data_7IAA
# 
_entry.id   7IAA 
# 
_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   7IAA         pdb_00007iaa 10.2210/pdb7iaa/pdb 
WWPDB D_1001408513 ?            ?                   
# 
_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                        7IAA 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                                     5067.486  1  
?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                              18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                               78.133    1  
?                           ?    ? ? 
4 non-polymer syn '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-(oxan-4-yl)acetamide' 425.911   1  
?                           ?    ? ? 
5 water       nat water                                                                                              18.015    85 
?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                               DMS   
4 '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-(oxan-4-yl)acetamide' A1B8T 
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 
A1B8T non-polymer         . '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-(oxan-4-yl)acetamide' ? 
'C22 H24 Cl N5 O2' 425.911 
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 A1B8T 1  202 203 A1B8T LIG B . 
E 5 HOH   1  101 134 HOH   HOH A . 
E 5 HOH   2  102 34  HOH   HOH A . 
E 5 HOH   3  103 118 HOH   HOH A . 
E 5 HOH   4  104 48  HOH   HOH A . 
E 5 HOH   5  105 98  HOH   HOH A . 
E 5 HOH   6  106 65  HOH   HOH A . 
E 5 HOH   7  107 16  HOH   HOH A . 
E 5 HOH   8  108 121 HOH   HOH A . 
E 5 HOH   9  109 28  HOH   HOH A . 
E 5 HOH   10 110 129 HOH   HOH A . 
E 5 HOH   11 111 119 HOH   HOH A . 
E 5 HOH   12 112 105 HOH   HOH A . 
E 5 HOH   13 113 49  HOH   HOH A . 
E 5 HOH   14 114 50  HOH   HOH A . 
E 5 HOH   15 115 29  HOH   HOH A . 
E 5 HOH   16 116 27  HOH   HOH A . 
E 5 HOH   17 117 128 HOH   HOH A . 
F 5 HOH   1  301 92  HOH   HOH B . 
F 5 HOH   2  302 90  HOH   HOH B . 
F 5 HOH   3  303 5   HOH   HOH B . 
F 5 HOH   4  304 9   HOH   HOH B . 
F 5 HOH   5  305 14  HOH   HOH B . 
F 5 HOH   6  306 11  HOH   HOH B . 
F 5 HOH   7  307 42  HOH   HOH B . 
F 5 HOH   8  308 132 HOH   HOH B . 
F 5 HOH   9  309 58  HOH   HOH B . 
F 5 HOH   10 310 24  HOH   HOH B . 
F 5 HOH   11 311 31  HOH   HOH B . 
F 5 HOH   12 312 81  HOH   HOH B . 
F 5 HOH   13 313 135 HOH   HOH B . 
F 5 HOH   14 314 4   HOH   HOH B . 
F 5 HOH   15 315 117 HOH   HOH B . 
F 5 HOH   16 316 32  HOH   HOH B . 
F 5 HOH   17 317 46  HOH   HOH B . 
F 5 HOH   18 318 63  HOH   HOH B . 
F 5 HOH   19 319 108 HOH   HOH B . 
F 5 HOH   20 320 12  HOH   HOH B . 
F 5 HOH   21 321 10  HOH   HOH B . 
F 5 HOH   22 322 68  HOH   HOH B . 
F 5 HOH   23 323 1   HOH   HOH B . 
F 5 HOH   24 324 13  HOH   HOH B . 
F 5 HOH   25 325 2   HOH   HOH B . 
F 5 HOH   26 326 66  HOH   HOH B . 
F 5 HOH   27 327 20  HOH   HOH B . 
F 5 HOH   28 328 56  HOH   HOH B . 
F 5 HOH   29 329 120 HOH   HOH B . 
F 5 HOH   30 330 30  HOH   HOH B . 
F 5 HOH   31 331 23  HOH   HOH B . 
F 5 HOH   32 332 103 HOH   HOH B . 
F 5 HOH   33 333 35  HOH   HOH B . 
F 5 HOH   34 334 102 HOH   HOH B . 
F 5 HOH   35 335 72  HOH   HOH B . 
F 5 HOH   36 336 18  HOH   HOH B . 
F 5 HOH   37 337 94  HOH   HOH B . 
F 5 HOH   38 338 133 HOH   HOH B . 
F 5 HOH   39 339 21  HOH   HOH B . 
F 5 HOH   40 340 69  HOH   HOH B . 
F 5 HOH   41 341 54  HOH   HOH B . 
F 5 HOH   42 342 67  HOH   HOH B . 
F 5 HOH   43 343 3   HOH   HOH B . 
F 5 HOH   44 344 107 HOH   HOH B . 
F 5 HOH   45 345 116 HOH   HOH B . 
F 5 HOH   46 346 62  HOH   HOH B . 
F 5 HOH   47 347 130 HOH   HOH B . 
F 5 HOH   48 348 127 HOH   HOH B . 
F 5 HOH   49 349 137 HOH   HOH B . 
F 5 HOH   50 350 64  HOH   HOH B . 
F 5 HOH   51 351 60  HOH   HOH B . 
F 5 HOH   52 352 43  HOH   HOH B . 
F 5 HOH   53 353 61  HOH   HOH B . 
F 5 HOH   54 354 131 HOH   HOH B . 
F 5 HOH   55 355 106 HOH   HOH B . 
F 5 HOH   56 356 123 HOH   HOH B . 
F 5 HOH   57 357 136 HOH   HOH B . 
F 5 HOH   58 358 26  HOH   HOH B . 
F 5 HOH   59 359 79  HOH   HOH B . 
F 5 HOH   60 360 45  HOH   HOH B . 
F 5 HOH   61 361 87  HOH   HOH B . 
F 5 HOH   62 362 80  HOH   HOH B . 
F 5 HOH   63 363 109 HOH   HOH B . 
F 5 HOH   64 364 44  HOH   HOH B . 
F 5 HOH   65 365 126 HOH   HOH B . 
F 5 HOH   66 366 75  HOH   HOH B . 
F 5 HOH   67 367 59  HOH   HOH B . 
F 5 HOH   68 368 57  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           7IAA 
_cell.length_a           42.609 
_cell.length_b           42.609 
_cell.length_c           216.395 
_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                         7IAA 
_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          7IAA 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.060 
_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   41.93 
_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   2024-08-01 
_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                     7IAA 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             216.400 
_reflns.d_resolution_high            1.950 
_reflns.number_obs                   15555 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.325 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.800 
_reflns.B_iso_Wilson_estimate        40.510 
_reflns.pdbx_redundancy              25.300 
_reflns.pdbx_Rrim_I_all              0.332 
_reflns.pdbx_Rpim_I_all              0.065 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     393855 
_reflns.pdbx_scaling_rejects         190 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.950 2.070   ? 65553 ? ? 9.796 ? ? ? 27.000 ? 0.500  ? 2432 ? ? ? ? 100.000 9.981 1.899 0.431 ? 
1 2 5.860 216.400 ? 14390 ? ? 0.077 ? ? ? 20.000 ? 28.200 ? 720  ? ? ? ? 100.000 0.079 0.017 0.998 ? 
# 
_refine.entry_id                                 7IAA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.9540 
_refine.ls_d_res_low                             54.1000 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4000 
_refine.ls_number_reflns_obs                     15385 
_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                          0.2338 
_refine.ls_R_factor_R_work                       0.2312 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2830 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  741 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               52.5400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -4.1912 
_refine.aniso_B[2][2]                            -4.1912 
_refine.aniso_B[3][3]                            8.3824 
_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               0.9440 
_refine.correlation_coeff_Fo_to_Fc_free          0.9290 
_refine.overall_SU_R_Cruickshank_DPI             0.1930 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.1800 
_refine.pdbx_overall_SU_R_Blow_DPI               0.2100 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.1870 
_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                                101.810 
_refine.B_iso_min                                33.490 
_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                        7IAA 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.300 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.9540 
_refine_hist.d_res_low                        54.1000 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             85 
_refine_hist.number_atoms_total               1595 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           55.09 
_refine_hist.pdbx_B_iso_mean_solvent          54.03 
_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        546  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              271  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1580 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     0    ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 197  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1208 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1580 0.008  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2153 1.030  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.330  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    19.000 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       1.9500 
_refine_ls_shell.d_res_low                        1.9700 
_refine_ls_shell.pdbx_total_number_of_bins_used   38 
_refine_ls_shell.percent_reflns_obs               97.3200 
_refine_ls_shell.number_reflns_R_work             390 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.4086 
_refine_ls_shell.R_factor_R_free                  0.4657 
_refine_ls_shell.percent_reflns_R_free            6.2500 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                416 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAA 
_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-0029888-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAA 
_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 7IAA A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAA 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 7IAA SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAA MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAA MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAA 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)' 4340 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9580 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7IAA 
_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 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     348 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     348 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_554 
_pdbx_validate_symm_contact.dist              1.03 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30 ? ? -89.48 -157.27 
2 1 CYS B 80 ? ? 80.01  -19.11  
# 
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 -13.4797 -2.1425 -19.3695 -0.0462 -0.0690 -0.2028 0.1631 0.1756 0.1649 4.2125 3.9740 3.9455 
-2.1418 0.5357 0.5553  0.5052 -0.4670 -0.0382 0.3675 0.3338 -0.3908 -0.5367 0.0735 0.3958 
'X-RAY DIFFRACTION' 2 ? refined -18.1472 0.3965  -15.6149 0.0636  0.0273  -0.0781 0.1742 0.0656 0.0554 1.0726 1.8901 1.9577 
-1.1073 0.3318 -0.4440 0.3638 -0.3489 -0.0149 0.1227 0.2403 -0.0033 -0.1680 0.1102 0.1724 
# 
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 
A1B8T N1   N  N N 1   
A1B8T N3   N  N N 2   
A1B8T C4   C  N N 3   
A1B8T C5   C  N N 4   
A1B8T C6   C  N N 5   
A1B8T C7   C  N R 6   
A1B8T C8   C  Y N 7   
A1B8T C10  C  Y N 8   
A1B8T C13  C  Y N 9   
A1B8T C15  C  N N 10  
A1B8T C17  C  Y N 11  
A1B8T C20  C  Y N 12  
A1B8T C21  C  Y N 13  
A1B8T C22  C  Y N 14  
A1B8T O1   O  N N 15  
A1B8T C1   C  N N 16  
A1B8T C2   C  N N 17  
A1B8T C3   C  N N 18  
A1B8T O2   O  N N 19  
A1B8T N2   N  N N 20  
A1B8T C9   C  Y N 21  
A1B8T C11  C  Y N 22  
A1B8T C12  C  Y N 23  
A1B8T C14  C  N N 24  
A1B8T C16  C  Y N 25  
A1B8T C18  C  Y N 26  
A1B8T CL1  CL N N 27  
A1B8T C19  C  Y N 28  
A1B8T N4   N  Y N 29  
A1B8T N5   N  Y N 30  
A1B8T H1   H  N N 31  
A1B8T H2   H  N N 32  
A1B8T H4   H  N N 33  
A1B8T H5   H  N N 34  
A1B8T H6   H  N N 35  
A1B8T H7   H  N N 36  
A1B8T H8   H  N N 37  
A1B8T H9   H  N N 38  
A1B8T H10  H  N N 39  
A1B8T H11  H  N N 40  
A1B8T H12  H  N N 41  
A1B8T H13  H  N N 42  
A1B8T H14  H  N N 43  
A1B8T H15  H  N N 44  
A1B8T H16  H  N N 45  
A1B8T H17  H  N N 46  
A1B8T H18  H  N N 47  
A1B8T H19  H  N N 48  
A1B8T H20  H  N N 49  
A1B8T H21  H  N N 50  
A1B8T H22  H  N N 51  
A1B8T H23  H  N N 52  
A1B8T H24  H  N N 53  
A1B8T H25  H  N N 54  
ALA   N    N  N N 55  
ALA   CA   C  N S 56  
ALA   C    C  N N 57  
ALA   O    O  N N 58  
ALA   CB   C  N N 59  
ALA   OXT  O  N N 60  
ALA   H    H  N N 61  
ALA   H2   H  N N 62  
ALA   HA   H  N N 63  
ALA   HB1  H  N N 64  
ALA   HB2  H  N N 65  
ALA   HB3  H  N N 66  
ALA   HXT  H  N N 67  
ARG   N    N  N N 68  
ARG   CA   C  N S 69  
ARG   C    C  N N 70  
ARG   O    O  N N 71  
ARG   CB   C  N N 72  
ARG   CG   C  N N 73  
ARG   CD   C  N N 74  
ARG   NE   N  N N 75  
ARG   CZ   C  N N 76  
ARG   NH1  N  N N 77  
ARG   NH2  N  N N 78  
ARG   OXT  O  N N 79  
ARG   H    H  N N 80  
ARG   H2   H  N N 81  
ARG   HA   H  N N 82  
ARG   HB2  H  N N 83  
ARG   HB3  H  N N 84  
ARG   HG2  H  N N 85  
ARG   HG3  H  N N 86  
ARG   HD2  H  N N 87  
ARG   HD3  H  N N 88  
ARG   HE   H  N N 89  
ARG   HH11 H  N N 90  
ARG   HH12 H  N N 91  
ARG   HH21 H  N N 92  
ARG   HH22 H  N N 93  
ARG   HXT  H  N N 94  
ASN   N    N  N N 95  
ASN   CA   C  N S 96  
ASN   C    C  N N 97  
ASN   O    O  N N 98  
ASN   CB   C  N N 99  
ASN   CG   C  N N 100 
ASN   OD1  O  N N 101 
ASN   ND2  N  N N 102 
ASN   OXT  O  N N 103 
ASN   H    H  N N 104 
ASN   H2   H  N N 105 
ASN   HA   H  N N 106 
ASN   HB2  H  N N 107 
ASN   HB3  H  N N 108 
ASN   HD21 H  N N 109 
ASN   HD22 H  N N 110 
ASN   HXT  H  N N 111 
ASP   N    N  N N 112 
ASP   CA   C  N S 113 
ASP   C    C  N N 114 
ASP   O    O  N N 115 
ASP   CB   C  N N 116 
ASP   CG   C  N N 117 
ASP   OD1  O  N N 118 
ASP   OD2  O  N N 119 
ASP   OXT  O  N N 120 
ASP   H    H  N N 121 
ASP   H2   H  N N 122 
ASP   HA   H  N N 123 
ASP   HB2  H  N N 124 
ASP   HB3  H  N N 125 
ASP   HD2  H  N N 126 
ASP   HXT  H  N N 127 
CYS   N    N  N N 128 
CYS   CA   C  N R 129 
CYS   C    C  N N 130 
CYS   O    O  N N 131 
CYS   CB   C  N N 132 
CYS   SG   S  N N 133 
CYS   OXT  O  N N 134 
CYS   H    H  N N 135 
CYS   H2   H  N N 136 
CYS   HA   H  N N 137 
CYS   HB2  H  N N 138 
CYS   HB3  H  N N 139 
CYS   HG   H  N N 140 
CYS   HXT  H  N N 141 
DMS   S    S  N N 142 
DMS   O    O  N N 143 
DMS   C1   C  N N 144 
DMS   C2   C  N N 145 
DMS   H11  H  N N 146 
DMS   H12  H  N N 147 
DMS   H13  H  N N 148 
DMS   H21  H  N N 149 
DMS   H22  H  N N 150 
DMS   H23  H  N N 151 
GLN   N    N  N N 152 
GLN   CA   C  N S 153 
GLN   C    C  N N 154 
GLN   O    O  N N 155 
GLN   CB   C  N N 156 
GLN   CG   C  N N 157 
GLN   CD   C  N N 158 
GLN   OE1  O  N N 159 
GLN   NE2  N  N N 160 
GLN   OXT  O  N N 161 
GLN   H    H  N N 162 
GLN   H2   H  N N 163 
GLN   HA   H  N N 164 
GLN   HB2  H  N N 165 
GLN   HB3  H  N N 166 
GLN   HG2  H  N N 167 
GLN   HG3  H  N N 168 
GLN   HE21 H  N N 169 
GLN   HE22 H  N N 170 
GLN   HXT  H  N N 171 
GLU   N    N  N N 172 
GLU   CA   C  N S 173 
GLU   C    C  N N 174 
GLU   O    O  N N 175 
GLU   CB   C  N N 176 
GLU   CG   C  N N 177 
GLU   CD   C  N N 178 
GLU   OE1  O  N N 179 
GLU   OE2  O  N N 180 
GLU   OXT  O  N N 181 
GLU   H    H  N N 182 
GLU   H2   H  N N 183 
GLU   HA   H  N N 184 
GLU   HB2  H  N N 185 
GLU   HB3  H  N N 186 
GLU   HG2  H  N N 187 
GLU   HG3  H  N N 188 
GLU   HE2  H  N N 189 
GLU   HXT  H  N N 190 
GLY   N    N  N N 191 
GLY   CA   C  N N 192 
GLY   C    C  N N 193 
GLY   O    O  N N 194 
GLY   OXT  O  N N 195 
GLY   H    H  N N 196 
GLY   H2   H  N N 197 
GLY   HA2  H  N N 198 
GLY   HA3  H  N N 199 
GLY   HXT  H  N N 200 
HIS   N    N  N N 201 
HIS   CA   C  N S 202 
HIS   C    C  N N 203 
HIS   O    O  N N 204 
HIS   CB   C  N N 205 
HIS   CG   C  Y N 206 
HIS   ND1  N  Y N 207 
HIS   CD2  C  Y N 208 
HIS   CE1  C  Y N 209 
HIS   NE2  N  Y N 210 
HIS   OXT  O  N N 211 
HIS   H    H  N N 212 
HIS   H2   H  N N 213 
HIS   HA   H  N N 214 
HIS   HB2  H  N N 215 
HIS   HB3  H  N N 216 
HIS   HD1  H  N N 217 
HIS   HD2  H  N N 218 
HIS   HE1  H  N N 219 
HIS   HE2  H  N N 220 
HIS   HXT  H  N N 221 
HOH   O    O  N N 222 
HOH   H1   H  N N 223 
HOH   H2   H  N N 224 
ILE   N    N  N N 225 
ILE   CA   C  N S 226 
ILE   C    C  N N 227 
ILE   O    O  N N 228 
ILE   CB   C  N S 229 
ILE   CG1  C  N N 230 
ILE   CG2  C  N N 231 
ILE   CD1  C  N N 232 
ILE   OXT  O  N N 233 
ILE   H    H  N N 234 
ILE   H2   H  N N 235 
ILE   HA   H  N N 236 
ILE   HB   H  N N 237 
ILE   HG12 H  N N 238 
ILE   HG13 H  N N 239 
ILE   HG21 H  N N 240 
ILE   HG22 H  N N 241 
ILE   HG23 H  N N 242 
ILE   HD11 H  N N 243 
ILE   HD12 H  N N 244 
ILE   HD13 H  N N 245 
ILE   HXT  H  N N 246 
LEU   N    N  N N 247 
LEU   CA   C  N S 248 
LEU   C    C  N N 249 
LEU   O    O  N N 250 
LEU   CB   C  N N 251 
LEU   CG   C  N N 252 
LEU   CD1  C  N N 253 
LEU   CD2  C  N N 254 
LEU   OXT  O  N N 255 
LEU   H    H  N N 256 
LEU   H2   H  N N 257 
LEU   HA   H  N N 258 
LEU   HB2  H  N N 259 
LEU   HB3  H  N N 260 
LEU   HG   H  N N 261 
LEU   HD11 H  N N 262 
LEU   HD12 H  N N 263 
LEU   HD13 H  N N 264 
LEU   HD21 H  N N 265 
LEU   HD22 H  N N 266 
LEU   HD23 H  N N 267 
LEU   HXT  H  N N 268 
LYS   N    N  N N 269 
LYS   CA   C  N S 270 
LYS   C    C  N N 271 
LYS   O    O  N N 272 
LYS   CB   C  N N 273 
LYS   CG   C  N N 274 
LYS   CD   C  N N 275 
LYS   CE   C  N N 276 
LYS   NZ   N  N N 277 
LYS   OXT  O  N N 278 
LYS   H    H  N N 279 
LYS   H2   H  N N 280 
LYS   HA   H  N N 281 
LYS   HB2  H  N N 282 
LYS   HB3  H  N N 283 
LYS   HG2  H  N N 284 
LYS   HG3  H  N N 285 
LYS   HD2  H  N N 286 
LYS   HD3  H  N N 287 
LYS   HE2  H  N N 288 
LYS   HE3  H  N N 289 
LYS   HZ1  H  N N 290 
LYS   HZ2  H  N N 291 
LYS   HZ3  H  N N 292 
LYS   HXT  H  N N 293 
MET   N    N  N N 294 
MET   CA   C  N S 295 
MET   C    C  N N 296 
MET   O    O  N N 297 
MET   CB   C  N N 298 
MET   CG   C  N N 299 
MET   SD   S  N N 300 
MET   CE   C  N N 301 
MET   OXT  O  N N 302 
MET   H    H  N N 303 
MET   H2   H  N N 304 
MET   HA   H  N N 305 
MET   HB2  H  N N 306 
MET   HB3  H  N N 307 
MET   HG2  H  N N 308 
MET   HG3  H  N N 309 
MET   HE1  H  N N 310 
MET   HE2  H  N N 311 
MET   HE3  H  N N 312 
MET   HXT  H  N N 313 
PHE   N    N  N N 314 
PHE   CA   C  N S 315 
PHE   C    C  N N 316 
PHE   O    O  N N 317 
PHE   CB   C  N N 318 
PHE   CG   C  Y N 319 
PHE   CD1  C  Y N 320 
PHE   CD2  C  Y N 321 
PHE   CE1  C  Y N 322 
PHE   CE2  C  Y N 323 
PHE   CZ   C  Y N 324 
PHE   OXT  O  N N 325 
PHE   H    H  N N 326 
PHE   H2   H  N N 327 
PHE   HA   H  N N 328 
PHE   HB2  H  N N 329 
PHE   HB3  H  N N 330 
PHE   HD1  H  N N 331 
PHE   HD2  H  N N 332 
PHE   HE1  H  N N 333 
PHE   HE2  H  N N 334 
PHE   HZ   H  N N 335 
PHE   HXT  H  N N 336 
PRO   N    N  N N 337 
PRO   CA   C  N S 338 
PRO   C    C  N N 339 
PRO   O    O  N N 340 
PRO   CB   C  N N 341 
PRO   CG   C  N N 342 
PRO   CD   C  N N 343 
PRO   OXT  O  N N 344 
PRO   H    H  N N 345 
PRO   HA   H  N N 346 
PRO   HB2  H  N N 347 
PRO   HB3  H  N N 348 
PRO   HG2  H  N N 349 
PRO   HG3  H  N N 350 
PRO   HD2  H  N N 351 
PRO   HD3  H  N N 352 
PRO   HXT  H  N N 353 
SER   N    N  N N 354 
SER   CA   C  N S 355 
SER   C    C  N N 356 
SER   O    O  N N 357 
SER   CB   C  N N 358 
SER   OG   O  N N 359 
SER   OXT  O  N N 360 
SER   H    H  N N 361 
SER   H2   H  N N 362 
SER   HA   H  N N 363 
SER   HB2  H  N N 364 
SER   HB3  H  N N 365 
SER   HG   H  N N 366 
SER   HXT  H  N N 367 
THR   N    N  N N 368 
THR   CA   C  N S 369 
THR   C    C  N N 370 
THR   O    O  N N 371 
THR   CB   C  N R 372 
THR   OG1  O  N N 373 
THR   CG2  C  N N 374 
THR   OXT  O  N N 375 
THR   H    H  N N 376 
THR   H2   H  N N 377 
THR   HA   H  N N 378 
THR   HB   H  N N 379 
THR   HG1  H  N N 380 
THR   HG21 H  N N 381 
THR   HG22 H  N N 382 
THR   HG23 H  N N 383 
THR   HXT  H  N N 384 
TRP   N    N  N N 385 
TRP   CA   C  N S 386 
TRP   C    C  N N 387 
TRP   O    O  N N 388 
TRP   CB   C  N N 389 
TRP   CG   C  Y N 390 
TRP   CD1  C  Y N 391 
TRP   CD2  C  Y N 392 
TRP   NE1  N  Y N 393 
TRP   CE2  C  Y N 394 
TRP   CE3  C  Y N 395 
TRP   CZ2  C  Y N 396 
TRP   CZ3  C  Y N 397 
TRP   CH2  C  Y N 398 
TRP   OXT  O  N N 399 
TRP   H    H  N N 400 
TRP   H2   H  N N 401 
TRP   HA   H  N N 402 
TRP   HB2  H  N N 403 
TRP   HB3  H  N N 404 
TRP   HD1  H  N N 405 
TRP   HE1  H  N N 406 
TRP   HE3  H  N N 407 
TRP   HZ2  H  N N 408 
TRP   HZ3  H  N N 409 
TRP   HH2  H  N N 410 
TRP   HXT  H  N N 411 
TYR   N    N  N N 412 
TYR   CA   C  N S 413 
TYR   C    C  N N 414 
TYR   O    O  N N 415 
TYR   CB   C  N N 416 
TYR   CG   C  Y N 417 
TYR   CD1  C  Y N 418 
TYR   CD2  C  Y N 419 
TYR   CE1  C  Y N 420 
TYR   CE2  C  Y N 421 
TYR   CZ   C  Y N 422 
TYR   OH   O  N N 423 
TYR   OXT  O  N N 424 
TYR   H    H  N N 425 
TYR   H2   H  N N 426 
TYR   HA   H  N N 427 
TYR   HB2  H  N N 428 
TYR   HB3  H  N N 429 
TYR   HD1  H  N N 430 
TYR   HD2  H  N N 431 
TYR   HE1  H  N N 432 
TYR   HE2  H  N N 433 
TYR   HH   H  N N 434 
TYR   HXT  H  N N 435 
VAL   N    N  N N 436 
VAL   CA   C  N S 437 
VAL   C    C  N N 438 
VAL   O    O  N N 439 
VAL   CB   C  N N 440 
VAL   CG1  C  N N 441 
VAL   CG2  C  N N 442 
VAL   OXT  O  N N 443 
VAL   H    H  N N 444 
VAL   H2   H  N N 445 
VAL   HA   H  N N 446 
VAL   HB   H  N N 447 
VAL   HG11 H  N N 448 
VAL   HG12 H  N N 449 
VAL   HG13 H  N N 450 
VAL   HG21 H  N N 451 
VAL   HG22 H  N N 452 
VAL   HG23 H  N N 453 
VAL   HXT  H  N N 454 
# 
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 
A1B8T CL1 C18  sing N N 1   
A1B8T C19 C20  doub Y N 2   
A1B8T C19 C18  sing Y N 3   
A1B8T N4  C20  sing Y N 4   
A1B8T N4  N5   sing Y N 5   
A1B8T C20 C22  sing Y N 6   
A1B8T C18 C17  doub Y N 7   
A1B8T N5  C21  doub Y N 8   
A1B8T C22 C21  sing Y N 9   
A1B8T C22 C16  doub Y N 10  
A1B8T C17 C16  sing Y N 11  
A1B8T C16 C7   sing N N 12  
A1B8T O1  C1   doub N N 13  
A1B8T C7  C1   sing N N 14  
A1B8T C7  N2   sing N N 15  
A1B8T C1  N1   sing N N 16  
A1B8T C6  C5   sing N N 17  
A1B8T C6  C2   sing N N 18  
A1B8T N2  C8   sing N N 19  
A1B8T C5  O2   sing N N 20  
A1B8T N1  C2   sing N N 21  
A1B8T C2  C3   sing N N 22  
A1B8T C8  C13  doub Y N 23  
A1B8T C8  C9   sing Y N 24  
A1B8T O2  C4   sing N N 25  
A1B8T C13 C12  sing Y N 26  
A1B8T C9  C10  doub Y N 27  
A1B8T C3  C4   sing N N 28  
A1B8T C12 C11  doub Y N 29  
A1B8T C12 C14  sing N N 30  
A1B8T C10 C11  sing Y N 31  
A1B8T C11 C15  sing N N 32  
A1B8T C14 N3   sing N N 33  
A1B8T C15 N3   sing N N 34  
A1B8T N1  H1   sing N N 35  
A1B8T N3  H2   sing N N 36  
A1B8T C4  H4   sing N N 37  
A1B8T C4  H5   sing N N 38  
A1B8T C5  H6   sing N N 39  
A1B8T C5  H7   sing N N 40  
A1B8T C6  H8   sing N N 41  
A1B8T C6  H9   sing N N 42  
A1B8T C7  H10  sing N N 43  
A1B8T C10 H11  sing N N 44  
A1B8T C13 H12  sing N N 45  
A1B8T C15 H13  sing N N 46  
A1B8T C15 H14  sing N N 47  
A1B8T C17 H15  sing N N 48  
A1B8T C21 H16  sing N N 49  
A1B8T C2  H17  sing N N 50  
A1B8T C3  H18  sing N N 51  
A1B8T C3  H19  sing N N 52  
A1B8T N2  H20  sing N N 53  
A1B8T C9  H21  sing N N 54  
A1B8T C14 H22  sing N N 55  
A1B8T C14 H23  sing N N 56  
A1B8T C19 H24  sing N N 57  
A1B8T N4  H25  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
DMS   S   O    doub N N 141 
DMS   S   C1   sing N N 142 
DMS   S   C2   sing N N 143 
DMS   C1  H11  sing N N 144 
DMS   C1  H12  sing N N 145 
DMS   C1  H13  sing N N 146 
DMS   C2  H21  sing N N 147 
DMS   C2  H22  sing N N 148 
DMS   C2  H23  sing N N 149 
GLN   N   CA   sing N N 150 
GLN   N   H    sing N N 151 
GLN   N   H2   sing N N 152 
GLN   CA  C    sing N N 153 
GLN   CA  CB   sing N N 154 
GLN   CA  HA   sing N N 155 
GLN   C   O    doub N N 156 
GLN   C   OXT  sing N N 157 
GLN   CB  CG   sing N N 158 
GLN   CB  HB2  sing N N 159 
GLN   CB  HB3  sing N N 160 
GLN   CG  CD   sing N N 161 
GLN   CG  HG2  sing N N 162 
GLN   CG  HG3  sing N N 163 
GLN   CD  OE1  doub N N 164 
GLN   CD  NE2  sing N N 165 
GLN   NE2 HE21 sing N N 166 
GLN   NE2 HE22 sing N N 167 
GLN   OXT HXT  sing N N 168 
GLU   N   CA   sing N N 169 
GLU   N   H    sing N N 170 
GLU   N   H2   sing N N 171 
GLU   CA  C    sing N N 172 
GLU   CA  CB   sing N N 173 
GLU   CA  HA   sing N N 174 
GLU   C   O    doub N N 175 
GLU   C   OXT  sing N N 176 
GLU   CB  CG   sing N N 177 
GLU   CB  HB2  sing N N 178 
GLU   CB  HB3  sing N N 179 
GLU   CG  CD   sing N N 180 
GLU   CG  HG2  sing N N 181 
GLU   CG  HG3  sing N N 182 
GLU   CD  OE1  doub N N 183 
GLU   CD  OE2  sing N N 184 
GLU   OE2 HE2  sing N N 185 
GLU   OXT HXT  sing N N 186 
GLY   N   CA   sing N N 187 
GLY   N   H    sing N N 188 
GLY   N   H2   sing N N 189 
GLY   CA  C    sing N N 190 
GLY   CA  HA2  sing N N 191 
GLY   CA  HA3  sing N N 192 
GLY   C   O    doub N N 193 
GLY   C   OXT  sing N N 194 
GLY   OXT HXT  sing N N 195 
HIS   N   CA   sing N N 196 
HIS   N   H    sing N N 197 
HIS   N   H2   sing N N 198 
HIS   CA  C    sing N N 199 
HIS   CA  CB   sing N N 200 
HIS   CA  HA   sing N N 201 
HIS   C   O    doub N N 202 
HIS   C   OXT  sing N N 203 
HIS   CB  CG   sing N N 204 
HIS   CB  HB2  sing N N 205 
HIS   CB  HB3  sing N N 206 
HIS   CG  ND1  sing Y N 207 
HIS   CG  CD2  doub Y N 208 
HIS   ND1 CE1  doub Y N 209 
HIS   ND1 HD1  sing N N 210 
HIS   CD2 NE2  sing Y N 211 
HIS   CD2 HD2  sing N N 212 
HIS   CE1 NE2  sing Y N 213 
HIS   CE1 HE1  sing N N 214 
HIS   NE2 HE2  sing N N 215 
HIS   OXT HXT  sing N N 216 
HOH   O   H1   sing N N 217 
HOH   O   H2   sing N N 218 
ILE   N   CA   sing N N 219 
ILE   N   H    sing N N 220 
ILE   N   H2   sing N N 221 
ILE   CA  C    sing N N 222 
ILE   CA  CB   sing N N 223 
ILE   CA  HA   sing N N 224 
ILE   C   O    doub N N 225 
ILE   C   OXT  sing N N 226 
ILE   CB  CG1  sing N N 227 
ILE   CB  CG2  sing N N 228 
ILE   CB  HB   sing N N 229 
ILE   CG1 CD1  sing N N 230 
ILE   CG1 HG12 sing N N 231 
ILE   CG1 HG13 sing N N 232 
ILE   CG2 HG21 sing N N 233 
ILE   CG2 HG22 sing N N 234 
ILE   CG2 HG23 sing N N 235 
ILE   CD1 HD11 sing N N 236 
ILE   CD1 HD12 sing N N 237 
ILE   CD1 HD13 sing N N 238 
ILE   OXT HXT  sing N N 239 
LEU   N   CA   sing N N 240 
LEU   N   H    sing N N 241 
LEU   N   H2   sing N N 242 
LEU   CA  C    sing N N 243 
LEU   CA  CB   sing N N 244 
LEU   CA  HA   sing N N 245 
LEU   C   O    doub N N 246 
LEU   C   OXT  sing N N 247 
LEU   CB  CG   sing N N 248 
LEU   CB  HB2  sing N N 249 
LEU   CB  HB3  sing N N 250 
LEU   CG  CD1  sing N N 251 
LEU   CG  CD2  sing N N 252 
LEU   CG  HG   sing N N 253 
LEU   CD1 HD11 sing N N 254 
LEU   CD1 HD12 sing N N 255 
LEU   CD1 HD13 sing N N 256 
LEU   CD2 HD21 sing N N 257 
LEU   CD2 HD22 sing N N 258 
LEU   CD2 HD23 sing N N 259 
LEU   OXT HXT  sing N N 260 
LYS   N   CA   sing N N 261 
LYS   N   H    sing N N 262 
LYS   N   H2   sing N N 263 
LYS   CA  C    sing N N 264 
LYS   CA  CB   sing N N 265 
LYS   CA  HA   sing N N 266 
LYS   C   O    doub N N 267 
LYS   C   OXT  sing N N 268 
LYS   CB  CG   sing N N 269 
LYS   CB  HB2  sing N N 270 
LYS   CB  HB3  sing N N 271 
LYS   CG  CD   sing N N 272 
LYS   CG  HG2  sing N N 273 
LYS   CG  HG3  sing N N 274 
LYS   CD  CE   sing N N 275 
LYS   CD  HD2  sing N N 276 
LYS   CD  HD3  sing N N 277 
LYS   CE  NZ   sing N N 278 
LYS   CE  HE2  sing N N 279 
LYS   CE  HE3  sing N N 280 
LYS   NZ  HZ1  sing N N 281 
LYS   NZ  HZ2  sing N N 282 
LYS   NZ  HZ3  sing N N 283 
LYS   OXT HXT  sing N N 284 
MET   N   CA   sing N N 285 
MET   N   H    sing N N 286 
MET   N   H2   sing N N 287 
MET   CA  C    sing N N 288 
MET   CA  CB   sing N N 289 
MET   CA  HA   sing N N 290 
MET   C   O    doub N N 291 
MET   C   OXT  sing N N 292 
MET   CB  CG   sing N N 293 
MET   CB  HB2  sing N N 294 
MET   CB  HB3  sing N N 295 
MET   CG  SD   sing N N 296 
MET   CG  HG2  sing N N 297 
MET   CG  HG3  sing N N 298 
MET   SD  CE   sing N N 299 
MET   CE  HE1  sing N N 300 
MET   CE  HE2  sing N N 301 
MET   CE  HE3  sing N N 302 
MET   OXT HXT  sing N N 303 
PHE   N   CA   sing N N 304 
PHE   N   H    sing N N 305 
PHE   N   H2   sing N N 306 
PHE   CA  C    sing N N 307 
PHE   CA  CB   sing N N 308 
PHE   CA  HA   sing N N 309 
PHE   C   O    doub N N 310 
PHE   C   OXT  sing N N 311 
PHE   CB  CG   sing N N 312 
PHE   CB  HB2  sing N N 313 
PHE   CB  HB3  sing N N 314 
PHE   CG  CD1  doub Y N 315 
PHE   CG  CD2  sing Y N 316 
PHE   CD1 CE1  sing Y N 317 
PHE   CD1 HD1  sing N N 318 
PHE   CD2 CE2  doub Y N 319 
PHE   CD2 HD2  sing N N 320 
PHE   CE1 CZ   doub Y N 321 
PHE   CE1 HE1  sing N N 322 
PHE   CE2 CZ   sing Y N 323 
PHE   CE2 HE2  sing N N 324 
PHE   CZ  HZ   sing N N 325 
PHE   OXT HXT  sing N N 326 
PRO   N   CA   sing N N 327 
PRO   N   CD   sing N N 328 
PRO   N   H    sing N N 329 
PRO   CA  C    sing N N 330 
PRO   CA  CB   sing N N 331 
PRO   CA  HA   sing N N 332 
PRO   C   O    doub N N 333 
PRO   C   OXT  sing N N 334 
PRO   CB  CG   sing N N 335 
PRO   CB  HB2  sing N N 336 
PRO   CB  HB3  sing N N 337 
PRO   CG  CD   sing N N 338 
PRO   CG  HG2  sing N N 339 
PRO   CG  HG3  sing N N 340 
PRO   CD  HD2  sing N N 341 
PRO   CD  HD3  sing N N 342 
PRO   OXT HXT  sing N N 343 
SER   N   CA   sing N N 344 
SER   N   H    sing N N 345 
SER   N   H2   sing N N 346 
SER   CA  C    sing N N 347 
SER   CA  CB   sing N N 348 
SER   CA  HA   sing N N 349 
SER   C   O    doub N N 350 
SER   C   OXT  sing N N 351 
SER   CB  OG   sing N N 352 
SER   CB  HB2  sing N N 353 
SER   CB  HB3  sing N N 354 
SER   OG  HG   sing N N 355 
SER   OXT HXT  sing N N 356 
THR   N   CA   sing N N 357 
THR   N   H    sing N N 358 
THR   N   H2   sing N N 359 
THR   CA  C    sing N N 360 
THR   CA  CB   sing N N 361 
THR   CA  HA   sing N N 362 
THR   C   O    doub N N 363 
THR   C   OXT  sing N N 364 
THR   CB  OG1  sing N N 365 
THR   CB  CG2  sing N N 366 
THR   CB  HB   sing N N 367 
THR   OG1 HG1  sing N N 368 
THR   CG2 HG21 sing N N 369 
THR   CG2 HG22 sing N N 370 
THR   CG2 HG23 sing N N 371 
THR   OXT HXT  sing N N 372 
TRP   N   CA   sing N N 373 
TRP   N   H    sing N N 374 
TRP   N   H2   sing N N 375 
TRP   CA  C    sing N N 376 
TRP   CA  CB   sing N N 377 
TRP   CA  HA   sing N N 378 
TRP   C   O    doub N N 379 
TRP   C   OXT  sing N N 380 
TRP   CB  CG   sing N N 381 
TRP   CB  HB2  sing N N 382 
TRP   CB  HB3  sing N N 383 
TRP   CG  CD1  doub Y N 384 
TRP   CG  CD2  sing Y N 385 
TRP   CD1 NE1  sing Y N 386 
TRP   CD1 HD1  sing N N 387 
TRP   CD2 CE2  doub Y N 388 
TRP   CD2 CE3  sing Y N 389 
TRP   NE1 CE2  sing Y N 390 
TRP   NE1 HE1  sing N N 391 
TRP   CE2 CZ2  sing Y N 392 
TRP   CE3 CZ3  doub Y N 393 
TRP   CE3 HE3  sing N N 394 
TRP   CZ2 CH2  doub Y N 395 
TRP   CZ2 HZ2  sing N N 396 
TRP   CZ3 CH2  sing Y N 397 
TRP   CZ3 HZ3  sing N N 398 
TRP   CH2 HH2  sing N N 399 
TRP   OXT HXT  sing N N 400 
TYR   N   CA   sing N N 401 
TYR   N   H    sing N N 402 
TYR   N   H2   sing N N 403 
TYR   CA  C    sing N N 404 
TYR   CA  CB   sing N N 405 
TYR   CA  HA   sing N N 406 
TYR   C   O    doub N N 407 
TYR   C   OXT  sing N N 408 
TYR   CB  CG   sing N N 409 
TYR   CB  HB2  sing N N 410 
TYR   CB  HB3  sing N N 411 
TYR   CG  CD1  doub Y N 412 
TYR   CG  CD2  sing Y N 413 
TYR   CD1 CE1  sing Y N 414 
TYR   CD1 HD1  sing N N 415 
TYR   CD2 CE2  doub Y N 416 
TYR   CD2 HD2  sing N N 417 
TYR   CE1 CZ   doub Y N 418 
TYR   CE1 HE1  sing N N 419 
TYR   CE2 CZ   sing Y N 420 
TYR   CE2 HE2  sing N N 421 
TYR   CZ  OH   sing N N 422 
TYR   OH  HH   sing N N 423 
TYR   OXT HXT  sing N N 424 
VAL   N   CA   sing N N 425 
VAL   N   H    sing N N 426 
VAL   N   H2   sing N N 427 
VAL   CA  C    sing N N 428 
VAL   CA  CB   sing N N 429 
VAL   CA  HA   sing N N 430 
VAL   C   O    doub N N 431 
VAL   C   OXT  sing N N 432 
VAL   CB  CG1  sing N N 433 
VAL   CB  CG2  sing N N 434 
VAL   CB  HB   sing N N 435 
VAL   CG1 HG11 sing N N 436 
VAL   CG1 HG12 sing N N 437 
VAL   CG1 HG13 sing N N 438 
VAL   CG2 HG21 sing N N 439 
VAL   CG2 HG22 sing N N 440 
VAL   CG2 HG23 sing N N 441 
VAL   OXT HXT  sing N N 442 
# 
_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                    7IAA 
_atom_sites.fract_transf_matrix[1][1]   0.023469 
_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]   0.023469 
_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]   0.004621 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -21.409 19.096  -7.439  1.00 59.23  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.395 18.013  -7.501  1.00 59.25  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.278 17.267  -8.837  1.00 57.64  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.041 17.885  -9.876  1.00 58.75  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.832 18.560  -7.294  1.00 62.23  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.700 17.742  -6.340  1.00 69.08  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.323 18.348  -5.432  1.00 69.46  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.761 16.493  -6.505  1.00 72.71  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.410 15.941  -8.801  1.00 54.87  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.328 15.138  -10.012 1.00 52.54  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.717 14.865  -10.587 1.00 49.89  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.702 14.778  -9.846  1.00 49.33  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.580 13.813  -9.769  1.00 52.52  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.115 13.983  -9.493  1.00 52.96  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.264 12.407  -9.184  1.00 52.65  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.551 13.010  -9.032  1.00 53.56  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.786 14.721  -11.914 1.00 47.77  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.039 14.455  -12.607 1.00 46.67  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.879 13.428  -13.736 1.00 45.03  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.763 13.170  -14.184 1.00 44.14  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.701 15.755  -13.097 1.00 46.73  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.891 16.518  -14.122 1.00 48.16  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -23.966 17.477  -13.732 1.00 49.18  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.090 16.322  -15.484 1.00 49.09  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.214 18.175  -14.670 1.00 50.54  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.368 17.036  -16.431 1.00 49.96  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.433 17.968  -16.020 1.00 51.28  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.682 18.653  -16.949 1.00 53.25  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -25.992 12.819  -14.180 1.00 44.40  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.923 11.831  -15.253 1.00 44.36  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.672 12.314  -16.507 1.00 44.72  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.612 13.123  -16.424 1.00 44.72  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.335 10.399  -14.798 1.00 44.54  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.791 10.340  -14.274 1.00 45.19  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.365 9.869   -13.740 1.00 44.78  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.325 8.911   -14.129 1.00 46.00  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.185 11.876  -17.670 1.00 44.67  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.745 12.196  -18.977 1.00 45.29  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.807 10.944  -19.802 1.00 45.69  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.790 10.256  -19.902 1.00 45.72  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -25.832 13.178  -19.706 1.00 48.24  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.113 14.633  -19.389 1.00 54.21  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.230 15.627  -20.118 1.00 60.92  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.307 15.197  -20.849 1.00 61.63  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.458 16.845  -19.946 1.00 65.06  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -27.947 10.653  -20.442 1.00 46.01  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.035 9.455   -21.281 1.00 46.91  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.092 9.539   -22.481 1.00 47.79  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -26.953 10.611  -23.085 1.00 48.71  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.467 9.171   -21.725 1.00 47.56  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.700 7.682   -21.917 1.00 50.87  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.148 7.359   -22.226 1.00 53.76  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.338 5.928   -22.452 1.00 55.14  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.237 5.341   -23.638 1.00 56.39  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.959 6.058   -24.721 1.00 57.80  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.419 4.031   -23.756 1.00 53.84  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.428 8.434   -22.813 1.00 47.10  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.513 8.411   -23.962 1.00 47.92  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.828 7.324   -25.005 1.00 48.57  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.154 7.275   -26.018 1.00 48.68  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.065 8.287   -23.496 1.00 47.94  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -26.815 6.465   -24.759 1.00 48.67  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.180 5.429   -25.719 1.00 49.06  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.750 4.149   -25.139 1.00 49.28  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -27.809 3.980   -23.923 1.00 48.82  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.221 3.260   -26.013 1.00 49.90  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.767 1.955   -25.645 1.00 51.19  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.638 0.974   -25.458 1.00 52.87  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.574 1.139   -26.062 1.00 53.42  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -29.661 1.398   -26.766 1.00 52.48  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -30.965 2.126   -26.981 1.00 58.73  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.209 3.122   -26.277 1.00 60.57  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.742 1.708   -27.870 1.00 60.65  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -27.884 -0.099  -24.689 1.00 53.25  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -26.882 -1.142  -24.545 1.00 53.87  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.216 -2.282  -25.505 1.00 55.05  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.096 -3.097  -25.223 1.00 54.87  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.713 -1.584  -23.091 1.00 53.26  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.217 -0.393  -22.260 1.00 53.76  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -25.747 -2.740  -23.035 1.00 53.13  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.141 -0.639  -20.825 1.00 54.59  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.551 -2.300  -26.671 0.50 55.54  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.542 -2.310  -26.659 0.50 55.83  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -26.752 -3.322  -27.700 0.50 56.65  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -26.804 -3.288  -27.713 0.50 57.22  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -25.445 -3.740  -28.349 0.50 57.99  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -25.501 -3.701  -28.424 0.50 58.32  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -24.530 -2.933  -28.482 0.50 57.73  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -24.606 -2.874  -28.593 0.50 58.11  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -27.673 -2.821  -28.832 0.50 57.50  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -27.861 -2.678  -28.674 0.50 58.70  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.189 -1.579  -29.354 0.50 57.55  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.095 -2.528  -27.963 0.50 59.69  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.129 -2.742  -28.419 0.50 58.11  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.093 -3.503  -29.930 0.50 58.99  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -25.390 -4.979  -28.833 1.00 59.43  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.228 -5.469  -29.564 1.00 62.47  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.365 -4.956  -31.028 1.00 66.11  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -25.451 -5.032  -31.614 1.00 66.39  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.221 -7.007  -29.522 1.00 62.40  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -23.144 -7.684  -30.327 1.00 62.91  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -23.199 -8.030  -31.648 1.00 63.77  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -21.933 -8.256  -29.815 1.00 63.09  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.057 -8.703  -32.008 1.00 64.03  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -21.273 -8.876  -30.895 1.00 63.89  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.328 -8.279  -28.555 1.00 63.26  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.050 -9.522  -30.744 1.00 64.44  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.117 -8.913  -28.414 1.00 64.07  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -19.484 -9.514  -29.498 1.00 64.29  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.285 -4.402  -31.606 1.00 68.62  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.323 -3.914  -32.987 1.00 71.47  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -22.633 -4.894  -33.903 1.00 74.54  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -21.414 -5.048  -33.800 1.00 74.64  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -22.620 -2.546  -33.124 1.00 74.26  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -22.671 -1.995  -34.549 1.00 81.82  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -21.570 -1.036  -34.968 1.00 89.27  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -20.804 -0.581  -34.087 1.00 91.98  ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -21.472 -0.744  -36.183 1.00 90.65  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.369 -5.512  -34.851 1.00 76.90  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -22.723 -6.408  -35.822 1.00 79.74  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -21.881 -5.530  -36.748 1.00 81.52  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.318 -4.440  -37.109 1.00 82.35  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -23.750 -7.190  -36.652 1.00 82.87  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -24.867 -7.836  -35.838 1.00 88.97  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -25.927 -8.431  -36.782 1.00 94.56  ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -27.139 -8.977  -36.064 1.00 98.88  ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -28.126 -9.540  -37.024 1.00 101.81 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -20.657 -5.944  -37.041 1.00 82.17  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -19.748 -5.149  -37.861 1.00 83.44  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.260 -3.889  -37.143 1.00 83.10  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -19.286 -2.797  -37.702 1.00 83.51  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -20.327 -4.831  -39.255 1.00 87.01  ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -20.467 -6.065  -40.116 1.00 94.78  ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -19.517 -6.883  -40.140 1.00 96.55  ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -21.530 -6.223  -40.757 1.00 98.17  ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -18.810 -4.055  -35.900 1.00 82.35  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.184 -2.989  -35.123 1.00 81.89  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -16.646 -3.084  -35.372 1.00 81.21  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -16.173 -4.080  -35.940 1.00 81.17  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -18.499 -3.175  -33.640 1.00 81.97  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -15.869 -2.056  -34.972 1.00 80.43  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -14.410 -2.102  -35.149 1.00 80.00  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -13.802 -3.171  -34.217 1.00 77.88  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -13.979 -3.096  -33.009 1.00 77.12  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -13.777 -0.725  -34.869 1.00 83.40  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -12.270 -0.707  -35.078 1.00 89.20  ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -11.508 0.350   -34.300 1.00 95.84  ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -12.159 1.212   -33.664 1.00 97.17  ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -10.255 0.312   -34.325 1.00 96.99  ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -13.127 -4.182  -34.792 1.00 76.44  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -12.502 -5.278  -34.035 1.00 75.33  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.016 -4.953  -33.829 1.00 74.03  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.283 -4.830  -34.809 1.00 74.50  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -12.683 -6.677  -34.697 1.00 75.98  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.479 -7.786  -33.682 1.00 76.25  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.048 -6.824  -35.374 1.00 76.83  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -10.574 -4.793  -32.567 1.00 72.44  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -9.188  -4.431  -32.231 1.00 71.73  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -8.817  -4.915  -30.798 1.00 71.13  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -9.674  -5.386  -30.069 1.00 70.52  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.004  -2.897  -32.387 1.00 73.20  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -7.626  -2.582  -32.593 1.00 74.26  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -9.544  -2.122  -31.203 1.00 73.41  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -7.544  -4.820  -30.428 1.00 70.59  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.088  -5.200  -29.108 1.00 70.21  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -6.586  -6.620  -29.024 1.00 70.17  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.107  -7.517  -29.689 1.00 70.30  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -5.584  -6.825  -28.171 1.00 69.75  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -4.988  -8.134  -27.945 1.00 69.46  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -5.635  -8.862  -26.724 1.00 67.01  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.625  -8.373  -26.181 1.00 66.59  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.453  -8.006  -27.865 1.00 72.22  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -2.938  -7.224  -26.682 1.00 77.42  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.318  -6.073  -26.444 1.00 78.92  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.025  -7.834  -25.930 1.00 79.20  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.148  -10.072 -26.368 1.00 65.40  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -5.665  -10.906 -25.276 1.00 64.04  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.508  -11.390 -24.349 1.00 61.87  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.184  -12.584 -24.325 1.00 61.61  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.387  -12.125 -25.856 1.00 66.20  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.290  -11.810 -26.899 1.00 69.61  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -3.853  -10.491 -23.594 1.00 60.24  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -2.721  -10.935 -22.754 1.00 59.18  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.136  -11.737 -21.531 1.00 57.67  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.207  -11.499 -20.989 1.00 56.68  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.061  -9.619  -22.342 1.00 60.12  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.206  -8.636  -22.313 1.00 60.86  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.086  -9.038  -23.468 1.00 59.58  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.282  -12.688 -21.101 1.00 57.47  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.482  -13.482 -19.880 1.00 57.63  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.533  -12.864 -18.859 1.00 56.74  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.325  -12.972 -19.022 1.00 57.17  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.124  -14.959 -20.122 1.00 59.51  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -2.985  -15.591 -21.204 1.00 63.60  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.234  -17.067 -20.955 1.00 68.63  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -3.798  -17.725 -22.140 1.00 72.70  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.100  -17.873 -22.366 1.00 74.58  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -5.991  -17.415 -21.491 1.00 75.08  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.522  -18.486 -23.465 1.00 72.99  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.060  -12.147 -17.864 1.00 55.53  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.217  -11.419 -16.912 1.00 54.68  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.346  -11.881 -15.488 1.00 54.32  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.458  -12.073 -15.038 1.00 54.11  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.578  -9.919  -16.970 1.00 53.87  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.476  -9.267  -18.341 1.00 53.79  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -1.964  -7.842  -18.295 1.00 53.75  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.030  -9.333  -18.864 1.00 53.84  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.238  -11.955 -14.743 1.00 53.97  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.299  -12.280 -13.314 1.00 54.59  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.494  -10.967 -12.548 1.00 53.56  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.337   -10.066 -12.676 1.00 53.93  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.982   -12.972 -12.842 1.00 57.49  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 1.049   -14.459 -13.133 1.00 66.03  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.193   -14.956 -13.892 1.00 67.88  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 1.965   -15.125 -12.605 1.00 69.95  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.621  -10.816 -11.830 1.00 51.74  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -1.903  -9.562  -11.130 1.00 50.96  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.261  -9.768  -9.651  1.00 50.05  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.702  -10.851 -9.259  1.00 50.13  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -2.999  -8.698  -11.842 1.00 51.10  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.639  -8.374  -13.292 1.00 51.08  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.358  -9.368  -11.759 1.00 51.54  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.082  -8.713  -8.836  1.00 48.86  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.465  -8.713  -7.425  1.00 48.14  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.442  -7.562  -7.185  1.00 47.08  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.298  -6.514  -7.804  1.00 47.44  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.248  -8.580  -6.515  1.00 48.30  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.444  -7.764  -6.313  1.00 45.28  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.455  -6.752  -6.007  1.00 43.93  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.342  -6.347  -4.529  1.00 45.11  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.496  -7.198  -3.622  1.00 45.33  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.850  -7.305  -6.322  1.00 42.47  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.039  -6.389  -5.997  1.00 41.84  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.003  -5.131  -6.791  1.00 40.36  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.378  -7.119  -6.159  1.00 42.38  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -4.987  -5.074  -4.277  1.00 44.98  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -4.812  -4.631  -2.898  1.00 45.81  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.166  -4.217  -2.260  1.00 46.61  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.203  -4.194  -2.940  1.00 46.98  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.694  -3.554  -2.777  1.00 47.33  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -3.996  -2.164  -3.334  1.00 50.56  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.177  -1.875  -3.596  1.00 50.55  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.042  -1.355  -3.476  1.00 52.57  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.155  -3.928  -0.948  1.00 46.66  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.333  -3.520  -0.202  1.00 47.14  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -7.971  -2.231  -0.738  1.00 46.78  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.163  -2.024  -0.557  1.00 47.25  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.980  -3.392  1.292   1.00 50.20  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.164  -3.536  2.231   1.00 55.77  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.806  -3.384  3.695   1.00 62.26  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.610  -2.230  4.143   1.00 62.35  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.692  -4.422  4.388   1.00 65.14  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.203  -1.383  -1.427  1.00 45.97  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.737  -0.143  -1.993  1.00 45.34  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.418  -0.319  -3.354  1.00 43.69  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.810  0.680   -3.965  1.00 43.07  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.627  0.890   -2.128  1.00 47.02  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.051  1.148   -0.861  1.00 49.83  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.527  -1.552  -3.847  1.00 42.85  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.117  -1.794  -5.163  1.00 42.41  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.170  -1.531  -6.321  1.00 42.13  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.605  -1.436  -7.469  1.00 41.67  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.851  -1.476  -6.050  1.00 42.41  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.855  -1.231  -7.098  1.00 42.73  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.127  -2.504  -7.568  1.00 42.64  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.508  -3.204  -6.762  1.00 41.88  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.819  -0.199  -6.618  1.00 43.78  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.393  1.179   -6.397  1.00 48.06  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.288  1.566   -7.139  1.00 50.01  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -4.933  1.867   -5.487  1.00 51.41  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.183  -2.787  -8.881  1.00 42.75  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.468  -3.918  -9.469  1.00 43.20  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.012  -3.539  -9.703  1.00 45.69  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.677  -2.366  -9.919  1.00 45.35  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.094  -4.353  -10.808 1.00 41.96  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.422  -5.068  -10.696 1.00 41.67  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.483  -6.398  -10.305 1.00 41.99  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.609  -4.414  -10.994 1.00 41.42  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.708  -7.055  -10.223 1.00 42.07  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.828  -5.073  -10.893 1.00 41.06  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.867  -6.385  -10.523 1.00 41.03  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.143  -4.536  -9.646  1.00 47.82  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.716  -4.365  -9.903  1.00 50.55  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.157  -5.610  -10.597 1.00 53.60  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.702  -6.697  -10.421 1.00 53.35  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? 0.042   -4.113  -8.609  1.00 52.02  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.220  -5.143  -7.669  1.00 54.71  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.935   -5.464  -11.378 1.00 56.03  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.538   -6.615  -12.047 1.00 58.62  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.471   -7.368  -11.124 1.00 60.68  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.400   -6.785  -10.563 1.00 60.41  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.326   -6.202  -13.301 1.00 59.53  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.508   -5.832  -14.528 1.00 62.30  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.425   -5.421  -15.660 1.00 63.44  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.641   -7.000  -14.984 1.00 63.19  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.262   -8.678  -11.018 1.00 62.75  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.124   -9.572  -10.245 1.00 65.45  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.128   -10.181 -11.215 1.00 68.62  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.726   -10.680 -12.270 1.00 69.36  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.290   -10.678 -9.569  1.00 65.86  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.189   -11.721 -8.917  1.00 66.62  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.321   -10.080 -8.558  1.00 66.07  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.427   -10.092 -10.915 1.00 70.34  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.447   -10.679 -11.788 1.00 72.62  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.498   -11.460 -10.984 1.00 73.52  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.152   -12.248 -10.099 1.00 73.94  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.112   -9.620  -12.691 1.00 76.32  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.137   -8.756  -13.483 1.00 82.90  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 6.005   -9.126  -14.949 1.00 90.08  ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 7.022   -9.543  -15.551 1.00 90.99  ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 4.887   -8.990  -15.497 1.00 92.52  ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -35.496 11.359  -11.878 1.00 63.93  ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.638 11.924  -13.216 1.00 64.39  ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.591 10.887  -14.328 1.00 64.33  ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.581 10.182  -14.570 1.00 65.09  ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.437 10.769  -15.013 1.00 62.90  ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.292 9.800   -16.095 1.00 61.74  ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -33.951 8.390   -15.579 1.00 60.60  ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -32.832 8.146   -15.117 1.00 61.20  ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -33.245 10.275  -17.112 1.00 63.15  ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -33.415 9.642   -18.476 1.00 66.34  ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -32.473 10.165  -19.544 1.00 72.75  ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -31.569 10.971  -19.220 1.00 73.52  ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -32.667 9.788   -20.721 1.00 75.17  ? 17  GLU   B OE2 1 
ATOM   325  N  N   A THR   B 2 9   ? -34.910 7.460   -15.651 0.50 59.60  ? 18  THR   B N   1 
ATOM   326  N  N   B THR   B 2 9   ? -34.918 7.475   -15.667 0.50 59.54  ? 18  THR   B N   1 
ATOM   327  C  CA  A THR   B 2 9   ? -34.666 6.080   -15.207 0.50 58.99  ? 18  THR   B CA  1 
ATOM   328  C  CA  B THR   B 2 9   ? -34.758 6.093   -15.212 0.50 58.86  ? 18  THR   B CA  1 
ATOM   329  C  C   A THR   B 2 9   ? -34.635 5.067   -16.356 0.50 57.80  ? 18  THR   B C   1 
ATOM   330  C  C   B THR   B 2 9   ? -34.587 5.084   -16.350 0.50 57.72  ? 18  THR   B C   1 
ATOM   331  O  O   A THR   B 2 9   ? -34.575 3.866   -16.095 0.50 57.90  ? 18  THR   B O   1 
ATOM   332  O  O   B THR   B 2 9   ? -34.434 3.894   -16.075 0.50 57.81  ? 18  THR   B O   1 
ATOM   333  C  CB  A THR   B 2 9   ? -35.623 5.623   -14.092 0.50 60.57  ? 18  THR   B CB  1 
ATOM   334  C  CB  B THR   B 2 9   ? -35.979 5.686   -14.377 0.50 60.30  ? 18  THR   B CB  1 
ATOM   335  O  OG1 A THR   B 2 9   ? -36.901 6.265   -14.209 0.50 62.02  ? 18  THR   B OG1 1 
ATOM   336  O  OG1 B THR   B 2 9   ? -37.130 5.601   -15.230 0.50 61.25  ? 18  THR   B OG1 1 
ATOM   337  C  CG2 A THR   B 2 9   ? -35.034 5.830   -12.698 0.50 60.92  ? 18  THR   B CG2 1 
ATOM   338  C  CG2 B THR   B 2 9   ? -36.252 6.655   -13.232 0.50 60.91  ? 18  THR   B CG2 1 
ATOM   339  N  N   . THR   B 2 10  ? -34.656 5.532   -17.613 1.00 56.52  ? 19  THR   B N   1 
ATOM   340  C  CA  . THR   B 2 10  ? -34.584 4.655   -18.775 1.00 54.77  ? 19  THR   B CA  1 
ATOM   341  C  C   . THR   B 2 10  ? -33.324 3.789   -18.764 1.00 51.83  ? 19  THR   B C   1 
ATOM   342  O  O   . THR   B 2 10  ? -32.253 4.301   -18.451 1.00 51.83  ? 19  THR   B O   1 
ATOM   343  C  CB  . THR   B 2 10  ? -34.583 5.512   -20.060 1.00 56.83  ? 19  THR   B CB  1 
ATOM   344  O  OG1 . THR   B 2 10  ? -35.676 6.445   -20.029 1.00 59.66  ? 19  THR   B OG1 1 
ATOM   345  C  CG2 . THR   B 2 10  ? -34.650 4.665   -21.320 1.00 56.56  ? 19  THR   B CG2 1 
ATOM   346  N  N   . ASP   B 2 11  ? -33.442 2.488   -19.099 1.00 49.41  ? 20  ASP   B N   1 
ATOM   347  C  CA  . ASP   B 2 11  ? -32.291 1.594   -19.222 1.00 48.72  ? 20  ASP   B CA  1 
ATOM   348  C  C   . ASP   B 2 11  ? -31.302 2.177   -20.279 1.00 48.00  ? 20  ASP   B C   1 
ATOM   349  O  O   . ASP   B 2 11  ? -31.740 2.869   -21.198 1.00 48.63  ? 20  ASP   B O   1 
ATOM   350  C  CB  . ASP   B 2 11  ? -32.756 0.206   -19.709 1.00 50.47  ? 20  ASP   B CB  1 
ATOM   351  C  CG  . ASP   B 2 11  ? -33.276 -0.764  -18.661 1.00 55.97  ? 20  ASP   B CG  1 
ATOM   352  O  OD1 . ASP   B 2 11  ? -33.658 -0.300  -17.550 1.00 55.28  ? 20  ASP   B OD1 1 
ATOM   353  O  OD2 . ASP   B 2 11  ? -33.305 -1.995  -18.952 1.00 58.01  ? 20  ASP   B OD2 1 
ATOM   354  N  N   . GLY   B 2 12  ? -30.010 1.889   -20.154 1.00 46.17  ? 21  GLY   B N   1 
ATOM   355  C  CA  . GLY   B 2 12  ? -29.028 2.403   -21.100 1.00 44.56  ? 21  GLY   B CA  1 
ATOM   356  C  C   . GLY   B 2 12  ? -27.708 2.773   -20.459 1.00 42.99  ? 21  GLY   B C   1 
ATOM   357  O  O   . GLY   B 2 12  ? -27.481 2.492   -19.278 1.00 41.82  ? 21  GLY   B O   1 
ATOM   358  N  N   . VAL   B 2 13  ? -26.814 3.380   -21.255 1.00 41.89  ? 22  VAL   B N   1 
ATOM   359  C  CA  . VAL   B 2 13  ? -25.492 3.811   -20.789 1.00 40.71  ? 22  VAL   B CA  1 
ATOM   360  C  C   . VAL   B 2 13  ? -25.548 5.341   -20.592 1.00 40.32  ? 22  VAL   B C   1 
ATOM   361  O  O   . VAL   B 2 13  ? -26.242 6.035   -21.334 1.00 40.42  ? 22  VAL   B O   1 
ATOM   362  C  CB  . VAL   B 2 13  ? -24.344 3.314   -21.721 1.00 40.53  ? 22  VAL   B CB  1 
ATOM   363  C  CG1 . VAL   B 2 13  ? -24.431 3.920   -23.136 1.00 40.03  ? 22  VAL   B CG1 1 
ATOM   364  C  CG2 . VAL   B 2 13  ? -22.984 3.556   -21.106 1.00 40.44  ? 22  VAL   B CG2 1 
ATOM   365  N  N   . TYR   B 2 14  ? -24.937 5.842   -19.515 1.00 39.61  ? 23  TYR   B N   1 
ATOM   366  C  CA  . TYR   B 2 14  ? -24.996 7.255   -19.147 1.00 39.27  ? 23  TYR   B CA  1 
ATOM   367  C  C   . TYR   B 2 14  ? -23.604 7.815   -18.893 1.00 39.73  ? 23  TYR   B C   1 
ATOM   368  O  O   . TYR   B 2 14  ? -22.735 7.097   -18.428 1.00 40.01  ? 23  TYR   B O   1 
ATOM   369  C  CB  . TYR   B 2 14  ? -25.785 7.390   -17.823 1.00 39.04  ? 23  TYR   B CB  1 
ATOM   370  C  CG  . TYR   B 2 14  ? -27.279 7.233   -17.983 1.00 39.21  ? 23  TYR   B CG  1 
ATOM   371  C  CD1 . TYR   B 2 14  ? -27.840 6.003   -18.296 1.00 39.42  ? 23  TYR   B CD1 1 
ATOM   372  C  CD2 . TYR   B 2 14  ? -28.128 8.324   -17.853 1.00 40.47  ? 23  TYR   B CD2 1 
ATOM   373  C  CE1 . TYR   B 2 14  ? -29.201 5.870   -18.533 1.00 40.77  ? 23  TYR   B CE1 1 
ATOM   374  C  CE2 . TYR   B 2 14  ? -29.494 8.205   -18.092 1.00 41.97  ? 23  TYR   B CE2 1 
ATOM   375  C  CZ  . TYR   B 2 14  ? -30.031 6.970   -18.415 1.00 42.64  ? 23  TYR   B CZ  1 
ATOM   376  O  OH  . TYR   B 2 14  ? -31.394 6.831   -18.558 1.00 44.46  ? 23  TYR   B OH  1 
ATOM   377  N  N   . ARG   B 2 15  ? -23.419 9.109   -19.099 1.00 39.76  ? 24  ARG   B N   1 
ATOM   378  C  CA  . ARG   B 2 15  ? -22.171 9.784   -18.756 1.00 39.76  ? 24  ARG   B CA  1 
ATOM   379  C  C   . ARG   B 2 15  ? -22.317 10.276  -17.331 1.00 39.78  ? 24  ARG   B C   1 
ATOM   380  O  O   . ARG   B 2 15  ? -23.395 10.708  -16.949 1.00 39.96  ? 24  ARG   B O   1 
ATOM   381  C  CB  . ARG   B 2 15  ? -21.946 11.018  -19.645 1.00 40.55  ? 24  ARG   B CB  1 
ATOM   382  C  CG  . ARG   B 2 15  ? -21.763 10.715  -21.124 1.00 41.56  ? 24  ARG   B CG  1 
ATOM   383  C  CD  . ARG   B 2 15  ? -21.628 12.009  -21.921 1.00 43.97  ? 24  ARG   B CD  1 
ATOM   384  N  NE  . ARG   B 2 15  ? -21.850 11.776  -23.352 1.00 46.59  ? 24  ARG   B NE  1 
ATOM   385  C  CZ  . ARG   B 2 15  ? -20.911 11.392  -24.214 1.00 48.35  ? 24  ARG   B CZ  1 
ATOM   386  N  NH1 . ARG   B 2 15  ? -19.652 11.244  -23.816 1.00 47.64  ? 24  ARG   B NH1 1 
ATOM   387  N  NH2 . ARG   B 2 15  ? -21.223 11.161  -25.482 1.00 47.31  ? 24  ARG   B NH2 1 
ATOM   388  N  N   . VAL   B 2 16  ? -21.236 10.242  -16.547 1.00 39.73  ? 25  VAL   B N   1 
ATOM   389  C  CA  . VAL   B 2 16  ? -21.226 10.784  -15.189 1.00 39.20  ? 25  VAL   B CA  1 
ATOM   390  C  C   . VAL   B 2 16  ? -20.397 12.059  -15.301 1.00 38.99  ? 25  VAL   B C   1 
ATOM   391  O  O   . VAL   B 2 16  ? -19.214 12.008  -15.648 1.00 38.87  ? 25  VAL   B O   1 
ATOM   392  C  CB  . VAL   B 2 16  ? -20.626 9.812   -14.141 1.00 39.45  ? 25  VAL   B CB  1 
ATOM   393  C  CG1 . VAL   B 2 16  ? -20.701 10.414  -12.742 1.00 39.81  ? 25  VAL   B CG1 1 
ATOM   394  C  CG2 . VAL   B 2 16  ? -21.305 8.455   -14.193 1.00 39.45  ? 25  VAL   B CG2 1 
ATOM   395  N  N   . MET   B 2 17  ? -21.037 13.189  -15.107 1.00 39.53  ? 26  MET   B N   1 
ATOM   396  C  CA  . MET   B 2 17  ? -20.434 14.498  -15.268 1.00 41.21  ? 26  MET   B CA  1 
ATOM   397  C  C   . MET   B 2 17  ? -20.299 15.239  -13.948 1.00 44.33  ? 26  MET   B C   1 
ATOM   398  O  O   . MET   B 2 17  ? -20.977 14.918  -12.983 1.00 44.38  ? 26  MET   B O   1 
ATOM   399  C  CB  . MET   B 2 17  ? -21.325 15.351  -16.197 1.00 41.22  ? 26  MET   B CB  1 
ATOM   400  C  CG  . MET   B 2 17  ? -21.760 14.663  -17.483 1.00 42.23  ? 26  MET   B CG  1 
ATOM   401  S  SD  . MET   B 2 17  ? -20.407 14.537  -18.656 1.00 45.64  ? 26  MET   B SD  1 
ATOM   402  C  CE  . MET   B 2 17  ? -20.168 16.273  -19.038 1.00 44.22  ? 26  MET   B CE  1 
ATOM   403  N  N   . THR   B 2 18  ? -19.458 16.278  -13.933 1.00 46.69  ? 27  THR   B N   1 
ATOM   404  C  CA  . THR   B 2 18  ? -19.312 17.193  -12.815 1.00 49.32  ? 27  THR   B CA  1 
ATOM   405  C  C   . THR   B 2 18  ? -19.126 18.633  -13.307 1.00 52.06  ? 27  THR   B C   1 
ATOM   406  O  O   . THR   B 2 18  ? -18.605 18.868  -14.394 1.00 51.31  ? 27  THR   B O   1 
ATOM   407  C  CB  . THR   B 2 18  ? -18.202 16.797  -11.832 1.00 50.42  ? 27  THR   B CB  1 
ATOM   408  O  OG1 . THR   B 2 18  ? -18.351 17.631  -10.672 1.00 51.79  ? 27  THR   B OG1 1 
ATOM   409  C  CG2 . THR   B 2 18  ? -16.791 16.968  -12.417 1.00 50.10  ? 27  THR   B CG2 1 
ATOM   410  N  N   . ARG   B 2 19  ? -19.540 19.594  -12.486 1.00 54.91  ? 28  ARG   B N   1 
ATOM   411  C  CA  . ARG   B 2 19  ? -19.335 21.004  -12.790 1.00 58.35  ? 28  ARG   B CA  1 
ATOM   412  C  C   . ARG   B 2 19  ? -18.324 21.676  -11.816 1.00 60.77  ? 28  ARG   B C   1 
ATOM   413  O  O   . ARG   B 2 19  ? -18.134 22.886  -11.884 1.00 61.22  ? 28  ARG   B O   1 
ATOM   414  C  CB  . ARG   B 2 19  ? -20.672 21.765  -12.878 1.00 61.08  ? 28  ARG   B CB  1 
ATOM   415  C  CG  . ARG   B 2 19  ? -21.502 21.375  -14.109 1.00 66.68  ? 28  ARG   B CG  1 
ATOM   416  C  CD  . ARG   B 2 19  ? -22.508 22.449  -14.500 1.00 72.01  ? 28  ARG   B CD  1 
ATOM   417  N  NE  . ARG   B 2 19  ? -23.444 22.019  -15.549 1.00 76.29  ? 28  ARG   B NE  1 
ATOM   418  C  CZ  . ARG   B 2 19  ? -24.686 21.591  -15.317 1.00 78.97  ? 28  ARG   B CZ  1 
ATOM   419  N  NH1 . ARG   B 2 19  ? -25.145 21.499  -14.072 1.00 78.85  ? 28  ARG   B NH1 1 
ATOM   420  N  NH2 . ARG   B 2 19  ? -25.470 21.228  -16.328 1.00 78.38  ? 28  ARG   B NH2 1 
ATOM   421  N  N   . ARG   B 2 20  ? -17.643 20.877  -10.958 1.00 62.29  ? 29  ARG   B N   1 
ATOM   422  C  CA  . ARG   B 2 20  ? -16.661 21.316  -9.963  1.00 64.19  ? 29  ARG   B CA  1 
ATOM   423  C  C   . ARG   B 2 20  ? -15.352 21.830  -10.583 1.00 64.53  ? 29  ARG   B C   1 
ATOM   424  O  O   . ARG   B 2 20  ? -14.767 22.789  -10.084 1.00 65.33  ? 29  ARG   B O   1 
ATOM   425  C  CB  . ARG   B 2 20  ? -16.362 20.173  -8.977  1.00 67.07  ? 29  ARG   B CB  1 
ATOM   426  C  CG  . ARG   B 2 20  ? -15.638 20.624  -7.717  1.00 73.25  ? 29  ARG   B CG  1 
ATOM   427  C  CD  . ARG   B 2 20  ? -15.295 19.453  -6.814  1.00 79.18  ? 29  ARG   B CD  1 
ATOM   428  N  NE  . ARG   B 2 20  ? -14.226 18.615  -7.367  1.00 84.37  ? 29  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   B 2 20  ? -12.954 18.665  -6.975  1.00 88.03  ? 29  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   B 2 20  ? -12.575 19.517  -6.027  1.00 88.24  ? 29  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   B 2 20  ? -12.052 17.858  -7.525  1.00 87.98  ? 29  ARG   B NH2 1 
ATOM   432  N  N   . LEU   B 2 21  ? -14.893 21.202  -11.662 1.00 63.77  ? 30  LEU   B N   1 
ATOM   433  C  CA  . LEU   B 2 21  ? -13.655 21.606  -12.331 1.00 63.24  ? 30  LEU   B CA  1 
ATOM   434  C  C   . LEU   B 2 21  ? -13.968 22.684  -13.428 1.00 62.35  ? 30  LEU   B C   1 
ATOM   435  O  O   . LEU   B 2 21  ? -14.987 23.381  -13.323 1.00 62.74  ? 30  LEU   B O   1 
ATOM   436  C  CB  . LEU   B 2 21  ? -12.994 20.333  -12.910 1.00 63.54  ? 30  LEU   B CB  1 
ATOM   437  C  CG  . LEU   B 2 21  ? -12.058 19.489  -12.014 1.00 65.48  ? 30  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   B 2 21  ? -12.547 19.377  -10.584 1.00 66.14  ? 30  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   B 2 21  ? -11.864 18.090  -12.595 1.00 66.13  ? 30  LEU   B CD2 1 
ATOM   440  N  N   . LEU   B 2 22  ? -13.100 22.853  -14.449 1.00 60.93  ? 31  LEU   B N   1 
ATOM   441  C  CA  . LEU   B 2 22  ? -13.354 23.815  -15.519 1.00 59.80  ? 31  LEU   B CA  1 
ATOM   442  C  C   . LEU   B 2 22  ? -14.490 23.300  -16.404 1.00 58.73  ? 31  LEU   B C   1 
ATOM   443  O  O   . LEU   B 2 22  ? -14.522 22.108  -16.712 1.00 58.80  ? 31  LEU   B O   1 
ATOM   444  C  CB  . LEU   B 2 22  ? -12.100 23.982  -16.366 1.00 59.51  ? 31  LEU   B CB  1 
ATOM   445  C  CG  . LEU   B 2 22  ? -12.209 25.066  -17.385 1.00 60.16  ? 31  LEU   B CG  1 
ATOM   446  C  CD1 . LEU   B 2 22  ? -12.120 26.429  -16.727 1.00 60.57  ? 31  LEU   B CD1 1 
ATOM   447  C  CD2 . LEU   B 2 22  ? -11.204 24.867  -18.502 1.00 60.65  ? 31  LEU   B CD2 1 
ATOM   448  N  N   . GLY   B 2 23  ? -15.427 24.175  -16.770 1.00 57.35  ? 32  GLY   B N   1 
ATOM   449  C  CA  . GLY   B 2 23  ? -16.579 23.813  -17.593 1.00 56.65  ? 32  GLY   B CA  1 
ATOM   450  C  C   . GLY   B 2 23  ? -17.359 22.625  -17.063 1.00 55.90  ? 32  GLY   B C   1 
ATOM   451  O  O   . GLY   B 2 23  ? -17.621 22.526  -15.862 1.00 56.02  ? 32  GLY   B O   1 
ATOM   452  N  N   . SER   B 2 24  ? -17.665 21.679  -17.947 1.00 54.94  ? 33  SER   B N   1 
ATOM   453  C  CA  . SER   B 2 24  ? -18.330 20.435  -17.578 1.00 54.22  ? 33  SER   B CA  1 
ATOM   454  C  C   . SER   B 2 24  ? -17.354 19.320  -17.887 1.00 52.47  ? 33  SER   B C   1 
ATOM   455  O  O   . SER   B 2 24  ? -16.799 19.268  -18.984 1.00 52.30  ? 33  SER   B O   1 
ATOM   456  C  CB  . SER   B 2 24  ? -19.625 20.249  -18.361 1.00 56.38  ? 33  SER   B CB  1 
ATOM   457  O  OG  . SER   B 2 24  ? -20.561 21.255  -18.011 1.00 59.85  ? 33  SER   B OG  1 
ATOM   458  N  N   . THR   B 2 25  ? -17.107 18.448  -16.912 1.00 51.06  ? 34  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 25  ? -16.124 17.383  -17.076 1.00 50.25  ? 34  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 25  ? -16.707 15.995  -16.880 1.00 48.98  ? 34  THR   B C   1 
ATOM   461  O  O   . THR   B 2 25  ? -17.411 15.754  -15.897 1.00 49.42  ? 34  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 25  ? -14.929 17.632  -16.142 1.00 51.78  ? 34  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 25  ? -14.498 19.001  -16.241 1.00 52.54  ? 34  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 25  ? -13.764 16.692  -16.425 1.00 52.00  ? 34  THR   B CG2 1 
ATOM   465  N  N   . GLN   B 2 26  ? -16.378 15.065  -17.782 1.00 47.22  ? 35  GLN   B N   1 
ATOM   466  C  CA  . GLN   B 2 26  ? -16.839 13.686  -17.640 1.00 46.32  ? 35  GLN   B CA  1 
ATOM   467  C  C   . GLN   B 2 26  ? -15.830 12.879  -16.798 1.00 46.50  ? 35  GLN   B C   1 
ATOM   468  O  O   . GLN   B 2 26  ? -14.687 12.693  -17.221 1.00 46.91  ? 35  GLN   B O   1 
ATOM   469  C  CB  . GLN   B 2 26  ? -17.038 13.031  -19.005 1.00 44.80  ? 35  GLN   B CB  1 
ATOM   470  C  CG  . GLN   B 2 26  ? -17.467 11.585  -18.885 1.00 43.31  ? 35  GLN   B CG  1 
ATOM   471  C  CD  . GLN   B 2 26  ? -17.793 11.017  -20.223 1.00 40.61  ? 35  GLN   B CD  1 
ATOM   472  O  OE1 . GLN   B 2 26  ? -18.394 11.685  -21.065 1.00 39.57  ? 35  GLN   B OE1 1 
ATOM   473  N  NE2 . GLN   B 2 26  ? -17.387 9.777   -20.451 1.00 37.27  ? 35  GLN   B NE2 1 
ATOM   474  N  N   . VAL   B 2 27  ? -16.252 12.426  -15.610 1.00 45.39  ? 36  VAL   B N   1 
ATOM   475  C  CA  . VAL   B 2 27  ? -15.405 11.669  -14.686 1.00 44.52  ? 36  VAL   B CA  1 
ATOM   476  C  C   . VAL   B 2 27  ? -15.530 10.133  -14.862 1.00 43.04  ? 36  VAL   B C   1 
ATOM   477  O  O   . VAL   B 2 27  ? -14.611 9.382   -14.530 1.00 42.87  ? 36  VAL   B O   1 
ATOM   478  C  CB  . VAL   B 2 27  ? -15.647 12.122  -13.226 1.00 45.94  ? 36  VAL   B CB  1 
ATOM   479  C  CG1 . VAL   B 2 27  ? -15.157 13.553  -13.040 1.00 46.96  ? 36  VAL   B CG1 1 
ATOM   480  C  CG2 . VAL   B 2 27  ? -17.125 12.011  -12.832 1.00 45.66  ? 36  VAL   B CG2 1 
ATOM   481  N  N   . GLY   B 2 28  ? -16.636 9.690   -15.438 1.00 41.28  ? 37  GLY   B N   1 
ATOM   482  C  CA  . GLY   B 2 28  ? -16.861 8.283   -15.695 1.00 40.13  ? 37  GLY   B CA  1 
ATOM   483  C  C   . GLY   B 2 28  ? -18.148 8.054   -16.454 1.00 39.31  ? 37  GLY   B C   1 
ATOM   484  O  O   . GLY   B 2 28  ? -18.726 8.984   -17.014 1.00 39.23  ? 37  GLY   B O   1 
ATOM   485  N  N   . VAL   B 2 29  ? -18.600 6.797   -16.469 1.00 38.31  ? 38  VAL   B N   1 
ATOM   486  C  CA  . VAL   B 2 29  ? -19.777 6.299   -17.188 1.00 37.71  ? 38  VAL   B CA  1 
ATOM   487  C  C   . VAL   B 2 29  ? -20.498 5.265   -16.279 1.00 37.77  ? 38  VAL   B C   1 
ATOM   488  O  O   . VAL   B 2 29  ? -19.880 4.651   -15.392 1.00 37.63  ? 38  VAL   B O   1 
ATOM   489  C  CB  . VAL   B 2 29  ? -19.284 5.626   -18.512 1.00 37.50  ? 38  VAL   B CB  1 
ATOM   490  C  CG1 . VAL   B 2 29  ? -20.375 4.832   -19.212 1.00 38.15  ? 38  VAL   B CG1 1 
ATOM   491  C  CG2 . VAL   B 2 29  ? -18.675 6.631   -19.474 1.00 37.89  ? 38  VAL   B CG2 1 
ATOM   492  N  N   . GLY   B 2 30  ? -21.776 5.026   -16.553 1.00 37.65  ? 39  GLY   B N   1 
ATOM   493  C  CA  . GLY   B 2 30  ? -22.521 4.010   -15.831 1.00 37.79  ? 39  GLY   B CA  1 
ATOM   494  C  C   . GLY   B 2 30  ? -23.619 3.348   -16.631 1.00 37.62  ? 39  GLY   B C   1 
ATOM   495  O  O   . GLY   B 2 30  ? -23.949 3.783   -17.744 1.00 37.15  ? 39  GLY   B O   1 
ATOM   496  N  N   . VAL   B 2 31  ? -24.222 2.306   -16.033 1.00 37.01  ? 40  VAL   B N   1 
ATOM   497  C  CA  . VAL   B 2 31  ? -25.298 1.542   -16.642 1.00 37.17  ? 40  VAL   B CA  1 
ATOM   498  C  C   . VAL   B 2 31  ? -26.584 1.670   -15.828 1.00 36.81  ? 40  VAL   B C   1 
ATOM   499  O  O   . VAL   B 2 31  ? -26.587 1.378   -14.632 1.00 36.16  ? 40  VAL   B O   1 
ATOM   500  C  CB  . VAL   B 2 31  ? -24.896 0.045   -16.765 1.00 38.55  ? 40  VAL   B CB  1 
ATOM   501  C  CG1 . VAL   B 2 31  ? -26.058 -0.797  -17.258 1.00 39.74  ? 40  VAL   B CG1 1 
ATOM   502  C  CG2 . VAL   B 2 31  ? -23.686 -0.129  -17.674 1.00 38.73  ? 40  VAL   B CG2 1 
ATOM   503  N  N   . MET   B 2 32  ? -27.677 2.096   -16.464 1.00 36.77  ? 41  MET   B N   1 
ATOM   504  C  CA  . MET   B 2 32  ? -28.967 2.120   -15.793 1.00 37.10  ? 41  MET   B CA  1 
ATOM   505  C  C   . MET   B 2 32  ? -29.634 0.810   -16.187 1.00 38.55  ? 41  MET   B C   1 
ATOM   506  O  O   . MET   B 2 32  ? -29.718 0.508   -17.380 1.00 39.01  ? 41  MET   B O   1 
ATOM   507  C  CB  . MET   B 2 32  ? -29.826 3.312   -16.252 1.00 37.54  ? 41  MET   B CB  1 
ATOM   508  C  CG  . MET   B 2 32  ? -31.072 3.551   -15.386 1.00 39.79  ? 41  MET   B CG  1 
ATOM   509  S  SD  . MET   B 2 32  ? -30.748 4.096   -13.682 1.00 46.90  ? 41  MET   B SD  1 
ATOM   510  C  CE  . MET   B 2 32  ? -30.432 5.816   -13.963 1.00 44.01  ? 41  MET   B CE  1 
ATOM   511  N  N   . GLN   B 2 33  ? -30.076 0.012   -15.214 1.00 38.98  ? 42  GLN   B N   1 
ATOM   512  C  CA  . GLN   B 2 33  ? -30.769 -1.242  -15.514 1.00 40.22  ? 42  GLN   B CA  1 
ATOM   513  C  C   . GLN   B 2 33  ? -31.710 -1.604  -14.383 1.00 40.75  ? 42  GLN   B C   1 
ATOM   514  O  O   . GLN   B 2 33  ? -31.292 -1.577  -13.227 1.00 41.04  ? 42  GLN   B O   1 
ATOM   515  C  CB  . GLN   B 2 33  ? -29.795 -2.398  -15.785 1.00 42.64  ? 42  GLN   B CB  1 
ATOM   516  C  CG  . GLN   B 2 33  ? -30.542 -3.598  -16.343 1.00 48.03  ? 42  GLN   B CG  1 
ATOM   517  C  CD  . GLN   B 2 33  ? -29.642 -4.709  -16.774 1.00 56.04  ? 42  GLN   B CD  1 
ATOM   518  O  OE1 . GLN   B 2 33  ? -29.673 -5.805  -16.211 1.00 58.64  ? 42  GLN   B OE1 1 
ATOM   519  N  NE2 . GLN   B 2 33  ? -28.823 -4.452  -17.788 1.00 58.21  ? 42  GLN   B NE2 1 
ATOM   520  N  N   . GLU   B 2 34  ? -32.973 -1.914  -14.694 1.00 40.47  ? 43  GLU   B N   1 
ATOM   521  C  CA  . GLU   B 2 34  ? -33.983 -2.237  -13.686 1.00 41.23  ? 43  GLU   B CA  1 
ATOM   522  C  C   . GLU   B 2 34  ? -34.128 -1.146  -12.568 1.00 41.79  ? 43  GLU   B C   1 
ATOM   523  O  O   . GLU   B 2 34  ? -34.333 -1.462  -11.397 1.00 42.33  ? 43  GLU   B O   1 
ATOM   524  C  CB  . GLU   B 2 34  ? -33.753 -3.640  -13.092 1.00 43.81  ? 43  GLU   B CB  1 
ATOM   525  C  CG  . GLU   B 2 34  ? -33.887 -4.770  -14.113 1.00 47.36  ? 43  GLU   B CG  1 
ATOM   526  C  CD  . GLU   B 2 34  ? -33.272 -6.105  -13.722 1.00 54.59  ? 43  GLU   B CD  1 
ATOM   527  O  OE1 . GLU   B 2 34  ? -33.727 -6.705  -12.723 1.00 56.75  ? 43  GLU   B OE1 1 
ATOM   528  O  OE2 . GLU   B 2 34  ? -32.332 -6.555  -14.416 1.00 57.59  ? 43  GLU   B OE2 1 
ATOM   529  N  N   . GLY   B 2 35  ? -34.026 0.116   -12.947 1.00 41.04  ? 44  GLY   B N   1 
ATOM   530  C  CA  . GLY   B 2 35  ? -34.160 1.228   -12.012 1.00 41.10  ? 44  GLY   B CA  1 
ATOM   531  C  C   . GLY   B 2 35  ? -32.956 1.490   -11.129 1.00 41.05  ? 44  GLY   B C   1 
ATOM   532  O  O   . GLY   B 2 35  ? -33.043 2.292   -10.198 1.00 42.13  ? 44  GLY   B O   1 
ATOM   533  N  N   . VAL   B 2 36  ? -31.825 0.812   -11.407 1.00 39.92  ? 45  VAL   B N   1 
ATOM   534  C  CA  . VAL   B 2 36  ? -30.579 0.905   -10.663 1.00 38.70  ? 45  VAL   B CA  1 
ATOM   535  C  C   . VAL   B 2 36  ? -29.419 1.464   -11.527 1.00 38.12  ? 45  VAL   B C   1 
ATOM   536  O  O   . VAL   B 2 36  ? -29.204 1.026   -12.674 1.00 37.25  ? 45  VAL   B O   1 
ATOM   537  C  CB  . VAL   B 2 36  ? -30.225 -0.453  -10.013 1.00 39.35  ? 45  VAL   B CB  1 
ATOM   538  C  CG1 . VAL   B 2 36  ? -28.830 -0.430  -9.390  1.00 39.88  ? 45  VAL   B CG1 1 
ATOM   539  C  CG2 . VAL   B 2 36  ? -31.279 -0.847  -8.967  1.00 39.43  ? 45  VAL   B CG2 1 
ATOM   540  N  N   . PHE   B 2 37  ? -28.694 2.462   -10.977 1.00 36.77  ? 46  PHE   B N   1 
ATOM   541  C  CA  . PHE   B 2 37  ? -27.543 3.021   -11.669 1.00 36.18  ? 46  PHE   B CA  1 
ATOM   542  C  C   . PHE   B 2 37  ? -26.272 2.324   -11.134 1.00 35.06  ? 46  PHE   B C   1 
ATOM   543  O  O   . PHE   B 2 37  ? -26.054 2.289   -9.928  1.00 34.66  ? 46  PHE   B O   1 
ATOM   544  C  CB  . PHE   B 2 37  ? -27.478 4.552   -11.495 1.00 35.84  ? 46  PHE   B CB  1 
ATOM   545  C  CG  . PHE   B 2 37  ? -26.452 5.148   -12.431 1.00 36.52  ? 46  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   B 2 37  ? -26.586 5.020   -13.801 1.00 36.13  ? 46  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   B 2 37  ? -25.309 5.752   -11.937 1.00 37.51  ? 46  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   B 2 37  ? -25.647 5.560   -14.657 1.00 37.02  ? 46  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   B 2 37  ? -24.355 6.269   -12.797 1.00 37.43  ? 46  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   B 2 37  ? -24.538 6.177   -14.150 1.00 37.02  ? 46  PHE   B CZ  1 
