data_7HOT
# 
_entry.id   7HOT 
# 
_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   7HOT         pdb_00007hot 10.2210/pdb7hot/pdb 
WWPDB D_1001407743 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-26 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
loop_
_database_PDB_caveat.id 
_database_PDB_caveat.text 
1 
;Residues ASN B 152 and GLY B 153 that are next to each other in the sample sequence are not properly linked: distance between C (D conformer) and N is 1.62.
;
2 
;Residues ASN B 152 and GLY B 153 that are next to each other in the sample sequence are not properly linked: distance between C (C conformer) and N is 1.63.
;
# 
_pdbx_database_status.entry_id                        7HOT 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                           5067.486  1  ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                    18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                     78.133    6  ?                           ?    ? ? 
4 non-polymer syn 'N-(3-methylpyridin-4-yl)-3-(1,3-thiazol-2-yl)benzamide' 295.359   1  ?                           ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                            96.063    1  ?                           ?    ? ? 
6 water       nat water                                                    18.015    98 ?                           ?    ? ? 
# 
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 'N-(3-methylpyridin-4-yl)-3-(1,3-thiazol-2-yl)benzamide' A1BG2 
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 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BG2 non-polymer         . 'N-(3-methylpyridin-4-yl)-3-(1,3-thiazol-2-yl)benzamide' ? 'C16 H13 N3 O S' 295.359 
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        A1BG2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BG2 
_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  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BG2 1  204 301 A1BG2 LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 3 DMS   1  206 303 DMS   DMS B . 
I 3 DMS   1  207 304 DMS   DMS B . 
J 3 DMS   1  208 1   DMS   DMS B . 
K 6 HOH   1  101 121 HOH   HOH A . 
K 6 HOH   2  102 105 HOH   HOH A . 
K 6 HOH   3  103 81  HOH   HOH A . 
K 6 HOH   4  104 48  HOH   HOH A . 
K 6 HOH   5  105 16  HOH   HOH A . 
K 6 HOH   6  106 65  HOH   HOH A . 
K 6 HOH   7  107 98  HOH   HOH A . 
K 6 HOH   8  108 34  HOH   HOH A . 
K 6 HOH   9  109 110 HOH   HOH A . 
K 6 HOH   10 110 28  HOH   HOH A . 
K 6 HOH   11 111 118 HOH   HOH A . 
K 6 HOH   12 112 49  HOH   HOH A . 
K 6 HOH   13 113 50  HOH   HOH A . 
K 6 HOH   14 114 20  HOH   HOH A . 
K 6 HOH   15 115 29  HOH   HOH A . 
K 6 HOH   16 116 12  HOH   HOH A . 
K 6 HOH   17 117 40  HOH   HOH A . 
K 6 HOH   18 118 120 HOH   HOH A . 
K 6 HOH   19 119 70  HOH   HOH A . 
K 6 HOH   20 120 129 HOH   HOH A . 
K 6 HOH   21 121 119 HOH   HOH A . 
K 6 HOH   22 122 27  HOH   HOH A . 
K 6 HOH   23 123 85  HOH   HOH A . 
L 6 HOH   1  301 54  HOH   HOH B . 
L 6 HOH   2  302 57  HOH   HOH B . 
L 6 HOH   3  303 51  HOH   HOH B . 
L 6 HOH   4  304 11  HOH   HOH B . 
L 6 HOH   5  305 106 HOH   HOH B . 
L 6 HOH   6  306 92  HOH   HOH B . 
L 6 HOH   7  307 5   HOH   HOH B . 
L 6 HOH   8  308 58  HOH   HOH B . 
L 6 HOH   9  309 79  HOH   HOH B . 
L 6 HOH   10 310 90  HOH   HOH B . 
L 6 HOH   11 311 35  HOH   HOH B . 
L 6 HOH   12 312 66  HOH   HOH B . 
L 6 HOH   13 313 14  HOH   HOH B . 
L 6 HOH   14 314 1   HOH   HOH B . 
L 6 HOH   15 315 117 HOH   HOH B . 
L 6 HOH   16 316 24  HOH   HOH B . 
L 6 HOH   17 317 42  HOH   HOH B . 
L 6 HOH   18 318 4   HOH   HOH B . 
L 6 HOH   19 319 126 HOH   HOH B . 
L 6 HOH   20 320 130 HOH   HOH B . 
L 6 HOH   21 321 128 HOH   HOH B . 
L 6 HOH   22 322 89  HOH   HOH B . 
L 6 HOH   23 323 125 HOH   HOH B . 
L 6 HOH   24 324 23  HOH   HOH B . 
L 6 HOH   25 325 30  HOH   HOH B . 
L 6 HOH   26 326 60  HOH   HOH B . 
L 6 HOH   27 327 31  HOH   HOH B . 
L 6 HOH   28 328 62  HOH   HOH B . 
L 6 HOH   29 329 46  HOH   HOH B . 
L 6 HOH   30 330 36  HOH   HOH B . 
L 6 HOH   31 331 108 HOH   HOH B . 
L 6 HOH   32 332 112 HOH   HOH B . 
L 6 HOH   33 333 109 HOH   HOH B . 
L 6 HOH   34 334 56  HOH   HOH B . 
L 6 HOH   35 335 21  HOH   HOH B . 
L 6 HOH   36 336 63  HOH   HOH B . 
L 6 HOH   37 337 127 HOH   HOH B . 
L 6 HOH   38 338 116 HOH   HOH B . 
L 6 HOH   39 339 13  HOH   HOH B . 
L 6 HOH   40 340 103 HOH   HOH B . 
L 6 HOH   41 341 2   HOH   HOH B . 
L 6 HOH   42 342 9   HOH   HOH B . 
L 6 HOH   43 343 67  HOH   HOH B . 
L 6 HOH   44 344 80  HOH   HOH B . 
L 6 HOH   45 345 77  HOH   HOH B . 
L 6 HOH   46 346 69  HOH   HOH B . 
L 6 HOH   47 347 32  HOH   HOH B . 
L 6 HOH   48 348 100 HOH   HOH B . 
L 6 HOH   49 349 115 HOH   HOH B . 
L 6 HOH   50 350 10  HOH   HOH B . 
L 6 HOH   51 351 123 HOH   HOH B . 
L 6 HOH   52 352 68  HOH   HOH B . 
L 6 HOH   53 353 72  HOH   HOH B . 
L 6 HOH   54 354 102 HOH   HOH B . 
L 6 HOH   55 355 3   HOH   HOH B . 
L 6 HOH   56 356 18  HOH   HOH B . 
L 6 HOH   57 357 82  HOH   HOH B . 
L 6 HOH   58 358 83  HOH   HOH B . 
L 6 HOH   59 359 17  HOH   HOH B . 
L 6 HOH   60 360 131 HOH   HOH B . 
L 6 HOH   61 361 94  HOH   HOH B . 
L 6 HOH   62 362 43  HOH   HOH B . 
L 6 HOH   63 363 64  HOH   HOH B . 
L 6 HOH   64 364 107 HOH   HOH B . 
L 6 HOH   65 365 122 HOH   HOH B . 
L 6 HOH   66 366 124 HOH   HOH B . 
L 6 HOH   67 367 26  HOH   HOH B . 
L 6 HOH   68 368 61  HOH   HOH B . 
L 6 HOH   69 369 87  HOH   HOH B . 
L 6 HOH   70 370 39  HOH   HOH B . 
L 6 HOH   71 371 73  HOH   HOH B . 
L 6 HOH   72 372 59  HOH   HOH B . 
L 6 HOH   73 373 45  HOH   HOH B . 
L 6 HOH   74 374 44  HOH   HOH B . 
L 6 HOH   75 375 75  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HOT 
_cell.length_a           42.514 
_cell.length_b           42.514 
_cell.length_c           216.443 
_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                         7HOT 
_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          7HOT 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.68 
_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                     7HOT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.43 
_reflns.d_resolution_high            1.59 
_reflns.number_obs                   28124 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.135 
_reflns.pdbx_netI_over_sigmaI        8.5 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.138 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     716262 
_reflns.pdbx_chi_squared             0.26 
_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                  1.59 
_reflns_shell.d_res_low                   1.62 
_reflns_shell.number_measured_all         31370 
_reflns_shell.number_unique_obs           1337 
_reflns_shell.Rmerge_I_obs                6.191 
_reflns_shell.pdbx_chi_squared            0.06 
_reflns_shell.pdbx_redundancy             23.5 
_reflns_shell.percent_possible_obs        99.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             6.328 
_reflns_shell.pdbx_Rpim_I_all             1.298 
_reflns_shell.pdbx_CC_half                0.344 
_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                                 7HOT 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24031 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.11 
_refine.ls_d_res_high                            1.59 
_refine.ls_percent_reflns_obs                    90.40 
_refine.ls_R_factor_obs                          0.25576 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.25412 
_refine.ls_R_factor_R_free                       0.28683 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1303 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.B_iso_mean                               43.067 
_refine.aniso_B[1][1]                            -0.59 
_refine.aniso_B[2][2]                            -0.59 
_refine.aniso_B[3][3]                            1.19 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.174 
_refine.pdbx_overall_ESU_R_Free                  0.152 
_refine.overall_SU_ML                            0.271 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             21.028 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             98 
_refine_hist.number_atoms_total               1624 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        54.11 
# 
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 
r_bond_refined_d             0.024  0.014  ? 3046 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.014  0.015  ? 2153 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.128  1.633  ? 3243 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.590  1.582  ? 4957 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       9.094  5.000  ? 313  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.447 23.077 ? 104  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.576 15.000 ? 346  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       18.382 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.085  0.200  ? 282  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.014  0.020  ? 2835 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 559  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.995  1.579  ? 1505 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.000  1.435  ? 1467 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.974  2.178  ? 1509 'X-RAY DIFFRACTION' ? 
r_mcangle_other              1.973  2.181  ? 1510 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.165  1.863  ? 1541 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.165  1.869  ? 1542 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.075  2.629  ? 1735 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       17.205 17.483 ? 2611 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         17.184 17.399 ? 2606 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.590 
_refine_ls_shell.d_res_low                        1.631 
_refine_ls_shell.number_reflns_R_work             188 
_refine_ls_shell.R_factor_R_work                  0.708 
_refine_ls_shell.percent_reflns_obs               10.00 
_refine_ls_shell.R_factor_R_free                  0.646 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             14 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOT 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014668-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOT 
_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 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 6 ? 
L 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 7HOT A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOT 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 7HOT SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOT MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOT MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOT LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5430 ? 
1 MORE         -25  ? 
1 'SSA (A^2)'  9700 ? 
# 
_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,H,I,J,K,L 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.524 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 9 ? 
# 
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 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA2 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA2 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA2 5 TYR B 152 ? THR B 157 ? TYR B 161 THR B 166 
AA2 6 VAL B 137 ? VAL B 146 ? VAL B 146 VAL B 155 
AA2 7 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 8 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 9 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA2 2 3 N VAL A 33  ? N VAL A 76  O LYS B 108 ? O LYS B 117 
AA2 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA2 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA2 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA2 6 7 O GLY B 139 ? O GLY B 148 N ILE B 130 ? N ILE B 139 
AA2 7 8 O PRO B 129 ? O PRO B 138 N LEU B 89  ? N LEU B 98  
AA2 8 9 N ALA B 90  ? N ALA B 99  O LYS B 98  ? O LYS B 107 
# 
_pdbx_entry_details.entry_id                   7HOT 
_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   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    90 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    93 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CA B GLY 81  ? C C B GLY 81  ? C 1.619 1.514 0.105  0.016 N 
2  1 CA B GLY 81  ? D C B GLY 81  ? D 1.621 1.514 0.107  0.016 N 
3  1 C  B GLY 81  ? A O B GLY 81  ? A 1.524 1.232 0.292  0.016 N 
4  1 C  B GLY 81  ? B O B GLY 81  ? B 1.526 1.232 0.294  0.016 N 
5  1 C  B GLY 81  ? C O B GLY 81  ? C 1.382 1.232 0.150  0.016 N 
6  1 C  B GLY 81  ? D O B GLY 81  ? D 1.383 1.232 0.151  0.016 N 
7  1 C  B GLY 81  ? A N B PRO 82  ? A 1.503 1.338 0.165  0.019 Y 
8  1 C  B GLY 81  ? B N B PRO 82  ? B 1.501 1.338 0.163  0.019 Y 
9  1 C  B GLY 81  ? C N B PRO 82  ? C 1.527 1.338 0.189  0.019 Y 
10 1 C  B GLY 81  ? D N B PRO 82  ? D 1.529 1.338 0.191  0.019 Y 
11 1 C  B GLU 94  ? ? O B GLU 94  ? ? 1.414 1.229 0.185  0.019 N 
12 1 C  B PRO 113 ? ? O B PRO 113 ? ? 1.389 1.228 0.161  0.020 N 
13 1 C  B LEU 149 ? A O B LEU 149 ? A 1.386 1.229 0.157  0.019 N 
14 1 C  B LEU 149 ? B O B LEU 149 ? B 1.390 1.229 0.161  0.019 N 
15 1 C  B LEU 149 ? C O B LEU 149 ? C 1.511 1.229 0.282  0.019 N 
16 1 C  B LEU 149 ? D O B LEU 149 ? D 1.507 1.229 0.278  0.019 N 
17 1 C  B TYR 150 ? A O B TYR 150 ? A 1.392 1.229 0.163  0.019 N 
18 1 C  B TYR 150 ? B O B TYR 150 ? B 1.394 1.229 0.165  0.019 N 
19 1 C  B GLY 151 ? C O B GLY 151 ? C 1.372 1.232 0.140  0.016 N 
20 1 C  B GLY 151 ? D O B GLY 151 ? D 1.372 1.232 0.140  0.016 N 
21 1 C  B ASN 152 ? A N B GLY 153 ? ? 1.588 1.336 0.252  0.023 Y 
22 1 C  B ASN 152 ? B N B GLY 153 ? ? 1.590 1.336 0.254  0.023 Y 
23 1 C  B ASN 152 ? C N B GLY 153 ? ? 1.626 1.336 0.290  0.023 Y 
24 1 C  B ASN 152 ? D N B GLY 153 ? ? 1.625 1.336 0.289  0.023 Y 
25 1 C  B ALA 164 ? C N B ILE 165 ? C 1.493 1.336 0.157  0.023 Y 
26 1 C  B ALA 164 ? D N B ILE 165 ? D 1.493 1.336 0.157  0.023 Y 
27 1 C  B THR 166 ? C O B THR 166 ? C 1.114 1.229 -0.115 0.019 N 
28 1 C  B THR 166 ? A N B GLN 167 ? A 1.488 1.336 0.152  0.023 Y 
29 1 C  B THR 166 ? B N B GLN 167 ? B 1.488 1.336 0.152  0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 O  A THR 60  ? B C A THR 60  ? B N A TRP 61  ? ? 139.16 122.70 16.46  1.60 Y 
2  1 O  A THR 60  ? D C A THR 60  ? D N A TRP 61  ? ? 139.16 122.70 16.46  1.60 Y 
3  1 CA A ALA 65  ? ? C A ALA 65  ? ? O A ALA 65  ? ? 105.46 120.10 -14.64 2.10 N 
4  1 CA B ASN 152 ? C C B ASN 152 ? C N B GLY 153 ? ? 103.17 116.20 -13.03 2.00 Y 
5  1 CA B ASN 152 ? D C B ASN 152 ? D N B GLY 153 ? ? 103.20 116.20 -13.00 2.00 Y 
6  1 O  B ASN 152 ? A C B ASN 152 ? A N B GLY 153 ? ? 137.05 123.20 13.85  1.70 Y 
7  1 O  B ASN 152 ? B C B ASN 152 ? B N B GLY 153 ? ? 137.05 123.20 13.85  1.70 Y 
8  1 O  B ASN 152 ? C C B ASN 152 ? C N B GLY 153 ? ? 137.48 123.20 14.28  1.70 Y 
9  1 O  B ASN 152 ? D C B ASN 152 ? D N B GLY 153 ? ? 137.59 123.20 14.39  1.70 Y 
10 1 O  B ALA 164 ? A C B ALA 164 ? A N B ILE 165 ? A 133.79 122.70 11.09  1.60 Y 
11 1 O  B ALA 164 ? B C B ALA 164 ? B N B ILE 165 ? B 133.62 122.70 10.92  1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 65  ? ? -48.47  159.86  
2  1 LEU B 30  ? ? -114.52 -165.55 
3  1 CYS B 80  ? C 85.78   -11.91  
4  1 CYS B 80  ? D 85.60   -12.09  
5  1 LEU B 92  ? ? -131.37 -44.89  
6  1 ALA B 127 ? ? -101.63 78.84   
7  1 ALA B 127 ? ? -108.29 78.84   
8  1 ALA B 127 ? ? -101.72 78.84   
9  1 ALA B 127 ? ? -108.39 78.84   
10 1 LYS B 157 ? A -28.38  -46.80  
11 1 LYS B 157 ? B -28.31  -46.83  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASP A 64  ? ? ALA A 65  ? ? 145.32 
2 1 ALA A 65  ? ? GLU A 66  ? ? 147.29 
3 1 ALA B 164 ? A ILE B 165 ? A 146.70 
4 1 ALA B 164 ? B ILE B 165 ? B 146.81 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ALA A 65  ? ? -12.06 
2 1 THR B 166 ? A -11.68 
3 1 THR B 166 ? B -11.72 
4 1 THR B 166 ? C -10.66 
5 1 THR B 166 ? D -10.75 
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C B ASN 152 ? D N B GLY 153 ? ? 1.62 
2 1 C B ASN 152 ? C N B GLY 153 ? ? 1.63 
# 
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 370 ? L HOH . 
2 1 B HOH 373 ? L HOH . 
3 1 B HOH 374 ? L 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 -13.3801 -1.8854 -19.2893 0.4230 0.4255 0.0846 0.1674 0.0699 0.0852  1.8809 1.4773 0.7171 -0.5370 
-0.6398 0.0341 0.2975 0.2728 0.3220 -0.2089 -0.2771 -0.2514 0.0060 0.1488 -0.0204 
'X-RAY DIFFRACTION' 2 ? refined -18.7864 0.9877  -15.8786 0.4266 0.4060 0.0853 0.1161 0.0355 -0.0032 1.1770 0.2210 0.4597 -0.2521 
-0.0410 0.0819 0.2171 0.1222 0.1532 -0.0785 -0.2015 0.0426  0.0790 0.0530 -0.0155 
# 
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 50 ? ? A 88  ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 304 ? ? ? ? 
# 
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 
A1BG2 N1   N Y N 1   
A1BG2 N3   N Y N 2   
A1BG2 C4   C Y N 3   
A1BG2 C5   C Y N 4   
A1BG2 C6   C Y N 5   
A1BG2 C7   C N N 6   
A1BG2 C8   C Y N 7   
A1BG2 C10  C Y N 8   
A1BG2 C13  C Y N 9   
A1BG2 C15  C Y N 10  
A1BG2 C1   C N N 11  
A1BG2 C2   C Y N 12  
A1BG2 C3   C Y N 13  
A1BG2 N2   N N N 14  
A1BG2 O1   O N N 15  
A1BG2 C9   C Y N 16  
A1BG2 C11  C Y N 17  
A1BG2 C12  C Y N 18  
A1BG2 C14  C Y N 19  
A1BG2 S1   S Y N 20  
A1BG2 C16  C Y N 21  
A1BG2 H5   H N N 22  
A1BG2 H6   H N N 23  
A1BG2 H9   H N N 24  
A1BG2 H12  H N N 25  
A1BG2 H1   H N N 26  
A1BG2 H3   H N N 27  
A1BG2 H2   H N N 28  
A1BG2 H4   H N N 29  
A1BG2 H7   H N N 30  
A1BG2 H8   H N N 31  
A1BG2 H10  H N N 32  
A1BG2 H11  H N N 33  
A1BG2 H13  H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
DMS   S    S N N 122 
DMS   O    O N N 123 
DMS   C1   C N N 124 
DMS   C2   C N N 125 
DMS   H11  H N N 126 
DMS   H12  H N N 127 
DMS   H13  H N N 128 
DMS   H21  H N N 129 
DMS   H22  H N N 130 
DMS   H23  H N N 131 
GLN   N    N N N 132 
GLN   CA   C N S 133 
GLN   C    C N N 134 
GLN   O    O N N 135 
GLN   CB   C N N 136 
GLN   CG   C N N 137 
GLN   CD   C N N 138 
GLN   OE1  O N N 139 
GLN   NE2  N N N 140 
GLN   OXT  O N N 141 
GLN   H    H N N 142 
GLN   H2   H N N 143 
GLN   HA   H N N 144 
GLN   HB2  H N N 145 
GLN   HB3  H N N 146 
GLN   HG2  H N N 147 
GLN   HG3  H N N 148 
GLN   HE21 H N N 149 
GLN   HE22 H N N 150 
GLN   HXT  H N N 151 
GLU   N    N N N 152 
GLU   CA   C N S 153 
GLU   C    C N N 154 
GLU   O    O N N 155 
GLU   CB   C N N 156 
GLU   CG   C N N 157 
GLU   CD   C N N 158 
GLU   OE1  O N N 159 
GLU   OE2  O N N 160 
GLU   OXT  O N N 161 
GLU   H    H N N 162 
GLU   H2   H N N 163 
GLU   HA   H N N 164 
GLU   HB2  H N N 165 
GLU   HB3  H N N 166 
GLU   HG2  H N N 167 
GLU   HG3  H N N 168 
GLU   HE2  H N N 169 
GLU   HXT  H N N 170 
GLY   N    N N N 171 
GLY   CA   C N N 172 
GLY   C    C N N 173 
GLY   O    O N N 174 
GLY   OXT  O N N 175 
GLY   H    H N N 176 
GLY   H2   H N N 177 
GLY   HA2  H N N 178 
GLY   HA3  H N N 179 
GLY   HXT  H N N 180 
HIS   N    N N N 181 
HIS   CA   C N S 182 
HIS   C    C N N 183 
HIS   O    O N N 184 
HIS   CB   C N N 185 
HIS   CG   C Y N 186 
HIS   ND1  N Y N 187 
HIS   CD2  C Y N 188 
HIS   CE1  C Y N 189 
HIS   NE2  N Y N 190 
HIS   OXT  O N N 191 
HIS   H    H N N 192 
HIS   H2   H N N 193 
HIS   HA   H N N 194 
HIS   HB2  H N N 195 
HIS   HB3  H N N 196 
HIS   HD1  H N N 197 
HIS   HD2  H N N 198 
HIS   HE1  H N N 199 
HIS   HE2  H N N 200 
HIS   HXT  H N N 201 
HOH   O    O N N 202 
HOH   H1   H N N 203 
HOH   H2   H N N 204 
ILE   N    N N N 205 
ILE   CA   C N S 206 
ILE   C    C N N 207 
ILE   O    O N N 208 
ILE   CB   C N S 209 
ILE   CG1  C N N 210 
ILE   CG2  C N N 211 
ILE   CD1  C N N 212 
ILE   OXT  O N N 213 
ILE   H    H N N 214 
ILE   H2   H N N 215 
ILE   HA   H N N 216 
ILE   HB   H N N 217 
ILE   HG12 H N N 218 
ILE   HG13 H N N 219 
ILE   HG21 H N N 220 
ILE   HG22 H N N 221 
ILE   HG23 H N N 222 
ILE   HD11 H N N 223 
ILE   HD12 H N N 224 
ILE   HD13 H N N 225 
ILE   HXT  H N N 226 
LEU   N    N N N 227 
LEU   CA   C N S 228 
LEU   C    C N N 229 
LEU   O    O N N 230 
LEU   CB   C N N 231 
LEU   CG   C N N 232 
LEU   CD1  C N N 233 
LEU   CD2  C N N 234 
LEU   OXT  O N N 235 
LEU   H    H N N 236 
LEU   H2   H N N 237 
LEU   HA   H N N 238 
LEU   HB2  H N N 239 
LEU   HB3  H N N 240 
LEU   HG   H N N 241 
LEU   HD11 H N N 242 
LEU   HD12 H N N 243 
LEU   HD13 H N N 244 
LEU   HD21 H N N 245 
LEU   HD22 H N N 246 
LEU   HD23 H N N 247 
LEU   HXT  H N N 248 
LYS   N    N N N 249 
LYS   CA   C N S 250 
LYS   C    C N N 251 
LYS   O    O N N 252 
LYS   CB   C N N 253 
LYS   CG   C N N 254 
LYS   CD   C N N 255 
LYS   CE   C N N 256 
LYS   NZ   N N N 257 
LYS   OXT  O N N 258 
LYS   H    H N N 259 
LYS   H2   H N N 260 
LYS   HA   H N N 261 
LYS   HB2  H N N 262 
LYS   HB3  H N N 263 
LYS   HG2  H N N 264 
LYS   HG3  H N N 265 
LYS   HD2  H N N 266 
LYS   HD3  H N N 267 
LYS   HE2  H N N 268 
LYS   HE3  H N N 269 
LYS   HZ1  H N N 270 
LYS   HZ2  H N N 271 
LYS   HZ3  H N N 272 
LYS   HXT  H N N 273 
MET   N    N N N 274 
MET   CA   C N S 275 
MET   C    C N N 276 
MET   O    O N N 277 
MET   CB   C N N 278 
MET   CG   C N N 279 
MET   SD   S N N 280 
MET   CE   C N N 281 
MET   OXT  O N N 282 
MET   H    H N N 283 
MET   H2   H N N 284 
MET   HA   H N N 285 
MET   HB2  H N N 286 
MET   HB3  H N N 287 
MET   HG2  H N N 288 
MET   HG3  H N N 289 
MET   HE1  H N N 290 
MET   HE2  H N N 291 
MET   HE3  H N N 292 
MET   HXT  H N N 293 
PHE   N    N N N 294 
PHE   CA   C N S 295 
PHE   C    C N N 296 
PHE   O    O N N 297 
PHE   CB   C N N 298 
PHE   CG   C Y N 299 
PHE   CD1  C Y N 300 
PHE   CD2  C Y N 301 
PHE   CE1  C Y N 302 
PHE   CE2  C Y N 303 
PHE   CZ   C Y N 304 
PHE   OXT  O N N 305 
PHE   H    H N N 306 
PHE   H2   H N N 307 
PHE   HA   H N N 308 
PHE   HB2  H N N 309 
PHE   HB3  H N N 310 
PHE   HD1  H N N 311 
PHE   HD2  H N N 312 
PHE   HE1  H N N 313 
PHE   HE2  H N N 314 
PHE   HZ   H N N 315 
PHE   HXT  H N N 316 
PRO   N    N N N 317 
PRO   CA   C N S 318 
PRO   C    C N N 319 
PRO   O    O N N 320 
PRO   CB   C N N 321 
PRO   CG   C N N 322 
PRO   CD   C N N 323 
PRO   OXT  O N N 324 
PRO   H    H N N 325 
PRO   HA   H N N 326 
PRO   HB2  H N N 327 
PRO   HB3  H N N 328 
PRO   HG2  H N N 329 
PRO   HG3  H N N 330 
PRO   HD2  H N N 331 
PRO   HD3  H N N 332 
PRO   HXT  H N N 333 
SER   N    N N N 334 
SER   CA   C N S 335 
SER   C    C N N 336 
SER   O    O N N 337 
SER   CB   C N N 338 
SER   OG   O N N 339 
SER   OXT  O N N 340 
SER   H    H N N 341 
SER   H2   H N N 342 
SER   HA   H N N 343 
SER   HB2  H N N 344 
SER   HB3  H N N 345 
SER   HG   H N N 346 
SER   HXT  H N N 347 
SO4   S    S N N 348 
SO4   O1   O N N 349 
SO4   O2   O N N 350 
SO4   O3   O N N 351 
SO4   O4   O N N 352 
THR   N    N N N 353 
THR   CA   C N S 354 
THR   C    C N N 355 
THR   O    O N N 356 
THR   CB   C N R 357 
THR   OG1  O N N 358 
THR   CG2  C N N 359 
THR   OXT  O N N 360 
THR   H    H N N 361 
THR   H2   H N N 362 
THR   HA   H N N 363 
THR   HB   H N N 364 
THR   HG1  H N N 365 
THR   HG21 H N N 366 
THR   HG22 H N N 367 
THR   HG23 H N N 368 
THR   HXT  H N N 369 
TRP   N    N N N 370 
TRP   CA   C N S 371 
TRP   C    C N N 372 
TRP   O    O N N 373 
TRP   CB   C N N 374 
TRP   CG   C Y N 375 
TRP   CD1  C Y N 376 
TRP   CD2  C Y N 377 
TRP   NE1  N Y N 378 
TRP   CE2  C Y N 379 
TRP   CE3  C Y N 380 
TRP   CZ2  C Y N 381 
TRP   CZ3  C Y N 382 
TRP   CH2  C Y N 383 
TRP   OXT  O N N 384 
TRP   H    H N N 385 
TRP   H2   H N N 386 
TRP   HA   H N N 387 
TRP   HB2  H N N 388 
TRP   HB3  H N N 389 
TRP   HD1  H N N 390 
TRP   HE1  H N N 391 
TRP   HE3  H N N 392 
TRP   HZ2  H N N 393 
TRP   HZ3  H N N 394 
TRP   HH2  H N N 395 
TRP   HXT  H N N 396 
TYR   N    N N N 397 
TYR   CA   C N S 398 
TYR   C    C N N 399 
TYR   O    O N N 400 
TYR   CB   C N N 401 
TYR   CG   C Y N 402 
TYR   CD1  C Y N 403 
TYR   CD2  C Y N 404 
TYR   CE1  C Y N 405 
TYR   CE2  C Y N 406 
TYR   CZ   C Y N 407 
TYR   OH   O N N 408 
TYR   OXT  O N N 409 
TYR   H    H N N 410 
TYR   H2   H N N 411 
TYR   HA   H N N 412 
TYR   HB2  H N N 413 
TYR   HB3  H N N 414 
TYR   HD1  H N N 415 
TYR   HD2  H N N 416 
TYR   HE1  H N N 417 
TYR   HE2  H N N 418 
TYR   HH   H N N 419 
TYR   HXT  H N N 420 
VAL   N    N N N 421 
VAL   CA   C N S 422 
VAL   C    C N N 423 
VAL   O    O N N 424 
VAL   CB   C N N 425 
VAL   CG1  C N N 426 
VAL   CG2  C N N 427 
VAL   OXT  O N N 428 
VAL   H    H N N 429 
VAL   H2   H N N 430 
VAL   HA   H N N 431 
VAL   HB   H N N 432 
VAL   HG11 H N N 433 
VAL   HG12 H N N 434 
VAL   HG13 H N N 435 
VAL   HG21 H N N 436 
VAL   HG22 H N N 437 
VAL   HG23 H N N 438 
VAL   HXT  H N N 439 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BG2 C1  C2   sing N N 1   
A1BG2 C2  C3   doub Y N 2   
A1BG2 C3  N1   sing Y N 3   
A1BG2 N1  C4   doub Y N 4   
A1BG2 C4  C5   sing Y N 5   
A1BG2 C5  C6   doub Y N 6   
A1BG2 C6  N2   sing N N 7   
A1BG2 N2  C7   sing N N 8   
A1BG2 C7  O1   doub N N 9   
A1BG2 C7  C8   sing N N 10  
A1BG2 C8  C9   doub Y N 11  
A1BG2 C9  C10  sing Y N 12  
A1BG2 C10 C11  doub Y N 13  
A1BG2 C11 C12  sing Y N 14  
A1BG2 C12 C13  sing N N 15  
A1BG2 C13 N3   doub Y N 16  
A1BG2 N3  C14  sing Y N 17  
A1BG2 C14 C15  doub Y N 18  
A1BG2 C15 S1   sing Y N 19  
A1BG2 C12 C16  doub Y N 20  
A1BG2 C2  C6   sing Y N 21  
A1BG2 C8  C16  sing Y N 22  
A1BG2 C13 S1   sing Y N 23  
A1BG2 C4  H5   sing N N 24  
A1BG2 C5  H6   sing N N 25  
A1BG2 C10 H9   sing N N 26  
A1BG2 C15 H12  sing N N 27  
A1BG2 C1  H1   sing N N 28  
A1BG2 C1  H3   sing N N 29  
A1BG2 C1  H2   sing N N 30  
A1BG2 C3  H4   sing N N 31  
A1BG2 N2  H7   sing N N 32  
A1BG2 C9  H8   sing N N 33  
A1BG2 C11 H10  sing N N 34  
A1BG2 C14 H11  sing N N 35  
A1BG2 C16 H13  sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
DMS   S   O    doub N N 119 
DMS   S   C1   sing N N 120 
DMS   S   C2   sing N N 121 
DMS   C1  H11  sing N N 122 
DMS   C1  H12  sing N N 123 
DMS   C1  H13  sing N N 124 
DMS   C2  H21  sing N N 125 
DMS   C2  H22  sing N N 126 
DMS   C2  H23  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
SO4   S   O1   doub N N 335 
SO4   S   O2   doub N N 336 
SO4   S   O3   sing N N 337 
SO4   S   O4   sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    7HOT 
_atom_sites.fract_transf_matrix[1][1]   0.023522 
_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]   0.023522 
_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]   0.004620 
_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   ? -20.748 19.101  -7.600  1.00 60.40  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.058 18.393  -7.617  1.00 58.26  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.213 17.682  -8.969  1.00 54.99  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.016 18.326  -10.037 1.00 56.81  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.190 19.369  -7.310  1.00 60.21  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.514 18.701  -7.011  1.00 60.47  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.656 18.118  -5.900  1.00 62.39  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.405 18.782  -7.885  1.00 61.49  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.488 16.386  -8.925  1.00 49.93  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.379 15.506  -10.106 1.00 46.85  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.792 15.237  -10.611 1.00 44.47  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.704 15.124  -9.775  1.00 42.62  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.691 14.183  -9.766  1.00 46.02  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.235 14.339  -9.470  1.00 46.75  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.466 12.739  -9.210  1.00 46.03  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.756 13.250  -9.064  1.00 47.46  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.958 15.138  -11.931 1.00 41.97  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.255 14.863  -12.595 1.00 40.80  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.024 13.910  -13.770 1.00 39.51  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.906 13.774  -14.239 1.00 38.40  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.925 16.169  -13.024 1.00 41.88  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.149 16.952  -14.043 1.00 43.30  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.121 17.789  -13.649 1.00 44.11  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.411 16.824  -15.404 1.00 43.80  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.390 18.514  -14.569 1.00 45.67  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.688 17.547  -16.344 1.00 45.07  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.670 18.392  -15.922 1.00 46.17  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.901 19.085  -16.816 1.00 47.65  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.085 13.212  -14.156 1.00 38.92  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.050 12.208  -15.250 1.00 38.33  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.866 12.711  -16.451 1.00 39.21  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.864 13.437  -16.253 1.00 38.89  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.495 10.816  -14.775 1.00 37.20  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -27.934 10.748  -14.286 1.00 36.95  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.528 10.262  -13.749 1.00 36.81  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.360 9.337   -14.067 1.00 36.41  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.389 12.345  -17.653 1.00 39.65  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -26.981 12.661  -18.995 1.00 40.94  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.032 11.331  -19.762 1.00 39.61  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.003 10.628  -19.758 1.00 37.84  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.105 13.634  -19.787 1.00 42.93  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.210 15.089  -19.409 1.00 45.12  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.180 15.979  -20.106 1.00 47.67  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.275 15.464  -20.816 1.00 49.30  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.259 17.198  -19.933 1.00 50.72  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.195 10.933  -20.291 1.00 40.26  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.298 9.685   -21.105 1.00 40.77  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.397 9.819   -22.331 1.00 40.82  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.360 10.936  -22.893 1.00 42.33  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.707 9.420   -21.626 1.00 42.01  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -29.940 7.970   -22.021 1.00 42.30  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.410 7.572   -21.911 1.00 43.37  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.642 6.163   -22.164 1.00 43.48  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.525 5.607   -23.385 1.00 44.21  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.131 6.342   -24.402 1.00 45.90  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.713 4.309   -23.564 1.00 43.52  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.678 8.755   -22.695 1.00 40.26  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.792 8.720   -23.893 1.00 40.97  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.203 7.649   -24.904 1.00 41.25  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.613 7.675   -26.009 1.00 41.68  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.351 8.512   -23.514 1.00 40.51  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.095 6.716   -24.580 1.00 40.47  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.454 5.682   -25.560 1.00 41.20  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.140 4.493   -24.960 1.00 40.63  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.174 4.358   -23.640 1.00 37.73  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.632 3.632   -25.858 1.00 41.67  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.160 2.284   -25.530 1.00 42.69  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -27.963 1.370   -25.347 1.00 43.25  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.894 1.639   -25.959 1.00 45.38  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.093 1.715   -26.599 1.00 43.99  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.430 2.408   -26.672 1.00 45.30  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.618 3.388   -25.932 1.00 44.95  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.283 1.980   -27.485 1.00 46.33  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.142 0.299   -24.590 1.00 42.99  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.123 -0.775  -24.469 1.00 43.31  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.526 -1.912  -25.431 1.00 44.29  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.538 -2.641  -25.192 1.00 43.76  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -26.947 -1.169  -23.008 1.00 42.11  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.320 -0.002  -22.235 1.00 41.71  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.103 -2.416  -22.928 1.00 42.79  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.499 -0.088  -20.724 1.00 40.90  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.769 -2.022  -26.529 0.25 45.28  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.771 -2.060  -26.524 0.25 45.13  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.769 -2.022  -26.529 0.25 45.28  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.771 -2.060  -26.524 0.25 45.13  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.057 -2.907  -27.691 0.25 46.53  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.123 -2.979  -27.640 0.25 46.24  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.057 -2.907  -27.691 0.25 46.53  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.123 -2.979  -27.640 0.25 46.24  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.769 -3.367  -28.438 0.25 47.08  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -25.918 -3.331  -28.606 0.25 47.10  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.769 -3.367  -28.438 0.25 47.08  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -25.918 -3.331  -28.606 0.25 47.10  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.875 -2.426  -28.640 0.25 47.93  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.247 -2.252  -28.825 0.25 47.79  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.875 -2.426  -28.640 0.25 47.93  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.247 -2.252  -28.825 0.25 47.79  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -27.865 -2.176  -28.766 0.25 47.79  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.205 -2.352  -28.525 0.25 47.22  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -27.865 -2.176  -28.766 0.25 47.79  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.205 -2.352  -28.525 0.25 47.22  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -26.971 -1.349  -29.509 0.25 48.55  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.433 -2.310  -27.790 0.25 46.32  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -26.971 -1.349  -29.509 0.25 48.55  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.433 -2.310  -27.790 0.25 46.32  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -28.970 -1.317  -28.199 0.25 47.70  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.376 -3.120  -29.813 0.25 48.70  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -28.970 -1.317  -28.199 0.25 47.70  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.376 -3.120  -29.813 0.25 48.70  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.732 -4.729  -28.640 1.00 46.95  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.702 -5.293  -29.541 1.00 47.98  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -24.926 -4.699  -30.943 1.00 51.21  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.090 -4.632  -31.396 1.00 52.42  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.748 -6.816  -29.517 1.00 46.77  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.636 -7.419  -30.306 1.00 47.58  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.635 -7.597  -31.664 1.00 48.14  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.384 -7.943  -29.824 1.00 46.34  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.451 -8.162  -32.058 1.00 48.53  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.672 -8.408  -30.956 1.00 47.57  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.783 -8.055  -28.568 1.00 44.63  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.398 -8.972  -30.863 1.00 47.81  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.531 -8.620  -28.481 1.00 44.61  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -19.848 -9.078  -29.598 1.00 46.35  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -23.846 -4.294  -31.614 0.25 51.94  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -23.846 -4.294  -31.614 0.25 51.94  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -23.845 -4.205  -31.567 0.25 51.73  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -23.845 -4.205  -31.567 0.25 51.73  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -23.898 -3.689  -32.970 0.25 54.24  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -23.898 -3.689  -32.970 0.25 54.24  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -23.824 -3.694  -32.967 0.25 53.96  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -23.824 -3.694  -32.967 0.25 53.96  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.069 -4.542  -33.940 0.25 56.02  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.069 -4.542  -33.940 0.25 56.02  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.093 -4.690  -33.870 0.25 55.76  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.093 -4.690  -33.870 0.25 55.76  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -21.840 -4.655  -33.741 0.25 55.10  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -21.840 -4.655  -33.741 0.25 55.10  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -21.939 -5.047  -33.562 0.25 54.96  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -21.939 -5.047  -33.562 0.25 54.96  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.432 -2.232  -32.905 0.25 54.11  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.432 -2.232  -32.905 0.25 54.11  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.113 -2.344  -33.114 0.25 53.80  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.113 -2.344  -33.114 0.25 53.80  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.392 -1.323  -32.143 0.25 53.38  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.392 -1.323  -32.143 0.25 53.38  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.346 -1.725  -34.492 0.25 55.62  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.346 -1.725  -34.492 0.25 55.62  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.778 -1.176  -32.752 0.25 54.37  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.778 -1.176  -32.752 0.25 54.37  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.305 -0.746  -35.017 0.25 56.16  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.305 -0.746  -35.017 0.25 56.16  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -25.850 -0.909  -33.990 0.25 55.71  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -25.850 -0.909  -33.990 0.25 55.71  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -21.572 -0.156  -34.202 0.25 55.24  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -21.572 -0.156  -34.202 0.25 55.24  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -26.781 -1.326  -31.985 0.25 53.06  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.781 -1.326  -31.985 0.25 53.06  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.234 -0.573  -36.257 0.25 57.93  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.234 -0.573  -36.257 0.25 57.93  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -23.717 -5.080  -34.985 1.00 58.65  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.053 -5.965  -35.975 1.00 62.12  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -22.075 -5.114  -36.773 1.00 63.39  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -22.377 -3.948  -37.041 1.00 64.83  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -24.091 -6.651  -36.851 1.00 67.63  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -24.847 -7.763  -36.140 1.00 70.26  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -26.141 -8.114  -36.867 1.00 74.89  ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -26.686 -9.475  -36.484 1.00 77.31  ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -28.161 -9.431  -36.328 1.00 78.45  ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -20.910 -5.650  -37.079 1.00 65.37  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -19.861 -4.861  -37.776 1.00 69.46  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -19.641 -3.531  -37.031 1.00 67.86  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -19.545 -2.468  -37.712 1.00 67.29  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -20.201 -4.505  -39.236 1.00 76.02  ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -20.569 -5.635  -40.197 1.00 80.80  ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -19.707 -5.938  -41.125 1.00 81.46  ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -21.756 -6.139  -40.084 1.00 85.47  ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -19.524 -3.567  -35.703 1.00 62.83  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -18.608 -2.612  -35.026 1.00 62.34  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.259 -2.581  -35.681 1.00 62.22  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -17.022 -3.683  -35.953 1.00 64.44  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -18.450 -3.050  -33.489 1.00 60.21  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -16.358 -1.557  -35.553 1.00 61.18  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -14.847 -1.598  -35.542 1.00 61.93  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -14.339 -2.694  -34.548 1.00 59.25  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -14.930 -2.797  -33.477 1.00 53.18  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -14.309 -0.259  -35.016 1.00 66.13  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -12.792 -0.150  -35.125 1.00 70.43  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -12.141 0.982   -34.331 1.00 75.17  ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -12.849 2.007   -34.019 1.00 77.92  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -10.917 0.833   -34.024 1.00 77.92  ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -13.301 -3.494  -34.933 1.00 57.57  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -12.766 -4.626  -34.097 1.00 56.64  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -11.285 -4.348  -33.839 1.00 55.60  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -10.560 -4.146  -34.817 1.00 56.17  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.007 -6.005  -34.743 1.00 57.70  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -12.463 -7.144  -33.903 1.00 56.14  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -14.487 -6.229  -35.038 1.00 58.76  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -10.855 -4.340  -32.559 1.00 52.62  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -9.472  -3.949  -32.186 1.00 52.36  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -9.140  -4.377  -30.731 1.00 51.16  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.063 -4.877  -29.924 1.00 48.57  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -9.301  -2.445  -32.468 1.00 53.34  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -7.908  -2.164  -32.545 1.00 55.56  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -9.933  -1.538  -31.437 1.00 52.67  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -7.869  -4.183  -30.358 1.00 51.87  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -7.359  -4.608  -29.043 1.00 51.28  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -6.746  -5.984  -29.171 1.00 52.27  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -7.157  -6.743  -30.113 1.00 53.69  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -5.774  -6.277  -28.288 1.00 51.76  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -5.148  -7.618  -28.186 1.00 51.65  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -5.676  -8.286  -26.900 1.00 49.00  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -6.632  -7.711  -26.282 1.00 47.12  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -3.631  -7.467  -28.338 1.00 53.71  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -3.017  -6.801  -27.122 1.00 53.18  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -3.447  -5.723  -26.717 1.00 52.67  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -2.006  -7.432  -26.548 1.00 54.70  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -5.177  -9.478  -26.559 1.00 48.80  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -5.728  -10.371 -25.494 1.00 48.88  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -4.671  -10.777 -24.471 1.00 48.92  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -4.450  -11.964 -24.254 1.00 49.28  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -6.364  -11.598 -26.074 1.00 49.26  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -7.403  -11.243 -26.966 1.00 52.14  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.009  -9.829  -23.778 1.00 48.75  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -2.838  -10.158 -22.967 1.00 48.92  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.244  -10.981 -21.737 1.00 47.65  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.326  -10.752 -21.210 1.00 45.48  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.256  -8.771  -22.644 1.00 48.92  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -3.488  -7.893  -22.577 1.00 48.48  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -4.346  -8.397  -23.728 1.00 49.18  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -2.416  -11.960 -21.393 1.00 49.68  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -2.515  -12.757 -20.138 1.00 51.69  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -1.534  -12.172 -19.106 1.00 49.19  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -0.331  -12.335 -19.292 1.00 47.77  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -2.248  -14.245 -20.397 1.00 56.81  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -3.306  -14.939 -21.253 1.00 61.12  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -2.915  -16.351 -21.719 1.00 66.68  ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -3.837  -16.961 -22.703 1.00 70.99  ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -4.973  -17.606 -22.396 1.00 69.76  ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -5.357  -17.693 -21.127 1.00 70.42  ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -5.741  -18.118 -23.353 1.00 64.52  ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.035  -11.513 -18.050 1.00 45.98  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.160  -10.764 -17.120 1.00 45.63  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.373  -11.281 -15.686 1.00 43.74  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -2.519  -11.413 -15.277 1.00 42.14  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -1.463  -9.269  -17.222 1.00 45.20  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.178  -8.605  -18.576 1.00 45.86  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -1.754  -7.197  -18.592 1.00 45.45  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? 0.318   -8.576  -18.862 1.00 46.88  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.288  -11.558 -14.988 1.00 44.47  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.295  -11.756 -13.517 1.00 45.13  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.498  -10.415 -12.829 1.00 43.60  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.367   -9.496  -13.031 1.00 44.03  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 1.006   -12.393 -13.070 1.00 47.91  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 1.116   -13.817 -13.562 1.00 50.54  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? 0.082   -14.536 -13.539 1.00 51.87  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 2.220   -14.178 -13.991 1.00 55.19  ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.565  -10.321 -12.028 1.00 42.05  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -1.907  -9.053  -11.323 1.00 41.38  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.259  -9.362  -9.848  1.00 41.13  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.605  -10.543 -9.492  1.00 40.04  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -2.998  -8.227  -12.046 1.00 40.66  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -2.741  -8.066  -13.556 1.00 41.04  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.397  -8.786  -11.837 1.00 39.82  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.146  -8.324  -9.026  1.00 40.80  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.490  -8.322  -7.584  1.00 40.52  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.503  -7.205  -7.354  1.00 39.48  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.395  -6.194  -8.037  1.00 39.81  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.241  -8.108  -6.785  1.00 42.13  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.472  -7.394  -6.459  1.00 38.90  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.514  -6.386  -6.155  1.00 37.96  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.357  -5.967  -4.691  1.00 38.61  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.472  -6.858  -3.813  1.00 38.85  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.896  -6.990  -6.439  1.00 36.96  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.098  -6.088  -6.160  1.00 36.25  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.036  -4.791  -6.935  1.00 36.12  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.399  -6.819  -6.409  1.00 35.37  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -5.027  -4.699  -4.441  1.00 38.80  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.772  -4.238  -3.044  1.00 39.67  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.095  -3.816  -2.394  1.00 38.96  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.151  -3.794  -3.061  1.00 36.60  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.683  -3.169  -3.014  1.00 41.05  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -4.096  -1.791  -3.519  1.00 41.01  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.308  -1.562  -3.754  1.00 40.30  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.189  -0.954  -3.665  1.00 42.30  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.052  -3.534  -1.081  1.00 40.00  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.266  -3.228  -0.305  1.00 40.42  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.908  -1.921  -0.806  1.00 39.81  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.142  -1.788  -0.646  1.00 39.19  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.879  -3.222  1.180   1.00 42.35  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -8.064  -2.977  2.086   1.00 43.52  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.721  -2.968  3.568   1.00 45.69  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.340  -1.888  4.133   1.00 47.83  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.769  -4.064  4.155   1.00 47.45  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.144  -1.004  -1.427  1.00 40.39  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.688  0.252   -2.006  1.00 40.35  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.234  0.013   -3.419  1.00 39.19  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.576  1.011   -4.062  1.00 39.32  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.672  1.350   -2.043  1.00 42.12  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -6.058  1.506   -0.781  1.00 44.54  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.406  -1.236  -3.867  1.00 38.45  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -9.014  -1.502  -5.196  1.00 37.68  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -8.112  -1.156  -6.384  1.00 38.34  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.656  -1.071  -7.512  1.00 36.65  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.796  -1.043  -6.168  1.00 40.05  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.773  -0.751  -7.208  1.00 41.45  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -5.140  -2.081  -7.613  1.00 40.70  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.620  -2.789  -6.742  1.00 39.61  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.732  0.275   -6.730  1.00 44.09  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.356  1.598   -6.302  1.00 45.98  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.209  2.112   -7.024  1.00 46.70  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -5.046  2.063   -5.198  1.00 49.96  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.199  -2.400  -8.903  1.00 39.30  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.475  -3.529  -9.538  1.00 39.18  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.027  -3.137  -9.801  1.00 40.80  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.768  -1.974  -10.105 1.00 41.35  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.122  -3.904  -10.866 1.00 37.74  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.411  -4.664  -10.750 1.00 36.06  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.412  -5.998  -10.400 1.00 35.63  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.623  -4.056  -11.023 1.00 35.61  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.601  -6.701  -10.313 1.00 34.91  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -8.814  -4.767  -10.948 1.00 34.76  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -8.798  -6.091  -10.611 1.00 34.31  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.119  -4.103  -9.719  1.00 42.34  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.679  -3.917  -9.982  1.00 44.56  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.142  -5.153  -10.715 1.00 45.66  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.746  -6.266  -10.609 1.00 44.32  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? 0.069   -3.634  -8.707  1.00 46.30  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? -0.095  -4.685  -7.760  1.00 45.97  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.929   -4.962  -11.484 1.00 48.36  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.547   -6.086  -12.227 1.00 50.45  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.485   -6.807  -11.279 1.00 51.86  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.419   -6.170  -10.790 1.00 52.23  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.310   -5.574  -13.451 1.00 51.86  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.427   -5.182  -14.628 1.00 52.03  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 2.250   -4.433  -15.658 1.00 54.20  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.781   -6.423  -15.239 1.00 51.89  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.247   -8.097  -11.105 1.00 54.12  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 3.191   -9.064  -10.474 1.00 57.85  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 4.215   -9.473  -11.537 1.00 62.20  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.808   -9.737  -12.696 1.00 65.53  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.404   -10.288 -9.985  1.00 56.64  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.316   -11.384 -9.459  1.00 57.78  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.343   -9.885  -8.972  1.00 55.72  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.490   -9.535  -11.196 1.00 67.57  ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.496   -10.167 -12.094 1.00 72.31  ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.472   -11.003 -11.251 1.00 74.38  ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 7.097   -11.854 -10.434 1.00 72.72  ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 7.201   -9.087  -12.911 1.00 74.81  ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.273   -8.295  -13.822 1.00 76.46  ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.149   -8.857  -15.225 1.00 76.10  ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.162   -10.097 -15.364 1.00 76.00  ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 6.087   -8.051  -16.170 1.00 79.57  ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.620 12.167  -11.947 1.00 60.08  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.409 12.111  -12.836 1.00 60.34  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -35.544 11.085  -13.960 1.00 57.92  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -36.515 10.288  -13.943 1.00 60.19  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -34.590 11.067  -14.896 1.00 54.49  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -34.593 10.115  -16.038 1.00 50.90  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.212 8.716   -15.527 1.00 47.22  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.109 8.527   -15.003 1.00 46.47  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -33.646 10.576  -17.147 1.00 53.03  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -33.750 9.727   -18.400 1.00 53.56  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -33.038 10.336  -19.596 1.00 55.63  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -32.093 11.157  -19.394 1.00 54.39  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -33.452 10.011  -20.742 1.00 61.50  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.116 7.750   -15.696 0.25 46.48  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.132 7.763   -15.688 0.25 46.25  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.116 7.750   -15.696 0.25 46.48  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.132 7.763   -15.688 0.25 46.25  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -34.975 6.367   -15.174 0.25 45.66  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -35.025 6.376   -15.169 0.25 45.27  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -34.975 6.367   -15.174 0.25 45.66  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -35.025 6.376   -15.169 0.25 45.27  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -35.023 5.350   -16.316 0.25 44.92  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -34.777 5.399   -16.325 0.25 44.66  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -35.023 5.350   -16.316 0.25 44.92  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -34.777 5.399   -16.325 0.25 44.66  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -35.059 4.145   -16.012 0.25 44.99  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -34.273 4.294   -16.050 0.25 44.40  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -35.059 4.145   -16.012 0.25 44.99  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -34.273 4.294   -16.050 0.25 44.40  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -36.073 6.073   -14.146 0.25 45.85  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -36.266 6.034   -14.331 0.25 45.25  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -36.073 6.073   -14.146 0.25 45.85  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -36.266 6.034   -14.331 0.25 45.25  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -36.424 7.327   -13.559 0.25 46.23  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.436 6.358   -15.085 0.25 45.24  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -36.424 7.327   -13.559 0.25 46.23  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.436 6.358   -15.085 0.25 45.24  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.647 5.070   -13.093 0.25 45.68  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -36.299 6.778   -13.012 0.25 45.33  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.647 5.070   -13.093 0.25 45.68  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -36.299 6.778   -13.012 0.25 45.33  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -35.044 5.805   -17.574 1.00 44.45  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -34.941 4.911   -18.748 1.00 42.80  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -33.632 4.113   -18.720 1.00 40.27  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -32.571 4.739   -18.596 1.00 41.44  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -34.995 5.709   -20.064 1.00 42.93  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.092 6.631   -20.044 1.00 43.76  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -35.185 4.788   -21.234 1.00 43.20  ? 19  THR   B CG2 1 
