data_7IAH
# 
_entry.id   7IAH 
# 
_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   7IAH         pdb_00007iah 10.2210/pdb7iah/pdb 
WWPDB D_1001408520 ?            ?                   
# 
_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                        7IAH 
_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 '(2S)-[(2,3-dihydro-1H-isoindol-5-yl)amino](isoquinolin-4-yl)acetonitrile' 300.357   1  ? ?    ? ? 
5 water       nat water                                                                      18.015    67 ? ?    ? ? 
# 
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 '(2S)-[(2,3-dihydro-1H-isoindol-5-yl)amino](isoquinolin-4-yl)acetonitrile' A1B84 
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 
A1B84 non-polymer         . '(2S)-[(2,3-dihydro-1H-isoindol-5-yl)amino](isoquinolin-4-yl)acetonitrile' ? 'C19 H16 N4'     300.357 
ALA   'L-peptide linking' y ALANINE                                                                    ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                   ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                 ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                            ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                   ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                       ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                  ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                            ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                    ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                  ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                      ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                 ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                    ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                     ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                 ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                              ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                    ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                     ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                  ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                 ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                   ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                     ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B84 1  202 203 A1B84 LIG B . 
E 5 HOH   1  101 117 HOH   HOH A . 
E 5 HOH   2  102 131 HOH   HOH A . 
E 5 HOH   3  103 98  HOH   HOH A . 
E 5 HOH   4  104 20  HOH   HOH A . 
E 5 HOH   5  105 54  HOH   HOH A . 
E 5 HOH   6  106 34  HOH   HOH A . 
E 5 HOH   7  107 65  HOH   HOH A . 
E 5 HOH   8  108 50  HOH   HOH A . 
E 5 HOH   9  109 129 HOH   HOH A . 
E 5 HOH   10 110 120 HOH   HOH A . 
E 5 HOH   11 111 40  HOH   HOH A . 
E 5 HOH   12 112 66  HOH   HOH A . 
E 5 HOH   13 113 124 HOH   HOH A . 
E 5 HOH   14 114 29  HOH   HOH A . 
E 5 HOH   15 115 118 HOH   HOH A . 
E 5 HOH   16 116 27  HOH   HOH A . 
E 5 HOH   17 117 123 HOH   HOH A . 
F 5 HOH   1  301 57  HOH   HOH B . 
F 5 HOH   2  302 90  HOH   HOH B . 
F 5 HOH   3  303 11  HOH   HOH B . 
F 5 HOH   4  304 46  HOH   HOH B . 
F 5 HOH   5  305 1   HOH   HOH B . 
F 5 HOH   6  306 14  HOH   HOH B . 
F 5 HOH   7  307 100 HOH   HOH B . 
F 5 HOH   8  308 51  HOH   HOH B . 
F 5 HOH   9  309 115 HOH   HOH B . 
F 5 HOH   10 310 81  HOH   HOH B . 
F 5 HOH   11 311 128 HOH   HOH B . 
F 5 HOH   12 312 125 HOH   HOH B . 
F 5 HOH   13 313 56  HOH   HOH B . 
F 5 HOH   14 314 4   HOH   HOH B . 
F 5 HOH   15 315 58  HOH   HOH B . 
F 5 HOH   16 316 69  HOH   HOH B . 
F 5 HOH   17 317 36  HOH   HOH B . 
F 5 HOH   18 318 10  HOH   HOH B . 
F 5 HOH   19 319 2   HOH   HOH B . 
F 5 HOH   20 320 35  HOH   HOH B . 
F 5 HOH   21 321 9   HOH   HOH B . 
F 5 HOH   22 322 39  HOH   HOH B . 
F 5 HOH   23 323 127 HOH   HOH B . 
F 5 HOH   24 324 64  HOH   HOH B . 
F 5 HOH   25 325 130 HOH   HOH B . 
F 5 HOH   26 326 28  HOH   HOH B . 
F 5 HOH   27 327 5   HOH   HOH B . 
F 5 HOH   28 328 13  HOH   HOH B . 
F 5 HOH   29 329 21  HOH   HOH B . 
F 5 HOH   30 330 89  HOH   HOH B . 
F 5 HOH   31 331 106 HOH   HOH B . 
F 5 HOH   32 332 23  HOH   HOH B . 
F 5 HOH   33 333 26  HOH   HOH B . 
F 5 HOH   34 334 3   HOH   HOH B . 
F 5 HOH   35 335 72  HOH   HOH B . 
F 5 HOH   36 336 102 HOH   HOH B . 
F 5 HOH   37 337 94  HOH   HOH B . 
F 5 HOH   38 338 108 HOH   HOH B . 
F 5 HOH   39 339 116 HOH   HOH B . 
F 5 HOH   40 340 87  HOH   HOH B . 
F 5 HOH   41 341 43  HOH   HOH B . 
F 5 HOH   42 342 68  HOH   HOH B . 
F 5 HOH   43 343 122 HOH   HOH B . 
F 5 HOH   44 344 60  HOH   HOH B . 
F 5 HOH   45 345 44  HOH   HOH B . 
F 5 HOH   46 346 80  HOH   HOH B . 
F 5 HOH   47 347 105 HOH   HOH B . 
F 5 HOH   48 348 67  HOH   HOH B . 
F 5 HOH   49 349 79  HOH   HOH B . 
F 5 HOH   50 350 126 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           7IAH 
_cell.length_a           42.550 
_cell.length_b           42.550 
_cell.length_c           217.210 
_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                         7IAH 
_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          7IAH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.000 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   41.99 
_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                     7IAH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             72.400 
_reflns.d_resolution_high            2.190 
_reflns.number_obs                   11220 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.410 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.900 
_reflns.B_iso_Wilson_estimate        44.630 
_reflns.pdbx_redundancy              24.700 
_reflns.pdbx_Rrim_I_all              0.419 
_reflns.pdbx_Rpim_I_all              0.083 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     277053 
_reflns.pdbx_scaling_rejects         0 
_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 2.190 2.250  ? 21100 ? ? ?     ? ? ? 25.900 ? 0.100  ? 815 ? ? ? ? 99.700 68.471 13.337 0.355 ? 
1 2 9.790 72.400 ? 2470  ? ? 0.085 ? ? ? 13.400 ? 22.300 ? 184 ? ? ? ? 99.700 0.088  0.022  0.999 ? 
# 
_refine.entry_id                                 7IAH 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.1900 
_refine.ls_d_res_low                             42.5500 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    95.5000 
_refine.ls_number_reflns_obs                     10649 
_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                          0.2779 
_refine.ls_R_factor_R_work                       0.2760 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.3136 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  514 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               66.1600 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            2.0259 
_refine.aniso_B[2][2]                            2.0259 
_refine.aniso_B[3][3]                            -4.0519 
_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               0.9330 
_refine.correlation_coeff_Fo_to_Fc_free          0.9070 
_refine.overall_SU_R_Cruickshank_DPI             0.3740 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2690 
_refine.pdbx_overall_SU_R_Blow_DPI               0.4290 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2800 
_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                                110.510 
_refine.B_iso_min                                38.300 
_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                        7IAH 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.490 
_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                       2.1900 
_refine_hist.d_res_low                        42.5500 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             67 
_refine_hist.number_atoms_total               1570 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           68.15 
_refine_hist.pdbx_B_iso_mean_solvent          56.83 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        534  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              268  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1564 ?      ? 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 195  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1083 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1564 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2128 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.780  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    17.600 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.1900 
_refine_ls_shell.d_res_low                        2.2300 
_refine_ls_shell.pdbx_total_number_of_bins_used   26 
_refine_ls_shell.percent_reflns_obs               70.7700 
_refine_ls_shell.number_reflns_R_work             404 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.6757 
_refine_ls_shell.R_factor_R_free                  0.6530 
_refine_ls_shell.percent_reflns_R_free            5.1600 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                426 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAH 
_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-0029845-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAH 
_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 7IAH A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAH B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7IAH SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAH MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAH MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAH 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)' 4270 ? 
1 MORE         -25  ? 
1 'SSA (A^2)'  9750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? 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 
AA4 1 2 ? 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 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 2 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 3 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 4 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 5 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 6 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 
AA4 1 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA4 2 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
# 
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 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 2 3 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 3 4 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 4 5 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 5 6 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA4 1 2 N SER B 51  ? N SER B 60  O GLY B 54  ? O GLY B 63  
# 
_pdbx_entry_details.entry_id                   7IAH 
_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 ASP A 64  ? ? 73.86   40.56   
2 1 LEU B 30  ? ? -90.12  -159.16 
3 1 ASP B 71  ? ? -161.04 118.62  
4 1 CYS B 80  ? ? 76.14   -25.24  
5 1 LEU B 92  ? ? -141.78 -49.30  
6 1 ALA B 127 ? ? -91.83  57.13   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 322 ? F HOH . 
2 1 B HOH 345 ? F HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.5142 -1.4199 -19.3292 0.2860 0.3133 -0.3683 0.1622 0.0771 0.0844 3.4220 3.7837 3.0694 -2.0948 
0.3946 0.4463  0.1817 -0.2531 0.0714 0.3396 0.1776 -0.4208 -0.5532 -0.2562 0.2559 
'X-RAY DIFFRACTION' 2 ? refined -18.5951 1.0009  -15.6748 0.3498 0.3265 -0.2959 0.1932 0.0255 0.0368 2.1017 2.8756 3.5161 -1.3146 
0.1736 -0.0278 0.3931 -0.4221 0.0290 0.1626 0.1700 0.0668  -0.2801 0.0993  0.1488 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 50 A 88  '{ A|* }' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 B 171 '{ B|* }' ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B84 N1   N N N 1   
A1B84 N3   N N N 2   
A1B84 C4   C Y N 3   
A1B84 C5   C Y N 4   
A1B84 C6   C Y N 5   
A1B84 C7   C Y N 6   
A1B84 C8   C Y N 7   
A1B84 C10  C N N 8   
A1B84 C13  C Y N 9   
A1B84 C15  C Y N 10  
A1B84 C17  C Y N 11  
A1B84 C1   C N N 12  
A1B84 C2   C N S 13  
A1B84 N2   N N N 14  
A1B84 C3   C Y N 15  
A1B84 C9   C N N 16  
A1B84 C11  C Y N 17  
A1B84 C12  C Y N 18  
A1B84 N4   N Y N 19  
A1B84 C14  C Y N 20  
A1B84 C16  C Y N 21  
A1B84 C18  C Y N 22  
A1B84 C19  C Y N 23  
A1B84 H17  H N N 24  
A1B84 H3   H N N 25  
A1B84 H4   H N N 26  
A1B84 H5   H N N 27  
A1B84 H10  H N N 28  
A1B84 H9   H N N 29  
A1B84 H12  H N N 30  
A1B84 H13  H N N 31  
A1B84 H15  H N N 32  
A1B84 H1   H N N 33  
A1B84 H2   H N N 34  
A1B84 H7   H N N 35  
A1B84 H6   H N N 36  
A1B84 H11  H N N 37  
A1B84 H14  H N N 38  
A1B84 H16  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
DMS   S    S N N 127 
DMS   O    O N N 128 
DMS   C1   C N N 129 
DMS   C2   C N N 130 
DMS   H11  H N N 131 
DMS   H12  H N N 132 
DMS   H13  H N N 133 
DMS   H21  H N N 134 
DMS   H22  H N N 135 
DMS   H23  H N N 136 
GLN   N    N N N 137 
GLN   CA   C N S 138 
GLN   C    C N N 139 
GLN   O    O N N 140 
GLN   CB   C N N 141 
GLN   CG   C N N 142 
GLN   CD   C N N 143 
GLN   OE1  O N N 144 
GLN   NE2  N N N 145 
GLN   OXT  O N N 146 
GLN   H    H N N 147 
GLN   H2   H N N 148 
GLN   HA   H N N 149 
GLN   HB2  H N N 150 
GLN   HB3  H N N 151 
GLN   HG2  H N N 152 
GLN   HG3  H N N 153 
GLN   HE21 H N N 154 
GLN   HE22 H N N 155 
GLN   HXT  H N N 156 
GLU   N    N N N 157 
GLU   CA   C N S 158 
GLU   C    C N N 159 
GLU   O    O N N 160 
GLU   CB   C N N 161 
GLU   CG   C N N 162 
GLU   CD   C N N 163 
GLU   OE1  O N N 164 
GLU   OE2  O N N 165 
GLU   OXT  O N N 166 
GLU   H    H N N 167 
GLU   H2   H N N 168 
GLU   HA   H N N 169 
GLU   HB2  H N N 170 
GLU   HB3  H N N 171 
GLU   HG2  H N N 172 
GLU   HG3  H N N 173 
GLU   HE2  H N N 174 
GLU   HXT  H N N 175 
GLY   N    N N N 176 
GLY   CA   C N N 177 
GLY   C    C N N 178 
GLY   O    O N N 179 
GLY   OXT  O N N 180 
GLY   H    H N N 181 
GLY   H2   H N N 182 
GLY   HA2  H N N 183 
GLY   HA3  H N N 184 
GLY   HXT  H N N 185 
HIS   N    N N N 186 
HIS   CA   C N S 187 
HIS   C    C N N 188 
HIS   O    O N N 189 
HIS   CB   C N N 190 
HIS   CG   C Y N 191 
HIS   ND1  N Y N 192 
HIS   CD2  C Y N 193 
HIS   CE1  C Y N 194 
HIS   NE2  N Y N 195 
HIS   OXT  O N N 196 
HIS   H    H N N 197 
HIS   H2   H N N 198 
HIS   HA   H N N 199 
HIS   HB2  H N N 200 
HIS   HB3  H N N 201 
HIS   HD1  H N N 202 
HIS   HD2  H N N 203 
HIS   HE1  H N N 204 
HIS   HE2  H N N 205 
HIS   HXT  H N N 206 
HOH   O    O N N 207 
HOH   H1   H N N 208 
HOH   H2   H N N 209 
ILE   N    N N N 210 
ILE   CA   C N S 211 
ILE   C    C N N 212 
ILE   O    O N N 213 
ILE   CB   C N S 214 
ILE   CG1  C N N 215 
ILE   CG2  C N N 216 
ILE   CD1  C N N 217 
ILE   OXT  O N N 218 
ILE   H    H N N 219 
ILE   H2   H N N 220 
ILE   HA   H N N 221 
ILE   HB   H N N 222 
ILE   HG12 H N N 223 
ILE   HG13 H N N 224 
ILE   HG21 H N N 225 
ILE   HG22 H N N 226 
ILE   HG23 H N N 227 
ILE   HD11 H N N 228 
ILE   HD12 H N N 229 
ILE   HD13 H N N 230 
ILE   HXT  H N N 231 
LEU   N    N N N 232 
LEU   CA   C N S 233 
LEU   C    C N N 234 
LEU   O    O N N 235 
LEU   CB   C N N 236 
LEU   CG   C N N 237 
LEU   CD1  C N N 238 
LEU   CD2  C N N 239 
LEU   OXT  O N N 240 
LEU   H    H N N 241 
LEU   H2   H N N 242 
LEU   HA   H N N 243 
LEU   HB2  H N N 244 
LEU   HB3  H N N 245 
LEU   HG   H N N 246 
LEU   HD11 H N N 247 
LEU   HD12 H N N 248 
LEU   HD13 H N N 249 
LEU   HD21 H N N 250 
LEU   HD22 H N N 251 
LEU   HD23 H N N 252 
LEU   HXT  H N N 253 
LYS   N    N N N 254 
LYS   CA   C N S 255 
LYS   C    C N N 256 
LYS   O    O N N 257 
LYS   CB   C N N 258 
LYS   CG   C N N 259 
LYS   CD   C N N 260 
LYS   CE   C N N 261 
LYS   NZ   N N N 262 
LYS   OXT  O N N 263 
LYS   H    H N N 264 
LYS   H2   H N N 265 
LYS   HA   H N N 266 
LYS   HB2  H N N 267 
LYS   HB3  H N N 268 
LYS   HG2  H N N 269 
LYS   HG3  H N N 270 
LYS   HD2  H N N 271 
LYS   HD3  H N N 272 
LYS   HE2  H N N 273 
LYS   HE3  H N N 274 
LYS   HZ1  H N N 275 
LYS   HZ2  H N N 276 
LYS   HZ3  H N N 277 
LYS   HXT  H N N 278 
MET   N    N N N 279 
MET   CA   C N S 280 
MET   C    C N N 281 
MET   O    O N N 282 
MET   CB   C N N 283 
MET   CG   C N N 284 
MET   SD   S N N 285 
MET   CE   C N N 286 
MET   OXT  O N N 287 
MET   H    H N N 288 
MET   H2   H N N 289 
MET   HA   H N N 290 
MET   HB2  H N N 291 
MET   HB3  H N N 292 
MET   HG2  H N N 293 
MET   HG3  H N N 294 
MET   HE1  H N N 295 
MET   HE2  H N N 296 
MET   HE3  H N N 297 
MET   HXT  H N N 298 
PHE   N    N N N 299 
PHE   CA   C N S 300 
PHE   C    C N N 301 
PHE   O    O N N 302 
PHE   CB   C N N 303 
PHE   CG   C Y N 304 
PHE   CD1  C Y N 305 
PHE   CD2  C Y N 306 
PHE   CE1  C Y N 307 
PHE   CE2  C Y N 308 
PHE   CZ   C Y N 309 
PHE   OXT  O N N 310 
PHE   H    H N N 311 
PHE   H2   H N N 312 
PHE   HA   H N N 313 
PHE   HB2  H N N 314 
PHE   HB3  H N N 315 
PHE   HD1  H N N 316 
PHE   HD2  H N N 317 
PHE   HE1  H N N 318 
PHE   HE2  H N N 319 
PHE   HZ   H N N 320 
PHE   HXT  H N N 321 
PRO   N    N N N 322 
PRO   CA   C N S 323 
PRO   C    C N N 324 
PRO   O    O N N 325 
PRO   CB   C N N 326 
PRO   CG   C N N 327 
PRO   CD   C N N 328 
PRO   OXT  O N N 329 
PRO   H    H N N 330 
PRO   HA   H N N 331 
PRO   HB2  H N N 332 
PRO   HB3  H N N 333 
PRO   HG2  H N N 334 
PRO   HG3  H N N 335 
PRO   HD2  H N N 336 
PRO   HD3  H N N 337 
PRO   HXT  H N N 338 
SER   N    N N N 339 
SER   CA   C N S 340 
SER   C    C N N 341 
SER   O    O N N 342 
SER   CB   C N N 343 
SER   OG   O N N 344 
SER   OXT  O N N 345 
SER   H    H N N 346 
SER   H2   H N N 347 
SER   HA   H N N 348 
SER   HB2  H N N 349 
SER   HB3  H N N 350 
SER   HG   H N N 351 
SER   HXT  H N N 352 
THR   N    N N N 353 
THR   CA   C N S 354 
THR   C    C N N 355 
THR   O    O N N 356 
THR   CB   C N R 357 
THR   OG1  O N N 358 
THR   CG2  C N N 359 
THR   OXT  O N N 360 
THR   H    H N N 361 
THR   H2   H N N 362 
THR   HA   H N N 363 
THR   HB   H N N 364 
THR   HG1  H N N 365 
THR   HG21 H N N 366 
THR   HG22 H N N 367 
THR   HG23 H N N 368 
THR   HXT  H N N 369 
TRP   N    N N N 370 
TRP   CA   C N S 371 
TRP   C    C N N 372 
TRP   O    O N N 373 
TRP   CB   C N N 374 
TRP   CG   C Y N 375 
TRP   CD1  C Y N 376 
TRP   CD2  C Y N 377 
TRP   NE1  N Y N 378 
TRP   CE2  C Y N 379 
TRP   CE3  C Y N 380 
TRP   CZ2  C Y N 381 
TRP   CZ3  C Y N 382 
TRP   CH2  C Y N 383 
TRP   OXT  O N N 384 
TRP   H    H N N 385 
TRP   H2   H N N 386 
TRP   HA   H N N 387 
TRP   HB2  H N N 388 
TRP   HB3  H N N 389 
TRP   HD1  H N N 390 
TRP   HE1  H N N 391 
TRP   HE3  H N N 392 
TRP   HZ2  H N N 393 
TRP   HZ3  H N N 394 
TRP   HH2  H N N 395 
TRP   HXT  H N N 396 
TYR   N    N N N 397 
TYR   CA   C N S 398 
TYR   C    C N N 399 
TYR   O    O N N 400 
TYR   CB   C N N 401 
TYR   CG   C Y N 402 
TYR   CD1  C Y N 403 
TYR   CD2  C Y N 404 
TYR   CE1  C Y N 405 
TYR   CE2  C Y N 406 
TYR   CZ   C Y N 407 
TYR   OH   O N N 408 
TYR   OXT  O N N 409 
TYR   H    H N N 410 
TYR   H2   H N N 411 
TYR   HA   H N N 412 
TYR   HB2  H N N 413 
TYR   HB3  H N N 414 
TYR   HD1  H N N 415 
TYR   HD2  H N N 416 
TYR   HE1  H N N 417 
TYR   HE2  H N N 418 
TYR   HH   H N N 419 
TYR   HXT  H N N 420 
VAL   N    N N N 421 
VAL   CA   C N S 422 
VAL   C    C N N 423 
VAL   O    O N N 424 
VAL   CB   C N N 425 
VAL   CG1  C N N 426 
VAL   CG2  C N N 427 
VAL   OXT  O N N 428 
VAL   H    H N N 429 
VAL   H2   H N N 430 
VAL   HA   H N N 431 
VAL   HB   H N N 432 
VAL   HG11 H N N 433 
VAL   HG12 H N N 434 
VAL   HG13 H N N 435 
VAL   HG21 H N N 436 
VAL   HG22 H N N 437 
VAL   HG23 H N N 438 
VAL   HXT  H N N 439 
# 
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 
A1B84 N1  C1   trip N N 1   
A1B84 C1  C2   sing N N 2   
A1B84 C2  N2   sing N N 3   
A1B84 N2  C3   sing N N 4   
A1B84 C3  C4   doub Y N 5   
A1B84 C4  C5   sing Y N 6   
A1B84 C5  C6   doub Y N 7   
A1B84 C6  C7   sing Y N 8   
A1B84 C7  C8   doub Y N 9   
A1B84 C7  C9   sing N N 10  
A1B84 C9  N3   sing N N 11  
A1B84 N3  C10  sing N N 12  
A1B84 C2  C11  sing N N 13  
A1B84 C11 C12  doub Y N 14  
A1B84 C12 N4   sing Y N 15  
A1B84 N4  C13  doub Y N 16  
A1B84 C13 C14  sing Y N 17  
A1B84 C14 C15  doub Y N 18  
A1B84 C15 C16  sing Y N 19  
A1B84 C16 C17  doub Y N 20  
A1B84 C17 C18  sing Y N 21  
A1B84 C18 C19  doub Y N 22  
A1B84 C3  C8   sing Y N 23  
A1B84 C11 C19  sing Y N 24  
A1B84 C6  C10  sing N N 25  
A1B84 C14 C19  sing Y N 26  
A1B84 N3  H17  sing N N 27  
A1B84 C4  H3   sing N N 28  
A1B84 C5  H4   sing N N 29  
A1B84 C8  H5   sing N N 30  
A1B84 C10 H10  sing N N 31  
A1B84 C10 H9   sing N N 32  
A1B84 C13 H12  sing N N 33  
A1B84 C15 H13  sing N N 34  
A1B84 C17 H15  sing N N 35  
A1B84 C2  H1   sing N N 36  
A1B84 N2  H2   sing N N 37  
A1B84 C9  H7   sing N N 38  
A1B84 C9  H6   sing N N 39  
A1B84 C12 H11  sing N N 40  
A1B84 C16 H14  sing N N 41  
A1B84 C18 H16  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002345 
_pdbx_deposit_group.group_description   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7IAH 
_atom_sites.fract_transf_matrix[1][1]   0.023502 
_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]   0.023502 
_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]   0.004604 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -20.758 19.150  -7.481  1.00 72.38  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -21.987 18.366  -7.416  1.00 72.37  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.268 17.703  -8.768  1.00 70.76  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.495 18.381  -9.773  1.00 70.63  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.169 19.224  -6.927  1.00 75.34  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.426 18.417  -6.666  1.00 81.62  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.556 17.860  -5.539  1.00 81.94  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.276 18.324  -7.593  1.00 84.31  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.206 16.367  -8.787  1.00 69.01  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.359 15.579  -9.995  1.00 67.73  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.797 15.391  -10.451 1.00 65.97  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.713 15.354  -9.626  1.00 65.61  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.651 14.229  -9.849  1.00 68.35  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.200 14.380  -9.508  1.00 70.39  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.326 12.826  -9.306  1.00 74.49  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.732 13.452  -8.785  1.00 72.32  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.977 15.283  -11.788 1.00 63.98  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.263 15.075  -12.460 1.00 63.16  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.134 14.106  -13.650 1.00 62.50  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.032 13.874  -14.132 1.00 61.90  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.912 16.407  -12.896 1.00 62.98  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.167 17.182  -13.962 1.00 63.78  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.147 18.062  -13.625 1.00 64.58  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.578 17.149  -15.292 1.00 64.75  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.484 18.807  -14.594 1.00 65.35  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.914 17.878  -16.271 1.00 65.42  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.875 18.719  -15.916 1.00 66.40  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.225 19.465  -16.877 1.00 68.24  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.263 13.538  -14.124 1.00 61.94  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.244 12.576  -15.214 1.00 61.33  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.104 13.010  -16.418 1.00 62.06  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.195 13.557  -16.246 1.00 62.19  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.601 11.146  -14.715 1.00 60.60  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.075 11.006  -14.306 1.00 60.37  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.668 10.700  -13.573 1.00 60.90  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.501 9.551   -14.024 1.00 60.74  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.572 12.789  -17.636 1.00 62.25  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.208 13.071  -18.932 1.00 63.05  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.234 11.741  -19.704 1.00 63.43  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.215 11.061  -19.735 1.00 63.73  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.360 14.064  -19.757 1.00 65.62  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.169 15.454  -19.171 1.00 71.80  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.543 16.431  -20.156 1.00 80.27  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.799 15.978  -21.055 1.00 80.25  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.799 17.653  -20.033 1.00 84.60  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.346 11.388  -20.370 1.00 62.94  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.419 10.123  -21.106 1.00 62.63  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.584 10.130  -22.377 1.00 62.77  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.540 11.137  -23.074 1.00 62.83  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.871 9.773   -21.404 1.00 63.65  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.100 8.323   -21.764 1.00 65.33  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.507 8.140   -22.283 1.00 67.40  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.842 6.723   -22.402 1.00 70.02  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.889 6.063   -23.553 1.00 72.98  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.650 6.690   -24.699 1.00 73.84  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.189 4.772   -23.572 1.00 72.90  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.911 9.011   -22.677 1.00 62.57  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -26.056 8.893   -23.858 1.00 62.81  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.464 7.800   -24.851 1.00 63.33  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.709 7.523   -25.777 1.00 63.70  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.610 8.695   -23.441 1.00 62.86  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.627 7.189   -24.669 1.00 63.48  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -28.107 6.175   -25.600 1.00 64.25  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.542 4.856   -25.000 1.00 65.26  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.482 4.664   -23.792 1.00 64.59  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -29.005 3.943   -25.866 1.00 66.43  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.448 2.597   -25.495 1.00 67.45  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.266 1.666   -25.332 1.00 68.57  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.216 1.892   -25.926 1.00 68.84  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.348 2.008   -26.606 1.00 68.48  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.725 2.624   -26.705 1.00 72.74  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.990 3.597   -25.983 1.00 72.64  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.531 2.153   -27.534 1.00 75.60  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.453 0.578   -24.577 1.00 69.17  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.428 -0.437  -24.444 1.00 69.91  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.804 -1.588  -25.383 1.00 71.20  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.679 -2.399  -25.075 1.00 70.98  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.261 -0.852  -22.978 1.00 69.89  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.626 0.302   -22.187 1.00 70.51  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.416 -2.104  -22.876 1.00 70.31  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.600 0.131   -20.714 1.00 71.20  ? 59  ILE   A CD1 1 
ATOM   82   N N   . THR   A 1 17  ? -27.215 -1.582  -26.589 1.00 72.53  ? 60  THR   A N   1 
ATOM   83   C CA  . THR   A 1 17  ? -27.496 -2.592  -27.604 1.00 74.24  ? 60  THR   A CA  1 
ATOM   84   C C   . THR   A 1 17  ? -26.221 -3.130  -28.253 1.00 76.03  ? 60  THR   A C   1 
ATOM   85   O O   . THR   A 1 17  ? -25.210 -2.435  -28.309 1.00 75.54  ? 60  THR   A O   1 
ATOM   86   C CB  . THR   A 1 17  ? -28.403 -2.008  -28.707 1.00 75.34  ? 60  THR   A CB  1 
ATOM   87   O OG1 . THR   A 1 17  ? -27.692 -1.011  -29.465 1.00 76.52  ? 60  THR   A OG1 1 
ATOM   88   C CG2 . THR   A 1 17  ? -29.726 -1.459  -28.174 1.00 75.36  ? 60  THR   A CG2 1 
ATOM   89   N N   . TRP   A 1 18  ? -26.292 -4.343  -28.805 1.00 78.02  ? 61  TRP   A N   1 
ATOM   90   C CA  . TRP   A 1 18  ? -25.176 -4.907  -29.564 1.00 80.47  ? 61  TRP   A CA  1 
ATOM   91   C C   . TRP   A 1 18  ? -25.252 -4.340  -30.993 1.00 82.53  ? 61  TRP   A C   1 
ATOM   92   O O   . TRP   A 1 18  ? -26.334 -4.277  -31.576 1.00 82.50  ? 61  TRP   A O   1 
ATOM   93   C CB  . TRP   A 1 18  ? -25.261 -6.446  -29.591 1.00 80.50  ? 61  TRP   A CB  1 
ATOM   94   C CG  . TRP   A 1 18  ? -24.135 -7.132  -30.313 1.00 81.13  ? 61  TRP   A CG  1 
ATOM   95   C CD1 . TRP   A 1 18  ? -24.123 -7.536  -31.616 1.00 82.26  ? 61  TRP   A CD1 1 
ATOM   96   C CD2 . TRP   A 1 18  ? -22.894 -7.574  -29.744 1.00 81.23  ? 61  TRP   A CD2 1 
ATOM   97   N NE1 . TRP   A 1 18  ? -22.937 -8.173  -31.902 1.00 82.55  ? 61  TRP   A NE1 1 
ATOM   98   C CE2 . TRP   A 1 18  ? -22.166 -8.213  -30.768 1.00 82.04  ? 61  TRP   A CE2 1 
ATOM   99   C CE3 . TRP   A 1 18  ? -22.307 -7.456  -28.480 1.00 81.38  ? 61  TRP   A CE3 1 
ATOM   100  C CZ2 . TRP   A 1 18  ? -20.897 -8.753  -30.555 1.00 82.41  ? 61  TRP   A CZ2 1 
ATOM   101  C CZ3 . TRP   A 1 18  ? -21.062 -8.010  -28.269 1.00 81.92  ? 61  TRP   A CZ3 1 
ATOM   102  C CH2 . TRP   A 1 18  ? -20.363 -8.631  -29.300 1.00 82.21  ? 61  TRP   A CH2 1 
ATOM   103  N N   . GLU   A 1 19  ? -24.122 -3.892  -31.540 1.00 84.24  ? 62  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 19  ? -24.083 -3.358  -32.897 1.00 86.44  ? 62  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 19  ? -23.395 -4.363  -33.832 1.00 88.97  ? 62  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 19  ? -22.192 -4.579  -33.685 1.00 89.73  ? 62  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 19  ? -23.336 -2.006  -32.938 1.00 88.41  ? 62  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 19  ? -23.173 -1.454  -34.351 1.00 94.06  ? 62  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 19  ? -22.144 -0.354  -34.529 1.00 98.89  ? 62  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 19  ? -21.456 -0.013  -33.540 1.00 99.79  ? 62  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 19  ? -22.030 0.172   -35.660 1.00 99.43  ? 62  GLU   A OE2 1 
ATOM   112  N N   . LYS   A 1 20  ? -24.138 -4.986  -34.768 1.00 89.97  ? 63  LYS   A N   1 
ATOM   113  C CA  . LYS   A 1 20  ? -23.506 -5.898  -35.721 1.00 91.86  ? 63  LYS   A CA  1 
ATOM   114  C C   . LYS   A 1 20  ? -22.748 -5.019  -36.717 1.00 93.05  ? 63  LYS   A C   1 
ATOM   115  O O   . LYS   A 1 20  ? -23.258 -3.968  -37.123 1.00 93.13  ? 63  LYS   A O   1 
ATOM   116  C CB  . LYS   A 1 20  ? -24.534 -6.749  -36.486 1.00 94.68  ? 63  LYS   A CB  1 
ATOM   117  C CG  . LYS   A 1 20  ? -25.618 -7.398  -35.635 1.00 99.82  ? 63  LYS   A CG  1 
ATOM   118  C CD  . LYS   A 1 20  ? -26.627 -8.128  -36.548 1.00 104.37 ? 63  LYS   A CD  1 
ATOM   119  C CE  . LYS   A 1 20  ? -27.960 -8.379  -35.879 1.00 107.89 ? 63  LYS   A CE  1 
ATOM   120  N NZ  . LYS   A 1 20  ? -28.797 -9.325  -36.661 1.00 109.34 ? 63  LYS   A NZ  1 
ATOM   121  N N   . ASP   A 1 21  ? -21.542 -5.439  -37.104 1.00 93.75  ? 64  ASP   A N   1 
ATOM   122  C CA  . ASP   A 1 21  ? -20.690 -4.681  -38.029 1.00 94.81  ? 64  ASP   A CA  1 
ATOM   123  C C   . ASP   A 1 21  ? -20.082 -3.456  -37.327 1.00 94.69  ? 64  ASP   A C   1 
ATOM   124  O O   . ASP   A 1 21  ? -19.990 -2.370  -37.910 1.00 94.92  ? 64  ASP   A O   1 
ATOM   125  C CB  . ASP   A 1 21  ? -21.408 -4.305  -39.349 1.00 96.99  ? 64  ASP   A CB  1 
ATOM   126  C CG  . ASP   A 1 21  ? -21.902 -5.496  -40.148 1.00 103.59 ? 64  ASP   A CG  1 
ATOM   127  O OD1 . ASP   A 1 21  ? -21.287 -6.583  -40.038 1.00 104.63 ? 64  ASP   A OD1 1 
ATOM   128  O OD2 . ASP   A 1 21  ? -22.892 -5.337  -40.903 1.00 107.02 ? 64  ASP   A OD2 1 
ATOM   129  N N   . ALA   A 1 22  ? -19.665 -3.647  -36.075 1.00 93.87  ? 65  ALA   A N   1 
ATOM   130  C CA  . ALA   A 1 22  ? -18.998 -2.606  -35.298 1.00 93.97  ? 65  ALA   A CA  1 
ATOM   131  C C   . ALA   A 1 22  ? -17.473 -2.688  -35.544 1.00 94.01  ? 65  ALA   A C   1 
ATOM   132  O O   . ALA   A 1 22  ? -16.986 -3.681  -36.092 1.00 94.55  ? 65  ALA   A O   1 
ATOM   133  C CB  . ALA   A 1 22  ? -19.308 -2.784  -33.817 1.00 93.91  ? 65  ALA   A CB  1 
ATOM   134  N N   . GLU   A 1 23  ? -16.727 -1.632  -35.194 1.00 93.27  ? 66  GLU   A N   1 
ATOM   135  C CA  . GLU   A 1 23  ? -15.280 -1.607  -35.374 1.00 92.94  ? 66  GLU   A CA  1 
ATOM   136  C C   . GLU   A 1 23  ? -14.630 -2.657  -34.456 1.00 91.96  ? 66  GLU   A C   1 
ATOM   137  O O   . GLU   A 1 23  ? -14.829 -2.610  -33.248 1.00 91.81  ? 66  GLU   A O   1 
ATOM   138  C CB  . GLU   A 1 23  ? -14.762 -0.204  -35.043 1.00 95.62  ? 66  GLU   A CB  1 
ATOM   139  C CG  . GLU   A 1 23  ? -13.272 -0.017  -35.235 1.00 100.89 ? 66  GLU   A CG  1 
ATOM   140  C CD  . GLU   A 1 23  ? -12.832 1.410   -34.978 1.00 106.81 ? 66  GLU   A CD  1 
ATOM   141  O OE1 . GLU   A 1 23  ? -13.137 1.939   -33.883 1.00 106.20 ? 66  GLU   A OE1 1 
ATOM   142  O OE2 . GLU   A 1 23  ? -12.201 2.006   -35.882 1.00 109.26 ? 66  GLU   A OE2 1 
ATOM   143  N N   . VAL   A 1 24  ? -13.900 -3.630  -35.030 1.00 91.16  ? 67  VAL   A N   1 
ATOM   144  C CA  . VAL   A 1 24  ? -13.259 -4.695  -34.244 1.00 90.84  ? 67  VAL   A CA  1 
ATOM   145  C C   . VAL   A 1 24  ? -11.776 -4.370  -34.020 1.00 89.79  ? 67  VAL   A C   1 
ATOM   146  O O   . VAL   A 1 24  ? -10.991 -4.453  -34.963 1.00 89.93  ? 67  VAL   A O   1 
ATOM   147  C CB  . VAL   A 1 24  ? -13.431 -6.102  -34.884 1.00 91.64  ? 67  VAL   A CB  1 
ATOM   148  C CG1 . VAL   A 1 24  ? -13.067 -7.183  -33.887 1.00 92.56  ? 67  VAL   A CG1 1 
ATOM   149  C CG2 . VAL   A 1 24  ? -14.850 -6.323  -35.394 1.00 91.83  ? 67  VAL   A CG2 1 
ATOM   150  N N   . THR   A 1 25  ? -11.386 -3.991  -32.787 1.00 88.53  ? 68  THR   A N   1 
ATOM   151  C CA  . THR   A 1 25  ? -9.986  -3.643  -32.513 1.00 87.79  ? 68  THR   A CA  1 
ATOM   152  C C   . THR   A 1 25  ? -9.521  -4.143  -31.117 1.00 87.09  ? 68  THR   A C   1 
ATOM   153  O O   . THR   A 1 25  ? -10.307 -4.734  -30.387 1.00 86.97  ? 68  THR   A O   1 
ATOM   154  C CB  . THR   A 1 25  ? -9.778  -2.131  -32.747 1.00 88.67  ? 68  THR   A CB  1 
ATOM   155  O OG1 . THR   A 1 25  ? -8.385  -1.866  -32.938 1.00 89.42  ? 68  THR   A OG1 1 
ATOM   156  C CG2 . THR   A 1 25  ? -10.333 -1.290  -31.625 1.00 88.70  ? 68  THR   A CG2 1 
ATOM   157  N N   . GLY   A 1 26  ? -8.237  -3.962  -30.796 1.00 86.50  ? 69  GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 26  ? -7.667  -4.371  -29.523 1.00 86.39  ? 69  GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 26  ? -7.140  -5.789  -29.492 1.00 85.95  ? 69  GLY   A C   1 
ATOM   160  O O   . GLY   A 1 26  ? -7.611  -6.658  -30.227 1.00 85.95  ? 69  GLY   A O   1 
ATOM   161  N N   . ASN   A 1 27  ? -6.167  -6.038  -28.623 1.00 85.39  ? 70  ASN   A N   1 
ATOM   162  C CA  . ASN   A 1 27  ? -5.602  -7.377  -28.459 1.00 85.22  ? 70  ASN   A CA  1 
ATOM   163  C C   . ASN   A 1 27  ? -6.197  -8.091  -27.201 1.00 83.57  ? 70  ASN   A C   1 
ATOM   164  O O   . ASN   A 1 27  ? -7.083  -7.532  -26.555 1.00 83.93  ? 70  ASN   A O   1 
ATOM   165  C CB  . ASN   A 1 27  ? -4.061  -7.317  -28.466 1.00 87.12  ? 70  ASN   A CB  1 
ATOM   166  C CG  . ASN   A 1 27  ? -3.485  -6.287  -27.530 1.00 91.14  ? 70  ASN   A CG  1 
ATOM   167  O OD1 . ASN   A 1 27  ? -3.530  -5.082  -27.796 1.00 92.97  ? 70  ASN   A OD1 1 
ATOM   168  N ND2 . ASN   A 1 27  ? -2.926  -6.735  -26.418 1.00 91.59  ? 70  ASN   A ND2 1 
ATOM   169  N N   . SER   A 1 28  ? -5.771  -9.338  -26.896 1.00 81.88  ? 71  SER   A N   1 
ATOM   170  C CA  . SER   A 1 28  ? -6.254  -10.126 -25.745 1.00 80.81  ? 71  SER   A CA  1 
ATOM   171  C C   . SER   A 1 28  ? -5.060  -10.607 -24.903 1.00 79.41  ? 71  SER   A C   1 
ATOM   172  O O   . SER   A 1 28  ? -4.653  -11.769 -24.995 1.00 79.44  ? 71  SER   A O   1 
ATOM   173  C CB  . SER   A 1 28  ? -7.059  -11.338 -26.213 1.00 82.15  ? 71  SER   A CB  1 
ATOM   174  O OG  . SER   A 1 28  ? -7.890  -11.055 -27.325 1.00 84.54  ? 71  SER   A OG  1 
ATOM   175  N N   . PRO   A 1 29  ? -4.457  -9.716  -24.100 1.00 78.03  ? 72  PRO   A N   1 
ATOM   176  C CA  . PRO   A 1 29  ? -3.259  -10.115 -23.351 1.00 77.07  ? 72  PRO   A CA  1 
ATOM   177  C C   . PRO   A 1 29  ? -3.526  -10.926 -22.089 1.00 75.58  ? 72  PRO   A C   1 
ATOM   178  O O   . PRO   A 1 29  ? -4.605  -10.859 -21.511 1.00 75.48  ? 72  PRO   A O   1 
ATOM   179  C CB  . PRO   A 1 29  ? -2.568  -8.783  -23.059 1.00 78.05  ? 72  PRO   A CB  1 
ATOM   180  C CG  . PRO   A 1 29  ? -3.693  -7.803  -22.964 1.00 78.85  ? 72  PRO   A CG  1 
ATOM   181  C CD  . PRO   A 1 29  ? -4.793  -8.293  -23.882 1.00 77.47  ? 72  PRO   A CD  1 
ATOM   182  N N   . ARG   A 1 30  ? -2.536  -11.711 -21.682 1.00 74.44  ? 73  ARG   A N   1 
ATOM   183  C CA  . ARG   A 1 30  ? -2.616  -12.531 -20.479 1.00 73.85  ? 73  ARG   A CA  1 
ATOM   184  C C   . ARG   A 1 30  ? -1.651  -11.901 -19.475 1.00 72.47  ? 73  ARG   A C   1 
ATOM   185  O O   . ARG   A 1 30  ? -0.435  -12.038 -19.623 1.00 72.24  ? 73  ARG   A O   1 
ATOM   186  C CB  . ARG   A 1 30  ? -2.221  -13.976 -20.811 1.00 75.86  ? 73  ARG   A CB  1 
