data_7HOO
# 
_entry.id   7HOO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HOO         pdb_00007hoo 10.2210/pdb7hoo/pdb 
WWPDB D_1001407738 ?            ?                   
# 
_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       2025-05-28 
_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                        7HOO 
_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 man 'DIMETHYL SULFOXIDE'                                                   78.133    1  ?                           
None ? ? 
4 non-polymer syn '(2P)-2-(5-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' 308.335   1  ?                           
?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                          96.063    1  ?                           
?    ? ? 
6 water       nat water                                                                  18.015    99 ?                           
?    ? ? 
# 
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 '(2P)-2-(5-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' A1BGX 
5 'SULFATE ION'                                                          SO4   
6 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample ?                     ? ?   ? ? ? ? ? ? ? ? ? '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 
A1BGX non-polymer         . '(2P)-2-(5-methoxypyridin-3-yl)-N-(1-methyl-1H-pyrazol-4-yl)benzamide' ? 'C17 H16 N4 O2'  308.335 
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                          ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                             ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGX 
_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 A1BGX 1  202 301 A1BGX LIG B . 
E 5 SO4   1  203 302 SO4   SO4 B . 
F 6 HOH   1  101 48  HOH   HOH A . 
F 6 HOH   2  102 98  HOH   HOH A . 
F 6 HOH   3  103 118 HOH   HOH A . 
F 6 HOH   4  104 137 HOH   HOH A . 
F 6 HOH   5  105 34  HOH   HOH A . 
F 6 HOH   6  106 117 HOH   HOH A . 
F 6 HOH   7  107 36  HOH   HOH A . 
F 6 HOH   8  108 49  HOH   HOH A . 
F 6 HOH   9  109 126 HOH   HOH A . 
F 6 HOH   10 110 65  HOH   HOH A . 
F 6 HOH   11 111 28  HOH   HOH A . 
F 6 HOH   12 112 20  HOH   HOH A . 
F 6 HOH   13 113 16  HOH   HOH A . 
F 6 HOH   14 114 120 HOH   HOH A . 
F 6 HOH   15 115 70  HOH   HOH A . 
F 6 HOH   16 116 110 HOH   HOH A . 
F 6 HOH   17 117 124 HOH   HOH A . 
F 6 HOH   18 118 29  HOH   HOH A . 
F 6 HOH   19 119 129 HOH   HOH A . 
F 6 HOH   20 120 105 HOH   HOH A . 
F 6 HOH   21 121 50  HOH   HOH A . 
F 6 HOH   22 122 54  HOH   HOH A . 
F 6 HOH   23 123 119 HOH   HOH A . 
F 6 HOH   24 124 121 HOH   HOH A . 
F 6 HOH   25 125 27  HOH   HOH A . 
F 6 HOH   26 126 40  HOH   HOH A . 
F 6 HOH   27 127 136 HOH   HOH A . 
F 6 HOH   28 128 133 HOH   HOH A . 
G 6 HOH   1  301 123 HOH   HOH B . 
G 6 HOH   2  302 115 HOH   HOH B . 
G 6 HOH   3  303 92  HOH   HOH B . 
G 6 HOH   4  304 51  HOH   HOH B . 
G 6 HOH   5  305 11  HOH   HOH B . 
G 6 HOH   6  306 24  HOH   HOH B . 
G 6 HOH   7  307 90  HOH   HOH B . 
G 6 HOH   8  308 46  HOH   HOH B . 
G 6 HOH   9  309 57  HOH   HOH B . 
G 6 HOH   10 310 77  HOH   HOH B . 
G 6 HOH   11 311 63  HOH   HOH B . 
G 6 HOH   12 312 66  HOH   HOH B . 
G 6 HOH   13 313 14  HOH   HOH B . 
G 6 HOH   14 314 89  HOH   HOH B . 
G 6 HOH   15 315 31  HOH   HOH B . 
G 6 HOH   16 316 58  HOH   HOH B . 
G 6 HOH   17 317 9   HOH   HOH B . 
G 6 HOH   18 318 108 HOH   HOH B . 
G 6 HOH   19 319 68  HOH   HOH B . 
G 6 HOH   20 320 127 HOH   HOH B . 
G 6 HOH   21 321 2   HOH   HOH B . 
G 6 HOH   22 322 5   HOH   HOH B . 
G 6 HOH   23 323 106 HOH   HOH B . 
G 6 HOH   24 324 39  HOH   HOH B . 
G 6 HOH   25 325 72  HOH   HOH B . 
G 6 HOH   26 326 4   HOH   HOH B . 
G 6 HOH   27 327 32  HOH   HOH B . 
G 6 HOH   28 328 56  HOH   HOH B . 
G 6 HOH   29 329 1   HOH   HOH B . 
G 6 HOH   30 330 60  HOH   HOH B . 
G 6 HOH   31 331 69  HOH   HOH B . 
G 6 HOH   32 332 100 HOH   HOH B . 
G 6 HOH   33 333 10  HOH   HOH B . 
G 6 HOH   34 334 132 HOH   HOH B . 
G 6 HOH   35 335 12  HOH   HOH B . 
G 6 HOH   36 336 42  HOH   HOH B . 
G 6 HOH   37 337 131 HOH   HOH B . 
G 6 HOH   38 338 67  HOH   HOH B . 
G 6 HOH   39 339 23  HOH   HOH B . 
G 6 HOH   40 340 3   HOH   HOH B . 
G 6 HOH   41 341 116 HOH   HOH B . 
G 6 HOH   42 342 80  HOH   HOH B . 
G 6 HOH   43 343 81  HOH   HOH B . 
G 6 HOH   44 344 35  HOH   HOH B . 
G 6 HOH   45 345 102 HOH   HOH B . 
G 6 HOH   46 346 21  HOH   HOH B . 
G 6 HOH   47 347 107 HOH   HOH B . 
G 6 HOH   48 348 18  HOH   HOH B . 
G 6 HOH   49 349 103 HOH   HOH B . 
G 6 HOH   50 350 64  HOH   HOH B . 
G 6 HOH   51 351 13  HOH   HOH B . 
G 6 HOH   52 352 82  HOH   HOH B . 
G 6 HOH   53 353 62  HOH   HOH B . 
G 6 HOH   54 354 43  HOH   HOH B . 
G 6 HOH   55 355 17  HOH   HOH B . 
G 6 HOH   56 356 73  HOH   HOH B . 
G 6 HOH   57 357 26  HOH   HOH B . 
G 6 HOH   58 358 87  HOH   HOH B . 
G 6 HOH   59 359 122 HOH   HOH B . 
G 6 HOH   60 360 61  HOH   HOH B . 
G 6 HOH   61 361 125 HOH   HOH B . 
G 6 HOH   62 362 112 HOH   HOH B . 
G 6 HOH   63 363 44  HOH   HOH B . 
G 6 HOH   64 364 94  HOH   HOH B . 
G 6 HOH   65 365 79  HOH   HOH B . 
G 6 HOH   66 366 45  HOH   HOH B . 
G 6 HOH   67 367 59  HOH   HOH B . 
G 6 HOH   68 368 134 HOH   HOH B . 
G 6 HOH   69 369 130 HOH   HOH B . 
G 6 HOH   70 370 109 HOH   HOH B . 
G 6 HOH   71 371 75  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (20-OCT-2021)' ? 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           7HOO 
_cell.length_a           42.454 
_cell.length_b           42.454 
_cell.length_c           216.494 
_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                         7HOO 
_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          7HOO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.10 
_exptl_crystal.density_percent_sol   41.53 
_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   2023-09-19 
_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                     7HOO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.58 
_reflns.d_resolution_high            1.49 
_reflns.number_obs                   33869 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.118 
_reflns.pdbx_netI_over_sigmaI        8.7 
_reflns.pdbx_redundancy              24.6 
_reflns.pdbx_Rrim_I_all              0.121 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     833134 
_reflns.pdbx_chi_squared             0.22 
_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                  1.49 
_reflns_shell.d_res_low                   1.52 
_reflns_shell.number_measured_all         33645 
_reflns_shell.number_unique_obs           1721 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.06 
_reflns_shell.pdbx_redundancy             19.5 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.0 
_reflns_shell.pdbx_Rrim_I_all             19.464 
_reflns_shell.pdbx_Rpim_I_all             4.360 
_reflns_shell.pdbx_CC_half                0.272 
_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                                 7HOO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27272 
_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                             23.08 
_refine.ls_d_res_high                            1.492 
_refine.ls_percent_reflns_obs                    81.1 
_refine.ls_R_factor_obs                          0.2555 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2540 
_refine.ls_R_factor_R_free                       0.2844 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.080 
_refine.ls_number_reflns_R_free                  1385 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.924 
_refine.B_iso_mean                               53.77 
_refine.aniso_B[1][1]                            -6.24280 
_refine.aniso_B[2][2]                            -6.24280 
_refine.aniso_B[3][3]                            12.48560 
_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             0.122 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.117 
_refine.pdbx_overall_SU_R_Blow_DPI               0.129 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.121 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HOO 
_refine_analyze.Luzzati_coordinate_error_obs    0.48 
_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         32 
_refine_hist.number_atoms_solvent             99 
_refine_hist.number_atoms_total               1607 
_refine_hist.d_res_high                       1.492 
_refine_hist.d_res_low                        23.08 
# 
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  1731 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.97  ? 2.00  2370 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  605  '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  306  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1731 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.30  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.11 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  215  '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  1402 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.49 
_refine_ls_shell.d_res_low                        1.58 
_refine_ls_shell.number_reflns_R_work             520 
_refine_ls_shell.R_factor_R_work                  0.7386 
_refine_ls_shell.percent_reflns_obs               10.20 
_refine_ls_shell.R_factor_R_free                  0.7256 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.76 
_refine_ls_shell.number_reflns_R_free             26 
_refine_ls_shell.number_reflns_all                546 
_refine_ls_shell.R_factor_all                     0.7381 
# 
_struct.entry_id                  7HOO 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014643-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOO 
_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 6 ? 
G N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOO A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOO 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 7HOO SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOO MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOO MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOO LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O ILE B 100 ? O ILE B 109 N LEU B 88  ? N LEU B 97  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HOO 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    CYS 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     80 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             78.40 
_pdbx_validate_torsion.psi             -11.44 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 324 ? G HOH . 
2 1 B HOH 366 ? G HOH . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[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 -15.0928 -1.6690 -20.8834 0.0520 -0.0307 -0.1907 0.2190 0.1188 0.1007 3.1490 3.2924 4.2056 -1.7271 
0.2072 0.9452  0.5673 0.5641 0.3012 -0.5666 -0.5212 -0.2506 -0.0572 0.4066 -0.0460 
'X-RAY DIFFRACTION' 2 ? refined -18.0418 0.7796  -15.4520 0.1104 0.0325  -0.0335 0.1827 0.0474 0.0377 1.0843 0.9502 2.0325 -0.8472 
0.8344 -0.2537 0.3524 0.2122 0.1659 -0.1789 -0.3488 0.0559  0.1346  0.2351 -0.0037 
# 
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 
A1BGX N1   N Y N 1   
A1BGX N3   N Y N 2   
A1BGX C4   C Y N 3   
A1BGX C5   C Y N 4   
A1BGX C6   C Y N 5   
A1BGX C7   C Y N 6   
A1BGX C8   C Y N 7   
A1BGX C10  C Y N 8   
A1BGX C13  C Y N 9   
A1BGX C15  C N N 10  
A1BGX C17  C Y N 11  
A1BGX C1   C N N 12  
A1BGX O1   O N N 13  
A1BGX C2   C Y N 14  
A1BGX C3   C Y N 15  
A1BGX C9   C Y N 16  
A1BGX C11  C Y N 17  
A1BGX C12  C N N 18  
A1BGX O2   O N N 19  
A1BGX N2   N N N 20  
A1BGX C14  C Y N 21  
A1BGX N4   N Y N 22  
A1BGX C16  C Y N 23  
A1BGX H5   H N N 24  
A1BGX H6   H N N 25  
A1BGX H7   H N N 26  
A1BGX H9   H N N 27  
A1BGX H12  H N N 28  
A1BGX H14  H N N 29  
A1BGX H13  H N N 30  
A1BGX H16  H N N 31  
A1BGX H3   H N N 32  
A1BGX H1   H N N 33  
A1BGX H2   H N N 34  
A1BGX H4   H N N 35  
A1BGX H8   H N N 36  
A1BGX H10  H N N 37  
A1BGX H11  H N N 38  
A1BGX H15  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
DMS   S    S N N 127 
DMS   O    O N N 128 
DMS   C1   C N N 129 
DMS   C2   C N N 130 
DMS   H11  H N N 131 
DMS   H12  H N N 132 
DMS   H13  H N N 133 
DMS   H21  H N N 134 
DMS   H22  H N N 135 
DMS   H23  H N N 136 
GLN   N    N N N 137 
GLN   CA   C N S 138 
GLN   C    C N N 139 
GLN   O    O N N 140 
GLN   CB   C N N 141 
GLN   CG   C N N 142 
GLN   CD   C N N 143 
GLN   OE1  O N N 144 
GLN   NE2  N N N 145 
GLN   OXT  O N N 146 
GLN   H    H N N 147 
GLN   H2   H N N 148 
GLN   HA   H N N 149 
GLN   HB2  H N N 150 
GLN   HB3  H N N 151 
GLN   HG2  H N N 152 
GLN   HG3  H N N 153 
GLN   HE21 H N N 154 
GLN   HE22 H N N 155 
GLN   HXT  H N N 156 
GLU   N    N N N 157 
GLU   CA   C N S 158 
GLU   C    C N N 159 
GLU   O    O N N 160 
GLU   CB   C N N 161 
GLU   CG   C N N 162 
GLU   CD   C N N 163 
GLU   OE1  O N N 164 
GLU   OE2  O N N 165 
GLU   OXT  O N N 166 
GLU   H    H N N 167 
GLU   H2   H N N 168 
GLU   HA   H N N 169 
GLU   HB2  H N N 170 
GLU   HB3  H N N 171 
GLU   HG2  H N N 172 
GLU   HG3  H N N 173 
GLU   HE2  H N N 174 
GLU   HXT  H N N 175 
GLY   N    N N N 176 
GLY   CA   C N N 177 
GLY   C    C N N 178 
GLY   O    O N N 179 
GLY   OXT  O N N 180 
GLY   H    H N N 181 
GLY   H2   H N N 182 
GLY   HA2  H N N 183 
GLY   HA3  H N N 184 
GLY   HXT  H N N 185 
HIS   N    N N N 186 
HIS   CA   C N S 187 
HIS   C    C N N 188 
HIS   O    O N N 189 
HIS   CB   C N N 190 
HIS   CG   C Y N 191 
HIS   ND1  N Y N 192 
HIS   CD2  C Y N 193 
HIS   CE1  C Y N 194 
HIS   NE2  N Y N 195 
HIS   OXT  O N N 196 
HIS   H    H N N 197 
HIS   H2   H N N 198 
HIS   HA   H N N 199 
HIS   HB2  H N N 200 
HIS   HB3  H N N 201 
HIS   HD1  H N N 202 
HIS   HD2  H N N 203 
HIS   HE1  H N N 204 
HIS   HE2  H N N 205 
HIS   HXT  H N N 206 
HOH   O    O N N 207 
HOH   H1   H N N 208 
HOH   H2   H N N 209 
ILE   N    N N N 210 
ILE   CA   C N S 211 
ILE   C    C N N 212 
ILE   O    O N N 213 
ILE   CB   C N S 214 
ILE   CG1  C N N 215 
ILE   CG2  C N N 216 
ILE   CD1  C N N 217 
ILE   OXT  O N N 218 
ILE   H    H N N 219 
ILE   H2   H N N 220 
ILE   HA   H N N 221 
ILE   HB   H N N 222 
ILE   HG12 H N N 223 
ILE   HG13 H N N 224 
ILE   HG21 H N N 225 
ILE   HG22 H N N 226 
ILE   HG23 H N N 227 
ILE   HD11 H N N 228 
ILE   HD12 H N N 229 
ILE   HD13 H N N 230 
ILE   HXT  H N N 231 
LEU   N    N N N 232 
LEU   CA   C N S 233 
LEU   C    C N N 234 
LEU   O    O N N 235 
LEU   CB   C N N 236 
LEU   CG   C N N 237 
LEU   CD1  C N N 238 
LEU   CD2  C N N 239 
LEU   OXT  O N N 240 
LEU   H    H N N 241 
LEU   H2   H N N 242 
LEU   HA   H N N 243 
LEU   HB2  H N N 244 
LEU   HB3  H N N 245 
LEU   HG   H N N 246 
LEU   HD11 H N N 247 
LEU   HD12 H N N 248 
LEU   HD13 H N N 249 
LEU   HD21 H N N 250 
LEU   HD22 H N N 251 
LEU   HD23 H N N 252 
LEU   HXT  H N N 253 
LYS   N    N N N 254 
LYS   CA   C N S 255 
LYS   C    C N N 256 
LYS   O    O N N 257 
LYS   CB   C N N 258 
LYS   CG   C N N 259 
LYS   CD   C N N 260 
LYS   CE   C N N 261 
LYS   NZ   N N N 262 
LYS   OXT  O N N 263 
LYS   H    H N N 264 
LYS   H2   H N N 265 
LYS   HA   H N N 266 
LYS   HB2  H N N 267 
LYS   HB3  H N N 268 
LYS   HG2  H N N 269 
LYS   HG3  H N N 270 
LYS   HD2  H N N 271 
LYS   HD3  H N N 272 
LYS   HE2  H N N 273 
LYS   HE3  H N N 274 
LYS   HZ1  H N N 275 
LYS   HZ2  H N N 276 
LYS   HZ3  H N N 277 
LYS   HXT  H N N 278 
MET   N    N N N 279 
MET   CA   C N S 280 
MET   C    C N N 281 
MET   O    O N N 282 
MET   CB   C N N 283 
MET   CG   C N N 284 
MET   SD   S N N 285 
MET   CE   C N N 286 
MET   OXT  O N N 287 
MET   H    H N N 288 
MET   H2   H N N 289 
MET   HA   H N N 290 
MET   HB2  H N N 291 
MET   HB3  H N N 292 
MET   HG2  H N N 293 
MET   HG3  H N N 294 
MET   HE1  H N N 295 
MET   HE2  H N N 296 
MET   HE3  H N N 297 
MET   HXT  H N N 298 
PHE   N    N N N 299 
PHE   CA   C N S 300 
PHE   C    C N N 301 
PHE   O    O N N 302 
PHE   CB   C N N 303 
PHE   CG   C Y N 304 
PHE   CD1  C Y N 305 
PHE   CD2  C Y N 306 
PHE   CE1  C Y N 307 
PHE   CE2  C Y N 308 
PHE   CZ   C Y N 309 
PHE   OXT  O N N 310 
PHE   H    H N N 311 
PHE   H2   H N N 312 
PHE   HA   H N N 313 
PHE   HB2  H N N 314 
PHE   HB3  H N N 315 
PHE   HD1  H N N 316 
PHE   HD2  H N N 317 
PHE   HE1  H N N 318 
PHE   HE2  H N N 319 
PHE   HZ   H N N 320 
PHE   HXT  H N N 321 
PRO   N    N N N 322 
PRO   CA   C N S 323 
PRO   C    C N N 324 
PRO   O    O N N 325 
PRO   CB   C N N 326 
PRO   CG   C N N 327 
PRO   CD   C N N 328 
PRO   OXT  O N N 329 
PRO   H    H N N 330 
PRO   HA   H N N 331 
PRO   HB2  H N N 332 
PRO   HB3  H N N 333 
PRO   HG2  H N N 334 
PRO   HG3  H N N 335 
PRO   HD2  H N N 336 
PRO   HD3  H N N 337 
PRO   HXT  H N N 338 
SER   N    N N N 339 
SER   CA   C N S 340 
SER   C    C N N 341 
SER   O    O N N 342 
SER   CB   C N N 343 
SER   OG   O N N 344 
SER   OXT  O N N 345 
SER   H    H N N 346 
SER   H2   H N N 347 
SER   HA   H N N 348 
SER   HB2  H N N 349 
SER   HB3  H N N 350 
SER   HG   H N N 351 
SER   HXT  H N N 352 
SO4   S    S N N 353 
SO4   O1   O N N 354 
SO4   O2   O N N 355 
SO4   O3   O N N 356 
SO4   O4   O N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1BGX C1  O1   sing N N 1   
A1BGX O1  C2   sing N N 2   
A1BGX C2  C3   doub Y N 3   
A1BGX C3  N1   sing Y N 4   
A1BGX N1  C4   doub Y N 5   
A1BGX C4  C5   sing Y N 6   
A1BGX C5  C6   sing N N 7   
A1BGX C6  C7   doub Y N 8   
A1BGX C7  C8   sing Y N 9   
A1BGX C8  C9   doub Y N 10  
A1BGX C9  C10  sing Y N 11  
A1BGX C10 C11  doub Y N 12  
A1BGX C11 C12  sing N N 13  
A1BGX C12 O2   doub N N 14  
A1BGX C12 N2   sing N N 15  
A1BGX N2  C13  sing N N 16  
A1BGX C13 C14  sing Y N 17  
A1BGX C14 N3   doub Y N 18  
A1BGX N3  N4   sing Y N 19  
A1BGX N4  C15  sing N N 20  
A1BGX N4  C16  sing Y N 21  
A1BGX C5  C17  doub Y N 22  
A1BGX C2  C17  sing Y N 23  
A1BGX C6  C11  sing Y N 24  
A1BGX C13 C16  doub Y N 25  
A1BGX C4  H5   sing N N 26  
A1BGX C7  H6   sing N N 27  
A1BGX C8  H7   sing N N 28  
A1BGX C10 H9   sing N N 29  
A1BGX C15 H12  sing N N 30  
A1BGX C15 H14  sing N N 31  
A1BGX C15 H13  sing N N 32  
A1BGX C17 H16  sing N N 33  
A1BGX C1  H3   sing N N 34  
A1BGX C1  H1   sing N N 35  
A1BGX C1  H2   sing N N 36  
A1BGX C3  H4   sing N N 37  
A1BGX C9  H8   sing N N 38  
A1BGX N2  H10  sing N N 39  
A1BGX C14 H11  sing N N 40  
A1BGX C16 H15  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
SO4   S   O1   doub N N 340 
SO4   S   O2   doub N N 341 
SO4   S   O3   sing N N 342 
SO4   S   O4   sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease 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                    7HOO 
_atom_sites.fract_transf_matrix[1][1]   0.023555 
_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]   0.023555 
_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]   0.004619 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -20.620 19.272  -7.592  1.00 56.54  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -21.906 18.584  -7.658  1.00 56.36  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.019 17.772  -8.948  1.00 54.04  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -21.758 18.296  -10.037 1.00 54.96  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.052 19.585  -7.568  1.00 59.94  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.332 18.918  -7.133  1.00 67.63  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.314 18.225  -6.085  1.00 68.83  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.354 19.072  -7.845  1.00 71.01  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.417 16.505  -8.830  1.00 50.81  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.478 15.629  -9.986  1.00 48.11  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.873 15.367  -10.521 1.00 45.80  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.830 15.228  -9.758  1.00 45.75  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.767 14.315  -9.697  1.00 47.61  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.317 14.498  -9.398  1.00 48.12  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.476 12.919  -9.184  1.00 48.26  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.783 13.517  -9.122  1.00 51.30  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.974 15.310  -11.849 1.00 43.45  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.227 15.063  -12.536 1.00 43.33  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.075 14.050  -13.672 1.00 42.86  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.970 13.851  -14.181 1.00 42.60  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.887 16.376  -13.006 1.00 43.37  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.111 17.167  -14.043 1.00 44.93  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.169 18.113  -13.663 1.00 46.40  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.368 17.015  -15.402 1.00 46.60  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.472 18.861  -14.607 1.00 48.13  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.672 17.754  -16.359 1.00 48.14  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.723 18.678  -15.956 1.00 49.64  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.997 19.398  -16.891 1.00 52.35  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.174 13.386  -14.052 1.00 42.27  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.141 12.411  -15.135 1.00 42.42  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.939 12.885  -16.375 1.00 43.07  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.901 13.653  -16.244 1.00 43.18  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.557 10.995  -14.671 1.00 42.86  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.016 10.956  -14.180 1.00 42.84  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.584 10.425  -13.607 1.00 43.05  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.499 9.495   -13.936 1.00 44.18  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.513 12.429  -17.573 1.00 43.74  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.137 12.780  -18.859 1.00 45.09  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.225 11.508  -19.679 1.00 45.34  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.206 10.821  -19.809 1.00 45.37  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.242 13.742  -19.664 1.00 47.57  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.205 15.186  -19.212 1.00 53.35  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.321 16.068  -20.082 1.00 60.91  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.511 15.531  -20.876 1.00 63.30  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.431 17.308  -19.957 1.00 62.73  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.389 11.217  -20.306 1.00 45.40  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.480 9.994   -21.116 1.00 46.39  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.526 10.056  -22.310 1.00 46.29  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.307 11.137  -22.844 1.00 47.21  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.914 9.695   -21.557 1.00 48.45  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.088 8.230   -21.944 1.00 51.70  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.527 7.750   -21.854 1.00 55.87  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.626 6.320   -22.154 1.00 57.51  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.723 5.823   -23.387 1.00 58.25  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.756 6.634   -24.437 1.00 60.15  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.766 4.510   -23.580 1.00 54.44  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.869 8.933   -22.651 1.00 45.91  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.947 8.874   -23.783 1.00 46.58  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.307 7.814   -24.835 1.00 47.15  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.766 7.855   -25.930 1.00 47.75  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.507 8.710   -23.332 1.00 46.82  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.221 6.902   -24.515 1.00 47.23  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.669 5.907   -25.476 1.00 47.73  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.303 4.670   -24.889 1.00 47.95  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.428 4.542   -23.665 1.00 47.58  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.709 3.749   -25.785 1.00 48.91  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.269 2.438   -25.461 1.00 50.15  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.108 1.461   -25.348 1.00 51.65  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.109 1.591   -26.064 1.00 52.95  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.177 1.910   -26.592 1.00 51.95  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.568 2.504   -26.675 1.00 57.23  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.816 3.522   -26.013 1.00 56.48  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.397 1.982   -27.469 1.00 60.57  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.276 0.430   -24.533 1.00 51.35  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.269 -0.614  -24.409 1.00 52.01  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.675 -1.740  -25.344 1.00 53.64  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.583 -2.515  -25.028 1.00 53.16  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.175 -1.043  -22.954 1.00 51.95  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.688 0.138   -22.099 1.00 52.10  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.281 -2.248  -22.816 1.00 52.20  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.758 -0.077  -20.631 1.00 53.03  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.045 -1.798  -26.529 0.25 54.09  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.025 -1.819  -26.512 0.25 53.99  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -27.045 -1.798  -26.529 0.25 54.10  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -27.029 -1.822  -26.514 0.25 54.00  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.305 -2.828  -27.537 0.25 55.00  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.342 -2.814  -27.535 0.25 54.79  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.305 -2.829  -27.537 0.25 55.01  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.347 -2.826  -27.528 0.25 54.79  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -26.007 -3.296  -28.189 0.25 56.04  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.068 -3.258  -28.275 0.25 55.99  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -26.007 -3.296  -28.189 0.25 56.06  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.077 -3.258  -28.281 0.25 55.99  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.053 -2.525  -28.305 0.25 56.20  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.160 -2.452  -28.471 0.25 56.20  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.053 -2.525  -28.304 0.25 56.21  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.178 -2.443  -28.486 0.25 56.20  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.255 -2.327  -28.658 0.25 56.11  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.418 -2.227  -28.479 0.25 55.59  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.255 -2.327  -28.658 0.25 56.11  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.463 -2.275  -28.451 0.25 55.57  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.621 -1.306  -29.437 0.25 56.93  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.613 -1.978  -27.732 0.25 56.17  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.621 -1.306  -29.437 0.25 56.93  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.665 -2.118  -27.692 0.25 56.15  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.611 -1.856  -28.144 0.25 56.47  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.739 -3.123  -29.657 0.25 55.76  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.611 -1.856  -28.144 0.25 56.48  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.736 -3.150  -29.656 0.25 55.75  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.990 -4.539  -28.668 1.00 56.64  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.834 -5.056  -29.403 1.00 60.36  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.005 -4.518  -30.852 1.00 65.72  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.118 -4.568  -31.394 1.00 66.40  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.881 -6.586  -29.438 1.00 59.63  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.808 -7.221  -30.274 1.00 59.68  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.876 -7.542  -31.602 1.00 60.70  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.548 -7.713  -29.805 1.00 59.44  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.714 -8.159  -31.996 1.00 60.96  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.887 -8.290  -30.906 1.00 60.28  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.897 -7.688  -28.566 1.00 59.31  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.619 -8.858  -30.796 1.00 60.64  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.650 -8.263  -28.457 1.00 60.22  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.020 -8.834  -29.561 1.00 60.52  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -23.931 -4.003  -31.459 0.17 66.57  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -23.933 -3.999  -31.461 0.17 66.60  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -23.924 -4.000  -31.457 0.33 66.52  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -23.924 -4.000  -31.457 0.33 66.52  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.013 -3.483  -32.820 0.17 67.97  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.024 -3.482  -32.823 0.17 68.02  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -23.973 -3.479  -32.821 0.33 67.90  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -23.973 -3.479  -32.821 0.33 67.90  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.282 -4.386  -33.801 0.17 69.38  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.282 -4.372  -33.807 0.17 69.40  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.283 -4.430  -33.785 0.33 69.32  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.283 -4.430  -33.785 0.33 69.32  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.094 -4.649  -33.627 0.17 69.48  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.091 -4.620  -33.637 0.17 69.49  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -22.106 -4.729  -33.608 0.33 69.41  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -22.106 -4.729  -33.608 0.33 69.41  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.496 -2.041  -32.892 0.17 70.04  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.557 -2.024  -32.902 0.17 70.18  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.307 -2.095  -32.920 0.33 69.95  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.307 -2.095  -32.920 0.33 69.95  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.404 -1.050  -32.185 0.17 74.18  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.423 -1.080  -32.085 0.17 74.47  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.430 -1.485  -34.309 0.33 74.09  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.430 -1.485  -34.309 0.33 74.09  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.772 -0.873  -32.814 0.17 80.12  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.873 -0.978  -32.517 0.17 80.67  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.335 -0.522  -34.726 0.33 78.81  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.335 -0.522  -34.726 0.33 78.81  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -26.761 -0.746  -32.057 0.17 80.86  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -26.752 -0.909  -31.627 0.17 81.60  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -21.553 -0.091  -33.850 0.33 79.93  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -21.553 -0.091  -33.850 0.33 79.93  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -25.856 -0.855  -34.064 0.17 82.04  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.132 -0.958  -33.742 0.17 82.82  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.263 -0.194  -35.933 0.33 80.31  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.263 -0.194  -35.933 0.33 80.31  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -23.997 -4.881  -34.819 1.00 70.38  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.413 -5.766  -35.823 1.00 74.44  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -22.512 -4.923  -36.712 1.00 76.73  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -22.876 -3.797  -37.063 1.00 77.25  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -24.512 -6.425  -36.675 1.00 78.70  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -25.381 -7.420  -35.909 1.00 85.01  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -26.642 -7.756  -36.707 1.00 90.34  ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -27.202 -9.114  -36.364 1.00 94.73  ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -28.132 -9.593  -37.422 1.00 97.54  ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -21.320 -5.432  -37.016 1.00 77.82  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -20.355 -4.704  -37.840 1.00 79.59  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -19.801 -3.471  -37.121 1.00 78.67  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -19.621 -2.414  -37.724 1.00 78.96  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -20.906 -4.356  -39.241 1.00 84.29  ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -21.042 -5.546  -40.172 1.00 93.62  ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -19.998 -6.143  -40.531 1.00 96.43  ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -22.188 -5.859  -40.573 1.00 96.57  ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -19.536 -3.612  -35.818 1.00 77.15  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -18.881 -2.556  -35.059 1.00 76.01  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.374 -2.651  -35.392 1.00 75.16  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -16.902 -3.698  -35.855 1.00 74.96  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -19.084 -2.794  -33.569 1.00 75.86  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -16.608 -1.582  -35.131 1.00 74.65  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -15.158 -1.602  -35.351 1.00 74.55  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -14.521 -2.660  -34.417 1.00 73.06  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -14.812 -2.669  -33.225 1.00 71.59  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -14.565 -0.217  -35.048 1.00 78.24  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -13.056 -0.157  -35.206 1.00 86.01  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -12.396 0.946   -34.401 1.00 95.72  ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -13.082 1.945   -34.082 1.00 97.11  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -11.190 0.811   -34.091 1.00 99.04  ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -13.730 -3.588  -34.970 1.00 72.50  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -13.108 -4.645  -34.168 1.00 72.28  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -11.634 -4.311  -33.947 1.00 71.33  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -10.886 -4.256  -34.919 1.00 71.76  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.262 -6.056  -34.801 1.00 73.37  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -12.951 -7.134  -33.779 1.00 73.89  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -14.656 -6.271  -35.386 1.00 74.09  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -11.214 -4.063  -32.678 1.00 69.91  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -9.817  -3.717  -32.378 1.00 68.94  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -9.395  -4.202  -30.963 1.00 67.45  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.202 -4.795  -30.269 1.00 66.40  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -9.577  -2.207  -32.619 1.00 70.80  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -8.167  -1.976  -32.706 1.00 72.18  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -10.183 -1.349  -31.536 1.00 71.06  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -8.138  -3.988  -30.573 1.00 66.97  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -7.643  -4.388  -29.267 1.00 67.09  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -7.088  -5.795  -29.254 1.00 66.99  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -7.570  -6.663  -29.983 1.00 67.61  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -6.057  -6.022  -28.441 1.00 65.93  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -5.475  -7.351  -28.303 1.00 65.39  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -6.046  -8.074  -27.031 1.00 63.67  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -6.951  -7.539  -26.391 1.00 62.41  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -3.934  -7.292  -28.380 1.00 67.76  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -3.260  -6.613  -27.210 1.00 72.24  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -3.685  -5.549  -26.743 1.00 73.68  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -2.164  -7.205  -26.732 1.00 73.42  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -5.584  -9.299  -26.709 1.00 62.91  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -6.096  -10.109 -25.588 1.00 63.08  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -4.939  -10.567 -24.667 1.00 62.42  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -4.591  -11.748 -24.637 1.00 62.73  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -6.844  -11.333 -26.126 1.00 65.04  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -7.547  -11.085 -27.336 1.00 68.04  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.314  -9.646  -23.920 1.00 61.34  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -3.150  -10.040 -23.108 1.00 60.73  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.477  -10.832 -21.850 1.00 59.91  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.475  -10.558 -21.186 1.00 59.78  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.489  -8.702  -22.780 1.00 61.64  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -3.660  -7.727  -22.713 1.00 62.05  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -4.603  -8.198  -23.803 1.00 60.68  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -2.631  -11.814 -21.517 1.00 59.41  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -2.775  -12.602 -20.286 1.00 59.89  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -1.737  -12.054 -19.307 1.00 58.62  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -0.542  -12.170 -19.559 1.00 58.73  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -2.582  -14.114 -20.544 1.00 62.94  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -3.732  -14.705 -21.379 1.00 69.19  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -3.742  -16.229 -21.431 1.00 74.82  ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -4.554  -16.730 -22.549 1.00 79.00  ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -5.532  -17.626 -22.428 1.00 81.30  ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -5.825  -18.145 -21.240 1.00 82.84  ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -6.216  -18.018 -23.496 1.00 78.92  ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.191  -11.384 -18.240 1.00 57.16  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.306  -10.706 -17.297 1.00 56.31  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.476  -11.173 -15.856 1.00 55.42  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -2.601  -11.257 -15.387 1.00 55.47  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -1.614  -9.189  -17.343 1.00 56.41  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.497  -8.519  -18.712 1.00 57.48  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -2.141  -7.138  -18.709 1.00 57.68  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? -0.048  -8.449  -19.161 1.00 57.88  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.373  -11.390 -15.127 1.00 54.78  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.452  -11.740 -13.705 1.00 54.54  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.620  -10.444 -12.921 1.00 52.39  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.241   -9.569  -13.006 1.00 52.63  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 0.815   -12.465 -13.245 1.00 58.16  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 1.002   -13.840 -13.861 1.00 66.26  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? 