data_7HP9
# 
_entry.id   7HP9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HP9         pdb_00007hp9 10.2210/pdb7hp9/pdb 
WWPDB D_1001407759 ?            ?                   
# 
_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       2025-02-26 
_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                        7HP9 
_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   2024-11-07 
_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 
'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                     'PanDDA analysis group deposition' 
_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 '{2-[(3R)-piperidin-3-yl]-1,3-thiazol-4-yl}[(3S)-3-(pyridin-3-yl)pyrrolidin-1-yl]methanone' 342.458   1  ? ?    
? ? 
5 water       nat water                                                                                       18.015    50 ? ?    
? ? 
# 
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 '{2-[(3R)-piperidin-3-yl]-1,3-thiazol-4-yl}[(3S)-3-(pyridin-3-yl)pyrrolidin-1-yl]methanone' A1BGP 
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 
A1BGP non-polymer         . '{2-[(3R)-piperidin-3-yl]-1,3-thiazol-4-yl}[(3S)-3-(pyridin-3-yl)pyrrolidin-1-yl]methanone' ? 
'C18 H22 N4 O S' 342.458 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 A1BGP 1  202 301 A1BGP LIG B . 
E 5 HOH   1  101 98  HOH   HOH A . 
E 5 HOH   2  102 87  HOH   HOH A . 
E 5 HOH   3  103 20  HOH   HOH A . 
E 5 HOH   4  104 40  HOH   HOH A . 
E 5 HOH   5  105 105 HOH   HOH A . 
E 5 HOH   6  106 29  HOH   HOH A . 
E 5 HOH   7  107 119 HOH   HOH A . 
E 5 HOH   8  108 127 HOH   HOH A . 
F 5 HOH   1  301 57  HOH   HOH B . 
F 5 HOH   2  302 11  HOH   HOH B . 
F 5 HOH   3  303 14  HOH   HOH B . 
F 5 HOH   4  304 31  HOH   HOH B . 
F 5 HOH   5  305 46  HOH   HOH B . 
F 5 HOH   6  306 117 HOH   HOH B . 
F 5 HOH   7  307 32  HOH   HOH B . 
F 5 HOH   8  308 115 HOH   HOH B . 
F 5 HOH   9  309 69  HOH   HOH B . 
F 5 HOH   10 310 3   HOH   HOH B . 
F 5 HOH   11 311 124 HOH   HOH B . 
F 5 HOH   12 312 2   HOH   HOH B . 
F 5 HOH   13 313 89  HOH   HOH B . 
F 5 HOH   14 314 58  HOH   HOH B . 
F 5 HOH   15 315 35  HOH   HOH B . 
F 5 HOH   16 316 128 HOH   HOH B . 
F 5 HOH   17 317 5   HOH   HOH B . 
F 5 HOH   18 318 61  HOH   HOH B . 
F 5 HOH   19 319 103 HOH   HOH B . 
F 5 HOH   20 320 36  HOH   HOH B . 
F 5 HOH   21 321 64  HOH   HOH B . 
F 5 HOH   22 322 102 HOH   HOH B . 
F 5 HOH   23 323 28  HOH   HOH B . 
F 5 HOH   24 324 116 HOH   HOH B . 
F 5 HOH   25 325 126 HOH   HOH B . 
F 5 HOH   26 326 26  HOH   HOH B . 
F 5 HOH   27 327 18  HOH   HOH B . 
F 5 HOH   28 328 123 HOH   HOH B . 
F 5 HOH   29 329 62  HOH   HOH B . 
F 5 HOH   30 330 17  HOH   HOH B . 
F 5 HOH   31 331 49  HOH   HOH B . 
F 5 HOH   32 332 9   HOH   HOH B . 
F 5 HOH   33 333 125 HOH   HOH B . 
F 5 HOH   34 334 23  HOH   HOH B . 
F 5 HOH   35 335 92  HOH   HOH B . 
F 5 HOH   36 336 54  HOH   HOH B . 
F 5 HOH   37 337 73  HOH   HOH B . 
F 5 HOH   38 338 80  HOH   HOH B . 
F 5 HOH   39 339 72  HOH   HOH B . 
F 5 HOH   40 340 75  HOH   HOH B . 
F 5 HOH   41 341 100 HOH   HOH B . 
F 5 HOH   42 342 107 HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (26-JUL-2023)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
'data reduction' XDS     .                      ? 5 
'data reduction' XDS     .                      ? 6 
'data reduction' XDS     .                      ? 7 
'data reduction' XDS     .                      ? 8 
# 
_cell.entry_id           7HP9 
_cell.length_a           42.772 
_cell.length_b           42.772 
_cell.length_c           216.408 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HP9 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                95 
# 
_exptl.entry_id          7HP9 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.37 
_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   2023-11-20 
_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   0.92124 
_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        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HP9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             54.102 
_reflns.d_resolution_high            2.159 
_reflns.number_obs                   4837 
_reflns.percent_possible_obs         41.4 
_reflns.pdbx_Rmerge_I_obs            0.161 
_reflns.pdbx_netI_over_sigmaI        8.3 
_reflns.pdbx_redundancy              12.8 
_reflns.pdbx_Rrim_I_all              0.168 
_reflns.pdbx_Rpim_I_all              0.044 
_reflns.pdbx_number_measured_all     62137 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  2.159 
_reflns_shell.d_res_low                   2.422 
_reflns_shell.number_measured_all         4659 
_reflns_shell.number_unique_obs           242 
_reflns_shell.Rmerge_I_obs                1.111 
_reflns_shell.pdbx_redundancy             19.3 
_reflns_shell.percent_possible_obs        7.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.9 
_reflns_shell.pdbx_Rrim_I_all             1.145 
_reflns_shell.pdbx_Rpim_I_all             0.263 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HP9 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     4837 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.10 
_refine.ls_d_res_high                            2.159 
_refine.ls_percent_reflns_obs                    41.5 
_refine.ls_R_factor_obs                          0.2136 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2078 
_refine.ls_R_factor_R_free                       0.3168 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.110 
_refine.ls_number_reflns_R_free                  247 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.889 
_refine.correlation_coeff_Fo_to_Fc_free          0.811 
_refine.B_iso_mean                               41.28 
_refine.aniso_B[1][1]                            8.08260 
_refine.aniso_B[2][2]                            8.08260 
_refine.aniso_B[3][3]                            -16.16520 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.537 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HP9 
_refine_analyze.Luzzati_coordinate_error_obs    0.41 
_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.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               1554 
_refine_hist.d_res_high                       2.159 
_refine_hist.d_res_low                        54.10 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.008 ? 2.00  1557 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.96  ? 2.00  2116 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  542  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  269  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1530 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           2.80  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           19.84 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  194  'X-RAY DIFFRACTION' SEMIHARMONIC 
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      ?     ? 4.00  1116 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   13 
_refine_ls_shell.d_res_high                       2.16 
_refine_ls_shell.d_res_low                        2.54 
_refine_ls_shell.number_reflns_R_work             380 
_refine_ls_shell.R_factor_R_work                  0.2584 
_refine_ls_shell.percent_reflns_obs               9.30 
_refine_ls_shell.R_factor_R_free                  0.3561 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.94 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_all                404 
_refine_ls_shell.R_factor_all                     0.2657 
# 
_struct.entry_id                  7HP9 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0015097-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP9 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, 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 7HP9 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP9 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 7HP9 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP9 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP9 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP9 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              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)' 4230  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  10330 ? 
# 
_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 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 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 TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O ILE B 106 ? O ILE B 115 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
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                   7HP9 
_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     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU B 30  ? ? -110.71 -154.79 
2 1 LYS B 54  ? ? 55.05   15.05   
3 1 CYS B 80  ? ? 76.46   -24.81  
4 1 ALA B 127 ? ? -101.32 76.37   
5 1 ALA B 132 ? ? -39.08  -35.23  
# 
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[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -13.4531 -2.1256 -19.1630 -0.0418 0.0061 -0.3853 0.1670 0.1549 0.1201 4.5744 3.8711 3.5287 -1.8945 
0.2899 1.5630 0.3835 0.3702 0.1596 -0.4936 -0.2571 -0.5196 -0.5053 0.4010 -0.1264 
'X-RAY DIFFRACTION' 2 ? refined -18.3272 0.4291  -15.6738 0.1627  0.0182 -0.2371 0.2169 0.0577 0.0613 0.6802 1.4044 3.6062 -0.8534 
0.9935 0.3007 0.3509 0.2146 0.1858 -0.2034 -0.3389 0.0236  -0.0482 0.1128 -0.0120 
# 
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.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
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 
A1BGP N1   N N N 1   
A1BGP N3   N N N 2   
A1BGP C4   C Y N 3   
A1BGP C5   C N S 4   
A1BGP C6   C N N 5   
A1BGP C7   C N N 6   
A1BGP C8   C N N 7   
A1BGP C10  C N N 8   
A1BGP C13  C Y N 9   
A1BGP C15  C Y N 10  
A1BGP C17  C Y N 11  
A1BGP O1   O N N 12  
A1BGP C1   C N N 13  
A1BGP C2   C Y N 14  
A1BGP C3   C Y N 15  
A1BGP S1   S Y N 16  
A1BGP C9   C N N 17  
A1BGP N2   N Y N 18  
A1BGP C11  C N N 19  
A1BGP C12  C N R 20  
A1BGP C14  C Y N 21  
A1BGP C16  C Y N 22  
A1BGP N4   N Y N 23  
A1BGP C18  C N N 24  
A1BGP H9   H N N 25  
A1BGP H2   H N N 26  
A1BGP H4   H N N 27  
A1BGP H3   H N N 28  
A1BGP H5   H N N 29  
A1BGP H6   H N N 30  
A1BGP H7   H N N 31  
A1BGP H8   H N N 32  
A1BGP H13  H N N 33  
A1BGP H12  H N N 34  
A1BGP H18  H N N 35  
A1BGP H20  H N N 36  
A1BGP H1   H N N 37  
A1BGP H10  H N N 38  
A1BGP H11  H N N 39  
A1BGP H15  H N N 40  
A1BGP H14  H N N 41  
A1BGP H16  H N N 42  
A1BGP H17  H N N 43  
A1BGP H19  H N N 44  
A1BGP H22  H N N 45  
A1BGP H21  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
DMS   S    S N N 134 
DMS   O    O N N 135 
DMS   C1   C N N 136 
DMS   C2   C N N 137 
DMS   H11  H N N 138 
DMS   H12  H N N 139 
DMS   H13  H N N 140 
DMS   H21  H N N 141 
DMS   H22  H N N 142 
DMS   H23  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
HIS   N    N N N 193 
HIS   CA   C N S 194 
HIS   C    C N N 195 
HIS   O    O N N 196 
HIS   CB   C N N 197 
HIS   CG   C Y N 198 
HIS   ND1  N Y N 199 
HIS   CD2  C Y N 200 
HIS   CE1  C Y N 201 
HIS   NE2  N Y N 202 
HIS   OXT  O N N 203 
HIS   H    H N N 204 
HIS   H2   H N N 205 
HIS   HA   H N N 206 
HIS   HB2  H N N 207 
HIS   HB3  H N N 208 
HIS   HD1  H N N 209 
HIS   HD2  H N N 210 
HIS   HE1  H N N 211 
HIS   HE2  H N N 212 
HIS   HXT  H N N 213 
HOH   O    O N N 214 
HOH   H1   H N N 215 
HOH   H2   H N N 216 
ILE   N    N N N 217 
ILE   CA   C N S 218 
ILE   C    C N N 219 
ILE   O    O N N 220 
ILE   CB   C N S 221 
ILE   CG1  C N N 222 
ILE   CG2  C N N 223 
ILE   CD1  C N N 224 
ILE   OXT  O N N 225 
ILE   H    H N N 226 
ILE   H2   H N N 227 
ILE   HA   H N N 228 
ILE   HB   H N N 229 
ILE   HG12 H N N 230 
ILE   HG13 H N N 231 
ILE   HG21 H N N 232 
ILE   HG22 H N N 233 
ILE   HG23 H N N 234 
ILE   HD11 H N N 235 
ILE   HD12 H N N 236 
ILE   HD13 H N N 237 
ILE   HXT  H N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
THR   N    N N N 360 
THR   CA   C N S 361 
THR   C    C N N 362 
THR   O    O N N 363 
THR   CB   C N R 364 
THR   OG1  O N N 365 
THR   CG2  C N N 366 
THR   OXT  O N N 367 
THR   H    H N N 368 
THR   H2   H N N 369 
THR   HA   H N N 370 
THR   HB   H N N 371 
THR   HG1  H N N 372 
THR   HG21 H N N 373 
THR   HG22 H N N 374 
THR   HG23 H N N 375 
THR   HXT  H N N 376 
TRP   N    N N N 377 
TRP   CA   C N S 378 
TRP   C    C N N 379 
TRP   O    O N N 380 
TRP   CB   C N N 381 
TRP   CG   C Y N 382 
TRP   CD1  C Y N 383 
TRP   CD2  C Y N 384 
TRP   NE1  N Y N 385 
TRP   CE2  C Y N 386 
TRP   CE3  C Y N 387 
TRP   CZ2  C Y N 388 
TRP   CZ3  C Y N 389 
TRP   CH2  C Y N 390 
TRP   OXT  O N N 391 
TRP   H    H N N 392 
TRP   H2   H N N 393 
TRP   HA   H N N 394 
TRP   HB2  H N N 395 
TRP   HB3  H N N 396 
TRP   HD1  H N N 397 
TRP   HE1  H N N 398 
TRP   HE3  H N N 399 
TRP   HZ2  H N N 400 
TRP   HZ3  H N N 401 
TRP   HH2  H N N 402 
TRP   HXT  H N N 403 
TYR   N    N N N 404 
TYR   CA   C N S 405 
TYR   C    C N N 406 
TYR   O    O N N 407 
TYR   CB   C N N 408 
TYR   CG   C Y N 409 
TYR   CD1  C Y N 410 
TYR   CD2  C Y N 411 
TYR   CE1  C Y N 412 
TYR   CE2  C Y N 413 
TYR   CZ   C Y N 414 
TYR   OH   O N N 415 
TYR   OXT  O N N 416 
TYR   H    H N N 417 
TYR   H2   H N N 418 
TYR   HA   H N N 419 
TYR   HB2  H N N 420 
TYR   HB3  H N N 421 
TYR   HD1  H N N 422 
TYR   HD2  H N N 423 
TYR   HE1  H N N 424 
TYR   HE2  H N N 425 
TYR   HH   H N N 426 
TYR   HXT  H N N 427 
VAL   N    N N N 428 
VAL   CA   C N S 429 
VAL   C    C N N 430 
VAL   O    O N N 431 
VAL   CB   C N N 432 
VAL   CG1  C N N 433 
VAL   CG2  C N N 434 
VAL   OXT  O N N 435 
VAL   H    H N N 436 
VAL   H2   H N N 437 
VAL   HA   H N N 438 
VAL   HB   H N N 439 
VAL   HG11 H N N 440 
VAL   HG12 H N N 441 
VAL   HG13 H N N 442 
VAL   HG21 H N N 443 
VAL   HG22 H N N 444 
VAL   HG23 H N N 445 
VAL   HXT  H N N 446 
# 
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 
A1BGP O1  C1   doub N N 1   
A1BGP C1  C2   sing N N 2   
A1BGP C2  C3   doub Y N 3   
A1BGP C3  S1   sing Y N 4   
A1BGP S1  C4   sing Y N 5   
A1BGP C4  C5   sing N N 6   
A1BGP C5  C6   sing N N 7   
A1BGP C6  C7   sing N N 8   
A1BGP C7  C8   sing N N 9   
A1BGP C8  N1   sing N N 10  
A1BGP N1  C9   sing N N 11  
A1BGP C4  N2   doub Y N 12  
A1BGP C1  N3   sing N N 13  
A1BGP N3  C10  sing N N 14  
A1BGP C10 C11  sing N N 15  
A1BGP C11 C12  sing N N 16  
A1BGP C12 C13  sing N N 17  
A1BGP C13 C14  doub Y N 18  
A1BGP C14 C15  sing Y N 19  
A1BGP C15 C16  doub Y N 20  
A1BGP C16 N4   sing Y N 21  
A1BGP N4  C17  doub Y N 22  
A1BGP C12 C18  sing N N 23  
A1BGP C2  N2   sing Y N 24  
A1BGP N3  C18  sing N N 25  
A1BGP C5  C9   sing N N 26  
A1BGP C13 C17  sing Y N 27  
A1BGP N1  H9   sing N N 28  
A1BGP C5  H2   sing N N 29  
A1BGP C6  H4   sing N N 30  
A1BGP C6  H3   sing N N 31  
A1BGP C7  H5   sing N N 32  
A1BGP C7  H6   sing N N 33  
A1BGP C8  H7   sing N N 34  
A1BGP C8  H8   sing N N 35  
A1BGP C10 H13  sing N N 36  
A1BGP C10 H12  sing N N 37  
A1BGP C15 H18  sing N N 38  
A1BGP C17 H20  sing N N 39  
A1BGP C3  H1   sing N N 40  
A1BGP C9  H10  sing N N 41  
A1BGP C9  H11  sing N N 42  
A1BGP C11 H15  sing N N 43  
A1BGP C11 H14  sing N N 44  
A1BGP C12 H16  sing N N 45  
A1BGP C14 H17  sing N N 46  
A1BGP C16 H19  sing N N 47  
A1BGP C18 H22  sing N N 48  
A1BGP C18 H21  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
DMS   S   O    doub N N 132 
DMS   S   C1   sing N N 133 
DMS   S   C2   sing N N 134 
DMS   C1  H11  sing N N 135 
DMS   C1  H12  sing N N 136 
DMS   C1  H13  sing N N 137 
DMS   C2  H21  sing N N 138 
DMS   C2  H22  sing N N 139 
DMS   C2  H23  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
_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_1002322 
_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         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HP9 
_atom_sites.fract_transf_matrix[1][1]   0.023380 
_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]   0.023380 
_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 
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   ? -21.953 19.258  -6.991  1.00 44.34 ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.726 18.041  -7.249  1.00 44.63 ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.441 17.446  -8.637  1.00 44.08 ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.025 18.153  -9.562  1.00 44.22 ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -24.250 18.287  -7.061  1.00 46.64 ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.880 17.615  -5.838  1.00 51.03 ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.535 18.010  -4.694  1.00 51.49 ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.732 16.708  -6.027  1.00 52.76 ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.653 16.132  -8.757  1.00 43.26 ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.498 15.386  -10.000 1.00 42.99 ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.885 15.050  -10.541 1.00 42.44 ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.841 14.943  -9.769  1.00 42.33 ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.713 14.085  -9.777  1.00 43.76 ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.264 14.290  -9.403  1.00 46.05 ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.408 12.695  -9.308  1.00 50.32 ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.740 13.237  -9.032  1.00 49.42 ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.998 14.877  -11.867 1.00 41.82 ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.273 14.577  -12.512 1.00 41.66 ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.112 13.589  -13.674 1.00 41.98 ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.039 13.515  -14.272 1.00 42.49 ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.970 15.873  -12.973 1.00 41.37 ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.250 16.607  -14.082 1.00 42.03 ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.292 17.571  -13.798 1.00 42.90 ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.558 16.369  -15.416 1.00 42.76 ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.629 18.252  -14.816 1.00 43.72 ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.890 17.030  -16.441 1.00 43.41 ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.941 17.987  -16.138 1.00 44.31 ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.276 18.642  -17.147 1.00 45.45 ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.181 12.847  -14.017 1.00 41.36 ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.131 11.874  -15.108 1.00 40.92 ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.881 12.377  -16.377 1.00 41.97 ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.783 13.216  -16.260 1.00 42.31 ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.597 10.475  -14.626 1.00 39.82 ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.092 10.444  -14.321 1.00 39.60 ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.798 10.038  -13.421 1.00 40.01 ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.644 9.077   -14.164 1.00 40.06 ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.472 11.889  -17.581 1.00 42.18 ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.044 12.266  -18.895 1.00 43.05 ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.057 11.051  -19.831 1.00 43.64 ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -25.992 10.503  -20.072 1.00 44.07 ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.178 13.356  -19.566 1.00 45.00 ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.570 14.784  -19.236 1.00 49.42 ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.837 15.855  -20.023 1.00 55.29 ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -25.204 15.526  -21.052 1.00 56.81 ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.913 17.036  -19.614 1.00 57.03 ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.212 10.659  -20.405 1.00 43.48 ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.250 9.479   -21.283 1.00 44.02 ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.294 9.563   -22.474 1.00 45.07 ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.107 10.640  -23.039 1.00 45.83 ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.672 9.150   -21.754 1.00 44.57 ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -29.882 7.650   -21.918 1.00 45.93 ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.332 7.291   -22.144 1.00 47.41 ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.508 5.858   -22.383 1.00 49.01 ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.390 5.279   -23.574 1.00 51.62 ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.068 5.997   -24.643 1.00 51.77 ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.571 3.973   -23.703 1.00 51.84 ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.683 8.422   -22.848 1.00 45.01 ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.728 8.334   -23.953 1.00 45.47 ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.105 7.299   -25.032 1.00 45.75 ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.559 7.346   -26.132 1.00 46.61 ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.339 8.046   -23.412 1.00 45.71 ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.023 6.387   -24.727 1.00 45.35 ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.456 5.390   -25.699 1.00 45.53 ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.044 4.122   -25.119 1.00 45.61 ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.109 3.961   -23.902 1.00 45.47 ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.504 3.217   -25.989 1.00 45.46 ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.066 1.941   -25.555 1.00 46.04 ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.955 0.948   -25.307 1.00 46.40 ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.855 1.126   -25.828 1.00 46.37 ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -29.936 1.342   -26.666 1.00 47.71 ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.164 2.119   -27.031 1.00 52.48 ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.444 3.129   -26.360 1.00 52.68 ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -31.847 1.723   -28.005 1.00 55.30 ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.254 -0.145  -24.588 1.00 46.29 ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.285 -1.217  -24.419 1.00 46.59 ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.684 -2.334  -25.391 1.00 47.37 ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.545 -3.158  -25.071 1.00 47.08 ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.228 -1.716  -22.983 1.00 46.66 ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -27.023 -0.555  -22.004 1.00 47.79 ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.145 -2.747  -22.859 1.00 46.75 ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -27.668 -0.790  -20.625 1.00 49.05 ? 59  ILE   A CD1 1 
ATOM   82   N N   . THR   A 1 17  ? -27.105 -2.310  -26.606 1.00 48.08 ? 60  THR   A N   1 
ATOM   83   C CA  . THR   A 1 17  ? -27.400 -3.262  -27.676 1.00 49.68 ? 60  THR   A CA  1 
ATOM   84   C C   . THR   A 1 17  ? -26.122 -3.774  -28.365 1.00 50.95 ? 60  THR   A C   1 
ATOM   85   O O   . THR   A 1 17  ? -25.170 -3.011  -28.524 1.00 50.93 ? 60  THR   A O   1 
ATOM   86   C CB  . THR   A 1 17  ? -28.296 -2.576  -28.726 1.00 51.48 ? 60  THR   A CB  1 
ATOM   87   O OG1 . THR   A 1 17  ? -27.627 -1.419  -29.255 1.00 52.19 ? 60  THR   A OG1 1 
ATOM   88   C CG2 . THR   A 1 17  ? -29.677 -2.190  -28.173 1.00 52.15 ? 60  THR   A CG2 1 
ATOM   89   N N   . TRP   A 1 18  ? -26.104 -5.045  -28.796 1.00 52.09 ? 61  TRP   A N   1 
ATOM   90   C CA  . TRP   A 1 18  ? -24.955 -5.578  -29.530 1.00 54.20 ? 61  TRP   A CA  1 
ATOM   91   C C   . TRP   A 1 18  ? -25.081 -5.084  -30.981 1.00 57.17 ? 61  TRP   A C   1 
ATOM   92   O O   . TRP   A 1 18  ? -26.137 -5.253  -31.598 1.00 57.31 ? 61  TRP   A O   1 
ATOM   93   C CB  . TRP   A 1 18  ? -24.943 -7.117  -29.485 1.00 53.99 ? 61  TRP   A CB  1 
ATOM   94   C CG  . TRP   A 1 18  ? -23.854 -7.769  -30.296 1.00 54.52 ? 61  TRP   A CG  1 
ATOM   95   C CD1 . TRP   A 1 18  ? -23.910 -8.123  -31.615 1.00 55.28 ? 61  TRP   A CD1 1 
ATOM   96   C CD2 . TRP   A 1 18  ? -22.578 -8.215  -29.816 1.00 54.64 ? 61  TRP   A CD2 1 
ATOM   97   N NE1 . TRP   A 1 18  ? -22.731 -8.717  -31.995 1.00 55.49 ? 61  TRP   A NE1 1 
ATOM   98   C CE2 . TRP   A 1 18  ? -21.896 -8.785  -30.910 1.00 55.45 ? 61  TRP   A CE2 1 
ATOM   99   C CE3 . TRP   A 1 18  ? -21.919 -8.128  -28.587 1.00 54.99 ? 61  TRP   A CE3 1 
ATOM   100  C CZ2 . TRP   A 1 18  ? -20.607 -9.301  -30.793 1.00 56.18 ? 61  TRP   A CZ2 1 
ATOM   101  C CZ3 . TRP   A 1 18  ? -20.662 -8.675  -28.463 1.00 55.80 ? 61  TRP   A CZ3 1 
ATOM   102  C CH2 . TRP   A 1 18  ? -20.009 -9.232  -29.560 1.00 56.14 ? 61  TRP   A CH2 1 
ATOM   103  N N   . GLU   A 1 19  ? -24.023 -4.463  -31.524 1.00 59.07 ? 62  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 19  ? -24.070 -3.940  -32.885 1.00 61.24 ? 62  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 19  ? -23.142 -4.686  -33.806 1.00 63.04 ? 62  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 19  ? -21.929 -4.560  -33.666 1.00 63.08 ? 62  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 19  ? -23.725 -2.444  -32.910 1.00 64.23 ? 62  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 19  ? -24.640 -1.572  -32.060 1.00 69.46 ? 62  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 19  ? -26.081 -1.463  -32.524 1.00 76.01 ? 62  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 19  ? -26.327 -0.952  -33.645 1.00 77.49 ? 62  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 19  ? -26.969 -1.886  -31.751 1.00 77.66 ? 62  GLU   A OE2 1 
ATOM   112  N N   . LYS   A 1 20  ? -23.705 -5.433  -34.775 1.00 64.40 ? 63  LYS   A N   1 
ATOM   113  C CA  . LYS   A 1 20  ? -22.922 -6.191  -35.757 1.00 66.10 ? 63  LYS   A CA  1 
ATOM   114  C C   . LYS   A 1 20  ? -22.065 -5.246  -36.590 1.00 67.29 ? 63  LYS   A C   1 
ATOM   115  O O   . LYS   A 1 20  ? -22.441 -4.092  -36.790 1.00 67.58 ? 63  LYS   A O   1 
ATOM   116  C CB  . LYS   A 1 20  ? -23.850 -6.935  -36.727 1.00 68.77 ? 63  LYS   A CB  1 
ATOM   117  C CG  . LYS   A 1 20  ? -24.686 -8.066  -36.145 1.00 73.71 ? 63  LYS   A CG  1 
ATOM   118  C CD  . LYS   A 1 20  ? -25.315 -8.863  -37.314 1.00 78.23 ? 63  LYS   A CD  1 
ATOM   119  C CE  . LYS   A 1 20  ? -26.386 -9.844  -36.893 1.00 81.97 ? 63  LYS   A CE  1 
ATOM   120  N NZ  . LYS   A 1 20  ? -27.708 -9.184  -36.707 1.00 84.15 ? 63  LYS   A NZ  1 
ATOM   121  N N   . ASP   A 1 21  ? -20.948 -5.747  -37.123 1.00 68.06 ? 64  ASP   A N   1 
ATOM   122  C CA  . ASP   A 1 21  ? -20.050 -4.960  -37.975 1.00 69.50 ? 64  ASP   A CA  1 
ATOM   123  C C   . ASP   A 1 21  ? -19.450 -3.757  -37.256 1.00 69.59 ? 64  ASP   A C   1 
ATOM   124  O O   . ASP   A 1 21  ? -19.397 -2.650  -37.806 1.00 70.00 ? 64  ASP   A O   1 
ATOM   125  C CB  . ASP   A 1 21  ? -20.714 -4.541  -39.300 1.00 72.43 ? 64  ASP   A CB  1 
ATOM   126  C CG  . ASP   A 1 21  ? -20.984 -5.687  -40.249 1.00 80.22 ? 64  ASP   A CG  1 
ATOM   127  O OD1 . ASP   A 1 21  ? -20.103 -6.569  -40.380 1.00 82.15 ? 64  ASP   A OD1 1 
ATOM   128  O OD2 . ASP   A 1 21  ? -22.062 -5.685  -40.890 1.00 83.21 ? 64  ASP   A OD2 1 
ATOM   129  N N   . ALA   A 1 22  ? -19.015 -3.982  -36.018 1.00 68.95 ? 65  ALA   A N   1 
ATOM   130  C CA  . ALA   A 1 22  ? -18.360 -2.964  -35.208 1.00 68.86 ? 65  ALA   A CA  1 
ATOM   131  C C   . ALA   A 1 22  ? -16.831 -3.075  -35.408 1.00 68.75 ? 65  ALA   A C   1 
ATOM   132  O O   . ALA   A 1 22  ? -16.348 -4.097  -35.902 1.00 68.50 ? 65  ALA   A O   1 
ATOM   133  C CB  . ALA   A 1 22  ? -18.721 -3.165  -33.744 1.00 68.88 ? 65  ALA   A CB  1 
ATOM   134  N N   . GLU   A 1 23  ? -16.074 -2.030  -35.036 1.00 68.70 ? 66  GLU   A N   1 
ATOM   135  C CA  . GLU   A 1 23  ? -14.611 -2.014  -35.179 1.00 68.99 ? 66  GLU   A CA  1 
ATOM   136  C C   . GLU   A 1 23  ? -13.933 -3.080  -34.296 1.00 67.45 ? 66  GLU   A C   1 
ATOM   137  O O   . GLU   A 1 23  ? -13.933 -2.936  -33.078 1.00 67.17 ? 66  GLU   A O   1 
ATOM   138  C CB  . GLU   A 1 23  ? -14.068 -0.615  -34.824 1.00 73.04 ? 66  GLU   A CB  1 
ATOM   139  C CG  . GLU   A 1 23  ? -12.561 -0.463  -34.973 1.00 79.92 ? 66  GLU   A CG  1 
ATOM   140  C CD  . GLU   A 1 23  ? -11.973 0.782   -34.334 1.00 87.21 ? 66  GLU   A CD  1 
ATOM   141  O OE1 . GLU   A 1 23  ? -12.753 1.677   -33.930 1.00 88.45 ? 66  GLU   A OE1 1 
ATOM   142  O OE2 . GLU   A 1 23  ? -10.726 0.861   -34.237 1.00 89.30 ? 66  GLU   A OE2 1 
ATOM   143  N N   . VAL   A 1 24  ? -13.354 -4.137  -34.904 1.00 66.13 ? 67  VAL   A N   1 
ATOM   144  C CA  . VAL   A 1 24  ? -12.710 -5.204  -34.131 1.00 65.49 ? 67  VAL   A CA  1 
ATOM   145  C C   . VAL   A 1 24  ? -11.221 -4.943  -33.893 1.00 65.16 ? 67  VAL   A C   1 
ATOM   146  O O   . VAL   A 1 24  ? -10.422 -5.071  -34.809 1.00 65.62 ? 67  VAL   A O   1 
ATOM   147  C CB  . VAL   A 1 24  ? -12.943 -6.630  -34.694 1.00 65.57 ? 67  VAL   A CB  1 
ATOM   148  C CG1 . VAL   A 1 24  ? -12.626 -7.675  -33.629 1.00 66.06 ? 67  VAL   A CG1 1 
ATOM   149  C CG2 . VAL   A 1 24  ? -14.371 -6.809  -35.209 1.00 65.62 ? 67  VAL   A CG2 1 
ATOM   150  N N   . THR   A 1 25  ? -10.848 -4.614  -32.656 1.00 64.46 ? 68  THR   A N   1 
ATOM   151  C CA  . THR   A 1 25  ? -9.461  -4.329  -32.280 1.00 64.12 ? 68  THR   A CA  1 
ATOM   152  C C   . THR   A 1 25  ? -9.152  -4.833  -30.847 1.00 63.36 ? 68  THR   A C   1 
ATOM   153  O O   . THR   A 1 25  ? -10.058 -5.200  -30.113 1.00 63.04 ? 68  THR   A O   1 
ATOM   154  C CB  . THR   A 1 25  ? -9.181  -2.816  -32.428 1.00 65.45 ? 68  THR   A CB  1 
ATOM   155  O OG1 . THR   A 1 25  ? -7.796  -2.582  -32.182 1.00 66.69 ? 68  THR   A OG1 1 
ATOM   156  C CG2 . THR   A 1 25  ? -9.999  -1.972  -31.461 1.00 65.47 ? 68  THR   A CG2 1 
ATOM   157  N N   . GLY   A 1 26  ? -7.877  -4.857  -30.472 1.00 62.87 ? 69  GLY   A N   1 
ATOM   158  C CA  . GLY   A 1 26  ? -7.468  -5.280  -29.144 1.00 62.76 ? 69  GLY   A CA  1 
ATOM   159  C C   . GLY   A 1 26  ? -7.007  -6.716  -29.055 1.00 62.32 ? 69  GLY   A C   1 
ATOM   160  O O   . GLY   A 1 26  ? -7.733  -7.636  -29.432 1.00 62.43 ? 69  GLY   A O   1 
ATOM   161  N N   . ASN   A 1 27  ? -5.801  -6.915  -28.523 1.00 61.60 ? 70  ASN   A N   1 
ATOM   162  C CA  . ASN   A 1 27  ? -5.226  -8.245  -28.310 1.00 61.07 ? 70  ASN   A CA  1 
ATOM   163  C C   . ASN   A 1 27  ? -5.834  -8.917  -27.026 1.00 58.95 ? 70  ASN   A C   1 
ATOM   164  O O   . ASN   A 1 27  ? -6.592  -8.268  -26.313 1.00 59.30 ? 70  ASN   A O   1 
ATOM   165  C CB  . ASN   A 1 27  ? -3.695  -8.129  -28.220 1.00 63.01 ? 70  ASN   A CB  1 
ATOM   166  C CG  . ASN   A 1 27  ? -3.235  -7.466  -26.944 1.00 66.81 ? 70  ASN   A CG  1 
ATOM   167  O OD1 . ASN   A 1 27  ? -3.579  -6.314  -26.660 1.00 68.38 ? 70  ASN   A OD1 1 
ATOM   168  N ND2 . ASN   A 1 27  ? -2.466  -8.187  -26.140 1.00 67.19 ? 70  ASN   A ND2 1 
ATOM   169  N N   . SER   A 1 28  ? -5.514  -10.199 -26.744 1.00 56.81 ? 71  SER   A N   1 
ATOM   170  C CA  . SER   A 1 28  ? -6.053  -10.925 -25.579 1.00 55.48 ? 71  SER   A CA  1 
ATOM   171  C C   . SER   A 1 28  ? -4.924  -11.456 -24.668 1.00 53.71 ? 71  SER   A C   1 
ATOM   172  O O   . SER   A 1 28  ? -4.565  -12.637 -24.756 1.00 53.85 ? 71  SER   A O   1 
ATOM   173  C CB  . SER   A 1 28  ? -6.920  -12.100 -26.034 1.00 56.64 ? 71  SER   A CB  1 
ATOM   174  O OG  . SER   A 1 28  ? -7.672  -11.836 -27.205 1.00 58.68 ? 71  SER   A OG  1 
ATOM   175  N N   . PRO   A 1 29  ? -4.347  -10.617 -23.784 1.00 51.89 ? 72  PRO   A N   1 
ATOM   176  C CA  . PRO   A 1 29  ? -3.211  -11.095 -22.961 1.00 50.61 ? 72  PRO   A CA  1 
ATOM   177  C C   . PRO   A 1 29  ? -3.553  -11.848 -21.673 1.00 48.81 ? 72  PRO   A C   1 
ATOM   178  O O   . PRO   A 1 29  ? -4.591  -11.584 -21.088 1.00 48.31 ? 72  PRO   A O   1 
ATOM   179  C CB  . PRO   A 1 29  ? -2.430  -9.811  -22.657 1.00 51.41 ? 72  PRO   A CB  1 
ATOM   180  C CG  . PRO   A 1 29  ? -3.433  -8.693  -22.793 1.00 52.11 ? 72  PRO   A CG  1 
ATOM   181  C CD  . PRO   A 1 29  ? -4.632  -9.184  -23.561 1.00 50.95 ? 72  PRO   A CD  1 
ATOM   182  N N   . ARG   A 1 30  ? -2.666  -12.774 -21.225 1.00 47.91 ? 73  ARG   A N   1 
ATOM   183  C CA  . ARG   A 1 30  ? -2.794  -13.498 -19.936 1.00 47.49 ? 73  ARG   A CA  1 
ATOM   184  C C   . ARG   A 1 30  ? -1.762  -12.889 -18.971 1.00 45.31 ? 73  ARG   A C   1 
ATOM   185  O O   . ARG   A 1 30  ? -0.571  -13.174 -19.085 1.00 45.22 ? 73  ARG   A O   1 
ATOM   186  C CB  . ARG   A 1 30  ? -2.526  -15.009 -20.075 1.00 50.13 ? 73  ARG   A CB  1 
ATOM   187  C CG  . ARG   A 1 30  ? -3.638  -15.813 -20.746 1.00 55.67 ? 73  ARG   A CG  1 
ATOM   188  C CD  . ARG   A 1 30  ? -3.264  -17.291 -20.771 1.00 61.27 ? 73  ARG   A CD  1 
ATOM   189  N NE  . ARG   A 1 30  ? -4.105  -18.093 -21.668 1.00 65.96 ? 73  ARG   A NE  1 
ATOM   190  C CZ  . ARG   A 1 30  ? -5.056  -18.930 -21.256 1.00 69.42 ? 73  ARG   A CZ  1 
ATOM   191  N NH1 . ARG   A 1 30  ? -5.309  -19.075 -19.958 1.00 69.45 ? 73  ARG   A NH1 1 
ATOM   192  N NH2 . ARG   A 1 30  ? -5.763  -19.625 -22.137 1.00 69.51 ? 73  ARG   A NH2 1 
ATOM   193  N N   . LEU   A 1 31  ? -2.209  -12.023 -18.060 1.00 43.59 ? 74  LEU   A N   1 
ATOM   194  C CA  . LEU   A 1 31  ? -1.314  -11.312 -17.145 1.00 42.59 ? 74  LEU   A CA  1 
ATOM   195  C C   . LEU   A 1 31  ? -1.449  -11.784 -15.703 1.00 41.80 ? 74  LEU   A C   1 
ATOM   196  O O   . LEU   A 1 31  ? -2.562  -11.821 -15.195 1.00 41.75 ? 74  LEU   A O   1 
ATOM   197  C CB  . LEU   A 1 31  ? -1.623  -9.804  -17.172 1.00 42.31 ? 74  LEU   A CB  1 
ATOM   198  C CG  . LEU   A 1 31  ? -1.901  -9.177  -18.517 1.00 43.02 ? 74  LEU   A CG  1 
ATOM   199  C CD1 . LEU   A 1 31  ? -2.542  -7.844  -18.359 1.00 43.43 ? 74  LEU   A CD1 1 
ATOM   200  C CD2 . LEU   A 1 31  ? -0.653  -9.086  -19.329 1.00 43.61 ? 74  LEU   A CD2 1 
ATOM   201  N N   . ASP   A 1 32  ? -0.328  -12.066 -15.020 1.00 41.00 ? 75  ASP   A N   1 
ATOM   202  C CA  . ASP   A 1 32  ? -0.388  -12.460 -13.614 1.00 41.00 ? 75  ASP   A CA  1 
ATOM   203  C C   . ASP   A 1 32  ? -0.519  -11.193 -12.766 1.00 40.39 ? 75  ASP   A C   1 
ATOM   204  O O   . ASP   A 1 32  ? 0.442   -10.437 -12.664 1.00 40.40 ? 75  ASP   A O   1 
ATOM   205  C CB  . ASP   A 1 32  ? 0.855   -13.269 -13.214 1.00 42.96 ? 75  ASP   A CB  1 
ATOM   206  C CG  . ASP   A 1 32  ? 0.633   -14.769 -13.251 1.00 47.34 ? 75  ASP   A CG  1 
ATOM   207  O OD1 . ASP   A 1 32  ? 0.056   -15.305 -12.287 1.00 47.35 ? 75  ASP   A OD1 1 
ATOM   208  O OD2 . ASP   A 1 32  ? 1.028   -15.402 -14.253 1.00 50.34 ? 75  ASP   A OD2 1 
ATOM   209  N N   . VAL   A 1 33  ? -1.717  -10.930 -12.203 1.00 39.72 ? 76  VAL   A N   1 
ATOM   210  C CA  . VAL   A 1 33  ? -1.960  -9.703  -11.437 1.00 39.73 ? 76  VAL   A CA  1 
ATOM   211  C C   . VAL   A 1 33  ? -2.352  -9.941  -9.941  1.00 39.76 ? 76  VAL   A C   1 
ATOM   212  O O   . VAL   A 1 33  ? -2.602  -11.074 -9.532  1.00 39.71 ? 76  VAL   A O   1 
ATOM   213  C CB  . VAL   A 1 33  ? -3.008  -8.810  -12.154 1.00 40.27 ? 76  VAL   A CB  1 
ATOM   214  C CG1 . VAL   A 1 33  ? -2.692  -8.622  -13.637 1.00 40.77 ? 76  VAL   A CG1 1 
ATOM   215  C CG2 . VAL   A 1 33  ? -4.402  -9.370  -11.960 1.00 40.83 ? 76  VAL   A CG2 1 
ATOM   216  N N   . ALA   A 1 34  ? -2.358  -8.858  -9.129  1.00 39.59 ? 77  ALA   A N   1 
ATOM   217  C CA  . ALA   A 1 34  ? -2.748  -8.839  -7.714  1.00 39.73 ? 77  ALA   A CA  1 
ATOM   218  C C   . ALA   A 1 34  ? -3.761  -7.702  -7.454  1.00 39.66 ? 77  ALA   A C   1 
ATOM   219  O O   . ALA   A 1 34  ? -3.752  -6.688  -8.157  1.00 40.07 ? 77  ALA   A O   1 
ATOM   220  C CB  . ALA   A 1 34  ? -1.528  -8.658  -6.829  1.00 39.77 ? 77  ALA   A CB  1 
ATOM   221  N N   . LEU   A 1 35  ? -4.657  -7.884  -6.474  1.00 38.68 ? 78  LEU   A N   1 
ATOM   222  C CA  . LEU   A 1 35  ? -5.662  -6.867  -6.168  1.00 38.18 ? 78  LEU   A CA  1 
ATOM   223  C C   . LEU   A 1 35  ? -5.522  -6.466  -4.704  1.00 38.32 ? 78  LEU   A C   1 
ATOM   224  O O   . LEU   A 1 35  ? -5.637  -7.309  -3.798  1.00 38.53 ? 78  LEU   A O   1 
ATOM   225  C CB  . LEU   A 1 35  ? -7.071  -7.379  -6.498  1.00 37.82 ? 78  LEU   A CB  1 
ATOM   226  C CG  . LEU   A 1 35  ? -8.215  -6.428  -6.210  1.00 38.52 ? 78  LEU   A CG  1 
ATOM   227  C CD1 . LEU   A 1 35  ? -8.109  -5.183  -7.047  1.00 38.98 ? 78  LEU   A CD1 1 
ATOM   228  C CD2 . LEU   A 1 35  ? -9.545  -7.104  -6.438  1.00 38.85 ? 78  LEU   A CD2 1 
ATOM   229  N N   . ASP   A 1 36  ? -5.178  -5.196  -4.473  1.00 37.81 ? 79  ASP   A N   1 
ATOM   230  C CA  . ASP   A 1 36  ? -4.941  -4.725  -3.120  1.00 37.66 ? 79  ASP   A CA  1 
ATOM   231  C C   . ASP   A 1 36  ? -6.254  -4.333  -2.401  1.00 37.14 ? 79  ASP   A C   1 
ATOM   232  O O   . ASP   A 1 36  ? -7.312  -4.232  -3.035  1.00 37.15 ? 79  ASP   A O   1 