ATOM   401  N N   . ASP   B 2 11  ? -33.702 2.793   -18.868 1.00 38.33  ? 20  ASP   B N   1 
ATOM   402  C CA  . ASP   B 2 11  ? -32.516 1.926   -19.062 1.00 37.79  ? 20  ASP   B CA  1 
ATOM   403  C C   . ASP   B 2 11  ? -31.566 2.550   -20.098 1.00 38.20  ? 20  ASP   B C   1 
ATOM   404  O O   . ASP   B 2 11  ? -32.085 3.193   -21.069 1.00 38.46  ? 20  ASP   B O   1 
ATOM   405  C CB  . ASP   B 2 11  ? -32.929 0.523   -19.503 1.00 38.32  ? 20  ASP   B CB  1 
ATOM   406  C CG  . ASP   B 2 11  ? -33.526 -0.400  -18.443 1.00 39.06  ? 20  ASP   B CG  1 
ATOM   407  O OD1 . ASP   B 2 11  ? -33.709 0.050   -17.317 1.00 37.19  ? 20  ASP   B OD1 1 
ATOM   408  O OD2 . ASP   B 2 11  ? -33.787 -1.585  -18.791 1.00 40.30  ? 20  ASP   B OD2 1 
ATOM   409  N N   . GLY   B 2 12  ? -30.255 2.321   -19.971 1.00 36.38  ? 21  GLY   B N   1 
ATOM   410  C CA  . GLY   B 2 12  ? -29.267 2.730   -20.982 1.00 35.75  ? 21  GLY   B CA  1 
ATOM   411  C C   . GLY   B 2 12  ? -27.979 3.166   -20.342 1.00 34.78  ? 21  GLY   B C   1 
ATOM   412  O O   . GLY   B 2 12  ? -27.814 2.984   -19.084 1.00 33.43  ? 21  GLY   B O   1 
ATOM   413  N N   . VAL   B 2 13  ? -27.083 3.725   -21.146 1.00 33.56  ? 22  VAL   B N   1 
ATOM   414  C CA  . VAL   B 2 13  ? -25.742 4.199   -20.697 1.00 33.02  ? 22  VAL   B CA  1 
ATOM   415  C C   . VAL   B 2 13  ? -25.853 5.708   -20.496 1.00 33.36  ? 22  VAL   B C   1 
ATOM   416  O O   . VAL   B 2 13  ? -26.677 6.352   -21.168 1.00 34.64  ? 22  VAL   B O   1 
ATOM   417  C CB  . VAL   B 2 13  ? -24.626 3.734   -21.647 1.00 32.88  ? 22  VAL   B CB  1 
ATOM   418  C CG1 . VAL   B 2 13  ? -24.790 4.318   -23.098 1.00 33.03  ? 22  VAL   B CG1 1 
ATOM   419  C CG2 . VAL   B 2 13  ? -23.235 4.013   -21.120 1.00 32.72  ? 22  VAL   B CG2 1 
ATOM   420  N N   . TYR   B 2 14  ? -25.170 6.249   -19.489 1.00 32.95  ? 23  TYR   B N   1 
ATOM   421  C CA  . TYR   B 2 14  ? -25.240 7.668   -19.091 1.00 33.10  ? 23  TYR   B CA  1 
ATOM   422  C C   . TYR   B 2 14  ? -23.846 8.191   -18.816 1.00 33.12  ? 23  TYR   B C   1 
ATOM   423  O O   . TYR   B 2 14  ? -22.979 7.461   -18.288 1.00 32.68  ? 23  TYR   B O   1 
ATOM   424  C CB  . TYR   B 2 14  ? -26.048 7.849   -17.800 1.00 33.06  ? 23  TYR   B CB  1 
ATOM   425  C CG  . TYR   B 2 14  ? -27.513 7.637   -17.988 1.00 33.20  ? 23  TYR   B CG  1 
ATOM   426  C CD1 . TYR   B 2 14  ? -28.019 6.395   -18.370 1.00 33.07  ? 23  TYR   B CD1 1 
ATOM   427  C CD2 . TYR   B 2 14  ? -28.374 8.699   -17.750 1.00 33.86  ? 23  TYR   B CD2 1 
ATOM   428  C CE1 . TYR   B 2 14  ? -29.374 6.207   -18.545 1.00 33.58  ? 23  TYR   B CE1 1 
ATOM   429  C CE2 . TYR   B 2 14  ? -29.740 8.527   -17.873 1.00 34.46  ? 23  TYR   B CE2 1 
ATOM   430  C CZ  . TYR   B 2 14  ? -30.232 7.285   -18.282 1.00 34.64  ? 23  TYR   B CZ  1 
ATOM   431  O OH  . TYR   B 2 14  ? -31.589 7.194   -18.420 1.00 36.50  ? 23  TYR   B OH  1 
ATOM   432  N N   . ARG   B 2 15  ? -23.660 9.469   -19.117 1.00 33.88  ? 24  ARG   B N   1 
ATOM   433  C CA  . ARG   B 2 15  ? -22.440 10.207  -18.735 1.00 34.27  ? 24  ARG   B CA  1 
ATOM   434  C C   . ARG   B 2 15  ? -22.594 10.692  -17.287 1.00 34.33  ? 24  ARG   B C   1 
ATOM   435  O O   . ARG   B 2 15  ? -23.687 11.122  -16.915 1.00 33.65  ? 24  ARG   B O   1 
ATOM   436  C CB  . ARG   B 2 15  ? -22.217 11.411  -19.636 1.00 35.15  ? 24  ARG   B CB  1 
ATOM   437  C CG  . ARG   B 2 15  ? -22.154 11.054  -21.117 1.00 35.62  ? 24  ARG   B CG  1 
ATOM   438  C CD  . ARG   B 2 15  ? -22.009 12.335  -21.904 1.00 36.76  ? 24  ARG   B CD  1 
ATOM   439  N NE  . ARG   B 2 15  ? -22.154 12.060  -23.342 1.00 37.48  ? 24  ARG   B NE  1 
ATOM   440  C CZ  . ARG   B 2 15  ? -21.141 11.793  -24.171 1.00 37.89  ? 24  ARG   B CZ  1 
ATOM   441  N NH1 . ARG   B 2 15  ? -19.893 11.851  -23.733 1.00 37.52  ? 24  ARG   B NH1 1 
ATOM   442  N NH2 . ARG   B 2 15  ? -21.390 11.498  -25.443 1.00 38.53  ? 24  ARG   B NH2 1 
ATOM   443  N N   . VAL   B 2 16  ? -21.472 10.724  -16.584 1.00 34.90  ? 25  VAL   B N   1 
ATOM   444  C CA  . VAL   B 2 16  ? -21.354 11.313  -15.230 1.00 35.09  ? 25  VAL   B CA  1 
ATOM   445  C C   . VAL   B 2 16  ? -20.499 12.582  -15.295 1.00 35.92  ? 25  VAL   B C   1 
ATOM   446  O O   . VAL   B 2 16  ? -19.307 12.490  -15.591 1.00 36.46  ? 25  VAL   B O   1 
ATOM   447  C CB  . VAL   B 2 16  ? -20.778 10.260  -14.267 1.00 34.91  ? 25  VAL   B CB  1 
ATOM   448  C CG1 . VAL   B 2 16  ? -20.735 10.837  -12.849 1.00 34.83  ? 25  VAL   B CG1 1 
ATOM   449  C CG2 . VAL   B 2 16  ? -21.592 8.964   -14.312 1.00 34.57  ? 25  VAL   B CG2 1 
ATOM   450  N N   . MET   B 2 17  ? -21.113 13.717  -14.998 1.00 37.21  ? 26  MET   B N   1 
ATOM   451  C CA  . MET   B 2 17  ? -20.580 15.075  -15.220 1.00 39.32  ? 26  MET   B CA  1 
ATOM   452  C C   . MET   B 2 17  ? -20.439 15.801  -13.871 1.00 40.97  ? 26  MET   B C   1 
ATOM   453  O O   . MET   B 2 17  ? -21.223 15.514  -12.952 1.00 39.57  ? 26  MET   B O   1 
ATOM   454  C CB  . MET   B 2 17  ? -21.561 15.869  -16.079 1.00 40.12  ? 26  MET   B CB  1 
ATOM   455  C CG  . MET   B 2 17  ? -21.972 15.164  -17.388 1.00 40.73  ? 26  MET   B CG  1 
ATOM   456  S SD  . MET   B 2 17  ? -20.633 14.930  -18.615 1.00 40.84  ? 26  MET   B SD  1 
ATOM   457  C CE  . MET   B 2 17  ? -20.059 16.622  -18.732 1.00 42.42  ? 26  MET   B CE  1 
ATOM   458  N N   . THR   B 2 18  ? -19.509 16.745  -13.805 1.00 43.54  ? 27  THR   B N   1 
ATOM   459  C CA  . THR   B 2 18  ? -19.344 17.709  -12.702 1.00 47.21  ? 27  THR   B CA  1 
ATOM   460  C C   . THR   B 2 18  ? -19.174 19.125  -13.272 1.00 50.65  ? 27  THR   B C   1 
ATOM   461  O O   . THR   B 2 18  ? -18.574 19.270  -14.366 1.00 48.27  ? 27  THR   B O   1 
ATOM   462  C CB  . THR   B 2 18  ? -18.159 17.314  -11.813 1.00 47.00  ? 27  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 18  ? -18.212 18.246  -10.731 1.00 48.76  ? 27  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 18  ? -16.821 17.359  -12.514 1.00 47.33  ? 27  THR   B CG2 1 
ATOM   465  N N   . ARG   B 2 19  ? -19.633 20.134  -12.523 1.00 54.87  ? 28  ARG   B N   1 
ATOM   466  C CA  . ARG   B 2 19  ? -19.355 21.558  -12.843 1.00 60.24  ? 28  ARG   B CA  1 
ATOM   467  C C   . ARG   B 2 19  ? -18.340 22.150  -11.850 1.00 61.65  ? 28  ARG   B C   1 
ATOM   468  O O   . ARG   B 2 19  ? -18.033 23.339  -11.976 1.00 62.04  ? 28  ARG   B O   1 
ATOM   469  C CB  . ARG   B 2 19  ? -20.684 22.307  -12.938 1.00 63.26  ? 28  ARG   B CB  1 
ATOM   470  C CG  . ARG   B 2 19  ? -21.565 21.788  -14.066 1.00 65.45  ? 28  ARG   B CG  1 
ATOM   471  C CD  . ARG   B 2 19  ? -22.377 22.866  -14.762 1.00 68.11  ? 28  ARG   B CD  1 
ATOM   472  N NE  . ARG   B 2 19  ? -23.552 22.363  -15.474 1.00 69.87  ? 28  ARG   B NE  1 
ATOM   473  C CZ  . ARG   B 2 19  ? -24.674 21.915  -14.894 1.00 72.80  ? 28  ARG   B CZ  1 
ATOM   474  N NH1 . ARG   B 2 19  ? -24.786 21.881  -13.571 1.00 73.35  ? 28  ARG   B NH1 1 
ATOM   475  N NH2 . ARG   B 2 19  ? -25.683 21.486  -15.642 1.00 72.67  ? 28  ARG   B NH2 1 
ATOM   476  N N   . ARG   B 2 20  ? -17.734 21.324  -10.997 1.00 64.70  ? 29  ARG   B N   1 
ATOM   477  C CA  . ARG   B 2 20  ? -16.864 21.768  -9.871  1.00 69.52  ? 29  ARG   B CA  1 
ATOM   478  C C   . ARG   B 2 20  ? -15.468 22.131  -10.399 1.00 68.25  ? 29  ARG   B C   1 
ATOM   479  O O   . ARG   B 2 20  ? -14.637 22.620  -9.612  1.00 68.88  ? 29  ARG   B O   1 
ATOM   480  C CB  . ARG   B 2 20  ? -16.783 20.664  -8.809  1.00 73.91  ? 29  ARG   B CB  1 
ATOM   481  C CG  . ARG   B 2 20  ? -16.693 21.158  -7.372  1.00 80.18  ? 29  ARG   B CG  1 
ATOM   482  C CD  . ARG   B 2 20  ? -16.474 19.987  -6.428  1.00 86.83  ? 29  ARG   B CD  1 
ATOM   483  N NE  . ARG   B 2 20  ? -15.525 19.030  -7.011  1.00 92.50  ? 29  ARG   B NE  1 
ATOM   484  C CZ  . ARG   B 2 20  ? -14.194 19.073  -6.881  1.00 97.74  ? 29  ARG   B CZ  1 
ATOM   485  N NH1 . ARG   B 2 20  ? -13.613 20.019  -6.157  1.00 100.68 ? 29  ARG   B NH1 1 
ATOM   486  N NH2 . ARG   B 2 20  ? -13.442 18.159  -7.476  1.00 97.57  ? 29  ARG   B NH2 1 
ATOM   487  N N   . LEU   B 2 21  ? -15.200 21.842  -11.672 1.00 65.67  ? 30  LEU   B N   1 
ATOM   488  C CA  . LEU   B 2 21  ? -13.949 22.216  -12.383 1.00 62.92  ? 30  LEU   B CA  1 
ATOM   489  C C   . LEU   B 2 21  ? -14.313 23.213  -13.489 1.00 60.41  ? 30  LEU   B C   1 
ATOM   490  O O   . LEU   B 2 21  ? -15.430 23.761  -13.437 1.00 59.48  ? 30  LEU   B O   1 
ATOM   491  C CB  . LEU   B 2 21  ? -13.318 20.933  -12.923 1.00 62.78  ? 30  LEU   B CB  1 
ATOM   492  C CG  . LEU   B 2 21  ? -12.350 20.206  -11.998 1.00 63.18  ? 30  LEU   B CG  1 
ATOM   493  C CD1 . LEU   B 2 21  ? -12.809 20.237  -10.550 1.00 63.82  ? 30  LEU   B CD1 1 
ATOM   494  C CD2 . LEU   B 2 21  ? -12.161 18.772  -12.465 1.00 63.02  ? 30  LEU   B CD2 1 
ATOM   495  N N   . LEU   B 2 22  ? -13.400 23.457  -14.436 1.00 60.08  ? 31  LEU   B N   1 
ATOM   496  C CA  . LEU   B 2 22  ? -13.640 24.359  -15.596 1.00 58.46  ? 31  LEU   B CA  1 
ATOM   497  C C   . LEU   B 2 22  ? -14.754 23.776  -16.468 1.00 57.10  ? 31  LEU   B C   1 
ATOM   498  O O   . LEU   B 2 22  ? -14.764 22.542  -16.638 1.00 57.22  ? 31  LEU   B O   1 
ATOM   499  C CB  . LEU   B 2 22  ? -12.347 24.504  -16.389 1.00 57.91  ? 31  LEU   B CB  1 
ATOM   500  C CG  . LEU   B 2 22  ? -12.371 25.635  -17.405 1.00 58.27  ? 31  LEU   B CG  1 
ATOM   501  C CD1 . LEU   B 2 22  ? -12.197 26.994  -16.730 1.00 58.25  ? 31  LEU   B CD1 1 
ATOM   502  C CD2 . LEU   B 2 22  ? -11.314 25.381  -18.475 1.00 58.51  ? 31  LEU   B CD2 1 
ATOM   503  N N   . GLY   B 2 23  ? -15.662 24.617  -16.974 1.00 56.05  ? 32  GLY   B N   1 
ATOM   504  C CA  . GLY   B 2 23  ? -16.835 24.174  -17.753 1.00 54.66  ? 32  GLY   B CA  1 
ATOM   505  C C   . GLY   B 2 23  ? -17.525 22.973  -17.110 1.00 53.12  ? 32  GLY   B C   1 
ATOM   506  O O   . GLY   B 2 23  ? -17.535 22.877  -15.861 1.00 53.25  ? 32  GLY   B O   1 
ATOM   507  N N   . SER   B 2 24  ? -18.146 22.120  -17.932 1.00 51.16  ? 33  SER   B N   1 
ATOM   508  C CA  . SER   B 2 24  ? -18.772 20.829  -17.543 1.00 48.69  ? 33  SER   B CA  1 
ATOM   509  C C   . SER   B 2 24  ? -17.773 19.728  -17.859 1.00 47.16  ? 33  SER   B C   1 
ATOM   510  O O   . SER   B 2 24  ? -17.338 19.689  -19.016 1.00 46.67  ? 33  SER   B O   1 
ATOM   511  C CB  . SER   B 2 24  ? -20.048 20.610  -18.285 1.00 48.46  ? 33  SER   B CB  1 
ATOM   512  O OG  . SER   B 2 24  ? -20.994 21.606  -17.941 1.00 50.33  ? 33  SER   B OG  1 
ATOM   513  N N   . THR   B 2 25  ? -17.389 18.890  -16.897 1.00 44.56  ? 34  THR   B N   1 
ATOM   514  C CA  . THR   B 2 25  ? -16.312 17.888  -17.097 1.00 43.63  ? 34  THR   B CA  1 
ATOM   515  C C   . THR   B 2 25  ? -16.895 16.490  -16.923 1.00 42.31  ? 34  THR   B C   1 
ATOM   516  O O   . THR   B 2 25  ? -17.659 16.305  -15.954 1.00 41.15  ? 34  THR   B O   1 
ATOM   517  C CB  . THR   B 2 25  ? -15.132 18.120  -16.151 1.00 43.91  ? 34  THR   B CB  1 
ATOM   518  O OG1 . THR   B 2 25  ? -14.617 19.436  -16.359 1.00 45.12  ? 34  THR   B OG1 1 
ATOM   519  C CG2 . THR   B 2 25  ? -14.021 17.123  -16.365 1.00 43.65  ? 34  THR   B CG2 1 
ATOM   520  N N   . GLN   B 2 26  ? -16.556 15.550  -17.805 1.00 40.58  ? 35  GLN   B N   1 
ATOM   521  C CA  . GLN   B 2 26  ? -17.089 14.165  -17.702 1.00 39.40  ? 35  GLN   B CA  1 
ATOM   522  C C   . GLN   B 2 26  ? -16.099 13.371  -16.855 1.00 39.11  ? 35  GLN   B C   1 
ATOM   523  O O   . GLN   B 2 26  ? -14.948 13.195  -17.292 1.00 39.67  ? 35  GLN   B O   1 
ATOM   524  C CB  . GLN   B 2 26  ? -17.292 13.484  -19.058 1.00 38.62  ? 35  GLN   B CB  1 
ATOM   525  C CG  . GLN   B 2 26  ? -17.867 12.063  -18.976 1.00 37.39  ? 35  GLN   B CG  1 
ATOM   526  C CD  . GLN   B 2 26  ? -18.115 11.450  -20.343 1.00 37.02  ? 35  GLN   B CD  1 
ATOM   527  O OE1 . GLN   B 2 26  ? -18.797 12.044  -21.175 1.00 37.23  ? 35  GLN   B OE1 1 
ATOM   528  N NE2 . GLN   B 2 26  ? -17.680 10.221  -20.550 1.00 35.89  ? 35  GLN   B NE2 1 
ATOM   529  N N   . VAL   B 2 27  ? -16.523 12.946  -15.670 1.00 38.38  ? 36  VAL   B N   1 
ATOM   530  C CA  . VAL   B 2 27  ? -15.632 12.210  -14.716 1.00 37.16  ? 36  VAL   B CA  1 
ATOM   531  C C   . VAL   B 2 27  ? -15.781 10.700  -14.960 1.00 35.80  ? 36  VAL   B C   1 
ATOM   532  O O   . VAL   B 2 27  ? -14.879 9.948   -14.637 1.00 36.31  ? 36  VAL   B O   1 
ATOM   533  C CB  . VAL   B 2 27  ? -15.966 12.681  -13.297 1.00 37.50  ? 36  VAL   B CB  1 
ATOM   534  C CG1 . VAL   B 2 27  ? -15.523 14.125  -13.139 1.00 38.50  ? 36  VAL   B CG1 1 
ATOM   535  C CG2 . VAL   B 2 27  ? -17.437 12.542  -12.972 1.00 36.93  ? 36  VAL   B CG2 1 
ATOM   536  N N   . GLY   B 2 28  ? -16.860 10.259  -15.594 1.00 34.49  ? 37  GLY   B N   1 
ATOM   537  C CA  . GLY   B 2 28  ? -17.021 8.851   -15.988 1.00 33.04  ? 37  GLY   B CA  1 
ATOM   538  C C   . GLY   B 2 28  ? -18.382 8.587   -16.584 1.00 32.29  ? 37  GLY   B C   1 
ATOM   539  O O   . GLY   B 2 28  ? -19.025 9.527   -17.086 1.00 32.85  ? 37  GLY   B O   1 
ATOM   540  N N   . VAL   B 2 29  ? -18.785 7.321   -16.548 1.00 31.48  ? 38  VAL   B N   1 
ATOM   541  C CA  . VAL   B 2 29  ? -19.962 6.729   -17.234 1.00 31.26  ? 38  VAL   B CA  1 
ATOM   542  C C   . VAL   B 2 29  ? -20.637 5.736   -16.292 1.00 30.85  ? 38  VAL   B C   1 
ATOM   543  O O   . VAL   B 2 29  ? -19.948 5.255   -15.331 1.00 30.32  ? 38  VAL   B O   1 
ATOM   544  C CB  . VAL   B 2 29  ? -19.457 6.033   -18.522 1.00 31.65  ? 38  VAL   B CB  1 
ATOM   545  C CG1 . VAL   B 2 29  ? -20.552 5.403   -19.354 1.00 31.71  ? 38  VAL   B CG1 1 
ATOM   546  C CG2 . VAL   B 2 29  ? -18.617 6.979   -19.337 1.00 31.93  ? 38  VAL   B CG2 1 
ATOM   547  N N   . GLY   B 2 30  ? -21.891 5.381   -16.561 1.00 30.75  ? 39  GLY   B N   1 
ATOM   548  C CA  . GLY   B 2 30  ? -22.538 4.255   -15.873 1.00 30.29  ? 39  GLY   B CA  1 
ATOM   549  C C   . GLY   B 2 30  ? -23.779 3.763   -16.542 1.00 30.54  ? 39  GLY   B C   1 
ATOM   550  O O   . GLY   B 2 30  ? -24.104 4.255   -17.670 1.00 30.65  ? 39  GLY   B O   1 
ATOM   551  N N   . VAL   B 2 31  ? -24.372 2.733   -15.959 1.00 30.09  ? 40  VAL   B N   1 
ATOM   552  C CA  . VAL   B 2 31  ? -25.480 1.929   -16.532 1.00 30.56  ? 40  VAL   B CA  1 
ATOM   553  C C   . VAL   B 2 31  ? -26.718 2.031   -15.670 1.00 31.14  ? 40  VAL   B C   1 
ATOM   554  O O   . VAL   B 2 31  ? -26.608 1.736   -14.446 1.00 30.11  ? 40  VAL   B O   1 
ATOM   555  C CB  . VAL   B 2 31  ? -25.056 0.464   -16.683 1.00 30.63  ? 40  VAL   B CB  1 
ATOM   556  C CG1 . VAL   B 2 31  ? -26.212 -0.409  -17.156 1.00 30.95  ? 40  VAL   B CG1 1 
ATOM   557  C CG2 . VAL   B 2 31  ? -23.876 0.328   -17.632 1.00 30.74  ? 40  VAL   B CG2 1 
ATOM   558  N N   . MET   B 2 32  ? -27.823 2.496   -16.243 1.00 31.84  ? 41  MET   B N   1 
ATOM   559  C CA  . MET   B 2 32  ? -29.165 2.470   -15.623 1.00 32.44  ? 41  MET   B CA  1 
ATOM   560  C C   . MET   B 2 32  ? -29.880 1.179   -16.059 1.00 33.40  ? 41  MET   B C   1 
ATOM   561  O O   . MET   B 2 32  ? -30.045 0.898   -17.300 1.00 32.61  ? 41  MET   B O   1 
ATOM   562  C CB  . MET   B 2 32  ? -29.942 3.725   -16.032 1.00 32.97  ? 41  MET   B CB  1 
ATOM   563  C CG  . MET   B 2 32  ? -31.241 3.940   -15.296 1.00 33.26  ? 41  MET   B CG  1 
ATOM   564  S SD  . MET   B 2 32  ? -30.925 4.451   -13.548 1.00 33.66  ? 41  MET   B SD  1 
ATOM   565  C CE  . MET   B 2 32  ? -30.216 6.066   -13.840 1.00 33.96  ? 41  MET   B CE  1 
ATOM   566  N N   . GLN   B 2 33  ? -30.224 0.322   -15.117 1.00 34.34  ? 42  GLN   B N   1 
ATOM   567  C CA  . GLN   B 2 33  ? -30.955 -0.941  -15.374 1.00 36.12  ? 42  GLN   B CA  1 
ATOM   568  C C   . GLN   B 2 33  ? -31.896 -1.209  -14.215 1.00 37.80  ? 42  GLN   B C   1 
ATOM   569  O O   . GLN   B 2 33  ? -31.419 -1.131  -13.034 1.00 36.16  ? 42  GLN   B O   1 
ATOM   570  C CB  . GLN   B 2 33  ? -30.023 -2.147  -15.540 1.00 37.21  ? 42  GLN   B CB  1 
ATOM   571  C CG  . GLN   B 2 33  ? -30.808 -3.414  -15.903 1.00 38.73  ? 42  GLN   B CG  1 
ATOM   572  C CD  . GLN   B 2 33  ? -30.012 -4.555  -16.502 1.00 40.38  ? 42  GLN   B CD  1 
ATOM   573  O OE1 . GLN   B 2 33  ? -30.142 -5.705  -16.080 1.00 44.90  ? 42  GLN   B OE1 1 
ATOM   574  N NE2 . GLN   B 2 33  ? -29.095 -4.269  -17.396 1.00 39.03  ? 42  GLN   B NE2 1 
ATOM   575  N N   . GLU   B 2 34  ? -33.146 -1.546  -14.514 1.00 39.48  ? 43  GLU   B N   1 
ATOM   576  C CA  . GLU   B 2 34  ? -34.167 -1.827  -13.475 1.00 40.71  ? 43  GLU   B CA  1 
ATOM   577  C C   . GLU   B 2 34  ? -34.232 -0.701  -12.433 1.00 40.57  ? 43  GLU   B C   1 
ATOM   578  O O   . GLU   B 2 34  ? -34.435 -1.006  -11.247 1.00 39.55  ? 43  GLU   B O   1 
ATOM   579  C CB  . GLU   B 2 34  ? -33.807 -3.173  -12.842 1.00 42.73  ? 43  GLU   B CB  1 
ATOM   580  C CG  . GLU   B 2 34  ? -34.184 -4.343  -13.716 1.00 44.62  ? 43  GLU   B CG  1 
ATOM   581  C CD  . GLU   B 2 34  ? -33.460 -5.651  -13.468 1.00 46.40  ? 43  GLU   B CD  1 
ATOM   582  O OE1 . GLU   B 2 34  ? -33.872 -6.371  -12.575 1.00 48.43  ? 43  GLU   B OE1 1 
ATOM   583  O OE2 . GLU   B 2 34  ? -32.501 -5.956  -14.198 1.00 48.51  ? 43  GLU   B OE2 1 
ATOM   584  N N   . GLY   B 2 35  ? -34.086 0.570   -12.820 1.00 39.32  ? 44  GLY   B N   1 
ATOM   585  C CA  . GLY   B 2 35  ? -34.217 1.703   -11.887 1.00 38.27  ? 44  GLY   B CA  1 
ATOM   586  C C   . GLY   B 2 35  ? -32.992 1.898   -11.006 1.00 36.87  ? 44  GLY   B C   1 
ATOM   587  O O   . GLY   B 2 35  ? -33.017 2.817   -10.178 1.00 37.05  ? 44  GLY   B O   1 
ATOM   588  N N   . VAL   B 2 36  ? -31.938 1.109   -11.203 1.00 35.21  ? 45  VAL   B N   1 
ATOM   589  C CA  . VAL   B 2 36  ? -30.666 1.222   -10.453 1.00 33.80  ? 45  VAL   B CA  1 
ATOM   590  C C   . VAL   B 2 36  ? -29.572 1.765   -11.380 1.00 32.86  ? 45  VAL   B C   1 
ATOM   591  O O   . VAL   B 2 36  ? -29.430 1.258   -12.536 1.00 33.05  ? 45  VAL   B O   1 
ATOM   592  C CB  . VAL   B 2 36  ? -30.305 -0.105  -9.746  1.00 33.61  ? 45  VAL   B CB  1 
ATOM   593  C CG1 . VAL   B 2 36  ? -28.861 -0.084  -9.250  1.00 33.39  ? 45  VAL   B CG1 1 
ATOM   594  C CG2 . VAL   B 2 36  ? -31.239 -0.365  -8.550  1.00 33.88  ? 45  VAL   B CG2 1 
ATOM   595  N N   . PHE   B 2 37  ? -28.826 2.751   -10.880 1.00 31.94  ? 46  PHE   B N   1 
ATOM   596  C CA  . PHE   B 2 37  ? -27.662 3.352   -11.554 1.00 31.71  ? 46  PHE   B CA  1 
ATOM   597  C C   . PHE   B 2 37  ? -26.381 2.701   -11.032 1.00 31.18  ? 46  PHE   B C   1 
ATOM   598  O O   . PHE   B 2 37  ? -26.106 2.677   -9.827  1.00 30.82  ? 46  PHE   B O   1 
ATOM   599  C CB  . PHE   B 2 37  ? -27.641 4.871   -11.475 1.00 31.83  ? 46  PHE   B CB  1 
ATOM   600  C CG  . PHE   B 2 37  ? -26.618 5.451   -12.419 1.00 32.27  ? 46  PHE   B CG  1 
ATOM   601  C CD1 . PHE   B 2 37  ? -26.775 5.353   -13.791 1.00 32.70  ? 46  PHE   B CD1 1 
ATOM   602  C CD2 . PHE   B 2 37  ? -25.496 6.075   -11.933 1.00 32.41  ? 46  PHE   B CD2 1 
ATOM   603  C CE1 . PHE   B 2 37  ? -25.815 5.868   -14.649 1.00 33.32  ? 46  PHE   B CE1 1 
ATOM   604  C CE2 . PHE   B 2 37  ? -24.539 6.600   -12.770 1.00 32.91  ? 46  PHE   B CE2 1 
ATOM   605  C CZ  . PHE   B 2 37  ? -24.712 6.517   -14.138 1.00 33.24  ? 46  PHE   B CZ  1 
ATOM   606  N N   . HIS   B 2 38  ? -25.610 2.162   -11.967 1.00 30.38  ? 47  HIS   B N   1 
ATOM   607  C CA  . HIS   B 2 38  ? -24.374 1.366   -11.740 1.00 30.14  ? 47  HIS   B CA  1 
ATOM   608  C C   . HIS   B 2 38  ? -23.157 2.121   -12.269 1.00 30.38  ? 47  HIS   B C   1 
ATOM   609  O O   . HIS   B 2 38  ? -23.118 2.426   -13.477 1.00 30.14  ? 47  HIS   B O   1 
ATOM   610  C CB  . HIS   B 2 38  ? -24.443 -0.000  -12.389 1.00 29.95  ? 47  HIS   B CB  1 
ATOM   611  C CG  . HIS   B 2 38  ? -25.655 -0.806  -12.123 1.00 30.14  ? 47  HIS   B CG  1 
ATOM   612  N ND1 . HIS   B 2 38  ? -26.884 -0.397  -12.485 1.00 30.38  ? 47  HIS   B ND1 1 
ATOM   613  C CD2 . HIS   B 2 38  ? -25.820 -1.966  -11.419 1.00 30.31  ? 47  HIS   B CD2 1 
ATOM   614  C CE1 . HIS   B 2 38  ? -27.776 -1.294  -12.121 1.00 30.54  ? 47  HIS   B CE1 1 
ATOM   615  N NE2 . HIS   B 2 38  ? -27.149 -2.251  -11.420 1.00 30.44  ? 47  HIS   B NE2 1 
ATOM   616  N N   . THR   B 2 39  ? -22.153 2.377   -11.433 1.00 30.50  ? 48  THR   B N   1 
ATOM   617  C CA  . THR   B 2 39  ? -20.891 2.980   -11.911 1.00 30.59  ? 48  THR   B CA  1 
ATOM   618  C C   . THR   B 2 39  ? -19.721 2.402   -11.131 1.00 31.05  ? 48  THR   B C   1 
ATOM   619  O O   . THR   B 2 39  ? -19.953 1.519   -10.199 1.00 30.23  ? 48  THR   B O   1 
ATOM   620  C CB  . THR   B 2 39  ? -21.002 4.510   -11.976 1.00 30.89  ? 48  THR   B CB  1 
ATOM   621  O OG1 . THR   B 2 39  ? -19.899 5.057   -12.711 1.00 30.95  ? 48  THR   B OG1 1 
ATOM   622  C CG2 . THR   B 2 39  ? -21.012 5.186   -10.622 1.00 31.09  ? 48  THR   B CG2 1 
ATOM   623  N N   . MET   B 2 40  ? -18.521 2.912   -11.429 1.00 31.57  ? 49  MET   B N   1 
ATOM   624  C CA  . MET   B 2 40  ? -17.318 2.589   -10.629 1.00 31.79  ? 49  MET   B CA  1 
ATOM   625  C C   . MET   B 2 40  ? -17.163 3.563   -9.445  1.00 31.43  ? 49  MET   B C   1 
ATOM   626  O O   . MET   B 2 40  ? -17.458 4.781   -9.559  1.00 31.31  ? 49  MET   B O   1 
ATOM   627  C CB  . MET   B 2 40  ? -16.066 2.549   -11.494 1.00 32.77  ? 49  MET   B CB  1 
ATOM   628  C CG  . MET   B 2 40  ? -16.271 1.727   -12.804 1.00 33.61  ? 49  MET   B CG  1 
ATOM   629  S SD  . MET   B 2 40  ? -14.805 0.850   -13.261 1.00 35.16  ? 49  MET   B SD  1 
ATOM   630  C CE  . MET   B 2 40  ? -14.814 -0.657  -12.298 1.00 35.17  ? 49  MET   B CE  1 
ATOM   631  N N   A TRP   B 2 41  ? -16.699 3.033   -8.311  0.20 31.40  ? 50  TRP   B N   1 
ATOM   632  N N   B TRP   B 2 41  ? -16.715 3.043   -8.298  0.20 31.10  ? 50  TRP   B N   1 
ATOM   633  N N   C TRP   B 2 41  ? -16.701 3.032   -8.310  0.25 31.39  ? 50  TRP   B N   1 
ATOM   634  N N   D TRP   B 2 41  ? -16.717 3.043   -8.298  0.25 31.10  ? 50  TRP   B N   1 
ATOM   635  C CA  A TRP   B 2 41  ? -16.543 3.810   -7.057  0.20 31.54  ? 50  TRP   B CA  1 
ATOM   636  C CA  B TRP   B 2 41  ? -16.568 3.844   -7.056  0.20 31.07  ? 50  TRP   B CA  1 
ATOM   637  C CA  C TRP   B 2 41  ? -16.544 3.810   -7.057  0.25 31.53  ? 50  TRP   B CA  1 
ATOM   638  C CA  D TRP   B 2 41  ? -16.569 3.844   -7.057  0.25 31.07  ? 50  TRP   B CA  1 
ATOM   639  C C   A TRP   B 2 41  ? -15.623 5.015   -7.295  0.20 31.75  ? 50  TRP   B C   1 
ATOM   640  C C   B TRP   B 2 41  ? -15.625 5.030   -7.298  0.20 31.48  ? 50  TRP   B C   1 
ATOM   641  C C   C TRP   B 2 41  ? -15.624 5.015   -7.296  0.25 31.75  ? 50  TRP   B C   1 
ATOM   642  C C   D TRP   B 2 41  ? -15.625 5.030   -7.299  0.25 31.48  ? 50  TRP   B C   1 
ATOM   643  O O   A TRP   B 2 41  ? -15.968 6.113   -6.831  0.20 31.77  ? 50  TRP   B O   1 
ATOM   644  O O   B TRP   B 2 41  ? -15.949 6.133   -6.833  0.20 31.53  ? 50  TRP   B O   1 
ATOM   645  O O   C TRP   B 2 41  ? -15.971 6.114   -6.843  0.25 31.74  ? 50  TRP   B O   1 
ATOM   646  O O   D TRP   B 2 41  ? -15.950 6.134   -6.842  0.25 31.51  ? 50  TRP   B O   1 
ATOM   647  C CB  A TRP   B 2 41  ? -16.036 2.941   -5.899  0.20 31.58  ? 50  TRP   B CB  1 
ATOM   648  C CB  B TRP   B 2 41  ? -16.089 2.993   -5.874  0.20 30.78  ? 50  TRP   B CB  1 
ATOM   649  C CB  C TRP   B 2 41  ? -16.034 2.940   -5.900  0.25 31.58  ? 50  TRP   B CB  1 
ATOM   650  C CB  D TRP   B 2 41  ? -16.089 2.991   -5.875  0.25 30.77  ? 50  TRP   B CB  1 
ATOM   651  C CG  A TRP   B 2 41  ? -16.156 3.691   -4.613  0.20 31.85  ? 50  TRP   B CG  1 
ATOM   652  C CG  B TRP   B 2 41  ? -15.919 3.826   -4.644  0.20 30.76  ? 50  TRP   B CG  1 
ATOM   653  C CG  C TRP   B 2 41  ? -16.155 3.691   -4.614  0.25 31.85  ? 50  TRP   B CG  1 
ATOM   654  C CG  D TRP   B 2 41  ? -15.918 3.825   -4.645  0.25 30.75  ? 50  TRP   B CG  1 
ATOM   655  C CD1 A TRP   B 2 41  ? -17.209 3.661   -3.750  0.20 31.87  ? 50  TRP   B CD1 1 
ATOM   656  C CD1 B TRP   B 2 41  ? -14.869 4.642   -4.341  0.20 30.88  ? 50  TRP   B CD1 1 
ATOM   657  C CD1 C TRP   B 2 41  ? -17.209 3.660   -3.752  0.25 31.86  ? 50  TRP   B CD1 1 
ATOM   658  C CD1 D TRP   B 2 41  ? -14.867 4.640   -4.341  0.25 30.88  ? 50  TRP   B CD1 1 
ATOM   659  C CD2 A TRP   B 2 41  ? -15.232 4.662   -4.091  0.20 32.18  ? 50  TRP   B CD2 1 
ATOM   660  C CD2 B TRP   B 2 41  ? -16.855 3.961   -3.563  0.20 30.66  ? 50  TRP   B CD2 1 
ATOM   661  C CD2 C TRP   B 2 41  ? -15.231 4.662   -4.091  0.25 32.18  ? 50  TRP   B CD2 1 
ATOM   662  C CD2 D TRP   B 2 41  ? -16.854 3.960   -3.565  0.25 30.65  ? 50  TRP   B CD2 1 
ATOM   663  N NE1 A TRP   B 2 41  ? -16.991 4.527   -2.716  0.20 32.21  ? 50  TRP   B NE1 1 
ATOM   664  N NE1 B TRP   B 2 41  ? -15.083 5.271   -3.147  0.20 30.99  ? 50  TRP   B NE1 1 
ATOM   665  N NE1 C TRP   B 2 41  ? -16.992 4.529   -2.720  0.25 32.22  ? 50  TRP   B NE1 1 
ATOM   666  N NE1 D TRP   B 2 41  ? -15.083 5.271   -3.150  0.25 30.97  ? 50  TRP   B NE1 1 
ATOM   667  C CE2 A TRP   B 2 41  ? -15.788 5.154   -2.896  0.20 32.33  ? 50  TRP   B CE2 1 
ATOM   668  C CE2 B TRP   B 2 41  ? -16.294 4.875   -2.647  0.20 30.88  ? 50  TRP   B CE2 1 
ATOM   669  C CE2 C TRP   B 2 41  ? -15.789 5.155   -2.898  0.25 32.33  ? 50  TRP   B CE2 1 
ATOM   670  C CE2 D TRP   B 2 41  ? -16.294 4.876   -2.650  0.25 30.88  ? 50  TRP   B CE2 1 
ATOM   671  C CE3 A TRP   B 2 41  ? -13.989 5.152   -4.502  0.20 32.42  ? 50  TRP   B CE3 1 
ATOM   672  C CE3 B TRP   B 2 41  ? -18.113 3.414   -3.289  0.20 30.54  ? 50  TRP   B CE3 1 
ATOM   673  C CE3 C TRP   B 2 41  ? -13.987 5.151   -4.500  0.25 32.43  ? 50  TRP   B CE3 1 
ATOM   674  C CE3 D TRP   B 2 41  ? -18.113 3.415   -3.293  0.25 30.54  ? 50  TRP   B CE3 1 
ATOM   675  C CZ2 A TRP   B 2 41  ? -15.141 6.104   -2.110  0.20 32.79  ? 50  TRP   B CZ2 1 
ATOM   676  C CZ2 B TRP   B 2 41  ? -16.936 5.224   -1.457  0.20 31.01  ? 50  TRP   B CZ2 1 
ATOM   677  C CZ2 C TRP   B 2 41  ? -15.143 6.106   -2.112  0.25 32.80  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -16.936 5.223   -1.460  0.25 31.00  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.350 6.094   -3.727  0.20 32.74  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 B TRP   B 2 41  ? -18.742 3.755   -2.107  0.20 30.66  ? 50  TRP   B CZ3 1 
ATOM   681  C CZ3 C TRP   B 2 41  ? -13.350 6.094   -3.726  0.25 32.75  ? 50  TRP   B CZ3 1 
ATOM   682  C CZ3 D TRP   B 2 41  ? -18.741 3.754   -2.110  0.25 30.66  ? 50  TRP   B CZ3 1 
ATOM   683  C CH2 A TRP   B 2 41  ? -13.918 6.559   -2.545  0.20 32.91  ? 50  TRP   B CH2 1 
ATOM   684  C CH2 B TRP   B 2 41  ? -18.166 4.659   -1.216  0.20 30.87  ? 50  TRP   B CH2 1 
ATOM   685  C CH2 C TRP   B 2 41  ? -13.919 6.560   -2.545  0.25 32.92  ? 50  TRP   B CH2 1 
ATOM   686  C CH2 D TRP   B 2 41  ? -18.166 4.659   -1.219  0.25 30.86  ? 50  TRP   B CH2 1 
ATOM   687  N N   . HIS   B 2 42  ? -14.522 4.835   -8.034  1.00 31.78  ? 51  HIS   B N   1 
ATOM   688  C CA  . HIS   B 2 42  ? -13.526 5.929   -8.240  1.00 32.42  ? 51  HIS   B CA  1 
ATOM   689  C C   . HIS   B 2 42  ? -14.143 7.101   -9.046  1.00 33.78  ? 51  HIS   B C   1 
ATOM   690  O O   . HIS   B 2 42  ? -13.617 8.210   -8.941  1.00 34.84  ? 51  HIS   B O   1 
ATOM   691  C CB  . HIS   B 2 42  ? -12.200 5.418   -8.783  1.00 32.52  ? 51  HIS   B CB  1 
ATOM   692  C CG  . HIS   B 2 42  ? -12.228 5.168   -10.257 1.00 32.05  ? 51  HIS   B CG  1 
ATOM   693  N ND1 . HIS   B 2 42  ? -12.276 3.891   -10.774 1.00 31.87  ? 51  HIS   B ND1 1 
ATOM   694  C CD2 . HIS   B 2 42  ? -12.173 6.006   -11.320 1.00 32.85  ? 51  HIS   B CD2 1 
ATOM   695  C CE1 . HIS   B 2 42  ? -12.252 3.949   -12.123 1.00 32.04  ? 51  HIS   B CE1 1 
ATOM   696  N NE2 . HIS   B 2 42  ? -12.209 5.238   -12.474 1.00 31.89  ? 51  HIS   B NE2 1 
ATOM   697  N N   . VAL   B 2 43  ? -15.270 6.928   -9.731  1.00 34.35  ? 52  VAL   B N   1 
ATOM   698  C CA  . VAL   B 2 43  ? -15.927 8.015   -10.515 1.00 35.08  ? 52  VAL   B CA  1 
ATOM   699  C C   . VAL   B 2 43  ? -16.629 9.004   -9.576  1.00 35.98  ? 52  VAL   B C   1 
ATOM   700  O O   . VAL   B 2 43  ? -16.418 10.221  -9.739  1.00 36.35  ? 52  VAL   B O   1 
ATOM   701  C CB  . VAL   B 2 43  ? -16.878 7.391   -11.548 1.00 35.54  ? 52  VAL   B CB  1 
ATOM   702  C CG1 . VAL   B 2 43  ? -17.812 8.394   -12.220 1.00 36.12  ? 52  VAL   B CG1 1 
ATOM   703  C CG2 . VAL   B 2 43  ? -16.083 6.646   -12.596 1.00 35.71  ? 52  VAL   B CG2 1 
ATOM   704  N N   . THR   B 2 44  ? -17.438 8.512   -8.628  1.00 35.13  ? 53  THR   B N   1 
ATOM   705  C CA  . THR   B 2 44  ? -18.321 9.356   -7.768  1.00 36.30  ? 53  THR   B CA  1 
ATOM   706  C C   . THR   B 2 44  ? -17.727 9.497   -6.366  1.00 37.22  ? 53  THR   B C   1 
ATOM   707  O O   . THR   B 2 44  ? -18.064 10.500  -5.711  1.00 37.35  ? 53  THR   B O   1 
ATOM   708  C CB  . THR   B 2 44  ? -19.756 8.815   -7.714  1.00 35.48  ? 53  THR   B CB  1 
ATOM   709  O OG1 . THR   B 2 44  ? -19.765 7.558   -7.035  1.00 34.41  ? 53  THR   B OG1 1 
ATOM   710  C CG2 . THR   B 2 44  ? -20.330 8.676   -9.118  1.00 35.37  ? 53  THR   B CG2 1 
ATOM   711  N N   . LYS   B 2 45  ? -16.819 8.596   -5.991  1.00 38.75  ? 54  LYS   B N   1 
ATOM   712  C CA  . LYS   B 2 45  ? -16.322 8.418   -4.591  1.00 42.13  ? 54  LYS   B CA  1 
ATOM   713  C C   . LYS   B 2 45  ? -17.516 8.218   -3.651  1.00 42.14  ? 54  LYS   B C   1 
ATOM   714  O O   . LYS   B 2 45  ? -17.402 8.580   -2.473  1.00 44.40  ? 54  LYS   B O   1 
ATOM   715  C CB  . LYS   B 2 45  ? -15.488 9.615   -4.119  1.00 45.05  ? 54  LYS   B CB  1 
ATOM   716  C CG  . LYS   B 2 45  ? -14.460 10.138  -5.110  1.00 47.90  ? 54  LYS   B CG  1 
ATOM   717  C CD  . LYS   B 2 45  ? -13.208 9.310   -5.176  1.00 50.40  ? 54  LYS   B CD  1 
ATOM   718  C CE  . LYS   B 2 45  ? -12.129 9.993   -5.991  1.00 52.43  ? 54  LYS   B CE  1 
ATOM   719  N NZ  . LYS   B 2 45  ? -11.732 9.168   -7.163  1.00 54.26  ? 54  LYS   B NZ  1 
ATOM   720  N N   . GLY   B 2 46  ? -18.633 7.690   -4.143  1.00 42.10  ? 55  GLY   B N   1 
ATOM   721  C CA  . GLY   B 2 46  ? -19.844 7.434   -3.345  1.00 42.44  ? 55  GLY   B CA  1 
ATOM   722  C C   . GLY   B 2 46  ? -20.737 8.656   -3.149  1.00 43.46  ? 55  GLY   B C   1 
ATOM   723  O O   . GLY   B 2 46  ? -21.710 8.505   -2.456  1.00 42.96  ? 55  GLY   B O   1 
ATOM   724  N N   . ALA   B 2 47  ? -20.491 9.800   -3.800  1.00 44.01  ? 56  ALA   B N   1 
ATOM   725  C CA  . ALA   B 2 47  ? -21.311 11.034  -3.672  1.00 43.80  ? 56  ALA   B CA  1 
ATOM   726  C C   . ALA   B 2 47  ? -22.707 10.832  -4.283  1.00 42.81  ? 56  ALA   B C   1 
ATOM   727  O O   . ALA   B 2 47  ? -22.854 9.977   -5.132  1.00 42.44  ? 56  ALA   B O   1 
ATOM   728  C CB  . ALA   B 2 47  ? -20.605 12.207  -4.318  1.00 44.47  ? 56  ALA   B CB  1 
ATOM   729  N N   . ALA   B 2 48  ? -23.695 11.639  -3.882  1.00 41.66  ? 57  ALA   B N   1 
ATOM   730  C CA  . ALA   B 2 48  ? -25.023 11.718  -4.529  1.00 41.28  ? 57  ALA   B CA  1 
ATOM   731  C C   . ALA   B 2 48  ? -24.890 12.245  -5.960  1.00 40.79  ? 57  ALA   B C   1 
ATOM   732  O O   . ALA   B 2 48  ? -23.869 12.890  -6.248  1.00 40.72  ? 57  ALA   B O   1 
ATOM   733  C CB  . ALA   B 2 48  ? -25.929 12.613  -3.739  1.00 42.45  ? 57  ALA   B CB  1 
ATOM   734  N N   . LEU   B 2 49  ? -25.906 11.984  -6.784  1.00 40.29  ? 58  LEU   B N   1 
ATOM   735  C CA  . LEU   B 2 49  ? -26.005 12.426  -8.204  1.00 41.34  ? 58  LEU   B CA  1 
ATOM   736  C C   . LEU   B 2 49  ? -27.355 13.096  -8.465  1.00 43.09  ? 58  LEU   B C   1 
ATOM   737  O O   . LEU   B 2 49  ? -28.374 12.740  -7.818  1.00 43.32  ? 58  LEU   B O   1 
ATOM   738  C CB  . LEU   B 2 49  ? -25.858 11.230  -9.146  1.00 39.87  ? 58  LEU   B CB  1 
ATOM   739  C CG  . LEU   B 2 49  ? -24.593 10.392  -8.999  1.00 39.08  ? 58  LEU   B CG  1 
ATOM   740  C CD1 . LEU   B 2 49  ? -24.711 9.105   -9.755  1.00 38.15  ? 58  LEU   B CD1 1 
ATOM   741  C CD2 . LEU   B 2 49  ? -23.340 11.155  -9.382  1.00 39.44  ? 58  LEU   B CD2 1 
ATOM   742  N N   . ARG   B 2 50  ? -27.363 13.994  -9.441  1.00 44.88  ? 59  ARG   B N   1 
ATOM   743  C CA  . ARG   B 2 50  ? -28.582 14.659  -9.934  1.00 47.17  ? 59  ARG   B CA  1 
ATOM   744  C C   . ARG   B 2 50  ? -28.958 14.037  -11.280 1.00 48.01  ? 59  ARG   B C   1 
ATOM   745  O O   . ARG   B 2 50  ? -28.046 13.740  -12.073 1.00 45.87  ? 59  ARG   B O   1 
ATOM   746  C CB  . ARG   B 2 50  ? -28.276 16.152  -9.999  1.00 50.17  ? 59  ARG   B CB  1 
ATOM   747  C CG  . ARG   B 2 50  ? -29.436 17.001  -10.484 1.00 53.67  ? 59  ARG   B CG  1 
ATOM   748  C CD  . ARG   B 2 50  ? -29.255 18.447  -10.080 1.00 56.03  ? 59  ARG   B CD  1 
ATOM   749  N NE  . ARG   B 2 50  ? -27.843 18.787  -10.176 1.00 57.37  ? 59  ARG   B NE  1 
ATOM   750  C CZ  . ARG   B 2 50  ? -27.222 19.178  -11.271 1.00 58.73  ? 59  ARG   B CZ  1 
ATOM   751  N NH1 . ARG   B 2 50  ? -27.883 19.267  -12.414 1.00 60.35  ? 59  ARG   B NH1 1 
ATOM   752  N NH2 . ARG   B 2 50  ? -25.929 19.457  -11.218 1.00 60.68  ? 59  ARG   B NH2 1 
ATOM   753  N N   . SER   B 2 51  ? -30.244 13.786  -11.491 1.00 49.44  ? 60  SER   B N   1 
ATOM   754  C CA  . SER   B 2 51  ? -30.849 13.485  -12.810 1.00 51.69  ? 60  SER   B CA  1 
ATOM   755  C C   . SER   B 2 51  ? -32.049 14.420  -13.058 1.00 54.35  ? 60  SER   B C   1 
ATOM   756  O O   . SER   B 2 51  ? -33.161 14.093  -12.611 1.00 56.56  ? 60  SER   B O   1 
ATOM   757  C CB  . SER   B 2 51  ? -31.254 12.049  -12.876 1.00 50.78  ? 60  SER   B CB  1 
ATOM   758  O OG  . SER   B 2 51  ? -31.913 11.793  -14.098 1.00 51.40  ? 60  SER   B OG  1 
ATOM   759  N N   . GLY   B 2 52  ? -31.855 15.561  -13.718 1.00 56.84  ? 61  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 52  ? -32.892 16.616  -13.764 1.00 59.28  ? 61  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 52  ? -32.981 17.336  -12.427 1.00 62.10  ? 61  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 52  ? -31.930 17.780  -11.922 1.00 63.28  ? 61  GLY   B O   1 
ATOM   763  N N   . GLU   B 2 53  ? -34.170 17.436  -11.836 1.00 65.46  ? 62  GLU   B N   1 
ATOM   764  C CA  . GLU   B 2 53  ? -34.301 17.904  -10.427 1.00 68.35  ? 62  GLU   B CA  1 
ATOM   765  C C   . GLU   B 2 53  ? -34.480 16.710  -9.485  1.00 65.65  ? 62  GLU   B C   1 
ATOM   766  O O   . GLU   B 2 53  ? -34.599 16.967  -8.292  1.00 64.86  ? 62  GLU   B O   1 
ATOM   767  C CB  . GLU   B 2 53  ? -35.400 18.956  -10.299 1.00 72.52  ? 62  GLU   B CB  1 
ATOM   768  C CG  . GLU   B 2 53  ? -34.879 20.339  -10.651 1.00 78.01  ? 62  GLU   B CG  1 
ATOM   769  C CD  . GLU   B 2 53  ? -35.892 21.467  -10.601 1.00 84.19  ? 62  GLU   B CD  1 
ATOM   770  O OE1 . GLU   B 2 53  ? -37.088 21.201  -10.885 1.00 90.45  ? 62  GLU   B OE1 1 
ATOM   771  O OE2 . GLU   B 2 53  ? -35.484 22.610  -10.269 1.00 88.33  ? 62  GLU   B OE2 1 
ATOM   772  N N   . GLY   B 2 54  ? -34.407 15.472  -9.999  1.00 63.16  ? 63  GLY   B N   1 
ATOM   773  C CA  . GLY   B 2 54  ? -34.368 14.223  -9.211  1.00 60.34  ? 63  GLY   B CA  1 
ATOM   774  C C   . GLY   B 2 54  ? -32.990 13.966  -8.626  1.00 58.75  ? 63  GLY   B C   1 
ATOM   775  O O   . GLY   B 2 54  ? -32.007 14.432  -9.223  1.00 59.22  ? 63  GLY   B O   1 
ATOM   776  N N   . ARG   B 2 55  ? -32.927 13.275  -7.478  1.00 56.61  ? 64  ARG   B N   1 
ATOM   777  C CA  . ARG   B 2 55  ? -31.674 12.911  -6.755  1.00 54.02  ? 64  ARG   B CA  1 
ATOM   778  C C   . ARG   B 2 55  ? -31.481 11.384  -6.806  1.00 49.66  ? 64  ARG   B C   1 
ATOM   779  O O   . ARG   B 2 55  ? -32.468 10.636  -6.753  1.00 50.17  ? 64  ARG   B O   1 
ATOM   780  C CB  . ARG   B 2 55  ? -31.714 13.428  -5.314  1.00 55.69  ? 64  ARG   B CB  1 
ATOM   781  C CG  . ARG   B 2 55  ? -30.363 13.448  -4.614  1.00 57.58  ? 64  ARG   B CG  1 
ATOM   782  C CD  . ARG   B 2 55  ? -30.527 13.903  -3.168  1.00 60.86  ? 64  ARG   B CD  1 
ATOM   783  N NE  . ARG   B 2 55  ? -29.384 13.563  -2.332  1.00 62.36  ? 64  ARG   B NE  1 
ATOM   784  C CZ  . ARG   B 2 55  ? -28.689 14.407  -1.563  1.00 65.01  ? 64  ARG   B CZ  1 
ATOM   785  N NH1 . ARG   B 2 55  ? -29.012 15.688  -1.477  1.00 65.97  ? 64  ARG   B NH1 1 
ATOM   786  N NH2 . ARG   B 2 55  ? -27.680 13.949  -0.838  1.00 66.42  ? 64  ARG   B NH2 1 
ATOM   787  N N   . LEU   B 2 56  ? -30.240 10.933  -6.924  1.00 44.77  ? 65  LEU   B N   1 
ATOM   788  C CA  . LEU   B 2 56  ? -29.887 9.504   -6.853  1.00 42.34  ? 65  LEU   B CA  1 
ATOM   789  C C   . LEU   B 2 56  ? -28.969 9.344   -5.652  1.00 39.99  ? 65  LEU   B C   1 
ATOM   790  O O   . LEU   B 2 56  ? -27.873 9.954   -5.665  1.00 38.20  ? 65  LEU   B O   1 
ATOM   791  C CB  . LEU   B 2 56  ? -29.159 9.068   -8.135  1.00 41.98  ? 65  LEU   B CB  1 
ATOM   792  C CG  . LEU   B 2 56  ? -29.878 9.174   -9.478  1.00 43.04  ? 65  LEU   B CG  1 
ATOM   793  C CD1 . LEU   B 2 56  ? -29.267 8.162   -10.439 1.00 42.72  ? 65  LEU   B CD1 1 
ATOM   794  C CD2 . LEU   B 2 56  ? -31.371 8.919   -9.386  1.00 43.84  ? 65  LEU   B CD2 1 
ATOM   795  N N   . ASP   B 2 57  ? -29.420 8.621   -4.624  1.00 39.65  ? 66  ASP   B N   1 
ATOM   796  C CA  . ASP   B 2 57  ? -28.578 8.334   -3.439  1.00 38.17  ? 66  ASP   B CA  1 
ATOM   797  C C   . ASP   B 2 57  ? -27.896 6.977   -3.586  1.00 35.87  ? 66  ASP   B C   1 
ATOM   798  O O   . ASP   B 2 57  ? -28.491 5.998   -4.073  1.00 36.02  ? 66  ASP   B O   1 
ATOM   799  C CB  . ASP   B 2 57  ? -29.400 8.371   -2.152  1.00 40.25  ? 66  ASP   B CB  1 
ATOM   800  C CG  . ASP   B 2 57  ? -30.061 9.720   -1.928  1.00 42.18  ? 66  ASP   B CG  1 
ATOM   801  O OD1 . ASP   B 2 57  ? -29.364 10.729  -2.080  1.00 44.11  ? 66  ASP   B OD1 1 
ATOM   802  O OD2 . ASP   B 2 57  ? -31.269 9.742   -1.674  1.00 43.97  ? 66  ASP   B OD2 1 
ATOM   803  N N   . PRO   B 2 58  ? -26.625 6.877   -3.152  1.00 34.11  ? 67  PRO   B N   1 
ATOM   804  C CA  . PRO   B 2 58  ? -25.921 5.603   -3.112  1.00 33.32  ? 67  PRO   B CA  1 
ATOM   805  C C   . PRO   B 2 58  ? -26.730 4.597   -2.273  1.00 32.87  ? 67  PRO   B C   1 
ATOM   806  O O   . PRO   B 2 58  ? -27.404 5.012   -1.305  1.00 32.63  ? 67  PRO   B O   1 
ATOM   807  C CB  . PRO   B 2 58  ? -24.557 5.984   -2.514  1.00 33.66  ? 67  PRO   B CB  1 
ATOM   808  C CG  . PRO   B 2 58  ? -24.825 7.228   -1.694  1.00 34.48  ? 67  PRO   B CG  1 
ATOM   809  C CD  . PRO   B 2 58  ? -25.858 7.965   -2.518  1.00 34.92  ? 67  PRO   B CD  1 
ATOM   810  N N   . TYR   B 2 59  ? -26.669 3.322   -2.616  1.00 31.85  ? 68  TYR   B N   1 
ATOM   811  C CA  . TYR   B 2 59  ? -27.355 2.202   -1.934  1.00 31.31  ? 68  TYR   B CA  1 
ATOM   812  C C   . TYR   B 2 59  ? -26.335 1.165   -1.475  1.00 30.61  ? 68  TYR   B C   1 
ATOM   813  O O   . TYR   B 2 59  ? -26.465 0.609   -0.358  1.00 30.47  ? 68  TYR   B O   1 
ATOM   814  C CB  . TYR   B 2 59  ? -28.368 1.526   -2.858  1.00 31.55  ? 68  TYR   B CB  1 
ATOM   815  C CG  . TYR   B 2 59  ? -29.200 0.470   -2.173  1.00 31.78  ? 68  TYR   B CG  1 
ATOM   816  C CD1 . TYR   B 2 59  ? -28.743 -0.830  -2.114  1.00 31.78  ? 68  TYR   B CD1 1 
ATOM   817  C CD2 . TYR   B 2 59  ? -30.468 0.763   -1.657  1.00 31.79  ? 68  TYR   B CD2 1 
ATOM   818  C CE1 . TYR   B 2 59  ? -29.534 -1.828  -1.574  1.00 32.14  ? 68  TYR   B CE1 1 
ATOM   819  C CE2 . TYR   B 2 59  ? -31.287 -0.229  -1.134  1.00 32.02  ? 68  TYR   B CE2 1 
ATOM   820  C CZ  . TYR   B 2 59  ? -30.786 -1.517  -1.036  1.00 32.19  ? 68  TYR   B CZ  1 
ATOM   821  O OH  . TYR   B 2 59  ? -31.554 -2.530  -0.535  1.00 32.94  ? 68  TYR   B OH  1 
ATOM   822  N N   . TRP   B 2 60  ? -25.405 0.822   -2.340  1.00 29.56  ? 69  TRP   B N   1 
ATOM   823  C CA  . TRP   B 2 60  ? -24.347 -0.194  -2.110  1.00 29.11  ? 69  TRP   B CA  1 
ATOM   824  C C   . TRP   B 2 60  ? -23.052 0.277   -2.748  1.00 29.74  ? 69  TRP   B C   1 
ATOM   825  O O   . TRP   B 2 60  ? -23.095 0.746   -3.972  1.00 29.32  ? 69  TRP   B O   1 
ATOM   826  C CB  . TRP   B 2 60  ? -24.735 -1.575  -2.607  1.00 28.40  ? 69  TRP   B CB  1 
ATOM   827  C CG  . TRP   B 2 60  ? -23.586 -2.532  -2.564  1.00 28.07  ? 69  TRP   B CG  1 
ATOM   828  C CD1 . TRP   B 2 60  ? -23.133 -3.234  -1.470  1.00 27.99  ? 69  TRP   B CD1 1 
ATOM   829  C CD2 . TRP   B 2 60  ? -22.680 -2.844  -3.639  1.00 27.51  ? 69  TRP   B CD2 1 
ATOM   830  N NE1 . TRP   B 2 60  ? -22.014 -3.952  -1.798  1.00 27.88  ? 69  TRP   B NE1 1 
ATOM   831  C CE2 . TRP   B 2 60  ? -21.727 -3.748  -3.146  1.00 27.61  ? 69  TRP   B CE2 1 
ATOM   832  C CE3 . TRP   B 2 60  ? -22.609 -2.441  -4.994  1.00 27.33  ? 69  TRP   B CE3 1 
ATOM   833  C CZ2 . TRP   B 2 60  ? -20.693 -4.250  -3.923  1.00 27.44  ? 69  TRP   B CZ2 1 
ATOM   834  C CZ3 . TRP   B 2 60  ? -21.580 -2.939  -5.761  1.00 27.18  ? 69  TRP   B CZ3 1 
ATOM   835  C CH2 . TRP   B 2 60  ? -20.644 -3.833  -5.254  1.00 27.38  ? 69  TRP   B CH2 1 
ATOM   836  N N   . GLY   B 2 61  ? -21.937 0.098   -2.047  1.00 30.54  ? 70  GLY   B N   1 
ATOM   837  C CA  . GLY   B 2 61  ? -20.607 0.289   -2.661  1.00 31.01  ? 70  GLY   B CA  1 
ATOM   838  C C   . GLY   B 2 61  ? -19.514 -0.484  -1.978  1.00 31.74  ? 70  GLY   B C   1 
ATOM   839  O O   . GLY   B 2 61  ? -19.667 -0.804  -0.718  1.00 31.38  ? 70  GLY   B O   1 
ATOM   840  N N   . ASP   B 2 62  ? -18.411 -0.665  -2.682  1.00 32.19  ? 71  ASP   B N   1 
ATOM   841  C CA  . ASP   B 2 62  ? -17.206 -1.397  -2.205  1.00 33.33  ? 71  ASP   B CA  1 
ATOM   842  C C   . ASP   B 2 62  ? -15.982 -0.884  -2.951  1.00 33.31  ? 71  ASP   B C   1 
ATOM   843  O O   . ASP   B 2 62  ? -15.851 -1.189  -4.179  1.00 33.09  ? 71  ASP   B O   1 
ATOM   844  C CB  . ASP   B 2 62  ? -17.419 -2.894  -2.317  1.00 35.02  ? 71  ASP   B CB  1 
ATOM   845  C CG  . ASP   B 2 62  ? -16.309 -3.743  -1.748  1.00 37.70  ? 71  ASP   B CG  1 
ATOM   846  O OD1 . ASP   B 2 62  ? -15.149 -3.460  -1.987  1.00 40.13  ? 71  ASP   B OD1 1 
ATOM   847  O OD2 . ASP   B 2 62  ? -16.630 -4.623  -0.960  1.00 43.41  ? 71  ASP   B OD2 1 
ATOM   848  N N   . VAL   B 2 63  ? -15.118 -0.166  -2.237  1.00 33.01  ? 72  VAL   B N   1 
ATOM   849  C CA  . VAL   B 2 63  ? -13.840 0.444   -2.707  1.00 33.15  ? 72  VAL   B CA  1 
ATOM   850  C C   . VAL   B 2 63  ? -12.933 -0.661  -3.264  1.00 33.52  ? 72  VAL   B C   1 
ATOM   851  O O   . VAL   B 2 63  ? -12.278 -0.436  -4.371  1.00 32.67  ? 72  VAL   B O   1 
ATOM   852  C CB  . VAL   B 2 63  ? -13.152 1.280   -1.600  1.00 33.77  ? 72  VAL   B CB  1 
ATOM   853  C CG1 . VAL   B 2 63  ? -11.650 1.362   -1.745  1.00 34.24  ? 72  VAL   B CG1 1 
ATOM   854  C CG2 . VAL   B 2 63  ? -13.722 2.688   -1.497  1.00 33.83  ? 72  VAL   B CG2 1 
ATOM   855  N N   . LYS   B 2 64  ? -12.968 -1.865  -2.694  1.00 33.27  ? 73  LYS   B N   1 
ATOM   856  C CA  . LYS   B 2 64  ? -12.063 -2.932  -3.190  1.00 33.86  ? 73  LYS   B CA  1 
ATOM   857  C C   . LYS   B 2 64  ? -12.510 -3.446  -4.578  1.00 32.92  ? 73  LYS   B C   1 
ATOM   858  O O   . LYS   B 2 64  ? -11.629 -3.706  -5.402  1.00 33.93  ? 73  LYS   B O   1 
ATOM   859  C CB  . LYS   B 2 64  ? -11.974 -4.132  -2.265  1.00 34.17  ? 73  LYS   B CB  1 
ATOM   860  C CG  . LYS   B 2 64  ? -10.750 -4.948  -2.623  1.00 35.43  ? 73  LYS   B CG  1 
ATOM   861  C CD  . LYS   B 2 64  ? -10.518 -6.121  -1.790  1.00 36.18  ? 73  LYS   B CD  1 
ATOM   862  C CE  . LYS   B 2 64  ? -9.424  -6.972  -2.385  1.00 36.98  ? 73  LYS   B CE  1 
ATOM   863  N NZ  . LYS   B 2 64  ? -9.062  -7.991  -1.383  1.00 37.81  ? 73  LYS   B NZ  1 
ATOM   864  N N   . GLN   B 2 65  ? -13.815 -3.667  -4.775  1.00 32.79  ? 74  GLN   B N   1 
ATOM   865  C CA  . GLN   B 2 65  ? -14.407 -4.091  -6.087  1.00 32.64  ? 74  GLN   B CA  1 
ATOM   866  C C   . GLN   B 2 65  ? -14.396 -2.894  -7.051  1.00 31.66  ? 74  GLN   B C   1 
ATOM   867  O O   . GLN   B 2 65  ? -14.596 -3.151  -8.332  1.00 30.84  ? 74  GLN   B O   1 
ATOM   868  C CB  . GLN   B 2 65  ? -15.852 -4.597  -5.976  1.00 33.66  ? 74  GLN   B CB  1 
ATOM   869  C CG  . GLN   B 2 65  ? -16.050 -5.835  -5.088  1.00 35.44  ? 74  GLN   B CG  1 
ATOM   870  C CD  . GLN   B 2 65  ? -17.492 -6.304  -4.988  1.00 36.65  ? 74  GLN   B CD  1 
ATOM   871  O OE1 . GLN   B 2 65  ? -18.245 -6.443  -5.977  1.00 38.82  ? 74  GLN   B OE1 1 
ATOM   872  N NE2 . GLN   B 2 65  ? -17.930 -6.527  -3.769  1.00 37.83  ? 74  GLN   B NE2 1 
ATOM   873  N N   . ASP   B 2 66  ? -14.176 -1.671  -6.536  1.00 30.78  ? 75  ASP   B N   1 
ATOM   874  C CA  . ASP   B 2 66  ? -14.336 -0.336  -7.185  1.00 30.65  ? 75  ASP   B CA  1 
ATOM   875  C C   . ASP   B 2 66  ? -15.689 -0.235  -7.898  1.00 30.45  ? 75  ASP   B C   1 
ATOM   876  O O   . ASP   B 2 66  ? -15.687 0.172   -9.094  1.00 29.84  ? 75  ASP   B O   1 
ATOM   877  C CB  . ASP   B 2 66  ? -13.175 -0.082  -8.166  1.00 30.99  ? 75  ASP   B CB  1 
ATOM   878  C CG  . ASP   B 2 66  ? -13.126 1.311   -8.764  1.00 31.20  ? 75  ASP   B CG  1 
ATOM   879  O OD1 . ASP   B 2 66  ? -13.379 2.264   -8.039  1.00 30.93  ? 75  ASP   B OD1 1 
ATOM   880  O OD2 . ASP   B 2 66  ? -12.752 1.414   -10.035 1.00 31.20  ? 75  ASP   B OD2 1 
ATOM   881  N N   . LEU   B 2 67  ? -16.804 -0.595  -7.240  1.00 29.88  ? 76  LEU   B N   1 
ATOM   882  C CA  . LEU   B 2 67  ? -18.198 -0.491  -7.730  1.00 29.73  ? 76  LEU   B CA  1 
ATOM   883  C C   . LEU   B 2 67  ? -19.110 0.247   -6.764  1.00 30.16  ? 76  LEU   B C   1 
ATOM   884  O O   . LEU   B 2 67  ? -18.882 0.167   -5.479  1.00 29.87  ? 76  LEU   B O   1 
ATOM   885  C CB  . LEU   B 2 67  ? -18.732 -1.898  -7.959  1.00 29.78  ? 76  LEU   B CB  1 
ATOM   886  C CG  . LEU   B 2 67  ? -18.117 -2.702  -9.104  1.00 29.80  ? 76  LEU   B CG  1 
ATOM   887  C CD1 . LEU   B 2 67  ? -18.814 -4.049  -9.190  1.00 30.00  ? 76  LEU   B CD1 1 
ATOM   888  C CD2 . LEU   B 2 67  ? -18.263 -1.952  -10.464 1.00 29.77  ? 76  LEU   B CD2 1 
ATOM   889  N N   . VAL   B 2 68  ? -20.173 0.847   -7.311  1.00 30.11  ? 77  VAL   B N   1 
ATOM   890  C CA  . VAL   B 2 68  ? -21.224 1.519   -6.487  1.00 29.75  ? 77  VAL   B CA  1 
ATOM   891  C C   . VAL   B 2 68  ? -22.553 1.439   -7.238  1.00 29.78  ? 77  VAL   B C   1 
ATOM   892  O O   . VAL   B 2 68  ? -22.548 1.548   -8.537  1.00 29.17  ? 77  VAL   B O   1 
ATOM   893  C CB  . VAL   B 2 68  ? -20.807 2.961   -6.161  1.00 29.94  ? 77  VAL   B CB  1 
ATOM   894  C CG1 . VAL   B 2 68  ? -20.538 3.785   -7.432  1.00 29.96  ? 77  VAL   B CG1 1 
ATOM   895  C CG2 . VAL   B 2 68  ? -21.841 3.684   -5.309  1.00 30.00  ? 77  VAL   B CG2 1 
ATOM   896  N N   . SER   B 2 69  ? -23.664 1.233   -6.544  1.00 29.25  ? 78  SER   B N   1 
ATOM   897  C CA  . SER   B 2 69  ? -25.049 1.283   -7.085  1.00 29.51  ? 78  SER   B CA  1 
ATOM   898  C C   . SER   B 2 69  ? -25.865 2.392   -6.415  1.00 29.97  ? 78  SER   B C   1 
ATOM   899  O O   . SER   B 2 69  ? -25.647 2.692   -5.129  1.00 30.03  ? 78  SER   B O   1 
ATOM   900  C CB  . SER   B 2 69  ? -25.709 -0.091  -6.964  1.00 29.53  ? 78  SER   B CB  1 
ATOM   901  O OG  . SER   B 2 69  ? -26.076 -0.418  -5.588  1.00 29.77  ? 78  SER   B OG  1 
ATOM   902  N N   A TYR   B 2 70  ? -26.800 2.985   -7.162  0.19 30.09  ? 79  TYR   B N   1 
ATOM   903  N N   B TYR   B 2 70  ? -26.800 2.985   -7.162  0.20 30.09  ? 79  TYR   B N   1 
ATOM   904  N N   C TYR   B 2 70  ? -26.803 2.978   -7.163  0.31 30.10  ? 79  TYR   B N   1 
ATOM   905  N N   D TYR   B 2 70  ? -26.803 2.978   -7.163  0.30 30.10  ? 79  TYR   B N   1 
ATOM   906  C CA  A TYR   B 2 70  ? -27.696 4.086   -6.715  0.19 30.36  ? 79  TYR   B CA  1 
ATOM   907  C CA  B TYR   B 2 70  ? -27.696 4.086   -6.715  0.20 30.36  ? 79  TYR   B CA  1 
ATOM   908  C CA  C TYR   B 2 70  ? -27.695 4.086   -6.725  0.31 30.40  ? 79  TYR   B CA  1 
ATOM   909  C CA  D TYR   B 2 70  ? -27.695 4.086   -6.725  0.30 30.40  ? 79  TYR   B CA  1 
ATOM   910  C C   A TYR   B 2 70  ? -29.157 3.641   -6.854  0.19 30.61  ? 79  TYR   B C   1 
ATOM   911  C C   B TYR   B 2 70  ? -29.157 3.641   -6.854  0.20 30.62  ? 79  TYR   B C   1 
ATOM   912  C C   C TYR   B 2 70  ? -29.161 3.659   -6.856  0.31 30.73  ? 79  TYR   B C   1 
ATOM   913  C C   D TYR   B 2 70  ? -29.161 3.658   -6.856  0.30 30.73  ? 79  TYR   B C   1 
ATOM   914  O O   A TYR   B 2 70  ? -29.483 3.010   -7.862  0.19 30.58  ? 79  TYR   B O   1 
ATOM   915  O O   B TYR   B 2 70  ? -29.483 3.010   -7.861  0.20 30.58  ? 79  TYR   B O   1 
ATOM   916  O O   C TYR   B 2 70  ? -29.508 3.025   -7.851  0.31 30.63  ? 79  TYR   B O   1 
ATOM   917  O O   D TYR   B 2 70  ? -29.508 3.025   -7.851  0.30 30.63  ? 79  TYR   B O   1 
ATOM   918  C CB  A TYR   B 2 70  ? -27.413 5.372   -7.499  0.19 30.53  ? 79  TYR   B CB  1 
ATOM   919  C CB  B TYR   B 2 70  ? -27.413 5.372   -7.499  0.20 30.53  ? 79  TYR   B CB  1 
ATOM   920  C CB  C TYR   B 2 70  ? -27.411 5.376   -7.503  0.31 30.54  ? 79  TYR   B CB  1 
ATOM   921  C CB  D TYR   B 2 70  ? -27.411 5.376   -7.504  0.30 30.54  ? 79  TYR   B CB  1 
ATOM   922  C CG  A TYR   B 2 70  ? -26.071 5.998   -7.210  0.19 30.57  ? 79  TYR   B CG  1 
ATOM   923  C CG  B TYR   B 2 70  ? -26.071 5.998   -7.210  0.20 30.57  ? 79  TYR   B CG  1 
ATOM   924  C CG  C TYR   B 2 70  ? -26.070 6.001   -7.215  0.31 30.57  ? 79  TYR   B CG  1 
ATOM   925  C CG  D TYR   B 2 70  ? -26.070 6.000   -7.215  0.30 30.57  ? 79  TYR   B CG  1 
ATOM   926  C CD1 A TYR   B 2 70  ? -24.903 5.493   -7.763  0.19 30.49  ? 79  TYR   B CD1 1 
ATOM   927  C CD1 B TYR   B 2 70  ? -24.903 5.493   -7.763  0.20 30.49  ? 79  TYR   B CD1 1 
ATOM   928  C CD1 C TYR   B 2 70  ? -24.902 5.496   -7.768  0.31 30.49  ? 79  TYR   B CD1 1 
ATOM   929  C CD1 D TYR   B 2 70  ? -24.902 5.496   -7.768  0.30 30.49  ? 79  TYR   B CD1 1 
ATOM   930  C CD2 A TYR   B 2 70  ? -25.964 7.092   -6.371  0.19 30.90  ? 79  TYR   B CD2 1 
ATOM   931  C CD2 B TYR   B 2 70  ? -25.964 7.092   -6.371  0.20 30.90  ? 79  TYR   B CD2 1 
ATOM   932  C CD2 C TYR   B 2 70  ? -25.962 7.090   -6.371  0.31 30.92  ? 79  TYR   B CD2 1 
ATOM   933  C CD2 D TYR   B 2 70  ? -25.962 7.090   -6.371  0.30 30.92  ? 79  TYR   B CD2 1 
ATOM   934  C CE1 A TYR   B 2 70  ? -23.667 6.061   -7.490  0.19 30.60  ? 79  TYR   B CE1 1 
ATOM   935  C CE1 B TYR   B 2 70  ? -23.667 6.061   -7.490  0.20 30.60  ? 79  TYR   B CE1 1 
ATOM   936  C CE1 C TYR   B 2 70  ? -23.665 6.064   -7.494  0.31 30.61  ? 79  TYR   B CE1 1 
ATOM   937  C CE1 D TYR   B 2 70  ? -23.665 6.064   -7.493  0.30 30.61  ? 79  TYR   B CE1 1 
ATOM   938  C CE2 A TYR   B 2 70  ? -24.738 7.667   -6.079  0.19 31.02  ? 79  TYR   B CE2 1 
ATOM   939  C CE2 B TYR   B 2 70  ? -24.738 7.667   -6.079  0.20 31.02  ? 79  TYR   B CE2 1 
ATOM   940  C CE2 C TYR   B 2 70  ? -24.735 7.662   -6.074  0.31 31.04  ? 79  TYR   B CE2 1 
ATOM   941  C CE2 D TYR   B 2 70  ? -24.736 7.662   -6.074  0.30 31.03  ? 79  TYR   B CE2 1 
ATOM   942  C CZ  A TYR   B 2 70  ? -23.585 7.151   -6.641  0.19 30.85  ? 79  TYR   B CZ  1 
ATOM   943  C CZ  B TYR   B 2 70  ? -23.585 7.151   -6.641  0.20 30.85  ? 79  TYR   B CZ  1 
ATOM   944  C CZ  C TYR   B 2 70  ? -23.583 7.148   -6.638  0.31 30.85  ? 79  TYR   B CZ  1 
ATOM   945  C CZ  D TYR   B 2 70  ? -23.583 7.148   -6.638  0.30 30.85  ? 79  TYR   B CZ  1 
ATOM   946  O OH  A TYR   B 2 70  ? -22.383 7.729   -6.344  0.19 31.18  ? 79  TYR   B OH  1 
ATOM   947  O OH  B TYR   B 2 70  ? -22.383 7.729   -6.344  0.20 31.18  ? 79  TYR   B OH  1 
ATOM   948  O OH  C TYR   B 2 70  ? -22.384 7.728   -6.330  0.31 31.21  ? 79  TYR   B OH  1 
ATOM   949  O OH  D TYR   B 2 70  ? -22.385 7.728   -6.330  0.30 31.21  ? 79  TYR   B OH  1 
ATOM   950  N N   A CYS   B 2 71  ? -29.999 3.900   -5.835  0.19 30.84  ? 80  CYS   B N   1 