ATOM   187  C CG  . ARG   A 1 30  ? -2.278  -14.932 -19.638 1.00 80.74  ? 73  ARG   A CG  1 
ATOM   188  C CD  . ARG   A 1 30  ? -1.668  -16.280 -19.993 1.00 85.49  ? 73  ARG   A CD  1 
ATOM   189  N NE  . ARG   A 1 30  ? -1.702  -17.208 -18.859 1.00 89.73  ? 73  ARG   A NE  1 
ATOM   190  C CZ  . ARG   A 1 30  ? -2.715  -18.026 -18.589 1.00 92.60  ? 73  ARG   A CZ  1 
ATOM   191  N NH1 . ARG   A 1 30  ? -3.792  -18.043 -19.368 1.00 92.45  ? 73  ARG   A NH1 1 
ATOM   192  N NH2 . ARG   A 1 30  ? -2.661  -18.834 -17.536 1.00 92.83  ? 73  ARG   A NH2 1 
ATOM   193  N N   . LEU   A 1 31  ? -2.189  -11.151 -18.497 1.00 71.40  ? 74  LEU   A N   1 
ATOM   194  C CA  . LEU   A 1 31  ? -1.380  -10.434 -17.512 1.00 70.76  ? 74  LEU   A CA  1 
ATOM   195  C C   . LEU   A 1 31  ? -1.482  -11.004 -16.096 1.00 70.14  ? 74  LEU   A C   1 
ATOM   196  O O   . LEU   A 1 31  ? -2.534  -11.489 -15.700 1.00 70.20  ? 74  LEU   A O   1 
ATOM   197  C CB  . LEU   A 1 31  ? -1.795  -8.955  -17.485 1.00 70.84  ? 74  LEU   A CB  1 
ATOM   198  C CG  . LEU   A 1 31  ? -1.727  -8.220  -18.813 1.00 72.46  ? 74  LEU   A CG  1 
ATOM   199  C CD1 . LEU   A 1 31  ? -2.423  -6.887  -18.729 1.00 72.99  ? 74  LEU   A CD1 1 
ATOM   200  C CD2 . LEU   A 1 31  ? -0.291  -8.051  -19.276 1.00 73.29  ? 74  LEU   A CD2 1 
ATOM   201  N N   . ASP   A 1 32  ? -0.390  -10.915 -15.322 1.00 69.23  ? 75  ASP   A N   1 
ATOM   202  C CA  . ASP   A 1 32  ? -0.380  -11.349 -13.933 1.00 68.56  ? 75  ASP   A CA  1 
ATOM   203  C C   . ASP   A 1 32  ? -0.531  -10.093 -13.103 1.00 66.44  ? 75  ASP   A C   1 
ATOM   204  O O   . ASP   A 1 32  ? 0.305   -9.198  -13.208 1.00 66.35  ? 75  ASP   A O   1 
ATOM   205  C CB  . ASP   A 1 32  ? 0.928   -12.074 -13.587 1.00 71.58  ? 75  ASP   A CB  1 
ATOM   206  C CG  . ASP   A 1 32  ? 0.996   -13.500 -14.098 1.00 78.75  ? 75  ASP   A CG  1 
ATOM   207  O OD1 . ASP   A 1 32  ? -0.080  -14.082 -14.391 1.00 79.75  ? 75  ASP   A OD1 1 
ATOM   208  O OD2 . ASP   A 1 32  ? 2.123   -14.037 -14.209 1.00 82.20  ? 75  ASP   A OD2 1 
ATOM   209  N N   . VAL   A 1 33  ? -1.641  -9.975  -12.356 1.00 64.75  ? 76  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 33  ? -1.932  -8.769  -11.572 1.00 63.69  ? 76  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 33  ? -2.290  -9.068  -10.108 1.00 62.80  ? 76  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 33  ? -2.647  -10.199 -9.777  1.00 62.81  ? 76  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 33  ? -3.033  -7.884  -12.241 1.00 63.70  ? 76  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 33  ? -2.587  -7.343  -13.591 1.00 64.35  ? 76  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 33  ? -4.347  -8.640  -12.363 1.00 63.52  ? 76  VAL   A CG2 1 
ATOM   216  N N   . ALA   A 1 34  ? -2.206  -8.035  -9.237  1.00 62.05  ? 77  ALA   A N   1 
ATOM   217  C CA  . ALA   A 1 34  ? -2.555  -8.101  -7.819  1.00 61.74  ? 77  ALA   A CA  1 
ATOM   218  C C   . ALA   A 1 34  ? -3.497  -6.943  -7.508  1.00 61.28  ? 77  ALA   A C   1 
ATOM   219  O O   . ALA   A 1 34  ? -3.265  -5.830  -7.969  1.00 61.72  ? 77  ALA   A O   1 
ATOM   220  C CB  . ALA   A 1 34  ? -1.306  -8.009  -6.945  1.00 61.59  ? 77  ALA   A CB  1 
ATOM   221  N N   . LEU   A 1 35  ? -4.557  -7.197  -6.735  1.00 60.08  ? 78  LEU   A N   1 
ATOM   222  C CA  . LEU   A 1 35  ? -5.523  -6.161  -6.398  1.00 59.80  ? 78  LEU   A CA  1 
ATOM   223  C C   . LEU   A 1 35  ? -5.367  -5.800  -4.921  1.00 60.30  ? 78  LEU   A C   1 
ATOM   224  O O   . LEU   A 1 35  ? -5.476  -6.675  -4.057  1.00 61.25  ? 78  LEU   A O   1 
ATOM   225  C CB  . LEU   A 1 35  ? -6.942  -6.656  -6.724  1.00 58.81  ? 78  LEU   A CB  1 
ATOM   226  C CG  . LEU   A 1 35  ? -8.099  -5.733  -6.375  1.00 58.43  ? 78  LEU   A CG  1 
ATOM   227  C CD1 . LEU   A 1 35  ? -8.174  -4.555  -7.329  1.00 58.73  ? 78  LEU   A CD1 1 
ATOM   228  C CD2 . LEU   A 1 35  ? -9.387  -6.489  -6.395  1.00 58.27  ? 78  LEU   A CD2 1 
ATOM   229  N N   . ASP   A 1 36  ? -5.026  -4.538  -4.630  1.00 59.98  ? 79  ASP   A N   1 
ATOM   230  C CA  . ASP   A 1 36  ? -4.798  -4.122  -3.244  1.00 60.43  ? 79  ASP   A CA  1 
ATOM   231  C C   . ASP   A 1 36  ? -6.112  -3.698  -2.520  1.00 60.89  ? 79  ASP   A C   1 
ATOM   232  O O   . ASP   A 1 36  ? -7.189  -3.754  -3.110  1.00 61.47  ? 79  ASP   A O   1 
ATOM   233  C CB  . ASP   A 1 36  ? -3.673  -3.057  -3.157  1.00 62.04  ? 79  ASP   A CB  1 
ATOM   234  C CG  . ASP   A 1 36  ? -4.016  -1.653  -3.616  1.00 65.86  ? 79  ASP   A CG  1 
ATOM   235  O OD1 . ASP   A 1 36  ? -5.200  -1.375  -3.825  1.00 66.73  ? 79  ASP   A OD1 1 
ATOM   236  O OD2 . ASP   A 1 36  ? -3.089  -0.825  -3.739  1.00 68.26  ? 79  ASP   A OD2 1 
ATOM   237  N N   . GLU   A 1 37  ? -6.023  -3.307  -1.234  1.00 60.88  ? 80  GLU   A N   1 
ATOM   238  C CA  . GLU   A 1 37  ? -7.184  -2.901  -0.449  1.00 60.63  ? 80  GLU   A CA  1 
ATOM   239  C C   . GLU   A 1 37  ? -7.913  -1.667  -1.042  1.00 60.14  ? 80  GLU   A C   1 
ATOM   240  O O   . GLU   A 1 37  ? -9.117  -1.531  -0.861  1.00 59.78  ? 80  GLU   A O   1 
ATOM   241  C CB  . GLU   A 1 37  ? -6.755  -2.660  1.008   1.00 62.98  ? 80  GLU   A CB  1 
ATOM   242  C CG  . GLU   A 1 37  ? -7.892  -2.648  2.012   1.00 66.08  ? 80  GLU   A CG  1 
ATOM   243  C CD  . GLU   A 1 37  ? -7.503  -2.013  3.332   1.00 69.73  ? 80  GLU   A CD  1 
ATOM   244  O OE1 . GLU   A 1 37  ? -7.688  -0.780  3.468   1.00 68.13  ? 80  GLU   A OE1 1 
ATOM   245  O OE2 . GLU   A 1 37  ? -7.001  -2.742  4.222   1.00 70.88  ? 80  GLU   A OE2 1 
ATOM   246  N N   . SER   A 1 38  ? -7.207  -0.806  -1.790  1.00 59.70  ? 81  SER   A N   1 
ATOM   247  C CA  . SER   A 1 38  ? -7.808  0.393   -2.359  1.00 60.01  ? 81  SER   A CA  1 
ATOM   248  C C   . SER   A 1 38  ? -8.424  0.211   -3.755  1.00 60.27  ? 81  SER   A C   1 
ATOM   249  O O   . SER   A 1 38  ? -8.790  1.210   -4.369  1.00 60.69  ? 81  SER   A O   1 
ATOM   250  C CB  . SER   A 1 38  ? -6.795  1.528   -2.402  1.00 61.48  ? 81  SER   A CB  1 
ATOM   251  O OG  . SER   A 1 38  ? -6.228  1.757   -1.125  1.00 64.13  ? 81  SER   A OG  1 
ATOM   252  N N   . GLY   A 1 39  ? -8.525  -1.027  -4.245  1.00 59.79  ? 82  GLY   A N   1 
ATOM   253  C CA  . GLY   A 1 39  ? -9.116  -1.309  -5.553  1.00 59.92  ? 82  GLY   A CA  1 
ATOM   254  C C   . GLY   A 1 39  ? -8.238  -0.949  -6.740  1.00 60.05  ? 82  GLY   A C   1 
ATOM   255  O O   . GLY   A 1 39  ? -8.736  -0.753  -7.851  1.00 60.69  ? 82  GLY   A O   1 
ATOM   256  N N   . ASP   A 1 40  ? -6.924  -0.866  -6.512  1.00 59.57  ? 83  ASP   A N   1 
ATOM   257  C CA  . ASP   A 1 40  ? -5.933  -0.509  -7.514  1.00 59.38  ? 83  ASP   A CA  1 
ATOM   258  C C   . ASP   A 1 40  ? -5.126  -1.733  -7.965  1.00 59.42  ? 83  ASP   A C   1 
ATOM   259  O O   . ASP   A 1 40  ? -4.405  -2.333  -7.165  1.00 59.44  ? 83  ASP   A O   1 
ATOM   260  C CB  . ASP   A 1 40  ? -4.992  0.580   -6.960  1.00 60.47  ? 83  ASP   A CB  1 
ATOM   261  C CG  . ASP   A 1 40  ? -5.706  1.870   -6.613  1.00 63.31  ? 83  ASP   A CG  1 
ATOM   262  O OD1 . ASP   A 1 40  ? -6.754  2.143   -7.218  1.00 63.39  ? 83  ASP   A OD1 1 
ATOM   263  O OD2 . ASP   A 1 40  ? -5.216  2.603   -5.732  1.00 65.57  ? 83  ASP   A OD2 1 
ATOM   264  N N   . PHE   A 1 41  ? -5.255  -2.101  -9.249  1.00 59.37  ? 84  PHE   A N   1 
ATOM   265  C CA  . PHE   A 1 41  ? -4.531  -3.221  -9.836  1.00 59.64  ? 84  PHE   A CA  1 
ATOM   266  C C   . PHE   A 1 41  ? -3.069  -2.865  -10.084 1.00 61.63  ? 84  PHE   A C   1 
ATOM   267  O O   . PHE   A 1 41  ? -2.740  -1.699  -10.301 1.00 61.44  ? 84  PHE   A O   1 
ATOM   268  C CB  . PHE   A 1 41  ? -5.180  -3.650  -11.155 1.00 58.21  ? 84  PHE   A CB  1 
ATOM   269  C CG  . PHE   A 1 41  ? -6.481  -4.406  -11.018 1.00 57.49  ? 84  PHE   A CG  1 
ATOM   270  C CD1 . PHE   A 1 41  ? -6.491  -5.732  -10.629 1.00 57.33  ? 84  PHE   A CD1 1 
ATOM   271  C CD2 . PHE   A 1 41  ? -7.683  -3.818  -11.371 1.00 57.52  ? 84  PHE   A CD2 1 
ATOM   272  C CE1 . PHE   A 1 41  ? -7.682  -6.437  -10.554 1.00 57.72  ? 84  PHE   A CE1 1 
ATOM   273  C CE2 . PHE   A 1 41  ? -8.877  -4.523  -11.276 1.00 57.21  ? 84  PHE   A CE2 1 
ATOM   274  C CZ  . PHE   A 1 41  ? -8.869  -5.830  -10.892 1.00 56.94  ? 84  PHE   A CZ  1 
ATOM   275  N N   . SER   A 1 42  ? -2.193  -3.868  -10.062 1.00 63.46  ? 85  SER   A N   1 
ATOM   276  C CA  . SER   A 1 42  ? -0.777  -3.646  -10.331 1.00 66.26  ? 85  SER   A CA  1 
ATOM   277  C C   . SER   A 1 42  ? -0.162  -4.844  -11.038 1.00 69.23  ? 85  SER   A C   1 
ATOM   278  O O   . SER   A 1 42  ? -0.604  -5.972  -10.827 1.00 69.36  ? 85  SER   A O   1 
ATOM   279  C CB  . SER   A 1 42  ? -0.017  -3.333  -9.049  1.00 67.41  ? 85  SER   A CB  1 
ATOM   280  O OG  . SER   A 1 42  ? -0.043  -4.428  -8.148  1.00 70.29  ? 85  SER   A OG  1 
ATOM   281  N N   . LEU   A 1 43  ? 0.855   -4.610  -11.880 1.00 71.34  ? 86  LEU   A N   1 
ATOM   282  C CA  . LEU   A 1 43  ? 1.504   -5.712  -12.584 1.00 73.62  ? 86  LEU   A CA  1 
ATOM   283  C C   . LEU   A 1 43  ? 2.496   -6.474  -11.713 1.00 75.38  ? 86  LEU   A C   1 
ATOM   284  O O   . LEU   A 1 43  ? 3.291   -5.880  -10.982 1.00 75.41  ? 86  LEU   A O   1 
ATOM   285  C CB  . LEU   A 1 43  ? 2.170   -5.247  -13.878 1.00 74.16  ? 86  LEU   A CB  1 
ATOM   286  C CG  . LEU   A 1 43  ? 1.217   -4.907  -15.008 1.00 76.40  ? 86  LEU   A CG  1 
ATOM   287  C CD1 . LEU   A 1 43  ? 1.971   -4.385  -16.210 1.00 77.18  ? 86  LEU   A CD1 1 
ATOM   288  C CD2 . LEU   A 1 43  ? 0.394   -6.112  -15.418 1.00 77.41  ? 86  LEU   A CD2 1 
ATOM   289  N N   . VAL   A 1 44  ? 2.437   -7.798  -11.805 1.00 76.64  ? 87  VAL   A N   1 
ATOM   290  C CA  . VAL   A 1 44  ? 3.333   -8.714  -11.107 1.00 78.47  ? 87  VAL   A CA  1 
ATOM   291  C C   . VAL   A 1 44  ? 4.206   -9.384  -12.176 1.00 80.83  ? 87  VAL   A C   1 
ATOM   292  O O   . VAL   A 1 44  ? 3.690   -9.757  -13.237 1.00 81.31  ? 87  VAL   A O   1 
ATOM   293  C CB  . VAL   A 1 44  ? 2.514   -9.763  -10.323 1.00 78.85  ? 87  VAL   A CB  1 
ATOM   294  C CG1 . VAL   A 1 44  ? 3.411   -10.866 -9.772  1.00 79.36  ? 87  VAL   A CG1 1 
ATOM   295  C CG2 . VAL   A 1 44  ? 1.706   -9.107  -9.211  1.00 79.18  ? 87  VAL   A CG2 1 
ATOM   296  N N   . GLU   A 1 45  ? 5.524   -9.493  -11.940 1.00 82.13  ? 88  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 45  ? 6.407   -10.129 -12.922 1.00 83.90  ? 88  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 45  ? 7.150   -11.331 -12.330 1.00 84.59  ? 88  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 45  ? 6.921   -12.464 -12.755 1.00 84.82  ? 88  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 45  ? 7.384   -9.115  -13.551 1.00 87.36  ? 88  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 45  ? 6.699   -7.981  -14.298 1.00 93.58  ? 88  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 45  ? 6.480   -8.219  -15.779 1.00 102.14 ? 88  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 45  ? 6.680   -9.368  -16.238 1.00 103.94 ? 88  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 45  ? 6.116   -7.252  -16.486 1.00 104.94 ? 88  GLU   A OE2 1 
ATOM   305  N N   . GLY   B 2 7   ? -35.857 12.202  -11.389 1.00 75.73  ? 16  GLY   B N   1 
ATOM   306  C CA  . GLY   B 2 7   ? -36.124 12.614  -12.759 1.00 76.35  ? 16  GLY   B CA  1 
ATOM   307  C C   . GLY   B 2 7   ? -36.161 11.453  -13.736 1.00 76.80  ? 16  GLY   B C   1 
ATOM   308  O O   . GLY   B 2 7   ? -36.863 10.465  -13.492 1.00 77.56  ? 16  GLY   B O   1 
ATOM   309  N N   . GLU   B 2 8   ? -35.412 11.562  -14.859 1.00 75.82  ? 17  GLU   B N   1 
ATOM   310  C CA  . GLU   B 2 8   ? -35.353 10.521  -15.891 1.00 75.08  ? 17  GLU   B CA  1 
ATOM   311  C C   . GLU   B 2 8   ? -34.713 9.225   -15.386 1.00 73.27  ? 17  GLU   B C   1 
ATOM   312  O O   . GLU   B 2 8   ? -33.542 9.214   -15.013 1.00 73.24  ? 17  GLU   B O   1 
ATOM   313  C CB  . GLU   B 2 8   ? -34.618 11.015  -17.148 1.00 77.71  ? 17  GLU   B CB  1 
ATOM   314  C CG  . GLU   B 2 8   ? -34.572 9.980   -18.263 1.00 82.71  ? 17  GLU   B CG  1 
ATOM   315  C CD  . GLU   B 2 8   ? -33.666 10.321  -19.430 1.00 88.75  ? 17  GLU   B CD  1 
ATOM   316  O OE1 . GLU   B 2 8   ? -32.689 11.077  -19.225 1.00 89.57  ? 17  GLU   B OE1 1 
ATOM   317  O OE2 . GLU   B 2 8   ? -33.951 9.854   -20.556 1.00 91.14  ? 17  GLU   B OE2 1 
ATOM   318  N N   A THR   B 2 9   ? -35.481 8.132   -15.387 0.50 72.44  ? 18  THR   B N   1 
ATOM   319  N N   B THR   B 2 9   ? -35.484 8.135   -15.385 0.50 72.50  ? 18  THR   B N   1 
ATOM   320  C CA  A THR   B 2 9   ? -34.976 6.835   -14.925 0.50 72.17  ? 18  THR   B CA  1 
ATOM   321  C CA  B THR   B 2 9   ? -35.002 6.829   -14.936 0.50 72.31  ? 18  THR   B CA  1 
ATOM   322  C C   A THR   B 2 9   ? -35.016 5.754   -16.024 0.50 71.30  ? 18  THR   B C   1 
ATOM   323  C C   B THR   B 2 9   ? -35.028 5.755   -16.027 0.50 71.37  ? 18  THR   B C   1 
ATOM   324  O O   A THR   B 2 9   ? -34.910 4.569   -15.712 0.50 71.48  ? 18  THR   B O   1 
ATOM   325  O O   B THR   B 2 9   ? -34.925 4.571   -15.709 0.50 71.55  ? 18  THR   B O   1 
ATOM   326  C CB  A THR   B 2 9   ? -35.677 6.353   -13.621 0.50 73.69  ? 18  THR   B CB  1 
ATOM   327  C CB  B THR   B 2 9   ? -35.776 6.365   -13.697 0.50 74.03  ? 18  THR   B CB  1 
ATOM   328  O OG1 A THR   B 2 9   ? -36.406 7.408   -12.972 0.50 74.85  ? 18  THR   B OG1 1 
ATOM   329  O OG1 B THR   B 2 9   ? -37.183 6.509   -13.930 0.50 75.19  ? 18  THR   B OG1 1 
ATOM   330  C CG2 A THR   B 2 9   ? -34.701 5.718   -12.635 0.50 74.01  ? 18  THR   B CG2 1 
ATOM   331  C CG2 B THR   B 2 9   ? -35.363 7.118   -12.438 0.50 74.53  ? 18  THR   B CG2 1 
ATOM   332  N N   . THR   B 2 10  ? -35.165 6.154   -17.300 1.00 70.21  ? 19  THR   B N   1 
ATOM   333  C CA  . THR   B 2 10  ? -35.216 5.227   -18.420 1.00 68.54  ? 19  THR   B CA  1 
ATOM   334  C C   . THR   B 2 10  ? -33.902 4.463   -18.523 1.00 66.51  ? 19  THR   B C   1 
ATOM   335  O O   . THR   B 2 10  ? -32.842 5.053   -18.353 1.00 66.24  ? 19  THR   B O   1 
ATOM   336  C CB  . THR   B 2 10  ? -35.507 6.016   -19.732 1.00 69.70  ? 19  THR   B CB  1 
ATOM   337  O OG1 . THR   B 2 10  ? -36.690 6.807   -19.575 1.00 70.80  ? 19  THR   B OG1 1 
ATOM   338  C CG2 . THR   B 2 10  ? -35.651 5.112   -20.948 1.00 69.77  ? 19  THR   B CG2 1 
ATOM   339  N N   . ASP   B 2 11  ? -33.968 3.148   -18.761 1.00 65.36  ? 20  ASP   B N   1 
ATOM   340  C CA  . ASP   B 2 11  ? -32.788 2.302   -18.959 1.00 65.01  ? 20  ASP   B CA  1 
ATOM   341  C C   . ASP   B 2 11  ? -31.879 2.856   -20.076 1.00 63.57  ? 20  ASP   B C   1 
ATOM   342  O O   . ASP   B 2 11  ? -32.366 3.484   -21.018 1.00 63.42  ? 20  ASP   B O   1 
ATOM   343  C CB  . ASP   B 2 11  ? -33.222 0.887   -19.382 1.00 67.78  ? 20  ASP   B CB  1 
ATOM   344  C CG  . ASP   B 2 11  ? -33.683 -0.016  -18.258 1.00 72.94  ? 20  ASP   B CG  1 
ATOM   345  O OD1 . ASP   B 2 11  ? -34.030 0.508   -17.184 1.00 73.39  ? 20  ASP   B OD1 1 
ATOM   346  O OD2 . ASP   B 2 11  ? -33.705 -1.254  -18.462 1.00 75.60  ? 20  ASP   B OD2 1 
ATOM   347  N N   . GLY   B 2 12  ? -30.581 2.602   -19.970 1.00 62.31  ? 21  GLY   B N   1 
ATOM   348  C CA  . GLY   B 2 12  ? -29.626 3.063   -20.968 1.00 61.38  ? 21  GLY   B CA  1 
ATOM   349  C C   . GLY   B 2 12  ? -28.302 3.508   -20.388 1.00 60.16  ? 21  GLY   B C   1 
ATOM   350  O O   . GLY   B 2 12  ? -28.100 3.431   -19.180 1.00 60.24  ? 21  GLY   B O   1 
ATOM   351  N N   . VAL   B 2 13  ? -27.378 3.970   -21.245 1.00 58.89  ? 22  VAL   B N   1 
ATOM   352  C CA  . VAL   B 2 13  ? -26.069 4.437   -20.787 1.00 58.18  ? 22  VAL   B CA  1 
ATOM   353  C C   . VAL   B 2 13  ? -26.119 5.955   -20.491 1.00 57.39  ? 22  VAL   B C   1 
ATOM   354  O O   . VAL   B 2 13  ? -26.859 6.667   -21.152 1.00 57.25  ? 22  VAL   B O   1 
ATOM   355  C CB  . VAL   B 2 13  ? -24.929 4.005   -21.743 1.00 58.74  ? 22  VAL   B CB  1 
ATOM   356  C CG1 . VAL   B 2 13  ? -25.025 4.690   -23.102 1.00 58.73  ? 22  VAL   B CG1 1 
ATOM   357  C CG2 . VAL   B 2 13  ? -23.569 4.231   -21.114 1.00 59.32  ? 22  VAL   B CG2 1 
ATOM   358  N N   . TYR   B 2 14  ? -25.467 6.424   -19.406 1.00 56.62  ? 23  TYR   B N   1 
ATOM   359  C CA  . TYR   B 2 14  ? -25.523 7.840   -19.026 1.00 55.84  ? 23  TYR   B CA  1 
ATOM   360  C C   . TYR   B 2 14  ? -24.137 8.394   -18.767 1.00 55.62  ? 23  TYR   B C   1 
ATOM   361  O O   . TYR   B 2 14  ? -23.323 7.710   -18.180 1.00 56.04  ? 23  TYR   B O   1 
ATOM   362  C CB  . TYR   B 2 14  ? -26.331 8.023   -17.721 1.00 54.97  ? 23  TYR   B CB  1 
ATOM   363  C CG  . TYR   B 2 14  ? -27.829 7.889   -17.859 1.00 54.51  ? 23  TYR   B CG  1 
ATOM   364  C CD1 . TYR   B 2 14  ? -28.421 6.649   -18.032 1.00 55.00  ? 23  TYR   B CD1 1 
ATOM   365  C CD2 . TYR   B 2 14  ? -28.662 8.986   -17.702 1.00 54.94  ? 23  TYR   B CD2 1 
ATOM   366  C CE1 . TYR   B 2 14  ? -29.790 6.523   -18.202 1.00 55.77  ? 23  TYR   B CE1 1 
ATOM   367  C CE2 . TYR   B 2 14  ? -30.038 8.869   -17.829 1.00 55.76  ? 23  TYR   B CE2 1 
ATOM   368  C CZ  . TYR   B 2 14  ? -30.601 7.630   -18.067 1.00 56.72  ? 23  TYR   B CZ  1 
ATOM   369  O OH  . TYR   B 2 14  ? -31.960 7.486   -18.178 1.00 58.35  ? 23  TYR   B OH  1 
ATOM   370  N N   . ARG   B 2 15  ? -23.896 9.653   -19.104 1.00 55.08  ? 24  ARG   B N   1 
ATOM   371  C CA  . ARG   B 2 15  ? -22.631 10.318  -18.790 1.00 54.96  ? 24  ARG   B CA  1 
ATOM   372  C C   . ARG   B 2 15  ? -22.731 10.887  -17.375 1.00 54.62  ? 24  ARG   B C   1 
ATOM   373  O O   . ARG   B 2 15  ? -23.792 11.342  -16.982 1.00 54.14  ? 24  ARG   B O   1 
ATOM   374  C CB  . ARG   B 2 15  ? -22.357 11.497  -19.745 1.00 55.30  ? 24  ARG   B CB  1 
ATOM   375  C CG  . ARG   B 2 15  ? -22.672 11.280  -21.201 1.00 55.60  ? 24  ARG   B CG  1 
ATOM   376  C CD  . ARG   B 2 15  ? -22.341 12.542  -21.965 1.00 57.61  ? 24  ARG   B CD  1 
ATOM   377  N NE  . ARG   B 2 15  ? -22.548 12.395  -23.417 1.00 57.46  ? 24  ARG   B NE  1 
ATOM   378  C CZ  . ARG   B 2 15  ? -21.610 12.008  -24.271 1.00 57.53  ? 24  ARG   B CZ  1 
ATOM   379  N NH1 . ARG   B 2 15  ? -20.372 11.779  -23.851 1.00 54.74  ? 24  ARG   B NH1 1 
ATOM   380  N NH2 . ARG   B 2 15  ? -21.889 11.894  -25.564 1.00 58.80  ? 24  ARG   B NH2 1 
ATOM   381  N N   . VAL   B 2 16  ? -21.624 10.910  -16.635 1.00 55.39  ? 25  VAL   B N   1 
ATOM   382  C CA  . VAL   B 2 16  ? -21.549 11.461  -15.280 1.00 56.77  ? 25  VAL   B CA  1 
ATOM   383  C C   . VAL   B 2 16  ? -20.728 12.753  -15.377 1.00 58.13  ? 25  VAL   B C   1 
ATOM   384  O O   . VAL   B 2 16  ? -19.537 12.718  -15.667 1.00 58.40  ? 25  VAL   B O   1 
ATOM   385  C CB  . VAL   B 2 16  ? -20.954 10.444  -14.259 1.00 57.86  ? 25  VAL   B CB  1 
ATOM   386  C CG1 . VAL   B 2 16  ? -20.645 11.113  -12.923 1.00 58.30  ? 25  VAL   B CG1 1 
ATOM   387  C CG2 . VAL   B 2 16  ? -21.889 9.251   -14.048 1.00 58.33  ? 25  VAL   B CG2 1 
ATOM   388  N N   . MET   B 2 17  ? -21.385 13.897  -15.203 1.00 59.21  ? 26  MET   B N   1 
ATOM   389  C CA  . MET   B 2 17  ? -20.774 15.213  -15.358 1.00 60.37  ? 26  MET   B CA  1 
ATOM   390  C C   . MET   B 2 17  ? -20.641 15.998  -14.046 1.00 62.40  ? 26  MET   B C   1 
ATOM   391  O O   . MET   B 2 17  ? -21.344 15.721  -13.080 1.00 62.92  ? 26  MET   B O   1 
ATOM   392  C CB  . MET   B 2 17  ? -21.630 16.044  -16.338 1.00 60.04  ? 26  MET   B CB  1 
ATOM   393  C CG  . MET   B 2 17  ? -21.953 15.345  -17.639 1.00 59.91  ? 26  MET   B CG  1 
ATOM   394  S SD  . MET   B 2 17  ? -20.589 15.421  -18.813 1.00 62.35  ? 26  MET   B SD  1 
ATOM   395  C CE  . MET   B 2 17  ? -20.323 17.195  -18.890 1.00 54.94  ? 26  MET   B CE  1 
ATOM   396  N N   . THR   B 2 18  ? -19.765 17.015  -14.029 1.00 63.38  ? 27  THR   B N   1 
ATOM   397  C CA  . THR   B 2 18  ? -19.600 17.899  -12.876 1.00 64.54  ? 27  THR   B CA  1 
ATOM   398  C C   . THR   B 2 18  ? -19.364 19.350  -13.329 1.00 66.75  ? 27  THR   B C   1 
ATOM   399  O O   . THR   B 2 18  ? -18.672 19.584  -14.319 1.00 67.00  ? 27  THR   B O   1 
ATOM   400  C CB  . THR   B 2 18  ? -18.512 17.386  -11.903 1.00 64.68  ? 27  THR   B CB  1 
ATOM   401  O OG1 . THR   B 2 18  ? -18.296 18.362  -10.880 1.00 65.50  ? 27  THR   B OG1 1 
ATOM   402  C CG2 . THR   B 2 18  ? -17.196 17.099  -12.584 1.00 64.48  ? 27  THR   B CG2 1 
ATOM   403  N N   . ARG   B 2 19  ? -19.939 20.321  -12.610 1.00 68.29  ? 28  ARG   B N   1 
ATOM   404  C CA  . ARG   B 2 19  ? -19.704 21.735  -12.916 1.00 70.32  ? 28  ARG   B CA  1 
ATOM   405  C C   . ARG   B 2 19  ? -18.779 22.423  -11.876 1.00 71.73  ? 28  ARG   B C   1 
ATOM   406  O O   . ARG   B 2 19  ? -18.712 23.653  -11.823 1.00 71.96  ? 28  ARG   B O   1 
ATOM   407  C CB  . ARG   B 2 19  ? -21.024 22.505  -13.112 1.00 72.22  ? 28  ARG   B CB  1 
ATOM   408  C CG  . ARG   B 2 19  ? -21.665 22.233  -14.475 1.00 76.22  ? 28  ARG   B CG  1 
ATOM   409  C CD  . ARG   B 2 19  ? -22.735 23.249  -14.830 1.00 80.15  ? 28  ARG   B CD  1 
ATOM   410  N NE  . ARG   B 2 19  ? -23.577 22.801  -15.944 1.00 83.62  ? 28  ARG   B NE  1 
ATOM   411  C CZ  . ARG   B 2 19  ? -24.865 22.482  -15.832 1.00 86.10  ? 28  ARG   B CZ  1 
ATOM   412  N NH1 . ARG   B 2 19  ? -25.478 22.567  -14.654 1.00 86.47  ? 28  ARG   B NH1 1 
ATOM   413  N NH2 . ARG   B 2 19  ? -25.550 22.082  -16.896 1.00 85.24  ? 28  ARG   B NH2 1 
ATOM   414  N N   . ARG   B 2 20  ? -18.053 21.623  -11.072 1.00 72.41  ? 29  ARG   B N   1 
ATOM   415  C CA  . ARG   B 2 20  ? -17.142 22.086  -10.022 1.00 73.56  ? 29  ARG   B CA  1 
ATOM   416  C C   . ARG   B 2 20  ? -15.811 22.594  -10.595 1.00 73.61  ? 29  ARG   B C   1 
ATOM   417  O O   . ARG   B 2 20  ? -15.194 23.500  -10.027 1.00 73.76  ? 29  ARG   B O   1 
ATOM   418  C CB  . ARG   B 2 20  ? -16.902 20.953  -9.009  1.00 75.73  ? 29  ARG   B CB  1 
ATOM   419  C CG  . ARG   B 2 20  ? -16.229 21.398  -7.717  1.00 80.68  ? 29  ARG   B CG  1 
ATOM   420  C CD  . ARG   B 2 20  ? -15.779 20.208  -6.889  1.00 85.60  ? 29  ARG   B CD  1 
ATOM   421  N NE  . ARG   B 2 20  ? -14.843 19.345  -7.618  1.00 89.74  ? 29  ARG   B NE  1 
ATOM   422  C CZ  . ARG   B 2 20  ? -13.597 19.087  -7.225  1.00 92.49  ? 29  ARG   B CZ  1 
ATOM   423  N NH1 . ARG   B 2 20  ? -13.131 19.598  -6.089  1.00 92.41  ? 29  ARG   B NH1 1 
ATOM   424  N NH2 . ARG   B 2 20  ? -12.819 18.289  -7.947  1.00 92.01  ? 29  ARG   B NH2 1 
ATOM   425  N N   . LEU   B 2 21  ? -15.377 22.014  -11.720 1.00 73.20  ? 30  LEU   B N   1 
ATOM   426  C CA  . LEU   B 2 21  ? -14.147 22.392  -12.408 1.00 73.40  ? 30  LEU   B CA  1 
ATOM   427  C C   . LEU   B 2 21  ? -14.463 23.511  -13.452 1.00 73.20  ? 30  LEU   B C   1 
ATOM   428  O O   . LEU   B 2 21  ? -15.477 24.207  -13.311 1.00 73.23  ? 30  LEU   B O   1 
ATOM   429  C CB  . LEU   B 2 21  ? -13.546 21.121  -13.063 1.00 73.97  ? 30  LEU   B CB  1 
ATOM   430  C CG  . LEU   B 2 21  ? -12.404 20.403  -12.330 1.00 75.90  ? 30  LEU   B CG  1 
ATOM   431  C CD1 . LEU   B 2 21  ? -12.719 20.165  -10.868 1.00 76.66  ? 30  LEU   B CD1 1 
ATOM   432  C CD2 . LEU   B 2 21  ? -12.074 19.085  -13.000 1.00 76.53  ? 30  LEU   B CD2 1 
ATOM   433  N N   . LEU   B 2 22  ? -13.604 23.710  -14.472 1.00 72.65  ? 31  LEU   B N   1 
ATOM   434  C CA  . LEU   B 2 22  ? -13.857 24.723  -15.494 1.00 72.62  ? 31  LEU   B CA  1 
ATOM   435  C C   . LEU   B 2 22  ? -14.877 24.161  -16.484 1.00 72.60  ? 31  LEU   B C   1 
ATOM   436  O O   . LEU   B 2 22  ? -14.703 23.041  -16.953 1.00 73.36  ? 31  LEU   B O   1 
ATOM   437  C CB  . LEU   B 2 22  ? -12.555 25.072  -16.209 1.00 72.39  ? 31  LEU   B CB  1 
ATOM   438  C CG  . LEU   B 2 22  ? -12.687 26.030  -17.358 1.00 72.92  ? 31  LEU   B CG  1 
ATOM   439  C CD1 . LEU   B 2 22  ? -12.228 27.402  -16.964 1.00 72.95  ? 31  LEU   B CD1 1 
ATOM   440  C CD2 . LEU   B 2 22  ? -11.934 25.516  -18.552 1.00 73.54  ? 31  LEU   B CD2 1 
ATOM   441  N N   . GLY   B 2 23  ? -15.934 24.922  -16.763 1.00 71.56  ? 32  GLY   B N   1 
ATOM   442  C CA  . GLY   B 2 23  ? -17.005 24.491  -17.652 1.00 70.86  ? 32  GLY   B CA  1 
ATOM   443  C C   . GLY   B 2 23  ? -17.747 23.273  -17.143 1.00 69.74  ? 32  GLY   B C   1 
ATOM   444  O O   . GLY   B 2 23  ? -18.015 23.159  -15.946 1.00 69.64  ? 32  GLY   B O   1 
ATOM   445  N N   . SER   B 2 24  ? -18.054 22.336  -18.048 1.00 68.86  ? 33  SER   B N   1 
ATOM   446  C CA  . SER   B 2 24  ? -18.721 21.077  -17.725 1.00 68.37  ? 33  SER   B CA  1 
ATOM   447  C C   . SER   B 2 24  ? -17.761 19.938  -18.063 1.00 67.05  ? 33  SER   B C   1 
ATOM   448  O O   . SER   B 2 24  ? -17.470 19.728  -19.235 1.00 67.16  ? 33  SER   B O   1 
ATOM   449  C CB  . SER   B 2 24  ? -20.004 20.933  -18.541 1.00 70.49  ? 33  SER   B CB  1 
ATOM   450  O OG  . SER   B 2 24  ? -21.067 21.701  -17.996 1.00 73.79  ? 33  SER   B OG  1 
ATOM   451  N N   . THR   B 2 25  ? -17.246 19.221  -17.048 1.00 65.77  ? 34  THR   B N   1 
ATOM   452  C CA  . THR   B 2 25  ? -16.281 18.142  -17.268 1.00 64.74  ? 34  THR   B CA  1 
ATOM   453  C C   . THR   B 2 25  ? -16.865 16.744  -17.025 1.00 63.13  ? 34  THR   B C   1 
ATOM   454  O O   . THR   B 2 25  ? -17.440 16.507  -15.965 1.00 63.22  ? 34  THR   B O   1 
ATOM   455  C CB  . THR   B 2 25  ? -15.020 18.374  -16.406 1.00 65.93  ? 34  THR   B CB  1 
ATOM   456  O OG1 . THR   B 2 25  ? -14.347 19.566  -16.838 1.00 66.68  ? 34  THR   B OG1 1 
ATOM   457  C CG2 . THR   B 2 25  ? -14.052 17.193  -16.455 1.00 66.05  ? 34  THR   B CG2 1 
ATOM   458  N N   . GLN   B 2 26  ? -16.675 15.810  -17.985 1.00 61.48  ? 35  GLN   B N   1 
ATOM   459  C CA  . GLN   B 2 26  ? -17.140 14.431  -17.833 1.00 60.20  ? 35  GLN   B CA  1 
ATOM   460  C C   . GLN   B 2 26  ? -16.156 13.610  -16.989 1.00 60.11  ? 35  GLN   B C   1 
ATOM   461  O O   . GLN   B 2 26  ? -15.019 13.367  -17.413 1.00 60.95  ? 35  GLN   B O   1 
ATOM   462  C CB  . GLN   B 2 26  ? -17.381 13.745  -19.188 1.00 59.48  ? 35  GLN   B CB  1 
ATOM   463  C CG  . GLN   B 2 26  ? -18.088 12.396  -19.060 1.00 59.37  ? 35  GLN   B CG  1 
ATOM   464  C CD  . GLN   B 2 26  ? -18.331 11.708  -20.384 1.00 61.29  ? 35  GLN   B CD  1 
ATOM   465  O OE1 . GLN   B 2 26  ? -19.068 12.200  -21.247 1.00 62.20  ? 35  GLN   B OE1 1 
ATOM   466  N NE2 . GLN   B 2 26  ? -17.742 10.532  -20.573 1.00 60.22  ? 35  GLN   B NE2 1 
ATOM   467  N N   . VAL   B 2 27  ? -16.596 13.165  -15.810 1.00 58.29  ? 36  VAL   B N   1 
ATOM   468  C CA  . VAL   B 2 27  ? -15.738 12.365  -14.930 1.00 57.18  ? 36  VAL   B CA  1 
ATOM   469  C C   . VAL   B 2 27  ? -15.932 10.840  -15.066 1.00 54.96  ? 36  VAL   B C   1 
ATOM   470  O O   . VAL   B 2 27  ? -15.143 10.070  -14.506 1.00 55.17  ? 36  VAL   B O   1 
ATOM   471  C CB  . VAL   B 2 27  ? -15.878 12.810  -13.463 1.00 58.12  ? 36  VAL   B CB  1 
ATOM   472  C CG1 . VAL   B 2 27  ? -15.209 14.160  -13.247 1.00 59.09  ? 36  VAL   B CG1 1 
ATOM   473  C CG2 . VAL   B 2 27  ? -17.341 12.858  -13.034 1.00 58.51  ? 36  VAL   B CG2 1 
ATOM   474  N N   . GLY   B 2 28  ? -16.972 10.426  -15.785 1.00 52.36  ? 37  GLY   B N   1 
ATOM   475  C CA  . GLY   B 2 28  ? -17.287 9.023   -15.954 1.00 50.90  ? 37  GLY   B CA  1 
ATOM   476  C C   . GLY   B 2 28  ? -18.602 8.784   -16.660 1.00 49.96  ? 37  GLY   B C   1 
ATOM   477  O O   . GLY   B 2 28  ? -19.178 9.699   -17.251 1.00 49.78  ? 37  GLY   B O   1 
ATOM   478  N N   . VAL   B 2 29  ? -19.059 7.535   -16.627 1.00 49.30  ? 38  VAL   B N   1 
ATOM   479  C CA  . VAL   B 2 29  ? -20.257 6.993   -17.276 1.00 49.24  ? 38  VAL   B CA  1 
ATOM   480  C C   . VAL   B 2 29  ? -20.949 5.986   -16.295 1.00 48.09  ? 38  VAL   B C   1 
ATOM   481  O O   . VAL   B 2 29  ? -20.308 5.473   -15.376 1.00 47.68  ? 38  VAL   B O   1 
ATOM   482  C CB  . VAL   B 2 29  ? -19.830 6.293   -18.618 1.00 50.41  ? 38  VAL   B CB  1 
ATOM   483  C CG1 . VAL   B 2 29  ? -20.956 5.471   -19.228 1.00 51.30  ? 38  VAL   B CG1 1 
ATOM   484  C CG2 . VAL   B 2 29  ? -19.291 7.292   -19.650 1.00 50.53  ? 38  VAL   B CG2 1 
ATOM   485  N N   . GLY   B 2 30  ? -22.228 5.699   -16.510 1.00 47.39  ? 39  GLY   B N   1 
ATOM   486  C CA  . GLY   B 2 30  ? -22.954 4.729   -15.700 1.00 47.91  ? 39  GLY   B CA  1 
ATOM   487  C C   . GLY   B 2 30  ? -24.077 4.027   -16.439 1.00 48.60  ? 39  GLY   B C   1 
ATOM   488  O O   . GLY   B 2 30  ? -24.409 4.403   -17.561 1.00 47.43  ? 39  GLY   B O   1 
ATOM   489  N N   . VAL   B 2 31  ? -24.672 2.990   -15.817 1.00 49.77  ? 40  VAL   B N   1 
ATOM   490  C CA  . VAL   B 2 31  ? -25.753 2.203   -16.427 1.00 51.32  ? 40  VAL   B CA  1 
ATOM   491  C C   . VAL   B 2 31  ? -27.046 2.299   -15.628 1.00 52.32  ? 40  VAL   B C   1 
ATOM   492  O O   . VAL   B 2 31  ? -27.037 2.032   -14.429 1.00 52.60  ? 40  VAL   B O   1 
ATOM   493  C CB  . VAL   B 2 31  ? -25.323 0.716   -16.589 1.00 52.21  ? 40  VAL   B CB  1 
ATOM   494  C CG1 . VAL   B 2 31  ? -26.493 -0.174  -17.012 1.00 52.55  ? 40  VAL   B CG1 1 
ATOM   495  C CG2 . VAL   B 2 31  ? -24.168 0.588   -17.573 1.00 52.74  ? 40  VAL   B CG2 1 
ATOM   496  N N   . MET   B 2 32  ? -28.161 2.653   -16.280 1.00 52.67  ? 41  MET   B N   1 
ATOM   497  C CA  . MET   B 2 32  ? -29.440 2.700   -15.578 1.00 53.53  ? 41  MET   B CA  1 
ATOM   498  C C   . MET   B 2 32  ? -30.181 1.416   -15.935 1.00 55.44  ? 41  MET   B C   1 
ATOM   499  O O   . MET   B 2 32  ? -30.391 1.166   -17.110 1.00 56.04  ? 41  MET   B O   1 
ATOM   500  C CB  . MET   B 2 32  ? -30.252 3.930   -16.019 1.00 53.04  ? 41  MET   B CB  1 
ATOM   501  C CG  . MET   B 2 32  ? -31.481 4.174   -15.199 1.00 53.84  ? 41  MET   B CG  1 
ATOM   502  S SD  . MET   B 2 32  ? -31.076 4.746   -13.524 1.00 56.94  ? 41  MET   B SD  1 
ATOM   503  C CE  . MET   B 2 32  ? -30.914 6.496   -13.816 1.00 57.20  ? 41  MET   B CE  1 
ATOM   504  N N   . GLN   B 2 33  ? -30.532 0.579   -14.949 1.00 56.26  ? 42  GLN   B N   1 
ATOM   505  C CA  . GLN   B 2 33  ? -31.279 -0.651  -15.218 1.00 56.78  ? 42  GLN   B CA  1 
ATOM   506  C C   . GLN   B 2 33  ? -32.176 -0.947  -14.051 1.00 57.01  ? 42  GLN   B C   1 
ATOM   507  O O   . GLN   B 2 33  ? -31.725 -0.838  -12.919 1.00 57.75  ? 42  GLN   B O   1 
ATOM   508  C CB  . GLN   B 2 33  ? -30.356 -1.845  -15.498 1.00 58.14  ? 42  GLN   B CB  1 
ATOM   509  C CG  . GLN   B 2 33  ? -31.138 -3.062  -16.001 1.00 61.47  ? 42  GLN   B CG  1 
ATOM   510  C CD  . GLN   B 2 33  ? -30.283 -4.268  -16.304 1.00 65.48  ? 42  GLN   B CD  1 
ATOM   511  O OE1 . GLN   B 2 33  ? -30.284 -5.272  -15.568 1.00 67.87  ? 42  GLN   B OE1 1 
ATOM   512  N NE2 . GLN   B 2 33  ? -29.530 -4.200  -17.392 1.00 64.74  ? 42  GLN   B NE2 1 
ATOM   513  N N   . GLU   B 2 34  ? -33.452 -1.276  -14.292 1.00 56.61  ? 43  GLU   B N   1 
ATOM   514  C CA  . GLU   B 2 34  ? -34.418 -1.586  -13.217 1.00 56.70  ? 43  GLU   B CA  1 
ATOM   515  C C   . GLU   B 2 34  ? -34.502 -0.516  -12.096 1.00 55.69  ? 43  GLU   B C   1 
ATOM   516  O O   . GLU   B 2 34  ? -34.789 -0.830  -10.935 1.00 55.38  ? 43  GLU   B O   1 
ATOM   517  C CB  . GLU   B 2 34  ? -34.157 -2.984  -12.624 1.00 59.74  ? 43  GLU   B CB  1 
ATOM   518  C CG  . GLU   B 2 34  ? -34.042 -4.074  -13.685 1.00 64.87  ? 43  GLU   B CG  1 
ATOM   519  C CD  . GLU   B 2 34  ? -33.503 -5.407  -13.195 1.00 72.14  ? 43  GLU   B CD  1 
ATOM   520  O OE1 . GLU   B 2 34  ? -33.967 -5.888  -12.136 1.00 72.99  ? 43  GLU   B OE1 1 
ATOM   521  O OE2 . GLU   B 2 34  ? -32.622 -5.979  -13.880 1.00 74.89  ? 43  GLU   B OE2 1 
ATOM   522  N N   . GLY   B 2 35  ? -34.278 0.739   -12.468 1.00 54.54  ? 44  GLY   B N   1 
ATOM   523  C CA  . GLY   B 2 35  ? -34.337 1.863   -11.547 1.00 53.39  ? 44  GLY   B CA  1 
ATOM   524  C C   . GLY   B 2 35  ? -33.088 2.059   -10.715 1.00 52.44  ? 44  GLY   B C   1 
ATOM   525  O O   . GLY   B 2 35  ? -33.117 2.792   -9.721  1.00 52.00  ? 44  GLY   B O   1 
ATOM   526  N N   . VAL   B 2 36  ? -31.982 1.407   -11.096 1.00 51.60  ? 45  VAL   B N   1 
ATOM   527  C CA  . VAL   B 2 36  ? -30.741 1.510   -10.345 1.00 51.32  ? 45  VAL   B CA  1 
ATOM   528  C C   . VAL   B 2 36  ? -29.629 2.036   -11.236 1.00 51.06  ? 45  VAL   B C   1 
ATOM   529  O O   . VAL   B 2 36  ? -29.411 1.505   -12.316 1.00 51.31  ? 45  VAL   B O   1 
ATOM   530  C CB  . VAL   B 2 36  ? -30.376 0.152   -9.670  1.00 51.63  ? 45  VAL   B CB  1 
ATOM   531  C CG1 . VAL   B 2 36  ? -28.985 0.172   -9.045  1.00 51.52  ? 45  VAL   B CG1 1 
ATOM   532  C CG2 . VAL   B 2 36  ? -31.424 -0.248  -8.635  1.00 51.66  ? 45  VAL   B CG2 1 
ATOM   533  N N   . PHE   B 2 37  ? -28.929 3.082   -10.795 1.00 50.68  ? 46  PHE   B N   1 
ATOM   534  C CA  . PHE   B 2 37  ? -27.786 3.601   -11.536 1.00 50.47  ? 46  PHE   B CA  1 
ATOM   535  C C   . PHE   B 2 37  ? -26.555 2.861   -11.023 1.00 49.76  ? 46  PHE   B C   1 
ATOM   536  O O   . PHE   B 2 37  ? -26.356 2.752   -9.816  1.00 50.02  ? 46  PHE   B O   1 
ATOM   537  C CB  . PHE   B 2 37  ? -27.628 5.100   -11.325 1.00 50.92  ? 46  PHE   B CB  1 
ATOM   538  C CG  . PHE   B 2 37  ? -26.688 5.745   -12.308 1.00 52.74  ? 46  PHE   B CG  1 
ATOM   539  C CD1 . PHE   B 2 37  ? -26.990 5.783   -13.658 1.00 53.88  ? 46  PHE   B CD1 1 
ATOM   540  C CD2 . PHE   B 2 37  ? -25.496 6.301   -11.887 1.00 54.00  ? 46  PHE   B CD2 1 
ATOM   541  C CE1 . PHE   B 2 37  ? -26.132 6.390   -14.559 1.00 54.83  ? 46  PHE   B CE1 1 
ATOM   542  C CE2 . PHE   B 2 37  ? -24.640 6.905   -12.789 1.00 54.81  ? 46  PHE   B CE2 1 
ATOM   543  C CZ  . PHE   B 2 37  ? -24.966 6.954   -14.119 1.00 54.79  ? 46  PHE   B CZ  1 
ATOM   544  N N   . HIS   B 2 38  ? -25.765 2.311   -11.929 1.00 48.90  ? 47  HIS   B N   1 
ATOM   545  C CA  . HIS   B 2 38  ? -24.589 1.524   -11.596 1.00 48.53  ? 47  HIS   B CA  1 
ATOM   546  C C   . HIS   B 2 38  ? -23.374 2.233   -12.164 1.00 48.51  ? 47  HIS   B C   1 
ATOM   547  O O   . HIS   B 2 38  ? -23.328 2.425   -13.360 1.00 47.68  ? 47  HIS   B O   1 
ATOM   548  C CB  . HIS   B 2 38  ? -24.679 0.145   -12.289 1.00 47.98  ? 47  HIS   B CB  1 
ATOM   549  C CG  . HIS   B 2 38  ? -25.925 -0.636  -11.998 1.00 48.72  ? 47  HIS   B CG  1 
ATOM   550  N ND1 . HIS   B 2 38  ? -27.120 -0.350  -12.626 1.00 50.10  ? 47  HIS   B ND1 1 
ATOM   551  C CD2 . HIS   B 2 38  ? -26.102 -1.715  -11.205 1.00 49.82  ? 47  HIS   B CD2 1 
ATOM   552  C CE1 . HIS   B 2 38  ? -27.991 -1.234  -12.165 1.00 50.10  ? 47  HIS   B CE1 1 
ATOM   553  N NE2 . HIS   B 2 38  ? -27.426 -2.074  -11.312 1.00 50.48  ? 47  HIS   B NE2 1 
ATOM   554  N N   . THR   B 2 39  ? -22.375 2.585   -11.335 1.00 48.57  ? 48  THR   B N   1 
ATOM   555  C CA  . THR   B 2 39  ? -21.147 3.198   -11.872 1.00 48.26  ? 48  THR   B CA  1 
ATOM   556  C C   . THR   B 2 39  ? -19.911 2.664   -11.086 1.00 47.77  ? 48  THR   B C   1 
ATOM   557  O O   . THR   B 2 39  ? -20.046 1.773   -10.242 1.00 46.98  ? 48  THR   B O   1 
ATOM   558  C CB  . THR   B 2 39  ? -21.303 4.743   -11.947 1.00 49.23  ? 48  THR   B CB  1 
ATOM   559  O OG1 . THR   B 2 39  ? -20.308 5.296   -12.827 1.00 49.70  ? 48  THR   B OG1 1 
ATOM   560  C CG2 . THR   B 2 39  ? -21.251 5.404   -10.585 1.00 49.23  ? 48  THR   B CG2 1 
ATOM   561  N N   . MET   B 2 40  ? -18.712 3.149   -11.417 1.00 47.83  ? 49  MET   B N   1 
ATOM   562  C CA  . MET   B 2 40  ? -17.493 2.765   -10.732 1.00 48.34  ? 49  MET   B CA  1 
ATOM   563  C C   . MET   B 2 40  ? -17.313 3.723   -9.563  1.00 48.50  ? 49  MET   B C   1 
ATOM   564  O O   . MET   B 2 40  ? -17.619 4.907   -9.694  1.00 49.39  ? 49  MET   B O   1 
ATOM   565  C CB  . MET   B 2 40  ? -16.292 2.834   -11.679 1.00 49.53  ? 49  MET   B CB  1 
ATOM   566  C CG  . MET   B 2 40  ? -16.475 2.012   -12.938 1.00 52.95  ? 49  MET   B CG  1 
ATOM   567  S SD  . MET   B 2 40  ? -15.014 1.017   -13.366 1.00 56.37  ? 49  MET   B SD  1 
ATOM   568  C CE  . MET   B 2 40  ? -15.254 -0.382  -12.271 1.00 48.15  ? 49  MET   B CE  1 
ATOM   569  N N   . TRP   B 2 41  ? -16.831 3.216   -8.423  1.00 47.03  ? 50  TRP   B N   1 
ATOM   570  C CA  A TRP   B 2 41  ? -16.635 4.022   -7.219  0.50 47.33  ? 50  TRP   B CA  1 
ATOM   571  C CA  B TRP   B 2 41  ? -16.631 4.005   -7.220  0.50 46.40  ? 50  TRP   B CA  1 
ATOM   572  C C   . TRP   B 2 41  ? -15.724 5.224   -7.423  1.00 46.84  ? 50  TRP   B C   1 
ATOM   573  O O   . TRP   B 2 41  ? -15.968 6.265   -6.810  1.00 47.41  ? 50  TRP   B O   1 
ATOM   574  C CB  A TRP   B 2 41  ? -16.146 3.174   -6.022  0.50 47.77  ? 50  TRP   B CB  1 
ATOM   575  C CB  B TRP   B 2 41  ? -16.111 3.111   -6.080  0.50 45.53  ? 50  TRP   B CB  1 
ATOM   576  C CG  A TRP   B 2 41  ? -16.275 3.872   -4.693  0.50 48.99  ? 50  TRP   B CG  1 
ATOM   577  C CG  B TRP   B 2 41  ? -15.965 3.829   -4.773  0.50 44.93  ? 50  TRP   B CG  1 
ATOM   578  C CD1 A TRP   B 2 41  ? -17.354 3.848   -3.862  0.50 49.90  ? 50  TRP   B CD1 1 
ATOM   579  C CD1 B TRP   B 2 41  ? -14.870 4.502   -4.321  0.50 45.52  ? 50  TRP   B CD1 1 
ATOM   580  C CD2 A TRP   B 2 41  ? -15.307 4.733   -4.068  0.50 49.55  ? 50  TRP   B CD2 1 
ATOM   581  C CD2 B TRP   B 2 41  ? -16.969 3.974   -3.770  0.50 44.17  ? 50  TRP   B CD2 1 
ATOM   582  N NE1 A TRP   B 2 41  ? -17.128 4.655   -2.771  0.50 50.58  ? 50  TRP   B NE1 1 
ATOM   583  N NE1 B TRP   B 2 41  ? -15.139 5.080   -3.109  0.50 45.34  ? 50  TRP   B NE1 1 
ATOM   584  C CE2 A TRP   B 2 41  ? -15.878 5.208   -2.873  0.50 50.47  ? 50  TRP   B CE2 1 
ATOM   585  C CE2 B TRP   B 2 41  ? -16.425 4.773   -2.745  0.50 44.94  ? 50  TRP   B CE2 1 
ATOM   586  C CE3 A TRP   B 2 41  ? -14.016 5.156   -4.410  0.50 50.40  ? 50  TRP   B CE3 1 
ATOM   587  C CE3 B TRP   B 2 41  ? -18.288 3.529   -3.648  0.50 44.28  ? 50  TRP   B CE3 1 
ATOM   588  C CZ2 A TRP   B 2 41  ? -15.204 6.079   -2.018  0.50 51.44  ? 50  TRP   B CZ2 1 
ATOM   589  C CZ2 B TRP   B 2 41  ? -17.148 5.115   -1.602  0.50 45.27  ? 50  TRP   B CZ2 1 
ATOM   590  C CZ3 A TRP   B 2 41  ? -13.353 6.023   -3.565  0.50 51.21  ? 50  TRP   B CZ3 1 
ATOM   591  C CZ3 B TRP   B 2 41  ? -19.004 3.879   -2.519  0.50 45.34  ? 50  TRP   B CZ3 1 
ATOM   592  C CH2 A TRP   B 2 41  ? -13.937 6.458   -2.376  0.50 51.59  ? 50  TRP   B CH2 1 
ATOM   593  C CH2 B TRP   B 2 41  ? -18.427 4.642   -1.502  0.50 45.26  ? 50  TRP   B CH2 1 
ATOM   594  N N   . HIS   B 2 42  ? -14.651 5.093   -8.222  1.00 45.50  ? 51  HIS   B N   1 
ATOM   595  C CA  . HIS   B 2 42  ? -13.726 6.223   -8.416  1.00 46.06  ? 51  HIS   B CA  1 
ATOM   596  C C   . HIS   B 2 42  ? -14.293 7.383   -9.271  1.00 47.46  ? 51  HIS   B C   1 
