data_7HP2
# 
_entry.id   7HP2 
# 
_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   7HP2         pdb_00007hp2 10.2210/pdb7hp2/pdb 
WWPDB D_1001407752 ?            ?                   
# 
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' 
# 
_pdbx_database_status.entry_id                        7HP2 
_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    10 ?                           ?    ? ? 
4 non-polymer syn 
'3-chloro-5-[({3-[(dimethylamino)methyl]-4-hydroxyphenyl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' 405.918   1  ? 
?    ? ? 
5 non-polymer syn 'SULFATE ION' 96.063    1  ?                           ?    ? ? 
6 water       nat water 18.015    45 ?                           ?    ? ? 
# 
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 '3-chloro-5-[({3-[(dimethylamino)methyl]-4-hydroxyphenyl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' A1BHC 
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 
A1BHC non-polymer         . 
'3-chloro-5-[({3-[(dimethylamino)methyl]-4-hydroxyphenyl}methyl)amino]-N-(1-hydroxy-2-methylpropan-2-yl)benzamide' ? 
'C21 H28 Cl N3 O3' 405.918 
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        A1BHC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BHC 
_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  101 101 DMS   DMS A . 
D 3 DMS   1  102 304 DMS   DMS A . 
E 3 DMS   1  103 2   DMS   DMS A . 
F 3 DMS   1  201 201 DMS   DMS B . 
G 3 DMS   1  202 202 DMS   DMS B . 
H 3 DMS   1  203 203 DMS   DMS B . 
I 4 A1BHC 1  204 301 A1BHC LIG B . 
J 5 SO4   1  205 303 SO4   SO4 B . 
K 3 DMS   1  206 305 DMS   DMS B . 
L 3 DMS   1  207 306 DMS   DMS B . 
M 3 DMS   1  208 307 DMS   DMS B . 
N 3 DMS   1  209 1   DMS   DMS B . 
O 6 HOH   1  201 6   HOH   HOH A . 
O 6 HOH   2  202 34  HOH   HOH A . 
O 6 HOH   3  203 9   HOH   HOH A . 
O 6 HOH   4  204 11  HOH   HOH A . 
O 6 HOH   5  205 40  HOH   HOH A . 
O 6 HOH   6  206 33  HOH   HOH A . 
O 6 HOH   7  207 39  HOH   HOH A . 
O 6 HOH   8  208 24  HOH   HOH A . 
O 6 HOH   9  209 35  HOH   HOH A . 
O 6 HOH   10 210 14  HOH   HOH A . 
O 6 HOH   11 211 38  HOH   HOH A . 
O 6 HOH   12 212 37  HOH   HOH A . 
P 6 HOH   1  301 30  HOH   HOH B . 
P 6 HOH   2  302 13  HOH   HOH B . 
P 6 HOH   3  303 17  HOH   HOH B . 
P 6 HOH   4  304 7   HOH   HOH B . 
P 6 HOH   5  305 16  HOH   HOH B . 
P 6 HOH   6  306 36  HOH   HOH B . 
P 6 HOH   7  307 31  HOH   HOH B . 
P 6 HOH   8  308 20  HOH   HOH B . 
P 6 HOH   9  309 25  HOH   HOH B . 
P 6 HOH   10 310 22  HOH   HOH B . 
P 6 HOH   11 311 29  HOH   HOH B . 
P 6 HOH   12 312 5   HOH   HOH B . 
P 6 HOH   13 313 45  HOH   HOH B . 
P 6 HOH   14 314 18  HOH   HOH B . 
P 6 HOH   15 315 28  HOH   HOH B . 
P 6 HOH   16 316 19  HOH   HOH B . 
P 6 HOH   17 317 2   HOH   HOH B . 
P 6 HOH   18 318 4   HOH   HOH B . 
P 6 HOH   19 319 15  HOH   HOH B . 
P 6 HOH   20 320 42  HOH   HOH B . 
P 6 HOH   21 321 27  HOH   HOH B . 