ATOM   951  N N   B CYS   B 2 71  ? -29.999 3.900   -5.835  0.20 30.84  ? 80  CYS   B N   1 
ATOM   952  N N   C CYS   B 2 71  ? -29.973 3.992   -5.834  0.31 31.32  ? 80  CYS   B N   1 
ATOM   953  N N   D CYS   B 2 71  ? -29.973 3.993   -5.835  0.30 31.31  ? 80  CYS   B N   1 
ATOM   954  C CA  A CYS   B 2 71  ? -31.483 3.716   -5.853  0.19 31.07  ? 80  CYS   B CA  1 
ATOM   955  C CA  B CYS   B 2 71  ? -31.483 3.716   -5.852  0.20 31.07  ? 80  CYS   B CA  1 
ATOM   956  C CA  C CYS   B 2 71  ? -31.459 3.872   -5.798  0.31 31.79  ? 80  CYS   B CA  1 
ATOM   957  C CA  D CYS   B 2 71  ? -31.460 3.872   -5.799  0.30 31.79  ? 80  CYS   B CA  1 
ATOM   958  C C   A CYS   B 2 71  ? -31.868 2.244   -5.632  0.19 30.98  ? 80  CYS   B C   1 
ATOM   959  C C   B CYS   B 2 71  ? -31.867 2.243   -5.629  0.20 30.98  ? 80  CYS   B C   1 
ATOM   960  C C   C CYS   B 2 71  ? -31.875 2.454   -5.353  0.31 31.61  ? 80  CYS   B C   1 
ATOM   961  C C   D CYS   B 2 71  ? -31.876 2.454   -5.355  0.30 31.61  ? 80  CYS   B C   1 
ATOM   962  O O   A CYS   B 2 71  ? -33.052 1.887   -5.895  0.19 31.26  ? 80  CYS   B O   1 
ATOM   963  O O   B CYS   B 2 71  ? -33.051 1.886   -5.892  0.20 31.26  ? 80  CYS   B O   1 
ATOM   964  O O   C CYS   B 2 71  ? -33.041 2.277   -4.959  0.31 31.99  ? 80  CYS   B O   1 
ATOM   965  O O   D CYS   B 2 71  ? -33.041 2.277   -4.960  0.30 31.99  ? 80  CYS   B O   1 
ATOM   966  C CB  A CYS   B 2 71  ? -32.089 4.202   -7.170  0.19 31.31  ? 80  CYS   B CB  1 
ATOM   967  C CB  B CYS   B 2 71  ? -32.089 4.201   -7.169  0.20 31.31  ? 80  CYS   B CB  1 
ATOM   968  C CB  C CYS   B 2 71  ? -32.082 4.322   -7.125  0.31 32.36  ? 80  CYS   B CB  1 
ATOM   969  C CB  D CYS   B 2 71  ? -32.082 4.323   -7.125  0.30 32.35  ? 80  CYS   B CB  1 
ATOM   970  S SG  A CYS   B 2 71  ? -31.162 5.582   -7.884  0.19 31.53  ? 80  CYS   B SG  1 
ATOM   971  S SG  B CYS   B 2 71  ? -31.162 5.581   -7.883  0.20 31.54  ? 80  CYS   B SG  1 
ATOM   972  S SG  C CYS   B 2 71  ? -31.899 6.112   -7.351  0.31 33.41  ? 80  CYS   B SG  1 
ATOM   973  S SG  D CYS   B 2 71  ? -31.901 6.112   -7.352  0.30 33.40  ? 80  CYS   B SG  1 
ATOM   974  N N   A GLY   B 2 72  ? -30.915 1.403   -5.177  0.19 30.71  ? 81  GLY   B N   1 
ATOM   975  N N   B GLY   B 2 72  ? -30.914 1.403   -5.174  0.20 30.71  ? 81  GLY   B N   1 
ATOM   976  N N   C GLY   B 2 72  ? -30.940 1.499   -5.306  0.31 31.20  ? 81  GLY   B N   1 
ATOM   977  N N   D GLY   B 2 72  ? -30.942 1.498   -5.312  0.30 31.20  ? 81  GLY   B N   1 
ATOM   978  C CA  A GLY   B 2 72  ? -31.152 -0.040  -4.971  0.19 30.73  ? 81  GLY   B CA  1 
ATOM   979  C CA  B GLY   B 2 72  ? -31.152 -0.040  -4.969  0.20 30.73  ? 81  GLY   B CA  1 
ATOM   980  C CA  C GLY   B 2 72  ? -31.211 0.078   -5.007  0.31 31.13  ? 81  GLY   B CA  1 
ATOM   981  C CA  D GLY   B 2 72  ? -31.212 0.078   -5.005  0.30 31.13  ? 81  GLY   B CA  1 
ATOM   982  C C   A GLY   B 2 72  ? -29.744 -0.770  -4.970  0.19 30.51  ? 81  GLY   B C   1 
ATOM   983  C C   B GLY   B 2 72  ? -29.746 -0.770  -4.967  0.20 30.51  ? 81  GLY   B C   1 
ATOM   984  C C   C GLY   B 2 72  ? -29.785 -0.672  -5.169  0.31 30.83  ? 81  GLY   B C   1 
ATOM   985  C C   D GLY   B 2 72  ? -29.784 -0.672  -5.169  0.30 30.83  ? 81  GLY   B C   1 
ATOM   986  O O   A GLY   B 2 72  ? -28.433 -0.068  -5.305  0.19 30.62  ? 81  GLY   B O   1 
ATOM   987  O O   B GLY   B 2 72  ? -28.434 -0.067  -5.305  0.20 30.62  ? 81  GLY   B O   1 
ATOM   988  O O   C GLY   B 2 72  ? -28.570 -0.061  -5.413  0.31 31.21  ? 81  GLY   B O   1 
ATOM   989  O O   D GLY   B 2 72  ? -28.568 -0.060  -5.413  0.30 31.20  ? 81  GLY   B O   1 
ATOM   990  N N   A PRO   B 2 73  ? -30.007 -2.230  -4.729  0.19 30.52  ? 82  PRO   B N   1 
ATOM   991  N N   B PRO   B 2 73  ? -30.007 -2.229  -4.727  0.20 30.52  ? 82  PRO   B N   1 
ATOM   992  N N   C PRO   B 2 73  ? -30.077 -2.124  -4.798  0.31 30.62  ? 82  PRO   B N   1 
ATOM   993  N N   D PRO   B 2 73  ? -30.078 -2.126  -4.797  0.30 30.62  ? 82  PRO   B N   1 
ATOM   994  C CA  A PRO   B 2 73  ? -28.904 -3.213  -4.945  0.19 30.58  ? 82  PRO   B CA  1 
ATOM   995  C CA  B PRO   B 2 73  ? -28.903 -3.211  -4.944  0.20 30.58  ? 82  PRO   B CA  1 
ATOM   996  C CA  C PRO   B 2 73  ? -28.994 -3.164  -4.958  0.31 30.66  ? 82  PRO   B CA  1 
ATOM   997  C CA  D PRO   B 2 73  ? -28.995 -3.165  -4.960  0.30 30.66  ? 82  PRO   B CA  1 
ATOM   998  C C   A PRO   B 2 73  ? -28.410 -3.248  -6.409  0.19 30.61  ? 82  PRO   B C   1 
ATOM   999  C C   B PRO   B 2 73  ? -28.409 -3.246  -6.408  0.20 30.61  ? 82  PRO   B C   1 
ATOM   1000 C C   C PRO   B 2 73  ? -28.475 -3.300  -6.417  0.31 30.66  ? 82  PRO   B C   1 
ATOM   1001 C C   D PRO   B 2 73  ? -28.474 -3.299  -6.419  0.30 30.66  ? 82  PRO   B C   1 
ATOM   1002 O O   A PRO   B 2 73  ? -29.155 -2.773  -7.255  0.19 30.81  ? 82  PRO   B O   1 
ATOM   1003 O O   B PRO   B 2 73  ? -29.155 -2.770  -7.253  0.20 30.81  ? 82  PRO   B O   1 
ATOM   1004 O O   C PRO   B 2 73  ? -29.282 -3.034  -7.274  0.31 31.07  ? 82  PRO   B O   1 
ATOM   1005 O O   D PRO   B 2 73  ? -29.279 -3.030  -7.278  0.30 31.06  ? 82  PRO   B O   1 
ATOM   1006 C CB  A PRO   B 2 73  ? -29.535 -4.550  -4.514  0.19 30.78  ? 82  PRO   B CB  1 
ATOM   1007 C CB  B PRO   B 2 73  ? -29.534 -4.549  -4.513  0.20 30.78  ? 82  PRO   B CB  1 
ATOM   1008 C CB  C PRO   B 2 73  ? -29.693 -4.463  -4.516  0.31 30.82  ? 82  PRO   B CB  1 
ATOM   1009 C CB  D PRO   B 2 73  ? -29.694 -4.464  -4.518  0.30 30.82  ? 82  PRO   B CB  1 
ATOM   1010 C CG  A PRO   B 2 73  ? -31.018 -4.416  -4.841  0.19 30.89  ? 82  PRO   B CG  1 
ATOM   1011 C CG  B PRO   B 2 73  ? -31.017 -4.416  -4.840  0.20 30.89  ? 82  PRO   B CG  1 
ATOM   1012 C CG  C PRO   B 2 73  ? -31.142 -4.293  -4.950  0.31 30.91  ? 82  PRO   B CG  1 
ATOM   1013 C CG  D PRO   B 2 73  ? -31.142 -4.294  -4.952  0.30 30.91  ? 82  PRO   B CG  1 
ATOM   1014 C CD  A PRO   B 2 73  ? -31.348 -2.936  -4.840  0.19 30.71  ? 82  PRO   B CD  1 
ATOM   1015 C CD  B PRO   B 2 73  ? -31.348 -2.937  -4.839  0.20 30.71  ? 82  PRO   B CD  1 
ATOM   1016 C CD  C PRO   B 2 73  ? -31.445 -2.812  -4.836  0.31 30.74  ? 82  PRO   B CD  1 
ATOM   1017 C CD  D PRO   B 2 73  ? -31.446 -2.813  -4.840  0.30 30.75  ? 82  PRO   B CD  1 
ATOM   1018 N N   A TRP   B 2 74  ? -27.183 -3.790  -6.611  0.19 30.78  ? 83  TRP   B N   1 
ATOM   1019 N N   B TRP   B 2 74  ? -27.183 -3.789  -6.611  0.20 30.78  ? 83  TRP   B N   1 
ATOM   1020 N N   C TRP   B 2 74  ? -27.203 -3.743  -6.614  0.31 30.79  ? 83  TRP   B N   1 
ATOM   1021 N N   D TRP   B 2 74  ? -27.203 -3.745  -6.614  0.30 30.79  ? 83  TRP   B N   1 
ATOM   1022 C CA  A TRP   B 2 74  ? -26.531 -4.132  -7.913  0.19 30.93  ? 83  TRP   B CA  1 
ATOM   1023 C CA  B TRP   B 2 74  ? -26.532 -4.131  -7.913  0.20 30.93  ? 83  TRP   B CA  1 
ATOM   1024 C CA  C TRP   B 2 74  ? -26.541 -4.119  -7.908  0.31 30.94  ? 83  TRP   B CA  1 
ATOM   1025 C CA  D TRP   B 2 74  ? -26.541 -4.119  -7.908  0.30 30.94  ? 83  TRP   B CA  1 
ATOM   1026 C C   A TRP   B 2 74  ? -27.388 -5.146  -8.679  0.19 31.70  ? 83  TRP   B C   1 
ATOM   1027 C C   B TRP   B 2 74  ? -27.388 -5.145  -8.679  0.20 31.70  ? 83  TRP   B C   1 
ATOM   1028 C C   C TRP   B 2 74  ? -27.392 -5.138  -8.674  0.31 31.72  ? 83  TRP   B C   1 
ATOM   1029 C C   D TRP   B 2 74  ? -27.392 -5.138  -8.674  0.30 31.72  ? 83  TRP   B C   1 
ATOM   1030 O O   A TRP   B 2 74  ? -27.712 -6.194  -8.096  0.19 31.88  ? 83  TRP   B O   1 
ATOM   1031 O O   B TRP   B 2 74  ? -27.712 -6.194  -8.096  0.20 31.88  ? 83  TRP   B O   1 
ATOM   1032 O O   C TRP   B 2 74  ? -27.714 -6.186  -8.093  0.31 31.89  ? 83  TRP   B O   1 
ATOM   1033 O O   D TRP   B 2 74  ? -27.714 -6.186  -8.093  0.30 31.89  ? 83  TRP   B O   1 
ATOM   1034 C CB  A TRP   B 2 74  ? -25.112 -4.685  -7.673  0.19 30.66  ? 83  TRP   B CB  1 
ATOM   1035 C CB  B TRP   B 2 74  ? -25.112 -4.684  -7.673  0.20 30.66  ? 83  TRP   B CB  1 
ATOM   1036 C CB  C TRP   B 2 74  ? -25.118 -4.675  -7.672  0.31 30.68  ? 83  TRP   B CB  1 
ATOM   1037 C CB  D TRP   B 2 74  ? -25.118 -4.675  -7.672  0.30 30.68  ? 83  TRP   B CB  1 
ATOM   1038 C CG  A TRP   B 2 74  ? -24.298 -4.863  -8.920  0.19 30.31  ? 83  TRP   B CG  1 
ATOM   1039 C CG  B TRP   B 2 74  ? -24.299 -4.863  -8.920  0.20 30.31  ? 83  TRP   B CG  1 
ATOM   1040 C CG  C TRP   B 2 74  ? -24.302 -4.858  -8.921  0.31 30.31  ? 83  TRP   B CG  1 
ATOM   1041 C CG  D TRP   B 2 74  ? -24.302 -4.858  -8.921  0.30 30.31  ? 83  TRP   B CG  1 
ATOM   1042 C CD1 A TRP   B 2 74  ? -24.203 -5.983  -9.695  0.19 30.42  ? 83  TRP   B CD1 1 
ATOM   1043 C CD1 B TRP   B 2 74  ? -24.204 -5.983  -9.695  0.20 30.42  ? 83  TRP   B CD1 1 
ATOM   1044 C CD1 C TRP   B 2 74  ? -24.205 -5.980  -9.695  0.31 30.43  ? 83  TRP   B CD1 1 
ATOM   1045 C CD1 D TRP   B 2 74  ? -24.205 -5.980  -9.695  0.30 30.43  ? 83  TRP   B CD1 1 
ATOM   1046 C CD2 A TRP   B 2 74  ? -23.441 -3.882  -9.532  0.19 30.01  ? 83  TRP   B CD2 1 
ATOM   1047 C CD2 B TRP   B 2 74  ? -23.441 -3.882  -9.532  0.20 30.01  ? 83  TRP   B CD2 1 
ATOM   1048 C CD2 C TRP   B 2 74  ? -23.439 -3.881  -9.531  0.31 30.01  ? 83  TRP   B CD2 1 
ATOM   1049 C CD2 D TRP   B 2 74  ? -23.439 -3.881  -9.531  0.30 30.01  ? 83  TRP   B CD2 1 
ATOM   1050 N NE1 A TRP   B 2 74  ? -23.368 -5.758  -10.760 0.19 30.28  ? 83  TRP   B NE1 1 
ATOM   1051 N NE1 B TRP   B 2 74  ? -23.368 -5.758  -10.760 0.20 30.28  ? 83  TRP   B NE1 1 
ATOM   1052 N NE1 C TRP   B 2 74  ? -23.370 -5.756  -10.764 0.31 30.28  ? 83  TRP   B NE1 1 
ATOM   1053 N NE1 D TRP   B 2 74  ? -23.369 -5.756  -10.764 0.30 30.28  ? 83  TRP   B NE1 1 
ATOM   1054 C CE2 A TRP   B 2 74  ? -22.889 -4.478  -10.689 0.19 30.05  ? 83  TRP   B CE2 1 
ATOM   1055 C CE2 B TRP   B 2 74  ? -22.889 -4.478  -10.689 0.20 30.05  ? 83  TRP   B CE2 1 
ATOM   1056 C CE2 C TRP   B 2 74  ? -22.890 -4.475  -10.693 0.31 30.05  ? 83  TRP   B CE2 1 
ATOM   1057 C CE2 D TRP   B 2 74  ? -22.890 -4.476  -10.693 0.30 30.05  ? 83  TRP   B CE2 1 
ATOM   1058 C CE3 A TRP   B 2 74  ? -23.112 -2.553  -9.236  0.19 29.80  ? 83  TRP   B CE3 1 
ATOM   1059 C CE3 B TRP   B 2 74  ? -23.112 -2.553  -9.236  0.20 29.80  ? 83  TRP   B CE3 1 
ATOM   1060 C CE3 C TRP   B 2 74  ? -23.111 -2.551  -9.236  0.31 29.80  ? 83  TRP   B CE3 1 
ATOM   1061 C CE3 D TRP   B 2 74  ? -23.111 -2.551  -9.236  0.30 29.80  ? 83  TRP   B CE3 1 
ATOM   1062 C CZ2 A TRP   B 2 74  ? -22.012 -3.795  -11.533 0.19 29.93  ? 83  TRP   B CZ2 1 
ATOM   1063 C CZ2 B TRP   B 2 74  ? -22.013 -3.795  -11.533 0.20 29.93  ? 83  TRP   B CZ2 1 
ATOM   1064 C CZ2 C TRP   B 2 74  ? -22.013 -3.792  -11.536 0.31 29.93  ? 83  TRP   B CZ2 1 
ATOM   1065 C CZ2 D TRP   B 2 74  ? -22.012 -3.792  -11.536 0.30 29.93  ? 83  TRP   B CZ2 1 
ATOM   1066 C CZ3 A TRP   B 2 74  ? -22.253 -1.876  -10.077 0.19 29.77  ? 83  TRP   B CZ3 1 
ATOM   1067 C CZ3 B TRP   B 2 74  ? -22.253 -1.876  -10.077 0.20 29.77  ? 83  TRP   B CZ3 1 
ATOM   1068 C CZ3 C TRP   B 2 74  ? -22.252 -1.874  -10.080 0.31 29.78  ? 83  TRP   B CZ3 1 
ATOM   1069 C CZ3 D TRP   B 2 74  ? -22.252 -1.874  -10.080 0.30 29.78  ? 83  TRP   B CZ3 1 
ATOM   1070 C CH2 A TRP   B 2 74  ? -21.710 -2.493  -11.209 0.19 29.79  ? 83  TRP   B CH2 1 
ATOM   1071 C CH2 B TRP   B 2 74  ? -21.710 -2.493  -11.209 0.20 29.79  ? 83  TRP   B CH2 1 
ATOM   1072 C CH2 C TRP   B 2 74  ? -21.710 -2.492  -11.213 0.31 29.78  ? 83  TRP   B CH2 1 
ATOM   1073 C CH2 D TRP   B 2 74  ? -21.710 -2.492  -11.213 0.30 29.78  ? 83  TRP   B CH2 1 
ATOM   1074 N N   . LYS   B 2 75  ? -27.676 -4.870  -9.963  1.00 32.20  ? 84  LYS   B N   1 
ATOM   1075 C CA  . LYS   B 2 75  ? -28.609 -5.687  -10.785 1.00 33.77  ? 84  LYS   B CA  1 
ATOM   1076 C C   . LYS   B 2 75  ? -27.875 -6.484  -11.862 1.00 35.01  ? 84  LYS   B C   1 
ATOM   1077 O O   . LYS   B 2 75  ? -28.501 -7.416  -12.349 1.00 36.98  ? 84  LYS   B O   1 
ATOM   1078 C CB  . LYS   B 2 75  ? -29.599 -4.781  -11.518 1.00 35.06  ? 84  LYS   B CB  1 
ATOM   1079 C CG  . LYS   B 2 75  ? -30.477 -3.895  -10.662 1.00 35.35  ? 84  LYS   B CG  1 
ATOM   1080 C CD  . LYS   B 2 75  ? -31.481 -4.669  -9.883  1.00 37.17  ? 84  LYS   B CD  1 
ATOM   1081 C CE  . LYS   B 2 75  ? -32.304 -3.756  -8.997  1.00 37.53  ? 84  LYS   B CE  1 
ATOM   1082 N NZ  . LYS   B 2 75  ? -33.341 -4.535  -8.298  1.00 39.07  ? 84  LYS   B NZ  1 
ATOM   1083 N N   . LEU   B 2 76  ? -26.626 -6.177  -12.216 1.00 35.62  ? 85  LEU   B N   1 
ATOM   1084 C CA  . LEU   B 2 76  ? -25.945 -6.732  -13.441 1.00 37.04  ? 85  LEU   B CA  1 
ATOM   1085 C C   . LEU   B 2 76  ? -25.260 -8.043  -13.048 1.00 38.63  ? 85  LEU   B C   1 
ATOM   1086 O O   . LEU   B 2 76  ? -24.400 -8.029  -12.150 1.00 38.38  ? 85  LEU   B O   1 
ATOM   1087 C CB  . LEU   B 2 76  ? -24.952 -5.686  -13.966 1.00 36.29  ? 85  LEU   B CB  1 
ATOM   1088 C CG  . LEU   B 2 76  ? -25.546 -4.278  -14.030 1.00 36.36  ? 85  LEU   B CG  1 
ATOM   1089 C CD1 . LEU   B 2 76  ? -24.592 -3.263  -14.632 1.00 36.60  ? 85  LEU   B CD1 1 
ATOM   1090 C CD2 . LEU   B 2 76  ? -26.871 -4.290  -14.769 1.00 37.46  ? 85  LEU   B CD2 1 
ATOM   1091 N N   . ASP   B 2 77  ? -25.689 -9.162  -13.612 1.00 40.68  ? 86  ASP   B N   1 
ATOM   1092 C CA  . ASP   B 2 77  ? -25.197 -10.488 -13.160 1.00 43.56  ? 86  ASP   B CA  1 
ATOM   1093 C C   . ASP   B 2 77  ? -24.595 -11.293 -14.324 1.00 41.94  ? 86  ASP   B C   1 
ATOM   1094 O O   . ASP   B 2 77  ? -24.057 -12.357 -14.091 1.00 41.47  ? 86  ASP   B O   1 
ATOM   1095 C CB  . ASP   B 2 77  ? -26.293 -11.246 -12.405 1.00 47.75  ? 86  ASP   B CB  1 
ATOM   1096 C CG  . ASP   B 2 77  ? -27.584 -11.361 -13.186 1.00 52.07  ? 86  ASP   B CG  1 
ATOM   1097 O OD1 . ASP   B 2 77  ? -27.663 -10.761 -14.295 1.00 57.74  ? 86  ASP   B OD1 1 
ATOM   1098 O OD2 . ASP   B 2 77  ? -28.503 -12.059 -12.705 1.00 57.43  ? 86  ASP   B OD2 1 
ATOM   1099 N N   . ALA   B 2 78  ? -24.583 -10.789 -15.547 1.00 40.28  ? 87  ALA   B N   1 
ATOM   1100 C CA  . ALA   B 2 78  ? -24.036 -11.574 -16.661 1.00 39.84  ? 87  ALA   B CA  1 
ATOM   1101 C C   . ALA   B 2 78  ? -22.525 -11.698 -16.465 1.00 38.87  ? 87  ALA   B C   1 
ATOM   1102 O O   . ALA   B 2 78  ? -21.908 -10.787 -15.792 1.00 37.46  ? 87  ALA   B O   1 
ATOM   1103 C CB  . ALA   B 2 78  ? -24.427 -10.936 -17.979 1.00 40.36  ? 87  ALA   B CB  1 
ATOM   1104 N N   . ALA   B 2 79  ? -21.941 -12.755 -17.056 1.00 38.97  ? 88  ALA   B N   1 
ATOM   1105 C CA  . ALA   B 2 79  ? -20.490 -13.027 -17.008 1.00 39.29  ? 88  ALA   B CA  1 
ATOM   1106 C C   . ALA   B 2 79  ? -19.941 -13.249 -18.414 1.00 39.31  ? 88  ALA   B C   1 
ATOM   1107 O O   . ALA   B 2 79  ? -20.633 -13.902 -19.194 1.00 38.95  ? 88  ALA   B O   1 
ATOM   1108 C CB  . ALA   B 2 79  ? -20.214 -14.235 -16.149 1.00 40.11  ? 88  ALA   B CB  1 
ATOM   1109 N N   . TRP   B 2 80  ? -18.709 -12.794 -18.655 1.00 39.35  ? 89  TRP   B N   1 
ATOM   1110 C CA  . TRP   B 2 80  ? -17.852 -13.226 -19.784 1.00 40.72  ? 89  TRP   B CA  1 
ATOM   1111 C C   . TRP   B 2 80  ? -17.832 -14.751 -19.825 1.00 41.92  ? 89  TRP   B C   1 
ATOM   1112 O O   . TRP   B 2 80  ? -17.680 -15.377 -18.740 1.00 39.80  ? 89  TRP   B O   1 
ATOM   1113 C CB  . TRP   B 2 80  ? -16.432 -12.646 -19.725 1.00 40.59  ? 89  TRP   B CB  1 
ATOM   1114 C CG  . TRP   B 2 80  ? -15.636 -12.994 -20.945 1.00 40.75  ? 89  TRP   B CG  1 
ATOM   1115 C CD1 . TRP   B 2 80  ? -16.098 -13.040 -22.234 1.00 41.57  ? 89  TRP   B CD1 1 
ATOM   1116 C CD2 . TRP   B 2 80  ? -14.243 -13.362 -21.004 1.00 41.13  ? 89  TRP   B CD2 1 
ATOM   1117 N NE1 . TRP   B 2 80  ? -15.098 -13.414 -23.083 1.00 41.62  ? 89  TRP   B NE1 1 
ATOM   1118 C CE2 . TRP   B 2 80  ? -13.952 -13.629 -22.362 1.00 41.10  ? 89  TRP   B CE2 1 
ATOM   1119 C CE3 . TRP   B 2 80  ? -13.221 -13.528 -20.057 1.00 40.40  ? 89  TRP   B CE3 1 
ATOM   1120 C CZ2 . TRP   B 2 80  ? -12.686 -14.013 -22.794 1.00 41.33  ? 89  TRP   B CZ2 1 
ATOM   1121 C CZ3 . TRP   B 2 80  ? -11.967 -13.926 -20.487 1.00 40.58  ? 89  TRP   B CZ3 1 
ATOM   1122 C CH2 . TRP   B 2 80  ? -11.704 -14.142 -21.845 1.00 41.15  ? 89  TRP   B CH2 1 
ATOM   1123 N N   . ASP   B 2 81  ? -18.033 -15.323 -21.024 1.00 42.57  ? 90  ASP   B N   1 
ATOM   1124 C CA  . ASP   B 2 81  ? -18.129 -16.799 -21.202 1.00 44.46  ? 90  ASP   B CA  1 
ATOM   1125 C C   . ASP   B 2 81  ? -16.716 -17.393 -20.978 1.00 45.43  ? 90  ASP   B C   1 
ATOM   1126 O O   . ASP   B 2 81  ? -16.634 -18.578 -20.586 1.00 47.47  ? 90  ASP   B O   1 
ATOM   1127 C CB  . ASP   B 2 81  ? -18.801 -17.190 -22.552 1.00 44.38  ? 90  ASP   B CB  1 
ATOM   1128 C CG  . ASP   B 2 81  ? -18.092 -16.730 -23.799 1.00 45.38  ? 90  ASP   B CG  1 
ATOM   1129 O OD1 . ASP   B 2 81  ? -16.954 -16.257 -23.655 1.00 45.99  ? 90  ASP   B OD1 1 
ATOM   1130 O OD2 . ASP   B 2 81  ? -18.707 -16.791 -24.913 1.00 45.73  ? 90  ASP   B OD2 1 
ATOM   1131 N N   . GLY   B 2 82  ? -15.665 -16.590 -21.219 1.00 46.22  ? 91  GLY   B N   1 
ATOM   1132 C CA  . GLY   B 2 82  ? -14.240 -16.982 -21.207 1.00 46.09  ? 91  GLY   B CA  1 
ATOM   1133 C C   . GLY   B 2 82  ? -13.710 -17.316 -22.613 1.00 47.98  ? 91  GLY   B C   1 
ATOM   1134 O O   . GLY   B 2 82  ? -12.541 -17.756 -22.677 1.00 48.45  ? 91  GLY   B O   1 
ATOM   1135 N N   . LEU   B 2 83  ? -14.525 -17.188 -23.678 1.00 48.65  ? 92  LEU   B N   1 
ATOM   1136 C CA  . LEU   B 2 83  ? -14.200 -17.634 -25.071 1.00 50.66  ? 92  LEU   B CA  1 
ATOM   1137 C C   . LEU   B 2 83  ? -14.488 -16.546 -26.125 1.00 50.50  ? 92  LEU   B C   1 
ATOM   1138 O O   . LEU   B 2 83  ? -13.702 -16.424 -27.121 1.00 49.76  ? 92  LEU   B O   1 
ATOM   1139 C CB  . LEU   B 2 83  ? -15.074 -18.842 -25.414 1.00 53.43  ? 92  LEU   B CB  1 
ATOM   1140 C CG  . LEU   B 2 83  ? -14.685 -20.195 -24.832 1.00 55.54  ? 92  LEU   B CG  1 
ATOM   1141 C CD1 . LEU   B 2 83  ? -15.658 -21.244 -25.355 1.00 57.36  ? 92  LEU   B CD1 1 
ATOM   1142 C CD2 . LEU   B 2 83  ? -13.259 -20.583 -25.212 1.00 56.27  ? 92  LEU   B CD2 1 
ATOM   1143 N N   . SER   B 2 84  ? -15.643 -15.881 -26.034 1.00 48.95  ? 93  SER   B N   1 
ATOM   1144 C CA  . SER   B 2 84  ? -16.206 -15.075 -27.152 1.00 49.10  ? 93  SER   B CA  1 
ATOM   1145 C C   . SER   B 2 84  ? -15.705 -13.633 -27.075 1.00 47.61  ? 93  SER   B C   1 
ATOM   1146 O O   . SER   B 2 84  ? -15.325 -13.160 -25.957 1.00 47.20  ? 93  SER   B O   1 
ATOM   1147 C CB  . SER   B 2 84  ? -17.706 -15.102 -27.139 1.00 49.45  ? 93  SER   B CB  1 
ATOM   1148 O OG  . SER   B 2 84  ? -18.173 -16.412 -26.862 1.00 49.61  ? 93  SER   B OG  1 
ATOM   1149 N N   . GLU   B 2 85  ? -15.718 -12.982 -28.233 1.00 46.28  ? 94  GLU   B N   1 
ATOM   1150 C CA  . GLU   B 2 85  ? -15.514 -11.515 -28.412 1.00 45.08  ? 94  GLU   B CA  1 
ATOM   1151 C C   . GLU   B 2 85  ? -16.812 -10.783 -27.834 1.00 42.69  ? 94  GLU   B C   1 
ATOM   1152 O O   . GLU   B 2 85  ? -18.114 -11.267 -27.570 1.00 42.61  ? 94  GLU   B O   1 
ATOM   1153 C CB  . GLU   B 2 85  ? -15.315 -11.126 -29.891 1.00 45.95  ? 94  GLU   B CB  1 
ATOM   1154 C CG  . GLU   B 2 85  ? -13.881 -11.315 -30.406 1.00 46.54  ? 94  GLU   B CG  1 
ATOM   1155 C CD  . GLU   B 2 85  ? -13.521 -10.752 -31.796 1.00 49.03  ? 94  GLU   B CD  1 
ATOM   1156 O OE1 . GLU   B 2 85  ? -14.330 -10.014 -32.388 1.00 48.01  ? 94  GLU   B OE1 1 
ATOM   1157 O OE2 . GLU   B 2 85  ? -12.401 -11.054 -32.293 1.00 49.87  ? 94  GLU   B OE2 1 
ATOM   1158 N N   . VAL   B 2 86  ? -16.398 -9.629  -27.177 1.00 40.79  ? 95  VAL   B N   1 
ATOM   1159 C CA  . VAL   B 2 86  ? -17.316 -8.725  -26.436 1.00 38.99  ? 95  VAL   B CA  1 
ATOM   1160 C C   . VAL   B 2 86  ? -17.231 -7.339  -27.046 1.00 38.57  ? 95  VAL   B C   1 
ATOM   1161 O O   . VAL   B 2 86  ? -16.343 -7.130  -27.912 1.00 40.62  ? 95  VAL   B O   1 
ATOM   1162 C CB  . VAL   B 2 86  ? -16.948 -8.663  -24.925 1.00 37.35  ? 95  VAL   B CB  1 
ATOM   1163 C CG1 . VAL   B 2 86  ? -16.856 -10.050 -24.347 1.00 37.38  ? 95  VAL   B CG1 1 
ATOM   1164 C CG2 . VAL   B 2 86  ? -15.629 -7.928  -24.723 1.00 37.17  ? 95  VAL   B CG2 1 
ATOM   1165 N N   . GLN   B 2 87  ? -18.103 -6.427  -26.602 1.00 37.52  ? 96  GLN   B N   1 
ATOM   1166 C CA  . GLN   B 2 87  ? -18.080 -5.023  -27.075 1.00 37.41  ? 96  GLN   B CA  1 
ATOM   1167 C C   . GLN   B 2 87  ? -18.003 -4.094  -25.883 1.00 36.19  ? 96  GLN   B C   1 
ATOM   1168 O O   . GLN   B 2 87  ? -18.859 -4.235  -25.030 1.00 37.07  ? 96  GLN   B O   1 
ATOM   1169 C CB  . GLN   B 2 87  ? -19.268 -4.677  -27.983 1.00 37.42  ? 96  GLN   B CB  1 
ATOM   1170 C CG  . GLN   B 2 87  ? -19.221 -5.452  -29.289 1.00 38.15  ? 96  GLN   B CG  1 
ATOM   1171 C CD  . GLN   B 2 87  ? -20.262 -4.996  -30.277 1.00 38.66  ? 96  GLN   B CD  1 
ATOM   1172 O OE1 . GLN   B 2 87  ? -21.176 -4.223  -29.963 1.00 38.47  ? 96  GLN   B OE1 1 
ATOM   1173 N NE2 . GLN   B 2 87  ? -20.068 -5.429  -31.531 1.00 39.24  ? 96  GLN   B NE2 1 
ATOM   1174 N N   . LEU   B 2 88  ? -16.977 -3.241  -25.859 1.00 35.42  ? 97  LEU   B N   1 
ATOM   1175 C CA  . LEU   B 2 88  ? -16.947 -2.042  -25.003 1.00 34.84  ? 97  LEU   B CA  1 
ATOM   1176 C C   . LEU   B 2 88  ? -17.829 -0.995  -25.661 1.00 35.02  ? 97  LEU   B C   1 
ATOM   1177 O O   . LEU   B 2 88  ? -17.524 -0.539  -26.809 1.00 35.62  ? 97  LEU   B O   1 
ATOM   1178 C CB  . LEU   B 2 88  ? -15.511 -1.538  -24.830 1.00 34.78  ? 97  LEU   B CB  1 
ATOM   1179 C CG  . LEU   B 2 88  ? -15.368 -0.208  -24.116 1.00 34.57  ? 97  LEU   B CG  1 
ATOM   1180 C CD1 . LEU   B 2 88  ? -15.789 -0.341  -22.637 1.00 34.17  ? 97  LEU   B CD1 1 
ATOM   1181 C CD2 . LEU   B 2 88  ? -13.935 0.286   -24.198 1.00 34.76  ? 97  LEU   B CD2 1 
ATOM   1182 N N   A LEU   B 2 89  ? -18.916 -0.629  -24.985 0.25 34.60  ? 98  LEU   B N   1 
ATOM   1183 N N   B LEU   B 2 89  ? -18.916 -0.629  -24.985 0.25 34.60  ? 98  LEU   B N   1 
ATOM   1184 N N   C LEU   B 2 89  ? -18.937 -0.645  -25.005 0.25 34.63  ? 98  LEU   B N   1 
ATOM   1185 N N   D LEU   B 2 89  ? -18.937 -0.645  -25.005 0.25 34.63  ? 98  LEU   B N   1 
ATOM   1186 C CA  A LEU   B 2 89  ? -19.764 0.521   -25.370 0.25 34.76  ? 98  LEU   B CA  1 
ATOM   1187 C CA  B LEU   B 2 89  ? -19.764 0.521   -25.370 0.25 34.76  ? 98  LEU   B CA  1 
ATOM   1188 C CA  C LEU   B 2 89  ? -19.759 0.526   -25.395 0.25 34.80  ? 98  LEU   B CA  1 
ATOM   1189 C CA  D LEU   B 2 89  ? -19.759 0.526   -25.395 0.25 34.80  ? 98  LEU   B CA  1 
ATOM   1190 C C   A LEU   B 2 89  ? -19.110 1.772   -24.776 0.25 34.71  ? 98  LEU   B C   1 
ATOM   1191 C C   B LEU   B 2 89  ? -19.110 1.772   -24.776 0.25 34.71  ? 98  LEU   B C   1 
ATOM   1192 C C   C LEU   B 2 89  ? -19.095 1.755   -24.771 0.25 34.72  ? 98  LEU   B C   1 
ATOM   1193 C C   D LEU   B 2 89  ? -19.095 1.755   -24.771 0.25 34.72  ? 98  LEU   B C   1 
ATOM   1194 O O   A LEU   B 2 89  ? -19.589 2.264   -23.722 0.25 34.48  ? 98  LEU   B O   1 
ATOM   1195 O O   B LEU   B 2 89  ? -19.589 2.264   -23.722 0.25 34.48  ? 98  LEU   B O   1 
ATOM   1196 O O   C LEU   B 2 89  ? -19.551 2.209   -23.693 0.25 34.49  ? 98  LEU   B O   1 
ATOM   1197 O O   D LEU   B 2 89  ? -19.551 2.209   -23.693 0.25 34.49  ? 98  LEU   B O   1 
ATOM   1198 C CB  A LEU   B 2 89  ? -21.184 0.257   -24.866 0.25 34.50  ? 98  LEU   B CB  1 
ATOM   1199 C CB  B LEU   B 2 89  ? -21.184 0.257   -24.866 0.25 34.50  ? 98  LEU   B CB  1 
ATOM   1200 C CB  C LEU   B 2 89  ? -21.207 0.331   -24.938 0.25 34.57  ? 98  LEU   B CB  1 
ATOM   1201 C CB  D LEU   B 2 89  ? -21.207 0.331   -24.938 0.25 34.57  ? 98  LEU   B CB  1 
ATOM   1202 C CG  A LEU   B 2 89  ? -22.219 1.364   -25.076 0.25 34.62  ? 98  LEU   B CG  1 
ATOM   1203 C CG  B LEU   B 2 89  ? -22.219 1.364   -25.076 0.25 34.62  ? 98  LEU   B CG  1 
ATOM   1204 C CG  C LEU   B 2 89  ? -22.208 1.381   -25.429 0.25 34.82  ? 98  LEU   B CG  1 
ATOM   1205 C CG  D LEU   B 2 89  ? -22.208 1.381   -25.429 0.25 34.82  ? 98  LEU   B CG  1 
ATOM   1206 C CD1 A LEU   B 2 89  ? -21.692 2.486   -25.950 0.25 35.05  ? 98  LEU   B CD1 1 
ATOM   1207 C CD1 B LEU   B 2 89  ? -21.692 2.486   -25.950 0.25 35.05  ? 98  LEU   B CD1 1 
ATOM   1208 C CD1 C LEU   B 2 89  ? -22.174 1.514   -26.946 0.25 35.50  ? 98  LEU   B CD1 1 
ATOM   1209 C CD1 D LEU   B 2 89  ? -22.174 1.514   -26.946 0.25 35.50  ? 98  LEU   B CD1 1 
ATOM   1210 C CD2 A LEU   B 2 89  ? -23.506 0.790   -25.648 0.25 34.88  ? 98  LEU   B CD2 1 
ATOM   1211 C CD2 B LEU   B 2 89  ? -23.506 0.790   -25.648 0.25 34.88  ? 98  LEU   B CD2 1 
ATOM   1212 C CD2 C LEU   B 2 89  ? -23.618 1.050   -24.962 0.25 34.65  ? 98  LEU   B CD2 1 
ATOM   1213 C CD2 D LEU   B 2 89  ? -23.618 1.050   -24.962 0.25 34.65  ? 98  LEU   B CD2 1 
ATOM   1214 N N   . ALA   B 2 90  ? -18.025 2.231   -25.417 1.00 35.06  ? 99  ALA   B N   1 
ATOM   1215 C CA  . ALA   B 2 90  ? -17.249 3.400   -24.968 1.00 34.92  ? 99  ALA   B CA  1 
ATOM   1216 C C   . ALA   B 2 90  ? -18.104 4.650   -25.155 1.00 35.22  ? 99  ALA   B C   1 
ATOM   1217 O O   . ALA   B 2 90  ? -18.719 4.854   -26.298 1.00 35.20  ? 99  ALA   B O   1 
ATOM   1218 C CB  . ALA   B 2 90  ? -15.916 3.500   -25.659 1.00 35.43  ? 99  ALA   B CB  1 
ATOM   1219 N N   . VAL   B 2 91  ? -18.176 5.430   -24.062 1.00 34.79  ? 100 VAL   B N   1 
ATOM   1220 C CA  . VAL   B 2 91  ? -18.733 6.800   -24.040 1.00 34.93  ? 100 VAL   B CA  1 
ATOM   1221 C C   . VAL   B 2 91  ? -17.615 7.762   -23.641 1.00 35.42  ? 100 VAL   B C   1 
ATOM   1222 O O   . VAL   B 2 91  ? -17.475 8.162   -22.475 1.00 34.73  ? 100 VAL   B O   1 
ATOM   1223 C CB  . VAL   B 2 91  ? -19.957 6.850   -23.124 1.00 34.34  ? 100 VAL   B CB  1 
ATOM   1224 C CG1 . VAL   B 2 91  ? -20.691 8.177   -23.205 1.00 34.49  ? 100 VAL   B CG1 1 
ATOM   1225 C CG2 . VAL   B 2 91  ? -20.908 5.693   -23.430 1.00 34.35  ? 100 VAL   B CG2 1 
ATOM   1226 N N   . PRO   B 2 92  ? -16.770 8.187   -24.610 1.00 35.84  ? 101 PRO   B N   1 
ATOM   1227 C CA  . PRO   B 2 92  ? -15.648 9.087   -24.332 1.00 36.09  ? 101 PRO   B CA  1 
ATOM   1228 C C   . PRO   B 2 92  ? -16.151 10.491  -24.052 1.00 36.63  ? 101 PRO   B C   1 
ATOM   1229 O O   . PRO   B 2 92  ? -17.285 10.839  -24.407 1.00 37.12  ? 101 PRO   B O   1 
ATOM   1230 C CB  . PRO   B 2 92  ? -14.774 9.008   -25.604 1.00 36.76  ? 101 PRO   B CB  1 
ATOM   1231 C CG  . PRO   B 2 92  ? -15.315 7.815   -26.360 1.00 36.54  ? 101 PRO   B CG  1 
ATOM   1232 C CD  . PRO   B 2 92  ? -16.787 7.790   -26.046 1.00 36.44  ? 101 PRO   B CD  1 
ATOM   1233 N N   . PRO   B 2 93  ? -15.336 11.356  -23.416 1.00 37.54  ? 102 PRO   B N   1 
ATOM   1234 C CA  . PRO   B 2 93  ? -15.770 12.711  -23.095 1.00 38.61  ? 102 PRO   B CA  1 
ATOM   1235 C C   . PRO   B 2 93  ? -15.935 13.560  -24.369 1.00 39.80  ? 102 PRO   B C   1 
ATOM   1236 O O   . PRO   B 2 93  ? -15.021 13.565  -25.182 1.00 40.60  ? 102 PRO   B O   1 
ATOM   1237 C CB  . PRO   B 2 93  ? -14.669 13.228  -22.156 1.00 38.56  ? 102 PRO   B CB  1 
ATOM   1238 C CG  . PRO   B 2 93  ? -14.120 11.944  -21.564 1.00 37.91  ? 102 PRO   B CG  1 
ATOM   1239 C CD  . PRO   B 2 93  ? -14.043 11.045  -22.786 1.00 37.94  ? 102 PRO   B CD  1 
ATOM   1240 N N   . GLY   B 2 94  ? -17.094 14.200  -24.496 1.00 40.36  ? 103 GLY   B N   1 
ATOM   1241 C CA  . GLY   B 2 94  ? -17.498 15.047  -25.631 1.00 41.98  ? 103 GLY   B CA  1 
ATOM   1242 C C   . GLY   B 2 94  ? -17.673 14.303  -26.957 1.00 42.82  ? 103 GLY   B C   1 
ATOM   1243 O O   . GLY   B 2 94  ? -17.833 14.996  -27.969 1.00 43.13  ? 103 GLY   B O   1 
ATOM   1244 N N   . GLU   B 2 95  ? -17.719 12.973  -26.977 1.00 43.11  ? 104 GLU   B N   1 
ATOM   1245 C CA  . GLU   B 2 95  ? -17.789 12.162  -28.224 1.00 44.19  ? 104 GLU   B CA  1 
ATOM   1246 C C   . GLU   B 2 95  ? -18.953 11.190  -28.099 1.00 44.35  ? 104 GLU   B C   1 
ATOM   1247 O O   . GLU   B 2 95  ? -19.317 10.831  -26.960 1.00 42.36  ? 104 GLU   B O   1 
ATOM   1248 C CB  . GLU   B 2 95  ? -16.482 11.404  -28.461 1.00 45.04  ? 104 GLU   B CB  1 
ATOM   1249 C CG  . GLU   B 2 95  ? -15.244 12.277  -28.260 1.00 46.36  ? 104 GLU   B CG  1 
ATOM   1250 C CD  . GLU   B 2 95  ? -13.890 11.574  -28.371 1.00 47.67  ? 104 GLU   B CD  1 
ATOM   1251 O OE1 . GLU   B 2 95  ? -13.900 10.340  -28.340 1.00 49.15  ? 104 GLU   B OE1 1 
ATOM   1252 O OE2 . GLU   B 2 95  ? -12.809 12.271  -28.506 1.00 48.59  ? 104 GLU   B OE2 1 
ATOM   1253 N N   . ARG   B 2 96  ? -19.527 10.757  -29.209 1.00 44.74  ? 105 ARG   B N   1 
ATOM   1254 C CA  . ARG   B 2 96  ? -20.733 9.894   -29.205 1.00 46.25  ? 105 ARG   B CA  1 
ATOM   1255 C C   . ARG   B 2 96  ? -20.351 8.515   -28.689 1.00 44.83  ? 105 ARG   B C   1 
ATOM   1256 O O   . ARG   B 2 96  ? -19.172 8.121   -28.841 1.00 42.99  ? 105 ARG   B O   1 
ATOM   1257 C CB  . ARG   B 2 96  ? -21.318 9.780   -30.620 1.00 50.72  ? 105 ARG   B CB  1 
ATOM   1258 C CG  . ARG   B 2 96  ? -22.679 9.098   -30.651 1.00 53.32  ? 105 ARG   B CG  1 
ATOM   1259 C CD  . ARG   B 2 96  ? -23.516 9.562   -31.828 1.00 56.31  ? 105 ARG   B CD  1 
ATOM   1260 N NE  . ARG   B 2 96  ? -22.846 9.509   -33.117 1.00 60.00  ? 105 ARG   B NE  1 
ATOM   1261 C CZ  . ARG   B 2 96  ? -22.354 10.562  -33.788 1.00 64.19  ? 105 ARG   B CZ  1 
ATOM   1262 N NH1 . ARG   B 2 96  ? -22.423 11.793  -33.300 1.00 64.82  ? 105 ARG   B NH1 1 
ATOM   1263 N NH2 . ARG   B 2 96  ? -21.814 10.380  -34.986 1.00 67.21  ? 105 ARG   B NH2 1 
ATOM   1264 N N   . ALA   B 2 97  ? -21.297 7.836   -28.036 1.00 44.39  ? 106 ALA   B N   1 
ATOM   1265 C CA  . ALA   B 2 97  ? -21.202 6.401   -27.702 1.00 43.89  ? 106 ALA   B CA  1 
ATOM   1266 C C   . ALA   B 2 97  ? -20.765 5.663   -28.970 1.00 44.89  ? 106 ALA   B C   1 
ATOM   1267 O O   . ALA   B 2 97  ? -21.396 5.893   -30.007 1.00 44.55  ? 106 ALA   B O   1 
ATOM   1268 C CB  . ALA   B 2 97  ? -22.528 5.892   -27.207 1.00 43.58  ? 106 ALA   B CB  1 
ATOM   1269 N N   . LYS   B 2 98  ? -19.760 4.793   -28.855 1.00 45.48  ? 107 LYS   B N   1 
ATOM   1270 C CA  . LYS   B 2 98  ? -19.244 3.943   -29.962 1.00 47.29  ? 107 LYS   B CA  1 
ATOM   1271 C C   . LYS   B 2 98  ? -18.916 2.552   -29.397 1.00 45.27  ? 107 LYS   B C   1 
ATOM   1272 O O   . LYS   B 2 98  ? -18.221 2.480   -28.302 1.00 43.46  ? 107 LYS   B O   1 
ATOM   1273 C CB  . LYS   B 2 98  ? -18.040 4.692   -30.537 1.00 50.70  ? 107 LYS   B CB  1 
ATOM   1274 C CG  . LYS   B 2 98  ? -17.276 4.068   -31.705 1.00 53.59  ? 107 LYS   B CG  1 
ATOM   1275 C CD  . LYS   B 2 98  ? -15.797 4.511   -31.692 1.00 56.62  ? 107 LYS   B CD  1 
ATOM   1276 C CE  . LYS   B 2 98  ? -15.306 4.907   -30.300 1.00 57.96  ? 107 LYS   B CE  1 
ATOM   1277 N NZ  . LYS   B 2 98  ? -13.885 5.336   -30.325 1.00 60.89  ? 107 LYS   B NZ  1 
ATOM   1278 N N   . ASN   B 2 99  ? -19.484 1.503   -30.003 1.00 42.41  ? 108 ASN   B N   1 
ATOM   1279 C CA  . ASN   B 2 99  ? -19.165 0.084   -29.697 1.00 42.18  ? 108 ASN   B CA  1 
ATOM   1280 C C   . ASN   B 2 99  ? -17.803 -0.304  -30.267 1.00 41.96  ? 108 ASN   B C   1 
ATOM   1281 O O   . ASN   B 2 99  ? -17.549 -0.145  -31.516 1.00 41.55  ? 108 ASN   B O   1 
ATOM   1282 C CB  . ASN   B 2 99  ? -20.231 -0.909  -30.173 1.00 42.63  ? 108 ASN   B CB  1 
ATOM   1283 C CG  . ASN   B 2 99  ? -21.574 -0.625  -29.499 1.00 43.14  ? 108 ASN   B CG  1 
ATOM   1284 O OD1 . ASN   B 2 99  ? -21.978 0.630   -29.740 1.00 46.25  ? 108 ASN   B OD1 1 
ATOM   1285 N ND2 . ASN   B 2 99  ? -22.279 -1.767  -29.164 1.00 42.93  ? 108 ASN   B ND2 1 
ATOM   1286 N N   . ILE   B 2 100 ? -16.963 -0.906  -29.449 1.00 40.12  ? 109 ILE   B N   1 
ATOM   1287 C CA  . ILE   B 2 100 ? -15.655 -1.432  -29.895 1.00 40.49  ? 109 ILE   B CA  1 
ATOM   1288 C C   . ILE   B 2 100 ? -15.585 -2.904  -29.544 1.00 40.11  ? 109 ILE   B C   1 
ATOM   1289 O O   . ILE   B 2 100 ? -15.647 -3.259  -28.292 1.00 38.91  ? 109 ILE   B O   1 
ATOM   1290 C CB  . ILE   B 2 100 ? -14.509 -0.647  -29.260 1.00 40.80  ? 109 ILE   B CB  1 
ATOM   1291 C CG1 . ILE   B 2 100 ? -14.707 0.866   -29.393 1.00 41.63  ? 109 ILE   B CG1 1 
ATOM   1292 C CG2 . ILE   B 2 100 ? -13.187 -1.144  -29.802 1.00 41.05  ? 109 ILE   B CG2 1 
ATOM   1293 C CD1 . ILE   B 2 100 ? -14.138 1.455   -30.677 1.00 42.64  ? 109 ILE   B CD1 1 
ATOM   1294 N N   . GLN   B 2 101 ? -15.368 -3.756  -30.527 1.00 40.42  ? 110 GLN   B N   1 
ATOM   1295 C CA  . GLN   B 2 101 ? -15.419 -5.215  -30.320 1.00 41.21  ? 110 GLN   B CA  1 
ATOM   1296 C C   . GLN   B 2 101 ? -13.991 -5.716  -30.138 1.00 41.75  ? 110 GLN   B C   1 
ATOM   1297 O O   . GLN   B 2 101 ? -13.120 -5.209  -30.840 1.00 42.04  ? 110 GLN   B O   1 
ATOM   1298 C CB  . GLN   B 2 101 ? -16.174 -5.901  -31.440 1.00 43.00  ? 110 GLN   B CB  1 
ATOM   1299 C CG  . GLN   B 2 101 ? -16.109 -7.410  -31.350 1.00 43.32  ? 110 GLN   B CG  1 
ATOM   1300 C CD  . GLN   B 2 101 ? -17.092 -7.994  -32.331 1.00 44.12  ? 110 GLN   B CD  1 
ATOM   1301 O OE1 . GLN   B 2 101 ? -18.182 -7.467  -32.562 1.00 44.06  ? 110 GLN   B OE1 1 
ATOM   1302 N NE2 . GLN   B 2 101 ? -16.710 -9.106  -32.921 1.00 45.41  ? 110 GLN   B NE2 1 
ATOM   1303 N N   . THR   B 2 102 ? -13.756 -6.581  -29.115 1.00 41.76  ? 111 THR   B N   1 
ATOM   1304 C CA  . THR   B 2 102 ? -12.415 -7.082  -28.697 1.00 41.53  ? 111 THR   B CA  1 
ATOM   1305 C C   . THR   B 2 102 ? -12.542 -8.471  -28.060 1.00 40.90  ? 111 THR   B C   1 
ATOM   1306 O O   . THR   B 2 102 ? -13.651 -8.845  -27.597 1.00 42.07  ? 111 THR   B O   1 
ATOM   1307 C CB  . THR   B 2 102 ? -11.666 -6.091  -27.765 1.00 40.69  ? 111 THR   B CB  1 
ATOM   1308 O OG1 . THR   B 2 102 ? -10.181 -6.512  -27.743 1.00 41.22  ? 111 THR   B OG1 1 
ATOM   1309 C CG2 . THR   B 2 102 ? -12.226 -5.908  -26.372 1.00 40.53  ? 111 THR   B CG2 1 
ATOM   1310 N N   . LEU   B 2 103 ? -11.460 -9.240  -28.115 1.00 40.85  ? 112 LEU   B N   1 
ATOM   1311 C CA  . LEU   B 2 103 ? -11.319 -10.541 -27.414 1.00 40.48  ? 112 LEU   B CA  1 
ATOM   1312 C C   . LEU   B 2 103 ? -10.578 -10.294 -26.086 1.00 40.08  ? 112 LEU   B C   1 
ATOM   1313 O O   . LEU   B 2 103 ? -9.384  -9.915  -26.012 1.00 40.03  ? 112 LEU   B O   1 
ATOM   1314 C CB  . LEU   B 2 103 ? -10.613 -11.611 -28.261 1.00 40.57  ? 112 LEU   B CB  1 
ATOM   1315 C CG  . LEU   B 2 103 ? -10.523 -12.965 -27.546 1.00 40.60  ? 112 LEU   B CG  1 
ATOM   1316 C CD1 . LEU   B 2 103 ? -11.857 -13.697 -27.543 1.00 40.74  ? 112 LEU   B CD1 1 
ATOM   1317 C CD2 . LEU   B 2 103 ? -9.434  -13.845 -28.101 1.00 41.29  ? 112 LEU   B CD2 1 
ATOM   1318 N N   . PRO   B 2 104 ? -11.276 -10.404 -24.935 1.00 39.64  ? 113 PRO   B N   1 
ATOM   1319 C CA  . PRO   B 2 104 ? -10.609 -10.157 -23.671 1.00 39.55  ? 113 PRO   B CA  1 
ATOM   1320 C C   . PRO   B 2 104 ? -9.476  -11.169 -23.368 1.00 40.23  ? 113 PRO   B C   1 
ATOM   1321 O O   . PRO   B 2 104 ? -9.699  -12.480 -23.769 1.00 42.34  ? 113 PRO   B O   1 
ATOM   1322 C CB  . PRO   B 2 104 ? -11.688 -10.381 -22.596 1.00 38.91  ? 113 PRO   B CB  1 
ATOM   1323 C CG  . PRO   B 2 104 ? -12.994 -10.390 -23.318 1.00 38.68  ? 113 PRO   B CG  1 
ATOM   1324 C CD  . PRO   B 2 104 ? -12.692 -10.771 -24.774 1.00 39.62  ? 113 PRO   B CD  1 
ATOM   1325 N N   . GLY   B 2 105 ? -8.300  -10.540 -23.021 1.00 41.22  ? 114 GLY   B N   1 
ATOM   1326 C CA  . GLY   B 2 105 ? -7.264  -11.260 -22.267 1.00 41.19  ? 114 GLY   B CA  1 
ATOM   1327 C C   . GLY   B 2 105 ? -7.754  -11.622 -20.863 1.00 41.22  ? 114 GLY   B C   1 
ATOM   1328 O O   . GLY   B 2 105 ? -8.988  -11.571 -20.600 1.00 40.26  ? 114 GLY   B O   1 
ATOM   1329 N N   . ILE   B 2 106 ? -6.800  -12.028 -20.031 1.00 42.05  ? 115 ILE   B N   1 
ATOM   1330 C CA  . ILE   B 2 106 ? -7.005  -12.577 -18.657 1.00 42.28  ? 115 ILE   B CA  1 
ATOM   1331 C C   . ILE   B 2 106 ? -6.122  -11.815 -17.680 1.00 41.82  ? 115 ILE   B C   1 
ATOM   1332 O O   . ILE   B 2 106 ? -4.934  -11.725 -17.886 1.00 42.89  ? 115 ILE   B O   1 
ATOM   1333 C CB  . ILE   B 2 106 ? -6.651  -14.066 -18.570 1.00 43.73  ? 115 ILE   B CB  1 
ATOM   1334 C CG1 . ILE   B 2 106 ? -7.432  -14.937 -19.546 1.00 45.69  ? 115 ILE   B CG1 1 
ATOM   1335 C CG2 . ILE   B 2 106 ? -6.854  -14.548 -17.148 1.00 44.60  ? 115 ILE   B CG2 1 
ATOM   1336 C CD1 . ILE   B 2 106 ? -8.860  -15.160 -19.165 1.00 45.68  ? 115 ILE   B CD1 1 
ATOM   1337 N N   . PHE   B 2 107 ? -6.700  -11.375 -16.578 1.00 41.03  ? 116 PHE   B N   1 
ATOM   1338 C CA  . PHE   B 2 107 ? -5.948  -11.031 -15.348 1.00 40.36  ? 116 PHE   B CA  1 
ATOM   1339 C C   . PHE   B 2 107 ? -5.904  -12.321 -14.535 1.00 41.32  ? 116 PHE   B C   1 
ATOM   1340 O O   . PHE   B 2 107 ? -7.011  -12.884 -14.326 1.00 40.87  ? 116 PHE   B O   1 
ATOM   1341 C CB  . PHE   B 2 107 ? -6.714  -9.942  -14.617 1.00 40.29  ? 116 PHE   B CB  1 
ATOM   1342 C CG  . PHE   B 2 107 ? -6.429  -8.503  -14.950 1.00 40.31  ? 116 PHE   B CG  1 
ATOM   1343 C CD1 . PHE   B 2 107 ? -5.624  -8.114  -16.006 1.00 40.49  ? 116 PHE   B CD1 1 
ATOM   1344 C CD2 . PHE   B 2 107 ? -7.057  -7.521  -14.194 1.00 40.20  ? 116 PHE   B CD2 1 
ATOM   1345 C CE1 . PHE   B 2 107 ? -5.402  -6.771  -16.250 1.00 40.30  ? 116 PHE   B CE1 1 
ATOM   1346 C CE2 . PHE   B 2 107 ? -6.854  -6.178  -14.457 1.00 40.04  ? 116 PHE   B CE2 1 
ATOM   1347 C CZ  . PHE   B 2 107 ? -6.045  -5.806  -15.499 1.00 40.69  ? 116 PHE   B CZ  1 
ATOM   1348 N N   . LYS   B 2 108 ? -4.702  -12.810 -14.219 1.00 42.47  ? 117 LYS   B N   1 
ATOM   1349 C CA  . LYS   B 2 108 ? -4.455  -13.962 -13.318 1.00 43.83  ? 117 LYS   B CA  1 
ATOM   1350 C C   . LYS   B 2 108 ? -4.167  -13.382 -11.921 1.00 41.61  ? 117 LYS   B C   1 
ATOM   1351 O O   . LYS   B 2 108 ? -3.246  -12.543 -11.804 1.00 39.27  ? 117 LYS   B O   1 
ATOM   1352 C CB  . LYS   B 2 108 ? -3.319  -14.842 -13.852 1.00 47.42  ? 117 LYS   B CB  1 
ATOM   1353 C CG  . LYS   B 2 108 ? -3.682  -15.683 -15.079 1.00 52.59  ? 117 LYS   B CG  1 
ATOM   1354 C CD  . LYS   B 2 108 ? -2.564  -16.143 -16.030 1.00 56.00  ? 117 LYS   B CD  1 
ATOM   1355 C CE  . LYS   B 2 108 ? -3.161  -16.781 -17.284 1.00 60.80  ? 117 LYS   B CE  1 
ATOM   1356 N NZ  . LYS   B 2 108 ? -2.191  -17.267 -18.323 1.00 63.20  ? 117 LYS   B NZ  1 
ATOM   1357 N N   . THR   B 2 109 ? -4.981  -13.737 -10.923 1.00 41.93  ? 118 THR   B N   1 
ATOM   1358 C CA  . THR   B 2 109 ? -4.824  -13.288 -9.502  1.00 41.79  ? 118 THR   B CA  1 
ATOM   1359 C C   . THR   B 2 109 ? -4.871  -14.482 -8.546  1.00 42.78  ? 118 THR   B C   1 
ATOM   1360 O O   . THR   B 2 109 ? -5.453  -15.536 -8.869  1.00 41.50  ? 118 THR   B O   1 
ATOM   1361 C CB  . THR   B 2 109 ? -5.945  -12.348 -9.040  1.00 40.93  ? 118 THR   B CB  1 
ATOM   1362 O OG1 . THR   B 2 109 ? -7.035  -13.152 -8.562  1.00 40.39  ? 118 THR   B OG1 1 
ATOM   1363 C CG2 . THR   B 2 109 ? -6.383  -11.395 -10.138 1.00 40.80  ? 118 THR   B CG2 1 
ATOM   1364 N N   . LYS   B 2 110 ? -4.345  -14.302 -7.340  1.00 44.71  ? 119 LYS   B N   1 
ATOM   1365 C CA  . LYS   B 2 110 ? -4.357  -15.387 -6.335  1.00 46.32  ? 119 LYS   B CA  1 
ATOM   1366 C C   . LYS   B 2 110 ? -5.797  -15.852 -6.068  1.00 47.48  ? 119 LYS   B C   1 
ATOM   1367 O O   . LYS   B 2 110 ? -5.948  -17.005 -5.609  1.00 50.77  ? 119 LYS   B O   1 
ATOM   1368 C CB  . LYS   B 2 110 ? -3.691  -14.943 -5.030  1.00 47.00  ? 119 LYS   B CB  1 
ATOM   1369 C CG  . LYS   B 2 110 ? -4.022  -13.539 -4.547  1.00 47.83  ? 119 LYS   B CG  1 
ATOM   1370 C CD  . LYS   B 2 110 ? -3.584  -13.257 -3.120  1.00 49.92  ? 119 LYS   B CD  1 
ATOM   1371 C CE  . LYS   B 2 110 ? -4.699  -13.432 -2.118  1.00 51.73  ? 119 LYS   B CE  1 
ATOM   1372 N NZ  . LYS   B 2 110 ? -5.498  -12.191 -1.979  1.00 52.80  ? 119 LYS   B NZ  1 
ATOM   1373 N N   . ASP   B 2 111 ? -6.809  -15.001 -6.277  1.00 45.81  ? 120 ASP   B N   1 
ATOM   1374 C CA  . ASP   B 2 111 ? -8.225  -15.357 -6.012  1.00 46.07  ? 120 ASP   B CA  1 
ATOM   1375 C C   . ASP   B 2 111 ? -8.923  -15.764 -7.293  1.00 46.94  ? 120 ASP   B C   1 
ATOM   1376 O O   . ASP   B 2 111 ? -10.142 -15.942 -7.263  1.00 48.02  ? 120 ASP   B O   1 
ATOM   1377 C CB  . ASP   B 2 111 ? -8.949  -14.225 -5.285  1.00 46.23  ? 120 ASP   B CB  1 
ATOM   1378 C CG  . ASP   B 2 111 ? -8.304  -14.020 -3.926  1.00 46.14  ? 120 ASP   B CG  1 
ATOM   1379 O OD1 . ASP   B 2 111 ? -7.866  -15.011 -3.351  1.00 46.51  ? 120 ASP   B OD1 1 
ATOM   1380 O OD2 . ASP   B 2 111 ? -8.164  -12.878 -3.517  1.00 47.37  ? 120 ASP   B OD2 1 
ATOM   1381 N N   . GLY   B 2 112 ? -8.189  -15.883 -8.394  1.00 46.87  ? 121 GLY   B N   1 
ATOM   1382 C CA  . GLY   B 2 112 ? -8.790  -16.420 -9.615  1.00 47.24  ? 121 GLY   B CA  1 
ATOM   1383 C C   . GLY   B 2 112 ? -8.619  -15.487 -10.794 1.00 47.22  ? 121 GLY   B C   1 
ATOM   1384 O O   . GLY   B 2 112 ? -8.097  -14.374 -10.634 1.00 46.44  ? 121 GLY   B O   1 
ATOM   1385 N N   . ASP   B 2 113 ? -9.075  -15.955 -11.945 1.00 47.87  ? 122 ASP   B N   1 
ATOM   1386 C CA  . ASP   B 2 113 ? -8.874  -15.283 -13.249 1.00 48.30  ? 122 ASP   B CA  1 
ATOM   1387 C C   . ASP   B 2 113 ? -10.051 -14.328 -13.468 1.00 46.59  ? 122 ASP   B C   1 
ATOM   1388 O O   . ASP   B 2 113 ? -11.167 -14.616 -12.966 1.00 43.83  ? 122 ASP   B O   1 
ATOM   1389 C CB  . ASP   B 2 113 ? -8.677  -16.324 -14.345 1.00 50.66  ? 122 ASP   B CB  1 
ATOM   1390 C CG  . ASP   B 2 113 ? -7.290  -16.945 -14.371 1.00 53.11  ? 122 ASP   B CG  1 
ATOM   1391 O OD1 . ASP   B 2 113 ? -6.437  -16.529 -13.572 1.00 58.04  ? 122 ASP   B OD1 1 
ATOM   1392 O OD2 . ASP   B 2 113 ? -7.067  -17.829 -15.212 1.00 57.13  ? 122 ASP   B OD2 1 
ATOM   1393 N N   . ILE   B 2 114 ? -9.780  -13.213 -14.152 1.00 44.29  ? 123 ILE   B N   1 
ATOM   1394 C CA  . ILE   B 2 114 ? -10.788 -12.173 -14.484 1.00 42.81  ? 123 ILE   B CA  1 
ATOM   1395 C C   . ILE   B 2 114 ? -10.539 -11.802 -15.939 1.00 40.35  ? 123 ILE   B C   1 
ATOM   1396 O O   . ILE   B 2 114 ? -9.377  -11.546 -16.236 1.00 38.90  ? 123 ILE   B O   1 
ATOM   1397 C CB  . ILE   B 2 114 ? -10.602 -10.926 -13.610 1.00 42.66  ? 123 ILE   B CB  1 
ATOM   1398 C CG1 . ILE   B 2 114 ? -10.160 -11.293 -12.206 1.00 43.97  ? 123 ILE   B CG1 1 
ATOM   1399 C CG2 . ILE   B 2 114 ? -11.834 -10.062 -13.597 1.00 43.15  ? 123 ILE   B CG2 1 
ATOM   1400 C CD1 . ILE   B 2 114 ? -10.244 -10.144 -11.245 1.00 44.55  ? 123 ILE   B CD1 1 
ATOM   1401 N N   . GLY   B 2 115 ? -11.597 -11.636 -16.728 1.00 40.20  ? 124 GLY   B N   1 
ATOM   1402 C CA  . GLY   B 2 115 ? -11.449 -11.124 -18.104 1.00 38.54  ? 124 GLY   B CA  1 
ATOM   1403 C C   . GLY   B 2 115 ? -10.873 -9.714  -18.053 1.00 38.11  ? 124 GLY   B C   1 
ATOM   1404 O O   . GLY   B 2 115 ? -10.997 -8.998  -16.979 1.00 35.77  ? 124 GLY   B O   1 
ATOM   1405 N N   . ALA   B 2 116 ? -10.227 -9.295  -19.136 1.00 37.41  ? 125 ALA   B N   1 
ATOM   1406 C CA  . ALA   B 2 116 ? -9.561  -7.982  -19.230 1.00 37.68  ? 125 ALA   B CA  1 
ATOM   1407 C C   . ALA   B 2 116 ? -9.665  -7.517  -20.671 1.00 38.14  ? 125 ALA   B C   1 
ATOM   1408 O O   . ALA   B 2 116 ? -9.601  -8.370  -21.522 1.00 37.74  ? 125 ALA   B O   1 
ATOM   1409 C CB  . ALA   B 2 116 ? -8.125  -8.091  -18.810 1.00 38.45  ? 125 ALA   B CB  1 
ATOM   1410 N N   A VAL   B 2 117 ? -9.822  -6.208  -20.914 0.19 38.01  ? 126 VAL   B N   1 
ATOM   1411 N N   B VAL   B 2 117 ? -9.788  -6.203  -20.879 0.20 38.20  ? 126 VAL   B N   1 
ATOM   1412 N N   C VAL   B 2 117 ? -9.827  -6.209  -20.912 0.31 37.99  ? 126 VAL   B N   1 
ATOM   1413 N N   D VAL   B 2 117 ? -9.789  -6.203  -20.877 0.30 38.19  ? 126 VAL   B N   1 
ATOM   1414 C CA  A VAL   B 2 117 ? -9.936  -5.629  -22.291 0.19 38.47  ? 126 VAL   B CA  1 
ATOM   1415 C CA  B VAL   B 2 117 ? -9.958  -5.529  -22.203 0.20 38.76  ? 126 VAL   B CA  1 
ATOM   1416 C CA  C VAL   B 2 117 ? -9.936  -5.630  -22.291 0.31 38.43  ? 126 VAL   B CA  1 
ATOM   1417 C CA  D VAL   B 2 117 ? -9.956  -5.527  -22.202 0.30 38.75  ? 126 VAL   B CA  1 
ATOM   1418 C C   A VAL   B 2 117 ? -8.836  -4.582  -22.523 0.19 39.00  ? 126 VAL   B C   1 
ATOM   1419 C C   B VAL   B 2 117 ? -8.729  -4.641  -22.451 0.20 39.19  ? 126 VAL   B C   1 
ATOM   1420 C C   C VAL   B 2 117 ? -8.836  -4.584  -22.522 0.31 39.01  ? 126 VAL   B C   1 
ATOM   1421 C C   D VAL   B 2 117 ? -8.726  -4.641  -22.450 0.30 39.20  ? 126 VAL   B C   1 
ATOM   1422 O O   A VAL   B 2 117 ? -8.717  -3.642  -21.720 0.19 38.85  ? 126 VAL   B O   1 
ATOM   1423 O O   B VAL   B 2 117 ? -8.337  -3.915  -21.519 0.20 39.09  ? 126 VAL   B O   1 
ATOM   1424 O O   C VAL   B 2 117 ? -8.720  -3.640  -21.727 0.31 38.88  ? 126 VAL   B O   1 
ATOM   1425 O O   D VAL   B 2 117 ? -8.325  -3.918  -21.523 0.30 39.14  ? 126 VAL   B O   1 
ATOM   1426 C CB  A VAL   B 2 117 ? -11.340 -5.057  -22.574 0.19 38.22  ? 126 VAL   B CB  1 
ATOM   1427 C CB  B VAL   B 2 117 ? -11.285 -4.743  -22.205 0.20 38.68  ? 126 VAL   B CB  1 
ATOM   1428 C CB  C VAL   B 2 117 ? -11.338 -5.059  -22.577 0.31 38.17  ? 126 VAL   B CB  1 
ATOM   1429 C CB  D VAL   B 2 117 ? -11.284 -4.742  -22.205 0.30 38.67  ? 126 VAL   B CB  1 
ATOM   1430 C CG1 A VAL   B 2 117 ? -12.389 -6.156  -22.567 0.19 38.14  ? 126 VAL   B CG1 1 
ATOM   1431 C CG1 B VAL   B 2 117 ? -11.331 -3.619  -23.225 0.20 39.21  ? 126 VAL   B CG1 1 
ATOM   1432 C CG1 C VAL   B 2 117 ? -12.387 -6.160  -22.576 0.31 38.09  ? 126 VAL   B CG1 1 
ATOM   1433 C CG1 D VAL   B 2 117 ? -11.333 -3.617  -23.223 0.30 39.27  ? 126 VAL   B CG1 1 
ATOM   1434 C CG2 A VAL   B 2 117 ? -11.734 -3.926  -21.632 0.19 37.80  ? 126 VAL   B CG2 1 
ATOM   1435 C CG2 B VAL   B 2 117 ? -12.471 -5.678  -22.391 0.20 38.72  ? 126 VAL   B CG2 1 
ATOM   1436 C CG2 C VAL   B 2 117 ? -11.739 -3.928  -21.638 0.31 37.76  ? 126 VAL   B CG2 1 
ATOM   1437 C CG2 D VAL   B 2 117 ? -12.468 -5.680  -22.393 0.30 38.72  ? 126 VAL   B CG2 1 
ATOM   1438 N N   . ALA   B 2 118 ? -8.106  -4.710  -23.638 1.00 39.66  ? 127 ALA   B N   1 
ATOM   1439 C CA  . ALA   B 2 118 ? -6.895  -3.892  -23.910 1.00 40.63  ? 127 ALA   B CA  1 
ATOM   1440 C C   . ALA   B 2 118 ? -7.255  -2.785  -24.888 1.00 42.24  ? 127 ALA   B C   1 
ATOM   1441 O O   . ALA   B 2 118 ? -7.085  -3.008  -26.112 1.00 42.79  ? 127 ALA   B O   1 
ATOM   1442 C CB  . ALA   B 2 118 ? -5.744  -4.742  -24.394 1.00 40.82  ? 127 ALA   B CB  1 
ATOM   1443 N N   . LEU   B 2 119 ? -7.889  -1.718  -24.391 1.00 42.46  ? 128 LEU   B N   1 
ATOM   1444 C CA  . LEU   B 2 119 ? -8.399  -0.589  -25.200 1.00 43.80  ? 128 LEU   B CA  1 
ATOM   1445 C C   . LEU   B 2 119 ? -8.045  0.698   -24.468 1.00 45.95  ? 128 LEU   B C   1 
ATOM   1446 O O   . LEU   B 2 119 ? -8.293  0.782   -23.253 1.00 47.24  ? 128 LEU   B O   1 
ATOM   1447 C CB  . LEU   B 2 119 ? -9.906  -0.750  -25.383 1.00 43.01  ? 128 LEU   B CB  1 
ATOM   1448 C CG  . LEU   B 2 119 ? -10.361 -1.988  -26.157 1.00 43.30  ? 128 LEU   B CG  1 
ATOM   1449 C CD1 . LEU   B 2 119 ? -11.878 -2.111  -26.192 1.00 42.52  ? 128 LEU   B CD1 1 
ATOM   1450 C CD2 . LEU   B 2 119 ? -9.821  -1.957  -27.584 1.00 44.30  ? 128 LEU   B CD2 1 
ATOM   1451 N N   A ASP   B 2 120 ? -7.482  1.682   -25.178 0.19 46.78  ? 129 ASP   B N   1 
ATOM   1452 N N   B ASP   B 2 120 ? -7.482  1.682   -25.178 0.20 46.78  ? 129 ASP   B N   1 
ATOM   1453 N N   C ASP   B 2 120 ? -7.460  1.655   -25.188 0.31 47.17  ? 129 ASP   B N   1 
ATOM   1454 N N   D ASP   B 2 120 ? -7.460  1.655   -25.188 0.30 47.17  ? 129 ASP   B N   1 
ATOM   1455 C CA  A ASP   B 2 120 ? -6.974  2.952   -24.586 0.19 47.10  ? 129 ASP   B CA  1 
ATOM   1456 C CA  B ASP   B 2 120 ? -6.974  2.952   -24.586 0.20 47.11  ? 129 ASP   B CA  1 
ATOM   1457 C CA  C ASP   B 2 120 ? -7.019  2.966   -24.648 0.31 47.74  ? 129 ASP   B CA  1 
ATOM   1458 C CA  D ASP   B 2 120 ? -7.018  2.966   -24.647 0.30 47.73  ? 129 ASP   B CA  1 
ATOM   1459 C C   A ASP   B 2 120 ? -8.036  4.049   -24.760 0.19 47.13  ? 129 ASP   B C   1 
ATOM   1460 C C   B ASP   B 2 120 ? -8.036  4.049   -24.760 0.20 47.13  ? 129 ASP   B C   1 
ATOM   1461 C C   C ASP   B 2 120 ? -8.163  3.972   -24.770 0.31 47.51  ? 129 ASP   B C   1 
ATOM   1462 C C   D ASP   B 2 120 ? -8.163  3.972   -24.771 0.30 47.50  ? 129 ASP   B C   1 
ATOM   1463 O O   A ASP   B 2 120 ? -8.318  4.420   -25.916 0.19 48.00  ? 129 ASP   B O   1 
ATOM   1464 O O   B ASP   B 2 120 ? -8.318  4.420   -25.916 0.20 48.00  ? 129 ASP   B O   1 
ATOM   1465 O O   C ASP   B 2 120 ? -8.635  4.196   -25.900 0.31 48.67  ? 129 ASP   B O   1 
ATOM   1466 O O   D ASP   B 2 120 ? -8.634  4.196   -25.901 0.30 48.66  ? 129 ASP   B O   1 
ATOM   1467 C CB  A ASP   B 2 120 ? -5.619  3.331   -25.202 0.19 47.82  ? 129 ASP   B CB  1 
ATOM   1468 C CB  B ASP   B 2 120 ? -5.619  3.330   -25.201 0.20 47.83  ? 129 ASP   B CB  1 
ATOM   1469 C CB  C ASP   B 2 120 ? -5.769  3.454   -25.380 0.31 48.82  ? 129 ASP   B CB  1 
ATOM   1470 C CB  D ASP   B 2 120 ? -5.769  3.455   -25.380 0.30 48.82  ? 129 ASP   B CB  1 
ATOM   1471 C CG  A ASP   B 2 120 ? -4.692  4.115   -24.281 0.19 48.01  ? 129 ASP   B CG  1 
ATOM   1472 C CG  B ASP   B 2 120 ? -4.692  4.115   -24.280 0.20 48.01  ? 129 ASP   B CG  1 
ATOM   1473 C CG  C ASP   B 2 120 ? -4.561  2.574   -25.131 0.31 49.12  ? 129 ASP   B CG  1 
ATOM   1474 C CG  D ASP   B 2 120 ? -4.560  2.575   -25.131 0.30 49.11  ? 129 ASP   B CG  1 
ATOM   1475 O OD1 A ASP   B 2 120 ? -4.803  3.955   -23.045 0.19 47.09  ? 129 ASP   B OD1 1 
ATOM   1476 O OD1 B ASP   B 2 120 ? -4.802  3.955   -23.044 0.20 47.09  ? 129 ASP   B OD1 1 
ATOM   1477 O OD1 C ASP   B 2 120 ? -4.683  1.619   -24.314 0.31 48.62  ? 129 ASP   B OD1 1 
ATOM   1478 O OD1 D ASP   B 2 120 ? -4.683  1.619   -24.315 0.30 48.62  ? 129 ASP   B OD1 1 
ATOM   1479 O OD2 A ASP   B 2 120 ? -3.850  4.875   -24.810 0.19 48.84  ? 129 ASP   B OD2 1 
ATOM   1480 O OD2 B ASP   B 2 120 ? -3.851  4.876   -24.809 0.20 48.84  ? 129 ASP   B OD2 1 
ATOM   1481 O OD2 C ASP   B 2 120 ? -3.510  2.848   -25.757 0.31 50.74  ? 129 ASP   B OD2 1 
ATOM   1482 O OD2 D ASP   B 2 120 ? -3.509  2.849   -25.755 0.30 50.73  ? 129 ASP   B OD2 1 
ATOM   1483 N N   . TYR   B 2 121 ? -8.592  4.551   -23.651 1.00 46.53  ? 130 TYR   B N   1 
ATOM   1484 C CA  . TYR   B 2 121 ? -9.600  5.640   -23.633 1.00 46.32  ? 130 TYR   B CA  1 
ATOM   1485 C C   . TYR   B 2 121 ? -9.282  6.542   -22.450 1.00 45.93  ? 130 TYR   B C   1 
ATOM   1486 O O   . TYR   B 2 121 ? -8.681  6.089   -21.472 1.00 45.42  ? 130 TYR   B O   1 
ATOM   1487 C CB  . TYR   B 2 121 ? -11.024 5.088   -23.567 1.00 46.88  ? 130 TYR   B CB  1 
ATOM   1488 C CG  . TYR   B 2 121 ? -11.572 4.568   -24.874 1.00 49.06  ? 130 TYR   B CG  1 
ATOM   1489 C CD1 . TYR   B 2 121 ? -11.930 5.447   -25.882 1.00 50.21  ? 130 TYR   B CD1 1 
ATOM   1490 C CD2 . TYR   B 2 121 ? -11.722 3.211   -25.124 1.00 49.63  ? 130 TYR   B CD2 1 
ATOM   1491 C CE1 . TYR   B 2 121 ? -12.411 4.992   -27.096 1.00 52.47  ? 130 TYR   B CE1 1 
ATOM   1492 C CE2 . TYR   B 2 121 ? -12.206 2.737   -26.336 1.00 51.38  ? 130 TYR   B CE2 1 
ATOM   1493 C CZ  . TYR   B 2 121 ? -12.552 3.636   -27.328 1.00 52.45  ? 130 TYR   B CZ  1 
ATOM   1494 O OH  . TYR   B 2 121 ? -13.053 3.255   -28.541 1.00 57.61  ? 130 TYR   B OH  1 
ATOM   1495 N N   . PRO   B 2 122 ? -9.677  7.825   -22.480 1.00 44.83  ? 131 PRO   B N   1 
ATOM   1496 C CA  . PRO   B 2 122 ? -9.349  8.728   -21.389 1.00 44.84  ? 131 PRO   B CA  1 
ATOM   1497 C C   . PRO   B 2 122 ? -10.020 8.224   -20.090 1.00 42.29  ? 131 PRO   B C   1 
ATOM   1498 O O   . PRO   B 2 122 ? -10.938 7.416   -20.147 1.00 41.21  ? 131 PRO   B O   1 
ATOM   1499 C CB  . PRO   B 2 122 ? -9.874  10.098  -21.842 1.00 45.87  ? 131 PRO   B CB  1 
ATOM   1500 C CG  . PRO   B 2 122 ? -10.261 9.940   -23.291 1.00 47.30  ? 131 PRO   B CG  1 
ATOM   1501 C CD  . PRO   B 2 122 ? -10.495 8.460   -23.516 1.00 47.11  ? 131 PRO   B CD  1 
ATOM   1502 N N   . ALA   B 2 123 ? -9.530  8.673   -18.952 1.00 41.57  ? 132 ALA   B N   1 
ATOM   1503 C CA  . ALA   B 2 123 ? -10.014 8.198   -17.629 1.00 39.85  ? 132 ALA   B CA  1 
ATOM   1504 C C   . ALA   B 2 123 ? -11.502 8.517   -17.435 1.00 38.51  ? 132 ALA   B C   1 
ATOM   1505 O O   . ALA   B 2 123 ? -12.226 7.685   -16.812 1.00 37.43  ? 132 ALA   B O   1 
ATOM   1506 C CB  . ALA   B 2 123 ? -9.134  8.738   -16.526 1.00 40.03  ? 132 ALA   B CB  1 
ATOM   1507 N N   . GLY   B 2 124 ? -11.991 9.622   -18.006 1.00 37.41  ? 133 GLY   B N   1 
ATOM   1508 C CA  . GLY   B 2 124 ? -13.421 9.981   -17.966 1.00 36.22  ? 133 GLY   B CA  1 
ATOM   1509 C C   . GLY   B 2 124 ? -14.334 8.928   -18.600 1.00 35.06  ? 133 GLY   B C   1 
ATOM   1510 O O   . GLY   B 2 124 ? -15.558 9.102   -18.405 1.00 34.85  ? 133 GLY   B O   1 
ATOM   1511 N N   . THR   B 2 125 ? -13.806 7.929   -19.344 1.00 34.45  ? 134 THR   B N   1 
ATOM   1512 C CA  . THR   B 2 125 ? -14.580 6.793   -19.949 1.00 34.41  ? 134 THR   B CA  1 
ATOM   1513 C C   . THR   B 2 125 ? -14.851 5.691   -18.909 1.00 33.96  ? 134 THR   B C   1 
ATOM   1514 O O   . THR   B 2 125 ? -15.702 4.774   -19.163 1.00 33.57  ? 134 THR   B O   1 
ATOM   1515 C CB  . THR   B 2 125 ? -13.872 6.221   -21.195 1.00 35.65  ? 134 THR   B CB  1 
ATOM   1516 O OG1 . THR   B 2 125 ? -13.508 7.320   -22.023 1.00 36.16  ? 134 THR   B OG1 1 
ATOM   1517 C CG2 . THR   B 2 125 ? -14.717 5.322   -22.068 1.00 35.63  ? 134 THR   B CG2 1 
ATOM   1518 N N   . SER   B 2 126 ? -14.182 5.780   -17.744 1.00 33.24  ? 135 SER   B N   1 
ATOM   1519 C CA  . SER   B 2 126 ? -14.391 4.813   -16.643 1.00 32.56  ? 135 SER   B CA  1 
ATOM   1520 C C   . SER   B 2 126 ? -15.909 4.616   -16.526 1.00 31.58  ? 135 SER   B C   1 
ATOM   1521 O O   . SER   B 2 126 ? -16.647 5.655   -16.430 1.00 31.93  ? 135 SER   B O   1 
ATOM   1522 C CB  . SER   B 2 126 ? -13.755 5.296   -15.388 1.00 32.68  ? 135 SER   B CB  1 
ATOM   1523 O OG  . SER   B 2 126 ? -12.375 5.063   -15.420 1.00 33.39  ? 135 SER   B OG  1 
ATOM   1524 N N   . GLY   B 2 127 ? -16.348 3.363   -16.510 1.00 30.79  ? 136 GLY   B N   1 
ATOM   1525 C CA  . GLY   B 2 127 ? -17.737 2.992   -16.182 1.00 30.50  ? 136 GLY   B CA  1 
ATOM   1526 C C   . GLY   B 2 127 ? -18.526 2.615   -17.380 1.00 30.36  ? 136 GLY   B C   1 
ATOM   1527 O O   . GLY   B 2 127 ? -19.638 2.072   -17.236 1.00 30.12  ? 136 GLY   B O   1 
ATOM   1528 N N   . SER   B 2 128 ? -17.939 2.848   -18.567 1.00 30.49  ? 137 SER   B N   1 
ATOM   1529 C CA  . SER   B 2 128 ? -18.555 2.333   -19.779 1.00 30.38  ? 137 SER   B CA  1 
ATOM   1530 C C   . SER   B 2 128 ? -18.797 0.836   -19.574 1.00 30.07  ? 137 SER   B C   1 
ATOM   1531 O O   . SER   B 2 128 ? -17.919 0.095   -19.115 1.00 30.14  ? 137 SER   B O   1 
ATOM   1532 C CB  . SER   B 2 128 ? -17.639 2.682   -20.959 1.00 30.63  ? 137 SER   B CB  1 
ATOM   1533 O OG  . SER   B 2 128 ? -17.577 4.094   -21.127 1.00 30.86  ? 137 SER   B OG  1 
ATOM   1534 N N   . PRO   B 2 129 ? -19.983 0.333   -19.931 1.00 30.30  ? 138 PRO   B N   1 
ATOM   1535 C CA  . PRO   B 2 129 ? -20.231 -1.096  -19.955 1.00 30.65  ? 138 PRO   B CA  1 
ATOM   1536 C C   . PRO   B 2 129 ? -19.603 -1.936  -21.074 1.00 31.97  ? 138 PRO   B C   1 
ATOM   1537 O O   . PRO   B 2 129 ? -19.523 -1.462  -22.203 1.00 31.97  ? 138 PRO   B O   1 
ATOM   1538 C CB  . PRO   B 2 129 ? -21.737 -1.173  -20.201 1.00 30.70  ? 138 PRO   B CB  1 
ATOM   1539 C CG  . PRO   B 2 129 ? -22.118 0.093   -20.977 1.00 30.76  ? 138 PRO   B CG  1 
ATOM   1540 C CD  . PRO   B 2 129 ? -21.096 1.113   -20.528 1.00 30.65  ? 138 PRO   B CD  1 
ATOM   1541 N N   . ILE   B 2 130 ? -19.272 -3.168  -20.709 1.00 32.89  ? 139 ILE   B N   1 
ATOM   1542 C CA  . ILE   B 2 130 ? -18.827 -4.278  -21.574 1.00 34.45  ? 139 ILE   B CA  1 
ATOM   1543 C C   . ILE   B 2 130 ? -19.996 -5.236  -21.737 1.00 35.76  ? 139 ILE   B C   1 
ATOM   1544 O O   . ILE   B 2 130 ? -20.654 -5.518  -20.774 1.00 34.51  ? 139 ILE   B O   1 
ATOM   1545 C CB  . ILE   B 2 130 ? -17.586 -4.958  -21.032 1.00 34.55  ? 139 ILE   B CB  1 
ATOM   1546 C CG1 . ILE   B 2 130 ? -16.428 -3.972  -20.915 1.00 34.88  ? 139 ILE   B CG1 1 
ATOM   1547 C CG2 . ILE   B 2 130 ? -17.241 -6.170  -21.863 1.00 35.02  ? 139 ILE   B CG2 1 
ATOM   1548 C CD1 . ILE   B 2 130 ? -15.482 -4.348  -19.832 1.00 35.09  ? 139 ILE   B CD1 1 
ATOM   1549 N N   . LEU   B 2 131 ? -20.284 -5.594  -22.994 1.00 37.70  ? 140 LEU   B N   1 
ATOM   1550 C CA  . LEU   B 2 131 ? -21.483 -6.364  -23.407 1.00 39.62  ? 140 LEU   B CA  1 
ATOM   1551 C C   . LEU   B 2 131 ? -21.115 -7.726  -23.995 1.00 40.57  ? 140 LEU   B C   1 
ATOM   1552 O O   . LEU   B 2 131 ? -20.069 -7.825  -24.679 1.00 40.39  ? 140 LEU   B O   1 
ATOM   1553 C CB  . LEU   B 2 131 ? -22.183 -5.603  -24.539 1.00 41.30  ? 140 LEU   B CB  1 
ATOM   1554 C CG  . LEU   B 2 131 ? -22.481 -4.136  -24.298 1.00 41.62  ? 140 LEU   B CG  1 
ATOM   1555 C CD1 . LEU   B 2 131 ? -23.349 -3.595  -25.427 1.00 42.70  ? 140 LEU   B CD1 1 
ATOM   1556 C CD2 . LEU   B 2 131 ? -23.161 -3.951  -22.939 1.00 41.64  ? 140 LEU   B CD2 1 