ATOM   597  O O   . HIS   B 2 42  ? -13.657 8.432   -9.408  1.00 48.32  ? 51  HIS   B O   1 
ATOM   598  C CB  . HIS   B 2 42  ? -12.383 5.745   -8.974  1.00 46.52  ? 51  HIS   B CB  1 
ATOM   599  C CG  . HIS   B 2 42  ? -12.447 5.298   -10.401 1.00 49.03  ? 51  HIS   B CG  1 
ATOM   600  N ND1 . HIS   B 2 42  ? -12.743 3.986   -10.737 1.00 50.97  ? 51  HIS   B ND1 1 
ATOM   601  C CD2 . HIS   B 2 42  ? -12.201 5.990   -11.533 1.00 49.57  ? 51  HIS   B CD2 1 
ATOM   602  C CE1 . HIS   B 2 42  ? -12.665 3.931   -12.052 1.00 50.77  ? 51  HIS   B CE1 1 
ATOM   603  N NE2 . HIS   B 2 42  ? -12.357 5.116   -12.572 1.00 50.59  ? 51  HIS   B NE2 1 
ATOM   604  N N   . VAL   B 2 43  ? -15.449 7.170   -9.895  1.00 47.41  ? 52  VAL   B N   1 
ATOM   605  C CA  . VAL   B 2 43  ? -16.125 8.168   -10.696 1.00 47.23  ? 52  VAL   B CA  1 
ATOM   606  C C   . VAL   B 2 43  ? -16.853 9.150   -9.757  1.00 47.36  ? 52  VAL   B C   1 
ATOM   607  O O   . VAL   B 2 43  ? -16.718 10.360  -9.913  1.00 47.73  ? 52  VAL   B O   1 
ATOM   608  C CB  . VAL   B 2 43  ? -17.122 7.463   -11.644 1.00 48.13  ? 52  VAL   B CB  1 
ATOM   609  C CG1 . VAL   B 2 43  ? -17.984 8.470   -12.408 1.00 48.72  ? 52  VAL   B CG1 1 
ATOM   610  C CG2 . VAL   B 2 43  ? -16.394 6.515   -12.605 1.00 48.98  ? 52  VAL   B CG2 1 
ATOM   611  N N   . THR   B 2 44  ? -17.595 8.631   -8.755  1.00 46.63  ? 53  THR   B N   1 
ATOM   612  C CA  . THR   B 2 44  ? -18.391 9.491   -7.883  1.00 46.40  ? 53  THR   B CA  1 
ATOM   613  C C   . THR   B 2 44  ? -17.855 9.658   -6.467  1.00 47.28  ? 53  THR   B C   1 
ATOM   614  O O   . THR   B 2 44  ? -18.298 10.573  -5.772  1.00 47.37  ? 53  THR   B O   1 
ATOM   615  C CB  . THR   B 2 44  ? -19.840 8.987   -7.844  1.00 46.48  ? 53  THR   B CB  1 
ATOM   616  O OG1 . THR   B 2 44  ? -19.891 7.768   -7.092  1.00 46.39  ? 53  THR   B OG1 1 
ATOM   617  C CG2 . THR   B 2 44  ? -20.430 8.754   -9.256  1.00 47.55  ? 53  THR   B CG2 1 
ATOM   618  N N   . LYS   B 2 45  ? -16.929 8.772   -6.036  1.00 47.40  ? 54  LYS   B N   1 
ATOM   619  C CA  . LYS   B 2 45  ? -16.378 8.704   -4.676  1.00 48.50  ? 54  LYS   B CA  1 
ATOM   620  C C   . LYS   B 2 45  ? -17.484 8.493   -3.614  1.00 48.94  ? 54  LYS   B C   1 
ATOM   621  O O   . LYS   B 2 45  ? -17.282 8.848   -2.451  1.00 49.29  ? 54  LYS   B O   1 
ATOM   622  C CB  . LYS   B 2 45  ? -15.506 9.926   -4.326  1.00 50.93  ? 54  LYS   B CB  1 
ATOM   623  C CG  . LYS   B 2 45  ? -14.443 10.258  -5.372  1.00 55.44  ? 54  LYS   B CG  1 
ATOM   624  C CD  . LYS   B 2 45  ? -13.117 9.585   -5.074  1.00 60.56  ? 54  LYS   B CD  1 
ATOM   625  C CE  . LYS   B 2 45  ? -12.028 10.125  -5.976  1.00 65.32  ? 54  LYS   B CE  1 
ATOM   626  N NZ  . LYS   B 2 45  ? -12.278 9.807   -7.420  1.00 67.58  ? 54  LYS   B NZ  1 
ATOM   627  N N   . GLY   B 2 46  ? -18.630 7.945   -4.030  1.00 48.91  ? 55  GLY   B N   1 
ATOM   628  C CA  . GLY   B 2 46  ? -19.781 7.711   -3.176  1.00 50.39  ? 55  GLY   B CA  1 
ATOM   629  C C   . GLY   B 2 46  ? -20.735 8.881   -3.041  1.00 51.66  ? 55  GLY   B C   1 
ATOM   630  O O   . GLY   B 2 46  ? -21.754 8.751   -2.376  1.00 51.95  ? 55  GLY   B O   1 
ATOM   631  N N   . ALA   B 2 47  ? -20.450 10.024  -3.686  1.00 52.72  ? 56  ALA   B N   1 
ATOM   632  C CA  . ALA   B 2 47  ? -21.336 11.192  -3.606  1.00 53.76  ? 56  ALA   B CA  1 
ATOM   633  C C   . ALA   B 2 47  ? -22.683 11.013  -4.312  1.00 55.80  ? 56  ALA   B C   1 
ATOM   634  O O   . ALA   B 2 47  ? -22.786 10.283  -5.297  1.00 55.99  ? 56  ALA   B O   1 
ATOM   635  C CB  . ALA   B 2 47  ? -20.631 12.427  -4.142  1.00 53.50  ? 56  ALA   B CB  1 
ATOM   636  N N   . ALA   B 2 48  ? -23.713 11.704  -3.815  1.00 57.00  ? 57  ALA   B N   1 
ATOM   637  C CA  . ALA   B 2 48  ? -25.054 11.679  -4.394  1.00 58.59  ? 57  ALA   B CA  1 
ATOM   638  C C   . ALA   B 2 48  ? -25.058 12.417  -5.733  1.00 60.20  ? 57  ALA   B C   1 
ATOM   639  O O   . ALA   B 2 48  ? -24.414 13.457  -5.859  1.00 60.67  ? 57  ALA   B O   1 
ATOM   640  C CB  . ALA   B 2 48  ? -26.040 12.342  -3.440  1.00 58.67  ? 57  ALA   B CB  1 
ATOM   641  N N   . LEU   B 2 49  ? -25.792 11.883  -6.724  1.00 60.98  ? 58  LEU   B N   1 
ATOM   642  C CA  . LEU   B 2 49  ? -25.900 12.440  -8.074  1.00 61.99  ? 58  LEU   B CA  1 
ATOM   643  C C   . LEU   B 2 49  ? -27.202 13.236  -8.280  1.00 63.01  ? 58  LEU   B C   1 
ATOM   644  O O   . LEU   B 2 49  ? -28.093 13.216  -7.440  1.00 63.44  ? 58  LEU   B O   1 
ATOM   645  C CB  . LEU   B 2 49  ? -25.823 11.308  -9.122  1.00 62.10  ? 58  LEU   B CB  1 
ATOM   646  C CG  . LEU   B 2 49  ? -24.654 10.349  -9.005  1.00 63.60  ? 58  LEU   B CG  1 
ATOM   647  C CD1 . LEU   B 2 49  ? -24.783 9.250   -10.010 1.00 63.82  ? 58  LEU   B CD1 1 
ATOM   648  C CD2 . LEU   B 2 49  ? -23.339 11.068  -9.173  1.00 64.22  ? 58  LEU   B CD2 1 
ATOM   649  N N   . ARG   B 2 50  ? -27.306 13.930  -9.404  1.00 63.47  ? 59  ARG   B N   1 
ATOM   650  C CA  . ARG   B 2 50  ? -28.486 14.707  -9.738  1.00 64.91  ? 59  ARG   B CA  1 
ATOM   651  C C   . ARG   B 2 50  ? -29.009 14.278  -11.129 1.00 65.50  ? 59  ARG   B C   1 
ATOM   652  O O   . ARG   B 2 50  ? -28.219 13.931  -12.006 1.00 65.15  ? 59  ARG   B O   1 
ATOM   653  C CB  . ARG   B 2 50  ? -28.144 16.206  -9.648  1.00 67.01  ? 59  ARG   B CB  1 
ATOM   654  C CG  . ARG   B 2 50  ? -29.151 17.138  -10.295 1.00 71.60  ? 59  ARG   B CG  1 
ATOM   655  C CD  . ARG   B 2 50  ? -28.892 18.596  -9.954  1.00 75.32  ? 59  ARG   B CD  1 
ATOM   656  N NE  . ARG   B 2 50  ? -27.558 19.059  -10.356 1.00 78.01  ? 59  ARG   B NE  1 
ATOM   657  C CZ  . ARG   B 2 50  ? -27.261 19.548  -11.556 1.00 79.87  ? 59  ARG   B CZ  1 
ATOM   658  N NH1 . ARG   B 2 50  ? -28.188 19.605  -12.505 1.00 79.60  ? 59  ARG   B NH1 1 
ATOM   659  N NH2 . ARG   B 2 50  ? -26.032 19.971  -11.822 1.00 79.88  ? 59  ARG   B NH2 1 
ATOM   660  N N   . SER   B 2 51  ? -30.330 14.202  -11.296 1.00 66.37  ? 60  SER   B N   1 
ATOM   661  C CA  . SER   B 2 51  ? -30.931 13.824  -12.575 1.00 67.87  ? 60  SER   B CA  1 
ATOM   662  C C   . SER   B 2 51  ? -32.098 14.776  -12.843 1.00 69.72  ? 60  SER   B C   1 
ATOM   663  O O   . SER   B 2 51  ? -33.245 14.458  -12.532 1.00 70.29  ? 60  SER   B O   1 
ATOM   664  C CB  . SER   B 2 51  ? -31.420 12.381  -12.531 1.00 68.90  ? 60  SER   B CB  1 
ATOM   665  O OG  . SER   B 2 51  ? -31.946 11.986  -13.787 1.00 70.76  ? 60  SER   B OG  1 
ATOM   666  N N   . GLY   B 2 52  ? -31.794 15.950  -13.383 1.00 70.39  ? 61  GLY   B N   1 
ATOM   667  C CA  . GLY   B 2 52  ? -32.802 16.984  -13.575 1.00 71.42  ? 61  GLY   B CA  1 
ATOM   668  C C   . GLY   B 2 52  ? -33.072 17.603  -12.220 1.00 72.36  ? 61  GLY   B C   1 
ATOM   669  O O   . GLY   B 2 52  ? -32.135 18.041  -11.552 1.00 72.79  ? 61  GLY   B O   1 
ATOM   670  N N   . GLU   B 2 53  ? -34.330 17.584  -11.765 1.00 72.65  ? 62  GLU   B N   1 
ATOM   671  C CA  . GLU   B 2 53  ? -34.665 18.070  -10.426 1.00 73.55  ? 62  GLU   B CA  1 
ATOM   672  C C   . GLU   B 2 53  ? -34.512 16.969  -9.348  1.00 73.65  ? 62  GLU   B C   1 
ATOM   673  O O   . GLU   B 2 53  ? -34.386 17.289  -8.161  1.00 73.87  ? 62  GLU   B O   1 
ATOM   674  C CB  . GLU   B 2 53  ? -36.089 18.640  -10.389 1.00 76.76  ? 62  GLU   B CB  1 
ATOM   675  C CG  . GLU   B 2 53  ? -36.163 20.141  -10.579 1.00 83.20  ? 62  GLU   B CG  1 
ATOM   676  C CD  . GLU   B 2 53  ? -37.583 20.657  -10.720 1.00 92.71  ? 62  GLU   B CD  1 
ATOM   677  O OE1 . GLU   B 2 53  ? -38.385 19.988  -11.415 1.00 94.83  ? 62  GLU   B OE1 1 
ATOM   678  O OE2 . GLU   B 2 53  ? -37.893 21.731  -10.150 1.00 94.75  ? 62  GLU   B OE2 1 
ATOM   679  N N   . GLY   B 2 54  ? -34.551 15.701  -9.764  1.00 73.14  ? 63  GLY   B N   1 
ATOM   680  C CA  . GLY   B 2 54  ? -34.452 14.557  -8.867  1.00 73.03  ? 63  GLY   B CA  1 
ATOM   681  C C   . GLY   B 2 54  ? -33.059 14.273  -8.346  1.00 72.40  ? 63  GLY   B C   1 
ATOM   682  O O   . GLY   B 2 54  ? -32.060 14.605  -8.989  1.00 72.94  ? 63  GLY   B O   1 
ATOM   683  N N   . ARG   B 2 55  ? -32.991 13.612  -7.189  1.00 71.06  ? 64  ARG   B N   1 
ATOM   684  C CA  . ARG   B 2 55  ? -31.736 13.252  -6.537  1.00 70.03  ? 64  ARG   B CA  1 
ATOM   685  C C   . ARG   B 2 55  ? -31.514 11.724  -6.540  1.00 68.29  ? 64  ARG   B C   1 
ATOM   686  O O   . ARG   B 2 55  ? -32.461 10.963  -6.347  1.00 68.68  ? 64  ARG   B O   1 
ATOM   687  C CB  . ARG   B 2 55  ? -31.766 13.780  -5.093  1.00 71.20  ? 64  ARG   B CB  1 
ATOM   688  C CG  . ARG   B 2 55  ? -30.462 13.639  -4.328  1.00 74.25  ? 64  ARG   B CG  1 
ATOM   689  C CD  . ARG   B 2 55  ? -30.588 14.174  -2.913  1.00 76.93  ? 64  ARG   B CD  1 
ATOM   690  N NE  . ARG   B 2 55  ? -29.452 13.777  -2.082  1.00 79.24  ? 64  ARG   B NE  1 
ATOM   691  C CZ  . ARG   B 2 55  ? -28.753 14.610  -1.314  1.00 80.13  ? 64  ARG   B CZ  1 
ATOM   692  N NH1 . ARG   B 2 55  ? -29.052 15.905  -1.281  1.00 79.03  ? 64  ARG   B NH1 1 
ATOM   693  N NH2 . ARG   B 2 55  ? -27.740 14.157  -0.583  1.00 78.96  ? 64  ARG   B NH2 1 
ATOM   694  N N   . LEU   B 2 56  ? -30.270 11.279  -6.746  1.00 66.12  ? 65  LEU   B N   1 
ATOM   695  C CA  . LEU   B 2 56  ? -29.949 9.857   -6.715  1.00 64.87  ? 65  LEU   B CA  1 
ATOM   696  C C   . LEU   B 2 56  ? -29.025 9.609   -5.543  1.00 63.37  ? 65  LEU   B C   1 
ATOM   697  O O   . LEU   B 2 56  ? -27.897 10.096  -5.543  1.00 63.63  ? 65  LEU   B O   1 
ATOM   698  C CB  . LEU   B 2 56  ? -29.249 9.398   -8.009  1.00 65.02  ? 65  LEU   B CB  1 
ATOM   699  C CG  . LEU   B 2 56  ? -29.972 9.608   -9.335  1.00 66.14  ? 65  LEU   B CG  1 
ATOM   700  C CD1 . LEU   B 2 56  ? -29.193 8.983   -10.454 1.00 66.01  ? 65  LEU   B CD1 1 
ATOM   701  C CD2 . LEU   B 2 56  ? -31.379 9.025   -9.306  1.00 67.05  ? 65  LEU   B CD2 1 
ATOM   702  N N   . ASP   B 2 57  ? -29.482 8.853   -4.550  1.00 61.55  ? 66  ASP   B N   1 
ATOM   703  C CA  . ASP   B 2 57  ? -28.679 8.570   -3.368  1.00 60.23  ? 66  ASP   B CA  1 
ATOM   704  C C   . ASP   B 2 57  ? -27.966 7.211   -3.462  1.00 58.23  ? 66  ASP   B C   1 
ATOM   705  O O   . ASP   B 2 57  ? -28.556 6.245   -3.933  1.00 58.29  ? 66  ASP   B O   1 
ATOM   706  C CB  . ASP   B 2 57  ? -29.578 8.598   -2.135  1.00 62.40  ? 66  ASP   B CB  1 
ATOM   707  C CG  . ASP   B 2 57  ? -30.274 9.927   -1.929  1.00 67.93  ? 66  ASP   B CG  1 
ATOM   708  O OD1 . ASP   B 2 57  ? -29.581 10.972  -1.960  1.00 68.80  ? 66  ASP   B OD1 1 
ATOM   709  O OD2 . ASP   B 2 57  ? -31.513 9.926   -1.738  1.00 70.20  ? 66  ASP   B OD2 1 
ATOM   710  N N   . PRO   B 2 58  ? -26.704 7.107   -3.004  1.00 56.31  ? 67  PRO   B N   1 
ATOM   711  C CA  . PRO   B 2 58  ? -26.022 5.803   -3.028  1.00 54.74  ? 67  PRO   B CA  1 
ATOM   712  C C   . PRO   B 2 58  ? -26.717 4.768   -2.143  1.00 53.30  ? 67  PRO   B C   1 
ATOM   713  O O   . PRO   B 2 58  ? -27.255 5.111   -1.106  1.00 53.24  ? 67  PRO   B O   1 
ATOM   714  C CB  . PRO   B 2 58  ? -24.611 6.130   -2.538  1.00 55.74  ? 67  PRO   B CB  1 
ATOM   715  C CG  . PRO   B 2 58  ? -24.770 7.362   -1.712  1.00 56.54  ? 67  PRO   B CG  1 
ATOM   716  C CD  . PRO   B 2 58  ? -25.863 8.152   -2.386  1.00 55.61  ? 67  PRO   B CD  1 
ATOM   717  N N   . TYR   B 2 59  ? -26.734 3.508   -2.572  1.00 51.68  ? 68  TYR   B N   1 
ATOM   718  C CA  . TYR   B 2 59  ? -27.391 2.448   -1.825  1.00 49.74  ? 68  TYR   B CA  1 
ATOM   719  C C   . TYR   B 2 59  ? -26.371 1.426   -1.372  1.00 49.95  ? 68  TYR   B C   1 
ATOM   720  O O   . TYR   B 2 59  ? -26.399 1.007   -0.234  1.00 50.00  ? 68  TYR   B O   1 
ATOM   721  C CB  . TYR   B 2 59  ? -28.495 1.823   -2.682  1.00 47.95  ? 68  TYR   B CB  1 
ATOM   722  C CG  . TYR   B 2 59  ? -29.245 0.674   -2.048  1.00 46.16  ? 68  TYR   B CG  1 
ATOM   723  C CD1 . TYR   B 2 59  ? -28.708 -0.607  -2.032  1.00 45.93  ? 68  TYR   B CD1 1 
ATOM   724  C CD2 . TYR   B 2 59  ? -30.543 0.837   -1.593  1.00 45.49  ? 68  TYR   B CD2 1 
ATOM   725  C CE1 . TYR   B 2 59  ? -29.403 -1.672  -1.487  1.00 45.79  ? 68  TYR   B CE1 1 
ATOM   726  C CE2 . TYR   B 2 59  ? -31.256 -0.226  -1.062  1.00 45.67  ? 68  TYR   B CE2 1 
ATOM   727  C CZ  . TYR   B 2 59  ? -30.681 -1.482  -1.015  1.00 46.40  ? 68  TYR   B CZ  1 
ATOM   728  O OH  . TYR   B 2 59  ? -31.396 -2.552  -0.544  1.00 47.70  ? 68  TYR   B OH  1 
ATOM   729  N N   . TRP   B 2 60  ? -25.510 0.985   -2.265  1.00 50.14  ? 69  TRP   B N   1 
ATOM   730  C CA  . TRP   B 2 60  ? -24.452 0.029   -1.946  1.00 50.97  ? 69  TRP   B CA  1 
ATOM   731  C C   . TRP   B 2 60  ? -23.150 0.529   -2.627  1.00 50.19  ? 69  TRP   B C   1 
ATOM   732  O O   . TRP   B 2 60  ? -23.213 1.273   -3.591  1.00 49.96  ? 69  TRP   B O   1 
ATOM   733  C CB  . TRP   B 2 60  ? -24.844 -1.394  -2.410  1.00 51.58  ? 69  TRP   B CB  1 
ATOM   734  C CG  . TRP   B 2 60  ? -23.710 -2.375  -2.377  1.00 52.43  ? 69  TRP   B CG  1 
ATOM   735  C CD1 . TRP   B 2 60  ? -23.226 -3.035  -1.280  1.00 53.31  ? 69  TRP   B CD1 1 
ATOM   736  C CD2 . TRP   B 2 60  ? -22.812 -2.673  -3.456  1.00 51.97  ? 69  TRP   B CD2 1 
ATOM   737  N NE1 . TRP   B 2 60  ? -22.118 -3.773  -1.629  1.00 53.68  ? 69  TRP   B NE1 1 
ATOM   738  C CE2 . TRP   B 2 60  ? -21.833 -3.554  -2.956  1.00 52.75  ? 69  TRP   B CE2 1 
ATOM   739  C CE3 . TRP   B 2 60  ? -22.726 -2.257  -4.794  1.00 52.57  ? 69  TRP   B CE3 1 
ATOM   740  C CZ2 . TRP   B 2 60  ? -20.803 -4.052  -3.755  1.00 53.35  ? 69  TRP   B CZ2 1 
ATOM   741  C CZ3 . TRP   B 2 60  ? -21.722 -2.769  -5.588  1.00 53.15  ? 69  TRP   B CZ3 1 
ATOM   742  C CH2 . TRP   B 2 60  ? -20.765 -3.644  -5.066  1.00 53.44  ? 69  TRP   B CH2 1 
ATOM   743  N N   . GLY   B 2 61  ? -21.999 0.164   -2.090  1.00 49.94  ? 70  GLY   B N   1 
ATOM   744  C CA  . GLY   B 2 61  ? -20.713 0.589   -2.630  1.00 50.46  ? 70  GLY   B CA  1 
ATOM   745  C C   . GLY   B 2 61  ? -19.550 -0.174  -2.038  1.00 51.00  ? 70  GLY   B C   1 
ATOM   746  O O   . GLY   B 2 61  ? -19.674 -0.709  -0.946  1.00 51.70  ? 70  GLY   B O   1 
ATOM   747  N N   . ASP   B 2 62  ? -18.411 -0.231  -2.734  1.00 51.28  ? 71  ASP   B N   1 
ATOM   748  C CA  . ASP   B 2 62  ? -17.243 -0.970  -2.235  1.00 51.59  ? 71  ASP   B CA  1 
ATOM   749  C C   . ASP   B 2 62  ? -16.009 -0.467  -2.978  1.00 50.94  ? 71  ASP   B C   1 
ATOM   750  O O   . ASP   B 2 62  ? -15.941 -0.610  -4.192  1.00 49.79  ? 71  ASP   B O   1 
ATOM   751  C CB  . ASP   B 2 62  ? -17.427 -2.477  -2.515  1.00 53.96  ? 71  ASP   B CB  1 
ATOM   752  C CG  . ASP   B 2 62  ? -16.515 -3.391  -1.731  1.00 59.34  ? 71  ASP   B CG  1 
ATOM   753  O OD1 . ASP   B 2 62  ? -15.283 -3.304  -1.915  1.00 59.52  ? 71  ASP   B OD1 1 
ATOM   754  O OD2 . ASP   B 2 62  ? -17.035 -4.211  -0.946  1.00 62.70  ? 71  ASP   B OD2 1 
ATOM   755  N N   . VAL   B 2 63  ? -15.034 0.102   -2.253  1.00 50.82  ? 72  VAL   B N   1 
ATOM   756  C CA  . VAL   B 2 63  ? -13.799 0.628   -2.834  1.00 51.31  ? 72  VAL   B CA  1 
ATOM   757  C C   . VAL   B 2 63  ? -12.936 -0.474  -3.468  1.00 51.74  ? 72  VAL   B C   1 
ATOM   758  O O   . VAL   B 2 63  ? -12.277 -0.206  -4.466  1.00 51.94  ? 72  VAL   B O   1 
ATOM   759  C CB  . VAL   B 2 63  ? -13.016 1.479   -1.789  1.00 52.12  ? 72  VAL   B CB  1 
ATOM   760  C CG1 . VAL   B 2 63  ? -11.538 1.632   -2.138  1.00 52.65  ? 72  VAL   B CG1 1 
ATOM   761  C CG2 . VAL   B 2 63  ? -13.656 2.842   -1.617  1.00 52.63  ? 72  VAL   B CG2 1 
ATOM   762  N N   . LYS   B 2 64  ? -12.946 -1.700  -2.920  1.00 52.20  ? 73  LYS   B N   1 
ATOM   763  C CA  . LYS   B 2 64  ? -12.112 -2.771  -3.459  1.00 53.13  ? 73  LYS   B CA  1 
ATOM   764  C C   . LYS   B 2 64  ? -12.653 -3.288  -4.780  1.00 53.41  ? 73  LYS   B C   1 
ATOM   765  O O   . LYS   B 2 64  ? -11.935 -3.258  -5.778  1.00 54.07  ? 73  LYS   B O   1 
ATOM   766  C CB  . LYS   B 2 64  ? -11.855 -3.892  -2.443  1.00 55.73  ? 73  LYS   B CB  1 
ATOM   767  C CG  . LYS   B 2 64  ? -10.759 -4.819  -2.943  1.00 60.74  ? 73  LYS   B CG  1 
ATOM   768  C CD  . LYS   B 2 64  ? -10.301 -5.782  -1.879  1.00 64.98  ? 73  LYS   B CD  1 
ATOM   769  C CE  . LYS   B 2 64  ? -9.461  -6.840  -2.522  1.00 68.79  ? 73  LYS   B CE  1 
ATOM   770  N NZ  . LYS   B 2 64  ? -9.154  -7.928  -1.575  1.00 70.94  ? 73  LYS   B NZ  1 
ATOM   771  N N   . GLN   B 2 65  ? -13.940 -3.644  -4.829  1.00 52.69  ? 74  GLN   B N   1 
ATOM   772  C CA  . GLN   B 2 65  ? -14.580 -4.014  -6.091  1.00 52.06  ? 74  GLN   B CA  1 
ATOM   773  C C   . GLN   B 2 65  ? -14.630 -2.821  -7.071  1.00 51.10  ? 74  GLN   B C   1 
ATOM   774  O O   . GLN   B 2 65  ? -14.701 -3.029  -8.285  1.00 50.75  ? 74  GLN   B O   1 
ATOM   775  C CB  . GLN   B 2 65  ? -16.009 -4.513  -5.842  1.00 53.63  ? 74  GLN   B CB  1 
ATOM   776  C CG  . GLN   B 2 65  ? -16.088 -5.785  -5.005  1.00 56.55  ? 74  GLN   B CG  1 
ATOM   777  C CD  . GLN   B 2 65  ? -17.522 -6.250  -4.847  1.00 61.74  ? 74  GLN   B CD  1 
ATOM   778  O OE1 . GLN   B 2 65  ? -18.294 -6.338  -5.826  1.00 62.92  ? 74  GLN   B OE1 1 
ATOM   779  N NE2 . GLN   B 2 65  ? -17.909 -6.564  -3.604  1.00 62.35  ? 74  GLN   B NE2 1 
ATOM   780  N N   . ASP   B 2 66  ? -14.577 -1.576  -6.542  1.00 49.58  ? 75  ASP   B N   1 
ATOM   781  C CA  . ASP   B 2 66  ? -14.645 -0.322  -7.291  1.00 48.69  ? 75  ASP   B CA  1 
ATOM   782  C C   . ASP   B 2 66  ? -15.997 -0.170  -7.955  1.00 48.16  ? 75  ASP   B C   1 
ATOM   783  O O   . ASP   B 2 66  ? -16.071 0.254   -9.110  1.00 48.03  ? 75  ASP   B O   1 
ATOM   784  C CB  . ASP   B 2 66  ? -13.492 -0.158  -8.315  1.00 48.91  ? 75  ASP   B CB  1 
ATOM   785  C CG  . ASP   B 2 66  ? -13.365 1.267   -8.820  1.00 50.75  ? 75  ASP   B CG  1 
ATOM   786  O OD1 . ASP   B 2 66  ? -13.734 2.194   -8.074  1.00 51.28  ? 75  ASP   B OD1 1 
ATOM   787  O OD2 . ASP   B 2 66  ? -12.915 1.454   -9.953  1.00 52.25  ? 75  ASP   B OD2 1 
ATOM   788  N N   . LEU   B 2 67  ? -17.084 -0.516  -7.243  1.00 47.37  ? 76  LEU   B N   1 
ATOM   789  C CA  . LEU   B 2 67  ? -18.428 -0.387  -7.835  1.00 47.04  ? 76  LEU   B CA  1 
ATOM   790  C C   . LEU   B 2 67  ? -19.387 0.321   -6.882  1.00 46.51  ? 76  LEU   B C   1 
ATOM   791  O O   . LEU   B 2 67  ? -19.156 0.319   -5.681  1.00 46.06  ? 76  LEU   B O   1 
ATOM   792  C CB  . LEU   B 2 67  ? -18.994 -1.756  -8.220  1.00 47.01  ? 76  LEU   B CB  1 
ATOM   793  C CG  . LEU   B 2 67  ? -18.253 -2.549  -9.270  1.00 47.70  ? 76  LEU   B CG  1 
ATOM   794  C CD1 . LEU   B 2 67  ? -18.788 -3.935  -9.338  1.00 47.96  ? 76  LEU   B CD1 1 
ATOM   795  C CD2 . LEU   B 2 67  ? -18.349 -1.876  -10.678 1.00 48.24  ? 76  LEU   B CD2 1 
ATOM   796  N N   . VAL   B 2 68  ? -20.458 0.949   -7.416  1.00 46.05  ? 77  VAL   B N   1 
ATOM   797  C CA  . VAL   B 2 68  ? -21.426 1.656   -6.585  1.00 46.48  ? 77  VAL   B CA  1 
ATOM   798  C C   . VAL   B 2 68  ? -22.808 1.701   -7.257  1.00 47.09  ? 77  VAL   B C   1 
ATOM   799  O O   . VAL   B 2 68  ? -22.926 2.053   -8.416  1.00 46.89  ? 77  VAL   B O   1 
ATOM   800  C CB  . VAL   B 2 68  ? -20.912 3.057   -6.132  1.00 46.80  ? 77  VAL   B CB  1 
ATOM   801  C CG1 . VAL   B 2 68  ? -20.504 3.917   -7.311  1.00 47.86  ? 77  VAL   B CG1 1 
ATOM   802  C CG2 . VAL   B 2 68  ? -21.917 3.784   -5.249  1.00 47.01  ? 77  VAL   B CG2 1 
ATOM   803  N N   . SER   B 2 69  ? -23.860 1.351   -6.509  1.00 47.63  ? 78  SER   B N   1 
ATOM   804  C CA  . SER   B 2 69  ? -25.221 1.390   -7.032  1.00 47.28  ? 78  SER   B CA  1 
ATOM   805  C C   . SER   B 2 69  ? -26.003 2.512   -6.317  1.00 47.07  ? 78  SER   B C   1 
ATOM   806  O O   . SER   B 2 69  ? -25.699 2.854   -5.176  1.00 48.06  ? 78  SER   B O   1 
ATOM   807  C CB  . SER   B 2 69  ? -25.902 0.028   -6.881  1.00 46.70  ? 78  SER   B CB  1 
ATOM   808  O OG  . SER   B 2 69  ? -26.329 -0.198  -5.549  1.00 44.79  ? 78  SER   B OG  1 
ATOM   809  N N   . TYR   B 2 70  ? -26.988 3.089   -7.007  1.00 45.99  ? 79  TYR   B N   1 
ATOM   810  C CA  . TYR   B 2 70  ? -27.822 4.196   -6.547  1.00 45.45  ? 79  TYR   B CA  1 
ATOM   811  C C   . TYR   B 2 70  ? -29.281 3.782   -6.662  1.00 46.51  ? 79  TYR   B C   1 
ATOM   812  O O   . TYR   B 2 70  ? -29.660 3.150   -7.649  1.00 46.24  ? 79  TYR   B O   1 
ATOM   813  C CB  . TYR   B 2 70  ? -27.612 5.442   -7.449  1.00 44.38  ? 79  TYR   B CB  1 
ATOM   814  C CG  . TYR   B 2 70  ? -26.281 6.122   -7.228  1.00 42.74  ? 79  TYR   B CG  1 
ATOM   815  C CD1 . TYR   B 2 70  ? -25.139 5.691   -7.891  1.00 41.67  ? 79  TYR   B CD1 1 
ATOM   816  C CD2 . TYR   B 2 70  ? -26.144 7.132   -6.284  1.00 42.17  ? 79  TYR   B CD2 1 
ATOM   817  C CE1 . TYR   B 2 70  ? -23.896 6.250   -7.624  1.00 41.99  ? 79  TYR   B CE1 1 
ATOM   818  C CE2 . TYR   B 2 70  ? -24.908 7.702   -6.008  1.00 42.24  ? 79  TYR   B CE2 1 
ATOM   819  C CZ  . TYR   B 2 70  ? -23.787 7.270   -6.693  1.00 43.06  ? 79  TYR   B CZ  1 
ATOM   820  O OH  . TYR   B 2 70  ? -22.568 7.834   -6.425  1.00 44.43  ? 79  TYR   B OH  1 
ATOM   821  N N   . CYS   B 2 71  ? -30.099 4.159   -5.656  1.00 46.38  ? 80  CYS   B N   1 
ATOM   822  C CA  . CYS   B 2 71  ? -31.545 3.915   -5.572  1.00 47.75  ? 80  CYS   B CA  1 
ATOM   823  C C   . CYS   B 2 71  ? -31.925 2.488   -5.202  1.00 47.06  ? 80  CYS   B C   1 
ATOM   824  O O   . CYS   B 2 71  ? -33.008 2.277   -4.635  1.00 46.86  ? 80  CYS   B O   1 
ATOM   825  C CB  . CYS   B 2 71  ? -32.275 4.373   -6.826  1.00 50.79  ? 80  CYS   B CB  1 
ATOM   826  S SG  . CYS   B 2 71  ? -32.007 6.117   -7.222  1.00 61.63  ? 80  CYS   B SG  1 
ATOM   827  N N   . GLY   B 2 72  ? -31.052 1.533   -5.490  1.00 46.19  ? 81  GLY   B N   1 
ATOM   828  C CA  . GLY   B 2 72  ? -31.342 0.148   -5.162  1.00 46.63  ? 81  GLY   B CA  1 
ATOM   829  C C   . GLY   B 2 72  ? -30.138 -0.750  -5.233  1.00 46.78  ? 81  GLY   B C   1 
ATOM   830  O O   . GLY   B 2 72  ? -29.030 -0.306  -5.544  1.00 46.46  ? 81  GLY   B O   1 
ATOM   831  N N   . PRO   B 2 73  ? -30.344 -2.038  -4.919  1.00 46.67  ? 82  PRO   B N   1 
ATOM   832  C CA  . PRO   B 2 73  ? -29.213 -2.980  -4.966  1.00 46.85  ? 82  PRO   B CA  1 
ATOM   833  C C   . PRO   B 2 73  ? -28.682 -3.206  -6.384  1.00 47.71  ? 82  PRO   B C   1 
ATOM   834  O O   . PRO   B 2 73  ? -29.395 -2.971  -7.357  1.00 46.95  ? 82  PRO   B O   1 
ATOM   835  C CB  . PRO   B 2 73  ? -29.774 -4.262  -4.338  1.00 47.40  ? 82  PRO   B CB  1 
ATOM   836  C CG  . PRO   B 2 73  ? -31.275 -4.129  -4.407  1.00 47.38  ? 82  PRO   B CG  1 
ATOM   837  C CD  . PRO   B 2 73  ? -31.617 -2.680  -4.520  1.00 45.83  ? 82  PRO   B CD  1 
ATOM   838  N N   . TRP   B 2 74  ? -27.415 -3.652  -6.507  1.00 48.60  ? 83  TRP   B N   1 
ATOM   839  C CA  . TRP   B 2 74  ? -26.783 -3.925  -7.801  1.00 48.96  ? 83  TRP   B CA  1 
ATOM   840  C C   . TRP   B 2 74  ? -27.622 -4.949  -8.602  1.00 51.23  ? 83  TRP   B C   1 
ATOM   841  O O   . TRP   B 2 74  ? -27.949 -6.004  -8.061  1.00 51.68  ? 83  TRP   B O   1 
ATOM   842  C CB  . TRP   B 2 74  ? -25.339 -4.411  -7.584  1.00 48.31  ? 83  TRP   B CB  1 
ATOM   843  C CG  . TRP   B 2 74  ? -24.539 -4.521  -8.847  1.00 48.25  ? 83  TRP   B CG  1 
ATOM   844  C CD1 . TRP   B 2 74  ? -24.421 -5.617  -9.645  1.00 48.48  ? 83  TRP   B CD1 1 
ATOM   845  C CD2 . TRP   B 2 74  ? -23.704 -3.507  -9.429  1.00 48.26  ? 83  TRP   B CD2 1 
ATOM   846  N NE1 . TRP   B 2 74  ? -23.578 -5.349  -10.694 1.00 49.26  ? 83  TRP   B NE1 1 
ATOM   847  C CE2 . TRP   B 2 74  ? -23.159 -4.043  -10.611 1.00 48.84  ? 83  TRP   B CE2 1 
ATOM   848  C CE3 . TRP   B 2 74  ? -23.385 -2.184  -9.076  1.00 48.54  ? 83  TRP   B CE3 1 
ATOM   849  C CZ2 . TRP   B 2 74  ? -22.297 -3.317  -11.435 1.00 49.22  ? 83  TRP   B CZ2 1 
ATOM   850  C CZ3 . TRP   B 2 74  ? -22.543 -1.462  -9.898  1.00 49.23  ? 83  TRP   B CZ3 1 
ATOM   851  C CH2 . TRP   B 2 74  ? -22.020 -2.023  -11.074 1.00 49.39  ? 83  TRP   B CH2 1 
ATOM   852  N N   . LYS   B 2 75  ? -28.023 -4.610  -9.868  1.00 52.20  ? 84  LYS   B N   1 
ATOM   853  C CA  . LYS   B 2 75  ? -28.914 -5.447  -10.685 1.00 53.59  ? 84  LYS   B CA  1 
ATOM   854  C C   . LYS   B 2 75  ? -28.239 -6.217  -11.821 1.00 55.17  ? 84  LYS   B C   1 
ATOM   855  O O   . LYS   B 2 75  ? -28.860 -7.112  -12.393 1.00 54.90  ? 84  LYS   B O   1 
ATOM   856  C CB  . LYS   B 2 75  ? -30.016 -4.579  -11.328 1.00 54.50  ? 84  LYS   B CB  1 
ATOM   857  C CG  . LYS   B 2 75  ? -30.836 -3.749  -10.376 1.00 56.92  ? 84  LYS   B CG  1 
ATOM   858  C CD  . LYS   B 2 75  ? -31.903 -4.581  -9.724  1.00 60.92  ? 84  LYS   B CD  1 
ATOM   859  C CE  . LYS   B 2 75  ? -32.670 -3.795  -8.699  1.00 63.89  ? 84  LYS   B CE  1 
ATOM   860  N NZ  . LYS   B 2 75  ? -33.925 -4.484  -8.316  1.00 65.52  ? 84  LYS   B NZ  1 
ATOM   861  N N   . LEU   B 2 76  ? -27.023 -5.819  -12.210 1.00 56.18  ? 85  LEU   B N   1 
ATOM   862  C CA  . LEU   B 2 76  ? -26.302 -6.420  -13.329 1.00 57.18  ? 85  LEU   B CA  1 
ATOM   863  C C   . LEU   B 2 76  ? -25.640 -7.716  -12.886 1.00 58.72  ? 85  LEU   B C   1 
ATOM   864  O O   . LEU   B 2 76  ? -24.849 -7.712  -11.945 1.00 58.86  ? 85  LEU   B O   1 
ATOM   865  C CB  . LEU   B 2 76  ? -25.270 -5.424  -13.897 1.00 57.05  ? 85  LEU   B CB  1 
ATOM   866  C CG  . LEU   B 2 76  ? -25.782 -4.000  -14.154 1.00 57.86  ? 85  LEU   B CG  1 
ATOM   867  C CD1 . LEU   B 2 76  ? -24.693 -3.120  -14.697 1.00 57.97  ? 85  LEU   B CD1 1 
ATOM   868  C CD2 . LEU   B 2 76  ? -26.919 -3.996  -15.137 1.00 58.72  ? 85  LEU   B CD2 1 
ATOM   869  N N   . ASP   B 2 77  ? -25.987 -8.834  -13.535 1.00 59.53  ? 86  ASP   B N   1 
ATOM   870  C CA  . ASP   B 2 77  ? -25.479 -10.142 -13.122 1.00 60.91  ? 86  ASP   B CA  1 
ATOM   871  C C   . ASP   B 2 77  ? -25.039 -11.062 -14.271 1.00 61.46  ? 86  ASP   B C   1 
ATOM   872  O O   . ASP   B 2 77  ? -25.015 -12.276 -14.089 1.00 61.95  ? 86  ASP   B O   1 
ATOM   873  C CB  . ASP   B 2 77  ? -26.525 -10.865 -12.249 1.00 63.10  ? 86  ASP   B CB  1 
ATOM   874  C CG  . ASP   B 2 77  ? -27.829 -11.195 -12.969 1.00 69.47  ? 86  ASP   B CG  1 
ATOM   875  O OD1 . ASP   B 2 77  ? -28.107 -10.572 -14.024 1.00 71.36  ? 86  ASP   B OD1 1 
ATOM   876  O OD2 . ASP   B 2 77  ? -28.572 -12.068 -12.478 1.00 71.97  ? 86  ASP   B OD2 1 
ATOM   877  N N   . ALA   B 2 78  ? -24.686 -10.510 -15.424 1.00 61.66  ? 87  ALA   B N   1 
ATOM   878  C CA  . ALA   B 2 78  ? -24.238 -11.325 -16.558 1.00 62.50  ? 87  ALA   B CA  1 
ATOM   879  C C   . ALA   B 2 78  ? -22.722 -11.498 -16.534 1.00 63.87  ? 87  ALA   B C   1 
ATOM   880  O O   . ALA   B 2 78  ? -22.014 -10.641 -16.009 1.00 64.42  ? 87  ALA   B O   1 
ATOM   881  C CB  . ALA   B 2 78  ? -24.692 -10.715 -17.876 1.00 61.95  ? 87  ALA   B CB  1 
ATOM   882  N N   . ALA   B 2 79  ? -22.217 -12.611 -17.075 1.00 64.50  ? 88  ALA   B N   1 
ATOM   883  C CA  . ALA   B 2 79  ? -20.782 -12.859 -17.048 1.00 65.78  ? 88  ALA   B CA  1 
ATOM   884  C C   . ALA   B 2 79  ? -20.236 -13.221 -18.402 1.00 66.96  ? 88  ALA   B C   1 
ATOM   885  O O   . ALA   B 2 79  ? -20.891 -13.934 -19.152 1.00 67.15  ? 88  ALA   B O   1 
ATOM   886  C CB  . ALA   B 2 79  ? -20.472 -13.966 -16.052 1.00 66.09  ? 88  ALA   B CB  1 
ATOM   887  N N   . TRP   B 2 80  ? -19.006 -12.774 -18.699 1.00 67.71  ? 89  TRP   B N   1 
ATOM   888  C CA  . TRP   B 2 80  ? -18.287 -13.130 -19.918 1.00 69.32  ? 89  TRP   B CA  1 
ATOM   889  C C   . TRP   B 2 80  ? -18.067 -14.644 -19.913 1.00 71.26  ? 89  TRP   B C   1 
ATOM   890  O O   . TRP   B 2 80  ? -17.698 -15.188 -18.875 1.00 71.69  ? 89  TRP   B O   1 
ATOM   891  C CB  . TRP   B 2 80  ? -16.932 -12.414 -19.953 1.00 69.24  ? 89  TRP   B CB  1 
ATOM   892  C CG  . TRP   B 2 80  ? -16.084 -12.773 -21.137 1.00 69.77  ? 89  TRP   B CG  1 
ATOM   893  C CD1 . TRP   B 2 80  ? -16.449 -12.738 -22.449 1.00 70.91  ? 89  TRP   B CD1 1 
ATOM   894  C CD2 . TRP   B 2 80  ? -14.704 -13.158 -21.113 1.00 69.72  ? 89  TRP   B CD2 1 
ATOM   895  N NE1 . TRP   B 2 80  ? -15.392 -13.120 -23.245 1.00 71.45  ? 89  TRP   B NE1 1 
ATOM   896  C CE2 . TRP   B 2 80  ? -14.301 -13.365 -22.448 1.00 70.62  ? 89  TRP   B CE2 1 
ATOM   897  C CE3 . TRP   B 2 80  ? -13.767 -13.348 -20.091 1.00 69.78  ? 89  TRP   B CE3 1 
ATOM   898  C CZ2 . TRP   B 2 80  ? -13.008 -13.766 -22.784 1.00 70.80  ? 89  TRP   B CZ2 1 
ATOM   899  C CZ3 . TRP   B 2 80  ? -12.490 -13.753 -20.429 1.00 70.62  ? 89  TRP   B CZ3 1 
ATOM   900  C CH2 . TRP   B 2 80  ? -12.116 -13.934 -21.764 1.00 70.67  ? 89  TRP   B CH2 1 
ATOM   901  N N   . ASP   B 2 81  ? -18.369 -15.331 -21.025 1.00 72.62  ? 90  ASP   B N   1 
ATOM   902  C CA  . ASP   B 2 81  ? -18.244 -16.793 -21.080 1.00 74.40  ? 90  ASP   B CA  1 
ATOM   903  C C   . ASP   B 2 81  ? -16.800 -17.319 -21.246 1.00 75.40  ? 90  ASP   B C   1 
ATOM   904  O O   . ASP   B 2 81  ? -16.606 -18.525 -21.414 1.00 75.32  ? 90  ASP   B O   1 
ATOM   905  C CB  . ASP   B 2 81  ? -19.164 -17.385 -22.167 1.00 76.73  ? 90  ASP   B CB  1 
ATOM   906  C CG  . ASP   B 2 81  ? -18.829 -16.986 -23.589 1.00 83.17  ? 90  ASP   B CG  1 
ATOM   907  O OD1 . ASP   B 2 81  ? -17.977 -16.087 -23.771 1.00 84.83  ? 90  ASP   B OD1 1 
ATOM   908  O OD2 . ASP   B 2 81  ? -19.423 -17.572 -24.533 1.00 85.42  ? 90  ASP   B OD2 1 
ATOM   909  N N   . GLY   B 2 82  ? -15.821 -16.418 -21.212 1.00 75.79  ? 91  GLY   B N   1 
ATOM   910  C CA  . GLY   B 2 82  ? -14.413 -16.754 -21.374 1.00 76.42  ? 91  GLY   B CA  1 
ATOM   911  C C   . GLY   B 2 82  ? -14.048 -17.197 -22.777 1.00 76.74  ? 91  GLY   B C   1 
ATOM   912  O O   . GLY   B 2 82  ? -12.993 -17.805 -22.978 1.00 77.03  ? 91  GLY   B O   1 
ATOM   913  N N   . LEU   B 2 83  ? -14.915 -16.915 -23.766 1.00 76.58  ? 92  LEU   B N   1 
ATOM   914  C CA  . LEU   B 2 83  ? -14.698 -17.375 -25.124 1.00 76.80  ? 92  LEU   B CA  1 
ATOM   915  C C   . LEU   B 2 83  ? -15.094 -16.379 -26.216 1.00 76.61  ? 92  LEU   B C   1 
ATOM   916  O O   . LEU   B 2 83  ? -14.328 -16.175 -27.156 1.00 76.90  ? 92  LEU   B O   1 
ATOM   917  C CB  . LEU   B 2 83  ? -15.482 -18.686 -25.328 1.00 77.61  ? 92  LEU   B CB  1 
ATOM   918  C CG  . LEU   B 2 83  ? -14.768 -19.968 -24.916 1.00 79.87  ? 92  LEU   B CG  1 
ATOM   919  C CD1 . LEU   B 2 83  ? -15.705 -20.914 -24.193 1.00 80.90  ? 92  LEU   B CD1 1 
ATOM   920  C CD2 . LEU   B 2 83  ? -14.161 -20.638 -26.101 1.00 79.57  ? 92  LEU   B CD2 1 
ATOM   921  N N   . SER   B 2 84  ? -16.310 -15.810 -26.137 1.00 75.83  ? 93  SER   B N   1 
ATOM   922  C CA  . SER   B 2 84  ? -16.849 -14.942 -27.194 1.00 75.23  ? 93  SER   B CA  1 
ATOM   923  C C   . SER   B 2 84  ? -16.305 -13.530 -27.189 1.00 74.48  ? 93  SER   B C   1 
ATOM   924  O O   . SER   B 2 84  ? -15.833 -13.047 -26.167 1.00 74.97  ? 93  SER   B O   1 
ATOM   925  C CB  . SER   B 2 84  ? -18.376 -14.866 -27.115 1.00 76.46  ? 93  SER   B CB  1 
ATOM   926  O OG  . SER   B 2 84  ? -19.008 -16.020 -26.588 1.00 79.26  ? 93  SER   B OG  1 
ATOM   927  N N   . GLU   B 2 85  ? -16.405 -12.850 -28.334 1.00 73.58  ? 94  GLU   B N   1 
ATOM   928  C CA  . GLU   B 2 85  ? -16.045 -11.448 -28.415 1.00 73.00  ? 94  GLU   B CA  1 
ATOM   929  C C   . GLU   B 2 85  ? -17.133 -10.647 -27.673 1.00 71.93  ? 94  GLU   B C   1 
ATOM   930  O O   . GLU   B 2 85  ? -18.278 -11.079 -27.534 1.00 72.30  ? 94  GLU   B O   1 
ATOM   931  C CB  . GLU   B 2 85  ? -15.932 -10.978 -29.877 1.00 74.80  ? 94  GLU   B CB  1 
ATOM   932  C CG  . GLU   B 2 85  ? -14.799 -11.637 -30.646 1.00 77.96  ? 94  GLU   B CG  1 
ATOM   933  C CD  . GLU   B 2 85  ? -14.278 -10.808 -31.803 1.00 79.30  ? 94  GLU   B CD  1 
ATOM   934  O OE1 . GLU   B 2 85  ? -15.100 -10.145 -32.474 1.00 79.36  ? 94  GLU   B OE1 1 
ATOM   935  O OE2 . GLU   B 2 85  ? -13.048 -10.810 -32.035 1.00 79.19  ? 94  GLU   B OE2 1 
ATOM   936  N N   . VAL   B 2 86  ? -16.744 -9.510  -27.139 1.00 70.35  ? 95  VAL   B N   1 
ATOM   937  C CA  . VAL   B 2 86  ? -17.628 -8.625  -26.391 1.00 68.77  ? 95  VAL   B CA  1 
ATOM   938  C C   . VAL   B 2 86  ? -17.619 -7.234  -27.072 1.00 67.29  ? 95  VAL   B C   1 
ATOM   939  O O   . VAL   B 2 86  ? -16.894 -7.030  -28.053 1.00 67.58  ? 95  VAL   B O   1 
ATOM   940  C CB  . VAL   B 2 86  ? -17.166 -8.552  -24.911 1.00 68.88  ? 95  VAL   B CB  1 
ATOM   941  C CG1 . VAL   B 2 86  ? -17.021 -9.943  -24.307 1.00 68.99  ? 95  VAL   B CG1 1 
ATOM   942  C CG2 . VAL   B 2 86  ? -15.870 -7.764  -24.797 1.00 69.33  ? 95  VAL   B CG2 1 
ATOM   943  N N   . GLN   B 2 87  ? -18.450 -6.294  -26.592 1.00 65.30  ? 96  GLN   B N   1 
ATOM   944  C CA  . GLN   B 2 87  ? -18.474 -4.948  -27.143 1.00 63.84  ? 96  GLN   B CA  1 
ATOM   945  C C   . GLN   B 2 87  ? -18.408 -3.915  -26.032 1.00 62.81  ? 96  GLN   B C   1 
ATOM   946  O O   . GLN   B 2 87  ? -19.169 -3.996  -25.072 1.00 63.22  ? 96  GLN   B O   1 
ATOM   947  C CB  . GLN   B 2 87  ? -19.706 -4.720  -28.039 1.00 64.19  ? 96  GLN   B CB  1 
ATOM   948  C CG  . GLN   B 2 87  ? -19.342 -4.711  -29.509 1.00 66.11  ? 96  GLN   B CG  1 
ATOM   949  C CD  . GLN   B 2 87  ? -20.552 -4.726  -30.415 1.00 68.15  ? 96  GLN   B CD  1 
ATOM   950  O OE1 . GLN   B 2 87  ? -21.613 -4.165  -30.108 1.00 67.39  ? 96  GLN   B OE1 1 
ATOM   951  N NE2 . GLN   B 2 87  ? -20.408 -5.372  -31.555 1.00 70.03  ? 96  GLN   B NE2 1 
ATOM   952  N N   . LEU   B 2 88  ? -17.456 -2.989  -26.123 1.00 61.16  ? 97  LEU   B N   1 
ATOM   953  C CA  . LEU   B 2 88  ? -17.362 -1.917  -25.151 1.00 60.02  ? 97  LEU   B CA  1 
ATOM   954  C C   . LEU   B 2 88  ? -18.250 -0.797  -25.693 1.00 60.22  ? 97  LEU   B C   1 
ATOM   955  O O   . LEU   B 2 88  ? -17.980 -0.305  -26.786 1.00 60.18  ? 97  LEU   B O   1 
ATOM   956  C CB  . LEU   B 2 88  ? -15.919 -1.406  -25.027 1.00 59.17  ? 97  LEU   B CB  1 
ATOM   957  C CG  . LEU   B 2 88  ? -15.757 -0.150  -24.149 1.00 59.40  ? 97  LEU   B CG  1 
ATOM   958  C CD1 . LEU   B 2 88  ? -16.201 -0.411  -22.732 1.00 59.01  ? 97  LEU   B CD1 1 
ATOM   959  C CD2 . LEU   B 2 88  ? -14.340 0.388   -24.183 1.00 59.58  ? 97  LEU   B CD2 1 
ATOM   960  N N   . LEU   B 2 89  ? -19.310 -0.406  -24.964 1.00 59.86  ? 98  LEU   B N   1 
ATOM   961  C CA  . LEU   B 2 89  ? -20.125 0.721   -25.397 1.00 60.03  ? 98  LEU   B CA  1 
ATOM   962  C C   . LEU   B 2 89  ? -19.417 1.923   -24.776 1.00 60.36  ? 98  LEU   B C   1 
ATOM   963  O O   . LEU   B 2 89  ? -19.715 2.319   -23.650 1.00 60.17  ? 98  LEU   B O   1 
ATOM   964  C CB  . LEU   B 2 89  ? -21.593 0.585   -24.946 1.00 60.21  ? 98  LEU   B CB  1 
ATOM   965  C CG  . LEU   B 2 89  ? -22.562 1.760   -25.248 1.00 61.93  ? 98  LEU   B CG  1 
ATOM   966  C CD1 . LEU   B 2 89  ? -22.398 2.305   -26.645 1.00 61.98  ? 98  LEU   B CD1 1 
ATOM   967  C CD2 . LEU   B 2 89  ? -23.995 1.347   -25.053 1.00 62.79  ? 98  LEU   B CD2 1 
ATOM   968  N N   . ALA   B 2 90  ? -18.372 2.408   -25.468 1.00 60.13  ? 99  ALA   B N   1 
ATOM   969  C CA  . ALA   B 2 90  ? -17.551 3.496   -24.952 1.00 59.65  ? 99  ALA   B CA  1 
ATOM   970  C C   . ALA   B 2 90  ? -18.206 4.831   -25.156 1.00 59.25  ? 99  ALA   B C   1 
ATOM   971  O O   . ALA   B 2 90  ? -18.498 5.196   -26.289 1.00 58.59  ? 99  ALA   B O   1 
ATOM   972  C CB  . ALA   B 2 90  ? -16.184 3.485   -25.618 1.00 59.51  ? 99  ALA   B CB  1 
ATOM   973  N N   . VAL   B 2 91  ? -18.392 5.586   -24.063 1.00 58.99  ? 100 VAL   B N   1 
ATOM   974  C CA  . VAL   B 2 91  ? -18.992 6.911   -24.106 1.00 59.39  ? 100 VAL   B CA  1 
ATOM   975  C C   . VAL   B 2 91  ? -17.908 7.901   -23.671 1.00 60.72  ? 100 VAL   B C   1 
ATOM   976  O O   . VAL   B 2 91  ? -17.756 8.184   -22.487 1.00 60.65  ? 100 VAL   B O   1 
ATOM   977  C CB  . VAL   B 2 91  ? -20.234 6.970   -23.177 1.00 59.03  ? 100 VAL   B CB  1 
ATOM   978  C CG1 . VAL   B 2 91  ? -20.918 8.329   -23.238 1.00 59.27  ? 100 VAL   B CG1 1 
ATOM   979  C CG2 . VAL   B 2 91  ? -21.217 5.853   -23.499 1.00 58.97  ? 100 VAL   B CG2 1 
ATOM   980  N N   . PRO   B 2 92  ? -17.119 8.420   -24.621 1.00 61.77  ? 101 PRO   B N   1 
ATOM   981  C CA  . PRO   B 2 92  ? -16.011 9.318   -24.250 1.00 62.78  ? 101 PRO   B CA  1 
ATOM   982  C C   . PRO   B 2 92  ? -16.424 10.769  -24.007 1.00 64.56  ? 101 PRO   B C   1 
ATOM   983  O O   . PRO   B 2 92  ? -17.411 11.229  -24.580 1.00 64.92  ? 101 PRO   B O   1 
ATOM   984  C CB  . PRO   B 2 92  ? -15.070 9.221   -25.469 1.00 62.43  ? 101 PRO   B CB  1 
ATOM   985  C CG  . PRO   B 2 92  ? -15.671 8.158   -26.374 1.00 62.30  ? 101 PRO   B CG  1 
ATOM   986  C CD  . PRO   B 2 92  ? -17.114 8.146   -26.070 1.00 60.78  ? 101 PRO   B CD  1 
ATOM   987  N N   . PRO   B 2 93  ? -15.623 11.535  -23.242 1.00 65.45  ? 102 PRO   B N   1 
ATOM   988  C CA  . PRO   B 2 93  ? -15.957 12.954  -23.027 1.00 66.26  ? 102 PRO   B CA  1 
ATOM   989  C C   . PRO   B 2 93  ? -16.096 13.762  -24.317 1.00 67.94  ? 102 PRO   B C   1 
ATOM   990  O O   . PRO   B 2 93  ? -15.233 13.720  -25.201 1.00 68.77  ? 102 PRO   B O   1 
ATOM   991  C CB  . PRO   B 2 93  ? -14.805 13.463  -22.149 1.00 66.58  ? 102 PRO   B CB  1 
ATOM   992  C CG  . PRO   B 2 93  ? -14.269 12.244  -21.475 1.00 66.64  ? 102 PRO   B CG  1 
ATOM   993  C CD  . PRO   B 2 93  ? -14.415 11.141  -22.489 1.00 65.08  ? 102 PRO   B CD  1 
ATOM   994  N N   . GLY   B 2 94  ? -17.231 14.441  -24.441 1.00 68.11  ? 103 GLY   B N   1 
ATOM   995  C CA  . GLY   B 2 94  ? -17.570 15.270  -25.589 1.00 68.22  ? 103 GLY   B CA  1 
ATOM   996  C C   . GLY   B 2 94  ? -17.913 14.526  -26.869 1.00 68.52  ? 103 GLY   B C   1 
ATOM   997  O O   . GLY   B 2 94  ? -18.354 15.135  -27.841 1.00 67.81  ? 103 GLY   B O   1 
ATOM   998  N N   . GLU   B 2 95  ? -17.709 13.212  -26.894 1.00 68.99  ? 104 GLU   B N   1 
ATOM   999  C CA  . GLU   B 2 95  ? -17.946 12.407  -28.085 1.00 69.74  ? 104 GLU   B CA  1 
ATOM   1000 C C   . GLU   B 2 95  ? -19.171 11.503  -27.949 1.00 70.88  ? 104 GLU   B C   1 
ATOM   1001 O O   . GLU   B 2 95  ? -19.549 11.128  -26.839 1.00 70.82  ? 104 GLU   B O   1 
ATOM   1002 C CB  . GLU   B 2 95  ? -16.696 11.573  -28.404 1.00 71.84  ? 104 GLU   B CB  1 
ATOM   1003 C CG  . GLU   B 2 95  ? -15.442 12.416  -28.566 1.00 76.66  ? 104 GLU   B CG  1 
ATOM   1004 C CD  . GLU   B 2 95  ? -14.194 11.666  -28.999 1.00 81.73  ? 104 GLU   B CD  1 
ATOM   1005 O OE1 . GLU   B 2 95  ? -14.260 10.423  -29.140 1.00 82.22  ? 104 GLU   B OE1 1 
ATOM   1006 O OE2 . GLU   B 2 95  ? -13.147 12.324  -29.197 1.00 83.08  ? 104 GLU   B OE2 1 
ATOM   1007 N N   . ARG   B 2 96  ? -19.772 11.134  -29.086 1.00 71.58  ? 105 ARG   B N   1 