ATOM   551  N  N   . HIS   B 2 38  ? -25.494 1.705   -12.014 1.00 34.31  ? 47  HIS   B N   1 
ATOM   552  C  CA  . HIS   B 2 38  ? -24.291 0.937   -11.690 1.00 33.82  ? 47  HIS   B CA  1 
ATOM   553  C  C   . HIS   B 2 38  ? -23.077 1.670   -12.228 1.00 34.82  ? 47  HIS   B C   1 
ATOM   554  O  O   . HIS   B 2 38  ? -23.049 1.989   -13.421 1.00 35.02  ? 47  HIS   B O   1 
ATOM   555  C  CB  . HIS   B 2 38  ? -24.338 -0.429  -12.406 1.00 33.82  ? 47  HIS   B CB  1 
ATOM   556  C  CG  . HIS   B 2 38  ? -25.572 -1.228  -12.128 1.00 35.88  ? 47  HIS   B CG  1 
ATOM   557  N  ND1 . HIS   B 2 38  ? -26.803 -0.856  -12.630 1.00 37.23  ? 47  HIS   B ND1 1 
ATOM   558  C  CD2 . HIS   B 2 38  ? -25.730 -2.333  -11.365 1.00 37.21  ? 47  HIS   B CD2 1 
ATOM   559  C  CE1 . HIS   B 2 38  ? -27.663 -1.758  -12.186 1.00 37.53  ? 47  HIS   B CE1 1 
ATOM   560  N  NE2 . HIS   B 2 38  ? -27.069 -2.657  -11.412 1.00 37.96  ? 47  HIS   B NE2 1 
ATOM   561  N  N   . THR   B 2 39  ? -22.039 1.888   -11.388 1.00 34.97  ? 48  THR   B N   1 
ATOM   562  C  CA  . THR   B 2 39  ? -20.821 2.524   -11.914 1.00 35.51  ? 48  THR   B CA  1 
ATOM   563  C  C   . THR   B 2 39  ? -19.590 2.025   -11.117 1.00 35.77  ? 48  THR   B C   1 
ATOM   564  O  O   . THR   B 2 39  ? -19.702 1.100   -10.306 1.00 35.19  ? 48  THR   B O   1 
ATOM   565  C  CB  . THR   B 2 39  ? -21.003 4.084   -12.012 1.00 36.46  ? 48  THR   B CB  1 
ATOM   566  O  OG1 . THR   B 2 39  ? -19.890 4.618   -12.705 1.00 37.26  ? 48  THR   B OG1 1 
ATOM   567  C  CG2 . THR   B 2 39  ? -21.131 4.748   -10.646 1.00 36.74  ? 48  THR   B CG2 1 
ATOM   568  N  N   . MET   B 2 40  ? -18.408 2.600   -11.388 1.00 35.65  ? 49  MET   B N   1 
ATOM   569  C  CA  . MET   B 2 40  ? -17.207 2.266   -10.660 1.00 35.30  ? 49  MET   B CA  1 
ATOM   570  C  C   . MET   B 2 40  ? -17.087 3.195   -9.426  1.00 36.26  ? 49  MET   B C   1 
ATOM   571  O  O   . MET   B 2 40  ? -17.425 4.378   -9.519  1.00 36.19  ? 49  MET   B O   1 
ATOM   572  C  CB  . MET   B 2 40  ? -16.017 2.316   -11.617 1.00 35.64  ? 49  MET   B CB  1 
ATOM   573  C  CG  . MET   B 2 40  ? -16.215 1.354   -12.809 1.00 36.77  ? 49  MET   B CG  1 
ATOM   574  S  SD  . MET   B 2 40  ? -14.725 0.537   -13.319 1.00 45.41  ? 49  MET   B SD  1 
ATOM   575  C  CE  . MET   B 2 40  ? -14.746 -0.919  -12.275 1.00 40.90  ? 49  MET   B CE  1 
ATOM   576  N  N   . TRP   B 2 41  ? -16.666 2.648   -8.262  1.00 35.95  ? 50  TRP   B N   1 
ATOM   577  C  CA  A TRP   B 2 41  ? -16.548 3.435   -7.027  0.50 36.92  ? 50  TRP   B CA  1 
ATOM   578  C  CA  B TRP   B 2 41  ? -16.545 3.419   -7.026  0.50 36.38  ? 50  TRP   B CA  1 
ATOM   579  C  C   . TRP   B 2 41  ? -15.626 4.628   -7.197  1.00 36.94  ? 50  TRP   B C   1 
ATOM   580  O  O   . TRP   B 2 41  ? -15.949 5.706   -6.707  1.00 36.31  ? 50  TRP   B O   1 
ATOM   581  C  CB  A TRP   B 2 41  ? -16.063 2.587   -5.836  0.50 37.31  ? 50  TRP   B CB  1 
ATOM   582  C  CB  B TRP   B 2 41  ? -16.046 2.535   -5.868  0.50 36.00  ? 50  TRP   B CB  1 
ATOM   583  C  CG  A TRP   B 2 41  ? -16.211 3.292   -4.516  0.50 38.81  ? 50  TRP   B CG  1 
ATOM   584  C  CG  B TRP   B 2 41  ? -15.918 3.294   -4.584  0.50 36.47  ? 50  TRP   B CG  1 
ATOM   585  C  CD1 A TRP   B 2 41  ? -17.298 3.267   -3.696  0.50 39.88  ? 50  TRP   B CD1 1 
ATOM   586  C  CD1 B TRP   B 2 41  ? -14.839 4.011   -4.160  0.50 37.24  ? 50  TRP   B CD1 1 
ATOM   587  C  CD2 A TRP   B 2 41  ? -15.262 4.175   -3.895  0.50 39.21  ? 50  TRP   B CD2 1 
ATOM   588  C  CD2 B TRP   B 2 41  ? -16.953 3.521   -3.626  0.50 36.30  ? 50  TRP   B CD2 1 
ATOM   589  N  NE1 A TRP   B 2 41  ? -17.087 4.074   -2.604  0.50 40.41  ? 50  TRP   B NE1 1 
ATOM   590  N  NE1 B TRP   B 2 41  ? -15.131 4.646   -2.981  0.50 37.41  ? 50  TRP   B NE1 1 
ATOM   591  C  CE2 A TRP   B 2 41  ? -15.845 4.645   -2.703  0.50 40.17  ? 50  TRP   B CE2 1 
ATOM   592  C  CE2 B TRP   B 2 41  ? -16.425 4.366   -2.631  0.50 37.06  ? 50  TRP   B CE2 1 
ATOM   593  C  CE3 A TRP   B 2 41  ? -13.978 4.621   -4.236  0.50 39.99  ? 50  TRP   B CE3 1 
ATOM   594  C  CE3 B TRP   B 2 41  ? -18.280 3.094   -3.512  0.50 36.85  ? 50  TRP   B CE3 1 
ATOM   595  C  CZ2 A TRP   B 2 41  ? -15.179 5.516   -1.839  0.50 41.02  ? 50  TRP   B CZ2 1 
ATOM   596  C  CZ2 B TRP   B 2 41  ? -17.168 4.772   -1.527  0.50 37.50  ? 50  TRP   B CZ2 1 
ATOM   597  C  CZ3 A TRP   B 2 41  ? -13.327 5.493   -3.385  0.50 41.05  ? 50  TRP   B CZ3 1 
ATOM   598  C  CZ3 B TRP   B 2 41  ? -19.010 3.486   -2.408  0.50 37.51  ? 50  TRP   B CZ3 1 
ATOM   599  C  CH2 A TRP   B 2 41  ? -13.918 5.914   -2.192  0.50 41.16  ? 50  TRP   B CH2 1 
ATOM   600  C  CH2 B TRP   B 2 41  ? -18.451 4.313   -1.431  0.50 37.71  ? 50  TRP   B CH2 1 
ATOM   601  N  N   . HIS   B 2 42  ? -14.461 4.436   -7.848  1.00 36.68  ? 51  HIS   B N   1 
ATOM   602  C  CA  . HIS   B 2 42  ? -13.504 5.526   -8.036  1.00 37.24  ? 51  HIS   B CA  1 
ATOM   603  C  C   . HIS   B 2 42  ? -14.057 6.707   -8.845  1.00 38.66  ? 51  HIS   B C   1 
ATOM   604  O  O   . HIS   B 2 42  ? -13.502 7.802   -8.750  1.00 39.30  ? 51  HIS   B O   1 
ATOM   605  C  CB  . HIS   B 2 42  ? -12.179 5.025   -8.632  1.00 36.34  ? 51  HIS   B CB  1 
ATOM   606  C  CG  . HIS   B 2 42  ? -12.226 4.766   -10.103 1.00 36.88  ? 51  HIS   B CG  1 
ATOM   607  N  ND1 . HIS   B 2 42  ? -12.341 3.475   -10.609 1.00 38.36  ? 51  HIS   B ND1 1 
ATOM   608  C  CD2 . HIS   B 2 42  ? -12.115 5.636   -11.141 1.00 37.17  ? 51  HIS   B CD2 1 
ATOM   609  C  CE1 . HIS   B 2 42  ? -12.354 3.612   -11.924 1.00 38.64  ? 51  HIS   B CE1 1 
ATOM   610  N  NE2 . HIS   B 2 42  ? -12.225 4.902   -12.286 1.00 38.00  ? 51  HIS   B NE2 1 
ATOM   611  N  N   . VAL   B 2 43  ? -15.142 6.499   -9.628  1.00 38.93  ? 52  VAL   B N   1 
ATOM   612  C  CA  . VAL   B 2 43  ? -15.787 7.561   -10.412 1.00 39.62  ? 52  VAL   B CA  1 
ATOM   613  C  C   . VAL   B 2 43  ? -16.526 8.567   -9.502  1.00 40.64  ? 52  VAL   B C   1 
ATOM   614  O  O   . VAL   B 2 43  ? -16.258 9.764   -9.566  1.00 41.76  ? 52  VAL   B O   1 
ATOM   615  C  CB  . VAL   B 2 43  ? -16.731 6.971   -11.498 1.00 39.78  ? 52  VAL   B CB  1 
ATOM   616  C  CG1 . VAL   B 2 43  ? -17.589 8.062   -12.145 1.00 40.25  ? 52  VAL   B CG1 1 
ATOM   617  C  CG2 . VAL   B 2 43  ? -15.941 6.206   -12.552 1.00 39.80  ? 52  VAL   B CG2 1 
ATOM   618  N  N   . THR   B 2 44  ? -17.419 8.075   -8.623  1.00 40.16  ? 53  THR   B N   1 
ATOM   619  C  CA  . THR   B 2 44  ? -18.233 8.929   -7.762  1.00 40.15  ? 53  THR   B CA  1 
ATOM   620  C  C   . THR   B 2 44  ? -17.754 9.065   -6.325  1.00 40.42  ? 53  THR   B C   1 
ATOM   621  O  O   . THR   B 2 44  ? -18.179 9.985   -5.638  1.00 39.98  ? 53  THR   B O   1 
ATOM   622  C  CB  . THR   B 2 44  ? -19.692 8.425   -7.749  1.00 40.65  ? 53  THR   B CB  1 
ATOM   623  O  OG1 . THR   B 2 44  ? -19.776 7.217   -6.974  1.00 40.98  ? 53  THR   B OG1 1 
ATOM   624  C  CG2 . THR   B 2 44  ? -20.253 8.176   -9.155  1.00 40.26  ? 53  THR   B CG2 1 
ATOM   625  N  N   . LYS   B 2 45  ? -16.903 8.143   -5.867  1.00 40.99  ? 54  LYS   B N   1 
ATOM   626  C  CA  . LYS   B 2 45  ? -16.440 8.018   -4.470  1.00 42.44  ? 54  LYS   B CA  1 
ATOM   627  C  C   . LYS   B 2 45  ? -17.611 7.822   -3.493  1.00 42.54  ? 54  LYS   B C   1 
ATOM   628  O  O   . LYS   B 2 45  ? -17.479 8.156   -2.323  1.00 43.18  ? 54  LYS   B O   1 
ATOM   629  C  CB  . LYS   B 2 45  ? -15.534 9.169   -3.999  1.00 44.66  ? 54  LYS   B CB  1 
ATOM   630  C  CG  . LYS   B 2 45  ? -14.481 9.553   -4.997  1.00 51.57  ? 54  LYS   B CG  1 
ATOM   631  C  CD  . LYS   B 2 45  ? -13.091 9.194   -4.537  1.00 57.86  ? 54  LYS   B CD  1 
ATOM   632  C  CE  . LYS   B 2 45  ? -12.083 9.923   -5.396  1.00 62.83  ? 54  LYS   B CE  1 
ATOM   633  N  NZ  . LYS   B 2 45  ? -12.374 9.748   -6.853  1.00 65.83  ? 54  LYS   B NZ  1 
ATOM   634  N  N   . GLY   B 2 46  ? -18.727 7.286   -3.980  1.00 42.08  ? 55  GLY   B N   1 
ATOM   635  C  CA  . GLY   B 2 46  ? -19.920 7.061   -3.182  1.00 42.54  ? 55  GLY   B CA  1 
ATOM   636  C  C   . GLY   B 2 46  ? -20.852 8.249   -3.079  1.00 43.32  ? 55  GLY   B C   1 
ATOM   637  O  O   . GLY   B 2 46  ? -21.914 8.133   -2.474  1.00 43.77  ? 55  GLY   B O   1 
ATOM   638  N  N   . ALA   B 2 47  ? -20.485 9.399   -3.659  1.00 43.43  ? 56  ALA   B N   1 
ATOM   639  C  CA  . ALA   B 2 47  ? -21.309 10.610  -3.586  1.00 43.92  ? 56  ALA   B CA  1 
ATOM   640  C  C   . ALA   B 2 47  ? -22.646 10.456  -4.302  1.00 43.73  ? 56  ALA   B C   1 
ATOM   641  O  O   . ALA   B 2 47  ? -22.734 9.697   -5.267  1.00 43.72  ? 56  ALA   B O   1 
ATOM   642  C  CB  . ALA   B 2 47  ? -20.545 11.793  -4.186  1.00 44.09  ? 56  ALA   B CB  1 
ATOM   643  N  N   . ALA   B 2 48  ? -23.654 11.250  -3.892  1.00 43.65  ? 57  ALA   B N   1 
ATOM   644  C  CA  . ALA   B 2 48  ? -24.978 11.273  -4.518  1.00 44.43  ? 57  ALA   B CA  1 
ATOM   645  C  C   . ALA   B 2 48  ? -24.898 11.799  -5.948  1.00 45.56  ? 57  ALA   B C   1 
ATOM   646  O  O   . ALA   B 2 48  ? -23.967 12.527  -6.297  1.00 46.34  ? 57  ALA   B O   1 
ATOM   647  C  CB  . ALA   B 2 48  ? -25.932 12.135  -3.704  1.00 44.48  ? 57  ALA   B CB  1 
ATOM   648  N  N   . LEU   B 2 49  ? -25.862 11.417  -6.783  1.00 45.28  ? 58  LEU   B N   1 
ATOM   649  C  CA  . LEU   B 2 49  ? -25.908 11.837  -8.176  1.00 45.87  ? 58  LEU   B CA  1 
ATOM   650  C  C   . LEU   B 2 49  ? -27.235 12.543  -8.482  1.00 47.32  ? 58  LEU   B C   1 
ATOM   651  O  O   . LEU   B 2 49  ? -28.233 12.331  -7.796  1.00 47.78  ? 58  LEU   B O   1 
ATOM   652  C  CB  . LEU   B 2 49  ? -25.750 10.618  -9.107  1.00 45.55  ? 58  LEU   B CB  1 
ATOM   653  C  CG  . LEU   B 2 49  ? -24.469 9.804   -9.007  1.00 46.08  ? 58  LEU   B CG  1 
ATOM   654  C  CD1 . LEU   B 2 49  ? -24.500 8.673   -9.986  1.00 46.48  ? 58  LEU   B CD1 1 
ATOM   655  C  CD2 . LEU   B 2 49  ? -23.247 10.644  -9.304  1.00 46.05  ? 58  LEU   B CD2 1 
ATOM   656  N  N   . ARG   B 2 50  ? -27.248 13.374  -9.511  1.00 47.98  ? 59  ARG   B N   1 
ATOM   657  C  CA  . ARG   B 2 50  ? -28.438 14.099  -9.921  1.00 49.33  ? 59  ARG   B CA  1 
ATOM   658  C  C   . ARG   B 2 50  ? -28.844 13.658  -11.342 1.00 50.43  ? 59  ARG   B C   1 
ATOM   659  O  O   . ARG   B 2 50  ? -27.986 13.382  -12.164 1.00 49.39  ? 59  ARG   B O   1 
ATOM   660  C  CB  . ARG   B 2 50  ? -28.157 15.613  -9.800  1.00 51.61  ? 59  ARG   B CB  1 
ATOM   661  C  CG  . ARG   B 2 50  ? -28.859 16.511  -10.793 1.00 57.89  ? 59  ARG   B CG  1 
ATOM   662  C  CD  . ARG   B 2 50  ? -28.725 17.982  -10.429 1.00 64.34  ? 59  ARG   B CD  1 
ATOM   663  N  NE  . ARG   B 2 50  ? -27.372 18.507  -10.626 1.00 68.97  ? 59  ARG   B NE  1 
ATOM   664  C  CZ  . ARG   B 2 50  ? -26.888 18.925  -11.793 1.00 72.52  ? 59  ARG   B CZ  1 
ATOM   665  N  NH1 . ARG   B 2 50  ? -27.623 18.832  -12.898 1.00 71.96  ? 59  ARG   B NH1 1 
ATOM   666  N  NH2 . ARG   B 2 50  ? -25.657 19.418  -11.870 1.00 73.33  ? 59  ARG   B NH2 1 
ATOM   667  N  N   . SER   B 2 51  ? -30.144 13.569  -11.624 1.00 52.29  ? 60  SER   B N   1 
ATOM   668  C  CA  . SER   B 2 51  ? -30.647 13.208  -12.951 1.00 54.72  ? 60  SER   B CA  1 
ATOM   669  C  C   . SER   B 2 51  ? -31.805 14.182  -13.249 1.00 57.72  ? 60  SER   B C   1 
ATOM   670  O  O   . SER   B 2 51  ? -32.956 13.932  -12.877 1.00 57.78  ? 60  SER   B O   1 
ATOM   671  C  CB  . SER   B 2 51  ? -31.137 11.766  -12.958 1.00 56.54  ? 60  SER   B CB  1 
ATOM   672  O  OG  . SER   B 2 51  ? -31.589 11.413  -14.254 1.00 60.60  ? 60  SER   B OG  1 
ATOM   673  N  N   . GLY   B 2 52  ? -31.475 15.335  -13.826 1.00 59.40  ? 61  GLY   B N   1 
ATOM   674  C  CA  . GLY   B 2 52  ? -32.455 16.389  -14.048 1.00 61.23  ? 61  GLY   B CA  1 
ATOM   675  C  C   . GLY   B 2 52  ? -32.751 17.001  -12.699 1.00 63.38  ? 61  GLY   B C   1 
ATOM   676  O  O   . GLY   B 2 52  ? -31.831 17.462  -12.019 1.00 64.00  ? 61  GLY   B O   1 
ATOM   677  N  N   . GLU   B 2 53  ? -34.002 16.906  -12.248 1.00 64.31  ? 62  GLU   B N   1 
ATOM   678  C  CA  . GLU   B 2 53  ? -34.350 17.341  -10.896 1.00 65.62  ? 62  GLU   B CA  1 
ATOM   679  C  C   . GLU   B 2 53  ? -34.242 16.191  -9.858  1.00 65.29  ? 62  GLU   B C   1 
ATOM   680  O  O   . GLU   B 2 53  ? -34.171 16.459  -8.649  1.00 65.82  ? 62  GLU   B O   1 
ATOM   681  C  CB  . GLU   B 2 53  ? -35.753 17.933  -10.862 1.00 69.96  ? 62  GLU   B CB  1 
ATOM   682  C  CG  . GLU   B 2 53  ? -35.767 19.411  -10.535 1.00 77.55  ? 62  GLU   B CG  1 
ATOM   683  C  CD  . GLU   B 2 53  ? -37.161 19.928  -10.243 1.00 87.46  ? 62  GLU   B CD  1 
ATOM   684  O  OE1 . GLU   B 2 53  ? -37.984 19.148  -9.709  1.00 89.55  ? 62  GLU   B OE1 1 
ATOM   685  O  OE2 . GLU   B 2 53  ? -37.429 21.115  -10.544 1.00 90.62  ? 62  GLU   B OE2 1 
ATOM   686  N  N   . GLY   B 2 54  ? -34.252 14.943  -10.339 1.00 63.98  ? 63  GLY   B N   1 
ATOM   687  C  CA  . GLY   B 2 54  ? -34.183 13.752  -9.507  1.00 63.19  ? 63  GLY   B CA  1 
ATOM   688  C  C   . GLY   B 2 54  ? -32.845 13.539  -8.828  1.00 61.66  ? 63  GLY   B C   1 
ATOM   689  O  O   . GLY   B 2 54  ? -31.807 13.980  -9.329  1.00 62.06  ? 63  GLY   B O   1 
ATOM   690  N  N   . ARG   B 2 55  ? -32.860 12.851  -7.680  1.00 59.07  ? 64  ARG   B N   1 
ATOM   691  C  CA  . ARG   B 2 55  ? -31.633 12.577  -6.951  1.00 57.04  ? 64  ARG   B CA  1 
ATOM   692  C  C   . ARG   B 2 55  ? -31.446 11.066  -6.773  1.00 54.36  ? 64  ARG   B C   1 
ATOM   693  O  O   . ARG   B 2 55  ? -32.351 10.382  -6.286  1.00 54.56  ? 64  ARG   B O   1 
ATOM   694  C  CB  . ARG   B 2 55  ? -31.668 13.285  -5.585  1.00 58.35  ? 64  ARG   B CB  1 
ATOM   695  C  CG  . ARG   B 2 55  ? -30.418 13.123  -4.732  1.00 61.43  ? 64  ARG   B CG  1 
ATOM   696  C  CD  . ARG   B 2 55  ? -30.707 13.520  -3.295  1.00 65.11  ? 64  ARG   B CD  1 
ATOM   697  N  NE  . ARG   B 2 55  ? -29.577 13.238  -2.412  1.00 68.52  ? 64  ARG   B NE  1 
ATOM   698  C  CZ  . ARG   B 2 55  ? -28.891 14.161  -1.742  1.00 71.72  ? 64  ARG   B CZ  1 
ATOM   699  N  NH1 . ARG   B 2 55  ? -29.220 15.445  -1.840  1.00 72.46  ? 64  ARG   B NH1 1 
ATOM   700  N  NH2 . ARG   B 2 55  ? -27.878 13.805  -0.962  1.00 71.26  ? 64  ARG   B NH2 1 
ATOM   701  N  N   . LEU   B 2 56  ? -30.271 10.556  -7.152  1.00 51.45  ? 65  LEU   B N   1 
ATOM   702  C  CA  . LEU   B 2 56  ? -29.902 9.157   -6.970  1.00 49.58  ? 65  LEU   B CA  1 
ATOM   703  C  C   . LEU   B 2 56  ? -28.969 9.033   -5.750  1.00 48.00  ? 65  LEU   B C   1 
ATOM   704  O  O   . LEU   B 2 56  ? -27.905 9.661   -5.713  1.00 48.14  ? 65  LEU   B O   1 
ATOM   705  C  CB  . LEU   B 2 56  ? -29.170 8.601   -8.207  1.00 49.53  ? 65  LEU   B CB  1 
ATOM   706  C  CG  . LEU   B 2 56  ? -29.752 8.831   -9.600  1.00 51.67  ? 65  LEU   B CG  1 
ATOM   707  C  CD1 . LEU   B 2 56  ? -29.091 7.901   -10.602 1.00 51.67  ? 65  LEU   B CD1 1 
ATOM   708  C  CD2 . LEU   B 2 56  ? -31.251 8.588   -9.639  1.00 53.33  ? 65  LEU   B CD2 1 
ATOM   709  N  N   . ASP   B 2 57  ? -29.348 8.222   -4.765  1.00 46.40  ? 66  ASP   B N   1 
ATOM   710  C  CA  . ASP   B 2 57  ? -28.509 8.019   -3.575  1.00 45.19  ? 66  ASP   B CA  1 
ATOM   711  C  C   . ASP   B 2 57  ? -27.788 6.662   -3.639  1.00 42.51  ? 66  ASP   B C   1 
ATOM   712  O  O   . ASP   B 2 57  ? -28.309 5.706   -4.225  1.00 41.91  ? 66  ASP   B O   1 
ATOM   713  C  CB  . ASP   B 2 57  ? -29.353 8.109   -2.303  1.00 48.88  ? 66  ASP   B CB  1 
ATOM   714  C  CG  . ASP   B 2 57  ? -29.998 9.470   -2.121  1.00 57.13  ? 66  ASP   B CG  1 
ATOM   715  O  OD1 . ASP   B 2 57  ? -29.271 10.488  -2.215  1.00 58.61  ? 66  ASP   B OD1 1 
ATOM   716  O  OD2 . ASP   B 2 57  ? -31.227 9.516   -1.890  1.00 60.20  ? 66  ASP   B OD2 1 
ATOM   717  N  N   . PRO   B 2 58  ? -26.565 6.572   -3.096  1.00 40.70  ? 67  PRO   B N   1 
ATOM   718  C  CA  . PRO   B 2 58  ? -25.851 5.282   -3.130  1.00 39.67  ? 67  PRO   B CA  1 
ATOM   719  C  C   . PRO   B 2 58  ? -26.594 4.240   -2.283  1.00 39.68  ? 67  PRO   B C   1 
ATOM   720  O  O   . PRO   B 2 58  ? -27.235 4.578   -1.286  1.00 40.26  ? 67  PRO   B O   1 
ATOM   721  C  CB  . PRO   B 2 58  ? -24.470 5.627   -2.570  1.00 40.09  ? 67  PRO   B CB  1 
ATOM   722  C  CG  . PRO   B 2 58  ? -24.695 6.816   -1.714  1.00 40.66  ? 67  PRO   B CG  1 
ATOM   723  C  CD  . PRO   B 2 58  ? -25.801 7.606   -2.366  1.00 39.73  ? 67  PRO   B CD  1 
ATOM   724  N  N   . TYR   B 2 59  ? -26.582 2.986   -2.722  1.00 38.30  ? 68  TYR   B N   1 
ATOM   725  C  CA  . TYR   B 2 59  ? -27.301 1.924   -2.049  1.00 36.89  ? 68  TYR   B CA  1 
ATOM   726  C  C   . TYR   B 2 59  ? -26.323 0.854   -1.566  1.00 36.30  ? 68  TYR   B C   1 
ATOM   727  O  O   . TYR   B 2 59  ? -26.491 0.319   -0.498  1.00 36.20  ? 68  TYR   B O   1 
ATOM   728  C  CB  . TYR   B 2 59  ? -28.375 1.345   -2.997  1.00 35.89  ? 68  TYR   B CB  1 
ATOM   729  C  CG  . TYR   B 2 59  ? -29.202 0.217   -2.400  1.00 36.45  ? 68  TYR   B CG  1 
ATOM   730  C  CD1 . TYR   B 2 59  ? -28.715 -1.092  -2.360  1.00 36.47  ? 68  TYR   B CD1 1 
ATOM   731  C  CD2 . TYR   B 2 59  ? -30.499 0.442   -1.943  1.00 35.64  ? 68  TYR   B CD2 1 
ATOM   732  C  CE1 . TYR   B 2 59  ? -29.460 -2.121  -1.801  1.00 36.45  ? 68  TYR   B CE1 1 
ATOM   733  C  CE2 . TYR   B 2 59  ? -31.265 -0.591  -1.417  1.00 36.17  ? 68  TYR   B CE2 1 
ATOM   734  C  CZ  . TYR   B 2 59  ? -30.750 -1.875  -1.367  1.00 37.73  ? 68  TYR   B CZ  1 
ATOM   735  O  OH  . TYR   B 2 59  ? -31.492 -2.895  -0.798  1.00 39.34  ? 68  TYR   B OH  1 
ATOM   736  N  N   . TRP   B 2 60  ? -25.355 0.496   -2.389  1.00 35.72  ? 69  TRP   B N   1 
ATOM   737  C  CA  . TRP   B 2 60  ? -24.368 -0.525  -2.077  1.00 35.24  ? 69  TRP   B CA  1 
ATOM   738  C  C   . TRP   B 2 60  ? -23.065 -0.076  -2.740  1.00 36.20  ? 69  TRP   B C   1 
ATOM   739  O  O   . TRP   B 2 60  ? -23.087 0.554   -3.802  1.00 36.92  ? 69  TRP   B O   1 
ATOM   740  C  CB  . TRP   B 2 60  ? -24.816 -1.922  -2.594  1.00 34.16  ? 69  TRP   B CB  1 
ATOM   741  C  CG  . TRP   B 2 60  ? -23.704 -2.932  -2.556  1.00 34.72  ? 69  TRP   B CG  1 
ATOM   742  C  CD1 . TRP   B 2 60  ? -23.262 -3.626  -1.469  1.00 35.85  ? 69  TRP   B CD1 1 
ATOM   743  C  CD2 . TRP   B 2 60  ? -22.769 -3.209  -3.614  1.00 34.70  ? 69  TRP   B CD2 1 
ATOM   744  N  NE1 . TRP   B 2 60  ? -22.114 -4.328  -1.787  1.00 35.83  ? 69  TRP   B NE1 1 
ATOM   745  C  CE2 . TRP   B 2 60  ? -21.809 -4.110  -3.103  1.00 35.12  ? 69  TRP   B CE2 1 
ATOM   746  C  CE3 . TRP   B 2 60  ? -22.635 -2.760  -4.938  1.00 34.27  ? 69  TRP   B CE3 1 
ATOM   747  C  CZ2 . TRP   B 2 60  ? -20.743 -4.574  -3.874  1.00 35.33  ? 69  TRP   B CZ2 1 
ATOM   748  C  CZ3 . TRP   B 2 60  ? -21.586 -3.232  -5.700  1.00 34.86  ? 69  TRP   B CZ3 1 
ATOM   749  C  CH2 . TRP   B 2 60  ? -20.680 -4.157  -5.183  1.00 35.11  ? 69  TRP   B CH2 1 
ATOM   750  N  N   . GLY   B 2 61  ? -21.944 -0.419  -2.133  1.00 35.96  ? 70  GLY   B N   1 
ATOM   751  C  CA  . GLY   B 2 61  ? -20.640 -0.094  -2.699  1.00 36.32  ? 70  GLY   B CA  1 
ATOM   752  C  C   . GLY   B 2 61  ? -19.515 -0.810  -1.983  1.00 36.47  ? 70  GLY   B C   1 
ATOM   753  O  O   . GLY   B 2 61  ? -19.677 -1.224  -0.834  1.00 36.02  ? 70  GLY   B O   1 
ATOM   754  N  N   . ASP   B 2 62  ? -18.373 -0.972  -2.657  1.00 36.66  ? 71  ASP   B N   1 
ATOM   755  C  CA  . ASP   B 2 62  ? -17.209 -1.651  -2.086  1.00 36.50  ? 71  ASP   B CA  1 
ATOM   756  C  C   . ASP   B 2 62  ? -15.940 -1.139  -2.780  1.00 36.58  ? 71  ASP   B C   1 
ATOM   757  O  O   . ASP   B 2 62  ? -15.832 -1.260  -3.987  1.00 36.19  ? 71  ASP   B O   1 
ATOM   758  C  CB  . ASP   B 2 62  ? -17.360 -3.156  -2.290  1.00 39.01  ? 71  ASP   B CB  1 
ATOM   759  C  CG  . ASP   B 2 62  ? -16.308 -3.970  -1.574  1.00 46.06  ? 71  ASP   B CG  1 
ATOM   760  O  OD1 . ASP   B 2 62  ? -15.220 -4.143  -2.128  1.00 47.44  ? 71  ASP   B OD1 1 
ATOM   761  O  OD2 . ASP   B 2 62  ? -16.579 -4.429  -0.457  1.00 49.17  ? 71  ASP   B OD2 1 
ATOM   762  N  N   . VAL   B 2 63  ? -15.013 -0.530  -2.041  1.00 36.74  ? 72  VAL   B N   1 
ATOM   763  C  CA  . VAL   B 2 63  ? -13.777 0.016   -2.609  1.00 37.21  ? 72  VAL   B CA  1 
ATOM   764  C  C   . VAL   B 2 63  ? -12.903 -1.076  -3.250  1.00 38.00  ? 72  VAL   B C   1 
ATOM   765  O  O   . VAL   B 2 63  ? -12.355 -0.852  -4.335  1.00 38.34  ? 72  VAL   B O   1 
ATOM   766  C  CB  . VAL   B 2 63  ? -13.020 0.838   -1.520  1.00 37.29  ? 72  VAL   B CB  1 
ATOM   767  C  CG1 . VAL   B 2 63  ? -11.552 1.048   -1.860  1.00 37.31  ? 72  VAL   B CG1 1 
ATOM   768  C  CG2 . VAL   B 2 63  ? -13.710 2.176   -1.255  1.00 37.63  ? 72  VAL   B CG2 1 
ATOM   769  N  N   . LYS   B 2 64  ? -12.783 -2.262  -2.611  1.00 38.23  ? 73  LYS   B N   1 
ATOM   770  C  CA  . LYS   B 2 64  ? -11.959 -3.338  -3.187  1.00 38.38  ? 73  LYS   B CA  1 
ATOM   771  C  C   . LYS   B 2 64  ? -12.505 -3.852  -4.518  1.00 38.18  ? 73  LYS   B C   1 
ATOM   772  O  O   . LYS   B 2 64  ? -11.730 -4.027  -5.463  1.00 38.01  ? 73  LYS   B O   1 
ATOM   773  C  CB  . LYS   B 2 64  ? -11.708 -4.480  -2.193  1.00 39.64  ? 73  LYS   B CB  1 
ATOM   774  C  CG  . LYS   B 2 64  ? -10.683 -5.486  -2.729  1.00 42.36  ? 73  LYS   B CG  1 
ATOM   775  C  CD  . LYS   B 2 64  ? -10.354 -6.535  -1.714  1.00 46.54  ? 73  LYS   B CD  1 
ATOM   776  C  CE  . LYS   B 2 64  ? -9.386  -7.546  -2.257  1.00 50.35  ? 73  LYS   B CE  1 
ATOM   777  N  NZ  . LYS   B 2 64  ? -8.784  -8.323  -1.141  1.00 52.23  ? 73  LYS   B NZ  1 
ATOM   778  N  N   . GLN   B 2 65  ? -13.836 -4.083  -4.623  1.00 38.07  ? 74  GLN   B N   1 
ATOM   779  C  CA  . GLN   B 2 65  ? -14.410 -4.486  -5.927  1.00 37.78  ? 74  GLN   B CA  1 
ATOM   780  C  C   . GLN   B 2 65  ? -14.449 -3.301  -6.926  1.00 36.85  ? 74  GLN   B C   1 
ATOM   781  O  O   . GLN   B 2 65  ? -14.598 -3.519  -8.131  1.00 36.88  ? 74  GLN   B O   1 
ATOM   782  C  CB  . GLN   B 2 65  ? -15.829 -5.066  -5.773  1.00 39.99  ? 74  GLN   B CB  1 
ATOM   783  C  CG  . GLN   B 2 65  ? -15.929 -6.258  -4.826  1.00 45.11  ? 74  GLN   B CG  1 
ATOM   784  C  CD  . GLN   B 2 65  ? -17.373 -6.738  -4.686  1.00 50.69  ? 74  GLN   B CD  1 
ATOM   785  O  OE1 . GLN   B 2 65  ? -18.112 -6.863  -5.668  1.00 52.58  ? 74  GLN   B OE1 1 
ATOM   786  N  NE2 . GLN   B 2 65  ? -17.810 -7.020  -3.470  1.00 51.36  ? 74  GLN   B NE2 1 
ATOM   787  N  N   . ASP   B 2 66  ? -14.310 -2.060  -6.423  1.00 35.64  ? 75  ASP   B N   1 
ATOM   788  C  CA  . ASP   B 2 66  ? -14.368 -0.799  -7.156  1.00 35.15  ? 75  ASP   B CA  1 
ATOM   789  C  C   . ASP   B 2 66  ? -15.712 -0.639  -7.848  1.00 34.39  ? 75  ASP   B C   1 
ATOM   790  O  O   . ASP   B 2 66  ? -15.776 -0.189  -8.993  1.00 33.52  ? 75  ASP   B O   1 
ATOM   791  C  CB  . ASP   B 2 66  ? -13.180 -0.573  -8.126  1.00 35.44  ? 75  ASP   B CB  1 
ATOM   792  C  CG  . ASP   B 2 66  ? -13.133 0.854   -8.643  1.00 38.70  ? 75  ASP   B CG  1 
ATOM   793  O  OD1 . ASP   B 2 66  ? -13.441 1.785   -7.860  1.00 39.80  ? 75  ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   B 2 66  ? -12.850 1.039   -9.832  1.00 41.27  ? 75  ASP   B OD2 1 
ATOM   795  N  N   . LEU   B 2 67  ? -16.797 -0.955  -7.128  1.00 33.85  ? 76  LEU   B N   1 
ATOM   796  C  CA  . LEU   B 2 67  ? -18.140 -0.849  -7.706  1.00 33.91  ? 76  LEU   B CA  1 
ATOM   797  C  C   . LEU   B 2 67  ? -19.102 -0.118  -6.802  1.00 34.28  ? 76  LEU   B C   1 
ATOM   798  O  O   . LEU   B 2 67  ? -18.911 -0.119  -5.583  1.00 35.13  ? 76  LEU   B O   1 
ATOM   799  C  CB  . LEU   B 2 67  ? -18.696 -2.250  -7.959  1.00 33.51  ? 76  LEU   B CB  1 
ATOM   800  C  CG  . LEU   B 2 67  ? -18.056 -3.042  -9.071  1.00 34.32  ? 76  LEU   B CG  1 
ATOM   801  C  CD1 . LEU   B 2 67  ? -18.691 -4.372  -9.156  1.00 34.97  ? 76  LEU   B CD1 1 
ATOM   802  C  CD2 . LEU   B 2 67  ? -18.099 -2.292  -10.428 1.00 33.72  ? 76  LEU   B CD2 1 
ATOM   803  N  N   . VAL   B 2 68  ? -20.172 0.459   -7.375  1.00 33.95  ? 77  VAL   B N   1 
ATOM   804  C  CA  . VAL   B 2 68  ? -21.210 1.144   -6.572  1.00 33.72  ? 77  VAL   B CA  1 
ATOM   805  C  C   . VAL   B 2 68  ? -22.564 1.111   -7.327  1.00 33.76  ? 77  VAL   B C   1 
ATOM   806  O  O   . VAL   B 2 68  ? -22.573 1.180   -8.548  1.00 33.77  ? 77  VAL   B O   1 
ATOM   807  C  CB  . VAL   B 2 68  ? -20.770 2.586   -6.148  1.00 34.46  ? 77  VAL   B CB  1 
ATOM   808  C  CG1 . VAL   B 2 68  ? -20.422 3.449   -7.361  1.00 35.60  ? 77  VAL   B CG1 1 
ATOM   809  C  CG2 . VAL   B 2 68  ? -21.794 3.277   -5.234  1.00 34.40  ? 77  VAL   B CG2 1 
ATOM   810  N  N   . SER   B 2 69  ? -23.682 0.911   -6.607  1.00 33.49  ? 78  SER   B N   1 
ATOM   811  C  CA  . SER   B 2 69  ? -25.031 0.917   -7.171  1.00 33.67  ? 78  SER   B CA  1 
ATOM   812  C  C   . SER   B 2 69  ? -25.871 2.002   -6.499  1.00 34.37  ? 78  SER   B C   1 
ATOM   813  O  O   . SER   B 2 69  ? -25.671 2.320   -5.321  1.00 33.90  ? 78  SER   B O   1 
ATOM   814  C  CB  . SER   B 2 69  ? -25.703 -0.456  -7.092  1.00 34.52  ? 78  SER   B CB  1 
ATOM   815  O  OG  . SER   B 2 69  ? -26.131 -0.778  -5.778  1.00 37.42  ? 78  SER   B OG  1 
ATOM   816  N  N   . TYR   B 2 70  ? -26.818 2.568   -7.249  1.00 34.68  ? 79  TYR   B N   1 
ATOM   817  C  CA  . TYR   B 2 70  ? -27.667 3.673   -6.799  1.00 35.56  ? 79  TYR   B CA  1 
ATOM   818  C  C   . TYR   B 2 70  ? -29.144 3.274   -6.949  1.00 35.92  ? 79  TYR   B C   1 
ATOM   819  O  O   . TYR   B 2 70  ? -29.492 2.680   -7.965  1.00 36.10  ? 79  TYR   B O   1 
ATOM   820  C  CB  . TYR   B 2 70  ? -27.362 4.905   -7.674  1.00 35.50  ? 79  TYR   B CB  1 
ATOM   821  C  CG  . TYR   B 2 70  ? -26.040 5.572   -7.355  1.00 36.36  ? 79  TYR   B CG  1 
ATOM   822  C  CD1 . TYR   B 2 70  ? -24.836 5.059   -7.840  1.00 37.45  ? 79  TYR   B CD1 1 
ATOM   823  C  CD2 . TYR   B 2 70  ? -25.992 6.729   -6.592  1.00 37.60  ? 79  TYR   B CD2 1 
ATOM   824  C  CE1 . TYR   B 2 70  ? -23.617 5.653   -7.520  1.00 38.16  ? 79  TYR   B CE1 1 
ATOM   825  C  CE2 . TYR   B 2 70  ? -24.785 7.310   -6.240  1.00 38.73  ? 79  TYR   B CE2 1 
ATOM   826  C  CZ  . TYR   B 2 70  ? -23.601 6.792   -6.734  1.00 39.82  ? 79  TYR   B CZ  1 
ATOM   827  O  OH  . TYR   B 2 70  ? -22.432 7.411   -6.376  1.00 41.51  ? 79  TYR   B OH  1 
ATOM   828  N  N   . CYS   B 2 71  ? -29.997 3.575   -5.956  1.00 35.80  ? 80  CYS   B N   1 
ATOM   829  C  CA  . CYS   B 2 71  ? -31.452 3.294   -5.975  1.00 37.25  ? 80  CYS   B CA  1 
ATOM   830  C  C   . CYS   B 2 71  ? -31.812 1.840   -5.631  1.00 37.38  ? 80  CYS   B C   1 
ATOM   831  O  O   . CYS   B 2 71  ? -32.956 1.568   -5.279  1.00 38.75  ? 80  CYS   B O   1 
ATOM   832  C  CB  . CYS   B 2 71  ? -32.114 3.726   -7.284  1.00 40.27  ? 80  CYS   B CB  1 
ATOM   833  S  SG  . CYS   B 2 71  ? -31.699 5.413   -7.826  1.00 47.79  ? 80  CYS   B SG  1 
ATOM   834  N  N   . GLY   B 2 72  ? -30.861 0.927   -5.738  1.00 35.80  ? 81  GLY   B N   1 
ATOM   835  C  CA  . GLY   B 2 72  ? -31.119 -0.460  -5.395  1.00 35.33  ? 81  GLY   B CA  1 
ATOM   836  C  C   . GLY   B 2 72  ? -29.878 -1.301  -5.435  1.00 34.97  ? 81  GLY   B C   1 
ATOM   837  O  O   . GLY   B 2 72  ? -28.784 -0.801  -5.723  1.00 34.78  ? 81  GLY   B O   1 
ATOM   838  N  N   . PRO   B 2 73  ? -30.042 -2.594  -5.112  1.00 34.79  ? 82  PRO   B N   1 
ATOM   839  C  CA  . PRO   B 2 73  ? -28.900 -3.522  -5.171  1.00 35.56  ? 82  PRO   B CA  1 
ATOM   840  C  C   . PRO   B 2 73  ? -28.342 -3.734  -6.578  1.00 37.56  ? 82  PRO   B C   1 
ATOM   841  O  O   . PRO   B 2 73  ? -29.051 -3.493  -7.556  1.00 38.42  ? 82  PRO   B O   1 
ATOM   842  C  CB  . PRO   B 2 73  ? -29.495 -4.840  -4.665  1.00 35.75  ? 82  PRO   B CB  1 
ATOM   843  C  CG  . PRO   B 2 73  ? -30.956 -4.744  -4.956  1.00 35.58  ? 82  PRO   B CG  1 
ATOM   844  C  CD  . PRO   B 2 73  ? -31.297 -3.285  -4.755  1.00 33.86  ? 82  PRO   B CD  1 
ATOM   845  N  N   . TRP   B 2 74  ? -27.087 -4.249  -6.686  1.00 37.86  ? 83  TRP   B N   1 
ATOM   846  C  CA  . TRP   B 2 74  ? -26.431 -4.538  -7.963  1.00 38.36  ? 83  TRP   B CA  1 
ATOM   847  C  C   . TRP   B 2 74  ? -27.297 -5.528  -8.756  1.00 40.52  ? 83  TRP   B C   1 
ATOM   848  O  O   . TRP   B 2 74  ? -27.659 -6.569  -8.208  1.00 40.69  ? 83  TRP   B O   1 
ATOM   849  C  CB  . TRP   B 2 74  ? -25.009 -5.103  -7.717  1.00 37.51  ? 83  TRP   B CB  1 
ATOM   850  C  CG  . TRP   B 2 74  ? -24.179 -5.245  -8.967  1.00 36.27  ? 83  TRP   B CG  1 
ATOM   851  C  CD1 . TRP   B 2 74  ? -24.097 -6.340  -9.774  1.00 36.36  ? 83  TRP   B CD1 1 
ATOM   852  C  CD2 . TRP   B 2 74  ? -23.332 -4.247  -9.556  1.00 36.11  ? 83  TRP   B CD2 1 
ATOM   853  N  NE1 . TRP   B 2 74  ? -23.266 -6.085  -10.840 1.00 36.02  ? 83  TRP   B NE1 1 
ATOM   854  C  CE2 . TRP   B 2 74  ? -22.798 -4.800  -10.744 1.00 36.39  ? 83  TRP   B CE2 1 
ATOM   855  C  CE3 . TRP   B 2 74  ? -23.010 -2.922  -9.222  1.00 36.47  ? 83  TRP   B CE3 1 
ATOM   856  C  CZ2 . TRP   B 2 74  ? -21.934 -4.084  -11.582 1.00 37.11  ? 83  TRP   B CZ2 1 
ATOM   857  C  CZ3 . TRP   B 2 74  ? -22.163 -2.211  -10.054 1.00 37.28  ? 83  TRP   B CZ3 1 
ATOM   858  C  CH2 . TRP   B 2 74  ? -21.634 -2.790  -11.221 1.00 37.44  ? 83  TRP   B CH2 1 
ATOM   859  N  N   . LYS   B 2 75  ? -27.677 -5.172  -10.019 1.00 41.18  ? 84  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 2 75  ? -28.578 -5.948  -10.877 1.00 42.08  ? 84  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 2 75  ? -27.898 -6.745  -11.996 1.00 43.82  ? 84  LYS   B C   1 
ATOM   862  O  O   . LYS   B 2 75  ? -28.551 -7.587  -12.611 1.00 44.24  ? 84  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 2 75  ? -29.623 -5.025  -11.532 1.00 42.38  ? 84  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 2 75  ? -30.518 -4.279  -10.564 1.00 44.06  ? 84  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 2 75  ? -31.528 -5.198  -9.918  1.00 45.75  ? 84  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 2 75  ? -32.107 -4.576  -8.679  1.00 48.80  ? 84  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 2 75  ? -33.494 -4.111  -8.899  1.00 51.61  ? 84  LYS   B NZ  1 
ATOM   868  N  N   . LEU   B 2 76  ? -26.641 -6.425  -12.328 1.00 44.37  ? 85  LEU   B N   1 
ATOM   869  C  CA  . LEU   B 2 76  ? -25.929 -7.059  -13.450 1.00 44.63  ? 85  LEU   B CA  1 
ATOM   870  C  C   . LEU   B 2 76  ? -25.231 -8.351  -13.024 1.00 46.21  ? 85  LEU   B C   1 
ATOM   871  O  O   . LEU   B 2 76  ? -24.379 -8.316  -12.150 1.00 46.62  ? 85  LEU   B O   1 
ATOM   872  C  CB  . LEU   B 2 76  ? -24.914 -6.084  -14.058 1.00 43.89  ? 85  LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 2 76  ? -25.361 -4.638  -14.247 1.00 43.68  ? 85  LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 2 76  ? -24.225 -3.786  -14.740 1.00 43.76  ? 85  LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 2 76  ? -26.514 -4.547  -15.203 1.00 43.84  ? 85  LEU   B CD2 1 
ATOM   876  N  N   . ASP   B 2 77  ? -25.570 -9.483  -13.644 1.00 47.40  ? 86  ASP   B N   1 
ATOM   877  C  CA  . ASP   B 2 77  ? -25.010 -10.773 -13.225 1.00 49.01  ? 86  ASP   B CA  1 
ATOM   878  C  C   . ASP   B 2 77  ? -24.432 -11.649 -14.374 1.00 49.80  ? 86  ASP   B C   1 
ATOM   879  O  O   . ASP   B 2 77  ? -23.795 -12.664 -14.092 1.00 50.34  ? 86  ASP   B O   1 
ATOM   880  C  CB  . ASP   B 2 77  ? -26.057 -11.556 -12.409 1.00 51.02  ? 86  ASP   B CB  1 
ATOM   881  C  CG  . ASP   B 2 77  ? -27.372 -11.816 -13.135 1.00 57.08  ? 86  ASP   B CG  1 
ATOM   882  O  OD1 . ASP   B 2 77  ? -27.535 -11.329 -14.280 1.00 56.75  ? 86  ASP   B OD1 1 
ATOM   883  O  OD2 . ASP   B 2 77  ? -28.241 -12.502 -12.559 1.00 61.57  ? 86  ASP   B OD2 1 
ATOM   884  N  N   . ALA   B 2 78  ? -24.617 -11.257 -15.642 1.00 49.52  ? 87  ALA   B N   1 
ATOM   885  C  CA  . ALA   B 2 78  ? -24.066 -12.020 -16.768 1.00 49.88  ? 87  ALA   B CA  1 
ATOM   886  C  C   . ALA   B 2 78  ? -22.527 -12.123 -16.666 1.00 50.49  ? 87  ALA   B C   1 
ATOM   887  O  O   . ALA   B 2 78  ? -21.878 -11.228 -16.102 1.00 51.15  ? 87  ALA   B O   1 
ATOM   888  C  CB  . ALA   B 2 78  ? -24.472 -11.383 -18.085 1.00 49.49  ? 87  ALA   B CB  1 
ATOM   889  N  N   . ALA   B 2 79  ? -21.957 -13.230 -17.151 1.00 49.64  ? 88  ALA   B N   1 
ATOM   890  C  CA  . ALA   B 2 79  ? -20.525 -13.465 -17.049 1.00 49.52  ? 88  ALA   B CA  1 
ATOM   891  C  C   . ALA   B 2 79  ? -19.898 -13.786 -18.393 1.00 49.84  ? 88  ALA   B C   1 
ATOM   892  O  O   . ALA   B 2 79  ? -20.555 -14.390 -19.243 1.00 49.47  ? 88  ALA   B O   1 
ATOM   893  C  CB  . ALA   B 2 79  ? -20.272 -14.615 -16.090 1.00 49.44  ? 88  ALA   B CB  1 
ATOM   894  N  N   . TRP   B 2 80  ? -18.606 -13.410 -18.582 1.00 50.41  ? 89  TRP   B N   1 
ATOM   895  C  CA  . TRP   B 2 80  ? -17.850 -13.736 -19.798 1.00 51.64  ? 89  TRP   B CA  1 
ATOM   896  C  C   . TRP   B 2 80  ? -17.701 -15.264 -19.831 1.00 53.57  ? 89  TRP   B C   1 
ATOM   897  O  O   . TRP   B 2 80  ? -17.428 -15.857 -18.795 1.00 52.59  ? 89  TRP   B O   1 
ATOM   898  C  CB  . TRP   B 2 80  ? -16.469 -13.036 -19.823 1.00 50.98  ? 89  TRP   B CB  1 
ATOM   899  C  CG  . TRP   B 2 80  ? -15.626 -13.389 -21.028 1.00 51.03  ? 89  TRP   B CG  1 
ATOM   900  C  CD1 . TRP   B 2 80  ? -15.999 -13.322 -22.338 1.00 52.08  ? 89  TRP   B CD1 1 
ATOM   901  C  CD2 . TRP   B 2 80  ? -14.246 -13.786 -21.026 1.00 50.61  ? 89  TRP   B CD2 1 
ATOM   902  N  NE1 . TRP   B 2 80  ? -14.951 -13.698 -23.151 1.00 52.28  ? 89  TRP   B NE1 1 
ATOM   903  C  CE2 . TRP   B 2 80  ? -13.869 -14.007 -22.368 1.00 51.67  ? 89  TRP   B CE2 1 
ATOM   904  C  CE3 . TRP   B 2 80  ? -13.298 -14.003 -20.022 1.00 51.05  ? 89  TRP   B CE3 1 
ATOM   905  C  CZ2 . TRP   B 2 80  ? -12.586 -14.438 -22.724 1.00 51.76  ? 89  TRP   B CZ2 1 
ATOM   906  C  CZ3 . TRP   B 2 80  ? -12.036 -14.447 -20.379 1.00 51.63  ? 89  TRP   B CZ3 1 
ATOM   907  C  CH2 . TRP   B 2 80  ? -11.681 -14.623 -21.718 1.00 51.30  ? 89  TRP   B CH2 1 
ATOM   908  N  N   . ASP   B 2 81  ? -17.984 -15.908 -20.982 1.00 55.95  ? 90  ASP   B N   1 
ATOM   909  C  CA  . ASP   B 2 81  ? -17.930 -17.382 -21.052 1.00 58.12  ? 90  ASP   B CA  1 
ATOM   910  C  C   . ASP   B 2 81  ? -16.521 -17.981 -21.086 1.00 60.62  ? 90  ASP   B C   1 
ATOM   911  O  O   . ASP   B 2 81  ? -16.378 -19.206 -21.001 1.00 61.48  ? 90  ASP   B O   1 
ATOM   912  C  CB  . ASP   B 2 81  ? -18.765 -17.939 -22.219 1.00 58.89  ? 90  ASP   B CB  1 
ATOM   913  C  CG  . ASP   B 2 81  ? -18.385 -17.462 -23.600 1.00 64.40  ? 90  ASP   B CG  1 
ATOM   914  O  OD1 . ASP   B 2 81  ? -17.350 -16.774 -23.730 1.00 65.53  ? 90  ASP   B OD1 1 
ATOM   915  O  OD2 . ASP   B 2 81  ? -19.129 -17.771 -24.561 1.00 66.89  ? 90  ASP   B OD2 1 
ATOM   916  N  N   . GLY   B 2 82  ? -15.507 -17.131 -21.210 1.00 61.46  ? 91  GLY   B N   1 
ATOM   917  C  CA  . GLY   B 2 82  ? -14.119 -17.557 -21.280 1.00 62.40  ? 91  GLY   B CA  1 
ATOM   918  C  C   . GLY   B 2 82  ? -13.635 -17.839 -22.688 1.00 63.42  ? 91  GLY   B C   1 
ATOM   919  O  O   . GLY   B 2 82  ? -12.445 -18.077 -22.875 1.00 64.07  ? 91  GLY   B O   1 
ATOM   920  N  N   . LEU   B 2 83  ? -14.526 -17.823 -23.699 1.00 63.80  ? 92  LEU   B N   1 
ATOM   921  C  CA  . LEU   B 2 83  ? -14.132 -18.137 -25.075 1.00 64.57  ? 92  LEU   B CA  1 
ATOM   922  C  C   . LEU   B 2 83  ? -14.458 -17.083 -26.108 1.00 64.65  ? 92  LEU   B C   1 
ATOM   923  O  O   . LEU   B 2 83  ? -13.710 -16.907 -27.070 1.00 65.14  ? 92  LEU   B O   1 
ATOM   924  C  CB  . LEU   B 2 83  ? -14.853 -19.408 -25.543 1.00 65.74  ? 92  LEU   B CB  1 
ATOM   925  C  CG  . LEU   B 2 83  ? -14.649 -20.709 -24.809 1.00 68.11  ? 92  LEU   B CG  1 
ATOM   926  C  CD1 . LEU   B 2 83  ? -15.338 -21.821 -25.572 1.00 68.94  ? 92  LEU   B CD1 1 
ATOM   927  C  CD2 . LEU   B 2 83  ? -13.173 -21.041 -24.675 1.00 69.17  ? 92  LEU   B CD2 1 
ATOM   928  N  N   . SER   B 2 84  ? -15.638 -16.478 -26.003 1.00 64.19  ? 93  SER   B N   1 
ATOM   929  C  CA  . SER   B 2 84  ? -16.152 -15.579 -27.022 1.00 63.72  ? 93  SER   B CA  1 
ATOM   930  C  C   . SER   B 2 84  ? -15.637 -14.149 -26.974 1.00 62.09  ? 93  SER   B C   1 
ATOM   931  O  O   . SER   B 2 84  ? -15.221 -13.657 -25.918 1.00 61.91  ? 93  SER   B O   1 
ATOM   932  C  CB  . SER   B 2 84  ? -17.680 -15.570 -26.985 1.00 65.85  ? 93  SER   B CB  1 
ATOM   933  O  OG  . SER   B 2 84  ? -18.233 -16.864 -26.812 1.00 68.41  ? 93  SER   B OG  1 
ATOM   934  N  N   . GLU   B 2 85  ? -15.696 -13.479 -28.137 1.00 60.47  ? 94  GLU   B N   1 
ATOM   935  C  CA  . GLU   B 2 85  ? -15.366 -12.068 -28.252 1.00 59.43  ? 94  GLU   B CA  1 
ATOM   936  C  C   . GLU   B 2 85  ? -16.509 -11.261 -27.581 1.00 57.71  ? 94  GLU   B C   1 
ATOM   937  O  O   . GLU   B 2 85  ? -17.641 -11.737 -27.416 1.00 57.73  ? 94  GLU   B O   1 
ATOM   938  C  CB  . GLU   B 2 85  ? -15.155 -11.635 -29.727 1.00 61.89  ? 94  GLU   B CB  1 
ATOM   939  C  CG  . GLU   B 2 85  ? -13.847 -12.112 -30.355 1.00 66.10  ? 94  GLU   B CG  1 
ATOM   940  C  CD  . GLU   B 2 85  ? -13.309 -11.304 -31.521 1.00 72.51  ? 94  GLU   B CD  1 
ATOM   941  O  OE1 . GLU   B 2 85  ? -14.117 -10.667 -32.235 1.00 74.15  ? 94  GLU   B OE1 1 
ATOM   942  O  OE2 . GLU   B 2 85  ? -12.074 -11.309 -31.726 1.00 74.16  ? 94  GLU   B OE2 1 
ATOM   943  N  N   . VAL   B 2 86  ? -16.167 -10.075 -27.104 1.00 55.29  ? 95  VAL   B N   1 
ATOM   944  C  CA  . VAL   B 2 86  ? -17.076 -9.189  -26.391 1.00 52.77  ? 95  VAL   B CA  1 
ATOM   945  C  C   . VAL   B 2 86  ? -16.967 -7.802  -27.028 1.00 51.95  ? 95  VAL   B C   1 
ATOM   946  O  O   . VAL   B 2 86  ? -16.083 -7.567  -27.871 1.00 52.63  ? 95  VAL   B O   1 
ATOM   947  C  CB  . VAL   B 2 86  ? -16.735 -9.150  -24.850 1.00 51.09  ? 95  VAL   B CB  1 
ATOM   948  C  CG1 . VAL   B 2 86  ? -16.559 -10.553 -24.277 1.00 50.69  ? 95  VAL   B CG1 1 
ATOM   949  C  CG2 . VAL   B 2 86  ? -15.488 -8.312  -24.585 1.00 50.64  ? 95  VAL   B CG2 1 
ATOM   950  N  N   . GLN   B 2 87  ? -17.861 -6.880  -26.639 1.00 50.33  ? 96  GLN   B N   1 
ATOM   951  C  CA  . GLN   B 2 87  ? -17.769 -5.516  -27.111 1.00 49.64  ? 96  GLN   B CA  1 
ATOM   952  C  C   . GLN   B 2 87  ? -17.703 -4.577  -25.918 1.00 49.28  ? 96  GLN   B C   1 
ATOM   953  O  O   . GLN   B 2 87  ? -18.482 -4.712  -24.980 1.00 48.91  ? 96  GLN   B O   1 
ATOM   954  C  CB  . GLN   B 2 87  ? -18.943 -5.144  -28.045 1.00 50.24  ? 96  GLN   B CB  1 
ATOM   955  C  CG  . GLN   B 2 87  ? -18.761 -5.718  -29.440 1.00 52.78  ? 96  GLN   B CG  1 
ATOM   956  C  CD  . GLN   B 2 87  ? -19.825 -5.330  -30.440 1.00 57.04  ? 96  GLN   B CD  1 
ATOM   957  O  OE1 . GLN   B 2 87  ? -20.749 -4.571  -30.166 1.00 57.77  ? 96  GLN   B OE1 1 
ATOM   958  N  NE2 . GLN   B 2 87  ? -19.719 -5.863  -31.642 1.00 57.86  ? 96  GLN   B NE2 1 
ATOM   959  N  N   . LEU   B 2 88  ? -16.773 -3.626  -25.959 1.00 48.53  ? 97  LEU   B N   1 
ATOM   960  C  CA  . LEU   B 2 88  ? -16.714 -2.558  -24.989 1.00 47.78  ? 97  LEU   B CA  1 
ATOM   961  C  C   . LEU   B 2 88  ? -17.575 -1.435  -25.622 1.00 47.49  ? 97  LEU   B C   1 
ATOM   962  O  O   . LEU   B 2 88  ? -17.315 -1.007  -26.759 1.00 47.62  ? 97  LEU   B O   1 
ATOM   963  C  CB  . LEU   B 2 88  ? -15.261 -2.082  -24.790 1.00 47.57  ? 97  LEU   B CB  1 
ATOM   964  C  CG  . LEU   B 2 88  ? -15.089 -0.720  -24.106 1.00 48.16  ? 97  LEU   B CG  1 
ATOM   965  C  CD1 . LEU   B 2 88  ? -15.683 -0.723  -22.706 1.00 48.04  ? 97  LEU   B CD1 1 
ATOM   966  C  CD2 . LEU   B 2 88  ? -13.648 -0.280  -24.105 1.00 48.65  ? 97  LEU   B CD2 1 
ATOM   967  N  N   . LEU   B 2 89  ? -18.639 -1.015  -24.924 1.00 46.42  ? 98  LEU   B N   1 
ATOM   968  C  CA  . LEU   B 2 89  ? -19.458 0.082   -25.402 1.00 46.13  ? 98  LEU   B CA  1 
ATOM   969  C  C   . LEU   B 2 89  ? -18.802 1.297   -24.777 1.00 46.30  ? 98  LEU   B C   1 
ATOM   970  O  O   . LEU   B 2 89  ? -19.101 1.663   -23.635 1.00 45.13  ? 98  LEU   B O   1 
ATOM   971  C  CB  . LEU   B 2 89  ? -20.931 -0.067  -24.984 1.00 46.26  ? 98  LEU   B CB  1 
ATOM   972  C  CG  . LEU   B 2 89  ? -21.921 1.062   -25.388 1.00 48.16  ? 98  LEU   B CG  1 
ATOM   973  C  CD1 . LEU   B 2 89  ? -21.761 1.495   -26.824 1.00 49.74  ? 98  LEU   B CD1 1 
ATOM   974  C  CD2 . LEU   B 2 89  ? -23.354 0.632   -25.173 1.00 48.66  ? 98  LEU   B CD2 1 
ATOM   975  N  N   . ALA   B 2 90  ? -17.801 1.846   -25.492 1.00 46.87  ? 99  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 90  ? -17.007 2.962   -24.990 1.00 47.25  ? 99  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 90  ? -17.719 4.284   -25.107 1.00 47.10  ? 99  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 90  ? -18.230 4.617   -26.174 1.00 47.19  ? 99  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 90  ? -15.666 3.022   -25.710 1.00 47.27  ? 99  ALA   B CB  1 
