL   B 91  ? 0.5361 0.3517 0.3355 0.1689  0.0233  0.0196  100 VAL   B CG1 
986  C  CG2 . VAL   B 91  ? 0.5170 0.3489 0.3247 0.1778  0.0079  0.0086  100 VAL   B CG2 
987  N  N   . PRO   B 92  ? 0.5467 0.3835 0.3346 0.1703  0.0473  0.0522  101 PRO   B N   
988  C  CA  . PRO   B 92  ? 0.5472 0.3874 0.3407 0.1563  0.0585  0.0636  101 PRO   B CA  
989  C  C   . PRO   B 92  ? 0.5406 0.3612 0.3309 0.1485  0.0624  0.0656  101 PRO   B C   
990  O  O   . PRO   B 92  ? 0.5611 0.3653 0.3387 0.1595  0.0592  0.0617  101 PRO   B O   
991  C  CB  . PRO   B 92  ? 0.5680 0.4152 0.3493 0.1688  0.0665  0.0753  101 PRO   B CB  
992  C  CG  . PRO   B 92  ? 0.5784 0.4291 0.3497 0.1887  0.0576  0.0680  101 PRO   B CG  
993  C  CD  . PRO   B 92  ? 0.5551 0.3912 0.3258 0.1912  0.0471  0.0551  101 PRO   B CD  
994  N  N   . PRO   B 93  ? 0.5371 0.3585 0.3382 0.1301  0.0684  0.0712  102 PRO   B N   
995  C  CA  . PRO   B 93  ? 0.5516 0.3510 0.3481 0.1226  0.0709  0.0727  102 PRO   B CA  
996  C  C   . PRO   B 93  ? 0.5923 0.3733 0.3684 0.1349  0.0772  0.0815  102 PRO   B C   
997  O  O   . PRO   B 93  ? 0.5942 0.3822 0.3651 0.1394  0.0854  0.0931  102 PRO   B O   
998  C  CB  . PRO   B 93  ? 0.5482 0.3549 0.3602 0.1016  0.0763  0.0788  102 PRO   B CB  
999  C  CG  . PRO   B 93  ? 0.5420 0.3747 0.3695 0.0973  0.0725  0.0741  102 PRO   B CG  
1000 C  CD  . PRO   B 93  ? 0.5186 0.3606 0.3363 0.1159  0.0718  0.0753  102 PRO   B CD  
1001 N  N   . GLY   B 94  ? 0.6114 0.3703 0.3750 0.1422  0.0731  0.0759  103 GLY   B N   
1002 C  CA  . GLY   B 94  ? 0.6331 0.3707 0.3743 0.1557  0.0778  0.0828  103 GLY   B CA  
1003 C  C   . GLY   B 94  ? 0.6405 0.3830 0.3668 0.1783  0.0774  0.0842  103 GLY   B C   
1004 O  O   . GLY   B 94  ? 0.6588 0.3858 0.3649 0.1908  0.0830  0.0922  103 GLY   B O   
1005 N  N   . GLU   B 95  ? 0.6299 0.3929 0.3645 0.1843  0.0705  0.0765  104 GLU   B N   
1006 C  CA  . GLU   B 95  ? 0.6479 0.4166 0.3689 0.2062  0.0682  0.0762  104 GLU   B CA  
1007 C  C   . GLU   B 95  ? 0.6463 0.4184 0.3696 0.2167  0.0538  0.0598  104 GLU   B C   
1008 O  O   . GLU   B 95  ? 0.6191 0.3981 0.3593 0.2047  0.0472  0.0505  104 GLU   B O   
1009 C  CB  . GLU   B 95  ? 0.6473 0.4384 0.3736 0.2055  0.0745  0.0855  104 GLU   B CB  
1010 C  CG  . GLU   B 95  ? 0.6681 0.4609 0.3974 0.1920  0.0889  0.1020  104 GLU   B CG  
1011 C  CD  . GLU   B 95  ? 0.7306 0.5492 0.4676 0.1900  0.0964  0.1119  104 GLU   B CD  
1012 O  OE1 . GLU   B 95  ? 0.6851 0.5209 0.4268 0.1969  0.0895  0.1048  104 GLU   B OE1 
1013 O  OE2 . GLU   B 95  ? 0.7462 0.5678 0.4840 0.1819  0.1091  0.1271  104 GLU   B OE2 
1014 N  N   . ARG   B 96  ? 0.6600 0.4272 0.3661 0.2393  0.0488  0.0563  105 ARG   B N   
1015 C  CA  . ARG   B 96  ? 0.6698 0.4400 0.3784 0.2498  0.0343  0.0406  105 ARG   B CA  
1016 C  C   . ARG   B 96  ? 0.6396 0.4285 0.3638 0.2443  0.0277  0.0349  105 ARG   B C   
1017 O  O   . ARG   B 96  ? 0.6262 0.4264 0.3507 0.2435  0.0333  0.0431  105 ARG   B O   
1018 C  CB  . ARG   B 96  ? 0.7380 0.5002 0.4237 0.2763  0.0304  0.0391  105 ARG   B CB  
1019 C  CG  . ARG   B 96  ? 0.8205 0.5800 0.5066 0.2878  0.0152  0.0224  105 ARG   B CG  
1020 C  CD  . ARG   B 96  ? 0.9016 0.6456 0.5632 0.3114  0.0131  0.0210  105 ARG   B CD  
1021 N  NE  . ARG   B 96  ? 0.9670 0.7089 0.6074 0.3285  0.0196  0.0314  105 ARG   B NE  
1022 C  CZ  . ARG   B 96  ? 1.0327 0.7601 0.6522 0.3368  0.0310  0.0440  105 ARG   B CZ  
1023 N  NH1 . ARG   B 96  ? 1.0386 0.7497 0.6547 0.3294  0.0362  0.0472  105 ARG   B NH1 
1024 N  NH2 . ARG   B 96  ? 1.0430 0.7715 0.6438 0.3532  0.0373  0.0539  105 ARG   B NH2 
1025 N  N   . ALA   B 97  ? 0.6320 0.4246 0.3686 0.2418  0.0155  0.0211  106 ALA   B N   
1026 C  CA  . ALA   B 97  ? 0.6300 0.4365 0.3795 0.2378  0.0075  0.0149  106 ALA   B CA  
1027 C  C   . ALA   B 97  ? 0.6487 0.4571 0.3829 0.2582  0.0033  0.0153  106 ALA   B C   
1028 O  O   . ALA   B 97  ? 0.6642 0.4632 0.3820 0.2771  -0.0007 0.0123  106 ALA   B O   
1029 C  CB  . ALA   B 97  ? 0.6217 0.4294 0.3845 0.2338  -0.0046 0.0010  106 ALA   B CB  
1030 N  N   . LYS   B 98  ? 0.6420 0.4621 0.3796 0.2560  0.0041  0.0188  107 LYS   B N   
1031 C  CA  . LYS   B 98  ? 0.6768 0.4995 0.3984 0.2761  0.0008  0.0199  107 LYS   B CA  
1032 C  C   . LYS   B 98  ? 0.6606 0.4927 0.3911 0.2727  -0.0074 0.0145  107 LYS   B C   
1033 O  O   . LYS   B 98  ? 0.6359 0.4775 0.3813 0.2548  -0.0028 0.0180  107 LYS   B O   
1034 C  CB  . LYS   B 98  ? 0.7367 0.5642 0.4468 0.2800  0.0162  0.0358  107 LYS   B CB  
1035 C  CG  . LYS   B 98  ? 0.8466 0.6770 0.5352 0.3043  0.0166  0.0401  107 LYS   B CG  
1036 C  CD  . LYS   B 98  ? 0.9394 0.7825 0.6250 0.3010  0.0339  0.0577  107 LYS   B CD  
1037 C  CE  . LYS   B 98  ? 0.9932 0.8500 0.7014 0.2758  0.0404  0.0624  107 LYS   B CE  
1038 N  NZ  . LYS   B 98  ? 1.0239 0.8998 0.7311 0.2760  0.0529  0.0764  107 LYS   B NZ  
1039 N  N   . ASN   B 99  ? 0.6551 0.4829 0.3759 0.2899  -0.0208 0.0053  108 ASN   B N   
1040 C  CA  . ASN   B 99  ? 0.6549 0.4868 0.3803 0.2894  -0.0307 -0.0006 108 ASN   B CA  
1041 C  C   . ASN   B 99  ? 0.6575 0.4984 0.3686 0.3024  -0.0257 0.0074  108 ASN   B C   
1042 O  O   . ASN   B 99  ? 0.6651 0.5043 0.3562 0.3233  -0.0236 0.0110  108 ASN   B O   
1043 C  CB  . ASN   B 99  ? 0.6665 0.4875 0.3885 0.3012  -0.0492 -0.0153 108 ASN   B CB  
1044 C  CG  . ASN   B 99  ? 0.6934 0.5095 0.4324 0.2883  -0.0560 -0.0246 108 ASN   B CG  
1045 O  OD1 . ASN   B 99  ? 0.7168 0.5300 0.4558 0.2883  -0.0518 -0.0243 108 ASN   B OD1 
1046 N  ND2 . ASN   B 99  ? 0.6761 0.4916 0.4297 0.2774  -0.0666 -0.0326 108 ASN   B ND2 
1047 N  N   . ILE   B 100 ? 0.6391 0.4903 0.3592 0.2919  -0.0240 0.0101  109 ILE   B N   
1048 C  CA  . ILE   B 100 ? 0.6374 0.5004 0.3459 0.3039  -0.0199 0.0169  109 ILE   B CA  
1049 C  C   . ILE   B 100 ? 0.6397 0.4997 0.3482 0.3065  -0.0336 0.0079  109 ILE   B C   
1050 O  O   . ILE   B 100 ? 0.6134 0.4737 0.3383 0.2880  -0.0360 0.0050  109 ILE   B O   
1051 C  CB  . ILE   B 100 ? 0.6486 0.5298 0.3665 0.2901  -0.0030 0.0305  109 ILE   B CB  
1052 C  CG1 . ILE   B 100 ? 0.6738 0.5539 0.3937 0.2832  0.0101  0.0395  109 ILE   B CG1 
1053 C  CG2 . ILE   B 100 ? 0.6512 0.5489 0.3573 0.3047  0.0015  0.0377  109 ILE   B CG2 
1054 C  CD1 . ILE   B 100 ? 0.7111 0.5904 0.4097 0.3045  0.0166  0.0472  109 ILE   B CD1 
1055 N  N   . GLN   B 101 ? 0.6564 0.5118 0.3450 0.3302  -0.0430 0.0035  110 GLN   B N   