0.015   -14.388 -14.413 1.00 68.19  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 2.134   -14.371 -13.793 1.00 69.44  ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.752  -10.279 -12.220 1.00 49.99  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -2.016  -9.038  -11.504 1.00 48.61  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.349  -9.275  -10.006 1.00 47.81  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.680  -10.389 -9.582  1.00 47.76  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -3.100  -8.156  -12.219 1.00 48.57  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -2.900  -8.100  -13.732 1.00 49.20  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.500  -8.624  -11.888 1.00 48.43  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.224  -8.209  -9.211  1.00 46.28  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.536  -8.208  -7.791  1.00 45.32  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.535  -7.077  -7.556  1.00 44.26  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.464  -6.055  -8.223  1.00 44.06  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.277  -7.979  -6.968  1.00 44.84  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.471  -7.270  -6.631  1.00 43.52  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.479  -6.279  -6.326  1.00 43.25  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.342  -5.912  -4.845  1.00 43.81  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.391  -6.807  -3.978  1.00 44.29  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.865  -6.857  -6.628  1.00 43.03  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.043  -5.986  -6.205  1.00 43.64  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.048  -4.666  -6.938  1.00 43.33  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.352  -6.708  -6.413  1.00 44.25  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -5.059  -4.633  -4.559  1.00 42.95  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.843  -4.224  -3.180  1.00 43.25  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.156  -3.783  -2.494  1.00 43.36  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.200  -3.687  -3.143  1.00 43.44  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.703  -3.179  -3.065  1.00 44.73  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -3.981  -1.760  -3.565  1.00 47.88  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.154  -1.442  -3.847  1.00 46.84  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.026  -0.967  -3.651  1.00 51.05  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.101  -3.553  -1.178  1.00 43.67  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.261  -3.140  -0.413  1.00 43.62  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.899  -1.836  -0.941  1.00 43.31  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.109  -1.675  -0.845  1.00 43.52  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.875  -3.037  1.073   1.00 46.01  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -8.076  -3.029  1.990   1.00 52.43  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.715  -3.015  3.458   1.00 57.36  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.514  -1.910  4.009   1.00 56.45  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.617  -4.111  4.056   1.00 61.55  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.114  -0.942  -1.557  1.00 42.69  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.651  0.302   -2.126  1.00 43.33  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.310  0.132   -3.517  1.00 42.63  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.703  1.130   -4.122  1.00 43.17  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.555  1.354   -2.223  1.00 45.72  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -6.000  1.614   -0.944  1.00 50.51  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.418  -1.098  -4.023  1.00 41.33  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -9.039  -1.330  -5.329  1.00 41.50  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -8.154  -1.008  -6.524  1.00 42.05  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.641  -0.896  -7.652  1.00 42.13  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.832  -0.927  -6.301  1.00 42.15  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.866  -0.673  -7.357  1.00 43.48  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -5.194  -1.961  -7.808  1.00 44.35  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.650  -2.717  -6.999  1.00 44.41  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.782  0.327   -6.899  1.00 45.94  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.287  1.739   -6.677  1.00 52.62  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.401  2.050   -7.138  1.00 54.02  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -4.567  2.530   -6.043  1.00 56.53  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.209  -2.183  -9.111  1.00 44.46  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.543  -3.313  -9.733  1.00 44.98  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.082  -2.972  -9.979  1.00 48.39  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.745  -1.822  -10.281 1.00 48.99  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.225  -3.647  -11.062 1.00 42.64  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.497  -4.442  -10.916 1.00 41.14  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.460  -5.781  -10.566 1.00 40.66  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.733  -3.862  -11.172 1.00 40.93  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.634  -6.520  -10.463 1.00 41.02  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -8.906  -4.609  -11.077 1.00 40.86  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -8.850  -5.931  -10.734 1.00 40.34  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.205  -3.966  -9.857  1.00 50.27  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.788  -3.781  -10.143 1.00 52.64  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.236  -5.030  -10.828 1.00 55.75  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.739  -6.130  -10.591 1.00 55.73  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? 0.000   -3.477  -8.871  1.00 54.07  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? -0.060  -4.528  -7.916  1.00 55.46  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.784   -4.870  -11.690 1.00 58.29  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.376   -6.025  -12.369 1.00 61.30  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.315   -6.784  -11.448 1.00 63.90  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.147   -6.179  -10.779 1.00 64.02  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.155   -5.606  -13.626 1.00 62.04  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.350   -5.147  -14.843 1.00 64.47  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 2.271   -4.939  -16.037 1.00 65.38  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.298   -6.168  -15.230 1.00 65.63  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.213   -8.111  -11.445 1.00 65.93  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 3.114   -8.965  -10.678 1.00 68.40  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 4.107   -9.539  -11.680 1.00 71.30  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.688   -10.088 -12.702 1.00 71.72  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.350   -10.106 -9.967  1.00 68.91  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.316   -11.133 -9.377  1.00 69.45  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.410   -9.556  -8.904  1.00 69.09  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.407   -9.383  -11.431 1.00 73.28  ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.412   -9.924  -12.352 1.00 75.78  ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.420   -10.848 -11.667 1.00 76.79  ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 7.183   -11.334 -10.557 1.00 77.40  ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 7.111   -8.802  -13.130 1.00 79.65  ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.180   -7.990  -14.017 1.00 85.70  ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.301   -8.309  -15.493 1.00 94.23  ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.678   -9.456  -15.826 1.00 95.64  ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 6.025   -7.408  -16.318 1.00 97.67  ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.288 12.539  -11.994 1.00 58.34  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.525 12.720  -13.224 1.00 58.85  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -35.674 11.588  -14.226 1.00 58.84  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -36.718 10.928  -14.263 1.00 59.96  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -34.640 11.354  -15.057 1.00 57.02  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -34.703 10.280  -16.045 1.00 55.62  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.302 8.925   -15.469 1.00 53.88  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.195 8.767   -14.951 1.00 54.60  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -33.891 10.605  -17.311 1.00 57.87  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -34.286 9.732   -18.489 1.00 62.41  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -33.653 10.110  -19.814 1.00 69.11  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -32.636 10.841  -19.793 1.00 69.34  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -34.194 9.709   -20.874 1.00 70.96  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.203 7.944   -15.554 0.25 53.36  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.203 7.942   -15.545 0.25 53.11  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.203 7.944   -15.554 0.25 53.36  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.203 7.942   -15.545 0.25 53.11  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -34.923 6.603   -15.026 0.25 53.28  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -34.918 6.597   -15.040 0.25 52.78  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -34.923 6.603   -15.026 0.25 53.28  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -34.918 6.597   -15.040 0.25 52.78  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -34.998 5.510   -16.118 0.25 52.54  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -34.959 5.513   -16.121 0.25 52.30  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -34.998 5.510   -16.118 0.25 52.54  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -34.959 5.513   -16.121 0.25 52.30  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -35.004 4.323   -15.793 0.25 52.74  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -34.921 4.329   -15.787 0.25 52.49  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -35.004 4.323   -15.793 0.25 52.74  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -34.921 4.329   -15.787 0.25 52.49  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -35.807 6.263   -13.790 0.25 55.03  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -35.868 6.237   -13.898 0.25 53.89  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -35.807 6.263   -13.790 0.25 55.03  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -35.868 6.237   -13.898 0.25 53.89  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -36.301 7.447   -13.152 0.25 56.35  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.213 6.377   -14.355 0.25 54.63  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -36.301 7.447   -13.152 0.25 56.35  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.213 6.377   -14.355 0.25 54.63  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.065 5.419   -12.757 0.25 55.54  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -35.630 7.077   -12.653 0.25 54.28  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.065 5.419   -12.757 0.25 55.54  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -35.630 7.077   -12.653 0.25 54.28  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -35.033 5.900   -17.404 1.00 51.54  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -35.084 4.956   -18.508 1.00 48.54  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -33.767 4.196   -18.572 1.00 45.37  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -32.704 4.792   -18.353 1.00 45.68  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -35.218 5.766   -19.850 1.00 50.07  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.218 6.784   -19.738 1.00 51.81  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -35.536 4.893   -21.053 1.00 50.63  ? 19  THR   B CG2 1 
ATOM   401  N N   A ASP   B 2 11  ? -33.826 2.888   -18.873 0.25 44.68  ? 20  ASP   B N   1 
ATOM   402  N N   B ASP   B 2 11  ? -33.826 2.888   -18.873 0.25 44.68  ? 20  ASP   B N   1 
ATOM   403  N N   C ASP   B 2 11  ? -33.825 2.888   -18.873 0.25 44.67  ? 20  ASP   B N   1 
ATOM   404  N N   D ASP   B 2 11  ? -33.825 2.888   -18.873 0.25 44.67  ? 20  ASP   B N   1 
ATOM   405  C CA  A ASP   B 2 11  ? -32.646 2.039   -19.029 0.25 44.71  ? 20  ASP   B CA  1 
ATOM   406  C CA  B ASP   B 2 11  ? -32.647 2.039   -19.030 0.25 44.71  ? 20  ASP   B CA  1 
ATOM   407  C CA  C ASP   B 2 11  ? -32.644 2.041   -19.033 0.25 44.69  ? 20  ASP   B CA  1 
ATOM   408  C CA  D ASP   B 2 11  ? -32.644 2.041   -19.033 0.25 44.69  ? 20  ASP   B CA  1 
ATOM   409  C C   A ASP   B 2 11  ? -31.708 2.611   -20.100 0.25 44.63  ? 20  ASP   B C   1 
ATOM   410  C C   B ASP   B 2 11  ? -31.708 2.610   -20.100 0.25 44.63  ? 20  ASP   B C   1 
ATOM   411  C C   C ASP   B 2 11  ? -31.707 2.615   -20.100 0.25 44.62  ? 20  ASP   B C   1 
ATOM   412  C C   D ASP   B 2 11  ? -31.707 2.615   -20.100 0.25 44.62  ? 20  ASP   B C   1 
ATOM   413  O O   A ASP   B 2 11  ? -32.176 3.174   -21.086 0.25 44.72  ? 20  ASP   B O   1 
ATOM   414  O O   B ASP   B 2 11  ? -32.176 3.174   -21.087 0.25 44.72  ? 20  ASP   B O   1 
ATOM   415  O O   C ASP   B 2 11  ? -32.173 3.180   -21.086 0.25 44.71  ? 20  ASP   B O   1 
ATOM   416  O O   D ASP   B 2 11  ? -32.173 3.180   -21.086 0.25 44.71  ? 20  ASP   B O   1 
ATOM   417  C CB  A ASP   B 2 11  ? -33.062 0.617   -19.445 0.25 46.32  ? 20  ASP   B CB  1 
ATOM   418  C CB  B ASP   B 2 11  ? -33.063 0.617   -19.446 0.25 46.33  ? 20  ASP   B CB  1 
ATOM   419  C CB  C ASP   B 2 11  ? -33.057 0.622   -19.456 0.25 46.27  ? 20  ASP   B CB  1 
ATOM   420  C CB  D ASP   B 2 11  ? -33.057 0.622   -19.456 0.25 46.27  ? 20  ASP   B CB  1 
ATOM   421  C CG  A ASP   B 2 11  ? -33.815 -0.171  -18.392 0.25 50.44  ? 20  ASP   B CG  1 
ATOM   422  C CG  B ASP   B 2 11  ? -33.814 -0.171  -18.392 0.25 50.44  ? 20  ASP   B CG  1 
ATOM   423  C CG  C ASP   B 2 11  ? -33.349 -0.323  -18.312 0.25 50.30  ? 20  ASP   B CG  1 
ATOM   424  C CG  D ASP   B 2 11  ? -33.349 -0.323  -18.312 0.25 50.30  ? 20  ASP   B CG  1 
ATOM   425  O OD1 A ASP   B 2 11  ? -33.840 0.271   -17.227 0.25 50.63  ? 20  ASP   B OD1 1 
ATOM   426  O OD1 B ASP   B 2 11  ? -33.837 0.271   -17.226 0.25 50.63  ? 20  ASP   B OD1 1 
ATOM   427  O OD1 C ASP   B 2 11  ? -33.765 0.158   -17.238 0.25 50.49  ? 20  ASP   B OD1 1 
ATOM   428  O OD1 D ASP   B 2 11  ? -33.765 0.158   -17.238 0.25 50.49  ? 20  ASP   B OD1 1 
ATOM   429  O OD2 A ASP   B 2 11  ? -34.366 -1.242  -18.734 0.25 52.49  ? 20  ASP   B OD2 1 
ATOM   430  O OD2 B ASP   B 2 11  ? -34.368 -1.241  -18.734 0.25 52.49  ? 20  ASP   B OD2 1 
ATOM   431  O OD2 C ASP   B 2 11  ? -33.173 -1.550  -18.497 0.25 52.23  ? 20  ASP   B OD2 1 
ATOM   432  O OD2 D ASP   B 2 11  ? -33.173 -1.550  -18.497 0.25 52.23  ? 20  ASP   B OD2 1 
ATOM   433  N N   . GLY   B 2 12  ? -30.407 2.467   -19.897 1.00 44.19  ? 21  GLY   B N   1 
ATOM   434  C CA  . GLY   B 2 12  ? -29.425 2.963   -20.849 1.00 42.80  ? 21  GLY   B CA  1 
ATOM   435  C C   . GLY   B 2 12  ? -28.110 3.352   -20.222 1.00 40.73  ? 21  GLY   B C   1 
ATOM   436  O O   . GLY   B 2 12  ? -27.904 3.153   -19.016 1.00 39.33  ? 21  GLY   B O   1 
ATOM   437  N N   . VAL   B 2 13  ? -27.200 3.887   -21.058 1.00 39.35  ? 22  VAL   B N   1 
ATOM   438  C CA  . VAL   B 2 13  ? -25.885 4.351   -20.632 1.00 38.43  ? 22  VAL   B CA  1 
ATOM   439  C C   . VAL   B 2 13  ? -25.955 5.872   -20.437 1.00 38.19  ? 22  VAL   B C   1 
ATOM   440  O O   . VAL   B 2 13  ? -26.651 6.573   -21.189 1.00 39.19  ? 22  VAL   B O   1 
ATOM   441  C CB  . VAL   B 2 13  ? -24.790 3.898   -21.622 1.00 38.65  ? 22  VAL   B CB  1 
ATOM   442  C CG1 . VAL   B 2 13  ? -24.955 4.546   -23.010 1.00 39.56  ? 22  VAL   B CG1 1 
ATOM   443  C CG2 . VAL   B 2 13  ? -23.400 4.131   -21.066 1.00 38.08  ? 22  VAL   B CG2 1 
ATOM   444  N N   . TYR   B 2 14  ? -25.302 6.374   -19.386 1.00 36.83  ? 23  TYR   B N   1 
ATOM   445  C CA  . TYR   B 2 14  ? -25.351 7.782   -19.035 1.00 37.64  ? 23  TYR   B CA  1 
ATOM   446  C C   . TYR   B 2 14  ? -23.963 8.350   -18.766 1.00 37.73  ? 23  TYR   B C   1 
ATOM   447  O O   . TYR   B 2 14  ? -23.092 7.650   -18.273 1.00 38.19  ? 23  TYR   B O   1 
ATOM   448  C CB  . TYR   B 2 14  ? -26.205 7.981   -17.757 1.00 37.88  ? 23  TYR   B CB  1 
ATOM   449  C CG  . TYR   B 2 14  ? -27.701 7.818   -17.928 1.00 38.04  ? 23  TYR   B CG  1 
ATOM   450  C CD1 . TYR   B 2 14  ? -28.262 6.568   -18.159 1.00 38.77  ? 23  TYR   B CD1 1 
ATOM   451  C CD2 . TYR   B 2 14  ? -28.561 8.880   -17.718 1.00 39.24  ? 23  TYR   B CD2 1 
ATOM   452  C CE1 . TYR   B 2 14  ? -29.634 6.397   -18.247 1.00 39.67  ? 23  TYR   B CE1 1 
ATOM   453  C CE2 . TYR   B 2 14  ? -29.937 8.733   -17.855 1.00 40.43  ? 23  TYR   B CE2 1 
ATOM   454  C CZ  . TYR   B 2 14  ? -30.472 7.483   -18.095 1.00 41.66  ? 23  TYR   B CZ  1 
ATOM   455  O OH  . TYR   B 2 14  ? -31.831 7.304   -18.202 1.00 44.27  ? 23  TYR   B OH  1 
ATOM   456  N N   . ARG   B 2 15  ? -23.789 9.649   -19.011 1.00 37.52  ? 24  ARG   B N   1 
ATOM   457  C CA  . ARG   B 2 15  ? -22.544 10.333  -18.676 1.00 37.54  ? 24  ARG   B CA  1 
ATOM   458  C C   . ARG   B 2 15  ? -22.656 10.850  -17.243 1.00 37.91  ? 24  ARG   B C   1 
ATOM   459  O O   . ARG   B 2 15  ? -23.727 11.261  -16.841 1.00 37.60  ? 24  ARG   B O   1 
ATOM   460  C CB  . ARG   B 2 15  ? -22.316 11.541  -19.590 1.00 37.17  ? 24  ARG   B CB  1 
ATOM   461  C CG  . ARG   B 2 15  ? -22.169 11.191  -21.077 1.00 38.94  ? 24  ARG   B CG  1 
ATOM   462  C CD  . ARG   B 2 15  ? -22.113 12.489  -21.880 1.00 40.89  ? 24  ARG   B CD  1 
ATOM   463  N NE  . ARG   B 2 15  ? -22.352 12.248  -23.300 1.00 41.95  ? 24  ARG   B NE  1 
ATOM   464  C CZ  . ARG   B 2 15  ? -21.411 11.927  -24.183 1.00 43.58  ? 24  ARG   B CZ  1 
ATOM   465  N NH1 . ARG   B 2 15  ? -20.146 11.797  -23.801 1.00 42.38  ? 24  ARG   B NH1 1 
ATOM   466  N NH2 . ARG   B 2 15  ? -21.732 11.702  -25.449 1.00 45.02  ? 24  ARG   B NH2 1 
ATOM   467  N N   . VAL   B 2 16  ? -21.551 10.883  -16.513 1.00 37.94  ? 25  VAL   B N   1 
ATOM   468  C CA  . VAL   B 2 16  ? -21.450 11.416  -15.167 1.00 38.47  ? 25  VAL   B CA  1 
ATOM   469  C C   . VAL   B 2 16  ? -20.638 12.694  -15.263 1.00 39.03  ? 25  VAL   B C   1 
ATOM   470  O O   . VAL   B 2 16  ? -19.457 12.667  -15.577 1.00 39.57  ? 25  VAL   B O   1 
ATOM   471  C CB  . VAL   B 2 16  ? -20.785 10.416  -14.189 1.00 39.94  ? 25  VAL   B CB  1 
ATOM   472  C CG1 . VAL   B 2 16  ? -20.785 10.997  -12.778 1.00 40.21  ? 25  VAL   B CG1 1 
ATOM   473  C CG2 . VAL   B 2 16  ? -21.478 9.046   -14.227 1.00 40.35  ? 25  VAL   B CG2 1 
ATOM   474  N N   . MET   B 2 17  ? -21.284 13.820  -15.050 1.00 39.86  ? 26  MET   B N   1 
ATOM   475  C CA  . MET   B 2 17  ? -20.691 15.132  -15.218 1.00 41.23  ? 26  MET   B CA  1 
ATOM   476  C C   . MET   B 2 17  ? -20.506 15.880  -13.900 1.00 44.32  ? 26  MET   B C   1 
ATOM   477  O O   . MET   B 2 17  ? -21.224 15.630  -12.936 1.00 44.21  ? 26  MET   B O   1 
ATOM   478  C CB  . MET   B 2 17  ? -21.638 15.970  -16.098 1.00 40.49  ? 26  MET   B CB  1 
ATOM   479  C CG  . MET   B 2 17  ? -22.106 15.282  -17.373 1.00 42.84  ? 26  MET   B CG  1 
ATOM   480  S SD  . MET   B 2 17  ? -20.761 15.107  -18.565 1.00 45.37  ? 26  MET   B SD  1 
ATOM   481  C CE  . MET   B 2 17  ? -20.393 16.856  -18.873 1.00 41.36  ? 26  MET   B CE  1 
ATOM   482  N N   . THR   B 2 18  ? -19.624 16.888  -13.898 1.00 46.62  ? 27  THR   B N   1 
ATOM   483  C CA  . THR   B 2 18  ? -19.424 17.764  -12.756 1.00 49.58  ? 27  THR   B CA  1 
ATOM   484  C C   . THR   B 2 18  ? -19.243 19.222  -13.227 1.00 52.19  ? 27  THR   B C   1 
ATOM   485  O O   . THR   B 2 18  ? -18.633 19.462  -14.274 1.00 51.83  ? 27  THR   B O   1 
ATOM   486  C CB  . THR   B 2 18  ? -18.248 17.274  -11.882 1.00 51.32  ? 27  THR   B CB  1 
ATOM   487  O OG1 . THR   B 2 18  ? -18.161 18.114  -10.724 1.00 53.28  ? 27  THR   B OG1 1 
ATOM   488  C CG2 . THR   B 2 18  ? -16.910 17.277  -12.627 1.00 51.01  ? 27  THR   B CG2 1 
ATOM   489  N N   . ARG   B 2 19  ? -19.777 20.193  -12.467 1.00 54.35  ? 28  ARG   B N   1 
ATOM   490  C CA  . ARG   B 2 19  ? -19.582 21.614  -12.768 1.00 56.96  ? 28  ARG   B CA  1 
ATOM   491  C C   . ARG   B 2 19  ? -18.623 22.324  -11.773 1.00 59.00  ? 28  ARG   B C   1 
ATOM   492  O O   . ARG   B 2 19  ? -18.487 23.548  -11.817 1.00 59.21  ? 28  ARG   B O   1 
ATOM   493  C CB  . ARG   B 2 19  ? -20.913 22.362  -12.893 1.00 59.34  ? 28  ARG   B CB  1 
ATOM   494  C CG  . ARG   B 2 19  ? -21.466 22.340  -14.314 1.00 64.15  ? 28  ARG   B CG  1 
ATOM   495  C CD  . ARG   B 2 19  ? -22.807 23.019  -14.389 1.00 68.53  ? 28  ARG   B CD  1 
ATOM   496  N NE  . ARG   B 2 19  ? -23.551 22.658  -15.598 1.00 73.17  ? 28  ARG   B NE  1 
ATOM   497  C CZ  . ARG   B 2 19  ? -24.788 22.168  -15.595 1.00 76.92  ? 28  ARG   B CZ  1 
ATOM   498  N NH1 . ARG   B 2 19  ? -25.427 21.960  -14.448 1.00 77.65  ? 28  ARG   B NH1 1 
ATOM   499  N NH2 . ARG   B 2 19  ? -25.395 21.877  -16.739 1.00 76.81  ? 28  ARG   B NH2 1 
ATOM   500  N N   . ARG   B 2 20  ? -17.941 21.549  -10.914 1.00 60.64  ? 29  ARG   B N   1 
ATOM   501  C CA  . ARG   B 2 20  ? -17.008 22.036  -9.895  1.00 62.66  ? 29  ARG   B CA  1 
ATOM   502  C C   . ARG   B 2 20  ? -15.741 22.592  -10.547 1.00 63.37  ? 29  ARG   B C   1 
ATOM   503  O O   . ARG   B 2 20  ? -15.248 23.650  -10.148 1.00 64.06  ? 29  ARG   B O   1 
ATOM   504  C CB  . ARG   B 2 20  ? -16.671 20.892  -8.913  1.00 65.20  ? 29  ARG   B CB  1 
ATOM   505  C CG  . ARG   B 2 20  ? -15.600 21.235  -7.881  1.00 70.44  ? 29  ARG   B CG  1 
ATOM   506  C CD  . ARG   B 2 20  ? -15.291 20.062  -6.970  1.00 75.11  ? 29  ARG   B CD  1 
ATOM   507  N NE  . ARG   B 2 20  ? -14.636 18.954  -7.675  1.00 79.56  ? 29  ARG   B NE  1 
ATOM   508  C CZ  . ARG   B 2 20  ? -13.336 18.678  -7.595  1.00 82.92  ? 29  ARG   B CZ  1 
ATOM   509  N NH1 . ARG   B 2 20  ? -12.530 19.441  -6.865  1.00 83.04  ? 29  ARG   B NH1 1 
ATOM   510  N NH2 . ARG   B 2 20  ? -12.827 17.650  -8.265  1.00 82.91  ? 29  ARG   B NH2 1 
ATOM   511  N N   . LEU   B 2 21  ? -15.248 21.900  -11.580 1.00 62.81  ? 30  LEU   B N   1 
ATOM   512  C CA  . LEU   B 2 21  ? -14.045 22.279  -12.326 1.00 62.57  ? 30  LEU   B CA  1 
ATOM   513  C C   . LEU   B 2 21  ? -14.382 23.304  -13.459 1.00 61.61  ? 30  LEU   B C   1 
ATOM   514  O O   . LEU   B 2 21  ? -15.464 23.903  -13.434 1.00 61.78  ? 30  LEU   B O   1 
ATOM   515  C CB  . LEU   B 2 21  ? -13.408 20.972  -12.872 1.00 63.25  ? 30  LEU   B CB  1 
ATOM   516  C CG  . LEU   B 2 21  ? -12.326 20.233  -12.048 1.00 65.27  ? 30  LEU   B CG  1 
ATOM   517  C CD1 . LEU   B 2 21  ? -12.428 20.475  -10.538 1.00 66.14  ? 30  LEU   B CD1 1 
ATOM   518  C CD2 . LEU   B 2 21  ? -12.352 18.746  -12.329 1.00 66.02  ? 30  LEU   B CD2 1 
ATOM   519  N N   . LEU   B 2 22  ? -13.462 23.536  -14.427 1.00 60.39  ? 31  LEU   B N   1 
ATOM   520  C CA  . LEU   B 2 22  ? -13.702 24.467  -15.538 1.00 59.50  ? 31  LEU   B CA  1 
ATOM   521  C C   . LEU   B 2 22  ? -14.817 23.905  -16.430 1.00 58.24  ? 31  LEU   B C   1 
ATOM   522  O O   . LEU   B 2 22  ? -14.791 22.715  -16.735 1.00 58.61  ? 31  LEU   B O   1 
ATOM   523  C CB  . LEU   B 2 22  ? -12.409 24.624  -16.347 1.00 59.84  ? 31  LEU   B CB  1 
ATOM   524  C CG  . LEU   B 2 22  ? -12.415 25.683  -17.428 1.00 61.07  ? 31  LEU   B CG  1 
ATOM   525  C CD1 . LEU   B 2 22  ? -12.324 27.090  -16.834 1.00 61.20  ? 31  LEU   B CD1 1 
ATOM   526  C CD2 . LEU   B 2 22  ? -11.278 25.451  -18.408 1.00 61.69  ? 31  LEU   B CD2 1 
ATOM   527  N N   . GLY   B 2 23  ? -15.812 24.732  -16.782 1.00 56.55  ? 32  GLY   B N   1 
ATOM   528  C CA  . GLY   B 2 23  ? -16.960 24.302  -17.582 1.00 55.20  ? 32  GLY   B CA  1 
ATOM   529  C C   . GLY   B 2 23  ? -17.665 23.062  -17.037 1.00 53.91  ? 32  GLY   B C   1 
ATOM   530  O O   . GLY   B 2 23  ? -17.722 22.853  -15.820 1.00 53.56  ? 32  GLY   B O   1 
ATOM   531  N N   . SER   B 2 24  ? -18.212 22.232  -17.936 1.00 52.63  ? 33  SER   B N   1 
ATOM   532  C CA  . SER   B 2 24  ? -18.849 20.971  -17.550 1.00 51.91  ? 33  SER   B CA  1 
ATOM   533  C C   . SER   B 2 24  ? -17.862 19.893  -17.920 1.00 50.32  ? 33  SER   B C   1 
ATOM   534  O O   . SER   B 2 24  ? -17.481 19.802  -19.085 1.00 50.25  ? 33  SER   B O   1 
ATOM   535  C CB  . SER   B 2 24  ? -20.145 20.749  -18.323 1.00 53.61  ? 33  SER   B CB  1 
ATOM   536  O OG  . SER   B 2 24  ? -21.214 21.491  -17.757 1.00 56.86  ? 33  SER   B OG  1 
ATOM   537  N N   . THR   B 2 25  ? -17.412 19.106  -16.940 1.00 48.95  ? 34  THR   B N   1 
ATOM   538  C CA  . THR   B 2 25  ? -16.413 18.075  -17.168 1.00 47.82  ? 34  THR   B CA  1 
ATOM   539  C C   . THR   B 2 25  ? -16.986 16.681  -16.961 1.00 46.64  ? 34  THR   B C   1 
ATOM   540  O O   . THR   B 2 25  ? -17.683 16.441  -15.971 1.00 45.89  ? 34  THR   B O   1 
ATOM   541  C CB  . THR   B 2 25  ? -15.196 18.308  -16.242 1.00 48.67  ? 34  THR   B CB  1 
ATOM   542  O OG1 . THR   B 2 25  ? -14.735 19.659  -16.376 1.00 49.83  ? 34  THR   B OG1 1 
ATOM   543  C CG2 . THR   B 2 25  ? -14.051 17.326  -16.506 1.00 48.37  ? 34  THR   B CG2 1 
ATOM   544  N N   . GLN   B 2 26  ? -16.677 15.751  -17.878 1.00 45.74  ? 35  GLN   B N   1 
ATOM   545  C CA  . GLN   B 2 26  ? -17.139 14.374  -17.722 1.00 44.96  ? 35  GLN   B CA  1 
ATOM   546  C C   . GLN   B 2 26  ? -16.160 13.559  -16.874 1.00 45.61  ? 35  GLN   B C   1 
ATOM   547  O O   . GLN   B 2 26  ? -15.035 13.272  -17.314 1.00 46.23  ? 35  GLN   B O   1 
ATOM   548  C CB  . GLN   B 2 26  ? -17.383 13.700  -19.077 1.00 43.85  ? 35  GLN   B CB  1 
ATOM   549  C CG  . GLN   B 2 26  ? -17.979 12.300  -18.931 1.00 43.30  ? 35  GLN   B CG  1 
ATOM   550  C CD  . GLN   B 2 26  ? -18.279 11.664  -20.262 1.00 44.04  ? 35  GLN   B CD  1 
ATOM   551  O OE1 . GLN   B 2 26  ? -18.951 12.256  -21.104 1.00 44.78  ? 35  GLN   B OE1 1 
ATOM   552  N NE2 . GLN   B 2 26  ? -17.825 10.435  -20.472 1.00 42.41  ? 35  GLN   B NE2 1 
ATOM   553  N N   . VAL   B 2 27  ? -16.588 13.167  -15.665 1.00 44.58  ? 36  VAL   B N   1 
ATOM   554  C CA  . VAL   B 2 27  ? -15.721 12.364  -14.790 1.00 43.81  ? 36  VAL   B CA  1 
ATOM   555  C C   . VAL   B 2 27  ? -15.892 10.847  -14.997 1.00 42.31  ? 36  VAL   B C   1 
ATOM   556  O O   . VAL   B 2 27  ? -15.023 10.074  -14.587 1.00 42.44  ? 36  VAL   B O   1 
ATOM   557  C CB  . VAL   B 2 27  ? -15.875 12.761  -13.310 1.00 44.73  ? 36  VAL   B CB  1 
ATOM   558  C CG1 . VAL   B 2 27  ? -15.227 14.118  -13.052 1.00 45.72  ? 36  VAL   B CG1 1 
ATOM   559  C CG2 . VAL   B 2 27  ? -17.341 12.776  -12.898 1.00 44.53  ? 36  VAL   B CG2 1 
ATOM   560  N N   . GLY   B 2 28  ? -16.975 10.431  -15.648 1.00 40.60  ? 37  GLY   B N   1 
ATOM   561  C CA  . GLY   B 2 28  ? -17.202 9.018   -15.914 1.00 39.26  ? 37  GLY   B CA  1 
ATOM   562  C C   . GLY   B 2 28  ? -18.524 8.715   -16.578 1.00 38.42  ? 37  GLY   B C   1 
ATOM   563  O O   . GLY   B 2 28  ? -19.170 9.600   -17.132 1.00 39.25  ? 37  GLY   B O   1 
ATOM   564  N N   . VAL   B 2 29  ? -18.912 7.442   -16.559 1.00 37.15  ? 38  VAL   B N   1 
ATOM   565  C CA  . VAL   B 2 29  ? -20.085 6.885   -17.220 1.00 36.93  ? 38  VAL   B CA  1 
ATOM   566  C C   . VAL   B 2 29  ? -20.786 5.862   -16.310 1.00 36.45  ? 38  VAL   B C   1 
ATOM   567  O O   . VAL   B 2 29  ? -20.169 5.328   -15.383 1.00 35.86  ? 38  VAL   B O   1 
ATOM   568  C CB  . VAL   B 2 29  ? -19.630 6.220   -18.558 1.00 37.29  ? 38  VAL   B CB  1 
ATOM   569  C CG1 . VAL   B 2 29  ? -20.769 5.524   -19.275 1.00 37.43  ? 38  VAL   B CG1 1 
ATOM   570  C CG2 . VAL   B 2 29  ? -18.964 7.228   -19.486 1.00 37.17  ? 38  VAL   B CG2 1 
ATOM   571  N N   . GLY   B 2 30  ? -22.073 5.620   -16.550 1.00 35.21  ? 39  GLY   B N   1 
ATOM   572  C CA  . GLY   B 2 30  ? -22.811 4.628   -15.787 1.00 35.23  ? 39  GLY   B CA  1 
ATOM   573  C C   . GLY   B 2 30  ? -23.941 3.958   -16.539 1.00 35.94  ? 39  GLY   B C   1 
ATOM   574  O O   . GLY   B 2 30  ? -24.291 4.366   -17.656 1.00 37.01  ? 39  GLY   B O   1 
ATOM   575  N N   . VAL   B 2 31  ? -24.523 2.923   -15.925 1.00 34.01  ? 40  VAL   B N   1 
ATOM   576  C CA  . VAL   B 2 31  ? -25.605 2.121   -16.478 1.00 34.28  ? 40  VAL   B CA  1 
ATOM   577  C C   . VAL   B 2 31  ? -26.861 2.211   -15.631 1.00 34.79  ? 40  VAL   B C   1 
ATOM   578  O O   . VAL   B 2 31  ? -26.827 1.872   -14.430 1.00 34.21  ? 40  VAL   B O   1 
ATOM   579  C CB  . VAL   B 2 31  ? -25.159 0.633   -16.594 1.00 35.91  ? 40  VAL   B CB  1 
ATOM   580  C CG1 . VAL   B 2 31  ? -26.331 -0.254  -17.008 1.00 37.70  ? 40  VAL   B CG1 1 
ATOM   581  C CG2 . VAL   B 2 31  ? -23.997 0.486   -17.571 1.00 35.99  ? 40  VAL   B CG2 1 
ATOM   582  N N   . MET   B 2 32  ? -27.981 2.617   -16.247 1.00 34.03  ? 41  MET   B N   1 
ATOM   583  C CA  . MET   B 2 32  ? -29.261 2.627   -15.578 1.00 34.64  ? 41  MET   B CA  1 
ATOM   584  C C   . MET   B 2 32  ? -29.968 1.312   -16.006 1.00 35.70  ? 41  MET   B C   1 
ATOM   585  O O   . MET   B 2 32  ? -30.129 1.042   -17.207 1.00 35.58  ? 41  MET   B O   1 
ATOM   586  C CB  . MET   B 2 32  ? -30.062 3.873   -16.002 1.00 34.35  ? 41  MET   B CB  1 
ATOM   587  C CG  . MET   B 2 32  ? -31.342 4.095   -15.221 1.00 35.59  ? 41  MET   B CG  1 
ATOM   588  S SD  . MET   B 2 32  ? -30.955 4.615   -13.523 1.00 39.15  ? 41  MET   B SD  1 
ATOM   589  C CE  . MET   B 2 32  ? -30.696 6.375   -13.785 1.00 37.15  ? 41  MET   B CE  1 
ATOM   590  N N   . GLN   B 2 33  ? -30.320 0.472   -15.033 1.00 35.10  ? 42  GLN   B N   1 
ATOM   591  C CA  . GLN   B 2 33  ? -31.020 -0.771  -15.308 1.00 36.62  ? 42  GLN   B CA  1 
ATOM   592  C C   . GLN   B 2 33  ? -31.917 -1.069  -14.145 1.00 37.96  ? 42  GLN   B C   1 
ATOM   593  O O   . GLN   B 2 33  ? -31.469 -0.996  -12.987 1.00 37.88  ? 42  GLN   B O   1 
ATOM   594  C CB  . GLN   B 2 33  ? -30.071 -1.969  -15.566 1.00 38.41  ? 42  GLN   B CB  1 
ATOM   595  C CG  . GLN   B 2 33  ? -30.870 -3.210  -15.982 1.00 43.14  ? 42  GLN   B CG  1 
ATOM   596  C CD  . GLN   B 2 33  ? -30.019 -4.372  -16.427 1.00 48.97  ? 42  GLN   B CD  1 
ATOM   597  O OE1 . GLN   B 2 33  ? -30.148 -5.499  -15.924 1.00 52.26  ? 42  GLN   B OE1 1 
ATOM   598  N NE2 . GLN   B 2 33  ? -29.115 -4.119  -17.366 1.00 46.91  ? 42  GLN   B NE2 1 
ATOM   599  N N   . GLU   B 2 34  ? -33.198 -1.345  -14.431 1.00 38.92  ? 43  GLU   B N   1 
ATOM   600  C CA  . GLU   B 2 34  ? -34.221 -1.646  -13.421 1.00 40.44  ? 43  GLU   B CA  1 
ATOM   601  C C   . GLU   B 2 34  ? -34.348 -0.580  -12.327 1.00 41.39  ? 43  GLU   B C   1 
ATOM   602  O O   . GLU   B 2 34  ? -34.526 -0.919  -11.155 1.00 42.62  ? 43  GLU   B O   1 
ATOM   603  C CB  . GLU   B 2 34  ? -33.992 -3.043  -12.811 1.00 43.75  ? 43  GLU   B CB  1 
ATOM   604  C CG  . GLU   B 2 34  ? -34.043 -4.162  -13.838 1.00 48.54  ? 43  GLU   B CG  1 
ATOM   605  C CD  . GLU   B 2 34  ? -33.395 -5.465  -13.408 1.00 56.02  ? 43  GLU   B CD  1 
ATOM   606  O OE1 . GLU   B 2 34  ? -33.770 -5.989  -12.335 1.00 57.84  ? 43  GLU   B OE1 1 
ATOM   607  O OE2 . GLU   B 2 34  ? -32.508 -5.960  -14.140 1.00 59.00  ? 43  GLU   B OE2 1 
ATOM   608  N N   . GLY   B 2 35  ? -34.246 0.696   -12.702 1.00 40.09  ? 44  GLY   B N   1 
ATOM   609  C CA  . GLY   B 2 35  ? -34.343 1.794   -11.750 1.00 39.42  ? 44  GLY   B CA  1 
ATOM   610  C C   . GLY   B 2 35  ? -33.131 2.011   -10.851 1.00 37.76  ? 44  GLY   B C   1 
ATOM   611  O O   . GLY   B 2 35  ? -33.187 2.829   -9.927  1.00 37.94  ? 44  GLY   B O   1 
ATOM   612  N N   . VAL   B 2 36  ? -32.020 1.311   -11.126 1.00 35.85  ? 45  VAL   B N   1 
ATOM   613  C CA  . VAL   B 2 36  ? -30.786 1.418   -10.351 1.00 35.24  ? 45  VAL   B CA  1 
ATOM   614  C C   . VAL   B 2 36  ? -29.656 1.925   -11.259 1.00 34.59  ? 45  VAL   B C   1 
ATOM   615  O O   . VAL   B 2 36  ? -29.510 1.447   -12.407 1.00 35.12  ? 45  VAL   B O   1 
ATOM   616  C CB  . VAL   B 2 36  ? -30.453 0.038   -9.697  1.00 35.99  ? 45  VAL   B CB  1 
ATOM   617  C CG1 . VAL   B 2 36  ? -29.010 -0.021  -9.179  1.00 36.20  ? 45  VAL   B CG1 1 
ATOM   618  C CG2 . VAL   B 2 36  ? -31.445 -0.266  -8.576  1.00 36.75  ? 45  VAL   B CG2 1 
ATOM   619  N N   . PHE   B 2 37  ? -28.900 2.930   -10.768 1.00 32.92  ? 46  PHE   B N   1 
ATOM   620  C CA  . PHE   B 2 37  ? -27.777 3.479   -11.513 1.00 32.81  ? 46  PHE   B CA  1 
ATOM   621  C C   . PHE   B 2 37  ? -26.482 2.823   -11.007 1.00 32.37  ? 46  PHE   B C   1 
ATOM   622  O O   . PHE   B 2 37  ? -26.212 2.814   -9.811  1.00 31.62  ? 46  PHE   B O   1 
ATOM   623  C CB  . PHE   B 2 37  ? -27.720 5.012   -11.388 1.00 32.41  ? 46  PHE   B CB  1 
ATOM   624  C CG  . PHE   B 2 37  ? -26.691 5.603   -12.325 1.00 32.55  ? 46  PHE   B CG  1 
ATOM   625  C CD1 . PHE   B 2 37  ? -26.832 5.487   -13.697 1.00 32.51  ? 46  PHE   B CD1 1 
ATOM   626  C CD2 . PHE   B 2 37  ? -25.565 6.234   -11.831 1.00 33.31  ? 46  PHE   B CD2 1 
ATOM   627  C CE1 . PHE   B 2 37  ? -25.884 6.031   -14.566 1.00 33.72  ? 46  PHE   B CE1 1 
ATOM   628  C CE2 . PHE   B 2 37  ? -24.603 6.750   -12.695 1.00 33.74  ? 46  PHE   B CE2 1 
ATOM   629  C CZ  . PHE   B 2 37  ? -24.785 6.673   -14.058 1.00 33.98  ? 46  PHE   B CZ  1 
ATOM   630  N N   . HIS   B 2 38  ? -25.709 2.236   -11.929 1.00 31.93  ? 47  HIS   B N   1 
ATOM   631  C CA  . HIS   B 2 38  ? -24.487 1.507   -11.627 1.00 31.90  ? 47  HIS   B CA  1 
ATOM   632  C C   . HIS   B 2 38  ? -23.281 2.241   -12.184 1.00 33.56  ? 47  HIS   B C   1 
ATOM   633  O O   . HIS   B 2 38  ? -23.248 2.528   -13.389 1.00 34.49  ? 47  HIS   B O   1 
ATOM   634  C CB  . HIS   B 2 38  ? -24.528 0.134   -12.334 1.00 31.22  ? 47  HIS   B CB  1 
ATOM   635  C CG  . HIS   B 2 38  ? -25.740 -0.680  -12.013 1.00 33.33  ? 47  HIS   B CG  1 
ATOM   636  N ND1 . HIS   B 2 38  ? -26.985 -0.350  -12.517 1.00 34.76  ? 47  HIS   B ND1 1 
ATOM   637  C CD2 . HIS   B 2 38  ? -25.863 -1.785  -11.234 1.00 34.21  ? 47  HIS   B CD2 1 
ATOM   638  C CE1 . HIS   B 2 38  ? -27.828 -1.246  -12.020 1.00 35.52  ? 47  HIS   B CE1 1 
ATOM   639  N NE2 . HIS   B 2 38  ? -27.194 -2.134  -11.247 1.00 35.83  ? 47  HIS   B NE2 1 
ATOM   640  N N   . THR   B 2 39  ? -22.249 2.471   -11.343 1.00 33.04  ? 48  THR   B N   1 
ATOM   641  C CA  . THR   B 2 39  ? -21.026 3.082   -11.871 1.00 33.64  ? 48  THR   B CA  1 
ATOM   642  C C   . THR   B 2 39  ? -19.793 2.562   -11.081 1.00 34.12  ? 48  THR   B C   1 
ATOM   643  O O   . THR   B 2 39  ? -19.916 1.678   -10.211 1.00 34.32  ? 48  THR   B O   1 
ATOM   644  C CB  . THR   B 2 39  ? -21.172 4.643   -11.969 1.00 34.19  ? 48  THR   B CB  1 
ATOM   645  O OG1 . THR   B 2 39  ? -20.061 5.162   -12.709 1.00 33.75  ? 48  THR   B OG1 1 
ATOM   646  C CG2 . THR   B 2 39  ? -21.279 5.321   -10.597 1.00 35.20  ? 48  THR   B CG2 1 
ATOM   647  N N   . MET   B 2 40  ? -18.598 3.095   -11.398 1.00 34.61  ? 49  MET   B N   1 
ATOM   648  C CA  . MET   B 2 40  ? -17.396 2.726   -10.665 1.00 34.11  ? 49  MET   B CA  1 
ATOM   649  C C   . MET   B 2 40  ? -17.206 3.687   -9.499  1.00 34.14  ? 49  MET   B C   1 
ATOM   650  O O   . MET   B 2 40  ? -17.477 4.886   -9.626  1.00 33.79  ? 49  MET   B O   1 
ATOM   651  C CB  . MET   B 2 40  ? -16.172 2.709   -11.584 1.00 34.75  ? 49  MET   B CB  1 
ATOM   652  C CG  . MET   B 2 40  ? -16.399 1.924   -12.889 1.00 37.29  ? 49  MET   B CG  1 
ATOM   653  S SD  . MET   B 2 40  ? -14.909 1.098   -13.471 1.00 44.59  ? 49  MET   B SD  1 
ATOM   654  C CE  . MET   B 2 40  ? -14.827 -0.290  -12.341 1.00 43.24  ? 49  MET   B CE  1 
ATOM   655  N N   A TRP   B 2 41  ? -16.737 3.170   -8.354  0.50 34.44  ? 50  TRP   B N   1 
ATOM   656  N N   D TRP   B 2 41  ? -16.751 3.170   -8.351  0.50 33.85  ? 50  TRP   B N   1 
ATOM   657  C CA  A TRP   B 2 41  ? -16.527 3.971   -7.151  0.50 35.48  ? 50  TRP   B CA  1 
ATOM   658  C CA  D TRP   B 2 41  ? -16.551 3.986   -7.157  0.50 34.31  ? 50  TRP   B CA  1 
ATOM   659  C C   A TRP   B 2 41  ? -15.603 5.158   -7.400  0.50 35.14  ? 50  TRP   B C   1 
ATOM   660  C C   D TRP   B 2 41  ? -15.606 5.164   -7.402  0.50 34.59  ? 50  TRP   B C   1 
ATOM   661  O O   A TRP   B 2 41  ? -15.897 6.241   -6.926  0.50 34.56  ? 50  TRP   B O   1 
ATOM   662  O O   D TRP   B 2 41  ? -15.901 6.254   -6.941  0.50 33.98  ? 50  TRP   B O   1 
ATOM   663  C CB  A TRP   B 2 41  ? -16.017 3.123   -5.961  0.50 36.37  ? 50  TRP   B CB  1 
ATOM   664  C CB  D TRP   B 2 41  ? -16.104 3.146   -5.936  0.50 34.35  ? 50  TRP   B CB  1 
ATOM   665  C CG  A TRP   B 2 41  ? -16.080 3.855   -4.654  0.50 38.41  ? 50  TRP   B CG  1 
ATOM   666  C CG  D TRP   B 2 41  ? -15.976 3.966   -4.688  0.50 35.30  ? 50  TRP   B CG  1 
ATOM   667  C CD1 A TRP   B 2 41  ? -17.121 3.865   -3.774  0.50 39.49  ? 50  TRP   B CD1 1 
ATOM   668  C CD1 D TRP   B 2 41  ? -14.917 4.742   -4.320  0.50 36.18  ? 50  TRP   B CD1 1 
ATOM   669  C CD2 A TRP   B 2 41  ? -15.075 4.721   -4.098  0.50 39.33  ? 50  TRP   B CD2 1 
ATOM   670  C CD2 D TRP   B 2 41  ? -16.957 4.110   -3.654  0.50 35.43  ? 50  TRP   B CD2 1 
ATOM   671  N NE1 A TRP   B 2 41  ? -16.838 4.699   -2.717  0.50 40.31  ? 50  TRP   B NE1 1 
ATOM   672  N NE1 D TRP   B 2 41  ? -15.196 5.395   -3.146  0.50 36.33  ? 50  TRP   B NE1 1 
ATOM   673  C CE2 A TRP   B 2 41  ? -15.587 5.236   -2.892  0.50 40.35  ? 50  TRP   B CE2 1 
ATOM   674  C CE2 D TRP   B 2 41  ? -16.440 5.020   -2.709  0.50 36.30  ? 50  TRP   B CE2 1 
ATOM   675  C CE3 A TRP   B 2 41  ? -13.793 5.113   -4.508  0.50 40.31  ? 50  TRP   B CE3 1 
ATOM   676  C CE3 D TRP   B 2 41  ? -18.239 3.592   -3.454  0.50 36.19  ? 50  TRP   B CE3 1 
ATOM   677  C CZ2 A TRP   B 2 41  ? -14.853 6.105   -2.080  0.50 41.60  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -17.140 5.380   -1.554  0.50 36.95  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.077 5.988   -3.714  0.50 41.45  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 D TRP   B 2 41  ? -18.926 3.940   -2.301  0.50 37.19  ? 50  TRP   B CZ3 1 
ATOM   681  C CH2 A TRP   B 2 41  ? -13.602 6.470   -2.515  0.50 41.78  ? 50  TRP   B CH2 1 
ATOM   682  C CH2 D TRP   B 2 41  ? -18.386 4.841   -1.379  0.50 37.06  ? 50  TRP   B CH2 1 
ATOM   683  N N   . HIS   B 2 42  ? -14.502 4.972   -8.150  1.00 34.88  ? 51  HIS   B N   1 
ATOM   684  C CA  . HIS   B 2 42  ? -13.562 6.090   -8.386  1.00 35.93  ? 51  HIS   B CA  1 
ATOM   685  C C   . HIS   B 2 42  ? -14.185 7.266   -9.205  1.00 37.20  ? 51  HIS   B C   1 
ATOM   686  O O   . HIS   B 2 42  ? -13.655 8.373   -9.158  1.00 38.21  ? 51  HIS   B O   1 
ATOM   687  C CB  . HIS   B 2 42  ? -12.227 5.635   -8.967  1.00 36.44  ? 51  HIS   B CB  1 
ATOM   688  C CG  . HIS   B 2 42  ? -12.299 5.282   -10.412 1.00 37.88  ? 51  HIS   B CG  1 
ATOM   689  N ND1 . HIS   B 2 42  ? -12.567 3.984   -10.827 1.00 39.49  ? 51  HIS   B ND1 1 
ATOM   690  C CD2 . HIS   B 2 42  ? -12.166 6.076   -11.503 1.00 38.65  ? 51  HIS   B CD2 1 
ATOM   691  C CE1 . HIS   B 2 42  ? -12.529 4.021   -12.151 1.00 39.69  ? 51  HIS   B CE1 1 
ATOM   692  N NE2 . HIS   B 2 42  ? -12.320 5.265   -12.602 1.00 39.41  ? 51  HIS   B NE2 1 
ATOM   693  N N   . VAL   B 2 43  ? -15.347 7.056   -9.859  1.00 36.29  ? 52  VAL   B N   1 
ATOM   694  C CA  . VAL   B 2 43  ? -16.003 8.120   -10.605 1.00 36.55  ? 52  VAL   B CA  1 
ATOM   695  C C   . VAL   B 2 43  ? -16.703 9.133   -9.675  1.00 37.10  ? 52  VAL   B C   1 
ATOM   696  O O   . VAL   B 2 43  ? -16.506 10.348  -9.825  1.00 37.73  ? 52  VAL   B O   1 
ATOM   697  C CB  . VAL   B 2 43  ? -16.977 7.535   -11.662 1.00 37.44  ? 52  VAL   B CB  1 
ATOM   698  C CG1 . VAL   B 2 43  ? -17.885 8.623   -12.259 1.00 37.70  ? 52  VAL   B CG1 1 
ATOM   699  C CG2 . VAL   B 2 43  ? -16.217 6.794   -12.764 1.00 37.49  ? 52  VAL   B CG2 1 
ATOM   700  N N   . THR   B 2 44  ? -17.543 8.644   -8.744  1.00 35.15  ? 53  THR   B N   1 
ATOM   701  C CA  . THR   B 2 44  ? -18.315 9.530   -7.861  1.00 35.69  ? 53  THR   B CA  1 
ATOM   702  C C   . THR   B 2 44  ? -17.769 9.639   -6.439  1.00 36.44  ? 53  THR   B C   1 
ATOM   703  O O   . THR   B 2 44  ? -18.169 10.543  -5.708  1.00 36.84  ? 53  THR   B O   1 
ATOM   704  C CB  . THR   B 2 44  ? -19.770 9.015   -7.748  1.00 35.64  ? 53  THR   B CB  1 
ATOM   705  O OG1 . THR   B 2 44  ? -19.769 7.757   -7.055  1.00 35.58  ? 53  THR   B OG1 1 
ATOM   706  C CG2 . THR   B 2 44  ? -20.436 8.828   -9.113  1.00 36.17  ? 53  THR   B CG2 1 
ATOM   707  N N   . LYS   B 2 45  ? -16.932 8.681   -6.025  1.00 36.82  ? 54  LYS   B N   1 
ATOM   708  C CA  . LYS   B 2 45  ? -16.420 8.520   -4.651  1.00 38.92  ? 54  LYS   B CA  1 
ATOM   709  C C   . LYS   B 2 45  ? -17.600 8.335   -3.642  1.00 39.57  ? 54  LYS   B C   1 
ATOM   710  O O   . LYS   B 2 45  ? -17.488 8.714   -2.472  1.00 40.70  ? 54  LYS   B O   1 
ATOM   711  C CB  . LYS   B 2 45  ? -15.497 9.680   -4.215  1.00 43.15  ? 54  LYS   B CB  1 
ATOM   712  C CG  . LYS   B 2 45  ? -14.476 10.146  -5.251  1.00 49.54  ? 54  LYS   B CG  1 
ATOM   713  C CD  . LYS   B 2 45  ? -13.424 9.116   -5.624  1.00 56.86  ? 54  LYS   B CD  1 
ATOM   714  C CE  . LYS   B 2 45  ? -12.312 9.809   -6.397  1.00 62.80  ? 54  LYS   B CE  1 
ATOM   715  N NZ  . LYS   B 2 45  ? -11.613 8.904   -7.360  1.00 65.82  ? 54  LYS   B NZ  1 
ATOM   716  N N   . GLY   B 2 46  ? -18.721 7.793   -4.111  1.00 39.22  ? 55  GLY   B N   1 
ATOM   717  C CA  . GLY   B 2 46  ? -19.902 7.583   -3.287  1.00 39.78  ? 55  GLY   B CA  1 
ATOM   718  C C   . GLY   B 2 46  ? -20.775 8.806   -3.081  1.00 40.77  ? 55  GLY   B C   1 
ATOM   719  O O   . GLY   B 2 46  ? -21.690 8.758   -2.264  1.00 41.36  ? 55  GLY   B O   1 
ATOM   720  N N   . ALA   B 2 47  ? -20.499 9.931   -3.774  1.00 40.81  ? 56  ALA   B N   1 
ATOM   721  C CA  . ALA   B 2 47  ? -21.308 11.145  -3.601  1.00 40.43  ? 56  ALA   B CA  1 
ATOM   722  C C   . ALA   B 2 47  ? -22.692 11.001  -4.243  1.00 40.54  ? 56  ALA   B C   1 
ATOM   723  O O   . ALA   B 2 47  ? -22.852 10.220  -5.163  1.00 40.09  ? 56  ALA   B O   1 
ATOM   724  C CB  . ALA   B 2 47  ? -20.588 12.349  -4.195  1.00 40.39  ? 56  ALA   B CB  1 
ATOM   725  N N   . ALA   B 2 48  ? -23.676 11.793  -3.801  1.00 40.82  ? 57  ALA   B N   1 