ATOM   233  C CB  . ASP   A 1 36  ? -3.856  -3.614  -3.094  1.00 39.41 ? 79  ASP   A CB  1 
ATOM   234  C CG  . ASP   A 1 36  ? -4.285  -2.204  -3.460  1.00 44.25 ? 79  ASP   A CG  1 
ATOM   235  O OD1 . ASP   A 1 36  ? -5.459  -2.017  -3.810  1.00 45.77 ? 79  ASP   A OD1 1 
ATOM   236  O OD2 . ASP   A 1 36  ? -3.446  -1.278  -3.360  1.00 45.78 ? 79  ASP   A OD2 1 
ATOM   237  N N   . GLU   A 1 37  ? -6.180  -4.139  -1.074  1.00 36.35 ? 80  GLU   A N   1 
ATOM   238  C CA  . GLU   A 1 37  ? -7.329  -3.752  -0.256  1.00 36.23 ? 80  GLU   A CA  1 
ATOM   239  C C   . GLU   A 1 37  ? -7.999  -2.445  -0.751  1.00 35.70 ? 80  GLU   A C   1 
ATOM   240  O O   . GLU   A 1 37  ? -9.168  -2.217  -0.471  1.00 35.60 ? 80  GLU   A O   1 
ATOM   241  C CB  . GLU   A 1 37  ? -6.904  -3.632  1.222   1.00 37.93 ? 80  GLU   A CB  1 
ATOM   242  C CG  . GLU   A 1 37  ? -8.055  -3.403  2.191   1.00 42.29 ? 80  GLU   A CG  1 
ATOM   243  C CD  . GLU   A 1 37  ? -7.652  -3.050  3.614   1.00 46.17 ? 80  GLU   A CD  1 
ATOM   244  O OE1 . GLU   A 1 37  ? -8.005  -1.941  4.079   1.00 45.82 ? 80  GLU   A OE1 1 
ATOM   245  O OE2 . GLU   A 1 37  ? -6.971  -3.879  4.259   1.00 48.10 ? 80  GLU   A OE2 1 
ATOM   246  N N   . SER   A 1 38  ? -7.275  -1.616  -1.515  1.00 34.92 ? 81  SER   A N   1 
ATOM   247  C CA  . SER   A 1 38  ? -7.777  -0.349  -2.025  1.00 34.59 ? 81  SER   A CA  1 
ATOM   248  C C   . SER   A 1 38  ? -8.340  -0.405  -3.431  1.00 34.38 ? 81  SER   A C   1 
ATOM   249  O O   . SER   A 1 38  ? -8.546  0.650   -4.017  1.00 35.05 ? 81  SER   A O   1 
ATOM   250  C CB  . SER   A 1 38  ? -6.680  0.703   -1.968  1.00 35.99 ? 81  SER   A CB  1 
ATOM   251  O OG  . SER   A 1 38  ? -6.218  0.866   -0.634  1.00 38.69 ? 81  SER   A OG  1 
ATOM   252  N N   . GLY   A 1 39  ? -8.553  -1.598  -3.985  1.00 33.55 ? 82  GLY   A N   1 
ATOM   253  C CA  . GLY   A 1 39  ? -9.096  -1.747  -5.335  1.00 33.15 ? 82  GLY   A CA  1 
ATOM   254  C C   . GLY   A 1 39  ? -8.123  -1.513  -6.482  1.00 32.65 ? 82  GLY   A C   1 
ATOM   255  O O   . GLY   A 1 39  ? -8.529  -1.500  -7.648  1.00 32.41 ? 82  GLY   A O   1 
ATOM   256  N N   . ASP   A 1 40  ? -6.830  -1.327  -6.172  1.00 32.21 ? 83  ASP   A N   1 
ATOM   257  C CA  . ASP   A 1 40  ? -5.789  -1.112  -7.177  1.00 32.27 ? 83  ASP   A CA  1 
ATOM   258  C C   . ASP   A 1 40  ? -5.280  -2.460  -7.715  1.00 32.51 ? 83  ASP   A C   1 
ATOM   259  O O   . ASP   A 1 40  ? -4.998  -3.377  -6.935  1.00 32.31 ? 83  ASP   A O   1 
ATOM   260  C CB  . ASP   A 1 40  ? -4.592  -0.335  -6.582  1.00 33.36 ? 83  ASP   A CB  1 
ATOM   261  C CG  . ASP   A 1 40  ? -4.854  1.103   -6.180  1.00 37.44 ? 83  ASP   A CG  1 
ATOM   262  O OD1 . ASP   A 1 40  ? -5.224  1.899   -7.050  1.00 37.41 ? 83  ASP   A OD1 1 
ATOM   263  O OD2 . ASP   A 1 40  ? -4.646  1.437   -4.993  1.00 40.93 ? 83  ASP   A OD2 1 
ATOM   264  N N   . PHE   A 1 41  ? -5.128  -2.569  -9.043  1.00 32.64 ? 84  PHE   A N   1 
ATOM   265  C CA  . PHE   A 1 41  ? -4.594  -3.780  -9.646  1.00 33.38 ? 84  PHE   A CA  1 
ATOM   266  C C   . PHE   A 1 41  ? -3.103  -3.582  -9.870  1.00 35.35 ? 84  PHE   A C   1 
ATOM   267  O O   . PHE   A 1 41  ? -2.681  -2.564  -10.409 1.00 35.30 ? 84  PHE   A O   1 
ATOM   268  C CB  . PHE   A 1 41  ? -5.281  -4.092  -10.973 1.00 32.63 ? 84  PHE   A CB  1 
ATOM   269  C CG  . PHE   A 1 41  ? -6.585  -4.840  -10.869 1.00 32.42 ? 84  PHE   A CG  1 
ATOM   270  C CD1 . PHE   A 1 41  ? -6.604  -6.193  -10.593 1.00 32.85 ? 84  PHE   A CD1 1 
ATOM   271  C CD2 . PHE   A 1 41  ? -7.790  -4.197  -11.084 1.00 32.52 ? 84  PHE   A CD2 1 
ATOM   272  C CE1 . PHE   A 1 41  ? -7.803  -6.882  -10.517 1.00 33.13 ? 84  PHE   A CE1 1 
ATOM   273  C CE2 . PHE   A 1 41  ? -8.987  -4.890  -11.002 1.00 32.77 ? 84  PHE   A CE2 1 
ATOM   274  C CZ  . PHE   A 1 41  ? -8.985  -6.225  -10.722 1.00 32.53 ? 84  PHE   A CZ  1 
ATOM   275  N N   . SER   A 1 42  ? -2.306  -4.542  -9.409  1.00 36.89 ? 85  SER   A N   1 
ATOM   276  C CA  . SER   A 1 42  ? -0.849  -4.541  -9.518  1.00 38.46 ? 85  SER   A CA  1 
ATOM   277  C C   . SER   A 1 42  ? -0.417  -5.652  -10.480 1.00 40.01 ? 85  SER   A C   1 
ATOM   278  O O   . SER   A 1 42  ? -1.119  -6.654  -10.620 1.00 39.96 ? 85  SER   A O   1 
ATOM   279  C CB  . SER   A 1 42  ? -0.216  -4.813  -8.151  1.00 39.84 ? 85  SER   A CB  1 
ATOM   280  O OG  . SER   A 1 42  ? -0.831  -4.130  -7.065  1.00 42.07 ? 85  SER   A OG  1 
ATOM   281  N N   . LEU   A 1 43  ? 0.740   -5.491  -11.130 1.00 41.12 ? 86  LEU   A N   1 
ATOM   282  C CA  . LEU   A 1 43  ? 1.265   -6.532  -12.002 1.00 42.62 ? 86  LEU   A CA  1 
ATOM   283  C C   . LEU   A 1 43  ? 2.284   -7.339  -11.206 1.00 44.84 ? 86  LEU   A C   1 
ATOM   284  O O   . LEU   A 1 43  ? 3.161   -6.764  -10.552 1.00 45.01 ? 86  LEU   A O   1 
ATOM   285  C CB  . LEU   A 1 43  ? 1.905   -5.927  -13.228 1.00 42.65 ? 86  LEU   A CB  1 
ATOM   286  C CG  . LEU   A 1 43  ? 1.258   -6.331  -14.512 1.00 44.11 ? 86  LEU   A CG  1 
ATOM   287  C CD1 . LEU   A 1 43  ? 1.512   -5.312  -15.570 1.00 44.60 ? 86  LEU   A CD1 1 
ATOM   288  C CD2 . LEU   A 1 43  ? 1.724   -7.705  -14.937 1.00 44.94 ? 86  LEU   A CD2 1 
ATOM   289  N N   . VAL   A 1 44  ? 2.134   -8.670  -11.211 1.00 46.14 ? 87  VAL   A N   1 
ATOM   290  C CA  . VAL   A 1 44  ? 3.006   -9.584  -10.470 1.00 47.55 ? 87  VAL   A CA  1 
ATOM   291  C C   . VAL   A 1 44  ? 4.096   -10.119 -11.391 1.00 48.99 ? 87  VAL   A C   1 
ATOM   292  O O   . VAL   A 1 44  ? 3.794   -10.582 -12.493 1.00 49.21 ? 87  VAL   A O   1 
ATOM   293  C CB  . VAL   A 1 44  ? 2.185   -10.736 -9.844  1.00 48.18 ? 87  VAL   A CB  1 
ATOM   294  C CG1 . VAL   A 1 44  ? 3.072   -11.662 -9.020  1.00 48.80 ? 87  VAL   A CG1 1 
ATOM   295  C CG2 . VAL   A 1 44  ? 1.043   -10.191 -9.001  1.00 48.51 ? 87  VAL   A CG2 1 
ATOM   296  N N   . GLU   A 1 45  ? 5.359   -10.034 -10.959 1.00 49.86 ? 88  GLU   A N   1 
ATOM   297  C CA  . GLU   A 1 45  ? 6.484   -10.512 -11.754 1.00 51.42 ? 88  GLU   A CA  1 
ATOM   298  C C   . GLU   A 1 45  ? 7.553   -11.165 -10.867 1.00 52.27 ? 88  GLU   A C   1 
ATOM   299  O O   . GLU   A 1 45  ? 8.470   -11.811 -11.380 1.00 52.67 ? 88  GLU   A O   1 
ATOM   300  C CB  . GLU   A 1 45  ? 7.088   -9.364  -12.586 1.00 54.53 ? 88  GLU   A CB  1 
ATOM   301  C CG  . GLU   A 1 45  ? 6.404   -9.126  -13.925 1.00 60.53 ? 88  GLU   A CG  1 
ATOM   302  C CD  . GLU   A 1 45  ? 7.201   -9.555  -15.140 1.00 67.54 ? 88  GLU   A CD  1 
ATOM   303  O OE1 . GLU   A 1 45  ? 8.247   -10.226 -14.972 1.00 68.75 ? 88  GLU   A OE1 1 
ATOM   304  O OE2 . GLU   A 1 45  ? 6.779   -9.207  -16.267 1.00 70.26 ? 88  GLU   A OE2 1 
ATOM   305  N N   . GLY   B 2 7   ? -36.063 11.571  -11.397 1.00 60.15 ? 16  GLY   B N   1 
ATOM   306  C CA  . GLY   B 2 7   ? -36.417 12.043  -12.729 1.00 60.77 ? 16  GLY   B CA  1 
ATOM   307  C C   . GLY   B 2 7   ? -36.255 10.994  -13.819 1.00 61.13 ? 16  GLY   B C   1 
ATOM   308  O O   . GLY   B 2 7   ? -36.970 9.983   -13.821 1.00 61.67 ? 16  GLY   B O   1 
ATOM   309  N N   . GLU   B 2 8   ? -35.316 11.230  -14.770 1.00 60.27 ? 17  GLU   B N   1 
ATOM   310  C CA  . GLU   B 2 8   ? -35.042 10.298  -15.866 1.00 59.83 ? 17  GLU   B CA  1 
ATOM   311  C C   . GLU   B 2 8   ? -34.447 8.971   -15.354 1.00 58.38 ? 17  GLU   B C   1 
ATOM   312  O O   . GLU   B 2 8   ? -33.321 8.943   -14.855 1.00 58.45 ? 17  GLU   B O   1 
ATOM   313  C CB  . GLU   B 2 8   ? -34.108 10.937  -16.907 1.00 62.70 ? 17  GLU   B CB  1 
ATOM   314  C CG  . GLU   B 2 8   ? -33.789 10.012  -18.070 1.00 68.43 ? 17  GLU   B CG  1 
ATOM   315  C CD  . GLU   B 2 8   ? -32.802 10.545  -19.092 1.00 75.65 ? 17  GLU   B CD  1 
ATOM   316  O OE1 . GLU   B 2 8   ? -32.132 11.567  -18.814 1.00 76.71 ? 17  GLU   B OE1 1 
ATOM   317  O OE2 . GLU   B 2 8   ? -32.715 9.944   -20.186 1.00 78.68 ? 17  GLU   B OE2 1 
ATOM   318  N N   . THR   B 2 9   ? -35.215 7.879   -15.473 1.00 56.75 ? 18  THR   B N   1 
ATOM   319  C CA  . THR   B 2 9   ? -34.778 6.552   -15.030 1.00 55.56 ? 18  THR   B CA  1 
ATOM   320  C C   . THR   B 2 9   ? -34.800 5.489   -16.137 1.00 53.37 ? 18  THR   B C   1 
ATOM   321  O O   . THR   B 2 9   ? -34.627 4.304   -15.840 1.00 53.85 ? 18  THR   B O   1 
ATOM   322  C CB  . THR   B 2 9   ? -35.611 6.090   -13.833 1.00 57.37 ? 18  THR   B CB  1 
ATOM   323  O OG1 . THR   B 2 9   ? -36.997 6.150   -14.192 1.00 58.77 ? 18  THR   B OG1 1 
ATOM   324  C CG2 . THR   B 2 9   ? -35.346 6.924   -12.587 1.00 57.81 ? 18  THR   B CG2 1 
ATOM   325  N N   . THR   B 2 10  ? -35.010 5.901   -17.395 1.00 50.69 ? 19  THR   B N   1 
ATOM   326  C CA  . THR   B 2 10  ? -35.066 5.015   -18.548 1.00 48.73 ? 19  THR   B CA  1 
ATOM   327  C C   . THR   B 2 10  ? -33.790 4.163   -18.662 1.00 46.13 ? 19  THR   B C   1 
ATOM   328  O O   . THR   B 2 10  ? -32.687 4.667   -18.472 1.00 46.29 ? 19  THR   B O   1 
ATOM   329  C CB  . THR   B 2 10  ? -35.397 5.859   -19.807 1.00 50.00 ? 19  THR   B CB  1 
ATOM   330  O OG1 . THR   B 2 10  ? -36.807 6.095   -19.851 1.00 50.96 ? 19  THR   B OG1 1 
ATOM   331  C CG2 . THR   B 2 10  ? -34.942 5.213   -21.109 1.00 50.29 ? 19  THR   B CG2 1 
ATOM   332  N N   . ASP   B 2 11  ? -33.952 2.863   -18.930 1.00 43.65 ? 20  ASP   B N   1 
ATOM   333  C CA  . ASP   B 2 11  ? -32.851 1.919   -19.104 1.00 41.66 ? 20  ASP   B CA  1 
ATOM   334  C C   . ASP   B 2 11  ? -31.837 2.421   -20.161 1.00 38.91 ? 20  ASP   B C   1 
ATOM   335  O O   . ASP   B 2 11  ? -32.234 3.112   -21.097 1.00 38.68 ? 20  ASP   B O   1 
ATOM   336  C CB  . ASP   B 2 11  ? -33.430 0.564   -19.551 1.00 43.59 ? 20  ASP   B CB  1 
ATOM   337  C CG  . ASP   B 2 11  ? -33.325 -0.540  -18.522 1.00 49.00 ? 20  ASP   B CG  1 
ATOM   338  O OD1 . ASP   B 2 11  ? -33.774 -0.326  -17.368 1.00 49.34 ? 20  ASP   B OD1 1 
ATOM   339  O OD2 . ASP   B 2 11  ? -32.794 -1.623  -18.867 1.00 51.62 ? 20  ASP   B OD2 1 
ATOM   340  N N   . GLY   B 2 12  ? -30.555 2.089   -19.998 1.00 36.52 ? 21  GLY   B N   1 
ATOM   341  C CA  . GLY   B 2 12  ? -29.530 2.489   -20.959 1.00 34.76 ? 21  GLY   B CA  1 
ATOM   342  C C   . GLY   B 2 12  ? -28.182 2.849   -20.368 1.00 32.86 ? 21  GLY   B C   1 
ATOM   343  O O   . GLY   B 2 12  ? -27.940 2.620   -19.190 1.00 32.71 ? 21  GLY   B O   1 
ATOM   344  N N   . VAL   B 2 13  ? -27.280 3.395   -21.188 1.00 31.52 ? 22  VAL   B N   1 
ATOM   345  C CA  . VAL   B 2 13  ? -25.955 3.825   -20.737 1.00 30.83 ? 22  VAL   B CA  1 
ATOM   346  C C   . VAL   B 2 13  ? -25.969 5.341   -20.545 1.00 30.94 ? 22  VAL   B C   1 
ATOM   347  O O   . VAL   B 2 13  ? -26.612 6.052   -21.316 1.00 31.31 ? 22  VAL   B O   1 
ATOM   348  C CB  . VAL   B 2 13  ? -24.809 3.343   -21.652 1.00 30.94 ? 22  VAL   B CB  1 
ATOM   349  C CG1 . VAL   B 2 13  ? -24.817 4.065   -23.002 1.00 31.59 ? 22  VAL   B CG1 1 
ATOM   350  C CG2 . VAL   B 2 13  ? -23.460 3.485   -20.963 1.00 30.77 ? 22  VAL   B CG2 1 
ATOM   351  N N   . TYR   B 2 14  ? -25.346 5.830   -19.462 1.00 30.47 ? 23  TYR   B N   1 
ATOM   352  C CA  . TYR   B 2 14  ? -25.367 7.242   -19.087 1.00 30.23 ? 23  TYR   B CA  1 
ATOM   353  C C   . TYR   B 2 14  ? -23.974 7.813   -18.852 1.00 31.36 ? 23  TYR   B C   1 
ATOM   354  O O   . TYR   B 2 14  ? -23.079 7.091   -18.434 1.00 32.14 ? 23  TYR   B O   1 
ATOM   355  C CB  . TYR   B 2 14  ? -26.164 7.396   -17.780 1.00 29.03 ? 23  TYR   B CB  1 
ATOM   356  C CG  . TYR   B 2 14  ? -27.661 7.348   -17.965 1.00 28.15 ? 23  TYR   B CG  1 
ATOM   357  C CD1 . TYR   B 2 14  ? -28.297 6.174   -18.333 1.00 28.34 ? 23  TYR   B CD1 1 
ATOM   358  C CD2 . TYR   B 2 14  ? -28.446 8.463   -17.725 1.00 28.43 ? 23  TYR   B CD2 1 
ATOM   359  C CE1 . TYR   B 2 14  ? -29.665 6.132   -18.543 1.00 29.00 ? 23  TYR   B CE1 1 
ATOM   360  C CE2 . TYR   B 2 14  ? -29.819 8.431   -17.920 1.00 29.19 ? 23  TYR   B CE2 1 
ATOM   361  C CZ  . TYR   B 2 14  ? -30.426 7.261   -18.331 1.00 29.94 ? 23  TYR   B CZ  1 
ATOM   362  O OH  . TYR   B 2 14  ? -31.777 7.216   -18.551 1.00 31.57 ? 23  TYR   B OH  1 
ATOM   363  N N   . ARG   B 2 15  ? -23.807 9.120   -19.044 1.00 31.26 ? 24  ARG   B N   1 
ATOM   364  C CA  . ARG   B 2 15  ? -22.544 9.797   -18.778 1.00 31.63 ? 24  ARG   B CA  1 
ATOM   365  C C   . ARG   B 2 15  ? -22.663 10.388  -17.396 1.00 32.25 ? 24  ARG   B C   1 
ATOM   366  O O   . ARG   B 2 15  ? -23.697 10.971  -17.071 1.00 32.48 ? 24  ARG   B O   1 
ATOM   367  C CB  . ARG   B 2 15  ? -22.297 10.973  -19.749 1.00 32.59 ? 24  ARG   B CB  1 
ATOM   368  C CG  . ARG   B 2 15  ? -22.311 10.676  -21.249 1.00 34.34 ? 24  ARG   B CG  1 
ATOM   369  C CD  . ARG   B 2 15  ? -21.958 11.967  -21.981 1.00 37.44 ? 24  ARG   B CD  1 
ATOM   370  N NE  . ARG   B 2 15  ? -22.192 11.894  -23.424 1.00 39.37 ? 24  ARG   B NE  1 
ATOM   371  C CZ  . ARG   B 2 15  ? -21.290 11.488  -24.309 1.00 40.89 ? 24  ARG   B CZ  1 
ATOM   372  N NH1 . ARG   B 2 15  ? -20.071 11.136  -23.913 1.00 40.67 ? 24  ARG   B NH1 1 
ATOM   373  N NH2 . ARG   B 2 15  ? -21.594 11.443  -25.601 1.00 39.89 ? 24  ARG   B NH2 1 
ATOM   374  N N   . VAL   B 2 16  ? -21.594 10.296  -16.602 1.00 32.39 ? 25  VAL   B N   1 
ATOM   375  C CA  . VAL   B 2 16  ? -21.518 10.885  -15.267 1.00 32.85 ? 25  VAL   B CA  1 
ATOM   376  C C   . VAL   B 2 16  ? -20.679 12.172  -15.386 1.00 33.52 ? 25  VAL   B C   1 
ATOM   377  O O   . VAL   B 2 16  ? -19.499 12.109  -15.737 1.00 33.65 ? 25  VAL   B O   1 
ATOM   378  C CB  . VAL   B 2 16  ? -20.920 9.879   -14.263 1.00 33.36 ? 25  VAL   B CB  1 
ATOM   379  C CG1 . VAL   B 2 16  ? -20.850 10.471  -12.865 1.00 33.65 ? 25  VAL   B CG1 1 
ATOM   380  C CG2 . VAL   B 2 16  ? -21.722 8.589   -14.258 1.00 33.91 ? 25  VAL   B CG2 1 
ATOM   381  N N   . MET   B 2 17  ? -21.310 13.336  -15.168 1.00 33.78 ? 26  MET   B N   1 
ATOM   382  C CA  . MET   B 2 17  ? -20.680 14.645  -15.326 1.00 34.91 ? 26  MET   B CA  1 
ATOM   383  C C   . MET   B 2 17  ? -20.543 15.421  -14.000 1.00 37.06 ? 26  MET   B C   1 
ATOM   384  O O   . MET   B 2 17  ? -21.092 15.005  -12.988 1.00 37.07 ? 26  MET   B O   1 
ATOM   385  C CB  . MET   B 2 17  ? -21.529 15.494  -16.292 1.00 34.95 ? 26  MET   B CB  1 
ATOM   386  C CG  . MET   B 2 17  ? -21.917 14.810  -17.581 1.00 35.75 ? 26  MET   B CG  1 
ATOM   387  S SD  . MET   B 2 17  ? -20.544 14.628  -18.728 1.00 35.82 ? 26  MET   B SD  1 
ATOM   388  C CE  . MET   B 2 17  ? -20.084 16.324  -18.974 1.00 33.06 ? 26  MET   B CE  1 
ATOM   389  N N   . THR   B 2 18  ? -19.839 16.575  -14.025 1.00 38.83 ? 27  THR   B N   1 
ATOM   390  C CA  . THR   B 2 18  ? -19.687 17.491  -12.895 1.00 41.03 ? 27  THR   B CA  1 
ATOM   391  C C   . THR   B 2 18  ? -19.444 18.955  -13.335 1.00 43.76 ? 27  THR   B C   1 
ATOM   392  O O   . THR   B 2 18  ? -18.935 19.217  -14.422 1.00 43.23 ? 27  THR   B O   1 
ATOM   393  C CB  . THR   B 2 18  ? -18.616 17.018  -11.907 1.00 41.96 ? 27  THR   B CB  1 
ATOM   394  O OG1 . THR   B 2 18  ? -18.552 17.962  -10.833 1.00 43.34 ? 27  THR   B OG1 1 
ATOM   395  C CG2 . THR   B 2 18  ? -17.248 16.865  -12.547 1.00 41.78 ? 27  THR   B CG2 1 
ATOM   396  N N   . ARG   B 2 19  ? -19.769 19.908  -12.458 1.00 46.26 ? 28  ARG   B N   1 
ATOM   397  C CA  . ARG   B 2 19  ? -19.534 21.332  -12.730 1.00 48.73 ? 28  ARG   B CA  1 
ATOM   398  C C   . ARG   B 2 19  ? -18.538 21.983  -11.711 1.00 50.24 ? 28  ARG   B C   1 
ATOM   399  O O   . ARG   B 2 19  ? -18.374 23.207  -11.695 1.00 49.99 ? 28  ARG   B O   1 
ATOM   400  C CB  . ARG   B 2 19  ? -20.866 22.103  -12.800 1.00 50.89 ? 28  ARG   B CB  1 
ATOM   401  C CG  . ARG   B 2 19  ? -21.796 21.631  -13.912 1.00 55.00 ? 28  ARG   B CG  1 
ATOM   402  C CD  . ARG   B 2 19  ? -22.737 22.744  -14.344 1.00 59.55 ? 28  ARG   B CD  1 
ATOM   403  N NE  . ARG   B 2 19  ? -23.434 22.443  -15.599 1.00 63.07 ? 28  ARG   B NE  1 
ATOM   404  C CZ  . ARG   B 2 19  ? -24.727 22.138  -15.683 1.00 65.56 ? 28  ARG   B CZ  1 
ATOM   405  N NH1 . ARG   B 2 19  ? -25.481 22.094  -14.586 1.00 65.38 ? 28  ARG   B NH1 1 
ATOM   406  N NH2 . ARG   B 2 19  ? -25.278 21.874  -16.863 1.00 65.00 ? 28  ARG   B NH2 1 
ATOM   407  N N   . ARG   B 2 20  ? -17.852 21.142  -10.898 1.00 51.53 ? 29  ARG   B N   1 
ATOM   408  C CA  . ARG   B 2 20  ? -16.880 21.511  -9.858  1.00 53.18 ? 29  ARG   B CA  1 
ATOM   409  C C   . ARG   B 2 20  ? -15.571 22.107  -10.448 1.00 53.97 ? 29  ARG   B C   1 
ATOM   410  O O   . ARG   B 2 20  ? -14.883 22.897  -9.790  1.00 54.24 ? 29  ARG   B O   1 
ATOM   411  C CB  . ARG   B 2 20  ? -16.574 20.257  -9.017  1.00 55.34 ? 29  ARG   B CB  1 
ATOM   412  C CG  . ARG   B 2 20  ? -15.850 20.500  -7.702  1.00 60.16 ? 29  ARG   B CG  1 
ATOM   413  C CD  . ARG   B 2 20  ? -15.316 19.193  -7.130  1.00 64.82 ? 29  ARG   B CD  1 
ATOM   414  N NE  . ARG   B 2 20  ? -14.153 18.694  -7.871  1.00 69.13 ? 29  ARG   B NE  1 
ATOM   415  C CZ  . ARG   B 2 20  ? -12.950 18.489  -7.334  1.00 72.30 ? 29  ARG   B CZ  1 
ATOM   416  N NH1 . ARG   B 2 20  ? -12.743 18.717  -6.040  1.00 72.31 ? 29  ARG   B NH1 1 
ATOM   417  N NH2 . ARG   B 2 20  ? -11.950 18.036  -8.082  1.00 72.57 ? 29  ARG   B NH2 1 
ATOM   418  N N   . LEU   B 2 21  ? -15.238 21.726  -11.687 1.00 53.93 ? 30  LEU   B N   1 
ATOM   419  C CA  . LEU   B 2 21  ? -14.032 22.188  -12.366 1.00 54.39 ? 30  LEU   B CA  1 
ATOM   420  C C   . LEU   B 2 21  ? -14.402 23.137  -13.545 1.00 54.13 ? 30  LEU   B C   1 
ATOM   421  O O   . LEU   B 2 21  ? -15.458 23.769  -13.492 1.00 54.21 ? 30  LEU   B O   1 
ATOM   422  C CB  . LEU   B 2 21  ? -13.196 20.965  -12.819 1.00 55.10 ? 30  LEU   B CB  1 
ATOM   423  C CG  . LEU   B 2 21  ? -12.364 20.272  -11.749 1.00 57.24 ? 30  LEU   B CG  1 
ATOM   424  C CD1 . LEU   B 2 21  ? -13.135 19.137  -11.108 1.00 57.95 ? 30  LEU   B CD1 1 
ATOM   425  C CD2 . LEU   B 2 21  ? -11.078 19.737  -12.339 1.00 58.21 ? 30  LEU   B CD2 1 
ATOM   426  N N   . LEU   B 2 22  ? -13.549 23.262  -14.580 1.00 53.63 ? 31  LEU   B N   1 
ATOM   427  C CA  . LEU   B 2 22  ? -13.806 24.159  -15.700 1.00 53.91 ? 31  LEU   B CA  1 
ATOM   428  C C   . LEU   B 2 22  ? -14.945 23.686  -16.598 1.00 54.36 ? 31  LEU   B C   1 
ATOM   429  O O   . LEU   B 2 22  ? -14.782 22.710  -17.332 1.00 54.93 ? 31  LEU   B O   1 
ATOM   430  C CB  . LEU   B 2 22  ? -12.539 24.332  -16.520 1.00 53.74 ? 31  LEU   B CB  1 
ATOM   431  C CG  . LEU   B 2 22  ? -12.567 25.511  -17.445 1.00 54.38 ? 31  LEU   B CG  1 
ATOM   432  C CD1 . LEU   B 2 22  ? -12.034 26.745  -16.756 1.00 54.45 ? 31  LEU   B CD1 1 
ATOM   433  C CD2 . LEU   B 2 22  ? -11.794 25.207  -18.692 1.00 55.04 ? 31  LEU   B CD2 1 
ATOM   434  N N   . GLY   B 2 23  ? -16.073 24.398  -16.544 1.00 53.70 ? 32  GLY   B N   1 
ATOM   435  C CA  . GLY   B 2 23  ? -17.277 24.048  -17.289 1.00 53.33 ? 32  GLY   B CA  1 
ATOM   436  C C   . GLY   B 2 23  ? -17.796 22.678  -16.886 1.00 52.39 ? 32  GLY   B C   1 
ATOM   437  O O   . GLY   B 2 23  ? -17.650 22.276  -15.730 1.00 52.56 ? 32  GLY   B O   1 
ATOM   438  N N   . SER   B 2 24  ? -18.367 21.930  -17.837 1.00 51.15 ? 33  SER   B N   1 
ATOM   439  C CA  . SER   B 2 24  ? -18.831 20.571  -17.569 1.00 50.04 ? 33  SER   B CA  1 
ATOM   440  C C   . SER   B 2 24  ? -17.681 19.619  -17.906 1.00 48.44 ? 33  SER   B C   1 
ATOM   441  O O   . SER   B 2 24  ? -17.000 19.810  -18.924 1.00 48.59 ? 33  SER   B O   1 
ATOM   442  C CB  . SER   B 2 24  ? -20.056 20.243  -18.419 1.00 51.49 ? 33  SER   B CB  1 
ATOM   443  O OG  . SER   B 2 24  ? -21.049 21.251  -18.317 1.00 53.84 ? 33  SER   B OG  1 
ATOM   444  N N   . THR   B 2 25  ? -17.448 18.613  -17.052 1.00 46.73 ? 34  THR   B N   1 
ATOM   445  C CA  . THR   B 2 25  ? -16.356 17.654  -17.235 1.00 45.77 ? 34  THR   B CA  1 
ATOM   446  C C   . THR   B 2 25  ? -16.846 16.219  -17.006 1.00 44.34 ? 34  THR   B C   1 
ATOM   447  O O   . THR   B 2 25  ? -17.427 15.946  -15.959 1.00 44.10 ? 34  THR   B O   1 
ATOM   448  C CB  . THR   B 2 25  ? -15.217 17.975  -16.246 1.00 46.95 ? 34  THR   B CB  1 
ATOM   449  O OG1 . THR   B 2 25  ? -14.757 19.317  -16.444 1.00 47.69 ? 34  THR   B OG1 1 
ATOM   450  C CG2 . THR   B 2 25  ? -14.056 16.995  -16.349 1.00 47.40 ? 34  THR   B CG2 1 
ATOM   451  N N   . GLN   B 2 26  ? -16.605 15.298  -17.965 1.00 43.04 ? 35  GLN   B N   1 
ATOM   452  C CA  . GLN   B 2 26  ? -17.031 13.902  -17.789 1.00 42.13 ? 35  GLN   B CA  1 
ATOM   453  C C   . GLN   B 2 26  ? -16.079 13.121  -16.873 1.00 41.51 ? 35  GLN   B C   1 
ATOM   454  O O   . GLN   B 2 26  ? -14.927 12.897  -17.257 1.00 42.40 ? 35  GLN   B O   1 
ATOM   455  C CB  . GLN   B 2 26  ? -17.175 13.176  -19.136 1.00 42.31 ? 35  GLN   B CB  1 
ATOM   456  C CG  . GLN   B 2 26  ? -17.722 11.767  -18.987 1.00 44.09 ? 35  GLN   B CG  1 
ATOM   457  C CD  . GLN   B 2 26  ? -18.044 11.134  -20.309 1.00 48.07 ? 35  GLN   B CD  1 
ATOM   458  O OE1 . GLN   B 2 26  ? -18.834 11.642  -21.098 1.00 49.91 ? 35  GLN   B OE1 1 
ATOM   459  N NE2 . GLN   B 2 26  ? -17.452 9.996   -20.583 1.00 48.76 ? 35  GLN   B NE2 1 
ATOM   460  N N   . VAL   B 2 27  ? -16.552 12.696  -15.682 1.00 39.50 ? 36  VAL   B N   1 
ATOM   461  C CA  . VAL   B 2 27  ? -15.726 11.931  -14.748 1.00 38.19 ? 36  VAL   B CA  1 
ATOM   462  C C   . VAL   B 2 27  ? -15.797 10.402  -14.986 1.00 36.27 ? 36  VAL   B C   1 
ATOM   463  O O   . VAL   B 2 27  ? -14.856 9.669   -14.666 1.00 36.38 ? 36  VAL   B O   1 
ATOM   464  C CB  . VAL   B 2 27  ? -16.041 12.292  -13.272 1.00 39.29 ? 36  VAL   B CB  1 
ATOM   465  C CG1 . VAL   B 2 27  ? -15.466 13.649  -12.900 1.00 40.20 ? 36  VAL   B CG1 1 
ATOM   466  C CG2 . VAL   B 2 27  ? -17.536 12.254  -12.994 1.00 39.75 ? 36  VAL   B CG2 1 
ATOM   467  N N   . GLY   B 2 28  ? -16.919 9.937   -15.516 1.00 34.22 ? 37  GLY   B N   1 
ATOM   468  C CA  . GLY   B 2 28  ? -17.130 8.519   -15.763 1.00 32.57 ? 37  GLY   B CA  1 
ATOM   469  C C   . GLY   B 2 28  ? -18.416 8.228   -16.509 1.00 30.67 ? 37  GLY   B C   1 
ATOM   470  O O   . GLY   B 2 28  ? -19.058 9.141   -17.032 1.00 30.59 ? 37  GLY   B O   1 
ATOM   471  N N   . VAL   B 2 29  ? -18.776 6.935   -16.583 1.00 28.99 ? 38  VAL   B N   1 
ATOM   472  C CA  . VAL   B 2 29  ? -19.945 6.363   -17.264 1.00 28.04 ? 38  VAL   B CA  1 
ATOM   473  C C   . VAL   B 2 29  ? -20.662 5.360   -16.310 1.00 27.16 ? 38  VAL   B C   1 
ATOM   474  O O   . VAL   B 2 29  ? -20.038 4.801   -15.414 1.00 26.90 ? 38  VAL   B O   1 
ATOM   475  C CB  . VAL   B 2 29  ? -19.495 5.666   -18.598 1.00 28.38 ? 38  VAL   B CB  1 
ATOM   476  C CG1 . VAL   B 2 29  ? -20.637 4.906   -19.263 1.00 28.86 ? 38  VAL   B CG1 1 
ATOM   477  C CG2 . VAL   B 2 29  ? -18.881 6.665   -19.579 1.00 28.32 ? 38  VAL   B CG2 1 
ATOM   478  N N   . GLY   B 2 30  ? -21.956 5.157   -16.499 1.00 26.55 ? 39  GLY   B N   1 
ATOM   479  C CA  . GLY   B 2 30  ? -22.714 4.190   -15.722 1.00 26.59 ? 39  GLY   B CA  1 
ATOM   480  C C   . GLY   B 2 30  ? -23.796 3.505   -16.533 1.00 26.98 ? 39  GLY   B C   1 
ATOM   481  O O   . GLY   B 2 30  ? -24.118 3.941   -17.634 1.00 27.16 ? 39  GLY   B O   1 
ATOM   482  N N   . VAL   B 2 31  ? -24.373 2.427   -15.998 1.00 27.06 ? 40  VAL   B N   1 
ATOM   483  C CA  . VAL   B 2 31  ? -25.443 1.668   -16.655 1.00 27.48 ? 40  VAL   B CA  1 
ATOM   484  C C   . VAL   B 2 31  ? -26.729 1.718   -15.822 1.00 28.10 ? 40  VAL   B C   1 
ATOM   485  O O   . VAL   B 2 31  ? -26.719 1.311   -14.662 1.00 28.41 ? 40  VAL   B O   1 
ATOM   486  C CB  . VAL   B 2 31  ? -25.010 0.199   -16.821 1.00 27.72 ? 40  VAL   B CB  1 
ATOM   487  C CG1 . VAL   B 2 31  ? -26.132 -0.650  -17.392 1.00 28.06 ? 40  VAL   B CG1 1 
ATOM   488  C CG2 . VAL   B 2 31  ? -23.751 0.091   -17.654 1.00 27.95 ? 40  VAL   B CG2 1 
ATOM   489  N N   . MET   B 2 32  ? -27.825 2.198   -16.398 1.00 27.94 ? 41  MET   B N   1 
ATOM   490  C CA  . MET   B 2 32  ? -29.112 2.205   -15.705 1.00 28.61 ? 41  MET   B CA  1 
ATOM   491  C C   . MET   B 2 32  ? -29.784 0.883   -16.096 1.00 29.07 ? 41  MET   B C   1 
ATOM   492  O O   . MET   B 2 32  ? -29.778 0.541   -17.268 1.00 29.63 ? 41  MET   B O   1 
ATOM   493  C CB  . MET   B 2 32  ? -29.963 3.420   -16.153 1.00 29.41 ? 41  MET   B CB  1 
ATOM   494  C CG  . MET   B 2 32  ? -31.302 3.558   -15.441 1.00 32.21 ? 41  MET   B CG  1 
ATOM   495  S SD  . MET   B 2 32  ? -31.184 4.227   -13.748 1.00 40.37 ? 41  MET   B SD  1 
ATOM   496  C CE  . MET   B 2 32  ? -30.530 5.861   -14.107 1.00 39.14 ? 41  MET   B CE  1 
ATOM   497  N N   . GLN   B 2 33  ? -30.292 0.108   -15.136 1.00 28.96 ? 42  GLN   B N   1 
ATOM   498  C CA  . GLN   B 2 33  ? -30.969 -1.153  -15.447 1.00 29.38 ? 42  GLN   B CA  1 
ATOM   499  C C   . GLN   B 2 33  ? -31.886 -1.541  -14.319 1.00 28.90 ? 42  GLN   B C   1 
ATOM   500  O O   . GLN   B 2 33  ? -31.447 -1.602  -13.169 1.00 29.14 ? 42  GLN   B O   1 
ATOM   501  C CB  . GLN   B 2 33  ? -29.991 -2.295  -15.754 1.00 31.94 ? 42  GLN   B CB  1 
ATOM   502  C CG  . GLN   B 2 33  ? -30.732 -3.553  -16.194 1.00 37.47 ? 42  GLN   B CG  1 
ATOM   503  C CD  . GLN   B 2 33  ? -29.839 -4.630  -16.741 1.00 43.57 ? 42  GLN   B CD  1 
ATOM   504  O OE1 . GLN   B 2 33  ? -29.689 -5.695  -16.134 1.00 45.26 ? 42  GLN   B OE1 1 
ATOM   505  N NE2 . GLN   B 2 33  ? -29.244 -4.389  -17.914 1.00 45.11 ? 42  GLN   B NE2 1 
ATOM   506  N N   . GLU   B 2 34  ? -33.169 -1.773  -14.642 1.00 28.21 ? 43  GLU   B N   1 
ATOM   507  C CA  . GLU   B 2 34  ? -34.214 -2.139  -13.687 1.00 28.23 ? 43  GLU   B CA  1 
ATOM   508  C C   . GLU   B 2 34  ? -34.415 -1.071  -12.590 1.00 27.35 ? 43  GLU   B C   1 
ATOM   509  O O   . GLU   B 2 34  ? -34.797 -1.394  -11.472 1.00 27.30 ? 43  GLU   B O   1 
ATOM   510  C CB  . GLU   B 2 34  ? -33.951 -3.529  -13.076 1.00 31.14 ? 43  GLU   B CB  1 
ATOM   511  C CG  . GLU   B 2 34  ? -33.745 -4.632  -14.101 1.00 35.83 ? 43  GLU   B CG  1 
ATOM   512  C CD  . GLU   B 2 34  ? -33.467 -6.004  -13.514 1.00 43.73 ? 43  GLU   B CD  1 
ATOM   513  O OE1 . GLU   B 2 34  ? -33.962 -6.295  -12.401 1.00 45.71 ? 43  GLU   B OE1 1 
ATOM   514  O OE2 . GLU   B 2 34  ? -32.753 -6.793  -14.173 1.00 46.75 ? 43  GLU   B OE2 1 
ATOM   515  N N   . GLY   B 2 35  ? -34.174 0.189   -12.930 1.00 26.50 ? 44  GLY   B N   1 
ATOM   516  C CA  . GLY   B 2 35  ? -34.321 1.291   -11.991 1.00 26.12 ? 44  GLY   B CA  1 
ATOM   517  C C   . GLY   B 2 35  ? -33.166 1.422   -11.021 1.00 25.55 ? 44  GLY   B C   1 
ATOM   518  O O   . GLY   B 2 35  ? -33.331 2.002   -9.942  1.00 26.20 ? 44  GLY   B O   1 
ATOM   519  N N   . VAL   B 2 36  ? -31.992 0.848   -11.378 1.00 24.27 ? 45  VAL   B N   1 
ATOM   520  C CA  . VAL   B 2 36  ? -30.770 0.875   -10.559 1.00 23.30 ? 45  VAL   B CA  1 
ATOM   521  C C   . VAL   B 2 36  ? -29.586 1.391   -11.406 1.00 22.44 ? 45  VAL   B C   1 
ATOM   522  O O   . VAL   B 2 36  ? -29.308 0.868   -12.494 1.00 21.75 ? 45  VAL   B O   1 
ATOM   523  C CB  . VAL   B 2 36  ? -30.454 -0.482  -9.847  1.00 23.28 ? 45  VAL   B CB  1 
ATOM   524  C CG1 . VAL   B 2 36  ? -29.092 -0.451  -9.169  1.00 23.67 ? 45  VAL   B CG1 1 
ATOM   525  C CG2 . VAL   B 2 36  ? -31.530 -0.850  -8.836  1.00 23.31 ? 45  VAL   B CG2 1 
ATOM   526  N N   . PHE   B 2 37  ? -28.919 2.448   -10.916 1.00 21.85 ? 46  PHE   B N   1 
ATOM   527  C CA  . PHE   B 2 37  ? -27.778 3.007   -11.619 1.00 21.68 ? 46  PHE   B CA  1 
ATOM   528  C C   . PHE   B 2 37  ? -26.534 2.326   -11.129 1.00 21.52 ? 46  PHE   B C   1 
ATOM   529  O O   . PHE   B 2 37  ? -26.233 2.444   -9.948  1.00 21.75 ? 46  PHE   B O   1 
ATOM   530  C CB  . PHE   B 2 37  ? -27.638 4.498   -11.349 1.00 21.31 ? 46  PHE   B CB  1 
ATOM   531  C CG  . PHE   B 2 37  ? -26.679 5.110   -12.337 1.00 21.64 ? 46  PHE   B CG  1 
ATOM   532  C CD1 . PHE   B 2 37  ? -26.973 5.127   -13.693 1.00 21.72 ? 46  PHE   B CD1 1 
ATOM   533  C CD2 . PHE   B 2 37  ? -25.461 5.620   -11.920 1.00 22.15 ? 46  PHE   B CD2 1 
ATOM   534  C CE1 . PHE   B 2 37  ? -26.098 5.691   -14.598 1.00 22.22 ? 46  PHE   B CE1 1 
ATOM   535  C CE2 . PHE   B 2 37  ? -24.576 6.163   -12.835 1.00 22.50 ? 46  PHE   B CE2 1 
ATOM   536  C CZ  . PHE   B 2 37  ? -24.916 6.220   -14.164 1.00 22.27 ? 46  PHE   B CZ  1 
ATOM   537  N N   . HIS   B 2 38  ? -25.804 1.633   -12.024 1.00 20.62 ? 47  HIS   B N   1 
ATOM   538  C CA  . HIS   B 2 38  ? -24.593 0.891   -11.702 1.00 20.25 ? 47  HIS   B CA  1 
ATOM   539  C C   . HIS   B 2 38  ? -23.400 1.600   -12.252 1.00 20.28 ? 47  HIS   B C   1 
ATOM   540  O O   . HIS   B 2 38  ? -23.327 1.738   -13.448 1.00 20.27 ? 47  HIS   B O   1 
ATOM   541  C CB  . HIS   B 2 38  ? -24.640 -0.475  -12.391 1.00 20.48 ? 47  HIS   B CB  1 
ATOM   542  C CG  . HIS   B 2 38  ? -25.858 -1.276  -12.082 1.00 21.98 ? 47  HIS   B CG  1 
ATOM   543  N ND1 . HIS   B 2 38  ? -27.071 -0.996  -12.675 1.00 23.48 ? 47  HIS   B ND1 1 
ATOM   544  C CD2 . HIS   B 2 38  ? -26.009 -2.334  -11.255 1.00 22.82 ? 47  HIS   B CD2 1 
ATOM   545  C CE1 . HIS   B 2 38  ? -27.917 -1.899  -12.203 1.00 23.77 ? 47  HIS   B CE1 1 
ATOM   546  N NE2 . HIS   B 2 38  ? -27.322 -2.723  -11.348 1.00 23.69 ? 47  HIS   B NE2 1 
ATOM   547  N N   . THR   B 2 39  ? -22.430 1.975   -11.428 1.00 20.70 ? 48  THR   B N   1 
ATOM   548  C CA  . THR   B 2 39  ? -21.200 2.620   -11.929 1.00 21.48 ? 48  THR   B CA  1 
ATOM   549  C C   . THR   B 2 39  ? -19.973 2.144   -11.117 1.00 21.84 ? 48  THR   B C   1 
ATOM   550  O O   . THR   B 2 39  ? -20.133 1.311   -10.218 1.00 21.41 ? 48  THR   B O   1 
ATOM   551  C CB  . THR   B 2 39  ? -21.371 4.168   -11.988 1.00 22.84 ? 48  THR   B CB  1 
ATOM   552  O OG1 . THR   B 2 39  ? -20.315 4.727   -12.772 1.00 23.52 ? 48  THR   B OG1 1 
ATOM   553  C CG2 . THR   B 2 39  ? -21.339 4.810   -10.599 1.00 23.38 ? 48  THR   B CG2 1 
ATOM   554  N N   . MET   B 2 40  ? -18.756 2.634   -11.437 1.00 22.20 ? 49  MET   B N   1 
ATOM   555  C CA  . MET   B 2 40  ? -17.570 2.271   -10.661 1.00 23.17 ? 49  MET   B CA  1 
ATOM   556  C C   . MET   B 2 40  ? -17.384 3.276   -9.502  1.00 24.02 ? 49  MET   B C   1 
ATOM   557  O O   . MET   B 2 40  ? -17.663 4.459   -9.678  1.00 24.56 ? 49  MET   B O   1 
ATOM   558  C CB  . MET   B 2 40  ? -16.327 2.202   -11.552 1.00 23.90 ? 49  MET   B CB  1 
ATOM   559  C CG  . MET   B 2 40  ? -16.526 1.356   -12.793 1.00 25.18 ? 49  MET   B CG  1 
ATOM   560  S SD  . MET   B 2 40  ? -15.002 0.523   -13.282 1.00 26.55 ? 49  MET   B SD  1 
ATOM   561  C CE  . MET   B 2 40  ? -14.935 -0.748  -12.103 1.00 17.86 ? 49  MET   B CE  1 
ATOM   562  N N   . TRP   B 2 41  ? -16.931 2.804   -8.327  1.00 23.93 ? 50  TRP   B N   1 
ATOM   563  C CA  A TRP   B 2 41  ? -16.738 3.643   -7.146  0.50 24.75 ? 50  TRP   B CA  1 
ATOM   564  C CA  B TRP   B 2 41  ? -16.760 3.653   -7.150  0.50 24.59 ? 50  TRP   B CA  1 
ATOM   565  C C   . TRP   B 2 41  ? -15.837 4.845   -7.379  1.00 25.54 ? 50  TRP   B C   1 
ATOM   566  O O   . TRP   B 2 41  ? -16.141 5.921   -6.885  1.00 26.26 ? 50  TRP   B O   1 
ATOM   567  C CB  A TRP   B 2 41  ? -16.200 2.821   -5.965  0.50 24.54 ? 50  TRP   B CB  1 
ATOM   568  C CB  B TRP   B 2 41  ? -16.310 2.835   -5.922  0.50 24.16 ? 50  TRP   B CB  1 
ATOM   569  C CG  A TRP   B 2 41  ? -16.114 3.577   -4.671  0.50 24.84 ? 50  TRP   B CG  1 
ATOM   570  C CG  B TRP   B 2 41  ? -16.208 3.614   -4.638  0.50 24.15 ? 50  TRP   B CG  1 
ATOM   571  C CD1 A TRP   B 2 41  ? -17.049 3.609   -3.681  0.50 25.54 ? 50  TRP   B CD1 1 
ATOM   572  C CD1 B TRP   B 2 41  ? -15.146 4.355   -4.210  0.50 24.82 ? 50  TRP   B CD1 1 
ATOM   573  C CD2 A TRP   B 2 41  ? -14.999 4.348   -4.195  0.50 24.93 ? 50  TRP   B CD2 1 
ATOM   574  C CD2 B TRP   B 2 41  ? -17.163 3.632   -3.568  0.50 24.01 ? 50  TRP   B CD2 1 
ATOM   575  N NE1 A TRP   B 2 41  ? -16.603 4.381   -2.636  0.50 25.71 ? 50  TRP   B NE1 1 
ATOM   576  N NE1 B TRP   B 2 41  ? -15.403 4.878   -2.967  0.50 24.79 ? 50  TRP   B NE1 1 
ATOM   577  C CE2 A TRP   B 2 41  ? -15.346 4.843   -2.923  0.50 25.47 ? 50  TRP   B CE2 1 
ATOM   578  C CE2 B TRP   B 2 41  ? -16.638 4.454   -2.551  0.50 24.60 ? 50  TRP   B CE2 1 
ATOM   579  C CE3 A TRP   B 2 41  ? -13.751 4.689   -4.731  0.50 25.55 ? 50  TRP   B CE3 1 
ATOM   580  C CE3 B TRP   B 2 41  ? -18.428 3.063   -3.385  0.50 24.55 ? 50  TRP   B CE3 1 
ATOM   581  C CZ2 A TRP   B 2 41  ? -14.497 5.666   -2.188  0.50 26.24 ? 50  TRP   B CZ2 1 
ATOM   582  C CZ2 B TRP   B 2 41  ? -17.335 4.718   -1.370  0.50 25.22 ? 50  TRP   B CZ2 1 
ATOM   583  C CZ3 A TRP   B 2 41  ? -12.911 5.498   -3.996  0.50 26.36 ? 50  TRP   B CZ3 1 
ATOM   584  C CZ3 B TRP   B 2 41  ? -19.112 3.325   -2.212  0.50 25.29 ? 50  TRP   B CZ3 1 
ATOM   585  C CH2 A TRP   B 2 41  ? -13.277 5.959   -2.732  0.50 26.42 ? 50  TRP   B CH2 1 
ATOM   586  C CH2 B TRP   B 2 41  ? -18.562 4.131   -1.215  0.50 25.28 ? 50  TRP   B CH2 1 
ATOM   587  N N   . HIS   B 2 42  ? -14.706 4.667   -8.086  1.00 25.40 ? 51  HIS   B N   1 
ATOM   588  C CA  . HIS   B 2 42  ? -13.767 5.774   -8.283  1.00 25.99 ? 51  HIS   B CA  1 
ATOM   589  C C   . HIS   B 2 42  ? -14.343 6.969   -9.083  1.00 27.77 ? 51  HIS   B C   1 
ATOM   590  O O   . HIS   B 2 42  ? -13.727 8.039   -9.129  1.00 28.56 ? 51  HIS   B O   1 
ATOM   591  C CB  . HIS   B 2 42  ? -12.452 5.269   -8.889  1.00 25.84 ? 51  HIS   B CB  1 
ATOM   592  C CG  . HIS   B 2 42  ? -12.520 4.981   -10.358 1.00 26.65 ? 51  HIS   B CG  1 
ATOM   593  N ND1 . HIS   B 2 42  ? -12.662 3.692   -10.835 1.00 28.04 ? 51  HIS   B ND1 1 
ATOM   594  C CD2 . HIS   B 2 42  ? -12.419 5.826   -11.412 1.00 27.15 ? 51  HIS   B CD2 1 
ATOM   595  C CE1 . HIS   B 2 42  ? -12.681 3.801   -12.153 1.00 27.94 ? 51  HIS   B CE1 1 
ATOM   596  N NE2 . HIS   B 2 42  ? -12.550 5.067   -12.542 1.00 27.59 ? 51  HIS   B NE2 1 
ATOM   597  N N   . VAL   B 2 43  ? -15.507 6.787   -9.726  1.00 28.12 ? 52  VAL   B N   1 
ATOM   598  C CA  . VAL   B 2 43  ? -16.125 7.851   -10.508 1.00 28.35 ? 52  VAL   B CA  1 
ATOM   599  C C   . VAL   B 2 43  ? -16.812 8.836   -9.571  1.00 28.62 ? 52  VAL   B C   1 
ATOM   600  O O   . VAL   B 2 43  ? -16.481 10.019  -9.576  1.00 28.77 ? 52  VAL   B O   1 
ATOM   601  C CB  . VAL   B 2 43  ? -17.104 7.283   -11.560 1.00 29.28 ? 52  VAL   B CB  1 
ATOM   602  C CG1 . VAL   B 2 43  ? -17.756 8.408   -12.349 1.00 30.01 ? 52  VAL   B CG1 1 
ATOM   603  C CG2 . VAL   B 2 43  ? -16.411 6.290   -12.487 1.00 29.85 ? 52  VAL   B CG2 1 
ATOM   604  N N   . THR   B 2 44  ? -17.689 8.330   -8.692  1.00 28.58 ? 53  THR   B N   1 
ATOM   605  C CA  . THR   B 2 44  ? -18.465 9.144   -7.761  1.00 28.56 ? 53  THR   B CA  1 
ATOM   606  C C   . THR   B 2 44  ? -17.912 9.193   -6.341  1.00 28.94 ? 53  THR   B C   1 
ATOM   607  O O   . THR   B 2 44  ? -18.390 10.002  -5.553  1.00 29.30 ? 53  THR   B O   1 
ATOM   608  C CB  . THR   B 2 44  ? -19.922 8.651   -7.731  1.00 29.03 ? 53  THR   B CB  1 
ATOM   609  O OG1 . THR   B 2 44  ? -19.991 7.401   -7.037  1.00 29.18 ? 53  THR   B OG1 1 
ATOM   610  C CG2 . THR   B 2 44  ? -20.528 8.499   -9.133  1.00 29.49 ? 53  THR   B CG2 1 
ATOM   611  N N   . LYS   B 2 45  ? -16.971 8.314   -5.988  1.00 28.68 ? 54  LYS   B N   1 
ATOM   612  C CA  . LYS   B 2 45  ? -16.426 8.220   -4.633  1.00 29.51 ? 54  LYS   B CA  1 
ATOM   613  C C   . LYS   B 2 45  ? -17.518 8.013   -3.532  1.00 29.74 ? 54  LYS   B C   1 
ATOM   614  O O   . LYS   B 2 45  ? -17.237 8.198   -2.338  1.00 29.18 ? 54  LYS   B O   1 
ATOM   615  C CB  . LYS   B 2 45  ? -15.532 9.424   -4.315  1.00 32.03 ? 54  LYS   B CB  1 
ATOM   616  C CG  . LYS   B 2 45  ? -14.369 9.578   -5.265  1.00 36.91 ? 54  LYS   B CG  1 
ATOM   617  C CD  . LYS   B 2 45  ? -13.079 9.081   -4.642  1.00 42.82 ? 54  LYS   B CD  1 
ATOM   618  C CE  . LYS   B 2 45  ? -11.902 9.254   -5.575  1.00 48.00 ? 54  LYS   B CE  1 
ATOM   619  N NZ  . LYS   B 2 45  ? -12.140 8.624   -6.907  1.00 50.67 ? 54  LYS   B NZ  1 
ATOM   620  N N   . GLY   B 2 46  ? -18.735 7.638   -3.968  1.00 29.88 ? 55  GLY   B N   1 
ATOM   621  C CA  . GLY   B 2 46  ? -19.909 7.404   -3.137  1.00 30.31 ? 55  GLY   B CA  1 
ATOM   622  C C   . GLY   B 2 46  ? -20.915 8.543   -3.103  1.00 30.77 ? 55  GLY   B C   1 
ATOM   623  O O   . GLY   B 2 46  ? -21.969 8.411   -2.483  1.00 30.95 ? 55  GLY   B O   1 
ATOM   624  N N   . ALA   B 2 47  ? -20.606 9.678   -3.743  1.00 30.93 ? 56  ALA   B N   1 
ATOM   625  C CA  . ALA   B 2 47  ? -21.475 10.856  -3.728  1.00 31.59 ? 56  ALA   B CA  1 
ATOM   626  C C   . ALA   B 2 47  ? -22.823 10.667  -4.418  1.00 32.23 ? 56  ALA   B C   1 
ATOM   627  O O   . ALA   B 2 47  ? -22.943 9.836   -5.315  1.00 32.27 ? 56  ALA   B O   1 
ATOM   628  C CB  . ALA   B 2 47  ? -20.747 12.052  -4.321  1.00 31.62 ? 56  ALA   B CB  1 
ATOM   629  N N   . ALA   B 2 48  ? -23.836 11.443  -3.995  1.00 32.57 ? 57  ALA   B N   1 
ATOM   630  C CA  . ALA   B 2 48  ? -25.165 11.396  -4.588  1.00 33.60 ? 57  ALA   B CA  1 
ATOM   631  C C   . ALA   B 2 48  ? -25.149 12.021  -5.992  1.00 35.42 ? 57  ALA   B C   1 
ATOM   632  O O   . ALA   B 2 48  ? -24.260 12.812  -6.316  1.00 35.98 ? 57  ALA   B O   1 
ATOM   633  C CB  . ALA   B 2 48  ? -26.154 12.125  -3.701  1.00 33.32 ? 57  ALA   B CB  1 
ATOM   634  N N   . LEU   B 2 49  ? -26.121 11.660  -6.834  1.00 36.09 ? 58  LEU   B N   1 
ATOM   635  C CA  . LEU   B 2 49  ? -26.185 12.187  -8.207  1.00 37.00 ? 58  LEU   B CA  1 