ATOM   980  N  N   . VAL   B 2 91  ? -17.795 5.041   -23.996 1.00 46.41  ? 100 VAL   B N   1 
ATOM   981  C  CA  . VAL   B 2 91  ? -18.426 6.355   -24.023 1.00 46.48  ? 100 VAL   B CA  1 
ATOM   982  C  C   . VAL   B 2 91  ? -17.355 7.380   -23.641 1.00 47.38  ? 100 VAL   B C   1 
ATOM   983  O  O   . VAL   B 2 91  ? -17.267 7.778   -22.477 1.00 47.58  ? 100 VAL   B O   1 
ATOM   984  C  CB  . VAL   B 2 91  ? -19.683 6.425   -23.124 1.00 46.55  ? 100 VAL   B CB  1 
ATOM   985  C  CG1 . VAL   B 2 91  ? -20.351 7.799   -23.223 1.00 47.16  ? 100 VAL   B CG1 1 
ATOM   986  C  CG2 . VAL   B 2 91  ? -20.670 5.312   -23.480 1.00 46.31  ? 100 VAL   B CG2 1 
ATOM   987  N  N   . PRO   B 2 92  ? -16.523 7.814   -24.617 1.00 47.69  ? 101 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 92  ? -15.429 8.740   -24.297 1.00 47.64  ? 101 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 92  ? -15.881 10.169  -24.042 1.00 47.70  ? 101 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 92  ? -16.881 10.621  -24.596 1.00 46.91  ? 101 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 92  ? -14.504 8.640   -25.531 1.00 49.00  ? 101 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 92  ? -15.059 7.522   -26.392 1.00 49.45  ? 101 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 92  ? -16.508 7.452   -26.048 1.00 47.55  ? 101 PRO   B CD  1 
ATOM   994  N  N   . PRO   B 2 93  ? -15.109 10.920  -23.249 1.00 48.69  ? 102 PRO   B N   1 
ATOM   995  C  CA  . PRO   B 2 93  ? -15.491 12.314  -22.964 1.00 49.65  ? 102 PRO   B CA  1 
ATOM   996  C  C   . PRO   B 2 93  ? -15.658 13.164  -24.218 1.00 51.13  ? 102 PRO   B C   1 
ATOM   997  O  O   . PRO   B 2 93  ? -14.793 13.154  -25.093 1.00 51.27  ? 102 PRO   B O   1 
ATOM   998  C  CB  . PRO   B 2 93  ? -14.348 12.809  -22.069 1.00 49.89  ? 102 PRO   B CB  1 
ATOM   999  C  CG  . PRO   B 2 93  ? -13.863 11.537  -21.375 1.00 50.09  ? 102 PRO   B CG  1 
ATOM   1000 C  CD  . PRO   B 2 93  ? -13.903 10.526  -22.493 1.00 48.34  ? 102 PRO   B CD  1 
ATOM   1001 N  N   . GLY   B 2 94  ? -16.815 13.817  -24.323 1.00 51.69  ? 103 GLY   B N   1 
ATOM   1002 C  CA  . GLY   B 2 94  ? -17.183 14.697  -25.436 1.00 51.91  ? 103 GLY   B CA  1 
ATOM   1003 C  C   . GLY   B 2 94  ? -17.340 14.014  -26.780 1.00 52.52  ? 103 GLY   B C   1 
ATOM   1004 O  O   . GLY   B 2 94  ? -17.423 14.684  -27.807 1.00 53.28  ? 103 GLY   B O   1 
ATOM   1005 N  N   . GLU   B 2 95  ? -17.340 12.682  -26.799 1.00 52.53  ? 104 GLU   B N   1 
ATOM   1006 C  CA  . GLU   B 2 95  ? -17.441 11.890  -28.026 1.00 53.00  ? 104 GLU   B CA  1 
ATOM   1007 C  C   . GLU   B 2 95  ? -18.601 10.905  -27.926 1.00 53.65  ? 104 GLU   B C   1 
ATOM   1008 O  O   . GLU   B 2 95  ? -18.989 10.520  -26.839 1.00 53.45  ? 104 GLU   B O   1 
ATOM   1009 C  CB  . GLU   B 2 95  ? -16.115 11.124  -28.300 1.00 53.70  ? 104 GLU   B CB  1 
ATOM   1010 C  CG  . GLU   B 2 95  ? -14.938 12.055  -28.534 1.00 56.09  ? 104 GLU   B CG  1 
ATOM   1011 C  CD  . GLU   B 2 95  ? -13.581 11.395  -28.669 1.00 59.80  ? 104 GLU   B CD  1 
ATOM   1012 O  OE1 . GLU   B 2 95  ? -13.485 10.164  -28.471 1.00 57.87  ? 104 GLU   B OE1 1 
ATOM   1013 O  OE2 . GLU   B 2 95  ? -12.606 12.119  -28.973 1.00 62.00  ? 104 GLU   B OE2 1 
ATOM   1014 N  N   . ARG   B 2 96  ? -19.139 10.496  -29.064 1.00 54.24  ? 105 ARG   B N   1 
ATOM   1015 C  CA  . ARG   B 2 96  ? -20.270 9.581   -29.172 1.00 55.05  ? 105 ARG   B CA  1 
ATOM   1016 C  C   . ARG   B 2 96  ? -19.945 8.176   -28.663 1.00 54.51  ? 105 ARG   B C   1 
ATOM   1017 O  O   . ARG   B 2 96  ? -18.802 7.738   -28.784 1.00 54.61  ? 105 ARG   B O   1 
ATOM   1018 C  CB  . ARG   B 2 96  ? -20.634 9.475   -30.661 1.00 58.00  ? 105 ARG   B CB  1 
ATOM   1019 C  CG  . ARG   B 2 96  ? -22.089 9.164   -30.950 1.00 63.96  ? 105 ARG   B CG  1 
ATOM   1020 C  CD  . ARG   B 2 96  ? -22.622 10.075  -32.050 1.00 69.65  ? 105 ARG   B CD  1 
ATOM   1021 N  NE  . ARG   B 2 96  ? -21.865 9.944   -33.292 1.00 75.29  ? 105 ARG   B NE  1 
ATOM   1022 C  CZ  . ARG   B 2 96  ? -21.474 10.967  -34.050 1.00 79.77  ? 105 ARG   B CZ  1 
ATOM   1023 N  NH1 . ARG   B 2 96  ? -21.768 12.217  -33.698 1.00 78.99  ? 105 ARG   B NH1 1 
ATOM   1024 N  NH2 . ARG   B 2 96  ? -20.793 10.749  -35.169 1.00 81.03  ? 105 ARG   B NH2 1 
ATOM   1025 N  N   . ALA   B 2 97  ? -20.971 7.449   -28.156 1.00 53.64  ? 106 ALA   B N   1 
ATOM   1026 C  CA  . ALA   B 2 97  ? -20.867 6.051   -27.748 1.00 53.67  ? 106 ALA   B CA  1 
ATOM   1027 C  C   . ALA   B 2 97  ? -20.403 5.209   -28.962 1.00 53.79  ? 106 ALA   B C   1 
ATOM   1028 O  O   . ALA   B 2 97  ? -20.897 5.417   -30.064 1.00 54.58  ? 106 ALA   B O   1 
ATOM   1029 C  CB  . ALA   B 2 97  ? -22.224 5.558   -27.271 1.00 53.61  ? 106 ALA   B CB  1 
ATOM   1030 N  N   . LYS   B 2 98  ? -19.461 4.289   -28.775 1.00 53.54  ? 107 LYS   B N   1 
ATOM   1031 C  CA  . LYS   B 2 98  ? -18.920 3.495   -29.887 1.00 54.04  ? 107 LYS   B CA  1 
ATOM   1032 C  C   . LYS   B 2 98  ? -18.635 2.076   -29.442 1.00 53.43  ? 107 LYS   B C   1 
ATOM   1033 O  O   . LYS   B 2 98  ? -17.983 1.909   -28.418 1.00 53.13  ? 107 LYS   B O   1 
ATOM   1034 C  CB  . LYS   B 2 98  ? -17.617 4.161   -30.343 1.00 57.64  ? 107 LYS   B CB  1 
ATOM   1035 C  CG  . LYS   B 2 98  ? -16.855 3.473   -31.451 1.00 66.08  ? 107 LYS   B CG  1 
ATOM   1036 C  CD  . LYS   B 2 98  ? -15.509 4.196   -31.730 1.00 73.02  ? 107 LYS   B CD  1 
ATOM   1037 C  CE  . LYS   B 2 98  ? -14.728 4.471   -30.446 1.00 78.14  ? 107 LYS   B CE  1 
ATOM   1038 N  NZ  . LYS   B 2 98  ? -13.330 3.958   -30.516 1.00 81.39  ? 107 LYS   B NZ  1 
ATOM   1039 N  N   . ASN   B 2 99  ? -19.114 1.051   -30.189 1.00 52.66  ? 108 ASN   B N   1 
ATOM   1040 C  CA  . ASN   B 2 99  ? -18.847 -0.353  -29.842 1.00 52.19  ? 108 ASN   B CA  1 
ATOM   1041 C  C   . ASN   B 2 99  ? -17.509 -0.780  -30.392 1.00 52.51  ? 108 ASN   B C   1 
ATOM   1042 O  O   . ASN   B 2 99  ? -17.221 -0.536  -31.561 1.00 53.09  ? 108 ASN   B O   1 
ATOM   1043 C  CB  . ASN   B 2 99  ? -19.917 -1.310  -30.368 1.00 51.93  ? 108 ASN   B CB  1 
ATOM   1044 C  CG  . ASN   B 2 99  ? -21.292 -1.051  -29.834 1.00 54.32  ? 108 ASN   B CG  1 
ATOM   1045 O  OD1 . ASN   B 2 99  ? -21.829 0.042   -29.981 1.00 55.36  ? 108 ASN   B OD1 1 
ATOM   1046 N  ND2 . ASN   B 2 99  ? -21.903 -2.053  -29.227 1.00 54.31  ? 108 ASN   B ND2 1 
ATOM   1047 N  N   . ILE   B 2 100 ? -16.691 -1.409  -29.563 1.00 51.74  ? 109 ILE   B N   1 
ATOM   1048 C  CA  . ILE   B 2 100 ? -15.378 -1.897  -29.960 1.00 52.91  ? 109 ILE   B CA  1 
ATOM   1049 C  C   . ILE   B 2 100 ? -15.296 -3.354  -29.597 1.00 52.38  ? 109 ILE   B C   1 
ATOM   1050 O  O   . ILE   B 2 100 ? -15.343 -3.695  -28.416 1.00 52.01  ? 109 ILE   B O   1 
ATOM   1051 C  CB  . ILE   B 2 100 ? -14.242 -1.133  -29.262 1.00 54.47  ? 109 ILE   B CB  1 
ATOM   1052 C  CG1 . ILE   B 2 100 ? -14.380 0.371   -29.492 1.00 56.55  ? 109 ILE   B CG1 1 
ATOM   1053 C  CG2 . ILE   B 2 100 ? -12.864 -1.683  -29.709 1.00 54.59  ? 109 ILE   B CG2 1 
ATOM   1054 C  CD1 . ILE   B 2 100 ? -14.203 0.783   -30.964 1.00 58.84  ? 109 ILE   B CD1 1 
ATOM   1055 N  N   . GLN   B 2 101 ? -15.175 -4.209  -30.595 1.00 51.99  ? 110 GLN   B N   1 
ATOM   1056 C  CA  . GLN   B 2 101 ? -15.117 -5.640  -30.377 1.00 53.19  ? 110 GLN   B CA  1 
ATOM   1057 C  C   . GLN   B 2 101 ? -13.698 -6.133  -30.158 1.00 54.21  ? 110 GLN   B C   1 
ATOM   1058 O  O   . GLN   B 2 101 ? -12.774 -5.733  -30.876 1.00 55.12  ? 110 GLN   B O   1 
ATOM   1059 C  CB  . GLN   B 2 101 ? -15.750 -6.363  -31.555 1.00 55.43  ? 110 GLN   B CB  1 
ATOM   1060 C  CG  . GLN   B 2 101 ? -15.936 -7.848  -31.314 1.00 59.08  ? 110 GLN   B CG  1 
ATOM   1061 C  CD  . GLN   B 2 101 ? -16.879 -8.414  -32.335 1.00 63.30  ? 110 GLN   B CD  1 
ATOM   1062 O  OE1 . GLN   B 2 101 ? -17.866 -7.773  -32.737 1.00 63.91  ? 110 GLN   B OE1 1 
ATOM   1063 N  NE2 . GLN   B 2 101 ? -16.601 -9.629  -32.763 1.00 64.11  ? 110 GLN   B NE2 1 
ATOM   1064 N  N   . THR   B 2 102 ? -13.512 -7.022  -29.167 1.00 53.45  ? 111 THR   B N   1 
ATOM   1065 C  CA  . THR   B 2 102 ? -12.200 -7.544  -28.851 1.00 53.57  ? 111 THR   B CA  1 
ATOM   1066 C  C   . THR   B 2 102 ? -12.319 -8.913  -28.187 1.00 54.10  ? 111 THR   B C   1 
ATOM   1067 O  O   . THR   B 2 102 ? -13.385 -9.240  -27.663 1.00 55.40  ? 111 THR   B O   1 
ATOM   1068 C  CB  . THR   B 2 102 ? -11.486 -6.526  -27.932 1.00 54.63  ? 111 THR   B CB  1 
ATOM   1069 O  OG1 . THR   B 2 102 ? -10.105 -6.885  -27.783 1.00 55.68  ? 111 THR   B OG1 1 
ATOM   1070 C  CG2 . THR   B 2 102 ? -12.194 -6.325  -26.574 1.00 54.95  ? 111 THR   B CG2 1 
ATOM   1071 N  N   . LEU   B 2 103 ? -11.235 -9.720  -28.180 1.00 53.60  ? 112 LEU   B N   1 
ATOM   1072 C  CA  . LEU   B 2 103 ? -11.256 -10.981 -27.448 1.00 53.29  ? 112 LEU   B CA  1 
ATOM   1073 C  C   . LEU   B 2 103 ? -10.509 -10.717 -26.158 1.00 52.72  ? 112 LEU   B C   1 
ATOM   1074 O  O   . LEU   B 2 103 ? -9.305  -10.415 -26.187 1.00 52.98  ? 112 LEU   B O   1 
ATOM   1075 C  CB  . LEU   B 2 103 ? -10.582 -12.164 -28.162 1.00 53.92  ? 112 LEU   B CB  1 
ATOM   1076 C  CG  . LEU   B 2 103 ? -10.707 -13.456 -27.349 1.00 56.57  ? 112 LEU   B CG  1 
ATOM   1077 C  CD1 . LEU   B 2 103 ? -12.032 -14.086 -27.571 1.00 57.67  ? 112 LEU   B CD1 1 
ATOM   1078 C  CD2 . LEU   B 2 103 ? -9.588  -14.419 -27.623 1.00 57.97  ? 112 LEU   B CD2 1 
ATOM   1079 N  N   . PRO   B 2 104 ? -11.160 -10.943 -25.012 1.00 51.63  ? 113 PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 2 104 ? -10.478 -10.696 -23.749 1.00 51.39  ? 113 PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 2 104 ? -9.328  -11.648 -23.424 1.00 52.99  ? 113 PRO   B C   1 
ATOM   1082 O  O   . PRO   B 2 104 ? -9.270  -12.797 -23.875 1.00 53.73  ? 113 PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 2 104 ? -11.599 -10.795 -22.704 1.00 51.73  ? 113 PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 2 104 ? -12.856 -10.747 -23.435 1.00 52.03  ? 113 PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 2 104 ? -12.567 -11.317 -24.803 1.00 50.60  ? 113 PRO   B CD  1 
ATOM   1086 N  N   . GLY   B 2 105 ? -8.385  -11.101 -22.684 1.00 52.91  ? 114 GLY   B N   1 
ATOM   1087 C  CA  . GLY   B 2 105 ? -7.281  -11.816 -22.088 1.00 53.66  ? 114 GLY   B CA  1 
ATOM   1088 C  C   . GLY   B 2 105 ? -7.689  -12.241 -20.686 1.00 54.29  ? 114 GLY   B C   1 
ATOM   1089 O  O   . GLY   B 2 105 ? -8.884  -12.299 -20.371 1.00 54.17  ? 114 GLY   B O   1 
ATOM   1090 N  N   . ILE   B 2 106 ? -6.706  -12.556 -19.829 1.00 54.32  ? 115 ILE   B N   1 
ATOM   1091 C  CA  . ILE   B 2 106 ? -6.964  -13.037 -18.480 1.00 54.64  ? 115 ILE   B CA  1 
ATOM   1092 C  C   . ILE   B 2 106 ? -6.098  -12.319 -17.474 1.00 54.38  ? 115 ILE   B C   1 
ATOM   1093 O  O   . ILE   B 2 106 ? -4.928  -12.081 -17.724 1.00 54.45  ? 115 ILE   B O   1 
ATOM   1094 C  CB  . ILE   B 2 106 ? -6.666  -14.578 -18.400 1.00 56.09  ? 115 ILE   B CB  1 
ATOM   1095 C  CG1 . ILE   B 2 106 ? -7.638  -15.401 -19.236 1.00 57.55  ? 115 ILE   B CG1 1 
ATOM   1096 C  CG2 . ILE   B 2 106 ? -6.635  -15.107 -16.955 1.00 57.32  ? 115 ILE   B CG2 1 
ATOM   1097 C  CD1 . ILE   B 2 106 ? -9.005  -15.235 -18.839 1.00 59.18  ? 115 ILE   B CD1 1 
ATOM   1098 N  N   . PHE   B 2 107 ? -6.650  -12.060 -16.297 1.00 54.16  ? 116 PHE   B N   1 
ATOM   1099 C  CA  . PHE   B 2 107 ? -5.924  -11.574 -15.142 1.00 53.72  ? 116 PHE   B CA  1 
ATOM   1100 C  C   . PHE   B 2 107 ? -5.866  -12.789 -14.214 1.00 54.87  ? 116 PHE   B C   1 
ATOM   1101 O  O   . PHE   B 2 107 ? -6.909  -13.194 -13.692 1.00 55.05  ? 116 PHE   B O   1 
ATOM   1102 C  CB  . PHE   B 2 107 ? -6.740  -10.487 -14.430 1.00 52.60  ? 116 PHE   B CB  1 
ATOM   1103 C  CG  . PHE   B 2 107 ? -6.427  -9.054  -14.778 1.00 52.20  ? 116 PHE   B CG  1 
ATOM   1104 C  CD1 . PHE   B 2 107 ? -5.703  -8.741  -15.921 1.00 52.24  ? 116 PHE   B CD1 1 
ATOM   1105 C  CD2 . PHE   B 2 107 ? -6.895  -8.015  -13.987 1.00 52.53  ? 116 PHE   B CD2 1 
ATOM   1106 C  CE1 . PHE   B 2 107 ? -5.448  -7.416  -16.260 1.00 52.45  ? 116 PHE   B CE1 1 
ATOM   1107 C  CE2 . PHE   B 2 107 ? -6.629  -6.693  -14.324 1.00 52.94  ? 116 PHE   B CE2 1 
ATOM   1108 C  CZ  . PHE   B 2 107 ? -5.917  -6.400  -15.460 1.00 52.26  ? 116 PHE   B CZ  1 
ATOM   1109 N  N   . LYS   B 2 108 ? -4.679  -13.385 -14.008 1.00 55.13  ? 117 LYS   B N   1 
ATOM   1110 C  CA  . LYS   B 2 108 ? -4.550  -14.496 -13.078 1.00 55.84  ? 117 LYS   B CA  1 
ATOM   1111 C  C   . LYS   B 2 108 ? -4.258  -13.902 -11.709 1.00 55.77  ? 117 LYS   B C   1 
ATOM   1112 O  O   . LYS   B 2 108 ? -3.288  -13.159 -11.559 1.00 56.12  ? 117 LYS   B O   1 
ATOM   1113 C  CB  . LYS   B 2 108 ? -3.410  -15.458 -13.477 1.00 58.84  ? 117 LYS   B CB  1 
ATOM   1114 C  CG  . LYS   B 2 108 ? -3.441  -15.904 -14.933 1.00 65.23  ? 117 LYS   B CG  1 
ATOM   1115 C  CD  . LYS   B 2 108 ? -2.536  -17.104 -15.188 1.00 71.74  ? 117 LYS   B CD  1 
ATOM   1116 C  CE  . LYS   B 2 108 ? -2.203  -17.252 -16.658 1.00 77.10  ? 117 LYS   B CE  1 
ATOM   1117 N  NZ  . LYS   B 2 108 ? -1.352  -18.447 -16.937 1.00 79.56  ? 117 LYS   B NZ  1 
ATOM   1118 N  N   . THR   B 2 109 ? -5.099  -14.207 -10.714 1.00 54.91  ? 118 THR   B N   1 
ATOM   1119 C  CA  . THR   B 2 109 ? -4.900  -13.735 -9.339  1.00 54.62  ? 118 THR   B CA  1 
ATOM   1120 C  C   . THR   B 2 109 ? -4.870  -14.941 -8.400  1.00 55.47  ? 118 THR   B C   1 
ATOM   1121 O  O   . THR   B 2 109 ? -5.373  -16.004 -8.762  1.00 55.17  ? 118 THR   B O   1 
ATOM   1122 C  CB  . THR   B 2 109 ? -6.005  -12.728 -8.894  1.00 54.78  ? 118 THR   B CB  1 
ATOM   1123 O  OG1 . THR   B 2 109 ? -7.171  -13.413 -8.433  1.00 55.15  ? 118 THR   B OG1 1 
ATOM   1124 C  CG2 . THR   B 2 109 ? -6.376  -11.725 -9.958  1.00 54.67  ? 118 THR   B CG2 1 
ATOM   1125 N  N   . LYS   B 2 110 ? -4.380  -14.750 -7.155  1.00 56.31  ? 119 LYS   B N   1 
ATOM   1126 C  CA  . LYS   B 2 110 ? -4.384  -15.796 -6.131  1.00 57.30  ? 119 LYS   B CA  1 
ATOM   1127 C  C   . LYS   B 2 110 ? -5.834  -16.248 -5.782  1.00 58.47  ? 119 LYS   B C   1 
ATOM   1128 O  O   . LYS   B 2 110 ? -6.018  -17.335 -5.230  1.00 58.93  ? 119 LYS   B O   1 
ATOM   1129 C  CB  . LYS   B 2 110 ? -3.646  -15.304 -4.873  1.00 58.28  ? 119 LYS   B CB  1 
ATOM   1130 C  CG  . LYS   B 2 110 ? -4.397  -14.216 -4.107  1.00 62.39  ? 119 LYS   B CG  1 
ATOM   1131 C  CD  . LYS   B 2 110 ? -3.523  -13.561 -3.040  1.00 66.37  ? 119 LYS   B CD  1 
ATOM   1132 C  CE  . LYS   B 2 110 ? -4.271  -13.251 -1.770  1.00 69.25  ? 119 LYS   B CE  1 
ATOM   1133 N  NZ  . LYS   B 2 110 ? -5.219  -12.130 -1.949  1.00 71.76  ? 119 LYS   B NZ  1 
ATOM   1134 N  N   . ASP   B 2 111 ? -6.854  -15.429 -6.121  1.00 58.30  ? 120 ASP   B N   1 
ATOM   1135 C  CA  . ASP   B 2 111 ? -8.251  -15.753 -5.867  1.00 58.85  ? 120 ASP   B CA  1 
ATOM   1136 C  C   . ASP   B 2 111 ? -9.008  -16.249 -7.123  1.00 59.34  ? 120 ASP   B C   1 
ATOM   1137 O  O   . ASP   B 2 111 ? -10.229 -16.393 -7.071  1.00 60.13  ? 120 ASP   B O   1 
ATOM   1138 C  CB  . ASP   B 2 111 ? -8.981  -14.549 -5.252  1.00 60.44  ? 120 ASP   B CB  1 
ATOM   1139 C  CG  . ASP   B 2 111 ? -8.528  -14.173 -3.851  1.00 66.12  ? 120 ASP   B CG  1 
ATOM   1140 O  OD1 . ASP   B 2 111 ? -7.835  -14.991 -3.210  1.00 67.09  ? 120 ASP   B OD1 1 
ATOM   1141 O  OD2 . ASP   B 2 111 ? -8.875  -13.062 -3.392  1.00 68.31  ? 120 ASP   B OD2 1 
ATOM   1142 N  N   . GLY   B 2 112 ? -8.306  -16.495 -8.226  1.00 58.53  ? 121 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 112 ? -8.941  -16.969 -9.448  1.00 58.45  ? 121 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 112 ? -8.815  -16.037 -10.641 1.00 57.96  ? 121 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 112 ? -8.443  -14.874 -10.484 1.00 57.91  ? 121 GLY   B O   1 
ATOM   1146 N  N   . ASP   B 2 113 ? -9.138  -16.545 -11.843 1.00 57.21  ? 122 ASP   B N   1 
ATOM   1147 C  CA  . ASP   B 2 113 ? -9.050  -15.786 -13.086 1.00 57.45  ? 122 ASP   B CA  1 
ATOM   1148 C  C   . ASP   B 2 113 ? -10.240 -14.859 -13.346 1.00 56.83  ? 122 ASP   B C   1 
ATOM   1149 O  O   . ASP   B 2 113 ? -11.388 -15.207 -13.076 1.00 56.76  ? 122 ASP   B O   1 
ATOM   1150 C  CB  . ASP   B 2 113 ? -8.889  -16.719 -14.301 1.00 59.10  ? 122 ASP   B CB  1 
ATOM   1151 C  CG  . ASP   B 2 113 ? -7.596  -17.510 -14.349 1.00 64.87  ? 122 ASP   B CG  1 
ATOM   1152 O  OD1 . ASP   B 2 113 ? -6.819  -17.443 -13.367 1.00 64.37  ? 122 ASP   B OD1 1 
ATOM   1153 O  OD2 . ASP   B 2 113 ? -7.359  -18.196 -15.377 1.00 68.64  ? 122 ASP   B OD2 1 
ATOM   1154 N  N   . ILE   B 2 114 ? -9.945  -13.695 -13.922 1.00 56.07  ? 123 ILE   B N   1 
ATOM   1155 C  CA  . ILE   B 2 114 ? -10.916 -12.677 -14.323 1.00 55.94  ? 123 ILE   B CA  1 
ATOM   1156 C  C   . ILE   B 2 114 ? -10.614 -12.348 -15.782 1.00 54.48  ? 123 ILE   B C   1 
ATOM   1157 O  O   . ILE   B 2 114 ? -9.447  -12.300 -16.169 1.00 54.06  ? 123 ILE   B O   1 
ATOM   1158 C  CB  . ILE   B 2 114 ? -10.769 -11.349 -13.506 1.00 57.52  ? 123 ILE   B CB  1 
ATOM   1159 C  CG1 . ILE   B 2 114 ? -10.440 -11.562 -12.039 1.00 59.78  ? 123 ILE   B CG1 1 
ATOM   1160 C  CG2 . ILE   B 2 114 ? -11.991 -10.466 -13.650 1.00 58.28  ? 123 ILE   B CG2 1 
ATOM   1161 C  CD1 . ILE   B 2 114 ? -10.007 -10.253 -11.317 1.00 61.95  ? 123 ILE   B CD1 1 
ATOM   1162 N  N   . GLY   B 2 115 ? -11.639 -12.029 -16.554 1.00 53.72  ? 124 GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 2 115 ? -11.442 -11.563 -17.921 1.00 53.58  ? 124 GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 2 115 ? -10.757 -10.202 -17.925 1.00 53.09  ? 124 GLY   B C   1 
ATOM   1165 O  O   . GLY   B 2 115 ? -10.784 -9.476  -16.920 1.00 52.69  ? 124 GLY   B O   1 
ATOM   1166 N  N   . ALA   B 2 116 ? -10.112 -9.851  -19.034 1.00 52.62  ? 125 ALA   B N   1 
ATOM   1167 C  CA  . ALA   B 2 116 ? -9.425  -8.566  -19.148 1.00 52.52  ? 125 ALA   B CA  1 
ATOM   1168 C  C   . ALA   B 2 116 ? -9.541  -8.016  -20.557 1.00 52.99  ? 125 ALA   B C   1 
ATOM   1169 O  O   . ALA   B 2 116 ? -9.281  -8.738  -21.498 1.00 53.59  ? 125 ALA   B O   1 
ATOM   1170 C  CB  . ALA   B 2 116 ? -7.959  -8.713  -18.773 1.00 52.12  ? 125 ALA   B CB  1 
ATOM   1171 N  N   . VAL   B 2 117 ? -9.911  -6.740  -20.707 1.00 52.70  ? 126 VAL   B N   1 
ATOM   1172 C  CA  A VAL   B 2 117 ? -10.017 -6.134  -22.027 0.50 53.32  ? 126 VAL   B CA  1 
ATOM   1173 C  CA  B VAL   B 2 117 ? -10.060 -6.079  -21.997 0.50 53.07  ? 126 VAL   B CA  1 
ATOM   1174 C  C   . VAL   B 2 117 ? -8.845  -5.178  -22.267 1.00 53.62  ? 126 VAL   B C   1 
ATOM   1175 O  O   . VAL   B 2 117 ? -8.595  -4.256  -21.495 1.00 53.62  ? 126 VAL   B O   1 
ATOM   1176 C  CB  A VAL   B 2 117 ? -11.403 -5.525  -22.317 0.50 54.20  ? 126 VAL   B CB  1 
ATOM   1177 C  CB  B VAL   B 2 117 ? -11.382 -5.288  -21.988 0.50 53.42  ? 126 VAL   B CB  1 
ATOM   1178 C  CG1 A VAL   B 2 117 ? -12.433 -6.630  -22.520 0.50 54.86  ? 126 VAL   B CG1 1 
ATOM   1179 C  CG1 B VAL   B 2 117 ? -11.532 -4.443  -23.240 0.50 54.07  ? 126 VAL   B CG1 1 
ATOM   1180 C  CG2 A VAL   B 2 117 ? -11.839 -4.580  -21.210 0.50 54.76  ? 126 VAL   B CG2 1 
ATOM   1181 C  CG2 B VAL   B 2 117 ? -12.565 -6.230  -21.823 0.50 53.67  ? 126 VAL   B CG2 1 
ATOM   1182 N  N   . ALA   B 2 118 ? -8.062  -5.462  -23.319 1.00 54.02  ? 127 ALA   B N   1 
ATOM   1183 C  CA  . ALA   B 2 118 ? -6.867  -4.670  -23.603 1.00 55.14  ? 127 ALA   B CA  1 
ATOM   1184 C  C   . ALA   B 2 118 ? -7.120  -3.522  -24.576 1.00 56.08  ? 127 ALA   B C   1 
ATOM   1185 O  O   . ALA   B 2 118 ? -6.754  -3.612  -25.739 1.00 55.99  ? 127 ALA   B O   1 
ATOM   1186 C  CB  . ALA   B 2 118 ? -5.744  -5.572  -24.095 1.00 55.39  ? 127 ALA   B CB  1 
ATOM   1187 N  N   . LEU   B 2 119 ? -7.797  -2.448  -24.101 1.00 56.27  ? 128 LEU   B N   1 
ATOM   1188 C  CA  . LEU   B 2 119 ? -8.126  -1.279  -24.920 1.00 56.46  ? 128 LEU   B CA  1 
ATOM   1189 C  C   . LEU   B 2 119 ? -7.793  -0.003  -24.142 1.00 56.74  ? 128 LEU   B C   1 
ATOM   1190 O  O   . LEU   B 2 119 ? -7.988  0.057   -22.923 1.00 56.98  ? 128 LEU   B O   1 
ATOM   1191 C  CB  . LEU   B 2 119 ? -9.609  -1.296  -25.313 1.00 56.68  ? 128 LEU   B CB  1 
ATOM   1192 C  CG  . LEU   B 2 119 ? -10.066 -2.491  -26.144 1.00 58.89  ? 128 LEU   B CG  1 
ATOM   1193 C  CD1 . LEU   B 2 119 ? -11.573 -2.519  -26.273 1.00 59.72  ? 128 LEU   B CD1 1 
ATOM   1194 C  CD2 . LEU   B 2 119 ? -9.443  -2.463  -27.529 1.00 59.63  ? 128 LEU   B CD2 1 
ATOM   1195 N  N   . ASP   B 2 120 ? -7.319  1.020   -24.846 1.00 56.36  ? 129 ASP   B N   1 
ATOM   1196 C  CA  . ASP   B 2 120 ? -6.913  2.286   -24.246 1.00 56.72  ? 129 ASP   B CA  1 
ATOM   1197 C  C   . ASP   B 2 120 ? -7.876  3.408   -24.492 1.00 55.86  ? 129 ASP   B C   1 
ATOM   1198 O  O   . ASP   B 2 120 ? -8.080  3.815   -25.632 1.00 56.07  ? 129 ASP   B O   1 
ATOM   1199 C  CB  . ASP   B 2 120 ? -5.554  2.715   -24.778 1.00 60.31  ? 129 ASP   B CB  1 
ATOM   1200 C  CG  . ASP   B 2 120 ? -4.468  2.544   -23.759 1.00 67.43  ? 129 ASP   B CG  1 
ATOM   1201 O  OD1 . ASP   B 2 120 ? -4.524  3.235   -22.709 1.00 69.32  ? 129 ASP   B OD1 1 
ATOM   1202 O  OD2 . ASP   B 2 120 ? -3.569  1.714   -23.993 1.00 69.55  ? 129 ASP   B OD2 1 
ATOM   1203 N  N   . TYR   B 2 121 ? -8.409  3.960   -23.412 1.00 54.63  ? 130 TYR   B N   1 
ATOM   1204 C  CA  . TYR   B 2 121 ? -9.348  5.061   -23.441 1.00 54.41  ? 130 TYR   B CA  1 
ATOM   1205 C  C   . TYR   B 2 121 ? -9.034  6.011   -22.290 1.00 53.48  ? 130 TYR   B C   1 
ATOM   1206 O  O   . TYR   B 2 121 ? -8.528  5.575   -21.243 1.00 53.96  ? 130 TYR   B O   1 
ATOM   1207 C  CB  . TYR   B 2 121 ? -10.786 4.521   -23.318 1.00 55.10  ? 130 TYR   B CB  1 
ATOM   1208 C  CG  . TYR   B 2 121 ? -11.272 3.898   -24.604 1.00 57.14  ? 130 TYR   B CG  1 
ATOM   1209 C  CD1 . TYR   B 2 121 ? -11.857 4.674   -25.598 1.00 59.01  ? 130 TYR   B CD1 1 
ATOM   1210 C  CD2 . TYR   B 2 121 ? -11.084 2.548   -24.859 1.00 58.49  ? 130 TYR   B CD2 1 
ATOM   1211 C  CE1 . TYR   B 2 121 ? -12.242 4.119   -26.811 1.00 60.25  ? 130 TYR   B CE1 1 
ATOM   1212 C  CE2 . TYR   B 2 121 ? -11.458 1.984   -26.068 1.00 59.94  ? 130 TYR   B CE2 1 
ATOM   1213 C  CZ  . TYR   B 2 121 ? -12.052 2.771   -27.036 1.00 61.49  ? 130 TYR   B CZ  1 
ATOM   1214 O  OH  . TYR   B 2 121 ? -12.429 2.216   -28.229 1.00 63.79  ? 130 TYR   B OH  1 
ATOM   1215 N  N   . PRO   B 2 122 ? -9.345  7.314   -22.442 1.00 52.07  ? 131 PRO   B N   1 
ATOM   1216 C  CA  . PRO   B 2 122 ? -9.126  8.252   -21.330 1.00 51.24  ? 131 PRO   B CA  1 
ATOM   1217 C  C   . PRO   B 2 122 ? -9.836  7.809   -20.034 1.00 49.38  ? 131 PRO   B C   1 
ATOM   1218 O  O   . PRO   B 2 122 ? -10.802 7.053   -20.100 1.00 49.81  ? 131 PRO   B O   1 
ATOM   1219 C  CB  . PRO   B 2 122 ? -9.703  9.579   -21.864 1.00 52.27  ? 131 PRO   B CB  1 
ATOM   1220 C  CG  . PRO   B 2 122 ? -9.693  9.443   -23.357 1.00 53.30  ? 131 PRO   B CG  1 
ATOM   1221 C  CD  . PRO   B 2 122 ? -9.969  7.986   -23.600 1.00 52.13  ? 131 PRO   B CD  1 
ATOM   1222 N  N   . ALA   B 2 123 ? -9.316  8.224   -18.866 1.00 47.02  ? 132 ALA   B N   1 
ATOM   1223 C  CA  . ALA   B 2 123 ? -9.843  7.894   -17.539 1.00 45.34  ? 132 ALA   B CA  1 
ATOM   1224 C  C   . ALA   B 2 123 ? -11.360 8.185   -17.362 1.00 43.45  ? 132 ALA   B C   1 
ATOM   1225 O  O   . ALA   B 2 123 ? -12.051 7.439   -16.681 1.00 42.76  ? 132 ALA   B O   1 
ATOM   1226 C  CB  . ALA   B 2 123 ? -9.033  8.614   -16.484 1.00 45.19  ? 132 ALA   B CB  1 
ATOM   1227 N  N   . GLY   B 2 124 ? -11.864 9.211   -18.046 1.00 42.35  ? 133 GLY   B N   1 
ATOM   1228 C  CA  . GLY   B 2 124 ? -13.282 9.570   -18.038 1.00 41.37  ? 133 GLY   B CA  1 
ATOM   1229 C  C   . GLY   B 2 124 ? -14.192 8.561   -18.723 1.00 40.52  ? 133 GLY   B C   1 
ATOM   1230 O  O   . GLY   B 2 124 ? -15.413 8.688   -18.663 1.00 40.43  ? 133 GLY   B O   1 
ATOM   1231 N  N   . THR   B 2 125 ? -13.606 7.541   -19.374 1.00 40.04  ? 134 THR   B N   1 
ATOM   1232 C  CA  . THR   B 2 125 ? -14.323 6.429   -20.009 1.00 40.44  ? 134 THR   B CA  1 
ATOM   1233 C  C   . THR   B 2 125 ? -14.662 5.312   -18.946 1.00 39.44  ? 134 THR   B C   1 
ATOM   1234 O  O   . THR   B 2 125 ? -15.454 4.427   -19.260 1.00 38.74  ? 134 THR   B O   1 
ATOM   1235 C  CB  . THR   B 2 125 ? -13.516 5.882   -21.242 1.00 42.57  ? 134 THR   B CB  1 
ATOM   1236 O  OG1 . THR   B 2 125 ? -12.956 6.984   -21.954 1.00 44.32  ? 134 THR   B OG1 1 
ATOM   1237 C  CG2 . THR   B 2 125 ? -14.371 5.095   -22.236 1.00 42.98  ? 134 THR   B CG2 1 
ATOM   1238 N  N   . SER   B 2 126 ? -14.060 5.365   -17.707 1.00 39.09  ? 135 SER   B N   1 
ATOM   1239 C  CA  . SER   B 2 126 ? -14.267 4.392   -16.616 1.00 39.22  ? 135 SER   B CA  1 
ATOM   1240 C  C   . SER   B 2 126 ? -15.732 4.158   -16.363 1.00 38.23  ? 135 SER   B C   1 
ATOM   1241 O  O   . SER   B 2 126 ? -16.443 5.110   -16.141 1.00 38.95  ? 135 SER   B O   1 
ATOM   1242 C  CB  . SER   B 2 126 ? -13.682 4.900   -15.302 1.00 42.07  ? 135 SER   B CB  1 
ATOM   1243 O  OG  . SER   B 2 126 ? -12.266 4.871   -15.232 1.00 45.88  ? 135 SER   B OG  1 
ATOM   1244 N  N   . GLY   B 2 127 ? -16.169 2.911   -16.336 1.00 36.87  ? 136 GLY   B N   1 
ATOM   1245 C  CA  . GLY   B 2 127 ? -17.566 2.583   -16.083 1.00 36.91  ? 136 GLY   B CA  1 
ATOM   1246 C  C   . GLY   B 2 127 ? -18.346 2.158   -17.311 1.00 37.21  ? 136 GLY   B C   1 
ATOM   1247 O  O   . GLY   B 2 127 ? -19.492 1.717   -17.188 1.00 36.77  ? 136 GLY   B O   1 
ATOM   1248 N  N   . SER   B 2 128 ? -17.728 2.277   -18.518 1.00 37.52  ? 137 SER   B N   1 
ATOM   1249 C  CA  . SER   B 2 128 ? -18.348 1.858   -19.780 1.00 38.01  ? 137 SER   B CA  1 
ATOM   1250 C  C   . SER   B 2 128 ? -18.638 0.358   -19.728 1.00 38.88  ? 137 SER   B C   1 
ATOM   1251 O  O   . SER   B 2 128 ? -17.778 -0.403  -19.316 1.00 39.57  ? 137 SER   B O   1 
ATOM   1252 C  CB  . SER   B 2 128 ? -17.421 2.179   -20.954 1.00 37.91  ? 137 SER   B CB  1 
ATOM   1253 O  OG  . SER   B 2 128 ? -17.363 3.583   -21.142 1.00 37.78  ? 137 SER   B OG  1 
ATOM   1254 N  N   . PRO   B 2 129 ? -19.842 -0.087  -20.122 1.00 39.25  ? 138 PRO   B N   1 
ATOM   1255 C  CA  . PRO   B 2 129 ? -20.146 -1.527  -20.040 1.00 39.97  ? 138 PRO   B CA  1 
ATOM   1256 C  C   . PRO   B 2 129 ? -19.492 -2.412  -21.089 1.00 41.55  ? 138 PRO   B C   1 
ATOM   1257 O  O   . PRO   B 2 129 ? -19.282 -2.018  -22.248 1.00 42.41  ? 138 PRO   B O   1 
ATOM   1258 C  CB  . PRO   B 2 129 ? -21.677 -1.571  -20.144 1.00 39.98  ? 138 PRO   B CB  1 
ATOM   1259 C  CG  . PRO   B 2 129 ? -22.024 -0.361  -20.985 1.00 39.89  ? 138 PRO   B CG  1 
ATOM   1260 C  CD  . PRO   B 2 129 ? -20.993 0.690   -20.635 1.00 38.36  ? 138 PRO   B CD  1 
ATOM   1261 N  N   . ILE   B 2 130 ? -19.191 -3.639  -20.674 1.00 42.46  ? 139 ILE   B N   1 
ATOM   1262 C  CA  . ILE   B 2 130 ? -18.670 -4.685  -21.533 1.00 44.18  ? 139 ILE   B CA  1 
ATOM   1263 C  C   . ILE   B 2 130 ? -19.849 -5.639  -21.774 1.00 45.28  ? 139 ILE   B C   1 
ATOM   1264 O  O   . ILE   B 2 130 ? -20.529 -6.017  -20.824 1.00 44.48  ? 139 ILE   B O   1 
ATOM   1265 C  CB  . ILE   B 2 130 ? -17.451 -5.393  -20.902 1.00 44.61  ? 139 ILE   B CB  1 
ATOM   1266 C  CG1 . ILE   B 2 130 ? -16.312 -4.390  -20.686 1.00 45.44  ? 139 ILE   B CG1 1 
ATOM   1267 C  CG2 . ILE   B 2 130 ? -17.006 -6.545  -21.795 1.00 45.39  ? 139 ILE   B CG2 1 
ATOM   1268 C  CD1 . ILE   B 2 130 ? -15.302 -4.822  -19.708 1.00 46.83  ? 139 ILE   B CD1 1 
ATOM   1269 N  N   . LEU   B 2 131 ? -20.129 -5.975  -23.039 1.00 46.46  ? 140 LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 131 ? -21.298 -6.778  -23.388 1.00 49.13  ? 140 LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 131 ? -20.999 -8.102  -24.062 1.00 51.43  ? 140 LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 131 ? -19.999 -8.237  -24.759 1.00 51.97  ? 140 LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 131 ? -22.272 -5.995  -24.321 1.00 49.94  ? 140 LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 131 ? -22.092 -4.490  -24.524 1.00 51.31  ? 140 LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 131 ? -22.962 -4.003  -25.649 1.00 50.88  ? 140 LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 131 ? -22.415 -3.726  -23.240 1.00 52.15  ? 140 LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 132 ? -21.895 -9.077  -23.874 1.00 52.52  ? 141 ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 132 ? -21.825 -10.362 -24.559 1.00 53.88  ? 141 ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 132 ? -22.661 -10.279 -25.874 1.00 55.74  ? 141 ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 132 ? -23.323 -9.270  -26.103 1.00 55.45  ? 141 ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 132 ? -22.262 -11.508 -23.645 1.00 54.65  ? 141 ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 132 ? -23.730 -11.599 -23.297 1.00 59.02  ? 141 ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 132 ? -24.511 -10.762 -23.785 1.00 59.07  ? 141 ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 132 ? -24.099 -12.514 -22.532 1.00 62.23  ? 141 ASP   B OD2 1 
ATOM   1285 N  N   . LYS   B 2 133 ? -22.651 -11.327 -26.716 1.00 57.60  ? 142 LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 2 133 ? -23.354 -11.331 -28.007 1.00 59.34  ? 142 LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 2 133 ? -24.870 -11.089 -27.889 1.00 59.39  ? 142 LYS   B C   1 
ATOM   1288 O  O   . LYS   B 2 133 ? -25.496 -10.639 -28.854 1.00 59.21  ? 142 LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 2 133 ? -23.027 -12.613 -28.795 1.00 63.29  ? 142 LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 2 133 ? -21.515 -12.755 -29.025 1.00 70.12  ? 142 LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 2 133 ? -21.070 -14.128 -29.574 1.00 76.42  ? 142 LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 2 133 ? -19.589 -14.140 -29.907 1.00 81.01  ? 142 LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 2 133 ? -19.093 -15.494 -30.307 1.00 83.84  ? 142 LYS   B NZ  1 
ATOM   1294 N  N   . CYS   B 2 134 ? -25.447 -11.299 -26.688 1.00 59.27  ? 143 CYS   B N   1 
ATOM   1295 C  CA  . CYS   B 2 134 ? -26.875 -11.008 -26.483 1.00 59.01  ? 143 CYS   B CA  1 
ATOM   1296 C  C   . CYS   B 2 134 ? -27.153 -9.630  -25.931 1.00 57.21  ? 143 CYS   B C   1 
ATOM   1297 O  O   . CYS   B 2 134 ? -28.298 -9.358  -25.589 1.00 57.80  ? 143 CYS   B O   1 
ATOM   1298 C  CB  . CYS   B 2 134 ? -27.536 -12.069 -25.618 1.00 61.16  ? 143 CYS   B CB  1 
ATOM   1299 S  SG  . CYS   B 2 134 ? -27.011 -13.749 -26.010 1.00 68.57  ? 143 CYS   B SG  1 
ATOM   1300 N  N   . GLY   B 2 135 ? -26.141 -8.776  -25.832 1.00 55.23  ? 144 GLY   B N   1 
ATOM   1301 C  CA  . GLY   B 2 135 ? -26.306 -7.432  -25.293 1.00 53.88  ? 144 GLY   B CA  1 
ATOM   1302 C  C   . GLY   B 2 135 ? -26.394 -7.368  -23.774 1.00 51.67  ? 144 GLY   B C   1 
ATOM   1303 O  O   . GLY   B 2 135 ? -26.821 -6.349  -23.224 1.00 51.28  ? 144 GLY   B O   1 
ATOM   1304 N  N   . ARG   B 2 136 ? -26.033 -8.455  -23.078 1.00 50.11  ? 145 ARG   B N   1 
ATOM   1305 C  CA  . ARG   B 2 136 ? -26.060 -8.473  -21.608 1.00 49.17  ? 145 ARG   B CA  1 
ATOM   1306 C  C   . ARG   B 2 136 ? -24.748 -7.930  -21.064 1.00 46.99  ? 145 ARG   B C   1 
ATOM   1307 O  O   . ARG   B 2 136 ? -23.682 -8.260  -21.602 1.00 45.88  ? 145 ARG   B O   1 
ATOM   1308 C  CB  . ARG   B 2 136 ? -26.278 -9.894  -21.076 1.00 51.75  ? 145 ARG   B CB  1 
ATOM   1309 C  CG  . ARG   B 2 136 ? -27.697 -10.397 -21.269 1.00 57.18  ? 145 ARG   B CG  1 
ATOM   1310 C  CD  . ARG   B 2 136 ? -27.845 -11.785 -20.694 1.00 62.79  ? 145 ARG   B CD  1 
ATOM   1311 N  NE  . ARG   B 2 136 ? -27.336 -12.798 -21.618 1.00 69.26  ? 145 ARG   B NE  1 
ATOM   1312 C  CZ  . ARG   B 2 136 ? -26.783 -13.949 -21.246 1.00 74.23  ? 145 ARG   B CZ  1 
ATOM   1313 N  NH1 . ARG   B 2 136 ? -26.623 -14.233 -19.956 1.00 75.23  ? 145 ARG   B NH1 1 
ATOM   1314 N  NH2 . ARG   B 2 136 ? -26.363 -14.816 -22.161 1.00 74.84  ? 145 ARG   B NH2 1 
ATOM   1315 N  N   . VAL   B 2 137 ? -24.814 -7.110  -19.983 1.00 45.80  ? 146 VAL   B N   1 
ATOM   1316 C  CA  . VAL   B 2 137 ? -23.607 -6.546  -19.387 1.00 44.56  ? 146 VAL   B CA  1 
ATOM   1317 C  C   . VAL   B 2 137 ? -22.916 -7.579  -18.538 1.00 44.55  ? 146 VAL   B C   1 
ATOM   1318 O  O   . VAL   B 2 137 ? -23.461 -8.000  -17.521 1.00 45.34  ? 146 VAL   B O   1 
ATOM   1319 C  CB  . VAL   B 2 137 ? -23.868 -5.242  -18.605 1.00 44.02  ? 146 VAL   B CB  1 
ATOM   1320 C  CG1 . VAL   B 2 137 ? -22.573 -4.681  -18.028 1.00 44.32  ? 146 VAL   B CG1 1 
ATOM   1321 C  CG2 . VAL   B 2 137 ? -24.549 -4.206  -19.482 1.00 43.80  ? 146 VAL   B CG2 1 
ATOM   1322 N  N   . ILE   B 2 138 ? -21.724 -8.013  -18.974 1.00 43.19  ? 147 ILE   B N   1 
ATOM   1323 C  CA  . ILE   B 2 138 ? -20.882 -8.978  -18.265 1.00 42.19  ? 147 ILE   B CA  1 
ATOM   1324 C  C   . ILE   B 2 138 ? -19.830 -8.299  -17.333 1.00 41.59  ? 147 ILE   B C   1 
ATOM   1325 O  O   . ILE   B 2 138 ? -19.093 -8.989  -16.615 1.00 41.75  ? 147 ILE   B O   1 
ATOM   1326 C  CB  . ILE   B 2 138 ? -20.237 -9.971  -19.276 1.00 42.35  ? 147 ILE   B CB  1 
ATOM   1327 C  CG1 . ILE   B 2 138 ? -19.358 -9.226  -20.298 1.00 43.43  ? 147 ILE   B CG1 1 
ATOM   1328 C  CG2 . ILE   B 2 138 ? -21.318 -10.789 -19.975 1.00 42.54  ? 147 ILE   B CG2 1 
ATOM   1329 C  CD1 . ILE   B 2 138 ? -18.650 -10.094 -21.336 1.00 45.35  ? 147 ILE   B CD1 1 
ATOM   1330 N  N   . GLY   B 2 139 ? -19.807 -6.966  -17.298 1.00 40.26  ? 148 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 139 ? -18.898 -6.246  -16.417 1.00 39.29  ? 148 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 139 ? -18.640 -4.823  -16.844 1.00 38.49  ? 148 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 139 ? -19.107 -4.400  -17.898 1.00 39.40  ? 148 GLY   B O   1 
ATOM   1334 N  N   . LEU   B 2 140 ? -17.888 -4.072  -16.036 1.00 37.51  ? 149 LEU   B N   1 
ATOM   1335 C  CA  . LEU   B 2 140 ? -17.555 -2.679  -16.354 1.00 36.65  ? 149 LEU   B CA  1 
ATOM   1336 C  C   . LEU   B 2 140 ? -16.049 -2.558  -16.582 1.00 37.23  ? 149 LEU   B C   1 
ATOM   1337 O  O   . LEU   B 2 140 ? -15.252 -3.254  -15.942 1.00 37.33  ? 149 LEU   B O   1 
ATOM   1338 C  CB  . LEU   B 2 140 ? -17.995 -1.714  -15.241 1.00 35.59  ? 149 LEU   B CB  1 
ATOM   1339 C  CG  . LEU   B 2 140 ? -19.492 -1.700  -14.833 1.00 35.54  ? 149 LEU   B CG  1 
ATOM   1340 C  CD1 . LEU   B 2 140 ? -19.781 -0.533  -13.899 1.00 35.81  ? 149 LEU   B CD1 1 
ATOM   1341 C  CD2 . LEU   B 2 140 ? -20.431 -1.626  -16.049 1.00 34.78  ? 149 LEU   B CD2 1 
ATOM   1342 N  N   . TYR   B 2 141 ? -15.677 -1.676  -17.511 1.00 37.27  ? 150 TYR   B N   1 
ATOM   1343 C  CA  . TYR   B 2 141 ? -14.298 -1.367  -17.919 1.00 38.30  ? 150 TYR   B CA  1 
ATOM   1344 C  C   . TYR   B 2 141 ? -13.862 -0.131  -17.137 1.00 38.74  ? 150 TYR   B C   1 
ATOM   1345 O  O   . TYR   B 2 141 ? -14.666 0.789   -17.004 1.00 38.94  ? 150 TYR   B O   1 
ATOM   1346 C  CB  . TYR   B 2 141 ? -14.320 -1.032  -19.447 1.00 38.74  ? 150 TYR   B CB  1 
ATOM   1347 C  CG  . TYR   B 2 141 ? -13.094 -0.320  -19.996 1.00 40.27  ? 150 TYR   B CG  1 
ATOM   1348 C  CD1 . TYR   B 2 141 ? -13.034 1.069   -20.047 1.00 41.68  ? 150 TYR   B CD1 1 
ATOM   1349 C  CD2 . TYR   B 2 141 ? -12.040 -1.037  -20.553 1.00 41.45  ? 150 TYR   B CD2 1 
ATOM   1350 C  CE1 . TYR   B 2 141 ? -11.912 1.727   -20.549 1.00 43.53  ? 150 TYR   B CE1 1 
ATOM   1351 C  CE2 . TYR   B 2 141 ? -10.917 -0.393  -21.072 1.00 42.71  ? 150 TYR   B CE2 1 
ATOM   1352 C  CZ  . TYR   B 2 141 ? -10.858 0.990   -21.075 1.00 44.86  ? 150 TYR   B CZ  1 
ATOM   1353 O  OH  . TYR   B 2 141 ? -9.745  1.625   -21.584 1.00 47.97  ? 150 TYR   B OH  1 
ATOM   1354 N  N   . GLY   B 2 142 ? -12.620 -0.078  -16.671 1.00 38.66  ? 151 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 142 ? -12.151 1.103   -15.953 1.00 39.56  ? 151 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 142 ? -11.335 0.882   -14.698 1.00 39.83  ? 151 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 142 ? -10.998 1.846   -14.004 1.00 39.42  ? 151 GLY   B O   1 
ATOM   1358 N  N   . ASN   B 2 143 ? -10.991 -0.376  -14.394 1.00 39.70  ? 152 ASN   B N   1 
ATOM   1359 C  CA  . ASN   B 2 143 ? -10.111 -0.671  -13.268 1.00 40.26  ? 152 ASN   B CA  1 
ATOM   1360 C  C   . ASN   B 2 143 ? -9.150  -1.746  -13.758 1.00 40.84  ? 152 ASN   B C   1 
ATOM   1361 O  O   . ASN   B 2 143 ? -9.574  -2.837  -14.130 1.00 40.51  ? 152 ASN   B O   1 
ATOM   1362 C  CB  . ASN   B 2 143 ? -10.863 -1.148  -12.010 1.00 41.23  ? 152 ASN   B CB  1 
ATOM   1363 C  CG  . ASN   B 2 143 ? -9.964  -1.173  -10.785 1.00 45.81  ? 152 ASN   B CG  1 
ATOM   1364 O  OD1 . ASN   B 2 143 ? -8.991  -0.410  -10.701 1.00 47.96  ? 152 ASN   B OD1 1 
ATOM   1365 N  ND2 . ASN   B 2 143 ? -10.244 -2.052  -9.807  1.00 45.10  ? 152 ASN   B ND2 1 
ATOM   1366 N  N   . GLY   B 2 144 ? -7.880  -1.408  -13.801 1.00 41.31  ? 153 GLY   B N   1 
ATOM   1367 C  CA  . GLY   B 2 144 ? -6.886  -2.341  -14.280 1.00 42.98  ? 153 GLY   B CA  1 
ATOM   1368 C  C   . GLY   B 2 144 ? -5.453  -1.952  -14.041 1.00 44.37  ? 153 GLY   B C   1 
ATOM   1369 O  O   . GLY   B 2 144 ? -5.099  -1.397  -12.997 1.00 43.74  ? 153 GLY   B O   1 
ATOM   1370 N  N   . VAL   B 2 145 ? -4.633  -2.251  -15.035 1.00 46.44  ? 154 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 145 ? -3.201  -2.088  -14.937 1.00 49.64  ? 154 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 145 ? -2.569  -1.480  -16.189 1.00 52.85  ? 154 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 145 ? -3.161  -1.484  -17.261 1.00 52.54  ? 154 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 145 ? -2.637  -3.490  -14.579 1.00 50.52  ? 154 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 145 ? -2.381  -4.339  -15.816 1.00 50.49  ? 154 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 145 ? -1.419  -3.407  -13.676 1.00 51.83  ? 154 VAL   B CG2 1 
ATOM   1377 N  N   . VAL   B 2 146 ? -1.374  -0.926  -16.033 1.00 55.82  ? 155 VAL   B N   1 
ATOM   1378 C  CA  . VAL   B 2 146 ? -0.607  -0.368  -17.132 1.00 58.87  ? 155 VAL   B CA  1 
ATOM   1379 C  C   . VAL   B 2 146 ? 0.551   -1.331  -17.354 1.00 62.07  ? 155 VAL   B C   1 
ATOM   1380 O  O   . VAL   B 2 146 ? 1.282   -1.640  -16.418 1.00 62.14  ? 155 VAL   B O   1 
ATOM   1381 C  CB  . VAL   B 2 146 ? -0.113  1.066   -16.841 1.00 59.73  ? 155 VAL   B CB  1 
ATOM   1382 C  CG1 . VAL   B 2 146 ? 0.627   1.633   -18.043 1.00 60.67  ? 155 VAL   B CG1 1 
ATOM   1383 C  CG2 . VAL   B 2 146 ? -1.269  1.972   -16.444 1.00 59.95  ? 155 VAL   B CG2 1 
ATOM   1384 N  N   . ILE   B 2 147 ? 0.685   -1.854  -18.580 1.00 64.58  ? 156 ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 2 147 ? 1.726   -2.828  -18.883 1.00 67.08  ? 156 ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 2 147 ? 3.013   -2.145  -19.430 1.00 69.39  ? 156 ILE   B C   1 
ATOM   1387 O  O   . ILE   B 2 147 ? 3.037   -0.927  -19.587 1.00 69.24  ? 156 ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 2 147 ? 1.161   -3.954  -19.801 1.00 67.71  ? 156 ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 2 147 ? 0.641   -3.393  -21.120 1.00 68.70  ? 156 ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 2 147 ? 0.086   -4.755  -19.086 1.00 68.46  ? 156 ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 2 147 ? 0.357   -4.454  -22.169 1.00 69.93  ? 156 ILE   B CD1 1 
ATOM   1392 N  N   . LYS   B 2 148 ? 4.087   -2.940  -19.640 1.00 71.08  ? 157 LYS   B N   1 
ATOM   1393 C  CA  . LYS   B 2 148 ? 5.428   -2.585  -20.103 1.00 73.36  ? 157 LYS   B CA  1 
ATOM   1394 C  C   . LYS   B 2 148 ? 5.510   -1.467  -21.150 1.00 74.86  ? 157 LYS   B C   1 
ATOM   1395 O  O   . LYS   B 2 148 ? 6.303   -0.542  -20.974 1.00 75.91  ? 157 LYS   B O   1 
ATOM   1396 C  CB  . LYS   B 2 148 ? 6.169   -3.838  -20.619 1.00 76.45  ? 157 LYS   B CB  1 
ATOM   1397 C  CG  . LYS   B 2 148 ? 5.457   -4.622  -21.742 1.00 81.75  ? 157 LYS   B CG  1 
ATOM   1398 C  CD  . LYS   B 2 148 ? 4.342   -5.590  -21.271 1.00 86.74  ? 157 LYS   B CD  1 
ATOM   1399 C  CE  . LYS   B 2 148 ? 4.711   -6.461  -20.086 1.00 90.50  ? 157 LYS   B CE  1 
ATOM   1400 N  NZ  . LYS   B 2 148 ? 4.119   -5.946  -18.818 1.00 92.15  ? 157 LYS   B NZ  1 
ATOM   1401 N  N   . ASN   B 2 149 ? 4.714   -1.530  -22.226 1.00 74.72  ? 158 ASN   B N   1 
ATOM   1402 C  CA  . ASN   B 2 149 ? 4.756   -0.508  -23.269 1.00 74.83  ? 158 ASN   B CA  1 
