data_7IA3
# 
_entry.id   7IA3 
# 
_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   7IA3         pdb_00007ia3 10.2210/pdb7ia3/pdb 
WWPDB D_1001408506 ?            ?                   
# 
_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                        7IA3 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                               5067.486  1  ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                        18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                         78.133    1  ?                           ?    ? ? 
4 non-polymer syn '3-chloro-4-cyano-N-(2,3-dihydro-1H-isoindol-5-yl)benzamide' 297.739   1  ?                           ?    ? ? 
5 water       nat water                                                        18.015    93 ?                           ?    ? ? 
# 
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-chloro-4-cyano-N-(2,3-dihydro-1H-isoindol-5-yl)benzamide' A1B8I 
5 water                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B8I non-polymer         . '3-chloro-4-cyano-N-(2,3-dihydro-1H-isoindol-5-yl)benzamide' ? 'C16 H12 Cl N3 O' 297.739 
ALA   'L-peptide linking' y ALANINE                                                      ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                     ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                   ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                              ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                     ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                         ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                    ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                              ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                      ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                    ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                        ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                   ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                      ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                       ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                   ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                      ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                       ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                    ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                   ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                     ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                       ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 171 ?   ?   ?   B A n 
B 2 164 GLU 164 171 ?   ?   ?   B B n 
B 2 165 THR 165 171 ?   ?   ?   B C n 
B 2 166 PRO 166 171 ?   ?   ?   B D n 
B 2 167 VAL 167 172 172 VAL VAL B . n 
B 2 168 GLU 168 173 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B8I 1  202 203 A1B8I LIG B . 
E 5 HOH   1  101 126 HOH   HOH A . 
E 5 HOH   2  102 20  HOH   HOH A . 
E 5 HOH   3  103 118 HOH   HOH A . 
E 5 HOH   4  104 127 HOH   HOH A . 
E 5 HOH   5  105 98  HOH   HOH A . 
E 5 HOH   6  106 34  HOH   HOH A . 
E 5 HOH   7  107 49  HOH   HOH A . 
E 5 HOH   8  108 65  HOH   HOH A . 
E 5 HOH   9  109 28  HOH   HOH A . 
E 5 HOH   10 110 83  HOH   HOH A . 
E 5 HOH   11 111 128 HOH   HOH A . 
E 5 HOH   12 112 105 HOH   HOH A . 
E 5 HOH   13 113 16  HOH   HOH A . 
E 5 HOH   14 114 134 HOH   HOH A . 
E 5 HOH   15 115 29  HOH   HOH A . 
E 5 HOH   16 116 110 HOH   HOH A . 
E 5 HOH   17 117 50  HOH   HOH A . 
E 5 HOH   18 118 120 HOH   HOH A . 
E 5 HOH   19 119 121 HOH   HOH A . 
E 5 HOH   20 120 119 HOH   HOH A . 
E 5 HOH   21 121 70  HOH   HOH A . 
E 5 HOH   22 122 60  HOH   HOH A . 
E 5 HOH   23 123 40  HOH   HOH A . 
E 5 HOH   24 124 27  HOH   HOH A . 
F 5 HOH   1  301 92  HOH   HOH B . 
F 5 HOH   2  302 11  HOH   HOH B . 
F 5 HOH   3  303 90  HOH   HOH B . 
F 5 HOH   4  304 51  HOH   HOH B . 
F 5 HOH   5  305 63  HOH   HOH B . 
F 5 HOH   6  306 14  HOH   HOH B . 
F 5 HOH   7  307 132 HOH   HOH B . 
F 5 HOH   8  308 5   HOH   HOH B . 
F 5 HOH   9  309 31  HOH   HOH B . 
F 5 HOH   10 310 46  HOH   HOH B . 
F 5 HOH   11 311 69  HOH   HOH B . 
F 5 HOH   12 312 68  HOH   HOH B . 
F 5 HOH   13 313 48  HOH   HOH B . 
F 5 HOH   14 314 130 HOH   HOH B . 
F 5 HOH   15 315 1   HOH   HOH B . 
F 5 HOH   16 316 100 HOH   HOH B . 
F 5 HOH   17 317 4   HOH   HOH B . 
F 5 HOH   18 318 133 HOH   HOH B . 
F 5 HOH   19 319 123 HOH   HOH B . 
F 5 HOH   20 320 36  HOH   HOH B . 
F 5 HOH   21 321 32  HOH   HOH B . 
F 5 HOH   22 322 39  HOH   HOH B . 
F 5 HOH   23 323 106 HOH   HOH B . 
F 5 HOH   24 324 117 HOH   HOH B . 
F 5 HOH   25 325 24  HOH   HOH B . 
F 5 HOH   26 326 10  HOH   HOH B . 
F 5 HOH   27 327 108 HOH   HOH B . 
F 5 HOH   28 328 129 HOH   HOH B . 
F 5 HOH   29 329 13  HOH   HOH B . 
F 5 HOH   30 330 66  HOH   HOH B . 
F 5 HOH   31 331 112 HOH   HOH B . 
F 5 HOH   32 332 67  HOH   HOH B . 
F 5 HOH   33 333 81  HOH   HOH B . 
F 5 HOH   34 334 2   HOH   HOH B . 
F 5 HOH   35 335 107 HOH   HOH B . 
F 5 HOH   36 336 58  HOH   HOH B . 
F 5 HOH   37 337 9   HOH   HOH B . 
F 5 HOH   38 338 56  HOH   HOH B . 
F 5 HOH   39 339 21  HOH   HOH B . 
F 5 HOH   40 340 94  HOH   HOH B . 
F 5 HOH   41 341 61  HOH   HOH B . 
F 5 HOH   42 342 54  HOH   HOH B . 
F 5 HOH   43 343 131 HOH   HOH B . 
F 5 HOH   44 344 30  HOH   HOH B . 
F 5 HOH   45 345 80  HOH   HOH B . 
F 5 HOH   46 346 12  HOH   HOH B . 
F 5 HOH   47 347 3   HOH   HOH B . 
F 5 HOH   48 348 62  HOH   HOH B . 
F 5 HOH   49 349 116 HOH   HOH B . 
F 5 HOH   50 350 82  HOH   HOH B . 
F 5 HOH   51 351 35  HOH   HOH B . 
F 5 HOH   52 352 73  HOH   HOH B . 
F 5 HOH   53 353 42  HOH   HOH B . 
F 5 HOH   54 354 102 HOH   HOH B . 
F 5 HOH   55 355 17  HOH   HOH B . 
F 5 HOH   56 356 43  HOH   HOH B . 
F 5 HOH   57 357 23  HOH   HOH B . 
F 5 HOH   58 358 125 HOH   HOH B . 
F 5 HOH   59 359 135 HOH   HOH B . 
F 5 HOH   60 360 115 HOH   HOH B . 
F 5 HOH   61 361 18  HOH   HOH B . 
F 5 HOH   62 362 64  HOH   HOH B . 
F 5 HOH   63 363 26  HOH   HOH B . 
F 5 HOH   64 364 87  HOH   HOH B . 
F 5 HOH   65 365 79  HOH   HOH B . 
F 5 HOH   66 366 59  HOH   HOH B . 
F 5 HOH   67 367 57  HOH   HOH B . 
F 5 HOH   68 368 44  HOH   HOH B . 
F 5 HOH   69 369 124 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           7IA3 
_cell.length_a           42.685 
_cell.length_b           42.685 
_cell.length_c           216.597 
_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                         7IA3 
_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          7IA3 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.090 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   42.19 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IA3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             108.300 
_reflns.d_resolution_high            2.120 
_reflns.number_obs                   12330 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.363 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.200 
_reflns.B_iso_Wilson_estimate        38.730 
_reflns.pdbx_redundancy              24.900 
_reflns.pdbx_Rrim_I_all              0.371 
_reflns.pdbx_Rpim_I_all              0.074 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     306921 
_reflns.pdbx_scaling_rejects         405 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 2.120 2.240   ? 45559 ? ? 4.199 ? ? ? 26.100 ? 0.800  ? 1744 ? ? ? ? 100.000 4.282 0.832 0.760 ? 
1 2 6.710 108.300 ? 9170  ? ? 0.108 ? ? ? 18.500 ? 21.000 ? 497  ? ? ? ? 99.600  0.111 0.025 0.996 ? 
# 
_refine.entry_id                                 7IA3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.1210 
_refine.ls_d_res_low                             41.8800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.9000 
_refine.ls_number_reflns_obs                     12246 
_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                          0.2356 
_refine.ls_R_factor_R_work                       0.2333 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2789 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               48.0900 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -5.4996 
_refine.aniso_B[2][2]                            -5.4996 
_refine.aniso_B[3][3]                            10.9992 
_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               0.9320 
_refine.correlation_coeff_Fo_to_Fc_free          0.8880 
_refine.overall_SU_R_Cruickshank_DPI             0.2630 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2150 
_refine.pdbx_overall_SU_R_Blow_DPI               0.2990 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2250 
_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                                99.480 
_refine.B_iso_min                                23.630 
_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                        7IA3 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.360 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.1210 
_refine_hist.d_res_low                        41.8800 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             93 
_refine_hist.number_atoms_total               1601 
_refine_hist.pdbx_number_residues_total       196 
_refine_hist.pdbx_B_iso_mean_ligand           46.24 
_refine_hist.pdbx_B_iso_mean_solvent          46.15 
_refine_hist.pdbx_number_atoms_protein        1483 
_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        537  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              270  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1572 ?      ? 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      1229 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1572 0.008  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2140 0.930  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.150  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    16.550 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.1200 
_refine_ls_shell.d_res_low                        2.1500 
_refine_ls_shell.pdbx_total_number_of_bins_used   30 
_refine_ls_shell.percent_reflns_obs               98.3600 
_refine_ls_shell.number_reflns_R_work             401 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3561 
_refine_ls_shell.R_factor_R_free                  0.4295 
_refine_ls_shell.percent_reflns_R_free            5.2000 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                423 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IA3 
_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-0029909-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IA3 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7IA3 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IA3 B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 173 
# 
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 7IA3 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IA3 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IA3 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IA3 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4210 ? 
1 MORE         -27  ? 
1 'SSA (A^2)'  9890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N 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 LYS B 98  ? O LYS B 107 N ALA B 90  ? N ALA B 99  
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                   7IA3 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30 ? ? -82.03 -159.73 
2 1 CYS B 80 ? ? 76.64  -13.51  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     368 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.8834 -1.4220 -19.4674 0.0423 -0.0778 -0.2878 0.1997 0.1022 0.0982 4.7771 4.3544 4.8221 -2.4918 
0.6021 0.9760  0.5372 -0.4420 -0.0952 0.5059 0.1653 -0.3089 -0.5969 -0.0265 0.4814 
'X-RAY DIFFRACTION' 2 ? refined -18.7353 0.9988  -15.5634 0.1000 0.0361  -0.1165 0.1851 0.0191 0.0245 1.7897 1.3879 2.4236 -1.3339 
1.0474 -0.3607 0.4217 -0.3968 -0.0249 0.2136 0.1016 0.0741  -0.1034 0.1491  0.2521 
# 
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 172 '{ 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 171 A B GLU 163 
15 1 Y 1 B GLU 171 B B GLU 164 
16 1 Y 1 B THR 171 C B THR 165 
17 1 Y 1 B PRO 171 D B PRO 166 
18 1 Y 1 B GLU 173 ? 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 
A1B8I N1   N  N N 1   
A1B8I N3   N  N N 2   
A1B8I C4   C  Y N 3   
A1B8I C5   C  Y N 4   
A1B8I C6   C  N N 5   
A1B8I C7   C  Y N 6   
A1B8I C8   C  Y N 7   
A1B8I C10  C  Y N 8   
A1B8I C13  C  N N 9   
A1B8I C15  C  Y N 10  
A1B8I C1   C  N N 11  
A1B8I C2   C  Y N 12  
A1B8I C3   C  Y N 13  
A1B8I O1   O  N N 14  
A1B8I N2   N  N N 15  
A1B8I C9   C  Y N 16  
A1B8I C11  C  Y N 17  
A1B8I C12  C  Y N 18  
A1B8I C14  C  N N 19  
A1B8I C16  C  Y N 20  
A1B8I CL1  CL N N 21  
A1B8I H9   H  N N 22  
A1B8I H2   H  N N 23  
A1B8I H4   H  N N 24  
A1B8I H7   H  N N 25  
A1B8I H8   H  N N 26  
A1B8I H12  H  N N 27  
A1B8I H1   H  N N 28  
A1B8I H3   H  N N 29  
A1B8I H5   H  N N 30  
A1B8I H6   H  N N 31  
A1B8I H10  H  N N 32  
A1B8I H11  H  N N 33  
ALA   N    N  N N 34  
ALA   CA   C  N S 35  
ALA   C    C  N N 36  
ALA   O    O  N N 37  
ALA   CB   C  N N 38  
ALA   OXT  O  N N 39  
ALA   H    H  N N 40  
ALA   H2   H  N N 41  
ALA   HA   H  N N 42  
ALA   HB1  H  N N 43  
ALA   HB2  H  N N 44  
ALA   HB3  H  N N 45  
ALA   HXT  H  N N 46  
ARG   N    N  N N 47  
ARG   CA   C  N S 48  
ARG   C    C  N N 49  
ARG   O    O  N N 50  
ARG   CB   C  N N 51  
ARG   CG   C  N N 52  
ARG   CD   C  N N 53  
ARG   NE   N  N N 54  
ARG   CZ   C  N N 55  
ARG   NH1  N  N N 56  
ARG   NH2  N  N N 57  
ARG   OXT  O  N N 58  
ARG   H    H  N N 59  
ARG   H2   H  N N 60  
ARG   HA   H  N N 61  
ARG   HB2  H  N N 62  
ARG   HB3  H  N N 63  
ARG   HG2  H  N N 64  
ARG   HG3  H  N N 65  
ARG   HD2  H  N N 66  
ARG   HD3  H  N N 67  
ARG   HE   H  N N 68  
ARG   HH11 H  N N 69  
ARG   HH12 H  N N 70  
ARG   HH21 H  N N 71  
ARG   HH22 H  N N 72  
ARG   HXT  H  N N 73  
ASN   N    N  N N 74  
ASN   CA   C  N S 75  
ASN   C    C  N N 76  
ASN   O    O  N N 77  
ASN   CB   C  N N 78  
ASN   CG   C  N N 79  
ASN   OD1  O  N N 80  
ASN   ND2  N  N N 81  
ASN   OXT  O  N N 82  
ASN   H    H  N N 83  
ASN   H2   H  N N 84  
ASN   HA   H  N N 85  
ASN   HB2  H  N N 86  
ASN   HB3  H  N N 87  
ASN   HD21 H  N N 88  
ASN   HD22 H  N N 89  
ASN   HXT  H  N N 90  
ASP   N    N  N N 91  
ASP   CA   C  N S 92  
ASP   C    C  N N 93  
ASP   O    O  N N 94  
ASP   CB   C  N N 95  
ASP   CG   C  N N 96  
ASP   OD1  O  N N 97  
ASP   OD2  O  N N 98  
ASP   OXT  O  N N 99  
ASP   H    H  N N 100 
ASP   H2   H  N N 101 
ASP   HA   H  N N 102 
ASP   HB2  H  N N 103 
ASP   HB3  H  N N 104 
ASP   HD2  H  N N 105 
ASP   HXT  H  N N 106 
CYS   N    N  N N 107 
CYS   CA   C  N R 108 
CYS   C    C  N N 109 
CYS   O    O  N N 110 
CYS   CB   C  N N 111 
CYS   SG   S  N N 112 
CYS   OXT  O  N N 113 
CYS   H    H  N N 114 
CYS   H2   H  N N 115 
CYS   HA   H  N N 116 
CYS   HB2  H  N N 117 
CYS   HB3  H  N N 118 
CYS   HG   H  N N 119 
CYS   HXT  H  N N 120 
DMS   S    S  N N 121 
DMS   O    O  N N 122 
DMS   C1   C  N N 123 
DMS   C2   C  N N 124 
DMS   H11  H  N N 125 
DMS   H12  H  N N 126 
DMS   H13  H  N N 127 
DMS   H21  H  N N 128 
DMS   H22  H  N N 129 
DMS   H23  H  N N 130 
GLN   N    N  N N 131 
GLN   CA   C  N S 132 
GLN   C    C  N N 133 
GLN   O    O  N N 134 
GLN   CB   C  N N 135 
GLN   CG   C  N N 136 
GLN   CD   C  N N 137 
GLN   OE1  O  N N 138 
GLN   NE2  N  N N 139 
GLN   OXT  O  N N 140 
GLN   H    H  N N 141 
GLN   H2   H  N N 142 
GLN   HA   H  N N 143 
GLN   HB2  H  N N 144 
GLN   HB3  H  N N 145 
GLN   HG2  H  N N 146 
GLN   HG3  H  N N 147 
GLN   HE21 H  N N 148 
GLN   HE22 H  N N 149 
GLN   HXT  H  N N 150 
GLU   N    N  N N 151 
GLU   CA   C  N S 152 
GLU   C    C  N N 153 
GLU   O    O  N N 154 
GLU   CB   C  N N 155 
GLU   CG   C  N N 156 
GLU   CD   C  N N 157 
GLU   OE1  O  N N 158 
GLU   OE2  O  N N 159 
GLU   OXT  O  N N 160 
GLU   H    H  N N 161 
GLU   H2   H  N N 162 
GLU   HA   H  N N 163 
GLU   HB2  H  N N 164 
GLU   HB3  H  N N 165 
GLU   HG2  H  N N 166 
GLU   HG3  H  N N 167 
GLU   HE2  H  N N 168 
GLU   HXT  H  N N 169 
GLY   N    N  N N 170 
GLY   CA   C  N N 171 
GLY   C    C  N N 172 
GLY   O    O  N N 173 
GLY   OXT  O  N N 174 
GLY   H    H  N N 175 
GLY   H2   H  N N 176 
GLY   HA2  H  N N 177 
GLY   HA3  H  N N 178 
GLY   HXT  H  N N 179 
HIS   N    N  N N 180 
HIS   CA   C  N S 181 
HIS   C    C  N N 182 
HIS   O    O  N N 183 
HIS   CB   C  N N 184 
HIS   CG   C  Y N 185 
HIS   ND1  N  Y N 186 
HIS   CD2  C  Y N 187 
HIS   CE1  C  Y N 188 
HIS   NE2  N  Y N 189 
HIS   OXT  O  N N 190 
HIS   H    H  N N 191 
HIS   H2   H  N N 192 
HIS   HA   H  N N 193 
HIS   HB2  H  N N 194 
HIS   HB3  H  N N 195 
HIS   HD1  H  N N 196 
HIS   HD2  H  N N 197 
HIS   HE1  H  N N 198 
HIS   HE2  H  N N 199 
HIS   HXT  H  N N 200 
HOH   O    O  N N 201 
HOH   H1   H  N N 202 
HOH   H2   H  N N 203 
ILE   N    N  N N 204 
ILE   CA   C  N S 205 
ILE   C    C  N N 206 
ILE   O    O  N N 207 
ILE   CB   C  N S 208 
ILE   CG1  C  N N 209 
ILE   CG2  C  N N 210 
ILE   CD1  C  N N 211 
ILE   OXT  O  N N 212 
ILE   H    H  N N 213 
ILE   H2   H  N N 214 
ILE   HA   H  N N 215 
ILE   HB   H  N N 216 
ILE   HG12 H  N N 217 
ILE   HG13 H  N N 218 
ILE   HG21 H  N N 219 
ILE   HG22 H  N N 220 
ILE   HG23 H  N N 221 
ILE   HD11 H  N N 222 
ILE   HD12 H  N N 223 
ILE   HD13 H  N N 224 
ILE   HXT  H  N N 225 
LEU   N    N  N N 226 
LEU   CA   C  N S 227 
LEU   C    C  N N 228 
LEU   O    O  N N 229 
LEU   CB   C  N N 230 
LEU   CG   C  N N 231 
LEU   CD1  C  N N 232 
LEU   CD2  C  N N 233 
LEU   OXT  O  N N 234 
LEU   H    H  N N 235 
LEU   H2   H  N N 236 
LEU   HA   H  N N 237 
LEU   HB2  H  N N 238 
LEU   HB3  H  N N 239 
LEU   HG   H  N N 240 
LEU   HD11 H  N N 241 
LEU   HD12 H  N N 242 
LEU   HD13 H  N N 243 
LEU   HD21 H  N N 244 
LEU   HD22 H  N N 245 
LEU   HD23 H  N N 246 
LEU   HXT  H  N N 247 
LYS   N    N  N N 248 
LYS   CA   C  N S 249 
LYS   C    C  N N 250 
LYS   O    O  N N 251 
LYS   CB   C  N N 252 
LYS   CG   C  N N 253 
LYS   CD   C  N N 254 
LYS   CE   C  N N 255 
LYS   NZ   N  N N 256 
LYS   OXT  O  N N 257 
LYS   H    H  N N 258 
LYS   H2   H  N N 259 
LYS   HA   H  N N 260 
LYS   HB2  H  N N 261 
LYS   HB3  H  N N 262 
LYS   HG2  H  N N 263 
LYS   HG3  H  N N 264 
LYS   HD2  H  N N 265 
LYS   HD3  H  N N 266 
LYS   HE2  H  N N 267 
LYS   HE3  H  N N 268 
LYS   HZ1  H  N N 269 
LYS   HZ2  H  N N 270 
LYS   HZ3  H  N N 271 
LYS   HXT  H  N N 272 
MET   N    N  N N 273 
MET   CA   C  N S 274 
MET   C    C  N N 275 
MET   O    O  N N 276 
MET   CB   C  N N 277 
MET   CG   C  N N 278 
MET   SD   S  N N 279 
MET   CE   C  N N 280 
MET   OXT  O  N N 281 
MET   H    H  N N 282 
MET   H2   H  N N 283 
MET   HA   H  N N 284 
MET   HB2  H  N N 285 
MET   HB3  H  N N 286 
MET   HG2  H  N N 287 
MET   HG3  H  N N 288 
MET   HE1  H  N N 289 
MET   HE2  H  N N 290 
MET   HE3  H  N N 291 
MET   HXT  H  N N 292 
PHE   N    N  N N 293 
PHE   CA   C  N S 294 
PHE   C    C  N N 295 
PHE   O    O  N N 296 
PHE   CB   C  N N 297 
PHE   CG   C  Y N 298 
PHE   CD1  C  Y N 299 
PHE   CD2  C  Y N 300 
PHE   CE1  C  Y N 301 
PHE   CE2  C  Y N 302 
PHE   CZ   C  Y N 303 
PHE   OXT  O  N N 304 
PHE   H    H  N N 305 
PHE   H2   H  N N 306 
PHE   HA   H  N N 307 
PHE   HB2  H  N N 308 
PHE   HB3  H  N N 309 
PHE   HD1  H  N N 310 
PHE   HD2  H  N N 311 
PHE   HE1  H  N N 312 
PHE   HE2  H  N N 313 
PHE   HZ   H  N N 314 
PHE   HXT  H  N N 315 
PRO   N    N  N N 316 
PRO   CA   C  N S 317 
PRO   C    C  N N 318 
PRO   O    O  N N 319 
PRO   CB   C  N N 320 
PRO   CG   C  N N 321 
PRO   CD   C  N N 322 
PRO   OXT  O  N N 323 
PRO   H    H  N N 324 
PRO   HA   H  N N 325 
PRO   HB2  H  N N 326 
PRO   HB3  H  N N 327 
PRO   HG2  H  N N 328 
PRO   HG3  H  N N 329 
PRO   HD2  H  N N 330 
PRO   HD3  H  N N 331 
PRO   HXT  H  N N 332 
SER   N    N  N N 333 
SER   CA   C  N S 334 
SER   C    C  N N 335 
SER   O    O  N N 336 
SER   CB   C  N N 337 
SER   OG   O  N N 338 
SER   OXT  O  N N 339 
SER   H    H  N N 340 
SER   H2   H  N N 341 
SER   HA   H  N N 342 
SER   HB2  H  N N 343 
SER   HB3  H  N N 344 
SER   HG   H  N N 345 
SER   HXT  H  N N 346 
THR   N    N  N N 347 
THR   CA   C  N S 348 
THR   C    C  N N 349 
THR   O    O  N N 350 
THR   CB   C  N R 351 
THR   OG1  O  N N 352 
THR   CG2  C  N N 353 
THR   OXT  O  N N 354 
THR   H    H  N N 355 
THR   H2   H  N N 356 
THR   HA   H  N N 357 
THR   HB   H  N N 358 
THR   HG1  H  N N 359 
THR   HG21 H  N N 360 
THR   HG22 H  N N 361 
THR   HG23 H  N N 362 
THR   HXT  H  N N 363 
TRP   N    N  N N 364 
TRP   CA   C  N S 365 
TRP   C    C  N N 366 
TRP   O    O  N N 367 
TRP   CB   C  N N 368 
TRP   CG   C  Y N 369 
TRP   CD1  C  Y N 370 
TRP   CD2  C  Y N 371 
TRP   NE1  N  Y N 372 
TRP   CE2  C  Y N 373 
TRP   CE3  C  Y N 374 
TRP   CZ2  C  Y N 375 
TRP   CZ3  C  Y N 376 
TRP   CH2  C  Y N 377 
TRP   OXT  O  N N 378 
TRP   H    H  N N 379 
TRP   H2   H  N N 380 
TRP   HA   H  N N 381 
TRP   HB2  H  N N 382 
TRP   HB3  H  N N 383 
TRP   HD1  H  N N 384 
TRP   HE1  H  N N 385 
TRP   HE3  H  N N 386 
TRP   HZ2  H  N N 387 
TRP   HZ3  H  N N 388 
TRP   HH2  H  N N 389 
TRP   HXT  H  N N 390 
TYR   N    N  N N 391 
TYR   CA   C  N S 392 
TYR   C    C  N N 393 
TYR   O    O  N N 394 
TYR   CB   C  N N 395 
TYR   CG   C  Y N 396 
TYR   CD1  C  Y N 397 
TYR   CD2  C  Y N 398 
TYR   CE1  C  Y N 399 
TYR   CE2  C  Y N 400 
TYR   CZ   C  Y N 401 
TYR   OH   O  N N 402 
TYR   OXT  O  N N 403 
TYR   H    H  N N 404 
TYR   H2   H  N N 405 
TYR   HA   H  N N 406 
TYR   HB2  H  N N 407 
TYR   HB3  H  N N 408 
TYR   HD1  H  N N 409 
TYR   HD2  H  N N 410 
TYR   HE1  H  N N 411 
TYR   HE2  H  N N 412 
TYR   HH   H  N N 413 
TYR   HXT  H  N N 414 
VAL   N    N  N N 415 
VAL   CA   C  N S 416 
VAL   C    C  N N 417 
VAL   O    O  N N 418 
VAL   CB   C  N N 419 
VAL   CG1  C  N N 420 
VAL   CG2  C  N N 421 
VAL   OXT  O  N N 422 
VAL   H    H  N N 423 
VAL   H2   H  N N 424 
VAL   HA   H  N N 425 
VAL   HB   H  N N 426 
VAL   HG11 H  N N 427 
VAL   HG12 H  N N 428 
VAL   HG13 H  N N 429 
VAL   HG21 H  N N 430 
VAL   HG22 H  N N 431 
VAL   HG23 H  N N 432 
VAL   HXT  H  N N 433 
# 
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 
A1B8I N1  C1   trip N N 1   
A1B8I C1  C2   sing N N 2   
A1B8I C2  C3   doub Y N 3   
A1B8I C3  C4   sing Y N 4   
A1B8I C4  C5   doub Y N 5   
A1B8I C5  C6   sing N N 6   
A1B8I C6  O1   doub N N 7   
A1B8I C6  N2   sing N N 8   
A1B8I N2  C7   sing N N 9   
A1B8I C7  C8   doub Y N 10  
A1B8I C8  C9   sing Y N 11  
A1B8I C9  C10  doub Y N 12  
A1B8I C10 C11  sing Y N 13  
A1B8I C11 C12  doub Y N 14  
A1B8I C11 C13  sing N N 15  
A1B8I C13 N3   sing N N 16  
A1B8I N3  C14  sing N N 17  
A1B8I C5  C15  sing Y N 18  
A1B8I C15 C16  doub Y N 19  
A1B8I C16 CL1  sing N N 20  
A1B8I C2  C16  sing Y N 21  
A1B8I C7  C12  sing Y N 22  
A1B8I C10 C14  sing N N 23  
A1B8I N3  H9   sing N N 24  
A1B8I C4  H2   sing N N 25  
A1B8I C8  H4   sing N N 26  
A1B8I C13 H7   sing N N 27  
A1B8I C13 H8   sing N N 28  
A1B8I C15 H12  sing N N 29  
A1B8I C3  H1   sing N N 30  
A1B8I N2  H3   sing N N 31  
A1B8I C9  H5   sing N N 32  
A1B8I C12 H6   sing N N 33  
A1B8I C14 H10  sing N N 34  
A1B8I C14 H11  sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
DMS   S   O    doub N N 118 
DMS   S   C1   sing N N 119 
DMS   S   C2   sing N N 120 
DMS   C1  H11  sing N N 121 
DMS   C1  H12  sing N N 122 
DMS   C1  H13  sing N N 123 
DMS   C2  H21  sing N N 124 
DMS   C2  H22  sing N N 125 
DMS   C2  H23  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_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                    7IA3 
_atom_sites.fract_transf_matrix[1][1]   0.023427 
_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]   0.023427 
_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]   0.004617 
_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   ? -21.979 19.553  -7.120  1.00 55.44 ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.951 18.484  -7.328  1.00 55.41 ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.774 17.802  -8.686  1.00 53.75 ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.672 18.471  -9.718  1.00 54.76 ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -24.393 19.014  -7.182  1.00 58.30 ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -25.230 18.267  -6.148  1.00 65.47 ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.784 18.930  -5.240  1.00 66.77 ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.336 17.016  -6.251  1.00 68.55 ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.762 16.469  -8.685  1.00 50.80 ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.656 15.707  -9.917  1.00 48.35 ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -24.043 15.431  -10.483 1.00 46.03 ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -25.006 15.285  -9.729  1.00 45.48 ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.926 14.380  -9.688  1.00 48.29 ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.444 14.521  -9.614  1.00 49.03 ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.636 12.929  -9.344  1.00 49.62 ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.982 13.498  -9.057  1.00 48.86 ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -24.144 15.358  -11.815 1.00 44.49 ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.414 15.093  -12.484 1.00 43.78 ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.266 14.108  -13.639 1.00 42.56 ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.177 13.948  -14.174 1.00 42.04 ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -26.105 16.386  -12.928 1.00 44.01 ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.351 17.171  -13.977 1.00 45.83 ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.428 18.145  -13.617 1.00 47.15 ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.613 16.993  -15.331 1.00 46.95 ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.750 18.887  -14.578 1.00 48.45 ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.930 17.716  -16.300 1.00 48.05 ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.996 18.664  -15.920 1.00 49.82 ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.302 19.376  -16.877 1.00 52.78 ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.363 13.442  -14.019 1.00 41.92 ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.356 12.465  -15.098 1.00 41.48 ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -27.174 12.913  -16.337 1.00 41.30 ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -28.175 13.643  -16.226 1.00 41.13 ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.767 11.061  -14.593 1.00 41.94 ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.218 11.009  -14.109 1.00 42.41 ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.804 10.560  -13.509 1.00 42.53 ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.715 9.588   -13.974 1.00 43.17 ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.702 12.496  -17.531 1.00 41.22 ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.332 12.813  -18.815 1.00 42.00 ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.387 11.555  -19.654 1.00 42.84 ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.357 10.887  -19.791 1.00 42.30 ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.516 13.871  -19.578 1.00 43.88 ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.699 15.280  -19.057 1.00 49.87 ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.922 16.338  -19.816 1.00 58.06 ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.975 15.972  -20.552 1.00 58.57 ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -26.252 17.539  -19.664 1.00 61.42 ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.555 11.238  -20.254 1.00 43.16 ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.646 10.025  -21.065 1.00 43.76 ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.786 10.126  -22.294 1.00 43.77 ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.787 11.156  -22.946 1.00 44.24 ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -30.093 9.691   -21.429 1.00 45.61 ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.295 8.206   -21.701 1.00 48.83 ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.755 7.881   -21.912 1.00 51.93 ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.933 6.460   -22.189 1.00 54.98 ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -32.010 5.943   -23.412 1.00 57.48 ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.970 6.732   -24.479 1.00 58.84 ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -32.144 4.635   -23.579 1.00 56.47 ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.995 9.089   -22.574 1.00 43.55 ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -26.139 9.068   -23.758 1.00 44.03 ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.545 8.012   -24.801 1.00 44.33 ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -26.008 8.034   -25.905 1.00 45.35 ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.674 8.916   -23.373 1.00 44.34 ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.509 7.146   -24.489 1.00 43.87 ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.990 6.170   -25.458 1.00 44.60 ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.503 4.855   -24.910 1.00 45.61 ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.552 4.654   -23.695 1.00 45.51 ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.941 3.967   -25.813 1.00 45.97 ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.427 2.639   -25.456 1.00 47.29 ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.242 1.682   -25.321 1.00 48.62 ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -27.229 1.834   -26.005 1.00 48.65 ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.338 2.066   -26.554 1.00 48.78 ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.721 2.648   -26.636 1.00 54.77 ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.973 3.668   -25.974 1.00 54.53 ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.543 2.116   -27.417 1.00 58.43 ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.405 0.652   -24.501 1.00 49.45 ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.386 -0.366  -24.354 1.00 50.66 ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.739 -1.472  -25.334 1.00 52.90 ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.618 -2.296  -25.064 1.00 52.54 ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.275 -0.785  -22.891 1.00 50.59 ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.666 0.383   -22.099 1.00 51.21 ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.441 -2.047  -22.753 1.00 50.84 ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.681 0.243   -20.672 1.00 52.45 ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.103 -1.435  -26.523 0.50 53.86 ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -27.097 -1.452  -26.512 0.50 54.04 ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.319 -2.415  -27.588 0.50 55.28 ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.381 -2.405  -27.580 0.50 55.63 ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.019 -2.885  -28.212 0.50 56.84 ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.098 -2.834  -28.313 0.50 57.07 ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.055 -2.128  -28.291 0.50 56.75 ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.184 -2.026  -28.478 0.50 57.08 ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.196 -1.847  -28.724 0.50 56.20 ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.474 -1.804  -28.495 0.50 56.93 ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.559 -0.717  -29.328 0.50 56.52 ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.739 -1.941  -27.844 0.50 58.10 ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.596 -1.518  -28.275 0.50 56.82 ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.539 -2.444  -29.864 0.50 57.10 ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.014 -4.117  -28.710 1.00 58.16 ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.866 -4.653  -29.435 1.00 61.34 ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.980 -4.145  -30.884 1.00 65.11 ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.068 -4.173  -31.467 1.00 65.62 ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.911 -6.190  -29.406 1.00 61.00 ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -23.900 -6.891  -30.263 1.00 61.52 ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -24.071 -7.306  -31.554 1.00 62.66 ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.639 -7.424  -29.836 1.00 61.64 ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.958 -7.985  -31.981 1.00 63.06 ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -22.081 -8.111  -30.931 1.00 62.56 ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.914 -7.368  -28.637 1.00 62.00 ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.836 -8.738  -30.863 1.00 62.95 ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.685 -7.989  -28.574 1.00 62.63 ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.150 -8.649  -29.677 1.00 62.75 ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.877 -3.656  -31.461 1.00 67.59 ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.890 -3.164  -32.836 1.00 70.18 ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.193 -4.151  -33.762 1.00 73.07 ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.012 -4.435  -33.575 1.00 73.08 ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.237 -1.772  -32.946 1.00 72.74 ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.179 -1.247  -34.377 1.00 79.99 ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.256 -0.067  -34.620 1.00 88.43 ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -21.547 0.341   -33.671 1.00 91.26 ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.241 0.452   -35.759 1.00 90.75 ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.913 -4.668  -34.766 1.00 75.30 ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -23.309 -5.577  -35.736 1.00 78.18 ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.386 -4.755  -36.623 1.00 80.18 ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.736 -3.629  -36.998 1.00 80.51 ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -24.384 -6.251  -36.612 1.00 81.34 ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -25.358 -7.135  -35.840 1.00 87.13 ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -26.385 -7.778  -36.776 1.00 91.94 ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -27.498 -8.490  -36.042 1.00 96.16 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -28.379 -9.249  -36.971 1.00 98.78 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.215 -5.311  -36.965 1.00 81.30 ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.234 -4.631  -37.821 1.00 82.87 ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.668 -3.368  -37.159 1.00 82.65 ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -19.457 -2.346  -37.823 1.00 83.19 ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -20.788 -4.321  -39.231 1.00 86.27 ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.323 -5.527  -39.979 1.00 94.95 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -20.641 -6.582  -39.975 1.00 97.24 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.419 -5.413  -40.582 1.00 98.10 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.438 -3.439  -35.849 1.00 81.47 ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.804 -2.346  -35.132 1.00 80.86 ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.281 -2.435  -35.404 1.00 80.14 ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -16.784 -3.473  -35.865 1.00 79.89 ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.086 -2.475  -33.641 1.00 80.97 ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -16.539 -1.357  -35.128 1.00 79.66 ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.088 -1.352  -35.323 1.00 79.35 ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.407 -2.332  -34.331 1.00 77.38 ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -14.481 -2.131  -33.126 1.00 76.80 ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.556 0.075   -35.136 1.00 82.86 ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -13.096 0.243   -35.504 1.00 89.08 ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -12.343 1.101   -34.506 1.00 96.66 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -12.965 2.020   -33.923 1.00 97.03 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -11.133 0.846   -34.300 1.00 99.48 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -13.783 -3.407  -34.855 1.00 76.16 ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.106 -4.453  -34.073 1.00 75.38 ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.634 -4.101  -33.869 1.00 74.25 ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.882 -4.097  -34.836 1.00 74.81 ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.226 -5.875  -34.697 1.00 75.82 ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.947 -6.932  -33.650 1.00 76.56 ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.592 -6.117  -35.328 1.00 76.07 ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.213 -3.816  -32.629 1.00 72.33 ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -9.816  -3.462  -32.352 1.00 71.11 ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.367  -3.976  -30.962 1.00 70.28 ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.189 -4.441  -30.187 1.00 70.15 ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.625  -1.943  -32.506 1.00 71.62 ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.238  -1.651  -32.653 1.00 71.94 ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.177 -1.176  -31.330 1.00 71.95 ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.069  -3.934  -30.677 1.00 69.49 ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.549  -4.369  -29.389 1.00 68.90 ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.097  -5.813  -29.304 1.00 67.83 ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.705  -6.717  -29.885 1.00 67.68 ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.037  -6.033  -28.533 1.00 66.82 ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.493  -7.367  -28.323 1.00 66.19 ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -6.063  -8.028  -27.024 1.00 64.24 ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.911  -7.432  -26.358 1.00 64.11 ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.952  -7.332  -28.388 1.00 67.90 ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.283  -6.580  -27.261 1.00 71.04 ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.874  -5.722  -26.606 1.00 71.09 ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.010  -6.880  -27.033 1.00 72.41 ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.664  -9.278  -26.714 1.00 62.90 ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.156  -10.059 -25.563 1.00 62.31 ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.987  -10.516 -24.664 1.00 61.36 ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.639  -11.697 -24.654 1.00 61.62 ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.938  -11.282 -26.049 1.00 63.93 ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.670  -11.053 -27.243 1.00 67.05 ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.368  -9.609  -23.889 1.00 60.45 ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.200  -10.015 -23.090 1.00 59.87 ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.502  -10.750 -21.788 1.00 58.81 ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.388  -10.341 -21.046 1.00 58.72 ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.481  -8.689  -22.837 1.00 60.86 ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.596  -7.682  -22.768 1.00 61.31 ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.644  -8.161  -23.753 1.00 59.88 ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.748  -11.819 -21.500 1.00 58.05 ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.899  -12.555 -20.241 1.00 58.17 ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.882  -11.972 -19.259 1.00 56.67 ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.681  -12.054 -19.500 1.00 56.87 ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.712  -14.066 -20.443 1.00 60.78 ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -3.658  -14.610 -21.515 1.00 66.37 ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -4.231  -15.978 -21.195 1.00 71.70 ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.997  -16.508 -22.326 1.00 76.56 ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.676  -17.652 -22.308 1.00 79.44 ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -5.707  -18.398 -21.207 1.00 79.63 ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -6.333  -18.059 -23.391 1.00 78.52 ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.366  -11.292 -18.209 1.00 54.77 ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.486  -10.603 -17.271 1.00 53.33 ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.594  -11.120 -15.850 1.00 52.51 ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.690  -11.386 -15.383 1.00 52.69 ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.828  -9.098  -17.277 1.00 52.98 ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.837  -8.403  -18.638 1.00 53.65 ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.188  -6.959  -18.498 1.00 53.71 ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.467  -8.525  -19.328 1.00 54.57 ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.465  -11.204 -15.135 1.00 51.61 ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.476  -11.594 -13.733 1.00 51.02 ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.652  -10.316 -12.937 1.00 49.04 ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.207   -9.443  -13.022 1.00 49.02 ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.837   -12.283 -13.355 1.00 53.91 ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 0.979   -13.696 -13.894 1.00 60.81 ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? -0.035  -14.255 -14.383 1.00 61.97 ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 2.104   -14.249 -13.825 1.00 64.05 ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.803  -10.153 -12.247 1.00 47.27 ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -2.096  -8.923  -11.508 1.00 46.05 ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.392  -9.172  -10.012 1.00 45.69 ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.634  -10.313 -9.591  1.00 46.55 ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.222  -8.062  -12.178 1.00 45.78 ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.904  -7.717  -13.630 1.00 46.05 ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.576  -8.736  -12.065 1.00 45.62 ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.303  -8.097  -9.203  1.00 44.07 ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.601  -8.096  -7.770  1.00 43.09 ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.611  -6.971  -7.512  1.00 41.91 ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.552  -5.931  -8.168  1.00 42.03 ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.337  -7.862  -6.947  1.00 42.80 ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.545  -7.186  -6.592  1.00 40.47 ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.559  -6.186  -6.282  1.00 40.15 ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.462  -5.812  -4.804  1.00 40.85 ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.564  -6.691  -3.926  1.00 41.82 ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.953  -6.715  -6.643  1.00 39.29 ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.126  -5.820  -6.246  1.00 39.07 ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.139  -4.566  -7.060  1.00 39.23 ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.428  -6.550  -6.373  1.00 38.62 ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.176  -4.534  -4.515  1.00 40.58 ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -5.024  -4.123  -3.114  1.00 41.29 ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.368  -3.644  -2.495  1.00 42.03 ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.385  -3.543  -3.194  1.00 42.07 ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.869  -3.108  -2.927  1.00 42.28 ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.052  -1.726  -3.535  1.00 45.41 ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.206  -1.301  -3.714  1.00 45.53 ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.037  -1.058  -3.795  1.00 47.84 ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.350  -3.365  -1.184  1.00 42.42 ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.478  -2.904  -0.390  1.00 42.99 ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -8.093  -1.619  -0.961  1.00 42.35 ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.298  -1.441  -0.866  1.00 42.62 ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -7.026  -2.725  1.068   1.00 46.73 ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.165  -2.575  2.060   1.00 53.87 ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.759  -2.810  3.496   1.00 61.22 ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.296  -1.846  4.147   1.00 62.23 ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.886  -3.964  3.967   1.00 64.38 ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.295  -0.768  -1.628  1.00 41.23 ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.824  0.453   -2.244  1.00 40.42 ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.472  0.215   -3.633  1.00 39.45 ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.824  1.186   -4.314  1.00 38.89 ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.725  1.500   -2.375  1.00 41.90 ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.138  1.802   -1.121  1.00 45.39 ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.620  -1.048  -4.046  1.00 38.56 ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.216  -1.374  -5.334  1.00 38.34 ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.334  -1.045  -6.523  1.00 38.25 ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.818  -0.976  -7.648  1.00 38.05 ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -7.024  -0.885  -6.297  1.00 38.18 ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -6.080  -0.583  -7.362  1.00 38.59 ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.310  -1.834  -7.806  1.00 39.51 ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.739  -2.551  -6.979  1.00 40.20 ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -5.088  0.494   -6.901  1.00 39.15 ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.740  1.820   -6.590  1.00 40.90 ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.774  2.119   -7.197  1.00 40.26 ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -5.199  2.563   -5.747  1.00 43.00 ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.260  -2.071  -9.112  1.00 39.48 ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.529  -3.192  -9.679  1.00 39.79 ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.058  -2.846  -9.851  1.00 42.49 ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.681  -1.673  -9.953  1.00 42.73 ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.131  -3.622  -11.029 1.00 38.22 ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.447  -4.352  -10.920 1.00 37.52 ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.492  -5.675  -10.508 1.00 37.70 ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.642  -3.712  -11.205 1.00 37.21 ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.710  -6.339  -10.388 1.00 37.98 ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.854  -4.390  -11.115 1.00 37.39 ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.880  -5.698  -10.709 1.00 37.21 ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.224  -3.875  -9.896  1.00 44.18 ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.800  -3.721  -10.132 1.00 46.82 ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.284  -4.951  -10.886 1.00 49.51 ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.856  -6.033  -10.742 1.00 49.54 ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? -0.047  -3.537  -8.816  1.00 48.39 ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.289  -4.595  -7.899  1.00 50.80 ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.776   -4.795  -11.700 1.00 51.72 ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.347   -5.944  -12.405 1.00 54.51 ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.268   -6.706  -11.482 1.00 56.85 ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.111   -6.107  -10.818 1.00 57.06 ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.112   -5.524  -13.666 1.00 55.21 ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.238   -5.013  -14.817 1.00 57.49 ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.087   -4.618  -16.014 1.00 58.19 ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.209   -6.054  -15.242 1.00 58.40 ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.103   -8.025  -11.435 1.00 58.53 ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 2.916   -8.934  -10.627 1.00 60.41 ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.057   -9.439  -11.496 1.00 62.94 ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.813   -9.946  -12.589 1.00 63.04 ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.045   -10.115 -10.127 1.00 60.75 ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 2.892   -11.254 -9.572  1.00 61.24 ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.021   -9.645  -9.105  1.00 61.02 ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.300   -9.287  -11.036 1.00 64.95 ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.456   -9.779  -11.781 1.00 67.14 ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.481   -10.379 -10.806 1.00 67.93 ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.736   -11.584 -10.807 1.00 68.27 ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.096   -8.654  -12.622 1.00 71.03 ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.180   -7.986  -13.642 1.00 77.14 ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 6.708   -7.962  -15.065 1.00 85.31 ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 7.722   -8.648  -15.342 1.00 87.29 ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 6.106   -7.251  -15.904 1.00 87.41 ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -35.969 12.409  -11.721 1.00 53.09 ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -36.145 12.748  -13.130 1.00 53.76 ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -36.107 11.554  -14.079 1.00 53.88 ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.891 10.609  -13.916 1.00 54.53 ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -35.204 11.587  -15.092 1.00 52.52 ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -35.091 10.502  -16.071 1.00 51.68 ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -34.552 9.199   -15.489 1.00 50.22 ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -33.419 9.138   -15.012 1.00 50.47 ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -34.282 10.914  -17.308 1.00 54.09 ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -34.363 9.870   -18.412 1.00 58.85 ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -33.755 10.285  -19.735 1.00 64.20 ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -32.785 11.077  -19.715 1.00 64.14 ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -34.264 9.841   -20.792 1.00 66.24 ? 17  GLU   B OE2 1 
ATOM   325  N  N   A THR   B 2 9   ? -35.368 8.147   -15.529 0.50 49.44 ? 18  THR   B N   1 
ATOM   326  N  N   B THR   B 2 9   ? -35.374 8.155   -15.530 0.50 49.45 ? 18  THR   B N   1 
ATOM   327  C  CA  A THR   B 2 9   ? -34.966 6.841   -14.994 0.50 49.11 ? 18  THR   B CA  1 
ATOM   328  C  CA  B THR   B 2 9   ? -35.022 6.838   -15.002 0.50 49.14 ? 18  THR   B CA  1 
ATOM   329  C  C   A THR   B 2 9   ? -35.018 5.724   -16.053 0.50 48.01 ? 18  THR   B C   1 
ATOM   330  C  C   B THR   B 2 9   ? -35.022 5.731   -16.056 0.50 48.02 ? 18  THR   B C   1 
ATOM   331  O  O   A THR   B 2 9   ? -34.921 4.554   -15.698 0.50 48.11 ? 18  THR   B O   1 
ATOM   332  O  O   B THR   B 2 9   ? -34.912 4.565   -15.690 0.50 48.11 ? 18  THR   B O   1 
ATOM   333  C  CB  A THR   B 2 9   ? -35.766 6.462   -13.713 0.50 50.89 ? 18  THR   B CB  1 
ATOM   334  C  CB  B THR   B 2 9   ? -36.009 6.453   -13.898 0.50 50.92 ? 18  THR   B CB  1 
ATOM   335  O  OG1 A THR   B 2 9   ? -36.364 7.614   -13.097 0.50 52.26 ? 18  THR   B OG1 1 
ATOM   336  O  OG1 B THR   B 2 9   ? -37.344 6.592   -14.400 0.50 51.90 ? 18  THR   B OG1 1 
ATOM   337  C  CG2 A THR   B 2 9   ? -34.914 5.718   -12.687 0.50 51.25 ? 18  THR   B CG2 1 
ATOM   338  C  CG2 B THR   B 2 9   ? -35.827 7.290   -12.640 0.50 51.63 ? 18  THR   B CG2 1 
ATOM   339  N  N   . THR   B 2 10  ? -35.170 6.077   -17.344 1.00 46.96 ? 19  THR   B N   1 
ATOM   340  C  CA  . THR   B 2 10  ? -35.227 5.117   -18.440 1.00 45.38 ? 19  THR   B CA  1 
ATOM   341  C  C   . THR   B 2 10  ? -33.923 4.343   -18.540 1.00 43.05 ? 19  THR   B C   1 
ATOM   342  O  O   . THR   B 2 10  ? -32.855 4.917   -18.334 1.00 42.73 ? 19  THR   B O   1 
ATOM   343  C  CB  . THR   B 2 10  ? -35.534 5.868   -19.763 1.00 47.12 ? 19  THR   B CB  1 
ATOM   344  O  OG1 . THR   B 2 10  ? -36.662 6.738   -19.582 1.00 48.81 ? 19  THR   B OG1 1 
ATOM   345  C  CG2 . THR   B 2 10  ? -35.797 4.924   -20.937 1.00 47.19 ? 19  THR   B CG2 1 
ATOM   346  N  N   . ASP   B 2 11  ? -34.008 3.033   -18.826 1.00 41.41 ? 20  ASP   B N   1 
ATOM   347  C  CA  . ASP   B 2 11  ? -32.843 2.174   -19.021 1.00 40.78 ? 20  ASP   B CA  1 
ATOM   348  C  C   . ASP   B 2 11  ? -31.927 2.749   -20.125 1.00 40.55 ? 20  ASP   B C   1 
ATOM   349  O  O   . ASP   B 2 11  ? -32.420 3.308   -21.107 1.00 40.34 ? 20  ASP   B O   1 
ATOM   350  C  CB  . ASP   B 2 11  ? -33.291 0.756   -19.441 1.00 41.84 ? 20  ASP   B CB  1 
ATOM   351  C  CG  . ASP   B 2 11  ? -33.753 -0.142  -18.309 1.00 46.80 ? 20  ASP   B CG  1 
ATOM   352  O  OD1 . ASP   B 2 11  ? -33.913 0.363   -17.181 1.00 46.64 ? 20  ASP   B OD1 1 
ATOM   353  O  OD2 . ASP   B 2 11  ? -33.958 -1.359  -18.557 1.00 49.55 ? 20  ASP   B OD2 1 
ATOM   354  N  N   . GLY   B 2 12  ? -30.615 2.611   -19.949 1.00 39.87 ? 21  GLY   B N   1 
ATOM   355  C  CA  . GLY   B 2 12  ? -29.648 3.113   -20.913 1.00 38.86 ? 21  GLY   B CA  1 
ATOM   356  C  C   . GLY   B 2 12  ? -28.324 3.503   -20.290 1.00 37.82 ? 21  GLY   B C   1 
ATOM   357  O  O   . GLY   B 2 12  ? -28.110 3.304   -19.088 1.00 37.85 ? 21  GLY   B O   1 
ATOM   358  N  N   . VAL   B 2 13  ? -27.414 4.036   -21.116 1.00 36.24 ? 22  VAL   B N   1 
ATOM   359  C  CA  . VAL   B 2 13  ? -26.095 4.482   -20.677 1.00 35.47 ? 22  VAL   B CA  1 
ATOM   360  C  C   . VAL   B 2 13  ? -26.148 6.003   -20.439 1.00 35.75 ? 22  VAL   B C   1 
ATOM   361  O  O   . VAL   B 2 13  ? -26.856 6.720   -21.147 1.00 36.51 ? 22  VAL   B O   1 
ATOM   362  C  CB  . VAL   B 2 13  ? -24.980 4.027   -21.656 1.00 35.54 ? 22  VAL   B CB  1 
ATOM   363  C  CG1 . VAL   B 2 13  ? -25.120 4.696   -23.030 1.00 35.72 ? 22  VAL   B CG1 1 
ATOM   364  C  CG2 . VAL   B 2 13  ? -23.590 4.251   -21.075 1.00 35.11 ? 22  VAL   B CG2 1 
ATOM   365  N  N   . TYR   B 2 14  ? -25.523 6.472   -19.360 1.00 34.95 ? 23  TYR   B N   1 
ATOM   366  C  CA  . TYR   B 2 14  ? -25.559 7.882   -19.004 1.00 34.15 ? 23  TYR   B CA  1 
ATOM   367  C  C   . TYR   B 2 14  ? -24.160 8.423   -18.757 1.00 34.24 ? 23  TYR   B C   1 
ATOM   368  O  O   . TYR   B 2 14  ? -23.291 7.700   -18.284 1.00 34.74 ? 23  TYR   B O   1 
ATOM   369  C  CB  . TYR   B 2 14  ? -26.391 8.079   -17.713 1.00 33.66 ? 23  TYR   B CB  1 
ATOM   370  C  CG  . TYR   B 2 14  ? -27.893 7.933   -17.873 1.00 33.30 ? 23  TYR   B CG  1 
ATOM   371  C  CD1 . TYR   B 2 14  ? -28.466 6.700   -18.165 1.00 33.69 ? 23  TYR   B CD1 1 
ATOM   372  C  CD2 . TYR   B 2 14  ? -28.743 8.998   -17.625 1.00 33.77 ? 23  TYR   B CD2 1 
ATOM   373  C  CE1 . TYR   B 2 14  ? -29.838 6.558   -18.310 1.00 34.29 ? 23  TYR   B CE1 1 
ATOM   374  C  CE2 . TYR   B 2 14  ? -30.123 8.865   -17.744 1.00 34.54 ? 23  TYR   B CE2 1 
ATOM   375  C  CZ  . TYR   B 2 14  ? -30.668 7.642   -18.082 1.00 35.45 ? 23  TYR   B CZ  1 
ATOM   376  O  OH  . TYR   B 2 14  ? -32.026 7.494   -18.174 1.00 36.68 ? 23  TYR   B OH  1 
ATOM   377  N  N   . ARG   B 2 15  ? -23.971 9.715   -18.989 1.00 33.81 ? 24  ARG   B N   1 
ATOM   378  C  CA  . ARG   B 2 15  ? -22.736 10.426  -18.677 1.00 33.68 ? 24  ARG   B CA  1 
ATOM   379  C  C   . ARG   B 2 15  ? -22.870 10.992  -17.264 1.00 33.73 ? 24  ARG   B C   1 
ATOM   380  O  O   . ARG   B 2 15  ? -23.937 11.460  -16.888 1.00 34.11 ? 24  ARG   B O   1 
ATOM   381  C  CB  . ARG   B 2 15  ? -22.529 11.623  -19.626 1.00 34.37 ? 24  ARG   B CB  1 
ATOM   382  C  CG  . ARG   B 2 15  ? -22.443 11.296  -21.110 1.00 34.84 ? 24  ARG   B CG  1 
ATOM   383  C  CD  . ARG   B 2 15  ? -22.313 12.589  -21.902 1.00 36.15 ? 24  ARG   B CD  1 
ATOM   384  N  NE  . ARG   B 2 15  ? -22.516 12.363  -23.335 1.00 37.03 ? 24  ARG   B NE  1 
ATOM   385  C  CZ  . ARG   B 2 15  ? -21.557 12.015  -24.184 1.00 38.02 ? 24  ARG   B CZ  1 
ATOM   386  N  NH1 . ARG   B 2 15  ? -20.302 11.881  -23.765 1.00 35.32 ? 24  ARG   B NH1 1 
ATOM   387  N  NH2 . ARG   B 2 15  ? -21.844 11.795  -25.463 1.00 39.04 ? 24  ARG   B NH2 1 
ATOM   388  N  N   . VAL   B 2 16  ? -21.786 10.998  -16.511 1.00 33.43 ? 25  VAL   B N   1 
ATOM   389  C  CA  . VAL   B 2 16  ? -21.709 11.558  -15.175 1.00 34.24 ? 25  VAL   B CA  1 
ATOM   390  C  C   . VAL   B 2 16  ? -20.876 12.832  -15.314 1.00 35.88 ? 25  VAL   B C   1 
ATOM   391  O  O   . VAL   B 2 16  ? -19.710 12.792  -15.682 1.00 35.97 ? 25  VAL   B O   1 
ATOM   392  C  CB  . VAL   B 2 16  ? -21.101 10.562  -14.144 1.00 34.66 ? 25  VAL   B CB  1 
ATOM   393  C  CG1 . VAL   B 2 16  ? -21.161 11.154  -12.742 1.00 34.99 ? 25  VAL   B CG1 1 
ATOM   394  C  CG2 . VAL   B 2 16  ? -21.812 9.201   -14.191 1.00 34.44 ? 25  VAL   B CG2 1 
ATOM   395  N  N   . MET   B 2 17  ? -21.496 13.961  -15.077 1.00 37.39 ? 26  MET   B N   1 
ATOM   396  C  CA  . MET   B 2 17  ? -20.894 15.264  -15.273 1.00 39.47 ? 26  MET   B CA  1 
ATOM   397  C  C   . MET   B 2 17  ? -20.735 16.042  -13.963 1.00 42.36 ? 26  MET   B C   1 
ATOM   398  O  O   . MET   B 2 17  ? -21.368 15.706  -12.966 1.00 42.74 ? 26  MET   B O   1 
ATOM   399  C  CB  . MET   B 2 17  ? -21.809 16.087  -16.212 1.00 39.50 ? 26  MET   B CB  1 
ATOM   400  C  CG  . MET   B 2 17  ? -22.298 15.355  -17.458 1.00 40.37 ? 26  MET   B CG  1 
ATOM   401  S  SD  . MET   B 2 17  ? -20.990 15.136  -18.677 1.00 42.42 ? 26  MET   B SD  1 
ATOM   402  C  CE  . MET   B 2 17  ? -20.545 16.867  -18.979 1.00 41.76 ? 26  MET   B CE  1 
ATOM   403  N  N   . THR   B 2 18  ? -19.951 17.133  -13.990 1.00 44.28 ? 27  THR   B N   1 
ATOM   404  C  CA  . THR   B 2 18  ? -19.767 18.009  -12.839 1.00 46.57 ? 27  THR   B CA  1 
ATOM   405  C  C   . THR   B 2 18  ? -19.565 19.459  -13.292 1.00 48.68 ? 27  THR   B C   1 
ATOM   406  O  O   . THR   B 2 18  ? -18.924 19.709  -14.309 1.00 48.46 ? 27  THR   B O   1 
ATOM   407  C  CB  . THR   B 2 18  ? -18.611 17.506  -11.938 1.00 48.01 ? 27  THR   B CB  1 
ATOM   408  O  OG1 . THR   B 2 18  ? -18.497 18.352  -10.785 1.00 49.03 ? 27  THR   B OG1 1 
ATOM   409  C  CG2 . THR   B 2 18  ? -17.277 17.449  -12.671 1.00 48.38 ? 27  THR   B CG2 1 
ATOM   410  N  N   . ARG   B 2 19  ? -20.128 20.411  -12.553 1.00 50.77 ? 28  ARG   B N   1 
ATOM   411  C  CA  . ARG   B 2 19  ? -19.925 21.833  -12.847 1.00 53.31 ? 28  ARG   B CA  1 
ATOM   412  C  C   . ARG   B 2 19  ? -18.960 22.492  -11.816 1.00 54.79 ? 28  ARG   B C   1 
ATOM   413  O  O   . ARG   B 2 19  ? -18.957 23.717  -11.675 1.00 55.13 ? 28  ARG   B O   1 
ATOM   414  C  CB  . ARG   B 2 19  ? -21.266 22.583  -12.910 1.00 55.82 ? 28  ARG   B CB  1 
ATOM   415  C  CG  . ARG   B 2 19  ? -21.886 22.644  -14.308 1.00 60.71 ? 28  ARG   B CG  1 
ATOM   416  C  CD  . ARG   B 2 19  ? -23.396 22.660  -14.199 1.00 65.76 ? 28  ARG   B CD  1 
ATOM   417  N  NE  . ARG   B 2 19  ? -24.063 22.490  -15.492 1.00 70.71 ? 28  ARG   B NE  1 
ATOM   418  C  CZ  . ARG   B 2 19  ? -25.299 22.013  -15.640 1.00 74.30 ? 28  ARG   B CZ  1 
ATOM   419  N  NH1 . ARG   B 2 19  ? -26.006 21.631  -14.579 1.00 74.74 ? 28  ARG   B NH1 1 
ATOM   420  N  NH2 . ARG   B 2 19  ? -25.827 21.887  -16.851 1.00 74.12 ? 28  ARG   B NH2 1 
ATOM   421  N  N   . ARG   B 2 20  ? -18.134 21.677  -11.122 1.00 55.57 ? 29  ARG   B N   1 
ATOM   422  C  CA  . ARG   B 2 20  ? -17.188 22.125  -10.093 1.00 56.99 ? 29  ARG   B CA  1 
ATOM   423  C  C   . ARG   B 2 20  ? -15.915 22.680  -10.717 1.00 57.31 ? 29  ARG   B C   1 
ATOM   424  O  O   . ARG   B 2 20  ? -15.423 23.727  -10.287 1.00 57.60 ? 29  ARG   B O   1 
ATOM   425  C  CB  . ARG   B 2 20  ? -16.863 20.980  -9.105  1.00 59.18 ? 29  ARG   B CB  1 
ATOM   426  C  CG  . ARG   B 2 20  ? -15.855 21.367  -8.027  1.00 63.80 ? 29  ARG   B CG  1 
ATOM   427  C  CD  . ARG   B 2 20  ? -15.513 20.216  -7.103  1.00 68.43 ? 29  ARG   B CD  1 
ATOM   428  N  NE  . ARG   B 2 20  ? -14.952 19.066  -7.819  1.00 72.64 ? 29  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   B 2 20  ? -13.650 18.828  -7.955  1.00 75.69 ? 29  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   B 2 20  ? -12.755 19.662  -7.437  1.00 75.77 ? 29  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   B 2 20  ? -13.232 17.754  -8.613  1.00 75.66 ? 29  ARG   B NH2 1 
ATOM   432  N  N   . LEU   B 2 21  ? -15.393 22.000  -11.748 1.00 56.86 ? 30  LEU   B N   1 
ATOM   433  C  CA  . LEU   B 2 21  ? -14.199 22.473  -12.449 1.00 57.06 ? 30  LEU   B CA  1 
ATOM   434  C  C   . LEU   B 2 21  ? -14.606 23.560  -13.500 1.00 56.35 ? 30  LEU   B C   1 
ATOM   435  O  O   . LEU   B 2 21  ? -15.677 24.168  -13.372 1.00 56.29 ? 30  LEU   B O   1 
ATOM   436  C  CB  . LEU   B 2 21  ? -13.458 21.275  -13.107 1.00 57.79 ? 30  LEU   B CB  1 
ATOM   437  C  CG  . LEU   B 2 21  ? -12.778 20.227  -12.211 1.00 59.87 ? 30  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   B 2 21  ? -12.053 20.860  -11.019 1.00 60.75 ? 30  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   B 2 21  ? -13.748 19.160  -11.770 1.00 60.78 ? 30  LEU   B CD2 1 
ATOM   440  N  N   . LEU   B 2 22  ? -13.757 23.819  -14.514 1.00 55.44 ? 31  LEU   B N   1 
ATOM   441  C  CA  . LEU   B 2 22  ? -14.067 24.773  -15.575 1.00 55.13 ? 31  LEU   B CA  1 
ATOM   442  C  C   . LEU   B 2 22  ? -15.122 24.143  -16.499 1.00 54.63 ? 31  LEU   B C   1 
ATOM   443  O  O   . LEU   B 2 22  ? -15.019 22.952  -16.817 1.00 55.46 ? 31  LEU   B O   1 
ATOM   444  C  CB  . LEU   B 2 22  ? -12.793 25.050  -16.359 1.00 55.15 ? 31  LEU   B CB  1 
ATOM   445  C  CG  . LEU   B 2 22  ? -12.866 26.132  -17.397 1.00 56.26 ? 31  LEU   B CG  1 
ATOM   446  C  CD1 . LEU   B 2 22  ? -12.611 27.502  -16.783 1.00 56.31 ? 31  LEU   B CD1 1 
ATOM   447  C  CD2 . LEU   B 2 22  ? -11.874 25.848  -18.495 1.00 57.03 ? 31  LEU   B CD2 1 
ATOM   448  N  N   . GLY   B 2 23  ? -16.135 24.926  -16.880 1.00 52.91 ? 32  GLY   B N   1 
ATOM   449  C  CA  . GLY   B 2 23  ? -17.240 24.468  -17.718 1.00 51.72 ? 32  GLY   B CA  1 
ATOM   450  C  C   . GLY   B 2 23  ? -17.958 23.243  -17.174 1.00 50.47 ? 32  GLY   B C   1 
ATOM   451  O  O   . GLY   B 2 23  ? -18.082 23.071  -15.955 1.00 50.77 ? 32  GLY   B O   1 
ATOM   452  N  N   . SER   B 2 24  ? -18.412 22.363  -18.072 1.00 48.74 ? 33  SER   B N   1 
ATOM   453  C  CA  . SER   B 2 24  ? -19.072 21.115  -17.687 1.00 47.36 ? 33  SER   B CA  1 
ATOM   454  C  C   . SER   B 2 24  ? -18.092 19.993  -18.003 1.00 45.35 ? 33  SER   B C   1 
ATOM   455  O  O   . SER   B 2 24  ? -17.756 19.808  -19.162 1.00 45.23 ? 33  SER   B O   1 
ATOM   456  C  CB  . SER   B 2 24  ? -20.352 20.916  -18.497 1.00 48.65 ? 33  SER   B CB  1 
ATOM   457  O  OG  . SER   B 2 24  ? -21.344 21.876  -18.171 1.00 50.63 ? 33  SER   B OG  1 
ATOM   458  N  N   . THR   B 2 25  ? -17.615 19.266  -16.989 1.00 43.79 ? 34  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 25  ? -16.632 18.212  -17.194 1.00 42.83 ? 34  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 25  ? -17.207 16.814  -16.971 1.00 41.68 ? 34  THR   B C   1 
ATOM   461  O  O   . THR   B 2 25  ? -17.908 16.585  -15.985 1.00 41.61 ? 34  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 25  ? -15.387 18.480  -16.321 1.00 44.01 ? 34  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 25  ? -14.873 19.782  -16.634 1.00 46.02 ? 34  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 25  ? -14.290 17.438  -16.516 1.00 43.61 ? 34  THR   B CG2 1 
ATOM   465  N  N   . GLN   B 2 26  ? -16.902 15.875  -17.880 1.00 40.44 ? 35  GLN   B N   1 
ATOM   466  C  CA  . GLN   B 2 26  ? -17.369 14.508  -17.729 1.00 39.56 ? 35  GLN   B CA  1 
ATOM   467  C  C   . GLN   B 2 26  ? -16.397 13.741  -16.842 1.00 40.08 ? 35  GLN   B C   1 
ATOM   468  O  O   . GLN   B 2 26  ? -15.227 13.563  -17.204 1.00 40.65 ? 35  GLN   B O   1 
ATOM   469  C  CB  . GLN   B 2 26  ? -17.544 13.812  -19.094 1.00 38.60 ? 35  GLN   B CB  1 
ATOM   470  C  CG  . GLN   B 2 26  ? -17.978 12.359  -18.966 1.00 37.54 ? 35  GLN   B CG  1 
ATOM   471  C  CD  . GLN   B 2 26  ? -18.314 11.726  -20.282 1.00 37.25 ? 35  GLN   B CD  1 
ATOM   472  O  OE1 . GLN   B 2 26  ? -19.000 12.309  -21.114 1.00 37.72 ? 35  GLN   B OE1 1 
ATOM   473  N  NE2 . GLN   B 2 26  ? -17.872 10.502  -20.490 1.00 36.49 ? 35  GLN   B NE2 1 
ATOM   474  N  N   . VAL   B 2 27  ? -16.872 13.285  -15.674 1.00 39.27 ? 36  VAL   B N   1 
ATOM   475  C  CA  . VAL   B 2 27  ? -16.023 12.509  -14.762 1.00 38.68 ? 36  VAL   B CA  1 
ATOM   476  C  C   . VAL   B 2 27  ? -16.168 10.990  -14.931 1.00 37.60 ? 36  VAL   B C   1 
ATOM   477  O  O   . VAL   B 2 27  ? -15.360 10.238  -14.387 1.00 37.80 ? 36  VAL   B O   1 
ATOM   478  C  CB  . VAL   B 2 27  ? -16.222 12.919  -13.277 1.00 39.85 ? 36  VAL   B CB  1 
ATOM   479  C  CG1 . VAL   B 2 27  ? -15.615 14.286  -13.001 1.00 40.93 ? 36  VAL   B CG1 1 
ATOM   480  C  CG2 . VAL   B 2 27  ? -17.694 12.892  -12.882 1.00 39.88 ? 36  VAL   B CG2 1 
ATOM   481  N  N   . GLY   B 2 28  ? -17.188 10.548  -15.654 1.00 36.20 ? 37  GLY   B N   1 
ATOM   482  C  CA  . GLY   B 2 28  ? -17.431 9.129   -15.843 1.00 35.33 ? 37  GLY   B CA  1 
ATOM   483  C  C   . GLY   B 2 28  ? -18.736 8.835   -16.543 1.00 34.70 ? 37  GLY   B C   1 
ATOM   484  O  O   . GLY   B 2 28  ? -19.402 9.738   -17.045 1.00 34.84 ? 37  GLY   B O   1 
ATOM   485  N  N   . VAL   B 2 29  ? -19.099 7.561   -16.571 1.00 34.23 ? 38  VAL   B N   1 
ATOM   486  C  CA  . VAL   B 2 29  ? -20.263 6.983   -17.242 1.00 34.26 ? 38  VAL   B CA  1 
ATOM   487  C  C   . VAL   B 2 29  ? -20.957 5.964   -16.298 1.00 33.67 ? 38  VAL   B C   1 
ATOM   488  O  O   . VAL   B 2 29  ? -20.374 5.537   -15.300 1.00 33.63 ? 38  VAL   B O   1 
ATOM   489  C  CB  . VAL   B 2 29  ? -19.800 6.307   -18.578 1.00 35.15 ? 38  VAL   B CB  1 
ATOM   490  C  CG1 . VAL   B 2 29  ? -20.928 5.538   -19.245 1.00 35.36 ? 38  VAL   B CG1 1 
ATOM   491  C  CG2 . VAL   B 2 29  ? -19.216 7.327   -19.553 1.00 35.51 ? 38  VAL   B CG2 1 
ATOM   492  N  N   . GLY   B 2 30  ? -22.199 5.611   -16.602 1.00 32.88 ? 39  GLY   B N   1 
ATOM   493  C  CA  . GLY   B 2 30  ? -22.948 4.658   -15.802 1.00 32.53 ? 39  GLY   B CA  1 
ATOM   494  C  C   . GLY   B 2 30  ? -24.094 4.001   -16.537 1.00 32.56 ? 39  GLY   B C   1 
ATOM   495  O  O   . GLY   B 2 30  ? -24.457 4.421   -17.639 1.00 32.63 ? 39  GLY   B O   1 
ATOM   496  N  N   . VAL   B 2 31  ? -24.653 2.934   -15.944 1.00 32.42 ? 40  VAL   B N   1 
ATOM   497  C  CA  . VAL   B 2 31  ? -25.757 2.162   -16.520 1.00 32.10 ? 40  VAL   B CA  1 
ATOM   498  C  C   . VAL   B 2 31  ? -27.013 2.299   -15.683 1.00 32.13 ? 40  VAL   B C   1 
ATOM   499  O  O   . VAL   B 2 31  ? -26.974 2.022   -14.494 1.00 31.83 ? 40  VAL   B O   1 
ATOM   500  C  CB  . VAL   B 2 31  ? -25.381 0.666   -16.626 1.00 32.19 ? 40  VAL   B CB  1 
ATOM   501  C  CG1 . VAL   B 2 31  ? -26.563 -0.173  -17.105 1.00 32.14 ? 40  VAL   B CG1 1 
ATOM   502  C  CG2 . VAL   B 2 31  ? -24.165 0.468   -17.521 1.00 32.87 ? 40  VAL   B CG2 1 
ATOM   503  N  N   . MET   B 2 32  ? -28.137 2.647   -16.310 1.00 32.29 ? 41  MET   B N   1 
ATOM   504  C  CA  . MET   B 2 32  ? -29.398 2.693   -15.614 1.00 32.78 ? 41  MET   B CA  1 
ATOM   505  C  C   . MET   B 2 32  ? -30.150 1.418   -15.986 1.00 33.91 ? 41  MET   B C   1 
ATOM   506  O  O   . MET   B 2 32  ? -30.396 1.181   -17.163 1.00 34.54 ? 41  MET   B O   1 
ATOM   507  C  CB  . MET   B 2 32  ? -30.178 3.948   -15.987 1.00 32.65 ? 41  MET   B CB  1 
ATOM   508  C  CG  . MET   B 2 32  ? -31.423 4.146   -15.176 1.00 34.13 ? 41  MET   B CG  1 
ATOM   509  S  SD  . MET   B 2 32  ? -31.095 4.704   -13.477 1.00 37.32 ? 41  MET   B SD  1 
ATOM   510  C  CE  . MET   B 2 32  ? -30.767 6.470   -13.796 1.00 35.76 ? 41  MET   B CE  1 
ATOM   511  N  N   . GLN   B 2 33  ? -30.442 0.558   -15.008 1.00 33.70 ? 42  GLN   B N   1 
ATOM   512  C  CA  . GLN   B 2 33  ? -31.179 -0.669  -15.269 1.00 34.02 ? 42  GLN   B CA  1 
ATOM   513  C  C   . GLN   B 2 33  ? -32.083 -0.940  -14.099 1.00 34.13 ? 42  GLN   B C   1 
ATOM   514  O  O   . GLN   B 2 33  ? -31.631 -0.850  -12.964 1.00 34.37 ? 42  GLN   B O   1 
ATOM   515  C  CB  . GLN   B 2 33  ? -30.234 -1.858  -15.509 1.00 36.19 ? 42  GLN   B CB  1 
ATOM   516  C  CG  . GLN   B 2 33  ? -31.003 -3.128  -15.854 1.00 41.38 ? 42  GLN   B CG  1 
ATOM   517  C  CD  . GLN   B 2 33  ? -30.141 -4.239  -16.391 1.00 47.96 ? 42  GLN   B CD  1 
ATOM   518  O  OE1 . GLN   B 2 33  ? -30.205 -5.392  -15.928 1.00 49.49 ? 42  GLN   B OE1 1 
ATOM   519  N  NE2 . GLN   B 2 33  ? -29.304 -3.920  -17.378 1.00 49.54 ? 42  GLN   B NE2 1 
ATOM   520  N  N   . GLU   B 2 34  ? -33.362 -1.230  -14.351 1.00 34.17 ? 43  GLU   B N   1 
ATOM   521  C  CA  . GLU   B 2 34  ? -34.349 -1.521  -13.312 1.00 34.78 ? 43  GLU   B CA  1 
ATOM   522  C  C   . GLU   B 2 34  ? -34.433 -0.445  -12.195 1.00 35.20 ? 43  GLU   B C   1 
ATOM   523  O  O   . GLU   B 2 34  ? -34.598 -0.777  -11.021 1.00 35.87 ? 43  GLU   B O   1 
ATOM   524  C  CB  . GLU   B 2 34  ? -34.118 -2.920  -12.724 1.00 37.32 ? 43  GLU   B CB  1 
ATOM   525  C  CG  . GLU   B 2 34  ? -34.110 -4.028  -13.774 1.00 41.65 ? 43  GLU   B CG  1 
ATOM   526  C  CD  . GLU   B 2 34  ? -33.437 -5.330  -13.364 1.00 48.19 ? 43  GLU   B CD  1 
ATOM   527  O  OE1 . GLU   B 2 34  ? -33.750 -5.846  -12.267 1.00 48.82 ? 43  GLU   B OE1 1 
ATOM   528  O  OE2 . GLU   B 2 34  ? -32.595 -5.836  -14.141 1.00 51.29 ? 43  GLU   B OE2 1 
ATOM   529  N  N   . GLY   B 2 35  ? -34.336 0.830   -12.573 1.00 34.46 ? 44  GLY   B N   1 
ATOM   530  C  CA  . GLY   B 2 35  ? -34.401 1.939   -11.622 1.00 34.04 ? 44  GLY   B CA  1 
ATOM   531  C  C   . GLY   B 2 35  ? -33.156 2.120   -10.773 1.00 33.49 ? 44  GLY   B C   1 
ATOM   532  O  O   . GLY   B 2 35  ? -33.184 2.859   -9.783  1.00 33.88 ? 44  GLY   B O   1 
ATOM   533  N  N   . VAL   B 2 36  ? -32.059 1.429   -11.128 1.00 32.55 ? 45  VAL   B N   1 
ATOM   534  C  CA  . VAL   B 2 36  ? -30.799 1.488   -10.389 1.00 32.13 ? 45  VAL   B CA  1 
ATOM   535  C  C   . VAL   B 2 36  ? -29.697 2.052   -11.274 1.00 30.83 ? 45  VAL   B C   1 
ATOM   536  O  O   . VAL   B 2 36  ? -29.581 1.653   -12.429 1.00 31.09 ? 45  VAL   B O   1 
ATOM   537  C  CB  . VAL   B 2 36  ? -30.415 0.107   -9.764  1.00 33.01 ? 45  VAL   B CB  1 
ATOM   538  C  CG1 . VAL   B 2 36  ? -28.998 0.120   -9.179  1.00 33.39 ? 45  VAL   B CG1 1 
ATOM   539  C  CG2 . VAL   B 2 36  ? -31.419 -0.297  -8.690  1.00 33.30 ? 45  VAL   B CG2 1 
ATOM   540  N  N   . PHE   B 2 37  ? -28.946 3.036   -10.772 1.00 29.90 ? 46  PHE   B N   1 
ATOM   541  C  CA  . PHE   B 2 37  ? -27.845 3.598   -11.523 1.00 30.07 ? 46  PHE   B CA  1 
ATOM   542  C  C   . PHE   B 2 37  ? -26.568 2.927   -11.026 1.00 29.36 ? 46  PHE   B C   1 
ATOM   543  O  O   . PHE   B 2 37  ? -26.296 2.937   -9.838  1.00 29.13 ? 46  PHE   B O   1 
ATOM   544  C  CB  . PHE   B 2 37  ? -27.784 5.125   -11.390 1.00 30.27 ? 46  PHE   B CB  1 
ATOM   545  C  CG  . PHE   B 2 37  ? -26.765 5.735   -12.325 1.00 31.42 ? 46  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   B 2 37  ? -26.949 5.700   -13.696 1.00 32.11 ? 46  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   B 2 37  ? -25.617 6.330   -11.832 1.00 32.19 ? 46  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   B 2 37  ? -26.011 6.256   -14.553 1.00 32.60 ? 46  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   B 2 37  ? -24.682 6.884   -12.690 1.00 32.62 ? 46  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   B 2 37  ? -24.892 6.854   -14.044 1.00 32.62 ? 46  PHE   B CZ  1 
ATOM   551  N  N   . HIS   B 2 38  ? -25.824 2.300   -11.932 1.00 28.89 ? 47  HIS   B N   1 
ATOM   552  C  CA  . HIS   B 2 38  ? -24.599 1.565   -11.636 1.00 28.83 ? 47  HIS   B CA  1 
ATOM   553  C  C   . HIS   B 2 38  ? -23.425 2.305   -12.222 1.00 29.13 ? 47  HIS   B C   1 
ATOM   554  O  O   . HIS   B 2 38  ? -23.426 2.582   -13.413 1.00 29.14 ? 47  HIS   B O   1 
ATOM   555  C  CB  . HIS   B 2 38  ? -24.635 0.175   -12.317 1.00 28.45 ? 47  HIS   B CB  1 
ATOM   556  C  CG  . HIS   B 2 38  ? -25.886 -0.600  -12.045 1.00 30.48 ? 47  HIS   B CG  1 
ATOM   557  N  ND1 . HIS   B 2 38  ? -27.107 -0.233  -12.611 1.00 31.97 ? 47  HIS   B ND1 1 
ATOM   558  C  CD2 . HIS   B 2 38  ? -26.084 -1.663  -11.233 1.00 31.57 ? 47  HIS   B CD2 1 
ATOM   559  C  CE1 . HIS   B 2 38  ? -27.995 -1.097  -12.141 1.00 32.54 ? 47  HIS   B CE1 1 
ATOM   560  N  NE2 . HIS   B 2 38  ? -27.427 -1.977  -11.308 1.00 32.81 ? 47  HIS   B NE2 1 
ATOM   561  N  N   . THR   B 2 39  ? -22.389 2.563   -11.414 1.00 28.86 ? 48  THR   B N   1 
ATOM   562  C  CA  . THR   B 2 39  ? -21.172 3.173   -11.934 1.00 28.79 ? 48  THR   B CA  1 
ATOM   563  C  C   . THR   B 2 39  ? -19.931 2.659   -11.143 1.00 28.13 ? 48  THR   B C   1 
ATOM   564  O  O   . THR   B 2 39  ? -20.049 1.752   -10.312 1.00 27.11 ? 48  THR   B O   1 
ATOM   565  C  CB  . THR   B 2 39  ? -21.305 4.718   -12.044 1.00 29.83 ? 48  THR   B CB  1 
ATOM   566  O  OG1 . THR   B 2 39  ? -20.204 5.167   -12.834 1.00 30.44 ? 48  THR   B OG1 1 
ATOM   567  C  CG2 . THR   B 2 39  ? -21.310 5.412   -10.685 1.00 29.44 ? 48  THR   B CG2 1 
ATOM   568  N  N   . MET   B 2 40  ? -18.741 3.188   -11.448 1.00 28.47 ? 49  MET   B N   1 
ATOM   569  C  CA  . MET   B 2 40  ? -17.541 2.828   -10.718 1.00 29.51 ? 49  MET   B CA  1 
ATOM   570  C  C   . MET   B 2 40  ? -17.399 3.751   -9.513  1.00 30.60 ? 49  MET   B C   1 
ATOM   571  O  O   . MET   B 2 40  ? -17.764 4.935   -9.577  1.00 30.91 ? 49  MET   B O   1 
ATOM   572  C  CB  . MET   B 2 40  ? -16.337 2.863   -11.649 1.00 30.07 ? 49  MET   B CB  1 
ATOM   573  C  CG  . MET   B 2 40  ? -16.524 1.948   -12.851 1.00 32.47 ? 49  MET   B CG  1 
ATOM   574  S  SD  . MET   B 2 40  ? -15.037 1.020   -13.306 1.00 39.38 ? 49  MET   B SD  1 
ATOM   575  C  CE  . MET   B 2 40  ? -15.066 -0.308  -12.142 1.00 31.90 ? 49  MET   B CE  1 
ATOM   576  N  N   . TRP   B 2 41  ? -16.896 3.215   -8.393  1.00 30.92 ? 50  TRP   B N   1 
ATOM   577  C  CA  A TRP   B 2 41  ? -16.742 4.005   -7.176  0.50 31.99 ? 50  TRP   B CA  1 
ATOM   578  C  CA  B TRP   B 2 41  ? -16.738 3.992   -7.174  0.50 31.21 ? 50  TRP   B CA  1 
ATOM   579  C  C   . TRP   B 2 41  ? -15.878 5.238   -7.382  1.00 32.21 ? 50  TRP   B C   1 
ATOM   580  O  O   . TRP   B 2 41  ? -16.225 6.307   -6.880  1.00 32.38 ? 50  TRP   B O   1 
ATOM   581  C  CB  A TRP   B 2 41  ? -16.195 3.164   -5.997  0.50 32.50 ? 50  TRP   B CB  1 
ATOM   582  C  CB  B TRP   B 2 41  ? -16.182 3.127   -6.010  0.50 30.62 ? 50  TRP   B CB  1 
ATOM   583  C  CG  A TRP   B 2 41  ? -16.318 3.858   -4.670  0.50 33.68 ? 50  TRP   B CG  1 
ATOM   584  C  CG  B TRP   B 2 41  ? -15.993 3.914   -4.749  0.50 30.25 ? 50  TRP   B CG  1 
ATOM   585  C  CD1 A TRP   B 2 41  ? -17.391 3.829   -3.832  0.50 34.89 ? 50  TRP   B CD1 1 
ATOM   586  C  CD1 B TRP   B 2 41  ? -14.948 4.736   -4.448  0.50 30.85 ? 50  TRP   B CD1 1 
ATOM   587  C  CD2 A TRP   B 2 41  ? -15.366 4.757   -4.073  0.50 34.26 ? 50  TRP   B CD2 1 
ATOM   588  C  CD2 B TRP   B 2 41  ? -16.948 4.079   -3.699  0.50 30.04 ? 50  TRP   B CD2 1 
ATOM   589  N  NE1 A TRP   B 2 41  ? -17.159 4.633   -2.738  0.50 35.42 ? 50  TRP   B NE1 1 
ATOM   590  N  NE1 B TRP   B 2 41  ? -15.191 5.398   -3.272  0.50 30.91 ? 50  TRP   B NE1 1 
ATOM   591  C  CE2 A TRP   B 2 41  ? -15.927 5.222   -2.867  0.50 35.18 ? 50  TRP   B CE2 1 
ATOM   592  C  CE2 B TRP   B 2 41  ? -16.405 5.002   -2.781  0.50 30.57 ? 50  TRP   B CE2 1 
ATOM   593  C  CE3 A TRP   B 2 41  ? -14.087 5.204   -4.436  0.50 35.16 ? 50  TRP   B CE3 1 
ATOM   594  C  CE3 B TRP   B 2 41  ? -18.203 3.525   -3.433  0.50 30.43 ? 50  TRP   B CE3 1 
ATOM   595  C  CZ2 A TRP   B 2 41  ? -15.254 6.104   -2.022  0.50 36.12 ? 50  TRP   B CZ2 1 
ATOM   596  C  CZ2 B TRP   B 2 41  ? -17.071 5.375   -1.618  0.50 30.79 ? 50  TRP   B CZ2 1 
ATOM   597  C  CZ3 A TRP   B 2 41  ? -13.426 6.085   -3.601  0.50 36.28 ? 50  TRP   B CZ3 1 
ATOM   598  C  CZ3 B TRP   B 2 41  ? -18.844 3.875   -2.264  0.50 30.92 ? 50  TRP   B CZ3 1 
ATOM   599  C  CH2 A TRP   B 2 41  ? -13.994 6.501   -2.395  0.50 36.43 ? 50  TRP   B CH2 1 
ATOM   600  C  CH2 B TRP   B 2 41  ? -18.287 4.804   -1.381  0.50 30.76 ? 50  TRP   B CH2 1 
ATOM   601  N  N   . HIS   B 2 42  ? -14.738 5.093   -8.072  1.00 32.56 ? 51  HIS   B N   1 
ATOM   602  C  CA  . HIS   B 2 42  ? -13.841 6.231   -8.262  1.00 33.40 ? 51  HIS   B CA  1 
ATOM   603  C  C   . HIS   B 2 42  ? -14.449 7.372   -9.108  1.00 33.89 ? 51  HIS   B C   1 
ATOM   604  O  O   . HIS   B 2 42  ? -13.882 8.442   -9.122  1.00 34.13 ? 51  HIS   B O   1 
ATOM   605  C  CB  . HIS   B 2 42  ? -12.474 5.783   -8.803  1.00 33.81 ? 51  HIS   B CB  1 
ATOM   606  C  CG  . HIS   B 2 42  ? -12.464 5.450   -10.262 1.00 34.85 ? 51  HIS   B CG  1 
ATOM   607  N  ND1 . HIS   B 2 42  ? -12.690 4.154   -10.717 1.00 36.22 ? 51  HIS   B ND1 1 
ATOM   608  C  CD2 . HIS   B 2 42  ? -12.266 6.258   -11.329 1.00 35.65 ? 51  HIS   B CD2 1 
ATOM   609  C  CE1 . HIS   B 2 42  ? -12.608 4.221   -12.034 1.00 36.17 ? 51  HIS   B CE1 1 