ATOM   1557 N N   . ASP   B 2 132 ? -22.044 -8.676  -23.887 1.00 41.13  ? 141 ASP   B N   1 
ATOM   1558 C CA  . ASP   B 2 132 ? -21.997 -9.962  -24.605 1.00 42.69  ? 141 ASP   B CA  1 
ATOM   1559 C C   . ASP   B 2 132 ? -22.936 -9.872  -25.802 1.00 45.02  ? 141 ASP   B C   1 
ATOM   1560 O O   . ASP   B 2 132 ? -23.645 -8.851  -25.941 1.00 43.64  ? 141 ASP   B O   1 
ATOM   1561 C CB  . ASP   B 2 132 ? -22.372 -11.156 -23.724 1.00 42.90  ? 141 ASP   B CB  1 
ATOM   1562 C CG  . ASP   B 2 132 ? -23.800 -11.223 -23.217 1.00 42.62  ? 141 ASP   B CG  1 
ATOM   1563 O OD1 . ASP   B 2 132 ? -24.618 -10.351 -23.514 1.00 41.94  ? 141 ASP   B OD1 1 
ATOM   1564 O OD2 . ASP   B 2 132 ? -24.048 -12.163 -22.439 1.00 44.46  ? 141 ASP   B OD2 1 
ATOM   1565 N N   . LYS   B 2 133 ? -22.980 -10.964 -26.556 1.00 47.88  ? 142 LYS   B N   1 
ATOM   1566 C CA  . LYS   B 2 133 ? -23.553 -11.018 -27.922 1.00 51.84  ? 142 LYS   B CA  1 
ATOM   1567 C C   . LYS   B 2 133 ? -25.052 -10.759 -27.809 1.00 51.69  ? 142 LYS   B C   1 
ATOM   1568 O O   . LYS   B 2 133 ? -25.650 -10.382 -28.839 1.00 49.57  ? 142 LYS   B O   1 
ATOM   1569 C CB  . LYS   B 2 133 ? -23.186 -12.361 -28.573 1.00 54.89  ? 142 LYS   B CB  1 
ATOM   1570 C CG  . LYS   B 2 133 ? -21.818 -12.345 -29.252 1.00 59.44  ? 142 LYS   B CG  1 
ATOM   1571 C CD  . LYS   B 2 133 ? -21.073 -13.685 -29.330 1.00 62.21  ? 142 LYS   B CD  1 
ATOM   1572 C CE  . LYS   B 2 133 ? -19.818 -13.598 -30.186 1.00 63.53  ? 142 LYS   B CE  1 
ATOM   1573 N NZ  . LYS   B 2 133 ? -19.148 -14.912 -30.377 1.00 65.02  ? 142 LYS   B NZ  1 
ATOM   1574 N N   . CYS   B 2 134 ? -25.602 -10.920 -26.595 1.00 49.92  ? 143 CYS   B N   1 
ATOM   1575 C CA  . CYS   B 2 134 ? -27.044 -10.774 -26.315 1.00 50.07  ? 143 CYS   B CA  1 
ATOM   1576 C C   . CYS   B 2 134 ? -27.338 -9.388  -25.731 1.00 46.56  ? 143 CYS   B C   1 
ATOM   1577 O O   . CYS   B 2 134 ? -28.481 -9.116  -25.440 1.00 45.34  ? 143 CYS   B O   1 
ATOM   1578 C CB  . CYS   B 2 134 ? -27.510 -11.867 -25.372 1.00 52.97  ? 143 CYS   B CB  1 
ATOM   1579 S SG  . CYS   B 2 134 ? -27.719 -13.440 -26.234 1.00 58.89  ? 143 CYS   B SG  1 
ATOM   1580 N N   . GLY   B 2 135 ? -26.349 -8.502  -25.696 1.00 44.81  ? 144 GLY   B N   1 
ATOM   1581 C CA  . GLY   B 2 135 ? -26.521 -7.122  -25.211 1.00 43.31  ? 144 GLY   B CA  1 
ATOM   1582 C C   . GLY   B 2 135 ? -26.556 -7.077  -23.679 1.00 41.65  ? 144 GLY   B C   1 
ATOM   1583 O O   . GLY   B 2 135 ? -27.041 -6.099  -23.136 1.00 41.39  ? 144 GLY   B O   1 
ATOM   1584 N N   . ARG   B 2 136 ? -26.103 -8.128  -23.006 1.00 40.83  ? 145 ARG   B N   1 
ATOM   1585 C CA  . ARG   B 2 136 ? -26.080 -8.147  -21.509 1.00 40.46  ? 145 ARG   B CA  1 
ATOM   1586 C C   . ARG   B 2 136 ? -24.798 -7.488  -21.026 1.00 38.22  ? 145 ARG   B C   1 
ATOM   1587 O O   . ARG   B 2 136 ? -23.729 -7.800  -21.627 1.00 36.87  ? 145 ARG   B O   1 
ATOM   1588 C CB  . ARG   B 2 136 ? -26.296 -9.575  -21.040 1.00 42.28  ? 145 ARG   B CB  1 
ATOM   1589 C CG  . ARG   B 2 136 ? -27.780 -9.895  -21.004 1.00 45.15  ? 145 ARG   B CG  1 
ATOM   1590 C CD  . ARG   B 2 136 ? -28.034 -11.302 -20.557 1.00 48.26  ? 145 ARG   B CD  1 
ATOM   1591 N NE  . ARG   B 2 136 ? -27.228 -12.165 -21.378 1.00 52.26  ? 145 ARG   B NE  1 
ATOM   1592 C CZ  . ARG   B 2 136 ? -26.723 -13.334 -21.026 1.00 55.19  ? 145 ARG   B CZ  1 
ATOM   1593 N NH1 . ARG   B 2 136 ? -26.896 -13.827 -19.802 1.00 58.45  ? 145 ARG   B NH1 1 
ATOM   1594 N NH2 . ARG   B 2 136 ? -26.016 -13.995 -21.926 1.00 57.58  ? 145 ARG   B NH2 1 
ATOM   1595 N N   . VAL   B 2 137 ? -24.883 -6.698  -19.927 1.00 36.82  ? 146 VAL   B N   1 
ATOM   1596 C CA  . VAL   B 2 137 ? -23.682 -6.032  -19.331 1.00 36.04  ? 146 VAL   B CA  1 
ATOM   1597 C C   . VAL   B 2 137 ? -22.945 -7.103  -18.513 1.00 36.19  ? 146 VAL   B C   1 
ATOM   1598 O O   . VAL   B 2 137 ? -23.496 -7.582  -17.470 1.00 35.58  ? 146 VAL   B O   1 
ATOM   1599 C CB  . VAL   B 2 137 ? -23.978 -4.752  -18.525 1.00 35.36  ? 146 VAL   B CB  1 
ATOM   1600 C CG1 . VAL   B 2 137 ? -22.695 -4.131  -17.977 1.00 35.09  ? 146 VAL   B CG1 1 
ATOM   1601 C CG2 . VAL   B 2 137 ? -24.715 -3.698  -19.349 1.00 35.78  ? 146 VAL   B CG2 1 
ATOM   1602 N N   . ILE   B 2 138 ? -21.732 -7.443  -18.932 1.00 35.75  ? 147 ILE   B N   1 
ATOM   1603 C CA  . ILE   B 2 138 ? -20.877 -8.464  -18.245 1.00 36.00  ? 147 ILE   B CA  1 
ATOM   1604 C C   . ILE   B 2 138 ? -19.891 -7.758  -17.296 1.00 34.96  ? 147 ILE   B C   1 
ATOM   1605 O O   . ILE   B 2 138 ? -19.155 -8.453  -16.523 1.00 35.16  ? 147 ILE   B O   1 
ATOM   1606 C CB  . ILE   B 2 138 ? -20.203 -9.375  -19.301 1.00 36.66  ? 147 ILE   B CB  1 
ATOM   1607 C CG1 . ILE   B 2 138 ? -19.405 -8.604  -20.352 1.00 36.26  ? 147 ILE   B CG1 1 
ATOM   1608 C CG2 . ILE   B 2 138 ? -21.222 -10.300 -19.955 1.00 36.75  ? 147 ILE   B CG2 1 
ATOM   1609 C CD1 . ILE   B 2 138 ? -18.366 -9.452  -21.056 1.00 37.60  ? 147 ILE   B CD1 1 
ATOM   1610 N N   . GLY   B 2 139 ? -19.889 -6.430  -17.309 1.00 34.21  ? 148 GLY   B N   1 
ATOM   1611 C CA  . GLY   B 2 139 ? -19.060 -5.652  -16.387 1.00 33.55  ? 148 GLY   B CA  1 
ATOM   1612 C C   . GLY   B 2 139 ? -18.788 -4.273  -16.896 1.00 33.36  ? 148 GLY   B C   1 
ATOM   1613 O O   . GLY   B 2 139 ? -19.297 -3.893  -18.009 1.00 33.74  ? 148 GLY   B O   1 
ATOM   1614 N N   A LEU   B 2 140 ? -18.007 -3.520  -16.123 0.19 33.00  ? 149 LEU   B N   1 
ATOM   1615 N N   B LEU   B 2 140 ? -18.005 -3.521  -16.124 0.20 33.00  ? 149 LEU   B N   1 
ATOM   1616 N N   C LEU   B 2 140 ? -17.964 -3.530  -16.164 0.31 33.19  ? 149 LEU   B N   1 
ATOM   1617 N N   D LEU   B 2 140 ? -17.966 -3.529  -16.162 0.30 33.19  ? 149 LEU   B N   1 
ATOM   1618 C CA  A LEU   B 2 140 ? -17.663 -2.100  -16.371 0.19 32.88  ? 149 LEU   B CA  1 
ATOM   1619 C CA  B LEU   B 2 140 ? -17.662 -2.100  -16.372 0.20 32.88  ? 149 LEU   B CA  1 
ATOM   1620 C CA  C LEU   B 2 140 ? -17.646 -2.107  -16.430 0.31 33.21  ? 149 LEU   B CA  1 
ATOM   1621 C CA  D LEU   B 2 140 ? -17.647 -2.107  -16.429 0.30 33.21  ? 149 LEU   B CA  1 
ATOM   1622 C C   A LEU   B 2 140 ? -16.168 -2.068  -16.783 0.19 33.05  ? 149 LEU   B C   1 
ATOM   1623 C C   B LEU   B 2 140 ? -16.167 -2.066  -16.785 0.20 33.05  ? 149 LEU   B C   1 
ATOM   1624 C C   C LEU   B 2 140 ? -16.139 -2.057  -16.843 0.31 33.52  ? 149 LEU   B C   1 
ATOM   1625 C C   D LEU   B 2 140 ? -16.140 -2.057  -16.842 0.30 33.52  ? 149 LEU   B C   1 
ATOM   1626 O O   A LEU   B 2 140 ? -15.296 -2.959  -16.178 0.19 32.94  ? 149 LEU   B O   1 
ATOM   1627 O O   B LEU   B 2 140 ? -15.292 -2.957  -16.175 0.20 32.94  ? 149 LEU   B O   1 
ATOM   1628 O O   C LEU   B 2 140 ? -15.239 -3.041  -16.132 0.31 33.48  ? 149 LEU   B O   1 
ATOM   1629 O O   D LEU   B 2 140 ? -15.242 -3.040  -16.135 0.30 33.48  ? 149 LEU   B O   1 
ATOM   1630 C CB  A LEU   B 2 140 ? -18.024 -1.254  -15.131 0.19 32.48  ? 149 LEU   B CB  1 
ATOM   1631 C CB  B LEU   B 2 140 ? -18.023 -1.254  -15.132 0.20 32.48  ? 149 LEU   B CB  1 
ATOM   1632 C CB  C LEU   B 2 140 ? -18.049 -1.250  -15.206 0.31 32.77  ? 149 LEU   B CB  1 
ATOM   1633 C CB  D LEU   B 2 140 ? -18.049 -1.249  -15.205 0.30 32.77  ? 149 LEU   B CB  1 
ATOM   1634 C CG  A LEU   B 2 140 ? -19.512 -1.241  -14.743 0.19 32.27  ? 149 LEU   B CG  1 
ATOM   1635 C CG  B LEU   B 2 140 ? -19.511 -1.242  -14.744 0.20 32.27  ? 149 LEU   B CG  1 
ATOM   1636 C CG  C LEU   B 2 140 ? -19.546 -1.256  -14.842 0.31 32.54  ? 149 LEU   B CG  1 
ATOM   1637 C CG  D LEU   B 2 140 ? -19.546 -1.256  -14.841 0.30 32.54  ? 149 LEU   B CG  1 
ATOM   1638 C CD1 A LEU   B 2 140 ? -19.820 -0.149  -13.720 0.19 32.12  ? 149 LEU   B CD1 1 
ATOM   1639 C CD1 B LEU   B 2 140 ? -19.819 -0.149  -13.720 0.20 32.12  ? 149 LEU   B CD1 1 
ATOM   1640 C CD1 C LEU   B 2 140 ? -19.887 -0.171  -13.819 0.31 32.40  ? 149 LEU   B CD1 1 
ATOM   1641 C CD1 D LEU   B 2 140 ? -19.887 -0.171  -13.818 0.30 32.40  ? 149 LEU   B CD1 1 
ATOM   1642 C CD2 A LEU   B 2 140 ? -20.417 -1.080  -15.955 0.19 32.42  ? 149 LEU   B CD2 1 
ATOM   1643 C CD2 B LEU   B 2 140 ? -20.417 -1.081  -15.956 0.20 32.42  ? 149 LEU   B CD2 1 
ATOM   1644 C CD2 C LEU   B 2 140 ? -20.439 -1.103  -16.061 0.31 32.70  ? 149 LEU   B CD2 1 
ATOM   1645 C CD2 D LEU   B 2 140 ? -20.439 -1.103  -16.061 0.30 32.71  ? 149 LEU   B CD2 1 
ATOM   1646 N N   A TYR   B 2 141 ? -15.890 -0.998  -17.647 0.19 33.33  ? 150 TYR   B N   1 
ATOM   1647 N N   B TYR   B 2 141 ? -15.891 -0.998  -17.651 0.20 33.33  ? 150 TYR   B N   1 
ATOM   1648 N N   C TYR   B 2 141 ? -15.849 -0.837  -17.531 0.31 33.92  ? 150 TYR   B N   1 
ATOM   1649 N N   D TYR   B 2 141 ? -15.848 -0.838  -17.529 0.30 33.92  ? 150 TYR   B N   1 
ATOM   1650 C CA  A TYR   B 2 141 ? -14.514 -0.764  -18.160 0.19 33.69  ? 150 TYR   B CA  1 
ATOM   1651 C CA  B TYR   B 2 141 ? -14.515 -0.765  -18.163 0.20 33.69  ? 150 TYR   B CA  1 
ATOM   1652 C CA  C TYR   B 2 141 ? -14.470 -0.576  -18.018 0.31 34.42  ? 150 TYR   B CA  1 
ATOM   1653 C CA  D TYR   B 2 141 ? -14.470 -0.576  -18.016 0.30 34.42  ? 150 TYR   B CA  1 
ATOM   1654 C C   A TYR   B 2 141 ? -13.918 0.474   -17.478 0.19 33.70  ? 150 TYR   B C   1 
ATOM   1655 C C   B TYR   B 2 141 ? -13.920 0.473   -17.480 0.20 33.70  ? 150 TYR   B C   1 
ATOM   1656 C C   C TYR   B 2 141 ? -13.893 0.628   -17.263 0.31 34.56  ? 150 TYR   B C   1 
ATOM   1657 C C   D TYR   B 2 141 ? -13.894 0.628   -17.261 0.30 34.56  ? 150 TYR   B C   1 
ATOM   1658 O O   A TYR   B 2 141 ? -14.585 1.687   -17.328 0.19 33.90  ? 150 TYR   B O   1 
ATOM   1659 O O   B TYR   B 2 141 ? -14.588 1.687   -17.326 0.20 33.90  ? 150 TYR   B O   1 
ATOM   1660 O O   C TYR   B 2 141 ? -14.650 1.702   -17.027 0.31 35.17  ? 150 TYR   B O   1 
ATOM   1661 O O   D TYR   B 2 141 ? -14.651 1.702   -17.029 0.30 35.16  ? 150 TYR   B O   1 
ATOM   1662 C CB  A TYR   B 2 141 ? -14.539 -0.434  -19.658 0.19 34.26  ? 150 TYR   B CB  1 
ATOM   1663 C CB  B TYR   B 2 141 ? -14.539 -0.435  -19.661 0.20 34.26  ? 150 TYR   B CB  1 
ATOM   1664 C CB  C TYR   B 2 141 ? -14.499 -0.257  -19.519 0.31 35.21  ? 150 TYR   B CB  1 
ATOM   1665 C CB  D TYR   B 2 141 ? -14.498 -0.258  -19.518 0.30 35.21  ? 150 TYR   B CB  1 
ATOM   1666 C CG  A TYR   B 2 141 ? -13.299 0.260   -20.165 0.19 34.72  ? 150 TYR   B CG  1 
ATOM   1667 C CG  B TYR   B 2 141 ? -13.299 0.259   -20.167 0.20 34.72  ? 150 TYR   B CG  1 
ATOM   1668 C CG  C TYR   B 2 141 ? -13.234 0.376   -20.034 0.31 35.77  ? 150 TYR   B CG  1 
ATOM   1669 C CG  D TYR   B 2 141 ? -13.233 0.375   -20.033 0.30 35.77  ? 150 TYR   B CG  1 
ATOM   1670 C CD1 A TYR   B 2 141 ? -13.156 1.639   -20.090 0.19 34.98  ? 150 TYR   B CD1 1 
ATOM   1671 C CD1 B TYR   B 2 141 ? -13.156 1.638   -20.091 0.20 34.98  ? 150 TYR   B CD1 1 
ATOM   1672 C CD1 C TYR   B 2 141 ? -13.030 1.745   -19.951 0.31 36.13  ? 150 TYR   B CD1 1 
ATOM   1673 C CD1 D TYR   B 2 141 ? -13.030 1.744   -19.950 0.30 36.13  ? 150 TYR   B CD1 1 
ATOM   1674 C CD2 A TYR   B 2 141 ? -12.260 -0.471  -20.720 0.19 35.09  ? 150 TYR   B CD2 1 
ATOM   1675 C CD2 B TYR   B 2 141 ? -12.260 -0.472  -20.723 0.20 35.09  ? 150 TYR   B CD2 1 
ATOM   1676 C CD2 C TYR   B 2 141 ? -12.226 -0.403  -20.585 0.31 36.29  ? 150 TYR   B CD2 1 
ATOM   1677 C CD2 D TYR   B 2 141 ? -12.225 -0.404  -20.585 0.30 36.28  ? 150 TYR   B CD2 1 
ATOM   1678 C CE1 A TYR   B 2 141 ? -12.010 2.270   -20.554 0.19 35.51  ? 150 TYR   B CE1 1 
ATOM   1679 C CE1 B TYR   B 2 141 ? -12.010 2.269   -20.554 0.20 35.51  ? 150 TYR   B CE1 1 
ATOM   1680 C CE1 C TYR   B 2 141 ? -11.855 2.325   -20.408 0.31 36.83  ? 150 TYR   B CE1 1 
ATOM   1681 C CE1 D TYR   B 2 141 ? -11.856 2.324   -20.408 0.30 36.82  ? 150 TYR   B CE1 1 
ATOM   1682 C CE2 A TYR   B 2 141 ? -11.111 0.143   -21.190 0.19 35.42  ? 150 TYR   B CE2 1 
ATOM   1683 C CE2 B TYR   B 2 141 ? -11.110 0.143   -21.192 0.20 35.42  ? 150 TYR   B CE2 1 
ATOM   1684 C CE2 C TYR   B 2 141 ? -11.050 0.160   -21.053 0.31 36.64  ? 150 TYR   B CE2 1 
ATOM   1685 C CE2 D TYR   B 2 141 ? -11.050 0.160   -21.053 0.30 36.63  ? 150 TYR   B CE2 1 
ATOM   1686 C CZ  A TYR   B 2 141 ? -10.986 1.520   -21.113 0.19 35.74  ? 150 TYR   B CZ  1 
ATOM   1687 C CZ  B TYR   B 2 141 ? -10.986 1.519   -21.114 0.20 35.74  ? 150 TYR   B CZ  1 
ATOM   1688 C CZ  C TYR   B 2 141 ? -10.863 1.529   -20.970 0.31 37.10  ? 150 TYR   B CZ  1 
ATOM   1689 C CZ  D TYR   B 2 141 ? -10.864 1.529   -20.970 0.30 37.09  ? 150 TYR   B CZ  1 
ATOM   1690 O OH  A TYR   B 2 141 ? -9.850  2.127   -21.583 0.19 36.53  ? 150 TYR   B OH  1 
ATOM   1691 O OH  B TYR   B 2 141 ? -9.850  2.127   -21.583 0.20 36.54  ? 150 TYR   B OH  1 
ATOM   1692 O OH  C TYR   B 2 141 ? -9.690  2.071   -21.439 0.31 38.17  ? 150 TYR   B OH  1 
ATOM   1693 O OH  D TYR   B 2 141 ? -9.691  2.072   -21.440 0.30 38.16  ? 150 TYR   B OH  1 
ATOM   1694 N N   A GLY   B 2 142 ? -12.702 0.263   -16.869 0.19 33.81  ? 151 GLY   B N   1 
ATOM   1695 N N   B GLY   B 2 142 ? -12.704 0.261   -16.869 0.20 33.81  ? 151 GLY   B N   1 
ATOM   1696 N N   C GLY   B 2 142 ? -12.620 0.520   -16.809 0.31 34.67  ? 151 GLY   B N   1 
ATOM   1697 N N   D GLY   B 2 142 ? -12.620 0.520   -16.807 0.30 34.67  ? 151 GLY   B N   1 
ATOM   1698 C CA  A GLY   B 2 142 ? -11.908 1.427   -16.414 0.19 34.22  ? 151 GLY   B CA  1 
ATOM   1699 C CA  B GLY   B 2 142 ? -11.910 1.426   -16.417 0.20 34.21  ? 151 GLY   B CA  1 
ATOM   1700 C CA  C GLY   B 2 142 ? -11.980 1.681   -16.152 0.31 35.07  ? 151 GLY   B CA  1 
ATOM   1701 C CA  D GLY   B 2 142 ? -11.979 1.681   -16.150 0.30 35.07  ? 151 GLY   B CA  1 
ATOM   1702 C C   A GLY   B 2 142 ? -11.293 1.277   -15.033 0.19 34.24  ? 151 GLY   B C   1 
ATOM   1703 C C   B GLY   B 2 142 ? -11.294 1.278   -15.036 0.20 34.24  ? 151 GLY   B C   1 
ATOM   1704 C C   C GLY   B 2 142 ? -11.059 1.320   -14.991 0.31 35.06  ? 151 GLY   B C   1 
ATOM   1705 C C   D GLY   B 2 142 ? -11.059 1.319   -14.990 0.30 35.06  ? 151 GLY   B C   1 
ATOM   1706 O O   A GLY   B 2 142 ? -10.752 2.345   -14.541 0.19 34.39  ? 151 GLY   B O   1 
ATOM   1707 O O   B GLY   B 2 142 ? -10.751 2.348   -14.546 0.20 34.39  ? 151 GLY   B O   1 
ATOM   1708 O O   C GLY   B 2 142 ? -10.076 2.217   -14.656 0.31 35.48  ? 151 GLY   B O   1 
ATOM   1709 O O   D GLY   B 2 142 ? -10.074 2.215   -14.659 0.30 35.48  ? 151 GLY   B O   1 
ATOM   1710 N N   A ASN   B 2 143 ? -11.331 0.013   -14.481 0.19 34.47  ? 152 ASN   B N   1 
ATOM   1711 N N   B ASN   B 2 143 ? -11.333 0.014   -14.482 0.20 34.47  ? 152 ASN   B N   1 
ATOM   1712 N N   C ASN   B 2 143 ? -11.306 0.061   -14.423 0.31 35.21  ? 152 ASN   B N   1 
ATOM   1713 N N   D ASN   B 2 143 ? -11.305 0.061   -14.422 0.30 35.21  ? 152 ASN   B N   1 
ATOM   1714 C CA  A ASN   B 2 143 ? -10.289 -0.420  -13.467 0.19 34.80  ? 152 ASN   B CA  1 
ATOM   1715 C CA  B ASN   B 2 143 ? -10.289 -0.420  -13.469 0.20 34.80  ? 152 ASN   B CA  1 
ATOM   1716 C CA  C ASN   B 2 143 ? -10.276 -0.473  -13.432 0.31 35.49  ? 152 ASN   B CA  1 
ATOM   1717 C CA  D ASN   B 2 143 ? -10.275 -0.473  -13.430 0.30 35.49  ? 152 ASN   B CA  1 
ATOM   1718 C C   A ASN   B 2 143 ? -9.418  -1.601  -14.031 0.19 35.12  ? 152 ASN   B C   1 
ATOM   1719 C C   B ASN   B 2 143 ? -9.420  -1.602  -14.028 0.20 35.12  ? 152 ASN   B C   1 
ATOM   1720 C C   C ASN   B 2 143 ? -9.438  -1.668  -13.963 0.31 35.53  ? 152 ASN   B C   1 
ATOM   1721 C C   D ASN   B 2 143 ? -9.437  -1.666  -13.966 0.30 35.53  ? 152 ASN   B C   1 
ATOM   1722 O O   A ASN   B 2 143 ? -9.967  -2.561  -14.365 0.19 35.21  ? 152 ASN   B O   1 
ATOM   1723 O O   B ASN   B 2 143 ? -9.969  -2.559  -14.365 0.20 35.21  ? 152 ASN   B O   1 
ATOM   1724 O O   C ASN   B 2 143 ? -9.976  -2.634  -14.288 0.31 35.82  ? 152 ASN   B O   1 
ATOM   1725 O O   D ASN   B 2 143 ? -9.977  -2.633  -14.288 0.30 35.81  ? 152 ASN   B O   1 
ATOM   1726 C CB  A ASN   B 2 143 ? -10.909 -0.788  -12.100 0.19 34.61  ? 152 ASN   B CB  1 
ATOM   1727 C CB  B ASN   B 2 143 ? -10.908 -0.791  -12.102 0.20 34.61  ? 152 ASN   B CB  1 
ATOM   1728 C CB  C ASN   B 2 143 ? -10.912 -0.873  -12.084 0.31 35.40  ? 152 ASN   B CB  1 
ATOM   1729 C CB  D ASN   B 2 143 ? -10.912 -0.871  -12.083 0.30 35.39  ? 152 ASN   B CB  1 
ATOM   1730 C CG  A ASN   B 2 143 ? -9.870  -0.830  -10.995 0.19 34.78  ? 152 ASN   B CG  1 
ATOM   1731 C CG  B ASN   B 2 143 ? -9.869  -0.830  -10.998 0.20 34.78  ? 152 ASN   B CG  1 
ATOM   1732 C CG  C ASN   B 2 143 ? -9.906  -0.827  -10.948 0.31 35.74  ? 152 ASN   B CG  1 
ATOM   1733 C CG  D ASN   B 2 143 ? -9.906  -0.827  -10.946 0.30 35.74  ? 152 ASN   B CG  1 
ATOM   1734 O OD1 A ASN   B 2 143 ? -8.786  -0.256  -11.159 0.19 35.14  ? 152 ASN   B OD1 1 
ATOM   1735 O OD1 B ASN   B 2 143 ? -8.784  -0.256  -11.163 0.20 35.14  ? 152 ASN   B OD1 1 
ATOM   1736 O OD1 C ASN   B 2 143 ? -8.908  -0.098  -11.043 0.31 36.36  ? 152 ASN   B OD1 1 
ATOM   1737 O OD1 D ASN   B 2 143 ? -8.909  -0.098  -11.040 0.30 36.35  ? 152 ASN   B OD1 1 
ATOM   1738 N ND2 A ASN   B 2 143 ? -10.179 -1.515  -9.889  0.19 34.51  ? 152 ASN   B ND2 1 
ATOM   1739 N ND2 B ASN   B 2 143 ? -10.177 -1.514  -9.889  0.20 34.51  ? 152 ASN   B ND2 1 
ATOM   1740 N ND2 C ASN   B 2 143 ? -10.149 -1.610  -9.892  0.31 35.35  ? 152 ASN   B ND2 1 
ATOM   1741 N ND2 D ASN   B 2 143 ? -10.150 -1.610  -9.891  0.30 35.35  ? 152 ASN   B ND2 1 
ATOM   1742 N N   . GLY   B 2 144 ? -7.916  -1.096  -13.932 1.00 35.51  ? 153 GLY   B N   1 
ATOM   1743 C CA  . GLY   B 2 144 ? -6.903  -2.085  -14.297 1.00 36.66  ? 153 GLY   B CA  1 
ATOM   1744 C C   . GLY   B 2 144 ? -5.516  -1.530  -14.156 1.00 38.80  ? 153 GLY   B C   1 
ATOM   1745 O O   . GLY   B 2 144 ? -5.196  -0.953  -13.084 1.00 40.11  ? 153 GLY   B O   1 
ATOM   1746 N N   . VAL   B 2 145 ? -4.701  -1.737  -15.190 1.00 41.76  ? 154 VAL   B N   1 
ATOM   1747 C CA  . VAL   B 2 145 ? -3.234  -1.637  -15.083 1.00 44.51  ? 154 VAL   B CA  1 
ATOM   1748 C C   . VAL   B 2 145 ? -2.649  -1.023  -16.361 1.00 48.13  ? 154 VAL   B C   1 
ATOM   1749 O O   . VAL   B 2 145 ? -3.182  -1.269  -17.453 1.00 46.15  ? 154 VAL   B O   1 
ATOM   1750 C CB  . VAL   B 2 145 ? -2.761  -3.067  -14.784 1.00 45.51  ? 154 VAL   B CB  1 
ATOM   1751 C CG1 . VAL   B 2 145 ? -2.245  -3.818  -15.985 1.00 44.57  ? 154 VAL   B CG1 1 
ATOM   1752 C CG2 . VAL   B 2 145 ? -1.809  -3.113  -13.611 1.00 46.34  ? 154 VAL   B CG2 1 
ATOM   1753 N N   A VAL   B 2 146 ? -1.534  -0.302  -16.210 0.19 48.52  ? 155 VAL   B N   1 
ATOM   1754 N N   B VAL   B 2 146 ? -1.533  -0.302  -16.209 0.20 48.52  ? 155 VAL   B N   1 
ATOM   1755 N N   C VAL   B 2 146 ? -1.640  -0.162  -16.191 0.31 49.39  ? 155 VAL   B N   1 
ATOM   1756 N N   D VAL   B 2 146 ? -1.640  -0.162  -16.191 0.30 49.39  ? 155 VAL   B N   1 
ATOM   1757 C CA  A VAL   B 2 146 ? -0.604  0.100   -17.309 0.19 49.87  ? 155 VAL   B CA  1 
ATOM   1758 C CA  B VAL   B 2 146 ? -0.604  0.100   -17.308 0.20 49.87  ? 155 VAL   B CA  1 
ATOM   1759 C CA  C VAL   B 2 146 ? -0.869  0.493   -17.288 0.31 51.49  ? 155 VAL   B CA  1 
ATOM   1760 C CA  D VAL   B 2 146 ? -0.869  0.493   -17.288 0.30 51.48  ? 155 VAL   B CA  1 
ATOM   1761 C C   A VAL   B 2 146 ? 0.369   -1.063  -17.550 0.19 50.45  ? 155 VAL   B C   1 
ATOM   1762 C C   B VAL   B 2 146 ? 0.369   -1.063  -17.550 0.20 50.44  ? 155 VAL   B C   1 
ATOM   1763 C C   C VAL   B 2 146 ? 0.346   -0.386  -17.585 0.31 52.75  ? 155 VAL   B C   1 
ATOM   1764 C C   D VAL   B 2 146 ? 0.346   -0.386  -17.585 0.30 52.75  ? 155 VAL   B C   1 
ATOM   1765 O O   A VAL   B 2 146 ? 0.701   -1.761  -16.573 0.19 50.52  ? 155 VAL   B O   1 
ATOM   1766 O O   B VAL   B 2 146 ? 0.702   -1.762  -16.573 0.20 50.52  ? 155 VAL   B O   1 
ATOM   1767 O O   C VAL   B 2 146 ? 1.120   -0.647  -16.653 0.31 53.12  ? 155 VAL   B O   1 
ATOM   1768 O O   D VAL   B 2 146 ? 1.121   -0.647  -16.652 0.30 53.12  ? 155 VAL   B O   1 
ATOM   1769 C CB  A VAL   B 2 146 ? 0.128   1.408   -16.952 0.19 50.32  ? 155 VAL   B CB  1 
ATOM   1770 C CB  B VAL   B 2 146 ? 0.128   1.408   -16.952 0.20 50.32  ? 155 VAL   B CB  1 
ATOM   1771 C CB  C VAL   B 2 146 ? -0.455  1.927   -16.908 0.31 51.87  ? 155 VAL   B CB  1 
ATOM   1772 C CB  D VAL   B 2 146 ? -0.454  1.927   -16.908 0.30 51.87  ? 155 VAL   B CB  1 
ATOM   1773 C CG1 A VAL   B 2 146 ? 1.220   1.745   -17.954 0.19 51.21  ? 155 VAL   B CG1 1 
ATOM   1774 C CG1 B VAL   B 2 146 ? 1.220   1.744   -17.953 0.20 51.21  ? 155 VAL   B CG1 1 
ATOM   1775 C CG1 C VAL   B 2 146 ? 0.597   2.489   -17.847 0.31 52.79  ? 155 VAL   B CG1 1 
ATOM   1776 C CG1 D VAL   B 2 146 ? 0.598   2.489   -17.847 0.30 52.78  ? 155 VAL   B CG1 1 
ATOM   1777 C CG2 A VAL   B 2 146 ? -0.845  2.568   -16.814 0.19 50.45  ? 155 VAL   B CG2 1 
ATOM   1778 C CG2 B VAL   B 2 146 ? -0.845  2.568   -16.814 0.20 50.45  ? 155 VAL   B CG2 1 
ATOM   1779 C CG2 C VAL   B 2 146 ? -1.655  2.856   -16.851 0.31 51.92  ? 155 VAL   B CG2 1 
ATOM   1780 C CG2 D VAL   B 2 146 ? -1.655  2.856   -16.851 0.30 51.92  ? 155 VAL   B CG2 1 
ATOM   1781 N N   A ILE   B 2 147 ? 0.809   -1.272  -18.797 0.19 51.51  ? 156 ILE   B N   1 
ATOM   1782 N N   B ILE   B 2 147 ? 0.809   -1.271  -18.797 0.20 51.52  ? 156 ILE   B N   1 
ATOM   1783 N N   C ILE   B 2 147 ? 0.500   -0.819  -18.836 0.31 54.74  ? 156 ILE   B N   1 
ATOM   1784 N N   D ILE   B 2 147 ? 0.500   -0.819  -18.836 0.30 54.74  ? 156 ILE   B N   1 
ATOM   1785 C CA  A ILE   B 2 147 ? 1.627   -2.461  -19.192 0.19 52.01  ? 156 ILE   B CA  1 
ATOM   1786 C CA  B ILE   B 2 147 ? 1.627   -2.461  -19.191 0.20 52.01  ? 156 ILE   B CA  1 
ATOM   1787 C CA  C ILE   B 2 147 ? 1.565   -1.779  -19.252 0.31 56.27  ? 156 ILE   B CA  1 
ATOM   1788 C CA  D ILE   B 2 147 ? 1.565   -1.779  -19.252 0.30 56.27  ? 156 ILE   B CA  1 
ATOM   1789 C C   A ILE   B 2 147 ? 2.963   -2.009  -19.795 0.19 52.90  ? 156 ILE   B C   1 
ATOM   1790 C C   B ILE   B 2 147 ? 2.963   -2.009  -19.795 0.20 52.89  ? 156 ILE   B C   1 
ATOM   1791 C C   C ILE   B 2 147 ? 2.789   -0.979  -19.718 0.31 58.37  ? 156 ILE   B C   1 
ATOM   1792 C C   D ILE   B 2 147 ? 2.788   -0.979  -19.719 0.30 58.38  ? 156 ILE   B C   1 
ATOM   1793 O O   A ILE   B 2 147 ? 3.084   -0.822  -20.141 0.19 52.77  ? 156 ILE   B O   1 
ATOM   1794 O O   B ILE   B 2 147 ? 3.084   -0.822  -20.141 0.20 52.76  ? 156 ILE   B O   1 
ATOM   1795 O O   C ILE   B 2 147 ? 2.811   0.251   -19.491 0.31 59.00  ? 156 ILE   B O   1 
ATOM   1796 O O   D ILE   B 2 147 ? 2.809   0.251   -19.495 0.30 59.00  ? 156 ILE   B O   1 
ATOM   1797 C CB  A ILE   B 2 147 ? 0.831   -3.387  -20.135 0.19 52.24  ? 156 ILE   B CB  1 
ATOM   1798 C CB  B ILE   B 2 147 ? 0.831   -3.386  -20.135 0.20 52.24  ? 156 ILE   B CB  1 
ATOM   1799 C CB  C ILE   B 2 147 ? 1.021   -2.778  -20.296 0.31 56.54  ? 156 ILE   B CB  1 
ATOM   1800 C CB  D ILE   B 2 147 ? 1.021   -2.778  -20.296 0.30 56.54  ? 156 ILE   B CB  1 
ATOM   1801 C CG1 A ILE   B 2 147 ? 0.344   -2.671  -21.400 0.19 52.71  ? 156 ILE   B CG1 1 
ATOM   1802 C CG1 B ILE   B 2 147 ? 0.345   -2.672  -21.400 0.20 52.70  ? 156 ILE   B CG1 1 
ATOM   1803 C CG1 C ILE   B 2 147 ? 0.416   -2.091  -21.528 0.31 56.97  ? 156 ILE   B CG1 1 
ATOM   1804 C CG1 D ILE   B 2 147 ? 0.417   -2.091  -21.528 0.30 56.97  ? 156 ILE   B CG1 1 
ATOM   1805 C CG2 A ILE   B 2 147 ? -0.322  -4.036  -19.384 0.19 51.74  ? 156 ILE   B CG2 1 
ATOM   1806 C CG2 B ILE   B 2 147 ? -0.323  -4.035  -19.384 0.20 51.74  ? 156 ILE   B CG2 1 
ATOM   1807 C CG2 C ILE   B 2 147 ? 0.022   -3.714  -19.630 0.31 55.91  ? 156 ILE   B CG2 1 
ATOM   1808 C CG2 D ILE   B 2 147 ? 0.022   -3.715  -19.630 0.30 55.91  ? 156 ILE   B CG2 1 
ATOM   1809 C CD1 A ILE   B 2 147 ? -0.056  -3.610  -22.512 0.19 52.98  ? 156 ILE   B CD1 1 
ATOM   1810 C CD1 B ILE   B 2 147 ? -0.059  -3.615  -22.509 0.20 52.97  ? 156 ILE   B CD1 1 
ATOM   1811 C CD1 C ILE   B 2 147 ? -0.062  -3.047  -22.597 0.31 57.21  ? 156 ILE   B CD1 1 
ATOM   1812 C CD1 D ILE   B 2 147 ? -0.062  -3.048  -22.597 0.30 57.21  ? 156 ILE   B CD1 1 
ATOM   1813 N N   A LYS   B 2 148 ? 3.927   -2.935  -19.895 0.19 53.87  ? 157 LYS   B N   1 
ATOM   1814 N N   B LYS   B 2 148 ? 3.927   -2.935  -19.894 0.20 53.87  ? 157 LYS   B N   1 
ATOM   1815 N N   C LYS   B 2 148 ? 3.799   -1.663  -20.259 0.31 60.51  ? 157 LYS   B N   1 
ATOM   1816 N N   D LYS   B 2 148 ? 3.799   -1.663  -20.259 0.30 60.52  ? 157 LYS   B N   1 
ATOM   1817 C CA  A LYS   B 2 148 ? 5.298   -2.716  -20.442 0.19 55.14  ? 157 LYS   B CA  1 
ATOM   1818 C CA  B LYS   B 2 148 ? 5.298   -2.716  -20.442 0.20 55.14  ? 157 LYS   B CA  1 
ATOM   1819 C CA  C LYS   B 2 148 ? 5.044   -1.053  -20.804 0.31 63.16  ? 157 LYS   B CA  1 
ATOM   1820 C CA  D LYS   B 2 148 ? 5.044   -1.053  -20.804 0.30 63.16  ? 157 LYS   B CA  1 
ATOM   1821 C C   A LYS   B 2 148 ? 5.293   -1.591  -21.482 0.19 55.73  ? 157 LYS   B C   1 
ATOM   1822 C C   B LYS   B 2 148 ? 5.292   -1.591  -21.482 0.20 55.73  ? 157 LYS   B C   1 
ATOM   1823 C C   C LYS   B 2 148 ? 4.675   -0.062  -21.921 0.31 63.97  ? 157 LYS   B C   1 
ATOM   1824 C C   D LYS   B 2 148 ? 4.676   -0.062  -21.921 0.30 63.96  ? 157 LYS   B C   1 
ATOM   1825 O O   A LYS   B 2 148 ? 6.181   -0.716  -21.411 0.19 56.34  ? 157 LYS   B O   1 
ATOM   1826 O O   B LYS   B 2 148 ? 6.180   -0.716  -21.411 0.20 56.34  ? 157 LYS   B O   1 
ATOM   1827 O O   C LYS   B 2 148 ? 5.262   1.039   -21.950 0.31 64.20  ? 157 LYS   B O   1 
ATOM   1828 O O   D LYS   B 2 148 ? 5.263   1.038   -21.950 0.30 64.20  ? 157 LYS   B O   1 
ATOM   1829 C CB  A LYS   B 2 148 ? 5.827   -3.985  -21.121 0.19 55.82  ? 157 LYS   B CB  1 
ATOM   1830 C CB  B LYS   B 2 148 ? 5.827   -3.985  -21.121 0.20 55.82  ? 157 LYS   B CB  1 
ATOM   1831 C CB  C LYS   B 2 148 ? 6.033   -2.123  -21.295 0.31 64.90  ? 157 LYS   B CB  1 
ATOM   1832 C CB  D LYS   B 2 148 ? 6.033   -2.123  -21.295 0.30 64.89  ? 157 LYS   B CB  1 
ATOM   1833 C CG  A LYS   B 2 148 ? 6.350   -5.068  -20.188 0.19 56.11  ? 157 LYS   B CG  1 
ATOM   1834 C CG  B LYS   B 2 148 ? 6.350   -5.069  -20.189 0.20 56.12  ? 157 LYS   B CG  1 
ATOM   1835 C CG  C LYS   B 2 148 ? 5.447   -3.349  -21.996 0.31 66.37  ? 157 LYS   B CG  1 
ATOM   1836 C CG  D LYS   B 2 148 ? 5.447   -3.349  -21.996 0.30 66.36  ? 157 LYS   B CG  1 
ATOM   1837 C CD  A LYS   B 2 148 ? 6.912   -6.275  -20.917 0.19 56.18  ? 157 LYS   B CD  1 
ATOM   1838 C CD  B LYS   B 2 148 ? 6.912   -6.275  -20.917 0.20 56.18  ? 157 LYS   B CD  1 
ATOM   1839 C CD  C LYS   B 2 148 ? 4.852   -4.455  -21.105 0.31 67.01  ? 157 LYS   B CD  1 
ATOM   1840 C CD  D LYS   B 2 148 ? 4.852   -4.455  -21.105 0.30 67.00  ? 157 LYS   B CD  1 
ATOM   1841 C CE  A LYS   B 2 148 ? 8.274   -6.031  -21.531 0.19 56.71  ? 157 LYS   B CE  1 
ATOM   1842 C CE  B LYS   B 2 148 ? 8.274   -6.031  -21.532 0.20 56.71  ? 157 LYS   B CE  1 
ATOM   1843 C CE  C LYS   B 2 148 ? 5.421   -4.566  -19.700 0.31 68.16  ? 157 LYS   B CE  1 
ATOM   1844 C CE  D LYS   B 2 148 ? 5.421   -4.566  -19.701 0.30 68.14  ? 157 LYS   B CE  1 
ATOM   1845 N NZ  A LYS   B 2 148 ? 9.353   -6.020  -20.515 0.19 56.59  ? 157 LYS   B NZ  1 
ATOM   1846 N NZ  B LYS   B 2 148 ? 9.353   -6.021  -20.515 0.20 56.59  ? 157 LYS   B NZ  1 
ATOM   1847 N NZ  C LYS   B 2 148 ? 6.814   -5.076  -19.700 0.31 69.64  ? 157 LYS   B NZ  1 
ATOM   1848 N NZ  D LYS   B 2 148 ? 6.815   -5.076  -19.701 0.30 69.60  ? 157 LYS   B NZ  1 
ATOM   1849 N N   A ASN   B 2 149 ? 4.325   -1.640  -22.405 0.19 55.64  ? 158 ASN   B N   1 
ATOM   1850 N N   B ASN   B 2 149 ? 4.325   -1.640  -22.404 0.20 55.63  ? 158 ASN   B N   1 
ATOM   1851 N N   C ASN   B 2 149 ? 3.702   -0.424  -22.764 0.31 64.03  ? 158 ASN   B N   1 
ATOM   1852 N N   D ASN   B 2 149 ? 3.703   -0.424  -22.765 0.30 64.03  ? 158 ASN   B N   1 
ATOM   1853 C CA  A ASN   B 2 149 ? 4.184   -0.747  -23.586 0.19 55.92  ? 158 ASN   B CA  1 
ATOM   1854 C CA  B ASN   B 2 149 ? 4.182   -0.746  -23.585 0.20 55.91  ? 158 ASN   B CA  1 
ATOM   1855 C CA  C ASN   B 2 149 ? 3.257   0.347   -23.961 0.31 65.01  ? 158 ASN   B CA  1 
ATOM   1856 C CA  D ASN   B 2 149 ? 3.258   0.347   -23.961 0.30 64.99  ? 158 ASN   B CA  1 
ATOM   1857 C C   A ASN   B 2 149 ? 3.934   0.701   -23.135 0.19 55.18  ? 158 ASN   B C   1 
ATOM   1858 C C   B ASN   B 2 149 ? 3.931   0.702   -23.133 0.20 55.15  ? 158 ASN   B C   1 
ATOM   1859 C C   C ASN   B 2 149 ? 2.821   1.764   -23.555 0.31 62.93  ? 158 ASN   B C   1 
ATOM   1860 C C   D ASN   B 2 149 ? 2.822   1.764   -23.555 0.30 62.92  ? 158 ASN   B C   1 
ATOM   1861 O O   A ASN   B 2 149 ? 4.538   1.618   -23.735 0.19 55.97  ? 158 ASN   B O   1 
ATOM   1862 O O   B ASN   B 2 149 ? 4.532   1.620   -23.736 0.20 55.96  ? 158 ASN   B O   1 
ATOM   1863 O O   C ASN   B 2 149 ? 2.750   2.628   -24.450 0.31 63.09  ? 158 ASN   B O   1 
ATOM   1864 O O   D ASN   B 2 149 ? 2.752   2.628   -24.450 0.30 63.09  ? 158 ASN   B O   1 
ATOM   1865 C CB  A ASN   B 2 149 ? 3.060   -1.239  -24.506 0.19 56.55  ? 158 ASN   B CB  1 
ATOM   1866 C CB  B ASN   B 2 149 ? 3.059   -1.239  -24.505 0.20 56.55  ? 158 ASN   B CB  1 
ATOM   1867 C CB  C ASN   B 2 149 ? 2.120   -0.365  -24.706 0.31 66.37  ? 158 ASN   B CB  1 
ATOM   1868 C CB  D ASN   B 2 149 ? 2.120   -0.365  -24.706 0.30 66.35  ? 158 ASN   B CB  1 
ATOM   1869 C CG  A ASN   B 2 149 ? 3.109   -2.732  -24.767 0.19 56.83  ? 158 ASN   B CG  1 
ATOM   1870 C CG  B ASN   B 2 149 ? 3.110   -2.732  -24.767 0.20 56.83  ? 158 ASN   B CG  1 
ATOM   1871 C CG  C ASN   B 2 149 ? 2.330   -1.860  -24.868 0.31 67.69  ? 158 ASN   B CG  1 
ATOM   1872 C CG  D ASN   B 2 149 ? 2.331   -1.860  -24.868 0.30 67.67  ? 158 ASN   B CG  1 
ATOM   1873 O OD1 A ASN   B 2 149 ? 3.875   -3.455  -24.133 0.19 56.59  ? 158 ASN   B OD1 1 
ATOM   1874 O OD1 B ASN   B 2 149 ? 3.876   -3.455  -24.134 0.20 56.59  ? 158 ASN   B OD1 1 
ATOM   1875 O OD1 C ASN   B 2 149 ? 3.162   -2.460  -24.186 0.31 66.34  ? 158 ASN   B OD1 1 
ATOM   1876 O OD1 D ASN   B 2 149 ? 3.163   -2.460  -24.187 0.30 66.34  ? 158 ASN   B OD1 1 
ATOM   1877 N ND2 A ASN   B 2 149 ? 2.294   -3.208  -25.696 0.19 57.54  ? 158 ASN   B ND2 1 
ATOM   1878 N ND2 B ASN   B 2 149 ? 2.295   -3.208  -25.696 0.20 57.55  ? 158 ASN   B ND2 1 
ATOM   1879 N ND2 C ASN   B 2 149 ? 1.572   -2.475  -25.764 0.31 69.43  ? 158 ASN   B ND2 1 
ATOM   1880 N ND2 D ASN   B 2 149 ? 1.572   -2.476  -25.764 0.30 69.38  ? 158 ASN   B ND2 1 
ATOM   1881 N N   A GLY   B 2 150 ? 3.069   0.891   -22.132 0.19 53.45  ? 159 GLY   B N   1 
ATOM   1882 N N   B GLY   B 2 150 ? 3.070   0.892   -22.126 0.20 53.38  ? 159 GLY   B N   1 
ATOM   1883 N N   C GLY   B 2 150 ? 2.542   1.990   -22.263 0.31 60.40  ? 159 GLY   B N   1 
ATOM   1884 N N   D GLY   B 2 150 ? 2.543   1.989   -22.263 0.30 60.39  ? 159 GLY   B N   1 
ATOM   1885 C CA  A GLY   B 2 150 ? 2.609   2.208   -21.646 0.19 52.41  ? 159 GLY   B CA  1 
ATOM   1886 C CA  B GLY   B 2 150 ? 2.606   2.210   -21.641 0.20 52.28  ? 159 GLY   B CA  1 
ATOM   1887 C CA  C GLY   B 2 150 ? 1.910   3.215   -21.730 0.31 58.17  ? 159 GLY   B CA  1 
ATOM   1888 C CA  D GLY   B 2 150 ? 1.910   3.215   -21.731 0.30 58.17  ? 159 GLY   B CA  1 
ATOM   1889 C C   A GLY   B 2 150 ? 1.111   2.388   -21.833 0.19 51.27  ? 159 GLY   B C   1 
ATOM   1890 C C   B GLY   B 2 150 ? 1.108   2.385   -21.840 0.20 51.05  ? 159 GLY   B C   1 
ATOM   1891 C C   C GLY   B 2 150 ? 0.396   3.134   -21.862 0.31 55.85  ? 159 GLY   B C   1 
ATOM   1892 C C   D GLY   B 2 150 ? 0.397   3.132   -21.861 0.30 55.85  ? 159 GLY   B C   1 
ATOM   1893 O O   A GLY   B 2 150 ? 0.566   3.376   -21.286 0.19 50.76  ? 159 GLY   B O   1 
ATOM   1894 O O   B GLY   B 2 150 ? 0.551   3.375   -21.309 0.20 50.63  ? 159 GLY   B O   1 
ATOM   1895 O O   C GLY   B 2 150 ? -0.308  4.011   -21.314 0.31 54.47  ? 159 GLY   B O   1 
ATOM   1896 O O   D GLY   B 2 150 ? -0.308  4.009   -21.312 0.30 54.49  ? 159 GLY   B O   1 
ATOM   1897 N N   A SER   B 2 151 ? 0.468   1.484   -22.587 0.19 50.09  ? 160 SER   B N   1 
ATOM   1898 N N   B SER   B 2 151 ? 0.487   1.462   -22.590 0.20 49.55  ? 160 SER   B N   1 
ATOM   1899 N N   C SER   B 2 151 ? -0.068  2.096   -22.570 0.31 53.99  ? 160 SER   B N   1 
ATOM   1900 N N   D SER   B 2 151 ? -0.068  2.095   -22.569 0.30 53.99  ? 160 SER   B N   1 
ATOM   1901 C CA  A SER   B 2 151 ? -1.000  1.457   -22.817 0.19 48.90  ? 160 SER   B CA  1 
ATOM   1902 C CA  B SER   B 2 151 ? -0.975  1.367   -22.841 0.20 48.16  ? 160 SER   B CA  1 
ATOM   1903 C CA  C SER   B 2 151 ? -1.485  1.713   -22.784 0.31 52.46  ? 160 SER   B CA  1 
ATOM   1904 C CA  D SER   B 2 151 ? -1.485  1.712   -22.784 0.30 52.46  ? 160 SER   B CA  1 
ATOM   1905 C C   A SER   B 2 151 ? -1.706  0.816   -21.617 0.19 47.32  ? 160 SER   B C   1 
ATOM   1906 C C   B SER   B 2 151 ? -1.708  0.924   -21.569 0.20 46.82  ? 160 SER   B C   1 
ATOM   1907 C C   C SER   B 2 151 ? -2.108  1.276   -21.453 0.31 50.07  ? 160 SER   B C   1 
ATOM   1908 C C   D SER   B 2 151 ? -2.108  1.275   -21.453 0.30 50.07  ? 160 SER   B C   1 
ATOM   1909 O O   A SER   B 2 151 ? -1.012  0.349   -20.686 0.19 46.42  ? 160 SER   B O   1 
ATOM   1910 O O   B SER   B 2 151 ? -1.035  0.691   -20.540 0.20 45.87  ? 160 SER   B O   1 
ATOM   1911 O O   C SER   B 2 151 ? -1.346  1.074   -20.478 0.31 48.69  ? 160 SER   B O   1 
ATOM   1912 O O   D SER   B 2 151 ? -1.347  1.073   -20.478 0.30 48.71  ? 160 SER   B O   1 
ATOM   1913 C CB  A SER   B 2 151 ? -1.354  0.749   -24.099 0.19 49.66  ? 160 SER   B CB  1 
ATOM   1914 C CB  B SER   B 2 151 ? -1.248  0.410   -23.969 0.20 48.54  ? 160 SER   B CB  1 
ATOM   1915 C CB  C SER   B 2 151 ? -1.564  0.610   -23.814 0.31 53.49  ? 160 SER   B CB  1 
ATOM   1916 C CB  D SER   B 2 151 ? -1.564  0.610   -23.814 0.30 53.48  ? 160 SER   B CB  1 
ATOM   1917 O OG  A SER   B 2 151 ? -2.639  1.157   -24.551 0.19 49.65  ? 160 SER   B OG  1 
ATOM   1918 O OG  B SER   B 2 151 ? -0.706  -0.866  -23.665 0.20 47.67  ? 160 SER   B OG  1 
ATOM   1919 O OG  C SER   B 2 151 ? -2.885  0.456   -24.315 0.31 54.03  ? 160 SER   B OG  1 
ATOM   1920 O OG  D SER   B 2 151 ? -2.885  0.455   -24.313 0.30 54.01  ? 160 SER   B OG  1 
ATOM   1921 N N   A TYR   B 2 152 ? -3.039  0.786   -21.670 0.19 45.68  ? 161 TYR   B N   1 
ATOM   1922 N N   B TYR   B 2 152 ? -3.034  0.791   -21.664 0.20 45.49  ? 161 TYR   B N   1 
ATOM   1923 N N   C TYR   B 2 152 ? -3.436  1.119   -21.431 0.31 48.12  ? 161 TYR   B N   1 
ATOM   1924 N N   D TYR   B 2 152 ? -3.436  1.120   -21.431 0.30 48.11  ? 161 TYR   B N   1 
ATOM   1925 C CA  A TYR   B 2 152 ? -3.946  0.454   -20.544 0.19 44.35  ? 161 TYR   B CA  1 
ATOM   1926 C CA  B TYR   B 2 152 ? -3.947  0.460   -20.542 0.20 44.27  ? 161 TYR   B CA  1 
ATOM   1927 C CA  C TYR   B 2 152 ? -4.219  0.618   -20.269 0.31 46.31  ? 161 TYR   B CA  1 
ATOM   1928 C CA  D TYR   B 2 152 ? -4.220  0.618   -20.270 0.30 46.30  ? 161 TYR   B CA  1 
ATOM   1929 C C   A TYR   B 2 152 ? -4.609  -0.904  -20.795 0.19 43.03  ? 161 TYR   B C   1 
ATOM   1930 C C   B TYR   B 2 152 ? -4.608  -0.899  -20.793 0.20 42.99  ? 161 TYR   B C   1 
ATOM   1931 C C   C TYR   B 2 152 ? -4.856  -0.727  -20.640 0.31 44.25  ? 161 TYR   B C   1 
ATOM   1932 C C   D TYR   B 2 152 ? -4.856  -0.726  -20.640 0.30 44.25  ? 161 TYR   B C   1 
ATOM   1933 O O   A TYR   B 2 152 ? -4.965  -1.205  -21.940 0.19 42.51  ? 161 TYR   B O   1 
ATOM   1934 O O   B TYR   B 2 152 ? -4.963  -1.200  -21.938 0.20 42.49  ? 161 TYR   B O   1 
ATOM   1935 O O   C TYR   B 2 152 ? -5.400  -0.866  -21.743 0.31 43.26  ? 161 TYR   B O   1 
ATOM   1936 O O   D TYR   B 2 152 ? -5.402  -0.865  -21.743 0.30 43.27  ? 161 TYR   B O   1 
ATOM   1937 C CB  A TYR   B 2 152 ? -4.992  1.561   -20.397 0.19 44.44  ? 161 TYR   B CB  1 
ATOM   1938 C CB  B TYR   B 2 152 ? -4.994  1.566   -20.397 0.20 44.40  ? 161 TYR   B CB  1 
ATOM   1939 C CB  C TYR   B 2 152 ? -5.290  1.634   -19.853 0.31 46.82  ? 161 TYR   B CB  1 
ATOM   1940 C CB  D TYR   B 2 152 ? -5.290  1.635   -19.853 0.30 46.81  ? 161 TYR   B CB  1 
ATOM   1941 C CG  A TYR   B 2 152 ? -5.962  1.355   -19.262 0.19 44.03  ? 161 TYR   B CG  1 
ATOM   1942 C CG  B TYR   B 2 152 ? -5.963  1.359   -19.263 0.20 44.01  ? 161 TYR   B CG  1 
ATOM   1943 C CG  C TYR   B 2 152 ? -5.703  1.586   -18.400 0.31 46.85  ? 161 TYR   B CG  1 
ATOM   1944 C CG  D TYR   B 2 152 ? -5.704  1.586   -18.400 0.30 46.85  ? 161 TYR   B CG  1 
ATOM   1945 C CD1 A TYR   B 2 152 ? -5.513  1.253   -17.956 0.19 43.88  ? 161 TYR   B CD1 1 
ATOM   1946 C CD1 B TYR   B 2 152 ? -5.514  1.256   -17.956 0.20 43.87  ? 161 TYR   B CD1 1 
ATOM   1947 C CD1 C TYR   B 2 152 ? -4.897  2.130   -17.412 0.31 47.26  ? 161 TYR   B CD1 1 
ATOM   1948 C CD1 D TYR   B 2 152 ? -4.897  2.130   -17.413 0.30 47.25  ? 161 TYR   B CD1 1 
ATOM   1949 C CD2 A TYR   B 2 152 ? -7.324  1.263   -19.493 0.19 43.82  ? 161 TYR   B CD2 1 
ATOM   1950 C CD2 B TYR   B 2 152 ? -7.326  1.265   -19.493 0.20 43.81  ? 161 TYR   B CD2 1 
ATOM   1951 C CD2 C TYR   B 2 152 ? -6.913  1.033   -18.001 0.31 46.71  ? 161 TYR   B CD2 1 
ATOM   1952 C CD2 D TYR   B 2 152 ? -6.913  1.033   -18.002 0.30 46.70  ? 161 TYR   B CD2 1 
ATOM   1953 C CE1 A TYR   B 2 152 ? -6.394  1.072   -16.902 0.19 43.51  ? 161 TYR   B CE1 1 
ATOM   1954 C CE1 B TYR   B 2 152 ? -6.394  1.074   -16.903 0.20 43.50  ? 161 TYR   B CE1 1 
ATOM   1955 C CE1 C TYR   B 2 152 ? -5.261  2.108   -16.075 0.31 46.74  ? 161 TYR   B CE1 1 
ATOM   1956 C CE1 D TYR   B 2 152 ? -5.261  2.108   -16.075 0.30 46.74  ? 161 TYR   B CE1 1 
ATOM   1957 C CE2 A TYR   B 2 152 ? -8.220  1.080   -18.453 0.19 43.41  ? 161 TYR   B CE2 1 
ATOM   1958 C CE2 B TYR   B 2 152 ? -8.220  1.081   -18.453 0.20 43.41  ? 161 TYR   B CE2 1 
ATOM   1959 C CE2 C TYR   B 2 152 ? -7.296  1.004   -16.666 0.31 46.29  ? 161 TYR   B CE2 1 
ATOM   1960 C CE2 D TYR   B 2 152 ? -7.296  1.004   -16.666 0.30 46.28  ? 161 TYR   B CE2 1 
ATOM   1961 C CZ  A TYR   B 2 152 ? -7.752  0.986   -17.152 0.19 43.26  ? 161 TYR   B CZ  1 
ATOM   1962 C CZ  B TYR   B 2 152 ? -7.752  0.986   -17.152 0.20 43.26  ? 161 TYR   B CZ  1 
ATOM   1963 C CZ  C TYR   B 2 152 ? -6.467  1.543   -15.697 0.31 46.36  ? 161 TYR   B CZ  1 
ATOM   1964 C CZ  D TYR   B 2 152 ? -6.467  1.543   -15.697 0.30 46.35  ? 161 TYR   B CZ  1 
ATOM   1965 O OH  A TYR   B 2 152 ? -8.628  0.801   -16.125 0.19 42.51  ? 161 TYR   B OH  1 
ATOM   1966 O OH  B TYR   B 2 152 ? -8.628  0.800   -16.125 0.20 42.51  ? 161 TYR   B OH  1 
ATOM   1967 O OH  C TYR   B 2 152 ? -6.838  1.524   -14.380 0.31 45.56  ? 161 TYR   B OH  1 
ATOM   1968 O OH  D TYR   B 2 152 ? -6.838  1.523   -14.380 0.30 45.56  ? 161 TYR   B OH  1 
ATOM   1969 N N   A VAL   B 2 153 ? -4.770  -1.696  -19.734 0.19 41.46  ? 162 VAL   B N   1 
ATOM   1970 N N   B VAL   B 2 153 ? -4.767  -1.693  -19.733 0.20 41.45  ? 162 VAL   B N   1 
ATOM   1971 N N   C VAL   B 2 153 ? -4.769  -1.693  -19.727 0.31 41.77  ? 162 VAL   B N   1 
ATOM   1972 N N   D VAL   B 2 153 ? -4.769  -1.693  -19.727 0.30 41.77  ? 162 VAL   B N   1 
ATOM   1973 C CA  A VAL   B 2 153 ? -5.597  -2.938  -19.742 0.19 40.35  ? 162 VAL   B CA  1 
ATOM   1974 C CA  B VAL   B 2 153 ? -5.595  -2.934  -19.742 0.20 40.34  ? 162 VAL   B CA  1 
ATOM   1975 C CA  C VAL   B 2 153 ? -5.593  -2.936  -19.744 0.31 40.47  ? 162 VAL   B CA  1 
ATOM   1976 C CA  D VAL   B 2 153 ? -5.592  -2.935  -19.743 0.30 40.47  ? 162 VAL   B CA  1 
ATOM   1977 C C   A VAL   B 2 153 ? -6.533  -2.878  -18.531 0.19 38.92  ? 162 VAL   B C   1 
ATOM   1978 C C   B VAL   B 2 153 ? -6.532  -2.875  -18.531 0.20 38.92  ? 162 VAL   B C   1 
ATOM   1979 C C   C VAL   B 2 153 ? -6.527  -2.878  -18.530 0.31 38.94  ? 162 VAL   B C   1 
ATOM   1980 C C   D VAL   B 2 153 ? -6.527  -2.878  -18.530 0.30 38.94  ? 162 VAL   B C   1 
ATOM   1981 O O   A VAL   B 2 153 ? -6.025  -2.834  -17.397 0.19 38.69  ? 162 VAL   B O   1 
ATOM   1982 O O   B VAL   B 2 153 ? -6.025  -2.834  -17.396 0.20 38.69  ? 162 VAL   B O   1 
ATOM   1983 O O   C VAL   B 2 153 ? -6.019  -2.828  -17.398 0.31 38.70  ? 162 VAL   B O   1 
ATOM   1984 O O   D VAL   B 2 153 ? -6.019  -2.828  -17.397 0.30 38.70  ? 162 VAL   B O   1 
ATOM   1985 C CB  A VAL   B 2 153 ? -4.719  -4.203  -19.740 0.19 40.44  ? 162 VAL   B CB  1 
ATOM   1986 C CB  B VAL   B 2 153 ? -4.719  -4.200  -19.740 0.20 40.44  ? 162 VAL   B CB  1 
ATOM   1987 C CB  C VAL   B 2 153 ? -4.716  -4.201  -19.742 0.31 40.46  ? 162 VAL   B CB  1 
ATOM   1988 C CB  D VAL   B 2 153 ? -4.716  -4.201  -19.742 0.30 40.46  ? 162 VAL   B CB  1 
ATOM   1989 C CG1 A VAL   B 2 153 ? -5.559  -5.471  -19.815 0.19 40.31  ? 162 VAL   B CG1 1 
ATOM   1990 C CG1 B VAL   B 2 153 ? -5.560  -5.468  -19.816 0.20 40.31  ? 162 VAL   B CG1 1 
ATOM   1991 C CG1 C VAL   B 2 153 ? -5.560  -5.467  -19.822 0.31 40.31  ? 162 VAL   B CG1 1 
ATOM   1992 C CG1 D VAL   B 2 153 ? -5.559  -5.467  -19.822 0.30 40.31  ? 162 VAL   B CG1 1 
ATOM   1993 C CG2 A VAL   B 2 153 ? -3.695  -4.168  -20.865 0.19 41.25  ? 162 VAL   B CG2 1 
ATOM   1994 C CG2 B VAL   B 2 153 ? -3.695  -4.167  -20.866 0.20 41.25  ? 162 VAL   B CG2 1 
ATOM   1995 C CG2 C VAL   B 2 153 ? -3.691  -4.164  -20.865 0.31 41.35  ? 162 VAL   B CG2 1 
ATOM   1996 C CG2 D VAL   B 2 153 ? -3.691  -4.164  -20.866 0.30 41.34  ? 162 VAL   B CG2 1 
ATOM   1997 N N   A SER   B 2 154 ? -7.846  -2.844  -18.797 0.19 37.77  ? 163 SER   B N   1 
ATOM   1998 N N   B SER   B 2 154 ? -7.845  -2.841  -18.798 0.20 37.77  ? 163 SER   B N   1 
ATOM   1999 N N   C SER   B 2 154 ? -7.837  -2.872  -18.794 0.31 37.77  ? 163 SER   B N   1 
ATOM   2000 N N   D SER   B 2 154 ? -7.837  -2.872  -18.794 0.30 37.77  ? 163 SER   B N   1 
ATOM   2001 C CA  A SER   B 2 154 ? -8.930  -2.817  -17.786 0.19 36.51  ? 163 SER   B CA  1 
ATOM   2002 C CA  B SER   B 2 154 ? -8.929  -2.816  -17.787 0.20 36.51  ? 163 SER   B CA  1 
ATOM   2003 C CA  C SER   B 2 154 ? -8.909  -2.810  -17.777 0.31 36.40  ? 163 SER   B CA  1 
ATOM   2004 C CA  D SER   B 2 154 ? -8.909  -2.810  -17.777 0.30 36.40  ? 163 SER   B CA  1 
ATOM   2005 C C   A SER   B 2 154 ? -9.317  -4.266  -17.477 0.19 35.74  ? 163 SER   B C   1 
ATOM   2006 C C   B SER   B 2 154 ? -9.315  -4.266  -17.480 0.20 35.74  ? 163 SER   B C   1 
ATOM   2007 C C   C SER   B 2 154 ? -9.387  -4.243  -17.538 0.31 35.59  ? 163 SER   B C   1 
ATOM   2008 C C   D SER   B 2 154 ? -9.388  -4.242  -17.537 0.30 35.59  ? 163 SER   B C   1 
ATOM   2009 O O   A SER   B 2 154 ? -9.428  -5.082  -18.430 0.19 35.34  ? 163 SER   B O   1 
ATOM   2010 O O   B SER   B 2 154 ? -9.425  -5.082  -18.433 0.20 35.34  ? 163 SER   B O   1 
ATOM   2011 O O   C SER   B 2 154 ? -9.508  -5.030  -18.511 0.31 34.91  ? 163 SER   B O   1 
ATOM   2012 O O   D SER   B 2 154 ? -9.509  -5.029  -18.510 0.30 34.92  ? 163 SER   B O   1 
ATOM   2013 C CB  A SER   B 2 154 ? -10.118 -2.023  -18.286 0.19 36.55  ? 163 SER   B CB  1 
ATOM   2014 C CB  B SER   B 2 154 ? -10.119 -2.023  -18.286 0.20 36.55  ? 163 SER   B CB  1 
ATOM   2015 C CB  C SER   B 2 154 ? -10.043 -1.915  -18.220 0.31 36.49  ? 163 SER   B CB  1 
ATOM   2016 C CB  D SER   B 2 154 ? -10.042 -1.914  -18.220 0.30 36.49  ? 163 SER   B CB  1 
ATOM   2017 O OG  A SER   B 2 154 ? -11.179 -2.025  -17.317 0.19 36.13  ? 163 SER   B OG  1 
ATOM   2018 O OG  B SER   B 2 154 ? -11.178 -2.025  -17.315 0.20 36.13  ? 163 SER   B OG  1 
ATOM   2019 O OG  C SER   B 2 154 ? -11.141 -1.970  -17.242 0.31 36.09  ? 163 SER   B OG  1 
ATOM   2020 O OG  D SER   B 2 154 ? -11.141 -1.969  -17.246 0.30 36.10  ? 163 SER   B OG  1 
ATOM   2021 N N   A ALA   B 2 155 ? -9.519  -4.570  -16.199 0.19 34.55  ? 164 ALA   B N   1 
ATOM   2022 N N   B ALA   B 2 155 ? -9.517  -4.571  -16.201 0.20 34.55  ? 164 ALA   B N   1 
ATOM   2023 N N   C ALA   B 2 155 ? -9.647  -4.566  -16.282 0.31 34.22  ? 164 ALA   B N   1 
ATOM   2024 N N   D ALA   B 2 155 ? -9.648  -4.565  -16.280 0.30 34.23  ? 164 ALA   B N   1 
ATOM   2025 C CA  A ALA   B 2 155 ? -10.417 -5.668  -15.799 0.19 34.11  ? 164 ALA   B CA  1 
ATOM   2026 C CA  B ALA   B 2 155 ? -10.416 -5.668  -15.802 0.20 34.11  ? 164 ALA   B CA  1 
ATOM   2027 C CA  C ALA   B 2 155 ? -10.529 -5.697  -15.954 0.31 33.88  ? 164 ALA   B CA  1 
ATOM   2028 C CA  D ALA   B 2 155 ? -10.529 -5.696  -15.951 0.30 33.88  ? 164 ALA   B CA  1 
ATOM   2029 C C   A ALA   B 2 155 ? -11.752 -5.387  -16.606 0.19 33.82  ? 164 ALA   B C   1 
ATOM   2030 C C   B ALA   B 2 155 ? -11.751 -5.386  -16.605 0.20 33.82  ? 164 ALA   B C   1 
ATOM   2031 C C   C ALA   B 2 155 ? -11.846 -5.422  -16.653 0.31 33.68  ? 164 ALA   B C   1 
ATOM   2032 C C   D ALA   B 2 155 ? -11.847 -5.422  -16.654 0.30 33.69  ? 164 ALA   B C   1 
ATOM   2033 O O   A ALA   B 2 155 ? -12.031 -4.177  -16.826 0.19 34.44  ? 164 ALA   B O   1 
ATOM   2034 O O   B ALA   B 2 155 ? -12.033 -4.177  -16.826 0.20 34.44  ? 164 ALA   B O   1 
ATOM   2035 O O   C ALA   B 2 155 ? -12.178 -4.260  -16.914 0.31 34.58  ? 164 ALA   B O   1 
ATOM   2036 O O   D ALA   B 2 155 ? -12.176 -4.260  -16.914 0.30 34.57  ? 164 ALA   B O   1 
ATOM   2037 C CB  A ALA   B 2 155 ? -10.564 -5.715  -14.254 0.19 33.64  ? 164 ALA   B CB  1 
ATOM   2038 C CB  B ALA   B 2 155 ? -10.566 -5.715  -14.257 0.20 33.64  ? 164 ALA   B CB  1 
ATOM   2039 C CB  C ALA   B 2 155 ? -10.738 -5.753  -14.387 0.31 33.30  ? 164 ALA   B CB  1 
ATOM   2040 C CB  D ALA   B 2 155 ? -10.736 -5.752  -14.384 0.30 33.31  ? 164 ALA   B CB  1 
ATOM   2041 N N   A ILE   B 2 156 ? -12.457 -6.600  -16.777 0.19 33.42  ? 165 ILE   B N   1 
ATOM   2042 N N   B ILE   B 2 156 ? -12.456 -6.601  -16.780 0.20 33.42  ? 165 ILE   B N   1 
ATOM   2043 N N   C ILE   B 2 156 ? -12.592 -6.704  -16.827 0.31 33.35  ? 165 ILE   B N   1 
ATOM   2044 N N   D ILE   B 2 156 ? -12.593 -6.704  -16.821 0.30 33.35  ? 165 ILE   B N   1 
ATOM   2045 C CA  A ILE   B 2 156 ? -13.950 -6.604  -16.795 0.19 33.17  ? 165 ILE   B CA  1 
ATOM   2046 C CA  B ILE   B 2 156 ? -13.949 -6.604  -16.798 0.20 33.17  ? 165 ILE   B CA  1 
ATOM   2047 C CA  C ILE   B 2 156 ? -14.084 -6.659  -16.871 0.31 33.21  ? 165 ILE   B CA  1 
ATOM   2048 C CA  D ILE   B 2 156 ? -14.085 -6.659  -16.868 0.30 33.21  ? 165 ILE   B CA  1 
ATOM   2049 C C   A ILE   B 2 156 ? -14.378 -6.724  -15.327 0.19 32.61  ? 165 ILE   B C   1 
ATOM   2050 C C   B ILE   B 2 156 ? -14.375 -6.724  -15.328 0.20 32.61  ? 165 ILE   B C   1 
ATOM   2051 C C   C ILE   B 2 156 ? -14.581 -6.723  -15.419 0.31 32.59  ? 165 ILE   B C   1 
ATOM   2052 C C   D ILE   B 2 156 ? -14.583 -6.724  -15.417 0.30 32.60  ? 165 ILE   B C   1 
ATOM   2053 O O   A ILE   B 2 156 ? -14.275 -7.852  -14.807 0.19 32.56  ? 165 ILE   B O   1 
ATOM   2054 O O   B ILE   B 2 156 ? -14.269 -7.850  -14.808 0.20 32.56  ? 165 ILE   B O   1 
ATOM   2055 O O   C ILE   B 2 156 ? -14.895 -7.845  -14.972 0.31 32.70  ? 165 ILE   B O   1 
ATOM   2056 O O   D ILE   B 2 156 ? -14.899 -7.845  -14.970 0.30 32.70  ? 165 ILE   B O   1 
ATOM   2057 C CB  A ILE   B 2 156 ? -14.447 -7.781  -17.653 0.19 33.48  ? 165 ILE   B CB  1 
ATOM   2058 C CB  B ILE   B 2 156 ? -14.447 -7.781  -17.654 0.20 33.48  ? 165 ILE   B CB  1 
ATOM   2059 C CB  C ILE   B 2 156 ? -14.610 -7.841  -17.691 0.31 33.47  ? 165 ILE   B CB  1 
ATOM   2060 C CB  D ILE   B 2 156 ? -14.611 -7.840  -17.689 0.30 33.47  ? 165 ILE   B CB  1 
ATOM   2061 C CG1 A ILE   B 2 156 ? -13.806 -7.730  -19.045 0.19 33.95  ? 165 ILE   B CG1 1 
ATOM   2062 C CG1 B ILE   B 2 156 ? -13.806 -7.730  -19.046 0.20 33.95  ? 165 ILE   B CG1 1 
ATOM   2063 C CG1 C ILE   B 2 156 ? -13.862 -7.917  -19.023 0.31 34.04  ? 165 ILE   B CG1 1 
ATOM   2064 C CG1 D ILE   B 2 156 ? -13.862 -7.916  -19.021 0.30 34.03  ? 165 ILE   B CG1 1 
ATOM   2065 C CG2 A ILE   B 2 156 ? -15.969 -7.823  -17.718 0.19 33.51  ? 165 ILE   B CG2 1 
ATOM   2066 C CG2 B ILE   B 2 156 ? -15.969 -7.823  -17.719 0.20 33.51  ? 165 ILE   B CG2 1 
ATOM   2067 C CG2 C ILE   B 2 156 ? -16.123 -7.752  -17.875 0.31 33.48  ? 165 ILE   B CG2 1 
ATOM   2068 C CG2 D ILE   B 2 156 ? -16.123 -7.752  -17.874 0.30 33.48  ? 165 ILE   B CG2 1 
ATOM   2069 C CD1 A ILE   B 2 156 ? -14.160 -8.887  -19.936 0.19 34.36  ? 165 ILE   B CD1 1 
ATOM   2070 C CD1 B ILE   B 2 156 ? -14.160 -8.888  -19.938 0.20 34.37  ? 165 ILE   B CD1 1 
ATOM   2071 C CD1 C ILE   B 2 156 ? -14.181 -9.135  -19.830 0.31 34.47  ? 165 ILE   B CD1 1 
ATOM   2072 C CD1 D ILE   B 2 156 ? -14.181 -9.134  -19.829 0.30 34.47  ? 165 ILE   B CD1 1 
ATOM   2073 N N   A THR   B 2 157 ? -14.740 -5.595  -14.691 0.19 32.36  ? 166 THR   B N   1 
ATOM   2074 N N   B THR   B 2 157 ? -14.739 -5.596  -14.693 0.20 32.36  ? 166 THR   B N   1 
ATOM   2075 N N   C THR   B 2 157 ? -14.607 -5.575  -14.722 0.31 32.48  ? 166 THR   B N   1 
ATOM   2076 N N   D THR   B 2 157 ? -14.608 -5.576  -14.719 0.30 32.48  ? 166 THR   B N   1 
ATOM   2077 C CA  A THR   B 2 157 ? -15.378 -5.561  -13.324 0.19 31.93  ? 166 THR   B CA  1 
ATOM   2078 C CA  B THR   B 2 157 ? -15.377 -5.561  -13.326 0.20 31.93  ? 166 THR   B CA  1 
ATOM   2079 C CA  C THR   B 2 157 ? -15.319 -5.487  -13.381 0.31 31.93  ? 166 THR   B CA  1 
ATOM   2080 C CA  D THR   B 2 157 ? -15.320 -5.487  -13.378 0.30 31.93  ? 166 THR   B CA  1 
ATOM   2081 C C   A THR   B 2 157 ? -16.901 -5.913  -13.579 0.19 32.11  ? 166 THR   B C   1 
ATOM   2082 C C   B THR   B 2 157 ? -16.900 -5.914  -13.580 0.20 32.11  ? 166 THR   B C   1 
ATOM   2083 C C   C THR   B 2 157 ? -16.882 -5.761  -13.524 0.31 32.19  ? 166 THR   B C   1 
ATOM   2084 C C   D THR   B 2 157 ? -16.882 -5.762  -13.524 0.30 32.19  ? 166 THR   B C   1 
ATOM   2085 O O   A THR   B 2 157 ? -17.611 -5.209  -14.121 0.19 32.10  ? 166 THR   B O   1 
ATOM   2086 O O   B THR   B 2 157 ? -17.609 -5.207  -14.123 0.20 32.10  ? 166 THR   B O   1 
ATOM   2087 O O   C THR   B 2 157 ? -17.605 -5.000  -13.898 0.31 32.46  ? 166 THR   B O   1 
ATOM   2088 O O   D THR   B 2 157 ? -17.606 -4.998  -13.900 0.30 32.45  ? 166 THR   B O   1 
ATOM   2089 C CB  A THR   B 2 157 ? -15.113 -4.212  -12.619 0.19 31.65  ? 166 THR   B CB  1 
ATOM   2090 C CB  B THR   B 2 157 ? -15.114 -4.211  -12.621 0.20 31.65  ? 166 THR   B CB  1 
ATOM   2091 C CB  C THR   B 2 157 ? -14.991 -4.136  -12.699 0.31 31.70  ? 166 THR   B CB  1 
ATOM   2092 C CB  D THR   B 2 157 ? -14.990 -4.137  -12.696 0.30 31.69  ? 166 THR   B CB  1 
ATOM   2093 O OG1 A THR   B 2 157 ? -13.713 -3.875  -13.007 0.19 31.58  ? 166 THR   B OG1 1 
ATOM   2094 O OG1 B THR   B 2 157 ? -13.713 -3.872  -13.005 0.20 31.58  ? 166 THR   B OG1 1 
ATOM   2095 O OG1 C THR   B 2 157 ? -13.516 -3.878  -12.918 0.31 31.66  ? 166 THR   B OG1 1 
ATOM   2096 O OG1 D THR   B 2 157 ? -13.517 -3.883  -12.921 0.30 31.66  ? 166 THR   B OG1 1 
ATOM   2097 C CG2 A THR   B 2 157 ? -15.450 -4.259  -11.115 0.19 31.49  ? 166 THR   B CG2 1 
ATOM   2098 C CG2 B THR   B 2 157 ? -15.450 -4.259  -11.116 0.20 31.49  ? 166 THR   B CG2 1 
ATOM   2099 C CG2 C THR   B 2 157 ? -15.352 -4.148  -11.178 0.31 31.43  ? 166 THR   B CG2 1 
ATOM   2100 C CG2 D THR   B 2 157 ? -15.354 -4.147  -11.175 0.30 31.43  ? 166 THR   B CG2 1 
ATOM   2101 N N   A GLN   B 2 158 ? -17.328 -6.885  -12.536 0.19 32.32  ? 167 GLN   B N   1 
ATOM   2102 N N   B GLN   B 2 158 ? -17.327 -6.886  -12.537 0.20 32.32  ? 167 GLN   B N   1 
ATOM   2103 N N   C GLN   B 2 158 ? -17.290 -6.836  -12.655 0.31 32.31  ? 167 GLN   B N   1 
ATOM   2104 N N   D GLN   B 2 158 ? -17.290 -6.837  -12.652 0.30 32.31  ? 167 GLN   B N   1 
ATOM   2105 C CA  A GLN   B 2 158 ? -18.759 -7.290  -12.403 0.19 32.63  ? 167 GLN   B CA  1 
ATOM   2106 C CA  B GLN   B 2 158 ? -18.758 -7.291  -12.403 0.20 32.62  ? 167 GLN   B CA  1 
ATOM   2107 C CA  C GLN   B 2 158 ? -18.732 -7.147  -12.425 0.31 32.48  ? 167 GLN   B CA  1 
ATOM   2108 C CA  D GLN   B 2 158 ? -18.732 -7.148  -12.424 0.30 32.48  ? 167 GLN   B CA  1 
ATOM   2109 C C   A GLN   B 2 158 ? -19.085 -7.504  -10.916 0.19 33.35  ? 167 GLN   B C   1 
ATOM   2110 C C   B GLN   B 2 158 ? -19.085 -7.504  -10.917 0.20 33.35  ? 167 GLN   B C   1 
ATOM   2111 C C   C GLN   B 2 158 ? -18.976 -7.207  -10.906 0.31 33.13  ? 167 GLN   B C   1 
ATOM   2112 C C   D GLN   B 2 158 ? -18.977 -7.208  -10.905 0.30 33.14  ? 167 GLN   B C   1 
ATOM   2113 O O   A GLN   B 2 158 ? -18.330 -8.247  -10.273 0.19 33.12  ? 167 GLN   B O   1 
ATOM   2114 O O   B GLN   B 2 158 ? -18.330 -8.248  -10.274 0.20 33.11  ? 167 GLN   B O   1 
ATOM   2115 O O   C GLN   B 2 158 ? -18.018 -7.501  -10.206 0.31 32.83  ? 167 GLN   B O   1 
ATOM   2116 O O   D GLN   B 2 158 ? -18.019 -7.503  -10.204 0.30 32.83  ? 167 GLN   B O   1 
ATOM   2117 C CB  A GLN   B 2 158 ? -19.043 -8.594  -13.150 0.19 32.68  ? 167 GLN   B CB  1 
ATOM   2118 C CB  B GLN   B 2 158 ? -19.043 -8.594  -13.150 0.20 32.68  ? 167 GLN   B CB  1 
ATOM   2119 C CB  C GLN   B 2 158 ? -19.107 -8.491  -13.049 0.31 32.46  ? 167 GLN   B CB  1 
ATOM   2120 C CB  D GLN   B 2 158 ? -19.107 -8.491  -13.049 0.30 32.46  ? 167 GLN   B CB  1 
ATOM   2121 C CG  A GLN   B 2 158 ? -20.516 -8.985  -13.207 0.19 32.61  ? 167 GLN   B CG  1 
ATOM   2122 C CG  B GLN   B 2 158 ? -20.516 -8.985  -13.208 0.20 32.61  ? 167 GLN   B CG  1 
ATOM   2123 C CG  C GLN   B 2 158 ? -20.595 -8.809  -13.047 0.31 32.38  ? 167 GLN   B CG  1 
ATOM   2124 C CG  D GLN   B 2 158 ? -20.595 -8.809  -13.047 0.30 32.38  ? 167 GLN   B CG  1 
ATOM   2125 C CD  A GLN   B 2 158 ? -21.412 -7.885  -13.732 0.19 32.39  ? 167 GLN   B CD  1 
ATOM   2126 C CD  B GLN   B 2 158 ? -21.412 -7.885  -13.733 0.20 32.38  ? 167 GLN   B CD  1 
ATOM   2127 C CD  C GLN   B 2 158 ? -21.452 -7.743  -13.694 0.31 32.15  ? 167 GLN   B CD  1 
ATOM   2128 C CD  D GLN   B 2 158 ? -21.452 -7.743  -13.692 0.30 32.15  ? 167 GLN   B CD  1 
ATOM   2129 O OE1 A GLN   B 2 158 ? -21.558 -6.824  -13.125 0.19 32.03  ? 167 GLN   B OE1 1 
ATOM   2130 O OE1 B GLN   B 2 158 ? -21.557 -6.823  -13.127 0.20 32.03  ? 167 GLN   B OE1 1 
ATOM   2131 O OE1 C GLN   B 2 158 ? -21.569 -6.617  -13.203 0.31 31.76  ? 167 GLN   B OE1 1 
ATOM   2132 O OE1 D GLN   B 2 158 ? -21.569 -6.617  -13.201 0.30 31.76  ? 167 GLN   B OE1 1 
ATOM   2133 N NE2 A GLN   B 2 158 ? -22.035 -8.127  -14.878 0.19 32.52  ? 167 GLN   B NE2 1 
ATOM   2134 N NE2 B GLN   B 2 158 ? -22.035 -8.127  -14.879 0.20 32.52  ? 167 GLN   B NE2 1 
ATOM   2135 N NE2 C GLN   B 2 158 ? -22.065 -8.085  -14.822 0.31 32.30  ? 167 GLN   B NE2 1 
ATOM   2136 N NE2 D GLN   B 2 158 ? -22.065 -8.084  -14.821 0.30 32.30  ? 167 GLN   B NE2 1 
ATOM   2137 N N   A GLY   B 2 159 ? -20.192 -6.929  -10.432 0.19 34.46  ? 168 GLY   B N   1 
ATOM   2138 N N   B GLY   B 2 159 ? -20.192 -6.929  -10.432 0.20 34.46  ? 168 GLY   B N   1 
ATOM   2139 N N   C GLY   B 2 159 ? -20.208 -6.954  -10.458 0.31 34.39  ? 168 GLY   B N   1 
ATOM   2140 N N   D GLY   B 2 159 ? -20.208 -6.954  -10.457 0.30 34.40  ? 168 GLY   B N   1 
ATOM   2141 C CA  A GLY   B 2 159 ? -20.659 -7.088  -9.036  0.19 35.84  ? 168 GLY   B CA  1 
ATOM   2142 C CA  B GLY   B 2 159 ? -20.658 -7.088  -9.036  0.20 35.84  ? 168 GLY   B CA  1 
ATOM   2143 C CA  C GLY   B 2 159 ? -20.649 -7.103  -9.050  0.31 35.79  ? 168 GLY   B CA  1 
ATOM   2144 C CA  D GLY   B 2 159 ? -20.650 -7.103  -9.049  0.30 35.79  ? 168 GLY   B CA  1 
ATOM   2145 C C   A GLY   B 2 159 ? -21.502 -8.342  -8.863  0.19 37.59  ? 168 GLY   B C   1 
ATOM   2146 C C   B GLY   B 2 159 ? -21.502 -8.342  -8.863  0.20 37.59  ? 168 GLY   B C   1 
ATOM   2147 C C   C GLY   B 2 159 ? -21.504 -8.347  -8.864  0.31 37.55  ? 168 GLY   B C   1 
ATOM   2148 C C   D GLY   B 2 159 ? -21.505 -8.347  -8.864  0.30 37.55  ? 168 GLY   B C   1 
ATOM   2149 O O   A GLY   B 2 159 ? -21.718 -9.054  -9.856  0.19 38.31  ? 168 GLY   B O   1 
ATOM   2150 O O   B GLY   B 2 159 ? -21.718 -9.054  -9.855  0.20 38.31  ? 168 GLY   B O   1 
ATOM   2151 O O   C GLY   B 2 159 ? -21.729 -9.064  -9.846  0.31 38.38  ? 168 GLY   B O   1 
ATOM   2152 O O   D GLY   B 2 159 ? -21.729 -9.064  -9.847  0.30 38.37  ? 168 GLY   B O   1 
ATOM   2153 N N   . LYS   B 2 160 ? -21.960 -8.616  -7.637  1.00 39.58  ? 169 LYS   B N   1 
ATOM   2154 C CA  . LYS   B 2 160 ? -22.823 -9.793  -7.336  1.00 43.46  ? 169 LYS   B CA  1 
ATOM   2155 C C   . LYS   B 2 160 ? -24.265 -9.263  -7.299  1.00 48.64  ? 169 LYS   B C   1 
ATOM   2156 O O   . LYS   B 2 160 ? -24.482 -8.167  -6.714  1.00 48.25  ? 169 LYS   B O   1 
ATOM   2157 C CB  . LYS   B 2 160 ? -22.409 -10.433 -6.004  1.00 47.77  ? 169 LYS   B CB  1 
ATOM   2158 C CG  . LYS   B 2 160 ? -22.811 -11.897 -5.863  1.00 51.27  ? 169 LYS   B CG  1 
ATOM   2159 C CD  . LYS   B 2 160 ? -22.424 -12.526 -4.530  1.00 53.52  ? 169 LYS   B CD  1 
ATOM   2160 C CE  . LYS   B 2 160 ? -23.556 -13.308 -3.888  1.00 55.45  ? 169 LYS   B CE  1 
ATOM   2161 N NZ  . LYS   B 2 160 ? -23.516 -13.179 -2.409  1.00 58.64  ? 169 LYS   B NZ  1 
ATOM   2162 N N   . ARG   B 2 161 ? -25.215 -10.000 -7.882  1.00 52.53  ? 170 ARG   B N   1 