1056 C  CA  . GLN   B 101 ? 0.6703 0.5184 0.3552 0.3350  -0.0577 -0.0055 110 GLN   B CA  
1057 C  C   . GLN   B 101 ? 0.6828 0.5470 0.3628 0.3387  -0.0513 0.0020  110 GLN   B C   
1058 O  O   . GLN   B 101 ? 0.7080 0.5876 0.3778 0.3505  -0.0399 0.0119  110 GLN   B O   
1059 C  CB  . GLN   B 101 ? 0.7116 0.5440 0.3760 0.3601  -0.0736 -0.0159 110 GLN   B CB  
1060 C  CG  . GLN   B 101 ? 0.7094 0.5275 0.3710 0.3628  -0.0918 -0.0273 110 GLN   B CG  
1061 C  CD  . GLN   B 101 ? 0.7525 0.5513 0.4015 0.3803  -0.1100 -0.0404 110 GLN   B CD  
1062 O  OE1 . GLN   B 101 ? 0.7370 0.5306 0.3914 0.3788  -0.1118 -0.0445 110 GLN   B OE1 
1063 N  NE2 . GLN   B 101 ? 0.7966 0.5840 0.4280 0.3982  -0.1247 -0.0480 110 GLN   B NE2 
1064 N  N   . THR   B 102 ? 0.6497 0.5112 0.3365 0.3292  -0.0584 -0.0023 111 THR   B N   
1065 C  CA  . THR   B 102 ? 0.6342 0.5116 0.3172 0.3323  -0.0533 0.0036  111 THR   B CA  
1066 C  C   . THR   B 102 ? 0.6352 0.4991 0.3159 0.3312  -0.0679 -0.0052 111 THR   B C   
1067 O  O   . THR   B 102 ? 0.6515 0.4971 0.3415 0.3190  -0.0780 -0.0133 111 THR   B O   
1068 C  CB  . THR   B 102 ? 0.6288 0.5280 0.3311 0.3114  -0.0356 0.0150  111 THR   B CB  
1069 O  OG1 . THR   B 102 ? 0.6498 0.5707 0.3469 0.3189  -0.0286 0.0223  111 THR   B OG1 
1070 C  CG2 . THR   B 102 ? 0.6236 0.5166 0.3475 0.2848  -0.0370 0.0116  111 THR   B CG2 
1071 N  N   . LEU   B 103 ? 0.6192 0.4919 0.2872 0.3441  -0.0689 -0.0033 112 LEU   B N   
1072 C  CA  . LEU   B 103 ? 0.6243 0.4831 0.2885 0.3427  -0.0817 -0.0103 112 LEU   B CA  
1073 C  C   . LEU   B 103 ? 0.6269 0.5035 0.3075 0.3236  -0.0704 -0.0031 112 LEU   B C   
1074 O  O   . LEU   B 103 ? 0.6256 0.5277 0.3051 0.3287  -0.0588 0.0054  112 LEU   B O   
1075 C  CB  . LEU   B 103 ? 0.6473 0.5030 0.2842 0.3711  -0.0916 -0.0139 112 LEU   B CB  
1076 C  CG  . LEU   B 103 ? 0.7019 0.5389 0.3335 0.3687  -0.1053 -0.0210 112 LEU   B CG  
1077 C  CD1 . LEU   B 103 ? 0.7188 0.5222 0.3494 0.3650  -0.1232 -0.0326 112 LEU   B CD1 
1078 C  CD2 . LEU   B 103 ? 0.7379 0.5806 0.3452 0.3938  -0.1099 -0.0213 112 LEU   B CD2 
1079 N  N   . PRO   B 104 ? 0.6223 0.4876 0.3188 0.3017  -0.0734 -0.0062 113 PRO   B N   
1080 C  CA  . PRO   B 104 ? 0.6040 0.4863 0.3155 0.2843  -0.0629 0.0001  113 PRO   B CA  
1081 C  C   . PRO   B 104 ? 0.6097 0.5010 0.3086 0.2961  -0.0650 0.0012  113 PRO   B C   
1082 O  O   . PRO   B 104 ? 0.6297 0.5043 0.3093 0.3127  -0.0784 -0.0052 113 PRO   B O   
1083 C  CB  . PRO   B 104 ? 0.6196 0.4833 0.3448 0.2635  -0.0689 -0.0049 113 PRO   B CB  
1084 C  CG  . PRO   B 104 ? 0.6227 0.4691 0.3497 0.2637  -0.0760 -0.0109 113 PRO   B CG  
1085 C  CD  . PRO   B 104 ? 0.6197 0.4594 0.3229 0.2911  -0.0852 -0.0148 113 PRO   B CD  
1086 N  N   . GLY   B 105 ? 0.6030 0.5201 0.3130 0.2874  -0.0525 0.0087  114 GLY   B N   
1087 C  CA  . GLY   B 105 ? 0.6074 0.5367 0.3107 0.2938  -0.0531 0.0098  114 GLY   B CA  
1088 C  C   . GLY   B 105 ? 0.6165 0.5327 0.3290 0.2755  -0.0572 0.0067  114 GLY   B C   
1089 O  O   . GLY   B 105 ? 0.6147 0.5099 0.3353 0.2616  -0.0617 0.0029  114 GLY   B O   
1090 N  N   . ILE   B 106 ? 0.6203 0.5496 0.3314 0.2759  -0.0556 0.0083  115 ILE   B N   
1091 C  CA  . ILE   B 106 ? 0.6386 0.5552 0.3554 0.2607  -0.0592 0.0060  115 ILE   B CA  
1092 C  C   . ILE   B 106 ? 0.6204 0.5646 0.3526 0.2485  -0.0480 0.0111  115 ILE   B C   
1093 O  O   . ILE   B 106 ? 0.6356 0.6058 0.3649 0.2594  -0.0432 0.0143  115 ILE   B O   
1094 C  CB  . ILE   B 106 ? 0.6806 0.5772 0.3740 0.2761  -0.0729 0.0007  115 ILE   B CB  
1095 C  CG1 . ILE   B 106 ? 0.7401 0.6099 0.4137 0.2933  -0.0866 -0.0056 115 ILE   B CG1 
1096 C  CG2 . ILE   B 106 ? 0.6966 0.5754 0.3935 0.2607  -0.0767 -0.0009 115 ILE   B CG2 
1097 C  CD1 . ILE   B 106 ? 0.7721 0.6170 0.4534 0.2807  -0.0921 -0.0093 115 ILE   B CD1 
1098 N  N   . PHE   B 107 ? 0.5918 0.5305 0.3390 0.2277  -0.0451 0.0112  116 PHE   B N   
1099 C  CA  . PHE   B 107 ? 0.5782 0.5370 0.3370 0.2169  -0.0382 0.0138  116 PHE   B CA  
1100 C  C   . PHE   B 107 ? 0.6212 0.5616 0.3651 0.2213  -0.0478 0.0099  116 PHE   B C   
1101 O  O   . PHE   B 107 ? 0.6367 0.5500 0.3789 0.2129  -0.0536 0.0074  116 PHE   B O   
1102 C  CB  . PHE   B 107 ? 0.5462 0.5056 0.3263 0.1935  -0.0308 0.0153  116 PHE   B CB  
1103 C  CG  . PHE   B 107 ? 0.5240 0.5057 0.3210 0.1854  -0.0194 0.0201  116 PHE   B CG  
1104 C  CD1 . PHE   B 107 ? 0.5250 0.5248 0.3191 0.1977  -0.0150 0.0241  116 PHE   B CD1 
1105 C  CD2 . PHE   B 107 ? 0.5143 0.4967 0.3287 0.1662  -0.0132 0.0210  116 PHE   B CD2 
1106 C  CE1 . PHE   B 107 ? 0.5201 0.5369 0.3290 0.1893  -0.0042 0.0297  116 PHE   B CE1 
1107 C  CE2 . PHE   B 107 ? 0.5006 0.4986 0.3287 0.1586  -0.0037 0.0255  116 PHE   B CE2 
1108 C  CZ  . PHE   B 107 ? 0.5060 0.5208 0.3317 0.1693  0.0010  0.0303  116 PHE   B CZ  
1109 N  N   . LYS   B 108 ? 0.6343 0.5897 0.3680 0.2339  -0.0492 0.0099  117 LYS   B N   
1110 C  CA  . LYS   B 108 ? 0.6613 0.5995 0.3787 0.2394  -0.0578 0.0068  117 LYS   B CA  
1111 C  C   . LYS   B 108 ? 0.6507 0.6032 0.3815 0.2248  -0.0514 0.0083  117 LYS   B C   
1112 O  O   . LYS   B 108 ? 0.6374 0.6228 0.3796 0.2242  -0.0440 0.0103  117 LYS   B O   
1113 C  CB  . LYS   B 108 ? 0.7047 0.6518 0.4009 0.2643  -0.0637 0.0051  117 LYS   B CB  
1114 C  CG  . LYS   B 108 ? 0.8088 0.7408 0.4870 0.2831  -0.0718 0.0026  117 LYS   B CG  
1115 C  CD  . LYS   B 108 ? 0.8923 0.8450 0.5534 0.3083  -0.0740 0.0020  117 LYS   B CD  
1116 C  CE  . LYS   B 108 ? 0.9820 0.9114 0.6164 0.3315  -0.0864 -0.0026 117 LYS   B CE  
1117 N  NZ  . LYS   B 108 ? 1.0259 0.9615 0.6365 0.3559  -0.0932 -0.0053 117 LYS   B NZ  
1118 N  N   . THR   B 109 ? 0.6496 0.5789 0.3799 0.2127  -0.0541 0.0075  118 THR   B N   
1119 C  CA  . THR   B 109 ? 0.6497 0.5908 0.3905 0.2003  -0.0487 0.0085  118 THR   B CA  
1120 C  C   . THR   B 109 ? 0.6777 0.5978 0.3990 0.2059  -0.0560 0.0071  118 THR   B C   
1121 O  O   . THR   B 109 ? 0.6929 0.5836 0.3959 0.2142  -0.0651 0.0060  118 THR   B O   
1122 C  CB  . THR   B 109 ? 0.6375 0.5757 0.3990 0.1784  -0.0417 0.0100  118 THR   B CB  
1123 O  OG1 . THR   B 109 ? 0.6517 0.5589 0.4073 0.1713  -0.0463 0.0099  118 THR   B OG1 
1124 C  CG2 . THR   B 109 ? 0.6236 0.5710 0.3993 0.1739  -0.0364 0.0114  118 THR   B CG2 
1125 N  N   . LYS   B 110 ? 0.6822 0.6149 0.4074 0.2006  -0.0525 0.0073  119 LYS   B N   