ATOM   726  C CA  . ALA   B 2 48  ? -25.010 11.779  -4.390  1.00 41.19  ? 57  ALA   B CA  1 
ATOM   727  C C   . ALA   B 2 48  ? -24.962 12.329  -5.829  1.00 40.89  ? 57  ALA   B C   1 
ATOM   728  O O   . ALA   B 2 48  ? -24.043 13.061  -6.191  1.00 41.17  ? 57  ALA   B O   1 
ATOM   729  C CB  . ALA   B 2 48  ? -25.971 12.622  -3.545  1.00 41.98  ? 57  ALA   B CB  1 
ATOM   730  N N   . LEU   B 2 49  ? -25.953 11.977  -6.644  1.00 39.81  ? 58  LEU   B N   1 
ATOM   731  C CA  . LEU   B 2 49  ? -26.026 12.416  -8.034  1.00 40.15  ? 58  LEU   B CA  1 
ATOM   732  C C   . LEU   B 2 49  ? -27.336 13.130  -8.286  1.00 42.33  ? 58  LEU   B C   1 
ATOM   733  O O   . LEU   B 2 49  ? -28.324 12.883  -7.607  1.00 42.92  ? 58  LEU   B O   1 
ATOM   734  C CB  . LEU   B 2 49  ? -25.936 11.216  -8.997  1.00 39.24  ? 58  LEU   B CB  1 
ATOM   735  C CG  . LEU   B 2 49  ? -24.681 10.370  -8.895  1.00 40.33  ? 58  LEU   B CG  1 
ATOM   736  C CD1 . LEU   B 2 49  ? -24.783 9.150   -9.764  1.00 40.33  ? 58  LEU   B CD1 1 
ATOM   737  C CD2 . LEU   B 2 49  ? -23.465 11.156  -9.266  1.00 41.40  ? 58  LEU   B CD2 1 
ATOM   738  N N   . ARG   B 2 50  ? -27.357 13.971  -9.300  1.00 43.22  ? 59  ARG   B N   1 
ATOM   739  C CA  . ARG   B 2 50  ? -28.538 14.685  -9.718  1.00 45.48  ? 59  ARG   B CA  1 
ATOM   740  C C   . ARG   B 2 50  ? -28.970 14.148  -11.105 1.00 46.64  ? 59  ARG   B C   1 
ATOM   741  O O   . ARG   B 2 50  ? -28.120 13.832  -11.945 1.00 45.55  ? 59  ARG   B O   1 
ATOM   742  C CB  . ARG   B 2 50  ? -28.171 16.171  -9.807  1.00 48.07  ? 59  ARG   B CB  1 
ATOM   743  C CG  . ARG   B 2 50  ? -29.325 17.086  -10.092 1.00 54.30  ? 59  ARG   B CG  1 
ATOM   744  C CD  . ARG   B 2 50  ? -28.997 18.558  -9.855  1.00 59.55  ? 59  ARG   B CD  1 
ATOM   745  N NE  . ARG   B 2 50  ? -27.733 19.003  -10.458 1.00 63.80  ? 59  ARG   B NE  1 
ATOM   746  C CZ  . ARG   B 2 50  ? -27.591 19.358  -11.731 1.00 67.51  ? 59  ARG   B CZ  1 
ATOM   747  N NH1 . ARG   B 2 50  ? -28.619 19.276  -12.570 1.00 66.95  ? 59  ARG   B NH1 1 
ATOM   748  N NH2 . ARG   B 2 50  ? -26.416 19.779  -12.181 1.00 68.89  ? 59  ARG   B NH2 1 
ATOM   749  N N   . SER   B 2 51  ? -30.278 14.017  -11.331 1.00 47.81  ? 60  SER   B N   1 
ATOM   750  C CA  . SER   B 2 51  ? -30.827 13.628  -12.633 1.00 49.89  ? 60  SER   B CA  1 
ATOM   751  C C   . SER   B 2 51  ? -31.986 14.601  -12.858 1.00 52.44  ? 60  SER   B C   1 
ATOM   752  O O   . SER   B 2 51  ? -33.081 14.378  -12.344 1.00 53.16  ? 60  SER   B O   1 
ATOM   753  C CB  . SER   B 2 51  ? -31.340 12.195  -12.599 1.00 50.40  ? 60  SER   B CB  1 
ATOM   754  O OG  . SER   B 2 51  ? -31.848 11.807  -13.863 1.00 51.78  ? 60  SER   B OG  1 
ATOM   755  N N   . GLY   B 2 52  ? -31.712 15.735  -13.495 1.00 53.69  ? 61  GLY   B N   1 
ATOM   756  C CA  . GLY   B 2 52  ? -32.716 16.787  -13.645 1.00 55.23  ? 61  GLY   B CA  1 
ATOM   757  C C   . GLY   B 2 52  ? -32.924 17.418  -12.285 1.00 56.90  ? 61  GLY   B C   1 
ATOM   758  O O   . GLY   B 2 52  ? -31.942 17.768  -11.629 1.00 57.50  ? 61  GLY   B O   1 
ATOM   759  N N   . GLU   B 2 53  ? -34.175 17.477  -11.801 1.00 57.43  ? 62  GLU   B N   1 
ATOM   760  C CA  . GLU   B 2 53  ? -34.433 17.970  -10.448 1.00 58.59  ? 62  GLU   B CA  1 
ATOM   761  C C   . GLU   B 2 53  ? -34.465 16.845  -9.375  1.00 58.35  ? 62  GLU   B C   1 
ATOM   762  O O   . GLU   B 2 53  ? -34.586 17.138  -8.187  1.00 59.04  ? 62  GLU   B O   1 
ATOM   763  C CB  . GLU   B 2 53  ? -35.702 18.837  -10.389 1.00 62.58  ? 62  GLU   B CB  1 
ATOM   764  C CG  . GLU   B 2 53  ? -35.401 20.321  -10.278 1.00 71.23  ? 62  GLU   B CG  1 
ATOM   765  C CD  . GLU   B 2 53  ? -36.615 21.191  -10.013 1.00 84.01  ? 62  GLU   B CD  1 
ATOM   766  O OE1 . GLU   B 2 53  ? -37.704 20.867  -10.545 1.00 87.36  ? 62  GLU   B OE1 1 
ATOM   767  O OE2 . GLU   B 2 53  ? -36.481 22.199  -9.277  1.00 87.01  ? 62  GLU   B OE2 1 
ATOM   768  N N   . GLY   B 2 54  ? -34.312 15.588  -9.790  1.00 57.13  ? 63  GLY   B N   1 
ATOM   769  C CA  . GLY   B 2 54  ? -34.322 14.453  -8.877  1.00 56.40  ? 63  GLY   B CA  1 
ATOM   770  C C   . GLY   B 2 54  ? -32.952 14.108  -8.329  1.00 55.08  ? 63  GLY   B C   1 
ATOM   771  O O   . GLY   B 2 54  ? -31.932 14.382  -8.967  1.00 55.69  ? 63  GLY   B O   1 
ATOM   772  N N   . ARG   B 2 55  ? -32.916 13.515  -7.134  1.00 52.64  ? 64  ARG   B N   1 
ATOM   773  C CA  . ARG   B 2 55  ? -31.661 13.137  -6.503  1.00 50.62  ? 64  ARG   B CA  1 
ATOM   774  C C   . ARG   B 2 55  ? -31.495 11.607  -6.520  1.00 47.94  ? 64  ARG   B C   1 
ATOM   775  O O   . ARG   B 2 55  ? -32.471 10.879  -6.350  1.00 48.66  ? 64  ARG   B O   1 
ATOM   776  C CB  . ARG   B 2 55  ? -31.630 13.667  -5.052  1.00 52.37  ? 64  ARG   B CB  1 
ATOM   777  C CG  . ARG   B 2 55  ? -30.274 13.524  -4.356  1.00 55.11  ? 64  ARG   B CG  1 
ATOM   778  C CD  . ARG   B 2 55  ? -30.334 14.117  -2.961  1.00 57.88  ? 64  ARG   B CD  1 
ATOM   779  N NE  . ARG   B 2 55  ? -29.211 13.704  -2.117  1.00 60.28  ? 64  ARG   B NE  1 
ATOM   780  C CZ  . ARG   B 2 55  ? -28.510 14.533  -1.344  1.00 62.15  ? 64  ARG   B CZ  1 
ATOM   781  N NH1 . ARG   B 2 55  ? -28.788 15.832  -1.326  1.00 60.84  ? 64  ARG   B NH1 1 
ATOM   782  N NH2 . ARG   B 2 55  ? -27.520 14.071  -0.591  1.00 61.73  ? 64  ARG   B NH2 1 
ATOM   783  N N   . LEU   B 2 56  ? -30.265 11.125  -6.736  1.00 44.41  ? 65  LEU   B N   1 
ATOM   784  C CA  . LEU   B 2 56  ? -29.954 9.711   -6.696  1.00 42.60  ? 65  LEU   B CA  1 
ATOM   785  C C   . LEU   B 2 56  ? -29.022 9.527   -5.497  1.00 41.19  ? 65  LEU   B C   1 
ATOM   786  O O   . LEU   B 2 56  ? -27.922 10.085  -5.492  1.00 41.07  ? 65  LEU   B O   1 
ATOM   787  C CB  . LEU   B 2 56  ? -29.205 9.234   -7.970  1.00 41.84  ? 65  LEU   B CB  1 
ATOM   788  C CG  . LEU   B 2 56  ? -29.827 9.373   -9.376  1.00 43.74  ? 65  LEU   B CG  1 
ATOM   789  C CD1 . LEU   B 2 56  ? -29.216 8.323   -10.338 1.00 43.65  ? 65  LEU   B CD1 1 
ATOM   790  C CD2 . LEU   B 2 56  ? -31.355 9.216   -9.374  1.00 45.46  ? 65  LEU   B CD2 1 
ATOM   791  N N   . ASP   B 2 57  ? -29.437 8.749   -4.504  1.00 39.96  ? 66  ASP   B N   1 
ATOM   792  C CA  . ASP   B 2 57  ? -28.607 8.486   -3.335  1.00 39.92  ? 66  ASP   B CA  1 
ATOM   793  C C   . ASP   B 2 57  ? -27.885 7.141   -3.449  1.00 38.94  ? 66  ASP   B C   1 
ATOM   794  O O   . ASP   B 2 57  ? -28.447 6.154   -3.960  1.00 38.94  ? 66  ASP   B O   1 
ATOM   795  C CB  . ASP   B 2 57  ? -29.466 8.525   -2.062  1.00 43.59  ? 66  ASP   B CB  1 
ATOM   796  C CG  . ASP   B 2 57  ? -30.037 9.912   -1.833  1.00 51.17  ? 66  ASP   B CG  1 
ATOM   797  O OD1 . ASP   B 2 57  ? -29.280 10.893  -1.986  1.00 52.41  ? 66  ASP   B OD1 1 
ATOM   798  O OD2 . ASP   B 2 57  ? -31.250 10.017  -1.548  1.00 54.55  ? 66  ASP   B OD2 1 
ATOM   799  N N   . PRO   B 2 58  ? -26.619 7.063   -2.990  1.00 37.86  ? 67  PRO   B N   1 
ATOM   800  C CA  . PRO   B 2 58  ? -25.926 5.766   -3.011  1.00 36.31  ? 67  PRO   B CA  1 
ATOM   801  C C   . PRO   B 2 58  ? -26.676 4.726   -2.164  1.00 35.66  ? 67  PRO   B C   1 
ATOM   802  O O   . PRO   B 2 58  ? -27.297 5.057   -1.143  1.00 35.90  ? 67  PRO   B O   1 
ATOM   803  C CB  . PRO   B 2 58  ? -24.537 6.093   -2.455  1.00 37.10  ? 67  PRO   B CB  1 
ATOM   804  C CG  . PRO   B 2 58  ? -24.742 7.338   -1.632  1.00 38.52  ? 67  PRO   B CG  1 
ATOM   805  C CD  . PRO   B 2 58  ? -25.809 8.115   -2.334  1.00 37.77  ? 67  PRO   B CD  1 
ATOM   806  N N   . TYR   B 2 59  ? -26.609 3.468   -2.576  1.00 34.31  ? 68  TYR   B N   1 
ATOM   807  C CA  . TYR   B 2 59  ? -27.296 2.394   -1.888  1.00 34.38  ? 68  TYR   B CA  1 
ATOM   808  C C   . TYR   B 2 59  ? -26.295 1.321   -1.445  1.00 34.14  ? 68  TYR   B C   1 
ATOM   809  O O   . TYR   B 2 59  ? -26.393 0.803   -0.329  1.00 33.92  ? 68  TYR   B O   1 
ATOM   810  C CB  . TYR   B 2 59  ? -28.361 1.808   -2.818  1.00 34.63  ? 68  TYR   B CB  1 
ATOM   811  C CG  . TYR   B 2 59  ? -29.170 0.692   -2.200  1.00 35.44  ? 68  TYR   B CG  1 
ATOM   812  C CD1 . TYR   B 2 59  ? -28.680 -0.606  -2.159  1.00 36.22  ? 68  TYR   B CD1 1 
ATOM   813  C CD2 . TYR   B 2 59  ? -30.452 0.923   -1.713  1.00 36.30  ? 68  TYR   B CD2 1 
ATOM   814  C CE1 . TYR   B 2 59  ? -29.417 -1.634  -1.599  1.00 36.67  ? 68  TYR   B CE1 1 
ATOM   815  C CE2 . TYR   B 2 59  ? -31.210 -0.107  -1.171  1.00 36.82  ? 68  TYR   B CE2 1 
ATOM   816  C CZ  . TYR   B 2 59  ? -30.692 -1.389  -1.137  1.00 37.28  ? 68  TYR   B CZ  1 
ATOM   817  O OH  . TYR   B 2 59  ? -31.418 -2.423  -0.617  1.00 38.38  ? 68  TYR   B OH  1 
ATOM   818  N N   . TRP   B 2 60  ? -25.356 0.989   -2.315  1.00 33.57  ? 69  TRP   B N   1 
ATOM   819  C CA  . TRP   B 2 60  ? -24.309 0.007   -2.023  1.00 33.18  ? 69  TRP   B CA  1 
ATOM   820  C C   . TRP   B 2 60  ? -23.007 0.454   -2.693  1.00 33.40  ? 69  TRP   B C   1 
ATOM   821  O O   . TRP   B 2 60  ? -23.023 0.957   -3.819  1.00 32.32  ? 69  TRP   B O   1 
ATOM   822  C CB  . TRP   B 2 60  ? -24.716 -1.417  -2.482  1.00 33.37  ? 69  TRP   B CB  1 
ATOM   823  C CG  . TRP   B 2 60  ? -23.573 -2.408  -2.488  1.00 33.52  ? 69  TRP   B CG  1 
ATOM   824  C CD1 . TRP   B 2 60  ? -23.111 -3.139  -1.426  1.00 34.19  ? 69  TRP   B CD1 1 
ATOM   825  C CD2 . TRP   B 2 60  ? -22.679 -2.687  -3.589  1.00 32.36  ? 69  TRP   B CD2 1 
ATOM   826  N NE1 . TRP   B 2 60  ? -22.013 -3.890  -1.813  1.00 34.19  ? 69  TRP   B NE1 1 
ATOM   827  C CE2 . TRP   B 2 60  ? -21.697 -3.582  -3.116  1.00 33.17  ? 69  TRP   B CE2 1 
ATOM   828  C CE3 . TRP   B 2 60  ? -22.609 -2.246  -4.927  1.00 32.51  ? 69  TRP   B CE3 1 
ATOM   829  C CZ2 . TRP   B 2 60  ? -20.676 -4.068  -3.936  1.00 33.08  ? 69  TRP   B CZ2 1 
ATOM   830  C CZ3 . TRP   B 2 60  ? -21.571 -2.701  -5.725  1.00 32.80  ? 69  TRP   B CZ3 1 
ATOM   831  C CH2 . TRP   B 2 60  ? -20.657 -3.646  -5.245  1.00 33.07  ? 69  TRP   B CH2 1 
ATOM   832  N N   . GLY   B 2 61  ? -21.887 0.167   -2.043  1.00 33.64  ? 70  GLY   B N   1 
ATOM   833  C CA  . GLY   B 2 61  ? -20.589 0.492   -2.622  1.00 34.01  ? 70  GLY   B CA  1 
ATOM   834  C C   . GLY   B 2 61  ? -19.477 -0.293  -1.975  1.00 34.32  ? 70  GLY   B C   1 
ATOM   835  O O   . GLY   B 2 61  ? -19.624 -0.746  -0.831  1.00 34.57  ? 70  GLY   B O   1 
ATOM   836  N N   . ASP   B 2 62  ? -18.343 -0.399  -2.684  1.00 33.91  ? 71  ASP   B N   1 
ATOM   837  C CA  . ASP   B 2 62  ? -17.181 -1.131  -2.183  1.00 34.28  ? 71  ASP   B CA  1 
ATOM   838  C C   . ASP   B 2 62  ? -15.957 -0.644  -2.958  1.00 34.18  ? 71  ASP   B C   1 
ATOM   839  O O   . ASP   B 2 62  ? -15.877 -0.803  -4.182  1.00 34.58  ? 71  ASP   B O   1 
ATOM   840  C CB  . ASP   B 2 62  ? -17.389 -2.642  -2.374  1.00 35.33  ? 71  ASP   B CB  1 
ATOM   841  C CG  . ASP   B 2 62  ? -16.328 -3.509  -1.736  1.00 43.13  ? 71  ASP   B CG  1 
ATOM   842  O OD1 . ASP   B 2 62  ? -15.171 -3.463  -2.192  1.00 43.36  ? 71  ASP   B OD1 1 
ATOM   843  O OD2 . ASP   B 2 62  ? -16.661 -4.249  -0.790  1.00 47.57  ? 71  ASP   B OD2 1 
ATOM   844  N N   . VAL   B 2 63  ? -15.007 -0.027  -2.225  1.00 33.95  ? 72  VAL   B N   1 
ATOM   845  C CA  . VAL   B 2 63  ? -13.774 0.521   -2.784  1.00 34.29  ? 72  VAL   B CA  1 
ATOM   846  C C   . VAL   B 2 63  ? -12.893 -0.566  -3.402  1.00 35.25  ? 72  VAL   B C   1 
ATOM   847  O O   . VAL   B 2 63  ? -12.280 -0.312  -4.440  1.00 35.20  ? 72  VAL   B O   1 
ATOM   848  C CB  . VAL   B 2 63  ? -13.020 1.390   -1.744  1.00 34.33  ? 72  VAL   B CB  1 
ATOM   849  C CG1 . VAL   B 2 63  ? -11.565 1.645   -2.129  1.00 35.37  ? 72  VAL   B CG1 1 
ATOM   850  C CG2 . VAL   B 2 63  ? -13.747 2.703   -1.500  1.00 33.61  ? 72  VAL   B CG2 1 
ATOM   851  N N   . LYS   B 2 64  ? -12.866 -1.777  -2.816  1.00 35.75  ? 73  LYS   B N   1 
ATOM   852  C CA  . LYS   B 2 64  ? -11.986 -2.825  -3.381  1.00 36.21  ? 73  LYS   B CA  1 
ATOM   853  C C   . LYS   B 2 64  ? -12.507 -3.359  -4.725  1.00 35.68  ? 73  LYS   B C   1 
ATOM   854  O O   . LYS   B 2 64  ? -11.746 -3.551  -5.660  1.00 36.14  ? 73  LYS   B O   1 
ATOM   855  C CB  . LYS   B 2 64  ? -11.736 -3.957  -2.399  1.00 36.87  ? 73  LYS   B CB  1 
ATOM   856  C CG  . LYS   B 2 64  ? -10.628 -4.866  -2.920  1.00 40.59  ? 73  LYS   B CG  1 
ATOM   857  C CD  . LYS   B 2 64  ? -10.272 -5.892  -1.879  1.00 42.32  ? 73  LYS   B CD  1 
ATOM   858  C CE  . LYS   B 2 64  ? -9.341  -6.909  -2.465  1.00 45.72  ? 73  LYS   B CE  1 
ATOM   859  N NZ  . LYS   B 2 64  ? -9.096  -8.010  -1.499  1.00 47.56  ? 73  LYS   B NZ  1 
ATOM   860  N N   . GLN   B 2 65  ? -13.835 -3.533  -4.829  1.00 35.81  ? 74  GLN   B N   1 
ATOM   861  C CA  . GLN   B 2 65  ? -14.446 -3.923  -6.104  1.00 35.32  ? 74  GLN   B CA  1 
ATOM   862  C C   . GLN   B 2 65  ? -14.461 -2.727  -7.098  1.00 34.96  ? 74  GLN   B C   1 
ATOM   863  O O   . GLN   B 2 65  ? -14.593 -2.941  -8.314  1.00 34.61  ? 74  GLN   B O   1 
ATOM   864  C CB  . GLN   B 2 65  ? -15.888 -4.413  -5.885  1.00 37.51  ? 74  GLN   B CB  1 
ATOM   865  C CG  . GLN   B 2 65  ? -15.986 -5.774  -5.204  1.00 42.92  ? 74  GLN   B CG  1 
ATOM   866  C CD  . GLN   B 2 65  ? -17.423 -6.218  -5.006  1.00 49.60  ? 74  GLN   B CD  1 
ATOM   867  O OE1 . GLN   B 2 65  ? -18.221 -6.314  -5.960  1.00 51.47  ? 74  GLN   B OE1 1 
ATOM   868  N NE2 . GLN   B 2 65  ? -17.783 -6.521  -3.761  1.00 50.54  ? 74  GLN   B NE2 1 
ATOM   869  N N   . ASP   B 2 66  ? -14.391 -1.477  -6.562  1.00 33.99  ? 75  ASP   B N   1 
ATOM   870  C CA  . ASP   B 2 66  ? -14.457 -0.210  -7.289  1.00 34.00  ? 75  ASP   B CA  1 
ATOM   871  C C   . ASP   B 2 66  ? -15.805 -0.097  -7.952  1.00 33.54  ? 75  ASP   B C   1 
ATOM   872  O O   . ASP   B 2 66  ? -15.884 0.347   -9.097  1.00 33.73  ? 75  ASP   B O   1 
ATOM   873  C CB  . ASP   B 2 66  ? -13.294 -0.020  -8.310  1.00 35.30  ? 75  ASP   B CB  1 
ATOM   874  C CG  . ASP   B 2 66  ? -13.191 1.394   -8.848  1.00 37.85  ? 75  ASP   B CG  1 
ATOM   875  O OD1 . ASP   B 2 66  ? -13.480 2.334   -8.089  1.00 37.86  ? 75  ASP   B OD1 1 
ATOM   876  O OD2 . ASP   B 2 66  ? -12.797 1.559   -10.035 1.00 40.31  ? 75  ASP   B OD2 1 
ATOM   877  N N   . LEU   B 2 67  ? -16.888 -0.421  -7.217  1.00 32.35  ? 76  LEU   B N   1 
ATOM   878  C CA  . LEU   B 2 67  ? -18.258 -0.329  -7.755  1.00 32.07  ? 76  LEU   B CA  1 
ATOM   879  C C   . LEU   B 2 67  ? -19.193 0.369   -6.767  1.00 33.32  ? 76  LEU   B C   1 
ATOM   880  O O   . LEU   B 2 67  ? -18.978 0.308   -5.548  1.00 33.39  ? 76  LEU   B O   1 
ATOM   881  C CB  . LEU   B 2 67  ? -18.824 -1.725  -8.036  1.00 31.92  ? 76  LEU   B CB  1 
ATOM   882  C CG  . LEU   B 2 67  ? -18.143 -2.482  -9.168  1.00 32.23  ? 76  LEU   B CG  1 
ATOM   883  C CD1 . LEU   B 2 67  ? -18.631 -3.917  -9.233  1.00 32.86  ? 76  LEU   B CD1 1 
ATOM   884  C CD2 . LEU   B 2 67  ? -18.316 -1.738  -10.519 1.00 30.86  ? 76  LEU   B CD2 1 
ATOM   885  N N   . VAL   B 2 68  ? -20.276 0.969   -7.302  1.00 32.84  ? 77  VAL   B N   1 
ATOM   886  C CA  . VAL   B 2 68  ? -21.306 1.630   -6.490  1.00 32.86  ? 77  VAL   B CA  1 
ATOM   887  C C   . VAL   B 2 68  ? -22.635 1.583   -7.263  1.00 32.23  ? 77  VAL   B C   1 
ATOM   888  O O   . VAL   B 2 68  ? -22.655 1.633   -8.511  1.00 31.49  ? 77  VAL   B O   1 
ATOM   889  C CB  . VAL   B 2 68  ? -20.873 3.086   -6.088  1.00 33.26  ? 77  VAL   B CB  1 
ATOM   890  C CG1 . VAL   B 2 68  ? -20.430 3.883   -7.315  1.00 33.35  ? 77  VAL   B CG1 1 
ATOM   891  C CG2 . VAL   B 2 68  ? -21.956 3.839   -5.297  1.00 33.94  ? 77  VAL   B CG2 1 
ATOM   892  N N   . SER   B 2 69  ? -23.740 1.423   -6.527  1.00 31.13  ? 78  SER   B N   1 
ATOM   893  C CA  . SER   B 2 69  ? -25.089 1.430   -7.102  1.00 31.67  ? 78  SER   B CA  1 
ATOM   894  C C   . SER   B 2 69  ? -25.891 2.526   -6.382  1.00 32.25  ? 78  SER   B C   1 
ATOM   895  O O   . SER   B 2 69  ? -25.652 2.839   -5.184  1.00 31.92  ? 78  SER   B O   1 
ATOM   896  C CB  . SER   B 2 69  ? -25.770 0.060   -6.967  1.00 32.99  ? 78  SER   B CB  1 
ATOM   897  O OG  . SER   B 2 69  ? -26.072 -0.301  -5.626  1.00 35.93  ? 78  SER   B OG  1 
ATOM   898  N N   . TYR   B 2 70  ? -26.864 3.092   -7.092  1.00 31.91  ? 79  TYR   B N   1 
ATOM   899  C CA  . TYR   B 2 70  ? -27.705 4.183   -6.602  1.00 32.87  ? 79  TYR   B CA  1 
ATOM   900  C C   . TYR   B 2 70  ? -29.172 3.779   -6.739  1.00 32.83  ? 79  TYR   B C   1 
ATOM   901  O O   . TYR   B 2 70  ? -29.535 3.161   -7.760  1.00 31.97  ? 79  TYR   B O   1 
ATOM   902  C CB  . TYR   B 2 70  ? -27.460 5.448   -7.469  1.00 33.70  ? 79  TYR   B CB  1 
ATOM   903  C CG  . TYR   B 2 70  ? -26.131 6.115   -7.193  1.00 34.37  ? 79  TYR   B CG  1 
ATOM   904  C CD1 . TYR   B 2 70  ? -24.959 5.640   -7.765  1.00 34.89  ? 79  TYR   B CD1 1 
ATOM   905  C CD2 . TYR   B 2 70  ? -26.046 7.208   -6.342  1.00 35.80  ? 79  TYR   B CD2 1 
ATOM   906  C CE1 . TYR   B 2 70  ? -23.732 6.233   -7.491  1.00 35.63  ? 79  TYR   B CE1 1 
ATOM   907  C CE2 . TYR   B 2 70  ? -24.829 7.807   -6.058  1.00 36.24  ? 79  TYR   B CE2 1 
ATOM   908  C CZ  . TYR   B 2 70  ? -23.671 7.304   -6.620  1.00 36.00  ? 79  TYR   B CZ  1 
ATOM   909  O OH  . TYR   B 2 70  ? -22.483 7.920   -6.335  1.00 36.22  ? 79  TYR   B OH  1 
ATOM   910  N N   . CYS   B 2 71  ? -30.002 4.102   -5.712  1.00 33.60  ? 80  CYS   B N   1 
ATOM   911  C CA  . CYS   B 2 71  ? -31.457 3.866   -5.696  1.00 35.74  ? 80  CYS   B CA  1 
ATOM   912  C C   . CYS   B 2 71  ? -31.862 2.417   -5.391  1.00 36.41  ? 80  CYS   B C   1 
ATOM   913  O O   . CYS   B 2 71  ? -33.048 2.160   -5.152  1.00 38.03  ? 80  CYS   B O   1 
ATOM   914  C CB  . CYS   B 2 71  ? -32.115 4.347   -6.991  1.00 38.65  ? 80  CYS   B CB  1 
ATOM   915  S SG  . CYS   B 2 71  ? -31.721 6.062   -7.449  1.00 44.50  ? 80  CYS   B SG  1 
ATOM   916  N N   . GLY   B 2 72  ? -30.913 1.493   -5.405  1.00 34.66  ? 81  GLY   B N   1 
ATOM   917  C CA  . GLY   B 2 72  ? -31.218 0.090   -5.160  1.00 34.57  ? 81  GLY   B CA  1 
ATOM   918  C C   . GLY   B 2 72  ? -29.981 -0.769  -5.231  1.00 33.87  ? 81  GLY   B C   1 
ATOM   919  O O   . GLY   B 2 72  ? -28.878 -0.279  -5.477  1.00 33.76  ? 81  GLY   B O   1 
ATOM   920  N N   . PRO   B 2 73  ? -30.136 -2.076  -4.977  1.00 33.54  ? 82  PRO   B N   1 
ATOM   921  C CA  . PRO   B 2 73  ? -28.977 -2.965  -5.013  1.00 34.22  ? 82  PRO   B CA  1 
ATOM   922  C C   . PRO   B 2 73  ? -28.456 -3.222  -6.436  1.00 34.85  ? 82  PRO   B C   1 
ATOM   923  O O   . PRO   B 2 73  ? -29.214 -3.049  -7.388  1.00 34.43  ? 82  PRO   B O   1 
ATOM   924  C CB  . PRO   B 2 73  ? -29.520 -4.259  -4.393  1.00 35.12  ? 82  PRO   B CB  1 
ATOM   925  C CG  . PRO   B 2 73  ? -30.973 -4.247  -4.771  1.00 35.16  ? 82  PRO   B CG  1 
ATOM   926  C CD  . PRO   B 2 73  ? -31.380 -2.802  -4.656  1.00 33.42  ? 82  PRO   B CD  1 
ATOM   927  N N   . TRP   B 2 74  ? -27.186 -3.656  -6.574  1.00 35.17  ? 83  TRP   B N   1 
ATOM   928  C CA  . TRP   B 2 74  ? -26.552 -3.997  -7.854  1.00 36.07  ? 83  TRP   B CA  1 
ATOM   929  C C   . TRP   B 2 74  ? -27.409 -5.016  -8.629  1.00 37.08  ? 83  TRP   B C   1 
ATOM   930  O O   . TRP   B 2 74  ? -27.684 -6.088  -8.099  1.00 36.48  ? 83  TRP   B O   1 
ATOM   931  C CB  . TRP   B 2 74  ? -25.137 -4.587  -7.622  1.00 35.67  ? 83  TRP   B CB  1 
ATOM   932  C CG  . TRP   B 2 74  ? -24.336 -4.738  -8.887  1.00 35.17  ? 83  TRP   B CG  1 
ATOM   933  C CD1 . TRP   B 2 74  ? -24.242 -5.847  -9.675  1.00 35.23  ? 83  TRP   B CD1 1 
ATOM   934  C CD2 . TRP   B 2 74  ? -23.509 -3.734  -9.504  1.00 34.56  ? 83  TRP   B CD2 1 
ATOM   935  N NE1 . TRP   B 2 74  ? -23.425 -5.591  -10.758 1.00 35.66  ? 83  TRP   B NE1 1 
ATOM   936  C CE2 . TRP   B 2 74  ? -22.957 -4.302  -10.672 1.00 35.59  ? 83  TRP   B CE2 1 
ATOM   937  C CE3 . TRP   B 2 74  ? -23.189 -2.403  -9.181  1.00 33.54  ? 83  TRP   B CE3 1 
ATOM   938  C CZ2 . TRP   B 2 74  ? -22.141 -3.572  -11.547 1.00 35.14  ? 83  TRP   B CZ2 1 
ATOM   939  C CZ3 . TRP   B 2 74  ? -22.354 -1.696  -10.022 1.00 34.40  ? 83  TRP   B CZ3 1 
ATOM   940  C CH2 . TRP   B 2 74  ? -21.856 -2.271  -11.205 1.00 34.57  ? 83  TRP   B CH2 1 
ATOM   941  N N   . LYS   B 2 75  ? -27.806 -4.691  -9.886  1.00 37.95  ? 84  LYS   B N   1 
ATOM   942  C CA  . LYS   B 2 75  ? -28.694 -5.549  -10.682 1.00 38.82  ? 84  LYS   B CA  1 
ATOM   943  C C   . LYS   B 2 75  ? -27.987 -6.348  -11.770 1.00 40.54  ? 84  LYS   B C   1 
ATOM   944  O O   . LYS   B 2 75  ? -28.587 -7.272  -12.312 1.00 41.68  ? 84  LYS   B O   1 
ATOM   945  C CB  . LYS   B 2 75  ? -29.779 -4.697  -11.376 1.00 39.77  ? 84  LYS   B CB  1 
ATOM   946  C CG  . LYS   B 2 75  ? -30.606 -3.791  -10.457 1.00 41.91  ? 84  LYS   B CG  1 
ATOM   947  C CD  . LYS   B 2 75  ? -31.616 -4.608  -9.660  1.00 45.28  ? 84  LYS   B CD  1 
ATOM   948  C CE  . LYS   B 2 75  ? -32.560 -3.736  -8.866  1.00 48.36  ? 84  LYS   B CE  1 
ATOM   949  N NZ  . LYS   B 2 75  ? -33.654 -4.529  -8.265  1.00 51.30  ? 84  LYS   B NZ  1 
ATOM   950  N N   . LEU   B 2 76  ? -26.761 -5.972  -12.142 1.00 40.25  ? 85  LEU   B N   1 
ATOM   951  C CA  . LEU   B 2 76  ? -26.057 -6.578  -13.268 1.00 41.02  ? 85  LEU   B CA  1 
ATOM   952  C C   . LEU   B 2 76  ? -25.376 -7.880  -12.887 1.00 42.95  ? 85  LEU   B C   1 
ATOM   953  O O   . LEU   B 2 76  ? -24.502 -7.868  -12.026 1.00 42.57  ? 85  LEU   B O   1 
ATOM   954  C CB  . LEU   B 2 76  ? -25.064 -5.567  -13.888 1.00 40.28  ? 85  LEU   B CB  1 
ATOM   955  C CG  . LEU   B 2 76  ? -25.579 -4.107  -14.055 1.00 40.58  ? 85  LEU   B CG  1 
ATOM   956  C CD1 . LEU   B 2 76  ? -24.564 -3.223  -14.707 1.00 40.53  ? 85  LEU   B CD1 1 
ATOM   957  C CD2 . LEU   B 2 76  ? -26.865 -4.046  -14.824 1.00 41.79  ? 85  LEU   B CD2 1 
ATOM   958  N N   . ASP   B 2 77  ? -25.790 -9.009  -13.499 1.00 44.60  ? 86  ASP   B N   1 
ATOM   959  C CA  . ASP   B 2 77  ? -25.202 -10.297 -13.121 1.00 47.38  ? 86  ASP   B CA  1 
ATOM   960  C C   . ASP   B 2 77  ? -24.662 -11.142 -14.282 1.00 47.18  ? 86  ASP   B C   1 
ATOM   961  O O   . ASP   B 2 77  ? -24.134 -12.228 -14.035 1.00 47.86  ? 86  ASP   B O   1 
ATOM   962  C CB  . ASP   B 2 77  ? -26.182 -11.123 -12.272 1.00 52.65  ? 86  ASP   B CB  1 
ATOM   963  C CG  . ASP   B 2 77  ? -27.540 -11.366 -12.905 1.00 62.24  ? 86  ASP   B CG  1 
ATOM   964  O OD1 . ASP   B 2 77  ? -27.763 -10.894 -14.042 1.00 65.10  ? 86  ASP   B OD1 1 
ATOM   965  O OD2 . ASP   B 2 77  ? -28.379 -12.032 -12.267 1.00 65.93  ? 86  ASP   B OD2 1 
ATOM   966  N N   . ALA   B 2 78  ? -24.734 -10.644 -15.512 1.00 46.50  ? 87  ALA   B N   1 
ATOM   967  C CA  . ALA   B 2 78  ? -24.210 -11.380 -16.657 1.00 46.55  ? 87  ALA   B CA  1 
ATOM   968  C C   . ALA   B 2 78  ? -22.682 -11.472 -16.555 1.00 46.92  ? 87  ALA   B C   1 
ATOM   969  O O   . ALA   B 2 78  ? -22.028 -10.571 -16.000 1.00 46.56  ? 87  ALA   B O   1 
ATOM   970  C CB  . ALA   B 2 78  ? -24.639 -10.732 -17.972 1.00 45.65  ? 87  ALA   B CB  1 
ATOM   971  N N   . ALA   B 2 79  ? -22.128 -12.591 -17.044 1.00 46.82  ? 88  ALA   B N   1 
ATOM   972  C CA  . ALA   B 2 79  ? -20.696 -12.853 -16.987 1.00 47.70  ? 88  ALA   B CA  1 
ATOM   973  C C   . ALA   B 2 79  ? -20.112 -13.154 -18.356 1.00 47.47  ? 88  ALA   B C   1 
ATOM   974  O O   . ALA   B 2 79  ? -20.778 -13.769 -19.190 1.00 47.28  ? 88  ALA   B O   1 
ATOM   975  C CB  . ALA   B 2 79  ? -20.423 -14.038 -16.063 1.00 48.17  ? 88  ALA   B CB  1 
ATOM   976  N N   . TRP   B 2 80  ? -18.837 -12.764 -18.581 1.00 48.21  ? 89  TRP   B N   1 
ATOM   977  C CA  . TRP   B 2 80  ? -18.099 -13.096 -19.799 1.00 50.61  ? 89  TRP   B CA  1 
ATOM   978  C C   . TRP   B 2 80  ? -17.966 -14.618 -19.837 1.00 51.84  ? 89  TRP   B C   1 
ATOM   979  O O   . TRP   B 2 80  ? -17.702 -15.215 -18.791 1.00 50.58  ? 89  TRP   B O   1 
ATOM   980  C CB  . TRP   B 2 80  ? -16.688 -12.472 -19.795 1.00 51.24  ? 89  TRP   B CB  1 
ATOM   981  C CG  . TRP   B 2 80  ? -15.901 -12.778 -21.043 1.00 52.58  ? 89  TRP   B CG  1 
ATOM   982  C CD1 . TRP   B 2 80  ? -16.354 -12.742 -22.330 1.00 53.69  ? 89  TRP   B CD1 1 
ATOM   983  C CD2 . TRP   B 2 80  ? -14.534 -13.218 -21.110 1.00 52.70  ? 89  TRP   B CD2 1 
ATOM   984  N NE1 . TRP   B 2 80  ? -15.356 -13.131 -23.197 1.00 54.09  ? 89  TRP   B NE1 1 
ATOM   985  C CE2 . TRP   B 2 80  ? -14.227 -13.425 -22.474 1.00 53.47  ? 89  TRP   B CE2 1 
ATOM   986  C CE3 . TRP   B 2 80  ? -13.541 -13.455 -20.154 1.00 53.34  ? 89  TRP   B CE3 1 
ATOM   987  C CZ2 . TRP   B 2 80  ? -12.958 -13.802 -22.902 1.00 53.90  ? 89  TRP   B CZ2 1 
ATOM   988  C CZ3 . TRP   B 2 80  ? -12.292 -13.873 -20.580 1.00 53.80  ? 89  TRP   B CZ3 1 
ATOM   989  C CH2 . TRP   B 2 80  ? -12.011 -14.042 -21.940 1.00 53.85  ? 89  TRP   B CH2 1 
ATOM   990  N N   . ASP   B 2 81  ? -18.271 -15.249 -20.990 1.00 53.81  ? 90  ASP   B N   1 
ATOM   991  C CA  . ASP   B 2 81  ? -18.200 -16.715 -21.066 1.00 56.25  ? 90  ASP   B CA  1 
ATOM   992  C C   . ASP   B 2 81  ? -16.762 -17.276 -21.127 1.00 59.28  ? 90  ASP   B C   1 
ATOM   993  O O   . ASP   B 2 81  ? -16.588 -18.495 -21.044 1.00 60.52  ? 90  ASP   B O   1 
ATOM   994  C CB  . ASP   B 2 81  ? -19.059 -17.273 -22.226 1.00 57.34  ? 90  ASP   B CB  1 
ATOM   995  C CG  . ASP   B 2 81  ? -18.625 -16.860 -23.608 1.00 62.60  ? 90  ASP   B CG  1 
ATOM   996  O OD1 . ASP   B 2 81  ? -17.557 -16.224 -23.732 1.00 62.79  ? 90  ASP   B OD1 1 
ATOM   997  O OD2 . ASP   B 2 81  ? -19.364 -17.164 -24.583 1.00 66.80  ? 90  ASP   B OD2 1 
ATOM   998  N N   . GLY   B 2 82  ? -15.765 -16.407 -21.295 1.00 60.20  ? 91  GLY   B N   1 
ATOM   999  C CA  . GLY   B 2 82  ? -14.364 -16.816 -21.370 1.00 61.82  ? 91  GLY   B CA  1 
ATOM   1000 C C   . GLY   B 2 82  ? -13.901 -17.226 -22.760 1.00 63.57  ? 91  GLY   B C   1 
ATOM   1001 O O   . GLY   B 2 82  ? -12.753 -17.643 -22.934 1.00 64.37  ? 91  GLY   B O   1 
ATOM   1002 N N   . LEU   B 2 83  ? -14.784 -17.131 -23.760 1.00 63.93  ? 92  LEU   B N   1 
ATOM   1003 C CA  . LEU   B 2 83  ? -14.473 -17.548 -25.121 1.00 65.43  ? 92  LEU   B CA  1 
ATOM   1004 C C   . LEU   B 2 83  ? -14.723 -16.474 -26.163 1.00 65.33  ? 92  LEU   B C   1 
ATOM   1005 O O   . LEU   B 2 83  ? -13.919 -16.302 -27.080 1.00 66.09  ? 92  LEU   B O   1 
ATOM   1006 C CB  . LEU   B 2 83  ? -15.369 -18.743 -25.500 1.00 66.78  ? 92  LEU   B CB  1 
ATOM   1007 C CG  . LEU   B 2 83  ? -15.041 -20.124 -24.982 1.00 69.55  ? 92  LEU   B CG  1 
ATOM   1008 C CD1 . LEU   B 2 83  ? -15.973 -21.135 -25.630 1.00 70.09  ? 92  LEU   B CD1 1 
ATOM   1009 C CD2 . LEU   B 2 83  ? -13.616 -20.510 -25.330 1.00 70.58  ? 92  LEU   B CD2 1 
ATOM   1010 N N   . SER   B 2 84  ? -15.897 -15.832 -26.101 1.00 64.30  ? 93  SER   B N   1 
ATOM   1011 C CA  . SER   B 2 84  ? -16.396 -14.933 -27.127 1.00 63.41  ? 93  SER   B CA  1 
ATOM   1012 C C   . SER   B 2 84  ? -15.925 -13.496 -27.056 1.00 61.61  ? 93  SER   B C   1 
ATOM   1013 O O   . SER   B 2 84  ? -15.549 -13.002 -25.984 1.00 61.39  ? 93  SER   B O   1 
ATOM   1014 C CB  . SER   B 2 84  ? -17.928 -14.945 -27.137 1.00 64.93  ? 93  SER   B CB  1 
ATOM   1015 O OG  . SER   B 2 84  ? -18.475 -16.211 -26.808 1.00 67.38  ? 93  SER   B OG  1 
ATOM   1016 N N   . GLU   B 2 85  ? -15.994 -12.815 -28.212 1.00 59.72  ? 94  GLU   B N   1 
ATOM   1017 C CA  . GLU   B 2 85  ? -15.716 -11.393 -28.320 1.00 58.23  ? 94  GLU   B CA  1 
ATOM   1018 C C   . GLU   B 2 85  ? -16.854 -10.637 -27.606 1.00 56.09  ? 94  GLU   B C   1 
ATOM   1019 O O   . GLU   B 2 85  ? -17.956 -11.157 -27.385 1.00 55.84  ? 94  GLU   B O   1 
ATOM   1020 C CB  . GLU   B 2 85  ? -15.550 -10.938 -29.799 1.00 60.54  ? 94  GLU   B CB  1 
ATOM   1021 C CG  . GLU   B 2 85  ? -14.208 -11.353 -30.400 1.00 64.74  ? 94  GLU   B CG  1 
ATOM   1022 C CD  . GLU   B 2 85  ? -13.787 -10.656 -31.685 1.00 71.23  ? 94  GLU   B CD  1 
ATOM   1023 O OE1 . GLU   B 2 85  ? -14.655 -10.070 -32.372 1.00 71.60  ? 94  GLU   B OE1 1 
ATOM   1024 O OE2 . GLU   B 2 85  ? -12.578 -10.702 -32.008 1.00 73.71  ? 94  GLU   B OE2 1 
ATOM   1025 N N   . VAL   B 2 86  ? -16.547 -9.428  -27.182 1.00 53.72  ? 95  VAL   B N   1 
ATOM   1026 C CA  . VAL   B 2 86  ? -17.462 -8.578  -26.437 1.00 51.18  ? 95  VAL   B CA  1 
ATOM   1027 C C   . VAL   B 2 86  ? -17.400 -7.180  -27.040 1.00 50.02  ? 95  VAL   B C   1 
ATOM   1028 O O   . VAL   B 2 86  ? -16.538 -6.906  -27.881 1.00 51.74  ? 95  VAL   B O   1 
ATOM   1029 C CB  . VAL   B 2 86  ? -17.031 -8.542  -24.923 1.00 49.98  ? 95  VAL   B CB  1 
ATOM   1030 C CG1 . VAL   B 2 86  ? -16.849 -9.947  -24.350 1.00 50.19  ? 95  VAL   B CG1 1 
ATOM   1031 C CG2 . VAL   B 2 86  ? -15.761 -7.713  -24.738 1.00 49.35  ? 95  VAL   B CG2 1 
ATOM   1032 N N   . GLN   B 2 87  ? -18.311 -6.283  -26.618 1.00 47.24  ? 96  GLN   B N   1 
ATOM   1033 C CA  . GLN   B 2 87  ? -18.256 -4.920  -27.064 1.00 46.74  ? 96  GLN   B CA  1 
ATOM   1034 C C   . GLN   B 2 87  ? -18.170 -3.958  -25.906 1.00 46.48  ? 96  GLN   B C   1 
ATOM   1035 O O   . GLN   B 2 87  ? -18.930 -4.074  -24.964 1.00 46.24  ? 96  GLN   B O   1 
ATOM   1036 C CB  . GLN   B 2 87  ? -19.452 -4.572  -27.978 1.00 46.38  ? 96  GLN   B CB  1 
ATOM   1037 C CG  . GLN   B 2 87  ? -19.186 -5.053  -29.402 1.00 49.13  ? 96  GLN   B CG  1 
ATOM   1038 C CD  . GLN   B 2 87  ? -20.299 -4.766  -30.369 1.00 51.62  ? 96  GLN   B CD  1 
ATOM   1039 O OE1 . GLN   B 2 87  ? -21.208 -3.977  -30.102 1.00 48.78  ? 96  GLN   B OE1 1 
ATOM   1040 N NE2 . GLN   B 2 87  ? -20.226 -5.410  -31.539 1.00 52.97  ? 96  GLN   B NE2 1 
ATOM   1041 N N   . LEU   B 2 88  ? -17.236 -3.021  -25.977 1.00 46.03  ? 97  LEU   B N   1 
ATOM   1042 C CA  . LEU   B 2 88  ? -17.143 -1.930  -25.040 1.00 45.75  ? 97  LEU   B CA  1 
ATOM   1043 C C   . LEU   B 2 88  ? -18.039 -0.853  -25.636 1.00 45.31  ? 97  LEU   B C   1 
ATOM   1044 O O   . LEU   B 2 88  ? -17.782 -0.413  -26.768 1.00 46.06  ? 97  LEU   B O   1 
ATOM   1045 C CB  . LEU   B 2 88  ? -15.700 -1.391  -24.929 1.00 46.03  ? 97  LEU   B CB  1 
ATOM   1046 C CG  . LEU   B 2 88  ? -15.573 -0.052  -24.196 1.00 47.92  ? 97  LEU   B CG  1 
ATOM   1047 C CD1 . LEU   B 2 88  ? -16.035 -0.187  -22.706 1.00 48.32  ? 97  LEU   B CD1 1 
ATOM   1048 C CD2 . LEU   B 2 88  ? -14.182 0.516   -24.323 1.00 48.64  ? 97  LEU   B CD2 1 
ATOM   1049 N N   . LEU   B 2 89  ? -19.080 -0.427  -24.910 1.00 44.51  ? 98  LEU   B N   1 
ATOM   1050 C CA  . LEU   B 2 89  ? -19.914 0.661   -25.383 1.00 45.00  ? 98  LEU   B CA  1 
ATOM   1051 C C   . LEU   B 2 89  ? -19.267 1.897   -24.783 1.00 46.03  ? 98  LEU   B C   1 
ATOM   1052 O O   . LEU   B 2 89  ? -19.649 2.366   -23.690 1.00 46.05  ? 98  LEU   B O   1 
ATOM   1053 C CB  . LEU   B 2 89  ? -21.384 0.479   -24.969 1.00 45.21  ? 98  LEU   B CB  1 
ATOM   1054 C CG  . LEU   B 2 89  ? -22.392 1.602   -25.341 1.00 46.54  ? 98  LEU   B CG  1 
ATOM   1055 C CD1 . LEU   B 2 89  ? -22.272 2.028   -26.786 1.00 48.41  ? 98  LEU   B CD1 1 
ATOM   1056 C CD2 . LEU   B 2 89  ? -23.810 1.158   -25.079 1.00 47.34  ? 98  LEU   B CD2 1 
ATOM   1057 N N   . ALA   B 2 90  ? -18.211 2.373   -25.470 1.00 45.70  ? 99  ALA   B N   1 
ATOM   1058 C CA  . ALA   B 2 90  ? -17.428 3.524   -25.034 1.00 46.01  ? 99  ALA   B CA  1 
ATOM   1059 C C   . ALA   B 2 90  ? -18.188 4.815   -25.148 1.00 45.00  ? 99  ALA   B C   1 
ATOM   1060 O O   . ALA   B 2 90  ? -18.675 5.148   -26.232 1.00 45.27  ? 99  ALA   B O   1 
ATOM   1061 C CB  . ALA   B 2 90  ? -16.143 3.631   -25.832 1.00 46.85  ? 99  ALA   B CB  1 
ATOM   1062 N N   . VAL   B 2 91  ? -18.234 5.587   -24.045 1.00 43.66  ? 100 VAL   B N   1 
ATOM   1063 C CA  . VAL   B 2 91  ? -18.865 6.906   -24.037 1.00 42.42  ? 100 VAL   B CA  1 
ATOM   1064 C C   . VAL   B 2 91  ? -17.756 7.922   -23.645 1.00 43.22  ? 100 VAL   B C   1 
ATOM   1065 O O   . VAL   B 2 91  ? -17.622 8.295   -22.476 1.00 41.98  ? 100 VAL   B O   1 
ATOM   1066 C CB  . VAL   B 2 91  ? -20.108 6.953   -23.106 1.00 41.57  ? 100 VAL   B CB  1 
ATOM   1067 C CG1 . VAL   B 2 91  ? -20.797 8.331   -23.146 1.00 41.32  ? 100 VAL   B CG1 1 
ATOM   1068 C CG2 . VAL   B 2 91  ? -21.101 5.849   -23.468 1.00 41.21  ? 100 VAL   B CG2 1 
ATOM   1069 N N   . PRO   B 2 92  ? -16.896 8.329   -24.615 1.00 44.51  ? 101 PRO   B N   1 
ATOM   1070 C CA  . PRO   B 2 92  ? -15.800 9.256   -24.280 1.00 45.10  ? 101 PRO   B CA  1 
ATOM   1071 C C   . PRO   B 2 92  ? -16.281 10.678  -24.041 1.00 45.88  ? 101 PRO   B C   1 
ATOM   1072 O O   . PRO   B 2 92  ? -17.326 11.063  -24.541 1.00 46.39  ? 101 PRO   B O   1 
ATOM   1073 C CB  . PRO   B 2 92  ? -14.873 9.188   -25.518 1.00 46.53  ? 101 PRO   B CB  1 
ATOM   1074 C CG  . PRO   B 2 92  ? -15.430 8.097   -26.410 1.00 47.14  ? 101 PRO   B CG  1 
ATOM   1075 C CD  . PRO   B 2 92  ? -16.889 7.992   -26.051 1.00 44.86  ? 101 PRO   B CD  1 
ATOM   1076 N N   . PRO   B 2 93  ? -15.525 11.481  -23.272 1.00 46.24  ? 102 PRO   B N   1 
ATOM   1077 C CA  . PRO   B 2 93  ? -15.946 12.866  -23.017 1.00 46.53  ? 102 PRO   B CA  1 
ATOM   1078 C C   . PRO   B 2 93  ? -16.113 13.689  -24.305 1.00 47.27  ? 102 PRO   B C   1 
ATOM   1079 O O   . PRO   B 2 93  ? -15.263 13.647  -25.189 1.00 47.06  ? 102 PRO   B O   1 
ATOM   1080 C CB  . PRO   B 2 93  ? -14.826 13.407  -22.118 1.00 46.69  ? 102 PRO   B CB  1 
ATOM   1081 C CG  . PRO   B 2 93  ? -14.271 12.179  -21.442 1.00 47.20  ? 102 PRO   B CG  1 
ATOM   1082 C CD  . PRO   B 2 93  ? -14.269 11.165  -22.563 1.00 45.85  ? 102 PRO   B CD  1 
ATOM   1083 N N   . GLY   B 2 94  ? -17.247 14.372  -24.426 1.00 47.50  ? 103 GLY   B N   1 
ATOM   1084 C CA  . GLY   B 2 94  ? -17.587 15.202  -25.577 1.00 47.90  ? 103 GLY   B CA  1 
ATOM   1085 C C   . GLY   B 2 94  ? -17.764 14.462  -26.893 1.00 48.04  ? 103 GLY   B C   1 
ATOM   1086 O O   . GLY   B 2 94  ? -17.846 15.078  -27.950 1.00 48.53  ? 103 GLY   B O   1 
ATOM   1087 N N   . GLU   B 2 95  ? -17.818 13.132  -26.850 1.00 48.20  ? 104 GLU   B N   1 
ATOM   1088 C CA  . GLU   B 2 95  ? -17.930 12.313  -28.052 1.00 49.12  ? 104 GLU   B CA  1 
ATOM   1089 C C   . GLU   B 2 95  ? -19.106 11.363  -27.970 1.00 49.88  ? 104 GLU   B C   1 
ATOM   1090 O O   . GLU   B 2 95  ? -19.533 10.989  -26.874 1.00 49.35  ? 104 GLU   B O   1 
ATOM   1091 C CB  . GLU   B 2 95  ? -16.619 11.542  -28.314 1.00 50.57  ? 104 GLU   B CB  1 
ATOM   1092 C CG  . GLU   B 2 95  ? -15.419 12.459  -28.513 1.00 54.02  ? 104 GLU   B CG  1 
ATOM   1093 C CD  . GLU   B 2 95  ? -14.071 11.772  -28.650 1.00 58.53  ? 104 GLU   B CD  1 
ATOM   1094 O OE1 . GLU   B 2 95  ? -14.029 10.528  -28.531 1.00 58.65  ? 104 GLU   B OE1 1 
ATOM   1095 O OE2 . GLU   B 2 95  ? -13.059 12.474  -28.889 1.00 59.04  ? 104 GLU   B OE2 1 
ATOM   1096 N N   . ARG   B 2 96  ? -19.642 10.979  -29.136 1.00 50.30  ? 105 ARG   B N   1 
ATOM   1097 C CA  . ARG   B 2 96  ? -20.794 10.089  -29.222 1.00 51.61  ? 105 ARG   B CA  1 
ATOM   1098 C C   . ARG   B 2 96  ? -20.485 8.707   -28.706 1.00 51.22  ? 105 ARG   B C   1 
ATOM   1099 O O   . ARG   B 2 96  ? -19.346 8.248   -28.839 1.00 51.48  ? 105 ARG   B O   1 
ATOM   1100 C CB  . ARG   B 2 96  ? -21.241 9.961   -30.685 1.00 54.87  ? 105 ARG   B CB  1 
ATOM   1101 C CG  . ARG   B 2 96  ? -22.650 9.390   -30.859 1.00 60.52  ? 105 ARG   B CG  1 
ATOM   1102 C CD  . ARG   B 2 96  ? -23.383 9.941   -32.074 1.00 65.20  ? 105 ARG   B CD  1 
ATOM   1103 N NE  . ARG   B 2 96  ? -22.602 9.848   -33.308 1.00 69.98  ? 105 ARG   B NE  1 
ATOM   1104 C CZ  . ARG   B 2 96  ? -22.210 10.898  -34.028 1.00 73.70  ? 105 ARG   B CZ  1 
ATOM   1105 N NH1 . ARG   B 2 96  ? -22.533 12.131  -33.650 1.00 72.99  ? 105 ARG   B NH1 1 
ATOM   1106 N NH2 . ARG   B 2 96  ? -21.496 10.722  -35.136 1.00 73.94  ? 105 ARG   B NH2 1 
ATOM   1107 N N   . ALA   B 2 97  ? -21.510 8.011   -28.138 1.00 50.41  ? 106 ALA   B N   1 
ATOM   1108 C CA  . ALA   B 2 97  ? -21.405 6.620   -27.689 1.00 49.95  ? 106 ALA   B CA  1 
ATOM   1109 C C   . ALA   B 2 97  ? -21.008 5.756   -28.912 1.00 50.53  ? 106 ALA   B C   1 
ATOM   1110 O O   . ALA   B 2 97  ? -21.604 5.918   -29.978 1.00 50.55  ? 106 ALA   B O   1 
ATOM   1111 C CB  . ALA   B 2 97  ? -22.744 6.152   -27.153 1.00 49.16  ? 106 ALA   B CB  1 
ATOM   1112 N N   . LYS   B 2 98  ? -19.993 4.898   -28.774 1.00 50.82  ? 107 LYS   B N   1 
ATOM   1113 C CA  . LYS   B 2 98  ? -19.486 4.087   -29.880 1.00 52.56  ? 107 LYS   B CA  1 
ATOM   1114 C C   . LYS   B 2 98  ? -19.192 2.660   -29.400 1.00 52.17  ? 107 LYS   B C   1 
ATOM   1115 O O   . LYS   B 2 98  ? -18.582 2.496   -28.340 1.00 52.30  ? 107 LYS   B O   1 
ATOM   1116 C CB  . LYS   B 2 98  ? -18.198 4.750   -30.392 1.00 56.01  ? 107 LYS   B CB  1 
ATOM   1117 C CG  . LYS   B 2 98  ? -17.490 4.055   -31.547 1.00 63.47  ? 107 LYS   B CG  1 
ATOM   1118 C CD  . LYS   B 2 98  ? -16.148 4.746   -31.866 1.00 69.67  ? 107 LYS   B CD  1 
ATOM   1119 C CE  . LYS   B 2 98  ? -15.297 5.005   -30.630 1.00 74.32  ? 107 LYS   B CE  1 
ATOM   1120 N NZ  . LYS   B 2 98  ? -13.843 4.859   -30.912 1.00 77.05  ? 107 LYS   B NZ  1 
ATOM   1121 N N   . ASN   B 2 99  ? -19.665 1.638   -30.130 1.00 51.34  ? 108 ASN   B N   1 
ATOM   1122 C CA  . ASN   B 2 99  ? -19.408 0.236   -29.779 1.00 52.01  ? 108 ASN   B CA  1 
ATOM   1123 C C   . ASN   B 2 99  ? -18.105 -0.225  -30.383 1.00 52.53  ? 108 ASN   B C   1 
ATOM   1124 O O   . ASN   B 2 99  ? -17.936 -0.151  -31.606 1.00 52.56  ? 108 ASN   B O   1 
ATOM   1125 C CB  . ASN   B 2 99  ? -20.506 -0.690  -30.316 1.00 53.23  ? 108 ASN   B CB  1 
ATOM   1126 C CG  . ASN   B 2 99  ? -21.860 -0.447  -29.721 1.00 56.46  ? 108 ASN   B CG  1 
ATOM   1127 O OD1 . ASN   B 2 99  ? -22.440 0.617   -29.904 1.00 57.62  ? 108 ASN   B OD1 1 
ATOM   1128 N ND2 . ASN   B 2 99  ? -22.412 -1.442  -29.034 1.00 57.09  ? 108 ASN   B ND2 1 
ATOM   1129 N N   . ILE   B 2 100 ? -17.206 -0.775  -29.561 1.00 52.02  ? 109 ILE   B N   1 
ATOM   1130 C CA  . ILE   B 2 100 ? -15.944 -1.297  -30.037 1.00 52.94  ? 109 ILE   B CA  1 
ATOM   1131 C C   . ILE   B 2 100 ? -15.855 -2.769  -29.667 1.00 53.18  ? 109 ILE   B C   1 
ATOM   1132 O O   . ILE   B 2 100 ? -15.920 -3.115  -28.488 1.00 53.08  ? 109 ILE   B O   1 
ATOM   1133 C CB  . ILE   B 2 100 ? -14.755 -0.518  -29.453 1.00 54.51  ? 109 ILE   B CB  1 
ATOM   1134 C CG1 . ILE   B 2 100 ? -14.869 0.973   -29.743 1.00 56.27  ? 109 ILE   B CG1 1 
ATOM   1135 C CG2 . ILE   B 2 100 ? -13.441 -1.091  -29.984 1.00 55.30  ? 109 ILE   B CG2 1 
ATOM   1136 C CD1 . ILE   B 2 100 ? -14.860 1.329   -31.231 1.00 57.64  ? 109 ILE   B CD1 1 
ATOM   1137 N N   . GLN   B 2 101 ? -15.700 -3.637  -30.666 1.00 53.03  ? 110 GLN   B N   1 
ATOM   1138 C CA  . GLN   B 2 101 ? -15.650 -5.065  -30.448 1.00 53.38  ? 110 GLN   B CA  1 
ATOM   1139 C C   . GLN   B 2 101 ? -14.226 -5.531  -30.231 1.00 54.39  ? 110 GLN   B C   1 
ATOM   1140 O O   . GLN   B 2 101 ? -13.322 -5.058  -30.908 1.00 55.50  ? 110 GLN   B O   1 
ATOM   1141 C CB  . GLN   B 2 101 ? -16.280 -5.789  -31.631 1.00 55.62  ? 110 GLN   B CB  1 
ATOM   1142 C CG  . GLN   B 2 101 ? -16.342 -7.306  -31.477 1.00 56.23  ? 110 GLN   B CG  1 
ATOM   1143 C CD  . GLN   B 2 101 ? -17.351 -7.883  -32.443 1.00 59.29  ? 110 GLN   B CD  1 
ATOM   1144 O OE1 . GLN   B 2 101 ? -18.379 -7.272  -32.756 1.00 58.55  ? 110 GLN   B OE1 1 
ATOM   1145 N NE2 . GLN   B 2 101 ? -17.075 -9.068  -32.942 1.00 62.26  ? 110 GLN   B NE2 1 
ATOM   1146 N N   . THR   B 2 102 ? -14.021 -6.433  -29.260 1.00 53.39  ? 111 THR   B N   1 
ATOM   1147 C CA  . THR   B 2 102 ? -12.704 -6.940  -28.916 1.00 53.62  ? 111 THR   B CA  1 
ATOM   1148 C C   . THR   B 2 102 ? -12.765 -8.325  -28.281 1.00 54.50  ? 111 THR   B C   1 
ATOM   1149 O O   . THR   B 2 102 ? -13.804 -8.719  -27.755 1.00 56.02  ? 111 THR   B O   1 
ATOM   1150 C CB  . THR   B 2 102 ? -11.964 -5.937  -28.000 1.00 54.91  ? 111 THR   B CB  1 
ATOM   1151 O OG1 . THR   B 2 102 ? -10.559 -6.248  -27.988 1.00 56.05  ? 111 THR   B OG1 1 
ATOM   1152 C CG2 . THR   B 2 102 ? -12.547 -5.876  -26.563 1.00 55.16  ? 111 THR   B CG2 1 
ATOM   1153 N N   . LEU   B 2 103 ? -11.652 -9.063  -28.307 1.00 53.51  ? 112 LEU   B N   1 
ATOM   1154 C CA  . LEU   B 2 103 ? -11.589 -10.342 -27.607 1.00 53.37  ? 112 LEU   B CA  1 
ATOM   1155 C C   . LEU   B 2 103 ? -10.852 -10.045 -26.313 1.00 53.36  ? 112 LEU   B C   1 
ATOM   1156 O O   . LEU   B 2 103 ? -9.675  -9.645  -26.343 1.00 53.18  ? 112 LEU   B O   1 
ATOM   1157 C CB  . LEU   B 2 103 ? -10.854 -11.456 -28.393 1.00 54.50  ? 112 LEU   B CB  1 
ATOM   1158 C CG  . LEU   B 2 103 ? -10.741 -12.740 -27.569 1.00 57.57  ? 112 LEU   B CG  1 
ATOM   1159 C CD1 . LEU   B 2 103 ? -12.064 -13.437 -27.437 1.00 58.22  ? 112 LEU   B CD1 1 
ATOM   1160 C CD2 . LEU   B 2 103 ? -9.696  -13.652 -28.097 1.00 59.71  ? 112 LEU   B CD2 1 
ATOM   1161 N N   . PRO   B 2 104 ? -11.497 -10.286 -25.154 1.00 52.92  ? 113 PRO   B N   1 
ATOM   1162 C CA  . PRO   B 2 104 ? -10.820 -9.978  -23.899 1.00 52.97  ? 113 PRO   B CA  1 
ATOM   1163 C C   . PRO   B 2 104 ? -9.647  -10.886 -23.646 1.00 54.22  ? 113 PRO   B C   1 
ATOM   1164 O O   . PRO   B 2 104 ? -9.666  -12.058 -23.995 1.00 55.13  ? 113 PRO   B O   1 
ATOM   1165 C CB  . PRO   B 2 104 ? -11.893 -10.232 -22.819 1.00 53.39  ? 113 PRO   B CB  1 
ATOM   1166 C CG  . PRO   B 2 104 ? -13.207 -10.174 -23.545 1.00 53.56  ? 113 PRO   B CG  1 
ATOM   1167 C CD  . PRO   B 2 104 ? -12.882 -10.740 -24.931 1.00 52.41  ? 113 PRO   B CD  1 
ATOM   1168 N N   . GLY   B 2 105 ? -8.654  -10.322 -22.994 1.00 54.17  ? 114 GLY   B N   1 
ATOM   1169 C CA  . GLY   B 2 105 ? -7.547  -11.049 -22.414 1.00 53.85  ? 114 GLY   B CA  1 
ATOM   1170 C C   . GLY   B 2 105 ? -7.958  -11.470 -21.005 1.00 53.86  ? 114 GLY   B C   1 
ATOM   1171 O O   . GLY   B 2 105 ? -9.156  -11.488 -20.670 1.00 53.28  ? 114 GLY   B O   1 
ATOM   1172 N N   . ILE   B 2 106 ? -6.982  -11.785 -20.150 1.00 54.05  ? 115 ILE   B N   1 
ATOM   1173 C CA  . ILE   B 2 106 ? -7.250  -12.266 -18.791 1.00 55.10  ? 115 ILE   B CA  1 
ATOM   1174 C C   . ILE   B 2 106 ? -6.272  -11.696 -17.764 1.00 55.16  ? 115 ILE   B C   1 
ATOM   1175 O O   . ILE   B 2 106 ? -5.067  -11.697 -17.982 1.00 56.93  ? 115 ILE   B O   1 
ATOM   1176 C CB  . ILE   B 2 106 ? -7.160  -13.835 -18.778 1.00 57.16  ? 115 ILE   B CB  1 
ATOM   1177 C CG1 . ILE   B 2 106 ? -8.284  -14.498 -19.606 1.00 59.62  ? 115 ILE   B CG1 1 