ATOM   2163 C CA  . ARG   B 2 161 ? -26.678 -9.791  -7.673  1.00 56.33  ? 170 ARG   B CA  1 
ATOM   2164 C C   . ARG   B 2 161 ? -27.124 -10.723 -6.520  1.00 61.20  ? 170 ARG   B C   1 
ATOM   2165 O O   . ARG   B 2 161 ? -26.756 -11.916 -6.545  1.00 61.67  ? 170 ARG   B O   1 
ATOM   2166 C CB  . ARG   B 2 161 ? -27.361 -10.003 -9.033  1.00 56.60  ? 170 ARG   B CB  1 
ATOM   2167 C CG  . ARG   B 2 161 ? -28.756 -9.410  -9.180  1.00 56.28  ? 170 ARG   B CG  1 
ATOM   2168 C CD  . ARG   B 2 161 ? -29.491 -9.972  -10.398 1.00 56.28  ? 170 ARG   B CD  1 
ATOM   2169 N NE  . ARG   B 2 161 ? -30.923 -9.760  -10.233 1.00 57.13  ? 170 ARG   B NE  1 
ATOM   2170 C CZ  . ARG   B 2 161 ? -31.668 -8.830  -10.832 1.00 57.24  ? 170 ARG   B CZ  1 
ATOM   2171 N NH1 . ARG   B 2 161 ? -31.151 -7.987  -11.711 1.00 55.92  ? 170 ARG   B NH1 1 
ATOM   2172 N NH2 . ARG   B 2 161 ? -32.955 -8.753  -10.535 1.00 59.16  ? 170 ARG   B NH2 1 
ATOM   2173 N N   . GLU   B 2 162 ? -27.828 -10.207 -5.502  1.00 67.15  ? 171 GLU   B N   1 
ATOM   2174 C CA  . GLU   B 2 162 ? -28.368 -11.027 -4.373  1.00 72.27  ? 171 GLU   B CA  1 
ATOM   2175 C C   . GLU   B 2 162 ? -29.827 -11.394 -4.673  1.00 73.08  ? 171 GLU   B C   1 
ATOM   2176 O O   . GLU   B 2 162 ? -30.221 -12.561 -4.605  1.00 78.15  ? 171 GLU   B O   1 
ATOM   2177 C CB  . GLU   B 2 162 ? -28.267 -10.276 -3.044  1.00 75.82  ? 171 GLU   B CB  1 
ATOM   2178 C CG  . GLU   B 2 162 ? -26.877 -9.725  -2.737  1.00 80.31  ? 171 GLU   B CG  1 
ATOM   2179 C CD  . GLU   B 2 162 ? -25.920 -10.638 -1.973  1.00 85.92  ? 171 GLU   B CD  1 
ATOM   2180 O OE1 . GLU   B 2 162 ? -24.721 -10.683 -2.356  1.00 89.28  ? 171 GLU   B OE1 1 
ATOM   2181 O OE2 . GLU   B 2 162 ? -26.354 -11.282 -0.980  1.00 90.02  ? 171 GLU   B OE2 1 
HETATM 2182 S S   A DMS   C 3 .   ? -8.061  5.406   -18.542 0.19 81.78  ? 201 DMS   B S   1 
HETATM 2183 S S   B DMS   C 3 .   ? -8.061  5.406   -18.542 0.20 81.78  ? 201 DMS   B S   1 
HETATM 2184 O O   A DMS   C 3 .   ? -6.903  4.792   -19.279 0.19 82.90  ? 201 DMS   B O   1 
HETATM 2185 O O   B DMS   C 3 .   ? -6.903  4.792   -19.279 0.20 82.91  ? 201 DMS   B O   1 
HETATM 2186 C C1  A DMS   C 3 .   ? -7.829  5.020   -16.826 0.19 81.48  ? 201 DMS   B C1  1 
HETATM 2187 C C1  B DMS   C 3 .   ? -7.829  5.021   -16.826 0.20 81.48  ? 201 DMS   B C1  1 
HETATM 2188 C C2  A DMS   C 3 .   ? -9.453  4.346   -18.840 0.19 81.15  ? 201 DMS   B C2  1 
HETATM 2189 C C2  B DMS   C 3 .   ? -9.453  4.346   -18.840 0.20 81.15  ? 201 DMS   B C2  1 
HETATM 2190 S S   A DMS   D 3 .   ? -18.429 11.188  -0.415  0.50 359.51 ? 202 DMS   B S   1 
HETATM 2191 S S   B DMS   D 3 .   ? -18.429 11.188  -0.415  0.50 359.51 ? 202 DMS   B S   1 
HETATM 2192 O O   A DMS   D 3 .   ? -19.118 9.924   -0.850  0.50 355.41 ? 202 DMS   B O   1 
HETATM 2193 O O   B DMS   D 3 .   ? -19.118 9.924   -0.850  0.50 355.41 ? 202 DMS   B O   1 
HETATM 2194 C C1  A DMS   D 3 .   ? -19.610 12.493  -0.636  0.50 354.64 ? 202 DMS   B C1  1 
HETATM 2195 C C1  B DMS   D 3 .   ? -19.610 12.493  -0.636  0.50 354.64 ? 202 DMS   B C1  1 
HETATM 2196 C C2  A DMS   D 3 .   ? -17.328 11.640  -1.732  0.50 350.02 ? 202 DMS   B C2  1 
HETATM 2197 C C2  B DMS   D 3 .   ? -17.328 11.640  -1.732  0.50 350.02 ? 202 DMS   B C2  1 
HETATM 2198 S S   A DMS   E 3 .   ? -7.195  2.876   -13.930 0.19 61.55  ? 203 DMS   B S   1 
HETATM 2199 S S   B DMS   E 3 .   ? -7.196  2.876   -13.930 0.20 61.55  ? 203 DMS   B S   1 
HETATM 2200 O O   A DMS   E 3 .   ? -7.148  1.381   -13.804 0.19 60.10  ? 203 DMS   B O   1 
HETATM 2201 O O   B DMS   E 3 .   ? -7.149  1.381   -13.804 0.20 60.10  ? 203 DMS   B O   1 
HETATM 2202 C C1  A DMS   E 3 .   ? -8.145  3.446   -12.542 0.19 61.52  ? 203 DMS   B C1  1 
HETATM 2203 C C1  B DMS   E 3 .   ? -8.145  3.446   -12.542 0.20 61.52  ? 203 DMS   B C1  1 
HETATM 2204 C C2  A DMS   E 3 .   ? -5.609  3.477   -13.395 0.19 61.85  ? 203 DMS   B C2  1 
HETATM 2205 C C2  B DMS   E 3 .   ? -5.609  3.477   -13.395 0.20 61.85  ? 203 DMS   B C2  1 
HETATM 2206 N N1  C A1BG2 F 4 .   ? -8.628  4.294   -9.128  0.31 44.71  ? 204 A1BG2 B N1  1 
HETATM 2207 N N1  D A1BG2 F 4 .   ? -8.627  4.294   -9.129  0.30 44.70  ? 204 A1BG2 B N1  1 
HETATM 2208 N N3  C A1BG2 F 4 .   ? -5.996  5.190   -20.177 0.31 46.42  ? 204 A1BG2 B N3  1 
HETATM 2209 N N3  D A1BG2 F 4 .   ? -5.996  5.190   -20.176 0.30 46.43  ? 204 A1BG2 B N3  1 
HETATM 2210 C C4  C A1BG2 F 4 .   ? -8.646  3.208   -9.906  0.31 44.34  ? 204 A1BG2 B C4  1 
HETATM 2211 C C4  D A1BG2 F 4 .   ? -8.646  3.209   -9.907  0.30 44.34  ? 204 A1BG2 B C4  1 
HETATM 2212 C C5  C A1BG2 F 4 .   ? -8.646  3.248   -11.274 0.31 44.25  ? 204 A1BG2 B C5  1 
HETATM 2213 C C5  D A1BG2 F 4 .   ? -8.646  3.248   -11.275 0.30 44.25  ? 204 A1BG2 B C5  1 
HETATM 2214 C C6  C A1BG2 F 4 .   ? -8.621  4.479   -11.914 0.31 44.66  ? 204 A1BG2 B C6  1 
HETATM 2215 C C6  D A1BG2 F 4 .   ? -8.621  4.479   -11.914 0.30 44.65  ? 204 A1BG2 B C6  1 
HETATM 2216 C C7  C A1BG2 F 4 .   ? -7.674  5.051   -14.174 0.31 44.84  ? 204 A1BG2 B C7  1 
HETATM 2217 C C7  D A1BG2 F 4 .   ? -7.673  5.051   -14.174 0.30 44.84  ? 204 A1BG2 B C7  1 
HETATM 2218 C C8  C A1BG2 F 4 .   ? -7.859  4.863   -15.659 0.31 44.87  ? 204 A1BG2 B C8  1 
HETATM 2219 C C8  D A1BG2 F 4 .   ? -7.859  4.863   -15.659 0.30 44.87  ? 204 A1BG2 B C8  1 
HETATM 2220 C C10 C A1BG2 F 4 .   ? -9.251  4.273   -17.544 0.31 44.76  ? 204 A1BG2 B C10 1 
HETATM 2221 C C10 D A1BG2 F 4 .   ? -9.251  4.273   -17.543 0.30 44.76  ? 204 A1BG2 B C10 1 
HETATM 2222 C C13 C A1BG2 F 4 .   ? -5.857  5.152   -18.868 0.31 46.55  ? 204 A1BG2 B C13 1 
HETATM 2223 C C13 D A1BG2 F 4 .   ? -5.857  5.152   -18.868 0.30 46.55  ? 204 A1BG2 B C13 1 
HETATM 2224 C C15 C A1BG2 F 4 .   ? -3.746  5.524   -19.970 0.31 47.20  ? 204 A1BG2 B C15 1 
HETATM 2225 C C15 D A1BG2 F 4 .   ? -3.746  5.524   -19.970 0.30 47.20  ? 204 A1BG2 B C15 1 
HETATM 2226 C C1  C A1BG2 F 4 .   ? -8.593  7.017   -11.732 0.31 44.96  ? 204 A1BG2 B C1  1 
HETATM 2227 C C1  D A1BG2 F 4 .   ? -8.593  7.017   -11.732 0.30 44.96  ? 204 A1BG2 B C1  1 
HETATM 2228 C C2  C A1BG2 F 4 .   ? -8.612  5.635   -11.124 0.31 44.65  ? 204 A1BG2 B C2  1 
HETATM 2229 C C2  D A1BG2 F 4 .   ? -8.612  5.635   -11.124 0.30 44.65  ? 204 A1BG2 B C2  1 
HETATM 2230 C C3  C A1BG2 F 4 .   ? -8.608  5.490   -9.745  0.31 44.76  ? 204 A1BG2 B C3  1 
HETATM 2231 C C3  D A1BG2 F 4 .   ? -8.608  5.490   -9.746  0.30 44.76  ? 204 A1BG2 B C3  1 
HETATM 2232 N N2  C A1BG2 F 4 .   ? -8.639  4.561   -13.350 0.31 44.38  ? 204 A1BG2 B N2  1 
HETATM 2233 N N2  D A1BG2 F 4 .   ? -8.639  4.562   -13.350 0.30 44.38  ? 204 A1BG2 B N2  1 
HETATM 2234 O O1  C A1BG2 F 4 .   ? -6.679  5.617   -13.730 0.31 45.17  ? 204 A1BG2 B O1  1 
HETATM 2235 O O1  D A1BG2 F 4 .   ? -6.679  5.617   -13.731 0.30 45.16  ? 204 A1BG2 B O1  1 
HETATM 2236 C C9  C A1BG2 F 4 .   ? -9.083  4.448   -16.183 0.31 44.53  ? 204 A1BG2 B C9  1 
HETATM 2237 C C9  D A1BG2 F 4 .   ? -9.083  4.448   -16.183 0.30 44.53  ? 204 A1BG2 B C9  1 
HETATM 2238 C C11 C A1BG2 F 4 .   ? -8.202  4.507   -18.412 0.31 45.34  ? 204 A1BG2 B C11 1 
HETATM 2239 C C11 D A1BG2 F 4 .   ? -8.202  4.507   -18.412 0.30 45.34  ? 204 A1BG2 B C11 1 
HETATM 2240 C C12 C A1BG2 F 4 .   ? -6.967  4.929   -17.928 0.31 45.72  ? 204 A1BG2 B C12 1 
HETATM 2241 C C12 D A1BG2 F 4 .   ? -6.967  4.929   -17.927 0.30 45.72  ? 204 A1BG2 B C12 1 
HETATM 2242 C C14 C A1BG2 F 4 .   ? -4.772  5.264   -20.784 0.31 46.97  ? 204 A1BG2 B C14 1 
HETATM 2243 C C14 D A1BG2 F 4 .   ? -4.773  5.264   -20.784 0.30 46.97  ? 204 A1BG2 B C14 1 
HETATM 2244 S S1  C A1BG2 F 4 .   ? -4.211  5.322   -18.338 0.31 47.63  ? 204 A1BG2 B S1  1 
HETATM 2245 S S1  D A1BG2 F 4 .   ? -4.211  5.322   -18.338 0.30 47.62  ? 204 A1BG2 B S1  1 
HETATM 2246 C C16 C A1BG2 F 4 .   ? -6.804  5.095   -16.546 0.31 45.40  ? 204 A1BG2 B C16 1 
HETATM 2247 C C16 D A1BG2 F 4 .   ? -6.804  5.095   -16.546 0.30 45.40  ? 204 A1BG2 B C16 1 
HETATM 2248 S S   C SO4   G 5 .   ? -18.651 11.394  -0.331  0.50 94.16  ? 205 SO4   B S   1 
HETATM 2249 S S   D SO4   G 5 .   ? -18.651 11.394  -0.331  0.50 94.16  ? 205 SO4   B S   1 
HETATM 2250 O O1  C SO4   G 5 .   ? -18.659 12.166  -1.548  0.50 93.60  ? 205 SO4   B O1  1 
HETATM 2251 O O1  D SO4   G 5 .   ? -18.659 12.166  -1.548  0.50 93.60  ? 205 SO4   B O1  1 
HETATM 2252 O O2  C SO4   G 5 .   ? -19.020 12.243  0.771   0.50 92.95  ? 205 SO4   B O2  1 
HETATM 2253 O O2  D SO4   G 5 .   ? -19.020 12.243  0.771   0.50 92.95  ? 205 SO4   B O2  1 
HETATM 2254 O O3  C SO4   G 5 .   ? -19.590 10.302  -0.422  0.50 92.09  ? 205 SO4   B O3  1 
HETATM 2255 O O3  D SO4   G 5 .   ? -19.590 10.302  -0.422  0.50 92.09  ? 205 SO4   B O3  1 
HETATM 2256 O O4  C SO4   G 5 .   ? -17.328 10.865  -0.119  0.50 94.77  ? 205 SO4   B O4  1 
HETATM 2257 O O4  D SO4   G 5 .   ? -17.328 10.865  -0.119  0.50 94.77  ? 205 SO4   B O4  1 
HETATM 2258 S S   C DMS   H 3 .   ? -6.127  0.590   -28.332 0.31 67.73  ? 206 DMS   B S   1 
HETATM 2259 S S   D DMS   H 3 .   ? -6.127  0.590   -28.332 0.30 67.72  ? 206 DMS   B S   1 
HETATM 2260 O O   C DMS   H 3 .   ? -5.409  1.255   -29.479 0.31 69.27  ? 206 DMS   B O   1 
HETATM 2261 O O   D DMS   H 3 .   ? -5.408  1.256   -29.478 0.30 69.25  ? 206 DMS   B O   1 
HETATM 2262 C C1  C DMS   H 3 .   ? -6.243  -1.119  -28.785 0.31 66.92  ? 206 DMS   B C1  1 
HETATM 2263 C C1  D DMS   H 3 .   ? -6.243  -1.119  -28.785 0.30 66.93  ? 206 DMS   B C1  1 
HETATM 2264 C C2  C DMS   H 3 .   ? -7.842  1.011   -28.509 0.31 67.01  ? 206 DMS   B C2  1 
HETATM 2265 C C2  D DMS   H 3 .   ? -7.842  1.011   -28.509 0.30 67.01  ? 206 DMS   B C2  1 
HETATM 2266 S S   C DMS   I 3 .   ? -5.057  9.241   -17.006 0.31 64.34  ? 207 DMS   B S   1 
HETATM 2267 S S   D DMS   I 3 .   ? -5.057  9.241   -17.006 0.30 64.33  ? 207 DMS   B S   1 
HETATM 2268 O O   C DMS   I 3 .   ? -5.604  9.308   -18.410 0.31 64.10  ? 207 DMS   B O   1 
HETATM 2269 O O   D DMS   I 3 .   ? -5.603  9.309   -18.411 0.30 64.10  ? 207 DMS   B O   1 
HETATM 2270 C C1  C DMS   I 3 .   ? -5.348  10.843  -16.294 0.31 64.33  ? 207 DMS   B C1  1 
HETATM 2271 C C1  D DMS   I 3 .   ? -5.348  10.843  -16.294 0.30 64.33  ? 207 DMS   B C1  1 
HETATM 2272 C C2  C DMS   I 3 .   ? -3.289  9.355   -17.147 0.31 64.14  ? 207 DMS   B C2  1 
HETATM 2273 C C2  D DMS   I 3 .   ? -3.289  9.355   -17.147 0.30 64.14  ? 207 DMS   B C2  1 
HETATM 2274 S S   C DMS   J 3 .   ? -16.428 -20.500 -30.004 0.50 115.66 ? 208 DMS   B S   1 
HETATM 2275 S S   D DMS   J 3 .   ? -16.428 -20.500 -30.004 0.50 115.66 ? 208 DMS   B S   1 
HETATM 2276 O O   C DMS   J 3 .   ? -16.591 -20.329 -31.490 0.50 114.43 ? 208 DMS   B O   1 
HETATM 2277 O O   D DMS   J 3 .   ? -16.591 -20.329 -31.490 0.50 114.43 ? 208 DMS   B O   1 
HETATM 2278 C C1  C DMS   J 3 .   ? -16.060 -18.888 -29.367 0.50 111.35 ? 208 DMS   B C1  1 
HETATM 2279 C C1  D DMS   J 3 .   ? -16.060 -18.888 -29.367 0.50 111.35 ? 208 DMS   B C1  1 
HETATM 2280 C C2  C DMS   J 3 .   ? -14.826 -21.208 -29.784 0.50 113.61 ? 208 DMS   B C2  1 
HETATM 2281 C C2  D DMS   J 3 .   ? -14.826 -21.208 -29.784 0.50 113.61 ? 208 DMS   B C2  1 
HETATM 2282 O O   A HOH   K 6 .   ? -26.926 0.962   -29.674 0.50 68.96  ? 101 HOH   A O   1 
HETATM 2283 O O   B HOH   K 6 .   ? -26.926 0.962   -29.674 0.50 68.96  ? 101 HOH   A O   1 
HETATM 2284 O O   . HOH   K 6 .   ? -27.789 -6.032  -28.231 1.00 46.19  ? 102 HOH   A O   1 
HETATM 2285 O O   . HOH   K 6 .   ? 5.240   -5.659  -12.475 1.00 126.27 ? 103 HOH   A O   1 
HETATM 2286 O O   . HOH   K 6 .   ? -8.083  0.464   3.467   1.00 48.87  ? 104 HOH   A O   1 
HETATM 2287 O O   . HOH   K 6 .   ? -28.892 15.499  -15.067 1.00 50.09  ? 105 HOH   A O   1 
HETATM 2288 O O   . HOH   K 6 .   ? -24.026 9.037   -27.547 1.00 38.04  ? 106 HOH   A O   1 
HETATM 2289 O O   A HOH   K 6 .   ? -23.363 18.915  -19.445 0.50 52.94  ? 107 HOH   A O   1 
HETATM 2290 O O   B HOH   K 6 .   ? -23.363 18.915  -19.445 0.50 52.94  ? 107 HOH   A O   1 
HETATM 2291 O O   . HOH   K 6 .   ? -2.222  -4.034  -6.344  1.00 58.90  ? 108 HOH   A O   1 
HETATM 2292 O O   . HOH   K 6 .   ? -3.748  -3.817  0.311   1.00 60.90  ? 109 HOH   A O   1 
HETATM 2293 O O   . HOH   K 6 .   ? -2.858  -11.744 -7.010  1.00 40.46  ? 110 HOH   A O   1 
HETATM 2294 O O   . HOH   K 6 .   ? -3.979  -14.468 -25.464 1.00 39.67  ? 111 HOH   A O   1 
HETATM 2295 O O   . HOH   K 6 .   ? -8.136  -1.744  6.894   1.00 49.03  ? 112 HOH   A O   1 
HETATM 2296 O O   . HOH   K 6 .   ? -30.617 0.281   -23.086 1.00 52.74  ? 113 HOH   A O   1 
HETATM 2297 O O   . HOH   K 6 .   ? -6.981  -9.212  -3.028  1.00 47.12  ? 114 HOH   A O   1 
HETATM 2298 O O   . HOH   K 6 .   ? -4.716  -10.181 -5.599  1.00 50.40  ? 115 HOH   A O   1 
HETATM 2299 O O   A HOH   K 6 .   ? -5.170  -6.273  -0.311  0.50 92.55  ? 116 HOH   A O   1 
HETATM 2300 O O   B HOH   K 6 .   ? -5.170  -6.273  -0.311  0.50 92.55  ? 116 HOH   A O   1 
HETATM 2301 O O   . HOH   K 6 .   ? -5.659  2.198   -9.982  1.00 53.05  ? 117 HOH   A O   1 
HETATM 2302 O O   . HOH   K 6 .   ? -23.285 -9.710  -34.517 1.00 61.37  ? 118 HOH   A O   1 
HETATM 2303 O O   . HOH   K 6 .   ? -26.571 -3.855  -35.253 1.00 61.21  ? 119 HOH   A O   1 
HETATM 2304 O O   C HOH   K 6 .   ? -16.090 2.103   -33.773 0.50 70.66  ? 120 HOH   A O   1 
HETATM 2305 O O   D HOH   K 6 .   ? -16.090 2.103   -33.773 0.50 70.66  ? 120 HOH   A O   1 
HETATM 2306 O O   . HOH   K 6 .   ? -3.867  -1.076  -0.053  1.00 54.62  ? 121 HOH   A O   1 
HETATM 2307 O O   . HOH   K 6 .   ? -1.604  -5.995  -3.974  1.00 56.68  ? 122 HOH   A O   1 
HETATM 2308 O O   A HOH   K 6 .   ? -9.024  5.086   -7.402  0.20 44.66  ? 123 HOH   A O   1 
HETATM 2309 O O   B HOH   K 6 .   ? -9.024  5.086   -7.402  0.20 44.66  ? 123 HOH   A O   1 
HETATM 2310 O O   A HOH   L 6 .   ? 3.463   -4.585  -19.293 0.50 82.75  ? 301 HOH   B O   1 
HETATM 2311 O O   B HOH   L 6 .   ? 3.463   -4.585  -19.293 0.50 82.75  ? 301 HOH   B O   1 
HETATM 2312 O O   A HOH   L 6 .   ? -16.851 25.579  -13.190 0.50 63.33  ? 302 HOH   B O   1 
HETATM 2313 O O   B HOH   L 6 .   ? -16.851 25.579  -13.190 0.50 63.33  ? 302 HOH   B O   1 
HETATM 2314 O O   . HOH   L 6 .   ? -30.362 12.709  -19.459 1.00 59.01  ? 303 HOH   B O   1 
HETATM 2315 O O   . HOH   L 6 .   ? -33.739 1.484   -15.439 1.00 45.22  ? 304 HOH   B O   1 
HETATM 2316 O O   . HOH   L 6 .   ? -18.646 -19.883 -20.487 1.00 73.42  ? 305 HOH   B O   1 
HETATM 2317 O O   . HOH   L 6 .   ? -15.616 -10.123 -15.231 1.00 56.69  ? 306 HOH   B O   1 
HETATM 2318 O O   . HOH   L 6 .   ? -25.745 -8.055  -16.749 1.00 50.23  ? 307 HOH   B O   1 
HETATM 2319 O O   . HOH   L 6 .   ? -16.957 12.725  -5.536  1.00 49.98  ? 308 HOH   B O   1 
HETATM 2320 O O   . HOH   L 6 .   ? -22.466 -9.741  -2.916  1.00 95.62  ? 309 HOH   B O   1 
HETATM 2321 O O   . HOH   L 6 .   ? -19.427 -12.263 -25.663 1.00 55.17  ? 310 HOH   B O   1 
HETATM 2322 O O   . HOH   L 6 .   ? -16.782 -15.784 -30.343 1.00 74.44  ? 311 HOH   B O   1 
HETATM 2323 O O   A HOH   L 6 .   ? -23.486 11.288  -26.845 0.50 77.80  ? 312 HOH   B O   1 
HETATM 2324 O O   B HOH   L 6 .   ? -23.486 11.288  -26.845 0.50 77.80  ? 312 HOH   B O   1 
HETATM 2325 O O   . HOH   L 6 .   ? -6.290  -0.407  -10.683 1.00 41.79  ? 313 HOH   B O   1 
HETATM 2326 O O   . HOH   L 6 .   ? -12.914 -2.438  -14.952 1.00 37.21  ? 314 HOH   B O   1 
HETATM 2327 O O   . HOH   L 6 .   ? -9.093  -6.462  -25.417 1.00 58.29  ? 315 HOH   B O   1 
HETATM 2328 O O   . HOH   L 6 .   ? -16.641 -7.113  -8.034  1.00 54.22  ? 316 HOH   B O   1 
HETATM 2329 O O   . HOH   L 6 .   ? -20.312 -7.999  -5.590  1.00 55.88  ? 317 HOH   B O   1 
HETATM 2330 O O   . HOH   L 6 .   ? -17.940 -10.795 -16.482 1.00 43.57  ? 318 HOH   B O   1 
HETATM 2331 O O   C HOH   L 6 .   ? -21.383 14.065  -34.171 0.50 68.55  ? 319 HOH   B O   1 
HETATM 2332 O O   D HOH   L 6 .   ? -21.383 14.065  -34.171 0.50 68.55  ? 319 HOH   B O   1 
HETATM 2333 O O   C HOH   L 6 .   ? -28.476 -10.256 0.238   0.50 97.56  ? 320 HOH   B O   1 
HETATM 2334 O O   D HOH   L 6 .   ? -28.476 -10.256 0.238   0.50 97.56  ? 320 HOH   B O   1 
HETATM 2335 O O   C HOH   L 6 .   ? -9.895  8.567   -8.985  0.31 67.88  ? 321 HOH   B O   1 
HETATM 2336 O O   D HOH   L 6 .   ? -9.897  8.566   -8.986  0.30 67.88  ? 321 HOH   B O   1 
HETATM 2337 O O   . HOH   L 6 .   ? -28.698 -4.096  -22.575 1.00 60.80  ? 322 HOH   B O   1 
HETATM 2338 O O   C HOH   L 6 .   ? -20.502 14.147  1.935   0.50 66.61  ? 323 HOH   B O   1 
HETATM 2339 O O   D HOH   L 6 .   ? -20.502 14.147  1.935   0.50 66.61  ? 323 HOH   B O   1 
HETATM 2340 O O   . HOH   L 6 .   ? -31.655 7.118   -4.593  1.00 59.79  ? 324 HOH   B O   1 
HETATM 2341 O O   A HOH   L 6 .   ? -7.508  10.425  -19.297 0.19 42.32  ? 325 HOH   B O   1 
HETATM 2342 O O   B HOH   L 6 .   ? -7.505  10.422  -19.295 0.20 42.32  ? 325 HOH   B O   1 
HETATM 2343 O O   C HOH   L 6 .   ? -10.286 11.873  -19.142 0.31 45.15  ? 325 HOH   B O   1 
HETATM 2344 O O   D HOH   L 6 .   ? -10.287 11.881  -19.145 0.30 45.14  ? 325 HOH   B O   1 
HETATM 2345 O O   A HOH   L 6 .   ? -21.427 6.438   -32.652 0.50 66.54  ? 326 HOH   B O   1 
HETATM 2346 O O   B HOH   L 6 .   ? -21.427 6.438   -32.652 0.50 66.54  ? 326 HOH   B O   1 
HETATM 2347 O O   . HOH   L 6 .   ? -12.096 2.162   -5.648  1.00 43.65  ? 327 HOH   B O   1 
HETATM 2348 O O   . HOH   L 6 .   ? -14.629 -6.346  -1.614  1.00 63.54  ? 328 HOH   B O   1 
HETATM 2349 O O   . HOH   L 6 .   ? -16.259 20.703  -14.336 1.00 55.11  ? 329 HOH   B O   1 
HETATM 2350 O O   . HOH   L 6 .   ? -30.517 12.249  -16.398 1.00 59.63  ? 330 HOH   B O   1 
HETATM 2351 O O   . HOH   L 6 .   ? -21.495 -12.164 -13.131 1.00 57.09  ? 331 HOH   B O   1 
HETATM 2352 O O   A HOH   L 6 .   ? -29.629 -8.165  -5.158  0.50 95.20  ? 332 HOH   B O   1 
HETATM 2353 O O   B HOH   L 6 .   ? -29.629 -8.165  -5.158  0.50 95.20  ? 332 HOH   B O   1 
HETATM 2354 O O   A HOH   L 6 .   ? -28.653 -10.577 0.369   0.50 128.47 ? 333 HOH   B O   1 
HETATM 2355 O O   B HOH   L 6 .   ? -28.653 -10.577 0.369   0.50 128.47 ? 333 HOH   B O   1 
HETATM 2356 O O   . HOH   L 6 .   ? -16.084 -14.839 -16.549 1.00 51.46  ? 334 HOH   B O   1 
HETATM 2357 O O   . HOH   L 6 .   ? -14.988 16.459  -19.893 1.00 55.59  ? 335 HOH   B O   1 
HETATM 2358 O O   A HOH   L 6 .   ? -27.517 -6.881  -5.418  0.50 52.67  ? 336 HOH   B O   1 
HETATM 2359 O O   B HOH   L 6 .   ? -27.517 -6.881  -5.418  0.50 52.67  ? 336 HOH   B O   1 
HETATM 2360 O O   C HOH   L 6 .   ? -7.559  11.232  -18.990 0.31 49.49  ? 337 HOH   B O   1 
HETATM 2361 O O   D HOH   L 6 .   ? -7.561  11.232  -18.989 0.30 49.46  ? 337 HOH   B O   1 
HETATM 2362 O O   . HOH   L 6 .   ? -14.266 -12.463 -16.410 1.00 42.95  ? 338 HOH   B O   1 
HETATM 2363 O O   . HOH   L 6 .   ? -29.595 -1.172  -19.168 1.00 50.31  ? 339 HOH   B O   1 
HETATM 2364 O O   . HOH   L 6 .   ? -21.740 2.146   -32.117 1.00 68.98  ? 340 HOH   B O   1 
HETATM 2365 O O   . HOH   L 6 .   ? -27.681 -6.373  -18.656 1.00 48.47  ? 341 HOH   B O   1 
HETATM 2366 O O   . HOH   L 6 .   ? -15.200 -4.698  1.484   1.00 38.44  ? 342 HOH   B O   1 
HETATM 2367 O O   . HOH   L 6 .   ? -23.799 -14.665 -18.022 1.00 68.39  ? 343 HOH   B O   1 
HETATM 2368 O O   A HOH   L 6 .   ? -29.058 -7.644  -5.464  0.19 53.28  ? 344 HOH   B O   1 
HETATM 2369 O O   B HOH   L 6 .   ? -29.063 -7.646  -5.461  0.20 53.29  ? 344 HOH   B O   1 
HETATM 2370 O O   . HOH   L 6 .   ? -9.293  2.367   -7.143  1.00 75.70  ? 345 HOH   B O   1 
HETATM 2371 O O   . HOH   L 6 .   ? -7.153  -11.013 -5.431  1.00 52.91  ? 346 HOH   B O   1 
HETATM 2372 O O   . HOH   L 6 .   ? -12.381 -3.498  -10.319 1.00 37.42  ? 347 HOH   B O   1 
HETATM 2373 O O   A HOH   L 6 .   ? -34.042 4.922   -13.442 0.50 108.25 ? 348 HOH   B O   1 
HETATM 2374 O O   B HOH   L 6 .   ? -34.042 4.922   -13.442 0.50 108.25 ? 348 HOH   B O   1 
HETATM 2375 O O   . HOH   L 6 .   ? -15.218 8.969   -0.603  1.00 57.75  ? 349 HOH   B O   1 
HETATM 2376 O O   . HOH   L 6 .   ? -18.642 14.892  -22.162 1.00 40.47  ? 350 HOH   B O   1 
HETATM 2377 O O   C HOH   L 6 .   ? -22.082 15.164  -6.159  0.50 44.04  ? 351 HOH   B O   1 
HETATM 2378 O O   D HOH   L 6 .   ? -22.082 15.164  -6.159  0.50 44.04  ? 351 HOH   B O   1 
HETATM 2379 O O   . HOH   L 6 .   ? -21.373 -13.759 -22.034 1.00 67.99  ? 352 HOH   B O   1 
HETATM 2380 O O   . HOH   L 6 .   ? -17.098 14.552  -30.784 1.00 53.58  ? 353 HOH   B O   1 
HETATM 2381 O O   . HOH   L 6 .   ? -30.734 4.600   -2.775  1.00 52.12  ? 354 HOH   B O   1 
HETATM 2382 O O   . HOH   L 6 .   ? -25.938 -4.492  -4.010  1.00 37.90  ? 355 HOH   B O   1 
HETATM 2383 O O   . HOH   L 6 .   ? -19.318 -13.386 -22.970 1.00 44.82  ? 356 HOH   B O   1 
HETATM 2384 O O   . HOH   L 6 .   ? -11.177 -4.823  -8.187  1.00 59.31  ? 357 HOH   B O   1 
HETATM 2385 O O   A HOH   L 6 .   ? -9.585  7.029   -6.957  0.20 35.20  ? 358 HOH   B O   1 
HETATM 2386 O O   B HOH   L 6 .   ? -10.236 7.198   -6.128  0.20 25.61  ? 358 HOH   B O   1 
HETATM 2387 O O   A HOH   L 6 .   ? -0.488  0.345   -13.403 0.19 35.27  ? 359 HOH   B O   1 
HETATM 2388 O O   B HOH   L 6 .   ? -0.490  0.339   -13.403 0.20 35.28  ? 359 HOH   B O   1 
HETATM 2389 O O   C HOH   L 6 .   ? -4.795  2.795   -12.465 0.31 54.61  ? 360 HOH   B O   1 
HETATM 2390 O O   D HOH   L 6 .   ? -4.793  2.796   -12.460 0.30 54.62  ? 360 HOH   B O   1 
HETATM 2391 O O   . HOH   L 6 .   ? -10.587 22.385  -13.747 1.00 89.52  ? 361 HOH   B O   1 
HETATM 2392 O O   A HOH   L 6 .   ? -18.912 25.282  -14.477 0.50 62.45  ? 362 HOH   B O   1 
HETATM 2393 O O   B HOH   L 6 .   ? -18.912 25.282  -14.477 0.50 62.45  ? 362 HOH   B O   1 
HETATM 2394 O O   . HOH   L 6 .   ? -19.539 -5.791  -0.847  1.00 42.48  ? 363 HOH   B O   1 
HETATM 2395 O O   . HOH   L 6 .   ? -8.994  -10.845 -7.630  1.00 66.47  ? 364 HOH   B O   1 
HETATM 2396 O O   A HOH   L 6 .   ? -20.167 24.556  -16.848 0.50 81.28  ? 365 HOH   B O   1 
HETATM 2397 O O   B HOH   L 6 .   ? -20.167 24.556  -16.848 0.50 81.28  ? 365 HOH   B O   1 
HETATM 2398 O O   C HOH   L 6 .   ? -21.741 -13.983 -25.845 0.50 47.55  ? 366 HOH   B O   1 
HETATM 2399 O O   D HOH   L 6 .   ? -21.741 -13.983 -25.845 0.50 47.55  ? 366 HOH   B O   1 
HETATM 2400 O O   . HOH   L 6 .   ? -16.609 16.186  -21.753 1.00 65.12  ? 367 HOH   B O   1 
HETATM 2401 O O   . HOH   L 6 .   ? -29.561 -5.296  -0.947  1.00 50.77  ? 368 HOH   B O   1 
HETATM 2402 O O   . HOH   L 6 .   ? -1.077  -14.635 -9.850  1.00 58.40  ? 369 HOH   B O   1 
HETATM 2403 O O   . HOH   L 6 .   ? -21.257 5.631   0.000   0.50 75.94  ? 370 HOH   B O   1 
HETATM 2404 O O   A HOH   L 6 .   ? -8.980  7.046   -13.524 0.19 44.86  ? 371 HOH   B O   1 
HETATM 2405 O O   B HOH   L 6 .   ? -8.979  7.046   -13.521 0.20 44.86  ? 371 HOH   B O   1 
HETATM 2406 O O   A HOH   L 6 .   ? -18.892 -12.060 -13.668 0.19 28.40  ? 372 HOH   B O   1 
HETATM 2407 O O   B HOH   L 6 .   ? -18.892 -12.057 -13.666 0.20 28.40  ? 372 HOH   B O   1 
HETATM 2408 O O   A HOH   L 6 .   ? -30.233 -12.281 -27.055 0.25 79.91  ? 373 HOH   B O   1 
HETATM 2409 O O   B HOH   L 6 .   ? -30.233 -12.281 -27.055 0.25 79.91  ? 373 HOH   B O   1 
HETATM 2410 O O   . HOH   L 6 .   ? -21.257 4.184   0.000   0.50 60.41  ? 374 HOH   B O   1 
HETATM 2411 O O   A HOH   L 6 .   ? -6.619  10.669  -15.579 0.19 80.87  ? 375 HOH   B O   1 
HETATM 2412 O O   B HOH   L 6 .   ? -6.620  10.670  -15.583 0.20 80.88  ? 375 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   ? 0.8174 0.6639 0.8135 0.0023  0.1910  -0.0104 50  ASP   A N   
2    C CA  . ASP   A 7   ? 0.8001 0.6446 0.7686 0.0102  0.1847  -0.0082 50  ASP   A CA  
3    C C   . ASP   A 7   ? 0.7607 0.6136 0.7147 0.0270  0.1817  0.0129  50  ASP   A C   
4    O O   . ASP   A 7   ? 0.7785 0.6301 0.7499 0.0360  0.1931  0.0299  50  ASP   A O   
5    C CB  . ASP   A 7   ? 0.8255 0.6543 0.8078 0.0091  0.1966  -0.0118 50  ASP   A CB  
6    C CG  . ASP   A 7   ? 0.8378 0.6644 0.7954 0.0136  0.1900  -0.0147 50  ASP   A CG  
7    O OD1 . ASP   A 7   ? 0.8678 0.6953 0.8074 0.0048  0.1807  -0.0314 50  ASP   A OD1 
8    O OD2 . ASP   A 7   ? 0.8514 0.6761 0.8089 0.0262  0.1945  0.0000  50  ASP   A OD2 
9    N N   . MET   A 8   ? 0.7040 0.5655 0.6273 0.0310  0.1674  0.0116  51  MET   A N   
10   C CA  . MET   A 8   ? 0.6671 0.5392 0.5737 0.0451  0.1616  0.0277  51  MET   A CA  
11   C C   . MET   A 8   ? 0.6423 0.5118 0.5356 0.0561  0.1604  0.0345  51  MET   A C   
12   O O   . MET   A 8   ? 0.6232 0.4866 0.5095 0.0508  0.1576  0.0231  51  MET   A O   
13   C CB  . MET   A 8   ? 0.6604 0.5441 0.5439 0.0426  0.1464  0.0215  51  MET   A CB  
14   C CG  . MET   A 8   ? 0.6630 0.5531 0.5599 0.0343  0.1462  0.0174  51  MET   A CG  
15   S SD  . MET   A 8   ? 0.6581 0.5626 0.5280 0.0343  0.1288  0.0134  51  MET   A SD  
16   C CE  . MET   A 8   ? 0.6649 0.5779 0.5603 0.0260  0.1318  0.0115  51  MET   A CE  
17   N N   . TYR   A 9   ? 0.6099 0.4847 0.4997 0.0712  0.1626  0.0524  52  TYR   A N   
18   C CA  . TYR   A 9   ? 0.5987 0.4745 0.4767 0.0836  0.1601  0.0602  52  TYR   A CA  
19   C C   . TYR   A 9   ? 0.5848 0.4735 0.4427 0.0972  0.1522  0.0722  52  TYR   A C   
20   O O   . TYR   A 9   ? 0.5686 0.4631 0.4270 0.0991  0.1532  0.0786  52  TYR   A O   
21   C CB  . TYR   A 9   ? 0.6077 0.4746 0.5087 0.0893  0.1748  0.0703  52  TYR   A CB  
22   C CG  . TYR   A 9   ? 0.6199 0.4877 0.5375 0.0976  0.1869  0.0879  52  TYR   A CG  
23   C CD1 . TYR   A 9   ? 0.6242 0.4858 0.5660 0.0877  0.1974  0.0854  52  TYR   A CD1 
24   C CD2 . TYR   A 9   ? 0.6264 0.5020 0.5354 0.1155  0.1878  0.1069  52  TYR   A CD2 
25   C CE1 . TYR   A 9   ? 0.6379 0.4995 0.5975 0.0950  0.2103  0.1022  52  TYR   A CE1 
26   C CE2 . TYR   A 9   ? 0.6377 0.5137 0.5609 0.1241  0.2004  0.1246  52  TYR   A CE2 
27   C CZ  . TYR   A 9   ? 0.6454 0.5138 0.5949 0.1136  0.2124  0.1228  52  TYR   A CZ  
28   O OH  . TYR   A 9   ? 0.6587 0.5270 0.6246 0.1213  0.2264  0.1406  52  TYR   A OH  
29   N N   . ILE   A 10  ? 0.5815 0.4746 0.4224 0.1057  0.1439  0.0733  53  ILE   A N   
30   C CA  . ILE   A 10  ? 0.5771 0.4827 0.3965 0.1189  0.1347  0.0817  53  ILE   A CA  
31   C C   . ILE   A 10  ? 0.5863 0.4956 0.4076 0.1354  0.1391  0.0973  53  ILE   A C   
32   O O   . ILE   A 10  ? 0.5801 0.4833 0.4141 0.1360  0.1443  0.0978  53  ILE   A O   
33   C CB  . ILE   A 10  ? 0.5688 0.4788 0.3658 0.1156  0.1197  0.0690  53  ILE   A CB  
34   C CG1 . ILE   A 10  ? 0.5671 0.4729 0.3640 0.1140  0.1165  0.0613  53  ILE   A CG1 
35   C CG2 . ILE   A 10  ? 0.5657 0.4743 0.3583 0.1024  0.1151  0.0571  53  ILE   A CG2 
36   C CD1 . ILE   A 10  ? 0.5653 0.4763 0.3416 0.1132  0.1030  0.0518  53  ILE   A CD1 
37   N N   . GLU   A 11  ? 0.5926 0.5121 0.4016 0.1487  0.1375  0.1099  54  GLU   A N   
38   C CA  . GLU   A 11  ? 0.6079 0.5349 0.4125 0.1675  0.1399  0.1267  54  GLU   A CA  
39   C C   . GLU   A 11  ? 0.5961 0.5365 0.3723 0.1771  0.1257  0.1254  54  GLU   A C   
40   O O   . GLU   A 11  ? 0.5760 0.5195 0.3421 0.1740  0.1225  0.1224  54  GLU   A O   
41   C CB  . GLU   A 11  ? 0.6293 0.5552 0.4467 0.1754  0.1550  0.1451  54  GLU   A CB  
42   C CG  . GLU   A 11  ? 0.6511 0.5644 0.4986 0.1711  0.1713  0.1508  54  GLU   A CG  
43   C CD  . GLU   A 11  ? 0.6790 0.5901 0.5420 0.1770  0.1876  0.1684  54  GLU   A CD  
44   O OE1 . GLU   A 11  ? 0.7011 0.6205 0.5514 0.1834  0.1866  0.1756  54  GLU   A OE1 
45   O OE2 . GLU   A 11  ? 0.7125 0.6128 0.6017 0.1750  0.2024  0.1749  54  GLU   A OE2 
46   N N   . ARG   A 12  ? 0.6054 0.5536 0.3707 0.1868  0.1168  0.1251  55  ARG   A N   
47   C CA  . ARG   A 12  ? 0.6161 0.5775 0.3553 0.1965  0.1032  0.1226  55  ARG   A CA  
48   C C   . ARG   A 12  ? 0.6177 0.5866 0.3465 0.2107  0.1086  0.1386  55  ARG   A C   
49   O O   . ARG   A 12  ? 0.6334 0.6011 0.3737 0.2195  0.1209  0.1550  55  ARG   A O   
50   C CB  . ARG   A 12  ? 0.6309 0.6015 0.3635 0.2064  0.0934  0.1211  55  ARG   A CB  
51   C CG  . ARG   A 12  ? 0.6387 0.6200 0.3484 0.2100  0.0774  0.1103  55  ARG   A CG  
52   C CD  . ARG   A 12  ? 0.6499 0.6368 0.3611 0.2109  0.0665  0.1005  55  ARG   A CD  
53   N NE  . ARG   A 12  ? 0.6543 0.6498 0.3477 0.2119  0.0518  0.0877  55  ARG   A NE  
54   C CZ  . ARG   A 12  ? 0.6656 0.6746 0.3394 0.2262  0.0443  0.0911  55  ARG   A CZ  
55   N NH1 . ARG   A 12  ? 0.6869 0.7021 0.3550 0.2407  0.0509  0.1080  55  ARG   A NH1 
56   N NH2 . ARG   A 12  ? 0.6596 0.6750 0.3190 0.2260  0.0315  0.0776  55  ARG   A NH2 
57   N N   . ALA   A 13  ? 0.6148 0.5903 0.3242 0.2128  0.1015  0.1345  56  ALA   A N   
58   C CA  . ALA   A 13  ? 0.6257 0.6092 0.3218 0.2270  0.1064  0.1486  56  ALA   A CA  
59   C C   . ALA   A 13  ? 0.6339 0.6312 0.3021 0.2406  0.0934  0.1457  56  ALA   A C   
60   O O   . ALA   A 13  ? 0.6414 0.6463 0.2959 0.2549  0.0979  0.1583  56  ALA   A O   
61   C CB  . ALA   A 13  ? 0.6200 0.5991 0.3198 0.2184  0.1123  0.1478  56  ALA   A CB  
62   N N   . GLY   A 14  ? 0.6256 0.6262 0.2856 0.2366  0.0787  0.1297  57  GLY   A N   
63   C CA  . GLY   A 14  ? 0.6388 0.6528 0.2738 0.2490  0.0661  0.1248  57  GLY   A CA  
64   C C   . GLY   A 14  ? 0.6330 0.6474 0.2632 0.2398  0.0515  0.1044  57  GLY   A C   
65   O O   . GLY   A 14  ? 0.5953 0.5981 0.2399 0.2224  0.0517  0.0938  57  GLY   A O   
66   N N   . ASP   A 15  ? 0.6484 0.6753 0.2593 0.2508  0.0395  0.0984  58  ASP   A N   
67   C CA  . ASP   A 15  ? 0.6632 0.6917 0.2672 0.2443  0.0255  0.0784  58  ASP   A CA  
68   C C   . ASP   A 15  ? 0.6753 0.6989 0.2691 0.2392  0.0263  0.0733  58  ASP   A C   
69   O O   . ASP   A 15  ? 0.7046 0.7298 0.2898 0.2468  0.0346  0.0850  58  ASP   A O   
70   C CB  . ASP   A 15  ? 0.6792 0.7238 0.2681 0.2578  0.0122  0.0724  58  ASP   A CB  
71   C CG  . ASP   A 15  ? 0.6896 0.7408 0.2908 0.2617  0.0082  0.0743  58  ASP   A CG  
72   O OD1 . ASP   A 15  ? 0.6815 0.7237 0.3025 0.2546  0.0174  0.0815  58  ASP   A OD1 
73   O OD2 . ASP   A 15  ? 0.7008 0.7670 0.2924 0.2722  -0.0040 0.0683  58  ASP   A OD2 
74   N N   . ILE   A 16  ? 0.6734 0.6918 0.2682 0.2280  0.0187  0.0571  59  ILE   A N   
75   C CA  . ILE   A 16  ? 0.6822 0.6970 0.2664 0.2245  0.0176  0.0507  59  ILE   A CA  
76   C C   . ILE   A 16  ? 0.6974 0.7224 0.2630 0.2345  0.0059  0.0397  59  ILE   A C   
77   O O   . ILE   A 16  ? 0.6893 0.7154 0.2580 0.2302  -0.0044 0.0250  59  ILE   A O   
78   C CB  . ILE   A 16  ? 0.6669 0.6688 0.2642 0.2068  0.0184  0.0420  59  ILE   A CB  
79   C CG1 . ILE   A 16  ? 0.6594 0.6532 0.2722 0.1988  0.0302  0.0527  59  ILE   A CG1 
80   C CG2 . ILE   A 16  ? 0.6798 0.6793 0.2664 0.2047  0.0154  0.0344  59  ILE   A CG2 
81   C CD1 . ILE   A 16  ? 0.6483 0.6306 0.2748 0.1819  0.0306  0.0442  59  ILE   A CD1 
82   N N   A THR   A 17  ? 0.7135 0.7459 0.2609 0.2479  0.0082  0.0466  60  THR   A N   
83   N N   B THR   A 17  ? 0.7116 0.7440 0.2589 0.2477  0.0080  0.0461  60  THR   A N   
84   N N   C THR   A 17  ? 0.7135 0.7459 0.2609 0.2479  0.0082  0.0466  60  THR   A N   
85   N N   D THR   A 17  ? 0.7116 0.7440 0.2589 0.2477  0.0080  0.0461  60  THR   A N   
86   C CA  A THR   A 17  ? 0.7324 0.7767 0.2586 0.2608  -0.0015 0.0379  60  THR   A CA  
87   C CA  B THR   A 17  ? 0.7287 0.7727 0.2554 0.2600  -0.0024 0.0364  60  THR   A CA  
88   C CA  C THR   A 17  ? 0.7324 0.7767 0.2586 0.2608  -0.0015 0.0379  60  THR   A CA  
89   C CA  D THR   A 17  ? 0.7287 0.7727 0.2554 0.2600  -0.0024 0.0364  60  THR   A CA  
90   C C   A THR   A 17  ? 0.7450 0.7911 0.2527 0.2699  0.0040  0.0426  60  THR   A C   
91   C C   B THR   A 17  ? 0.7451 0.7933 0.2509 0.2720  0.0028  0.0425  60  THR   A C   
92   C C   C THR   A 17  ? 0.7450 0.7911 0.2527 0.2699  0.0040  0.0426  60  THR   A C   
93   C C   D THR   A 17  ? 0.7451 0.7933 0.2509 0.2720  0.0028  0.0425  60  THR   A C   
94   O O   A THR   A 17  ? 0.7558 0.8009 0.2645 0.2744  0.0169  0.0606  60  THR   A O   
95   O O   B THR   A 17  ? 0.7533 0.8014 0.2610 0.2771  0.0149  0.0610  60  THR   A O   
96   O O   C THR   A 17  ? 0.7558 0.8009 0.2645 0.2744  0.0169  0.0606  60  THR   A O   
97   O O   D THR   A 17  ? 0.7533 0.8014 0.2610 0.2771  0.0149  0.0610  60  THR   A O   
98   C CB  A THR   A 17  ? 0.7464 0.8052 0.2640 0.2763  -0.0051 0.0451  60  THR   A CB  
99   C CB  B THR   A 17  ? 0.7381 0.7960 0.2599 0.2726  -0.0084 0.0400  60  THR   A CB  
100  C CB  C THR   A 17  ? 0.7464 0.8052 0.2640 0.2763  -0.0051 0.0451  60  THR   A CB  
101  C CB  D THR   A 17  ? 0.7381 0.7960 0.2599 0.2726  -0.0084 0.0400  60  THR   A CB  
102  O OG1 A THR   A 17  ? 0.7583 0.8203 0.2660 0.2882  0.0065  0.0642  60  THR   A OG1 
103  O OG1 B THR   A 17  ? 0.7212 0.7776 0.2609 0.2631  -0.0156 0.0306  60  THR   A OG1 
104  O OG1 C THR   A 17  ? 0.7583 0.8203 0.2660 0.2882  0.0065  0.0642  60  THR   A OG1 
105  O OG1 D THR   A 17  ? 0.7212 0.7776 0.2609 0.2631  -0.0156 0.0306  60  THR   A OG1 
106  C CG2 A THR   A 17  ? 0.7389 0.7973 0.2760 0.2709  -0.0064 0.0475  60  THR   A CG2 
107  C CG2 B THR   A 17  ? 0.7603 0.8323 0.2577 0.2877  -0.0181 0.0321  60  THR   A CG2 
108  C CG2 C THR   A 17  ? 0.7389 0.7973 0.2760 0.2709  -0.0064 0.0475  60  THR   A CG2 
109  C CG2 D THR   A 17  ? 0.7603 0.8323 0.2577 0.2877  -0.0181 0.0321  60  THR   A CG2 
110  N N   . TRP   A 18  ? 0.7469 0.7933 0.2435 0.2698  -0.0043 0.0263  61  TRP   A N   
111  C CA  . TRP   A 18  ? 0.7654 0.8156 0.2418 0.2810  -0.0006 0.0280  61  TRP   A CA  
112  C C   . TRP   A 18  ? 0.8082 0.8733 0.2642 0.3004  -0.0007 0.0370  61  TRP   A C   
113  O O   . TRP   A 18  ? 0.8215 0.8967 0.2734 0.3060  -0.0114 0.0305  61  TRP   A O   
114  C CB  . TRP   A 18  ? 0.7532 0.8005 0.2230 0.2778  -0.0093 0.0081  61  TRP   A CB  
115  C CG  . TRP   A 18  ? 0.7691 0.8183 0.2204 0.2879  -0.0041 0.0092  61  TRP   A CG  
116  C CD1 . TRP   A 18  ? 0.7803 0.8416 0.2069 0.3050  -0.0066 0.0078  61  TRP   A CD1 
117  C CD2 . TRP   A 18  ? 0.7553 0.7949 0.2104 0.2826  0.0042  0.0116  61  TRP   A CD2 
118  N NE1 . TRP   A 18  ? 0.7901 0.8488 0.2050 0.3105  0.0010  0.0096  61  TRP   A NE1 
119  C CE2 . TRP   A 18  ? 0.7761 0.8219 0.2092 0.2970  0.0075  0.0119  61  TRP   A CE2 
120  C CE3 . TRP   A 18  ? 0.7313 0.7588 0.2055 0.2679  0.0092  0.0139  61  TRP   A CE3 
121  C CZ2 . TRP   A 18  ? 0.7814 0.8214 0.2136 0.2970  0.0160  0.0145  61  TRP   A CZ2 
122  C CZ3 . TRP   A 18  ? 0.7330 0.7560 0.2058 0.2682  0.0163  0.0166  61  TRP   A CZ3 
123  C CH2 . TRP   A 18  ? 0.7595 0.7883 0.2129 0.2822  0.0200  0.0170  61  TRP   A CH2 
124  N N   A GLU   A 19  ? 0.8206 0.8879 0.2648 0.3110  0.0109  0.0519  62  GLU   A N   
125  N N   B GLU   A 19  ? 0.8206 0.8879 0.2648 0.3110  0.0109  0.0519  62  GLU   A N   
126  N N   C GLU   A 19  ? 0.8177 0.8846 0.2632 0.3105  0.0115  0.0531  62  GLU   A N   
127  N N   D GLU   A 19  ? 0.8177 0.8846 0.2632 0.3105  0.0115  0.0531  62  GLU   A N   
128  C CA  A GLU   A 19  ? 0.8524 0.9335 0.2747 0.3313  0.0135  0.0638  62  GLU   A CA  
129  C CA  B GLU   A 19  ? 0.8524 0.9335 0.2747 0.3313  0.0135  0.0638  62  GLU   A CA  
130  C CA  C GLU   A 19  ? 0.8491 0.9297 0.2713 0.3312  0.0142  0.0643  62  GLU   A CA  
131  C CA  D GLU   A 19  ? 0.8491 0.9297 0.2713 0.3312  0.0142  0.0643  62  GLU   A CA  
132  C C   A GLU   A 19  ? 0.8819 0.9677 0.2786 0.3435  0.0154  0.0599  62  GLU   A C   
133  C C   B GLU   A 19  ? 0.8819 0.9677 0.2786 0.3435  0.0154  0.0599  62  GLU   A C   
134  C C   C GLU   A 19  ? 0.8787 0.9638 0.2760 0.3421  0.0142  0.0574  62  GLU   A C   
135  C C   D GLU   A 19  ? 0.8787 0.9638 0.2760 0.3421  0.0142  0.0574  62  GLU   A C   
136  O O   A GLU   A 19  ? 0.8718 0.9501 0.2715 0.3411  0.0272  0.0671  62  GLU   A O   
137  O O   B GLU   A 19  ? 0.8718 0.9501 0.2715 0.3411  0.0272  0.0671  62  GLU   A O   
138  O O   C GLU   A 19  ? 0.8702 0.9468 0.2710 0.3377  0.0236  0.0601  62  GLU   A O   
139  O O   D GLU   A 19  ? 0.8702 0.9468 0.2710 0.3377  0.0236  0.0601  62  GLU   A O   
140  C CB  A GLU   A 19  ? 0.8478 0.9266 0.2812 0.3338  0.0287  0.0882  62  GLU   A CB  
141  C CB  B GLU   A 19  ? 0.8478 0.9266 0.2812 0.3338  0.0287  0.0882  62  GLU   A CB  
142  C CB  C GLU   A 19  ? 0.8455 0.9249 0.2739 0.3366  0.0309  0.0896  62  GLU   A CB  
143  C CB  D GLU   A 19  ? 0.8455 0.9249 0.2739 0.3366  0.0309  0.0896  62  GLU   A CB  
144  C CG  A GLU   A 19  ? 0.8322 0.9080 0.2880 0.3249  0.0267  0.0917  62  GLU   A CG  
145  C CG  B GLU   A 19  ? 0.8322 0.9080 0.2880 0.3249  0.0267  0.0917  62  GLU   A CG  
146  C CG  C GLU   A 19  ? 0.8714 0.9652 0.2766 0.3585  0.0333  0.1026  62  GLU   A CG  
147  C CG  D GLU   A 19  ? 0.8714 0.9652 0.2766 0.3585  0.0333  0.1026  62  GLU   A CG  
148  C CD  A GLU   A 19  ? 0.8430 0.9319 0.2905 0.3344  0.0141  0.0870  62  GLU   A CD  
149  C CD  B GLU   A 19  ? 0.8430 0.9319 0.2905 0.3344  0.0141  0.0870  62  GLU   A CD  
150  C CD  C GLU   A 19  ? 0.8792 0.9725 0.2821 0.3688  0.0525  0.1275  62  GLU   A CD  
151  C CD  D GLU   A 19  ? 0.8792 0.9725 0.2821 0.3688  0.0525  0.1275  62  GLU   A CD  
152  O OE1 A GLU   A 19  ? 0.8632 0.9654 0.2881 0.3536  0.0142  0.0956  62  GLU   A OE1 
153  O OE1 B GLU   A 19  ? 0.8632 0.9654 0.2881 0.3536  0.0142  0.0956  62  GLU   A OE1 
154  O OE1 C GLU   A 19  ? 0.8634 0.9454 0.2902 0.3573  0.0647  0.1374  62  GLU   A OE1 
155  O OE1 D GLU   A 19  ? 0.8634 0.9454 0.2902 0.3573  0.0647  0.1374  62  GLU   A OE1 
156  O OE2 A GLU   A 19  ? 0.8220 0.9084 0.2856 0.3230  0.0044  0.0750  62  GLU   A OE2 
157  O OE2 B GLU   A 19  ? 0.8220 0.9084 0.2856 0.3230  0.0044  0.0750  62  GLU   A OE2 
158  O OE2 C GLU   A 19  ? 0.9062 1.0111 0.2835 0.3887  0.0555  0.1368  62  GLU   A OE2 
159  O OE2 D GLU   A 19  ? 0.9062 1.0111 0.2835 0.3887  0.0555  0.1368  62  GLU   A OE2 
160  N N   . LYS   A 20  ? 0.9189 1.0177 0.2915 0.3569  0.0044  0.0491  63  LYS   A N   
161  C CA  . LYS   A 20  ? 0.9703 1.0743 0.3157 0.3696  0.0050  0.0421  63  LYS   A CA  
162  C C   . LYS   A 20  ? 0.9897 1.0976 0.3211 0.3846  0.0216  0.0656  63  LYS   A C   
163  O O   . LYS   A 20  ? 1.0057 1.1191 0.3382 0.3918  0.0266  0.0833  63  LYS   A O   
164  C CB  . LYS   A 20  ? 1.0423 1.1604 0.3666 0.3796  -0.0119 0.0233  63  LYS   A CB  
165  C CG  . LYS   A 20  ? 1.0727 1.1854 0.4113 0.3648  -0.0263 -0.0022 63  LYS   A CG  
166  C CD  . LYS   A 20  ? 1.1300 1.2589 0.4564 0.3726  -0.0445 -0.0194 63  LYS   A CD  
167  C CE  . LYS   A 20  ? 1.1591 1.2836 0.4945 0.3613  -0.0573 -0.0476 63  LYS   A CE  
168  N NZ  . LYS   A 20  ? 1.1661 1.3001 0.5144 0.3569  -0.0732 -0.0600 63  LYS   A NZ  
169  N N   . ASP   A 21  ? 1.0194 1.1235 0.3409 0.3886  0.0313  0.0671  64  ASP   A N   
170  C CA  . ASP   A 21  ? 1.0736 1.1802 0.3852 0.4020  0.0498  0.0905  64  ASP   A CA  
171  C C   . ASP   A 21  ? 1.0463 1.1461 0.3857 0.3936  0.0616  0.1117  64  ASP   A C   
172  O O   . ASP   A 21  ? 1.0394 1.1453 0.3718 0.4068  0.0722  0.1325  64  ASP   A O   
173  C CB  . ASP   A 21  ? 1.1627 1.2854 0.4402 0.4259  0.0497  0.0981  64  ASP   A CB  
174  C CG  . ASP   A 21  ? 1.2305 1.3637 0.4756 0.4379  0.0371  0.0773  64  ASP   A CG  
175  O OD1 . ASP   A 21  ? 1.2460 1.3829 0.4659 0.4527  0.0469  0.0815  64  ASP   A OD1 
176  O OD2 . ASP   A 21  ? 1.2880 1.4267 0.5326 0.4336  0.0180  0.0574  64  ASP   A OD2 
177  N N   . ALA   A 22  ? 0.9767 1.0642 0.3461 0.3731  0.0609  0.1072  65  ALA   A N   
178  C CA  . ALA   A 22  ? 0.9648 1.0437 0.3600 0.3648  0.0770  0.1257  65  ALA   A CA  
179  C C   . ALA   A 22  ? 0.9655 1.0455 0.3527 0.3749  0.0934  0.1390  65  ALA   A C   
180  O O   . ALA   A 22  ? 0.9983 1.0793 0.3708 0.3775  0.0882  0.1254  65  ALA   A O   
181  C CB  . ALA   A 22  ? 0.9326 0.9987 0.3564 0.3414  0.0724  0.1140  65  ALA   A CB  
182  N N   . GLU   A 23  ? 0.9476 1.0242 0.3528 0.3743  0.1112  0.1600  66  GLU   A N   
183  C CA  . GLU   A 23  ? 0.9547 1.0280 0.3701 0.3739  0.1274  0.1702  66  GLU   A CA  
184  C C   . GLU   A 23  ? 0.9187 0.9847 0.3477 0.3580  0.1203  0.1532  66  GLU   A C   
185  O O   . GLU   A 23  ? 0.8383 0.8981 0.2839 0.3422  0.1095  0.1423  66  GLU   A O   
186  C CB  . GLU   A 23  ? 0.9993 1.0676 0.4457 0.3667  0.1426  0.1897  66  GLU   A CB  
187  C CG  . GLU   A 23  ? 1.0497 1.1170 0.5090 0.3678  0.1604  0.2021  66  GLU   A CG  
188  C CD  . GLU   A 23  ? 1.0990 1.1603 0.5967 0.3553  0.1733  0.2160  66  GLU   A CD  
189  O OE1 . GLU   A 23  ? 1.1305 1.1886 0.6413 0.3511  0.1739  0.2226  66  GLU   A OE1 
190  O OE2 . GLU   A 23  ? 1.1282 1.1883 0.6440 0.3498  0.1829  0.2195  66  GLU   A OE2 
191  N N   . VAL   A 24  ? 0.8998 0.9668 0.3208 0.3635  0.1268  0.1516  67  VAL   A N   
192  C CA  . VAL   A 24  ? 0.8863 0.9472 0.3184 0.3512  0.1207  0.1367  67  VAL   A CA  
193  C C   . VAL   A 24  ? 0.8663 0.9261 0.3199 0.3483  0.1366  0.1500  67  VAL   A C   
194  O O   . VAL   A 24  ? 0.8754 0.9406 0.3181 0.3628  0.1506  0.1625  67  VAL   A O   
195  C CB  . VAL   A 24  ? 0.9083 0.9711 0.3127 0.3600  0.1116  0.1188  67  VAL   A CB  
196  C CG1 . VAL   A 24  ? 0.8868 0.9423 0.3037 0.3485  0.1069  0.1055  67  VAL   A CG1 
197  C CG2 . VAL   A 24  ? 0.9269 0.9927 0.3128 0.3628  0.0955  0.1050  67  VAL   A CG2 
198  N N   . THR   A 25  ? 0.8207 0.8747 0.3040 0.3305  0.1345  0.1473  68  THR   A N   
199  C CA  . THR   A 25  ? 0.8082 0.8631 0.3179 0.3257  0.1483  0.1597  68  THR   A CA  
200  C C   . THR   A 25  ? 0.7861 0.8360 0.3215 0.3067  0.1399  0.1501  68  THR   A C   
201  O O   . THR   A 25  ? 0.7559 0.8000 0.2894 0.2962  0.1243  0.1349  68  THR   A O   
202  C CB  . THR   A 25  ? 0.8153 0.8724 0.3390 0.3283  0.1624  0.1797  68  THR   A CB  
203  O OG1 . THR   A 25  ? 0.8356 0.8960 0.3794 0.3292  0.1784  0.1926  68  THR   A OG1 
204  C CG2 . THR   A 25  ? 0.8009 0.8528 0.3475 0.3129  0.1572  0.1794  68  THR   A CG2 
205  N N   . GLY   A 26  ? 0.7861 0.8388 0.3458 0.3021  0.1499  0.1587  69  GLY   A N   
206  C CA  . GLY   A 26  ? 0.7714 0.8220 0.3548 0.2862  0.1428  0.1512  69  GLY   A CA  
207  C C   . GLY   A 26  ? 0.7866 0.8380 0.3612 0.2911  0.1405  0.1433  69  GLY   A C   
208  O O   . GLY   A 26  ? 0.8145 0.8650 0.3604 0.3040  0.1391  0.1371  69  GLY   A O   
209  N N   . ASN   A 27  ? 0.7713 0.8250 0.3701 0.2819  0.1404  0.1434  70  ASN   A N   
210  C CA  . ASN   A 27  ? 0.7710 0.8248 0.3664 0.2849  0.1376  0.1360  70  ASN   A CA  
211  C C   . ASN   A 27  ? 0.7379 0.7853 0.3383 0.2712  0.1217  0.1226  70  ASN   A C   
212  O O   . ASN   A 27  ? 0.7152 0.7582 0.3168 0.2615  0.1136  0.1185  70  ASN   A O   
213  C CB  . ASN   A 27  ? 0.7867 0.8495 0.4042 0.2881  0.1511  0.1482  70  ASN   A CB  
214  C CG  . ASN   A 27  ? 0.7668 0.8344 0.4193 0.2726  0.1491  0.1522  70  ASN   A CG  
215  O OD1 . ASN   A 27  ? 0.7569 0.8237 0.4204 0.2639  0.1484  0.1553  70  ASN   A OD1 
216  N ND2 . ASN   A 27  ? 0.7781 0.8514 0.4487 0.2694  0.1483  0.1519  70  ASN   A ND2 
217  N N   . SER   A 28  ? 0.7354 0.7817 0.3368 0.2717  0.1179  0.1162  71  SER   A N   
218  C CA  . SER   A 28  ? 0.7392 0.7779 0.3399 0.2621  0.1040  0.1036  71  SER   A CA  
219  C C   . SER   A 28  ? 0.7303 0.7737 0.3544 0.2552  0.1024  0.1062  71  SER   A C   
220  O O   . SER   A 28  ? 0.7373 0.7771 0.3580 0.2577  0.0989  0.1004  71  SER   A O   
221  C CB  . SER   A 28  ? 0.7548 0.7854 0.3312 0.2704  0.0996  0.0913  71  SER   A CB  
222  O OG  . SER   A 28  ? 0.7993 0.8275 0.3540 0.2766  0.0988  0.0874  71  SER   A OG  
223  N N   . PRO   A 29  ? 0.7171 0.7688 0.3664 0.2461  0.1042  0.1146  72  PRO   A N   
224  C CA  . PRO   A 29  ? 0.7085 0.7688 0.3814 0.2418  0.1034  0.1184  72  PRO   A CA  
225  C C   . PRO   A 29  ? 0.6946 0.7492 0.3663 0.2331  0.0898  0.1092  72  PRO   A C   
226  O O   . PRO   A 29  ? 0.6728 0.7196 0.3355 0.2252  0.0816  0.1022  72  PRO   A O   
227  C CB  . PRO   A 29  ? 0.6965 0.7668 0.3952 0.2337  0.1084  0.1276  72  PRO   A CB  
228  C CG  . PRO   A 29  ? 0.6970 0.7595 0.3855 0.2275  0.1048  0.1239  72  PRO   A CG  
229  C CD  . PRO   A 29  ? 0.7188 0.7728 0.3770 0.2397  0.1071  0.1202  72  PRO   A CD  
230  N N   . ARG   A 30  ? 0.7167 0.7748 0.3962 0.2362  0.0887  0.1100  73  ARG   A N   
231  C CA  . ARG   A 30  ? 0.7420 0.7972 0.4245 0.2293  0.0773  0.1049  73  ARG   A CA  
232  C C   . ARG   A 30  ? 0.6964 0.7662 0.4062 0.2205  0.0738  0.1112  73  ARG   A C   
233  O O   . ARG   A 30  ? 0.6688 0.7502 0.3959 0.2257  0.0793  0.1187  73  ARG   A O   
234  C CB  . ARG   A 30  ? 0.8116 0.8611 0.4859 0.2392  0.0784  0.1021  73  ARG   A CB  
235  C CG  . ARG   A 30  ? 0.8798 0.9146 0.5279 0.2462  0.0793  0.0923  73  ARG   A CG  
236  C CD  . ARG   A 30  ? 0.9541 0.9831 0.5961 0.2573  0.0833  0.0892  73  ARG   A CD  
237  N NE  . ARG   A 30  ? 1.0208 1.0374 0.6390 0.2647  0.0850  0.0782  73  ARG   A NE  
238  C CZ  . ARG   A 30  ? 1.0138 1.0171 0.6194 0.2609  0.0774  0.0667  73  ARG   A CZ  
239  N NH1 . ARG   A 30  ? 1.0210 1.0207 0.6337 0.2501  0.0687  0.0660  73  ARG   A NH1 
240  N NH2 . ARG   A 30  ? 0.9569 0.9513 0.5431 0.2677  0.0787  0.0558  73  ARG   A NH2 
241  N N   . LEU   A 31  ? 0.6543 0.7242 0.3683 0.2077  0.0649  0.1077  74  LEU   A N   
242  C CA  . LEU   A 31  ? 0.6361 0.7213 0.3763 0.1984  0.0611  0.1117  74  LEU   A CA  
243  C C   . LEU   A 31  ? 0.6128 0.6977 0.3512 0.1907  0.0478  0.1068  74  LEU   A C   
244  O O   . LEU   A 31  ? 0.6028 0.6749 0.3233 0.1861  0.0422  0.0996  74  LEU   A O   
245  C CB  . LEU   A 31  ? 0.6271 0.7143 0.3760 0.1902  0.0644  0.1122  74  LEU   A CB  
246  C CG  . LEU   A 31  ? 0.6336 0.7225 0.3864 0.1979  0.0787  0.1196  74  LEU   A CG  
247  C CD1 . LEU   A 31  ? 0.6273 0.7140 0.3855 0.1897  0.0815  0.1195  74  LEU   A CD1 
248  C CD2 . LEU   A 31  ? 0.6326 0.7374 0.4111 0.2025  0.0864  0.1289  74  LEU   A CD2 
249  N N   . ASP   A 32  ? 0.6111 0.7104 0.3679 0.1901  0.0434  0.1111  75  ASP   A N   
250  C CA  . ASP   A 32  ? 0.6173 0.7214 0.3760 0.1820  0.0304  0.1080  75  ASP   A CA  
251  C C   . ASP   A 32  ? 0.5926 0.7026 0.3613 0.1685  0.0257  0.1036  75  ASP   A C   
252  O O   . ASP   A 32  ? 0.5850 0.7094 0.3785 0.1652  0.0296  0.1070  75  ASP   A O   
253  C CB  . ASP   A 32  ? 0.6409 0.7614 0.4178 0.1868  0.0271  0.1147  75  ASP   A CB  
254  C CG  . ASP   A 32  ? 0.6805 0.7928 0.4467 0.1998  0.0311  0.1182  75  ASP   A CG  
255  O OD1 . ASP   A 32  ? 0.7111 0.8054 0.4541 0.2015  0.0300  0.1132  75  ASP   A OD1 
256  O OD2 . ASP   A 32  ? 0.7301 0.8538 0.5129 0.2078  0.0362  0.1254  75  ASP   A OD2 
257  N N   . VAL   A 33  ? 0.5820 0.6815 0.3341 0.1609  0.0185  0.0961  76  VAL   A N   
258  C CA  . VAL   A 33  ? 0.5702 0.6728 0.3293 0.1477  0.0143  0.0901  76  VAL   A CA  
259  C C   . VAL   A 33  ? 0.5702 0.6731 0.3194 0.1408  0.0018  0.0845  76  VAL   A C   
260  O O   . VAL   A 33  ? 0.5648 0.6598 0.2966 0.1464  -0.0018 0.0854  76  VAL   A O   
261  C CB  . VAL   A 33  ? 0.5689 0.6574 0.3184 0.1450  0.0216  0.0865  76  VAL   A CB  
262  C CG1 . VAL   A 33  ? 0.5729 0.6601 0.3263 0.1543  0.0343  0.0931  76  VAL   A CG1 
263  C CG2 . VAL   A 33  ? 0.5733 0.6435 0.2959 0.1448  0.0185  0.0804  76  VAL   A CG2 
264  N N   . ALA   A 34  ? 0.5593 0.6710 0.3197 0.1294  -0.0036 0.0789  77  ALA   A N   
265  C CA  . ALA   A 34  ? 0.5584 0.6719 0.3092 0.1215  -0.0151 0.0723  77  ALA   A CA  
266  C C   . ALA   A 34  ? 0.5503 0.6536 0.2960 0.1109  -0.0136 0.0633  77  ALA   A C   
267  O O   . ALA   A 34  ? 0.5489 0.6534 0.3103 0.1075  -0.0064 0.0629  77  ALA   A O   
268  C CB  . ALA   A 34  ? 0.5641 0.7010 0.3355 0.1182  -0.0240 0.0726  77  ALA   A CB  
269  N N   . LEU   A 35  ? 0.5532 0.6462 0.2783 0.1065  -0.0189 0.0573  78  LEU   A N   
270  C CA  . LEU   A 35  ? 0.5468 0.6292 0.2662 0.0967  -0.0172 0.0484  78  LEU   A CA  
271  C C   . LEU   A 35  ? 0.5521 0.6439 0.2708 0.0872  -0.0276 0.0403  78  LEU   A C   
272  O O   . LEU   A 35  ? 0.5608 0.6526 0.2624 0.0899  -0.0348 0.0410  78  LEU   A O   
273  C CB  . LEU   A 35  ? 0.5491 0.6105 0.2445 0.1003  -0.0132 0.0477  78  LEU   A CB  
274  C CG  . LEU   A 35  ? 0.5466 0.5957 0.2350 0.0917  -0.0107 0.0393  78  LEU   A CG  
275  C CD1 . LEU   A 35  ? 0.5384 0.5887 0.2451 0.0876  -0.0033 0.0383  78  LEU   A CD1 
276  C CD2 . LEU   A 35  ? 0.5485 0.5792 0.2159 0.0957  -0.0076 0.0388  78  LEU   A CD2 
277  N N   . ASP   A 36  ? 0.5454 0.6457 0.2828 0.0773  -0.0280 0.0332  79  ASP   A N   
278  C CA  . ASP   A 36  ? 0.5525 0.6642 0.2903 0.0679  -0.0388 0.0234  79  ASP   A CA  
279  C C   . ASP   A 36  ? 0.5556 0.6510 0.2737 0.0611  -0.0378 0.0144  79  ASP   A C   
280  O O   . ASP   A 36  ? 0.5349 0.6120 0.2434 0.0630  -0.0290 0.0159  79  ASP   A O   
281  C CB  . ASP   A 36  ? 0.5531 0.6833 0.3230 0.0602  -0.0406 0.0186  79  ASP   A CB  
282  C CG  . ASP   A 36  ? 0.5498 0.6719 0.3362 0.0516  -0.0310 0.0127  79  ASP   A CG  
283  O OD1 . ASP   A 36  ? 0.5524 0.6551 0.3235 0.0508  -0.0242 0.0110  79  ASP   A OD1 
284  O OD2 . ASP   A 36  ? 0.5517 0.6874 0.3679 0.0460  -0.0300 0.0101  79  ASP   A OD2 
285  N N   . GLU   A 37  ? 0.5685 0.6714 0.2797 0.0539  -0.0471 0.0050  80  GLU   A N   
286  C CA  . GLU   A 37  ? 0.5856 0.6740 0.2760 0.0480  -0.0463 -0.0036 80  GLU   A CA  
287  C C   . GLU   A 37  ? 0.5771 0.6548 0.2808 0.0398  -0.0368 -0.0107 80  GLU   A C   
288  O O   . GLU   A 37  ? 0.5802 0.6407 0.2680 0.0378  -0.0317 -0.0143 80  GLU   A O   
289  C CB  . GLU   A 37  ? 0.6089 0.7109 0.2893 0.0434  -0.0587 -0.0119 80  GLU   A CB  
290  C CG  . GLU   A 37  ? 0.6362 0.7243 0.2930 0.0381  -0.0577 -0.0206 80  GLU   A CG  
291  C CD  . GLU   A 37  ? 0.6638 0.7654 0.3065 0.0345  -0.0697 -0.0291 80  GLU   A CD  
292  O OE1 . GLU   A 37  ? 0.6834 0.7956 0.3383 0.0243  -0.0745 -0.0428 80  GLU   A OE1 
293  O OE2 . GLU   A 37  ? 0.6932 0.7958 0.3136 0.0424  -0.0746 -0.0219 80  GLU   A OE2 
294  N N   . SER   A 38  ? 0.5716 0.6582 0.3046 0.0357  -0.0333 -0.0117 81  SER   A N   
295  C CA  . SER   A 38  ? 0.5695 0.6454 0.3181 0.0291  -0.0226 -0.0162 81  SER   A CA  
296  C C   . SER   A 38  ? 0.5595 0.6221 0.3074 0.0378  -0.0113 -0.0046 81  SER   A C   
297  O O   . SER   A 38  ? 0.5587 0.6139 0.3211 0.0347  -0.0016 -0.0052 81  SER   A O   
298  C CB  . SER   A 38  ? 0.5762 0.6661 0.3578 0.0209  -0.0222 -0.0218 81  SER   A CB  
299  O OG  . SER   A 38  ? 0.6012 0.7066 0.3843 0.0135  -0.0345 -0.0333 81  SER   A OG  
300  N N   . GLY   A 39  ? 0.5571 0.6159 0.2878 0.0486  -0.0120 0.0047  82  GLY   A N   
301  C CA  . GLY   A 39  ? 0.5527 0.5992 0.2797 0.0572  -0.0024 0.0137  82  GLY   A CA  
302  C C   . GLY   A 39  ? 0.5509 0.6053 0.3004 0.0619  0.0045  0.0222  82  GLY   A C   
303  O O   . GLY   A 39  ? 0.5334 0.5781 0.2810 0.0682  0.0135  0.0284  82  GLY   A O   
304  N N   . ASP   A 40  ? 0.5602 0.6322 0.3292 0.0600  0.0005  0.0229  83  ASP   A N   
305  C CA  . ASP   A 40  ? 0.5666 0.6483 0.3600 0.0643  0.0076  0.0316  83  ASP   A CA  
306  C C   . ASP   A 40  ? 0.5575 0.6458 0.3430 0.0757  0.0046  0.0407  83  ASP   A C   
307  O O   . ASP   A 40  ? 0.5418 0.6402 0.3226 0.0756  -0.0057 0.0388  83  ASP   A O   
308  C CB  . ASP   A 40  ? 0.5842 0.6818 0.4091 0.0542  0.0060  0.0259  83  ASP   A CB  
309  C CG  . ASP   A 40  ? 0.6076 0.6973 0.4417 0.0426  0.0098  0.0156  83  ASP   A CG  
310  O OD1 . ASP   A 40  ? 0.6227 0.6975 0.4539 0.0444  0.0202  0.0188  83  ASP   A OD1 
311  O OD2 . ASP   A 40  ? 0.6526 0.7509 0.4947 0.0323  0.0017  0.0039  83  ASP   A OD2 
312  N N   . PHE   A 41  ? 0.5423 0.6249 0.3257 0.0859  0.0139  0.0503  84  PHE   A N   
313  C CA  . PHE   A 41  ? 0.5397 0.6283 0.3205 0.0975  0.0143  0.0594  84  PHE   A CA  
314  C C   . PHE   A 41  ? 0.5439 0.6510 0.3550 0.0974  0.0169  0.0644  84  PHE   A C   
315  O O   . PHE   A 41  ? 0.5426 0.6527 0.3757 0.0918  0.0240  0.0642  84  PHE   A O   
316  C CB  . PHE   A 41  ? 0.5304 0.6061 0.2972 0.1083  0.0239  0.0661  84  PHE   A CB  
317  C CG  . PHE   A 41  ? 0.5241 0.5837 0.2622 0.1111  0.0208  0.0623  84  PHE   A CG  
318  C CD1 . PHE   A 41  ? 0.5244 0.5824 0.2470 0.1166  0.0145  0.0627  84  PHE   A CD1 
319  C CD2 . PHE   A 41  ? 0.5259 0.5722 0.2548 0.1086  0.0248  0.0587  84  PHE   A CD2 
320  C CE1 . PHE   A 41  ? 0.5279 0.5709 0.2275 0.1187  0.0128  0.0590  84  PHE   A CE1 
321  C CE2 . PHE   A 41  ? 0.5274 0.5601 0.2332 0.1110  0.0222  0.0549  84  PHE   A CE2 
322  C CZ  . PHE   A 41  ? 0.5270 0.5578 0.2187 0.1158  0.0165  0.0548  84  PHE   A CZ  
323  N N   . SER   A 42  ? 0.5588 0.6774 0.3726 0.1040  0.0123  0.0693  85  SER   A N   
324  C CA  . SER   A 42  ? 0.5704 0.7084 0.4143 0.1053  0.0145  0.0749  85  SER   A CA  
325  C C   . SER   A 42  ? 0.5856 0.7258 0.4233 0.1193  0.0175  0.0848  85  SER   A C   
326  O O   . SER   A 42  ? 0.5808 0.7106 0.3923 0.1260  0.0136  0.0851  85  SER   A O   
327  C CB  . SER   A 42  ? 0.5808 0.7369 0.4415 0.0957  0.0021  0.0676  85  SER   A CB  
328  O OG  . SER   A 42  ? 0.5832 0.7406 0.4229 0.0981  -0.0102 0.0654  85  SER   A OG  
329  N N   . LEU   A 43  ? 0.6078 0.7598 0.4698 0.1240  0.0258  0.0927  86  LEU   A N   
330  C CA  . LEU   A 43  ? 0.6344 0.7892 0.4933 0.1377  0.0302  0.1020  86  LEU   A CA  
331  C C   . LEU   A 43  ? 0.6428 0.8151 0.5123 0.1380  0.0184  0.1022  86  LEU   A C   
332  O O   . LEU   A 43  ? 0.6314 0.8228 0.5301 0.1311  0.0146  0.1009  86  LEU   A O   
333  C CB  . LEU   A 43  ? 0.6431 0.8036 0.5236 0.1434  0.0453  0.1111  86  LEU   A CB  
334  C CG  . LEU   A 43  ? 0.6564 0.7995 0.5206 0.1486  0.0582  0.1143  86  LEU   A CG  
335  C CD1 . LEU   A 43  ? 0.6731 0.8237 0.5622 0.1524  0.0736  0.1239  86  LEU   A CD1 
336  C CD2 . LEU   A 43  ? 0.6700 0.7994 0.5022 0.1609  0.0591  0.1158  86  LEU   A CD2 
337  N N   . VAL   A 44  ? 0.6808 0.8469 0.5287 0.1464  0.0137  0.1042  87  VAL   A N   
338  C CA  . VAL   A 44  ? 0.7202 0.9016 0.5760 0.1519  0.0052  0.1084  87  VAL   A CA  
339  C C   . VAL   A 44  ? 0.7667 0.9562 0.6402 0.1630  0.0160  0.1185  87  VAL   A C   
340  O O   . VAL   A 44  ? 0.8181 0.9931 0.6787 0.1713  0.0281  0.1221  87  VAL   A O   
341  C CB  . VAL   A 44  ? 0.7200 0.8872 0.5449 0.1574  -0.0009 0.1076  87  VAL   A CB  
342  C CG1 . VAL   A 44  ? 0.7279 0.9083 0.5590 0.1655  -0.0077 0.1141  87  VAL   A CG1 
343  C CG2 . VAL   A 44  ? 0.7174 0.8757 0.5239 0.1470  -0.0096 0.0982  87  VAL   A CG2 
344  N N   . GLU   A 45  ? 0.8178 1.0300 0.7194 0.1639  0.0120  0.1227  88  GLU   A N   
345  C CA  . GLU   A 45  ? 0.8700 1.0901 0.7874 0.1763  0.0218  0.1331  88  GLU   A CA  
346  C C   . GLU   A 45  ? 0.8851 1.1247 0.8163 0.1807  0.0108  0.1371  88  GLU   A C   
347  O O   . GLU   A 45  ? 0.8719 1.1073 0.7836 0.1831  0.0004  0.1360  88  GLU   A O   
348  C CB  . GLU   A 45  ? 0.8882 1.1183 0.8357 0.1736  0.0339  0.1366  88  GLU   A CB  
349  C CG  . GLU   A 45  ? 0.9200 1.1313 0.8536 0.1716  0.0460  0.1350  88  GLU   A CG  
350  C CD  . GLU   A 45  ? 0.9246 1.1231 0.8436 0.1855  0.0615  0.1424  88  GLU   A CD  
351  O OE1 . GLU   A 45  ? 0.9302 1.1236 0.8336 0.1960  0.0605  0.1448  88  GLU   A OE1 
352  O OE2 . GLU   A 45  ? 0.9681 1.1624 0.8926 0.1863  0.0749  0.1460  88  GLU   A OE2 
353  N N   . GLY   B 7   ? 0.8245 0.8277 0.6304 0.0792  0.0572  -0.0635 16  GLY   B N   
354  C CA  . GLY   B 7   ? 0.8310 0.8302 0.6313 0.0855  0.0578  -0.0543 16  GLY   B CA  
355  C C   . GLY   B 7   ? 0.8047 0.8044 0.5914 0.0925  0.0526  -0.0505 16  GLY   B C   
356  O O   . GLY   B 7   ? 0.8344 0.8368 0.6156 0.0911  0.0482  -0.0556 16  GLY   B O   
357  N N   . GLU   B 8   ? 0.7637 0.7613 0.5453 0.0996  0.0530  -0.0421 17  GLU   B N   
358  C CA  . GLU   B 8   ? 0.7221 0.7210 0.4907 0.1072  0.0481  -0.0386 17  GLU   B CA  
359  C C   . GLU   B 8   ? 0.6803 0.6770 0.4365 0.1016  0.0439  -0.0427 17  GLU   B C   
360  O O   . GLU   B 8   ? 0.6729 0.6663 0.4264 0.0977  0.0454  -0.0410 17  GLU   B O   
361  C CB  . GLU   B 8   ? 0.7495 0.7482 0.5170 0.1166  0.0503  -0.0283 17  GLU   B CB  
362  C CG  . GLU   B 8   ? 0.7593 0.7613 0.5144 0.1258  0.0454  -0.0253 17  GLU   B CG  
363  C CD  . GLU   B 8   ? 0.7846 0.7890 0.5398 0.1364  0.0480  -0.0145 17  GLU   B CD  
364  O OE1 . GLU   B 8   ? 0.7675 0.7690 0.5299 0.1355  0.0534  -0.0087 17  GLU   B OE1 
365  O OE2 . GLU   B 8   ? 0.8594 0.8692 0.6080 0.1457  0.0446  -0.0119 17  GLU   B OE2 
366  N N   A THR   B 9   ? 0.6726 0.6712 0.4220 0.1013  0.0386  -0.0477 18  THR   B N   
367  N N   B THR   B 9   ? 0.6697 0.6683 0.4193 0.1012  0.0386  -0.0477 18  THR   B N   
368  N N   C THR   B 9   ? 0.6726 0.6712 0.4220 0.1013  0.0386  -0.0477 18  THR   B N   
369  N N   D THR   B 9   ? 0.6697 0.6683 0.4193 0.1012  0.0386  -0.0477 18  THR   B N   
370  C CA  A THR   B 9   ? 0.6666 0.6626 0.4057 0.0955  0.0343  -0.0520 18  THR   B CA  
371  C CA  B THR   B 9   ? 0.6615 0.6576 0.4009 0.0954  0.0342  -0.0522 18  THR   B CA  
372  C CA  C THR   B 9   ? 0.6666 0.6626 0.4057 0.0955  0.0343  -0.0520 18  THR   B CA  