ATOM   1403 C  C   . ASN   B 2 149 ? 3.938   0.758   -22.971 1.00 73.38  ? 158 ASN   B C   1 
ATOM   1404 O  O   . ASN   B 2 149 ? 3.758   1.590   -23.863 1.00 74.42  ? 158 ASN   B O   1 
ATOM   1405 C  CB  . ASN   B 2 149 ? 4.363   -1.085  -24.643 1.00 77.69  ? 158 ASN   B CB  1 
ATOM   1406 C  CG  . ASN   B 2 149 ? 3.219   -2.085  -24.653 1.00 82.60  ? 158 ASN   B CG  1 
ATOM   1407 O  OD1 . ASN   B 2 149 ? 3.181   -3.017  -25.471 1.00 85.06  ? 158 ASN   B OD1 1 
ATOM   1408 N  ND2 . ASN   B 2 149 ? 2.255   -1.912  -23.776 1.00 82.95  ? 158 ASN   B ND2 1 
ATOM   1409 N  N   . GLY   B 2 150 ? 3.452   0.894   -21.742 1.00 70.78  ? 159 GLY   B N   1 
ATOM   1410 C  CA  . GLY   B 2 150 ? 2.649   2.038   -21.324 1.00 68.42  ? 159 GLY   B CA  1 
ATOM   1411 C  C   . GLY   B 2 150 ? 1.177   1.940   -21.671 1.00 65.50  ? 159 GLY   B C   1 
ATOM   1412 O  O   . GLY   B 2 150 ? 0.439   2.915   -21.496 1.00 65.14  ? 159 GLY   B O   1 
ATOM   1413 N  N   . SER   B 2 151 ? 0.728   0.768   -22.174 1.00 62.94  ? 160 SER   B N   1 
ATOM   1414 C  CA  A SER   B 2 151 ? -0.671  0.561   -22.550 0.50 62.05  ? 160 SER   B CA  1 
ATOM   1415 C  CA  B SER   B 2 151 ? -0.675  0.605   -22.535 0.50 61.84  ? 160 SER   B CA  1 
ATOM   1416 C  C   . SER   B 2 151 ? -1.521  0.090   -21.366 1.00 60.13  ? 160 SER   B C   1 
ATOM   1417 O  O   . SER   B 2 151 ? -0.995  -0.453  -20.406 1.00 60.22  ? 160 SER   B O   1 
ATOM   1418 C  CB  A SER   B 2 151 ? -0.782  -0.422  -23.713 0.50 64.11  ? 160 SER   B CB  1 
ATOM   1419 C  CB  B SER   B 2 151 ? -0.823  -0.260  -23.782 0.50 63.28  ? 160 SER   B CB  1 
ATOM   1420 O  OG  A SER   B 2 151 ? -2.116  -0.489  -24.196 0.50 67.37  ? 160 SER   B OG  1 
ATOM   1421 O  OG  B SER   B 2 151 ? -0.114  -1.477  -23.651 0.50 65.40  ? 160 SER   B OG  1 
ATOM   1422 N  N   . TYR   B 2 152 ? -2.832  0.286   -21.444 1.00 56.56  ? 161 TYR   B N   1 
ATOM   1423 C  CA  . TYR   B 2 152 ? -3.780  -0.059  -20.401 1.00 53.37  ? 161 TYR   B CA  1 
ATOM   1424 C  C   . TYR   B 2 152 ? -4.591  -1.343  -20.644 1.00 50.93  ? 161 TYR   B C   1 
ATOM   1425 O  O   . TYR   B 2 152 ? -5.076  -1.582  -21.744 1.00 50.47  ? 161 TYR   B O   1 
ATOM   1426 C  CB  . TYR   B 2 152 ? -4.712  1.141   -20.227 1.00 51.89  ? 161 TYR   B CB  1 
ATOM   1427 C  CG  . TYR   B 2 152 ? -5.722  0.988   -19.123 1.00 50.23  ? 161 TYR   B CG  1 
ATOM   1428 C  CD1 . TYR   B 2 152 ? -5.344  1.092   -17.792 1.00 50.26  ? 161 TYR   B CD1 1 
ATOM   1429 C  CD2 . TYR   B 2 152 ? -7.068  0.817   -19.406 1.00 49.96  ? 161 TYR   B CD2 1 
ATOM   1430 C  CE1 . TYR   B 2 152 ? -6.262  0.934   -16.770 1.00 50.11  ? 161 TYR   B CE1 1 
ATOM   1431 C  CE2 . TYR   B 2 152 ? -8.003  0.693   -18.392 1.00 50.37  ? 161 TYR   B CE2 1 
ATOM   1432 C  CZ  . TYR   B 2 152 ? -7.590  0.738   -17.073 1.00 50.51  ? 161 TYR   B CZ  1 
ATOM   1433 O  OH  . TYR   B 2 152 ? -8.499  0.649   -16.066 1.00 50.63  ? 161 TYR   B OH  1 
ATOM   1434 N  N   . VAL   B 2 153 ? -4.735  -2.162  -19.594 1.00 49.11  ? 162 VAL   B N   1 
ATOM   1435 C  CA  . VAL   B 2 153 ? -5.498  -3.408  -19.618 1.00 47.67  ? 162 VAL   B CA  1 
ATOM   1436 C  C   . VAL   B 2 153 ? -6.459  -3.368  -18.460 1.00 44.73  ? 162 VAL   B C   1 
ATOM   1437 O  O   . VAL   B 2 153 ? -6.038  -3.341  -17.316 1.00 43.61  ? 162 VAL   B O   1 
ATOM   1438 C  CB  . VAL   B 2 153 ? -4.616  -4.689  -19.543 1.00 48.76  ? 162 VAL   B CB  1 
ATOM   1439 C  CG1 . VAL   B 2 153 ? -5.438  -5.927  -19.885 1.00 48.80  ? 162 VAL   B CG1 1 
ATOM   1440 C  CG2 . VAL   B 2 153 ? -3.414  -4.587  -20.471 1.00 50.38  ? 162 VAL   B CG2 1 
ATOM   1441 N  N   . SER   B 2 154 ? -7.740  -3.374  -18.755 1.00 43.47  ? 163 SER   B N   1 
ATOM   1442 C  CA  . SER   B 2 154 ? -8.765  -3.302  -17.731 1.00 42.39  ? 163 SER   B CA  1 
ATOM   1443 C  C   . SER   B 2 154 ? -9.295  -4.677  -17.369 1.00 42.45  ? 163 SER   B C   1 
ATOM   1444 O  O   . SER   B 2 154 ? -9.416  -5.529  -18.233 1.00 43.26  ? 163 SER   B O   1 
ATOM   1445 C  CB  . SER   B 2 154 ? -9.916  -2.430  -18.225 1.00 41.75  ? 163 SER   B CB  1 
ATOM   1446 O  OG  . SER   B 2 154 ? -11.035 -2.458  -17.352 1.00 41.10  ? 163 SER   B OG  1 
ATOM   1447 N  N   . ALA   B 2 155 ? -9.691  -4.864  -16.128 1.00 41.83  ? 164 ALA   B N   1 
ATOM   1448 C  CA  . ALA   B 2 155 ? -10.357 -6.093  -15.696 1.00 41.95  ? 164 ALA   B CA  1 
ATOM   1449 C  C   . ALA   B 2 155 ? -11.795 -6.035  -16.219 1.00 42.58  ? 164 ALA   B C   1 
ATOM   1450 O  O   . ALA   B 2 155 ? -12.318 -4.934  -16.507 1.00 42.28  ? 164 ALA   B O   1 
ATOM   1451 C  CB  . ALA   B 2 155 ? -10.385 -6.165  -14.158 1.00 41.41  ? 164 ALA   B CB  1 
ATOM   1452 N  N   . ILE   B 2 156 ? -12.446 -7.209  -16.354 1.00 42.31  ? 165 ILE   B N   1 
ATOM   1453 C  CA  . ILE   B 2 156 ? -13.877 -7.203  -16.671 1.00 42.05  ? 165 ILE   B CA  1 
ATOM   1454 C  C   . ILE   B 2 156 ? -14.511 -7.285  -15.260 1.00 41.38  ? 165 ILE   B C   1 
ATOM   1455 O  O   . ILE   B 2 156 ? -14.655 -8.381  -14.709 1.00 41.71  ? 165 ILE   B O   1 
ATOM   1456 C  CB  . ILE   B 2 156 ? -14.351 -8.354  -17.568 1.00 42.62  ? 165 ILE   B CB  1 
ATOM   1457 C  CG1 . ILE   B 2 156 ? -13.550 -8.409  -18.889 1.00 44.30  ? 165 ILE   B CG1 1 
ATOM   1458 C  CG2 . ILE   B 2 156 ? -15.853 -8.186  -17.831 1.00 42.59  ? 165 ILE   B CG2 1 
ATOM   1459 C  CD1 . ILE   B 2 156 ? -13.898 -9.564  -19.795 1.00 45.74  ? 165 ILE   B CD1 1 
ATOM   1460 N  N   . THR   B 2 157 ? -14.748 -6.126  -14.634 1.00 40.76  ? 166 THR   B N   1 
ATOM   1461 C  CA  . THR   B 2 157 ? -15.262 -6.078  -13.263 1.00 40.85  ? 166 THR   B CA  1 
ATOM   1462 C  C   . THR   B 2 157 ? -16.760 -6.284  -13.169 1.00 41.42  ? 166 THR   B C   1 
ATOM   1463 O  O   . THR   B 2 157 ? -17.512 -5.425  -13.603 1.00 41.91  ? 166 THR   B O   1 
ATOM   1464 C  CB  . THR   B 2 157 ? -14.899 -4.766  -12.558 1.00 41.16  ? 166 THR   B CB  1 
ATOM   1465 O  OG1 . THR   B 2 157 ? -13.483 -4.564  -12.580 1.00 40.97  ? 166 THR   B OG1 1 
ATOM   1466 C  CG2 . THR   B 2 157 ? -15.402 -4.755  -11.109 1.00 41.50  ? 166 THR   B CG2 1 
ATOM   1467 N  N   . GLN   B 2 158 ? -17.193 -7.379  -12.552 1.00 41.39  ? 167 GLN   B N   1 
ATOM   1468 C  CA  . GLN   B 2 158 ? -18.615 -7.652  -12.383 1.00 42.06  ? 167 GLN   B CA  1 
ATOM   1469 C  C   . GLN   B 2 158 ? -18.993 -7.797  -10.880 1.00 43.75  ? 167 GLN   B C   1 
ATOM   1470 O  O   . GLN   B 2 158 ? -18.230 -8.340  -10.104 1.00 42.73  ? 167 GLN   B O   1 
ATOM   1471 C  CB  . GLN   B 2 158 ? -19.008 -8.913  -13.194 1.00 41.80  ? 167 GLN   B CB  1 
ATOM   1472 C  CG  . GLN   B 2 158 ? -20.500 -9.299  -13.182 1.00 42.67  ? 167 GLN   B CG  1 
ATOM   1473 C  CD  . GLN   B 2 158 ? -21.432 -8.238  -13.748 1.00 42.68  ? 167 GLN   B CD  1 
ATOM   1474 O  OE1 . GLN   B 2 158 ? -21.511 -7.112  -13.252 1.00 41.86  ? 167 GLN   B OE1 1 
ATOM   1475 N  NE2 . GLN   B 2 158 ? -22.189 -8.581  -14.770 1.00 42.07  ? 167 GLN   B NE2 1 
ATOM   1476 N  N   . GLY   B 2 159 ? -20.150 -7.283  -10.496 1.00 45.58  ? 168 GLY   B N   1 
ATOM   1477 C  CA  . GLY   B 2 159 ? -20.657 -7.432  -9.145  1.00 48.06  ? 168 GLY   B CA  1 
ATOM   1478 C  C   . GLY   B 2 159 ? -21.445 -8.715  -8.966  1.00 51.21  ? 168 GLY   B C   1 
ATOM   1479 O  O   . GLY   B 2 159 ? -21.578 -9.517  -9.890  1.00 51.21  ? 168 GLY   B O   1 
ATOM   1480 N  N   . LYS   B 2 160 ? -21.972 -8.921  -7.761  1.00 54.04  ? 169 LYS   B N   1 
ATOM   1481 C  CA  . LYS   B 2 160 ? -22.769 -10.095 -7.408  1.00 56.85  ? 169 LYS   B CA  1 
ATOM   1482 C  C   . LYS   B 2 160 ? -24.223 -9.664  -7.217  1.00 59.39  ? 169 LYS   B C   1 
ATOM   1483 O  O   . LYS   B 2 160 ? -24.489 -8.733  -6.455  1.00 59.69  ? 169 LYS   B O   1 
ATOM   1484 C  CB  . LYS   B 2 160 ? -22.239 -10.736 -6.111  1.00 59.39  ? 169 LYS   B CB  1 
ATOM   1485 C  CG  . LYS   B 2 160 ? -23.012 -11.984 -5.703  1.00 64.75  ? 169 LYS   B CG  1 
ATOM   1486 C  CD  . LYS   B 2 160 ? -22.685 -12.467 -4.288  1.00 69.44  ? 169 LYS   B CD  1 
ATOM   1487 C  CE  . LYS   B 2 160 ? -23.542 -13.657 -3.912  1.00 73.66  ? 169 LYS   B CE  1 
ATOM   1488 N  NZ  . LYS   B 2 160 ? -23.636 -13.847 -2.435  1.00 75.80  ? 169 LYS   B NZ  1 
ATOM   1489 N  N   . ARG   B 2 161 ? -25.163 -10.314 -7.918  1.00 60.94  ? 170 ARG   B N   1 
ATOM   1490 C  CA  . ARG   B 2 161 ? -26.582 -9.980  -7.766  1.00 62.79  ? 170 ARG   B CA  1 
ATOM   1491 C  C   . ARG   B 2 161 ? -27.126 -10.752 -6.556  1.00 64.82  ? 170 ARG   B C   1 
ATOM   1492 O  O   . ARG   B 2 161 ? -26.763 -11.917 -6.352  1.00 65.35  ? 170 ARG   B O   1 
ATOM   1493 C  CB  . ARG   B 2 161 ? -27.371 -10.328 -9.046  1.00 63.94  ? 170 ARG   B CB  1 
ATOM   1494 C  CG  . ARG   B 2 161 ? -28.739 -9.676  -9.113  1.00 66.52  ? 170 ARG   B CG  1 
ATOM   1495 C  CD  . ARG   B 2 161 ? -29.619 -10.289 -10.185 1.00 69.98  ? 170 ARG   B CD  1 
ATOM   1496 N  NE  . ARG   B 2 161 ? -31.010 -9.865  -10.026 1.00 73.28  ? 170 ARG   B NE  1 
ATOM   1497 C  CZ  . ARG   B 2 161 ? -31.657 -9.064  -10.869 1.00 75.62  ? 170 ARG   B CZ  1 
ATOM   1498 N  NH1 . ARG   B 2 161 ? -31.053 -8.610  -11.962 1.00 74.84  ? 170 ARG   B NH1 1 
ATOM   1499 N  NH2 . ARG   B 2 161 ? -32.914 -8.714  -10.627 1.00 75.86  ? 170 ARG   B NH2 1 
ATOM   1500 N  N   . GLU   B 2 162 ? -27.961 -10.106 -5.736  1.00 65.61  ? 171 GLU   B N   1 
ATOM   1501 C  CA  . GLU   B 2 162 ? -28.521 -10.756 -4.557  1.00 67.19  ? 171 GLU   B CA  1 
ATOM   1502 C  C   . GLU   B 2 162 ? -29.725 -11.626 -4.907  1.00 67.79  ? 171 GLU   B C   1 
ATOM   1503 O  O   . GLU   B 2 162 ? -30.290 -12.266 -4.021  1.00 68.31  ? 171 GLU   B O   1 
ATOM   1504 C  CB  . GLU   B 2 162 ? -28.886 -9.719  -3.477  1.00 70.24  ? 171 GLU   B CB  1 
ATOM   1505 C  CG  . GLU   B 2 162 ? -27.677 -9.092  -2.806  1.00 75.49  ? 171 GLU   B CG  1 
ATOM   1506 C  CD  . GLU   B 2 162 ? -26.811 -10.085 -2.063  1.00 83.95  ? 171 GLU   B CD  1 
ATOM   1507 O  OE1 . GLU   B 2 162 ? -27.236 -10.550 -0.979  1.00 85.06  ? 171 GLU   B OE1 1 
ATOM   1508 O  OE2 . GLU   B 2 162 ? -25.706 -10.400 -2.564  1.00 86.92  ? 171 GLU   B OE2 1 
HETATM 1509 S  S   . DMS   C 3 .   ? -18.570 11.127  -0.072  1.00 84.70  ? 201 DMS   B S   1 
HETATM 1510 O  O   . DMS   C 3 .   ? -19.221 9.793   -0.324  1.00 84.45  ? 201 DMS   B O   1 
HETATM 1511 C  C1  . DMS   C 3 .   ? -19.648 12.436  -0.690  1.00 84.61  ? 201 DMS   B C1  1 
HETATM 1512 C  C2  . DMS   C 3 .   ? -17.283 11.433  -1.320  1.00 84.51  ? 201 DMS   B C2  1 
HETATM 1513 N  N1  . A1B8T D 4 .   ? -5.996  3.196   -12.225 1.00 49.93  ? 202 A1B8T B N1  1 
HETATM 1514 N  N3  . A1B8T D 4 .   ? -8.855  2.230   -7.209  1.00 49.15  ? 202 A1B8T B N3  1 
HETATM 1515 C  C4  . A1B8T D 4 .   ? -3.253  1.291   -10.407 1.00 50.69  ? 202 A1B8T B C4  1 
HETATM 1516 C  C5  . A1B8T D 4 .   ? -2.825  1.123   -12.740 1.00 51.27  ? 202 A1B8T B C5  1 
HETATM 1517 C  C6  . A1B8T D 4 .   ? -4.110  1.813   -13.150 1.00 51.22  ? 202 A1B8T B C6  1 
HETATM 1518 C  C7  . A1B8T D 4 .   ? -7.688  4.166   -13.643 1.00 50.76  ? 202 A1B8T B C7  1 
HETATM 1519 C  C8  . A1B8T D 4 .   ? -8.871  4.072   -11.475 1.00 49.77  ? 202 A1B8T B C8  1 
HETATM 1520 C  C10 . A1B8T D 4 .   ? -8.403  5.164   -9.369  1.00 49.71  ? 202 A1B8T B C10 1 
HETATM 1521 C  C13 . A1B8T D 4 .   ? -9.206  2.886   -10.803 1.00 49.26  ? 202 A1B8T B C13 1 
HETATM 1522 C  C15 . A1B8T D 4 .   ? -8.816  3.703   -7.232  1.00 49.45  ? 202 A1B8T B C15 1 
HETATM 1523 C  C17 . A1B8T D 4 .   ? -9.024  4.052   -15.846 1.00 51.95  ? 202 A1B8T B C17 1 
HETATM 1524 C  C20 . A1B8T D 4 .   ? -6.760  4.582   -17.341 1.00 54.38  ? 202 A1B8T B C20 1 
HETATM 1525 C  C21 . A1B8T D 4 .   ? -5.287  4.694   -15.672 1.00 55.16  ? 202 A1B8T B C21 1 
HETATM 1526 C  C22 . A1B8T D 4 .   ? -6.667  4.518   -15.940 1.00 54.01  ? 202 A1B8T B C22 1 
HETATM 1527 O  O1  . A1B8T D 4 .   ? -7.088  1.815   -13.653 1.00 48.67  ? 202 A1B8T B O1  1 
HETATM 1528 C  C1  . A1B8T D 4 .   ? -6.853  2.941   -13.219 1.00 49.73  ? 202 A1B8T B C1  1 
HETATM 1529 C  C2  . A1B8T D 4 .   ? -4.687  2.594   -11.981 1.00 50.55  ? 202 A1B8T B C2  1 
HETATM 1530 C  C3  . A1B8T D 4 .   ? -4.640  1.840   -10.662 1.00 50.64  ? 202 A1B8T B C3  1 
HETATM 1531 O  O2  . A1B8T D 4 .   ? -2.354  1.594   -11.474 1.00 51.17  ? 202 A1B8T B O2  1 
HETATM 1532 N  N2  . A1B8T D 4 .   ? -8.906  4.117   -12.869 1.00 50.17  ? 202 A1B8T B N2  1 
HETATM 1533 C  C9  . A1B8T D 4 .   ? -8.413  5.185   -10.754 1.00 49.66  ? 202 A1B8T B C9  1 
HETATM 1534 C  C11 . A1B8T D 4 .   ? -8.743  3.990   -8.706  1.00 49.58  ? 202 A1B8T B C11 1 
HETATM 1535 C  C12 . A1B8T D 4 .   ? -9.137  2.862   -9.415  1.00 49.43  ? 202 A1B8T B C12 1 
HETATM 1536 C  C14 . A1B8T D 4 .   ? -9.488  1.762   -8.452  1.00 48.95  ? 202 A1B8T B C14 1 
HETATM 1537 C  C16 . A1B8T D 4 .   ? -7.820  4.245   -15.165 1.00 52.24  ? 202 A1B8T B C16 1 
HETATM 1538 C  C18 . A1B8T D 4 .   ? -9.078  4.148   -17.248 1.00 51.98  ? 202 A1B8T B C18 1 
HETATM 1539 CL CL1 . A1B8T D 4 .   ? -10.579 3.882   -18.098 1.00 51.01  ? 202 A1B8T B CL1 1 
HETATM 1540 C  C19 . A1B8T D 4 .   ? -7.961  4.399   -18.018 1.00 53.12  ? 202 A1B8T B C19 1 
HETATM 1541 N  N4  . A1B8T D 4 .   ? -5.504  4.762   -17.815 1.00 55.46  ? 202 A1B8T B N4  1 
HETATM 1542 N  N5  . A1B8T D 4 .   ? -4.601  4.823   -16.795 1.00 55.74  ? 202 A1B8T B N5  1 
HETATM 1543 O  O   . HOH   E 5 .   ? -6.882  -4.848  6.768   1.00 61.35  ? 101 HOH   A O   1 
HETATM 1544 O  O   . HOH   E 5 .   ? -2.039  -4.079  -6.110  1.00 46.87  ? 102 HOH   A O   1 
HETATM 1545 O  O   . HOH   E 5 .   ? -4.120  -15.064 -25.192 1.00 41.79  ? 103 HOH   A O   1 
HETATM 1546 O  O   . HOH   E 5 .   ? -8.093  0.293   3.546   1.00 50.44  ? 104 HOH   A O   1 
HETATM 1547 O  O   . HOH   E 5 .   ? -23.306 18.558  -19.550 1.00 54.32  ? 105 HOH   A O   1 
HETATM 1548 O  O   . HOH   E 5 .   ? -23.631 8.822   -27.639 1.00 40.34  ? 106 HOH   A O   1 
HETATM 1549 O  O   . HOH   E 5 .   ? -28.890 15.290  -15.374 1.00 52.63  ? 107 HOH   A O   1 
HETATM 1550 O  O   . HOH   E 5 .   ? -30.837 -0.291  -29.617 1.00 51.68  ? 108 HOH   A O   1 
HETATM 1551 O  O   . HOH   E 5 .   ? -2.852  -12.116 -6.739  1.00 39.48  ? 109 HOH   A O   1 
HETATM 1552 O  O   . HOH   E 5 .   ? -1.111  -0.485  -8.476  1.00 67.98  ? 110 HOH   A O   1 
HETATM 1553 O  O   . HOH   E 5 .   ? -4.049  -0.811  -0.011  1.00 54.63  ? 111 HOH   A O   1 
HETATM 1554 O  O   . HOH   E 5 .   ? -27.779 -6.658  -28.409 1.00 58.52  ? 112 HOH   A O   1 
HETATM 1555 O  O   . HOH   E 5 .   ? -8.181  -1.867  7.023   1.00 48.78  ? 113 HOH   A O   1 
HETATM 1556 O  O   . HOH   E 5 .   ? -30.419 -0.075  -23.148 1.00 58.86  ? 114 HOH   A O   1 
HETATM 1557 O  O   . HOH   E 5 .   ? -4.548  -10.667 -5.312  1.00 39.78  ? 115 HOH   A O   1 
HETATM 1558 O  O   . HOH   E 5 .   ? -3.011  -8.823  -2.762  1.00 65.10  ? 116 HOH   A O   1 
HETATM 1559 O  O   . HOH   E 5 .   ? -5.250  4.804   -7.852  1.00 60.45  ? 117 HOH   A O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -15.307 -10.724 -14.873 1.00 51.40  ? 301 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -19.149 -12.683 -25.725 1.00 63.04  ? 302 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -25.730 -8.525  -16.668 1.00 39.79  ? 303 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -15.225 -5.003  1.587   1.00 43.78  ? 304 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -6.500  -0.910  -10.585 1.00 37.71  ? 305 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -33.690 1.306   -15.569 1.00 47.28  ? 306 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -20.591 -7.723  -5.529  1.00 67.20  ? 307 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -23.753 -6.996  -4.565  1.00 48.50  ? 308 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -16.971 12.355  -5.220  1.00 47.67  ? 309 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -16.763 -7.535  -7.992  1.00 49.97  ? 310 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -11.565 1.400   -5.601  1.00 39.87  ? 311 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -35.133 -6.016  -10.519 1.00 56.35  ? 312 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -22.203 14.616  -6.162  1.00 49.89  ? 313 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -17.708 -11.357 -16.275 1.00 42.80  ? 314 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -9.139  -7.367  -25.236 1.00 54.10  ? 315 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -12.355 -3.868  -10.012 1.00 41.49  ? 316 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -16.253 20.381  -14.347 1.00 51.10  ? 317 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -27.166 -7.236  -5.530  1.00 52.99  ? 318 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -21.230 -12.721 -12.952 1.00 57.10  ? 319 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -7.132  -7.012  0.735   1.00 59.67  ? 320 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -18.454 14.411  -22.071 1.00 43.73  ? 321 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -21.954 -14.259 -21.803 1.00 60.06  ? 322 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -12.653 -2.768  -14.647 1.00 36.95  ? 323 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -29.394 -2.108  -19.347 1.00 57.34  ? 324 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -27.532 -6.803  -18.818 1.00 46.67  ? 325 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -23.947 11.095  -26.440 1.00 54.54  ? 326 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -6.843  -9.671  -2.843  1.00 40.65  ? 327 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -16.000 -15.237 -16.320 1.00 47.66  ? 328 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -19.906 -8.905  -34.504 1.00 71.33  ? 329 HOH   B O   1 
HETATM 1589 O  O   . HOH   F 5 .   ? -10.723 11.696  -19.094 1.00 39.82  ? 330 HOH   B O   1 
HETATM 1590 O  O   . HOH   F 5 .   ? -31.896 6.768   -4.853  1.00 74.39  ? 331 HOH   B O   1 
HETATM 1591 O  O   . HOH   F 5 .   ? -20.700 1.913   -32.509 1.00 53.10  ? 332 HOH   B O   1 
HETATM 1592 O  O   . HOH   F 5 .   ? -15.561 -15.083 -30.613 1.00 53.73  ? 333 HOH   B O   1 
HETATM 1593 O  O   . HOH   F 5 .   ? -30.717 4.580   -2.930  1.00 54.20  ? 334 HOH   B O   1 
HETATM 1594 O  O   . HOH   F 5 .   ? -16.969 14.502  -30.735 1.00 48.38  ? 335 HOH   B O   1 
HETATM 1595 O  O   . HOH   F 5 .   ? -19.576 -14.199 -22.831 1.00 55.54  ? 336 HOH   B O   1 
HETATM 1596 O  O   . HOH   F 5 .   ? -10.211 -19.324 -11.789 1.00 57.99  ? 337 HOH   B O   1 
HETATM 1597 O  O   . HOH   F 5 .   ? -15.061 -9.207  -11.500 1.00 54.11  ? 338 HOH   B O   1 
HETATM 1598 O  O   . HOH   F 5 .   ? -14.487 15.935  -19.945 1.00 46.91  ? 339 HOH   B O   1 
HETATM 1599 O  O   . HOH   F 5 .   ? -7.042  -11.324 -5.066  1.00 51.53  ? 340 HOH   B O   1 
HETATM 1600 O  O   . HOH   F 5 .   ? 6.557   -5.474  -17.040 1.00 67.00  ? 341 HOH   B O   1 
HETATM 1601 O  O   . HOH   F 5 .   ? -23.638 -15.526 -18.264 1.00 68.16  ? 342 HOH   B O   1 
HETATM 1602 O  O   . HOH   F 5 .   ? -25.942 -5.278  -4.026  1.00 49.29  ? 343 HOH   B O   1 
HETATM 1603 O  O   . HOH   F 5 .   ? -8.954  -11.345 -7.011  1.00 53.87  ? 344 HOH   B O   1 
HETATM 1604 O  O   . HOH   F 5 .   ? -14.607 -12.857 -16.504 1.00 53.08  ? 345 HOH   B O   1 
HETATM 1605 O  O   . HOH   F 5 .   ? -14.382 -6.980  -1.173  1.00 58.61  ? 346 HOH   B O   1 
HETATM 1606 O  O   . HOH   F 5 .   ? 0.324   -0.459  -13.458 1.00 60.15  ? 347 HOH   B O   1 
HETATM 1607 O  O   . HOH   F 5 .   ? 5.403   -4.948  -26.646 1.00 91.35  ? 348 HOH   B O   1 
HETATM 1608 O  O   . HOH   F 5 .   ? -28.409 -8.628  -16.980 1.00 77.76  ? 349 HOH   B O   1 
HETATM 1609 O  O   . HOH   F 5 .   ? -19.699 -6.249  -0.797  1.00 50.23  ? 350 HOH   B O   1 
HETATM 1610 O  O   . HOH   F 5 .   ? -19.671 5.862   -33.082 1.00 68.86  ? 351 HOH   B O   1 
HETATM 1611 O  O   . HOH   F 5 .   ? -19.102 25.032  -14.229 1.00 56.99  ? 352 HOH   B O   1 
HETATM 1612 O  O   . HOH   F 5 .   ? -29.873 -5.904  -1.247  1.00 44.61  ? 353 HOH   B O   1 
HETATM 1613 O  O   . HOH   F 5 .   ? 4.731   -1.862  -15.965 1.00 64.90  ? 354 HOH   B O   1 
HETATM 1614 O  O   . HOH   F 5 .   ? -18.357 18.114  -21.894 1.00 65.26  ? 355 HOH   B O   1 
HETATM 1615 O  O   . HOH   F 5 .   ? -9.156  7.600   -13.108 1.00 42.89  ? 356 HOH   B O   1 
HETATM 1616 O  O   . HOH   F 5 .   ? -35.169 0.611   -7.833  1.00 65.41  ? 357 HOH   B O   1 
HETATM 1617 O  O   . HOH   F 5 .   ? -16.479 16.235  -21.695 1.00 62.82  ? 358 HOH   B O   1 
HETATM 1618 O  O   . HOH   F 5 .   ? -23.061 -7.942  -2.185  1.00 60.36  ? 359 HOH   B O   1 
HETATM 1619 O  O   . HOH   F 5 .   ? -29.584 -10.449 -28.863 0.50 36.07  ? 360 HOH   B O   1 
HETATM 1620 O  O   . HOH   F 5 .   ? -1.111  -15.585 -9.791  1.00 59.62  ? 361 HOH   B O   1 
HETATM 1621 O  O   . HOH   F 5 .   ? -32.112 -7.650  -7.067  1.00 54.81  ? 362 HOH   B O   1 
HETATM 1622 O  O   . HOH   F 5 .   ? -10.950 -7.564  2.076   1.00 55.91  ? 363 HOH   B O   1 
HETATM 1623 O  O   . HOH   F 5 .   ? -22.166 3.317   -0.854  0.50 41.10  ? 364 HOH   B O   1 
HETATM 1624 O  O   . HOH   F 5 .   ? -7.610  11.876  -18.538 1.00 62.30  ? 365 HOH   B O   1 
HETATM 1625 O  O   . HOH   F 5 .   ? -11.113 11.583  -14.603 1.00 58.55  ? 366 HOH   B O   1 
HETATM 1626 O  O   . HOH   F 5 .   ? -18.652 -12.625 -13.614 1.00 50.55  ? 367 HOH   B O   1 
HETATM 1627 O  O   . HOH   F 5 .   ? -17.420 27.335  -14.069 1.00 53.20  ? 368 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 0.8431 0.4969 0.9103 0.1241  0.0684  -0.1294 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.8354 0.5445 0.8713 0.1400  0.0776  -0.1223 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.8139 0.5294 0.8469 0.1343  0.0939  -0.0806 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.8401 0.5100 0.8821 0.1349  0.1005  -0.0573 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.8801 0.5884 0.8959 0.1742  0.0746  -0.1426 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.9527 0.7266 0.9455 0.1866  0.0758  -0.1624 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 0.9596 0.7366 0.9428 0.2067  0.0677  -0.1958 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 0.9857 0.8069 0.9700 0.1768  0.0859  -0.1438 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.7656 0.5348 0.7841 0.1296  0.1003  -0.0709 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.7355 0.5134 0.7474 0.1269  0.1129  -0.0366 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.7034 0.4985 0.6938 0.1522  0.1158  -0.0329 51  MET   A C   
12   O  O   . MET   A 8   ? 0.6890 0.5144 0.6710 0.1657  0.1114  -0.0553 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.7215 0.5413 0.7328 0.1069  0.1164  -0.0273 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.7222 0.5301 0.7600 0.0828  0.1141  -0.0249 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.7028 0.5604 0.7373 0.0655  0.1158  -0.0155 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.7057 0.5452 0.7843 0.0402  0.1117  -0.0147 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.6844 0.4639 0.6668 0.1596  0.1233  -0.0051 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.6708 0.4670 0.6356 0.1844  0.1226  -0.0015 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.6496 0.4602 0.6012 0.1828  0.1290  0.0250  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6421 0.4388 0.5961 0.1667  0.1369  0.0451  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.6878 0.4395 0.6482 0.2113  0.1183  -0.0033 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.7265 0.4176 0.6858 0.2103  0.1256  0.0252  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7481 0.3926 0.7280 0.1945  0.1268  0.0239  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.7494 0.4289 0.6869 0.2264  0.1313  0.0533  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7826 0.3718 0.7659 0.1905  0.1373  0.0540  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7807 0.4046 0.7129 0.2272  0.1421  0.0837  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.8043 0.3827 0.7614 0.2078  0.1468  0.0858  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8473 0.3719 0.8041 0.2048  0.1613  0.1197  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.6351 0.4769 0.5749 0.1998  0.1246  0.0227  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.6355 0.4897 0.5604 0.2014  0.1267  0.0425  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.6533 0.4871 0.5589 0.2325  0.1220  0.0533  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.6548 0.4827 0.5616 0.2547  0.1145  0.0405  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.6185 0.5269 0.5471 0.1891  0.1238  0.0330  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.6103 0.5578 0.5490 0.2017  0.1163  0.0103  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.6142 0.5346 0.5528 0.1612  0.1290  0.0298  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.6021 0.5985 0.5473 0.1902  0.1143  0.0064  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.6639 0.4847 0.5487 0.2372  0.1264  0.0771  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.6876 0.4886 0.5446 0.2690  0.1216  0.0907  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.6898 0.5177 0.5286 0.2726  0.1171  0.0967  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.6908 0.5196 0.5267 0.2543  0.1270  0.1091  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.7498 0.4917 0.5913 0.2744  0.1356  0.1199  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.8373 0.5362 0.6862 0.2858  0.1347  0.1167  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.9476 0.5825 0.7845 0.2887  0.1503  0.1492  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.9628 0.5916 0.7873 0.2803  0.1652  0.1758  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.0136 0.6037 0.8545 0.2998  0.1487  0.1486  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.6907 0.5398 0.5178 0.2978  0.1009  0.0868  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7007 0.5719 0.5098 0.3030  0.0926  0.0884  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.7375 0.5715 0.5069 0.3163  0.1034  0.1178  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.7700 0.5633 0.5176 0.3369  0.1104  0.1368  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.6977 0.6016 0.5078 0.3273  0.0695  0.0684  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.7248 0.6669 0.5410 0.3162  0.0578  0.0559  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.7430 0.7254 0.5742 0.3344  0.0331  0.0319  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.7474 0.7599 0.5877 0.3215  0.0204  0.0194  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.7772 0.7806 0.5849 0.3403  0.0067  0.0213  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.8225 0.7909 0.5827 0.3745  0.0062  0.0379  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.7329 0.7599 0.5530 0.3265  -0.0066 0.0066  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.7281 0.5742 0.4874 0.3058  0.1065  0.1229  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.7609 0.5789 0.4808 0.3206  0.1194  0.1503  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.7747 0.6093 0.4614 0.3419  0.1044  0.1443  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.7960 0.6104 0.4433 0.3601  0.1148  0.1655  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.7590 0.5684 0.4941 0.2918  0.1423  0.1665  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.7584 0.6291 0.4619 0.3395  0.0809  0.1156  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.7677 0.6523 0.4441 0.3588  0.0617  0.1043  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.7467 0.6691 0.4566 0.3369  0.0434  0.0759  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.7209 0.6613 0.4729 0.3052  0.0488  0.0677  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7573 0.6907 0.4478 0.3549  0.0206  0.0603  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.7533 0.7163 0.4752 0.3346  0.0014  0.0340  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.7807 0.7318 0.4961 0.3152  0.0132  0.0414  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8089 0.7345 0.4862 0.3288  0.0293  0.0621  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7720 0.7469 0.4750 0.3636  -0.0315 0.0114  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8394 0.8364 0.5556 0.3849  -0.0513 -0.0034 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8544 0.8549 0.5920 0.3794  -0.0383 0.0046  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8628 0.8741 0.5676 0.4095  -0.0819 -0.0249 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.7673 0.7371 0.5189 0.2858  0.0050  0.0252  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.7823 0.7386 0.5260 0.2713  0.0118  0.0300  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8046 0.7577 0.5294 0.2871  -0.0148 0.0092  59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.7853 0.7557 0.5436 0.2711  -0.0354 -0.0134 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.7565 0.7246 0.5425 0.2314  0.0229  0.0310  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.7602 0.7267 0.5558 0.2217  0.0473  0.0493  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.7638 0.7159 0.5390 0.2215  0.0254  0.0342  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.7545 0.7350 0.5848 0.1886  0.0570  0.0491  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8357 0.7673 0.5072 0.3200  -0.0145 0.0162  60  THR   A N   
83   N  N   B THR   A 17  ? 0.8393 0.7708 0.5111 0.3196  -0.0144 0.0163  60  THR   A N   
84   C  CA  A THR   A 17  ? 0.8620 0.7859 0.5045 0.3425  -0.0410 -0.0055 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.8688 0.7936 0.5118 0.3430  -0.0417 -0.0059 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9030 0.8025 0.4978 0.3615  -0.0270 0.0078  60  THR   A C   
87   C  C   B THR   A 17  ? 0.9078 0.8075 0.5005 0.3638  -0.0282 0.0072  60  THR   A C   
88   O  O   A THR   A 17  ? 0.9105 0.8008 0.4822 0.3711  0.0015  0.0361  60  THR   A O   
89   O  O   B THR   A 17  ? 0.9165 0.8068 0.4848 0.3746  0.0000  0.0355  60  THR   A O   
90   C  CB  A THR   A 17  ? 0.8805 0.8105 0.4937 0.3808  -0.0646 -0.0190 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.8909 0.8257 0.5137 0.3769  -0.0649 -0.0196 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.8991 0.8158 0.4716 0.4076  -0.0430 0.0088  60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.8745 0.8400 0.5534 0.3558  -0.0799 -0.0369 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.8609 0.8225 0.5244 0.3677  -0.0886 -0.0428 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9113 0.8377 0.4924 0.4103  -0.0953 -0.0436 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9295 0.8186 0.5098 0.3694  -0.0478 -0.0137 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 0.9911 0.8600 0.5226 0.3943  -0.0376 -0.0061 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.0606 0.9238 0.5276 0.4452  -0.0446 -0.0066 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.0646 0.9340 0.5241 0.4623  -0.0763 -0.0314 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 0.9921 0.8474 0.5313 0.3861  -0.0610 -0.0329 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0224 0.8573 0.5105 0.4167  -0.0564 -0.0331 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0561 0.8799 0.4870 0.4612  -0.0750 -0.0512 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0268 0.8515 0.5187 0.4062  -0.0362 -0.0199 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.0759 0.8842 0.4729 0.4803  -0.0635 -0.0481 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0606 0.8699 0.4971 0.4466  -0.0406 -0.0294 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0133 0.8425 0.5477 0.3698  -0.0156 -0.0017 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.0736 0.8738 0.5011 0.4511  -0.0243 -0.0212 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0301 0.8496 0.5547 0.3743  -0.0017 0.0065  61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0541 0.8605 0.5280 0.4144  -0.0053 -0.0028 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.1104 0.9645 0.5322 0.4699  -0.0147 0.0218  62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.1720 1.0188 0.5246 0.5206  -0.0162 0.0271  62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.2325 1.0674 0.5323 0.5537  -0.0215 0.0150  62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.2371 1.0695 0.5296 0.5523  0.0085  0.0353  62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.2148 1.0582 0.5486 0.5290  0.0247  0.0713  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.3400 1.1728 0.5961 0.5833  0.0269  0.0829  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.4481 1.2720 0.6719 0.5978  0.0736  0.1298  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.4656 1.2931 0.7359 0.5621  0.1044  0.1541  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.4927 1.3069 0.6448 0.6452  0.0794  0.1422  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.2772 1.1067 0.5381 0.5871  -0.0594 -0.0189 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.3376 1.1536 0.5386 0.6262  -0.0657 -0.0335 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.3831 1.1981 0.5162 0.6677  -0.0293 0.0030  63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.3997 1.2171 0.5121 0.6826  -0.0223 0.0223  63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.3886 1.1983 0.5617 0.6549  -0.1180 -0.0811 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.4400 1.2546 0.6860 0.6134  -0.1556 -0.1156 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.5200 1.3325 0.7404 0.6445  -0.2093 -0.1633 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5448 1.3684 0.8439 0.6031  -0.2462 -0.1965 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.5878 1.4134 0.8671 0.6336  -0.3006 -0.2448 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.4017 1.2142 0.5062 0.6833  -0.0026 0.0161  64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.4359 1.2517 0.4826 0.7186  0.0392  0.0555  64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.4146 1.2389 0.5037 0.6855  0.0821  0.1027  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.4323 1.2530 0.4877 0.7054  0.1027  0.1333  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.5125 1.3208 0.4725 0.7780  0.0233  0.0493  64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.6318 1.4315 0.5380 0.8191  -0.0125 0.0050  64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.6566 1.4560 0.5561 0.8246  0.0003  -0.0001 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.6880 1.4816 0.5604 0.8469  -0.0554 -0.0272 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.3782 1.2108 0.5399 0.6361  0.0940  0.1078  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.3540 1.1951 0.5624 0.6020  0.1330  0.1474  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.3442 1.1989 0.5427 0.6114  0.1752  0.1747  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.3543 1.2119 0.5180 0.6394  0.1701  0.1580  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.3264 1.1727 0.6152 0.5471  0.1203  0.1346  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.3202 1.1843 0.5516 0.5892  0.2160  0.2148  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.3064 1.1917 0.5416 0.5941  0.2574  0.2411  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.2577 1.1585 0.5429 0.5684  0.2480  0.2195  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.2269 1.1290 0.5745 0.5246  0.2377  0.2131  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.3355 1.2270 0.6065 0.5701  0.3002  0.2870  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.3950 1.3155 0.6788 0.5733  0.3453  0.3160  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.4511 1.3842 0.8061 0.5304  0.3793  0.3498  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.4642 1.3772 0.8505 0.5014  0.3705  0.3540  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.4462 1.4107 0.8283 0.5265  0.4138  0.3701  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.2471 1.1577 0.4997 0.5996  0.2499  0.2072  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.2169 1.1381 0.5073 0.5841  0.2401  0.1871  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.1769 1.1338 0.5023 0.5766  0.2845  0.2181  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.1900 1.1643 0.4763 0.6124  0.3151  0.2370  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.2470 1.1536 0.4862 0.6226  0.2100  0.1490  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.2370 1.1389 0.5211 0.5977  0.1876  0.1242  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.2837 1.1615 0.4741 0.6439  0.1718  0.1220  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.1272 1.0984 0.5266 0.5316  0.2884  0.2235  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.0893 1.0997 0.5365 0.5186  0.3265  0.2502  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.0551 1.0768 0.5708 0.4796  0.3113  0.2367  68  THR   A C   
160  O  O   . THR   A 25  ? 1.0529 1.0495 0.5771 0.4605  0.2763  0.2123  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.0988 1.1172 0.5654 0.5024  0.3623  0.2903  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.0883 1.1482 0.5851 0.5040  0.4054  0.3190  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.0870 1.0923 0.6098 0.4535  0.3495  0.2910  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0193 1.0806 0.5824 0.4701  0.3376  0.2528  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 0.9891 1.0648 0.6136 0.4378  0.3243  0.2423  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 0.9908 1.0710 0.6042 0.4607  0.3074  0.2188  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0205 1.0729 0.5778 0.4920  0.2873  0.1973  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.9561 1.0694 0.6247 0.4452  0.3127  0.2210  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.9518 1.0703 0.6172 0.4663  0.2969  0.2009  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9281 1.0122 0.6058 0.4414  0.2568  0.1785  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.9292 0.9881 0.6130 0.4110  0.2426  0.1771  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9499 1.1298 0.6645 0.4725  0.3268  0.2166  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9797 1.1902 0.7718 0.4286  0.3312  0.2283  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9919 1.1988 0.8080 0.3964  0.3400  0.2432  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9786 1.2199 0.8108 0.4292  0.3238  0.2203  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.9100 0.9896 0.5854 0.4580  0.2390  0.1613  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.9028 0.9467 0.5836 0.4396  0.2039  0.1437  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.8515 0.9253 0.5741 0.4389  0.2018  0.1446  71  SER   A C   
179  O  O   . SER   A 28  ? 0.8604 0.9168 0.5638 0.4644  0.1850  0.1294  71  SER   A O   