ATOM   636  C C   . LEU   B 2 49  ? -27.515 12.927  -8.493  1.00 38.74 ? 58  LEU   B C   1 
ATOM   637  O O   . LEU   B 2 49  ? -28.464 12.821  -7.721  1.00 39.10 ? 58  LEU   B O   1 
ATOM   638  C CB  . LEU   B 2 49  ? -25.963 11.044  -9.218  1.00 36.34 ? 58  LEU   B CB  1 
ATOM   639  C CG  . LEU   B 2 49  ? -24.746 10.163  -8.968  1.00 36.92 ? 58  LEU   B CG  1 
ATOM   640  C CD1 . LEU   B 2 49  ? -24.747 8.979   -9.871  1.00 37.54 ? 58  LEU   B CD1 1 
ATOM   641  C CD2 . LEU   B 2 49  ? -23.473 10.933  -9.119  1.00 37.13 ? 58  LEU   B CD2 1 
ATOM   642  N N   . ARG   B 2 50  ? -27.569 13.703  -9.570  1.00 39.89 ? 59  ARG   B N   1 
ATOM   643  C CA  . ARG   B 2 50  ? -28.794 14.397  -9.949  1.00 41.71 ? 59  ARG   B CA  1 
ATOM   644  C C   . ARG   B 2 50  ? -29.210 13.909  -11.321 1.00 41.72 ? 59  ARG   B C   1 
ATOM   645  O O   . ARG   B 2 50  ? -28.378 13.827  -12.198 1.00 41.21 ? 59  ARG   B O   1 
ATOM   646  C CB  . ARG   B 2 50  ? -28.614 15.933  -9.917  1.00 44.97 ? 59  ARG   B CB  1 
ATOM   647  C CG  . ARG   B 2 50  ? -29.785 16.719  -10.548 1.00 50.53 ? 59  ARG   B CG  1 
ATOM   648  C CD  . ARG   B 2 50  ? -29.693 18.237  -10.414 1.00 55.28 ? 59  ARG   B CD  1 
ATOM   649  N NE  . ARG   B 2 50  ? -28.393 18.772  -10.831 1.00 59.32 ? 59  ARG   B NE  1 
ATOM   650  C CZ  . ARG   B 2 50  ? -28.094 19.148  -12.070 1.00 62.57 ? 59  ARG   B CZ  1 
ATOM   651  N NH1 . ARG   B 2 50  ? -28.996 19.046  -13.039 1.00 62.24 ? 59  ARG   B NH1 1 
ATOM   652  N NH2 . ARG   B 2 50  ? -26.889 19.629  -12.352 1.00 63.32 ? 59  ARG   B NH2 1 
ATOM   653  N N   . SER   B 2 51  ? -30.473 13.536  -11.495 1.00 42.67 ? 60  SER   B N   1 
ATOM   654  C CA  . SER   B 2 51  ? -30.978 13.096  -12.794 1.00 44.39 ? 60  SER   B CA  1 
ATOM   655  C C   . SER   B 2 51  ? -32.216 13.931  -13.131 1.00 46.39 ? 60  SER   B C   1 
ATOM   656  O O   . SER   B 2 51  ? -33.307 13.669  -12.613 1.00 47.00 ? 60  SER   B O   1 
ATOM   657  C CB  . SER   B 2 51  ? -31.325 11.613  -12.775 1.00 45.51 ? 60  SER   B CB  1 
ATOM   658  O OG  . SER   B 2 51  ? -31.618 11.157  -14.085 1.00 47.63 ? 60  SER   B OG  1 
ATOM   659  N N   . GLY   B 2 52  ? -32.026 14.974  -13.936 1.00 47.20 ? 61  GLY   B N   1 
ATOM   660  C CA  . GLY   B 2 52  ? -33.090 15.912  -14.271 1.00 48.35 ? 61  GLY   B CA  1 
ATOM   661  C C   . GLY   B 2 52  ? -33.297 16.751  -13.040 1.00 49.30 ? 61  GLY   B C   1 
ATOM   662  O O   . GLY   B 2 52  ? -32.378 17.458  -12.630 1.00 49.66 ? 61  GLY   B O   1 
ATOM   663  N N   . GLU   B 2 53  ? -34.428 16.559  -12.358 1.00 49.85 ? 62  GLU   B N   1 
ATOM   664  C CA  . GLU   B 2 53  ? -34.635 17.196  -11.043 1.00 50.85 ? 62  GLU   B CA  1 
ATOM   665  C C   . GLU   B 2 53  ? -34.639 16.166  -9.882  1.00 50.39 ? 62  GLU   B C   1 
ATOM   666  O O   . GLU   B 2 53  ? -34.919 16.531  -8.737  1.00 50.79 ? 62  GLU   B O   1 
ATOM   667  C CB  . GLU   B 2 53  ? -35.911 18.052  -11.012 1.00 54.28 ? 62  GLU   B CB  1 
ATOM   668  C CG  . GLU   B 2 53  ? -35.825 19.239  -10.068 1.00 59.98 ? 62  GLU   B CG  1 
ATOM   669  C CD  . GLU   B 2 53  ? -37.003 20.194  -10.114 1.00 68.43 ? 62  GLU   B CD  1 
ATOM   670  O OE1 . GLU   B 2 53  ? -37.952 19.932  -10.890 1.00 70.26 ? 62  GLU   B OE1 1 
ATOM   671  O OE2 . GLU   B 2 53  ? -36.975 21.209  -9.376  1.00 70.98 ? 62  GLU   B OE2 1 
ATOM   672  N N   . GLY   B 2 54  ? -34.309 14.904  -10.180 1.00 49.44 ? 63  GLY   B N   1 
ATOM   673  C CA  . GLY   B 2 54  ? -34.274 13.836  -9.193  1.00 49.05 ? 63  GLY   B CA  1 
ATOM   674  C C   . GLY   B 2 54  ? -32.977 13.745  -8.416  1.00 48.00 ? 63  GLY   B C   1 
ATOM   675  O O   . GLY   B 2 54  ? -32.067 14.555  -8.605  1.00 48.44 ? 63  GLY   B O   1 
ATOM   676  N N   . ARG   B 2 55  ? -32.891 12.757  -7.522  1.00 46.29 ? 64  ARG   B N   1 
ATOM   677  C CA  . ARG   B 2 55  ? -31.703 12.528  -6.709  1.00 44.93 ? 64  ARG   B CA  1 
ATOM   678  C C   . ARG   B 2 55  ? -31.424 11.036  -6.671  1.00 43.17 ? 64  ARG   B C   1 
ATOM   679  O O   . ARG   B 2 55  ? -32.323 10.250  -6.395  1.00 43.49 ? 64  ARG   B O   1 
ATOM   680  C CB  . ARG   B 2 55  ? -31.905 13.068  -5.284  1.00 45.97 ? 64  ARG   B CB  1 
ATOM   681  C CG  . ARG   B 2 55  ? -30.667 12.976  -4.417  1.00 49.07 ? 64  ARG   B CG  1 
ATOM   682  C CD  . ARG   B 2 55  ? -30.897 13.630  -3.064  1.00 52.83 ? 64  ARG   B CD  1 
ATOM   683  N NE  . ARG   B 2 55  ? -29.843 13.306  -2.098  1.00 55.46 ? 64  ARG   B NE  1 
ATOM   684  C CZ  . ARG   B 2 55  ? -29.163 14.209  -1.395  1.00 57.39 ? 64  ARG   B CZ  1 
ATOM   685  N NH1 . ARG   B 2 55  ? -29.424 15.506  -1.536  1.00 57.06 ? 64  ARG   B NH1 1 
ATOM   686  N NH2 . ARG   B 2 55  ? -28.219 13.823  -0.545  1.00 56.85 ? 64  ARG   B NH2 1 
ATOM   687  N N   . LEU   B 2 56  ? -30.201 10.643  -6.997  1.00 41.25 ? 65  LEU   B N   1 
ATOM   688  C CA  . LEU   B 2 56  ? -29.811 9.250   -6.967  1.00 39.97 ? 65  LEU   B CA  1 
ATOM   689  C C   . LEU   B 2 56  ? -28.960 9.102   -5.743  1.00 39.12 ? 65  LEU   B C   1 
ATOM   690  O O   . LEU   B 2 56  ? -27.855 9.631   -5.721  1.00 39.18 ? 65  LEU   B O   1 
ATOM   691  C CB  . LEU   B 2 56  ? -28.969 8.891   -8.201  1.00 39.73 ? 65  LEU   B CB  1 
ATOM   692  C CG  . LEU   B 2 56  ? -29.585 9.061   -9.578  1.00 40.29 ? 65  LEU   B CG  1 
ATOM   693  C CD1 . LEU   B 2 56  ? -28.675 8.503   -10.608 1.00 40.57 ? 65  LEU   B CD1 1 
ATOM   694  C CD2 . LEU   B 2 56  ? -30.912 8.352   -9.689  1.00 40.78 ? 65  LEU   B CD2 1 
ATOM   695  N N   . ASP   B 2 57  ? -29.470 8.436   -4.703  1.00 38.27 ? 66  ASP   B N   1 
ATOM   696  C CA  . ASP   B 2 57  ? -28.707 8.244   -3.467  1.00 37.86 ? 66  ASP   B CA  1 
ATOM   697  C C   . ASP   B 2 57  ? -28.125 6.845   -3.434  1.00 35.88 ? 66  ASP   B C   1 
ATOM   698  O O   . ASP   B 2 57  ? -28.813 5.908   -3.831  1.00 36.69 ? 66  ASP   B O   1 
ATOM   699  C CB  . ASP   B 2 57  ? -29.608 8.469   -2.258  1.00 41.45 ? 66  ASP   B CB  1 
ATOM   700  C CG  . ASP   B 2 57  ? -29.913 9.931   -2.029  1.00 49.51 ? 66  ASP   B CG  1 
ATOM   701  O OD1 . ASP   B 2 57  ? -28.997 10.663  -1.586  1.00 51.40 ? 66  ASP   B OD1 1 
ATOM   702  O OD2 . ASP   B 2 57  ? -31.072 10.348  -2.291  1.00 52.45 ? 66  ASP   B OD2 1 
ATOM   703  N N   . PRO   B 2 58  ? -26.865 6.662   -2.995  1.00 33.24 ? 67  PRO   B N   1 
ATOM   704  C CA  . PRO   B 2 58  ? -26.269 5.315   -3.029  1.00 31.52 ? 67  PRO   B CA  1 
ATOM   705  C C   . PRO   B 2 58  ? -26.978 4.259   -2.178  1.00 29.76 ? 67  PRO   B C   1 
ATOM   706  O O   . PRO   B 2 58  ? -27.602 4.563   -1.151  1.00 29.94 ? 67  PRO   B O   1 
ATOM   707  C CB  . PRO   B 2 58  ? -24.818 5.542   -2.592  1.00 32.18 ? 67  PRO   B CB  1 
ATOM   708  C CG  . PRO   B 2 58  ? -24.825 6.838   -1.888  1.00 33.01 ? 67  PRO   B CG  1 
ATOM   709  C CD  . PRO   B 2 58  ? -25.902 7.669   -2.519  1.00 32.13 ? 67  PRO   B CD  1 
ATOM   710  N N   . TYR   B 2 59  ? -26.898 3.001   -2.632  1.00 27.67 ? 68  TYR   B N   1 
ATOM   711  C CA  . TYR   B 2 59  ? -27.536 1.891   -1.930  1.00 26.07 ? 68  TYR   B CA  1 
ATOM   712  C C   . TYR   B 2 59  ? -26.510 0.847   -1.511  1.00 24.28 ? 68  TYR   B C   1 
ATOM   713  O O   . TYR   B 2 59  ? -26.556 0.371   -0.389  1.00 24.23 ? 68  TYR   B O   1 
ATOM   714  C CB  . TYR   B 2 59  ? -28.652 1.287   -2.785  1.00 25.59 ? 68  TYR   B CB  1 
ATOM   715  C CG  . TYR   B 2 59  ? -29.357 0.100   -2.174  1.00 25.92 ? 68  TYR   B CG  1 
ATOM   716  C CD1 . TYR   B 2 59  ? -28.743 -1.144  -2.113  1.00 26.91 ? 68  TYR   B CD1 1 
ATOM   717  C CD2 . TYR   B 2 59  ? -30.684 0.183   -1.789  1.00 26.68 ? 68  TYR   B CD2 1 
ATOM   718  C CE1 . TYR   B 2 59  ? -29.397 -2.251  -1.596  1.00 27.79 ? 68  TYR   B CE1 1 
ATOM   719  C CE2 . TYR   B 2 59  ? -31.361 -0.926  -1.301  1.00 27.84 ? 68  TYR   B CE2 1 
ATOM   720  C CZ  . TYR   B 2 59  ? -30.712 -2.145  -1.203  1.00 28.66 ? 68  TYR   B CZ  1 
ATOM   721  O OH  . TYR   B 2 59  ? -31.369 -3.252  -0.719  1.00 29.65 ? 68  TYR   B OH  1 
ATOM   722  N N   . TRP   B 2 60  ? -25.598 0.493   -2.403  1.00 22.67 ? 69  TRP   B N   1 
ATOM   723  C CA  . TRP   B 2 60  ? -24.542 -0.461  -2.110  1.00 22.17 ? 69  TRP   B CA  1 
ATOM   724  C C   . TRP   B 2 60  ? -23.263 0.010   -2.800  1.00 22.92 ? 69  TRP   B C   1 
ATOM   725  O O   . TRP   B 2 60  ? -23.307 0.448   -3.948  1.00 23.86 ? 69  TRP   B O   1 
ATOM   726  C CB  . TRP   B 2 60  ? -24.910 -1.867  -2.615  1.00 21.58 ? 69  TRP   B CB  1 
ATOM   727  C CG  . TRP   B 2 60  ? -23.752 -2.813  -2.540  1.00 21.68 ? 69  TRP   B CG  1 
ATOM   728  C CD1 . TRP   B 2 60  ? -23.211 -3.341  -1.409  1.00 22.81 ? 69  TRP   B CD1 1 
ATOM   729  C CD2 . TRP   B 2 60  ? -22.859 -3.161  -3.609  1.00 21.52 ? 69  TRP   B CD2 1 
ATOM   730  N NE1 . TRP   B 2 60  ? -22.078 -4.053  -1.714  1.00 23.13 ? 69  TRP   B NE1 1 
ATOM   731  C CE2 . TRP   B 2 60  ? -21.841 -3.960  -3.060  1.00 22.33 ? 69  TRP   B CE2 1 
ATOM   732  C CE3 . TRP   B 2 60  ? -22.823 -2.875  -4.980  1.00 21.57 ? 69  TRP   B CE3 1 
ATOM   733  C CZ2 . TRP   B 2 60  ? -20.825 -4.511  -3.840  1.00 22.62 ? 69  TRP   B CZ2 1 
ATOM   734  C CZ3 . TRP   B 2 60  ? -21.819 -3.425  -5.748  1.00 21.84 ? 69  TRP   B CZ3 1 
ATOM   735  C CH2 . TRP   B 2 60  ? -20.841 -4.236  -5.184  1.00 22.04 ? 69  TRP   B CH2 1 
ATOM   736  N N   . GLY   B 2 61  ? -22.130 -0.164  -2.144  1.00 22.27 ? 70  GLY   B N   1 
ATOM   737  C CA  . GLY   B 2 61  ? -20.845 0.213   -2.716  1.00 22.05 ? 70  GLY   B CA  1 
ATOM   738  C C   . GLY   B 2 61  ? -19.715 -0.517  -2.034  1.00 22.03 ? 70  GLY   B C   1 
ATOM   739  O O   . GLY   B 2 61  ? -19.821 -0.868  -0.850  1.00 22.33 ? 70  GLY   B O   1 
ATOM   740  N N   . ASP   B 2 62  ? -18.620 -0.726  -2.756  1.00 21.52 ? 71  ASP   B N   1 
ATOM   741  C CA  . ASP   B 2 62  ? -17.476 -1.458  -2.230  1.00 22.04 ? 71  ASP   B CA  1 
ATOM   742  C C   . ASP   B 2 62  ? -16.208 -0.966  -2.934  1.00 22.53 ? 71  ASP   B C   1 
ATOM   743  O O   . ASP   B 2 62  ? -16.123 -1.010  -4.170  1.00 23.24 ? 71  ASP   B O   1 
ATOM   744  C CB  . ASP   B 2 62  ? -17.703 -2.965  -2.454  1.00 24.03 ? 71  ASP   B CB  1 
ATOM   745  C CG  . ASP   B 2 62  ? -16.702 -3.893  -1.806  1.00 30.36 ? 71  ASP   B CG  1 
ATOM   746  O OD1 . ASP   B 2 62  ? -15.487 -3.757  -2.091  1.00 31.46 ? 71  ASP   B OD1 1 
ATOM   747  O OD2 . ASP   B 2 62  ? -17.133 -4.793  -1.054  1.00 33.44 ? 71  ASP   B OD2 1 
ATOM   748  N N   . VAL   B 2 63  ? -15.219 -0.516  -2.153  1.00 21.85 ? 72  VAL   B N   1 
ATOM   749  C CA  . VAL   B 2 63  ? -13.974 0.027   -2.673  1.00 22.05 ? 72  VAL   B CA  1 
ATOM   750  C C   . VAL   B 2 63  ? -13.058 -1.048  -3.237  1.00 22.31 ? 72  VAL   B C   1 
ATOM   751  O O   . VAL   B 2 63  ? -12.369 -0.753  -4.214  1.00 22.56 ? 72  VAL   B O   1 
ATOM   752  C CB  . VAL   B 2 63  ? -13.291 0.921   -1.620  1.00 22.99 ? 72  VAL   B CB  1 
ATOM   753  C CG1 . VAL   B 2 63  ? -11.799 1.115   -1.872  1.00 23.51 ? 72  VAL   B CG1 1 
ATOM   754  C CG2 . VAL   B 2 63  ? -13.994 2.259   -1.560  1.00 23.94 ? 72  VAL   B CG2 1 
ATOM   755  N N   . LYS   B 2 64  ? -13.058 -2.289  -2.684  1.00 22.16 ? 73  LYS   B N   1 
ATOM   756  C CA  . LYS   B 2 64  ? -12.192 -3.336  -3.252  1.00 22.23 ? 73  LYS   B CA  1 
ATOM   757  C C   . LYS   B 2 64  ? -12.705 -3.750  -4.632  1.00 22.32 ? 73  LYS   B C   1 
ATOM   758  O O   . LYS   B 2 64  ? -11.919 -3.876  -5.572  1.00 22.39 ? 73  LYS   B O   1 
ATOM   759  C CB  . LYS   B 2 64  ? -12.061 -4.558  -2.337  1.00 23.40 ? 73  LYS   B CB  1 
ATOM   760  C CG  . LYS   B 2 64  ? -10.929 -5.495  -2.779  1.00 27.05 ? 73  LYS   B CG  1 
ATOM   761  C CD  . LYS   B 2 64  ? -10.883 -6.773  -1.928  1.00 31.22 ? 73  LYS   B CD  1 
ATOM   762  C CE  . LYS   B 2 64  ? -9.494  -7.340  -1.736  1.00 33.57 ? 73  LYS   B CE  1 
ATOM   763  N NZ  . LYS   B 2 64  ? -9.103  -8.234  -2.851  1.00 35.06 ? 73  LYS   B NZ  1 
ATOM   764  N N   . GLN   B 2 65  ? -14.027 -3.937  -4.756  1.00 21.81 ? 74  GLN   B N   1 
ATOM   765  C CA  . GLN   B 2 65  ? -14.629 -4.291  -6.030  1.00 21.89 ? 74  GLN   B CA  1 
ATOM   766  C C   . GLN   B 2 65  ? -14.620 -3.116  -7.012  1.00 22.12 ? 74  GLN   B C   1 
ATOM   767  O O   . GLN   B 2 65  ? -14.602 -3.339  -8.231  1.00 22.74 ? 74  GLN   B O   1 
ATOM   768  C CB  . GLN   B 2 65  ? -16.064 -4.770  -5.818  1.00 23.64 ? 74  GLN   B CB  1 
ATOM   769  C CG  . GLN   B 2 65  ? -16.148 -6.110  -5.102  1.00 28.24 ? 74  GLN   B CG  1 
ATOM   770  C CD  . GLN   B 2 65  ? -17.578 -6.579  -4.912  1.00 33.47 ? 74  GLN   B CD  1 
ATOM   771  O OE1 . GLN   B 2 65  ? -18.279 -6.960  -5.875  1.00 34.89 ? 74  GLN   B OE1 1 
ATOM   772  N NE2 . GLN   B 2 65  ? -18.035 -6.579  -3.654  1.00 33.77 ? 74  GLN   B NE2 1 
ATOM   773  N N   . ASP   B 2 66  ? -14.630 -1.870  -6.479  1.00 21.71 ? 75  ASP   B N   1 
ATOM   774  C CA  . ASP   B 2 66  ? -14.672 -0.613  -7.222  1.00 21.63 ? 75  ASP   B CA  1 
ATOM   775  C C   . ASP   B 2 66  ? -16.024 -0.541  -7.932  1.00 21.30 ? 75  ASP   B C   1 
ATOM   776  O O   . ASP   B 2 66  ? -16.072 -0.274  -9.121  1.00 21.64 ? 75  ASP   B O   1 
ATOM   777  C CB  . ASP   B 2 66  ? -13.489 -0.481  -8.214  1.00 22.55 ? 75  ASP   B CB  1 
ATOM   778  C CG  . ASP   B 2 66  ? -13.261 0.936   -8.698  1.00 25.49 ? 75  ASP   B CG  1 
ATOM   779  O OD1 . ASP   B 2 66  ? -13.656 1.879   -7.979  1.00 26.29 ? 75  ASP   B OD1 1 
ATOM   780  O OD2 . ASP   B 2 66  ? -12.692 1.103   -9.794  1.00 26.18 ? 75  ASP   B OD2 1 
ATOM   781  N N   . LEU   B 2 67  ? -17.128 -0.804  -7.209  1.00 20.55 ? 76  LEU   B N   1 
ATOM   782  C CA  . LEU   B 2 67  ? -18.472 -0.777  -7.797  1.00 20.30 ? 76  LEU   B CA  1 
ATOM   783  C C   . LEU   B 2 67  ? -19.447 -0.085  -6.878  1.00 20.70 ? 76  LEU   B C   1 
ATOM   784  O O   . LEU   B 2 67  ? -19.325 -0.233  -5.667  1.00 21.75 ? 76  LEU   B O   1 
ATOM   785  C CB  . LEU   B 2 67  ? -18.983 -2.202  -8.075  1.00 20.08 ? 76  LEU   B CB  1 
ATOM   786  C CG  . LEU   B 2 67  ? -18.210 -3.014  -9.112  1.00 21.16 ? 76  LEU   B CG  1 
ATOM   787  C CD1 . LEU   B 2 67  ? -18.460 -4.500  -8.942  1.00 21.59 ? 76  LEU   B CD1 1 
ATOM   788  C CD2 . LEU   B 2 67  ? -18.474 -2.511  -10.555 1.00 21.38 ? 76  LEU   B CD2 1 
ATOM   789  N N   . VAL   B 2 68  ? -20.436 0.638   -7.427  1.00 20.31 ? 77  VAL   B N   1 
ATOM   790  C CA  . VAL   B 2 68  ? -21.452 1.318   -6.614  1.00 20.72 ? 77  VAL   B CA  1 
ATOM   791  C C   . VAL   B 2 68  ? -22.821 1.383   -7.351  1.00 21.70 ? 77  VAL   B C   1 
ATOM   792  O O   . VAL   B 2 68  ? -22.879 1.699   -8.543  1.00 22.30 ? 77  VAL   B O   1 
ATOM   793  C CB  . VAL   B 2 68  ? -20.965 2.692   -6.095  1.00 20.82 ? 77  VAL   B CB  1 
ATOM   794  C CG1 . VAL   B 2 68  ? -20.672 3.646   -7.240  1.00 21.55 ? 77  VAL   B CG1 1 
ATOM   795  C CG2 . VAL   B 2 68  ? -21.954 3.301   -5.119  1.00 20.91 ? 77  VAL   B CG2 1 
ATOM   796  N N   . SER   B 2 69  ? -23.910 0.998   -6.650  1.00 21.71 ? 78  SER   B N   1 
ATOM   797  C CA  . SER   B 2 69  ? -25.267 0.971   -7.196  1.00 21.76 ? 78  SER   B CA  1 
ATOM   798  C C   . SER   B 2 69  ? -26.185 1.946   -6.468  1.00 22.27 ? 78  SER   B C   1 
ATOM   799  O O   . SER   B 2 69  ? -26.155 2.022   -5.247  1.00 21.97 ? 78  SER   B O   1 
ATOM   800  C CB  . SER   B 2 69  ? -25.836 -0.443  -7.148  1.00 22.00 ? 78  SER   B CB  1 
ATOM   801  O OG  . SER   B 2 69  ? -25.927 -0.918  -5.820  1.00 22.54 ? 78  SER   B OG  1 
ATOM   802  N N   . TYR   B 2 70  ? -26.990 2.705   -7.227  1.00 22.72 ? 79  TYR   B N   1 
ATOM   803  C CA  . TYR   B 2 70  ? -27.897 3.746   -6.720  1.00 23.36 ? 79  TYR   B CA  1 
ATOM   804  C C   . TYR   B 2 70  ? -29.357 3.310   -6.840  1.00 23.83 ? 79  TYR   B C   1 
ATOM   805  O O   . TYR   B 2 70  ? -29.717 2.645   -7.808  1.00 23.97 ? 79  TYR   B O   1 
ATOM   806  C CB  . TYR   B 2 70  ? -27.668 5.052   -7.514  1.00 23.24 ? 79  TYR   B CB  1 
ATOM   807  C CG  . TYR   B 2 70  ? -26.293 5.642   -7.279  1.00 23.74 ? 79  TYR   B CG  1 
ATOM   808  C CD1 . TYR   B 2 70  ? -25.157 5.040   -7.800  1.00 24.30 ? 79  TYR   B CD1 1 
ATOM   809  C CD2 . TYR   B 2 70  ? -26.125 6.769   -6.491  1.00 24.77 ? 79  TYR   B CD2 1 
ATOM   810  C CE1 . TYR   B 2 70  ? -23.891 5.536   -7.533  1.00 25.23 ? 79  TYR   B CE1 1 
ATOM   811  C CE2 . TYR   B 2 70  ? -24.866 7.286   -6.232  1.00 25.73 ? 79  TYR   B CE2 1 
ATOM   812  C CZ  . TYR   B 2 70  ? -23.749 6.667   -6.758  1.00 26.62 ? 79  TYR   B CZ  1 
ATOM   813  O OH  . TYR   B 2 70  ? -22.496 7.149   -6.470  1.00 28.62 ? 79  TYR   B OH  1 
ATOM   814  N N   . CYS   B 2 71  ? -30.196 3.675   -5.864  1.00 23.77 ? 80  CYS   B N   1 
ATOM   815  C CA  . CYS   B 2 71  ? -31.630 3.339   -5.828  1.00 24.51 ? 80  CYS   B CA  1 
ATOM   816  C C   . CYS   B 2 71  ? -31.912 1.889   -5.422  1.00 23.54 ? 80  CYS   B C   1 
ATOM   817  O O   . CYS   B 2 71  ? -32.999 1.617   -4.919  1.00 24.15 ? 80  CYS   B O   1 
ATOM   818  C CB  . CYS   B 2 71  ? -32.361 3.697   -7.121  1.00 27.14 ? 80  CYS   B CB  1 
ATOM   819  S SG  . CYS   B 2 71  ? -31.988 5.348   -7.768  1.00 35.10 ? 80  CYS   B SG  1 
ATOM   820  N N   . GLY   B 2 72  ? -30.967 0.978   -5.630  1.00 21.93 ? 81  GLY   B N   1 
ATOM   821  C CA  . GLY   B 2 72  ? -31.180 -0.415  -5.266  1.00 21.36 ? 81  GLY   B CA  1 
ATOM   822  C C   . GLY   B 2 72  ? -29.934 -1.260  -5.319  1.00 21.12 ? 81  GLY   B C   1 
ATOM   823  O O   . GLY   B 2 72  ? -28.835 -0.758  -5.546  1.00 20.53 ? 81  GLY   B O   1 
ATOM   824  N N   . PRO   B 2 73  ? -30.099 -2.567  -5.082  1.00 21.78 ? 82  PRO   B N   1 
ATOM   825  C CA  . PRO   B 2 73  ? -28.941 -3.477  -5.116  1.00 22.43 ? 82  PRO   B CA  1 
ATOM   826  C C   . PRO   B 2 73  ? -28.393 -3.714  -6.519  1.00 23.38 ? 82  PRO   B C   1 
ATOM   827  O O   . PRO   B 2 73  ? -29.096 -3.497  -7.505  1.00 23.56 ? 82  PRO   B O   1 
ATOM   828  C CB  . PRO   B 2 73  ? -29.514 -4.785  -4.566  1.00 23.23 ? 82  PRO   B CB  1 
ATOM   829  C CG  . PRO   B 2 73  ? -30.972 -4.728  -4.890  1.00 23.42 ? 82  PRO   B CG  1 
ATOM   830  C CD  . PRO   B 2 73  ? -31.355 -3.281  -4.769  1.00 21.50 ? 82  PRO   B CD  1 
ATOM   831  N N   . TRP   B 2 74  ? -27.156 -4.241  -6.617  1.00 23.56 ? 83  TRP   B N   1 
ATOM   832  C CA  . TRP   B 2 74  ? -26.521 -4.560  -7.893  1.00 23.84 ? 83  TRP   B CA  1 
ATOM   833  C C   . TRP   B 2 74  ? -27.403 -5.551  -8.662  1.00 25.09 ? 83  TRP   B C   1 
ATOM   834  O O   . TRP   B 2 74  ? -27.847 -6.524  -8.060  1.00 25.15 ? 83  TRP   B O   1 
ATOM   835  C CB  . TRP   B 2 74  ? -25.106 -5.120  -7.677  1.00 23.32 ? 83  TRP   B CB  1 
ATOM   836  C CG  . TRP   B 2 74  ? -24.343 -5.238  -8.962  1.00 23.39 ? 83  TRP   B CG  1 
ATOM   837  C CD1 . TRP   B 2 74  ? -24.344 -6.296  -9.816  1.00 24.14 ? 83  TRP   B CD1 1 
ATOM   838  C CD2 . TRP   B 2 74  ? -23.557 -4.219  -9.585  1.00 23.11 ? 83  TRP   B CD2 1 
ATOM   839  N NE1 . TRP   B 2 74  ? -23.585 -6.012  -10.919 1.00 24.45 ? 83  TRP   B NE1 1 
ATOM   840  C CE2 . TRP   B 2 74  ? -23.090 -4.740  -10.805 1.00 24.12 ? 83  TRP   B CE2 1 
ATOM   841  C CE3 . TRP   B 2 74  ? -23.186 -2.923  -9.221  1.00 23.58 ? 83  TRP   B CE3 1 
ATOM   842  C CZ2 . TRP   B 2 74  ? -22.294 -3.999  -11.679 1.00 24.82 ? 83  TRP   B CZ2 1 
ATOM   843  C CZ3 . TRP   B 2 74  ? -22.380 -2.199  -10.074 1.00 24.69 ? 83  TRP   B CZ3 1 
ATOM   844  C CH2 . TRP   B 2 74  ? -21.955 -2.732  -11.296 1.00 24.89 ? 83  TRP   B CH2 1 
ATOM   845  N N   . LYS   B 2 75  ? -27.726 -5.254  -9.952  1.00 25.76 ? 84  LYS   B N   1 
ATOM   846  C CA  . LYS   B 2 75  ? -28.665 -6.025  -10.766 1.00 26.75 ? 84  LYS   B CA  1 
ATOM   847  C C   . LYS   B 2 75  ? -28.056 -6.780  -11.933 1.00 28.95 ? 84  LYS   B C   1 
ATOM   848  O O   . LYS   B 2 75  ? -28.729 -7.631  -12.519 1.00 29.21 ? 84  LYS   B O   1 
ATOM   849  C CB  . LYS   B 2 75  ? -29.743 -5.092  -11.333 1.00 27.30 ? 84  LYS   B CB  1 
ATOM   850  C CG  . LYS   B 2 75  ? -30.625 -4.439  -10.289 1.00 29.71 ? 84  LYS   B CG  1 
ATOM   851  C CD  . LYS   B 2 75  ? -31.822 -5.303  -9.949  1.00 32.65 ? 84  LYS   B CD  1 
ATOM   852  C CE  . LYS   B 2 75  ? -33.005 -4.486  -9.489  1.00 35.18 ? 84  LYS   B CE  1 
ATOM   853  N NZ  . LYS   B 2 75  ? -33.034 -4.337  -8.022  1.00 36.76 ? 84  LYS   B NZ  1 
ATOM   854  N N   . LEU   B 2 76  ? -26.837 -6.414  -12.341 1.00 30.15 ? 85  LEU   B N   1 
ATOM   855  C CA  . LEU   B 2 76  ? -26.178 -7.003  -13.513 1.00 31.02 ? 85  LEU   B CA  1 
ATOM   856  C C   . LEU   B 2 76  ? -25.513 -8.292  -13.068 1.00 33.33 ? 85  LEU   B C   1 
ATOM   857  O O   . LEU   B 2 76  ? -24.682 -8.254  -12.168 1.00 33.41 ? 85  LEU   B O   1 
ATOM   858  C CB  . LEU   B 2 76  ? -25.139 -6.033  -14.090 1.00 30.31 ? 85  LEU   B CB  1 
ATOM   859  C CG  . LEU   B 2 76  ? -25.514 -4.547  -14.133 1.00 30.86 ? 85  LEU   B CG  1 
ATOM   860  C CD1 . LEU   B 2 76  ? -24.383 -3.721  -14.677 1.00 31.52 ? 85  LEU   B CD1 1 
ATOM   861  C CD2 . LEU   B 2 76  ? -26.753 -4.311  -14.951 1.00 30.98 ? 85  LEU   B CD2 1 
ATOM   862  N N   . ASP   B 2 77  ? -25.888 -9.436  -13.661 1.00 35.01 ? 86  ASP   B N   1 
ATOM   863  C CA  . ASP   B 2 77  ? -25.369 -10.722 -13.202 1.00 37.01 ? 86  ASP   B CA  1 
ATOM   864  C C   . ASP   B 2 77  ? -24.808 -11.652 -14.279 1.00 38.88 ? 86  ASP   B C   1 
ATOM   865  O O   . ASP   B 2 77  ? -24.425 -12.762 -13.938 1.00 39.53 ? 86  ASP   B O   1 
ATOM   866  C CB  . ASP   B 2 77  ? -26.448 -11.468 -12.386 1.00 38.77 ? 86  ASP   B CB  1 
ATOM   867  C CG  . ASP   B 2 77  ? -27.729 -11.800 -13.145 1.00 42.87 ? 86  ASP   B CG  1 
ATOM   868  O OD1 . ASP   B 2 77  ? -28.003 -11.141 -14.179 1.00 42.86 ? 86  ASP   B OD1 1 
ATOM   869  O OD2 . ASP   B 2 77  ? -28.467 -12.706 -12.696 1.00 45.07 ? 86  ASP   B OD2 1 
ATOM   870  N N   . ALA   B 2 78  ? -24.743 -11.236 -15.550 1.00 39.83 ? 87  ALA   B N   1 
ATOM   871  C CA  . ALA   B 2 78  ? -24.189 -12.093 -16.613 1.00 40.96 ? 87  ALA   B CA  1 
ATOM   872  C C   . ALA   B 2 78  ? -22.645 -12.104 -16.584 1.00 42.59 ? 87  ALA   B C   1 
ATOM   873  O O   . ALA   B 2 78  ? -22.031 -11.161 -16.075 1.00 42.76 ? 87  ALA   B O   1 
ATOM   874  C CB  . ALA   B 2 78  ? -24.683 -11.632 -17.976 1.00 40.49 ? 87  ALA   B CB  1 
ATOM   875  N N   . ALA   B 2 79  ? -22.014 -13.157 -17.134 1.00 43.40 ? 88  ALA   B N   1 
ATOM   876  C CA  . ALA   B 2 79  ? -20.555 -13.225 -17.161 1.00 44.62 ? 88  ALA   B CA  1 
ATOM   877  C C   . ALA   B 2 79  ? -20.010 -13.815 -18.450 1.00 46.09 ? 88  ALA   B C   1 
ATOM   878  O O   . ALA   B 2 79  ? -20.630 -14.694 -19.051 1.00 46.42 ? 88  ALA   B O   1 
ATOM   879  C CB  . ALA   B 2 79  ? -20.045 -14.009 -15.978 1.00 44.93 ? 88  ALA   B CB  1 
ATOM   880  N N   . TRP   B 2 80  ? -18.817 -13.338 -18.858 1.00 46.64 ? 89  TRP   B N   1 
ATOM   881  C CA  . TRP   B 2 80  ? -18.071 -13.776 -20.030 1.00 47.59 ? 89  TRP   B CA  1 
ATOM   882  C C   . TRP   B 2 80  ? -17.895 -15.297 -19.991 1.00 49.81 ? 89  TRP   B C   1 
ATOM   883  O O   . TRP   B 2 80  ? -17.633 -15.838 -18.914 1.00 50.29 ? 89  TRP   B O   1 
ATOM   884  C CB  . TRP   B 2 80  ? -16.703 -13.080 -20.033 1.00 46.92 ? 89  TRP   B CB  1 
ATOM   885  C CG  . TRP   B 2 80  ? -15.812 -13.447 -21.189 1.00 47.02 ? 89  TRP   B CG  1 
ATOM   886  C CD1 . TRP   B 2 80  ? -16.127 -13.420 -22.521 1.00 47.88 ? 89  TRP   B CD1 1 
ATOM   887  C CD2 . TRP   B 2 80  ? -14.423 -13.784 -21.111 1.00 46.68 ? 89  TRP   B CD2 1 
ATOM   888  N NE1 . TRP   B 2 80  ? -15.026 -13.761 -23.272 1.00 47.97 ? 89  TRP   B NE1 1 
ATOM   889  C CE2 . TRP   B 2 80  ? -13.965 -13.984 -22.428 1.00 47.44 ? 89  TRP   B CE2 1 
ATOM   890  C CE3 . TRP   B 2 80  ? -13.521 -13.937 -20.054 1.00 46.88 ? 89  TRP   B CE3 1 
ATOM   891  C CZ2 . TRP   B 2 80  ? -12.648 -14.334 -22.708 1.00 47.77 ? 89  TRP   B CZ2 1 
ATOM   892  C CZ3 . TRP   B 2 80  ? -12.221 -14.289 -20.335 1.00 47.49 ? 89  TRP   B CZ3 1 
ATOM   893  C CH2 . TRP   B 2 80  ? -11.796 -14.479 -21.649 1.00 47.73 ? 89  TRP   B CH2 1 
ATOM   894  N N   . ASP   B 2 81  ? -18.091 -15.998 -21.129 1.00 51.03 ? 90  ASP   B N   1 
ATOM   895  C CA  . ASP   B 2 81  ? -17.962 -17.460 -21.115 1.00 52.52 ? 90  ASP   B CA  1 
ATOM   896  C C   . ASP   B 2 81  ? -16.509 -17.973 -21.255 1.00 53.69 ? 90  ASP   B C   1 
ATOM   897  O O   . ASP   B 2 81  ? -16.288 -19.185 -21.295 1.00 54.41 ? 90  ASP   B O   1 
ATOM   898  C CB  . ASP   B 2 81  ? -18.891 -18.126 -22.144 1.00 54.19 ? 90  ASP   B CB  1 
ATOM   899  C CG  . ASP   B 2 81  ? -18.708 -17.691 -23.578 1.00 58.85 ? 90  ASP   B CG  1 
ATOM   900  O OD1 . ASP   B 2 81  ? -17.867 -16.803 -23.827 1.00 60.69 ? 90  ASP   B OD1 1 
ATOM   901  O OD2 . ASP   B 2 81  ? -19.407 -18.241 -24.459 1.00 59.37 ? 90  ASP   B OD2 1 
ATOM   902  N N   . GLY   B 2 82  ? -15.537 -17.065 -21.305 1.00 53.42 ? 91  GLY   B N   1 
ATOM   903  C CA  . GLY   B 2 82  ? -14.139 -17.445 -21.452 1.00 53.42 ? 91  GLY   B CA  1 
ATOM   904  C C   . GLY   B 2 82  ? -13.740 -17.832 -22.864 1.00 52.92 ? 91  GLY   B C   1 
ATOM   905  O O   . GLY   B 2 82  ? -12.572 -18.139 -23.113 1.00 53.18 ? 91  GLY   B O   1 
ATOM   906  N N   . LEU   B 2 83  ? -14.695 -17.820 -23.806 1.00 52.14 ? 92  LEU   B N   1 
ATOM   907  C CA  . LEU   B 2 83  ? -14.425 -18.189 -25.179 1.00 51.96 ? 92  LEU   B CA  1 
ATOM   908  C C   . LEU   B 2 83  ? -14.849 -17.137 -26.183 1.00 51.49 ? 92  LEU   B C   1 
ATOM   909  O O   . LEU   B 2 83  ? -14.185 -16.983 -27.203 1.00 51.69 ? 92  LEU   B O   1 
ATOM   910  C CB  . LEU   B 2 83  ? -15.174 -19.475 -25.532 1.00 52.32 ? 92  LEU   B CB  1 
ATOM   911  C CG  . LEU   B 2 83  ? -14.845 -20.722 -24.761 1.00 53.80 ? 92  LEU   B CG  1 
ATOM   912  C CD1 . LEU   B 2 83  ? -15.684 -21.876 -25.269 1.00 54.54 ? 92  LEU   B CD1 1 
ATOM   913  C CD2 . LEU   B 2 83  ? -13.384 -21.063 -24.891 1.00 54.36 ? 92  LEU   B CD2 1 
ATOM   914  N N   . SER   B 2 84  ? -15.984 -16.473 -25.957 1.00 50.61 ? 93  SER   B N   1 
ATOM   915  C CA  . SER   B 2 84  ? -16.526 -15.544 -26.952 1.00 50.29 ? 93  SER   B CA  1 
ATOM   916  C C   . SER   B 2 84  ? -15.929 -14.142 -26.967 1.00 49.06 ? 93  SER   B C   1 
ATOM   917  O O   . SER   B 2 84  ? -15.399 -13.659 -25.969 1.00 49.37 ? 93  SER   B O   1 
ATOM   918  C CB  . SER   B 2 84  ? -18.045 -15.429 -26.810 1.00 52.38 ? 93  SER   B CB  1 
ATOM   919  O OG  . SER   B 2 84  ? -18.659 -16.618 -26.341 1.00 55.24 ? 93  SER   B OG  1 
ATOM   920  N N   . GLU   B 2 85  ? -16.055 -13.476 -28.115 1.00 47.80 ? 94  GLU   B N   1 
ATOM   921  C CA  . GLU   B 2 85  ? -15.693 -12.074 -28.253 1.00 46.61 ? 94  GLU   B CA  1 
ATOM   922  C C   . GLU   B 2 85  ? -16.825 -11.273 -27.582 1.00 44.88 ? 94  GLU   B C   1 
ATOM   923  O O   . GLU   B 2 85  ? -17.964 -11.742 -27.439 1.00 45.29 ? 94  GLU   B O   1 
ATOM   924  C CB  . GLU   B 2 85  ? -15.526 -11.655 -29.734 1.00 48.09 ? 94  GLU   B CB  1 
ATOM   925  C CG  . GLU   B 2 85  ? -14.134 -11.907 -30.303 1.00 50.73 ? 94  GLU   B CG  1 
ATOM   926  C CD  . GLU   B 2 85  ? -13.775 -11.127 -31.558 1.00 53.08 ? 94  GLU   B CD  1 
ATOM   927  O OE1 . GLU   B 2 85  ? -14.702 -10.619 -32.231 1.00 52.23 ? 94  GLU   B OE1 1 
ATOM   928  O OE2 . GLU   B 2 85  ? -12.564 -11.014 -31.865 1.00 53.33 ? 94  GLU   B OE2 1 
ATOM   929  N N   . VAL   B 2 86  ? -16.492 -10.089 -27.115 1.00 42.68 ? 95  VAL   B N   1 
ATOM   930  C CA  . VAL   B 2 86  ? -17.433 -9.228  -26.405 1.00 40.63 ? 95  VAL   B CA  1 
ATOM   931  C C   . VAL   B 2 86  ? -17.408 -7.812  -27.024 1.00 39.06 ? 95  VAL   B C   1 
ATOM   932  O O   . VAL   B 2 86  ? -16.604 -7.542  -27.923 1.00 38.94 ? 95  VAL   B O   1 
ATOM   933  C CB  . VAL   B 2 86  ? -17.116 -9.232  -24.867 1.00 39.73 ? 95  VAL   B CB  1 
ATOM   934  C CG1 . VAL   B 2 86  ? -17.196 -10.632 -24.290 1.00 39.78 ? 95  VAL   B CG1 1 
ATOM   935  C CG2 . VAL   B 2 86  ? -15.750 -8.630  -24.592 1.00 39.66 ? 95  VAL   B CG2 1 
ATOM   936  N N   . GLN   B 2 87  ? -18.283 -6.913  -26.554 1.00 37.85 ? 96  GLN   B N   1 
ATOM   937  C CA  . GLN   B 2 87  ? -18.299 -5.545  -27.048 1.00 36.96 ? 96  GLN   B CA  1 
ATOM   938  C C   . GLN   B 2 87  ? -18.220 -4.534  -25.910 1.00 35.51 ? 96  GLN   B C   1 
ATOM   939  O O   . GLN   B 2 87  ? -19.084 -4.520  -25.045 1.00 35.63 ? 96  GLN   B O   1 
ATOM   940  C CB  . GLN   B 2 87  ? -19.528 -5.270  -27.943 1.00 37.65 ? 96  GLN   B CB  1 
ATOM   941  C CG  . GLN   B 2 87  ? -19.252 -5.462  -29.428 1.00 39.95 ? 96  GLN   B CG  1 
ATOM   942  C CD  . GLN   B 2 87  ? -20.419 -5.098  -30.332 1.00 42.15 ? 96  GLN   B CD  1 
ATOM   943  O OE1 . GLN   B 2 87  ? -21.281 -4.274  -30.004 1.00 41.77 ? 96  GLN   B OE1 1 
ATOM   944  N NE2 . GLN   B 2 87  ? -20.459 -5.714  -31.508 1.00 42.77 ? 96  GLN   B NE2 1 
ATOM   945  N N   . LEU   B 2 88  ? -17.197 -3.677  -25.924 1.00 33.96 ? 97  LEU   B N   1 
ATOM   946  C CA  . LEU   B 2 88  ? -17.111 -2.577  -24.979 1.00 32.93 ? 97  LEU   B CA  1 
ATOM   947  C C   . LEU   B 2 88  ? -17.968 -1.470  -25.596 1.00 32.41 ? 97  LEU   B C   1 
ATOM   948  O O   . LEU   B 2 88  ? -17.604 -0.960  -26.664 1.00 32.76 ? 97  LEU   B O   1 
ATOM   949  C CB  . LEU   B 2 88  ? -15.657 -2.070  -24.851 1.00 32.45 ? 97  LEU   B CB  1 
ATOM   950  C CG  . LEU   B 2 88  ? -15.473 -0.728  -24.118 1.00 33.09 ? 97  LEU   B CG  1 
ATOM   951  C CD1 . LEU   B 2 88  ? -15.950 -0.810  -22.669 1.00 34.04 ? 97  LEU   B CD1 1 
ATOM   952  C CD2 . LEU   B 2 88  ? -14.047 -0.231  -24.206 1.00 33.07 ? 97  LEU   B CD2 1 
ATOM   953  N N   . LEU   B 2 89  ? -19.108 -1.123  -24.974 1.00 31.33 ? 98  LEU   B N   1 
ATOM   954  C CA  . LEU   B 2 89  ? -19.898 -0.003  -25.466 1.00 30.79 ? 98  LEU   B CA  1 
ATOM   955  C C   . LEU   B 2 89  ? -19.247 1.169   -24.776 1.00 31.38 ? 98  LEU   B C   1 
ATOM   956  O O   . LEU   B 2 89  ? -19.581 1.478   -23.625 1.00 31.78 ? 98  LEU   B O   1 
ATOM   957  C CB  . LEU   B 2 89  ? -21.376 -0.127  -25.091 1.00 30.31 ? 98  LEU   B CB  1 
ATOM   958  C CG  . LEU   B 2 89  ? -22.233 1.143   -25.212 1.00 31.56 ? 98  LEU   B CG  1 
ATOM   959  C CD1 . LEU   B 2 89  ? -22.094 1.815   -26.559 1.00 32.45 ? 98  LEU   B CD1 1 
ATOM   960  C CD2 . LEU   B 2 89  ? -23.670 0.834   -24.986 1.00 32.24 ? 98  LEU   B CD2 1 
ATOM   961  N N   . ALA   B 2 90  ? -18.212 1.725   -25.412 1.00 31.26 ? 99  ALA   B N   1 
ATOM   962  C CA  . ALA   B 2 90  ? -17.438 2.780   -24.785 1.00 32.12 ? 99  ALA   B CA  1 
ATOM   963  C C   . ALA   B 2 90  ? -18.030 4.119   -25.059 1.00 32.60 ? 99  ALA   B C   1 
ATOM   964  O O   . ALA   B 2 90  ? -18.224 4.451   -26.224 1.00 32.49 ? 99  ALA   B O   1 
ATOM   965  C CB  . ALA   B 2 90  ? -16.003 2.747   -25.273 1.00 32.45 ? 99  ALA   B CB  1 
ATOM   966  N N   . VAL   B 2 91  ? -18.305 4.897   -23.983 1.00 32.59 ? 100 VAL   B N   1 
ATOM   967  C CA  . VAL   B 2 91  ? -18.838 6.259   -24.066 1.00 33.02 ? 100 VAL   B CA  1 
ATOM   968  C C   . VAL   B 2 91  ? -17.698 7.254   -23.732 1.00 34.74 ? 100 VAL   B C   1 
ATOM   969  O O   . VAL   B 2 91  ? -17.465 7.563   -22.568 1.00 34.77 ? 100 VAL   B O   1 
ATOM   970  C CB  . VAL   B 2 91  ? -20.061 6.427   -23.137 1.00 32.30 ? 100 VAL   B CB  1 
ATOM   971  C CG1 . VAL   B 2 91  ? -20.622 7.841   -23.198 1.00 32.50 ? 100 VAL   B CG1 1 
ATOM   972  C CG2 . VAL   B 2 91  ? -21.138 5.399   -23.457 1.00 32.19 ? 100 VAL   B CG2 1 
ATOM   973  N N   . PRO   B 2 92  ? -16.926 7.722   -24.738 1.00 35.88 ? 101 PRO   B N   1 
ATOM   974  C CA  . PRO   B 2 92  ? -15.798 8.624   -24.439 1.00 36.94 ? 101 PRO   B CA  1 
ATOM   975  C C   . PRO   B 2 92  ? -16.190 10.081  -24.150 1.00 38.62 ? 101 PRO   B C   1 
ATOM   976  O O   . PRO   B 2 92  ? -17.197 10.579  -24.667 1.00 39.00 ? 101 PRO   B O   1 
ATOM   977  C CB  . PRO   B 2 92  ? -14.912 8.509   -25.691 1.00 37.04 ? 101 PRO   B CB  1 
ATOM   978  C CG  . PRO   B 2 92  ? -15.599 7.524   -26.603 1.00 36.96 ? 101 PRO   B CG  1 
ATOM   979  C CD  . PRO   B 2 92  ? -17.013 7.439   -26.179 1.00 35.22 ? 101 PRO   B CD  1 
ATOM   980  N N   . PRO   B 2 93  ? -15.381 10.789  -23.336 1.00 39.29 ? 102 PRO   B N   1 
ATOM   981  C CA  . PRO   B 2 93  ? -15.686 12.202  -23.040 1.00 39.92 ? 102 PRO   B CA  1 
ATOM   982  C C   . PRO   B 2 93  ? -15.722 13.070  -24.291 1.00 41.04 ? 102 PRO   B C   1 
ATOM   983  O O   . PRO   B 2 93  ? -14.824 13.002  -25.138 1.00 41.01 ? 102 PRO   B O   1 
ATOM   984  C CB  . PRO   B 2 93  ? -14.540 12.635  -22.116 1.00 40.48 ? 102 PRO   B CB  1 
ATOM   985  C CG  . PRO   B 2 93  ? -13.968 11.367  -21.581 1.00 40.74 ? 102 PRO   B CG  1 
ATOM   986  C CD  . PRO   B 2 93  ? -14.168 10.329  -22.634 1.00 38.86 ? 102 PRO   B CD  1 
ATOM   987  N N   . GLY   B 2 94  ? -16.788 13.847  -24.420 1.00 41.65 ? 103 GLY   B N   1 
ATOM   988  C CA  . GLY   B 2 94  ? -16.977 14.729  -25.565 1.00 42.55 ? 103 GLY   B CA  1 
ATOM   989  C C   . GLY   B 2 94  ? -17.357 14.031  -26.859 1.00 43.39 ? 103 GLY   B C   1 
ATOM   990  O O   . GLY   B 2 94  ? -17.798 14.682  -27.811 1.00 43.46 ? 103 GLY   B O   1 
ATOM   991  N N   . GLU   B 2 95  ? -17.178 12.710  -26.921 1.00 43.79 ? 104 GLU   B N   1 
ATOM   992  C CA  . GLU   B 2 95  ? -17.509 11.952  -28.122 1.00 44.75 ? 104 GLU   B CA  1 
ATOM   993  C C   . GLU   B 2 95  ? -18.749 11.074  -27.910 1.00 44.76 ? 104 GLU   B C   1 
ATOM   994  O O   . GLU   B 2 95  ? -19.105 10.756  -26.768 1.00 45.01 ? 104 GLU   B O   1 
ATOM   995  C CB  . GLU   B 2 95  ? -16.303 11.113  -28.590 1.00 47.66 ? 104 GLU   B CB  1 
ATOM   996  C CG  . GLU   B 2 95  ? -15.015 11.912  -28.716 1.00 53.14 ? 104 GLU   B CG  1 
ATOM   997  C CD  . GLU   B 2 95  ? -13.748 11.078  -28.738 1.00 60.19 ? 104 GLU   B CD  1 
ATOM   998  O OE1 . GLU   B 2 95  ? -13.847 9.845   -28.935 1.00 61.69 ? 104 GLU   B OE1 1 
ATOM   999  O OE2 . GLU   B 2 95  ? -12.653 11.659  -28.563 1.00 62.60 ? 104 GLU   B OE2 1 
ATOM   1000 N N   . ARG   B 2 96  ? -19.386 10.677  -29.014 1.00 44.09 ? 105 ARG   B N   1 
ATOM   1001 C CA  . ARG   B 2 96  ? -20.580 9.843   -29.054 1.00 44.52 ? 105 ARG   B CA  1 
ATOM   1002 C C   . ARG   B 2 96  ? -20.267 8.389   -28.677 1.00 43.86 ? 105 ARG   B C   1 
ATOM   1003 O O   . ARG   B 2 96  ? -19.152 7.937   -28.927 1.00 43.92 ? 105 ARG   B O   1 
ATOM   1004 C CB  . ARG   B 2 96  ? -21.143 9.913   -30.483 1.00 47.34 ? 105 ARG   B CB  1 
ATOM   1005 C CG  . ARG   B 2 96  ? -22.383 9.075   -30.763 1.00 52.42 ? 105 ARG   B CG  1 
ATOM   1006 C CD  . ARG   B 2 96  ? -23.180 9.615   -31.934 1.00 57.50 ? 105 ARG   B CD  1 
ATOM   1007 N NE  . ARG   B 2 96  ? -22.387 9.743   -33.163 1.00 62.24 ? 105 ARG   B NE  1 
ATOM   1008 C CZ  . ARG   B 2 96  ? -22.074 10.906  -33.732 1.00 65.87 ? 105 ARG   B CZ  1 
ATOM   1009 N NH1 . ARG   B 2 96  ? -22.468 12.052  -33.182 1.00 65.91 ? 105 ARG   B NH1 1 
ATOM   1010 N NH2 . ARG   B 2 96  ? -21.370 10.933  -34.857 1.00 65.73 ? 105 ARG   B NH2 1 
ATOM   1011 N N   . ALA   B 2 97  ? -21.248 7.655   -28.090 1.00 43.25 ? 106 ALA   B N   1 
ATOM   1012 C CA  . ALA   B 2 97  ? -21.118 6.239   -27.720 1.00 43.38 ? 106 ALA   B CA  1 
ATOM   1013 C C   . ALA   B 2 97  ? -20.675 5.405   -28.929 1.00 43.76 ? 106 ALA   B C   1 
ATOM   1014 O O   . ALA   B 2 97  ? -21.137 5.647   -30.035 1.00 43.85 ? 106 ALA   B O   1 
ATOM   1015 C CB  . ALA   B 2 97  ? -22.440 5.716   -27.191 1.00 43.38 ? 106 ALA   B CB  1 
ATOM   1016 N N   . LYS   B 2 98  ? -19.769 4.444   -28.725 1.00 43.97 ? 107 LYS   B N   1 
ATOM   1017 C CA  . LYS   B 2 98  ? -19.181 3.664   -29.812 1.00 44.46 ? 107 LYS   B CA  1 
ATOM   1018 C C   . LYS   B 2 98  ? -18.907 2.206   -29.398 1.00 44.14 ? 107 LYS   B C   1 
ATOM   1019 O O   . LYS   B 2 98  ? -18.203 1.983   -28.419 1.00 44.58 ? 107 LYS   B O   1 
ATOM   1020 C CB  . LYS   B 2 98  ? -17.863 4.361   -30.175 1.00 47.43 ? 107 LYS   B CB  1 
ATOM   1021 C CG  . LYS   B 2 98  ? -17.082 3.782   -31.345 1.00 53.79 ? 107 LYS   B CG  1 
ATOM   1022 C CD  . LYS   B 2 98  ? -15.673 4.419   -31.440 1.00 59.97 ? 107 LYS   B CD  1 
ATOM   1023 C CE  . LYS   B 2 98  ? -14.923 4.440   -30.108 1.00 64.53 ? 107 LYS   B CE  1 
ATOM   1024 N NZ  . LYS   B 2 98  ? -13.486 4.819   -30.258 1.00 67.17 ? 107 LYS   B NZ  1 
ATOM   1025 N N   . ASN   B 2 99  ? -19.455 1.217   -30.126 1.00 43.38 ? 108 ASN   B N   1 
ATOM   1026 C CA  . ASN   B 2 99  ? -19.222 -0.197  -29.797 1.00 43.34 ? 108 ASN   B CA  1 
ATOM   1027 C C   . ASN   B 2 99  ? -17.924 -0.721  -30.391 1.00 43.64 ? 108 ASN   B C   1 
ATOM   1028 O O   . ASN   B 2 99  ? -17.724 -0.639  -31.595 1.00 44.51 ? 108 ASN   B O   1 
ATOM   1029 C CB  . ASN   B 2 99  ? -20.364 -1.085  -30.277 1.00 43.69 ? 108 ASN   B CB  1 
ATOM   1030 C CG  . ASN   B 2 99  ? -21.691 -0.763  -29.664 1.00 45.61 ? 108 ASN   B CG  1 
ATOM   1031 O OD1 . ASN   B 2 99  ? -22.120 0.385   -29.652 1.00 46.93 ? 108 ASN   B OD1 1 
ATOM   1032 N ND2 . ASN   B 2 99  ? -22.386 -1.774  -29.171 1.00 45.28 ? 108 ASN   B ND2 1 
ATOM   1033 N N   . ILE   B 2 100 ? -17.056 -1.281  -29.564 1.00 43.34 ? 109 ILE   B N   1 
ATOM   1034 C CA  . ILE   B 2 100 ? -15.790 -1.830  -30.025 1.00 43.60 ? 109 ILE   B CA  1 
ATOM   1035 C C   . ILE   B 2 100 ? -15.747 -3.290  -29.667 1.00 43.97 ? 109 ILE   B C   1 
ATOM   1036 O O   . ILE   B 2 100 ? -15.819 -3.632  -28.490 1.00 43.99 ? 109 ILE   B O   1 
ATOM   1037 C CB  . ILE   B 2 100 ? -14.618 -1.098  -29.364 1.00 44.08 ? 109 ILE   B CB  1 
ATOM   1038 C CG1 . ILE   B 2 100 ? -14.724 0.431   -29.550 1.00 45.15 ? 109 ILE   B CG1 1 