ATOM   1008 C CA  . ARG   B 2 96  ? -20.962 10.289  -29.150 1.00 73.08  ? 105 ARG   B CA  1 
ATOM   1009 C C   . ARG   B 2 96  ? -20.639 8.845   -28.776 1.00 73.96  ? 105 ARG   B C   1 
ATOM   1010 O O   . ARG   B 2 96  ? -19.575 8.353   -29.150 1.00 74.77  ? 105 ARG   B O   1 
ATOM   1011 C CB  . ARG   B 2 96  ? -21.555 10.356  -30.574 1.00 75.53  ? 105 ARG   B CB  1 
ATOM   1012 C CG  . ARG   B 2 96  ? -22.729 9.419   -30.833 1.00 80.18  ? 105 ARG   B CG  1 
ATOM   1013 C CD  . ARG   B 2 96  ? -23.558 9.855   -32.024 1.00 84.78  ? 105 ARG   B CD  1 
ATOM   1014 N NE  . ARG   B 2 96  ? -22.880 9.617   -33.298 1.00 89.58  ? 105 ARG   B NE  1 
ATOM   1015 C CZ  . ARG   B 2 96  ? -22.422 10.579  -34.095 1.00 93.83  ? 105 ARG   B CZ  1 
ATOM   1016 N NH1 . ARG   B 2 96  ? -22.560 11.857  -33.755 1.00 94.01  ? 105 ARG   B NH1 1 
ATOM   1017 N NH2 . ARG   B 2 96  ? -21.836 10.272  -35.247 1.00 94.52  ? 105 ARG   B NH2 1 
ATOM   1018 N N   . ALA   B 2 97  ? -21.566 8.161   -28.066 1.00 73.83  ? 106 ALA   B N   1 
ATOM   1019 C CA  . ALA   B 2 97  ? -21.443 6.759   -27.661 1.00 74.36  ? 106 ALA   B CA  1 
ATOM   1020 C C   . ALA   B 2 97  ? -21.154 5.868   -28.864 1.00 74.79  ? 106 ALA   B C   1 
ATOM   1021 O O   . ALA   B 2 97  ? -21.749 6.064   -29.920 1.00 75.30  ? 106 ALA   B O   1 
ATOM   1022 C CB  . ALA   B 2 97  ? -22.722 6.306   -26.980 1.00 74.54  ? 106 ALA   B CB  1 
ATOM   1023 N N   . LYS   B 2 98  ? -20.240 4.905   -28.720 1.00 74.92  ? 107 LYS   B N   1 
ATOM   1024 C CA  . LYS   B 2 98  ? -19.838 4.072   -29.851 1.00 75.67  ? 107 LYS   B CA  1 
ATOM   1025 C C   . LYS   B 2 98  ? -19.413 2.652   -29.436 1.00 75.22  ? 107 LYS   B C   1 
ATOM   1026 O O   . LYS   B 2 98  ? -18.614 2.495   -28.523 1.00 75.42  ? 107 LYS   B O   1 
ATOM   1027 C CB  . LYS   B 2 98  ? -18.741 4.843   -30.603 1.00 78.85  ? 107 LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 2 98  ? -17.811 4.075   -31.525 1.00 84.64  ? 107 LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 2 98  ? -16.476 4.843   -31.658 1.00 89.77  ? 107 LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 2 98  ? -15.835 5.099   -30.296 1.00 93.02  ? 107 LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 2 98  ? -14.446 5.622   -30.397 1.00 95.28  ? 107 LYS   B NZ  1 
ATOM   1032 N N   . ASN   B 2 99  ? -19.978 1.618   -30.084 1.00 74.42  ? 108 ASN   B N   1 
ATOM   1033 C CA  . ASN   B 2 99  ? -19.670 0.220   -29.764 1.00 74.00  ? 108 ASN   B CA  1 
ATOM   1034 C C   . ASN   B 2 99  ? -18.363 -0.223  -30.409 1.00 73.50  ? 108 ASN   B C   1 
ATOM   1035 O O   . ASN   B 2 99  ? -18.183 -0.008  -31.598 1.00 73.62  ? 108 ASN   B O   1 
ATOM   1036 C CB  . ASN   B 2 99  ? -20.795 -0.711  -30.247 1.00 74.50  ? 108 ASN   B CB  1 
ATOM   1037 C CG  . ASN   B 2 99  ? -22.077 -0.613  -29.452 1.00 76.86  ? 108 ASN   B CG  1 
ATOM   1038 O OD1 . ASN   B 2 99  ? -22.728 0.427   -29.403 1.00 77.93  ? 108 ASN   B OD1 1 
ATOM   1039 N ND2 . ASN   B 2 99  ? -22.483 -1.703  -28.831 1.00 77.02  ? 108 ASN   B ND2 1 
ATOM   1040 N N   . ILE   B 2 100 ? -17.459 -0.834  -29.638 1.00 72.91  ? 109 ILE   B N   1 
ATOM   1041 C CA  . ILE   B 2 100 ? -16.184 -1.346  -30.139 1.00 72.84  ? 109 ILE   B CA  1 
ATOM   1042 C C   . ILE   B 2 100 ? -16.108 -2.822  -29.806 1.00 72.18  ? 109 ILE   B C   1 
ATOM   1043 O O   . ILE   B 2 100 ? -16.089 -3.167  -28.640 1.00 72.35  ? 109 ILE   B O   1 
ATOM   1044 C CB  . ILE   B 2 100 ? -14.972 -0.652  -29.490 1.00 73.75  ? 109 ILE   B CB  1 
ATOM   1045 C CG1 . ILE   B 2 100 ? -15.116 0.867   -29.460 1.00 74.59  ? 109 ILE   B CG1 1 
ATOM   1046 C CG2 . ILE   B 2 100 ? -13.687 -1.099  -30.193 1.00 74.55  ? 109 ILE   B CG2 1 
ATOM   1047 C CD1 . ILE   B 2 100 ? -15.123 1.504   -30.837 1.00 75.24  ? 109 ILE   B CD1 1 
ATOM   1048 N N   . GLN   B 2 101 ? -16.016 -3.683  -30.800 1.00 71.47  ? 110 GLN   B N   1 
ATOM   1049 C CA  . GLN   B 2 101 ? -15.943 -5.125  -30.583 1.00 71.06  ? 110 GLN   B CA  1 
ATOM   1050 C C   . GLN   B 2 101 ? -14.514 -5.567  -30.298 1.00 70.10  ? 110 GLN   B C   1 
ATOM   1051 O O   . GLN   B 2 101 ? -13.588 -5.135  -30.975 1.00 69.92  ? 110 GLN   B O   1 
ATOM   1052 C CB  . GLN   B 2 101 ? -16.505 -5.854  -31.812 1.00 73.61  ? 110 GLN   B CB  1 
ATOM   1053 C CG  . GLN   B 2 101 ? -16.562 -7.358  -31.642 1.00 76.89  ? 110 GLN   B CG  1 
ATOM   1054 C CD  . GLN   B 2 101 ? -17.608 -7.953  -32.532 1.00 79.45  ? 110 GLN   B CD  1 
ATOM   1055 O OE1 . GLN   B 2 101 ? -18.684 -7.384  -32.728 1.00 80.88  ? 110 GLN   B OE1 1 
ATOM   1056 N NE2 . GLN   B 2 101 ? -17.318 -9.125  -33.076 1.00 79.64  ? 110 GLN   B NE2 1 
ATOM   1057 N N   . THR   B 2 102 ? -14.317 -6.405  -29.268 1.00 69.60  ? 111 THR   B N   1 
ATOM   1058 C CA  . THR   B 2 102 ? -12.987 -6.886  -28.922 1.00 69.88  ? 111 THR   B CA  1 
ATOM   1059 C C   . THR   B 2 102 ? -13.067 -8.271  -28.293 1.00 70.65  ? 111 THR   B C   1 
ATOM   1060 O O   . THR   B 2 102 ? -14.136 -8.693  -27.871 1.00 71.46  ? 111 THR   B O   1 
ATOM   1061 C CB  . THR   B 2 102 ? -12.274 -5.863  -27.997 1.00 71.17  ? 111 THR   B CB  1 
ATOM   1062 O OG1 . THR   B 2 102 ? -10.858 -5.991  -28.133 1.00 72.38  ? 111 THR   B OG1 1 
ATOM   1063 C CG2 . THR   B 2 102 ? -12.688 -5.992  -26.527 1.00 70.82  ? 111 THR   B CG2 1 
ATOM   1064 N N   . LEU   B 2 103 ? -11.945 -8.989  -28.244 1.00 70.15  ? 112 LEU   B N   1 
ATOM   1065 C CA  . LEU   B 2 103 ? -11.896 -10.287 -27.598 1.00 69.92  ? 112 LEU   B CA  1 
ATOM   1066 C C   . LEU   B 2 103 ? -11.066 -10.030 -26.371 1.00 68.83  ? 112 LEU   B C   1 
ATOM   1067 O O   . LEU   B 2 103 ? -9.901  -9.644  -26.497 1.00 68.07  ? 112 LEU   B O   1 
ATOM   1068 C CB  . LEU   B 2 103 ? -11.229 -11.361 -28.476 1.00 70.76  ? 112 LEU   B CB  1 
ATOM   1069 C CG  . LEU   B 2 103 ? -11.289 -12.756 -27.838 1.00 73.54  ? 112 LEU   B CG  1 
ATOM   1070 C CD1 . LEU   B 2 103 ? -12.429 -13.552 -28.391 1.00 74.81  ? 112 LEU   B CD1 1 
ATOM   1071 C CD2 . LEU   B 2 103 ? -9.996  -13.506 -27.994 1.00 73.98  ? 112 LEU   B CD2 1 
ATOM   1072 N N   . PRO   B 2 104 ? -11.664 -10.120 -25.168 1.00 68.55  ? 113 PRO   B N   1 
ATOM   1073 C CA  . PRO   B 2 104 ? -10.885 -9.824  -23.965 1.00 68.93  ? 113 PRO   B CA  1 
ATOM   1074 C C   . PRO   B 2 104 ? -9.802  -10.844 -23.672 1.00 70.43  ? 113 PRO   B C   1 
ATOM   1075 O O   . PRO   B 2 104 ? -9.803  -11.957 -24.201 1.00 71.01  ? 113 PRO   B O   1 
ATOM   1076 C CB  . PRO   B 2 104 ? -11.940 -9.739  -22.846 1.00 69.23  ? 113 PRO   B CB  1 
ATOM   1077 C CG  . PRO   B 2 104 ? -13.274 -9.874  -23.519 1.00 69.61  ? 113 PRO   B CG  1 
ATOM   1078 C CD  . PRO   B 2 104 ? -13.039 -10.535 -24.840 1.00 67.62  ? 113 PRO   B CD  1 
ATOM   1079 N N   . GLY   B 2 105 ? -8.871  -10.434 -22.824 1.00 71.10  ? 114 GLY   B N   1 
ATOM   1080 C CA  . GLY   B 2 105 ? -7.792  -11.266 -22.332 1.00 71.55  ? 114 GLY   B CA  1 
ATOM   1081 C C   . GLY   B 2 105 ? -8.073  -11.729 -20.920 1.00 72.52  ? 114 GLY   B C   1 
ATOM   1082 O O   . GLY   B 2 105 ? -9.222  -11.730 -20.473 1.00 73.17  ? 114 GLY   B O   1 
ATOM   1083 N N   . ILE   B 2 106 ? -7.030  -12.141 -20.207 1.00 72.21  ? 115 ILE   B N   1 
ATOM   1084 C CA  . ILE   B 2 106 ? -7.171  -12.649 -18.854 1.00 72.28  ? 115 ILE   B CA  1 
ATOM   1085 C C   . ILE   B 2 106 ? -6.274  -11.888 -17.894 1.00 72.16  ? 115 ILE   B C   1 
ATOM   1086 O O   . ILE   B 2 106 ? -5.076  -11.755 -18.133 1.00 72.47  ? 115 ILE   B O   1 
ATOM   1087 C CB  . ILE   B 2 106 ? -6.818  -14.168 -18.841 1.00 73.13  ? 115 ILE   B CB  1 
ATOM   1088 C CG1 . ILE   B 2 106 ? -7.812  -15.010 -19.662 1.00 74.32  ? 115 ILE   B CG1 1 
ATOM   1089 C CG2 . ILE   B 2 106 ? -6.646  -14.726 -17.438 1.00 73.69  ? 115 ILE   B CG2 1 
ATOM   1090 C CD1 . ILE   B 2 106 ? -9.189  -14.956 -19.167 1.00 75.80  ? 115 ILE   B CD1 1 
ATOM   1091 N N   . PHE   B 2 107 ? -6.855  -11.422 -16.784 1.00 71.44  ? 116 PHE   B N   1 
ATOM   1092 C CA  . PHE   B 2 107 ? -6.169  -10.807 -15.665 1.00 70.92  ? 116 PHE   B CA  1 
ATOM   1093 C C   . PHE   B 2 107 ? -6.099  -11.976 -14.708 1.00 71.91  ? 116 PHE   B C   1 
ATOM   1094 O O   . PHE   B 2 107 ? -7.146  -12.387 -14.205 1.00 72.44  ? 116 PHE   B O   1 
ATOM   1095 C CB  . PHE   B 2 107 ? -7.068  -9.751  -15.009 1.00 69.88  ? 116 PHE   B CB  1 
ATOM   1096 C CG  . PHE   B 2 107 ? -6.705  -8.309  -15.234 1.00 69.66  ? 116 PHE   B CG  1 
ATOM   1097 C CD1 . PHE   B 2 107 ? -5.978  -7.924  -16.350 1.00 70.46  ? 116 PHE   B CD1 1 
ATOM   1098 C CD2 . PHE   B 2 107 ? -7.176  -7.323  -14.386 1.00 69.74  ? 116 PHE   B CD2 1 
ATOM   1099 C CE1 . PHE   B 2 107 ? -5.704  -6.581  -16.594 1.00 70.70  ? 116 PHE   B CE1 1 
ATOM   1100 C CE2 . PHE   B 2 107 ? -6.885  -5.986  -14.619 1.00 70.38  ? 116 PHE   B CE2 1 
ATOM   1101 C CZ  . PHE   B 2 107 ? -6.156  -5.622  -15.723 1.00 70.30  ? 116 PHE   B CZ  1 
ATOM   1102 N N   . LYS   B 2 108 ? -4.915  -12.550 -14.487 1.00 72.00  ? 117 LYS   B N   1 
ATOM   1103 C CA  . LYS   B 2 108 ? -4.794  -13.691 -13.581 1.00 72.69  ? 117 LYS   B CA  1 
ATOM   1104 C C   . LYS   B 2 108 ? -4.367  -13.209 -12.198 1.00 71.84  ? 117 LYS   B C   1 
ATOM   1105 O O   . LYS   B 2 108 ? -3.371  -12.496 -12.084 1.00 71.24  ? 117 LYS   B O   1 
ATOM   1106 C CB  . LYS   B 2 108 ? -3.825  -14.732 -14.156 1.00 76.76  ? 117 LYS   B CB  1 
ATOM   1107 C CG  . LYS   B 2 108 ? -3.716  -15.972 -13.293 1.00 83.95  ? 117 LYS   B CG  1 
ATOM   1108 C CD  . LYS   B 2 108 ? -2.611  -16.920 -13.761 1.00 90.80  ? 117 LYS   B CD  1 
ATOM   1109 C CE  . LYS   B 2 108 ? -2.054  -17.733 -12.602 1.00 95.79  ? 117 LYS   B CE  1 
ATOM   1110 N NZ  . LYS   B 2 108 ? -0.981  -18.659 -13.064 1.00 99.11  ? 117 LYS   B NZ  1 
ATOM   1111 N N   . THR   B 2 109 ? -5.166  -13.529 -11.153 1.00 71.68  ? 118 THR   B N   1 
ATOM   1112 C CA  . THR   B 2 109 ? -4.916  -13.099 -9.769  1.00 71.86  ? 118 THR   B CA  1 
ATOM   1113 C C   . THR   B 2 109 ? -4.868  -14.305 -8.779  1.00 71.36  ? 118 THR   B C   1 
ATOM   1114 O O   . THR   B 2 109 ? -5.187  -15.438 -9.153  1.00 71.19  ? 118 THR   B O   1 
ATOM   1115 C CB  . THR   B 2 109 ? -5.937  -11.989 -9.329  1.00 73.76  ? 118 THR   B CB  1 
ATOM   1116 O OG1 . THR   B 2 109 ? -7.181  -12.580 -8.957  1.00 75.54  ? 118 THR   B OG1 1 
ATOM   1117 C CG2 . THR   B 2 109 ? -6.192  -10.935 -10.395 1.00 74.14  ? 118 THR   B CG2 1 
ATOM   1118 N N   . LYS   B 2 110 ? -4.466  -14.054 -7.520  1.00 70.76  ? 119 LYS   B N   1 
ATOM   1119 C CA  . LYS   B 2 110 ? -4.381  -15.082 -6.479  1.00 70.75  ? 119 LYS   B CA  1 
ATOM   1120 C C   . LYS   B 2 110 ? -5.765  -15.639 -6.061  1.00 71.12  ? 119 LYS   B C   1 
ATOM   1121 O O   . LYS   B 2 110 ? -5.834  -16.698 -5.427  1.00 71.91  ? 119 LYS   B O   1 
ATOM   1122 C CB  . LYS   B 2 110 ? -3.596  -14.544 -5.263  1.00 71.70  ? 119 LYS   B CB  1 
ATOM   1123 C CG  . LYS   B 2 110 ? -4.393  -13.575 -4.390  1.00 74.67  ? 119 LYS   B CG  1 
ATOM   1124 C CD  . LYS   B 2 110 ? -3.501  -12.677 -3.548  1.00 78.68  ? 119 LYS   B CD  1 
ATOM   1125 C CE  . LYS   B 2 110 ? -4.010  -12.501 -2.130  1.00 82.14  ? 119 LYS   B CE  1 
ATOM   1126 N NZ  . LYS   B 2 110 ? -5.335  -11.823 -2.077  1.00 83.97  ? 119 LYS   B NZ  1 
ATOM   1127 N N   . ASP   B 2 111 ? -6.857  -14.930 -6.409  1.00 70.37  ? 120 ASP   B N   1 
ATOM   1128 C CA  . ASP   B 2 111 ? -8.218  -15.351 -6.099  1.00 69.99  ? 120 ASP   B CA  1 
ATOM   1129 C C   . ASP   B 2 111 ? -9.026  -15.804 -7.332  1.00 69.90  ? 120 ASP   B C   1 
ATOM   1130 O O   . ASP   B 2 111 ? -10.203 -16.122 -7.181  1.00 70.86  ? 120 ASP   B O   1 
ATOM   1131 C CB  . ASP   B 2 111 ? -8.994  -14.234 -5.384  1.00 71.17  ? 120 ASP   B CB  1 
ATOM   1132 C CG  . ASP   B 2 111 ? -8.318  -13.629 -4.174  1.00 73.98  ? 120 ASP   B CG  1 
ATOM   1133 O OD1 . ASP   B 2 111 ? -8.097  -14.371 -3.174  1.00 73.09  ? 120 ASP   B OD1 1 
ATOM   1134 O OD2 . ASP   B 2 111 ? -8.035  -12.410 -4.206  1.00 76.00  ? 120 ASP   B OD2 1 
ATOM   1135 N N   . GLY   B 2 112 ? -8.424  -15.817 -8.525  1.00 68.26  ? 121 GLY   B N   1 
ATOM   1136 C CA  . GLY   B 2 112 ? -9.119  -16.266 -9.724  1.00 67.12  ? 121 GLY   B CA  1 
ATOM   1137 C C   . GLY   B 2 112 ? -8.876  -15.417 -10.959 1.00 65.65  ? 121 GLY   B C   1 
ATOM   1138 O O   . GLY   B 2 112 ? -8.306  -14.330 -10.849 1.00 65.34  ? 121 GLY   B O   1 
ATOM   1139 N N   . ASP   B 2 113 ? -9.310  -15.910 -12.146 1.00 64.66  ? 122 ASP   B N   1 
ATOM   1140 C CA  . ASP   B 2 113 ? -9.170  -15.193 -13.432 1.00 64.49  ? 122 ASP   B CA  1 
ATOM   1141 C C   . ASP   B 2 113 ? -10.324 -14.232 -13.701 1.00 64.23  ? 122 ASP   B C   1 
ATOM   1142 O O   . ASP   B 2 113 ? -11.454 -14.480 -13.272 1.00 64.03  ? 122 ASP   B O   1 
ATOM   1143 C CB  . ASP   B 2 113 ? -9.048  -16.161 -14.627 1.00 65.99  ? 122 ASP   B CB  1 
ATOM   1144 C CG  . ASP   B 2 113 ? -7.792  -17.010 -14.641 1.00 70.66  ? 122 ASP   B CG  1 
ATOM   1145 O OD1 . ASP   B 2 113 ? -7.026  -16.954 -13.650 1.00 71.22  ? 122 ASP   B OD1 1 
ATOM   1146 O OD2 . ASP   B 2 113 ? -7.576  -17.743 -15.648 1.00 72.91  ? 122 ASP   B OD2 1 
ATOM   1147 N N   . ILE   B 2 114 ? -10.047 -13.147 -14.456 1.00 63.68  ? 123 ILE   B N   1 
ATOM   1148 C CA  . ILE   B 2 114 ? -11.034 -12.111 -14.765 1.00 63.91  ? 123 ILE   B CA  1 
ATOM   1149 C C   . ILE   B 2 114 ? -10.806 -11.604 -16.198 1.00 63.68  ? 123 ILE   B C   1 
ATOM   1150 O O   . ILE   B 2 114 ? -9.659  -11.467 -16.611 1.00 63.12  ? 123 ILE   B O   1 
ATOM   1151 C CB  . ILE   B 2 114 ? -10.913 -10.950 -13.726 1.00 64.19  ? 123 ILE   B CB  1 
ATOM   1152 C CG1 . ILE   B 2 114 ? -11.416 -11.370 -12.350 1.00 65.46  ? 123 ILE   B CG1 1 
ATOM   1153 C CG2 . ILE   B 2 114 ? -11.648 -9.698  -14.177 1.00 64.83  ? 123 ILE   B CG2 1 
ATOM   1154 C CD1 . ILE   B 2 114 ? -10.852 -10.527 -11.206 1.00 66.63  ? 123 ILE   B CD1 1 
ATOM   1155 N N   . GLY   B 2 115 ? -11.878 -11.348 -16.943 1.00 64.02  ? 124 GLY   B N   1 
ATOM   1156 C CA  . GLY   B 2 115 ? -11.746 -10.841 -18.310 1.00 64.88  ? 124 GLY   B CA  1 
ATOM   1157 C C   . GLY   B 2 115 ? -11.125 -9.458  -18.351 1.00 65.50  ? 124 GLY   B C   1 
ATOM   1158 O O   . GLY   B 2 115 ? -11.273 -8.690  -17.402 1.00 65.04  ? 124 GLY   B O   1 
ATOM   1159 N N   . ALA   B 2 116 ? -10.445 -9.112  -19.450 1.00 66.38  ? 125 ALA   B N   1 
ATOM   1160 C CA  . ALA   B 2 116 ? -9.800  -7.802  -19.561 1.00 67.33  ? 125 ALA   B CA  1 
ATOM   1161 C C   . ALA   B 2 116 ? -9.833  -7.204  -20.966 1.00 67.88  ? 125 ALA   B C   1 
ATOM   1162 O O   . ALA   B 2 116 ? -9.334  -7.809  -21.902 1.00 68.57  ? 125 ALA   B O   1 
ATOM   1163 C CB  . ALA   B 2 116 ? -8.369  -7.880  -19.052 1.00 67.66  ? 125 ALA   B CB  1 
ATOM   1164 N N   . VAL   B 2 117 ? -10.407 -6.012  -21.114 1.00 67.99  ? 126 VAL   B N   1 
ATOM   1165 C CA  A VAL   B 2 117 ? -10.484 -5.357  -22.419 0.50 68.64  ? 126 VAL   B CA  1 
ATOM   1166 C CA  B VAL   B 2 117 ? -10.506 -5.344  -22.399 0.50 68.85  ? 126 VAL   B CA  1 
ATOM   1167 C C   . VAL   B 2 117 ? -9.330  -4.369  -22.599 1.00 69.33  ? 126 VAL   B C   1 
ATOM   1168 O O   . VAL   B 2 117 ? -9.129  -3.465  -21.779 1.00 68.98  ? 126 VAL   B O   1 
ATOM   1169 C CB  A VAL   B 2 117 ? -11.867 -4.753  -22.744 0.50 69.04  ? 126 VAL   B CB  1 
ATOM   1170 C CB  B VAL   B 2 117 ? -11.902 -4.700  -22.521 0.50 69.63  ? 126 VAL   B CB  1 
ATOM   1171 C CG1 A VAL   B 2 117 ? -12.905 -5.856  -22.890 0.50 69.61  ? 126 VAL   B CG1 1 
ATOM   1172 C CG1 B VAL   B 2 117 ? -11.938 -3.615  -23.576 0.50 70.46  ? 126 VAL   B CG1 1 
ATOM   1173 C CG2 A VAL   B 2 117 ? -12.301 -3.733  -21.698 0.50 69.43  ? 126 VAL   B CG2 1 
ATOM   1174 C CG2 B VAL   B 2 117 ? -12.952 -5.765  -22.805 0.50 70.17  ? 126 VAL   B CG2 1 
ATOM   1175 N N   . ALA   B 2 118 ? -8.520  -4.600  -23.659 1.00 69.64  ? 127 ALA   B N   1 
ATOM   1176 C CA  . ALA   B 2 118 ? -7.339  -3.800  -23.976 1.00 70.86  ? 127 ALA   B CA  1 
ATOM   1177 C C   . ALA   B 2 118 ? -7.608  -2.628  -24.937 1.00 71.90  ? 127 ALA   B C   1 
ATOM   1178 O O   . ALA   B 2 118 ? -6.973  -2.513  -25.981 1.00 71.90  ? 127 ALA   B O   1 
ATOM   1179 C CB  . ALA   B 2 118 ? -6.230  -4.698  -24.517 1.00 70.92  ? 127 ALA   B CB  1 
ATOM   1180 N N   . LEU   B 2 119 ? -8.530  -1.736  -24.568 1.00 72.44  ? 128 LEU   B N   1 
ATOM   1181 C CA  . LEU   B 2 119 ? -8.831  -0.567  -25.396 1.00 73.28  ? 128 LEU   B CA  1 
ATOM   1182 C C   . LEU   B 2 119 ? -8.471  0.690   -24.605 1.00 73.27  ? 128 LEU   B C   1 
ATOM   1183 O O   . LEU   B 2 119 ? -8.806  0.763   -23.422 1.00 72.84  ? 128 LEU   B O   1 
ATOM   1184 C CB  . LEU   B 2 119 ? -10.316 -0.563  -25.791 1.00 74.06  ? 128 LEU   B CB  1 
ATOM   1185 C CG  . LEU   B 2 119 ? -10.831 -1.831  -26.475 1.00 75.84  ? 128 LEU   B CG  1 
ATOM   1186 C CD1 . LEU   B 2 119 ? -12.333 -1.777  -26.674 1.00 76.37  ? 128 LEU   B CD1 1 
ATOM   1187 C CD2 . LEU   B 2 119 ? -10.119 -2.088  -27.780 1.00 76.85  ? 128 LEU   B CD2 1 
ATOM   1188 N N   . ASP   B 2 120 ? -7.760  1.664   -25.226 1.00 73.03  ? 129 ASP   B N   1 
ATOM   1189 C CA  . ASP   B 2 120 ? -7.400  2.880   -24.480 1.00 73.26  ? 129 ASP   B CA  1 
ATOM   1190 C C   . ASP   B 2 120 ? -8.337  4.050   -24.754 1.00 72.29  ? 129 ASP   B C   1 
ATOM   1191 O O   . ASP   B 2 120 ? -8.519  4.433   -25.895 1.00 73.24  ? 129 ASP   B O   1 
ATOM   1192 C CB  . ASP   B 2 120 ? -5.931  3.284   -24.684 1.00 75.50  ? 129 ASP   B CB  1 
ATOM   1193 C CG  . ASP   B 2 120 ? -5.310  3.995   -23.483 1.00 81.13  ? 129 ASP   B CG  1 
ATOM   1194 O OD1 . ASP   B 2 120 ? -6.070  4.404   -22.565 1.00 82.24  ? 129 ASP   B OD1 1 
ATOM   1195 O OD2 . ASP   B 2 120 ? -4.068  4.124   -23.447 1.00 83.19  ? 129 ASP   B OD2 1 
ATOM   1196 N N   . TYR   B 2 121 ? -8.928  4.614   -23.703 1.00 70.77  ? 130 TYR   B N   1 
ATOM   1197 C CA  . TYR   B 2 121 ? -9.851  5.748   -23.793 1.00 69.61  ? 130 TYR   B CA  1 
ATOM   1198 C C   . TYR   B 2 121 ? -9.585  6.731   -22.632 1.00 67.49  ? 130 TYR   B C   1 
ATOM   1199 O O   . TYR   B 2 121 ? -8.996  6.323   -21.635 1.00 67.56  ? 130 TYR   B O   1 
ATOM   1200 C CB  . TYR   B 2 121 ? -11.307 5.238   -23.738 1.00 69.94  ? 130 TYR   B CB  1 
ATOM   1201 C CG  . TYR   B 2 121 ? -11.830 4.772   -25.077 1.00 70.87  ? 130 TYR   B CG  1 
ATOM   1202 C CD1 . TYR   B 2 121 ? -12.445 5.656   -25.950 1.00 72.32  ? 130 TYR   B CD1 1 
ATOM   1203 C CD2 . TYR   B 2 121 ? -11.711 3.448   -25.470 1.00 72.08  ? 130 TYR   B CD2 1 
ATOM   1204 C CE1 . TYR   B 2 121 ? -12.889 5.244   -27.201 1.00 73.48  ? 130 TYR   B CE1 1 
ATOM   1205 C CE2 . TYR   B 2 121 ? -12.145 3.023   -26.720 1.00 73.14  ? 130 TYR   B CE2 1 
ATOM   1206 C CZ  . TYR   B 2 121 ? -12.740 3.923   -27.580 1.00 74.62  ? 130 TYR   B CZ  1 
ATOM   1207 O OH  . TYR   B 2 121 ? -13.184 3.512   -28.811 1.00 77.03  ? 130 TYR   B OH  1 
ATOM   1208 N N   . PRO   B 2 122 ? -10.022 8.013   -22.701 1.00 65.48  ? 131 PRO   B N   1 
ATOM   1209 C CA  . PRO   B 2 122 ? -9.772  8.931   -21.567 1.00 63.58  ? 131 PRO   B CA  1 
ATOM   1210 C C   . PRO   B 2 122 ? -10.315 8.420   -20.225 1.00 61.37  ? 131 PRO   B C   1 
ATOM   1211 O O   . PRO   B 2 122 ? -11.165 7.524   -20.205 1.00 61.15  ? 131 PRO   B O   1 
ATOM   1212 C CB  . PRO   B 2 122 ? -10.472 10.223  -21.995 1.00 64.52  ? 131 PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 2 122 ? -10.470 10.164  -23.528 1.00 65.79  ? 131 PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 2 122 ? -10.696 8.703   -23.824 1.00 64.99  ? 131 PRO   B CD  1 
ATOM   1215 N N   . ALA   B 2 123 ? -9.829  8.984   -19.099 1.00 59.40  ? 132 ALA   B N   1 
ATOM   1216 C CA  . ALA   B 2 123 ? -10.285 8.570   -17.772 1.00 57.96  ? 132 ALA   B CA  1 
ATOM   1217 C C   . ALA   B 2 123 ? -11.800 8.797   -17.578 1.00 56.58  ? 132 ALA   B C   1 
ATOM   1218 O O   . ALA   B 2 123 ? -12.456 7.995   -16.921 1.00 56.49  ? 132 ALA   B O   1 
ATOM   1219 C CB  . ALA   B 2 123 ? -9.492  9.290   -16.693 1.00 58.01  ? 132 ALA   B CB  1 
ATOM   1220 N N   . GLY   B 2 124 ? -12.348 9.826   -18.224 1.00 55.45  ? 133 GLY   B N   1 
ATOM   1221 C CA  . GLY   B 2 124 ? -13.776 10.126  -18.186 1.00 54.72  ? 133 GLY   B CA  1 
ATOM   1222 C C   . GLY   B 2 124 ? -14.669 9.087   -18.850 1.00 54.01  ? 133 GLY   B C   1 
ATOM   1223 O O   . GLY   B 2 124 ? -15.896 9.170   -18.751 1.00 53.47  ? 133 GLY   B O   1 
ATOM   1224 N N   . THR   B 2 125 ? -14.072 8.102   -19.547 1.00 53.57  ? 134 THR   B N   1 
ATOM   1225 C CA  . THR   B 2 125 ? -14.831 7.014   -20.174 1.00 54.06  ? 134 THR   B CA  1 
ATOM   1226 C C   . THR   B 2 125 ? -15.199 5.908   -19.122 1.00 53.51  ? 134 THR   B C   1 
ATOM   1227 O O   . THR   B 2 125 ? -15.975 5.014   -19.446 1.00 53.95  ? 134 THR   B O   1 
ATOM   1228 C CB  . THR   B 2 125 ? -14.077 6.486   -21.448 1.00 55.80  ? 134 THR   B CB  1 
ATOM   1229 O OG1 . THR   B 2 125 ? -13.668 7.595   -22.257 1.00 57.22  ? 134 THR   B OG1 1 
ATOM   1230 C CG2 . THR   B 2 125 ? -14.936 5.576   -22.338 1.00 56.14  ? 134 THR   B CG2 1 
ATOM   1231 N N   . SER   B 2 126 ? -14.657 5.981   -17.874 1.00 52.84  ? 135 SER   B N   1 
ATOM   1232 C CA  . SER   B 2 126 ? -14.866 5.027   -16.764 1.00 52.85  ? 135 SER   B CA  1 
ATOM   1233 C C   . SER   B 2 126 ? -16.328 4.830   -16.402 1.00 52.83  ? 135 SER   B C   1 
ATOM   1234 O O   . SER   B 2 126 ? -16.989 5.785   -16.075 1.00 52.73  ? 135 SER   B O   1 
ATOM   1235 C CB  . SER   B 2 126 ? -14.153 5.508   -15.507 1.00 53.27  ? 135 SER   B CB  1 
ATOM   1236 O OG  . SER   B 2 126 ? -12.785 5.788   -15.739 1.00 55.01  ? 135 SER   B OG  1 
ATOM   1237 N N   . GLY   B 2 127 ? -16.795 3.594   -16.401 1.00 52.30  ? 136 GLY   B N   1 
ATOM   1238 C CA  . GLY   B 2 127 ? -18.186 3.265   -16.128 1.00 52.06  ? 136 GLY   B CA  1 
ATOM   1239 C C   . GLY   B 2 127 ? -18.929 2.793   -17.364 1.00 52.41  ? 136 GLY   B C   1 
ATOM   1240 O O   . GLY   B 2 127 ? -20.069 2.338   -17.271 1.00 52.68  ? 136 GLY   B O   1 
ATOM   1241 N N   . SER   B 2 128 ? -18.295 2.879   -18.543 1.00 52.50  ? 137 SER   B N   1 
ATOM   1242 C CA  . SER   B 2 128 ? -18.875 2.413   -19.793 1.00 53.04  ? 137 SER   B CA  1 
ATOM   1243 C C   . SER   B 2 128 ? -19.120 0.905   -19.693 1.00 53.28  ? 137 SER   B C   1 
ATOM   1244 O O   . SER   B 2 128 ? -18.272 0.169   -19.188 1.00 52.91  ? 137 SER   B O   1 
ATOM   1245 C CB  . SER   B 2 128 ? -17.921 2.694   -20.949 1.00 54.24  ? 137 SER   B CB  1 
ATOM   1246 O OG  . SER   B 2 128 ? -17.871 4.074   -21.270 1.00 56.17  ? 137 SER   B OG  1 
ATOM   1247 N N   . PRO   B 2 129 ? -20.316 0.453   -20.077 1.00 53.26  ? 138 PRO   B N   1 
ATOM   1248 C CA  . PRO   B 2 129 ? -20.605 -0.984  -19.997 1.00 53.45  ? 138 PRO   B CA  1 
ATOM   1249 C C   . PRO   B 2 129 ? -19.963 -1.810  -21.114 1.00 54.39  ? 138 PRO   B C   1 
ATOM   1250 O O   . PRO   B 2 129 ? -19.856 -1.353  -22.264 1.00 54.54  ? 138 PRO   B O   1 
ATOM   1251 C CB  . PRO   B 2 129 ? -22.129 -1.030  -20.114 1.00 54.40  ? 138 PRO   B CB  1 
ATOM   1252 C CG  . PRO   B 2 129 ? -22.476 0.161   -20.986 1.00 54.43  ? 138 PRO   B CG  1 
ATOM   1253 C CD  . PRO   B 2 129 ? -21.454 1.222   -20.628 1.00 52.85  ? 138 PRO   B CD  1 
ATOM   1254 N N   . ILE   B 2 130 ? -19.589 -3.050  -20.778 1.00 54.61  ? 139 ILE   B N   1 
ATOM   1255 C CA  . ILE   B 2 130 ? -19.071 -4.061  -21.689 1.00 55.72  ? 139 ILE   B CA  1 
ATOM   1256 C C   . ILE   B 2 130 ? -20.216 -5.075  -21.861 1.00 57.89  ? 139 ILE   B C   1 
ATOM   1257 O O   . ILE   B 2 130 ? -20.836 -5.479  -20.872 1.00 58.13  ? 139 ILE   B O   1 
ATOM   1258 C CB  . ILE   B 2 130 ? -17.805 -4.703  -21.129 1.00 56.08  ? 139 ILE   B CB  1 
ATOM   1259 C CG1 . ILE   B 2 130 ? -16.722 -3.652  -20.865 1.00 57.02  ? 139 ILE   B CG1 1 
ATOM   1260 C CG2 . ILE   B 2 130 ? -17.296 -5.807  -22.026 1.00 56.06  ? 139 ILE   B CG2 1 
ATOM   1261 C CD1 . ILE   B 2 130 ? -15.727 -4.137  -19.891 1.00 57.71  ? 139 ILE   B CD1 1 
ATOM   1262 N N   . LEU   B 2 131 ? -20.520 -5.457  -23.117 1.00 59.09  ? 140 LEU   B N   1 
ATOM   1263 C CA  . LEU   B 2 131 ? -21.679 -6.277  -23.466 1.00 60.61  ? 140 LEU   B CA  1 
ATOM   1264 C C   . LEU   B 2 131 ? -21.431 -7.643  -24.089 1.00 62.43  ? 140 LEU   B C   1 
ATOM   1265 O O   . LEU   B 2 131 ? -20.500 -7.818  -24.877 1.00 63.03  ? 140 LEU   B O   1 
ATOM   1266 C CB  . LEU   B 2 131 ? -22.529 -5.497  -24.493 1.00 60.70  ? 140 LEU   B CB  1 
ATOM   1267 C CG  . LEU   B 2 131 ? -22.760 -4.013  -24.282 1.00 61.31  ? 140 LEU   B CG  1 
ATOM   1268 C CD1 . LEU   B 2 131 ? -23.605 -3.455  -25.402 1.00 60.71  ? 140 LEU   B CD1 1 
ATOM   1269 C CD2 . LEU   B 2 131 ? -23.393 -3.756  -22.930 1.00 61.65  ? 140 LEU   B CD2 1 
ATOM   1270 N N   . ASP   B 2 132 ? -22.383 -8.563  -23.885 1.00 63.44  ? 141 ASP   B N   1 
ATOM   1271 C CA  . ASP   B 2 132 ? -22.359 -9.844  -24.592 1.00 65.26  ? 141 ASP   B CA  1 
ATOM   1272 C C   . ASP   B 2 132 ? -23.243 -9.731  -25.869 1.00 67.52  ? 141 ASP   B C   1 
ATOM   1273 O O   . ASP   B 2 132 ? -23.913 -8.707  -26.047 1.00 67.67  ? 141 ASP   B O   1 
ATOM   1274 C CB  . ASP   B 2 132 ? -22.752 -11.027 -23.678 1.00 66.53  ? 141 ASP   B CB  1 
ATOM   1275 C CG  . ASP   B 2 132 ? -24.086 -10.937 -22.975 1.00 70.61  ? 141 ASP   B CG  1 
ATOM   1276 O OD1 . ASP   B 2 132 ? -25.005 -10.320 -23.529 1.00 71.52  ? 141 ASP   B OD1 1 
ATOM   1277 O OD2 . ASP   B 2 132 ? -24.215 -11.512 -21.879 1.00 73.41  ? 141 ASP   B OD2 1 
ATOM   1278 N N   . LYS   B 2 133 ? -23.261 -10.759 -26.742 1.00 69.07  ? 142 LYS   B N   1 
ATOM   1279 C CA  . LYS   B 2 133 ? -24.034 -10.733 -27.992 1.00 71.43  ? 142 LYS   B CA  1 
ATOM   1280 C C   . LYS   B 2 133 ? -25.551 -10.518 -27.808 1.00 72.61  ? 142 LYS   B C   1 
ATOM   1281 O O   . LYS   B 2 133 ? -26.243 -10.153 -28.769 1.00 73.05  ? 142 LYS   B O   1 
ATOM   1282 C CB  . LYS   B 2 133 ? -23.759 -11.988 -28.835 1.00 74.87  ? 142 LYS   B CB  1 
ATOM   1283 C CG  . LYS   B 2 133 ? -22.386 -11.974 -29.501 1.00 81.28  ? 142 LYS   B CG  1 
ATOM   1284 C CD  . LYS   B 2 133 ? -21.512 -13.186 -29.112 1.00 87.03  ? 142 LYS   B CD  1 
ATOM   1285 C CE  . LYS   B 2 133 ? -20.672 -13.642 -30.296 1.00 91.07  ? 142 LYS   B CE  1 
ATOM   1286 N NZ  . LYS   B 2 133 ? -19.747 -14.754 -29.934 1.00 93.71  ? 142 LYS   B NZ  1 
ATOM   1287 N N   . CYS   B 2 134 ? -26.051 -10.725 -26.577 1.00 73.01  ? 143 CYS   B N   1 
ATOM   1288 C CA  . CYS   B 2 134 ? -27.447 -10.492 -26.195 1.00 73.69  ? 143 CYS   B CA  1 
ATOM   1289 C C   . CYS   B 2 134 ? -27.731 -9.054  -25.739 1.00 72.41  ? 143 CYS   B C   1 
ATOM   1290 O O   . CYS   B 2 134 ? -28.872 -8.744  -25.412 1.00 72.94  ? 143 CYS   B O   1 
ATOM   1291 C CB  . CYS   B 2 134 ? -27.873 -11.481 -25.116 1.00 76.07  ? 143 CYS   B CB  1 
ATOM   1292 S SG  . CYS   B 2 134 ? -28.164 -13.156 -25.726 1.00 84.16  ? 143 CYS   B SG  1 
ATOM   1293 N N   . GLY   B 2 135 ? -26.707 -8.213  -25.659 1.00 70.73  ? 144 GLY   B N   1 
ATOM   1294 C CA  . GLY   B 2 135 ? -26.849 -6.853  -25.156 1.00 69.34  ? 144 GLY   B CA  1 
ATOM   1295 C C   . GLY   B 2 135 ? -26.925 -6.775  -23.640 1.00 67.37  ? 144 GLY   B C   1 
ATOM   1296 O O   . GLY   B 2 135 ? -27.322 -5.745  -23.091 1.00 67.79  ? 144 GLY   B O   1 
ATOM   1297 N N   . ARG   B 2 136 ? -26.546 -7.852  -22.940 1.00 65.51  ? 145 ARG   B N   1 
ATOM   1298 C CA  . ARG   B 2 136 ? -26.568 -7.865  -21.476 1.00 63.90  ? 145 ARG   B CA  1 
ATOM   1299 C C   . ARG   B 2 136 ? -25.272 -7.302  -20.915 1.00 61.30  ? 145 ARG   B C   1 
ATOM   1300 O O   . ARG   B 2 136 ? -24.195 -7.582  -21.443 1.00 60.95  ? 145 ARG   B O   1 
ATOM   1301 C CB  . ARG   B 2 136 ? -26.822 -9.275  -20.936 1.00 65.84  ? 145 ARG   B CB  1 
ATOM   1302 C CG  . ARG   B 2 136 ? -28.272 -9.717  -21.047 1.00 69.38  ? 145 ARG   B CG  1 
ATOM   1303 C CD  . ARG   B 2 136 ? -28.417 -11.167 -20.636 1.00 72.99  ? 145 ARG   B CD  1 
ATOM   1304 N NE  . ARG   B 2 136 ? -27.879 -12.056 -21.663 1.00 76.25  ? 145 ARG   B NE  1 
ATOM   1305 C CZ  . ARG   B 2 136 ? -27.256 -13.204 -21.421 1.00 78.62  ? 145 ARG   B CZ  1 
ATOM   1306 N NH1 . ARG   B 2 136 ? -27.078 -13.621 -20.172 1.00 77.76  ? 145 ARG   B NH1 1 
ATOM   1307 N NH2 . ARG   B 2 136 ? -26.810 -13.950 -22.427 1.00 79.15  ? 145 ARG   B NH2 1 
ATOM   1308 N N   . VAL   B 2 137 ? -25.368 -6.515  -19.837 1.00 59.28  ? 146 VAL   B N   1 
ATOM   1309 C CA  . VAL   B 2 137 ? -24.191 -5.897  -19.247 1.00 57.84  ? 146 VAL   B CA  1 
ATOM   1310 C C   . VAL   B 2 137 ? -23.376 -6.909  -18.443 1.00 56.49  ? 146 VAL   B C   1 
ATOM   1311 O O   . VAL   B 2 137 ? -23.810 -7.349  -17.371 1.00 57.57  ? 146 VAL   B O   1 
ATOM   1312 C CB  . VAL   B 2 137 ? -24.549 -4.636  -18.423 1.00 58.25  ? 146 VAL   B CB  1 
ATOM   1313 C CG1 . VAL   B 2 137 ? -23.290 -3.888  -18.012 1.00 58.76  ? 146 VAL   B CG1 1 
ATOM   1314 C CG2 . VAL   B 2 137 ? -25.492 -3.716  -19.204 1.00 58.18  ? 146 VAL   B CG2 1 
ATOM   1315 N N   . ILE   B 2 138 ? -22.203 -7.285  -18.970 1.00 54.42  ? 147 ILE   B N   1 
ATOM   1316 C CA  . ILE   B 2 138 ? -21.295 -8.250  -18.340 1.00 53.10  ? 147 ILE   B CA  1 
ATOM   1317 C C   . ILE   B 2 138 ? -20.228 -7.596  -17.421 1.00 53.27  ? 147 ILE   B C   1 
ATOM   1318 O O   . ILE   B 2 138 ? -19.494 -8.308  -16.722 1.00 54.22  ? 147 ILE   B O   1 
ATOM   1319 C CB  . ILE   B 2 138 ? -20.643 -9.191  -19.400 1.00 51.98  ? 147 ILE   B CB  1 
ATOM   1320 C CG1 . ILE   B 2 138 ? -19.933 -8.401  -20.504 1.00 52.54  ? 147 ILE   B CG1 1 
ATOM   1321 C CG2 . ILE   B 2 138 ? -21.664 -10.148 -19.973 1.00 51.04  ? 147 ILE   B CG2 1 
ATOM   1322 C CD1 . ILE   B 2 138 ? -19.032 -9.235  -21.343 1.00 53.62  ? 147 ILE   B CD1 1 
ATOM   1323 N N   . GLY   B 2 139 ? -20.187 -6.265  -17.383 1.00 52.05  ? 148 GLY   B N   1 
ATOM   1324 C CA  . GLY   B 2 139 ? -19.245 -5.546  -16.544 1.00 51.27  ? 148 GLY   B CA  1 
ATOM   1325 C C   . GLY   B 2 139 ? -19.047 -4.099  -16.932 1.00 50.53  ? 148 GLY   B C   1 
ATOM   1326 O O   . GLY   B 2 139 ? -19.606 -3.628  -17.924 1.00 50.46  ? 148 GLY   B O   1 
ATOM   1327 N N   . LEU   B 2 140 ? -18.247 -3.380  -16.149 1.00 50.29  ? 149 LEU   B N   1 
ATOM   1328 C CA  . LEU   B 2 140 ? -17.945 -1.982  -16.436 1.00 50.60  ? 149 LEU   B CA  1 
ATOM   1329 C C   . LEU   B 2 140 ? -16.446 -1.798  -16.660 1.00 51.26  ? 149 LEU   B C   1 
ATOM   1330 O O   . LEU   B 2 140 ? -15.627 -2.492  -16.051 1.00 51.50  ? 149 LEU   B O   1 
ATOM   1331 C CB  . LEU   B 2 140 ? -18.433 -1.033  -15.331 1.00 50.19  ? 149 LEU   B CB  1 
ATOM   1332 C CG  . LEU   B 2 140 ? -19.890 -1.109  -14.905 1.00 51.16  ? 149 LEU   B CG  1 
ATOM   1333 C CD1 . LEU   B 2 140 ? -20.187 -0.028  -13.875 1.00 52.08  ? 149 LEU   B CD1 1 
ATOM   1334 C CD2 . LEU   B 2 140 ? -20.838 -0.989  -16.076 1.00 51.66  ? 149 LEU   B CD2 1 
ATOM   1335 N N   . TYR   B 2 141 ? -16.105 -0.838  -17.518 1.00 51.23  ? 150 TYR   B N   1 
ATOM   1336 C CA  . TYR   B 2 141 ? -14.745 -0.509  -17.927 1.00 52.45  ? 150 TYR   B CA  1 
ATOM   1337 C C   . TYR   B 2 141 ? -14.202 0.658   -17.128 1.00 52.22  ? 150 TYR   B C   1 
ATOM   1338 O O   . TYR   B 2 141 ? -14.933 1.597   -16.884 1.00 51.98  ? 150 TYR   B O   1 
ATOM   1339 C CB  . TYR   B 2 141 ? -14.791 -0.117  -19.415 1.00 53.41  ? 150 TYR   B CB  1 
ATOM   1340 C CG  . TYR   B 2 141 ? -13.550 0.535   -20.000 1.00 55.32  ? 150 TYR   B CG  1 
ATOM   1341 C CD1 . TYR   B 2 141 ? -13.446 1.917   -20.099 1.00 56.72  ? 150 TYR   B CD1 1 
ATOM   1342 C CD2 . TYR   B 2 141 ? -12.535 -0.229  -20.549 1.00 56.48  ? 150 TYR   B CD2 1 
ATOM   1343 C CE1 . TYR   B 2 141 ? -12.324 2.520   -20.651 1.00 57.69  ? 150 TYR   B CE1 1 
ATOM   1344 C CE2 . TYR   B 2 141 ? -11.426 0.361   -21.143 1.00 58.09  ? 150 TYR   B CE2 1 
ATOM   1345 C CZ  . TYR   B 2 141 ? -11.333 1.739   -21.214 1.00 58.58  ? 150 TYR   B CZ  1 
ATOM   1346 O OH  . TYR   B 2 141 ? -10.226 2.326   -21.781 1.00 58.11  ? 150 TYR   B OH  1 
ATOM   1347 N N   . GLY   B 2 142 ? -12.902 0.659   -16.858 1.00 52.12  ? 151 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 142 ? -12.272 1.772   -16.168 1.00 52.68  ? 151 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 142 ? -11.430 1.418   -14.960 1.00 52.65  ? 151 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 142 ? -10.960 2.324   -14.269 1.00 53.10  ? 151 GLY   B O   1 
ATOM   1351 N N   . ASN   B 2 143 ? -11.225 0.117   -14.678 1.00 52.23  ? 152 ASN   B N   1 
ATOM   1352 C CA  . ASN   B 2 143 ? -10.355 -0.274  -13.563 1.00 53.02  ? 152 ASN   B CA  1 
ATOM   1353 C C   . ASN   B 2 143 ? -9.372  -1.338  -14.018 1.00 55.20  ? 152 ASN   B C   1 
ATOM   1354 O O   . ASN   B 2 143 ? -9.751  -2.490  -14.224 1.00 55.26  ? 152 ASN   B O   1 
ATOM   1355 C CB  . ASN   B 2 143 ? -11.155 -0.752  -12.346 1.00 52.24  ? 152 ASN   B CB  1 
ATOM   1356 C CG  . ASN   B 2 143 ? -10.317 -0.921  -11.089 1.00 53.03  ? 152 ASN   B CG  1 
ATOM   1357 O OD1 . ASN   B 2 143 ? -9.180  -0.436  -11.007 1.00 52.95  ? 152 ASN   B OD1 1 
ATOM   1358 N ND2 . ASN   B 2 143 ? -10.863 -1.627  -10.081 1.00 51.88  ? 152 ASN   B ND2 1 
ATOM   1359 N N   . GLY   B 2 144 ? -8.116  -0.953  -14.147 1.00 56.80  ? 153 GLY   B N   1 
ATOM   1360 C CA  . GLY   B 2 144 ? -7.095  -1.881  -14.601 1.00 59.10  ? 153 GLY   B CA  1 
ATOM   1361 C C   . GLY   B 2 144 ? -5.667  -1.456  -14.379 1.00 61.78  ? 153 GLY   B C   1 
ATOM   1362 O O   . GLY   B 2 144 ? -5.332  -0.905  -13.333 1.00 61.76  ? 153 GLY   B O   1 
ATOM   1363 N N   . VAL   B 2 145 ? -4.817  -1.693  -15.380 1.00 64.18  ? 154 VAL   B N   1 
ATOM   1364 C CA  . VAL   B 2 145 ? -3.396  -1.456  -15.229 1.00 66.72  ? 154 VAL   B CA  1 
ATOM   1365 C C   . VAL   B 2 145 ? -2.726  -0.791  -16.449 1.00 69.54  ? 154 VAL   B C   1 
ATOM   1366 O O   . VAL   B 2 145 ? -3.311  -0.698  -17.531 1.00 69.36  ? 154 VAL   B O   1 
ATOM   1367 C CB  . VAL   B 2 145 ? -2.760  -2.825  -14.867 1.00 67.27  ? 154 VAL   B CB  1 
ATOM   1368 C CG1 . VAL   B 2 145 ? -2.479  -3.656  -16.120 1.00 67.86  ? 154 VAL   B CG1 1 
ATOM   1369 C CG2 . VAL   B 2 145 ? -1.518  -2.652  -14.008 1.00 67.62  ? 154 VAL   B CG2 1 
ATOM   1370 N N   . VAL   B 2 146 ? -1.504  -0.290  -16.249 1.00 71.81  ? 155 VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 146 ? -0.721  0.339   -17.301 1.00 74.44  ? 155 VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 146 ? 0.391   -0.646  -17.641 1.00 77.46  ? 155 VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 146 ? 1.176   -1.002  -16.767 1.00 77.92  ? 155 VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 146 ? -0.167  1.707   -16.849 1.00 74.94  ? 155 VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 146 ? 0.524   2.413   -18.006 1.00 75.52  ? 155 VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 146 ? -1.279  2.586   -16.281 1.00 75.18  ? 155 VAL   B CG2 1 
ATOM   1377 N N   . ILE   B 2 147 ? 0.408   -1.146  -18.880 1.00 79.44  ? 156 ILE   B N   1 
ATOM   1378 C CA  . ILE   B 2 147 ? 1.366   -2.155  -19.336 1.00 81.85  ? 156 ILE   B CA  1 
ATOM   1379 C C   . ILE   B 2 147 ? 2.662   -1.543  -19.928 1.00 85.07  ? 156 ILE   B C   1 
ATOM   1380 O O   . ILE   B 2 147 ? 2.742   -0.324  -20.076 1.00 86.02  ? 156 ILE   B O   1 
ATOM   1381 C CB  . ILE   B 2 147 ? 0.640   -3.106  -20.331 1.00 81.88  ? 156 ILE   B CB  1 
ATOM   1382 C CG1 . ILE   B 2 147 ? 0.163   -2.344  -21.590 1.00 82.52  ? 156 ILE   B CG1 1 
ATOM   1383 C CG2 . ILE   B 2 147 ? -0.514  -3.832  -19.651 1.00 81.95  ? 156 ILE   B CG2 1 
ATOM   1384 C CD1 . ILE   B 2 147 ? -0.404  -3.233  -22.669 1.00 83.21  ? 156 ILE   B CD1 1 
ATOM   1385 N N   . LYS   B 2 148 ? 3.669   -2.384  -20.273 1.00 86.45  ? 157 LYS   B N   1 
ATOM   1386 C CA  . LYS   B 2 148 ? 4.953   -1.963  -20.860 1.00 88.35  ? 157 LYS   B CA  1 
ATOM   1387 C C   . LYS   B 2 148 ? 4.812   -1.053  -22.093 1.00 89.20  ? 157 LYS   B C   1 
ATOM   1388 O O   . LYS   B 2 148 ? 5.752   -0.335  -22.430 1.00 89.54  ? 157 LYS   B O   1 
ATOM   1389 C CB  . LYS   B 2 148 ? 5.813   -3.188  -21.236 1.00 91.36  ? 157 LYS   B CB  1 
ATOM   1390 C CG  . LYS   B 2 148 ? 5.815   -4.305  -20.191 1.00 97.39  ? 157 LYS   B CG  1 
ATOM   1391 C CD  . LYS   B 2 148 ? 6.644   -5.498  -20.670 1.00 103.42 ? 157 LYS   B CD  1 
ATOM   1392 C CE  . LYS   B 2 148 ? 8.132   -5.266  -20.524 1.00 107.84 ? 157 LYS   B CE  1 
ATOM   1393 N NZ  . LYS   B 2 148 ? 8.533   -5.178  -19.091 1.00 110.51 ? 157 LYS   B NZ  1 
ATOM   1394 N N   . ASN   B 2 149 ? 3.661   -1.107  -22.784 1.00 89.30  ? 158 ASN   B N   1 
ATOM   1395 C CA  . ASN   B 2 149 ? 3.409   -0.285  -23.976 1.00 89.63  ? 158 ASN   B CA  1 
ATOM   1396 C C   . ASN   B 2 149 ? 2.831   1.117   -23.660 1.00 88.79  ? 158 ASN   B C   1 
ATOM   1397 O O   . ASN   B 2 149 ? 2.587   1.895   -24.585 1.00 89.11  ? 158 ASN   B O   1 
ATOM   1398 C CB  . ASN   B 2 149 ? 2.452   -1.001  -24.952 1.00 91.84  ? 158 ASN   B CB  1 
ATOM   1399 C CG  . ASN   B 2 149 ? 2.683   -2.485  -25.129 1.00 96.35  ? 158 ASN   B CG  1 
ATOM   1400 O OD1 . ASN   B 2 149 ? 3.770   -3.017  -24.863 1.00 98.19  ? 158 ASN   B OD1 1 
ATOM   1401 N ND2 . ASN   B 2 149 ? 1.651   -3.187  -25.588 1.00 97.00  ? 158 ASN   B ND2 1 
ATOM   1402 N N   . GLY   B 2 150 ? 2.566   1.406   -22.387 1.00 87.36  ? 159 GLY   B N   1 
ATOM   1403 C CA  . GLY   B 2 150 ? 1.985   2.680   -21.982 1.00 86.59  ? 159 GLY   B CA  1 
ATOM   1404 C C   . GLY   B 2 150 ? 0.465   2.667   -21.992 1.00 85.28  ? 159 GLY   B C   1 
ATOM   1405 O O   . GLY   B 2 150 ? -0.171  3.373   -21.202 1.00 85.18  ? 159 GLY   B O   1 
ATOM   1406 N N   . SER   B 2 151 ? -0.128  1.854   -22.898 1.00 83.58  ? 160 SER   B N   1 
ATOM   1407 C CA  A SER   B 2 151 ? -1.580  1.724   -23.044 0.50 83.00  ? 160 SER   B CA  1 
ATOM   1408 C CA  B SER   B 2 151 ? -1.578  1.723   -23.043 0.50 83.12  ? 160 SER   B CA  1 
ATOM   1409 C C   . SER   B 2 151 ? -2.249  1.130   -21.793 1.00 81.89  ? 160 SER   B C   1 
ATOM   1410 O O   . SER   B 2 151 ? -1.579  0.515   -20.956 1.00 82.07  ? 160 SER   B O   1 
ATOM   1411 C CB  A SER   B 2 151 ? -1.920  0.900   -24.285 0.50 84.35  ? 160 SER   B CB  1 
ATOM   1412 C CB  B SER   B 2 151 ? -1.913  0.897   -24.283 0.50 84.81  ? 160 SER   B CB  1 
ATOM   1413 O OG  A SER   B 2 151 ? -3.319  0.708   -24.424 0.50 86.51  ? 160 SER   B OG  1 
ATOM   1414 O OG  B SER   B 2 151 ? -1.205  -0.332  -24.287 0.50 87.52  ? 160 SER   B OG  1 
ATOM   1415 N N   . TYR   B 2 152 ? -3.577  1.325   -21.658 1.00 79.27  ? 161 TYR   B N   1 
ATOM   1416 C CA  . TYR   B 2 152 ? -4.356  0.842   -20.517 1.00 76.91  ? 161 TYR   B CA  1 