ATOM   1178 C CG2 . ILE   B 2 106 ? -7.090  -14.424 -17.369 1.00 58.06  ? 115 ILE   B CG2 1 
ATOM   1179 C CD1 . ILE   B 2 106 ? -8.089  -15.976 -19.810 1.00 62.23  ? 115 ILE   B CD1 1 
ATOM   1180 N N   . PHE   B 2 107 ? -6.792  -11.289 -16.616 1.00 53.00  ? 116 PHE   B N   1 
ATOM   1181 C CA  . PHE   B 2 107 ? -6.025  -10.889 -15.446 1.00 52.30  ? 116 PHE   B CA  1 
ATOM   1182 C C   . PHE   B 2 107 ? -5.993  -12.139 -14.587 1.00 53.23  ? 116 PHE   B C   1 
ATOM   1183 O O   . PHE   B 2 107 ? -7.055  -12.604 -14.173 1.00 53.67  ? 116 PHE   B O   1 
ATOM   1184 C CB  . PHE   B 2 107 ? -6.784  -9.814  -14.654 1.00 51.40  ? 116 PHE   B CB  1 
ATOM   1185 C CG  . PHE   B 2 107 ? -6.562  -8.374  -15.039 1.00 51.30  ? 116 PHE   B CG  1 
ATOM   1186 C CD1 . PHE   B 2 107 ? -5.819  -8.044  -16.162 1.00 51.43  ? 116 PHE   B CD1 1 
ATOM   1187 C CD2 . PHE   B 2 107 ? -7.111  -7.347  -14.287 1.00 51.49  ? 116 PHE   B CD2 1 
ATOM   1188 C CE1 . PHE   B 2 107 ? -5.633  -6.716  -16.524 1.00 52.21  ? 116 PHE   B CE1 1 
ATOM   1189 C CE2 . PHE   B 2 107 ? -6.915  -6.020  -14.645 1.00 51.80  ? 116 PHE   B CE2 1 
ATOM   1190 C CZ  . PHE   B 2 107 ? -6.182  -5.710  -15.759 1.00 51.81  ? 116 PHE   B CZ  1 
ATOM   1191 N N   . LYS   B 2 108 ? -4.803  -12.675 -14.287 1.00 53.34  ? 117 LYS   B N   1 
ATOM   1192 C CA  . LYS   B 2 108 ? -4.680  -13.840 -13.423 1.00 53.74  ? 117 LYS   B CA  1 
ATOM   1193 C C   . LYS   B 2 108 ? -4.332  -13.331 -12.026 1.00 53.06  ? 117 LYS   B C   1 
ATOM   1194 O O   . LYS   B 2 108 ? -3.337  -12.634 -11.874 1.00 52.93  ? 117 LYS   B O   1 
ATOM   1195 C CB  . LYS   B 2 108 ? -3.576  -14.797 -13.930 1.00 57.33  ? 117 LYS   B CB  1 
ATOM   1196 C CG  . LYS   B 2 108 ? -3.784  -15.246 -15.385 1.00 64.24  ? 117 LYS   B CG  1 
ATOM   1197 C CD  . LYS   B 2 108 ? -2.699  -16.227 -15.883 1.00 71.63  ? 117 LYS   B CD  1 
ATOM   1198 C CE  . LYS   B 2 108 ? -2.896  -16.569 -17.348 1.00 78.37  ? 117 LYS   B CE  1 
ATOM   1199 N NZ  . LYS   B 2 108 ? -1.803  -17.419 -17.929 1.00 82.04  ? 117 LYS   B NZ  1 
ATOM   1200 N N   . THR   B 2 109 ? -5.160  -13.627 -11.024 1.00 52.49  ? 118 THR   B N   1 
ATOM   1201 C CA  . THR   B 2 109 ? -4.906  -13.168 -9.651  1.00 53.13  ? 118 THR   B CA  1 
ATOM   1202 C C   . THR   B 2 109 ? -4.862  -14.387 -8.674  1.00 54.16  ? 118 THR   B C   1 
ATOM   1203 O O   . THR   B 2 109 ? -5.204  -15.503 -9.074  1.00 54.18  ? 118 THR   B O   1 
ATOM   1204 C CB  . THR   B 2 109 ? -6.002  -12.115 -9.203  1.00 53.75  ? 118 THR   B CB  1 
ATOM   1205 O OG1 . THR   B 2 109 ? -7.143  -12.787 -8.656  1.00 54.31  ? 118 THR   B OG1 1 
ATOM   1206 C CG2 . THR   B 2 109 ? -6.401  -11.130 -10.286 1.00 53.24  ? 118 THR   B CG2 1 
ATOM   1207 N N   A LYS   B 2 110 ? -4.449  -14.165 -7.418  0.25 54.36  ? 119 LYS   B N   1 
ATOM   1208 N N   B LYS   B 2 110 ? -4.449  -14.165 -7.418  0.25 54.36  ? 119 LYS   B N   1 
ATOM   1209 N N   C LYS   B 2 110 ? -4.450  -14.161 -7.417  0.25 54.37  ? 119 LYS   B N   1 
ATOM   1210 N N   D LYS   B 2 110 ? -4.450  -14.161 -7.417  0.25 54.37  ? 119 LYS   B N   1 
ATOM   1211 C CA  A LYS   B 2 110 ? -4.412  -15.240 -6.428  0.25 54.97  ? 119 LYS   B CA  1 
ATOM   1212 C CA  B LYS   B 2 110 ? -4.412  -15.240 -6.428  0.25 54.97  ? 119 LYS   B CA  1 
ATOM   1213 C CA  C LYS   B 2 110 ? -4.410  -15.217 -6.404  0.25 54.98  ? 119 LYS   B CA  1 
ATOM   1214 C CA  D LYS   B 2 110 ? -4.410  -15.217 -6.404  0.25 54.98  ? 119 LYS   B CA  1 
ATOM   1215 C C   A LYS   B 2 110 ? -5.821  -15.755 -6.057  0.25 55.67  ? 119 LYS   B C   1 
ATOM   1216 C C   B LYS   B 2 110 ? -5.821  -15.755 -6.057  0.25 55.67  ? 119 LYS   B C   1 
ATOM   1217 C C   C LYS   B 2 110 ? -5.817  -15.745 -6.049  0.25 55.68  ? 119 LYS   B C   1 
ATOM   1218 C C   D LYS   B 2 110 ? -5.817  -15.745 -6.049  0.25 55.68  ? 119 LYS   B C   1 
ATOM   1219 O O   A LYS   B 2 110 ? -5.943  -16.845 -5.504  0.25 56.12  ? 119 LYS   B O   1 
ATOM   1220 O O   B LYS   B 2 110 ? -5.943  -16.845 -5.504  0.25 56.12  ? 119 LYS   B O   1 
ATOM   1221 O O   C LYS   B 2 110 ? -5.934  -16.833 -5.489  0.25 56.12  ? 119 LYS   B O   1 
ATOM   1222 O O   D LYS   B 2 110 ? -5.934  -16.833 -5.489  0.25 56.12  ? 119 LYS   B O   1 
ATOM   1223 C CB  A LYS   B 2 110 ? -3.642  -14.799 -5.172  0.25 56.35  ? 119 LYS   B CB  1 
ATOM   1224 C CB  B LYS   B 2 110 ? -3.642  -14.799 -5.172  0.25 56.35  ? 119 LYS   B CB  1 
ATOM   1225 C CB  C LYS   B 2 110 ? -3.697  -14.714 -5.138  0.25 56.37  ? 119 LYS   B CB  1 
ATOM   1226 C CB  D LYS   B 2 110 ? -3.697  -14.714 -5.138  0.25 56.37  ? 119 LYS   B CB  1 
ATOM   1227 C CG  A LYS   B 2 110 ? -4.375  -13.766 -4.332  0.25 59.87  ? 119 LYS   B CG  1 
ATOM   1228 C CG  B LYS   B 2 110 ? -4.375  -13.766 -4.332  0.25 59.87  ? 119 LYS   B CG  1 
ATOM   1229 C CG  C LYS   B 2 110 ? -4.404  -13.539 -4.480  0.25 59.93  ? 119 LYS   B CG  1 
ATOM   1230 C CG  D LYS   B 2 110 ? -4.404  -13.539 -4.480  0.25 59.93  ? 119 LYS   B CG  1 
ATOM   1231 C CD  A LYS   B 2 110 ? -3.633  -13.471 -3.037  0.25 63.90  ? 119 LYS   B CD  1 
ATOM   1232 C CD  B LYS   B 2 110 ? -3.633  -13.471 -3.037  0.25 63.90  ? 119 LYS   B CD  1 
ATOM   1233 C CD  C LYS   B 2 110 ? -3.774  -13.144 -3.154  0.25 64.04  ? 119 LYS   B CD  1 
ATOM   1234 C CD  D LYS   B 2 110 ? -3.774  -13.144 -3.154  0.25 64.04  ? 119 LYS   B CD  1 
ATOM   1235 C CE  A LYS   B 2 110 ? -4.525  -12.820 -2.009  0.25 67.42  ? 119 LYS   B CE  1 
ATOM   1236 C CE  B LYS   B 2 110 ? -4.525  -12.820 -2.009  0.25 67.42  ? 119 LYS   B CE  1 
ATOM   1237 C CE  C LYS   B 2 110 ? -4.577  -12.064 -2.472  0.25 67.58  ? 119 LYS   B CE  1 
ATOM   1238 C CE  D LYS   B 2 110 ? -4.577  -12.064 -2.472  0.25 67.58  ? 119 LYS   B CE  1 
ATOM   1239 N NZ  A LYS   B 2 110 ? -5.073  -11.527 -2.487  0.25 69.60  ? 119 LYS   B NZ  1 
ATOM   1240 N NZ  B LYS   B 2 110 ? -5.073  -11.527 -2.487  0.25 69.60  ? 119 LYS   B NZ  1 
ATOM   1241 N NZ  C LYS   B 2 110 ? -3.963  -11.643 -1.187  0.25 70.03  ? 119 LYS   B NZ  1 
ATOM   1242 N NZ  D LYS   B 2 110 ? -3.963  -11.643 -1.187  0.25 70.03  ? 119 LYS   B NZ  1 
ATOM   1243 N N   . ASP   B 2 111 ? -6.875  -14.983 -6.367  1.00 55.63  ? 120 ASP   B N   1 
ATOM   1244 C CA  . ASP   B 2 111 ? -8.245  -15.377 -6.081  1.00 56.54  ? 120 ASP   B CA  1 
ATOM   1245 C C   . ASP   B 2 111 ? -9.043  -15.731 -7.348  1.00 57.16  ? 120 ASP   B C   1 
ATOM   1246 O O   . ASP   B 2 111 ? -10.268 -15.738 -7.291  1.00 57.92  ? 120 ASP   B O   1 
ATOM   1247 C CB  . ASP   B 2 111 ? -8.960  -14.240 -5.348  1.00 58.16  ? 120 ASP   B CB  1 
ATOM   1248 C CG  . ASP   B 2 111 ? -8.316  -13.884 -4.026  1.00 62.68  ? 120 ASP   B CG  1 
ATOM   1249 O OD1 . ASP   B 2 111 ? -7.918  -14.816 -3.291  1.00 63.22  ? 120 ASP   B OD1 1 
ATOM   1250 O OD2 . ASP   B 2 111 ? -8.216  -12.676 -3.723  1.00 64.80  ? 120 ASP   B OD2 1 
ATOM   1251 N N   . GLY   B 2 112 ? -8.374  -15.985 -8.471  1.00 56.64  ? 121 GLY   B N   1 
ATOM   1252 C CA  . GLY   B 2 112 ? -9.062  -16.335 -9.704  1.00 56.80  ? 121 GLY   B CA  1 
ATOM   1253 C C   . GLY   B 2 112 ? -8.828  -15.420 -10.891 1.00 56.61  ? 121 GLY   B C   1 
ATOM   1254 O O   . GLY   B 2 112 ? -8.308  -14.312 -10.751 1.00 57.01  ? 121 GLY   B O   1 
ATOM   1255 N N   . ASP   B 2 113 ? -9.230  -15.888 -12.074 1.00 55.60  ? 122 ASP   B N   1 
ATOM   1256 C CA  . ASP   B 2 113 ? -9.079  -15.155 -13.325 1.00 55.30  ? 122 ASP   B CA  1 
ATOM   1257 C C   . ASP   B 2 113 ? -10.264 -14.219 -13.585 1.00 54.58  ? 122 ASP   B C   1 
ATOM   1258 O O   . ASP   B 2 113 ? -11.401 -14.517 -13.219 1.00 54.42  ? 122 ASP   B O   1 
ATOM   1259 C CB  . ASP   B 2 113 ? -8.916  -16.124 -14.500 1.00 57.47  ? 122 ASP   B CB  1 
ATOM   1260 C CG  . ASP   B 2 113 ? -7.631  -16.936 -14.500 1.00 63.65  ? 122 ASP   B CG  1 
ATOM   1261 O OD1 . ASP   B 2 113 ? -6.818  -16.761 -13.571 1.00 64.68  ? 122 ASP   B OD1 1 
ATOM   1262 O OD2 . ASP   B 2 113 ? -7.437  -17.742 -15.443 1.00 67.41  ? 122 ASP   B OD2 1 
ATOM   1263 N N   . ILE   B 2 114 ? -9.980  -13.084 -14.230 1.00 53.44  ? 123 ILE   B N   1 
ATOM   1264 C CA  . ILE   B 2 114 ? -10.958 -12.070 -14.590 1.00 52.92  ? 123 ILE   B CA  1 
ATOM   1265 C C   . ILE   B 2 114 ? -10.686 -11.666 -16.048 1.00 50.83  ? 123 ILE   B C   1 
ATOM   1266 O O   . ILE   B 2 114 ? -9.524  -11.565 -16.431 1.00 50.30  ? 123 ILE   B O   1 
ATOM   1267 C CB  . ILE   B 2 114 ? -10.810 -10.815 -13.666 1.00 54.09  ? 123 ILE   B CB  1 
ATOM   1268 C CG1 . ILE   B 2 114 ? -10.708 -11.174 -12.175 1.00 56.14  ? 123 ILE   B CG1 1 
ATOM   1269 C CG2 . ILE   B 2 114 ? -11.916 -9.813  -13.919 1.00 54.74  ? 123 ILE   B CG2 1 
ATOM   1270 C CD1 . ILE   B 2 114 ? -10.415 -9.954  -11.236 1.00 57.91  ? 123 ILE   B CD1 1 
ATOM   1271 N N   . GLY   B 2 115 ? -11.734 -11.413 -16.841 1.00 49.08  ? 124 GLY   B N   1 
ATOM   1272 C CA  . GLY   B 2 115 ? -11.549 -10.935 -18.207 1.00 48.46  ? 124 GLY   B CA  1 
ATOM   1273 C C   . GLY   B 2 115 ? -10.970 -9.530  -18.185 1.00 47.43  ? 124 GLY   B C   1 
ATOM   1274 O O   . GLY   B 2 115 ? -11.105 -8.811  -17.187 1.00 46.56  ? 124 GLY   B O   1 
ATOM   1275 N N   . ALA   B 2 116 ? -10.274 -9.145  -19.245 1.00 47.34  ? 125 ALA   B N   1 
ATOM   1276 C CA  . ALA   B 2 116 ? -9.671  -7.822  -19.338 1.00 48.04  ? 125 ALA   B CA  1 
ATOM   1277 C C   . ALA   B 2 116 ? -9.757  -7.275  -20.755 1.00 49.46  ? 125 ALA   B C   1 
ATOM   1278 O O   . ALA   B 2 116 ? -9.605  -8.024  -21.704 1.00 49.75  ? 125 ALA   B O   1 
ATOM   1279 C CB  . ALA   B 2 116 ? -8.228  -7.859  -18.862 1.00 47.82  ? 125 ALA   B CB  1 
ATOM   1280 N N   . VAL   B 2 117 ? -10.017 -5.977  -20.913 1.00 49.41  ? 126 VAL   B N   1 
ATOM   1281 C CA  . VAL   B 2 117 ? -10.147 -5.347  -22.214 1.00 51.37  ? 126 VAL   B CA  1 
ATOM   1282 C C   . VAL   B 2 117 ? -8.988  -4.360  -22.492 1.00 52.51  ? 126 VAL   B C   1 
ATOM   1283 O O   . VAL   B 2 117 ? -8.745  -3.431  -21.711 1.00 52.03  ? 126 VAL   B O   1 
ATOM   1284 C CB  . VAL   B 2 117 ? -11.565 -4.732  -22.288 1.00 52.06  ? 126 VAL   B CB  1 
ATOM   1285 C CG1 . VAL   B 2 117 ? -11.660 -3.567  -23.250 1.00 53.72  ? 126 VAL   B CG1 1 
ATOM   1286 C CG2 . VAL   B 2 117 ? -12.587 -5.815  -22.609 1.00 52.09  ? 126 VAL   B CG2 1 
ATOM   1287 N N   . ALA   B 2 118 ? -8.245  -4.594  -23.598 1.00 52.92  ? 127 ALA   B N   1 
ATOM   1288 C CA  . ALA   B 2 118 ? -7.104  -3.752  -23.918 1.00 54.19  ? 127 ALA   B CA  1 
ATOM   1289 C C   . ALA   B 2 118 ? -7.492  -2.679  -24.917 1.00 56.11  ? 127 ALA   B C   1 
ATOM   1290 O O   . ALA   B 2 118 ? -7.192  -2.760  -26.118 1.00 56.05  ? 127 ALA   B O   1 
ATOM   1291 C CB  . ALA   B 2 118 ? -5.931  -4.598  -24.423 1.00 54.43  ? 127 ALA   B CB  1 
ATOM   1292 N N   . LEU   B 2 119 ? -8.270  -1.705  -24.436 1.00 56.59  ? 128 LEU   B N   1 
ATOM   1293 C CA  . LEU   B 2 119 ? -8.703  -0.599  -25.265 1.00 57.25  ? 128 LEU   B CA  1 
ATOM   1294 C C   . LEU   B 2 119 ? -8.369  0.676   -24.493 1.00 59.03  ? 128 LEU   B C   1 
ATOM   1295 O O   . LEU   B 2 119 ? -8.611  0.744   -23.275 1.00 59.68  ? 128 LEU   B O   1 
ATOM   1296 C CB  . LEU   B 2 119 ? -10.209 -0.696  -25.572 1.00 57.15  ? 128 LEU   B CB  1 
ATOM   1297 C CG  . LEU   B 2 119 ? -10.681 -1.928  -26.362 1.00 57.79  ? 128 LEU   B CG  1 
ATOM   1298 C CD1 . LEU   B 2 119 ? -12.198 -2.029  -26.357 1.00 57.69  ? 128 LEU   B CD1 1 
ATOM   1299 C CD2 . LEU   B 2 119 ? -10.146 -1.924  -27.807 1.00 58.59  ? 128 LEU   B CD2 1 
ATOM   1300 N N   . ASP   B 2 120 ? -7.786  1.675   -25.178 1.00 59.59  ? 129 ASP   B N   1 
ATOM   1301 C CA  . ASP   B 2 120 ? -7.381  2.902   -24.498 1.00 60.05  ? 129 ASP   B CA  1 
ATOM   1302 C C   . ASP   B 2 120 ? -8.320  4.069   -24.727 1.00 58.19  ? 129 ASP   B C   1 
ATOM   1303 O O   . ASP   B 2 120 ? -8.550  4.490   -25.862 1.00 59.02  ? 129 ASP   B O   1 
ATOM   1304 C CB  . ASP   B 2 120 ? -5.932  3.288   -24.843 1.00 64.01  ? 129 ASP   B CB  1 
ATOM   1305 C CG  . ASP   B 2 120 ? -5.141  3.841   -23.660 1.00 71.41  ? 129 ASP   B CG  1 
ATOM   1306 O OD1 . ASP   B 2 120 ? -5.762  4.177   -22.628 1.00 72.59  ? 129 ASP   B OD1 1 
ATOM   1307 O OD2 . ASP   B 2 120 ? -3.905  3.942   -23.771 1.00 75.00  ? 129 ASP   B OD2 1 
ATOM   1308 N N   . TYR   B 2 121 ? -8.833  4.622   -23.634 1.00 55.80  ? 130 TYR   B N   1 
ATOM   1309 C CA  . TYR   B 2 121 ? -9.752  5.749   -23.693 1.00 54.19  ? 130 TYR   B CA  1 
ATOM   1310 C C   . TYR   B 2 121 ? -9.439  6.777   -22.607 1.00 52.51  ? 130 TYR   B C   1 
ATOM   1311 O O   . TYR   B 2 121 ? -8.848  6.414   -21.586 1.00 52.82  ? 130 TYR   B O   1 
ATOM   1312 C CB  . TYR   B 2 121 ? -11.189 5.231   -23.531 1.00 54.52  ? 130 TYR   B CB  1 
ATOM   1313 C CG  . TYR   B 2 121 ? -11.772 4.731   -24.830 1.00 55.44  ? 130 TYR   B CG  1 
ATOM   1314 C CD1 . TYR   B 2 121 ? -12.280 5.615   -25.771 1.00 56.47  ? 130 TYR   B CD1 1 
ATOM   1315 C CD2 . TYR   B 2 121 ? -11.760 3.380   -25.144 1.00 56.27  ? 130 TYR   B CD2 1 
ATOM   1316 C CE1 . TYR   B 2 121 ? -12.781 5.164   -26.982 1.00 57.76  ? 130 TYR   B CE1 1 
ATOM   1317 C CE2 . TYR   B 2 121 ? -12.258 2.917   -26.354 1.00 57.61  ? 130 TYR   B CE2 1 
ATOM   1318 C CZ  . TYR   B 2 121 ? -12.758 3.815   -27.276 1.00 59.26  ? 130 TYR   B CZ  1 
ATOM   1319 O OH  . TYR   B 2 121 ? -13.264 3.373   -28.471 1.00 62.43  ? 130 TYR   B OH  1 
ATOM   1320 N N   . PRO   B 2 122 ? -9.891  8.047   -22.739 1.00 51.29  ? 131 PRO   B N   1 
ATOM   1321 C CA  . PRO   B 2 122 ? -9.657  9.012   -21.650 1.00 50.59  ? 131 PRO   B CA  1 
ATOM   1322 C C   . PRO   B 2 122 ? -10.227 8.505   -20.304 1.00 49.41  ? 131 PRO   B C   1 
ATOM   1323 O O   . PRO   B 2 122 ? -11.136 7.671   -20.295 1.00 49.23  ? 131 PRO   B O   1 
ATOM   1324 C CB  . PRO   B 2 122 ? -10.369 10.278  -22.141 1.00 51.51  ? 131 PRO   B CB  1 
ATOM   1325 C CG  . PRO   B 2 122 ? -10.427 10.139  -23.640 1.00 52.35  ? 131 PRO   B CG  1 
ATOM   1326 C CD  . PRO   B 2 122 ? -10.616 8.666   -23.871 1.00 51.09  ? 131 PRO   B CD  1 
ATOM   1327 N N   . ALA   B 2 123 ? -9.646  8.938   -19.176 1.00 48.44  ? 132 ALA   B N   1 
ATOM   1328 C CA  . ALA   B 2 123 ? -10.092 8.497   -17.852 1.00 47.78  ? 132 ALA   B CA  1 
ATOM   1329 C C   . ALA   B 2 123 ? -11.588 8.739   -17.597 1.00 46.50  ? 132 ALA   B C   1 
ATOM   1330 O O   . ALA   B 2 123 ? -12.240 7.931   -16.926 1.00 46.41  ? 132 ALA   B O   1 
ATOM   1331 C CB  . ALA   B 2 123 ? -9.251  9.145   -16.766 1.00 48.28  ? 132 ALA   B CB  1 
ATOM   1332 N N   . GLY   B 2 124 ? -12.125 9.806   -18.196 1.00 45.09  ? 133 GLY   B N   1 
ATOM   1333 C CA  . GLY   B 2 124 ? -13.536 10.155  -18.101 1.00 43.49  ? 133 GLY   B CA  1 
ATOM   1334 C C   . GLY   B 2 124 ? -14.489 9.165   -18.746 1.00 41.23  ? 133 GLY   B C   1 
ATOM   1335 O O   . GLY   B 2 124 ? -15.707 9.328   -18.623 1.00 40.67  ? 133 GLY   B O   1 
ATOM   1336 N N   . THR   B 2 125 ? -13.952 8.115   -19.411 1.00 39.06  ? 134 THR   B N   1 
ATOM   1337 C CA  . THR   B 2 125 ? -14.727 7.009   -20.006 1.00 39.23  ? 134 THR   B CA  1 
ATOM   1338 C C   . THR   B 2 125 ? -15.016 5.870   -18.971 1.00 38.85  ? 134 THR   B C   1 
ATOM   1339 O O   . THR   B 2 125 ? -15.784 4.959   -19.264 1.00 39.26  ? 134 THR   B O   1 
ATOM   1340 C CB  . THR   B 2 125 ? -13.982 6.439   -21.256 1.00 41.16  ? 134 THR   B CB  1 
ATOM   1341 O OG1 . THR   B 2 125 ? -13.556 7.509   -22.097 1.00 42.14  ? 134 THR   B OG1 1 
ATOM   1342 C CG2 . THR   B 2 125 ? -14.833 5.497   -22.097 1.00 40.97  ? 134 THR   B CG2 1 
ATOM   1343 N N   . SER   B 2 126 ? -14.379 5.907   -17.779 1.00 37.49  ? 135 SER   B N   1 
ATOM   1344 C CA  . SER   B 2 126 ? -14.589 4.898   -16.709 1.00 37.07  ? 135 SER   B CA  1 
ATOM   1345 C C   . SER   B 2 126 ? -16.076 4.744   -16.381 1.00 36.25  ? 135 SER   B C   1 
ATOM   1346 O O   . SER   B 2 126 ? -16.735 5.739   -16.199 1.00 35.85  ? 135 SER   B O   1 
ATOM   1347 C CB  . SER   B 2 126 ? -13.894 5.340   -15.428 1.00 38.66  ? 135 SER   B CB  1 
ATOM   1348 O OG  . SER   B 2 126 ? -12.484 5.351   -15.527 1.00 40.31  ? 135 SER   B OG  1 
ATOM   1349 N N   . GLY   B 2 127 ? -16.579 3.516   -16.342 1.00 35.85  ? 136 GLY   B N   1 
ATOM   1350 C CA  . GLY   B 2 127 ? -17.981 3.212   -16.093 1.00 35.75  ? 136 GLY   B CA  1 
ATOM   1351 C C   . GLY   B 2 127 ? -18.737 2.771   -17.336 1.00 36.09  ? 136 GLY   B C   1 
ATOM   1352 O O   . GLY   B 2 127 ? -19.888 2.325   -17.249 1.00 35.85  ? 136 GLY   B O   1 
ATOM   1353 N N   . SER   B 2 128 ? -18.112 2.898   -18.542 1.00 36.03  ? 137 SER   B N   1 
ATOM   1354 C CA  . SER   B 2 128 ? -18.730 2.449   -19.772 1.00 35.97  ? 137 SER   B CA  1 
ATOM   1355 C C   . SER   B 2 128 ? -18.946 0.931   -19.695 1.00 36.10  ? 137 SER   B C   1 
ATOM   1356 O O   . SER   B 2 128 ? -18.069 0.228   -19.255 1.00 36.54  ? 137 SER   B O   1 
ATOM   1357 C CB  . SER   B 2 128 ? -17.804 2.764   -20.953 1.00 36.12  ? 137 SER   B CB  1 
ATOM   1358 O OG  . SER   B 2 128 ? -17.783 4.166   -21.177 1.00 37.01  ? 137 SER   B OG  1 
ATOM   1359 N N   . PRO   B 2 129 ? -20.122 0.441   -20.089 1.00 37.33  ? 138 PRO   B N   1 
ATOM   1360 C CA  . PRO   B 2 129 ? -20.389 -0.993  -20.005 1.00 37.89  ? 138 PRO   B CA  1 
ATOM   1361 C C   . PRO   B 2 129 ? -19.750 -1.830  -21.096 1.00 39.55  ? 138 PRO   B C   1 
ATOM   1362 O O   . PRO   B 2 129 ? -19.611 -1.409  -22.258 1.00 39.23  ? 138 PRO   B O   1 
ATOM   1363 C CB  . PRO   B 2 129 ? -21.908 -1.078  -20.159 1.00 38.72  ? 138 PRO   B CB  1 
ATOM   1364 C CG  . PRO   B 2 129 ? -22.280 0.136   -20.986 1.00 38.99  ? 138 PRO   B CG  1 
ATOM   1365 C CD  . PRO   B 2 129 ? -21.280 1.196   -20.615 1.00 37.55  ? 138 PRO   B CD  1 
ATOM   1366 N N   . ILE   B 2 130 ? -19.455 -3.073  -20.724 1.00 40.18  ? 139 ILE   B N   1 
ATOM   1367 C CA  . ILE   B 2 130 ? -18.958 -4.103  -21.624 1.00 41.97  ? 139 ILE   B CA  1 
ATOM   1368 C C   . ILE   B 2 130 ? -20.137 -5.066  -21.795 1.00 42.76  ? 139 ILE   B C   1 
ATOM   1369 O O   . ILE   B 2 130 ? -20.759 -5.438  -20.796 1.00 42.33  ? 139 ILE   B O   1 
ATOM   1370 C CB  . ILE   B 2 130 ? -17.729 -4.770  -21.006 1.00 42.67  ? 139 ILE   B CB  1 
ATOM   1371 C CG1 . ILE   B 2 130 ? -16.633 -3.729  -20.757 1.00 44.49  ? 139 ILE   B CG1 1 
ATOM   1372 C CG2 . ILE   B 2 130 ? -17.216 -5.953  -21.869 1.00 42.73  ? 139 ILE   B CG2 1 
ATOM   1373 C CD1 . ILE   B 2 130 ? -15.575 -4.237  -19.810 1.00 46.88  ? 139 ILE   B CD1 1 
ATOM   1374 N N   . LEU   B 2 131 ? -20.477 -5.417  -23.050 1.00 43.64  ? 140 LEU   B N   1 
ATOM   1375 C CA  . LEU   B 2 131 ? -21.641 -6.238  -23.377 1.00 45.53  ? 140 LEU   B CA  1 
ATOM   1376 C C   . LEU   B 2 131 ? -21.354 -7.575  -24.024 1.00 46.36  ? 140 LEU   B C   1 
ATOM   1377 O O   . LEU   B 2 131 ? -20.417 -7.690  -24.815 1.00 46.65  ? 140 LEU   B O   1 
ATOM   1378 C CB  . LEU   B 2 131 ? -22.550 -5.476  -24.368 1.00 47.38  ? 140 LEU   B CB  1 
ATOM   1379 C CG  . LEU   B 2 131 ? -22.763 -3.985  -24.164 1.00 50.21  ? 140 LEU   B CG  1 
ATOM   1380 C CD1 . LEU   B 2 131 ? -23.685 -3.431  -25.225 1.00 51.31  ? 140 LEU   B CD1 1 
ATOM   1381 C CD2 . LEU   B 2 131 ? -23.283 -3.698  -22.767 1.00 51.42  ? 140 LEU   B CD2 1 
ATOM   1382 N N   . ASP   B 2 132 ? -22.233 -8.559  -23.788 1.00 46.47  ? 141 ASP   B N   1 
ATOM   1383 C CA  . ASP   B 2 132 ? -22.157 -9.818  -24.521 1.00 47.95  ? 141 ASP   B CA  1 
ATOM   1384 C C   . ASP   B 2 132 ? -23.019 -9.691  -25.807 1.00 50.97  ? 141 ASP   B C   1 
ATOM   1385 O O   . ASP   B 2 132 ? -23.662 -8.650  -26.021 1.00 50.88  ? 141 ASP   B O   1 
ATOM   1386 C CB  . ASP   B 2 132 ? -22.547 -11.033 -23.668 1.00 48.54  ? 141 ASP   B CB  1 
ATOM   1387 C CG  . ASP   B 2 132 ? -23.958 -11.074 -23.120 1.00 51.59  ? 141 ASP   B CG  1 
ATOM   1388 O OD1 . ASP   B 2 132 ? -24.825 -10.353 -23.646 1.00 50.90  ? 141 ASP   B OD1 1 
ATOM   1389 O OD2 . ASP   B 2 132 ? -24.189 -11.820 -22.160 1.00 54.17  ? 141 ASP   B OD2 1 
ATOM   1390 N N   . LYS   B 2 133 ? -23.079 -10.754 -26.630 1.00 53.18  ? 142 LYS   B N   1 
ATOM   1391 C CA  . LYS   B 2 133 ? -23.816 -10.735 -27.898 1.00 55.44  ? 142 LYS   B CA  1 
ATOM   1392 C C   . LYS   B 2 133 ? -25.322 -10.536 -27.750 1.00 56.38  ? 142 LYS   B C   1 
ATOM   1393 O O   . LYS   B 2 133 ? -25.976 -10.183 -28.724 1.00 56.61  ? 142 LYS   B O   1 
ATOM   1394 C CB  . LYS   B 2 133 ? -23.500 -11.987 -28.732 1.00 59.07  ? 142 LYS   B CB  1 
ATOM   1395 C CG  . LYS   B 2 133 ? -22.058 -11.987 -29.226 1.00 66.44  ? 142 LYS   B CG  1 
ATOM   1396 C CD  . LYS   B 2 133 ? -21.620 -13.341 -29.782 1.00 73.48  ? 142 LYS   B CD  1 
ATOM   1397 C CE  . LYS   B 2 133 ? -20.115 -13.481 -29.769 1.00 78.69  ? 142 LYS   B CE  1 
ATOM   1398 N NZ  . LYS   B 2 133 ? -19.671 -14.833 -30.222 1.00 81.82  ? 142 LYS   B NZ  1 
ATOM   1399 N N   . CYS   B 2 134 ? -25.873 -10.736 -26.544 1.00 56.53  ? 143 CYS   B N   1 
ATOM   1400 C CA  . CYS   B 2 134 ? -27.294 -10.462 -26.305 1.00 56.77  ? 143 CYS   B CA  1 
ATOM   1401 C C   . CYS   B 2 134 ? -27.546 -9.068  -25.752 1.00 54.54  ? 143 CYS   B C   1 
ATOM   1402 O O   . CYS   B 2 134 ? -28.678 -8.783  -25.376 1.00 55.00  ? 143 CYS   B O   1 
ATOM   1403 C CB  . CYS   B 2 134 ? -27.915 -11.509 -25.395 1.00 59.80  ? 143 CYS   B CB  1 
ATOM   1404 S SG  . CYS   B 2 134 ? -27.576 -13.201 -25.898 1.00 69.18  ? 143 CYS   B SG  1 
ATOM   1405 N N   . GLY   B 2 135 ? -26.520 -8.226  -25.682 1.00 52.18  ? 144 GLY   B N   1 
ATOM   1406 C CA  . GLY   B 2 135 ? -26.657 -6.881  -25.151 1.00 50.47  ? 144 GLY   B CA  1 
ATOM   1407 C C   . GLY   B 2 135 ? -26.657 -6.818  -23.633 1.00 48.49  ? 144 GLY   B C   1 
ATOM   1408 O O   . GLY   B 2 135 ? -26.882 -5.748  -23.076 1.00 48.46  ? 144 GLY   B O   1 
ATOM   1409 N N   . ARG   B 2 136 ? -26.396 -7.948  -22.943 1.00 47.01  ? 145 ARG   B N   1 
ATOM   1410 C CA  . ARG   B 2 136 ? -26.372 -7.945  -21.474 1.00 46.44  ? 145 ARG   B CA  1 
ATOM   1411 C C   . ARG   B 2 136 ? -25.063 -7.368  -20.970 1.00 44.29  ? 145 ARG   B C   1 
ATOM   1412 O O   . ARG   B 2 136 ? -24.001 -7.665  -21.526 1.00 43.86  ? 145 ARG   B O   1 
ATOM   1413 C CB  . ARG   B 2 136 ? -26.603 -9.346  -20.910 1.00 49.28  ? 145 ARG   B CB  1 
ATOM   1414 C CG  . ARG   B 2 136 ? -28.024 -9.865  -21.111 1.00 54.33  ? 145 ARG   B CG  1 
ATOM   1415 C CD  . ARG   B 2 136 ? -28.139 -11.299 -20.645 1.00 59.61  ? 145 ARG   B CD  1 
ATOM   1416 N NE  . ARG   B 2 136 ? -27.297 -12.187 -21.442 1.00 65.88  ? 145 ARG   B NE  1 
ATOM   1417 C CZ  . ARG   B 2 136 ? -26.816 -13.354 -21.021 1.00 70.02  ? 145 ARG   B CZ  1 
ATOM   1418 N NH1 . ARG   B 2 136 ? -27.059 -13.775 -19.783 1.00 69.86  ? 145 ARG   B NH1 1 
ATOM   1419 N NH2 . ARG   B 2 136 ? -26.055 -14.090 -21.820 1.00 71.06  ? 145 ARG   B NH2 1 
ATOM   1420 N N   . VAL   B 2 137 ? -25.131 -6.534  -19.924 1.00 42.46  ? 146 VAL   B N   1 
ATOM   1421 C CA  . VAL   B 2 137 ? -23.944 -5.914  -19.355 1.00 41.96  ? 146 VAL   B CA  1 
ATOM   1422 C C   . VAL   B 2 137 ? -23.181 -6.918  -18.498 1.00 41.95  ? 146 VAL   B C   1 
ATOM   1423 O O   . VAL   B 2 137 ? -23.660 -7.334  -17.439 1.00 41.46  ? 146 VAL   B O   1 
ATOM   1424 C CB  . VAL   B 2 137 ? -24.282 -4.620  -18.559 1.00 41.66  ? 146 VAL   B CB  1 
ATOM   1425 C CG1 . VAL   B 2 137 ? -23.022 -4.017  -17.956 1.00 42.04  ? 146 VAL   B CG1 1 
ATOM   1426 C CG2 . VAL   B 2 137 ? -25.004 -3.596  -19.448 1.00 42.12  ? 146 VAL   B CG2 1 
ATOM   1427 N N   . ILE   B 2 138 ? -21.995 -7.328  -18.967 1.00 41.87  ? 147 ILE   B N   1 
ATOM   1428 C CA  . ILE   B 2 138 ? -21.151 -8.277  -18.246 1.00 41.72  ? 147 ILE   B CA  1 
ATOM   1429 C C   . ILE   B 2 138 ? -20.102 -7.626  -17.323 1.00 40.15  ? 147 ILE   B C   1 
ATOM   1430 O O   . ILE   B 2 138 ? -19.369 -8.326  -16.620 1.00 40.16  ? 147 ILE   B O   1 
ATOM   1431 C CB  . ILE   B 2 138 ? -20.474 -9.247  -19.262 1.00 42.29  ? 147 ILE   B CB  1 
ATOM   1432 C CG1 . ILE   B 2 138 ? -19.633 -8.471  -20.278 1.00 43.31  ? 147 ILE   B CG1 1 
ATOM   1433 C CG2 . ILE   B 2 138 ? -21.485 -10.166 -19.938 1.00 42.41  ? 147 ILE   B CG2 1 
ATOM   1434 C CD1 . ILE   B 2 138 ? -18.717 -9.362  -21.147 1.00 45.80  ? 147 ILE   B CD1 1 
ATOM   1435 N N   . GLY   B 2 139 ? -20.053 -6.303  -17.301 1.00 39.13  ? 148 GLY   B N   1 
ATOM   1436 C CA  . GLY   B 2 139 ? -19.134 -5.576  -16.433 1.00 38.52  ? 148 GLY   B CA  1 
ATOM   1437 C C   . GLY   B 2 139 ? -18.927 -4.143  -16.885 1.00 38.49  ? 148 GLY   B C   1 
ATOM   1438 O O   . GLY   B 2 139 ? -19.388 -3.761  -17.966 1.00 39.51  ? 148 GLY   B O   1 
ATOM   1439 N N   . LEU   B 2 140 ? -18.156 -3.369  -16.117 1.00 37.17  ? 149 LEU   B N   1 
ATOM   1440 C CA  . LEU   B 2 140 ? -17.850 -1.982  -16.437 1.00 37.52  ? 149 LEU   B CA  1 
ATOM   1441 C C   . LEU   B 2 140 ? -16.345 -1.813  -16.678 1.00 38.93  ? 149 LEU   B C   1 
ATOM   1442 O O   . LEU   B 2 140 ? -15.517 -2.485  -16.040 1.00 39.34  ? 149 LEU   B O   1 
ATOM   1443 C CB  . LEU   B 2 140 ? -18.311 -1.029  -15.303 1.00 37.01  ? 149 LEU   B CB  1 
ATOM   1444 C CG  . LEU   B 2 140 ? -19.783 -1.110  -14.859 1.00 37.57  ? 149 LEU   B CG  1 
ATOM   1445 C CD1 . LEU   B 2 140 ? -20.108 -0.027  -13.803 1.00 38.49  ? 149 LEU   B CD1 1 
ATOM   1446 C CD2 . LEU   B 2 140 ? -20.745 -1.036  -16.053 1.00 37.71  ? 149 LEU   B CD2 1 
ATOM   1447 N N   . TYR   B 2 141 ? -16.014 -0.887  -17.587 1.00 39.40  ? 150 TYR   B N   1 
ATOM   1448 C CA  . TYR   B 2 141 ? -14.672 -0.539  -18.036 1.00 40.41  ? 150 TYR   B CA  1 
ATOM   1449 C C   . TYR   B 2 141 ? -14.126 0.589   -17.191 1.00 41.11  ? 150 TYR   B C   1 
ATOM   1450 O O   . TYR   B 2 141 ? -14.855 1.527   -16.952 1.00 42.09  ? 150 TYR   B O   1 
ATOM   1451 C CB  . TYR   B 2 141 ? -14.785 -0.042  -19.512 1.00 41.58  ? 150 TYR   B CB  1 
ATOM   1452 C CG  . TYR   B 2 141 ? -13.516 0.558   -20.074 1.00 43.48  ? 150 TYR   B CG  1 
ATOM   1453 C CD1 . TYR   B 2 141 ? -13.329 1.936   -20.108 1.00 44.41  ? 150 TYR   B CD1 1 
ATOM   1454 C CD2 . TYR   B 2 141 ? -12.510 -0.250  -20.590 1.00 44.81  ? 150 TYR   B CD2 1 
ATOM   1455 C CE1 . TYR   B 2 141 ? -12.160 2.491   -20.620 1.00 45.81  ? 150 TYR   B CE1 1 
ATOM   1456 C CE2 . TYR   B 2 141 ? -11.350 0.294   -21.137 1.00 45.61  ? 150 TYR   B CE2 1 
ATOM   1457 C CZ  . TYR   B 2 141 ? -11.166 1.664   -21.125 1.00 47.42  ? 150 TYR   B CZ  1 
ATOM   1458 O OH  . TYR   B 2 141 ? -10.021 2.204   -21.670 1.00 50.66  ? 150 TYR   B OH  1 
ATOM   1459 N N   . GLY   B 2 142 ? -12.843 0.559   -16.828 1.00 41.35  ? 151 GLY   B N   1 
ATOM   1460 C CA  . GLY   B 2 142 ? -12.254 1.680   -16.098 1.00 42.08  ? 151 GLY   B CA  1 
ATOM   1461 C C   . GLY   B 2 142 ? -11.336 1.404   -14.924 1.00 42.05  ? 151 GLY   B C   1 
ATOM   1462 O O   . GLY   B 2 142 ? -10.736 2.350   -14.402 1.00 42.43  ? 151 GLY   B O   1 
ATOM   1463 N N   . ASN   B 2 143 ? -11.196 0.131   -14.495 1.00 40.74  ? 152 ASN   B N   1 
ATOM   1464 C CA  . ASN   B 2 143 ? -10.266 -0.189  -13.409 1.00 41.20  ? 152 ASN   B CA  1 
ATOM   1465 C C   . ASN   B 2 143 ? -9.320  -1.266  -13.881 1.00 42.94  ? 152 ASN   B C   1 
ATOM   1466 O O   . ASN   B 2 143 ? -9.741  -2.387  -14.131 1.00 42.85  ? 152 ASN   B O   1 
ATOM   1467 C CB  . ASN   B 2 143 ? -10.977 -0.666  -12.146 1.00 40.24  ? 152 ASN   B CB  1 
ATOM   1468 C CG  . ASN   B 2 143 ? -10.057 -0.658  -10.928 1.00 41.69  ? 152 ASN   B CG  1 
ATOM   1469 O OD1 . ASN   B 2 143 ? -9.114  0.156   -10.829 1.00 42.46  ? 152 ASN   B OD1 1 
ATOM   1470 N ND2 . ASN   B 2 143 ? -10.308 -1.563  -9.967  1.00 39.26  ? 152 ASN   B ND2 1 
ATOM   1471 N N   . GLY   B 2 144 ? -8.062  -0.914  -14.011 1.00 44.69  ? 153 GLY   B N   1 
ATOM   1472 C CA  . GLY   B 2 144 ? -7.069  -1.848  -14.499 1.00 47.26  ? 153 GLY   B CA  1 
ATOM   1473 C C   . GLY   B 2 144 ? -5.644  -1.422  -14.273 1.00 49.75  ? 153 GLY   B C   1 
ATOM   1474 O O   . GLY   B 2 144 ? -5.307  -0.868  -13.222 1.00 49.75  ? 153 GLY   B O   1 
ATOM   1475 N N   . VAL   B 2 145 ? -4.797  -1.670  -15.278 1.00 51.42  ? 154 VAL   B N   1 
ATOM   1476 C CA  . VAL   B 2 145 ? -3.377  -1.431  -15.134 1.00 53.89  ? 154 VAL   B CA  1 
ATOM   1477 C C   . VAL   B 2 145 ? -2.727  -0.814  -16.379 1.00 57.26  ? 154 VAL   B C   1 
ATOM   1478 O O   . VAL   B 2 145 ? -3.261  -0.905  -17.480 1.00 56.55  ? 154 VAL   B O   1 
ATOM   1479 C CB  . VAL   B 2 145 ? -2.740  -2.795  -14.758 1.00 54.80  ? 154 VAL   B CB  1 
ATOM   1480 C CG1 . VAL   B 2 145 ? -2.595  -3.712  -15.965 1.00 54.17  ? 154 VAL   B CG1 1 
ATOM   1481 C CG2 . VAL   B 2 145 ? -1.430  -2.632  -14.005 1.00 56.04  ? 154 VAL   B CG2 1 
ATOM   1482 N N   . VAL   B 2 146 ? -1.576  -0.174  -16.183 1.00 60.51  ? 155 VAL   B N   1 
ATOM   1483 C CA  . VAL   B 2 146 ? -0.785  0.405   -17.261 1.00 64.08  ? 155 VAL   B CA  1 
ATOM   1484 C C   . VAL   B 2 146 ? 0.273   -0.628  -17.603 1.00 67.43  ? 155 VAL   B C   1 
ATOM   1485 O O   . VAL   B 2 146 ? 0.970   -1.106  -16.712 1.00 67.36  ? 155 VAL   B O   1 
ATOM   1486 C CB  . VAL   B 2 146 ? -0.178  1.753   -16.826 1.00 65.18  ? 155 VAL   B CB  1 
ATOM   1487 C CG1 . VAL   B 2 146 ? 0.869   2.228   -17.820 1.00 66.28  ? 155 VAL   B CG1 1 
ATOM   1488 C CG2 . VAL   B 2 146 ? -1.274  2.800   -16.650 1.00 65.47  ? 155 VAL   B CG2 1 
ATOM   1489 N N   . ILE   B 2 147 ? 0.354   -1.033  -18.878 1.00 70.32  ? 156 ILE   B N   1 
ATOM   1490 C CA  . ILE   B 2 147 ? 1.297   -2.074  -19.284 1.00 73.53  ? 156 ILE   B CA  1 
ATOM   1491 C C   . ILE   B 2 147 ? 2.693   -1.463  -19.680 1.00 76.58  ? 156 ILE   B C   1 
ATOM   1492 O O   . ILE   B 2 147 ? 2.861   -0.243  -19.602 1.00 77.19  ? 156 ILE   B O   1 
ATOM   1493 C CB  . ILE   B 2 147 ? 0.609   -2.961  -20.367 1.00 74.54  ? 156 ILE   B CB  1 
ATOM   1494 C CG1 . ILE   B 2 147 ? 0.220   -2.136  -21.609 1.00 75.61  ? 156 ILE   B CG1 1 
ATOM   1495 C CG2 . ILE   B 2 147 ? -0.601  -3.676  -19.754 1.00 75.16  ? 156 ILE   B CG2 1 
ATOM   1496 C CD1 . ILE   B 2 147 ? -0.414  -2.930  -22.730 1.00 76.84  ? 156 ILE   B CD1 1 
ATOM   1497 N N   A LYS   B 2 148 ? 3.666   -2.344  -20.000 0.15 76.70  ? 157 LYS   B N   1 
ATOM   1498 N N   B LYS   B 2 148 ? 3.665   -2.339  -20.021 0.13 76.72  ? 157 LYS   B N   1 
ATOM   1499 N N   C LYS   B 2 148 ? 3.660   -2.291  -20.108 0.37 77.30  ? 157 LYS   B N   1 
ATOM   1500 N N   D LYS   B 2 148 ? 3.651   -2.288  -20.139 0.35 77.29  ? 157 LYS   B N   1 
ATOM   1501 C CA  A LYS   B 2 148 ? 5.059   -2.064  -20.365 0.15 77.31  ? 157 LYS   B CA  1 
ATOM   1502 C CA  B LYS   B 2 148 ? 5.052   -2.033  -20.391 0.13 77.34  ? 157 LYS   B CA  1 
ATOM   1503 C CA  C LYS   B 2 148 ? 4.983   -1.805  -20.519 0.37 78.48  ? 157 LYS   B CA  1 
ATOM   1504 C CA  D LYS   B 2 148 ? 4.971   -1.807  -20.563 0.35 78.48  ? 157 LYS   B CA  1 
ATOM   1505 C C   A LYS   B 2 148 ? 5.260   -0.832  -21.236 0.15 77.68  ? 157 LYS   B C   1 
ATOM   1506 C C   B LYS   B 2 148 ? 5.192   -0.912  -21.411 0.13 77.73  ? 157 LYS   B C   1 
ATOM   1507 C C   C LYS   B 2 148 ? 4.901   -0.776  -21.659 0.37 79.28  ? 157 LYS   B C   1 
ATOM   1508 C C   D LYS   B 2 148 ? 4.881   -0.780  -21.704 0.35 79.29  ? 157 LYS   B C   1 
ATOM   1509 O O   A LYS   B 2 148 ? 5.492   0.258   -20.716 0.15 77.80  ? 157 LYS   B O   1 
ATOM   1510 O O   B LYS   B 2 148 ? 5.547   0.208   -21.050 0.13 77.88  ? 157 LYS   B O   1 
ATOM   1511 O O   C LYS   B 2 148 ? 5.743   0.116   -21.753 0.37 79.59  ? 157 LYS   B O   1 
ATOM   1512 O O   D LYS   B 2 148 ? 5.718   0.116   -21.799 0.35 79.59  ? 157 LYS   B O   1 
ATOM   1513 C CB  A LYS   B 2 148 ? 5.674   -3.291  -21.054 0.15 79.12  ? 157 LYS   B CB  1 
ATOM   1514 C CB  B LYS   B 2 148 ? 5.740   -3.296  -20.927 0.13 79.17  ? 157 LYS   B CB  1 
ATOM   1515 C CB  C LYS   B 2 148 ? 5.869   -2.979  -20.962 0.37 80.55  ? 157 LYS   B CB  1 
ATOM   1516 C CB  D LYS   B 2 148 ? 5.852   -2.985  -21.006 0.35 80.55  ? 157 LYS   B CB  1 
ATOM   1517 C CG  A LYS   B 2 148 ? 5.568   -4.565  -20.227 0.15 83.08  ? 157 LYS   B CG  1 
ATOM   1518 C CG  B LYS   B 2 148 ? 5.672   -4.477  -19.972 0.13 83.13  ? 157 LYS   B CG  1 
ATOM   1519 C CG  C LYS   B 2 148 ? 5.930   -4.126  -19.963 0.37 85.09  ? 157 LYS   B CG  1 
ATOM   1520 C CG  D LYS   B 2 148 ? 5.941   -4.106  -19.980 0.35 85.13  ? 157 LYS   B CG  1 
ATOM   1521 C CD  A LYS   B 2 148 ? 5.318   -5.784  -21.100 0.15 87.26  ? 157 LYS   B CD  1 
ATOM   1522 C CD  B LYS   B 2 148 ? 5.522   -5.797  -20.712 0.13 87.34  ? 157 LYS   B CD  1 
ATOM   1523 C CD  C LYS   B 2 148 ? 6.671   -5.315  -20.556 0.37 89.88  ? 157 LYS   B CD  1 
ATOM   1524 C CD  D LYS   B 2 148 ? 6.701   -5.297  -20.543 0.35 89.98  ? 157 LYS   B CD  1 
ATOM   1525 C CE  A LYS   B 2 148 ? 3.934   -5.764  -21.699 0.15 90.80  ? 157 LYS   B CE  1 
ATOM   1526 C CE  B LYS   B 2 148 ? 4.174   -5.912  -21.381 0.13 90.90  ? 157 LYS   B CE  1 
ATOM   1527 C CE  C LYS   B 2 148 ? 6.634   -6.530  -19.666 0.37 93.81  ? 157 LYS   B CE  1 
ATOM   1528 C CE  D LYS   B 2 148 ? 6.724   -6.469  -19.596 0.35 93.99  ? 157 LYS   B CE  1 
ATOM   1529 N NZ  A LYS   B 2 148 ? 2.884   -5.743  -20.647 0.15 92.93  ? 157 LYS   B NZ  1 
ATOM   1530 N NZ  B LYS   B 2 148 ? 3.064   -5.755  -20.405 0.13 93.01  ? 157 LYS   B NZ  1 
ATOM   1531 N NZ  C LYS   B 2 148 ? 7.249   -7.706  -20.335 0.37 96.35  ? 157 LYS   B NZ  1 
ATOM   1532 N NZ  D LYS   B 2 148 ? 7.404   -7.644  -20.202 0.35 96.61  ? 157 LYS   B NZ  1 
ATOM   1533 N N   C ASN   B 2 149 ? 3.882   -0.903  -22.515 0.51 79.36  ? 158 ASN   B N   1 
ATOM   1534 N N   D ASN   B 2 149 ? 3.859   -0.908  -22.558 0.49 79.39  ? 158 ASN   B N   1 
ATOM   1535 C CA  C ASN   B 2 149 ? 3.667   -0.038  -23.670 0.51 79.92  ? 158 ASN   B CA  1 
ATOM   1536 C CA  D ASN   B 2 149 ? 3.649   -0.022  -23.700 0.49 79.99  ? 158 ASN   B CA  1 
ATOM   1537 C C   C ASN   B 2 149 ? 3.157   1.371   -23.302 0.51 79.54  ? 158 ASN   B C   1 
ATOM   1538 C C   D ASN   B 2 149 ? 3.120   1.376   -23.320 0.49 79.57  ? 158 ASN   B C   1 
ATOM   1539 O O   C ASN   B 2 149 ? 3.283   2.295   -24.108 0.51 79.81  ? 158 ASN   B O   1 
ATOM   1540 O O   D ASN   B 2 149 ? 3.200   2.298   -24.134 0.49 79.84  ? 158 ASN   B O   1 
ATOM   1541 C CB  C ASN   B 2 149 ? 2.695   -0.700  -24.669 0.51 81.83  ? 158 ASN   B CB  1 
ATOM   1542 C CB  D ASN   B 2 149 ? 2.702   -0.676  -24.723 0.49 81.99  ? 158 ASN   B CB  1 
ATOM   1543 C CG  C ASN   B 2 149 ? 2.853   -2.199  -24.865 0.51 85.86  ? 158 ASN   B CG  1 
ATOM   1544 C CG  D ASN   B 2 149 ? 2.959   -2.146  -24.976 0.49 86.20  ? 158 ASN   B CG  1 
ATOM   1545 O OD1 C ASN   B 2 149 ? 3.851   -2.817  -24.471 0.51 87.29  ? 158 ASN   B OD1 1 
ATOM   1546 O OD1 D ASN   B 2 149 ? 4.055   -2.665  -24.732 0.49 87.81  ? 158 ASN   B OD1 1 
ATOM   1547 N ND2 C ASN   B 2 149 ? 1.861   -2.820  -25.487 0.51 86.71  ? 158 ASN   B ND2 1 
ATOM   1548 N ND2 D ASN   B 2 149 ? 1.948   -2.851  -25.464 0.49 87.04  ? 158 ASN   B ND2 1 
ATOM   1549 N N   . GLY   B 2 150 ? 2.565   1.515   -22.118 1.00 78.52  ? 159 GLY   B N   1 
ATOM   1550 C CA  . GLY   B 2 150 ? 2.009   2.780   -21.655 1.00 76.85  ? 159 GLY   B CA  1 
ATOM   1551 C C   . GLY   B 2 150 ? 0.498   2.831   -21.793 1.00 74.85  ? 159 GLY   B C   1 
ATOM   1552 O O   . GLY   B 2 150 ? -0.150  3.714   -21.223 1.00 74.76  ? 159 GLY   B O   1 
ATOM   1553 N N   . SER   B 2 151 ? -0.077  1.888   -22.575 1.00 73.07  ? 160 SER   B N   1 
ATOM   1554 C CA  . SER   B 2 151 ? -1.513  1.761   -22.793 1.00 71.47  ? 160 SER   B CA  1 
ATOM   1555 C C   . SER   B 2 151 ? -2.191  1.149   -21.550 1.00 68.37  ? 160 SER   B C   1 
ATOM   1556 O O   . SER   B 2 151 ? -1.524  0.537   -20.714 1.00 68.33  ? 160 SER   B O   1 
ATOM   1557 C CB  . SER   B 2 151 ? -1.784  0.893   -24.021 1.00 73.71  ? 160 SER   B CB  1 
ATOM   1558 O OG  . SER   B 2 151 ? -3.163  0.907   -24.362 1.00 77.39  ? 160 SER   B OG  1 
ATOM   1559 N N   . TYR   B 2 152 ? -3.513  1.327   -21.432 1.00 65.65  ? 161 TYR   B N   1 
ATOM   1560 C CA  . TYR   B 2 152 ? -4.290  0.820   -20.303 1.00 63.15  ? 161 TYR   B CA  1 
ATOM   1561 C C   . TYR   B 2 152 ? -4.978  -0.490  -20.673 1.00 59.69  ? 161 TYR   B C   1 
ATOM   1562 O O   . TYR   B 2 152 ? -5.479  -0.639  -21.786 1.00 59.88  ? 161 TYR   B O   1 
ATOM   1563 C CB  . TYR   B 2 152 ? -5.371  1.848   -19.906 1.00 63.27  ? 161 TYR   B CB  1 
ATOM   1564 C CG  . TYR   B 2 152 ? -5.846  1.771   -18.466 1.00 63.75  ? 161 TYR   B CG  1 
ATOM   1565 C CD1 . TYR   B 2 152 ? -5.006  2.112   -17.417 1.00 64.42  ? 161 TYR   B CD1 1 
ATOM   1566 C CD2 . TYR   B 2 152 ? -7.170  1.477   -18.162 1.00 64.48  ? 161 TYR   B CD2 1 
ATOM   1567 C CE1 . TYR   B 2 152 ? -5.442  2.072   -16.095 1.00 65.30  ? 161 TYR   B CE1 1 
ATOM   1568 C CE2 . TYR   B 2 152 ? -7.626  1.459   -16.844 1.00 65.09  ? 161 TYR   B CE2 1 
ATOM   1569 C CZ  . TYR   B 2 152 ? -6.759  1.762   -15.808 1.00 65.76  ? 161 TYR   B CZ  1 
ATOM   1570 O OH  . TYR   B 2 152 ? -7.195  1.777   -14.490 1.00 65.89  ? 161 TYR   B OH  1 
ATOM   1571 N N   . VAL   B 2 153 ? -5.007  -1.437  -19.732 1.00 55.75  ? 162 VAL   B N   1 
ATOM   1572 C CA  . VAL   B 2 153 ? -5.747  -2.678  -19.874 1.00 52.38  ? 162 VAL   B CA  1 
ATOM   1573 C C   . VAL   B 2 153 ? -6.712  -2.716  -18.670 1.00 48.86  ? 162 VAL   B C   1 
ATOM   1574 O O   . VAL   B 2 153 ? -6.281  -2.731  -17.520 1.00 47.25  ? 162 VAL   B O   1 
ATOM   1575 C CB  . VAL   B 2 153 ? -4.862  -3.938  -19.981 1.00 52.92  ? 162 VAL   B CB  1 
ATOM   1576 C CG1 . VAL   B 2 153 ? -5.720  -5.198  -19.936 1.00 52.81  ? 162 VAL   B CG1 1 
ATOM   1577 C CG2 . VAL   B 2 153 ? -4.029  -3.904  -21.267 1.00 54.34  ? 162 VAL   B CG2 1 
ATOM   1578 N N   . SER   B 2 154 ? -8.004  -2.642  -18.946 1.00 46.98  ? 163 SER   B N   1 
ATOM   1579 C CA  . SER   B 2 154 ? -9.018  -2.603  -17.898 1.00 45.44  ? 163 SER   B CA  1 
ATOM   1580 C C   . SER   B 2 154 ? -9.560  -3.993  -17.574 1.00 44.37  ? 163 SER   B C   1 
ATOM   1581 O O   . SER   B 2 154 ? -9.757  -4.776  -18.486 1.00 44.67  ? 163 SER   B O   1 
ATOM   1582 C CB  . SER   B 2 154 ? -10.174 -1.714  -18.353 1.00 45.15  ? 163 SER   B CB  1 
ATOM   1583 O OG  . SER   B 2 154 ? -11.290 -1.808  -17.481 1.00 46.07  ? 163 SER   B OG  1 
ATOM   1584 N N   . ALA   B 2 155 ? -9.900  -4.260  -16.306 1.00 42.68  ? 164 ALA   B N   1 
ATOM   1585 C CA  . ALA   B 2 155 ? -10.572 -5.507  -15.940 1.00 41.19  ? 164 ALA   B CA  1 
ATOM   1586 C C   . ALA   B 2 155 ? -12.031 -5.401  -16.466 1.00 40.62  ? 164 ALA   B C   1 
ATOM   1587 O O   . ALA   B 2 155 ? -12.544 -4.297  -16.675 1.00 39.99  ? 164 ALA   B O   1 
ATOM   1588 C CB  . ALA   B 2 155 ? -10.614 -5.644  -14.402 1.00 41.20  ? 164 ALA   B CB  1 
ATOM   1589 N N   . ILE   B 2 156 ? -12.711 -6.536  -16.621 1.00 40.41  ? 165 ILE   B N   1 
ATOM   1590 C CA  . ILE   B 2 156 ? -14.150 -6.535  -16.876 1.00 40.57  ? 165 ILE   B CA  1 
ATOM   1591 C C   . ILE   B 2 156 ? -14.720 -6.623  -15.428 1.00 39.13  ? 165 ILE   B C   1 
ATOM   1592 O O   . ILE   B 2 156 ? -14.834 -7.723  -14.872 1.00 38.65  ? 165 ILE   B O   1 
ATOM   1593 C CB  . ILE   B 2 156 ? -14.603 -7.753  -17.713 1.00 41.90  ? 165 ILE   B CB  1 
ATOM   1594 C CG1 . ILE   B 2 156 ? -13.932 -7.728  -19.120 1.00 43.86  ? 165 ILE   B CG1 1 
ATOM   1595 C CG2 . ILE   B 2 156 ? -16.150 -7.725  -17.840 1.00 42.75  ? 165 ILE   B CG2 1 
ATOM   1596 C CD1 . ILE   B 2 156 ? -14.331 -8.887  -20.047 1.00 46.40  ? 165 ILE   B CD1 1 
ATOM   1597 N N   . THR   B 2 157 ? -14.963 -5.468  -14.780 1.00 38.47  ? 166 THR   B N   1 
ATOM   1598 C CA  . THR   B 2 157 ? -15.415 -5.473  -13.370 1.00 37.55  ? 166 THR   B CA  1 
ATOM   1599 C C   . THR   B 2 157 ? -16.920 -5.648  -13.241 1.00 37.24  ? 166 THR   B C   1 
ATOM   1600 O O   . THR   B 2 157 ? -17.672 -4.771  -13.668 1.00 36.06  ? 166 THR   B O   1 
ATOM   1601 C CB  . THR   B 2 157 ? -14.984 -4.202  -12.644 1.00 37.80  ? 166 THR   B CB  1 
ATOM   1602 O OG1 . THR   B 2 157 ? -13.555 -4.064  -12.713 1.00 38.03  ? 166 THR   B OG1 1 
ATOM   1603 C CG2 . THR   B 2 157 ? -15.447 -4.205  -11.162 1.00 37.49  ? 166 THR   B CG2 1 
ATOM   1604 N N   . GLN   B 2 158 ? -17.363 -6.767  -12.655 1.00 36.65  ? 167 GLN   B N   1 
ATOM   1605 C CA  . GLN   B 2 158 ? -18.786 -7.058  -12.453 1.00 36.82  ? 167 GLN   B CA  1 
ATOM   1606 C C   . GLN   B 2 158 ? -19.101 -7.167  -10.933 1.00 37.81  ? 167 GLN   B C   1 
ATOM   1607 O O   . GLN   B 2 158 ? -18.273 -7.656  -10.171 1.00 36.30  ? 167 GLN   B O   1 
ATOM   1608 C CB  . GLN   B 2 158 ? -19.131 -8.401  -13.133 1.00 37.72  ? 167 GLN   B CB  1 
ATOM   1609 C CG  . GLN   B 2 158 ? -20.626 -8.781  -13.159 1.00 39.42  ? 167 GLN   B CG  1 
ATOM   1610 C CD  . GLN   B 2 158 ? -21.540 -7.681  -13.696 1.00 39.54  ? 167 GLN   B CD  1 
ATOM   1611 O OE1 . GLN   B 2 158 ? -21.663 -6.587  -13.106 1.00 37.98  ? 167 GLN   B OE1 1 
ATOM   1612 N NE2 . GLN   B 2 158 ? -22.228 -7.941  -14.791 1.00 37.77  ? 167 GLN   B NE2 1 
ATOM   1613 N N   . GLY   B 2 159 ? -20.289 -6.723  -10.525 1.00 39.70  ? 168 GLY   B N   1 
ATOM   1614 C CA  . GLY   B 2 159 ? -20.734 -6.842  -9.139  1.00 43.05  ? 168 GLY   B CA  1 
ATOM   1615 C C   . GLY   B 2 159 ? -21.480 -8.144  -8.920  1.00 47.59  ? 168 GLY   B C   1 
ATOM   1616 O O   . GLY   B 2 159 ? -21.474 -9.032  -9.783  1.00 48.87  ? 168 GLY   B O   1 
ATOM   1617 N N   . LYS   B 2 160 ? -22.134 -8.277  -7.769  1.00 50.05  ? 169 LYS   B N   1 
ATOM   1618 C CA  . LYS   B 2 160 ? -22.900 -9.481  -7.465  1.00 52.75  ? 169 LYS   B CA  1 
ATOM   1619 C C   . LYS   B 2 160 ? -24.349 -9.082  -7.256  1.00 54.98  ? 169 LYS   B C   1 
ATOM   1620 O O   . LYS   B 2 160 ? -24.614 -8.121  -6.533  1.00 55.13  ? 169 LYS   B O   1 
ATOM   1621 C CB  . LYS   B 2 160 ? -22.349 -10.155 -6.197  1.00 55.57  ? 169 LYS   B CB  1 
ATOM   1622 C CG  . LYS   B 2 160 ? -23.045 -11.460 -5.846  1.00 61.34  ? 169 LYS   B CG  1 
ATOM   1623 C CD  . LYS   B 2 160 ? -22.599 -11.986 -4.484  1.00 67.03  ? 169 LYS   B CD  1 
ATOM   1624 C CE  . LYS   B 2 160 ? -23.335 -13.249 -4.103  1.00 71.71  ? 169 LYS   B CE  1 
ATOM   1625 N NZ  . LYS   B 2 160 ? -23.175 -13.565 -2.656  1.00 75.07  ? 169 LYS   B NZ  1 
ATOM   1626 N N   . ARG   B 2 161 ? -25.285 -9.787  -7.900  1.00 56.50  ? 170 ARG   B N   1 
ATOM   1627 C CA  . ARG   B 2 161 ? -26.702 -9.491  -7.713  1.00 58.76  ? 170 ARG   B CA  1 
ATOM   1628 C C   . ARG   B 2 161 ? -27.185 -10.320 -6.511  1.00 61.35  ? 170 ARG   B C   1 
ATOM   1629 O O   . ARG   B 2 161 ? -27.369 -11.536 -6.621  1.00 61.65  ? 170 ARG   B O   1 