ATOM   610  N  NE2 . HIS   B 2 42  ? -12.359 5.468   -12.447 1.00 36.20 ? 51  HIS   B NE2 1 
ATOM   611  N  N   . VAL   B 2 43  ? -15.581 7.153   -9.796  1.00 34.17 ? 52  VAL   B N   1 
ATOM   612  C  CA  . VAL   B 2 43  ? -16.231 8.201   -10.574 1.00 34.74 ? 52  VAL   B CA  1 
ATOM   613  C  C   . VAL   B 2 43  ? -16.908 9.213   -9.633  1.00 35.41 ? 52  VAL   B C   1 
ATOM   614  O  O   . VAL   B 2 43  ? -16.648 10.415  -9.727  1.00 35.94 ? 52  VAL   B O   1 
ATOM   615  C  CB  . VAL   B 2 43  ? -17.235 7.615   -11.617 1.00 35.31 ? 52  VAL   B CB  1 
ATOM   616  C  CG1 . VAL   B 2 43  ? -18.163 8.692   -12.180 1.00 35.40 ? 52  VAL   B CG1 1 
ATOM   617  C  CG2 . VAL   B 2 43  ? -16.502 6.898   -12.756 1.00 35.55 ? 52  VAL   B CG2 1 
ATOM   618  N  N   . THR   B 2 44  ? -17.767 8.727   -8.714  1.00 35.20 ? 53  THR   B N   1 
ATOM   619  C  CA  . THR   B 2 44  ? -18.530 9.587   -7.814  1.00 35.06 ? 53  THR   B CA  1 
ATOM   620  C  C   . THR   B 2 44  ? -17.986 9.705   -6.378  1.00 36.07 ? 53  THR   B C   1 
ATOM   621  O  O   . THR   B 2 44  ? -18.399 10.617  -5.662  1.00 36.60 ? 53  THR   B O   1 
ATOM   622  C  CB  . THR   B 2 44  ? -19.955 9.050   -7.725  1.00 35.20 ? 53  THR   B CB  1 
ATOM   623  O  OG1 . THR   B 2 44  ? -19.939 7.784   -7.048  1.00 35.40 ? 53  THR   B OG1 1 
ATOM   624  C  CG2 . THR   B 2 44  ? -20.617 8.906   -9.085  1.00 35.73 ? 53  THR   B CG2 1 
ATOM   625  N  N   . LYS   B 2 45  ? -17.116 8.771   -5.945  1.00 36.01 ? 54  LYS   B N   1 
ATOM   626  C  CA  . LYS   B 2 45  ? -16.614 8.647   -4.564  1.00 37.22 ? 54  LYS   B CA  1 
ATOM   627  C  C   . LYS   B 2 45  ? -17.784 8.434   -3.556  1.00 36.89 ? 54  LYS   B C   1 
ATOM   628  O  O   . LYS   B 2 45  ? -17.670 8.808   -2.384  1.00 36.79 ? 54  LYS   B O   1 
ATOM   629  C  CB  . LYS   B 2 45  ? -15.739 9.839   -4.121  1.00 40.49 ? 54  LYS   B CB  1 
ATOM   630  C  CG  . LYS   B 2 45  ? -14.762 10.372  -5.164  1.00 46.85 ? 54  LYS   B CG  1 
ATOM   631  C  CD  . LYS   B 2 45  ? -13.652 9.404   -5.522  1.00 52.83 ? 54  LYS   B CD  1 
ATOM   632  C  CE  . LYS   B 2 45  ? -12.691 10.089  -6.473  1.00 58.37 ? 54  LYS   B CE  1 
ATOM   633  N  NZ  . LYS   B 2 45  ? -11.914 9.117   -7.306  1.00 61.47 ? 54  LYS   B NZ  1 
ATOM   634  N  N   . GLY   B 2 46  ? -18.896 7.865   -4.028  1.00 36.03 ? 55  GLY   B N   1 
ATOM   635  C  CA  . GLY   B 2 46  ? -20.078 7.654   -3.209  1.00 35.84 ? 55  GLY   B CA  1 
ATOM   636  C  C   . GLY   B 2 46  ? -20.969 8.870   -3.031  1.00 35.88 ? 55  GLY   B C   1 
ATOM   637  O  O   . GLY   B 2 46  ? -21.930 8.812   -2.266  1.00 36.20 ? 55  GLY   B O   1 
ATOM   638  N  N   . ALA   B 2 47  ? -20.664 9.990   -3.702  1.00 35.76 ? 56  ALA   B N   1 
ATOM   639  C  CA  . ALA   B 2 47  ? -21.473 11.207  -3.565  1.00 36.74 ? 56  ALA   B CA  1 
ATOM   640  C  C   . ALA   B 2 47  ? -22.852 11.082  -4.237  1.00 37.33 ? 56  ALA   B C   1 
ATOM   641  O  O   . ALA   B 2 47  ? -23.036 10.248  -5.116  1.00 36.92 ? 56  ALA   B O   1 
ATOM   642  C  CB  . ALA   B 2 47  ? -20.711 12.413  -4.120  1.00 36.87 ? 56  ALA   B CB  1 
ATOM   643  N  N   . ALA   B 2 48  ? -23.810 11.928  -3.833  1.00 38.00 ? 57  ALA   B N   1 
ATOM   644  C  CA  . ALA   B 2 48  ? -25.153 11.947  -4.401  1.00 38.92 ? 57  ALA   B CA  1 
ATOM   645  C  C   . ALA   B 2 48  ? -25.128 12.463  -5.838  1.00 39.93 ? 57  ALA   B C   1 
ATOM   646  O  O   . ALA   B 2 48  ? -24.256 13.249  -6.197  1.00 40.80 ? 57  ALA   B O   1 
ATOM   647  C  CB  . ALA   B 2 48  ? -26.068 12.827  -3.555  1.00 38.86 ? 57  ALA   B CB  1 
ATOM   648  N  N   . LEU   B 2 49  ? -26.071 12.014  -6.664  1.00 39.57 ? 58  LEU   B N   1 
ATOM   649  C  CA  . LEU   B 2 49  ? -26.152 12.448  -8.054  1.00 39.82 ? 58  LEU   B CA  1 
ATOM   650  C  C   . LEU   B 2 49  ? -27.472 13.179  -8.312  1.00 41.04 ? 58  LEU   B C   1 
ATOM   651  O  O   . LEU   B 2 49  ? -28.426 13.046  -7.555  1.00 41.37 ? 58  LEU   B O   1 
ATOM   652  C  CB  . LEU   B 2 49  ? -26.002 11.252  -9.021  1.00 39.37 ? 58  LEU   B CB  1 
ATOM   653  C  CG  . LEU   B 2 49  ? -24.758 10.398  -8.849  1.00 39.94 ? 58  LEU   B CG  1 
ATOM   654  C  CD1 . LEU   B 2 49  ? -24.807 9.187   -9.739  1.00 39.45 ? 58  LEU   B CD1 1 
ATOM   655  C  CD2 . LEU   B 2 49  ? -23.503 11.195  -9.078  1.00 40.72 ? 58  LEU   B CD2 1 
ATOM   656  N  N   . ARG   B 2 50  ? -27.525 13.944  -9.379  1.00 42.10 ? 59  ARG   B N   1 
ATOM   657  C  CA  . ARG   B 2 50  ? -28.716 14.675  -9.756  1.00 44.08 ? 59  ARG   B CA  1 
ATOM   658  C  C   . ARG   B 2 50  ? -29.179 14.223  -11.149 1.00 45.21 ? 59  ARG   B C   1 
ATOM   659  O  O   . ARG   B 2 50  ? -28.349 13.919  -11.999 1.00 45.04 ? 59  ARG   B O   1 
ATOM   660  C  CB  . ARG   B 2 50  ? -28.396 16.171  -9.703  1.00 46.39 ? 59  ARG   B CB  1 
ATOM   661  C  CG  . ARG   B 2 50  ? -29.460 17.066  -10.285 1.00 51.90 ? 59  ARG   B CG  1 
ATOM   662  C  CD  . ARG   B 2 50  ? -29.213 18.538  -9.981  1.00 56.34 ? 59  ARG   B CD  1 
ATOM   663  N  NE  . ARG   B 2 50  ? -27.856 18.979  -10.323 1.00 59.87 ? 59  ARG   B NE  1 
ATOM   664  C  CZ  . ARG   B 2 50  ? -27.472 19.374  -11.532 1.00 62.98 ? 59  ARG   B CZ  1 
ATOM   665  N  NH1 . ARG   B 2 50  ? -28.330 19.356  -12.549 1.00 62.78 ? 59  ARG   B NH1 1 
ATOM   666  N  NH2 . ARG   B 2 50  ? -26.225 19.779  -11.739 1.00 63.68 ? 59  ARG   B NH2 1 
ATOM   667  N  N   . SER   B 2 51  ? -30.486 14.094  -11.362 1.00 46.37 ? 60  SER   B N   1 
ATOM   668  C  CA  . SER   B 2 51  ? -31.028 13.753  -12.680 1.00 48.51 ? 60  SER   B CA  1 
ATOM   669  C  C   . SER   B 2 51  ? -32.165 14.735  -12.915 1.00 50.92 ? 60  SER   B C   1 
ATOM   670  O  O   . SER   B 2 51  ? -33.314 14.453  -12.579 1.00 51.60 ? 60  SER   B O   1 
ATOM   671  C  CB  . SER   B 2 51  ? -31.524 12.310  -12.724 1.00 49.67 ? 60  SER   B CB  1 
ATOM   672  O  OG  . SER   B 2 51  ? -31.991 11.961  -14.017 1.00 51.87 ? 60  SER   B OG  1 
ATOM   673  N  N   . GLY   B 2 52  ? -31.817 15.927  -13.381 1.00 51.96 ? 61  GLY   B N   1 
ATOM   674  C  CA  . GLY   B 2 52  ? -32.786 16.998  -13.554 1.00 53.02 ? 61  GLY   B CA  1 
ATOM   675  C  C   . GLY   B 2 52  ? -33.135 17.561  -12.196 1.00 54.37 ? 61  GLY   B C   1 
ATOM   676  O  O   . GLY   B 2 52  ? -32.242 17.974  -11.455 1.00 55.11 ? 61  GLY   B O   1 
ATOM   677  N  N   . GLU   B 2 53  ? -34.420 17.529  -11.826 1.00 54.47 ? 62  GLU   B N   1 
ATOM   678  C  CA  . GLU   B 2 53  ? -34.840 17.985  -10.502 1.00 55.10 ? 62  GLU   B CA  1 
ATOM   679  C  C   . GLU   B 2 53  ? -34.664 16.902  -9.424  1.00 55.20 ? 62  GLU   B C   1 
ATOM   680  O  O   . GLU   B 2 53  ? -34.554 17.230  -8.235  1.00 55.82 ? 62  GLU   B O   1 
ATOM   681  C  CB  . GLU   B 2 53  ? -36.300 18.464  -10.523 1.00 58.49 ? 62  GLU   B CB  1 
ATOM   682  C  CG  . GLU   B 2 53  ? -36.463 19.974  -10.553 1.00 65.92 ? 62  GLU   B CG  1 
ATOM   683  C  CD  . GLU   B 2 53  ? -37.910 20.437  -10.526 1.00 75.63 ? 62  GLU   B CD  1 
ATOM   684  O  OE1 . GLU   B 2 53  ? -38.736 19.847  -11.263 1.00 77.79 ? 62  GLU   B OE1 1 
ATOM   685  O  OE2 . GLU   B 2 53  ? -38.220 21.389  -9.771  1.00 78.45 ? 62  GLU   B OE2 1 
ATOM   686  N  N   . GLY   B 2 54  ? -34.663 15.632  -9.837  1.00 54.51 ? 63  GLY   B N   1 
ATOM   687  C  CA  . GLY   B 2 54  ? -34.534 14.490  -8.944  1.00 54.04 ? 63  GLY   B CA  1 
ATOM   688  C  C   . GLY   B 2 54  ? -33.152 14.271  -8.369  1.00 53.41 ? 63  GLY   B C   1 
ATOM   689  O  O   . GLY   B 2 54  ? -32.149 14.719  -8.931  1.00 53.97 ? 63  GLY   B O   1 
ATOM   690  N  N   . ARG   B 2 55  ? -33.098 13.552  -7.246  1.00 51.79 ? 64  ARG   B N   1 
ATOM   691  C  CA  . ARG   B 2 55  ? -31.864 13.227  -6.540  1.00 50.35 ? 64  ARG   B CA  1 
ATOM   692  C  C   . ARG   B 2 55  ? -31.647 11.701  -6.507  1.00 47.99 ? 64  ARG   B C   1 
ATOM   693  O  O   . ARG   B 2 55  ? -32.591 10.950  -6.282  1.00 48.41 ? 64  ARG   B O   1 
ATOM   694  C  CB  . ARG   B 2 55  ? -31.936 13.782  -5.102  1.00 51.82 ? 64  ARG   B CB  1 
ATOM   695  C  CG  . ARG   B 2 55  ? -30.650 13.594  -4.299  1.00 55.61 ? 64  ARG   B CG  1 
ATOM   696  C  CD  . ARG   B 2 55  ? -30.789 14.115  -2.878  1.00 59.28 ? 64  ARG   B CD  1 
ATOM   697  N  NE  . ARG   B 2 55  ? -29.598 13.844  -2.068  1.00 62.44 ? 64  ARG   B NE  1 
ATOM   698  C  CZ  . ARG   B 2 55  ? -28.878 14.784  -1.458  1.00 65.14 ? 64  ARG   B CZ  1 
ATOM   699  N  NH1 . ARG   B 2 55  ? -29.220 16.066  -1.559  1.00 64.84 ? 64  ARG   B NH1 1 
ATOM   700  N  NH2 . ARG   B 2 55  ? -27.817 14.449  -0.730  1.00 64.66 ? 64  ARG   B NH2 1 
ATOM   701  N  N   . LEU   B 2 56  ? -30.415 11.247  -6.732  1.00 45.40 ? 65  LEU   B N   1 
ATOM   702  C  CA  . LEU   B 2 56  ? -30.076 9.830   -6.671  1.00 43.61 ? 65  LEU   B CA  1 
ATOM   703  C  C   . LEU   B 2 56  ? -29.168 9.626   -5.474  1.00 41.51 ? 65  LEU   B C   1 
ATOM   704  O  O   . LEU   B 2 56  ? -28.092 10.219  -5.421  1.00 41.15 ? 65  LEU   B O   1 
ATOM   705  C  CB  . LEU   B 2 56  ? -29.319 9.384   -7.931  1.00 43.80 ? 65  LEU   B CB  1 
ATOM   706  C  CG  . LEU   B 2 56  ? -29.973 9.544   -9.290  1.00 45.62 ? 65  LEU   B CG  1 
ATOM   707  C  CD1 . LEU   B 2 56  ? -29.174 8.807   -10.341 1.00 46.11 ? 65  LEU   B CD1 1 
ATOM   708  C  CD2 . LEU   B 2 56  ? -31.399 9.028   -9.297  1.00 46.35 ? 65  LEU   B CD2 1 
ATOM   709  N  N   . ASP   B 2 57  ? -29.592 8.821   -4.502  1.00 40.21 ? 66  ASP   B N   1 
ATOM   710  C  CA  . ASP   B 2 57  ? -28.782 8.585   -3.308  1.00 39.43 ? 66  ASP   B CA  1 
ATOM   711  C  C   . ASP   B 2 57  ? -28.069 7.241   -3.416  1.00 37.51 ? 66  ASP   B C   1 
ATOM   712  O  O   . ASP   B 2 57  ? -28.647 6.280   -3.922  1.00 37.48 ? 66  ASP   B O   1 
ATOM   713  C  CB  . ASP   B 2 57  ? -29.659 8.628   -2.054  1.00 42.89 ? 66  ASP   B CB  1 
ATOM   714  C  CG  . ASP   B 2 57  ? -30.396 9.945   -1.868  1.00 50.83 ? 66  ASP   B CG  1 
ATOM   715  O  OD1 . ASP   B 2 57  ? -29.771 11.016  -2.089  1.00 51.91 ? 66  ASP   B OD1 1 
ATOM   716  O  OD2 . ASP   B 2 57  ? -31.594 9.908   -1.496  1.00 54.25 ? 66  ASP   B OD2 1 
ATOM   717  N  N   . PRO   B 2 58  ? -26.803 7.154   -2.979  1.00 36.01 ? 67  PRO   B N   1 
ATOM   718  C  CA  . PRO   B 2 58  ? -26.095 5.862   -3.040  1.00 35.30 ? 67  PRO   B CA  1 
ATOM   719  C  C   . PRO   B 2 58  ? -26.790 4.805   -2.177  1.00 34.39 ? 67  PRO   B C   1 
ATOM   720  O  O   . PRO   B 2 58  ? -27.380 5.131   -1.157  1.00 35.14 ? 67  PRO   B O   1 
ATOM   721  C  CB  . PRO   B 2 58  ? -24.702 6.201   -2.499  1.00 35.98 ? 67  PRO   B CB  1 
ATOM   722  C  CG  . PRO   B 2 58  ? -24.923 7.402   -1.632  1.00 36.38 ? 67  PRO   B CG  1 
ATOM   723  C  CD  . PRO   B 2 58  ? -25.979 8.195   -2.332  1.00 35.14 ? 67  PRO   B CD  1 
ATOM   724  N  N   . TYR   B 2 59  ? -26.748 3.554   -2.597  1.00 32.81 ? 68  TYR   B N   1 
ATOM   725  C  CA  . TYR   B 2 59  ? -27.399 2.467   -1.892  1.00 31.51 ? 68  TYR   B CA  1 
ATOM   726  C  C   . TYR   B 2 59  ? -26.380 1.429   -1.449  1.00 31.16 ? 68  TYR   B C   1 
ATOM   727  O  O   . TYR   B 2 59  ? -26.410 0.989   -0.313  1.00 32.21 ? 68  TYR   B O   1 
ATOM   728  C  CB  . TYR   B 2 59  ? -28.478 1.856   -2.796  1.00 30.91 ? 68  TYR   B CB  1 
ATOM   729  C  CG  . TYR   B 2 59  ? -29.265 0.730   -2.167  1.00 30.76 ? 68  TYR   B CG  1 
ATOM   730  C  CD1 . TYR   B 2 59  ? -28.720 -0.541  -2.047  1.00 31.30 ? 68  TYR   B CD1 1 
ATOM   731  C  CD2 . TYR   B 2 59  ? -30.588 0.905   -1.796  1.00 31.05 ? 68  TYR   B CD2 1 
ATOM   732  C  CE1 . TYR   B 2 59  ? -29.434 -1.582  -1.472  1.00 32.15 ? 68  TYR   B CE1 1 
ATOM   733  C  CE2 . TYR   B 2 59  ? -31.331 -0.141  -1.269  1.00 32.16 ? 68  TYR   B CE2 1 
ATOM   734  C  CZ  . TYR   B 2 59  ? -30.753 -1.389  -1.120  1.00 32.88 ? 68  TYR   B CZ  1 
ATOM   735  O  OH  . TYR   B 2 59  ? -31.476 -2.433  -0.600  1.00 33.98 ? 68  TYR   B OH  1 
ATOM   736  N  N   . TRP   B 2 60  ? -25.492 1.032   -2.331  1.00 30.66 ? 69  TRP   B N   1 
ATOM   737  C  CA  . TRP   B 2 60  ? -24.454 0.061   -2.030  1.00 30.80 ? 69  TRP   B CA  1 
ATOM   738  C  C   . TRP   B 2 60  ? -23.148 0.533   -2.678  1.00 31.23 ? 69  TRP   B C   1 
ATOM   739  O  O   . TRP   B 2 60  ? -23.168 1.050   -3.781  1.00 31.15 ? 69  TRP   B O   1 
ATOM   740  C  CB  . TRP   B 2 60  ? -24.844 -1.346  -2.547  1.00 30.72 ? 69  TRP   B CB  1 
ATOM   741  C  CG  . TRP   B 2 60  ? -23.694 -2.317  -2.509  1.00 31.19 ? 69  TRP   B CG  1 
ATOM   742  C  CD1 . TRP   B 2 60  ? -23.209 -2.969  -1.411  1.00 32.16 ? 69  TRP   B CD1 1 
ATOM   743  C  CD2 . TRP   B 2 60  ? -22.775 -2.592  -3.579  1.00 31.14 ? 69  TRP   B CD2 1 
ATOM   744  N  NE1 . TRP   B 2 60  ? -22.089 -3.692  -1.749  1.00 32.59 ? 69  TRP   B NE1 1 
ATOM   745  C  CE2 . TRP   B 2 60  ? -21.776 -3.444  -3.065  1.00 32.01 ? 69  TRP   B CE2 1 
ATOM   746  C  CE3 . TRP   B 2 60  ? -22.672 -2.157  -4.908  1.00 31.43 ? 69  TRP   B CE3 1 
ATOM   747  C  CZ2 . TRP   B 2 60  ? -20.723 -3.914  -3.848  1.00 32.37 ? 69  TRP   B CZ2 1 
ATOM   748  C  CZ3 . TRP   B 2 60  ? -21.646 -2.642  -5.689  1.00 32.32 ? 69  TRP   B CZ3 1 
ATOM   749  C  CH2 . TRP   B 2 60  ? -20.683 -3.510  -5.160  1.00 32.67 ? 69  TRP   B CH2 1 
ATOM   750  N  N   . GLY   B 2 61  ? -22.025 0.289   -2.024  1.00 31.86 ? 70  GLY   B N   1 
ATOM   751  C  CA  . GLY   B 2 61  ? -20.724 0.660   -2.575  1.00 32.49 ? 70  GLY   B CA  1 
ATOM   752  C  C   . GLY   B 2 61  ? -19.594 -0.116  -1.947  1.00 32.42 ? 70  GLY   B C   1 
ATOM   753  O  O   . GLY   B 2 61  ? -19.723 -0.576  -0.816  1.00 32.94 ? 70  GLY   B O   1 
ATOM   754  N  N   . ASP   B 2 62  ? -18.479 -0.256  -2.660  1.00 32.16 ? 71  ASP   B N   1 
ATOM   755  C  CA  . ASP   B 2 62  ? -17.307 -0.986  -2.181  1.00 32.08 ? 71  ASP   B CA  1 
ATOM   756  C  C   . ASP   B 2 62  ? -16.079 -0.449  -2.928  1.00 31.37 ? 71  ASP   B C   1 
ATOM   757  O  O   . ASP   B 2 62  ? -16.057 -0.513  -4.136  1.00 30.96 ? 71  ASP   B O   1 
ATOM   758  C  CB  . ASP   B 2 62  ? -17.494 -2.483  -2.471  1.00 34.30 ? 71  ASP   B CB  1 
ATOM   759  C  CG  . ASP   B 2 62  ? -16.523 -3.393  -1.760  1.00 40.70 ? 71  ASP   B CG  1 
ATOM   760  O  OD1 . ASP   B 2 62  ? -15.323 -3.360  -2.098  1.00 41.70 ? 71  ASP   B OD1 1 
ATOM   761  O  OD2 . ASP   B 2 62  ? -16.965 -4.153  -0.876  1.00 44.52 ? 71  ASP   B OD2 1 
ATOM   762  N  N   . VAL   B 2 63  ? -15.064 0.074   -2.211  1.00 31.51 ? 72  VAL   B N   1 
ATOM   763  C  CA  . VAL   B 2 63  ? -13.848 0.649   -2.797  1.00 31.33 ? 72  VAL   B CA  1 
ATOM   764  C  C   . VAL   B 2 63  ? -12.966 -0.414  -3.468  1.00 31.22 ? 72  VAL   B C   1 
ATOM   765  O  O   . VAL   B 2 63  ? -12.346 -0.126  -4.497  1.00 31.48 ? 72  VAL   B O   1 
ATOM   766  C  CB  . VAL   B 2 63  ? -13.067 1.505   -1.756  1.00 31.67 ? 72  VAL   B CB  1 
ATOM   767  C  CG1 . VAL   B 2 63  ? -11.611 1.722   -2.155  1.00 32.23 ? 72  VAL   B CG1 1 
ATOM   768  C  CG2 . VAL   B 2 63  ? -13.750 2.844   -1.523  1.00 32.04 ? 72  VAL   B CG2 1 
ATOM   769  N  N   . LYS   B 2 64  ? -12.942 -1.634  -2.932  1.00 30.94 ? 73  LYS   B N   1 
ATOM   770  C  CA  . LYS   B 2 64  ? -12.087 -2.688  -3.497  1.00 30.99 ? 73  LYS   B CA  1 
ATOM   771  C  C   . LYS   B 2 64  ? -12.637 -3.219  -4.800  1.00 31.45 ? 73  LYS   B C   1 
ATOM   772  O  O   . LYS   B 2 64  ? -11.895 -3.300  -5.778  1.00 31.53 ? 73  LYS   B O   1 
ATOM   773  C  CB  . LYS   B 2 64  ? -11.792 -3.802  -2.489  1.00 32.24 ? 73  LYS   B CB  1 
ATOM   774  C  CG  . LYS   B 2 64  ? -10.728 -4.755  -3.016  1.00 35.94 ? 73  LYS   B CG  1 
ATOM   775  C  CD  . LYS   B 2 64  ? -10.243 -5.686  -1.928  1.00 39.59 ? 73  LYS   B CD  1 
ATOM   776  C  CE  . LYS   B 2 64  ? -9.504  -6.832  -2.549  1.00 43.39 ? 73  LYS   B CE  1 
ATOM   777  N  NZ  . LYS   B 2 64  ? -9.204  -7.887  -1.549  1.00 46.60 ? 73  LYS   B NZ  1 
ATOM   778  N  N   . GLN   B 2 65  ? -13.942 -3.518  -4.853  1.00 31.63 ? 74  GLN   B N   1 
ATOM   779  C  CA  . GLN   B 2 65  ? -14.565 -3.910  -6.121  1.00 32.00 ? 74  GLN   B CA  1 
ATOM   780  C  C   . GLN   B 2 65  ? -14.635 -2.726  -7.112  1.00 31.86 ? 74  GLN   B C   1 
ATOM   781  O  O   . GLN   B 2 65  ? -14.821 -2.938  -8.314  1.00 31.48 ? 74  GLN   B O   1 
ATOM   782  C  CB  . GLN   B 2 65  ? -15.984 -4.425  -5.911  1.00 34.01 ? 74  GLN   B CB  1 
ATOM   783  C  CG  . GLN   B 2 65  ? -16.089 -5.678  -5.075  1.00 39.41 ? 74  GLN   B CG  1 
ATOM   784  C  CD  . GLN   B 2 65  ? -17.542 -6.111  -5.002  1.00 45.68 ? 74  GLN   B CD  1 
ATOM   785  O  OE1 . GLN   B 2 65  ? -18.293 -6.077  -6.007  1.00 46.90 ? 74  GLN   B OE1 1 
ATOM   786  N  NE2 . GLN   B 2 65  ? -17.971 -6.536  -3.819  1.00 46.82 ? 74  GLN   B NE2 1 
ATOM   787  N  N   . ASP   B 2 66  ? -14.524 -1.486  -6.589  1.00 31.38 ? 75  ASP   B N   1 
ATOM   788  C  CA  . ASP   B 2 66  ? -14.611 -0.224  -7.312  1.00 30.85 ? 75  ASP   B CA  1 
ATOM   789  C  C   . ASP   B 2 66  ? -15.988 -0.069  -7.923  1.00 29.97 ? 75  ASP   B C   1 
ATOM   790  O  O   . ASP   B 2 66  ? -16.100 0.492   -8.985  1.00 29.58 ? 75  ASP   B O   1 
ATOM   791  C  CB  . ASP   B 2 66  ? -13.489 -0.056  -8.363  1.00 32.31 ? 75  ASP   B CB  1 
ATOM   792  C  CG  . ASP   B 2 66  ? -13.367 1.368   -8.859  1.00 35.56 ? 75  ASP   B CG  1 
ATOM   793  O  OD1 . ASP   B 2 66  ? -13.625 2.294   -8.066  1.00 36.38 ? 75  ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   B 2 66  ? -13.016 1.556   -10.033 1.00 37.65 ? 75  ASP   B OD2 1 
ATOM   795  N  N   . LEU   B 2 67  ? -17.052 -0.501  -7.226  1.00 29.62 ? 76  LEU   B N   1 
ATOM   796  C  CA  . LEU   B 2 67  ? -18.415 -0.365  -7.731  1.00 29.25 ? 76  LEU   B CA  1 
ATOM   797  C  C   . LEU   B 2 67  ? -19.320 0.410   -6.776  1.00 29.41 ? 76  LEU   B C   1 
ATOM   798  O  O   . LEU   B 2 67  ? -19.039 0.498   -5.579  1.00 28.91 ? 76  LEU   B O   1 
ATOM   799  C  CB  . LEU   B 2 67  ? -19.007 -1.744  -8.033  1.00 28.93 ? 76  LEU   B CB  1 
ATOM   800  C  CG  . LEU   B 2 67  ? -18.314 -2.468  -9.178  1.00 30.04 ? 76  LEU   B CG  1 
ATOM   801  C  CD1 . LEU   B 2 67  ? -18.780 -3.880  -9.270  1.00 30.75 ? 76  LEU   B CD1 1 
ATOM   802  C  CD2 . LEU   B 2 67  ? -18.476 -1.715  -10.516 1.00 30.39 ? 76  LEU   B CD2 1 
ATOM   803  N  N   . VAL   B 2 68  ? -20.414 0.972   -7.310  1.00 29.07 ? 77  VAL   B N   1 
ATOM   804  C  CA  . VAL   B 2 68  ? -21.397 1.706   -6.500  1.00 28.95 ? 77  VAL   B CA  1 
ATOM   805  C  C   . VAL   B 2 68  ? -22.770 1.663   -7.210  1.00 28.91 ? 77  VAL   B C   1 
ATOM   806  O  O   . VAL   B 2 68  ? -22.827 1.678   -8.425  1.00 28.60 ? 77  VAL   B O   1 
ATOM   807  C  CB  . VAL   B 2 68  ? -20.915 3.165   -6.168  1.00 29.08 ? 77  VAL   B CB  1 
ATOM   808  C  CG1 . VAL   B 2 68  ? -20.707 3.994   -7.439  1.00 28.94 ? 77  VAL   B CG1 1 
ATOM   809  C  CG2 . VAL   B 2 68  ? -21.855 3.882   -5.188  1.00 29.42 ? 77  VAL   B CG2 1 
ATOM   810  N  N   . SER   B 2 69  ? -23.860 1.545   -6.455  1.00 29.26 ? 78  SER   B N   1 
ATOM   811  C  CA  . SER   B 2 69  ? -25.213 1.564   -7.016  1.00 28.91 ? 78  SER   B CA  1 
ATOM   812  C  C   . SER   B 2 69  ? -26.041 2.687   -6.348  1.00 28.86 ? 78  SER   B C   1 
ATOM   813  O  O   . SER   B 2 69  ? -25.714 3.152   -5.248  1.00 28.80 ? 78  SER   B O   1 
ATOM   814  C  CB  . SER   B 2 69  ? -25.895 0.197   -6.927  1.00 28.94 ? 78  SER   B CB  1 
ATOM   815  O  OG  . SER   B 2 69  ? -26.297 -0.137  -5.609  1.00 29.85 ? 78  SER   B OG  1 
ATOM   816  N  N   . TYR   B 2 70  ? -27.046 3.181   -7.067  1.00 28.58 ? 79  TYR   B N   1 
ATOM   817  C  CA  . TYR   B 2 70  ? -27.875 4.298   -6.654  1.00 29.25 ? 79  TYR   B CA  1 
ATOM   818  C  C   . TYR   B 2 70  ? -29.323 3.902   -6.769  1.00 30.24 ? 79  TYR   B C   1 
ATOM   819  O  O   . TYR   B 2 70  ? -29.721 3.288   -7.775  1.00 30.32 ? 79  TYR   B O   1 
ATOM   820  C  CB  . TYR   B 2 70  ? -27.607 5.510   -7.572  1.00 29.19 ? 79  TYR   B CB  1 
ATOM   821  C  CG  . TYR   B 2 70  ? -26.282 6.174   -7.281  1.00 29.88 ? 79  TYR   B CG  1 
ATOM   822  C  CD1 . TYR   B 2 70  ? -25.101 5.698   -7.844  1.00 29.94 ? 79  TYR   B CD1 1 
ATOM   823  C  CD2 . TYR   B 2 70  ? -26.204 7.264   -6.426  1.00 30.77 ? 79  TYR   B CD2 1 
ATOM   824  C  CE1 . TYR   B 2 70  ? -23.874 6.281   -7.542  1.00 30.70 ? 79  TYR   B CE1 1 
ATOM   825  C  CE2 . TYR   B 2 70  ? -24.985 7.837   -6.097  1.00 31.30 ? 79  TYR   B CE2 1 
ATOM   826  C  CZ  . TYR   B 2 70  ? -23.821 7.336   -6.645  1.00 31.87 ? 79  TYR   B CZ  1 
ATOM   827  O  OH  . TYR   B 2 70  ? -22.636 7.942   -6.320  1.00 33.02 ? 79  TYR   B OH  1 
ATOM   828  N  N   . CYS   B 2 71  ? -30.107 4.237   -5.737  1.00 30.81 ? 80  CYS   B N   1 
ATOM   829  C  CA  . CYS   B 2 71  ? -31.551 3.983   -5.672  1.00 32.46 ? 80  CYS   B CA  1 
ATOM   830  C  C   . CYS   B 2 71  ? -31.918 2.520   -5.361  1.00 32.52 ? 80  CYS   B C   1 
ATOM   831  O  O   . CYS   B 2 71  ? -33.073 2.257   -5.010  1.00 33.19 ? 80  CYS   B O   1 
ATOM   832  C  CB  . CYS   B 2 71  ? -32.261 4.480   -6.930  1.00 34.83 ? 80  CYS   B CB  1 
ATOM   833  S  SG  . CYS   B 2 71  ? -31.895 6.205   -7.359  1.00 42.05 ? 80  CYS   B SG  1 
ATOM   834  N  N   . GLY   B 2 72  ? -30.959 1.596   -5.455  1.00 30.93 ? 81  GLY   B N   1 
ATOM   835  C  CA  . GLY   B 2 72  ? -31.257 0.201   -5.158  1.00 30.62 ? 81  GLY   B CA  1 
ATOM   836  C  C   . GLY   B 2 72  ? -30.053 -0.694  -5.262  1.00 30.38 ? 81  GLY   B C   1 
ATOM   837  O  O   . GLY   B 2 72  ? -28.952 -0.244  -5.581  1.00 30.18 ? 81  GLY   B O   1 
ATOM   838  N  N   . PRO   B 2 73  ? -30.240 -1.978  -4.942  1.00 30.47 ? 82  PRO   B N   1 
ATOM   839  C  CA  . PRO   B 2 73  ? -29.105 -2.912  -4.994  1.00 30.87 ? 82  PRO   B CA  1 
ATOM   840  C  C   . PRO   B 2 73  ? -28.600 -3.168  -6.412  1.00 31.55 ? 82  PRO   B C   1 
ATOM   841  O  O   . PRO   B 2 73  ? -29.373 -3.051  -7.367  1.00 32.09 ? 82  PRO   B O   1 
ATOM   842  C  CB  . PRO   B 2 73  ? -29.681 -4.185  -4.363  1.00 31.45 ? 82  PRO   B CB  1 
ATOM   843  C  CG  . PRO   B 2 73  ? -31.161 -4.099  -4.620  1.00 31.57 ? 82  PRO   B CG  1 
ATOM   844  C  CD  . PRO   B 2 73  ? -31.482 -2.642  -4.494  1.00 29.66 ? 82  PRO   B CD  1 
ATOM   845  N  N   . TRP   B 2 74  ? -27.321 -3.557  -6.552  1.00 31.67 ? 83  TRP   B N   1 
ATOM   846  C  CA  . TRP   B 2 74  ? -26.683 -3.885  -7.835  1.00 32.70 ? 83  TRP   B CA  1 
ATOM   847  C  C   . TRP   B 2 74  ? -27.558 -4.895  -8.648  1.00 34.23 ? 83  TRP   B C   1 
ATOM   848  O  O   . TRP   B 2 74  ? -27.953 -5.928  -8.109  1.00 34.11 ? 83  TRP   B O   1 
ATOM   849  C  CB  . TRP   B 2 74  ? -25.245 -4.428  -7.585  1.00 32.08 ? 83  TRP   B CB  1 
ATOM   850  C  CG  . TRP   B 2 74  ? -24.429 -4.610  -8.837  1.00 31.83 ? 83  TRP   B CG  1 
ATOM   851  C  CD1 . TRP   B 2 74  ? -24.360 -5.729  -9.611  1.00 32.26 ? 83  TRP   B CD1 1 
ATOM   852  C  CD2 . TRP   B 2 74  ? -23.596 -3.622  -9.482  1.00 31.69 ? 83  TRP   B CD2 1 
ATOM   853  N  NE1 . TRP   B 2 74  ? -23.575 -5.491  -10.718 1.00 32.57 ? 83  TRP   B NE1 1 
ATOM   854  C  CE2 . TRP   B 2 74  ? -23.118 -4.197  -10.680 1.00 32.11 ? 83  TRP   B CE2 1 
ATOM   855  C  CE3 . TRP   B 2 74  ? -23.247 -2.289  -9.185  1.00 31.53 ? 83  TRP   B CE3 1 
ATOM   856  C  CZ2 . TRP   B 2 74  ? -22.264 -3.510  -11.550 1.00 32.30 ? 83  TRP   B CZ2 1 
ATOM   857  C  CZ3 . TRP   B 2 74  ? -22.417 -1.606  -10.055 1.00 31.89 ? 83  TRP   B CZ3 1 
ATOM   858  C  CH2 . TRP   B 2 74  ? -21.956 -2.205  -11.237 1.00 32.08 ? 83  TRP   B CH2 1 
ATOM   859  N  N   . LYS   B 2 75  ? -27.928 -4.558  -9.902  1.00 35.08 ? 84  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 2 75  ? -28.826 -5.417  -10.700 1.00 36.04 ? 84  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 2 75  ? -28.135 -6.238  -11.777 1.00 37.41 ? 84  LYS   B C   1 
ATOM   862  O  O   . LYS   B 2 75  ? -28.696 -7.219  -12.260 1.00 37.79 ? 84  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 2 75  ? -29.918 -4.567  -11.380 1.00 36.60 ? 84  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 2 75  ? -30.755 -3.732  -10.435 1.00 37.36 ? 84  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 2 75  ? -31.776 -4.582  -9.713  1.00 41.36 ? 84  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 2 75  ? -32.628 -3.753  -8.794  1.00 46.43 ? 84  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 2 75  ? -33.595 -4.579  -8.017  1.00 49.53 ? 84  LYS   B NZ  1 
ATOM   868  N  N   . LEU   B 2 76  ? -26.961 -5.809  -12.207 1.00 37.99 ? 85  LEU   B N   1 
ATOM   869  C  CA  . LEU   B 2 76  ? -26.245 -6.441  -13.304 1.00 38.43 ? 85  LEU   B CA  1 
ATOM   870  C  C   . LEU   B 2 76  ? -25.565 -7.738  -12.868 1.00 40.92 ? 85  LEU   B C   1 
ATOM   871  O  O   . LEU   B 2 76  ? -24.713 -7.722  -11.981 1.00 41.26 ? 85  LEU   B O   1 
ATOM   872  C  CB  . LEU   B 2 76  ? -25.226 -5.443  -13.908 1.00 37.55 ? 85  LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 2 76  ? -25.708 -3.979  -14.092 1.00 37.50 ? 85  LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 2 76  ? -24.643 -3.108  -14.685 1.00 37.40 ? 85  LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 2 76  ? -26.947 -3.899  -14.942 1.00 37.37 ? 85  LEU   B CD2 1 
ATOM   876  N  N   . ASP   B 2 77  ? -25.927 -8.860  -13.497 1.00 42.41 ? 86  ASP   B N   1 
ATOM   877  C  CA  . ASP   B 2 77  ? -25.340 -10.150 -13.152 1.00 44.38 ? 86  ASP   B CA  1 
ATOM   878  C  C   . ASP   B 2 77  ? -24.830 -10.973 -14.355 1.00 44.93 ? 86  ASP   B C   1 
ATOM   879  O  O   . ASP   B 2 77  ? -24.453 -12.126 -14.160 1.00 45.64 ? 86  ASP   B O   1 
ATOM   880  C  CB  . ASP   B 2 77  ? -26.310 -10.989 -12.295 1.00 47.88 ? 86  ASP   B CB  1 
ATOM   881  C  CG  . ASP   B 2 77  ? -27.647 -11.300 -12.948 1.00 55.76 ? 86  ASP   B CG  1 
ATOM   882  O  OD1 . ASP   B 2 77  ? -28.022 -10.591 -13.911 1.00 56.93 ? 86  ASP   B OD1 1 
ATOM   883  O  OD2 . ASP   B 2 77  ? -28.327 -12.245 -12.489 1.00 59.06 ? 86  ASP   B OD2 1 
ATOM   884  N  N   . ALA   B 2 78  ? -24.801 -10.406 -15.576 1.00 44.58 ? 87  ALA   B N   1 
ATOM   885  C  CA  . ALA   B 2 78  ? -24.302 -11.150 -16.737 1.00 44.71 ? 87  ALA   B CA  1 
ATOM   886  C  C   . ALA   B 2 78  ? -22.778 -11.328 -16.650 1.00 45.34 ? 87  ALA   B C   1 
ATOM   887  O  O   . ALA   B 2 78  ? -22.082 -10.505 -16.047 1.00 45.60 ? 87  ALA   B O   1 
ATOM   888  C  CB  . ALA   B 2 78  ? -24.703 -10.477 -18.039 1.00 44.22 ? 87  ALA   B CB  1 
ATOM   889  N  N   . ALA   B 2 79  ? -22.268 -12.425 -17.208 1.00 45.21 ? 88  ALA   B N   1 
ATOM   890  C  CA  . ALA   B 2 79  ? -20.847 -12.729 -17.124 1.00 45.78 ? 88  ALA   B CA  1 
ATOM   891  C  C   . ALA   B 2 79  ? -20.238 -13.064 -18.473 1.00 46.55 ? 88  ALA   B C   1 
ATOM   892  O  O   . ALA   B 2 79  ? -20.902 -13.647 -19.318 1.00 46.11 ? 88  ALA   B O   1 
ATOM   893  C  CB  . ALA   B 2 79  ? -20.634 -13.888 -16.168 1.00 45.73 ? 88  ALA   B CB  1 
ATOM   894  N  N   . TRP   B 2 80  ? -18.960 -12.726 -18.665 1.00 47.56 ? 89  TRP   B N   1 
ATOM   895  C  CA  . TRP   B 2 80  ? -18.239 -13.063 -19.883 1.00 49.25 ? 89  TRP   B CA  1 
ATOM   896  C  C   . TRP   B 2 80  ? -18.084 -14.581 -19.926 1.00 50.98 ? 89  TRP   B C   1 
ATOM   897  O  O   . TRP   B 2 80  ? -17.882 -15.199 -18.882 1.00 51.17 ? 89  TRP   B O   1 
ATOM   898  C  CB  . TRP   B 2 80  ? -16.863 -12.386 -19.892 1.00 49.27 ? 89  TRP   B CB  1 
ATOM   899  C  CG  . TRP   B 2 80  ? -16.046 -12.688 -21.114 1.00 49.73 ? 89  TRP   B CG  1 
ATOM   900  C  CD1 . TRP   B 2 80  ? -16.435 -12.564 -22.413 1.00 50.57 ? 89  TRP   B CD1 1 
ATOM   901  C  CD2 . TRP   B 2 80  ? -14.671 -13.093 -21.142 1.00 49.64 ? 89  TRP   B CD2 1 
ATOM   902  N  NE1 . TRP   B 2 80  ? -15.401 -12.921 -23.250 1.00 50.89 ? 89  TRP   B NE1 1 
ATOM   903  C  CE2 . TRP   B 2 80  ? -14.301 -13.229 -22.494 1.00 50.35 ? 89  TRP   B CE2 1 
ATOM   904  C  CE3 . TRP   B 2 80  ? -13.719 -13.361 -20.154 1.00 49.97 ? 89  TRP   B CE3 1 
ATOM   905  C  CZ2 . TRP   B 2 80  ? -13.023 -13.640 -22.881 1.00 50.65 ? 89  TRP   B CZ2 1 
ATOM   906  C  CZ3 . TRP   B 2 80  ? -12.455 -13.772 -20.540 1.00 50.69 ? 89  TRP   B CZ3 1 
ATOM   907  C  CH2 . TRP   B 2 80  ? -12.115 -13.897 -21.887 1.00 50.57 ? 89  TRP   B CH2 1 
ATOM   908  N  N   . ASP   B 2 81  ? -18.278 -15.187 -21.101 1.00 52.04 ? 90  ASP   B N   1 
ATOM   909  C  CA  . ASP   B 2 81  ? -18.207 -16.640 -21.218 1.00 53.49 ? 90  ASP   B CA  1 
ATOM   910  C  C   . ASP   B 2 81  ? -16.764 -17.198 -21.297 1.00 55.25 ? 90  ASP   B C   1 
ATOM   911  O  O   . ASP   B 2 81  ? -16.588 -18.417 -21.311 1.00 55.43 ? 90  ASP   B O   1 
ATOM   912  C  CB  . ASP   B 2 81  ? -19.078 -17.148 -22.388 1.00 54.63 ? 90  ASP   B CB  1 
ATOM   913  C  CG  . ASP   B 2 81  ? -18.606 -16.740 -23.765 1.00 60.85 ? 90  ASP   B CG  1 
ATOM   914  O  OD1 . ASP   B 2 81  ? -17.686 -15.904 -23.855 1.00 62.19 ? 90  ASP   B OD1 1 
ATOM   915  O  OD2 . ASP   B 2 81  ? -19.163 -17.253 -24.763 1.00 64.27 ? 90  ASP   B OD2 1 
ATOM   916  N  N   . GLY   B 2 82  ? -15.766 -16.320 -21.355 1.00 56.17 ? 91  GLY   B N   1 
ATOM   917  C  CA  . GLY   B 2 82  ? -14.369 -16.721 -21.447 1.00 57.46 ? 91  GLY   B CA  1 
ATOM   918  C  C   . GLY   B 2 82  ? -13.916 -17.098 -22.849 1.00 58.76 ? 91  GLY   B C   1 
ATOM   919  O  O   . GLY   B 2 82  ? -12.767 -17.505 -23.032 1.00 58.70 ? 91  GLY   B O   1 
ATOM   920  N  N   . LEU   B 2 83  ? -14.802 -16.968 -23.861 1.00 59.59 ? 92  LEU   B N   1 
ATOM   921  C  CA  . LEU   B 2 83  ? -14.458 -17.353 -25.227 1.00 60.77 ? 92  LEU   B CA  1 
ATOM   922  C  C   . LEU   B 2 83  ? -14.751 -16.295 -26.254 1.00 61.52 ? 92  LEU   B C   1 
ATOM   923  O  O   . LEU   B 2 83  ? -14.018 -16.168 -27.235 1.00 62.47 ? 92  LEU   B O   1 
ATOM   924  C  CB  . LEU   B 2 83  ? -15.261 -18.598 -25.645 1.00 61.60 ? 92  LEU   B CB  1 
ATOM   925  C  CG  . LEU   B 2 83  ? -15.063 -19.888 -24.873 1.00 64.47 ? 92  LEU   B CG  1 
ATOM   926  C  CD1 . LEU   B 2 83  ? -15.872 -20.998 -25.523 1.00 65.59 ? 92  LEU   B CD1 1 
ATOM   927  C  CD2 . LEU   B 2 83  ? -13.612 -20.297 -24.871 1.00 65.21 ? 92  LEU   B CD2 1 
ATOM   928  N  N   . SER   B 2 84  ? -15.896 -15.630 -26.115 1.00 60.84 ? 93  SER   B N   1 
ATOM   929  C  CA  . SER   B 2 84  ? -16.410 -14.723 -27.116 1.00 60.41 ? 93  SER   B CA  1 
ATOM   930  C  C   . SER   B 2 84  ? -15.894 -13.302 -27.050 1.00 59.90 ? 93  SER   B C   1 
ATOM   931  O  O   . SER   B 2 84  ? -15.435 -12.833 -26.000 1.00 60.54 ? 93  SER   B O   1 
ATOM   932  C  CB  . SER   B 2 84  ? -17.937 -14.701 -27.053 1.00 61.84 ? 93  SER   B CB  1 
ATOM   933  O  OG  . SER   B 2 84  ? -18.498 -15.995 -26.928 1.00 63.81 ? 93  SER   B OG  1 
ATOM   934  N  N   . GLU   B 2 85  ? -16.010 -12.603 -28.182 1.00 58.48 ? 94  GLU   B N   1 
ATOM   935  C  CA  . GLU   B 2 85  ? -15.689 -11.192 -28.260 1.00 57.52 ? 94  GLU   B CA  1 
ATOM   936  C  C   . GLU   B 2 85  ? -16.829 -10.411 -27.595 1.00 55.68 ? 94  GLU   B C   1 
ATOM   937  O  O   . GLU   B 2 85  ? -17.959 -10.890 -27.465 1.00 55.93 ? 94  GLU   B O   1 
ATOM   938  C  CB  . GLU   B 2 85  ? -15.485 -10.735 -29.722 1.00 59.62 ? 94  GLU   B CB  1 
ATOM   939  C  CG  . GLU   B 2 85  ? -14.211 -11.286 -30.340 1.00 64.02 ? 94  GLU   B CG  1 
ATOM   940  C  CD  . GLU   B 2 85  ? -13.673 -10.550 -31.552 1.00 68.48 ? 94  GLU   B CD  1 
ATOM   941  O  OE1 . GLU   B 2 85  ? -14.448 -9.812  -32.202 1.00 67.42 ? 94  GLU   B OE1 1 
ATOM   942  O  OE2 . GLU   B 2 85  ? -12.466 -10.709 -31.845 1.00 70.59 ? 94  GLU   B OE2 1 
ATOM   943  N  N   . VAL   B 2 86  ? -16.512 -9.229  -27.119 1.00 53.76 ? 95  VAL   B N   1 
ATOM   944  C  CA  . VAL   B 2 86  ? -17.463 -8.381  -26.409 1.00 51.92 ? 95  VAL   B CA  1 
ATOM   945  C  C   . VAL   B 2 86  ? -17.419 -6.983  -27.020 1.00 50.82 ? 95  VAL   B C   1 
ATOM   946  O  O   . VAL   B 2 86  ? -16.515 -6.681  -27.799 1.00 51.38 ? 95  VAL   B O   1 
ATOM   947  C  CB  . VAL   B 2 86  ? -17.094 -8.341  -24.894 1.00 51.29 ? 95  VAL   B CB  1 
ATOM   948  C  CG1 . VAL   B 2 86  ? -16.929 -9.747  -24.313 1.00 51.22 ? 95  VAL   B CG1 1 
ATOM   949  C  CG2 . VAL   B 2 86  ? -15.832 -7.514  -24.665 1.00 51.29 ? 95  VAL   B CG2 1 
ATOM   950  N  N   . GLN   B 2 87  ? -18.367 -6.115  -26.647 1.00 49.28 ? 96  GLN   B N   1 
ATOM   951  C  CA  . GLN   B 2 87  ? -18.343 -4.739  -27.091 1.00 47.71 ? 96  GLN   B CA  1 
ATOM   952  C  C   . GLN   B 2 87  ? -18.276 -3.771  -25.919 1.00 45.83 ? 96  GLN   B C   1 
ATOM   953  O  O   . GLN   B 2 87  ? -19.064 -3.862  -24.985 1.00 45.55 ? 96  GLN   B O   1 
ATOM   954  C  CB  . GLN   B 2 87  ? -19.532 -4.425  -28.009 1.00 49.02 ? 96  GLN   B CB  1 
ATOM   955  C  CG  . GLN   B 2 87  ? -19.212 -4.745  -29.461 1.00 50.65 ? 96  GLN   B CG  1 
ATOM   956  C  CD  . GLN   B 2 87  ? -20.398 -4.611  -30.369 1.00 52.71 ? 96  GLN   B CD  1 
ATOM   957  O  OE1 . GLN   B 2 87  ? -21.360 -3.875  -30.094 1.00 52.51 ? 96  GLN   B OE1 1 
ATOM   958  N  NE2 . GLN   B 2 87  ? -20.344 -5.323  -31.488 1.00 52.60 ? 96  GLN   B NE2 1 
ATOM   959  N  N   . LEU   B 2 88  ? -17.314 -2.862  -25.959 1.00 44.09 ? 97  LEU   B N   1 
ATOM   960  C  CA  . LEU   B 2 88  ? -17.249 -1.785  -25.001 1.00 42.92 ? 97  LEU   B CA  1 
ATOM   961  C  C   . LEU   B 2 88  ? -18.160 -0.709  -25.615 1.00 41.90 ? 97  LEU   B C   1 
ATOM   962  O  O   . LEU   B 2 88  ? -17.901 -0.266  -26.738 1.00 42.09 ? 97  LEU   B O   1 
ATOM   963  C  CB  . LEU   B 2 88  ? -15.809 -1.246  -24.877 1.00 43.05 ? 97  LEU   B CB  1 
ATOM   964  C  CG  . LEU   B 2 88  ? -15.656 0.137   -24.205 1.00 44.50 ? 97  LEU   B CG  1 
ATOM   965  C  CD1 . LEU   B 2 88  ? -16.274 0.159   -22.812 1.00 44.76 ? 97  LEU   B CD1 1 
ATOM   966  C  CD2 . LEU   B 2 88  ? -14.211 0.574   -24.164 1.00 45.14 ? 97  LEU   B CD2 1 
ATOM   967  N  N   . LEU   B 2 89  ? -19.236 -0.318  -24.922 1.00 40.79 ? 98  LEU   B N   1 
ATOM   968  C  CA  . LEU   B 2 89  ? -20.085 0.763   -25.413 1.00 39.70 ? 98  LEU   B CA  1 
ATOM   969  C  C   . LEU   B 2 89  ? -19.459 1.986   -24.773 1.00 39.95 ? 98  LEU   B C   1 
ATOM   970  O  O   . LEU   B 2 89  ? -19.833 2.378   -23.670 1.00 39.89 ? 98  LEU   B O   1 
ATOM   971  C  CB  . LEU   B 2 89  ? -21.563 0.559   -25.042 1.00 39.24 ? 98  LEU   B CB  1 
ATOM   972  C  CG  . LEU   B 2 89  ? -22.555 1.748   -25.246 1.00 40.51 ? 98  LEU   B CG  1 
ATOM   973  C  CD1 . LEU   B 2 89  ? -22.339 2.478   -26.552 1.00 41.00 ? 98  LEU   B CD1 1 
ATOM   974  C  CD2 . LEU   B 2 89  ? -23.979 1.282   -25.156 1.00 41.14 ? 98  LEU   B CD2 1 
ATOM   975  N  N   . ALA   B 2 90  ? -18.380 2.484   -25.403 1.00 40.19 ? 99  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 90  ? -17.584 3.596   -24.888 1.00 40.33 ? 99  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 90  ? -18.315 4.880   -25.054 1.00 40.25 ? 99  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 90  ? -18.745 5.161   -26.159 1.00 41.16 ? 99  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 90  ? -16.262 3.689   -25.635 1.00 40.14 ? 99  ALA   B CB  1 
ATOM   980  N  N   . VAL   B 2 91  ? -18.418 5.692   -23.990 1.00 39.01 ? 100 VAL   B N   1 
ATOM   981  C  CA  . VAL   B 2 91  ? -19.049 7.005   -24.057 1.00 38.92 ? 100 VAL   B CA  1 
ATOM   982  C  C   . VAL   B 2 91  ? -17.966 8.043   -23.679 1.00 40.20 ? 100 VAL   B C   1 
ATOM   983  O  O   . VAL   B 2 91  ? -17.838 8.412   -22.516 1.00 40.82 ? 100 VAL   B O   1 
ATOM   984  C  CB  . VAL   B 2 91  ? -20.287 7.048   -23.127 1.00 38.52 ? 100 VAL   B CB  1 
ATOM   985  C  CG1 . VAL   B 2 91  ? -20.995 8.407   -23.177 1.00 38.75 ? 100 VAL   B CG1 1 
ATOM   986  C  CG2 . VAL   B 2 91  ? -21.251 5.912   -23.448 1.00 38.07 ? 100 VAL   B CG2 1 
ATOM   987  N  N   . PRO   B 2 92  ? -17.121 8.476   -24.638 1.00 40.78 ? 101 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 92  ? -16.027 9.405   -24.291 1.00 41.10 ? 101 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 92  ? -16.489 10.847  -24.076 1.00 41.45 ? 101 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 92  ? -17.535 11.231  -24.581 1.00 41.32 ? 101 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 92  ? -15.055 9.283   -25.489 1.00 41.78 ? 101 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 92  ? -15.624 8.206   -26.386 1.00 42.16 ? 101 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 92  ? -17.083 8.115   -26.066 1.00 40.48 ? 101 PRO   B CD  1 
ATOM   994  N  N   . PRO   B 2 93  ? -15.731 11.657  -23.317 1.00 41.76 ? 102 PRO   B N   1 
ATOM   995  C  CA  . PRO   B 2 93  ? -16.158 13.046  -23.083 1.00 42.27 ? 102 PRO   B CA  1 
ATOM   996  C  C   . PRO   B 2 93  ? -16.300 13.857  -24.373 1.00 43.51 ? 102 PRO   B C   1 
ATOM   997  O  O   . PRO   B 2 93  ? -15.430 13.815  -25.234 1.00 44.08 ? 102 PRO   B O   1 
ATOM   998  C  CB  . PRO   B 2 93  ? -15.066 13.600  -22.158 1.00 42.66 ? 102 PRO   B CB  1 
ATOM   999  C  CG  . PRO   B 2 93  ? -14.452 12.371  -21.508 1.00 42.91 ? 102 PRO   B CG  1 
ATOM   1000 C  CD  . PRO   B 2 93  ? -14.485 11.340  -22.594 1.00 41.37 ? 102 PRO   B CD  1 
ATOM   1001 N  N   . GLY   B 2 94  ? -17.436 14.536  -24.520 1.00 43.57 ? 103 GLY   B N   1 
ATOM   1002 C  CA  . GLY   B 2 94  ? -17.752 15.360  -25.682 1.00 43.55 ? 103 GLY   B CA  1 
ATOM   1003 C  C   . GLY   B 2 94  ? -17.964 14.602  -26.979 1.00 43.35 ? 103 GLY   B C   1 
ATOM   1004 O  O   . GLY   B 2 94  ? -18.061 15.208  -28.039 1.00 42.64 ? 103 GLY   B O   1 
ATOM   1005 N  N   . GLU   B 2 95  ? -17.977 13.270  -26.922 1.00 43.67 ? 104 GLU   B N   1 
ATOM   1006 C  CA  . GLU   B 2 95  ? -18.107 12.447  -28.118 1.00 44.15 ? 104 GLU   B CA  1 
ATOM   1007 C  C   . GLU   B 2 95  ? -19.286 11.487  -27.962 1.00 45.02 ? 104 GLU   B C   1 
ATOM   1008 O  O   . GLU   B 2 95  ? -19.649 11.136  -26.846 1.00 44.84 ? 104 GLU   B O   1 
ATOM   1009 C  CB  . GLU   B 2 95  ? -16.785 11.686  -28.397 1.00 44.96 ? 104 GLU   B CB  1 
ATOM   1010 C  CG  . GLU   B 2 95  ? -15.570 12.590  -28.609 1.00 48.69 ? 104 GLU   B CG  1 
ATOM   1011 C  CD  . GLU   B 2 95  ? -14.206 11.908  -28.682 1.00 54.37 ? 104 GLU   B CD  1 
ATOM   1012 O  OE1 . GLU   B 2 95  ? -14.143 10.674  -28.478 1.00 54.89 ? 104 GLU   B OE1 1 
ATOM   1013 O  OE2 . GLU   B 2 95  ? -13.196 12.609  -28.935 1.00 55.98 ? 104 GLU   B OE2 1 
ATOM   1014 N  N   . ARG   B 2 96  ? -19.876 11.067  -29.078 1.00 45.93 ? 105 ARG   B N   1 
ATOM   1015 C  CA  . ARG   B 2 96  ? -21.026 10.172  -29.125 1.00 47.85 ? 105 ARG   B CA  1 
ATOM   1016 C  C   . ARG   B 2 96  ? -20.695 8.762   -28.622 1.00 49.20 ? 105 ARG   B C   1 
ATOM   1017 O  O   . ARG   B 2 96  ? -19.539 8.339   -28.717 1.00 49.83 ? 105 ARG   B O   1 
ATOM   1018 C  CB  . ARG   B 2 96  ? -21.524 10.106  -30.581 1.00 50.27 ? 105 ARG   B CB  1 
ATOM   1019 C  CG  . ARG   B 2 96  ? -22.928 9.551   -30.755 1.00 55.25 ? 105 ARG   B CG  1 
ATOM   1020 C  CD  . ARG   B 2 96  ? -23.655 10.202  -31.918 1.00 60.72 ? 105 ARG   B CD  1 
ATOM   1021 N  NE  . ARG   B 2 96  ? -22.966 10.018  -33.196 1.00 64.93 ? 105 ARG   B NE  1 
ATOM   1022 C  CZ  . ARG   B 2 96  ? -22.556 11.012  -33.979 1.00 68.21 ? 105 ARG   B CZ  1 
ATOM   1023 N  NH1 . ARG   B 2 96  ? -22.763 12.278  -33.623 1.00 67.93 ? 105 ARG   B NH1 1 
ATOM   1024 N  NH2 . ARG   B 2 96  ? -21.939 10.751  -35.127 1.00 68.36 ? 105 ARG   B NH2 1 
ATOM   1025 N  N   . ALA   B 2 97  ? -21.710 8.030   -28.100 1.00 49.34 ? 106 ALA   B N   1 
ATOM   1026 C  CA  . ALA   B 2 97  ? -21.592 6.643   -27.644 1.00 50.24 ? 106 ALA   B CA  1 
ATOM   1027 C  C   . ALA   B 2 97  ? -21.149 5.789   -28.837 1.00 51.84 ? 106 ALA   B C   1 
ATOM   1028 O  O   . ALA   B 2 97  ? -21.691 5.933   -29.933 1.00 52.56 ? 106 ALA   B O   1 
ATOM   1029 C  CB  . ALA   B 2 97  ? -22.931 6.150   -27.126 1.00 50.05 ? 106 ALA   B CB  1 
ATOM   1030 N  N   . LYS   B 2 98  ? -20.134 4.956   -28.649 1.00 52.41 ? 107 LYS   B N   1 