ATOM   1039 C CG2 . ILE   B 2 100 ? -13.285 -1.674  -29.842 1.00 44.25 ? 109 ILE   B CG2 1 
ATOM   1040 C CD1 . ILE   B 2 100 ? -14.482 0.934   -30.952 1.00 46.39 ? 109 ILE   B CD1 1 
ATOM   1041 N N   . GLN   B 2 101 ? -15.623 -4.153  -30.660 1.00 44.15 ? 110 GLN   B N   1 
ATOM   1042 C CA  . GLN   B 2 101 ? -15.587 -5.587  -30.423 1.00 45.13 ? 110 GLN   B CA  1 
ATOM   1043 C C   . GLN   B 2 101 ? -14.152 -6.083  -30.229 1.00 45.78 ? 110 GLN   B C   1 
ATOM   1044 O O   . GLN   B 2 101 ? -13.251 -5.626  -30.933 1.00 45.87 ? 110 GLN   B O   1 
ATOM   1045 C CB  . GLN   B 2 101 ? -16.268 -6.322  -31.578 1.00 46.84 ? 110 GLN   B CB  1 
ATOM   1046 C CG  . GLN   B 2 101 ? -16.701 -7.714  -31.188 1.00 49.93 ? 110 GLN   B CG  1 
ATOM   1047 C CD  . GLN   B 2 101 ? -17.455 -8.345  -32.306 1.00 52.73 ? 110 GLN   B CD  1 
ATOM   1048 O OE1 . GLN   B 2 101 ? -18.343 -7.733  -32.898 1.00 53.28 ? 110 GLN   B OE1 1 
ATOM   1049 N NE2 . GLN   B 2 101 ? -17.118 -9.583  -32.604 1.00 53.26 ? 110 GLN   B NE2 1 
ATOM   1050 N N   . THR   B 2 102 ? -13.939 -7.013  -29.265 1.00 45.81 ? 111 THR   B N   1 
ATOM   1051 C CA  . THR   B 2 102 ? -12.625 -7.590  -28.955 1.00 46.24 ? 111 THR   B CA  1 
ATOM   1052 C C   . THR   B 2 102 ? -12.757 -8.968  -28.275 1.00 46.53 ? 111 THR   B C   1 
ATOM   1053 O O   . THR   B 2 102 ? -13.852 -9.333  -27.855 1.00 46.69 ? 111 THR   B O   1 
ATOM   1054 C CB  . THR   B 2 102 ? -11.851 -6.635  -28.020 1.00 47.86 ? 111 THR   B CB  1 
ATOM   1055 O OG1 . THR   B 2 102 ? -10.526 -7.146  -27.838 1.00 49.00 ? 111 THR   B OG1 1 
ATOM   1056 C CG2 . THR   B 2 102 ? -12.530 -6.459  -26.664 1.00 48.36 ? 111 THR   B CG2 1 
ATOM   1057 N N   . LEU   B 2 103 ? -11.643 -9.733  -28.149 1.00 46.19 ? 112 LEU   B N   1 
ATOM   1058 C CA  . LEU   B 2 103 ? -11.654 -10.991 -27.405 1.00 46.13 ? 112 LEU   B CA  1 
ATOM   1059 C C   . LEU   B 2 103 ? -10.874 -10.715 -26.132 1.00 46.52 ? 112 LEU   B C   1 
ATOM   1060 O O   . LEU   B 2 103 ? -9.684  -10.403 -26.206 1.00 46.86 ? 112 LEU   B O   1 
ATOM   1061 C CB  . LEU   B 2 103 ? -10.987 -12.150 -28.156 1.00 45.86 ? 112 LEU   B CB  1 
ATOM   1062 C CG  . LEU   B 2 103 ? -11.001 -13.455 -27.355 1.00 46.88 ? 112 LEU   B CG  1 
ATOM   1063 C CD1 . LEU   B 2 103 ? -12.287 -14.191 -27.553 1.00 47.27 ? 112 LEU   B CD1 1 
ATOM   1064 C CD2 . LEU   B 2 103 ? -9.839  -14.334 -27.692 1.00 47.49 ? 112 LEU   B CD2 1 
ATOM   1065 N N   . PRO   B 2 104 ? -11.510 -10.790 -24.959 1.00 46.19 ? 113 PRO   B N   1 
ATOM   1066 C CA  . PRO   B 2 104 ? -10.771 -10.483 -23.732 1.00 46.17 ? 113 PRO   B CA  1 
ATOM   1067 C C   . PRO   B 2 104 ? -9.727  -11.529 -23.374 1.00 46.69 ? 113 PRO   B C   1 
ATOM   1068 O O   . PRO   B 2 104 ? -9.806  -12.688 -23.785 1.00 46.90 ? 113 PRO   B O   1 
ATOM   1069 C CB  . PRO   B 2 104 ? -11.852 -10.300 -22.660 1.00 46.54 ? 113 PRO   B CB  1 
ATOM   1070 C CG  . PRO   B 2 104 ? -13.119 -10.666 -23.272 1.00 47.12 ? 113 PRO   B CG  1 
ATOM   1071 C CD  . PRO   B 2 104 ? -12.918 -11.128 -24.691 1.00 45.69 ? 113 PRO   B CD  1 
ATOM   1072 N N   . GLY   B 2 105 ? -8.708  -11.061 -22.673 1.00 46.49 ? 114 GLY   B N   1 
ATOM   1073 C CA  . GLY   B 2 105 ? -7.640  -11.883 -22.138 1.00 46.59 ? 114 GLY   B CA  1 
ATOM   1074 C C   . GLY   B 2 105 ? -7.955  -12.271 -20.706 1.00 46.09 ? 114 GLY   B C   1 
ATOM   1075 O O   . GLY   B 2 105 ? -9.116  -12.221 -20.286 1.00 46.07 ? 114 GLY   B O   1 
ATOM   1076 N N   . ILE   B 2 106 ? -6.929  -12.660 -19.938 1.00 45.76 ? 115 ILE   B N   1 
ATOM   1077 C CA  . ILE   B 2 106 ? -7.095  -13.119 -18.555 1.00 45.88 ? 115 ILE   B CA  1 
ATOM   1078 C C   . ILE   B 2 106 ? -6.214  -12.366 -17.549 1.00 45.92 ? 115 ILE   B C   1 
ATOM   1079 O O   . ILE   B 2 106 ? -5.075  -12.030 -17.850 1.00 45.83 ? 115 ILE   B O   1 
ATOM   1080 C CB  . ILE   B 2 106 ? -6.759  -14.638 -18.513 1.00 46.57 ? 115 ILE   B CB  1 
ATOM   1081 C CG1 . ILE   B 2 106 ? -7.703  -15.473 -19.395 1.00 47.49 ? 115 ILE   B CG1 1 
ATOM   1082 C CG2 . ILE   B 2 106 ? -6.682  -15.197 -17.091 1.00 47.39 ? 115 ILE   B CG2 1 
ATOM   1083 C CD1 . ILE   B 2 106 ? -9.077  -15.461 -18.961 1.00 48.60 ? 115 ILE   B CD1 1 
ATOM   1084 N N   . PHE   B 2 107 ? -6.737  -12.145 -16.341 1.00 46.08 ? 116 PHE   B N   1 
ATOM   1085 C CA  . PHE   B 2 107 ? -6.005  -11.586 -15.207 1.00 46.80 ? 116 PHE   B CA  1 
ATOM   1086 C C   . PHE   B 2 107 ? -5.843  -12.752 -14.242 1.00 47.51 ? 116 PHE   B C   1 
ATOM   1087 O O   . PHE   B 2 107 ? -6.801  -13.095 -13.566 1.00 47.74 ? 116 PHE   B O   1 
ATOM   1088 C CB  . PHE   B 2 107 ? -6.829  -10.497 -14.500 1.00 46.56 ? 116 PHE   B CB  1 
ATOM   1089 C CG  . PHE   B 2 107 ? -6.642  -9.076  -14.978 1.00 47.11 ? 116 PHE   B CG  1 
ATOM   1090 C CD1 . PHE   B 2 107 ? -5.908  -8.800  -16.122 1.00 47.97 ? 116 PHE   B CD1 1 
ATOM   1091 C CD2 . PHE   B 2 107 ? -7.233  -8.019  -14.306 1.00 47.72 ? 116 PHE   B CD2 1 
ATOM   1092 C CE1 . PHE   B 2 107 ? -5.746  -7.493  -16.565 1.00 48.68 ? 116 PHE   B CE1 1 
ATOM   1093 C CE2 . PHE   B 2 107 ? -7.068  -6.716  -14.750 1.00 48.53 ? 116 PHE   B CE2 1 
ATOM   1094 C CZ  . PHE   B 2 107 ? -6.342  -6.463  -15.887 1.00 48.60 ? 116 PHE   B CZ  1 
ATOM   1095 N N   . LYS   B 2 108 ? -4.675  -13.399 -14.214 1.00 47.74 ? 117 LYS   B N   1 
ATOM   1096 C CA  . LYS   B 2 108 ? -4.441  -14.533 -13.332 1.00 48.35 ? 117 LYS   B CA  1 
ATOM   1097 C C   . LYS   B 2 108 ? -4.175  -14.058 -11.910 1.00 48.95 ? 117 LYS   B C   1 
ATOM   1098 O O   . LYS   B 2 108 ? -3.113  -13.501 -11.638 1.00 49.20 ? 117 LYS   B O   1 
ATOM   1099 C CB  . LYS   B 2 108 ? -3.270  -15.382 -13.850 1.00 50.70 ? 117 LYS   B CB  1 
ATOM   1100 C CG  . LYS   B 2 108 ? -3.543  -16.034 -15.202 1.00 56.50 ? 117 LYS   B CG  1 
ATOM   1101 C CD  . LYS   B 2 108 ? -2.380  -16.911 -15.690 1.00 63.54 ? 117 LYS   B CD  1 
ATOM   1102 C CE  . LYS   B 2 108 ? -2.656  -17.496 -17.070 1.00 70.12 ? 117 LYS   B CE  1 
ATOM   1103 N NZ  . LYS   B 2 108 ? -1.444  -18.079 -17.733 1.00 73.36 ? 117 LYS   B NZ  1 
ATOM   1104 N N   . THR   B 2 109 ? -5.141  -14.263 -10.997 1.00 48.86 ? 118 THR   B N   1 
ATOM   1105 C CA  . THR   B 2 109 ? -4.981  -13.854 -9.597  1.00 49.00 ? 118 THR   B CA  1 
ATOM   1106 C C   . THR   B 2 109 ? -4.961  -15.069 -8.644  1.00 49.01 ? 118 THR   B C   1 
ATOM   1107 O O   . THR   B 2 109 ? -5.269  -16.190 -9.055  1.00 49.10 ? 118 THR   B O   1 
ATOM   1108 C CB  . THR   B 2 109 ? -6.039  -12.768 -9.176  1.00 50.09 ? 118 THR   B CB  1 
ATOM   1109 O OG1 . THR   B 2 109 ? -7.270  -13.364 -8.750  1.00 50.69 ? 118 THR   B OG1 1 
ATOM   1110 C CG2 . THR   B 2 109 ? -6.291  -11.723 -10.246 1.00 50.45 ? 118 THR   B CG2 1 
ATOM   1111 N N   . LYS   B 2 110 ? -4.598  -14.841 -7.368  1.00 48.62 ? 119 LYS   B N   1 
ATOM   1112 C CA  . LYS   B 2 110 ? -4.611  -15.873 -6.336  1.00 48.83 ? 119 LYS   B CA  1 
ATOM   1113 C C   . LYS   B 2 110 ? -6.064  -16.266 -5.925  1.00 49.33 ? 119 LYS   B C   1 
ATOM   1114 O O   . LYS   B 2 110 ? -6.246  -17.283 -5.254  1.00 49.66 ? 119 LYS   B O   1 
ATOM   1115 C CB  . LYS   B 2 110 ? -3.811  -15.400 -5.108  1.00 49.62 ? 119 LYS   B CB  1 
ATOM   1116 C CG  . LYS   B 2 110 ? -4.505  -14.310 -4.304  1.00 52.67 ? 119 LYS   B CG  1 
ATOM   1117 C CD  . LYS   B 2 110 ? -3.632  -13.819 -3.160  1.00 56.85 ? 119 LYS   B CD  1 
ATOM   1118 C CE  . LYS   B 2 110 ? -4.375  -12.963 -2.157  1.00 60.12 ? 119 LYS   B CE  1 
ATOM   1119 N NZ  . LYS   B 2 110 ? -4.281  -11.513 -2.469  1.00 62.03 ? 119 LYS   B NZ  1 
ATOM   1120 N N   . ASP   B 2 111 ? -7.084  -15.458 -6.319  1.00 48.93 ? 120 ASP   B N   1 
ATOM   1121 C CA  . ASP   B 2 111 ? -8.497  -15.673 -6.012  1.00 48.80 ? 120 ASP   B CA  1 
ATOM   1122 C C   . ASP   B 2 111 ? -9.363  -15.948 -7.249  1.00 48.58 ? 120 ASP   B C   1 
ATOM   1123 O O   . ASP   B 2 111 ? -10.568 -15.703 -7.214  1.00 48.82 ? 120 ASP   B O   1 
ATOM   1124 C CB  . ASP   B 2 111 ? -9.061  -14.452 -5.287  1.00 50.32 ? 120 ASP   B CB  1 
ATOM   1125 C CG  . ASP   B 2 111 ? -8.434  -14.192 -3.947  1.00 54.87 ? 120 ASP   B CG  1 
ATOM   1126 O OD1 . ASP   B 2 111 ? -8.070  -15.176 -3.261  1.00 55.43 ? 120 ASP   B OD1 1 
ATOM   1127 O OD2 . ASP   B 2 111 ? -8.324  -13.006 -3.568  1.00 57.25 ? 120 ASP   B OD2 1 
ATOM   1128 N N   . GLY   B 2 112 ? -8.759  -16.425 -8.330  1.00 48.00 ? 121 GLY   B N   1 
ATOM   1129 C CA  . GLY   B 2 112 ? -9.508  -16.756 -9.538  1.00 47.77 ? 121 GLY   B CA  1 
ATOM   1130 C C   . GLY   B 2 112 ? -9.231  -15.918 -10.767 1.00 47.04 ? 121 GLY   B C   1 
ATOM   1131 O O   . GLY   B 2 112 ? -8.683  -14.819 -10.672 1.00 47.16 ? 121 GLY   B O   1 
ATOM   1132 N N   . ASP   B 2 113 ? -9.622  -16.434 -11.937 1.00 46.21 ? 122 ASP   B N   1 
ATOM   1133 C CA  . ASP   B 2 113 ? -9.435  -15.711 -13.195 1.00 45.90 ? 122 ASP   B CA  1 
ATOM   1134 C C   . ASP   B 2 113 ? -10.563 -14.702 -13.451 1.00 44.95 ? 122 ASP   B C   1 
ATOM   1135 O O   . ASP   B 2 113 ? -11.703 -14.881 -13.003 1.00 44.43 ? 122 ASP   B O   1 
ATOM   1136 C CB  . ASP   B 2 113 ? -9.282  -16.664 -14.395 1.00 47.42 ? 122 ASP   B CB  1 
ATOM   1137 C CG  . ASP   B 2 113 ? -8.055  -17.556 -14.367 1.00 52.59 ? 122 ASP   B CG  1 
ATOM   1138 O OD1 . ASP   B 2 113 ? -7.283  -17.482 -13.380 1.00 53.48 ? 122 ASP   B OD1 1 
ATOM   1139 O OD2 . ASP   B 2 113 ? -7.870  -18.337 -15.324 1.00 55.37 ? 122 ASP   B OD2 1 
ATOM   1140 N N   . ILE   B 2 114 ? -10.215 -13.613 -14.152 1.00 44.19 ? 123 ILE   B N   1 
ATOM   1141 C CA  . ILE   B 2 114 ? -11.133 -12.533 -14.510 1.00 43.60 ? 123 ILE   B CA  1 
ATOM   1142 C C   . ILE   B 2 114 ? -10.813 -12.144 -15.952 1.00 43.06 ? 123 ILE   B C   1 
ATOM   1143 O O   . ILE   B 2 114 ? -9.644  -12.094 -16.334 1.00 42.97 ? 123 ILE   B O   1 
ATOM   1144 C CB  . ILE   B 2 114 ? -10.986 -11.302 -13.562 1.00 43.68 ? 123 ILE   B CB  1 
ATOM   1145 C CG1 . ILE   B 2 114 ? -10.923 -11.703 -12.106 1.00 45.02 ? 123 ILE   B CG1 1 
ATOM   1146 C CG2 . ILE   B 2 114 ? -12.077 -10.267 -13.774 1.00 43.87 ? 123 ILE   B CG2 1 
ATOM   1147 C CD1 . ILE   B 2 114 ? -9.639  -11.409 -11.469 1.00 46.62 ? 123 ILE   B CD1 1 
ATOM   1148 N N   . GLY   B 2 115 ? -11.840 -11.875 -16.739 1.00 42.69 ? 124 GLY   B N   1 
ATOM   1149 C CA  . GLY   B 2 115 ? -11.645 -11.435 -18.114 1.00 43.21 ? 124 GLY   B CA  1 
ATOM   1150 C C   . GLY   B 2 115 ? -11.074 -10.031 -18.156 1.00 43.18 ? 124 GLY   B C   1 
ATOM   1151 O O   . GLY   B 2 115 ? -11.279 -9.252  -17.219 1.00 43.41 ? 124 GLY   B O   1 
ATOM   1152 N N   . ALA   B 2 116 ? -10.352 -9.693  -19.228 1.00 42.71 ? 125 ALA   B N   1 
ATOM   1153 C CA  . ALA   B 2 116 ? -9.764  -8.360  -19.337 1.00 42.87 ? 125 ALA   B CA  1 
ATOM   1154 C C   . ALA   B 2 116 ? -9.698  -7.807  -20.766 1.00 42.78 ? 125 ALA   B C   1 
ATOM   1155 O O   . ALA   B 2 116 ? -9.213  -8.462  -21.670 1.00 43.23 ? 125 ALA   B O   1 
ATOM   1156 C CB  . ALA   B 2 116 ? -8.395  -8.338  -18.699 1.00 42.87 ? 125 ALA   B CB  1 
ATOM   1157 N N   . VAL   B 2 117 ? -10.182 -6.590  -20.947 1.00 42.07 ? 126 VAL   B N   1 
ATOM   1158 C CA  A VAL   B 2 117 ? -10.164 -5.933  -22.243 0.50 42.18 ? 126 VAL   B CA  1 
ATOM   1159 C CA  B VAL   B 2 117 ? -10.212 -5.892  -22.218 0.50 42.25 ? 126 VAL   B CA  1 
ATOM   1160 C C   . VAL   B 2 117 ? -8.918  -5.060  -22.396 1.00 42.36 ? 126 VAL   B C   1 
ATOM   1161 O O   . VAL   B 2 117 ? -8.542  -4.318  -21.488 1.00 43.04 ? 126 VAL   B O   1 
ATOM   1162 C CB  A VAL   B 2 117 ? -11.478 -5.186  -22.560 0.50 42.81 ? 126 VAL   B CB  1 
ATOM   1163 C CB  B VAL   B 2 117 ? -11.530 -5.064  -22.248 0.50 43.02 ? 126 VAL   B CB  1 
ATOM   1164 C CG1 A VAL   B 2 117 ? -12.627 -6.174  -22.725 0.50 43.38 ? 126 VAL   B CG1 1 
ATOM   1165 C CG1 B VAL   B 2 117 ? -11.352 -3.649  -22.791 0.50 43.59 ? 126 VAL   B CG1 1 
ATOM   1166 C CG2 A VAL   B 2 117 ? -11.806 -4.145  -21.493 0.50 43.21 ? 126 VAL   B CG2 1 
ATOM   1167 C CG2 B VAL   B 2 117 ? -12.633 -5.814  -22.983 0.50 43.54 ? 126 VAL   B CG2 1 
ATOM   1168 N N   . ALA   B 2 118 ? -8.219  -5.211  -23.527 1.00 41.48 ? 127 ALA   B N   1 
ATOM   1169 C CA  . ALA   B 2 118 ? -6.998  -4.453  -23.781 1.00 41.22 ? 127 ALA   B CA  1 
ATOM   1170 C C   . ALA   B 2 118 ? -7.358  -3.316  -24.724 1.00 41.47 ? 127 ALA   B C   1 
ATOM   1171 O O   . ALA   B 2 118 ? -7.163  -3.424  -25.936 1.00 42.01 ? 127 ALA   B O   1 
ATOM   1172 C CB  . ALA   B 2 118 ? -5.947  -5.352  -24.405 1.00 40.90 ? 127 ALA   B CB  1 
ATOM   1173 N N   . LEU   B 2 119 ? -8.003  -2.273  -24.182 1.00 40.89 ? 128 LEU   B N   1 
ATOM   1174 C CA  . LEU   B 2 119 ? -8.460  -1.119  -24.956 1.00 40.61 ? 128 LEU   B CA  1 
ATOM   1175 C C   . LEU   B 2 119 ? -8.132  0.145   -24.182 1.00 40.85 ? 128 LEU   B C   1 
ATOM   1176 O O   . LEU   B 2 119 ? -8.506  0.254   -23.014 1.00 41.61 ? 128 LEU   B O   1 
ATOM   1177 C CB  . LEU   B 2 119 ? -9.979  -1.203  -25.232 1.00 40.30 ? 128 LEU   B CB  1 
ATOM   1178 C CG  . LEU   B 2 119 ? -10.425 -2.314  -26.196 1.00 41.22 ? 128 LEU   B CG  1 
ATOM   1179 C CD1 . LEU   B 2 119 ? -11.923 -2.473  -26.204 1.00 41.42 ? 128 LEU   B CD1 1 
ATOM   1180 C CD2 . LEU   B 2 119 ? -9.897  -2.078  -27.609 1.00 41.80 ? 128 LEU   B CD2 1 
ATOM   1181 N N   . ASP   B 2 120 ? -7.393  1.072   -24.792 1.00 40.40 ? 129 ASP   B N   1 
ATOM   1182 C CA  . ASP   B 2 120 ? -7.014  2.303   -24.112 1.00 40.79 ? 129 ASP   B CA  1 
ATOM   1183 C C   . ASP   B 2 120 ? -7.968  3.450   -24.431 1.00 40.31 ? 129 ASP   B C   1 
ATOM   1184 O O   . ASP   B 2 120 ? -8.172  3.776   -25.594 1.00 40.92 ? 129 ASP   B O   1 
ATOM   1185 C CB  . ASP   B 2 120 ? -5.556  2.673   -24.409 1.00 43.43 ? 129 ASP   B CB  1 
ATOM   1186 C CG  . ASP   B 2 120 ? -4.830  3.291   -23.225 1.00 50.87 ? 129 ASP   B CG  1 
ATOM   1187 O OD1 . ASP   B 2 120 ? -5.520  3.828   -22.310 1.00 51.58 ? 129 ASP   B OD1 1 
ATOM   1188 O OD2 . ASP   B 2 120 ? -3.576  3.232   -23.201 1.00 54.41 ? 129 ASP   B OD2 1 
ATOM   1189 N N   . TYR   B 2 121 ? -8.578  4.030   -23.394 1.00 39.39 ? 130 TYR   B N   1 
ATOM   1190 C CA  . TYR   B 2 121 ? -9.545  5.125   -23.489 1.00 38.87 ? 130 TYR   B CA  1 
ATOM   1191 C C   . TYR   B 2 121 ? -9.298  6.125   -22.360 1.00 37.96 ? 130 TYR   B C   1 
ATOM   1192 O O   . TYR   B 2 121 ? -8.896  5.714   -21.266 1.00 37.98 ? 130 TYR   B O   1 
ATOM   1193 C CB  . TYR   B 2 121 ? -10.978 4.567   -23.376 1.00 39.10 ? 130 TYR   B CB  1 
ATOM   1194 C CG  . TYR   B 2 121 ? -11.474 4.006   -24.686 1.00 40.08 ? 130 TYR   B CG  1 
ATOM   1195 C CD1 . TYR   B 2 121 ? -12.101 4.818   -25.615 1.00 40.77 ? 130 TYR   B CD1 1 
ATOM   1196 C CD2 . TYR   B 2 121 ? -11.274 2.672   -25.014 1.00 41.06 ? 130 TYR   B CD2 1 
ATOM   1197 C CE1 . TYR   B 2 121 ? -12.520 4.319   -26.836 1.00 41.86 ? 130 TYR   B CE1 1 
ATOM   1198 C CE2 . TYR   B 2 121 ? -11.677 2.164   -26.239 1.00 41.88 ? 130 TYR   B CE2 1 
ATOM   1199 C CZ  . TYR   B 2 121 ? -12.291 2.995   -27.155 1.00 42.81 ? 130 TYR   B CZ  1 
ATOM   1200 O OH  . TYR   B 2 121 ? -12.675 2.520   -28.388 1.00 44.30 ? 130 TYR   B OH  1 
ATOM   1201 N N   . PRO   B 2 122 ? -9.583  7.426   -22.591 1.00 36.50 ? 131 PRO   B N   1 
ATOM   1202 C CA  . PRO   B 2 122 ? -9.364  8.442   -21.536 1.00 35.18 ? 131 PRO   B CA  1 
ATOM   1203 C C   . PRO   B 2 122 ? -10.124 8.162   -20.254 1.00 33.71 ? 131 PRO   B C   1 
ATOM   1204 O O   . PRO   B 2 122 ? -11.210 7.614   -20.322 1.00 33.76 ? 131 PRO   B O   1 
ATOM   1205 C CB  . PRO   B 2 122 ? -9.849  9.738   -22.174 1.00 36.37 ? 131 PRO   B CB  1 
ATOM   1206 C CG  . PRO   B 2 122 ? -10.666 9.316   -23.368 1.00 37.52 ? 131 PRO   B CG  1 
ATOM   1207 C CD  . PRO   B 2 122 ? -10.079 8.032   -23.838 1.00 36.06 ? 131 PRO   B CD  1 
ATOM   1208 N N   . ALA   B 2 123 ? -9.546  8.533   -19.095 1.00 32.30 ? 132 ALA   B N   1 
ATOM   1209 C CA  . ALA   B 2 123 ? -10.052 8.287   -17.737 1.00 31.46 ? 132 ALA   B CA  1 
ATOM   1210 C C   . ALA   B 2 123 ? -11.572 8.422   -17.538 1.00 30.82 ? 132 ALA   B C   1 
ATOM   1211 O O   . ALA   B 2 123 ? -12.150 7.663   -16.766 1.00 30.98 ? 132 ALA   B O   1 
ATOM   1212 C CB  . ALA   B 2 123 ? -9.327  9.176   -16.750 1.00 31.37 ? 132 ALA   B CB  1 
ATOM   1213 N N   . GLY   B 2 124 ? -12.200 9.361   -18.246 1.00 30.00 ? 133 GLY   B N   1 
ATOM   1214 C CA  . GLY   B 2 124 ? -13.640 9.606   -18.176 1.00 28.96 ? 133 GLY   B CA  1 
ATOM   1215 C C   . GLY   B 2 124 ? -14.510 8.547   -18.825 1.00 27.25 ? 133 GLY   B C   1 
ATOM   1216 O O   . GLY   B 2 124 ? -15.732 8.602   -18.729 1.00 26.67 ? 133 GLY   B O   1 
ATOM   1217 N N   . THR   B 2 125 ? -13.899 7.585   -19.506 1.00 26.48 ? 134 THR   B N   1 
ATOM   1218 C CA  . THR   B 2 125 ? -14.621 6.469   -20.110 1.00 26.36 ? 134 THR   B CA  1 
ATOM   1219 C C   . THR   B 2 125 ? -14.974 5.387   -19.049 1.00 26.06 ? 134 THR   B C   1 
ATOM   1220 O O   . THR   B 2 125 ? -15.832 4.541   -19.314 1.00 26.91 ? 134 THR   B O   1 
ATOM   1221 C CB  . THR   B 2 125 ? -13.846 5.926   -21.317 1.00 27.58 ? 134 THR   B CB  1 
ATOM   1222 O OG1 . THR   B 2 125 ? -13.519 7.012   -22.194 1.00 28.66 ? 134 THR   B OG1 1 
ATOM   1223 C CG2 . THR   B 2 125 ? -14.633 4.918   -22.097 1.00 28.06 ? 134 THR   B CG2 1 
ATOM   1224 N N   . SER   B 2 126 ? -14.329 5.431   -17.851 1.00 24.41 ? 135 SER   B N   1 
ATOM   1225 C CA  . SER   B 2 126 ? -14.528 4.501   -16.753 1.00 23.55 ? 135 SER   B CA  1 
ATOM   1226 C C   . SER   B 2 126 ? -15.980 4.357   -16.389 1.00 23.30 ? 135 SER   B C   1 
ATOM   1227 O O   . SER   B 2 126 ? -16.620 5.340   -16.061 1.00 23.09 ? 135 SER   B O   1 
ATOM   1228 C CB  . SER   B 2 126 ? -13.787 4.993   -15.525 1.00 24.19 ? 135 SER   B CB  1 
ATOM   1229 O OG  . SER   B 2 126 ? -12.441 4.561   -15.526 1.00 26.33 ? 135 SER   B OG  1 
ATOM   1230 N N   . GLY   B 2 127 ? -16.469 3.130   -16.400 1.00 23.12 ? 136 GLY   B N   1 
ATOM   1231 C CA  . GLY   B 2 127 ? -17.848 2.792   -16.095 1.00 23.63 ? 136 GLY   B CA  1 
ATOM   1232 C C   . GLY   B 2 127 ? -18.564 2.176   -17.279 1.00 24.80 ? 136 GLY   B C   1 
ATOM   1233 O O   . GLY   B 2 127 ? -19.570 1.498   -17.087 1.00 25.53 ? 136 GLY   B O   1 
ATOM   1234 N N   . SER   B 2 128 ? -18.069 2.423   -18.514 1.00 24.74 ? 137 SER   B N   1 
ATOM   1235 C CA  . SER   B 2 128 ? -18.614 1.895   -19.757 1.00 25.60 ? 137 SER   B CA  1 
ATOM   1236 C C   . SER   B 2 128 ? -18.806 0.374   -19.712 1.00 26.63 ? 137 SER   B C   1 
ATOM   1237 O O   . SER   B 2 128 ? -17.887 -0.357  -19.352 1.00 27.31 ? 137 SER   B O   1 
ATOM   1238 C CB  . SER   B 2 128 ? -17.703 2.265   -20.923 1.00 26.81 ? 137 SER   B CB  1 
ATOM   1239 O OG  . SER   B 2 128 ? -17.506 3.667   -20.981 1.00 28.77 ? 137 SER   B OG  1 
ATOM   1240 N N   . PRO   B 2 129 ? -19.992 -0.125  -20.098 1.00 26.45 ? 138 PRO   B N   1 
ATOM   1241 C CA  . PRO   B 2 129 ? -20.233 -1.574  -20.033 1.00 26.62 ? 138 PRO   B CA  1 
ATOM   1242 C C   . PRO   B 2 129 ? -19.573 -2.465  -21.088 1.00 27.30 ? 138 PRO   B C   1 
ATOM   1243 O O   . PRO   B 2 129 ? -19.299 -2.064  -22.220 1.00 28.05 ? 138 PRO   B O   1 
ATOM   1244 C CB  . PRO   B 2 129 ? -21.754 -1.674  -20.148 1.00 27.01 ? 138 PRO   B CB  1 
ATOM   1245 C CG  . PRO   B 2 129 ? -22.146 -0.482  -20.918 1.00 27.47 ? 138 PRO   B CG  1 
ATOM   1246 C CD  . PRO   B 2 129 ? -21.200 0.609   -20.517 1.00 25.83 ? 138 PRO   B CD  1 
ATOM   1247 N N   . ILE   B 2 130 ? -19.380 -3.721  -20.708 1.00 27.26 ? 139 ILE   B N   1 
ATOM   1248 C CA  . ILE   B 2 130 ? -18.893 -4.778  -21.576 1.00 27.97 ? 139 ILE   B CA  1 
ATOM   1249 C C   . ILE   B 2 130 ? -20.096 -5.706  -21.785 1.00 29.19 ? 139 ILE   B C   1 
ATOM   1250 O O   . ILE   B 2 130 ? -20.749 -6.108  -20.825 1.00 28.85 ? 139 ILE   B O   1 
ATOM   1251 C CB  . ILE   B 2 130 ? -17.641 -5.474  -21.012 1.00 27.90 ? 139 ILE   B CB  1 
ATOM   1252 C CG1 . ILE   B 2 130 ? -16.473 -4.481  -20.949 1.00 28.48 ? 139 ILE   B CG1 1 
ATOM   1253 C CG2 . ILE   B 2 130 ? -17.269 -6.694  -21.843 1.00 28.26 ? 139 ILE   B CG2 1 
ATOM   1254 C CD1 . ILE   B 2 130 ? -15.478 -4.798  -19.838 1.00 29.27 ? 139 ILE   B CD1 1 
ATOM   1255 N N   . LEU   B 2 131 ? -20.428 -5.969  -23.051 1.00 30.27 ? 140 LEU   B N   1 
ATOM   1256 C CA  . LEU   B 2 131 ? -21.634 -6.683  -23.458 1.00 31.77 ? 140 LEU   B CA  1 
ATOM   1257 C C   . LEU   B 2 131 ? -21.370 -7.988  -24.168 1.00 33.29 ? 140 LEU   B C   1 
ATOM   1258 O O   . LEU   B 2 131 ? -20.468 -8.061  -24.999 1.00 33.58 ? 140 LEU   B O   1 
ATOM   1259 C CB  . LEU   B 2 131 ? -22.451 -5.809  -24.449 1.00 31.83 ? 140 LEU   B CB  1 
ATOM   1260 C CG  . LEU   B 2 131 ? -22.315 -4.298  -24.362 1.00 33.15 ? 140 LEU   B CG  1 
ATOM   1261 C CD1 . LEU   B 2 131 ? -22.878 -3.635  -25.570 1.00 33.51 ? 140 LEU   B CD1 1 
ATOM   1262 C CD2 . LEU   B 2 131 ? -22.919 -3.771  -23.073 1.00 34.11 ? 140 LEU   B CD2 1 
ATOM   1263 N N   . ASP   B 2 132 ? -22.253 -8.974  -23.956 1.00 34.04 ? 141 ASP   B N   1 
ATOM   1264 C CA  . ASP   B 2 132 ? -22.173 -10.221 -24.701 1.00 35.45 ? 141 ASP   B CA  1 
ATOM   1265 C C   . ASP   B 2 132 ? -23.059 -10.171 -25.989 1.00 37.18 ? 141 ASP   B C   1 
ATOM   1266 O O   . ASP   B 2 132 ? -23.703 -9.152  -26.249 1.00 36.86 ? 141 ASP   B O   1 
ATOM   1267 C CB  . ASP   B 2 132 ? -22.461 -11.432 -23.803 1.00 36.57 ? 141 ASP   B CB  1 
ATOM   1268 C CG  . ASP   B 2 132 ? -23.832 -11.457 -23.193 1.00 41.26 ? 141 ASP   B CG  1 
ATOM   1269 O OD1 . ASP   B 2 132 ? -24.729 -10.784 -23.730 1.00 41.46 ? 141 ASP   B OD1 1 
ATOM   1270 O OD2 . ASP   B 2 132 ? -24.012 -12.159 -22.176 1.00 44.97 ? 141 ASP   B OD2 1 
ATOM   1271 N N   . LYS   B 2 133 ? -23.094 -11.266 -26.782 1.00 38.66 ? 142 LYS   B N   1 
ATOM   1272 C CA  . LYS   B 2 133 ? -23.835 -11.348 -28.041 1.00 40.38 ? 142 LYS   B CA  1 
ATOM   1273 C C   . LYS   B 2 133 ? -25.329 -11.020 -27.912 1.00 41.06 ? 142 LYS   B C   1 
ATOM   1274 O O   . LYS   B 2 133 ? -25.965 -10.691 -28.921 1.00 41.02 ? 142 LYS   B O   1 
ATOM   1275 C CB  . LYS   B 2 133 ? -23.621 -12.715 -28.717 1.00 43.58 ? 142 LYS   B CB  1 
ATOM   1276 C CG  . LYS   B 2 133 ? -22.146 -13.017 -29.029 1.00 49.98 ? 142 LYS   B CG  1 
ATOM   1277 C CD  . LYS   B 2 133 ? -21.948 -14.407 -29.694 1.00 56.83 ? 142 LYS   B CD  1 
ATOM   1278 C CE  . LYS   B 2 133 ? -20.496 -14.873 -29.726 1.00 61.59 ? 142 LYS   B CE  1 
ATOM   1279 N NZ  . LYS   B 2 133 ? -20.331 -16.228 -30.341 1.00 63.29 ? 142 LYS   B NZ  1 
ATOM   1280 N N   . CYS   B 2 134 ? -25.879 -11.044 -26.679 1.00 41.24 ? 143 CYS   B N   1 
ATOM   1281 C CA  . CYS   B 2 134 ? -27.292 -10.682 -26.488 1.00 42.04 ? 143 CYS   B CA  1 
ATOM   1282 C C   . CYS   B 2 134 ? -27.515 -9.284  -25.950 1.00 41.54 ? 143 CYS   B C   1 
ATOM   1283 O O   . CYS   B 2 134 ? -28.649 -8.949  -25.606 1.00 42.10 ? 143 CYS   B O   1 
ATOM   1284 C CB  . CYS   B 2 134 ? -28.002 -11.704 -25.619 1.00 44.02 ? 143 CYS   B CB  1 
ATOM   1285 S SG  . CYS   B 2 134 ? -27.554 -13.400 -26.004 1.00 52.49 ? 143 CYS   B SG  1 
ATOM   1286 N N   . GLY   B 2 135 ? -26.463 -8.479  -25.878 1.00 40.23 ? 144 GLY   B N   1 
ATOM   1287 C CA  . GLY   B 2 135 ? -26.550 -7.156  -25.291 1.00 39.22 ? 144 GLY   B CA  1 
ATOM   1288 C C   . GLY   B 2 135 ? -26.667 -7.210  -23.779 1.00 37.61 ? 144 GLY   B C   1 
ATOM   1289 O O   . GLY   B 2 135 ? -27.062 -6.217  -23.173 1.00 37.94 ? 144 GLY   B O   1 
ATOM   1290 N N   . ARG   B 2 136 ? -26.338 -8.358  -23.146 1.00 36.12 ? 145 ARG   B N   1 
ATOM   1291 C CA  . ARG   B 2 136 ? -26.401 -8.493  -21.682 1.00 35.49 ? 145 ARG   B CA  1 
ATOM   1292 C C   . ARG   B 2 136 ? -25.137 -7.932  -21.054 1.00 34.25 ? 145 ARG   B C   1 
ATOM   1293 O O   . ARG   B 2 136 ? -24.051 -8.218  -21.552 1.00 34.90 ? 145 ARG   B O   1 
ATOM   1294 C CB  . ARG   B 2 136 ? -26.578 -9.959  -21.266 1.00 36.65 ? 145 ARG   B CB  1 
ATOM   1295 C CG  . ARG   B 2 136 ? -28.022 -10.391 -21.224 1.00 40.77 ? 145 ARG   B CG  1 
ATOM   1296 C CD  . ARG   B 2 136 ? -28.125 -11.840 -20.838 1.00 46.14 ? 145 ARG   B CD  1 
ATOM   1297 N NE  . ARG   B 2 136 ? -27.827 -12.704 -21.978 1.00 52.27 ? 145 ARG   B NE  1 
ATOM   1298 C CZ  . ARG   B 2 136 ? -26.956 -13.709 -21.953 1.00 56.16 ? 145 ARG   B CZ  1 
ATOM   1299 N NH1 . ARG   B 2 136 ? -26.270 -13.977 -20.847 1.00 56.04 ? 145 ARG   B NH1 1 
ATOM   1300 N NH2 . ARG   B 2 136 ? -26.751 -14.444 -23.041 1.00 56.71 ? 145 ARG   B NH2 1 
ATOM   1301 N N   . VAL   B 2 137 ? -25.259 -7.130  -19.983 1.00 32.43 ? 146 VAL   B N   1 
ATOM   1302 C CA  . VAL   B 2 137 ? -24.074 -6.549  -19.348 1.00 31.10 ? 146 VAL   B CA  1 
ATOM   1303 C C   . VAL   B 2 137 ? -23.314 -7.571  -18.522 1.00 29.75 ? 146 VAL   B C   1 
ATOM   1304 O O   . VAL   B 2 137 ? -23.825 -8.046  -17.506 1.00 29.66 ? 146 VAL   B O   1 
ATOM   1305 C CB  . VAL   B 2 137 ? -24.338 -5.261  -18.543 1.00 31.26 ? 146 VAL   B CB  1 
ATOM   1306 C CG1 . VAL   B 2 137 ? -23.027 -4.558  -18.239 1.00 31.47 ? 146 VAL   B CG1 1 
ATOM   1307 C CG2 . VAL   B 2 137 ? -25.272 -4.330  -19.294 1.00 31.78 ? 146 VAL   B CG2 1 
ATOM   1308 N N   . ILE   B 2 138 ? -22.087 -7.906  -18.970 1.00 28.29 ? 147 ILE   B N   1 
ATOM   1309 C CA  . ILE   B 2 138 ? -21.201 -8.856  -18.299 1.00 27.01 ? 147 ILE   B CA  1 
ATOM   1310 C C   . ILE   B 2 138 ? -20.121 -8.195  -17.405 1.00 25.86 ? 147 ILE   B C   1 
ATOM   1311 O O   . ILE   B 2 138 ? -19.333 -8.918  -16.790 1.00 25.63 ? 147 ILE   B O   1 
ATOM   1312 C CB  . ILE   B 2 138 ? -20.565 -9.837  -19.304 1.00 26.78 ? 147 ILE   B CB  1 
ATOM   1313 C CG1 . ILE   B 2 138 ? -19.836 -9.087  -20.416 1.00 27.36 ? 147 ILE   B CG1 1 
ATOM   1314 C CG2 . ILE   B 2 138 ? -21.596 -10.798 -19.845 1.00 27.33 ? 147 ILE   B CG2 1 
ATOM   1315 C CD1 . ILE   B 2 138 ? -18.931 -9.901  -21.164 1.00 28.73 ? 147 ILE   B CD1 1 
ATOM   1316 N N   . GLY   B 2 139 ? -20.108 -6.863  -17.319 1.00 25.06 ? 148 GLY   B N   1 
ATOM   1317 C CA  . GLY   B 2 139 ? -19.158 -6.143  -16.478 1.00 25.39 ? 148 GLY   B CA  1 
ATOM   1318 C C   . GLY   B 2 139 ? -18.930 -4.697  -16.867 1.00 25.63 ? 148 GLY   B C   1 
ATOM   1319 O O   . GLY   B 2 139 ? -19.470 -4.248  -17.872 1.00 26.22 ? 148 GLY   B O   1 
ATOM   1320 N N   . LEU   B 2 140 ? -18.124 -3.948  -16.089 1.00 25.24 ? 149 LEU   B N   1 
ATOM   1321 C CA  . LEU   B 2 140 ? -17.799 -2.556  -16.417 1.00 25.66 ? 149 LEU   B CA  1 
ATOM   1322 C C   . LEU   B 2 140 ? -16.283 -2.362  -16.644 1.00 26.20 ? 149 LEU   B C   1 
ATOM   1323 O O   . LEU   B 2 140 ? -15.474 -3.022  -15.999 1.00 26.39 ? 149 LEU   B O   1 
ATOM   1324 C CB  . LEU   B 2 140 ? -18.307 -1.555  -15.355 1.00 25.70 ? 149 LEU   B CB  1 
ATOM   1325 C CG  . LEU   B 2 140 ? -19.782 -1.612  -14.930 1.00 27.17 ? 149 LEU   B CG  1 
ATOM   1326 C CD1 . LEU   B 2 140 ? -20.086 -0.557  -13.862 1.00 28.18 ? 149 LEU   B CD1 1 
ATOM   1327 C CD2 . LEU   B 2 140 ? -20.726 -1.463  -16.085 1.00 27.42 ? 149 LEU   B CD2 1 
ATOM   1328 N N   . TYR   B 2 141 ? -15.916 -1.447  -17.562 1.00 26.51 ? 150 TYR   B N   1 
ATOM   1329 C CA  . TYR   B 2 141 ? -14.540 -1.079  -17.938 1.00 27.34 ? 150 TYR   B CA  1 
ATOM   1330 C C   . TYR   B 2 141 ? -14.084 0.090   -17.095 1.00 26.47 ? 150 TYR   B C   1 
ATOM   1331 O O   . TYR   B 2 141 ? -14.869 0.994   -16.900 1.00 26.29 ? 150 TYR   B O   1 
ATOM   1332 C CB  . TYR   B 2 141 ? -14.527 -0.647  -19.430 1.00 28.60 ? 150 TYR   B CB  1 
ATOM   1333 C CG  . TYR   B 2 141 ? -13.298 0.109   -19.909 1.00 31.08 ? 150 TYR   B CG  1 
ATOM   1334 C CD1 . TYR   B 2 141 ? -13.208 1.491   -19.779 1.00 32.43 ? 150 TYR   B CD1 1 
ATOM   1335 C CD2 . TYR   B 2 141 ? -12.278 -0.541  -20.587 1.00 33.29 ? 150 TYR   B CD2 1 
ATOM   1336 C CE1 . TYR   B 2 141 ? -12.070 2.183   -20.177 1.00 34.03 ? 150 TYR   B CE1 1 
ATOM   1337 C CE2 . TYR   B 2 141 ? -11.163 0.150   -21.054 1.00 34.80 ? 150 TYR   B CE2 1 
ATOM   1338 C CZ  . TYR   B 2 141 ? -11.062 1.516   -20.851 1.00 35.86 ? 150 TYR   B CZ  1 
ATOM   1339 O OH  . TYR   B 2 141 ? -9.962  2.197   -21.331 1.00 37.63 ? 150 TYR   B OH  1 
ATOM   1340 N N   . GLY   B 2 142 ? -12.818 0.127   -16.696 1.00 26.24 ? 151 GLY   B N   1 
ATOM   1341 C CA  . GLY   B 2 142 ? -12.308 1.265   -15.946 1.00 27.29 ? 151 GLY   B CA  1 
ATOM   1342 C C   . GLY   B 2 142 ? -11.399 0.955   -14.781 1.00 28.71 ? 151 GLY   B C   1 
ATOM   1343 O O   . GLY   B 2 142 ? -10.831 1.880   -14.196 1.00 29.27 ? 151 GLY   B O   1 
ATOM   1344 N N   . ASN   B 2 143 ? -11.249 -0.326  -14.419 1.00 29.10 ? 152 ASN   B N   1 
ATOM   1345 C CA  . ASN   B 2 143 ? -10.327 -0.688  -13.349 1.00 30.29 ? 152 ASN   B CA  1 
ATOM   1346 C C   . ASN   B 2 143 ? -9.407  -1.754  -13.868 1.00 31.23 ? 152 ASN   B C   1 
ATOM   1347 O O   . ASN   B 2 143 ? -9.858  -2.854  -14.166 1.00 30.68 ? 152 ASN   B O   1 
ATOM   1348 C CB  . ASN   B 2 143 ? -11.051 -1.140  -12.076 1.00 31.49 ? 152 ASN   B CB  1 
ATOM   1349 C CG  . ASN   B 2 143 ? -10.137 -1.327  -10.869 1.00 34.00 ? 152 ASN   B CG  1 
ATOM   1350 O OD1 . ASN   B 2 143 ? -9.080  -0.692  -10.741 1.00 34.79 ? 152 ASN   B OD1 1 
ATOM   1351 N ND2 . ASN   B 2 143 ? -10.534 -2.197  -9.946  1.00 34.19 ? 152 ASN   B ND2 1 
ATOM   1352 N N   . GLY   B 2 144 ? -8.136  -1.412  -14.011 1.00 32.75 ? 153 GLY   B N   1 
ATOM   1353 C CA  . GLY   B 2 144 ? -7.161  -2.358  -14.526 1.00 35.32 ? 153 GLY   B CA  1 
ATOM   1354 C C   . GLY   B 2 144 ? -5.716  -2.052  -14.192 1.00 38.12 ? 153 GLY   B C   1 
ATOM   1355 O O   . GLY   B 2 144 ? -5.408  -1.609  -13.083 1.00 38.12 ? 153 GLY   B O   1 
ATOM   1356 N N   . VAL   B 2 145 ? -4.811  -2.293  -15.164 1.00 40.12 ? 154 VAL   B N   1 
ATOM   1357 C CA  . VAL   B 2 145 ? -3.376  -2.107  -14.971 1.00 42.66 ? 154 VAL   B CA  1 
ATOM   1358 C C   . VAL   B 2 145 ? -2.651  -1.624  -16.249 1.00 45.10 ? 154 VAL   B C   1 
ATOM   1359 O O   . VAL   B 2 145 ? -3.199  -1.706  -17.350 1.00 45.49 ? 154 VAL   B O   1 
ATOM   1360 C CB  . VAL   B 2 145 ? -2.798  -3.454  -14.475 1.00 43.86 ? 154 VAL   B CB  1 
ATOM   1361 C CG1 . VAL   B 2 145 ? -2.667  -4.454  -15.630 1.00 44.42 ? 154 VAL   B CG1 1 
ATOM   1362 C CG2 . VAL   B 2 145 ? -1.471  -3.267  -13.742 1.00 44.54 ? 154 VAL   B CG2 1 
ATOM   1363 N N   . VAL   B 2 146 ? -1.415  -1.125  -16.100 1.00 46.67 ? 155 VAL   B N   1 
ATOM   1364 C CA  . VAL   B 2 146 ? -0.590  -0.703  -17.225 1.00 48.72 ? 155 VAL   B CA  1 
ATOM   1365 C C   . VAL   B 2 146 ? 0.514   -1.750  -17.403 1.00 51.57 ? 155 VAL   B C   1 
ATOM   1366 O O   . VAL   B 2 146 ? 1.284   -1.992  -16.481 1.00 52.11 ? 155 VAL   B O   1 
ATOM   1367 C CB  . VAL   B 2 146 ? -0.011  0.709   -17.017 1.00 49.08 ? 155 VAL   B CB  1 
ATOM   1368 C CG1 . VAL   B 2 146 ? 1.059   1.021   -18.061 1.00 49.86 ? 155 VAL   B CG1 1 
ATOM   1369 C CG2 . VAL   B 2 146 ? -1.119  1.750   -17.049 1.00 49.32 ? 155 VAL   B CG2 1 
ATOM   1370 N N   . ILE   B 2 147 ? 0.573   -2.388  -18.570 1.00 53.42 ? 156 ILE   B N   1 
ATOM   1371 C CA  . ILE   B 2 147 ? 1.545   -3.446  -18.845 1.00 55.28 ? 156 ILE   B CA  1 
ATOM   1372 C C   . ILE   B 2 147 ? 2.905   -2.907  -19.381 1.00 56.96 ? 156 ILE   B C   1 
ATOM   1373 O O   . ILE   B 2 147 ? 3.018   -1.707  -19.644 1.00 57.42 ? 156 ILE   B O   1 
ATOM   1374 C CB  . ILE   B 2 147 ? 0.896   -4.500  -19.792 1.00 55.76 ? 156 ILE   B CB  1 
ATOM   1375 C CG1 . ILE   B 2 147 ? 0.730   -3.963  -21.222 1.00 56.36 ? 156 ILE   B CG1 1 
ATOM   1376 C CG2 . ILE   B 2 147 ? -0.423  -5.019  -19.223 1.00 56.29 ? 156 ILE   B CG2 1 
ATOM   1377 C CD1 . ILE   B 2 147 ? 0.620   -5.069  -22.250 1.00 57.36 ? 156 ILE   B CD1 1 
ATOM   1378 N N   . LYS   B 2 148 ? 3.925   -3.803  -19.526 1.00 57.41 ? 157 LYS   B N   1 
ATOM   1379 C CA  . LYS   B 2 148 ? 5.282   -3.529  -20.009 1.00 58.22 ? 157 LYS   B CA  1 
ATOM   1380 C C   . LYS   B 2 148 ? 5.401   -2.532  -21.177 1.00 59.01 ? 157 LYS   B C   1 
ATOM   1381 O O   . LYS   B 2 148 ? 6.181   -1.588  -21.060 1.00 59.72 ? 157 LYS   B O   1 
ATOM   1382 C CB  . LYS   B 2 148 ? 6.001   -4.833  -20.383 1.00 60.22 ? 157 LYS   B CB  1 
ATOM   1383 C CG  . LYS   B 2 148 ? 7.318   -5.005  -19.638 1.00 64.52 ? 157 LYS   B CG  1 
ATOM   1384 C CD  . LYS   B 2 148 ? 8.358   -5.805  -20.417 1.00 68.34 ? 157 LYS   B CD  1 
ATOM   1385 C CE  . LYS   B 2 148 ? 9.695   -5.750  -19.707 1.00 71.69 ? 157 LYS   B CE  1 
ATOM   1386 N NZ  . LYS   B 2 148 ? 10.807  -6.339  -20.507 1.00 73.71 ? 157 LYS   B NZ  1 
ATOM   1387 N N   . ASN   B 2 149 ? 4.660   -2.718  -22.291 1.00 58.75 ? 158 ASN   B N   1 
ATOM   1388 C CA  . ASN   B 2 149 ? 4.784   -1.779  -23.422 1.00 59.10 ? 158 ASN   B CA  1 
ATOM   1389 C C   . ASN   B 2 149 ? 4.041   -0.422  -23.212 1.00 58.49 ? 158 ASN   B C   1 
ATOM   1390 O O   . ASN   B 2 149 ? 4.089   0.454   -24.084 1.00 58.99 ? 158 ASN   B O   1 
ATOM   1391 C CB  . ASN   B 2 149 ? 4.414   -2.419  -24.781 1.00 60.54 ? 158 ASN   B CB  1 
ATOM   1392 C CG  . ASN   B 2 149 ? 2.987   -2.900  -24.978 1.00 63.82 ? 158 ASN   B CG  1 
ATOM   1393 O OD1 . ASN   B 2 149 ? 2.693   -3.603  -25.954 1.00 65.29 ? 158 ASN   B OD1 1 
ATOM   1394 N ND2 . ASN   B 2 149 ? 2.064   -2.536  -24.098 1.00 64.04 ? 158 ASN   B ND2 1 
ATOM   1395 N N   . GLY   B 2 150 ? 3.375   -0.264  -22.076 1.00 57.04 ? 159 GLY   B N   1 
ATOM   1396 C CA  . GLY   B 2 150 ? 2.686   0.973   -21.750 1.00 56.22 ? 159 GLY   B CA  1 
ATOM   1397 C C   . GLY   B 2 150 ? 1.190   0.967   -21.966 1.00 54.78 ? 159 GLY   B C   1 
ATOM   1398 O O   . GLY   B 2 150 ? 0.488   1.803   -21.385 1.00 55.30 ? 159 GLY   B O   1 
ATOM   1399 N N   . SER   B 2 151 ? 0.680   0.036   -22.799 1.00 52.72 ? 160 SER   B N   1 
ATOM   1400 C CA  A SER   B 2 151 ? -0.760  -0.015  -23.065 0.50 52.01 ? 160 SER   B CA  1 
ATOM   1401 C CA  B SER   B 2 151 ? -0.754  -0.053  -23.077 0.50 52.12 ? 160 SER   B CA  1 
ATOM   1402 C C   . SER   B 2 151 ? -1.580  -0.384  -21.826 1.00 50.89 ? 160 SER   B C   1 
ATOM   1403 O O   . SER   B 2 151 ? -1.050  -0.929  -20.849 1.00 50.79 ? 160 SER   B O   1 
ATOM   1404 C CB  A SER   B 2 151 ? -1.088  -0.920  -24.253 0.50 53.04 ? 160 SER   B CB  1 
ATOM   1405 C CB  B SER   B 2 151 ? -1.036  -1.036  -24.214 0.50 53.45 ? 160 SER   B CB  1 
ATOM   1406 O OG  A SER   B 2 151 ? -2.449  -0.776  -24.631 0.50 54.58 ? 160 SER   B OG  1 
ATOM   1407 O OG  B SER   B 2 151 ? -0.304  -2.244  -24.081 0.50 55.46 ? 160 SER   B OG  1 
ATOM   1408 N N   . TYR   B 2 152 ? -2.860  -0.038  -21.847 1.00 48.58 ? 161 TYR   B N   1 
ATOM   1409 C CA  . TYR   B 2 152 ? -3.736  -0.263  -20.718 1.00 47.14 ? 161 TYR   B CA  1 
ATOM   1410 C C   . TYR   B 2 152 ? -4.658  -1.495  -20.866 1.00 45.27 ? 161 TYR   B C   1 
ATOM   1411 O O   . TYR   B 2 152 ? -5.297  -1.689  -21.895 1.00 44.96 ? 161 TYR   B O   1 
ATOM   1412 C CB  . TYR   B 2 152 ? -4.523  1.032   -20.460 1.00 46.90 ? 161 TYR   B CB  1 
ATOM   1413 C CG  . TYR   B 2 152 ? -5.552  0.918   -19.370 1.00 46.94 ? 161 TYR   B CG  1 
ATOM   1414 C CD1 . TYR   B 2 152 ? -5.176  0.884   -18.034 1.00 47.70 ? 161 TYR   B CD1 1 
ATOM   1415 C CD2 . TYR   B 2 152 ? -6.902  0.849   -19.670 1.00 47.54 ? 161 TYR   B CD2 1 
ATOM   1416 C CE1 . TYR   B 2 152 ? -6.116  0.740   -17.026 1.00 48.04 ? 161 TYR   B CE1 1 
ATOM   1417 C CE2 . TYR   B 2 152 ? -7.852  0.734   -18.670 1.00 48.48 ? 161 TYR   B CE2 1 
ATOM   1418 C CZ  . TYR   B 2 152 ? -7.451  0.649   -17.352 1.00 48.99 ? 161 TYR   B CZ  1 
ATOM   1419 O OH  . TYR   B 2 152 ? -8.385  0.526   -16.369 1.00 50.78 ? 161 TYR   B OH  1 
ATOM   1420 N N   . VAL   B 2 153 ? -4.706  -2.340  -19.826 1.00 43.71 ? 162 VAL   B N   1 
ATOM   1421 C CA  . VAL   B 2 153 ? -5.575  -3.516  -19.833 1.00 42.26 ? 162 VAL   B CA  1 
ATOM   1422 C C   . VAL   B 2 153 ? -6.487  -3.441  -18.619 1.00 40.41 ? 162 VAL   B C   1 
ATOM   1423 O O   . VAL   B 2 153 ? -6.014  -3.526  -17.498 1.00 39.76 ? 162 VAL   B O   1 
ATOM   1424 C CB  . VAL   B 2 153 ? -4.816  -4.867  -19.937 1.00 42.75 ? 162 VAL   B CB  1 
ATOM   1425 C CG1 . VAL   B 2 153 ? -5.790  -6.042  -19.930 1.00 42.70 ? 162 VAL   B CG1 1 
ATOM   1426 C CG2 . VAL   B 2 153 ? -3.954  -4.907  -21.198 1.00 43.52 ? 162 VAL   B CG2 1 
ATOM   1427 N N   . SER   B 2 154 ? -7.790  -3.210  -18.865 1.00 39.22 ? 163 SER   B N   1 
ATOM   1428 C CA  . SER   B 2 154 ? -8.843  -3.075  -17.862 1.00 38.05 ? 163 SER   B CA  1 
ATOM   1429 C C   . SER   B 2 154 ? -9.564  -4.389  -17.635 1.00 37.10 ? 163 SER   B C   1 
ATOM   1430 O O   . SER   B 2 154 ? -9.923  -5.053  -18.592 1.00 36.98 ? 163 SER   B O   1 
ATOM   1431 C CB  . SER   B 2 154 ? -9.876  -2.058  -18.330 1.00 38.64 ? 163 SER   B CB  1 
ATOM   1432 O OG  . SER   B 2 154 ? -11.052 -2.092  -17.537 1.00 40.38 ? 163 SER   B OG  1 
ATOM   1433 N N   . ALA   B 2 155 ? -9.895  -4.695  -16.381 1.00 36.11 ? 164 ALA   B N   1 
ATOM   1434 C CA  . ALA   B 2 155 ? -10.653 -5.900  -16.064 1.00 35.41 ? 164 ALA   B CA  1 
ATOM   1435 C C   . ALA   B 2 155 ? -12.145 -5.762  -16.480 1.00 33.88 ? 164 ALA   B C   1 
ATOM   1436 O O   . ALA   B 2 155 ? -12.643 -4.656  -16.731 1.00 33.94 ? 164 ALA   B O   1 
ATOM   1437 C CB  . ALA   B 2 155 ? -10.549 -6.198  -14.566 1.00 35.69 ? 164 ALA   B CB  1 
ATOM   1438 N N   . ILE   B 2 156 ? -12.828 -6.903  -16.608 1.00 31.96 ? 165 ILE   B N   1 
ATOM   1439 C CA  . ILE   B 2 156 ? -14.248 -6.930  -16.837 1.00 30.41 ? 165 ILE   B CA  1 
ATOM   1440 C C   . ILE   B 2 156 ? -14.763 -7.032  -15.402 1.00 29.75 ? 165 ILE   B C   1 