P 6 HOH   22 322 43  HOH   HOH B . 
P 6 HOH   23 323 1   HOH   HOH B . 
P 6 HOH   24 324 12  HOH   HOH B . 
P 6 HOH   25 325 23  HOH   HOH B . 
P 6 HOH   26 326 26  HOH   HOH B . 
P 6 HOH   27 327 21  HOH   HOH B . 
P 6 HOH   28 328 8   HOH   HOH B . 
P 6 HOH   29 329 41  HOH   HOH B . 
P 6 HOH   30 330 10  HOH   HOH B . 
P 6 HOH   31 331 3   HOH   HOH B . 
P 6 HOH   32 332 32  HOH   HOH B . 
P 6 HOH   33 333 44  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           7HP2 
_cell.length_a           42.119 
_cell.length_b           42.119 
_cell.length_c           215.607 
_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                         7HP2 
_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          7HP2 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.06 
_exptl_crystal.density_percent_sol   40.35 
_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   2023-09-29 
_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                     7HP2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             215.62 
_reflns.d_resolution_high            1.54 
_reflns.number_obs                   30137 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.084 
_reflns.pdbx_netI_over_sigmaI        14.3 
_reflns.pdbx_redundancy              25.1 
_reflns.pdbx_Rrim_I_all              0.086 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     756986 
_reflns.pdbx_chi_squared             0.31 
_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                  1.54 
_reflns_shell.d_res_low                   1.57 
_reflns_shell.number_measured_all         32290 
_reflns_shell.number_unique_obs           1529 
_reflns_shell.Rmerge_I_obs                8.470 
_reflns_shell.pdbx_chi_squared            0.09 
_reflns_shell.pdbx_redundancy             21.1 
_reflns_shell.percent_possible_obs        99.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             8.679 
_reflns_shell.pdbx_Rpim_I_all             1.877 
_reflns_shell.pdbx_CC_half                0.425 
_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                                 7HP2 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25320 
_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                             53.90 
_refine.ls_d_res_high                            1.54 
_refine.ls_percent_reflns_obs                    88.90 
_refine.ls_R_factor_obs                          0.24915 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.24671 
_refine.ls_R_factor_R_free                       0.29563 
_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                  1366 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               47.400 
_refine.aniso_B[1][1]                            -1.14 
_refine.aniso_B[2][2]                            -1.14 
_refine.aniso_B[3][3]                            2.28 
_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                       0.157 
_refine.pdbx_overall_ESU_R_Free                  0.149 
_refine.overall_SU_ML                            0.241 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             18.164 
_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         73 
_refine_hist.number_atoms_solvent             45 
_refine_hist.number_atoms_total               1594 
_refine_hist.d_res_high                       1.54 
_refine_hist.d_res_low                        53.90 
# 
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             0.013  0.014  ? 2968 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.004  0.015  ? 2236 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.649  1.631  ? 3230 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.311  1.586  ? 5138 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.513  5.000  ? 310  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.850 23.853 ? 109  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.961 15.000 ? 364  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       13.877 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.084  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 2765 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 507  '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                  1.277  1.418  ? 1487 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.299  1.248  ? 1433 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.239  1.814  ? 1500 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.239  1.819  ? 1501 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.423  1.692  ? 1480 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.423  1.698  ? 1481 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.504  2.256  ? 1731 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.310  13.770 ? 2446 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         9.308  13.826 ? 2447 '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                       1.542 
_refine_ls_shell.d_res_low                        1.582 
_refine_ls_shell.number_reflns_R_work             418 
_refine_ls_shell.R_factor_R_work                  0.579 
_refine_ls_shell.percent_reflns_obs               20.37 
_refine_ls_shell.R_factor_R_free                  0.596 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HP2 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014767-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HP2 
_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 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 6 ? 
P 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 7HP2 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HP2 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 7HP2 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HP2 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HP2 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HP2 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)' 5900  ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  10720 ? 