ATOM   1031 C  CA  . LYS   B 2 98  ? -19.556 4.182   -29.740 1.00 52.98 ? 107 LYS   B CA  1 
ATOM   1032 C  C   . LYS   B 2 98  ? -19.219 2.754   -29.305 1.00 52.21 ? 107 LYS   B C   1 
ATOM   1033 O  O   . LYS   B 2 98  ? -18.512 2.572   -28.324 1.00 52.31 ? 107 LYS   B O   1 
ATOM   1034 C  CB  . LYS   B 2 98  ? -18.294 4.928   -30.206 1.00 56.04 ? 107 LYS   B CB  1 
ATOM   1035 C  CG  . LYS   B 2 98  ? -17.592 4.388   -31.445 1.00 62.57 ? 107 LYS   B CG  1 
ATOM   1036 C  CD  . LYS   B 2 98  ? -16.240 5.103   -31.681 1.00 69.03 ? 107 LYS   B CD  1 
ATOM   1037 C  CE  . LYS   B 2 98  ? -15.447 5.337   -30.398 1.00 73.97 ? 107 LYS   B CE  1 
ATOM   1038 N  NZ  . LYS   B 2 98  ? -13.982 5.111   -30.567 1.00 76.92 ? 107 LYS   B NZ  1 
ATOM   1039 N  N   . ASN   B 2 99  ? -19.722 1.746   -30.034 1.00 51.54 ? 108 ASN   B N   1 
ATOM   1040 C  CA  . ASN   B 2 99  ? -19.453 0.340   -29.736 1.00 51.81 ? 108 ASN   B CA  1 
ATOM   1041 C  C   . ASN   B 2 99  ? -18.117 -0.078  -30.336 1.00 52.39 ? 108 ASN   B C   1 
ATOM   1042 O  O   . ASN   B 2 99  ? -17.878 0.165   -31.516 1.00 53.16 ? 108 ASN   B O   1 
ATOM   1043 C  CB  . ASN   B 2 99  ? -20.551 -0.560  -30.312 1.00 52.24 ? 108 ASN   B CB  1 
ATOM   1044 C  CG  . ASN   B 2 99  ? -21.894 -0.378  -29.659 1.00 54.43 ? 108 ASN   B CG  1 
ATOM   1045 O  OD1 . ASN   B 2 99  ? -22.535 0.663   -29.789 1.00 55.31 ? 108 ASN   B OD1 1 
ATOM   1046 N  ND2 . ASN   B 2 99  ? -22.363 -1.398  -28.959 1.00 54.64 ? 108 ASN   B ND2 1 
ATOM   1047 N  N   . ILE   B 2 100 ? -17.258 -0.706  -29.543 1.00 51.98 ? 109 ILE   B N   1 
ATOM   1048 C  CA  . ILE   B 2 100 ? -15.959 -1.189  -29.988 1.00 52.30 ? 109 ILE   B CA  1 
ATOM   1049 C  C   . ILE   B 2 100 ? -15.853 -2.672  -29.632 1.00 52.67 ? 109 ILE   B C   1 
ATOM   1050 O  O   . ILE   B 2 100 ? -15.830 -3.020  -28.456 1.00 52.61 ? 109 ILE   B O   1 
ATOM   1051 C  CB  . ILE   B 2 100 ? -14.813 -0.408  -29.312 1.00 52.91 ? 109 ILE   B CB  1 
ATOM   1052 C  CG1 . ILE   B 2 100 ? -14.967 1.109   -29.477 1.00 54.07 ? 109 ILE   B CG1 1 
ATOM   1053 C  CG2 . ILE   B 2 100 ? -13.456 -0.907  -29.791 1.00 53.27 ? 109 ILE   B CG2 1 
ATOM   1054 C  CD1 . ILE   B 2 100 ? -14.756 1.626   -30.902 1.00 55.17 ? 109 ILE   B CD1 1 
ATOM   1055 N  N   . GLN   B 2 101 ? -15.791 -3.543  -30.639 1.00 52.68 ? 110 GLN   B N   1 
ATOM   1056 C  CA  . GLN   B 2 101 ? -15.707 -4.974  -30.417 1.00 53.22 ? 110 GLN   B CA  1 
ATOM   1057 C  C   . GLN   B 2 101 ? -14.258 -5.411  -30.208 1.00 53.60 ? 110 GLN   B C   1 
ATOM   1058 O  O   . GLN   B 2 101 ? -13.356 -4.908  -30.872 1.00 53.85 ? 110 GLN   B O   1 
ATOM   1059 C  CB  . GLN   B 2 101 ? -16.354 -5.723  -31.585 1.00 55.08 ? 110 GLN   B CB  1 
ATOM   1060 C  CG  . GLN   B 2 101 ? -16.361 -7.241  -31.443 1.00 57.73 ? 110 GLN   B CG  1 
ATOM   1061 C  CD  . GLN   B 2 101 ? -17.404 -7.844  -32.351 1.00 60.42 ? 110 GLN   B CD  1 
ATOM   1062 O  OE1 . GLN   B 2 101 ? -18.494 -7.288  -32.537 1.00 60.23 ? 110 GLN   B OE1 1 
ATOM   1063 N  NE2 . GLN   B 2 101 ? -17.093 -8.990  -32.930 1.00 60.81 ? 110 GLN   B NE2 1 
ATOM   1064 N  N   . THR   B 2 102 ? -14.023 -6.298  -29.242 1.00 53.52 ? 111 THR   B N   1 
ATOM   1065 C  CA  . THR   B 2 102 ? -12.677 -6.783  -28.950 1.00 54.08 ? 111 THR   B CA  1 
ATOM   1066 C  C   . THR   B 2 102 ? -12.737 -8.155  -28.313 1.00 54.29 ? 111 THR   B C   1 
ATOM   1067 O  O   . THR   B 2 102 ? -13.782 -8.533  -27.794 1.00 54.51 ? 111 THR   B O   1 
ATOM   1068 C  CB  . THR   B 2 102 ? -11.940 -5.787  -28.017 1.00 56.00 ? 111 THR   B CB  1 
ATOM   1069 O  OG1 . THR   B 2 102 ? -10.563 -6.164  -27.910 1.00 57.71 ? 111 THR   B OG1 1 
ATOM   1070 C  CG2 . THR   B 2 102 ? -12.576 -5.669  -26.636 1.00 56.37 ? 111 THR   B CG2 1 
ATOM   1071 N  N   . LEU   B 2 103 ? -11.619 -8.906  -28.334 1.00 54.36 ? 112 LEU   B N   1 
ATOM   1072 C  CA  . LEU   B 2 103 ? -11.575 -10.174 -27.631 1.00 54.87 ? 112 LEU   B CA  1 
ATOM   1073 C  C   . LEU   B 2 103 ? -10.833 -9.885  -26.339 1.00 55.19 ? 112 LEU   B C   1 
ATOM   1074 O  O   . LEU   B 2 103 ? -9.670  -9.450  -26.364 1.00 55.46 ? 112 LEU   B O   1 
ATOM   1075 C  CB  . LEU   B 2 103 ? -10.865 -11.294 -28.401 1.00 55.45 ? 112 LEU   B CB  1 
ATOM   1076 C  CG  . LEU   B 2 103 ? -10.893 -12.604 -27.615 1.00 57.45 ? 112 LEU   B CG  1 
ATOM   1077 C  CD1 . LEU   B 2 103 ? -12.247 -13.252 -27.703 1.00 58.50 ? 112 LEU   B CD1 1 
ATOM   1078 C  CD2 . LEU   B 2 103 ? -9.822  -13.541 -28.054 1.00 58.16 ? 112 LEU   B CD2 1 
ATOM   1079 N  N   . PRO   B 2 104 ? -11.488 -10.094 -25.192 1.00 54.72 ? 113 PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 2 104 ? -10.818 -9.789  -23.928 1.00 54.74 ? 113 PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 2 104 ? -9.720  -10.780 -23.608 1.00 55.47 ? 113 PRO   B C   1 
ATOM   1082 O  O   . PRO   B 2 104 ? -9.825  -11.963 -23.935 1.00 55.77 ? 113 PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 2 104 ? -11.941 -9.867  -22.883 1.00 55.04 ? 113 PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 2 104 ? -13.220 -9.960  -23.668 1.00 55.58 ? 113 PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 2 104 ? -12.864 -10.576 -24.984 1.00 53.97 ? 113 PRO   B CD  1 
ATOM   1086 N  N   . GLY   B 2 105 ? -8.683  -10.271 -22.957 1.00 55.25 ? 114 GLY   B N   1 
ATOM   1087 C  CA  . GLY   B 2 105 ? -7.609  -11.059 -22.385 1.00 55.18 ? 114 GLY   B CA  1 
ATOM   1088 C  C   . GLY   B 2 105 ? -8.044  -11.538 -21.011 1.00 55.02 ? 114 GLY   B C   1 
ATOM   1089 O  O   . GLY   B 2 105 ? -9.247  -11.619 -20.725 1.00 55.19 ? 114 GLY   B O   1 
ATOM   1090 N  N   . ILE   B 2 106 ? -7.077  -11.846 -20.136 1.00 54.32 ? 115 ILE   B N   1 
ATOM   1091 C  CA  . ILE   B 2 106 ? -7.348  -12.376 -18.805 1.00 54.24 ? 115 ILE   B CA  1 
ATOM   1092 C  C   . ILE   B 2 106 ? -6.425  -11.740 -17.780 1.00 53.66 ? 115 ILE   B C   1 
ATOM   1093 O  O   . ILE   B 2 106 ? -5.222  -11.679 -18.007 1.00 54.65 ? 115 ILE   B O   1 
ATOM   1094 C  CB  . ILE   B 2 106 ? -7.028  -13.904 -18.793 1.00 55.85 ? 115 ILE   B CB  1 
ATOM   1095 C  CG1 . ILE   B 2 106 ? -7.788  -14.704 -19.867 1.00 58.29 ? 115 ILE   B CG1 1 
ATOM   1096 C  CG2 . ILE   B 2 106 ? -7.220  -14.511 -17.429 1.00 56.52 ? 115 ILE   B CG2 1 
ATOM   1097 C  CD1 . ILE   B 2 106 ? -9.212  -14.892 -19.622 1.00 60.37 ? 115 ILE   B CD1 1 
ATOM   1098 N  N   . PHE   B 2 107 ? -6.956  -11.375 -16.609 1.00 51.93 ? 116 PHE   B N   1 
ATOM   1099 C  CA  . PHE   B 2 107 ? -6.169  -10.968 -15.457 1.00 50.76 ? 116 PHE   B CA  1 
ATOM   1100 C  C   . PHE   B 2 107 ? -6.112  -12.225 -14.609 1.00 50.29 ? 116 PHE   B C   1 
ATOM   1101 O  O   . PHE   B 2 107 ? -7.161  -12.748 -14.249 1.00 49.78 ? 116 PHE   B O   1 
ATOM   1102 C  CB  . PHE   B 2 107 ? -6.889  -9.888  -14.625 1.00 49.97 ? 116 PHE   B CB  1 
ATOM   1103 C  CG  . PHE   B 2 107 ? -6.682  -8.449  -15.032 1.00 49.42 ? 116 PHE   B CG  1 
ATOM   1104 C  CD1 . PHE   B 2 107 ? -5.979  -8.129  -16.184 1.00 49.47 ? 116 PHE   B CD1 1 
ATOM   1105 C  CD2 . PHE   B 2 107 ? -7.184  -7.417  -14.259 1.00 49.40 ? 116 PHE   B CD2 1 
ATOM   1106 C  CE1 . PHE   B 2 107 ? -5.787  -6.805  -16.554 1.00 49.90 ? 116 PHE   B CE1 1 
ATOM   1107 C  CE2 . PHE   B 2 107 ? -6.989  -6.096  -14.630 1.00 50.08 ? 116 PHE   B CE2 1 
ATOM   1108 C  CZ  . PHE   B 2 107 ? -6.313  -5.798  -15.787 1.00 49.86 ? 116 PHE   B CZ  1 
ATOM   1109 N  N   . LYS   B 2 108 ? -4.915  -12.731 -14.304 1.00 50.55 ? 117 LYS   B N   1 
ATOM   1110 C  CA  . LYS   B 2 108 ? -4.779  -13.901 -13.444 1.00 51.43 ? 117 LYS   B CA  1 
ATOM   1111 C  C   . LYS   B 2 108 ? -4.459  -13.364 -12.063 1.00 50.71 ? 117 LYS   B C   1 
ATOM   1112 O  O   . LYS   B 2 108 ? -3.455  -12.676 -11.917 1.00 50.67 ? 117 LYS   B O   1 
ATOM   1113 C  CB  . LYS   B 2 108 ? -3.646  -14.829 -13.937 1.00 54.94 ? 117 LYS   B CB  1 
ATOM   1114 C  CG  . LYS   B 2 108 ? -3.783  -15.223 -15.413 1.00 61.66 ? 117 LYS   B CG  1 
ATOM   1115 C  CD  . LYS   B 2 108 ? -2.613  -16.102 -15.913 1.00 68.95 ? 117 LYS   B CD  1 
ATOM   1116 C  CE  . LYS   B 2 108 ? -2.675  -16.329 -17.416 1.00 75.21 ? 117 LYS   B CE  1 
ATOM   1117 N  NZ  . LYS   B 2 108 ? -1.536  -17.146 -17.943 1.00 78.12 ? 117 LYS   B NZ  1 
ATOM   1118 N  N   . THR   B 2 109 ? -5.335  -13.601 -11.067 1.00 50.23 ? 118 THR   B N   1 
ATOM   1119 C  CA  . THR   B 2 109 ? -5.123  -13.140 -9.680  1.00 50.37 ? 118 THR   B CA  1 
ATOM   1120 C  C   . THR   B 2 109 ? -5.034  -14.340 -8.696  1.00 50.37 ? 118 THR   B C   1 
ATOM   1121 O  O   . THR   B 2 109 ? -5.359  -15.466 -9.072  1.00 50.15 ? 118 THR   B O   1 
ATOM   1122 C  CB  . THR   B 2 109 ? -6.206  -12.088 -9.218  1.00 51.29 ? 118 THR   B CB  1 
ATOM   1123 O  OG1 . THR   B 2 109 ? -7.386  -12.735 -8.743  1.00 52.30 ? 118 THR   B OG1 1 
ATOM   1124 C  CG2 . THR   B 2 109 ? -6.557  -11.064 -10.273 1.00 51.18 ? 118 THR   B CG2 1 
ATOM   1125 N  N   . LYS   B 2 110 ? -4.630  -14.094 -7.437  1.00 50.60 ? 119 LYS   B N   1 
ATOM   1126 C  CA  . LYS   B 2 110 ? -4.579  -15.145 -6.406  1.00 51.35 ? 119 LYS   B CA  1 
ATOM   1127 C  C   . LYS   B 2 110 ? -5.997  -15.675 -6.040  1.00 52.61 ? 119 LYS   B C   1 
ATOM   1128 O  O   . LYS   B 2 110 ? -6.121  -16.762 -5.467  1.00 53.02 ? 119 LYS   B O   1 
ATOM   1129 C  CB  . LYS   B 2 110 ? -3.818  -14.661 -5.148  1.00 51.41 ? 119 LYS   B CB  1 
ATOM   1130 C  CG  . LYS   B 2 110 ? -4.644  -13.803 -4.186  1.00 54.51 ? 119 LYS   B CG  1 
ATOM   1131 C  CD  . LYS   B 2 110 ? -3.791  -13.137 -3.104  1.00 57.69 ? 119 LYS   B CD  1 
ATOM   1132 C  CE  . LYS   B 2 110 ? -4.588  -12.639 -1.913  1.00 60.74 ? 119 LYS   B CE  1 
ATOM   1133 N  NZ  . LYS   B 2 110 ? -5.531  -11.553 -2.284  1.00 62.31 ? 119 LYS   B NZ  1 
ATOM   1134 N  N   . ASP   B 2 111 ? -7.046  -14.900 -6.369  1.00 52.78 ? 120 ASP   B N   1 
ATOM   1135 C  CA  . ASP   B 2 111 ? -8.434  -15.236 -6.099  1.00 53.68 ? 120 ASP   B CA  1 
ATOM   1136 C  C   . ASP   B 2 111 ? -9.231  -15.644 -7.343  1.00 54.77 ? 120 ASP   B C   1 
ATOM   1137 O  O   . ASP   B 2 111 ? -10.449 -15.741 -7.261  1.00 55.48 ? 120 ASP   B O   1 
ATOM   1138 C  CB  . ASP   B 2 111 ? -9.134  -14.053 -5.412  1.00 55.21 ? 120 ASP   B CB  1 
ATOM   1139 C  CG  . ASP   B 2 111 ? -8.494  -13.650 -4.105  1.00 59.24 ? 120 ASP   B CG  1 
ATOM   1140 O  OD1 . ASP   B 2 111 ? -8.266  -14.541 -3.259  1.00 59.78 ? 120 ASP   B OD1 1 
ATOM   1141 O  OD2 . ASP   B 2 111 ? -8.222  -12.446 -3.927  1.00 61.57 ? 120 ASP   B OD2 1 
ATOM   1142 N  N   . GLY   B 2 112 ? -8.567  -15.860 -8.476  1.00 54.83 ? 121 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 112 ? -9.242  -16.279 -9.695  1.00 55.28 ? 121 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 112 ? -8.990  -15.392 -10.895 1.00 55.55 ? 121 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 112 ? -8.376  -14.329 -10.776 1.00 55.73 ? 121 GLY   B O   1 
ATOM   1146 N  N   . ASP   B 2 113 ? -9.482  -15.815 -12.063 1.00 55.19 ? 122 ASP   B N   1 
ATOM   1147 C  CA  . ASP   B 2 113 ? -9.298  -15.048 -13.285 1.00 55.35 ? 122 ASP   B CA  1 
ATOM   1148 C  C   . ASP   B 2 113 ? -10.479 -14.119 -13.601 1.00 54.88 ? 122 ASP   B C   1 
ATOM   1149 O  O   . ASP   B 2 113 ? -11.635 -14.421 -13.293 1.00 55.27 ? 122 ASP   B O   1 
ATOM   1150 C  CB  . ASP   B 2 113 ? -8.986  -15.964 -14.477 1.00 57.71 ? 122 ASP   B CB  1 
ATOM   1151 C  CG  . ASP   B 2 113 ? -7.743  -16.825 -14.317 1.00 64.40 ? 122 ASP   B CG  1 
ATOM   1152 O  OD1 . ASP   B 2 113 ? -6.995  -16.620 -13.331 1.00 65.75 ? 122 ASP   B OD1 1 
ATOM   1153 O  OD2 . ASP   B 2 113 ? -7.523  -17.710 -15.170 1.00 67.53 ? 122 ASP   B OD2 1 
ATOM   1154 N  N   . ILE   B 2 114 ? -10.168 -12.974 -14.210 1.00 53.36 ? 123 ILE   B N   1 
ATOM   1155 C  CA  . ILE   B 2 114 ? -11.151 -11.970 -14.589 1.00 52.72 ? 123 ILE   B CA  1 
ATOM   1156 C  C   . ILE   B 2 114 ? -10.855 -11.549 -16.020 1.00 50.69 ? 123 ILE   B C   1 
ATOM   1157 O  O   . ILE   B 2 114 ? -9.692  -11.380 -16.367 1.00 49.89 ? 123 ILE   B O   1 
ATOM   1158 C  CB  . ILE   B 2 114 ? -11.066 -10.741 -13.628 1.00 53.69 ? 123 ILE   B CB  1 
ATOM   1159 C  CG1 . ILE   B 2 114 ? -11.159 -11.168 -12.162 1.00 55.36 ? 123 ILE   B CG1 1 
ATOM   1160 C  CG2 . ILE   B 2 114 ? -12.121 -9.692  -13.953 1.00 54.08 ? 123 ILE   B CG2 1 
ATOM   1161 C  CD1 . ILE   B 2 114 ? -10.855 -10.056 -11.157 1.00 57.43 ? 123 ILE   B CD1 1 
ATOM   1162 N  N   . GLY   B 2 115 ? -11.895 -11.362 -16.835 1.00 49.51 ? 124 GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 2 115 ? -11.714 -10.893 -18.206 1.00 48.96 ? 124 GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 2 115 ? -11.161 -9.479  -18.217 1.00 48.47 ? 124 GLY   B C   1 
ATOM   1165 O  O   . GLY   B 2 115 ? -11.307 -8.751  -17.229 1.00 48.35 ? 124 GLY   B O   1 
ATOM   1166 N  N   . ALA   B 2 116 ? -10.460 -9.099  -19.286 1.00 48.04 ? 125 ALA   B N   1 
ATOM   1167 C  CA  . ALA   B 2 116 ? -9.885  -7.760  -19.371 1.00 48.34 ? 125 ALA   B CA  1 
ATOM   1168 C  C   . ALA   B 2 116 ? -9.853  -7.218  -20.795 1.00 49.14 ? 125 ALA   B C   1 
ATOM   1169 O  O   . ALA   B 2 116 ? -9.433  -7.903  -21.708 1.00 50.13 ? 125 ALA   B O   1 
ATOM   1170 C  CB  . ALA   B 2 116 ? -8.499  -7.735  -18.754 1.00 47.99 ? 125 ALA   B CB  1 
ATOM   1171 N  N   . VAL   B 2 117 ? -10.288 -5.987  -20.981 1.00 49.01 ? 126 VAL   B N   1 
ATOM   1172 C  CA  A VAL   B 2 117 ? -10.293 -5.368  -22.306 0.50 49.60 ? 126 VAL   B CA  1 
ATOM   1173 C  CA  B VAL   B 2 117 ? -10.337 -5.336  -22.274 0.50 49.68 ? 126 VAL   B CA  1 
ATOM   1174 C  C   . VAL   B 2 117 ? -9.106  -4.414  -22.459 1.00 50.68 ? 126 VAL   B C   1 
ATOM   1175 O  O   . VAL   B 2 117 ? -8.785  -3.638  -21.553 1.00 50.89 ? 126 VAL   B O   1 
ATOM   1176 C  CB  A VAL   B 2 117 ? -11.644 -4.744  -22.721 0.50 49.64 ? 126 VAL   B CB  1 
ATOM   1177 C  CB  B VAL   B 2 117 ? -11.712 -4.627  -22.358 0.50 49.87 ? 126 VAL   B CB  1 
ATOM   1178 C  CG1 A VAL   B 2 117 ? -12.727 -5.816  -22.783 0.50 49.80 ? 126 VAL   B CG1 1 
ATOM   1179 C  CG1 B VAL   B 2 117 ? -11.663 -3.317  -23.118 0.50 50.33 ? 126 VAL   B CG1 1 
ATOM   1180 C  CG2 A VAL   B 2 117 ? -12.053 -3.609  -21.791 0.50 50.03 ? 126 VAL   B CG2 1 
ATOM   1181 C  CG2 B VAL   B 2 117 ? -12.774 -5.567  -22.913 0.50 50.03 ? 126 VAL   B CG2 1 
ATOM   1182 N  N   . ALA   B 2 118 ? -8.383  -4.539  -23.591 1.00 51.20 ? 127 ALA   B N   1 
ATOM   1183 C  CA  . ALA   B 2 118 ? -7.205  -3.707  -23.823 1.00 52.60 ? 127 ALA   B CA  1 
ATOM   1184 C  C   . ALA   B 2 118 ? -7.550  -2.542  -24.751 1.00 54.28 ? 127 ALA   B C   1 
ATOM   1185 O  O   . ALA   B 2 118 ? -7.184  -2.537  -25.919 1.00 55.28 ? 127 ALA   B O   1 
ATOM   1186 C  CB  . ALA   B 2 118 ? -6.074  -4.541  -24.399 1.00 52.88 ? 127 ALA   B CB  1 
ATOM   1187 N  N   . LEU   B 2 119 ? -8.304  -1.572  -24.237 1.00 54.39 ? 128 LEU   B N   1 
ATOM   1188 C  CA  . LEU   B 2 119 ? -8.734  -0.414  -24.996 1.00 55.00 ? 128 LEU   B CA  1 
ATOM   1189 C  C   . LEU   B 2 119 ? -8.395  0.841   -24.188 1.00 55.49 ? 128 LEU   B C   1 
ATOM   1190 O  O   . LEU   B 2 119 ? -8.688  0.892   -22.991 1.00 55.78 ? 128 LEU   B O   1 
ATOM   1191 C  CB  . LEU   B 2 119 ? -10.247 -0.512  -25.242 1.00 55.41 ? 128 LEU   B CB  1 
ATOM   1192 C  CG  . LEU   B 2 119 ? -10.678 -1.626  -26.195 1.00 56.73 ? 128 LEU   B CG  1 
ATOM   1193 C  CD1 . LEU   B 2 119 ? -12.183 -1.797  -26.197 1.00 56.97 ? 128 LEU   B CD1 1 
ATOM   1194 C  CD2 . LEU   B 2 119 ? -10.198 -1.349  -27.591 1.00 57.66 ? 128 LEU   B CD2 1 
ATOM   1195 N  N   . ASP   B 2 120 ? -7.754  1.839   -24.816 1.00 55.30 ? 129 ASP   B N   1 
ATOM   1196 C  CA  . ASP   B 2 120 ? -7.354  3.046   -24.090 1.00 55.55 ? 129 ASP   B CA  1 
ATOM   1197 C  C   . ASP   B 2 120 ? -8.261  4.247   -24.384 1.00 54.11 ? 129 ASP   B C   1 
ATOM   1198 O  O   . ASP   B 2 120 ? -8.491  4.575   -25.538 1.00 54.39 ? 129 ASP   B O   1 
ATOM   1199 C  CB  . ASP   B 2 120 ? -5.868  3.363   -24.335 1.00 58.81 ? 129 ASP   B CB  1 
ATOM   1200 C  CG  . ASP   B 2 120 ? -5.232  4.250   -23.272 1.00 65.43 ? 129 ASP   B CG  1 
ATOM   1201 O  OD1 . ASP   B 2 120 ? -5.523  5.476   -23.263 1.00 67.24 ? 129 ASP   B OD1 1 
ATOM   1202 O  OD2 . ASP   B 2 120 ? -4.431  3.728   -22.465 1.00 67.12 ? 129 ASP   B OD2 1 
ATOM   1203 N  N   . TYR   B 2 121 ? -8.781  4.898   -23.338 1.00 52.69 ? 130 TYR   B N   1 
ATOM   1204 C  CA  . TYR   B 2 121 ? -9.712  6.027   -23.476 1.00 51.62 ? 130 TYR   B CA  1 
ATOM   1205 C  C   . TYR   B 2 121 ? -9.467  7.107   -22.407 1.00 50.09 ? 130 TYR   B C   1 
ATOM   1206 O  O   . TYR   B 2 121 ? -8.886  6.789   -21.372 1.00 50.12 ? 130 TYR   B O   1 
ATOM   1207 C  CB  . TYR   B 2 121 ? -11.153 5.495   -23.333 1.00 51.77 ? 130 TYR   B CB  1 
ATOM   1208 C  CG  . TYR   B 2 121 ? -11.754 5.000   -24.628 1.00 52.86 ? 130 TYR   B CG  1 
ATOM   1209 C  CD1 . TYR   B 2 121 ? -12.475 5.851   -25.451 1.00 53.85 ? 130 TYR   B CD1 1 
ATOM   1210 C  CD2 . TYR   B 2 121 ? -11.616 3.676   -25.022 1.00 53.90 ? 130 TYR   B CD2 1 
ATOM   1211 C  CE1 . TYR   B 2 121 ? -13.017 5.408   -26.649 1.00 55.06 ? 130 TYR   B CE1 1 
ATOM   1212 C  CE2 . TYR   B 2 121 ? -12.143 3.223   -26.225 1.00 55.02 ? 130 TYR   B CE2 1 
ATOM   1213 C  CZ  . TYR   B 2 121 ? -12.845 4.094   -27.035 1.00 56.08 ? 130 TYR   B CZ  1 
ATOM   1214 O  OH  . TYR   B 2 121 ? -13.390 3.662   -28.216 1.00 58.08 ? 130 TYR   B OH  1 
ATOM   1215 N  N   . PRO   B 2 122 ? -9.962  8.368   -22.568 1.00 48.93 ? 131 PRO   B N   1 
ATOM   1216 C  CA  . PRO   B 2 122 ? -9.802  9.360   -21.478 1.00 48.14 ? 131 PRO   B CA  1 
ATOM   1217 C  C   . PRO   B 2 122 ? -10.443 8.847   -20.182 1.00 47.08 ? 131 PRO   B C   1 
ATOM   1218 O  O   . PRO   B 2 122 ? -11.464 8.177   -20.263 1.00 47.38 ? 131 PRO   B O   1 
ATOM   1219 C  CB  . PRO   B 2 122 ? -10.531 10.603  -22.013 1.00 48.75 ? 131 PRO   B CB  1 
ATOM   1220 C  CG  . PRO   B 2 122 ? -10.565 10.423  -23.515 1.00 49.22 ? 131 PRO   B CG  1 
ATOM   1221 C  CD  . PRO   B 2 122 ? -10.711 8.939   -23.709 1.00 48.04 ? 131 PRO   B CD  1 
ATOM   1222 N  N   . ALA   B 2 123 ? -9.816  9.070   -19.009 1.00 45.57 ? 132 ALA   B N   1 
ATOM   1223 C  CA  . ALA   B 2 123 ? -10.313 8.535   -17.732 1.00 44.21 ? 132 ALA   B CA  1 
ATOM   1224 C  C   . ALA   B 2 123 ? -11.819 8.806   -17.459 1.00 42.49 ? 132 ALA   B C   1 
ATOM   1225 O  O   . ALA   B 2 123 ? -12.481 7.971   -16.835 1.00 42.10 ? 132 ALA   B O   1 
ATOM   1226 C  CB  . ALA   B 2 123 ? -9.445  9.014   -16.577 1.00 44.28 ? 132 ALA   B CB  1 
ATOM   1227 N  N   . GLY   B 2 124 ? -12.361 9.900   -18.017 1.00 41.20 ? 133 GLY   B N   1 
ATOM   1228 C  CA  . GLY   B 2 124 ? -13.785 10.227  -17.932 1.00 39.56 ? 133 GLY   B CA  1 
ATOM   1229 C  C   . GLY   B 2 124 ? -14.695 9.247   -18.664 1.00 38.11 ? 133 GLY   B C   1 
ATOM   1230 O  O   . GLY   B 2 124 ? -15.908 9.427   -18.685 1.00 37.81 ? 133 GLY   B O   1 
ATOM   1231 N  N   . THR   B 2 125 ? -14.122 8.207   -19.294 1.00 37.45 ? 134 THR   B N   1 
ATOM   1232 C  CA  . THR   B 2 125 ? -14.850 7.129   -19.970 1.00 37.50 ? 134 THR   B CA  1 
ATOM   1233 C  C   . THR   B 2 125 ? -15.149 5.967   -18.955 1.00 36.41 ? 134 THR   B C   1 
ATOM   1234 O  O   . THR   B 2 125 ? -15.954 5.101   -19.269 1.00 35.90 ? 134 THR   B O   1 
ATOM   1235 C  CB  . THR   B 2 125 ? -14.072 6.670   -21.241 1.00 39.70 ? 134 THR   B CB  1 
ATOM   1236 O  OG1 . THR   B 2 125 ? -13.767 7.799   -22.062 1.00 40.87 ? 134 THR   B OG1 1 
ATOM   1237 C  CG2 . THR   B 2 125 ? -14.810 5.629   -22.080 1.00 40.03 ? 134 THR   B CG2 1 
ATOM   1238 N  N   . SER   B 2 126 ? -14.508 5.959   -17.744 1.00 35.92 ? 135 SER   B N   1 
ATOM   1239 C  CA  . SER   B 2 126 ? -14.709 4.940   -16.695 1.00 36.09 ? 135 SER   B CA  1 
ATOM   1240 C  C   . SER   B 2 126 ? -16.196 4.851   -16.328 1.00 35.74 ? 135 SER   B C   1 
ATOM   1241 O  O   . SER   B 2 126 ? -16.845 5.881   -16.185 1.00 35.04 ? 135 SER   B O   1 
ATOM   1242 C  CB  . SER   B 2 126 ? -13.912 5.285   -15.441 1.00 37.70 ? 135 SER   B CB  1 
ATOM   1243 O  OG  . SER   B 2 126 ? -12.531 5.484   -15.700 1.00 40.19 ? 135 SER   B OG  1 
ATOM   1244 N  N   . GLY   B 2 127 ? -16.717 3.632   -16.250 1.00 35.26 ? 136 GLY   B N   1 
ATOM   1245 C  CA  . GLY   B 2 127 ? -18.123 3.364   -15.997 1.00 35.77 ? 136 GLY   B CA  1 
ATOM   1246 C  C   . GLY   B 2 127 ? -18.875 2.900   -17.234 1.00 36.34 ? 136 GLY   B C   1 
ATOM   1247 O  O   . GLY   B 2 127 ? -20.021 2.454   -17.129 1.00 36.49 ? 136 GLY   B O   1 
ATOM   1248 N  N   . SER   B 2 128 ? -18.261 3.048   -18.435 1.00 36.40 ? 137 SER   B N   1 
ATOM   1249 C  CA  . SER   B 2 128 ? -18.848 2.607   -19.696 1.00 36.49 ? 137 SER   B CA  1 
ATOM   1250 C  C   . SER   B 2 128 ? -19.074 1.091   -19.645 1.00 36.79 ? 137 SER   B C   1 
ATOM   1251 O  O   . SER   B 2 128 ? -18.200 0.342   -19.198 1.00 36.50 ? 137 SER   B O   1 
ATOM   1252 C  CB  . SER   B 2 128 ? -17.934 2.960   -20.873 1.00 37.71 ? 137 SER   B CB  1 
ATOM   1253 O  OG  . SER   B 2 128 ? -17.821 4.360   -21.077 1.00 39.08 ? 137 SER   B OG  1 
ATOM   1254 N  N   . PRO   B 2 129 ? -20.258 0.630   -20.072 1.00 36.91 ? 138 PRO   B N   1 
ATOM   1255 C  CA  . PRO   B 2 129 ? -20.542 -0.812  -20.004 1.00 37.06 ? 138 PRO   B CA  1 
ATOM   1256 C  C   . PRO   B 2 129 ? -19.919 -1.686  -21.089 1.00 38.26 ? 138 PRO   B C   1 
ATOM   1257 O  O   . PRO   B 2 129 ? -19.845 -1.324  -22.264 1.00 37.63 ? 138 PRO   B O   1 
ATOM   1258 C  CB  . PRO   B 2 129 ? -22.066 -0.876  -20.097 1.00 37.49 ? 138 PRO   B CB  1 
ATOM   1259 C  CG  . PRO   B 2 129 ? -22.449 0.360   -20.893 1.00 37.89 ? 138 PRO   B CG  1 
ATOM   1260 C  CD  . PRO   B 2 129 ? -21.415 1.409   -20.570 1.00 36.29 ? 138 PRO   B CD  1 
ATOM   1261 N  N   . ILE   B 2 130 ? -19.526 -2.891  -20.682 1.00 39.24 ? 139 ILE   B N   1 
ATOM   1262 C  CA  . ILE   B 2 130 ? -19.021 -3.906  -21.593 1.00 39.65 ? 139 ILE   B CA  1 
ATOM   1263 C  C   . ILE   B 2 130 ? -20.188 -4.878  -21.798 1.00 40.49 ? 139 ILE   B C   1 
ATOM   1264 O  O   . ILE   B 2 130 ? -20.866 -5.244  -20.836 1.00 40.52 ? 139 ILE   B O   1 
ATOM   1265 C  CB  . ILE   B 2 130 ? -17.761 -4.564  -21.029 1.00 39.99 ? 139 ILE   B CB  1 
ATOM   1266 C  CG1 . ILE   B 2 130 ? -16.631 -3.521  -20.912 1.00 41.10 ? 139 ILE   B CG1 1 
ATOM   1267 C  CG2 . ILE   B 2 130 ? -17.339 -5.751  -21.884 1.00 40.36 ? 139 ILE   B CG2 1 
ATOM   1268 C  CD1 . ILE   B 2 130 ? -15.453 -3.970  -20.044 1.00 42.25 ? 139 ILE   B CD1 1 
ATOM   1269 N  N   . LEU   B 2 131 ? -20.484 -5.218  -23.058 1.00 41.06 ? 140 LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 131 ? -21.652 -6.017  -23.392 1.00 42.56 ? 140 LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 131 ? -21.346 -7.331  -24.023 1.00 44.97 ? 140 LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 131 ? -20.350 -7.457  -24.730 1.00 46.43 ? 140 LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 131 ? -22.508 -5.255  -24.413 1.00 42.47 ? 140 LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 131 ? -22.699 -3.772  -24.230 1.00 43.23 ? 140 LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 131 ? -23.471 -3.206  -25.394 1.00 43.34 ? 140 LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 131 ? -23.350 -3.479  -22.905 1.00 43.56 ? 140 LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 132 ? -22.266 -8.288  -23.881 1.00 45.73 ? 141 ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 132 ? -22.152 -9.551  -24.602 1.00 47.03 ? 141 ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 132 ? -23.009 -9.467  -25.898 1.00 49.35 ? 141 ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 132 ? -23.698 -8.457  -26.112 1.00 49.78 ? 141 ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 132 ? -22.491 -10.756 -23.705 1.00 46.64 ? 141 ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 132 ? -23.911 -10.868 -23.187 1.00 47.35 ? 141 ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 132 ? -24.778 -10.118 -23.657 1.00 45.22 ? 141 ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 132 ? -24.153 -11.729 -22.327 1.00 50.01 ? 141 ASP   B OD2 1 
ATOM   1285 N  N   . LYS   B 2 133 ? -22.985 -10.508 -26.751 1.00 50.53 ? 142 LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 2 133 ? -23.727 -10.516 -28.020 1.00 52.17 ? 142 LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 2 133 ? -25.250 -10.336 -27.833 1.00 52.53 ? 142 LYS   B C   1 
ATOM   1288 O  O   . LYS   B 2 133 ? -25.940 -9.987  -28.792 1.00 52.41 ? 142 LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 2 133 ? -23.393 -11.765 -28.872 1.00 55.77 ? 142 LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 2 133 ? -21.909 -12.189 -28.775 1.00 62.46 ? 142 LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 2 133 ? -21.476 -13.268 -29.788 1.00 68.46 ? 142 LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 2 133 ? -19.991 -13.547 -29.654 1.00 72.98 ? 142 LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 2 133 ? -19.561 -14.815 -30.325 1.00 75.38 ? 142 LYS   B NZ  1 
ATOM   1294 N  N   . CYS   B 2 134 ? -25.763 -10.497 -26.598 1.00 52.51 ? 143 CYS   B N   1 
ATOM   1295 C  CA  . CYS   B 2 134 ? -27.182 -10.256 -26.313 1.00 52.88 ? 143 CYS   B CA  1 
ATOM   1296 C  C   . CYS   B 2 134 ? -27.502 -8.849  -25.831 1.00 51.76 ? 143 CYS   B C   1 
ATOM   1297 O  O   . CYS   B 2 134 ? -28.672 -8.556  -25.592 1.00 52.19 ? 143 CYS   B O   1 
ATOM   1298 C  CB  . CYS   B 2 134 ? -27.724 -11.289 -25.337 1.00 54.86 ? 143 CYS   B CB  1 
ATOM   1299 S  SG  . CYS   B 2 134 ? -27.878 -12.939 -26.043 1.00 61.84 ? 143 CYS   B SG  1 
ATOM   1300 N  N   . GLY   B 2 135 ? -26.497 -7.997  -25.681 1.00 50.45 ? 144 GLY   B N   1 
ATOM   1301 C  CA  . GLY   B 2 135 ? -26.707 -6.645  -25.175 1.00 49.98 ? 144 GLY   B CA  1 
ATOM   1302 C  C   . GLY   B 2 135 ? -26.740 -6.557  -23.657 1.00 49.08 ? 144 GLY   B C   1 
ATOM   1303 O  O   . GLY   B 2 135 ? -27.013 -5.487  -23.101 1.00 48.76 ? 144 GLY   B O   1 
ATOM   1304 N  N   . ARG   B 2 136 ? -26.470 -7.685  -22.970 1.00 48.21 ? 145 ARG   B N   1 
ATOM   1305 C  CA  . ARG   B 2 136 ? -26.442 -7.752  -21.510 1.00 47.99 ? 145 ARG   B CA  1 
ATOM   1306 C  C   . ARG   B 2 136 ? -25.125 -7.209  -20.984 1.00 46.27 ? 145 ARG   B C   1 
ATOM   1307 O  O   . ARG   B 2 136 ? -24.068 -7.472  -21.560 1.00 46.25 ? 145 ARG   B O   1 
ATOM   1308 C  CB  . ARG   B 2 136 ? -26.687 -9.185  -21.019 1.00 50.41 ? 145 ARG   B CB  1 
ATOM   1309 C  CG  . ARG   B 2 136 ? -28.142 -9.613  -21.168 1.00 54.80 ? 145 ARG   B CG  1 
ATOM   1310 C  CD  . ARG   B 2 136 ? -28.328 -11.067 -20.807 1.00 59.11 ? 145 ARG   B CD  1 
ATOM   1311 N  NE  . ARG   B 2 136 ? -27.775 -11.947 -21.835 1.00 63.47 ? 145 ARG   B NE  1 
ATOM   1312 C  CZ  . ARG   B 2 136 ? -27.032 -13.022 -21.585 1.00 66.69 ? 145 ARG   B CZ  1 
ATOM   1313 N  NH1 . ARG   B 2 136 ? -26.726 -13.352 -20.332 1.00 67.09 ? 145 ARG   B NH1 1 
ATOM   1314 N  NH2 . ARG   B 2 136 ? -26.569 -13.764 -22.585 1.00 66.02 ? 145 ARG   B NH2 1 
ATOM   1315 N  N   . VAL   B 2 137 ? -25.193 -6.420  -19.914 1.00 44.66 ? 146 VAL   B N   1 
ATOM   1316 C  CA  . VAL   B 2 137 ? -24.008 -5.802  -19.339 1.00 43.36 ? 146 VAL   B CA  1 
ATOM   1317 C  C   . VAL   B 2 137 ? -23.218 -6.806  -18.501 1.00 42.24 ? 146 VAL   B C   1 
ATOM   1318 O  O   . VAL   B 2 137 ? -23.648 -7.190  -17.419 1.00 42.55 ? 146 VAL   B O   1 
ATOM   1319 C  CB  . VAL   B 2 137 ? -24.375 -4.522  -18.555 1.00 43.30 ? 146 VAL   B CB  1 
ATOM   1320 C  CG1 . VAL   B 2 137 ? -23.128 -3.828  -18.034 1.00 43.66 ? 146 VAL   B CG1 1 
ATOM   1321 C  CG2 . VAL   B 2 137 ? -25.196 -3.573  -19.426 1.00 43.48 ? 146 VAL   B CG2 1 
ATOM   1322 N  N   . ILE   B 2 138 ? -22.078 -7.250  -19.019 1.00 40.72 ? 147 ILE   B N   1 
ATOM   1323 C  CA  . ILE   B 2 138 ? -21.217 -8.218  -18.329 1.00 39.20 ? 147 ILE   B CA  1 
ATOM   1324 C  C   . ILE   B 2 138 ? -20.188 -7.563  -17.368 1.00 37.95 ? 147 ILE   B C   1 
ATOM   1325 O  O   . ILE   B 2 138 ? -19.491 -8.270  -16.626 1.00 38.05 ? 147 ILE   B O   1 
ATOM   1326 C  CB  . ILE   B 2 138 ? -20.531 -9.155  -19.367 1.00 39.26 ? 147 ILE   B CB  1 
ATOM   1327 C  CG1 . ILE   B 2 138 ? -19.807 -8.342  -20.457 1.00 39.97 ? 147 ILE   B CG1 1 
ATOM   1328 C  CG2 . ILE   B 2 138 ? -21.544 -10.090 -20.012 1.00 39.45 ? 147 ILE   B CG2 1 
ATOM   1329 C  CD1 . ILE   B 2 138 ? -18.822 -9.166  -21.246 1.00 41.36 ? 147 ILE   B CD1 1 
ATOM   1330 N  N   . GLY   B 2 139 ? -20.128 -6.238  -17.351 1.00 36.49 ? 148 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 139 ? -19.213 -5.527  -16.470 1.00 36.36 ? 148 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 139 ? -19.035 -4.075  -16.849 1.00 36.43 ? 148 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 139 ? -19.639 -3.605  -17.813 1.00 37.25 ? 148 GLY   B O   1 
ATOM   1334 N  N   . LEU   B 2 140 ? -18.210 -3.351  -16.102 1.00 35.49 ? 149 LEU   B N   1 
ATOM   1335 C  CA  . LEU   B 2 140 ? -17.939 -1.943  -16.388 1.00 35.12 ? 149 LEU   B CA  1 
ATOM   1336 C  C   . LEU   B 2 140 ? -16.440 -1.764  -16.612 1.00 35.41 ? 149 LEU   B C   1 
ATOM   1337 O  O   . LEU   B 2 140 ? -15.614 -2.453  -15.999 1.00 35.36 ? 149 LEU   B O   1 
ATOM   1338 C  CB  . LEU   B 2 140 ? -18.405 -1.008  -15.248 1.00 34.49 ? 149 LEU   B CB  1 
ATOM   1339 C  CG  . LEU   B 2 140 ? -19.880 -1.024  -14.865 1.00 35.41 ? 149 LEU   B CG  1 
ATOM   1340 C  CD1 . LEU   B 2 140 ? -20.174 0.034   -13.781 1.00 35.89 ? 149 LEU   B CD1 1 
ATOM   1341 C  CD2 . LEU   B 2 140 ? -20.779 -0.819  -16.053 1.00 35.56 ? 149 LEU   B CD2 1 
ATOM   1342 N  N   . TYR   B 2 141 ? -16.112 -0.823  -17.489 1.00 35.15 ? 150 TYR   B N   1 
ATOM   1343 C  CA  . TYR   B 2 141 ? -14.769 -0.479  -17.928 1.00 35.37 ? 150 TYR   B CA  1 
ATOM   1344 C  C   . TYR   B 2 141 ? -14.262 0.698   -17.114 1.00 35.75 ? 150 TYR   B C   1 
ATOM   1345 O  O   . TYR   B 2 141 ? -15.008 1.640   -16.910 1.00 35.43 ? 150 TYR   B O   1 
ATOM   1346 C  CB  . TYR   B 2 141 ? -14.869 -0.092  -19.428 1.00 35.34 ? 150 TYR   B CB  1 
ATOM   1347 C  CG  . TYR   B 2 141 ? -13.668 0.613   -20.024 1.00 36.21 ? 150 TYR   B CG  1 
ATOM   1348 C  CD1 . TYR   B 2 141 ? -13.651 1.997   -20.179 1.00 36.98 ? 150 TYR   B CD1 1 
ATOM   1349 C  CD2 . TYR   B 2 141 ? -12.578 -0.107  -20.497 1.00 37.33 ? 150 TYR   B CD2 1 
ATOM   1350 C  CE1 . TYR   B 2 141 ? -12.547 2.650   -20.726 1.00 38.27 ? 150 TYR   B CE1 1 
ATOM   1351 C  CE2 . TYR   B 2 141 ? -11.475 0.531   -21.058 1.00 38.37 ? 150 TYR   B CE2 1 
ATOM   1352 C  CZ  . TYR   B 2 141 ? -11.458 1.910   -21.169 1.00 39.50 ? 150 TYR   B CZ  1 
ATOM   1353 O  OH  . TYR   B 2 141 ? -10.365 2.531   -21.757 1.00 41.15 ? 150 TYR   B OH  1 
ATOM   1354 N  N   . GLY   B 2 142 ? -12.999 0.674   -16.705 1.00 36.31 ? 151 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 142 ? -12.433 1.796   -15.958 1.00 37.12 ? 151 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 142 ? -11.474 1.450   -14.843 1.00 37.52 ? 151 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 142 ? -10.897 2.360   -14.236 1.00 38.10 ? 151 GLY   B O   1 
ATOM   1358 N  N   . ASN   B 2 143 ? -11.306 0.145   -14.537 1.00 36.99 ? 152 ASN   B N   1 
ATOM   1359 C  CA  . ASN   B 2 143 ? -10.367 -0.260  -13.500 1.00 37.36 ? 152 ASN   B CA  1 
ATOM   1360 C  C   . ASN   B 2 143 ? -9.448  -1.370  -13.962 1.00 38.68 ? 152 ASN   B C   1 
ATOM   1361 O  O   . ASN   B 2 143 ? -9.858  -2.521  -14.080 1.00 38.77 ? 152 ASN   B O   1 
ATOM   1362 C  CB  . ASN   B 2 143 ? -11.075 -0.681  -12.206 1.00 37.70 ? 152 ASN   B CB  1 
ATOM   1363 C  CG  . ASN   B 2 143 ? -10.135 -0.769  -11.031 1.00 37.98 ? 152 ASN   B CG  1 
ATOM   1364 O  OD1 . ASN   B 2 143 ? -9.076  -0.131  -11.002 1.00 38.05 ? 152 ASN   B OD1 1 
ATOM   1365 N  ND2 . ASN   B 2 143 ? -10.498 -1.562  -10.037 1.00 37.21 ? 152 ASN   B ND2 1 
ATOM   1366 N  N   . GLY   B 2 144 ? -8.192  -1.028  -14.142 1.00 39.36 ? 153 GLY   B N   1 
ATOM   1367 C  CA  . GLY   B 2 144 ? -7.203  -1.991  -14.568 1.00 41.20 ? 153 GLY   B CA  1 
ATOM   1368 C  C   . GLY   B 2 144 ? -5.776  -1.605  -14.288 1.00 43.18 ? 153 GLY   B C   1 
ATOM   1369 O  O   . GLY   B 2 144 ? -5.446  -1.099  -13.211 1.00 43.01 ? 153 GLY   B O   1 
ATOM   1370 N  N   . VAL   B 2 145 ? -4.925  -1.830  -15.284 1.00 44.99 ? 154 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 145 ? -3.501  -1.664  -15.097 1.00 47.22 ? 154 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 145 ? -2.790  -0.963  -16.282 1.00 49.42 ? 154 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 145 ? -3.307  -0.910  -17.396 1.00 49.64 ? 154 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 145 ? -2.949  -3.087  -14.788 1.00 47.67 ? 154 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 145 ? -2.594  -3.854  -16.050 1.00 47.43 ? 154 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 145 ? -1.806  -3.053  -13.794 1.00 48.65 ? 154 VAL   B CG2 1 
ATOM   1377 N  N   . VAL   B 2 146 ? -1.623  -0.375  -16.007 1.00 50.89 ? 155 VAL   B N   1 
ATOM   1378 C  CA  . VAL   B 2 146 ? -0.819  0.314   -17.005 1.00 52.67 ? 155 VAL   B CA  1 
ATOM   1379 C  C   . VAL   B 2 146 ? 0.290   -0.630  -17.424 1.00 54.76 ? 155 VAL   B C   1 
ATOM   1380 O  O   . VAL   B 2 146 ? 0.995   -1.155  -16.572 1.00 54.66 ? 155 VAL   B O   1 
ATOM   1381 C  CB  . VAL   B 2 146 ? -0.258  1.639   -16.451 1.00 53.31 ? 155 VAL   B CB  1 
ATOM   1382 C  CG1 . VAL   B 2 146 ? 0.593   2.352   -17.490 1.00 54.05 ? 155 VAL   B CG1 1 
ATOM   1383 C  CG2 . VAL   B 2 146 ? -1.386  2.539   -15.973 1.00 53.86 ? 155 VAL   B CG2 1 
ATOM   1384 N  N   . ILE   B 2 147 ? 0.410   -0.897  -18.728 1.00 56.63 ? 156 ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 2 147 ? 1.424   -1.816  -19.236 1.00 59.12 ? 156 ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 2 147 ? 2.684   -1.064  -19.733 1.00 61.99 ? 156 ILE   B C   1 
ATOM   1387 O  O   . ILE   B 2 147 ? 2.684   0.164   -19.756 1.00 62.44 ? 156 ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 2 147 ? 0.778   -2.744  -20.300 1.00 59.81 ? 156 ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 2 147 ? 0.196   -1.925  -21.473 1.00 60.70 ? 156 ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 2 147 ? -0.301  -3.619  -19.654 1.00 60.17 ? 156 ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 2 147 ? -0.369  -2.761  -22.624 1.00 61.59 ? 156 ILE   B CD1 1 
ATOM   1392 N  N   . LYS   B 2 148 ? 3.756   -1.794  -20.097 1.00 63.69 ? 157 LYS   B N   1 
ATOM   1393 C  CA  . LYS   B 2 148 ? 5.050   -1.257  -20.548 1.00 65.73 ? 157 LYS   B CA  1 
ATOM   1394 C  C   . LYS   B 2 148 ? 4.993   -0.044  -21.503 1.00 66.69 ? 157 LYS   B C   1 
ATOM   1395 O  O   . LYS   B 2 148 ? 5.726   0.927   -21.297 1.00 66.70 ? 157 LYS   B O   1 
ATOM   1396 C  CB  . LYS   B 2 148 ? 5.896   -2.375  -21.176 1.00 69.03 ? 157 LYS   B CB  1 
ATOM   1397 C  CG  . LYS   B 2 148 ? 6.112   -3.541  -20.199 1.00 75.64 ? 157 LYS   B CG  1 
ATOM   1398 C  CD  . LYS   B 2 148 ? 7.081   -4.600  -20.726 1.00 82.24 ? 157 LYS   B CD  1 
ATOM   1399 C  CE  . LYS   B 2 148 ? 8.539   -4.272  -20.466 1.00 87.18 ? 157 LYS   B CE  1 
ATOM   1400 N  NZ  . LYS   B 2 148 ? 8.867   -4.279  -19.013 1.00 89.85 ? 157 LYS   B NZ  1 
ATOM   1401 N  N   . ASN   B 2 149 ? 4.126   -0.081  -22.518 1.00 67.16 ? 158 ASN   B N   1 
ATOM   1402 C  CA  . ASN   B 2 149 ? 4.032   1.023   -23.476 1.00 68.27 ? 158 ASN   B CA  1 
ATOM   1403 C  C   . ASN   B 2 149 ? 3.201   2.233   -22.992 1.00 66.99 ? 158 ASN   B C   1 
ATOM   1404 O  O   . ASN   B 2 149 ? 2.928   3.131   -23.787 1.00 67.45 ? 158 ASN   B O   1 
ATOM   1405 C  CB  . ASN   B 2 149 ? 3.544   0.547   -24.865 1.00 71.60 ? 158 ASN   B CB  1 
ATOM   1406 C  CG  . ASN   B 2 149 ? 2.452   -0.508  -24.861 1.00 76.89 ? 158 ASN   B CG  1 
ATOM   1407 O  OD1 . ASN   B 2 149 ? 2.569   -1.577  -24.229 1.00 78.21 ? 158 ASN   B OD1 1 
ATOM   1408 N  ND2 . ASN   B 2 149 ? 1.381   -0.239  -25.610 1.00 77.79 ? 158 ASN   B ND2 1 
ATOM   1409 N  N   . GLY   B 2 150 ? 2.859   2.271   -21.704 1.00 65.25 ? 159 GLY   B N   1 
ATOM   1410 C  CA  . GLY   B 2 150 ? 2.087   3.360   -21.111 1.00 63.68 ? 159 GLY   B CA  1 
ATOM   1411 C  C   . GLY   B 2 150 ? 0.582   3.240   -21.275 1.00 61.88 ? 159 GLY   B C   1 
ATOM   1412 O  O   . GLY   B 2 150 ? -0.170  4.005   -20.670 1.00 61.71 ? 159 GLY   B O   1 
ATOM   1413 N  N   . SER   B 2 151 ? 0.133   2.286   -22.116 1.00 60.38 ? 160 SER   B N   1 
ATOM   1414 C  CA  . SER   B 2 151 ? -1.267  1.982   -22.434 1.00 58.65 ? 160 SER   B CA  1 
ATOM   1415 C  C   . SER   B 2 151 ? -2.019  1.359   -21.222 1.00 55.49 ? 160 SER   B C   1 
ATOM   1416 O  O   . SER   B 2 151 ? -1.390  0.917   -20.257 1.00 55.28 ? 160 SER   B O   1 
ATOM   1417 C  CB  . SER   B 2 151 ? -1.309  1.044   -23.644 1.00 60.90 ? 160 SER   B CB  1 
ATOM   1418 O  OG  . SER   B 2 151 ? -2.561  0.412   -23.860 1.00 64.35 ? 160 SER   B OG  1 
ATOM   1419 N  N   . TYR   B 2 152 ? -3.366  1.330   -21.286 1.00 52.79 ? 161 TYR   B N   1 
ATOM   1420 C  CA  . TYR   B 2 152 ? -4.210  0.785   -20.224 1.00 50.49 ? 161 TYR   B CA  1 
ATOM   1421 C  C   . TYR   B 2 152 ? -4.928  -0.492  -20.662 1.00 48.67 ? 161 TYR   B C   1 
ATOM   1422 O  O   . TYR   B 2 152 ? -5.340  -0.612  -21.811 1.00 48.43 ? 161 TYR   B O   1 
ATOM   1423 C  CB  . TYR   B 2 152 ? -5.273  1.824   -19.810 1.00 49.46 ? 161 TYR   B CB  1 
ATOM   1424 C  CG  . TYR   B 2 152 ? -5.753  1.721   -18.376 1.00 48.67 ? 161 TYR   B CG  1 
ATOM   1425 C  CD1 . TYR   B 2 152 ? -4.944  2.120   -17.322 1.00 48.95 ? 161 TYR   B CD1 1 
ATOM   1426 C  CD2 . TYR   B 2 152 ? -7.039  1.291   -18.080 1.00 48.74 ? 161 TYR   B CD2 1 
ATOM   1427 C  CE1 . TYR   B 2 152 ? -5.389  2.058   -16.005 1.00 49.12 ? 161 TYR   B CE1 1 
ATOM   1428 C  CE2 . TYR   B 2 152 ? -7.498  1.232   -16.767 1.00 48.73 ? 161 TYR   B CE2 1 
ATOM   1429 C  CZ  . TYR   B 2 152 ? -6.675  1.634   -15.734 1.00 49.29 ? 161 TYR   B CZ  1 
ATOM   1430 O  OH  . TYR   B 2 152 ? -7.132  1.643   -14.440 1.00 49.67 ? 161 TYR   B OH  1 
ATOM   1431 N  N   . VAL   B 2 153 ? -5.108  -1.424  -19.718 1.00 47.16 ? 162 VAL   B N   1 
ATOM   1432 C  CA  . VAL   B 2 153 ? -5.850  -2.669  -19.899 1.00 45.92 ? 162 VAL   B CA  1 
ATOM   1433 C  C   . VAL   B 2 153 ? -6.835  -2.746  -18.724 1.00 44.27 ? 162 VAL   B C   1 
ATOM   1434 O  O   . VAL   B 2 153 ? -6.418  -2.919  -17.588 1.00 44.23 ? 162 VAL   B O   1 
ATOM   1435 C  CB  . VAL   B 2 153 ? -4.925  -3.916  -19.989 1.00 46.32 ? 162 VAL   B CB  1 
ATOM   1436 C  CG1 . VAL   B 2 153 ? -5.742  -5.207  -19.942 1.00 46.30 ? 162 VAL   B CG1 1 
ATOM   1437 C  CG2 . VAL   B 2 153 ? -4.078  -3.870  -21.260 1.00 47.52 ? 162 VAL   B CG2 1 
ATOM   1438 N  N   . SER   B 2 154 ? -8.127  -2.496  -18.982 1.00 42.88 ? 163 SER   B N   1 
ATOM   1439 C  CA  . SER   B 2 154 ? -9.131  -2.501  -17.920 1.00 41.68 ? 163 SER   B CA  1 
ATOM   1440 C  C   . SER   B 2 154 ? -9.712  -3.884  -17.675 1.00 40.76 ? 163 SER   B C   1 
ATOM   1441 O  O   . SER   B 2 154 ? -9.929  -4.626  -18.617 1.00 40.30 ? 163 SER   B O   1 
ATOM   1442 C  CB  . SER   B 2 154 ? -10.256 -1.520  -18.248 1.00 41.31 ? 163 SER   B CB  1 
ATOM   1443 O  OG  . SER   B 2 154 ? -11.446 -1.744  -17.505 1.00 40.56 ? 163 SER   B OG  1 
ATOM   1444 N  N   . ALA   B 2 155 ? -10.070 -4.181  -16.423 1.00 39.87 ? 164 ALA   B N   1 
ATOM   1445 C  CA  . ALA   B 2 155 ? -10.745 -5.430  -16.104 1.00 39.66 ? 164 ALA   B CA  1 
ATOM   1446 C  C   . ALA   B 2 155 ? -12.229 -5.308  -16.523 1.00 39.27 ? 164 ALA   B C   1 
ATOM   1447 O  O   . ALA   B 2 155 ? -12.742 -4.200  -16.749 1.00 39.02 ? 164 ALA   B O   1 
ATOM   1448 C  CB  . ALA   B 2 155 ? -10.647 -5.703  -14.597 1.00 40.25 ? 164 ALA   B CB  1 