1126 C  CA  . LYS   B 110 ? 0.7159 0.6282 0.4221 0.2054  -0.0582 0.0069  119 LYS   B CA  
1127 C  C   . LYS   B 110 ? 0.7433 0.6199 0.4462 0.1934  -0.0605 0.0093  119 LYS   B C   
1128 O  O   . LYS   B 110 ? 0.7735 0.6249 0.4573 0.1979  -0.0663 0.0102  119 LYS   B O   
1129 C  CB  . LYS   B 110 ? 0.7259 0.6612 0.4384 0.2019  -0.0535 0.0062  119 LYS   B CB  
1130 C  CG  . LYS   B 110 ? 0.7657 0.7074 0.4996 0.1813  -0.0454 0.0076  119 LYS   B CG  
1131 C  CD  . LYS   B 110 ? 0.8120 0.7699 0.5469 0.1803  -0.0433 0.0059  119 LYS   B CD  
1132 C  CE  . LYS   B 110 ? 0.8605 0.8040 0.5990 0.1662  -0.0397 0.0077  119 LYS   B CE  
1133 N  NZ  . LYS   B 110 ? 0.8764 0.8345 0.6396 0.1500  -0.0324 0.0075  119 LYS   B NZ  
1134 N  N   . ASP   B 111 ? 0.7277 0.6028 0.4491 0.1782  -0.0556 0.0105  120 ASP   B N   
1135 C  CA  . ASP   B 111 ? 0.7427 0.5902 0.4658 0.1655  -0.0567 0.0129  120 ASP   B CA  
1136 C  C   . ASP   B 111 ? 0.7499 0.5783 0.4722 0.1668  -0.0628 0.0117  120 ASP   B C   
1137 O  O   . ASP   B 111 ? 0.7617 0.5748 0.4930 0.1538  -0.0624 0.0132  120 ASP   B O   
1138 C  CB  . ASP   B 111 ? 0.7516 0.6123 0.4964 0.1474  -0.0470 0.0146  120 ASP   B CB  
1139 C  CG  . ASP   B 111 ? 0.7978 0.6716 0.5412 0.1459  -0.0426 0.0152  120 ASP   B CG  
1140 O  OD1 . ASP   B 111 ? 0.8173 0.6767 0.5420 0.1531  -0.0468 0.0164  120 ASP   B OD1 
1141 O  OD2 . ASP   B 111 ? 0.8096 0.7066 0.5695 0.1381  -0.0357 0.0141  120 ASP   B OD2 
1142 N  N   . GLY   B 112 ? 0.7405 0.5710 0.4522 0.1829  -0.0686 0.0088  121 GLY   B N   
1143 C  CA  . GLY   B 112 ? 0.7441 0.5568 0.4529 0.1868  -0.0758 0.0065  121 GLY   B CA  
1144 C  C   . GLY   B 112 ? 0.7232 0.5584 0.4422 0.1921  -0.0720 0.0049  121 GLY   B C   
1145 O  O   . GLY   B 112 ? 0.7084 0.5738 0.4401 0.1897  -0.0626 0.0065  121 GLY   B O   
1146 N  N   . ASP   B 113 ? 0.7141 0.5336 0.4268 0.1996  -0.0796 0.0020  122 ASP   B N   
1147 C  CA  . ASP   B 113 ? 0.6975 0.5333 0.4152 0.2076  -0.0773 0.0008  122 ASP   B CA  
1148 C  C   . ASP   B 113 ? 0.6735 0.5093 0.4111 0.1925  -0.0726 0.0011  122 ASP   B C   
1149 O  O   . ASP   B 113 ? 0.6820 0.4973 0.4247 0.1810  -0.0764 0.0001  122 ASP   B O   
1150 C  CB  . ASP   B 113 ? 0.7362 0.5542 0.4316 0.2285  -0.0897 -0.0035 122 ASP   B CB  
1151 C  CG  . ASP   B 113 ? 0.8273 0.6521 0.5018 0.2487  -0.0936 -0.0043 122 ASP   B CG  
1152 O  OD1 . ASP   B 113 ? 0.8436 0.6880 0.5215 0.2463  -0.0868 -0.0015 122 ASP   B OD1 
1153 O  OD2 . ASP   B 113 ? 0.8843 0.6951 0.5384 0.2679  -0.1040 -0.0082 122 ASP   B OD2 
1154 N  N   . ILE   B 114 ? 0.6389 0.4987 0.3879 0.1928  -0.0640 0.0027  123 ILE   B N   
1155 C  CA  . ILE   B 114 ? 0.6285 0.4905 0.3944 0.1813  -0.0590 0.0029  123 ILE   B CA  
1156 C  C   . ILE   B 114 ? 0.6015 0.4710 0.3623 0.1957  -0.0592 0.0023  123 ILE   B C   
1157 O  O   . ILE   B 114 ? 0.5860 0.4744 0.3404 0.2077  -0.0554 0.0047  123 ILE   B O   
1158 C  CB  . ILE   B 114 ? 0.6333 0.5175 0.4181 0.1656  -0.0461 0.0069  123 ILE   B CB  
1159 C  CG1 . ILE   B 114 ? 0.6683 0.5506 0.4543 0.1559  -0.0450 0.0080  123 ILE   B CG1 
1160 C  CG2 . ILE   B 114 ? 0.6456 0.5293 0.4463 0.1535  -0.0415 0.0068  123 ILE   B CG2 
1161 C  CD1 . ILE   B 114 ? 0.6812 0.5873 0.4824 0.1444  -0.0342 0.0107  123 ILE   B CD1 
1162 N  N   . GLY   B 115 ? 0.5904 0.4478 0.3544 0.1950  -0.0627 -0.0006 124 GLY   B N   
1163 C  CA  . GLY   B 115 ? 0.5791 0.4439 0.3376 0.2090  -0.0618 -0.0007 124 GLY   B CA  
1164 C  C   . GLY   B 115 ? 0.5532 0.4449 0.3248 0.2029  -0.0472 0.0056  124 GLY   B C   
1165 O  O   . GLY   B 115 ? 0.5321 0.4312 0.3195 0.1855  -0.0398 0.0080  124 GLY   B O   
1166 N  N   . ALA   B 116 ? 0.5451 0.4514 0.3097 0.2171  -0.0431 0.0087  125 ALA   B N   
1167 C  CA  . ALA   B 116 ? 0.5380 0.4687 0.3148 0.2109  -0.0292 0.0158  125 ALA   B CA  
1168 C  C   . ALA   B 116 ? 0.5561 0.4896 0.3258 0.2241  -0.0265 0.0181  125 ALA   B C   
1169 O  O   . ALA   B 116 ? 0.5758 0.5041 0.3279 0.2439  -0.0336 0.0158  125 ALA   B O   
1170 C  CB  . ALA   B 116 ? 0.5351 0.4903 0.3126 0.2134  -0.0233 0.0204  125 ALA   B CB  
1171 N  N   . VAL   B 117 ? 0.5365 0.4770 0.3180 0.2145  -0.0166 0.0227  126 VAL   B N   
1172 C  CA  A VAL   B 117 ? 0.5492 0.4916 0.3226 0.2272  -0.0129 0.0260  126 VAL   B CA  
1173 C  CA  B VAL   B 117 ? 0.5569 0.4986 0.3318 0.2255  -0.0125 0.0260  126 VAL   B CA  
1174 C  C   . VAL   B 117 ? 0.5507 0.5193 0.3306 0.2254  0.0018  0.0367  126 VAL   B C   
1175 O  O   . VAL   B 117 ? 0.5329 0.5122 0.3295 0.2075  0.0106  0.0411  126 VAL   B O   
1176 C  CB  A VAL   B 117 ? 0.5568 0.4800 0.3324 0.2235  -0.0161 0.0219  126 VAL   B CB  
1177 C  CB  B VAL   B 117 ? 0.5802 0.5047 0.3630 0.2150  -0.0138 0.0225  126 VAL   B CB  
1178 C  CG1 A VAL   B 117 ? 0.5740 0.4739 0.3442 0.2262  -0.0313 0.0117  126 VAL   B CG1 
1179 C  CG1 B VAL   B 117 ? 0.5909 0.5206 0.3742 0.2167  -0.0039 0.0288  126 VAL   B CG1 
1180 C  CG2 A VAL   B 117 ? 0.5451 0.4709 0.3392 0.2022  -0.0074 0.0247  126 VAL   B CG2 
1181 C  CG2 B VAL   B 117 ? 0.6029 0.5039 0.3761 0.2237  -0.0285 0.0128  126 VAL   B CG2 
1182 N  N   . ALA   B 118 ? 0.5529 0.5333 0.3187 0.2453  0.0038  0.0410  127 ALA   B N   
1183 C  CA  . ALA   B 118 ? 0.5651 0.5733 0.3363 0.2455  0.0178  0.0521  127 ALA   B CA  
1184 C  C   . ALA   B 118 ? 0.5881 0.5939 0.3575 0.2476  0.0264  0.0589  127 ALA   B C   
1185 O  O   . ALA   B 118 ? 0.5980 0.6115 0.3532 0.2663  0.0300  0.0641  127 ALA   B O   
1186 C  CB  . ALA   B 118 ? 0.5750 0.6016 0.3325 0.2664  0.0166  0.0541  127 ALA   B CB  
1187 N  N   . LEU   B 119 ? 0.5835 0.5770 0.3655 0.2293  0.0293  0.0585  128 LEU   B N   
1188 C  CA  . LEU   B 119 ? 0.5933 0.5801 0.3743 0.2279  0.0372  0.0645  128 LEU   B CA  
1189 C  C   . LEU   B 119 ? 0.5999 0.5948 0.4011 0.2040  0.0478  0.0710  128 LEU   B C   
1190 O  O   . LEU   B 119 ? 0.5982 0.5901 0.4128 0.1876  0.0442  0.0655  128 LEU   B O   
1191 C  CB  . LEU   B 119 ? 0.6010 0.5594 0.3748 0.2312  0.0273  0.0551  128 LEU   B CB  
1192 C  CG  . LEU   B 119 ? 0.6323 0.5792 0.3864 0.2542  0.0149  0.0475  128 LEU   B CG  
1193 C  CD1 . LEU   B 119 ? 0.6411 0.5627 0.3945 0.2525  0.0030  0.0362  128 LEU   B CD1 
1194 C  CD2 . LEU   B 119 ? 0.6527 0.6071 0.3888 0.2761  0.0207  0.0548  128 LEU   B CD2 
1195 N  N   . ASP   B 120 ? 0.6017 0.6059 0.4044 0.2022  0.0605  0.0826  129 ASP   B N   
1196 C  CA  . ASP   B 120 ? 0.6108 0.6218 0.4323 0.1796  0.0699  0.0891  129 ASP   B CA  