ATOM   1441 O O   . ILE   B 2 156 ? -14.842 -8.143  -14.859 1.00 29.60 ? 165 ILE   B O   1 
ATOM   1442 C CB  . ILE   B 2 156 ? -14.657 -8.156  -17.685 1.00 30.12 ? 165 ILE   B CB  1 
ATOM   1443 C CG1 . ILE   B 2 156 ? -13.964 -8.125  -19.073 1.00 30.83 ? 165 ILE   B CG1 1 
ATOM   1444 C CG2 . ILE   B 2 156 ? -16.179 -8.205  -17.833 1.00 30.28 ? 165 ILE   B CG2 1 
ATOM   1445 C CD1 . ILE   B 2 156 ? -14.180 -9.320  -19.898 1.00 31.39 ? 165 ILE   B CD1 1 
ATOM   1446 N N   . THR   B 2 157 ? -14.994 -5.875  -14.743 1.00 28.89 ? 166 THR   B N   1 
ATOM   1447 C CA  . THR   B 2 157 ? -15.462 -5.873  -13.348 1.00 28.63 ? 166 THR   B CA  1 
ATOM   1448 C C   . THR   B 2 157 ? -16.973 -6.116  -13.228 1.00 28.02 ? 166 THR   B C   1 
ATOM   1449 O O   . THR   B 2 157 ? -17.754 -5.258  -13.630 1.00 28.00 ? 166 THR   B O   1 
ATOM   1450 C CB  . THR   B 2 157 ? -15.115 -4.550  -12.656 1.00 29.68 ? 166 THR   B CB  1 
ATOM   1451 O OG1 . THR   B 2 157 ? -13.723 -4.282  -12.758 1.00 30.87 ? 166 THR   B OG1 1 
ATOM   1452 C CG2 . THR   B 2 157 ? -15.501 -4.557  -11.228 1.00 30.00 ? 166 THR   B CG2 1 
ATOM   1453 N N   . GLN   B 2 158 ? -17.389 -7.243  -12.645 1.00 27.51 ? 167 GLN   B N   1 
ATOM   1454 C CA  . GLN   B 2 158 ? -18.815 -7.516  -12.467 1.00 27.91 ? 167 GLN   B CA  1 
ATOM   1455 C C   . GLN   B 2 158 ? -19.205 -7.673  -10.965 1.00 29.93 ? 167 GLN   B C   1 
ATOM   1456 O O   . GLN   B 2 158 ? -18.431 -8.174  -10.161 1.00 29.65 ? 167 GLN   B O   1 
ATOM   1457 C CB  . GLN   B 2 158 ? -19.238 -8.712  -13.329 1.00 27.36 ? 167 GLN   B CB  1 
ATOM   1458 C CG  . GLN   B 2 158 ? -20.677 -9.177  -13.179 1.00 26.97 ? 167 GLN   B CG  1 
ATOM   1459 C CD  . GLN   B 2 158 ? -21.665 -8.211  -13.756 1.00 27.20 ? 167 GLN   B CD  1 
ATOM   1460 O OE1 . GLN   B 2 158 ? -21.872 -7.108  -13.223 1.00 27.77 ? 167 GLN   B OE1 1 
ATOM   1461 N NE2 . GLN   B 2 158 ? -22.331 -8.623  -14.819 1.00 24.95 ? 167 GLN   B NE2 1 
ATOM   1462 N N   . GLY   B 2 159 ? -20.379 -7.186  -10.607 1.00 31.71 ? 168 GLY   B N   1 
ATOM   1463 C CA  . GLY   B 2 159 ? -20.889 -7.286  -9.258  1.00 34.39 ? 168 GLY   B CA  1 
ATOM   1464 C C   . GLY   B 2 159 ? -21.687 -8.547  -9.016  1.00 37.30 ? 168 GLY   B C   1 
ATOM   1465 O O   . GLY   B 2 159 ? -21.846 -9.386  -9.903  1.00 36.74 ? 168 GLY   B O   1 
ATOM   1466 N N   . LYS   B 2 160 ? -22.171 -8.698  -7.789  1.00 40.30 ? 169 LYS   B N   1 
ATOM   1467 C CA  . LYS   B 2 160 ? -22.967 -9.856  -7.415  1.00 43.48 ? 169 LYS   B CA  1 
ATOM   1468 C C   . LYS   B 2 160 ? -24.448 -9.474  -7.250  1.00 46.33 ? 169 LYS   B C   1 
ATOM   1469 O O   . LYS   B 2 160 ? -24.769 -8.451  -6.635  1.00 46.77 ? 169 LYS   B O   1 
ATOM   1470 C CB  . LYS   B 2 160 ? -22.424 -10.492 -6.127  1.00 45.68 ? 169 LYS   B CB  1 
ATOM   1471 C CG  . LYS   B 2 160 ? -23.034 -11.862 -5.838  1.00 50.44 ? 169 LYS   B CG  1 
ATOM   1472 C CD  . LYS   B 2 160 ? -23.154 -12.116 -4.346  1.00 55.40 ? 169 LYS   B CD  1 
ATOM   1473 C CE  . LYS   B 2 160 ? -23.838 -13.422 -4.046  1.00 59.75 ? 169 LYS   B CE  1 
ATOM   1474 N NZ  . LYS   B 2 160 ? -24.074 -13.580 -2.584  1.00 62.58 ? 169 LYS   B NZ  1 
ATOM   1475 N N   . ARG   B 2 161 ? -25.348 -10.288 -7.815  1.00 47.86 ? 170 ARG   B N   1 
ATOM   1476 C CA  . ARG   B 2 161 ? -26.780 -10.055 -7.674  1.00 49.61 ? 170 ARG   B CA  1 
ATOM   1477 C C   . ARG   B 2 161 ? -27.233 -10.717 -6.370  1.00 51.25 ? 170 ARG   B C   1 
ATOM   1478 O O   . ARG   B 2 161 ? -26.766 -11.817 -6.039  1.00 51.84 ? 170 ARG   B O   1 
ATOM   1479 C CB  . ARG   B 2 161 ? -27.538 -10.647 -8.868  1.00 51.09 ? 170 ARG   B CB  1 
ATOM   1480 C CG  . ARG   B 2 161 ? -28.742 -9.827  -9.257  1.00 54.22 ? 170 ARG   B CG  1 
ATOM   1481 C CD  . ARG   B 2 161 ? -29.938 -10.697 -9.562  1.00 58.02 ? 170 ARG   B CD  1 
ATOM   1482 N NE  . ARG   B 2 161 ? -31.139 -9.882  -9.729  1.00 61.49 ? 170 ARG   B NE  1 
ATOM   1483 C CZ  . ARG   B 2 161 ? -31.577 -9.416  -10.896 1.00 63.68 ? 170 ARG   B CZ  1 
ATOM   1484 N NH1 . ARG   B 2 161 ? -30.932 -9.707  -12.020 1.00 63.55 ? 170 ARG   B NH1 1 
ATOM   1485 N NH2 . ARG   B 2 161 ? -32.665 -8.661  -10.947 1.00 63.53 ? 170 ARG   B NH2 1 
ATOM   1486 N N   . GLU   B 2 162 ? -28.105 -10.046 -5.610  1.00 51.69 ? 171 GLU   B N   1 
ATOM   1487 C CA  . GLU   B 2 162 ? -28.569 -10.608 -4.348  1.00 52.60 ? 171 GLU   B CA  1 
ATOM   1488 C C   . GLU   B 2 162 ? -29.991 -11.159 -4.439  1.00 52.95 ? 171 GLU   B C   1 
ATOM   1489 O O   . GLU   B 2 162 ? -30.178 -12.372 -4.542  1.00 53.06 ? 171 GLU   B O   1 
ATOM   1490 C CB  . GLU   B 2 162 ? -28.407 -9.594  -3.207  1.00 55.46 ? 171 GLU   B CB  1 
ATOM   1491 C CG  . GLU   B 2 162 ? -27.113 -9.771  -2.430  1.00 61.22 ? 171 GLU   B CG  1 
ATOM   1492 C CD  . GLU   B 2 162 ? -27.075 -10.988 -1.519  1.00 68.69 ? 171 GLU   B CD  1 
ATOM   1493 O OE1 . GLU   B 2 162 ? -27.535 -10.882 -0.357  1.00 69.16 ? 171 GLU   B OE1 1 
ATOM   1494 O OE2 . GLU   B 2 162 ? -26.574 -12.046 -1.966  1.00 71.53 ? 171 GLU   B OE2 1 
HETATM 1495 S S   . DMS   C 3 .   ? -18.687 11.667  -0.203  1.00 58.58 ? 201 DMS   B S   1 
HETATM 1496 O O   . DMS   C 3 .   ? -19.684 10.597  -0.562  1.00 58.45 ? 201 DMS   B O   1 
HETATM 1497 C C1  . DMS   C 3 .   ? -19.556 12.914  0.800   1.00 58.65 ? 201 DMS   B C1  1 
HETATM 1498 C C2  . DMS   C 3 .   ? -18.407 12.727  -1.653  1.00 58.52 ? 201 DMS   B C2  1 
HETATM 1499 N N1  . A1BGP D 4 .   ? -5.665  5.290   -19.775 0.97 81.44 ? 202 A1BGP B N1  1 
HETATM 1500 N N3  . A1BGP D 4 .   ? -7.616  3.553   -12.861 0.97 65.13 ? 202 A1BGP B N3  1 
HETATM 1501 C C4  . A1BGP D 4 .   ? -7.416  5.298   -16.824 0.97 72.53 ? 202 A1BGP B C4  1 
HETATM 1502 C C5  . A1BGP D 4 .   ? -6.406  6.152   -17.568 0.97 76.66 ? 202 A1BGP B C5  1 
HETATM 1503 C C6  . A1BGP D 4 .   ? -4.968  5.741   -17.198 0.97 78.30 ? 202 A1BGP B C6  1 
HETATM 1504 C C7  . A1BGP D 4 .   ? -3.933  6.236   -18.227 0.97 84.01 ? 202 A1BGP B C7  1 
HETATM 1505 C C8  . A1BGP D 4 .   ? -4.279  5.763   -19.630 0.97 85.27 ? 202 A1BGP B C8  1 
HETATM 1506 C C10 . A1BGP D 4 .   ? -6.359  3.186   -12.191 0.97 66.49 ? 202 A1BGP B C10 1 
HETATM 1507 C C13 . A1BGP D 4 .   ? -8.116  3.697   -9.492  0.97 60.96 ? 202 A1BGP B C13 1 
HETATM 1508 C C15 . A1BGP D 4 .   ? -8.240  3.389   -7.125  0.97 59.15 ? 202 A1BGP B C15 1 
HETATM 1509 C C17 . A1BGP D 4 .   ? -8.911  2.575   -9.632  0.97 60.36 ? 202 A1BGP B C17 1 
HETATM 1510 O O1  . A1BGP D 4 .   ? -8.067  1.851   -14.207 0.97 65.35 ? 202 A1BGP B O1  1 
HETATM 1511 C C1  . A1BGP D 4 .   ? -7.959  3.065   -14.059 0.97 65.79 ? 202 A1BGP B C1  1 
HETATM 1512 C C2  . A1BGP D 4 .   ? -8.154  3.946   -15.241 0.97 67.76 ? 202 A1BGP B C2  1 
HETATM 1513 C C3  . A1BGP D 4 .   ? -9.157  3.770   -16.147 0.97 67.35 ? 202 A1BGP B C3  1 
HETATM 1514 S S1  . A1BGP D 4 .   ? -8.867  4.684   -17.567 0.97 70.47 ? 202 A1BGP B S1  1 
HETATM 1515 C C9  . A1BGP D 4 .   ? -6.614  6.178   -19.083 0.97 78.88 ? 202 A1BGP B C9  1 
HETATM 1516 N N2  . A1BGP D 4 .   ? -7.277  4.968   -15.574 0.97 70.59 ? 202 A1BGP B N2  1 
HETATM 1517 C C11 . A1BGP D 4 .   ? -6.211  4.259   -11.142 0.97 66.02 ? 202 A1BGP B C11 1 
HETATM 1518 C C12 . A1BGP D 4 .   ? -7.645  4.496   -10.691 0.97 63.20 ? 202 A1BGP B C12 1 
HETATM 1519 C C14 . A1BGP D 4 .   ? -7.792  4.105   -8.207  0.97 60.49 ? 202 A1BGP B C14 1 
HETATM 1520 C C16 . A1BGP D 4 .   ? -9.008  2.285   -7.353  0.97 59.22 ? 202 A1BGP B C16 1 
HETATM 1521 N N4  . A1BGP D 4 .   ? -9.356  1.869   -8.577  0.97 59.79 ? 202 A1BGP B N4  1 
HETATM 1522 C C18 . A1BGP D 4 .   ? -8.476  4.368   -11.982 0.97 63.17 ? 202 A1BGP B C18 1 
HETATM 1523 O O   . HOH   E 5 .   ? -23.937 18.819  -19.784 1.00 25.28 ? 101 HOH   A O   1 
HETATM 1524 O O   . HOH   E 5 .   ? -1.052  -15.249 -9.839  1.00 14.69 ? 102 HOH   A O   1 
HETATM 1525 O O   . HOH   E 5 .   ? -6.624  -9.900  -2.993  1.00 32.17 ? 103 HOH   A O   1 
HETATM 1526 O O   . HOH   E 5 .   ? -4.231  1.471   -9.794  1.00 25.05 ? 104 HOH   A O   1 
HETATM 1527 O O   . HOH   E 5 .   ? -28.226 -7.367  -28.701 1.00 36.13 ? 105 HOH   A O   1 
HETATM 1528 O O   . HOH   E 5 .   ? -6.022  -10.691 -5.464  1.00 12.99 ? 106 HOH   A O   1 
HETATM 1529 O O   . HOH   E 5 .   ? -3.916  -1.849  -0.143  1.00 26.30 ? 107 HOH   A O   1 
HETATM 1530 O O   . HOH   E 5 .   ? -6.220  -7.119  0.612   1.00 31.32 ? 108 HOH   A O   1 
HETATM 1531 O O   . HOH   F 5 .   ? -17.513 25.057  -13.381 1.00 37.16 ? 301 HOH   B O   1 
HETATM 1532 O O   . HOH   F 5 .   ? -34.341 1.342   -15.620 1.00 23.82 ? 302 HOH   B O   1 
HETATM 1533 O O   . HOH   F 5 .   ? -6.449  -0.652  -10.793 1.00 10.67 ? 303 HOH   B O   1 
HETATM 1534 O O   . HOH   F 5 .   ? -12.345 1.588   -5.442  1.00 16.32 ? 304 HOH   B O   1 
HETATM 1535 O O   . HOH   F 5 .   ? -16.610 20.431  -14.085 1.00 21.43 ? 305 HOH   B O   1 
HETATM 1536 O O   . HOH   F 5 .   ? -9.294  -7.014  -25.475 1.00 15.56 ? 306 HOH   B O   1 
HETATM 1537 O O   . HOH   F 5 .   ? -12.617 -4.793  -9.398  1.00 38.15 ? 307 HOH   B O   1 
HETATM 1538 O O   . HOH   F 5 .   ? -15.284 8.705   -0.494  1.00 36.02 ? 308 HOH   B O   1 
HETATM 1539 O O   . HOH   F 5 .   ? -8.783  -11.595 -7.313  1.00 21.44 ? 309 HOH   B O   1 
HETATM 1540 O O   . HOH   F 5 .   ? -24.727 -6.673  -4.511  1.00 12.55 ? 310 HOH   B O   1 
HETATM 1541 O O   . HOH   F 5 .   ? -20.471 14.002  -33.478 1.00 14.77 ? 311 HOH   B O   1 
HETATM 1542 O O   . HOH   F 5 .   ? -27.956 -6.756  -18.806 1.00 32.74 ? 312 HOH   B O   1 
HETATM 1543 O O   . HOH   F 5 .   ? -29.186 -4.610  -22.158 1.00 35.93 ? 313 HOH   B O   1 
HETATM 1544 O O   . HOH   F 5 .   ? -17.277 12.627  -5.664  1.00 23.08 ? 314 HOH   B O   1 
HETATM 1545 O O   . HOH   F 5 .   ? -16.247 -14.857 -30.614 1.00 8.98  ? 315 HOH   B O   1 
HETATM 1546 O O   . HOH   F 5 .   ? -27.591 20.075  -15.334 1.00 32.72 ? 316 HOH   B O   1 
HETATM 1547 O O   . HOH   F 5 .   ? -26.532 -8.566  -16.587 1.00 24.87 ? 317 HOH   B O   1 
HETATM 1548 O O   . HOH   F 5 .   ? -30.985 -6.081  -1.346  1.00 6.68  ? 318 HOH   B O   1 
HETATM 1549 O O   . HOH   F 5 .   ? -20.647 2.004   -32.678 1.00 23.56 ? 319 HOH   B O   1 
HETATM 1550 O O   . HOH   F 5 .   ? -30.705 12.872  -16.281 1.00 37.27 ? 320 HOH   B O   1 
HETATM 1551 O O   . HOH   F 5 .   ? -22.784 -5.920  0.485   1.00 25.23 ? 321 HOH   B O   1 
HETATM 1552 O O   . HOH   F 5 .   ? -30.887 4.231   -2.468  1.00 21.74 ? 322 HOH   B O   1 
HETATM 1553 O O   . HOH   F 5 .   ? -3.311  -12.190 -6.598  1.00 25.05 ? 323 HOH   B O   1 
HETATM 1554 O O   . HOH   F 5 .   ? -14.433 -13.522 -16.457 1.00 12.90 ? 324 HOH   B O   1 
HETATM 1555 O O   . HOH   F 5 .   ? -15.807 7.724   -30.194 1.00 12.86 ? 325 HOH   B O   1 
HETATM 1556 O O   . HOH   F 5 .   ? -18.262 15.564  -22.220 1.00 14.52 ? 326 HOH   B O   1 
HETATM 1557 O O   . HOH   F 5 .   ? -20.790 -14.475 -22.241 1.00 14.67 ? 327 HOH   B O   1 
HETATM 1558 O O   . HOH   F 5 .   ? -9.220  -15.848 -23.968 1.00 10.49 ? 328 HOH   B O   1 
HETATM 1559 O O   . HOH   F 5 .   ? -14.473 -6.786  -1.310  1.00 20.03 ? 329 HOH   B O   1 
HETATM 1560 O O   . HOH   F 5 .   ? 0.623   -0.286  -13.609 1.00 23.65 ? 330 HOH   B O   1 
HETATM 1561 O O   . HOH   F 5 .   ? -35.690 0.730   -7.897  1.00 22.72 ? 331 HOH   B O   1 
HETATM 1562 O O   . HOH   F 5 .   ? -14.654 -5.230  1.340   1.00 3.00  ? 332 HOH   B O   1 
HETATM 1563 O O   . HOH   F 5 .   ? -16.488 1.774   -34.107 1.00 36.58 ? 333 HOH   B O   1 
HETATM 1564 O O   . HOH   F 5 .   ? -32.710 6.663   -4.294  1.00 34.93 ? 334 HOH   B O   1 
HETATM 1565 O O   . HOH   F 5 .   ? -16.468 -11.237 -16.125 1.00 19.28 ? 335 HOH   B O   1 
HETATM 1566 O O   . HOH   F 5 .   ? 4.883   -2.937  -15.994 1.00 25.97 ? 336 HOH   B O   1 
HETATM 1567 O O   . HOH   F 5 .   ? -10.028 7.814   -13.604 1.00 23.96 ? 337 HOH   B O   1 
HETATM 1568 O O   . HOH   F 5 .   ? -31.576 -7.848  -6.474  1.00 33.16 ? 338 HOH   B O   1 
HETATM 1569 O O   . HOH   F 5 .   ? -17.058 13.200  -31.316 1.00 18.94 ? 339 HOH   B O   1 
HETATM 1570 O O   . HOH   F 5 .   ? -12.190 13.849  -14.558 1.00 12.97 ? 340 HOH   B O   1 
HETATM 1571 O O   . HOH   F 5 .   ? -36.258 5.041   -9.978  1.00 23.11 ? 341 HOH   B O   1 
HETATM 1572 O O   . HOH   F 5 .   ? -11.481 -11.475 -8.348  1.00 23.00 ? 342 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   ? 0.8834 0.3712 0.4299 0.2127  0.0063  -0.1485 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.8742 0.4219 0.3996 0.2276  0.0129  -0.1326 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.8748 0.4084 0.3916 0.2196  0.0310  -0.0899 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.9004 0.3676 0.4123 0.2153  0.0394  -0.0695 50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.9047 0.4624 0.4049 0.2665  0.0034  -0.1506 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.9346 0.5706 0.4336 0.2770  -0.0028 -0.1766 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.9337 0.5809 0.4417 0.2734  -0.0139 -0.2077 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.9433 0.6291 0.4324 0.2892  0.0039  -0.1665 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8446 0.4405 0.3587 0.2181  0.0376  -0.0765 51  MET   A N   
10   C CA  . MET   A 8   ? 0.8445 0.4403 0.3487 0.2150  0.0524  -0.0416 51  MET   A CA  
11   C C   . MET   A 8   ? 0.8422 0.4507 0.3197 0.2480  0.0489  -0.0388 51  MET   A C   
12   O O   . MET   A 8   ? 0.8295 0.4736 0.3053 0.2660  0.0388  -0.0624 51  MET   A O   
13   C CB  . MET   A 8   ? 0.8279 0.4834 0.3514 0.1927  0.0595  -0.0318 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.8480 0.4989 0.4029 0.1607  0.0625  -0.0337 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.8730 0.5918 0.4470 0.1415  0.0694  -0.0199 51  MET   A SD  
16   C CE  . MET   A 8   ? 0.8525 0.5571 0.4683 0.1071  0.0721  -0.0249 51  MET   A CE  
17   N N   . TYR   A 9   ? 0.8494 0.4329 0.3068 0.2571  0.0575  -0.0117 52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.8509 0.4466 0.2854 0.2901  0.0513  -0.0109 52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.8531 0.4648 0.2772 0.2899  0.0611  0.0155  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.8668 0.4568 0.2907 0.2699  0.0750  0.0385  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.8782 0.4079 0.2859 0.3194  0.0423  -0.0145 52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.9196 0.3727 0.3046 0.3155  0.0534  0.0162  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.9453 0.3428 0.3420 0.2928  0.0597  0.0191  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.9461 0.3813 0.2972 0.3356  0.0580  0.0417  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.9861 0.3113 0.3637 0.2864  0.0747  0.0509  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.9869 0.3515 0.3109 0.3329  0.0721  0.0739  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 1.0126 0.3205 0.3503 0.3074  0.0822  0.0802  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 1.0590 0.2960 0.3720 0.3019  0.1008  0.1155  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.8341 0.4853 0.2522 0.3129  0.0540  0.0098  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.8255 0.4947 0.2345 0.3164  0.0595  0.0287  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.8647 0.4953 0.2348 0.3526  0.0524  0.0374  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.8806 0.4891 0.2378 0.3791  0.0394  0.0230  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.7769 0.5220 0.2142 0.3104  0.0572  0.0170  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.7609 0.5391 0.2046 0.3366  0.0438  -0.0075 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.7598 0.5350 0.2255 0.2791  0.0636  0.0127  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.7355 0.5797 0.2069 0.3321  0.0438  -0.0147 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.8775 0.4993 0.2260 0.3561  0.0602  0.0604  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.9157 0.5015 0.2185 0.3924  0.0538  0.0724  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.9117 0.5372 0.2091 0.3991  0.0543  0.0785  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.9129 0.5452 0.2165 0.3746  0.0707  0.0953  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.9797 0.4848 0.2455 0.3896  0.0689  0.1030  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 1.0620 0.5042 0.3114 0.4051  0.0612  0.0989  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.1785 0.5333 0.3891 0.4046  0.0773  0.1328  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.2113 0.5533 0.3938 0.4033  0.0936  0.1618  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.2205 0.5179 0.4287 0.4062  0.0744  0.1301  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.9044 0.5557 0.1919 0.4331  0.0357  0.0632  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.8988 0.5889 0.1848 0.4404  0.0331  0.0634  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.9404 0.5913 0.1809 0.4435  0.0483  0.0946  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.9867 0.5749 0.1799 0.4601  0.0536  0.1155  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.8945 0.6183 0.1805 0.4783  0.0076  0.0376  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.8782 0.6671 0.1997 0.4710  0.0023  0.0220  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.8759 0.7089 0.2168 0.5015  -0.0232 -0.0105 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.8644 0.7544 0.2433 0.4928  -0.0285 -0.0263 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.9041 0.7976 0.2596 0.5117  -0.0364 -0.0260 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.9446 0.7891 0.2332 0.5407  -0.0376 -0.0070 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.8763 0.8200 0.2732 0.5023  -0.0427 -0.0442 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.9229 0.6100 0.1772 0.4285  0.0567  0.0983  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.9499 0.6124 0.1653 0.4303  0.0742  0.1254  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.9469 0.6450 0.1463 0.4562  0.0627  0.1156  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.9806 0.6567 0.1337 0.4700  0.0743  0.1362  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.9411 0.6089 0.1868 0.3869  0.0986  0.1401  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.9108 0.6634 0.1488 0.4628  0.0410  0.0839  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.9037 0.6917 0.1345 0.4874  0.0258  0.0677  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.8617 0.7139 0.1575 0.4748  0.0109  0.0357  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.8370 0.7090 0.1817 0.4459  0.0145  0.0287  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.8491 0.7331 0.1450 0.4974  -0.0062 0.0157  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.8156 0.7569 0.1769 0.4845  -0.0199 -0.0147 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.8065 0.7615 0.1948 0.4523  -0.0032 -0.0054 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.8269 0.7563 0.1788 0.4497  0.0143  0.0183  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.8301 0.7987 0.1840 0.5223  -0.0473 -0.0438 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.8982 0.8646 0.2312 0.5612  -0.0711 -0.0611 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.9105 0.8536 0.2375 0.5592  -0.0664 -0.0515 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.9300 0.9186 0.2525 0.5964  -0.0963 -0.0865 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.7702 0.7663 0.2223 0.4299  -0.0086 -0.0242 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.7607 0.7699 0.2394 0.4048  0.0025  -0.0184 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.7570 0.7941 0.2486 0.4247  -0.0167 -0.0453 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.7243 0.7949 0.2695 0.4192  -0.0317 -0.0713 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.7368 0.7645 0.2715 0.3675  0.0108  -0.0170 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.7626 0.7674 0.2856 0.3529  0.0242  0.0011  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.7294 0.7633 0.2834 0.3465  0.0212  -0.0080 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7538 0.7845 0.3256 0.3305  0.0247  -0.0075 59  ILE   A CD1 
82   N N   . THR   A 17  ? 0.7873 0.8107 0.2290 0.4491  -0.0158 -0.0402 60  THR   A N   
83   C CA  . THR   A 17  ? 0.7993 0.8466 0.2419 0.4746  -0.0357 -0.0680 60  THR   A CA  
84   C C   . THR   A 17  ? 0.8259 0.8673 0.2427 0.4758  -0.0214 -0.0562 60  THR   A C   
85   O O   . THR   A 17  ? 0.8501 0.8631 0.2218 0.4732  0.0023  -0.0250 60  THR   A O   
86   C CB  . THR   A 17  ? 0.8408 0.8827 0.2325 0.5208  -0.0562 -0.0816 60  THR   A CB  
87   O OG1 . THR   A 17  ? 0.8895 0.8882 0.2053 0.5359  -0.0378 -0.0480 60  THR   A OG1 
88   C CG2 . THR   A 17  ? 0.8335 0.8911 0.2567 0.5264  -0.0753 -0.1019 60  THR   A CG2 
89   N N   . TRP   A 18  ? 0.8211 0.8896 0.2684 0.4808  -0.0353 -0.0827 61  TRP   A N   
90   C CA  . TRP   A 18  ? 0.8557 0.9242 0.2794 0.4877  -0.0240 -0.0775 61  TRP   A CA  
91   C C   . TRP   A 18  ? 0.9211 0.9822 0.2690 0.5344  -0.0308 -0.0817 61  TRP   A C   
92   O O   . TRP   A 18  ? 0.9193 0.9957 0.2625 0.5646  -0.0596 -0.1123 61  TRP   A O   
93   C CB  . TRP   A 18  ? 0.8238 0.9205 0.3071 0.4798  -0.0394 -0.1077 61  TRP   A CB  
94   C CG  . TRP   A 18  ? 0.8354 0.9374 0.2988 0.4918  -0.0316 -0.1098 61  TRP   A CG  
95   C CD1 . TRP   A 18  ? 0.8534 0.9674 0.2795 0.5309  -0.0455 -0.1336 61  TRP   A CD1 
96   C CD2 . TRP   A 18  ? 0.8310 0.9311 0.3139 0.4668  -0.0100 -0.0914 61  TRP   A CD2 
97   N NE1 . TRP   A 18  ? 0.8564 0.9761 0.2760 0.5315  -0.0311 -0.1300 61  TRP   A NE1 
98   C CE2 . TRP   A 18  ? 0.8461 0.9581 0.3027 0.4923  -0.0096 -0.1044 61  TRP   A CE2 
99   C CE3 . TRP   A 18  ? 0.8272 0.9187 0.3436 0.4285  0.0085  -0.0659 61  TRP   A CE3 
100  C CZ2 . TRP   A 18  ? 0.8492 0.9667 0.3187 0.4796  0.0088  -0.0939 61  TRP   A CZ2 
101  C CZ3 . TRP   A 18  ? 0.8313 0.9279 0.3611 0.4165  0.0236  -0.0563 61  TRP   A CZ3 
102  C CH2 . TRP   A 18  ? 0.8384 0.9483 0.3464 0.4415  0.0245  -0.0699 61  TRP   A CH2 
103  N N   . GLU   A 19  ? 0.9719 1.0113 0.2610 0.5412  -0.0042 -0.0512 62  GLU   A N   
104  C CA  . GLU   A 19  ? 1.0306 1.0586 0.2376 0.5863  -0.0054 -0.0482 62  GLU   A CA  
105  C C   . GLU   A 19  ? 1.0557 1.1004 0.2392 0.6020  0.0039  -0.0542 62  GLU   A C   
106  O O   . GLU   A 19  ? 1.0605 1.0978 0.2383 0.5818  0.0359  -0.0267 62  GLU   A O   
107  C CB  . GLU   A 19  ? 1.1035 1.0869 0.2501 0.5865  0.0210  -0.0043 62  GLU   A CB  
108  C CG  . GLU   A 19  ? 1.1713 1.1347 0.3334 0.5766  0.0116  0.0008  62  GLU   A CG  
109  C CD  . GLU   A 19  ? 1.2553 1.2285 0.4042 0.6147  -0.0247 -0.0291 62  GLU   A CD  
110  O OE1 . GLU   A 19  ? 1.3041 1.2617 0.3785 0.6588  -0.0316 -0.0258 62  GLU   A OE1 
111  O OE2 . GLU   A 19  ? 1.2462 1.2444 0.4601 0.6009  -0.0458 -0.0557 62  GLU   A OE2 
112  N N   . LYS   A 20  ? 1.0687 1.1387 0.2394 0.6397  -0.0246 -0.0926 63  LYS   A N   
113  C CA  . LYS   A 20  ? 1.0925 1.1824 0.2366 0.6624  -0.0199 -0.1059 63  LYS   A CA  
114  C C   . LYS   A 20  ? 1.1450 1.2124 0.1994 0.6818  0.0143  -0.0670 63  LYS   A C   
115  O O   . LYS   A 20  ? 1.1780 1.2138 0.1760 0.6958  0.0208  -0.0413 63  LYS   A O   
116  C CB  . LYS   A 20  ? 1.1207 1.2381 0.2543 0.7071  -0.0607 -0.1562 63  LYS   A CB  
117  C CG  . LYS   A 20  ? 1.1435 1.2879 0.3692 0.6919  -0.0957 -0.2019 63  LYS   A CG  
118  C CD  . LYS   A 20  ? 1.1959 1.3699 0.4065 0.7397  -0.1339 -0.2551 63  LYS   A CD  
119  C CE  . LYS   A 20  ? 1.2044 1.4043 0.5059 0.7288  -0.1722 -0.3045 63  LYS   A CE  
120  N NZ  . LYS   A 20  ? 1.2280 1.4312 0.5382 0.7380  -0.1961 -0.3162 63  LYS   A NZ  
121  N N   . ASP   A 21  ? 1.1539 1.2375 0.1944 0.6852  0.0362  -0.0636 64  ASP   A N   
122  C CA  . ASP   A 21  ? 1.2046 1.2728 0.1632 0.7023  0.0743  -0.0266 64  ASP   A CA  
123  C C   . ASP   A 21  ? 1.2194 1.2500 0.1746 0.6652  0.1120  0.0255  64  ASP   A C   
124  O O   . ASP   A 21  ? 1.2605 1.2573 0.1420 0.6811  0.1334  0.0604  64  ASP   A O   
125  C CB  . ASP   A 21  ? 1.2765 1.3371 0.1385 0.7611  0.0607  -0.0322 64  ASP   A CB  
126  C CG  . ASP   A 21  ? 1.3659 1.4668 0.2155 0.8036  0.0310  -0.0823 64  ASP   A CG  
127  O OD1 . ASP   A 21  ? 1.3730 1.5024 0.2461 0.7980  0.0433  -0.0950 64  ASP   A OD1 
128  O OD2 . ASP   A 21  ? 1.4139 1.5188 0.2288 0.8452  -0.0056 -0.1107 64  ASP   A OD2 
129  N N   . ALA   A 22  ? 1.1836 1.2181 0.2182 0.6168  0.1187  0.0301  65  ALA   A N   
130  C CA  . ALA   A 22  ? 1.1888 1.1933 0.2344 0.5778  0.1513  0.0723  65  ALA   A CA  
131  C C   . ALA   A 22  ? 1.1815 1.2014 0.2294 0.5613  0.1922  0.0931  65  ALA   A C   
132  O O   . ALA   A 22  ? 1.1628 1.2201 0.2199 0.5753  0.1904  0.0703  65  ALA   A O   
133  C CB  . ALA   A 22  ? 1.1613 1.1668 0.2889 0.5377  0.1354  0.0633  65  ALA   A CB  
134  N N   . GLU   A 23  ? 1.1910 1.1844 0.2350 0.5321  0.2285  0.1337  66  GLU   A N   
135  C CA  . GLU   A 23  ? 1.1848 1.1965 0.2399 0.5124  0.2700  0.1540  66  GLU   A CA  
136  C C   . GLU   A 23  ? 1.1222 1.1753 0.2654 0.4835  0.2625  0.1307  66  GLU   A C   
137  O O   . GLU   A 23  ? 1.1019 1.1474 0.3027 0.4477  0.2558  0.1334  66  GLU   A O   
138  C CB  . GLU   A 23  ? 1.2531 1.2241 0.2981 0.4823  0.3065  0.1993  66  GLU   A CB  
139  C CG  . GLU   A 23  ? 1.3267 1.3183 0.3917 0.4574  0.3525  0.2213  66  GLU   A CG  
140  C CD  . GLU   A 23  ? 1.4247 1.3804 0.5083 0.4168  0.3840  0.2584  66  GLU   A CD  
141  O OE1 . GLU   A 23  ? 1.4630 1.3691 0.5285 0.4129  0.3729  0.2718  66  GLU   A OE1 
142  O OE2 . GLU   A 23  ? 1.4313 1.4101 0.5514 0.3892  0.4190  0.2716  66  GLU   A OE2 
143  N N   . VAL   A 24  ? 1.0889 1.1845 0.2393 0.5016  0.2629  0.1076  67  VAL   A N   
144  C CA  . VAL   A 24  ? 1.0422 1.1742 0.2721 0.4802  0.2533  0.0849  67  VAL   A CA  
145  C C   . VAL   A 24  ? 1.0199 1.1736 0.2821 0.4520  0.2926  0.1056  67  VAL   A C   
146  O O   . VAL   A 24  ? 1.0259 1.2055 0.2620 0.4684  0.3199  0.1091  67  VAL   A O   
147  C CB  . VAL   A 24  ? 1.0293 1.1947 0.2675 0.5123  0.2254  0.0418  67  VAL   A CB  
148  C CG1 . VAL   A 24  ? 1.0003 1.1861 0.3237 0.4882  0.2059  0.0201  67  VAL   A CG1 
149  C CG2 . VAL   A 24  ? 1.0479 1.1975 0.2478 0.5456  0.1895  0.0188  67  VAL   A CG2 
150  N N   . THR   A 25  ? 0.9932 1.1411 0.3148 0.4109  0.2947  0.1164  68  THR   A N   
151  C CA  . THR   A 25  ? 0.9665 1.1386 0.3310 0.3811  0.3278  0.1319  68  THR   A CA  
152  C C   . THR   A 25  ? 0.9255 1.1111 0.3710 0.3493  0.3078  0.1195  68  THR   A C   
153  O O   . THR   A 25  ? 0.9220 1.0900 0.3833 0.3466  0.2743  0.1068  68  THR   A O   
154  C CB  . THR   A 25  ? 1.0047 1.1445 0.3375 0.3624  0.3653  0.1722  68  THR   A CB  
155  O OG1 . THR   A 25  ? 0.9945 1.1653 0.3743 0.3343  0.3993  0.1834  68  THR   A OG1 
156  C CG2 . THR   A 25  ? 1.0181 1.1111 0.3582 0.3398  0.3495  0.1844  68  THR   A CG2 
157  N N   . GLY   A 26  ? 0.8915 1.1104 0.3870 0.3271  0.3288  0.1230  69  GLY   A N   
158  C CA  . GLY   A 26  ? 0.8614 1.0951 0.4282 0.3005  0.3105  0.1126  69  GLY   A CA  
159  C C   . GLY   A 26  ? 0.8290 1.1024 0.4365 0.3153  0.2913  0.0834  69  GLY   A C   
160  O O   . GLY   A 26  ? 0.8371 1.1063 0.4287 0.3417  0.2656  0.0624  69  GLY   A O   
161  N N   . ASN   A 27  ? 0.7884 1.0998 0.4524 0.2985  0.3019  0.0800  70  ASN   A N   
162  C CA  . ASN   A 27  ? 0.7543 1.1027 0.4633 0.3121  0.2831  0.0531  70  ASN   A CA  
163  C C   . ASN   A 27  ? 0.7234 1.0512 0.4652 0.3034  0.2423  0.0432  70  ASN   A C   
164  O O   . ASN   A 27  ? 0.7429 1.0357 0.4744 0.2853  0.2332  0.0567  70  ASN   A O   
165  C CB  . ASN   A 27  ? 0.7452 1.1447 0.5043 0.2984  0.3093  0.0533  70  ASN   A CB  
166  C CG  . ASN   A 27  ? 0.7780 1.1763 0.5840 0.2613  0.3083  0.0648  70  ASN   A CG  
167  O OD1 . ASN   A 27  ? 0.8140 1.1818 0.6025 0.2385  0.3215  0.0866  70  ASN   A OD1 
168  N ND2 . ASN   A 27  ? 0.7529 1.1822 0.6180 0.2571  0.2897  0.0486  70  ASN   A ND2 
169  N N   . SER   A 28  ? 0.6775 1.0250 0.4562 0.3173  0.2193  0.0208  71  SER   A N   
170  C CA  . SER   A 28  ? 0.6591 0.9843 0.4644 0.3109  0.1841  0.0152  71  SER   A CA  
171  C C   . SER   A 28  ? 0.6072 0.9631 0.4706 0.3035  0.1754  0.0088  71  SER   A C   
172  O O   . SER   A 28  ? 0.5960 0.9667 0.4834 0.3244  0.1592  -0.0107 71  SER   A O   
173  C CB  . SER   A 28  ? 0.6839 0.9910 0.4771 0.3374  0.1581  -0.0056 71  SER   A CB  
174  O OG  . SER   A 28  ? 0.7303 1.0262 0.4731 0.3560  0.1657  -0.0097 71  SER   A OG  
175  N N   . PRO   A 29  ? 0.5727 0.9382 0.4605 0.2764  0.1834  0.0225  72  PRO   A N   
176  C CA  . PRO   A 29  ? 0.5262 0.9274 0.4695 0.2731  0.1732  0.0133  72  PRO   A CA  
177  C C   . PRO   A 29  ? 0.5049 0.8846 0.4652 0.2730  0.1375  0.0122  72  PRO   A C   
178  O O   . PRO   A 29  ? 0.5201 0.8599 0.4555 0.2620  0.1264  0.0244  72  PRO   A O   
179  C CB  . PRO   A 29  ? 0.5219 0.9458 0.4857 0.2444  0.1974  0.0252  72  PRO   A CB  
180  C CG  . PRO   A 29  ? 0.5606 0.9412 0.4782 0.2280  0.2092  0.0451  72  PRO   A CG  
181  C CD  . PRO   A 29  ? 0.5737 0.9206 0.4416 0.2499  0.2017  0.0437  72  PRO   A CD  
182  N N   . ARG   A 30  ? 0.4708 0.8774 0.4722 0.2865  0.1208  -0.0015 73  ARG   A N   
183  C CA  . ARG   A 30  ? 0.4671 0.8542 0.4832 0.2884  0.0883  0.0010  73  ARG   A CA  
184  C C   . ARG   A 30  ? 0.4159 0.8379 0.4678 0.2728  0.0870  0.0023  73  ARG   A C   
185  O O   . ARG   A 30  ? 0.3849 0.8548 0.4785 0.2823  0.0891  -0.0127 73  ARG   A O   
186  C CB  . ARG   A 30  ? 0.4941 0.8811 0.5296 0.3187  0.0661  -0.0153 73  ARG   A CB  
187  C CG  . ARG   A 30  ? 0.5871 0.9329 0.5952 0.3340  0.0573  -0.0202 73  ARG   A CG  
188  C CD  . ARG   A 30  ? 0.6508 0.9925 0.6847 0.3627  0.0336  -0.0373 73  ARG   A CD  
189  N NE  . ARG   A 30  ? 0.7250 1.0379 0.7431 0.3803  0.0270  -0.0513 73  ARG   A NE  
190  C CZ  . ARG   A 30  ? 0.7870 1.0496 0.8011 0.3828  0.0049  -0.0482 73  ARG   A CZ  
191  N NH1 . ARG   A 30  ? 0.7957 1.0296 0.8136 0.3697  -0.0101 -0.0274 73  ARG   A NH1 
192  N NH2 . ARG   A 30  ? 0.7976 1.0391 0.8045 0.3982  -0.0017 -0.0663 73  ARG   A NH2 
193  N N   . LEU   A 31  ? 0.4051 0.8075 0.4436 0.2500  0.0835  0.0169  74  LEU   A N   
194  C CA  . LEU   A 31  ? 0.3706 0.8056 0.4422 0.2340  0.0806  0.0145  74  LEU   A CA  
195  C C   . LEU   A 31  ? 0.3663 0.7854 0.4364 0.2384  0.0478  0.0192  74  LEU   A C   
196  O O   . LEU   A 31  ? 0.3935 0.7672 0.4255 0.2345  0.0389  0.0341  74  LEU   A O   
197  C CB  . LEU   A 31  ? 0.3741 0.8012 0.4322 0.2041  0.1032  0.0248  74  LEU   A CB  
198  C CG  . LEU   A 31  ? 0.3923 0.8135 0.4287 0.1987  0.1364  0.0303  74  LEU   A CG  
199  C CD1 . LEU   A 31  ? 0.4160 0.8077 0.4263 0.1735  0.1506  0.0450  74  LEU   A CD1 
200  C CD2 . LEU   A 31  ? 0.3690 0.8433 0.4448 0.2005  0.1599  0.0184  74  LEU   A CD2 
201  N N   . ASP   A 32  ? 0.3295 0.7882 0.4399 0.2468  0.0309  0.0068  75  ASP   A N   
202  C CA  . ASP   A 32  ? 0.3367 0.7818 0.4392 0.2544  -0.0008 0.0125  75  ASP   A CA  
203  C C   . ASP   A 32  ? 0.3309 0.7777 0.4262 0.2288  0.0005  0.0163  75  ASP   A C   
204  O O   . ASP   A 32  ? 0.3025 0.7942 0.4382 0.2163  0.0058  0.0011  75  ASP   A O   
205  C CB  . ASP   A 32  ? 0.3334 0.8202 0.4788 0.2787  -0.0237 -0.0043 75  ASP   A CB  
206  C CG  . ASP   A 32  ? 0.4028 0.8597 0.5363 0.3098  -0.0441 0.0000  75  ASP   A CG  
207  O OD1 . ASP   A 32  ? 0.4272 0.8430 0.5287 0.3176  -0.0656 0.0169  75  ASP   A OD1 
208  O OD2 . ASP   A 32  ? 0.4281 0.9010 0.5837 0.3266  -0.0373 -0.0135 75  ASP   A OD2 
209  N N   . VAL   A 33  ? 0.3538 0.7536 0.4017 0.2200  -0.0027 0.0342  76  VAL   A N   
210  C CA  . VAL   A 33  ? 0.3587 0.7557 0.3953 0.1976  -0.0012 0.0357  76  VAL   A CA  
211  C C   . VAL   A 33  ? 0.3750 0.7540 0.3815 0.2054  -0.0286 0.0444  76  VAL   A C   
212  O O   . VAL   A 33  ? 0.3878 0.7460 0.3751 0.2262  -0.0453 0.0557  76  VAL   A O   
213  C CB  . VAL   A 33  ? 0.3866 0.7504 0.3931 0.1777  0.0251  0.0464  76  VAL   A CB  
214  C CG1 . VAL   A 33  ? 0.3830 0.7598 0.4063 0.1743  0.0529  0.0420  76  VAL   A CG1 
215  C CG2 . VAL   A 33  ? 0.4261 0.7406 0.3846 0.1845  0.0199  0.0644  76  VAL   A CG2 
216  N N   . ALA   A 34  ? 0.3718 0.7584 0.3742 0.1895  -0.0324 0.0386  77  ALA   A N   
217  C CA  . ALA   A 34  ? 0.3892 0.7630 0.3572 0.1960  -0.0549 0.0445  77  ALA   A CA  
218  C C   . ALA   A 34  ? 0.4080 0.7550 0.3438 0.1751  -0.0419 0.0496  77  ALA   A C   
219  O O   . ALA   A 34  ? 0.4068 0.7560 0.3596 0.1542  -0.0215 0.0420  77  ALA   A O   
220  C CB  . ALA   A 34  ? 0.3634 0.7840 0.3635 0.2034  -0.0798 0.0231  77  ALA   A CB  
221  N N   . LEU   A 35  ? 0.4206 0.7405 0.3087 0.1819  -0.0520 0.0638  78  LEU   A N   
222  C CA  . LEU   A 35  ? 0.4321 0.7292 0.2893 0.1661  -0.0413 0.0664  78  LEU   A CA  
223  C C   . LEU   A 35  ? 0.4367 0.7465 0.2728 0.1725  -0.0635 0.0583  78  LEU   A C   
224  O O   . LEU   A 35  ? 0.4513 0.7562 0.2565 0.1925  -0.0804 0.0708  78  LEU   A O   
225  C CB  . LEU   A 35  ? 0.4541 0.7092 0.2736 0.1670  -0.0268 0.0892  78  LEU   A CB  
226  C CG  . LEU   A 35  ? 0.4807 0.7141 0.2690 0.1542  -0.0157 0.0914  78  LEU   A CG  
227  C CD1 . LEU   A 35  ? 0.4792 0.7134 0.2883 0.1354  0.0007  0.0779  78  LEU   A CD1 
228  C CD2 . LEU   A 35  ? 0.5056 0.7062 0.2643 0.1572  -0.0045 0.1117  78  LEU   A CD2 
229  N N   . ASP   A 36  ? 0.4187 0.7452 0.2726 0.1571  -0.0646 0.0361  79  ASP   A N   
230  C CA  . ASP   A 36  ? 0.4164 0.7604 0.2541 0.1645  -0.0885 0.0210  79  ASP   A CA  
231  C C   . ASP   A 36  ? 0.4389 0.7529 0.2195 0.1650  -0.0837 0.0315  79  ASP   A C   
232  O O   . ASP   A 36  ? 0.4555 0.7376 0.2184 0.1557  -0.0610 0.0470  79  ASP   A O   
233  C CB  . ASP   A 36  ? 0.4087 0.7886 0.3000 0.1490  -0.0965 -0.0131 79  ASP   A CB  
234  C CG  . ASP   A 36  ? 0.4727 0.8350 0.3736 0.1229  -0.0788 -0.0246 79  ASP   A CG  
235  O OD1 . ASP   A 36  ? 0.5170 0.8404 0.3818 0.1180  -0.0600 -0.0071 79  ASP   A OD1 
236  O OD2 . ASP   A 36  ? 0.4687 0.8554 0.4154 0.1078  -0.0850 -0.0523 79  ASP   A OD2 
237  N N   . GLU   A 37  ? 0.4339 0.7619 0.1853 0.1784  -0.1058 0.0213  80  GLU   A N   
238  C CA  . GLU   A 37  ? 0.4572 0.7656 0.1537 0.1822  -0.1022 0.0278  80  GLU   A CA  
239  C C   . GLU   A 37  ? 0.4537 0.7443 0.1585 0.1600  -0.0839 0.0149  80  GLU   A C   
240  O O   . GLU   A 37  ? 0.4728 0.7417 0.1382 0.1608  -0.0721 0.0247  80  GLU   A O   
241  C CB  . GLU   A 37  ? 0.4800 0.8145 0.1468 0.2028  -0.1318 0.0122  80  GLU   A CB  
242  C CG  . GLU   A 37  ? 0.5619 0.8813 0.1637 0.2127  -0.1276 0.0214  80  GLU   A CG  
243  C CD  . GLU   A 37  ? 0.6129 0.9600 0.1812 0.2340  -0.1567 0.0003  80  GLU   A CD  
244  O OE1 . GLU   A 37  ? 0.6097 0.9615 0.1698 0.2289  -0.1598 -0.0255 80  GLU   A OE1 
245  O OE2 . GLU   A 37  ? 0.6382 1.0018 0.1875 0.2582  -0.1782 0.0079  80  GLU   A OE2 
246  N N   . SER   A 38  ? 0.4238 0.7224 0.1808 0.1406  -0.0800 -0.0056 81  SER   A N   
247  C CA  . SER   A 38  ? 0.4236 0.6998 0.1907 0.1204  -0.0639 -0.0169 81  SER   A CA  
248  C C   . SER   A 38  ? 0.4279 0.6746 0.2038 0.1078  -0.0352 0.0027  81  SER   A C   
249  O O   . SER   A 38  ? 0.4387 0.6652 0.2278 0.0917  -0.0218 -0.0052 81  SER   A O   
250  C CB  . SER   A 38  ? 0.4173 0.7144 0.2355 0.1049  -0.0750 -0.0500 81  SER   A CB  
251  O OG  . SER   A 38  ? 0.4452 0.7711 0.2536 0.1186  -0.1053 -0.0742 81  SER   A OG  
252  N N   . GLY   A 39  ? 0.4213 0.6637 0.1898 0.1165  -0.0272 0.0265  82  GLY   A N   
253  C CA  . GLY   A 39  ? 0.4227 0.6405 0.1962 0.1089  -0.0032 0.0426  82  GLY   A CA  
254  C C   . GLY   A 39  ? 0.3979 0.6248 0.2179 0.0961  0.0084  0.0377  82  GLY   A C   
255  O O   . GLY   A 39  ? 0.4015 0.6084 0.2213 0.0915  0.0286  0.0493  82  GLY   A O   
256  N N   . ASP   A 40  ? 0.3678 0.6281 0.2281 0.0913  -0.0039 0.0194  83  ASP   A N   
257  C CA  . ASP   A 40  ? 0.3458 0.6234 0.2568 0.0777  0.0094  0.0134  83  ASP   A CA  
258  C C   . ASP   A 40  ? 0.3378 0.6355 0.2620 0.0920  0.0089  0.0238  83  ASP   A C   
259  O O   . ASP   A 40  ? 0.3310 0.6473 0.2494 0.1100  -0.0127 0.0236  83  ASP   A O   
260  C CB  . ASP   A 40  ? 0.3322 0.6436 0.2918 0.0649  -0.0041 -0.0150 83  ASP   A CB  
261  C CG  . ASP   A 40  ? 0.3901 0.6816 0.3508 0.0476  -0.0034 -0.0310 83  ASP   A CG  
262  O OD1 . ASP   A 40  ? 0.3995 0.6595 0.3626 0.0315  0.0206  -0.0236 83  ASP   A OD1 
263  O OD2 . ASP   A 40  ? 0.4299 0.7368 0.3885 0.0523  -0.0282 -0.0522 83  ASP   A OD2 
264  N N   . PHE   A 41  ? 0.3358 0.6289 0.2756 0.0863  0.0323  0.0323  84  PHE   A N   
265  C CA  . PHE   A 41  ? 0.3330 0.6462 0.2891 0.1008  0.0327  0.0377  84  PHE   A CA  
266  C C   . PHE   A 41  ? 0.3219 0.6820 0.3390 0.0926  0.0341  0.0195  84  PHE   A C   
267  O O   . PHE   A 41  ? 0.3102 0.6751 0.3559 0.0710  0.0536  0.0128  84  PHE   A O   
268  C CB  . PHE   A 41  ? 0.3389 0.6257 0.2751 0.1036  0.0559  0.0539  84  PHE   A CB  
269  C CG  . PHE   A 41  ? 0.3628 0.6161 0.2530 0.1176  0.0509  0.0696  84  PHE   A CG  
270  C CD1 . PHE   A 41  ? 0.3686 0.6255 0.2542 0.1364  0.0361  0.0756  84  PHE   A CD1 
271  C CD2 . PHE   A 41  ? 0.3872 0.6052 0.2430 0.1118  0.0619  0.0779  84  PHE   A CD2 
272  C CE1 . PHE   A 41  ? 0.3938 0.6198 0.2451 0.1454  0.0341  0.0899  84  PHE   A CE1 
273  C CE2 . PHE   A 41  ? 0.4096 0.6032 0.2324 0.1228  0.0584  0.0896  84  PHE   A CE2 