ATOM   1449 N  N   . ILE   B 2 156 ? -12.912 -6.448  -16.659 1.00 39.04 ? 165 ILE   B N   1 
ATOM   1450 C  CA  . ILE   B 2 156 ? -14.346 -6.450  -16.891 1.00 39.19 ? 165 ILE   B CA  1 
ATOM   1451 C  C   . ILE   B 2 156 ? -14.902 -6.572  -15.461 1.00 38.94 ? 165 ILE   B C   1 
ATOM   1452 O  O   . ILE   B 2 156 ? -14.990 -7.688  -14.940 1.00 38.56 ? 165 ILE   B O   1 
ATOM   1453 C  CB  . ILE   B 2 156 ? -14.812 -7.620  -17.792 1.00 39.51 ? 165 ILE   B CB  1 
ATOM   1454 C  CG1 . ILE   B 2 156 ? -14.098 -7.595  -19.175 1.00 40.76 ? 165 ILE   B CG1 1 
ATOM   1455 C  CG2 . ILE   B 2 156 ? -16.348 -7.601  -17.947 1.00 39.48 ? 165 ILE   B CG2 1 
ATOM   1456 C  CD1 . ILE   B 2 156 ? -14.448 -8.764  -20.101 1.00 41.02 ? 165 ILE   B CD1 1 
ATOM   1457 N  N   . THR   B 2 157 ? -15.182 -5.418  -14.795 1.00 38.35 ? 166 THR   B N   1 
ATOM   1458 C  CA  . THR   B 2 157 ? -15.655 -5.394  -13.410 1.00 37.88 ? 166 THR   B CA  1 
ATOM   1459 C  C   . THR   B 2 157 ? -17.160 -5.590  -13.256 1.00 37.76 ? 166 THR   B C   1 
ATOM   1460 O  O   . THR   B 2 157 ? -17.930 -4.703  -13.596 1.00 37.73 ? 166 THR   B O   1 
ATOM   1461 C  CB  . THR   B 2 157 ? -15.233 -4.104  -12.723 1.00 39.15 ? 166 THR   B CB  1 
ATOM   1462 O  OG1 . THR   B 2 157 ? -13.821 -3.937  -12.833 1.00 40.33 ? 166 THR   B OG1 1 
ATOM   1463 C  CG2 . THR   B 2 157 ? -15.626 -4.082  -11.277 1.00 39.32 ? 166 THR   B CG2 1 
ATOM   1464 N  N   . GLN   B 2 158 ? -17.575 -6.705  -12.661 1.00 37.79 ? 167 GLN   B N   1 
ATOM   1465 C  CA  . GLN   B 2 158 ? -18.985 -6.997  -12.440 1.00 38.03 ? 167 GLN   B CA  1 
ATOM   1466 C  C   . GLN   B 2 158 ? -19.305 -7.121  -10.938 1.00 39.32 ? 167 GLN   B C   1 
ATOM   1467 O  O   . GLN   B 2 158 ? -18.483 -7.610  -10.161 1.00 39.06 ? 167 GLN   B O   1 
ATOM   1468 C  CB  . GLN   B 2 158 ? -19.381 -8.277  -13.204 1.00 38.23 ? 167 GLN   B CB  1 
ATOM   1469 C  CG  . GLN   B 2 158 ? -20.866 -8.642  -13.170 1.00 38.96 ? 167 GLN   B CG  1 
ATOM   1470 C  CD  . GLN   B 2 158 ? -21.771 -7.587  -13.770 1.00 39.47 ? 167 GLN   B CD  1 
ATOM   1471 O  OE1 . GLN   B 2 158 ? -21.911 -6.477  -13.254 1.00 39.62 ? 167 GLN   B OE1 1 
ATOM   1472 N  NE2 . GLN   B 2 158 ? -22.446 -7.925  -14.843 1.00 38.50 ? 167 GLN   B NE2 1 
ATOM   1473 N  N   . GLY   B 2 159 ? -20.479 -6.646  -10.541 1.00 40.53 ? 168 GLY   B N   1 
ATOM   1474 C  CA  . GLY   B 2 159 ? -20.929 -6.748  -9.168  1.00 43.21 ? 168 GLY   B CA  1 
ATOM   1475 C  C   . GLY   B 2 159 ? -21.698 -8.030  -8.928  1.00 46.90 ? 168 GLY   B C   1 
ATOM   1476 O  O   . GLY   B 2 159 ? -21.802 -8.885  -9.812  1.00 47.32 ? 168 GLY   B O   1 
ATOM   1477 N  N   . LYS   B 2 160 ? -22.248 -8.177  -7.729  1.00 49.41 ? 169 LYS   B N   1 
ATOM   1478 C  CA  . LYS   B 2 160 ? -23.022 -9.358  -7.377  1.00 52.25 ? 169 LYS   B CA  1 
ATOM   1479 C  C   . LYS   B 2 160 ? -24.478 -8.962  -7.149  1.00 55.19 ? 169 LYS   B C   1 
ATOM   1480 O  O   . LYS   B 2 160 ? -24.746 -7.945  -6.512  1.00 55.27 ? 169 LYS   B O   1 
ATOM   1481 C  CB  . LYS   B 2 160 ? -22.438 -10.027 -6.120  1.00 54.19 ? 169 LYS   B CB  1 
ATOM   1482 C  CG  . LYS   B 2 160 ? -22.981 -11.426 -5.862  1.00 59.35 ? 169 LYS   B CG  1 
ATOM   1483 C  CD  . LYS   B 2 160 ? -22.587 -11.932 -4.476  1.00 64.77 ? 169 LYS   B CD  1 
ATOM   1484 C  CE  . LYS   B 2 160 ? -23.093 -13.329 -4.197  1.00 68.63 ? 169 LYS   B CE  1 
ATOM   1485 N  NZ  . LYS   B 2 160 ? -22.623 -13.825 -2.871  1.00 71.23 ? 169 LYS   B NZ  1 
ATOM   1486 N  N   . ARG   B 2 161 ? -25.413 -9.742  -7.697  1.00 57.60 ? 170 ARG   B N   1 
ATOM   1487 C  CA  . ARG   B 2 161 ? -26.840 -9.506  -7.509  1.00 60.46 ? 170 ARG   B CA  1 
ATOM   1488 C  C   . ARG   B 2 161 ? -27.272 -10.347 -6.298  1.00 63.71 ? 170 ARG   B C   1 
ATOM   1489 O  O   . ARG   B 2 161 ? -26.986 -11.542 -6.257  1.00 64.02 ? 170 ARG   B O   1 
ATOM   1490 C  CB  . ARG   B 2 161 ? -27.633 -9.907  -8.770  1.00 61.23 ? 170 ARG   B CB  1 
ATOM   1491 C  CG  . ARG   B 2 161 ? -28.958 -9.169  -8.913  1.00 62.96 ? 170 ARG   B CG  1 
ATOM   1492 C  CD  . ARG   B 2 161 ? -29.894 -9.775  -9.946  1.00 65.35 ? 170 ARG   B CD  1 
ATOM   1493 N  NE  . ARG   B 2 161 ? -31.249 -9.247  -9.784  1.00 67.74 ? 170 ARG   B NE  1 
ATOM   1494 C  CZ  . ARG   B 2 161 ? -31.840 -8.405  -10.627 1.00 69.18 ? 170 ARG   B CZ  1 
ATOM   1495 N  NH1 . ARG   B 2 161 ? -31.226 -8.029  -11.742 1.00 67.62 ? 170 ARG   B NH1 1 
ATOM   1496 N  NH2 . ARG   B 2 161 ? -33.058 -7.948  -10.372 1.00 69.45 ? 170 ARG   B NH2 1 
ATOM   1497 N  N   . GLU   B 2 162 ? -27.914 -9.722  -5.300  1.00 66.00 ? 171 GLU   B N   1 
ATOM   1498 C  CA  . GLU   B 2 162 ? -28.347 -10.413 -4.079  1.00 68.78 ? 171 GLU   B CA  1 
ATOM   1499 C  C   . GLU   B 2 162 ? -29.731 -11.068 -4.197  1.00 70.82 ? 171 GLU   B C   1 
ATOM   1500 O  O   . GLU   B 2 162 ? -30.660 -10.441 -4.711  1.00 71.17 ? 171 GLU   B O   1 
ATOM   1501 C  CB  . GLU   B 2 162 ? -28.309 -9.452  -2.882  1.00 71.89 ? 171 GLU   B CB  1 
ATOM   1502 C  CG  . GLU   B 2 162 ? -26.907 -9.221  -2.346  1.00 78.61 ? 171 GLU   B CG  1 
ATOM   1503 C  CD  . GLU   B 2 162 ? -26.292 -10.440 -1.683  1.00 87.23 ? 171 GLU   B CD  1 
ATOM   1504 O  OE1 . GLU   B 2 162 ? -26.702 -10.766 -0.544  1.00 88.68 ? 171 GLU   B OE1 1 
ATOM   1505 O  OE2 . GLU   B 2 162 ? -25.408 -11.076 -2.302  1.00 89.94 ? 171 GLU   B OE2 1 
ATOM   1506 N  N   . VAL   B 2 167 ? -29.865 -12.317 -3.691  1.00 71.92 ? 172 VAL   B N   1 
ATOM   1507 C  CA  . VAL   B 2 167 ? -31.099 -13.125 -3.721  1.00 73.37 ? 172 VAL   B CA  1 
ATOM   1508 C  C   . VAL   B 2 167 ? -31.664 -13.258 -5.149  1.00 73.99 ? 172 VAL   B C   1 
ATOM   1509 O  O   . VAL   B 2 167 ? -31.871 -14.366 -5.644  1.00 74.24 ? 172 VAL   B O   1 
ATOM   1510 C  CB  . VAL   B 2 167 ? -32.176 -12.647 -2.701  1.00 74.64 ? 172 VAL   B CB  1 
ATOM   1511 C  CG1 . VAL   B 2 167 ? -33.508 -13.370 -2.913  1.00 75.42 ? 172 VAL   B CG1 1 
ATOM   1512 C  CG2 . VAL   B 2 167 ? -31.692 -12.827 -1.263  1.00 75.21 ? 172 VAL   B CG2 1 
HETATM 1513 S  S   . DMS   C 3 .   ? -18.814 12.096  -0.300  1.00 73.76 ? 201 DMS   B S   1 
HETATM 1514 O  O   . DMS   C 3 .   ? -19.735 10.937  -0.497  1.00 73.68 ? 201 DMS   B O   1 
HETATM 1515 C  C1  . DMS   C 3 .   ? -19.690 13.606  -0.778  1.00 73.91 ? 201 DMS   B C1  1 
HETATM 1516 C  C2  . DMS   C 3 .   ? -17.656 12.172  -1.697  1.00 73.59 ? 201 DMS   B C2  1 
HETATM 1517 N  N1  . A1B8I D 4 .   ? -7.603  4.310   -20.693 1.00 43.43 ? 202 A1B8I B N1  1 
HETATM 1518 N  N3  . A1B8I D 4 .   ? -9.280  2.613   -7.548  1.00 37.32 ? 202 A1B8I B N3  1 
HETATM 1519 C  C4  . A1B8I D 4 .   ? -6.819  5.247   -16.030 1.00 42.82 ? 202 A1B8I B C4  1 
HETATM 1520 C  C5  . A1B8I D 4 .   ? -8.024  5.025   -15.374 1.00 42.80 ? 202 A1B8I B C5  1 
HETATM 1521 C  C6  . A1B8I D 4 .   ? -8.083  5.279   -13.898 1.00 42.48 ? 202 A1B8I B C6  1 
HETATM 1522 C  C7  . A1B8I D 4 .   ? -9.103  4.499   -11.766 1.00 39.54 ? 202 A1B8I B C7  1 
HETATM 1523 C  C8  . A1B8I D 4 .   ? -8.848  5.639   -11.005 1.00 39.21 ? 202 A1B8I B C8  1 
HETATM 1524 C  C10 . A1B8I D 4 .   ? -9.237  4.395   -9.002  1.00 38.00 ? 202 A1B8I B C10 1 
HETATM 1525 C  C13 . A1B8I D 4 .   ? -9.794  2.109   -8.827  1.00 37.21 ? 202 A1B8I B C13 1 
HETATM 1526 C  C15 . A1B8I D 4 .   ? -9.152  4.688   -16.113 1.00 43.28 ? 202 A1B8I B C15 1 
HETATM 1527 C  C1  . A1B8I D 4 .   ? -7.712  4.506   -19.562 1.00 43.46 ? 202 A1B8I B C1  1 
HETATM 1528 C  C2  . A1B8I D 4 .   ? -7.836  4.700   -18.134 1.00 43.25 ? 202 A1B8I B C2  1 
HETATM 1529 C  C3  . A1B8I D 4 .   ? -6.722  5.096   -17.401 1.00 42.97 ? 202 A1B8I B C3  1 
HETATM 1530 O  O1  . A1B8I D 4 .   ? -7.262  6.026   -13.374 1.00 43.50 ? 202 A1B8I B O1  1 
HETATM 1531 N  N2  . A1B8I D 4 .   ? -8.980  4.554   -13.185 1.00 40.98 ? 202 A1B8I B N2  1 
HETATM 1532 C  C9  . A1B8I D 4 .   ? -8.953  5.604   -9.624  1.00 38.62 ? 202 A1B8I B C9  1 
HETATM 1533 C  C11 . A1B8I D 4 .   ? -9.486  3.254   -9.752  1.00 37.99 ? 202 A1B8I B C11 1 
HETATM 1534 C  C12 . A1B8I D 4 .   ? -9.364  3.274   -11.136 1.00 38.57 ? 202 A1B8I B C12 1 
HETATM 1535 C  C14 . A1B8I D 4 .   ? -9.401  4.081   -7.542  1.00 37.53 ? 202 A1B8I B C14 1 
HETATM 1536 C  C16 . A1B8I D 4 .   ? -9.055  4.487   -17.483 1.00 43.71 ? 202 A1B8I B C16 1 
HETATM 1537 CL CL1 . A1B8I D 4 .   ? -10.494 4.088   -18.377 1.00 44.28 ? 202 A1B8I B CL1 1 
HETATM 1538 O  O   . HOH   E 5 .   ? -1.643  0.177   -8.562  1.00 53.19 ? 101 HOH   A O   1 
HETATM 1539 O  O   . HOH   E 5 .   ? -6.949  -8.815  -3.193  1.00 24.93 ? 102 HOH   A O   1 
HETATM 1540 O  O   . HOH   E 5 .   ? -4.679  -14.286 -25.340 1.00 40.40 ? 103 HOH   A O   1 
HETATM 1541 O  O   . HOH   E 5 .   ? -3.159  1.625   -4.228  1.00 44.38 ? 104 HOH   A O   1 
HETATM 1542 O  O   . HOH   E 5 .   ? -23.908 19.048  -19.509 1.00 43.17 ? 105 HOH   A O   1 
HETATM 1543 O  O   . HOH   E 5 .   ? -2.303  -3.809  -6.191  1.00 30.53 ? 106 HOH   A O   1 
HETATM 1544 O  O   . HOH   E 5 .   ? -8.155  -1.626  6.781   1.00 41.73 ? 107 HOH   A O   1 
HETATM 1545 O  O   . HOH   E 5 .   ? -24.140 9.452   -27.420 1.00 35.56 ? 108 HOH   A O   1 
HETATM 1546 O  O   . HOH   E 5 .   ? -3.170  -11.575 -7.049  1.00 36.03 ? 109 HOH   A O   1 
HETATM 1547 O  O   . HOH   E 5 .   ? -9.444  3.964   -3.824  1.00 46.14 ? 110 HOH   A O   1 
HETATM 1548 O  O   . HOH   E 5 .   ? -7.065  4.535   -4.722  1.00 46.38 ? 111 HOH   A O   1 
HETATM 1549 O  O   . HOH   E 5 .   ? -28.379 -5.714  -28.113 1.00 42.31 ? 112 HOH   A O   1 
HETATM 1550 O  O   . HOH   E 5 .   ? -29.164 16.097  -14.917 1.00 51.90 ? 113 HOH   A O   1 
HETATM 1551 O  O   . HOH   E 5 .   ? -6.701  -15.895 -25.384 1.00 40.33 ? 114 HOH   A O   1 
HETATM 1552 O  O   . HOH   E 5 .   ? -4.649  -9.968  -5.566  1.00 36.78 ? 115 HOH   A O   1 
HETATM 1553 O  O   . HOH   E 5 .   ? -4.109  -4.675  0.280   1.00 51.92 ? 116 HOH   A O   1 
HETATM 1554 O  O   . HOH   E 5 .   ? -31.084 0.467   -23.073 1.00 44.72 ? 117 HOH   A O   1 
HETATM 1555 O  O   . HOH   E 5 .   ? -21.331 -8.526  -34.590 1.00 54.01 ? 118 HOH   A O   1 
HETATM 1556 O  O   . HOH   E 5 .   ? -32.149 -0.074  -29.644 1.00 65.67 ? 119 HOH   A O   1 
HETATM 1557 O  O   . HOH   E 5 .   ? -4.101  -0.383  -0.064  1.00 46.76 ? 120 HOH   A O   1 
HETATM 1558 O  O   . HOH   E 5 .   ? -26.459 -2.806  -35.306 1.00 57.67 ? 121 HOH   A O   1 
HETATM 1559 O  O   . HOH   E 5 .   ? -6.173  -21.584 -21.032 1.00 47.36 ? 122 HOH   A O   1 
HETATM 1560 O  O   . HOH   E 5 .   ? -5.432  2.057   -10.191 1.00 37.87 ? 123 HOH   A O   1 
HETATM 1561 O  O   . HOH   E 5 .   ? -2.676  -8.791  -3.249  1.00 42.31 ? 124 HOH   A O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -15.651 -9.882  -15.230 1.00 39.73 ? 301 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -34.187 2.052   -15.459 1.00 40.64 ? 302 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -19.645 -11.894 -26.006 1.00 56.03 ? 303 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -30.931 12.651  -19.113 1.00 50.93 ? 304 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -27.932 -6.698  -5.713  1.00 54.10 ? 305 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -6.551  -0.350  -10.891 1.00 31.20 ? 306 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -20.594 -7.106  -5.622  1.00 48.54 ? 307 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -26.035 -7.765  -16.695 1.00 34.26 ? 308 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -11.864 1.964   -5.919  1.00 36.70 ? 309 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -16.840 21.212  -14.495 1.00 54.68 ? 310 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -7.027  -10.551 -5.270  1.00 37.73 ? 311 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -21.924 -13.686 -21.742 1.00 56.66 ? 312 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -34.461 0.685   -3.398  1.00 39.20 ? 313 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -5.896  -9.620  -0.477  1.00 46.46 ? 314 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -13.145 -2.127  -14.724 1.00 29.56 ? 315 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -35.172 4.488   -8.938  1.00 55.97 ? 316 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -18.095 -10.590 -16.671 1.00 37.96 ? 317 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -14.781 8.779   -30.307 1.00 44.58 ? 318 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -5.782  3.082   -12.573 1.00 38.59 ? 319 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -31.035 12.866  -16.400 1.00 42.13 ? 320 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -12.637 -3.261  -10.052 1.00 23.63 ? 321 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -21.812 7.152   -0.094  0.50 25.05 ? 322 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -18.755 19.177  -21.639 1.00 45.26 ? 323 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -9.374  -6.531  -25.447 1.00 43.10 ? 324 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -16.538 -6.937  -8.312  1.00 48.29 ? 325 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -18.991 15.145  -22.251 1.00 36.36 ? 326 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -21.875 -12.410 -13.024 1.00 41.68 ? 327 HOH   B O   1 
HETATM 1589 O  O   . HOH   F 5 .   ? -10.569 6.992   -5.991  1.00 53.11 ? 328 HOH   B O   1 
HETATM 1590 O  O   . HOH   F 5 .   ? -29.329 -1.684  -19.181 1.00 51.52 ? 329 HOH   B O   1 
HETATM 1591 O  O   . HOH   F 5 .   ? -11.856 -17.822 -28.162 1.00 52.93 ? 330 HOH   B O   1 
HETATM 1592 O  O   . HOH   F 5 .   ? -30.490 -7.582  -5.064  1.00 52.32 ? 331 HOH   B O   1 
HETATM 1593 O  O   . HOH   F 5 .   ? -23.952 -14.424 -18.434 1.00 47.60 ? 332 HOH   B O   1 
HETATM 1594 O  O   . HOH   F 5 .   ? -35.714 -5.400  -10.192 1.00 59.51 ? 333 HOH   B O   1 
HETATM 1595 O  O   . HOH   F 5 .   ? -27.974 -6.141  -18.672 1.00 41.08 ? 334 HOH   B O   1 
HETATM 1596 O  O   . HOH   F 5 .   ? -8.732  -10.665 -7.226  1.00 48.19 ? 335 HOH   B O   1 
HETATM 1597 O  O   . HOH   F 5 .   ? -17.087 13.219  -5.583  1.00 54.68 ? 336 HOH   B O   1 
HETATM 1598 O  O   . HOH   F 5 .   ? -15.218 -4.957  1.316   1.00 49.07 ? 337 HOH   B O   1 
HETATM 1599 O  O   . HOH   F 5 .   ? -16.344 27.787  -16.338 1.00 54.95 ? 338 HOH   B O   1 
HETATM 1600 O  O   . HOH   F 5 .   ? -15.260 16.726  -20.170 1.00 47.80 ? 339 HOH   B O   1 
HETATM 1601 O  O   . HOH   F 5 .   ? -10.747 -18.494 -12.003 1.00 57.43 ? 340 HOH   B O   1 
HETATM 1602 O  O   . HOH   F 5 .   ? -29.988 -5.008  -0.870  1.00 44.15 ? 341 HOH   B O   1 
HETATM 1603 O  O   . HOH   F 5 .   ? 6.895   -3.839  -16.806 1.00 61.07 ? 342 HOH   B O   1 
HETATM 1604 O  O   . HOH   F 5 .   ? -21.917 15.119  -6.107  1.00 49.21 ? 343 HOH   B O   1 
HETATM 1605 O  O   . HOH   F 5 .   ? -11.453 12.639  -18.901 1.00 44.20 ? 344 HOH   B O   1 
HETATM 1606 O  O   . HOH   F 5 .   ? -32.058 -7.011  -6.993  1.00 51.98 ? 345 HOH   B O   1 
HETATM 1607 O  O   . HOH   F 5 .   ? -7.408  -6.353  0.425   1.00 48.90 ? 346 HOH   B O   1 
HETATM 1608 O  O   . HOH   F 5 .   ? -25.924 -4.623  -4.024  1.00 36.81 ? 347 HOH   B O   1 
HETATM 1609 O  O   . HOH   F 5 .   ? -14.755 -6.417  -1.856  1.00 45.99 ? 348 HOH   B O   1 
HETATM 1610 O  O   . HOH   F 5 .   ? -14.845 -12.433 -16.456 1.00 41.84 ? 349 HOH   B O   1 
HETATM 1611 O  O   . HOH   F 5 .   ? -11.686 -5.049  -8.422  1.00 53.85 ? 350 HOH   B O   1 
HETATM 1612 O  O   . HOH   F 5 .   ? -15.917 -14.300 -30.882 1.00 45.08 ? 351 HOH   B O   1 
HETATM 1613 O  O   . HOH   F 5 .   ? -11.288 8.153   -13.798 1.00 45.11 ? 352 HOH   B O   1 
HETATM 1614 O  O   . HOH   F 5 .   ? -20.694 -7.795  -2.724  1.00 57.74 ? 353 HOH   B O   1 
HETATM 1615 O  O   . HOH   F 5 .   ? -30.710 4.466   -2.248  1.00 40.28 ? 354 HOH   B O   1 
HETATM 1616 O  O   . HOH   F 5 .   ? -0.847  0.192   -12.897 1.00 38.73 ? 355 HOH   B O   1 
HETATM 1617 O  O   . HOH   F 5 .   ? -19.268 25.767  -14.538 1.00 57.37 ? 356 HOH   B O   1 
HETATM 1618 O  O   . HOH   F 5 .   ? -32.470 7.240   -4.363  1.00 60.69 ? 357 HOH   B O   1 
HETATM 1619 O  O   . HOH   F 5 .   ? -2.909  4.857   -19.055 1.00 54.37 ? 358 HOH   B O   1 
HETATM 1620 O  O   . HOH   F 5 .   ? -11.612 -13.030 -8.726  1.00 55.58 ? 359 HOH   B O   1 
HETATM 1621 O  O   . HOH   F 5 .   ? -15.158 9.888   -0.547  1.00 56.69 ? 360 HOH   B O   1 
HETATM 1622 O  O   . HOH   F 5 .   ? -19.696 -13.272 -23.377 1.00 42.40 ? 361 HOH   B O   1 
HETATM 1623 O  O   . HOH   F 5 .   ? -22.876 -5.876  0.635   1.00 44.99 ? 362 HOH   B O   1 
HETATM 1624 O  O   . HOH   F 5 .   ? -17.300 16.816  -21.993 1.00 41.94 ? 363 HOH   B O   1 
HETATM 1625 O  O   . HOH   F 5 .   ? -0.717  -13.368 -9.691  1.00 50.43 ? 364 HOH   B O   1 
HETATM 1626 O  O   . HOH   F 5 .   ? -23.799 -7.578  -2.303  1.00 53.46 ? 365 HOH   B O   1 
HETATM 1627 O  O   . HOH   F 5 .   ? -19.196 -11.904 -13.794 1.00 38.90 ? 366 HOH   B O   1 
HETATM 1628 O  O   . HOH   F 5 .   ? -17.793 28.028  -14.124 1.00 41.87 ? 367 HOH   B O   1 
HETATM 1629 O  O   . HOH   F 5 .   ? -21.342 4.361   0.000   0.50 65.32 ? 368 HOH   B O   1 
HETATM 1630 O  O   . HOH   F 5 .   ? -3.289  5.788   -16.177 1.00 50.36 ? 369 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   ? 0.9886 0.4125 0.7054 0.1987  -0.0125 -0.1530 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9722 0.4613 0.6719 0.2173  -0.0018 -0.1415 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9492 0.4422 0.6509 0.2061  0.0149  -0.1005 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.9831 0.4180 0.6797 0.2076  0.0196  -0.0795 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0171 0.5050 0.6928 0.2601  -0.0077 -0.1597 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.0844 0.6511 0.7519 0.2775  -0.0066 -0.1810 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.1056 0.6710 0.7605 0.3030  -0.0170 -0.2143 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.1010 0.7292 0.7743 0.2662  0.0058  -0.1639 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.8889 0.4473 0.5939 0.1977  0.0237  -0.0891 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.8552 0.4234 0.5587 0.1916  0.0369  -0.0559 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.8246 0.4146 0.5099 0.2226  0.0371  -0.0533 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8054 0.4342 0.4885 0.2404  0.0321  -0.0748 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.8316 0.4535 0.5497 0.1677  0.0436  -0.0466 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.8389 0.4440 0.5801 0.1372  0.0456  -0.0404 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.8206 0.4895 0.5752 0.1171  0.0507  -0.0315 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8057 0.4550 0.5958 0.0860  0.0480  -0.0343 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8159 0.3854 0.4890 0.2302  0.0432  -0.0278 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8043 0.3962 0.4629 0.2608  0.0394  -0.0270 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.7843 0.3955 0.4372 0.2571  0.0461  -0.0026 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.7851 0.3750 0.4371 0.2372  0.0563  0.0188  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8331 0.3695 0.4697 0.2937  0.0309  -0.0306 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.8879 0.3483 0.5053 0.2911  0.0376  -0.0019 52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9225 0.3218 0.5472 0.2717  0.0402  -0.0003 52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9149 0.3630 0.5062 0.3096  0.0411  0.0233  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.9673 0.2955 0.5780 0.2661  0.0507  0.0302  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.9599 0.3379 0.5281 0.3088  0.0516  0.0545  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.9985 0.3161 0.5782 0.2851  0.0586  0.0600  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.0656 0.3132 0.6265 0.2801  0.0737  0.0952  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.7621 0.4168 0.4137 0.2770  0.0400  -0.0083 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.7519 0.4269 0.3972 0.2778  0.0414  0.0078  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.7661 0.4199 0.3834 0.3149  0.0320  0.0142  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.7668 0.4166 0.3792 0.3436  0.0210  -0.0007 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.7258 0.4702 0.3975 0.2640  0.0403  -0.0033 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.7107 0.5014 0.3992 0.2833  0.0311  -0.0265 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.7229 0.4813 0.4117 0.2314  0.0494  -0.0041 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.6905 0.5432 0.4065 0.2695  0.0311  -0.0316 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.7770 0.4170 0.3720 0.3179  0.0359  0.0361  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.8058 0.4252 0.3647 0.3556  0.0263  0.0450  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8046 0.4630 0.3599 0.3578  0.0213  0.0469  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.7967 0.4566 0.3537 0.3336  0.0341  0.0607  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.8684 0.4108 0.3881 0.3627  0.0392  0.0757  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.9642 0.4522 0.4783 0.3727  0.0378  0.0729  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1077 0.5121 0.5861 0.3763  0.0524  0.1066  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.1219 0.5165 0.5871 0.3618  0.0699  0.1341  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.1738 0.5214 0.6383 0.3938  0.0476  0.1062  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.7997 0.4894 0.3509 0.3884  0.0010  0.0312  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7962 0.5207 0.3456 0.3915  -0.0083 0.0274  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.8279 0.5095 0.3256 0.4051  0.0005  0.0550  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.8644 0.4971 0.3195 0.4324  0.0030  0.0726  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.7994 0.5708 0.3628 0.4204  -0.0353 0.0003  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8145 0.6365 0.4044 0.4076  -0.0468 -0.0154 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8254 0.7020 0.4455 0.4293  -0.0742 -0.0464 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8403 0.7586 0.4900 0.4137  -0.0868 -0.0627 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8814 0.7988 0.5039 0.4375  -0.1065 -0.0693 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9311 0.8120 0.4925 0.4803  -0.1144 -0.0584 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8475 0.7974 0.5007 0.4206  -0.1192 -0.0871 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.8193 0.5163 0.3190 0.3866  0.0079  0.0608  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.8522 0.5180 0.3025 0.4010  0.0194  0.0864  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.8529 0.5481 0.2832 0.4255  -0.0001 0.0726  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.8904 0.5627 0.2698 0.4478  0.0071  0.0914  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.8568 0.5097 0.3182 0.3654  0.0469  0.1072  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.8178 0.5623 0.2866 0.4231  -0.0245 0.0399  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.8226 0.5937 0.2784 0.4462  -0.0487 0.0202  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.7993 0.6209 0.3129 0.4214  -0.0656 -0.0104 57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.7749 0.6155 0.3388 0.3859  -0.0568 -0.0148 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7998 0.6419 0.3050 0.4417  -0.0913 -0.0323 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.7846 0.6674 0.3446 0.4182  -0.1095 -0.0615 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8070 0.6757 0.3647 0.3935  -0.0943 -0.0513 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8344 0.6732 0.3408 0.4087  -0.0801 -0.0312 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7980 0.7047 0.3507 0.4516  -0.1478 -0.0939 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8559 0.7949 0.4300 0.4746  -0.1722 -0.1157 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8516 0.7871 0.4332 0.4731  -0.1581 -0.1028 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8901 0.8582 0.4718 0.4982  -0.2076 -0.1480 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.7915 0.6832 0.4042 0.3585  -0.0980 -0.0655 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8112 0.6897 0.4240 0.3386  -0.0886 -0.0595 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8388 0.7240 0.4470 0.3562  -0.1188 -0.0882 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8091 0.7189 0.4682 0.3398  -0.1401 -0.1144 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.7894 0.6786 0.4540 0.2940  -0.0733 -0.0536 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8053 0.6807 0.4597 0.2844  -0.0452 -0.0268 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.7951 0.6720 0.4647 0.2768  -0.0713 -0.0530 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8033 0.6912 0.4981 0.2493  -0.0313 -0.0215 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8786 0.7429 0.4250 0.3918  -0.1213 -0.0845 60  THR   A N   
83   N  N   B THR   A 17  ? 0.8807 0.7450 0.4277 0.3912  -0.1212 -0.0845 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.9021 0.7682 0.4301 0.4174  -0.1519 -0.1142 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.9056 0.7729 0.4353 0.4173  -0.1529 -0.1151 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9468 0.7880 0.4251 0.4328  -0.1387 -0.1026 60  THR   A C   
87   C  C   B THR   A 17  ? 0.9507 0.7925 0.4255 0.4367  -0.1408 -0.1039 60  THR   A C   
88   O  O   A THR   A 17  ? 0.9636 0.7886 0.4039 0.4395  -0.1076 -0.0698 60  THR   A O   
89   O  O   B THR   A 17  ? 0.9702 0.7954 0.4031 0.4466  -0.1106 -0.0714 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.9234 0.7988 0.4130 0.4645  -0.1784 -0.1313 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.9244 0.8072 0.4314 0.4575  -0.1808 -0.1345 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9588 0.8095 0.3794 0.4951  -0.1552 -0.0989 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.9039 0.8227 0.4807 0.4362  -0.2005 -0.1585 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.9019 0.8120 0.4449 0.4569  -0.1991 -0.1520 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9432 0.8227 0.4035 0.5002  -0.2113 -0.1615 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9636 0.8029 0.4434 0.4406  -0.1632 -0.1314 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 1.0270 0.8472 0.4565 0.4638  -0.1551 -0.1274 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.1002 0.9188 0.4548 0.5204  -0.1660 -0.1327 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.1032 0.9343 0.4556 0.5427  -0.2010 -0.1625 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 1.0151 0.8285 0.4742 0.4536  -0.1817 -0.1608 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0448 0.8411 0.4518 0.4857  -0.1818 -0.1674 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0770 0.8703 0.4334 0.5329  -0.2095 -0.1973 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0511 0.8338 0.4570 0.4741  -0.1580 -0.1505 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.0991 0.8780 0.4187 0.5532  -0.2003 -0.1977 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0836 0.8566 0.4369 0.5168  -0.1698 -0.1701 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0443 0.8248 0.4864 0.4356  -0.1290 -0.1221 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.0961 0.8596 0.4362 0.5217  -0.1523 -0.1618 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0598 0.8307 0.4892 0.4402  -0.1141 -0.1142 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0799 0.8437 0.4605 0.4828  -0.1246 -0.1332 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.1562 0.9621 0.4496 0.5448  -0.1357 -0.1032 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.2178 1.0192 0.4295 0.6014  -0.1400 -0.1016 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.2714 1.0691 0.4359 0.6356  -0.1481 -0.1203 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.2744 1.0682 0.4340 0.6270  -0.1185 -0.1010 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.2684 1.0570 0.4382 0.6087  -0.0967 -0.0510 62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.3947 1.1742 0.4705 0.6691  -0.0946 -0.0411 62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.5230 1.2840 0.5531 0.6757  -0.0449 0.0137  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.5449 1.3021 0.6206 0.6315  -0.0119 0.0420  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.5832 1.3328 0.5320 0.7252  -0.0392 0.0284  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.3099 1.1114 0.4397 0.6774  -0.1895 -0.1602 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.3658 1.1627 0.4419 0.7181  -0.2008 -0.1831 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.4216 1.2155 0.4093 0.7602  -0.1615 -0.1439 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.4398 1.2311 0.3881 0.7794  -0.1505 -0.1186 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.4098 1.2120 0.4688 0.7553  -0.2593 -0.2396 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.4504 1.2579 0.6024 0.7127  -0.2991 -0.2802 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.5125 1.3284 0.6524 0.7496  -0.3595 -0.3401 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5287 1.3554 0.7696 0.7042  -0.3973 -0.3781 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.5605 1.3953 0.7974 0.7376  -0.4591 -0.4419 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.4459 1.2402 0.4029 0.7757  -0.1393 -0.1377 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.4914 1.2891 0.3682 0.8142  -0.0960 -0.0987 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.4828 1.2781 0.3797 0.7787  -0.0437 -0.0392 64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.5119 1.3014 0.3476 0.8053  -0.0144 -0.0019 64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.5674 1.3633 0.3473 0.8829  -0.1156 -0.1101 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.6851 1.4835 0.4391 0.9236  -0.1706 -0.1734 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.7107 1.5109 0.4733 0.9258  -0.1735 -0.1958 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.7348 1.5329 0.4598 0.9559  -0.2128 -0.2028 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.4392 1.2359 0.4204 0.7193  -0.0331 -0.0307 65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.4230 1.2178 0.4315 0.6826  0.0131  0.0191  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.4147 1.2260 0.4043 0.6892  0.0582  0.0469  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.4135 1.2381 0.3838 0.7146  0.0500  0.0230  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.3938 1.1883 0.4943 0.6221  0.0052  0.0134  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.4057 1.2175 0.4037 0.6671  0.1051  0.0954  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.3949 1.2311 0.3888 0.6677  0.1514  0.1238  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.3390 1.1965 0.4047 0.6339  0.1458  0.1038  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.3102 1.1634 0.4445 0.5852  0.1423  0.1063  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.4387 1.2676 0.4418 0.6420  0.1993  0.1782  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.5090 1.3685 0.5073 0.6440  0.2523  0.2125  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.5787 1.4434 0.6503 0.5870  0.2871  0.2464  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.5872 1.4190 0.6806 0.5587  0.2821  0.2591  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.5892 1.4927 0.6981 0.5722  0.3171  0.2573  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.3238 1.2019 0.3682 0.6648  0.1423  0.0821  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.2898 1.1843 0.3901 0.6442  0.1344  0.0617  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.2537 1.1863 0.3809 0.6305  0.1840  0.0955  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.2679 1.2261 0.3486 0.6675  0.2131  0.1085  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.3070 1.1990 0.3749 0.6862  0.0990  0.0148  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.2957 1.1851 0.4280 0.6573  0.0786  -0.0087 67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.3337 1.1965 0.3599 0.7131  0.0537  -0.0186 67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.2018 1.1426 0.4040 0.5792  0.1938  0.1084  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.1593 1.1423 0.4002 0.5619  0.2373  0.1369  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.1187 1.1137 0.4377 0.5221  0.2245  0.1245  68  THR   A C   
160  O  O   . THR   A 25  ? 1.1199 1.0854 0.4603 0.5036  0.1879  0.1017  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.1658 1.1481 0.4073 0.5413  0.2782  0.1832  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.1457 1.1760 0.4118 0.5365  0.3252  0.2108  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.1604 1.1168 0.4565 0.4898  0.2677  0.1905  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0798 1.1208 0.4397 0.5119  0.2546  0.1392  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.0441 1.1005 0.4733 0.4796  0.2428  0.1288  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.0263 1.0948 0.4562 0.5067  0.2208  0.0976  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0492 1.0903 0.4321 0.5411  0.1933  0.0703  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.9818 1.0893 0.4676 0.4915  0.2295  0.0992  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.9685 1.0864 0.4599 0.5174  0.2087  0.0716  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9475 1.0251 0.4683 0.4916  0.1684  0.0534  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.9516 0.9986 0.4859 0.4557  0.1585  0.0610  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9533 1.1444 0.4823 0.5274  0.2420  0.0822  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9559 1.1820 0.5613 0.4809  0.2558  0.1001  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9582 1.1587 0.5843 0.4397  0.2528  0.1132  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9374 1.2265 0.5874 0.4894  0.2702  0.0983  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.9308 1.0040 0.4552 0.5133  0.1453  0.0298  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.9315 0.9613 0.4748 0.4950  0.1091  0.0153  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.8932 0.9578 0.4801 0.4953  0.1086  0.0145  71  SER   A C   
179  O  O   . SER   A 28  ? 0.9049 0.9559 0.4805 0.5258  0.0882  -0.0058 71  SER   A O   
180  C  CB  . SER   A 28  ? 0.9852 0.9589 0.4849 0.5239  0.0742  -0.0147 71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.0457 1.0041 0.4979 0.5431  0.0746  -0.0215 71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.8506 0.9583 0.4880 0.4634  0.1277  0.0342  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.8150 0.9647 0.4952 0.4682  0.1250  0.0306  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.8124 0.9210 0.5012 0.4564  0.0906  0.0222  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.8227 0.8949 0.5136 0.4220  0.0804  0.0298  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.7893 1.0005 0.5224 0.4366  0.1568  0.0523  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.8118 0.9840 0.5335 0.4007  0.1609  0.0670  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.8317 0.9531 0.4903 0.4248  0.1512  0.0582  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.7995 0.9148 0.4913 0.4872  0.0741  0.0079  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.8129 0.8890 0.5084 0.4807  0.0436  0.0042  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.7554 0.8937 0.5042 0.4655  0.0501  0.0124  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.7269 0.9294 0.5043 0.4894  0.0606  0.0067  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.8695 0.9062 0.5336 0.5250  0.0180  -0.0158 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.9749 0.9560 0.5908 0.5420  0.0096  -0.0300 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.0804 0.9776 0.6664 0.5552  -0.0262 -0.0443 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.1704 1.0222 0.7164 0.5746  -0.0369 -0.0645 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.2416 1.0145 0.7625 0.5842  -0.0681 -0.0811 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.2577 0.9832 0.7848 0.5757  -0.0883 -0.0747 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.2522 0.9906 0.7407 0.6023  -0.0800 -0.1042 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.7299 0.8560 0.4952 0.4258  0.0452  0.0240  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.6751 0.8595 0.4917 0.4083  0.0482  0.0281  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.6764 0.8315 0.4873 0.4049  0.0188  0.0272  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.7115 0.8016 0.4888 0.3899  0.0061  0.0333  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6552 0.8592 0.4986 0.3651  0.0708  0.0415  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6565 0.8824 0.4996 0.3643  0.1035  0.0495  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.6468 0.8797 0.5142 0.3222  0.1220  0.0641  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.6318 0.9333 0.5081 0.3907  0.1236  0.0454  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.6361 0.8435 0.4812 0.4184  0.0091  0.0205  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.6390 0.8245 0.4748 0.4187  -0.0187 0.0211  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5955 0.8061 0.4618 0.3772  -0.0135 0.0262  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5529 0.8352 0.4746 0.3658  -0.0011 0.0206  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.6526 0.8862 0.5096 0.4577  -0.0354 0.0083  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7659 0.9601 0.5845 0.5045  -0.0485 0.0012  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.8224 0.9390 0.5933 0.5040  -0.0506 0.0062  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.7846 1.0259 0.6231 0.5428  -0.0582 -0.0116 75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.6033 0.7560 0.4368 0.3532  -0.0205 0.0362  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.5749 0.7443 0.4307 0.3165  -0.0165 0.0385  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.5878 0.7308 0.4173 0.3158  -0.0407 0.0407  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.6287 0.7250 0.4150 0.3384  -0.0568 0.0470  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5836 0.7241 0.4319 0.2846  0.0053  0.0477  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5723 0.7387 0.4388 0.2879  0.0306  0.0485  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.6242 0.6895 0.4197 0.2819  -0.0017 0.0568  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.5488 0.7220 0.4038 0.2918  -0.0432 0.0353  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.5510 0.7072 0.3791 0.2903  -0.0634 0.0358  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.5426 0.6810 0.3688 0.2540  -0.0515 0.0386  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5231 0.6857 0.3880 0.2307  -0.0343 0.0339  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.5142 0.7344 0.3777 0.3039  -0.0845 0.0179  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.5541 0.6492 0.3342 0.2509  -0.0588 0.0477  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.5571 0.6363 0.3319 0.2219  -0.0486 0.0487  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.5669 0.6590 0.3264 0.2244  -0.0669 0.0401  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.6015 0.6717 0.3157 0.2456  -0.0805 0.0494  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.5793 0.5988 0.3147 0.2145  -0.0355 0.0667  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.5855 0.5885 0.3105 0.1899  -0.0255 0.0684  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.5679 0.5909 0.3318 0.1689  -0.0116 0.0590  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.6085 0.5608 0.2982 0.1858  -0.0167 0.0855  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.5395 0.6668 0.3354 0.2058  -0.0691 0.0216  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.5484 0.6915 0.3288 0.2117  -0.0905 0.0072  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.5839 0.6899 0.3232 0.1989  -0.0820 0.0131  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.5978 0.6708 0.3299 0.1828  -0.0603 0.0267  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.5199 0.7235 0.3629 0.2028  -0.1052 -0.0220 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.5413 0.7515 0.4324 0.1678  -0.0894 -0.0322 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.5649 0.7340 0.4311 0.1530  -0.0732 -0.0223 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.5352 0.7920 0.4904 0.1556  -0.0939 -0.0500 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.5946 0.7107 0.3065 0.2096  -0.1002 0.0011  80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.6236 0.7157 0.2939 0.2044  -0.0942 0.0030  80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.6057 0.6939 0.3094 0.1751  -0.0792 -0.0083 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.6278 0.6880 0.3034 0.1679  -0.0636 0.0013  80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.6737 0.7888 0.3131 0.2266  -0.1210 -0.0149 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.7924 0.8835 0.3708 0.2324  -0.1136 -0.0075 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.8978 1.0044 0.4240 0.2648  -0.1383 -0.0163 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.8959 1.0339 0.4346 0.2682  -0.1605 -0.0507 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.9634 1.0481 0.4346 0.2880  -0.1368 0.0108  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.5622 0.6769 0.3275 0.1584  -0.0817 -0.0261 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.5460 0.6486 0.3412 0.1320  -0.0670 -0.0335 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.5409 0.6158 0.3424 0.1202  -0.0399 -0.0103 81  SER   A C   