373  C CA  D THR   B 9   ? 0.6615 0.6576 0.4009 0.0954  0.0342  -0.0522 18  THR   B CA  
374  C C   A THR   B 9   ? 0.6607 0.6573 0.3887 0.1029  0.0287  -0.0509 18  THR   B C   
375  C C   B THR   B 9   ? 0.6577 0.6536 0.3853 0.1033  0.0293  -0.0498 18  THR   B C   
376  C C   C THR   B 9   ? 0.6607 0.6573 0.3887 0.1029  0.0287  -0.0509 18  THR   B C   
377  C C   D THR   B 9   ? 0.6577 0.6536 0.3853 0.1033  0.0293  -0.0498 18  THR   B C   
378  O O   A THR   B 9   ? 0.6650 0.6590 0.3853 0.0989  0.0246  -0.0548 18  THR   B O   
379  O O   B THR   B 9   ? 0.6585 0.6508 0.3773 0.1001  0.0262  -0.0512 18  THR   B O   
380  O O   C THR   B 9   ? 0.6650 0.6590 0.3853 0.0989  0.0246  -0.0548 18  THR   B O   
381  O O   D THR   B 9   ? 0.6585 0.6508 0.3773 0.1001  0.0262  -0.0512 18  THR   B O   
382  C CB  A THR   B 9   ? 0.6671 0.6647 0.4101 0.0865  0.0331  -0.0602 18  THR   B CB  
383  C CB  B THR   B 9   ? 0.6594 0.6577 0.4021 0.0877  0.0325  -0.0605 18  THR   B CB  
384  C CB  C THR   B 9   ? 0.6671 0.6647 0.4101 0.0865  0.0331  -0.0602 18  THR   B CB  
385  C CB  D THR   B 9   ? 0.6594 0.6577 0.4021 0.0877  0.0325  -0.0605 18  THR   B CB  
386  O OG1 A THR   B 9   ? 0.6669 0.6669 0.4226 0.0838  0.0381  -0.0616 18  THR   B OG1 
387  O OG1 B THR   B 9   ? 0.6562 0.6594 0.4029 0.0932  0.0308  -0.0621 18  THR   B OG1 
388  O OG1 C THR   B 9   ? 0.6669 0.6669 0.4226 0.0838  0.0381  -0.0616 18  THR   B OG1 
389  O OG1 D THR   B 9   ? 0.6562 0.6594 0.4029 0.0932  0.0308  -0.0621 18  THR   B OG1 
390  C CG2 A THR   B 9   ? 0.6681 0.6625 0.4049 0.0776  0.0318  -0.0633 18  THR   B CG2 
391  C CG2 B THR   B 9   ? 0.6571 0.6559 0.4093 0.0790  0.0371  -0.0638 18  THR   B CG2 
392  C CG2 C THR   B 9   ? 0.6681 0.6625 0.4049 0.0776  0.0318  -0.0633 18  THR   B CG2 
393  C CG2 D THR   B 9   ? 0.6571 0.6559 0.4093 0.0790  0.0371  -0.0638 18  THR   B CG2 
394  N N   . THR   B 10  ? 0.6537 0.6538 0.3813 0.1135  0.0286  -0.0459 19  THR   B N   
395  C CA  . THR   B 10  ? 0.6357 0.6378 0.3525 0.1219  0.0234  -0.0448 19  THR   B CA  
396  C C   . THR   B 10  ? 0.6084 0.6058 0.3156 0.1217  0.0225  -0.0420 19  THR   B C   
397  O O   . THR   B 10  ? 0.6231 0.6188 0.3323 0.1223  0.0269  -0.0359 19  THR   B O   
398  C CB  . THR   B 10  ? 0.6348 0.6432 0.3531 0.1339  0.0246  -0.0382 19  THR   B CB  
399  O OG1 . THR   B 10  ? 0.6404 0.6529 0.3690 0.1345  0.0264  -0.0395 19  THR   B OG1 
400  C CG2 . THR   B 10  ? 0.6401 0.6531 0.3482 0.1424  0.0187  -0.0393 19  THR   B CG2 
401  N N   . ASP   B 11  ? 0.5875 0.5830 0.2856 0.1213  0.0169  -0.0464 20  ASP   B N   
402  C CA  . ASP   B 11  ? 0.5853 0.5770 0.2735 0.1232  0.0150  -0.0440 20  ASP   B CA  
403  C C   . ASP   B 11  ? 0.5901 0.5854 0.2759 0.1334  0.0175  -0.0356 20  ASP   B C   
404  O O   . ASP   B 11  ? 0.5904 0.5923 0.2786 0.1416  0.0179  -0.0330 20  ASP   B O   
405  C CB  . ASP   B 11  ? 0.5951 0.5858 0.2749 0.1248  0.0081  -0.0499 20  ASP   B CB  
406  C CG  . ASP   B 11  ? 0.6060 0.5915 0.2864 0.1143  0.0054  -0.0569 20  ASP   B CG  
407  O OD1 . ASP   B 11  ? 0.5809 0.5646 0.2675 0.1055  0.0089  -0.0576 20  ASP   B OD1 
408  O OD2 . ASP   B 11  ? 0.6243 0.6079 0.2989 0.1152  -0.0001 -0.0617 20  ASP   B OD2 
409  N N   . GLY   B 12  ? 0.5697 0.5618 0.2506 0.1335  0.0190  -0.0313 21  GLY   B N   
410  C CA  . GLY   B 12  ? 0.5616 0.5576 0.2391 0.1433  0.0210  -0.0232 21  GLY   B CA  
411  C C   . GLY   B 12  ? 0.5496 0.5424 0.2293 0.1394  0.0259  -0.0179 21  GLY   B C   
412  O O   . GLY   B 12  ? 0.5335 0.5209 0.2157 0.1293  0.0269  -0.0213 21  GLY   B O   
413  N N   . VAL   B 13  ? 0.5331 0.5298 0.2121 0.1471  0.0290  -0.0098 22  VAL   B N   
414  C CA  . VAL   B 13  ? 0.5260 0.5209 0.2076 0.1446  0.0339  -0.0039 22  VAL   B CA  
415  C C   . VAL   B 13  ? 0.5252 0.5214 0.2207 0.1430  0.0404  0.0007  22  VAL   B C   
416  O O   . VAL   B 13  ? 0.5385 0.5387 0.2387 0.1483  0.0411  0.0027  22  VAL   B O   
417  C CB  . VAL   B 13  ? 0.5262 0.5246 0.1985 0.1534  0.0329  0.0015  22  VAL   B CB  
418  C CG1 . VAL   B 13  ? 0.5252 0.5323 0.1972 0.1656  0.0339  0.0083  22  VAL   B CG1 
419  C CG2 . VAL   B 13  ? 0.5240 0.5208 0.1981 0.1502  0.0372  0.0064  22  VAL   B CG2 
420  N N   . TYR   B 14  ? 0.5187 0.5116 0.2215 0.1353  0.0448  0.0014  23  TYR   B N   
421  C CA  . TYR   B 14  ? 0.5156 0.5085 0.2335 0.1320  0.0511  0.0043  23  TYR   B CA  
422  C C   . TYR   B 14  ? 0.5144 0.5070 0.2369 0.1303  0.0559  0.0098  23  TYR   B C   
423  O O   . TYR   B 14  ? 0.5115 0.5025 0.2274 0.1266  0.0545  0.0081  23  TYR   B O   
424  C CB  . TYR   B 14  ? 0.5138 0.5032 0.2390 0.1215  0.0513  -0.0040 23  TYR   B CB  
425  C CG  . TYR   B 14  ? 0.5154 0.5058 0.2401 0.1224  0.0478  -0.0092 23  TYR   B CG  
426  C CD1 . TYR   B 14  ? 0.5176 0.5082 0.2305 0.1247  0.0415  -0.0133 23  TYR   B CD1 
427  C CD2 . TYR   B 14  ? 0.5193 0.5104 0.2566 0.1206  0.0510  -0.0104 23  TYR   B CD2 
428  C CE1 . TYR   B 14  ? 0.5233 0.5156 0.2367 0.1252  0.0383  -0.0185 23  TYR   B CE1 
429  C CE2 . TYR   B 14  ? 0.5263 0.5191 0.2638 0.1211  0.0479  -0.0155 23  TYR   B CE2 
430  C CZ  . TYR   B 14  ? 0.5322 0.5259 0.2577 0.1234  0.0415  -0.0195 23  TYR   B CZ  
431  O OH  . TYR   B 14  ? 0.5544 0.5506 0.2816 0.1238  0.0387  -0.0246 23  TYR   B OH  
432  N N   . ARG   B 15  ? 0.5195 0.5136 0.2542 0.1325  0.0617  0.0163  24  ARG   B N   
433  C CA  . ARG   B 15  ? 0.5216 0.5153 0.2651 0.1293  0.0673  0.0210  24  ARG   B CA  
434  C C   . ARG   B 15  ? 0.5199 0.5101 0.2742 0.1177  0.0695  0.0135  24  ARG   B C   
435  O O   . ARG   B 15  ? 0.5095 0.4983 0.2707 0.1148  0.0696  0.0087  24  ARG   B O   
436  C CB  . ARG   B 15  ? 0.5282 0.5247 0.2824 0.1360  0.0729  0.0311  24  ARG   B CB  
437  C CG  . ARG   B 15  ? 0.5356 0.5377 0.2798 0.1483  0.0711  0.0390  24  ARG   B CG  
438  C CD  . ARG   B 15  ? 0.5450 0.5501 0.3014 0.1544  0.0772  0.0499  24  ARG   B CD  
439  N NE  . ARG   B 15  ? 0.5549 0.5672 0.3019 0.1668  0.0755  0.0573  24  ARG   B NE  
440  C CZ  . ARG   B 15  ? 0.5605 0.5785 0.3005 0.1738  0.0763  0.0652  24  ARG   B CZ  
441  N NH1 . ARG   B 15  ? 0.5553 0.5723 0.2979 0.1696  0.0793  0.0674  24  ARG   B NH1 
442  N NH2 . ARG   B 15  ? 0.5690 0.5949 0.2998 0.1853  0.0742  0.0706  24  ARG   B NH2 
443  N N   . VAL   B 16  ? 0.5265 0.5164 0.2830 0.1123  0.0717  0.0132  25  VAL   B N   
444  C CA  . VAL   B 16  ? 0.5254 0.5140 0.2935 0.1018  0.0746  0.0066  25  VAL   B CA  
445  C C   . VAL   B 16  ? 0.5306 0.5199 0.3143 0.1014  0.0813  0.0122  25  VAL   B C   
446  O O   . VAL   B 16  ? 0.5373 0.5287 0.3190 0.1034  0.0829  0.0178  25  VAL   B O   
447  C CB  . VAL   B 16  ? 0.5264 0.5152 0.2845 0.0955  0.0712  0.0008  25  VAL   B CB  
448  C CG1 . VAL   B 16  ? 0.5215 0.5108 0.2907 0.0850  0.0738  -0.0066 25  VAL   B CG1 
449  C CG2 . VAL   B 16  ? 0.5276 0.5149 0.2710 0.0964  0.0647  -0.0035 25  VAL   B CG2 
450  N N   . MET   B 17  ? 0.5421 0.5298 0.3416 0.0986  0.0851  0.0104  26  MET   B N   
451  C CA  . MET   B 17  ? 0.5630 0.5502 0.3806 0.0991  0.0919  0.0162  26  MET   B CA  
452  C C   . MET   B 17  ? 0.5793 0.5657 0.4117 0.0887  0.0949  0.0075  26  MET   B C   
453  O O   . MET   B 17  ? 0.5621 0.5484 0.3929 0.0828  0.0922  -0.0023 26  MET   B O   
454  C CB  . MET   B 17  ? 0.5711 0.5567 0.3965 0.1057  0.0938  0.0214  26  MET   B CB  
455  C CG  . MET   B 17  ? 0.5829 0.5709 0.3937 0.1164  0.0902  0.0283  26  MET   B CG  
456  S SD  . MET   B 17  ? 0.5853 0.5777 0.3887 0.1254  0.0918  0.0414  26  MET   B SD  
457  C CE  . MET   B 17  ? 0.5978 0.5886 0.4251 0.1247  0.1008  0.0496  26  MET   B CE  
458  N N   . THR   B 18  ? 0.6068 0.5934 0.4540 0.0868  0.1004  0.0110  27  THR   B N   
459  C CA  . THR   B 18  ? 0.6473 0.6335 0.5129 0.0780  0.1042  0.0034  27  THR   B CA  
460  C C   . THR   B 18  ? 0.6850 0.6680 0.5712 0.0806  0.1108  0.0105  27  THR   B C   
461  O O   . THR   B 18  ? 0.6550 0.6382 0.5406 0.0877  0.1132  0.0224  27  THR   B O   
462  C CB  . THR   B 18  ? 0.6440 0.6343 0.5074 0.0712  0.1039  -0.0013 27  THR   B CB  
463  O OG1 . THR   B 18  ? 0.6601 0.6510 0.5413 0.0629  0.1071  -0.0104 27  THR   B OG1 
464  C CG2 . THR   B 18  ? 0.6475 0.6398 0.5110 0.0749  0.1066  0.0083  27  THR   B CG2 
465  N N   . ARG   B 19  ? 0.7331 0.7138 0.6376 0.0749  0.1139  0.0033  28  ARG   B N   
466  C CA  . ARG   B 19  ? 0.7945 0.7716 0.7224 0.0756  0.1207  0.0086  28  ARG   B CA  
467  C C   . ARG   B 19  ? 0.8068 0.7856 0.7500 0.0666  0.1241  0.0018  28  ARG   B C   
468  O O   . ARG   B 19  ? 0.8056 0.7812 0.7703 0.0657  0.1299  0.0048  28  ARG   B O   
469  C CB  . ARG   B 19  ? 0.8308 0.8034 0.7692 0.0776  0.1218  0.0066  28  ARG   B CB  
470  C CG  . ARG   B 19  ? 0.8633 0.8355 0.7877 0.0875  0.1188  0.0147  28  ARG   B CG  
471  C CD  . ARG   B 19  ? 0.8937 0.8614 0.8328 0.0934  0.1226  0.0210  28  ARG   B CD  
472  N NE  . ARG   B 19  ? 0.9199 0.8885 0.8463 0.1009  0.1186  0.0236  28  ARG   B NE  
473  C CZ  . ARG   B 19  ? 0.9588 0.9283 0.8787 0.0983  0.1143  0.0134  28  ARG   B CZ  
474  N NH1 . ARG   B 19  ? 0.9642 0.9342 0.8882 0.0886  0.1133  0.0002  28  ARG   B NH1 
475  N NH2 . ARG   B 19  ? 0.9603 0.9312 0.8696 0.1055  0.1108  0.0165  28  ARG   B NH2 
476  N N   . ARG   B 20  ? 0.8470 0.8314 0.7796 0.0607  0.1208  -0.0056 29  ARG   B N   
477  C CA  . ARG   B 20  ? 0.9025 0.8908 0.8479 0.0515  0.1229  -0.0148 29  ARG   B CA  
478  C C   . ARG   B 20  ? 0.8835 0.8729 0.8367 0.0525  0.1271  -0.0060 29  ARG   B C   
479  O O   . ARG   B 20  ? 0.8859 0.8788 0.8523 0.0454  0.1295  -0.0124 29  ARG   B O   
480  C CB  . ARG   B 20  ? 0.9614 0.9562 0.8905 0.0459  0.1175  -0.0251 29  ARG   B CB  
481  C CG  . ARG   B 20  ? 1.0350 1.0347 0.9768 0.0361  0.1183  -0.0396 29  ARG   B CG  
482  C CD  . ARG   B 20  ? 1.1225 1.1299 1.0467 0.0316  0.1131  -0.0471 29  ARG   B CD  
483  N NE  . ARG   B 20  ? 1.1991 1.2083 1.1071 0.0356  0.1110  -0.0383 29  ARG   B NE  
484  C CZ  . ARG   B 20  ? 1.2626 1.2766 1.1742 0.0335  0.1127  -0.0368 29  ARG   B CZ  
485  N NH1 . ARG   B 20  ? 1.2922 1.3099 1.2231 0.0270  0.1164  -0.0438 29  ARG   B NH1 
486  N NH2 . ARG   B 20  ? 1.2652 1.2807 1.1612 0.0380  0.1106  -0.0286 29  ARG   B NH2 
487  N N   . LEU   B 21  ? 0.8541 0.8421 0.7987 0.0611  0.1277  0.0078  30  LEU   B N   
488  C CA  . LEU   B 21  ? 0.8163 0.8058 0.7683 0.0636  0.1322  0.0187  30  LEU   B CA  
489  C C   . LEU   B 21  ? 0.7820 0.7656 0.7477 0.0703  0.1374  0.0307  30  LEU   B C   
490  O O   . LEU   B 21  ? 0.7694 0.7478 0.7427 0.0710  0.1379  0.0279  30  LEU   B O   
491  C CB  . LEU   B 21  ? 0.8208 0.8152 0.7492 0.0686  0.1282  0.0247  30  LEU   B CB  
492  C CG  . LEU   B 21  ? 0.8260 0.8273 0.7469 0.0623  0.1255  0.0171  30  LEU   B CG  
493  C CD1 . LEU   B 21  ? 0.8324 0.8351 0.7572 0.0531  0.1232  0.0015  30  LEU   B CD1 
494  C CD2 . LEU   B 21  ? 0.8317 0.8361 0.7266 0.0680  0.1200  0.0210  30  LEU   B CD2 
495  N N   . LEU   B 22  ? 0.7761 0.7611 0.7453 0.0752  0.1414  0.0439  31  LEU   B N   
496  C CA  . LEU   B 22  ? 0.7531 0.7337 0.7344 0.0826  0.1468  0.0579  31  LEU   B CA  
497  C C   . LEU   B 22  ? 0.7420 0.7216 0.7059 0.0921  0.1430  0.0635  31  LEU   B C   
498  O O   . LEU   B 22  ? 0.7498 0.7338 0.6903 0.0952  0.1373  0.0625  31  LEU   B O   
499  C CB  . LEU   B 22  ? 0.7436 0.7283 0.7283 0.0858  0.1512  0.0708  31  LEU   B CB  
500  C CG  . LEU   B 22  ? 0.7435 0.7243 0.7461 0.0915  0.1582  0.0855  31  LEU   B CG  
501  C CD1 . LEU   B 22  ? 0.7349 0.7099 0.7683 0.0835  0.1642  0.0811  31  LEU   B CD1 
502  C CD2 . LEU   B 22  ? 0.7464 0.7337 0.7428 0.0981  0.1609  0.1005  31  LEU   B CD2 
503  N N   . GLY   B 23  ? 0.7267 0.7009 0.7020 0.0965  0.1459  0.0686  32  GLY   B N   
504  C CA  . GLY   B 23  ? 0.7140 0.6879 0.6749 0.1054  0.1423  0.0728  32  GLY   B CA  
505  C C   . GLY   B 23  ? 0.7007 0.6766 0.6410 0.1030  0.1344  0.0605  32  GLY   B C   
506  O O   . GLY   B 23  ? 0.7015 0.6767 0.6449 0.0936  0.1327  0.0470  32  GLY   B O   
507  N N   . SER   B 24  ? 0.6814 0.6600 0.6022 0.1113  0.1299  0.0649  33  SER   B N   
508  C CA  . SER   B 24  ? 0.6566 0.6374 0.5559 0.1105  0.1222  0.0555  33  SER   B CA  
509  C C   . SER   B 24  ? 0.6413 0.6275 0.5227 0.1126  0.1193  0.0585  33  SER   B C   
510  O O   . SER   B 24  ? 0.6355 0.6252 0.5123 0.1213  0.1209  0.0708  33  SER   B O   
511  C CB  . SER   B 24  ? 0.6565 0.6371 0.5473 0.1183  0.1192  0.0579  33  SER   B CB  
512  O OG  . SER   B 24  ? 0.6763 0.6521 0.5837 0.1163  0.1217  0.0545  33  SER   B OG  
513  N N   . THR   B 25  ? 0.6111 0.5988 0.4832 0.1056  0.1154  0.0485  34  THR   B N   
514  C CA  . THR   B 25  ? 0.6026 0.5953 0.4595 0.1072  0.1129  0.0511  34  THR   B CA  
515  C C   . THR   B 25  ? 0.5929 0.5865 0.4280 0.1081  0.1053  0.0443  34  THR   B C   
516  O O   . THR   B 25  ? 0.5790 0.5702 0.4141 0.1016  0.1026  0.0335  34  THR   B O   
517  C CB  . THR   B 25  ? 0.6027 0.5971 0.4686 0.0985  0.1154  0.0466  34  THR   B CB  
518  O OG1 . THR   B 25  ? 0.6111 0.6043 0.4988 0.0975  0.1227  0.0529  34  THR   B OG1 
519  C CG2 . THR   B 25  ? 0.6025 0.6024 0.4535 0.1005  0.1130  0.0494  34  THR   B CG2 
520  N N   . GLN   B 26  ? 0.5754 0.5727 0.3936 0.1157  0.1021  0.0501  35  GLN   B N   
521  C CA  . GLN   B 26  ? 0.5671 0.5646 0.3653 0.1169  0.0947  0.0438  35  GLN   B CA  
522  C C   . GLN   B 26  ? 0.5653 0.5645 0.3562 0.1109  0.0925  0.0385  35  GLN   B C   
523  O O   . GLN   B 26  ? 0.5721 0.5752 0.3600 0.1140  0.0939  0.0447  35  GLN   B O   
524  C CB  . GLN   B 26  ? 0.5609 0.5617 0.3445 0.1283  0.0916  0.0511  35  GLN   B CB  
525  C CG  . GLN   B 26  ? 0.5517 0.5521 0.3165 0.1294  0.0840  0.0441  35  GLN   B CG  
526  C CD  . GLN   B 26  ? 0.5501 0.5546 0.3018 0.1410  0.0808  0.0501  35  GLN   B CD  
527  O OE1 . GLN   B 26  ? 0.5509 0.5570 0.3066 0.1474  0.0824  0.0555  35  GLN   B OE1 
528  N NE2 . GLN   B 26  ? 0.5404 0.5468 0.2763 0.1438  0.0759  0.0483  35  GLN   B NE2 
529  N N   . VAL   B 27  ? 0.5574 0.5545 0.3461 0.1028  0.0895  0.0277  36  VAL   B N   
530  C CA  . VAL   B 27  ? 0.5433 0.5427 0.3258 0.0966  0.0874  0.0222  36  VAL   B CA  
531  C C   . VAL   B 27  ? 0.5330 0.5322 0.2947 0.1004  0.0807  0.0208  36  VAL   B C   
532  O O   . VAL   B 27  ? 0.5415 0.5430 0.2949 0.0993  0.0788  0.0201  36  VAL   B O   
533  C CB  . VAL   B 27  ? 0.5444 0.5429 0.3374 0.0859  0.0884  0.0120  36  VAL   B CB  
534  C CG1 . VAL   B 27  ? 0.5498 0.5488 0.3640 0.0827  0.0951  0.0137  36  VAL   B CG1 
535  C CG2 . VAL   B 27  ? 0.5389 0.5340 0.3301 0.0841  0.0856  0.0055  36  VAL   B CG2 
536  N N   . GLY   B 28  ? 0.5199 0.5167 0.2736 0.1055  0.0772  0.0208  37  GLY   B N   
537  C CA  . GLY   B 28  ? 0.5078 0.5041 0.2432 0.1101  0.0709  0.0197  37  GLY   B CA  
538  C C   . GLY   B 28  ? 0.5006 0.4947 0.2313 0.1144  0.0675  0.0181  37  GLY   B C   
539  O O   . GLY   B 28  ? 0.5047 0.4988 0.2447 0.1172  0.0705  0.0212  37  GLY   B O   
540  N N   . VAL   B 29  ? 0.4956 0.4878 0.2124 0.1152  0.0615  0.0136  38  VAL   B N   
541  C CA  . VAL   B 29  ? 0.4959 0.4868 0.2050 0.1202  0.0569  0.0116  38  VAL   B CA  
542  C C   . VAL   B 29  ? 0.4942 0.4812 0.1967 0.1134  0.0520  0.0027  38  VAL   B C   
543  O O   . VAL   B 29  ? 0.4886 0.4747 0.1886 0.1072  0.0515  0.0000  38  VAL   B O   
544  C CB  . VAL   B 29  ? 0.5037 0.4977 0.2010 0.1310  0.0542  0.0171  38  VAL   B CB  
545  C CG1 . VAL   B 29  ? 0.5071 0.5013 0.1964 0.1373  0.0492  0.0148  38  VAL   B CG1 
546  C CG2 . VAL   B 29  ? 0.5034 0.5024 0.2072 0.1370  0.0595  0.0268  38  VAL   B CG2 
547  N N   . GLY   B 30  ? 0.4944 0.4799 0.1941 0.1147  0.0485  -0.0012 39  GLY   B N   
548  C CA  . GLY   B 30  ? 0.4922 0.4742 0.1844 0.1095  0.0434  -0.0085 39  GLY   B CA  
549  C C   . GLY   B 30  ? 0.4969 0.4783 0.1849 0.1135  0.0390  -0.0117 39  GLY   B C   
550  O O   . GLY   B 30  ? 0.4969 0.4816 0.1862 0.1218  0.0396  -0.0077 39  GLY   B O   
551  N N   . VAL   B 31  ? 0.4943 0.4723 0.1766 0.1087  0.0346  -0.0180 40  VAL   B N   
552  C CA  . VAL   B 31  ? 0.5024 0.4794 0.1791 0.1117  0.0292  -0.0222 40  VAL   B CA  
553  C C   . VAL   B 31  ? 0.5080 0.4840 0.1908 0.1037  0.0289  -0.0286 40  VAL   B C   
554  O O   . VAL   B 31  ? 0.4955 0.4692 0.1791 0.0948  0.0294  -0.0317 40  VAL   B O   
555  C CB  . VAL   B 31  ? 0.5084 0.4819 0.1733 0.1135  0.0238  -0.0240 40  VAL   B CB  
556  C CG1 . VAL   B 31  ? 0.5143 0.4863 0.1750 0.1153  0.0181  -0.0297 40  VAL   B CG1 
557  C CG2 . VAL   B 31  ? 0.5113 0.4869 0.1697 0.1224  0.0239  -0.0181 40  VAL   B CG2 
558  N N   . MET   B 32  ? 0.5145 0.4932 0.2018 0.1068  0.0284  -0.0302 41  MET   B N   
559  C CA  . MET   B 32  ? 0.5205 0.4992 0.2128 0.1006  0.0272  -0.0368 41  MET   B CA  
560  C C   . MET   B 32  ? 0.5358 0.5128 0.2201 0.1022  0.0207  -0.0414 41  MET   B C   
561  O O   . MET   B 32  ? 0.5267 0.5060 0.2062 0.1114  0.0175  -0.0405 41  MET   B O   
562  C CB  . MET   B 32  ? 0.5223 0.5053 0.2248 0.1036  0.0304  -0.0358 41  MET   B CB  
563  C CG  . MET   B 32  ? 0.5233 0.5074 0.2328 0.0968  0.0303  -0.0423 41  MET   B CG  
564  S SD  . MET   B 32  ? 0.5261 0.5093 0.2435 0.0846  0.0350  -0.0452 41  MET   B SD  
565  C CE  . MET   B 32  ? 0.5256 0.5106 0.2538 0.0884  0.0416  -0.0393 41  MET   B CE  
566  N N   . GLN   B 33  ? 0.5495 0.5230 0.2320 0.0941  0.0184  -0.0462 42  GLN   B N   
567  C CA  . GLN   B 33  ? 0.5748 0.5457 0.2517 0.0939  0.0124  -0.0513 42  GLN   B CA  
568  C C   . GLN   B 33  ? 0.5948 0.5649 0.2765 0.0835  0.0123  -0.0565 42  GLN   B C   
569  O O   . GLN   B 33  ? 0.5739 0.5427 0.2571 0.0758  0.0152  -0.0557 42  GLN   B O   
570  C CB  . GLN   B 33  ? 0.5936 0.5593 0.2606 0.0959  0.0089  -0.0501 42  GLN   B CB  
571  C CG  . GLN   B 33  ? 0.6153 0.5780 0.2783 0.0963  0.0026  -0.0558 42  GLN   B CG  
572  C CD  . GLN   B 33  ? 0.6407 0.5988 0.2944 0.1017  -0.0016 -0.0554 42  GLN   B CD  
573  O OE1 . GLN   B 33  ? 0.7009 0.6531 0.3519 0.0974  -0.0051 -0.0586 42  GLN   B OE1 
574  N NE2 . GLN   B 33  ? 0.6243 0.5850 0.2734 0.1106  -0.0010 -0.0511 42  GLN   B NE2 
575  N N   . GLU   B 34  ? 0.6148 0.5864 0.2987 0.0832  0.0091  -0.0616 43  GLU   B N   
576  C CA  . GLU   B 34  ? 0.6285 0.6005 0.3175 0.0734  0.0089  -0.0667 43  GLU   B CA  
577  C C   . GLU   B 34  ? 0.6229 0.5987 0.3200 0.0671  0.0147  -0.0662 43  GLU   B C   
578  O O   . GLU   B 34  ? 0.6094 0.5851 0.3082 0.0580  0.0158  -0.0682 43  GLU   B O   
579  C CB  . GLU   B 34  ? 0.6582 0.6238 0.3412 0.0679  0.0060  -0.0673 43  GLU   B CB  
580  C CG  . GLU   B 34  ? 0.6850 0.6471 0.3633 0.0721  -0.0001 -0.0705 43  GLU   B CG  
581  C CD  . GLU   B 34  ? 0.7125 0.6668 0.3838 0.0704  -0.0031 -0.0695 43  GLU   B CD  
582  O OE1 . GLU   B 34  ? 0.7386 0.6898 0.4114 0.0622  -0.0039 -0.0711 43  GLU   B OE1 
583  O OE2 . GLU   B 34  ? 0.7423 0.6939 0.4069 0.0777  -0.0048 -0.0669 43  GLU   B OE2 
584  N N   . GLY   B 35  ? 0.6039 0.5835 0.3065 0.0716  0.0185  -0.0637 44  GLY   B N   
585  C CA  . GLY   B 35  ? 0.5862 0.5695 0.2981 0.0661  0.0238  -0.0645 44  GLY   B CA  
586  C C   . GLY   B 35  ? 0.5693 0.5511 0.2803 0.0618  0.0273  -0.0615 44  GLY   B C   
587  O O   . GLY   B 35  ? 0.5678 0.5531 0.2868 0.0570  0.0317  -0.0629 44  GLY   B O   
588  N N   . VAL   B 36  ? 0.5527 0.5301 0.2548 0.0640  0.0254  -0.0578 45  VAL   B N   
589  C CA  . VAL   B 36  ? 0.5356 0.5123 0.2360 0.0608  0.0283  -0.0547 45  VAL   B CA  
590  C C   . VAL   B 36  ? 0.5246 0.5004 0.2235 0.0690  0.0300  -0.0488 45  VAL   B C   
591  O O   . VAL   B 36  ? 0.5298 0.5034 0.2222 0.0770  0.0267  -0.0464 45  VAL   B O   
592  C CB  . VAL   B 36  ? 0.5373 0.5103 0.2294 0.0558  0.0254  -0.0549 45  VAL   B CB  
593  C CG1 . VAL   B 36  ? 0.5358 0.5084 0.2245 0.0550  0.0275  -0.0508 45  VAL   B CG1 
594  C CG2 . VAL   B 36  ? 0.5385 0.5143 0.2342 0.0462  0.0257  -0.0595 45  VAL   B CG2 
595  N N   . PHE   B 37  ? 0.5100 0.4882 0.2152 0.0671  0.0349  -0.0469 46  PHE   B N   
596  C CA  . PHE   B 37  ? 0.5069 0.4851 0.2125 0.0733  0.0374  -0.0409 46  PHE   B CA  
597  C C   . PHE   B 37  ? 0.5030 0.4797 0.2016 0.0712  0.0371  -0.0385 46  PHE   B C   
598  O O   . PHE   B 37  ? 0.4974 0.4759 0.1977 0.0635  0.0387  -0.0409 46  PHE   B O   
599  C CB  . PHE   B 37  ? 0.5031 0.4846 0.2214 0.0732  0.0430  -0.0400 46  PHE   B CB  
600  C CG  . PHE   B 37  ? 0.5084 0.4898 0.2276 0.0808  0.0454  -0.0328 46  PHE   B CG  
601  C CD1 . PHE   B 37  ? 0.5154 0.4965 0.2304 0.0904  0.0436  -0.0285 46  PHE   B CD1 
602  C CD2 . PHE   B 37  ? 0.5082 0.4908 0.2324 0.0783  0.0495  -0.0305 46  PHE   B CD2 
603  C CE1 . PHE   B 37  ? 0.5227 0.5048 0.2383 0.0975  0.0461  -0.0211 46  PHE   B CE1 
604  C CE2 . PHE   B 37  ? 0.5138 0.4968 0.2395 0.0848  0.0521  -0.0234 46  PHE   B CE2 
605  C CZ  . PHE   B 37  ? 0.5195 0.5023 0.2409 0.0945  0.0506  -0.0183 46  PHE   B CZ  
606  N N   . HIS   B 38  ? 0.4963 0.4708 0.1869 0.0785  0.0350  -0.0339 47  HIS   B N   
607  C CA  . HIS   B 38  ? 0.4967 0.4693 0.1789 0.0788  0.0338  -0.0311 47  HIS   B CA  
608  C C   . HIS   B 38  ? 0.4982 0.4733 0.1827 0.0838  0.0374  -0.0252 47  HIS   B C   
609  O O   . HIS   B 38  ? 0.4952 0.4708 0.1791 0.0922  0.0374  -0.0214 47  HIS   B O   
610  C CB  . HIS   B 38  ? 0.4996 0.4678 0.1706 0.0834  0.0280  -0.0310 47  HIS   B CB  
611  C CG  . HIS   B 38  ? 0.5035 0.4688 0.1727 0.0796  0.0241  -0.0362 47  HIS   B CG  
612  N ND1 . HIS   B 38  ? 0.5043 0.4711 0.1787 0.0800  0.0238  -0.0394 47  HIS   B ND1 
613  C CD2 . HIS   B 38  ? 0.5087 0.4702 0.1726 0.0745  0.0209  -0.0385 47  HIS   B CD2 
614  C CE1 . HIS   B 38  ? 0.5079 0.4721 0.1802 0.0758  0.0202  -0.0438 47  HIS   B CE1 
615  N NE2 . HIS   B 38  ? 0.5098 0.4705 0.1761 0.0719  0.0186  -0.0431 47  HIS   B NE2 
616  N N   . THR   B 39  ? 0.4982 0.4755 0.1849 0.0793  0.0402  -0.0243 48  THR   B N   
617  C CA  . THR   B 39  ? 0.4978 0.4777 0.1866 0.0838  0.0435  -0.0186 48  THR   B CA  
618  C C   . THR   B 39  ? 0.5050 0.4859 0.1887 0.0805  0.0432  -0.0179 48  THR   B C   
619  O O   . THR   B 39  ? 0.4968 0.4764 0.1752 0.0748  0.0404  -0.0216 48  THR   B O   
620  C CB  . THR   B 39  ? 0.4959 0.4788 0.1987 0.0831  0.0491  -0.0175 48  THR   B CB  
621  O OG1 . THR   B 39  ? 0.4952 0.4803 0.2003 0.0887  0.0521  -0.0108 48  THR   B OG1 
622  C CG2 . THR   B 39  ? 0.4942 0.4802 0.2067 0.0735  0.0524  -0.0225 48  THR   B CG2 
623  N N   . MET   B 40  ? 0.5097 0.4939 0.1959 0.0835  0.0462  -0.0132 49  MET   B N   
624  C CA  . MET   B 40  ? 0.5124 0.4995 0.1960 0.0801  0.0468  -0.0127 49  MET   B CA  
625  C C   . MET   B 40  ? 0.5022 0.4945 0.1973 0.0715  0.0511  -0.0164 49  MET   B C   
626  O O   . MET   B 40  ? 0.4960 0.4900 0.2034 0.0705  0.0553  -0.0170 49  MET   B O   
627  C CB  . MET   B 40  ? 0.5253 0.5143 0.2054 0.0874  0.0476  -0.0063 49  MET   B CB  
628  C CG  . MET   B 40  ? 0.5407 0.5260 0.2104 0.0970  0.0435  -0.0032 49  MET   B CG  
629  S SD  . MET   B 40  ? 0.5632 0.5501 0.2226 0.1034  0.0416  0.0014  49  MET   B SD  
630  C CE  . MET   B 40  ? 0.5683 0.5507 0.2171 0.0992  0.0362  -0.0026 49  MET   B CE  
631  N N   A TRP   B 41  ? 0.5019 0.4972 0.1937 0.0657  0.0501  -0.0191 50  TRP   B N   
632  N N   B TRP   B 41  ? 0.4981 0.4934 0.1900 0.0656  0.0502  -0.0192 50  TRP   B N   
633  N N   C TRP   B 41  ? 0.5019 0.4971 0.1936 0.0657  0.0501  -0.0191 50  TRP   B N   
634  N N   D TRP   B 41  ? 0.4981 0.4933 0.1900 0.0656  0.0502  -0.0192 50  TRP   B N   
635  C CA  A TRP   B 41  ? 0.4982 0.5001 0.1998 0.0573  0.0535  -0.0241 50  TRP   B CA  
636  C CA  B TRP   B 41  ? 0.4922 0.4941 0.1941 0.0573  0.0536  -0.0242 50  TRP   B CA  
637  C CA  C TRP   B 41  ? 0.4982 0.5000 0.1997 0.0573  0.0535  -0.0241 50  TRP   B CA  
638  C CA  D TRP   B 41  ? 0.4921 0.4940 0.1940 0.0573  0.0536  -0.0242 50  TRP   B CA  
639  C C   A TRP   B 41  ? 0.4956 0.5019 0.2088 0.0581  0.0585  -0.0221 50  TRP   B C   
640  C C   B TRP   B 41  ? 0.4922 0.4985 0.2055 0.0581  0.0586  -0.0221 50  TRP   B C   
641  C C   C TRP   B 41  ? 0.4956 0.5019 0.2088 0.0581  0.0585  -0.0221 50  TRP   B C   
642  C C   D TRP   B 41  ? 0.4921 0.4984 0.2054 0.0581  0.0586  -0.0221 50  TRP   B C   
643  O O   A TRP   B 41  ? 0.4905 0.4997 0.2167 0.0534  0.0622  -0.0262 50  TRP   B O   
644  O O   B TRP   B 41  ? 0.4874 0.4967 0.2138 0.0534  0.0623  -0.0262 50  TRP   B O   
645  O O   C TRP   B 41  ? 0.4901 0.4993 0.2164 0.0535  0.0622  -0.0261 50  TRP   B O   
646  O O   D TRP   B 41  ? 0.4871 0.4963 0.2135 0.0535  0.0623  -0.0261 50  TRP   B O   
647  C CB  A TRP   B 41  ? 0.4999 0.5057 0.1942 0.0525  0.0514  -0.0261 50  TRP   B CB  
648  C CB  B TRP   B 41  ? 0.4895 0.4954 0.1844 0.0522  0.0515  -0.0264 50  TRP   B CB  
649  C CB  C TRP   B 41  ? 0.4998 0.5057 0.1941 0.0525  0.0514  -0.0261 50  TRP   B CB  
650  C CB  D TRP   B 41  ? 0.4894 0.4954 0.1843 0.0522  0.0515  -0.0263 50  TRP   B CB  
651  C CG  A TRP   B 41  ? 0.4975 0.5113 0.2013 0.0440  0.0543  -0.0324 50  TRP   B CG  
652  C CG  B TRP   B 41  ? 0.4830 0.4976 0.1880 0.0442  0.0549  -0.0320 50  TRP   B CG  
653  C CG  C TRP   B 41  ? 0.4976 0.5113 0.2013 0.0440  0.0543  -0.0324 50  TRP   B CG  
654  C CG  D TRP   B 41  ? 0.4829 0.4975 0.1879 0.0443  0.0549  -0.0320 50  TRP   B CG  
655  C CD1 A TRP   B 41  ? 0.4966 0.5121 0.2020 0.0379  0.0539  -0.0379 50  TRP   B CD1 
656  C CD1 B TRP   B 41  ? 0.4794 0.5009 0.1929 0.0426  0.0585  -0.0326 50  TRP   B CD1 
657  C CD1 C TRP   B 41  ? 0.4966 0.5120 0.2020 0.0379  0.0539  -0.0379 50  TRP   B CD1 
658  C CD1 D TRP   B 41  ? 0.4794 0.5008 0.1928 0.0426  0.0585  -0.0326 50  TRP   B CD1 
659  C CD2 A TRP   B 41  ? 0.4956 0.5173 0.2098 0.0408  0.0583  -0.0345 50  TRP   B CD2 
660  C CD2 B TRP   B 41  ? 0.4793 0.4976 0.1878 0.0370  0.0551  -0.0386 50  TRP   B CD2 
661  C CD2 C TRP   B 41  ? 0.4956 0.5173 0.2098 0.0408  0.0583  -0.0345 50  TRP   B CD2 
662  C CD2 D TRP   B 41  ? 0.4792 0.4975 0.1876 0.0370  0.0551  -0.0385 50  TRP   B CD2 
663  N NE1 A TRP   B 41  ? 0.4946 0.5191 0.2100 0.0315  0.0572  -0.0436 50  TRP   B NE1 
664  N NE1 B TRP   B 41  ? 0.4753 0.5045 0.1974 0.0349  0.0606  -0.0397 50  TRP   B NE1 
665  N NE1 C TRP   B 41  ? 0.4947 0.5192 0.2102 0.0315  0.0572  -0.0436 50  TRP   B NE1 
666  N NE1 D TRP   B 41  ? 0.4752 0.5043 0.1972 0.0349  0.0606  -0.0397 50  TRP   B NE1 
667  C CE2 A TRP   B 41  ? 0.4929 0.5212 0.2143 0.0330  0.0599  -0.0420 50  TRP   B CE2 
668  C CE2 B TRP   B 41  ? 0.4756 0.5033 0.1944 0.0315  0.0587  -0.0434 50  TRP   B CE2 
669  C CE2 C TRP   B 41  ? 0.4929 0.5212 0.2143 0.0330  0.0599  -0.0420 50  TRP   B CE2 
670  C CE2 D TRP   B 41  ? 0.4755 0.5032 0.1943 0.0315  0.0587  -0.0434 50  TRP   B CE2 
671  C CE3 A TRP   B 41  ? 0.4962 0.5208 0.2148 0.0436  0.0608  -0.0311 50  TRP   B CE3 
672  C CE3 B TRP   B 41  ? 0.4802 0.4955 0.1846 0.0345  0.0528  -0.0411 50  TRP   B CE3 
673  C CE3 C TRP   B 41  ? 0.4963 0.5210 0.2149 0.0436  0.0608  -0.0311 50  TRP   B CE3 
674  C CE3 D TRP   B 41  ? 0.4802 0.4955 0.1846 0.0345  0.0528  -0.0410 50  TRP   B CE3 
675  C CZ2 A TRP   B 41  ? 0.4918 0.5292 0.2246 0.0281  0.0634  -0.0469 50  TRP   B CZ2 
676  C CZ2 B TRP   B 41  ? 0.4730 0.5077 0.1972 0.0241  0.0598  -0.0508 50  TRP   B CZ2 
677  C CZ2 C TRP   B 41  ? 0.4920 0.5294 0.2248 0.0281  0.0634  -0.0469 50  TRP   B CZ2 
678  C CZ2 D TRP   B 41  ? 0.4729 0.5076 0.1971 0.0241  0.0598  -0.0508 50  TRP   B CZ2 
679  C CZ3 A TRP   B 41  ? 0.4934 0.5266 0.2238 0.0384  0.0645  -0.0355 50  TRP   B CZ3 
680  C CZ3 B TRP   B 41  ? 0.4776 0.4998 0.1873 0.0270  0.0541  -0.0476 50  TRP   B CZ3 
681  C CZ3 C TRP   B 41  ? 0.4935 0.5268 0.2240 0.0384  0.0645  -0.0355 50  TRP   B CZ3 
682  C CZ3 D TRP   B 41  ? 0.4776 0.4998 0.1873 0.0270  0.0541  -0.0476 50  TRP   B CZ3 
683  C CH2 A TRP   B 41  ? 0.4910 0.5305 0.2285 0.0307  0.0656  -0.0436 50  TRP   B CH2 
684  C CH2 B TRP   B 41  ? 0.4739 0.5059 0.1932 0.0221  0.0576  -0.0525 50  TRP   B CH2 
685  C CH2 C TRP   B 41  ? 0.4911 0.5307 0.2287 0.0307  0.0656  -0.0436 50  TRP   B CH2 
686  C CH2 D TRP   B 41  ? 0.4737 0.5057 0.1931 0.0221  0.0576  -0.0525 50  TRP   B CH2 
687  N N   . HIS   B 42  ? 0.4970 0.5037 0.2065 0.0639  0.0588  -0.0161 51  HIS   B N   
688  C CA  . HIS   B 42  ? 0.4997 0.5112 0.2208 0.0643  0.0637  -0.0136 51  HIS   B CA  
689  C C   . HIS   B 42  ? 0.5139 0.5226 0.2470 0.0668  0.0675  -0.0116 51  HIS   B C   
690  O O   . HIS   B 42  ? 0.5215 0.5337 0.2684 0.0645  0.0723  -0.0113 51  HIS   B O   
691  C CB  . HIS   B 42  ? 0.5024 0.5162 0.2167 0.0697  0.0631  -0.0076 51  HIS   B CB  
692  C CG  . HIS   B 42  ? 0.4999 0.5093 0.2082 0.0794  0.0622  -0.0006 51  HIS   B CG  
693  N ND1 . HIS   B 42  ? 0.5039 0.5096 0.1971 0.0850  0.0571  0.0013  51  HIS   B ND1 
694  C CD2 . HIS   B 42  ? 0.5078 0.5169 0.2232 0.0846  0.0656  0.0047  51  HIS   B CD2 
695  C CE1 . HIS   B 42  ? 0.5075 0.5115 0.1983 0.0937  0.0573  0.0071  51  HIS   B CE1 
696  N NE2 . HIS   B 42  ? 0.5005 0.5068 0.2044 0.0937  0.0625  0.0098  51  HIS   B NE2 
697  N N   . VAL   B 43  ? 0.5241 0.5272 0.2537 0.0705  0.0656  -0.0108 52  VAL   B N   
698  C CA  . VAL   B 43  ? 0.5305 0.5313 0.2710 0.0736  0.0691  -0.0083 52  VAL   B CA  
699  C C   . VAL   B 43  ? 0.5368 0.5388 0.2915 0.0659  0.0721  -0.0154 52  VAL   B C   
700  O O   . VAL   B 43  ? 0.5362 0.5392 0.3058 0.0654  0.0770  -0.0140 52  VAL   B O   
701  C CB  . VAL   B 43  ? 0.5412 0.5370 0.2721 0.0807  0.0654  -0.0057 52  VAL   B CB  
702  C CG1 . VAL   B 43  ? 0.5458 0.5397 0.2868 0.0836  0.0681  -0.0040 52  VAL   B CG1 
703  C CG2 . VAL   B 43  ? 0.5470 0.5429 0.2667 0.0892  0.0633  0.0011  52  VAL   B CG2 
704  N N   . THR   B 44  ? 0.5271 0.5294 0.2780 0.0601  0.0693  -0.0226 53  THR   B N   
705  C CA  . THR   B 44  ? 0.5374 0.5412 0.3004 0.0534  0.0716  -0.0301 53  THR   B CA  
706  C C   . THR   B 44  ? 0.5452 0.5562 0.3126 0.0451  0.0727  -0.0369 53  THR   B C   
707  O O   . THR   B 44  ? 0.5411 0.5552 0.3225 0.0399  0.0760  -0.0430 53  THR   B O   
708  C CB  . THR   B 44  ? 0.5301 0.5308 0.2871 0.0530  0.0682  -0.0336 53  THR   B CB  
709  O OG1 . THR   B 44  ? 0.5205 0.5223 0.2644 0.0500  0.0638  -0.0360 53  THR   B OG1 
710  C CG2 . THR   B 44  ? 0.5319 0.5271 0.2846 0.0617  0.0667  -0.0276 53  THR   B CG2 
711  N N   . LYS   B 45  ? 0.5671 0.5812 0.3241 0.0444  0.0704  -0.0357 54  LYS   B N   
712  C CA  . LYS   B 45  ? 0.6070 0.6294 0.3642 0.0370  0.0702  -0.0420 54  LYS   B CA  
713  C C   . LYS   B 45  ? 0.6068 0.6312 0.3631 0.0313  0.0687  -0.0493 54  LYS   B C   
714  O O   . LYS   B 45  ? 0.6307 0.6632 0.3930 0.0245  0.0700  -0.0564 54  LYS   B O   
715  C CB  . LYS   B 45  ? 0.6365 0.6653 0.4097 0.0330  0.0750  -0.0454 54  LYS   B CB  
716  C CG  . LYS   B 45  ? 0.6713 0.6983 0.4501 0.0382  0.0778  -0.0382 54  LYS   B CG  
717  C CD  . LYS   B 45  ? 0.7053 0.7357 0.4737 0.0405  0.0760  -0.0338 54  LYS   B CD  
718  C CE  . LYS   B 45  ? 0.7280 0.7589 0.5048 0.0443  0.0797  -0.0276 54  LYS   B CE  
719  N NZ  . LYS   B 45  ? 0.7570 0.7836 0.5208 0.0529  0.0775  -0.0183 54  LYS   B NZ  
720  N N   . GLY   B 46  ? 0.6106 0.6287 0.3603 0.0338  0.0660  -0.0481 55  GLY   B N   
721  C CA  . GLY   B 46  ? 0.6146 0.6345 0.3631 0.0287  0.0645  -0.0542 55  GLY   B CA  
722  C C   . GLY   B 46  ? 0.6221 0.6434 0.3856 0.0260  0.0679  -0.0601 55  GLY   B C   
723  O O   . GLY   B 46  ? 0.6150 0.6391 0.3783 0.0217  0.0670  -0.0656 55  GLY   B O   
724  N N   . ALA   B 47  ? 0.6256 0.6446 0.4018 0.0288  0.0717  -0.0586 56  ALA   B N   
725  C CA  . ALA   B 47  ? 0.6176 0.6369 0.4096 0.0268  0.0751  -0.0640 56  ALA   B CA  
726  C C   . ALA   B 47  ? 0.6078 0.6218 0.3969 0.0300  0.0732  -0.0632 56  ALA   B C   
727  O O   . ALA   B 47  ? 0.6088 0.6175 0.3861 0.0353  0.0700  -0.0571 56  ALA   B O   
728  C CB  . ALA   B 47  ? 0.6221 0.6392 0.4283 0.0297  0.0796  -0.0607 56  ALA   B CB  
729  N N   . ALA   B 48  ? 0.5889 0.6047 0.3893 0.0271  0.0751  -0.0696 57  ALA   B N   
730  C CA  . ALA   B 48  ? 0.5853 0.5967 0.3864 0.0306  0.0741  -0.0692 57  ALA   B CA  
731  C C   . ALA   B 48  ? 0.5802 0.5845 0.3851 0.0390  0.0755  -0.0609 57  ALA   B C   
732  O O   . ALA   B 48  ? 0.5771 0.5806 0.3892 0.0406  0.0787  -0.0572 57  ALA   B O   
733  C CB  . ALA   B 48  ? 0.5942 0.6100 0.4085 0.0258  0.0765  -0.0781 57  ALA   B CB  
734  N N   . LEU   B 49  ? 0.5766 0.5769 0.3772 0.0441  0.0733  -0.0583 58  LEU   B N   
735  C CA  . LEU   B 49  ? 0.5908 0.5858 0.3939 0.0530  0.0742  -0.0502 58  LEU   B CA  
736  C C   . LEU   B 49  ? 0.6103 0.6047 0.4221 0.0549  0.0750  -0.0528 58  LEU   B C   
737  O O   . LEU   B 49  ? 0.6130 0.6101 0.4228 0.0507  0.0728  -0.0596 58  LEU   B O   
738  C CB  . LEU   B 49  ? 0.5787 0.5709 0.3651 0.0592  0.0697  -0.0436 58  LEU   B CB  
739  C CG  . LEU   B 49  ? 0.5722 0.5647 0.3480 0.0585  0.0682  -0.0406 58  LEU   B CG  
740  C CD1 . LEU   B 49  ? 0.5667 0.5564 0.3262 0.0637  0.0631  -0.0367 58  LEU   B CD1 
741  C CD2 . LEU   B 49  ? 0.5742 0.5667 0.3573 0.0611  0.0724  -0.0349 58  LEU   B CD2 
742  N N   . ARG   B 50  ? 0.6311 0.6222 0.4519 0.0615  0.0779  -0.0466 59  ARG   B N   
743  C CA  . ARG   B 50  ? 0.6577 0.6478 0.4866 0.0655  0.0786  -0.0470 59  ARG   B CA  
744  C C   . ARG   B 50  ? 0.6727 0.6610 0.4904 0.0746  0.0752  -0.0394 59  ARG   B C   
745  O O   . ARG   B 50  ? 0.6483 0.6350 0.4593 0.0798  0.0751  -0.0315 59  ARG   B O   
746  C CB  . ARG   B 50  ? 0.6899 0.6782 0.5381 0.0663  0.0846  -0.0454 59  ARG   B CB  
747  C CG  . ARG   B 50  ? 0.7310 0.7180 0.5900 0.0707  0.0860  -0.0452 59  ARG   B CG  
748  C CD  . ARG   B 50  ? 0.7543 0.7397 0.6348 0.0685  0.0918  -0.0474 59  ARG   B CD  
749  N NE  . ARG   B 50  ? 0.7704 0.7538 0.6554 0.0679  0.0951  -0.0423 59  ARG   B NE  
750  C CZ  . ARG   B 50  ? 0.7879 0.7679 0.6755 0.0750  0.0976  -0.0309 59  ARG   B CZ  
751  N NH1 . ARG   B 50  ? 0.8097 0.7882 0.6951 0.0839  0.0970  -0.0232 59  ARG   B NH1 
752  N NH2 . ARG   B 50  ? 0.8112 0.7905 0.7037 0.0733  0.1007  -0.0273 59  ARG   B NH2 
753  N N   . SER   B 51  ? 0.6913 0.6807 0.5065 0.0764  0.0724  -0.0425 60  SER   B N   
754  C CA  . SER   B 51  ? 0.7221 0.7112 0.5305 0.0859  0.0697  -0.0365 60  SER   B CA  
755  C C   . SER   B 51  ? 0.7515 0.7418 0.5718 0.0889  0.0713  -0.0379 60  SER   B C   
756  O O   . SER   B 51  ? 0.7789 0.7719 0.5981 0.0857  0.0687  -0.0451 60  SER   B O   
757  C CB  . SER   B 51  ? 0.7155 0.7058 0.5078 0.0853  0.0635  -0.0392 60  SER   B CB  
758  O OG  . SER   B 51  ? 0.7249 0.7162 0.5117 0.0942  0.0607  -0.0351 60  SER   B OG  
759  N N   . GLY   B 52  ? 0.7795 0.7681 0.6117 0.0947  0.0757  -0.0312 61  GLY   B N   
760  C CA  . GLY   B 52  ? 0.8055 0.7946 0.6520 0.0967  0.0781  -0.0330 61  GLY   B CA  
761  C C   . GLY   B 52  ? 0.8368 0.8257 0.6970 0.0876  0.0814  -0.0421 61  GLY   B C   
762  O O   . GLY   B 52  ? 0.8502 0.8369 0.7171 0.0835  0.0850  -0.0419 61  GLY   B O   
763  N N   . GLU   B 53  ? 0.8768 0.8688 0.7413 0.0844  0.0803  -0.0506 62  GLU   B N   
764  C CA  . GLU   B 53  ? 0.9093 0.9032 0.7843 0.0749  0.0825  -0.0613 62  GLU   B CA  
765  C C   . GLU   B 53  ? 0.8780 0.8763 0.7400 0.0671  0.0785  -0.0690 62  GLU   B C   
766  O O   . GLU   B 53  ? 0.8646 0.8664 0.7332 0.0593  0.0799  -0.0780 62  GLU   B O   
767  C CB  . GLU   B 53  ? 0.9566 0.9515 0.8472 0.0764  0.0849  -0.0656 62  GLU   B CB  
768  C CG  . GLU   B 53  ? 1.0219 1.0117 0.9304 0.0801  0.0906  -0.0604 62  GLU   B CG  
769  C CD  . GLU   B 53  ? 1.0944 1.0842 1.0202 0.0825  0.0933  -0.0638 62  GLU   B CD  
770  O OE1 . GLU   B 53  ? 1.1737 1.1672 1.0956 0.0858  0.0904  -0.0657 62  GLU   B OE1 
771  O OE2 . GLU   B 53  ? 1.1420 1.1281 1.0857 0.0811  0.0983  -0.0649 62  GLU   B OE2 
772  N N   . GLY   B 54  ? 0.8521 0.8504 0.6971 0.0691  0.0738  -0.0654 63  GLY   B N   
773  C CA  . GLY   B 54  ? 0.8199 0.8211 0.6517 0.0622  0.0700  -0.0704 63  GLY   B CA  
774  C C   . GLY   B 54  ? 0.8013 0.8013 0.6295 0.0576  0.0713  -0.0695 63  GLY   B C   
775  O O   . GLY   B 54  ? 0.8075 0.8038 0.6386 0.0617  0.0737  -0.0626 63  GLY   B O   
776  N N   . ARG   B 55  ? 0.7747 0.7787 0.5973 0.0493  0.0698  -0.0760 64  ARG   B N   
777  C CA  . ARG   B 55  ? 0.7432 0.7479 0.5613 0.0442  0.0705  -0.0761 64  ARG   B CA  
778  C C   . ARG   B 55  ? 0.6942 0.6982 0.4943 0.0434  0.0656  -0.0738 64  ARG   B C   
779  O O   . ARG   B 55  ? 0.7023 0.7078 0.4961 0.0422  0.0622  -0.0764 64  ARG   B O   
780  C CB  . ARG   B 55  ? 0.7591 0.7702 0.5864 0.0356  0.0731  -0.0856 64  ARG   B CB  
781  C CG  . ARG   B 55  ? 0.7825 0.7955 0.6097 0.0312  0.0749  -0.0861 64  ARG   B CG  
782  C CD  . ARG   B 55  ? 0.8184 0.8398 0.6539 0.0229  0.0770  -0.0966 64  ARG   B CD  
783  N NE  . ARG   B 55  ? 0.8374 0.8632 0.6688 0.0179  0.0773  -0.0981 64  ARG   B NE  
784  C CZ  . ARG   B 55  ? 0.8655 0.8960 0.7083 0.0138  0.0807  -0.1037 64  ARG   B CZ  
785  N NH1 . ARG   B 55  ? 0.8718 0.9025 0.7321 0.0138  0.0844  -0.1088 64  ARG   B NH1 
786  N NH2 . ARG   B 55  ? 0.8836 0.9192 0.7207 0.0096  0.0803  -0.1047 64  ARG   B NH2 
787  N N   . LEU   B 56  ? 0.6354 0.6372 0.4283 0.0440  0.0652  -0.0689 65  LEU   B N   
788  C CA  . LEU   B 56  ? 0.6102 0.6110 0.3873 0.0429  0.0609  -0.0669 65  LEU   B CA  
789  C C   . LEU   B 56  ? 0.5794 0.5843 0.3555 0.0358  0.0622  -0.0699 65  LEU   B C   
790  O O   . LEU   B 56  ? 0.5551 0.5598 0.3362 0.0365  0.0652  -0.0675 65  LEU   B O   
791  C CB  . LEU   B 56  ? 0.6103 0.6056 0.3790 0.0512  0.0591  -0.0582 65  LEU   B CB  
792  C CG  . LEU   B 56  ? 0.6249 0.6173 0.3929 0.0598  0.0576  -0.0540 65  LEU   B CG  
793  C CD1 . LEU   B 56  ? 0.6265 0.6154 0.3810 0.0661  0.0538  -0.0478 65  LEU   B CD1 
794  C CD2 . LEU   B 56  ? 0.6342 0.6285 0.4026 0.0584  0.0551  -0.0593 65  LEU   B CD2 
795  N N   . ASP   B 57  ? 0.5754 0.5849 0.3463 0.0291  0.0604  -0.0749 66  ASP   B N   
796  C CA  . ASP   B 57  ? 0.5555 0.5706 0.3238 0.0226  0.0612  -0.0774 66  ASP   B CA  
797  C C   . ASP   B 57  ? 0.5326 0.5444 0.2857 0.0237  0.0574  -0.0720 66  ASP   B C   
798  O O   . ASP   B 57  ? 0.5388 0.5465 0.2829 0.0257  0.0535  -0.0697 66  ASP   B O   
799  C CB  . ASP   B 57  ? 0.5779 0.6016 0.3498 0.0148  0.0618  -0.0855 66  ASP   B CB  
800  C CG  . ASP   B 57  ? 0.5958 0.6231 0.3834 0.0138  0.0655  -0.0919 66  ASP   B CG  
801  O OD1 . ASP   B 57  ? 0.6172 0.6437 0.4148 0.0154  0.0689  -0.0921 66  ASP   B OD1 
802  O OD2 . ASP   B 57  ? 0.6165 0.6470 0.4068 0.0118  0.0650  -0.0964 66  ASP   B OD2 
803  N N   . PRO   B 58  ? 0.5104 0.5244 0.2610 0.0223  0.0583  -0.0702 67  PRO   B N   
804  C CA  . PRO   B 58  ? 0.5058 0.5176 0.2426 0.0228  0.0549  -0.0656 67  PRO   B CA  
805  C C   . PRO   B 58  ? 0.5015 0.5161 0.2313 0.0173  0.0523  -0.0681 67  PRO   B C   
806  O O   . PRO   B 58  ? 0.4938 0.5160 0.2298 0.0112  0.0541  -0.0743 67  PRO   B O   
807  C CB  . PRO   B 58  ? 0.5077 0.5244 0.2467 0.0208  0.0574  -0.0654 67  PRO   B CB  
808  C CG  . PRO   B 58  ? 0.5107 0.5351 0.2640 0.0158  0.0616  -0.0729 67  PRO   B CG  
809  C CD  . PRO   B 58  ? 0.5152 0.5349 0.2767 0.0193  0.0626  -0.0737 67  PRO   B CD  
810  N N   . TYR   B 59  ? 0.4943 0.5035 0.2124 0.0192  0.0482  -0.0636 68  TYR   B N   
811  C CA  . TYR   B 59  ? 0.4894 0.4996 0.2004 0.0144  0.0455  -0.0642 68  TYR   B CA  
812  C C   . TYR   B 59  ? 0.4842 0.4939 0.1849 0.0136  0.0436  -0.0597 68  TYR   B C   
813  O O   . TYR   B 59  ? 0.4815 0.4971 0.1791 0.0076  0.0435  -0.0606 68  TYR   B O   
814  C CB  . TYR   B 59  ? 0.4961 0.4989 0.2036 0.0177  0.0419  -0.0631 68  TYR   B CB  
815  C CG  . TYR   B 59  ? 0.5002 0.5040 0.2031 0.0122  0.0395  -0.0639 68  TYR   B CG  
816  C CD1 . TYR   B 59  ? 0.5053 0.5042 0.1980 0.0123  0.0363  -0.0593 68  TYR   B CD1 
817  C CD2 . TYR   B 59  ? 0.4965 0.5057 0.2056 0.0073  0.0406  -0.0691 68  TYR   B CD2 
818  C CE1 . TYR   B 59  ? 0.5109 0.5097 0.2004 0.0074  0.0342  -0.0593 68  TYR   B CE1 
819  C CE2 . TYR   B 59  ? 0.5003 0.5103 0.2059 0.0024  0.0385  -0.0692 68  TYR   B CE2 
820  C CZ  . TYR   B 59  ? 0.5074 0.5122 0.2034 0.0021  0.0355  -0.0641 68  TYR   B CZ  
821  O OH  . TYR   B 59  ? 0.5177 0.5225 0.2111 -0.0027 0.0337  -0.0633 68  TYR   B OH  
822  N N   . TRP   B 60  ? 0.4749 0.4781 0.1700 0.0199  0.0420  -0.0546 69  TRP   B N   
823  C CA  . TRP   B 60  ? 0.4731 0.4746 0.1581 0.0208  0.0398  -0.0496 69  TRP   B CA  
824  C C   . TRP   B 60  ? 0.4814 0.4818 0.1665 0.0264  0.0410  -0.0464 69  TRP   B C   
825  O O   . TRP   B 60  ? 0.4770 0.4721 0.1646 0.0328  0.0411  -0.0450 69  TRP   B O   
826  C CB  . TRP   B 60  ? 0.4702 0.4629 0.1460 0.0231  0.0351  -0.0462 69  TRP   B CB  
827  C CG  . TRP   B 60  ? 0.4700 0.4597 0.1365 0.0256  0.0329  -0.0409 69  TRP   B CG  
828  C CD1 . TRP   B 60  ? 0.4694 0.4632 0.1309 0.0212  0.0326  -0.0388 69  TRP   B CD1 
829  C CD2 . TRP   B 60  ? 0.4669 0.4500 0.1280 0.0336  0.0310  -0.0368 69  TRP   B CD2 
830  N NE1 . TRP   B 60  ? 0.4719 0.4614 0.1257 0.0260  0.0305  -0.0338 69  TRP   B NE1 
831  C CE2 . TRP   B 60  ? 0.4710 0.4538 0.1243 0.0337  0.0294  -0.0327 69  TRP   B CE2 
832  C CE3 . TRP   B 60  ? 0.4659 0.4442 0.1281 0.0411  0.0305  -0.0359 69  TRP   B CE3 
833  C CZ2 . TRP   B 60  ? 0.4726 0.4504 0.1195 0.0407  0.0274  -0.0285 69  TRP   B CZ2 
834  C CZ3 . TRP   B 60  ? 0.4677 0.4417 0.1232 0.0480  0.0286  -0.0315 69  TRP   B CZ3 
835  C CH2 . TRP   B 60  ? 0.4729 0.4464 0.1210 0.0479  0.0270  -0.0282 69  TRP   B CH2 
836  N N   . GLY   B 61  ? 0.4910 0.4964 0.1729 0.0248  0.0417  -0.0448 70  GLY   B N   
837  C CA  . GLY   B 61  ? 0.4979 0.5020 0.1782 0.0304  0.0423  -0.0408 70  GLY   B CA  
838  C C   . GLY   B 61  ? 0.5085 0.5161 0.1812 0.0295  0.0411  -0.0377 70  GLY   B C   
839  O O   . GLY   B 61  ? 0.5021 0.5167 0.1733 0.0231  0.0413  -0.0396 70  GLY   B O   
840  N N   . ASP   B 62  ? 0.5165 0.5213 0.1851 0.0355  0.0404  -0.0333 71  ASP   B N   
841  C CA  . ASP   B 62  ? 0.5324 0.5402 0.1936 0.0364  0.0391  -0.0296 71  ASP   B CA  
842  C C   . ASP   B 62  ? 0.5313 0.5400 0.1942 0.0420  0.0406  -0.0268 71  ASP   B C   
843  O O   . ASP   B 62  ? 0.5324 0.5333 0.1913 0.0492  0.0389  -0.0232 71  ASP   B O   
844  C CB  . ASP   B 62  ? 0.5601 0.5602 0.2101 0.0384  0.0345  -0.0258 71  ASP   B CB  
845  C CG  . ASP   B 62  ? 0.5958 0.5986 0.2380 0.0393  0.0329  -0.0217 71  ASP   B CG  
846  O OD1 . ASP   B 62  ? 0.6254 0.6316 0.2675 0.0428  0.0339  -0.0198 71  ASP   B OD1 
847  O OD2 . ASP   B 62  ? 0.6697 0.6726 0.3069 0.0358  0.0311  -0.0204 71  ASP   B OD2 
848  N N   . VAL   B 63  ? 0.5223 0.5409 0.1909 0.0388  0.0437  -0.0286 72  VAL   B N   
849  C CA  . VAL   B 63  ? 0.5216 0.5438 0.1940 0.0425  0.0459  -0.0265 72  VAL   B CA  
850  C C   . VAL   B 63  ? 0.5315 0.5495 0.1924 0.0491  0.0426  -0.0203 72  VAL   B C   
851  O O   . VAL   B 63  ? 0.5215 0.5368 0.1828 0.0558  0.0431  -0.0166 72  VAL   B O   
852  C CB  . VAL   B 63  ? 0.5224 0.5573 0.2032 0.0366  0.0493  -0.0309 72  VAL   B CB  
853  C CG1 . VAL   B 63  ? 0.5267 0.5668 0.2073 0.0397  0.0501  -0.0279 72  VAL   B CG1 
854  C CG2 . VAL   B 63  ? 0.5172 0.5552 0.2126 0.0326  0.0534  -0.0366 72  VAL   B CG2 
855  N N   . LYS   B 64  ? 0.5321 0.5486 0.1832 0.0484  0.0390  -0.0186 73  LYS   B N   
856  C CA  . LYS   B 64  ? 0.5444 0.5568 0.1852 0.0550  0.0358  -0.0131 73  LYS   B CA  
857  C C   . LYS   B 64  ? 0.5380 0.5388 0.1740 0.0623  0.0331  -0.0105 73  LYS   B C   
858  O O   . LYS   B 64  ? 0.5526 0.5518 0.1846 0.0693  0.0321  -0.0069 73  LYS   B O   
859  C CB  . LYS   B 64  ? 0.5512 0.5639 0.1832 0.0530  0.0327  -0.0112 73  LYS   B CB  
860  C CG  . LYS   B 64  ? 0.5701 0.5818 0.1941 0.0596  0.0303  -0.0061 73  LYS   B CG  
861  C CD  . LYS   B 64  ? 0.5823 0.5941 0.1980 0.0587  0.0274  -0.0031 73  LYS   B CD  
862  C CE  . LYS   B 64  ? 0.5962 0.6046 0.2042 0.0666  0.0247  0.0017  73  LYS   B CE  
863  N NZ  . LYS   B 64  ? 0.6082 0.6188 0.2093 0.0654  0.0224  0.0050  73  LYS   B NZ  
864  N N   . GLN   B 65  ? 0.5386 0.5326 0.1746 0.0608  0.0316  -0.0126 74  GLN   B N   
865  C CA  . GLN   B 65  ? 0.5411 0.5252 0.1736 0.0674  0.0288  -0.0116 74  GLN   B CA  
866  C C   . GLN   B 65  ? 0.5257 0.5116 0.1657 0.0710  0.0320  -0.0117 74  GLN   B C   
867  O O   . GLN   B 65  ? 0.5183 0.4984 0.1548 0.0785  0.0300  -0.0100 74  GLN   B O   
868  C CB  . GLN   B 65  ? 0.5565 0.5342 0.1882 0.0641  0.0264  -0.0144 74  GLN   B CB  
869  C CG  . GLN   B 65  ? 0.5822 0.5569 0.2074 0.0605  0.0233  -0.0135 74  GLN   B CG  
870  C CD  . GLN   B 65  ? 0.5992 0.5680 0.2251 0.0568  0.0213  -0.0161 74  GLN   B CD  
871  O OE1 . GLN   B 65  ? 0.6289 0.5910 0.2549 0.0605  0.0193  -0.0177 74  GLN   B OE1 
872  N NE2 . GLN   B 65  ? 0.6127 0.5852 0.2395 0.0493  0.0219  -0.0169 74  GLN   B NE2 
873  N N   . ASP   B 66  ? 0.5086 0.5022 0.1586 0.0664  0.0367  -0.0136 75  ASP   B N   
874  C CA  . ASP   B 66  ? 0.5027 0.4984 0.1631 0.0676  0.0408  -0.0140 75  ASP   B CA  
875  C C   . ASP   B 66  ? 0.5019 0.4913 0.1636 0.0693  0.0397  -0.0156 75  ASP   B C   
876  O O   . ASP   B 66  ? 0.4943 0.4817 0.1575 0.0760  0.0404  -0.0128 75  ASP   B O   
877  C CB  . ASP   B 66  ? 0.5067 0.5040 0.1666 0.0750  0.0421  -0.0089 75  ASP   B CB  
878  C CG  . ASP   B 66  ? 0.5045 0.5048 0.1762 0.0762  0.0470  -0.0078 75  ASP   B CG  
879  O OD1 . ASP   B 66  ? 0.4962 0.5005 0.1785 0.0697  0.0504  -0.0115 75  ASP   B OD1 
880  O OD2 . ASP   B 66  ? 0.5054 0.5043 0.1754 0.0844  0.0473  -0.0028 75  ASP   B OD2 
881  N N   . LEU   B 67  ? 0.4956 0.4828 0.1569 0.0639  0.0380  -0.0196 76  LEU   B N   
882  C CA  . LEU   B 67  ? 0.4945 0.4771 0.1580 0.0642  0.0369  -0.0222 76  LEU   B CA  
883  C C   . LEU   B 67  ? 0.4955 0.4821 0.1680 0.0560  0.0395  -0.0275 76  LEU   B C   
884  O O   . LEU   B 67  ? 0.4898 0.4819 0.1630 0.0491  0.0404  -0.0299 76  LEU   B O   
885  C CB  . LEU   B 67  ? 0.5009 0.4763 0.1543 0.0661  0.0315  -0.0221 76  LEU   B CB  
886  C CG  . LEU   B 67  ? 0.5056 0.4761 0.1503 0.0752  0.0281  -0.0183 76  LEU   B CG  
887  C CD1 . LEU   B 67  ? 0.5132 0.4762 0.1504 0.0756  0.0228  -0.0197 76  LEU   B CD1 
888  C CD2 . LEU   B 67  ? 0.5041 0.4747 0.1520 0.0827  0.0293  -0.0167 76  LEU   B CD2 
889  N N   . VAL   B 68  ? 0.4937 0.4783 0.1720 0.0570  0.0402  -0.0295 77  VAL   B N   
890  C CA  . VAL   B 68  ? 0.4850 0.4732 0.1720 0.0499  0.0424  -0.0352 77  VAL   B CA  
891  C C   . VAL   B 68  ? 0.4867 0.4703 0.1743 0.0524  0.0404  -0.0367 77  VAL   B C   
892  O O   . VAL   B 68  ? 0.4806 0.4606 0.1669 0.0604  0.0395  -0.0334 77  VAL   B O   
893  C CB  . VAL   B 68  ? 0.4812 0.4755 0.1807 0.0475  0.0477  -0.0369 77  VAL   B CB  
894  C CG1 . VAL   B 68  ? 0.4805 0.4724 0.1852 0.0548  0.0498  -0.0328 77  VAL   B CG1 
895  C CG2 . VAL   B 68  ? 0.4774 0.4760 0.1864 0.0407  0.0499  -0.0434 77  VAL   B CG2 
896  N N   . SER   B 69  ? 0.4791 0.4636 0.1684 0.0466  0.0395  -0.0413 78  SER   B N   
897  C CA  . SER   B 69  ? 0.4823 0.4643 0.1742 0.0477  0.0381  -0.0440 78  SER   B CA  
898  C C   . SER   B 69  ? 0.4825 0.4701 0.1861 0.0423  0.0417  -0.0492 78  SER   B C   
899  O O   . SER   B 69  ? 0.4798 0.4737 0.1872 0.0349  0.0442  -0.0524 78  SER   B O   
900  C CB  . SER   B 69  ? 0.4868 0.4645 0.1704 0.0460  0.0333  -0.0448 78  SER   B CB  
901  O OG  . SER   B 69  ? 0.4884 0.4702 0.1726 0.0371  0.0338  -0.0478 78  SER   B OG  
902  N N   A TYR   B 70  ? 0.4824 0.4689 0.1917 0.0456  0.0421  -0.0505 79  TYR   B N   
903  N N   B TYR   B 70  ? 0.4824 0.4689 0.1917 0.0456  0.0421  -0.0505 79  TYR   B N   
904  N N   C TYR   B 70  ? 0.4826 0.4690 0.1918 0.0456  0.0420  -0.0505 79  TYR   B N   
905  N N   D TYR   B 70  ? 0.4826 0.4690 0.1918 0.0456  0.0420  -0.0505 79  TYR   B N   
906  C CA  A TYR   B 70  ? 0.4804 0.4715 0.2016 0.0418  0.0454  -0.0555 79  TYR   B CA  
907  C CA  B TYR   B 70  ? 0.4804 0.4715 0.2016 0.0419  0.0454  -0.0555 79  TYR   B CA  
908  C CA  C TYR   B 70  ? 0.4809 0.4719 0.2021 0.0419  0.0454  -0.0554 79  TYR   B CA  
909  C CA  D TYR   B 70  ? 0.4809 0.4719 0.2021 0.0419  0.0454  -0.0554 79  TYR   B CA  
910  C C   A TYR   B 70  ? 0.4840 0.4744 0.2047 0.0408  0.0426  -0.0590 79  TYR   B C   
911  C C   B TYR   B 70  ? 0.4840 0.4744 0.2047 0.0408  0.0426  -0.0590 79  TYR   B C   
912  C C   C TYR   B 70  ? 0.4854 0.4759 0.2062 0.0408  0.0426  -0.0590 79  TYR   B C   
913  C C   D TYR   B 70  ? 0.4854 0.4759 0.2062 0.0408  0.0426  -0.0590 79  TYR   B C   
914  O O   A TYR   B 70  ? 0.4870 0.4728 0.2018 0.0465  0.0390  -0.0568 79  TYR   B O   
915  O O   B TYR   B 70  ? 0.4870 0.4728 0.2018 0.0465  0.0390  -0.0568 79  TYR   B O   
916  O O   C TYR   B 70  ? 0.4876 0.4735 0.2026 0.0464  0.0390  -0.0569 79  TYR   B O   
917  O O   D TYR   B 70  ? 0.4876 0.4735 0.2026 0.0464  0.0390  -0.0569 79  TYR   B O   
918  C CB  A TYR   B 70  ? 0.4794 0.4704 0.2100 0.0473  0.0490  -0.0532 79  TYR   B CB  
919  C CB  B TYR   B 70  ? 0.4794 0.4704 0.2100 0.0473  0.0490  -0.0532 79  TYR   B CB  
920  C CB  C TYR   B 70  ? 0.4795 0.4705 0.2102 0.0473  0.0490  -0.0532 79  TYR   B CB  
921  C CB  D TYR   B 70  ? 0.4795 0.4705 0.2102 0.0473  0.0490  -0.0532 79  TYR   B CB  
922  C CG  A TYR   B 70  ? 0.4779 0.4709 0.2125 0.0468  0.0526  -0.0508 79  TYR   B CG  
923  C CG  B TYR   B 70  ? 0.4779 0.4709 0.2125 0.0468  0.0526  -0.0508 79  TYR   B CG  
924  C CG  C TYR   B 70  ? 0.4779 0.4709 0.2125 0.0468  0.0526  -0.0508 79  TYR   B CG  
925  C CG  D TYR   B 70  ? 0.4780 0.4709 0.2125 0.0468  0.0526  -0.0508 79  TYR   B CG  
926  C CD1 A TYR   B 70  ? 0.4804 0.4707 0.2071 0.0514  0.0515  -0.0450 79  TYR   B CD1 
927  C CD1 B TYR   B 70  ? 0.4804 0.4707 0.2071 0.0514  0.0515  -0.0450 79  TYR   B CD1 
928  C CD1 C TYR   B 70  ? 0.4804 0.4708 0.2072 0.0514  0.0515  -0.0449 79  TYR   B CD1 
929  C CD1 D TYR   B 70  ? 0.4804 0.4708 0.2072 0.0514  0.0515  -0.0449 79  TYR   B CD1 
930  C CD2 A TYR   B 70  ? 0.4764 0.4744 0.2231 0.0417  0.0570  -0.0551 79  TYR   B CD2 
931  C CD2 B TYR   B 70  ? 0.4764 0.4744 0.2231 0.0417  0.0570  -0.0551 79  TYR   B CD2 
932  C CD2 C TYR   B 70  ? 0.4766 0.4746 0.2233 0.0417  0.0570  -0.0551 79  TYR   B CD2 
933  C CD2 D TYR   B 70  ? 0.4766 0.4746 0.2233 0.0417  0.0570  -0.0551 79  TYR   B CD2 
934  C CE1 A TYR   B 70  ? 0.4795 0.4725 0.2105 0.0506  0.0548  -0.0430 79  TYR   B CE1 
935  C CE1 B TYR   B 70  ? 0.4795 0.4725 0.2105 0.0506  0.0548  -0.0430 79  TYR   B CE1 
936  C CE1 C TYR   B 70  ? 0.4796 0.4726 0.2106 0.0507  0.0548  -0.0430 79  TYR   B CE1 
937  C CE1 D TYR   B 70  ? 0.4796 0.4725 0.2106 0.0507  0.0548  -0.0430 79  TYR   B CE1 
938  C CE2 A TYR   B 70  ? 0.4755 0.4759 0.2270 0.0407  0.0601  -0.0538 79  TYR   B CE2 
939  C CE2 B TYR   B 70  ? 0.4755 0.4759 0.2270 0.0407  0.0601  -0.0538 79  TYR   B CE2 
940  C CE2 C TYR   B 70  ? 0.4757 0.4762 0.2272 0.0407  0.0601  -0.0538 79  TYR   B CE2 
941  C CE2 D TYR   B 70  ? 0.4757 0.4761 0.2271 0.0407  0.0601  -0.0538 79  TYR   B CE2 
942  C CZ  A TYR   B 70  ? 0.4768 0.4747 0.2204 0.0451  0.0591  -0.0475 79  TYR   B CZ  
943  C CZ  B TYR   B 70  ? 0.4768 0.4747 0.2204 0.0451  0.0591  -0.0475 79  TYR   B CZ  
944  C CZ  C TYR   B 70  ? 0.4769 0.4748 0.2204 0.0451  0.0591  -0.0475 79  TYR   B CZ  
945  C CZ  D TYR   B 70  ? 0.4769 0.4748 0.2204 0.0451  0.0591  -0.0475 79  TYR   B CZ  
946  O OH  A TYR   B 70  ? 0.4781 0.4792 0.2272 0.0439  0.0623  -0.0463 79  TYR   B OH  
947  O OH  B TYR   B 70  ? 0.4781 0.4792 0.2272 0.0439  0.0623  -0.0463 79  TYR   B OH  
948  O OH  C TYR   B 70  ? 0.4785 0.4797 0.2276 0.0438  0.0623  -0.0464 79  TYR   B OH  
949  O OH  D TYR   B 70  ? 0.4785 0.4797 0.2276 0.0438  0.0623  -0.0464 79  TYR   B OH  
950  N N   A CYS   B 71  ? 0.4830 0.4789 0.2096 0.0336  0.0440  -0.0647 80  CYS   B N   
951  N N   B CYS   B 71  ? 0.4831 0.4789 0.2096 0.0336  0.0440  -0.0647 80  CYS   B N   
952  N N   C CYS   B 71  ? 0.4888 0.4849 0.2161 0.0337  0.0443  -0.0648 80  CYS   B N   
953  N N   D CYS   B 71  ? 0.4888 0.4848 0.2160 0.0337  0.0443  -0.0648 80  CYS   B N   
954  C CA  A CYS   B 71  ? 0.4847 0.4818 0.2137 0.0318  0.0423  -0.0689 80  CYS   B CA  
955  C CA  B CYS   B 71  ? 0.4847 0.4819 0.2137 0.0318  0.0423  -0.0689 80  CYS   B CA  
956  C CA  C CYS   B 71  ? 0.4932 0.4910 0.2235 0.0316  0.0428  -0.0692 80  CYS   B CA  
957  C CA  D CYS   B 71  ? 0.4932 0.4910 0.2235 0.0316  0.0428  -0.0692 80  CYS   B CA  
958  C C   A CYS   B 71  ? 0.4876 0.4823 0.2070 0.0288  0.0379  -0.0687 80  CYS   B C   
959  C C   B CYS   B 71  ? 0.4876 0.4823 0.2070 0.0288  0.0379  -0.0687 80  CYS   B C   
960  C C   C CYS   B 71  ? 0.4943 0.4908 0.2157 0.0273  0.0389  -0.0696 80  CYS   B C   
961  C C   D CYS   B 71  ? 0.4943 0.4908 0.2157 0.0273  0.0389  -0.0696 80  CYS   B C   
962  O O   A CYS   B 71  ? 0.4909 0.4855 0.2111 0.0284  0.0355  -0.0714 80  CYS   B O   
963  O O   B CYS   B 71  ? 0.4909 0.4855 0.2112 0.0283  0.0356  -0.0714 80  CYS   B O   
964  O O   C CYS   B 71  ? 0.4971 0.4968 0.2213 0.0231  0.0382  -0.0738 80  CYS   B O   
965  O O   D CYS   B 71  ? 0.4971 0.4968 0.2213 0.0231  0.0382  -0.0738 80  CYS   B O   
966  C CB  A CYS   B 71  ? 0.4876 0.4820 0.2200 0.0397  0.0414  -0.0678 80  CYS   B CB  
967  C CB  B CYS   B 71  ? 0.4877 0.4820 0.2200 0.0397  0.0414  -0.0678 80  CYS   B CB  
968  C CB  C CYS   B 71  ? 0.5004 0.4951 0.2338 0.0395  0.0419  -0.0680 80  CYS   B CB  
969  C CB  D CYS   B 71  ? 0.5003 0.4951 0.2337 0.0395  0.0419  -0.0680 80  CYS   B CB  
970  S SG  A CYS   B 71  ? 0.4882 0.4817 0.2282 0.0462  0.0458  -0.0636 80  CYS   B SG  
971  S SG  B CYS   B 71  ? 0.4882 0.4817 0.2282 0.0462  0.0458  -0.0636 80  CYS   B SG  
972  S SG  C CYS   B 71  ? 0.5082 0.5055 0.2557 0.0426  0.0474  -0.0681 80  CYS   B SG  
973  S SG  D CYS   B 71  ? 0.5080 0.5053 0.2555 0.0426  0.0474  -0.0681 80  CYS   B SG  
974  N N   A GLY   B 72  ? 0.4876 0.4804 0.1988 0.0269  0.0367  -0.0655 81  GLY   B N   
975  N N   B GLY   B 72  ? 0.4876 0.4804 0.1988 0.0269  0.0367  -0.0655 81  GLY   B N   
976  N N   C GLY   B 72  ? 0.4937 0.4862 0.2055 0.0277  0.0368  -0.0654 81  GLY   B N   
977  N N   D GLY   B 72  ? 0.4937 0.4862 0.2055 0.0278  0.0368  -0.0654 81  GLY   B N   
978  C CA  A GLY   B 72  ? 0.4919 0.4810 0.1945 0.0244  0.0327  -0.0642 81  GLY   B CA  
979  C CA  B GLY   B 72  ? 0.4919 0.4810 0.1945 0.0244  0.0327  -0.0642 81  GLY   B CA  
980  C CA  C GLY   B 72  ? 0.4966 0.4860 0.2001 0.0246  0.0329  -0.0645 81  GLY   B CA  
981  C CA  D GLY   B 72  ? 0.4966 0.4860 0.2001 0.0245  0.0329  -0.0645 81  GLY   B CA  
982  C C   A GLY   B 72  ? 0.4937 0.4784 0.1871 0.0265  0.0314  -0.0588 81  GLY   B C   
983  C C   B GLY   B 72  ? 0.4937 0.4784 0.1871 0.0265  0.0314  -0.0588 81  GLY   B C   
984  C C   C GLY   B 72  ? 0.4977 0.4820 0.1917 0.0277  0.0314  -0.0588 81  GLY   B C   
985  C C   D GLY   B 72  ? 0.4977 0.4820 0.1917 0.0277  0.0314  -0.0588 81  GLY   B C   
986  O O   A GLY   B 72  ? 0.4949 0.4798 0.1885 0.0312  0.0338  -0.0556 81  GLY   B O   
987  O O   B GLY   B 72  ? 0.4950 0.4798 0.1885 0.0312  0.0338  -0.0556 81  GLY   B O   
988  O O   C GLY   B 72  ? 0.5025 0.4870 0.1963 0.0316  0.0336  -0.0558 81  GLY   B O   
989  O O   D GLY   B 72  ? 0.5024 0.4869 0.1962 0.0316  0.0336  -0.0558 81  GLY   B O   
990  N N   A PRO   B 73  ? 0.4977 0.4780 0.1838 0.0239  0.0275  -0.0573 82  PRO   B N   
991  N N   B PRO   B 73  ? 0.4977 0.4780 0.1837 0.0239  0.0275  -0.0573 82  PRO   B N   
992  N N   C PRO   B 73  ? 0.4986 0.4791 0.1854 0.0242  0.0276  -0.0577 82  PRO   B N   
993  N N   D PRO   B 73  ? 0.4986 0.4791 0.1854 0.0242  0.0276  -0.0577 82  PRO   B N   
994  C CA  A PRO   B 73  ? 0.5036 0.4777 0.1803 0.0271  0.0249  -0.0523 82  PRO   B CA  
995  C CA  B PRO   B 73  ? 0.5036 0.4777 0.1803 0.0271  0.0249  -0.0523 82  PRO   B CA  
996  C CA  C PRO   B 73  ? 0.5044 0.4787 0.1816 0.0270  0.0250  -0.0526 82  PRO   B CA  
997  C CA  D PRO   B 73  ? 0.5044 0.4787 0.1816 0.0270  0.0250  -0.0526 82  PRO   B CA  
998  C C   A PRO   B 73  ? 0.5074 0.4752 0.1804 0.0369  0.0226  -0.0502 82  PRO   B C   
999  C C   B PRO   B 73  ? 0.5074 0.4752 0.1804 0.0369  0.0226  -0.0502 82  PRO   B C   
1000 C C   C PRO   B 73  ? 0.5081 0.4757 0.1811 0.0368  0.0223  -0.0503 82  PRO   B C   
1001 C C   D PRO   B 73  ? 0.5081 0.4757 0.1811 0.0368  0.0223  -0.0503 82  PRO   B C   
1002 O O   A PRO   B 73  ? 0.5086 0.4762 0.1856 0.0406  0.0220  -0.0525 82  PRO   B O   
1003 O O   B PRO   B 73  ? 0.5086 0.4762 0.1856 0.0406  0.0220  -0.0525 82  PRO   B O   
1004 O O   C PRO   B 73  ? 0.5125 0.4791 0.1886 0.0404  0.0211  -0.0527 82  PRO   B O   
1005 O O   D PRO   B 73  ? 0.5125 0.4790 0.1886 0.0404  0.0211  -0.0527 82  PRO   B O   
1006 C CB  A PRO   B 73  ? 0.5087 0.4790 0.1815 0.0226  0.0216  -0.0519 82  PRO   B CB  