ATOM   1417 C C   . TYR   B 2 152 ? -5.060  -0.490  -20.796 1.00 74.23  ? 161 TYR   B C   1 
ATOM   1418 O O   . TYR   B 2 152 ? -5.610  -0.683  -21.870 1.00 74.11  ? 161 TYR   B O   1 
ATOM   1419 C CB  . TYR   B 2 152 ? -5.410  1.897   -20.122 1.00 76.67  ? 161 TYR   B CB  1 
ATOM   1420 C CG  . TYR   B 2 152 ? -5.843  1.838   -18.671 1.00 76.90  ? 161 TYR   B CG  1 
ATOM   1421 C CD1 . TYR   B 2 152 ? -5.004  2.273   -17.659 1.00 77.64  ? 161 TYR   B CD1 1 
ATOM   1422 C CD2 . TYR   B 2 152 ? -7.116  1.408   -18.319 1.00 77.59  ? 161 TYR   B CD2 1 
ATOM   1423 C CE1 . TYR   B 2 152 ? -5.400  2.240   -16.325 1.00 78.45  ? 161 TYR   B CE1 1 
ATOM   1424 C CE2 . TYR   B 2 152 ? -7.524  1.368   -16.987 1.00 78.18  ? 161 TYR   B CE2 1 
ATOM   1425 C CZ  . TYR   B 2 152 ? -6.662  1.786   -15.990 1.00 79.06  ? 161 TYR   B CZ  1 
ATOM   1426 O OH  . TYR   B 2 152 ? -7.041  1.768   -14.659 1.00 79.80  ? 161 TYR   B OH  1 
ATOM   1427 N N   . VAL   B 2 153 ? -5.064  -1.402  -19.812 1.00 71.75  ? 162 VAL   B N   1 
ATOM   1428 C CA  . VAL   B 2 153 ? -5.797  -2.656  -19.936 1.00 69.21  ? 162 VAL   B CA  1 
ATOM   1429 C C   . VAL   B 2 153 ? -6.764  -2.715  -18.745 1.00 66.14  ? 162 VAL   B C   1 
ATOM   1430 O O   . VAL   B 2 153 ? -6.335  -2.772  -17.603 1.00 66.03  ? 162 VAL   B O   1 
ATOM   1431 C CB  . VAL   B 2 153 ? -4.907  -3.917  -20.086 1.00 69.81  ? 162 VAL   B CB  1 
ATOM   1432 C CG1 . VAL   B 2 153 ? -5.769  -5.169  -20.198 1.00 70.23  ? 162 VAL   B CG1 1 
ATOM   1433 C CG2 . VAL   B 2 153 ? -3.988  -3.799  -21.306 1.00 70.49  ? 162 VAL   B CG2 1 
ATOM   1434 N N   . SER   B 2 154 ? -8.059  -2.612  -19.016 1.00 63.88  ? 163 SER   B N   1 
ATOM   1435 C CA  . SER   B 2 154 ? -9.096  -2.586  -17.997 1.00 62.12  ? 163 SER   B CA  1 
ATOM   1436 C C   . SER   B 2 154 ? -9.690  -3.955  -17.727 1.00 60.27  ? 163 SER   B C   1 
ATOM   1437 O O   . SER   B 2 154 ? -9.834  -4.751  -18.638 1.00 59.28  ? 163 SER   B O   1 
ATOM   1438 C CB  . SER   B 2 154 ? -10.209 -1.638  -18.436 1.00 62.13  ? 163 SER   B CB  1 
ATOM   1439 O OG  . SER   B 2 154 ? -11.379 -1.709  -17.632 1.00 61.75  ? 163 SER   B OG  1 
ATOM   1440 N N   . ALA   B 2 155 ? -10.092 -4.208  -16.487 1.00 59.18  ? 164 ALA   B N   1 
ATOM   1441 C CA  . ALA   B 2 155 ? -10.764 -5.450  -16.129 1.00 58.77  ? 164 ALA   B CA  1 
ATOM   1442 C C   . ALA   B 2 155 ? -12.262 -5.369  -16.589 1.00 58.04  ? 164 ALA   B C   1 
ATOM   1443 O O   . ALA   B 2 155 ? -12.747 -4.305  -17.015 1.00 56.55  ? 164 ALA   B O   1 
ATOM   1444 C CB  . ALA   B 2 155 ? -10.676 -5.651  -14.611 1.00 59.59  ? 164 ALA   B CB  1 
ATOM   1445 N N   . ILE   B 2 156 ? -12.976 -6.506  -16.548 1.00 58.22  ? 165 ILE   B N   1 
ATOM   1446 C CA  . ILE   B 2 156 ? -14.404 -6.521  -16.810 1.00 58.72  ? 165 ILE   B CA  1 
ATOM   1447 C C   . ILE   B 2 156 ? -14.981 -6.704  -15.415 1.00 58.93  ? 165 ILE   B C   1 
ATOM   1448 O O   . ILE   B 2 156 ? -15.115 -7.839  -14.946 1.00 59.16  ? 165 ILE   B O   1 
ATOM   1449 C CB  . ILE   B 2 156 ? -14.853 -7.637  -17.785 1.00 59.28  ? 165 ILE   B CB  1 
ATOM   1450 C CG1 . ILE   B 2 156 ? -14.086 -7.540  -19.112 1.00 60.20  ? 165 ILE   B CG1 1 
ATOM   1451 C CG2 . ILE   B 2 156 ? -16.372 -7.560  -18.001 1.00 59.58  ? 165 ILE   B CG2 1 
ATOM   1452 C CD1 . ILE   B 2 156 ? -14.378 -8.662  -20.107 1.00 61.63  ? 165 ILE   B CD1 1 
ATOM   1453 N N   . THR   B 2 157 ? -15.203 -5.572  -14.720 1.00 58.41  ? 166 THR   B N   1 
ATOM   1454 C CA  . THR   B 2 157 ? -15.694 -5.512  -13.342 1.00 58.80  ? 166 THR   B CA  1 
ATOM   1455 C C   . THR   B 2 157 ? -17.192 -5.684  -13.244 1.00 58.96  ? 166 THR   B C   1 
ATOM   1456 O O   . THR   B 2 157 ? -17.954 -4.829  -13.697 1.00 58.99  ? 166 THR   B O   1 
ATOM   1457 C CB  . THR   B 2 157 ? -15.285 -4.208  -12.663 1.00 59.48  ? 166 THR   B CB  1 
ATOM   1458 O OG1 . THR   B 2 157 ? -13.894 -3.981  -12.869 1.00 59.89  ? 166 THR   B OG1 1 
ATOM   1459 C CG2 . THR   B 2 157 ? -15.549 -4.240  -11.195 1.00 60.63  ? 166 THR   B CG2 1 
ATOM   1460 N N   . GLN   B 2 158 ? -17.611 -6.789  -12.647 1.00 58.58  ? 167 GLN   B N   1 
ATOM   1461 C CA  . GLN   B 2 158 ? -19.017 -7.072  -12.451 1.00 59.05  ? 167 GLN   B CA  1 
ATOM   1462 C C   . GLN   B 2 158 ? -19.297 -7.201  -10.935 1.00 60.76  ? 167 GLN   B C   1 
ATOM   1463 O O   . GLN   B 2 158 ? -18.434 -7.632  -10.174 1.00 60.22  ? 167 GLN   B O   1 
ATOM   1464 C CB  . GLN   B 2 158 ? -19.396 -8.353  -13.203 1.00 59.11  ? 167 GLN   B CB  1 
ATOM   1465 C CG  . GLN   B 2 158 ? -20.874 -8.714  -13.161 1.00 61.09  ? 167 GLN   B CG  1 
ATOM   1466 C CD  . GLN   B 2 158 ? -21.771 -7.718  -13.854 1.00 64.11  ? 167 GLN   B CD  1 
ATOM   1467 O OE1 . GLN   B 2 158 ? -21.820 -6.533  -13.511 1.00 65.42  ? 167 GLN   B OE1 1 
ATOM   1468 N NE2 . GLN   B 2 158 ? -22.534 -8.183  -14.821 1.00 63.87  ? 167 GLN   B NE2 1 
ATOM   1469 N N   . GLY   B 2 159 ? -20.478 -6.785  -10.517 1.00 62.48  ? 168 GLY   B N   1 
ATOM   1470 C CA  . GLY   B 2 159 ? -20.883 -6.891  -9.130  1.00 65.09  ? 168 GLY   B CA  1 
ATOM   1471 C C   . GLY   B 2 159 ? -21.612 -8.187  -8.857  1.00 67.90  ? 168 GLY   B C   1 
ATOM   1472 O O   . GLY   B 2 159 ? -21.563 -9.132  -9.653  1.00 67.80  ? 168 GLY   B O   1 
ATOM   1473 N N   . LYS   B 2 160 ? -22.311 -8.227  -7.724  1.00 70.32  ? 169 LYS   B N   1 
ATOM   1474 C CA  . LYS   B 2 160 ? -23.085 -9.387  -7.303  1.00 72.94  ? 169 LYS   B CA  1 
ATOM   1475 C C   . LYS   B 2 160 ? -24.550 -8.958  -7.152  1.00 75.48  ? 169 LYS   B C   1 
ATOM   1476 O O   . LYS   B 2 160 ? -24.827 -7.924  -6.544  1.00 75.98  ? 169 LYS   B O   1 
ATOM   1477 C CB  . LYS   B 2 160 ? -22.539 -9.928  -5.962  1.00 74.93  ? 169 LYS   B CB  1 
ATOM   1478 C CG  . LYS   B 2 160 ? -23.003 -11.340 -5.637  1.00 79.05  ? 169 LYS   B CG  1 
ATOM   1479 C CD  . LYS   B 2 160 ? -22.340 -11.893 -4.382  1.00 83.61  ? 169 LYS   B CD  1 
ATOM   1480 C CE  . LYS   B 2 160 ? -22.820 -13.289 -4.061  1.00 87.32  ? 169 LYS   B CE  1 
ATOM   1481 N NZ  . LYS   B 2 160 ? -23.070 -13.462 -2.601  1.00 90.47  ? 169 LYS   B NZ  1 
ATOM   1482 N N   . ARG   B 2 161 ? -25.482 -9.728  -7.720  1.00 77.00  ? 170 ARG   B N   1 
ATOM   1483 C CA  . ARG   B 2 161 ? -26.905 -9.421  -7.597  1.00 78.81  ? 170 ARG   B CA  1 
ATOM   1484 C C   . ARG   B 2 161 ? -27.441 -10.219 -6.413  1.00 80.47  ? 170 ARG   B C   1 
ATOM   1485 O O   . ARG   B 2 161 ? -27.490 -11.447 -6.482  1.00 80.95  ? 170 ARG   B O   1 
ATOM   1486 C CB  . ARG   B 2 161 ? -27.660 -9.790  -8.890  1.00 80.04  ? 170 ARG   B CB  1 
ATOM   1487 C CG  . ARG   B 2 161 ? -29.142 -9.440  -8.858  1.00 82.59  ? 170 ARG   B CG  1 
ATOM   1488 C CD  . ARG   B 2 161 ? -29.866 -9.880  -10.115 1.00 85.62  ? 170 ARG   B CD  1 
ATOM   1489 N NE  . ARG   B 2 161 ? -31.312 -9.687  -9.998  1.00 88.06  ? 170 ARG   B NE  1 
ATOM   1490 C CZ  . ARG   B 2 161 ? -32.014 -8.800  -10.697 1.00 89.67  ? 170 ARG   B CZ  1 
ATOM   1491 N NH1 . ARG   B 2 161 ? -31.416 -8.029  -11.597 1.00 88.71  ? 170 ARG   B NH1 1 
ATOM   1492 N NH2 . ARG   B 2 161 ? -33.322 -8.686  -10.509 1.00 89.63  ? 170 ARG   B NH2 1 
ATOM   1493 N N   . GLU   B 2 162 ? -27.795 -9.543  -5.314  1.00 81.17  ? 171 GLU   B N   1 
ATOM   1494 C CA  . GLU   B 2 162 ? -28.292 -10.238 -4.124  1.00 82.53  ? 171 GLU   B CA  1 
ATOM   1495 C C   . GLU   B 2 162 ? -29.731 -10.742 -4.299  1.00 83.06  ? 171 GLU   B C   1 
ATOM   1496 O O   . GLU   B 2 162 ? -29.955 -11.947 -4.419  1.00 83.21  ? 171 GLU   B O   1 
ATOM   1497 C CB  . GLU   B 2 162 ? -28.169 -9.345  -2.872  1.00 85.34  ? 171 GLU   B CB  1 
ATOM   1498 C CG  . GLU   B 2 162 ? -26.747 -9.189  -2.356  1.00 90.97  ? 171 GLU   B CG  1 
ATOM   1499 C CD  . GLU   B 2 162 ? -26.282 -10.285 -1.413  1.00 98.28  ? 171 GLU   B CD  1 
ATOM   1500 O OE1 . GLU   B 2 162 ? -26.514 -10.149 -0.188  1.00 99.62  ? 171 GLU   B OE1 1 
ATOM   1501 O OE2 . GLU   B 2 162 ? -25.682 -11.275 -1.894  1.00 100.36 ? 171 GLU   B OE2 1 
HETATM 1502 S S   . DMS   C 3 .   ? -18.744 12.182  -0.324  1.00 98.60  ? 201 DMS   B S   1 
HETATM 1503 O O   . DMS   C 3 .   ? -19.700 11.037  -0.415  1.00 98.44  ? 201 DMS   B O   1 
HETATM 1504 C C1  . DMS   C 3 .   ? -19.625 13.695  -0.799  1.00 98.66  ? 201 DMS   B C1  1 
HETATM 1505 C C2  . DMS   C 3 .   ? -17.704 12.188  -1.813  1.00 98.40  ? 201 DMS   B C2  1 
HETATM 1506 N N1  . A1B84 D 4 .   ? -10.295 7.632   -13.778 1.00 62.38  ? 202 A1B84 B N1  1 
HETATM 1507 N N3  . A1B84 D 4 .   ? -9.180  3.219   -7.285  1.00 62.78  ? 202 A1B84 B N3  1 
HETATM 1508 C C4  . A1B84 D 4 .   ? -8.919  3.404   -11.865 1.00 63.43  ? 202 A1B84 B C4  1 
HETATM 1509 C C5  . A1B84 D 4 .   ? -9.405  2.597   -10.855 1.00 63.19  ? 202 A1B84 B C5  1 
HETATM 1510 C C6  . A1B84 D 4 .   ? -9.395  3.072   -9.553  1.00 62.99  ? 202 A1B84 B C6  1 
HETATM 1511 C C7  . A1B84 D 4 .   ? -8.968  4.361   -9.267  1.00 63.23  ? 202 A1B84 B C7  1 
HETATM 1512 C C8  . A1B84 D 4 .   ? -8.465  5.182   -10.270 1.00 63.45  ? 202 A1B84 B C8  1 
HETATM 1513 C C10 . A1B84 D 4 .   ? -9.879  2.414   -8.296  1.00 62.52  ? 202 A1B84 B C10 1 
HETATM 1514 C C13 . A1B84 D 4 .   ? -6.164  5.631   -17.295 1.00 62.72  ? 202 A1B84 B C13 1 
HETATM 1515 C C15 . A1B84 D 4 .   ? -8.037  4.889   -18.774 1.00 62.47  ? 202 A1B84 B C15 1 
HETATM 1516 C C17 . A1B84 D 4 .   ? -10.199 4.524   -17.776 1.00 62.55  ? 202 A1B84 B C17 1 
HETATM 1517 C C1  . A1B84 D 4 .   ? -9.596  6.724   -13.841 1.00 62.46  ? 202 A1B84 B C1  1 
HETATM 1518 C C2  . A1B84 D 4 .   ? -8.686  5.543   -13.867 1.00 62.89  ? 202 A1B84 B C2  1 
HETATM 1519 N N2  . A1B84 D 4 .   ? -7.953  5.463   -12.610 1.00 63.74  ? 202 A1B84 B N2  1 
HETATM 1520 C C3  . A1B84 D 4 .   ? -8.407  4.670   -11.568 1.00 63.42  ? 202 A1B84 B C3  1 
HETATM 1521 C C9  . A1B84 D 4 .   ? -9.086  4.600   -7.789  1.00 63.06  ? 202 A1B84 B C9  1 
HETATM 1522 C C11 . A1B84 D 4 .   ? -7.800  5.541   -15.101 1.00 62.78  ? 202 A1B84 B C11 1 
HETATM 1523 C C12 . A1B84 D 4 .   ? -6.460  5.893   -15.031 1.00 62.87  ? 202 A1B84 B C12 1 
HETATM 1524 N N4  . A1B84 D 4 .   ? -5.653  5.911   -16.108 1.00 62.98  ? 202 A1B84 B N4  1 
HETATM 1525 C C14 . A1B84 D 4 .   ? -7.511  5.243   -17.513 1.00 62.60  ? 202 A1B84 B C14 1 
HETATM 1526 C C16 . A1B84 D 4 .   ? -9.351  4.543   -18.895 1.00 62.47  ? 202 A1B84 B C16 1 
HETATM 1527 C C18 . A1B84 D 4 .   ? -9.712  4.822   -16.537 1.00 62.43  ? 202 A1B84 B C18 1 
HETATM 1528 C C19 . A1B84 D 4 .   ? -8.359  5.207   -16.370 1.00 62.52  ? 202 A1B84 B C19 1 
HETATM 1529 O O   . HOH   E 5 .   ? -9.423  -8.291  -29.440 1.00 67.72  ? 101 HOH   A O   1 
HETATM 1530 O O   . HOH   E 5 .   ? -21.935 20.896  -10.104 1.00 52.84  ? 102 HOH   A O   1 
HETATM 1531 O O   . HOH   E 5 .   ? -23.686 19.317  -19.543 1.00 64.46  ? 103 HOH   A O   1 
HETATM 1532 O O   . HOH   E 5 .   ? -6.882  -8.951  -3.266  1.00 48.92  ? 104 HOH   A O   1 
HETATM 1533 O O   . HOH   E 5 .   ? 6.908   -4.538  -16.827 1.00 61.32  ? 105 HOH   A O   1 
HETATM 1534 O O   . HOH   E 5 .   ? -1.981  -3.613  -6.209  1.00 44.90  ? 106 HOH   A O   1 
HETATM 1535 O O   . HOH   E 5 .   ? -24.402 9.445   -27.501 1.00 49.19  ? 107 HOH   A O   1 
HETATM 1536 O O   . HOH   E 5 .   ? -30.886 0.261   -22.984 1.00 68.27  ? 108 HOH   A O   1 
HETATM 1537 O O   . HOH   E 5 .   ? -28.572 -5.965  -27.909 1.00 40.16  ? 109 HOH   A O   1 
HETATM 1538 O O   . HOH   E 5 .   ? -22.549 -9.195  -34.690 1.00 58.77  ? 110 HOH   A O   1 
HETATM 1539 O O   . HOH   E 5 .   ? -2.272  0.443   -12.345 1.00 71.03  ? 111 HOH   A O   1 
HETATM 1540 O O   . HOH   E 5 .   ? -25.564 13.371  -23.904 1.00 48.49  ? 112 HOH   A O   1 
HETATM 1541 O O   . HOH   E 5 .   ? -8.135  4.407   -4.261  1.00 38.30  ? 113 HOH   A O   1 
HETATM 1542 O O   . HOH   E 5 .   ? -4.914  -10.321 -5.812  1.00 58.93  ? 114 HOH   A O   1 
HETATM 1543 O O   . HOH   E 5 .   ? -5.169  -15.209 -25.321 1.00 47.89  ? 115 HOH   A O   1 
HETATM 1544 O O   . HOH   E 5 .   ? -2.341  -8.317  -3.323  1.00 40.49  ? 116 HOH   A O   1 
HETATM 1545 O O   . HOH   E 5 .   ? -5.088  2.346   -10.491 1.00 52.27  ? 117 HOH   A O   1 
HETATM 1546 O O   . HOH   F 5 .   ? -16.410 26.343  -12.517 1.00 72.97  ? 301 HOH   B O   1 
HETATM 1547 O O   . HOH   F 5 .   ? -19.882 -12.108 -25.904 1.00 50.25  ? 302 HOH   B O   1 
HETATM 1548 O O   . HOH   F 5 .   ? -34.123 1.971   -15.126 1.00 63.10  ? 303 HOH   B O   1 
HETATM 1549 O O   . HOH   F 5 .   ? -16.692 21.195  -14.653 1.00 66.12  ? 304 HOH   B O   1 
HETATM 1550 O O   . HOH   F 5 .   ? -13.026 -2.370  -14.682 1.00 59.26  ? 305 HOH   B O   1 
HETATM 1551 O O   . HOH   F 5 .   ? -6.556  -0.214  -10.999 1.00 42.71  ? 306 HOH   B O   1 
HETATM 1552 O O   . HOH   F 5 .   ? -35.350 3.093   -8.354  1.00 47.33  ? 307 HOH   B O   1 
HETATM 1553 O O   . HOH   F 5 .   ? -31.016 13.144  -19.259 1.00 80.68  ? 308 HOH   B O   1 
HETATM 1554 O O   . HOH   F 5 .   ? -15.469 9.634   -0.671  1.00 57.38  ? 309 HOH   B O   1 
HETATM 1555 O O   . HOH   F 5 .   ? -35.835 -5.442  -10.269 1.00 53.29  ? 310 HOH   B O   1 
HETATM 1556 O O   . HOH   F 5 .   ? -12.101 2.067   -5.937  1.00 44.66  ? 311 HOH   B O   1 
HETATM 1557 O O   . HOH   F 5 .   ? -22.986 -6.417  -5.216  1.00 53.47  ? 312 HOH   B O   1 
HETATM 1558 O O   . HOH   F 5 .   ? -16.376 -14.647 -16.542 1.00 56.66  ? 313 HOH   B O   1 
HETATM 1559 O O   . HOH   F 5 .   ? -17.948 -10.606 -16.512 1.00 55.39  ? 314 HOH   B O   1 
HETATM 1560 O O   . HOH   F 5 .   ? -17.032 13.060  -5.368  1.00 57.69  ? 315 HOH   B O   1 
HETATM 1561 O O   . HOH   F 5 .   ? -8.155  -11.008 -6.670  1.00 59.67  ? 316 HOH   B O   1 
HETATM 1562 O O   . HOH   F 5 .   ? -31.325 12.972  -16.404 1.00 60.28  ? 317 HOH   B O   1 
HETATM 1563 O O   . HOH   F 5 .   ? -19.021 15.145  -22.318 1.00 45.99  ? 318 HOH   B O   1 
HETATM 1564 O O   . HOH   F 5 .   ? -28.599 -6.768  -18.277 1.00 60.09  ? 319 HOH   B O   1 
HETATM 1565 O O   . HOH   F 5 .   ? -17.130 -14.701 -31.176 1.00 60.33  ? 320 HOH   B O   1 
HETATM 1566 O O   . HOH   F 5 .   ? -15.283 -5.117  1.178   1.00 46.61  ? 321 HOH   B O   1 
HETATM 1567 O O   . HOH   F 5 .   ? -21.275 7.090   0.000   0.50 42.32  ? 322 HOH   B O   1 
HETATM 1568 O O   . HOH   F 5 .   ? -21.200 14.445  -33.433 1.00 50.26  ? 323 HOH   B O   1 
HETATM 1569 O O   . HOH   F 5 .   ? -19.405 -5.934  -0.680  1.00 61.62  ? 324 HOH   B O   1 
HETATM 1570 O O   . HOH   F 5 .   ? -22.047 -14.277 -21.849 1.00 64.36  ? 325 HOH   B O   1 
HETATM 1571 O O   . HOH   F 5 .   ? -2.790  -11.602 -7.041  1.00 70.37  ? 326 HOH   B O   1 
HETATM 1572 O O   . HOH   F 5 .   ? -26.682 -7.929  -16.614 1.00 44.28  ? 327 HOH   B O   1 
HETATM 1573 O O   . HOH   F 5 .   ? -30.157 -1.698  -19.133 1.00 62.15  ? 328 HOH   B O   1 
HETATM 1574 O O   . HOH   F 5 .   ? -14.582 16.749  -20.183 1.00 42.87  ? 329 HOH   B O   1 
HETATM 1575 O O   . HOH   F 5 .   ? -29.918 -4.361  -21.844 1.00 70.74  ? 330 HOH   B O   1 
HETATM 1576 O O   . HOH   F 5 .   ? -18.329 19.244  -22.275 1.00 49.84  ? 331 HOH   B O   1 
HETATM 1577 O O   . HOH   F 5 .   ? -32.529 7.722   -4.448  1.00 68.61  ? 332 HOH   B O   1 
HETATM 1578 O O   . HOH   F 5 .   ? -16.994 16.719  -22.118 1.00 53.50  ? 333 HOH   B O   1 
HETATM 1579 O O   . HOH   F 5 .   ? -25.862 -5.043  -3.989  1.00 61.63  ? 334 HOH   B O   1 
HETATM 1580 O O   . HOH   F 5 .   ? -18.366 12.723  -31.651 1.00 50.03  ? 335 HOH   B O   1 
HETATM 1581 O O   . HOH   F 5 .   ? -30.903 4.557   -2.169  1.00 63.75  ? 336 HOH   B O   1 
HETATM 1582 O O   . HOH   F 5 .   ? -10.555 23.276  -13.025 1.00 74.69  ? 337 HOH   B O   1 
HETATM 1583 O O   . HOH   F 5 .   ? -21.903 -12.217 -12.692 1.00 69.75  ? 338 HOH   B O   1 
HETATM 1584 O O   . HOH   F 5 .   ? -15.198 -12.249 -16.209 1.00 52.04  ? 339 HOH   B O   1 
HETATM 1585 O O   . HOH   F 5 .   ? -1.140  -14.516 -10.222 1.00 56.25  ? 340 HOH   B O   1 
HETATM 1586 O O   . HOH   F 5 .   ? -18.385 26.286  -14.289 1.00 74.60  ? 341 HOH   B O   1 
HETATM 1587 O O   . HOH   F 5 .   ? -20.175 -13.265 -23.311 1.00 56.55  ? 342 HOH   B O   1 
HETATM 1588 O O   . HOH   F 5 .   ? -20.876 25.286  -17.503 1.00 56.02  ? 343 HOH   B O   1 
HETATM 1589 O O   . HOH   F 5 .   ? -19.971 7.279   -33.109 1.00 46.98  ? 344 HOH   B O   1 
HETATM 1590 O O   . HOH   F 5 .   ? -21.275 3.261   0.000   0.50 101.08 ? 345 HOH   B O   1 
HETATM 1591 O O   . HOH   F 5 .   ? -31.197 -7.761  -5.458  1.00 61.00  ? 346 HOH   B O   1 
HETATM 1592 O O   . HOH   F 5 .   ? -30.911 -10.147 -28.398 1.00 48.42  ? 347 HOH   B O   1 
HETATM 1593 O O   . HOH   F 5 .   ? -27.865 -17.307 -18.847 1.00 58.76  ? 348 HOH   B O   1 
HETATM 1594 O O   . HOH   F 5 .   ? -22.814 -7.620  -2.524  1.00 62.17  ? 349 HOH   B O   1 
HETATM 1595 O O   . HOH   F 5 .   ? -19.323 -12.111 -13.422 1.00 40.13  ? 350 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP   A 7   ? 1.3090 0.9014 0.5397 0.2608  -0.1688 -0.0972 50  ASP   A N   
2    C CA  . ASP   A 7   ? 1.3015 0.9392 0.5089 0.2844  -0.1584 -0.0952 50  ASP   A CA  
3    C C   . ASP   A 7   ? 1.2762 0.9275 0.4848 0.2757  -0.1375 -0.0672 50  ASP   A C   
4    O O   . ASP   A 7   ? 1.2913 0.9027 0.4898 0.2769  -0.1351 -0.0539 50  ASP   A O   
5    C CB  . ASP   A 7   ? 1.3554 0.9749 0.5322 0.3193  -0.1712 -0.1138 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.4216 1.0963 0.5832 0.3433  -0.1606 -0.1148 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.4140 1.1279 0.5716 0.3540  -0.1612 -0.1288 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.4563 1.1361 0.6109 0.3517  -0.1513 -0.1011 50  ASP   A OD2 
9    N N   . MET   A 8   ? 1.2328 0.9377 0.4516 0.2680  -0.1233 -0.0584 51  MET   A N   
10   C CA  . MET   A 8   ? 1.2102 0.9320 0.4313 0.2594  -0.1056 -0.0356 51  MET   A CA  
11   C C   . MET   A 8   ? 1.1887 0.9282 0.3898 0.2835  -0.1026 -0.0343 51  MET   A C   
12   O O   . MET   A 8   ? 1.1789 0.9423 0.3719 0.3046  -0.1081 -0.0497 51  MET   A O   
13   C CB  . MET   A 8   ? 1.1958 0.9624 0.4387 0.2408  -0.0937 -0.0283 51  MET   A CB  
14   C CG  . MET   A 8   ? 1.2171 0.9722 0.4851 0.2177  -0.0976 -0.0299 51  MET   A CG  
15   S SD  . MET   A 8   ? 1.2439 1.0495 0.5366 0.1993  -0.0849 -0.0214 51  MET   A SD  
16   C CE  . MET   A 8   ? 1.2124 0.9979 0.5376 0.1768  -0.0960 -0.0286 51  MET   A CE  
17   N N   . TYR   A 9   ? 1.1694 0.8985 0.3629 0.2814  -0.0939 -0.0161 52  TYR   A N   
18   C CA  . TYR   A 9   ? 1.1588 0.9045 0.3366 0.3030  -0.0933 -0.0143 52  TYR   A CA  
19   C C   . TYR   A 9   ? 1.1436 0.9077 0.3236 0.2928  -0.0806 0.0031  52  TYR   A C   
20   O O   . TYR   A 9   ? 1.1380 0.8892 0.3249 0.2716  -0.0709 0.0171  52  TYR   A O   
21   C CB  . TYR   A 9   ? 1.1814 0.8788 0.3329 0.3253  -0.1050 -0.0162 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 1.2154 0.8547 0.3534 0.3151  -0.1016 0.0034  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 1.2384 0.8312 0.3841 0.2989  -0.1046 0.0047  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 1.2389 0.8665 0.3549 0.3248  -0.0968 0.0199  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 1.2694 0.8076 0.4060 0.2882  -0.0981 0.0259  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 1.2714 0.8440 0.3701 0.3177  -0.0903 0.0415  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.2951 0.8225 0.4055 0.2985  -0.0892 0.0459  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.3412 0.8132 0.4383 0.2898  -0.0794 0.0704  52  TYR   A OH  
29   N N   . ILE   A 10  ? 1.1271 0.9231 0.3031 0.3089  -0.0814 0.0007  53  ILE   A N   
30   C CA  . ILE   A 10  ? 1.1131 0.9275 0.2897 0.3026  -0.0732 0.0123  53  ILE   A CA  
31   C C   . ILE   A 10  ? 1.1372 0.9340 0.2867 0.3247  -0.0805 0.0167  53  ILE   A C   
32   O O   . ILE   A 10  ? 1.1407 0.9396 0.2825 0.3485  -0.0925 0.0056  53  ILE   A O   
33   C CB  . ILE   A 10  ? 1.0751 0.9485 0.2790 0.2958  -0.0676 0.0055  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 1.0571 0.9668 0.2699 0.3165  -0.0751 -0.0090 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 1.0676 0.9546 0.2917 0.2762  -0.0605 0.0039  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 1.0333 0.9979 0.2767 0.3079  -0.0677 -0.0122 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 1.1510 0.9303 0.2838 0.3192  -0.0732 0.0329  54  GLU   A N   
38   C CA  . GLU   A 11  ? 1.1783 0.9392 0.2782 0.3409  -0.0796 0.0395  54  GLU   A CA  
39   C C   . GLU   A 11  ? 1.1697 0.9658 0.2744 0.3365  -0.0754 0.0403  54  GLU   A C   
40   O O   . GLU   A 11  ? 1.1678 0.9698 0.2837 0.3147  -0.0614 0.0487  54  GLU   A O   
41   C CB  . GLU   A 11  ? 1.2425 0.9410 0.3096 0.3393  -0.0718 0.0616  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.3394 0.9895 0.3993 0.3426  -0.0768 0.0628  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.4792 1.0647 0.5059 0.3435  -0.0684 0.0877  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.4839 1.0652 0.5001 0.3328  -0.0524 0.1064  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.5555 1.0931 0.5658 0.3558  -0.0768 0.0892  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 1.1588 0.9767 0.2557 0.3580  -0.0886 0.0306  55  ARG   A N   
47   C CA  . ARG   A 12  ? 1.1427 0.9917 0.2454 0.3549  -0.0885 0.0273  55  ARG   A CA  
48   C C   . ARG   A 12  ? 1.1687 0.9842 0.2323 0.3562  -0.0794 0.0453  55  ARG   A C   
49   O O   . ARG   A 12  ? 1.1974 0.9693 0.2206 0.3726  -0.0803 0.0583  55  ARG   A O   
50   C CB  . ARG   A 12  ? 1.1408 1.0250 0.2527 0.3770  -0.1084 0.0084  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 1.1399 1.0659 0.2764 0.3690  -0.1113 -0.0023 55  ARG   A CG  
52   C CD  . ARG   A 12  ? 1.1534 1.1093 0.2982 0.3925  -0.1342 -0.0212 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 1.1601 1.1590 0.3413 0.3813  -0.1389 -0.0352 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 1.2033 1.2021 0.3673 0.3898  -0.1496 -0.0413 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 1.2463 1.2064 0.3528 0.4119  -0.1552 -0.0326 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 1.1774 1.2127 0.3799 0.3777  -0.1551 -0.0560 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 1.1564 0.9908 0.2303 0.3406  -0.0691 0.0471  56  ALA   A N   
58   C CA  . ALA   A 13  ? 1.1800 0.9888 0.2175 0.3426  -0.0570 0.0638  56  ALA   A CA  
59   C C   . ALA   A 13  ? 1.1835 1.0146 0.2082 0.3557  -0.0662 0.0529  56  ALA   A C   
60   O O   . ALA   A 13  ? 1.2034 1.0188 0.1979 0.3584  -0.0546 0.0648  56  ALA   A O   
61   C CB  . ALA   A 13  ? 1.1767 0.9800 0.2318 0.3147  -0.0341 0.0779  56  ALA   A CB  
62   N N   . GLY   A 14  ? 1.1651 1.0329 0.2140 0.3641  -0.0865 0.0300  57  GLY   A N   
63   C CA  . GLY   A 14  ? 1.1705 1.0589 0.2119 0.3769  -0.1005 0.0150  57  GLY   A CA  
64   C C   . GLY   A 14  ? 1.1495 1.0848 0.2451 0.3606  -0.1074 -0.0053 57  GLY   A C   
65   O O   . GLY   A 14  ? 1.1200 1.0754 0.2587 0.3398  -0.0997 -0.0064 57  GLY   A O   
66   N N   . ASP   A 15  ? 1.1603 1.1113 0.2522 0.3715  -0.1230 -0.0219 58  ASP   A N   
67   C CA  . ASP   A 15  ? 1.1429 1.1336 0.2864 0.3567  -0.1316 -0.0419 58  ASP   A CA  
68   C C   . ASP   A 15  ? 1.1554 1.1428 0.3071 0.3352  -0.1127 -0.0345 58  ASP   A C   
69   O O   . ASP   A 15  ? 1.1817 1.1408 0.2931 0.3387  -0.0982 -0.0192 58  ASP   A O   
70   C CB  . ASP   A 15  ? 1.1544 1.1582 0.2892 0.3787  -0.1597 -0.0655 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 1.1991 1.2211 0.3434 0.3994  -0.1843 -0.0804 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 1.1981 1.2164 0.3453 0.4012  -0.1786 -0.0705 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 1.2282 1.2679 0.3762 0.4161  -0.2110 -0.1036 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 1.1354 1.1525 0.3401 0.3145  -0.1126 -0.0449 59  ILE   A N   
75   C CA  . ILE   A 16  ? 1.1423 1.1573 0.3567 0.2972  -0.0984 -0.0407 59  ILE   A CA  
76   C C   . ILE   A 16  ? 1.1559 1.1781 0.3714 0.3059  -0.1166 -0.0624 59  ILE   A C   
77   O O   . ILE   A 16  ? 1.1288 1.1775 0.3905 0.2980  -0.1312 -0.0805 59  ILE   A O   
78   C CB  . ILE   A 16  ? 1.1188 1.1536 0.3831 0.2710  -0.0852 -0.0353 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 1.1350 1.1559 0.3882 0.2653  -0.0686 -0.0158 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 1.1191 1.1544 0.3981 0.2561  -0.0758 -0.0351 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 1.1241 1.1643 0.4169 0.2469  -0.0592 -0.0119 59  ILE   A CD1 
82   N N   . THR   A 17  ? 1.1982 1.1963 0.3613 0.3245  -0.1169 -0.0613 60  THR   A N   
83   C CA  . THR   A 17  ? 1.2228 1.2223 0.3756 0.3383  -0.1365 -0.0842 60  THR   A CA  
84   C C   . THR   A 17  ? 1.2644 1.2430 0.3815 0.3423  -0.1208 -0.0772 60  THR   A C   
85   O O   . THR   A 17  ? 1.2754 1.2351 0.3598 0.3434  -0.0970 -0.0534 60  THR   A O   
86   C CB  . THR   A 17  ? 1.2523 1.2460 0.3643 0.3706  -0.1613 -0.0972 60  THR   A CB  
87   O OG1 . THR   A 17  ? 1.3007 1.2618 0.3447 0.3904  -0.1467 -0.0758 60  THR   A OG1 
88   C CG2 . THR   A 17  ? 1.2323 1.2507 0.3803 0.3716  -0.1795 -0.1071 60  THR   A CG2 
89   N N   . TRP   A 18  ? 1.2863 1.2680 0.4100 0.3463  -0.1349 -0.0993 61  TRP   A N   
90   C CA  . TRP   A 18  ? 1.3361 1.2995 0.4218 0.3565  -0.1227 -0.0971 61  TRP   A CA  
91   C C   . TRP   A 18  ? 1.3930 1.3371 0.4058 0.3933  -0.1319 -0.1007 61  TRP   A C   
92   O O   . TRP   A 18  ? 1.3940 1.3427 0.3980 0.4117  -0.1617 -0.1227 61  TRP   A O   
93   C CB  . TRP   A 18  ? 1.3231 1.2930 0.4426 0.3489  -0.1367 -0.1218 61  TRP   A CB  
94   C CG  . TRP   A 18  ? 1.3489 1.3015 0.4320 0.3617  -0.1255 -0.1231 61  TRP   A CG  
95   C CD1 . TRP   A 18  ? 1.3845 1.3232 0.4180 0.3920  -0.1406 -0.1427 61  TRP   A CD1 
96   C CD2 . TRP   A 18  ? 1.3468 1.2967 0.4426 0.3466  -0.0987 -0.1069 61  TRP   A CD2 
97   N NE1 . TRP   A 18  ? 1.3986 1.3262 0.4117 0.3973  -0.1221 -0.1386 61  TRP   A NE1 
98   C CE2 . TRP   A 18  ? 1.3762 1.3116 0.4296 0.3692  -0.0967 -0.1167 61  TRP   A CE2 
99   C CE3 . TRP   A 18  ? 1.3323 1.2916 0.4683 0.3191  -0.0770 -0.0857 61  TRP   A CE3 
100  C CZ2 . TRP   A 18  ? 1.3811 1.3136 0.4366 0.3641  -0.0731 -0.1059 61  TRP   A CZ2 
101  C CZ3 . TRP   A 18  ? 1.3396 1.2954 0.4777 0.3139  -0.0563 -0.0759 61  TRP   A CZ3 
102  C CH2 . TRP   A 18  ? 1.3600 1.3037 0.4600 0.3360  -0.0538 -0.0854 61  TRP   A CH2 
103  N N   . GLU   A 19  ? 1.4385 1.3624 0.4000 0.4048  -0.1059 -0.0784 62  GLU   A N   
104  C CA  . GLU   A 19  ? 1.4990 1.4017 0.3838 0.4418  -0.1089 -0.0766 62  GLU   A CA  
105  C C   . GLU   A 19  ? 1.5451 1.4400 0.3952 0.4605  -0.1074 -0.0901 62  GLU   A C   
106  O O   . GLU   A 19  ? 1.5552 1.4480 0.4062 0.4510  -0.0783 -0.0737 62  GLU   A O   
107  C CB  . GLU   A 19  ? 1.5429 1.4258 0.3902 0.4442  -0.0775 -0.0387 62  GLU   A CB  
108  C CG  . GLU   A 19  ? 1.6517 1.5088 0.4133 0.4834  -0.0741 -0.0304 62  GLU   A CG  
109  C CD  . GLU   A 19  ? 1.7326 1.5671 0.4575 0.4841  -0.0354 0.0102  62  GLU   A CD  
110  O OE1 . GLU   A 19  ? 1.7273 1.5674 0.4970 0.4525  -0.0117 0.0302  62  GLU   A OE1 
111  O OE2 . GLU   A 19  ? 1.7717 1.5825 0.4235 0.5168  -0.0291 0.0221  62  GLU   A OE2 
112  N N   . LYS   A 20  ? 1.5682 1.4604 0.3898 0.4883  -0.1397 -0.1218 63  LYS   A N   
113  C CA  . LYS   A 20  ? 1.6093 1.4911 0.3897 0.5116  -0.1400 -0.1374 63  LYS   A CA  
114  C C   . LYS   A 20  ? 1.6597 1.5201 0.3555 0.5424  -0.1137 -0.1111 63  LYS   A C   
115  O O   . LYS   A 20  ? 1.6781 1.5271 0.3333 0.5602  -0.1178 -0.0991 63  LYS   A O   
116  C CB  . LYS   A 20  ? 1.6474 1.5305 0.4197 0.5345  -0.1858 -0.1820 63  LYS   A CB  
117  C CG  . LYS   A 20  ? 1.6771 1.5821 0.5334 0.5066  -0.2160 -0.2079 63  LYS   A CG  
118  C CD  . LYS   A 20  ? 1.7380 1.6437 0.5837 0.5323  -0.2638 -0.2535 63  LYS   A CD  
119  C CE  . LYS   A 20  ? 1.7470 1.6784 0.6740 0.5086  -0.2954 -0.2767 63  LYS   A CE  
120  N NZ  . LYS   A 20  ? 1.7637 1.6970 0.6938 0.5285  -0.3428 -0.3246 63  LYS   A NZ  
121  N N   . ASP   A 21  ? 1.6791 1.5340 0.3488 0.5498  -0.0858 -0.1009 64  ASP   A N   
122  C CA  . ASP   A 21  ? 1.7236 1.5612 0.3176 0.5769  -0.0532 -0.0718 64  ASP   A CA  
123  C C   . ASP   A 21  ? 1.7165 1.5521 0.3292 0.5514  -0.0168 -0.0278 64  ASP   A C   
124  O O   . ASP   A 21  ? 1.7436 1.5600 0.3029 0.5689  -0.0007 -0.0015 64  ASP   A O   
125  C CB  . ASP   A 21  ? 1.7863 1.6043 0.2947 0.6245  -0.0746 -0.0826 64  ASP   A CB  
126  C CG  . ASP   A 21  ? 1.8791 1.6964 0.3605 0.6545  -0.1108 -0.1279 64  ASP   A CG  
127  O OD1 . ASP   A 21  ? 1.8835 1.7074 0.3844 0.6494  -0.1053 -0.1426 64  ASP   A OD1 
128  O OD2 . ASP   A 21  ? 1.9393 1.7483 0.3789 0.6851  -0.1461 -0.1500 64  ASP   A OD2 
129  N N   . ALA   A 22  ? 1.6751 1.5283 0.3633 0.5109  -0.0052 -0.0205 65  ALA   A N   
130  C CA  . ALA   A 22  ? 1.6670 1.5203 0.3830 0.4835  0.0263  0.0161  65  ALA   A CA  
131  C C   . ALA   A 22  ? 1.6696 1.5266 0.3759 0.4824  0.0687  0.0406  65  ALA   A C   
132  O O   . ALA   A 22  ? 1.6803 1.5437 0.3685 0.4993  0.0719  0.0263  65  ALA   A O   
133  C CB  . ALA   A 22  ? 1.6324 1.5046 0.4311 0.4440  0.0158  0.0097  65  ALA   A CB  
134  N N   . GLU   A 23  ? 1.6573 1.5105 0.3760 0.4641  0.1007  0.0763  66  GLU   A N   
135  C CA  . GLU   A 23  ? 1.6494 1.5116 0.3702 0.4596  0.1424  0.1013  66  GLU   A CA  
136  C C   . GLU   A 23  ? 1.6052 1.4966 0.3922 0.4358  0.1435  0.0876  66  GLU   A C   
137  O O   . GLU   A 23  ? 1.5794 1.4813 0.4277 0.4045  0.1334  0.0847  66  GLU   A O   
138  C CB  . GLU   A 23  ? 1.6829 1.5341 0.4161 0.4397  0.1711  0.1400  66  GLU   A CB  
139  C CG  . GLU   A 23  ? 1.7422 1.6057 0.4854 0.4324  0.2165  0.1687  66  GLU   A CG  
140  C CD  . GLU   A 23  ? 1.8181 1.6659 0.5741 0.4125  0.2434  0.2065  66  GLU   A CD  
141  O OE1 . GLU   A 23  ? 1.7954 1.6399 0.5997 0.3840  0.2295  0.2064  66  GLU   A OE1 
142  O OE2 . GLU   A 23  ? 1.8659 1.7028 0.5828 0.4263  0.2789  0.2364  66  GLU   A OE2 
143  N N   . VAL   A 24  ? 1.5967 1.4995 0.3674 0.4539  0.1544  0.0779  67  VAL   A N   
144  C CA  . VAL   A 24  ? 1.5656 1.4928 0.3929 0.4369  0.1545  0.0641  67  VAL   A CA  
145  C C   . VAL   A 24  ? 1.5356 1.4839 0.3921 0.4232  0.1960  0.0925  67  VAL   A C   
146  O O   . VAL   A 24  ? 1.5484 1.5013 0.3672 0.4463  0.2236  0.1035  67  VAL   A O   
147  C CB  . VAL   A 24  ? 1.5848 1.5114 0.3857 0.4646  0.1357  0.0305  67  VAL   A CB  
148  C CG1 . VAL   A 24  ? 1.5695 1.5137 0.4335 0.4443  0.1272  0.0143  67  VAL   A CG1 
149  C CG2 . VAL   A 24  ? 1.6060 1.5121 0.3710 0.4834  0.0959  0.0026  67  VAL   A CG2 
150  N N   . THR   A 25  ? 1.4921 1.4554 0.4161 0.3871  0.2006  0.1037  68  THR   A N   
151  C CA  . THR   A 25  ? 1.4621 1.4494 0.4240 0.3716  0.2366  0.1284  68  THR   A CA  
152  C C   . THR   A 25  ? 1.4195 1.4316 0.4577 0.3422  0.2281  0.1202  68  THR   A C   
153  O O   . THR   A 25  ? 1.4134 1.4209 0.4702 0.3344  0.1973  0.0985  68  THR   A O   
154  C CB  . THR   A 25  ? 1.4808 1.4551 0.4331 0.3615  0.2611  0.1626  68  THR   A CB  
155  O OG1 . THR   A 25  ? 1.4741 1.4723 0.4513 0.3549  0.3012  0.1871  68  THR   A OG1 
156  C CG2 . THR   A 25  ? 1.4709 1.4355 0.4640 0.3308  0.2436  0.1661  68  THR   A CG2 
157  N N   . GLY   A 26  ? 1.3887 1.4283 0.4697 0.3285  0.2556  0.1374  69  GLY   A N   
158  C CA  . GLY   A 26  ? 1.3561 1.4208 0.5058 0.3044  0.2485  0.1313  69  GLY   A CA  
159  C C   . GLY   A 26  ? 1.3401 1.4239 0.5017 0.3187  0.2449  0.1121  69  GLY   A C   
160  O O   . GLY   A 26  ? 1.3588 1.4292 0.4776 0.3446  0.2340  0.0935  69  GLY   A O   
161  N N   . ASN   A 27  ? 1.3034 1.4173 0.5236 0.3032  0.2513  0.1147  70  ASN   A N   
162  C CA  . ASN   A 27  ? 1.2900 1.4214 0.5265 0.3166  0.2467  0.0973  70  ASN   A CA  
163  C C   . ASN   A 27  ? 1.2616 1.3852 0.5287 0.3025  0.2135  0.0795  70  ASN   A C   
164  O O   . ASN   A 27  ? 1.2696 1.3772 0.5423 0.2840  0.1963  0.0806  70  ASN   A O   
165  C CB  . ASN   A 27  ? 1.2862 1.4596 0.5644 0.3157  0.2773  0.1113  70  ASN   A CB  
166  C CG  . ASN   A 27  ? 1.3102 1.5044 0.6482 0.2834  0.2837  0.1285  70  ASN   A CG  
167  O OD1 . ASN   A 27  ? 1.3373 1.5229 0.6724 0.2690  0.2962  0.1476  70  ASN   A OD1 
168  N ND2 . ASN   A 27  ? 1.2892 1.5089 0.6818 0.2726  0.2737  0.1212  70  ASN   A ND2 
169  N N   . SER   A 28  ? 1.2323 1.3642 0.5146 0.3138  0.2054  0.0639  71  SER   A N   
170  C CA  . SER   A 28  ? 1.2134 1.3356 0.5213 0.3033  0.1778  0.0503  71  SER   A CA  
171  C C   . SER   A 28  ? 1.1688 1.3219 0.5264 0.3001  0.1830  0.0527  71  SER   A C   
172  O O   . SER   A 28  ? 1.1683 1.3230 0.5271 0.3184  0.1796  0.0400  71  SER   A O   
173  C CB  . SER   A 28  ? 1.2508 1.3441 0.5263 0.3225  0.1580  0.0270  71  SER   A CB  
174  O OG  . SER   A 28  ? 1.3053 1.3767 0.5301 0.3357  0.1555  0.0211  71  SER   A OG  
175  N N   . PRO   A 29  ? 1.1293 1.3068 0.5288 0.2787  0.1897  0.0674  72  PRO   A N   
176  C CA  . PRO   A 29  ? 1.0892 1.3010 0.5380 0.2778  0.1929  0.0683  72  PRO   A CA  
177  C C   . PRO   A 29  ? 1.0675 1.2698 0.5344 0.2736  0.1667  0.0586  72  PRO   A C   
178  O O   . PRO   A 29  ? 1.0793 1.2549 0.5335 0.2619  0.1482  0.0560  72  PRO   A O   
179  C CB  . PRO   A 29  ? 1.0798 1.3194 0.5664 0.2562  0.2080  0.0858  72  PRO   A CB  
180  C CG  . PRO   A 29  ? 1.1077 1.3175 0.5708 0.2393  0.1990  0.0913  72  PRO   A CG  
181  C CD  . PRO   A 29  ? 1.1212 1.2961 0.5260 0.2562  0.1934  0.0822  72  PRO   A CD  
182  N N   . ARG   A 30  ? 1.0359 1.2609 0.5315 0.2852  0.1665  0.0541  73  ARG   A N   
183  C CA  . ARG   A 30  ? 1.0261 1.2427 0.5373 0.2853  0.1440  0.0478  73  ARG   A CA  
184  C C   . ARG   A 30  ? 0.9791 1.2341 0.5402 0.2730  0.1433  0.0554  73  ARG   A C   
185  O O   . ARG   A 30  ? 0.9530 1.2456 0.5463 0.2826  0.1554  0.0559  73  ARG   A O   
186  C CB  . ARG   A 30  ? 1.0569 1.2660 0.5593 0.3124  0.1416  0.0355  73  ARG   A CB  
187  C CG  . ARG   A 30  ? 1.1193 1.3148 0.6338 0.3163  0.1204  0.0315  73  ARG   A CG  
188  C CD  . ARG   A 30  ? 1.1823 1.3727 0.6931 0.3452  0.1200  0.0201  73  ARG   A CD  
189  N NE  . ARG   A 30  ? 1.2396 1.4112 0.7586 0.3506  0.1004  0.0191  73  ARG   A NE  
190  C CZ  . ARG   A 30  ? 1.2997 1.4234 0.7951 0.3501  0.0851  0.0151  73  ARG   A CZ  
191  N NH1 . ARG   A 30  ? 1.3179 1.4108 0.7839 0.3444  0.0841  0.0084  73  ARG   A NH1 
192  N NH2 . ARG   A 30  ? 1.3060 1.4125 0.8085 0.3557  0.0707  0.0184  73  ARG   A NH2 
193  N N   . LEU   A 31  ? 0.9653 1.2132 0.5342 0.2524  0.1290  0.0599  74  LEU   A N   
194  C CA  . LEU   A 31  ? 0.9311 1.2122 0.5453 0.2400  0.1236  0.0638  74  LEU   A CA  
195  C C   . LEU   A 31  ? 0.9232 1.1983 0.5436 0.2428  0.0990  0.0596  74  LEU   A C   
196  O O   . LEU   A 31  ? 0.9464 1.1859 0.5350 0.2433  0.0869  0.0586  74  LEU   A O   
197  C CB  . LEU   A 31  ? 0.9313 1.2105 0.5497 0.2156  0.1271  0.0717  74  LEU   A CB  
198  C CG  . LEU   A 31  ? 0.9547 1.2354 0.5629 0.2117  0.1524  0.0803  74  LEU   A CG  
199  C CD1 . LEU   A 31  ? 0.9694 1.2333 0.5705 0.1901  0.1513  0.0879  74  LEU   A CD1 
200  C CD2 . LEU   A 31  ? 0.9358 1.2617 0.5871 0.2150  0.1739  0.0853  74  LEU   A CD2 
201  N N   . ASP   A 32  ? 0.8856 1.1970 0.5480 0.2450  0.0918  0.0577  75  ASP   A N   
202  C CA  . ASP   A 32  ? 0.8769 1.1855 0.5426 0.2508  0.0679  0.0546  75  ASP   A CA  
203  C C   . ASP   A 32  ? 0.8426 1.1590 0.5226 0.2303  0.0568  0.0554  75  ASP   A C   
204  O O   . ASP   A 32  ? 0.8162 1.1669 0.5379 0.2189  0.0613  0.0543  75  ASP   A O   
205  C CB  . ASP   A 32  ? 0.8913 1.2358 0.5924 0.2703  0.0629  0.0492  75  ASP   A CB  
206  C CG  . ASP   A 32  ? 0.9943 1.3225 0.6753 0.2953  0.0679  0.0464  75  ASP   A CG  
207  O OD1 . ASP   A 32  ? 1.0366 1.3187 0.6747 0.2980  0.0659  0.0479  75  ASP   A OD1 
208  O OD2 . ASP   A 32  ? 1.0168 1.3788 0.7278 0.3125  0.0736  0.0417  75  ASP   A OD2 
209  N N   . VAL   A 33  ? 0.8432 1.1270 0.4899 0.2247  0.0440  0.0573  76  VAL   A N   
210  C CA  . VAL   A 33  ? 0.8274 1.1127 0.4799 0.2078  0.0326  0.0561  76  VAL   A CA  
211  C C   . VAL   A 33  ? 0.8258 1.1001 0.4601 0.2164  0.0101  0.0541  76  VAL   A C   
212  O O   . VAL   A 33  ? 0.8411 1.0958 0.4496 0.2319  0.0065  0.0580  76  VAL   A O   
213  C CB  . VAL   A 33  ? 0.8446 1.1034 0.4723 0.1907  0.0433  0.0608  76  VAL   A CB  
214  C CG1 . VAL   A 33  ? 0.8432 1.1143 0.4874 0.1824  0.0655  0.0648  76  VAL   A CG1 
215  C CG2 . VAL   A 33  ? 0.8700 1.0908 0.4526 0.1967  0.0441  0.0643  76  VAL   A CG2 
216  N N   . ALA   A 34  ? 0.8091 1.0936 0.4549 0.2070  -0.0048 0.0484  77  ALA   A N   
217  C CA  . ALA   A 34  ? 0.8157 1.0910 0.4390 0.2165  -0.0260 0.0458  77  ALA   A CA  
218  C C   . ALA   A 34  ? 0.8215 1.0794 0.4273 0.2014  -0.0295 0.0440  77  ALA   A C   
219  O O   . ALA   A 34  ? 0.8158 1.0828 0.4466 0.1842  -0.0262 0.0395  77  ALA   A O   
220  C CB  . ALA   A 34  ? 0.7908 1.1016 0.4479 0.2268  -0.0468 0.0348  77  ALA   A CB  
221  N N   . LEU   A 35  ? 0.8288 1.0612 0.3927 0.2085  -0.0346 0.0486  78  LEU   A N   
222  C CA  . LEU   A 35  ? 0.8372 1.0535 0.3814 0.1983  -0.0376 0.0462  78  LEU   A CA  
223  C C   . LEU   A 35  ? 0.8452 1.0680 0.3780 0.2100  -0.0607 0.0374  78  LEU   A C   
224  O O   . LEU   A 35  ? 0.8673 1.0856 0.3744 0.2291  -0.0672 0.0426  78  LEU   A O   
225  C CB  . LEU   A 35  ? 0.8469 1.0331 0.3544 0.1977  -0.0236 0.0575  78  LEU   A CB  
226  C CG  . LEU   A 35  ? 0.8550 1.0254 0.3398 0.1907  -0.0246 0.0561  78  LEU   A CG  
227  C CD1 . LEU   A 35  ? 0.8536 1.0226 0.3553 0.1730  -0.0188 0.0513  78  LEU   A CD1 
228  C CD2 . LEU   A 35  ? 0.8700 1.0187 0.3253 0.1937  -0.0132 0.0671  78  LEU   A CD2 
229  N N   . ASP   A 36  ? 0.8316 1.0640 0.3833 0.2004  -0.0741 0.0236  79  ASP   A N   
230  C CA  . ASP   A 36  ? 0.8389 1.0781 0.3791 0.2138  -0.0999 0.0105  79  ASP   A CA  
231  C C   . ASP   A 36  ? 0.8694 1.0833 0.3611 0.2197  -0.1011 0.0116  79  ASP   A C   
232  O O   . ASP   A 36  ? 0.8895 1.0834 0.3629 0.2116  -0.0822 0.0225  79  ASP   A O   
233  C CB  . ASP   A 36  ? 0.8345 1.0984 0.4245 0.2027  -0.1187 -0.0088 79  ASP   A CB  
234  C CG  . ASP   A 36  ? 0.8821 1.1332 0.4871 0.1805  -0.1168 -0.0158 79  ASP   A CG  
235  O OD1 . ASP   A 36  ? 0.9135 1.1372 0.4849 0.1768  -0.1041 -0.0080 79  ASP   A OD1 
236  O OD2 . ASP   A 36  ? 0.8907 1.1593 0.5437 0.1672  -0.1288 -0.0293 79  ASP   A OD2 
237  N N   . GLU   A 37  ? 0.8753 1.0923 0.3457 0.2363  -0.1237 -0.0005 80  GLU   A N   
238  C CA  . GLU   A 37  ? 0.8943 1.0920 0.3174 0.2464  -0.1247 -0.0007 80  GLU   A CA  
239  C C   . GLU   A 37  ? 0.8911 1.0735 0.3203 0.2277  -0.1189 -0.0070 80  GLU   A C   
240  O O   . GLU   A 37  ? 0.9037 1.0694 0.2984 0.2321  -0.1089 -0.0011 80  GLU   A O   