256  O  O   . SER   A 38  ? 0.5295 0.5926 0.3555 0.1012  -0.0270 -0.0130 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.5319 0.6687 0.3915 0.1160  -0.0786 -0.0591 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.5675 0.7319 0.4253 0.1271  -0.1082 -0.0867 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.5418 0.6036 0.3197 0.1332  -0.0334 0.0108  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.5466 0.5837 0.3265 0.1265  -0.0127 0.0285  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.5234 0.5804 0.3495 0.1191  -0.0039 0.0274  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.5263 0.5648 0.3544 0.1132  0.0135  0.0385  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.4963 0.5949 0.3595 0.1212  -0.0155 0.0143  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.4754 0.6027 0.3882 0.1137  -0.0036 0.0146  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4807 0.6276 0.3928 0.1372  -0.0059 0.0214  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4866 0.6513 0.3895 0.1565  -0.0264 0.0146  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4502 0.6183 0.4192 0.0971  -0.0132 -0.0067 83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.4786 0.6227 0.4529 0.0746  -0.0114 -0.0162 83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.4915 0.5956 0.4424 0.0681  0.0059  -0.0027 83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.4885 0.6542 0.4912 0.0656  -0.0297 -0.0397 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4790 0.6228 0.3982 0.1393  0.0139  0.0337  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4767 0.6388 0.3963 0.1642  0.0136  0.0376  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4682 0.6967 0.4496 0.1637  0.0149  0.0267  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4471 0.7010 0.4754 0.1382  0.0244  0.0211  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4744 0.6068 0.3708 0.1709  0.0332  0.0520  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.5028 0.5775 0.3453 0.1766  0.0279  0.0604  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.5225 0.5762 0.3337 0.1987  0.0124  0.0627  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.5153 0.5568 0.3419 0.1595  0.0381  0.0660  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5572 0.5584 0.3275 0.1986  0.0093  0.0714  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5454 0.5423 0.3328 0.1624  0.0338  0.0722  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5581 0.5355 0.3203 0.1794  0.0204  0.0753  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4792 0.7355 0.4639 0.1919  0.0055  0.0234  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4675 0.7964 0.5150 0.1961  0.0076  0.0124  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.5017 0.8428 0.5367 0.2320  0.0106  0.0164  85  SER   A C   
285  O  O   . SER   A 42  ? 0.5367 0.8299 0.5155 0.2558  -0.0019 0.0220  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4638 0.8341 0.5408 0.1976  -0.0218 -0.0087 85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.5212 0.8645 0.5446 0.2272  -0.0485 -0.0097 85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4913 0.8948 0.5791 0.2360  0.0281  0.0135  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5242 0.9455 0.6015 0.2752  0.0304  0.0133  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5364 0.9959 0.6277 0.3045  -0.0004 -0.0034 86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.4999 1.0198 0.6485 0.2931  -0.0113 -0.0183 86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4984 0.9768 0.6227 0.2729  0.0648  0.0181  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5511 0.9874 0.6457 0.2576  0.0960  0.0376  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5256 1.0225 0.6628 0.2585  0.1330  0.0457  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.6129 0.9767 0.6292 0.2837  0.0878  0.0427  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5876 1.0095 0.6268 0.3431  -0.0167 -0.0022 87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.6035 1.0496 0.6421 0.3806  -0.0476 -0.0153 87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6014 1.1122 0.6779 0.4129  -0.0379 -0.0247 87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6190 1.1062 0.6699 0.4283  -0.0194 -0.0176 87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6651 1.0217 0.6215 0.4046  -0.0690 -0.0049 87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6710 1.0404 0.6155 0.4533  -0.0982 -0.0143 87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6966 1.0025 0.6192 0.3763  -0.0781 0.0038  87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5775 1.1741 0.7163 0.4249  -0.0506 -0.0429 88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.5664 1.2370 0.7478 0.4591  -0.0414 -0.0540 88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.5516 1.2737 0.7558 0.4974  -0.0787 -0.0748 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.5777 1.2758 0.7404 0.5473  -0.0975 -0.0782 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.5600 1.3143 0.8243 0.4267  -0.0035 -0.0541 88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.6605 1.3686 0.9017 0.3932  0.0342  -0.0321 88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.7392 1.4967 1.0056 0.4037  0.0747  -0.0251 88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.7318 1.5565 1.0284 0.4420  0.0746  -0.0381 88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.7795 1.5094 1.0323 0.3766  0.1070  -0.0063 88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.7214 0.7079 0.5878 0.2077  0.0722  -0.0788 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.7330 0.7103 0.5992 0.2204  0.0671  -0.0792 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.7276 0.7134 0.6061 0.2163  0.0611  -0.0749 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.7220 0.7328 0.6173 0.2104  0.0593  -0.0764 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.7199 0.6854 0.5902 0.2201  0.0572  -0.0691 17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.7054 0.6754 0.5827 0.2204  0.0497  -0.0662 17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.6832 0.6583 0.5669 0.2029  0.0476  -0.0615 17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.6936 0.6555 0.5685 0.1938  0.0503  -0.0551 17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.7469 0.6971 0.6114 0.2324  0.0472  -0.0605 17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 0.8038 0.7598 0.6725 0.2388  0.0379  -0.0605 17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 0.8809 0.8228 0.7359 0.2557  0.0360  -0.0551 17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 0.8893 0.8150 0.7329 0.2556  0.0424  -0.0462 17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 0.9043 0.8520 0.7604 0.2693  0.0278  -0.0592 17  GLU   B OE2 
325  N  N   A THR   B 9   ? 0.6616 0.6555 0.5613 0.1979  0.0417  -0.0644 18  THR   B N   
326  N  N   B THR   B 9   ? 0.6617 0.6556 0.5614 0.1980  0.0417  -0.0645 18  THR   B N   
327  C  CA  A THR   B 9   ? 0.6546 0.6510 0.5603 0.1813  0.0381  -0.0596 18  THR   B CA  
328  C  CA  B THR   B 9   ? 0.6544 0.6517 0.5608 0.1815  0.0380  -0.0599 18  THR   B CA  
329  C  C   A THR   B 9   ? 0.6396 0.6339 0.5507 0.1843  0.0247  -0.0602 18  THR   B C   
330  C  C   B THR   B 9   ? 0.6398 0.6341 0.5508 0.1844  0.0248  -0.0603 18  THR   B C   
331  O  O   A THR   B 9   ? 0.6381 0.6339 0.5559 0.1715  0.0189  -0.0574 18  THR   B O   
332  O  O   B THR   B 9   ? 0.6383 0.6339 0.5559 0.1715  0.0191  -0.0573 18  THR   B O   
333  C  CB  A THR   B 9   ? 0.6649 0.6835 0.5850 0.1673  0.0431  -0.0597 18  THR   B CB  
334  C  CB  B THR   B 9   ? 0.6633 0.6851 0.5863 0.1694  0.0418  -0.0610 18  THR   B CB  
335  O  OG1 A THR   B 9   ? 0.6793 0.7083 0.5980 0.1737  0.0524  -0.0642 18  THR   B OG1 
336  O  OG1 B THR   B 9   ? 0.6634 0.7060 0.6024 0.1777  0.0382  -0.0677 18  THR   B OG1 
337  C  CG2 A THR   B 9   ? 0.6731 0.6857 0.5885 0.1504  0.0459  -0.0523 18  THR   B CG2 
338  C  CG2 B THR   B 9   ? 0.6745 0.6981 0.5893 0.1658  0.0538  -0.0604 18  THR   B CG2 
339  N  N   . THR   B 10  ? 0.6297 0.6188 0.5359 0.2023  0.0189  -0.0641 19  THR   B N   
340  C  CA  . THR   B 10  ? 0.6105 0.5957 0.5179 0.2098  0.0045  -0.0668 19  THR   B CA  
341  C  C   . THR   B 10  ? 0.5913 0.5592 0.4852 0.2064  0.0008  -0.0602 19  THR   B C   
342  O  O   . THR   B 10  ? 0.5955 0.5527 0.4753 0.2070  0.0096  -0.0535 19  THR   B O   
343  C  CB  . THR   B 10  ? 0.6361 0.6184 0.5357 0.2334  0.0012  -0.0716 19  THR   B CB  
344  O  OG1 . THR   B 10  ? 0.6491 0.6468 0.5587 0.2381  0.0060  -0.0776 19  THR   B OG1 
345  C  CG2 . THR   B 10  ? 0.6373 0.6177 0.5379 0.2447  -0.0158 -0.0773 19  THR   B CG2 
346  N  N   . ASP   B 11  ? 0.5699 0.5350 0.4685 0.2027  -0.0131 -0.0622 20  ASP   B N   
347  C  CA  . ASP   B 11  ? 0.5723 0.5209 0.4563 0.2030  -0.0191 -0.0576 20  ASP   B CA  
348  C  C   . ASP   B 11  ? 0.5794 0.5183 0.4430 0.2245  -0.0175 -0.0548 20  ASP   B C   
349  O  O   . ASP   B 11  ? 0.5766 0.5182 0.4380 0.2419  -0.0197 -0.0592 20  ASP   B O   
350  C  CB  . ASP   B 11  ? 0.5851 0.5288 0.4759 0.2013  -0.0386 -0.0630 20  ASP   B CB  
351  C  CG  . ASP   B 11  ? 0.6409 0.5889 0.5482 0.1772  -0.0413 -0.0605 20  ASP   B CG  
352  O  OD1 . ASP   B 11  ? 0.6325 0.5921 0.5475 0.1631  -0.0273 -0.0557 20  ASP   B OD1 
353  O  OD2 . ASP   B 11  ? 0.6775 0.6160 0.5891 0.1731  -0.0583 -0.0631 20  ASP   B OD2 
354  N  N   . GLY   B 12  ? 0.5785 0.5084 0.4281 0.2236  -0.0132 -0.0468 21  GLY   B N   
355  C  CA  . GLY   B 12  ? 0.5731 0.4982 0.4052 0.2424  -0.0100 -0.0408 21  GLY   B CA  
356  C  C   . GLY   B 12  ? 0.5633 0.4859 0.3877 0.2347  0.0015  -0.0296 21  GLY   B C   
357  O  O   . GLY   B 12  ? 0.5618 0.4842 0.3921 0.2157  0.0057  -0.0278 21  GLY   B O   
358  N  N   . VAL   B 13  ? 0.5476 0.4701 0.3594 0.2498  0.0063  -0.0212 22  VAL   B N   
359  C  CA  . VAL   B 13  ? 0.5391 0.4624 0.3462 0.2434  0.0165  -0.0091 22  VAL   B CA  
360  C  C   . VAL   B 13  ? 0.5409 0.4639 0.3533 0.2387  0.0291  -0.0036 22  VAL   B C   
361  O  O   . VAL   B 13  ? 0.5509 0.4733 0.3629 0.2503  0.0303  -0.0056 22  VAL   B O   
362  C  CB  . VAL   B 13  ? 0.5440 0.4706 0.3358 0.2615  0.0140  -0.0012 22  VAL   B CB  
363  C  CG1 . VAL   B 13  ? 0.5479 0.4783 0.3312 0.2849  0.0157  0.0024  22  VAL   B CG1 
364  C  CG2 . VAL   B 13  ? 0.5372 0.4689 0.3280 0.2522  0.0228  0.0112  22  VAL   B CG2 
365  N  N   . TYR   B 14  ? 0.5298 0.4511 0.3470 0.2213  0.0366  0.0016  23  TYR   B N   
366  C  CA  . TYR   B 14  ? 0.5199 0.4362 0.3415 0.2155  0.0457  0.0054  23  TYR   B CA  
367  C  C   . TYR   B 14  ? 0.5215 0.4372 0.3424 0.2083  0.0522  0.0188  23  TYR   B C   
368  O  O   . TYR   B 14  ? 0.5264 0.4470 0.3467 0.2009  0.0508  0.0221  23  TYR   B O   
369  C  CB  . TYR   B 14  ? 0.5118 0.4254 0.3418 0.1999  0.0469  -0.0043 23  TYR   B CB  
370  C  CG  . TYR   B 14  ? 0.5041 0.4217 0.3394 0.2054  0.0428  -0.0159 23  TYR   B CG  
371  C  CD1 . TYR   B 14  ? 0.5059 0.4300 0.3441 0.2081  0.0337  -0.0223 23  TYR   B CD1 
372  C  CD2 . TYR   B 14  ? 0.5097 0.4250 0.3484 0.2066  0.0471  -0.0210 23  TYR   B CD2 
373  C  CE1 . TYR   B 14  ? 0.5083 0.4392 0.3553 0.2114  0.0291  -0.0322 23  TYR   B CE1 
374  C  CE2 . TYR   B 14  ? 0.5143 0.4381 0.3600 0.2119  0.0436  -0.0313 23  TYR   B CE2 
375  C  CZ  . TYR   B 14  ? 0.5208 0.4540 0.3724 0.2133  0.0348  -0.0365 23  TYR   B CZ  
376  O  OH  . TYR   B 14  ? 0.5289 0.4736 0.3913 0.2166  0.0305  -0.0459 23  TYR   B OH  
377  N  N   . ARG   B 15  ? 0.5177 0.4270 0.3401 0.2090  0.0584  0.0264  24  ARG   B N   
378  C  CA  . ARG   B 15  ? 0.5151 0.4230 0.3415 0.1988  0.0637  0.0398  24  ARG   B CA  
379  C  C   . ARG   B 15  ? 0.5174 0.4143 0.3498 0.1802  0.0639  0.0330  24  ARG   B C   
380  O  O   . ARG   B 15  ? 0.5253 0.4134 0.3574 0.1802  0.0633  0.0223  24  ARG   B O   
381  C  CB  . ARG   B 15  ? 0.5259 0.4285 0.3515 0.2075  0.0692  0.0526  24  ARG   B CB  
382  C  CG  . ARG   B 15  ? 0.5311 0.4446 0.3481 0.2296  0.0703  0.0607  24  ARG   B CG  
383  C  CD  . ARG   B 15  ? 0.5504 0.4567 0.3666 0.2364  0.0767  0.0747  24  ARG   B CD  
384  N  NE  . ARG   B 15  ? 0.5624 0.4776 0.3671 0.2612  0.0778  0.0801  24  ARG   B NE  
385  C  CZ  . ARG   B 15  ? 0.5706 0.5032 0.3708 0.2726  0.0817  0.0954  24  ARG   B CZ  
386  N  NH1 . ARG   B 15  ? 0.5296 0.4741 0.3382 0.2604  0.0854  0.1077  24  ARG   B NH1 
387  N  NH2 . ARG   B 15  ? 0.5855 0.5255 0.3722 0.2981  0.0817  0.0982  24  ARG   B NH2 
388  N  N   . VAL   B 16  ? 0.5116 0.4100 0.3486 0.1663  0.0644  0.0390  25  VAL   B N   
389  C  CA  . VAL   B 16  ? 0.5243 0.4118 0.3649 0.1501  0.0632  0.0331  25  VAL   B CA  
390  C  C   . VAL   B 16  ? 0.5461 0.4238 0.3932 0.1437  0.0649  0.0454  25  VAL   B C   
391  O  O   . VAL   B 16  ? 0.5419 0.4295 0.3952 0.1404  0.0665  0.0596  25  VAL   B O   
392  C  CB  . VAL   B 16  ? 0.5268 0.4225 0.3677 0.1389  0.0604  0.0298  25  VAL   B CB  
393  C  CG1 . VAL   B 16  ? 0.5345 0.4186 0.3763 0.1251  0.0586  0.0218  25  VAL   B CG1 
394  C  CG2 . VAL   B 16  ? 0.5230 0.4272 0.3584 0.1450  0.0578  0.0213  25  VAL   B CG2 
395  N  N   . MET   B 17  ? 0.5720 0.4306 0.4180 0.1427  0.0641  0.0406  26  MET   B N   
396  C  CA  . MET   B 17  ? 0.6017 0.4446 0.4533 0.1368  0.0638  0.0518  26  MET   B CA  
397  C  C   . MET   B 17  ? 0.6442 0.4679 0.4974 0.1222  0.0575  0.0436  26  MET   B C   
398  O  O   . MET   B 17  ? 0.6517 0.4737 0.4985 0.1208  0.0550  0.0279  26  MET   B O   
399  C  CB  . MET   B 17  ? 0.6085 0.4384 0.4539 0.1511  0.0659  0.0526  26  MET   B CB  
400  C  CG  . MET   B 17  ? 0.6160 0.4619 0.4559 0.1696  0.0702  0.0553  26  MET   B CG  
401  S  SD  . MET   B 17  ? 0.6341 0.4986 0.4791 0.1742  0.0758  0.0794  26  MET   B SD  
402  C  CE  . MET   B 17  ? 0.6312 0.4734 0.4822 0.1676  0.0774  0.0961  26  MET   B CE  
403  N  N   . THR   B 18  ? 0.6711 0.4792 0.5322 0.1124  0.0543  0.0546  27  THR   B N   
404  C  CA  . THR   B 18  ? 0.7077 0.4925 0.5693 0.0999  0.0453  0.0465  27  THR   B CA  
405  C  C   . THR   B 18  ? 0.7420 0.4997 0.6079 0.0964  0.0411  0.0568  27  THR   B C   
406  O  O   . THR   B 18  ? 0.7339 0.4977 0.6097 0.0953  0.0455  0.0768  27  THR   B O   
407  C  CB  . THR   B 18  ? 0.7191 0.5153 0.5899 0.0841  0.0410  0.0479  27  THR   B CB  
408  O  OG1 . THR   B 18  ? 0.7408 0.5125 0.6097 0.0740  0.0303  0.0375  27  THR   B OG1 
409  C  CG2 . THR   B 18  ? 0.7125 0.5253 0.6005 0.0757  0.0435  0.0700  27  THR   B CG2 
410  N  N   . ARG   B 19  ? 0.7815 0.5089 0.6386 0.0959  0.0325  0.0438  28  ARG   B N   
411  C  CA  . ARG   B 19  ? 0.8237 0.5185 0.6834 0.0913  0.0255  0.0522  28  ARG   B CA  
412  C  C   . ARG   B 19  ? 0.8459 0.5211 0.7146 0.0716  0.0118  0.0512  28  ARG   B C   
413  O  O   . ARG   B 19  ? 0.8629 0.5022 0.7297 0.0674  0.0011  0.0508  28  ARG   B O   
414  C  CB  . ARG   B 19  ? 0.8702 0.5395 0.7114 0.1079  0.0231  0.0385  28  ARG   B CB  
415  C  CG  . ARG   B 19  ? 0.9317 0.6061 0.7688 0.1240  0.0324  0.0485  28  ARG   B CG  
416  C  CD  . ARG   B 19  ? 1.0034 0.6725 0.8224 0.1437  0.0332  0.0291  28  ARG   B CD  
417  N  NE  . ARG   B 19  ? 1.0638 0.7441 0.8787 0.1608  0.0418  0.0357  28  ARG   B NE  
418  C  CZ  . ARG   B 19  ? 1.1080 0.8019 0.9133 0.1780  0.0456  0.0217  28  ARG   B CZ  
419  N  NH1 . ARG   B 19  ? 1.1131 0.8137 0.9128 0.1798  0.0435  0.0022  28  ARG   B NH1 
420  N  NH2 . ARG   B 19  ? 1.1038 0.8066 0.9056 0.1936  0.0516  0.0278  28  ARG   B NH2 
421  N  N   . ARG   B 20  ? 0.8453 0.5426 0.7235 0.0601  0.0109  0.0506  29  ARG   B N   
422  C  CA  . ARG   B 20  ? 0.8647 0.5485 0.7522 0.0420  -0.0029 0.0479  29  ARG   B CA  
423  C  C   . ARG   B 20  ? 0.8600 0.5450 0.7727 0.0242  -0.0057 0.0726  29  ARG   B C   
424  O  O   . ARG   B 20  ? 0.8706 0.5265 0.7914 0.0104  -0.0202 0.0741  29  ARG   B O   
425  C  CB  . ARG   B 20  ? 0.8848 0.5933 0.7704 0.0389  -0.0025 0.0368  29  ARG   B CB  
426  C  CG  . ARG   B 20  ? 0.9439 0.6415 0.8387 0.0216  -0.0176 0.0330  29  ARG   B CG  
427  C  CD  . ARG   B 20  ? 0.9954 0.7180 0.8867 0.0203  -0.0166 0.0232  29  ARG   B CD  
428  N  NE  . ARG   B 20  ? 1.0322 0.7933 0.9344 0.0202  -0.0042 0.0378  29  ARG   B NE  
429  C  CZ  . ARG   B 20  ? 1.0573 0.8387 0.9800 0.0068  -0.0058 0.0525  29  ARG   B CZ  
430  N  NH1 . ARG   B 20  ? 1.0578 0.8254 0.9958 -0.0101 -0.0197 0.0555  29  ARG   B NH1 
431  N  NH2 . ARG   B 20  ? 1.0435 0.8595 0.9719 0.0109  0.0054  0.0640  29  ARG   B NH2 
432  N  N   . LEU   B 21  ? 0.8388 0.5575 0.7640 0.0251  0.0074  0.0925  30  LEU   B N   
433  C  CA  . LEU   B 21  ? 0.8297 0.5577 0.7806 0.0098  0.0077  0.1197  30  LEU   B CA  
434  C  C   . LEU   B 21  ? 0.8291 0.5327 0.7794 0.0140  0.0099  0.1345  30  LEU   B C   
435  O  O   . LEU   B 21  ? 0.8457 0.5166 0.7766 0.0249  0.0055  0.1201  30  LEU   B O   
436  C  CB  . LEU   B 21  ? 0.8189 0.5961 0.7807 0.0127  0.0213  0.1348  30  LEU   B CB  
437  C  CG  . LEU   B 21  ? 0.8351 0.6386 0.8012 0.0068  0.0191  0.1262  30  LEU   B CG  
438  C  CD1 . LEU   B 21  ? 0.8476 0.6341 0.8263 -0.0139 0.0022  0.1202  30  LEU   B CD1 
439  C  CD2 . LEU   B 21  ? 0.8528 0.6617 0.7949 0.0230  0.0234  0.1041  30  LEU   B CD2 
440  N  N   . LEU   B 22  ? 0.8053 0.5253 0.7759 0.0062  0.0167  0.1638  31  LEU   B N   
441  C  CA  . LEU   B 22  ? 0.8082 0.5084 0.7781 0.0107  0.0204  0.1815  31  LEU   B CA  
442  C  C   . LEU   B 22  ? 0.8049 0.5182 0.7527 0.0381  0.0349  0.1771  31  LEU   B C   
443  O  O   . LEU   B 22  ? 0.8033 0.5548 0.7491 0.0482  0.0456  0.1768  31  LEU   B O   
444  C  CB  . LEU   B 22  ? 0.7908 0.5146 0.7900 -0.0046 0.0260  0.2161  31  LEU   B CB  
445  C  CG  . LEU   B 22  ? 0.8103 0.5140 0.8132 -0.0047 0.0293  0.2403  31  LEU   B CG  
446  C  CD1 . LEU   B 22  ? 0.8237 0.4787 0.8372 -0.0262 0.0102  0.2422  31  LEU   B CD1 
447  C  CD2 . LEU   B 22  ? 0.7981 0.5459 0.8227 -0.0078 0.0441  0.2746  31  LEU   B CD2 
448  N  N   . GLY   B 23  ? 0.7998 0.4801 0.7303 0.0504  0.0333  0.1720  32  GLY   B N   
449  C  CA  . GLY   B 23  ? 0.7891 0.4774 0.6985 0.0766  0.0441  0.1656  32  GLY   B CA  
450  C  C   . GLY   B 23  ? 0.7709 0.4800 0.6668 0.0891  0.0470  0.1408  32  GLY   B C   
451  O  O   . GLY   B 23  ? 0.7782 0.4794 0.6715 0.0818  0.0384  0.1211  32  GLY   B O   
452  N  N   . SER   B 24  ? 0.7430 0.4788 0.6302 0.1081  0.0586  0.1423  33  SER   B N   
453  C  CA  . SER   B 24  ? 0.7221 0.4787 0.5987 0.1191  0.0611  0.1218  33  SER   B CA  
454  C  C   . SER   B 24  ? 0.6801 0.4756 0.5675 0.1167  0.0681  0.1337  33  SER   B C   
455  O  O   . SER   B 24  ? 0.6716 0.4858 0.5611 0.1262  0.0768  0.1521  33  SER   B O   
456  C  CB  . SER   B 24  ? 0.7443 0.5009 0.6032 0.1431  0.0662  0.1133  33  SER   B CB  
457  O  OG  . SER   B 24  ? 0.7845 0.5078 0.6316 0.1484  0.0598  0.1002  33  SER   B OG  
458  N  N   . THR   B 25  ? 0.6543 0.4623 0.5470 0.1057  0.0642  0.1237  34  THR   B N   
459  C  CA  . THR   B 25  ? 0.6273 0.4708 0.5291 0.1039  0.0692  0.1338  34  THR   B CA  
460  C  C   . THR   B 25  ? 0.6112 0.4721 0.5004 0.1157  0.0708  0.1167  34  THR   B C   
461  O  O   . THR   B 25  ? 0.6168 0.4658 0.4982 0.1132  0.0654  0.0965  34  THR   B O   
462  C  CB  . THR   B 25  ? 0.6350 0.4814 0.5559 0.0807  0.0628  0.1407  34  THR   B CB  
463  O  OG1 . THR   B 25  ? 0.6615 0.4905 0.5964 0.0687  0.0603  0.1585  34  THR   B OG1 
464  C  CG2 . THR   B 25  ? 0.6135 0.4990 0.5446 0.0797  0.0678  0.1520  34  THR   B CG2 
465  N  N   . GLN   B 26  ? 0.5871 0.4757 0.4739 0.1289  0.0775  0.1255  35  GLN   B N   
466  C  CA  . GLN   B 26  ? 0.5751 0.4775 0.4505 0.1393  0.0769  0.1108  35  GLN   B CA  
467  C  C   . GLN   B 26  ? 0.5742 0.4920 0.4566 0.1271  0.0738  0.1097  35  GLN   B C   
468  O  O   . GLN   B 26  ? 0.5708 0.5106 0.4633 0.1249  0.0768  0.1260  35  GLN   B O   
469  C  CB  . GLN   B 26  ? 0.5600 0.4808 0.4258 0.1620  0.0826  0.1176  35  GLN   B CB  
470  C  CG  . GLN   B 26  ? 0.5467 0.4783 0.4013 0.1719  0.0792  0.1026  35  GLN   B CG  
471  C  CD  . GLN   B 26  ? 0.5429 0.4870 0.3855 0.1961  0.0816  0.1054  35  GLN   B CD  
472  O  OE1 . GLN   B 26  ? 0.5533 0.4896 0.3901 0.2084  0.0840  0.1075  35  GLN   B OE1 
473  N  NE2 . GLN   B 26  ? 0.5294 0.4914 0.3657 0.2051  0.0795  0.1042  35  GLN   B NE2 
474  N  N   . VAL   B 27  ? 0.5689 0.4774 0.4460 0.1201  0.0680  0.0911  36  VAL   B N   
475  C  CA  . VAL   B 27  ? 0.5560 0.4770 0.4367 0.1099  0.0643  0.0884  36  VAL   B CA  
476  C  C   . VAL   B 27  ? 0.5407 0.4777 0.4101 0.1218  0.0645  0.0820  36  VAL   B C   
477  O  O   . VAL   B 27  ? 0.5387 0.4885 0.4092 0.1169  0.0619  0.0823  36  VAL   B O   
478  C  CB  . VAL   B 27  ? 0.5772 0.4792 0.4580 0.0946  0.0573  0.0741  36  VAL   B CB  
479  C  CG1 . VAL   B 27  ? 0.5914 0.4784 0.4853 0.0805  0.0535  0.0818  36  VAL   B CG1 
480  C  CG2 . VAL   B 27  ? 0.5874 0.4730 0.4548 0.1010  0.0565  0.0561  36  VAL   B CG2 
481  N  N   . GLY   B 28  ? 0.5275 0.4621 0.3859 0.1372  0.0659  0.0758  37  GLY   B N   
482  C  CA  . GLY   B 28  ? 0.5170 0.4612 0.3643 0.1482  0.0633  0.0687  37  GLY   B CA  
483  C  C   . GLY   B 28  ? 0.5145 0.4517 0.3524 0.1625  0.0624  0.0596  37  GLY   B C   
484  O  O   . GLY   B 28  ? 0.5190 0.4469 0.3580 0.1671  0.0652  0.0602  37  GLY   B O   
485  N  N   . VAL   B 29  ? 0.5103 0.4509 0.3394 0.1696  0.0573  0.0511  38  VAL   B N   
486  C  CA  . VAL   B 29  ? 0.5146 0.4511 0.3361 0.1831  0.0534  0.0416  38  VAL   B CA  
487  C  C   . VAL   B 29  ? 0.5100 0.4405 0.3290 0.1748  0.0470  0.0282  38  VAL   B C   
488  O  O   . VAL   B 29  ? 0.5092 0.4403 0.3284 0.1629  0.0458  0.0278  38  VAL   B O   
489  C  CB  . VAL   B 29  ? 0.5250 0.4736 0.3369 0.2043  0.0514  0.0484  38  VAL   B CB  
490  C  CG1 . VAL   B 29  ? 0.5323 0.4754 0.3359 0.2186  0.0437  0.0369  38  VAL   B CG1 
491  C  CG2 . VAL   B 29  ? 0.5258 0.4831 0.3403 0.2133  0.0594  0.0641  38  VAL   B CG2 
492  N  N   . GLY   B 30  ? 0.5020 0.4277 0.3196 0.1808  0.0429  0.0184  39  GLY   B N   
493  C  CA  . GLY   B 30  ? 0.4987 0.4204 0.3168 0.1723  0.0371  0.0083  39  GLY   B CA  
494  C  C   . GLY   B 30  ? 0.4997 0.4201 0.3174 0.1825  0.0295  0.0001  39  GLY   B C   
495  O  O   . GLY   B 30  ? 0.5006 0.4222 0.3168 0.1973  0.0291  0.0002  39  GLY   B O   
496  N  N   . VAL   B 31  ? 0.4984 0.4158 0.3175 0.1747  0.0224  -0.0064 40  VAL   B N   
497  C  CA  . VAL   B 31  ? 0.4941 0.4096 0.3161 0.1808  0.0123  -0.0144 40  VAL   B CA  
498  C  C   . VAL   B 31  ? 0.4886 0.4079 0.3243 0.1675  0.0143  -0.0205 40  VAL   B C   
499  O  O   . VAL   B 31  ? 0.4838 0.4035 0.3223 0.1520  0.0174  -0.0194 40  VAL   B O   
500  C  CB  . VAL   B 31  ? 0.5004 0.4085 0.3141 0.1828  -0.0003 -0.0155 40  VAL   B CB  
501  C  CG1 . VAL   B 31  ? 0.4994 0.4029 0.3189 0.1856  -0.0135 -0.0242 40  VAL   B CG1 
502  C  CG2 . VAL   B 31  ? 0.5140 0.4222 0.3126 0.2000  -0.0027 -0.0100 40  VAL   B CG2 
503  N  N   . MET   B 32  ? 0.4864 0.4104 0.3302 0.1747  0.0123  -0.0265 41  MET   B N   
504  C  CA  . MET   B 32  ? 0.4847 0.4175 0.3432 0.1640  0.0137  -0.0318 41  MET   B CA  
505  C  C   . MET   B 32  ? 0.4965 0.4291 0.3628 0.1627  -0.0004 -0.0365 41  MET   B C   
506  O  O   . MET   B 32  ? 0.5062 0.4356 0.3704 0.1774  -0.0103 -0.0409 41  MET   B O   
507  C  CB  . MET   B 32  ? 0.4789 0.4189 0.3428 0.1725  0.0202  -0.0358 41  MET   B CB  
508  C  CG  . MET   B 32  ? 0.4881 0.4420 0.3668 0.1631  0.0240  -0.0406 41  MET   B CG  
509  S  SD  . MET   B 32  ? 0.5283 0.4849 0.4048 0.1477  0.0368  -0.0372 41  MET   B SD  
510  C  CE  . MET   B 32  ? 0.5143 0.4628 0.3816 0.1598  0.0450  -0.0381 41  MET   B CE  
511  N  N   . GLN   B 33  ? 0.4909 0.4248 0.3648 0.1457  -0.0026 -0.0347 42  GLN   B N   
512  C  CA  . GLN   B 33  ? 0.4923 0.4239 0.3763 0.1408  -0.0175 -0.0377 42  GLN   B CA  
513  C  C   . GLN   B 33  ? 0.4834 0.4284 0.3851 0.1210  -0.0129 -0.0347 42  GLN   B C   
514  O  O   . GLN   B 33  ? 0.4874 0.4339 0.3847 0.1099  -0.0029 -0.0286 42  GLN   B O   
515  C  CB  . GLN   B 33  ? 0.5313 0.4432 0.4008 0.1427  -0.0298 -0.0356 42  GLN   B CB  
516  C  CG  . GLN   B 33  ? 0.5963 0.5002 0.4756 0.1382  -0.0487 -0.0395 42  GLN   B CG  
517  C  CD  . GLN   B 33  ? 0.6934 0.5740 0.5547 0.1467  -0.0645 -0.0405 42  GLN   B CD  
518  O  OE1 . GLN   B 33  ? 0.7168 0.5840 0.5796 0.1347  -0.0757 -0.0383 42  GLN   B OE1 
519  N  NE2 . GLN   B 33  ? 0.7215 0.5967 0.5642 0.1688  -0.0660 -0.0431 42  GLN   B NE2 
520  N  N   . GLU   B 34  ? 0.4728 0.4304 0.3950 0.1172  -0.0198 -0.0384 43  GLU   B N   
521  C  CA  . GLU   B 34  ? 0.4674 0.4440 0.4103 0.0985  -0.0151 -0.0336 43  GLU   B CA  
522  C  C   . GLU   B 34  ? 0.4670 0.4612 0.4091 0.0947  0.0050  -0.0304 43  GLU   B C   
523  O  O   . GLU   B 34  ? 0.4708 0.4743 0.4179 0.0798  0.0121  -0.0229 43  GLU   B O   
524  C  CB  . GLU   B 34  ? 0.5031 0.4673 0.4476 0.0818  -0.0242 -0.0260 43  GLU   B CB  
525  C  CG  . GLU   B 34  ? 0.5650 0.5085 0.5092 0.0861  -0.0468 -0.0306 43  GLU   B CG  
526  C  CD  . GLU   B 34  ? 0.6590 0.5787 0.5933 0.0757  -0.0576 -0.0243 43  GLU   B CD  
527  O  OE1 . GLU   B 34  ? 0.6618 0.5872 0.6061 0.0559  -0.0531 -0.0144 43  GLU   B OE1 
528  O  OE2 . GLU   B 34  ? 0.7127 0.6081 0.6278 0.0887  -0.0704 -0.0289 43  GLU   B OE2 
529  N  N   . GLY   B 35  ? 0.4592 0.4563 0.3937 0.1093  0.0130  -0.0360 44  GLY   B N   
530  C  CA  . GLY   B 35  ? 0.4512 0.4602 0.3819 0.1092  0.0291  -0.0354 44  GLY   B CA  
531  C  C   . GLY   B 35  ? 0.4553 0.4503 0.3669 0.1049  0.0364  -0.0307 44  GLY   B C   
532  O  O   . GLY   B 35  ? 0.4590 0.4621 0.3663 0.1029  0.0477  -0.0303 44  GLY   B O   
533  N  N   . VAL   B 36  ? 0.4542 0.4290 0.3536 0.1046  0.0289  -0.0277 45  VAL   B N   
534  C  CA  . VAL   B 36  ? 0.4586 0.4211 0.3411 0.1006  0.0337  -0.0231 45  VAL   B CA  
535  C  C   . VAL   B 36  ? 0.4515 0.3993 0.3205 0.1133  0.0320  -0.0242 45  VAL   B C   
536  O  O   . VAL   B 36  ? 0.4575 0.3985 0.3254 0.1228  0.0228  -0.0257 45  VAL   B O   
537  C  CB  . VAL   B 36  ? 0.4731 0.4281 0.3529 0.0876  0.0278  -0.0163 45  VAL   B CB  
538  C  CG1 . VAL   B 36  ? 0.4886 0.4304 0.3497 0.0865  0.0305  -0.0127 45  VAL   B CG1 
539  C  CG2 . VAL   B 36  ? 0.4667 0.4390 0.3595 0.0734  0.0331  -0.0117 45  VAL   B CG2 
540  N  N   . PHE   B 37  ? 0.4441 0.3884 0.3037 0.1143  0.0404  -0.0234 46  PHE   B N   
541  C  CA  . PHE   B 37  ? 0.4531 0.3865 0.3028 0.1238  0.0398  -0.0214 46  PHE   B CA  
542  C  C   . PHE   B 37  ? 0.4502 0.3759 0.2896 0.1176  0.0378  -0.0157 46  PHE   B C   
543  O  O   . PHE   B 37  ? 0.4481 0.3745 0.2841 0.1075  0.0421  -0.0144 46  PHE   B O   
544  C  CB  . PHE   B 37  ? 0.4567 0.3889 0.3045 0.1281  0.0479  -0.0232 46  PHE   B CB  
545  C  CG  . PHE   B 37  ? 0.4763 0.3995 0.3179 0.1372  0.0475  -0.0186 46  PHE   B CG  
546  C  CD1 . PHE   B 37  ? 0.4850 0.4079 0.3271 0.1508  0.0434  -0.0181 46  PHE   B CD1 
547  C  CD2 . PHE   B 37  ? 0.4901 0.4068 0.3260 0.1324  0.0508  -0.0139 46  PHE   B CD2 
548  C  CE1 . PHE   B 37  ? 0.4949 0.4128 0.3312 0.1598  0.0446  -0.0113 46  PHE   B CE1 
549  C  CE2 . PHE   B 37  ? 0.4980 0.4101 0.3313 0.1392  0.0511  -0.0069 46  PHE   B CE2 
550  C  CZ  . PHE   B 37  ? 0.4975 0.4110 0.3308 0.1531  0.0490  -0.0048 46  PHE   B CZ  
551  N  N   . HIS   B 38  ? 0.4483 0.3678 0.2815 0.1255  0.0305  -0.0127 47  HIS   B N   
552  C  CA  . HIS   B 38  ? 0.4531 0.3667 0.2757 0.1231  0.0270  -0.0076 47  HIS   B CA  
553  C  C   . HIS   B 38  ? 0.4584 0.3726 0.2758 0.1315  0.0300  -0.0026 47  HIS   B C   
554  O  O   . HIS   B 38  ? 0.4581 0.3736 0.2754 0.1447  0.0286  -0.0016 47  HIS   B O   
555  C  CB  . HIS   B 38  ? 0.4521 0.3588 0.2701 0.1288  0.0145  -0.0081 47  HIS   B CB  
556  C  CG  . HIS   B 38  ? 0.4748 0.3809 0.3022 0.1206  0.0091  -0.0117 47  HIS   B CG  
557  N  ND1 . HIS   B 38  ? 0.4872 0.4003 0.3272 0.1239  0.0085  -0.0167 47  HIS   B ND1 
558  C  CD2 . HIS   B 38  ? 0.4905 0.3913 0.3176 0.1087  0.0043  -0.0095 47  HIS   B CD2 
559  C  CE1 . HIS   B 38  ? 0.4909 0.4050 0.3405 0.1129  0.0033  -0.0172 47  HIS   B CE1 
560  N  NE2 . HIS   B 38  ? 0.4996 0.4054 0.3417 0.1029  0.0008  -0.0122 47  HIS   B NE2 
561  N  N   . THR   B 39  ? 0.4562 0.3707 0.2695 0.1243  0.0336  0.0015  48  THR   B N   
562  C  CA  . THR   B 39  ? 0.4546 0.3730 0.2664 0.1301  0.0359  0.0085  48  THR   B CA  
563  C  C   . THR   B 39  ? 0.4476 0.3680 0.2532 0.1239  0.0341  0.0127  48  THR   B C   
564  O  O   . THR   B 39  ? 0.4382 0.3542 0.2378 0.1173  0.0306  0.0099  48  THR   B O   
565  C  CB  . THR   B 39  ? 0.4651 0.3836 0.2847 0.1290  0.0431  0.0096  48  THR   B CB  
566  O  OG1 . THR   B 39  ? 0.4707 0.3948 0.2911 0.1356  0.0446  0.0193  48  THR   B OG1 
567  C  CG2 . THR   B 39  ? 0.4609 0.3753 0.2823 0.1156  0.0467  0.0060  48  THR   B CG2 
568  N  N   . MET   B 40  ? 0.4487 0.3769 0.2561 0.1265  0.0362  0.0204  49  MET   B N   
569  C  CA  . MET   B 40  ? 0.4614 0.3947 0.2650 0.1211  0.0344  0.0241  49  MET   B CA  
570  C  C   . MET   B 40  ? 0.4745 0.4047 0.2835 0.1067  0.0377  0.0216  49  MET   B C   
571  O  O   . MET   B 40  ? 0.4768 0.4036 0.2939 0.1034  0.0418  0.0209  49  MET   B O   
572  C  CB  . MET   B 40  ? 0.4632 0.4110 0.2682 0.1315  0.0344  0.0343  49  MET   B CB  
573  C  CG  . MET   B 40  ? 0.4961 0.4457 0.2919 0.1496  0.0299  0.0350  49  MET   B CG  
574  S  SD  . MET   B 40  ? 0.5816 0.5472 0.3676 0.1635  0.0253  0.0427  49  MET   B SD  
575  C  CE  . MET   B 40  ? 0.4961 0.4475 0.2684 0.1571  0.0164  0.0346  49  MET   B CE  
576  N  N   . TRP   B 41  ? 0.4810 0.4104 0.2835 0.0992  0.0349  0.0195  50  TRP   B N   
577  C  CA  A TRP   B 41  ? 0.4951 0.4208 0.2995 0.0876  0.0361  0.0155  50  TRP   B CA  
578  C  CA  B TRP   B 41  ? 0.4853 0.4110 0.2896 0.0877  0.0361  0.0155  50  TRP   B CA  
579  C  C   . TRP   B 41  ? 0.4923 0.4225 0.3088 0.0838  0.0368  0.0206  50  TRP   B C   
580  O  O   . TRP   B 41  ? 0.4960 0.4174 0.3168 0.0774  0.0378  0.0160  50  TRP   B O   
581  C  CB  A TRP   B 41  ? 0.5054 0.4307 0.2988 0.0826  0.0321  0.0133  50  TRP   B CB  
582  C  CB  B TRP   B 41  ? 0.4816 0.4071 0.2748 0.0828  0.0320  0.0135  50  TRP   B CB  
583  C  CG  A TRP   B 41  ? 0.5231 0.4425 0.3141 0.0734  0.0327  0.0066  50  TRP   B CG  
584  C  CG  B TRP   B 41  ? 0.4784 0.4000 0.2710 0.0734  0.0318  0.0081  50  TRP   B CG  
585  C  CD1 A TRP   B 41  ? 0.5432 0.4556 0.3271 0.0706  0.0356  -0.0002 50  TRP   B CD1 
586  C  CD1 B TRP   B 41  ? 0.4822 0.4078 0.2822 0.0681  0.0287  0.0096  50  TRP   B CD1 
587  C  CD2 A TRP   B 41  ? 0.5282 0.4491 0.3243 0.0670  0.0295  0.0059  50  TRP   B CD2 
588  C  CD2 B TRP   B 41  ? 0.4810 0.3943 0.2661 0.0692  0.0342  0.0001  50  TRP   B CD2 
589  N  NE1 A TRP   B 41  ? 0.5522 0.4608 0.3330 0.0653  0.0346  -0.0061 50  TRP   B NE1 
590  N  NE1 B TRP   B 41  ? 0.4873 0.4040 0.2830 0.0617  0.0274  0.0012  50  TRP   B NE1 
591  C  CE2 A TRP   B 41  ? 0.5454 0.4572 0.3340 0.0624  0.0297  -0.0032 50  TRP   B CE2 
592  C  CE2 B TRP   B 41  ? 0.4888 0.3990 0.2739 0.0635  0.0315  -0.0046 50  TRP   B CE2 
593  C  CE3 A TRP   B 41  ? 0.5325 0.4633 0.3399 0.0649  0.0260  0.0126  50  TRP   B CE3 
594  C  CE3 B TRP   B 41  ? 0.4890 0.3990 0.2681 0.0700  0.0381  -0.0031 50  TRP   B CE3 
595  C  CZ2 A TRP   B 41  ? 0.5582 0.4662 0.3480 0.0566  0.0244  -0.0078 50  TRP   B CZ2 
596  C  CZ2 B TRP   B 41  ? 0.4970 0.4003 0.2725 0.0615  0.0327  -0.0132 50  TRP   B CZ2 
597  C  CZ3 A TRP   B 41  ? 0.5458 0.4743 0.3582 0.0563  0.0210  0.0093  50  TRP   B CZ3 
598  C  CZ3 B TRP   B 41  ? 0.4986 0.4057 0.2706 0.0667  0.0410  -0.0095 50  TRP   B CZ3 
599  C  CH2 A TRP   B 41  ? 0.5554 0.4708 0.3579 0.0526  0.0192  -0.0017 50  TRP   B CH2 
600  C  CH2 B TRP   B 41  ? 0.4988 0.4023 0.2674 0.0639  0.0385  -0.0151 50  TRP   B CH2 
601  N  N   . HIS   B 42  ? 0.4902 0.4343 0.3125 0.0877  0.0356  0.0304  51  HIS   B N   
602  C  CA  . HIS   B 42  ? 0.4935 0.4445 0.3311 0.0815  0.0360  0.0382  51  HIS   B CA  
603  C  C   . HIS   B 42  ? 0.4989 0.4430 0.3459 0.0829  0.0405  0.0416  51  HIS   B C   
604  O  O   . HIS   B 42  ? 0.4977 0.4414 0.3575 0.0750  0.0398  0.0475  51  HIS   B O   
605  C  CB  . HIS   B 42  ? 0.4892 0.4627 0.3327 0.0859  0.0348  0.0499  51  HIS   B CB  
606  C  CG  . HIS   B 42  ? 0.4983 0.4838 0.3420 0.1008  0.0389  0.0592  51  HIS   B CG  
607  N  ND1 . HIS   B 42  ? 0.5200 0.5076 0.3487 0.1148  0.0370  0.0567  51  HIS   B ND1 
608  C  CD2 . HIS   B 42  ? 0.5014 0.4959 0.3570 0.1045  0.0440  0.0708  51  HIS   B CD2 
609  C  CE1 . HIS   B 42  ? 0.5150 0.5136 0.3457 0.1282  0.0406  0.0655  51  HIS   B CE1 
610  N  NE2 . HIS   B 42  ? 0.5080 0.5125 0.3548 0.1226  0.0459  0.0750  51  HIS   B NE2 
611  N  N   . VAL   B 43  ? 0.5066 0.4443 0.3474 0.0924  0.0439  0.0382  52  VAL   B N   
612  C  CA  . VAL   B 43  ? 0.5143 0.4442 0.3613 0.0956  0.0478  0.0406  52  VAL   B CA  
613  C  C   . VAL   B 43  ? 0.5289 0.4404 0.3760 0.0866  0.0465  0.0307  52  VAL   B C   
614  O  O   . VAL   B 43  ? 0.5356 0.4387 0.3914 0.0812  0.0458  0.0346  52  VAL   B O   
615  C  CB  . VAL   B 43  ? 0.5238 0.4541 0.3639 0.1102  0.0503  0.0387  52  VAL   B CB  
616  C  CG1 . VAL   B 43  ? 0.5274 0.4466 0.3709 0.1139  0.0537  0.0375  52  VAL   B CG1 
617  C  CG2 . VAL   B 43  ? 0.5217 0.4687 0.3603 0.1230  0.0508  0.0492  52  VAL   B CG2 
618  N  N   . THR   B 44  ? 0.5318 0.4368 0.3686 0.0855  0.0457  0.0184  53  THR   B N   
619  C  CA  . THR   B 44  ? 0.5362 0.4263 0.3695 0.0813  0.0450  0.0077  53  THR   B CA  
620  C  C   . THR   B 44  ? 0.5522 0.4377 0.3807 0.0718  0.0399  0.0012  53  THR   B C   
621  O  O   . THR   B 44  ? 0.5647 0.4364 0.3897 0.0697  0.0375  -0.0073 53  THR   B O   
622  C  CB  . THR   B 44  ? 0.5406 0.4308 0.3662 0.0880  0.0486  -0.0009 53  THR   B CB  
623  O  OG1 . THR   B 44  ? 0.5429 0.4408 0.3613 0.0856  0.0479  -0.0030 53  THR   B OG1 
624  C  CG2 . THR   B 44  ? 0.5448 0.4387 0.3740 0.0986  0.0517  0.0029  53  THR   B CG2 
625  N  N   . LYS   B 45  ? 0.5487 0.4448 0.3748 0.0682  0.0374  0.0041  54  LYS   B N   
626  C  CA  . LYS   B 45  ? 0.5672 0.4611 0.3860 0.0613  0.0323  -0.0024 54  LYS   B CA  
627  C  C   . LYS   B 45  ? 0.5699 0.4575 0.3742 0.0639  0.0348  -0.0139 54  LYS   B C   
628  O  O   . LYS   B 45  ? 0.5737 0.4546 0.3697 0.0610  0.0308  -0.0219 54  LYS   B O   
629  C  CB  . LYS   B 45  ? 0.6087 0.4940 0.4358 0.0527  0.0247  -0.0031 54  LYS   B CB  
630  C  CG  . LYS   B 45  ? 0.6810 0.5727 0.5266 0.0487  0.0236  0.0104  54  LYS   B CG  
631  C  CD  . LYS   B 45  ? 0.7474 0.6611 0.5989 0.0483  0.0235  0.0208  54  LYS   B CD  
632  C  CE  . LYS   B 45  ? 0.8074 0.7311 0.6792 0.0441  0.0234  0.0358  54  LYS   B CE  
633  N  NZ  . LYS   B 45  ? 0.8367 0.7861 0.7127 0.0507  0.0272  0.0480  54  LYS   B NZ  
634  N  N   . GLY   B 46  ? 0.5585 0.4499 0.3605 0.0701  0.0409  -0.0142 55  GLY   B N   
635  C  CA  . GLY   B 46  ? 0.5595 0.4507 0.3516 0.0725  0.0450  -0.0221 55  GLY   B CA  
636  C  C   . GLY   B 46  ? 0.5632 0.4458 0.3543 0.0770  0.0465  -0.0304 55  GLY   B C   
637  O  O   . GLY   B 46  ? 0.5689 0.4549 0.3517 0.0806  0.0505  -0.0369 55  GLY   B O   
638  N  N   . ALA   B 47  ? 0.5627 0.4345 0.3616 0.0776  0.0435  -0.0296 56  ALA   B N   
639  C  CA  . ALA   B 47  ? 0.5804 0.4397 0.3760 0.0835  0.0432  -0.0381 56  ALA   B CA  
640  C  C   . ALA   B 47  ? 0.5848 0.4514 0.3824 0.0926  0.0503  -0.0395 56  ALA   B C   
641  O  O   . ALA   B 47  ? 0.5735 0.4510 0.3784 0.0935  0.0537  -0.0326 56  ALA   B O   
642  C  CB  . ALA   B 47  ? 0.5849 0.4275 0.3886 0.0803  0.0367  -0.0350 56  ALA   B CB  
643  N  N   . ALA   B 48  ? 0.5974 0.4582 0.3883 0.1006  0.0514  -0.0491 57  ALA   B N   
644  C  CA  . ALA   B 48  ? 0.6051 0.4750 0.3989 0.1102  0.0574  -0.0516 57  ALA   B CA  
645  C  C   . ALA   B 48  ? 0.6172 0.4794 0.4205 0.1141  0.0566  -0.0460 57  ALA   B C   
646  O  O   . ALA   B 48  ? 0.6330 0.4787 0.4384 0.1109  0.0515  -0.0421 57  ALA   B O   
647  C  CB  . ALA   B 48  ? 0.6093 0.4756 0.3917 0.1201  0.0581  -0.0637 57  ALA   B CB  
648  N  N   . LEU   B 49  ? 0.6064 0.4811 0.4159 0.1207  0.0612  -0.0447 58  LEU   B N   
649  C  CA  . LEU   B 49  ? 0.6092 0.4783 0.4253 0.1273  0.0608  -0.0397 58  LEU   B CA  
650  C  C   . LEU   B 49  ? 0.6253 0.4944 0.4396 0.1403  0.0629  -0.0477 58  LEU   B C   
651  O  O   . LEU   B 49  ? 0.6265 0.5076 0.4378 0.1441  0.0660  -0.0558 58  LEU   B O   
652  C  CB  . LEU   B 49  ? 0.5963 0.4790 0.4205 0.1267  0.0619  -0.0314 58  LEU   B CB  
653  C  CG  . LEU   B 49  ? 0.6025 0.4878 0.4273 0.1168  0.0597  -0.0236 58  LEU   B CG  
654  C  CD1 . LEU   B 49  ? 0.5909 0.4878 0.4201 0.1196  0.0591  -0.0182 58  LEU   B CD1 
655  C  CD2 . LEU   B 49  ? 0.6161 0.4888 0.4422 0.1127  0.0567  -0.0165 58  LEU   B CD2 
656  N  N   . ARG   B 50  ? 0.6420 0.4995 0.4579 0.1480  0.0616  -0.0447 59  ARG   B N   
657  C  CA  . ARG   B 50  ? 0.6685 0.5247 0.4817 0.1622  0.0627  -0.0520 59  ARG   B CA  
658  C  C   . ARG   B 50  ? 0.6767 0.5432 0.4979 0.1703  0.0642  -0.0470 59  ARG   B C   
659  O  O   . ARG   B 50  ? 0.6744 0.5378 0.4990 0.1677  0.0632  -0.0368 59  ARG   B O   
660  C  CB  . ARG   B 50  ? 0.7104 0.5377 0.5146 0.1663  0.0580  -0.0540 59  ARG   B CB  
661  C  CG  . ARG   B 50  ? 0.7842 0.6044 0.5834 0.1829  0.0578  -0.0601 59  ARG   B CG  
662  C  CD  . ARG   B 50  ? 0.8553 0.6426 0.6425 0.1869  0.0511  -0.0642 59  ARG   B CD  