180  C  CB  . SER   A 28  ? 0.9665 0.9583 0.5907 0.4666  0.1767  0.1185  71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.0309 1.0019 0.6120 0.4787  0.1767  0.1137  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.7969 0.9149 0.5770 0.4121  0.2167  0.1605  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.7585 0.9109 0.5793 0.4151  0.2122  0.1593  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.7532 0.8686 0.5695 0.4014  0.1781  0.1470  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.7557 0.8358 0.5621 0.3732  0.1642  0.1453  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.7308 0.9379 0.6157 0.3863  0.2351  0.1774  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.7526 0.9311 0.6287 0.3552  0.2366  0.1838  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.7714 0.9090 0.5834 0.3796  0.2359  0.1783  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.7453 0.8698 0.5684 0.4233  0.1658  0.1399  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.7599 0.8516 0.5784 0.4142  0.1355  0.1329  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.7107 0.8581 0.5871 0.3980  0.1381  0.1406  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.6892 0.8867 0.5963 0.4203  0.1474  0.1412  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.8057 0.8658 0.5896 0.4542  0.1181  0.1197  73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.8938 0.9001 0.6228 0.4729  0.1125  0.1071  73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 0.9909 0.9339 0.6827 0.4929  0.0828  0.0926  73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.0731 0.9725 0.7168 0.5190  0.0765  0.0751  73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.1236 0.9703 0.7397 0.5011  0.0623  0.0666  73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.1294 0.9619 0.7612 0.4572  0.0560  0.0759  73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.1296 0.9402 0.7035 0.5284  0.0532  0.0469  73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.6904 0.8346 0.5847 0.3605  0.1308  0.1448  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.6430 0.8408 0.5936 0.3432  0.1309  0.1484  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.6469 0.8259 0.5911 0.3337  0.1027  0.1442  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.6727 0.8015 0.5818 0.3171  0.0909  0.1441  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6154 0.8336 0.5979 0.3080  0.1490  0.1563  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6065 0.8426 0.5946 0.3144  0.1805  0.1660  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.5959 0.8374 0.6090 0.2794  0.1945  0.1748  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.5727 0.8714 0.6017 0.3382  0.1994  0.1704  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.6153 0.8393 0.5962 0.3426  0.0929  0.1415  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.6305 0.8412 0.6026 0.3353  0.0658  0.1387  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5967 0.8344 0.6041 0.2982  0.0670  0.1379  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5621 0.8588 0.6282 0.2896  0.0782  0.1360  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.6488 0.8952 0.6405 0.3664  0.0501  0.1338  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7881 0.9889 0.7319 0.4043  0.0378  0.1328  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.8439 0.9903 0.7449 0.4074  0.0437  0.1341  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.8295 1.0483 0.7798 0.4320  0.0202  0.1293  75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.5989 0.7937 0.5733 0.2755  0.0577  0.1391  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.5732 0.7879 0.5751 0.2431  0.0583  0.1354  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.5761 0.7736 0.5521 0.2361  0.0344  0.1320  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.6080 0.7619 0.5347 0.2492  0.0222  0.1377  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5849 0.7764 0.5804 0.2189  0.0782  0.1394  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5720 0.7812 0.5876 0.2272  0.1036  0.1453  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.6302 0.7599 0.5681 0.2151  0.0726  0.1429  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.5397 0.7692 0.5476 0.2159  0.0282  0.1230  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.5436 0.7614 0.5242 0.2095  0.0076  0.1181  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.5325 0.7408 0.5155 0.1788  0.0162  0.1132  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5149 0.7457 0.5418 0.1626  0.0305  0.1089  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.5180 0.7862 0.5311 0.2208  -0.0150 0.1057  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.5369 0.7110 0.4725 0.1721  0.0092  0.1154  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.5240 0.6885 0.4566 0.1474  0.0166  0.1095  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.5371 0.7176 0.4594 0.1457  -0.0034 0.0967  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.5610 0.7248 0.4365 0.1596  -0.0162 0.1031  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.5371 0.6522 0.4243 0.1416  0.0289  0.1222  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.5351 0.6399 0.4148 0.1199  0.0371  0.1169  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.4963 0.6177 0.4194 0.1056  0.0496  0.1088  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.5696 0.6324 0.4084 0.1154  0.0464  0.1293  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.5105 0.7228 0.4759 0.1310  -0.0074 0.0785  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.5182 0.7482 0.4744 0.1322  -0.0299 0.0609  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.5519 0.7536 0.4654 0.1211  -0.0240 0.0589  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.5704 0.7431 0.4713 0.1100  -0.0029 0.0700  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.4983 0.7769 0.5231 0.1236  -0.0432 0.0380  79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.5236 0.8035 0.5941 0.0968  -0.0290 0.0282  79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.5441 0.7895 0.5870 0.0866  -0.0127 0.0345  79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.5150 0.8310 0.6515 0.0863  -0.0351 0.0142  79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.5566 0.7698 0.4464 0.1269  -0.0432 0.0437  80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.5827 0.7774 0.4311 0.1208  -0.0381 0.0394  80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.5681 0.7592 0.4502 0.0989  -0.0242 0.0268  80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.5908 0.7617 0.4430 0.0931  -0.0111 0.0293  80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.6255 0.8391 0.4426 0.1364  -0.0640 0.0219  80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.7251 0.9179 0.4759 0.1411  -0.0564 0.0276  80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.8140 1.0259 0.5258 0.1607  -0.0818 0.0097  80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.8009 1.0335 0.5346 0.1565  -0.0963 -0.0220 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.8710 1.0750 0.5290 0.1819  -0.0887 0.0268  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.5304 0.7404 0.4757 0.0870  -0.0254 0.0152  81  SER   A N   
254  C  CA  . SER   A 38  ? 0.5149 0.7153 0.4924 0.0675  -0.0124 0.0060  81  SER   A CA  
255  C  C   . SER   A 38  ? 0.5010 0.6764 0.4825 0.0600  0.0148  0.0279  81  SER   A C   
256  O  O   . SER   A 38  ? 0.4879 0.6530 0.4956 0.0464  0.0264  0.0239  81  SER   A O   
257  C  CB  . SER   A 38  ? 0.5043 0.7319 0.5502 0.0558  -0.0242 -0.0137 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.5326 0.7841 0.5766 0.0631  -0.0537 -0.0396 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.5031 0.6667 0.4585 0.0702  0.0230  0.0496  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.5045 0.6458 0.4611 0.0664  0.0448  0.0672  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.4805 0.6356 0.4846 0.0645  0.0535  0.0728  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.4790 0.6177 0.4866 0.0620  0.0716  0.0845  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.4609 0.6494 0.5012 0.0677  0.0412  0.0654  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.4405 0.6510 0.5321 0.0658  0.0525  0.0722  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4382 0.6598 0.5222 0.0865  0.0529  0.0852  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4259 0.6643 0.5011 0.1000  0.0336  0.0799  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4212 0.6682 0.5741 0.0529  0.0405  0.0540  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.4746 0.7066 0.6447 0.0327  0.0420  0.0407  83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5143 0.7157 0.6703 0.0270  0.0608  0.0512  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.5017 0.7521 0.6997 0.0243  0.0223  0.0181  83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4427 0.6542 0.5275 0.0920  0.0738  0.1011  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4469 0.6682 0.5264 0.1144  0.0758  0.1112  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4397 0.7135 0.5829 0.1157  0.0780  0.1084  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4117 0.7060 0.6054 0.0965  0.0877  0.1053  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4498 0.6419 0.5027 0.1231  0.0962  0.1261  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.4812 0.6261 0.4761 0.1254  0.0923  0.1292  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.5040 0.6298 0.4615 0.1416  0.0793  0.1321  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.4908 0.6107 0.4723 0.1112  0.1015  0.1297  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5344 0.6174 0.4468 0.1396  0.0773  0.1362  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5128 0.5965 0.4506 0.1113  0.0982  0.1317  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5290 0.5950 0.4350 0.1236  0.0870  0.1354  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4592 0.7546 0.6033 0.1384  0.0689  0.1095  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4531 0.8064 0.6611 0.1438  0.0714  0.1070  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4948 0.8548 0.6869 0.1758  0.0763  0.1165  85  SER   A C   
285  O  O   . SER   A 42  ? 0.5244 0.8452 0.6575 0.1940  0.0660  0.1198  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4482 0.8393 0.6890 0.1402  0.0427  0.0878  85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.5082 0.8777 0.6929 0.1599  0.0184  0.0843  85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4911 0.9005 0.7372 0.1833  0.0926  0.1208  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5247 0.9450 0.7576 0.2179  0.0975  0.1270  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5354 0.9888 0.7814 0.2393  0.0695  0.1155  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.4917 1.0021 0.8014 0.2304  0.0595  0.1045  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.5052 0.9694 0.7871 0.2218  0.1301  0.1381  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5623 0.9907 0.8141 0.2170  0.1601  0.1537  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5439 1.0222 0.8442 0.2233  0.1940  0.1671  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.6196 0.9900 0.7912 0.2426  0.1550  0.1557  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5928 1.0104 0.7811 0.2690  0.0561  0.1176  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.6191 1.0594 0.8082 0.2978  0.0293  0.1096  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6375 1.1166 0.8532 0.3297  0.0430  0.1124  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6689 1.1159 0.8505 0.3436  0.0623  0.1215  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6746 1.0455 0.7824 0.3128  0.0083  0.1135  87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6817 1.0676 0.7819 0.3494  -0.0181 0.1089  87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6964 1.0361 0.7777 0.2839  -0.0026 0.1112  87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.6137 1.1659 0.8932 0.3420  0.0340  0.1029  88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.6173 1.2154 0.9266 0.3757  0.0479  0.1045  88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.6091 1.2477 0.9366 0.4098  0.0169  0.0923  88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.6494 1.2407 0.9191 0.4265  -0.0126 0.0900  88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.6150 1.2807 1.0041 0.3571  0.0828  0.1096  88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.7169 1.3441 1.0887 0.3259  0.1129  0.1233  88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.8210 1.4360 1.1655 0.3473  0.1466  0.1371  88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.8034 1.4728 1.1809 0.3763  0.1604  0.1379  88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.8905 1.4445 1.1802 0.3371  0.1585  0.1459  88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.8032 0.8169 0.8089 0.1923  0.1241  -0.0080 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.8108 0.8201 0.8156 0.2066  0.1191  -0.0059 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.8058 0.8232 0.8154 0.2071  0.1058  -0.0034 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.8027 0.8411 0.8294 0.2077  0.0986  -0.0046 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.7982 0.7990 0.7929 0.2070  0.1020  0.0002  17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.7827 0.7870 0.7763 0.2099  0.0892  0.0022  17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.7655 0.7758 0.7613 0.1947  0.0830  0.0013  17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.7806 0.7797 0.7649 0.1857  0.0861  0.0031  17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.8128 0.7980 0.7885 0.2192  0.0890  0.0077  17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 0.8540 0.8413 0.8253 0.2309  0.0764  0.0093  17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 0.9473 0.9169 0.9000 0.2433  0.0782  0.0164  17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 0.9639 0.9199 0.9096 0.2401  0.0892  0.0210  17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 0.9806 0.9497 0.9258 0.2568  0.0684  0.0176  17  GLU   B OE2 
325  N  N   A THR   B 9   ? 0.7420 0.7697 0.7530 0.1917  0.0739  -0.0012 18  THR   B N   
326  N  N   B THR   B 9   ? 0.7411 0.7688 0.7522 0.1920  0.0739  -0.0012 18  THR   B N   
327  C  CA  A THR   B 9   ? 0.7326 0.7636 0.7453 0.1774  0.0673  -0.0015 18  THR   B CA  
328  C  CA  B THR   B 9   ? 0.7301 0.7623 0.7441 0.1777  0.0672  -0.0017 18  THR   B CA  
329  C  C   A THR   B 9   ? 0.7195 0.7483 0.7281 0.1817  0.0505  -0.0017 18  THR   B C   
330  C  C   B THR   B 9   ? 0.7190 0.7472 0.7269 0.1817  0.0509  -0.0016 18  THR   B C   
331  O  O   A THR   B 9   ? 0.7199 0.7500 0.7300 0.1709  0.0429  -0.0024 18  THR   B O   
332  O  O   B THR   B 9   ? 0.7201 0.7484 0.7280 0.1709  0.0437  -0.0021 18  THR   B O   
333  C  CB  A THR   B 9   ? 0.7398 0.7894 0.7723 0.1656  0.0712  -0.0033 18  THR   B CB  
334  C  CB  B THR   B 9   ? 0.7332 0.7872 0.7706 0.1690  0.0688  -0.0037 18  THR   B CB  
335  O  OG1 A THR   B 9   ? 0.7458 0.8132 0.7974 0.1737  0.0735  -0.0047 18  THR   B OG1 
336  O  OG1 B THR   B 9   ? 0.7342 0.8040 0.7892 0.1774  0.0586  -0.0052 18  THR   B OG1 
337  C  CG2 A THR   B 9   ? 0.7488 0.7923 0.7737 0.1548  0.0843  -0.0029 18  THR   B CG2 
338  C  CG2 B THR   B 9   ? 0.7384 0.7963 0.7795 0.1678  0.0851  -0.0042 18  THR   B CG2 
339  N  N   . THR   B 10  ? 0.7079 0.7309 0.7086 0.1982  0.0445  -0.0010 19  THR   B N   
340  C  CA  . THR   B 10  ? 0.6908 0.7080 0.6822 0.2057  0.0280  -0.0018 19  THR   B CA  
341  C  C   . THR   B 10  ? 0.6654 0.6671 0.6369 0.2005  0.0257  0.0007  19  THR   B C   
342  O  O   . THR   B 10  ? 0.6727 0.6646 0.6322 0.1996  0.0369  0.0049  19  THR   B O   
343  C  CB  . THR   B 10  ? 0.7233 0.7329 0.7029 0.2270  0.0258  -0.0001 19  THR   B CB  
344  O  OG1 . THR   B 10  ? 0.7492 0.7721 0.7454 0.2337  0.0295  -0.0020 19  THR   B OG1 
345  C  CG2 . THR   B 10  ? 0.7262 0.7291 0.6937 0.2383  0.0074  -0.0019 19  THR   B CG2 
346  N  N   . ASP   B 11  ? 0.6365 0.6358 0.6051 0.1970  0.0105  -0.0019 20  ASP   B N   
347  C  CA  . ASP   B 11  ? 0.6401 0.6237 0.5873 0.1954  0.0066  0.0002  20  ASP   B CA  
348  C  C   . ASP   B 11  ? 0.6433 0.6131 0.5672 0.2137  0.0095  0.0051  20  ASP   B C   
349  O  O   . ASP   B 11  ? 0.6519 0.6217 0.5740 0.2289  0.0074  0.0053  20  ASP   B O   
350  C  CB  . ASP   B 11  ? 0.6644 0.6437 0.6094 0.1936  -0.0133 -0.0043 20  ASP   B CB  
351  C  CG  . ASP   B 11  ? 0.7262 0.7127 0.6876 0.1733  -0.0164 -0.0065 20  ASP   B CG  
352  O  OD1 . ASP   B 11  ? 0.7068 0.7071 0.6864 0.1614  -0.0035 -0.0054 20  ASP   B OD1 
353  O  OD2 . ASP   B 11  ? 0.7578 0.7343 0.7122 0.1698  -0.0317 -0.0091 20  ASP   B OD2 
354  N  N   . GLY   B 12  ? 0.6293 0.5886 0.5363 0.2128  0.0145  0.0097  21  GLY   B N   
355  C  CA  . GLY   B 12  ? 0.6189 0.5679 0.5064 0.2294  0.0193  0.0165  21  GLY   B CA  
356  C  C   . GLY   B 12  ? 0.6011 0.5479 0.4844 0.2229  0.0334  0.0233  21  GLY   B C   
357  O  O   . GLY   B 12  ? 0.5821 0.5331 0.4736 0.2063  0.0375  0.0216  21  GLY   B O   
358  N  N   . VAL   B 13  ? 0.5937 0.5340 0.4640 0.2365  0.0404  0.0314  22  VAL   B N   
359  C  CA  . VAL   B 13  ? 0.5791 0.5192 0.4483 0.2312  0.0533  0.0393  22  VAL   B CA  
360  C  C   . VAL   B 13  ? 0.5697 0.5112 0.4511 0.2297  0.0665  0.0430  22  VAL   B C   
361  O  O   . VAL   B 13  ? 0.5719 0.5109 0.4530 0.2415  0.0667  0.0434  22  VAL   B O   
362  C  CB  . VAL   B 13  ? 0.5859 0.5196 0.4343 0.2459  0.0529  0.0475  22  VAL   B CB  
363  C  CG1 . VAL   B 13  ? 0.5860 0.5133 0.4216 0.2683  0.0543  0.0536  22  VAL   B CG1 
364  C  CG2 . VAL   B 13  ? 0.5822 0.5201 0.4342 0.2376  0.0643  0.0553  22  VAL   B CG2 
365  N  N   . TYR   B 14  ? 0.5563 0.5004 0.4482 0.2147  0.0759  0.0443  23  TYR   B N   
366  C  CA  . TYR   B 14  ? 0.5492 0.4910 0.4519 0.2108  0.0869  0.0463  23  TYR   B CA  
367  C  C   . TYR   B 14  ? 0.5551 0.4946 0.4597 0.2050  0.0967  0.0550  23  TYR   B C   
368  O  O   . TYR   B 14  ? 0.5577 0.5015 0.4608 0.1975  0.0952  0.0563  23  TYR   B O   
369  C  CB  . TYR   B 14  ? 0.5405 0.4868 0.4562 0.1956  0.0874  0.0369  23  TYR   B CB  
370  C  CG  . TYR   B 14  ? 0.5389 0.4907 0.4604 0.2001  0.0809  0.0297  23  TYR   B CG  
371  C  CD1 . TYR   B 14  ? 0.5405 0.4976 0.4595 0.2018  0.0687  0.0255  23  TYR   B CD1 
372  C  CD2 . TYR   B 14  ? 0.5521 0.5036 0.4820 0.2030  0.0864  0.0273  23  TYR   B CD2 
373  C  CE1 . TYR   B 14  ? 0.5523 0.5167 0.4801 0.2057  0.0616  0.0196  23  TYR   B CE1 
374  C  CE2 . TYR   B 14  ? 0.5657 0.5257 0.5033 0.2088  0.0803  0.0216  23  TYR   B CE2 
375  C  CZ  . TYR   B 14  ? 0.5713 0.5392 0.5097 0.2092  0.0677  0.0179  23  TYR   B CZ  
376  O  OH  . TYR   B 14  ? 0.5865 0.5657 0.5373 0.2125  0.0608  0.0124  23  TYR   B OH  
377  N  N   . ARG   B 15  ? 0.5561 0.4889 0.4657 0.2071  0.1062  0.0608  24  ARG   B N   
378  C  CA  . ARG   B 15  ? 0.5544 0.4851 0.4710 0.1984  0.1149  0.0689  24  ARG   B CA  
379  C  C   . ARG   B 15  ? 0.5519 0.4804 0.4793 0.1807  0.1161  0.0607  24  ARG   B C   
380  O  O   . ARG   B 15  ? 0.5548 0.4793 0.4842 0.1802  0.1157  0.0529  24  ARG   B O   
381  C  CB  . ARG   B 15  ? 0.5675 0.4887 0.4846 0.2082  0.1246  0.0796  24  ARG   B CB  
382  C  CG  . ARG   B 15  ? 0.5848 0.5059 0.4882 0.2288  0.1256  0.0894  24  ARG   B CG  
383  C  CD  . ARG   B 15  ? 0.6192 0.5289 0.5224 0.2382  0.1364  0.1005  24  ARG   B CD  
384  N  NE  . ARG   B 15  ? 0.6591 0.5662 0.5447 0.2616  0.1362  0.1073  24  ARG   B NE  
385  C  CZ  . ARG   B 15  ? 0.6834 0.5940 0.5598 0.2730  0.1408  0.1197  24  ARG   B CZ  
386  N  NH1 . ARG   B 15  ? 0.6680 0.5875 0.5547 0.2624  0.1466  0.1278  24  ARG   B NH1 
387  N  NH2 . ARG   B 15  ? 0.6784 0.5843 0.5348 0.2964  0.1395  0.1243  24  ARG   B NH2 
388  N  N   . VAL   B 16  ? 0.5482 0.4793 0.4819 0.1674  0.1174  0.0626  25  VAL   B N   
389  C  CA  . VAL   B 16  ? 0.5407 0.4669 0.4817 0.1515  0.1179  0.0549  25  VAL   B CA  
390  C  C   . VAL   B 16  ? 0.5382 0.4549 0.4883 0.1471  0.1251  0.0630  25  VAL   B C   
391  O  O   . VAL   B 16  ? 0.5329 0.4552 0.4889 0.1450  0.1274  0.0732  25  VAL   B O   
392  C  CB  . VAL   B 16  ? 0.5412 0.4759 0.4819 0.1394  0.1121  0.0500  25  VAL   B CB  
393  C  CG1 . VAL   B 16  ? 0.5470 0.4742 0.4912 0.1254  0.1120  0.0412  25  VAL   B CG1 
394  C  CG2 . VAL   B 16  ? 0.5416 0.4841 0.4732 0.1439  0.1051  0.0448  25  VAL   B CG2 
395  N  N   . MET   B 17  ? 0.5495 0.4518 0.5008 0.1469  0.1288  0.0596  26  MET   B N   
396  C  CA  . MET   B 17  ? 0.5729 0.4611 0.5317 0.1430  0.1352  0.0669  26  MET   B CA  
397  C  C   . MET   B 17  ? 0.6154 0.4906 0.5782 0.1277  0.1331  0.0581  26  MET   B C   
398  O  O   . MET   B 17  ? 0.6181 0.4934 0.5749 0.1241  0.1288  0.0459  26  MET   B O   
399  C  CB  . MET   B 17  ? 0.5791 0.4550 0.5322 0.1577  0.1409  0.0701  26  MET   B CB  
400  C  CG  . MET   B 17  ? 0.5916 0.4769 0.5361 0.1759  0.1409  0.0757  26  MET   B CG  
401  S  SD  . MET   B 17  ? 0.6319 0.5233 0.5789 0.1820  0.1473  0.0944  26  MET   B SD  
402  C  CE  . MET   B 17  ? 0.6192 0.4888 0.5723 0.1815  0.1580  0.1046  26  MET   B CE  
403  N  N   . THR   B 18  ? 0.6464 0.5090 0.6187 0.1194  0.1363  0.0648  27  THR   B N   
404  C  CA  . THR   B 18  ? 0.6851 0.5294 0.6594 0.1061  0.1332  0.0567  27  THR   B CA  
405  C  C   . THR   B 18  ? 0.7258 0.5474 0.7051 0.1056  0.1391  0.0644  27  THR   B C   
406  O  O   . THR   B 18  ? 0.7128 0.5370 0.6997 0.1103  0.1457  0.0791  27  THR   B O   
407  C  CB  . THR   B 18  ? 0.6935 0.5457 0.6764 0.0895  0.1258  0.0540  27  THR   B CB  
408  O  OG1 . THR   B 18  ? 0.7194 0.5507 0.6978 0.0796  0.1209  0.0424  27  THR   B OG1 
409  C  CG2 . THR   B 18  ? 0.6804 0.5410 0.6822 0.0821  0.1278  0.0690  27  THR   B CG2 
410  N  N   . ARG   B 19  ? 0.7718 0.5694 0.7450 0.1006  0.1369  0.0546  28  ARG   B N   
411  C  CA  . ARG   B 19  ? 0.8233 0.5941 0.7997 0.0983  0.1409  0.0606  28  ARG   B CA  
412  C  C   . ARG   B 19  ? 0.8559 0.6109 0.8422 0.0779  0.1335  0.0576  28  ARG   B C   
413  O  O   . ARG   B 19  ? 0.8696 0.5980 0.8585 0.0731  0.1348  0.0610  28  ARG   B O   
414  C  CB  . ARG   B 19  ? 0.8703 0.6206 0.8299 0.1125  0.1447  0.0536  28  ARG   B CB  
415  C  CG  . ARG   B 19  ? 0.9390 0.7016 0.8930 0.1325  0.1518  0.0604  28  ARG   B CG  
416  C  CD  . ARG   B 19  ? 1.0183 0.7576 0.9600 0.1465  0.1569  0.0589  28  ARG   B CD  
417  N  NE  . ARG   B 19  ? 1.0703 0.8230 1.0053 0.1666  0.1610  0.0624  28  ARG   B NE  
418  C  CZ  . ARG   B 19  ? 1.1037 0.8663 1.0305 0.1777  0.1589  0.0517  28  ARG   B CZ  
419  N  NH1 . ARG   B 19  ? 1.1038 0.8654 1.0268 0.1717  0.1547  0.0380  28  ARG   B NH1 
420  N  NH2 . ARG   B 19  ? 1.0935 0.8681 1.0163 0.1952  0.1607  0.0552  28  ARG   B NH2 
421  N  N   . ARG   B 20  ? 0.8679 0.6387 0.8599 0.0660  0.1249  0.0518  29  ARG   B N   
422  C  CA  . ARG   B 20  ? 0.8923 0.6528 0.8938 0.0467  0.1147  0.0471  29  ARG   B CA  
423  C  C   . ARG   B 20  ? 0.8868 0.6502 0.9147 0.0340  0.1161  0.0635  29  ARG   B C   
424  O  O   . ARG   B 20  ? 0.9008 0.6434 0.9378 0.0191  0.1093  0.0621  29  ARG   B O   
425  C  CB  . ARG   B 20  ? 0.9231 0.7036 0.9218 0.0410  0.1058  0.0373  29  ARG   B CB  
426  C  CG  . ARG   B 20  ? 1.0055 0.7714 1.0063 0.0241  0.0927  0.0272  29  ARG   B CG  
427  C  CD  . ARG   B 20  ? 1.0749 0.8616 1.0718 0.0201  0.0844  0.0192  29  ARG   B CD  
428  N  NE  . ARG   B 20  ? 1.1235 0.9410 1.1412 0.0155  0.0846  0.0319  29  ARG   B NE  
429  C  CZ  . ARG   B 20  ? 1.1607 0.9863 1.1977 0.0002  0.0755  0.0350  29  ARG   B CZ  
430  N  NH1 . ARG   B 20  ? 1.1707 0.9738 1.2084 -0.0131 0.0638  0.0256  29  ARG   B NH1 
431  N  NH2 . ARG   B 20  ? 1.1438 1.0000 1.1990 -0.0010 0.0772  0.0473  29  ARG   B NH2 
432  N  N   . LEU   B 21  ? 0.8647 0.6534 0.9048 0.0402  0.1245  0.0794  30  LEU   B N   
433  C  CA  . LEU   B 21  ? 0.8463 0.6430 0.9134 0.0301  0.1285  0.0978  30  LEU   B CA  
434  C  C   . LEU   B 21  ? 0.8420 0.6180 0.9092 0.0378  0.1406  0.1110  30  LEU   B C   
435  O  O   . LEU   B 21  ? 0.8623 0.6110 0.9105 0.0456  0.1416  0.1024  30  LEU   B O   
436  C  CB  . LEU   B 21  ? 0.8340 0.6691 0.9110 0.0354  0.1321  0.1083  30  LEU   B CB  
437  C  CG  . LEU   B 21  ? 0.8471 0.7050 0.9360 0.0228  0.1211  0.1034  30  LEU   B CG  
438  C  CD1 . LEU   B 21  ? 0.8654 0.7094 0.9384 0.0160  0.1079  0.0818  30  LEU   B CD1 
439  C  CD2 . LEU   B 21  ? 0.8453 0.7357 0.9315 0.0353  0.1251  0.1095  30  LEU   B CD2 
440  N  N   . LEU   B 22  ? 0.8132 0.6012 0.9008 0.0366  0.1503  0.1323  31  LEU   B N   
441  C  CA  . LEU   B 22  ? 0.8057 0.5744 0.8920 0.0451  0.1628  0.1465  31  LEU   B CA  
442  C  C   . LEU   B 22  ? 0.7989 0.5721 0.8606 0.0710  0.1713  0.1463  31  LEU   B C   
443  O  O   . LEU   B 22  ? 0.7919 0.5931 0.8492 0.0812  0.1719  0.1465  31  LEU   B O   
444  C  CB  . LEU   B 22  ? 0.7871 0.5719 0.9020 0.0380  0.1723  0.1708  31  LEU   B CB  
445  C  CG  . LEU   B 22  ? 0.8028 0.5648 0.9183 0.0438  0.1855  0.1874  31  LEU   B CG  
446  C  CD1 . LEU   B 22  ? 0.8182 0.5424 0.9406 0.0256  0.1791  0.1832  31  LEU   B CD1 
447  C  CD2 . LEU   B 22  ? 0.7936 0.5805 0.9301 0.0469  0.1997  0.2136  31  LEU   B CD2 
448  N  N   . GLY   B 23  ? 0.7964 0.5413 0.8413 0.0819  0.1761  0.1446  32  GLY   B N   
449  C  CA  . GLY   B 23  ? 0.7945 0.5413 0.8165 0.1066  0.1822  0.1432  32  GLY   B CA  
450  C  C   . GLY   B 23  ? 0.7832 0.5492 0.7916 0.1141  0.1742  0.1265  32  GLY   B C   
451  O  O   . GLY   B 23  ? 0.7873 0.5487 0.7924 0.1043  0.1644  0.1100  32  GLY   B O   
452  N  N   . SER   B 24  ? 0.7667 0.5539 0.7670 0.1311  0.1782  0.1313  33  SER   B N   
453  C  CA  . SER   B 24  ? 0.7545 0.5613 0.7442 0.1375  0.1707  0.1179  33  SER   B CA  
454  C  C   . SER   B 24  ? 0.7197 0.5549 0.7189 0.1357  0.1706  0.1264  33  SER   B C   
455  O  O   . SER   B 24  ? 0.7137 0.5568 0.7166 0.1444  0.1792  0.1431  33  SER   B O   
456  C  CB  . SER   B 24  ? 0.7888 0.5940 0.7593 0.1598  0.1729  0.1146  33  SER   B CB  
457  O  OG  . SER   B 24  ? 0.8439 0.6246 0.8054 0.1627  0.1729  0.1060  33  SER   B OG  
458  N  N   . THR   B 25  ? 0.6959 0.5458 0.6982 0.1254  0.1613  0.1156  34  THR   B N   
459  C  CA  . THR   B 25  ? 0.6741 0.5501 0.6851 0.1233  0.1602  0.1227  34  THR   B CA  
460  C  C   . THR   B 25  ? 0.6574 0.5492 0.6543 0.1311  0.1531  0.1120  34  THR   B C   
461  O  O   . THR   B 25  ? 0.6666 0.5544 0.6567 0.1257  0.1455  0.0963  34  THR   B O   
462  C  CB  . THR   B 25  ? 0.6852 0.5652 0.7172 0.1014  0.1556  0.1237  34  THR   B CB  
463  O  OG1 . THR   B 25  ? 0.6965 0.5576 0.7421 0.0920  0.1605  0.1324  34  THR   B OG1 
464  C  CG2 . THR   B 25  ? 0.6743 0.5828 0.7187 0.1003  0.1562  0.1345  34  THR   B CG2 
465  N  N   . GLN   B 26  ? 0.6309 0.5400 0.6233 0.1439  0.1556  0.1208  35  GLN   B N   
466  C  CA  . GLN   B 26  ? 0.6196 0.5416 0.5987 0.1506  0.1478  0.1116  35  GLN   B CA  
467  C  C   . GLN   B 26  ? 0.6135 0.5518 0.6016 0.1380  0.1419  0.1099  35  GLN   B C   
468  O  O   . GLN   B 26  ? 0.6106 0.5627 0.6090 0.1381  0.1460  0.1228  35  GLN   B O   
469  C  CB  . GLN   B 26  ? 0.6028 0.5314 0.5680 0.1722  0.1512  0.1200  35  GLN   B CB  
470  C  CG  . GLN   B 26  ? 0.5851 0.5239 0.5365 0.1782  0.1417  0.1105  35  GLN   B CG  
471  C  CD  . GLN   B 26  ? 0.5561 0.4966 0.4905 0.2005  0.1427  0.1165  35  GLN   B CD  
472  O  OE1 . GLN   B 26  ? 0.5486 0.4786 0.4763 0.2129  0.1474  0.1204  35  GLN   B OE1 
473  N  NE2 . GLN   B 26  ? 0.5131 0.4649 0.4382 0.2071  0.1377  0.1170  35  GLN   B NE2 
474  N  N   . VAL   B 27  ? 0.6011 0.5383 0.5852 0.1280  0.1330  0.0949  36  VAL   B N   
475  C  CA  . VAL   B 27  ? 0.5839 0.5341 0.5735 0.1166  0.1261  0.0915  36  VAL   B CA  
476  C  C   . VAL   B 27  ? 0.5656 0.5287 0.5410 0.1260  0.1210  0.0887  36  VAL   B C   
477  O  O   . VAL   B 27  ? 0.5579 0.5347 0.5364 0.1224  0.1174  0.0911  36  VAL   B O   
478  C  CB  . VAL   B 27  ? 0.6049 0.5441 0.5965 0.1005  0.1196  0.0777  36  VAL   B CB  
479  C  CG1 . VAL   B 27  ? 0.6171 0.5432 0.6239 0.0895  0.1226  0.0818  36  VAL   B CG1 
480  C  CG2 . VAL   B 27  ? 0.6103 0.5381 0.5863 0.1049  0.1175  0.0644  36  VAL   B CG2 
481  N  N   . GLY   B 28  ? 0.5500 0.5081 0.5102 0.1387  0.1201  0.0844  37  GLY   B N   
482  C  CA  . GLY   B 28  ? 0.5378 0.5035 0.4835 0.1477  0.1141  0.0815  37  GLY   B CA  
483  C  C   . GLY   B 28  ? 0.5342 0.4925 0.4667 0.1611  0.1125  0.0773  37  GLY   B C   
484  O  O   . GLY   B 28  ? 0.5355 0.4854 0.4697 0.1669  0.1176  0.0794  37  GLY   B O   
485  N  N   . VAL   B 29  ? 0.5249 0.4860 0.4447 0.1660  0.1045  0.0713  38  VAL   B N   
486  C  CA  . VAL   B 29  ? 0.5229 0.4792 0.4307 0.1781  0.0994  0.0666  38  VAL   B CA  
487  C  C   . VAL   B 29  ? 0.5250 0.4819 0.4284 0.1696  0.0903  0.0550  38  VAL   B C   
488  O  O   . VAL   B 29  ? 0.5219 0.4827 0.4250 0.1597  0.0878  0.0529  38  VAL   B O   
489  C  CB  . VAL   B 29  ? 0.5243 0.4825 0.4180 0.1966  0.0983  0.0754  38  VAL   B CB  
490  C  CG1 . VAL   B 29  ? 0.5394 0.4918 0.4184 0.2088  0.0887  0.0691  38  VAL   B CG1 
491  C  CG2 . VAL   B 29  ? 0.5282 0.4859 0.4254 0.2067  0.1089  0.0886  38  VAL   B CG2 
492  N  N   . GLY   B 30  ? 0.5257 0.4792 0.4258 0.1743  0.0852  0.0484  39  GLY   B N   
493  C  CA  . GLY   B 30  ? 0.5278 0.4824 0.4255 0.1668  0.0772  0.0394  39  GLY   B CA  
494  C  C   . GLY   B 30  ? 0.5282 0.4809 0.4202 0.1763  0.0683  0.0356  39  GLY   B C   
495  O  O   . GLY   B 30  ? 0.5242 0.4743 0.4131 0.1902  0.0680  0.0385  39  GLY   B O   
496  N  N   . VAL   B 31  ? 0.5206 0.4740 0.4117 0.1685  0.0605  0.0290  40  VAL   B N   
497  C  CA  . VAL   B 31  ? 0.5239 0.4756 0.4126 0.1739  0.0494  0.0244  40  VAL   B CA  
498  C  C   . VAL   B 31  ? 0.5117 0.4704 0.4167 0.1629  0.0496  0.0178  40  VAL   B C   
499  O  O   . VAL   B 31  ? 0.5011 0.4624 0.4105 0.1493  0.0527  0.0154  40  VAL   B O   
500  C  CB  . VAL   B 31  ? 0.5488 0.4938 0.4222 0.1746  0.0386  0.0237  40  VAL   B CB  
501  C  CG1 . VAL   B 31  ? 0.5651 0.5067 0.4382 0.1768  0.0251  0.0180  40  VAL   B CG1 
502  C  CG2 . VAL   B 31  ? 0.5586 0.4982 0.4146 0.1889  0.0387  0.0308  40  VAL   B CG2 
503  N  N   . MET   B 32  ? 0.5070 0.4696 0.4206 0.1700  0.0467  0.0154  41  MET   B N   
504  C  CA  . MET   B 32  ? 0.5020 0.4747 0.4332 0.1612  0.0465  0.0101  41  MET   B CA  
505  C  C   . MET   B 32  ? 0.5203 0.4928 0.4515 0.1600  0.0316  0.0069  41  MET   B C   
506  O  O   . MET   B 32  ? 0.5310 0.4977 0.4534 0.1726  0.0210  0.0067  41  MET   B O   
507  C  CB  . MET   B 32  ? 0.5016 0.4805 0.4441 0.1701  0.0507  0.0093  41  MET   B CB  
508  C  CG  . MET   B 32  ? 0.5190 0.5115 0.4815 0.1617  0.0545  0.0050  41  MET   B CG  
509  S  SD  . MET   B 32  ? 0.6075 0.6014 0.5732 0.1478  0.0696  0.0043  41  MET   B SD  
510  C  CE  . MET   B 32  ? 0.5742 0.5609 0.5370 0.1580  0.0800  0.0061  41  MET   B CE  
511  N  N   . GLN   B 33  ? 0.5216 0.4984 0.4611 0.1454  0.0302  0.0047  42  GLN   B N   
512  C  CA  . GLN   B 33  ? 0.5368 0.5121 0.4792 0.1414  0.0155  0.0020  42  GLN   B CA  
513  C  C   . GLN   B 33  ? 0.5329 0.5202 0.4953 0.1251  0.0189  0.0009  42  GLN   B C   
514  O  O   . GLN   B 33  ? 0.5370 0.5247 0.4976 0.1154  0.0297  0.0026  42  GLN   B O   
515  C  CB  . GLN   B 33  ? 0.5807 0.5390 0.5003 0.1427  0.0064  0.0030  42  GLN   B CB  
516  C  CG  . GLN   B 33  ? 0.6509 0.6029 0.5711 0.1412  -0.0116 -0.0006 42  GLN   B CG  
517  C  CD  . GLN   B 33  ? 0.7679 0.6996 0.6619 0.1461  -0.0220 -0.0004 42  GLN   B CD  
518  O  OE1 . GLN   B 33  ? 0.8047 0.7281 0.6954 0.1350  -0.0278 -0.0009 42  GLN   B OE1 
519  N  NE2 . GLN   B 33  ? 0.8052 0.7278 0.6789 0.1639  -0.0239 0.0012  42  GLN   B NE2 
520  N  N   . GLU   B 34  ? 0.5192 0.5173 0.5012 0.1227  0.0102  -0.0014 43  GLU   B N   
521  C  CA  . GLU   B 34  ? 0.5159 0.5293 0.5214 0.1076  0.0147  -0.0006 43  GLU   B CA  
522  C  C   . GLU   B 34  ? 0.5158 0.5420 0.5302 0.1048  0.0345  0.0011  43  GLU   B C   
523  O  O   . GLU   B 34  ? 0.5189 0.5504 0.5393 0.0927  0.0433  0.0034  43  GLU   B O   
524  C  CB  . GLU   B 34  ? 0.5541 0.5571 0.5534 0.0938  0.0090  0.0011  43  GLU   B CB  
525  C  CG  . GLU   B 34  ? 0.6058 0.5952 0.5986 0.0955  -0.0122 -0.0015 43  GLU   B CG  
526  C  CD  . GLU   B 34  ? 0.7095 0.6795 0.6852 0.0863  -0.0187 -0.0001 43  GLU   B CD  
527  O  OE1 . GLU   B 34  ? 0.7313 0.7057 0.7192 0.0705  -0.0143 0.0031  43  GLU   B OE1 
528  O  OE2 . GLU   B 34  ? 0.7631 0.7130 0.7122 0.0960  -0.0275 -0.0016 43  GLU   B OE2 
529  N  N   . GLY   B 35  ? 0.5060 0.5346 0.5189 0.1168  0.0411  0.0001  44  GLY   B N   
530  C  CA  . GLY   B 35  ? 0.5024 0.5388 0.5203 0.1166  0.0579  0.0005  44  GLY   B CA  
531  C  C   . GLY   B 35  ? 0.5128 0.5359 0.5112 0.1126  0.0679  0.0014  44  GLY   B C   
532  O  O   . GLY   B 35  ? 0.5249 0.5513 0.5245 0.1112  0.0806  0.0009  44  GLY   B O   
533  N  N   . VAL   B 36  ? 0.5097 0.5176 0.4894 0.1116  0.0614  0.0024  45  VAL   B N   
534  C  CA  . VAL   B 36  ? 0.5041 0.5005 0.4660 0.1077  0.0677  0.0034  45  VAL   B CA  
535  C  C   . VAL   B 36  ? 0.5050 0.4905 0.4529 0.1179  0.0660  0.0049  45  VAL   B C   
536  O  O   . VAL   B 36  ? 0.4974 0.4783 0.4395 0.1261  0.0563  0.0061  45  VAL   B O   
537  C  CB  . VAL   B 36  ? 0.5171 0.5075 0.4704 0.0970  0.0633  0.0048  45  VAL   B CB  
538  C  CG1 . VAL   B 36  ? 0.5341 0.5130 0.4680 0.0950  0.0672  0.0057  45  VAL   B CG1 
539  C  CG2 . VAL   B 36  ? 0.5100 0.5112 0.4772 0.0861  0.0691  0.0054  45  VAL   B CG2 
540  N  N   . PHE   B 37  ? 0.4910 0.4722 0.4337 0.1177  0.0756  0.0050  46  PHE   B N   
541  C  CA  . PHE   B 37  ? 0.4895 0.4624 0.4225 0.1251  0.0757  0.0082  46  PHE   B CA  
542  C  C   . PHE   B 37  ? 0.4820 0.4485 0.4017 0.1189  0.0741  0.0101  46  PHE   B C   
543  O  O   . PHE   B 37  ? 0.4780 0.4436 0.3952 0.1095  0.0786  0.0081  46  PHE   B O   
544  C  CB  . PHE   B 37  ? 0.4846 0.4553 0.4218 0.1283  0.0854  0.0078  46  PHE   B CB  
545  C  CG  . PHE   B 37  ? 0.4976 0.4611 0.4288 0.1364  0.0857  0.0131  46  PHE   B CG  
546  C  CD1 . PHE   B 37  ? 0.4933 0.4567 0.4226 0.1488  0.0805  0.0166  46  PHE   B CD1 
547  C  CD2 . PHE   B 37  ? 0.5135 0.4707 0.4409 0.1315  0.0907  0.0151  46  PHE   B CD2 
548  C  CE1 . PHE   B 37  ? 0.5086 0.4661 0.4320 0.1572  0.0828  0.0232  46  PHE   B CE1 
549  C  CE2 . PHE   B 37  ? 0.5147 0.4676 0.4399 0.1380  0.0920  0.0219  46  PHE   B CE2 
550  C  CZ  . PHE   B 37  ? 0.5101 0.4634 0.4330 0.1511  0.0892  0.0265  46  PHE   B CZ  
551  N  N   . HIS   B 38  ? 0.4771 0.4394 0.3870 0.1254  0.0673  0.0139  47  HIS   B N   
552  C  CA  . HIS   B 38  ? 0.4767 0.4345 0.3738 0.1226  0.0645  0.0165  47  HIS   B CA  
553  C  C   . HIS   B 38  ? 0.4903 0.4475 0.3850 0.1290  0.0682  0.0220  47  HIS   B C   
554  O  O   . HIS   B 38  ? 0.4932 0.4499 0.3875 0.1407  0.0675  0.0259  47  HIS   B O   
555  C  CB  . HIS   B 38  ? 0.4818 0.4348 0.3682 0.1277  0.0534  0.0173  47  HIS   B CB  
556  C  CG  . HIS   B 38  ? 0.5061 0.4594 0.3976 0.1213  0.0478  0.0133  47  HIS   B CG  
557  N  ND1 . HIS   B 38  ? 0.5167 0.4760 0.4220 0.1238  0.0464  0.0109  47  HIS   B ND1 
558  C  CD2 . HIS   B 38  ? 0.5260 0.4753 0.4126 0.1119  0.0440  0.0120  47  HIS   B CD2 
559  C  CE1 . HIS   B 38  ? 0.5182 0.4787 0.4290 0.1151  0.0414  0.0086  47  HIS   B CE1 
560  N  NE2 . HIS   B 38  ? 0.5299 0.4833 0.4292 0.1074  0.0404  0.0096  47  HIS   B NE2 
561  N  N   . THR   B 39  ? 0.4927 0.4503 0.3858 0.1220  0.0717  0.0231  48  THR   B N   
562  C  CA  . THR   B 39  ? 0.4982 0.4579 0.3930 0.1267  0.0750  0.0299  48  THR   B CA  
563  C  C   . THR   B 39  ? 0.5023 0.4646 0.3920 0.1204  0.0732  0.0314  48  THR   B C   
564  O  O   . THR   B 39  ? 0.4986 0.4588 0.3797 0.1147  0.0690  0.0273  48  THR   B O   
565  C  CB  . THR   B 39  ? 0.5067 0.4651 0.4137 0.1261  0.0829  0.0306  48  THR   B CB  
566  O  OG1 . THR   B 39  ? 0.5148 0.4756 0.4253 0.1311  0.0862  0.0394  48  THR   B OG1 
567  C  CG2 . THR   B 39  ? 0.5097 0.4651 0.4212 0.1137  0.0864  0.0243  48  THR   B CG2 
568  N  N   . MET   B 40  ? 0.4971 0.4647 0.3926 0.1219  0.0763  0.0381  49  MET   B N   
569  C  CA  . MET   B 40  ? 0.4912 0.4645 0.3856 0.1163  0.0741  0.0397  49  MET   B CA  
570  C  C   . MET   B 40  ? 0.5013 0.4723 0.4040 0.1028  0.0761  0.0341  49  MET   B C   
571  O  O   . MET   B 40  ? 0.4984 0.4655 0.4112 0.1004  0.0810  0.0335  49  MET   B O   
572  C  CB  . MET   B 40  ? 0.4909 0.4738 0.3894 0.1254  0.0759  0.0507  49  MET   B CB  
573  C  CG  . MET   B 40  ? 0.5105 0.4917 0.3950 0.1412  0.0731  0.0548  49  MET   B CG  
574  S  SD  . MET   B 40  ? 0.6185 0.6108 0.4961 0.1522  0.0717  0.0648  49  MET   B SD  
575  C  CE  . MET   B 40  ? 0.5693 0.5555 0.4293 0.1476  0.0620  0.0570  49  MET   B CE  
576  N  N   . TRP   B 41  ? 0.4998 0.4708 0.3955 0.0952  0.0716  0.0295  50  TRP   B N   
577  C  CA  A TRP   B 41  ? 0.5125 0.4789 0.4112 0.0840  0.0716  0.0228  50  TRP   B CA  
578  C  CA  B TRP   B 41  ? 0.5058 0.4722 0.4044 0.0841  0.0716  0.0229  50  TRP   B CA  
579  C  C   . TRP   B 41  ? 0.5060 0.4761 0.4214 0.0799  0.0730  0.0270  50  TRP   B C   
580  O  O   . TRP   B 41  ? 0.4994 0.4605 0.4198 0.0736  0.0750  0.0220  50  TRP   B O   
581  C  CB  A TRP   B 41  ? 0.5218 0.4879 0.4079 0.0789  0.0656  0.0184  50  TRP   B CB  
582  C  CB  B TRP   B 41  ? 0.5052 0.4717 0.3911 0.0792  0.0655  0.0186  50  TRP   B CB  
583  C  CG  A TRP   B 41  ? 0.5446 0.5022 0.4277 0.0697  0.0650  0.0096  50  TRP   B CG  
584  C  CG  B TRP   B 41  ? 0.5137 0.4735 0.3986 0.0696  0.0640  0.0109  50  TRP   B CG  
585  C  CD1 A TRP   B 41  ? 0.5652 0.5127 0.4373 0.0675  0.0679  0.0022  50  TRP   B CD1 
586  C  CD1 B TRP   B 41  ? 0.5194 0.4822 0.4134 0.0634  0.0598  0.0107  50  TRP   B CD1 
587  C  CD2 A TRP   B 41  ? 0.5471 0.5047 0.4379 0.0623  0.0611  0.0075  50  TRP   B CD2 
588  C  CD2 B TRP   B 41  ? 0.5188 0.4668 0.3935 0.0660  0.0667  0.0022  50  TRP   B CD2 
589  N  NE1 A TRP   B 41  ? 0.5757 0.5152 0.4446 0.0610  0.0663  -0.0049 50  TRP   B NE1 
590  N  NE1 B TRP   B 41  ? 0.5278 0.4786 0.4150 0.0565  0.0582  0.0012  50  TRP   B NE1 
591  C  CE2 A TRP   B 41  ? 0.5673 0.5116 0.4475 0.0571  0.0610  -0.0025 50  TRP   B CE2 
592  C  CE2 B TRP   B 41  ? 0.5307 0.4725 0.4049 0.0590  0.0634  -0.0039 50  TRP   B CE2 
593  C  CE3 A TRP   B 41  ? 0.5483 0.5162 0.4550 0.0595  0.0574  0.0134  50  TRP   B CE3 
594  C  CE3 B TRP   B 41  ? 0.5300 0.4731 0.3969 0.0684  0.0716  -0.0006 50  TRP   B CE3 
595  C  CZ2 A TRP   B 41  ? 0.5795 0.5175 0.4614 0.0497  0.0554  -0.0083 50  TRP   B CZ2 
596  C  CZ2 B TRP   B 41  ? 0.5447 0.4737 0.4066 0.0564  0.0654  -0.0129 50  TRP   B CZ2 
597  C  CZ3 A TRP   B 41  ? 0.5610 0.5249 0.4738 0.0501  0.0518  0.0084  50  TRP   B CZ3 
598  C  CZ3 B TRP   B 41  ? 0.5445 0.4783 0.4025 0.0650  0.0750  -0.0081 50  TRP   B CZ3 
599  C  CH2 A TRP   B 41  ? 0.5725 0.5201 0.4715 0.0454  0.0498  -0.0031 50  TRP   B CH2 
600  C  CH2 B TRP   B 41  ? 0.5511 0.4771 0.4046 0.0601  0.0722  -0.0143 50  TRP   B CH2 
601  N  N   . HIS   B 42  ? 0.4956 0.4784 0.4195 0.0833  0.0720  0.0364  51  HIS   B N   
602  C  CA  . HIS   B 42  ? 0.4942 0.4828 0.4380 0.0778  0.0735  0.0424  51  HIS   B CA  
603  C  C   . HIS   B 42  ? 0.5113 0.4923 0.4653 0.0795  0.0811  0.0459  51  HIS   B C   
604  O  O   . HIS   B 42  ? 0.5147 0.4940 0.4844 0.0717  0.0821  0.0486  51  HIS   B O   
605  C  CB  . HIS   B 42  ? 0.4734 0.4810 0.4265 0.0825  0.0725  0.0538  51  HIS   B CB  
606  C  CG  . HIS   B 42  ? 0.4781 0.4918 0.4314 0.0967  0.0792  0.0646  51  HIS   B CG  
607  N  ND1 . HIS   B 42  ? 0.5016 0.5181 0.4379 0.1092  0.0774  0.0663  51  HIS   B ND1 
608  C  CD2 . HIS   B 42  ? 0.4767 0.4926 0.4432 0.1010  0.0872  0.0744  51  HIS   B CD2 
609  C  CE1 . HIS   B 42  ? 0.5034 0.5232 0.4415 0.1215  0.0838  0.0759  51  HIS   B CE1 
610  N  NE2 . HIS   B 42  ? 0.4892 0.5093 0.4452 0.1173  0.0905  0.0815  51  HIS   B NE2 
611  N  N   . VAL   B 43  ? 0.5194 0.4948 0.4648 0.0896  0.0855  0.0459  52  VAL   B N   
612  C  CA  . VAL   B 43  ? 0.5288 0.4959 0.4806 0.0936  0.0925  0.0488  52  VAL   B CA  
613  C  C   . VAL   B 43  ? 0.5470 0.4985 0.4987 0.0851  0.0930  0.0387  52  VAL   B C   
614  O  O   . VAL   B 43  ? 0.5601 0.5039 0.5227 0.0803  0.0958  0.0410  52  VAL   B O   
615  C  CB  . VAL   B 43  ? 0.5343 0.5011 0.4760 0.1080  0.0949  0.0509  52  VAL   B CB  
616  C  CG1 . VAL   B 43  ? 0.5423 0.4990 0.4879 0.1130  0.1011  0.0516  52  VAL   B CG1 
617  C  CG2 . VAL   B 43  ? 0.5313 0.5098 0.4710 0.1193  0.0953  0.0617  52  VAL   B CG2 
618  N  N   . THR   B 44  ? 0.5470 0.4930 0.4858 0.0835  0.0904  0.0281  53  THR   B N   
619  C  CA  . THR   B 44  ? 0.5530 0.4847 0.4880 0.0788  0.0919  0.0185  53  THR   B CA  
620  C  C   . THR   B 44  ? 0.5602 0.4856 0.4897 0.0681  0.0863  0.0101  53  THR   B C   
621  O  O   . THR   B 44  ? 0.5608 0.4715 0.4867 0.0647  0.0870  0.0027  53  THR   B O   
622  C  CB  . THR   B 44  ? 0.5628 0.4935 0.4881 0.0856  0.0946  0.0131  53  THR   B CB  
623  O  OG1 . THR   B 44  ? 0.5688 0.5047 0.4835 0.0828  0.0905  0.0090  53  THR   B OG1 
624  C  CG2 . THR   B 44  ? 0.5548 0.4914 0.4835 0.0972  0.0975  0.0198  53  THR   B CG2 
625  N  N   . LYS   B 45  ? 0.5654 0.5004 0.4918 0.0644  0.0801  0.0108  54  LYS   B N   
626  C  CA  . LYS   B 45  ? 0.5883 0.5186 0.5057 0.0561  0.0732  0.0025  54  LYS   B CA  
627  C  C   . LYS   B 45  ? 0.5991 0.5189 0.4985 0.0575  0.0754  -0.0076 54  LYS   B C   
628  O  O   . LYS   B 45  ? 0.6141 0.5233 0.5033 0.0525  0.0714  -0.0160 54  LYS   B O   
629  C  CB  . LYS   B 45  ? 0.6155 0.5383 0.5431 0.0464  0.0679  0.0005  54  LYS   B CB  
630  C  CG  . LYS   B 45  ? 0.6919 0.6259 0.6416 0.0444  0.0682  0.0124  54  LYS   B CG  
631  C  CD  . LYS   B 45  ? 0.7644 0.7108 0.7232 0.0367  0.0590  0.0146  54  LYS   B CD  
632  C  CE  . LYS   B 45  ? 0.8155 0.7712 0.8007 0.0322  0.0604  0.0265  54  LYS   B CE  
633  N  NZ  . LYS   B 45  ? 0.8487 0.8132 0.8394 0.0433  0.0711  0.0386  54  LYS   B NZ  
634  N  N   . GLY   B 46  ? 0.5933 0.5163 0.4891 0.0647  0.0814  -0.0063 55  GLY   B N   
635  C  CA  . GLY   B 46  ? 0.6054 0.5227 0.4883 0.0666  0.0856  -0.0133 55  GLY   B CA  
636  C  C   . GLY   B 46  ? 0.6187 0.5249 0.5024 0.0696  0.0918  -0.0181 55  GLY   B C   
637  O  O   . GLY   B 46  ? 0.6281 0.5319 0.5031 0.0728  0.0971  -0.0227 55  GLY   B O   
638  N  N   . ALA   B 47  ? 0.6191 0.5182 0.5131 0.0693  0.0921  -0.0162 56  ALA   B N   
639  C  CA  . ALA   B 47  ? 0.6303 0.5155 0.5230 0.0734  0.0975  -0.0209 56  ALA   B CA  
640  C  C   . ALA   B 47  ? 0.6241 0.5168 0.5207 0.0831  0.1051  -0.0186 56  ALA   B C   
641  O  O   . ALA   B 47  ? 0.6168 0.5230 0.5214 0.0864  0.1050  -0.0117 56  ALA   B O   