1197 C  C   . ASP   B 120 ? 0.6098 0.6002 0.4295 0.1729  0.0745  0.0923  129 ASP   B C   
1198 O  O   . ASP   B 120 ? 0.6237 0.6123 0.4324 0.1829  0.0820  0.1009  129 ASP   B O   
1199 C  CB  . ASP   B 120 ? 0.6422 0.6848 0.4721 0.1776  0.0816  0.1013  129 ASP   B CB  
1200 C  CG  . ASP   B 120 ? 0.7099 0.7637 0.5630 0.1525  0.0883  0.1057  129 ASP   B CG  
1201 O  OD1 . ASP   B 120 ? 0.7361 0.7719 0.5969 0.1374  0.0839  0.0992  129 ASP   B OD1 
1202 O  OD2 . ASP   B 120 ? 0.7307 0.8120 0.5943 0.1483  0.0975  0.1154  129 ASP   B OD2 
1203 N  N   . TYR   B 121 ? 0.5853 0.5602 0.4148 0.1568  0.0704  0.0856  130 TYR   B N   
1204 C  CA  . TYR   B 121 ? 0.5790 0.5329 0.4066 0.1502  0.0736  0.0871  130 TYR   B CA  
1205 C  C   . TYR   B 121 ? 0.5548 0.5094 0.4005 0.1262  0.0779  0.0891  130 TYR   B C   
1206 O  O   . TYR   B 121 ? 0.5468 0.5163 0.4062 0.1157  0.0759  0.0863  130 TYR   B O   
1207 C  CB  . TYR   B 121 ? 0.5946 0.5261 0.4142 0.1568  0.0621  0.0748  130 TYR   B CB  
1208 C  CG  . TYR   B 121 ? 0.6089 0.5325 0.4089 0.1798  0.0583  0.0735  130 TYR   B CG  
1209 C  CD1 . TYR   B 121 ? 0.6349 0.5468 0.4220 0.1886  0.0641  0.0797  130 TYR   B CD1 
1210 C  CD2 . TYR   B 121 ? 0.6229 0.5498 0.4158 0.1937  0.0485  0.0661  130 TYR   B CD2 
1211 C  CE1 . TYR   B 121 ? 0.6656 0.5708 0.4334 0.2114  0.0601  0.0780  130 TYR   B CE1 
1212 C  CE2 . TYR   B 121 ? 0.6485 0.5672 0.4228 0.2157  0.0434  0.0637  130 TYR   B CE2 
1213 C  CZ  . TYR   B 121 ? 0.6836 0.5927 0.4454 0.2250  0.0494  0.0696  130 TYR   B CZ  
1214 O  OH  . TYR   B 121 ? 0.7331 0.6346 0.4750 0.2484  0.0441  0.0669  130 TYR   B OH  
1215 N  N   . PRO   B 122 ? 0.5479 0.4851 0.3924 0.1182  0.0829  0.0933  131 PRO   B N   
1216 C  CA  . PRO   B 122 ? 0.5330 0.4674 0.3930 0.0962  0.0850  0.0937  131 PRO   B CA  
1217 C  C   . PRO   B 122 ? 0.5081 0.4390 0.3765 0.0885  0.0748  0.0805  131 PRO   B C   
1218 O  O   . PRO   B 122 ? 0.5073 0.4285 0.3677 0.0986  0.0669  0.0718  131 PRO   B O   
1219 C  CB  . PRO   B 122 ? 0.5639 0.4721 0.4141 0.0949  0.0887  0.0973  131 PRO   B CB  
1220 C  CG  . PRO   B 122 ? 0.5806 0.4878 0.4136 0.1136  0.0942  0.1055  131 PRO   B CG  
1221 C  CD  . PRO   B 122 ? 0.5588 0.4768 0.3861 0.1299  0.0863  0.0978  131 PRO   B CD  
1222 N  N   . ALA   B 123 ? 0.4848 0.4241 0.3690 0.0713  0.0748  0.0793  132 ALA   B N   
1223 C  CA  . ALA   B 123 ? 0.4760 0.4130 0.3676 0.0637  0.0664  0.0679  132 ALA   B CA  
1224 C  C   . ALA   B 123 ? 0.4599 0.3728 0.3434 0.0666  0.0604  0.0594  132 ALA   B C   
1225 O  O   . ALA   B 123 ? 0.4509 0.3631 0.3353 0.0685  0.0530  0.0503  132 ALA   B O   
1226 C  CB  . ALA   B 123 ? 0.4807 0.4253 0.3883 0.0449  0.0680  0.0687  132 ALA   B CB  
1227 N  N   . GLY   B 124 ? 0.4650 0.3591 0.3403 0.0676  0.0638  0.0628  133 GLY   B N   
1228 C  CA  . GLY   B 124 ? 0.4769 0.3499 0.3438 0.0721  0.0587  0.0553  133 GLY   B CA  
1229 C  C   . GLY   B 124 ? 0.4589 0.3298 0.3162 0.0886  0.0530  0.0497  133 GLY   B C   
1230 O  O   . GLY   B 124 ? 0.4658 0.3236 0.3186 0.0928  0.0478  0.0423  133 GLY   B O   
1231 N  N   . THR   B 125 ? 0.4332 0.3177 0.2880 0.0982  0.0531  0.0525  134 THR   B N   
1232 C  CA  . THR   B 125 ? 0.4379 0.3206 0.2843 0.1136  0.0459  0.0465  134 THR   B CA  
1233 C  C   . THR   B 125 ? 0.4249 0.3152 0.2802 0.1093  0.0380  0.0379  134 THR   B C   
1234 O  O   . THR   B 125 ? 0.4289 0.3160 0.2803 0.1184  0.0305  0.0316  134 THR   B O   
1235 C  CB  . THR   B 125 ? 0.4695 0.3610 0.3060 0.1278  0.0490  0.0534  134 THR   B CB  
1236 O  OG1 . THR   B 125 ? 0.4778 0.3651 0.3078 0.1289  0.0586  0.0639  134 THR   B OG1 
1237 C  CG2 . THR   B 125 ? 0.4887 0.3740 0.3137 0.1454  0.0408  0.0471  134 THR   B CG2 
1238 N  N   . SER   B 126 ? 0.3937 0.2936 0.2609 0.0954  0.0394  0.0379  135 SER   B N   
1239 C  CA  . SER   B 126 ? 0.3975 0.3038 0.2717 0.0911  0.0331  0.0310  135 SER   B CA  
1240 C  C   . SER   B 126 ? 0.4004 0.2950 0.2740 0.0929  0.0266  0.0228  135 SER   B C   
1241 O  O   . SER   B 126 ? 0.4110 0.2956 0.2845 0.0897  0.0278  0.0210  135 SER   B O   
1242 C  CB  . SER   B 126 ? 0.4262 0.3396 0.3114 0.0761  0.0355  0.0310  135 SER   B CB  
1243 O  OG  . SER   B 126 ? 0.4612 0.3901 0.3510 0.0726  0.0403  0.0375  135 SER   B OG  
1244 N  N   . GLY   B 127 ? 0.3836 0.2797 0.2570 0.0976  0.0198  0.0180  136 GLY   B N   
1245 C  CA  . GLY   B 127 ? 0.3927 0.2812 0.2682 0.0985  0.0136  0.0108  136 GLY   B CA  
1246 C  C   . GLY   B 127 ? 0.3998 0.2806 0.2672 0.1122  0.0082  0.0081  136 GLY   B C   
1247 O  O   . GLY   B 127 ? 0.3990 0.2756 0.2697 0.1136  0.0017  0.0017  136 GLY   B O   
1248 N  N   . SER   B 128 ? 0.3985 0.2784 0.2554 0.1231  0.0106  0.0129  137 SER   B N   
1249 C  CA  . SER   B 128 ? 0.4103 0.2827 0.2575 0.1383  0.0043  0.0095  137 SER   B CA  
1250 C  C   . SER   B 128 ? 0.4144 0.2874 0.2627 0.1417  -0.0054 0.0041  137 SER   B C   
1251 O  O   . SER   B 128 ? 0.4193 0.2989 0.2684 0.1390  -0.0054 0.0064  137 SER   B O   
1252 C  CB  . SER   B 128 ? 0.4343 0.3076 0.2686 0.1504  0.0092  0.0166  137 SER   B CB  
1253 O  OG  . SER   B 128 ? 0.4794 0.3475 0.3115 0.1475  0.0172  0.0214  137 SER   B OG  
1254 N  N   . PRO   B 129 ? 0.4356 0.3009 0.2838 0.1478  -0.0144 -0.0033 138 PRO   B N   
1255 C  CA  . PRO   B 129 ? 0.4405 0.3032 0.2905 0.1492  -0.0246 -0.0085 138 PRO   B CA  
1256 C  C   . PRO   B 129 ? 0.4598 0.3189 0.2954 0.1651  -0.0302 -0.0084 138 PRO   B C   
1257 O  O   . PRO   B 129 ? 0.4633 0.3198 0.2873 0.1790  -0.0294 -0.0073 138 PRO   B O   
1258 C  CB  . PRO   B 129 ? 0.4512 0.3085 0.3085 0.1490  -0.0322 -0.0166 138 PRO   B CB  
1259 C  CG  . PRO   B 129 ? 0.4682 0.3224 0.3182 0.1583  -0.0288 -0.0165 138 PRO   B CG  
1260 C  CD  . PRO   B 129 ? 0.4511 0.3098 0.2988 0.1524  -0.0162 -0.0078 138 PRO   B CD  
1261 N  N   . ILE   B 130 ? 0.4483 0.3060 0.2833 0.1643  -0.0364 -0.0099 139 ILE   B N   
1262 C  CA  . ILE   B 130 ? 0.4846 0.3366 0.3049 0.1802  -0.0446 -0.0117 139 ILE   B CA  
1263 C  C   . ILE   B 130 ? 0.4932 0.3321 0.3167 0.1811  -0.0589 -0.0210 139 ILE   B C   
1264 O  O   . ILE   B 130 ? 0.4869 0.3244 0.3235 0.1666  -0.0609 -0.0229 139 ILE   B O   
1265 C  CB  . ILE   B 130 ? 0.5027 0.3612 0.3195 0.1784  -0.0420 -0.0070 139 ILE   B CB  
1266 C  CG1 . ILE   B 130 ? 0.5335 0.4076 0.3514 0.1751  -0.0281 0.0020  139 ILE   B CG1 