241  C CB  . GLU   A 37  ? 0.9289 1.1352 0.3288 0.2705  -0.1531 -0.0164 80  GLU   A CB  
242  C CG  . GLU   A 37  ? 0.9939 1.1837 0.3333 0.2910  -0.1505 -0.0115 80  GLU   A CG  
243  C CD  . GLU   A 37  ? 1.0462 1.2420 0.3611 0.3140  -0.1815 -0.0336 80  GLU   A CD  
244  O OE1 . GLU   A 37  ? 1.0268 1.2164 0.3453 0.3082  -0.1946 -0.0535 80  GLU   A OE1 
245  O OE2 . GLU   A 37  ? 1.0661 1.2707 0.3563 0.3394  -0.1942 -0.0320 80  GLU   A OE2 
246  N N   . SER   A 38  ? 0.8687 1.0567 0.3430 0.2071  -0.1230 -0.0170 81  SER   A N   
247  C CA  . SER   A 38  ? 0.8772 1.0463 0.3566 0.1907  -0.1186 -0.0218 81  SER   A CA  
248  C C   . SER   A 38  ? 0.8828 1.0397 0.3674 0.1747  -0.0913 -0.0046 81  SER   A C   
249  O O   . SER   A 38  ? 0.8910 1.0319 0.3829 0.1612  -0.0873 -0.0069 81  SER   A O   
250  C CB  . SER   A 38  ? 0.8787 1.0543 0.4029 0.1763  -0.1375 -0.0405 81  SER   A CB  
251  O OG  . SER   A 38  ? 0.9095 1.0968 0.4304 0.1921  -0.1674 -0.0608 81  SER   A OG  
252  N N   . GLY   A 39  ? 0.8768 1.0389 0.3562 0.1779  -0.0746 0.0112  82  GLY   A N   
253  C CA  . GLY   A 39  ? 0.8817 1.0328 0.3622 0.1664  -0.0518 0.0247  82  GLY   A CA  
254  C C   . GLY   A 39  ? 0.8682 1.0261 0.3874 0.1494  -0.0433 0.0261  82  GLY   A C   
255  O O   . GLY   A 39  ? 0.8816 1.0264 0.3982 0.1400  -0.0274 0.0341  82  GLY   A O   
256  N N   . ASP   A 40  ? 0.8424 1.0229 0.3980 0.1467  -0.0536 0.0186  83  ASP   A N   
257  C CA  . ASP   A 40  ? 0.8209 1.0148 0.4207 0.1307  -0.0440 0.0208  83  ASP   A CA  
258  C C   . ASP   A 40  ? 0.8077 1.0251 0.4249 0.1372  -0.0339 0.0278  83  ASP   A C   
259  O O   . ASP   A 40  ? 0.7972 1.0356 0.4256 0.1492  -0.0478 0.0215  83  ASP   A O   
260  C CB  . ASP   A 40  ? 0.8171 1.0234 0.4573 0.1203  -0.0631 0.0053  83  ASP   A CB  
261  C CG  . ASP   A 40  ? 0.8671 1.0457 0.4926 0.1138  -0.0733 -0.0033 83  ASP   A CG  
262  O OD1 . ASP   A 40  ? 0.8862 1.0389 0.4833 0.1111  -0.0593 0.0060  83  ASP   A OD1 
263  O OD2 . ASP   A 40  ? 0.8888 1.0715 0.5311 0.1133  -0.0974 -0.0212 83  ASP   A OD2 
264  N N   . PHE   A 41  ? 0.8092 1.0216 0.4252 0.1323  -0.0109 0.0400  84  PHE   A N   
265  C CA  . PHE   A 41  ? 0.8014 1.0330 0.4314 0.1401  0.0008  0.0457  84  PHE   A CA  
266  C C   . PHE   A 41  ? 0.7966 1.0625 0.4826 0.1317  0.0024  0.0421  84  PHE   A C   
267  O O   . PHE   A 41  ? 0.7841 1.0523 0.4982 0.1142  0.0037  0.0404  84  PHE   A O   
268  C CB  . PHE   A 41  ? 0.7970 1.0110 0.4038 0.1398  0.0233  0.0569  84  PHE   A CB  
269  C CG  . PHE   A 41  ? 0.8113 0.9995 0.3737 0.1496  0.0228  0.0601  84  PHE   A CG  
270  C CD1 . PHE   A 41  ? 0.8126 1.0016 0.3642 0.1644  0.0201  0.0615  84  PHE   A CD1 
271  C CD2 . PHE   A 41  ? 0.8291 0.9922 0.3643 0.1440  0.0262  0.0624  84  PHE   A CD2 
272  C CE1 . PHE   A 41  ? 0.8364 1.0017 0.3550 0.1701  0.0216  0.0656  84  PHE   A CE1 
273  C CE2 . PHE   A 41  ? 0.8418 0.9865 0.3454 0.1512  0.0264  0.0648  84  PHE   A CE2 
274  C CZ  . PHE   A 41  ? 0.8399 0.9858 0.3376 0.1626  0.0249  0.0668  84  PHE   A CZ  
275  N N   . SER   A 42  ? 0.8043 1.0969 0.5099 0.1441  0.0029  0.0413  85  SER   A N   
276  C CA  . SER   A 42  ? 0.8065 1.1394 0.5718 0.1378  0.0063  0.0379  85  SER   A CA  
277  C C   . SER   A 42  ? 0.8350 1.1877 0.6078 0.1529  0.0214  0.0432  85  SER   A C   
278  O O   . SER   A 42  ? 0.8530 1.1916 0.5910 0.1716  0.0176  0.0445  85  SER   A O   
279  C CB  . SER   A 42  ? 0.8017 1.1594 0.6001 0.1396  -0.0227 0.0219  85  SER   A CB  
280  O OG  . SER   A 42  ? 0.8452 1.2056 0.6197 0.1637  -0.0391 0.0176  85  SER   A OG  
281  N N   . LEU   A 43  ? 0.8359 1.2200 0.6545 0.1455  0.0396  0.0469  86  LEU   A N   
282  C CA  . LEU   A 43  ? 0.8548 1.2607 0.6817 0.1626  0.0550  0.0503  86  LEU   A CA  
283  C C   . LEU   A 43  ? 0.8545 1.2960 0.7137 0.1797  0.0359  0.0393  86  LEU   A C   
284  O O   . LEU   A 43  ? 0.8282 1.3013 0.7358 0.1722  0.0192  0.0293  86  LEU   A O   
285  C CB  . LEU   A 43  ? 0.8437 1.2715 0.7024 0.1522  0.0861  0.0603  86  LEU   A CB  
286  C CG  . LEU   A 43  ? 0.9000 1.2908 0.7122 0.1471  0.1086  0.0731  86  LEU   A CG  
287  C CD1 . LEU   A 43  ? 0.8922 1.3056 0.7345 0.1378  0.1407  0.0856  86  LEU   A CD1 
288  C CD2 . LEU   A 43  ? 0.9402 1.3038 0.6971 0.1691  0.1109  0.0731  86  LEU   A CD2 
289  N N   . VAL   A 44  ? 0.8818 1.3162 0.7140 0.2038  0.0368  0.0402  87  VAL   A N   
290  C CA  . VAL   A 44  ? 0.8883 1.3511 0.7421 0.2264  0.0204  0.0318  87  VAL   A CA  
291  C C   . VAL   A 44  ? 0.8997 1.3920 0.7795 0.2389  0.0434  0.0342  87  VAL   A C   
292  O O   . VAL   A 44  ? 0.9249 1.3933 0.7714 0.2424  0.0653  0.0420  87  VAL   A O   
293  C CB  . VAL   A 44  ? 0.9252 1.3484 0.7222 0.2466  0.0042  0.0329  87  VAL   A CB  
294  C CG1 . VAL   A 44  ? 0.9201 1.3649 0.7304 0.2749  -0.0091 0.0274  87  VAL   A CG1 
295  C CG2 . VAL   A 44  ? 0.9457 1.3458 0.7171 0.2380  -0.0168 0.0306  87  VAL   A CG2 
296  N N   . GLU   A 45  ? 0.8780 1.4245 0.8182 0.2466  0.0386  0.0263  88  GLU   A N   
297  C CA  . GLU   A 45  ? 0.8799 1.4603 0.8478 0.2613  0.0619  0.0279  88  GLU   A CA  
298  C C   . GLU   A 45  ? 0.8782 1.4795 0.8565 0.2938  0.0449  0.0186  88  GLU   A C   
299  O O   . GLU   A 45  ? 0.9008 1.4795 0.8426 0.3171  0.0526  0.0207  88  GLU   A O   
300  C CB  . GLU   A 45  ? 0.8820 1.5156 0.9216 0.2407  0.0823  0.0302  88  GLU   A CB  
301  C CG  . GLU   A 45  ? 0.9737 1.5824 0.9997 0.2115  0.1034  0.0427  88  GLU   A CG  
302  C CD  . GLU   A 45  ? 1.0951 1.6928 1.0930 0.2163  0.1407  0.0560  88  GLU   A CD  
303  O OE1 . GLU   A 45  ? 1.1226 1.7243 1.1024 0.2436  0.1493  0.0538  88  GLU   A OE1 
304  O OE2 . GLU   A 45  ? 1.1377 1.7206 1.1290 0.1948  0.1605  0.0681  88  GLU   A OE2 
305  N N   . GLY   B 7   ? 1.0565 1.1874 0.6334 0.2905  0.0578  -0.0888 16  GLY   B N   
306  C CA  . GLY   B 7   ? 1.0681 1.1926 0.6403 0.3145  0.0428  -0.0861 16  GLY   B CA  
307  C C   . GLY   B 7   ? 1.0629 1.2079 0.6474 0.3075  0.0257  -0.0839 16  GLY   B C   
308  O O   . GLY   B 7   ? 1.0471 1.2350 0.6650 0.2950  0.0220  -0.0903 16  GLY   B O   
309  N N   . GLU   B 8   ? 1.0702 1.1835 0.6272 0.3155  0.0156  -0.0749 17  GLU   B N   
310  C CA  . GLU   B 8   ? 1.0559 1.1810 0.6158 0.3128  -0.0019 -0.0737 17  GLU   B CA  
311  C C   . GLU   B 8   ? 1.0302 1.1593 0.5945 0.2815  0.0001  -0.0721 17  GLU   B C   
312  O O   . GLU   B 8   ? 1.0478 1.1462 0.5886 0.2681  0.0094  -0.0637 17  GLU   B O   
313  C CB  . GLU   B 8   ? 1.1141 1.2013 0.6371 0.3316  -0.0097 -0.0629 17  GLU   B CB  
314  C CG  . GLU   B 8   ? 1.1753 1.2720 0.6952 0.3334  -0.0288 -0.0632 17  GLU   B CG  
315  C CD  . GLU   B 8   ? 1.2784 1.3367 0.7569 0.3501  -0.0329 -0.0505 17  GLU   B CD  
316  O OE1 . GLU   B 8   ? 1.3094 1.3308 0.7631 0.3482  -0.0180 -0.0384 17  GLU   B OE1 
317  O OE2 . GLU   B 8   ? 1.3089 1.3743 0.7797 0.3655  -0.0512 -0.0528 17  GLU   B OE2 
318  N N   A THR   B 9   ? 0.9969 1.1635 0.5920 0.2701  -0.0095 -0.0802 18  THR   B N   
319  N N   B THR   B 9   ? 0.9976 1.1643 0.5929 0.2701  -0.0094 -0.0802 18  THR   B N   
320  C CA  A THR   B 9   ? 0.9920 1.1595 0.5905 0.2415  -0.0085 -0.0786 18  THR   B CA  
321  C CA  B THR   B 9   ? 0.9934 1.1616 0.5925 0.2417  -0.0087 -0.0788 18  THR   B CA  
322  C C   A THR   B 9   ? 0.9801 1.1508 0.5781 0.2404  -0.0297 -0.0811 18  THR   B C   
323  C C   B THR   B 9   ? 0.9807 1.1518 0.5791 0.2405  -0.0298 -0.0812 18  THR   B C   
324  O O   A THR   B 9   ? 0.9784 1.1531 0.5842 0.2181  -0.0320 -0.0822 18  THR   B O   
325  O O   B THR   B 9   ? 0.9789 1.1543 0.5854 0.2181  -0.0320 -0.0823 18  THR   B O   
326  C CB  A THR   B 9   ? 0.9895 1.1897 0.6209 0.2207  0.0040  -0.0841 18  THR   B CB  
327  C CB  B THR   B 9   ? 0.9922 1.1949 0.6257 0.2222  0.0028  -0.0848 18  THR   B CB  
328  O OG1 A THR   B 9   ? 0.9941 1.2108 0.6389 0.2334  0.0166  -0.0885 18  THR   B OG1 
329  O OG1 B THR   B 9   ? 0.9793 1.2265 0.6511 0.2334  -0.0044 -0.0949 18  THR   B OG1 
330  C CG2 A THR   B 9   ? 1.0054 1.1855 0.6211 0.1954  0.0168  -0.0773 18  THR   B CG2 
331  C CG2 B THR   B 9   ? 1.0071 1.1960 0.6288 0.2176  0.0248  -0.0816 18  THR   B CG2 
332  N N   . THR   B 10  ? 0.9725 1.1378 0.5576 0.2656  -0.0456 -0.0822 19  THR   B N   
333  C CA  . THR   B 10  ? 0.9534 1.1186 0.5321 0.2693  -0.0678 -0.0865 19  THR   B CA  
334  C C   . THR   B 10  ? 0.9503 1.0803 0.4964 0.2572  -0.0653 -0.0777 19  THR   B C   
335  O O   . THR   B 10  ? 0.9661 1.0666 0.4843 0.2601  -0.0513 -0.0658 19  THR   B O   
336  C CB  . THR   B 10  ? 0.9760 1.1358 0.5366 0.3039  -0.0828 -0.0871 19  THR   B CB  
337  O OG1 . THR   B 10  ? 0.9691 1.1618 0.5593 0.3184  -0.0842 -0.0947 19  THR   B OG1 
338  C CG2 . THR   B 10  ? 0.9800 1.1404 0.5306 0.3118  -0.1086 -0.0941 19  THR   B CG2 
339  N N   . ASP   B 11  ? 0.9329 1.0663 0.4842 0.2430  -0.0786 -0.0837 20  ASP   B N   
340  C CA  . ASP   B 11  ? 0.9497 1.0509 0.4695 0.2352  -0.0786 -0.0770 20  ASP   B CA  
341  C C   . ASP   B 11  ? 0.9556 1.0271 0.4326 0.2611  -0.0811 -0.0678 20  ASP   B C   
342  O O   . ASP   B 11  ? 0.9550 1.0300 0.4247 0.2855  -0.0922 -0.0705 20  ASP   B O   
343  C CB  . ASP   B 11  ? 0.9803 1.0862 0.5090 0.2236  -0.0987 -0.0880 20  ASP   B CB  
344  C CG  . ASP   B 11  ? 1.0300 1.1512 0.5903 0.1918  -0.0927 -0.0917 20  ASP   B CG  
345  O OD1 . ASP   B 11  ? 1.0218 1.1617 0.6049 0.1811  -0.0750 -0.0887 20  ASP   B OD1 
346  O OD2 . ASP   B 11  ? 1.0670 1.1788 0.6267 0.1785  -0.1055 -0.0974 20  ASP   B OD2 
347  N N   . GLY   B 12  ? 0.9579 1.0023 0.4072 0.2566  -0.0703 -0.0565 21  GLY   B N   
348  C CA  . GLY   B 12  ? 0.9678 0.9863 0.3781 0.2786  -0.0684 -0.0453 21  GLY   B CA  
349  C C   . GLY   B 12  ? 0.9632 0.9636 0.3592 0.2708  -0.0471 -0.0300 21  GLY   B C   
350  O O   . GLY   B 12  ? 0.9566 0.9625 0.3696 0.2491  -0.0356 -0.0293 21  GLY   B O   
351  N N   . VAL   B 13  ? 0.9644 0.9442 0.3289 0.2884  -0.0418 -0.0174 22  VAL   B N   
352  C CA  . VAL   B 13  ? 0.9631 0.9294 0.3180 0.2807  -0.0222 -0.0023 22  VAL   B CA  
353  C C   . VAL   B 13  ? 0.9530 0.9137 0.3137 0.2833  -0.0087 0.0050  22  VAL   B C   
354  O O   . VAL   B 13  ? 0.9533 0.9121 0.3097 0.3020  -0.0140 0.0036  22  VAL   B O   
355  C CB  . VAL   B 13  ? 0.9864 0.9368 0.3086 0.2946  -0.0205 0.0087  22  VAL   B CB  
356  C CG1 . VAL   B 13  ? 0.9995 0.9375 0.2945 0.3238  -0.0229 0.0158  22  VAL   B CG1 
357  C CG2 . VAL   B 13  ? 0.9956 0.9412 0.3172 0.2815  -0.0021 0.0224  22  VAL   B CG2 
358  N N   . TYR   B 14  ? 0.9406 0.8985 0.3122 0.2645  0.0064  0.0103  23  TYR   B N   
359  C CA  . TYR   B 14  ? 0.9327 0.8800 0.3090 0.2650  0.0179  0.0149  23  TYR   B CA  
360  C C   . TYR   B 14  ? 0.9376 0.8692 0.3066 0.2547  0.0334  0.0292  23  TYR   B C   
361  O O   . TYR   B 14  ? 0.9390 0.8774 0.3127 0.2384  0.0364  0.0304  23  TYR   B O   
362  C CB  . TYR   B 14  ? 0.9083 0.8697 0.3108 0.2497  0.0196  0.0024  23  TYR   B CB  
363  C CG  . TYR   B 14  ? 0.8905 0.8716 0.3090 0.2596  0.0079  -0.0110 23  TYR   B CG  
364  C CD1 . TYR   B 14  ? 0.8866 0.8879 0.3155 0.2560  -0.0056 -0.0205 23  TYR   B CD1 
365  C CD2 . TYR   B 14  ? 0.8933 0.8744 0.3198 0.2706  0.0106  -0.0150 23  TYR   B CD2 
366  C CE1 . TYR   B 14  ? 0.8816 0.9063 0.3310 0.2634  -0.0174 -0.0328 23  TYR   B CE1 
367  C CE2 . TYR   B 14  ? 0.8889 0.8950 0.3348 0.2808  -0.0002 -0.0272 23  TYR   B CE2 
368  C CZ  . TYR   B 14  ? 0.8882 0.9188 0.3482 0.2758  -0.0143 -0.0362 23  TYR   B CZ  
369  O OH  . TYR   B 14  ? 0.8902 0.9511 0.3758 0.2832  -0.0257 -0.0487 23  TYR   B OH  
370  N N   . ARG   B 15  ? 0.9407 0.8514 0.3006 0.2627  0.0429  0.0394  24  ARG   B N   
371  C CA  . ARG   B 15  ? 0.9441 0.8407 0.3035 0.2490  0.0577  0.0524  24  ARG   B CA  
372  C C   . ARG   B 15  ? 0.9341 0.8291 0.3120 0.2288  0.0618  0.0432  24  ARG   B C   
373  O O   . ARG   B 15  ? 0.9265 0.8203 0.3104 0.2338  0.0584  0.0323  24  ARG   B O   
374  C CB  . ARG   B 15  ? 0.9636 0.8327 0.3049 0.2639  0.0673  0.0683  24  ARG   B CB  
375  C CG  . ARG   B 15  ? 0.9773 0.8417 0.2933 0.2920  0.0623  0.0756  24  ARG   B CG  
376  C CD  . ARG   B 15  ? 1.0197 0.8528 0.3164 0.3044  0.0750  0.0936  24  ARG   B CD  
377  N NE  . ARG   B 15  ? 1.0306 0.8564 0.2961 0.3342  0.0715  0.1029  24  ARG   B NE  
378  C CZ  . ARG   B 15  ? 1.0378 0.8634 0.2846 0.3416  0.0797  0.1182  24  ARG   B CZ  
379  N NH1 . ARG   B 15  ? 0.9950 0.8297 0.2551 0.3210  0.0922  0.1271  24  ARG   B NH1 
380  N NH2 . ARG   B 15  ? 1.0679 0.8849 0.2814 0.3715  0.0755  0.1250  24  ARG   B NH2 
381  N N   . VAL   B 16  ? 0.9410 0.8365 0.3270 0.2081  0.0688  0.0472  25  VAL   B N   
382  C CA  . VAL   B 16  ? 0.9556 0.8470 0.3544 0.1890  0.0717  0.0381  25  VAL   B CA  
383  C C   . VAL   B 16  ? 0.9824 0.8470 0.3792 0.1820  0.0820  0.0489  25  VAL   B C   
384  O O   . VAL   B 16  ? 0.9843 0.8510 0.3837 0.1729  0.0879  0.0616  25  VAL   B O   
385  C CB  . VAL   B 16  ? 0.9588 0.8720 0.3677 0.1703  0.0685  0.0321  25  VAL   B CB  
386  C CG1 . VAL   B 16  ? 0.9640 0.8701 0.3808 0.1516  0.0712  0.0239  25  VAL   B CG1 
387  C CG2 . VAL   B 16  ? 0.9572 0.8907 0.3683 0.1747  0.0594  0.0215  25  VAL   B CG2 
388  N N   . MET   B 17  ? 1.0060 0.8450 0.3987 0.1871  0.0846  0.0447  26  MET   B N   
389  C CA  . MET   B 17  ? 1.0336 0.8383 0.4219 0.1813  0.0939  0.0547  26  MET   B CA  
390  C C   . MET   B 17  ? 1.0626 0.8503 0.4580 0.1626  0.0942  0.0424  26  MET   B C   
391  O O   . MET   B 17  ? 1.0644 0.8631 0.4632 0.1612  0.0884  0.0254  26  MET   B O   
392  C CB  . MET   B 17  ? 1.0446 0.8219 0.4147 0.2065  0.0963  0.0608  26  MET   B CB  
393  C CG  . MET   B 17  ? 1.0425 0.8339 0.4001 0.2296  0.0929  0.0695  26  MET   B CG  
394  S SD  . MET   B 17  ? 1.0792 0.8636 0.4262 0.2295  0.1051  0.0957  26  MET   B SD  
395  C CE  . MET   B 17  ? 1.0055 0.7384 0.3435 0.2258  0.1184  0.1086  26  MET   B CE  
396  N N   . THR   B 18  ? 1.0843 0.8429 0.4808 0.1487  0.1012  0.0509  27  THR   B N   
397  C CA  . THR   B 18  ? 1.1063 0.8405 0.5056 0.1316  0.0998  0.0383  27  THR   B CA  
398  C C   . THR   B 18  ? 1.1541 0.8380 0.5442 0.1302  0.1077  0.0481  27  THR   B C   
399  O O   . THR   B 18  ? 1.1597 0.8353 0.5508 0.1281  0.1165  0.0685  27  THR   B O   
400  C CB  . THR   B 18  ? 1.0946 0.8519 0.5112 0.1048  0.0951  0.0327  27  THR   B CB  
401  O OG1 . THR   B 18  ? 1.1148 0.8429 0.5311 0.0885  0.0923  0.0204  27  THR   B OG1 
402  C CG2 . THR   B 18  ? 1.0814 0.8558 0.5127 0.0924  0.1003  0.0514  27  THR   B CG2 
403  N N   . ARG   B 19  ? 1.1890 0.8372 0.5684 0.1322  0.1057  0.0343  28  ARG   B N   
404  C CA  . ARG   B 19  ? 1.2372 0.8293 0.6054 0.1292  0.1123  0.0420  28  ARG   B CA  
405  C C   . ARG   B 19  ? 1.2594 0.8286 0.6376 0.0976  0.1090  0.0329  28  ARG   B C   
406  O O   . ARG   B 19  ? 1.2835 0.7994 0.6513 0.0924  0.1119  0.0335  28  ARG   B O   
407  C CB  . ARG   B 19  ? 1.2807 0.8384 0.6250 0.1583  0.1126  0.0354  28  ARG   B CB  
408  C CG  . ARG   B 19  ? 1.3318 0.8996 0.6648 0.1880  0.1160  0.0499  28  ARG   B CG  
409  C CD  . ARG   B 19  ? 1.4043 0.9285 0.7126 0.2164  0.1177  0.0493  28  ARG   B CD  
410  N NE  . ARG   B 19  ? 1.4453 0.9883 0.7435 0.2480  0.1163  0.0578  28  ARG   B NE  
411  C CZ  . ARG   B 19  ? 1.4691 1.0360 0.7665 0.2728  0.1083  0.0437  28  ARG   B CZ  
412  N NH1 . ARG   B 19  ? 1.4687 1.0434 0.7734 0.2710  0.1039  0.0219  28  ARG   B NH1 
413  N NH2 . ARG   B 19  ? 1.4548 1.0393 0.7444 0.2999  0.1046  0.0511  28  ARG   B NH2 
414  N N   . ARG   B 20  ? 1.2488 0.8564 0.6460 0.0771  0.1017  0.0243  29  ARG   B N   
415  C CA  . ARG   B 20  ? 1.2635 0.8594 0.6722 0.0473  0.0944  0.0130  29  ARG   B CA  
416  C C   . ARG   B 20  ? 1.2605 0.8464 0.6898 0.0220  0.1008  0.0320  29  ARG   B C   
417  O O   . ARG   B 20  ? 1.2716 0.8243 0.7068 -0.0013 0.0968  0.0258  29  ARG   B O   
418  C CB  . ARG   B 20  ? 1.2712 0.9157 0.6907 0.0383  0.0838  -0.0012 29  ARG   B CB  
419  C CG  . ARG   B 20  ? 1.3360 0.9689 0.7604 0.0132  0.0721  -0.0192 29  ARG   B CG  
420  C CD  . ARG   B 20  ? 1.3780 1.0614 0.8129 0.0049  0.0624  -0.0277 29  ARG   B CD  
421  N NE  . ARG   B 20  ? 1.4079 1.1342 0.8676 -0.0027 0.0658  -0.0085 29  ARG   B NE  
422  C CZ  . ARG   B 20  ? 1.4262 1.1786 0.9095 -0.0258 0.0585  -0.0074 29  ARG   B CZ  
423  N NH1 . ARG   B 20  ? 1.4288 1.1685 0.9139 -0.0451 0.0452  -0.0253 29  ARG   B NH1 
424  N NH2 . ARG   B 20  ? 1.3995 1.1922 0.9041 -0.0279 0.0634  0.0106  29  ARG   B NH2 
425  N N   . LEU   B 21  ? 1.2422 0.8566 0.6826 0.0266  0.1109  0.0550  30  LEU   B N   
426  C CA  . LEU   B 21  ? 1.2379 0.8510 0.7000 0.0054  0.1211  0.0770  30  LEU   B CA  
427  C C   . LEU   B 21  ? 1.2599 0.8178 0.7033 0.0157  0.1355  0.0955  30  LEU   B C   
428  O O   . LEU   B 21  ? 1.2841 0.7978 0.7005 0.0329  0.1333  0.0857  30  LEU   B O   
429  C CB  . LEU   B 21  ? 1.2194 0.8926 0.6986 0.0095  0.1260  0.0921  30  LEU   B CB  
430  C CG  . LEU   B 21  ? 1.2172 0.9375 0.7292 -0.0158 0.1182  0.0879  30  LEU   B CG  
431  C CD1 . LEU   B 21  ? 1.2255 0.9519 0.7352 -0.0233 0.0998  0.0596  30  LEU   B CD1 
432  C CD2 . LEU   B 21  ? 1.2045 0.9788 0.7247 -0.0031 0.1229  0.1009  30  LEU   B CD2 
433  N N   . LEU   B 22  ? 1.2483 0.8075 0.7046 0.0065  0.1509  0.1228  31  LEU   B N   
434  C CA  . LEU   B 22  ? 1.2729 0.7784 0.7080 0.0171  0.1662  0.1434  31  LEU   B CA  
435  C C   . LEU   B 22  ? 1.2799 0.7935 0.6850 0.0580  0.1708  0.1518  31  LEU   B C   
436  O O   . LEU   B 22  ? 1.2705 0.8347 0.6821 0.0680  0.1725  0.1588  31  LEU   B O   
437  C CB  . LEU   B 22  ? 1.2606 0.7691 0.7207 -0.0077 0.1831  0.1711  31  LEU   B CB  
438  C CG  . LEU   B 22  ? 1.2929 0.7479 0.7300 0.0025  0.2023  0.1978  31  LEU   B CG  
439  C CD1 . LEU   B 22  ? 1.3106 0.7055 0.7556 -0.0280 0.2051  0.1995  31  LEU   B CD1 
440  C CD2 . LEU   B 22  ? 1.2861 0.7761 0.7318 0.0070  0.2219  0.2285  31  LEU   B CD2 
441  N N   . GLY   B 23  ? 1.2940 0.7584 0.6664 0.0821  0.1711  0.1495  32  GLY   B N   
442  C CA  . GLY   B 23  ? 1.2927 0.7629 0.6366 0.1221  0.1719  0.1544  32  GLY   B CA  
443  C C   . GLY   B 23  ? 1.2595 0.7823 0.6080 0.1362  0.1571  0.1332  32  GLY   B C   
444  O O   . GLY   B 23  ? 1.2514 0.7838 0.6106 0.1250  0.1452  0.1096  32  GLY   B O   
445  N N   . SER   B 24  ? 1.2403 0.7962 0.5797 0.1601  0.1581  0.1419  33  SER   B N   
446  C CA  . SER   B 24  ? 1.2159 0.8213 0.5605 0.1722  0.1450  0.1249  33  SER   B CA  
447  C C   . SER   B 24  ? 1.1775 0.8306 0.5394 0.1618  0.1480  0.1347  33  SER   B C   
448  O O   . SER   B 24  ? 1.1814 0.8384 0.5321 0.1749  0.1576  0.1550  33  SER   B O   
449  C CB  . SER   B 24  ? 1.2520 0.8552 0.5710 0.2101  0.1405  0.1243  33  SER   B CB  
450  O OG  . SER   B 24  ? 1.3074 0.8814 0.6150 0.2232  0.1342  0.1091  33  SER   B OG  
451  N N   . THR   B 25  ? 1.1416 0.8293 0.5279 0.1404  0.1401  0.1210  34  THR   B N   
452  C CA  . THR   B 25  ? 1.1081 0.8407 0.5112 0.1317  0.1422  0.1294  34  THR   B CA  
453  C C   . THR   B 25  ? 1.0747 0.8471 0.4766 0.1443  0.1298  0.1151  34  THR   B C   
454  O O   . THR   B 25  ? 1.0720 0.8512 0.4788 0.1391  0.1187  0.0947  34  THR   B O   
455  C CB  . THR   B 25  ? 1.1096 0.8524 0.5429 0.0969  0.1433  0.1286  34  THR   B CB  
456  O OG1 . THR   B 25  ? 1.1291 0.8377 0.5668 0.0830  0.1568  0.1461  34  THR   B OG1 
457  C CG2 . THR   B 25  ? 1.0874 0.8819 0.5401 0.0898  0.1432  0.1339  34  THR   B CG2 
458  N N   . GLN   B 26  ? 1.0483 0.8453 0.4425 0.1602  0.1323  0.1262  35  GLN   B N   
459  C CA  . GLN   B 26  ? 1.0215 0.8519 0.4141 0.1704  0.1203  0.1138  35  GLN   B CA  
460  C C   . GLN   B 26  ? 1.0018 0.8654 0.4165 0.1497  0.1171  0.1095  35  GLN   B C   
461  O O   . GLN   B 26  ? 1.0036 0.8842 0.4278 0.1440  0.1255  0.1243  35  GLN   B O   
462  C CB  . GLN   B 26  ? 1.0170 0.8552 0.3879 0.1977  0.1215  0.1243  35  GLN   B CB  
463  C CG  . GLN   B 26  ? 1.0084 0.8721 0.3753 0.2086  0.1067  0.1089  35  GLN   B CG  
464  C CD  . GLN   B 26  ? 1.0390 0.9076 0.3821 0.2354  0.1048  0.1163  35  GLN   B CD  
465  O OE1 . GLN   B 26  ? 1.0639 0.9133 0.3862 0.2568  0.1042  0.1201  35  GLN   B OE1 
466  N NE2 . GLN   B 26  ? 1.0175 0.9105 0.3601 0.2372  0.1024  0.1172  35  GLN   B NE2 
467  N N   . VAL   B 27  ? 0.9727 0.8472 0.3948 0.1405  0.1055  0.0902  36  VAL   B N   
468  C CA  . VAL   B 27  ? 0.9433 0.8473 0.3822 0.1236  0.1004  0.0851  36  VAL   B CA  
469  C C   . VAL   B 27  ? 0.9086 0.8392 0.3403 0.1357  0.0927  0.0809  36  VAL   B C   
470  O O   . VAL   B 27  ? 0.9000 0.8546 0.3417 0.1263  0.0890  0.0796  36  VAL   B O   
471  C CB  . VAL   B 27  ? 0.9542 0.8515 0.4025 0.1043  0.0932  0.0680  36  VAL   B CB  
472  C CG1 . VAL   B 27  ? 0.9706 0.8444 0.4301 0.0862  0.0992  0.0726  36  VAL   B CG1 
473  C CG2 . VAL   B 27  ? 0.9681 0.8519 0.4031 0.1151  0.0872  0.0521  36  VAL   B CG2 
474  N N   . GLY   B 28  ? 0.8833 0.8082 0.2978 0.1564  0.0891  0.0783  37  GLY   B N   
475  C CA  . GLY   B 28  ? 0.8615 0.8045 0.2677 0.1671  0.0804  0.0728  37  GLY   B CA  
476  C C   . GLY   B 28  ? 0.8576 0.7920 0.2487 0.1868  0.0737  0.0667  37  GLY   B C   
477  O O   . GLY   B 28  ? 0.8638 0.7799 0.2477 0.1974  0.0769  0.0696  37  GLY   B O   
478  N N   . VAL   B 29  ? 0.8466 0.7939 0.2328 0.1922  0.0637  0.0583  38  VAL   B N   
479  C CA  . VAL   B 29  ? 0.8497 0.7957 0.2253 0.2087  0.0534  0.0502  38  VAL   B CA  
480  C C   . VAL   B 29  ? 0.8280 0.7863 0.2130 0.1975  0.0439  0.0353  38  VAL   B C   
481  O O   . VAL   B 29  ? 0.8181 0.7843 0.2090 0.1827  0.0450  0.0343  38  VAL   B O   
482  C CB  . VAL   B 29  ? 0.8715 0.8176 0.2263 0.2287  0.0515  0.0592  38  VAL   B CB  
483  C CG1 . VAL   B 29  ? 0.8866 0.8324 0.2303 0.2441  0.0367  0.0482  38  VAL   B CG1 
484  C CG2 . VAL   B 29  ? 0.8810 0.8148 0.2240 0.2411  0.0636  0.0763  38  VAL   B CG2 
485  N N   . GLY   B 30  ? 0.8178 0.7785 0.2043 0.2049  0.0347  0.0247  39  GLY   B N   
486  C CA  . GLY   B 30  ? 0.8172 0.7894 0.2139 0.1937  0.0274  0.0126  39  GLY   B CA  
487  C C   . GLY   B 30  ? 0.8243 0.8015 0.2207 0.2045  0.0141  0.0038  39  GLY   B C   
488  O O   . GLY   B 30  ? 0.8143 0.7866 0.2013 0.2233  0.0092  0.0054  39  GLY   B O   
489  N N   . VAL   B 31  ? 0.8328 0.8192 0.2392 0.1925  0.0077  -0.0053 40  VAL   B N   
490  C CA  . VAL   B 31  ? 0.8485 0.8415 0.2600 0.1977  -0.0069 -0.0154 40  VAL   B CA  
491  C C   . VAL   B 31  ? 0.8455 0.8575 0.2850 0.1863  -0.0070 -0.0259 40  VAL   B C   
492  O O   . VAL   B 31  ? 0.8440 0.8613 0.2933 0.1683  0.0012  -0.0268 40  VAL   B O   
493  C CB  . VAL   B 31  ? 0.8669 0.8513 0.2655 0.1935  -0.0157 -0.0163 40  VAL   B CB  
494  C CG1 . VAL   B 31  ? 0.8662 0.8560 0.2746 0.1922  -0.0320 -0.0289 40  VAL   B CG1 
495  C CG2 . VAL   B 31  ? 0.8879 0.8575 0.2584 0.2107  -0.0162 -0.0070 40  VAL   B CG2 
496  N N   . MET   B 32  ? 0.8416 0.8661 0.2936 0.1979  -0.0160 -0.0337 41  MET   B N   
497  C CA  . MET   B 32  ? 0.8338 0.8832 0.3170 0.1884  -0.0157 -0.0436 41  MET   B CA  
498  C C   . MET   B 32  ? 0.8501 0.9101 0.3461 0.1811  -0.0314 -0.0527 41  MET   B C   
499  O O   . MET   B 32  ? 0.8616 0.9184 0.3492 0.1958  -0.0475 -0.0569 41  MET   B O   
500  C CB  . MET   B 32  ? 0.8206 0.8811 0.3138 0.2068  -0.0164 -0.0471 41  MET   B CB  
501  C CG  . MET   B 32  ? 0.8096 0.8997 0.3363 0.1999  -0.0120 -0.0562 41  MET   B CG  
502  S SD  . MET   B 32  ? 0.8494 0.9365 0.3778 0.1838  0.0109  -0.0528 41  MET   B SD  
503  C CE  . MET   B 32  ? 0.8621 0.9334 0.3777 0.2058  0.0174  -0.0499 41  MET   B CE  
504  N N   . GLN   B 33  ? 0.8519 0.9209 0.3649 0.1584  -0.0271 -0.0553 42  GLN   B N   
505  C CA  . GLN   B 33  ? 0.8507 0.9273 0.3794 0.1469  -0.0415 -0.0638 42  GLN   B CA  
506  C C   . GLN   B 33  ? 0.8344 0.9353 0.3963 0.1246  -0.0313 -0.0666 42  GLN   B C   
507  O O   . GLN   B 33  ? 0.8473 0.9434 0.4036 0.1135  -0.0139 -0.0595 42  GLN   B O   
508  C CB  . GLN   B 33  ? 0.8875 0.9333 0.3881 0.1421  -0.0487 -0.0603 42  GLN   B CB  
509  C CG  . GLN   B 33  ? 0.9253 0.9715 0.4388 0.1314  -0.0669 -0.0708 42  GLN   B CG  
510  C CD  . GLN   B 33  ? 0.9986 1.0089 0.4805 0.1299  -0.0754 -0.0688 42  GLN   B CD  
511  O OE1 . GLN   B 33  ? 1.0325 1.0302 0.5159 0.1096  -0.0725 -0.0670 42  GLN   B OE1 
512  N NE2 . GLN   B 33  ? 1.0061 0.9975 0.4562 0.1530  -0.0849 -0.0682 42  GLN   B NE2 
513  N N   . GLU   B 34  ? 0.8081 0.9377 0.4052 0.1185  -0.0413 -0.0768 43  GLU   B N   
514  C CA  . GLU   B 34  ? 0.7869 0.9460 0.4213 0.0964  -0.0296 -0.0785 43  GLU   B CA  
515  C C   . GLU   B 34  ? 0.7668 0.9418 0.4075 0.0985  -0.0063 -0.0738 43  GLU   B C   
516  O O   . GLU   B 34  ? 0.7548 0.9409 0.4085 0.0803  0.0102  -0.0700 43  GLU   B O   
517  C CB  . GLU   B 34  ? 0.8335 0.9733 0.4630 0.0705  -0.0272 -0.0739 43  GLU   B CB  
518  C CG  . GLU   B 34  ? 0.9091 1.0269 0.5288 0.0686  -0.0509 -0.0802 43  GLU   B CG  
519  C CD  . GLU   B 34  ? 1.0185 1.1026 0.6198 0.0485  -0.0493 -0.0742 43  GLU   B CD  
520  O OE1 . GLU   B 34  ? 1.0200 1.1129 0.6406 0.0249  -0.0353 -0.0693 43  GLU   B OE1 
521  O OE2 . GLU   B 34  ? 1.0773 1.1251 0.6430 0.0578  -0.0613 -0.0737 43  GLU   B OE2 
522  N N   . GLY   B 35  ? 0.7564 0.9301 0.3857 0.1216  -0.0050 -0.0740 44  GLY   B N   
523  C CA  . GLY   B 35  ? 0.7385 0.9210 0.3690 0.1273  0.0142  -0.0719 44  GLY   B CA  
524  C C   . GLY   B 35  ? 0.7483 0.8996 0.3447 0.1221  0.0280  -0.0628 44  GLY   B C   
525  O O   . GLY   B 35  ? 0.7418 0.8972 0.3367 0.1223  0.0442  -0.0621 44  GLY   B O   
526  N N   . VAL   B 36  ? 0.7570 0.8780 0.3255 0.1187  0.0210  -0.0565 45  VAL   B N   
527  C CA  . VAL   B 36  ? 0.7718 0.8672 0.3108 0.1137  0.0313  -0.0482 45  VAL   B CA  
528  C C   . VAL   B 36  ? 0.7852 0.8564 0.2983 0.1290  0.0245  -0.0433 45  VAL   B C   
529  O O   . VAL   B 36  ? 0.7938 0.8565 0.2995 0.1363  0.0109  -0.0429 45  VAL   B O   
530  C CB  . VAL   B 36  ? 0.7821 0.8667 0.3128 0.0936  0.0335  -0.0430 45  VAL   B CB  
531  C CG1 . VAL   B 36  ? 0.7998 0.8591 0.2985 0.0916  0.0397  -0.0347 45  VAL   B CG1 
532  C CG2 . VAL   B 36  ? 0.7667 0.8745 0.3215 0.0770  0.0456  -0.0447 45  VAL   B CG2 
533  N N   . PHE   B 37  ? 0.7890 0.8486 0.2881 0.1338  0.0341  -0.0397 46  PHE   B N   
534  C CA  . PHE   B 37  ? 0.8007 0.8388 0.2781 0.1448  0.0309  -0.0327 46  PHE   B CA  
535  C C   . PHE   B 37  ? 0.8027 0.8264 0.2615 0.1336  0.0328  -0.0254 46  PHE   B C   
536  O O   . PHE   B 37  ? 0.8068 0.8309 0.2630 0.1211  0.0412  -0.0253 46  PHE   B O   
537  C CB  . PHE   B 37  ? 0.8100 0.8407 0.2842 0.1535  0.0392  -0.0326 46  PHE   B CB  
538  C CG  . PHE   B 37  ? 0.8451 0.8561 0.3025 0.1657  0.0366  -0.0243 46  PHE   B CG  
539  C CD1 . PHE   B 37  ? 0.8610 0.8708 0.3156 0.1828  0.0272  -0.0227 46  PHE   B CD1 
540  C CD2 . PHE   B 37  ? 0.8707 0.8656 0.3154 0.1598  0.0435  -0.0177 46  PHE   B CD2 
541  C CE1 . PHE   B 37  ? 0.8850 0.8762 0.3220 0.1947  0.0279  -0.0128 46  PHE   B CE1 
542  C CE2 . PHE   B 37  ? 0.8902 0.8693 0.3231 0.1690  0.0437  -0.0082 46  PHE   B CE2 
543  C CZ  . PHE   B 37  ? 0.8924 0.8690 0.3203 0.1868  0.0373  -0.0048 46  PHE   B CZ  
544  N N   . HIS   B 38  ? 0.8006 0.8126 0.2449 0.1402  0.0247  -0.0195 47  HIS   B N   
545  C CA  . HIS   B 38  ? 0.8053 0.8062 0.2325 0.1338  0.0249  -0.0124 47  HIS   B CA  
546  C C   . HIS   B 38  ? 0.8121 0.8042 0.2271 0.1434  0.0270  -0.0039 47  HIS   B C   
547  O O   . HIS   B 38  ? 0.8045 0.7926 0.2143 0.1580  0.0224  -0.0011 47  HIS   B O   
548  C CB  . HIS   B 38  ? 0.8030 0.7973 0.2226 0.1358  0.0134  -0.0129 47  HIS   B CB  
549  C CG  . HIS   B 38  ? 0.8044 0.8068 0.2400 0.1250  0.0093  -0.0207 47  HIS   B CG  
550  N ND1 . HIS   B 38  ? 0.8108 0.8272 0.2656 0.1303  0.0027  -0.0289 47  HIS   B ND1 
551  C CD2 . HIS   B 38  ? 0.8197 0.8181 0.2551 0.1094  0.0107  -0.0206 47  HIS   B CD2 
552  C CE1 . HIS   B 38  ? 0.8029 0.8271 0.2734 0.1154  0.0008  -0.0339 47  HIS   B CE1 
553  N NE2 . HIS   B 38  ? 0.8160 0.8276 0.2744 0.1020  0.0064  -0.0283 47  HIS   B NE2 
554  N N   . THR   B 39  ? 0.8151 0.8052 0.2254 0.1353  0.0337  0.0007  48  THR   B N   
555  C CA  . THR   B 39  ? 0.8145 0.8004 0.2188 0.1413  0.0364  0.0100  48  THR   B CA  
556  C C   . THR   B 39  ? 0.8095 0.7984 0.2073 0.1325  0.0371  0.0150  48  THR   B C   
557  O O   . THR   B 39  ? 0.8009 0.7904 0.1936 0.1246  0.0349  0.0119  48  THR   B O   
558  C CB  . THR   B 39  ? 0.8257 0.8070 0.2377 0.1429  0.0430  0.0097  48  THR   B CB  
559  O OG1 . THR   B 39  ? 0.8348 0.8110 0.2427 0.1503  0.0462  0.0208  48  THR   B OG1 
560  C CG2 . THR   B 39  ? 0.8242 0.8051 0.2412 0.1288  0.0484  0.0038  48  THR   B CG2 
561  N N   . MET   B 40  ? 0.8092 0.8010 0.2073 0.1349  0.0401  0.0237  49  MET   B N   
562  C CA  . MET   B 40  ? 0.8134 0.8137 0.2097 0.1283  0.0394  0.0282  49  MET   B CA  
563  C C   . MET   B 40  ? 0.8122 0.8140 0.2168 0.1134  0.0422  0.0229  49  MET   B C   
564  O O   . MET   B 40  ? 0.8230 0.8181 0.2357 0.1110  0.0467  0.0207  49  MET   B O   
565  C CB  . MET   B 40  ? 0.8252 0.8339 0.2228 0.1378  0.0419  0.0402  49  MET   B CB  
566  C CG  . MET   B 40  ? 0.8747 0.8784 0.2589 0.1562  0.0393  0.0443  49  MET   B CG  
567  S SD  . MET   B 40  ? 0.9168 0.9331 0.2919 0.1686  0.0385  0.0549  49  MET   B SD  
568  C CE  . MET   B 40  ? 0.8194 0.8287 0.1814 0.1633  0.0289  0.0474  49  MET   B CE  
569  N N   . TRP   B 41  ? 0.7935 0.8008 0.1927 0.1049  0.0387  0.0203  50  TRP   B N   
570  C CA  A TRP   B 41  ? 0.7964 0.8037 0.1982 0.0920  0.0389  0.0131  50  TRP   B CA  
571  C CA  B TRP   B 41  ? 0.7846 0.7921 0.1863 0.0920  0.0388  0.0131  50  TRP   B CA  
572  C C   . TRP   B 41  ? 0.7840 0.7947 0.2009 0.0858  0.0403  0.0158  50  TRP   B C   
573  O O   . TRP   B 41  ? 0.7935 0.7943 0.2134 0.0770  0.0415  0.0077  50  TRP   B O   
574  C CB  A TRP   B 41  ? 0.8044 0.8174 0.1931 0.0870  0.0331  0.0110  50  TRP   B CB  
575  C CB  B TRP   B 41  ? 0.7758 0.7894 0.1646 0.0876  0.0329  0.0117  50  TRP   B CB  
576  C CG  A TRP   B 41  ? 0.8230 0.8320 0.2065 0.0761  0.0325  0.0006  50  TRP   B CG  
577  C CG  B TRP   B 41  ? 0.7700 0.7821 0.1552 0.0763  0.0311  0.0024  50  TRP   B CG  
578  C CD1 A TRP   B 41  ? 0.8418 0.8411 0.2133 0.0736  0.0367  -0.0076 50  TRP   B CD1 
579  C CD1 B TRP   B 41  ? 0.7718 0.7927 0.1650 0.0683  0.0255  0.0007  50  TRP   B CD1 
580  C CD2 A TRP   B 41  ? 0.8261 0.8406 0.2158 0.0669  0.0272  -0.0034 50  TRP   B CD2 
581  C CD2 B TRP   B 41  ? 0.7681 0.7697 0.1404 0.0722  0.0346  -0.0074 50  TRP   B CD2 
582  N NE1 A TRP   B 41  ? 0.8537 0.8495 0.2188 0.0659  0.0347  -0.0170 50  TRP   B NE1 
583  N NE1 B TRP   B 41  ? 0.7758 0.7883 0.1585 0.0602  0.0234  -0.0112 50  TRP   B NE1 
584  C CE2 A TRP   B 41  ? 0.8459 0.8496 0.2220 0.0608  0.0274  -0.0156 50  TRP   B CE2 
585  C CE2 B TRP   B 41  ? 0.7796 0.7803 0.1478 0.0637  0.0302  -0.0158 50  TRP   B CE2 
586  C CE3 A TRP   B 41  ? 0.8263 0.8553 0.2332 0.0626  0.0224  0.0018  50  TRP   B CE3 
587  C CE3 B TRP   B 41  ? 0.7741 0.7688 0.1394 0.0747  0.0413  -0.0102 50  TRP   B CE3 
588  C CZ2 A TRP   B 41  ? 0.8587 0.8614 0.2344 0.0511  0.0204  -0.0245 50  TRP   B CZ2 
589  C CZ2 B TRP   B 41  ? 0.7926 0.7831 0.1444 0.0606  0.0331  -0.0268 50  TRP   B CZ2 
590  C CZ3 A TRP   B 41  ? 0.8340 0.8653 0.2464 0.0503  0.0156  -0.0062 50  TRP   B CZ3 
591  C CZ3 B TRP   B 41  ? 0.7932 0.7822 0.1471 0.0704  0.0462  -0.0193 50  TRP   B CZ3 
592  C CH2 A TRP   B 41  ? 0.8495 0.8660 0.2446 0.0448  0.0133  -0.0201 50  TRP   B CH2 
593  C CH2 B TRP   B 41  ? 0.7965 0.7823 0.1408 0.0649  0.0425  -0.0275 50  TRP   B CH2 
594  N N   . HIS   B 42  ? 0.7595 0.7834 0.1860 0.0897  0.0405  0.0270  51  HIS   B N   
595  C CA  . HIS   B 42  ? 0.7585 0.7876 0.2040 0.0804  0.0432  0.0315  51  HIS   B CA  
596  C C   . HIS   B 42  ? 0.7808 0.7909 0.2315 0.0820  0.0517  0.0341  51  HIS   B C   
597  O O   . HIS   B 42  ? 0.7880 0.7947 0.2532 0.0719  0.0551  0.0377  51  HIS   B O   
598  C CB  . HIS   B 42  ? 0.7518 0.8063 0.2095 0.0841  0.0433  0.0442  51  HIS   B CB  
599  C CG  . HIS   B 42  ? 0.7848 0.8401 0.2380 0.1016  0.0503  0.0559  51  HIS   B CG  
600  N ND1 . HIS   B 42  ? 0.8150 0.8710 0.2505 0.1170  0.0469  0.0569  51  HIS   B ND1 
601  C CD2 . HIS   B 42  ? 0.7895 0.8430 0.2510 0.1062  0.0602  0.0671  51  HIS   B CD2 
602  C CE1 . HIS   B 42  ? 0.8137 0.8691 0.2462 0.1315  0.0536  0.0668  51  HIS   B CE1 
603  N NE2 . HIS   B 42  ? 0.8068 0.8615 0.2537 0.1263  0.0625  0.0740  51  HIS   B NE2 
604  N N   . VAL   B 43  ? 0.7883 0.7858 0.2274 0.0949  0.0544  0.0329  52  VAL   B N   
605  C CA  . VAL   B 43  ? 0.7922 0.7708 0.2317 0.1009  0.0610  0.0349  52  VAL   B CA  
606  C C   . VAL   B 43  ? 0.8002 0.7605 0.2387 0.0922  0.0607  0.0218  52  VAL   B C   
607  O O   . VAL   B 43  ? 0.8090 0.7519 0.2526 0.0873  0.0650  0.0231  52  VAL   B O   
608  C CB  . VAL   B 43  ? 0.8084 0.7843 0.2361 0.1194  0.0605  0.0362  52  VAL   B CB  
609  C CG1 . VAL   B 43  ? 0.8232 0.7798 0.2483 0.1291  0.0652  0.0369  52  VAL   B CG1 
610  C CG2 . VAL   B 43  ? 0.8163 0.8054 0.2395 0.1307  0.0605  0.0477  52  VAL   B CG2 
611  N N   . THR   B 44  ? 0.7930 0.7554 0.2232 0.0906  0.0566  0.0096  53  THR   B N   
612  C CA  . THR   B 44  ? 0.7970 0.7433 0.2228 0.0868  0.0579  -0.0035 53  THR   B CA  
613  C C   . THR   B 44  ? 0.8094 0.7558 0.2311 0.0724  0.0530  -0.0135 53  THR   B C   
614  O O   . THR   B 44  ? 0.8184 0.7471 0.2343 0.0692  0.0540  -0.0246 53  THR   B O   
615  C CB  . THR   B 44  ? 0.7991 0.7480 0.2190 0.0975  0.0595  -0.0103 53  THR   B CB  
616  O OG1 . THR   B 44  ? 0.7948 0.7590 0.2088 0.0933  0.0563  -0.0130 53  THR   B OG1 
617  C CG2 . THR   B 44  ? 0.8112 0.7616 0.2340 0.1131  0.0606  -0.0028 53  THR   B CG2 
618  N N   . LYS   B 45  ? 0.8047 0.7698 0.2264 0.0661  0.0470  -0.0103 54  LYS   B N   
619  C CA  . LYS   B 45  ? 0.8199 0.7890 0.2339 0.0552  0.0397  -0.0195 54  LYS   B CA  
620  C C   . LYS   B 45  ? 0.8343 0.7962 0.2289 0.0583  0.0418  -0.0316 54  LYS   B C   
621  O O   . LYS   B 45  ? 0.8447 0.8011 0.2272 0.0515  0.0372  -0.0425 54  LYS   B O   
622  C CB  . LYS   B 45  ? 0.8509 0.8099 0.2742 0.0412  0.0350  -0.0246 54  LYS   B CB  
623  C CG  . LYS   B 45  ? 0.8973 0.8652 0.3438 0.0360  0.0363  -0.0108 54  LYS   B CG  
624  C CD  . LYS   B 45  ? 0.9486 0.9460 0.4062 0.0290  0.0278  -0.0058 54  LYS   B CD  
625  C CE  . LYS   B 45  ? 0.9959 1.0049 0.4810 0.0209  0.0308  0.0070  54  LYS   B CE  
626  N NZ  . LYS   B 45  ? 1.0235 1.0330 0.5114 0.0350  0.0429  0.0227  54  LYS   B NZ  
627  N N   . GLY   B 46  ? 0.8342 0.7977 0.2266 0.0684  0.0486  -0.0298 55  GLY   B N   
628  C CA  . GLY   B 46  ? 0.8578 0.8196 0.2374 0.0717  0.0541  -0.0386 55  GLY   B CA  
629  C C   . GLY   B 46  ? 0.8790 0.8257 0.2581 0.0768  0.0605  -0.0489 55  GLY   B C   
630  O O   . GLY   B 46  ? 0.8847 0.8336 0.2554 0.0811  0.0673  -0.0561 55  GLY   B O   
631  N N   . ALA   B 47  ? 0.8948 0.8257 0.2825 0.0776  0.0599  -0.0488 56  ALA   B N   
632  C CA  . ALA   B 47  ? 0.9156 0.8269 0.2999 0.0854  0.0655  -0.0585 56  ALA   B CA  
633  C C   . ALA   B 47  ? 0.9359 0.8557 0.3286 0.1005  0.0726  -0.0570 56  ALA   B C   
634  O O   . ALA   B 47  ? 0.9298 0.8636 0.3338 0.1046  0.0715  -0.0469 56  ALA   B O   
635  C CB  . ALA   B 47  ? 0.9190 0.8056 0.3081 0.0813  0.0627  -0.0572 56  ALA   B CB  
636  N N   . ALA   B 48  ? 0.9557 0.8675 0.3427 0.1102  0.0791  -0.0680 57  ALA   B N   
637  C CA  . ALA   B 48  ? 0.9680 0.8919 0.3664 0.1258  0.0852  -0.0687 57  ALA   B CA  
638  C C   . ALA   B 48  ? 0.9902 0.9002 0.3969 0.1362  0.0826  -0.0616 57  ALA   B C   
639  O O   . ALA   B 48  ? 1.0081 0.8893 0.4075 0.1344  0.0811  -0.0614 57  ALA   B O   
640  C CB  . ALA   B 48  ? 0.9736 0.8927 0.3628 0.1356  0.0935  -0.0827 57  ALA   B CB  
641  N N   . LEU   B 49  ? 0.9891 0.9180 0.4098 0.1468  0.0817  -0.0558 58  LEU   B N   
642  C CA  . LEU   B 49  ? 1.0043 0.9221 0.4289 0.1603  0.0789  -0.0481 58  LEU   B CA  
643  C C   . LEU   B 49  ? 1.0162 0.9330 0.4448 0.1812  0.0822  -0.0555 58  LEU   B C   
644  O O   . LEU   B 49  ? 1.0152 0.9471 0.4482 0.1852  0.0875  -0.0660 58  LEU   B O   
645  C CB  . LEU   B 49  ? 0.9959 0.9341 0.4296 0.1614  0.0727  -0.0380 58  LEU   B CB  
646  C CG  . LEU   B 49  ? 1.0143 0.9575 0.4447 0.1454  0.0693  -0.0304 58  LEU   B CG  
647  C CD1 . LEU   B 49  ? 1.0097 0.9696 0.4455 0.1500  0.0631  -0.0234 58  LEU   B CD1 
648  C CD2 . LEU   B 49  ? 1.0320 0.9527 0.4551 0.1384  0.0697  -0.0229 58  LEU   B CD2 
649  N N   . ARG   B 50  ? 1.0286 0.9284 0.4546 0.1964  0.0798  -0.0490 59  ARG   B N   
650  C CA  . ARG   B 50  ? 1.0467 0.9445 0.4751 0.2200  0.0812  -0.0547 59  ARG   B CA  
651  C C   . ARG   B 50  ? 1.0457 0.9599 0.4829 0.2358  0.0733  -0.0471 59  ARG   B C   
652  O O   . ARG   B 50  ? 1.0458 0.9528 0.4769 0.2321  0.0690  -0.0352 59  ARG   B O   
653  C CB  . ARG   B 50  ? 1.0953 0.9464 0.5045 0.2268  0.0851  -0.0556 59  ARG   B CB  
654  C CG  . ARG   B 50  ? 1.1589 0.9973 0.5644 0.2555  0.0852  -0.0571 59  ARG   B CG  
655  C CD  . ARG   B 50  ? 1.2303 1.0174 0.6142 0.2612  0.0900  -0.0607 59  ARG   B CD  
656  N NE  . ARG   B 50  ? 1.2815 1.0300 0.6524 0.2452  0.0900  -0.0485 59  ARG   B NE  
657  C CZ  . ARG   B 50  ? 1.3165 1.0399 0.6783 0.2547  0.0896  -0.0335 59  ARG   B CZ  
658  N NH1 . ARG   B 50  ? 1.3104 1.0424 0.6716 0.2818  0.0868  -0.0295 59  ARG   B NH1 
659  N NH2 . ARG   B 50  ? 1.3300 1.0216 0.6837 0.2374  0.0922  -0.0217 59  ARG   B NH2 
660  N N   . SER   B 51  ? 1.0431 0.9834 0.4953 0.2534  0.0710  -0.0545 60  SER   B N   
661  C CA  . SER   B 51  ? 1.0536 1.0112 0.5140 0.2703  0.0605  -0.0503 60  SER   B CA  
662  C C   . SER   B 51  ? 1.0758 1.0340 0.5393 0.2988  0.0598  -0.0566 60  SER   B C   
663  O O   . SER   B 51  ? 1.0623 1.0586 0.5498 0.3065  0.0586  -0.0668 60  SER   B O   
664  C CB  . SER   B 51  ? 1.0441 1.0455 0.5282 0.2598  0.0541  -0.0544 60  SER   B CB  
665  O OG  . SER   B 51  ? 1.0609 1.0768 0.5509 0.2749  0.0407  -0.0520 60  SER   B OG  
666  N N   . GLY   B 52  ? 1.1060 1.0224 0.5461 0.3142  0.0614  -0.0499 61  GLY   B N   
667  C CA  . GLY   B 52  ? 1.1229 1.0310 0.5598 0.3439  0.0614  -0.0551 61  GLY   B CA  
668  C C   . GLY   B 52  ? 1.1366 1.0386 0.5743 0.3415  0.0726  -0.0676 61  GLY   B C   
669  O O   . GLY   B 52  ? 1.1600 1.0259 0.5797 0.3256  0.0799  -0.0668 61  GLY   B O   