ATOM   1630 C CB  . ARG   B 2 161 ? -27.507 -9.803  -8.981  1.00 59.69  ? 170 ARG   B CB  1 
ATOM   1631 C CG  . ARG   B 2 161 ? -28.897 -9.210  -8.974  1.00 61.79  ? 170 ARG   B CG  1 
ATOM   1632 C CD  . ARG   B 2 161 ? -29.752 -9.759  -10.099 1.00 64.76  ? 170 ARG   B CD  1 
ATOM   1633 N NE  . ARG   B 2 161 ? -31.154 -9.381  -9.926  1.00 67.38  ? 170 ARG   B NE  1 
ATOM   1634 C CZ  . ARG   B 2 161 ? -31.809 -8.534  -10.714 1.00 69.06  ? 170 ARG   B CZ  1 
ATOM   1635 N NH1 . ARG   B 2 161 ? -31.204 -7.985  -11.758 1.00 67.61  ? 170 ARG   B NH1 1 
ATOM   1636 N NH2 . ARG   B 2 161 ? -33.077 -8.236  -10.466 1.00 69.54  ? 170 ARG   B NH2 1 
ATOM   1637 N N   . GLU   B 2 162 ? -27.286 -9.665  -5.347  1.00 62.74  ? 171 GLU   B N   1 
ATOM   1638 C CA  . GLU   B 2 162 ? -27.701 -10.258 -4.078  1.00 64.95  ? 171 GLU   B CA  1 
ATOM   1639 C C   . GLU   B 2 162 ? -29.108 -10.854 -4.140  1.00 65.98  ? 171 GLU   B C   1 
ATOM   1640 O O   . GLU   B 2 162 ? -29.391 -11.826 -3.442  1.00 66.62  ? 171 GLU   B O   1 
ATOM   1641 C CB  . GLU   B 2 162 ? -27.616 -9.203  -2.957  1.00 68.16  ? 171 GLU   B CB  1 
ATOM   1642 C CG  . GLU   B 2 162 ? -26.299 -9.222  -2.200  1.00 75.04  ? 171 GLU   B CG  1 
ATOM   1643 C CD  . GLU   B 2 162 ? -26.176 -10.375 -1.223  1.00 84.04  ? 171 GLU   B CD  1 
ATOM   1644 O OE1 . GLU   B 2 162 ? -26.986 -10.429 -0.267  1.00 85.41  ? 171 GLU   B OE1 1 
ATOM   1645 O OE2 . GLU   B 2 162 ? -25.277 -11.229 -1.413  1.00 86.93  ? 171 GLU   B OE2 1 
HETATM 1646 S S   A DMS   C 3 .   ? -17.368 12.175  -0.340  0.50 297.97 ? 201 DMS   B S   1 
HETATM 1647 S S   B DMS   C 3 .   ? -17.368 12.175  -0.340  0.50 297.97 ? 201 DMS   B S   1 
HETATM 1648 O O   A DMS   C 3 .   ? -17.220 10.730  -0.127  0.50 297.98 ? 201 DMS   B O   1 
HETATM 1649 O O   B DMS   C 3 .   ? -17.220 10.730  -0.127  0.50 297.98 ? 201 DMS   B O   1 
HETATM 1650 C C1  A DMS   C 3 .   ? -19.094 12.404  -0.652  0.50 297.98 ? 201 DMS   B C1  1 
HETATM 1651 C C1  B DMS   C 3 .   ? -19.094 12.404  -0.652  0.50 297.98 ? 201 DMS   B C1  1 
HETATM 1652 C C2  A DMS   C 3 .   ? -16.765 12.442  -1.979  0.50 297.95 ? 201 DMS   B C2  1 
HETATM 1653 C C2  B DMS   C 3 .   ? -16.765 12.442  -1.979  0.50 297.95 ? 201 DMS   B C2  1 
HETATM 1654 N N1  . A1BGX D 4 .   ? -4.039  6.058   -15.634 0.72 66.54  ? 202 A1BGX B N1  1 
HETATM 1655 N N3  . A1BGX D 4 .   ? -8.925  3.859   -10.489 0.72 62.70  ? 202 A1BGX B N3  1 
HETATM 1656 C C4  . A1BGX D 4 .   ? -5.230  5.565   -15.987 0.72 66.26  ? 202 A1BGX B C4  1 
HETATM 1657 C C5  . A1BGX D 4 .   ? -6.117  6.179   -16.863 0.72 65.87  ? 202 A1BGX B C5  1 
HETATM 1658 C C6  . A1BGX D 4 .   ? -7.422  5.560   -17.249 0.72 64.89  ? 202 A1BGX B C6  1 
HETATM 1659 C C7  . A1BGX D 4 .   ? -7.635  5.213   -18.584 0.72 64.52  ? 202 A1BGX B C7  1 
HETATM 1660 C C8  . A1BGX D 4 .   ? -8.793  4.582   -18.992 0.72 64.30  ? 202 A1BGX B C8  1 
HETATM 1661 C C10 . A1BGX D 4 .   ? -9.596  4.621   -16.754 0.72 64.18  ? 202 A1BGX B C10 1 
HETATM 1662 C C13 . A1BGX D 4 .   ? -8.748  4.595   -12.620 0.72 63.13  ? 202 A1BGX B C13 1 
HETATM 1663 C C15 . A1BGX D 4 .   ? -8.563  5.952   -9.262  0.72 62.60  ? 202 A1BGX B C15 1 
HETATM 1664 C C17 . A1BGX D 4 .   ? -5.697  7.384   -17.428 0.72 66.40  ? 202 A1BGX B C17 1 
HETATM 1665 C C1  . A1BGX D 4 .   ? -4.788  10.254  -17.344 0.72 67.44  ? 202 A1BGX B C1  1 
HETATM 1666 O O1  . A1BGX D 4 .   ? -4.012  9.083   -17.580 0.72 67.37  ? 202 A1BGX B O1  1 
HETATM 1667 C C2  . A1BGX D 4 .   ? -4.479  7.917   -17.063 0.72 66.85  ? 202 A1BGX B C2  1 
HETATM 1668 C C3  . A1BGX D 4 .   ? -3.665  7.216   -16.191 0.72 66.69  ? 202 A1BGX B C3  1 
HETATM 1669 C C9  . A1BGX D 4 .   ? -9.793  4.324   -18.086 0.72 64.10  ? 202 A1BGX B C9  1 
HETATM 1670 C C11 . A1BGX D 4 .   ? -8.448  5.292   -16.327 0.72 64.38  ? 202 A1BGX B C11 1 
HETATM 1671 C C12 . A1BGX D 4 .   ? -8.375  5.587   -14.857 0.72 64.00  ? 202 A1BGX B C12 1 
HETATM 1672 O O2  . A1BGX D 4 .   ? -7.984  6.669   -14.448 0.72 64.20  ? 202 A1BGX B O2  1 
HETATM 1673 N N2  . A1BGX D 4 .   ? -8.740  4.570   -14.025 0.72 63.49  ? 202 A1BGX B N2  1 
HETATM 1674 C C14 . A1BGX D 4 .   ? -8.966  3.505   -11.765 0.72 62.84  ? 202 A1BGX B C14 1 
HETATM 1675 N N4  . A1BGX D 4 .   ? -8.680  5.208   -10.513 0.72 62.66  ? 202 A1BGX B N4  1 
HETATM 1676 C C16 . A1BGX D 4 .   ? -8.578  5.686   -11.776 0.72 62.88  ? 202 A1BGX B C16 1 
HETATM 1677 S S   C SO4   E 5 .   ? -18.909 11.642  -0.251  0.50 90.16  ? 203 SO4   B S   1 
HETATM 1678 S S   D SO4   E 5 .   ? -18.909 11.642  -0.251  0.50 90.16  ? 203 SO4   B S   1 
HETATM 1679 O O1  C SO4   E 5 .   ? -18.382 12.060  -1.550  0.50 90.05  ? 203 SO4   B O1  1 
HETATM 1680 O O1  D SO4   E 5 .   ? -18.382 12.060  -1.550  0.50 90.05  ? 203 SO4   B O1  1 
HETATM 1681 O O2  C SO4   E 5 .   ? -19.767 12.694  0.296   0.50 90.16  ? 203 SO4   B O2  1 
HETATM 1682 O O2  D SO4   E 5 .   ? -19.767 12.694  0.296   0.50 90.16  ? 203 SO4   B O2  1 
HETATM 1683 O O3  C SO4   E 5 .   ? -19.686 10.413  -0.388  0.50 90.11  ? 203 SO4   B O3  1 
HETATM 1684 O O3  D SO4   E 5 .   ? -19.686 10.413  -0.388  0.50 90.11  ? 203 SO4   B O3  1 
HETATM 1685 O O4  C SO4   E 5 .   ? -17.791 11.393  0.658   0.50 90.30  ? 203 SO4   B O4  1 
HETATM 1686 O O4  D SO4   E 5 .   ? -17.791 11.393  0.658   0.50 90.30  ? 203 SO4   B O4  1 
HETATM 1687 O O   . HOH   F 6 .   ? -7.924  0.543   3.379   1.00 47.68  ? 101 HOH   A O   1 
HETATM 1688 O O   . HOH   F 6 .   ? -23.484 18.976  -19.501 1.00 52.18  ? 102 HOH   A O   1 
HETATM 1689 O O   . HOH   F 6 .   ? -4.091  -14.198 -25.471 1.00 39.85  ? 103 HOH   A O   1 
HETATM 1690 O O   C HOH   F 6 .   ? -26.137 16.252  -5.928  0.50 59.82  ? 104 HOH   A O   1 
HETATM 1691 O O   D HOH   F 6 .   ? -26.137 16.252  -5.928  0.50 59.82  ? 104 HOH   A O   1 
HETATM 1692 O O   . HOH   F 6 .   ? -2.031  -3.685  -6.280  1.00 51.76  ? 105 HOH   A O   1 
HETATM 1693 O O   . HOH   F 6 .   ? -9.295  -6.528  -25.500 1.00 49.46  ? 106 HOH   A O   1 
HETATM 1694 O O   . HOH   F 6 .   ? -30.547 12.955  -16.494 1.00 53.99  ? 107 HOH   A O   1 
HETATM 1695 O O   A HOH   F 6 .   ? -7.915  -1.645  6.715   0.50 55.97  ? 108 HOH   A O   1 
HETATM 1696 O O   B HOH   F 6 .   ? -7.915  -1.645  6.715   0.50 55.97  ? 108 HOH   A O   1 
HETATM 1697 O O   C HOH   F 6 .   ? -25.157 12.582  -23.832 0.50 45.87  ? 109 HOH   A O   1 
HETATM 1698 O O   D HOH   F 6 .   ? -25.157 12.582  -23.832 0.50 45.87  ? 109 HOH   A O   1 
HETATM 1699 O O   . HOH   F 6 .   ? -24.108 9.407   -27.547 1.00 45.11  ? 110 HOH   A O   1 
HETATM 1700 O O   . HOH   F 6 .   ? -2.847  -11.701 -7.089  1.00 41.07  ? 111 HOH   A O   1 
HETATM 1701 O O   . HOH   F 6 .   ? -6.892  -9.054  -3.152  1.00 44.35  ? 112 HOH   A O   1 
HETATM 1702 O O   A HOH   F 6 .   ? -29.096 15.924  -15.049 0.50 54.08  ? 113 HOH   A O   1 
HETATM 1703 O O   B HOH   F 6 .   ? -29.096 15.924  -15.049 0.50 54.08  ? 113 HOH   A O   1 
HETATM 1704 O O   . HOH   F 6 .   ? -22.332 -9.268  -34.642 1.00 56.02  ? 114 HOH   A O   1 
HETATM 1705 O O   . HOH   F 6 .   ? -26.613 -3.710  -35.349 1.00 68.14  ? 115 HOH   A O   1 
HETATM 1706 O O   . HOH   F 6 .   ? -3.687  -4.282  0.303   1.00 53.19  ? 116 HOH   A O   1 
HETATM 1707 O O   C HOH   F 6 .   ? -21.926 15.213  -6.168  0.50 45.74  ? 117 HOH   A O   1 
HETATM 1708 O O   D HOH   F 6 .   ? -21.926 15.213  -6.168  0.50 45.74  ? 117 HOH   A O   1 
HETATM 1709 O O   . HOH   F 6 .   ? -4.573  -10.137 -5.564  1.00 44.97  ? 118 HOH   A O   1 
HETATM 1710 O O   C HOH   F 6 .   ? -26.360 2.207   -29.056 0.50 47.46  ? 119 HOH   A O   1 
HETATM 1711 O O   D HOH   F 6 .   ? -28.044 1.132   -29.332 0.50 54.70  ? 119 HOH   A O   1 
HETATM 1712 O O   . HOH   F 6 .   ? -28.551 -6.225  -27.965 1.00 57.03  ? 120 HOH   A O   1 
HETATM 1713 O O   . HOH   F 6 .   ? -31.063 0.299   -23.059 1.00 51.95  ? 121 HOH   A O   1 
HETATM 1714 O O   A HOH   F 6 .   ? 7.336   -4.617  -17.185 0.50 58.87  ? 122 HOH   A O   1 
HETATM 1715 O O   B HOH   F 6 .   ? 5.821   -4.799  -16.562 0.50 58.47  ? 122 HOH   A O   1 
HETATM 1716 O O   . HOH   F 6 .   ? -3.757  -0.648  -0.187  1.00 56.18  ? 123 HOH   A O   1 
HETATM 1717 O O   A HOH   F 6 .   ? 0.386   -10.866 -22.655 0.50 54.22  ? 124 HOH   A O   1 
HETATM 1718 O O   B HOH   F 6 .   ? -0.682  -12.530 -23.585 0.50 45.15  ? 124 HOH   A O   1 
HETATM 1719 O O   . HOH   F 6 .   ? -2.702  -8.798  -3.343  1.00 59.99  ? 125 HOH   A O   1 
HETATM 1720 O O   . HOH   F 6 .   ? -4.831  2.448   -10.175 1.00 69.94  ? 126 HOH   A O   1 
HETATM 1721 O O   C HOH   F 6 .   ? -24.522 15.412  -24.349 0.50 73.83  ? 127 HOH   A O   1 
HETATM 1722 O O   D HOH   F 6 .   ? -24.522 15.412  -24.349 0.50 73.83  ? 127 HOH   A O   1 
HETATM 1723 O O   C HOH   F 6 .   ? -1.360  -5.928  -3.981  0.50 63.14  ? 128 HOH   A O   1 
HETATM 1724 O O   D HOH   F 6 .   ? -1.360  -5.928  -3.981  0.50 63.14  ? 128 HOH   A O   1 
HETATM 1725 O O   C HOH   G 6 .   ? -20.023 14.335  1.875   0.50 63.76  ? 301 HOH   B O   1 
HETATM 1726 O O   D HOH   G 6 .   ? -20.023 14.335  1.875   0.50 63.76  ? 301 HOH   B O   1 
HETATM 1727 O O   . HOH   G 6 .   ? -15.294 9.409   -0.679  1.00 46.04  ? 302 HOH   B O   1 
HETATM 1728 O O   . HOH   G 6 .   ? -15.700 -10.033 -15.092 1.00 51.70  ? 303 HOH   B O   1 
HETATM 1729 O O   . HOH   G 6 .   ? -30.857 12.536  -19.323 1.00 55.91  ? 304 HOH   B O   1 
HETATM 1730 O O   . HOH   G 6 .   ? -34.122 1.929   -15.369 1.00 46.83  ? 305 HOH   B O   1 
HETATM 1731 O O   . HOH   G 6 .   ? -16.592 -7.213  -8.323  1.00 58.88  ? 306 HOH   B O   1 
HETATM 1732 O O   . HOH   G 6 .   ? -19.430 -12.010 -25.501 1.00 54.33  ? 307 HOH   B O   1 
HETATM 1733 O O   . HOH   G 6 .   ? -16.570 20.993  -14.351 1.00 55.67  ? 308 HOH   B O   1 
HETATM 1734 O O   . HOH   G 6 .   ? -16.413 26.055  -12.392 1.00 71.33  ? 309 HOH   B O   1 
HETATM 1735 O O   . HOH   G 6 .   ? -9.374  2.261   -8.483  1.00 48.45  ? 310 HOH   B O   1 
HETATM 1736 O O   . HOH   G 6 .   ? -27.708 -6.848  -5.597  1.00 50.77  ? 311 HOH   B O   1 
HETATM 1737 O O   A HOH   G 6 .   ? -11.940 -17.821 -27.942 0.50 54.33  ? 312 HOH   B O   1 
HETATM 1738 O O   B HOH   G 6 .   ? -11.940 -17.821 -27.942 0.50 54.33  ? 312 HOH   B O   1 
HETATM 1739 O O   . HOH   G 6 .   ? -6.450  -0.296  -10.906 1.00 38.71  ? 313 HOH   B O   1 
HETATM 1740 O O   A HOH   G 6 .   ? -28.970 -4.446  -22.084 0.50 71.69  ? 314 HOH   B O   1 
HETATM 1741 O O   B HOH   G 6 .   ? -28.970 -4.446  -22.084 0.50 71.69  ? 314 HOH   B O   1 
HETATM 1742 O O   A HOH   G 6 .   ? -12.490 2.183   -5.631  0.50 37.99  ? 315 HOH   B O   1 
HETATM 1743 O O   B HOH   G 6 .   ? -11.406 1.891   -5.872  0.50 41.11  ? 315 HOH   B O   1 
HETATM 1744 O O   . HOH   G 6 .   ? -17.188 13.002  -5.450  1.00 46.35  ? 316 HOH   B O   1 
HETATM 1745 O O   . HOH   G 6 .   ? -15.241 -4.521  1.478   1.00 41.60  ? 317 HOH   B O   1 
HETATM 1746 O O   . HOH   G 6 .   ? -21.665 -12.376 -12.965 1.00 52.11  ? 318 HOH   B O   1 
HETATM 1747 O O   . HOH   G 6 .   ? -21.834 -13.723 -21.674 1.00 59.38  ? 319 HOH   B O   1 
HETATM 1748 O O   C HOH   G 6 .   ? -5.510  2.817   -12.632 0.37 62.20  ? 320 HOH   B O   1 
HETATM 1749 O O   D HOH   G 6 .   ? -5.507  2.821   -12.636 0.35 62.29  ? 320 HOH   B O   1 
HETATM 1750 O O   . HOH   G 6 .   ? -27.846 -6.202  -18.572 1.00 47.96  ? 321 HOH   B O   1 
HETATM 1751 O O   . HOH   G 6 .   ? -26.174 -7.954  -16.536 1.00 40.42  ? 322 HOH   B O   1 
HETATM 1752 O O   A HOH   G 6 .   ? -18.486 19.382  -21.635 0.50 58.32  ? 323 HOH   B O   1 
HETATM 1753 O O   B HOH   G 6 .   ? -18.486 19.382  -21.635 0.50 58.32  ? 323 HOH   B O   1 
HETATM 1754 O O   . HOH   G 6 .   ? -21.227 7.215   -0.000  0.50 44.00  ? 324 HOH   B O   1 
HETATM 1755 O O   . HOH   G 6 .   ? -17.365 15.165  -30.694 1.00 56.28  ? 325 HOH   B O   1 
HETATM 1756 O O   . HOH   G 6 .   ? -17.978 -10.743 -16.461 1.00 43.58  ? 326 HOH   B O   1 
HETATM 1757 O O   . HOH   G 6 .   ? -12.441 -3.366  -10.167 1.00 33.46  ? 327 HOH   B O   1 
HETATM 1758 O O   . HOH   G 6 .   ? -16.156 -14.535 -16.547 1.00 49.13  ? 328 HOH   B O   1 
HETATM 1759 O O   . HOH   G 6 .   ? -13.018 -2.143  -14.794 1.00 35.86  ? 329 HOH   B O   1 
HETATM 1760 O O   . HOH   G 6 .   ? -21.411 5.856   -32.791 1.00 61.03  ? 330 HOH   B O   1 
HETATM 1761 O O   . HOH   G 6 .   ? -7.084  -10.688 -5.423  1.00 50.97  ? 331 HOH   B O   1 
HETATM 1762 O O   . HOH   G 6 .   ? -35.512 3.935   -8.694  1.00 64.69  ? 332 HOH   B O   1 
HETATM 1763 O O   . HOH   G 6 .   ? -18.882 14.917  -22.143 1.00 40.07  ? 333 HOH   B O   1 
HETATM 1764 O O   C HOH   G 6 .   ? -21.386 14.568  -34.638 0.50 63.11  ? 334 HOH   B O   1 
HETATM 1765 O O   D HOH   G 6 .   ? -21.386 14.568  -34.638 0.50 63.11  ? 334 HOH   B O   1 
HETATM 1766 O O   . HOH   G 6 .   ? -7.330  -6.639  0.309   1.00 47.30  ? 335 HOH   B O   1 
HETATM 1767 O O   . HOH   G 6 .   ? -20.164 -7.814  -2.775  1.00 62.09  ? 336 HOH   B O   1 
HETATM 1768 O O   C HOH   G 6 .   ? -7.369  10.737  -19.424 0.37 31.14  ? 337 HOH   B O   1 
HETATM 1769 O O   D HOH   G 6 .   ? -7.995  12.433  -19.773 0.35 46.10  ? 337 HOH   B O   1 
HETATM 1770 O O   . HOH   G 6 .   ? -23.867 -14.706 -18.040 1.00 64.90  ? 338 HOH   B O   1 
HETATM 1771 O O   . HOH   G 6 .   ? -31.942 7.268   -4.325  1.00 63.70  ? 339 HOH   B O   1 
HETATM 1772 O O   . HOH   G 6 .   ? -26.048 -4.483  -4.006  1.00 37.99  ? 340 HOH   B O   1 
HETATM 1773 O O   . HOH   G 6 .   ? -14.505 -12.274 -16.393 1.00 47.54  ? 341 HOH   B O   1 
HETATM 1774 O O   A HOH   G 6 .   ? -32.386 -6.859  -6.989  0.50 54.36  ? 342 HOH   B O   1 
HETATM 1775 O O   B HOH   G 6 .   ? -32.386 -6.859  -6.989  0.50 54.36  ? 342 HOH   B O   1 
HETATM 1776 O O   . HOH   G 6 .   ? -35.761 -5.341  -10.264 1.00 55.29  ? 343 HOH   B O   1 
HETATM 1777 O O   . HOH   G 6 .   ? -16.002 -14.320 -30.811 1.00 61.48  ? 344 HOH   B O   1 
HETATM 1778 O O   . HOH   G 6 .   ? -30.585 4.656   -2.432  1.00 54.54  ? 345 HOH   B O   1 
HETATM 1779 O O   . HOH   G 6 .   ? -14.997 16.743  -20.190 1.00 54.97  ? 346 HOH   B O   1 
HETATM 1780 O O   . HOH   G 6 .   ? -8.793  -10.559 -7.438  1.00 60.07  ? 347 HOH   B O   1 
HETATM 1781 O O   . HOH   G 6 .   ? -19.564 -13.410 -23.056 1.00 41.97  ? 348 HOH   B O   1 
HETATM 1782 O O   A HOH   G 6 .   ? -21.303 2.471   -32.595 0.50 59.59  ? 349 HOH   B O   1 
HETATM 1783 O O   B HOH   G 6 .   ? -21.303 2.471   -32.595 0.50 59.59  ? 349 HOH   B O   1 
HETATM 1784 O O   . HOH   G 6 .   ? -19.442 -5.620  -0.847  1.00 46.37  ? 350 HOH   B O   1 
HETATM 1785 O O   . HOH   G 6 .   ? -29.588 -1.507  -19.021 1.00 58.43  ? 351 HOH   B O   1 
HETATM 1786 O O   . HOH   G 6 .   ? -11.696 -5.160  -8.362  1.00 44.16  ? 352 HOH   B O   1 
HETATM 1787 O O   . HOH   G 6 .   ? -14.633 -6.595  -1.546  1.00 60.20  ? 353 HOH   B O   1 
HETATM 1788 O O   . HOH   G 6 .   ? -18.931 25.479  -14.448 1.00 59.99  ? 354 HOH   B O   1 
HETATM 1789 O O   . HOH   G 6 .   ? -0.742  0.692   -13.196 1.00 68.01  ? 355 HOH   B O   1 
HETATM 1790 O O   . HOH   G 6 .   ? -10.981 7.877   -13.942 1.00 54.88  ? 356 HOH   B O   1 
HETATM 1791 O O   . HOH   G 6 .   ? -17.220 16.642  -21.967 1.00 51.02  ? 357 HOH   B O   1 
HETATM 1792 O O   . HOH   G 6 .   ? -0.932  -13.849 -9.888  1.00 63.76  ? 358 HOH   B O   1 
HETATM 1793 O O   A HOH   G 6 .   ? -20.682 24.806  -17.069 0.50 64.40  ? 359 HOH   B O   1 
HETATM 1794 O O   B HOH   G 6 .   ? -20.682 24.806  -17.069 0.50 64.40  ? 359 HOH   B O   1 
HETATM 1795 O O   . HOH   G 6 .   ? -29.549 -5.323  -0.850  1.00 47.92  ? 360 HOH   B O   1 
HETATM 1796 O O   C HOH   G 6 .   ? -9.873  -16.008 -24.261 0.50 51.23  ? 361 HOH   B O   1 
HETATM 1797 O O   D HOH   G 6 .   ? -9.873  -16.008 -24.261 0.50 51.23  ? 361 HOH   B O   1 
HETATM 1798 O O   A HOH   G 6 .   ? -30.304 -7.693  -5.155  0.50 58.57  ? 362 HOH   B O   1 
HETATM 1799 O O   B HOH   G 6 .   ? -30.304 -7.693  -5.155  0.50 58.57  ? 362 HOH   B O   1 
HETATM 1800 O O   A HOH   G 6 .   ? -23.065 2.940   0.140   0.50 43.21  ? 363 HOH   B O   1 
HETATM 1801 O O   B HOH   G 6 .   ? -22.378 4.358   0.623   0.50 65.38  ? 363 HOH   B O   1 
HETATM 1802 O O   A HOH   G 6 .   ? -10.073 21.972  -14.442 0.50 73.93  ? 364 HOH   B O   1 
HETATM 1803 O O   B HOH   G 6 .   ? -10.073 21.972  -14.442 0.50 73.93  ? 364 HOH   B O   1 
HETATM 1804 O O   . HOH   G 6 .   ? -23.200 -7.528  -2.499  1.00 67.55  ? 365 HOH   B O   1 
HETATM 1805 O O   A HOH   G 6 .   ? -31.512 -10.934 -27.063 0.25 85.71  ? 366 HOH   B O   1 
HETATM 1806 O O   B HOH   G 6 .   ? -31.512 -10.934 -27.063 0.25 85.71  ? 366 HOH   B O   1 
HETATM 1807 O O   . HOH   G 6 .   ? -19.162 -11.908 -13.621 1.00 48.27  ? 367 HOH   B O   1 
HETATM 1808 O O   C HOH   G 6 .   ? -9.869  9.000   -11.676 0.37 46.55  ? 368 HOH   B O   1 
HETATM 1809 O O   D HOH   G 6 .   ? -10.260 9.291   -10.075 0.35 40.94  ? 368 HOH   B O   1 
HETATM 1810 O O   C HOH   G 6 .   ? -19.276 -20.050 -28.032 0.50 64.45  ? 369 HOH   B O   1 
HETATM 1811 O O   D HOH   G 6 .   ? -19.276 -20.050 -28.032 0.50 64.45  ? 369 HOH   B O   1 
HETATM 1812 O O   A HOH   G 6 .   ? -11.284 -7.041  1.930   0.50 62.90  ? 370 HOH   B O   1 
HETATM 1813 O O   B HOH   G 6 .   ? -11.284 -7.041  1.930   0.50 62.90  ? 370 HOH   B O   1 
HETATM 1814 O O   A HOH   G 6 .   ? -11.719 13.832  -14.080 0.50 73.00  ? 371 HOH   B O   1 
HETATM 1815 O O   B HOH   G 6 .   ? -11.719 13.832  -14.080 0.50 73.00  ? 371 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   ? 0.9369 0.3730 0.8383 0.0604  0.0969  -0.0521 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.9292 0.4023 0.8098 0.0896  0.0943  -0.0572 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.8944 0.3904 0.7684 0.0992  0.1044  -0.0293 50  ASP   A C   
4    O O   . ASP   A 7   ? 0.9211 0.3797 0.7876 0.1031  0.1143  -0.0058 50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.9949 0.4297 0.8530 0.1193  0.0893  -0.0711 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 1.0792 0.5641 0.9265 0.1435  0.0844  -0.0874 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 1.0773 0.6060 0.9321 0.1330  0.0799  -0.1044 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 1.1280 0.6105 0.9596 0.1733  0.0855  -0.0827 50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.8339 0.3883 0.7082 0.1036  0.1023  -0.0320 51  MET   A N   
10   C CA  . MET   A 8   ? 0.7934 0.3722 0.6623 0.1115  0.1091  -0.0098 51  MET   A CA  
11   C C   . MET   A 8   ? 0.7648 0.3598 0.6157 0.1431  0.1059  -0.0120 51  MET   A C   
12   O O   . MET   A 8   ? 0.7564 0.3752 0.6066 0.1540  0.0990  -0.0332 51  MET   A O   
13   C CB  . MET   A 8   ? 0.7656 0.3938 0.6494 0.0921  0.1089  -0.0079 51  MET   A CB  
14   C CG  . MET   A 8   ? 0.7675 0.3881 0.6728 0.0635  0.1117  -0.0034 51  MET   A CG  
15   S SD  . MET   A 8   ? 0.7456 0.4234 0.6645 0.0477  0.1102  0.0001  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.7783 0.4431 0.7279 0.0179  0.1146  0.0065  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.7431 0.3279 0.5801 0.1585  0.1113  0.0095  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.7411 0.3429 0.5623 0.1902  0.1060  0.0078  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.7285 0.3565 0.5434 0.1952  0.1086  0.0253  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.7282 0.3467 0.5438 0.1800  0.1179  0.0448  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.7660 0.3169 0.5651 0.2187  0.1046  0.0100  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.8113 0.3043 0.5918 0.2201  0.1156  0.0388  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.8447 0.2868 0.6315 0.1981  0.1233  0.0446  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.8427 0.3300 0.5979 0.2446  0.1185  0.0595  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.8900 0.2771 0.6615 0.1965  0.1370  0.0733  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.8878 0.3200 0.6211 0.2470  0.1320  0.0890  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.9207 0.3022 0.6633 0.2214  0.1429  0.0972  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.9798 0.3060 0.7033 0.2195  0.1601  0.1290  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.7103 0.3747 0.5211 0.2163  0.0999  0.0164  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.7069 0.3953 0.5095 0.2243  0.0989  0.0283  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.7295 0.4022 0.5049 0.2621  0.0937  0.0359  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.7363 0.3986 0.5057 0.2849  0.0867  0.0244  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.6871 0.4325 0.5089 0.2132  0.0919  0.0126  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.6728 0.4495 0.5053 0.2279  0.0821  -0.0114 53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.6798 0.4364 0.5196 0.1793  0.0972  0.0106  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.6656 0.4959 0.5171 0.2160  0.0770  -0.0237 53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.7448 0.4161 0.5011 0.2714  0.0967  0.0547  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.7779 0.4341 0.5010 0.3099  0.0912  0.0643  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.7693 0.4655 0.4878 0.3170  0.0839  0.0634  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.7665 0.4690 0.4884 0.2968  0.0929  0.0749  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.8399 0.4360 0.5317 0.3160  0.1073  0.0958  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.9341 0.4733 0.6198 0.3164  0.1138  0.1008  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 1.0604 0.5379 0.7158 0.3191  0.1325  0.1351  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 1.0918 0.5763 0.7372 0.3133  0.1443  0.1557  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 1.1073 0.5275 0.7486 0.3270  0.1367  0.1417  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.7644 0.4866 0.4742 0.3477  0.0666  0.0493  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.7666 0.5242 0.4717 0.3547  0.0570  0.0451  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.7885 0.5159 0.4544 0.3672  0.0679  0.0734  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.8257 0.5074 0.4606 0.3851  0.0774  0.0943  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.7794 0.5742 0.4874 0.3842  0.0341  0.0213  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.8018 0.6409 0.5217 0.3787  0.0216  0.0069  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.8280 0.7186 0.5762 0.3894  0.0000  -0.0251 55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.8317 0.7584 0.5948 0.3780  -0.0114 -0.0396 55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.8477 0.7802 0.5852 0.4035  -0.0259 -0.0419 55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.8951 0.8018 0.5886 0.4431  -0.0298 -0.0289 55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.7855 0.7453 0.5376 0.3905  -0.0366 -0.0569 55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.7760 0.5250 0.4432 0.3555  0.0694  0.0759  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.8036 0.5320 0.4341 0.3684  0.0815  0.1014  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.8083 0.5652 0.4180 0.3929  0.0656  0.0916  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.8346 0.5750 0.4045 0.4141  0.0735  0.1110  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.8045 0.5246 0.4498 0.3348  0.1029  0.1184  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.7870 0.5849 0.4226 0.3900  0.0442  0.0614  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.7899 0.6140 0.4096 0.4125  0.0250  0.0466  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.7651 0.6319 0.4248 0.3926  0.0072  0.0156  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.7432 0.6220 0.4428 0.3608  0.0112  0.0065  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.7746 0.6624 0.4214 0.4119  -0.0124 -0.0008 58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.7671 0.6905 0.4478 0.3941  -0.0304 -0.0300 58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.7903 0.7043 0.4679 0.3731  -0.0200 -0.0213 58  ASP   A C   
69   O O   . ASP   A 15  ? 0.8262 0.7183 0.4671 0.3874  -0.0078 0.0000  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.7873 0.7338 0.4529 0.4269  -0.0590 -0.0537 58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.8403 0.8130 0.5211 0.4475  -0.0781 -0.0740 58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.8292 0.7951 0.5218 0.4444  -0.0675 -0.0657 58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.8741 0.8743 0.5529 0.4705  -0.1052 -0.0994 58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.7687 0.7000 0.4822 0.3424  -0.0254 -0.0383 59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.7813 0.7034 0.4912 0.3258  -0.0195 -0.0335 59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.8024 0.7355 0.5002 0.3425  -0.0428 -0.0558 59  ILE   A C   
77   O O   . ILE   A 16  ? 0.7794 0.7327 0.5078 0.3285  -0.0601 -0.0818 59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.7661 0.6926 0.5150 0.2851  -0.0114 -0.0366 59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.7700 0.6837 0.5259 0.2723  0.0097  -0.0164 59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.7739 0.6908 0.5186 0.2714  -0.0099 -0.0354 59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.7683 0.6885 0.5582 0.2376  0.0166  -0.0209 59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.8274 0.7478 0.4801 0.3735  -0.0432 -0.0466 60  THR   A N   
83   N N   B THR   A 17  ? 0.8260 0.7463 0.4791 0.3728  -0.0430 -0.0466 60  THR   A N   
84   N N   C THR   A 17  ? 0.8275 0.7479 0.4802 0.3735  -0.0432 -0.0466 60  THR   A N   
85   N N   D THR   A 17  ? 0.8260 0.7464 0.4792 0.3728  -0.0431 -0.0467 60  THR   A N   
86   C CA  A THR   A 17  ? 0.8436 0.7704 0.4756 0.3954  -0.0662 -0.0683 60  THR   A CA  
87   C CA  B THR   A 17  ? 0.8406 0.7680 0.4734 0.3953  -0.0667 -0.0689 60  THR   A CA  
88   C CA  C THR   A 17  ? 0.8437 0.7705 0.4758 0.3954  -0.0662 -0.0683 60  THR   A CA  
89   C CA  D THR   A 17  ? 0.8404 0.7679 0.4736 0.3950  -0.0669 -0.0692 60  THR   A CA  
90   C C   A THR   A 17  ? 0.8759 0.7842 0.4693 0.4095  -0.0552 -0.0531 60  THR   A C   
91   C C   B THR   A 17  ? 0.8758 0.7847 0.4669 0.4125  -0.0565 -0.0538 60  THR   A C   
92   C C   C THR   A 17  ? 0.8761 0.7843 0.4695 0.4095  -0.0552 -0.0531 60  THR   A C   
93   C C   D THR   A 17  ? 0.8758 0.7849 0.4668 0.4128  -0.0567 -0.0541 60  THR   A C   
94   O O   A THR   A 17  ? 0.8895 0.7841 0.4618 0.4157  -0.0307 -0.0235 60  THR   A O   
95   O O   B THR   A 17  ? 0.8909 0.7862 0.4581 0.4216  -0.0328 -0.0244 60  THR   A O   
96   O O   C THR   A 17  ? 0.8896 0.7843 0.4620 0.4157  -0.0307 -0.0235 60  THR   A O   
97   O O   D THR   A 17  ? 0.8911 0.7865 0.4578 0.4223  -0.0332 -0.0246 60  THR   A O   
98   C CB  A THR   A 17  ? 0.8622 0.8012 0.4684 0.4358  -0.0863 -0.0808 60  THR   A CB  
99   C CB  B THR   A 17  ? 0.8514 0.7938 0.4669 0.4310  -0.0868 -0.0826 60  THR   A CB  
100  C CB  C THR   A 17  ? 0.8623 0.8013 0.4685 0.4358  -0.0863 -0.0808 60  THR   A CB  
101  C CB  D THR   A 17  ? 0.8498 0.7936 0.4681 0.4295  -0.0881 -0.0846 60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.8955 0.8148 0.4527 0.4670  -0.0698 -0.0521 60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.8347 0.8024 0.4971 0.4134  -0.0978 -0.1017 60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.8956 0.8148 0.4528 0.4670  -0.0698 -0.0521 60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.8320 0.8022 0.4992 0.4100  -0.1005 -0.1060 60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.8453 0.8101 0.4903 0.4286  -0.0995 -0.0989 60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.8608 0.8102 0.4476 0.4612  -0.1134 -0.1066 60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.8454 0.8102 0.4904 0.4286  -0.0995 -0.0989 60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.8610 0.8101 0.4473 0.4613  -0.1134 -0.1065 60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.8865 0.7950 0.4707 0.4162  -0.0733 -0.0744 61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.9516 0.8463 0.4956 0.4366  -0.0655 -0.0644 61  TRP   A CA  
112  C C   . TRP   A 18  ? 1.0367 0.9329 0.5273 0.4853  -0.0719 -0.0621 61  TRP   A C   
113  O O   . TRP   A 18  ? 1.0424 0.9508 0.5295 0.5030  -0.0984 -0.0867 61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.9421 0.8318 0.4919 0.4301  -0.0865 -0.0922 61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.9612 0.8388 0.4677 0.4569  -0.0827 -0.0882 61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.9899 0.8673 0.4492 0.4988  -0.0981 -0.1015 61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.9617 0.8281 0.4685 0.4454  -0.0647 -0.0733 61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 1.0065 0.8737 0.4362 0.5144  -0.0879 -0.0944 61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.9896 0.8511 0.4498 0.4821  -0.0680 -0.0776 61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.9503 0.8128 0.4905 0.4107  -0.0465 -0.0572 61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 0.9996 0.8547 0.4498 0.4846  -0.0534 -0.0670 61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.9676 0.8232 0.4975 0.4133  -0.0343 -0.0472 61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.9863 0.8396 0.4736 0.4497  -0.0373 -0.0520 61  TRP   A CH2 
124  N N   A GLU   A 19  ? 1.0643 0.9503 0.5146 0.5067  -0.0478 -0.0331 62  GLU   A N   
125  N N   B GLU   A 19  ? 1.0647 0.9508 0.5151 0.5067  -0.0478 -0.0331 62  GLU   A N   
126  N N   C GLU   A 19  ? 1.0637 0.9497 0.5141 0.5066  -0.0476 -0.0329 62  GLU   A N   
127  N N   D GLU   A 19  ? 1.0637 0.9497 0.5141 0.5066  -0.0476 -0.0329 62  GLU   A N   
128  C CA  A GLU   A 19  ? 1.1022 0.9858 0.4944 0.5545  -0.0500 -0.0265 62  GLU   A CA  
129  C CA  B GLU   A 19  ? 1.1029 0.9865 0.4950 0.5545  -0.0502 -0.0266 62  GLU   A CA  
130  C CA  C GLU   A 19  ? 1.1017 0.9849 0.4932 0.5543  -0.0488 -0.0253 62  GLU   A CA  
131  C CA  D GLU   A 19  ? 1.1017 0.9849 0.4932 0.5543  -0.0488 -0.0253 62  GLU   A CA  
132  C C   A GLU   A 19  ? 1.1361 1.0172 0.4830 0.5845  -0.0522 -0.0317 62  GLU   A C   
133  C C   B GLU   A 19  ? 1.1363 1.0174 0.4831 0.5846  -0.0521 -0.0317 62  GLU   A C   
134  C C   C GLU   A 19  ? 1.1347 1.0160 0.4832 0.5834  -0.0531 -0.0332 62  GLU   A C   
135  C C   D GLU   A 19  ? 1.1347 1.0160 0.4832 0.5834  -0.0531 -0.0332 62  GLU   A C   
136  O O   A GLU   A 19  ? 1.1394 1.0169 0.4837 0.5768  -0.0285 -0.0133 62  GLU   A O   
137  O O   B GLU   A 19  ? 1.1396 1.0170 0.4837 0.5769  -0.0285 -0.0132 62  GLU   A O   
138  O O   C GLU   A 19  ? 1.1376 1.0153 0.4842 0.5754  -0.0309 -0.0166 62  GLU   A O   
139  O O   D GLU   A 19  ? 1.1376 1.0153 0.4842 0.5754  -0.0309 -0.0166 62  GLU   A O   
140  C CB  A GLU   A 19  ? 1.1384 1.0099 0.5128 0.5605  -0.0191 0.0128  62  GLU   A CB  
141  C CB  B GLU   A 19  ? 1.1402 1.0117 0.5144 0.5608  -0.0197 0.0123  62  GLU   A CB  
142  C CB  C GLU   A 19  ? 1.1387 1.0091 0.5100 0.5602  -0.0145 0.0164  62  GLU   A CB  
143  C CB  D GLU   A 19  ? 1.1387 1.0091 0.5100 0.5602  -0.0145 0.0164  62  GLU   A CB  
144  C CG  A GLU   A 19  ? 1.1792 1.0502 0.5890 0.5406  -0.0210 0.0144  62  GLU   A CG  
145  C CG  B GLU   A 19  ? 1.1822 1.0536 0.5937 0.5394  -0.0213 0.0138  62  GLU   A CG  
146  C CG  C GLU   A 19  ? 1.2160 1.0786 0.5204 0.6109  -0.0135 0.0283  62  GLU   A CG  
147  C CG  D GLU   A 19  ? 1.2160 1.0786 0.5204 0.6109  -0.0135 0.0283  62  GLU   A CG  
148  C CD  A GLU   A 19  ? 1.2553 1.1358 0.6530 0.5682  -0.0502 -0.0077 62  GLU   A CD  
149  C CD  B GLU   A 19  ? 1.2575 1.1414 0.6661 0.5613  -0.0532 -0.0129 62  GLU   A CD  
150  C CD  C GLU   A 19  ? 1.2928 1.1386 0.5632 0.6213  0.0262  0.0727  62  GLU   A CD  
151  C CD  D GLU   A 19  ? 1.2928 1.1386 0.5632 0.6213  0.0262  0.0727  62  GLU   A CD  
152  O OE1 A GLU   A 19  ? 1.2469 1.1381 0.6872 0.5482  -0.0605 -0.0204 62  GLU   A OE1 
153  O OE1 B GLU   A 19  ? 1.2495 1.1453 0.7055 0.5364  -0.0631 -0.0269 62  GLU   A OE1 
154  O OE1 C GLU   A 19  ? 1.2966 1.1375 0.6029 0.5857  0.0530  0.0951  62  GLU   A OE1 
155  O OE1 D GLU   A 19  ? 1.2966 1.1375 0.6029 0.5857  0.0530  0.0951  62  GLU   A OE1 
156  O OE2 A GLU   A 19  ? 1.2973 1.1774 0.6425 0.6120  -0.0631 -0.0131 62  GLU   A OE2 
157  O OE2 B GLU   A 19  ? 1.3011 1.1859 0.6599 0.6048  -0.0684 -0.0205 62  GLU   A OE2 
158  O OE2 C GLU   A 19  ? 1.3354 1.1730 0.5429 0.6649  0.0308  0.0850  62  GLU   A OE2 
159  O OE2 D GLU   A 19  ? 1.3354 1.1730 0.5429 0.6649  0.0308  0.0850  62  GLU   A OE2 
160  N N   . LYS   A 20  ? 1.1585 1.0443 0.4712 0.6199  -0.0821 -0.0597 63  LYS   A N   
161  C CA  . LYS   A 20  ? 1.2271 1.1099 0.4914 0.6539  -0.0886 -0.0704 63  LYS   A CA  
162  C C   . LYS   A 20  ? 1.2770 1.1547 0.4835 0.6882  -0.0571 -0.0334 63  LYS   A C   
163  O O   . LYS   A 20  ? 1.2923 1.1659 0.4770 0.7039  -0.0485 -0.0138 63  LYS   A O   
164  C CB  . LYS   A 20  ? 1.2860 1.1755 0.5286 0.6839  -0.1319 -0.1128 63  LYS   A CB  
165  C CG  . LYS   A 20  ? 1.3453 1.2393 0.6455 0.6490  -0.1626 -0.1518 63  LYS   A CG  
166  C CD  . LYS   A 20  ? 1.4118 1.3192 0.7017 0.6746  -0.2060 -0.1935 63  LYS   A CD  
167  C CE  . LYS   A 20  ? 1.4515 1.3590 0.7887 0.6448  -0.2367 -0.2353 63  LYS   A CE  
168  N NZ  . LYS   A 20  ? 1.4885 1.4090 0.8086 0.6754  -0.2805 -0.2795 63  LYS   A NZ  
169  N N   . ASP   A 21  ? 1.2984 1.1758 0.4827 0.6978  -0.0372 -0.0218 64  ASP   A N   
170  C CA  . ASP   A 21  ? 1.3382 1.2147 0.4711 0.7271  -0.0018 0.0155  64  ASP   A CA  
171  C C   . ASP   A 21  ? 1.3181 1.1904 0.4805 0.6959  0.0362  0.0574  64  ASP   A C   
172  O O   . ASP   A 21  ? 1.3371 1.2004 0.4627 0.7154  0.0594  0.0886  64  ASP   A O   
173  C CB  . ASP   A 21  ? 1.4237 1.2962 0.4826 0.7830  -0.0138 0.0128  64  ASP   A CB  
174  C CG  . ASP   A 21  ? 1.5548 1.4320 0.5703 0.8222  -0.0431 -0.0233 64  ASP   A CG  
175  O OD1 . ASP   A 21  ? 1.5960 1.4778 0.5901 0.8350  -0.0269 -0.0188 64  ASP   A OD1 
176  O OD2 . ASP   A 21  ? 1.5963 1.4742 0.5988 0.8421  -0.0830 -0.0577 64  ASP   A OD2 
177  N N   . ALA   A 22  ? 1.2761 1.1518 0.5035 0.6475  0.0418  0.0574  65  ALA   A N   
178  C CA  . ALA   A 22  ? 1.2517 1.1246 0.5117 0.6153  0.0762  0.0927  65  ALA   A CA  
179  C C   . ALA   A 22  ? 1.2411 1.1270 0.4877 0.6216  0.1109  0.1178  65  ALA   A C   
180  O O   . ALA   A 22  ? 1.2412 1.1389 0.4681 0.6420  0.1041  0.1021  65  ALA   A O   
181  C CB  . ALA   A 22  ? 1.2259 1.1013 0.5553 0.5657  0.0675  0.0803  65  ALA   A CB  
182  N N   . GLU   A 23  ? 1.2300 1.1150 0.4912 0.6030  0.1479  0.1548  66  GLU   A N   
183  C CA  . GLU   A 23  ? 1.2220 1.1274 0.4832 0.6031  0.1836  0.1790  66  GLU   A CA  
184  C C   . GLU   A 23  ? 1.1798 1.1061 0.4900 0.5776  0.1750  0.1593  66  GLU   A C   
185  O O   . GLU   A 23  ? 1.1457 1.0676 0.5067 0.5403  0.1624  0.1488  66  GLU   A O   
186  C CB  . GLU   A 23  ? 1.2638 1.1627 0.5462 0.5774  0.2218  0.2191  66  GLU   A CB  
187  C CG  . GLU   A 23  ? 1.3487 1.2758 0.6435 0.5712  0.2610  0.2444  66  GLU   A CG  
188  C CD  . GLU   A 23  ? 1.4546 1.3810 0.8011 0.5274  0.2910  0.2727  66  GLU   A CD  
189  O OE1 . GLU   A 23  ? 1.4814 1.3758 0.8327 0.5125  0.2898  0.2828  66  GLU   A OE1 
190  O OE2 . GLU   A 23  ? 1.4737 1.4325 0.8571 0.5091  0.3145  0.2829  66  GLU   A OE2 
191  N N   . VAL   A 24  ? 1.1727 1.1195 0.4623 0.6020  0.1790  0.1521  67  VAL   A N   
192  C CA  . VAL   A 24  ? 1.1518 1.1146 0.4799 0.5851  0.1692  0.1332  67  VAL   A CA  
193  C C   . VAL   A 24  ? 1.1194 1.1150 0.4759 0.5724  0.2070  0.1596  67  VAL   A C   
194  O O   . VAL   A 24  ? 1.1295 1.1448 0.4524 0.6019  0.2318  0.1754  67  VAL   A O   
195  C CB  . VAL   A 24  ? 1.1787 1.1396 0.4696 0.6209  0.1420  0.1005  67  VAL   A CB  
196  C CG1 . VAL   A 24  ? 1.1713 1.1339 0.5025 0.5994  0.1245  0.0784  67  VAL   A CG1 
197  C CG2 . VAL   A 24  ? 1.2086 1.1436 0.4630 0.6417  0.1079  0.0757  67  VAL   A CG2 
198  N N   . THR   A 25  ? 1.0775 1.0822 0.4963 0.5292  0.2120  0.1641  68  THR   A N   
199  C CA  . THR   A 25  ? 1.0406 1.0824 0.4966 0.5134  0.2452  0.1860  68  THR   A CA  
200  C C   . THR   A 25  ? 0.9979 1.0519 0.5132 0.4793  0.2324  0.1719  68  THR   A C   
201  O O   . THR   A 25  ? 0.9905 1.0202 0.5123 0.4688  0.2009  0.1484  68  THR   A O   
202  C CB  . THR   A 25  ? 1.0620 1.1030 0.5249 0.4977  0.2806  0.2226  68  THR   A CB  
203  O OG1 . THR   A 25  ? 1.0560 1.1400 0.5465 0.4912  0.3162  0.2434  68  THR   A OG1 
204  C CG2 . THR   A 25  ? 1.0598 1.0767 0.5633 0.4560  0.2731  0.2252  68  THR   A CG2 
205  N N   . GLY   A 26  ? 0.9650 1.0580 0.5216 0.4640  0.2564  0.1857  69  GLY   A N   
206  C CA  . GLY   A 26  ? 0.9441 1.0517 0.5532 0.4359  0.2445  0.1736  69  GLY   A CA  
207  C C   . GLY   A 26  ? 0.9398 1.0645 0.5411 0.4608  0.2292  0.1523  69  GLY   A C   
208  O O   . GLY   A 26  ? 0.9697 1.0758 0.5235 0.4944  0.2126  0.1360  69  GLY   A O   
209  N N   . ASN   A 27  ? 0.8994 1.0592 0.5463 0.4468  0.2338  0.1512  70  ASN   A N   
210  C CA  . ASN   A 27  ? 0.8897 1.0635 0.5313 0.4712  0.2179  0.1310  70  ASN   A CA  
211  C C   . ASN   A 27  ? 0.8752 1.0147 0.5293 0.4524  0.1830  0.1097  70  ASN   A C   
212  O O   . ASN   A 27  ? 0.8663 0.9751 0.5300 0.4232  0.1731  0.1102  70  ASN   A O   
213  C CB  . ASN   A 27  ? 0.8861 1.1253 0.5631 0.4780  0.2443  0.1417  70  ASN   A CB  
214  C CG  . ASN   A 27  ? 0.9102 1.1802 0.6544 0.4382  0.2515  0.1492  70  ASN   A CG  
215  O OD1 . ASN   A 27  ? 0.9256 1.1806 0.6933 0.4026  0.2572  0.1611  70  ASN   A OD1 
216  N ND2 . ASN   A 27  ? 0.8993 1.2148 0.6755 0.4461  0.2506  0.1410  70  ASN   A ND2 
217  N N   . SER   A 28  ? 0.8671 1.0076 0.5155 0.4716  0.1648  0.0913  71  SER   A N   
218  C CA  . SER   A 28  ? 0.8812 0.9834 0.5321 0.4583  0.1337  0.0733  71  SER   A CA  
219  C C   . SER   A 28  ? 0.8510 0.9852 0.5353 0.4579  0.1307  0.0700  71  SER   A C   
220  O O   . SER   A 28  ? 0.8649 0.9896 0.5291 0.4851  0.1144  0.0546  71  SER   A O   
221  C CB  . SER   A 28  ? 0.9387 0.9940 0.5387 0.4862  0.1083  0.0514  71  SER   A CB  
222  O OG  . SER   A 28  ? 0.9932 1.0355 0.5564 0.5034  0.1122  0.0514  71  SER   A OG  
223  N N   . PRO   A 29  ? 0.8078 0.9801 0.5426 0.4294  0.1451  0.0829  72  PRO   A N   
224  C CA  . PRO   A 29  ? 0.7758 0.9873 0.5443 0.4327  0.1412  0.0780  72  PRO   A CA  
225  C C   . PRO   A 29  ? 0.7802 0.9532 0.5429 0.4249  0.1108  0.0639  72  PRO   A C   
226  O O   . PRO   A 29  ? 0.7940 0.9251 0.5521 0.3976  0.0998  0.0636  72  PRO   A O   
227  C CB  . PRO   A 29  ? 0.7516 1.0135 0.5771 0.4013  0.1651  0.0946  72  PRO   A CB  
228  C CG  . PRO   A 29  ? 0.7721 0.9935 0.5920 0.3699  0.1681  0.1040  72  PRO   A CG  
229  C CD  . PRO   A 29  ? 0.7870 0.9678 0.5506 0.3946  0.1641  0.1009  72  PRO   A CD  
230  N N   . ARG   A 30  ? 0.7698 0.9568 0.5307 0.4507  0.0982  0.0530  73  ARG   A N   
231  C CA  . ARG   A 30  ? 0.7908 0.9420 0.5429 0.4472  0.0709  0.0424  73  ARG   A CA  
232  C C   . ARG   A 30  ? 0.7393 0.9454 0.5427 0.4333  0.0737  0.0455  73  ARG   A C   
233  O O   . ARG   A 30  ? 0.7128 0.9777 0.5409 0.4549  0.0818  0.0438  73  ARG   A O   
234  C CB  . ARG   A 30  ? 0.8545 0.9738 0.5631 0.4886  0.0514  0.0272  73  ARG   A CB  
235  C CG  . ARG   A 30  ? 0.9704 1.0291 0.6294 0.4984  0.0436  0.0198  73  ARG   A CG  
236  C CD  . ARG   A 30  ? 1.0749 1.0796 0.6884 0.5297  0.0186  0.0029  73  ARG   A CD  
237  N NE  . ARG   A 30  ? 1.1552 1.1194 0.7270 0.5466  0.0135  -0.0079 73  ARG   A NE  
238  C CZ  . ARG   A 30  ? 1.2210 1.1119 0.7562 0.5460  -0.0090 -0.0209 73  ARG   A CZ  
239  N NH1 . ARG   A 30  ? 1.2565 1.1033 0.7879 0.5294  -0.0257 -0.0214 73  ARG   A NH1 
240  N NH2 . ARG   A 30  ? 1.2118 1.0731 0.7136 0.5617  -0.0150 -0.0337 73  ARG   A NH2 
241  N N   . LEU   A 31  ? 0.7187 0.9116 0.5413 0.3972  0.0681  0.0490  74  LEU   A N   
242  C CA  . LEU   A 31  ? 0.6737 0.9184 0.5473 0.3796  0.0691  0.0497  74  LEU   A CA  
243  C C   . LEU   A 31  ? 0.6761 0.8907 0.5389 0.3731  0.0432  0.0419  74  LEU   A C   
244  O O   . LEU   A 31  ? 0.7058 0.8619 0.5398 0.3558  0.0342  0.0429  74  LEU   A O   
245  C CB  . LEU   A 31  ? 0.6569 0.9189 0.5674 0.3399  0.0894  0.0616  74  LEU   A CB  
246  C CG  . LEU   A 31  ? 0.6587 0.9467 0.5785 0.3419  0.1188  0.0742  74  LEU   A CG  
247  C CD1 . LEU   A 31  ? 0.6578 0.9361 0.5977 0.3038  0.1346  0.0867  74  LEU   A CD1 
248  C CD2 . LEU   A 31  ? 0.6246 0.9898 0.5849 0.3582  0.1352  0.0756  74  LEU   A CD2 
249  N N   . ASP   A 32  ? 0.6449 0.9034 0.5330 0.3855  0.0324  0.0345  75  ASP   A N   
250  C CA  . ASP   A 32  ? 0.6542 0.8880 0.5300 0.3811  0.0082  0.0282  75  ASP   A CA  
251  C C   . ASP   A 32  ? 0.6075 0.8608 0.5222 0.3403  0.0129  0.0305  75  ASP   A C   
252  O O   . ASP   A 32  ? 0.5701 0.8892 0.5405 0.3286  0.0243  0.0295  75  ASP   A O   
253  C CB  . ASP   A 32  ? 0.6829 0.9583 0.5685 0.4150  -0.0080 0.0176  75  ASP   A CB  
254  C CG  . ASP   A 32  ? 0.8093 1.0576 0.6508 0.4598  -0.0168 0.0130  75  ASP   A CG  
255  O OD1 . ASP   A 32  ? 0.8715 1.0533 0.6662 0.4624  -0.0165 0.0164  75  ASP   A OD1 
256  O OD2 . ASP   A 32  ? 0.8298 1.1239 0.6846 0.4933  -0.0252 0.0042  75  ASP   A OD2 
257  N N   . VAL   A 33  ? 0.6049 0.8020 0.4926 0.3174  0.0062  0.0332  76  VAL   A N   
258  C CA  . VAL   A 33  ? 0.5730 0.7819 0.4921 0.2807  0.0103  0.0337  76  VAL   A CA  
259  C C   . VAL   A 33  ? 0.5811 0.7591 0.4762 0.2746  -0.0113 0.0279  76  VAL   A C   
260  O O   . VAL   A 33  ? 0.6121 0.7439 0.4585 0.2937  -0.0261 0.0279  76  VAL   A O   
261  C CB  . VAL   A 33  ? 0.5810 0.7639 0.5006 0.2540  0.0303  0.0436  76  VAL   A CB  
262  C CG1 . VAL   A 33  ? 0.5807 0.7821 0.5066 0.2663  0.0507  0.0514  76  VAL   A CG1 
263  C CG2 . VAL   A 33  ? 0.6188 0.7315 0.4898 0.2473  0.0228  0.0457  76  VAL   A CG2 
264  N N   . ALA   A 34  ? 0.5426 0.7450 0.4707 0.2487  -0.0125 0.0229  77  ALA   A N   
265  C CA  . ALA   A 34  ? 0.5453 0.7245 0.4523 0.2414  -0.0305 0.0167  77  ALA   A CA  
266  C C   . ALA   A 34  ? 0.5363 0.6943 0.4512 0.2059  -0.0195 0.0189  77  ALA   A C   
267  O O   . ALA   A 34  ? 0.5121 0.6950 0.4669 0.1866  -0.0028 0.0211  77  ALA   A O   
268  C CB  . ALA   A 34  ? 0.5083 0.7454 0.4498 0.2489  -0.0473 0.0026  77  ALA   A CB  