642  C  CB  . ALA   B 47  ? 0.6322 0.5072 0.5360 0.0704  0.0958  -0.0175 56  ALA   B CB  
643  N  N   . ALA   B 48  ? 0.6280 0.5113 0.5190 0.0887  0.1110  -0.0244 57  ALA   B N   
644  C  CA  . ALA   B 48  ? 0.6332 0.5248 0.5302 0.0986  0.1179  -0.0227 57  ALA   B CA  
645  C  C   . ALA   B 48  ? 0.6432 0.5353 0.5526 0.1041  0.1183  -0.0157 57  ALA   B C   
646  O  O   . ALA   B 48  ? 0.6557 0.5371 0.5680 0.1008  0.1160  -0.0129 57  ALA   B O   
647  C  CB  . ALA   B 48  ? 0.6406 0.5214 0.5281 0.1048  0.1244  -0.0302 57  ALA   B CB  
648  N  N   . LEU   B 49  ? 0.6328 0.5377 0.5498 0.1124  0.1210  -0.0124 58  LEU   B N   
649  C  CA  . LEU   B 49  ? 0.6372 0.5427 0.5628 0.1204  0.1214  -0.0057 58  LEU   B CA  
650  C  C   . LEU   B 49  ? 0.6548 0.5600 0.5830 0.1320  0.1270  -0.0080 58  LEU   B C   
651  O  O   . LEU   B 49  ? 0.6585 0.5710 0.5860 0.1341  0.1303  -0.0130 58  LEU   B O   
652  C  CB  . LEU   B 49  ? 0.6263 0.5473 0.5572 0.1219  0.1165  0.0006  58  LEU   B CB  
653  C  CG  . LEU   B 49  ? 0.6328 0.5569 0.5613 0.1136  0.1111  0.0041  58  LEU   B CG  
654  C  CD1 . LEU   B 49  ? 0.6332 0.5694 0.5633 0.1185  0.1064  0.0093  58  LEU   B CD1 
655  C  CD2 . LEU   B 49  ? 0.6347 0.5492 0.5658 0.1105  0.1112  0.0091  58  LEU   B CD2 
656  N  N   . ARG   B 50  ? 0.6645 0.5624 0.5960 0.1402  0.1286  -0.0034 59  ARG   B N   
657  C  CA  . ARG   B 50  ? 0.6811 0.5784 0.6147 0.1532  0.1332  -0.0048 59  ARG   B CA  
658  C  C   . ARG   B 50  ? 0.6883 0.5981 0.6296 0.1632  0.1303  0.0015  59  ARG   B C   
659  O  O   . ARG   B 50  ? 0.6755 0.5843 0.6169 0.1626  0.1271  0.0083  59  ARG   B O   
660  C  CB  . ARG   B 50  ? 0.7208 0.5931 0.6473 0.1559  0.1374  -0.0059 59  ARG   B CB  
661  C  CG  . ARG   B 50  ? 0.8020 0.6681 0.7297 0.1708  0.1411  -0.0027 59  ARG   B CG  
662  C  CD  . ARG   B 50  ? 0.8963 0.7342 0.8143 0.1731  0.1453  -0.0054 59  ARG   B CD  
663  N  NE  . ARG   B 50  ? 0.9613 0.7809 0.8785 0.1633  0.1435  0.0001  59  ARG   B NE  
664  C  CZ  . ARG   B 50  ? 1.0071 0.8203 0.9281 0.1673  0.1448  0.0101  59  ARG   B CZ  
665  N  NH1 . ARG   B 50  ? 0.9961 0.8187 0.9192 0.1819  0.1468  0.0150  59  ARG   B NH1 
666  N  NH2 . ARG   B 50  ? 1.0215 0.8199 0.9448 0.1569  0.1441  0.0160  59  ARG   B NH2 
667  N  N   . SER   B 51  ? 0.7056 0.6279 0.6531 0.1732  0.1310  -0.0006 60  SER   B N   
668  C  CA  . SER   B 51  ? 0.7308 0.6638 0.6844 0.1843  0.1262  0.0038  60  SER   B CA  
669  C  C   . SER   B 51  ? 0.7681 0.7006 0.7244 0.1989  0.1304  0.0018  60  SER   B C   
670  O  O   . SER   B 51  ? 0.7602 0.7091 0.7258 0.2022  0.1309  -0.0025 60  SER   B O   
671  C  CB  . SER   B 51  ? 0.7441 0.6981 0.7060 0.1801  0.1191  0.0025  60  SER   B CB  
672  O  OG  . SER   B 51  ? 0.7917 0.7535 0.7574 0.1912  0.1122  0.0057  60  SER   B OG  
673  N  N   . GLY   B 52  ? 0.7983 0.7118 0.7470 0.2072  0.1343  0.0054  61  GLY   B N   
674  C  CA  . GLY   B 52  ? 0.8233 0.7318 0.7712 0.2220  0.1388  0.0036  61  GLY   B CA  
675  C  C   . GLY   B 52  ? 0.8546 0.7553 0.7984 0.2181  0.1455  -0.0036 61  GLY   B C   
676  O  O   . GLY   B 52  ? 0.8722 0.7531 0.8065 0.2084  0.1479  -0.0047 61  GLY   B O   
677  N  N   . GLU   B 53  ? 0.8582 0.7758 0.8096 0.2250  0.1479  -0.0085 62  GLU   B N   
678  C  CA  . GLU   B 53  ? 0.8783 0.7909 0.8239 0.2231  0.1550  -0.0152 62  GLU   B CA  
679  C  C   . GLU   B 53  ? 0.8675 0.7958 0.8176 0.2086  0.1544  -0.0179 62  GLU   B C   
680  O  O   . GLU   B 53  ? 0.8804 0.7999 0.8206 0.2046  0.1597  -0.0231 62  GLU   B O   
681  C  CB  . GLU   B 53  ? 0.9283 0.8513 0.8787 0.2400  0.1605  -0.0180 62  GLU   B CB  
682  C  CG  . GLU   B 53  ? 1.0400 0.9338 0.9729 0.2504  0.1671  -0.0212 62  GLU   B CG  
683  C  CD  . GLU   B 53  ? 1.1604 1.0662 1.0964 0.2677  0.1739  -0.0248 62  GLU   B CD  
684  O  OE1 . GLU   B 53  ? 1.1723 1.1075 1.1226 0.2666  0.1762  -0.0261 62  GLU   B OE1 
685  O  OE2 . GLU   B 53  ? 1.2108 1.0967 1.1355 0.2825  0.1774  -0.0255 62  GLU   B OE2 
686  N  N   . GLY   B 54  ? 0.8397 0.7888 0.8025 0.2022  0.1476  -0.0145 63  GLY   B N   
687  C  CA  . GLY   B 54  ? 0.8231 0.7869 0.7908 0.1890  0.1464  -0.0156 63  GLY   B CA  
688  C  C   . GLY   B 54  ? 0.8139 0.7610 0.7680 0.1752  0.1450  -0.0164 63  GLY   B C   
689  O  O   . GLY   B 54  ? 0.8273 0.7568 0.7738 0.1730  0.1421  -0.0140 63  GLY   B O   
690  N  N   . ARG   B 55  ? 0.7796 0.7332 0.7314 0.1659  0.1473  -0.0191 64  ARG   B N   
691  C  CA  . ARG   B 55  ? 0.7629 0.7026 0.7017 0.1535  0.1450  -0.0206 64  ARG   B CA  
692  C  C   . ARG   B 55  ? 0.7221 0.6773 0.6661 0.1428  0.1402  -0.0180 64  ARG   B C   
693  O  O   . ARG   B 55  ? 0.7164 0.6886 0.6681 0.1419  0.1434  -0.0180 64  ARG   B O   
694  C  CB  . ARG   B 55  ? 0.7894 0.7147 0.7128 0.1538  0.1518  -0.0273 64  ARG   B CB  
695  C  CG  . ARG   B 55  ? 0.8385 0.7482 0.7471 0.1419  0.1481  -0.0301 64  ARG   B CG  
696  C  CD  . ARG   B 55  ? 0.8943 0.7935 0.7860 0.1440  0.1543  -0.0374 64  ARG   B CD  
697  N  NE  . ARG   B 55  ? 0.9469 0.8329 0.8239 0.1332  0.1491  -0.0408 64  ARG   B NE  
698  C  CZ  . ARG   B 55  ? 1.0016 0.8619 0.8615 0.1321  0.1466  -0.0474 64  ARG   B CZ  
699  N  NH1 . ARG   B 55  ? 1.0191 0.8614 0.8727 0.1412  0.1494  -0.0513 64  ARG   B NH1 
700  N  NH2 . ARG   B 55  ? 1.0027 0.8540 0.8510 0.1222  0.1402  -0.0506 64  ARG   B NH2 
701  N  N   . LEU   B 56  ? 0.6885 0.6376 0.6286 0.1351  0.1330  -0.0151 65  LEU   B N   
702  C  CA  . LEU   B 56  ? 0.6616 0.6201 0.6023 0.1256  0.1277  -0.0129 65  LEU   B CA  
703  C  C   . LEU   B 56  ? 0.6503 0.5974 0.5760 0.1163  0.1282  -0.0160 65  LEU   B C   
704  O  O   . LEU   B 56  ? 0.6596 0.5918 0.5776 0.1137  0.1259  -0.0169 65  LEU   B O   
705  C  CB  . LEU   B 56  ? 0.6596 0.6192 0.6032 0.1257  0.1190  -0.0074 65  LEU   B CB  
706  C  CG  . LEU   B 56  ? 0.6817 0.6468 0.6348 0.1367  0.1162  -0.0042 65  LEU   B CG  
707  C  CD1 . LEU   B 56  ? 0.6813 0.6485 0.6333 0.1369  0.1072  0.0007  65  LEU   B CD1 
708  C  CD2 . LEU   B 56  ? 0.6926 0.6745 0.6592 0.1416  0.1174  -0.0058 65  LEU   B CD2 
709  N  N   . ASP   B 57  ? 0.6290 0.5831 0.5511 0.1111  0.1309  -0.0173 66  ASP   B N   
710  C  CA  . ASP   B 57  ? 0.6228 0.5661 0.5282 0.1037  0.1306  -0.0206 66  ASP   B CA  
711  C  C   . ASP   B 57  ? 0.5879 0.5360 0.4913 0.0954  0.1234  -0.0168 66  ASP   B C   
712  O  O   . ASP   B 57  ? 0.5730 0.5334 0.4862 0.0947  0.1210  -0.0125 66  ASP   B O   
713  C  CB  . ASP   B 57  ? 0.6717 0.6163 0.5692 0.1056  0.1399  -0.0243 66  ASP   B CB  
714  C  CG  . ASP   B 57  ? 0.7795 0.7166 0.6747 0.1157  0.1470  -0.0288 66  ASP   B CG  
715  O  OD1 . ASP   B 57  ? 0.8071 0.7257 0.6942 0.1170  0.1440  -0.0326 66  ASP   B OD1 
716  O  OD2 . ASP   B 57  ? 0.8119 0.7616 0.7140 0.1224  0.1556  -0.0282 66  ASP   B OD2 
717  N  N   . PRO   B 58  ? 0.5728 0.5103 0.4633 0.0896  0.1188  -0.0184 67  PRO   B N   
718  C  CA  . PRO   B 58  ? 0.5600 0.5011 0.4463 0.0835  0.1121  -0.0148 67  PRO   B CA  
719  C  C   . PRO   B 58  ? 0.5597 0.5069 0.4412 0.0802  0.1160  -0.0140 67  PRO   B C   
720  O  O   . PRO   B 58  ? 0.5696 0.5153 0.4449 0.0815  0.1240  -0.0171 67  PRO   B O   
721  C  CB  . PRO   B 58  ? 0.5730 0.5027 0.4477 0.0792  0.1071  -0.0175 67  PRO   B CB  
722  C  CG  . PRO   B 58  ? 0.5865 0.5046 0.4538 0.0809  0.1119  -0.0243 67  PRO   B CG  
723  C  CD  . PRO   B 58  ? 0.5698 0.4910 0.4487 0.0884  0.1184  -0.0241 67  PRO   B CD  
724  N  N   . TYR   B 59  ? 0.5393 0.4926 0.4235 0.0769  0.1109  -0.0092 68  TYR   B N   
725  C  CA  . TYR   B 59  ? 0.5204 0.4786 0.4025 0.0725  0.1143  -0.0066 68  TYR   B CA  
726  C  C   . TYR   B 59  ? 0.5209 0.4715 0.3868 0.0673  0.1083  -0.0049 68  TYR   B C   
727  O  O   . TYR   B 59  ? 0.5245 0.4721 0.3789 0.0639  0.1127  -0.0044 68  TYR   B O   
728  C  CB  . TYR   B 59  ? 0.4972 0.4680 0.3984 0.0728  0.1127  -0.0024 68  TYR   B CB  
729  C  CG  . TYR   B 59  ? 0.5014 0.4783 0.4054 0.0663  0.1159  0.0019  68  TYR   B CG  
730  C  CD1 . TYR   B 59  ? 0.5067 0.4773 0.4018 0.0603  0.1090  0.0054  68  TYR   B CD1 
731  C  CD2 . TYR   B 59  ? 0.4825 0.4721 0.3997 0.0665  0.1260  0.0034  68  TYR   B CD2 
732  C  CE1 . TYR   B 59  ? 0.5045 0.4783 0.4023 0.0531  0.1122  0.0103  68  TYR   B CE1 
733  C  CE2 . TYR   B 59  ? 0.4848 0.4815 0.4080 0.0593  0.1299  0.0092  68  TYR   B CE2 
734  C  CZ  . TYR   B 59  ? 0.5106 0.4984 0.4244 0.0519  0.1228  0.0128  68  TYR   B CZ  
735  O  OH  . TYR   B 59  ? 0.5277 0.5201 0.4471 0.0437  0.1271  0.0195  68  TYR   B OH  
736  N  N   . TRP   B 60  ? 0.5149 0.4629 0.3795 0.0679  0.0989  -0.0032 69  TRP   B N   
737  C  CA  . TRP   B 60  ? 0.5160 0.4575 0.3655 0.0651  0.0923  -0.0014 69  TRP   B CA  
738  C  C   . TRP   B 60  ? 0.5287 0.4689 0.3778 0.0685  0.0855  -0.0015 69  TRP   B C   
739  O  O   . TRP   B 60  ? 0.5323 0.4767 0.3939 0.0729  0.0845  -0.0003 69  TRP   B O   
740  C  CB  . TRP   B 60  ? 0.5017 0.4438 0.3523 0.0630  0.0875  0.0036  69  TRP   B CB  
741  C  CG  . TRP   B 60  ? 0.5171 0.4509 0.3514 0.0630  0.0794  0.0058  69  TRP   B CG  
742  C  CD1 . TRP   B 60  ? 0.5400 0.4660 0.3562 0.0597  0.0797  0.0062  69  TRP   B CD1 
743  C  CD2 . TRP   B 60  ? 0.5175 0.4505 0.3503 0.0686  0.0705  0.0078  69  TRP   B CD2 
744  N  NE1 . TRP   B 60  ? 0.5454 0.4662 0.3498 0.0629  0.0708  0.0080  69  TRP   B NE1 
745  C  CE2 . TRP   B 60  ? 0.5315 0.4570 0.3460 0.0685  0.0655  0.0092  69  TRP   B CE2 
746  C  CE3 . TRP   B 60  ? 0.5068 0.4448 0.3505 0.0753  0.0670  0.0090  69  TRP   B CE3 
747  C  CZ2 . TRP   B 60  ? 0.5365 0.4610 0.3449 0.0751  0.0575  0.0119  69  TRP   B CZ2 
748  C  CZ3 . TRP   B 60  ? 0.5173 0.4534 0.3538 0.0818  0.0597  0.0121  69  TRP   B CZ3 
749  C  CH2 . TRP   B 60  ? 0.5282 0.4582 0.3477 0.0818  0.0551  0.0135  69  TRP   B CH2 
750  N  N   . GLY   B 61  ? 0.5319 0.4672 0.3674 0.0669  0.0810  -0.0019 70  GLY   B N   
751  C  CA  . GLY   B 61  ? 0.5349 0.4724 0.3726 0.0694  0.0748  -0.0005 70  GLY   B CA  
752  C  C   . GLY   B 61  ? 0.5428 0.4774 0.3654 0.0682  0.0688  -0.0003 70  GLY   B C   
753  O  O   . GLY   B 61  ? 0.5441 0.4723 0.3521 0.0651  0.0701  -0.0030 70  GLY   B O   
754  N  N   . ASP   B 62  ? 0.5425 0.4826 0.3679 0.0717  0.0626  0.0036  71  ASP   B N   
755  C  CA  . ASP   B 62  ? 0.5446 0.4849 0.3575 0.0722  0.0559  0.0044  71  ASP   B CA  
756  C  C   . ASP   B 62  ? 0.5376 0.4891 0.3630 0.0752  0.0518  0.0083  71  ASP   B C   
757  O  O   . ASP   B 62  ? 0.5280 0.4853 0.3616 0.0813  0.0521  0.0141  71  ASP   B O   
758  C  CB  . ASP   B 62  ? 0.5828 0.5179 0.3815 0.0760  0.0527  0.0082  71  ASP   B CB  
759  C  CG  . ASP   B 62  ? 0.6785 0.6114 0.4602 0.0778  0.0464  0.0088  71  ASP   B CG  
760  O  OD1 . ASP   B 62  ? 0.6923 0.6335 0.4766 0.0834  0.0411  0.0126  71  ASP   B OD1 
761  O  OD2 . ASP   B 62  ? 0.7264 0.6500 0.4920 0.0745  0.0472  0.0061  71  ASP   B OD2 
762  N  N   . VAL   B 63  ? 0.5378 0.4926 0.3656 0.0710  0.0480  0.0055  72  VAL   B N   
763  C  CA  . VAL   B 63  ? 0.5338 0.5019 0.3781 0.0718  0.0444  0.0104  72  VAL   B CA  
764  C  C   . VAL   B 63  ? 0.5418 0.5198 0.3822 0.0805  0.0402  0.0180  72  VAL   B C   
765  O  O   . VAL   B 63  ? 0.5376 0.5272 0.3920 0.0857  0.0417  0.0255  72  VAL   B O   
766  C  CB  . VAL   B 63  ? 0.5337 0.5020 0.3812 0.0639  0.0388  0.0045  72  VAL   B CB  
767  C  CG1 . VAL   B 63  ? 0.5227 0.5081 0.3868 0.0637  0.0326  0.0103  72  VAL   B CG1 
768  C  CG2 . VAL   B 63  ? 0.5387 0.4974 0.3937 0.0576  0.0429  -0.0016 72  VAL   B CG2 
769  N  N   . LYS   B 64  ? 0.5534 0.5258 0.3732 0.0833  0.0358  0.0166  73  LYS   B N   
770  C  CA  . LYS   B 64  ? 0.5554 0.5347 0.3680 0.0935  0.0315  0.0234  73  LYS   B CA  
771  C  C   . LYS   B 64  ? 0.5543 0.5308 0.3655 0.1024  0.0347  0.0288  73  LYS   B C   
772  O  O   . LYS   B 64  ? 0.5468 0.5343 0.3632 0.1119  0.0341  0.0361  73  LYS   B O   
773  C  CB  . LYS   B 64  ? 0.5824 0.5531 0.3707 0.0954  0.0257  0.0208  73  LYS   B CB  
774  C  CG  . LYS   B 64  ? 0.6167 0.5953 0.3975 0.1074  0.0205  0.0276  73  LYS   B CG  
775  C  CD  . LYS   B 64  ? 0.6809 0.6502 0.4371 0.1101  0.0145  0.0253  73  LYS   B CD  
776  C  CE  . LYS   B 64  ? 0.7302 0.7060 0.4769 0.1238  0.0095  0.0319  73  LYS   B CE  
777  N  NZ  . LYS   B 64  ? 0.7626 0.7334 0.4886 0.1264  0.0025  0.0296  73  LYS   B NZ  
778  N  N   . GLN   B 65  ? 0.5598 0.5224 0.3642 0.1002  0.0379  0.0255  74  GLN   B N   
779  C  CA  . GLN   B 65  ? 0.5576 0.5165 0.3614 0.1085  0.0389  0.0294  74  GLN   B CA  
780  C  C   . GLN   B 65  ? 0.5355 0.5044 0.3601 0.1104  0.0443  0.0327  74  GLN   B C   
781  O  O   . GLN   B 65  ? 0.5362 0.5050 0.3603 0.1204  0.0446  0.0372  74  GLN   B O   
782  C  CB  . GLN   B 65  ? 0.5938 0.5372 0.3884 0.1044  0.0394  0.0252  74  GLN   B CB  
783  C  CG  . GLN   B 65  ? 0.6699 0.6005 0.4437 0.1018  0.0355  0.0233  74  GLN   B CG  
784  C  CD  . GLN   B 65  ? 0.7459 0.6638 0.5164 0.0957  0.0372  0.0209  74  GLN   B CD  
785  O  OE1 . GLN   B 65  ? 0.7690 0.6840 0.5449 0.0985  0.0360  0.0217  74  GLN   B OE1 
786  N  NE2 . GLN   B 65  ? 0.7595 0.6702 0.5216 0.0875  0.0399  0.0182  74  GLN   B NE2 
787  N  N   . ASP   B 66  ? 0.5130 0.4879 0.3534 0.1017  0.0481  0.0304  75  ASP   B N   
788  C  CA  . ASP   B 66  ? 0.4981 0.4794 0.3580 0.1012  0.0538  0.0333  75  ASP   B CA  
789  C  C   . ASP   B 66  ? 0.4912 0.4640 0.3514 0.1038  0.0575  0.0315  75  ASP   B C   
790  O  O   . ASP   B 66  ? 0.4764 0.4526 0.3445 0.1112  0.0607  0.0367  75  ASP   B O   
791  C  CB  . ASP   B 66  ? 0.4930 0.4893 0.3643 0.1094  0.0549  0.0434  75  ASP   B CB  
792  C  CG  . ASP   B 66  ? 0.5256 0.5270 0.4180 0.1063  0.0614  0.0470  75  ASP   B CG  
793  O  OD1 . ASP   B 66  ? 0.5385 0.5349 0.4389 0.0950  0.0624  0.0410  75  ASP   B OD1 
794  O  OD2 . ASP   B 66  ? 0.5539 0.5619 0.4525 0.1159  0.0656  0.0558  75  ASP   B OD2 
795  N  N   . LEU   B 67  ? 0.4902 0.4531 0.3427 0.0979  0.0575  0.0247  76  LEU   B N   
796  C  CA  . LEU   B 67  ? 0.4918 0.4494 0.3473 0.0997  0.0601  0.0227  76  LEU   B CA  
797  C  C   . LEU   B 67  ? 0.4960 0.4499 0.3568 0.0908  0.0652  0.0162  76  LEU   B C   
798  O  O   . LEU   B 67  ? 0.5097 0.4607 0.3643 0.0837  0.0655  0.0121  76  LEU   B O   
799  C  CB  . LEU   B 67  ? 0.4939 0.4439 0.3355 0.1032  0.0544  0.0226  76  LEU   B CB  
800  C  CG  . LEU   B 67  ? 0.5074 0.4569 0.3398 0.1155  0.0488  0.0281  76  LEU   B CG  
801  C  CD1 . LEU   B 67  ? 0.5245 0.4620 0.3423 0.1169  0.0419  0.0264  76  LEU   B CD1 
802  C  CD2 . LEU   B 67  ? 0.4950 0.4494 0.3368 0.1255  0.0514  0.0325  76  LEU   B CD2 
803  N  N   . VAL   B 68  ? 0.4887 0.4423 0.3589 0.0929  0.0691  0.0151  77  VAL   B N   
804  C  CA  . VAL   B 68  ? 0.4850 0.4362 0.3599 0.0869  0.0750  0.0093  77  VAL   B CA  
805  C  C   . VAL   B 68  ? 0.4823 0.4353 0.3652 0.0910  0.0764  0.0091  77  VAL   B C   
806  O  O   . VAL   B 68  ? 0.4803 0.4353 0.3676 0.0991  0.0740  0.0126  77  VAL   B O   
807  C  CB  . VAL   B 68  ? 0.4926 0.4422 0.3744 0.0839  0.0795  0.0070  77  VAL   B CB  
808  C  CG1 . VAL   B 68  ? 0.5023 0.4547 0.3958 0.0901  0.0810  0.0121  77  VAL   B CG1 
809  C  CG2 . VAL   B 68  ? 0.4934 0.4383 0.3755 0.0801  0.0857  0.0005  77  VAL   B CG2 
810  N  N   . SER   B 69  ? 0.4782 0.4316 0.3626 0.0862  0.0798  0.0056  78  SER   B N   
811  C  CA  . SER   B 69  ? 0.4750 0.4335 0.3708 0.0888  0.0808  0.0051  78  SER   B CA  
812  C  C   . SER   B 69  ? 0.4801 0.4416 0.3841 0.0875  0.0901  0.0013  78  SER   B C   
813  O  O   . SER   B 69  ? 0.4779 0.4355 0.3746 0.0827  0.0952  -0.0017 78  SER   B O   
814  C  CB  . SER   B 69  ? 0.4862 0.4451 0.3802 0.0848  0.0759  0.0062  78  SER   B CB  
815  O  OG  . SER   B 69  ? 0.5242 0.4829 0.4148 0.0765  0.0816  0.0049  78  SER   B OG  
816  N  N   . TYR   B 70  ? 0.4777 0.4451 0.3947 0.0934  0.0918  0.0012  79  TYR   B N   
817  C  CA  . TYR   B 70  ? 0.4854 0.4558 0.4100 0.0954  0.1006  -0.0021 79  TYR   B CA  
818  C  C   . TYR   B 70  ? 0.4807 0.4641 0.4199 0.0962  0.1018  -0.0018 79  TYR   B C   
819  O  O   . TYR   B 70  ? 0.4789 0.4672 0.4255 0.0991  0.0941  0.0004  79  TYR   B O   
820  C  CB  . TYR   B 70  ? 0.4848 0.4509 0.4131 0.1037  0.1016  -0.0017 79  TYR   B CB  
821  C  CG  . TYR   B 70  ? 0.5024 0.4574 0.4218 0.1012  0.1022  -0.0019 79  TYR   B CG  
822  C  CD1 . TYR   B 70  ? 0.5185 0.4715 0.4329 0.1003  0.0961  0.0023  79  TYR   B CD1 
823  C  CD2 . TYR   B 70  ? 0.5219 0.4684 0.4384 0.1002  0.1081  -0.0062 79  TYR   B CD2 
824  C  CE1 . TYR   B 70  ? 0.5310 0.4773 0.4416 0.0967  0.0961  0.0030  79  TYR   B CE1 
825  C  CE2 . TYR   B 70  ? 0.5417 0.4778 0.4521 0.0960  0.1067  -0.0067 79  TYR   B CE2 
826  C  CZ  . TYR   B 70  ? 0.5551 0.4928 0.4649 0.0937  0.1007  -0.0017 79  TYR   B CZ  
827  O  OH  . TYR   B 70  ? 0.5795 0.5099 0.4877 0.0886  0.0989  -0.0017 79  TYR   B OH  
828  N  N   . CYS   B 71  ? 0.4759 0.4651 0.4191 0.0942  0.1109  -0.0037 80  CYS   B N   
829  C  CA  . CYS   B 71  ? 0.4827 0.4886 0.4440 0.0945  0.1140  -0.0023 80  CYS   B CA  
830  C  C   . CYS   B 71  ? 0.4811 0.4929 0.4464 0.0846  0.1107  0.0015  80  CYS   B C   
831  O  O   . CYS   B 71  ? 0.4884 0.5149 0.4692 0.0819  0.1157  0.0038  80  CYS   B O   
832  C  CB  . CYS   B 71  ? 0.5130 0.5271 0.4898 0.1034  0.1090  -0.0020 80  CYS   B CB  
833  S  SG  . CYS   B 71  ? 0.6135 0.6175 0.5849 0.1154  0.1129  -0.0048 80  CYS   B SG  
834  N  N   . GLY   B 72  ? 0.4691 0.4699 0.4212 0.0797  0.1027  0.0028  81  GLY   B N   
835  C  CA  . GLY   B 72  ? 0.4627 0.4643 0.4153 0.0703  0.0990  0.0065  81  GLY   B CA  
836  C  C   . GLY   B 72  ? 0.4700 0.4560 0.4027 0.0676  0.0910  0.0072  81  GLY   B C   
837  O  O   . GLY   B 72  ? 0.4745 0.4520 0.3951 0.0727  0.0887  0.0052  81  GLY   B O   
838  N  N   . PRO   B 73  ? 0.4698 0.4523 0.3997 0.0594  0.0872  0.0107  82  PRO   B N   
839  C  CA  . PRO   B 73  ? 0.4916 0.4584 0.4010 0.0581  0.0788  0.0116  82  PRO   B CA  
840  C  C   . PRO   B 73  ? 0.5199 0.4809 0.4262 0.0657  0.0661  0.0108  82  PRO   B C   
841  O  O   . PRO   B 73  ? 0.5238 0.4916 0.4445 0.0699  0.0613  0.0099  82  PRO   B O   
842  C  CB  . PRO   B 73  ? 0.4947 0.4585 0.4051 0.0479  0.0772  0.0161  82  PRO   B CB  
843  C  CG  . PRO   B 73  ? 0.4781 0.4580 0.4156 0.0444  0.0790  0.0178  82  PRO   B CG  
844  C  CD  . PRO   B 73  ? 0.4489 0.4418 0.3957 0.0510  0.0899  0.0148  82  PRO   B CD  
845  N  N   . TRP   B 74  ? 0.5346 0.4831 0.4209 0.0686  0.0603  0.0113  83  TRP   B N   
846  C  CA  . TRP   B 74  ? 0.5456 0.4875 0.4245 0.0780  0.0495  0.0115  83  TRP   B CA  
847  C  C   . TRP   B 74  ? 0.5726 0.5103 0.4568 0.0770  0.0382  0.0118  83  TRP   B C   
848  O  O   . TRP   B 74  ? 0.5778 0.5088 0.4593 0.0680  0.0354  0.0135  83  TRP   B O   
849  C  CB  . TRP   B 74  ? 0.5457 0.4767 0.4025 0.0807  0.0464  0.0131  83  TRP   B CB  
850  C  CG  . TRP   B 74  ? 0.5347 0.4609 0.3823 0.0931  0.0382  0.0144  83  TRP   B CG  
851  C  CD1 . TRP   B 74  ? 0.5438 0.4582 0.3794 0.0987  0.0266  0.0152  83  TRP   B CD1 
852  C  CD2 . TRP   B 74  ? 0.5304 0.4626 0.3791 0.1022  0.0415  0.0156  83  TRP   B CD2 
853  N  NE1 . TRP   B 74  ? 0.5424 0.4561 0.3702 0.1125  0.0233  0.0169  83  TRP   B NE1 
854  C  CE2 . TRP   B 74  ? 0.5398 0.4655 0.3772 0.1144  0.0329  0.0180  83  TRP   B CE2 
855  C  CE3 . TRP   B 74  ? 0.5287 0.4699 0.3870 0.1015  0.0508  0.0153  83  TRP   B CE3 
856  C  CZ2 . TRP   B 74  ? 0.5477 0.4782 0.3841 0.1258  0.0352  0.0215  83  TRP   B CZ2 
857  C  CZ3 . TRP   B 74  ? 0.5376 0.4822 0.3967 0.1109  0.0519  0.0185  83  TRP   B CZ3 
858  C  CH2 . TRP   B 74  ? 0.5442 0.4849 0.3933 0.1229  0.0451  0.0223  83  TRP   B CH2 
859  N  N   . LYS   B 75  ? 0.5773 0.5181 0.4692 0.0859  0.0314  0.0102  84  LYS   B N   
860  C  CA  . LYS   B 75  ? 0.5875 0.5249 0.4864 0.0860  0.0184  0.0090  84  LYS   B CA  
861  C  C   . LYS   B 75  ? 0.6221 0.5425 0.5005 0.0969  0.0041  0.0083  84  LYS   B C   
862  O  O   . LYS   B 75  ? 0.6298 0.5420 0.5092 0.0962  -0.0094 0.0064  84  LYS   B O   
863  C  CB  . LYS   B 75  ? 0.5790 0.5316 0.4997 0.0903  0.0190  0.0069  84  LYS   B CB  
864  C  CG  . LYS   B 75  ? 0.5873 0.5574 0.5294 0.0818  0.0321  0.0074  84  LYS   B CG  
865  C  CD  . LYS   B 75  ? 0.6023 0.5770 0.5590 0.0678  0.0304  0.0094  84  LYS   B CD  
866  C  CE  . LYS   B 75  ? 0.6311 0.6213 0.6020 0.0605  0.0468  0.0115  84  LYS   B CE  
867  N  NZ  . LYS   B 75  ? 0.6500 0.6610 0.6499 0.0601  0.0483  0.0114  84  LYS   B NZ  
868  N  N   . LEU   B 76  ? 0.6363 0.5522 0.4973 0.1080  0.0066  0.0098  85  LEU   B N   
869  C  CA  . LEU   B 76  ? 0.6516 0.5528 0.4912 0.1223  -0.0049 0.0100  85  LEU   B CA  
870  C  C   . LEU   B 76  ? 0.6845 0.5686 0.5026 0.1201  -0.0110 0.0111  85  LEU   B C   
871  O  O   . LEU   B 76  ? 0.6915 0.5772 0.5027 0.1168  -0.0028 0.0137  85  LEU   B O   
872  C  CB  . LEU   B 76  ? 0.6424 0.5495 0.4758 0.1363  0.0021  0.0130  85  LEU   B CB  
873  C  CG  . LEU   B 76  ? 0.6283 0.5507 0.4807 0.1380  0.0116  0.0131  85  LEU   B CG  
874  C  CD1 . LEU   B 76  ? 0.6303 0.5562 0.4762 0.1495  0.0192  0.0178  85  LEU   B CD1 
875  C  CD2 . LEU   B 76  ? 0.6270 0.5504 0.4884 0.1435  0.0030  0.0097  85  LEU   B CD2 
876  N  N   . ASP   B 77  ? 0.7096 0.5758 0.5157 0.1227  -0.0263 0.0088  86  ASP   B N   
877  C  CA  . ASP   B 77  ? 0.7440 0.5901 0.5281 0.1206  -0.0330 0.0098  86  ASP   B CA  
878  C  C   . ASP   B 77  ? 0.7710 0.5948 0.5264 0.1378  -0.0479 0.0082  86  ASP   B C   
879  O  O   . ASP   B 77  ? 0.7912 0.5970 0.5244 0.1395  -0.0530 0.0092  86  ASP   B O   
880  C  CB  . ASP   B 77  ? 0.7675 0.6078 0.5632 0.1017  -0.0364 0.0093  86  ASP   B CB  
881  C  CG  . ASP   B 77  ? 0.8396 0.6778 0.6513 0.0972  -0.0492 0.0055  86  ASP   B CG  
882  O  OD1 . ASP   B 77  ? 0.8341 0.6753 0.6468 0.1098  -0.0557 0.0023  86  ASP   B OD1 
883  O  OD2 . ASP   B 77  ? 0.8938 0.7279 0.7178 0.0813  -0.0529 0.0063  86  ASP   B OD2 
884  N  N   . ALA   B 78  ? 0.7682 0.5921 0.5214 0.1522  -0.0545 0.0059  87  ALA   B N   
885  C  CA  . ALA   B 78  ? 0.7902 0.5922 0.5128 0.1716  -0.0680 0.0043  87  ALA   B CA  
886  C  C   . ALA   B 78  ? 0.8058 0.6066 0.5059 0.1849  -0.0603 0.0097  87  ALA   B C   
887  O  O   . ALA   B 78  ? 0.8033 0.6249 0.5153 0.1826  -0.0446 0.0146  87  ALA   B O   
888  C  CB  . ALA   B 78  ? 0.7842 0.5889 0.5075 0.1866  -0.0738 0.0017  87  ALA   B CB  
889  N  N   . ALA   B 79  ? 0.8137 0.5902 0.4822 0.1981  -0.0717 0.0088  88  ALA   B N   
890  C  CA  . ALA   B 79  ? 0.8195 0.5956 0.4667 0.2118  -0.0654 0.0143  88  ALA   B CA  
891  C  C   . ALA   B 79  ? 0.8379 0.6004 0.4554 0.2392  -0.0729 0.0148  88  ALA   B C   
892  O  O   . ALA   B 79  ? 0.8458 0.5859 0.4480 0.2466  -0.0891 0.0087  88  ALA   B O   
893  C  CB  . ALA   B 79  ? 0.8289 0.5877 0.4619 0.2028  -0.0698 0.0140  88  ALA   B CB  
894  N  N   . TRP   B 80  ? 0.8435 0.6195 0.4522 0.2550  -0.0616 0.0224  89  TRP   B N   
895  C  CA  . TRP   B 80  ? 0.8728 0.6381 0.4509 0.2839  -0.0656 0.0250  89  TRP   B CA  
896  C  C   . TRP   B 80  ? 0.9203 0.6516 0.4634 0.2917  -0.0815 0.0205  89  TRP   B C   
897  O  O   . TRP   B 80  ? 0.9096 0.6368 0.4518 0.2799  -0.0808 0.0208  89  TRP   B O   
898  C  CB  . TRP   B 80  ? 0.8547 0.6459 0.4363 0.2963  -0.0483 0.0360  89  TRP   B CB  
899  C  CG  . TRP   B 80  ? 0.8688 0.6516 0.4187 0.3279  -0.0497 0.0408  89  TRP   B CG  
900  C  CD1 . TRP   B 80  ? 0.8922 0.6623 0.4242 0.3474  -0.0564 0.0390  89  TRP   B CD1 
901  C  CD2 . TRP   B 80  ? 0.8669 0.6562 0.3998 0.3452  -0.0430 0.0489  89  TRP   B CD2 
902  N  NE1 . TRP   B 80  ? 0.9061 0.6721 0.4082 0.3765  -0.0539 0.0456  89  TRP   B NE1 
903  C  CE2 . TRP   B 80  ? 0.8938 0.6724 0.3970 0.3757  -0.0455 0.0520  89  TRP   B CE2 
904  C  CE3 . TRP   B 80  ? 0.8659 0.6690 0.4048 0.3392  -0.0358 0.0539  89  TRP   B CE3 
905  C  CZ2 . TRP   B 80  ? 0.9010 0.6838 0.3817 0.4002  -0.0397 0.0605  89  TRP   B CZ2 
906  C  CZ3 . TRP   B 80  ? 0.8787 0.6864 0.3967 0.3627  -0.0314 0.0618  89  TRP   B CZ3 
907  C  CH2 . TRP   B 80  ? 0.8863 0.6857 0.3771 0.3928  -0.0323 0.0656  89  TRP   B CH2 
908  N  N   . ASP   B 81  ? 0.9693 0.6736 0.4829 0.3107  -0.0969 0.0153  90  ASP   B N   
909  C  CA  . ASP   B 81  ? 1.0214 0.6877 0.4993 0.3180  -0.1143 0.0098  90  ASP   B CA  
910  C  C   . ASP   B 81  ? 1.0648 0.7264 0.5122 0.3400  -0.1097 0.0159  90  ASP   B C   
911  O  O   . ASP   B 81  ? 1.0967 0.7260 0.5131 0.3462  -0.1227 0.0119  90  ASP   B O   
912  C  CB  . ASP   B 81  ? 1.0496 0.6839 0.5040 0.3300  -0.1358 0.0004  90  ASP   B CB  
913  C  CG  . ASP   B 81  ? 1.1255 0.7614 0.5600 0.3599  -0.1347 0.0024  90  ASP   B CG  
914  O  OD1 . ASP   B 81  ? 1.1308 0.7920 0.5672 0.3738  -0.1164 0.0126  90  ASP   B OD1 
915  O  OD2 . ASP   B 81  ? 1.1707 0.7828 0.5880 0.3697  -0.1524 -0.0059 90  ASP   B OD2 
916  N  N   . GLY   B 82  ? 1.0617 0.7548 0.5186 0.3516  -0.0915 0.0259  91  GLY   B N   
917  C  CA  . GLY   B 82  ? 1.0802 0.7769 0.5139 0.3736  -0.0848 0.0335  91  GLY   B CA  
918  C  C   . GLY   B 82  ? 1.1100 0.7926 0.5072 0.4089  -0.0888 0.0353  91  GLY   B C   
919  O  O   . GLY   B 82  ? 1.1213 0.8119 0.5010 0.4306  -0.0809 0.0434  91  GLY   B O   
920  N  N   . LEU   B 83  ? 1.1257 0.7880 0.5103 0.4166  -0.1012 0.0282  92  LEU   B N   
921  C  CA  . LEU   B 83  ? 1.1549 0.7994 0.4991 0.4526  -0.1064 0.0290  92  LEU   B CA  
922  C  C   . LEU   B 83  ? 1.1484 0.8073 0.5008 0.4636  -0.1002 0.0319  92  LEU   B C   
923  O  O   . LEU   B 83  ? 1.1610 0.8236 0.4903 0.4942  -0.0928 0.0394  92  LEU   B O   
924  C  CB  . LEU   B 83  ? 1.2000 0.7933 0.5047 0.4601  -0.1333 0.0155  92  LEU   B CB  
925  C  CG  . LEU   B 83  ? 1.2472 0.8110 0.5297 0.4554  -0.1450 0.0108  92  LEU   B CG  
926  C  CD1 . LEU   B 83  ? 1.2894 0.8003 0.5296 0.4677  -0.1722 -0.0020 92  LEU   B CD1 
927  C  CD2 . LEU   B 83  ? 1.2639 0.8380 0.5263 0.4778  -0.1323 0.0209  92  LEU   B CD2 
928  N  N   . SER   B 84  ? 1.1319 0.7948 0.5123 0.4417  -0.1049 0.0256  93  SER   B N   
929  C  CA  . SER   B 84  ? 1.1223 0.7921 0.5067 0.4522  -0.1030 0.0262  93  SER   B CA  
930  C  C   . SER   B 84  ? 1.0767 0.7885 0.4940 0.4498  -0.0781 0.0394  93  SER   B C   
931  O  O   . SER   B 84  ? 1.0542 0.7934 0.5046 0.4291  -0.0638 0.0455  93  SER   B O   
932  C  CB  . SER   B 84  ? 1.1490 0.8046 0.5486 0.4316  -0.1205 0.0135  93  SER   B CB  
933  O  OG  . SER   B 84  ? 1.2008 0.8193 0.5792 0.4257  -0.1437 0.0017  93  SER   B OG  
934  N  N   . GLU   B 85  ? 1.0587 0.7732 0.4656 0.4712  -0.0738 0.0435  94  GLU   B N   
935  C  CA  . GLU   B 85  ? 1.0240 0.7734 0.4608 0.4694  -0.0517 0.0559  94  GLU   B CA  
936  C  C   . GLU   B 85  ? 0.9848 0.7457 0.4623 0.4377  -0.0529 0.0496  94  GLU   B C   
937  O  O   . GLU   B 85  ? 0.9913 0.7328 0.4692 0.4245  -0.0714 0.0365  94  GLU   B O   
938  C  CB  . GLU   B 85  ? 1.0654 0.8107 0.4755 0.5031  -0.0470 0.0626  94  GLU   B CB  
939  C  CG  . GLU   B 85  ? 1.1301 0.8748 0.5066 0.5359  -0.0379 0.0736  94  GLU   B CG  
940  C  CD  . GLU   B 85  ? 1.2112 0.9681 0.5756 0.5649  -0.0215 0.0877  94  GLU   B CD  
941  O  OE1 . GLU   B 85  ? 1.2344 0.9851 0.5978 0.5692  -0.0247 0.0850  94  GLU   B OE1 
942  O  OE2 . GLU   B 85  ? 1.2295 1.0028 0.5856 0.5842  -0.0050 0.1022  94  GLU   B OE2 
943  N  N   . VAL   B 86  ? 0.9315 0.7248 0.4447 0.4245  -0.0329 0.0594  95  VAL   B N   
944  C  CA  . VAL   B 86  ? 0.8819 0.6894 0.4339 0.3964  -0.0302 0.0555  95  VAL   B CA  
945  C  C   . VAL   B 86  ? 0.8600 0.6870 0.4270 0.4041  -0.0138 0.0657  95  VAL   B C   
946  O  O   . VAL   B 86  ? 0.8723 0.7045 0.4229 0.4282  -0.0028 0.0773  95  VAL   B O   
947  C  CB  . VAL   B 86  ? 0.8447 0.6698 0.4266 0.3680  -0.0226 0.0563  95  VAL   B CB  
948  C  CG1 . VAL   B 86  ? 0.8527 0.6583 0.4149 0.3650  -0.0357 0.0496  95  VAL   B CG1 
949  C  CG2 . VAL   B 86  ? 0.8234 0.6778 0.4231 0.3692  -0.0010 0.0709  95  VAL   B CG2 
950  N  N   . GLN   B 87  ? 0.8260 0.6630 0.4232 0.3846  -0.0114 0.0623  96  GLN   B N   
951  C  CA  . GLN   B 87  ? 0.8064 0.6602 0.4196 0.3891  0.0045  0.0721  96  GLN   B CA  
952  C  C   . GLN   B 87  ? 0.7805 0.6573 0.4344 0.3611  0.0176  0.0750  96  GLN   B C   
953  O  O   . GLN   B 87  ? 0.7702 0.6464 0.4416 0.3384  0.0104  0.0651  96  GLN   B O   
954  C  CB  . GLN   B 87  ? 0.8211 0.6619 0.4259 0.3991  -0.0054 0.0656  96  GLN   B CB  
955  C  CG  . GLN   B 87  ? 0.8744 0.6946 0.4363 0.4331  -0.0137 0.0665  96  GLN   B CG  
956  C  CD  . GLN   B 87  ? 0.9364 0.7438 0.4871 0.4463  -0.0240 0.0607  96  GLN   B CD  
957  O  OE1 . GLN   B 87  ? 0.9345 0.7498 0.5107 0.4312  -0.0244 0.0565  96  GLN   B OE1 
958  N  NE2 . GLN   B 87  ? 0.9674 0.7539 0.4772 0.4769  -0.0333 0.0600  96  GLN   B NE2 
959  N  N   . LEU   B 88  ? 0.7596 0.6560 0.4282 0.3631  0.0368  0.0889  97  LEU   B N   
960  C  CA  . LEU   B 88  ? 0.7316 0.6470 0.4368 0.3392  0.0488  0.0919  97  LEU   B CA  
961  C  C   . LEU   B 88  ? 0.7259 0.6395 0.4391 0.3423  0.0526  0.0925  97  LEU   B C   
962  O  O   . LEU   B 88  ? 0.7329 0.6445 0.4321 0.3640  0.0594  0.1019  97  LEU   B O   
963  C  CB  . LEU   B 88  ? 0.7176 0.6541 0.4359 0.3397  0.0660  0.1071  97  LEU   B CB  
964  C  CG  . LEU   B 88  ? 0.7075 0.6612 0.4613 0.3197  0.0796  0.1128  97  LEU   B CG  
965  C  CD1 . LEU   B 88  ? 0.6992 0.6536 0.4726 0.2921  0.0733  0.1006  97  LEU   B CD1 
966  C  CD2 . LEU   B 88  ? 0.7023 0.6769 0.4694 0.3222  0.0950  0.1289  97  LEU   B CD2 
967  N  N   . LEU   B 89  ? 0.7058 0.6191 0.4387 0.3229  0.0479  0.0827  98  LEU   B N   
968  C  CA  . LEU   B 89  ? 0.6993 0.6121 0.4414 0.3251  0.0517  0.0829  98  LEU   B CA  
969  C  C   . LEU   B 89  ? 0.6872 0.6158 0.4562 0.3113  0.0694  0.0925  98  LEU   B C   
970  O  O   . LEU   B 89  ? 0.6629 0.5977 0.4543 0.2887  0.0706  0.0868  98  LEU   B O   
971  C  CB  . LEU   B 89  ? 0.7000 0.6065 0.4510 0.3124  0.0381  0.0683  98  LEU   B CB  
972  C  CG  . LEU   B 89  ? 0.7204 0.6272 0.4823 0.3144  0.0405  0.0669  98  LEU   B CG  
973  C  CD1 . LEU   B 89  ? 0.7498 0.6491 0.4909 0.3412  0.0438  0.0751  98  LEU   B CD1 
974  C  CD2 . LEU   B 89  ? 0.7265 0.6285 0.4938 0.3067  0.0244  0.0528  98  LEU   B CD2 
975  N  N   . ALA   B 90  ? 0.6935 0.6283 0.4591 0.3250  0.0832  0.1078  99  ALA   B N   
976  C  CA  . ALA   B 90  ? 0.6848 0.6341 0.4765 0.3121  0.0996  0.1187  99  ALA   B CA  
977  C  C   . ALA   B 90  ? 0.6795 0.6252 0.4850 0.3075  0.1061  0.1195  99  ALA   B C   
978  O  O   . ALA   B 90  ? 0.6887 0.6249 0.4794 0.3258  0.1064  0.1222  99  ALA   B O   
979  C  CB  . ALA   B 90  ? 0.6836 0.6427 0.4696 0.3278  0.1126  0.1363  99  ALA   B CB  
980  N  N   . VAL   B 91  ? 0.6602 0.6115 0.4916 0.2843  0.1102  0.1164  100 VAL   B N   
981  C  CA  . VAL   B 91  ? 0.6586 0.6047 0.5027 0.2798  0.1169  0.1172  100 VAL   B CA  
982  C  C   . VAL   B 91  ? 0.6600 0.6144 0.5258 0.2682  0.1315  0.1297  100 VAL   B C   
983  O  O   . VAL   B 91  ? 0.6550 0.6127 0.5402 0.2467  0.1316  0.1244  100 VAL   B O   
984  C  CB  . VAL   B 91  ? 0.6581 0.5995 0.5111 0.2649  0.1076  0.1011  100 VAL   B CB  
985  C  CG1 . VAL   B 91  ? 0.6647 0.5993 0.5276 0.2637  0.1146  0.1021  100 VAL   B CG1 
986  C  CG2 . VAL   B 91  ? 0.6628 0.5982 0.4985 0.2740  0.0920  0.0897  100 VAL   B CG2 
987  N  N   . PRO   B 92  ? 0.6640 0.6214 0.5267 0.2823  0.1437  0.1468  101 PRO   B N   
988  C  CA  . PRO   B 92  ? 0.6521 0.6190 0.5389 0.2700  0.1572  0.1604  101 PRO   B CA  
989  C  C   . PRO   B 92  ? 0.6513 0.6075 0.5535 0.2590  0.1635  0.1611  101 PRO   B C   
990  O  O   . PRO   B 92  ? 0.6498 0.5919 0.5405 0.2693  0.1626  0.1576  101 PRO   B O   
991  C  CB  . PRO   B 92  ? 0.6703 0.6444 0.5470 0.2915  0.1688  0.1795  101 PRO   B CB  
992  C  CG  . PRO   B 92  ? 0.6895 0.6563 0.5329 0.3154  0.1594  0.1737  101 PRO   B CG  
993  C  CD  . PRO   B 92  ? 0.6725 0.6249 0.5093 0.3106  0.1458  0.1552  101 PRO   B CD  
994  N  N   . PRO   B 93  ? 0.6535 0.6153 0.5813 0.2390  0.1695  0.1662  102 PRO   B N   
995  C  CA  . PRO   B 93  ? 0.6660 0.6136 0.6070 0.2280  0.1748  0.1665  102 PRO   B CA  
996  C  C   . PRO   B 93  ? 0.6913 0.6276 0.6238 0.2454  0.1864  0.1805  102 PRO   B C   
997  O  O   . PRO   B 93  ? 0.6906 0.6350 0.6223 0.2570  0.1972  0.1981  102 PRO   B O   
998  C  CB  . PRO   B 93  ? 0.6566 0.6136 0.6256 0.2056  0.1784  0.1723  102 PRO   B CB  
999  C  CG  . PRO   B 93  ? 0.6535 0.6276 0.6223 0.2001  0.1690  0.1648  102 PRO   B CG  
1000 C  CD  . PRO   B 93  ? 0.6371 0.6169 0.5828 0.2246  0.1696  0.1700  102 PRO   B CD  
1001 N  N   . GLY   B 94  ? 0.7071 0.6255 0.6312 0.2494  0.1842  0.1726  103 GLY   B N   
1002 C  CA  . GLY   B 94  ? 0.7186 0.6222 0.6316 0.2666  0.1939  0.1834  103 GLY   B CA  
1003 C  C   . GLY   B 94  ? 0.7347 0.6397 0.6213 0.2950  0.1949  0.1900  103 GLY   B C   
1004 O  O   . GLY   B 94  ? 0.7516 0.6458 0.6270 0.3118  0.2047  0.2023  103 GLY   B O   
1005 N  N   . GLU   B 95  ? 0.7350 0.6514 0.6096 0.3016  0.1848  0.1824  104 GLU   B N   
1006 C  CA  . GLU   B 95  ? 0.7505 0.6665 0.5967 0.3294  0.1832  0.1867  104 GLU   B CA  
1007 C  C   . GLU   B 95  ? 0.7656 0.6779 0.5950 0.3350  0.1644  0.1668  104 GLU   B C   
1008 O  O   . GLU   B 95  ? 0.7576 0.6743 0.5991 0.3166  0.1544  0.1524  104 GLU   B O   
1009 C  CB  . GLU   B 95  ? 0.7540 0.6869 0.5994 0.3349  0.1894  0.1994  104 GLU   B CB  
1010 C  CG  . GLU   B 95  ? 0.7755 0.7155 0.6400 0.3306  0.2088  0.2217  104 GLU   B CG  
1011 C  CD  . GLU   B 95  ? 0.8132 0.7749 0.6842 0.3332  0.2162  0.2352  104 GLU   B CD  
1012 O  OE1 . GLU   B 95  ? 0.7897 0.7598 0.6491 0.3376  0.2057  0.2261  104 GLU   B OE1 
1013 O  OE2 . GLU   B 95  ? 0.8322 0.8027 0.7208 0.3310  0.2328  0.2556  104 GLU   B OE2 
1014 N  N   . ARG   B 96  ? 0.7851 0.6891 0.5868 0.3607  0.1595  0.1666  105 ARG   B N   
1015 C  CA  . ARG   B 96  ? 0.8023 0.7017 0.5878 0.3683  0.1405  0.1491  105 ARG   B CA  
1016 C  C   . ARG   B 96  ? 0.7935 0.7019 0.5758 0.3620  0.1291  0.1406  105 ARG   B C   
1017 O  O   . ARG   B 96  ? 0.7930 0.7095 0.5726 0.3651  0.1359  0.1508  105 ARG   B O   
1018 C  CB  . ARG   B 96  ? 0.8543 0.7418 0.6078 0.4002  0.1384  0.1540  105 ARG   B CB  
1019 C  CG  . ARG   B 96  ? 0.9369 0.8154 0.6779 0.4092  0.1203  0.1376  105 ARG   B CG  
1020 C  CD  . ARG   B 96  ? 1.0190 0.8840 0.7434 0.4318  0.1251  0.1444  105 ARG   B CD  
1021 N  NE  . ARG   B 96  ? 1.1020 0.9606 0.7982 0.4588  0.1335  0.1595  105 ARG   B NE  
1022 C  CZ  . ARG   B 96  ? 1.1637 1.0146 0.8524 0.4729  0.1507  0.1768  105 ARG   B CZ  
1023 N  NH1 . ARG   B 96  ? 1.1493 0.9958 0.8563 0.4620  0.1603  0.1806  105 ARG   B NH1 
1024 N  NH2 . ARG   B 96  ? 1.1905 1.0365 0.8517 0.4991  0.1588  0.1910  105 ARG   B NH2 
1025 N  N   . ALA   B 97  ? 0.7832 0.6899 0.5649 0.3549  0.1118  0.1226  106 ALA   B N   
1026 C  CA  . ALA   B 97  ? 0.7847 0.6951 0.5596 0.3504  0.0987  0.1132  106 ALA   B CA  
1027 C  C   . ALA   B 97  ? 0.7992 0.7029 0.5419 0.3775  0.0951  0.1190  106 ALA   B C   
1028 O  O   . ALA   B 97  ? 0.8196 0.7123 0.5419 0.3995  0.0925  0.1207  106 ALA   B O   
1029 C  CB  . ALA   B 97  ? 0.7836 0.6910 0.5622 0.3420  0.0815  0.0953  106 ALA   B CB  
1030 N  N   . LYS   B 98  ? 0.7963 0.7055 0.5325 0.3776  0.0948  0.1219  107 LYS   B N   
1031 C  CA  . LYS   B 98  ? 0.8160 0.7181 0.5192 0.4051  0.0926  0.1279  107 LYS   B CA  
1032 C  C   . LYS   B 98  ? 0.8121 0.7133 0.5048 0.4019  0.0798  0.1193  107 LYS   B C   
1033 O  O   . LYS   B 98  ? 0.7975 0.7113 0.5098 0.3825  0.0842  0.1202  107 LYS   B O   
1034 C  CB  . LYS   B 98  ? 0.8573 0.7697 0.5630 0.4147  0.1144  0.1493  107 LYS   B CB  
1035 C  CG  . LYS   B 98  ? 0.9767 0.8848 0.6491 0.4451  0.1174  0.1594  107 LYS   B CG  
1036 C  CD  . LYS   B 98  ? 1.0554 0.9799 0.7390 0.4503  0.1417  0.1828  107 LYS   B CD  
1037 C  CE  . LYS   B 98  ? 1.1006 1.0457 0.8227 0.4203  0.1495  0.1862  107 LYS   B CE  
1038 N  NZ  . LYS   B 98  ? 1.1358 1.0983 0.8584 0.4277  0.1600  0.2003  107 LYS   B NZ  
1039 N  N   . ASN   B 99  ? 0.8184 0.7030 0.4794 0.4208  0.0631  0.1107  108 ASN   B N   
1040 C  CA  . ASN   B 99  ? 0.8192 0.6979 0.4657 0.4198  0.0499  0.1026  108 ASN   B CA  
1041 C  C   . ASN   B 99  ? 0.8292 0.7109 0.4552 0.4400  0.0599  0.1159  108 ASN   B C   
1042 O  O   . ASN   B 99  ? 0.8464 0.7222 0.4486 0.4672  0.0663  0.1256  108 ASN   B O   
1043 C  CB  . ASN   B 99  ? 0.8316 0.6885 0.4531 0.4302  0.0257  0.0869  108 ASN   B CB  
1044 C  CG  . ASN   B 99  ? 0.8549 0.7113 0.4979 0.4108  0.0139  0.0734  108 ASN   B CG  
1045 O  OD1 . ASN   B 99  ? 0.8612 0.7232 0.5191 0.4088  0.0207  0.0756  108 ASN   B OD1 
1046 N  ND2 . ASN   B 99  ? 0.8564 0.7058 0.5013 0.3971  -0.0035 0.0600  108 ASN   B ND2 
1047 N  N   . ILE   B 100 ? 0.8133 0.7049 0.4476 0.4285  0.0620  0.1171  109 ILE   B N   
1048 C  CA  . ILE   B 100 ? 0.8314 0.7296 0.4492 0.4468  0.0715  0.1298  109 ILE   B CA  
1049 C  C   . ILE   B 100 ? 0.8355 0.7215 0.4332 0.4479  0.0553  0.1190  109 ILE   B C   
1050 O  O   . ILE   B 100 ? 0.8223 0.7141 0.4397 0.4234  0.0505  0.1116  109 ILE   B O   
1051 C  CB  . ILE   B 100 ? 0.8307 0.7569 0.4821 0.4316  0.0919  0.1446  109 ILE   B CB  
1052 C  CG1 . ILE   B 100 ? 0.8464 0.7816 0.5206 0.4261  0.1072  0.1548  109 ILE   B CG1 
1053 C  CG2 . ILE   B 100 ? 0.8335 0.7706 0.4699 0.4522  0.1023  0.1590  109 ILE   B CG2 
1054 C  CD1 . ILE   B 100 ? 0.8858 0.8146 0.5351 0.4576  0.1170  0.1679  109 ILE   B CD1 
1055 N  N   . GLN   B 101 ? 0.8505 0.7177 0.4072 0.4769  0.0468  0.1179  110 GLN   B N   
1056 C  CA  . GLN   B 101 ? 0.8798 0.7296 0.4117 0.4811  0.0298  0.1073  110 GLN   B CA  
1057 C  C   . GLN   B 101 ? 0.8899 0.7533 0.4164 0.4902  0.0411  0.1187  110 GLN   B C   
1058 O  O   . GLN   B 101 ? 0.8996 0.7758 0.4188 0.5114  0.0579  0.1351  110 GLN   B O   
1059 C  CB  . GLN   B 101 ? 0.9336 0.7519 0.4207 0.5087  0.0120  0.0984  110 GLN   B CB  
1060 C  CG  . GLN   B 101 ? 0.9965 0.7900 0.4581 0.5095  -0.0099 0.0843  110 GLN   B CG  
1061 C  CD  . GLN   B 101 ? 1.0733 0.8338 0.4979 0.5295  -0.0319 0.0720  110 GLN   B CD  
1062 O  OE1 . GLN   B 101 ? 1.0798 0.8370 0.5116 0.5273  -0.0375 0.0670  110 GLN   B OE1 
1063 N  NE2 . GLN   B 101 ? 1.1059 0.8405 0.4896 0.5496  -0.0460 0.0663  110 GLN   B NE2 
1064 N  N   . THR   B 102 ? 0.8799 0.7411 0.4099 0.4749  0.0322  0.1110  111 THR   B N   
1065 C  CA  . THR   B 102 ? 0.8780 0.7532 0.4044 0.4826  0.0411  0.1206  111 THR   B CA  
1066 C  C   . THR   B 102 ? 0.8973 0.7527 0.4057 0.4770  0.0231  0.1076  111 THR   B C   
1067 O  O   . THR   B 102 ? 0.9178 0.7564 0.4307 0.4576  0.0073  0.0928  111 THR   B O   
1068 C  CB  . THR   B 102 ? 0.8639 0.7750 0.4369 0.4595  0.0599  0.1321  111 THR   B CB  
1069 O  OG1 . THR   B 102 ? 0.8708 0.8013 0.4435 0.4701  0.0707  0.1445  111 THR   B OG1 
1070 C  CG2 . THR   B 102 ? 0.8565 0.7704 0.4610 0.4229  0.0528  0.1203  111 THR   B CG2 
1071 N  N   . LEU   B 103 ? 0.8966 0.7543 0.3856 0.4938  0.0259  0.1137  112 LEU   B N   
1072 C  CA  . LEU   B 103 ? 0.9043 0.7433 0.3773 0.4875  0.0103  0.1028  112 LEU   B CA  
1073 C  C   . LEU   B 103 ? 0.8754 0.7437 0.3840 0.4644  0.0210  0.1085  112 LEU   B C   
1074 O  O   . LEU   B 103 ? 0.8662 0.7618 0.3849 0.4742  0.0371  0.1232  112 LEU   B O   
1075 C  CB  . LEU   B 103 ? 0.9351 0.7535 0.3601 0.5211  0.0038  0.1038  112 LEU   B CB  
1076 C  CG  . LEU   B 103 ? 0.9821 0.7768 0.3903 0.5123  -0.0134 0.0917  112 LEU   B CG  
1077 C  CD1 . LEU   B 103 ? 1.0158 0.7715 0.4039 0.5064  -0.0370 0.0743  112 LEU   B CD1 
1078 C  CD2 . LEU   B 103 ? 1.0133 0.8022 0.3871 0.5409  -0.0123 0.0976  112 LEU   B CD2 
1079 N  N   . PRO   B 104 ? 0.8580 0.7201 0.3835 0.4354  0.0112  0.0971  113 PRO   B N   
1080 C  CA  . PRO   B 104 ? 0.8361 0.7238 0.3925 0.4142  0.0198  0.1013  113 PRO   B CA  
1081 C  C   . PRO   B 104 ? 0.8610 0.7521 0.4004 0.4274  0.0199  0.1060  113 PRO   B C   
1082 O  O   . PRO   B 104 ? 0.8924 0.7570 0.3922 0.4476  0.0085  0.1014  113 PRO   B O   
1083 C  CB  . PRO   B 104 ? 0.8396 0.7147 0.4111 0.3837  0.0084  0.0874  113 PRO   B CB  
1084 C  CG  . PRO   B 104 ? 0.8547 0.7071 0.4152 0.3856  -0.0023 0.0784  113 PRO   B CG  
1085 C  CD  . PRO   B 104 ? 0.8558 0.6903 0.3764 0.4199  -0.0068 0.0810  113 PRO   B CD  
1086 N  N   . GLY   B 105 ? 0.8387 0.7631 0.4085 0.4169  0.0327  0.1155  114 GLY   B N   
1087 C  CA  . GLY   B 105 ? 0.8463 0.7817 0.4107 0.4233  0.0337  0.1201  114 GLY   B CA  
1088 C  C   . GLY   B 105 ? 0.8542 0.7810 0.4277 0.3967  0.0236  0.1089  114 GLY   B C   
1089 O  O   . GLY   B 105 ? 0.8599 0.7649 0.4332 0.3792  0.0137  0.0969  114 GLY   B O   
1090 N  N   . ILE   B 106 ? 0.8459 0.7905 0.4273 0.3941  0.0262  0.1131  115 ILE   B N   
1091 C  CA  . ILE   B 106 ? 0.8516 0.7875 0.4368 0.3724  0.0173  0.1038  115 ILE   B CA  
1092 C  C   . ILE   B 106 ? 0.8243 0.7962 0.4457 0.3568  0.0263  0.1102  115 ILE   B C   