1267 C  CG2 . ILE   B 130 ? 0.5122 0.3636 0.3122 0.1960  -0.0517 -0.0096 139 ILE   B CG2 
1268 C  CD1 . ILE   B 130 ? 0.5519 0.4365 0.3723 0.1684  -0.0243 0.0060  139 ILE   B CD1 
1269 N  N   . LEU   B 131 ? 0.5151 0.3449 0.3274 0.1977  -0.0685 -0.0268 140 LEU   B N   
1270 C  CA  . LEU   B 131 ? 0.5422 0.3597 0.3586 0.1989  -0.0833 -0.0367 140 LEU   B CA  
1271 C  C   . LEU   B 131 ? 0.5569 0.3610 0.3586 0.2127  -0.0969 -0.0416 140 LEU   B C   
1272 O  O   . LEU   B 131 ? 0.5652 0.3698 0.3487 0.2292  -0.0959 -0.0389 140 LEU   B O   
1273 C  CB  . LEU   B 131 ? 0.5728 0.3888 0.3878 0.2090  -0.0867 -0.0422 140 LEU   B CB  
1274 C  CG  . LEU   B 131 ? 0.6096 0.4353 0.4276 0.2064  -0.0735 -0.0371 140 LEU   B CG  
1275 C  CD1 . LEU   B 131 ? 0.6339 0.4552 0.4470 0.2196  -0.0794 -0.0437 140 LEU   B CD1 
1276 C  CD2 . LEU   B 131 ? 0.6154 0.4490 0.4530 0.1851  -0.0663 -0.0349 140 LEU   B CD2 
1277 N  N   . ASP   B 132 ? 0.5561 0.3478 0.3653 0.2068  -0.1103 -0.0491 141 ASP   B N   
1278 C  CA  . ASP   B 132 ? 0.5895 0.3639 0.3843 0.2205  -0.1262 -0.0560 141 ASP   B CA  
1279 C  C   . ASP   B 132 ? 0.6200 0.3881 0.4102 0.2353  -0.1376 -0.0656 141 ASP   B C   
1280 O  O   . ASP   B 132 ? 0.6019 0.3795 0.4009 0.2334  -0.1321 -0.0662 141 ASP   B O   
1281 C  CB  . ASP   B 132 ? 0.5994 0.3605 0.4027 0.2065  -0.1357 -0.0585 141 ASP   B CB  
1282 C  CG  . ASP   B 132 ? 0.6152 0.3757 0.4422 0.1886  -0.1404 -0.0630 141 ASP   B CG  
1283 O  OD1 . ASP   B 132 ? 0.6250 0.3921 0.4599 0.1911  -0.1417 -0.0679 141 ASP   B OD1 
1284 O  OD2 . ASP   B 132 ? 0.6277 0.3816 0.4647 0.1731  -0.1428 -0.0615 141 ASP   B OD2 
1285 N  N   . LYS   B 133 ? 0.6570 0.4078 0.4329 0.2503  -0.1545 -0.0740 142 LYS   B N   
1286 C  CA  . LYS   B 133 ? 0.6894 0.4330 0.4589 0.2666  -0.1674 -0.0845 142 LYS   B CA  
1287 C  C   . LYS   B 133 ? 0.6977 0.4421 0.4904 0.2531  -0.1749 -0.0923 142 LYS   B C   
1288 O  O   . LYS   B 133 ? 0.7108 0.4544 0.5012 0.2655  -0.1830 -0.1007 142 LYS   B O   
1289 C  CB  . LYS   B 133 ? 0.7458 0.4690 0.4937 0.2861  -0.1855 -0.0927 142 LYS   B CB  
1290 C  CG  . LYS   B 133 ? 0.8506 0.5769 0.5737 0.3044  -0.1781 -0.0856 142 LYS   B CG  
1291 C  CD  . LYS   B 133 ? 0.9539 0.6589 0.6543 0.3232  -0.1959 -0.0932 142 LYS   B CD  
1292 C  CE  . LYS   B 133 ? 1.0227 0.7335 0.7057 0.3322  -0.1868 -0.0843 142 LYS   B CE  
1293 N  NZ  . LYS   B 133 ? 1.0828 0.7709 0.7449 0.3471  -0.2043 -0.0914 142 LYS   B NZ  
1294 N  N   . CYS   B 134 ? 0.6895 0.4367 0.5044 0.2287  -0.1723 -0.0897 143 CYS   B N   
1295 C  CA  . CYS   B 134 ? 0.6883 0.4419 0.5286 0.2136  -0.1766 -0.0954 143 CYS   B CA  
1296 C  C   . CYS   B 134 ? 0.6694 0.4442 0.5223 0.2053  -0.1598 -0.0895 143 CYS   B C   
1297 O  O   . CYS   B 134 ? 0.6712 0.4554 0.5452 0.1937  -0.1614 -0.0935 143 CYS   B O   
1298 C  CB  . CYS   B 134 ? 0.7148 0.4606 0.5726 0.1923  -0.1829 -0.0955 143 CYS   B CB  
1299 S  SG  . CYS   B 134 ? 0.8299 0.5458 0.6749 0.2006  -0.2067 -0.1049 143 CYS   B SG  
1300 N  N   . GLY   B 135 ? 0.6526 0.4353 0.4930 0.2111  -0.1443 -0.0803 144 GLY   B N   
1301 C  CA  . GLY   B 135 ? 0.6198 0.4188 0.4692 0.2039  -0.1291 -0.0747 144 GLY   B CA  
1302 C  C   . GLY   B 135 ? 0.5980 0.4063 0.4646 0.1811  -0.1182 -0.0673 144 GLY   B C   
1303 O  O   . GLY   B 135 ? 0.6001 0.4210 0.4751 0.1739  -0.1065 -0.0634 144 GLY   B O   
1304 N  N   . ARG   B 136 ? 0.5662 0.3671 0.4359 0.1709  -0.1219 -0.0653 145 ARG   B N   
1305 C  CA  . ARG   B 136 ? 0.5467 0.3557 0.4305 0.1507  -0.1117 -0.0581 145 ARG   B CA  
1306 C  C   . ARG   B 136 ? 0.5149 0.3298 0.3878 0.1514  -0.0973 -0.0483 145 ARG   B C   
1307 O  O   . ARG   B 136 ? 0.5099 0.3185 0.3649 0.1637  -0.0983 -0.0463 145 ARG   B O   
1308 C  CB  . ARG   B 136 ? 0.5835 0.3806 0.4737 0.1399  -0.1212 -0.0591 145 ARG   B CB  
1309 C  CG  . ARG   B 136 ? 0.6397 0.4338 0.5471 0.1337  -0.1346 -0.0679 145 ARG   B CG  
1310 C  CD  . ARG   B 136 ? 0.7270 0.5062 0.6395 0.1218  -0.1437 -0.0675 145 ARG   B CD  
1311 N  NE  . ARG   B 136 ? 0.8339 0.5910 0.7251 0.1364  -0.1563 -0.0715 145 ARG   B NE  
1312 C  CZ  . ARG   B 136 ? 0.9056 0.6439 0.7915 0.1312  -0.1641 -0.0702 145 ARG   B CZ  
1313 N  NH1 . ARG   B 136 ? 0.9126 0.6515 0.8124 0.1111  -0.1589 -0.0636 145 ARG   B NH1 
1314 N  NH2 . ARG   B 136 ? 0.9243 0.6421 0.7887 0.1473  -0.1766 -0.0750 145 ARG   B NH2 
1315 N  N   . VAL   B 137 ? 0.4692 0.2970 0.3535 0.1378  -0.0847 -0.0426 146 VAL   B N   
1316 C  CA  . VAL   B 137 ? 0.4601 0.2944 0.3368 0.1368  -0.0720 -0.0344 146 VAL   B CA  
1317 C  C   . VAL   B 137 ? 0.4690 0.2985 0.3427 0.1305  -0.0726 -0.0303 146 VAL   B C   
1318 O  O   . VAL   B 137 ? 0.4636 0.2937 0.3492 0.1163  -0.0721 -0.0291 146 VAL   B O   
1319 C  CB  . VAL   B 137 ? 0.4543 0.3020 0.3420 0.1266  -0.0599 -0.0310 146 VAL   B CB  
1320 C  CG1 . VAL   B 137 ? 0.4505 0.3044 0.3317 0.1241  -0.0481 -0.0230 146 VAL   B CG1 
1321 C  CG2 . VAL   B 137 ? 0.4610 0.3110 0.3481 0.1355  -0.0600 -0.0352 146 VAL   B CG2 
1322 N  N   . ILE   B 138 ? 0.4784 0.3037 0.3354 0.1417  -0.0731 -0.0277 147 ILE   B N   
1323 C  CA  . ILE   B 138 ? 0.4864 0.3067 0.3370 0.1389  -0.0741 -0.0241 147 ILE   B CA  
1324 C  C   . ILE   B 138 ? 0.4572 0.2912 0.3083 0.1324  -0.0609 -0.0165 147 ILE   B C   
1325 O  O   . ILE   B 138 ? 0.4603 0.2922 0.3066 0.1297  -0.0608 -0.0135 147 ILE   B O   
1326 C  CB  . ILE   B 138 ? 0.5145 0.3222 0.3455 0.1565  -0.0844 -0.0269 147 ILE   B CB  
1327 C  CG1 . ILE   B 138 ? 0.5297 0.3460 0.3479 0.1731  -0.0794 -0.0251 147 ILE   B CG1 
1328 C  CG2 . ILE   B 138 ? 0.5300 0.3205 0.3613 0.1600  -0.1001 -0.0353 147 ILE   B CG2 
1329 C  CD1 . ILE   B 138 ? 0.5647 0.3737 0.3614 0.1921  -0.0866 -0.0259 147 ILE   B CD1 
1330 N  N   . GLY   B 139 ? 0.4439 0.2905 0.3010 0.1295  -0.0507 -0.0140 148 GLY   B N   
1331 C  CA  . GLY   B 139 ? 0.4216 0.2811 0.2814 0.1223  -0.0391 -0.0080 148 GLY   B CA  
1332 C  C   . GLY   B 139 ? 0.4284 0.2969 0.2890 0.1245  -0.0306 -0.0056 148 GLY   B C   
1333 O  O   . GLY   B 139 ? 0.4488 0.3134 0.3050 0.1342  -0.0330 -0.0080 148 GLY   B O   
1334 N  N   . LEU   B 140 ? 0.4140 0.2933 0.2784 0.1170  -0.0210 -0.0007 149 LEU   B N   
1335 C  CA  . LEU   B 140 ? 0.4080 0.2942 0.2734 0.1166  -0.0124 0.0027  149 LEU   B CA  
1336 C  C   . LEU   B 140 ? 0.4215 0.3180 0.2806 0.1211  -0.0067 0.0088  149 LEU   B C   
1337 O  O   . LEU   B 140 ? 0.4185 0.3210 0.2760 0.1203  -0.0074 0.0103  149 LEU   B O   