670  N N   . GLU   B 53  ? 1.1201 1.0605 0.5797 0.3562  0.0739  -0.0798 62  GLU   B N   
671  C CA  . GLU   B 53  ? 1.1318 1.0717 0.5910 0.3565  0.0861  -0.0925 62  GLU   B CA  
672  C C   . GLU   B 53  ? 1.1162 1.0902 0.5919 0.3286  0.0926  -0.0974 62  GLU   B C   
673  O O   . GLU   B 53  ? 1.1261 1.0895 0.5913 0.3223  0.1033  -0.1057 62  GLU   B O   
674  C CB  . GLU   B 53  ? 1.1591 1.1246 0.6329 0.3893  0.0874  -0.1025 62  GLU   B CB  
675  C CG  . GLU   B 53  ? 1.2680 1.1811 0.7120 0.4163  0.0902  -0.1042 62  GLU   B CG  
676  C CD  . GLU   B 53  ? 1.3742 1.3152 0.8330 0.4538  0.0897  -0.1130 62  GLU   B CD  
677  O OE1 . GLU   B 53  ? 1.3737 1.3664 0.8631 0.4638  0.0800  -0.1123 62  GLU   B OE1 
678  O OE2 . GLU   B 53  ? 1.4164 1.3275 0.8562 0.4740  0.0978  -0.1214 62  GLU   B OE2 
679  N N   . GLY   B 54  ? 1.0899 1.1013 0.5879 0.3139  0.0858  -0.0926 63  GLY   B N   
680  C CA  . GLY   B 54  ? 1.0736 1.1151 0.5862 0.2884  0.0915  -0.0948 63  GLY   B CA  
681  C C   . GLY   B 54  ? 1.0832 1.0943 0.5733 0.2626  0.0937  -0.0893 63  GLY   B C   
682  O O   . GLY   B 54  ? 1.1078 1.0842 0.5794 0.2589  0.0878  -0.0806 63  GLY   B O   
683  N N   . ARG   B 55  ? 1.0602 1.0870 0.5527 0.2451  0.1025  -0.0935 64  ARG   B N   
684  C CA  . ARG   B 55  ? 1.0615 1.0656 0.5338 0.2218  0.1035  -0.0897 64  ARG   B CA  
685  C C   . ARG   B 55  ? 1.0259 1.0572 0.5116 0.2012  0.1005  -0.0831 64  ARG   B C   
686  O O   . ARG   B 55  ? 1.0106 1.0796 0.5194 0.1996  0.1041  -0.0853 64  ARG   B O   
687  C CB  . ARG   B 55  ? 1.0861 1.0783 0.5409 0.2205  0.1153  -0.1003 64  ARG   B CB  
688  C CG  . ARG   B 55  ? 1.1406 1.1084 0.5721 0.1991  0.1144  -0.0989 64  ARG   B CG  
689  C CD  . ARG   B 55  ? 1.1857 1.1413 0.5959 0.2011  0.1242  -0.1114 64  ARG   B CD  
690  N NE  . ARG   B 55  ? 1.2267 1.1676 0.6165 0.1806  0.1216  -0.1111 64  ARG   B NE  
691  C CZ  . ARG   B 55  ? 1.2588 1.1648 0.6211 0.1781  0.1200  -0.1203 64  ARG   B CZ  
692  N NH1 . ARG   B 55  ? 1.2589 1.1353 0.6086 0.1942  0.1216  -0.1304 64  ARG   B NH1 
693  N NH2 . ARG   B 55  ? 1.2518 1.1504 0.5981 0.1602  0.1153  -0.1202 64  ARG   B NH2 
694  N N   . LEU   B 56  ? 1.0093 1.0215 0.4814 0.1858  0.0941  -0.0747 65  LEU   B N   
695  C CA  . LEU   B 56  ? 0.9853 1.0154 0.4641 0.1682  0.0908  -0.0685 65  LEU   B CA  
696  C C   . LEU   B 56  ? 0.9774 0.9941 0.4361 0.1516  0.0956  -0.0684 65  LEU   B C   
697  O O   . LEU   B 56  ? 0.9956 0.9851 0.4370 0.1472  0.0918  -0.0660 65  LEU   B O   
698  C CB  . LEU   B 56  ? 0.9901 1.0121 0.4682 0.1674  0.0786  -0.0584 65  LEU   B CB  
699  C CG  . LEU   B 56  ? 0.9979 1.0272 0.4881 0.1857  0.0704  -0.0574 65  LEU   B CG  
700  C CD1 . LEU   B 56  ? 1.0014 1.0221 0.4846 0.1844  0.0598  -0.0476 65  LEU   B CD1 
701  C CD2 . LEU   B 56  ? 0.9871 1.0549 0.5054 0.1900  0.0697  -0.0642 65  LEU   B CD2 
702  N N   . ASP   B 57  ? 0.9470 0.9832 0.4083 0.1424  0.1037  -0.0706 66  ASP   B N   
703  C CA  . ASP   B 57  ? 0.9419 0.9663 0.3802 0.1294  0.1077  -0.0708 66  ASP   B CA  
704  C C   . ASP   B 57  ? 0.9162 0.9444 0.3520 0.1142  0.1017  -0.0607 66  ASP   B C   
705  O O   . ASP   B 57  ? 0.9048 0.9518 0.3580 0.1108  0.1006  -0.0561 66  ASP   B O   
706  C CB  . ASP   B 57  ? 0.9652 1.0050 0.4007 0.1313  0.1226  -0.0780 66  ASP   B CB  
707  C CG  . ASP   B 57  ? 1.0376 1.0719 0.4713 0.1494  0.1293  -0.0893 66  ASP   B CG  
708  O OD1 . ASP   B 57  ? 1.0655 1.0678 0.4809 0.1541  0.1241  -0.0941 66  ASP   B OD1 
709  O OD2 . ASP   B 57  ? 1.0512 1.1131 0.5028 0.1588  0.1399  -0.0932 66  ASP   B OD2 
710  N N   . PRO   B 58  ? 0.9050 0.9150 0.3195 0.1053  0.0969  -0.0578 67  PRO   B N   
711  C CA  . PRO   B 58  ? 0.8861 0.8985 0.2954 0.0942  0.0915  -0.0483 67  PRO   B CA  
712  C C   . PRO   B 58  ? 0.8640 0.8902 0.2710 0.0866  0.1009  -0.0463 67  PRO   B C   
713  O O   . PRO   B 58  ? 0.8644 0.8951 0.2635 0.0877  0.1123  -0.0521 67  PRO   B O   
714  C CB  . PRO   B 58  ? 0.9116 0.9060 0.3001 0.0890  0.0851  -0.0478 67  PRO   B CB  
715  C CG  . PRO   B 58  ? 0.9292 0.9125 0.3065 0.0929  0.0902  -0.0592 67  PRO   B CG  
716  C CD  . PRO   B 58  ? 0.9104 0.8975 0.3051 0.1052  0.0952  -0.0640 67  PRO   B CD  
717  N N   . TYR   B 59  ? 0.8398 0.8711 0.2527 0.0794  0.0970  -0.0379 68  TYR   B N   
718  C CA  . TYR   B 59  ? 0.8123 0.8531 0.2244 0.0697  0.1065  -0.0335 68  TYR   B CA  
719  C C   . TYR   B 59  ? 0.8287 0.8532 0.2158 0.0618  0.1019  -0.0247 68  TYR   B C   
720  O O   . TYR   B 59  ? 0.8369 0.8582 0.2047 0.0565  0.1110  -0.0217 68  TYR   B O   
721  C CB  . TYR   B 59  ? 0.7731 0.8324 0.2163 0.0670  0.1059  -0.0323 68  TYR   B CB  
722  C CG  . TYR   B 59  ? 0.7453 0.8145 0.1942 0.0533  0.1160  -0.0263 68  TYR   B CG  
723  C CD1 . TYR   B 59  ? 0.7526 0.8050 0.1877 0.0429  0.1110  -0.0169 68  TYR   B CD1 
724  C CD2 . TYR   B 59  ? 0.7206 0.8163 0.1917 0.0512  0.1307  -0.0294 68  TYR   B CD2 
725  C CE1 . TYR   B 59  ? 0.7479 0.8042 0.1877 0.0285  0.1210  -0.0098 68  TYR   B CE1 
726  C CE2 . TYR   B 59  ? 0.7163 0.8224 0.1967 0.0360  0.1419  -0.0220 68  TYR   B CE2 
727  C CZ  . TYR   B 59  ? 0.7384 0.8222 0.2024 0.0236  0.1368  -0.0118 68  TYR   B CZ  
728  O OH  . TYR   B 59  ? 0.7500 0.8392 0.2232 0.0067  0.1481  -0.0032 68  TYR   B OH  
729  N N   . TRP   B 60  ? 0.8351 0.8494 0.2207 0.0631  0.0886  -0.0198 69  TRP   B N   
730  C CA  . TRP   B 60  ? 0.8584 0.8576 0.2206 0.0596  0.0824  -0.0115 69  TRP   B CA  
731  C C   . TRP   B 60  ? 0.8517 0.8449 0.2105 0.0669  0.0700  -0.0111 69  TRP   B C   
732  O O   . TRP   B 60  ? 0.8419 0.8393 0.2173 0.0730  0.0663  -0.0143 69  TRP   B O   
733  C CB  . TRP   B 60  ? 0.8667 0.8605 0.2327 0.0533  0.0801  -0.0039 69  TRP   B CB  
734  C CG  . TRP   B 60  ? 0.8916 0.8667 0.2336 0.0545  0.0714  0.0046  69  TRP   B CG  
735  C CD1 . TRP   B 60  ? 0.9165 0.8789 0.2304 0.0514  0.0746  0.0112  69  TRP   B CD1 
736  C CD2 . TRP   B 60  ? 0.8886 0.8564 0.2297 0.0628  0.0581  0.0073  69  TRP   B CD2 
737  N NE1 . TRP   B 60  ? 0.9312 0.8794 0.2289 0.0576  0.0631  0.0176  69  TRP   B NE1 
738  C CE2 . TRP   B 60  ? 0.9124 0.8648 0.2271 0.0648  0.0536  0.0151  69  TRP   B CE2 
739  C CE3 . TRP   B 60  ? 0.8889 0.8618 0.2466 0.0711  0.0502  0.0043  69  TRP   B CE3 
740  C CZ2 . TRP   B 60  ? 0.9250 0.8698 0.2323 0.0749  0.0422  0.0194  69  TRP   B CZ2 
741  C CZ3 . TRP   B 60  ? 0.9025 0.8664 0.2507 0.0804  0.0400  0.0092  69  TRP   B CZ3 
742  C CH2 . TRP   B 60  ? 0.9182 0.8696 0.2428 0.0824  0.0364  0.0164  69  TRP   B CH2 
743  N N   . GLY   B 61  ? 0.8583 0.8434 0.1960 0.0668  0.0644  -0.0067 70  GLY   B N   
744  C CA  . GLY   B 61  ? 0.8645 0.8498 0.2029 0.0721  0.0541  -0.0052 70  GLY   B CA  
745  C C   . GLY   B 61  ? 0.8799 0.8608 0.1970 0.0731  0.0471  0.0010  70  GLY   B C   
746  O O   . GLY   B 61  ? 0.8979 0.8725 0.1941 0.0699  0.0505  0.0023  70  GLY   B O   
747  N N   . ASP   B 62  ? 0.8805 0.8659 0.2019 0.0790  0.0379  0.0055  71  ASP   B N   
748  C CA  . ASP   B 62  ? 0.8902 0.8759 0.1940 0.0830  0.0298  0.0115  71  ASP   B CA  
749  C C   . ASP   B 62  ? 0.8718 0.8725 0.1911 0.0882  0.0222  0.0140  71  ASP   B C   
750  O O   . ASP   B 62  ? 0.8525 0.8552 0.1841 0.0947  0.0223  0.0185  71  ASP   B O   
751  C CB  . ASP   B 62  ? 0.9300 0.9013 0.2190 0.0881  0.0288  0.0200  71  ASP   B CB  
752  C CG  . ASP   B 62  ? 1.0086 0.9741 0.2719 0.0941  0.0222  0.0265  71  ASP   B CG  
753  O OD1 . ASP   B 62  ? 1.0055 0.9845 0.2716 0.1019  0.0133  0.0288  71  ASP   B OD1 
754  O OD2 . ASP   B 62  ? 1.0646 1.0126 0.3052 0.0915  0.0262  0.0304  71  ASP   B OD2 
755  N N   . VAL   B 63  ? 0.8665 0.8789 0.1855 0.0853  0.0158  0.0111  72  VAL   B N   
756  C CA  . VAL   B 63  ? 0.8594 0.8915 0.1985 0.0871  0.0095  0.0140  72  VAL   B CA  
757  C C   . VAL   B 63  ? 0.8628 0.9036 0.1993 0.1004  0.0047  0.0247  72  VAL   B C   
758  O O   . VAL   B 63  ? 0.8542 0.9095 0.2100 0.1052  0.0052  0.0302  72  VAL   B O   
759  C CB  . VAL   B 63  ? 0.8650 0.9086 0.2066 0.0782  0.0014  0.0061  72  VAL   B CB  
760  C CG1 . VAL   B 63  ? 0.8557 0.9263 0.2184 0.0795  -0.0072 0.0110  72  VAL   B CG1 
761  C CG2 . VAL   B 63  ? 0.8716 0.9059 0.2222 0.0673  0.0063  -0.0045 72  VAL   B CG2 
762  N N   . LYS   B 64  ? 0.8809 0.9108 0.1916 0.1077  0.0012  0.0285  73  LYS   B N   
763  C CA  . LYS   B 64  ? 0.8935 0.9277 0.1974 0.1234  -0.0040 0.0378  73  LYS   B CA  
764  C C   . LYS   B 64  ? 0.9008 0.9220 0.2066 0.1314  0.0013  0.0420  73  LYS   B C   
765  O O   . LYS   B 64  ? 0.9001 0.9357 0.2186 0.1417  0.0010  0.0472  73  LYS   B O   
766  C CB  . LYS   B 64  ? 0.9411 0.9631 0.2134 0.1307  -0.0104 0.0412  73  LYS   B CB  
767  C CG  . LYS   B 64  ? 1.0042 1.0333 0.2705 0.1500  -0.0170 0.0500  73  LYS   B CG  
768  C CD  . LYS   B 64  ? 1.0702 1.0921 0.3066 0.1597  -0.0256 0.0537  73  LYS   B CD  
769  C CE  . LYS   B 64  ? 1.1213 1.1439 0.3486 0.1820  -0.0309 0.0624  73  LYS   B CE  
770  N NZ  . LYS   B 64  ? 1.1638 1.1740 0.3574 0.1948  -0.0396 0.0672  73  LYS   B NZ  
771  N N   . GLN   B 65  ? 0.9031 0.9000 0.1988 0.1262  0.0064  0.0392  74  GLN   B N   
772  C CA  . GLN   B 65  ? 0.8981 0.8828 0.1970 0.1323  0.0088  0.0402  74  GLN   B CA  
773  C C   . GLN   B 65  ? 0.8725 0.8723 0.1966 0.1313  0.0133  0.0383  74  GLN   B C   
774  O O   . GLN   B 65  ? 0.8688 0.8651 0.1946 0.1419  0.0136  0.0408  74  GLN   B O   
775  C CB  . GLN   B 65  ? 0.9288 0.8900 0.2189 0.1230  0.0125  0.0361  74  GLN   B CB  
776  C CG  . GLN   B 65  ? 0.9823 0.9213 0.2449 0.1228  0.0105  0.0403  74  GLN   B CG  
777  C CD  . GLN   B 65  ? 1.0554 0.9747 0.3159 0.1104  0.0161  0.0376  74  GLN   B CD  
778  O OE1 . GLN   B 65  ? 1.0680 0.9820 0.3405 0.1096  0.0156  0.0340  74  GLN   B OE1 
779  N NE2 . GLN   B 65  ? 1.0711 0.9811 0.3170 0.1007  0.0216  0.0395  74  GLN   B NE2 
780  N N   . ASP   B 66  ? 0.8436 0.8565 0.1837 0.1198  0.0165  0.0339  75  ASP   B N   
781  C CA  . ASP   B 66  ? 0.8222 0.8440 0.1840 0.1170  0.0216  0.0329  75  ASP   B CA  
782  C C   . ASP   B 66  ? 0.8197 0.8271 0.1831 0.1174  0.0258  0.0286  75  ASP   B C   
783  O O   . ASP   B 66  ? 0.8149 0.8233 0.1865 0.1249  0.0282  0.0315  75  ASP   B O   
784  C CB  . ASP   B 66  ? 0.8153 0.8543 0.1886 0.1276  0.0221  0.0421  75  ASP   B CB  
785  C CG  . ASP   B 66  ? 0.8287 0.8756 0.2238 0.1213  0.0286  0.0431  75  ASP   B CG  
786  O OD1 . ASP   B 66  ? 0.8342 0.8777 0.2366 0.1076  0.0296  0.0359  75  ASP   B OD1 
787  O OD2 . ASP   B 66  ? 0.8433 0.8968 0.2453 0.1310  0.0333  0.0514  75  ASP   B OD2 
788  N N   . LEU   B 67  ? 0.8160 0.8118 0.1719 0.1100  0.0270  0.0223  76  LEU   B N   
789  C CA  . LEU   B 67  ? 0.8121 0.8004 0.1749 0.1098  0.0298  0.0173  76  LEU   B CA  
790  C C   . LEU   B 67  ? 0.8031 0.7921 0.1719 0.0986  0.0361  0.0091  76  LEU   B C   
791  O O   . LEU   B 67  ? 0.8004 0.7897 0.1601 0.0910  0.0377  0.0074  76  LEU   B O   
792  C CB  . LEU   B 67  ? 0.8198 0.7950 0.1716 0.1137  0.0252  0.0180  76  LEU   B CB  
793  C CG  . LEU   B 67  ? 0.8339 0.8035 0.1748 0.1285  0.0186  0.0240  76  LEU   B CG  
794  C CD1 . LEU   B 67  ? 0.8489 0.7986 0.1748 0.1291  0.0129  0.0230  76  LEU   B CD1 
795  C CD2 . LEU   B 67  ? 0.8364 0.8104 0.1860 0.1402  0.0185  0.0245  76  LEU   B CD2 
796  N N   . VAL   B 68  ? 0.7925 0.7825 0.1748 0.0998  0.0394  0.0039  77  VAL   B N   
797  C CA  . VAL   B 68  ? 0.7949 0.7877 0.1836 0.0928  0.0467  -0.0042 77  VAL   B CA  
798  C C   . VAL   B 68  ? 0.7960 0.7933 0.1999 0.0964  0.0480  -0.0091 77  VAL   B C   
799  O O   . VAL   B 68  ? 0.7909 0.7883 0.2023 0.1063  0.0440  -0.0083 77  VAL   B O   
800  C CB  . VAL   B 68  ? 0.7981 0.7908 0.1892 0.0908  0.0498  -0.0079 77  VAL   B CB  
801  C CG1 . VAL   B 68  ? 0.8089 0.7997 0.2099 0.0985  0.0482  -0.0042 77  VAL   B CG1 
802  C CG2 . VAL   B 68  ? 0.7999 0.7929 0.1934 0.0872  0.0576  -0.0176 77  VAL   B CG2 
803  N N   . SER   B 69  ? 0.7993 0.8024 0.2080 0.0889  0.0538  -0.0136 78  SER   B N   
804  C CA  . SER   B 69  ? 0.7843 0.7989 0.2133 0.0911  0.0546  -0.0190 78  SER   B CA  
805  C C   . SER   B 69  ? 0.7750 0.7998 0.2137 0.0918  0.0649  -0.0266 78  SER   B C   
806  O O   . SER   B 69  ? 0.7927 0.8140 0.2192 0.0868  0.0723  -0.0281 78  SER   B O   
807  C CB  . SER   B 69  ? 0.7749 0.7916 0.2080 0.0815  0.0535  -0.0177 78  SER   B CB  
808  O OG  . SER   B 69  ? 0.7506 0.7713 0.1801 0.0700  0.0651  -0.0174 78  SER   B OG  
809  N N   . TYR   B 70  ? 0.7508 0.7875 0.2090 0.1004  0.0643  -0.0320 79  TYR   B N   
810  C CA  . TYR   B 70  ? 0.7373 0.7838 0.2057 0.1064  0.0732  -0.0398 79  TYR   B CA  
811  C C   . TYR   B 70  ? 0.7331 0.8058 0.2281 0.1060  0.0757  -0.0444 79  TYR   B C   
812  O O   . TYR   B 70  ? 0.7227 0.8028 0.2314 0.1077  0.0653  -0.0440 79  TYR   B O   
813  C CB  . TYR   B 70  ? 0.7273 0.7635 0.1956 0.1217  0.0689  -0.0412 79  TYR   B CB  
814  C CG  . TYR   B 70  ? 0.7206 0.7343 0.1692 0.1200  0.0688  -0.0375 79  TYR   B CG  
815  C CD1 . TYR   B 70  ? 0.7134 0.7171 0.1528 0.1184  0.0615  -0.0288 79  TYR   B CD1 
816  C CD2 . TYR   B 70  ? 0.7196 0.7233 0.1593 0.1192  0.0759  -0.0435 79  TYR   B CD2 
817  C CE1 . TYR   B 70  ? 0.7262 0.7157 0.1538 0.1142  0.0616  -0.0251 79  TYR   B CE1 
818  C CE2 . TYR   B 70  ? 0.7316 0.7163 0.1568 0.1140  0.0740  -0.0415 79  TYR   B CE2 
819  C CZ  . TYR   B 70  ? 0.7447 0.7248 0.1667 0.1106  0.0669  -0.0318 79  TYR   B CZ  
820  O OH  . TYR   B 70  ? 0.7689 0.7362 0.1830 0.1039  0.0649  -0.0296 79  TYR   B OH  
821  N N   . CYS   B 71  ? 0.7237 0.8120 0.2267 0.1044  0.0892  -0.0496 80  CYS   B N   
822  C CA  . CYS   B 71  ? 0.7198 0.8408 0.2537 0.1036  0.0953  -0.0540 80  CYS   B CA  
823  C C   . CYS   B 71  ? 0.7037 0.8362 0.2482 0.0845  0.0982  -0.0487 80  CYS   B C   
824  O O   . CYS   B 71  ? 0.6841 0.8446 0.2518 0.0786  0.1099  -0.0504 80  CYS   B O   
825  C CB  . CYS   B 71  ? 0.7455 0.8814 0.3030 0.1185  0.0843  -0.0592 80  CYS   B CB  
826  S SG  . CYS   B 71  ? 0.8936 1.0108 0.4371 0.1419  0.0828  -0.0635 80  CYS   B SG  
827  N N   . GLY   B 72  ? 0.7056 0.8162 0.2331 0.0754  0.0890  -0.0418 81  GLY   B N   
828  C CA  . GLY   B 72  ? 0.7088 0.8211 0.2416 0.0571  0.0910  -0.0359 81  GLY   B CA  
829  C C   . GLY   B 72  ? 0.7314 0.8117 0.2345 0.0514  0.0827  -0.0279 81  GLY   B C   
830  O O   . GLY   B 72  ? 0.7408 0.8025 0.2221 0.0612  0.0758  -0.0268 81  GLY   B O   
831  N N   . PRO   B 73  ? 0.7322 0.8060 0.2350 0.0354  0.0842  -0.0217 82  PRO   B N   
832  C CA  . PRO   B 73  ? 0.7556 0.7967 0.2278 0.0325  0.0761  -0.0140 82  PRO   B CA  
833  C C   . PRO   B 73  ? 0.7719 0.7999 0.2412 0.0427  0.0567  -0.0165 82  PRO   B C   
834  O O   . PRO   B 73  ? 0.7495 0.7921 0.2422 0.0477  0.0478  -0.0238 82  PRO   B O   
835  C CB  . PRO   B 73  ? 0.7639 0.7989 0.2384 0.0129  0.0833  -0.0068 82  PRO   B CB  
836  C CG  . PRO   B 73  ? 0.7381 0.8071 0.2548 0.0039  0.0901  -0.0121 82  PRO   B CG  
837  C CD  . PRO   B 73  ? 0.7047 0.8003 0.2362 0.0192  0.0939  -0.0209 82  PRO   B CD  
838  N N   . TRP   B 74  ? 0.8019 0.8038 0.2411 0.0479  0.0499  -0.0105 83  TRP   B N   
839  C CA  . TRP   B 74  ? 0.8139 0.8018 0.2445 0.0601  0.0338  -0.0116 83  TRP   B CA  
840  C C   . TRP   B 74  ? 0.8399 0.8228 0.2839 0.0534  0.0223  -0.0160 83  TRP   B C   
841  O O   . TRP   B 74  ? 0.8505 0.8209 0.2923 0.0380  0.0247  -0.0123 83  TRP   B O   
842  C CB  . TRP   B 74  ? 0.8245 0.7890 0.2222 0.0659  0.0311  -0.0034 83  TRP   B CB  
843  C CG  . TRP   B 74  ? 0.8310 0.7847 0.2175 0.0821  0.0181  -0.0034 83  TRP   B CG  
844  C CD1 . TRP   B 74  ? 0.8446 0.7780 0.2195 0.0860  0.0062  -0.0037 83  TRP   B CD1 
845  C CD2 . TRP   B 74  ? 0.8298 0.7907 0.2132 0.0971  0.0171  -0.0024 83  TRP   B CD2 
846  N NE1 . TRP   B 74  ? 0.8595 0.7894 0.2228 0.1048  -0.0014 -0.0032 83  TRP   B NE1 
847  C CE2 . TRP   B 74  ? 0.8457 0.7937 0.2161 0.1109  0.0059  -0.0014 83  TRP   B CE2 
848  C CE3 . TRP   B 74  ? 0.8265 0.8014 0.2164 0.0998  0.0249  -0.0023 83  TRP   B CE3 
849  C CZ2 . TRP   B 74  ? 0.8511 0.8032 0.2159 0.1271  0.0048  0.0018  83  TRP   B CZ2 
850  C CZ3 . TRP   B 74  ? 0.8361 0.8122 0.2224 0.1132  0.0225  0.0006  83  TRP   B CZ3 
851  C CH2 . TRP   B 74  ? 0.8450 0.8117 0.2197 0.1267  0.0136  0.0036  83  TRP   B CH2 
852  N N   . LYS   B 75  ? 0.8447 0.8365 0.3023 0.0645  0.0095  -0.0242 84  LYS   B N   
853  C CA  . LYS   B 75  ? 0.8574 0.8480 0.3308 0.0586  -0.0048 -0.0318 84  LYS   B CA  
854  C C   . LYS   B 75  ? 0.8953 0.8572 0.3436 0.0708  -0.0225 -0.0337 84  LYS   B C   
855  O O   . LYS   B 75  ? 0.8929 0.8451 0.3479 0.0641  -0.0363 -0.0408 84  LYS   B O   
856  C CB  . LYS   B 75  ? 0.8472 0.8703 0.3534 0.0646  -0.0096 -0.0419 84  LYS   B CB  
857  C CG  . LYS   B 75  ? 0.8581 0.9132 0.3915 0.0573  0.0070  -0.0423 84  LYS   B CG  
858  C CD  . LYS   B 75  ? 0.8946 0.9641 0.4561 0.0338  0.0123  -0.0431 84  LYS   B CD  
859  C CE  . LYS   B 75  ? 0.9127 1.0158 0.4990 0.0285  0.0318  -0.0425 84  LYS   B CE  
860  N NZ  . LYS   B 75  ? 0.9133 1.0398 0.5362 0.0062  0.0372  -0.0435 84  LYS   B NZ  
861  N N   . LEU   B 76  ? 0.9209 0.8713 0.3424 0.0895  -0.0228 -0.0286 85  LEU   B N   
862  C CA  . LEU   B 76  ? 0.9506 0.8767 0.3453 0.1061  -0.0371 -0.0299 85  LEU   B CA  
863  C C   . LEU   B 76  ? 0.9893 0.8831 0.3586 0.1003  -0.0386 -0.0245 85  LEU   B C   
864  O O   . LEU   B 76  ? 0.9966 0.8862 0.3534 0.0977  -0.0271 -0.0148 85  LEU   B O   
865  C CB  . LEU   B 76  ? 0.9523 0.8835 0.3319 0.1281  -0.0334 -0.0245 85  LEU   B CB  
866  C CG  . LEU   B 76  ? 0.9471 0.9045 0.3470 0.1346  -0.0288 -0.0269 85  LEU   B CG  
867  C CD1 . LEU   B 76  ? 0.9541 0.9109 0.3378 0.1529  -0.0236 -0.0192 85  LEU   B CD1 
868  C CD2 . LEU   B 76  ? 0.9504 0.9161 0.3646 0.1401  -0.0433 -0.0382 85  LEU   B CD2 
869  N N   . ASP   B 77  ? 1.0108 0.8798 0.3714 0.0987  -0.0541 -0.0316 86  ASP   B N   
870  C CA  . ASP   B 77  ? 1.0493 0.8808 0.3841 0.0932  -0.0565 -0.0269 86  ASP   B CA  
871  C C   . ASP   B 77  ? 1.0780 0.8747 0.3824 0.1100  -0.0748 -0.0336 86  ASP   B C   
872  O O   . ASP   B 77  ? 1.1019 0.8623 0.3895 0.1022  -0.0815 -0.0342 86  ASP   B O   
873  C CB  . ASP   B 77  ? 1.0721 0.8983 0.4270 0.0637  -0.0527 -0.0270 86  ASP   B CB  
874  C CG  . ASP   B 77  ? 1.1416 0.9734 0.5245 0.0511  -0.0674 -0.0406 86  ASP   B CG  
875  O OD1 . ASP   B 77  ? 1.1566 1.0061 0.5485 0.0655  -0.0789 -0.0506 86  ASP   B OD1 
876  O OD2 . ASP   B 77  ? 1.1732 0.9920 0.5692 0.0269  -0.0676 -0.0409 86  ASP   B OD2 
877  N N   . ALA   B 78  ? 1.0815 0.8857 0.3755 0.1340  -0.0822 -0.0380 87  ALA   B N   
878  C CA  . ALA   B 78  ? 1.1143 0.8858 0.3744 0.1544  -0.0988 -0.0451 87  ALA   B CA  
879  C C   . ALA   B 78  ? 1.1477 0.9059 0.3734 0.1765  -0.0914 -0.0342 87  ALA   B C   
880  O O   . ALA   B 78  ? 1.1438 0.9277 0.3763 0.1802  -0.0759 -0.0230 87  ALA   B O   
881  C CB  . ALA   B 78  ? 1.1018 0.8872 0.3647 0.1711  -0.1113 -0.0557 87  ALA   B CB  
882  N N   . ALA   B 79  ? 1.1807 0.8994 0.3705 0.1913  -0.1030 -0.0380 88  ALA   B N   
883  C CA  . ALA   B 79  ? 1.2105 0.9197 0.3693 0.2144  -0.0960 -0.0277 88  ALA   B CA  
884  C C   . ALA   B 79  ? 1.2431 0.9340 0.3673 0.2464  -0.1067 -0.0340 88  ALA   B C   
885  O O   . ALA   B 79  ? 1.2600 0.9217 0.3699 0.2488  -0.1248 -0.0483 88  ALA   B O   
886  C CB  . ALA   B 79  ? 1.2310 0.9070 0.3732 0.2049  -0.0948 -0.0221 88  ALA   B CB  
887  N N   . TRP   B 80  ? 1.2517 0.9595 0.3616 0.2712  -0.0956 -0.0235 89  TRP   B N   
888  C CA  . TRP   B 80  ? 1.2894 0.9823 0.3622 0.3061  -0.1012 -0.0264 89  TRP   B CA  
889  C C   . TRP   B 80  ? 1.3438 0.9845 0.3793 0.3149  -0.1138 -0.0330 89  TRP   B C   
890  O O   . TRP   B 80  ? 1.3535 0.9827 0.3879 0.3055  -0.1087 -0.0254 89  TRP   B O   
891  C CB  . TRP   B 80  ? 1.2773 1.0040 0.3495 0.3262  -0.0827 -0.0105 89  TRP   B CB  
892  C CG  . TRP   B 80  ? 1.3003 1.0164 0.3343 0.3642  -0.0840 -0.0107 89  TRP   B CG  
893  C CD1 . TRP   B 80  ? 1.3265 1.0304 0.3374 0.3840  -0.0936 -0.0206 89  TRP   B CD1 
894  C CD2 . TRP   B 80  ? 1.3047 1.0255 0.3189 0.3894  -0.0742 -0.0002 89  TRP   B CD2 
895  N NE1 . TRP   B 80  ? 1.3475 1.0450 0.3221 0.4204  -0.0893 -0.0167 89  TRP   B NE1 
896  C CE2 . TRP   B 80  ? 1.3313 1.0418 0.3100 0.4243  -0.0766 -0.0039 89  TRP   B CE2 
897  C CE3 . TRP   B 80  ? 1.2978 1.0329 0.3206 0.3875  -0.0641 0.0118  89  TRP   B CE3 
898  C CZ2 . TRP   B 80  ? 1.3402 1.0559 0.2941 0.4571  -0.0674 0.0046  89  TRP   B CZ2 
899  C CZ3 . TRP   B 80  ? 1.3137 1.0553 0.3142 0.4196  -0.0572 0.0195  89  TRP   B CZ3 
900  C CH2 . TRP   B 80  ? 1.3277 1.0614 0.2959 0.4538  -0.0576 0.0163  89  TRP   B CH2 
901  N N   . ASP   B 81  ? 1.3835 0.9889 0.3869 0.3323  -0.1316 -0.0477 90  ASP   B N   
902  C CA  . ASP   B 81  ? 1.4383 0.9856 0.4030 0.3405  -0.1458 -0.0561 90  ASP   B CA  
903  C C   . ASP   B 81  ? 1.4676 1.0033 0.3940 0.3763  -0.1382 -0.0476 90  ASP   B C   
904  O O   . ASP   B 81  ? 1.4970 0.9803 0.3844 0.3897  -0.1502 -0.0551 90  ASP   B O   
905  C CB  . ASP   B 81  ? 1.4878 0.9967 0.4309 0.3444  -0.1708 -0.0780 90  ASP   B CB  
906  C CG  . ASP   B 81  ? 1.5766 1.0926 0.4909 0.3805  -0.1752 -0.0844 90  ASP   B CG  
907  O OD1 . ASP   B 81  ? 1.5822 1.1397 0.5013 0.3988  -0.1562 -0.0702 90  ASP   B OD1 
908  O OD2 . ASP   B 81  ? 1.6268 1.1059 0.5129 0.3903  -0.1978 -0.1037 90  ASP   B OD2 
909  N N   . GLY   B 82  ? 1.4523 1.0364 0.3911 0.3912  -0.1189 -0.0325 91  GLY   B N   
910  C CA  . GLY   B 82  ? 1.4679 1.0558 0.3798 0.4256  -0.1092 -0.0228 91  GLY   B CA  
911  C C   . GLY   B 82  ? 1.4951 1.0597 0.3609 0.4652  -0.1165 -0.0320 91  GLY   B C   
912  O O   . GLY   B 82  ? 1.5124 1.0672 0.3471 0.4974  -0.1121 -0.0277 91  GLY   B O   
913  N N   . LEU   B 83  ? 1.4982 1.0542 0.3572 0.4658  -0.1283 -0.0454 92  LEU   B N   
914  C CA  . LEU   B 83  ? 1.5269 1.0551 0.3361 0.5039  -0.1380 -0.0569 92  LEU   B CA  
915  C C   . LEU   B 83  ? 1.5151 1.0698 0.3259 0.5139  -0.1370 -0.0596 92  LEU   B C   
916  O O   . LEU   B 83  ? 1.5252 1.0902 0.3064 0.5507  -0.1278 -0.0551 92  LEU   B O   
917  C CB  . LEU   B 83  ? 1.5719 1.0296 0.3471 0.4999  -0.1656 -0.0788 92  LEU   B CB  
918  C CG  . LEU   B 83  ? 1.6285 1.0392 0.3669 0.5168  -0.1691 -0.0793 92  LEU   B CG  
919  C CD1 . LEU   B 83  ? 1.6600 1.0152 0.3985 0.4849  -0.1884 -0.0911 92  LEU   B CD1 
920  C CD2 . LEU   B 83  ? 1.6552 1.0344 0.3335 0.5651  -0.1753 -0.0889 92  LEU   B CD2 
921  N N   . SER   B 84  ? 1.4918 1.0556 0.3338 0.4839  -0.1465 -0.0669 93  SER   B N   
922  C CA  . SER   B 84  ? 1.4790 1.0608 0.3186 0.4939  -0.1499 -0.0715 93  SER   B CA  
923  C C   . SER   B 84  ? 1.4409 1.0799 0.3090 0.4961  -0.1240 -0.0506 93  SER   B C   
924  O O   . SER   B 84  ? 1.4244 1.0950 0.3290 0.4776  -0.1061 -0.0348 93  SER   B O   
925  C CB  . SER   B 84  ? 1.4895 1.0618 0.3538 0.4627  -0.1715 -0.0880 93  SER   B CB  
926  O OG  . SER   B 84  ? 1.5408 1.0686 0.4020 0.4421  -0.1914 -0.1030 93  SER   B OG  
927  N N   . GLU   B 85  ? 1.4320 1.0818 0.2820 0.5183  -0.1228 -0.0507 94  GLU   B N   
928  C CA  . GLU   B 85  ? 1.4000 1.0977 0.2759 0.5182  -0.0994 -0.0311 94  GLU   B CA  
929  C C   . GLU   B 85  ? 1.3633 1.0806 0.2892 0.4796  -0.1032 -0.0326 94  GLU   B C   
930  O O   . GLU   B 85  ? 1.3723 1.0691 0.3056 0.4613  -0.1255 -0.0503 94  GLU   B O   
931  C CB  . GLU   B 85  ? 1.4361 1.1339 0.2723 0.5547  -0.0970 -0.0299 94  GLU   B CB  
932  C CG  . GLU   B 85  ? 1.4967 1.1819 0.2833 0.5965  -0.0881 -0.0258 94  GLU   B CG  
933  C CD  . GLU   B 85  ? 1.5162 1.2209 0.2759 0.6300  -0.0699 -0.0118 94  GLU   B CD  
934  O OE1 . GLU   B 85  ? 1.5194 1.2233 0.2725 0.6321  -0.0776 -0.0158 94  GLU   B OE1 
935  O OE2 . GLU   B 85  ? 1.5137 1.2360 0.2592 0.6550  -0.0472 0.0040  94  GLU   B OE2 
936  N N   . VAL   B 86  ? 1.3178 1.0753 0.2798 0.4666  -0.0810 -0.0142 95  VAL   B N   
937  C CA  . VAL   B 86  ? 1.2753 1.0541 0.2835 0.4337  -0.0803 -0.0133 95  VAL   B CA  
938  C C   . VAL   B 86  ? 1.2464 1.0506 0.2596 0.4441  -0.0664 -0.0009 95  VAL   B C   
939  O O   . VAL   B 86  ? 1.2600 1.0657 0.2420 0.4745  -0.0560 0.0085  95  VAL   B O   
940  C CB  . VAL   B 86  ? 1.2576 1.0554 0.3041 0.4054  -0.0672 -0.0033 95  VAL   B CB  
941  C CG1 . VAL   B 86  ? 1.2730 1.0418 0.3064 0.4007  -0.0781 -0.0119 95  VAL   B CG1 
942  C CG2 . VAL   B 86  ? 1.2489 1.0798 0.3056 0.4137  -0.0413 0.0182  95  VAL   B CG2 
943  N N   . GLN   B 87  ? 1.2035 1.0249 0.2527 0.4209  -0.0659 -0.0005 96  GLN   B N   
944  C CA  . GLN   B 87  ? 1.1773 1.0173 0.2310 0.4292  -0.0527 0.0121  96  GLN   B CA  
945  C C   . GLN   B 87  ? 1.1399 1.0065 0.2402 0.4005  -0.0364 0.0236  96  GLN   B C   
946  O O   . GLN   B 87  ? 1.1340 1.0036 0.2645 0.3737  -0.0444 0.0143  96  GLN   B O   
947  C CB  . GLN   B 87  ? 1.1904 1.0187 0.2299 0.4399  -0.0725 -0.0016 96  GLN   B CB  
948  C CG  . GLN   B 87  ? 1.2360 1.0512 0.2248 0.4795  -0.0724 0.0018  96  GLN   B CG  
949  C CD  . GLN   B 87  ? 1.2740 1.0737 0.2416 0.4935  -0.0982 -0.0158 96  GLN   B CD  
950  O OE1 . GLN   B 87  ? 1.2512 1.0614 0.2479 0.4773  -0.1083 -0.0229 96  GLN   B OE1 
951  N NE2 . GLN   B 87  ? 1.3232 1.0990 0.2388 0.5259  -0.1102 -0.0241 96  GLN   B NE2 
952  N N   . LEU   B 88  ? 1.1107 0.9960 0.2169 0.4053  -0.0131 0.0437  97  LEU   B N   
953  C CA  . LEU   B 88  ? 1.0757 0.9822 0.2226 0.3793  0.0011  0.0535  97  LEU   B CA  
954  C C   . LEU   B 88  ? 1.0781 0.9828 0.2272 0.3827  0.0004  0.0545  97  LEU   B C   
955  O O   . LEU   B 88  ? 1.0871 0.9880 0.2113 0.4060  0.0090  0.0657  97  LEU   B O   
956  C CB  . LEU   B 88  ? 1.0550 0.9823 0.2108 0.3804  0.0254  0.0744  97  LEU   B CB  
957  C CG  . LEU   B 88  ? 1.0388 0.9846 0.2337 0.3547  0.0398  0.0847  97  LEU   B CG  
958  C CD1 . LEU   B 88  ? 1.0228 0.9721 0.2471 0.3256  0.0311  0.0731  97  LEU   B CD1 
959  C CD2 . LEU   B 88  ? 1.0301 0.9981 0.2357 0.3557  0.0624  0.1053  97  LEU   B CD2 
960  N N   . LEU   B 89  ? 1.0637 0.9707 0.2399 0.3622  -0.0089 0.0438  98  LEU   B N   
961  C CA  . LEU   B 89  ? 1.0649 0.9713 0.2445 0.3671  -0.0091 0.0453  98  LEU   B CA  
962  C C   . LEU   B 89  ? 1.0574 0.9754 0.2604 0.3524  0.0137  0.0624  98  LEU   B C   
963  O O   . LEU   B 89  ? 1.0417 0.9681 0.2765 0.3279  0.0156  0.0587  98  LEU   B O   
964  C CB  . LEU   B 89  ? 1.0599 0.9677 0.2600 0.3541  -0.0283 0.0262  98  LEU   B CB  
965  C CG  . LEU   B 89  ? 1.0784 0.9885 0.2862 0.3600  -0.0303 0.0258  98  LEU   B CG  
966  C CD1 . LEU   B 89  ? 1.0956 0.9931 0.2663 0.3919  -0.0279 0.0359  98  LEU   B CD1 
967  C CD2 . LEU   B 89  ? 1.0815 0.9978 0.3065 0.3535  -0.0525 0.0053  98  LEU   B CD2 
968  N N   . ALA   B 90  ? 1.0598 0.9782 0.2466 0.3667  0.0316  0.0814  99  ALA   B N   
969  C CA  . ALA   B 90  ? 1.0427 0.9711 0.2525 0.3512  0.0532  0.0986  99  ALA   B CA  
970  C C   . ALA   B 90  ? 1.0401 0.9575 0.2536 0.3513  0.0576  0.1036  99  ALA   B C   
971  O O   . ALA   B 90  ? 1.0459 0.9496 0.2305 0.3758  0.0575  0.1094  99  ALA   B O   
972  C CB  . ALA   B 90  ? 1.0432 0.9793 0.2385 0.3650  0.0722  0.1183  99  ALA   B CB  
973  N N   . VAL   B 91  ? 1.0249 0.9460 0.2705 0.3262  0.0616  0.1016  100 VAL   B N   
974  C CA  . VAL   B 91  ? 1.0331 0.9403 0.2832 0.3255  0.0664  0.1058  100 VAL   B CA  
975  C C   . VAL   B 91  ? 1.0440 0.9514 0.3118 0.3080  0.0876  0.1232  100 VAL   B C   
976  O O   . VAL   B 91  ? 1.0312 0.9454 0.3278 0.2826  0.0891  0.1179  100 VAL   B O   
977  C CB  . VAL   B 91  ? 1.0207 0.9299 0.2922 0.3121  0.0519  0.0862  100 VAL   B CB  
978  C CG1 . VAL   B 91  ? 1.0284 0.9215 0.3020 0.3156  0.0559  0.0891  100 VAL   B CG1 
979  C CG2 . VAL   B 91  ? 1.0215 0.9355 0.2835 0.3234  0.0304  0.0685  100 VAL   B CG2 
980  N N   . PRO   B 92  ? 1.0651 0.9657 0.3160 0.3209  0.1044  0.1442  101 PRO   B N   
981  C CA  . PRO   B 92  ? 1.0700 0.9730 0.3423 0.3012  0.1250  0.1619  101 PRO   B CA  
982  C C   . PRO   B 92  ? 1.0986 0.9760 0.3782 0.2916  0.1316  0.1668  101 PRO   B C   
983  O O   . PRO   B 92  ? 1.1178 0.9731 0.3757 0.3100  0.1258  0.1647  101 PRO   B O   
984  C CB  . PRO   B 92  ? 1.0720 0.9786 0.3214 0.3212  0.1421  0.1838  101 PRO   B CB  
985  C CG  . PRO   B 92  ? 1.0833 0.9878 0.2961 0.3520  0.1278  0.1745  101 PRO   B CG  
986  C CD  . PRO   B 92  ? 1.0689 0.9605 0.2800 0.3535  0.1062  0.1536  101 PRO   B CD  
987  N N   . PRO   B 93  ? 1.1002 0.9785 0.4081 0.2645  0.1435  0.1743  102 PRO   B N   
988  C CA  . PRO   B 93  ? 1.1196 0.9664 0.4315 0.2553  0.1500  0.1790  102 PRO   B CA  
989  C C   . PRO   B 93  ? 1.1612 0.9783 0.4418 0.2780  0.1629  0.1993  102 PRO   B C   
990  O O   . PRO   B 93  ? 1.1738 0.9957 0.4432 0.2863  0.1793  0.2204  102 PRO   B O   
991  C CB  . PRO   B 93  ? 1.1091 0.9650 0.4559 0.2222  0.1607  0.1852  102 PRO   B CB  
992  C CG  . PRO   B 93  ? 1.0907 0.9853 0.4558 0.2127  0.1522  0.1744  102 PRO   B CG  
993  C CD  . PRO   B 93  ? 1.0758 0.9830 0.4139 0.2413  0.1492  0.1768  102 PRO   B CD  
994  N N   . GLY   B 94  ? 1.1786 0.9664 0.4429 0.2909  0.1553  0.1930  103 GLY   B N   
995  C CA  . GLY   B 94  ? 1.2028 0.9567 0.4325 0.3157  0.1643  0.2104  103 GLY   B CA  
996  C C   . GLY   B 94  ? 1.2174 0.9769 0.4090 0.3513  0.1594  0.2144  103 GLY   B C   
997  O O   . GLY   B 94  ? 1.2294 0.9608 0.3864 0.3770  0.1634  0.2267  103 GLY   B O   
998  N N   . GLU   B 95  ? 1.2116 1.0039 0.4057 0.3546  0.1499  0.2039  104 GLU   B N   
999  C CA  . GLU   B 95  ? 1.2323 1.0291 0.3884 0.3878  0.1434  0.2053  104 GLU   B CA  
1000 C C   . GLU   B 95  ? 1.2444 1.0522 0.3965 0.3997  0.1147  0.1779  104 GLU   B C   
1001 O O   . GLU   B 95  ? 1.2279 1.0512 0.4117 0.3786  0.1028  0.1588  104 GLU   B O   
1002 C CB  . GLU   B 95  ? 1.2505 1.0725 0.4067 0.3866  0.1560  0.2163  104 GLU   B CB  
1003 C CG  . GLU   B 95  ? 1.3078 1.1278 0.4773 0.3709  0.1852  0.2437  104 GLU   B CG  
1004 C CD  . GLU   B 95  ? 1.3634 1.2112 0.5307 0.3759  0.2010  0.2581  104 GLU   B CD  
1005 O OE1 . GLU   B 95  ? 1.3677 1.2344 0.5219 0.3913  0.1881  0.2450  104 GLU   B OE1 
1006 O OE2 . GLU   B 95  ? 1.3756 1.2260 0.5549 0.3645  0.2267  0.2827  104 GLU   B OE2 
1007 N N   . ARG   B 96  ? 1.2688 1.0690 0.3819 0.4334  0.1037  0.1761  105 ARG   B N   
1008 C CA  . ARG   B 96  ? 1.2859 1.0965 0.3943 0.4462  0.0750  0.1507  105 ARG   B CA  
1009 C C   . ARG   B 96  ? 1.2844 1.1208 0.4049 0.4360  0.0644  0.1358  105 ARG   B C   
1010 O O   . ARG   B 96  ? 1.2963 1.1389 0.4056 0.4386  0.0768  0.1473  105 ARG   B O   
1011 C CB  . ARG   B 96  ? 1.3391 1.1326 0.3983 0.4867  0.0657  0.1543  105 ARG   B CB  
1012 C CG  . ARG   B 96  ? 1.3960 1.2019 0.4485 0.5019  0.0337  0.1278  105 ARG   B CG  
1013 C CD  . ARG   B 96  ? 1.4746 1.2623 0.4845 0.5403  0.0213  0.1293  105 ARG   B CD  
1014 N NE  . ARG   B 96  ? 1.5574 1.3309 0.5154 0.5694  0.0298  0.1449  105 ARG   B NE  
1015 C CZ  . ARG   B 96  ? 1.6317 1.3791 0.5545 0.5890  0.0505  0.1714  105 ARG   B CZ  
1016 N NH1 . ARG   B 96  ? 1.6363 1.3651 0.5706 0.5814  0.0640  0.1848  105 ARG   B NH1 
1017 N NH2 . ARG   B 96  ? 1.6603 1.3973 0.5338 0.6172  0.0588  0.1850  105 ARG   B NH2 
1018 N N   . ALA   B 97  ? 1.2706 1.1215 0.4131 0.4256  0.0422  0.1111  106 ALA   B N   
1019 C CA  . ALA   B 97  ? 1.2679 1.1372 0.4203 0.4157  0.0296  0.0955  106 ALA   B CA  
1020 C C   . ALA   B 97  ? 1.2889 1.1529 0.3997 0.4435  0.0234  0.0966  106 ALA   B C   
1021 O O   . ALA   B 97  ? 1.3111 1.1618 0.3882 0.4722  0.0146  0.0968  106 ALA   B O   
1022 C CB  . ALA   B 97  ? 1.2584 1.1393 0.4346 0.4057  0.0066  0.0710  106 ALA   B CB  
1023 N N   . LYS   B 98  ? 1.2878 1.1610 0.3979 0.4378  0.0275  0.0969  107 LYS   B N   
1024 C CA  . LYS   B 98  ? 1.3141 1.1801 0.3811 0.4664  0.0243  0.0986  107 LYS   B CA  
1025 C C   . LYS   B 98  ? 1.3043 1.1785 0.3750 0.4587  0.0152  0.0858  107 LYS   B C   
1026 O O   . LYS   B 98  ? 1.2931 1.1813 0.3913 0.4366  0.0272  0.0911  107 LYS   B O   
1027 C CB  . LYS   B 98  ? 1.3625 1.2241 0.4091 0.4800  0.0530  0.1270  107 LYS   B CB  
1028 C CG  . LYS   B 98  ? 1.4498 1.3099 0.4564 0.5069  0.0606  0.1353  107 LYS   B CG  
1029 C CD  . LYS   B 98  ? 1.5100 1.3793 0.5213 0.5044  0.0953  0.1653  107 LYS   B CD  
1030 C CE  . LYS   B 98  ? 1.5257 1.4170 0.5917 0.4659  0.1066  0.1687  107 LYS   B CE  
1031 N NZ  . LYS   B 98  ? 1.5455 1.4519 0.6227 0.4607  0.1379  0.1958  107 LYS   B NZ  
1032 N N   . ASN   B 99  ? 1.3074 1.1709 0.3495 0.4773  -0.0079 0.0682  108 ASN   B N   
1033 C CA  . ASN   B 99  ? 1.3032 1.1659 0.3426 0.4727  -0.0189 0.0548  108 ASN   B CA  
1034 C C   . ASN   B 99  ? 1.3084 1.1689 0.3154 0.4946  -0.0027 0.0686  108 ASN   B C   
1035 O O   . ASN   B 99  ? 1.3276 1.1772 0.2927 0.5260  0.0015  0.0765  108 ASN   B O   
1036 C CB  . ASN   B 99  ? 1.3207 1.1685 0.3413 0.4832  -0.0514 0.0293  108 ASN   B CB  
1037 C CG  . ASN   B 99  ? 1.3345 1.1911 0.3947 0.4580  -0.0690 0.0126  108 ASN   B CG  
1038 O OD1 . ASN   B 99  ? 1.3403 1.2046 0.4162 0.4558  -0.0678 0.0154  108 ASN   B OD1 
1039 N ND2 . ASN   B 99  ? 1.3317 1.1867 0.4080 0.4397  -0.0850 -0.0047 108 ASN   B ND2 
1040 N N   . ILE   B 100 ? 1.2911 1.1632 0.3159 0.4803  0.0068  0.0720  109 ILE   B N   
1041 C CA  . ILE   B 100 ? 1.2974 1.1733 0.2970 0.5011  0.0224  0.0842  109 ILE   B CA  
1042 C C   . ILE   B 100 ? 1.2957 1.1610 0.2859 0.5018  0.0056  0.0667  109 ILE   B C   
1043 O O   . ILE   B 100 ? 1.2838 1.1573 0.3078 0.4747  0.0027  0.0616  109 ILE   B O   
1044 C CB  . ILE   B 100 ? 1.2881 1.1923 0.3217 0.4845  0.0513  0.1069  109 ILE   B CB  
1045 C CG1 . ILE   B 100 ? 1.2902 1.2009 0.3429 0.4738  0.0674  0.1234  109 ILE   B CG1 
1046 C CG2 . ILE   B 100 ? 1.3032 1.2174 0.3118 0.5101  0.0689  0.1208  109 ILE   B CG2 
1047 C CD1 . ILE   B 100 ? 1.3164 1.2147 0.3276 0.5055  0.0775  0.1371  109 ILE   B CD1 
1048 N N   . GLN   B 101 ? 1.3100 1.1542 0.2514 0.5336  -0.0048 0.0582  110 GLN   B N   
1049 C CA  . GLN   B 101 ? 1.3162 1.1418 0.2418 0.5372  -0.0218 0.0410  110 GLN   B CA  
1050 C C   . GLN   B 101 ? 1.2989 1.1399 0.2245 0.5453  -0.0016 0.0549  110 GLN   B C   
1051 O O   . GLN   B 101 ? 1.2968 1.1532 0.2066 0.5677  0.0209  0.0734  110 GLN   B O   
1052 C CB  . GLN   B 101 ? 1.3784 1.1704 0.2481 0.5695  -0.0443 0.0233  110 GLN   B CB  
1053 C CG  . GLN   B 101 ? 1.4358 1.1993 0.2864 0.5720  -0.0654 0.0028  110 GLN   B CG  
1054 C CD  . GLN   B 101 ? 1.4931 1.2219 0.3039 0.5892  -0.0965 -0.0214 110 GLN   B CD  
1055 O OE1 . GLN   B 101 ? 1.5074 1.2374 0.3284 0.5812  -0.1110 -0.0297 110 GLN   B OE1 
1056 N NE2 . GLN   B 101 ? 1.5213 1.2184 0.2861 0.6140  -0.1088 -0.0345 110 GLN   B NE2 
1057 N N   . THR   B 102 ? 1.2866 1.1260 0.2319 0.5270  -0.0084 0.0472  111 THR   B N   
1058 C CA  . THR   B 102 ? 1.2838 1.1399 0.2314 0.5355  0.0078  0.0588  111 THR   B CA  
1059 C C   . THR   B 102 ? 1.3053 1.1355 0.2436 0.5316  -0.0109 0.0421  111 THR   B C   
1060 O O   . THR   B 102 ? 1.3221 1.1276 0.2654 0.5123  -0.0329 0.0245  111 THR   B O   
1061 C CB  . THR   B 102 ? 1.2684 1.1669 0.2688 0.5092  0.0306  0.0787  111 THR   B CB  
1062 O OG1 . THR   B 102 ? 1.2750 1.2005 0.2748 0.5269  0.0519  0.0955  111 THR   B OG1 
1063 C CG2 . THR   B 102 ? 1.2497 1.1508 0.2905 0.4716  0.0206  0.0707  111 THR   B CG2 
1064 N N   . LEU   B 103 ? 1.3016 1.1371 0.2265 0.5506  -0.0018 0.0482  112 LEU   B N   
1065 C CA  . LEU   B 103 ? 1.3115 1.1197 0.2253 0.5488  -0.0173 0.0352  112 LEU   B CA  
1066 C C   . LEU   B 103 ? 1.2714 1.1152 0.2287 0.5285  -0.0026 0.0494  112 LEU   B C   
1067 O O   . LEU   B 103 ? 1.2464 1.1269 0.2132 0.5428  0.0188  0.0668  112 LEU   B O   
1068 C CB  . LEU   B 103 ? 1.3490 1.1317 0.2078 0.5918  -0.0203 0.0297  112 LEU   B CB  
1069 C CG  . LEU   B 103 ? 1.4029 1.1465 0.2448 0.5906  -0.0387 0.0150  112 LEU   B CG  
1070 C CD1 . LEU   B 103 ? 1.4496 1.1371 0.2557 0.5920  -0.0678 -0.0098 112 LEU   B CD1 
1071 C CD2 . LEU   B 103 ? 1.4167 1.1629 0.2312 0.6262  -0.0280 0.0216  112 LEU   B CD2 
1072 N N   . PRO   B 104 ? 1.2596 1.0980 0.2469 0.4938  -0.0128 0.0431  113 PRO   B N   
1073 C CA  . PRO   B 104 ? 1.2400 1.1124 0.2665 0.4748  -0.0007 0.0556  113 PRO   B CA  
1074 C C   . PRO   B 104 ? 1.2648 1.1363 0.2750 0.4958  0.0009  0.0587  113 PRO   B C   
1075 O O   . PRO   B 104 ? 1.2990 1.1331 0.2658 0.5211  -0.0104 0.0484  113 PRO   B O   
1076 C CB  . PRO   B 104 ? 1.2391 1.0992 0.2923 0.4362  -0.0131 0.0464  113 PRO   B CB  
1077 C CG  . PRO   B 104 ? 1.2608 1.0878 0.2963 0.4336  -0.0299 0.0305  113 PRO   B CG  
1078 C CD  . PRO   B 104 ? 1.2599 1.0627 0.2467 0.4712  -0.0354 0.0247  113 PRO   B CD  
1079 N N   . GLY   B 105 ? 1.2478 1.1606 0.2930 0.4859  0.0140  0.0723  114 GLY   B N   
1080 C CA  . GLY   B 105 ? 1.2526 1.1742 0.2917 0.5031  0.0157  0.0770  114 GLY   B CA  
1081 C C   . GLY   B 105 ? 1.2648 1.1729 0.3178 0.4775  0.0039  0.0721  114 GLY   B C   
1082 O O   . GLY   B 105 ? 1.2814 1.1612 0.3374 0.4512  -0.0080 0.0619  114 GLY   B O   
1083 N N   . ILE   B 106 ? 1.2510 1.1807 0.3120 0.4864  0.0072  0.0797  115 ILE   B N   
1084 C CA  . ILE   B 106 ? 1.2543 1.1702 0.3218 0.4671  -0.0034 0.0769  115 ILE   B CA  
1085 C C   . ILE   B 106 ? 1.2193 1.1914 0.3309 0.4534  0.0061  0.0892  115 ILE   B C   
1086 O O   . ILE   B 106 ? 1.2050 1.2196 0.3290 0.4740  0.0168  0.0998  115 ILE   B O   
1087 C CB  . ILE   B 106 ? 1.2939 1.1680 0.3166 0.4957  -0.0145 0.0716  115 ILE   B CB  
1088 C CG1 . ILE   B 106 ? 1.3455 1.1551 0.3231 0.5046  -0.0284 0.0561  115 ILE   B CG1 
1089 C CG2 . ILE   B 106 ? 1.3030 1.1678 0.3289 0.4831  -0.0225 0.0732  115 ILE   B CG2 
1090 C CD1 . ILE   B 106 ? 1.3727 1.1501 0.3571 0.4690  -0.0398 0.0461  115 ILE   B CD1 
1091 N N   . PHE   B 107 ? 1.2020 1.1750 0.3373 0.4191  0.0016  0.0871  116 PHE   B N   
1092 C CA  . PHE   B 107 ? 1.1689 1.1851 0.3407 0.4026  0.0050  0.0947  116 PHE   B CA  
1093 C C   . PHE   B 107 ? 1.2000 1.1860 0.3461 0.4083  -0.0078 0.0914  116 PHE   B C   
1094 O O   . PHE   B 107 ? 1.2275 1.1689 0.3559 0.3915  -0.0170 0.0834  116 PHE   B O   
1095 C CB  . PHE   B 107 ? 1.1451 1.1650 0.3450 0.3642  0.0054  0.0912  116 PHE   B CB  
1096 C CG  . PHE   B 107 ? 1.1134 1.1792 0.3543 0.3501  0.0184  0.0985  116 PHE   B CG  
1097 C CD1 . PHE   B 107 ? 1.1116 1.2056 0.3601 0.3690  0.0315  0.1077  116 PHE   B CD1 
1098 C CD2 . PHE   B 107 ? 1.1018 1.1776 0.3705 0.3180  0.0185  0.0963  116 PHE   B CD2 
1099 C CE1 . PHE   B 107 ? 1.0903 1.2205 0.3754 0.3538  0.0446  0.1159  116 PHE   B CE1 