269  N N   . LEU   A 35  ? 0.5558 0.6667 0.4310 0.1990  -0.0274 0.0194  78  LEU   A N   
270  C CA  . LEU   A 35  ? 0.5585 0.6483 0.4365 0.1699  -0.0183 0.0198  78  LEU   A CA  
271  C C   . LEU   A 35  ? 0.5659 0.6601 0.4384 0.1638  -0.0345 0.0085  78  LEU   A C   
272  O O   . LEU   A 35  ? 0.5940 0.6649 0.4238 0.1808  -0.0492 0.0084  78  LEU   A O   
273  C CB  . LEU   A 35  ? 0.5895 0.6211 0.4243 0.1676  -0.0105 0.0300  78  LEU   A CB  
274  C CG  . LEU   A 35  ? 0.6062 0.6141 0.4378 0.1420  -0.0023 0.0296  78  LEU   A CG  
275  C CD1 . LEU   A 35  ? 0.5800 0.6116 0.4547 0.1234  0.0122  0.0291  78  LEU   A CD1 
276  C CD2 . LEU   A 35  ? 0.6434 0.6015 0.4366 0.1408  0.0035  0.0376  78  LEU   A CD2 
277  N N   . ASP   A 36  ? 0.5312 0.6554 0.4453 0.1422  -0.0330 -0.0017 79  ASP   A N   
278  C CA  . ASP   A 36  ? 0.5333 0.6661 0.4438 0.1384  -0.0507 -0.0164 79  ASP   A CA  
279  C C   . ASP   A 36  ? 0.5603 0.6487 0.4385 0.1227  -0.0459 -0.0160 79  ASP   A C   
280  O O   . ASP   A 36  ? 0.5751 0.6323 0.4431 0.1124  -0.0287 -0.0052 79  ASP   A O   
281  C CB  . ASP   A 36  ? 0.5114 0.7030 0.4851 0.1256  -0.0571 -0.0327 79  ASP   A CB  
282  C CG  . ASP   A 36  ? 0.5351 0.7317 0.5524 0.0939  -0.0405 -0.0345 79  ASP   A CG  
283  O OD1 . ASP   A 36  ? 0.5433 0.6974 0.5391 0.0824  -0.0264 -0.0255 79  ASP   A OD1 
284  O OD2 . ASP   A 36  ? 0.5412 0.7836 0.6148 0.0807  -0.0422 -0.0453 79  ASP   A OD2 
285  N N   . GLU   A 37  ? 0.5701 0.6586 0.4307 0.1238  -0.0619 -0.0287 80  GLU   A N   
286  C CA  . GLU   A 37  ? 0.5919 0.6448 0.4208 0.1123  -0.0574 -0.0302 80  GLU   A CA  
287  C C   . GLU   A 37  ? 0.5773 0.6277 0.4404 0.0860  -0.0416 -0.0334 80  GLU   A C   
288  O O   . GLU   A 37  ? 0.5991 0.6163 0.4382 0.0782  -0.0300 -0.0285 80  GLU   A O   
289  C CB  . GLU   A 37  ? 0.6270 0.6884 0.4328 0.1218  -0.0792 -0.0461 80  GLU   A CB  
290  C CG  . GLU   A 37  ? 0.7377 0.7597 0.4945 0.1183  -0.0739 -0.0446 80  GLU   A CG  
291  C CD  . GLU   A 37  ? 0.8095 0.8371 0.5330 0.1324  -0.0951 -0.0592 80  GLU   A CD  
292  O OE1 . GLU   A 37  ? 0.7838 0.8312 0.5297 0.1220  -0.1044 -0.0804 80  GLU   A OE1 
293  O OE2 . GLU   A 37  ? 0.8854 0.8952 0.5581 0.1551  -0.1033 -0.0499 80  GLU   A OE2 
294  N N   . SER   A 38  ? 0.5398 0.6238 0.4586 0.0731  -0.0395 -0.0402 81  SER   A N   
295  C CA  . SER   A 38  ? 0.5410 0.6160 0.4894 0.0501  -0.0240 -0.0407 81  SER   A CA  
296  C C   . SER   A 38  ? 0.5383 0.5945 0.4871 0.0485  -0.0021 -0.0210 81  SER   A C   
297  O O   . SER   A 38  ? 0.5408 0.5880 0.5116 0.0331  0.0112  -0.0188 81  SER   A O   
298  C CB  . SER   A 38  ? 0.5389 0.6519 0.5464 0.0341  -0.0286 -0.0540 81  SER   A CB  
299  O OG  . SER   A 38  ? 0.5929 0.7241 0.6022 0.0350  -0.0516 -0.0764 81  SER   A OG  
300  N N   . GLY   A 39  ? 0.5331 0.5810 0.4560 0.0657  0.0003  -0.0080 82  GLY   A N   
301  C CA  . GLY   A 39  ? 0.5419 0.5730 0.4617 0.0672  0.0176  0.0075  82  GLY   A CA  
302  C C   . GLY   A 39  ? 0.5260 0.5865 0.4851 0.0665  0.0281  0.0142  82  GLY   A C   
303  O O   . GLY   A 39  ? 0.5312 0.5795 0.4901 0.0666  0.0434  0.0259  82  GLY   A O   
304  N N   . ASP   A 40  ? 0.5024 0.6050 0.4942 0.0679  0.0199  0.0069  83  ASP   A N   
305  C CA  . ASP   A 40  ? 0.4934 0.6325 0.5262 0.0671  0.0320  0.0135  83  ASP   A CA  
306  C C   . ASP   A 40  ? 0.5017 0.6605 0.5231 0.0935  0.0278  0.0184  83  ASP   A C   
307  O O   . ASP   A 40  ? 0.5019 0.6738 0.5119 0.1085  0.0092  0.0096  83  ASP   A O   
308  C CB  . ASP   A 40  ? 0.4922 0.6733 0.5801 0.0486  0.0275  0.0005  83  ASP   A CB  
309  C CG  . ASP   A 40  ? 0.5777 0.7378 0.6837 0.0217  0.0340  -0.0043 83  ASP   A CG  
310  O OD1 . ASP   A 40  ? 0.6171 0.7364 0.6990 0.0185  0.0464  0.0058  83  ASP   A OD1 
311  O OD2 . ASP   A 40  ? 0.6064 0.7908 0.7509 0.0050  0.0251  -0.0197 83  ASP   A OD2 
312  N N   . PHE   A 41  ? 0.5022 0.6625 0.5245 0.1017  0.0446  0.0319  84  PHE   A N   
313  C CA  . PHE   A 41  ? 0.5053 0.6850 0.5187 0.1287  0.0433  0.0360  84  PHE   A CA  
314  C C   . PHE   A 41  ? 0.5089 0.7532 0.5763 0.1285  0.0475  0.0324  84  PHE   A C   
315  O O   . PHE   A 41  ? 0.4944 0.7614 0.6056 0.1054  0.0619  0.0345  84  PHE   A O   
316  C CB  . PHE   A 41  ? 0.4922 0.6467 0.4813 0.1391  0.0595  0.0498  84  PHE   A CB  
317  C CG  . PHE   A 41  ? 0.5088 0.6085 0.4460 0.1465  0.0519  0.0510  84  PHE   A CG  
318  C CD1 . PHE   A 41  ? 0.5198 0.6025 0.4226 0.1680  0.0367  0.0477  84  PHE   A CD1 
319  C CD2 . PHE   A 41  ? 0.5220 0.5870 0.4462 0.1323  0.0603  0.0553  84  PHE   A CD2 
320  C CE1 . PHE   A 41  ? 0.5559 0.5873 0.4155 0.1707  0.0318  0.0493  84  PHE   A CE1 
321  C CE2 . PHE   A 41  ? 0.5490 0.5706 0.4330 0.1370  0.0543  0.0551  84  PHE   A CE2 
322  C CZ  . PHE   A 41  ? 0.5582 0.5629 0.4117 0.1540  0.0410  0.0524  84  PHE   A CZ  
323  N N   . SER   A 42  ? 0.5233 0.7975 0.5893 0.1542  0.0355  0.0269  85  SER   A N   
324  C CA  . SER   A 42  ? 0.5117 0.8564 0.6321 0.1579  0.0396  0.0222  85  SER   A CA  
325  C C   . SER   A 42  ? 0.5517 0.9131 0.6536 0.1950  0.0387  0.0251  85  SER   A C   
326  O O   . SER   A 42  ? 0.5830 0.9026 0.6317 0.2182  0.0244  0.0247  85  SER   A O   
327  C CB  . SER   A 42  ? 0.5065 0.8887 0.6593 0.1505  0.0176  0.0030  85  SER   A CB  
328  O OG  . SER   A 42  ? 0.5448 0.9080 0.6543 0.1755  -0.0088 -0.0057 85  SER   A OG  
329  N N   . LEU   A 43  ? 0.5496 0.9703 0.6948 0.2009  0.0552  0.0282  86  LEU   A N   
330  C CA  . LEU   A 43  ? 0.5861 1.0277 0.7153 0.2397  0.0548  0.0288  86  LEU   A CA  
331  C C   . LEU   A 43  ? 0.6040 1.0820 0.7418 0.2636  0.0283  0.0121  86  LEU   A C   
332  O O   . LEU   A 43  ? 0.5699 1.1021 0.7605 0.2496  0.0209  0.0002  86  LEU   A O   
333  C CB  . LEU   A 43  ? 0.5626 1.0606 0.7341 0.2406  0.0844  0.0384  86  LEU   A CB  
334  C CG  . LEU   A 43  ? 0.6119 1.0753 0.7622 0.2317  0.1120  0.0574  86  LEU   A CG  
335  C CD1 . LEU   A 43  ? 0.5915 1.1150 0.7776 0.2393  0.1416  0.0676  86  LEU   A CD1 
336  C CD2 . LEU   A 43  ? 0.6726 1.0702 0.7507 0.2573  0.1034  0.0604  86  LEU   A CD2 
337  N N   . VAL   A 44  ? 0.6567 1.1051 0.7432 0.3009  0.0132  0.0102  87  VAL   A N   
338  C CA  . VAL   A 44  ? 0.6788 1.1562 0.7638 0.3323  -0.0128 -0.0041 87  VAL   A CA  
339  C C   . VAL   A 44  ? 0.6908 1.2228 0.7953 0.3655  -0.0027 -0.0053 87  VAL   A C   
340  O O   . VAL   A 44  ? 0.7179 1.2191 0.7880 0.3821  0.0107  0.0041  87  VAL   A O   
341  C CB  . VAL   A 44  ? 0.7366 1.1358 0.7458 0.3538  -0.0362 -0.0039 87  VAL   A CB  
342  C CG1 . VAL   A 44  ? 0.7399 1.1620 0.7371 0.3959  -0.0618 -0.0158 87  VAL   A CG1 
343  C CG2 . VAL   A 44  ? 0.7607 1.1134 0.7509 0.3235  -0.0448 -0.0032 87  VAL   A CG2 
344  N N   . GLU   A 45  ? 0.6691 1.2851 0.8302 0.3757  -0.0087 -0.0183 88  GLU   A N   
345  C CA  . GLU   A 45  ? 0.6730 1.3499 0.8562 0.4101  0.0018  -0.0210 88  GLU   A CA  
346  C C   . GLU   A 45  ? 0.6709 1.3890 0.8577 0.4517  -0.0273 -0.0391 88  GLU   A C   
347  O O   . GLU   A 45  ? 0.7055 1.3818 0.8535 0.4626  -0.0573 -0.0461 88  GLU   A O   
348  C CB  . GLU   A 45  ? 0.6701 1.4262 0.9302 0.3837  0.0347  -0.0159 88  GLU   A CB  
349  C CG  . GLU   A 45  ? 0.7646 1.4778 1.0137 0.3509  0.0651  0.0044  88  GLU   A CG  
350  C CD  . GLU   A 45  ? 0.8700 1.5995 1.1110 0.3708  0.0951  0.0171  88  GLU   A CD  
351  O OE1 . GLU   A 45  ? 0.8959 1.6312 1.1070 0.4165  0.0874  0.0111  88  GLU   A OE1 
352  O OE2 . GLU   A 45  ? 0.9053 1.6394 1.1664 0.3428  0.1262  0.0331  88  GLU   A OE2 
353  N N   . GLY   B 7   ? 0.7579 0.7284 0.7305 0.2002  0.0561  -0.0646 16  GLY   B N   
354  C CA  . GLY   B 7   ? 0.7744 0.7238 0.7379 0.2056  0.0534  -0.0581 16  GLY   B CA  
355  C C   . GLY   B 7   ? 0.7708 0.7270 0.7379 0.2050  0.0486  -0.0552 16  GLY   B C   
356  O O   . GLY   B 7   ? 0.7744 0.7516 0.7522 0.2041  0.0452  -0.0600 16  GLY   B O   
357  N N   . GLU   B 8   ? 0.7564 0.6955 0.7144 0.2058  0.0476  -0.0473 17  GLU   B N   
358  C CA  . GLU   B 8   ? 0.7377 0.6802 0.6955 0.2076  0.0417  -0.0452 17  GLU   B CA  
359  C C   . GLU   B 8   ? 0.7118 0.6614 0.6740 0.1931  0.0405  -0.0433 17  GLU   B C   
360  O O   . GLU   B 8   ? 0.7253 0.6663 0.6830 0.1845  0.0445  -0.0379 17  GLU   B O   
361  C CB  . GLU   B 8   ? 0.7767 0.7007 0.7214 0.2181  0.0409  -0.0376 17  GLU   B CB  
362  C CG  . GLU   B 8   ? 0.8337 0.7613 0.7761 0.2267  0.0330  -0.0385 17  GLU   B CG  
363  C CD  . GLU   B 8   ? 0.9285 0.8408 0.8567 0.2406  0.0323  -0.0315 17  GLU   B CD  
364  O OE1 . GLU   B 8   ? 0.9382 0.8373 0.8591 0.2401  0.0387  -0.0232 17  GLU   B OE1 
365  O OE2 . GLU   B 8   ? 0.9525 0.8667 0.8769 0.2523  0.0252  -0.0339 17  GLU   B OE2 
366  N N   A THR   B 9   ? 0.6972 0.6620 0.6683 0.1901  0.0343  -0.0476 18  THR   B N   
367  N N   B THR   B 9   ? 0.6940 0.6589 0.6652 0.1900  0.0343  -0.0476 18  THR   B N   
368  N N   C THR   B 9   ? 0.6972 0.6620 0.6683 0.1901  0.0343  -0.0476 18  THR   B N   
369  N N   D THR   B 9   ? 0.6940 0.6589 0.6652 0.1900  0.0343  -0.0476 18  THR   B N   
370  C CA  A THR   B 9   ? 0.6935 0.6629 0.6679 0.1761  0.0316  -0.0457 18  THR   B CA  
371  C CA  B THR   B 9   ? 0.6873 0.6566 0.6616 0.1762  0.0315  -0.0457 18  THR   B CA  
372  C CA  C THR   B 9   ? 0.6935 0.6629 0.6679 0.1761  0.0316  -0.0457 18  THR   B CA  
373  C CA  D THR   B 9   ? 0.6873 0.6566 0.6616 0.1762  0.0315  -0.0457 18  THR   B CA  
374  C C   A THR   B 9   ? 0.6871 0.6519 0.6573 0.1797  0.0212  -0.0450 18  THR   B C   
375  C C   B THR   B 9   ? 0.6842 0.6487 0.6542 0.1798  0.0213  -0.0449 18  THR   B C   
376  C C   C THR   B 9   ? 0.6871 0.6519 0.6573 0.1797  0.0212  -0.0450 18  THR   B C   
377  C C   D THR   B 9   ? 0.6842 0.6487 0.6542 0.1798  0.0213  -0.0449 18  THR   B C   
378  O O   A THR   B 9   ? 0.6882 0.6552 0.6607 0.1690  0.0162  -0.0443 18  THR   B O   
379  O O   B THR   B 9   ? 0.6853 0.6517 0.6574 0.1690  0.0165  -0.0441 18  THR   B O   
380  O O   C THR   B 9   ? 0.6882 0.6552 0.6607 0.1690  0.0162  -0.0443 18  THR   B O   
381  O O   D THR   B 9   ? 0.6853 0.6517 0.6574 0.1690  0.0165  -0.0441 18  THR   B O   
382  C CB  A THR   B 9   ? 0.7035 0.6947 0.6927 0.1640  0.0334  -0.0498 18  THR   B CB  
383  C CB  B THR   B 9   ? 0.6890 0.6803 0.6783 0.1648  0.0327  -0.0500 18  THR   B CB  
384  C CB  C THR   B 9   ? 0.7035 0.6947 0.6927 0.1640  0.0334  -0.0498 18  THR   B CB  
385  C CB  D THR   B 9   ? 0.6890 0.6803 0.6783 0.1648  0.0327  -0.0500 18  THR   B CB  
386  O OG1 A THR   B 9   ? 0.7159 0.7159 0.7094 0.1687  0.0399  -0.0540 18  THR   B OG1 
387  O OG1 B THR   B 9   ? 0.6894 0.6973 0.6891 0.1718  0.0279  -0.0559 18  THR   B OG1 
388  O OG1 C THR   B 9   ? 0.7159 0.7159 0.7094 0.1687  0.0399  -0.0540 18  THR   B OG1 
389  O OG1 D THR   B 9   ? 0.6894 0.6973 0.6891 0.1718  0.0279  -0.0559 18  THR   B OG1 
390  C CG2 A THR   B 9   ? 0.7107 0.7006 0.6990 0.1483  0.0362  -0.0458 18  THR   B CG2 
391  C CG2 B THR   B 9   ? 0.6926 0.6871 0.6829 0.1604  0.0423  -0.0506 18  THR   B CG2 
392  C CG2 C THR   B 9   ? 0.7107 0.7006 0.6990 0.1483  0.0362  -0.0458 18  THR   B CG2 
393  C CG2 D THR   B 9   ? 0.6926 0.6871 0.6829 0.1604  0.0423  -0.0506 18  THR   B CG2 
394  N N   . THR   B 10  ? 0.6797 0.6363 0.6421 0.1954  0.0171  -0.0452 19  THR   B N   
395  C CA  . THR   B 10  ? 0.6462 0.5965 0.6018 0.2021  0.0063  -0.0456 19  THR   B CA  
396  C C   . THR   B 10  ? 0.6152 0.5510 0.5577 0.1992  0.0061  -0.0391 19  THR   B C   
397  O O   . THR   B 10  ? 0.6243 0.5520 0.5595 0.1996  0.0148  -0.0329 19  THR   B O   
398  C CB  . THR   B 10  ? 0.6712 0.6140 0.6174 0.2224  0.0044  -0.0458 19  THR   B CB  
399  O OG1 . THR   B 10  ? 0.6867 0.6401 0.6419 0.2277  0.0070  -0.0509 19  THR   B OG1 
400  C CG2 . THR   B 10  ? 0.6819 0.6205 0.6214 0.2325  -0.0085 -0.0486 19  THR   B CG2 
401  N N   A ASP   B 11  ? 0.6089 0.5410 0.5479 0.1964  -0.0045 -0.0404 20  ASP   B N   
402  N N   B ASP   B 11  ? 0.6089 0.5410 0.5479 0.1964  -0.0045 -0.0404 20  ASP   B N   
403  N N   C ASP   B 11  ? 0.6088 0.5409 0.5477 0.1964  -0.0045 -0.0404 20  ASP   B N   
404  N N   D ASP   B 11  ? 0.6088 0.5409 0.5477 0.1964  -0.0045 -0.0404 20  ASP   B N   
405  C CA  A ASP   B 11  ? 0.6188 0.5369 0.5430 0.1965  -0.0068 -0.0354 20  ASP   B CA  
406  C CA  B ASP   B 11  ? 0.6188 0.5369 0.5430 0.1965  -0.0068 -0.0354 20  ASP   B CA  
407  C CA  C ASP   B 11  ? 0.6186 0.5366 0.5427 0.1966  -0.0069 -0.0354 20  ASP   B CA  
408  C CA  D ASP   B 11  ? 0.6186 0.5366 0.5427 0.1966  -0.0069 -0.0354 20  ASP   B CA  
409  C C   A ASP   B 11  ? 0.6267 0.5342 0.5349 0.2140  -0.0036 -0.0299 20  ASP   B C   
410  C C   B ASP   B 11  ? 0.6267 0.5342 0.5349 0.2140  -0.0036 -0.0299 20  ASP   B C   
411  C C   C ASP   B 11  ? 0.6266 0.5341 0.5347 0.2140  -0.0035 -0.0299 20  ASP   B C   
412  C C   D ASP   B 11  ? 0.6266 0.5341 0.5347 0.2140  -0.0035 -0.0299 20  ASP   B C   
413  O O   A ASP   B 11  ? 0.6289 0.5360 0.5342 0.2282  -0.0058 -0.0315 20  ASP   B O   
414  O O   B ASP   B 11  ? 0.6290 0.5360 0.5342 0.2282  -0.0058 -0.0315 20  ASP   B O   
415  O O   C ASP   B 11  ? 0.6288 0.5358 0.5340 0.2282  -0.0057 -0.0315 20  ASP   B O   
416  O O   D ASP   B 11  ? 0.6288 0.5358 0.5340 0.2282  -0.0057 -0.0315 20  ASP   B O   
417  C CB  A ASP   B 11  ? 0.6424 0.5548 0.5629 0.1950  -0.0222 -0.0394 20  ASP   B CB  
418  C CB  B ASP   B 11  ? 0.6424 0.5548 0.5629 0.1950  -0.0222 -0.0394 20  ASP   B CB  
419  C CB  C ASP   B 11  ? 0.6418 0.5541 0.5621 0.1954  -0.0222 -0.0394 20  ASP   B CB  
420  C CB  D ASP   B 11  ? 0.6418 0.5541 0.5621 0.1954  -0.0222 -0.0394 20  ASP   B CB  
421  C CG  A ASP   B 11  ? 0.6865 0.6082 0.6218 0.1756  -0.0262 -0.0423 20  ASP   B CG  
422  C CG  B ASP   B 11  ? 0.6865 0.6082 0.6218 0.1756  -0.0262 -0.0423 20  ASP   B CG  
423  C CG  C ASP   B 11  ? 0.6885 0.6048 0.6181 0.1755  -0.0254 -0.0403 20  ASP   B CG  
424  C CG  D ASP   B 11  ? 0.6885 0.6048 0.6181 0.1755  -0.0254 -0.0403 20  ASP   B CG  
425  O OD1 A ASP   B 11  ? 0.6819 0.6142 0.6277 0.1633  -0.0159 -0.0405 20  ASP   B OD1 
426  O OD1 B ASP   B 11  ? 0.6819 0.6142 0.6277 0.1633  -0.0159 -0.0405 20  ASP   B OD1 
427  O OD1 C ASP   B 11  ? 0.6812 0.6117 0.6254 0.1631  -0.0168 -0.0402 20  ASP   B OD1 
428  O OD1 D ASP   B 11  ? 0.6812 0.6117 0.6254 0.1631  -0.0168 -0.0402 20  ASP   B OD1 
429  O OD2 A ASP   B 11  ? 0.7136 0.6314 0.6493 0.1729  -0.0402 -0.0459 20  ASP   B OD2 
430  O OD2 B ASP   B 11  ? 0.7137 0.6314 0.6493 0.1729  -0.0402 -0.0459 20  ASP   B OD2 
431  O OD2 C ASP   B 11  ? 0.7197 0.6242 0.6406 0.1731  -0.0369 -0.0409 20  ASP   B OD2 
432  O OD2 D ASP   B 11  ? 0.7197 0.6242 0.6406 0.1731  -0.0369 -0.0409 20  ASP   B OD2 
433  N N   . GLY   B 12  ? 0.6267 0.5274 0.5249 0.2130  0.0018  -0.0229 21  GLY   B N   
434  C CA  . GLY   B 12  ? 0.6159 0.5103 0.5001 0.2283  0.0061  -0.0154 21  GLY   B CA  
435  C C   . GLY   B 12  ? 0.5904 0.4846 0.4727 0.2219  0.0169  -0.0067 21  GLY   B C   
436  O O   . GLY   B 12  ? 0.5690 0.4663 0.4591 0.2063  0.0202  -0.0073 21  GLY   B O   
437  N N   . VAL   B 13  ? 0.5771 0.4691 0.4490 0.2344  0.0220  0.0020  22  VAL   B N   
438  C CA  . VAL   B 13  ? 0.5649 0.4590 0.4362 0.2294  0.0320  0.0119  22  VAL   B CA  
439  C C   . VAL   B 13  ? 0.5587 0.4532 0.4391 0.2261  0.0411  0.0161  22  VAL   B C   
440  O O   . VAL   B 13  ? 0.5726 0.4645 0.4521 0.2361  0.0405  0.0151  22  VAL   B O   
441  C CB  . VAL   B 13  ? 0.5731 0.4673 0.4281 0.2443  0.0318  0.0203  22  VAL   B CB  
442  C CG1 . VAL   B 13  ? 0.5880 0.4810 0.4341 0.2631  0.0325  0.0249  22  VAL   B CG1 
443  C CG2 . VAL   B 13  ? 0.5634 0.4636 0.4197 0.2372  0.0407  0.0302  22  VAL   B CG2 
444  N N   . TYR   B 14  ? 0.5381 0.4344 0.4267 0.2122  0.0482  0.0197  23  TYR   B N   
445  C CA  . TYR   B 14  ? 0.5469 0.4399 0.4434 0.2072  0.0549  0.0226  23  TYR   B CA  
446  C C   . TYR   B 14  ? 0.5475 0.4411 0.4451 0.2010  0.0624  0.0342  23  TYR   B C   
447  O O   . TYR   B 14  ? 0.5517 0.4506 0.4486 0.1947  0.0631  0.0368  23  TYR   B O   
448  C CB  . TYR   B 14  ? 0.5457 0.4397 0.4539 0.1943  0.0546  0.0127  23  TYR   B CB  
449  C CG  . TYR   B 14  ? 0.5456 0.4423 0.4575 0.1988  0.0488  0.0022  23  TYR   B CG  
450  C CD1 . TYR   B 14  ? 0.5539 0.4552 0.4641 0.2005  0.0409  -0.0035 23  TYR   B CD1 
451  C CD2 . TYR   B 14  ? 0.5592 0.4545 0.4771 0.2001  0.0504  -0.0023 23  TYR   B CD2 
452  C CE1 . TYR   B 14  ? 0.5613 0.4680 0.4779 0.2024  0.0350  -0.0126 23  TYR   B CE1 
453  C CE2 . TYR   B 14  ? 0.5705 0.4723 0.4934 0.2045  0.0452  -0.0118 23  TYR   B CE2 
454  C CZ  . TYR   B 14  ? 0.5835 0.4924 0.5071 0.2047  0.0377  -0.0166 23  TYR   B CZ  
455  O OH  . TYR   B 14  ? 0.6110 0.5291 0.5422 0.2074  0.0319  -0.0253 23  TYR   B OH  
456  N N   . ARG   B 15  ? 0.5460 0.4336 0.4459 0.2016  0.0672  0.0409  24  ARG   B N   
457  C CA  . ARG   B 15  ? 0.5448 0.4326 0.4489 0.1927  0.0734  0.0523  24  ARG   B CA  
458  C C   . ARG   B 15  ? 0.5478 0.4306 0.4621 0.1769  0.0739  0.0460  24  ARG   B C   
459  O O   . ARG   B 15  ? 0.5449 0.4216 0.4619 0.1765  0.0715  0.0364  24  ARG   B O   
460  C CB  . ARG   B 15  ? 0.5434 0.4240 0.4449 0.1993  0.0773  0.0636  24  ARG   B CB  
461  C CG  . ARG   B 15  ? 0.5680 0.4539 0.4577 0.2172  0.0779  0.0715  24  ARG   B CG  
462  C CD  . ARG   B 15  ? 0.5967 0.4733 0.4838 0.2227  0.0819  0.0824  24  ARG   B CD  
463  N NE  . ARG   B 15  ? 0.6136 0.4927 0.4874 0.2425  0.0814  0.0868  24  ARG   B NE  
464  C CZ  . ARG   B 15  ? 0.6331 0.5234 0.4992 0.2518  0.0855  0.0998  24  ARG   B CZ  
465  N NH1 . ARG   B 15  ? 0.6121 0.5142 0.4840 0.2424  0.0907  0.1102  24  ARG   B NH1 
466  N NH2 . ARG   B 15  ? 0.6556 0.5472 0.5078 0.2717  0.0843  0.1022  24  ARG   B NH2 
467  N N   . VAL   B 16  ? 0.5452 0.4315 0.4647 0.1652  0.0766  0.0515  25  VAL   B N   
468  C CA  . VAL   B 16  ? 0.5510 0.4320 0.4786 0.1509  0.0766  0.0466  25  VAL   B CA  
469  C C   . VAL   B 16  ? 0.5594 0.4323 0.4914 0.1452  0.0794  0.0577  25  VAL   B C   
470  O O   . VAL   B 16  ? 0.5630 0.4435 0.4971 0.1422  0.0824  0.0699  25  VAL   B O   
471  C CB  . VAL   B 16  ? 0.5657 0.4564 0.4956 0.1414  0.0762  0.0439  25  VAL   B CB  
472  C CG1 . VAL   B 16  ? 0.5690 0.4534 0.5056 0.1284  0.0756  0.0375  25  VAL   B CG1 
473  C CG2 . VAL   B 16  ? 0.5706 0.4676 0.4948 0.1466  0.0726  0.0355  25  VAL   B CG2 
474  N N   . MET   B 17  ? 0.5747 0.4322 0.5077 0.1443  0.0777  0.0540  26  MET   B N   
475  C CA  . MET   B 17  ? 0.5956 0.4398 0.5313 0.1392  0.0784  0.0641  26  MET   B CA  
476  C C   . MET   B 17  ? 0.6368 0.4690 0.5782 0.1259  0.0750  0.0585  26  MET   B C   
477  O O   . MET   B 17  ? 0.6358 0.4670 0.5769 0.1246  0.0724  0.0447  26  MET   B O   
478  C CB  . MET   B 17  ? 0.5931 0.4234 0.5219 0.1511  0.0773  0.0638  26  MET   B CB  
479  C CG  . MET   B 17  ? 0.6223 0.4621 0.5434 0.1669  0.0790  0.0659  26  MET   B CG  
480  S SD  . MET   B 17  ? 0.6512 0.5024 0.5703 0.1702  0.0848  0.0866  26  MET   B SD  
481  C CE  . MET   B 17  ? 0.6067 0.4374 0.5273 0.1649  0.0857  0.0999  26  MET   B CE  
482  N N   . THR   B 18  ? 0.6679 0.4896 0.6139 0.1168  0.0743  0.0694  27  THR   B N   
483  C CA  . THR   B 18  ? 0.7095 0.5149 0.6594 0.1051  0.0690  0.0645  27  THR   B CA  
484  C C   . THR   B 18  ? 0.7507 0.5328 0.6995 0.1027  0.0659  0.0740  27  THR   B C   
485  O O   . THR   B 18  ? 0.7447 0.5297 0.6951 0.1032  0.0695  0.0900  27  THR   B O   
486  C CB  . THR   B 18  ? 0.7246 0.5419 0.6834 0.0912  0.0689  0.0672  27  THR   B CB  
487  O OG1 . THR   B 18  ? 0.7546 0.5543 0.7154 0.0813  0.0621  0.0602  27  THR   B OG1 
488  C CG2 . THR   B 18  ? 0.7139 0.5436 0.6805 0.0852  0.0726  0.0862  27  THR   B CG2 
489  N N   . ARG   B 19  ? 0.7872 0.5457 0.7322 0.1007  0.0589  0.0644  28  ARG   B N   
490  C CA  . ARG   B 19  ? 0.8302 0.5613 0.7728 0.0969  0.0536  0.0725  28  ARG   B CA  
491  C C   . ARG   B 19  ? 0.8583 0.5752 0.8081 0.0794  0.0462  0.0745  28  ARG   B C   
492  O O   . ARG   B 19  ? 0.8711 0.5603 0.8182 0.0746  0.0391  0.0792  28  ARG   B O   
493  C CB  . ARG   B 19  ? 0.8718 0.5813 0.8015 0.1107  0.0494  0.0617  28  ARG   B CB  
494  C CG  . ARG   B 19  ? 0.9343 0.6458 0.8574 0.1244  0.0542  0.0694  28  ARG   B CG  
495  C CD  . ARG   B 19  ? 1.0000 0.6934 0.9106 0.1393  0.0497  0.0572  28  ARG   B CD  
496  N NE  . ARG   B 19  ? 1.0573 0.7607 0.9620 0.1552  0.0545  0.0588  28  ARG   B NE  
497  C CZ  . ARG   B 19  ? 1.1039 0.8154 1.0035 0.1693  0.0543  0.0443  28  ARG   B CZ  
498  N NH1 . ARG   B 19  ? 1.1126 0.8253 1.0124 0.1697  0.0508  0.0280  28  ARG   B NH1 
499  N NH2 . ARG   B 19  ? 1.1014 0.8212 0.9960 0.1833  0.0573  0.0464  28  ARG   B NH2 
500  N N   . ARG   B 20  ? 0.8704 0.6050 0.8287 0.0701  0.0470  0.0714  29  ARG   B N   
501  C CA  . ARG   B 20  ? 0.8966 0.6219 0.8624 0.0538  0.0395  0.0717  29  ARG   B CA  
502  C C   . ARG   B 20  ? 0.9016 0.6271 0.8793 0.0400  0.0392  0.0930  29  ARG   B C   
503  O O   . ARG   B 20  ? 0.9168 0.6194 0.8979 0.0277  0.0299  0.0966  29  ARG   B O   
504  C CB  . ARG   B 20  ? 0.9195 0.6677 0.8900 0.0502  0.0416  0.0628  29  ARG   B CB  
505  C CG  . ARG   B 20  ? 0.9846 0.7278 0.9638 0.0339  0.0339  0.0630  29  ARG   B CG  
506  C CD  . ARG   B 20  ? 1.0352 0.8013 1.0172 0.0320  0.0366  0.0549  29  ARG   B CD  
507  N NE  . ARG   B 20  ? 1.0790 0.8754 1.0684 0.0320  0.0457  0.0663  29  ARG   B NE  
508  C CZ  . ARG   B 20  ? 1.1119 0.9249 1.1136 0.0206  0.0459  0.0766  29  ARG   B CZ  
509  N NH1 . ARG   B 20  ? 1.1144 0.9165 1.1241 0.0064  0.0371  0.0776  29  ARG   B NH1 
510  N NH2 . ARG   B 20  ? 1.1012 0.9419 1.1069 0.0240  0.0540  0.0858  29  ARG   B NH2 
511  N N   . LEU   B 21  ? 0.8841 0.6350 0.8674 0.0425  0.0489  0.1074  30  LEU   B N   
512  C CA  . LEU   B 21  ? 0.8741 0.6336 0.8698 0.0310  0.0514  0.1300  30  LEU   B CA  
513  C C   . LEU   B 21  ? 0.8707 0.6100 0.8603 0.0353  0.0517  0.1427  30  LEU   B C   
514  O O   . LEU   B 21  ? 0.8861 0.5991 0.8622 0.0449  0.0471  0.1319  30  LEU   B O   
515  C CB  . LEU   B 21  ? 0.8675 0.6665 0.8694 0.0351  0.0620  0.1382  30  LEU   B CB  
516  C CG  . LEU   B 21  ? 0.8810 0.7037 0.8953 0.0241  0.0618  0.1380  30  LEU   B CG  
517  C CD1 . LEU   B 21  ? 0.8974 0.7034 0.9122 0.0150  0.0518  0.1216  30  LEU   B CD1 
518  C CD2 . LEU   B 21  ? 0.8821 0.7341 0.8923 0.0364  0.0701  0.1342  30  LEU   B CD2 
519  N N   . LEU   B 22  ? 0.8481 0.5996 0.8468 0.0287  0.0569  0.1658  31  LEU   B N   
520  C CA  . LEU   B 22  ? 0.8449 0.5786 0.8373 0.0325  0.0580  0.1802  31  LEU   B CA  
521  C C   . LEU   B 22  ? 0.8325 0.5711 0.8091 0.0558  0.0651  0.1735  31  LEU   B C   
522  O O   . LEU   B 22  ? 0.8274 0.5955 0.8040 0.0653  0.0730  0.1711  31  LEU   B O   
523  C CB  . LEU   B 22  ? 0.8371 0.5922 0.8442 0.0211  0.0644  0.2075  31  LEU   B CB  
524  C CG  . LEU   B 22  ? 0.8602 0.5969 0.8632 0.0204  0.0652  0.2269  31  LEU   B CG  
525  C CD1 . LEU   B 22  ? 0.8749 0.5708 0.8798 0.0036  0.0514  0.2285  31  LEU   B CD1 
526  C CD2 . LEU   B 22  ? 0.8526 0.6231 0.8684 0.0153  0.0759  0.2537  31  LEU   B CD2 
527  N N   . GLY   B 23  ? 0.8258 0.5345 0.7883 0.0654  0.0610  0.1691  32  GLY   B N   
528  C CA  . GLY   B 23  ? 0.8129 0.5240 0.7605 0.0876  0.0658  0.1612  32  GLY   B CA  
529  C C   . GLY   B 23  ? 0.7910 0.5212 0.7360 0.0980  0.0678  0.1410  32  GLY   B C   
530  O O   . GLY   B 23  ? 0.7858 0.5143 0.7348 0.0909  0.0628  0.1269  32  GLY   B O   
531  N N   . SER   B 24  ? 0.7714 0.5191 0.7091 0.1149  0.0746  0.1399  33  SER   B N   
532  C CA  . SER   B 24  ? 0.7566 0.5233 0.6923 0.1239  0.0763  0.1231  33  SER   B CA  
533  C C   . SER   B 24  ? 0.7238 0.5216 0.6665 0.1223  0.0835  0.1333  33  SER   B C   
534  O O   . SER   B 24  ? 0.7202 0.5289 0.6602 0.1296  0.0894  0.1482  33  SER   B O   
535  C CB  . SER   B 24  ? 0.7834 0.5474 0.7061 0.1440  0.0770  0.1144  33  SER   B CB  
536  O OG  . SER   B 24  ? 0.8343 0.5755 0.7506 0.1479  0.0702  0.0997  33  SER   B OG  
537  N N   . THR   B 25  ? 0.6990 0.5112 0.6495 0.1138  0.0828  0.1258  34  THR   B N   
538  C CA  . THR   B 25  ? 0.6731 0.5144 0.6294 0.1125  0.0885  0.1343  34  THR   B CA  
539  C C   . THR   B 25  ? 0.6552 0.5113 0.6057 0.1226  0.0891  0.1200  34  THR   B C   
540  O O   . THR   B 25  ? 0.6482 0.4972 0.5981 0.1201  0.0847  0.1035  34  THR   B O   
541  C CB  . THR   B 25  ? 0.6772 0.5240 0.6481 0.0930  0.0866  0.1404  34  THR   B CB  
542  O OG1 . THR   B 25  ? 0.6956 0.5250 0.6725 0.0816  0.0840  0.1534  34  THR   B OG1 
543  C CG2 . THR   B 25  ? 0.6604 0.5395 0.6378 0.0923  0.0926  0.1508  34  THR   B CG2 
544  N N   . GLN   B 26  ? 0.6386 0.5150 0.5842 0.1340  0.0941  0.1266  35  GLN   B N   
545  C CA  . GLN   B 26  ? 0.6269 0.5152 0.5663 0.1428  0.0931  0.1140  35  GLN   B CA  
546  C C   . GLN   B 26  ? 0.6273 0.5320 0.5735 0.1333  0.0934  0.1136  35  GLN   B C   
547  O O   . GLN   B 26  ? 0.6280 0.5513 0.5773 0.1333  0.0976  0.1269  35  GLN   B O   
548  C CB  . GLN   B 26  ? 0.6134 0.5118 0.5409 0.1620  0.0959  0.1182  35  GLN   B CB  
549  C CG  . GLN   B 26  ? 0.6066 0.5122 0.5265 0.1706  0.0924  0.1043  35  GLN   B CG  
550  C CD  . GLN   B 26  ? 0.6181 0.5303 0.5247 0.1905  0.0929  0.1069  35  GLN   B CD  
551  O OE1 . GLN   B 26  ? 0.6326 0.5355 0.5332 0.2004  0.0929  0.1086  35  GLN   B OE1 
552  N NE2 . GLN   B 26  ? 0.5949 0.5215 0.4949 0.1981  0.0921  0.1061  35  GLN   B NE2 
553  N N   . VAL   B 27  ? 0.6154 0.5149 0.5634 0.1261  0.0890  0.0986  36  VAL   B N   
554  C CA  . VAL   B 27  ? 0.5995 0.5127 0.5522 0.1178  0.0886  0.0969  36  VAL   B CA  
555  C C   . VAL   B 27  ? 0.5797 0.5052 0.5226 0.1286  0.0882  0.0907  36  VAL   B C   
556  O O   . VAL   B 27  ? 0.5765 0.5158 0.5203 0.1258  0.0885  0.0923  36  VAL   B O   
557  C CB  . VAL   B 27  ? 0.6130 0.5147 0.5720 0.1037  0.0842  0.0861  36  VAL   B CB  
558  C CG1 . VAL   B 27  ? 0.6254 0.5170 0.5946 0.0911  0.0830  0.0948  36  VAL   B CG1 
559  C CG2 . VAL   B 27  ? 0.6173 0.5044 0.5701 0.1080  0.0809  0.0705  36  VAL   B CG2 
560  N N   . GLY   B 28  ? 0.5632 0.4831 0.4963 0.1411  0.0866  0.0838  37  GLY   B N   
561  C CA  . GLY   B 28  ? 0.5471 0.4746 0.4698 0.1514  0.0841  0.0778  37  GLY   B CA  
562  C C   . GLY   B 28  ? 0.5421 0.4613 0.4564 0.1631  0.0805  0.0693  37  GLY   B C   
563  O O   . GLY   B 28  ? 0.5554 0.4658 0.4701 0.1674  0.0813  0.0703  37  GLY   B O   
564  N N   . VAL   B 29  ? 0.5281 0.4494 0.4341 0.1688  0.0758  0.0611  38  VAL   B N   
565  C CA  . VAL   B 29  ? 0.5299 0.4455 0.4279 0.1799  0.0704  0.0529  38  VAL   B CA  
566  C C   . VAL   B 29  ? 0.5249 0.4376 0.4224 0.1734  0.0645  0.0403  38  VAL   B C   
567  O O   . VAL   B 29  ? 0.5159 0.4320 0.4145 0.1643  0.0645  0.0394  38  VAL   B O   
568  C CB  . VAL   B 29  ? 0.5368 0.4588 0.4213 0.1978  0.0693  0.0595  38  VAL   B CB  
569  C CG1 . VAL   B 29  ? 0.5440 0.4593 0.4190 0.2099  0.0615  0.0504  38  VAL   B CG1 
570  C CG2 . VAL   B 29  ? 0.5335 0.4606 0.4184 0.2044  0.0761  0.0738  38  VAL   B CG2 
571  N N   . GLY   B 30  ? 0.5114 0.4187 0.4077 0.1774  0.0595  0.0314  39  GLY   B N   
572  C CA  . GLY   B 30  ? 0.5120 0.4178 0.4087 0.1707  0.0536  0.0213  39  GLY   B CA  
573  C C   . GLY   B 30  ? 0.5237 0.4263 0.4156 0.1796  0.0456  0.0145  39  GLY   B C   
574  O O   . GLY   B 30  ? 0.5391 0.4400 0.4271 0.1923  0.0445  0.0161  39  GLY   B O   
575  N N   . VAL   B 31  ? 0.4996 0.4010 0.3916 0.1726  0.0393  0.0072  40  VAL   B N   
576  C CA  . VAL   B 31  ? 0.5050 0.4033 0.3943 0.1776  0.0295  0.0003  40  VAL   B CA  
577  C C   . VAL   B 31  ? 0.5055 0.4084 0.4082 0.1659  0.0286  -0.0071 40  VAL   B C   
578  O O   . VAL   B 31  ? 0.4955 0.4010 0.4032 0.1522  0.0305  -0.0087 40  VAL   B O   
579  C CB  . VAL   B 31  ? 0.5322 0.4239 0.4084 0.1796  0.0206  -0.0004 40  VAL   B CB  
580  C CG1 . VAL   B 31  ? 0.5571 0.4434 0.4320 0.1812  0.0085  -0.0080 40  VAL   B CG1 
581  C CG2 . VAL   B 31  ? 0.5387 0.4287 0.4000 0.1950  0.0209  0.0065  40  VAL   B CG2 
582  N N   . MET   B 32  ? 0.4932 0.3987 0.4013 0.1720  0.0256  -0.0117 41  MET   B N   
583  C CA  . MET   B 32  ? 0.4935 0.4076 0.4149 0.1630  0.0241  -0.0185 41  MET   B CA  
584  C C   . MET   B 32  ? 0.5084 0.4204 0.4277 0.1627  0.0114  -0.0228 41  MET   B C   
585  O O   . MET   B 32  ? 0.5114 0.4175 0.4228 0.1757  0.0037  -0.0240 41  MET   B O   
586  C CB  . MET   B 32  ? 0.4858 0.4050 0.4145 0.1706  0.0275  -0.0211 41  MET   B CB  
587  C CG  . MET   B 32  ? 0.4921 0.4246 0.4355 0.1628  0.0280  -0.0278 41  MET   B CG  
588  S SD  . MET   B 32  ? 0.5333 0.4711 0.4831 0.1485  0.0382  -0.0272 41  MET   B SD  
589  C CE  . MET   B 32  ? 0.5104 0.4423 0.4589 0.1582  0.0455  -0.0259 41  MET   B CE  
590  N N   . GLN   B 33  ? 0.4977 0.4131 0.4227 0.1481  0.0087  -0.0247 42  GLN   B N   
591  C CA  . GLN   B 33  ? 0.5183 0.4303 0.4428 0.1444  -0.0042 -0.0280 42  GLN   B CA  
592  C C   . GLN   B 33  ? 0.5259 0.4507 0.4657 0.1271  -0.0032 -0.0297 42  GLN   B C   
593  O O   . GLN   B 33  ? 0.5232 0.4514 0.4648 0.1166  0.0049  -0.0270 42  GLN   B O   
594  C CB  . GLN   B 33  ? 0.5526 0.4474 0.4593 0.1465  -0.0124 -0.0255 42  GLN   B CB  
595  C CG  . GLN   B 33  ? 0.6157 0.5028 0.5208 0.1436  -0.0286 -0.0296 42  GLN   B CG  
596  C CD  . GLN   B 33  ? 0.7034 0.5699 0.5874 0.1498  -0.0393 -0.0286 42  GLN   B CD  
597  O OE1 . GLN   B 33  ? 0.7494 0.6063 0.6302 0.1388  -0.0483 -0.0289 42  GLN   B OE1 
598  N NE2 . GLN   B 33  ? 0.6848 0.5443 0.5533 0.1681  -0.0385 -0.0270 42  GLN   B NE2 
599  N N   . GLU   B 34  ? 0.5310 0.4652 0.4825 0.1243  -0.0108 -0.0338 43  GLU   B N   
600  C CA  . GLU   B 34  ? 0.5387 0.4903 0.5074 0.1079  -0.0100 -0.0344 43  GLU   B CA  
601  C C   . GLU   B 34  ? 0.5416 0.5104 0.5205 0.1035  0.0047  -0.0339 43  GLU   B C   
602  O O   . GLU   B 34  ? 0.5518 0.5302 0.5372 0.0895  0.0090  -0.0316 43  GLU   B O   
603  C CB  . GLU   B 34  ? 0.5854 0.5274 0.5494 0.0934  -0.0172 -0.0309 43  GLU   B CB  
604  C CG  . GLU   B 34  ? 0.6556 0.5793 0.6096 0.0973  -0.0345 -0.0325 43  GLU   B CG  
605  C CD  . GLU   B 34  ? 0.7609 0.6656 0.7019 0.0877  -0.0424 -0.0290 43  GLU   B CD  
606  O OE1 . GLU   B 34  ? 0.7787 0.6904 0.7287 0.0699  -0.0415 -0.0255 43  GLU   B OE1 
607  O OE2 . GLU   B 34  ? 0.8127 0.6957 0.7335 0.0990  -0.0496 -0.0294 43  GLU   B OE2 
608  N N   . GLY   B 35  ? 0.5245 0.4956 0.5030 0.1159  0.0118  -0.0360 44  GLY   B N   
609  C CA  . GLY   B 35  ? 0.5097 0.4931 0.4949 0.1143  0.0239  -0.0368 44  GLY   B CA  
610  C C   . GLY   B 35  ? 0.4949 0.4689 0.4709 0.1096  0.0321  -0.0331 44  GLY   B C   
611  O O   . GLY   B 35  ? 0.4930 0.4755 0.4732 0.1075  0.0408  -0.0343 44  GLY   B O   
612  N N   . VAL   B 36  ? 0.4808 0.4377 0.4436 0.1093  0.0287  -0.0290 45  VAL   B N   
613  C CA  . VAL   B 36  ? 0.4787 0.4273 0.4329 0.1052  0.0350  -0.0253 45  VAL   B CA  
614  C C   . VAL   B 36  ? 0.4788 0.4136 0.4218 0.1171  0.0358  -0.0222 45  VAL   B C   
615  O O   . VAL   B 36  ? 0.4908 0.4174 0.4263 0.1261  0.0287  -0.0212 45  VAL   B O   
616  C CB  . VAL   B 36  ? 0.4918 0.4353 0.4405 0.0933  0.0306  -0.0224 45  VAL   B CB  
617  C CG1 . VAL   B 36  ? 0.5019 0.4345 0.4388 0.0921  0.0347  -0.0186 45  VAL   B CG1 
618  C CG2 . VAL   B 36  ? 0.4920 0.4518 0.4526 0.0801  0.0329  -0.0232 45  VAL   B CG2 
619  N N   . PHE   B 37  ? 0.4585 0.3916 0.4005 0.1176  0.0441  -0.0204 46  PHE   B N   
620  C CA  . PHE   B 37  ? 0.4632 0.3863 0.3969 0.1265  0.0461  -0.0154 46  PHE   B CA  
621  C C   . PHE   B 37  ? 0.4624 0.3798 0.3876 0.1210  0.0468  -0.0107 46  PHE   B C   
622  O O   . PHE   B 37  ? 0.4514 0.3713 0.3786 0.1111  0.0506  -0.0113 46  PHE   B O   
623  C CB  . PHE   B 37  ? 0.4568 0.3796 0.3949 0.1299  0.0530  -0.0154 46  PHE   B CB  
624  C CG  . PHE   B 37  ? 0.4638 0.3778 0.3952 0.1386  0.0546  -0.0085 46  PHE   B CG  
625  C CD1 . PHE   B 37  ? 0.4661 0.3770 0.3922 0.1510  0.0508  -0.0063 46  PHE   B CD1 
626  C CD2 . PHE   B 37  ? 0.4751 0.3849 0.4055 0.1342  0.0597  -0.0035 46  PHE   B CD2 
627  C CE1 . PHE   B 37  ? 0.4854 0.3907 0.4051 0.1593  0.0533  0.0018  46  PHE   B CE1 
628  C CE2 . PHE   B 37  ? 0.4837 0.3885 0.4097 0.1409  0.0616  0.0049  46  PHE   B CE2 
629  C CZ  . PHE   B 37  ? 0.4891 0.3923 0.4097 0.1536  0.0591  0.0079  46  PHE   B CZ  
630  N N   . HIS   B 38  ? 0.4627 0.3733 0.3774 0.1291  0.0427  -0.0064 47  HIS   B N   
631  C CA  . HIS   B 38  ? 0.4669 0.3732 0.3719 0.1270  0.0421  -0.0021 47  HIS   B CA  
632  C C   . HIS   B 38  ? 0.4890 0.3954 0.3907 0.1344  0.0471  0.0051  47  HIS   B C   
633  O O   . HIS   B 38  ? 0.5024 0.4076 0.4004 0.1465  0.0461  0.0082  47  HIS   B O   
634  C CB  . HIS   B 38  ? 0.4647 0.3638 0.3579 0.1330  0.0321  -0.0026 47  HIS   B CB  
635  C CG  . HIS   B 38  ? 0.4904 0.3886 0.3874 0.1254  0.0251  -0.0081 47  HIS   B CG  
636  N ND1 . HIS   B 38  ? 0.5038 0.4069 0.4100 0.1275  0.0226  -0.0123 47  HIS   B ND1 
637  C CD2 . HIS   B 38  ? 0.5041 0.3981 0.3976 0.1152  0.0202  -0.0092 47  HIS   B CD2 
638  C CE1 . HIS   B 38  ? 0.5119 0.4157 0.4218 0.1175  0.0165  -0.0153 47  HIS   B CE1 
639  N NE2 . HIS   B 38  ? 0.5207 0.4180 0.4227 0.1096  0.0149  -0.0132 47  HIS   B NE2 
640  N N   . THR   B 39  ? 0.4816 0.3900 0.3840 0.1274  0.0518  0.0084  48  THR   B N   
641  C CA  . THR   B 39  ? 0.4887 0.3999 0.3896 0.1329  0.0560  0.0168  48  THR   B CA  
642  C C   . THR   B 39  ? 0.4949 0.4094 0.3920 0.1272  0.0568  0.0199  48  THR   B C   
643  O O   . THR   B 39  ? 0.4996 0.4116 0.3927 0.1205  0.0537  0.0153  48  THR   B O   
644  C CB  . THR   B 39  ? 0.4921 0.4035 0.4033 0.1318  0.0618  0.0191  48  THR   B CB  
645  O OG1 . THR   B 39  ? 0.4857 0.4006 0.3959 0.1373  0.0653  0.0293  48  THR   B OG1 
646  C CG2 . THR   B 39  ? 0.5023 0.4129 0.4220 0.1191  0.0650  0.0148  48  THR   B CG2 
647  N N   . MET   B 40  ? 0.4986 0.4196 0.3970 0.1299  0.0609  0.0283  49  MET   B N   
648  C CA  . MET   B 40  ? 0.4908 0.4176 0.3875 0.1249  0.0618  0.0314  49  MET   B CA  
649  C C   . MET   B 40  ? 0.4872 0.4144 0.3955 0.1115  0.0656  0.0299  49  MET   B C   
650  O O   . MET   B 40  ? 0.4805 0.4056 0.3979 0.1090  0.0687  0.0313  49  MET   B O   
651  C CB  . MET   B 40  ? 0.4964 0.4341 0.3896 0.1348  0.0637  0.0417  49  MET   B CB  
652  C CG  . MET   B 40  ? 0.5334 0.4701 0.4134 0.1514  0.0597  0.0430  49  MET   B CG  
653  S SD  . MET   B 40  ? 0.6255 0.5755 0.4933 0.1646  0.0590  0.0512  49  MET   B SD  
654  C CE  . MET   B 40  ? 0.6150 0.5564 0.4716 0.1597  0.0517  0.0425  49  MET   B CE  
655  N N   A TRP   B 41  ? 0.4914 0.4195 0.3977 0.1038  0.0644  0.0268  50  TRP   B N   
656  N N   D TRP   B 41  ? 0.4840 0.4120 0.3903 0.1037  0.0644  0.0267  50  TRP   B N   
657  C CA  A TRP   B 41  ? 0.5020 0.4295 0.4167 0.0921  0.0666  0.0240  50  TRP   B CA  
658  C CA  D TRP   B 41  ? 0.4872 0.4145 0.4020 0.0921  0.0666  0.0239  50  TRP   B CA  
659  C C   A TRP   B 41  ? 0.4926 0.4250 0.4176 0.0895  0.0695  0.0317  50  TRP   B C   
660  C C   D TRP   B 41  ? 0.4855 0.4179 0.4107 0.0895  0.0696  0.0317  50  TRP   B C   
661  O O   A TRP   B 41  ? 0.4846 0.4110 0.4176 0.0829  0.0705  0.0294  50  TRP   B O   
662  O O   D TRP   B 41  ? 0.4772 0.4035 0.4103 0.0830  0.0705  0.0294  50  TRP   B O   
663  C CB  A TRP   B 41  ? 0.5150 0.4434 0.4235 0.0862  0.0644  0.0203  50  TRP   B CB  
664  C CB  D TRP   B 41  ? 0.4895 0.4173 0.3983 0.0859  0.0645  0.0198  50  TRP   B CB  
665  C CG  A TRP   B 41  ? 0.5397 0.4653 0.4542 0.0757  0.0655  0.0150  50  TRP   B CG  
666  C CG  D TRP   B 41  ? 0.4998 0.4259 0.4155 0.0756  0.0657  0.0156  50  TRP   B CG  
667  C CD1 A TRP   B 41  ? 0.5557 0.4756 0.4691 0.0711  0.0657  0.0070  50  TRP   B CD1 
668  C CD1 D TRP   B 41  ? 0.5071 0.4374 0.4303 0.0704  0.0662  0.0193  50  TRP   B CD1 
669  C CD2 A TRP   B 41  ? 0.5477 0.4766 0.4701 0.0694  0.0660  0.0174  50  TRP   B CD2 
670  C CD2 D TRP   B 41  ? 0.5037 0.4237 0.4190 0.0699  0.0660  0.0071  50  TRP   B CD2 
671  N NE1 A TRP   B 41  ? 0.5651 0.4833 0.4831 0.0641  0.0663  0.0034  50  TRP   B NE1 
672  N NE1 D TRP   B 41  ? 0.5100 0.4342 0.4363 0.0625  0.0657  0.0124  50  TRP   B NE1 
673  C CE2 A TRP   B 41  ? 0.5624 0.4846 0.4861 0.0623  0.0657  0.0094  50  TRP   B CE2 
674  C CE2 D TRP   B 41  ? 0.5132 0.4320 0.4341 0.0630  0.0662  0.0049  50  TRP   B CE2 
675  C CE3 A TRP   B 41  ? 0.5548 0.4929 0.4838 0.0689  0.0663  0.0260  50  TRP   B CE3 
676  C CE3 D TRP   B 41  ? 0.5156 0.4325 0.4271 0.0701  0.0659  0.0014  50  TRP   B CE3 
677  C CZ2 A TRP   B 41  ? 0.5765 0.4977 0.5064 0.0552  0.0642  0.0084  50  TRP   B CZ2 
678  C CZ2 D TRP   B 41  ? 0.5233 0.4373 0.4433 0.0584  0.0665  -0.0034 50  TRP   B CZ2 
679  C CZ3 A TRP   B 41  ? 0.5662 0.5049 0.5039 0.0599  0.0651  0.0260  50  TRP   B CZ3 
680  C CZ3 D TRP   B 41  ? 0.5283 0.4437 0.4409 0.0645  0.0674  -0.0054 50  TRP   B CZ3 
681  C CH2 A TRP   B 41  ? 0.5737 0.5024 0.5112 0.0533  0.0634  0.0167  50  TRP   B CH2 
682  C CH2 D TRP   B 41  ? 0.5262 0.4399 0.4419 0.0599  0.0678  -0.0081 50  TRP   B CH2 
683  N N   . HIS   B 42  ? 0.4857 0.4293 0.4105 0.0948  0.0706  0.0413  51  HIS   B N   
684  C CA  . HIS   B 42  ? 0.4925 0.4433 0.4294 0.0902  0.0734  0.0509  51  HIS   B CA  
685  C C   . HIS   B 42  ? 0.5090 0.4523 0.4522 0.0917  0.0757  0.0547  51  HIS   B C   
686  O O   . HIS   B 42  ? 0.5184 0.4612 0.4722 0.0844  0.0768  0.0609  51  HIS   B O   
687  C CB  . HIS   B 42  ? 0.4929 0.4621 0.4297 0.0955  0.0748  0.0615  51  HIS   B CB  
688  C CG  . HIS   B 42  ? 0.5114 0.4867 0.4413 0.1101  0.0768  0.0685  51  HIS   B CG  
689  N ND1 . HIS   B 42  ? 0.5371 0.5118 0.4514 0.1222  0.0738  0.0645  51  HIS   B ND1 
690  C CD2 . HIS   B 42  ? 0.5178 0.4980 0.4530 0.1146  0.0808  0.0789  51  HIS   B CD2 
691  C CE1 . HIS   B 42  ? 0.5391 0.5197 0.4494 0.1349  0.0759  0.0720  51  HIS   B CE1 
692  N NE2 . HIS   B 42  ? 0.5300 0.5147 0.4526 0.1309  0.0808  0.0811  51  HIS   B NE2 
693  N N   . VAL   B 43  ? 0.5022 0.4378 0.4388 0.1002  0.0755  0.0503  52  VAL   B N   
694  C CA  . VAL   B 43  ? 0.5069 0.4343 0.4474 0.1031  0.0772  0.0529  52  VAL   B CA  
695  C C   . VAL   B 43  ? 0.5166 0.4302 0.4629 0.0942  0.0758  0.0450  52  VAL   B C   
696  O O   . VAL   B 43  ? 0.5246 0.4312 0.4776 0.0903  0.0763  0.0499  52  VAL   B O   
697  C CB  . VAL   B 43  ? 0.5220 0.4473 0.4534 0.1165  0.0764  0.0505  52  VAL   B CB  
698  C CG1 . VAL   B 43  ? 0.5279 0.4426 0.4620 0.1200  0.0774  0.0503  52  VAL   B CG1 
699  C CG2 . VAL   B 43  ? 0.5211 0.4583 0.4451 0.1282  0.0774  0.0595  52  VAL   B CG2 
700  N N   . THR   B 44  ? 0.4945 0.4038 0.4371 0.0918  0.0737  0.0331  53  THR   B N   
701  C CA  . THR   B 44  ? 0.5041 0.4022 0.4497 0.0866  0.0725  0.0244  53  THR   B CA  
702  C C   . THR   B 44  ? 0.5133 0.4101 0.4609 0.0762  0.0706  0.0197  53  THR   B C   
703  O O   . THR   B 44  ? 0.5213 0.4078 0.4707 0.0726  0.0688  0.0135  53  THR   B O   
704  C CB  . THR   B 44  ? 0.5054 0.4024 0.4463 0.0918  0.0720  0.0145  53  THR   B CB  
705  O OG1 . THR   B 44  ? 0.5039 0.4078 0.4401 0.0889  0.0711  0.0104  53  THR   B OG1 
706  C CG2 . THR   B 44  ? 0.5126 0.4106 0.4509 0.1029  0.0723  0.0173  53  THR   B CG2 
707  N N   . LYS   B 45  ? 0.5158 0.4222 0.4611 0.0732  0.0703  0.0214  54  LYS   B N   
708  C CA  . LYS   B 45  ? 0.5424 0.4492 0.4872 0.0648  0.0682  0.0161  54  LYS   B CA  
709  C C   . LYS   B 45  ? 0.5541 0.4558 0.4935 0.0644  0.0679  0.0042  54  LYS   B C   
710  O O   . LYS   B 45  ? 0.5700 0.4675 0.5088 0.0590  0.0661  -0.0019 54  LYS   B O   
711  C CB  . LYS   B 45  ? 0.5948 0.4967 0.5481 0.0564  0.0656  0.0192  54  LYS   B CB  
712  C CG  . LYS   B 45  ? 0.6708 0.5790 0.6326 0.0554  0.0666  0.0328  54  LYS   B CG  
713  C CD  . LYS   B 45  ? 0.7576 0.6839 0.7189 0.0575  0.0682  0.0404  54  LYS   B CD  
714  C CE  . LYS   B 45  ? 0.8261 0.7615 0.7985 0.0541  0.0693  0.0545  54  LYS   B CE  
715  N NZ  . LYS   B 45  ? 0.8588 0.8132 0.8287 0.0627  0.0730  0.0642  54  LYS   B NZ  
716  N N   . GLY   B 46  ? 0.5504 0.4535 0.4862 0.0705  0.0695  0.0013  55  GLY   B N   
717  C CA  . GLY   B 46  ? 0.5586 0.4617 0.4912 0.0703  0.0701  -0.0080 55  GLY   B CA  
718  C C   . GLY   B 46  ? 0.5726 0.4685 0.5081 0.0729  0.0702  -0.0139 55  GLY   B C   
719  O O   . GLY   B 46  ? 0.5799 0.4784 0.5130 0.0733  0.0712  -0.0216 55  GLY   B O   
720  N N   . ALA   B 47  ? 0.5746 0.4616 0.5144 0.0750  0.0691  -0.0102 56  ALA   B N   
721  C CA  . ALA   B 47  ? 0.5730 0.4499 0.5132 0.0789  0.0680  -0.0163 56  ALA   B CA  
722  C C   . ALA   B 47  ? 0.5729 0.4547 0.5128 0.0877  0.0699  -0.0198 56  ALA   B C   
723  O O   . ALA   B 47  ? 0.5646 0.4534 0.5053 0.0907  0.0712  -0.0152 56  ALA   B O   
724  C CB  . ALA   B 47  ? 0.5758 0.4392 0.5197 0.0778  0.0653  -0.0100 56  ALA   B CB  
725  N N   . ALA   B 48  ? 0.5782 0.4562 0.5166 0.0928  0.0694  -0.0280 57  ALA   B N   
726  C CA  . ALA   B 48  ? 0.5803 0.4648 0.5198 0.1017  0.0708  -0.0316 57  ALA   B CA  
727  C C   . ALA   B 48  ? 0.5788 0.4549 0.5198 0.1080  0.0698  -0.0252 57  ALA   B C   
728  O O   . ALA   B 48  ? 0.5868 0.4498 0.5277 0.1058  0.0681  -0.0190 57  ALA   B O   
729  C CB  . ALA   B 48  ? 0.5917 0.4748 0.5284 0.1076  0.0704  -0.0419 57  ALA   B CB  
730  N N   . LEU   B 49  ? 0.5620 0.4460 0.5045 0.1157  0.0705  -0.0263 58  LEU   B N   
731  C CA  . LEU   B 49  ? 0.5686 0.4459 0.5108 0.1237  0.0696  -0.0207 58  LEU   B CA  
732  C C   . LEU   B 49  ? 0.5965 0.4735 0.5382 0.1345  0.0686  -0.0279 58  LEU   B C   
733  O O   . LEU   B 49  ? 0.5993 0.4885 0.5430 0.1361  0.0693  -0.0362 58  LEU   B O   
734  C CB  . LEU   B 49  ? 0.5535 0.4408 0.4965 0.1252  0.0699  -0.0151 58  LEU   B CB  
735  C CG  . LEU   B 49  ? 0.5670 0.4566 0.5088 0.1174  0.0705  -0.0081 58  LEU   B CG  
736  C CD1 . LEU   B 49  ? 0.5650 0.4628 0.5047 0.1213  0.0692  -0.0051 58  LEU   B CD1 
737  C CD2 . LEU   B 49  ? 0.5840 0.4634 0.5255 0.1154  0.0711  0.0009  58  LEU   B CD2 
738  N N   . ARG   B 50  ? 0.6128 0.4776 0.5519 0.1424  0.0671  -0.0240 59  ARG   B N   
739  C CA  . ARG   B 50  ? 0.6426 0.5056 0.5798 0.1547  0.0656  -0.0302 59  ARG   B CA  
740  C C   . ARG   B 50  ? 0.6549 0.5245 0.5929 0.1628  0.0652  -0.0261 59  ARG   B C   
741  O O   . ARG   B 50  ? 0.6429 0.5085 0.5792 0.1616  0.0657  -0.0165 59  ARG   B O   