663  N  NE  . ARG   B 50  ? 0.9063 0.6715 0.6968 0.1750  0.0463  -0.0521 59  ARG   B NE  
664  C  CZ  . ARG   B 50  ? 0.9479 0.7025 0.7427 0.1766  0.0465  -0.0398 59  ARG   B CZ  
665  N  NH1 . ARG   B 50  ? 0.9429 0.7051 0.7374 0.1909  0.0503  -0.0392 59  ARG   B NH1 
666  N  NH2 . ARG   B 50  ? 0.9602 0.6988 0.7605 0.1642  0.0428  -0.0271 59  ARG   B NH2 
667  N  N   . SER   B 51  ? 0.6853 0.5669 0.5096 0.1807  0.0661  -0.0543 60  SER   B N   
668  C  CA  . SER   B 51  ? 0.7075 0.5977 0.5382 0.1906  0.0654  -0.0520 60  SER   B CA  
669  C  C   . SER   B 51  ? 0.7398 0.6283 0.5667 0.2065  0.0657  -0.0606 60  SER   B C   
670  O  O   . SER   B 51  ? 0.7396 0.6491 0.5720 0.2115  0.0674  -0.0688 60  SER   B O   
671  C  CB  . SER   B 51  ? 0.7100 0.6249 0.5522 0.1859  0.0652  -0.0524 60  SER   B CB  
672  O  OG  . SER   B 51  ? 0.7340 0.6552 0.5815 0.1963  0.0620  -0.0514 60  SER   B OG  
673  N  N   . GLY   B 52  ? 0.7644 0.6280 0.5816 0.2139  0.0638  -0.0583 61  GLY   B N   
674  C  CA  . GLY   B 52  ? 0.7830 0.6390 0.5926 0.2305  0.0629  -0.0667 61  GLY   B CA  
675  C  C   . GLY   B 52  ? 0.8037 0.6568 0.6052 0.2306  0.0631  -0.0772 61  GLY   B C   
676  O  O   . GLY   B 52  ? 0.8221 0.6556 0.6163 0.2214  0.0607  -0.0759 61  GLY   B O   
677  N  N   . GLU   B 53  ? 0.7969 0.6722 0.6003 0.2415  0.0655  -0.0878 62  GLU   B N   
678  C  CA  . GLU   B 53  ? 0.8070 0.6853 0.6011 0.2451  0.0665  -0.0982 62  GLU   B CA  
679  C  C   . GLU   B 53  ? 0.7982 0.6997 0.5995 0.2305  0.0711  -0.0970 62  GLU   B C   
680  O  O   . GLU   B 53  ? 0.8108 0.7090 0.6011 0.2304  0.0714  -0.1030 62  GLU   B O   
681  C  CB  . GLU   B 53  ? 0.8448 0.7406 0.6369 0.2655  0.0680  -0.1093 62  GLU   B CB  
682  C  CG  . GLU   B 53  ? 0.9562 0.8207 0.7278 0.2826  0.0625  -0.1175 62  GLU   B CG  
683  C  CD  . GLU   B 53  ? 1.0737 0.9581 0.8419 0.3052  0.0639  -0.1293 62  GLU   B CD  
684  O  OE1 . GLU   B 53  ? 1.0860 0.9998 0.8699 0.3099  0.0670  -0.1284 62  GLU   B OE1 
685  O  OE2 . GLU   B 53  ? 1.1201 0.9909 0.8699 0.3193  0.0609  -0.1400 62  GLU   B OE2 
686  N  N   . GLY   B 54  ? 0.7768 0.6999 0.5944 0.2197  0.0736  -0.0896 63  GLY   B N   
687  C  CA  . GLY   B 54  ? 0.7614 0.7055 0.5865 0.2054  0.0776  -0.0864 63  GLY   B CA  
688  C  C   . GLY   B 54  ? 0.7618 0.6873 0.5801 0.1907  0.0757  -0.0806 63  GLY   B C   
689  O  O   . GLY   B 54  ? 0.7791 0.6790 0.5927 0.1877  0.0712  -0.0757 63  GLY   B O   
690  N  N   . ARG   B 55  ? 0.7363 0.6769 0.5547 0.1815  0.0794  -0.0800 64  ARG   B N   
691  C  CA  . ARG   B 55  ? 0.7246 0.6521 0.5363 0.1682  0.0775  -0.0755 64  ARG   B CA  
692  C  C   . ARG   B 55  ? 0.6850 0.6302 0.5083 0.1543  0.0796  -0.0667 64  ARG   B C   
693  O  O   . ARG   B 55  ? 0.6784 0.6495 0.5116 0.1533  0.0840  -0.0659 64  ARG   B O   
694  C  CB  . ARG   B 55  ? 0.7489 0.6748 0.5453 0.1720  0.0788  -0.0837 64  ARG   B CB  
695  C  CG  . ARG   B 55  ? 0.8049 0.7155 0.5925 0.1602  0.0751  -0.0811 64  ARG   B CG  
696  C  CD  . ARG   B 55  ? 0.8572 0.7676 0.6275 0.1668  0.0755  -0.0904 64  ARG   B CD  
697  N  NE  . ARG   B 55  ? 0.9039 0.8024 0.6661 0.1560  0.0713  -0.0886 64  ARG   B NE  
698  C  CZ  . ARG   B 55  ? 0.9516 0.8245 0.6991 0.1584  0.0627  -0.0962 64  ARG   B CZ  
699  N  NH1 . ARG   B 55  ? 0.9575 0.8108 0.6955 0.1712  0.0570  -0.1059 64  ARG   B NH1 
700  N  NH2 . ARG   B 55  ? 0.9497 0.8152 0.6917 0.1484  0.0583  -0.0946 64  ARG   B NH2 
701  N  N   . LEU   B 56  ? 0.6572 0.5885 0.4795 0.1438  0.0758  -0.0595 65  LEU   B N   
702  C  CA  . LEU   B 56  ? 0.6285 0.5706 0.4578 0.1320  0.0758  -0.0517 65  LEU   B CA  
703  C  C   . LEU   B 56  ? 0.6074 0.5436 0.4260 0.1230  0.0758  -0.0505 65  LEU   B C   
704  O  O   . LEU   B 56  ? 0.6117 0.5288 0.4230 0.1211  0.0716  -0.0503 65  LEU   B O   
705  C  CB  . LEU   B 56  ? 0.6323 0.5649 0.4670 0.1302  0.0707  -0.0447 65  LEU   B CB  
706  C  CG  . LEU   B 56  ? 0.6519 0.5868 0.4946 0.1405  0.0688  -0.0452 65  LEU   B CG  
707  C  CD1 . LEU   B 56  ? 0.6591 0.5885 0.5043 0.1394  0.0639  -0.0377 65  LEU   B CD1 
708  C  CD2 . LEU   B 56  ? 0.6498 0.6074 0.5038 0.1433  0.0707  -0.0491 65  LEU   B CD2 
709  N  N   . ASP   B 57  ? 0.5856 0.5387 0.4037 0.1176  0.0802  -0.0490 66  ASP   B N   
710  C  CA  . ASP   B 57  ? 0.5813 0.5299 0.3870 0.1110  0.0802  -0.0481 66  ASP   B CA  
711  C  C   . ASP   B 57  ? 0.5557 0.5047 0.3647 0.0994  0.0777  -0.0387 66  ASP   B C   
712  O  O   . ASP   B 57  ? 0.5479 0.5082 0.3680 0.0958  0.0781  -0.0334 66  ASP   B O   
713  C  CB  . ASP   B 57  ? 0.6213 0.5880 0.4202 0.1148  0.0874  -0.0516 66  ASP   B CB  
714  C  CG  . ASP   B 57  ? 0.7241 0.6908 0.5165 0.1295  0.0892  -0.0623 66  ASP   B CG  
715  O  OD1 . ASP   B 57  ? 0.7486 0.6913 0.5326 0.1345  0.0829  -0.0687 66  ASP   B OD1 
716  O  OD2 . ASP   B 57  ? 0.7581 0.7490 0.5540 0.1361  0.0963  -0.0638 66  ASP   B OD2 
717  N  N   . PRO   B 58  ? 0.5443 0.4803 0.3438 0.0941  0.0736  -0.0369 67  PRO   B N   
718  C  CA  . PRO   B 58  ? 0.5352 0.4709 0.3351 0.0854  0.0705  -0.0286 67  PRO   B CA  
719  C  C   . PRO   B 58  ? 0.5192 0.4695 0.3179 0.0797  0.0751  -0.0240 67  PRO   B C   
720  O  O   . PRO   B 58  ? 0.5274 0.4880 0.3199 0.0820  0.0813  -0.0268 67  PRO   B O   
721  C  CB  . PRO   B 58  ? 0.5518 0.4743 0.3409 0.0826  0.0659  -0.0294 67  PRO   B CB  
722  C  CG  . PRO   B 58  ? 0.5612 0.4798 0.3415 0.0878  0.0673  -0.0385 67  PRO   B CG  
723  C  CD  . PRO   B 58  ? 0.5421 0.4632 0.3300 0.0961  0.0702  -0.0430 67  PRO   B CD  
724  N  N   . TYR   B 59  ? 0.4970 0.4482 0.3012 0.0732  0.0719  -0.0163 68  TYR   B N   
725  C  CA  . TYR   B 59  ? 0.4763 0.4391 0.2819 0.0655  0.0752  -0.0092 68  TYR   B CA  
726  C  C   . TYR   B 59  ? 0.4793 0.4310 0.2737 0.0588  0.0703  -0.0027 68  TYR   B C   
727  O  O   . TYR   B 59  ? 0.4942 0.4507 0.2791 0.0545  0.0744  0.0018  68  TYR   B O   
728  C  CB  . TYR   B 59  ? 0.4594 0.4316 0.2835 0.0632  0.0735  -0.0059 68  TYR   B CB  
729  C  CG  . TYR   B 59  ? 0.4509 0.4360 0.2817 0.0527  0.0761  0.0037  68  TYR   B CG  
730  C  CD1 . TYR   B 59  ? 0.4633 0.4364 0.2894 0.0439  0.0696  0.0120  68  TYR   B CD1 
731  C  CD2 . TYR   B 59  ? 0.4422 0.4519 0.2857 0.0517  0.0841  0.0056  68  TYR   B CD2 
732  C  CE1 . TYR   B 59  ? 0.4687 0.4511 0.3017 0.0326  0.0712  0.0229  68  TYR   B CE1 
733  C  CE2 . TYR   B 59  ? 0.4481 0.4721 0.3015 0.0401  0.0867  0.0172  68  TYR   B CE2 
734  C  CZ  . TYR   B 59  ? 0.4641 0.4727 0.3125 0.0296  0.0798  0.0263  68  TYR   B CZ  
735  O  OH  . TYR   B 59  ? 0.4708 0.4907 0.3297 0.0165  0.0815  0.0397  68  TYR   B OH  
736  N  N   . TRP   B 60  ? 0.4777 0.4157 0.2716 0.0596  0.0619  -0.0017 69  TRP   B N   
737  C  CA  . TRP   B 60  ? 0.4870 0.4139 0.2693 0.0559  0.0559  0.0035  69  TRP   B CA  
738  C  C   . TRP   B 60  ? 0.4969 0.4143 0.2752 0.0619  0.0503  0.0004  69  TRP   B C   
739  O  O   . TRP   B 60  ? 0.4932 0.4099 0.2804 0.0676  0.0485  -0.0020 69  TRP   B O   
740  C  CB  . TRP   B 60  ? 0.4861 0.4079 0.2733 0.0509  0.0493  0.0106  69  TRP   B CB  
741  C  CG  . TRP   B 60  ? 0.5016 0.4084 0.2751 0.0507  0.0408  0.0146  69  TRP   B CG  
742  C  CD1 . TRP   B 60  ? 0.5203 0.4224 0.2792 0.0461  0.0410  0.0197  69  TRP   B CD1 
743  C  CD2 . TRP   B 60  ? 0.5054 0.4016 0.2760 0.0584  0.0315  0.0131  69  TRP   B CD2 
744  N  NE1 . TRP   B 60  ? 0.5340 0.4223 0.2818 0.0500  0.0315  0.0211  69  TRP   B NE1 
745  C  CE2 . TRP   B 60  ? 0.5252 0.4112 0.2800 0.0582  0.0260  0.0170  69  TRP   B CE2 
746  C  CE3 . TRP   B 60  ? 0.5064 0.4027 0.2850 0.0674  0.0280  0.0093  69  TRP   B CE3 
747  C  CZ2 . TRP   B 60  ? 0.5351 0.4125 0.2825 0.0670  0.0168  0.0168  69  TRP   B CZ2 
748  C  CZ3 . TRP   B 60  ? 0.5229 0.4112 0.2940 0.0760  0.0196  0.0101  69  TRP   B CZ3 
749  C  CH2 . TRP   B 60  ? 0.5351 0.4150 0.2911 0.0760  0.0141  0.0136  69  TRP   B CH2 
750  N  N   . GLY   B 61  ? 0.5109 0.4229 0.2766 0.0608  0.0474  0.0017  70  GLY   B N   
751  C  CA  . GLY   B 61  ? 0.5207 0.4286 0.2851 0.0654  0.0422  0.0008  70  GLY   B CA  
752  C  C   . GLY   B 61  ? 0.5259 0.4294 0.2767 0.0643  0.0371  0.0040  70  GLY   B C   
753  O  O   . GLY   B 61  ? 0.5364 0.4388 0.2762 0.0602  0.0387  0.0052  70  GLY   B O   
754  N  N   . ASP   B 62  ? 0.5226 0.4255 0.2736 0.0693  0.0312  0.0059  71  ASP   B N   
755  C  CA  . ASP   B 62  ? 0.5264 0.4275 0.2651 0.0707  0.0252  0.0086  71  ASP   B CA  
756  C  C   . ASP   B 62  ? 0.5124 0.4215 0.2579 0.0761  0.0219  0.0098  71  ASP   B C   
757  O  O   . ASP   B 62  ? 0.5040 0.4157 0.2565 0.0827  0.0207  0.0124  71  ASP   B O   
758  C  CB  . ASP   B 62  ? 0.5609 0.4522 0.2903 0.0731  0.0194  0.0134  71  ASP   B CB  
759  C  CG  . ASP   B 62  ? 0.6493 0.5354 0.3617 0.0749  0.0133  0.0161  71  ASP   B CG  
760  O  OD1 . ASP   B 62  ? 0.6607 0.5526 0.3711 0.0816  0.0087  0.0163  71  ASP   B OD1 
761  O  OD2 . ASP   B 62  ? 0.7044 0.5819 0.4055 0.0699  0.0134  0.0188  71  ASP   B OD2 
762  N  N   . VAL   B 63  ? 0.5128 0.4276 0.2569 0.0736  0.0201  0.0084  72  VAL   B N   
763  C  CA  . VAL   B 63  ? 0.5030 0.4299 0.2575 0.0762  0.0172  0.0114  72  VAL   B CA  
764  C  C   . VAL   B 63  ? 0.5014 0.4347 0.2502 0.0859  0.0118  0.0172  72  VAL   B C   
765  O  O   . VAL   B 63  ? 0.4971 0.4428 0.2562 0.0920  0.0117  0.0224  72  VAL   B O   
766  C  CB  . VAL   B 63  ? 0.5053 0.4362 0.2620 0.0694  0.0147  0.0075  72  VAL   B CB  
767  C  CG1 . VAL   B 63  ? 0.5034 0.4505 0.2706 0.0708  0.0098  0.0128  72  VAL   B CG1 
768  C  CG2 . VAL   B 63  ? 0.5089 0.4341 0.2745 0.0633  0.0184  0.0019  72  VAL   B CG2 
769  N  N   . LYS   B 64  ? 0.5065 0.4311 0.2378 0.0888  0.0074  0.0171  73  LYS   B N   
770  C  CA  . LYS   B 64  ? 0.5093 0.4372 0.2311 0.1006  0.0004  0.0212  73  LYS   B CA  
771  C  C   . LYS   B 64  ? 0.5166 0.4396 0.2386 0.1102  -0.0010 0.0232  73  LYS   B C   
772  O  O   . LYS   B 64  ? 0.5127 0.4481 0.2373 0.1219  -0.0033 0.0270  73  LYS   B O   
773  C  CB  . LYS   B 64  ? 0.5356 0.4528 0.2366 0.1017  -0.0055 0.0204  73  LYS   B CB  
774  C  CG  . LYS   B 64  ? 0.5845 0.5065 0.2747 0.1160  -0.0138 0.0236  73  LYS   B CG  
775  C  CD  . LYS   B 64  ? 0.6407 0.5534 0.3100 0.1177  -0.0201 0.0230  73  LYS   B CD  
776  C  CE  . LYS   B 64  ? 0.6945 0.6053 0.3489 0.1344  -0.0295 0.0252  73  LYS   B CE  
777  N  NZ  . LYS   B 64  ? 0.7483 0.6436 0.3788 0.1371  -0.0367 0.0249  73  LYS   B NZ  
778  N  N   . GLN   B 65  ? 0.5246 0.4320 0.2451 0.1060  0.0002  0.0209  74  GLN   B N   
779  C  CA  . GLN   B 65  ? 0.5305 0.4325 0.2529 0.1149  -0.0027 0.0211  74  GLN   B CA  
780  C  C   . GLN   B 65  ? 0.5183 0.4344 0.2579 0.1179  0.0037  0.0223  74  GLN   B C   
781  O  O   . GLN   B 65  ? 0.5130 0.4298 0.2531 0.1297  0.0012  0.0232  74  GLN   B O   
782  C  CB  . GLN   B 65  ? 0.5621 0.4469 0.2833 0.1075  -0.0035 0.0188  74  GLN   B CB  
783  C  CG  . GLN   B 65  ? 0.6416 0.5094 0.3466 0.1039  -0.0102 0.0202  74  GLN   B CG  
784  C  CD  . GLN   B 65  ? 0.7238 0.5786 0.4333 0.0948  -0.0105 0.0202  74  GLN   B CD  
785  O  OE1 . GLN   B 65  ? 0.7365 0.5897 0.4557 0.0980  -0.0126 0.0182  74  GLN   B OE1 
786  N  NE2 . GLN   B 65  ? 0.7428 0.5901 0.4461 0.0837  -0.0086 0.0234  74  GLN   B NE2 
787  N  N   . ASP   B 66  ? 0.5051 0.4301 0.2570 0.1080  0.0112  0.0220  75  ASP   B N   
788  C  CA  . ASP   B 66  ? 0.4899 0.4245 0.2580 0.1078  0.0174  0.0240  75  ASP   B CA  
789  C  C   . ASP   B 66  ? 0.4803 0.4060 0.2526 0.1088  0.0200  0.0206  75  ASP   B C   
790  O  O   . ASP   B 66  ? 0.4708 0.4022 0.2511 0.1158  0.0225  0.0231  75  ASP   B O   
791  C  CB  . ASP   B 66  ? 0.5006 0.4531 0.2739 0.1191  0.0170  0.0319  75  ASP   B CB  
792  C  CG  . ASP   B 66  ? 0.5324 0.4950 0.3236 0.1153  0.0238  0.0366  75  ASP   B CG  
793  O  OD1 . ASP   B 66  ? 0.5420 0.4994 0.3409 0.1025  0.0267  0.0333  75  ASP   B OD1 
794  O  OD2 . ASP   B 66  ? 0.5531 0.5280 0.3493 0.1261  0.0258  0.0439  75  ASP   B OD2 
795  N  N   . LEU   B 67  ? 0.4811 0.3949 0.2493 0.1016  0.0199  0.0156  76  LEU   B N   
796  C  CA  . LEU   B 67  ? 0.4760 0.3847 0.2507 0.1017  0.0219  0.0123  76  LEU   B CA  
797  C  C   . LEU   B 67  ? 0.4764 0.3844 0.2568 0.0907  0.0289  0.0079  76  LEU   B C   
798  O  O   . LEU   B 67  ? 0.4720 0.3796 0.2470 0.0830  0.0307  0.0069  76  LEU   B O   
799  C  CB  . LEU   B 67  ? 0.4781 0.3759 0.2451 0.1051  0.0137  0.0115  76  LEU   B CB  
800  C  CG  . LEU   B 67  ? 0.4952 0.3919 0.2545 0.1206  0.0052  0.0135  76  LEU   B CG  
801  C  CD1 . LEU   B 67  ? 0.5129 0.3933 0.2621 0.1228  -0.0059 0.0117  76  LEU   B CD1 
802  C  CD2 . LEU   B 67  ? 0.4941 0.3989 0.2617 0.1320  0.0077  0.0138  76  LEU   B CD2 
803  N  N   . VAL   B 68  ? 0.4687 0.3775 0.2585 0.0921  0.0324  0.0049  77  VAL   B N   
804  C  CA  . VAL   B 68  ? 0.4651 0.3755 0.2596 0.0851  0.0391  0.0002  77  VAL   B CA  
805  C  C   . VAL   B 68  ? 0.4607 0.3732 0.2645 0.0882  0.0399  -0.0025 77  VAL   B C   
806  O  O   . VAL   B 68  ? 0.4556 0.3676 0.2635 0.0971  0.0368  -0.0021 77  VAL   B O   
807  C  CB  . VAL   B 68  ? 0.4653 0.3768 0.2628 0.0838  0.0436  -0.0020 77  VAL   B CB  
808  C  CG1 . VAL   B 68  ? 0.4605 0.3728 0.2665 0.0915  0.0440  0.0002  77  VAL   B CG1 
809  C  CG2 . VAL   B 68  ? 0.4695 0.3816 0.2669 0.0796  0.0492  -0.0084 77  VAL   B CG2 
810  N  N   . SER   B 69  ? 0.4626 0.3794 0.2696 0.0818  0.0438  -0.0047 78  SER   B N   
811  C  CA  . SER   B 69  ? 0.4521 0.3753 0.2709 0.0837  0.0446  -0.0074 78  SER   B CA  
812  C  C   . SER   B 69  ? 0.4471 0.3795 0.2701 0.0830  0.0536  -0.0122 78  SER   B C   
813  O  O   . SER   B 69  ? 0.4488 0.3817 0.2639 0.0794  0.0582  -0.0134 78  SER   B O   
814  C  CB  . SER   B 69  ? 0.4513 0.3745 0.2736 0.0773  0.0393  -0.0040 78  SER   B CB  
815  O  OG  . SER   B 69  ? 0.4614 0.3908 0.2820 0.0669  0.0446  -0.0008 78  SER   B OG  
816  N  N   . TYR   B 70  ? 0.4378 0.3767 0.2714 0.0889  0.0549  -0.0160 79  TYR   B N   
817  C  CA  . TYR   B 70  ? 0.4424 0.3899 0.2792 0.0924  0.0622  -0.0218 79  TYR   B CA  
818  C  C   . TYR   B 70  ? 0.4449 0.4089 0.2953 0.0916  0.0637  -0.0226 79  TYR   B C   
819  O  O   . TYR   B 70  ? 0.4425 0.4072 0.3024 0.0935  0.0572  -0.0219 79  TYR   B O   
820  C  CB  . TYR   B 70  ? 0.4444 0.3834 0.2811 0.1028  0.0618  -0.0254 79  TYR   B CB  
821  C  CG  . TYR   B 70  ? 0.4608 0.3867 0.2877 0.1016  0.0613  -0.0241 79  TYR   B CG  
822  C  CD1 . TYR   B 70  ? 0.4648 0.3839 0.2891 0.1009  0.0565  -0.0179 79  TYR   B CD1 
823  C  CD2 . TYR   B 70  ? 0.4758 0.3970 0.2965 0.1018  0.0645  -0.0291 79  TYR   B CD2 
824  C  CE1 . TYR   B 70  ? 0.4786 0.3899 0.2978 0.0982  0.0556  -0.0155 79  TYR   B CE1 
825  C  CE2 . TYR   B 70  ? 0.4886 0.3977 0.3029 0.0986  0.0618  -0.0280 79  TYR   B CE2 
826  C  CZ  . TYR   B 70  ? 0.4967 0.4024 0.3119 0.0957  0.0578  -0.0205 79  TYR   B CZ  
827  O  OH  . TYR   B 70  ? 0.5148 0.4122 0.3274 0.0915  0.0549  -0.0186 79  TYR   B OH  
828  N  N   . CYS   B 71  ? 0.4467 0.4257 0.2983 0.0897  0.0715  -0.0242 80  CYS   B N   
829  C  CA  . CYS   B 71  ? 0.4547 0.4566 0.3219 0.0886  0.0750  -0.0238 80  CYS   B CA  
830  C  C   . CYS   B 71  ? 0.4494 0.4599 0.3263 0.0751  0.0724  -0.0146 80  CYS   B C   
831  O  O   . CYS   B 71  ? 0.4452 0.4790 0.3367 0.0709  0.0768  -0.0115 80  CYS   B O   
832  C  CB  . CYS   B 71  ? 0.4799 0.4850 0.3586 0.0987  0.0714  -0.0295 80  CYS   B CB  
833  S  SG  . CYS   B 71  ? 0.5796 0.5712 0.4468 0.1142  0.0737  -0.0383 80  CYS   B SG  
834  N  N   . GLY   B 72  ? 0.4376 0.4305 0.3071 0.0687  0.0652  -0.0096 81  GLY   B N   
835  C  CA  . GLY   B 72  ? 0.4305 0.4257 0.3073 0.0557  0.0608  -0.0003 81  GLY   B CA  
836  C  C   . GLY   B 72  ? 0.4398 0.4114 0.3029 0.0522  0.0521  0.0035  81  GLY   B C   
837  O  O   . GLY   B 72  ? 0.4466 0.4037 0.2963 0.0598  0.0501  -0.0005 81  GLY   B O   
838  N  N   . PRO   B 73  ? 0.4410 0.4093 0.3077 0.0405  0.0467  0.0122  82  PRO   B N   
839  C  CA  . PRO   B 73  ? 0.4589 0.4035 0.3103 0.0387  0.0373  0.0156  82  PRO   B CA  
840  C  C   . PRO   B 73  ? 0.4738 0.4015 0.3235 0.0485  0.0242  0.0099  82  PRO   B C   
841  O  O   . PRO   B 73  ? 0.4743 0.4068 0.3380 0.0527  0.0193  0.0055  82  PRO   B O   
842  C  CB  . PRO   B 73  ? 0.4641 0.4087 0.3220 0.0236  0.0340  0.0269  82  PRO   B CB  
843  C  CG  . PRO   B 73  ? 0.4498 0.4163 0.3334 0.0180  0.0360  0.0282  82  PRO   B CG  
844  C  CD  . PRO   B 73  ? 0.4185 0.4048 0.3037 0.0280  0.0487  0.0205  82  PRO   B CD  
845  N  N   . TRP   B 74  ? 0.4873 0.3968 0.3192 0.0536  0.0181  0.0101  83  TRP   B N   
846  C  CA  . TRP   B 74  ? 0.5073 0.4021 0.3331 0.0659  0.0060  0.0058  83  TRP   B CA  
847  C  C   . TRP   B 74  ? 0.5257 0.4124 0.3625 0.0641  -0.0084 0.0051  83  TRP   B C   
848  O  O   . TRP   B 74  ? 0.5255 0.4050 0.3656 0.0517  -0.0143 0.0113  83  TRP   B O   
849  C  CB  . TRP   B 74  ? 0.5114 0.3912 0.3165 0.0698  0.0015  0.0084  83  TRP   B CB  
850  C  CG  . TRP   B 74  ? 0.5144 0.3843 0.3106 0.0859  -0.0083 0.0045  83  TRP   B CG  
851  C  CD1 . TRP   B 74  ? 0.5276 0.3807 0.3174 0.0925  -0.0241 0.0033  83  TRP   B CD1 
852  C  CD2 . TRP   B 74  ? 0.5115 0.3887 0.3038 0.0987  -0.0033 0.0020  83  TRP   B CD2 
853  N  NE1 . TRP   B 74  ? 0.5348 0.3868 0.3157 0.1108  -0.0282 -0.0005 83  TRP   B NE1 
854  C  CE2 . TRP   B 74  ? 0.5227 0.3908 0.3065 0.1140  -0.0148 -0.0001 83  TRP   B CE2 
855  C  CE3 . TRP   B 74  ? 0.5042 0.3940 0.2996 0.0988  0.0091  0.0017  83  TRP   B CE3 
856  C  CZ2 . TRP   B 74  ? 0.5243 0.3996 0.3033 0.1291  -0.0122 -0.0003 83  TRP   B CZ2 
857  C  CZ3 . TRP   B 74  ? 0.5085 0.4022 0.3011 0.1113  0.0104  0.0017  83  TRP   B CZ3 
858  C  CH2 . TRP   B 74  ? 0.5149 0.4037 0.3002 0.1262  0.0010  0.0016  83  TRP   B CH2 
859  N  N   . LYS   B 75  ? 0.5337 0.4219 0.3774 0.0758  -0.0142 -0.0021 84  LYS   B N   
860  C  CA  . LYS   B 75  ? 0.5443 0.4253 0.3998 0.0749  -0.0297 -0.0048 84  LYS   B CA  
861  C  C   . LYS   B 75  ? 0.5742 0.4325 0.4147 0.0893  -0.0473 -0.0095 84  LYS   B C   
862  O  O   . LYS   B 75  ? 0.5817 0.4265 0.4276 0.0873  -0.0642 -0.0116 84  LYS   B O   
863  C  CB  . LYS   B 75  ? 0.5390 0.4384 0.4132 0.0795  -0.0266 -0.0110 84  LYS   B CB  
864  C  CG  . LYS   B 75  ? 0.5354 0.4595 0.4244 0.0690  -0.0103 -0.0079 84  LYS   B CG  
865  C  CD  . LYS   B 75  ? 0.5771 0.5097 0.4846 0.0502  -0.0129 -0.0006 84  LYS   B CD  
866  C  CE  . LYS   B 75  ? 0.6272 0.5889 0.5481 0.0428  0.0041  0.0028  84  LYS   B CE  
867  N  NZ  . LYS   B 75  ? 0.6554 0.6306 0.5958 0.0238  0.0039  0.0132  84  LYS   B NZ  
868  N  N   . LEU   B 76  ? 0.5886 0.4438 0.4111 0.1048  -0.0444 -0.0113 85  LEU   B N   
869  C  CA  . LEU   B 76  ? 0.6052 0.4439 0.4111 0.1235  -0.0592 -0.0159 85  LEU   B CA  
870  C  C   . LEU   B 76  ? 0.6496 0.4658 0.4394 0.1208  -0.0712 -0.0127 85  LEU   B C   
871  O  O   . LEU   B 76  ? 0.6570 0.4740 0.4367 0.1160  -0.0631 -0.0069 85  LEU   B O   
872  C  CB  . LEU   B 76  ? 0.5943 0.4436 0.3890 0.1410  -0.0495 -0.0164 85  LEU   B CB  
873  C  CG  . LEU   B 76  ? 0.5826 0.4519 0.3904 0.1420  -0.0347 -0.0174 85  LEU   B CG  
874  C  CD1 . LEU   B 76  ? 0.5822 0.4591 0.3798 0.1572  -0.0268 -0.0151 85  LEU   B CD1 
875  C  CD2 . LEU   B 76  ? 0.5757 0.4477 0.3967 0.1466  -0.0417 -0.0242 85  LEU   B CD2 
876  N  N   . ASP   B 77  ? 0.6767 0.4714 0.4631 0.1250  -0.0921 -0.0172 86  ASP   B N   
877  C  CA  . ASP   B 77  ? 0.7163 0.4845 0.4854 0.1240  -0.1065 -0.0148 86  ASP   B CA  
878  C  C   . ASP   B 77  ? 0.7377 0.4831 0.4863 0.1477  -0.1282 -0.0236 86  ASP   B C   
879  O  O   . ASP   B 77  ? 0.7607 0.4792 0.4941 0.1482  -0.1441 -0.0233 86  ASP   B O   
880  C  CB  . ASP   B 77  ? 0.7596 0.5164 0.5434 0.0993  -0.1128 -0.0084 86  ASP   B CB  
881  C  CG  . ASP   B 77  ? 0.8538 0.6064 0.6585 0.0934  -0.1270 -0.0132 86  ASP   B CG  
882  O  OD1 . ASP   B 77  ? 0.8619 0.6274 0.6738 0.1061  -0.1268 -0.0215 86  ASP   B OD1 
883  O  OD2 . ASP   B 77  ? 0.8973 0.6344 0.7123 0.0755  -0.1387 -0.0078 86  ASP   B OD2 
884  N  N   . ALA   B 78  ? 0.7312 0.4859 0.4769 0.1688  -0.1297 -0.0314 87  ALA   B N   
885  C  CA  . ALA   B 78  ? 0.7468 0.4822 0.4699 0.1954  -0.1501 -0.0403 87  ALA   B CA  
886  C  C   . ALA   B 78  ? 0.7637 0.4986 0.4604 0.2119  -0.1470 -0.0372 87  ALA   B C   
887  O  O   . ALA   B 78  ? 0.7590 0.5160 0.4577 0.2073  -0.1267 -0.0295 87  ALA   B O   
888  C  CB  . ALA   B 78  ? 0.7356 0.4833 0.4614 0.2150  -0.1516 -0.0484 87  ALA   B CB  
889  N  N   . ALA   B 79  ? 0.7788 0.4882 0.4509 0.2310  -0.1682 -0.0435 88  ALA   B N   
890  C  CA  . ALA   B 79  ? 0.7944 0.5041 0.4408 0.2484  -0.1673 -0.0410 88  ALA   B CA  
891  C  C   . ALA   B 79  ? 0.8139 0.5198 0.4351 0.2850  -0.1809 -0.0497 88  ALA   B C   
892  O  O   . ALA   B 79  ? 0.8171 0.5021 0.4328 0.2965  -0.2015 -0.0602 88  ALA   B O   
893  C  CB  . ALA   B 79  ? 0.8073 0.4876 0.4426 0.2365  -0.1794 -0.0383 88  ALA   B CB  
894  N  N   . TRP   B 80  ? 0.8248 0.5519 0.4303 0.3043  -0.1703 -0.0452 89  TRP   B N   
895  C  CA  . TRP   B 80  ? 0.8547 0.5833 0.4334 0.3423  -0.1812 -0.0515 89  TRP   B CA  
896  C  C   . TRP   B 80  ? 0.8991 0.5870 0.4509 0.3548  -0.2095 -0.0607 89  TRP   B C   
897  O  O   . TRP   B 80  ? 0.9080 0.5784 0.4577 0.3379  -0.2127 -0.0569 89  TRP   B O   
898  C  CB  . TRP   B 80  ? 0.8451 0.6099 0.4169 0.3562  -0.1619 -0.0415 89  TRP   B CB  
899  C  CG  . TRP   B 80  ? 0.8573 0.6309 0.4013 0.3972  -0.1702 -0.0456 89  TRP   B CG  
900  C  CD1 . TRP   B 80  ? 0.8702 0.6458 0.4054 0.4221  -0.1777 -0.0527 89  TRP   B CD1 
901  C  CD2 . TRP   B 80  ? 0.8593 0.6461 0.3806 0.4199  -0.1700 -0.0419 89  TRP   B CD2 
902  N  NE1 . TRP   B 80  ? 0.8798 0.6676 0.3861 0.4601  -0.1827 -0.0537 89  TRP   B NE1 
903  C  CE2 . TRP   B 80  ? 0.8726 0.6694 0.3711 0.4592  -0.1775 -0.0468 89  TRP   B CE2 
904  C  CE3 . TRP   B 80  ? 0.8629 0.6554 0.3802 0.4122  -0.1645 -0.0351 89  TRP   B CE3 
905  C  CZ2 . TRP   B 80  ? 0.8793 0.6934 0.3519 0.4912  -0.1791 -0.0445 89  TRP   B CZ2 
906  C  CZ3 . TRP   B 80  ? 0.8748 0.6837 0.3675 0.4429  -0.1670 -0.0336 89  TRP   B CZ3 
907  C  CH2 . TRP   B 80  ? 0.8764 0.6973 0.3477 0.4819  -0.1736 -0.0378 89  TRP   B CH2 
908  N  N   . ASP   B 81  ? 0.9253 0.5950 0.4568 0.3834  -0.2315 -0.0732 90  ASP   B N   
909  C  CA  . ASP   B 81  ? 0.9676 0.5928 0.4720 0.3968  -0.2622 -0.0839 90  ASP   B CA  
910  C  C   . ASP   B 81  ? 1.0005 0.6281 0.4706 0.4266  -0.2660 -0.0837 90  ASP   B C   
911  O  O   . ASP   B 81  ? 1.0246 0.6132 0.4685 0.4396  -0.2917 -0.0925 90  ASP   B O   
912  C  CB  . ASP   B 81  ? 0.9937 0.5925 0.4895 0.4147  -0.2888 -0.0997 90  ASP   B CB  
913  C  CG  . ASP   B 81  ? 1.0720 0.6927 0.5474 0.4558  -0.2885 -0.1059 90  ASP   B CG  
914  O  OD1 . ASP   B 81  ? 1.0757 0.7376 0.5497 0.4672  -0.2642 -0.0956 90  ASP   B OD1 
915  O  OD2 . ASP   B 81  ? 1.1278 0.7250 0.5891 0.4769  -0.3132 -0.1207 90  ASP   B OD2 
916  N  N   . GLY   B 82  ? 0.9969 0.6694 0.4680 0.4372  -0.2415 -0.0737 91  GLY   B N   
917  C  CA  . GLY   B 82  ? 1.0183 0.7035 0.4612 0.4659  -0.2419 -0.0718 91  GLY   B CA  
918  C  C   . GLY   B 82  ? 1.0447 0.7325 0.4553 0.5133  -0.2563 -0.0817 91  GLY   B C   
919  O  O   . GLY   B 82  ? 1.0487 0.7485 0.4331 0.5421  -0.2584 -0.0811 91  GLY   B O   
920  N  N   . LEU   B 83  ? 1.0582 0.7369 0.4693 0.5242  -0.2666 -0.0912 92  LEU   B N   
921  C  CA  . LEU   B 83  ? 1.0841 0.7631 0.4616 0.5719  -0.2822 -0.1020 92  LEU   B CA  
922  C  C   . LEU   B 83  ? 1.0789 0.7924 0.4662 0.5853  -0.2675 -0.0990 92  LEU   B C   
923  O  O   . LEU   B 83  ? 1.0903 0.8292 0.4539 0.6250  -0.2652 -0.0989 92  LEU   B O   
924  C  CB  . LEU   B 83  ? 1.1214 0.7416 0.4775 0.5826  -0.3210 -0.1221 92  LEU   B CB  
925  C  CG  . LEU   B 83  ? 1.1797 0.7524 0.5173 0.5769  -0.3446 -0.1283 92  LEU   B CG  
926  C  CD1 . LEU   B 83  ? 1.2201 0.7365 0.5357 0.5927  -0.3848 -0.1486 92  LEU   B CD1 
927  C  CD2 . LEU   B 83  ? 1.1946 0.7826 0.5005 0.6080  -0.3425 -0.1255 92  LEU   B CD2 
928  N  N   . SER   B 84  ? 1.0605 0.7720 0.4793 0.5557  -0.2605 -0.0980 93  SER   B N   
929  C  CA  . SER   B 84  ? 1.0447 0.7794 0.4714 0.5677  -0.2514 -0.0977 93  SER   B CA  
930  C  C   . SER   B 84  ? 1.0135 0.8005 0.4619 0.5595  -0.2158 -0.0784 93  SER   B C   
931  O  O   . SER   B 84  ? 1.0091 0.8133 0.4780 0.5318  -0.1962 -0.0652 93  SER   B O   
932  C  CB  . SER   B 84  ? 1.0644 0.7713 0.5138 0.5424  -0.2634 -0.1071 93  SER   B CB  
933  O  OG  . SER   B 84  ? 1.1103 0.7661 0.5480 0.5393  -0.2962 -0.1223 93  SER   B OG  
934  N  N   . GLU   B 85  ? 0.9891 0.7998 0.4331 0.5833  -0.2085 -0.0768 94  GLU   B N   
935  C  CA  . GLU   B 85  ? 0.9545 0.8105 0.4204 0.5749  -0.1768 -0.0583 94  GLU   B CA  
936  C  C   . GLU   B 85  ? 0.9215 0.7700 0.4241 0.5336  -0.1673 -0.0566 94  GLU   B C   
937  O  O   . GLU   B 85  ? 0.9338 0.7488 0.4426 0.5203  -0.1855 -0.0702 94  GLU   B O   
938  C  CB  . GLU   B 85  ? 0.9789 0.8607 0.4256 0.6155  -0.1727 -0.0560 94  GLU   B CB  
939  C  CG  . GLU   B 85  ? 1.0393 0.9410 0.4519 0.6577  -0.1756 -0.0534 94  GLU   B CG  
940  C  CD  . GLU   B 85  ? 1.0856 1.0305 0.4857 0.6929  -0.1596 -0.0411 94  GLU   B CD  
941  O  OE1 . GLU   B 85  ? 1.0681 1.0171 0.4764 0.6941  -0.1542 -0.0404 94  GLU   B OE1 
942  O  OE2 . GLU   B 85  ? 1.1077 1.0842 0.4900 0.7199  -0.1520 -0.0313 94  GLU   B OE2 
943  N  N   . VAL   B 86  ? 0.8784 0.7583 0.4059 0.5126  -0.1398 -0.0396 95  VAL   B N   
944  C  CA  . VAL   B 86  ? 0.8450 0.7219 0.4059 0.4752  -0.1283 -0.0367 95  VAL   B CA  
945  C  C   . VAL   B 86  ? 0.8160 0.7258 0.3892 0.4791  -0.1057 -0.0235 95  VAL   B C   
946  O  O   . VAL   B 86  ? 0.8185 0.7560 0.3777 0.5059  -0.0965 -0.0134 95  VAL   B O   
947  C  CB  . VAL   B 86  ? 0.8309 0.7071 0.4106 0.4399  -0.1182 -0.0293 95  VAL   B CB  
948  C  CG1 . VAL   B 86  ? 0.8459 0.6910 0.4092 0.4394  -0.1394 -0.0393 95  VAL   B CG1 
949  C  CG2 . VAL   B 86  ? 0.8161 0.7306 0.4021 0.4396  -0.0949 -0.0110 95  VAL   B CG2 
950  N  N   . GLN   B 87  ? 0.7885 0.6964 0.3877 0.4530  -0.0962 -0.0222 96  GLN   B N   
951  C  CA  . GLN   B 87  ? 0.7555 0.6900 0.3674 0.4532  -0.0751 -0.0089 96  GLN   B CA  
952  C  C   . GLN   B 87  ? 0.7189 0.6627 0.3598 0.4166  -0.0557 0.0023  96  GLN   B C   
953  O  O   . GLN   B 87  ? 0.7161 0.6417 0.3731 0.3894  -0.0592 -0.0048 96  GLN   B O   
954  C  CB  . GLN   B 87  ? 0.7755 0.7008 0.3864 0.4648  -0.0822 -0.0182 96  GLN   B CB  
955  C  CG  . GLN   B 87  ? 0.8033 0.7367 0.3845 0.5088  -0.0904 -0.0206 96  GLN   B CG  
956  C  CD  . GLN   B 87  ? 0.8349 0.7560 0.4120 0.5228  -0.1019 -0.0329 96  GLN   B CD  
957  O  OE1 . GLN   B 87  ? 0.8263 0.7432 0.4255 0.5018  -0.0963 -0.0343 96  GLN   B OE1 
958  N  NE2 . GLN   B 87  ? 0.8452 0.7608 0.3924 0.5610  -0.1190 -0.0429 96  GLN   B NE2 
959  N  N   . LEU   B 88  ? 0.6849 0.6578 0.3325 0.4166  -0.0361 0.0203  97  LEU   B N   
960  C  CA  . LEU   B 88  ? 0.6586 0.6396 0.3325 0.3852  -0.0189 0.0307  97  LEU   B CA  
961  C  C   . LEU   B 88  ? 0.6425 0.6239 0.3256 0.3856  -0.0115 0.0324  97  LEU   B C   
962  O  O   . LEU   B 88  ? 0.6429 0.6402 0.3160 0.4096  -0.0059 0.0408  97  LEU   B O   
963  C  CB  . LEU   B 88  ? 0.6483 0.6603 0.3270 0.3854  -0.0030 0.0501  97  LEU   B CB  
964  C  CG  . LEU   B 88  ? 0.6542 0.6770 0.3596 0.3578  0.0150  0.0635  97  LEU   B CG  
965  C  CD1 . LEU   B 88  ? 0.6595 0.6611 0.3803 0.3254  0.0126  0.0540  97  LEU   B CD1 
966  C  CD2 . LEU   B 88  ? 0.6494 0.7042 0.3616 0.3583  0.0279  0.0829  97  LEU   B CD2 
967  N  N   . LEU   B 89  ? 0.6283 0.5932 0.3284 0.3618  -0.0117 0.0246  98  LEU   B N   
968  C  CA  . LEU   B 89  ? 0.6114 0.5766 0.3203 0.3618  -0.0045 0.0259  98  LEU   B CA  
969  C  C   . LEU   B 89  ? 0.6045 0.5826 0.3308 0.3418  0.0142  0.0418  98  LEU   B C   
970  O  O   . LEU   B 89  ? 0.6013 0.5704 0.3440 0.3153  0.0177  0.0389  98  LEU   B O   
971  C  CB  . LEU   B 89  ? 0.6096 0.5537 0.3277 0.3491  -0.0150 0.0094  98  LEU   B CB  
972  C  CG  . LEU   B 89  ? 0.6218 0.5653 0.3523 0.3443  -0.0072 0.0091  98  LEU   B CG  
973  C  CD1 . LEU   B 89  ? 0.6280 0.5832 0.3468 0.3704  -0.0009 0.0182  98  LEU   B CD1 
974  C  CD2 . LEU   B 89  ? 0.6326 0.5609 0.3697 0.3391  -0.0208 -0.0080 98  LEU   B CD2 
975  N  N   . ALA   B 90  ? 0.6014 0.6019 0.3238 0.3546  0.0252  0.0593  99  ALA   B N   
976  C  CA  . ALA   B 90  ? 0.5927 0.6070 0.3326 0.3363  0.0412  0.0767  99  ALA   B CA  
977  C  C   . ALA   B 90  ? 0.5905 0.5976 0.3411 0.3287  0.0495  0.0807  99  ALA   B C   
978  O  O   . ALA   B 90  ? 0.6048 0.6138 0.3454 0.3497  0.0501  0.0826  99  ALA   B O   
979  C  CB  . ALA   B 90  ? 0.5824 0.6263 0.3165 0.3537  0.0499  0.0960  99  ALA   B CB  
980  N  N   . VAL   B 91  ? 0.5715 0.5701 0.3405 0.3010  0.0554  0.0821  100 VAL   B N   
981  C  CA  . VAL   B 91  ? 0.5704 0.5594 0.3489 0.2933  0.0627  0.0860  100 VAL   B CA  
982  C  C   . VAL   B 91  ? 0.5782 0.5774 0.3719 0.2772  0.0743  0.1056  100 VAL   B C   
983  O  O   . VAL   B 91  ? 0.5845 0.5751 0.3915 0.2531  0.0748  0.1031  100 VAL   B O   
984  C  CB  . VAL   B 91  ? 0.5703 0.5376 0.3557 0.2767  0.0567  0.0678  100 VAL   B CB  
985  C  CG1 . VAL   B 91  ? 0.5747 0.5305 0.3672 0.2715  0.0629  0.0699  100 VAL   B CG1 
986  C  CG2 . VAL   B 91  ? 0.5705 0.5307 0.3453 0.2893  0.0437  0.0503  100 VAL   B CG2 
987  N  N   . PRO   B 92  ? 0.5794 0.5985 0.3716 0.2906  0.0831  0.1259  101 PRO   B N   
988  C  CA  . PRO   B 92  ? 0.5734 0.6045 0.3837 0.2733  0.0930  0.1465  101 PRO   B CA  
989  C  C   . PRO   B 92  ? 0.5805 0.5919 0.4027 0.2578  0.0976  0.1519  101 PRO   B C   
990  O  O   . PRO   B 92  ? 0.5869 0.5824 0.4005 0.2679  0.0966  0.1451  101 PRO   B O   
991  C  CB  . PRO   B 92  ? 0.5737 0.6362 0.3778 0.2956  0.1011  0.1676  101 PRO   B CB  
992  C  CG  . PRO   B 92  ? 0.5862 0.6504 0.3653 0.3261  0.0936  0.1549  101 PRO   B CG  
993  C  CD  . PRO   B 92  ? 0.5768 0.6104 0.3510 0.3224  0.0841  0.1320  101 PRO   B CD  
994  N  N   . PRO   B 93  ? 0.5781 0.5890 0.4196 0.2339  0.1012  0.1630  102 PRO   B N   
995  C  CA  . PRO   B 93  ? 0.5892 0.5765 0.4402 0.2196  0.1032  0.1672  102 PRO   B CA  
996  C  C   . PRO   B 93  ? 0.6062 0.5949 0.4522 0.2353  0.1112  0.1849  102 PRO   B C   
997  O  O   . PRO   B 93  ? 0.6042 0.6191 0.4515 0.2460  0.1192  0.2061  102 PRO   B O   
998  C  CB  . PRO   B 93  ? 0.5857 0.5766 0.4585 0.1932  0.1036  0.1781  102 PRO   B CB  
999  C  CG  . PRO   B 93  ? 0.5828 0.5921 0.4554 0.1909  0.0993  0.1698  102 PRO   B CG  
1000 C  CD  . PRO   B 93  ? 0.5622 0.5920 0.4175 0.2189  0.1015  0.1707  102 PRO   B CD  
1001 N  N   . GLY   B 94  ? 0.6182 0.5805 0.4568 0.2391  0.1092  0.1759  103 GLY   B N   
1002 C  CA  . GLY   B 94  ? 0.6220 0.5799 0.4529 0.2549  0.1157  0.1903  103 GLY   B CA  
1003 C  C   . GLY   B 94  ? 0.6195 0.5967 0.4309 0.2870  0.1184  0.1922  103 GLY   B C   
1004 O  O   . GLY   B 94  ? 0.6128 0.5915 0.4160 0.3031  0.1251  0.2072  103 GLY   B O   
1005 N  N   . GLU   B 95  ? 0.6216 0.6132 0.4243 0.2974  0.1127  0.1779  104 GLU   B N   
1006 C  CA  . GLU   B 95  ? 0.6287 0.6377 0.4111 0.3295  0.1124  0.1774  104 GLU   B CA  
1007 C  C   . GLU   B 95  ? 0.6484 0.6440 0.4182 0.3391  0.0993  0.1482  104 GLU   B C   
1008 O  O   . GLU   B 95  ? 0.6474 0.6306 0.4256 0.3201  0.0922  0.1317  104 GLU   B O   
1009 C  CB  . GLU   B 95  ? 0.6276 0.6706 0.4102 0.3370  0.1169  0.1917  104 GLU   B CB  
1010 C  CG  . GLU   B 95  ? 0.6626 0.7256 0.4617 0.3270  0.1303  0.2233  104 GLU   B CG  
1011 C  CD  . GLU   B 95  ? 0.7202 0.8209 0.5248 0.3303  0.1351  0.2379  104 GLU   B CD  
1012 O  OE1 . GLU   B 95  ? 0.7277 0.8362 0.5216 0.3401  0.1271  0.2218  104 GLU   B OE1 
1013 O  OE2 . GLU   B 95  ? 0.7279 0.8508 0.5483 0.3229  0.1465  0.2659  104 GLU   B OE2 
1014 N  N   . ARG   B 96  ? 0.6653 0.6642 0.4155 0.3684  0.0957  0.1428  105 ARG   B N   
1015 C  CA  . ARG   B 96  ? 0.6971 0.6846 0.4363 0.3796  0.0817  0.1167  105 ARG   B CA  
1016 C  C   . ARG   B 96  ? 0.7125 0.7071 0.4497 0.3777  0.0719  0.1041  105 ARG   B C   
1017 O  O   . ARG   B 96  ? 0.7146 0.7286 0.4501 0.3811  0.0760  0.1163  105 ARG   B O   
1018 C  CB  . ARG   B 96  ? 0.7335 0.7256 0.4510 0.4145  0.0798  0.1171  105 ARG   B CB  
1019 C  CG  . ARG   B 96  ? 0.8042 0.7815 0.5136 0.4255  0.0649  0.0914  105 ARG   B CG  
1020 C  CD  . ARG   B 96  ? 0.8796 0.8531 0.5744 0.4508  0.0659  0.0934  105 ARG   B CD  
1021 N  NE  . ARG   B 96  ? 0.9335 0.9258 0.6076 0.4819  0.0703  0.1081  105 ARG   B NE  
1022 C  CZ  . ARG   B 96  ? 0.9750 0.9744 0.6424 0.4937  0.0838  0.1310  105 ARG   B CZ  
1023 N  NH1 . ARG   B 96  ? 0.9721 0.9573 0.6518 0.4761  0.0928  0.1412  105 ARG   B NH1 
1024 N  NH2 . ARG   B 96  ? 0.9766 0.9967 0.6238 0.5241  0.0882  0.1444  105 ARG   B NH2 
1025 N  N   . ALA   B 97  ? 0.7193 0.6988 0.4568 0.3727  0.0588  0.0806  106 ALA   B N   
1026 C  CA  . ALA   B 97  ? 0.7316 0.7117 0.4656 0.3712  0.0469  0.0671  106 ALA   B CA  
1027 C  C   . ALA   B 97  ? 0.7549 0.7481 0.4666 0.4039  0.0410  0.0686  106 ALA   B C   
1028 O  O   . ALA   B 97  ? 0.7687 0.7619 0.4665 0.4285  0.0383  0.0668  106 ALA   B O   
1029 C  CB  . ALA   B 97  ? 0.7335 0.6958 0.4725 0.3626  0.0342  0.0446  106 ALA   B CB  
1030 N  N   . LYS   B 98  ? 0.7599 0.7651 0.4665 0.4064  0.0392  0.0724  107 LYS   B N   
1031 C  CA  . LYS   B 98  ? 0.7699 0.7898 0.4531 0.4398  0.0343  0.0750  107 LYS   B CA  
1032 C  C   . LYS   B 98  ? 0.7645 0.7804 0.4390 0.4418  0.0201  0.0623  107 LYS   B C   
1033 O  O   . LYS   B 98  ? 0.7606 0.7806 0.4462 0.4215  0.0238  0.0667  107 LYS   B O   
1034 C  CB  . LYS   B 98  ? 0.7990 0.8474 0.4829 0.4471  0.0523  0.1022  107 LYS   B CB  
1035 C  CG  . LYS   B 98  ? 0.8822 0.9537 0.5412 0.4850  0.0520  0.1102  107 LYS   B CG  
1036 C  CD  . LYS   B 98  ? 0.9502 1.0557 0.6168 0.4857  0.0717  0.1403  107 LYS   B CD  
1037 C  CE  . LYS   B 98  ? 1.0024 1.1133 0.6947 0.4509  0.0784  0.1484  107 LYS   B CE  
1038 N  NZ  . LYS   B 98  ? 1.0273 1.1752 0.7202 0.4597  0.0877  0.1683  107 LYS   B NZ  
1039 N  N   . ASN   B 99  ? 0.7661 0.7721 0.4200 0.4667  0.0025  0.0462  108 ASN   B N   
1040 C  CA  . ASN   B 99  ? 0.7766 0.7734 0.4186 0.4718  -0.0141 0.0333  108 ASN   B CA  
1041 C  C   . ASN   B 99  ? 0.7823 0.8033 0.4051 0.4977  -0.0103 0.0453  108 ASN   B C   
1042 O  O   . ASN   B 99  ? 0.7923 0.8297 0.3978 0.5286  -0.0064 0.0531  108 ASN   B O   
1043 C  CB  . ASN   B 99  ? 0.7946 0.7683 0.4222 0.4886  -0.0373 0.0107  108 ASN   B CB  
1044 C  CG  . ASN   B 99  ? 0.8224 0.7754 0.4704 0.4631  -0.0434 -0.0024 108 ASN   B CG  
1045 O  OD1 . ASN   B 99  ? 0.8287 0.7843 0.4885 0.4565  -0.0335 0.0013  108 ASN   B OD1 
1046 N  ND2 . ASN   B 99  ? 0.8304 0.7630 0.4826 0.4491  -0.0599 -0.0174 108 ASN   B ND2 
1047 N  N   . ILE   B 100 ? 0.7750 0.8001 0.3998 0.4873  -0.0114 0.0471  109 ILE   B N   
1048 C  CA  . ILE   B 100 ? 0.7764 0.8270 0.3840 0.5115  -0.0085 0.0577  109 ILE   B CA  
1049 C  C   . ILE   B 100 ? 0.7932 0.8244 0.3836 0.5188  -0.0296 0.0402  109 ILE   B C   
1050 O  O   . ILE   B 100 ? 0.7926 0.8100 0.3962 0.4913  -0.0328 0.0353  109 ILE   B O   
1051 C  CB  . ILE   B 100 ? 0.7675 0.8465 0.3964 0.4908  0.0123  0.0802  109 ILE   B CB  
1052 C  CG1 . ILE   B 100 ? 0.7714 0.8623 0.4207 0.4768  0.0314  0.0976  109 ILE   B CG1 
1053 C  CG2 . ILE   B 100 ? 0.7664 0.8781 0.3797 0.5169  0.0160  0.0923  109 ILE   B CG2 
1054 C  CD1 . ILE   B 100 ? 0.7825 0.8967 0.4169 0.5094  0.0404  0.1121  109 ILE   B CD1 
1055 N  N   . GLN   B 101 ? 0.8045 0.8330 0.3640 0.5569  -0.0447 0.0307  110 GLN   B N   
1056 C  CA  . GLN   B 101 ? 0.8257 0.8312 0.3651 0.5677  -0.0676 0.0133  110 GLN   B CA  
1057 C  C   . GLN   B 101 ? 0.8256 0.8561 0.3548 0.5794  -0.0620 0.0241  110 GLN   B C   
1058 O  O   . GLN   B 101 ? 0.8179 0.8865 0.3417 0.5998  -0.0464 0.0419  110 GLN   B O   
1059 C  CB  . GLN   B 101 ? 0.8656 0.8526 0.3746 0.6047  -0.0898 -0.0042 110 GLN   B CB  
1060 C  CG  . GLN   B 101 ? 0.9172 0.8733 0.4029 0.6176  -0.1179 -0.0241 110 GLN   B CG  
1061 C  CD  . GLN   B 101 ? 0.9676 0.8944 0.4339 0.6406  -0.1434 -0.0452 110 GLN   B CD  
1062 O  OE1 . GLN   B 101 ? 0.9633 0.8804 0.4448 0.6286  -0.1439 -0.0502 110 GLN   B OE1 
1063 N  NE2 . GLN   B 101 ? 0.9890 0.9007 0.4208 0.6751  -0.1663 -0.0589 110 GLN   B NE2 
1064 N  N   . THR   B 102 ? 0.8313 0.8425 0.3596 0.5651  -0.0735 0.0153  111 THR   B N   
1065 C  CA  . THR   B 102 ? 0.8343 0.8678 0.3528 0.5758  -0.0701 0.0236  111 THR   B CA  
1066 C  C   . THR   B 102 ? 0.8543 0.8521 0.3562 0.5752  -0.0938 0.0057  111 THR   B C   
1067 O  O   . THR   B 102 ? 0.8677 0.8270 0.3764 0.5541  -0.1078 -0.0087 111 THR   B O   
1068 C  CB  . THR   B 102 ? 0.8382 0.9005 0.3891 0.5432  -0.0460 0.0438  111 THR   B CB  
1069 O  OG1 . THR   B 102 ? 0.8525 0.9454 0.3949 0.5581  -0.0411 0.0541  111 THR   B OG1 
1070 C  CG2 . THR   B 102 ? 0.8440 0.8786 0.4192 0.4995  -0.0474 0.0372  111 THR   B CG2 
1071 N  N   . LEU   B 103 ? 0.8577 0.8689 0.3386 0.5980  -0.0983 0.0074  112 LEU   B N   
1072 C  CA  . LEU   B 103 ? 0.8812 0.8575 0.3463 0.5958  -0.1200 -0.0077 112 LEU   B CA  
1073 C  C   . LEU   B 103 ? 0.8725 0.8644 0.3602 0.5649  -0.1055 0.0043  112 LEU   B C   
1074 O  O   . LEU   B 103 ? 0.8601 0.8950 0.3520 0.5733  -0.0891 0.0204  112 LEU   B O   
1075 C  CB  . LEU   B 103 ? 0.9030 0.8775 0.3263 0.6427  -0.1383 -0.0167 112 LEU   B CB  
1076 C  CG  . LEU   B 103 ? 0.9482 0.8796 0.3550 0.6378  -0.1624 -0.0323 112 LEU   B CG  
1077 C  CD1 . LEU   B 103 ? 0.9816 0.8584 0.3827 0.6302  -0.1879 -0.0524 112 LEU   B CD1 
1078 C  CD2 . LEU   B 103 ? 0.9667 0.9066 0.3365 0.6798  -0.1741 -0.0360 112 LEU   B CD2 
1079 N  N   . PRO   B 104 ? 0.8721 0.8317 0.3755 0.5291  -0.1111 -0.0026 113 PRO   B N   
1080 C  CA  . PRO   B 104 ? 0.8611 0.8342 0.3846 0.5003  -0.0980 0.0078  113 PRO   B CA  
1081 C  C   . PRO   B 104 ? 0.8769 0.8529 0.3779 0.5184  -0.1074 0.0061  113 PRO   B C   
1082 O  O   . PRO   B 104 ? 0.9008 0.8471 0.3711 0.5418  -0.1302 -0.0082 113 PRO   B O   
1083 C  CB  . PRO   B 104 ? 0.8717 0.8069 0.4125 0.4624  -0.1038 -0.0007 113 PRO   B CB  
1084 C  CG  . PRO   B 104 ? 0.8882 0.7980 0.4257 0.4678  -0.1156 -0.0123 113 PRO   B CG  
1085 C  CD  . PRO   B 104 ? 0.8776 0.7902 0.3828 0.5128  -0.1288 -0.0187 113 PRO   B CD  
1086 N  N   . GLY   B 105 ? 0.8571 0.8680 0.3740 0.5071  -0.0908 0.0205  114 GLY   B N   
1087 C  CA  . GLY   B 105 ? 0.8590 0.8765 0.3610 0.5171  -0.0967 0.0206  114 GLY   B CA  
1088 C  C   . GLY   B 105 ? 0.8674 0.8476 0.3755 0.4850  -0.1049 0.0130  114 GLY   B C   
1089 O  O   . GLY   B 105 ? 0.8797 0.8229 0.3943 0.4641  -0.1120 0.0044  114 GLY   B O   
1090 N  N   . ILE   B 106 ? 0.8551 0.8470 0.3619 0.4809  -0.1033 0.0172  115 ILE   B N   
1091 C  CA  . ILE   B 106 ? 0.8647 0.8233 0.3727 0.4545  -0.1110 0.0114  115 ILE   B CA  
1092 C  C   . ILE   B 106 ? 0.8395 0.8305 0.3688 0.4347  -0.0952 0.0232  115 ILE   B C   
1093 O  O   . ILE   B 106 ? 0.8399 0.8700 0.3664 0.4534  -0.0895 0.0313  115 ILE   B O   
1094 C  CB  . ILE   B 106 ? 0.9086 0.8353 0.3780 0.4801  -0.1352 -0.0007 115 ILE   B CB  
1095 C  CG1 . ILE   B 106 ? 0.9601 0.8511 0.4035 0.5047  -0.1563 -0.0147 115 ILE   B CG1 
1096 C  CG2 . ILE   B 106 ? 0.9288 0.8225 0.3964 0.4557  -0.1430 -0.0045 115 ILE   B CG2 
1097 C  CD1 . ILE   B 106 ? 0.9987 0.8446 0.4504 0.4794  -0.1661 -0.0232 115 ILE   B CD1 
1098 N  N   . PHE   B 107 ? 0.8169 0.7911 0.3652 0.3988  -0.0903 0.0234  116 PHE   B N   
1099 C  CA  . PHE   B 107 ? 0.7901 0.7847 0.3540 0.3795  -0.0806 0.0308  116 PHE   B CA  
1100 C  C   . PHE   B 107 ? 0.8044 0.7632 0.3432 0.3809  -0.0974 0.0217  116 PHE   B C   