1338 C  CB  . LEU   B 140 ? 0.3921 0.2822 0.2688 0.1027  -0.0064 0.0027  149 LEU   B CB  
1339 C  CG  . LEU   B 140 ? 0.3954 0.2807 0.2807 0.0971  -0.0099 -0.0024 149 LEU   B CG  
1340 C  CD1 . LEU   B 140 ? 0.3857 0.2759 0.2787 0.0867  -0.0031 -0.0021 149 LEU   B CD1 
1341 C  CD2 . LEU   B 140 ? 0.3995 0.2773 0.2823 0.1065  -0.0153 -0.0068 149 LEU   B CD2 
1342 N  N   . TYR   B 141 ? 0.4158 0.3149 0.2708 0.1269  -0.0013 0.0125  150 TYR   B N   
1343 C  CA  . TYR   B 141 ? 0.4297 0.3406 0.2799 0.1319  0.0051  0.0194  150 TYR   B CA  
1344 C  C   . TYR   B 141 ? 0.4284 0.3487 0.2885 0.1185  0.0142  0.0240  150 TYR   B C   
1345 O  O   . TYR   B 141 ? 0.4439 0.3572 0.3082 0.1122  0.0171  0.0233  150 TYR   B O   
1346 C  CB  . TYR   B 141 ? 0.4511 0.3577 0.2898 0.1467  0.0058  0.0216  150 TYR   B CB  
1347 C  CG  . TYR   B 141 ? 0.4765 0.3963 0.3117 0.1507  0.0153  0.0307  150 TYR   B CG  
1348 C  CD1 . TYR   B 141 ? 0.4910 0.4110 0.3296 0.1444  0.0243  0.0364  150 TYR   B CD1 
1349 C  CD2 . TYR   B 141 ? 0.4924 0.4240 0.3200 0.1616  0.0151  0.0340  150 TYR   B CD2 
1350 C  CE1 . TYR   B 141 ? 0.5088 0.4415 0.3458 0.1464  0.0338  0.0462  150 TYR   B CE1 
1351 C  CE2 . TYR   B 141 ? 0.5113 0.4587 0.3374 0.1652  0.0248  0.0433  150 TYR   B CE2 
1352 C  CZ  . TYR   B 141 ? 0.5302 0.4785 0.3621 0.1564  0.0345  0.0498  150 TYR   B CZ  
1353 O  OH  . TYR   B 141 ? 0.5643 0.5286 0.3961 0.1584  0.0447  0.0603  150 TYR   B OH  
1354 N  N   . GLY   B 142 ? 0.4240 0.3596 0.2873 0.1154  0.0183  0.0283  151 GLY   B N   
1355 C  CA  . GLY   B 142 ? 0.4284 0.3730 0.3022 0.1022  0.0260  0.0323  151 GLY   B CA  
1356 C  C   . GLY   B 142 ? 0.4277 0.3864 0.3100 0.0932  0.0265  0.0320  151 GLY   B C   
1357 O  O   . GLY   B 142 ? 0.4385 0.4046 0.3303 0.0820  0.0317  0.0346  151 GLY   B O   
1358 N  N   . ASN   B 143 ? 0.4124 0.3738 0.2906 0.0983  0.0206  0.0288  152 ASN   B N   
1359 C  CA  . ASN   B 143 ? 0.4175 0.3930 0.3016 0.0922  0.0207  0.0284  152 ASN   B CA  
1360 C  C   . ASN   B 143 ? 0.4322 0.4188 0.3077 0.1054  0.0182  0.0301  152 ASN   B C   
1361 O  O   . ASN   B 143 ? 0.4435 0.4191 0.3078 0.1157  0.0114  0.0271  152 ASN   B O   
1362 C  CB  . ASN   B 143 ? 0.4229 0.3898 0.3090 0.0850  0.0161  0.0226  152 ASN   B CB  
1363 C  CG  . ASN   B 143 ? 0.4303 0.4118 0.3225 0.0784  0.0168  0.0220  152 ASN   B CG  
1364 O  OD1 . ASN   B 143 ? 0.4261 0.4232 0.3263 0.0737  0.0215  0.0250  152 ASN   B OD1 
1365 N  ND2 . ASN   B 143 ? 0.4169 0.3940 0.3055 0.0780  0.0122  0.0183  152 ASN   B ND2 
1366 N  N   . GLY   B 144 ? 0.4411 0.4491 0.3217 0.1056  0.0234  0.0349  153 GLY   B N   
1367 C  CA  . GLY   B 144 ? 0.4528 0.4750 0.3250 0.1198  0.0220  0.0370  153 GLY   B CA  
1368 C  C   . GLY   B 144 ? 0.4629 0.5140 0.3456 0.1163  0.0275  0.0412  153 GLY   B C   
1369 O  O   . GLY   B 144 ? 0.4414 0.5001 0.3366 0.1028  0.0288  0.0396  153 GLY   B O   
1370 N  N   . VAL   B 145 ? 0.4822 0.5507 0.3601 0.1290  0.0306  0.0464  154 VAL   B N   
1371 C  CA  . VAL   B 145 ? 0.5097 0.6102 0.3980 0.1279  0.0357  0.0507  154 VAL   B CA  
1372 C  C   . VAL   B 145 ? 0.5516 0.6704 0.4423 0.1334  0.0451  0.0605  154 VAL   B C   
1373 O  O   . VAL   B 145 ? 0.5527 0.6582 0.4315 0.1435  0.0462  0.0631  154 VAL   B O   
1374 C  CB  . VAL   B 145 ? 0.5340 0.6429 0.4117 0.1413  0.0282  0.0459  154 VAL   B CB  
1375 C  CG1 . VAL   B 145 ? 0.5440 0.6506 0.4023 0.1638  0.0251  0.0471  154 VAL   B CG1 
1376 C  CG2 . VAL   B 145 ? 0.5394 0.6808 0.4306 0.1368  0.0308  0.0469  154 VAL   B CG2 
1377 N  N   . VAL   B 146 ? 0.5745 0.7241 0.4814 0.1260  0.0520  0.0660  155 VAL   B N   
1378 C  CA  . VAL   B 146 ? 0.6052 0.7773 0.5169 0.1299  0.0625  0.0770  155 VAL   B CA  
1379 C  C   . VAL   B 146 ? 0.6408 0.8420 0.5476 0.1466  0.0615  0.0777  155 VAL   B C   
1380 O  O   . VAL   B 146 ? 0.6294 0.8505 0.5466 0.1420  0.0588  0.0741  155 VAL   B O   
1381 C  CB  . VAL   B 146 ? 0.6036 0.7911 0.5394 0.1080  0.0711  0.0834  155 VAL   B CB  
1382 C  CG1 . VAL   B 146 ? 0.6040 0.8208 0.5470 0.1113  0.0829  0.0962  155 VAL   B CG1 
1383 C  CG2 . VAL   B 146 ? 0.6200 0.7763 0.5576 0.0934  0.0716  0.0824  155 VAL   B CG2 
1384 N  N   . ILE   B 147 ? 0.6820 0.8849 0.5711 0.1681  0.0623  0.0811  156 ILE   B N   
1385 C  CA  . ILE   B 147 ? 0.7142 0.9436 0.5951 0.1874  0.0603  0.0808  156 ILE   B CA  
1386 C  C   . ILE   B 147 ? 0.7277 1.0002 0.6234 0.1877  0.0732  0.0927  156 ILE   B C   
1387 O  O   . ILE   B 147 ? 0.7206 0.9975 0.6314 0.1722  0.0833  0.1015  156 ILE   B O   
1388 C  CB  . ILE   B 147 ? 0.7461 0.9535 0.5977 0.2125  0.0515  0.0759  156 ILE   B CB  
1389 C  CG1 . ILE   B 147 ? 0.7603 0.9670 0.6007 0.2259  0.0583  0.0839  156 ILE   B CG1 
1390 C  CG2 . ILE   B 147 ? 0.7710 0.9370 0.6127 0.2079  0.0401  0.0657  156 ILE   B CG2 
1391 C  CD1 . ILE   B 147 ? 0.7934 0.9827 0.6045 0.2534  0.0484  0.0783  156 ILE   B CD1 
1392 N  N   . LYS   B 148 ? 0.7390 1.0434 0.6307 0.2048  0.0727  0.0932  157 LYS   B N   
1393 C  CA  . LYS   B 148 ? 0.7472 1.0998 0.6545 0.2066  0.0843  0.1039  157 LYS   B CA  
1394 C  C   . LYS   B 148 ? 0.7618 1.1240 0.6661 0.2133  0.0973  0.1175  157 LYS   B C   
1395 O  O   . LYS   B 148 ? 0.7593 1.1596 0.6658 0.2261  0.1053  0.1257  157 LYS   B O   
1396 C  CB  . LYS   B 148 ? 0.7847 1.1671 0.6838 0.2278  0.0793  0.0998  157 LYS   B CB  
1397 C  CG  . LYS   B 148 ? 0.8831 1.2389 0.7485 0.2544  0.0668  0.0906  157 LYS   B CG  
1398 C  CD  . LYS   B 148 ? 0.9683 1.2969 0.8272 0.2500  0.0528  0.0775  157 LYS   B CD  
1399 C  CE  . LYS   B 148 ? 1.0147 1.3746 0.8898 0.2439  0.0511  0.0739  157 LYS   B CE  
1400 N  NZ  . LYS   B 148 ? 1.0394 1.3908 0.9366 0.2154  0.0511  0.0711  157 LYS   B NZ  
1401 N  N   . ASN   B 149 ? 0.7746 1.1042 0.6742 0.2052  0.0998  0.1203  158 ASN   B N   
1402 C  CA  . ASN   B 149 ? 0.7795 1.1120 0.6756 0.2091  0.1123  0.1335  158 ASN   B CA  
1403 C  C   . ASN   B 149 ? 0.7785 1.0845 0.6857 0.1851  0.1175  0.1377  158 ASN   B C   
1404 O  O   . ASN   B 149 ? 0.7910 1.0898 0.6916 0.1881  0.1267  0.1479  158 ASN   B O   
1405 C  CB  . ASN   B 149 ? 0.8205 1.1375 0.6840 0.2398  0.1087  0.1324  158 ASN   B CB  
1406 C  CG  . ASN   B 149 ? 0.8810 1.1743 0.7212 0.2582  0.0917  0.1175  158 ASN   B CG  
1407 O  OD1 . ASN   B 149 ? 0.8922 1.1987 0.7339 0.2621  0.0844  0.1103  158 ASN   B OD1 