1007 C CB  B PRO   B 73  ? 0.5087 0.4790 0.1815 0.0226  0.0216  -0.0519 82  PRO   B CB  
1008 C CB  C PRO   B 73  ? 0.5088 0.4795 0.1825 0.0223  0.0218  -0.0525 82  PRO   B CB  
1009 C CB  D PRO   B 73  ? 0.5088 0.4795 0.1825 0.0223  0.0218  -0.0525 82  PRO   B CB  
1010 C CG  A PRO   B 73  ? 0.5079 0.4789 0.1867 0.0210  0.0206  -0.0567 82  PRO   B CG  
1011 C CG  B PRO   B 73  ? 0.5079 0.4789 0.1867 0.0210  0.0206  -0.0567 82  PRO   B CG  
1012 C CG  C PRO   B 73  ? 0.5078 0.4791 0.1876 0.0214  0.0207  -0.0573 82  PRO   B CG  
1013 C CG  D PRO   B 73  ? 0.5078 0.4791 0.1876 0.0214  0.0207  -0.0573 82  PRO   B CG  
1014 C CD  A PRO   B 73  ? 0.5004 0.4787 0.1875 0.0212  0.0246  -0.0602 82  PRO   B CD  
1015 C CD  B PRO   B 73  ? 0.5004 0.4787 0.1875 0.0212  0.0246  -0.0602 82  PRO   B CD  
1016 C CD  C PRO   B 73  ? 0.5003 0.4793 0.1884 0.0211  0.0249  -0.0607 82  PRO   B CD  
1017 C CD  D PRO   B 73  ? 0.5003 0.4793 0.1884 0.0211  0.0249  -0.0607 82  PRO   B CD  
1018 N N   A TRP   B 74  ? 0.5131 0.4772 0.1789 0.0407  0.0214  -0.0458 83  TRP   B N   
1019 N N   B TRP   B 74  ? 0.5131 0.4772 0.1789 0.0407  0.0214  -0.0458 83  TRP   B N   
1020 N N   C TRP   B 74  ? 0.5131 0.4774 0.1792 0.0407  0.0215  -0.0459 83  TRP   B N   
1021 N N   D TRP   B 74  ? 0.5131 0.4774 0.1792 0.0407  0.0215  -0.0459 83  TRP   B N   
1022 C CA  A TRP   B 74  ? 0.5188 0.4773 0.1790 0.0502  0.0186  -0.0431 83  TRP   B CA  
1023 C CA  B TRP   B 74  ? 0.5188 0.4773 0.1790 0.0502  0.0186  -0.0431 83  TRP   B CA  
1024 C CA  C TRP   B 74  ? 0.5188 0.4774 0.1791 0.0501  0.0186  -0.0432 83  TRP   B CA  
1025 C CA  D TRP   B 74  ? 0.5188 0.4774 0.1791 0.0501  0.0186  -0.0432 83  TRP   B CA  
1026 C C   A TRP   B 74  ? 0.5317 0.4837 0.1889 0.0528  0.0134  -0.0453 83  TRP   B C   
1027 C C   B TRP   B 74  ? 0.5317 0.4837 0.1889 0.0528  0.0134  -0.0453 83  TRP   B C   
1028 C C   C TRP   B 74  ? 0.5319 0.4840 0.1891 0.0528  0.0135  -0.0453 83  TRP   B C   
1029 C C   D TRP   B 74  ? 0.5319 0.4840 0.1891 0.0528  0.0135  -0.0453 83  TRP   B C   
1030 O O   A TRP   B 74  ? 0.5361 0.4843 0.1908 0.0481  0.0110  -0.0456 83  TRP   B O   
1031 O O   B TRP   B 74  ? 0.5361 0.4844 0.1908 0.0481  0.0110  -0.0456 83  TRP   B O   
1032 O O   C TRP   B 74  ? 0.5362 0.4845 0.1910 0.0481  0.0111  -0.0457 83  TRP   B O   
1033 O O   D TRP   B 74  ? 0.5362 0.4845 0.1910 0.0481  0.0111  -0.0457 83  TRP   B O   
1034 C CB  A TRP   B 74  ? 0.5184 0.4750 0.1714 0.0520  0.0182  -0.0385 83  TRP   B CB  
1035 C CB  B TRP   B 74  ? 0.5184 0.4750 0.1714 0.0520  0.0182  -0.0385 83  TRP   B CB  
1036 C CB  C TRP   B 74  ? 0.5186 0.4753 0.1717 0.0520  0.0182  -0.0385 83  TRP   B CB  
1037 C CB  D TRP   B 74  ? 0.5186 0.4753 0.1717 0.0520  0.0182  -0.0385 83  TRP   B CB  
1038 C CG  A TRP   B 74  ? 0.5169 0.4699 0.1647 0.0618  0.0162  -0.0357 83  TRP   B CG  
1039 C CG  B TRP   B 74  ? 0.5169 0.4699 0.1647 0.0618  0.0162  -0.0357 83  TRP   B CG  
1040 C CG  C TRP   B 74  ? 0.5169 0.4699 0.1647 0.0618  0.0163  -0.0357 83  TRP   B CG  
1041 C CG  D TRP   B 74  ? 0.5169 0.4699 0.1647 0.0617  0.0163  -0.0357 83  TRP   B CG  
1042 C CD1 A TRP   B 74  ? 0.5229 0.4691 0.1638 0.0672  0.0114  -0.0353 83  TRP   B CD1 
1043 C CD1 B TRP   B 74  ? 0.5229 0.4691 0.1638 0.0672  0.0114  -0.0353 83  TRP   B CD1 
1044 C CD1 C TRP   B 74  ? 0.5230 0.4692 0.1639 0.0672  0.0114  -0.0353 83  TRP   B CD1 
1045 C CD1 D TRP   B 74  ? 0.5230 0.4692 0.1639 0.0672  0.0114  -0.0353 83  TRP   B CD1 
1046 C CD2 A TRP   B 74  ? 0.5112 0.4681 0.1607 0.0673  0.0192  -0.0331 83  TRP   B CD2 
1047 C CD2 B TRP   B 74  ? 0.5112 0.4681 0.1607 0.0673  0.0192  -0.0331 83  TRP   B CD2 
1048 C CD2 C TRP   B 74  ? 0.5112 0.4681 0.1607 0.0673  0.0192  -0.0331 83  TRP   B CD2 
1049 C CD2 D TRP   B 74  ? 0.5112 0.4681 0.1607 0.0673  0.0192  -0.0331 83  TRP   B CD2 
1050 N NE1 A TRP   B 74  ? 0.5221 0.4685 0.1596 0.0761  0.0111  -0.0328 83  TRP   B NE1 
1051 N NE1 B TRP   B 74  ? 0.5221 0.4685 0.1596 0.0761  0.0111  -0.0328 83  TRP   B NE1 
1052 N NE1 C TRP   B 74  ? 0.5221 0.4685 0.1597 0.0761  0.0111  -0.0328 83  TRP   B NE1 
1053 N NE1 D TRP   B 74  ? 0.5221 0.4685 0.1597 0.0761  0.0111  -0.0328 83  TRP   B NE1 
1054 C CE2 A TRP   B 74  ? 0.5153 0.4682 0.1580 0.0763  0.0160  -0.0309 83  TRP   B CE2 
1055 C CE2 B TRP   B 74  ? 0.5153 0.4682 0.1580 0.0763  0.0160  -0.0309 83  TRP   B CE2 
1056 C CE2 C TRP   B 74  ? 0.5153 0.4683 0.1580 0.0763  0.0160  -0.0309 83  TRP   B CE2 
1057 C CE2 D TRP   B 74  ? 0.5153 0.4683 0.1580 0.0763  0.0160  -0.0309 83  TRP   B CE2 
1058 C CE3 A TRP   B 74  ? 0.5040 0.4673 0.1609 0.0656  0.0244  -0.0325 83  TRP   B CE3 
1059 C CE3 B TRP   B 74  ? 0.5039 0.4673 0.1609 0.0656  0.0244  -0.0325 83  TRP   B CE3 
1060 C CE3 C TRP   B 74  ? 0.5039 0.4673 0.1608 0.0656  0.0244  -0.0325 83  TRP   B CE3 
1061 C CE3 D TRP   B 74  ? 0.5039 0.4673 0.1608 0.0656  0.0244  -0.0325 83  TRP   B CE3 
1062 C CZ2 A TRP   B 74  ? 0.5128 0.4688 0.1553 0.0835  0.0180  -0.0273 83  TRP   B CZ2 
1063 C CZ2 B TRP   B 74  ? 0.5128 0.4688 0.1553 0.0835  0.0180  -0.0273 83  TRP   B CZ2 
1064 C CZ2 C TRP   B 74  ? 0.5128 0.4688 0.1553 0.0835  0.0180  -0.0273 83  TRP   B CZ2 
1065 C CZ2 D TRP   B 74  ? 0.5128 0.4688 0.1553 0.0835  0.0180  -0.0273 83  TRP   B CZ2 
1066 C CZ3 A TRP   B 74  ? 0.5027 0.4680 0.1604 0.0724  0.0264  -0.0289 83  TRP   B CZ3 
1067 C CZ3 B TRP   B 74  ? 0.5027 0.4680 0.1604 0.0724  0.0264  -0.0289 83  TRP   B CZ3 
1068 C CZ3 C TRP   B 74  ? 0.5029 0.4681 0.1605 0.0724  0.0264  -0.0289 83  TRP   B CZ3 
1069 C CZ3 D TRP   B 74  ? 0.5029 0.4681 0.1605 0.0724  0.0264  -0.0289 83  TRP   B CZ3 
1070 C CH2 A TRP   B 74  ? 0.5065 0.4685 0.1567 0.0812  0.0233  -0.0260 83  TRP   B CH2 
1071 C CH2 B TRP   B 74  ? 0.5065 0.4685 0.1567 0.0812  0.0233  -0.0260 83  TRP   B CH2 
1072 C CH2 C TRP   B 74  ? 0.5064 0.4684 0.1566 0.0812  0.0233  -0.0260 83  TRP   B CH2 
1073 C CH2 D TRP   B 74  ? 0.5064 0.4684 0.1566 0.0812  0.0233  -0.0260 83  TRP   B CH2 
1074 N N   . LYS   B 75  ? 0.5382 0.4894 0.1957 0.0605  0.0118  -0.0465 84  LYS   B N   
1075 C CA  . LYS   B 75  ? 0.5600 0.5069 0.2161 0.0634  0.0068  -0.0501 84  LYS   B CA  
1076 C C   . LYS   B 75  ? 0.5800 0.5219 0.2283 0.0723  0.0028  -0.0487 84  LYS   B C   
1077 O O   . LYS   B 75  ? 0.6069 0.5445 0.2537 0.0737  -0.0018 -0.0521 84  LYS   B O   
1078 C CB  . LYS   B 75  ? 0.5727 0.5244 0.2349 0.0665  0.0075  -0.0532 84  LYS   B CB  
1079 C CG  . LYS   B 75  ? 0.5716 0.5289 0.2425 0.0592  0.0113  -0.0557 84  LYS   B CG  
1080 C CD  . LYS   B 75  ? 0.5944 0.5505 0.2673 0.0512  0.0095  -0.0593 84  LYS   B CD  
1081 C CE  . LYS   B 75  ? 0.5938 0.5569 0.2753 0.0442  0.0134  -0.0620 84  LYS   B CE  
1082 N NZ  . LYS   B 75  ? 0.6126 0.5756 0.2963 0.0366  0.0117  -0.0652 84  LYS   B NZ  
1083 N N   . LEU   B 76  ? 0.5887 0.5316 0.2329 0.0779  0.0043  -0.0443 85  LEU   B N   
1084 C CA  . LEU   B 76  ? 0.6099 0.5503 0.2470 0.0880  0.0008  -0.0432 85  LEU   B CA  
1085 C C   . LEU   B 76  ? 0.6346 0.5678 0.2653 0.0871  -0.0022 -0.0422 85  LEU   B C   
1086 O O   . LEU   B 76  ? 0.6319 0.5652 0.2611 0.0833  0.0002  -0.0383 85  LEU   B O   
1087 C CB  . LEU   B 76  ? 0.5987 0.5446 0.2355 0.0941  0.0047  -0.0385 85  LEU   B CB  
1088 C CG  . LEU   B 76  ? 0.5947 0.5470 0.2398 0.0932  0.0090  -0.0384 85  LEU   B CG  
1089 C CD1 . LEU   B 76  ? 0.5957 0.5530 0.2417 0.0994  0.0129  -0.0331 85  LEU   B CD1 
1090 C CD2 . LEU   B 76  ? 0.6074 0.5607 0.2551 0.0956  0.0062  -0.0430 85  LEU   B CD2 
1091 N N   . ASP   B 77  ? 0.6634 0.5908 0.2913 0.0898  -0.0076 -0.0459 86  ASP   B N   
1092 C CA  . ASP   B 77  ? 0.7041 0.6233 0.3276 0.0882  -0.0108 -0.0451 86  ASP   B CA  
1093 C C   . ASP   B 77  ? 0.6869 0.6024 0.3041 0.0982  -0.0154 -0.0465 86  ASP   B C   
1094 O O   . ASP   B 77  ? 0.6845 0.5931 0.2980 0.0985  -0.0181 -0.0458 86  ASP   B O   
1095 C CB  . ASP   B 77  ? 0.7573 0.6715 0.3852 0.0796  -0.0127 -0.0482 86  ASP   B CB  
1096 C CG  . ASP   B 77  ? 0.8106 0.7250 0.4428 0.0808  -0.0159 -0.0548 86  ASP   B CG  
1097 O OD1 . ASP   B 77  ? 0.8810 0.8003 0.5124 0.0885  -0.0164 -0.0568 86  ASP   B OD1 
1098 O OD2 . ASP   B 77  ? 0.8785 0.7886 0.5149 0.0743  -0.0178 -0.0577 86  ASP   B OD2 
1099 N N   . ALA   B 78  ? 0.6647 0.5855 0.2803 0.1070  -0.0161 -0.0481 87  ALA   B N   
1100 C CA  . ALA   B 78  ? 0.6618 0.5806 0.2713 0.1169  -0.0207 -0.0502 87  ALA   B CA  
1101 C C   . ALA   B 78  ? 0.6516 0.5700 0.2552 0.1202  -0.0190 -0.0445 87  ALA   B C   
1102 O O   . ALA   B 78  ? 0.6318 0.5548 0.2366 0.1168  -0.0137 -0.0389 87  ALA   B O   
1103 C CB  . ALA   B 78  ? 0.6659 0.5926 0.2751 0.1255  -0.0214 -0.0528 87  ALA   B CB  
1104 N N   . ALA   B 79  ? 0.6562 0.5699 0.2543 0.1269  -0.0235 -0.0464 88  ALA   B N   
1105 C CA  . ALA   B 79  ? 0.6624 0.5759 0.2545 0.1315  -0.0228 -0.0417 88  ALA   B CA  
1106 C C   . ALA   B 79  ? 0.6632 0.5806 0.2496 0.1439  -0.0258 -0.0439 88  ALA   B C   
1107 O O   . ALA   B 79  ? 0.6593 0.5746 0.2457 0.1480  -0.0307 -0.0506 88  ALA   B O   
1108 C CB  . ALA   B 79  ? 0.6765 0.5798 0.2676 0.1270  -0.0253 -0.0413 88  ALA   B CB  
1109 N N   . TRP   B 80  ? 0.6632 0.5866 0.2453 0.1494  -0.0230 -0.0385 89  TRP   B N   
1110 C CA  . TRP   B 80  ? 0.6816 0.6084 0.2569 0.1612  -0.0256 -0.0394 89  TRP   B CA  
1111 C C   . TRP   B 80  ? 0.7009 0.6177 0.2738 0.1632  -0.0318 -0.0449 89  TRP   B C   
1112 O O   . TRP   B 80  ? 0.6766 0.5846 0.2508 0.1561  -0.0320 -0.0431 89  TRP   B O   
1113 C CB  . TRP   B 80  ? 0.6789 0.6124 0.2508 0.1647  -0.0213 -0.0321 89  TRP   B CB  
1114 C CG  . TRP   B 80  ? 0.6813 0.6203 0.2465 0.1772  -0.0237 -0.0330 89  TRP   B CG  
1115 C CD1 . TRP   B 80  ? 0.6905 0.6352 0.2536 0.1860  -0.0266 -0.0377 89  TRP   B CD1 
1116 C CD2 . TRP   B 80  ? 0.6873 0.6282 0.2472 0.1827  -0.0234 -0.0296 89  TRP   B CD2 
1117 N NE1 . TRP   B 80  ? 0.6915 0.6416 0.2481 0.1965  -0.0281 -0.0374 89  TRP   B NE1 
1118 C CE2 . TRP   B 80  ? 0.6865 0.6339 0.2411 0.1947  -0.0263 -0.0325 89  TRP   B CE2 
1119 C CE3 . TRP   B 80  ? 0.6792 0.6176 0.2381 0.1790  -0.0213 -0.0246 89  TRP   B CE3 
1120 C CZ2 . TRP   B 80  ? 0.6899 0.6416 0.2386 0.2030  -0.0267 -0.0306 89  TRP   B CZ2 
1121 C CZ3 . TRP   B 80  ? 0.6821 0.6242 0.2353 0.1871  -0.0220 -0.0226 89  TRP   B CZ3 
1122 C CH2 . TRP   B 80  ? 0.6888 0.6374 0.2370 0.1989  -0.0245 -0.0255 89  TRP   B CH2 
1123 N N   . ASP   B 81  ? 0.7097 0.6280 0.2797 0.1723  -0.0366 -0.0514 90  ASP   B N   
1124 C CA  . ASP   B 81  ? 0.7371 0.6455 0.3063 0.1748  -0.0431 -0.0582 90  ASP   B CA  
1125 C C   . ASP   B 81  ? 0.7521 0.6578 0.3160 0.1790  -0.0433 -0.0544 90  ASP   B C   
1126 O O   . ASP   B 81  ? 0.7815 0.6759 0.3461 0.1777  -0.0471 -0.0571 90  ASP   B O   
1127 C CB  . ASP   B 81  ? 0.7351 0.6473 0.3036 0.1834  -0.0484 -0.0676 90  ASP   B CB  
1128 C CG  . ASP   B 81  ? 0.7457 0.6709 0.3076 0.1959  -0.0481 -0.0672 90  ASP   B CG  
1129 O OD1 . ASP   B 81  ? 0.7532 0.6830 0.3111 0.1984  -0.0442 -0.0598 90  ASP   B OD1 
1130 O OD2 . ASP   B 81  ? 0.7482 0.6800 0.3093 0.2030  -0.0516 -0.0741 90  ASP   B OD2 
1131 N N   . GLY   B 82  ? 0.7603 0.6759 0.3198 0.1839  -0.0391 -0.0481 91  GLY   B N   
1132 C CA  . GLY   B 82  ? 0.7602 0.6767 0.3142 0.1897  -0.0389 -0.0444 91  GLY   B CA  
1133 C C   . GLY   B 82  ? 0.7837 0.7075 0.3318 0.2033  -0.0421 -0.0487 91  GLY   B C   
1134 O O   . GLY   B 82  ? 0.7909 0.7155 0.3344 0.2089  -0.0425 -0.0466 91  GLY   B O   
1135 N N   . LEU   B 83  ? 0.7903 0.7196 0.3385 0.2086  -0.0447 -0.0550 92  LEU   B N   
1136 C CA  . LEU   B 83  ? 0.8150 0.7520 0.3577 0.2220  -0.0487 -0.0610 92  LEU   B CA  
1137 C C   . LEU   B 83  ? 0.8084 0.7610 0.3493 0.2283  -0.0462 -0.0597 92  LEU   B C   
1138 O O   . LEU   B 83  ? 0.7971 0.7614 0.3320 0.2395  -0.0461 -0.0590 92  LEU   B O   
1139 C CB  . LEU   B 83  ? 0.8522 0.7803 0.3974 0.2232  -0.0560 -0.0724 92  LEU   B CB  
1140 C CG  . LEU   B 83  ? 0.8834 0.7971 0.4297 0.2217  -0.0602 -0.0756 92  LEU   B CG  
1141 C CD1 . LEU   B 83  ? 0.9075 0.8140 0.4579 0.2234  -0.0672 -0.0877 92  LEU   B CD1 
1142 C CD2 . LEU   B 83  ? 0.8935 0.8112 0.4332 0.2314  -0.0605 -0.0737 92  LEU   B CD2 
1143 N N   . SER   B 84  ? 0.7868 0.7403 0.3326 0.2226  -0.0450 -0.0603 93  SER   B N   
1144 C CA  . SER   B 84  ? 0.7845 0.7518 0.3293 0.2294  -0.0443 -0.0612 93  SER   B CA  
1145 C C   . SER   B 84  ? 0.7622 0.7393 0.3073 0.2286  -0.0366 -0.0501 93  SER   B C   
1146 O O   . SER   B 84  ? 0.7577 0.7294 0.3063 0.2195  -0.0320 -0.0433 93  SER   B O   
1147 C CB  . SER   B 84  ? 0.7882 0.7520 0.3385 0.2243  -0.0470 -0.0677 93  SER   B CB  
1148 O OG  . SER   B 84  ? 0.7936 0.7450 0.3462 0.2214  -0.0531 -0.0768 93  SER   B OG  
1149 N N   . GLU   B 85  ? 0.7415 0.7331 0.2837 0.2381  -0.0355 -0.0486 94  GLU   B N   
1150 C CA  . GLU   B 85  ? 0.7221 0.7244 0.2662 0.2385  -0.0284 -0.0384 94  GLU   B CA  
1151 C C   . GLU   B 85  ? 0.6906 0.6887 0.2426 0.2289  -0.0265 -0.0383 94  GLU   B C   
1152 O O   . GLU   B 85  ? 0.6908 0.6813 0.2467 0.2234  -0.0308 -0.0465 94  GLU   B O   
1153 C CB  . GLU   B 85  ? 0.7292 0.7486 0.2678 0.2520  -0.0283 -0.0371 94  GLU   B CB  
1154 C CG  . GLU   B 85  ? 0.7362 0.7637 0.2683 0.2610  -0.0270 -0.0331 94  GLU   B CG  
1155 C CD  . GLU   B 85  ? 0.7630 0.8097 0.2899 0.2741  -0.0253 -0.0290 94  GLU   B CD  
1156 O OE1 . GLU   B 85  ? 0.7468 0.8018 0.2755 0.2767  -0.0240 -0.0273 94  GLU   B OE1 
1157 O OE2 . GLU   B 85  ? 0.7732 0.8274 0.2942 0.2823  -0.0250 -0.0271 94  GLU   B OE2 
1158 N N   . VAL   B 86  ? 0.6645 0.6638 0.2212 0.2229  -0.0193 -0.0286 95  VAL   B N   
1159 C CA  . VAL   B 86  ? 0.6402 0.6359 0.2052 0.2131  -0.0157 -0.0263 95  VAL   B CA  
1160 C C   . VAL   B 86  ? 0.6299 0.6375 0.1979 0.2173  -0.0099 -0.0179 95  VAL   B C   
1161 O O   . VAL   B 86  ? 0.6541 0.6719 0.2173 0.2268  -0.0082 -0.0130 95  VAL   B O   
1162 C CB  . VAL   B 86  ? 0.6214 0.6066 0.1911 0.2008  -0.0127 -0.0234 95  VAL   B CB  
1163 C CG1 . VAL   B 86  ? 0.6265 0.6005 0.1931 0.1977  -0.0180 -0.0298 95  VAL   B CG1 
1164 C CG2 . VAL   B 86  ? 0.6173 0.6077 0.1872 0.2015  -0.0068 -0.0143 95  VAL   B CG2 
1165 N N   . GLN   B 87  ? 0.6144 0.6207 0.1902 0.2105  -0.0067 -0.0159 96  GLN   B N   
1166 C CA  . GLN   B 87  ? 0.6083 0.6242 0.1888 0.2135  -0.0005 -0.0072 96  GLN   B CA  
1167 C C   . GLN   B 87  ? 0.5916 0.6017 0.1815 0.2023  0.0053  -0.0023 96  GLN   B C   
1168 O O   . GLN   B 87  ? 0.6041 0.6059 0.1983 0.1934  0.0040  -0.0072 96  GLN   B O   
1169 C CB  . GLN   B 87  ? 0.6057 0.6288 0.1870 0.2192  -0.0023 -0.0095 96  GLN   B CB  
1170 C CG  . GLN   B 87  ? 0.6150 0.6473 0.1871 0.2319  -0.0076 -0.0139 96  GLN   B CG  
1171 C CD  . GLN   B 87  ? 0.6178 0.6605 0.1905 0.2389  -0.0089 -0.0149 96  GLN   B CD  
1172 O OE1 . GLN   B 87  ? 0.6133 0.6547 0.1934 0.2339  -0.0066 -0.0135 96  GLN   B OE1 
1173 N NE2 . GLN   B 87  ? 0.6239 0.6785 0.1885 0.2515  -0.0123 -0.0168 96  GLN   B NE2 
1174 N N   . LEU   B 88  ? 0.5793 0.5943 0.1721 0.2031  0.0113  0.0066  97  LEU   B N   
1175 C CA  . LEU   B 88  ? 0.5691 0.5819 0.1727 0.1944  0.0179  0.0120  97  LEU   B CA  
1176 C C   . LEU   B 88  ? 0.5674 0.5862 0.1770 0.1978  0.0206  0.0156  97  LEU   B C   
1177 O O   . LEU   B 88  ? 0.5721 0.6015 0.1797 0.2079  0.0225  0.0219  97  LEU   B O   
1178 C CB  . LEU   B 88  ? 0.5665 0.5830 0.1719 0.1946  0.0231  0.0199  97  LEU   B CB  
1179 C CG  . LEU   B 88  ? 0.5599 0.5759 0.1777 0.1870  0.0302  0.0257  97  LEU   B CG  
1180 C CD1 . LEU   B 88  ? 0.5566 0.5624 0.1793 0.1742  0.0297  0.0199  97  LEU   B CD1 
1181 C CD2 . LEU   B 88  ? 0.5596 0.5814 0.1795 0.1889  0.0352  0.0337  97  LEU   B CD2 
1182 N N   A LEU   B 89  ? 0.5615 0.5747 0.1782 0.1901  0.0207  0.0119  98  LEU   B N   
1183 N N   B LEU   B 89  ? 0.5615 0.5747 0.1782 0.1901  0.0207  0.0119  98  LEU   B N   
1184 N N   C LEU   B 89  ? 0.5619 0.5752 0.1784 0.1902  0.0206  0.0118  98  LEU   B N   
1185 N N   D LEU   B 89  ? 0.5619 0.5752 0.1784 0.1902  0.0206  0.0118  98  LEU   B N   
1186 C CA  A LEU   B 89  ? 0.5595 0.5771 0.1842 0.1915  0.0242  0.0157  98  LEU   B CA  
1187 C CA  B LEU   B 89  ? 0.5595 0.5771 0.1842 0.1915  0.0242  0.0157  98  LEU   B CA  
1188 C CA  C LEU   B 89  ? 0.5599 0.5777 0.1846 0.1917  0.0242  0.0158  98  LEU   B CA  
1189 C CA  D LEU   B 89  ? 0.5599 0.5777 0.1846 0.1917  0.0242  0.0158  98  LEU   B CA  
1190 C C   A LEU   B 89  ? 0.5552 0.5725 0.1909 0.1861  0.0319  0.0235  98  LEU   B C   
1191 C C   B LEU   B 89  ? 0.5552 0.5725 0.1909 0.1861  0.0319  0.0235  98  LEU   B C   
1192 C C   C LEU   B 89  ? 0.5555 0.5727 0.1910 0.1861  0.0319  0.0234  98  LEU   B C   
1193 C C   D LEU   B 89  ? 0.5555 0.5727 0.1910 0.1861  0.0319  0.0234  98  LEU   B C   
1194 O O   A LEU   B 89  ? 0.5516 0.5625 0.1960 0.1762  0.0340  0.0210  98  LEU   B O   
1195 O O   B LEU   B 89  ? 0.5516 0.5625 0.1960 0.1762  0.0340  0.0210  98  LEU   B O   
1196 O O   C LEU   B 89  ? 0.5519 0.5625 0.1959 0.1760  0.0339  0.0208  98  LEU   B O   
1197 O O   D LEU   B 89  ? 0.5519 0.5625 0.1959 0.1760  0.0339  0.0208  98  LEU   B O   
1198 C CB  A LEU   B 89  ? 0.5571 0.5689 0.1845 0.1855  0.0206  0.0073  98  LEU   B CB  
1199 C CB  B LEU   B 89  ? 0.5571 0.5689 0.1845 0.1855  0.0206  0.0073  98  LEU   B CB  
1200 C CB  C LEU   B 89  ? 0.5578 0.5702 0.1855 0.1860  0.0208  0.0078  98  LEU   B CB  
1201 C CB  D LEU   B 89  ? 0.5578 0.5702 0.1855 0.1860  0.0208  0.0078  98  LEU   B CB  
1202 C CG  A LEU   B 89  ? 0.5546 0.5696 0.1910 0.1857  0.0235  0.0096  98  LEU   B CG  
1203 C CG  B LEU   B 89  ? 0.5546 0.5696 0.1910 0.1857  0.0235  0.0096  98  LEU   B CG  
1204 C CG  C LEU   B 89  ? 0.5567 0.5742 0.1918 0.1888  0.0233  0.0106  98  LEU   B CG  
1205 C CG  D LEU   B 89  ? 0.5567 0.5742 0.1918 0.1888  0.0233  0.0106  98  LEU   B CG  
1206 C CD1 A LEU   B 89  ? 0.5557 0.5797 0.1962 0.1935  0.0292  0.0205  98  LEU   B CD1 
1207 C CD1 B LEU   B 89  ? 0.5557 0.5797 0.1962 0.1935  0.0292  0.0205  98  LEU   B CD1 
1208 C CD1 C LEU   B 89  ? 0.5632 0.5926 0.1930 0.2024  0.0226  0.0154  98  LEU   B CD1 
1209 C CD1 D LEU   B 89  ? 0.5632 0.5926 0.1930 0.2024  0.0226  0.0154  98  LEU   B CD1 
1210 C CD2 A LEU   B 89  ? 0.5584 0.5757 0.1912 0.1894  0.0177  0.0024  98  LEU   B CD2 
1211 C CD2 B LEU   B 89  ? 0.5584 0.5757 0.1912 0.1894  0.0177  0.0024  98  LEU   B CD2 
1212 C CD2 C LEU   B 89  ? 0.5554 0.5683 0.1929 0.1832  0.0194  0.0018  98  LEU   B CD2 
1213 C CD2 D LEU   B 89  ? 0.5554 0.5683 0.1929 0.1832  0.0194  0.0018  98  LEU   B CD2 
1214 N N   . ALA   B 90  ? 0.5574 0.5818 0.1928 0.1924  0.0359  0.0322  99  ALA   B N   
1215 C CA  . ALA   B 90  ? 0.5517 0.5767 0.1982 0.1881  0.0434  0.0400  99  ALA   B CA  
1216 C C   . ALA   B 90  ? 0.5512 0.5776 0.2091 0.1879  0.0476  0.0442  99  ALA   B C   
1217 O O   . ALA   B 90  ? 0.5494 0.5830 0.2049 0.1975  0.0468  0.0476  99  ALA   B O   
1218 C CB  . ALA   B 90  ? 0.5567 0.5894 0.2001 0.1951  0.0463  0.0483  99  ALA   B CB  
1219 N N   . VAL   B 91  ? 0.5439 0.5640 0.2137 0.1777  0.0517  0.0435  100 VAL   B N   
1220 C CA  . VAL   B 91  ? 0.5409 0.5612 0.2249 0.1760  0.0571  0.0482  100 VAL   B CA  
1221 C C   . VAL   B 91  ? 0.5432 0.5638 0.2385 0.1721  0.0642  0.0552  100 VAL   B C   
1222 O O   . VAL   B 91  ? 0.5334 0.5483 0.2378 0.1618  0.0665  0.0515  100 VAL   B O   
1223 C CB  . VAL   B 91  ? 0.5341 0.5474 0.2232 0.1677  0.0552  0.0395  100 VAL   B CB  
1224 C CG1 . VAL   B 91  ? 0.5313 0.5449 0.2343 0.1673  0.0600  0.0434  100 VAL   B CG1 
1225 C CG2 . VAL   B 91  ? 0.5383 0.5511 0.2157 0.1706  0.0477  0.0316  100 VAL   B CG2 
1226 N N   . PRO   B 92  ? 0.5459 0.5741 0.2416 0.1801  0.0680  0.0656  101 PRO   B N   
1227 C CA  . PRO   B 92  ? 0.5448 0.5742 0.2521 0.1768  0.0748  0.0729  101 PRO   B CA  
1228 C C   . PRO   B 92  ? 0.5466 0.5730 0.2718 0.1727  0.0807  0.0765  101 PRO   B C   
1229 O O   . PRO   B 92  ? 0.5523 0.5781 0.2798 0.1756  0.0800  0.0763  101 PRO   B O   
1230 C CB  . PRO   B 92  ? 0.5520 0.5917 0.2529 0.1880  0.0765  0.0831  101 PRO   B CB  
1231 C CG  . PRO   B 92  ? 0.5537 0.5971 0.2376 0.1962  0.0692  0.0785  101 PRO   B CG  
1232 C CD  . PRO   B 92  ? 0.5539 0.5916 0.2391 0.1932  0.0658  0.0711  101 PRO   B CD  
1233 N N   . PRO   B 93  ? 0.5541 0.5787 0.2932 0.1660  0.0866  0.0795  102 PRO   B N   
1234 C CA  . PRO   B 93  ? 0.5627 0.5835 0.3206 0.1616  0.0924  0.0822  102 PRO   B CA  
1235 C C   . PRO   B 93  ? 0.5740 0.6004 0.3376 0.1716  0.0968  0.0950  102 PRO   B C   
1236 O O   . PRO   B 93  ? 0.5827 0.6164 0.3435 0.1782  0.0992  0.1044  102 PRO   B O   
1237 C CB  . PRO   B 93  ? 0.5587 0.5775 0.3285 0.1525  0.0969  0.0815  102 PRO   B CB  
1238 C CG  . PRO   B 93  ? 0.5553 0.5742 0.3106 0.1493  0.0914  0.0737  102 PRO   B CG  
1239 C CD  . PRO   B 93  ? 0.5592 0.5843 0.2978 0.1608  0.0876  0.0784  102 PRO   B CD  
1240 N N   . GLY   B 94  ? 0.5796 0.6033 0.3504 0.1727  0.0975  0.0951  103 GLY   B N   
1241 C CA  . GLY   B 94  ? 0.5965 0.6251 0.3734 0.1822  0.1013  0.1069  103 GLY   B CA  
1242 C C   . GLY   B 94  ? 0.6093 0.6479 0.3695 0.1951  0.0975  0.1120  103 GLY   B C   
1243 O O   . GLY   B 94  ? 0.6098 0.6545 0.3742 0.2039  0.1012  0.1235  103 GLY   B O   
1244 N N   . GLU   B 95  ? 0.6184 0.6588 0.3608 0.1966  0.0904  0.1039  104 GLU   B N   
1245 C CA  . GLU   B 95  ? 0.6340 0.6848 0.3600 0.2088  0.0862  0.1071  104 GLU   B CA  
1246 C C   . GLU   B 95  ? 0.6406 0.6892 0.3550 0.2090  0.0782  0.0952  104 GLU   B C   
1247 O O   . GLU   B 95  ? 0.6180 0.6575 0.3337 0.1988  0.0755  0.0844  104 GLU   B O   
1248 C CB  . GLU   B 95  ? 0.6464 0.7024 0.3623 0.2112  0.0855  0.1089  104 GLU   B CB  
1249 C CG  . GLU   B 95  ? 0.6587 0.7152 0.3874 0.2078  0.0932  0.1181  104 GLU   B CG  
1250 C CD  . GLU   B 95  ? 0.6765 0.7382 0.3965 0.2091  0.0928  0.1195  104 GLU   B CD  
1251 O OE1 . GLU   B 95  ? 0.7001 0.7623 0.4047 0.2106  0.0861  0.1112  104 GLU   B OE1 
1252 O OE2 . GLU   B 95  ? 0.6837 0.7492 0.4132 0.2088  0.0993  0.1292  104 GLU   B OE2 
1253 N N   . ARG   B 96  ? 0.6461 0.7037 0.3499 0.2199  0.0745  0.0969  105 ARG   B N   
1254 C CA  . ARG   B 96  ? 0.6687 0.7253 0.3631 0.2207  0.0669  0.0858  105 ARG   B CA  
1255 C C   . ARG   B 96  ? 0.6562 0.7090 0.3381 0.2165  0.0608  0.0751  105 ARG   B C   
1256 O O   . ARG   B 96  ? 0.6337 0.6893 0.3102 0.2182  0.0616  0.0782  105 ARG   B O   
1257 C CB  . ARG   B 96  ? 0.7239 0.7932 0.4101 0.2345  0.0645  0.0905  105 ARG   B CB  
1258 C CG  . ARG   B 96  ? 0.7590 0.8280 0.4387 0.2352  0.0574  0.0795  105 ARG   B CG  
1259 C CD  . ARG   B 96  ? 0.7933 0.8739 0.4722 0.2469  0.0572  0.0856  105 ARG   B CD  
1260 N NE  . ARG   B 96  ? 0.8380 0.9328 0.5089 0.2597  0.0583  0.0952  105 ARG   B NE  
1261 C CZ  . ARG   B 96  ? 0.8863 0.9882 0.5643 0.2663  0.0653  0.1102  105 ARG   B CZ  
1262 N NH1 . ARG   B 96  ? 0.8910 0.9861 0.5855 0.2611  0.0720  0.1174  105 ARG   B NH1 
1263 N NH2 . ARG   B 96  ? 0.9226 1.0392 0.5916 0.2785  0.0655  0.1181  105 ARG   B NH2 
1264 N N   . ALA   B 97  ? 0.6539 0.7001 0.3325 0.2106  0.0553  0.0633  106 ALA   B N   
1265 C CA  . ALA   B 97  ? 0.6529 0.6958 0.3189 0.2082  0.0483  0.0529  106 ALA   B CA  
1266 C C   . ALA   B 97  ? 0.6664 0.7200 0.3192 0.2205  0.0450  0.0553  106 ALA   B C   
1267 O O   . ALA   B 97  ? 0.6598 0.7226 0.3103 0.2300  0.0441  0.0586  106 ALA   B O   
1268 C CB  . ALA   B 97  ? 0.6510 0.6886 0.3160 0.2033  0.0431  0.0419  106 ALA   B CB  
1269 N N   . LYS   B 98  ? 0.6769 0.7298 0.3212 0.2204  0.0429  0.0532  107 LYS   B N   
1270 C CA  . LYS   B 98  ? 0.7009 0.7637 0.3320 0.2317  0.0392  0.0537  107 LYS   B CA  
1271 C C   . LYS   B 98  ? 0.6808 0.7368 0.3025 0.2275  0.0331  0.0433  107 LYS   B C   
1272 O O   . LYS   B 98  ? 0.6596 0.7067 0.2849 0.2180  0.0350  0.0422  107 LYS   B O   
1273 C CB  . LYS   B 98  ? 0.7405 0.8116 0.3743 0.2373  0.0457  0.0666  107 LYS   B CB  
1274 C CG  . LYS   B 98  ? 0.7768 0.8606 0.3986 0.2495  0.0438  0.0698  107 LYS   B CG  
1275 C CD  . LYS   B 98  ? 0.8131 0.9003 0.4379 0.2497  0.0500  0.0795  107 LYS   B CD  
1276 C CE  . LYS   B 98  ? 0.8307 0.9054 0.4659 0.2361  0.0536  0.0787  107 LYS   B CE  
1277 N NZ  . LYS   B 98  ? 0.8651 0.9442 0.5040 0.2364  0.0594  0.0877  107 LYS   B NZ  
1278 N N   . ASN   B 99  ? 0.6468 0.7060 0.2583 0.2335  0.0260  0.0352  108 ASN   B N   
1279 C CA  . ASN   B 99  ? 0.6489 0.7025 0.2510 0.2319  0.0197  0.0257  108 ASN   B CA  
1280 C C   . ASN   B 99  ? 0.6464 0.7068 0.2410 0.2392  0.0204  0.0301  108 ASN   B C   
1281 O O   . ASN   B 99  ? 0.6384 0.7125 0.2279 0.2513  0.0208  0.0353  108 ASN   B O   
1282 C CB  . ASN   B 99  ? 0.6566 0.7111 0.2519 0.2357  0.0118  0.0149  108 ASN   B CB  
1283 C CG  . ASN   B 99  ? 0.6629 0.7103 0.2658 0.2275  0.0108  0.0097  108 ASN   B CG  
1284 O OD1 . ASN   B 99  ? 0.6980 0.7504 0.3088 0.2289  0.0160  0.0173  108 ASN   B OD1 
1285 N ND2 . ASN   B 99  ? 0.6637 0.7044 0.2628 0.2237  0.0040  -0.0019 108 ASN   B ND2 
1286 N N   . ILE   B 100 ? 0.6262 0.6788 0.2191 0.2331  0.0198  0.0276  109 ILE   B N   
1287 C CA  . ILE   B 100 ? 0.6316 0.6899 0.2169 0.2396  0.0197  0.0303  109 ILE   B CA  
1288 C C   . ILE   B 100 ? 0.6320 0.6827 0.2092 0.2382  0.0126  0.0196  109 ILE   B C   
1289 O O   . ILE   B 100 ? 0.6200 0.6578 0.2004 0.2270  0.0117  0.0151  109 ILE   B O   
1290 C CB  . ILE   B 100 ? 0.6335 0.6907 0.2257 0.2342  0.0267  0.0391  109 ILE   B CB  
1291 C CG1 . ILE   B 100 ? 0.6388 0.7003 0.2423 0.2332  0.0341  0.0491  109 ILE   B CG1 
1292 C CG2 . ILE   B 100 ? 0.6366 0.7015 0.2213 0.2417  0.0268  0.0424  109 ILE   B CG2 
1293 C CD1 . ILE   B 100 ? 0.6472 0.7238 0.2490 0.2450  0.0379  0.0596  109 ILE   B CD1 
1294 N N   . GLN   B 101 ? 0.6367 0.6949 0.2040 0.2488  0.0079  0.0158  110 GLN   B N   
1295 C CA  . GLN   B 101 ? 0.6515 0.7023 0.2118 0.2485  0.0005  0.0047  110 GLN   B CA  
1296 C C   . GLN   B 101 ? 0.6599 0.7107 0.2156 0.2502  0.0012  0.0070  110 GLN   B C   
1297 O O   . GLN   B 101 ? 0.6603 0.7227 0.2141 0.2577  0.0051  0.0149  110 GLN   B O   
1298 C CB  . GLN   B 101 ? 0.6740 0.7322 0.2275 0.2585  -0.0058 -0.0030 110 GLN   B CB  
1299 C CG  . GLN   B 101 ? 0.6826 0.7337 0.2297 0.2594  -0.0133 -0.0143 110 GLN   B CG  
1300 C CD  . GLN   B 101 ? 0.6919 0.7494 0.2349 0.2672  -0.0197 -0.0235 110 GLN   B CD  
1301 O OE1 . GLN   B 101 ? 0.6888 0.7494 0.2356 0.2666  -0.0198 -0.0243 110 GLN   B OE1 
1302 N NE2 . GLN   B 101 ? 0.7099 0.7699 0.2454 0.2749  -0.0253 -0.0311 110 GLN   B NE2 
1303 N N   . THR   B 102 ? 0.6645 0.7025 0.2197 0.2425  -0.0016 0.0014  111 THR   B N   
1304 C CA  . THR   B 102 ? 0.6633 0.6993 0.2152 0.2424  -0.0009 0.0033  111 THR   B CA  
1305 C C   . THR   B 102 ? 0.6606 0.6841 0.2089 0.2387  -0.0074 -0.0062 111 THR   B C   
1306 O O   . THR   B 102 ? 0.6777 0.6918 0.2287 0.2325  -0.0109 -0.0128 111 THR   B O   
1307 C CB  . THR   B 102 ? 0.6506 0.6851 0.2101 0.2340  0.0062  0.0123  111 THR   B CB  
1308 O OG1 . THR   B 102 ? 0.6576 0.6957 0.2126 0.2377  0.0071  0.0153  111 THR   B OG1 
1309 C CG2 . THR   B 102 ? 0.6504 0.6723 0.2173 0.2203  0.0072  0.0103  111 THR   B CG2 
1310 N N   . LEU   B 103 ? 0.6618 0.6857 0.2043 0.2432  -0.0092 -0.0068 112 LEU   B N   
1311 C CA  . LEU   B 103 ? 0.6622 0.6736 0.2020 0.2397  -0.0145 -0.0140 112 LEU   B CA  
1312 C C   . LEU   B 103 ? 0.6580 0.6627 0.2020 0.2298  -0.0105 -0.0086 112 LEU   B C   
1313 O O   . LEU   B 103 ? 0.6555 0.6664 0.1989 0.2316  -0.0065 -0.0020 112 LEU   B O   
1314 C CB  . LEU   B 103 ? 0.6647 0.6804 0.1961 0.2511  -0.0194 -0.0189 112 LEU   B CB  
1315 C CG  . LEU   B 103 ? 0.6704 0.6721 0.2002 0.2477  -0.0249 -0.0261 112 LEU   B CG  
1316 C CD1 . LEU   B 103 ? 0.6747 0.6669 0.2063 0.2449  -0.0308 -0.0359 112 LEU   B CD1 
1317 C CD2 . LEU   B 103 ? 0.6801 0.6857 0.2029 0.2577  -0.0279 -0.0284 112 LEU   B CD2 
1318 N N   . PRO   B 104 ? 0.6548 0.6475 0.2038 0.2184  -0.0110 -0.0109 113 PRO   B N   
1319 C CA  . PRO   B 104 ? 0.6539 0.6420 0.2067 0.2093  -0.0074 -0.0063 113 PRO   B CA  
1320 C C   . PRO   B 104 ? 0.6653 0.6504 0.2127 0.2121  -0.0099 -0.0068 113 PRO   B C   
1321 O O   . PRO   B 104 ? 0.6959 0.6748 0.2378 0.2175  -0.0167 -0.0144 113 PRO   B O   
1322 C CB  . PRO   B 104 ? 0.6481 0.6243 0.2058 0.1980  -0.0089 -0.0103 113 PRO   B CB  
1323 C CG  . PRO   B 104 ? 0.6451 0.6210 0.2036 0.2002  -0.0119 -0.0157 113 PRO   B CG  
1324 C CD  . PRO   B 104 ? 0.6563 0.6409 0.2079 0.2138  -0.0149 -0.0180 113 PRO   B CD  
1325 N N   . GLY   B 105 ? 0.6752 0.6670 0.2239 0.2113  -0.0048 0.0003  114 GLY   B N   
1326 C CA  . GLY   B 105 ? 0.6769 0.6652 0.2230 0.2100  -0.0058 0.0012  114 GLY   B CA  
1327 C C   . GLY   B 105 ? 0.6800 0.6564 0.2295 0.1986  -0.0069 -0.0005 114 GLY   B C   
1328 O O   . GLY   B 105 ? 0.6689 0.6387 0.2219 0.1927  -0.0081 -0.0040 114 GLY   B O   
1329 N N   . ILE   B 106 ? 0.6915 0.6664 0.2398 0.1962  -0.0065 0.0018  115 ILE   B N   
1330 C CA  . ILE   B 106 ? 0.6971 0.6622 0.2472 0.1868  -0.0078 0.0011  115 ILE   B CA  
1331 C C   . ILE   B 106 ? 0.6878 0.6592 0.2417 0.1806  -0.0027 0.0069  115 ILE   B C   
1332 O O   . ILE   B 106 ? 0.6995 0.6786 0.2513 0.1855  -0.0010 0.0104  115 ILE   B O   
1333 C CB  . ILE   B 106 ? 0.7201 0.6768 0.2643 0.1912  -0.0136 -0.0021 115 ILE   B CB  
1334 C CG1 . ILE   B 106 ? 0.7481 0.6985 0.2891 0.1978  -0.0193 -0.0091 115 ILE   B CG1 
1335 C CG2 . ILE   B 106 ? 0.7335 0.6813 0.2798 0.1816  -0.0142 -0.0013 115 ILE   B CG2 
1336 C CD1 . ILE   B 106 ? 0.7500 0.6905 0.2950 0.1905  -0.0215 -0.0135 115 ILE   B CD1 
1337 N N   . PHE   B 107 ? 0.6771 0.6453 0.2364 0.1699  -0.0005 0.0073  116 PHE   B N   
1338 C CA  . PHE   B 107 ? 0.6663 0.6383 0.2286 0.1629  0.0026  0.0110  116 PHE   B CA  
1339 C C   . PHE   B 107 ? 0.6830 0.6460 0.2409 0.1611  -0.0017 0.0097  116 PHE   B C   
1340 O O   . PHE   B 107 ? 0.6805 0.6336 0.2386 0.1575  -0.0047 0.0062  116 PHE   B O   
1341 C CB  . PHE   B 107 ? 0.6622 0.6357 0.2327 0.1527  0.0068  0.0111  116 PHE   B CB  
1342 C CG  . PHE   B 107 ? 0.6568 0.6403 0.2342 0.1520  0.0126  0.0141  116 PHE   B CG  
1343 C CD1 . PHE   B 107 ? 0.6567 0.6482 0.2332 0.1603  0.0145  0.0173  116 PHE   B CD1 
1344 C CD2 . PHE   B 107 ? 0.6522 0.6370 0.2380 0.1426  0.0164  0.0136  116 PHE   B CD2 
1345 C CE1 . PHE   B 107 ? 0.6489 0.6490 0.2333 0.1588  0.0203  0.0208  116 PHE   B CE1 
1346 C CE2 . PHE   B 107 ? 0.6448 0.6376 0.2387 0.1414  0.0219  0.0163  116 PHE   B CE2 
1347 C CZ  . PHE   B 107 ? 0.6509 0.6508 0.2442 0.1494  0.0239  0.0202  116 PHE   B CZ  
1348 N N   . LYS   B 108 ? 0.6977 0.6639 0.2520 0.1644  -0.0022 0.0125  117 LYS   B N   
1349 C CA  . LYS   B 108 ? 0.7184 0.6776 0.2691 0.1628  -0.0057 0.0130  117 LYS   B CA  
1350 C C   . LYS   B 108 ? 0.6871 0.6520 0.2418 0.1533  -0.0020 0.0162  117 LYS   B C   
1351 O O   . LYS   B 108 ? 0.6528 0.6292 0.2100 0.1532  0.0018  0.0190  117 LYS   B O   
1352 C CB  . LYS   B 108 ? 0.7657 0.7258 0.3101 0.1730  -0.0087 0.0140  117 LYS   B CB  
1353 C CG  . LYS   B 108 ? 0.8350 0.7879 0.3750 0.1822  -0.0135 0.0094  117 LYS   B CG  
1354 C CD  . LYS   B 108 ? 0.8783 0.8365 0.4129 0.1942  -0.0152 0.0095  117 LYS   B CD  
1355 C CE  . LYS   B 108 ? 0.9419 0.8946 0.4734 0.2025  -0.0197 0.0035  117 LYS   B CE  
1356 N NZ  . LYS   B 108 ? 0.9723 0.9307 0.4984 0.2150  -0.0217 0.0023  117 LYS   B NZ  
1357 N N   . THR   B 109 ? 0.6928 0.6511 0.2489 0.1455  -0.0030 0.0156  118 THR   B N   
1358 C CA  . THR   B 109 ? 0.6880 0.6524 0.2475 0.1363  0.0000  0.0180  118 THR   B CA  
1359 C C   . THR   B 109 ? 0.7041 0.6615 0.2598 0.1342  -0.0033 0.0200  118 THR   B C   
1360 O O   . THR   B 109 ? 0.6928 0.6381 0.2457 0.1369  -0.0075 0.0187  118 THR   B O   
1361 C CB  . THR   B 109 ? 0.6744 0.6398 0.2407 0.1270  0.0030  0.0157  118 THR   B CB  
1362 O OG1 . THR   B 109 ? 0.6714 0.6263 0.2368 0.1227  0.0001  0.0143  118 THR   B OG1 
1363 C CG2 . THR   B 109 ? 0.6708 0.6381 0.2410 0.1294  0.0052  0.0134  118 THR   B CG2 
1364 N N   . LYS   B 110 ? 0.7257 0.6909 0.2822 0.1289  -0.0013 0.0231  119 LYS   B N   
1365 C CA  . LYS   B 110 ? 0.7489 0.7090 0.3020 0.1268  -0.0039 0.0264  119 LYS   B CA  
1366 C C   . LYS   B 110 ? 0.7667 0.7156 0.3216 0.1211  -0.0055 0.0248  119 LYS   B C   
1367 O O   . LYS   B 110 ? 0.8122 0.7526 0.3642 0.1214  -0.0087 0.0275  119 LYS   B O   
1368 C CB  . LYS   B 110 ? 0.7529 0.7258 0.3071 0.1213  -0.0010 0.0295  119 LYS   B CB  
1369 C CG  . LYS   B 110 ? 0.7575 0.7412 0.3186 0.1132  0.0038  0.0268  119 LYS   B CG  
1370 C CD  . LYS   B 110 ? 0.7794 0.7753 0.3417 0.1069  0.0060  0.0288  119 LYS   B CD  
1371 C CE  . LYS   B 110 ? 0.8028 0.7962 0.3664 0.0986  0.0061  0.0288  119 LYS   B CE  
1372 N NZ  . LYS   B 110 ? 0.8122 0.8108 0.3832 0.0913  0.0099  0.0239  119 LYS   B NZ  
1373 N N   . ASP   B 111 ? 0.7437 0.6929 0.3036 0.1159  -0.0034 0.0209  120 ASP   B N   
1374 C CA  . ASP   B 111 ? 0.7494 0.6893 0.3117 0.1099  -0.0046 0.0190  120 ASP   B CA  
1375 C C   . ASP   B 111 ? 0.7640 0.6931 0.3262 0.1151  -0.0078 0.0148  120 ASP   B C   
1376 O O   . ASP   B 111 ? 0.7790 0.7011 0.3442 0.1105  -0.0088 0.0122  120 ASP   B O   
1377 C CB  . ASP   B 111 ? 0.7467 0.6945 0.3150 0.1005  -0.0003 0.0172  120 ASP   B CB  
1378 C CG  . ASP   B 111 ? 0.7420 0.7008 0.3102 0.0954  0.0020  0.0207  120 ASP   B CG  
1379 O OD1 . ASP   B 111 ? 0.7490 0.7054 0.3128 0.0968  -0.0001 0.0252  120 ASP   B OD1 
1380 O OD2 . ASP   B 111 ? 0.7523 0.7223 0.3249 0.0910  0.0059  0.0190  120 ASP   B OD2 
1381 N N   . GLY   B 112 ? 0.7643 0.6932 0.3232 0.1245  -0.0094 0.0138  121 GLY   B N   
1382 C CA  . GLY   B 112 ? 0.7724 0.6918 0.3305 0.1305  -0.0132 0.0093  121 GLY   B CA  
1383 C C   . GLY   B 112 ? 0.7698 0.6959 0.3284 0.1359  -0.0115 0.0066  121 GLY   B C   
1384 O O   . GLY   B 112 ? 0.7554 0.6925 0.3163 0.1342  -0.0070 0.0085  121 GLY   B O   
1385 N N   . ASP   B 113 ? 0.7806 0.7004 0.3378 0.1424  -0.0150 0.0023  122 ASP   B N   
1386 C CA  . ASP   B 113 ? 0.7841 0.7102 0.3405 0.1498  -0.0142 0.0001  122 ASP   B CA  
1387 C C   . ASP   B 113 ? 0.7601 0.6880 0.3219 0.1448  -0.0119 -0.0025 122 ASP   B C   
1388 O O   . ASP   B 113 ? 0.7264 0.6472 0.2914 0.1381  -0.0131 -0.0048 122 ASP   B O   
1389 C CB  . ASP   B 113 ? 0.8177 0.7378 0.3693 0.1602  -0.0194 -0.0034 122 ASP   B CB  
1390 C CG  . ASP   B 113 ? 0.8497 0.7719 0.3962 0.1673  -0.0206 -0.0004 122 ASP   B CG  
1391 O OD1 . ASP   B 113 ? 0.9098 0.8389 0.4562 0.1643  -0.0173 0.0045  122 ASP   B OD1 
1392 O OD2 . ASP   B 113 ? 0.9034 0.8209 0.4461 0.1760  -0.0249 -0.0038 122 ASP   B OD2 
1393 N N   . ILE   B 114 ? 0.7273 0.6647 0.2907 0.1478  -0.0083 -0.0016 123 ILE   B N   
1394 C CA  . ILE   B 114 ? 0.7056 0.6461 0.2746 0.1444  -0.0057 -0.0035 123 ILE   B CA  
1395 C C   . ILE   B 114 ? 0.6734 0.6195 0.2402 0.1544  -0.0057 -0.0041 123 ILE   B C   
1396 O O   . ILE   B 114 ? 0.6533 0.6066 0.2178 0.1596  -0.0038 -0.0004 123 ILE   B O   
1397 C CB  . ILE   B 114 ? 0.6991 0.6475 0.2742 0.1366  0.0001  -0.0002 123 ILE   B CB  
1398 C CG1 . ILE   B 114 ? 0.7159 0.6636 0.2909 0.1297  0.0007  0.0020  123 ILE   B CG1 
1399 C CG2 . ILE   B 114 ? 0.7030 0.6516 0.2846 0.1310  0.0023  -0.0026 123 ILE   B CG2 
1400 C CD1 . ILE   B 114 ? 0.7185 0.6735 0.3004 0.1209  0.0059  0.0032  123 ILE   B CD1 
1401 N N   . GLY   B 115 ? 0.6714 0.6161 0.2396 0.1563  -0.0072 -0.0080 124 GLY   B N   
1402 C CA  . GLY   B 115 ? 0.6484 0.6008 0.2150 0.1657  -0.0066 -0.0078 124 GLY   B CA  
1403 C C   . GLY   B 115 ? 0.6379 0.6006 0.2093 0.1642  0.0000  -0.0020 124 GLY   B C   
1404 O O   . GLY   B 115 ? 0.6060 0.5692 0.1837 0.1547  0.0038  0.0000  124 GLY   B O   
1405 N N   . ALA   B 116 ? 0.6269 0.5983 0.1961 0.1732  0.0014  0.0007  125 ALA   B N   
1406 C CA  . ALA   B 116 ? 0.6251 0.6067 0.1996 0.1728  0.0079  0.0071  125 ALA   B CA  
1407 C C   . ALA   B 116 ? 0.6288 0.6181 0.2019 0.1825  0.0086  0.0087  125 ALA   B C   
1408 O O   . ALA   B 116 ? 0.6262 0.6156 0.1921 0.1911  0.0042  0.0057  125 ALA   B O   
1409 C CB  . ALA   B 116 ? 0.6340 0.6200 0.2068 0.1737  0.0097  0.0111  125 ALA   B CB  
1410 N N   A VAL   B 117 ? 0.6226 0.6185 0.2029 0.1812  0.0141  0.0133  126 VAL   B N   
1411 N N   B VAL   B 117 ? 0.6250 0.6209 0.2053 0.1810  0.0142  0.0134  126 VAL   B N   
1412 N N   C VAL   B 117 ? 0.6224 0.6183 0.2027 0.1812  0.0140  0.0132  126 VAL   B N   
1413 N N   D VAL   B 117 ? 0.6249 0.6208 0.2052 0.1810  0.0142  0.0134  126 VAL   B N   
1414 C CA  A VAL   B 117 ? 0.6257 0.6305 0.2052 0.1906  0.0156  0.0165  126 VAL   B CA  
1415 C CA  B VAL   B 117 ? 0.6291 0.6338 0.2097 0.1897  0.0161  0.0167  126 VAL   B CA  
1416 C CA  C VAL   B 117 ? 0.6252 0.6300 0.2048 0.1906  0.0156  0.0165  126 VAL   B CA  
1417 C CA  D VAL   B 117 ? 0.6289 0.6336 0.2095 0.1897  0.0161  0.0167  126 VAL   B CA  
1418 C C   A VAL   B 117 ? 0.6273 0.6425 0.2117 0.1925  0.0221  0.0250  126 VAL   B C   
1419 C C   B VAL   B 117 ? 0.6299 0.6449 0.2140 0.1923  0.0221  0.0250  126 VAL   B C   
1420 C C   C VAL   B 117 ? 0.6275 0.6426 0.2119 0.1925  0.0221  0.0250  126 VAL   B C   
1421 C C   D VAL   B 117 ? 0.6301 0.6451 0.2142 0.1923  0.0221  0.0250  126 VAL   B C   
1422 O O   A VAL   B 117 ? 0.6223 0.6375 0.2160 0.1842  0.0271  0.0281  126 VAL   B O   
1423 O O   B VAL   B 117 ? 0.6260 0.6410 0.2180 0.1840  0.0265  0.0278  126 VAL   B O   
1424 O O   C VAL   B 117 ? 0.6227 0.6379 0.2164 0.1843  0.0271  0.0281  126 VAL   B O   
1425 O O   D VAL   B 117 ? 0.6266 0.6416 0.2186 0.1841  0.0265  0.0279  126 VAL   B O   
1426 C CB  A VAL   B 117 ? 0.6215 0.6248 0.2057 0.1888  0.0157  0.0145  126 VAL   B CB  
1427 C CB  B VAL   B 117 ? 0.6265 0.6292 0.2138 0.1854  0.0175  0.0156  126 VAL   B CB  
1428 C CB  C VAL   B 117 ? 0.6210 0.6242 0.2051 0.1888  0.0157  0.0145  126 VAL   B CB  
1429 C CB  D VAL   B 117 ? 0.6264 0.6291 0.2137 0.1854  0.0175  0.0156  126 VAL   B CB  
1430 C CG1 A VAL   B 117 ? 0.6251 0.6197 0.2043 0.1885  0.0089  0.0059  126 VAL   B CG1 
1431 C CG1 B VAL   B 117 ? 0.6286 0.6411 0.2199 0.1914  0.0220  0.0219  126 VAL   B CG1 
1432 C CG1 C VAL   B 117 ? 0.6244 0.6191 0.2036 0.1886  0.0089  0.0059  126 VAL   B CG1 
1433 C CG1 D VAL   B 117 ? 0.6294 0.6419 0.2208 0.1914  0.0220  0.0219  126 VAL   B CG1 
1434 C CG2 A VAL   B 117 ? 0.6132 0.6145 0.2083 0.1784  0.0209  0.0167  126 VAL   B CG2 
1435 C CG2 B VAL   B 117 ? 0.6309 0.6264 0.2136 0.1861  0.0111  0.0076  126 VAL   B CG2 
1436 C CG2 C VAL   B 117 ? 0.6127 0.6140 0.2078 0.1784  0.0209  0.0167  126 VAL   B CG2 
1437 C CG2 D VAL   B 117 ? 0.6309 0.6264 0.2136 0.1861  0.0111  0.0076  126 VAL   B CG2 
1438 N N   . ALA   B 118 ? 0.6344 0.6588 0.2134 0.2032  0.0222  0.0285  127 ALA   B N   
1439 C CA  . ALA   B 118 ? 0.6419 0.6769 0.2249 0.2058  0.0282  0.0369  127 ALA   B CA  
1440 C C   . ALA   B 118 ? 0.6578 0.7013 0.2458 0.2106  0.0327  0.0433  127 ALA   B C   
1441 O O   . ALA   B 118 ? 0.6640 0.7162 0.2455 0.2217  0.0316  0.0453  127 ALA   B O   
1442 C CB  . ALA   B 118 ? 0.6453 0.6860 0.2196 0.2142  0.0260  0.0374  127 ALA   B CB  
1443 N N   . LEU   B 119 ? 0.6580 0.6986 0.2566 0.2029  0.0369  0.0454  128 LEU   B N   
1444 C CA  . LEU   B 119 ? 0.6707 0.7176 0.2759 0.2063  0.0413  0.0517  128 LEU   B CA  
1445 C C   . LEU   B 119 ? 0.6932 0.7402 0.3125 0.1976  0.0485  0.0574  128 LEU   B C   
1446 O O   . LEU   B 119 ? 0.7103 0.7492 0.3351 0.1871  0.0485  0.0528  128 LEU   B O   
1447 C CB  . LEU   B 119 ? 0.6630 0.7042 0.2668 0.2061  0.0375  0.0461  128 LEU   B CB  
1448 C CG  . LEU   B 119 ? 0.6708 0.7122 0.2621 0.2146  0.0302  0.0395  128 LEU   B CG  
1449 C CD1 . LEU   B 119 ? 0.6628 0.6983 0.2543 0.2128  0.0266  0.0333  128 LEU   B CD1 
1450 C CD2 . LEU   B 119 ? 0.6810 0.7358 0.2662 0.2278  0.0309  0.0449  128 LEU   B CD2 
1451 N N   A ASP   B 120 ? 0.6983 0.7548 0.3242 0.2019  0.0546  0.0669  129 ASP   B N   
1452 N N   B ASP   B 120 ? 0.6983 0.7548 0.3242 0.2019  0.0546  0.0669  129 ASP   B N   
1453 N N   C ASP   B 120 ? 0.7034 0.7600 0.3289 0.2021  0.0545  0.0669  129 ASP   B N   
1454 N N   D ASP   B 120 ? 0.7033 0.7599 0.3289 0.2021  0.0545  0.0669  129 ASP   B N   
1455 C CA  A ASP   B 120 ? 0.6970 0.7546 0.3381 0.1944  0.0620  0.0729  129 ASP   B CA  
1456 C CA  B ASP   B 120 ? 0.6970 0.7546 0.3381 0.1944  0.0620  0.0729  129 ASP   B CA  
1457 C CA  C ASP   B 120 ? 0.7049 0.7628 0.3459 0.1948  0.0620  0.0730  129 ASP   B CA  
1458 C CA  D ASP   B 120 ? 0.7049 0.7627 0.3458 0.1948  0.0620  0.0730  129 ASP   B CA  
1459 C C   A ASP   B 120 ? 0.6946 0.7500 0.3461 0.1923  0.0654  0.0757  129 ASP   B C   
1460 C C   B ASP   B 120 ? 0.6946 0.7500 0.3461 0.1923  0.0654  0.0757  129 ASP   B C   
1461 C C   C ASP   B 120 ? 0.6999 0.7546 0.3504 0.1925  0.0648  0.0750  129 ASP   B C   
1462 C C   D ASP   B 120 ? 0.6998 0.7546 0.3504 0.1925  0.0648  0.0750  129 ASP   B C   
1463 O O   A ASP   B 120 ? 0.7036 0.7659 0.3541 0.2011  0.0670  0.0822  129 ASP   B O   
1464 O O   B ASP   B 120 ? 0.7037 0.7659 0.3542 0.2011  0.0670  0.0822  129 ASP   B O   
1465 O O   C ASP   B 120 ? 0.7136 0.7740 0.3616 0.2013  0.0652  0.0797  129 ASP   B O   
1466 O O   D ASP   B 120 ? 0.7134 0.7739 0.3615 0.2013  0.0652  0.0797  129 ASP   B O   
1467 C CB  A ASP   B 120 ? 0.7015 0.7706 0.3448 0.1997  0.0668  0.0820  129 ASP   B CB  
1468 C CB  B ASP   B 120 ? 0.7015 0.7707 0.3448 0.1997  0.0668  0.0820  129 ASP   B CB  
1469 C CB  C ASP   B 120 ? 0.7138 0.7835 0.3576 0.2008  0.0672  0.0830  129 ASP   B CB  
1470 C CB  D ASP   B 120 ? 0.7137 0.7834 0.3575 0.2008  0.0672  0.0830  129 ASP   B CB  
1471 C CG  A ASP   B 120 ? 0.6993 0.7690 0.3556 0.1906  0.0724  0.0847  129 ASP   B CG  
1472 C CG  B ASP   B 120 ? 0.6993 0.7690 0.3557 0.1906  0.0724  0.0847  129 ASP   B CG  
1473 C CG  C ASP   B 120 ? 0.7189 0.7921 0.3552 0.2021  0.0651  0.0811  129 ASP   B CG  
1474 C CG  D ASP   B 120 ? 0.7188 0.7920 0.3551 0.2021  0.0651  0.0811  129 ASP   B CG  
1475 O OD1 A ASP   B 120 ? 0.6892 0.7512 0.3486 0.1808  0.0708  0.0776  129 ASP   B OD1 
1476 O OD1 B ASP   B 120 ? 0.6892 0.7511 0.3485 0.1808  0.0708  0.0776  129 ASP   B OD1 
1477 O OD1 C ASP   B 120 ? 0.7174 0.7828 0.3470 0.1978  0.0597  0.0724  129 ASP   B OD1 
1478 O OD1 D ASP   B 120 ? 0.7174 0.7828 0.3469 0.1979  0.0597  0.0724  129 ASP   B OD1 
1479 O OD2 A ASP   B 120 ? 0.7044 0.7831 0.3681 0.1934  0.0783  0.0938  129 ASP   B OD2 
1480 O OD2 B ASP   B 120 ? 0.7044 0.7831 0.3682 0.1934  0.0783  0.0938  129 ASP   B OD2 
1481 O OD2 C ASP   B 120 ? 0.7356 0.8194 0.3730 0.2075  0.0689  0.0888  129 ASP   B OD2 
1482 O OD2 D ASP   B 120 ? 0.7353 0.8191 0.3727 0.2075  0.0689  0.0888  129 ASP   B OD2 
1483 N N   . TYR   B 121 ? 0.6866 0.7336 0.3477 0.1815  0.0666  0.0712  130 TYR   B N   
1484 C CA  . TYR   B 121 ? 0.6811 0.7249 0.3538 0.1784  0.0701  0.0730  130 TYR   B CA  
1485 C C   . TYR   B 121 ? 0.6724 0.7123 0.3602 0.1668  0.0748  0.0720  130 TYR   B C   
1486 O O   . TYR   B 121 ? 0.6671 0.7048 0.3538 0.1603  0.0734  0.0668  130 TYR   B O   
1487 C CB  . TYR   B 121 ? 0.6925 0.7296 0.3590 0.1781  0.0644  0.0653  130 TYR   B CB  
1488 C CG  . TYR   B 121 ? 0.7220 0.7642 0.3776 0.1898  0.0608  0.0668  130 TYR   B CG  
1489 C CD1 . TYR   B 121 ? 0.7329 0.7815 0.3934 0.1967  0.0646  0.0750  130 TYR   B CD1 
1490 C CD2 . TYR   B 121 ? 0.7344 0.7757 0.3754 0.1943  0.0537  0.0601  130 TYR   B CD2 
1491 C CE1 . TYR   B 121 ? 0.7625 0.8179 0.4130 0.2079  0.0612  0.0763  130 TYR   B CE1 
1492 C CE2 . TYR   B 121 ? 0.7577 0.8049 0.3893 0.2052  0.0501  0.0605  130 TYR   B CE2 
1493 C CZ  . TYR   B 121 ? 0.7672 0.8223 0.4031 0.2122  0.0539  0.0685  130 TYR   B CZ  
1494 O OH  . TYR   B 121 ? 0.8329 0.8958 0.4599 0.2234  0.0506  0.0690  130 TYR   B OH  
1495 N N   . PRO   B 122 ? 0.6537 0.6930 0.3565 0.1642  0.0804  0.0765  131 PRO   B N   
1496 C CA  . PRO   B 122 ? 0.6497 0.6858 0.3682 0.1535  0.0850  0.0748  131 PRO   B CA  
1497 C C   . PRO   B 122 ? 0.6207 0.6488 0.3372 0.1441  0.0808  0.0630  131 PRO   B C   
1498 O O   . PRO   B 122 ? 0.6119 0.6360 0.3178 0.1459  0.0753  0.0576  131 PRO   B O   
1499 C CB  . PRO   B 122 ? 0.6576 0.6936 0.3915 0.1542  0.0910  0.0817  131 PRO   B CB  
1500 C CG  . PRO   B 122 ? 0.6768 0.7181 0.4022 0.1665  0.0902  0.0893  131 PRO   B CG  
1501 C CD  . PRO   B 122 ? 0.6810 0.7223 0.3866 0.1713  0.0823  0.0829  131 PRO   B CD  
1502 N N   . ALA   B 123 ? 0.6085 0.6355 0.3352 0.1345  0.0833  0.0591  132 ALA   B N   
1503 C CA  . ALA   B 123 ? 0.5892 0.6108 0.3140 0.1254  0.0797  0.0483  132 ALA   B CA  
1504 C C   . ALA   B 123 ? 0.5731 0.5885 0.3015 0.1229  0.0786  0.0437  132 ALA   B C   
1505 O O   . ALA   B 123 ? 0.5637 0.5747 0.2835 0.1196  0.0735  0.0360  132 ALA   B O   
1506 C CB  . ALA   B 123 ? 0.5870 0.6110 0.3230 0.1164  0.0831  0.0454  132 ALA   B CB  
1507 N N   . GLY   B 124 ? 0.5554 0.5705 0.2954 0.1250  0.0830  0.0488  133 GLY   B N   
1508 C CA  . GLY   B 124 ? 0.5408 0.5509 0.2846 0.1239  0.0822  0.0452  133 GLY   B CA  
1509 C C   . GLY   B 124 ? 0.5318 0.5403 0.2599 0.1303  0.0759  0.0432  133 GLY   B C   
1510 O O   . GLY   B 124 ? 0.5297 0.5342 0.2602 0.1283  0.0745  0.0387  133 GLY   B O   
1511 N N   . THR   B 125 ? 0.5278 0.5395 0.2415 0.1378  0.0723  0.0459  134 THR   B N   
1512 C CA  . THR   B 125 ? 0.5329 0.5433 0.2313 0.1439  0.0657  0.0427  134 THR   B CA  
1513 C C   . THR   B 125 ? 0.5317 0.5368 0.2218 0.1372  0.0603  0.0331  134 THR   B C   
1514 O O   . THR   B 125 ? 0.5311 0.5333 0.2112 0.1399  0.0547  0.0285  134 THR   B O   
1515 C CB  . THR   B 125 ? 0.5499 0.5668 0.2375 0.1551  0.0643  0.0492  134 THR   B CB  
1516 O OG1 . THR   B 125 ? 0.5514 0.5740 0.2481 0.1603  0.0703  0.0592  134 THR   B OG1 
1517 C CG2 . THR   B 125 ? 0.5538 0.5711 0.2287 0.1630  0.0584  0.0467  134 THR   B CG2 
1518 N N   . SER   B 126 ? 0.5213 0.5254 0.2161 0.1287  0.0619  0.0300  135 SER   B N   
1519 C CA  . SER   B 126 ? 0.5163 0.5162 0.2044 0.1218  0.0575  0.0219  135 SER   B CA  
1520 C C   . SER   B 126 ? 0.5059 0.5010 0.1930 0.1199  0.0544  0.0162  135 SER   B C   
1521 O O   . SER   B 126 ? 0.5067 0.5013 0.2051 0.1173  0.0577  0.0159  135 SER   B O   
1522 C CB  . SER   B 126 ? 0.5146 0.5157 0.2113 0.1124  0.0606  0.0191  135 SER   B CB  
1523 O OG  . SER   B 126 ? 0.5230 0.5284 0.2170 0.1142  0.0616  0.0228  135 SER   B OG  
1524 N N   . GLY   B 127 ? 0.5010 0.4925 0.1761 0.1210  0.0484  0.0119  136 GLY   B N   
1525 C CA  . GLY   B 127 ? 0.4993 0.4862 0.1732 0.1176  0.0450  0.0055  136 GLY   B CA  
1526 C C   . GLY   B 127 ? 0.4996 0.4865 0.1674 0.1260  0.0415  0.0060  136 GLY   B C   
1527 O O   . GLY   B 127 ? 0.4986 0.4820 0.1637 0.1241  0.0377  0.0004  136 GLY   B O   
1528 N N   . SER   B 128 ? 0.5003 0.4920 0.1659 0.1355  0.0428  0.0126  137 SER   B N   
1529 C CA  . SER   B 128 ? 0.5009 0.4944 0.1587 0.1448  0.0388  0.0128  137 SER   B CA  
1530 C C   . SER   B 128 ? 0.5024 0.4910 0.1489 0.1442  0.0320  0.0061  137 SER   B C   
1531 O O   . SER   B 128 ? 0.5059 0.4925 0.1468 0.1425  0.0305  0.0055  137 SER   B O   
1532 C CB  . SER   B 128 ? 0.5024 0.5031 0.1581 0.1548  0.0412  0.0212  137 SER   B CB  
1533 O OG  . SER   B 128 ? 0.5001 0.5042 0.1679 0.1548  0.0477  0.0276  137 SER   B OG  
1534 N N   . PRO   B 129 ? 0.5070 0.4937 0.1504 0.1458  0.0276  0.0010  138 PRO   B N   
1535 C CA  . PRO   B 129 ? 0.5161 0.4985 0.1498 0.1466  0.0210  -0.0049 138 PRO   B CA  
1536 C C   . PRO   B 129 ? 0.5353 0.5207 0.1586 0.1572  0.0173  -0.0039 138 PRO   B C   
1537 O O   . PRO   B 129 ? 0.5331 0.5258 0.1555 0.1662  0.0184  0.0001  138 PRO   B O   
1538 C CB  . PRO   B 129 ? 0.5165 0.4979 0.1521 0.1463  0.0180  -0.0104 138 PRO   B CB  
1539 C CG  . PRO   B 129 ? 0.5127 0.5009 0.1551 0.1515  0.0220  -0.0055 138 PRO   B CG  
1540 C CD  . PRO   B 129 ? 0.5084 0.4982 0.1577 0.1487  0.0286  0.0012  138 PRO   B CD  
1541 N N   . ILE   B 130 ? 0.5512 0.5311 0.1673 0.1558  0.0129  -0.0081 139 ILE   B N   
1542 C CA  . ILE   B 130 ? 0.5741 0.5547 0.1800 0.1645  0.0078  -0.0100 139 ILE   B CA  
1543 C C   . ILE   B 130 ? 0.5932 0.5690 0.1965 0.1642  0.0016  -0.0184 139 ILE   B C   
1544 O O   . ILE   B 130 ? 0.5785 0.5474 0.1852 0.1552  0.0006  -0.0223 139 ILE   B O   
1545 C CB  . ILE   B 130 ? 0.5780 0.5555 0.1791 0.1633  0.0074  -0.0086 139 ILE   B CB  
1546 C CG1 . ILE   B 130 ? 0.5790 0.5625 0.1837 0.1636  0.0137  -0.0006 139 ILE   B CG1 
1547 C CG2 . ILE   B 130 ? 0.5872 0.5644 0.1786 0.1720  0.0017  -0.0119 139 ILE   B CG2 
1548 C CD1 . ILE   B 130 ? 0.5832 0.5629 0.1872 0.1575  0.0145  0.0001  139 ILE   B CD1 
1549 N N   . LEU   B 131 ? 0.6178 0.5987 0.2160 0.1742  -0.0021 -0.0208 140 LEU   B N   
1550 C CA  . LEU   B 131 ? 0.6431 0.6220 0.2400 0.1755  -0.0080 -0.0293 140 LEU   B CA  
1551 C C   . LEU   B 131 ? 0.6586 0.6354 0.2472 0.1820  -0.0143 -0.0348 140 LEU   B C   
1552 O O   . LEU   B 131 ? 0.6566 0.6388 0.2392 0.1904  -0.0140 -0.0314 140 LEU   B O   
1553 C CB  . LEU   B 131 ? 0.6606 0.6498 0.2588 0.1834  -0.0076 -0.0283 140 LEU   B CB  
1554 C CG  . LEU   B 131 ? 0.6605 0.6536 0.2671 0.1802  -0.0012 -0.0220 140 LEU   B CG  
1555 C CD1 . LEU   B 131 ? 0.6706 0.6734 0.2781 0.1883  -0.0019 -0.0220 140 LEU   B CD1 
1556 C CD2 . LEU   B 131 ? 0.6610 0.6458 0.2752 0.1673  0.0002  -0.0246 140 LEU   B CD2 
1557 N N   . ASP   B 132 ? 0.6678 0.6383 0.2566 0.1792  -0.0199 -0.0433 141 ASP   B N   
1558 C CA  . ASP   B 132 ? 0.6901 0.6590 0.2729 0.1859  -0.0267 -0.0507 141 ASP   B CA  
1559 C C   . ASP   B 132 ? 0.7167 0.6946 0.2990 0.1938  -0.0301 -0.0560 141 ASP   B C   
1560 O O   . ASP   B 132 ? 0.6957 0.6798 0.2826 0.1930  -0.0270 -0.0534 141 ASP   B O   
1561 C CB  . ASP   B 132 ? 0.6965 0.6523 0.2811 0.1778  -0.0308 -0.0569 141 ASP   B CB  
1562 C CG  . ASP   B 132 ? 0.6920 0.6434 0.2837 0.1694  -0.0323 -0.0622 141 ASP   B CG  
1563 O OD1 . ASP   B 132 ? 0.6799 0.6381 0.2754 0.1695  -0.0306 -0.0620 141 ASP   B OD1 
1564 O OD2 . ASP   B 132 ? 0.7182 0.6590 0.3119 0.1623  -0.0350 -0.0659 141 ASP   B OD2 
1565 N N   . LYS   B 133 ? 0.7544 0.7326 0.3321 0.2006  -0.0364 -0.0639 142 LYS   B N   
1566 C CA  . LYS   B 133 ? 0.8017 0.7914 0.3765 0.2113  -0.0404 -0.0695 142 LYS   B CA  
1567 C C   . LYS   B 133 ? 0.7973 0.7874 0.3790 0.2062  -0.0418 -0.0745 142 LYS   B C   
1568 O O   . LYS   B 133 ? 0.7668 0.7690 0.3475 0.2141  -0.0434 -0.0768 142 LYS   B O   
1569 C CB  . LYS   B 133 ? 0.8427 0.8311 0.4119 0.2185  -0.0472 -0.0782 142 LYS   B CB  
1570 C CG  . LYS   B 133 ? 0.9005 0.8963 0.4615 0.2287  -0.0459 -0.0734 142 LYS   B CG  
1571 C CD  . LYS   B 133 ? 0.9393 0.9285 0.4959 0.2322  -0.0509 -0.0796 142 LYS   B CD  
1572 C CE  . LYS   B 133 ? 0.9551 0.9550 0.5034 0.2440  -0.0497 -0.0755 142 LYS   B CE  
1573 N NZ  . LYS   B 133 ? 0.9772 0.9717 0.5214 0.2487  -0.0550 -0.0826 142 LYS   B NZ  
1574 N N   . CYS   B 134 ? 0.7766 0.7552 0.3648 0.1936  -0.0410 -0.0755 143 CYS   B N   
1575 C CA  . CYS   B 134 ? 0.7763 0.7541 0.3720 0.1871  -0.0424 -0.0807 143 CYS   B CA  
1576 C C   . CYS   B 134 ? 0.7290 0.7097 0.3300 0.1817  -0.0356 -0.0727 143 CYS   B C   
1577 O O   . CYS   B 134 ? 0.7114 0.6922 0.3188 0.1763  -0.0358 -0.0759 143 CYS   B O   
1578 C CB  . CYS   B 134 ? 0.8161 0.7804 0.4161 0.1770  -0.0457 -0.0869 143 CYS   B CB  
1579 S SG  . CYS   B 134 ? 0.8926 0.8546 0.4902 0.1833  -0.0549 -0.0995 143 CYS   B SG  
1580 N N   . GLY   B 135 ? 0.7064 0.6906 0.3053 0.1841  -0.0299 -0.0631 144 GLY   B N   
1581 C CA  . GLY   B 135 ? 0.6844 0.6715 0.2893 0.1798  -0.0232 -0.0555 144 GLY   B CA  
1582 C C   . GLY   B 135 ? 0.6651 0.6416 0.2756 0.1664  -0.0202 -0.0542 144 GLY   B C   
1583 O O   . GLY   B 135 ? 0.6592 0.6368 0.2765 0.1609  -0.0158 -0.0511 144 GLY   B O   
1584 N N   . ARG   B 136 ? 0.6588 0.6257 0.2669 0.1615  -0.0226 -0.0567 145 ARG   B N   
1585 C CA  . ARG   B 136 ? 0.6555 0.6134 0.2681 0.1490  -0.0197 -0.0550 145 ARG   B CA  
1586 C C   . ARG   B 136 ? 0.6274 0.5859 0.2387 0.1483  -0.0142 -0.0465 145 ARG   B C   
1587 O O   . ARG   B 136 ? 0.6120 0.5723 0.2166 0.1559  -0.0149 -0.0440 145 ARG   B O   
1588 C CB  . ARG   B 136 ? 0.6823 0.6303 0.2938 0.1444  -0.0249 -0.0612 145 ARG   B CB  
1589 C CG  . ARG   B 136 ? 0.7170 0.6640 0.3343 0.1399  -0.0282 -0.0686 145 ARG   B CG  
1590 C CD  . ARG   B 136 ? 0.7597 0.6964 0.3773 0.1349  -0.0331 -0.0743 145 ARG   B CD  
1591 N NE  . ARG   B 136 ? 0.8131 0.7484 0.4240 0.1438  -0.0373 -0.0765 145 ARG   B NE  
1592 C CZ  . ARG   B 136 ? 0.8542 0.7798 0.4629 0.1422  -0.0403 -0.0782 145 ARG   B CZ  
1593 N NH1 . ARG   B 136 ? 0.8972 0.8134 0.5099 0.1316  -0.0395 -0.0770 145 ARG   B NH1 
1594 N NH2 . ARG   B 136 ? 0.8862 0.8124 0.4890 0.1517  -0.0441 -0.0809 145 ARG   B NH2 
1595 N N   . VAL   B 137 ? 0.6081 0.5651 0.2256 0.1392  -0.0092 -0.0430 146 VAL   B N   
1596 C CA  . VAL   B 137 ? 0.5979 0.5558 0.2156 0.1372  -0.0038 -0.0358 146 VAL   B CA  
1597 C C   . VAL   B 137 ? 0.6038 0.5538 0.2172 0.1329  -0.0057 -0.0362 146 VAL   B C   
1598 O O   . VAL   B 137 ? 0.5972 0.5411 0.2134 0.1236  -0.0065 -0.0390 146 VAL   B O   
1599 C CB  . VAL   B 137 ? 0.5855 0.5458 0.2120 0.1300  0.0021  -0.0327 146 VAL   B CB  
1600 C CG1 . VAL   B 137 ? 0.5813 0.5431 0.2087 0.1283  0.0072  -0.0262 146 VAL   B CG1 
1601 C CG2 . VAL   B 137 ? 0.5867 0.5543 0.2183 0.1349  0.0040  -0.0317 146 VAL   B CG2 
1602 N N   . ILE   B 138 ? 0.6001 0.5509 0.2071 0.1392  -0.0061 -0.0330 147 ILE   B N   
1603 C CA  . ILE   B 138 ? 0.6070 0.5511 0.2094 0.1367  -0.0079 -0.0325 147 ILE   B CA  
1604 C C   . ILE   B 138 ? 0.5926 0.5387 0.1969 0.1316  -0.0024 -0.0263 147 ILE   B C   
1605 O O   . ILE   B 138 ? 0.5976 0.5392 0.1989 0.1284  -0.0031 -0.0250 147 ILE   B O   
1606 C CB  . ILE   B 138 ? 0.6181 0.5621 0.2124 0.1472  -0.0124 -0.0340 147 ILE   B CB  
1607 C CG1 . ILE   B 138 ? 0.6108 0.5646 0.2023 0.1570  -0.0098 -0.0293 147 ILE   B CG1 
1608 C CG2 . ILE   B 138 ? 0.6208 0.5612 0.2141 0.1500  -0.0186 -0.0420 147 ILE   B CG2 
1609 C CD1 . ILE   B 138 ? 0.6302 0.5847 0.2136 0.1660  -0.0129 -0.0293 147 ILE   B CD1 
1610 N N   . GLY   B 139 ? 0.5789 0.5316 0.1890 0.1307  0.0027  -0.0228 148 GLY   B N   
1611 C CA  . GLY   B 139 ? 0.5683 0.5238 0.1824 0.1252  0.0081  -0.0181 148 GLY   B CA  
1612 C C   . GLY   B 139 ? 0.5616 0.5247 0.1811 0.1283  0.0133  -0.0135 148 GLY   B C   
1613 O O   . GLY   B 139 ? 0.5650 0.5318 0.1849 0.1353  0.0128  -0.0133 148 GLY   B O   
1614 N N   A LEU   B 140 ? 0.5544 0.5205 0.1788 0.1235  0.0181  -0.0099 149 LEU   B N   
1615 N N   B LEU   B 140 ? 0.5544 0.5205 0.1788 0.1236  0.0181  -0.0099 149 LEU   B N   
1616 N N   C LEU   B 140 ? 0.5569 0.5231 0.1810 0.1239  0.0181  -0.0097 149 LEU   B N   
1617 N N   D LEU   B 140 ? 0.5569 0.5231 0.1810 0.1239  0.0181  -0.0097 149 LEU   B N   
1618 C CA  A LEU   B 140 ? 0.5481 0.5208 0.1805 0.1245  0.0240  -0.0052 149 LEU   B CA  
1619 C CA  B LEU   B 140 ? 0.5481 0.5208 0.1805 0.1245  0.0240  -0.0052 149 LEU   B CA  
1620 C CA  C LEU   B 140 ? 0.5522 0.5250 0.1844 0.1250  0.0240  -0.0051 149 LEU   B CA  
1621 C CA  D LEU   B 140 ? 0.5522 0.5250 0.1844 0.1250  0.0240  -0.0051 149 LEU   B CA  
1622 C C   A LEU   B 140 ? 0.5498 0.5270 0.1788 0.1302  0.0258  0.0003  149 LEU   B C   
1623 C C   B LEU   B 140 ? 0.5498 0.5270 0.1788 0.1302  0.0258  0.0003  149 LEU   B C   
1624 C C   C LEU   B 140 ? 0.5557 0.5331 0.1845 0.1306  0.0258  0.0005  149 LEU   B C   
1625 C C   D LEU   B 140 ? 0.5557 0.5331 0.1845 0.1306  0.0258  0.0005  149 LEU   B C   
1626 O O   A LEU   B 140 ? 0.5511 0.5262 0.1740 0.1286  0.0238  0.0000  149 LEU   B O   
1627 O O   B LEU   B 140 ? 0.5511 0.5262 0.1741 0.1286  0.0238  0.0000  149 LEU   B O   
1628 O O   C LEU   B 140 ? 0.5583 0.5331 0.1807 0.1285  0.0236  0.0000  149 LEU   B O   
1629 O O   D LEU   B 140 ? 0.5582 0.5330 0.1806 0.1285  0.0236  0.0000  149 LEU   B O   
1630 C CB  A LEU   B 140 ? 0.5395 0.5125 0.1818 0.1140  0.0280  -0.0069 149 LEU   B CB  
1631 C CB  B LEU   B 140 ? 0.5395 0.5125 0.1818 0.1140  0.0280  -0.0069 149 LEU   B CB  
1632 C CB  C LEU   B 140 ? 0.5433 0.5164 0.1855 0.1145  0.0280  -0.0068 149 LEU   B CB  
1633 C CB  D LEU   B 140 ? 0.5433 0.5163 0.1855 0.1145  0.0280  -0.0068 149 LEU   B CB  
1634 C CG  A LEU   B 140 ? 0.5367 0.5065 0.1827 0.1087  0.0266  -0.0123 149 LEU   B CG  
1635 C CG  B LEU   B 140 ? 0.5367 0.5065 0.1827 0.1087  0.0266  -0.0123 149 LEU   B CG  
1636 C CG  C LEU   B 140 ? 0.5402 0.5100 0.1860 0.1093  0.0264  -0.0123 149 LEU   B CG  
1637 C CG  D LEU   B 140 ? 0.5402 0.5100 0.1860 0.1093  0.0264  -0.0123 149 LEU   B CG  
1638 C CD1 A LEU   B 140 ? 0.5303 0.5026 0.1874 0.1001  0.0314  -0.0137 149 LEU   B CD1 
1639 C CD1 B LEU   B 140 ? 0.5303 0.5026 0.1874 0.1001  0.0314  -0.0137 149 LEU   B CD1 
1640 C CD1 C LEU   B 140 ? 0.5340 0.5061 0.1909 0.1007  0.0311  -0.0137 149 LEU   B CD1 