1101 O  O   . PHE   B 107 ? 0.8148 0.7302 0.3465 0.3682  -0.1076 0.0136  116 PHE   B O   
1102 C  CB  . PHE   B 107 ? 0.7709 0.7625 0.3654 0.3416  -0.0674 0.0344  116 PHE   B CB  
1103 C  CG  . PHE   B 107 ? 0.7413 0.7708 0.3655 0.3324  -0.0488 0.0463  116 PHE   B CG  
1104 C  CD1 . PHE   B 107 ? 0.7296 0.7955 0.3546 0.3562  -0.0426 0.0552  116 PHE   B CD1 
1105 C  CD2 . PHE   B 107 ? 0.7328 0.7612 0.3829 0.3010  -0.0378 0.0493  116 PHE   B CD2 
1106 C  CE1 . PHE   B 107 ? 0.7146 0.8136 0.3676 0.3463  -0.0257 0.0684  116 PHE   B CE1 
1107 C  CE2 . PHE   B 107 ? 0.7227 0.7811 0.3991 0.2922  -0.0226 0.0604  116 PHE   B CE2 
1108 C  CZ  . PHE   B 107 ? 0.7079 0.8003 0.3863 0.3138  -0.0167 0.0705  116 PHE   B CZ  
1109 N  N   . LYS   B 108 ? 0.8061 0.7828 0.3317 0.3967  -0.1008 0.0237  117 LYS   B N   
1110 C  CA  . LYS   B 108 ? 0.8370 0.7795 0.3375 0.3986  -0.1166 0.0161  117 LYS   B CA  
1111 C  C   . LYS   B 108 ? 0.8180 0.7712 0.3375 0.3702  -0.1063 0.0216  117 LYS   B C   
1112 O  O   . LYS   B 108 ? 0.7972 0.7949 0.3331 0.3706  -0.0950 0.0299  117 LYS   B O   
1113 C  CB  . LYS   B 108 ? 0.8875 0.8420 0.3580 0.4370  -0.1283 0.0135  117 LYS   B CB  
1114 C  CG  . LYS   B 108 ? 0.9798 0.9325 0.4305 0.4709  -0.1374 0.0084  117 LYS   B CG  
1115 C  CD  . LYS   B 108 ? 1.0776 1.0458 0.4965 0.5131  -0.1487 0.0055  117 LYS   B CD  
1116 C  CE  . LYS   B 108 ? 1.1612 1.1353 0.5611 0.5493  -0.1554 0.0013  117 LYS   B CE  
1117 N  NZ  . LYS   B 108 ? 1.2028 1.1955 0.5699 0.5942  -0.1660 -0.0017 117 LYS   B NZ  
1118 N  N   . THR   B 109 ? 0.8246 0.7400 0.3441 0.3449  -0.1097 0.0178  118 THR   B N   
1119 C  CA  . THR   B 109 ? 0.8199 0.7409 0.3532 0.3192  -0.1014 0.0216  118 THR   B CA  
1120 C  C   . THR   B 109 ? 0.8411 0.7261 0.3465 0.3204  -0.1156 0.0169  118 THR   B C   
1121 O  O   . THR   B 109 ? 0.8592 0.7086 0.3378 0.3358  -0.1320 0.0109  118 THR   B O   
1122 C  CB  . THR   B 109 ? 0.8240 0.7399 0.3850 0.2867  -0.0885 0.0237  118 THR   B CB  
1123 O  OG1 . THR   B 109 ? 0.8552 0.7261 0.4059 0.2736  -0.0966 0.0188  118 THR   B OG1 
1124 C  CG2 . THR   B 109 ? 0.8073 0.7464 0.3907 0.2864  -0.0775 0.0273  118 THR   B CG2 
1125 N  N   . LYS   B 110 ? 0.8402 0.7316 0.3510 0.3041  -0.1103 0.0196  119 LYS   B N   
1126 C  CA  . LYS   B 110 ? 0.8696 0.7271 0.3543 0.3034  -0.1220 0.0170  119 LYS   B CA  
1127 C  C   . LYS   B 110 ? 0.9042 0.7125 0.3823 0.2851  -0.1276 0.0155  119 LYS   B C   
1128 O  O   . LYS   B 110 ? 0.9302 0.7016 0.3829 0.2874  -0.1404 0.0143  119 LYS   B O   
1129 C  CB  . LYS   B 110 ? 0.8605 0.7398 0.3531 0.2913  -0.1144 0.0202  119 LYS   B CB  
1130 C  CG  . LYS   B 110 ? 0.8939 0.7696 0.4078 0.2594  -0.1022 0.0225  119 LYS   B CG  
1131 C  CD  . LYS   B 110 ? 0.9215 0.8246 0.4457 0.2503  -0.0954 0.0242  119 LYS   B CD  
1132 C  CE  . LYS   B 110 ? 0.9626 0.8510 0.4942 0.2241  -0.0879 0.0247  119 LYS   B CE  
1133 N  NZ  . LYS   B 110 ? 0.9712 0.8663 0.5301 0.2062  -0.0759 0.0257  119 LYS   B NZ  
1134 N  N   . ASP   B 111 ? 0.8981 0.7073 0.3999 0.2671  -0.1180 0.0165  120 ASP   B N   
1135 C  CA  . ASP   B 111 ? 0.9214 0.6937 0.4244 0.2482  -0.1211 0.0165  120 ASP   B CA  
1136 C  C   . ASP   B 111 ? 0.9424 0.6952 0.4434 0.2576  -0.1311 0.0118  120 ASP   B C   
1137 O  O   . ASP   B 111 ? 0.9558 0.6862 0.4660 0.2400  -0.1319 0.0122  120 ASP   B O   
1138 C  CB  . ASP   B 111 ? 0.9260 0.7141 0.4575 0.2203  -0.1033 0.0204  120 ASP   B CB  
1139 C  CG  . ASP   B 111 ? 0.9718 0.7749 0.5043 0.2102  -0.0952 0.0235  120 ASP   B CG  
1140 O  OD1 . ASP   B 111 ? 0.9933 0.7745 0.5036 0.2115  -0.1032 0.0247  120 ASP   B OD1 
1141 O  OD2 . ASP   B 111 ? 0.9832 0.8183 0.5380 0.2015  -0.0820 0.0246  120 ASP   B OD2 
1142 N  N   . GLY   B 112 ? 0.9432 0.7070 0.4331 0.2855  -0.1385 0.0076  121 GLY   B N   
1143 C  CA  . GLY   B 112 ? 0.9572 0.7020 0.4413 0.2986  -0.1502 0.0015  121 GLY   B CA  
1144 C  C   . GLY   B 112 ? 0.9436 0.7252 0.4417 0.3133  -0.1411 0.0011  121 GLY   B C   
1145 O  O   . GLY   B 112 ? 0.9257 0.7485 0.4433 0.3087  -0.1239 0.0071  121 GLY   B O   
1146 N  N   . ASP   B 113 ? 0.9477 0.7134 0.4360 0.3308  -0.1534 -0.0056 122 ASP   B N   
1147 C  CA  . ASP   B 113 ? 0.9358 0.7339 0.4335 0.3477  -0.1456 -0.0054 122 ASP   B CA  
1148 C  C   . ASP   B 113 ? 0.9195 0.7210 0.4447 0.3276  -0.1351 -0.0044 122 ASP   B C   
1149 O  O   . ASP   B 113 ? 0.9332 0.7031 0.4636 0.3091  -0.1416 -0.0078 122 ASP   B O   
1150 C  CB  . ASP   B 113 ? 0.9801 0.7649 0.4477 0.3851  -0.1647 -0.0140 122 ASP   B CB  
1151 C  CG  . ASP   B 113 ? 1.0740 0.8604 0.5124 0.4110  -0.1749 -0.0155 122 ASP   B CG  
1152 O  OD1 . ASP   B 113 ? 1.0831 0.8880 0.5271 0.4007  -0.1654 -0.0090 122 ASP   B OD1 
1153 O  OD2 . ASP   B 113 ? 1.1293 0.8984 0.5382 0.4431  -0.1935 -0.0241 122 ASP   B OD2 
1154 N  N   . ILE   B 114 ? 0.8808 0.7222 0.4245 0.3313  -0.1187 0.0012  123 ILE   B N   
1155 C  CA  . ILE   B 114 ? 0.8619 0.7108 0.4304 0.3161  -0.1075 0.0026  123 ILE   B CA  
1156 C  C   . ILE   B 114 ? 0.8291 0.7020 0.3949 0.3427  -0.1052 0.0033  123 ILE   B C   
1157 O  O   . ILE   B 114 ? 0.8104 0.7146 0.3705 0.3619  -0.0998 0.0092  123 ILE   B O   
1158 C  CB  . ILE   B 114 ? 0.8564 0.7306 0.4532 0.2885  -0.0867 0.0114  123 ILE   B CB  
1159 C  CG1 . ILE   B 114 ? 0.8838 0.7404 0.4790 0.2671  -0.0879 0.0117  123 ILE   B CG1 
1160 C  CG2 . ILE   B 114 ? 0.8521 0.7302 0.4726 0.2728  -0.0762 0.0121  123 ILE   B CG2 
1161 C  CD1 . ILE   B 114 ? 0.8943 0.7760 0.5117 0.2453  -0.0704 0.0187  123 ILE   B CD1 
1162 N  N   . GLY   B 115 ? 0.8163 0.6776 0.3871 0.3443  -0.1085 -0.0017 124 GLY   B N   
1163 C  CA  . GLY   B 115 ? 0.8028 0.6870 0.3706 0.3698  -0.1051 -0.0004 124 GLY   B CA  
1164 C  C   . GLY   B 115 ? 0.7739 0.7015 0.3662 0.3612  -0.0813 0.0133  124 GLY   B C   
1165 O  O   . GLY   B 115 ? 0.7633 0.6959 0.3778 0.3321  -0.0693 0.0185  124 GLY   B O   
1166 N  N   . ALA   B 116 ? 0.7596 0.7187 0.3472 0.3869  -0.0751 0.0200  125 ALA   B N   
1167 C  CA  . ALA   B 116 ? 0.7415 0.7418 0.3536 0.3785  -0.0534 0.0354  125 ALA   B CA  
1168 C  C   . ALA   B 116 ? 0.7445 0.7682 0.3542 0.4029  -0.0470 0.0416  125 ALA   B C   
1169 O  O   . ALA   B 116 ? 0.7632 0.7930 0.3486 0.4365  -0.0557 0.0390  125 ALA   B O   
1170 C  CB  . ALA   B 116 ? 0.7259 0.7561 0.3415 0.3784  -0.0466 0.0451  125 ALA   B CB  
1171 N  N   . VAL   B 117 ? 0.7311 0.7671 0.3641 0.3878  -0.0323 0.0498  126 VAL   B N   
1172 C  CA  A VAL   B 117 ? 0.7315 0.7898 0.3631 0.4095  -0.0245 0.0578  126 VAL   B CA  
1173 C  CA  B VAL   B 117 ? 0.7325 0.7899 0.3651 0.4080  -0.0243 0.0577  126 VAL   B CA  
1174 C  C   . VAL   B 117 ? 0.7235 0.8294 0.3727 0.4096  -0.0054 0.0791  126 VAL   B C   
1175 O  O   . VAL   B 117 ? 0.7144 0.8305 0.3889 0.3811  0.0053  0.0876  126 VAL   B O   
1176 C  CB  A VAL   B 117 ? 0.7358 0.7743 0.3760 0.4007  -0.0234 0.0525  126 VAL   B CB  
1177 C  CB  B VAL   B 117 ? 0.7377 0.7732 0.3841 0.3904  -0.0220 0.0525  126 VAL   B CB  
1178 C  CG1 A VAL   B 117 ? 0.7576 0.7547 0.3799 0.4062  -0.0445 0.0325  126 VAL   B CG1 
1179 C  CG1 B VAL   B 117 ? 0.7296 0.7915 0.3912 0.3924  -0.0048 0.0673  126 VAL   B CG1 
1180 C  CG2 A VAL   B 117 ? 0.7312 0.7680 0.4016 0.3638  -0.0105 0.0578  126 VAL   B CG2 
1181 C  CG2 B VAL   B 117 ? 0.7581 0.7590 0.3838 0.4053  -0.0414 0.0346  126 VAL   B CG2 
1182 N  N   . ALA   B 118 ? 0.7246 0.8613 0.3594 0.4431  -0.0023 0.0881  127 ALA   B N   
1183 C  CA  . ALA   B 118 ? 0.7196 0.9067 0.3724 0.4448  0.0157  0.1110  127 ALA   B CA  
1184 C  C   . ALA   B 118 ? 0.7313 0.9344 0.3967 0.4467  0.0301  0.1251  127 ALA   B C   
1185 O  O   . ALA   B 118 ? 0.7399 0.9688 0.3916 0.4780  0.0346  0.1342  127 ALA   B O   
1186 C  CB  . ALA   B 118 ? 0.7200 0.9381 0.3510 0.4805  0.0124  0.1153  127 ALA   B CB  
1187 N  N   . LEU   B 119 ? 0.7307 0.9164 0.4195 0.4152  0.0367  0.1260  128 LEU   B N   
1188 C  CA  . LEU   B 119 ? 0.7317 0.9255 0.4326 0.4135  0.0493  0.1384  128 LEU   B CA  
1189 C  C   . LEU   B 119 ? 0.7226 0.9270 0.4588 0.3779  0.0626  0.1530  128 LEU   B C   
1190 O  O   . LEU   B 119 ? 0.7300 0.9116 0.4779 0.3498  0.0581  0.1431  128 LEU   B O   
1191 C  CB  . LEU   B 119 ? 0.7543 0.9067 0.4444 0.4134  0.0395  0.1203  128 LEU   B CB  
1192 C  CG  . LEU   B 119 ? 0.7865 0.9261 0.4428 0.4495  0.0244  0.1058  128 LEU   B CG  
1193 C  CD1 . LEU   B 119 ? 0.8052 0.9033 0.4562 0.4432  0.0123  0.0865  128 LEU   B CD1 
1194 C  CD2 . LEU   B 119 ? 0.7915 0.9640 0.4351 0.4834  0.0331  0.1205  128 LEU   B CD2 
1195 N  N   . ASP   B 120 ? 0.7034 0.9417 0.4560 0.3791  0.0783  0.1769  129 ASP   B N   
1196 C  CA  . ASP   B 120 ? 0.6923 0.9393 0.4792 0.3453  0.0888  0.1917  129 ASP   B CA  
1197 C  C   . ASP   B 120 ? 0.6768 0.9041 0.4749 0.3319  0.0955  0.1963  129 ASP   B C   
1198 O  O   . ASP   B 120 ? 0.6801 0.9169 0.4697 0.3521  0.1022  0.2063  129 ASP   B O   
1199 C  CB  . ASP   B 120 ? 0.7101 1.0098 0.5147 0.3486  0.1004  0.2174  129 ASP   B CB  
1200 C  CG  . ASP   B 120 ? 0.7795 1.0874 0.6193 0.3119  0.1047  0.2278  129 ASP   B CG  
1201 O  OD1 . ASP   B 120 ? 0.7982 1.0975 0.6591 0.2907  0.1118  0.2385  129 ASP   B OD1 
1202 O  OD2 . ASP   B 120 ? 0.7943 1.1162 0.6397 0.3054  0.0999  0.2250  129 ASP   B OD2 
1203 N  N   . TYR   B 121 ? 0.6624 0.8618 0.4776 0.2999  0.0933  0.1887  130 TYR   B N   
1204 C  CA  . TYR   B 121 ? 0.6539 0.8295 0.4781 0.2867  0.0976  0.1899  130 TYR   B CA  
1205 C  C   . TYR   B 121 ? 0.6278 0.7950 0.4806 0.2510  0.1002  0.1956  130 TYR   B C   
1206 O  O   . TYR   B 121 ? 0.6241 0.7944 0.4858 0.2354  0.0953  0.1907  130 TYR   B O   
1207 C  CB  . TYR   B 121 ? 0.6751 0.8114 0.4805 0.2908  0.0867  0.1644  130 TYR   B CB  
1208 C  CG  . TYR   B 121 ? 0.6972 0.8330 0.4783 0.3233  0.0845  0.1605  130 TYR   B CG  
1209 C  CD1 . TYR   B 121 ? 0.7126 0.8407 0.4926 0.3301  0.0902  0.1660  130 TYR   B CD1 
1210 C  CD2 . TYR   B 121 ? 0.7165 0.8573 0.4741 0.3486  0.0750  0.1503  130 TYR   B CD2 
1211 C  CE1 . TYR   B 121 ? 0.7357 0.8638 0.4923 0.3617  0.0871  0.1617  130 TYR   B CE1 
1212 C  CE2 . TYR   B 121 ? 0.7391 0.8784 0.4730 0.3804  0.0707  0.1454  130 TYR   B CE2 
1213 C  CZ  . TYR   B 121 ? 0.7544 0.8882 0.4881 0.3869  0.0769  0.1510  130 TYR   B CZ  
1214 O  OH  . TYR   B 121 ? 0.7886 0.9205 0.4979 0.4194  0.0716  0.1451  130 TYR   B OH  
1215 N  N   . PRO   B 122 ? 0.6139 0.7659 0.4791 0.2380  0.1058  0.2035  131 PRO   B N   
1216 C  CA  . PRO   B 122 ? 0.6009 0.7382 0.4902 0.2051  0.1046  0.2052  131 PRO   B CA  
1217 C  C   . PRO   B 122 ? 0.5992 0.7074 0.4823 0.1914  0.0934  0.1794  131 PRO   B C   
1218 O  O   . PRO   B 122 ? 0.6161 0.7046 0.4796 0.2030  0.0881  0.1615  131 PRO   B O   
1219 C  CB  . PRO   B 122 ? 0.6136 0.7311 0.5076 0.2009  0.1099  0.2129  131 PRO   B CB  
1220 C  CG  . PRO   B 122 ? 0.6178 0.7550 0.4974 0.2304  0.1181  0.2260  131 PRO   B CG  
1221 C  CD  . PRO   B 122 ? 0.6082 0.7528 0.4641 0.2538  0.1117  0.2098  131 PRO   B CD  
1222 N  N   . ALA   B 123 ? 0.5748 0.6827 0.4740 0.1683  0.0892  0.1779  132 ALA   B N   
1223 C  CA  . ALA   B 123 ? 0.5679 0.6521 0.4598 0.1569  0.0795  0.1554  132 ALA   B CA  
1224 C  C   . ALA   B 123 ? 0.5620 0.6093 0.4431 0.1542  0.0762  0.1377  132 ALA   B C   
1225 O  O   . ALA   B 123 ? 0.5665 0.5989 0.4343 0.1551  0.0697  0.1196  132 ALA   B O   
1226 C  CB  . ALA   B 123 ? 0.5610 0.6488 0.4725 0.1327  0.0756  0.1578  132 ALA   B CB  
1227 N  N   . GLY   B 124 ? 0.5480 0.5832 0.4341 0.1532  0.0808  0.1443  133 GLY   B N   
1228 C  CA  . GLY   B 124 ? 0.5405 0.5458 0.4167 0.1544  0.0786  0.1293  133 GLY   B CA  
1229 C  C   . GLY   B 124 ? 0.5294 0.5328 0.3857 0.1764  0.0770  0.1184  133 GLY   B C   
1230 O  O   . GLY   B 124 ? 0.5348 0.5179 0.3840 0.1791  0.0749  0.1061  133 GLY   B O   
1231 N  N   . THR   B 125 ? 0.5170 0.5418 0.3640 0.1934  0.0767  0.1225  134 THR   B N   
1232 C  CA  . THR   B 125 ? 0.5252 0.5472 0.3524 0.2150  0.0717  0.1112  134 THR   B CA  
1233 C  C   . THR   B 125 ? 0.5178 0.5284 0.3371 0.2085  0.0620  0.0934  134 THR   B C   
1234 O  O   . THR   B 125 ? 0.5192 0.5200 0.3248 0.2205  0.0551  0.0812  134 THR   B O   
1235 C  CB  . THR   B 125 ? 0.5472 0.5961 0.3653 0.2400  0.0753  0.1249  134 THR   B CB  
1236 O  OG1 . THR   B 125 ? 0.5553 0.6153 0.3823 0.2432  0.0856  0.1441  134 THR   B OG1 
1237 C  CG2 . THR   B 125 ? 0.5606 0.6041 0.3564 0.2653  0.0678  0.1128  134 THR   B CG2 
1238 N  N   . SER   B 126 ? 0.5084 0.5199 0.3367 0.1895  0.0607  0.0926  135 SER   B N   
1239 C  CA  . SER   B 126 ? 0.5165 0.5175 0.3372 0.1823  0.0526  0.0784  135 SER   B CA  
1240 C  C   . SER   B 126 ? 0.5215 0.4987 0.3376 0.1780  0.0489  0.0629  135 SER   B C   
1241 O  O   . SER   B 126 ? 0.5134 0.4805 0.3374 0.1699  0.0528  0.0615  135 SER   B O   
1242 C  CB  . SER   B 126 ? 0.5323 0.5357 0.3643 0.1618  0.0528  0.0801  135 SER   B CB  
1243 O  OG  . SER   B 126 ? 0.5523 0.5810 0.3936 0.1627  0.0562  0.0954  135 SER   B OG  
1244 N  N   . GLY   B 127 ? 0.5221 0.4916 0.3259 0.1844  0.0409  0.0523  136 GLY   B N   
1245 C  CA  . GLY   B 127 ? 0.5352 0.4872 0.3366 0.1811  0.0367  0.0392  136 GLY   B CA  
1246 C  C   . GLY   B 127 ? 0.5461 0.4956 0.3392 0.2005  0.0316  0.0352  136 GLY   B C   
1247 O  O   . GLY   B 127 ? 0.5522 0.4898 0.3443 0.1991  0.0257  0.0243  136 GLY   B O   
1248 N  N   . SER   B 128 ? 0.5444 0.5067 0.3321 0.2192  0.0337  0.0444  137 SER   B N   
1249 C  CA  . SER   B 128 ? 0.5497 0.5105 0.3263 0.2417  0.0278  0.0404  137 SER   B CA  
1250 C  C   . SER   B 128 ? 0.5612 0.5119 0.3247 0.2486  0.0135  0.0295  137 SER   B C   
1251 O  O   . SER   B 128 ? 0.5588 0.5125 0.3156 0.2480  0.0100  0.0314  137 SER   B O   
1252 C  CB  . SER   B 128 ? 0.5608 0.5407 0.3314 0.2618  0.0336  0.0544  137 SER   B CB  
1253 O  OG  . SER   B 128 ? 0.5721 0.5583 0.3546 0.2563  0.0455  0.0659  137 SER   B OG  
1254 N  N   . PRO   B 129 ? 0.5682 0.5058 0.3285 0.2548  0.0039  0.0179  138 PRO   B N   
1255 C  CA  . PRO   B 129 ? 0.5784 0.5018 0.3278 0.2592  -0.0121 0.0076  138 PRO   B CA  
1256 C  C   . PRO   B 129 ? 0.6000 0.5252 0.3287 0.2869  -0.0226 0.0071  138 PRO   B C   
1257 O  O   . PRO   B 129 ? 0.5915 0.5260 0.3124 0.3087  -0.0211 0.0101  138 PRO   B O   
1258 C  CB  . PRO   B 129 ? 0.5852 0.4964 0.3430 0.2543  -0.0191 -0.0036 138 PRO   B CB  
1259 C  CG  . PRO   B 129 ? 0.5853 0.5059 0.3485 0.2631  -0.0097 -0.0002 138 PRO   B CG  
1260 C  CD  . PRO   B 129 ? 0.5590 0.4931 0.3268 0.2567  0.0062  0.0136  138 PRO   B CD  
1261 N  N   . ILE   B 130 ? 0.6198 0.5340 0.3371 0.2876  -0.0343 0.0024  139 ILE   B N   
1262 C  CA  . ILE   B 130 ? 0.6339 0.5444 0.3280 0.3152  -0.0481 -0.0013 139 ILE   B CA  
1263 C  C   . ILE   B 130 ? 0.6549 0.5387 0.3448 0.3166  -0.0681 -0.0165 139 ILE   B C   
1264 O  O   . ILE   B 130 ? 0.6564 0.5252 0.3579 0.2933  -0.0723 -0.0211 139 ILE   B O   
1265 C  CB  . ILE   B 130 ? 0.6405 0.5553 0.3236 0.3167  -0.0491 0.0036  139 ILE   B CB  
1266 C  CG1 . ILE   B 130 ? 0.6416 0.5866 0.3335 0.3143  -0.0300 0.0195  139 ILE   B CG1 
1267 C  CG2 . ILE   B 130 ? 0.6570 0.5635 0.3130 0.3466  -0.0664 -0.0030 139 ILE   B CG2 
1268 C  CD1 . ILE   B 130 ? 0.6549 0.6075 0.3430 0.3085  -0.0288 0.0248  139 ILE   B CD1 
1269 N  N   . LEU   B 131 ? 0.6685 0.5479 0.3437 0.3433  -0.0802 -0.0237 140 LEU   B N   
1270 C  CA  . LEU   B 131 ? 0.6960 0.5510 0.3701 0.3451  -0.1009 -0.0385 140 LEU   B CA  
1271 C  C   . LEU   B 131 ? 0.7416 0.5772 0.3898 0.3690  -0.1239 -0.0482 140 LEU   B C   
1272 O  O   . LEU   B 131 ? 0.7638 0.6102 0.3902 0.3964  -0.1235 -0.0449 140 LEU   B O   
1273 C  CB  . LEU   B 131 ? 0.6908 0.5529 0.3699 0.3575  -0.0996 -0.0424 140 LEU   B CB  
1274 C  CG  . LEU   B 131 ? 0.6874 0.5699 0.3852 0.3451  -0.0772 -0.0326 140 LEU   B CG  
1275 C  CD1 . LEU   B 131 ? 0.6879 0.5742 0.3845 0.3633  -0.0796 -0.0376 140 LEU   B CD1 
1276 C  CD2 . LEU   B 131 ? 0.6848 0.5637 0.4066 0.3106  -0.0700 -0.0320 140 LEU   B CD2 
1277 N  N   . ASP   B 132 ? 0.7600 0.5672 0.4103 0.3610  -0.1452 -0.0605 141 ASP   B N   
1278 C  CA  . ASP   B 132 ? 0.7934 0.5754 0.4179 0.3855  -0.1721 -0.0727 141 ASP   B CA  
1279 C  C   . ASP   B 132 ? 0.8259 0.6037 0.4454 0.4079  -0.1859 -0.0845 141 ASP   B C   
1280 O  O   . ASP   B 132 ? 0.8197 0.6142 0.4574 0.4013  -0.1734 -0.0822 141 ASP   B O   
1281 C  CB  . ASP   B 132 ? 0.7985 0.5479 0.4255 0.3650  -0.1905 -0.0782 141 ASP   B CB  
1282 C  CG  . ASP   B 132 ? 0.8026 0.5389 0.4576 0.3358  -0.1976 -0.0827 141 ASP   B CG  
1283 O  OD1 . ASP   B 132 ? 0.7657 0.5153 0.4370 0.3343  -0.1924 -0.0851 141 ASP   B OD1 
1284 O  OD2 . ASP   B 132 ? 0.8420 0.5556 0.5024 0.3152  -0.2086 -0.0830 141 ASP   B OD2 
1285 N  N   . LYS   B 133 ? 0.8572 0.6117 0.4511 0.4352  -0.2125 -0.0980 142 LYS   B N   
1286 C  CA  . LYS   B 133 ? 0.8828 0.6316 0.4680 0.4603  -0.2288 -0.1111 142 LYS   B CA  
1287 C  C   . LYS   B 133 ? 0.8798 0.6205 0.4955 0.4357  -0.2359 -0.1182 142 LYS   B C   
1288 O  O   . LYS   B 133 ? 0.8770 0.6220 0.4923 0.4523  -0.2426 -0.1265 142 LYS   B O   
1289 C  CB  . LYS   B 133 ? 0.9496 0.6701 0.4994 0.4945  -0.2597 -0.1261 142 LYS   B CB  
1290 C  CG  . LYS   B 133 ? 1.0421 0.7680 0.5632 0.5147  -0.2551 -0.1194 142 LYS   B CG  
1291 C  CD  . LYS   B 133 ? 1.1397 0.8417 0.6199 0.5570  -0.2843 -0.1347 142 LYS   B CD  
1292 C  CE  . LYS   B 133 ? 1.2010 0.9164 0.6555 0.5771  -0.2757 -0.1262 142 LYS   B CE  
1293 N  NZ  . LYS   B 133 ? 1.2549 0.9413 0.6679 0.6156  -0.3064 -0.1419 142 LYS   B NZ  
1294 N  N   . CYS   B 134 ? 0.8729 0.6064 0.5157 0.3970  -0.2327 -0.1139 143 CYS   B N   
1295 C  CA  . CYS   B 134 ? 0.8668 0.6002 0.5423 0.3716  -0.2361 -0.1179 143 CYS   B CA  
1296 C  C   . CYS   B 134 ? 0.8336 0.5993 0.5336 0.3537  -0.2062 -0.1066 143 CYS   B C   
1297 O  O   . CYS   B 134 ? 0.8284 0.5991 0.5554 0.3348  -0.2068 -0.1094 143 CYS   B O   
1298 C  CB  . CYS   B 134 ? 0.8950 0.6030 0.5866 0.3414  -0.2517 -0.1193 143 CYS   B CB  
1299 S  SG  . CYS   B 134 ? 1.0059 0.6678 0.6758 0.3590  -0.2954 -0.1369 143 CYS   B SG  
1300 N  N   . GLY   B 135 ? 0.8128 0.5999 0.5043 0.3594  -0.1817 -0.0941 144 GLY   B N   
1301 C  CA  . GLY   B 135 ? 0.7911 0.6043 0.5036 0.3427  -0.1549 -0.0835 144 GLY   B CA  
1302 C  C   . GLY   B 135 ? 0.7720 0.5878 0.5049 0.3073  -0.1418 -0.0746 144 GLY   B C   
1303 O  O   . GLY   B 135 ? 0.7559 0.5903 0.5064 0.2918  -0.1216 -0.0673 144 GLY   B O   
1304 N  N   . ARG   B 136 ? 0.7691 0.5648 0.4978 0.2958  -0.1540 -0.0753 145 ARG   B N   
1305 C  CA  . ARG   B 136 ? 0.7610 0.5575 0.5050 0.2646  -0.1432 -0.0666 145 ARG   B CA  
1306 C  C   . ARG   B 136 ? 0.7384 0.5484 0.4715 0.2658  -0.1236 -0.0552 145 ARG   B C   
1307 O  O   . ARG   B 136 ? 0.7463 0.5550 0.4560 0.2883  -0.1266 -0.0543 145 ARG   B O   
1308 C  CB  . ARG   B 136 ? 0.8016 0.5694 0.5444 0.2524  -0.1647 -0.0706 145 ARG   B CB  
1309 C  CG  . ARG   B 136 ? 0.8527 0.6116 0.6178 0.2396  -0.1812 -0.0785 145 ARG   B CG  
1310 C  CD  . ARG   B 136 ? 0.9187 0.6455 0.6818 0.2285  -0.2053 -0.0814 145 ARG   B CD  
1311 N  NE  . ARG   B 136 ? 0.9924 0.6930 0.7262 0.2573  -0.2296 -0.0924 145 ARG   B NE  
1312 C  CZ  . ARG   B 136 ? 1.0495 0.7226 0.7619 0.2615  -0.2439 -0.0926 145 ARG   B CZ  
1313 N  NH1 . ARG   B 136 ? 1.0546 0.7226 0.7717 0.2378  -0.2356 -0.0816 145 ARG   B NH1 
1314 N  NH2 . ARG   B 136 ? 1.0584 0.7083 0.7419 0.2916  -0.2669 -0.1042 145 ARG   B NH2 
1315 N  N   . VAL   B 137 ? 0.7072 0.5322 0.4574 0.2429  -0.1039 -0.0466 146 VAL   B N   
1316 C  CA  . VAL   B 137 ? 0.6882 0.5269 0.4323 0.2409  -0.0859 -0.0360 146 VAL   B CA  
1317 C  C   . VAL   B 137 ? 0.6825 0.5074 0.4149 0.2337  -0.0918 -0.0330 146 VAL   B C   
1318 O  O   . VAL   B 137 ? 0.6855 0.5027 0.4283 0.2107  -0.0918 -0.0312 146 VAL   B O   
1319 C  CB  . VAL   B 137 ? 0.6746 0.5316 0.4388 0.2218  -0.0650 -0.0299 146 VAL   B CB  
1320 C  CG1 . VAL   B 137 ? 0.6765 0.5467 0.4357 0.2199  -0.0489 -0.0197 146 VAL   B CG1 
1321 C  CG2 . VAL   B 137 ? 0.6703 0.5380 0.4438 0.2310  -0.0609 -0.0335 146 VAL   B CG2 
1322 N  N   . ILE   B 138 ? 0.6714 0.4943 0.3813 0.2548  -0.0971 -0.0322 147 ILE   B N   
1323 C  CA  . ILE   B 138 ? 0.6616 0.4713 0.3567 0.2525  -0.1038 -0.0299 147 ILE   B CA  
1324 C  C   . ILE   B 138 ? 0.6386 0.4670 0.3365 0.2417  -0.0849 -0.0191 147 ILE   B C   
1325 O  O   . ILE   B 138 ? 0.6463 0.4660 0.3336 0.2374  -0.0885 -0.0166 147 ILE   B O   
1326 C  CB  . ILE   B 138 ? 0.6758 0.4730 0.3429 0.2836  -0.1219 -0.0361 147 ILE   B CB  
1327 C  CG1 . ILE   B 138 ? 0.6793 0.5021 0.3375 0.3098  -0.1118 -0.0324 147 ILE   B CG1 
1328 C  CG2 . ILE   B 138 ? 0.6887 0.4583 0.3520 0.2899  -0.1463 -0.0485 147 ILE   B CG2 
1329 C  CD1 . ILE   B 138 ? 0.7082 0.5268 0.3366 0.3418  -0.1247 -0.0355 147 ILE   B CD1 
1330 N  N   . GLY   B 139 ? 0.6075 0.4593 0.3195 0.2367  -0.0664 -0.0131 148 GLY   B N   
1331 C  CA  . GLY   B 139 ? 0.5986 0.4672 0.3157 0.2255  -0.0504 -0.0038 148 GLY   B CA  
1332 C  C   . GLY   B 139 ? 0.5877 0.4793 0.3170 0.2268  -0.0339 0.0026  148 GLY   B C   
1333 O  O   . GLY   B 139 ? 0.5960 0.4909 0.3285 0.2375  -0.0337 0.0004  148 GLY   B O   
1334 N  N   . LEU   B 140 ? 0.5688 0.4749 0.3048 0.2160  -0.0213 0.0107  149 LEU   B N   
1335 C  CA  . LEU   B 140 ? 0.5537 0.4787 0.3021 0.2149  -0.0068 0.0184  149 LEU   B CA  
1336 C  C   . LEU   B 140 ? 0.5521 0.4973 0.2961 0.2246  -0.0016 0.0289  149 LEU   B C   
1337 O  O   . LEU   B 140 ? 0.5537 0.5000 0.2899 0.2233  -0.0055 0.0300  149 LEU   B O   
1338 C  CB  . LEU   B 140 ? 0.5404 0.4650 0.3053 0.1908  0.0034  0.0187  149 LEU   B CB  
1339 C  CG  . LEU   B 140 ? 0.5536 0.4653 0.3265 0.1793  0.0015  0.0102  149 LEU   B CG  
1340 C  CD1 . LEU   B 140 ? 0.5543 0.4692 0.3403 0.1603  0.0126  0.0111  149 LEU   B CD1 
1341 C  CD2 . LEU   B 140 ? 0.5552 0.4657 0.3301 0.1925  -0.0016 0.0061  149 LEU   B CD2 
1342 N  N   . TYR   B 141 ? 0.5410 0.5037 0.2907 0.2342  0.0073  0.0375  150 TYR   B N   
1343 C  CA  . TYR   B 141 ? 0.5351 0.5235 0.2851 0.2445  0.0141  0.0507  150 TYR   B CA  
1344 C  C   . TYR   B 141 ? 0.5296 0.5289 0.2996 0.2231  0.0257  0.0595  150 TYR   B C   
1345 O  O   . TYR   B 141 ? 0.5245 0.5156 0.3063 0.2104  0.0312  0.0582  150 TYR   B O   
1346 C  CB  . TYR   B 141 ? 0.5324 0.5324 0.2778 0.2674  0.0172  0.0564  150 TYR   B CB  
1347 C  CG  . TYR   B 141 ? 0.5311 0.5623 0.2824 0.2763  0.0285  0.0743  150 TYR   B CG  
1348 C  CD1 . TYR   B 141 ? 0.5317 0.5725 0.3009 0.2660  0.0410  0.0859  150 TYR   B CD1 
1349 C  CD2 . TYR   B 141 ? 0.5425 0.5944 0.2814 0.2965  0.0262  0.0804  150 TYR   B CD2 
1350 C  CE1 . TYR   B 141 ? 0.5352 0.6060 0.3129 0.2719  0.0514  0.1050  150 TYR   B CE1 
1351 C  CE2 . TYR   B 141 ? 0.5416 0.6277 0.2885 0.3046  0.0375  0.0991  150 TYR   B CE2 
1352 C  CZ  . TYR   B 141 ? 0.5456 0.6416 0.3135 0.2909  0.0504  0.1123  150 TYR   B CZ  
1353 O  OH  . TYR   B 141 ? 0.5513 0.6827 0.3295 0.2975  0.0617  0.1335  150 TYR   B OH  
1354 N  N   . GLY   B 142 ? 0.5294 0.5474 0.3029 0.2205  0.0282  0.0680  151 GLY   B N   
1355 C  CA  . GLY   B 142 ? 0.5296 0.5575 0.3232 0.2001  0.0366  0.0762  151 GLY   B CA  
1356 C  C   . GLY   B 142 ? 0.5315 0.5667 0.3275 0.1890  0.0339  0.0766  151 GLY   B C   
1357 O  O   . GLY   B 142 ? 0.5301 0.5744 0.3432 0.1728  0.0386  0.0830  151 GLY   B O   
1358 N  N   . ASN   B 143 ? 0.5327 0.5617 0.3111 0.1975  0.0248  0.0692  152 ASN   B N   
1359 C  CA  . ASN   B 143 ? 0.5353 0.5712 0.3131 0.1897  0.0215  0.0692  152 ASN   B CA  
1360 C  C   . ASN   B 143 ? 0.5524 0.6030 0.3142 0.2112  0.0154  0.0716  152 ASN   B C   
1361 O  O   . ASN   B 143 ? 0.5667 0.5990 0.3076 0.2233  0.0056  0.0625  152 ASN   B O   
1362 C  CB  . ASN   B 143 ? 0.5505 0.5599 0.3219 0.1740  0.0161  0.0569  152 ASN   B CB  
1363 C  CG  . ASN   B 143 ? 0.5509 0.5678 0.3244 0.1633  0.0141  0.0575  152 ASN   B CG  
1364 O  OD1 . ASN   B 143 ? 0.5389 0.5802 0.3266 0.1601  0.0179  0.0666  152 ASN   B OD1 
1365 N  ND2 . ASN   B 143 ? 0.5521 0.5492 0.3124 0.1572  0.0079  0.0485  152 ASN   B ND2 
1366 N  N   . GLY   B 144 ? 0.5466 0.6300 0.3189 0.2152  0.0201  0.0837  153 GLY   B N   
1367 C  CA  . GLY   B 144 ? 0.5681 0.6715 0.3260 0.2378  0.0152  0.0871  153 GLY   B CA  
1368 C  C   . GLY   B 144 ? 0.5751 0.7162 0.3492 0.2349  0.0198  0.0994  153 GLY   B C   
1369 O  O   . GLY   B 144 ? 0.5678 0.7097 0.3568 0.2133  0.0202  0.0992  153 GLY   B O   
1370 N  N   . VAL   B 145 ? 0.5878 0.7624 0.3594 0.2577  0.0228  0.1105  154 VAL   B N   
1371 C  CA  . VAL   B 145 ? 0.5971 0.8136 0.3836 0.2586  0.0261  0.1230  154 VAL   B CA  
1372 C  C   . VAL   B 145 ? 0.6044 0.8656 0.4079 0.2705  0.0381  0.1438  154 VAL   B C   
1373 O  O   . VAL   B 145 ? 0.6106 0.8708 0.4047 0.2873  0.0423  0.1472  154 VAL   B O   
1374 C  CB  . VAL   B 145 ? 0.6121 0.8274 0.3719 0.2786  0.0146  0.1138  154 VAL   B CB  
1375 C  CG1 . VAL   B 145 ? 0.6098 0.8438 0.3485 0.3150  0.0131  0.1174  154 VAL   B CG1 
1376 C  CG2 . VAL   B 145 ? 0.6120 0.8515 0.3851 0.2681  0.0129  0.1174  154 VAL   B CG2 
1377 N  N   . VAL   B 146 ? 0.6008 0.9017 0.4309 0.2601  0.0437  0.1587  155 VAL   B N   
1378 C  CA  . VAL   B 146 ? 0.6005 0.9495 0.4515 0.2679  0.0560  0.1821  155 VAL   B CA  
1379 C  C   . VAL   B 146 ? 0.6173 1.0071 0.4561 0.2972  0.0547  0.1879  155 VAL   B C   
1380 O  O   . VAL   B 146 ? 0.6132 1.0120 0.4517 0.2948  0.0474  0.1825  155 VAL   B O   
1381 C  CB  . VAL   B 146 ? 0.5884 0.9565 0.4806 0.2358  0.0619  0.1966  155 VAL   B CB  
1382 C  CG1 . VAL   B 146 ? 0.5725 0.9921 0.4893 0.2417  0.0753  0.2243  155 VAL   B CG1 
1383 C  CG2 . VAL   B 146 ? 0.6078 0.9313 0.5075 0.2094  0.0612  0.1882  155 VAL   B CG2 
1384 N  N   . ILE   B 147 ? 0.6377 1.0509 0.4631 0.3276  0.0608  0.1973  156 ILE   B N   
1385 C  CA  . ILE   B 147 ? 0.6611 1.1144 0.4707 0.3611  0.0596  0.2022  156 ILE   B CA  
1386 C  C   . ILE   B 147 ? 0.6635 1.1858 0.5062 0.3618  0.0740  0.2310  156 ILE   B C   
1387 O  O   . ILE   B 147 ? 0.6542 1.1875 0.5309 0.3358  0.0841  0.2471  156 ILE   B O   
1388 C  CB  . ILE   B 147 ? 0.6898 1.1245 0.4584 0.3987  0.0544  0.1919  156 ILE   B CB  
1389 C  CG1 . ILE   B 147 ? 0.6974 1.1375 0.4713 0.4045  0.0665  0.2047  156 ILE   B CG1 
1390 C  CG2 . ILE   B 147 ? 0.7253 1.0960 0.4649 0.3958  0.0378  0.1646  156 ILE   B CG2 
1391 C  CD1 . ILE   B 147 ? 0.7262 1.1532 0.4607 0.4443  0.0610  0.1955  156 ILE   B CD1 
1392 N  N   . LYS   B 148 ? 0.6725 1.2413 0.5063 0.3910  0.0743  0.2379  157 LYS   B N   
1393 C  CA  . LYS   B 148 ? 0.6633 1.3057 0.5285 0.3949  0.0877  0.2661  157 LYS   B CA  
1394 C  C   . LYS   B 148 ? 0.6574 1.3270 0.5494 0.3871  0.1054  0.2927  157 LYS   B C   
1395 O  O   . LYS   B 148 ? 0.6302 1.3386 0.5655 0.3624  0.1146  0.3150  157 LYS   B O   
1396 C  CB  . LYS   B 148 ? 0.7003 1.3837 0.5388 0.4400  0.0859  0.2672  157 LYS   B CB  
1397 C  CG  . LYS   B 148 ? 0.7997 1.4602 0.6141 0.4470  0.0683  0.2439  157 LYS   B CG  
1398 C  CD  . LYS   B 148 ? 0.8777 1.5805 0.6664 0.4920  0.0653  0.2449  157 LYS   B CD  
1399 C  CE  . LYS   B 148 ? 0.9028 1.6824 0.7271 0.4901  0.0742  0.2670  157 LYS   B CE  
1400 N  NZ  . LYS   B 148 ? 0.9333 1.7046 0.7761 0.4613  0.0642  0.2579  157 LYS   B NZ  
1401 N  N   . ASN   B 149 ? 0.6789 1.3266 0.5463 0.4068  0.1092  0.2906  158 ASN   B N   
1402 C  CA  . ASN   B 149 ? 0.6783 1.3493 0.5666 0.4026  0.1261  0.3162  158 ASN   B CA  
1403 C  C   . ASN   B 149 ? 0.6674 1.2971 0.5807 0.3610  0.1277  0.3167  158 ASN   B C   
1404 O  O   . ASN   B 149 ? 0.6677 1.3034 0.5918 0.3585  0.1397  0.3345  158 ASN   B O   
1405 C  CB  . ASN   B 149 ? 0.7321 1.4048 0.5834 0.4454  0.1304  0.3165  158 ASN   B CB  
1406 C  CG  . ASN   B 149 ? 0.8348 1.4478 0.6390 0.4659  0.1136  0.2838  158 ASN   B CG  
1407 O  OD1 . ASN   B 149 ? 0.8641 1.4606 0.6467 0.4758  0.0989  0.2635  158 ASN   B OD1 
1408 N  ND2 . ASN   B 149 ? 0.8625 1.4431 0.6500 0.4735  0.1147  0.2791  158 ASN   B ND2 
1409 N  N   . GLY   B 150 ? 0.6559 1.2462 0.5773 0.3307  0.1158  0.2984  159 GLY   B N   
1410 C  CA  . GLY   B 150 ? 0.6426 1.1920 0.5849 0.2931  0.1150  0.2958  159 GLY   B CA  
1411 C  C   . GLY   B 150 ? 0.6497 1.1383 0.5631 0.2965  0.1096  0.2750  159 GLY   B C   
1412 O  O   . GLY   B 150 ? 0.6568 1.1062 0.5817 0.2681  0.1067  0.2677  159 GLY   B O   
1413 N  N   . SER   B 151 ? 0.6456 1.1272 0.5215 0.3326  0.1073  0.2652  160 SER   B N   
1414 C  CA  . SER   B 151 ? 0.6508 1.0805 0.4971 0.3421  0.1007  0.2451  160 SER   B CA  
1415 C  C   . SER   B 151 ? 0.6325 1.0105 0.4655 0.3262  0.0849  0.2166  160 SER   B C   
1416 O  O   . SER   B 151 ? 0.6264 1.0099 0.4642 0.3168  0.0782  0.2107  160 SER   B O   
1417 C  CB  . SER   B 151 ? 0.6868 1.1295 0.4976 0.3872  0.1000  0.2430  160 SER   B CB  
1418 O  OG  . SER   B 151 ? 0.7578 1.1507 0.5364 0.3999  0.0883  0.2191  160 SER   B OG  
1419 N  N   . TYR   B 152 ? 0.6197 0.9497 0.4362 0.3240  0.0793  0.2000  161 TYR   B N   
1420 C  CA  . TYR   B 152 ? 0.6105 0.8927 0.4151 0.3092  0.0661  0.1754  161 TYR   B CA  
1421 C  C   . TYR   B 152 ? 0.6089 0.8641 0.3761 0.3363  0.0540  0.1564  161 TYR   B C   
1422 O  O   . TYR   B 152 ? 0.6107 0.8673 0.3621 0.3605  0.0555  0.1579  161 TYR   B O   
1423 C  CB  . TYR   B 152 ? 0.6040 0.8520 0.4233 0.2815  0.0685  0.1710  161 TYR   B CB  
1424 C  CG  . TYR   B 152 ? 0.6045 0.8182 0.4264 0.2556  0.0596  0.1539  161 TYR   B CG  
1425 C  CD1 . TYR   B 152 ? 0.5970 0.8229 0.4401 0.2330  0.0594  0.1580  161 TYR   B CD1 
1426 C  CD2 . TYR   B 152 ? 0.6254 0.7963 0.4302 0.2533  0.0516  0.1344  161 TYR   B CD2 
1427 C  CE1 . TYR   B 152 ? 0.6092 0.8046 0.4525 0.2116  0.0516  0.1426  161 TYR   B CE1 
1428 C  CE2 . TYR   B 152 ? 0.6339 0.7768 0.4409 0.2306  0.0451  0.1208  161 TYR   B CE2 
1429 C  CZ  . TYR   B 152 ? 0.6310 0.7857 0.4559 0.2107  0.0455  0.1247  161 TYR   B CZ  
1430 O  OH  . TYR   B 152 ? 0.6446 0.7726 0.4699 0.1902  0.0397  0.1117  161 TYR   B OH  
1431 N  N   . VAL   B 153 ? 0.6035 0.8317 0.3567 0.3312  0.0410  0.1386  162 VAL   B N   
1432 C  CA  . VAL   B 153 ? 0.6101 0.8043 0.3304 0.3503  0.0262  0.1193  162 VAL   B CA  
1433 C  C   . VAL   B 153 ? 0.6029 0.7533 0.3257 0.3225  0.0188  0.1035  162 VAL   B C   
1434 O  O   . VAL   B 153 ? 0.6013 0.7489 0.3302 0.3056  0.0160  0.1006  162 VAL   B O   
1435 C  CB  . VAL   B 153 ? 0.6183 0.8269 0.3149 0.3775  0.0167  0.1158  162 VAL   B CB  
1436 C  CG1 . VAL   B 153 ? 0.6437 0.8074 0.3080 0.3906  -0.0020 0.0945  162 VAL   B CG1 
1437 C  CG2 . VAL   B 153 ? 0.6205 0.8740 0.3111 0.4101  0.0244  0.1310  162 VAL   B CG2 
1438 N  N   . SER   B 154 ? 0.5962 0.7165 0.3167 0.3168  0.0171  0.0950  163 SER   B N   
1439 C  CA  . SER   B 154 ? 0.5918 0.6755 0.3164 0.2913  0.0120  0.0820  163 SER   B CA  
1440 C  C   . SER   B 154 ? 0.5994 0.6504 0.2990 0.2999  -0.0044 0.0655  163 SER   B C   
1441 O  O   . SER   B 154 ? 0.6026 0.6468 0.2818 0.3250  -0.0131 0.0603  163 SER   B O   
1442 C  CB  . SER   B 154 ? 0.5874 0.6577 0.3246 0.2798  0.0185  0.0815  163 SER   B CB  
1443 O  OG  . SER   B 154 ? 0.5900 0.6254 0.3256 0.2634  0.0119  0.0673  163 SER   B OG  
1444 N  N   . ALA   B 155 ? 0.5952 0.6233 0.2966 0.2784  -0.0091 0.0574  164 ALA   B N   
1445 C  CA  . ALA   B 155 ? 0.6108 0.6044 0.2917 0.2815  -0.0245 0.0437  164 ALA   B CA  
1446 C  C   . ALA   B 155 ? 0.6134 0.5822 0.2965 0.2767  -0.0276 0.0356  164 ALA   B C   
1447 O  O   . ALA   B 155 ? 0.6017 0.5780 0.3026 0.2669  -0.0169 0.0396  164 ALA   B O   
1448 C  CB  . ALA   B 155 ? 0.6220 0.6023 0.3052 0.2594  -0.0265 0.0404  164 ALA   B CB  
1449 N  N   . ILE   B 156 ? 0.6263 0.5655 0.2917 0.2844  -0.0434 0.0244  165 ILE   B N   
1450 C  CA  . ILE   B 156 ? 0.6342 0.5503 0.3044 0.2768  -0.0484 0.0162  165 ILE   B CA  
1451 C  C   . ILE   B 156 ? 0.6339 0.5323 0.3133 0.2480  -0.0479 0.0135  165 ILE   B C   
1452 O  O   . ILE   B 156 ? 0.6411 0.5169 0.3071 0.2463  -0.0604 0.0084  165 ILE   B O   
1453 C  CB  . ILE   B 156 ? 0.6534 0.5463 0.3016 0.2992  -0.0679 0.0057  165 ILE   B CB  
1454 C  CG1 . ILE   B 156 ? 0.6673 0.5805 0.3009 0.3329  -0.0687 0.0086  165 ILE   B CG1 
1455 C  CG2 . ILE   B 156 ? 0.6570 0.5280 0.3149 0.2879  -0.0740 -0.0027 165 ILE   B CG2 
1456 C  CD1 . ILE   B 156 ? 0.6872 0.5766 0.2949 0.3596  -0.0905 -0.0035 165 ILE   B CD1 
1457 N  N   . THR   B 157 ? 0.6157 0.5250 0.3163 0.2268  -0.0334 0.0179  166 THR   B N   
1458 C  CA  . THR   B 157 ? 0.6111 0.5088 0.3195 0.2018  -0.0306 0.0163  166 THR   B CA  
1459 C  C   . THR   B 157 ? 0.6137 0.4919 0.3290 0.1899  -0.0346 0.0098  166 THR   B C   
1460 O  O   . THR   B 157 ? 0.6065 0.4908 0.3361 0.1855  -0.0274 0.0090  166 THR   B O   
1461 C  CB  . THR   B 157 ? 0.6150 0.5320 0.3403 0.1869  -0.0155 0.0226  166 THR   B CB  
1462 O  OG1 . THR   B 157 ? 0.6237 0.5620 0.3466 0.1959  -0.0124 0.0299  166 THR   B OG1 
1463 C  CG2 . THR   B 157 ? 0.6191 0.5262 0.3486 0.1651  -0.0128 0.0206  166 THR   B CG2 
1464 N  N   . GLN   B 158 ? 0.6244 0.4803 0.3310 0.1832  -0.0456 0.0062  167 GLN   B N   
1465 C  CA  . GLN   B 158 ? 0.6295 0.4698 0.3456 0.1697  -0.0499 0.0020  167 GLN   B CA  
1466 C  C   . GLN   B 158 ? 0.6459 0.4811 0.3669 0.1469  -0.0445 0.0053  167 GLN   B C   
1467 O  O   . GLN   B 158 ? 0.6481 0.4791 0.3570 0.1450  -0.0457 0.0085  167 GLN   B O   
1468 C  CB  . GLN   B 158 ? 0.6443 0.4605 0.3476 0.1816  -0.0700 -0.0040 167 GLN   B CB  
1469 C  CG  . GLN   B 158 ? 0.6540 0.4556 0.3706 0.1681  -0.0773 -0.0079 167 GLN   B CG  
1470 C  CD  . GLN   B 158 ? 0.6490 0.4662 0.3845 0.1670  -0.0690 -0.0105 167 GLN   B CD  
1471 O  OE1 . GLN   B 158 ? 0.6403 0.4757 0.3894 0.1564  -0.0525 -0.0071 167 GLN   B OE1 
1472 N  NE2 . GLN   B 158 ? 0.6394 0.4480 0.3755 0.1784  -0.0817 -0.0175 167 GLN   B NE2 
1473 N  N   . GLY   B 159 ? 0.6548 0.4926 0.3926 0.1317  -0.0381 0.0048  168 GLY   B N   
1474 C  CA  . GLY   B 159 ? 0.6878 0.5238 0.4302 0.1120  -0.0320 0.0086  168 GLY   B CA  
1475 C  C   . GLY   B 159 ? 0.7422 0.5572 0.4826 0.1036  -0.0444 0.0099  168 GLY   B C   
1476 O  O   . GLY   B 159 ? 0.7553 0.5534 0.4891 0.1133  -0.0601 0.0064  168 GLY   B O   
1477 N  N   . LYS   B 160 ? 0.7722 0.5874 0.5177 0.0857  -0.0381 0.0155  169 LYS   B N   
1478 C  CA  . LYS   B 160 ? 0.8138 0.6106 0.5607 0.0738  -0.0485 0.0202  169 LYS   B CA  
1479 C  C   . LYS   B 160 ? 0.8385 0.6490 0.6096 0.0589  -0.0414 0.0223  169 LYS   B C   
1480 O  O   . LYS   B 160 ? 0.8294 0.6615 0.6093 0.0532  -0.0252 0.0235  169 LYS   B O   
1481 C  CB  . LYS   B 160 ? 0.8469 0.6337 0.5782 0.0658  -0.0472 0.0281  169 LYS   B CB  
1482 C  CG  . LYS   B 160 ? 0.9220 0.6830 0.6501 0.0554  -0.0611 0.0347  169 LYS   B CG  
1483 C  CD  . LYS   B 160 ? 0.9970 0.7520 0.7119 0.0453  -0.0559 0.0448  169 LYS   B CD  
1484 C  CE  . LYS   B 160 ? 1.0569 0.7832 0.7677 0.0342  -0.0703 0.0536  169 LYS   B CE  
1485 N  NZ  . LYS   B 160 ? 1.0978 0.8167 0.7918 0.0269  -0.0652 0.0642  169 LYS   B NZ  
1486 N  N   . ARG   B 161 ? 0.8691 0.6680 0.6514 0.0538  -0.0545 0.0222  170 ARG   B N   
1487 C  CA  . ARG   B 161 ? 0.8914 0.7061 0.6996 0.0391  -0.0493 0.0253  170 ARG   B CA  
1488 C  C   . ARG   B 161 ? 0.9333 0.7429 0.7445 0.0193  -0.0481 0.0385  170 ARG   B C   
1489 O  O   . ARG   B 161 ? 0.9499 0.7322 0.7503 0.0161  -0.0630 0.0428  170 ARG   B O   
1490 C  CB  . ARG   B 161 ? 0.8993 0.7061 0.7209 0.0433  -0.0656 0.0185  170 ARG   B CB  
1491 C  CG  . ARG   B 161 ? 0.9032 0.7359 0.7532 0.0349  -0.0577 0.0179  170 ARG   B CG  
1492 C  CD  . ARG   B 161 ? 0.9309 0.7553 0.7970 0.0349  -0.0763 0.0124  170 ARG   B CD  
1493 N  NE  . ARG   B 161 ? 0.9418 0.7941 0.8378 0.0231  -0.0684 0.0146  170 ARG   B NE  
1494 C  CZ  . ARG   B 161 ? 0.9503 0.8195 0.8588 0.0331  -0.0668 0.0054  170 ARG   B CZ  
1495 N  NH1 . ARG   B 161 ? 0.9385 0.7984 0.8324 0.0547  -0.0727 -0.0057 170 ARG   B NH1 
1496 N  NH2 . ARG   B 161 ? 0.9355 0.8325 0.8708 0.0227  -0.0590 0.0079  170 ARG   B NH2 
1497 N  N   . GLU   B 162 ? 0.9498 0.7847 0.7733 0.0075  -0.0306 0.0454  171 GLU   B N   
1498 C  CA  . GLU   B 162 ? 0.9839 0.8193 0.8101 -0.0106 -0.0263 0.0603  171 GLU   B CA  
1499 C  C   . GLU   B 162 ? 0.9989 0.8390 0.8529 -0.0277 -0.0331 0.0684  171 GLU   B C   
1500 O  O   . GLU   B 162 ? 0.9888 0.8501 0.8652 -0.0277 -0.0303 0.0634  171 GLU   B O   
1501 C  CB  . GLU   B 162 ? 1.0155 0.8774 0.8384 -0.0126 -0.0042 0.0645  171 GLU   B CB  
1502 C  CG  . GLU   B 162 ? 1.1132 0.9656 0.9081 -0.0019 -0.0003 0.0614  171 GLU   B CG  
1503 C  CD  . GLU   B 162 ? 1.2370 1.0648 1.0126 -0.0071 -0.0082 0.0711  171 GLU   B CD  
1504 O  OE1 . GLU   B 162 ? 1.2534 1.0880 1.0281 -0.0189 0.0005  0.0839  171 GLU   B OE1 
1505 O  OE2 . GLU   B 162 ? 1.2851 1.0871 1.0451 0.0021  -0.0229 0.0664  171 GLU   B OE2 
1506 N  N   . VAL   B 167 ? 1.0196 0.8404 0.8728 -0.0427 -0.0423 0.0818  172 VAL   B N   
1507 C  CA  . VAL   B 167 ? 1.0282 0.8503 0.9094 -0.0629 -0.0512 0.0930  172 VAL   B CA  
1508 C  C   . VAL   B 167 ? 1.0340 0.8458 0.9314 -0.0584 -0.0710 0.0809  172 VAL   B C   
1509 O  O   . VAL   B 167 ? 1.0449 0.8284 0.9475 -0.0669 -0.0928 0.0838  172 VAL   B O   
1510 C  CB  . VAL   B 167 ? 1.0220 0.8864 0.9277 -0.0777 -0.0304 0.1060  172 VAL   B CB  
1511 C  CG1 . VAL   B 167 ? 1.0180 0.8892 0.9586 -0.0991 -0.0403 0.1177  172 VAL   B CG1 
1512 C  CG2 . VAL   B 167 ? 1.0332 0.9035 0.9208 -0.0824 -0.0141 0.1198  172 VAL   B CG2 
1513 S  S   . DMS   C .   ? 1.0636 0.8996 0.8393 0.0675  0.0178  -0.0537 201 DMS   B S   
1514 O  O   . DMS   C .   ? 1.0579 0.9115 0.8299 0.0726  0.0295  -0.0501 201 DMS   B O   
1515 C  C1  . DMS   C .   ? 1.0725 0.8872 0.8485 0.0746  0.0156  -0.0606 201 DMS   B C1  
1516 C  C2  . DMS   C .   ? 1.0525 0.8917 0.8519 0.0577  0.0157  -0.0379 201 DMS   B C2  
1517 N  N1  . A1B8I D .   ? 0.5381 0.7360 0.3761 0.2571  0.0818  0.1760  202 A1B8I B N1  
1518 N  N3  . A1B8I D .   ? 0.5262 0.5440 0.3480 0.0988  0.0193  0.0545  202 A1B8I B N3  
1519 C  C4  . A1B8I D .   ? 0.5268 0.6873 0.4130 0.1668  0.0649  0.1536  202 A1B8I B C4  
1520 C  C5  . A1B8I D .   ? 0.5441 0.6660 0.4160 0.1608  0.0590  0.1338  202 A1B8I B C5  
1521 C  C6  . A1B8I D .   ? 0.5441 0.6476 0.4223 0.1380  0.0526  0.1225  202 A1B8I B C6  
1522 C  C7  . A1B8I D .   ? 0.5282 0.5876 0.3864 0.1217  0.0402  0.0921  202 A1B8I B C7  
1523 C  C8  . A1B8I D .   ? 0.5196 0.5748 0.3956 0.1017  0.0394  0.0934  202 A1B8I B C8  
1524 C  C10 . A1B8I D .   ? 0.5206 0.5514 0.3719 0.0951  0.0285  0.0699  202 A1B8I B C10 
1525 C  C13 . A1B8I D .   ? 0.5268 0.5451 0.3420 0.1141  0.0226  0.0581  202 A1B8I B C13 
1526 C  C15 . A1B8I D .   ? 0.5623 0.6657 0.4165 0.1757  0.0592  0.1260  202 A1B8I B C15 
1527 C  C1  . A1B8I D .   ? 0.5410 0.7215 0.3889 0.2338  0.0773  0.1674  202 A1B8I B C1  
1528 C  C2  . A1B8I D .   ? 0.5419 0.7015 0.3999 0.2069  0.0712  0.1561  202 A1B8I B C2  
1529 C  C3  . A1B8I D .   ? 0.5242 0.7048 0.4038 0.1897  0.0719  0.1656  202 A1B8I B C3  
1530 O  O1  . A1B8I D .   ? 0.5461 0.6616 0.4450 0.1217  0.0523  0.1305  202 A1B8I B O1  
1531 N  N2  . A1B8I D .   ? 0.5404 0.6166 0.4001 0.1377  0.0464  0.1043  202 A1B8I B N2  
1532 C  C9  . A1B8I D .   ? 0.5186 0.5581 0.3905 0.0889  0.0329  0.0810  202 A1B8I B C9  
1533 C  C11 . A1B8I D .   ? 0.5249 0.5582 0.3602 0.1128  0.0289  0.0697  202 A1B8I B C11 
1534 C  C12 . A1B8I D .   ? 0.5264 0.5745 0.3645 0.1271  0.0338  0.0800  202 A1B8I B C12 
1535 C  C14 . A1B8I D .   ? 0.5231 0.5386 0.3642 0.0858  0.0224  0.0572  202 A1B8I B C14 
1536 C  C16 . A1B8I D .   ? 0.5645 0.6853 0.4111 0.1989  0.0642  0.1360  202 A1B8I B C16 
1537 CL CL1 . A1B8I D .   ? 0.5870 0.6834 0.4121 0.2174  0.0619  0.1242  202 A1B8I B CL1 
# 