1408 N  ND2 . ASN   B 149 ? 0.9043 1.1618 0.7216 0.2710  0.0848  0.1127  158 ASN   B ND2 
1409 N  N   . GLY   B 150 ? 0.7579 1.0488 0.6797 0.1633  0.1112  0.1298  159 GLY   B N   
1410 C  CA  . GLY   B 150 ? 0.7404 1.0039 0.6713 0.1413  0.1135  0.1312  159 GLY   B CA  
1411 C  C   . GLY   B 150 ? 0.7278 0.9467 0.6373 0.1484  0.1062  0.1244  159 GLY   B C   
1412 O  O   . GLY   B 150 ? 0.7382 0.9315 0.6524 0.1325  0.1065  0.1237  159 GLY   B O   
1413 N  N   . SER   B 151 ? 0.6989 0.9080 0.5846 0.1728  0.0989  0.1187  160 SER   B N   
1414 C  CA  A SER   B 151 ? 0.7026 0.8719 0.5693 0.1802  0.0911  0.1116  160 SER   B CA  
1415 C  CA  B SER   B 151 ? 0.7026 0.8722 0.5687 0.1811  0.0908  0.1114  160 SER   B CA  
1416 C  C   . SER   B 151 ? 0.6842 0.8297 0.5534 0.1697  0.0787  0.0981  160 SER   B C   
1417 O  O   . SER   B 151 ? 0.6799 0.8389 0.5614 0.1605  0.0753  0.0937  160 SER   B O   
1418 C  CB  A SER   B 151 ? 0.7283 0.8941 0.5692 0.2093  0.0869  0.1103  160 SER   B CB  
1419 C  CB  B SER   B 151 ? 0.7270 0.8947 0.5678 0.2104  0.0857  0.1093  160 SER   B CB  
1420 O  OG  A SER   B 151 ? 0.7676 0.9005 0.5936 0.2149  0.0837  0.1079  160 SER   B OG  
1421 O  OG  B SER   B 151 ? 0.7474 0.9289 0.5840 0.2210  0.0776  0.1022  160 SER   B OG  
1422 N  N   . TYR   B 152 ? 0.6472 0.7585 0.5050 0.1711  0.0724  0.0920  161 TYR   B N   
1423 C  CA  . TYR   B 152 ? 0.6130 0.7017 0.4730 0.1612  0.0621  0.0807  161 TYR   B CA  
1424 C  C   . TYR   B 152 ? 0.5732 0.6420 0.4142 0.1779  0.0496  0.0710  161 TYR   B C   
1425 O  O   . TYR   B 152 ? 0.5796 0.6370 0.4045 0.1939  0.0478  0.0714  161 TYR   B O   
1426 C  CB  . TYR   B 152 ? 0.6195 0.6861 0.4852 0.1465  0.0649  0.0813  161 TYR   B CB  
1427 C  CG  . TYR   B 152 ? 0.6315 0.6786 0.5022 0.1343  0.0564  0.0711  161 TYR   B CG  
1428 C  CD1 . TYR   B 152 ? 0.6324 0.6897 0.5187 0.1185  0.0559  0.0685  161 TYR   B CD1 
1429 C  CD2 . TYR   B 152 ? 0.6551 0.6748 0.5154 0.1388  0.0493  0.0641  161 TYR   B CD2 
1430 C  CE1 . TYR   B 152 ? 0.6516 0.6919 0.5411 0.1086  0.0491  0.0598  161 TYR   B CE1 
1431 C  CE2 . TYR   B 152 ? 0.6668 0.6713 0.5323 0.1279  0.0427  0.0558  161 TYR   B CE2 
1432 C  CZ  . TYR   B 152 ? 0.6710 0.6857 0.5503 0.1132  0.0431  0.0540  161 TYR   B CZ  
1433 O  OH  . TYR   B 152 ? 0.6902 0.6908 0.5733 0.1037  0.0375  0.0465  161 TYR   B OH  
1434 N  N   . VAL   B 153 ? 0.5282 0.5920 0.3707 0.1742  0.0407  0.0625  162 VAL   B N   
1435 C  CA  . VAL   B 153 ? 0.5005 0.5422 0.3271 0.1861  0.0283  0.0535  162 VAL   B CA  
1436 C  C   . VAL   B 153 ? 0.4694 0.4919 0.3042 0.1696  0.0227  0.0463  162 VAL   B C   
1437 O  O   . VAL   B 153 ? 0.4488 0.4807 0.2943 0.1582  0.0231  0.0449  162 VAL   B O   
1438 C  CB  . VAL   B 153 ? 0.5017 0.5549 0.3167 0.2023  0.0223  0.0510  162 VAL   B CB  
1439 C  CG1 . VAL   B 153 ? 0.5135 0.5390 0.3117 0.2130  0.0085  0.0418  162 VAL   B CG1 
1440 C  CG2 . VAL   B 153 ? 0.5114 0.5875 0.3185 0.2198  0.0287  0.0586  162 VAL   B CG2 
1441 N  N   . SER   B 154 ? 0.4657 0.4632 0.2958 0.1692  0.0178  0.0418  163 SER   B N   
1442 C  CA  . SER   B 154 ? 0.4521 0.4333 0.2901 0.1545  0.0135  0.0358  163 SER   B CA  
1443 C  C   . SER   B 154 ? 0.4448 0.4111 0.2733 0.1606  0.0021  0.0286  163 SER   B C   
1444 O  O   . SER   B 154 ? 0.4535 0.4092 0.2680 0.1757  -0.0047 0.0261  163 SER   B O   
1445 C  CB  . SER   B 154 ? 0.4685 0.4329 0.3077 0.1508  0.0145  0.0349  163 SER   B CB  
1446 O  OG  . SER   B 154 ? 0.4791 0.4284 0.3246 0.1394  0.0099  0.0288  163 SER   B OG  
1447 N  N   . ALA   B 155 ? 0.4361 0.3975 0.2715 0.1486  -0.0006 0.0250  164 ALA   B N   
1448 C  CA  . ALA   B 155 ? 0.4289 0.3715 0.2561 0.1517  -0.0110 0.0191  164 ALA   B CA  
1449 C  C   . ALA   B 155 ? 0.4435 0.3668 0.2713 0.1502  -0.0149 0.0155  164 ALA   B C   
1450 O  O   . ALA   B 155 ? 0.4529 0.3775 0.2893 0.1431  -0.0089 0.0170  164 ALA   B O   
1451 C  CB  . ALA   B 155 ? 0.4332 0.3753 0.2682 0.1380  -0.0110 0.0174  164 ALA   B CB  
1452 N  N   . ILE   B 156 ? 0.4383 0.3435 0.2573 0.1564  -0.0253 0.0105  165 ILE   B N   
1453 C  CA  . ILE   B 156 ? 0.4530 0.3415 0.2759 0.1523  -0.0306 0.0059  165 ILE   B CA  
1454 C  C   . ILE   B 156 ? 0.4441 0.3293 0.2780 0.1357  -0.0298 0.0051  165 ILE   B C   
1455 O  O   . ILE   B 156 ? 0.4649 0.3409 0.2941 0.1350  -0.0358 0.0037  165 ILE   B O   
1456 C  CB  . ILE   B 156 ? 0.4881 0.3585 0.2978 0.1653  -0.0434 0.0007  165 ILE   B CB  
1457 C  CG1 . ILE   B 156 ? 0.5227 0.3978 0.3186 0.1846  -0.0440 0.0017  165 ILE   B CG1 
1458 C  CG2 . ILE   B 156 ? 0.4879 0.3443 0.3062 0.1583  -0.0488 -0.0045 165 ILE   B CG2 
1459 C  CD1 . ILE   B 156 ? 0.5603 0.4163 0.3405 0.2004  -0.0583 -0.0048 165 ILE   B CD1 
1460 N  N   . THR   B 157 ? 0.4247 0.3172 0.2718 0.1232  -0.0219 0.0065  166 THR   B N   
1461 C  CA  . THR   B 157 ? 0.4108 0.3032 0.2670 0.1093  -0.0199 0.0062  166 THR   B CA  
1462 C  C   . THR   B 157 ? 0.4101 0.2902 0.2731 0.1027  -0.0243 0.0026  166 THR   B C   
1463 O  O   . THR   B 157 ? 0.4164 0.2965 0.2860 0.1009  -0.0226 0.0008  166 THR   B O   
1464 C  CB  . THR   B 157 ? 0.3944 0.3010 0.2599 0.0998  -0.0102 0.0090  166 THR   B CB  
1465 O  OG1 . THR   B 157 ? 0.3962 0.3168 0.2581 0.1039  -0.0066 0.0124  166 THR   B OG1 
1466 C  CG2 . THR   B 157 ? 0.3892 0.2954 0.2621 0.0877  -0.0085 0.0081  166 THR   B CG2 
1467 N  N   . GLN   B 158 ? 0.4056 0.2757 0.2671 0.0992  -0.0299 0.0018  167 GLN   B N   
1468 C  CA  . GLN   B 158 ? 0.4082 0.2692 0.2787 0.0915  -0.0338 -0.0009 167 GLN   B CA  
1469 C  C   . GLN   B 158 ? 0.4174 0.2807 0.2949 0.0787  -0.0295 0.0019  167 GLN   B C   
1470 O  O   . GLN   B 158 ? 0.4086 0.2716 0.2789 0.0786  -0.0285 0.0047  167 GLN   B O   
1471 C  CB  . GLN   B 158 ? 0.4374 0.2812 0.3004 0.0981  -0.0457 -0.0039 167 GLN   B CB  
1472 C  CG  . GLN   B 158 ? 0.4749 0.3103 0.3496 0.0898  -0.0512 -0.0069 167 GLN   B CG  
1473 C  CD  . GLN   B 158 ? 0.4705 0.3140 0.3565 0.0890  -0.0491 -0.0104 167 GLN   B CD  
1474 O  OE1 . GLN   B 158 ? 0.4148 0.2710 0.3087 0.0831  -0.0399 -0.0088 167 GLN   B OE1 
1475 N  NE2 . GLN   B 158 ? 0.4671 0.3023 0.3526 0.0961  -0.0584 -0.0160 167 GLN   B NE2 
1476 N  N   . GLY   B 159 ? 0.4530 0.3191 0.3433 0.0697  -0.0271 0.0009  168 GLY   B N   
1477 C  CA  . GLY   B 159 ? 0.4962 0.3658 0.3927 0.0588  -0.0223 0.0039  168 GLY   B CA  
1478 C  C   . GLY   B 159 ? 0.5696 0.4265 0.4675 0.0538  -0.0284 0.0053  168 GLY   B C   