274  C CZ  . PHE   A 41  ? 0.4051 0.6029 0.2279 0.1376  0.0457  0.0957  84  PHE   A CZ  
275  N N   . SER   A 42  ? 0.3226 0.7174 0.3615 0.1100  0.0132  0.0113  85  SER   A N   
276  C CA  . SER   A 42  ? 0.3030 0.7525 0.4059 0.1071  0.0097  -0.0097 85  SER   A CA  
277  C C   . SER   A 42  ? 0.3116 0.7782 0.4302 0.1238  0.0183  -0.0048 85  SER   A C   
278  O O   . SER   A 42  ? 0.3325 0.7722 0.4136 0.1437  0.0123  0.0106  85  SER   A O   
279  C CB  . SER   A 42  ? 0.3058 0.7865 0.4214 0.1209  -0.0271 -0.0272 85  SER   A CB  
280  O OG  . SER   A 42  ? 0.3529 0.8122 0.4334 0.1174  -0.0426 -0.0294 85  SER   A OG  
281  N N   . LEU   A 43  ? 0.2909 0.8034 0.4679 0.1159  0.0325  -0.0196 86  LEU   A N   
282  C CA  . LEU   A 43  ? 0.2958 0.8321 0.4915 0.1348  0.0393  -0.0201 86  LEU   A CA  
283  C C   . LEU   A 43  ? 0.2960 0.8787 0.5291 0.1565  0.0072  -0.0391 86  LEU   A C   
284  O O   . LEU   A 43  ? 0.2686 0.8935 0.5482 0.1469  -0.0049 -0.0607 86  LEU   A O   
285  C CB  . LEU   A 43  ? 0.2742 0.8373 0.5091 0.1167  0.0764  -0.0242 86  LEU   A CB  
286  C CG  . LEU   A 43  ? 0.3144 0.8489 0.5126 0.1248  0.1020  -0.0067 86  LEU   A CG  
287  C CD1 . LEU   A 43  ? 0.3139 0.8540 0.5268 0.1008  0.1428  -0.0017 86  LEU   A CD1 
288  C CD2 . LEU   A 43  ? 0.3126 0.8720 0.5227 0.1552  0.0931  -0.0137 86  LEU   A CD2 
289  N N   . VAL   A 44  ? 0.3226 0.8949 0.5354 0.1871  -0.0093 -0.0321 87  VAL   A N   
290  C CA  . VAL   A 44  ? 0.3202 0.9275 0.5592 0.2148  -0.0427 -0.0465 87  VAL   A CA  
291  C C   . VAL   A 44  ? 0.3022 0.9614 0.5978 0.2264  -0.0325 -0.0639 87  VAL   A C   
292  O O   . VAL   A 44  ? 0.3134 0.9582 0.5981 0.2311  -0.0100 -0.0557 87  VAL   A O   
293  C CB  . VAL   A 44  ? 0.3635 0.9216 0.5456 0.2423  -0.0676 -0.0263 87  VAL   A CB  
294  C CG1 . VAL   A 44  ? 0.3551 0.9423 0.5568 0.2745  -0.1044 -0.0379 87  VAL   A CG1 
295  C CG2 . VAL   A 44  ? 0.4023 0.9130 0.5278 0.2301  -0.0718 -0.0084 87  VAL   A CG2 
296  N N   . GLU   A 45  ? 0.2711 0.9946 0.6287 0.2321  -0.0489 -0.0907 88  GLU   A N   
297  C CA  . GLU   A 45  ? 0.2501 1.0338 0.6698 0.2442  -0.0396 -0.1114 88  GLU   A CA  
298  C C   . GLU   A 45  ? 0.2294 1.0643 0.6922 0.2733  -0.0798 -0.1359 88  GLU   A C   
299  O O   . GLU   A 45  ? 0.1993 1.0872 0.7148 0.2913  -0.0793 -0.1558 88  GLU   A O   
300  C CB  . GLU   A 45  ? 0.2566 1.0843 0.7312 0.2090  0.0002  -0.1234 88  GLU   A CB  
301  C CG  . GLU   A 45  ? 0.3542 1.1487 0.7969 0.1948  0.0438  -0.1030 88  GLU   A CG  
302  C CD  . GLU   A 45  ? 0.4120 1.2565 0.8975 0.2030  0.0719  -0.1147 88  GLU   A CD  
303  O OE1 . GLU   A 45  ? 0.3897 1.2929 0.9295 0.2248  0.0553  -0.1390 88  GLU   A OE1 
304  O OE2 . GLU   A 45  ? 0.4602 1.2864 0.9229 0.1898  0.1107  -0.1001 88  GLU   A OE2 
305  N N   . GLY   B 7   ? 0.8801 0.9038 0.5014 0.3854  0.0321  -0.0898 16  GLY   B N   
306  C CA  . GLY   B 7   ? 0.8981 0.9077 0.5031 0.4103  0.0227  -0.0938 16  GLY   B CA  
307  C C   . GLY   B 7   ? 0.8946 0.9130 0.5150 0.3994  0.0202  -0.0889 16  GLY   B C   
308  O O   . GLY   B 7   ? 0.8744 0.9434 0.5252 0.3895  0.0194  -0.0952 16  GLY   B O   
309  N N   . GLU   B 8   ? 0.9076 0.8764 0.5057 0.4011  0.0185  -0.0775 17  GLU   B N   
310  C CA  . GLU   B 8   ? 0.8988 0.8691 0.5054 0.3942  0.0156  -0.0721 17  GLU   B CA  
311  C C   . GLU   B 8   ? 0.8667 0.8530 0.4986 0.3610  0.0217  -0.0642 17  GLU   B C   
312  O O   . GLU   B 8   ? 0.8790 0.8369 0.5048 0.3437  0.0287  -0.0523 17  GLU   B O   
313  C CB  . GLU   B 8   ? 0.9649 0.8785 0.5388 0.4041  0.0144  -0.0604 17  GLU   B CB  
314  C CG  . GLU   B 8   ? 1.0359 0.9495 0.6148 0.4005  0.0113  -0.0549 17  GLU   B CG  
315  C CD  . GLU   B 8   ? 1.1547 1.0169 0.7027 0.4077  0.0126  -0.0414 17  GLU   B CD  
316  O OE1 . GLU   B 8   ? 1.1894 1.0117 0.7134 0.4082  0.0172  -0.0331 17  GLU   B OE1 
317  O OE2 . GLU   B 8   ? 1.1938 1.0554 0.7403 0.4127  0.0086  -0.0388 17  GLU   B OE2 
318  N N   . THR   B 9   ? 0.8221 0.8532 0.4809 0.3521  0.0179  -0.0714 18  THR   B N   
319  C CA  . THR   B 9   ? 0.7963 0.8400 0.4748 0.3217  0.0213  -0.0651 18  THR   B CA  
320  C C   . THR   B 9   ? 0.7652 0.8130 0.4497 0.3180  0.0130  -0.0640 18  THR   B C   
321  O O   . THR   B 9   ? 0.7622 0.8225 0.4613 0.2945  0.0128  -0.0612 18  THR   B O   
322  C CB  . THR   B 9   ? 0.7951 0.8859 0.4987 0.3066  0.0252  -0.0730 18  THR   B CB  
323  O OG1 . THR   B 9   ? 0.7926 0.9293 0.5113 0.3213  0.0183  -0.0874 18  THR   B OG1 
324  C CG2 . THR   B 9   ? 0.8063 0.8880 0.5022 0.3063  0.0341  -0.0719 18  THR   B CG2 
325  N N   . THR   B 10  ? 0.7408 0.7746 0.4104 0.3417  0.0053  -0.0663 19  THR   B N   
326  C CA  . THR   B 10  ? 0.7156 0.7495 0.3862 0.3435  -0.0043 -0.0663 19  THR   B CA  
327  C C   . THR   B 10  ? 0.6948 0.6995 0.3584 0.3251  -0.0011 -0.0523 19  THR   B C   
328  O O   . THR   B 10  ? 0.7133 0.6847 0.3608 0.3233  0.0074  -0.0409 19  THR   B O   
329  C CB  . THR   B 10  ? 0.7443 0.7617 0.3938 0.3762  -0.0118 -0.0706 19  THR   B CB  
330  O OG1 . THR   B 10  ? 0.7377 0.7970 0.4017 0.3910  -0.0199 -0.0874 19  THR   B OG1 
331  C CG2 . THR   B 10  ? 0.7596 0.7548 0.3962 0.3823  -0.0190 -0.0650 19  THR   B CG2 
332  N N   . ASP   B 11  ? 0.6551 0.6732 0.3300 0.3113  -0.0086 -0.0536 20  ASP   B N   
333  C CA  . ASP   B 11  ? 0.6415 0.6341 0.3074 0.2973  -0.0084 -0.0426 20  ASP   B CA  
334  C C   . ASP   B 11  ? 0.6284 0.5824 0.2676 0.3160  -0.0067 -0.0325 20  ASP   B C   
335  O O   . ASP   B 11  ? 0.6313 0.5794 0.2590 0.3397  -0.0110 -0.0360 20  ASP   B O   
336  C CB  . ASP   B 11  ? 0.6572 0.6662 0.3329 0.2873  -0.0217 -0.0484 20  ASP   B CB  
337  C CG  . ASP   B 11  ? 0.7188 0.7367 0.4063 0.2565  -0.0207 -0.0464 20  ASP   B CG  
338  O OD1 . ASP   B 11  ? 0.7101 0.7510 0.4135 0.2424  -0.0130 -0.0492 20  ASP   B OD1 
339  O OD2 . ASP   B 11  ? 0.7613 0.7611 0.4390 0.2478  -0.0281 -0.0422 20  ASP   B OD2 
340  N N   . GLY   B 12  ? 0.6095 0.5394 0.2386 0.3058  -0.0004 -0.0203 21  GLY   B N   
341  C CA  . GLY   B 12  ? 0.6053 0.5044 0.2110 0.3206  0.0029  -0.0093 21  GLY   B CA  
342  C C   . GLY   B 12  ? 0.5900 0.4697 0.1890 0.3097  0.0153  0.0036  21  GLY   B C   
343  O O   . GLY   B 12  ? 0.5816 0.4686 0.1928 0.2901  0.0202  0.0040  21  GLY   B O   
344  N N   . VAL   B 13  ? 0.5874 0.4436 0.1666 0.3216  0.0205  0.0145  22  VAL   B N   
345  C CA  . VAL   B 13  ? 0.5856 0.4264 0.1595 0.3109  0.0322  0.0273  22  VAL   B CA  
346  C C   . VAL   B 13  ? 0.5953 0.4198 0.1602 0.3158  0.0393  0.0305  22  VAL   B C   
347  O O   . VAL   B 13  ? 0.6076 0.4229 0.1592 0.3347  0.0361  0.0274  22  VAL   B O   
348  C CB  . VAL   B 13  ? 0.5956 0.4253 0.1549 0.3167  0.0345  0.0387  22  VAL   B CB  
349  C CG1 . VAL   B 13  ? 0.6166 0.4297 0.1538 0.3395  0.0351  0.0438  22  VAL   B CG1 
350  C CG2 . VAL   B 13  ? 0.5942 0.4194 0.1556 0.3008  0.0452  0.0498  22  VAL   B CG2 
351  N N   . TYR   B 14  ? 0.5893 0.4086 0.1598 0.2993  0.0472  0.0352  23  TYR   B N   
352  C CA  . TYR   B 14  ? 0.5963 0.3960 0.1564 0.3013  0.0519  0.0373  23  TYR   B CA  
353  C C   . TYR   B 14  ? 0.6199 0.3995 0.1723 0.2883  0.0613  0.0518  23  TYR   B C   
354  O O   . TYR   B 14  ? 0.6228 0.4122 0.1861 0.2734  0.0649  0.0570  23  TYR   B O   
355  C CB  . TYR   B 14  ? 0.5712 0.3854 0.1464 0.2933  0.0503  0.0261  23  TYR   B CB  
356  C CG  . TYR   B 14  ? 0.5516 0.3857 0.1322 0.3082  0.0421  0.0116  23  TYR   B CG  
357  C CD1 . TYR   B 14  ? 0.5406 0.4008 0.1353 0.3085  0.0350  0.0044  23  TYR   B CD1 
358  C CD2 . TYR   B 14  ? 0.5603 0.3881 0.1319 0.3217  0.0403  0.0044  23  TYR   B CD2 
359  C CE1 . TYR   B 14  ? 0.5387 0.4221 0.1411 0.3210  0.0270  -0.0091 23  TYR   B CE1 
360  C CE2 . TYR   B 14  ? 0.5597 0.4117 0.1377 0.3373  0.0325  -0.0098 23  TYR   B CE2 
361  C CZ  . TYR   B 14  ? 0.5532 0.4356 0.1488 0.3359  0.0262  -0.0165 23  TYR   B CZ  
362  O OH  . TYR   B 14  ? 0.5610 0.4723 0.1660 0.3498  0.0180  -0.0309 23  TYR   B OH  
363  N N   . ARG   B 15  ? 0.6344 0.3859 0.1674 0.2932  0.0644  0.0575  24  ARG   B N   
364  C CA  . ARG   B 15  ? 0.6482 0.3799 0.1739 0.2779  0.0726  0.0713  24  ARG   B CA  
365  C C   . ARG   B 15  ? 0.6560 0.3814 0.1879 0.2656  0.0719  0.0661  24  ARG   B C   
366  O O   . ARG   B 15  ? 0.6632 0.3821 0.1886 0.2767  0.0666  0.0559  24  ARG   B O   
367  C CB  . ARG   B 15  ? 0.6819 0.3789 0.1775 0.2878  0.0753  0.0816  24  ARG   B CB  
368  C CG  . ARG   B 15  ? 0.7094 0.4049 0.1903 0.3050  0.0760  0.0873  24  ARG   B CG  
369  C CD  . ARG   B 15  ? 0.7727 0.4288 0.2211 0.3096  0.0804  0.0996  24  ARG   B CD  
370  N NE  . ARG   B 15  ? 0.8068 0.4549 0.2343 0.3310  0.0799  0.1032  24  ARG   B NE  
371  C CZ  . ARG   B 15  ? 0.8255 0.4799 0.2482 0.3305  0.0876  0.1162  24  ARG   B CZ  
372  N NH1 . ARG   B 15  ? 0.8117 0.4832 0.2505 0.3093  0.0963  0.1267  24  ARG   B NH1 
373  N NH2 . ARG   B 15  ? 0.8232 0.4684 0.2241 0.3526  0.0863  0.1184  24  ARG   B NH2 
374  N N   . VAL   B 16  ? 0.6537 0.3808 0.1961 0.2448  0.0769  0.0729  25  VAL   B N   
375  C CA  . VAL   B 16  ? 0.6615 0.3790 0.2075 0.2321  0.0761  0.0693  25  VAL   B CA  
376  C C   . VAL   B 16  ? 0.6886 0.3702 0.2146 0.2238  0.0790  0.0814  25  VAL   B C   
377  O O   . VAL   B 16  ? 0.6892 0.3716 0.2176 0.2106  0.0851  0.0943  25  VAL   B O   
378  C CB  . VAL   B 16  ? 0.6518 0.3940 0.2215 0.2148  0.0777  0.0673  25  VAL   B CB  
379  C CG1 . VAL   B 16  ? 0.6583 0.3902 0.2303 0.2037  0.0762  0.0627  25  VAL   B CG1 
380  C CG2 . VAL   B 16  ? 0.6440 0.4160 0.2285 0.2209  0.0743  0.0574  25  VAL   B CG2 
381  N N   . MET   B 17  ? 0.7096 0.3599 0.2139 0.2324  0.0740  0.0775  26  MET   B N   
382  C CA  . MET   B 17  ? 0.7470 0.3542 0.2252 0.2252  0.0743  0.0885  26  MET   B CA  
383  C C   . MET   B 17  ? 0.7831 0.3683 0.2565 0.2138  0.0695  0.0847  26  MET   B C   
384  O O   . MET   B 17  ? 0.7722 0.3759 0.2605 0.2156  0.0663  0.0724  26  MET   B O   
385  C CB  . MET   B 17  ? 0.7687 0.3451 0.2143 0.2483  0.0699  0.0872  26  MET   B CB  
386  C CG  . MET   B 17  ? 0.7725 0.3671 0.2187 0.2648  0.0721  0.0879  26  MET   B CG  
387  S SD  . MET   B 17  ? 0.7755 0.3682 0.2174 0.2520  0.0829  0.1091  26  MET   B SD  
388  C CE  . MET   B 17  ? 0.7751 0.3064 0.1748 0.2468  0.0824  0.1216  26  MET   B CE  
389  N N   . THR   B 18  ? 0.8274 0.3705 0.2772 0.2021  0.0683  0.0954  27  THR   B N   
390  C CA  . THR   B 18  ? 0.8702 0.3815 0.3074 0.1925  0.0612  0.0926  27  THR   B CA  
391  C C   . THR   B 18  ? 0.9387 0.3897 0.3343 0.1903  0.0561  0.1022  27  THR   B C   
392  O O   . THR   B 18  ? 0.9411 0.3782 0.3234 0.1855  0.0614  0.1161  27  THR   B O   
393  C CB  . THR   B 18  ? 0.8663 0.3977 0.3305 0.1668  0.0639  0.0957  27  THR   B CB  
394  O OG1 . THR   B 18  ? 0.9004 0.3972 0.3490 0.1603  0.0551  0.0915  27  THR   B OG1 
395  C CG2 . THR   B 18  ? 0.8579 0.3977 0.3319 0.1447  0.0721  0.1130  27  THR   B CG2 
396  N N   . ARG   B 19  ? 0.9908 0.4035 0.3633 0.1932  0.0456  0.0952  28  ARG   B N   
397  C CA  . ARG   B 19  ? 1.0590 0.4059 0.3866 0.1897  0.0379  0.1036  28  ARG   B CA  
398  C C   . ARG   B 19  ? 1.0887 0.4074 0.4128 0.1619  0.0322  0.1091  28  ARG   B C   
399  O O   . ARG   B 19  ? 1.1191 0.3771 0.4033 0.1570  0.0228  0.1144  28  ARG   B O   
400  C CB  . ARG   B 19  ? 1.1104 0.4229 0.4001 0.2227  0.0268  0.0903  28  ARG   B CB  
401  C CG  . ARG   B 19  ? 1.1554 0.4899 0.4443 0.2495  0.0304  0.0855  28  ARG   B CG  
402  C CD  . ARG   B 19  ? 1.2473 0.5299 0.4854 0.2778  0.0190  0.0792  28  ARG   B CD  
403  N NE  . ARG   B 19  ? 1.2898 0.5850 0.5216 0.3010  0.0219  0.0777  28  ARG   B NE  
404  C CZ  . ARG   B 19  ? 1.3116 0.6328 0.5466 0.3322  0.0172  0.0603  28  ARG   B CZ  
405  N NH1 . ARG   B 19  ? 1.2999 0.6398 0.5446 0.3442  0.0110  0.0436  28  ARG   B NH1 
406  N NH2 . ARG   B 19  ? 1.3033 0.6343 0.5322 0.3519  0.0187  0.0594  28  ARG   B NH2 
407  N N   . ARG   B 20  ? 1.0777 0.4386 0.4417 0.1437  0.0368  0.1078  29  ARG   B N   
408  C CA  . ARG   B 20  ? 1.1010 0.4484 0.4711 0.1174  0.0315  0.1110  29  ARG   B CA  
409  C C   . ARG   B 20  ? 1.1198 0.4467 0.4842 0.0859  0.0347  0.1314  29  ARG   B C   
410  O O   . ARG   B 20  ? 1.1372 0.4320 0.4915 0.0641  0.0264  0.1357  29  ARG   B O   
411  C CB  . ARG   B 20  ? 1.0942 0.4992 0.5094 0.1111  0.0370  0.1035  29  ARG   B CB  
412  C CG  . ARG   B 20  ? 1.1556 0.5516 0.5784 0.0914  0.0295  0.1009  29  ARG   B CG  
413  C CD  . ARG   B 20  ? 1.1811 0.6346 0.6472 0.0824  0.0368  0.0974  29  ARG   B CD  
414  N NE  . ARG   B 20  ? 1.2177 0.7015 0.7074 0.0617  0.0465  0.1117  29  ARG   B NE  
415  C CZ  . ARG   B 20  ? 1.2446 0.7462 0.7563 0.0375  0.0465  0.1164  29  ARG   B CZ  
416  N NH1 . ARG   B 20  ? 1.2486 0.7376 0.7613 0.0304  0.0367  0.1080  29  ARG   B NH1 
417  N NH2 . ARG   B 20  ? 1.2300 0.7646 0.7627 0.0220  0.0560  0.1290  29  ARG   B NH2 
418  N N   . LEU   B 21  ? 1.1106 0.4572 0.4811 0.0835  0.0466  0.1439  30  LEU   B N   
419  C CA  . LEU   B 21  ? 1.1208 0.4576 0.4882 0.0544  0.0527  0.1645  30  LEU   B CA  
420  C C   . LEU   B 21  ? 1.1503 0.4351 0.4712 0.0625  0.0523  0.1750  30  LEU   B C   
421  O O   . LEU   B 21  ? 1.1775 0.4194 0.4628 0.0867  0.0420  0.1651  30  LEU   B O   
422  C CB  . LEU   B 21  ? 1.0920 0.4978 0.5039 0.0442  0.0678  0.1715  30  LEU   B CB  
423  C CG  . LEU   B 21  ? 1.0917 0.5396 0.5435 0.0267  0.0678  0.1669  30  LEU   B CG  
424  C CD1 . LEU   B 21  ? 1.0805 0.5660 0.5554 0.0491  0.0675  0.1490  30  LEU   B CD1 
425  C CD2 . LEU   B 21  ? 1.0793 0.5727 0.5597 0.0048  0.0802  0.1817  30  LEU   B CD2 
426  N N   . LEU   B 22  ? 1.1437 0.4315 0.4624 0.0436  0.0630  0.1948  31  LEU   B N   
427  C CA  . LEU   B 22  ? 1.1804 0.4159 0.4520 0.0491  0.0633  0.2065  31  LEU   B CA  
428  C C   . LEU   B 22  ? 1.1865 0.4313 0.4475 0.0871  0.0666  0.1982  31  LEU   B C   
429  O O   . LEU   B 22  ? 1.1679 0.4638 0.4556 0.0930  0.0794  0.2017  31  LEU   B O   
430  C CB  . LEU   B 22  ? 1.1735 0.4187 0.4496 0.0175  0.0761  0.2306  31  LEU   B CB  
431  C CG  . LEU   B 22  ? 1.2225 0.4000 0.4438 0.0119  0.0747  0.2462  31  LEU   B CG  
432  C CD1 . LEU   B 22  ? 1.2525 0.3699 0.4464 -0.0186 0.0620  0.2535  31  LEU   B CD1 
433  C CD2 . LEU   B 22  ? 1.2184 0.4258 0.4470 -0.0004 0.0932  0.2667  31  LEU   B CD2 
434  N N   . GLY   B 23  ? 1.2083 0.4032 0.4288 0.1135  0.0540  0.1869  32  GLY   B N   
435  C CA  . GLY   B 23  ? 1.2051 0.4070 0.4142 0.1515  0.0540  0.1760  32  GLY   B CA  
436  C C   . GLY   B 23  ? 1.1537 0.4258 0.4111 0.1671  0.0583  0.1603  32  GLY   B C   
437  O O   . GLY   B 23  ? 1.1384 0.4348 0.4239 0.1589  0.0551  0.1508  32  GLY   B O   
438  N N   . SER   B 24  ? 1.1248 0.4281 0.3906 0.1884  0.0651  0.1580  33  SER   B N   
439  C CA  . SER   B 24  ? 1.0750 0.4424 0.3841 0.2010  0.0688  0.1447  33  SER   B CA  
440  C C   . SER   B 24  ? 1.0269 0.4420 0.3717 0.1800  0.0823  0.1572  33  SER   B C   
441  O O   . SER   B 24  ? 1.0350 0.4434 0.3678 0.1722  0.0909  0.1738  33  SER   B O   
442  C CB  . SER   B 24  ? 1.0948 0.4691 0.3926 0.2357  0.0665  0.1344  33  SER   B CB  
443  O OG  . SER   B 24  ? 1.1528 0.4812 0.4118 0.2581  0.0540  0.1239  33  SER   B OG  
444  N N   . THR   B 25  ? 0.9757 0.4381 0.3615 0.1718  0.0840  0.1493  34  THR   B N   
445  C CA  . THR   B 25  ? 0.9365 0.4465 0.3560 0.1548  0.0949  0.1585  34  THR   B CA  
446  C C   . THR   B 25  ? 0.8907 0.4516 0.3425 0.1686  0.0955  0.1450  34  THR   B C   
447  O O   . THR   B 25  ? 0.8807 0.4496 0.3452 0.1719  0.0888  0.1307  34  THR   B O   
448  C CB  . THR   B 25  ? 0.9464 0.4569 0.3807 0.1232  0.0950  0.1650  34  THR   B CB  
449  O OG1 . THR   B 25  ? 0.9830 0.4432 0.3858 0.1068  0.0933  0.1784  34  THR   B OG1 
450  C CG2 . THR   B 25  ? 0.9225 0.4862 0.3924 0.1075  0.1052  0.1726  34  THR   B CG2 
451  N N   . GLN   B 26  ? 0.8596 0.4530 0.3226 0.1765  0.1030  0.1497  35  GLN   B N   
452  C CA  . GLN   B 26  ? 0.8249 0.4613 0.3145 0.1881  0.1019  0.1376  35  GLN   B CA  
453  C C   . GLN   B 26  ? 0.7953 0.4657 0.3160 0.1689  0.1045  0.1373  35  GLN   B C   
454  O O   . GLN   B 26  ? 0.7972 0.4867 0.3270 0.1565  0.1123  0.1495  35  GLN   B O   
455  C CB  . GLN   B 26  ? 0.8226 0.4767 0.3084 0.2060  0.1064  0.1412  35  GLN   B CB  
456  C CG  . GLN   B 26  ? 0.8255 0.5162 0.3334 0.2180  0.1026  0.1282  35  GLN   B CG  
457  C CD  . GLN   B 26  ? 0.8754 0.5765 0.3746 0.2385  0.1038  0.1299  35  GLN   B CD  
458  O OE1 . GLN   B 26  ? 0.9137 0.5925 0.3901 0.2560  0.1013  0.1291  35  GLN   B OE1 
459  N NE2 . GLN   B 26  ? 0.8682 0.6017 0.3829 0.2388  0.1065  0.1313  35  GLN   B NE2 
460  N N   . VAL   B 27  ? 0.7618 0.4414 0.2977 0.1677  0.0981  0.1235  36  VAL   B N   
461  C CA  . VAL   B 27  ? 0.7270 0.4350 0.2888 0.1520  0.0990  0.1217  36  VAL   B CA  
462  C C   . VAL   B 27  ? 0.6844 0.4304 0.2634 0.1617  0.0998  0.1159  36  VAL   B C   
463  O O   . VAL   B 27  ? 0.6716 0.4433 0.2673 0.1520  0.1021  0.1181  36  VAL   B O   
464  C CB  . VAL   B 27  ? 0.7442 0.4390 0.3098 0.1438  0.0920  0.1113  36  VAL   B CB  
465  C CG1 . VAL   B 27  ? 0.7723 0.4318 0.3233 0.1279  0.0903  0.1190  36  VAL   B CG1 
466  C CG2 . VAL   B 27  ? 0.7546 0.4425 0.3133 0.1623  0.0859  0.0969  36  VAL   B CG2 
467  N N   . GLY   B 28  ? 0.6598 0.4075 0.2329 0.1811  0.0964  0.1079  37  GLY   B N   
468  C CA  . GLY   B 28  ? 0.6256 0.4017 0.2101 0.1903  0.0945  0.1017  37  GLY   B CA  
469  C C   . GLY   B 28  ? 0.6052 0.3792 0.1809 0.2108  0.0896  0.0937  37  GLY   B C   
470  O O   . GLY   B 28  ? 0.6169 0.3693 0.1761 0.2209  0.0888  0.0942  37  GLY   B O   
471  N N   . VAL   B 29  ? 0.5738 0.3691 0.1585 0.2172  0.0853  0.0863  38  VAL   B N   
472  C CA  . VAL   B 29  ? 0.5616 0.3617 0.1422 0.2344  0.0787  0.0775  38  VAL   B CA  
473  C C   . VAL   B 29  ? 0.5402 0.3563 0.1354 0.2288  0.0722  0.0648  38  VAL   B C   
474  O O   . VAL   B 29  ? 0.5309 0.3551 0.1359 0.2153  0.0729  0.0644  38  VAL   B O   
475  C CB  . VAL   B 29  ? 0.5662 0.3739 0.1381 0.2476  0.0792  0.0841  38  VAL   B CB  
476  C CG1 . VAL   B 29  ? 0.5715 0.3849 0.1402 0.2639  0.0700  0.0741  38  VAL   B CG1 
477  C CG2 . VAL   B 29  ? 0.5762 0.3684 0.1313 0.2531  0.0869  0.0974  38  VAL   B CG2 
478  N N   . GLY   B 30  ? 0.5306 0.3515 0.1265 0.2386  0.0659  0.0546  39  GLY   B N   
479  C CA  . GLY   B 30  ? 0.5214 0.3589 0.1301 0.2318  0.0601  0.0437  39  GLY   B CA  
480  C C   . GLY   B 30  ? 0.5229 0.3710 0.1311 0.2441  0.0517  0.0358  39  GLY   B C   
481  O O   . GLY   B 30  ? 0.5307 0.3726 0.1286 0.2607  0.0500  0.0369  39  GLY   B O   
482  N N   . VAL   B 31  ? 0.5156 0.3786 0.1338 0.2353  0.0458  0.0279  40  VAL   B N   
483  C CA  . VAL   B 31  ? 0.5163 0.3915 0.1365 0.2425  0.0360  0.0195  40  VAL   B CA  
484  C C   . VAL   B 31  ? 0.5123 0.4078 0.1477 0.2353  0.0340  0.0085  40  VAL   B C   
485  O O   . VAL   B 31  ? 0.5110 0.4134 0.1550 0.2181  0.0365  0.0066  40  VAL   B O   
486  C CB  . VAL   B 31  ? 0.5209 0.3953 0.1368 0.2362  0.0288  0.0202  40  VAL   B CB  
487  C CG1 . VAL   B 31  ? 0.5211 0.4060 0.1391 0.2395  0.0167  0.0112  40  VAL   B CG1 
488  C CG2 . VAL   B 31  ? 0.5335 0.3941 0.1345 0.2463  0.0307  0.0303  40  VAL   B CG2 
489  N N   . MET   B 32  ? 0.5055 0.4124 0.1436 0.2492  0.0298  0.0010  41  MET   B N   
490  C CA  . MET   B 32  ? 0.4993 0.4338 0.1538 0.2442  0.0278  -0.0102 41  MET   B CA  
491  C C   . MET   B 32  ? 0.4970 0.4483 0.1591 0.2372  0.0172  -0.0161 41  MET   B C   
492  O O   . MET   B 32  ? 0.5093 0.4537 0.1630 0.2499  0.0092  -0.0160 41  MET   B O   
493  C CB  . MET   B 32  ? 0.5083 0.4486 0.1606 0.2651  0.0273  -0.0166 41  MET   B CB  
494  C CG  . MET   B 32  ? 0.5262 0.5016 0.1961 0.2635  0.0261  -0.0289 41  MET   B CG  
495  S SD  . MET   B 32  ? 0.6269 0.6054 0.3015 0.2518  0.0369  -0.0290 41  MET   B SD  
496  C CE  . MET   B 32  ? 0.6318 0.5732 0.2824 0.2725  0.0404  -0.0237 41  MET   B CE  
497  N N   . GLN   B 33  ? 0.4851 0.4548 0.1604 0.2165  0.0166  -0.0202 42  GLN   B N   
498  C CA  . GLN   B 33  ? 0.4841 0.4670 0.1652 0.2058  0.0054  -0.0253 42  GLN   B CA  
499  C C   . GLN   B 33  ? 0.4620 0.4748 0.1613 0.1848  0.0077  -0.0312 42  GLN   B C   
500  O O   . GLN   B 33  ? 0.4665 0.4748 0.1657 0.1703  0.0162  -0.0274 42  GLN   B O   
501  C CB  . GLN   B 33  ? 0.5314 0.4865 0.1958 0.1984  -0.0006 -0.0183 42  GLN   B CB  
502  C CG  . GLN   B 33  ? 0.5989 0.5606 0.2642 0.1885  -0.0151 -0.0239 42  GLN   B CG  
503  C CD  . GLN   B 33  ? 0.6944 0.6243 0.3369 0.1884  -0.0245 -0.0186 42  GLN   B CD  
504  O OE1 . GLN   B 33  ? 0.7216 0.6411 0.3571 0.1689  -0.0296 -0.0178 42  GLN   B OE1 
505  N NE2 . GLN   B 33  ? 0.7246 0.6372 0.3521 0.2115  -0.0274 -0.0150 42  GLN   B NE2 
506  N N   . GLU   B 34  ? 0.4371 0.4826 0.1522 0.1834  0.0003  -0.0407 43  GLU   B N   
507  C CA  . GLU   B 34  ? 0.4180 0.5013 0.1535 0.1628  0.0026  -0.0467 43  GLU   B CA  
508  C C   . GLU   B 34  ? 0.3975 0.4997 0.1419 0.1658  0.0165  -0.0485 43  GLU   B C   
509  O O   . GLU   B 34  ? 0.3868 0.5093 0.1411 0.1462  0.0229  -0.0491 43  GLU   B O   
510  C CB  . GLU   B 34  ? 0.4608 0.5316 0.1906 0.1333  -0.0006 -0.0418 43  GLU   B CB  
511  C CG  . GLU   B 34  ? 0.5325 0.5801 0.2487 0.1310  -0.0164 -0.0407 43  GLU   B CG  
512  C CD  . GLU   B 34  ? 0.6432 0.6711 0.3472 0.1031  -0.0219 -0.0362 43  GLU   B CD  
513  O OE1 . GLU   B 34  ? 0.6585 0.7056 0.3726 0.0796  -0.0155 -0.0363 43  GLU   B OE1 
514  O OE2 . GLU   B 34  ? 0.7009 0.6928 0.3825 0.1058  -0.0329 -0.0325 43  GLU   B OE2 
515  N N   . GLY   B 35  ? 0.3921 0.4851 0.1298 0.1908  0.0203  -0.0493 44  GLY   B N   
516  C CA  . GLY   B 35  ? 0.3830 0.4864 0.1232 0.1982  0.0309  -0.0516 44  GLY   B CA  
517  C C   . GLY   B 35  ? 0.3903 0.4626 0.1178 0.1881  0.0400  -0.0423 44  GLY   B C   
518  O O   . GLY   B 35  ? 0.3944 0.4767 0.1245 0.1867  0.0484  -0.0442 44  GLY   B O   
519  N N   . VAL   B 36  ? 0.3910 0.4271 0.1041 0.1818  0.0377  -0.0330 45  VAL   B N   
520  C CA  . VAL   B 36  ? 0.3924 0.3992 0.0937 0.1725  0.0445  -0.0244 45  VAL   B CA  
521  C C   . VAL   B 36  ? 0.3985 0.3706 0.0836 0.1865  0.0438  -0.0165 45  VAL   B C   
522  O O   . VAL   B 36  ? 0.3952 0.3571 0.0740 0.1922  0.0369  -0.0138 45  VAL   B O   
523  C CB  . VAL   B 36  ? 0.3943 0.3963 0.0939 0.1472  0.0437  -0.0208 45  VAL   B CB  
524  C CG1 . VAL   B 36  ? 0.4144 0.3848 0.1000 0.1418  0.0487  -0.0129 45  VAL   B CG1 
525  C CG2 . VAL   B 36  ? 0.3789 0.4143 0.0926 0.1308  0.0477  -0.0265 45  VAL   B CG2 
526  N N   . PHE   B 37  ? 0.3993 0.3540 0.0770 0.1921  0.0507  -0.0127 46  PHE   B N   
527  C CA  . PHE   B 37  ? 0.4117 0.3366 0.0754 0.2016  0.0516  -0.0039 46  PHE   B CA  
528  C C   . PHE   B 37  ? 0.4170 0.3250 0.0756 0.1871  0.0537  0.0038  46  PHE   B C   
529  O O   . PHE   B 37  ? 0.4204 0.3258 0.0804 0.1760  0.0584  0.0040  46  PHE   B O   
530  C CB  . PHE   B 37  ? 0.4141 0.3253 0.0702 0.2127  0.0564  -0.0033 46  PHE   B CB  
531  C CG  . PHE   B 37  ? 0.4324 0.3161 0.0739 0.2225  0.0567  0.0060  46  PHE   B CG  
532  C CD1 . PHE   B 37  ? 0.4358 0.3182 0.0712 0.2380  0.0521  0.0063  46  PHE   B CD1 
533  C CD2 . PHE   B 37  ? 0.4490 0.3096 0.0829 0.2152  0.0616  0.0148  46  PHE   B CD2 
534  C CE1 . PHE   B 37  ? 0.4554 0.3134 0.0756 0.2464  0.0538  0.0160  46  PHE   B CE1 
535  C CE2 . PHE   B 37  ? 0.4647 0.3041 0.0863 0.2214  0.0631  0.0246  46  PHE   B CE2 
536  C CZ  . PHE   B 37  ? 0.4649 0.3026 0.0787 0.2372  0.0599  0.0255  46  PHE   B CZ  
537  N N   . HIS   B 38  ? 0.4120 0.3087 0.0630 0.1892  0.0496  0.0097  47  HIS   B N   
538  C CA  . HIS   B 38  ? 0.4139 0.2971 0.0583 0.1792  0.0500  0.0161  47  HIS   B CA  
539  C C   . HIS   B 38  ? 0.4221 0.2896 0.0588 0.1870  0.0541  0.0252  47  HIS   B C   
540  O O   . HIS   B 38  ? 0.4250 0.2894 0.0556 0.2003  0.0523  0.0285  47  HIS   B O   
541  C CB  . HIS   B 38  ? 0.4188 0.3020 0.0572 0.1785  0.0410  0.0155  47  HIS   B CB  
542  C CG  . HIS   B 38  ? 0.4304 0.3289 0.0756 0.1685  0.0353  0.0074  47  HIS   B CG  
543  N ND1 . HIS   B 38  ? 0.4403 0.3571 0.0947 0.1761  0.0319  0.0010  47  HIS   B ND1 
544  C CD2 . HIS   B 38  ? 0.4419 0.3401 0.0852 0.1508  0.0323  0.0053  47  HIS   B CD2 
545  C CE1 . HIS   B 38  ? 0.4372 0.3680 0.0979 0.1611  0.0272  -0.0046 47  HIS   B CE1 
546  N NE2 . HIS   B 38  ? 0.4431 0.3612 0.0960 0.1449  0.0275  -0.0016 47  HIS   B NE2 
547  N N   . THR   B 39  ? 0.4305 0.2891 0.0668 0.1783  0.0592  0.0297  48  THR   B N   
548  C CA  . THR   B 39  ? 0.4457 0.2934 0.0768 0.1820  0.0634  0.0395  48  THR   B CA  
549  C C   . THR   B 39  ? 0.4508 0.2963 0.0825 0.1703  0.0647  0.0429  48  THR   B C   
550  O O   . THR   B 39  ? 0.4443 0.2921 0.0769 0.1611  0.0617  0.0374  48  THR   B O   
551  C CB  . THR   B 39  ? 0.4673 0.3041 0.0965 0.1867  0.0681  0.0419  48  THR   B CB  
552  O OG1 . THR   B 39  ? 0.4812 0.3086 0.1038 0.1900  0.0720  0.0527  48  THR   B OG1 
553  C CG2 . THR   B 39  ? 0.4751 0.3056 0.1078 0.1759  0.0707  0.0389  48  THR   B CG2 
554  N N   . MET   B 40  ? 0.4569 0.2991 0.0873 0.1703  0.0687  0.0517  49  MET   B N   
555  C CA  . MET   B 40  ? 0.4678 0.3120 0.1006 0.1605  0.0692  0.0537  49  MET   B CA  
556  C C   . MET   B 40  ? 0.4796 0.3151 0.1180 0.1490  0.0724  0.0529  49  MET   B C   
557  O O   . MET   B 40  ? 0.4898 0.3156 0.1275 0.1504  0.0754  0.0555  49  MET   B O   
558  C CB  . MET   B 40  ? 0.4748 0.3274 0.1059 0.1657  0.0716  0.0630  49  MET   B CB  
559  C CG  . MET   B 40  ? 0.4922 0.3503 0.1141 0.1806  0.0680  0.0639  49  MET   B CG  
560  S SD  . MET   B 40  ? 0.5060 0.3797 0.1231 0.1873  0.0675  0.0697  49  MET   B SD  
561  C CE  . MET   B 40  ? 0.3769 0.2482 0.0533 0.1817  0.0545  0.0487  49  MET   B CE  
562  N N   . TRP   B 41  ? 0.4779 0.3131 0.1181 0.1392  0.0704  0.0489  50  TRP   B N   
563  C CA  A TRP   B 41  ? 0.4905 0.3159 0.1339 0.1294  0.0717  0.0469  50  TRP   B CA  
564  C CA  B TRP   B 41  ? 0.4885 0.3138 0.1318 0.1295  0.0717  0.0468  50  TRP   B CA  
565  C C   . TRP   B 41  ? 0.5016 0.3208 0.1481 0.1251  0.0747  0.0550  50  TRP   B C   
566  O O   . TRP   B 41  ? 0.5164 0.3203 0.1609 0.1217  0.0751  0.0541  50  TRP   B O   
567  C CB  A TRP   B 41  ? 0.4882 0.3139 0.1304 0.1214  0.0683  0.0419  50  TRP   B CB  
568  C CB  B TRP   B 41  ? 0.4836 0.3087 0.1256 0.1214  0.0683  0.0413  50  TRP   B CB  
569  C CG  A TRP   B 41  ? 0.4956 0.3096 0.1386 0.1129  0.0683  0.0382  50  TRP   B CG  
570  C CG  B TRP   B 41  ? 0.4871 0.3005 0.1300 0.1130  0.0684  0.0378  50  TRP   B CG  
571  C CD1 A TRP   B 41  ? 0.5082 0.3154 0.1470 0.1110  0.0682  0.0308  50  TRP   B CD1 
572  C CD1 B TRP   B 41  ? 0.4959 0.3041 0.1429 0.1059  0.0678  0.0410  50  TRP   B CD1 
573  C CD2 A TRP   B 41  ? 0.4970 0.3059 0.1445 0.1052  0.0676  0.0414  50  TRP   B CD2 
574  C CD2 B TRP   B 41  ? 0.4892 0.2957 0.1276 0.1109  0.0682  0.0300  50  TRP   B CD2 
575  N NE1 A TRP   B 41  ? 0.5147 0.3097 0.1526 0.1051  0.0671  0.0289  50  TRP   B NE1 
576  N NE1 B TRP   B 41  ? 0.5014 0.2957 0.1448 0.1009  0.0662  0.0352  50  TRP   B NE1 
577  C CE2 A TRP   B 41  ? 0.5098 0.3045 0.1534 0.1005  0.0659  0.0351  50  TRP   B CE2 
578  C CE2 B TRP   B 41  ? 0.5011 0.2949 0.1387 0.1049  0.0671  0.0285  50  TRP   B CE2 
579  C CE3 A TRP   B 41  ? 0.4996 0.3166 0.1545 0.1013  0.0682  0.0492  50  TRP   B CE3 
580  C CE3 B TRP   B 41  ? 0.4953 0.3069 0.1304 0.1130  0.0691  0.0242  50  TRP   B CE3 
581  C CZ2 A TRP   B 41  ? 0.5225 0.3066 0.1678 0.0924  0.0631  0.0357  50  TRP   B CZ2 
582  C CZ2 B TRP   B 41  ? 0.5140 0.2990 0.1454 0.1038  0.0671  0.0214  50  TRP   B CZ2 
583  C CZ3 A TRP   B 41  ? 0.5106 0.3208 0.1701 0.0908  0.0662  0.0502  50  TRP   B CZ3 
584  C CZ3 B TRP   B 41  ? 0.5074 0.3147 0.1388 0.1100  0.0704  0.0179  50  TRP   B CZ3 
585  C CH2 A TRP   B 41  ? 0.5192 0.3113 0.1733 0.0865  0.0628  0.0432  50  TRP   B CH2 
586  C CH2 B TRP   B 41  ? 0.5128 0.3063 0.1413 0.1068  0.0696  0.0164  50  TRP   B CH2 
587  N N   . HIS   B 42  ? 0.4946 0.3257 0.1449 0.1246  0.0764  0.0629  51  HIS   B N   
588  C CA  . HIS   B 42  ? 0.5017 0.3297 0.1563 0.1160  0.0798  0.0720  51  HIS   B CA  
589  C C   . HIS   B 42  ? 0.5325 0.3433 0.1793 0.1195  0.0831  0.0779  51  HIS   B C   
590  O O   . HIS   B 42  ? 0.5464 0.3464 0.1924 0.1098  0.0850  0.0856  51  HIS   B O   
591  C CB  . HIS   B 42  ? 0.4893 0.3413 0.1512 0.1150  0.0820  0.0793  51  HIS   B CB  
592  C CG  . HIS   B 42  ? 0.4976 0.3603 0.1549 0.1273  0.0861  0.0863  51  HIS   B CG  
593  N ND1 . HIS   B 42  ? 0.5126 0.3880 0.1650 0.1405  0.0833  0.0827  51  HIS   B ND1 
594  C CD2 . HIS   B 42  ? 0.5061 0.3657 0.1599 0.1285  0.0922  0.0969  51  HIS   B CD2 
595  C CE1 . HIS   B 42  ? 0.5112 0.3921 0.1584 0.1506  0.0876  0.0904  51  HIS   B CE1 
596  N NE2 . HIS   B 42  ? 0.5094 0.3816 0.1572 0.1439  0.0936  0.0993  51  HIS   B NE2 
597  N N   . VAL   B 43  ? 0.5409 0.3476 0.1800 0.1328  0.0829  0.0744  52  VAL   B N   
598  C CA  . VAL   B 43  ? 0.5536 0.3421 0.1813 0.1398  0.0847  0.0786  52  VAL   B CA  
599  C C   . VAL   B 43  ? 0.5672 0.3324 0.1879 0.1377  0.0814  0.0723  52  VAL   B C   
600  O O   . VAL   B 43  ? 0.5797 0.3221 0.1911 0.1320  0.0813  0.0780  52  VAL   B O   
601  C CB  . VAL   B 43  ? 0.5649 0.3604 0.1872 0.1569  0.0843  0.0761  52  VAL   B CB  
602  C CG1 . VAL   B 43  ? 0.5861 0.3607 0.1936 0.1666  0.0853  0.0794  52  VAL   B CG1 
603  C CG2 . VAL   B 43  ? 0.5643 0.3801 0.1897 0.1617  0.0862  0.0817  52  VAL   B CG2 
604  N N   . THR   B 44  ? 0.5641 0.3345 0.1875 0.1413  0.0783  0.0608  53  THR   B N   
605  C CA  . THR   B 44  ? 0.5721 0.3254 0.1878 0.1434  0.0751  0.0530  53  THR   B CA  
606  C C   . THR   B 44  ? 0.5774 0.3256 0.1968 0.1311  0.0728  0.0492  53  THR   B C   
607  O O   . THR   B 44  ? 0.5910 0.3213 0.2010 0.1331  0.0696  0.0438  53  THR   B O   
608  C CB  . THR   B 44  ? 0.5732 0.3401 0.1896 0.1563  0.0742  0.0427  53  THR   B CB  
609  O OG1 . THR   B 44  ? 0.5649 0.3518 0.1921 0.1500  0.0742  0.0372  53  THR   B OG1 
610  C CG2 . THR   B 44  ? 0.5776 0.3517 0.1911 0.1697  0.0748  0.0447  53  THR   B CG2 
611  N N   . LYS   B 45  ? 0.5654 0.3285 0.1958 0.1210  0.0732  0.0508  54  LYS   B N   
612  C CA  . LYS   B 45  ? 0.5762 0.3356 0.2094 0.1108  0.0701  0.0463  54  LYS   B CA  
613  C C   . LYS   B 45  ? 0.5814 0.3389 0.2096 0.1157  0.0687  0.0350  54  LYS   B C   
614  O O   . LYS   B 45  ? 0.5787 0.3262 0.2039 0.1100  0.0657  0.0306  54  LYS   B O   
615  C CB  . LYS   B 45  ? 0.6163 0.3547 0.2461 0.1001  0.0671  0.0515  54  LYS   B CB  
616  C CG  . LYS   B 45  ? 0.6731 0.4192 0.3100 0.0917  0.0698  0.0634  54  LYS   B CG  
617  C CD  . LYS   B 45  ? 0.7387 0.4999 0.3885 0.0789  0.0678  0.0644  54  LYS   B CD  
618  C CE  . LYS   B 45  ? 0.7962 0.5722 0.4554 0.0698  0.0714  0.0765  54  LYS   B CE  
619  N NZ  . LYS   B 45  ? 0.8237 0.6181 0.4835 0.0810  0.0778  0.0820  54  LYS   B NZ  
620  N N   . GLY   B 46  ? 0.5796 0.3485 0.2071 0.1262  0.0709  0.0307  55  GLY   B N   
621  C CA  . GLY   B 46  ? 0.5838 0.3594 0.2086 0.1313  0.0715  0.0211  55  GLY   B CA  
622  C C   . GLY   B 46  ? 0.5963 0.3617 0.2112 0.1438  0.0707  0.0164  55  GLY   B C   
623  O O   . GLY   B 46  ? 0.5951 0.3721 0.2088 0.1501  0.0720  0.0082  55  GLY   B O   
624  N N   . ALA   B 47  ? 0.6087 0.3523 0.2143 0.1481  0.0683  0.0216  56  ALA   B N   
625  C CA  . ALA   B 47  ? 0.6280 0.3546 0.2178 0.1626  0.0653  0.0168  56  ALA   B CA  
626  C C   . ALA   B 47  ? 0.6287 0.3759 0.2199 0.1788  0.0670  0.0109  56  ALA   B C   
627  O O   . ALA   B 47  ? 0.6189 0.3859 0.2213 0.1783  0.0696  0.0137  56  ALA   B O   
628  C CB  . ALA   B 47  ? 0.6445 0.3372 0.2198 0.1612  0.0615  0.0250  56  ALA   B CB  
629  N N   . ALA   B 48  ? 0.6384 0.3817 0.2175 0.1945  0.0646  0.0021  57  ALA   B N   
630  C CA  . ALA   B 48  ? 0.6433 0.4093 0.2239 0.2119  0.0650  -0.0051 57  ALA   B CA  
631  C C   . ALA   B 48  ? 0.6757 0.4245 0.2454 0.2224  0.0621  0.0001  57  ALA   B C   
632  O O   . ALA   B 48  ? 0.6995 0.4130 0.2545 0.2183  0.0595  0.0085  57  ALA   B O   
633  C CB  . ALA   B 48  ? 0.6433 0.4110 0.2118 0.2281  0.0628  -0.0164 57  ALA   B CB  
634  N N   . LEU   B 49  ? 0.6739 0.4472 0.2500 0.2351  0.0623  -0.0045 58  LEU   B N   
635  C CA  . LEU   B 49  ? 0.6950 0.4523 0.2586 0.2477  0.0594  -0.0003 58  LEU   B CA  
636  C C   . LEU   B 49  ? 0.7200 0.4817 0.2703 0.2743  0.0543  -0.0116 58  LEU   B C   
637  O O   . LEU   B 49  ? 0.7135 0.5017 0.2705 0.2822  0.0544  -0.0228 58  LEU   B O   
638  C CB  . LEU   B 49  ? 0.6738 0.4526 0.2543 0.2409  0.0623  0.0052  58  LEU   B CB  
639  C CG  . LEU   B 49  ? 0.6759 0.4574 0.2696 0.2186  0.0664  0.0141  58  LEU   B CG  
640  C CD1 . LEU   B 49  ? 0.6722 0.4755 0.2787 0.2166  0.0673  0.0167  58  LEU   B CD1 
641  C CD2 . LEU   B 49  ? 0.6938 0.4417 0.2753 0.2096  0.0670  0.0255  58  LEU   B CD2 
642  N N   . ARG   B 50  ? 0.7501 0.4859 0.2798 0.2890  0.0500  -0.0087 59  ARG   B N   
643  C CA  . ARG   B 50  ? 0.7773 0.5160 0.2916 0.3173  0.0438  -0.0201 59  ARG   B CA  
644  C C   . ARG   B 50  ? 0.7704 0.5245 0.2902 0.3268  0.0428  -0.0196 59  ARG   B C   
645  O O   . ARG   B 50  ? 0.7735 0.5056 0.2869 0.3196  0.0444  -0.0078 59  ARG   B O   
646  C CB  . ARG   B 50  ? 0.8499 0.5342 0.3244 0.3313  0.0366  -0.0193 59  ARG   B CB  
647  C CG  . ARG   B 50  ? 0.9300 0.6090 0.3810 0.3646  0.0284  -0.0303 59  ARG   B CG  
648  C CD  . ARG   B 50  ? 1.0251 0.6449 0.4304 0.3806  0.0191  -0.0309 59  ARG   B CD  
649  N NE  . ARG   B 50  ? 1.1010 0.6669 0.4860 0.3622  0.0193  -0.0140 59  ARG   B NE  
650  C CZ  . ARG   B 50  ? 1.1593 0.6945 0.5236 0.3662  0.0179  -0.0048 59  ARG   B CZ  
651  N NH1 . ARG   B 50  ? 1.1516 0.7017 0.5114 0.3896  0.0151  -0.0117 59  ARG   B NH1 
652  N NH2 . ARG   B 50  ? 1.1891 0.6799 0.5370 0.3462  0.0194  0.0114  59  ARG   B NH2 
653  N N   . SER   B 51  ? 0.7647 0.5592 0.2974 0.3424  0.0403  -0.0324 60  SER   B N   
654  C CA  . SER   B 51  ? 0.7801 0.5895 0.3171 0.3539  0.0371  -0.0340 60  SER   B CA  
655  C C   . SER   B 51  ? 0.8095 0.6236 0.3296 0.3862  0.0288  -0.0478 60  SER   B C   
656  O O   . SER   B 51  ? 0.7966 0.6555 0.3338 0.3951  0.0275  -0.0614 60  SER   B O   
657  C CB  . SER   B 51  ? 0.7658 0.6251 0.3383 0.3395  0.0401  -0.0368 60  SER   B CB  
658  O OG  . SER   B 51  ? 0.7898 0.6562 0.3639 0.3488  0.0358  -0.0367 60  SER   B OG  
659  N N   . GLY   B 52  ? 0.8470 0.6146 0.3317 0.4038  0.0233  -0.0442 61  GLY   B N   
660  C CA  . GLY   B 52  ? 0.8719 0.6334 0.3317 0.4381  0.0137  -0.0574 61  GLY   B CA  
661  C C   . GLY   B 52  ? 0.8924 0.6428 0.3378 0.4449  0.0118  -0.0642 61  GLY   B C   
662  O O   . GLY   B 52  ? 0.9211 0.6223 0.3435 0.4346  0.0123  -0.0545 61  GLY   B O   
663  N N   . GLU   B 53  ? 0.8768 0.6775 0.3397 0.4580  0.0105  -0.0801 62  GLU   B N   
664  C CA  . GLU   B 53  ? 0.8938 0.6920 0.3463 0.4641  0.0099  -0.0871 62  GLU   B CA  
665  C C   . GLU   B 53  ? 0.8585 0.7060 0.3501 0.4392  0.0201  -0.0876 62  GLU   B C   
666  O O   . GLU   B 53  ? 0.8622 0.7180 0.3497 0.4446  0.0209  -0.0945 62  GLU   B O   
667  C CB  . GLU   B 53  ? 0.9393 0.7515 0.3716 0.5039  0.0003  -0.1056 62  GLU   B CB  
668  C CG  . GLU   B 53  ? 1.0388 0.8080 0.4323 0.5200  -0.0059 -0.1098 62  GLU   B CG  
669  C CD  . GLU   B 53  ? 1.1535 0.9281 0.5184 0.5643  -0.0175 -0.1284 62  GLU   B CD  
670  O OE1 . GLU   B 53  ? 1.1585 0.9749 0.5362 0.5833  -0.0208 -0.1388 62  GLU   B OE1 
671  O OE2 . GLU   B 53  ? 1.2108 0.9472 0.5388 0.5813  -0.0246 -0.1332 62  GLU   B OE2 
672  N N   . GLY   B 54  ? 0.8259 0.7017 0.3510 0.4134  0.0272  -0.0801 63  GLY   B N   
673  C CA  . GLY   B 54  ? 0.7960 0.7131 0.3545 0.3882  0.0363  -0.0792 63  GLY   B CA  
674  C C   . GLY   B 54  ? 0.7953 0.6780 0.3503 0.3627  0.0419  -0.0666 63  GLY   B C   
675  O O   . GLY   B 54  ? 0.8280 0.6560 0.3566 0.3622  0.0389  -0.0580 63  GLY   B O   
676  N N   . ARG   B 55  ? 0.7544 0.6693 0.3351 0.3407  0.0497  -0.0656 64  ARG   B N   
677  C CA  . ARG   B 55  ? 0.7460 0.6348 0.3262 0.3167  0.0546  -0.0553 64  ARG   B CA  
678  C C   . ARG   B 55  ? 0.7041 0.6224 0.3137 0.2904  0.0610  -0.0497 64  ARG   B C   
679  O O   . ARG   B 55  ? 0.6852 0.6511 0.3162 0.2870  0.0641  -0.0566 64  ARG   B O   
680  C CB  . ARG   B 55  ? 0.7625 0.6511 0.3333 0.3215  0.0560  -0.0617 64  ARG   B CB  
681  C CG  . ARG   B 55  ? 0.8142 0.6702 0.3800 0.3001  0.0588  -0.0524 64  ARG   B CG  
682  C CD  . ARG   B 55  ? 0.8683 0.7194 0.4197 0.3091  0.0584  -0.0597 64  ARG   B CD  
683  N NE  . ARG   B 55  ? 0.9074 0.7396 0.4602 0.2871  0.0616  -0.0527 64  ARG   B NE  
684  C CZ  . ARG   B 55  ? 0.9542 0.7433 0.4831 0.2892  0.0564  -0.0517 64  ARG   B CZ  
685  N NH1 . ARG   B 55  ? 0.9711 0.7272 0.4698 0.3119  0.0473  -0.0566 64  ARG   B NH1 
686  N NH2 . ARG   B 55  ? 0.9504 0.7266 0.4831 0.2691  0.0587  -0.0462 64  ARG   B NH2 
687  N N   . LEU   B 56  ? 0.6891 0.5798 0.2983 0.2723  0.0623  -0.0375 65  LEU   B N   
688  C CA  . LEU   B 56  ? 0.6595 0.5694 0.2897 0.2492  0.0665  -0.0321 65  LEU   B CA  
689  C C   . LEU   B 56  ? 0.6543 0.5494 0.2827 0.2323  0.0707  -0.0278 65  LEU   B C   
690  O O   . LEU   B 56  ? 0.6718 0.5299 0.2871 0.2279  0.0695  -0.0201 65  LEU   B O   