1093 O  O   . ILE   B 106 ? 0.8119 0.8127 0.4443 0.3697  0.0358  0.1224  115 ILE   B O   
1094 C  CB  . ILE   B 106 ? 0.8927 0.8019 0.4365 0.3898  0.0055  0.0996  115 ILE   B CB  
1095 C  CG1 . ILE   B 106 ? 0.9379 0.8047 0.4440 0.4016  -0.0078 0.0904  115 ILE   B CG1 
1096 C  CG2 . ILE   B 106 ? 0.9091 0.8132 0.4557 0.3709  -0.0013 0.0932  115 ILE   B CG2 
1097 C  CD1 . ILE   B 106 ? 0.9621 0.8094 0.4770 0.3772  -0.0161 0.0792  115 ILE   B CD1 
1098 N  N   . PHE   B 107 ? 0.8167 0.7862 0.4550 0.3298  0.0224  0.1019  116 PHE   B N   
1099 C  CA  . PHE   B 107 ? 0.7930 0.7890 0.4591 0.3138  0.0262  0.1043  116 PHE   B CA  
1100 C  C   . PHE   B 107 ? 0.8224 0.7988 0.4635 0.3132  0.0150  0.0971  116 PHE   B C   
1101 O  O   . PHE   B 107 ? 0.8379 0.7868 0.4670 0.2998  0.0069  0.0866  116 PHE   B O   
1102 C  CB  . PHE   B 107 ? 0.7678 0.7675 0.4631 0.2855  0.0284  0.0983  116 PHE   B CB  
1103 C  CG  . PHE   B 107 ? 0.7415 0.7693 0.4724 0.2789  0.0404  0.1066  116 PHE   B CG  
1104 C  CD1 . PHE   B 107 ? 0.7348 0.7802 0.4700 0.2980  0.0499  0.1194  116 PHE   B CD1 
1105 C  CD2 . PHE   B 107 ? 0.7344 0.7686 0.4927 0.2543  0.0426  0.1020  116 PHE   B CD2 
1106 C  CE1 . PHE   B 107 ? 0.7186 0.7875 0.4868 0.2910  0.0615  0.1282  116 PHE   B CE1 
1107 C  CE2 . PHE   B 107 ? 0.7219 0.7779 0.5116 0.2479  0.0529  0.1095  116 PHE   B CE2 
1108 C  CZ  . PHE   B 107 ? 0.7058 0.7787 0.5011 0.2654  0.0624  0.1229  116 PHE   B CZ  
1109 N  N   . LYS   B 108 ? 0.8238 0.8140 0.4570 0.3279  0.0148  0.1033  117 LYS   B N   
1110 C  CA  . LYS   B 108 ? 0.8470 0.8188 0.4560 0.3281  0.0047  0.0973  117 LYS   B CA  
1111 C  C   . LYS   B 108 ? 0.8305 0.8223 0.4664 0.3060  0.0053  0.0953  117 LYS   B C   
1112 O  O   . LYS   B 108 ? 0.8133 0.8412 0.4780 0.3052  0.0118  0.1031  117 LYS   B O   
1113 C  CB  . LYS   B 108 ? 0.8916 0.8677 0.4763 0.3568  0.0034  0.1046  117 LYS   B CB  
1114 C  CG  . LYS   B 108 ? 0.9862 0.9479 0.5443 0.3837  0.0044  0.1085  117 LYS   B CG  
1115 C  CD  . LYS   B 108 ? 1.0818 1.0374 0.6063 0.4131  0.0006  0.1130  117 LYS   B CD  
1116 C  CE  . LYS   B 108 ? 1.1574 1.1104 0.6615 0.4433  0.0054  0.1202  117 LYS   B CE  
1117 N  NZ  . LYS   B 108 ? 1.2040 1.1478 0.6710 0.4747  0.0016  0.1240  117 LYS   B NZ  
1118 N  N   . THR   B 109 ? 0.8302 0.7987 0.4574 0.2881  -0.0014 0.0852  118 THR   B N   
1119 C  CA  . THR   B 109 ? 0.8159 0.7977 0.4616 0.2689  -0.0022 0.0817  118 THR   B CA  
1120 C  C   . THR   B 109 ? 0.8449 0.8031 0.4596 0.2711  -0.0114 0.0768  118 THR   B C   
1121 O  O   . THR   B 109 ? 0.8626 0.7887 0.4450 0.2807  -0.0171 0.0741  118 THR   B O   
1122 C  CB  . THR   B 109 ? 0.8120 0.7902 0.4792 0.2437  0.0009  0.0749  118 THR   B CB  
1123 O  OG1 . THR   B 109 ? 0.8353 0.7794 0.4808 0.2345  -0.0046 0.0664  118 THR   B OG1 
1124 C  CG2 . THR   B 109 ? 0.7998 0.7890 0.4884 0.2428  0.0089  0.0785  118 THR   B CG2 
1125 N  N   . LYS   B 110 ? 0.8483 0.8192 0.4721 0.2610  -0.0135 0.0748  119 LYS   B N   
1126 C  CA  . LYS   B 110 ? 0.8780 0.8264 0.4728 0.2616  -0.0214 0.0704  119 LYS   B CA  
1127 C  C   . LYS   B 110 ? 0.9117 0.8218 0.4881 0.2476  -0.0237 0.0627  119 LYS   B C   
1128 O  O   . LYS   B 110 ? 0.9369 0.8193 0.4828 0.2507  -0.0298 0.0604  119 LYS   B O   
1129 C  CB  . LYS   B 110 ? 0.8774 0.8487 0.4883 0.2523  -0.0232 0.0692  119 LYS   B CB  
1130 C  CG  . LYS   B 110 ? 0.9208 0.8952 0.5544 0.2276  -0.0201 0.0628  119 LYS   B CG  
1131 C  CD  . LYS   B 110 ? 0.9560 0.9567 0.6090 0.2203  -0.0231 0.0617  119 LYS   B CD  
1132 C  CE  . LYS   B 110 ? 0.9993 0.9845 0.6472 0.2024  -0.0248 0.0529  119 LYS   B CE  
1133 N  NZ  . LYS   B 110 ? 1.0241 1.0087 0.6937 0.1851  -0.0180 0.0491  119 LYS   B NZ  
1134 N  N   . ASP   B 111 ? 0.9035 0.8125 0.4991 0.2328  -0.0187 0.0596  120 ASP   B N   
1135 C  CA  . ASP   B 111 ? 0.9240 0.8029 0.5091 0.2190  -0.0199 0.0536  120 ASP   B CA  
1136 C  C   . ASP   B 111 ? 0.9414 0.7988 0.5144 0.2265  -0.0225 0.0533  120 ASP   B C   
1137 O  O   . ASP   B 111 ? 0.9589 0.7956 0.5301 0.2139  -0.0237 0.0488  120 ASP   B O   
1138 C  CB  . ASP   B 111 ? 0.9309 0.8217 0.5440 0.1974  -0.0134 0.0494  120 ASP   B CB  
1139 C  CG  . ASP   B 111 ? 0.9975 0.8993 0.6157 0.1879  -0.0130 0.0471  120 ASP   B CG  
1140 O  OD1 . ASP   B 111 ? 1.0186 0.9146 0.6158 0.1961  -0.0184 0.0481  120 ASP   B OD1 
1141 O  OD2 . ASP   B 111 ? 1.0133 0.9279 0.6544 0.1733  -0.0081 0.0438  120 ASP   B OD2 
1142 N  N   . GLY   B 112 ? 0.9321 0.7947 0.4971 0.2472  -0.0238 0.0581  121 GLY   B N   
1143 C  CA  . GLY   B 112 ? 0.9435 0.7843 0.4932 0.2572  -0.0280 0.0571  121 GLY   B CA  
1144 C  C   . GLY   B 112 ? 0.9238 0.7857 0.4928 0.2650  -0.0217 0.0610  121 GLY   B C   
1145 O  O   . GLY   B 112 ? 0.9025 0.7955 0.5024 0.2576  -0.0130 0.0643  121 GLY   B O   
1146 N  N   . ASP   B 113 ? 0.9272 0.7699 0.4766 0.2804  -0.0266 0.0607  122 ASP   B N   
1147 C  CA  . ASP   B 113 ? 0.9212 0.7793 0.4823 0.2917  -0.0209 0.0650  122 ASP   B CA  
1148 C  C   . ASP   B 113 ? 0.9055 0.7645 0.4895 0.2748  -0.0181 0.0608  122 ASP   B C   
1149 O  O   . ASP   B 113 ? 0.9137 0.7498 0.4933 0.2612  -0.0247 0.0534  122 ASP   B O   
1150 C  CB  . ASP   B 113 ? 0.9615 0.7966 0.4875 0.3184  -0.0281 0.0660  122 ASP   B CB  
1151 C  CG  . ASP   B 113 ? 1.0411 0.8794 0.5441 0.3417  -0.0289 0.0720  122 ASP   B CG  
1152 O  OD1 . ASP   B 113 ? 1.0245 0.8825 0.5386 0.3364  -0.0252 0.0752  122 ASP   B OD1 
1153 O  OD2 . ASP   B 113 ? 1.1049 0.9258 0.5775 0.3667  -0.0336 0.0734  122 ASP   B OD2 
1154 N  N   . ILE   B 114 ? 0.8786 0.7646 0.4872 0.2770  -0.0080 0.0664  123 ILE   B N   
1155 C  CA  . ILE   B 114 ? 0.8683 0.7586 0.4987 0.2654  -0.0039 0.0639  123 ILE   B CA  
1156 C  C   . ILE   B 114 ? 0.8493 0.7456 0.4750 0.2868  0.0000  0.0704  123 ILE   B C   
1157 O  O   . ILE   B 114 ? 0.8384 0.7528 0.4627 0.3033  0.0063  0.0796  123 ILE   B O   
1158 C  CB  . ILE   B 114 ? 0.8665 0.7850 0.5338 0.2461  0.0066  0.0657  123 ILE   B CB  
1159 C  CG1 . ILE   B 114 ? 0.8925 0.8149 0.5638 0.2318  0.0055  0.0630  123 ILE   B CG1 
1160 C  CG2 . ILE   B 114 ? 0.8709 0.7870 0.5565 0.2316  0.0089  0.0609  123 ILE   B CG2 
1161 C  CD1 . ILE   B 114 ? 0.8993 0.8501 0.6042 0.2169  0.0144  0.0652  123 ILE   B CD1 
1162 N  N   . GLY   B 115 ? 0.8436 0.7280 0.4694 0.2864  -0.0026 0.0664  124 GLY   B N   
1163 C  CA  . GLY   B 115 ? 0.8414 0.7315 0.4630 0.3063  0.0023  0.0727  124 GLY   B CA  
1164 C  C   . GLY   B 115 ? 0.8127 0.7374 0.4671 0.3023  0.0181  0.0826  124 GLY   B C   
1165 O  O   . GLY   B 115 ? 0.7933 0.7333 0.4753 0.2808  0.0231  0.0815  124 GLY   B O   
1166 N  N   . ALA   B 116 ? 0.8042 0.7403 0.4549 0.3233  0.0261  0.0928  125 ALA   B N   
1167 C  CA  . ALA   B 116 ? 0.7817 0.7497 0.4642 0.3200  0.0416  0.1042  125 ALA   B CA  
1168 C  C   . ALA   B 116 ? 0.7894 0.7578 0.4661 0.3389  0.0486  0.1117  125 ALA   B C   
1169 O  O   . ALA   B 116 ? 0.8110 0.7678 0.4575 0.3643  0.0459  0.1145  125 ALA   B O   
1170 C  CB  . ALA   B 116 ? 0.7654 0.7590 0.4562 0.3263  0.0484  0.1146  125 ALA   B CB  
1171 N  N   . VAL   B 117 ? 0.7731 0.7532 0.4760 0.3281  0.0576  0.1150  126 VAL   B N   
1172 C  CA  A VAL   B 117 ? 0.7827 0.7631 0.4801 0.3461  0.0654  0.1232  126 VAL   B CA  
1173 C  CA  B VAL   B 117 ? 0.7790 0.7595 0.4778 0.3449  0.0655  0.1229  126 VAL   B CA  
1174 C  C   . VAL   B 117 ? 0.7673 0.7796 0.4903 0.3497  0.0835  0.1408  126 VAL   B C   
1175 O  O   . VAL   B 117 ? 0.7498 0.7806 0.5071 0.3283  0.0902  0.1436  126 VAL   B O   
1176 C  CB  A VAL   B 117 ? 0.7982 0.7626 0.4987 0.3375  0.0612  0.1145  126 VAL   B CB  
1177 C  CB  B VAL   B 117 ? 0.7834 0.7526 0.4938 0.3299  0.0628  0.1144  126 VAL   B CB  
1178 C  CG1 A VAL   B 117 ? 0.8270 0.7602 0.4972 0.3427  0.0432  0.1005  126 VAL   B CG1 
1179 C  CG1 B VAL   B 117 ? 0.7918 0.7623 0.5002 0.3460  0.0720  0.1232  126 VAL   B CG1 
1180 C  CG2 A VAL   B 117 ? 0.7904 0.7649 0.5251 0.3078  0.0642  0.1099  126 VAL   B CG2 
1181 C  CG2 B VAL   B 117 ? 0.8032 0.7438 0.4923 0.3261  0.0452  0.0985  126 VAL   B CG2 
1182 N  N   . ALA   B 118 ? 0.7760 0.7948 0.4818 0.3775  0.0910  0.1533  127 ALA   B N   
1183 C  CA  . ALA   B 118 ? 0.7707 0.8224 0.5019 0.3823  0.1091  0.1725  127 ALA   B CA  
1184 C  C   . ALA   B 118 ? 0.7785 0.8334 0.5188 0.3884  0.1221  0.1829  127 ALA   B C   
1185 O  O   . ALA   B 118 ? 0.7832 0.8394 0.5047 0.4155  0.1307  0.1945  127 ALA   B O   
1186 C  CB  . ALA   B 118 ? 0.7766 0.8395 0.4884 0.4088  0.1132  0.1829  127 ALA   B CB  
1187 N  N   . LEU   B 119 ? 0.7726 0.8264 0.5390 0.3644  0.1233  0.1784  128 LEU   B N   
1188 C  CA  . LEU   B 119 ? 0.7718 0.8258 0.5476 0.3678  0.1349  0.1875  128 LEU   B CA  
1189 C  C   . LEU   B 119 ? 0.7539 0.8275 0.5744 0.3408  0.1441  0.1934  128 LEU   B C   
1190 O  O   . LEU   B 119 ? 0.7509 0.8252 0.5888 0.3161  0.1359  0.1823  128 LEU   B O   
1191 C  CB  . LEU   B 119 ? 0.7918 0.8156 0.5463 0.3696  0.1239  0.1732  128 LEU   B CB  
1192 C  CG  . LEU   B 119 ? 0.8426 0.8425 0.5523 0.3953  0.1119  0.1657  128 LEU   B CG  
1193 C  CD1 . LEU   B 119 ? 0.8664 0.8397 0.5632 0.3906  0.0979  0.1496  128 LEU   B CD1 
1194 C  CD2 . LEU   B 119 ? 0.8582 0.8611 0.5462 0.4280  0.1236  0.1815  128 LEU   B CD2 
1195 N  N   . ASP   B 120 ? 0.7391 0.8259 0.5765 0.3457  0.1606  0.2107  129 ASP   B N   
1196 C  CA  . ASP   B 120 ? 0.7241 0.8276 0.6036 0.3214  0.1696  0.2183  129 ASP   B CA  
1197 C  C   . ASP   B 120 ? 0.7168 0.8035 0.6021 0.3130  0.1725  0.2157  129 ASP   B C   
1198 O  O   . ASP   B 120 ? 0.7260 0.8058 0.5987 0.3312  0.1821  0.2258  129 ASP   B O   
1199 C  CB  . ASP   B 120 ? 0.7523 0.8857 0.6536 0.3298  0.1875  0.2424  129 ASP   B CB  
1200 C  CG  . ASP   B 120 ? 0.8233 0.9843 0.7546 0.3135  0.1860  0.2454  129 ASP   B CG  
1201 O  OD1 . ASP   B 120 ? 0.8367 1.0003 0.7969 0.2850  0.1811  0.2387  129 ASP   B OD1 
1202 O  OD2 . ASP   B 120 ? 0.8463 1.0254 0.7707 0.3301  0.1888  0.2537  129 ASP   B OD2 
1203 N  N   . TYR   B 121 ? 0.6969 0.7774 0.6013 0.2864  0.1652  0.2034  130 TYR   B N   
1204 C  CA  . TYR   B 121 ? 0.6972 0.7613 0.6088 0.2761  0.1669  0.1992  130 TYR   B CA  
1205 C  C   . TYR   B 121 ? 0.6709 0.7428 0.6183 0.2467  0.1674  0.1977  130 TYR   B C   
1206 O  O   . TYR   B 121 ? 0.6693 0.7524 0.6286 0.2324  0.1600  0.1916  130 TYR   B O   
1207 C  CB  . TYR   B 121 ? 0.7228 0.7620 0.6088 0.2781  0.1525  0.1794  130 TYR   B CB  
1208 C  CG  . TYR   B 121 ? 0.7645 0.7907 0.6159 0.3068  0.1511  0.1806  130 TYR   B CG  
1209 C  CD1 . TYR   B 121 ? 0.7949 0.8093 0.6379 0.3194  0.1580  0.1863  130 TYR   B CD1 
1210 C  CD2 . TYR   B 121 ? 0.7910 0.8152 0.6162 0.3229  0.1429  0.1767  130 TYR   B CD2 
1211 C  CE1 . TYR   B 121 ? 0.8261 0.8279 0.6352 0.3475  0.1559  0.1875  130 TYR   B CE1 
1212 C  CE2 . TYR   B 121 ? 0.8255 0.8355 0.6164 0.3506  0.1404  0.1777  130 TYR   B CE2 
1213 C  CZ  . TYR   B 121 ? 0.8514 0.8505 0.6343 0.3629  0.1465  0.1826  130 TYR   B CZ  
1214 O  OH  . TYR   B 121 ? 0.8978 0.8816 0.6445 0.3915  0.1425  0.1827  130 TYR   B OH  
1215 N  N   . PRO   B 122 ? 0.6506 0.7143 0.6134 0.2379  0.1750  0.2025  131 PRO   B N   
1216 C  CA  . PRO   B 122 ? 0.6293 0.6948 0.6227 0.2101  0.1733  0.1990  131 PRO   B CA  
1217 C  C   . PRO   B 122 ? 0.6109 0.6662 0.5992 0.1943  0.1576  0.1769  131 PRO   B C   
1218 O  O   . PRO   B 122 ? 0.6292 0.6711 0.5921 0.2031  0.1494  0.1644  131 PRO   B O   
1219 C  CB  . PRO   B 122 ? 0.6461 0.6949 0.6448 0.2087  0.1821  0.2045  131 PRO   B CB  
1220 C  CG  . PRO   B 122 ? 0.6659 0.7140 0.6453 0.2359  0.1932  0.2186  131 PRO   B CG  
1221 C  CD  . PRO   B 122 ? 0.6608 0.7096 0.6105 0.2536  0.1839  0.2098  131 PRO   B CD  
1222 N  N   . ALA   B 123 ? 0.5709 0.6329 0.5828 0.1717  0.1530  0.1728  132 ALA   B N   
1223 C  CA  . ALA   B 123 ? 0.5538 0.6072 0.5618 0.1563  0.1396  0.1536  132 ALA   B CA  
1224 C  C   . ALA   B 123 ? 0.5436 0.5720 0.5354 0.1553  0.1352  0.1389  132 ALA   B C   
1225 O  O   . ALA   B 123 ? 0.5419 0.5634 0.5191 0.1529  0.1255  0.1244  132 ALA   B O   
1226 C  CB  . ALA   B 123 ? 0.5397 0.6012 0.5761 0.1337  0.1367  0.1535  132 ALA   B CB  
1227 N  N   . GLY   B 124 ? 0.5329 0.5491 0.5270 0.1588  0.1431  0.1441  133 GLY   B N   
1228 C  CA  . GLY   B 124 ? 0.5320 0.5273 0.5125 0.1608  0.1404  0.1324  133 GLY   B CA  
1229 C  C   . GLY   B 124 ? 0.5315 0.5220 0.4860 0.1790  0.1359  0.1267  133 GLY   B C   
1230 O  O   . GLY   B 124 ? 0.5381 0.5151 0.4828 0.1806  0.1319  0.1161  133 GLY   B O   
1231 N  N   . THR   B 125 ? 0.5255 0.5271 0.4687 0.1932  0.1357  0.1335  134 THR   B N   
1232 C  CA  . THR   B 125 ? 0.5413 0.5370 0.4582 0.2104  0.1288  0.1276  134 THR   B CA  
1233 C  C   . THR   B 125 ? 0.5314 0.5265 0.4407 0.2010  0.1160  0.1128  134 THR   B C   
1234 O  O   . THR   B 125 ? 0.5317 0.5186 0.4217 0.2104  0.1079  0.1051  134 THR   B O   
1235 C  CB  . THR   B 125 ? 0.5695 0.5739 0.4739 0.2325  0.1347  0.1420  134 THR   B CB  
1236 O  OG1 . THR   B 125 ? 0.5862 0.5946 0.5034 0.2367  0.1487  0.1581  134 THR   B OG1 
1237 C  CG2 . THR   B 125 ? 0.5889 0.5808 0.4636 0.2541  0.1283  0.1374  134 THR   B CG2 
1238 N  N   . SER   B 126 ? 0.5195 0.5223 0.4437 0.1826  0.1138  0.1092  135 SER   B N   
1239 C  CA  . SER   B 126 ? 0.5237 0.5257 0.4407 0.1733  0.1033  0.0970  135 SER   B CA  
1240 C  C   . SER   B 126 ? 0.5196 0.5071 0.4258 0.1716  0.0969  0.0839  135 SER   B C   
1241 O  O   . SER   B 126 ? 0.5283 0.5088 0.4429 0.1650  0.0998  0.0799  135 SER   B O   
1242 C  CB  . SER   B 126 ? 0.5521 0.5597 0.4868 0.1534  0.1024  0.0936  135 SER   B CB  
1243 O  OG  . SER   B 126 ? 0.5902 0.6150 0.5380 0.1516  0.1050  0.1037  135 SER   B OG  
1244 N  N   . GLY   B 127 ? 0.5095 0.4928 0.3986 0.1766  0.0882  0.0774  136 GLY   B N   
1245 C  CA  . GLY   B 127 ? 0.5159 0.4884 0.3981 0.1738  0.0816  0.0660  136 GLY   B CA  
1246 C  C   . GLY   B 127 ? 0.5270 0.4918 0.3949 0.1905  0.0773  0.0659  136 GLY   B C   
1247 O  O   . GLY   B 127 ? 0.5253 0.4831 0.3888 0.1886  0.0700  0.0570  136 GLY   B O   
1248 N  N   . SER   B 128 ? 0.5328 0.4993 0.3934 0.2074  0.0815  0.0763  137 SER   B N   
1249 C  CA  . SER   B 128 ? 0.5480 0.5055 0.3906 0.2265  0.0763  0.0765  137 SER   B CA  
1250 C  C   . SER   B 128 ? 0.5679 0.5175 0.3919 0.2300  0.0630  0.0690  137 SER   B C   
1251 O  O   . SER   B 128 ? 0.5777 0.5305 0.3955 0.2287  0.0614  0.0709  137 SER   B O   
1252 C  CB  . SER   B 128 ? 0.5479 0.5091 0.3833 0.2450  0.0848  0.0904  137 SER   B CB  
1253 O  OG  . SER   B 128 ? 0.5399 0.5042 0.3914 0.2424  0.0964  0.0975  137 SER   B OG  
1254 N  N   . PRO   B 129 ? 0.5789 0.5178 0.3945 0.2340  0.0524  0.0605  138 PRO   B N   
1255 C  CA  . PRO   B 129 ? 0.5971 0.5256 0.3959 0.2352  0.0385  0.0533  138 PRO   B CA  
1256 C  C   . PRO   B 129 ? 0.6292 0.5486 0.4009 0.2566  0.0328  0.0576  138 PRO   B C   
1257 O  O   . PRO   B 129 ? 0.6442 0.5619 0.4053 0.2756  0.0362  0.0642  138 PRO   B O   
1258 C  CB  . PRO   B 129 ? 0.5978 0.5199 0.4015 0.2312  0.0290  0.0436  138 PRO   B CB  
1259 C  CG  . PRO   B 129 ? 0.5937 0.5187 0.4034 0.2414  0.0357  0.0476  138 PRO   B CG  
1260 C  CD  . PRO   B 129 ? 0.5666 0.5024 0.3886 0.2371  0.0518  0.0571  138 PRO   B CD  
1261 N  N   . ILE   B 130 ? 0.6478 0.5597 0.4057 0.2548  0.0241  0.0540  139 ILE   B N   
1262 C  CA  . ILE   B 130 ? 0.6838 0.5828 0.4118 0.2750  0.0160  0.0557  139 ILE   B CA  
1263 C  C   . ILE   B 130 ? 0.7088 0.5878 0.4239 0.2747  -0.0025 0.0441  139 ILE   B C   
1264 O  O   . ILE   B 130 ? 0.6953 0.5724 0.4223 0.2554  -0.0080 0.0368  139 ILE   B O   
1265 C  CB  . ILE   B 130 ? 0.6904 0.5935 0.4111 0.2741  0.0187  0.0601  139 ILE   B CB  
1266 C  CG1 . ILE   B 130 ? 0.6875 0.6131 0.4260 0.2730  0.0357  0.0719  139 ILE   B CG1 
1267 C  CG2 . ILE   B 130 ? 0.7174 0.6038 0.4035 0.2969  0.0091  0.0607  139 ILE   B CG2 
1268 C  CD1 . ILE   B 130 ? 0.7004 0.6358 0.4431 0.2645  0.0385  0.0745  139 ILE   B CD1 
1269 N  N   . LEU   B 131 ? 0.7364 0.6006 0.4282 0.2958  -0.0121 0.0427  140 LEU   B N   
1270 C  CA  . LEU   B 131 ? 0.7800 0.6250 0.4617 0.2957  -0.0318 0.0314  140 LEU   B CA  
1271 C  C   . LEU   B 131 ? 0.8294 0.6496 0.4749 0.3130  -0.0471 0.0279  140 LEU   B C   
1272 O  O   . LEU   B 131 ? 0.8453 0.6621 0.4672 0.3347  -0.0424 0.0350  140 LEU   B O   
1273 C  CB  . LEU   B 131 ? 0.7888 0.6339 0.4750 0.3046  -0.0354 0.0289  140 LEU   B CB  
1274 C  CG  . LEU   B 131 ? 0.7941 0.6575 0.4978 0.3072  -0.0177 0.0372  140 LEU   B CG  
1275 C  CD1 . LEU   B 131 ? 0.7929 0.6502 0.4902 0.3224  -0.0246 0.0345  140 LEU   B CD1 
1276 C  CD2 . LEU   B 131 ? 0.7873 0.6684 0.5256 0.2812  -0.0073 0.0366  140 LEU   B CD2 
1277 N  N   . ASP   B 132 ? 0.8508 0.6529 0.4917 0.3038  -0.0656 0.0173  141 ASP   B N   
1278 C  CA  . ASP   B 132 ? 0.8899 0.6624 0.4949 0.3194  -0.0842 0.0117  141 ASP   B CA  
1279 C  C   . ASP   B 132 ? 0.9230 0.6813 0.5134 0.3368  -0.0992 0.0054  141 ASP   B C   
1280 O  O   . ASP   B 132 ? 0.9074 0.6808 0.5187 0.3339  -0.0945 0.0057  141 ASP   B O   
1281 C  CB  . ASP   B 132 ? 0.9041 0.6615 0.5107 0.2997  -0.0969 0.0044  141 ASP   B CB  
1282 C  CG  . ASP   B 132 ? 0.9517 0.7080 0.5830 0.2785  -0.1090 -0.0042 141 ASP   B CG  
1283 O  OD1 . ASP   B 132 ? 0.9429 0.7108 0.5908 0.2793  -0.1091 -0.0060 141 ASP   B OD1 
1284 O  OD2 . ASP   B 132 ? 0.9950 0.7397 0.6297 0.2614  -0.1178 -0.0085 141 ASP   B OD2 
1285 N  N   . LYS   B 133 ? 0.9690 0.6971 0.5224 0.3553  -0.1182 -0.0008 142 LYS   B N   
1286 C  CA  . LYS   B 133 ? 1.0033 0.7145 0.5368 0.3750  -0.1348 -0.0076 142 LYS   B CA  
1287 C  C   . LYS   B 133 ? 0.9928 0.7083 0.5554 0.3564  -0.1483 -0.0170 142 LYS   B C   
1288 O  O   . LYS   B 133 ? 0.9934 0.7060 0.5505 0.3704  -0.1569 -0.0207 142 LYS   B O   
1289 C  CB  . LYS   B 133 ? 1.0816 0.7558 0.5674 0.3972  -0.1545 -0.0137 142 LYS   B CB  
1290 C  CG  . LYS   B 133 ? 1.1777 0.8515 0.6348 0.4199  -0.1393 -0.0030 142 LYS   B CG  
1291 C  CD  . LYS   B 133 ? 1.2862 0.9224 0.6952 0.4401  -0.1569 -0.0087 142 LYS   B CD  
1292 C  CE  . LYS   B 133 ? 1.3524 0.9925 0.7331 0.4675  -0.1403 0.0032  142 LYS   B CE  
1293 N  NZ  . LYS   B 133 ? 1.4165 1.0198 0.7492 0.4879  -0.1561 -0.0022 142 LYS   B NZ  
1294 N  N   . CYS   B 134 ? 0.9770 0.7027 0.5723 0.3257  -0.1482 -0.0196 143 CYS   B N   
1295 C  CA  . CYS   B 134 ? 0.9592 0.6952 0.5878 0.3072  -0.1579 -0.0265 143 CYS   B CA  
1296 C  C   . CYS   B 134 ? 0.9128 0.6827 0.5783 0.2953  -0.1373 -0.0204 143 CYS   B C   
1297 O  O   . CYS   B 134 ? 0.9058 0.6884 0.6020 0.2789  -0.1423 -0.0249 143 CYS   B O   
1298 C  CB  . CYS   B 134 ? 0.9851 0.7109 0.6277 0.2820  -0.1717 -0.0329 143 CYS   B CB  
1299 S  SG  . CYS   B 134 ? 1.1087 0.7907 0.7061 0.2930  -0.1931 -0.0388 143 CYS   B SG  
1300 N  N   . GLY   B 135 ? 0.8835 0.6678 0.5470 0.3033  -0.1149 -0.0102 144 GLY   B N   
1301 C  CA  . GLY   B 135 ? 0.8464 0.6590 0.5418 0.2928  -0.0953 -0.0043 144 GLY   B CA  
1302 C  C   . GLY   B 135 ? 0.8031 0.6318 0.5284 0.2646  -0.0843 -0.0029 144 GLY   B C   
1303 O  O   . GLY   B 135 ? 0.7816 0.6314 0.5353 0.2532  -0.0719 -0.0007 144 GLY   B O   
1304 N  N   . ARG   B 136 ? 0.7898 0.6071 0.5071 0.2543  -0.0890 -0.0042 145 ARG   B N   
1305 C  CA  . ARG   B 136 ? 0.7657 0.5958 0.5066 0.2294  -0.0784 -0.0024 145 ARG   B CA  
1306 C  C   . ARG   B 136 ? 0.7355 0.5767 0.4733 0.2313  -0.0588 0.0064  145 ARG   B C   
1307 O  O   . ARG   B 136 ? 0.7333 0.5650 0.4451 0.2484  -0.0580 0.0106  145 ARG   B O   
1308 C  CB  . ARG   B 136 ? 0.8073 0.6186 0.5402 0.2174  -0.0923 -0.0071 145 ARG   B CB  
1309 C  CG  . ARG   B 136 ? 0.8733 0.6785 0.6206 0.2071  -0.1108 -0.0151 145 ARG   B CG  
1310 C  CD  . ARG   B 136 ? 0.9535 0.7384 0.6937 0.1934  -0.1230 -0.0180 145 ARG   B CD  
1311 N  NE  . ARG   B 136 ? 1.0589 0.8121 0.7605 0.2115  -0.1405 -0.0220 145 ARG   B NE  
1312 C  CZ  . ARG   B 136 ? 1.1371 0.8669 0.8165 0.2093  -0.1469 -0.0222 145 ARG   B CZ  
1313 N  NH1 . ARG   B 136 ? 1.1437 0.8791 0.8355 0.1899  -0.1366 -0.0180 145 ARG   B NH1 
1314 N  NH2 . ARG   B 136 ? 1.1676 0.8667 0.8093 0.2284  -0.1635 -0.0265 145 ARG   B NH2 
1315 N  N   . VAL   B 137 ? 0.7049 0.5662 0.4693 0.2143  -0.0435 0.0093  146 VAL   B N   
1316 C  CA  . VAL   B 137 ? 0.6851 0.5576 0.4502 0.2135  -0.0266 0.0169  146 VAL   B CA  
1317 C  C   . VAL   B 137 ? 0.6916 0.5559 0.4452 0.2059  -0.0282 0.0174  146 VAL   B C   
1318 O  O   . VAL   B 137 ? 0.6979 0.5621 0.4628 0.1876  -0.0295 0.0141  146 VAL   B O   
1319 C  CB  . VAL   B 137 ? 0.6620 0.5553 0.4554 0.2007  -0.0112 0.0190  146 VAL   B CB  
1320 C  CG1 . VAL   B 137 ? 0.6620 0.5653 0.4565 0.1993  0.0034  0.0262  146 VAL   B CG1 
1321 C  CG2 . VAL   B 137 ? 0.6540 0.5537 0.4566 0.2102  -0.0096 0.0189  146 VAL   B CG2 
1322 N  N   . ILE   B 138 ? 0.6847 0.5419 0.4145 0.2214  -0.0279 0.0221  147 ILE   B N   
1323 C  CA  . ILE   B 138 ? 0.6797 0.5288 0.3946 0.2186  -0.0291 0.0235  147 ILE   B CA  
1324 C  C   . ILE   B 138 ? 0.6616 0.5302 0.3885 0.2118  -0.0130 0.0301  147 ILE   B C   
1325 O  O   . ILE   B 138 ? 0.6680 0.5334 0.3851 0.2089  -0.0129 0.0316  147 ILE   B O   
1326 C  CB  . ILE   B 138 ? 0.7001 0.5290 0.3800 0.2413  -0.0398 0.0241  147 ILE   B CB  
1327 C  CG1 . ILE   B 138 ? 0.7131 0.5520 0.3851 0.2632  -0.0306 0.0321  147 ILE   B CG1 
1328 C  CG2 . ILE   B 138 ? 0.7145 0.5200 0.3819 0.2443  -0.0592 0.0156  147 ILE   B CG2 
1329 C  CD1 . ILE   B 138 ? 0.7556 0.5766 0.3910 0.2894  -0.0385 0.0340  147 ILE   B CD1 
1330 N  N   . GLY   B 139 ? 0.6313 0.5187 0.3797 0.2085  -0.0007 0.0336  148 GLY   B N   
1331 C  CA  . GLY   B 139 ? 0.6087 0.5133 0.3709 0.2003  0.0123  0.0387  148 GLY   B CA  
1332 C  C   . GLY   B 139 ? 0.5877 0.5080 0.3667 0.2038  0.0241  0.0444  148 GLY   B C   
1333 O  O   . GLY   B 139 ? 0.6006 0.5185 0.3780 0.2150  0.0233  0.0453  148 GLY   B O   
1334 N  N   . LEU   B 140 ? 0.5653 0.5003 0.3597 0.1943  0.0344  0.0484  149 LEU   B N   
1335 C  CA  . LEU   B 140 ? 0.5442 0.4923 0.3560 0.1954  0.0458  0.0546  149 LEU   B CA  
1336 C  C   . LEU   B 140 ? 0.5476 0.5079 0.3590 0.2037  0.0525  0.0650  149 LEU   B C   
1337 O  O   . LEU   B 140 ? 0.5497 0.5131 0.3554 0.2014  0.0502  0.0658  149 LEU   B O   
1338 C  CB  . LEU   B 140 ? 0.5214 0.4760 0.3548 0.1763  0.0519  0.0504  149 LEU   B CB  
1339 C  CG  . LEU   B 140 ? 0.5213 0.4690 0.3602 0.1667  0.0481  0.0412  149 LEU   B CG  
1340 C  CD1 . LEU   B 140 ? 0.5161 0.4705 0.3740 0.1529  0.0565  0.0387  149 LEU   B CD1 
1341 C  CD2 . LEU   B 140 ? 0.5148 0.4565 0.3503 0.1785  0.0437  0.0401  149 LEU   B CD2 
1342 N  N   . TYR   B 141 ? 0.5435 0.5111 0.3614 0.2141  0.0609  0.0739  150 TYR   B N   
1343 C  CA  . TYR   B 141 ? 0.5500 0.5328 0.3726 0.2230  0.0697  0.0867  150 TYR   B CA  
1344 C  C   . TYR   B 141 ? 0.5416 0.5380 0.3924 0.2061  0.0786  0.0898  150 TYR   B C   
1345 O  O   . TYR   B 141 ? 0.5419 0.5336 0.4041 0.1975  0.0813  0.0859  150 TYR   B O   
1346 C  CB  . TYR   B 141 ? 0.5594 0.5399 0.3724 0.2443  0.0747  0.0953  150 TYR   B CB  
1347 C  CG  . TYR   B 141 ? 0.5691 0.5673 0.3937 0.2525  0.0881  0.1112  150 TYR   B CG  
1348 C  CD1 . TYR   B 141 ? 0.5767 0.5826 0.4245 0.2445  0.0989  0.1177  150 TYR   B CD1 
1349 C  CD2 . TYR   B 141 ? 0.5857 0.5920 0.3973 0.2699  0.0903  0.1206  150 TYR   B CD2 
1350 C  CE1 . TYR   B 141 ? 0.5898 0.6125 0.4515 0.2503  0.1116  0.1339  150 TYR   B CE1 
1351 C  CE2 . TYR   B 141 ? 0.5906 0.6163 0.4158 0.2775  0.1039  0.1371  150 TYR   B CE2 
1352 C  CZ  . TYR   B 141 ? 0.6062 0.6404 0.4577 0.2669  0.1146  0.1441  150 TYR   B CZ  
1353 O  OH  . TYR   B 141 ? 0.6335 0.6876 0.5015 0.2728  0.1285  0.1619  150 TYR   B OH  
1354 N  N   . GLY   B 142 ? 0.5316 0.5439 0.3935 0.2021  0.0822  0.0966  151 GLY   B N   
1355 C  CA  . GLY   B 142 ? 0.5301 0.5537 0.4192 0.1855  0.0885  0.0993  151 GLY   B CA  
1356 C  C   . GLY   B 142 ? 0.5269 0.5609 0.4256 0.1719  0.0845  0.0966  151 GLY   B C   
1357 O  O   . GLY   B 142 ? 0.5124 0.5529 0.4325 0.1569  0.0871  0.0968  151 GLY   B O   
1358 N  N   . ASN   B 143 ? 0.5308 0.5648 0.4127 0.1775  0.0774  0.0940  152 ASN   B N   
1359 C  CA  . ASN   B 143 ? 0.5321 0.5771 0.4207 0.1678  0.0731  0.0924  152 ASN   B CA  
1360 C  C   . ASN   B 143 ? 0.5404 0.5953 0.4159 0.1848  0.0716  0.1001  152 ASN   B C   
1361 O  O   . ASN   B 143 ? 0.5496 0.5905 0.3989 0.1969  0.0663  0.0965  152 ASN   B O   
1362 C  CB  . ASN   B 143 ? 0.5526 0.5832 0.4305 0.1549  0.0646  0.0784  152 ASN   B CB  
1363 C  CG  . ASN   B 143 ? 0.6043 0.6457 0.4907 0.1439  0.0603  0.0764  152 ASN   B CG  
1364 O  OD1 . ASN   B 143 ? 0.6181 0.6774 0.5269 0.1392  0.0633  0.0832  152 ASN   B OD1 
1365 N  ND2 . ASN   B 143 ? 0.6044 0.6355 0.4736 0.1397  0.0527  0.0676  152 ASN   B ND2 
1366 N  N   . GLY   B 144 ? 0.5323 0.6109 0.4265 0.1862  0.0763  0.1109  153 GLY   B N   
1367 C  CA  . GLY   B 144 ? 0.5525 0.6441 0.4364 0.2041  0.0765  0.1197  153 GLY   B CA  
1368 C  C   . GLY   B 144 ? 0.5508 0.6734 0.4616 0.2017  0.0805  0.1310  153 GLY   B C   
1369 O  O   . GLY   B 144 ? 0.5329 0.6645 0.4645 0.1834  0.0766  0.1272  153 GLY   B O   
1370 N  N   . VAL   B 145 ? 0.5718 0.7110 0.4819 0.2213  0.0879  0.1450  154 VAL   B N   
1371 C  CA  . VAL   B 145 ? 0.5925 0.7654 0.5280 0.2228  0.0921  0.1579  154 VAL   B CA  
1372 C  C   . VAL   B 145 ? 0.6209 0.8141 0.5731 0.2359  0.1073  0.1771  154 VAL   B C   
1373 O  O   . VAL   B 145 ? 0.6276 0.8068 0.5618 0.2505  0.1139  0.1804  154 VAL   B O   
1374 C  CB  . VAL   B 145 ? 0.6104 0.7861 0.5231 0.2367  0.0841  0.1555  154 VAL   B CB  
1375 C  CG1 . VAL   B 145 ? 0.6186 0.7938 0.5059 0.2665  0.0900  0.1648  154 VAL   B CG1 
1376 C  CG2 . VAL   B 145 ? 0.6083 0.8137 0.5473 0.2279  0.0804  0.1595  154 VAL   B CG2 
1377 N  N   . VAL   B 146 ? 0.6355 0.8622 0.6233 0.2300  0.1128  0.1901  155 VAL   B N   
1378 C  CA  . VAL   B 146 ? 0.6591 0.9104 0.6672 0.2417  0.1288  0.2112  155 VAL   B CA  
1379 C  C   . VAL   B 146 ? 0.6915 0.9699 0.6968 0.2619  0.1309  0.2220  155 VAL   B C   
1380 O  O   . VAL   B 146 ? 0.6814 0.9781 0.7013 0.2536  0.1226  0.2195  155 VAL   B O   
1381 C  CB  . VAL   B 146 ? 0.6478 0.9183 0.7035 0.2184  0.1343  0.2199  155 VAL   B CB  
1382 C  CG1 . VAL   B 146 ? 0.6446 0.9394 0.7211 0.2308  0.1530  0.2438  155 VAL   B CG1 
1383 C  CG2 . VAL   B 146 ? 0.6605 0.9014 0.7159 0.1984  0.1301  0.2067  155 VAL   B CG2 
1384 N  N   . ILE   B 147 ? 0.7304 1.0098 0.7133 0.2905  0.1412  0.2330  156 ILE   B N   
1385 C  CA  . ILE   B 147 ? 0.7572 1.0599 0.7316 0.3143  0.1442  0.2434  156 ILE   B CA  
1386 C  C   . ILE   B 147 ? 0.7573 1.1058 0.7735 0.3186  0.1608  0.2684  156 ILE   B C   
1387 O  O   . ILE   B 147 ? 0.7409 1.0990 0.7909 0.3021  0.1694  0.2771  156 ILE   B O   
1388 C  CB  . ILE   B 147 ? 0.7924 1.0672 0.7131 0.3452  0.1436  0.2395  156 ILE   B CB  
1389 C  CG1 . ILE   B 147 ? 0.8121 1.0756 0.7224 0.3590  0.1568  0.2486  156 ILE   B CG1 
1390 C  CG2 . ILE   B 147 ? 0.8265 1.0621 0.7127 0.3384  0.1257  0.2163  156 ILE   B CG2 
1391 C  CD1 . ILE   B 147 ? 0.8516 1.0936 0.7116 0.3936  0.1573  0.2484  156 ILE   B CD1 
1392 N  N   . LYS   B 148 ? 0.7694 1.1465 0.7849 0.3398  0.1647  0.2797  157 LYS   B N   
1393 C  CA  . LYS   B 148 ? 0.7692 1.1953 0.8228 0.3483  0.1801  0.3045  157 LYS   B CA  
1394 C  C   . LYS   B 148 ? 0.7763 1.2145 0.8536 0.3492  0.2003  0.3244  157 LYS   B C   
1395 O  O   . LYS   B 148 ? 0.7608 1.2337 0.8899 0.3321  0.2080  0.3394  157 LYS   B O   
1396 C  CB  . LYS   B 148 ? 0.8126 1.2532 0.8391 0.3838  0.1839  0.3125  157 LYS   B CB  
1397 C  CG  . LYS   B 148 ? 0.9104 1.3167 0.8791 0.4165  0.1883  0.3101  157 LYS   B CG  
1398 C  CD  . LYS   B 148 ? 1.0071 1.3635 0.9252 0.4175  0.1688  0.2841  157 LYS   B CD  
1399 C  CE  . LYS   B 148 ? 1.0555 1.4144 0.9687 0.4118  0.1526  0.2720  157 LYS   B CE  
1400 N  NZ  . LYS   B 148 ? 1.0745 1.4206 1.0063 0.3757  0.1383  0.2552  157 LYS   B NZ  
1401 N  N   . ASN   B 149 ? 0.7964 1.2057 0.8369 0.3687  0.2085  0.3252  158 ASN   B N   
1402 C  CA  . ASN   B 149 ? 0.7894 1.2069 0.8469 0.3726  0.2284  0.3447  158 ASN   B CA  
1403 C  C   . ASN   B 149 ? 0.7708 1.1683 0.8489 0.3422  0.2265  0.3382  158 ASN   B C   
1404 O  O   . ASN   B 149 ? 0.7825 1.1778 0.8672 0.3461  0.2420  0.3521  158 ASN   B O   
1405 C  CB  . ASN   B 149 ? 0.8488 1.2462 0.8568 0.4104  0.2389  0.3505  158 ASN   B CB  
1406 C  CG  . ASN   B 149 ? 0.9463 1.2959 0.8963 0.4222  0.2223  0.3264  158 ASN   B CG  
1407 O  OD1 . ASN   B 149 ? 0.9965 1.3331 0.9024 0.4555  0.2240  0.3273  158 ASN   B OD1 
1408 N  ND2 . ASN   B 149 ? 0.9606 1.2824 0.9088 0.3962  0.2059  0.3050  158 ASN   B ND2 
1409 N  N   . GLY   B 150 ? 0.7404 1.1226 0.8263 0.3143  0.2083  0.3178  159 GLY   B N   
1410 C  CA  . GLY   B 150 ? 0.7122 1.0730 0.8145 0.2861  0.2045  0.3092  159 GLY   B CA  
1411 C  C   . GLY   B 150 ? 0.7048 1.0194 0.7645 0.2916  0.1991  0.2928  159 GLY   B C   
1412 O  O   . GLY   B 150 ? 0.7034 0.9989 0.7728 0.2726  0.1980  0.2869  159 GLY   B O   
1413 N  N   . SER   B 151 ? 0.6945 0.9901 0.7067 0.3178  0.1950  0.2852  160 SER   B N   
1414 C  CA  A SER   B 151 ? 0.7107 0.9642 0.6827 0.3244  0.1881  0.2695  160 SER   B CA  
1415 C  CA  B SER   B 151 ? 0.7075 0.9612 0.6807 0.3235  0.1882  0.2696  160 SER   B CA  
1416 C  C   . SER   B 151 ? 0.6990 0.9279 0.6578 0.3060  0.1678  0.2443  160 SER   B C   
1417 O  O   . SER   B 151 ? 0.6936 0.9345 0.6602 0.2975  0.1584  0.2383  160 SER   B O   
1418 C  CB  A SER   B 151 ? 0.7557 0.9977 0.6827 0.3611  0.1922  0.2734  160 SER   B CB  
1419 C  CB  B SER   B 151 ? 0.7444 0.9862 0.6739 0.3601  0.1937  0.2746  160 SER   B CB  
1420 O  OG  A SER   B 151 ? 0.8216 1.0247 0.7136 0.3672  0.1852  0.2596  160 SER   B OG  
1421 O  OG  B SER   B 151 ? 0.7729 1.0264 0.6855 0.3777  0.1893  0.2749  160 SER   B OG  
1422 N  N   . TYR   B 152 ? 0.6716 0.8672 0.6104 0.3010  0.1615  0.2303  161 TYR   B N   
1423 C  CA  . TYR   B 152 ? 0.6431 0.8146 0.5701 0.2838  0.1447  0.2080  161 TYR   B CA  
1424 C  C   . TYR   B 152 ? 0.6367 0.7804 0.5180 0.3007  0.1333  0.1944  161 TYR   B C   
1425 O  O   . TYR   B 152 ? 0.6449 0.7732 0.4995 0.3217  0.1364  0.1966  161 TYR   B O   
1426 C  CB  . TYR   B 152 ? 0.6250 0.7806 0.5661 0.2644  0.1456  0.2021  161 TYR   B CB  
1427 C  CG  . TYR   B 152 ? 0.6138 0.7472 0.5474 0.2454  0.1309  0.1808  161 TYR   B CG  
1428 C  CD1 . TYR   B 152 ? 0.6047 0.7470 0.5581 0.2237  0.1232  0.1736  161 TYR   B CD1 
1429 C  CD2 . TYR   B 152 ? 0.6284 0.7329 0.5368 0.2490  0.1252  0.1685  161 TYR   B CD2 
1430 C  CE1 . TYR   B 152 ? 0.6125 0.7346 0.5569 0.2082  0.1113  0.1552  161 TYR   B CE1 
1431 C  CE2 . TYR   B 152 ? 0.6411 0.7279 0.5449 0.2319  0.1136  0.1508  161 TYR   B CE2 
1432 C  CZ  . TYR   B 152 ? 0.6344 0.7298 0.5550 0.2122  0.1074  0.1445  161 TYR   B CZ  
1433 O  OH  . TYR   B 152 ? 0.6434 0.7218 0.5585 0.1967  0.0978  0.1284  161 TYR   B OH  
1434 N  N   . VAL   B 153 ? 0.6194 0.7552 0.4914 0.2912  0.1195  0.1803  162 VAL   B N   
1435 C  CA  . VAL   B 153 ? 0.6238 0.7316 0.4559 0.3023  0.1068  0.1666  162 VAL   B CA  
1436 C  C   . VAL   B 153 ? 0.5917 0.6816 0.4261 0.2780  0.0952  0.1491  162 VAL   B C   
1437 O  O   . VAL   B 153 ? 0.5687 0.6690 0.4193 0.2613  0.0909  0.1452  162 VAL   B O   
1438 C  CB  . VAL   B 153 ? 0.6420 0.7565 0.4541 0.3201  0.1025  0.1691  162 VAL   B CB  
1439 C  CG1 . VAL   B 153 ? 0.6688 0.7492 0.4363 0.3346  0.0901  0.1567  162 VAL   B CG1 
1440 C  CG2 . VAL   B 153 ? 0.6517 0.7930 0.4696 0.3426  0.1166  0.1890  162 VAL   B CG2 
1441 N  N   . SER   B 154 ? 0.5899 0.6538 0.4079 0.2769  0.0900  0.1389  163 SER   B N   
1442 C  CA  . SER   B 154 ? 0.5808 0.6284 0.4013 0.2553  0.0809  0.1235  163 SER   B CA  
1443 C  C   . SER   B 154 ? 0.5987 0.6247 0.3894 0.2591  0.0675  0.1118  163 SER   B C   
1444 O  O   . SER   B 154 ? 0.6228 0.6352 0.3856 0.2791  0.0635  0.1122  163 SER   B O   
1445 C  CB  . SER   B 154 ? 0.5757 0.6102 0.4002 0.2508  0.0834  0.1199  163 SER   B CB  
1446 O  OG  . SER   B 154 ? 0.5730 0.5914 0.3971 0.2334  0.0750  0.1053  163 SER   B OG  
1447 N  N   . ALA   B 155 ? 0.5916 0.6114 0.3863 0.2401  0.0605  0.1013  164 ALA   B N   
1448 C  CA  . ALA   B 155 ? 0.6095 0.6061 0.3782 0.2400  0.0483  0.0903  164 ALA   B CA  
1449 C  C   . ALA   B 155 ? 0.6275 0.6028 0.3875 0.2387  0.0440  0.0825  164 ALA   B C   
1450 O  O   . ALA   B 155 ? 0.6163 0.5961 0.3940 0.2326  0.0503  0.0834  164 ALA   B O   
1451 C  CB  . ALA   B 155 ? 0.5995 0.5970 0.3770 0.2193  0.0442  0.0828  164 ALA   B CB  
1452 N  N   . ILE   B 156 ? 0.6408 0.5925 0.3744 0.2444  0.0327  0.0750  165 ILE   B N   
1453 C  CA  . ILE   B 156 ? 0.6448 0.5782 0.3746 0.2395  0.0264  0.0665  165 ILE   B CA  
1454 C  C   . ILE   B 156 ? 0.6341 0.5638 0.3744 0.2161  0.0235  0.0580  165 ILE   B C   
1455 O  O   . ILE   B 156 ? 0.6487 0.5637 0.3725 0.2134  0.0150  0.0532  165 ILE   B O   
1456 C  CB  . ILE   B 156 ? 0.6706 0.5794 0.3693 0.2559  0.0143  0.0625  165 ILE   B CB  
1457 C  CG1 . ILE   B 156 ? 0.6966 0.6081 0.3786 0.2829  0.0178  0.0715  165 ILE   B CG1 
1458 C  CG2 . ILE   B 156 ? 0.6735 0.5685 0.3761 0.2480  0.0076  0.0539  165 ILE   B CG2 
1459 C  CD1 . ILE   B 156 ? 0.7358 0.6199 0.3821 0.3020  0.0045  0.0670  165 ILE   B CD1 
1460 N  N   . THR   B 157 ? 0.6133 0.5562 0.3793 0.2005  0.0314  0.0574  166 THR   B N   
1461 C  CA  . THR   B 157 ? 0.6120 0.5531 0.3870 0.1805  0.0307  0.0503  166 THR   B CA  
1462 C  C   . THR   B 157 ? 0.6240 0.5510 0.3988 0.1719  0.0257  0.0424  166 THR   B C   
1463 O  O   . THR   B 157 ? 0.6246 0.5549 0.4130 0.1701  0.0292  0.0412  166 THR   B O   
1464 C  CB  . THR   B 157 ? 0.6019 0.5604 0.4018 0.1681  0.0400  0.0519  166 THR   B CB  
1465 O  OG1 . THR   B 157 ? 0.5924 0.5670 0.3974 0.1737  0.0439  0.0599  166 THR   B OG1 
1466 C  CG2 . THR   B 157 ? 0.6059 0.5607 0.4101 0.1501  0.0393  0.0444  166 THR   B CG2 
1467 N  N   . GLN   B 158 ? 0.6329 0.5453 0.3944 0.1661  0.0181  0.0376  167 GLN   B N   
1468 C  CA  . GLN   B 158 ? 0.6440 0.5452 0.4088 0.1562  0.0134  0.0313  167 GLN   B CA  
1469 C  C   . GLN   B 158 ? 0.6638 0.5644 0.4339 0.1384  0.0163  0.0279  167 GLN   B C   
1470 O  O   . GLN   B 158 ? 0.6554 0.5536 0.4144 0.1368  0.0159  0.0290  167 GLN   B O   
1471 C  CB  . GLN   B 158 ? 0.6548 0.5352 0.3984 0.1657  0.0004  0.0292  167 GLN   B CB  
1472 C  CG  . GLN   B 158 ? 0.6674 0.5367 0.4170 0.1554  -0.0069 0.0234  167 GLN   B CG  
1473 C  CD  . GLN   B 158 ? 0.6570 0.5372 0.4276 0.1541  -0.0037 0.0215  167 GLN   B CD  
1474 O  OE1 . GLN   B 158 ? 0.6349 0.5312 0.4245 0.1470  0.0074  0.0223  167 GLN   B OE1 
1475 N  NE2 . GLN   B 158 ? 0.6540 0.5242 0.4204 0.1612  -0.0143 0.0185  167 GLN   B NE2 
1476 N  N   . GLY   B 159 ? 0.6806 0.5842 0.4669 0.1269  0.0198  0.0242  168 GLY   B N   
1477 C  CA  . GLY   B 159 ? 0.7111 0.6136 0.5011 0.1119  0.0237  0.0217  168 GLY   B CA  
1478 C  C   . GLY   B 159 ? 0.7598 0.6459 0.5401 0.1064  0.0159  0.0205  168 GLY   B C   
1479 O  O   . GLY   B 159 ? 0.7675 0.6410 0.5371 0.1140  0.0056  0.0204  168 GLY   B O   
1480 N  N   . LYS   B 160 ? 0.7951 0.6798 0.5782 0.0934  0.0207  0.0198  169 LYS   B N   
1481 C  CA  . LYS   B 160 ? 0.8377 0.7075 0.6149 0.0851  0.0154  0.0203  169 LYS   B CA  
1482 C  C   . LYS   B 160 ? 0.8589 0.7377 0.6599 0.0740  0.0201  0.0192  169 LYS   B C   
1483 O  O   . LYS   B 160 ? 0.8541 0.7466 0.6675 0.0687  0.0315  0.0186  169 LYS   B O   
1484 C  CB  . LYS   B 160 ? 0.8782 0.7396 0.6389 0.0795  0.0189  0.0224  169 LYS   B CB  
1485 C  CG  . LYS   B 160 ? 0.9541 0.7980 0.7082 0.0700  0.0147  0.0246  169 LYS   B CG  
1486 C  CD  . LYS   B 160 ? 1.0209 0.8575 0.7599 0.0639  0.0210  0.0275  169 LYS   B CD  
1487 C  CE  . LYS   B 160 ? 1.0817 0.9006 0.8166 0.0532  0.0183  0.0314  169 LYS   B CE  
1488 N  NZ  . LYS   B 160 ? 1.1126 0.9286 0.8390 0.0454  0.0288  0.0353  169 LYS   B NZ  
1489 N  N   . ARG   B 161 ? 0.8788 0.7504 0.6863 0.0713  0.0108  0.0187  170 ARG   B N   
1490 C  CA  . ARG   B 161 ? 0.8896 0.7730 0.7232 0.0608  0.0146  0.0185  170 ARG   B CA  
1491 C  C   . ARG   B 161 ? 0.9168 0.7950 0.7510 0.0465  0.0199  0.0226  170 ARG   B C   
1492 O  O   . ARG   B 161 ? 0.9363 0.7948 0.7518 0.0443  0.0133  0.0249  170 ARG   B O   
1493 C  CB  . ARG   B 161 ? 0.9022 0.7819 0.7454 0.0635  0.0008  0.0161  170 ARG   B CB  
1494 C  CG  . ARG   B 161 ? 0.9180 0.8169 0.7924 0.0566  0.0046  0.0154  170 ARG   B CG  
1495 C  CD  . ARG   B 161 ? 0.9603 0.8538 0.8448 0.0561  -0.0117 0.0130  170 ARG   B CD  
1496 N  NE  . ARG   B 161 ? 0.9843 0.8982 0.9018 0.0465  -0.0080 0.0137  170 ARG   B NE  
1497 C  CZ  . ARG   B 161 ? 1.0032 0.9317 0.9384 0.0531  -0.0111 0.0103  170 ARG   B CZ  
1498 N  NH1 . ARG   B 161 ? 0.9995 0.9228 0.9212 0.0692  -0.0177 0.0064  170 ARG   B NH1 
1499 N  NH2 . ARG   B 161 ? 0.9890 0.9382 0.9552 0.0447  -0.0070 0.0116  170 ARG   B NH2 
1500 N  N   . GLU   B 162 ? 0.9148 0.8096 0.7685 0.0380  0.0325  0.0243  171 GLU   B N   
1501 C  CA  . GLU   B 162 ? 0.9353 0.8273 0.7902 0.0255  0.0403  0.0299  171 GLU   B CA  
1502 C  C   . GLU   B 162 ? 0.9375 0.8272 0.8109 0.0141  0.0332  0.0334  171 GLU   B C   
1503 O  O   . GLU   B 162 ? 0.9432 0.8311 0.8211 0.0024  0.0399  0.0399  171 GLU   B O   
1504 C  CB  . GLU   B 162 ? 0.9645 0.8747 0.8295 0.0231  0.0580  0.0308  171 GLU   B CB  
1505 C  CG  . GLU   B 162 ? 1.0391 0.9464 0.8827 0.0307  0.0642  0.0281  171 GLU   B CG  
1506 C  CD  . GLU   B 162 ? 1.1618 1.0501 0.9778 0.0298  0.0622  0.0309  171 GLU   B CD  
1507 O  OE1 . GLU   B 162 ? 1.1786 1.0633 0.9899 0.0223  0.0708  0.0360  171 GLU   B OE1 
1508 O  OE2 . GLU   B 162 ? 1.2089 1.0863 1.0074 0.0376  0.0527  0.0288  171 GLU   B OE2 
1509 S  S   . DMS   C .   ? 1.1670 1.0212 1.0299 0.0496  0.0709  -0.0420 201 DMS   B S   
1510 O  O   . DMS   C .   ? 1.1592 1.0307 1.0188 0.0552  0.0771  -0.0372 201 DMS   B O   
1511 C  C1  . DMS   C .   ? 1.1695 1.0092 1.0360 0.0565  0.0801  -0.0428 201 DMS   B C1  
1512 C  C2  . DMS   C .   ? 1.1514 1.0170 1.0428 0.0422  0.0663  -0.0304 201 DMS   B C2  
1513 N  N1  . A1B8T D .   ? 0.5880 0.7106 0.5985 0.1259  0.0872  0.1244  202 A1B8T B N1  
1514 N  N3  . A1B8T D .   ? 0.6230 0.6749 0.5695 0.0866  0.0517  0.0602  202 A1B8T B N3  
1515 C  C4  . A1B8T D .   ? 0.5773 0.7504 0.5984 0.1265  0.0668  0.1259  202 A1B8T B C4  
1516 C  C5  . A1B8T D .   ? 0.5779 0.7693 0.6009 0.1561  0.0876  0.1515  202 A1B8T B C5  
1517 C  C6  . A1B8T D .   ? 0.5893 0.7537 0.6029 0.1521  0.0920  0.1457  202 A1B8T B C6  
1518 C  C7  . A1B8T D .   ? 0.6120 0.7059 0.6107 0.1342  0.0999  0.1255  202 A1B8T B C7  
1519 C  C8  . A1B8T D .   ? 0.6134 0.6807 0.5969 0.1113  0.0837  0.0971  202 A1B8T B C8  
1520 C  C10 . A1B8T D .   ? 0.6072 0.6707 0.6109 0.0811  0.0717  0.0835  202 A1B8T B C10 
1521 C  C13 . A1B8T D .   ? 0.6167 0.6777 0.5775 0.1140  0.0756  0.0873  202 A1B8T B C13 
1522 C  C15 . A1B8T D .   ? 0.6198 0.6703 0.5889 0.0754  0.0547  0.0611  202 A1B8T B C15 
1523 C  C17 . A1B8T D .   ? 0.6431 0.7178 0.6129 0.1639  0.1122  0.1330  202 A1B8T B C17 
1524 C  C20 . A1B8T D .   ? 0.6485 0.7662 0.6516 0.1794  0.1323  0.1693  202 A1B8T B C20 
1525 C  C21 . A1B8T D .   ? 0.6369 0.7823 0.6766 0.1538  0.1229  0.1681  202 A1B8T B C21 
1526 C  C22 . A1B8T D .   ? 0.6409 0.7586 0.6526 0.1601  0.1210  0.1568  202 A1B8T B C22 
1527 O  O1  . A1B8T D .   ? 0.5930 0.6974 0.5589 0.1561  0.0915  0.1245  202 A1B8T B O1  
1528 C  C1  . A1B8T D .   ? 0.5966 0.7055 0.5874 0.1402  0.0932  0.1256  202 A1B8T B C1  
1529 C  C2  . A1B8T D .   ? 0.5836 0.7323 0.6048 0.1292  0.0840  0.1317  202 A1B8T B C2  
1530 C  C3  . A1B8T D .   ? 0.5906 0.7349 0.5987 0.1225  0.0707  0.1181  202 A1B8T B C3  
1531 O  O2  . A1B8T D .   ? 0.5671 0.7661 0.6109 0.1356  0.0776  0.1446  202 A1B8T B O2  
1532 N  N2  . A1B8T D .   ? 0.6176 0.6884 0.6000 0.1263  0.0930  0.1088  202 A1B8T B N2  
1533 C  C9  . A1B8T D .   ? 0.6037 0.6732 0.6101 0.0942  0.0818  0.0959  202 A1B8T B C9  
1534 C  C11 . A1B8T D .   ? 0.6152 0.6736 0.5951 0.0852  0.0649  0.0743  202 A1B8T B C11 
1535 C  C12 . A1B8T D .   ? 0.6205 0.6775 0.5802 0.1007  0.0670  0.0766  202 A1B8T B C12 
1536 C  C14 . A1B8T D .   ? 0.6251 0.6732 0.5615 0.1005  0.0588  0.0659  202 A1B8T B C14 
1537 C  C16 . A1B8T D .   ? 0.6325 0.7271 0.6253 0.1528  0.1112  0.1382  202 A1B8T B C16 
1538 C  C18 . A1B8T D .   ? 0.6460 0.7207 0.6083 0.1826  0.1217  0.1447  202 A1B8T B C18 
1539 CL CL1 . A1B8T D .   ? 0.6514 0.7017 0.5850 0.1971  0.1199  0.1369  202 A1B8T B CL1 
1540 C  C19 . A1B8T D .   ? 0.6489 0.7439 0.6255 0.1915  0.1323  0.1629  202 A1B8T B C19 
1541 N  N4  . A1B8T D .   ? 0.6463 0.7904 0.6706 0.1842  0.1416  0.1874  202 A1B8T B N4  
1542 N  N5  . A1B8T D .   ? 0.6356 0.7980 0.6842 0.1679  0.1356  0.1867  202 A1B8T B N5  
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