1100 C CE2 . PHE   B 107 ? 1.0867 1.1968 0.3906 0.3042  0.0298  0.1025  116 PHE   B CE2 
1101 C CZ  . PHE   B 107 ? 1.0742 1.2102 0.3868 0.3209  0.0430  0.1129  116 PHE   B CZ  
1102 N N   . LYS   B 108 ? 1.1950 1.2033 0.3375 0.4330  -0.0082 0.0982  117 LYS   B N   
1103 C CA  . LYS   B 108 ? 1.2241 1.2003 0.3374 0.4421  -0.0206 0.0967  117 LYS   B CA  
1104 C C   . LYS   B 108 ? 1.1928 1.2029 0.3339 0.4232  -0.0236 0.1011  117 LYS   B C   
1105 O O   . LYS   B 108 ? 1.1531 1.2231 0.3306 0.4252  -0.0179 0.1080  117 LYS   B O   
1106 C CB  . LYS   B 108 ? 1.2867 1.2588 0.3710 0.4859  -0.0218 0.1000  117 LYS   B CB  
1107 C CG  . LYS   B 108 ? 1.4028 1.3352 0.4517 0.4985  -0.0347 0.0994  117 LYS   B CG  
1108 C CD  . LYS   B 108 ? 1.4978 1.4319 0.5203 0.5453  -0.0358 0.1033  117 LYS   B CD  
1109 C CE  . LYS   B 108 ? 1.5709 1.4936 0.5750 0.5578  -0.0467 0.1075  117 LYS   B CE  
1110 N NZ  . LYS   B 108 ? 1.6224 1.5446 0.5987 0.6070  -0.0481 0.1108  117 LYS   B NZ  
1111 N N   . THR   B 109 ? 1.2085 1.1813 0.3338 0.4028  -0.0322 0.0970  118 THR   B N   
1112 C CA  . THR   B 109 ? 1.1970 1.1934 0.3401 0.3845  -0.0366 0.0994  118 THR   B CA  
1113 C C   . THR   B 109 ? 1.2173 1.1739 0.3202 0.3961  -0.0478 0.1013  118 THR   B C   
1114 O O   . THR   B 109 ? 1.2459 1.1505 0.3084 0.4136  -0.0519 0.1002  118 THR   B O   
1115 C CB  . THR   B 109 ? 1.2131 1.2100 0.3795 0.3454  -0.0327 0.0939  118 THR   B CB  
1116 O OG1 . THR   B 109 ? 1.2647 1.2040 0.4016 0.3320  -0.0362 0.0887  118 THR   B OG1 
1117 C CG2 . THR   B 109 ? 1.1996 1.2212 0.3963 0.3358  -0.0220 0.0925  118 THR   B CG2 
1118 N N   . LYS   B 110 ? 1.1998 1.1777 0.3111 0.3868  -0.0535 0.1040  119 LYS   B N   
1119 C CA  . LYS   B 110 ? 1.2250 1.1666 0.2966 0.3977  -0.0635 0.1077  119 LYS   B CA  
1120 C C   . LYS   B 110 ? 1.2635 1.1369 0.3018 0.3774  -0.0630 0.1051  119 LYS   B C   
1121 O O   . LYS   B 110 ? 1.3025 1.1302 0.2994 0.3881  -0.0691 0.1097  119 LYS   B O   
1122 C CB  . LYS   B 110 ? 1.2162 1.2026 0.3055 0.3936  -0.0706 0.1104  119 LYS   B CB  
1123 C CG  . LYS   B 110 ? 1.2479 1.2372 0.3521 0.3568  -0.0686 0.1056  119 LYS   B CG  
1124 C CD  . LYS   B 110 ? 1.2682 1.3169 0.4044 0.3507  -0.0755 0.1046  119 LYS   B CD  
1125 C CE  . LYS   B 110 ? 1.3237 1.3556 0.4418 0.3323  -0.0808 0.1022  119 LYS   B CE  
1126 N NZ  . LYS   B 110 ? 1.3519 1.3620 0.4767 0.2997  -0.0704 0.0960  119 LYS   B NZ  
1127 N N   . ASP   B 111 ? 1.2498 1.1171 0.3069 0.3487  -0.0554 0.0987  120 ASP   B N   
1128 C CA  . ASP   B 111 ? 1.2703 1.0830 0.3061 0.3266  -0.0535 0.0960  120 ASP   B CA  
1129 C C   . ASP   B 111 ? 1.2840 1.0602 0.3114 0.3267  -0.0520 0.0896  120 ASP   B C   
1130 O O   . ASP   B 111 ? 1.3122 1.0495 0.3307 0.3052  -0.0505 0.0862  120 ASP   B O   
1131 C CB  . ASP   B 111 ? 1.2696 1.1024 0.3321 0.2928  -0.0471 0.0925  120 ASP   B CB  
1132 C CG  . ASP   B 111 ? 1.2896 1.1594 0.3618 0.2898  -0.0500 0.0954  120 ASP   B CG  
1133 O OD1 . ASP   B 111 ? 1.2969 1.1436 0.3366 0.2971  -0.0553 0.1015  120 ASP   B OD1 
1134 O OD2 . ASP   B 111 ? 1.2862 1.2050 0.3963 0.2797  -0.0477 0.0914  120 ASP   B OD2 
1135 N N   . GLY   B 112 ? 1.2574 1.0478 0.2882 0.3502  -0.0524 0.0877  121 GLY   B N   
1136 C CA  . GLY   B 112 ? 1.2592 1.0141 0.2768 0.3541  -0.0536 0.0801  121 GLY   B CA  
1137 C C   . GLY   B 112 ? 1.2189 1.0126 0.2629 0.3613  -0.0478 0.0764  121 GLY   B C   
1138 O O   . GLY   B 112 ? 1.1846 1.0338 0.2643 0.3558  -0.0409 0.0800  121 GLY   B O   
1139 N N   . ASP   B 113 ? 1.2234 0.9854 0.2479 0.3738  -0.0510 0.0691  122 ASP   B N   
1140 C CA  . ASP   B 113 ? 1.2064 0.9971 0.2469 0.3840  -0.0452 0.0660  122 ASP   B CA  
1141 C C   . ASP   B 113 ? 1.1923 0.9894 0.2587 0.3546  -0.0421 0.0595  122 ASP   B C   
1142 O O   . ASP   B 113 ? 1.2020 0.9662 0.2646 0.3313  -0.0473 0.0535  122 ASP   B O   
1143 C CB  . ASP   B 113 ? 1.2508 1.0041 0.2525 0.4156  -0.0512 0.0600  122 ASP   B CB  
1144 C CG  . ASP   B 113 ? 1.3183 1.0718 0.2947 0.4531  -0.0524 0.0663  122 ASP   B CG  
1145 O OD1 . ASP   B 113 ? 1.3124 1.0932 0.3006 0.4540  -0.0505 0.0754  122 ASP   B OD1 
1146 O OD2 . ASP   B 113 ? 1.3671 1.0931 0.3100 0.4835  -0.0560 0.0612  122 ASP   B OD2 
1147 N N   . ILE   B 114 ? 1.1625 1.0019 0.2552 0.3569  -0.0330 0.0614  123 ILE   B N   
1148 C CA  . ILE   B 114 ? 1.1535 1.0034 0.2713 0.3334  -0.0294 0.0565  123 ILE   B CA  
1149 C C   . ILE   B 114 ? 1.1451 1.0112 0.2631 0.3525  -0.0238 0.0566  123 ILE   B C   
1150 O O   . ILE   B 114 ? 1.1275 1.0233 0.2476 0.3745  -0.0157 0.0653  123 ILE   B O   
1151 C CB  . ILE   B 114 ? 1.1309 1.0211 0.2869 0.3083  -0.0214 0.0620  123 ILE   B CB  
1152 C CG1 . ILE   B 114 ? 1.1551 1.0250 0.3069 0.2876  -0.0262 0.0607  123 ILE   B CG1 
1153 C CG2 . ILE   B 114 ? 1.1236 1.0326 0.3070 0.2913  -0.0150 0.0592  123 ILE   B CG2 
1154 C CD1 . ILE   B 114 ? 1.1487 1.0562 0.3265 0.2728  -0.0209 0.0664  123 ILE   B CD1 
1155 N N   . GLY   B 115 ? 1.1563 1.0045 0.2716 0.3456  -0.0279 0.0477  124 GLY   B N   
1156 C CA  . GLY   B 115 ? 1.1651 1.0249 0.2751 0.3649  -0.0229 0.0482  124 GLY   B CA  
1157 C C   . GLY   B 115 ? 1.1447 1.0550 0.2891 0.3596  -0.0065 0.0602  124 GLY   B C   
1158 O O   . GLY   B 115 ? 1.1216 1.0523 0.2972 0.3338  -0.0024 0.0630  124 GLY   B O   
1159 N N   . ALA   B 116 ? 1.1517 1.0807 0.2897 0.3836  0.0035  0.0675  125 ALA   B N   
1160 C CA  . ALA   B 116 ? 1.1373 1.1122 0.3087 0.3776  0.0207  0.0808  125 ALA   B CA  
1161 C C   . ALA   B 116 ? 1.1466 1.1259 0.3068 0.3957  0.0301  0.0856  125 ALA   B C   
1162 O O   . ALA   B 116 ? 1.1678 1.1400 0.2976 0.4268  0.0322  0.0871  125 ALA   B O   
1163 C CB  . ALA   B 116 ? 1.1233 1.1362 0.3114 0.3858  0.0299  0.0928  125 ALA   B CB  
1164 N N   . VAL   B 117 ? 1.1376 1.1266 0.3190 0.3785  0.0363  0.0885  126 VAL   B N   
1165 C CA  A VAL   B 117 ? 1.1496 1.1404 0.3180 0.3956  0.0460  0.0949  126 VAL   B CA  
1166 C CA  B VAL   B 117 ? 1.1521 1.1428 0.3209 0.3950  0.0458  0.0948  126 VAL   B CA  
1167 C C   . VAL   B 117 ? 1.1351 1.1689 0.3301 0.3965  0.0688  0.1151  126 VAL   B C   
1168 O O   . VAL   B 117 ? 1.1101 1.1669 0.3438 0.3700  0.0754  0.1210  126 VAL   B O   
1169 C CB  A VAL   B 117 ? 1.1629 1.1315 0.3289 0.3838  0.0376  0.0858  126 VAL   B CB  
1170 C CB  B VAL   B 117 ? 1.1683 1.1382 0.3390 0.3795  0.0372  0.0854  126 VAL   B CB  
1171 C CG1 A VAL   B 117 ? 1.1935 1.1220 0.3294 0.3897  0.0156  0.0667  126 VAL   B CG1 
1172 C CG1 B VAL   B 117 ? 1.1783 1.1550 0.3437 0.3914  0.0498  0.0958  126 VAL   B CG1 
1173 C CG2 A VAL   B 117 ? 1.1503 1.1316 0.3559 0.3494  0.0393  0.0859  126 VAL   B CG2 
1174 C CG2 B VAL   B 117 ? 1.1986 1.1285 0.3390 0.3857  0.0155  0.0666  126 VAL   B CG2 
1175 N N   . ALA   B 118 ? 1.1424 1.1872 0.3163 0.4276  0.0811  0.1253  127 ALA   B N   
1176 C CA  . ALA   B 118 ? 1.1352 1.2236 0.3336 0.4317  0.1054  0.1465  127 ALA   B CA  
1177 C C   . ALA   B 118 ? 1.1499 1.2370 0.3449 0.4338  0.1201  0.1581  127 ALA   B C   
1178 O O   . ALA   B 118 ? 1.1541 1.2497 0.3279 0.4609  0.1358  0.1705  127 ALA   B O   
1179 C CB  . ALA   B 118 ? 1.1364 1.2425 0.3159 0.4656  0.1138  0.1532  127 ALA   B CB  
1180 N N   . LEU   B 119 ? 1.1544 1.2301 0.3680 0.4069  0.1161  0.1549  128 LEU   B N   
1181 C CA  . LEU   B 119 ? 1.1682 1.2382 0.3778 0.4082  0.1293  0.1666  128 LEU   B CA  
1182 C C   . LEU   B 119 ? 1.1444 1.2369 0.4026 0.3747  0.1410  0.1775  128 LEU   B C   
1183 O O   . LEU   B 119 ? 1.1309 1.2225 0.4142 0.3481  0.1288  0.1663  128 LEU   B O   
1184 C CB  . LEU   B 119 ? 1.2016 1.2304 0.3820 0.4120  0.1114  0.1510  128 LEU   B CB  
1185 C CG  . LEU   B 119 ? 1.2495 1.2503 0.3817 0.4417  0.0951  0.1363  128 LEU   B CG  
1186 C CD1 . LEU   B 119 ? 1.2730 1.2400 0.3888 0.4381  0.0740  0.1187  128 LEU   B CD1 
1187 C CD2 . LEU   B 119 ? 1.2733 1.2774 0.3693 0.4785  0.1102  0.1492  128 LEU   B CD2 
1188 N N   . ASP   B 120 ? 1.1309 1.2422 0.4017 0.3755  0.1649  0.1994  129 ASP   B N   
1189 C CA  . ASP   B 120 ? 1.1126 1.2409 0.4299 0.3415  0.1748  0.2089  129 ASP   B CA  
1190 C C   . ASP   B 120 ? 1.1127 1.2096 0.4242 0.3312  0.1765  0.2109  129 ASP   B C   
1191 O O   . ASP   B 120 ? 1.1392 1.2210 0.4225 0.3513  0.1880  0.2226  129 ASP   B O   
1192 C CB  . ASP   B 120 ? 1.1157 1.2886 0.4644 0.3389  0.1995  0.2318  129 ASP   B CB  
1193 C CG  . ASP   B 120 ? 1.1590 1.3599 0.5637 0.3012  0.2000  0.2334  129 ASP   B CG  
1194 O OD1 . ASP   B 120 ? 1.1765 1.3563 0.5918 0.2771  0.1846  0.2189  129 ASP   B OD1 
1195 O OD2 . ASP   B 120 ? 1.1592 1.4045 0.5973 0.2966  0.2152  0.2482  129 ASP   B OD2 
1196 N N   . TYR   B 121 ? 1.0892 1.1752 0.4245 0.3025  0.1651  0.1994  130 TYR   B N   
1197 C CA  . TYR   B 121 ? 1.0857 1.1411 0.4180 0.2922  0.1650  0.1991  130 TYR   B CA  
1198 C C   . TYR   B 121 ? 1.0423 1.1044 0.4176 0.2556  0.1666  0.1987  130 TYR   B C   
1199 O O   . TYR   B 121 ? 1.0260 1.1126 0.4282 0.2392  0.1602  0.1918  130 TYR   B O   
1200 C CB  . TYR   B 121 ? 1.1090 1.1341 0.4142 0.3013  0.1426  0.1776  130 TYR   B CB  
1201 C CG  . TYR   B 121 ? 1.1423 1.1489 0.4017 0.3357  0.1406  0.1786  130 TYR   B CG  
1202 C CD1 . TYR   B 121 ? 1.1755 1.1587 0.4138 0.3479  0.1471  0.1875  130 TYR   B CD1 
1203 C CD2 . TYR   B 121 ? 1.1648 1.1749 0.3990 0.3579  0.1315  0.1707  130 TYR   B CD2 
1204 C CE1 . TYR   B 121 ? 1.2109 1.1776 0.4035 0.3818  0.1443  0.1884  130 TYR   B CE1 
1205 C CE2 . TYR   B 121 ? 1.1995 1.1911 0.3884 0.3908  0.1284  0.1703  130 TYR   B CE2 
1206 C CZ  . TYR   B 121 ? 1.2320 1.2033 0.4000 0.4028  0.1343  0.1789  130 TYR   B CZ  
1207 O OH  . TYR   B 121 ? 1.2848 1.2374 0.4045 0.4371  0.1291  0.1773  130 TYR   B OH  
1208 N N   . PRO   B 122 ? 1.0234 1.0613 0.4032 0.2435  0.1732  0.2046  131 PRO   B N   
1209 C CA  . PRO   B 122 ? 0.9864 1.0256 0.4037 0.2092  0.1726  0.2015  131 PRO   B CA  
1210 C C   . PRO   B 122 ? 0.9546 0.9950 0.3823 0.1943  0.1511  0.1773  131 PRO   B C   
1211 O O   . PRO   B 122 ? 0.9623 0.9939 0.3673 0.2088  0.1368  0.1628  131 PRO   B O   
1212 C CB  . PRO   B 122 ? 1.0149 1.0154 0.4210 0.2072  0.1796  0.2081  131 PRO   B CB  
1213 C CG  . PRO   B 122 ? 1.0454 1.0371 0.4173 0.2377  0.1937  0.2260  131 PRO   B CG  
1214 C CD  . PRO   B 122 ? 1.0383 1.0445 0.3867 0.2622  0.1815  0.2148  131 PRO   B CD  
1215 N N   . ALA   B 123 ? 0.9151 0.9655 0.3762 0.1652  0.1487  0.1728  132 ALA   B N   
1216 C CA  . ALA   B 123 ? 0.8944 0.9454 0.3624 0.1517  0.1302  0.1513  132 ALA   B CA  
1217 C C   . ALA   B 123 ? 0.8955 0.9118 0.3423 0.1559  0.1199  0.1362  132 ALA   B C   
1218 O O   . ALA   B 123 ? 0.8970 0.9134 0.3359 0.1574  0.1059  0.1201  132 ALA   B O   
1219 C CB  . ALA   B 123 ? 0.8786 0.9432 0.3822 0.1214  0.1290  0.1492  132 ALA   B CB  
1220 N N   . GLY   B 124 ? 0.8939 0.8820 0.3309 0.1601  0.1277  0.1428  133 GLY   B N   
1221 C CA  . GLY   B 124 ? 0.9005 0.8594 0.3192 0.1680  0.1192  0.1302  133 GLY   B CA  
1222 C C   . GLY   B 124 ? 0.9007 0.8586 0.2930 0.1931  0.1099  0.1234  133 GLY   B C   
1223 O O   . GLY   B 124 ? 0.9027 0.8444 0.2847 0.1995  0.1008  0.1112  133 GLY   B O   
1224 N N   . THR   B 125 ? 0.8927 0.8683 0.2744 0.2081  0.1117  0.1306  134 THR   B N   
1225 C CA  . THR   B 125 ? 0.9086 0.8811 0.2642 0.2308  0.1004  0.1222  134 THR   B CA  
1226 C C   . THR   B 125 ? 0.8964 0.8788 0.2580 0.2216  0.0849  0.1042  134 THR   B C   
1227 O O   . THR   B 125 ? 0.9097 0.8863 0.2539 0.2347  0.0731  0.0942  134 THR   B O   
1228 C CB  . THR   B 125 ? 0.9350 0.9154 0.2698 0.2544  0.1093  0.1372  134 THR   B CB  
1229 O OG1 . THR   B 125 ? 0.9570 0.9285 0.2885 0.2590  0.1269  0.1564  134 THR   B OG1 
1230 C CG2 . THR   B 125 ? 0.9543 0.9231 0.2557 0.2808  0.0968  0.1284  134 THR   B CG2 
1231 N N   . SER   B 126 ? 0.8758 0.8711 0.2606 0.1989  0.0843  0.1001  135 SER   B N   
1232 C CA  . SER   B 126 ? 0.8720 0.8752 0.2608 0.1891  0.0724  0.0862  135 SER   B CA  
1233 C C   . SER   B 126 ? 0.8787 0.8673 0.2611 0.1885  0.0618  0.0706  135 SER   B C   
1234 O O   . SER   B 126 ? 0.8786 0.8567 0.2683 0.1813  0.0633  0.0662  135 SER   B O   
1235 C CB  . SER   B 126 ? 0.8655 0.8808 0.2777 0.1656  0.0738  0.0845  135 SER   B CB  
1236 O OG  . SER   B 126 ? 0.8762 0.9109 0.3031 0.1621  0.0834  0.0985  135 SER   B OG  
1237 N N   . GLY   B 127 ? 0.8760 0.8644 0.2466 0.1949  0.0514  0.0624  136 GLY   B N   
1238 C CA  . GLY   B 127 ? 0.8766 0.8561 0.2453 0.1933  0.0416  0.0485  136 GLY   B CA  
1239 C C   . GLY   B 127 ? 0.8899 0.8602 0.2411 0.2134  0.0338  0.0458  136 GLY   B C   
1240 O O   . GLY   B 127 ? 0.8942 0.8609 0.2463 0.2127  0.0237  0.0340  136 GLY   B O   
1241 N N   . SER   B 128 ? 0.8973 0.8650 0.2324 0.2319  0.0382  0.0567  137 SER   B N   
1242 C CA  . SER   B 128 ? 0.9152 0.8725 0.2274 0.2543  0.0294  0.0539  137 SER   B CA  
1243 C C   . SER   B 128 ? 0.9231 0.8765 0.2246 0.2560  0.0156  0.0431  137 SER   B C   
1244 O O   . SER   B 128 ? 0.9177 0.8752 0.2175 0.2514  0.0174  0.0459  137 SER   B O   
1245 C CB  . SER   B 128 ? 0.9373 0.8932 0.2303 0.2743  0.0398  0.0696  137 SER   B CB  
1246 O OG  . SER   B 128 ? 0.9615 0.9135 0.2593 0.2753  0.0518  0.0803  137 SER   B OG  
1247 N N   . PRO   B 129 ? 0.9274 0.8726 0.2237 0.2610  0.0008  0.0302  138 PRO   B N   
1248 C CA  . PRO   B 129 ? 0.9361 0.8722 0.2225 0.2600  -0.0134 0.0194  138 PRO   B CA  
1249 C C   . PRO   B 129 ? 0.9635 0.8865 0.2164 0.2840  -0.0185 0.0217  138 PRO   B C   
1250 O O   . PRO   B 129 ? 0.9731 0.8924 0.2067 0.3058  -0.0170 0.0268  138 PRO   B O   
1251 C CB  . PRO   B 129 ? 0.9448 0.8802 0.2419 0.2564  -0.0276 0.0048  138 PRO   B CB  
1252 C CG  . PRO   B 129 ? 0.9455 0.8835 0.2391 0.2725  -0.0250 0.0089  138 PRO   B CG  
1253 C CD  . PRO   B 129 ? 0.9214 0.8652 0.2213 0.2683  -0.0049 0.0246  138 PRO   B CD  
1254 N N   . ILE   B 130 ? 0.9732 0.8861 0.2156 0.2817  -0.0246 0.0176  139 ILE   B N   
1255 C CA  . ILE   B 130 ? 1.0045 0.9001 0.2124 0.3046  -0.0319 0.0162  139 ILE   B CA  
1256 C C   . ILE   B 130 ? 1.0417 0.9160 0.2419 0.3011  -0.0539 -0.0022 139 ILE   B C   
1257 O O   . ILE   B 130 ? 1.0381 0.9114 0.2591 0.2774  -0.0587 -0.0091 139 ILE   B O   
1258 C CB  . ILE   B 130 ? 1.0104 0.9080 0.2123 0.3053  -0.0234 0.0248  139 ILE   B CB  
1259 C CG1 . ILE   B 130 ? 1.0080 0.9321 0.2266 0.3035  -0.0030 0.0419  139 ILE   B CG1 
1260 C CG2 . ILE   B 130 ? 1.0298 0.9069 0.1934 0.3316  -0.0308 0.0221  139 ILE   B CG2 
1261 C CD1 . ILE   B 130 ? 1.0107 0.9449 0.2372 0.2955  0.0029  0.0478  139 ILE   B CD1 
1262 N N   . LEU   B 131 ? 1.0722 0.9300 0.2430 0.3242  -0.0674 -0.0101 140 LEU   B N   
1263 C CA  . LEU   B 131 ? 1.0995 0.9386 0.2648 0.3215  -0.0914 -0.0294 140 LEU   B CA  
1264 C C   . LEU   B 131 ? 1.1462 0.9519 0.2741 0.3369  -0.1070 -0.0396 140 LEU   B C   
1265 O O   . LEU   B 131 ? 1.1688 0.9646 0.2615 0.3644  -0.1023 -0.0337 140 LEU   B O   
1266 C CB  . LEU   B 131 ? 1.0999 0.9455 0.2610 0.3367  -0.1006 -0.0350 140 LEU   B CB  
1267 C CG  . LEU   B 131 ? 1.0900 0.9618 0.2776 0.3312  -0.0871 -0.0255 140 LEU   B CG  
1268 C CD1 . LEU   B 131 ? 1.0857 0.9582 0.2625 0.3501  -0.1007 -0.0330 140 LEU   B CD1 
1269 C CD2 . LEU   B 131 ? 1.0741 0.9628 0.3054 0.2987  -0.0829 -0.0280 140 LEU   B CD2 
1270 N N   . ASP   B 132 ? 1.1631 0.9503 0.2972 0.3211  -0.1269 -0.0562 141 ASP   B N   
1271 C CA  . ASP   B 132 ? 1.2115 0.9599 0.3082 0.3351  -0.1466 -0.0700 141 ASP   B CA  
1272 C C   . ASP   B 132 ? 1.2476 0.9893 0.3284 0.3516  -0.1691 -0.0862 141 ASP   B C   
1273 O O   . ASP   B 132 ? 1.2331 1.0019 0.3363 0.3494  -0.1686 -0.0856 141 ASP   B O   
1274 C CB  . ASP   B 132 ? 1.2319 0.9563 0.3396 0.3083  -0.1556 -0.0779 141 ASP   B CB  
1275 C CG  . ASP   B 132 ? 1.2641 1.0023 0.4165 0.2742  -0.1633 -0.0863 141 ASP   B CG  
1276 O OD1 . ASP   B 132 ? 1.2634 1.0212 0.4328 0.2745  -0.1731 -0.0947 141 ASP   B OD1 
1277 O OD2 . ASP   B 132 ? 1.2967 1.0263 0.4661 0.2486  -0.1593 -0.0842 141 ASP   B OD2 
1278 N N   . LYS   B 133 ? 1.2931 0.9976 0.3335 0.3695  -0.1900 -0.1014 142 LYS   B N   
1279 C CA  . LYS   B 133 ? 1.3333 1.0286 0.3521 0.3882  -0.2146 -0.1187 142 LYS   B CA  
1280 C C   . LYS   B 133 ? 1.3274 1.0416 0.3897 0.3626  -0.2332 -0.1332 142 LYS   B C   
1281 O O   . LYS   B 133 ? 1.3340 1.0543 0.3873 0.3784  -0.2512 -0.1447 142 LYS   B O   
1282 C CB  . LYS   B 133 ? 1.4105 1.0572 0.3769 0.4096  -0.2357 -0.1351 142 LYS   B CB  
1283 C CG  . LYS   B 133 ? 1.5131 1.1481 0.4270 0.4501  -0.2210 -0.1238 142 LYS   B CG  
1284 C CD  . LYS   B 133 ? 1.6063 1.2067 0.4939 0.4548  -0.2170 -0.1226 142 LYS   B CD  
1285 C CE  . LYS   B 133 ? 1.6887 1.2608 0.5107 0.5006  -0.2199 -0.1262 142 LYS   B CE  
1286 N NZ  . LYS   B 133 ? 1.7412 1.2823 0.5369 0.5100  -0.2139 -0.1237 142 LYS   B NZ  
1287 N N   . CYS   B 134 ? 1.3132 1.0392 0.4218 0.3251  -0.2282 -0.1319 143 CYS   B N   
1288 C CA  . CYS   B 134 ? 1.2964 1.0485 0.4549 0.2980  -0.2407 -0.1428 143 CYS   B CA  
1289 C C   . CYS   B 134 ? 1.2523 1.0511 0.4478 0.2932  -0.2219 -0.1298 143 CYS   B C   
1290 O O   . CYS   B 134 ? 1.2355 1.0619 0.4739 0.2743  -0.2297 -0.1376 143 CYS   B O   
1291 C CB  . CYS   B 134 ? 1.3210 1.0607 0.5088 0.2605  -0.2434 -0.1475 143 CYS   B CB  
1292 S SG  . CYS   B 134 ? 1.4527 1.1359 0.6090 0.2584  -0.2757 -0.1704 143 CYS   B SG  
1293 N N   . GLY   B 135 ? 1.2327 1.0403 0.4142 0.3086  -0.1970 -0.1103 144 GLY   B N   
1294 C CA  . GLY   B 135 ? 1.1928 1.0367 0.4052 0.3036  -0.1779 -0.0974 144 GLY   B CA  
1295 C C   . GLY   B 135 ? 1.1488 1.0093 0.4017 0.2708  -0.1602 -0.0892 144 GLY   B C   
1296 O O   . GLY   B 135 ? 1.1342 1.0239 0.4175 0.2625  -0.1474 -0.0825 144 GLY   B O   
1297 N N   . ARG   B 136 ? 1.1331 0.9725 0.3834 0.2537  -0.1592 -0.0895 145 ARG   B N   
1298 C CA  . ARG   B 136 ? 1.0982 0.9497 0.3800 0.2245  -0.1423 -0.0811 145 ARG   B CA  
1299 C C   . ARG   B 136 ? 1.0680 0.9232 0.3381 0.2311  -0.1181 -0.0623 145 ARG   B C   
1300 O O   . ARG   B 136 ? 1.0812 0.9184 0.3161 0.2520  -0.1157 -0.0565 145 ARG   B O   
1301 C CB  . ARG   B 136 ? 1.1314 0.9561 0.4140 0.2029  -0.1517 -0.0883 145 ARG   B CB  
1302 C CG  . ARG   B 136 ? 1.1637 0.9953 0.4772 0.1833  -0.1715 -0.1052 145 ARG   B CG  
1303 C CD  . ARG   B 136 ? 1.2230 1.0190 0.5314 0.1628  -0.1814 -0.1114 145 ARG   B CD  
1304 N NE  . ARG   B 136 ? 1.2945 1.0474 0.5554 0.1846  -0.1997 -0.1206 145 ARG   B NE  
1305 C CZ  . ARG   B 136 ? 1.3489 1.0577 0.5807 0.1822  -0.2017 -0.1196 145 ARG   B CZ  
1306 N NH1 . ARG   B 136 ? 1.3361 1.0378 0.5805 0.1586  -0.1865 -0.1085 145 ARG   B NH1 
1307 N NH2 . ARG   B 136 ? 1.3840 1.0533 0.5700 0.2059  -0.2190 -0.1298 145 ARG   B NH2 
1308 N N   . VAL   B 137 ? 1.0243 0.9039 0.3241 0.2139  -0.1006 -0.0536 146 VAL   B N   
1309 C CA  . VAL   B 137 ? 1.0060 0.8921 0.2996 0.2173  -0.0799 -0.0376 146 VAL   B CA  
1310 C C   . VAL   B 137 ? 0.9998 0.8668 0.2798 0.2087  -0.0752 -0.0321 146 VAL   B C   
1311 O O   . VAL   B 137 ? 1.0080 0.8744 0.3050 0.1854  -0.0722 -0.0328 146 VAL   B O   
1312 C CB  . VAL   B 137 ? 0.9910 0.9060 0.3162 0.2046  -0.0649 -0.0321 146 VAL   B CB  
1313 C CG1 . VAL   B 137 ? 0.9978 0.9187 0.3161 0.2092  -0.0466 -0.0171 146 VAL   B CG1 
1314 C CG2 . VAL   B 137 ? 0.9806 0.9118 0.3183 0.2149  -0.0712 -0.0383 146 VAL   B CG2 
1315 N N   . ILE   B 138 ? 0.9894 0.8411 0.2374 0.2293  -0.0739 -0.0259 147 ILE   B N   
1316 C CA  . ILE   B 138 ? 0.9848 0.8178 0.2151 0.2280  -0.0705 -0.0201 147 ILE   B CA  
1317 C C   . ILE   B 138 ? 0.9772 0.8309 0.2160 0.2248  -0.0517 -0.0052 147 ILE   B C   
1318 O O   . ILE   B 138 ? 0.9968 0.8398 0.2236 0.2237  -0.0487 0.0004  147 ILE   B O   
1319 C CB  . ILE   B 138 ? 0.9939 0.7976 0.1834 0.2543  -0.0813 -0.0235 147 ILE   B CB  
1320 C CG1 . ILE   B 138 ? 1.0019 0.8190 0.1755 0.2824  -0.0751 -0.0170 147 ILE   B CG1 
1321 C CG2 . ILE   B 138 ? 0.9949 0.7698 0.1748 0.2510  -0.1031 -0.0404 147 ILE   B CG2 
1322 C CD1 . ILE   B 138 ? 1.0373 0.8306 0.1693 0.3111  -0.0800 -0.0173 147 ILE   B CD1 
1323 N N   . GLY   B 139 ? 0.9457 0.8270 0.2049 0.2228  -0.0407 0.0002  148 GLY   B N   
1324 C CA  . GLY   B 139 ? 0.9254 0.8268 0.1959 0.2174  -0.0253 0.0120  148 GLY   B CA  
1325 C C   . GLY   B 139 ? 0.9040 0.8274 0.1885 0.2220  -0.0150 0.0182  148 GLY   B C   
1326 O O   . GLY   B 139 ? 0.9042 0.8269 0.1863 0.2329  -0.0188 0.0150  148 GLY   B O   
1327 N N   . LEU   B 140 ? 0.8906 0.8315 0.1887 0.2138  -0.0028 0.0272  149 LEU   B N   
1328 C CA  . LEU   B 140 ? 0.8845 0.8419 0.1962 0.2154  0.0080  0.0344  149 LEU   B CA  
1329 C C   . LEU   B 140 ? 0.8896 0.8602 0.1978 0.2253  0.0175  0.0475  149 LEU   B C   
1330 O O   . LEU   B 140 ? 0.8922 0.8673 0.1972 0.2240  0.0174  0.0506  149 LEU   B O   
1331 C CB  . LEU   B 140 ? 0.8679 0.8354 0.2038 0.1943  0.0139  0.0318  149 LEU   B CB  
1332 C CG  . LEU   B 140 ? 0.8783 0.8412 0.2245 0.1828  0.0080  0.0200  149 LEU   B CG  
1333 C CD1 . LEU   B 140 ? 0.8797 0.8531 0.2458 0.1670  0.0166  0.0185  149 LEU   B CD1 
1334 C CD2 . LEU   B 140 ? 0.8874 0.8450 0.2304 0.1956  0.0002  0.0142  149 LEU   B CD2 
1335 N N   . TYR   B 141 ? 0.8861 0.8643 0.1961 0.2354  0.0263  0.0562  150 TYR   B N   
1336 C CA  . TYR   B 141 ? 0.8954 0.8906 0.2069 0.2447  0.0383  0.0707  150 TYR   B CA  
1337 C C   . TYR   B 141 ? 0.8771 0.8899 0.2172 0.2251  0.0485  0.0770  150 TYR   B C   
1338 O O   . TYR   B 141 ? 0.8723 0.8790 0.2236 0.2137  0.0498  0.0733  150 TYR   B O   
1339 C CB  . TYR   B 141 ? 0.9153 0.9047 0.2095 0.2669  0.0434  0.0777  150 TYR   B CB  
1340 C CG  . TYR   B 141 ? 0.9313 0.9398 0.2307 0.2753  0.0606  0.0957  150 TYR   B CG  
1341 C CD1 . TYR   B 141 ? 0.9414 0.9553 0.2584 0.2656  0.0729  0.1054  150 TYR   B CD1 
1342 C CD2 . TYR   B 141 ? 0.9473 0.9663 0.2323 0.2948  0.0652  0.1036  150 TYR   B CD2 
1343 C CE1 . TYR   B 141 ? 0.9452 0.9768 0.2700 0.2706  0.0903  0.1235  150 TYR   B CE1 
1344 C CE2 . TYR   B 141 ? 0.9577 0.9988 0.2505 0.3028  0.0833  0.1215  150 TYR   B CE2 
1345 C CZ  . TYR   B 141 ? 0.9548 1.0024 0.2685 0.2894  0.0962  0.1321  150 TYR   B CZ  
1346 O OH  . TYR   B 141 ? 0.9376 1.0076 0.2625 0.2940  0.1157  0.1515  150 TYR   B OH  
1347 N N   . GLY   B 142 ? 0.8646 0.8995 0.2162 0.2234  0.0554  0.0866  151 GLY   B N   
1348 C CA  . GLY   B 142 ? 0.8564 0.9086 0.2366 0.2038  0.0633  0.0919  151 GLY   B CA  
1349 C C   . GLY   B 142 ? 0.8444 0.9165 0.2395 0.1912  0.0592  0.0904  151 GLY   B C   
1350 O O   . GLY   B 142 ? 0.8377 0.9231 0.2568 0.1729  0.0624  0.0918  151 GLY   B O   
1351 N N   . ASN   B 143 ? 0.8442 0.9164 0.2238 0.2013  0.0509  0.0870  152 ASN   B N   
1352 C CA  . ASN   B 143 ? 0.8442 0.9361 0.2343 0.1935  0.0460  0.0865  152 ASN   B CA  
1353 C C   . ASN   B 143 ? 0.8705 0.9769 0.2500 0.2155  0.0457  0.0938  152 ASN   B C   
1354 O O   . ASN   B 143 ? 0.8874 0.9730 0.2393 0.2302  0.0385  0.0893  152 ASN   B O   
1355 C CB  . ASN   B 143 ? 0.8437 0.9175 0.2238 0.1811  0.0352  0.0741  152 ASN   B CB  
1356 C CG  . ASN   B 143 ? 0.8445 0.9369 0.2335 0.1719  0.0293  0.0731  152 ASN   B CG  
1357 O OD1 . ASN   B 143 ? 0.8260 0.9488 0.2372 0.1693  0.0319  0.0797  152 ASN   B OD1 
1358 N ND2 . ASN   B 143 ? 0.8412 0.9167 0.2134 0.1669  0.0210  0.0651  152 ASN   B ND2 
1359 N N   . GLY   B 144 ? 0.8712 1.0132 0.2738 0.2174  0.0533  0.1046  153 GLY   B N   
1360 C CA  . GLY   B 144 ? 0.8960 1.0580 0.2915 0.2411  0.0550  0.1124  153 GLY   B CA  
1361 C C   . GLY   B 144 ? 0.9020 1.1130 0.3324 0.2381  0.0612  0.1229  153 GLY   B C   
1362 O O   . GLY   B 144 ? 0.8876 1.1162 0.3429 0.2171  0.0554  0.1194  153 GLY   B O   
1363 N N   . VAL   B 145 ? 0.9234 1.1585 0.3564 0.2596  0.0729  0.1353  154 VAL   B N   
1364 C CA  . VAL   B 145 ? 0.9255 1.2145 0.3951 0.2597  0.0793  0.1462  154 VAL   B CA  
1365 C C   . VAL   B 145 ? 0.9457 1.2623 0.4340 0.2673  0.1012  0.1636  154 VAL   B C   
1366 O O   . VAL   B 145 ? 0.9603 1.2514 0.4238 0.2802  0.1109  0.1677  154 VAL   B O   
1367 C CB  . VAL   B 145 ? 0.9342 1.2344 0.3874 0.2843  0.0695  0.1441  154 VAL   B CB  
1368 C CG1 . VAL   B 145 ? 0.9515 1.2494 0.3776 0.3205  0.0794  0.1517  154 VAL   B CG1 
1369 C CG2 . VAL   B 145 ? 0.9073 1.2612 0.4008 0.2763  0.0653  0.1478  154 VAL   B CG2 
1370 N N   . VAL   B 146 ? 0.9417 1.3117 0.4751 0.2583  0.1088  0.1742  155 VAL   B N   
1371 C CA  . VAL   B 146 ? 0.9557 1.3595 0.5132 0.2633  0.1320  0.1935  155 VAL   B CA  
1372 C C   . VAL   B 146 ? 0.9788 1.4252 0.5391 0.2941  0.1371  0.2016  155 VAL   B C   
1373 O O   . VAL   B 146 ? 0.9635 1.4474 0.5498 0.2914  0.1267  0.1987  155 VAL   B O   
1374 C CB  . VAL   B 146 ? 0.9335 1.3680 0.5457 0.2271  0.1380  0.2002  155 VAL   B CB  
1375 C CG1 . VAL   B 146 ? 0.9230 1.3874 0.5591 0.2298  0.1654  0.2229  155 VAL   B CG1 
1376 C CG2 . VAL   B 146 ? 0.9542 1.3427 0.5597 0.1989  0.1292  0.1885  155 VAL   B CG2 
1377 N N   . ILE   B 147 ? 1.0173 1.4552 0.5458 0.3266  0.1511  0.2101  156 ILE   B N   
1378 C CA  . ILE   B 147 ? 1.0389 1.5106 0.5606 0.3628  0.1573  0.2169  156 ILE   B CA  
1379 C C   . ILE   B 147 ? 1.0404 1.5809 0.6110 0.3642  0.1819  0.2387  156 ILE   B C   
1380 O O   . ILE   B 147 ? 1.0364 1.5903 0.6416 0.3361  0.1951  0.2493  156 ILE   B O   
1381 C CB  . ILE   B 147 ? 1.0769 1.4999 0.5341 0.3991  0.1582  0.2125  156 ILE   B CB  
1382 C CG1 . ILE   B 147 ? 1.0954 1.5015 0.5383 0.4022  0.1785  0.2241  156 ILE   B CG1 
1383 C CG2 . ILE   B 147 ? 1.1113 1.4740 0.5284 0.3957  0.1333  0.1915  156 ILE   B CG2 
1384 C CD1 . ILE   B 147 ? 1.1388 1.5034 0.5194 0.4401  0.1794  0.2200  156 ILE   B CD1 
1385 N N   . LYS   B 148 ? 1.0424 1.6260 0.6162 0.3970  0.1890  0.2460  157 LYS   B N   
1386 C CA  . LYS   B 148 ? 1.0260 1.6830 0.6481 0.4029  0.2141  0.2675  157 LYS   B CA  
1387 C C   . LYS   B 148 ? 1.0376 1.6920 0.6596 0.4003  0.2438  0.2868  157 LYS   B C   
1388 O O   . LYS   B 148 ? 1.0054 1.7183 0.6786 0.3899  0.2662  0.3066  157 LYS   B O   
1389 C CB  . LYS   B 148 ? 1.0579 1.7481 0.6653 0.4496  0.2182  0.2707  157 LYS   B CB  
1390 C CG  . LYS   B 148 ? 1.1447 1.8221 0.7336 0.4622  0.1892  0.2522  157 LYS   B CG  
1391 C CD  . LYS   B 148 ? 1.2185 1.9233 0.7879 0.5127  0.1946  0.2560  157 LYS   B CD  
1392 C CE  . LYS   B 148 ? 1.2201 2.0208 0.8564 0.5165  0.2095  0.2722  157 LYS   B CE  
1393 N NZ  . LYS   B 148 ? 1.2257 2.0639 0.9093 0.4920  0.1867  0.2639  157 LYS   B NZ  
1394 N N   . ASN   B 149 ? 1.0799 1.6683 0.6448 0.4107  0.2441  0.2819  158 ASN   B N   
1395 C CA  . ASN   B 149 ? 1.0920 1.6684 0.6453 0.4125  0.2704  0.2997  158 ASN   B CA  
1396 C C   . ASN   B 149 ? 1.0795 1.6351 0.6591 0.3676  0.2717  0.3028  158 ASN   B C   
1397 O O   . ASN   B 149 ? 1.0895 1.6339 0.6622 0.3660  0.2939  0.3195  158 ASN   B O   
1398 C CB  . ASN   B 149 ? 1.1659 1.6817 0.6421 0.4488  0.2683  0.2922  158 ASN   B CB  
1399 C CG  . ASN   B 149 ? 1.2363 1.7512 0.6732 0.4931  0.2607  0.2832  158 ASN   B CG  
1400 O OD1 . ASN   B 149 ? 1.2321 1.8021 0.6966 0.5081  0.2668  0.2895  158 ASN   B OD1 
1401 N ND2 . ASN   B 149 ? 1.2875 1.7388 0.6593 0.5153  0.2462  0.2675  158 ASN   B ND2 
1402 N N   . GLY   B 150 ? 1.0572 1.6022 0.6601 0.3346  0.2482  0.2867  159 GLY   B N   
1403 C CA  . GLY   B 150 ? 1.0488 1.5688 0.6725 0.2941  0.2466  0.2863  159 GLY   B CA  
1404 C C   . GLY   B 150 ? 1.0739 1.5203 0.6460 0.2943  0.2312  0.2702  159 GLY   B C   
1405 O O   . GLY   B 150 ? 1.0774 1.4979 0.6612 0.2632  0.2185  0.2598  159 GLY   B O   
1406 N N   . SER   B 151 ? 1.0825 1.4959 0.5972 0.3307  0.2318  0.2671  160 SER   B N   
1407 C CA  A SER   B 151 ? 1.1131 1.4615 0.5791 0.3347  0.2166  0.2515  160 SER   B CA  
1408 C CA  B SER   B 151 ? 1.1145 1.4630 0.5807 0.3347  0.2166  0.2515  160 SER   B CA  
1409 C C   . SER   B 151 ? 1.1083 1.4337 0.5694 0.3215  0.1870  0.2270  160 SER   B C   
1410 O O   . SER   B 151 ? 1.0939 1.4489 0.5755 0.3195  0.1771  0.2214  160 SER   B O   
1411 C CB  A SER   B 151 ? 1.1576 1.4813 0.5659 0.3772  0.2219  0.2527  160 SER   B CB  
1412 C CB  B SER   B 151 ? 1.1633 1.4871 0.5719 0.3770  0.2221  0.2529  160 SER   B CB  
1413 O OG  A SER   B 151 ? 1.2187 1.4844 0.5837 0.3812  0.2042  0.2359  160 SER   B OG  
1414 O OG  B SER   B 151 ? 1.1930 1.5415 0.5907 0.4063  0.2205  0.2509  160 SER   B OG  
1415 N N   . TYR   B 152 ? 1.1011 1.3754 0.5354 0.3133  0.1735  0.2132  161 TYR   B N   
1416 C CA  . TYR   B 152 ? 1.0818 1.3311 0.5093 0.2997  0.1486  0.1916  161 TYR   B CA  
1417 C C   . TYR   B 152 ? 1.0753 1.2910 0.4542 0.3265  0.1340  0.1777  161 TYR   B C   
1418 O O   . TYR   B 152 ? 1.0946 1.2840 0.4373 0.3480  0.1374  0.1784  161 TYR   B O   
1419 C CB  . TYR   B 152 ? 1.0878 1.3049 0.5204 0.2727  0.1433  0.1845  161 TYR   B CB  
1420 C CG  . TYR   B 152 ? 1.0890 1.2979 0.5348 0.2482  0.1241  0.1674  161 TYR   B CG  
1421 C CD1 . TYR   B 152 ? 1.0739 1.3155 0.5604 0.2250  0.1221  0.1682  161 TYR   B CD1 
1422 C CD2 . TYR   B 152 ? 1.1202 1.2895 0.5385 0.2478  0.1082  0.1505  161 TYR   B CD2 
1423 C CE1 . TYR   B 152 ? 1.0851 1.3175 0.5782 0.2050  0.1048  0.1524  161 TYR   B CE1 
1424 C CE2 . TYR   B 152 ? 1.1268 1.2890 0.5548 0.2266  0.0934  0.1363  161 TYR   B CE2 
1425 C CZ  . TYR   B 152 ? 1.1164 1.3086 0.5788 0.2065  0.0918  0.1373  161 TYR   B CZ  
1426 O OH  . TYR   B 152 ? 1.1270 1.3111 0.5941 0.1878  0.0774  0.1234  161 TYR   B OH  
1427 N N   . VAL   B 153 ? 1.0455 1.2589 0.4217 0.3247  0.1167  0.1648  162 VAL   B N   
1428 C CA  . VAL   B 153 ? 1.0408 1.2160 0.3730 0.3444  0.1012  0.1507  162 VAL   B CA  
1429 C C   . VAL   B 153 ? 1.0097 1.1589 0.3444 0.3189  0.0832  0.1347  162 VAL   B C   
1430 O O   . VAL   B 153 ? 0.9951 1.1619 0.3519 0.3031  0.0769  0.1322  162 VAL   B O   
1431 C CB  . VAL   B 153 ? 1.0497 1.2381 0.3646 0.3741  0.0995  0.1520  162 VAL   B CB  
1432 C CG1 . VAL   B 153 ? 1.0872 1.2263 0.3551 0.3905  0.0819  0.1361  162 VAL   B CG1 
1433 C CG2 . VAL   B 153 ? 1.0501 1.2666 0.3617 0.4014  0.1203  0.1685  162 VAL   B CG2 
1434 N N   . SER   B 154 ? 1.0008 1.1116 0.3148 0.3147  0.0759  0.1248  163 SER   B N   
1435 C CA  . SER   B 154 ? 0.9850 1.0730 0.3021 0.2913  0.0622  0.1109  163 SER   B CA  
1436 C C   . SER   B 154 ? 0.9822 1.0391 0.2689 0.3002  0.0463  0.0981  163 SER   B C   
1437 O O   . SER   B 154 ? 0.9865 1.0238 0.2421 0.3239  0.0429  0.0957  163 SER   B O   
1438 C CB  . SER   B 154 ? 0.9917 1.0601 0.3089 0.2812  0.0639  0.1077  163 SER   B CB  
1439 O OG  . SER   B 154 ? 0.9949 1.0403 0.3112 0.2634  0.0514  0.0935  163 SER   B OG  
1440 N N   . ALA   B 155 ? 0.9688 1.0175 0.2623 0.2808  0.0365  0.0898  164 ALA   B N   
1441 C CA  . ALA   B 155 ? 0.9839 0.9988 0.2504 0.2841  0.0226  0.0790  164 ALA   B CA  
1442 C C   . ALA   B 155 ? 0.9886 0.9725 0.2441 0.2775  0.0160  0.0682  164 ALA   B C   
1443 O O   . ALA   B 155 ? 0.9631 0.9533 0.2323 0.2703  0.0217  0.0690  164 ALA   B O   
1444 C CB  . ALA   B 155 ? 0.9896 1.0078 0.2665 0.2651  0.0169  0.0760  164 ALA   B CB  
1445 N N   . ILE   B 156 ? 1.0103 0.9606 0.2413 0.2809  0.0035  0.0583  165 ILE   B N   
1446 C CA  . ILE   B 156 ? 1.0260 0.9521 0.2530 0.2712  -0.0050 0.0469  165 ILE   B CA  
1447 C C   . ILE   B 156 ? 1.0265 0.9467 0.2657 0.2458  -0.0084 0.0423  165 ILE   B C   
1448 O O   . ILE   B 156 ? 1.0432 0.9397 0.2650 0.2451  -0.0162 0.0388  165 ILE   B O   
1449 C CB  . ILE   B 156 ? 1.0556 0.9478 0.2489 0.2901  -0.0175 0.0381  165 ILE   B CB  
1450 C CG1 . ILE   B 156 ? 1.0714 0.9702 0.2459 0.3201  -0.0122 0.0440  165 ILE   B CG1 
1451 C CG2 . ILE   B 156 ? 1.0641 0.9383 0.2615 0.2765  -0.0280 0.0254  165 ILE   B CG2 
1452 C CD1 . ILE   B 156 ? 1.1146 0.9776 0.2495 0.3431  -0.0255 0.0341  165 ILE   B CD1 
1453 N N   . THR   B 157 ? 1.0040 0.9450 0.2705 0.2267  -0.0010 0.0437  166 THR   B N   
1454 C CA  . THR   B 157 ? 1.0051 0.9457 0.2833 0.2037  -0.0009 0.0404  166 THR   B CA  
1455 C C   . THR   B 157 ? 1.0117 0.9353 0.2934 0.1901  -0.0060 0.0303  166 THR   B C   
1456 O O   . THR   B 157 ? 1.0045 0.9358 0.3011 0.1865  -0.0043 0.0263  166 THR   B O   
1457 C CB  . THR   B 157 ? 0.9963 0.9643 0.2996 0.1910  0.0084  0.0445  166 THR   B CB  
1458 O OG1 . THR   B 157 ? 0.9929 0.9825 0.3000 0.2020  0.0131  0.0541  166 THR   B OG1 
1459 C CG2 . THR   B 157 ? 1.0093 0.9770 0.3173 0.1723  0.0085  0.0415  166 THR   B CG2 
1460 N N   . GLN   B 158 ? 1.0184 0.9196 0.2876 0.1828  -0.0120 0.0270  167 GLN   B N   
1461 C CA  . GLN   B 158 ? 1.0262 0.9145 0.3031 0.1668  -0.0160 0.0184  167 GLN   B CA  
1462 C C   . GLN   B 158 ? 1.0459 0.9344 0.3283 0.1467  -0.0096 0.0204  167 GLN   B C   
1463 O O   . GLN   B 158 ? 1.0452 0.9297 0.3133 0.1486  -0.0077 0.0272  167 GLN   B O   
1464 C CB  . GLN   B 158 ? 1.0444 0.9008 0.3006 0.1742  -0.0287 0.0126  167 GLN   B CB  
1465 C CG  . GLN   B 158 ? 1.0688 0.9142 0.3380 0.1563  -0.0348 0.0030  167 GLN   B CG  
1466 C CD  . GLN   B 158 ? 1.0920 0.9587 0.3851 0.1553  -0.0362 -0.0044 167 GLN   B CD  
1467 O OE1 . GLN   B 158 ? 1.0934 0.9862 0.4060 0.1512  -0.0263 -0.0020 167 GLN   B OE1 
1468 N NE2 . GLN   B 158 ? 1.0938 0.9480 0.3848 0.1592  -0.0499 -0.0145 167 GLN   B NE2 
1469 N N   . GLY   B 159 ? 1.0588 0.9541 0.3609 0.1298  -0.0060 0.0148  168 GLY   B N   
1470 C CA  . GLY   B 159 ? 1.0906 0.9863 0.3960 0.1118  0.0021  0.0168  168 GLY   B CA  
1471 C C   . GLY   B 159 ? 1.1385 1.0072 0.4342 0.1007  -0.0014 0.0166  168 GLY   B C   
1472 O O   . GLY   B 159 ? 1.1503 0.9946 0.4311 0.1083  -0.0120 0.0149  168 GLY   B O   
1473 N N   . LYS   B 160 ? 1.1660 1.0371 0.4689 0.0826  0.0083  0.0183  169 LYS   B N   
1474 C CA  . LYS   B 160 ? 1.2091 1.0556 0.5066 0.0672  0.0088  0.0204  169 LYS   B CA  
1475 C C   . LYS   B 160 ? 1.2231 1.0903 0.5544 0.0489  0.0156  0.0145  169 LYS   B C   
1476 O O   . LYS   B 160 ? 1.2153 1.1096 0.5618 0.0454  0.0267  0.0136  169 LYS   B O   
1477 C CB  . LYS   B 160 ? 1.2485 1.0786 0.5197 0.0633  0.0171  0.0315  169 LYS   B CB  
1478 C CG  . LYS   B 160 ? 1.3182 1.1112 0.5740 0.0507  0.0170  0.0372  169 LYS   B CG  
1479 C CD  . LYS   B 160 ? 1.3929 1.1671 0.6170 0.0501  0.0255  0.0499  169 LYS   B CD  
1480 C CE  . LYS   B 160 ? 1.4588 1.1921 0.6670 0.0355  0.0279  0.0577  169 LYS   B CE  
1481 N NZ  . LYS   B 160 ? 1.5052 1.2340 0.6982 0.0245  0.0447  0.0696  169 LYS   B NZ  
1482 N N   . ARG   B 161 ? 1.2419 1.0976 0.5860 0.0381  0.0082  0.0094  170 ARG   B N   
1483 C CA  . ARG   B 161 ? 1.2441 1.1247 0.6258 0.0202  0.0140  0.0038  170 ARG   B CA  
1484 C C   . ARG   B 161 ? 1.2698 1.1377 0.6500 -0.0019 0.0272  0.0130  170 ARG   B C   
1485 O O   . ARG   B 161 ? 1.2912 1.1252 0.6594 -0.0115 0.0212  0.0162  170 ARG   B O   
1486 C CB  . ARG   B 161 ? 1.2531 1.1335 0.6545 0.0195  -0.0034 -0.0081 170 ARG   B CB  
1487 C CG  . ARG   B 161 ? 1.2593 1.1731 0.7057 0.0025  0.0003  -0.0150 170 ARG   B CG  
1488 C CD  . ARG   B 161 ? 1.2917 1.2046 0.7568 0.0011  -0.0204 -0.0279 170 ARG   B CD  
1489 N NE  . ARG   B 161 ? 1.2946 1.2434 0.8077 -0.0172 -0.0176 -0.0342 170 ARG   B NE  
1490 C CZ  . ARG   B 161 ? 1.2928 1.2783 0.8358 -0.0084 -0.0247 -0.0450 170 ARG   B CZ  
1491 N NH1 . ARG   B 161 ? 1.2858 1.2724 0.8125 0.0176  -0.0344 -0.0498 170 ARG   B NH1 
1492 N NH2 . ARG   B 161 ? 1.2646 1.2869 0.8540 -0.0248 -0.0216 -0.0502 170 ARG   B NH2 
1493 N N   . GLU   B 162 ? 1.2682 1.1592 0.6566 -0.0089 0.0458  0.0180  171 GLU   B N   
1494 C CA  . GLU   B 162 ? 1.2904 1.1710 0.6743 -0.0285 0.0622  0.0291  171 GLU   B CA  
1495 C C   . GLU   B 162 ? 1.2800 1.1725 0.7032 -0.0521 0.0646  0.0262  171 GLU   B C   
1496 O O   . GLU   B 162 ? 1.2944 1.1551 0.7122 -0.0670 0.0605  0.0309  171 GLU   B O   
1497 C CB  . GLU   B 162 ? 1.3208 1.2234 0.6981 -0.0262 0.0817  0.0342  171 GLU   B CB  
1498 C CG  . GLU   B 162 ? 1.4114 1.2975 0.7474 -0.0090 0.0800  0.0394  171 GLU   B CG  
1499 C CD  . GLU   B 162 ? 1.5291 1.3790 0.8262 -0.0130 0.0860  0.0539  171 GLU   B CD  
1500 O OE1 . GLU   B 162 ? 1.5494 1.4037 0.8321 -0.0170 0.1027  0.0614  171 GLU   B OE1 
1501 O OE2 . GLU   B 162 ? 1.5736 1.3884 0.8512 -0.0102 0.0741  0.0577  171 GLU   B OE2 
1502 S S   . DMS   C .   ? 1.5048 1.3914 0.8500 0.0508  0.0404  -0.0869 201 DMS   B S   
1503 O O   . DMS   C .   ? 1.4970 1.4039 0.8396 0.0615  0.0500  -0.0803 201 DMS   B O   
1504 C C1  . DMS   C .   ? 1.5171 1.3692 0.8623 0.0594  0.0478  -0.0948 201 DMS   B C1  
1505 C C2  . DMS   C .   ? 1.4889 1.3844 0.8656 0.0430  0.0376  -0.0690 201 DMS   B C2  
1506 N N1  . A1B84 D .   ? 0.9319 1.0072 0.4310 0.1057  0.0891  0.1048  202 A1B84 B N1  
1507 N N3  . A1B84 D .   ? 0.9293 1.0612 0.3949 0.0904  0.0184  0.0506  202 A1B84 B N3  
1508 C C4  . A1B84 D .   ? 0.9321 1.0693 0.4085 0.1308  0.0561  0.0899  202 A1B84 B C4  
1509 C C5  . A1B84 D .   ? 0.9385 1.0650 0.3972 0.1300  0.0441  0.0781  202 A1B84 B C5  
1510 C C6  . A1B84 D .   ? 0.9331 1.0606 0.3997 0.1114  0.0361  0.0680  202 A1B84 B C6  
1511 C C7  . A1B84 D .   ? 0.9250 1.0604 0.4170 0.0925  0.0380  0.0673  202 A1B84 B C7  
1512 C C8  . A1B84 D .   ? 0.9176 1.0623 0.4309 0.0903  0.0497  0.0793  202 A1B84 B C8  
1513 C C10 . A1B84 D .   ? 0.9375 1.0536 0.3845 0.1080  0.0251  0.0563  202 A1B84 B C10 
1514 C C13 . A1B84 D .   ? 0.8886 1.0834 0.4112 0.1653  0.1328  0.1698  202 A1B84 B C13 
1515 C C15 . A1B84 D .   ? 0.9285 1.0652 0.3799 0.2052  0.1304  0.1640  202 A1B84 B C15 
1516 C C17 . A1B84 D .   ? 0.9554 1.0423 0.3789 0.1984  0.1039  0.1330  202 A1B84 B C17 
1517 C C1  . A1B84 D .   ? 0.9240 1.0244 0.4248 0.1140  0.0873  0.1087  202 A1B84 B C1  
1518 C C2  . A1B84 D .   ? 0.9186 1.0504 0.4204 0.1262  0.0845  0.1132  202 A1B84 B C2  
1519 N N2  . A1B84 D .   ? 0.9153 1.0700 0.4368 0.1102  0.0740  0.1060  202 A1B84 B N2  
1520 C C3  . A1B84 D .   ? 0.9190 1.0666 0.4240 0.1104  0.0597  0.0918  202 A1B84 B C3  
1521 C C9  . A1B84 D .   ? 0.9252 1.0562 0.4146 0.0772  0.0261  0.0530  202 A1B84 B C9  
1522 C C11 . A1B84 D .   ? 0.9077 1.0606 0.4171 0.1399  0.0999  0.1325  202 A1B84 B C11 
1523 C C12 . A1B84 D .   ? 0.8847 1.0753 0.4287 0.1293  0.1069  0.1437  202 A1B84 B C12 
1524 N N4  . A1B84 D .   ? 0.8756 1.0890 0.4284 0.1413  0.1235  0.1624  202 A1B84 B N4  
1525 C C14 . A1B84 D .   ? 0.9129 1.0681 0.3976 0.1785  0.1240  0.1582  202 A1B84 B C14 
1526 C C16 . A1B84 D .   ? 0.9500 1.0525 0.3710 0.2146  0.1190  0.1507  202 A1B84 B C16 
1527 C C18 . A1B84 D .   ? 0.9399 1.0419 0.3902 0.1748  0.0991  0.1277  202 A1B84 B C18 
1528 C C19 . A1B84 D .   ? 0.9196 1.0551 0.4008 0.1640  0.1075  0.1392  202 A1B84 B C19 
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