691  C CB  . LEU   B 56  ? 0.6634 0.5540 0.2921 0.2443  0.0644  -0.0221 65  LEU   B CB  
692  C CG  . LEU   B 56  ? 0.6697 0.5655 0.2956 0.2617  0.0592  -0.0246 65  LEU   B CG  
693  C CD1 . LEU   B 56  ? 0.6785 0.5591 0.3038 0.2543  0.0587  -0.0141 65  LEU   B CD1 
694  C CD2 . LEU   B 56  ? 0.6539 0.5967 0.2988 0.2661  0.0575  -0.0355 65  LEU   B CD2 
695  N N   . ASP   B 57  ? 0.6300 0.5538 0.2702 0.2228  0.0754  -0.0326 66  ASP   B N   
696  C CA  . ASP   B 57  ? 0.6309 0.5404 0.2672 0.2082  0.0789  -0.0294 66  ASP   B CA  
697  C C   . ASP   B 57  ? 0.5998 0.5155 0.2479 0.1857  0.0813  -0.0232 66  ASP   B C   
698  O O   . ASP   B 57  ? 0.5960 0.5403 0.2576 0.1799  0.0820  -0.0250 66  ASP   B O   
699  C CB  . ASP   B 57  ? 0.6688 0.6015 0.3046 0.2141  0.0830  -0.0385 66  ASP   B CB  
700  C CG  . ASP   B 57  ? 0.7834 0.6984 0.3995 0.2377  0.0789  -0.0448 66  ASP   B CG  
701  O OD1 . ASP   B 57  ? 0.8268 0.7010 0.4251 0.2375  0.0756  -0.0411 66  ASP   B OD1 
702  O OD2 . ASP   B 57  ? 0.8113 0.7529 0.4285 0.2569  0.0779  -0.0539 66  ASP   B OD2 
703  N N   . PRO   B 58  ? 0.5776 0.4659 0.2194 0.1733  0.0813  -0.0162 67  PRO   B N   
704  C CA  . PRO   B 58  ? 0.5528 0.4436 0.2011 0.1553  0.0818  -0.0109 67  PRO   B CA  
705  C C   . PRO   B 58  ? 0.5201 0.4358 0.1749 0.1428  0.0859  -0.0147 67  PRO   B C   
706  O O   . PRO   B 58  ? 0.5188 0.4467 0.1719 0.1444  0.0903  -0.0201 67  PRO   B O   
707  C CB  . PRO   B 58  ? 0.5746 0.4342 0.2140 0.1482  0.0805  -0.0048 67  PRO   B CB  
708  C CG  . PRO   B 58  ? 0.5940 0.4375 0.2228 0.1576  0.0801  -0.0081 67  PRO   B CG  
709  C CD  . PRO   B 58  ? 0.5800 0.4333 0.2073 0.1756  0.0791  -0.0131 67  PRO   B CD  
710  N N   . TYR   B 59  ? 0.4899 0.4120 0.1496 0.1304  0.0840  -0.0116 68  TYR   B N   
711  C CA  . TYR   B 59  ? 0.4623 0.4033 0.1250 0.1147  0.0870  -0.0135 68  TYR   B CA  
712  C C   . TYR   B 59  ? 0.4512 0.3687 0.1027 0.0995  0.0849  -0.0081 68  TYR   B C   
713  O O   . TYR   B 59  ? 0.4534 0.3695 0.0977 0.0884  0.0885  -0.0086 68  TYR   B O   
714  C CB  . TYR   B 59  ? 0.4420 0.4127 0.1177 0.1128  0.0848  -0.0164 68  TYR   B CB  
715  C CG  . TYR   B 59  ? 0.4387 0.4287 0.1173 0.0927  0.0872  -0.0171 68  TYR   B CG  
716  C CD1 . TYR   B 59  ? 0.4618 0.4313 0.1295 0.0759  0.0831  -0.0119 68  TYR   B CD1 
717  C CD2 . TYR   B 59  ? 0.4307 0.4609 0.1222 0.0906  0.0926  -0.0229 68  TYR   B CD2 
718  C CE1 . TYR   B 59  ? 0.4694 0.4509 0.1356 0.0553  0.0842  -0.0115 68  TYR   B CE1 
719  C CE2 . TYR   B 59  ? 0.4378 0.4875 0.1325 0.0687  0.0951  -0.0222 68  TYR   B CE2 
720  C CZ  . TYR   B 59  ? 0.4621 0.4842 0.1427 0.0499  0.0907  -0.0160 68  TYR   B CZ  
721  O OH  . TYR   B 59  ? 0.4707 0.5058 0.1500 0.0260  0.0923  -0.0144 68  TYR   B OH  
722  N N   . TRP   B 60  ? 0.4379 0.3375 0.0858 0.1008  0.0788  -0.0031 69  TRP   B N   
723  C CA  . TRP   B 60  ? 0.4434 0.3206 0.0785 0.0909  0.0751  0.0010  69  TRP   B CA  
724  C C   . TRP   B 60  ? 0.4595 0.3188 0.0926 0.1002  0.0716  0.0058  69  TRP   B C   
725  O O   . TRP   B 60  ? 0.4678 0.3315 0.1072 0.1105  0.0699  0.0077  69  TRP   B O   
726  C CB  . TRP   B 60  ? 0.4367 0.3160 0.0673 0.0804  0.0696  0.0019  69  TRP   B CB  
727  C CG  . TRP   B 60  ? 0.4526 0.3053 0.0658 0.0758  0.0634  0.0056  69  TRP   B CG  
728  C CD1 . TRP   B 60  ? 0.4779 0.3131 0.0756 0.0668  0.0636  0.0057  69  TRP   B CD1 
729  C CD2 . TRP   B 60  ? 0.4563 0.2969 0.0644 0.0845  0.0562  0.0091  69  TRP   B CD2 
730  N NE1 . TRP   B 60  ? 0.4940 0.3076 0.0771 0.0695  0.0560  0.0082  69  TRP   B NE1 
731  C CE2 . TRP   B 60  ? 0.4802 0.2985 0.0699 0.0804  0.0517  0.0104  69  TRP   B CE2 
732  C CE3 . TRP   B 60  ? 0.4523 0.2993 0.0677 0.0969  0.0532  0.0110  69  TRP   B CE3 
733  C CZ2 . TRP   B 60  ? 0.4913 0.2973 0.0710 0.0889  0.0442  0.0132  69  TRP   B CZ2 
734  C CZ3 . TRP   B 60  ? 0.4635 0.2975 0.0687 0.1042  0.0467  0.0147  69  TRP   B CZ3 
735  C CH2 . TRP   B 60  ? 0.4779 0.2934 0.0661 0.1006  0.0423  0.0155  69  TRP   B CH2 
736  N N   . GLY   B 61  ? 0.4604 0.3015 0.0842 0.0963  0.0702  0.0079  70  GLY   B N   
737  C CA  . GLY   B 61  ? 0.4613 0.2914 0.0851 0.1026  0.0675  0.0127  70  GLY   B CA  
738  C C   . GLY   B 61  ? 0.4698 0.2853 0.0820 0.0969  0.0637  0.0134  70  GLY   B C   
739  O O   . GLY   B 61  ? 0.4791 0.2872 0.0822 0.0892  0.0644  0.0099  70  GLY   B O   
740  N N   . ASP   B 62  ? 0.4645 0.2771 0.0759 0.1020  0.0598  0.0175  71  ASP   B N   
741  C CA  . ASP   B 62  ? 0.4783 0.2805 0.0784 0.1001  0.0548  0.0172  71  ASP   B CA  
742  C C   . ASP   B 62  ? 0.4798 0.2884 0.0879 0.1070  0.0539  0.0222  71  ASP   B C   
743  O O   . ASP   B 62  ? 0.4844 0.3021 0.0966 0.1146  0.0538  0.0266  71  ASP   B O   
744  C CB  . ASP   B 62  ? 0.5118 0.3064 0.0949 0.0988  0.0484  0.0157  71  ASP   B CB  
745  C CG  . ASP   B 62  ? 0.6035 0.3825 0.1675 0.0985  0.0415  0.0136  71  ASP   B CG  
746  O OD1 . ASP   B 62  ? 0.6154 0.3986 0.1813 0.1064  0.0387  0.0151  71  ASP   B OD1 
747  O OD2 . ASP   B 62  ? 0.6537 0.4171 0.1996 0.0906  0.0388  0.0103  71  ASP   B OD2 
748  N N   . VAL   B 63  ? 0.4715 0.2770 0.0816 0.1041  0.0531  0.0215  72  VAL   B N   
749  C CA  . VAL   B 63  ? 0.4670 0.2834 0.0876 0.1071  0.0529  0.0265  72  VAL   B CA  
750  C C   . VAL   B 63  ? 0.4698 0.2947 0.0831 0.1150  0.0475  0.0274  72  VAL   B C   
751  O O   . VAL   B 63  ? 0.4646 0.3057 0.0870 0.1204  0.0493  0.0334  72  VAL   B O   
752  C CB  . VAL   B 63  ? 0.4784 0.2899 0.1051 0.0998  0.0526  0.0248  72  VAL   B CB  
753  C CG1 . VAL   B 63  ? 0.4770 0.3031 0.1132 0.0998  0.0501  0.0283  72  VAL   B CG1 
754  C CG2 . VAL   B 63  ? 0.4902 0.2950 0.1244 0.0963  0.0573  0.0265  72  VAL   B CG2 
755  N N   . LYS   B 64  ? 0.4782 0.2913 0.0724 0.1167  0.0409  0.0217  73  LYS   B N   
756  C CA  . LYS   B 64  ? 0.4814 0.2997 0.0635 0.1281  0.0339  0.0214  73  LYS   B CA  
757  C C   . LYS   B 64  ? 0.4820 0.3051 0.0610 0.1368  0.0338  0.0254  73  LYS   B C   
758  O O   . LYS   B 64  ? 0.4767 0.3160 0.0578 0.1481  0.0329  0.0291  73  LYS   B O   
759  C CB  . LYS   B 64  ? 0.5120 0.3093 0.0678 0.1291  0.0250  0.0141  73  LYS   B CB  
760  C CG  . LYS   B 64  ? 0.5611 0.3642 0.1026 0.1443  0.0161  0.0122  73  LYS   B CG  
761  C CD  . LYS   B 64  ? 0.6345 0.4090 0.1427 0.1470  0.0055  0.0047  73  LYS   B CD  
762  C CE  . LYS   B 64  ? 0.6657 0.4474 0.1624 0.1616  -0.0033 -0.0001 73  LYS   B CE  
763  N NZ  . LYS   B 64  ? 0.6888 0.4743 0.1688 0.1798  -0.0109 0.0000  73  LYS   B NZ  
764  N N   . GLN   B 65  ? 0.4808 0.2924 0.0554 0.1320  0.0347  0.0244  74  GLN   B N   
765  C CA  . GLN   B 65  ? 0.4818 0.2962 0.0536 0.1398  0.0332  0.0271  74  GLN   B CA  
766  C C   . GLN   B 65  ? 0.4721 0.3045 0.0640 0.1440  0.0413  0.0339  74  GLN   B C   
767  O O   . GLN   B 65  ? 0.4786 0.3178 0.0678 0.1554  0.0401  0.0374  74  GLN   B O   
768  C CB  . GLN   B 65  ? 0.5110 0.3119 0.0755 0.1312  0.0315  0.0236  74  GLN   B CB  
769  C CG  . GLN   B 65  ? 0.5856 0.3636 0.1239 0.1264  0.0224  0.0185  74  GLN   B CG  
770  C CD  . GLN   B 65  ? 0.6568 0.4254 0.1897 0.1142  0.0214  0.0163  74  GLN   B CD  
771  O OE1 . GLN   B 65  ? 0.6747 0.4447 0.2062 0.1168  0.0174  0.0169  74  GLN   B OE1 
772  N NE2 . GLN   B 65  ? 0.6645 0.4248 0.1939 0.1003  0.0247  0.0136  74  GLN   B NE2 
773  N N   . ASP   B 66  ? 0.4602 0.2966 0.0683 0.1356  0.0487  0.0357  75  ASP   B N   
774  C CA  . ASP   B 66  ? 0.4511 0.2967 0.0739 0.1370  0.0560  0.0422  75  ASP   B CA  
775  C C   . ASP   B 66  ? 0.4483 0.2909 0.0702 0.1410  0.0568  0.0414  75  ASP   B C   
776  O O   . ASP   B 66  ? 0.4502 0.2989 0.0732 0.1504  0.0585  0.0464  75  ASP   B O   
777  C CB  . ASP   B 66  ? 0.4559 0.3183 0.0826 0.1453  0.0579  0.0498  75  ASP   B CB  
778  C CG  . ASP   B 66  ? 0.4868 0.3551 0.1267 0.1419  0.0659  0.0579  75  ASP   B CG  
779  O OD1 . ASP   B 66  ? 0.4987 0.3560 0.1443 0.1322  0.0684  0.0568  75  ASP   B OD1 
780  O OD2 . ASP   B 66  ? 0.4906 0.3722 0.1321 0.1492  0.0694  0.0656  75  ASP   B OD2 
781  N N   . LEU   B 67  ? 0.4420 0.2771 0.0615 0.1344  0.0555  0.0350  76  LEU   B N   
782  C CA  . LEU   B 67  ? 0.4370 0.2746 0.0598 0.1375  0.0552  0.0325  76  LEU   B CA  
783  C C   . LEU   B 67  ? 0.4403 0.2780 0.0681 0.1302  0.0595  0.0280  76  LEU   B C   
784  O O   . LEU   B 67  ? 0.4563 0.2886 0.0814 0.1209  0.0600  0.0246  76  LEU   B O   
785  C CB  . LEU   B 67  ? 0.4357 0.2695 0.0577 0.1378  0.0460  0.0280  76  LEU   B CB  
786  C CG  . LEU   B 67  ? 0.4568 0.2888 0.0584 0.1494  0.0406  0.0316  76  LEU   B CG  
787  C CD1 . LEU   B 67  ? 0.4724 0.2909 0.0569 0.1465  0.0302  0.0269  76  LEU   B CD1 
788  C CD2 . LEU   B 67  ? 0.4570 0.2973 0.0581 0.1628  0.0423  0.0362  76  LEU   B CD2 
789  N N   . VAL   B 68  ? 0.4310 0.2753 0.0654 0.1361  0.0620  0.0270  77  VAL   B N   
790  C CA  . VAL   B 68  ? 0.4329 0.2814 0.0727 0.1330  0.0656  0.0214  77  VAL   B CA  
791  C C   . VAL   B 68  ? 0.4388 0.3017 0.0839 0.1404  0.0646  0.0172  77  VAL   B C   
792  O O   . VAL   B 68  ? 0.4461 0.3098 0.0912 0.1519  0.0633  0.0198  77  VAL   B O   
793  C CB  . VAL   B 68  ? 0.4371 0.2756 0.0783 0.1340  0.0698  0.0232  77  VAL   B CB  
794  C CG1 . VAL   B 68  ? 0.4481 0.2812 0.0893 0.1440  0.0709  0.0295  77  VAL   B CG1 
795  C CG2 . VAL   B 68  ? 0.4366 0.2785 0.0793 0.1336  0.0725  0.0164  77  VAL   B CG2 
796  N N   . SER   B 69  ? 0.4332 0.3095 0.0823 0.1335  0.0651  0.0105  78  SER   B N   
797  C CA  . SER   B 69  ? 0.4241 0.3212 0.0813 0.1385  0.0636  0.0050  78  SER   B CA  
798  C C   . SER   B 69  ? 0.4237 0.3349 0.0874 0.1425  0.0688  -0.0010 78  SER   B C   
799  O O   . SER   B 69  ? 0.4208 0.3312 0.0829 0.1345  0.0731  -0.0027 78  SER   B O   
800  C CB  . SER   B 69  ? 0.4241 0.3306 0.0812 0.1259  0.0589  0.0025  78  SER   B CB  
801  O OG  . SER   B 69  ? 0.4321 0.3382 0.0861 0.1104  0.0622  0.0011  78  SER   B OG  
802  N N   . TYR   B 70  ? 0.4240 0.3470 0.0924 0.1574  0.0679  -0.0048 79  TYR   B N   
803  C CA  . TYR   B 70  ? 0.4264 0.3633 0.0980 0.1676  0.0712  -0.0118 79  TYR   B CA  
804  C C   . TYR   B 70  ? 0.4152 0.3898 0.1003 0.1682  0.0701  -0.0202 79  TYR   B C   
805  O O   . TYR   B 70  ? 0.4119 0.3963 0.1025 0.1684  0.0646  -0.0207 79  TYR   B O   
806  C CB  . TYR   B 70  ? 0.4341 0.3525 0.0963 0.1867  0.0696  -0.0102 79  TYR   B CB  
807  C CG  . TYR   B 70  ? 0.4556 0.3404 0.1061 0.1834  0.0711  -0.0019 79  TYR   B CG  
808  C CD1 . TYR   B 70  ? 0.4678 0.3390 0.1164 0.1755  0.0702  0.0067  79  TYR   B CD1 
809  C CD2 . TYR   B 70  ? 0.4771 0.3456 0.1184 0.1878  0.0728  -0.0032 79  TYR   B CD2 
810  C CE1 . TYR   B 70  ? 0.4897 0.3374 0.1314 0.1703  0.0718  0.0140  79  TYR   B CE1 
811  C CE2 . TYR   B 70  ? 0.5021 0.3413 0.1343 0.1816  0.0731  0.0042  79  TYR   B CE2 
812  C CZ  . TYR   B 70  ? 0.5152 0.3468 0.1496 0.1720  0.0730  0.0129  79  TYR   B CZ  
813  O OH  . TYR   B 70  ? 0.5497 0.3593 0.1787 0.1643  0.0734  0.0199  79  TYR   B OH  
814  N N   . CYS   B 71  ? 0.4048 0.4026 0.0955 0.1688  0.0750  -0.0270 80  CYS   B N   
815  C CA  . CYS   B 71  ? 0.3939 0.4366 0.1008 0.1684  0.0754  -0.0355 80  CYS   B CA  
816  C C   . CYS   B 71  ? 0.3729 0.4330 0.0887 0.1430  0.0761  -0.0338 80  CYS   B C   
817  O O   . CYS   B 71  ? 0.3630 0.4623 0.0922 0.1361  0.0797  -0.0395 80  CYS   B O   
818  C CB  . CYS   B 71  ? 0.4202 0.4777 0.1331 0.1863  0.0687  -0.0408 80  CYS   B CB  
819  S SG  . CYS   B 71  ? 0.5371 0.5645 0.2319 0.2157  0.0662  -0.0413 80  CYS   B SG  
820  N N   . GLY   B 72  ? 0.3648 0.3967 0.0717 0.1294  0.0726  -0.0262 81  GLY   B N   
821  C CA  . GLY   B 72  ? 0.3549 0.3934 0.0632 0.1053  0.0714  -0.0242 81  GLY   B CA  
822  C C   . GLY   B 72  ? 0.3705 0.3699 0.0619 0.0954  0.0670  -0.0164 81  GLY   B C   
823  O O   . GLY   B 72  ? 0.3757 0.3473 0.0572 0.1058  0.0665  -0.0122 81  GLY   B O   
824  N N   . PRO   B 73  ? 0.3813 0.3785 0.0677 0.0746  0.0634  -0.0144 82  PRO   B N   
825  C CA  . PRO   B 73  ? 0.4093 0.3679 0.0752 0.0672  0.0575  -0.0082 82  PRO   B CA  
826  C C   . PRO   B 73  ? 0.4286 0.3706 0.0890 0.0794  0.0474  -0.0062 82  PRO   B C   
827  O O   . PRO   B 73  ? 0.4214 0.3809 0.0929 0.0884  0.0431  -0.0096 82  PRO   B O   
828  C CB  . PRO   B 73  ? 0.4210 0.3815 0.0803 0.0421  0.0549  -0.0075 82  PRO   B CB  
829  C CG  . PRO   B 73  ? 0.4020 0.4049 0.0829 0.0372  0.0553  -0.0130 82  PRO   B CG  
830  C CD  . PRO   B 73  ? 0.3633 0.3928 0.0608 0.0563  0.0640  -0.0178 82  PRO   B CD  
831  N N   . TRP   B 74  ? 0.4481 0.3573 0.0899 0.0805  0.0429  -0.0010 83  TRP   B N   
832  C CA  . TRP   B 74  ? 0.4599 0.3530 0.0929 0.0933  0.0338  0.0015  83  TRP   B CA  
833  C C   . TRP   B 74  ? 0.4744 0.3727 0.1060 0.0867  0.0228  -0.0015 83  TRP   B C   
834  O O   . TRP   B 74  ? 0.4788 0.3737 0.1033 0.0668  0.0193  -0.0022 83  TRP   B O   
835  C CB  . TRP   B 74  ? 0.4706 0.3328 0.0827 0.0944  0.0306  0.0064  83  TRP   B CB  
836  C CG  . TRP   B 74  ? 0.4781 0.3288 0.0820 0.1116  0.0238  0.0094  83  TRP   B CG  
837  C CD1 . TRP   B 74  ? 0.4970 0.3345 0.0858 0.1143  0.0115  0.0091  83  TRP   B CD1 
838  C CD2 . TRP   B 74  ? 0.4722 0.3246 0.0814 0.1289  0.0289  0.0134  83  TRP   B CD2 
839  N NE1 . TRP   B 74  ? 0.5039 0.3369 0.0882 0.1341  0.0094  0.0124  83  TRP   B NE1 
840  C CE2 . TRP   B 74  ? 0.4919 0.3351 0.0895 0.1421  0.0207  0.0157  83  TRP   B CE2 
841  C CE3 . TRP   B 74  ? 0.4723 0.3310 0.0928 0.1336  0.0390  0.0156  83  TRP   B CE3 
842  C CZ2 . TRP   B 74  ? 0.5000 0.3442 0.0987 0.1592  0.0242  0.0209  83  TRP   B CZ2 
843  C CZ3 . TRP   B 74  ? 0.4870 0.3432 0.1078 0.1482  0.0414  0.0210  83  TRP   B CZ3 
844  C CH2 . TRP   B 74  ? 0.4946 0.3456 0.1054 0.1604  0.0350  0.0239  83  TRP   B CH2 
845  N N   . LYS   B 75  ? 0.4780 0.3848 0.1161 0.1024  0.0173  -0.0034 84  LYS   B N   
846  C CA  . LYS   B 75  ? 0.4872 0.4022 0.1269 0.0981  0.0056  -0.0076 84  LYS   B CA  
847  C C   . LYS   B 75  ? 0.5303 0.4193 0.1503 0.1095  -0.0076 -0.0058 84  LYS   B C   
848  O O   . LYS   B 75  ? 0.5356 0.4232 0.1512 0.1036  -0.0203 -0.0093 84  LYS   B O   
849  C CB  . LYS   B 75  ? 0.4750 0.4245 0.1379 0.1089  0.0080  -0.0136 84  LYS   B CB  
850  C CG  . LYS   B 75  ? 0.4879 0.4703 0.1707 0.0997  0.0190  -0.0177 84  LYS   B CG  
851  C CD  . LYS   B 75  ? 0.5131 0.5210 0.2066 0.0771  0.0148  -0.0222 84  LYS   B CD  
852  C CE  . LYS   B 75  ? 0.5209 0.5758 0.2398 0.0778  0.0236  -0.0289 84  LYS   B CE  
853  N NZ  . LYS   B 75  ? 0.5369 0.6018 0.2578 0.0609  0.0354  -0.0271 84  LYS   B NZ  
854  N N   . LEU   B 76  ? 0.5553 0.4263 0.1640 0.1269  -0.0052 -0.0006 85  LEU   B N   
855  C CA  . LEU   B 76  ? 0.5799 0.4297 0.1689 0.1430  -0.0162 0.0014  85  LEU   B CA  
856  C C   . LEU   B 76  ? 0.6279 0.4478 0.1906 0.1333  -0.0252 0.0030  85  LEU   B C   
857  O O   . LEU   B 76  ? 0.6341 0.4447 0.1907 0.1287  -0.0186 0.0063  85  LEU   B O   
858  C CB  . LEU   B 76  ? 0.5714 0.4200 0.1603 0.1646  -0.0079 0.0071  85  LEU   B CB  
859  C CG  . LEU   B 76  ? 0.5643 0.4342 0.1741 0.1722  0.0038  0.0070  85  LEU   B CG  
860  C CD1 . LEU   B 76  ? 0.5764 0.4394 0.1817 0.1886  0.0114  0.0144  85  LEU   B CD1 
861  C CD2 . LEU   B 76  ? 0.5571 0.4433 0.1766 0.1798  -0.0019 0.0009  85  LEU   B CD2 
862  N N   . ASP   B 77  ? 0.6609 0.4634 0.2057 0.1303  -0.0415 0.0001  86  ASP   B N   
863  C CA  . ASP   B 77  ? 0.7081 0.4761 0.2220 0.1205  -0.0526 0.0008  86  ASP   B CA  
864  C C   . ASP   B 77  ? 0.7522 0.4903 0.2348 0.1378  -0.0699 0.0002  86  ASP   B C   
865  O O   . ASP   B 77  ? 0.7817 0.4866 0.2338 0.1304  -0.0822 -0.0004 86  ASP   B O   
866  C CB  . ASP   B 77  ? 0.7306 0.4974 0.2450 0.0900  -0.0572 -0.0020 86  ASP   B CB  
867  C CG  . ASP   B 77  ? 0.7751 0.5547 0.2992 0.0823  -0.0681 -0.0071 86  ASP   B CG  
868  O OD1 . ASP   B 77  ? 0.7638 0.5620 0.3026 0.1010  -0.0686 -0.0095 86  ASP   B OD1 
869  O OD2 . ASP   B 77  ? 0.8081 0.5794 0.3250 0.0567  -0.0764 -0.0086 86  ASP   B OD2 
870  N N   . ALA   B 78  ? 0.7606 0.5068 0.2461 0.1618  -0.0719 0.0002  87  ALA   B N   
871  C CA  . ALA   B 78  ? 0.7948 0.5133 0.2482 0.1820  -0.0883 -0.0006 87  ALA   B CA  
872  C C   . ALA   B 78  ? 0.8250 0.5331 0.2603 0.2013  -0.0839 0.0042  87  ALA   B C   
873  O O   . ALA   B 78  ? 0.8139 0.5426 0.2683 0.2025  -0.0670 0.0087  87  ALA   B O   
874  C CB  . ALA   B 78  ? 0.7817 0.5134 0.2434 0.2011  -0.0921 -0.0025 87  ALA   B CB  
875  N N   . ALA   B 79  ? 0.8579 0.5351 0.2560 0.2168  -0.1001 0.0027  88  ALA   B N   
876  C CA  . ALA   B 79  ? 0.8804 0.5536 0.2615 0.2376  -0.0968 0.0062  88  ALA   B CA  
877  C C   . ALA   B 79  ? 0.9140 0.5721 0.2651 0.2681  -0.1104 0.0052  88  ALA   B C   
878  O O   . ALA   B 79  ? 0.9347 0.5663 0.2626 0.2703  -0.1293 0.0002  88  ALA   B O   
879  C CB  . ALA   B 79  ? 0.8994 0.5485 0.2592 0.2253  -0.1014 0.0048  88  ALA   B CB  
880  N N   . TRP   B 80  ? 0.9152 0.5910 0.2659 0.2917  -0.1008 0.0100  89  TRP   B N   
881  C CA  . TRP   B 80  ? 0.9389 0.6078 0.2616 0.3248  -0.1098 0.0102  89  TRP   B CA  
882  C C   . TRP   B 80  ? 0.9979 0.6219 0.2726 0.3322  -0.1341 0.0033  89  TRP   B C   
883  O O   . TRP   B 80  ? 1.0140 0.6200 0.2766 0.3182  -0.1377 0.0011  89  TRP   B O   
884  C CB  . TRP   B 80  ? 0.9165 0.6167 0.2495 0.3412  -0.0931 0.0170  89  TRP   B CB  
885  C CG  . TRP   B 80  ? 0.9261 0.6283 0.2323 0.3769  -0.0989 0.0182  89  TRP   B CG  
886  C CD1 . TRP   B 80  ? 0.9408 0.6419 0.2366 0.3980  -0.1040 0.0189  89  TRP   B CD1 
887  C CD2 . TRP   B 80  ? 0.9242 0.6364 0.2132 0.3974  -0.0980 0.0193  89  TRP   B CD2 
888  N NE1 . TRP   B 80  ? 0.9476 0.6561 0.2188 0.4306  -0.1061 0.0207  89  TRP   B NE1 
889  C CE2 . TRP   B 80  ? 0.9390 0.6568 0.2068 0.4309  -0.1022 0.0208  89  TRP   B CE2 
890  C CE3 . TRP   B 80  ? 0.9244 0.6432 0.2135 0.3921  -0.0943 0.0185  89  TRP   B CE3 
891  C CZ2 . TRP   B 80  ? 0.9444 0.6781 0.1926 0.4589  -0.1022 0.0218  89  TRP   B CZ2 
892  C CZ3 . TRP   B 80  ? 0.9334 0.6674 0.2038 0.4197  -0.0953 0.0187  89  TRP   B CZ3 
893  C CH2 . TRP   B 80  ? 0.9398 0.6830 0.1908 0.4526  -0.0988 0.0204  89  TRP   B CH2 
894  N N   . ASP   B 81  ? 1.0313 0.6324 0.2752 0.3539  -0.1521 -0.0005 90  ASP   B N   
895  C CA  . ASP   B 81  ? 1.0842 0.6351 0.2765 0.3616  -0.1781 -0.0075 90  ASP   B CA  
896  C C   . ASP   B 81  ? 1.1117 0.6578 0.2704 0.3938  -0.1822 -0.0081 90  ASP   B C   
897  O O   . ASP   B 81  ? 1.1521 0.6537 0.2617 0.4061  -0.2051 -0.0146 90  ASP   B O   
898  C CB  . ASP   B 81  ? 1.1233 0.6436 0.2920 0.3680  -0.2001 -0.0130 90  ASP   B CB  
899  C CG  . ASP   B 81  ? 1.1775 0.7147 0.3439 0.4014  -0.1991 -0.0115 90  ASP   B CG  
900  O OD1 . ASP   B 81  ? 1.1805 0.7576 0.3678 0.4173  -0.1786 -0.0047 90  ASP   B OD1 
901  O OD2 . ASP   B 81  ? 1.2011 0.7110 0.3438 0.4110  -0.2192 -0.0169 90  ASP   B OD2 
902  N N   . GLY   B 82  ? 1.0847 0.6763 0.2686 0.4070  -0.1612 -0.0018 91  GLY   B N   
903  C CA  . GLY   B 82  ? 1.0906 0.6899 0.2491 0.4382  -0.1628 -0.0023 91  GLY   B CA  
904  C C   . GLY   B 82  ? 1.0958 0.6919 0.2232 0.4777  -0.1734 -0.0036 91  GLY   B C   
905  O O   . GLY   B 82  ? 1.1028 0.7101 0.2078 0.5080  -0.1750 -0.0044 91  GLY   B O   
906  N N   . LEU   B 83  ? 1.0909 0.6739 0.2163 0.4795  -0.1810 -0.0043 92  LEU   B N   
907  C CA  . LEU   B 83  ? 1.1015 0.6777 0.1951 0.5176  -0.1921 -0.0058 92  LEU   B CA  
908  C C   . LEU   B 83  ? 1.0748 0.6834 0.1980 0.5233  -0.1769 0.0011  92  LEU   B C   
909  O O   . LEU   B 83  ? 1.0751 0.7030 0.1859 0.5565  -0.1726 0.0045  92  LEU   B O   
910  C CB  . LEU   B 83  ? 1.1427 0.6566 0.1887 0.5212  -0.2245 -0.0158 92  LEU   B CB  
911  C CG  . LEU   B 83  ? 1.1932 0.6583 0.1926 0.5215  -0.2466 -0.0237 92  LEU   B CG  
912  C CD1 . LEU   B 83  ? 1.2393 0.6414 0.1915 0.5243  -0.2791 -0.0323 92  LEU   B CD1 
913  C CD2 . LEU   B 83  ? 1.2059 0.6832 0.1762 0.5599  -0.2470 -0.0248 92  LEU   B CD2 
914  N N   . SER   B 84  ? 1.0509 0.6634 0.2086 0.4936  -0.1702 0.0025  93  SER   B N   
915  C CA  . SER   B 84  ? 1.0324 0.6669 0.2116 0.5004  -0.1597 0.0073  93  SER   B CA  
916  C C   . SER   B 84  ? 0.9866 0.6722 0.2052 0.4987  -0.1293 0.0189  93  SER   B C   
917  O O   . SER   B 84  ? 0.9749 0.6827 0.2182 0.4805  -0.1139 0.0232  93  SER   B O   
918  C CB  . SER   B 84  ? 1.0584 0.6766 0.2553 0.4730  -0.1675 0.0025  93  SER   B CB  
919  O OG  . SER   B 84  ? 1.1176 0.6920 0.2894 0.4578  -0.1918 -0.0067 93  SER   B OG  
920  N N   . GLU   B 85  ? 0.9643 0.6652 0.1865 0.5169  -0.1216 0.0241  94  GLU   B N   
921  C CA  . GLU   B 85  ? 0.9242 0.6661 0.1806 0.5126  -0.0942 0.0358  94  GLU   B CA  
922  C C   . GLU   B 85  ? 0.8897 0.6329 0.1827 0.4787  -0.0873 0.0350  94  GLU   B C   
923  O O   . GLU   B 85  ? 0.9039 0.6221 0.1949 0.4659  -0.1032 0.0262  94  GLU   B O   
924  C CB  . GLU   B 85  ? 0.9442 0.6964 0.1866 0.5440  -0.0891 0.0418  94  GLU   B CB  
925  C CG  . GLU   B 85  ? 0.9782 0.7516 0.1979 0.5755  -0.0832 0.0477  94  GLU   B CG  
926  C CD  . GLU   B 85  ? 1.0015 0.7982 0.2172 0.5999  -0.0681 0.0584  94  GLU   B CD  
927  O OE1 . GLU   B 85  ? 0.9940 0.7783 0.2121 0.6007  -0.0689 0.0586  94  GLU   B OE1 
928  O OE2 . GLU   B 85  ? 0.9959 0.8247 0.2058 0.6181  -0.0551 0.0666  94  GLU   B OE2 
929  N N   . VAL   B 86  ? 0.8408 0.6141 0.1667 0.4636  -0.0644 0.0440  95  VAL   B N   
930  C CA  . VAL   B 86  ? 0.8022 0.5800 0.1617 0.4342  -0.0562 0.0436  95  VAL   B CA  
931  C C   . VAL   B 86  ? 0.7692 0.5684 0.1465 0.4382  -0.0367 0.0536  95  VAL   B C   
932  O O   . VAL   B 86  ? 0.7676 0.5795 0.1324 0.4604  -0.0283 0.0620  95  VAL   B O   
933  C CB  . VAL   B 86  ? 0.7821 0.5664 0.1613 0.4064  -0.0501 0.0429  95  VAL   B CB  
934  C CG1 . VAL   B 86  ? 0.7996 0.5565 0.1553 0.4029  -0.0700 0.0335  95  VAL   B CG1 
935  C CG2 . VAL   B 86  ? 0.7676 0.5814 0.1578 0.4087  -0.0316 0.0530  95  VAL   B CG2 
936  N N   . GLN   B 87  ? 0.7441 0.5464 0.1476 0.4176  -0.0297 0.0530  96  GLN   B N   
937  C CA  . GLN   B 87  ? 0.7243 0.5396 0.1403 0.4200  -0.0127 0.0621  96  GLN   B CA  
938  C C   . GLN   B 87  ? 0.6917 0.5200 0.1376 0.3929  0.0024  0.0662  96  GLN   B C   
939  O O   . GLN   B 87  ? 0.6897 0.5128 0.1513 0.3734  -0.0023 0.0585  96  GLN   B O   
940  C CB  . GLN   B 87  ? 0.7393 0.5413 0.1499 0.4308  -0.0211 0.0566  96  GLN   B CB  
941  C CG  . GLN   B 87  ? 0.7801 0.5759 0.1618 0.4635  -0.0245 0.0603  96  GLN   B CG  
942  C CD  . GLN   B 87  ? 0.8145 0.5971 0.1897 0.4763  -0.0328 0.0546  96  GLN   B CD  
943  O OE1 . GLN   B 87  ? 0.8029 0.5871 0.1972 0.4634  -0.0293 0.0518  96  GLN   B OE1 
944  N NE2 . GLN   B 87  ? 0.8366 0.6060 0.1827 0.5045  -0.0450 0.0522  96  GLN   B NE2 
945  N N   . LEU   B 88  ? 0.6640 0.5095 0.1169 0.3913  0.0202  0.0785  97  LEU   B N   
946  C CA  . LEU   B 88  ? 0.6399 0.4935 0.1176 0.3675  0.0338  0.0831  97  LEU   B CA  
947  C C   . LEU   B 88  ? 0.6364 0.4804 0.1146 0.3714  0.0384  0.0852  97  LEU   B C   
948  O O   . LEU   B 88  ? 0.6454 0.4898 0.1094 0.3878  0.0456  0.0943  97  LEU   B O   
949  C CB  . LEU   B 88  ? 0.6249 0.5001 0.1081 0.3637  0.0497  0.0959  97  LEU   B CB  
950  C CG  . LEU   B 88  ? 0.6243 0.5043 0.1287 0.3411  0.0642  0.1031  97  LEU   B CG  
951  C CD1 . LEU   B 88  ? 0.6317 0.5067 0.1548 0.3183  0.0596  0.0940  97  LEU   B CD1 
952  C CD2 . LEU   B 88  ? 0.6148 0.5181 0.1237 0.3375  0.0791  0.1167  97  LEU   B CD2 
953  N N   . LEU   B 89  ? 0.6208 0.4567 0.1128 0.3586  0.0340  0.0767  98  LEU   B N   
954  C CA  . LEU   B 89  ? 0.6175 0.4441 0.1084 0.3638  0.0379  0.0777  98  LEU   B CA  
955  C C   . LEU   B 89  ? 0.6199 0.4497 0.1226 0.3469  0.0535  0.0874  98  LEU   B C   
956  O O   . LEU   B 89  ? 0.6190 0.4495 0.1391 0.3281  0.0543  0.0825  98  LEU   B O   
957  C CB  . LEU   B 89  ? 0.6097 0.4316 0.1104 0.3594  0.0261  0.0635  98  LEU   B CB  
958  C CG  . LEU   B 89  ? 0.6269 0.4418 0.1305 0.3617  0.0299  0.0621  98  LEU   B CG  
959  C CD1 . LEU   B 89  ? 0.6499 0.4521 0.1308 0.3840  0.0341  0.0699  98  LEU   B CD1 
960  C CD2 . LEU   B 89  ? 0.6308 0.4495 0.1444 0.3611  0.0169  0.0471  98  LEU   B CD2 
961  N N   . ALA   B 90  ? 0.6205 0.4537 0.1134 0.3520  0.0657  0.1014  99  ALA   B N   
962  C CA  . ALA   B 90  ? 0.6271 0.4630 0.1301 0.3333  0.0797  0.1119  99  ALA   B CA  
963  C C   . ALA   B 90  ? 0.6428 0.4577 0.1381 0.3335  0.0845  0.1155  99  ALA   B C   
964  O O   . ALA   B 90  ? 0.6521 0.4556 0.1269 0.3518  0.0856  0.1200  99  ALA   B O   
965  C CB  . ALA   B 90  ? 0.6272 0.4806 0.1251 0.3353  0.0911  0.1261  99  ALA   B CB  
966  N N   . VAL   B 91  ? 0.6409 0.4483 0.1493 0.3147  0.0866  0.1131  100 VAL   B N   
967  C CA  . VAL   B 91  ? 0.6580 0.4407 0.1560 0.3141  0.0898  0.1157  100 VAL   B CA  
968  C C   . VAL   B 91  ? 0.6815 0.4588 0.1796 0.2951  0.1027  0.1306  100 VAL   B C   
969  O O   . VAL   B 91  ? 0.6767 0.4547 0.1899 0.2754  0.1037  0.1289  100 VAL   B O   
970  C CB  . VAL   B 91  ? 0.6471 0.4241 0.1563 0.3100  0.0808  0.1006  100 VAL   B CB  
971  C CG1 . VAL   B 91  ? 0.6638 0.4131 0.1579 0.3133  0.0822  0.1017  100 VAL   B CG1 
972  C CG2 . VAL   B 91  ? 0.6411 0.4285 0.1535 0.3244  0.0680  0.0866  100 VAL   B CG2 
973  N N   . PRO   B 92  ? 0.7030 0.4763 0.1840 0.2996  0.1126  0.1460  101 PRO   B N   
974  C CA  . PRO   B 92  ? 0.7166 0.4880 0.1991 0.2778  0.1248  0.1613  101 PRO   B CA  
975  C C   . PRO   B 92  ? 0.7552 0.4888 0.2236 0.2679  0.1257  0.1646  101 PRO   B C   
976  O O   . PRO   B 92  ? 0.7760 0.4821 0.2237 0.2841  0.1201  0.1596  101 PRO   B O   
977  C CB  . PRO   B 92  ? 0.7187 0.5020 0.1864 0.2873  0.1354  0.1766  101 PRO   B CB  
978  C CG  . PRO   B 92  ? 0.7192 0.5084 0.1768 0.3160  0.1272  0.1678  101 PRO   B CG  
979  C CD  . PRO   B 92  ? 0.7025 0.4740 0.1616 0.3237  0.1135  0.1506  101 PRO   B CD  
980  N N   . PRO   B 93  ? 0.7617 0.4922 0.2391 0.2420  0.1313  0.1725  102 PRO   B N   
981  C CA  . PRO   B 93  ? 0.7898 0.4783 0.2488 0.2321  0.1304  0.1761  102 PRO   B CA  
982  C C   . PRO   B 93  ? 0.8262 0.4833 0.2498 0.2417  0.1361  0.1891  102 PRO   B C   
983  O O   . PRO   B 93  ? 0.8234 0.4937 0.2412 0.2391  0.1472  0.2044  102 PRO   B O   
984  C CB  . PRO   B 93  ? 0.7889 0.4849 0.2643 0.2012  0.1359  0.1848  102 PRO   B CB  
985  C CG  . PRO   B 93  ? 0.7662 0.5089 0.2729 0.1976  0.1363  0.1794  102 PRO   B CG  
986  C CD  . PRO   B 93  ? 0.7367 0.5004 0.2394 0.2218  0.1370  0.1777  102 PRO   B CD  
987  N N   . GLY   B 94  ? 0.8557 0.4727 0.2542 0.2549  0.1282  0.1825  103 GLY   B N   
988  C CA  . GLY   B 94  ? 0.8933 0.4718 0.2517 0.2669  0.1313  0.1930  103 GLY   B CA  
989  C C   . GLY   B 94  ? 0.9042 0.4938 0.2505 0.2949  0.1321  0.1922  103 GLY   B C   
990  O O   . GLY   B 94  ? 0.9285 0.4837 0.2389 0.3116  0.1318  0.1967  103 GLY   B O   
991  N N   . GLU   B 95  ? 0.8857 0.5198 0.2583 0.3015  0.1320  0.1864  104 GLU   B N   
992  C CA  . GLU   B 95  ? 0.8981 0.5430 0.2591 0.3288  0.1308  0.1846  104 GLU   B CA  
993  C C   . GLU   B 95  ? 0.8900 0.5466 0.2640 0.3483  0.1156  0.1627  104 GLU   B C   
994  O O   . GLU   B 95  ? 0.8802 0.5502 0.2797 0.3374  0.1090  0.1505  104 GLU   B O   
995  C CB  . GLU   B 95  ? 0.9181 0.6017 0.2912 0.3248  0.1418  0.1963  104 GLU   B CB  
996  C CG  . GLU   B 95  ? 0.9895 0.6726 0.3569 0.3011  0.1578  0.2182  104 GLU   B CG  
997  C CD  . GLU   B 95  ? 1.0551 0.7874 0.4446 0.2925  0.1681  0.2271  104 GLU   B CD  
998  O OE1 . GLU   B 95  ? 1.0606 0.8220 0.4614 0.3104  0.1629  0.2175  104 GLU   B OE1 
999  O OE2 . GLU   B 95  ? 1.0807 0.8228 0.4751 0.2681  0.1806  0.2433  104 GLU   B OE2 
1000 N N   . ARG   B 96  ? 0.8892 0.5413 0.2449 0.3762  0.1100  0.1580  105 ARG   B N   
1001 C CA  . ARG   B 96  ? 0.8878 0.5510 0.2526 0.3957  0.0949  0.1384  105 ARG   B CA  
1002 C C   . ARG   B 96  ? 0.8569 0.5593 0.2503 0.3914  0.0914  0.1320  105 ARG   B C   
1003 O O   . ARG   B 96  ? 0.8511 0.5707 0.2469 0.3861  0.1005  0.1435  105 ARG   B O   
1004 C CB  . ARG   B 96  ? 0.9407 0.5847 0.2732 0.4264  0.0906  0.1381  105 ARG   B CB  
1005 C CG  . ARG   B 96  ? 0.9992 0.6547 0.3379 0.4488  0.0738  0.1185  105 ARG   B CG  
1006 C CD  . ARG   B 96  ? 1.0846 0.7116 0.3886 0.4784  0.0675  0.1156  105 ARG   B CD  
1007 N NE  . ARG   B 96  ? 1.1593 0.7726 0.4328 0.4908  0.0774  0.1321  105 ARG   B NE  
1008 C CZ  . ARG   B 96  ? 1.2287 0.8062 0.4677 0.4937  0.0868  0.1462  105 ARG   B CZ  
1009 N NH1 . ARG   B 96  ? 1.2425 0.7907 0.4711 0.4859  0.0861  0.1452  105 ARG   B NH1 
1010 N NH2 . ARG   B 96  ? 1.2390 0.8080 0.4506 0.5049  0.0967  0.1616  105 ARG   B NH2 
1011 N N   . ALA   B 97  ? 0.8380 0.5543 0.2511 0.3939  0.0781  0.1139  106 ALA   B N   
1012 C CA  . ALA   B 97  ? 0.8225 0.5683 0.2574 0.3901  0.0718  0.1063  106 ALA   B CA  
1013 C C   . ALA   B 97  ? 0.8305 0.5827 0.2495 0.4100  0.0707  0.1110  106 ALA   B C   
1014 O O   . ALA   B 97  ? 0.8447 0.5812 0.2403 0.4328  0.0670  0.1106  106 ALA   B O   
1015 C CB  . ALA   B 97  ? 0.8145 0.5685 0.2652 0.3925  0.0571  0.0872  106 ALA   B CB  
1016 N N   . LYS   B 98  ? 0.8226 0.5965 0.2515 0.4037  0.0731  0.1147  107 LYS   B N   
1017 C CA  . LYS   B 98  ? 0.8320 0.6136 0.2437 0.4236  0.0729  0.1200  107 LYS   B CA  
1018 C C   . LYS   B 98  ? 0.8172 0.6187 0.2411 0.4220  0.0633  0.1118  107 LYS   B C   
1019 O O   . LYS   B 98  ? 0.8114 0.6281 0.2543 0.4020  0.0678  0.1134  107 LYS   B O   
1020 C CB  . LYS   B 98  ? 0.8708 0.6578 0.2735 0.4180  0.0917  0.1400  107 LYS   B CB  
1021 C CG  . LYS   B 98  ? 0.9552 0.7522 0.3363 0.4401  0.0960  0.1490  107 LYS   B CG  
1022 C CD  . LYS   B 98  ? 1.0278 0.8421 0.4088 0.4275  0.1163  0.1690  107 LYS   B CD  
1023 C CE  . LYS   B 98  ? 1.0682 0.9040 0.4798 0.3979  0.1215  0.1702  107 LYS   B CE  
1024 N NZ  . LYS   B 98  ? 1.0911 0.9553 0.5059 0.3886  0.1384  0.1873  107 LYS   B NZ  
1025 N N   . ASN   B 99  ? 0.8131 0.6114 0.2237 0.4432  0.0488  0.1027  108 ASN   B N   
1026 C CA  . ASN   B 99  ? 0.8076 0.6167 0.2223 0.4435  0.0372  0.0946  108 ASN   B CA  
1027 C C   . ASN   B 99  ? 0.8121 0.6346 0.2114 0.4571  0.0434  0.1047  108 ASN   B C   
1028 O O   . ASN   B 99  ? 0.8327 0.6506 0.2078 0.4813  0.0447  0.1102  108 ASN   B O   
1029 C CB  . ASN   B 99  ? 0.8193 0.6160 0.2247 0.4585  0.0162  0.0796  108 ASN   B CB  
1030 C CG  . ASN   B 99  ? 0.8394 0.6312 0.2624 0.4464  0.0080  0.0675  108 ASN   B CG  
1031 O OD1 . ASN   B 99  ? 0.8567 0.6432 0.2831 0.4445  0.0154  0.0696  108 ASN   B OD1 
1032 N ND2 . ASN   B 99  ? 0.8317 0.6249 0.2638 0.4389  -0.0080 0.0544  108 ASN   B ND2 
1033 N N   . ILE   B 100 ? 0.7982 0.6385 0.2099 0.4439  0.0465  0.1063  109 ILE   B N   
1034 C CA  . ILE   B 100 ? 0.7996 0.6588 0.1983 0.4579  0.0518  0.1144  109 ILE   B CA  
1035 C C   . ILE   B 100 ? 0.8068 0.6646 0.1993 0.4641  0.0346  0.1026  109 ILE   B C   
1036 O O   . ILE   B 100 ? 0.8009 0.6596 0.2108 0.4435  0.0300  0.0959  109 ILE   B O   
1037 C CB  . ILE   B 100 ? 0.7910 0.6754 0.2082 0.4383  0.0709  0.1273  109 ILE   B CB  
1038 C CG1 . ILE   B 100 ? 0.8052 0.6833 0.2271 0.4264  0.0866  0.1391  109 ILE   B CG1 
1039 C CG2 . ILE   B 100 ? 0.7877 0.7000 0.1936 0.4543  0.0770  0.1351  109 ILE   B CG2 
1040 C CD1 . ILE   B 100 ? 0.8302 0.7056 0.2269 0.4476  0.0960  0.1512  109 ILE   B CD1 
1041 N N   . GLN   B 101 ? 0.8203 0.6726 0.1847 0.4928  0.0243  0.1001  110 GLN   B N   
1042 C CA  . GLN   B 101 ? 0.8403 0.6837 0.1905 0.5016  0.0052  0.0887  110 GLN   B CA  
1043 C C   . GLN   B 101 ? 0.8420 0.7106 0.1867 0.5093  0.0114  0.0943  110 GLN   B C   
1044 O O   . GLN   B 101 ? 0.8374 0.7295 0.1758 0.5234  0.0264  0.1064  110 GLN   B O   
1045 C CB  . GLN   B 101 ? 0.8804 0.7000 0.1993 0.5303  -0.0130 0.0811  110 GLN   B CB  
1046 C CG  . GLN   B 101 ? 0.9317 0.7297 0.2356 0.5327  -0.0373 0.0670  110 GLN   B CG  
1047 C CD  . GLN   B 101 ? 0.9857 0.7574 0.2603 0.5579  -0.0569 0.0589  110 GLN   B CD  
1048 O OE1 . GLN   B 101 ? 0.9943 0.7574 0.2726 0.5597  -0.0579 0.0574  110 GLN   B OE1 
1049 N NE2 . GLN   B 101 ? 1.0080 0.7647 0.2509 0.5788  -0.0742 0.0528  110 GLN   B NE2 
1050 N N   . THR   B 102 ? 0.8432 0.7080 0.1893 0.5002  0.0002  0.0855  111 THR   B N   
1051 C CA  . THR   B 102 ? 0.8430 0.7311 0.1829 0.5087  0.0029  0.0877  111 THR   B CA  
1052 C C   . THR   B 102 ? 0.8604 0.7247 0.1827 0.5105  -0.0195 0.0738  111 THR   B C   
1053 O O   . THR   B 102 ? 0.8728 0.7062 0.1950 0.4966  -0.0337 0.0642  111 THR   B O   
1054 C CB  . THR   B 102 ? 0.8417 0.7608 0.2160 0.4821  0.0230  0.0967  111 THR   B CB  
1055 O OG1 . THR   B 102 ? 0.8476 0.7969 0.2172 0.4935  0.0267  0.0992  111 THR   B OG1 
1056 C CG2 . THR   B 102 ? 0.8453 0.7492 0.2431 0.4498  0.0191  0.0894  111 THR   B CG2 
1057 N N   . LEU   B 103 ? 0.8568 0.7355 0.1626 0.5271  -0.0227 0.0726  112 LEU   B N   
1058 C CA  . LEU   B 103 ? 0.8715 0.7244 0.1568 0.5280  -0.0435 0.0601  112 LEU   B CA  
1059 C C   . LEU   B 103 ? 0.8601 0.7368 0.1706 0.5065  -0.0329 0.0619  112 LEU   B C   
1060 O O   . LEU   B 103 ? 0.8486 0.7651 0.1667 0.5159  -0.0194 0.0690  112 LEU   B O   
1061 C CB  . LEU   B 103 ? 0.8853 0.7310 0.1263 0.5671  -0.0589 0.0550  112 LEU   B CB  
1062 C CG  . LEU   B 103 ? 0.9187 0.7298 0.1327 0.5675  -0.0822 0.0420  112 LEU   B CG  
1063 C CD1 . LEU   B 103 ? 0.9490 0.7071 0.1401 0.5636  -0.1055 0.0322  112 LEU   B CD1 
1064 C CD2 . LEU   B 103 ? 0.9349 0.7557 0.1139 0.6034  -0.0904 0.0387  112 LEU   B CD2 
1065 N N   . PRO   B 104 ? 0.8583 0.7140 0.1827 0.4776  -0.0383 0.0557  113 PRO   B N   
1066 C CA  . PRO   B 104 ? 0.8432 0.7202 0.1908 0.4579  -0.0285 0.0570  113 PRO   B CA  
1067 C C   . PRO   B 104 ? 0.8569 0.7372 0.1797 0.4764  -0.0391 0.0507  113 PRO   B C   
1068 O O   . PRO   B 104 ? 0.8824 0.7342 0.1654 0.4994  -0.0590 0.0425  113 PRO   B O   
1069 C CB  . PRO   B 104 ? 0.8507 0.7019 0.2158 0.4246  -0.0318 0.0519  113 PRO   B CB  
1070 C CG  . PRO   B 104 ? 0.8735 0.6923 0.2245 0.4265  -0.0448 0.0470  113 PRO   B CG  
1071 C CD  . PRO   B 104 ? 0.8664 0.6821 0.1874 0.4609  -0.0525 0.0476  113 PRO   B CD  
1072 N N   . GLY   B 105 ? 0.8348 0.7512 0.1802 0.4681  -0.0261 0.0547  114 GLY   B N   
1073 C CA  . GLY   B 105 ? 0.8382 0.7652 0.1668 0.4829  -0.0339 0.0483  114 GLY   B CA  
1074 C C   . GLY   B 105 ? 0.8409 0.7394 0.1710 0.4592  -0.0429 0.0399  114 GLY   B C   
1075 O O   . GLY   B 105 ? 0.8507 0.7148 0.1849 0.4366  -0.0475 0.0374  114 GLY   B O   
1076 N N   . ILE   B 106 ? 0.8326 0.7471 0.1589 0.4647  -0.0453 0.0353  115 ILE   B N   
1077 C CA  . ILE   B 106 ? 0.8453 0.7314 0.1667 0.4462  -0.0547 0.0269  115 ILE   B CA  
1078 C C   . ILE   B 106 ? 0.8214 0.7464 0.1771 0.4303  -0.0409 0.0293  115 ILE   B C   
1079 O O   . ILE   B 106 ? 0.7995 0.7735 0.1685 0.4440  -0.0313 0.0334  115 ILE   B O   
1080 C CB  . ILE   B 106 ? 0.8834 0.7349 0.1513 0.4737  -0.0791 0.0149  115 ILE   B CB  
1081 C CG1 . ILE   B 106 ? 0.9236 0.7274 0.1533 0.4866  -0.0969 0.0111  115 ILE   B CG1 
1082 C CG2 . ILE   B 106 ? 0.9072 0.7304 0.1629 0.4597  -0.0892 0.0062  115 ILE   B CG2 
1083 C CD1 . ILE   B 106 ? 0.9498 0.7126 0.1840 0.4564  -0.1014 0.0101  115 ILE   B CD1 
1084 N N   . PHE   B 107 ? 0.8264 0.7296 0.1947 0.4017  -0.0408 0.0264  116 PHE   B N   
1085 C CA  . PHE   B 107 ? 0.8186 0.7466 0.2129 0.3858  -0.0325 0.0260  116 PHE   B CA  
1086 C C   . PHE   B 107 ? 0.8513 0.7433 0.2104 0.3919  -0.0511 0.0137  116 PHE   B C   
1087 O O   . PHE   B 107 ? 0.8730 0.7205 0.2205 0.3736  -0.0583 0.0099  116 PHE   B O   
1088 C CB  . PHE   B 107 ? 0.8059 0.7283 0.2349 0.3501  -0.0201 0.0312  116 PHE   B CB  
1089 C CG  . PHE   B 107 ? 0.7864 0.7483 0.2552 0.3382  0.0001  0.0433  116 PHE   B CG  
1090 C CD1 . PHE   B 107 ? 0.7829 0.7830 0.2565 0.3567  0.0082  0.0508  116 PHE   B CD1 
1091 C CD2 . PHE   B 107 ? 0.7858 0.7438 0.2836 0.3090  0.0106  0.0474  116 PHE   B CD2 
1092 C CE1 . PHE   B 107 ? 0.7706 0.8021 0.2768 0.3436  0.0267  0.0631  116 PHE   B CE1 
1093 C CE2 . PHE   B 107 ? 0.7761 0.7631 0.3046 0.2980  0.0274  0.0586  116 PHE   B CE2 
1094 C CZ  . PHE   B 107 ? 0.7643 0.7861 0.2963 0.3141  0.0354  0.0668  116 PHE   B CZ  
1095 N N   . LYS   B 108 ? 0.8552 0.7647 0.1940 0.4188  -0.0595 0.0074  117 LYS   B N   
1096 C CA  . LYS   B 108 ? 0.8889 0.7606 0.1877 0.4286  -0.0787 -0.0049 117 LYS   B CA  
1097 C C   . LYS   B 108 ? 0.8875 0.7643 0.2082 0.4055  -0.0735 -0.0075 117 LYS   B C   
1098 O O   . LYS   B 108 ? 0.8651 0.7913 0.2130 0.4081  -0.0646 -0.0067 117 LYS   B O   
1099 C CB  . LYS   B 108 ? 0.9228 0.8136 0.1901 0.4696  -0.0904 -0.0121 117 LYS   B CB  
1100 C CG  . LYS   B 108 ? 1.0120 0.8880 0.2467 0.4971  -0.0998 -0.0117 117 LYS   B CG  
1101 C CD  . LYS   B 108 ? 1.1052 1.0027 0.3063 0.5419  -0.1115 -0.0194 117 LYS   B CD  
1102 C CE  . LYS   B 108 ? 1.2044 1.0872 0.3725 0.5705  -0.1205 -0.0187 117 LYS   B CE  
1103 N NZ  . LYS   B 108 ? 1.2408 1.1615 0.3851 0.6164  -0.1265 -0.0238 117 LYS   B NZ  
1104 N N   . THR   B 109 ? 0.9063 0.7341 0.2162 0.3821  -0.0787 -0.0102 118 THR   B N   
1105 C CA  . THR   B 109 ? 0.9030 0.7297 0.2290 0.3611  -0.0747 -0.0130 118 THR   B CA  
1106 C C   . THR   B 109 ? 0.9368 0.7116 0.2138 0.3678  -0.0940 -0.0243 118 THR   B C   