742  C CB  . ARG   B 50  ? 0.6856 0.5244 0.6164 0.1580  0.0628  -0.0285 59  ARG   B CB  
743  C CG  . ARG   B 50  ? 0.7683 0.6008 0.6942 0.1721  0.0603  -0.0354 59  ARG   B CG  
744  C CD  . ARG   B 50  ? 0.8467 0.6517 0.7641 0.1746  0.0559  -0.0358 59  ARG   B CD  
745  N NE  . ARG   B 50  ? 0.9070 0.6936 0.8233 0.1665  0.0550  -0.0228 59  ARG   B NE  
746  C CZ  . ARG   B 50  ? 0.9582 0.7353 0.8717 0.1714  0.0551  -0.0130 59  ARG   B CZ  
747  N NH1 . ARG   B 50  ? 0.9501 0.7330 0.8609 0.1849  0.0554  -0.0155 59  ARG   B NH1 
748  N NH2 . ARG   B 50  ? 0.9800 0.7435 0.8939 0.1628  0.0549  0.0000  59  ARG   B NH2 
749  N N   . SER   B 51  ? 0.6649 0.5464 0.6053 0.1717  0.0639  -0.0336 60  SER   B N   
750  C CA  . SER   B 51  ? 0.6895 0.5760 0.6299 0.1813  0.0618  -0.0317 60  SER   B CA  
751  C C   . SER   B 51  ? 0.7230 0.6080 0.6617 0.1945  0.0598  -0.0392 60  SER   B C   
752  O O   . SER   B 51  ? 0.7242 0.6265 0.6689 0.1970  0.0594  -0.0480 60  SER   B O   
753  C CB  . SER   B 51  ? 0.6870 0.5937 0.6344 0.1771  0.0607  -0.0343 60  SER   B CB  
754  O OG  . SER   B 51  ? 0.7036 0.6136 0.6502 0.1868  0.0570  -0.0333 60  SER   B OG  
755  N N   . GLY   B 52  ? 0.7483 0.6129 0.6786 0.2025  0.0586  -0.0353 61  GLY   B N   
756  C CA  . GLY   B 52  ? 0.7713 0.6301 0.6969 0.2162  0.0560  -0.0425 61  GLY   B CA  
757  C C   . GLY   B 52  ? 0.7936 0.6500 0.7183 0.2137  0.0562  -0.0506 61  GLY   B C   
758  O O   . GLY   B 52  ? 0.8069 0.6490 0.7287 0.2040  0.0568  -0.0469 61  GLY   B O   
759  N N   . GLU   B 53  ? 0.7937 0.6669 0.7216 0.2220  0.0555  -0.0615 62  GLU   B N   
760  C CA  . GLU   B 53  ? 0.8085 0.6832 0.7343 0.2215  0.0560  -0.0699 62  GLU   B CA  
761  C C   . GLU   B 53  ? 0.7938 0.6936 0.7298 0.2093  0.0603  -0.0720 62  GLU   B C   
762  O O   . GLU   B 53  ? 0.8020 0.7053 0.7359 0.2085  0.0614  -0.0783 62  GLU   B O   
763  C CB  . GLU   B 53  ? 0.8596 0.7379 0.7805 0.2394  0.0533  -0.0805 62  GLU   B CB  
764  C CG  . GLU   B 53  ? 0.9857 0.8298 0.8908 0.2481  0.0484  -0.0817 62  GLU   B CG  
765  C CD  . GLU   B 53  ? 1.1497 0.9955 1.0468 0.2667  0.0451  -0.0939 62  GLU   B CD  
766  O OE1 . GLU   B 53  ? 1.1835 1.0502 1.0855 0.2784  0.0451  -0.0985 62  GLU   B OE1 
767  O OE2 . GLU   B 53  ? 1.1980 1.0244 1.0835 0.2704  0.0416  -0.0994 62  GLU   B OE2 
768  N N   . GLY   B 54  ? 0.7703 0.6848 0.7154 0.2003  0.0620  -0.0665 63  GLY   B N   
769  C CA  . GLY   B 54  ? 0.7512 0.6868 0.7049 0.1881  0.0653  -0.0669 63  GLY   B CA  
770  C C   . GLY   B 54  ? 0.7397 0.6628 0.6903 0.1743  0.0670  -0.0607 63  GLY   B C   
771  O O   . GLY   B 54  ? 0.7557 0.6590 0.7012 0.1720  0.0657  -0.0534 63  GLY   B O   
772  N N   . ARG   B 55  ? 0.7034 0.6396 0.6571 0.1654  0.0700  -0.0630 64  ARG   B N   
773  C CA  . ARG   B 55  ? 0.6820 0.6085 0.6326 0.1529  0.0713  -0.0581 64  ARG   B CA  
774  C C   . ARG   B 55  ? 0.6411 0.5823 0.5981 0.1420  0.0726  -0.0531 64  ARG   B C   
775  O O   . ARG   B 55  ? 0.6406 0.6030 0.6051 0.1411  0.0735  -0.0556 64  ARG   B O   
776  C CB  . ARG   B 55  ? 0.7059 0.6323 0.6518 0.1519  0.0728  -0.0646 64  ARG   B CB  
777  C CG  . ARG   B 55  ? 0.7465 0.6597 0.6879 0.1406  0.0728  -0.0607 64  ARG   B CG  
778  C CD  . ARG   B 55  ? 0.7842 0.6958 0.7191 0.1422  0.0729  -0.0685 64  ARG   B CD  
779  N NE  . ARG   B 55  ? 0.8174 0.7233 0.7494 0.1308  0.0731  -0.0659 64  ARG   B NE  
780  C CZ  . ARG   B 55  ? 0.8496 0.7381 0.7737 0.1302  0.0696  -0.0694 64  ARG   B CZ  
781  N NH1 . ARG   B 55  ? 0.8408 0.7128 0.7579 0.1402  0.0651  -0.0754 64  ARG   B NH1 
782  N NH2 . ARG   B 55  ? 0.8457 0.7317 0.7681 0.1201  0.0695  -0.0672 64  ARG   B NH2 
783  N N   . LEU   B 56  ? 0.6011 0.5310 0.5552 0.1339  0.0721  -0.0458 65  LEU   B N   
784  C CA  . LEU   B 56  ? 0.5744 0.5131 0.5310 0.1245  0.0722  -0.0413 65  LEU   B CA  
785  C C   . LEU   B 56  ? 0.5592 0.4942 0.5117 0.1148  0.0743  -0.0405 65  LEU   B C   
786  O O   . LEU   B 56  ? 0.5642 0.4840 0.5122 0.1131  0.0737  -0.0373 65  LEU   B O   
787  C CB  . LEU   B 56  ? 0.5688 0.4982 0.5229 0.1256  0.0693  -0.0336 65  LEU   B CB  
788  C CG  . LEU   B 56  ? 0.5927 0.5216 0.5477 0.1364  0.0662  -0.0328 65  LEU   B CG  
789  C CD1 . LEU   B 56  ? 0.5935 0.5197 0.5451 0.1360  0.0630  -0.0262 65  LEU   B CD1 
790  C CD2 . LEU   B 56  ? 0.6062 0.5521 0.5689 0.1407  0.0649  -0.0397 65  LEU   B CD2 
791  N N   . ASP   B 57  ? 0.5381 0.4874 0.4927 0.1082  0.0764  -0.0428 66  ASP   B N   
792  C CA  . ASP   B 57  ? 0.5403 0.4868 0.4897 0.0999  0.0782  -0.0424 66  ASP   B CA  
793  C C   . ASP   B 57  ? 0.5286 0.4750 0.4761 0.0911  0.0769  -0.0360 66  ASP   B C   
794  O O   . ASP   B 57  ? 0.5246 0.4791 0.4756 0.0892  0.0751  -0.0338 66  ASP   B O   
795  C CB  . ASP   B 57  ? 0.5814 0.5433 0.5315 0.0994  0.0820  -0.0484 66  ASP   B CB  
796  C CG  . ASP   B 57  ? 0.6789 0.6382 0.6273 0.1102  0.0824  -0.0558 66  ASP   B CG  
797  O OD1 . ASP   B 57  ? 0.7030 0.6426 0.6459 0.1133  0.0796  -0.0565 66  ASP   B OD1 
798  O OD2 . ASP   B 57  ? 0.7144 0.6915 0.6669 0.1159  0.0848  -0.0605 66  ASP   B OD2 
799  N N   . PRO   B 58  ? 0.5201 0.4566 0.4617 0.0859  0.0766  -0.0331 67  PRO   B N   
800  C CA  . PRO   B 58  ? 0.5019 0.4381 0.4396 0.0791  0.0749  -0.0277 67  PRO   B CA  
801  C C   . PRO   B 58  ? 0.4896 0.4381 0.4273 0.0724  0.0762  -0.0288 67  PRO   B C   
802  O O   . PRO   B 58  ? 0.4892 0.4469 0.4280 0.0714  0.0799  -0.0332 67  PRO   B O   
803  C CB  . PRO   B 58  ? 0.5169 0.4434 0.4493 0.0756  0.0749  -0.0259 67  PRO   B CB  
804  C CG  . PRO   B 58  ? 0.5356 0.4596 0.4685 0.0776  0.0765  -0.0322 67  PRO   B CG  
805  C CD  . PRO   B 58  ? 0.5237 0.4494 0.4618 0.0858  0.0769  -0.0352 67  PRO   B CD  
806  N N   . TYR   B 59  ? 0.4734 0.4215 0.4088 0.0683  0.0728  -0.0244 68  TYR   B N   
807  C CA  . TYR   B 59  ? 0.4711 0.4286 0.4066 0.0603  0.0729  -0.0234 68  TYR   B CA  
808  C C   . TYR   B 59  ? 0.4747 0.4231 0.3995 0.0539  0.0704  -0.0191 68  TYR   B C   
809  O O   . TYR   B 59  ? 0.4716 0.4245 0.3925 0.0468  0.0726  -0.0185 68  TYR   B O   
810  C CB  . TYR   B 59  ? 0.4697 0.4335 0.4125 0.0607  0.0688  -0.0224 68  TYR   B CB  
811  C CG  . TYR   B 59  ? 0.4757 0.4498 0.4211 0.0505  0.0679  -0.0198 68  TYR   B CG  
812  C CD1 . TYR   B 59  ? 0.4918 0.4557 0.4287 0.0434  0.0626  -0.0150 68  TYR   B CD1 
813  C CD2 . TYR   B 59  ? 0.4761 0.4707 0.4325 0.0483  0.0719  -0.0216 68  TYR   B CD2 
814  C CE1 . TYR   B 59  ? 0.4943 0.4654 0.4334 0.0325  0.0610  -0.0112 68  TYR   B CE1 
815  C CE2 . TYR   B 59  ? 0.4773 0.4835 0.4380 0.0373  0.0713  -0.0172 68  TYR   B CE2 
816  C CZ  . TYR   B 59  ? 0.4904 0.4834 0.4426 0.0287  0.0654  -0.0117 68  TYR   B CZ  
817  O OH  . TYR   B 59  ? 0.5001 0.5019 0.4561 0.0164  0.0639  -0.0061 68  TYR   B OH  
818  N N   . TRP   B 60  ? 0.4733 0.4098 0.3923 0.0575  0.0659  -0.0160 69  TRP   B N   
819  C CA  . TRP   B 60  ? 0.4754 0.4026 0.3826 0.0542  0.0626  -0.0124 69  TRP   B CA  
820  C C   . TRP   B 60  ? 0.4819 0.4017 0.3854 0.0610  0.0615  -0.0104 69  TRP   B C   
821  O O   . TRP   B 60  ? 0.4672 0.3859 0.3748 0.0684  0.0605  -0.0094 69  TRP   B O   
822  C CB  . TRP   B 60  ? 0.4814 0.4033 0.3833 0.0510  0.0556  -0.0093 69  TRP   B CB  
823  C CG  . TRP   B 60  ? 0.4925 0.4016 0.3797 0.0516  0.0504  -0.0060 69  TRP   B CG  
824  C CD1 . TRP   B 60  ? 0.5055 0.4105 0.3829 0.0451  0.0502  -0.0044 69  TRP   B CD1 
825  C CD2 . TRP   B 60  ? 0.4833 0.3833 0.3629 0.0610  0.0451  -0.0039 69  TRP   B CD2 
826  N NE1 . TRP   B 60  ? 0.5141 0.4071 0.3780 0.0501  0.0443  -0.0021 69  TRP   B NE1 
827  C CE2 . TRP   B 60  ? 0.5012 0.3925 0.3666 0.0602  0.0417  -0.0017 69  TRP   B CE2 
828  C CE3 . TRP   B 60  ? 0.4844 0.3838 0.3669 0.0712  0.0433  -0.0035 69  TRP   B CE3 
829  C CZ2 . TRP   B 60  ? 0.5063 0.3899 0.3607 0.0699  0.0365  0.0006  69  TRP   B CZ2 
830  C CZ3 . TRP   B 60  ? 0.4942 0.3865 0.3657 0.0805  0.0389  -0.0005 69  TRP   B CZ3 
831  C CH2 . TRP   B 60  ? 0.5046 0.3896 0.3623 0.0801  0.0352  0.0012  69  TRP   B CH2 
832  N N   . GLY   B 61  ? 0.4889 0.4048 0.3845 0.0589  0.0614  -0.0088 70  GLY   B N   
833  C CA  . GLY   B 61  ? 0.4953 0.4081 0.3886 0.0645  0.0604  -0.0055 70  GLY   B CA  
834  C C   . GLY   B 61  ? 0.5039 0.4136 0.3864 0.0625  0.0582  -0.0036 70  GLY   B C   
835  O O   . GLY   B 61  ? 0.5090 0.4181 0.3864 0.0561  0.0589  -0.0057 70  GLY   B O   
836  N N   . ASP   B 62  ? 0.5000 0.4095 0.3791 0.0689  0.0561  0.0006  71  ASP   B N   
837  C CA  . ASP   B 62  ? 0.5085 0.4169 0.3771 0.0693  0.0535  0.0024  71  ASP   B CA  
838  C C   . ASP   B 62  ? 0.5039 0.4193 0.3757 0.0761  0.0540  0.0075  71  ASP   B C   
839  O O   . ASP   B 62  ? 0.5091 0.4253 0.3796 0.0848  0.0524  0.0113  71  ASP   B O   
840  C CB  . ASP   B 62  ? 0.5300 0.4289 0.3837 0.0717  0.0472  0.0031  71  ASP   B CB  
841  C CG  . ASP   B 62  ? 0.6345 0.5299 0.4743 0.0728  0.0437  0.0041  71  ASP   B CG  
842  O OD1 . ASP   B 62  ? 0.6364 0.5372 0.4739 0.0803  0.0427  0.0072  71  ASP   B OD1 
843  O OD2 . ASP   B 62  ? 0.6960 0.5843 0.5271 0.0666  0.0420  0.0024  71  ASP   B OD2 
844  N N   . VAL   B 63  ? 0.4972 0.4188 0.3738 0.0721  0.0559  0.0079  72  VAL   B N   
845  C CA  . VAL   B 63  ? 0.4960 0.4280 0.3789 0.0758  0.0567  0.0140  72  VAL   B CA  
846  C C   . VAL   B 63  ? 0.5106 0.4468 0.3819 0.0857  0.0531  0.0184  72  VAL   B C   
847  O O   . VAL   B 63  ? 0.5056 0.4514 0.3805 0.0932  0.0542  0.0250  72  VAL   B O   
848  C CB  . VAL   B 63  ? 0.4919 0.4290 0.3833 0.0677  0.0578  0.0127  72  VAL   B CB  
849  C CG1 . VAL   B 63  ? 0.4984 0.4495 0.3959 0.0700  0.0574  0.0199  72  VAL   B CG1 
850  C CG2 . VAL   B 63  ? 0.4804 0.4131 0.3834 0.0615  0.0605  0.0095  72  VAL   B CG2 
851  N N   . LYS   B 64  ? 0.5245 0.4532 0.3805 0.0868  0.0487  0.0153  73  LYS   B N   
852  C CA  . LYS   B 64  ? 0.5342 0.4653 0.3763 0.0984  0.0441  0.0186  73  LYS   B CA  
853  C C   . LYS   B 64  ? 0.5320 0.4573 0.3665 0.1094  0.0411  0.0205  73  LYS   B C   
854  O O   . LYS   B 64  ? 0.5362 0.4704 0.3666 0.1215  0.0401  0.0254  73  LYS   B O   
855  C CB  . LYS   B 64  ? 0.5511 0.4730 0.3766 0.0976  0.0391  0.0150  73  LYS   B CB  
856  C CG  . LYS   B 64  ? 0.6016 0.5279 0.4129 0.1112  0.0341  0.0181  73  LYS   B CG  
857  C CD  . LYS   B 64  ? 0.6325 0.5489 0.4267 0.1107  0.0289  0.0146  73  LYS   B CD  
858  C CE  . LYS   B 64  ? 0.6810 0.5985 0.4576 0.1266  0.0226  0.0167  73  LYS   B CE  
859  N NZ  . LYS   B 64  ? 0.7157 0.6190 0.4722 0.1272  0.0162  0.0131  73  LYS   B NZ  
860  N N   . GLN   B 65  ? 0.5382 0.4506 0.3720 0.1055  0.0396  0.0166  74  GLN   B N   
861  C CA  . GLN   B 65  ? 0.5357 0.4420 0.3641 0.1153  0.0358  0.0174  74  GLN   B CA  
862  C C   . GLN   B 65  ? 0.5226 0.4405 0.3652 0.1193  0.0416  0.0218  74  GLN   B C   
863  O O   . GLN   B 65  ? 0.5201 0.4374 0.3573 0.1312  0.0392  0.0241  74  GLN   B O   
864  C CB  . GLN   B 65  ? 0.5692 0.4607 0.3954 0.1083  0.0320  0.0123  74  GLN   B CB  
865  C CG  . GLN   B 65  ? 0.6484 0.5248 0.4577 0.1057  0.0244  0.0098  74  GLN   B CG  
866  C CD  . GLN   B 65  ? 0.7366 0.6012 0.5468 0.0967  0.0208  0.0066  74  GLN   B CD  
867  O OE1 . GLN   B 65  ? 0.7612 0.6213 0.5730 0.1006  0.0169  0.0058  74  GLN   B OE1 
868  N NE2 . GLN   B 65  ? 0.7501 0.6107 0.5594 0.0847  0.0219  0.0053  74  GLN   B NE2 
869  N N   . ASP   B 66  ? 0.5020 0.4281 0.3612 0.1096  0.0485  0.0227  75  ASP   B N   
870  C CA  . ASP   B 66  ? 0.4948 0.4287 0.3682 0.1103  0.0540  0.0272  75  ASP   B CA  
871  C C   . ASP   B 66  ? 0.4916 0.4168 0.3660 0.1125  0.0530  0.0239  75  ASP   B C   
872  O O   . ASP   B 66  ? 0.4922 0.4206 0.3689 0.1210  0.0544  0.0282  75  ASP   B O   
873  C CB  . ASP   B 66  ? 0.5064 0.4548 0.3800 0.1212  0.0560  0.0365  75  ASP   B CB  
874  C CG  . ASP   B 66  ? 0.5308 0.4872 0.4201 0.1187  0.0621  0.0430  75  ASP   B CG  
875  O OD1 . ASP   B 66  ? 0.5281 0.4812 0.4291 0.1069  0.0646  0.0406  75  ASP   B OD1 
876  O OD2 . ASP   B 66  ? 0.5592 0.5246 0.4478 0.1295  0.0641  0.0509  75  ASP   B OD2 
877  N N   . LEU   B 67  ? 0.4798 0.3957 0.3537 0.1047  0.0511  0.0169  76  LEU   B N   
878  C CA  . LEU   B 67  ? 0.4771 0.3873 0.3541 0.1057  0.0496  0.0133  76  LEU   B CA  
879  C C   . LEU   B 67  ? 0.4894 0.3995 0.3770 0.0944  0.0534  0.0081  76  LEU   B C   
880  O O   . LEU   B 67  ? 0.4902 0.4008 0.3778 0.0858  0.0549  0.0057  76  LEU   B O   
881  C CB  . LEU   B 67  ? 0.4830 0.3829 0.3470 0.1091  0.0413  0.0104  76  LEU   B CB  
882  C CG  . LEU   B 67  ? 0.4923 0.3896 0.3425 0.1237  0.0356  0.0138  76  LEU   B CG  
883  C CD1 . LEU   B 67  ? 0.5103 0.3928 0.3456 0.1256  0.0252  0.0100  76  LEU   B CD1 
884  C CD2 . LEU   B 67  ? 0.4719 0.3741 0.3265 0.1348  0.0376  0.0171  76  LEU   B CD2 
885  N N   . VAL   B 68  ? 0.4809 0.3909 0.3760 0.0961  0.0544  0.0058  77  VAL   B N   
886  C CA  . VAL   B 68  ? 0.4773 0.3894 0.3818 0.0885  0.0577  0.0003  77  VAL   B CA  
887  C C   . VAL   B 68  ? 0.4680 0.3802 0.3762 0.0925  0.0553  -0.0025 77  VAL   B C   
888  O O   . VAL   B 68  ? 0.4598 0.3702 0.3664 0.1023  0.0529  -0.0001 77  VAL   B O   
889  C CB  . VAL   B 68  ? 0.4788 0.3931 0.3919 0.0862  0.0632  0.0007  77  VAL   B CB  
890  C CG1 . VAL   B 68  ? 0.4790 0.3930 0.3952 0.0944  0.0643  0.0064  77  VAL   B CG1 
891  C CG2 . VAL   B 68  ? 0.4844 0.4004 0.4046 0.0817  0.0661  -0.0059 77  VAL   B CG2 
892  N N   . SER   B 69  ? 0.4512 0.3673 0.3644 0.0856  0.0557  -0.0073 78  SER   B N   
893  C CA  . SER   B 69  ? 0.4545 0.3746 0.3742 0.0880  0.0534  -0.0105 78  SER   B CA  
894  C C   . SER   B 69  ? 0.4556 0.3844 0.3856 0.0853  0.0593  -0.0150 78  SER   B C   
895  O O   . SER   B 69  ? 0.4504 0.3818 0.3807 0.0790  0.0637  -0.0166 78  SER   B O   
896  C CB  . SER   B 69  ? 0.4724 0.3918 0.3892 0.0823  0.0470  -0.0112 78  SER   B CB  
897  O OG  . SER   B 69  ? 0.5074 0.4321 0.4257 0.0709  0.0497  -0.0121 78  SER   B OG  
898  N N   . TYR   B 70  ? 0.4474 0.3806 0.3845 0.0914  0.0589  -0.0176 79  TYR   B N   
899  C CA  . TYR   B 70  ? 0.4541 0.3953 0.3994 0.0925  0.0635  -0.0226 79  TYR   B CA  
900  C C   . TYR   B 70  ? 0.4465 0.4008 0.4002 0.0920  0.0614  -0.0260 79  TYR   B C   
901  O O   . TYR   B 70  ? 0.4359 0.3889 0.3900 0.0955  0.0553  -0.0250 79  TYR   B O   
902  C CB  . TYR   B 70  ? 0.4669 0.4009 0.4127 0.1027  0.0647  -0.0221 79  TYR   B CB  
903  C CG  . TYR   B 70  ? 0.4801 0.4042 0.4215 0.1014  0.0674  -0.0184 79  TYR   B CG  
904  C CD1 . TYR   B 70  ? 0.4907 0.4087 0.4261 0.1021  0.0658  -0.0117 79  TYR   B CD1 
905  C CD2 . TYR   B 70  ? 0.4985 0.4202 0.4416 0.0998  0.0707  -0.0218 79  TYR   B CD2 
906  C CE1 . TYR   B 70  ? 0.5024 0.4148 0.4363 0.0996  0.0680  -0.0075 79  TYR   B CE1 
907  C CE2 . TYR   B 70  ? 0.5081 0.4204 0.4486 0.0970  0.0715  -0.0183 79  TYR   B CE2 
908  C CZ  . TYR   B 70  ? 0.5071 0.4163 0.4443 0.0960  0.0705  -0.0107 79  TYR   B CZ  
909  O OH  . TYR   B 70  ? 0.5119 0.4152 0.4491 0.0921  0.0712  -0.0066 79  TYR   B OH  
910  N N   . CYS   B 71  ? 0.4494 0.4175 0.4097 0.0880  0.0658  -0.0299 80  CYS   B N   
911  C CA  . CYS   B 71  ? 0.4667 0.4532 0.4380 0.0870  0.0651  -0.0327 80  CYS   B CA  
912  C C   . CYS   B 71  ? 0.4719 0.4655 0.4460 0.0754  0.0613  -0.0292 80  CYS   B C   
913  O O   . CYS   B 71  ? 0.4824 0.4949 0.4676 0.0715  0.0613  -0.0301 80  CYS   B O   
914  C CB  . CYS   B 71  ? 0.5018 0.4888 0.4779 0.0978  0.0611  -0.0351 80  CYS   B CB  
915  S SG  . CYS   B 71  ? 0.5810 0.5568 0.5529 0.1114  0.0646  -0.0380 80  CYS   B SG  
916  N N   . GLY   B 72  ? 0.4578 0.4370 0.4220 0.0701  0.0576  -0.0248 81  GLY   B N   
917  C CA  . GLY   B 72  ? 0.4563 0.4367 0.4204 0.0590  0.0522  -0.0210 81  GLY   B CA  
918  C C   . GLY   B 72  ? 0.4590 0.4196 0.4084 0.0568  0.0478  -0.0171 81  GLY   B C   
919  O O   . GLY   B 72  ? 0.4641 0.4135 0.4050 0.0637  0.0495  -0.0170 81  GLY   B O   
920  N N   . PRO   B 73  ? 0.4573 0.4137 0.4032 0.0469  0.0417  -0.0134 82  PRO   B N   
921  C CA  . PRO   B 73  ? 0.4780 0.4146 0.4076 0.0462  0.0365  -0.0103 82  PRO   B CA  
922  C C   . PRO   B 73  ? 0.4938 0.4152 0.4150 0.0576  0.0280  -0.0109 82  PRO   B C   
923  O O   . PRO   B 73  ? 0.4852 0.4098 0.4133 0.0629  0.0236  -0.0132 82  PRO   B O   
924  C CB  . PRO   B 73  ? 0.4901 0.4255 0.4187 0.0324  0.0311  -0.0061 82  PRO   B CB  
925  C CG  . PRO   B 73  ? 0.4798 0.4310 0.4251 0.0284  0.0285  -0.0069 82  PRO   B CG  
926  C CD  . PRO   B 73  ? 0.4479 0.4174 0.4046 0.0357  0.0387  -0.0114 82  PRO   B CD  
927  N N   . TRP   B 74  ? 0.5082 0.4143 0.4138 0.0622  0.0254  -0.0088 83  TRP   B N   
928  C CA  . TRP   B 74  ? 0.5279 0.4205 0.4222 0.0748  0.0177  -0.0087 83  TRP   B CA  
929  C C   . TRP   B 74  ? 0.5440 0.4282 0.4366 0.0743  0.0047  -0.0098 83  TRP   B C   
930  O O   . TRP   B 74  ? 0.5402 0.4170 0.4287 0.0639  -0.0018 -0.0082 83  TRP   B O   
931  C CB  . TRP   B 74  ? 0.5326 0.4128 0.4098 0.0780  0.0161  -0.0058 83  TRP   B CB  
932  C CG  . TRP   B 74  ? 0.5334 0.4044 0.3986 0.0938  0.0107  -0.0052 83  TRP   B CG  
933  C CD1 . TRP   B 74  ? 0.5441 0.3997 0.3948 0.1008  -0.0016 -0.0056 83  TRP   B CD1 
934  C CD2 . TRP   B 74  ? 0.5233 0.4006 0.3894 0.1051  0.0173  -0.0034 83  TRP   B CD2 
935  N NE1 . TRP   B 74  ? 0.5531 0.4069 0.3949 0.1175  -0.0024 -0.0046 83  TRP   B NE1 
936  C CE2 . TRP   B 74  ? 0.5441 0.4121 0.3960 0.1196  0.0097  -0.0023 83  TRP   B CE2 
937  C CE3 . TRP   B 74  ? 0.5028 0.3917 0.3797 0.1043  0.0283  -0.0022 83  TRP   B CE3 
938  C CZ2 . TRP   B 74  ? 0.5372 0.4109 0.3870 0.1329  0.0142  0.0011  83  TRP   B CZ2 
939  C CZ3 . TRP   B 74  ? 0.5134 0.4052 0.3886 0.1156  0.0317  0.0014  83  TRP   B CZ3 
940  C CH2 . TRP   B 74  ? 0.5217 0.4075 0.3841 0.1297  0.0254  0.0036  83  TRP   B CH2 
941  N N   . LYS   B 75  ? 0.5543 0.4383 0.4491 0.0855  0.0002  -0.0125 84  LYS   B N   
942  C CA  . LYS   B 75  ? 0.5680 0.4444 0.4625 0.0857  -0.0134 -0.0148 84  LYS   B CA  
943  C C   . LYS   B 75  ? 0.6033 0.4591 0.4777 0.0993  -0.0254 -0.0155 84  LYS   B C   
944  O O   . LYS   B 75  ? 0.6231 0.4672 0.4934 0.0986  -0.0394 -0.0177 84  LYS   B O   
945  C CB  . LYS   B 75  ? 0.5702 0.4608 0.4802 0.0903  -0.0123 -0.0184 84  LYS   B CB  
946  C CG  . LYS   B 75  ? 0.5832 0.4963 0.5127 0.0809  -0.0011 -0.0189 84  LYS   B CG  
947  C CD  . LYS   B 75  ? 0.6199 0.5408 0.5598 0.0637  -0.0051 -0.0174 84  LYS   B CD  
948  C CE  . LYS   B 75  ? 0.6438 0.5908 0.6030 0.0570  0.0055  -0.0181 84  LYS   B CE  
949  N NZ  . LYS   B 75  ? 0.6728 0.6319 0.6446 0.0409  0.0013  -0.0154 84  LYS   B NZ  
950  N N   . LEU   B 76  ? 0.6048 0.4573 0.4673 0.1123  -0.0206 -0.0138 85  LEU   B N   
951  C CA  . LEU   B 76  ? 0.6263 0.4634 0.4690 0.1293  -0.0304 -0.0144 85  LEU   B CA  
952  C C   . LEU   B 76  ? 0.6632 0.4817 0.4870 0.1279  -0.0396 -0.0135 85  LEU   B C   
953  O O   . LEU   B 76  ? 0.6590 0.4795 0.4790 0.1237  -0.0324 -0.0103 85  LEU   B O   
954  C CB  . LEU   B 76  ? 0.6150 0.4608 0.4546 0.1444  -0.0204 -0.0114 85  LEU   B CB  
955  C CG  . LEU   B 76  ? 0.6073 0.4699 0.4647 0.1447  -0.0093 -0.0112 85  LEU   B CG  
956  C CD1 . LEU   B 76  ? 0.6062 0.4746 0.4594 0.1582  -0.0011 -0.0065 85  LEU   B CD1 
957  C CD2 . LEU   B 76  ? 0.6199 0.4833 0.4846 0.1475  -0.0165 -0.0159 85  LEU   B CD2 
958  N N   . ASP   B 77  ? 0.6948 0.4938 0.5061 0.1312  -0.0567 -0.0168 86  ASP   B N   
959  C CA  . ASP   B 77  ? 0.7440 0.5211 0.5350 0.1300  -0.0673 -0.0162 86  ASP   B CA  
960  C C   . ASP   B 77  ? 0.7572 0.5129 0.5224 0.1504  -0.0826 -0.0197 86  ASP   B C   
961  O O   . ASP   B 77  ? 0.7794 0.5144 0.5246 0.1521  -0.0929 -0.0199 86  ASP   B O   
962  C CB  . ASP   B 77  ? 0.8113 0.5798 0.6092 0.1086  -0.0750 -0.0157 86  ASP   B CB  
963  C CG  . ASP   B 77  ? 0.9300 0.6960 0.7389 0.1033  -0.0866 -0.0191 86  ASP   B CG  
964  O OD1 . ASP   B 77  ? 0.9649 0.7342 0.7745 0.1176  -0.0894 -0.0230 86  ASP   B OD1 
965  O OD2 . ASP   B 77  ? 0.9755 0.7370 0.7924 0.0847  -0.0930 -0.0173 86  ASP   B OD2 
966  N N   . ALA   B 78  ? 0.7477 0.5079 0.5111 0.1675  -0.0839 -0.0222 87  ALA   B N   
967  C CA  . ALA   B 78  ? 0.7632 0.5050 0.5004 0.1900  -0.0980 -0.0258 87  ALA   B CA  
968  C C   . ALA   B 78  ? 0.7733 0.5168 0.4927 0.2038  -0.0919 -0.0221 87  ALA   B C   
969  O O   . ALA   B 78  ? 0.7578 0.5225 0.4888 0.2000  -0.0746 -0.0167 87  ALA   B O   
970  C CB  . ALA   B 78  ? 0.7487 0.4976 0.4881 0.2061  -0.0992 -0.0286 87  ALA   B CB  
971  N N   . ALA   B 79  ? 0.7889 0.5098 0.4801 0.2193  -0.1071 -0.0254 88  ALA   B N   
972  C CA  . ALA   B 79  ? 0.8062 0.5283 0.4779 0.2345  -0.1038 -0.0226 88  ALA   B CA  
973  C C   . ALA   B 79  ? 0.8132 0.5299 0.4604 0.2648  -0.1122 -0.0252 88  ALA   B C   
974  O O   . ALA   B 79  ? 0.8218 0.5182 0.4563 0.2739  -0.1290 -0.0317 88  ALA   B O   
975  C CB  . ALA   B 79  ? 0.8251 0.5240 0.4812 0.2260  -0.1142 -0.0238 88  ALA   B CB  
976  N N   . TRP   B 80  ? 0.8190 0.5543 0.4585 0.2812  -0.1013 -0.0200 89  TRP   B N   
977  C CA  . TRP   B 80  ? 0.8583 0.5924 0.4720 0.3124  -0.1077 -0.0212 89  TRP   B CA  
978  C C   . TRP   B 80  ? 0.8960 0.5956 0.4781 0.3227  -0.1297 -0.0287 89  TRP   B C   
979  O O   . TRP   B 80  ? 0.8849 0.5733 0.4637 0.3100  -0.1322 -0.0285 89  TRP   B O   
980  C CB  . TRP   B 80  ? 0.8565 0.6202 0.4702 0.3244  -0.0912 -0.0125 89  TRP   B CB  
981  C CG  . TRP   B 80  ? 0.8809 0.6484 0.4684 0.3580  -0.0960 -0.0123 89  TRP   B CG  
982  C CD1 . TRP   B 80  ? 0.9003 0.6631 0.4767 0.3772  -0.1033 -0.0155 89  TRP   B CD1 
983  C CD2 . TRP   B 80  ? 0.8860 0.6633 0.4532 0.3780  -0.0949 -0.0092 89  TRP   B CD2 
984  N NE1 . TRP   B 80  ? 0.9122 0.6811 0.4617 0.4085  -0.1063 -0.0144 89  TRP   B NE1 
985  C CE2 . TRP   B 80  ? 0.9028 0.6820 0.4468 0.4097  -0.1009 -0.0103 89  TRP   B CE2 
986  C CE3 . TRP   B 80  ? 0.8914 0.6776 0.4575 0.3734  -0.0893 -0.0057 89  TRP   B CE3 
987  C CZ2 . TRP   B 80  ? 0.9110 0.7042 0.4326 0.4365  -0.1000 -0.0071 89  TRP   B CZ2 
988  C CZ3 . TRP   B 80  ? 0.9007 0.6991 0.4445 0.3996  -0.0898 -0.0032 89  TRP   B CZ3 
989  C CH2 . TRP   B 80  ? 0.9071 0.7098 0.4292 0.4310  -0.0948 -0.0037 89  TRP   B CH2 
990  N N   . ASP   B 81  ? 0.9353 0.6149 0.4944 0.3439  -0.1471 -0.0357 90  ASP   B N   
991  C CA  . ASP   B 81  ? 0.9896 0.6312 0.5163 0.3542  -0.1708 -0.0437 90  ASP   B CA  
992  C C   . ASP   B 81  ? 1.0371 0.6799 0.5353 0.3784  -0.1717 -0.0428 90  ASP   B C   
993  O O   . ASP   B 81  ? 1.0733 0.6833 0.5429 0.3867  -0.1910 -0.0492 90  ASP   B O   
994  C CB  . ASP   B 81  ? 1.0176 0.6332 0.5277 0.3685  -0.1923 -0.0531 90  ASP   B CB  
995  C CG  . ASP   B 81  ? 1.0845 0.7144 0.5797 0.4008  -0.1903 -0.0536 90  ASP   B CG  
996  O OD1 . ASP   B 81  ? 1.0766 0.7369 0.5723 0.4141  -0.1728 -0.0459 90  ASP   B OD1 
997  O OD2 . ASP   B 81  ? 1.1475 0.7592 0.6312 0.4129  -0.2064 -0.0613 90  ASP   B OD2 
998  N N   . GLY   B 82  ? 1.0340 0.7139 0.5395 0.3897  -0.1521 -0.0346 91  GLY   B N   
999  C CA  . GLY   B 82  ? 1.0590 0.7486 0.5413 0.4132  -0.1506 -0.0324 91  GLY   B CA  
1000 C C   . GLY   B 82  ? 1.0924 0.7798 0.5432 0.4514  -0.1604 -0.0361 91  GLY   B C   
1001 O O   . GLY   B 82  ? 1.1071 0.8034 0.5353 0.4752  -0.1606 -0.0349 91  GLY   B O   
1002 N N   . LEU   B 83  ? 1.1018 0.7780 0.5494 0.4593  -0.1693 -0.0411 92  LEU   B N   
1003 C CA  . LEU   B 83  ? 1.1333 0.8041 0.5486 0.4968  -0.1807 -0.0459 92  LEU   B CA  
1004 C C   . LEU   B 83  ? 1.1188 0.8167 0.5467 0.5071  -0.1683 -0.0407 92  LEU   B C   
1005 O O   . LEU   B 83  ? 1.1272 0.8458 0.5381 0.5375  -0.1632 -0.0368 92  LEU   B O   
1006 C CB  . LEU   B 83  ? 1.1759 0.7963 0.5653 0.5021  -0.2108 -0.0599 92  LEU   B CB  
1007 C CG  . LEU   B 83  ? 1.2339 0.8165 0.5922 0.5077  -0.2317 -0.0677 92  LEU   B CG  
1008 C CD1 . LEU   B 83  ? 1.2652 0.7997 0.5981 0.5162  -0.2622 -0.0810 92  LEU   B CD1 
1009 C CD2 . LEU   B 83  ? 1.2526 0.8487 0.5805 0.5423  -0.2299 -0.0664 92  LEU   B CD2 
1010 N N   . SER   B 84  ? 1.0976 0.7933 0.5522 0.4843  -0.1656 -0.0411 93  SER   B N   
1011 C CA  . SER   B 84  ? 1.0779 0.7898 0.5416 0.4934  -0.1587 -0.0386 93  SER   B CA  
1012 C C   . SER   B 84  ? 1.0310 0.7867 0.5232 0.4859  -0.1308 -0.0243 93  SER   B C   
1013 O O   . SER   B 84  ? 1.0147 0.7872 0.5305 0.4630  -0.1159 -0.0171 93  SER   B O   
1014 C CB  . SER   B 84  ? 1.1002 0.7887 0.5781 0.4739  -0.1706 -0.0466 93  SER   B CB  
1015 O OG  . SER   B 84  ? 1.1505 0.7977 0.6121 0.4678  -0.1952 -0.0578 93  SER   B OG  
1016 N N   . GLU   B 85  ? 1.0025 0.7744 0.4920 0.5050  -0.1248 -0.0204 94  GLU   B N   
1017 C CA  . GLU   B 85  ? 0.9625 0.7716 0.4782 0.4981  -0.1004 -0.0067 94  GLU   B CA  
1018 C C   . GLU   B 85  ? 0.9256 0.7304 0.4754 0.4641  -0.0953 -0.0076 94  GLU   B C   
1019 O O   . GLU   B 85  ? 0.9312 0.7081 0.4824 0.4517  -0.1107 -0.0184 94  GLU   B O   
1020 C CB  . GLU   B 85  ? 0.9917 0.8164 0.4922 0.5291  -0.0968 -0.0020 94  GLU   B CB  
1021 C CG  . GLU   B 85  ? 1.0474 0.8913 0.5212 0.5613  -0.0937 0.0040  94  GLU   B CG  
1022 C CD  . GLU   B 85  ? 1.1235 0.9948 0.5880 0.5889  -0.0827 0.0142  94  GLU   B CD  
1023 O OE1 . GLU   B 85  ? 1.1279 0.9949 0.5976 0.5901  -0.0829 0.0133  94  GLU   B OE1 
1024 O OE2 . GLU   B 85  ? 1.1500 1.0488 0.6019 0.6101  -0.0737 0.0236  94  GLU   B OE2 
1025 N N   . VAL   B 86  ? 0.8769 0.7101 0.4543 0.4484  -0.0738 0.0042  95  VAL   B N   
1026 C CA  . VAL   B 86  ? 0.8336 0.6678 0.4432 0.4180  -0.0661 0.0047  95  VAL   B CA  
1027 C C   . VAL   B 86  ? 0.8053 0.6649 0.4304 0.4205  -0.0487 0.0158  95  VAL   B C   
1028 O O   . VAL   B 86  ? 0.8247 0.7035 0.4379 0.4427  -0.0412 0.0248  95  VAL   B O   
1029 C CB  . VAL   B 86  ? 0.8105 0.6500 0.4385 0.3914  -0.0580 0.0077  95  VAL   B CB  
1030 C CG1 . VAL   B 86  ? 0.8277 0.6433 0.4361 0.3921  -0.0740 -0.0010 95  VAL   B CG1 
1031 C CG2 . VAL   B 86  ? 0.7881 0.6607 0.4263 0.3925  -0.0383 0.0218  95  VAL   B CG2 
1032 N N   . GLN   B 87  ? 0.7611 0.6214 0.4123 0.3985  -0.0423 0.0159  96  GLN   B N   
1033 C CA  . GLN   B 87  ? 0.7428 0.6240 0.4092 0.3983  -0.0261 0.0267  96  GLN   B CA  
1034 C C   . GLN   B 87  ? 0.7256 0.6189 0.4216 0.3700  -0.0115 0.0331  96  GLN   B C   
1035 O O   . GLN   B 87  ? 0.7220 0.6033 0.4318 0.3487  -0.0155 0.0256  96  GLN   B O   
1036 C CB  . GLN   B 87  ? 0.7421 0.6128 0.4073 0.4060  -0.0327 0.0211  96  GLN   B CB  
1037 C CG  . GLN   B 87  ? 0.7876 0.6562 0.4229 0.4400  -0.0409 0.0203  96  GLN   B CG  
1038 C CD  . GLN   B 87  ? 0.8239 0.6823 0.4551 0.4507  -0.0484 0.0144  96  GLN   B CD  
1039 O OE1 . GLN   B 87  ? 0.7811 0.6388 0.4334 0.4342  -0.0445 0.0131  96  GLN   B OE1 
1040 N NE2 . GLN   B 87  ? 0.8533 0.7041 0.4554 0.4809  -0.0599 0.0103  96  GLN   B NE2 
1041 N N   . LEU   B 88  ? 0.7088 0.6262 0.4141 0.3702  0.0047  0.0472  97  LEU   B N   
1042 C CA  . LEU   B 88  ? 0.6925 0.6207 0.4249 0.3457  0.0182  0.0540  97  LEU   B CA  
1043 C C   . LEU   B 88  ? 0.6844 0.6108 0.4264 0.3450  0.0224  0.0557  97  LEU   B C   
1044 O O   . LEU   B 88  ? 0.6939 0.6296 0.4266 0.3636  0.0268  0.0638  97  LEU   B O   
1045 C CB  . LEU   B 88  ? 0.6854 0.6400 0.4235 0.3464  0.0323  0.0693  97  LEU   B CB  
1046 C CG  . LEU   B 88  ? 0.6969 0.6619 0.4622 0.3234  0.0458  0.0779  97  LEU   B CG  
1047 C CD1 . LEU   B 88  ? 0.7009 0.6537 0.4813 0.2978  0.0428  0.0684  97  LEU   B CD1 
1048 C CD2 . LEU   B 88  ? 0.6948 0.6872 0.4660 0.3255  0.0585  0.0946  97  LEU   B CD2 
1049 N N   . LEU   B 89  ? 0.6721 0.5878 0.4314 0.3254  0.0212  0.0485  98  LEU   B N   
1050 C CA  . LEU   B 89  ? 0.6755 0.5899 0.4444 0.3245  0.0254  0.0499  98  LEU   B CA  
1051 C C   . LEU   B 89  ? 0.6778 0.6055 0.4655 0.3092  0.0406  0.0617  98  LEU   B C   
1052 O O   . LEU   B 89  ? 0.6733 0.5975 0.4789 0.2879  0.0433  0.0582  98  LEU   B O   
1053 C CB  . LEU   B 89  ? 0.6807 0.5791 0.4578 0.3137  0.0158  0.0360  98  LEU   B CB  
1054 C CG  . LEU   B 89  ? 0.6946 0.5913 0.4824 0.3123  0.0191  0.0354  98  LEU   B CG  
1055 C CD1 . LEU   B 89  ? 0.7220 0.6218 0.4955 0.3357  0.0206  0.0420  98  LEU   B CD1 
1056 C CD2 . LEU   B 89  ? 0.7069 0.5915 0.5003 0.3056  0.0074  0.0212  98  LEU   B CD2 
1057 N N   . ALA   B 90  ? 0.6697 0.6138 0.4529 0.3202  0.0500  0.0764  99  ALA   B N   
1058 C CA  . ALA   B 90  ? 0.6634 0.6210 0.4636 0.3066  0.0635  0.0900  99  ALA   B CA  
1059 C C   . ALA   B 90  ? 0.6492 0.5994 0.4612 0.2990  0.0681  0.0921  99  ALA   B C   
1060 O O   . ALA   B 90  ? 0.6569 0.6037 0.4595 0.3145  0.0674  0.0941  99  ALA   B O   
1061 C CB  . ALA   B 90  ? 0.6694 0.6489 0.4619 0.3210  0.0718  0.1063  99  ALA   B CB  
1062 N N   . VAL   B 91  ? 0.6267 0.5742 0.4579 0.2767  0.0726  0.0922  100 VAL   B N   
1063 C CA  . VAL   B 91  ? 0.6103 0.5492 0.4522 0.2689  0.0768  0.0945  100 VAL   B CA  
1064 C C   . VAL   B 91  ? 0.6126 0.5617 0.4679 0.2557  0.0873  0.1100  100 VAL   B C   
1065 O O   . VAL   B 91  ? 0.5932 0.5390 0.4627 0.2364  0.0884  0.1074  100 VAL   B O   
1066 C CB  . VAL   B 91  ? 0.6015 0.5253 0.4526 0.2560  0.0707  0.0788  100 VAL   B CB  
1067 C CG1 . VAL   B 91  ? 0.5988 0.5128 0.4584 0.2511  0.0741  0.0802  100 VAL   B CG1 
1068 C CG2 . VAL   B 91  ? 0.6030 0.5195 0.4432 0.2668  0.0595  0.0650  100 VAL   B CG2 
1069 N N   . PRO   B 92  ? 0.6259 0.5886 0.4765 0.2661  0.0946  0.1269  101 PRO   B N   
1070 C CA  . PRO   B 92  ? 0.6248 0.5989 0.4899 0.2521  0.1037  0.1432  101 PRO   B CA  
1071 C C   . PRO   B 92  ? 0.6362 0.5944 0.5124 0.2392  0.1061  0.1464  101 PRO   B C   
1072 O O   . PRO   B 92  ? 0.6500 0.5929 0.5197 0.2470  0.1032  0.1408  101 PRO   B O   
1073 C CB  . PRO   B 92  ? 0.6392 0.6344 0.4944 0.2696  0.1107  0.1608  101 PRO   B CB  
1074 C CG  . PRO   B 92  ? 0.6547 0.6484 0.4881 0.2940  0.1042  0.1515  101 PRO   B CG  
1075 C CD  . PRO   B 92  ? 0.6344 0.6035 0.4666 0.2910  0.0948  0.1326  101 PRO   B CD  
1076 N N   . PRO   B 93  ? 0.6346 0.5953 0.5271 0.2199  0.1102  0.1552  102 PRO   B N   
1077 C CA  . PRO   B 93  ? 0.6416 0.5835 0.5429 0.2078  0.1108  0.1581  102 PRO   B CA  
1078 C C   . PRO   B 93  ? 0.6551 0.5928 0.5483 0.2198  0.1152  0.1716  102 PRO   B C   
1079 O O   . PRO   B 93  ? 0.6474 0.6036 0.5369 0.2285  0.1218  0.1883  102 PRO   B O   
1080 C CB  . PRO   B 93  ? 0.6353 0.5845 0.5541 0.1867  0.1137  0.1676  102 PRO   B CB  
1081 C CG  . PRO   B 93  ? 0.6359 0.6016 0.5557 0.1853  0.1120  0.1604  102 PRO   B CG  
1082 C CD  . PRO   B 93  ? 0.6197 0.5993 0.5229 0.2083  0.1132  0.1619  102 PRO   B CD  
1083 N N   . GLY   B 94  ? 0.6670 0.5818 0.5561 0.2222  0.1114  0.1639  103 GLY   B N   
1084 C CA  . GLY   B 94  ? 0.6781 0.5841 0.5577 0.2341  0.1143  0.1745  103 GLY   B CA  
1085 C C   . GLY   B 94  ? 0.6820 0.5994 0.5439 0.2592  0.1156  0.1768  103 GLY   B C   
1086 O O   . GLY   B 94  ? 0.6924 0.6066 0.5448 0.2709  0.1193  0.1884  103 GLY   B O   
1087 N N   . GLU   B 95  ? 0.6821 0.6114 0.5378 0.2683  0.1118  0.1657  104 GLU   B N   
1088 C CA  . GLU   B 95  ? 0.6967 0.6360 0.5337 0.2932  0.1111  0.1663  104 GLU   B CA  
1089 C C   . GLU   B 95  ? 0.7125 0.6418 0.5409 0.3027  0.1004  0.1443  104 GLU   B C   
1090 O O   . GLU   B 95  ? 0.7049 0.6276 0.5427 0.2892  0.0949  0.1301  104 GLU   B O   
1091 C CB  . GLU   B 95  ? 0.7068 0.6732 0.5413 0.2988  0.1166  0.1780  104 GLU   B CB  
1092 C CG  . GLU   B 95  ? 0.7421 0.7237 0.5867 0.2898  0.1277  0.2023  104 GLU   B CG  
1093 C CD  . GLU   B 95  ? 0.7885 0.8014 0.6342 0.2933  0.1338  0.2145  104 GLU   B CD  
1094 O OE1 . GLU   B 95  ? 0.7902 0.8110 0.6272 0.3033  0.1288  0.2029  104 GLU   B OE1 
1095 O OE2 . GLU   B 95  ? 0.7860 0.8160 0.6412 0.2863  0.1433  0.2361  104 GLU   B OE2 
1096 N N   . ARG   B 96  ? 0.7242 0.6524 0.5346 0.3258  0.0969  0.1420  105 ARG   B N   
1097 C CA  . ARG   B 96  ? 0.7467 0.6653 0.5487 0.3358  0.0853  0.1221  105 ARG   B CA  
1098 C C   . ARG   B 96  ? 0.7397 0.6662 0.5400 0.3347  0.0793  0.1126  105 ARG   B C   
1099 O O   . ARG   B 96  ? 0.7390 0.6815 0.5354 0.3384  0.0839  0.1224  105 ARG   B O   
1100 C CB  . ARG   B 96  ? 0.7953 0.7126 0.5768 0.3627  0.0824  0.1235  105 ARG   B CB  
1101 C CG  . ARG   B 96  ? 0.8734 0.7773 0.6488 0.3715  0.0694  0.1035  105 ARG   B CG  
1102 C CD  . ARG   B 96  ? 0.9400 0.8361 0.7012 0.3920  0.0675  0.1048  105 ARG   B CD  
1103 N NE  . ARG   B 96  ? 1.0033 0.9100 0.7456 0.4136  0.0727  0.1192  105 ARG   B NE  
1104 C CZ  . ARG   B 96  ? 1.0515 0.9598 0.7888 0.4201  0.0825  0.1367  105 ARG   B CZ  
1105 N NH1 . ARG   B 96  ? 1.0427 0.9392 0.7914 0.4065  0.0871  0.1413  105 ARG   B NH1 
1106 N NH2 . ARG   B 96  ? 1.0562 0.9775 0.7758 0.4408  0.0876  0.1501  105 ARG   B NH2 
1107 N N   . ALA   B 97  ? 0.7323 0.6481 0.5349 0.3304  0.0687  0.0938  106 ALA   B N   
1108 C CA  . ALA   B 97  ? 0.7270 0.6453 0.5256 0.3300  0.0606  0.0833  106 ALA   B CA  
1109 C C   . ALA   B 97  ? 0.7399 0.6644 0.5157 0.3558  0.0565  0.0860  106 ALA   B C   
1110 O O   . ALA   B 97  ? 0.7460 0.6654 0.5094 0.3738  0.0531  0.0850  106 ALA   B O   
1111 C CB  . ALA   B 97  ? 0.7195 0.6251 0.5232 0.3236  0.0495  0.0649  106 ALA   B CB  
1112 N N   . LYS   B 98  ? 0.7422 0.6775 0.5113 0.3591  0.0568  0.0894  107 LYS   B N   
1113 C CA  . LYS   B 98  ? 0.7696 0.7121 0.5153 0.3852  0.0533  0.0924  107 LYS   B CA  
1114 C C   . LYS   B 98  ? 0.7683 0.7086 0.5054 0.3866  0.0433  0.0822  107 LYS   B C   
1115 O O   . LYS   B 98  ? 0.7642 0.7099 0.5131 0.3693  0.0468  0.0834  107 LYS   B O   
1116 C CB  . LYS   B 98  ? 0.8064 0.7707 0.5510 0.3915  0.0677  0.1136  107 LYS   B CB  
1117 C CG  . LYS   B 98  ? 0.9045 0.8823 0.6247 0.4204  0.0673  0.1202  107 LYS   B CG  
1118 C CD  . LYS   B 98  ? 0.9725 0.9776 0.6969 0.4220  0.0834  0.1432  107 LYS   B CD  
1119 C CE  . LYS   B 98  ? 1.0201 1.0364 0.7675 0.3959  0.0907  0.1493  107 LYS   B CE  
1120 N NZ  . LYS   B 98  ? 1.0455 1.0920 0.7901 0.4039  0.0999  0.1653  107 LYS   B NZ  
1121 N N   . ASN   B 99  ? 0.7683 0.6981 0.4844 0.4064  0.0296  0.0715  108 ASN   B N   
1122 C CA  . ASN   B 99  ? 0.7829 0.7064 0.4868 0.4101  0.0181  0.0618  108 ASN   B CA  
1123 C C   . ASN   B 99  ? 0.7899 0.7303 0.4755 0.4305  0.0222  0.0719  108 ASN   B C   
1124 O O   . ASN   B 99  ? 0.7943 0.7410 0.4618 0.4556  0.0230  0.0776  108 ASN   B O   
1125 C CB  . ASN   B 99  ? 0.8107 0.7127 0.4989 0.4225  -0.0009 0.0453  108 ASN   B CB  
1126 C CG  . ASN   B 99  ? 0.8506 0.7383 0.5564 0.4035  -0.0071 0.0340  108 ASN   B CG  
1127 O OD1 . ASN   B 99  ? 0.8606 0.7505 0.5782 0.3993  -0.0006 0.0369  108 ASN   B OD1 
1128 N ND2 . ASN   B 99  ? 0.8630 0.7361 0.5701 0.3928  -0.0204 0.0211  108 ASN   B ND2 
1129 N N   . ILE   B 100 ? 0.7802 0.7282 0.4682 0.4223  0.0240  0.0735  109 ILE   B N   
1130 C CA  . ILE   B 100 ? 0.7913 0.7579 0.4622 0.4422  0.0273  0.0822  109 ILE   B CA  
1131 C C   . ILE   B 100 ? 0.8052 0.7569 0.4587 0.4484  0.0119  0.0688  109 ILE   B C   
1132 O O   . ILE   B 100 ? 0.8027 0.7458 0.4683 0.4271  0.0089  0.0625  109 ILE   B O   
1133 C CB  . ILE   B 100 ? 0.7958 0.7897 0.4857 0.4283  0.0447  0.0991  109 ILE   B CB  
1134 C CG1 . ILE   B 100 ? 0.8088 0.8128 0.5164 0.4191  0.0585  0.1126  109 ILE   B CG1 
1135 C CG2 . ILE   B 100 ? 0.8036 0.8214 0.4761 0.4508  0.0483  0.1085  109 ILE   B CG2 
1136 C CD1 . ILE   B 100 ? 0.8289 0.8418 0.5195 0.4457  0.0622  0.1220  109 ILE   B CD1 
1137 N N   . GLN   B 101 ? 0.8146 0.7618 0.4383 0.4784  0.0015  0.0645  110 GLN   B N   
1138 C CA  . GLN   B 101 ? 0.8324 0.7607 0.4351 0.4874  -0.0157 0.0512  110 GLN   B CA  
1139 C C   . GLN   B 101 ? 0.8416 0.7903 0.4345 0.4978  -0.0102 0.0589  110 GLN   B C   
1140 O O   . GLN   B 101 ? 0.8476 0.8249 0.4362 0.5142  0.0022  0.0731  110 GLN   B O   
1141 C CB  . GLN   B 101 ? 0.8770 0.7857 0.4505 0.5154  -0.0328 0.0404  110 GLN   B CB  
1142 C CG  . GLN   B 101 ? 0.9017 0.7844 0.4505 0.5256  -0.0541 0.0255  110 GLN   B CG  
1143 C CD  . GLN   B 101 ? 0.9565 0.8125 0.4835 0.5443  -0.0739 0.0120  110 GLN   B CD  
1144 O OE1 . GLN   B 101 ? 0.9454 0.7950 0.4842 0.5373  -0.0748 0.0092  110 GLN   B OE1 
1145 N NE2 . GLN   B 101 ? 1.0106 0.8503 0.5046 0.5694  -0.0910 0.0030  110 GLN   B NE2 
1146 N N   . THR   B 102 ? 0.8341 0.7700 0.4247 0.4875  -0.0189 0.0506  111 THR   B N   
1147 C CA  . THR   B 102 ? 0.8337 0.7878 0.4158 0.4959  -0.0150 0.0562  111 THR   B CA  
1148 C C   . THR   B 102 ? 0.8600 0.7867 0.4240 0.4965  -0.0331 0.0418  111 THR   B C   
1149 O O   . THR   B 102 ? 0.8879 0.7846 0.4560 0.4798  -0.0452 0.0297  111 THR   B O   
1150 C CB  . THR   B 102 ? 0.8301 0.8125 0.4437 0.4713  0.0045  0.0702  111 THR   B CB  
1151 O OG1 . THR   B 102 ? 0.8382 0.8481 0.4436 0.4852  0.0109  0.0792  111 THR   B OG1 
1152 C CG2 . THR   B 102 ? 0.8315 0.7965 0.4679 0.4367  0.0026  0.0628  111 THR   B CG2 
1153 N N   . LEU   B 103 ? 0.8504 0.7880 0.3947 0.5154  -0.0350 0.0435  112 LEU   B N   
1154 C CA  . LEU   B 103 ? 0.8633 0.7746 0.3900 0.5152  -0.0515 0.0311  112 LEU   B CA  
1155 C C   . LEU   B 103 ? 0.8498 0.7786 0.3993 0.4914  -0.0395 0.0379  112 LEU   B C   
1156 O O   . LEU   B 103 ? 0.8339 0.7982 0.3884 0.4989  -0.0257 0.0503  112 LEU   B O   
1157 C CB  . LEU   B 103 ? 0.8922 0.7998 0.3786 0.5532  -0.0640 0.0265  112 LEU   B CB  
1158 C CG  . LEU   B 103 ? 0.9469 0.8253 0.4154 0.5510  -0.0810 0.0145  112 LEU   B CG  
1159 C CD1 . LEU   B 103 ? 0.9733 0.8047 0.4340 0.5402  -0.1020 -0.0009 112 LEU   B CD1 
1160 C CD2 . LEU   B 103 ? 0.9837 0.8680 0.4169 0.5864  -0.0885 0.0130  112 LEU   B CD2 
1161 N N   . PRO   B 104 ? 0.8475 0.7529 0.4102 0.4634  -0.0452 0.0301  113 PRO   B N   
1162 C CA  . PRO   B 104 ? 0.8360 0.7573 0.4195 0.4414  -0.0343 0.0359  113 PRO   B CA  
1163 C C   . PRO   B 104 ? 0.8564 0.7847 0.4191 0.4581  -0.0386 0.0356  113 PRO   B C   
1164 O O   . PRO   B 104 ? 0.8864 0.7910 0.4175 0.4784  -0.0556 0.0257  113 PRO   B O   
1165 C CB  . PRO   B 104 ? 0.8475 0.7380 0.4429 0.4124  -0.0424 0.0259  113 PRO   B CB  
1166 C CG  . PRO   B 104 ? 0.8575 0.7264 0.4512 0.4130  -0.0513 0.0189  113 PRO   B CG  
1167 C CD  . PRO   B 104 ? 0.8539 0.7214 0.4161 0.4493  -0.0604 0.0171  113 PRO   B CD  
1168 N N   . GLY   B 105 ? 0.8391 0.7987 0.4202 0.4486  -0.0240 0.0460  114 GLY   B N   
1169 C CA  . GLY   B 105 ? 0.8362 0.8051 0.4050 0.4570  -0.0262 0.0459  114 GLY   B CA  
1170 C C   . GLY   B 105 ? 0.8423 0.7854 0.4186 0.4306  -0.0326 0.0376  114 GLY   B C   
1171 O O   . GLY   B 105 ? 0.8424 0.7564 0.4254 0.4121  -0.0391 0.0301  114 GLY   B O   
1172 N N   . ILE   B 106 ? 0.8407 0.7962 0.4168 0.4283  -0.0303 0.0394  115 ILE   B N   
1173 C CA  . ILE   B 106 ? 0.8607 0.7927 0.4401 0.4062  -0.0364 0.0322  115 ILE   B CA  
1174 C C   . ILE   B 106 ? 0.8443 0.8060 0.4457 0.3914  -0.0234 0.0399  115 ILE   B C   
1175 O O   . ILE   B 106 ? 0.8575 0.8504 0.4554 0.4076  -0.0178 0.0469  115 ILE   B O   
1176 C CB  . ILE   B 106 ? 0.9106 0.8099 0.4513 0.4255  -0.0567 0.0208  115 ILE   B CB  
1177 C CG1 . ILE   B 106 ? 0.9616 0.8231 0.4806 0.4356  -0.0736 0.0109  115 ILE   B CG1 
1178 C CG2 . ILE   B 106 ? 0.9286 0.8091 0.4684 0.4075  -0.0621 0.0157  115 ILE   B CG2 
1179 C CD1 . ILE   B 106 ? 1.0189 0.8485 0.4970 0.4587  -0.0947 0.0006  115 ILE   B CD1 
1180 N N   . PHE   B 107 ? 0.8132 0.7650 0.4356 0.3617  -0.0200 0.0381  116 PHE   B N   
1181 C CA  . PHE   B 107 ? 0.7919 0.7629 0.4324 0.3455  -0.0114 0.0423  116 PHE   B CA  
1182 C C   . PHE   B 107 ? 0.8209 0.7632 0.4383 0.3464  -0.0250 0.0326  116 PHE   B C   
1183 O O   . PHE   B 107 ? 0.8400 0.7473 0.4518 0.3338  -0.0341 0.0246  116 PHE   B O   
1184 C CB  . PHE   B 107 ? 0.7704 0.7401 0.4423 0.3139  -0.0023 0.0439  116 PHE   B CB  
1185 C CG  . PHE   B 107 ? 0.7493 0.7500 0.4499 0.3059  0.0131  0.0552  116 PHE   B CG  
1186 C CD1 . PHE   B 107 ? 0.7418 0.7713 0.4411 0.3254  0.0194  0.0649  116 PHE   B CD1 
1187 C CD2 . PHE   B 107 ? 0.7428 0.7431 0.4704 0.2794  0.0209  0.0565  116 PHE   B CD2 
1188 C CE1 . PHE   B 107 ? 0.7343 0.7901 0.4596 0.3166  0.0331  0.0767  116 PHE   B CE1 
1189 C CE2 . PHE   B 107 ? 0.7304 0.7551 0.4826 0.2717  0.0335  0.0669  116 PHE   B CE2 
1190 C CZ  . PHE   B 107 ? 0.7219 0.7734 0.4733 0.2894  0.0395  0.0774  116 PHE   B CZ  
1191 N N   . LYS   B 108 ? 0.8214 0.7788 0.4265 0.3602  -0.0264 0.0337  117 LYS   B N   
1192 C CA  . LYS   B 108 ? 0.8432 0.7734 0.4252 0.3617  -0.0392 0.0251  117 LYS   B CA  
1193 C C   . LYS   B 108 ? 0.8234 0.7652 0.4274 0.3379  -0.0309 0.0273  117 LYS   B C   
1194 O O   . LYS   B 108 ? 0.8033 0.7829 0.4251 0.3377  -0.0199 0.0351  117 LYS   B O   
1195 C CB  . LYS   B 108 ? 0.8962 0.8345 0.4475 0.3945  -0.0472 0.0239  117 LYS   B CB  
1196 C CG  . LYS   B 108 ? 0.9945 0.9245 0.5218 0.4223  -0.0554 0.0217  117 LYS   B CG  
1197 C CD  . LYS   B 108 ? 1.0961 1.0351 0.5905 0.4581  -0.0637 0.0198  117 LYS   B CD  
1198 C CE  . LYS   B 108 ? 1.1947 1.1208 0.6622 0.4866  -0.0737 0.0161  117 LYS   B CE  
1199 N NZ  . LYS   B 108 ? 1.2452 1.1895 0.6827 0.5252  -0.0788 0.0160  117 LYS   B NZ  
1200 N N   . THR   B 109 ? 0.8265 0.7376 0.4304 0.3174  -0.0361 0.0211  118 THR   B N   
1201 C CA  . THR   B 109 ? 0.8257 0.7450 0.4480 0.2956  -0.0291 0.0222  118 THR   B CA  
1202 C C   . THR   B 109 ? 0.8574 0.7463 0.4542 0.2957  -0.0415 0.0148  118 THR   B C   
1203 O O   . THR   B 109 ? 0.8778 0.7353 0.4455 0.3087  -0.0557 0.0090  118 THR   B O   
1204 C CB  . THR   B 109 ? 0.8250 0.7408 0.4763 0.2674  -0.0204 0.0233  118 THR   B CB  
1205 O OG1 . THR   B 109 ? 0.8483 0.7264 0.4890 0.2552  -0.0293 0.0163  118 THR   B OG1 
1206 C CG2 . THR   B 109 ? 0.8073 0.7392 0.4765 0.2681  -0.0121 0.0288  118 THR   B CG2 
1207 N N   A LYS   B 110 ? 0.8540 0.7506 0.4609 0.2816  -0.0369 0.0151  119 LYS   B N   
1208 N N   B LYS   B 110 ? 0.8540 0.7506 0.4609 0.2816  -0.0369 0.0151  119 LYS   B N   
1209 N N   C LYS   B 110 ? 0.8541 0.7507 0.4611 0.2815  -0.0369 0.0151  119 LYS   B N   
1210 N N   D LYS   B 110 ? 0.8541 0.7507 0.4611 0.2815  -0.0369 0.0151  119 LYS   B N   
1211 C CA  A LYS   B 110 ? 0.8789 0.7471 0.4624 0.2805  -0.0475 0.0092  119 LYS   B CA  
1212 C CA  B LYS   B 110 ? 0.8789 0.7471 0.4624 0.2805  -0.0475 0.0092  119 LYS   B CA  
1213 C CA  C LYS   B 110 ? 0.8787 0.7474 0.4628 0.2800  -0.0472 0.0093  119 LYS   B CA  
1214 C CA  D LYS   B 110 ? 0.8787 0.7474 0.4628 0.2800  -0.0472 0.0093  119 LYS   B CA  