1479 O  O   . GLY   B 159 ? 0.5899 0.4330 0.4815 0.0592  -0.0375 0.0034  168 GLY   B O   
1480 N  N   . LYS   B 160 ? 0.6020 0.4626 0.5070 0.0435  -0.0234 0.0089  169 LYS   B N   
1481 C  CA  . LYS   B 160 ? 0.6339 0.4832 0.5423 0.0359  -0.0276 0.0119  169 LYS   B CA  
1482 C  C   . LYS   B 160 ? 0.6469 0.5067 0.5743 0.0268  -0.0249 0.0112  169 LYS   B C   
1483 O  O   . LYS   B 160 ? 0.6397 0.5155 0.5738 0.0244  -0.0165 0.0114  169 LYS   B O   
1484 C  CB  . LYS   B 160 ? 0.6785 0.5245 0.5783 0.0320  -0.0228 0.0186  169 LYS   B CB  
1485 C  CG  . LYS   B 160 ? 0.7672 0.6038 0.6724 0.0213  -0.0236 0.0241  169 LYS   B CG  
1486 C  CD  . LYS   B 160 ? 0.8576 0.6900 0.7514 0.0191  -0.0181 0.0313  169 LYS   B CD  
1487 C  CE  . LYS   B 160 ? 0.9347 0.7524 0.8310 0.0090  -0.0201 0.0380  169 LYS   B CE  
1488 N  NZ  . LYS   B 160 ? 0.9878 0.8016 0.8722 0.0071  -0.0134 0.0462  169 LYS   B NZ  
1489 N  N   . ARG   B 161 ? 0.6639 0.5155 0.6002 0.0224  -0.0327 0.0098  170 ARG   B N   
1490 C  CA  . ARG   B 161 ? 0.6848 0.5489 0.6412 0.0132  -0.0307 0.0092  170 ARG   B CA  
1491 C  C   . ARG   B 161 ? 0.7171 0.5797 0.6791 0.0005  -0.0265 0.0175  170 ARG   B C   
1492 O  O   . ARG   B 161 ? 0.7284 0.5730 0.6875 -0.0038 -0.0336 0.0202  170 ARG   B O   
1493 C  CB  . ARG   B 161 ? 0.7004 0.5588 0.6657 0.0149  -0.0421 0.0024  170 ARG   B CB  
1494 C  CG  . ARG   B 161 ? 0.7130 0.5901 0.6998 0.0087  -0.0400 -0.0003 170 ARG   B CG  
1495 C  CD  . ARG   B 161 ? 0.7352 0.6066 0.7335 0.0077  -0.0526 -0.0067 170 ARG   B CD  
1496 N  NE  . ARG   B 161 ? 0.7409 0.6330 0.7626 -0.0006 -0.0502 -0.0081 170 ARG   B NE  
1497 C  CZ  . ARG   B 161 ? 0.7377 0.6431 0.7677 0.0059  -0.0523 -0.0157 170 ARG   B CZ  
1498 N  NH1 . ARG   B 161 ? 0.7174 0.6158 0.7339 0.0203  -0.0566 -0.0221 170 ARG   B NH1 
1499 N  NH2 . ARG   B 161 ? 0.7251 0.6515 0.7768 -0.0014 -0.0500 -0.0168 170 ARG   B NH2 
1500 N  N   . GLU   B 162 ? 0.7298 0.6095 0.6974 -0.0043 -0.0150 0.0220  171 GLU   B N   
1501 C  CA  . GLU   B 162 ? 0.7580 0.6395 0.7302 -0.0154 -0.0087 0.0313  171 GLU   B CA  
1502 C  C   . GLU   B 162 ? 0.7674 0.6515 0.7605 -0.0273 -0.0126 0.0327  171 GLU   B C   
1503 O  O   . GLU   B 162 ? 0.7800 0.6567 0.7761 -0.0379 -0.0112 0.0410  171 GLU   B O   
1504 C  CB  . GLU   B 162 ? 0.7979 0.7003 0.7718 -0.0155 0.0042  0.0343  171 GLU   B CB  
1505 C  CG  . GLU   B 162 ? 0.8980 0.7996 0.8538 -0.0056 0.0079  0.0328  171 GLU   B CG  
1506 C  CD  . GLU   B 162 ? 1.0240 0.9128 0.9633 -0.0054 0.0098  0.0396  171 GLU   B CD  
1507 O  OE1 . GLU   B 162 ? 1.0545 0.9452 0.9957 -0.0127 0.0160  0.0478  171 GLU   B OE1 
1508 O  OE2 . GLU   B 162 ? 1.0656 0.9430 0.9895 0.0027  0.0054  0.0371  171 GLU   B OE2 
1509 S  S   . DMS   C .   ? 0.9344 0.8106 0.8187 0.0307  0.0083  -0.0410 201 DMS   B S   
1510 O  O   . DMS   C .   ? 0.9268 0.8174 0.8143 0.0354  0.0129  -0.0371 201 DMS   B O   
1511 C  C1  . DMS   C .   ? 0.9457 0.8007 0.8209 0.0358  0.0071  -0.0441 201 DMS   B C1  
1512 C  C2  . DMS   C .   ? 0.9290 0.8020 0.8219 0.0213  0.0096  -0.0339 201 DMS   B C2  
1513 S  S   . DMS   D .   ? 0.8720 0.9270 0.7963 0.0686  0.0431  0.0472  202 DMS   B S   
1514 O  O   . DMS   D .   ? 0.8753 0.9053 0.7865 0.0765  0.0415  0.0463  202 DMS   B O   
1515 C  C1  . DMS   D .   ? 0.8701 0.9229 0.8114 0.0470  0.0462  0.0470  202 DMS   B C1  
1516 C  C2  . DMS   D .   ? 0.8595 0.9430 0.7898 0.0731  0.0520  0.0581  202 DMS   B C2  
1517 N  N1  . A1B9N E .   ? 0.5821 0.5686 0.4961 0.0580  0.0441  0.0435  203 A1B9N B N1  
1518 N  N3  . A1B9N E .   ? 0.6467 0.5985 0.5916 -0.0004 0.0380  0.0260  203 A1B9N B N3  
1519 C  C4  . A1B9N E .   ? 0.5654 0.5369 0.4585 0.0804  0.0501  0.0532  203 A1B9N B C4  
1520 C  C5  . A1B9N E .   ? 0.5618 0.5534 0.4672 0.0708  0.0545  0.0576  203 A1B9N B C5  
1521 C  C6  . A1B9N E .   ? 0.5672 0.5625 0.4846 0.0565  0.0514  0.0521  203 A1B9N B C6  
1522 C  C7  . A1B9N E .   ? 0.5918 0.5797 0.5132 0.0479  0.0402  0.0373  203 A1B9N B C7  
1523 C  C8  . A1B9N E .   ? 0.5926 0.5851 0.5112 0.0522  0.0345  0.0320  203 A1B9N B C8  
1524 C  C10 . A1B9N E .   ? 0.6015 0.5936 0.5345 0.0314  0.0327  0.0252  203 A1B9N B C10 
1525 C  C13 . A1B9N E .   ? 0.5978 0.5815 0.5280 0.0343  0.0419  0.0366  203 A1B9N B C13 
1526 O  O   . A1B9N E .   ? 0.5569 0.5625 0.4865 0.0442  0.0553  0.0555  203 A1B9N B O   
1527 C  C3  . A1B9N E .   ? 0.5605 0.5280 0.4417 0.0945  0.0523  0.0576  203 A1B9N B C3  
1528 CL CL  . A1B9N E .   ? 0.5603 0.5037 0.4281 0.1059  0.0457  0.0510  203 A1B9N B CL  
1529 C  C2  . A1B9N E .   ? 0.5551 0.5385 0.4351 0.1000  0.0597  0.0672  203 A1B9N B C2  
1530 C  C14 . A1B9N E .   ? 0.5477 0.5569 0.4544 0.0747  0.0619  0.0672  203 A1B9N B C14 
1531 C  C1  . A1B9N E .   ? 0.5515 0.5570 0.4450 0.0896  0.0651  0.0725  203 A1B9N B C1  
1532 C  C   . A1B9N E .   ? 0.5556 0.5829 0.4500 0.0951  0.0742  0.0839  203 A1B9N B C   
1533 N  N   . A1B9N E .   ? 0.5630 0.5802 0.4555 0.0913  0.0829  0.0931  203 A1B9N B N   
1534 C  C11 . A1B9N E .   ? 0.6090 0.5944 0.5450 0.0262  0.0376  0.0300  203 A1B9N B C11 
1535 C  C9  . A1B9N E .   ? 0.5974 0.5921 0.5217 0.0439  0.0313  0.0266  203 A1B9N B C9  
1536 C  C12 . A1B9N E .   ? 0.6267 0.6028 0.5692 0.0135  0.0375  0.0276  203 A1B9N B C12 
1537 N  N5  . A1B9N E .   ? 0.6308 0.6089 0.5779 0.0069  0.0330  0.0209  203 A1B9N B N5  
1538 N  N4  . A1B9N E .   ? 0.6396 0.6026 0.5882 -0.0014 0.0333  0.0199  203 A1B9N B N4  
1539 N  N2  . A1B9N E .   ? 0.6391 0.6001 0.5803 0.0094  0.0411  0.0311  203 A1B9N B N2  
1540 S  S   . SO4   F .   ? 2.0587 2.0606 1.9070 0.1280  0.1140  0.1315  204 SO4   B S   
1541 O  O1  . SO4   F .   ? 2.0685 2.0436 1.9156 0.1162  0.1169  0.1340  204 SO4   B O1  
1542 O  O2  . SO4   F .   ? 2.0689 2.0612 1.8955 0.1527  0.1076  0.1259  204 SO4   B O2  
1543 O  O3  . SO4   F .   ? 2.0471 2.0780 1.9025 0.1272  0.1265  0.1462  204 SO4   B O3  
1544 O  O4  . SO4   F .   ? 2.0502 2.0601 1.9137 0.1165  0.1051  0.1205  204 SO4   B O4  
1545 S  S   . DMS   G .   ? 1.0267 0.9929 0.9342 0.0455  0.0954  0.1043  205 DMS   B S   
1546 O  O   . DMS   G .   ? 1.0121 1.0047 0.9339 0.0411  0.0909  0.0989  205 DMS   B O   
1547 C  C1  . DMS   G .   ? 1.0319 0.9715 0.9453 0.0253  0.0941  0.1024  205 DMS   B C1  
1548 C  C2  . DMS   G .   ? 1.0215 1.0018 0.9314 0.0436  0.1104  0.1236  205 DMS   B C2  
# 