1107 O O   . THR   B 109 ? 0.9676 0.6999 0.1980 0.3833  -0.1108 -0.0290 118 THR   B O   
1108 C CB  . THR   B 109 ? 0.9057 0.7290 0.2685 0.3250  -0.0594 -0.0052 118 THR   B CB  
1109 O OG1 . THR   B 109 ? 0.9395 0.7086 0.2778 0.3096  -0.0674 -0.0073 118 THR   B OG1 
1110 C CG2 . THR   B 109 ? 0.8863 0.7453 0.2854 0.3199  -0.0436 0.0058  118 THR   B CG2 
1111 N N   . LYS   B 110 ? 0.9293 0.7041 0.2140 0.3561  -0.0927 -0.0287 119 LYS   B N   
1112 C CA  . LYS   B 110 ? 0.9645 0.6875 0.2033 0.3590  -0.1092 -0.0385 119 LYS   B CA  
1113 C C   . LYS   B 110 ? 0.9975 0.6613 0.2156 0.3333  -0.1124 -0.0359 119 LYS   B C   
1114 O O   . LYS   B 110 ? 1.0357 0.6455 0.2054 0.3353  -0.1279 -0.0424 119 LYS   B O   
1115 C CB  . LYS   B 110 ? 0.9619 0.7051 0.2184 0.3532  -0.1055 -0.0434 119 LYS   B CB  
1116 C CG  . LYS   B 110 ? 0.9862 0.7333 0.2815 0.3181  -0.0898 -0.0371 119 LYS   B CG  
1117 C CD  . LYS   B 110 ? 1.0267 0.7948 0.3386 0.3150  -0.0879 -0.0427 119 LYS   B CD  
1118 C CE  . LYS   B 110 ? 1.0635 0.8209 0.3997 0.2835  -0.0767 -0.0388 119 LYS   B CE  
1119 N NZ  . LYS   B 110 ? 1.0523 0.8598 0.4448 0.2685  -0.0594 -0.0305 119 LYS   B NZ  
1120 N N   . ASP   B 111 ? 0.9770 0.6517 0.2302 0.3094  -0.0980 -0.0265 120 ASP   B N   
1121 C CA  . ASP   B 111 ? 0.9927 0.6254 0.2359 0.2837  -0.0984 -0.0234 120 ASP   B CA  
1122 C C   . ASP   B 111 ? 0.9949 0.6181 0.2328 0.2854  -0.1016 -0.0190 120 ASP   B C   
1123 O O   . ASP   B 111 ? 0.9975 0.6091 0.2483 0.2616  -0.0958 -0.0143 120 ASP   B O   
1124 C CB  . ASP   B 111 ? 0.9900 0.6438 0.2782 0.2548  -0.0799 -0.0179 120 ASP   B CB  
1125 C CG  . ASP   B 111 ? 1.0471 0.7006 0.3370 0.2491  -0.0782 -0.0225 120 ASP   B CG  
1126 O OD1 . ASP   B 111 ? 1.0813 0.6972 0.3277 0.2576  -0.0924 -0.0299 120 ASP   B OD1 
1127 O OD2 . ASP   B 111 ? 1.0522 0.7394 0.3837 0.2365  -0.0637 -0.0190 120 ASP   B OD2 
1128 N N   . GLY   B 112 ? 0.9910 0.6218 0.2109 0.3143  -0.1106 -0.0210 121 GLY   B N   
1129 C CA  . GLY   B 112 ? 0.9955 0.6141 0.2055 0.3196  -0.1162 -0.0179 121 GLY   B CA  
1130 C C   . GLY   B 112 ? 0.9582 0.6269 0.2024 0.3326  -0.1041 -0.0116 121 GLY   B C   
1131 O O   . GLY   B 112 ? 0.9297 0.6465 0.2157 0.3291  -0.0872 -0.0069 121 GLY   B O   
1132 N N   . ASP   B 113 ? 0.9589 0.6137 0.1833 0.3471  -0.1133 -0.0110 122 ASP   B N   
1133 C CA  . ASP   B 113 ? 0.9320 0.6291 0.1828 0.3611  -0.1025 -0.0045 122 ASP   B CA  
1134 C C   . ASP   B 113 ? 0.9029 0.6122 0.1929 0.3357  -0.0879 0.0032  122 ASP   B C   
1135 O O   . ASP   B 113 ? 0.9073 0.5862 0.1948 0.3124  -0.0914 0.0024  122 ASP   B O   
1136 C CB  . ASP   B 113 ? 0.9711 0.6498 0.1810 0.3928  -0.1193 -0.0080 122 ASP   B CB  
1137 C CG  . ASP   B 113 ? 1.0512 0.7254 0.2217 0.4257  -0.1335 -0.0160 122 ASP   B CG  
1138 O OD1 . ASP   B 113 ? 1.0576 0.7426 0.2318 0.4237  -0.1312 -0.0196 122 ASP   B OD1 
1139 O OD2 . ASP   B 113 ? 1.1036 0.7628 0.2375 0.4552  -0.1481 -0.0195 122 ASP   B OD2 
1140 N N   . ILE   B 114 ? 0.8658 0.6217 0.1916 0.3404  -0.0712 0.0109  123 ILE   B N   
1141 C CA  . ILE   B 114 ? 0.8416 0.6121 0.2028 0.3218  -0.0571 0.0181  123 ILE   B CA  
1142 C C   . ILE   B 114 ? 0.8238 0.6215 0.1906 0.3437  -0.0516 0.0242  123 ILE   B C   
1143 O O   . ILE   B 114 ? 0.8127 0.6407 0.1792 0.3638  -0.0475 0.0263  123 ILE   B O   
1144 C CB  . ILE   B 114 ? 0.8199 0.6173 0.2223 0.2984  -0.0391 0.0226  123 ILE   B CB  
1145 C CG1 . ILE   B 114 ? 0.8467 0.6235 0.2405 0.2835  -0.0439 0.0165  123 ILE   B CG1 
1146 C CG2 . ILE   B 114 ? 0.8109 0.6136 0.2425 0.2792  -0.0277 0.0280  123 ILE   B CG2 
1147 C CD1 . ILE   B 114 ? 0.8544 0.6583 0.2588 0.2886  -0.0387 0.0159  123 ILE   B CD1 
1148 N N   . GLY   B 115 ? 0.8207 0.6094 0.1920 0.3404  -0.0512 0.0268  124 GLY   B N   
1149 C CA  . GLY   B 115 ? 0.8184 0.6297 0.1936 0.3604  -0.0452 0.0331  124 GLY   B CA  
1150 C C   . GLY   B 115 ? 0.7907 0.6455 0.2045 0.3528  -0.0229 0.0431  124 GLY   B C   
1151 O O   . GLY   B 115 ? 0.7827 0.6433 0.2234 0.3281  -0.0131 0.0448  124 GLY   B O   
1152 N N   . ALA   B 116 ? 0.7746 0.6587 0.1893 0.3736  -0.0151 0.0501  125 ALA   B N   
1153 C CA  . ALA   B 116 ? 0.7523 0.6759 0.2007 0.3644  0.0058  0.0612  125 ALA   B CA  
1154 C C   . ALA   B 116 ? 0.7453 0.6866 0.1936 0.3808  0.0150  0.0706  125 ALA   B C   
1155 O O   . ALA   B 116 ? 0.7574 0.7039 0.1814 0.4085  0.0090  0.0702  125 ALA   B O   
1156 C CB  . ALA   B 116 ? 0.7384 0.6946 0.1958 0.3662  0.0109  0.0619  125 ALA   B CB  
1157 N N   . VAL   B 117 ? 0.7259 0.6740 0.1984 0.3646  0.0290  0.0789  126 VAL   B N   
1158 C CA  A VAL   B 117 ? 0.7235 0.6845 0.1947 0.3776  0.0390  0.0890  126 VAL   B CA  
1159 C CA  B VAL   B 117 ? 0.7243 0.6845 0.1964 0.3764  0.0392  0.0890  126 VAL   B CA  
1160 C C   . VAL   B 117 ? 0.7049 0.7093 0.1951 0.3747  0.0576  0.1016  126 VAL   B C   
1161 O O   . VAL   B 117 ? 0.7007 0.7180 0.2166 0.3507  0.0669  0.1051  126 VAL   B O   
1162 C CB  A VAL   B 117 ? 0.7372 0.6743 0.2149 0.3669  0.0408  0.0900  126 VAL   B CB  
1163 C CB  B VAL   B 117 ? 0.7384 0.6746 0.2215 0.3604  0.0415  0.0894  126 VAL   B CB  
1164 C CG1 A VAL   B 117 ? 0.7634 0.6654 0.2196 0.3750  0.0217  0.0784  126 VAL   B CG1 
1165 C CG1 B VAL   B 117 ? 0.7352 0.6871 0.2339 0.3539  0.0596  0.1027  126 VAL   B CG1 
1166 C CG2 A VAL   B 117 ? 0.7335 0.6686 0.2395 0.3364  0.0495  0.0914  126 VAL   B CG2 
1167 C CG2 B VAL   B 117 ? 0.7630 0.6690 0.2224 0.3755  0.0260  0.0816  126 VAL   B CG2 
1168 N N   . ALA   B 118 ? 0.6903 0.7190 0.1666 0.3993  0.0622  0.1081  127 ALA   B N   
1169 C CA  . ALA   B 118 ? 0.6657 0.7413 0.1592 0.3968  0.0803  0.1211  127 ALA   B CA  
1170 C C   . ALA   B 118 ? 0.6679 0.7424 0.1654 0.3921  0.0948  0.1345  127 ALA   B C   
1171 O O   . ALA   B 118 ? 0.6773 0.7622 0.1568 0.4151  0.0991  0.1410  127 ALA   B O   
1172 C CB  . ALA   B 118 ? 0.6572 0.7649 0.1320 0.4278  0.0778  0.1205  127 ALA   B CB  
1173 N N   . LEU   B 119 ? 0.6605 0.7162 0.1767 0.3647  0.1006  0.1375  128 LEU   B N   
1174 C CA  . LEU   B 119 ? 0.6604 0.7058 0.1767 0.3587  0.1125  0.1492  128 LEU   B CA  
1175 C C   . LEU   B 119 ? 0.6524 0.7045 0.1950 0.3263  0.1249  0.1577  128 LEU   B C   
1176 O O   . LEU   B 119 ? 0.6621 0.6996 0.2192 0.3072  0.1189  0.1496  128 LEU   B O   
1177 C CB  . LEU   B 119 ? 0.6761 0.6768 0.1782 0.3642  0.1013  0.1409  128 LEU   B CB  
1178 C CG  . LEU   B 119 ? 0.7019 0.6897 0.1746 0.3960  0.0882  0.1338  128 LEU   B CG  
1179 C CD1 . LEU   B 119 ? 0.7201 0.6684 0.1853 0.3961  0.0749  0.1233  128 LEU   B CD1 
1180 C CD2 . LEU   B 119 ? 0.7093 0.7144 0.1646 0.4184  0.0987  0.1461  128 LEU   B CD2 
1181 N N   . ASP   B 120 ? 0.6379 0.7119 0.1853 0.3195  0.1416  0.1740  129 ASP   B N   
1182 C CA  . ASP   B 120 ? 0.6344 0.7115 0.2038 0.2873  0.1522  0.1831  129 ASP   B CA  
1183 C C   . ASP   B 120 ? 0.6449 0.6814 0.2054 0.2773  0.1559  0.1888  129 ASP   B C   
1184 O O   . ASP   B 120 ? 0.6618 0.6904 0.2028 0.2907  0.1623  0.1977  129 ASP   B O   
1185 C CB  . ASP   B 120 ? 0.6467 0.7740 0.2294 0.2792  0.1676  0.1976  129 ASP   B CB  
1186 C CG  . ASP   B 120 ? 0.7258 0.8694 0.3377 0.2473  0.1709  0.1994  129 ASP   B CG  
1187 O OD1 . ASP   B 120 ? 0.7444 0.8525 0.3628 0.2286  0.1645  0.1933  129 ASP   B OD1 
1188 O OD2 . ASP   B 120 ? 0.7486 0.9420 0.3767 0.2418  0.1793  0.2063  129 ASP   B OD2 
1189 N N   . TYR   B 121 ? 0.6387 0.6479 0.2102 0.2564  0.1508  0.1828  130 TYR   B N   
1190 C CA  . TYR   B 121 ? 0.6489 0.6167 0.2111 0.2476  0.1515  0.1853  130 TYR   B CA  
1191 C C   . TYR   B 121 ? 0.6347 0.5933 0.2143 0.2168  0.1537  0.1874  130 TYR   B C   
1192 O O   . TYR   B 121 ? 0.6237 0.5972 0.2224 0.2057  0.1487  0.1797  130 TYR   B O   
1193 C CB  . TYR   B 121 ? 0.6657 0.6024 0.2175 0.2625  0.1371  0.1694  130 TYR   B CB  
1194 C CG  . TYR   B 121 ? 0.6876 0.6189 0.2162 0.2914  0.1343  0.1690  130 TYR   B CG  
1195 C CD1 . TYR   B 121 ? 0.7113 0.6174 0.2203 0.2994  0.1383  0.1756  130 TYR   B CD1 
1196 C CD2 . TYR   B 121 ? 0.6962 0.6452 0.2189 0.3121  0.1266  0.1619  130 TYR   B CD2 
1197 C CE1 . TYR   B 121 ? 0.7345 0.6353 0.2208 0.3272  0.1352  0.1751  130 TYR   B CE1 
1198 C CE2 . TYR   B 121 ? 0.7165 0.6591 0.2156 0.3396  0.1229  0.1615  130 TYR   B CE2 
1199 C CZ  . TYR   B 121 ? 0.7416 0.6613 0.2235 0.3470  0.1275  0.1681  130 TYR   B CZ  
1200 O OH  . TYR   B 121 ? 0.7712 0.6836 0.2283 0.3755  0.1233  0.1675  130 TYR   B OH  
1201 N N   . PRO   B 122 ? 0.6294 0.5584 0.1990 0.2041  0.1594  0.1969  131 PRO   B N   
1202 C CA  . PRO   B 122 ? 0.6139 0.5275 0.1953 0.1752  0.1596  0.1989  131 PRO   B CA  
1203 C C   . PRO   B 122 ? 0.5974 0.4945 0.1889 0.1718  0.1468  0.1817  131 PRO   B C   
1204 O O   . PRO   B 122 ? 0.6059 0.4879 0.1889 0.1893  0.1384  0.1700  131 PRO   B O   
1205 C CB  . PRO   B 122 ? 0.6504 0.5234 0.2082 0.1706  0.1642  0.2094  131 PRO   B CB  
1206 C CG  . PRO   B 122 ? 0.6762 0.5382 0.2111 0.2000  0.1632  0.2076  131 PRO   B CG  
1207 C CD  . PRO   B 122 ? 0.6408 0.5457 0.1836 0.2166  0.1649  0.2062  131 PRO   B CD  
1208 N N   . ALA   B 123 ? 0.5723 0.4734 0.1815 0.1487  0.1453  0.1805  132 ALA   B N   
1209 C CA  . ALA   B 123 ? 0.5620 0.4515 0.1818 0.1429  0.1346  0.1654  132 ALA   B CA  
1210 C C   . ALA   B 123 ? 0.5706 0.4237 0.1767 0.1541  0.1263  0.1541  132 ALA   B C   
1211 O O   . ALA   B 123 ? 0.5699 0.4243 0.1827 0.1592  0.1181  0.1404  132 ALA   B O   
1212 C CB  . ALA   B 123 ? 0.5578 0.4436 0.1904 0.1156  0.1350  0.1693  132 ALA   B CB  
1213 N N   . GLY   B 124 ? 0.5769 0.3998 0.1630 0.1584  0.1286  0.1600  133 GLY   B N   
1214 C CA  . GLY   B 124 ? 0.5786 0.3708 0.1508 0.1714  0.1209  0.1494  133 GLY   B CA  
1215 C C   . GLY   B 124 ? 0.5552 0.3570 0.1234 0.1953  0.1161  0.1402  133 GLY   B C   
1216 O O   . GLY   B 124 ? 0.5556 0.3407 0.1170 0.2062  0.1091  0.1296  133 GLY   B O   
1217 N N   . THR   B 125 ? 0.5350 0.3645 0.1066 0.2044  0.1190  0.1436  134 THR   B N   
1218 C CA  . THR   B 125 ? 0.5326 0.3699 0.0990 0.2261  0.1123  0.1347  134 THR   B CA  
1219 C C   . THR   B 125 ? 0.5202 0.3686 0.1013 0.2234  0.1030  0.1204  134 THR   B C   
1220 O O   . THR   B 125 ? 0.5325 0.3807 0.1092 0.2372  0.0948  0.1108  134 THR   B O   
1221 C CB  . THR   B 125 ? 0.5441 0.4017 0.1023 0.2397  0.1181  0.1443  134 THR   B CB  
1222 O OG1 . THR   B 125 ? 0.5667 0.4121 0.1100 0.2390  0.1280  0.1588  134 THR   B OG1 
1223 C CG2 . THR   B 125 ? 0.5536 0.4119 0.1007 0.2637  0.1096  0.1357  134 THR   B CG2 
1224 N N   . SER   B 126 ? 0.4915 0.3477 0.0882 0.2049  0.1035  0.1190  135 SER   B N   
1225 C CA  . SER   B 126 ? 0.4748 0.3382 0.0820 0.2003  0.0959  0.1071  135 SER   B CA  
1226 C C   . SER   B 126 ? 0.4774 0.3255 0.0822 0.2049  0.0882  0.0950  135 SER   B C   
1227 O O   . SER   B 126 ? 0.4811 0.3121 0.0843 0.2009  0.0890  0.0935  135 SER   B O   
1228 C CB  . SER   B 126 ? 0.4776 0.3432 0.0984 0.1799  0.0979  0.1077  135 SER   B CB  
1229 O OG  . SER   B 126 ? 0.4936 0.3844 0.1223 0.1754  0.1016  0.1139  135 SER   B OG  
1230 N N   . GLY   B 127 ? 0.4733 0.3282 0.0768 0.2127  0.0804  0.0863  136 GLY   B N   
1231 C CA  . GLY   B 127 ? 0.4822 0.3300 0.0858 0.2154  0.0729  0.0748  136 GLY   B CA  
1232 C C   . GLY   B 127 ? 0.5006 0.3484 0.0934 0.2333  0.0669  0.0720  136 GLY   B C   
1233 O O   . GLY   B 127 ? 0.5093 0.3574 0.1034 0.2345  0.0586  0.0621  136 GLY   B O   
1234 N N   . SER   B 128 ? 0.5035 0.3512 0.0852 0.2467  0.0707  0.0809  137 SER   B N   
1235 C CA  . SER   B 128 ? 0.5196 0.3654 0.0877 0.2665  0.0647  0.0792  137 SER   B CA  
1236 C C   . SER   B 128 ? 0.5321 0.3829 0.0968 0.2706  0.0531  0.0709  137 SER   B C   
1237 O O   . SER   B 128 ? 0.5385 0.3966 0.1024 0.2672  0.0525  0.0725  137 SER   B O   
1238 C CB  . SER   B 128 ? 0.5385 0.3863 0.0939 0.2787  0.0724  0.0919  137 SER   B CB  
1239 O OG  . SER   B 128 ? 0.5670 0.4048 0.1214 0.2727  0.0823  0.1007  137 SER   B OG  
1240 N N   . PRO   B 129 ? 0.5326 0.3786 0.0936 0.2782  0.0427  0.0617  138 PRO   B N   
1241 C CA  . PRO   B 129 ? 0.5372 0.3822 0.0919 0.2791  0.0298  0.0539  138 PRO   B CA  
1242 C C   . PRO   B 129 ? 0.5535 0.3959 0.0878 0.2978  0.0236  0.0569  138 PRO   B C   
1243 O O   . PRO   B 129 ? 0.5666 0.4091 0.0900 0.3154  0.0274  0.0634  138 PRO   B O   
1244 C CB  . PRO   B 129 ? 0.5412 0.3846 0.1003 0.2796  0.0207  0.0435  138 PRO   B CB  
1245 C CG  . PRO   B 129 ? 0.5479 0.3897 0.1060 0.2919  0.0266  0.0467  138 PRO   B CG  
1246 C CD  . PRO   B 129 ? 0.5261 0.3672 0.0883 0.2849  0.0410  0.0569  138 PRO   B CD  
1247 N N   . ILE   B 130 ? 0.5574 0.3950 0.0832 0.2951  0.0131  0.0515  139 ILE   B N   
1248 C CA  . ILE   B 130 ? 0.5766 0.4075 0.0787 0.3140  0.0030  0.0513  139 ILE   B CA  
1249 C C   . ILE   B 130 ? 0.6002 0.4155 0.0932 0.3142  -0.0147 0.0404  139 ILE   B C   
1250 O O   . ILE   B 130 ? 0.5944 0.4056 0.0961 0.2947  -0.0200 0.0337  139 ILE   B O   
1251 C CB  . ILE   B 130 ? 0.5771 0.4115 0.0715 0.3130  0.0033  0.0536  139 ILE   B CB  
1252 C CG1 . ILE   B 130 ? 0.5736 0.4286 0.0800 0.3122  0.0207  0.0648  139 ILE   B CG1 
1253 C CG2 . ILE   B 130 ? 0.5950 0.4186 0.0599 0.3349  -0.0105 0.0510  139 ILE   B CG2 
1254 C CD1 . ILE   B 130 ? 0.5789 0.4427 0.0904 0.3012  0.0232  0.0650  139 ILE   B CD1 
1255 N N   . LEU   B 131 ? 0.6219 0.4299 0.0984 0.3352  -0.0234 0.0391  140 LEU   B N   
1256 C CA  . LEU   B 131 ? 0.6475 0.4426 0.1170 0.3364  -0.0409 0.0290  140 LEU   B CA  
1257 C C   . LEU   B 131 ? 0.6839 0.4587 0.1222 0.3529  -0.0587 0.0253  140 LEU   B C   
1258 O O   . LEU   B 131 ? 0.6941 0.4682 0.1136 0.3761  -0.0568 0.0310  140 LEU   B O   
1259 C CB  . LEU   B 131 ? 0.6449 0.4452 0.1193 0.3498  -0.0392 0.0283  140 LEU   B CB  
1260 C CG  . LEU   B 131 ? 0.6516 0.4655 0.1424 0.3487  -0.0205 0.0358  140 LEU   B CG  
1261 C CD1 . LEU   B 131 ? 0.6594 0.4708 0.1429 0.3692  -0.0213 0.0358  140 LEU   B CD1 
1262 C CD2 . LEU   B 131 ? 0.6517 0.4759 0.1684 0.3236  -0.0142 0.0322  140 LEU   B CD2 
1263 N N   . ASP   B 132 ? 0.7011 0.4595 0.1326 0.3422  -0.0767 0.0157  141 ASP   B N   
1264 C CA  . ASP   B 132 ? 0.7391 0.4712 0.1366 0.3582  -0.0975 0.0108  141 ASP   B CA  
1265 C C   . ASP   B 132 ? 0.7653 0.4922 0.1552 0.3762  -0.1092 0.0058  141 ASP   B C   
1266 O O   . ASP   B 132 ? 0.7480 0.4929 0.1594 0.3762  -0.1001 0.0062  141 ASP   B O   
1267 C CB  . ASP   B 132 ? 0.7647 0.4742 0.1506 0.3371  -0.1129 0.0042  141 ASP   B CB  
1268 C CG  . ASP   B 132 ? 0.8152 0.5293 0.2231 0.3090  -0.1177 -0.0025 141 ASP   B CG  
1269 O OD1 . ASP   B 132 ? 0.8063 0.5366 0.2323 0.3115  -0.1165 -0.0053 141 ASP   B OD1 
1270 O OD2 . ASP   B 132 ? 0.8668 0.5693 0.2727 0.2850  -0.1228 -0.0050 141 ASP   B OD2 
1271 N N   . LYS   B 133 ? 0.8040 0.5040 0.1608 0.3927  -0.1306 0.0004  142 LYS   B N   
1272 C CA  . LYS   B 133 ? 0.8330 0.5238 0.1774 0.4125  -0.1448 -0.0052 142 LYS   B CA  
1273 C C   . LYS   B 133 ? 0.8289 0.5312 0.2001 0.3938  -0.1504 -0.0135 142 LYS   B C   
1274 O O   . LYS   B 133 ? 0.8285 0.5323 0.1976 0.4108  -0.1572 -0.0176 142 LYS   B O   
1275 C CB  . LYS   B 133 ? 0.9000 0.5546 0.2013 0.4301  -0.1700 -0.0109 142 LYS   B CB  
1276 C CG  . LYS   B 133 ? 0.9931 0.6410 0.2647 0.4570  -0.1655 -0.0039 142 LYS   B CG  
1277 C CD  . LYS   B 133 ? 1.1096 0.7166 0.3331 0.4761  -0.1932 -0.0111 142 LYS   B CD  
1278 C CE  . LYS   B 133 ? 1.1815 0.7842 0.3745 0.5018  -0.1901 -0.0059 142 LYS   B CE  
1279 N NZ  . LYS   B 133 ? 1.2349 0.7936 0.3762 0.5229  -0.2190 -0.0139 142 LYS   B NZ  
1280 N N   . CYS   B 134 ? 0.8189 0.5325 0.2155 0.3605  -0.1465 -0.0158 143 CYS   B N   
1281 C CA  . CYS   B 134 ? 0.8129 0.5462 0.2384 0.3427  -0.1499 -0.0237 143 CYS   B CA  
1282 C C   . CYS   B 134 ? 0.7841 0.5507 0.2437 0.3358  -0.1273 -0.0201 143 CYS   B C   
1283 O O   . CYS   B 134 ? 0.7753 0.5635 0.2607 0.3207  -0.1282 -0.0269 143 CYS   B O   
1284 C CB  . CYS   B 134 ? 0.8396 0.5645 0.2686 0.3106  -0.1637 -0.0301 143 CYS   B CB  
1285 S SG  . CYS   B 134 ? 0.9794 0.6544 0.3604 0.3156  -0.1910 -0.0332 143 CYS   B SG  
1286 N N   . GLY   B 135 ? 0.7660 0.5374 0.2250 0.3468  -0.1083 -0.0099 144 GLY   B N   
1287 C CA  . GLY   B 135 ? 0.7361 0.5319 0.2221 0.3396  -0.0879 -0.0058 144 GLY   B CA  
1288 C C   . GLY   B 135 ? 0.7052 0.5120 0.2118 0.3089  -0.0801 -0.0059 144 GLY   B C   
1289 O O   . GLY   B 135 ? 0.6948 0.5219 0.2249 0.3001  -0.0667 -0.0053 144 GLY   B O   
1290 N N   . ARG   B 136 ? 0.6956 0.4864 0.1904 0.2936  -0.0890 -0.0068 145 ARG   B N   
1291 C CA  . ARG   B 136 ? 0.6803 0.4780 0.1902 0.2648  -0.0819 -0.0065 145 ARG   B CA  
1292 C C   . ARG   B 136 ? 0.6641 0.4628 0.1744 0.2662  -0.0648 0.0028  145 ARG   B C   
1293 O O   . ARG   B 136 ? 0.6837 0.4691 0.1731 0.2833  -0.0651 0.0082  145 ARG   B O   
1294 C CB  . ARG   B 136 ? 0.7086 0.4833 0.2006 0.2476  -0.0991 -0.0107 145 ARG   B CB  
1295 C CG  . ARG   B 136 ? 0.7535 0.5373 0.2581 0.2297  -0.1119 -0.0197 145 ARG   B CG  
1296 C CD  . ARG   B 136 ? 0.8387 0.5935 0.3209 0.2105  -0.1294 -0.0224 145 ARG   B CD  
1297 N NE  . ARG   B 136 ? 0.9385 0.6610 0.3865 0.2305  -0.1497 -0.0249 145 ARG   B NE  
1298 C CZ  . ARG   B 136 ? 1.0127 0.6974 0.4239 0.2357  -0.1607 -0.0229 145 ARG   B CZ  
1299 N NH1 . ARG   B 136 ? 1.0167 0.6914 0.4212 0.2218  -0.1531 -0.0185 145 ARG   B NH1 
1300 N NH2 . ARG   B 136 ? 1.0402 0.6958 0.4187 0.2571  -0.1801 -0.0260 145 ARG   B NH2 
1301 N N   . VAL   B 137 ? 0.6275 0.4437 0.1611 0.2494  -0.0503 0.0044  146 VAL   B N   
1302 C CA  . VAL   B 137 ? 0.6094 0.4271 0.1451 0.2489  -0.0351 0.0126  146 VAL   B CA  
1303 C C   . VAL   B 137 ? 0.6029 0.4041 0.1235 0.2377  -0.0395 0.0135  146 VAL   B C   
1304 O O   . VAL   B 137 ? 0.6008 0.3999 0.1262 0.2157  -0.0419 0.0097  146 VAL   B O   
1305 C CB  . VAL   B 137 ? 0.5964 0.4337 0.1576 0.2386  -0.0191 0.0141  146 VAL   B CB  
1306 C CG1 . VAL   B 137 ? 0.5993 0.4363 0.1602 0.2425  -0.0055 0.0234  146 VAL   B CG1 
1307 C CG2 . VAL   B 137 ? 0.5946 0.4455 0.1673 0.2498  -0.0177 0.0109  146 VAL   B CG2 
1308 N N   . ILE   B 138 ? 0.5948 0.3850 0.0952 0.2542  -0.0405 0.0186  147 ILE   B N   
1309 C CA  . ILE   B 138 ? 0.5905 0.3640 0.0718 0.2499  -0.0457 0.0189  147 ILE   B CA  
1310 C C   . ILE   B 138 ? 0.5680 0.3538 0.0607 0.2449  -0.0303 0.0249  147 ILE   B C   
1311 O O   . ILE   B 138 ? 0.5742 0.3482 0.0515 0.2427  -0.0341 0.0245  147 ILE   B O   
1312 C CB  . ILE   B 138 ? 0.6028 0.3569 0.0578 0.2727  -0.0582 0.0167  147 ILE   B CB  
1313 C CG1 . ILE   B 138 ? 0.6053 0.3748 0.0596 0.2981  -0.0492 0.0235  147 ILE   B CG1 
1314 C CG2 . ILE   B 138 ? 0.6219 0.3548 0.0618 0.2714  -0.0774 0.0089  147 ILE   B CG2 
1315 C CD1 . ILE   B 138 ? 0.6358 0.3932 0.0628 0.3219  -0.0575 0.0229  147 ILE   B CD1 
1316 N N   . GLY   B 139 ? 0.5430 0.3494 0.0598 0.2430  -0.0147 0.0295  148 GLY   B N   
1317 C CA  . GLY   B 139 ? 0.5393 0.3568 0.0685 0.2360  -0.0014 0.0348  148 GLY   B CA  
1318 C C   . GLY   B 139 ? 0.5310 0.3651 0.0775 0.2408  0.0131  0.0419  148 GLY   B C   
1319 O O   . GLY   B 139 ? 0.5376 0.3740 0.0845 0.2522  0.0132  0.0430  148 GLY   B O   
1320 N N   . LEU   B 140 ? 0.5190 0.3622 0.0778 0.2321  0.0242  0.0468  149 LEU   B N   
1321 C CA  . LEU   B 140 ? 0.5165 0.3704 0.0881 0.2340  0.0372  0.0547  149 LEU   B CA  
1322 C C   . LEU   B 140 ? 0.5198 0.3859 0.0899 0.2396  0.0442  0.0635  149 LEU   B C   
1323 O O   . LEU   B 140 ? 0.5221 0.3914 0.0892 0.2361  0.0416  0.0620  149 LEU   B O   
1324 C CB  . LEU   B 140 ? 0.5110 0.3654 0.1001 0.2170  0.0444  0.0532  149 LEU   B CB  
1325 C CG  . LEU   B 140 ? 0.5288 0.3798 0.1239 0.2097  0.0400  0.0445  149 LEU   B CG  
1326 C CD1 . LEU   B 140 ? 0.5362 0.3890 0.1456 0.1970  0.0480  0.0435  149 LEU   B CD1 
1327 C CD2 . LEU   B 140 ? 0.5330 0.3843 0.1246 0.2233  0.0358  0.0425  149 LEU   B CD2 
1328 N N   . TYR   B 141 ? 0.5205 0.3945 0.0921 0.2482  0.0531  0.0727  150 TYR   B N   
1329 C CA  . TYR   B 141 ? 0.5246 0.4164 0.0977 0.2521  0.0622  0.0831  150 TYR   B CA  
1330 C C   . TYR   B 141 ? 0.5063 0.4024 0.0971 0.2331  0.0722  0.0881  150 TYR   B C   
1331 O O   . TYR   B 141 ? 0.5064 0.3898 0.1027 0.2255  0.0750  0.0877  150 TYR   B O   
1332 C CB  . TYR   B 141 ? 0.5431 0.4377 0.1058 0.2694  0.0671  0.0915  150 TYR   B CB  
1333 C CG  . TYR   B 141 ? 0.5666 0.4810 0.1333 0.2694  0.0804  0.1050  150 TYR   B CG  
1334 C CD1 . TYR   B 141 ? 0.5814 0.4926 0.1583 0.2552  0.0912  0.1134  150 TYR   B CD1 
1335 C CD2 . TYR   B 141 ? 0.5903 0.5261 0.1483 0.2844  0.0818  0.1098  150 TYR   B CD2 
1336 C CE1 . TYR   B 141 ? 0.5941 0.5237 0.1752 0.2506  0.1034  0.1268  150 TYR   B CE1 
1337 C CE2 . TYR   B 141 ? 0.5995 0.5595 0.1631 0.2827  0.0952  0.1231  150 TYR   B CE2 
1338 C CZ  . TYR   B 141 ? 0.6099 0.5667 0.1859 0.2639  0.1062  0.1321  150 TYR   B CZ  
1339 O OH  . TYR   B 141 ? 0.6225 0.6033 0.2038 0.2588  0.1196  0.1465  150 TYR   B OH  
1340 N N   . GLY   B 142 ? 0.4948 0.4092 0.0932 0.2271  0.0771  0.0930  151 GLY   B N   
1341 C CA  . GLY   B 142 ? 0.5016 0.4193 0.1162 0.2080  0.0852  0.0983  151 GLY   B CA  
1342 C C   . GLY   B 142 ? 0.5120 0.4419 0.1371 0.1964  0.0834  0.0948  151 GLY   B C   
1343 O O   . GLY   B 142 ? 0.5131 0.4474 0.1516 0.1804  0.0892  0.0995  151 GLY   B O   
1344 N N   . ASN   B 143 ? 0.5188 0.4513 0.1356 0.2043  0.0743  0.0864  152 ASN   B N   
1345 C CA  . ASN   B 143 ? 0.5278 0.4717 0.1513 0.1967  0.0715  0.0823  152 ASN   B CA  
1346 C C   . ASN   B 143 ? 0.5366 0.5010 0.1492 0.2146  0.0672  0.0815  152 ASN   B C   
1347 O O   . ASN   B 143 ? 0.5405 0.4918 0.1332 0.2289  0.0575  0.0751  152 ASN   B O   
1348 C CB  . ASN   B 143 ? 0.5518 0.4728 0.1720 0.1871  0.0636  0.0713  152 ASN   B CB  
1349 C CG  . ASN   B 143 ? 0.5791 0.5078 0.2050 0.1788  0.0606  0.0668  152 ASN   B CG  
1350 O OD1 . ASN   B 143 ? 0.5769 0.5278 0.2172 0.1729  0.0658  0.0720  152 ASN   B OD1 
1351 N ND2 . ASN   B 143 ? 0.5916 0.5018 0.2055 0.1773  0.0519  0.0570  152 ASN   B ND2 
1352 N N   . GLY   B 144 ? 0.5410 0.5378 0.1655 0.2141  0.0736  0.0881  153 GLY   B N   
1353 C CA  . GLY   B 144 ? 0.5681 0.5913 0.1826 0.2341  0.0702  0.0872  153 GLY   B CA  
1354 C C   . GLY   B 144 ? 0.5839 0.6478 0.2167 0.2291  0.0755  0.0909  153 GLY   B C   
1355 O O   . GLY   B 144 ? 0.5786 0.6431 0.2267 0.2111  0.0751  0.0881  153 GLY   B O   
1356 N N   . VAL   B 145 ? 0.5975 0.6982 0.2287 0.2458  0.0802  0.0970  154 VAL   B N   
1357 C CA  . VAL   B 145 ? 0.6072 0.7568 0.2571 0.2434  0.0854  0.1004  154 VAL   B CA  
1358 C C   . VAL   B 145 ? 0.6218 0.8127 0.2791 0.2502  0.0992  0.1146  154 VAL   B C   
1359 O O   . VAL   B 145 ? 0.6358 0.8157 0.2768 0.2644  0.1023  0.1198  154 VAL   B O   
1360 C CB  . VAL   B 145 ? 0.6246 0.7832 0.2588 0.2639  0.0718  0.0871  154 VAL   B CB  
1361 C CG1 . VAL   B 145 ? 0.6368 0.8058 0.2451 0.2969  0.0678  0.0863  154 VAL   B CG1 
1362 C CG2 . VAL   B 145 ? 0.6110 0.8135 0.2679 0.2563  0.0731  0.0855  154 VAL   B CG2 
1363 N N   . VAL   B 146 ? 0.6172 0.8570 0.2989 0.2396  0.1075  0.1209  155 VAL   B N   
1364 C CA  . VAL   B 146 ? 0.6243 0.9116 0.3151 0.2438  0.1220  0.1352  155 VAL   B CA  
1365 C C   . VAL   B 146 ? 0.6450 0.9823 0.3321 0.2703  0.1179  0.1291  155 VAL   B C   
1366 O O   . VAL   B 146 ? 0.6392 1.0007 0.3400 0.2665  0.1118  0.1209  155 VAL   B O   
1367 C CB  . VAL   B 146 ? 0.6112 0.9206 0.3330 0.2098  0.1349  0.1484  155 VAL   B CB  
1368 C CG1 . VAL   B 146 ? 0.5972 0.9666 0.3307 0.2123  0.1503  0.1631  155 VAL   B CG1 
1369 C CG2 . VAL   B 146 ? 0.6328 0.8902 0.3510 0.1891  0.1386  0.1550  155 VAL   B CG2 
1370 N N   . ILE   B 147 ? 0.6707 1.0221 0.3368 0.2996  0.1199  0.1319  156 ILE   B N   
1371 C CA  . ILE   B 147 ? 0.6827 1.0789 0.3386 0.3311  0.1147  0.1250  156 ILE   B CA  
1372 C C   . ILE   B 147 ? 0.6688 1.1440 0.3514 0.3280  0.1311  0.1373  156 ILE   B C   
1373 O O   . ILE   B 147 ? 0.6623 1.1512 0.3682 0.2999  0.1469  0.1528  156 ILE   B O   
1374 C CB  . ILE   B 147 ? 0.7119 1.0799 0.3268 0.3675  0.1058  0.1199  156 ILE   B CB  
1375 C CG1 . ILE   B 147 ? 0.7175 1.0966 0.3274 0.3739  0.1209  0.1357  156 ILE   B CG1 
1376 C CG2 . ILE   B 147 ? 0.7506 1.0457 0.3425 0.3661  0.0897  0.1083  156 ILE   B CG2 
1377 C CD1 . ILE   B 147 ? 0.7432 1.1204 0.3160 0.4160  0.1131  0.1309  156 ILE   B CD1 
1378 N N   . LYS   B 148 ? 0.6590 1.1856 0.3366 0.3571  0.1267  0.1300  157 LYS   B N   
1379 C CA  . LYS   B 148 ? 0.6328 1.2446 0.3348 0.3600  0.1406  0.1389  157 LYS   B CA  
1380 C C   . LYS   B 148 ? 0.6296 1.2694 0.3433 0.3472  0.1633  0.1610  157 LYS   B C   
1381 O O   . LYS   B 148 ? 0.6100 1.2999 0.3590 0.3193  0.1776  0.1729  157 LYS   B O   
1382 C CB  . LYS   B 148 ? 0.6530 1.3030 0.3319 0.4062  0.1311  0.1272  157 LYS   B CB  
1383 C CG  . LYS   B 148 ? 0.6748 1.3955 0.3813 0.4065  0.1297  0.1203  157 LYS   B CG  
1384 C CD  . LYS   B 148 ? 0.7034 1.4944 0.3989 0.4485  0.1310  0.1172  157 LYS   B CD  
1385 C CE  . LYS   B 148 ? 0.7085 1.5775 0.4378 0.4450  0.1311  0.1111  157 LYS   B CE  
1386 N NZ  . LYS   B 148 ? 0.7076 1.6597 0.4332 0.4834  0.1360  0.1101  157 LYS   B NZ  
1387 N N   . ASN   B 149 ? 0.6468 1.2549 0.3306 0.3662  0.1665  0.1669  158 ASN   B N   
1388 C CA  . ASN   B 149 ? 0.6411 1.2730 0.3316 0.3554  0.1884  0.1885  158 ASN   B CA  
1389 C C   . ASN   B 149 ? 0.6435 1.2308 0.3482 0.3124  0.1972  0.2012  158 ASN   B C   
1390 O O   . ASN   B 149 ? 0.6457 1.2430 0.3527 0.2997  0.2148  0.2198  158 ASN   B O   
1391 C CB  . ASN   B 149 ? 0.6747 1.2981 0.3272 0.3946  0.1899  0.1912  158 ASN   B CB  
1392 C CG  . ASN   B 149 ? 0.7557 1.2967 0.3724 0.4089  0.1753  0.1826  158 ASN   B CG  
1393 O OD1 . ASN   B 149 ? 0.7891 1.3193 0.3724 0.4439  0.1713  0.1808  158 ASN   B OD1 
1394 N ND2 . ASN   B 149 ? 0.7759 1.2592 0.3983 0.3831  0.1669  0.1772  158 ASN   B ND2 
1395 N N   . GLY   B 150 ? 0.6396 1.1774 0.3503 0.2922  0.1848  0.1910  159 GLY   B N   
1396 C CA  . GLY   B 150 ? 0.6403 1.1340 0.3616 0.2548  0.1901  0.2002  159 GLY   B CA  
1397 C C   . GLY   B 150 ? 0.6568 1.0744 0.3501 0.2609  0.1824  0.1962  159 GLY   B C   
1398 O O   . GLY   B 150 ? 0.6762 1.0495 0.3754 0.2343  0.1810  0.1976  159 GLY   B O   
1399 N N   . SER   B 151 ? 0.6461 1.0486 0.3083 0.2967  0.1763  0.1906  160 SER   B N   
1400 C CA  A SER   B 151 ? 0.6682 1.0031 0.3049 0.3035  0.1681  0.1861  160 SER   B CA  
1401 C CA  B SER   B 151 ? 0.6696 1.0049 0.3059 0.3043  0.1678  0.1859  160 SER   B CA  
1402 C C   . SER   B 151 ? 0.6696 0.9579 0.3060 0.2952  0.1506  0.1694  160 SER   B C   
1403 O O   . SER   B 151 ? 0.6597 0.9637 0.3063 0.2942  0.1418  0.1586  160 SER   B O   
1404 C CB  A SER   B 151 ? 0.6940 1.0240 0.2974 0.3427  0.1644  0.1841  160 SER   B CB  
1405 C CB  B SER   B 151 ? 0.6987 1.0304 0.3017 0.3442  0.1636  0.1832  160 SER   B CB  
1406 O OG  A SER   B 151 ? 0.7402 1.0108 0.3226 0.3460  0.1587  0.1822  160 SER   B OG  
1407 O OG  B SER   B 151 ? 0.7162 1.0804 0.3108 0.3721  0.1542  0.1722  160 SER   B OG  
1408 N N   . TYR   B 152 ? 0.6628 0.8956 0.2872 0.2890  0.1463  0.1677  161 TYR   B N   
1409 C CA  . TYR   B 152 ? 0.6591 0.8484 0.2834 0.2789  0.1324  0.1539  161 TYR   B CA  
1410 C C   . TYR   B 152 ? 0.6563 0.8114 0.2524 0.3043  0.1160  0.1401  161 TYR   B C   
1411 O O   . TYR   B 152 ? 0.6650 0.8030 0.2403 0.3222  0.1153  0.1422  161 TYR   B O   
1412 C CB  . TYR   B 152 ? 0.6650 0.8192 0.2978 0.2520  0.1381  0.1605  161 TYR   B CB  
1413 C CG  . TYR   B 152 ? 0.6801 0.7909 0.3124 0.2418  0.1257  0.1475  161 TYR   B CG  
1414 C CD1 . TYR   B 152 ? 0.6829 0.7977 0.3318 0.2255  0.1202  0.1398  161 TYR   B CD1 
1415 C CD2 . TYR   B 152 ? 0.7075 0.7759 0.3230 0.2489  0.1196  0.1427  161 TYR   B CD2 
1416 C CE1 . TYR   B 152 ? 0.7006 0.7776 0.3473 0.2173  0.1098  0.1282  161 TYR   B CE1 
1417 C CE2 . TYR   B 152 ? 0.7303 0.7650 0.3465 0.2393  0.1095  0.1311  161 TYR   B CE2 
1418 C CZ  . TYR   B 152 ? 0.7306 0.7695 0.3614 0.2240  0.1051  0.1242  161 TYR   B CZ  
1419 O OH  . TYR   B 152 ? 0.7639 0.7714 0.3940 0.2151  0.0964  0.1136  161 TYR   B OH  
1420 N N   . VAL   B 153 ? 0.6412 0.7846 0.2349 0.3053  0.1021  0.1258  162 VAL   B N   
1421 C CA  . VAL   B 153 ? 0.6443 0.7510 0.2105 0.3241  0.0852  0.1129  162 VAL   B CA  
1422 C C   . VAL   B 153 ? 0.6317 0.7002 0.2037 0.3029  0.0771  0.1038  162 VAL   B C   
1423 O O   . VAL   B 153 ? 0.6174 0.6923 0.2011 0.2907  0.0741  0.0983  162 VAL   B O   
1424 C CB  . VAL   B 153 ? 0.6517 0.7755 0.1971 0.3523  0.0739  0.1041  162 VAL   B CB  
1425 C CG1 . VAL   B 153 ? 0.6774 0.7546 0.1906 0.3680  0.0549  0.0916  162 VAL   B CG1 
1426 C CG2 . VAL   B 153 ? 0.6494 0.8155 0.1886 0.3756  0.0832  0.1134  162 VAL   B CG2 
1427 N N   . SER   B 154 ? 0.6312 0.6630 0.1959 0.2990  0.0744  0.1025  163 SER   B N   
1428 C CA  . SER   B 154 ? 0.6262 0.6238 0.1956 0.2804  0.0682  0.0947  163 SER   B CA  
1429 C C   . SER   B 154 ? 0.6316 0.6002 0.1777 0.2913  0.0514  0.0822  163 SER   B C   
1430 O O   . SER   B 154 ? 0.6406 0.5989 0.1657 0.3107  0.0446  0.0807  163 SER   B O   
1431 C CB  . SER   B 154 ? 0.6382 0.6171 0.2129 0.2715  0.0749  0.1003  163 SER   B CB  
1432 O OG  . SER   B 154 ? 0.6702 0.6185 0.2455 0.2597  0.0676  0.0915  163 SER   B OG  
1433 N N   . ALA   B 155 ? 0.6242 0.5752 0.1725 0.2767  0.0444  0.0736  164 ALA   B N   
1434 C CA  . ALA   B 155 ? 0.6337 0.5529 0.1587 0.2816  0.0286  0.0627  164 ALA   B CA  
1435 C C   . ALA   B 155 ? 0.6235 0.5177 0.1459 0.2770  0.0258  0.0611  164 ALA   B C   
1436 O O   . ALA   B 155 ? 0.6171 0.5156 0.1568 0.2681  0.0359  0.0668  164 ALA   B O   
1437 C CB  . ALA   B 155 ? 0.6402 0.5481 0.1678 0.2656  0.0238  0.0553  164 ALA   B CB  
1438 N N   . ILE   B 156 ? 0.6159 0.4841 0.1144 0.2843  0.0108  0.0532  165 ILE   B N   
1439 C CA  . ILE   B 156 ? 0.6037 0.4510 0.1009 0.2776  0.0057  0.0496  165 ILE   B CA  
1440 C C   . ILE   B 156 ? 0.5973 0.4310 0.1019 0.2542  0.0039  0.0437  165 ILE   B C   
1441 O O   . ILE   B 156 ? 0.6093 0.4218 0.0935 0.2523  -0.0084 0.0369  165 ILE   B O   
1442 C CB  . ILE   B 156 ? 0.6173 0.4432 0.0839 0.2954  -0.0110 0.0442  165 ILE   B CB  
1443 C CG1 . ILE   B 156 ? 0.6250 0.4660 0.0804 0.3226  -0.0090 0.0501  165 ILE   B CG1 
1444 C CG2 . ILE   B 156 ? 0.6249 0.4324 0.0934 0.2851  -0.0176 0.0395  165 ILE   B CG2 
1445 C CD1 . ILE   B 156 ? 0.6505 0.4697 0.0723 0.3435  -0.0264 0.0445  165 ILE   B CD1 
1446 N N   . THR   B 157 ? 0.5744 0.4186 0.1048 0.2373  0.0161  0.0467  166 THR   B N   
1447 C CA  . THR   B 157 ? 0.5722 0.4060 0.1097 0.2165  0.0161  0.0415  166 THR   B CA  
1448 C C   . THR   B 157 ? 0.5694 0.3888 0.1066 0.2061  0.0109  0.0362  166 THR   B C   
1449 O O   . THR   B 157 ? 0.5614 0.3889 0.1137 0.2044  0.0169  0.0377  166 THR   B O   
1450 C CB  . THR   B 157 ? 0.5722 0.4210 0.1344 0.2041  0.0295  0.0460  166 THR   B CB  
1451 O OG1 . THR   B 157 ? 0.5799 0.4468 0.1461 0.2105  0.0345  0.0513  166 THR   B OG1 
1452 C CG2 . THR   B 157 ? 0.5782 0.4169 0.1448 0.1860  0.0295  0.0406  166 THR   B CG2 
1453 N N   . GLN   B 158 ? 0.5755 0.3745 0.0951 0.1985  -0.0001 0.0299  167 GLN   B N   
1454 C CA  . GLN   B 158 ? 0.5827 0.3732 0.1044 0.1851  -0.0046 0.0252  167 GLN   B CA  
1455 C C   . GLN   B 158 ? 0.6100 0.3931 0.1343 0.1631  -0.0024 0.0217  167 GLN   B C   
1456 O O   . GLN   B 158 ? 0.6149 0.3860 0.1257 0.1602  -0.0047 0.0208  167 GLN   B O   
1457 C CB  . GLN   B 158 ? 0.5903 0.3617 0.0876 0.1931  -0.0207 0.0216  167 GLN   B CB  
1458 C CG  . GLN   B 158 ? 0.5875 0.3514 0.0859 0.1767  -0.0277 0.0166  167 GLN   B CG  
1459 C CD  . GLN   B 158 ? 0.5744 0.3609 0.0982 0.1771  -0.0209 0.0164  167 GLN   B CD  
1460 O OE1 . GLN   B 158 ? 0.5676 0.3728 0.1146 0.1709  -0.0077 0.0179  167 GLN   B OE1 
1461 N NE2 . GLN   B 158 ? 0.5492 0.3322 0.0665 0.1853  -0.0314 0.0137  167 GLN   B NE2 
1462 N N   . GLY   B 159 ? 0.6236 0.4163 0.1649 0.1496  0.0025  0.0197  168 GLY   B N   
1463 C CA  . GLY   B 159 ? 0.6577 0.4472 0.2017 0.1296  0.0060  0.0169  168 GLY   B CA  
1464 C C   . GLY   B 159 ? 0.7068 0.4780 0.2323 0.1156  -0.0050 0.0132  168 GLY   B C   
1465 O O   . GLY   B 159 ? 0.7096 0.4675 0.2188 0.1215  -0.0174 0.0121  168 GLY   B O   
1466 N N   . LYS   B 160 ? 0.7456 0.5142 0.2713 0.0964  -0.0010 0.0117  169 LYS   B N   
1467 C CA  . LYS   B 160 ? 0.7977 0.5487 0.3056 0.0778  -0.0098 0.0096  169 LYS   B CA  
1468 C C   . LYS   B 160 ? 0.8169 0.5950 0.3485 0.0620  -0.0037 0.0076  169 LYS   B C   
1469 O O   . LYS   B 160 ? 0.8067 0.6095 0.3610 0.0600  0.0094  0.0073  169 LYS   B O   
1470 C CB  . LYS   B 160 ? 0.8415 0.5675 0.3265 0.0665  -0.0101 0.0098  169 LYS   B CB  
1471 C CG  . LYS   B 160 ? 0.9213 0.6178 0.3773 0.0478  -0.0219 0.0091  169 LYS   B CG  
1472 C CD  . LYS   B 160 ? 0.9906 0.6773 0.4370 0.0276  -0.0154 0.0099  169 LYS   B CD  
1473 C CE  . LYS   B 160 ? 1.0650 0.7225 0.4827 0.0049  -0.0259 0.0106  169 LYS   B CE  
1474 N NZ  . LYS   B 160 ? 1.1071 0.7562 0.5143 -0.0154 -0.0176 0.0125  169 LYS   B NZ  
1475 N N   . ARG   B 161 ? 0.8393 0.6140 0.3651 0.0519  -0.0142 0.0057  170 ARG   B N   
1476 C CA  . ARG   B 161 ? 0.8434 0.6490 0.3926 0.0358  -0.0097 0.0031  170 ARG   B CA  
1477 C C   . ARG   B 161 ? 0.8703 0.6682 0.4088 0.0086  -0.0066 0.0044  170 ARG   B C   
1478 O O   . ARG   B 161 ? 0.9016 0.6609 0.4071 -0.0004 -0.0158 0.0065  170 ARG   B O   
1479 C CB  . ARG   B 161 ? 0.8614 0.6691 0.4107 0.0355  -0.0235 0.0002  170 ARG   B CB  
1480 C CG  . ARG   B 161 ? 0.8746 0.7271 0.4583 0.0353  -0.0176 -0.0039 170 ARG   B CG  
1481 C CD  . ARG   B 161 ? 0.9195 0.7800 0.5052 0.0158  -0.0290 -0.0072 170 ARG   B CD  
1482 N NE  . ARG   B 161 ? 0.9348 0.8455 0.5559 0.0150  -0.0222 -0.0123 170 ARG   B NE  
1483 C CZ  . ARG   B 161 ? 0.9516 0.8806 0.5874 0.0325  -0.0278 -0.0171 170 ARG   B CZ  
1484 N NH1 . ARG   B 161 ? 0.9650 0.8663 0.5831 0.0512  -0.0398 -0.0167 170 ARG   B NH1 
1485 N NH2 . ARG   B 161 ? 0.9239 0.8997 0.5904 0.0333  -0.0217 -0.0228 170 ARG   B NH2 
1486 N N   . GLU   B 162 ? 0.8560 0.6891 0.4189 -0.0030 0.0064  0.0033  171 GLU   B N   
1487 C CA  . GLU   B 162 ? 0.8718 0.7017 0.4251 -0.0288 0.0118  0.0055  171 GLU   B CA  
1488 C C   . GLU   B 162 ? 0.8644 0.7186 0.4290 -0.0534 0.0093  0.0045  171 GLU   B C   
1489 O O   . GLU   B 162 ? 0.8828 0.7093 0.4240 -0.0714 -0.0033 0.0065  171 GLU   B O   
1490 C CB  . GLU   B 162 ? 0.8975 0.7459 0.4636 -0.0251 0.0288  0.0056  171 GLU   B CB  
1491 C CG  . GLU   B 162 ? 0.9918 0.8027 0.5316 -0.0197 0.0291  0.0083  171 GLU   B CG  
1492 C CD  . GLU   B 162 ? 1.1086 0.8861 0.6152 -0.0419 0.0249  0.0116  171 GLU   B CD  
1493 O OE1 . GLU   B 162 ? 1.1108 0.8989 0.6179 -0.0572 0.0359  0.0130  171 GLU   B OE1 
1494 O OE2 . GLU   B 162 ? 1.1676 0.9059 0.6443 -0.0429 0.0103  0.0128  171 GLU   B OE2 
1495 S S   . DMS   C .   ? 0.9906 0.6647 0.5705 0.1274  0.0528  0.0155  201 DMS   B S   
1496 O O   . DMS   C .   ? 0.9746 0.6815 0.5646 0.1349  0.0600  0.0118  201 DMS   B O   
1497 C C1  . DMS   C .   ? 1.0098 0.6546 0.5641 0.1423  0.0461  0.0057  201 DMS   B C1  
1498 C C2  . DMS   C .   ? 0.9995 0.6529 0.5712 0.1285  0.0513  0.0257  201 DMS   B C2  
1499 N N1  . A1BGP D .   ? 1.1234 1.1955 0.7754 0.1728  0.1575  0.1864  202 A1BGP B N1  
1500 N N3  . A1BGP D .   ? 0.8897 0.8813 0.7036 0.1450  0.0769  0.0802  202 A1BGP B N3  
1501 C C4  . A1BGP D .   ? 1.0092 1.0123 0.7343 0.1552  0.1175  0.1352  202 A1BGP B C4  
1502 C C5  . A1BGP D .   ? 1.0665 1.0921 0.7543 0.1412  0.1391  0.1658  202 A1BGP B C5  
1503 C C6  . A1BGP D .   ? 1.0702 1.1459 0.7589 0.1342  0.1464  0.1735  202 A1BGP B C6  
1504 C C7  . A1BGP D .   ? 1.1279 1.2417 0.8223 0.1286  0.1609  0.1912  202 A1BGP B C7  
1505 C C8  . A1BGP D .   ? 1.1506 1.2657 0.8236 0.1539  0.1669  0.1972  202 A1BGP B C8  
1506 C C10 . A1BGP D .   ? 0.9007 0.9211 0.7046 0.1385  0.0776  0.0862  202 A1BGP B C10 
1507 C C13 . A1BGP D .   ? 0.8360 0.7892 0.6909 0.1198  0.0571  0.0495  202 A1BGP B C13 
1508 C C15 . A1BGP D .   ? 0.8165 0.7474 0.6835 0.1073  0.0458  0.0334  202 A1BGP B C15 
1509 C C17 . A1BGP D .   ? 0.8312 0.7760 0.6864 0.1315  0.0527  0.0428  202 A1BGP B C17 
1510 O O1  . A1BGP D .   ? 0.8922 0.8929 0.6980 0.1795  0.0745  0.0776  202 A1BGP B O1  
1511 C C1  . A1BGP D .   ? 0.9004 0.8956 0.7039 0.1629  0.0802  0.0841  202 A1BGP B C1  
1512 C C2  . A1BGP D .   ? 0.9357 0.9260 0.7128 0.1634  0.0924  0.0991  202 A1BGP B C2  
1513 C C3  . A1BGP D .   ? 0.9374 0.9115 0.7101 0.1797  0.0922  0.0952  202 A1BGP B C3  
1514 S S1  . A1BGP D .   ? 0.9886 0.9661 0.7229 0.1810  0.1085  0.1187  202 A1BGP B S1  
1515 C C9  . A1BGP D .   ? 1.1052 1.1309 0.7610 0.1570  0.1510  0.1808  202 A1BGP B C9  
1516 N N2  . A1BGP D .   ? 0.9764 0.9789 0.7267 0.1469  0.1067  0.1210  202 A1BGP B N2  
1517 C C11 . A1BGP D .   ? 0.8971 0.9044 0.7071 0.1153  0.0768  0.0849  202 A1BGP B C11 
1518 C C12 . A1BGP D .   ? 0.8671 0.8343 0.7000 0.1172  0.0683  0.0667  202 A1BGP B C12 
1519 C C14 . A1BGP D .   ? 0.8316 0.7775 0.6893 0.1055  0.0533  0.0447  202 A1BGP B C14 
1520 C C16 . A1BGP D .   ? 0.8201 0.7491 0.6809 0.1098  0.0419  0.0305  202 A1BGP B C16 
1521 N N4  . A1BGP D .   ? 0.8276 0.7620 0.6820 0.1212  0.0449  0.0344  202 A1BGP B N4  
1522 C C18 . A1BGP D .   ? 0.8699 0.8296 0.7005 0.1328  0.0718  0.0677  202 A1BGP B C18 
# 