1215 C C   A LYS   B 110 ? 0.9041 0.7310 0.4800 0.2641  -0.0550 0.0048  119 LYS   B C   
1216 C C   B LYS   B 110 ? 0.9041 0.7310 0.4800 0.2641  -0.0550 0.0048  119 LYS   B C   
1217 C C   C LYS   B 110 ? 0.9041 0.7312 0.4802 0.2641  -0.0550 0.0048  119 LYS   B C   
1218 C C   D LYS   B 110 ? 0.9041 0.7312 0.4802 0.2641  -0.0550 0.0048  119 LYS   B C   
1219 O O   A LYS   B 110 ? 0.9284 0.7245 0.4793 0.2656  -0.0666 0.0005  119 LYS   B O   
1220 O O   B LYS   B 110 ? 0.9284 0.7245 0.4793 0.2656  -0.0666 0.0005  119 LYS   B O   
1221 O O   C LYS   B 110 ? 0.9284 0.7247 0.4793 0.2658  -0.0666 0.0005  119 LYS   B O   
1222 O O   D LYS   B 110 ? 0.9284 0.7247 0.4793 0.2658  -0.0666 0.0005  119 LYS   B O   
1223 C CB  A LYS   B 110 ? 0.8853 0.7734 0.4824 0.2694  -0.0403 0.0108  119 LYS   B CB  
1224 C CB  B LYS   B 110 ? 0.8853 0.7734 0.4824 0.2694  -0.0403 0.0108  119 LYS   B CB  
1225 C CB  C LYS   B 110 ? 0.8847 0.7731 0.4842 0.2672  -0.0394 0.0109  119 LYS   B CB  
1226 C CB  D LYS   B 110 ? 0.8847 0.7731 0.4842 0.2672  -0.0394 0.0109  119 LYS   B CB  
1227 C CG  A LYS   B 110 ? 0.9187 0.8110 0.5450 0.2413  -0.0299 0.0123  119 LYS   B CG  
1228 C CG  B LYS   B 110 ? 0.9187 0.8110 0.5450 0.2413  -0.0299 0.0123  119 LYS   B CG  
1229 C CG  C LYS   B 110 ? 0.9168 0.8125 0.5478 0.2400  -0.0282 0.0131  119 LYS   B CG  
1230 C CG  D LYS   B 110 ? 0.9168 0.8125 0.5478 0.2400  -0.0282 0.0131  119 LYS   B CG  
1231 C CD  A LYS   B 110 ? 0.9607 0.8701 0.5972 0.2323  -0.0250 0.0126  119 LYS   B CD  
1232 C CD  B LYS   B 110 ? 0.9607 0.8701 0.5972 0.2323  -0.0250 0.0126  119 LYS   B CD  
1233 C CD  C LYS   B 110 ? 0.9605 0.8698 0.6028 0.2279  -0.0231 0.0130  119 LYS   B CD  
1234 C CD  D LYS   B 110 ? 0.9605 0.8698 0.6028 0.2279  -0.0231 0.0130  119 LYS   B CD  
1235 C CE  A LYS   B 110 ? 1.0064 0.9009 0.6544 0.2079  -0.0213 0.0104  119 LYS   B CE  
1236 C CE  B LYS   B 110 ? 1.0064 0.9009 0.6544 0.2079  -0.0213 0.0104  119 LYS   B CE  
1237 C CE  C LYS   B 110 ? 0.9959 0.9070 0.6648 0.2029  -0.0139 0.0137  119 LYS   B CE  
1238 C CE  D LYS   B 110 ? 0.9959 0.9070 0.6648 0.2029  -0.0139 0.0137  119 LYS   B CE  
1239 N NZ  A LYS   B 110 ? 1.0225 0.9245 0.6973 0.1927  -0.0121 0.0129  119 LYS   B NZ  
1240 N NZ  B LYS   B 110 ? 1.0225 0.9245 0.6973 0.1927  -0.0121 0.0129  119 LYS   B NZ  
1241 N NZ  C LYS   B 110 ? 1.0193 0.9431 0.6985 0.1922  -0.0099 0.0128  119 LYS   B NZ  
1242 N NZ  D LYS   B 110 ? 1.0193 0.9431 0.6985 0.1922  -0.0099 0.0128  119 LYS   B NZ  
1243 N N   . ASP   B 111 ? 0.8964 0.7234 0.4937 0.2489  -0.0488 0.0063  120 ASP   B N   
1244 C CA  . ASP   B 111 ? 0.9198 0.7142 0.5144 0.2328  -0.0549 0.0032  120 ASP   B CA  
1245 C C   . ASP   B 111 ? 0.9364 0.7134 0.5219 0.2421  -0.0636 0.0012  120 ASP   B C   
1246 O O   . ASP   B 111 ? 0.9496 0.7088 0.5422 0.2267  -0.0660 -0.0001 120 ASP   B O   
1247 C CB  . ASP   B 111 ? 0.9254 0.7327 0.5515 0.2075  -0.0419 0.0057  120 ASP   B CB  
1248 C CG  . ASP   B 111 ? 0.9757 0.7959 0.6101 0.1969  -0.0348 0.0066  120 ASP   B CG  
1249 O OD1 . ASP   B 111 ? 0.9952 0.7987 0.6082 0.2001  -0.0425 0.0043  120 ASP   B OD1 
1250 O OD2 . ASP   B 111 ? 0.9854 0.8303 0.6464 0.1857  -0.0226 0.0093  120 ASP   B OD2 
1251 N N   . GLY   B 112 ? 0.9321 0.7168 0.5032 0.2671  -0.0680 0.0009  121 GLY   B N   
1252 C CA  . GLY   B 112 ? 0.9434 0.7115 0.5034 0.2786  -0.0774 -0.0019 121 GLY   B CA  
1253 C C   . GLY   B 112 ? 0.9264 0.7241 0.5004 0.2908  -0.0682 0.0022  121 GLY   B C   
1254 O O   . GLY   B 112 ? 0.9117 0.7439 0.5106 0.2849  -0.0528 0.0085  121 GLY   B O   
1255 N N   . ASP   B 113 ? 0.9242 0.7070 0.4814 0.3079  -0.0786 -0.0011 122 ASP   B N   
1256 C CA  . ASP   B 113 ? 0.9096 0.7167 0.4747 0.3226  -0.0717 0.0028  122 ASP   B CA  
1257 C C   . ASP   B 113 ? 0.8912 0.7002 0.4824 0.3045  -0.0647 0.0042  122 ASP   B C   
1258 O O   . ASP   B 113 ? 0.8971 0.6800 0.4905 0.2881  -0.0718 -0.0003 122 ASP   B O   
1259 C CB  . ASP   B 113 ? 0.9540 0.7441 0.4855 0.3529  -0.0870 -0.0023 122 ASP   B CB  
1260 C CG  . ASP   B 113 ? 1.0398 0.8344 0.5441 0.3776  -0.0930 -0.0033 122 ASP   B CG  
1261 O OD1 . ASP   B 113 ? 1.0442 0.8566 0.5567 0.3706  -0.0850 0.0002  122 ASP   B OD1 
1262 O OD2 . ASP   B 113 ? 1.1023 0.8830 0.5762 0.4052  -0.1061 -0.0080 122 ASP   B OD2 
1263 N N   . ILE   B 114 ? 0.8597 0.7006 0.4703 0.3081  -0.0510 0.0111  123 ILE   B N   
1264 C CA  . ILE   B 114 ? 0.8432 0.6898 0.4777 0.2947  -0.0433 0.0131  123 ILE   B CA  
1265 C C   . ILE   B 114 ? 0.8126 0.6761 0.4425 0.3174  -0.0405 0.0172  123 ILE   B C   
1266 O O   . ILE   B 114 ? 0.7995 0.6878 0.4240 0.3345  -0.0350 0.0232  123 ILE   B O   
1267 C CB  . ILE   B 114 ? 0.8389 0.7103 0.5060 0.2720  -0.0263 0.0195  123 ILE   B CB  
1268 C CG1 . ILE   B 114 ? 0.8669 0.7298 0.5363 0.2545  -0.0268 0.0170  123 ILE   B CG1 
1269 C CG2 . ILE   B 114 ? 0.8393 0.7118 0.5289 0.2576  -0.0198 0.0203  123 ILE   B CG2 
1270 C CD1 . ILE   B 114 ? 0.8713 0.7589 0.5703 0.2348  -0.0113 0.0225  123 ILE   B CD1 
1271 N N   . GLY   B 115 ? 0.7930 0.6458 0.4260 0.3177  -0.0437 0.0147  124 GLY   B N   
1272 C CA  . GLY   B 115 ? 0.7808 0.6500 0.4103 0.3384  -0.0400 0.0193  124 GLY   B CA  
1273 C C   . GLY   B 115 ? 0.7465 0.6524 0.4033 0.3308  -0.0203 0.0310  124 GLY   B C   
1274 O O   . GLY   B 115 ? 0.7252 0.6379 0.4060 0.3067  -0.0113 0.0334  124 GLY   B O   
1275 N N   . ALA   B 116 ? 0.7387 0.6686 0.3913 0.3513  -0.0140 0.0390  125 ALA   B N   
1276 C CA  . ALA   B 116 ? 0.7277 0.6923 0.4053 0.3447  0.0038  0.0520  125 ALA   B CA  
1277 C C   . ALA   B 116 ? 0.7424 0.7201 0.4167 0.3629  0.0084  0.0587  125 ALA   B C   
1278 O O   . ALA   B 116 ? 0.7563 0.7294 0.4046 0.3893  0.0000  0.0560  125 ALA   B O   
1279 C CB  . ALA   B 116 ? 0.7150 0.7075 0.3947 0.3486  0.0107  0.0595  125 ALA   B CB  
1280 N N   . VAL   B 117 ? 0.7288 0.7210 0.4274 0.3502  0.0209  0.0672  126 VAL   B N   
1281 C CA  . VAL   B 117 ? 0.7503 0.7545 0.4471 0.3656  0.0264  0.0748  126 VAL   B CA  
1282 C C   . VAL   B 117 ? 0.7461 0.7901 0.4589 0.3670  0.0429  0.0927  126 VAL   B C   
1283 O O   . VAL   B 117 ? 0.7273 0.7831 0.4664 0.3440  0.0527  0.0993  126 VAL   B O   
1284 C CB  . VAL   B 117 ? 0.7620 0.7453 0.4706 0.3514  0.0248  0.0693  126 VAL   B CB  
1285 C CG1 . VAL   B 117 ? 0.7743 0.7736 0.4931 0.3561  0.0357  0.0804  126 VAL   B CG1 
1286 C CG2 . VAL   B 117 ? 0.7806 0.7311 0.4675 0.3607  0.0073  0.0545  126 VAL   B CG2 
1287 N N   . ALA   B 118 ? 0.7497 0.8150 0.4460 0.3945  0.0453  0.1007  127 ALA   B N   
1288 C CA  . ALA   B 118 ? 0.7472 0.8535 0.4583 0.3966  0.0608  0.1194  127 ALA   B CA  
1289 C C   . ALA   B 118 ? 0.7659 0.8808 0.4853 0.3992  0.0700  0.1303  127 ALA   B C   
1290 O O   . ALA   B 118 ? 0.7655 0.8955 0.4687 0.4249  0.0725  0.1376  127 ALA   B O   
1291 C CB  . ALA   B 118 ? 0.7489 0.8802 0.4392 0.4245  0.0599  0.1238  127 ALA   B CB  
1292 N N   . LEU   B 119 ? 0.7690 0.8706 0.5108 0.3740  0.0739  0.1302  128 LEU   B N   
1293 C CA  . LEU   B 119 ? 0.7729 0.8787 0.5235 0.3737  0.0822  0.1403  128 LEU   B CA  
1294 C C   . LEU   B 119 ? 0.7807 0.8984 0.5636 0.3451  0.0935  0.1513  128 LEU   B C   
1295 O O   . LEU   B 119 ? 0.7890 0.8928 0.5856 0.3224  0.0904  0.1429  128 LEU   B O   
1296 C CB  . LEU   B 119 ? 0.7864 0.8572 0.5280 0.3746  0.0725  0.1264  128 LEU   B CB  
1297 C CG  . LEU   B 119 ? 0.8109 0.8641 0.5206 0.4013  0.0584  0.1139  128 LEU   B CG  
1298 C CD1 . LEU   B 119 ? 0.8219 0.8406 0.5294 0.3946  0.0475  0.0989  128 LEU   B CD1 
1299 C CD2 . LEU   B 119 ? 0.8207 0.8941 0.5113 0.4323  0.0625  0.1245  128 LEU   B CD2 
1300 N N   . ASP   B 120 ? 0.7756 0.9188 0.5699 0.3461  0.1059  0.1704  129 ASP   B N   
1301 C CA  . ASP   B 120 ? 0.7680 0.9215 0.5923 0.3189  0.1151  0.1819  129 ASP   B CA  
1302 C C   . ASP   B 120 ? 0.7472 0.8816 0.5820 0.3068  0.1180  0.1842  129 ASP   B C   
1303 O O   . ASP   B 120 ? 0.7594 0.8971 0.5861 0.3209  0.1223  0.1930  129 ASP   B O   
1304 C CB  . ASP   B 120 ? 0.7999 0.9966 0.6356 0.3215  0.1268  0.2035  129 ASP   B CB  
1305 C CG  . ASP   B 120 ? 0.8803 1.0896 0.7434 0.2943  0.1303  0.2089  129 ASP   B CG  
1306 O OD1 . ASP   B 120 ? 0.9000 1.0833 0.7748 0.2722  0.1256  0.1981  129 ASP   B OD1 
1307 O OD2 . ASP   B 120 ? 0.9102 1.1564 0.7830 0.2959  0.1375  0.2237  129 ASP   B OD2 
1308 N N   . TYR   B 121 ? 0.7179 0.8326 0.5696 0.2817  0.1155  0.1765  130 TYR   B N   
1309 C CA  . TYR   B 121 ? 0.7012 0.7954 0.5626 0.2694  0.1170  0.1768  130 TYR   B CA  
1310 C C   . TYR   B 121 ? 0.6717 0.7646 0.5589 0.2409  0.1203  0.1813  130 TYR   B C   
1311 O O   . TYR   B 121 ? 0.6706 0.7702 0.5663 0.2293  0.1183  0.1774  130 TYR   B O   
1312 C CB  . TYR   B 121 ? 0.7201 0.7820 0.5695 0.2724  0.1064  0.1563  130 TYR   B CB  
1313 C CG  . TYR   B 121 ? 0.7408 0.7978 0.5677 0.2984  0.1031  0.1540  130 TYR   B CG  
1314 C CD1 . TYR   B 121 ? 0.7559 0.8085 0.5813 0.3047  0.1074  0.1617  130 TYR   B CD1 
1315 C CD2 . TYR   B 121 ? 0.7588 0.8150 0.5641 0.3178  0.0948  0.1445  130 TYR   B CD2 
1316 C CE1 . TYR   B 121 ? 0.7806 0.8294 0.5844 0.3299  0.1038  0.1595  130 TYR   B CE1 
1317 C CE2 . TYR   B 121 ? 0.7850 0.8358 0.5682 0.3428  0.0903  0.1418  130 TYR   B CE2 
1318 C CZ  . TYR   B 121 ? 0.8069 0.8552 0.5896 0.3491  0.0951  0.1494  130 TYR   B CZ  
1319 O OH  . TYR   B 121 ? 0.8564 0.8991 0.6165 0.3748  0.0900  0.1461  130 TYR   B OH  
1320 N N   . PRO   B 122 ? 0.6566 0.7372 0.5550 0.2293  0.1237  0.1878  131 PRO   B N   
1321 C CA  . PRO   B 122 ? 0.6424 0.7167 0.5631 0.2026  0.1243  0.1899  131 PRO   B CA  
1322 C C   . PRO   B 122 ? 0.6334 0.6885 0.5556 0.1908  0.1159  0.1696  131 PRO   B C   
1323 O O   . PRO   B 122 ? 0.6409 0.6811 0.5487 0.2006  0.1096  0.1542  131 PRO   B O   
1324 C CB  . PRO   B 122 ? 0.6589 0.7148 0.5835 0.1977  0.1265  0.1958  131 PRO   B CB  
1325 C CG  . PRO   B 122 ? 0.6712 0.7373 0.5804 0.2208  0.1314  0.2059  131 PRO   B CG  
1326 C CD  . PRO   B 122 ? 0.6603 0.7307 0.5501 0.2407  0.1262  0.1931  131 PRO   B CD  
1327 N N   . ALA   B 123 ? 0.6147 0.6719 0.5540 0.1703  0.1153  0.1702  132 ALA   B N   
1328 C CA  . ALA   B 123 ? 0.6112 0.6527 0.5517 0.1594  0.1082  0.1526  132 ALA   B CA  
1329 C C   . ALA   B 123 ? 0.6067 0.6181 0.5420 0.1576  0.1032  0.1377  132 ALA   B C   
1330 O O   . ALA   B 123 ? 0.6117 0.6120 0.5396 0.1580  0.0974  0.1221  132 ALA   B O   
1331 C CB  . ALA   B 123 ? 0.6092 0.6564 0.5690 0.1381  0.1082  0.1566  132 ALA   B CB  
1332 N N   . GLY   B 124 ? 0.5918 0.5917 0.5298 0.1569  0.1055  0.1433  133 GLY   B N   
1333 C CA  . GLY   B 124 ? 0.5816 0.5561 0.5149 0.1575  0.1013  0.1307  133 GLY   B CA  
1334 C C   . GLY   B 124 ? 0.5602 0.5297 0.4767 0.1751  0.0977  0.1203  133 GLY   B C   
1335 O O   . GLY   B 124 ? 0.5600 0.5116 0.4736 0.1758  0.0937  0.1089  133 GLY   B O   
1336 N N   . THR   B 125 ? 0.5312 0.5164 0.4364 0.1900  0.0980  0.1236  134 THR   B N   
1337 C CA  . THR   B 125 ? 0.5412 0.5207 0.4288 0.2071  0.0922  0.1132  134 THR   B CA  
1338 C C   . THR   B 125 ? 0.5396 0.5129 0.4236 0.2019  0.0849  0.0982  134 THR   B C   
1339 O O   . THR   B 125 ? 0.5519 0.5165 0.4232 0.2120  0.0781  0.0881  134 THR   B O   
1340 C CB  . THR   B 125 ? 0.5641 0.5617 0.4381 0.2279  0.0949  0.1239  134 THR   B CB  
1341 O OG1 . THR   B 125 ? 0.5720 0.5785 0.4508 0.2307  0.1030  0.1404  134 THR   B OG1 
1342 C CG2 . THR   B 125 ? 0.5713 0.5598 0.4256 0.2479  0.0876  0.1141  134 THR   B CG2 
1343 N N   . SER   B 126 ? 0.5175 0.4949 0.4121 0.1861  0.0858  0.0974  135 SER   B N   
1344 C CA  . SER   B 126 ? 0.5154 0.4867 0.4064 0.1799  0.0797  0.0847  135 SER   B CA  
1345 C C   . SER   B 126 ? 0.5120 0.4643 0.4010 0.1770  0.0741  0.0708  135 SER   B C   
1346 O O   . SER   B 126 ? 0.5067 0.4507 0.4048 0.1698  0.0760  0.0694  135 SER   B O   
1347 C CB  . SER   B 126 ? 0.5296 0.5050 0.4344 0.1617  0.0819  0.0856  135 SER   B CB  
1348 O OG  . SER   B 126 ? 0.5423 0.5381 0.4511 0.1622  0.0860  0.0974  135 SER   B OG  
1349 N N   . GLY   B 127 ? 0.5131 0.4590 0.3902 0.1830  0.0669  0.0615  136 GLY   B N   
1350 C CA  . GLY   B 127 ? 0.5170 0.4485 0.3930 0.1803  0.0609  0.0494  136 GLY   B CA  
1351 C C   . GLY   B 127 ? 0.5269 0.4528 0.3913 0.1967  0.0554  0.0469  136 GLY   B C   
1352 O O   . GLY   B 127 ? 0.5277 0.4436 0.3907 0.1956  0.0488  0.0371  136 GLY   B O   
1353 N N   . SER   B 128 ? 0.5264 0.4601 0.3825 0.2126  0.0578  0.0561  137 SER   B N   
1354 C CA  . SER   B 128 ? 0.5319 0.4603 0.3744 0.2306  0.0518  0.0536  137 SER   B CA  
1355 C C   . SER   B 128 ? 0.5413 0.4611 0.3693 0.2361  0.0404  0.0443  137 SER   B C   
1356 O O   . SER   B 128 ? 0.5475 0.4713 0.3696 0.2357  0.0395  0.0458  137 SER   B O   
1357 C CB  . SER   B 128 ? 0.5323 0.4734 0.3665 0.2473  0.0572  0.0665  137 SER   B CB  
1358 O OG  . SER   B 128 ? 0.5384 0.4832 0.3844 0.2426  0.0661  0.0753  137 SER   B OG  
1359 N N   . PRO   B 129 ? 0.5627 0.4700 0.3856 0.2407  0.0310  0.0348  138 PRO   B N   
1360 C CA  . PRO   B 129 ? 0.5783 0.4738 0.3876 0.2441  0.0183  0.0262  138 PRO   B CA  
1361 C C   . PRO   B 129 ? 0.6073 0.5015 0.3938 0.2669  0.0117  0.0281  138 PRO   B C   
1362 O O   . PRO   B 129 ? 0.6039 0.5036 0.3830 0.2841  0.0138  0.0332  138 PRO   B O   
1363 C CB  . PRO   B 129 ? 0.5908 0.4755 0.4049 0.2409  0.0102  0.0165  138 PRO   B CB  
1364 C CG  . PRO   B 129 ? 0.5902 0.4807 0.4104 0.2484  0.0167  0.0206  138 PRO   B CG  
1365 C CD  . PRO   B 129 ? 0.5647 0.4676 0.3943 0.2424  0.0306  0.0315  138 PRO   B CD  
1366 N N   . ILE   B 130 ? 0.6228 0.5077 0.3963 0.2681  0.0023  0.0231  139 ILE   B N   
1367 C CA  . ILE   B 130 ? 0.6559 0.5347 0.4041 0.2904  -0.0076 0.0218  139 ILE   B CA  
1368 C C   . ILE   B 130 ? 0.6765 0.5321 0.4161 0.2906  -0.0247 0.0096  139 ILE   B C   
1369 O O   . ILE   B 130 ? 0.6709 0.5172 0.4201 0.2714  -0.0288 0.0039  139 ILE   B O   
1370 C CB  . ILE   B 130 ? 0.6661 0.5498 0.4053 0.2913  -0.0066 0.0250  139 ILE   B CB  
1371 C CG1 . ILE   B 130 ? 0.6763 0.5851 0.4289 0.2874  0.0100  0.0375  139 ILE   B CG1 
1372 C CG2 . ILE   B 130 ? 0.6797 0.5546 0.3891 0.3163  -0.0188 0.0221  139 ILE   B CG2 
1373 C CD1 . ILE   B 130 ? 0.7052 0.6202 0.4560 0.2813  0.0117  0.0395  139 ILE   B CD1 
1374 N N   . LEU   B 131 ? 0.6960 0.5435 0.4189 0.3115  -0.0346 0.0060  140 LEU   B N   
1375 C CA  . LEU   B 131 ? 0.7294 0.5553 0.4452 0.3126  -0.0523 -0.0053 140 LEU   B CA  
1376 C C   . LEU   B 131 ? 0.7561 0.5628 0.4425 0.3319  -0.0699 -0.0115 140 LEU   B C   
1377 O O   . LEU   B 131 ? 0.7642 0.5770 0.4313 0.3550  -0.0686 -0.0073 140 LEU   B O   
1378 C CB  . LEU   B 131 ? 0.7501 0.5790 0.4711 0.3213  -0.0524 -0.0068 140 LEU   B CB  
1379 C CG  . LEU   B 131 ? 0.7723 0.6189 0.5165 0.3107  -0.0357 -0.0002 140 LEU   B CG  
1380 C CD1 . LEU   B 131 ? 0.7865 0.6322 0.5307 0.3225  -0.0389 -0.0029 140 LEU   B CD1 
1381 C CD2 . LEU   B 131 ? 0.7794 0.6277 0.5467 0.2828  -0.0310 -0.0023 140 LEU   B CD2 
1382 N N   . ASP   B 132 ? 0.7666 0.5501 0.4489 0.3239  -0.0873 -0.0215 141 ASP   B N   
1383 C CA  . ASP   B 132 ? 0.8031 0.5627 0.4559 0.3432  -0.1077 -0.0291 141 ASP   B CA  
1384 C C   . ASP   B 132 ? 0.8458 0.5988 0.4919 0.3595  -0.1182 -0.0351 141 ASP   B C   
1385 O O   . ASP   B 132 ? 0.8335 0.6009 0.4988 0.3542  -0.1088 -0.0329 141 ASP   B O   
1386 C CB  . ASP   B 132 ? 0.8205 0.5548 0.4688 0.3273  -0.1235 -0.0360 141 ASP   B CB  
1387 C CG  . ASP   B 132 ? 0.8544 0.5812 0.5246 0.3025  -0.1300 -0.0409 141 ASP   B CG  
1388 O OD1 . ASP   B 132 ? 0.8378 0.5738 0.5225 0.3020  -0.1279 -0.0424 141 ASP   B OD1 
1389 O OD2 . ASP   B 132 ? 0.8906 0.6038 0.5637 0.2840  -0.1369 -0.0426 141 ASP   B OD2 
1390 N N   . LYS   B 133 ? 0.8911 0.6205 0.5092 0.3795  -0.1389 -0.0435 142 LYS   B N   
1391 C CA  . LYS   B 133 ? 0.9260 0.6471 0.5335 0.3982  -0.1511 -0.0502 142 LYS   B CA  
1392 C C   . LYS   B 133 ? 0.9319 0.6480 0.5624 0.3789  -0.1586 -0.0566 142 LYS   B C   
1393 O O   . LYS   B 133 ? 0.9353 0.6519 0.5639 0.3918  -0.1639 -0.0606 142 LYS   B O   
1394 C CB  . LYS   B 133 ? 0.9934 0.6876 0.5635 0.4244  -0.1737 -0.0588 142 LYS   B CB  
1395 C CG  . LYS   B 133 ? 1.0906 0.7973 0.6365 0.4521  -0.1649 -0.0521 142 LYS   B CG  
1396 C CD  . LYS   B 133 ? 1.2018 0.8804 0.7096 0.4749  -0.1867 -0.0606 142 LYS   B CD  
1397 C CE  . LYS   B 133 ? 1.2686 0.9640 0.7572 0.4963  -0.1756 -0.0527 142 LYS   B CE  
1398 N NZ  . LYS   B 133 ? 1.3309 0.9980 0.7800 0.5205  -0.1975 -0.0618 142 LYS   B NZ  
1399 N N   . CYS   B 134 ? 0.9275 0.6410 0.5795 0.3488  -0.1584 -0.0570 143 CYS   B N   
1400 C CA  . CYS   B 134 ? 0.9213 0.6369 0.5988 0.3290  -0.1628 -0.0615 143 CYS   B CA  
1401 C C   . CYS   B 134 ? 0.8736 0.6181 0.5807 0.3144  -0.1402 -0.0543 143 CYS   B C   
1402 O O   . CYS   B 134 ? 0.8697 0.6201 0.5999 0.2969  -0.1414 -0.0572 143 CYS   B O   
1403 C CB  . CYS   B 134 ? 0.9636 0.6606 0.6478 0.3053  -0.1773 -0.0659 143 CYS   B CB  
1404 S SG  . CYS   B 134 ? 1.1081 0.7648 0.7557 0.3202  -0.2062 -0.0744 143 CYS   B SG  
1405 N N   . GLY   B 135 ? 0.8379 0.6001 0.5445 0.3213  -0.1206 -0.0451 144 GLY   B N   
1406 C CA  . GLY   B 135 ? 0.7999 0.5860 0.5318 0.3084  -0.1002 -0.0382 144 GLY   B CA  
1407 C C   . GLY   B 135 ? 0.7659 0.5587 0.5177 0.2808  -0.0910 -0.0351 144 GLY   B C   
1408 O O   . GLY   B 135 ? 0.7528 0.5630 0.5255 0.2688  -0.0759 -0.0308 144 GLY   B O   
1409 N N   . ARG   B 136 ? 0.7550 0.5326 0.4986 0.2716  -0.1003 -0.0372 145 ARG   B N   
1410 C CA  . ARG   B 136 ? 0.7402 0.5238 0.5006 0.2464  -0.0918 -0.0339 145 ARG   B CA  
1411 C C   . ARG   B 136 ? 0.7091 0.5058 0.4679 0.2480  -0.0747 -0.0253 145 ARG   B C   
1412 O O   . ARG   B 136 ? 0.7115 0.5051 0.4498 0.2662  -0.0754 -0.0227 145 ARG   B O   
1413 C CB  . ARG   B 136 ? 0.7864 0.5479 0.5382 0.2352  -0.1081 -0.0382 145 ARG   B CB  
1414 C CG  . ARG   B 136 ? 0.8505 0.6021 0.6115 0.2256  -0.1244 -0.0453 145 ARG   B CG  
1415 C CD  . ARG   B 136 ? 0.9297 0.6559 0.6792 0.2154  -0.1422 -0.0482 145 ARG   B CD  
1416 N NE  . ARG   B 136 ? 1.0281 0.7306 0.7446 0.2379  -0.1560 -0.0516 145 ARG   B NE  
1417 C CZ  . ARG   B 136 ? 1.0948 0.7732 0.7924 0.2357  -0.1681 -0.0525 145 ARG   B CZ  
1418 N NH1 . ARG   B 136 ? 1.0901 0.7652 0.7990 0.2108  -0.1671 -0.0493 145 ARG   B NH1 
1419 N NH2 . ARG   B 136 ? 1.1254 0.7833 0.7912 0.2597  -0.1809 -0.0564 145 ARG   B NH2 
1420 N N   . VAL   B 137 ? 0.6734 0.4859 0.4538 0.2297  -0.0598 -0.0211 146 VAL   B N   
1421 C CA  . VAL   B 137 ? 0.6621 0.4877 0.4443 0.2283  -0.0443 -0.0132 146 VAL   B CA  
1422 C C   . VAL   B 137 ? 0.6691 0.4849 0.4401 0.2221  -0.0482 -0.0127 146 VAL   B C   
1423 O O   . VAL   B 137 ? 0.6616 0.4726 0.4412 0.2031  -0.0503 -0.0147 146 VAL   B O   
1424 C CB  . VAL   B 137 ? 0.6441 0.4874 0.4513 0.2125  -0.0286 -0.0099 146 VAL   B CB  
1425 C CG1 . VAL   B 137 ? 0.6444 0.4993 0.4536 0.2101  -0.0148 -0.0021 146 VAL   B CG1 
1426 C CG2 . VAL   B 137 ? 0.6444 0.4956 0.4603 0.2207  -0.0252 -0.0103 146 VAL   B CG2 
1427 N N   . ILE   B 138 ? 0.6754 0.4891 0.4263 0.2391  -0.0494 -0.0097 147 ILE   B N   
1428 C CA  . ILE   B 138 ? 0.6811 0.4856 0.4184 0.2370  -0.0535 -0.0092 147 ILE   B CA  
1429 C C   . ILE   B 138 ? 0.6521 0.4746 0.3987 0.2291  -0.0376 -0.0019 147 ILE   B C   
1430 O O   . ILE   B 138 ? 0.6573 0.4746 0.3941 0.2267  -0.0397 -0.0014 147 ILE   B O   
1431 C CB  . ILE   B 138 ? 0.7029 0.4938 0.4100 0.2623  -0.0663 -0.0115 147 ILE   B CB  
1432 C CG1 . ILE   B 138 ? 0.7111 0.5211 0.4132 0.2835  -0.0564 -0.0050 147 ILE   B CG1 
1433 C CG2 . ILE   B 138 ? 0.7168 0.4830 0.4117 0.2676  -0.0863 -0.0203 147 ILE   B CG2 
1434 C CD1 . ILE   B 138 ? 0.7554 0.5583 0.4266 0.3109  -0.0659 -0.0057 147 ILE   B CD1 
1435 N N   . GLY   B 139 ? 0.6265 0.4687 0.3917 0.2247  -0.0231 0.0033  148 GLY   B N   
1436 C CA  . GLY   B 139 ? 0.6095 0.4682 0.3860 0.2156  -0.0093 0.0099  148 GLY   B CA  
1437 C C   . GLY   B 139 ? 0.5981 0.4753 0.3892 0.2178  0.0039  0.0167  148 GLY   B C   
1438 O O   . GLY   B 139 ? 0.6113 0.4891 0.4008 0.2295  0.0028  0.0170  148 GLY   B O   
1439 N N   . LEU   B 140 ? 0.5725 0.4640 0.3760 0.2081  0.0154  0.0227  149 LEU   B N   
1440 C CA  . LEU   B 140 ? 0.5671 0.4740 0.3846 0.2078  0.0273  0.0305  149 LEU   B CA  
1441 C C   . LEU   B 140 ? 0.5806 0.5042 0.3943 0.2164  0.0338  0.0404  149 LEU   B C   
1442 O O   . LEU   B 140 ? 0.5870 0.5131 0.3945 0.2149  0.0322  0.0406  149 LEU   B O   
1443 C CB  . LEU   B 140 ? 0.5529 0.4623 0.3909 0.1873  0.0346  0.0291  149 LEU   B CB  
1444 C CG  . LEU   B 140 ? 0.5612 0.4599 0.4063 0.1769  0.0302  0.0202  149 LEU   B CG  
1445 C CD1 . LEU   B 140 ? 0.5651 0.4689 0.4285 0.1606  0.0386  0.0195  149 LEU   B CD1 
1446 C CD2 . LEU   B 140 ? 0.5658 0.4594 0.4078 0.1883  0.0249  0.0174  149 LEU   B CD2 
1447 N N   . TYR   B 141 ? 0.5809 0.5170 0.3990 0.2249  0.0411  0.0493  150 TYR   B N   
1448 C CA  . TYR   B 141 ? 0.5871 0.5438 0.4047 0.2337  0.0487  0.0614  150 TYR   B CA  
1449 C C   . TYR   B 141 ? 0.5850 0.5534 0.4237 0.2158  0.0586  0.0682  150 TYR   B C   
1450 O O   . TYR   B 141 ? 0.5951 0.5573 0.4470 0.2047  0.0618  0.0669  150 TYR   B O   
1451 C CB  . TYR   B 141 ? 0.6017 0.5645 0.4138 0.2512  0.0515  0.0685  150 TYR   B CB  
1452 C CG  . TYR   B 141 ? 0.6164 0.6040 0.4315 0.2588  0.0615  0.0839  150 TYR   B CG  
1453 C CD1 . TYR   B 141 ? 0.6188 0.6163 0.4521 0.2486  0.0717  0.0944  150 TYR   B CD1 
1454 C CD2 . TYR   B 141 ? 0.6338 0.6354 0.4334 0.2767  0.0602  0.0885  150 TYR   B CD2 
1455 C CE1 . TYR   B 141 ? 0.6268 0.6488 0.4650 0.2536  0.0809  0.1104  150 TYR   B CE1 
1456 C CE2 . TYR   B 141 ? 0.6333 0.6624 0.4371 0.2840  0.0701  0.1041  150 TYR   B CE2 
1457 C CZ  . TYR   B 141 ? 0.6458 0.6858 0.4703 0.2710  0.0807  0.1157  150 TYR   B CZ  
1458 O OH  . TYR   B 141 ? 0.6752 0.7440 0.5057 0.2765  0.0905  0.1329  150 TYR   B OH  
1459 N N   . GLY   B 142 ? 0.5813 0.5670 0.4229 0.2145  0.0629  0.0756  151 GLY   B N   
1460 C CA  . GLY   B 142 ? 0.5799 0.5767 0.4422 0.1976  0.0710  0.0828  151 GLY   B CA  
1461 C C   . GLY   B 142 ? 0.5750 0.5802 0.4427 0.1868  0.0711  0.0823  151 GLY   B C   
1462 O O   . GLY   B 142 ? 0.5706 0.5862 0.4555 0.1736  0.0768  0.0889  151 GLY   B O   
1463 N N   . ASN   B 143 ? 0.5651 0.5648 0.4180 0.1921  0.0641  0.0747  152 ASN   B N   
1464 C CA  . ASN   B 143 ? 0.5670 0.5753 0.4230 0.1840  0.0638  0.0743  152 ASN   B CA  
1465 C C   . ASN   B 143 ? 0.5908 0.6112 0.4296 0.2022  0.0606  0.0769  152 ASN   B C   
1466 O O   . ASN   B 143 ? 0.6014 0.6068 0.4199 0.2139  0.0522  0.0693  152 ASN   B O   
1467 C CB  . ASN   B 143 ? 0.5622 0.5507 0.4161 0.1710  0.0584  0.0621  152 ASN   B CB  
1468 C CG  . ASN   B 143 ? 0.5753 0.5728 0.4361 0.1599  0.0594  0.0622  152 ASN   B CG  
1469 O OD1 . ASN   B 143 ? 0.5737 0.5904 0.4492 0.1546  0.0650  0.0708  152 ASN   B OD1 
1470 N ND2 . ASN   B 143 ? 0.5525 0.5361 0.4029 0.1558  0.0533  0.0530  152 ASN   B ND2 
1471 N N   . GLY   B 144 ? 0.6013 0.6487 0.4481 0.2048  0.0664  0.0878  153 GLY   B N   
1472 C CA  . GLY   B 144 ? 0.6335 0.6976 0.4646 0.2243  0.0643  0.0913  153 GLY   B CA  
1473 C C   . GLY   B 144 ? 0.6493 0.7466 0.4945 0.2219  0.0708  0.1028  153 GLY   B C   
1474 O O   . GLY   B 144 ? 0.6422 0.7435 0.5046 0.2032  0.0727  0.1029  153 GLY   B O   
1475 N N   . VAL   B 145 ? 0.6642 0.7871 0.5022 0.2416  0.0741  0.1127  154 VAL   B N   
1476 C CA  . VAL   B 145 ? 0.6792 0.8388 0.5296 0.2420  0.0798  0.1243  154 VAL   B CA  
1477 C C   . VAL   B 145 ? 0.7087 0.9007 0.5664 0.2535  0.0893  0.1417  154 VAL   B C   
1478 O O   . VAL   B 145 ? 0.7059 0.8920 0.5506 0.2689  0.0900  0.1434  154 VAL   B O   
1479 C CB  . VAL   B 145 ? 0.6971 0.8590 0.5261 0.2575  0.0720  0.1167  154 VAL   B CB  
1480 C CG1 . VAL   B 145 ? 0.6959 0.8636 0.4986 0.2881  0.0691  0.1177  154 VAL   B CG1 
1481 C CG2 . VAL   B 145 ? 0.6977 0.8896 0.5418 0.2503  0.0749  0.1228  154 VAL   B CG2 
1482 N N   . VAL   B 146 ? 0.7310 0.9581 0.6100 0.2456  0.0963  0.1552  155 VAL   B N   
1483 C CA  . VAL   B 146 ? 0.7606 1.0251 0.6493 0.2547  0.1064  0.1746  155 VAL   B CA  
1484 C C   . VAL   B 146 ? 0.7981 1.0927 0.6713 0.2792  0.1057  0.1775  155 VAL   B C   
1485 O O   . VAL   B 146 ? 0.7931 1.0975 0.6686 0.2759  0.1019  0.1730  155 VAL   B O   
1486 C CB  . VAL   B 146 ? 0.7561 1.0409 0.6795 0.2291  0.1137  0.1886  155 VAL   B CB  
1487 C CG1 . VAL   B 146 ? 0.7510 1.0810 0.6863 0.2375  0.1243  0.2110  155 VAL   B CG1 
1488 C CG2 . VAL   B 146 ? 0.7668 1.0193 0.7013 0.2088  0.1136  0.1854  155 VAL   B CG2 
1489 N N   . ILE   B 147 ? 0.8366 1.1441 0.6913 0.3059  0.1084  0.1834  156 ILE   B N   
1490 C CA  . ILE   B 147 ? 0.8746 1.2092 0.7099 0.3337  0.1068  0.1847  156 ILE   B CA  
1491 C C   . ILE   B 147 ? 0.8865 1.2798 0.7435 0.3359  0.1191  0.2071  156 ILE   B C   
1492 O O   . ILE   B 147 ? 0.8792 1.2872 0.7663 0.3135  0.1275  0.2210  156 ILE   B O   
1493 C CB  . ILE   B 147 ? 0.9063 1.2199 0.7058 0.3637  0.1006  0.1763  156 ILE   B CB  
1494 C CG1 . ILE   B 147 ? 0.9170 1.2361 0.7195 0.3693  0.1090  0.1883  156 ILE   B CG1 
1495 C CG2 . ILE   B 147 ? 0.9380 1.1988 0.7191 0.3588  0.0868  0.1544  156 ILE   B CG2 
1496 C CD1 . ILE   B 147 ? 0.9506 1.2502 0.7186 0.3991  0.1023  0.1803  156 ILE   B CD1 
1497 N N   A LYS   B 148 ? 0.8827 1.3076 0.7241 0.3622  0.1187  0.2096  157 LYS   B N   
1498 N N   B LYS   B 148 ? 0.8828 1.3077 0.7243 0.3621  0.1187  0.2096  157 LYS   B N   
1499 N N   C LYS   B 148 ? 0.8895 1.3159 0.7314 0.3626  0.1195  0.2108  157 LYS   B N   
1500 N N   D LYS   B 148 ? 0.8895 1.3160 0.7313 0.3628  0.1195  0.2109  157 LYS   B N   
1501 C CA  A LYS   B 148 ? 0.8650 1.3504 0.7222 0.3704  0.1291  0.2293  157 LYS   B CA  
1502 C CA  B LYS   B 148 ? 0.8652 1.3506 0.7229 0.3698  0.1291  0.2294  157 LYS   B CA  
1503 C CA  C LYS   B 148 ? 0.8776 1.3643 0.7400 0.3664  0.1313  0.2326  157 LYS   B CA  
1504 C CA  D LYS   B 148 ? 0.8776 1.3644 0.7398 0.3668  0.1313  0.2327  157 LYS   B CA  
1505 C C   A LYS   B 148 ? 0.8535 1.3678 0.7304 0.3661  0.1429  0.2520  157 LYS   B C   
1506 C C   B LYS   B 148 ? 0.8548 1.3687 0.7299 0.3678  0.1428  0.2517  157 LYS   B C   
1507 C C   C LYS   B 148 ? 0.8768 1.3830 0.7524 0.3654  0.1438  0.2527  157 LYS   B C   
1508 C C   D LYS   B 148 ? 0.8771 1.3832 0.7522 0.3659  0.1439  0.2527  157 LYS   B C   
1509 O O   A LYS   B 148 ? 0.8340 1.3767 0.7454 0.3425  0.1509  0.2679  157 LYS   B O   
1510 O O   B LYS   B 148 ? 0.8351 1.3794 0.7444 0.3455  0.1514  0.2686  157 LYS   B O   
1511 O O   C LYS   B 148 ? 0.8572 1.4036 0.7633 0.3509  0.1544  0.2729  157 LYS   B O   
1512 O O   D LYS   B 148 ? 0.8574 1.4037 0.7628 0.3516  0.1545  0.2730  157 LYS   B O   
1513 C CB  A LYS   B 148 ? 0.8920 1.3972 0.7171 0.4091  0.1253  0.2256  157 LYS   B CB  
1514 C CB  B LYS   B 148 ? 0.8918 1.3976 0.7185 0.4074  0.1250  0.2252  157 LYS   B CB  
1515 C CB  C LYS   B 148 ? 0.9023 1.4189 0.7394 0.4021  0.1292  0.2318  157 LYS   B CB  
1516 C CB  D LYS   B 148 ? 0.9024 1.4191 0.7392 0.4024  0.1292  0.2318  157 LYS   B CB  
1517 C CG  A LYS   B 148 ? 0.9601 1.4349 0.7616 0.4161  0.1106  0.2038  157 LYS   B CG  
1518 C CG  B LYS   B 148 ? 0.9596 1.4346 0.7643 0.4126  0.1104  0.2035  157 LYS   B CG  
1519 C CG  C LYS   B 148 ? 0.9732 1.4681 0.7916 0.4074  0.1158  0.2120  157 LYS   B CG  
1520 C CG  D LYS   B 148 ? 0.9735 1.4688 0.7922 0.4073  0.1159  0.2122  157 LYS   B CG  
1521 C CD  A LYS   B 148 ? 1.0331 1.4921 0.7903 0.4544  0.1015  0.1925  157 LYS   B CD  
1522 C CD  B LYS   B 148 ? 1.0330 1.4925 0.7931 0.4509  0.1010  0.1918  157 LYS   B CD  
1523 C CD  C LYS   B 148 ? 1.0357 1.5555 0.8239 0.4465  0.1125  0.2103  157 LYS   B CD  
1524 C CD  D LYS   B 148 ? 1.0365 1.5570 0.8253 0.4461  0.1126  0.2105  157 LYS   B CD  
1525 C CE  A LYS   B 148 ? 1.0998 1.5116 0.8386 0.4571  0.0961  0.1832  157 LYS   B CE  
1526 C CE  B LYS   B 148 ? 1.0994 1.5145 0.8398 0.4564  0.0961  0.1833  157 LYS   B CE  
1527 C CE  C LYS   B 148 ? 1.1001 1.5969 0.8674 0.4531  0.0986  0.1914  157 LYS   B CE  
1528 C CE  D LYS   B 148 ? 1.1014 1.5994 0.8701 0.4522  0.0989  0.1918  157 LYS   B CE  
1529 N NZ  A LYS   B 148 ? 1.1406 1.5032 0.8873 0.4277  0.0886  0.1690  157 LYS   B NZ  
1530 N NZ  B LYS   B 148 ? 1.1408 1.5051 0.8882 0.4275  0.0888  0.1694  157 LYS   B NZ  
1531 N NZ  C LYS   B 148 ? 1.1350 1.6549 0.8708 0.4933  0.0945  0.1894  157 LYS   B NZ  
1532 N NZ  D LYS   B 148 ? 1.1370 1.6588 0.8747 0.4921  0.0948  0.1899  157 LYS   B NZ  
1533 N N   C ASN   B 149 ? 0.8952 1.3721 0.7480 0.3800  0.1420  0.2472  158 ASN   B N   
1534 N N   D ASN   B 149 ? 0.8959 1.3723 0.7482 0.3804  0.1420  0.2471  158 ASN   B N   
1535 C CA  C ASN   B 149 ? 0.8960 1.3857 0.7547 0.3833  0.1529  0.2644  158 ASN   B CA  
1536 C CA  D ASN   B 149 ? 0.8973 1.3864 0.7555 0.3835  0.1528  0.2643  158 ASN   B CA  
1537 C C   C ASN   B 149 ? 0.8869 1.3595 0.7758 0.3480  0.1575  0.2718  158 ASN   B C   
1538 C C   D ASN   B 149 ? 0.8877 1.3594 0.7761 0.3482  0.1574  0.2715  158 ASN   B C   
1539 O O   C ASN   B 149 ? 0.8807 1.3707 0.7812 0.3456  0.1679  0.2905  158 ASN   B O   
1540 O O   D ASN   B 149 ? 0.8820 1.3700 0.7815 0.3460  0.1677  0.2898  158 ASN   B O   
1541 C CB  C ASN   B 149 ? 0.9421 1.4033 0.7639 0.4122  0.1475  0.2541  158 ASN   B CB  
1542 C CB  D ASN   B 149 ? 0.9443 1.4051 0.7658 0.4125  0.1475  0.2540  158 ASN   B CB  
1543 C CG  C ASN   B 149 ? 1.0083 1.4605 0.7933 0.4440  0.1361  0.2376  158 ASN   B CG  
1544 C CG  D ASN   B 149 ? 1.0118 1.4668 0.7968 0.4451  0.1367  0.2387  158 ASN   B CG  
1545 O OD1 C ASN   B 149 ? 1.0182 1.4980 0.8005 0.4541  0.1349  0.2377  158 ASN   B OD1 
1546 O OD1 D ASN   B 149 ? 1.0222 1.5087 0.8054 0.4561  0.1367  0.2407  158 ASN   B OD1 
1547 N ND2 C ASN   B 149 ? 1.0426 1.4546 0.7974 0.4609  0.1264  0.2226  158 ASN   B ND2 
1548 N ND2 D ASN   B 149 ? 1.0465 1.4598 0.8010 0.4616  0.1263  0.2227  158 ASN   B ND2 
1549 N N   . GLY   B 150 ? 0.8823 1.3199 0.7813 0.3227  0.1493  0.2571  159 GLY   B N   
1550 C CA  . GLY   B 150 ? 0.8600 1.2760 0.7841 0.2909  0.1512  0.2607  159 GLY   B CA  
1551 C C   . GLY   B 150 ? 0.8572 1.2218 0.7649 0.2905  0.1449  0.2455  159 GLY   B C   
1552 O O   . GLY   B 150 ? 0.8596 1.1980 0.7831 0.2659  0.1438  0.2429  159 GLY   B O   
1553 N N   . SER   B 151 ? 0.8502 1.2006 0.7255 0.3189  0.1401  0.2353  160 SER   B N   
1554 C CA  . SER   B 151 ? 0.8513 1.1559 0.7085 0.3226  0.1327  0.2199  160 SER   B CA  
1555 C C   . SER   B 151 ? 0.8254 1.0927 0.6796 0.3078  0.1208  0.1981  160 SER   B C   
1556 O O   . SER   B 151 ? 0.8215 1.0975 0.6773 0.3046  0.1170  0.1929  160 SER   B O   
1557 C CB  . SER   B 151 ? 0.8910 1.1951 0.7145 0.3582  0.1292  0.2156  160 SER   B CB  
1558 O OG  . SER   B 151 ? 0.9551 1.2211 0.7642 0.3622  0.1235  0.2049  160 SER   B OG  
1559 N N   . TYR   B 152 ? 0.8056 1.0331 0.6556 0.2995  0.1153  0.1860  161 TYR   B N   
1560 C CA  . TYR   B 152 ? 0.7865 0.9793 0.6336 0.2856  0.1050  0.1666  161 TYR   B CA  
1561 C C   . TYR   B 152 ? 0.7613 0.9298 0.5770 0.3070  0.0939  0.1509  161 TYR   B C   
1562 O O   . TYR   B 152 ? 0.7710 0.9334 0.5707 0.3255  0.0929  0.1513  161 TYR   B O   
1563 C CB  . TYR   B 152 ? 0.7919 0.9574 0.6546 0.2628  0.1054  0.1629  161 TYR   B CB  
1564 C CG  . TYR   B 152 ? 0.8034 0.9449 0.6740 0.2414  0.0988  0.1485  161 TYR   B CG  
1565 C CD1 . TYR   B 152 ? 0.8011 0.9563 0.6902 0.2237  0.1007  0.1517  161 TYR   B CD1 
1566 C CD2 . TYR   B 152 ? 0.8274 0.9337 0.6886 0.2379  0.0913  0.1329  161 TYR   B CD2 
1567 C CE1 . TYR   B 152 ? 0.8176 0.9512 0.7123 0.2055  0.0949  0.1388  161 TYR   B CE1 
1568 C CE2 . TYR   B 152 ? 0.8392 0.9260 0.7077 0.2187  0.0865  0.1211  161 TYR   B CE2 
1569 C CZ  . TYR   B 152 ? 0.8381 0.9380 0.7223 0.2032  0.0884  0.1240  161 TYR   B CZ  
1570 O OH  . TYR   B 152 ? 0.8441 0.9253 0.7341 0.1855  0.0839  0.1126  161 TYR   B OH  
1571 N N   . VAL   B 153 ? 0.7194 0.8729 0.5259 0.3045  0.0847  0.1373  162 VAL   B N   
1572 C CA  . VAL   B 153 ? 0.6960 0.8200 0.4744 0.3195  0.0719  0.1215  162 VAL   B CA  
1573 C C   . VAL   B 153 ? 0.6598 0.7513 0.4455 0.2959  0.0654  0.1078  162 VAL   B C   
1574 O O   . VAL   B 153 ? 0.6351 0.7290 0.4314 0.2804  0.0655  0.1055  162 VAL   B O   
1575 C CB  . VAL   B 153 ? 0.7071 0.8417 0.4619 0.3424  0.0655  0.1185  162 VAL   B CB  
1576 C CG1 . VAL   B 153 ? 0.7278 0.8243 0.4545 0.3531  0.0498  0.1010  162 VAL   B CG1 
1577 C CG2 . VAL   B 153 ? 0.7170 0.8851 0.4626 0.3688  0.0722  0.1319  162 VAL   B CG2 
1578 N N   . SER   B 154 ? 0.6465 0.7105 0.4280 0.2932  0.0608  0.0997  163 SER   B N   
1579 C CA  . SER   B 154 ? 0.6335 0.6701 0.4228 0.2719  0.0558  0.0881  163 SER   B CA  
1580 C C   . SER   B 154 ? 0.6363 0.6463 0.4030 0.2784  0.0420  0.0738  163 SER   B C   
1581 O O   . SER   B 154 ? 0.6503 0.6519 0.3950 0.2992  0.0344  0.0703  163 SER   B O   
1582 C CB  . SER   B 154 ? 0.6310 0.6545 0.4298 0.2649  0.0582  0.0874  163 SER   B CB  
1583 O OG  . SER   B 154 ? 0.6497 0.6477 0.4530 0.2483  0.0526  0.0754  163 SER   B OG  
1584 N N   . ALA   B 155 ? 0.6184 0.6129 0.3903 0.2602  0.0382  0.0656  164 ALA   B N   
1585 C CA  . ALA   B 155 ? 0.6156 0.5815 0.3681 0.2622  0.0250  0.0531  164 ALA   B CA  
1586 C C   . ALA   B 155 ? 0.6155 0.5601 0.3677 0.2600  0.0200  0.0468  164 ALA   B C   
1587 O O   . ALA   B 155 ? 0.5998 0.5500 0.3698 0.2513  0.0277  0.0505  164 ALA   B O   
1588 C CB  . ALA   B 155 ? 0.6157 0.5731 0.3768 0.2410  0.0244  0.0479  164 ALA   B CB  
1589 N N   . ILE   B 156 ? 0.6278 0.5471 0.3604 0.2668  0.0064  0.0372  165 ILE   B N   
1590 C CA  . ILE   B 156 ? 0.6359 0.5349 0.3708 0.2606  0.0002  0.0301  165 ILE   B CA  
1591 C C   . ILE   B 156 ? 0.6174 0.5049 0.3643 0.2358  -0.0003 0.0248  165 ILE   B C   
1592 O O   . ILE   B 156 ? 0.6221 0.4914 0.3551 0.2336  -0.0104 0.0188  165 ILE   B O   
1593 C CB  . ILE   B 156 ? 0.6691 0.5454 0.3776 0.2785  -0.0161 0.0224  165 ILE   B CB  
1594 C CG1 . ILE   B 156 ? 0.6947 0.5840 0.3879 0.3064  -0.0157 0.0275  165 ILE   B CG1 
1595 C CG2 . ILE   B 156 ? 0.6839 0.5411 0.3991 0.2682  -0.0231 0.0151  165 ILE   B CG2 
1596 C CD1 . ILE   B 156 ? 0.7443 0.6102 0.4085 0.3277  -0.0331 0.0192  165 ILE   B CD1 
1597 N N   . THR   B 157 ? 0.5974 0.4960 0.3683 0.2182  0.0109  0.0278  166 THR   B N   
1598 C CA  . THR   B 157 ? 0.5846 0.4761 0.3660 0.1966  0.0118  0.0236  166 THR   B CA  
1599 C C   . THR   B 157 ? 0.5847 0.4597 0.3706 0.1865  0.0061  0.0166  166 THR   B C   
1600 O O   . THR   B 157 ? 0.5639 0.4434 0.3630 0.1840  0.0105  0.0168  166 THR   B O   
1601 C CB  . THR   B 157 ? 0.5746 0.4838 0.3776 0.1832  0.0247  0.0288  166 THR   B CB  
1602 O OG1 . THR   B 157 ? 0.5721 0.4993 0.3736 0.1907  0.0295  0.0361  166 THR   B OG1 
1603 C CG2 . THR   B 157 ? 0.5702 0.4725 0.3819 0.1631  0.0256  0.0238  166 THR   B CG2 
1604 N N   . GLN   B 158 ? 0.5869 0.4436 0.3621 0.1806  -0.0038 0.0109  167 GLN   B N   
1605 C CA  . GLN   B 158 ? 0.5917 0.4350 0.3724 0.1693  -0.0101 0.0053  167 GLN   B CA  
1606 C C   . GLN   B 158 ? 0.6020 0.4434 0.3913 0.1487  -0.0069 0.0041  167 GLN   B C   
1607 O O   . GLN   B 158 ? 0.5865 0.4257 0.3670 0.1468  -0.0070 0.0053  167 GLN   B O   
1608 C CB  . GLN   B 158 ? 0.6177 0.4385 0.3771 0.1793  -0.0267 0.0007  167 GLN   B CB  
1609 C CG  . GLN   B 158 ? 0.6416 0.4492 0.4070 0.1688  -0.0356 -0.0044 167 GLN   B CG  
1610 C CD  . GLN   B 158 ? 0.6324 0.4529 0.4171 0.1669  -0.0293 -0.0049 167 GLN   B CD  
1611 O OE1 . GLN   B 158 ? 0.6009 0.4378 0.4045 0.1568  -0.0164 -0.0025 167 GLN   B OE1 
1612 N NE2 . GLN   B 158 ? 0.6144 0.4265 0.3940 0.1768  -0.0391 -0.0085 167 GLN   B NE2 
1613 N N   . GLY   B 159 ? 0.6199 0.4634 0.4252 0.1351  -0.0043 0.0018  168 GLY   B N   
1614 C CA  . GLY   B 159 ? 0.6599 0.5032 0.4727 0.1170  -0.0012 0.0010  168 GLY   B CA  
1615 C C   . GLY   B 159 ? 0.7268 0.5515 0.5298 0.1102  -0.0134 -0.0012 168 GLY   B C   
1616 O O   . GLY   B 159 ? 0.7534 0.5623 0.5411 0.1203  -0.0258 -0.0029 168 GLY   B O   
1617 N N   . LYS   B 160 ? 0.7548 0.5808 0.5660 0.0932  -0.0108 -0.0010 169 LYS   B N   
1618 C CA  . LYS   B 160 ? 0.7968 0.6062 0.6011 0.0834  -0.0220 -0.0012 169 LYS   B CA  
1619 C C   . LYS   B 160 ? 0.8145 0.6351 0.6394 0.0704  -0.0193 -0.0017 169 LYS   B C   
1620 O O   . LYS   B 160 ? 0.8050 0.6442 0.6454 0.0634  -0.0069 -0.0012 169 LYS   B O   
1621 C CB  . LYS   B 160 ? 0.8387 0.6403 0.6324 0.0745  -0.0214 0.0015  169 LYS   B CB  
1622 C CG  . LYS   B 160 ? 0.9217 0.7030 0.7060 0.0636  -0.0337 0.0031  169 LYS   B CG  
1623 C CD  . LYS   B 160 ? 0.9989 0.7742 0.7739 0.0537  -0.0313 0.0067  169 LYS   B CD  
1624 C CE  . LYS   B 160 ? 1.0679 0.8225 0.8345 0.0408  -0.0434 0.0100  169 LYS   B CE  
1625 N NZ  . LYS   B 160 ? 1.1129 0.8656 0.8739 0.0287  -0.0385 0.0148  169 LYS   B NZ  
1626 N N   . ARG   B 161 ? 0.8372 0.6474 0.6621 0.0679  -0.0314 -0.0030 170 ARG   B N   
1627 C CA  . ARG   B 161 ? 0.8544 0.6782 0.7001 0.0551  -0.0297 -0.0030 170 ARG   B CA  
1628 C C   . ARG   B 161 ? 0.8882 0.7081 0.7346 0.0362  -0.0315 0.0017  170 ARG   B C   
1629 O O   . ARG   B 161 ? 0.9032 0.7017 0.7375 0.0313  -0.0454 0.0034  170 ARG   B O   
1630 C CB  . ARG   B 161 ? 0.8676 0.6847 0.7155 0.0608  -0.0423 -0.0065 170 ARG   B CB  
1631 C CG  . ARG   B 161 ? 0.8794 0.7167 0.7515 0.0513  -0.0390 -0.0072 170 ARG   B CG  
1632 C CD  . ARG   B 161 ? 0.9195 0.7478 0.7931 0.0543  -0.0545 -0.0106 170 ARG   B CD  
1633 N NE  . ARG   B 161 ? 0.9375 0.7871 0.8356 0.0426  -0.0525 -0.0105 170 ARG   B NE  
1634 C CZ  . ARG   B 161 ? 0.9495 0.8139 0.8606 0.0508  -0.0506 -0.0148 170 ARG   B CZ  
1635 N NH1 . ARG   B 161 ? 0.9363 0.7949 0.8377 0.0701  -0.0506 -0.0188 170 ARG   B NH1 
1636 N NH2 . ARG   B 161 ? 0.9408 0.8270 0.8744 0.0402  -0.0488 -0.0146 170 ARG   B NH2 
1637 N N   . GLU   B 162 ? 0.8955 0.7346 0.7536 0.0267  -0.0178 0.0042  171 GLU   B N   
1638 C CA  . GLU   B 162 ? 0.9224 0.7632 0.7821 0.0095  -0.0157 0.0099  171 GLU   B CA  
1639 C C   . GLU   B 162 ? 0.9301 0.7743 0.8028 -0.0049 -0.0236 0.0132  171 GLU   B C   
1640 O O   . GLU   B 162 ? 0.9418 0.7785 0.8109 -0.0194 -0.0278 0.0195  171 GLU   B O   
1641 C CB  . GLU   B 162 ? 0.9517 0.8161 0.8222 0.0061  0.0013  0.0104  171 GLU   B CB  
1642 C CG  . GLU   B 162 ? 1.0464 0.9035 0.9014 0.0111  0.0066  0.0106  171 GLU   B CG  
1643 C CD  . GLU   B 162 ? 1.1701 1.0125 1.0104 0.0009  0.0024  0.0162  171 GLU   B CD  
1644 O OE1 . GLU   B 162 ? 1.1808 1.0352 1.0290 -0.0124 0.0082  0.0209  171 GLU   B OE1 
1645 O OE2 . GLU   B 162 ? 1.2211 1.0406 1.0412 0.0070  -0.0067 0.0162  171 GLU   B OE2 
1646 S S   A DMS   C .   ? 3.7860 3.7478 3.7878 0.0200  0.0076  -0.0178 201 DMS   B S   
1647 S S   B DMS   C .   ? 3.7860 3.7478 3.7878 0.0200  0.0076  -0.0178 201 DMS   B S   
1648 O O   A DMS   C .   ? 3.7844 3.7522 3.7852 0.0220  0.0108  -0.0212 201 DMS   B O   
1649 O O   B DMS   C .   ? 3.7844 3.7522 3.7852 0.0220  0.0108  -0.0212 201 DMS   B O   
1650 C C1  A DMS   C .   ? 3.7864 3.7475 3.7880 0.0241  0.0107  -0.0224 201 DMS   B C1  
1651 C C1  B DMS   C .   ? 3.7864 3.7475 3.7880 0.0241  0.0107  -0.0224 201 DMS   B C1  
1652 C C2  A DMS   C .   ? 3.7854 3.7451 3.7903 0.0190  0.0045  -0.0113 201 DMS   B C2  
1653 C C2  B DMS   C .   ? 3.7854 3.7451 3.7903 0.0190  0.0045  -0.0113 201 DMS   B C2  
1654 N N1  . A1BGX D .   ? 0.7968 0.9644 0.7671 0.1502  0.1120  0.1772  202 A1BGX B N1  
1655 N N3  . A1BGX D .   ? 0.8092 0.8360 0.7372 0.1200  0.0782  0.0864  202 A1BGX B N3  
1656 C C4  . A1BGX D .   ? 0.8083 0.9500 0.7592 0.1617  0.1087  0.1651  202 A1BGX B C4  
1657 C C5  . A1BGX D .   ? 0.8096 0.9362 0.7569 0.1658  0.1112  0.1677  202 A1BGX B C5  
1658 C C6  . A1BGX D .   ? 0.8127 0.9132 0.7395 0.1788  0.1064  0.1538  202 A1BGX B C6  
1659 C C7  . A1BGX D .   ? 0.8114 0.9174 0.7228 0.2004  0.1087  0.1588  202 A1BGX B C7  
1660 C C8  . A1BGX D .   ? 0.8223 0.9056 0.7151 0.2129  0.1029  0.1460  202 A1BGX B C8  
1661 C C10 . A1BGX D .   ? 0.8270 0.8794 0.7319 0.1829  0.0945  0.1246  202 A1BGX B C10 
1662 C C13 . A1BGX D .   ? 0.8085 0.8510 0.7392 0.1350  0.0860  0.1048  202 A1BGX B C13 
1663 C C15 . A1BGX D .   ? 0.7992 0.8219 0.7574 0.0911  0.0793  0.0897  202 A1BGX B C15 
1664 C C17 . A1BGX D .   ? 0.8072 0.9453 0.7705 0.1579  0.1180  0.1851  202 A1BGX B C17 
1665 C C1  . A1BGX D .   ? 0.8026 0.9476 0.8122 0.1178  0.1247  0.2152  202 A1BGX B C1  
1666 O O1  . A1BGX D .   ? 0.7948 0.9695 0.7957 0.1345  0.1273  0.2172  202 A1BGX B O1  
1667 C C2  . A1BGX D .   ? 0.7975 0.9611 0.7814 0.1446  0.1214  0.1986  202 A1BGX B C2  
1668 C C3  . A1BGX D .   ? 0.7891 0.9683 0.7764 0.1414  0.1182  0.1941  202 A1BGX B C3  
1669 C C9  . A1BGX D .   ? 0.8292 0.8859 0.7203 0.2030  0.0957  0.1293  202 A1BGX B C9  
1670 C C11 . A1BGX D .   ? 0.8171 0.8893 0.7396 0.1706  0.0994  0.1361  202 A1BGX B C11 
1671 C C12 . A1BGX D .   ? 0.8111 0.8744 0.7461 0.1501  0.0961  0.1284  202 A1BGX B C12 
1672 O O2  . A1BGX D .   ? 0.8067 0.8728 0.7597 0.1343  0.0985  0.1353  202 A1BGX B O2  
1673 N N2  . A1BGX D .   ? 0.8123 0.8638 0.7365 0.1506  0.0897  0.1139  202 A1BGX B N2  
1674 C C14 . A1BGX D .   ? 0.8118 0.8452 0.7308 0.1358  0.0801  0.0923  202 A1BGX B C14 
1675 N N4  . A1BGX D .   ? 0.8016 0.8318 0.7475 0.1087  0.0817  0.0943  202 A1BGX B N4  
1676 C C16 . A1BGX D .   ? 0.8006 0.8396 0.7489 0.1164  0.0865  0.1059  202 A1BGX B C16 
1677 S S   C SO4   E .   ? 1.2076 1.0747 1.1432 0.0583  0.0590  -0.0246 203 SO4   B S   
1678 S S   D SO4   E .   ? 1.2076 1.0747 1.1432 0.0583  0.0590  -0.0246 203 SO4   B S   
1679 O O1  C SO4   E .   ? 1.2053 1.0679 1.1482 0.0582  0.0586  -0.0149 203 SO4   B O1  
1680 O O1  D SO4   E .   ? 1.2053 1.0679 1.1482 0.0582  0.0586  -0.0149 203 SO4   B O1  
1681 O O2  C SO4   E .   ? 1.2132 1.0686 1.1440 0.0624  0.0560  -0.0346 203 SO4   B O2  
1682 O O2  D SO4   E .   ? 1.2132 1.0686 1.1440 0.0624  0.0560  -0.0346 203 SO4   B O2  
1683 O O3  C SO4   E .   ? 1.2038 1.0839 1.1362 0.0625  0.0643  -0.0254 203 SO4   B O3  
1684 O O3  D SO4   E .   ? 1.2038 1.0839 1.1362 0.0625  0.0643  -0.0254 203 SO4   B O3  
1685 O O4  C SO4   E .   ? 1.2084 1.0789 1.1438 0.0508  0.0564  -0.0234 203 SO4   B O4  
1686 O O4  D SO4   E .   ? 1.2084 1.0789 1.1438 0.0508  0.0564  -0.0234 203 SO4   B O4  
# 