1641 C CD1 D LEU   B 140 ? 0.5340 0.5061 0.1909 0.1007  0.0311  -0.0137 149 LEU   B CD1 
1642 C CD2 A LEU   B 140 ? 0.5384 0.5090 0.1843 0.1158  0.0249  -0.0128 149 LEU   B CD2 
1643 C CD2 B LEU   B 140 ? 0.5384 0.5090 0.1843 0.1158  0.0249  -0.0128 149 LEU   B CD2 
1644 C CD2 C LEU   B 140 ? 0.5421 0.5128 0.1876 0.1165  0.0246  -0.0127 149 LEU   B CD2 
1645 C CD2 D LEU   B 140 ? 0.5421 0.5128 0.1876 0.1165  0.0246  -0.0127 149 LEU   B CD2 
1646 N N   A TYR   B 141 ? 0.5496 0.5332 0.1836 0.1357  0.0300  0.0057  150 TYR   B N   
1647 N N   B TYR   B 141 ? 0.5496 0.5332 0.1836 0.1357  0.0300  0.0057  150 TYR   B N   
1648 N N   C TYR   B 141 ? 0.5564 0.5403 0.1919 0.1346  0.0308  0.0060  150 TYR   B N   
1649 N N   D TYR   B 141 ? 0.5564 0.5403 0.1919 0.1346  0.0308  0.0060  150 TYR   B N   
1650 C CA  A TYR   B 141 ? 0.5526 0.5422 0.1852 0.1414  0.0327  0.0120  150 TYR   B CA  
1651 C CA  B TYR   B 141 ? 0.5526 0.5422 0.1851 0.1414  0.0327  0.0120  150 TYR   B CA  
1652 C CA  C TYR   B 141 ? 0.5611 0.5510 0.1955 0.1401  0.0336  0.0123  150 TYR   B CA  
1653 C CA  D TYR   B 141 ? 0.5611 0.5510 0.1956 0.1401  0.0336  0.0123  150 TYR   B CA  
1654 C C   A TYR   B 141 ? 0.5477 0.5410 0.1918 0.1353  0.0392  0.0155  150 TYR   B C   
1655 C C   B TYR   B 141 ? 0.5476 0.5410 0.1917 0.1353  0.0392  0.0155  150 TYR   B C   
1656 C C   C TYR   B 141 ? 0.5578 0.5512 0.2039 0.1335  0.0400  0.0154  150 TYR   B C   
1657 C C   D TYR   B 141 ? 0.5579 0.5512 0.2039 0.1334  0.0400  0.0154  150 TYR   B C   
1658 O O   A TYR   B 141 ? 0.5460 0.5401 0.2018 0.1314  0.0435  0.0161  150 TYR   B O   
1659 O O   B TYR   B 141 ? 0.5460 0.5401 0.2018 0.1314  0.0435  0.0161  150 TYR   B O   
1660 O O   C TYR   B 141 ? 0.5620 0.5553 0.2188 0.1291  0.0436  0.0150  150 TYR   B O   
1661 O O   D TYR   B 141 ? 0.5619 0.5552 0.2187 0.1291  0.0436  0.0150  150 TYR   B O   
1662 C CB  A TYR   B 141 ? 0.5585 0.5539 0.1891 0.1523  0.0332  0.0166  150 TYR   B CB  
1663 C CB  B TYR   B 141 ? 0.5585 0.5539 0.1891 0.1523  0.0332  0.0166  150 TYR   B CB  
1664 C CB  C TYR   B 141 ? 0.5699 0.5654 0.2023 0.1510  0.0341  0.0170  150 TYR   B CB  
1665 C CB  D TYR   B 141 ? 0.5699 0.5654 0.2023 0.1510  0.0341  0.0170  150 TYR   B CB  
1666 C CG  A TYR   B 141 ? 0.5608 0.5640 0.1942 0.1569  0.0381  0.0245  150 TYR   B CG  
1667 C CG  B TYR   B 141 ? 0.5608 0.5640 0.1942 0.1570  0.0381  0.0245  150 TYR   B CG  
1668 C CG  C TYR   B 141 ? 0.5737 0.5768 0.2084 0.1558  0.0387  0.0247  150 TYR   B CG  
1669 C CG  D TYR   B 141 ? 0.5736 0.5768 0.2084 0.1558  0.0387  0.0247  150 TYR   B CG  
1670 C CD1 A TYR   B 141 ? 0.5588 0.5657 0.2044 0.1543  0.0446  0.0297  150 TYR   B CD1 
1671 C CD1 B TYR   B 141 ? 0.5588 0.5657 0.2044 0.1543  0.0446  0.0297  150 TYR   B CD1 
1672 C CD1 C TYR   B 141 ? 0.5729 0.5799 0.2198 0.1531  0.0453  0.0300  150 TYR   B CD1 
1673 C CD1 D TYR   B 141 ? 0.5729 0.5799 0.2198 0.1531  0.0453  0.0300  150 TYR   B CD1 
1674 C CD2 A TYR   B 141 ? 0.5672 0.5741 0.1918 0.1640  0.0362  0.0268  150 TYR   B CD2 
1675 C CD2 B TYR   B 141 ? 0.5672 0.5741 0.1918 0.1640  0.0362  0.0268  150 TYR   B CD2 
1676 C CD2 C TYR   B 141 ? 0.5821 0.5888 0.2077 0.1629  0.0367  0.0268  150 TYR   B CD2 
1677 C CD2 D TYR   B 141 ? 0.5821 0.5887 0.2076 0.1629  0.0366  0.0268  150 TYR   B CD2 
1678 C CE1 A TYR   B 141 ? 0.5619 0.5760 0.2112 0.1581  0.0493  0.0373  150 TYR   B CE1 
1679 C CE1 B TYR   B 141 ? 0.5619 0.5760 0.2112 0.1581  0.0493  0.0373  150 TYR   B CE1 
1680 C CE1 C TYR   B 141 ? 0.5782 0.5924 0.2285 0.1570  0.0498  0.0375  150 TYR   B CE1 
1681 C CE1 D TYR   B 141 ? 0.5782 0.5924 0.2284 0.1570  0.0498  0.0375  150 TYR   B CE1 
1682 C CE2 A TYR   B 141 ? 0.5678 0.5828 0.1952 0.1682  0.0408  0.0342  150 TYR   B CE2 
1683 C CE2 B TYR   B 141 ? 0.5678 0.5828 0.1952 0.1682  0.0408  0.0342  150 TYR   B CE2 
1684 C CE2 C TYR   B 141 ? 0.5831 0.5977 0.2111 0.1672  0.0410  0.0341  150 TYR   B CE2 
1685 C CE2 D TYR   B 141 ? 0.5831 0.5977 0.2110 0.1672  0.0410  0.0341  150 TYR   B CE2 
1686 C CZ  A TYR   B 141 ? 0.5664 0.5850 0.2063 0.1651  0.0475  0.0398  150 TYR   B CZ  
1687 C CZ  B TYR   B 141 ? 0.5664 0.5850 0.2063 0.1651  0.0475  0.0398  150 TYR   B CZ  
1688 C CZ  C TYR   B 141 ? 0.5835 0.6019 0.2239 0.1641  0.0477  0.0397  150 TYR   B CZ  
1689 C CZ  D TYR   B 141 ? 0.5834 0.6019 0.2239 0.1641  0.0477  0.0397  150 TYR   B CZ  
1690 O OH  A TYR   B 141 ? 0.5725 0.5992 0.2163 0.1689  0.0523  0.0476  150 TYR   B OH  
1691 O OH  B TYR   B 141 ? 0.5726 0.5993 0.2164 0.1689  0.0523  0.0476  150 TYR   B OH  
1692 O OH  C TYR   B 141 ? 0.5933 0.6199 0.2370 0.1680  0.0523  0.0473  150 TYR   B OH  
1693 O OH  D TYR   B 141 ? 0.5931 0.6197 0.2369 0.1680  0.0523  0.0473  150 TYR   B OH  
1694 N N   A GLY   B 142 ? 0.5487 0.5441 0.1917 0.1329  0.0403  0.0170  151 GLY   B N   
1695 N N   B GLY   B 142 ? 0.5486 0.5441 0.1916 0.1329  0.0403  0.0170  151 GLY   B N   
1696 N N   C GLY   B 142 ? 0.5584 0.5548 0.2038 0.1321  0.0416  0.0177  151 GLY   B N   
1697 N N   D GLY   B 142 ? 0.5585 0.5549 0.2039 0.1321  0.0416  0.0177  151 GLY   B N   
1698 C CA  A GLY   B 142 ? 0.5483 0.5490 0.2026 0.1285  0.0466  0.0206  151 GLY   B CA  
1699 C CA  B GLY   B 142 ? 0.5483 0.5490 0.2026 0.1286  0.0466  0.0206  151 GLY   B CA  
1700 C CA  C GLY   B 142 ? 0.5581 0.5588 0.2156 0.1261  0.0476  0.0201  151 GLY   B CA  
1701 C CA  D GLY   B 142 ? 0.5581 0.5588 0.2156 0.1261  0.0476  0.0201  151 GLY   B CA  
1702 C C   A GLY   B 142 ? 0.5478 0.5488 0.2042 0.1198  0.0471  0.0175  151 GLY   B C   
1703 C C   B GLY   B 142 ? 0.5478 0.5488 0.2042 0.1198  0.0471  0.0175  151 GLY   B C   
1704 C C   C GLY   B 142 ? 0.5577 0.5597 0.2145 0.1198  0.0476  0.0180  151 GLY   B C   
1705 C C   D GLY   B 142 ? 0.5577 0.5597 0.2145 0.1198  0.0476  0.0180  151 GLY   B C   
1706 O O   A GLY   B 142 ? 0.5443 0.5500 0.2122 0.1149  0.0524  0.0190  151 GLY   B O   
1707 O O   B GLY   B 142 ? 0.5443 0.5500 0.2122 0.1150  0.0524  0.0190  151 GLY   B O   
1708 O O   C GLY   B 142 ? 0.5579 0.5661 0.2241 0.1168  0.0527  0.0210  151 GLY   B O   
1709 O O   D GLY   B 142 ? 0.5578 0.5661 0.2240 0.1169  0.0527  0.0210  151 GLY   B O   
1710 N N   A ASN   B 143 ? 0.5555 0.5523 0.2017 0.1185  0.0420  0.0136  152 ASN   B N   
1711 N N   B ASN   B 143 ? 0.5555 0.5523 0.2017 0.1185  0.0420  0.0136  152 ASN   B N   
1712 N N   C ASN   B 143 ? 0.5647 0.5617 0.2115 0.1180  0.0422  0.0135  152 ASN   B N   
1713 N N   D ASN   B 143 ? 0.5647 0.5617 0.2115 0.1180  0.0422  0.0135  152 ASN   B N   
1714 C CA  A ASN   B 143 ? 0.5595 0.5589 0.2037 0.1141  0.0418  0.0129  152 ASN   B CA  
1715 C CA  B ASN   B 143 ? 0.5595 0.5589 0.2037 0.1141  0.0418  0.0129  152 ASN   B CA  
1716 C CA  C ASN   B 143 ? 0.5684 0.5678 0.2123 0.1140  0.0416  0.0128  152 ASN   B CA  
1717 C CA  D ASN   B 143 ? 0.5684 0.5677 0.2122 0.1140  0.0416  0.0128  152 ASN   B CA  
1718 C C   A ASN   B 143 ? 0.5676 0.5669 0.1997 0.1220  0.0378  0.0152  152 ASN   B C   
1719 C C   B ASN   B 143 ? 0.5676 0.5669 0.1997 0.1220  0.0378  0.0152  152 ASN   B C   
1720 C C   C ASN   B 143 ? 0.5731 0.5720 0.2048 0.1217  0.0375  0.0149  152 ASN   B C   
1721 C C   D ASN   B 143 ? 0.5730 0.5720 0.2047 0.1217  0.0376  0.0149  152 ASN   B C   
1722 O O   A ASN   B 143 ? 0.5735 0.5670 0.1973 0.1254  0.0331  0.0131  152 ASN   B O   
1723 O O   B ASN   B 143 ? 0.5735 0.5670 0.1973 0.1254  0.0331  0.0131  152 ASN   B O   
1724 O O   C ASN   B 143 ? 0.5814 0.5746 0.2048 0.1250  0.0329  0.0129  152 ASN   B O   
1725 O O   D ASN   B 143 ? 0.5814 0.5745 0.2048 0.1250  0.0329  0.0129  152 ASN   B O   
1726 C CB  A ASN   B 143 ? 0.5581 0.5542 0.2025 0.1048  0.0400  0.0072  152 ASN   B CB  
1727 C CB  B ASN   B 143 ? 0.5581 0.5543 0.2025 0.1048  0.0400  0.0072  152 ASN   B CB  
1728 C CB  C ASN   B 143 ? 0.5684 0.5642 0.2121 0.1049  0.0397  0.0071  152 ASN   B CB  
1729 C CB  D ASN   B 143 ? 0.5684 0.5642 0.2121 0.1049  0.0397  0.0071  152 ASN   B CB  
1730 C CG  A ASN   B 143 ? 0.5579 0.5596 0.2036 0.0996  0.0413  0.0068  152 ASN   B CG  
1731 C CG  B ASN   B 143 ? 0.5580 0.5597 0.2037 0.0997  0.0413  0.0069  152 ASN   B CG  
1732 C CG  C ASN   B 143 ? 0.5702 0.5718 0.2160 0.0993  0.0413  0.0066  152 ASN   B CG  
1733 C CG  D ASN   B 143 ? 0.5701 0.5717 0.2159 0.0993  0.0413  0.0066  152 ASN   B CG  
1734 O OD1 A ASN   B 143 ? 0.5588 0.5673 0.2090 0.1012  0.0446  0.0101  152 ASN   B OD1 
1735 O OD1 B ASN   B 143 ? 0.5589 0.5673 0.2090 0.1012  0.0446  0.0101  152 ASN   B OD1 
1736 O OD1 C ASN   B 143 ? 0.5736 0.5822 0.2255 0.0999  0.0451  0.0095  152 ASN   B OD1 
1737 O OD1 D ASN   B 143 ? 0.5735 0.5821 0.2254 0.0999  0.0451  0.0095  152 ASN   B OD1 
1738 N ND2 A ASN   B 143 ? 0.5564 0.5562 0.1984 0.0937  0.0387  0.0032  152 ASN   B ND2 
1739 N ND2 B ASN   B 143 ? 0.5564 0.5562 0.1984 0.0937  0.0388  0.0032  152 ASN   B ND2 
1740 N ND2 C ASN   B 143 ? 0.5675 0.5670 0.2086 0.0940  0.0384  0.0033  152 ASN   B ND2 
1741 N ND2 D ASN   B 143 ? 0.5675 0.5670 0.2086 0.0940  0.0384  0.0033  152 ASN   B ND2 
1742 N N   . GLY   B 144 ? 0.5684 0.5765 0.2044 0.1228  0.0417  0.0196  153 GLY   B N   
1743 C CA  . GLY   B 144 ? 0.5857 0.5956 0.2117 0.1295  0.0387  0.0218  153 GLY   B CA  
1744 C C   . GLY   B 144 ? 0.6079 0.6273 0.2389 0.1296  0.0427  0.0257  153 GLY   B C   
1745 O O   . GLY   B 144 ? 0.6205 0.6437 0.2594 0.1215  0.0455  0.0240  153 GLY   B O   
1746 N N   . VAL   B 145 ? 0.6453 0.6693 0.2719 0.1386  0.0428  0.0303  154 VAL   B N   
1747 C CA  . VAL   B 145 ? 0.6767 0.7098 0.3047 0.1402  0.0451  0.0338  154 VAL   B CA  
1748 C C   . VAL   B 145 ? 0.7192 0.7595 0.3499 0.1480  0.0487  0.0403  154 VAL   B C   
1749 O O   . VAL   B 145 ? 0.6967 0.7349 0.3218 0.1556  0.0471  0.0418  154 VAL   B O   
1750 C CB  . VAL   B 145 ? 0.6944 0.7248 0.3100 0.1436  0.0395  0.0319  154 VAL   B CB  
1751 C CG1 . VAL   B 145 ? 0.6850 0.7170 0.2912 0.1552  0.0369  0.0346  154 VAL   B CG1 
1752 C CG2 . VAL   B 145 ? 0.7021 0.7382 0.3202 0.1379  0.0403  0.0311  154 VAL   B CG2 
1753 N N   A VAL   B 146 ? 0.7183 0.7679 0.3570 0.1464  0.0534  0.0441  155 VAL   B N   
1754 N N   B VAL   B 146 ? 0.7183 0.7679 0.3571 0.1464  0.0534  0.0441  155 VAL   B N   
1755 N N   C VAL   B 146 ? 0.7290 0.7783 0.3691 0.1457  0.0539  0.0440  155 VAL   B N   
1756 N N   D VAL   B 146 ? 0.7290 0.7783 0.3691 0.1457  0.0539  0.0440  155 VAL   B N   
1757 C CA  A VAL   B 146 ? 0.7317 0.7907 0.3722 0.1541  0.0569  0.0512  155 VAL   B CA  
1758 C CA  B VAL   B 146 ? 0.7317 0.7907 0.3722 0.1541  0.0569  0.0512  155 VAL   B CA  
1759 C CA  C VAL   B 146 ? 0.7511 0.8094 0.3956 0.1523  0.0584  0.0514  155 VAL   B CA  
1760 C CA  D VAL   B 146 ? 0.7511 0.8093 0.3955 0.1523  0.0584  0.0514  155 VAL   B CA  
1761 C C   A VAL   B 146 ? 0.7417 0.8044 0.3704 0.1614  0.0531  0.0516  155 VAL   B C   
1762 C C   B VAL   B 146 ? 0.7417 0.8044 0.3704 0.1614  0.0531  0.0516  155 VAL   B C   
1763 C C   C VAL   B 146 ? 0.7680 0.8328 0.4034 0.1592  0.0562  0.0534  155 VAL   B C   
1764 C C   D VAL   B 146 ? 0.7680 0.8328 0.4035 0.1592  0.0562  0.0534  155 VAL   B C   
1765 O O   A VAL   B 146 ? 0.7446 0.8055 0.3692 0.1577  0.0500  0.0476  155 VAL   B O   
1766 O O   B VAL   B 146 ? 0.7446 0.8056 0.3693 0.1577  0.0500  0.0476  155 VAL   B O   
1767 O O   C VAL   B 146 ? 0.7714 0.8393 0.4075 0.1549  0.0557  0.0512  155 VAL   B O   
1768 O O   D VAL   B 146 ? 0.7714 0.8392 0.4074 0.1549  0.0557  0.0512  155 VAL   B O   
1769 C CB  A VAL   B 146 ? 0.7295 0.7965 0.3858 0.1481  0.0639  0.0546  155 VAL   B CB  
1770 C CB  B VAL   B 146 ? 0.7295 0.7966 0.3858 0.1481  0.0639  0.0546  155 VAL   B CB  
1771 C CB  C VAL   B 146 ? 0.7483 0.8125 0.4099 0.1452  0.0654  0.0542  155 VAL   B CB  
1772 C CB  D VAL   B 146 ? 0.7483 0.8125 0.4099 0.1452  0.0654  0.0542  155 VAL   B CB  
1773 C CG1 A VAL   B 146 ? 0.7364 0.8142 0.3949 0.1553  0.0677  0.0625  155 VAL   B CG1 
1774 C CG1 B VAL   B 146 ? 0.7365 0.8142 0.3950 0.1553  0.0677  0.0625  155 VAL   B CG1 
1775 C CG1 C VAL   B 146 ? 0.7547 0.8295 0.4213 0.1511  0.0702  0.0624  155 VAL   B CG1 
1776 C CG1 D VAL   B 146 ? 0.7546 0.8294 0.4212 0.1511  0.0702  0.0624  155 VAL   B CG1 
1777 C CG2 A VAL   B 146 ? 0.7283 0.7912 0.3971 0.1419  0.0677  0.0543  155 VAL   B CG2 
1778 C CG2 B VAL   B 146 ? 0.7284 0.7912 0.3971 0.1419  0.0677  0.0543  155 VAL   B CG2 
1779 C CG2 C VAL   B 146 ? 0.7478 0.8060 0.4189 0.1402  0.0679  0.0532  155 VAL   B CG2 
1780 C CG2 D VAL   B 146 ? 0.7478 0.8059 0.4188 0.1402  0.0679  0.0532  155 VAL   B CG2 
1781 N N   A ILE   B 147 ? 0.7552 0.8235 0.3784 0.1718  0.0532  0.0564  156 ILE   B N   
1782 N N   B ILE   B 147 ? 0.7552 0.8235 0.3785 0.1718  0.0533  0.0564  156 ILE   B N   
1783 N N   C ILE   B 147 ? 0.7949 0.8626 0.4223 0.1700  0.0549  0.0571  156 ILE   B N   
1784 N N   D ILE   B 147 ? 0.7949 0.8626 0.4224 0.1700  0.0549  0.0571  156 ILE   B N   
1785 C CA  A ILE   B 147 ? 0.7645 0.8360 0.3755 0.1805  0.0490  0.0561  156 ILE   B CA  
1786 C CA  B ILE   B 147 ? 0.7644 0.8359 0.3755 0.1805  0.0490  0.0561  156 ILE   B CA  
1787 C CA  C ILE   B 147 ? 0.8156 0.8891 0.4330 0.1782  0.0522  0.0583  156 ILE   B CA  
1788 C CA  D ILE   B 147 ? 0.8156 0.8892 0.4331 0.1782  0.0522  0.0583  156 ILE   B CA  
1789 C C   A ILE   B 147 ? 0.7699 0.8552 0.3847 0.1855  0.0535  0.0628  156 ILE   B C   
1790 C C   B ILE   B 147 ? 0.7699 0.8551 0.3846 0.1855  0.0535  0.0628  156 ILE   B C   
1791 C C   C ILE   B 147 ? 0.8352 0.9222 0.4604 0.1806  0.0582  0.0655  156 ILE   B C   
1792 C C   D ILE   B 147 ? 0.8352 0.9222 0.4605 0.1806  0.0582  0.0655  156 ILE   B C   
1793 O O   A ILE   B 147 ? 0.7625 0.8538 0.3884 0.1835  0.0596  0.0683  156 ILE   B O   
1794 O O   B ILE   B 147 ? 0.7624 0.8537 0.3883 0.1835  0.0596  0.0683  156 ILE   B O   
1795 O O   C ILE   B 147 ? 0.8375 0.9276 0.4766 0.1741  0.0640  0.0686  156 ILE   B O   
1796 O O   D ILE   B 147 ? 0.8374 0.9275 0.4765 0.1742  0.0640  0.0686  156 ILE   B O   
1797 C CB  A ILE   B 147 ? 0.7734 0.8388 0.3725 0.1893  0.0437  0.0537  156 ILE   B CB  
1798 C CB  B ILE   B 147 ? 0.7734 0.8388 0.3724 0.1893  0.0437  0.0537  156 ILE   B CB  
1799 C CB  C ILE   B 147 ? 0.8247 0.8944 0.4290 0.1887  0.0469  0.0568  156 ILE   B CB  
1800 C CB  D ILE   B 147 ? 0.8247 0.8944 0.4290 0.1887  0.0469  0.0568  156 ILE   B CB  
1801 C CG1 A ILE   B 147 ? 0.7771 0.8469 0.3784 0.1954  0.0467  0.0584  156 ILE   B CG1 
1802 C CG1 B ILE   B 147 ? 0.7771 0.8468 0.3784 0.1954  0.0467  0.0584  156 ILE   B CG1 
1803 C CG1 C ILE   B 147 ? 0.8285 0.9013 0.4348 0.1944  0.0497  0.0613  156 ILE   B CG1 
1804 C CG1 D ILE   B 147 ? 0.8284 0.9013 0.4347 0.1944  0.0497  0.0613  156 ILE   B CG1 
1805 C CG2 A ILE   B 147 ? 0.7728 0.8249 0.3680 0.1839  0.0387  0.0467  156 ILE   B CG2 
1806 C CG2 B ILE   B 147 ? 0.7727 0.8248 0.3680 0.1838  0.0387  0.0467  156 ILE   B CG2 
1807 C CG2 C ILE   B 147 ? 0.8234 0.8800 0.4208 0.1852  0.0408  0.0492  156 ILE   B CG2 
1808 C CG2 D ILE   B 147 ? 0.8234 0.8800 0.4208 0.1852  0.0408  0.0492  156 ILE   B CG2 
1809 C CD1 A ILE   B 147 ? 0.7849 0.8538 0.3740 0.2065  0.0416  0.0564  156 ILE   B CD1 
1810 C CD1 B ILE   B 147 ? 0.7848 0.8537 0.3738 0.2065  0.0416  0.0564  156 ILE   B CD1 
1811 C CD1 C ILE   B 147 ? 0.8362 0.9075 0.4298 0.2052  0.0444  0.0591  156 ILE   B CD1 
1812 C CD1 D ILE   B 147 ? 0.8361 0.9075 0.4298 0.2052  0.0444  0.0591  156 ILE   B CD1 
1813 N N   A LYS   B 148 ? 0.7835 0.8735 0.3897 0.1916  0.0506  0.0625  157 LYS   B N   
1814 N N   B LYS   B 148 ? 0.7834 0.8734 0.3897 0.1916  0.0505  0.0625  157 LYS   B N   
1815 N N   C LYS   B 148 ? 0.8622 0.9569 0.4799 0.1889  0.0567  0.0676  157 LYS   B N   
1816 N N   D LYS   B 148 ? 0.8623 0.9570 0.4800 0.1889  0.0567  0.0676  157 LYS   B N   
1817 C CA  A LYS   B 148 ? 0.7942 0.8984 0.4024 0.1972  0.0541  0.0683  157 LYS   B CA  
1818 C CA  B LYS   B 148 ? 0.7942 0.8984 0.4024 0.1972  0.0541  0.0683  157 LYS   B CA  
1819 C CA  C LYS   B 148 ? 0.8890 0.9979 0.5128 0.1924  0.0621  0.0748  157 LYS   B CA  
1820 C CA  D LYS   B 148 ? 0.8889 0.9979 0.5128 0.1924  0.0621  0.0748  157 LYS   B CA  
1821 C C   A LYS   B 148 ? 0.7964 0.9085 0.4126 0.2001  0.0603  0.0759  157 LYS   B C   
1822 C C   B LYS   B 148 ? 0.7964 0.9085 0.4126 0.2001  0.0603  0.0759  157 LYS   B C   
1823 C C   C LYS   B 148 ? 0.8956 1.0090 0.5257 0.1961  0.0673  0.0820  157 LYS   B C   
1824 C C   D LYS   B 148 ? 0.8955 1.0089 0.5257 0.1962  0.0673  0.0820  157 LYS   B C   
1825 O O   A LYS   B 148 ? 0.7971 0.9193 0.4243 0.1972  0.0662  0.0812  157 LYS   B O   
1826 O O   B LYS   B 148 ? 0.7971 0.9193 0.4243 0.1972  0.0662  0.0812  157 LYS   B O   
1827 O O   C LYS   B 148 ? 0.8914 1.0128 0.5348 0.1925  0.0740  0.0881  157 LYS   B O   
1828 O O   D LYS   B 148 ? 0.8914 1.0128 0.5348 0.1925  0.0740  0.0881  157 LYS   B O   
1829 C CB  A LYS   B 148 ? 0.8066 0.9132 0.4009 0.2086  0.0490  0.0671  157 LYS   B CB  
1830 C CB  B LYS   B 148 ? 0.8066 0.9133 0.4009 0.2086  0.0490  0.0671  157 LYS   B CB  
1831 C CB  C LYS   B 148 ? 0.9124 1.0283 0.5248 0.2022  0.0587  0.0751  157 LYS   B CB  
1832 C CB  D LYS   B 148 ? 0.9124 1.0283 0.5248 0.2022  0.0587  0.0751  157 LYS   B CB  
1833 C CG  A LYS   B 148 ? 0.8136 0.9168 0.4013 0.2075  0.0440  0.0621  157 LYS   B CG  
1834 C CG  B LYS   B 148 ? 0.8137 0.9168 0.4014 0.2075  0.0440  0.0621  157 LYS   B CG  
1835 C CG  C LYS   B 148 ? 0.9383 1.0480 0.5354 0.2117  0.0520  0.0711  157 LYS   B CG  
1836 C CG  D LYS   B 148 ? 0.9381 1.0479 0.5353 0.2117  0.0520  0.0711  157 LYS   B CG  
1837 C CD  A LYS   B 148 ? 0.8178 0.9235 0.3932 0.2194  0.0393  0.0609  157 LYS   B CD  
1838 C CD  B LYS   B 148 ? 0.8178 0.9235 0.3931 0.2194  0.0393  0.0609  157 LYS   B CD  
1839 C CD  C LYS   B 148 ? 0.9535 1.0500 0.5426 0.2085  0.0451  0.0628  157 LYS   B CD  
1840 C CD  D LYS   B 148 ? 0.9533 1.0498 0.5424 0.2085  0.0451  0.0628  157 LYS   B CD  
1841 C CE  A LYS   B 148 ? 0.8187 0.9405 0.3955 0.2259  0.0429  0.0664  157 LYS   B CE  
1842 C CE  B LYS   B 148 ? 0.8187 0.9405 0.3955 0.2259  0.0429  0.0664  157 LYS   B CE  
1843 C CE  C LYS   B 148 ? 0.9671 1.0625 0.5600 0.1999  0.0449  0.0603  157 LYS   B CE  
1844 C CE  D LYS   B 148 ? 0.9668 1.0623 0.5597 0.1999  0.0448  0.0603  157 LYS   B CE  
1845 N NZ  A LYS   B 148 ? 0.8136 0.9414 0.3950 0.2208  0.0441  0.0666  157 LYS   B NZ  
1846 N NZ  B LYS   B 148 ? 0.8136 0.9414 0.3949 0.2208  0.0441  0.0666  157 LYS   B NZ  
1847 N NZ  C LYS   B 148 ? 0.9836 1.0890 0.5731 0.2050  0.0445  0.0620  157 LYS   B NZ  
1848 N NZ  D LYS   B 148 ? 0.9831 1.0886 0.5727 0.2050  0.0445  0.0620  157 LYS   B NZ  
1849 N N   A ASN   B 149 ? 0.7981 0.9063 0.4095 0.2058  0.0590  0.0765  158 ASN   B N   
1850 N N   B ASN   B 149 ? 0.7981 0.9062 0.4094 0.2058  0.0590  0.0765  158 ASN   B N   
1851 N N   C ASN   B 149 ? 0.9007 1.0093 0.5227 0.2028  0.0643  0.0814  158 ASN   B N   
1852 N N   D ASN   B 149 ? 0.9007 1.0093 0.5226 0.2028  0.0643  0.0814  158 ASN   B N   
1853 C CA  A ASN   B 149 ? 0.7976 0.9134 0.4137 0.2112  0.0641  0.0844  158 ASN   B CA  
1854 C CA  B ASN   B 149 ? 0.7974 0.9133 0.4136 0.2112  0.0641  0.0844  158 ASN   B CA  
1855 C CA  C ASN   B 149 ? 0.9104 1.0240 0.5356 0.2086  0.0683  0.0885  158 ASN   B CA  
1856 C CA  D ASN   B 149 ? 0.9102 1.0238 0.5353 0.2086  0.0683  0.0885  158 ASN   B CA  
1857 C C   A ASN   B 149 ? 0.7827 0.8980 0.4158 0.2015  0.0708  0.0884  158 ASN   B C   
1858 C C   B ASN   B 149 ? 0.7823 0.8976 0.4154 0.2014  0.0708  0.0884  158 ASN   B C   
1859 C C   C ASN   B 149 ? 0.8793 0.9905 0.5211 0.1993  0.0745  0.0921  158 ASN   B C   
1860 C C   D ASN   B 149 ? 0.8792 0.9904 0.5210 0.1993  0.0745  0.0921  158 ASN   B C   
1861 O O   A ASN   B 149 ? 0.7862 0.9118 0.4285 0.2032  0.0772  0.0969  158 ASN   B O   
1862 O O   B ASN   B 149 ? 0.7861 0.9116 0.4283 0.2032  0.0772  0.0969  158 ASN   B O   
1863 O O   C ASN   B 149 ? 0.8772 0.9947 0.5253 0.2031  0.0797  0.1003  158 ASN   B O   
1864 O O   D ASN   B 149 ? 0.8771 0.9946 0.5253 0.2031  0.0797  0.1003  158 ASN   B O   
1865 C CB  A ASN   B 149 ? 0.8105 0.9214 0.4167 0.2188  0.0600  0.0823  158 ASN   B CB  
1866 C CB  B ASN   B 149 ? 0.8104 0.9213 0.4167 0.2188  0.0600  0.0823  158 ASN   B CB  
1867 C CB  C ASN   B 149 ? 0.9336 1.0410 0.5469 0.2158  0.0629  0.0847  158 ASN   B CB  
1868 C CB  D ASN   B 149 ? 0.9333 1.0407 0.5466 0.2158  0.0629  0.0847  158 ASN   B CB  
1869 C CG  A ASN   B 149 ? 0.8201 0.9283 0.4109 0.2268  0.0524  0.0758  158 ASN   B CG  
1870 C CG  B ASN   B 149 ? 0.8201 0.9283 0.4109 0.2268  0.0524  0.0758  158 ASN   B CG  
1871 C CG  C ASN   B 149 ? 0.9561 1.0617 0.5541 0.2230  0.0555  0.0783  158 ASN   B CG  
1872 C CG  D ASN   B 149 ? 0.9557 1.0614 0.5537 0.2230  0.0555  0.0783  158 ASN   B CG  
1873 O OD1 A ASN   B 149 ? 0.8184 0.9262 0.4055 0.2259  0.0498  0.0726  158 ASN   B OD1 
1874 O OD1 B ASN   B 149 ? 0.8184 0.9262 0.4055 0.2259  0.0498  0.0726  158 ASN   B OD1 
1875 O OD1 C ASN   B 149 ? 0.9397 1.0456 0.5353 0.2212  0.0537  0.0755  158 ASN   B OD1 
1876 O OD1 D ASN   B 149 ? 0.9397 1.0457 0.5353 0.2212  0.0537  0.0755  158 ASN   B OD1 
1877 N ND2 A ASN   B 149 ? 0.8324 0.9390 0.4147 0.2348  0.0488  0.0737  158 ASN   B ND2 
1878 N ND2 B ASN   B 149 ? 0.8325 0.9390 0.4148 0.2348  0.0488  0.0737  158 ASN   B ND2 
1879 N ND2 C ASN   B 149 ? 0.9818 1.0859 0.5700 0.2315  0.0512  0.0756  158 ASN   B ND2 
1880 N ND2 D ASN   B 149 ? 0.9813 1.0854 0.5694 0.2315  0.0512  0.0756  158 ASN   B ND2 
1881 N N   A GLY   B 150 ? 0.7630 0.8670 0.4006 0.1918  0.0694  0.0826  159 GLY   B N   
1882 N N   B GLY   B 150 ? 0.7622 0.8661 0.3998 0.1918  0.0695  0.0826  159 GLY   B N   
1883 N N   C GLY   B 150 ? 0.8477 0.9507 0.4964 0.1880  0.0742  0.0864  159 GLY   B N   
1884 N N   D GLY   B 150 ? 0.8475 0.9506 0.4963 0.1880  0.0742  0.0864  159 GLY   B N   
1885 C CA  A GLY   B 150 ? 0.7455 0.8467 0.3991 0.1825  0.0749  0.0845  159 GLY   B CA  
1886 C CA  B GLY   B 150 ? 0.7438 0.8450 0.3974 0.1824  0.0749  0.0845  159 GLY   B CA  
1887 C CA  C GLY   B 150 ? 0.8159 0.9142 0.4799 0.1786  0.0789  0.0871  159 GLY   B CA  
1888 C CA  D GLY   B 150 ? 0.8158 0.9142 0.4799 0.1786  0.0789  0.0871  159 GLY   B CA  
1889 C C   A GLY   B 150 ? 0.7346 0.8259 0.3874 0.1817  0.0733  0.0821  159 GLY   B C   
1890 C C   B GLY   B 150 ? 0.7319 0.8232 0.3846 0.1817  0.0733  0.0822  159 GLY   B C   
1891 C C   C GLY   B 150 ? 0.7913 0.8790 0.4516 0.1785  0.0758  0.0833  159 GLY   B C   
1892 C C   D GLY   B 150 ? 0.7913 0.8790 0.4516 0.1785  0.0758  0.0833  159 GLY   B C   
1893 O O   A GLY   B 150 ? 0.7254 0.8123 0.3908 0.1734  0.0769  0.0819  159 GLY   B O   
1894 O O   B GLY   B 150 ? 0.7238 0.8107 0.3892 0.1735  0.0769  0.0820  159 GLY   B O   
1895 O O   C GLY   B 150 ? 0.7720 0.8540 0.4436 0.1706  0.0785  0.0821  159 GLY   B O   
1896 O O   D GLY   B 150 ? 0.7722 0.8542 0.4438 0.1706  0.0785  0.0821  159 GLY   B O   
1897 N N   A SER   B 151 ? 0.7252 0.8134 0.3643 0.1901  0.0680  0.0800  160 SER   B N   
1898 N N   B SER   B 151 ? 0.7184 0.8068 0.3573 0.1902  0.0680  0.0800  160 SER   B N   
1899 N N   C SER   B 151 ? 0.7735 0.8592 0.4187 0.1872  0.0701  0.0811  160 SER   B N   
1900 N N   D SER   B 151 ? 0.7735 0.8592 0.4187 0.1872  0.0701  0.0811  160 SER   B N   
1901 C CA  A SER   B 151 ? 0.7140 0.7933 0.3504 0.1903  0.0653  0.0767  160 SER   B CA  
1902 C CA  B SER   B 151 ? 0.7050 0.7843 0.3403 0.1908  0.0649  0.0765  160 SER   B CA  
1903 C CA  C SER   B 151 ? 0.7593 0.8358 0.3980 0.1887  0.0657  0.0763  160 SER   B CA  
1904 C CA  D SER   B 151 ? 0.7593 0.8357 0.3980 0.1887  0.0657  0.0763  160 SER   B CA  
1905 C C   A SER   B 151 ? 0.6991 0.7664 0.3323 0.1822  0.0603  0.0671  160 SER   B C   
1906 C C   B SER   B 151 ? 0.6923 0.7596 0.3268 0.1814  0.0608  0.0674  160 SER   B C   
1907 C C   C SER   B 151 ? 0.7330 0.7981 0.3713 0.1789  0.0618  0.0672  160 SER   B C   
1908 C C   D SER   B 151 ? 0.7329 0.7981 0.3713 0.1789  0.0618  0.0672  160 SER   B C   
1909 O O   A SER   B 151 ? 0.6882 0.7550 0.3204 0.1775  0.0589  0.0637  160 SER   B O   
1910 O O   B SER   B 151 ? 0.6798 0.7468 0.3160 0.1752  0.0604  0.0643  160 SER   B O   
1911 O O   C SER   B 151 ? 0.7147 0.7804 0.3549 0.1730  0.0617  0.0646  160 SER   B O   
1912 O O   D SER   B 151 ? 0.7149 0.7805 0.3551 0.1730  0.0617  0.0646  160 SER   B O   
1913 C CB  A SER   B 151 ? 0.7269 0.8092 0.3507 0.2025  0.0616  0.0776  160 SER   B CB  
1914 C CB  B SER   B 151 ? 0.7139 0.7953 0.3348 0.2027  0.0601  0.0758  160 SER   B CB  
1915 C CB  C SER   B 151 ? 0.7767 0.8556 0.3999 0.2004  0.0604  0.0752  160 SER   B CB  
1916 C CB  D SER   B 151 ? 0.7765 0.8555 0.3998 0.2004  0.0604  0.0752  160 SER   B CB  
1917 O OG  A SER   B 151 ? 0.7277 0.8056 0.3529 0.2034  0.0614  0.0775  160 SER   B OG  
1918 O OG  B SER   B 151 ? 0.7072 0.7870 0.3170 0.2052  0.0545  0.0702  160 SER   B OG  
1919 O OG  C SER   B 151 ? 0.7869 0.8601 0.4058 0.2033  0.0573  0.0723  160 SER   B OG  
1920 O OG  D SER   B 151 ? 0.7867 0.8599 0.4056 0.2033  0.0573  0.0723  160 SER   B OG  
1921 N N   A TYR   B 152 ? 0.6815 0.7406 0.3134 0.1810  0.0579  0.0634  161 TYR   B N   
1922 N N   B TYR   B 152 ? 0.6790 0.7382 0.3110 0.1809  0.0579  0.0634  161 TYR   B N   
1923 N N   C TYR   B 152 ? 0.7119 0.7684 0.3478 0.1776  0.0587  0.0626  161 TYR   B N   
1924 N N   D TYR   B 152 ? 0.7119 0.7683 0.3477 0.1776  0.0587  0.0626  161 TYR   B N   
1925 C CA  A TYR   B 152 ? 0.6684 0.7164 0.3003 0.1721  0.0544  0.0553  161 TYR   B CA  
1926 C CA  B TYR   B 152 ? 0.6673 0.7154 0.2993 0.1721  0.0544  0.0553  161 TYR   B CA  
1927 C CA  C TYR   B 152 ? 0.6930 0.7389 0.3274 0.1692  0.0547  0.0541  161 TYR   B CA  
1928 C CA  D TYR   B 152 ? 0.6930 0.7388 0.3273 0.1692  0.0547  0.0541  161 TYR   B CA  
1929 C C   A TYR   B 152 ? 0.6585 0.6998 0.2764 0.1770  0.0469  0.0493  161 TYR   B C   
1930 C C   B TYR   B 152 ? 0.6580 0.6994 0.2760 0.1770  0.0469  0.0493  161 TYR   B C   
1931 C C   C TYR   B 152 ? 0.6738 0.7137 0.2938 0.1749  0.0473  0.0487  161 TYR   B C   
1932 C C   D TYR   B 152 ? 0.6738 0.7136 0.2938 0.1749  0.0473  0.0487  161 TYR   B C   
1933 O O   A TYR   B 152 ? 0.6535 0.6970 0.2647 0.1862  0.0449  0.0505  161 TYR   B O   
1934 O O   B TYR   B 152 ? 0.6531 0.6967 0.2644 0.1862  0.0449  0.0505  161 TYR   B O   
1935 O O   C TYR   B 152 ? 0.6624 0.7036 0.2774 0.1831  0.0458  0.0499  161 TYR   B O   
1936 O O   D TYR   B 152 ? 0.6626 0.7038 0.2776 0.1831  0.0458  0.0499  161 TYR   B O   
1937 C CB  A TYR   B 152 ? 0.6669 0.7112 0.3101 0.1665  0.0579  0.0557  161 TYR   B CB  
1938 C CB  B TYR   B 152 ? 0.6664 0.7107 0.3096 0.1665  0.0579  0.0557  161 TYR   B CB  
1939 C CB  C TYR   B 152 ? 0.6974 0.7382 0.3430 0.1618  0.0576  0.0530  161 TYR   B CB  
1940 C CB  D TYR   B 152 ? 0.6973 0.7381 0.3429 0.1618  0.0576  0.0530  161 TYR   B CB  
1941 C CG  A TYR   B 152 ? 0.6646 0.6991 0.3090 0.1573  0.0551  0.0479  161 TYR   B CG  
1942 C CG  B TYR   B 152 ? 0.6643 0.6989 0.3088 0.1572  0.0551  0.0479  161 TYR   B CG  
1943 C CG  C TYR   B 152 ? 0.6989 0.7328 0.3484 0.1505  0.0565  0.0460  161 TYR   B CG  
1944 C CG  D TYR   B 152 ? 0.6988 0.7328 0.3483 0.1505  0.0565  0.0460  161 TYR   B CG  
1945 C CD1 A TYR   B 152 ? 0.6622 0.6953 0.3098 0.1484  0.0551  0.0439  161 TYR   B CD1 
1946 C CD1 B TYR   B 152 ? 0.6620 0.6951 0.3097 0.1484  0.0552  0.0439  161 TYR   B CD1 
1947 C CD1 C TYR   B 152 ? 0.6998 0.7373 0.3584 0.1428  0.0599  0.0457  161 TYR   B CD1 
1948 C CD1 D TYR   B 152 ? 0.6996 0.7371 0.3583 0.1428  0.0599  0.0457  161 TYR   B CD1 
1949 C CD2 A TYR   B 152 ? 0.6648 0.6928 0.3073 0.1575  0.0525  0.0445  161 TYR   B CD2 
1950 C CD2 B TYR   B 152 ? 0.6647 0.6927 0.3071 0.1575  0.0525  0.0445  161 TYR   B CD2 
1951 C CD2 C TYR   B 152 ? 0.7015 0.7266 0.3464 0.1475  0.0520  0.0395  161 TYR   B CD2 
1952 C CD2 D TYR   B 152 ? 0.7014 0.7265 0.3463 0.1475  0.0520  0.0395  161 TYR   B CD2 
1953 C CE1 A TYR   B 152 ? 0.6596 0.6852 0.3082 0.1401  0.0529  0.0371  161 TYR   B CE1 
1954 C CE1 B TYR   B 152 ? 0.6595 0.6851 0.3082 0.1401  0.0529  0.0371  161 TYR   B CE1 
1955 C CE1 C TYR   B 152 ? 0.6935 0.7267 0.3556 0.1329  0.0590  0.0391  161 TYR   B CE1 
1956 C CE1 D TYR   B 152 ? 0.6934 0.7266 0.3555 0.1329  0.0590  0.0391  161 TYR   B CE1 
1957 C CE2 A TYR   B 152 ? 0.6618 0.6818 0.3058 0.1490  0.0502  0.0375  161 TYR   B CE2 
1958 C CE2 B TYR   B 152 ? 0.6617 0.6817 0.3057 0.1490  0.0503  0.0375  161 TYR   B CE2 
1959 C CE2 C TYR   B 152 ? 0.6965 0.7169 0.3451 0.1374  0.0513  0.0336  161 TYR   B CE2 
1960 C CE2 D TYR   B 152 ? 0.6965 0.7168 0.3450 0.1374  0.0513  0.0336  161 TYR   B CE2 
1961 C CZ  A TYR   B 152 ? 0.6592 0.6782 0.3062 0.1403  0.0505  0.0340  161 TYR   B CZ  
1962 C CZ  B TYR   B 152 ? 0.6592 0.6781 0.3061 0.1403  0.0505  0.0340  161 TYR   B CZ  
1963 C CZ  C TYR   B 152 ? 0.6932 0.7180 0.3500 0.1303  0.0547  0.0334  161 TYR   B CZ  
1964 C CZ  D TYR   B 152 ? 0.6932 0.7179 0.3500 0.1303  0.0547  0.0334  161 TYR   B CZ  
1965 O OH  A TYR   B 152 ? 0.6515 0.6640 0.2996 0.1322  0.0485  0.0276  161 TYR   B OH  
1966 O OH  B TYR   B 152 ? 0.6514 0.6639 0.2995 0.1322  0.0485  0.0276  161 TYR   B OH  
1967 O OH  C TYR   B 152 ? 0.6830 0.7048 0.3430 0.1208  0.0540  0.0274  161 TYR   B OH  
1968 O OH  D TYR   B 152 ? 0.6831 0.7049 0.3430 0.1208  0.0540  0.0274  161 TYR   B OH  
1969 N N   A VAL   B 153 ? 0.6424 0.6762 0.2565 0.1709  0.0429  0.0429  162 VAL   B N   
1970 N N   B VAL   B 153 ? 0.6422 0.6761 0.2564 0.1709  0.0429  0.0429  162 VAL   B N   
1971 N N   C VAL   B 153 ? 0.6463 0.6801 0.2605 0.1709  0.0429  0.0429  162 VAL   B N   
1972 N N   D VAL   B 153 ? 0.6463 0.6801 0.2605 0.1709  0.0429  0.0429  162 VAL   B N   
1973 C CA  A VAL   B 153 ? 0.6348 0.6597 0.2384 0.1730  0.0359  0.0363  162 VAL   B CA  
1974 C CA  B VAL   B 153 ? 0.6347 0.6596 0.2384 0.1730  0.0359  0.0364  162 VAL   B CA  
1975 C CA  C VAL   B 153 ? 0.6363 0.6613 0.2400 0.1730  0.0359  0.0364  162 VAL   B CA  
1976 C CA  D VAL   B 153 ? 0.6363 0.6613 0.2399 0.1730  0.0359  0.0364  162 VAL   B CA  
1977 C C   A VAL   B 153 ? 0.6181 0.6343 0.2262 0.1621  0.0350  0.0311  162 VAL   B C   
1978 C C   B VAL   B 153 ? 0.6181 0.6342 0.2262 0.1621  0.0350  0.0311  162 VAL   B C   
1979 C C   C VAL   B 153 ? 0.6184 0.6345 0.2264 0.1621  0.0350  0.0311  162 VAL   B C   
1980 C C   D VAL   B 153 ? 0.6184 0.6345 0.2264 0.1621  0.0350  0.0311  162 VAL   B C   
1981 O O   A VAL   B 153 ? 0.6141 0.6301 0.2255 0.1547  0.0361  0.0301  162 VAL   B O   
1982 O O   B VAL   B 153 ? 0.6141 0.6301 0.2255 0.1547  0.0361  0.0301  162 VAL   B O   
1983 O O   C VAL   B 153 ? 0.6142 0.6303 0.2257 0.1547  0.0361  0.0301  162 VAL   B O   
1984 O O   D VAL   B 153 ? 0.6142 0.6303 0.2257 0.1547  0.0361  0.0301  162 VAL   B O   
1985 C CB  A VAL   B 153 ? 0.6394 0.6643 0.2326 0.1782  0.0314  0.0347  162 VAL   B CB  
1986 C CB  B VAL   B 153 ? 0.6394 0.6643 0.2326 0.1782  0.0314  0.0347  162 VAL   B CB  
1987 C CB  C VAL   B 153 ? 0.6396 0.6646 0.2328 0.1782  0.0314  0.0347  162 VAL   B CB  
1988 C CB  D VAL   B 153 ? 0.6396 0.6646 0.2328 0.1782  0.0314  0.0347  162 VAL   B CB  
1989 C CG1 A VAL   B 153 ? 0.6441 0.6593 0.2281 0.1805  0.0244  0.0281  162 VAL   B CG1 
1990 C CG1 B VAL   B 153 ? 0.6441 0.6593 0.2281 0.1805  0.0244  0.0281  162 VAL   B CG1 
1991 C CG1 C VAL   B 153 ? 0.6441 0.6594 0.2280 0.1806  0.0244  0.0281  162 VAL   B CG1 
1992 C CG1 D VAL   B 153 ? 0.6441 0.6594 0.2281 0.1806  0.0244  0.0281  162 VAL   B CG1 
1993 C CG2 A VAL   B 153 ? 0.6473 0.6829 0.2370 0.1887  0.0330  0.0400  162 VAL   B CG2 
1994 C CG2 B VAL   B 153 ? 0.6474 0.6829 0.2370 0.1887  0.0330  0.0400  162 VAL   B CG2 
1995 C CG2 C VAL   B 153 ? 0.6485 0.6841 0.2382 0.1887  0.0330  0.0400  162 VAL   B CG2 
1996 C CG2 D VAL   B 153 ? 0.6485 0.6840 0.2381 0.1887  0.0330  0.0400  162 VAL   B CG2 
1997 N N   A SER   B 154 ? 0.6054 0.6159 0.2137 0.1616  0.0331  0.0279  163 SER   B N   
1998 N N   B SER   B 154 ? 0.6054 0.6159 0.2137 0.1616  0.0331  0.0279  163 SER   B N   
1999 N N   C SER   B 154 ? 0.6055 0.6159 0.2135 0.1616  0.0330  0.0278  163 SER   B N   
2000 N N   D SER   B 154 ? 0.6055 0.6159 0.2135 0.1616  0.0330  0.0278  163 SER   B N   
2001 C CA  A SER   B 154 ? 0.5908 0.5934 0.2029 0.1521  0.0320  0.0226  163 SER   B CA  
2002 C CA  B SER   B 154 ? 0.5908 0.5934 0.2029 0.1521  0.0320  0.0227  163 SER   B CA  
2003 C CA  C SER   B 154 ? 0.5893 0.5920 0.2015 0.1520  0.0321  0.0227  163 SER   B CA  
2004 C CA  D SER   B 154 ? 0.5893 0.5920 0.2015 0.1520  0.0321  0.0227  163 SER   B CA  
2005 C C   A SER   B 154 ? 0.5870 0.5813 0.1894 0.1523  0.0254  0.0171  163 SER   B C   
2006 C C   B SER   B 154 ? 0.5870 0.5814 0.1894 0.1523  0.0254  0.0171  163 SER   B C   
2007 C C   C SER   B 154 ? 0.5851 0.5794 0.1875 0.1526  0.0253  0.0171  163 SER   B C   
2008 C C   D SER   B 154 ? 0.5851 0.5794 0.1875 0.1525  0.0253  0.0171  163 SER   B C   
2009 O O   A SER   B 154 ? 0.5851 0.5782 0.1793 0.1609  0.0212  0.0158  163 SER   B O   
2010 O O   B SER   B 154 ? 0.5851 0.5782 0.1793 0.1609  0.0212  0.0158  163 SER   B O   
2011 O O   C SER   B 154 ? 0.5796 0.5728 0.1740 0.1612  0.0213  0.0158  163 SER   B O   
2012 O O   D SER   B 154 ? 0.5797 0.5729 0.1741 0.1612  0.0213  0.0158  163 SER   B O   
2013 C CB  A SER   B 154 ? 0.5896 0.5912 0.2075 0.1518  0.0336  0.0224  163 SER   B CB  
2014 C CB  B SER   B 154 ? 0.5896 0.5912 0.2075 0.1518  0.0336  0.0224  163 SER   B CB  
2015 C CB  C SER   B 154 ? 0.5884 0.5905 0.2073 0.1513  0.0342  0.0228  163 SER   B CB  
2016 C CB  D SER   B 154 ? 0.5884 0.5905 0.2073 0.1513  0.0342  0.0228  163 SER   B CB  
2017 O OG  A SER   B 154 ? 0.5855 0.5802 0.2070 0.1429  0.0325  0.0170  163 SER   B OG  
2018 O OG  B SER   B 154 ? 0.5855 0.5802 0.2070 0.1429  0.0325  0.0170  163 SER   B OG  
2019 O OG  C SER   B 154 ? 0.5847 0.5797 0.2069 0.1423  0.0328  0.0171  163 SER   B OG  
2020 O OG  D SER   B 154 ? 0.5847 0.5797 0.2069 0.1423  0.0328  0.0171  163 SER   B OG  
2021 N N   A ALA   B 155 ? 0.5731 0.5626 0.1769 0.1434  0.0245  0.0140  164 ALA   B N   
2022 N N   B ALA   B 155 ? 0.5731 0.5626 0.1768 0.1434  0.0245  0.0140  164 ALA   B N   
2023 N N   C ALA   B 155 ? 0.5691 0.5582 0.1728 0.1437  0.0243  0.0137  164 ALA   B N   
2024 N N   D ALA   B 155 ? 0.5692 0.5582 0.1729 0.1437  0.0243  0.0137  164 ALA   B N   
2025 C CA  A ALA   B 155 ? 0.5725 0.5525 0.1709 0.1410  0.0191  0.0086  164 ALA   B CA  
2026 C CA  B ALA   B 155 ? 0.5725 0.5525 0.1709 0.1410  0.0191  0.0086  164 ALA   B CA  
2027 C CA  C ALA   B 155 ? 0.5698 0.5495 0.1678 0.1419  0.0187  0.0084  164 ALA   B CA  
2028 C CA  D ALA   B 155 ? 0.5698 0.5495 0.1678 0.1418  0.0187  0.0084  164 ALA   B CA  
2029 C C   A ALA   B 155 ? 0.5691 0.5466 0.1693 0.1431  0.0180  0.0060  164 ALA   B C   
2030 C C   B ALA   B 155 ? 0.5691 0.5466 0.1693 0.1431  0.0180  0.0060  164 ALA   B C   
2031 C C   C ALA   B 155 ? 0.5676 0.5446 0.1675 0.1433  0.0177  0.0057  164 ALA   B C   
2032 C C   D ALA   B 155 ? 0.5676 0.5446 0.1675 0.1433  0.0177  0.0057  164 ALA   B C   
2033 O O   A ALA   B 155 ? 0.5727 0.5548 0.1807 0.1418  0.0225  0.0083  164 ALA   B O   
2034 O O   B ALA   B 155 ? 0.5728 0.5549 0.1808 0.1418  0.0225  0.0083  164 ALA   B O   
2035 O O   C ALA   B 155 ? 0.5750 0.5564 0.1824 0.1423  0.0219  0.0077  164 ALA   B O   
2036 O O   D ALA   B 155 ? 0.5749 0.5563 0.1823 0.1423  0.0219  0.0077  164 ALA   B O   
2037 C CB  A ALA   B 155 ? 0.5663 0.5437 0.1682 0.1301  0.0198  0.0067  164 ALA   B CB  
2038 C CB  B ALA   B 155 ? 0.5663 0.5437 0.1681 0.1301  0.0198  0.0067  164 ALA   B CB  
2039 C CB  C ALA   B 155 ? 0.5623 0.5389 0.1639 0.1307  0.0194  0.0063  164 ALA   B CB  
2040 C CB  D ALA   B 155 ? 0.5624 0.5390 0.1639 0.1306  0.0194  0.0063  164 ALA   B CB  
2041 N N   A ILE   B 156 ? 0.5689 0.5385 0.1625 0.1449  0.0120  0.0011  165 ILE   B N   
2042 N N   B ILE   B 156 ? 0.5689 0.5385 0.1624 0.1449  0.0120  0.0011  165 ILE   B N   
2043 N N   C ILE   B 156 ? 0.5684 0.5371 0.1615 0.1451  0.0114  0.0005  165 ILE   B N   
2044 N N   D ILE   B 156 ? 0.5684 0.5371 0.1615 0.1451  0.0114  0.0005  165 ILE   B N   
2045 C CA  A ILE   B 156 ? 0.5665 0.5310 0.1628 0.1414  0.0101  -0.0034 165 ILE   B CA  
2046 C CA  B ILE   B 156 ? 0.5665 0.5310 0.1628 0.1414  0.0101  -0.0034 165 ILE   B CA  
2047 C CA  C ILE   B 156 ? 0.5671 0.5311 0.1633 0.1417  0.0097  -0.0040 165 ILE   B CA  
2048 C CA  D ILE   B 156 ? 0.5671 0.5311 0.1633 0.1417  0.0097  -0.0040 165 ILE   B CA  
2049 C C   A ILE   B 156 ? 0.5597 0.5195 0.1598 0.1301  0.0106  -0.0055 165 ILE   B C   
2050 C C   B ILE   B 156 ? 0.5597 0.5195 0.1598 0.1301  0.0106  -0.0054 165 ILE   B C   
2051 C C   C ILE   B 156 ? 0.5595 0.5189 0.1598 0.1303  0.0103  -0.0061 165 ILE   B C   
2052 C C   D ILE   B 156 ? 0.5596 0.5189 0.1599 0.1302  0.0103  -0.0061 165 ILE   B C   
2053 O O   A ILE   B 156 ? 0.5628 0.5164 0.1579 0.1285  0.0069  -0.0072 165 ILE   B O   
2054 O O   B ILE   B 156 ? 0.5627 0.5164 0.1578 0.1285  0.0069  -0.0072 165 ILE   B O   
2055 O O   C ILE   B 156 ? 0.5647 0.5167 0.1609 0.1280  0.0061  -0.0091 165 ILE   B O   
2056 O O   D ILE   B 156 ? 0.5647 0.5167 0.1609 0.1280  0.0061  -0.0091 165 ILE   B O   
2057 C CB  A ILE   B 156 ? 0.5745 0.5338 0.1636 0.1483  0.0038  -0.0080 165 ILE   B CB  
2058 C CB  B ILE   B 156 ? 0.5745 0.5338 0.1636 0.1483  0.0038  -0.0080 165 ILE   B CB  
2059 C CB  C ILE   B 156 ? 0.5746 0.5333 0.1637 0.1482  0.0033  -0.0087 165 ILE   B CB  
2060 C CB  D ILE   B 156 ? 0.5746 0.5333 0.1637 0.1482  0.0033  -0.0087 165 ILE   B CB  
2061 C CG1 A ILE   B 156 ? 0.5797 0.5459 0.1640 0.1602  0.0033  -0.0058 165 ILE   B CG1 
2062 C CG1 B ILE   B 156 ? 0.5797 0.5459 0.1641 0.1602  0.0033  -0.0058 165 ILE   B CG1 
2063 C CG1 C ILE   B 156 ? 0.5815 0.5465 0.1651 0.1602  0.0025  -0.0066 165 ILE   B CG1 
2064 C CG1 D ILE   B 156 ? 0.5815 0.5464 0.1651 0.1602  0.0025  -0.0066 165 ILE   B CG1 
2065 C CG2 A ILE   B 156 ? 0.5752 0.5302 0.1676 0.1449  0.0016  -0.0132 165 ILE   B CG2 
2066 C CG2 B ILE   B 156 ? 0.5752 0.5302 0.1676 0.1449  0.0016  -0.0132 165 ILE   B CG2 
2067 C CG2 C ILE   B 156 ? 0.5746 0.5301 0.1673 0.1456  0.0015  -0.0135 165 ILE   B CG2 
2068 C CG2 D ILE   B 156 ? 0.5746 0.5301 0.1673 0.1456  0.0015  -0.0135 165 ILE   B CG2 
2069 C CD1 A ILE   B 156 ? 0.5885 0.5511 0.1659 0.1679  -0.0030 -0.0112 165 ILE   B CD1 
2070 C CD1 B ILE   B 156 ? 0.5886 0.5512 0.1659 0.1679  -0.0030 -0.0112 165 ILE   B CD1 
2071 C CD1 C ILE   B 156 ? 0.5908 0.5515 0.1674 0.1674  -0.0039 -0.0121 165 ILE   B CD1 
2072 C CD1 D ILE   B 156 ? 0.5907 0.5515 0.1674 0.1674  -0.0039 -0.0121 165 ILE   B CD1 
2073 N N   A THR   B 157 ? 0.5525 0.5158 0.1611 0.1231  0.0153  -0.0048 166 THR   B N   
2074 N N   B THR   B 157 ? 0.5525 0.5158 0.1612 0.1231  0.0153  -0.0048 166 THR   B N   
2075 N N   C THR   B 157 ? 0.5540 0.5178 0.1624 0.1236  0.0155  -0.0044 166 THR   B N   
2076 N N   D THR   B 157 ? 0.5539 0.5177 0.1624 0.1236  0.0155  -0.0044 166 THR   B N   
2077 C CA  A THR   B 157 ? 0.5464 0.5071 0.1595 0.1122  0.0161  -0.0075 166 THR   B CA  
2078 C CA  B THR   B 157 ? 0.5464 0.5071 0.1594 0.1122  0.0161  -0.0075 166 THR   B CA  
2079 C CA  C THR   B 157 ? 0.5462 0.5074 0.1595 0.1126  0.0164  -0.0072 166 THR   B CA  
2080 C CA  D THR   B 157 ? 0.5462 0.5074 0.1595 0.1126  0.0164  -0.0072 166 THR   B CA  
2081 C C   A THR   B 157 ? 0.5504 0.5055 0.1642 0.1107  0.0129  -0.0124 166 THR   B C   
2082 C C   B THR   B 157 ? 0.5504 0.5055 0.1642 0.1108  0.0129  -0.0124 166 THR   B C   
2083 C C   C THR   B 157 ? 0.5508 0.5066 0.1655 0.1102  0.0136  -0.0122 166 THR   B C   
2084 C C   D THR   B 157 ? 0.5508 0.5066 0.1655 0.1102  0.0136  -0.0122 166 THR   B C   
2085 O O   A THR   B 157 ? 0.5480 0.5051 0.1663 0.1120  0.0142  -0.0134 166 THR   B O   
2086 O O   B THR   B 157 ? 0.5480 0.5051 0.1662 0.1120  0.0142  -0.0134 166 THR   B O   
2087 O O   C THR   B 157 ? 0.5518 0.5096 0.1717 0.1102  0.0152  -0.0132 166 THR   B O   
2088 O O   D THR   B 157 ? 0.5517 0.5096 0.1716 0.1102  0.0152  -0.0132 166 THR   B O   
2089 C CB  A THR   B 157 ? 0.5375 0.5051 0.1599 0.1061  0.0221  -0.0059 166 THR   B CB  
2090 C CB  B THR   B 157 ? 0.5375 0.5051 0.1599 0.1061  0.0221  -0.0059 166 THR   B CB  
2091 C CB  C THR   B 157 ? 0.5378 0.5060 0.1603 0.1068  0.0225  -0.0054 166 THR   B CB  
2092 C CB  D THR   B 157 ? 0.5378 0.5060 0.1603 0.1068  0.0225  -0.0054 166 THR   B CB  
2093 O OG1 A THR   B 157 ? 0.5349 0.5083 0.1565 0.1112  0.0246  -0.0011 166 THR   B OG1 
2094 O OG1 B THR   B 157 ? 0.5349 0.5083 0.1565 0.1112  0.0246  -0.0011 166 THR   B OG1 
2095 O OG1 C THR   B 157 ? 0.5357 0.5098 0.1571 0.1110  0.0248  -0.0007 166 THR   B OG1 
2096 O OG1 D THR   B 157 ? 0.5357 0.5098 0.1571 0.1110  0.0248  -0.0007 166 THR   B OG1 
2097 C CG2 A THR   B 157 ? 0.5344 0.5017 0.1600 0.0956  0.0230  -0.0085 166 THR   B CG2 
2098 C CG2 B THR   B 157 ? 0.5344 0.5017 0.1600 0.0956  0.0230  -0.0085 166 THR   B CG2 
2099 C CG2 C THR   B 157 ? 0.5334 0.5014 0.1594 0.0960  0.0234  -0.0082 166 THR   B CG2 
2100 C CG2 D THR   B 157 ? 0.5334 0.5014 0.1594 0.0960  0.0234  -0.0082 166 THR   B CG2 
2101 N N   A GLN   B 158 ? 0.5557 0.5047 0.1675 0.1038  0.0101  -0.0150 167 GLN   B N   
2102 N N   B GLN   B 158 ? 0.5557 0.5046 0.1674 0.1038  0.0101  -0.0150 167 GLN   B N   
2103 N N   C GLN   B 158 ? 0.5554 0.5048 0.1671 0.1047  0.0102  -0.0148 167 GLN   B N   
2104 N N   D GLN   B 158 ? 0.5554 0.5048 0.1672 0.1046  0.0102  -0.0148 167 GLN   B N   
2105 C CA  A GLN   B 158 ? 0.5606 0.5044 0.1744 0.0997  0.0075  -0.0197 167 GLN   B CA  
2106 C CA  B GLN   B 158 ? 0.5606 0.5044 0.1744 0.0997  0.0075  -0.0197 167 GLN   B CA  
2107 C CA  C GLN   B 158 ? 0.5583 0.5029 0.1727 0.0997  0.0080  -0.0195 167 GLN   B CA  
2108 C CA  D GLN   B 158 ? 0.5583 0.5029 0.1727 0.0997  0.0080  -0.0195 167 GLN   B CA  
2109 C C   A GLN   B 158 ? 0.5692 0.5121 0.1856 0.0892  0.0085  -0.0203 167 GLN   B C   
2110 C C   B GLN   B 158 ? 0.5692 0.5120 0.1856 0.0892  0.0085  -0.0203 167 GLN   B C   
2111 C C   C GLN   B 158 ? 0.5655 0.5102 0.1830 0.0892  0.0097  -0.0199 167 GLN   B C   
2112 C C   D GLN   B 158 ? 0.5656 0.5102 0.1831 0.0892  0.0097  -0.0199 167 GLN   B C   
2113 O O   A GLN   B 158 ? 0.5684 0.5094 0.1803 0.0880  0.0075  -0.0179 167 GLN   B O   
2114 O O   B GLN   B 158 ? 0.5684 0.5093 0.1803 0.0880  0.0075  -0.0179 167 GLN   B O   
2115 O O   C GLN   B 158 ? 0.5622 0.5081 0.1768 0.0876  0.0104  -0.0169 167 GLN   B O   
2116 O O   D GLN   B 158 ? 0.5623 0.5082 0.1769 0.0876  0.0104  -0.0169 167 GLN   B O   
2117 C CB  A GLN   B 158 ? 0.5659 0.5023 0.1735 0.1051  0.0015  -0.0223 167 GLN   B CB  
2118 C CB  B GLN   B 158 ? 0.5659 0.5022 0.1735 0.1051  0.0015  -0.0223 167 GLN   B CB  
2119 C CB  C GLN   B 158 ? 0.5626 0.4994 0.1710 0.1042  0.0019  -0.0223 167 GLN   B CB  
2120 C CB  D GLN   B 158 ? 0.5626 0.4994 0.1710 0.1042  0.0019  -0.0223 167 GLN   B CB  
2121 C CG  A GLN   B 158 ? 0.5655 0.4973 0.1761 0.1017  -0.0013 -0.0275 167 GLN   B CG  
2122 C CG  B GLN   B 158 ? 0.5655 0.4973 0.1761 0.1017  -0.0013 -0.0275 167 GLN   B CG  
2123 C CG  C GLN   B 158 ? 0.5619 0.4944 0.1737 0.1003  -0.0005 -0.0274 167 GLN   B CG  
2124 C CG  D GLN   B 158 ? 0.5619 0.4945 0.1737 0.1003  -0.0005 -0.0274 167 GLN   B CG  
2125 C CD  A GLN   B 158 ? 0.5589 0.4959 0.1755 0.1021  0.0008  -0.0295 167 GLN   B CD  
2126 C CD  B GLN   B 158 ? 0.5589 0.4959 0.1755 0.1021  0.0008  -0.0295 167 GLN   B CD  
2127 C CD  C GLN   B 158 ? 0.5555 0.4932 0.1729 0.1017  0.0014  -0.0294 167 GLN   B CD  
2128 C CD  D GLN   B 158 ? 0.5555 0.4932 0.1729 0.1017  0.0014  -0.0294 167 GLN   B CD  
2129 O OE1 A GLN   B 158 ? 0.5507 0.4927 0.1734 0.0969  0.0054  -0.0283 167 GLN   B OE1 
2130 O OE1 B GLN   B 158 ? 0.5507 0.4927 0.1734 0.0970  0.0054  -0.0283 167 GLN   B OE1 
2131 O OE1 C GLN   B 158 ? 0.5467 0.4898 0.1702 0.0973  0.0061  -0.0281 167 GLN   B OE1 
2132 O OE1 D GLN   B 158 ? 0.5467 0.4898 0.1702 0.0973  0.0061  -0.0281 167 GLN   B OE1 
2133 N NE2 A GLN   B 158 ? 0.5613 0.4976 0.1766 0.1086  -0.0025 -0.0329 167 GLN   B NE2 
2134 N NE2 B GLN   B 158 ? 0.5613 0.4976 0.1766 0.1086  -0.0025 -0.0329 167 GLN   B NE2 
2135 N NE2 C GLN   B 158 ? 0.5583 0.4948 0.1740 0.1081  -0.0023 -0.0329 167 GLN   B NE2 
2136 N NE2 D GLN   B 158 ? 0.5583 0.4948 0.1741 0.1081  -0.0023 -0.0329 167 GLN   B NE2 
2137 N N   A GLY   B 159 ? 0.5806 0.5251 0.2036 0.0827  0.0103  -0.0233 168 GLY   B N   
2138 N N   B GLY   B 159 ? 0.5806 0.5251 0.2036 0.0827  0.0103  -0.0233 168 GLY   B N   
2139 N N   C GLY   B 159 ? 0.5798 0.5241 0.2027 0.0828  0.0102  -0.0233 168 GLY   B N   
2140 N N   D GLY   B 159 ? 0.5799 0.5242 0.2027 0.0828  0.0102  -0.0233 168 GLY   B N   
2141 C CA  A GLY   B 159 ? 0.5969 0.5421 0.2227 0.0728  0.0115  -0.0242 168 GLY   B CA  
2142 C CA  B GLY   B 159 ? 0.5969 0.5421 0.2227 0.0728  0.0115  -0.0242 168 GLY   B CA  
2143 C CA  C GLY   B 159 ? 0.5964 0.5414 0.2220 0.0729  0.0114  -0.0242 168 GLY   B CA  
2144 C CA  D GLY   B 159 ? 0.5964 0.5415 0.2220 0.0729  0.0114  -0.0242 168 GLY   B CA  
2145 C C   A GLY   B 159 ? 0.6225 0.5599 0.2457 0.0702  0.0071  -0.0262 168 GLY   B C   
2146 C C   B GLY   B 159 ? 0.6225 0.5599 0.2457 0.0702  0.0071  -0.0262 168 GLY   B C   
2147 C C   C GLY   B 159 ? 0.6220 0.5594 0.2452 0.0702  0.0071  -0.0262 168 GLY   B C   
2148 C C   D GLY   B 159 ? 0.6220 0.5594 0.2453 0.0702  0.0071  -0.0262 168 GLY   B C   
2149 O O   A GLY   B 159 ? 0.6347 0.5660 0.2546 0.0762  0.0030  -0.0277 168 GLY   B O   
2150 O O   B GLY   B 159 ? 0.6348 0.5661 0.2547 0.0762  0.0030  -0.0277 168 GLY   B O   
2151 O O   C GLY   B 159 ? 0.6356 0.5669 0.2555 0.0762  0.0029  -0.0277 168 GLY   B O   
2152 O O   D GLY   B 159 ? 0.6356 0.5668 0.2555 0.0762  0.0029  -0.0277 168 GLY   B O   
2153 N N   . LYS   B 160 ? 0.6468 0.5849 0.2720 0.0616  0.0080  -0.0262 169 LYS   B N   
2154 C CA  . LYS   B 160 ? 0.6986 0.6296 0.3230 0.0578  0.0044  -0.0273 169 LYS   B CA  
2155 C C   . LYS   B 160 ? 0.7611 0.6943 0.3926 0.0530  0.0053  -0.0320 169 LYS   B C   
2156 O O   . LYS   B 160 ? 0.7516 0.6930 0.3884 0.0486  0.0096  -0.0330 169 LYS   B O   
2157 C CB  . LYS   B 160 ? 0.7537 0.6853 0.3759 0.0517  0.0052  -0.0233 169 LYS   B CB  
2158 C CG  . LYS   B 160 ? 0.8020 0.7239 0.4218 0.0503  0.0011  -0.0221 169 LYS   B CG  
2159 C CD  . LYS   B 160 ? 0.8308 0.7540 0.4486 0.0445  0.0021  -0.0169 169 LYS   B CD  
2160 C CE  . LYS   B 160 ? 0.8553 0.7746 0.4766 0.0373  0.0011  -0.0167 169 LYS   B CE  
2161 N NZ  . LYS   B 160 ? 0.8928 0.8206 0.5146 0.0295  0.0046  -0.0128 169 LYS   B NZ  
2162 N N   . ARG   B 161 ? 0.8121 0.7390 0.4446 0.0537  0.0014  -0.0353 170 ARG   B N   
2163 C CA  . ARG   B 161 ? 0.8574 0.7860 0.4967 0.0479  0.0017  -0.0396 170 ARG   B CA  
2164 C C   . ARG   B 161 ? 0.9197 0.8457 0.5598 0.0395  0.0012  -0.0379 170 ARG   B C   
2165 O O   . ARG   B 161 ? 0.9296 0.8475 0.5658 0.0407  -0.0019 -0.0355 170 ARG   B O   
2166 C CB  . ARG   B 161 ? 0.8619 0.7865 0.5020 0.0542  -0.0022 -0.0442 170 ARG   B CB  
2167 C CG  . ARG   B 161 ? 0.8540 0.7828 0.5014 0.0511  -0.0016 -0.0493 170 ARG   B CG  
2168 C CD  . ARG   B 161 ? 0.8553 0.7798 0.5031 0.0565  -0.0066 -0.0542 170 ARG   B CD  
2169 N NE  . ARG   B 161 ? 0.8625 0.7902 0.5177 0.0512  -0.0066 -0.0588 170 ARG   B NE  
2170 C CZ  . ARG   B 161 ? 0.8604 0.7942 0.5200 0.0537  -0.0057 -0.0623 170 ARG   B CZ  
2171 N NH1 . ARG   B 161 ? 0.8432 0.7806 0.5009 0.0618  -0.0046 -0.0614 170 ARG   B NH1 
2172 N NH2 . ARG   B 161 ? 0.8815 0.8183 0.5479 0.0481  -0.0057 -0.0664 170 ARG   B NH2 
2173 N N   . GLU   B 162 ? 0.9910 0.9241 0.6363 0.0313  0.0046  -0.0386 171 GLU   B N   
2174 C CA  . GLU   B 162 ? 1.0555 0.9881 0.7023 0.0229  0.0048  -0.0363 171 GLU   B CA  
2175 C C   . GLU   B 162 ? 1.0646 0.9945 0.7175 0.0195  0.0027  -0.0408 171 GLU   B C   
2176 O O   . GLU   B 162 ? 1.1311 1.0535 0.7844 0.0172  -0.0002 -0.0398 171 GLU   B O   
2177 C CB  . GLU   B 162 ? 1.0961 1.0399 0.7447 0.0161  0.0098  -0.0346 171 GLU   B CB  
2178 C CG  . GLU   B 162 ? 1.1529 1.1015 0.7970 0.0190  0.0122  -0.0315 171 GLU   B CG  
2179 C CD  . GLU   B 162 ? 1.2265 1.1734 0.8643 0.0181  0.0117  -0.0250 171 GLU   B CD  
2180 O OE1 . GLU   B 162 ? 1.2715 1.2164 0.9042 0.0242  0.0109  -0.0224 171 GLU   B OE1 
2181 O OE2 . GLU   B 162 ? 1.2778 1.2263 0.9161 0.0116  0.0122  -0.0221 171 GLU   B OE2 
2182 S S   A DMS   C .   ? 1.1293 1.1589 0.8189 0.1395  0.0703  0.0511  201 DMS   B S   
2183 S S   B DMS   C .   ? 1.1293 1.1590 0.8189 0.1395  0.0703  0.0511  201 DMS   B S   
2184 O O   A DMS   C .   ? 1.1441 1.1806 0.8249 0.1475  0.0697  0.0562  201 DMS   B O   
2185 O O   B DMS   C .   ? 1.1442 1.1807 0.8250 0.1475  0.0697  0.0562  201 DMS   B O   
2186 C C1  A DMS   C .   ? 1.1261 1.1527 0.8169 0.1280  0.0684  0.0421  201 DMS   B C1  
2187 C C1  B DMS   C .   ? 1.1262 1.1528 0.8169 0.1280  0.0684  0.0421  201 DMS   B C1  
2188 C C2  A DMS   C .   ? 1.1282 1.1507 0.8043 0.1432  0.0632  0.0453  201 DMS   B C2  
2189 C C2  B DMS   C .   ? 1.1282 1.1507 0.8043 0.1432  0.0632  0.0453  201 DMS   B C2  
2190 S S   A DMS   D .   ? 4.6045 4.6522 4.4029 0.0101  0.0777  -0.0786 202 DMS   B S   
2191 S S   B DMS   D .   ? 4.6045 4.6522 4.4029 0.0101  0.0777  -0.0786 202 DMS   B S   
2192 O O   A DMS   D .   ? 4.5602 4.6019 4.3416 0.0135  0.0734  -0.0730 202 DMS   B O   
2193 O O   B DMS   D .   ? 4.5602 4.6019 4.3416 0.0135  0.0734  -0.0730 202 DMS   B O   
2194 C C1  A DMS   D .   ? 4.5382 4.5823 4.3539 0.0096  0.0811  -0.0838 202 DMS   B C1  
2195 C C1  B DMS   D .   ? 4.5382 4.5823 4.3539 0.0096  0.0811  -0.0838 202 DMS   B C1  
2196 C C2  A DMS   D .   ? 4.4851 4.5258 4.2882 0.0167  0.0800  -0.0693 202 DMS   B C2  
2197 C C2  B DMS   D .   ? 4.4851 4.5258 4.2882 0.0167  0.0800  -0.0693 202 DMS   B C2  
2198 S S   A DMS   E .   ? 0.8799 0.9032 0.5552 0.1138  0.0592  0.0265  203 DMS   B S   
2199 S S   B DMS   E .   ? 0.8800 0.9032 0.5553 0.1138  0.0592  0.0265  203 DMS   B S   
2200 O O   A DMS   E .   ? 0.8679 0.8877 0.5279 0.1168  0.0530  0.0243  203 DMS   B O   
2201 O O   B DMS   E .   ? 0.8679 0.8876 0.5278 0.1169  0.0529  0.0243  203 DMS   B O   
2202 C C1  A DMS   E .   ? 0.8774 0.8978 0.5621 0.1020  0.0602  0.0188  203 DMS   B C1  
2203 C C1  B DMS   E .   ? 0.8775 0.8978 0.5621 0.1020  0.0602  0.0188  203 DMS   B C1  
2204 C C2  A DMS   E .   ? 0.8775 0.9107 0.5616 0.1104  0.0637  0.0288  203 DMS   B C2  
2205 C C2  B DMS   E .   ? 0.8775 0.9108 0.5616 0.1104  0.0637  0.0288  203 DMS   B C2  
2206 N N1  C A1BG2 F .   ? 0.6570 0.6830 0.3585 0.0779  0.0624  0.0025  204 A1BG2 B N1  
2207 N N1  D A1BG2 F .   ? 0.6569 0.6830 0.3584 0.0779  0.0624  0.0025  204 A1BG2 B N1  
2208 N N3  C A1BG2 F .   ? 0.6786 0.7234 0.3616 0.1539  0.0735  0.0647  204 A1BG2 B N3  
2209 N N3  D A1BG2 F .   ? 0.6787 0.7235 0.3617 0.1539  0.0735  0.0647  204 A1BG2 B N3  
2210 C C4  C A1BG2 F .   ? 0.6585 0.6800 0.3463 0.0853  0.0583  0.0062  204 A1BG2 B C4  
2211 C C4  D A1BG2 F .   ? 0.6585 0.6799 0.3463 0.0853  0.0583  0.0062  204 A1BG2 B C4  
2212 C C5  C A1BG2 F .   ? 0.6590 0.6779 0.3443 0.0937  0.0586  0.0120  204 A1BG2 B C5  
2213 C C5  D A1BG2 F .   ? 0.6590 0.6779 0.3443 0.0938  0.0586  0.0120  204 A1BG2 B C5  
2214 C C6  C A1BG2 F .   ? 0.6594 0.6802 0.3569 0.0949  0.0637  0.0155  204 A1BG2 B C6  
2215 C C6  D A1BG2 F .   ? 0.6593 0.6802 0.3569 0.0949  0.0637  0.0155  204 A1BG2 B C6  
2216 C C7  C A1BG2 F .   ? 0.6598 0.6851 0.3587 0.1094  0.0680  0.0294  204 A1BG2 B C7  
2217 C C7  D A1BG2 F .   ? 0.6598 0.6851 0.3587 0.1094  0.0680  0.0294  204 A1BG2 B C7  
2218 C C8  C A1BG2 F .   ? 0.6626 0.6873 0.3550 0.1200  0.0673  0.0359  204 A1BG2 B C8  
2219 C C8  D A1BG2 F .   ? 0.6626 0.6873 0.3550 0.1200  0.0673  0.0359  204 A1BG2 B C8  
2220 C C10 C A1BG2 F .   ? 0.6670 0.6871 0.3465 0.1338  0.0630  0.0397  204 A1BG2 B C10 
2221 C C10 D A1BG2 F .   ? 0.6671 0.6871 0.3466 0.1338  0.0630  0.0397  204 A1BG2 B C10 
2222 C C13 C A1BG2 F .   ? 0.6800 0.7214 0.3672 0.1442  0.0730  0.0582  204 A1BG2 B C13 
2223 C C13 D A1BG2 F .   ? 0.6800 0.7214 0.3672 0.1442  0.0730  0.0582  204 A1BG2 B C13 
2224 C C15 C A1BG2 F .   ? 0.6820 0.7392 0.3721 0.1529  0.0790  0.0711  204 A1BG2 B C15 
2225 C C15 D A1BG2 F .   ? 0.6820 0.7392 0.3721 0.1529  0.0790  0.0711  204 A1BG2 B C15 
2226 C C1  C A1BG2 F .   ? 0.6514 0.6768 0.3797 0.0877  0.0742  0.0161  204 A1BG2 B C1  
2227 C C1  D A1BG2 F .   ? 0.6514 0.6768 0.3798 0.0877  0.0742  0.0161  204 A1BG2 B C1  
2228 C C2  C A1BG2 F .   ? 0.6531 0.6773 0.3660 0.0871  0.0683  0.0122  204 A1BG2 B C2  
2229 C C2  D A1BG2 F .   ? 0.6531 0.6773 0.3660 0.0871  0.0683  0.0122  204 A1BG2 B C2  
2230 C C3  C A1BG2 F .   ? 0.6532 0.6801 0.3674 0.0788  0.0673  0.0052  204 A1BG2 B C3  
2231 C C3  D A1BG2 F .   ? 0.6532 0.6800 0.3674 0.0788  0.0673  0.0052  204 A1BG2 B C3  
2232 N N2  C A1BG2 F .   ? 0.6571 0.6769 0.3520 0.1042  0.0644  0.0224  204 A1BG2 B N2  
2233 N N2  D A1BG2 F .   ? 0.6571 0.6769 0.3520 0.1042  0.0644  0.0224  204 A1BG2 B N2  
2234 O O1  C A1BG2 F .   ? 0.6590 0.6904 0.3666 0.1058  0.0716  0.0303  204 A1BG2 B O1  
2235 O O1  D A1BG2 F .   ? 0.6590 0.6903 0.3665 0.1058  0.0716  0.0303  204 A1BG2 B O1  
2236 C C9  C A1BG2 F .   ? 0.6625 0.6813 0.3481 0.1237  0.0638  0.0343  204 A1BG2 B C9  
2237 C C9  D A1BG2 F .   ? 0.6625 0.6813 0.3481 0.1237  0.0638  0.0343  204 A1BG2 B C9  
2238 C C11 C A1BG2 F .   ? 0.6718 0.6991 0.3515 0.1406  0.0659  0.0474  204 A1BG2 B C11 
2239 C C11 D A1BG2 F .   ? 0.6719 0.6991 0.3516 0.1406  0.0659  0.0474  204 A1BG2 B C11 
2240 C C12 C A1BG2 F .   ? 0.6724 0.7053 0.3592 0.1370  0.0697  0.0497  204 A1BG2 B C12 
2241 C C12 D A1BG2 F .   ? 0.6724 0.7053 0.3592 0.1370  0.0697  0.0497  204 A1BG2 B C12 
2242 C C14 C A1BG2 F .   ? 0.6826 0.7364 0.3655 0.1593  0.0763  0.0717  204 A1BG2 B C14 
2243 C C14 D A1BG2 F .   ? 0.6827 0.7365 0.3656 0.1593  0.0763  0.0717  204 A1BG2 B C14 
2244 S S1  C A1BG2 F .   ? 0.6892 0.7387 0.3818 0.1410  0.0762  0.0604  204 A1BG2 B S1  
2245 S S1  D A1BG2 F .   ? 0.6890 0.7385 0.3816 0.1410  0.0762  0.0604  204 A1BG2 B S1  
2246 C C16 C A1BG2 F .   ? 0.6668 0.6982 0.3599 0.1266  0.0702  0.0436  204 A1BG2 B C16 
2247 C C16 D A1BG2 F .   ? 0.6667 0.6982 0.3599 0.1266  0.0702  0.0436  204 A1BG2 B C16 
2248 S S   C SO4   G .   ? 1.2427 1.2907 1.0439 0.0094  0.0782  -0.0802 205 SO4   B S   
2249 S S   D SO4   G .   ? 1.2427 1.2907 1.0439 0.0094  0.0782  -0.0802 205 SO4   B S   
2250 O O1  C SO4   G .   ? 1.2357 1.2747 1.0459 0.0148  0.0808  -0.0748 205 SO4   B O1  
2251 O O1  D SO4   G .   ? 1.2357 1.2747 1.0459 0.0148  0.0808  -0.0748 205 SO4   B O1  
2252 O O2  C SO4   G .   ? 1.2202 1.2771 1.0341 0.0029  0.0806  -0.0912 205 SO4   B O2  
2253 O O2  D SO4   G .   ? 1.2202 1.2771 1.0341 0.0029  0.0806  -0.0912 205 SO4   B O2  
2254 O O3  C SO4   G .   ? 1.2225 1.2670 1.0093 0.0107  0.0743  -0.0778 205 SO4   B O3  
2255 O O3  D SO4   G .   ? 1.2225 1.2670 1.0093 0.0107  0.0743  -0.0778 205 SO4   B O3  
2256 O O4  C SO4   G .   ? 1.2511 1.3038 1.0457 0.0095  0.0773  -0.0773 205 SO4   B O4  
2257 O O4  D SO4   G .   ? 1.2511 1.3038 1.0457 0.0095  0.0773  -0.0773 205 SO4   B O4  
2258 S S   C DMS   H .   ? 0.9620 1.0466 0.5645 0.2335  0.0520  0.0767  206 DMS   B S   
2259 S S   D DMS   H .   ? 0.9619 1.0465 0.5643 0.2335  0.0520  0.0767  206 DMS   B S   
2260 O O   C DMS   H .   ? 0.9760 1.0758 0.5798 0.2428  0.0574  0.0879  206 DMS   B O   
2261 O O   D DMS   H .   ? 0.9758 1.0756 0.5796 0.2428  0.0574  0.0879  206 DMS   B O   
2262 C C1  C DMS   H .   ? 0.9579 1.0416 0.5432 0.2417  0.0427  0.0666  206 DMS   B C1  
2263 C C1  D DMS   H .   ? 0.9579 1.0417 0.5432 0.2417  0.0427  0.0666  206 DMS   B C1  
2264 C C2  C DMS   H .   ? 0.9539 1.0327 0.5593 0.2322  0.0505  0.0739  206 DMS   B C2  
2265 C C2  D DMS   H .   ? 0.9539 1.0327 0.5593 0.2322  0.0505  0.0739  206 DMS   B C2  
2266 S S   C DMS   I .   ? 0.8840 0.9297 0.6306 0.1195  0.0924  0.0604  207 DMS   B S   
2267 S S   D DMS   I .   ? 0.8839 0.9296 0.6305 0.1195  0.0924  0.0604  207 DMS   B S   
2268 O O   C DMS   I .   ? 0.8827 0.9279 0.6246 0.1296  0.0929  0.0685  207 DMS   B O   
2269 O O   D DMS   I .   ? 0.8827 0.9280 0.6246 0.1296  0.0929  0.0685  207 DMS   B O   
2270 C C1  C DMS   I .   ? 0.8766 0.9201 0.6476 0.1099  0.0988  0.0583  207 DMS   B C1  
2271 C C1  D DMS   I .   ? 0.8766 0.9200 0.6476 0.1099  0.0988  0.0583  207 DMS   B C1  
2272 C C2  C DMS   I .   ? 0.8766 0.9330 0.6274 0.1206  0.0959  0.0660  207 DMS   B C2  
2273 C C2  D DMS   I .   ? 0.8766 0.9330 0.6274 0.1206  0.0959  0.0660  207 DMS   B C2  
# 