# 
_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,M,N,O,P 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? B CYS 134 SG ? ? ? 1_555 B CYS 134 SG ? ? B CYS 143 B CYS 143 8_554 ? ? ? ? ? ? ? 2.038 ? ? 
covale1 covale none ? E DMS .   S  C ? ? 1_555 N DMS .   C1 C ? A DMS 103 B DMS 209 8_664 ? ? ? ? ? ? ? 1.656 ? ? 
covale2 covale none ? E DMS .   S  D ? ? 1_555 N DMS .   C1 D ? A DMS 103 B DMS 209 8_664 ? ? ? ? ? ? ? 1.656 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
_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_554 
_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 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? VAL A 44  ? PHE A 84  VAL A 87  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N TYR B 14  ? N TYR B 23  O GLY B 30  ? O GLY B 39  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O VAL A 44  ? O VAL A 87  N ASP A 32  ? N ASP A 75  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HP2 
_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 
# 
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 C B GLY 70  ? ? O B GLY 70  ? ? 1.333 1.232 0.101 0.016 N 
2 1 C B ASN 152 ? A O B ASN 152 ? A 1.364 1.229 0.135 0.019 N 
3 1 C B ASN 152 ? B O B ASN 152 ? B 1.362 1.229 0.133 0.019 N 
4 1 C B ASN 152 ? C O B ASN 152 ? C 1.367 1.229 0.138 0.019 N 
5 1 C B ASN 152 ? D O B ASN 152 ? D 1.366 1.229 0.137 0.019 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 64  ? A 62.88   68.96  
2 1 ASP A 64  ? B 62.88   68.96  
3 1 LYS B 54  ? ? 49.51   29.80  
4 1 CYS B 80  ? ? 78.44   -2.82  
5 1 LEU B 92  ? ? -121.80 -51.35 
6 1 ALA B 127 ? ? -103.31 78.99  
7 1 ALA B 127 ? ? -103.37 78.99  
8 1 LYS B 157 ? C 53.18   -95.83 
9 1 LYS B 157 ? D 53.22   -95.78 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     319 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   P 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 8.3349 18.2247 -19.4974 0.4963 0.4966 0.0442 0.1301 0.0683 0.0534 1.7220 2.0316 1.9579 -0.2484 
-0.2558 -0.0571 0.2723 0.2174 0.2695 -0.2003 -0.2502 -0.0697 0.1780 0.2590 -0.0221 
'X-RAY DIFFRACTION' 2 ? refined 3.6775 20.7287 -15.8664 0.5207 0.5335 0.1193 0.1270 0.0539 0.0327 0.8526 0.1163 0.4944 -0.0187 
0.3367  -0.0395 0.2305 0.1238 0.1386 -0.0879 -0.1923 0.0502  0.0795 0.0972 -0.0382 
# 
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 101 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 16 ? ? B 307 ? ? ? ? 
# 
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 
A1BHC N1   N  N N 1   
A1BHC N3   N  N N 2   
A1BHC C4   C  Y N 3   
A1BHC C5   C  Y N 4   
A1BHC C6   C  Y N 5   
A1BHC C7   C  N N 6   
A1BHC C8   C  Y N 7   
A1BHC C10  C  Y N 8   
A1BHC C13  C  N N 9   
A1BHC C15  C  N N 10  
A1BHC C17  C  N N 11  
A1BHC C20  C  Y N 12  
A1BHC C21  C  Y N 13  
A1BHC C1   C  N N 14  
A1BHC C2   C  N N 15  
A1BHC C3   C  N N 16  
A1BHC N2   N  N N 17  
A1BHC C9   C  Y N 18  
A1BHC CL1  CL N N 19  
A1BHC C11  C  Y N 20  
A1BHC C12  C  Y N 21  
A1BHC O1   O  N N 22  
A1BHC C14  C  N N 23  
A1BHC C16  C  N N 24  
A1BHC O2   O  N N 25  
A1BHC C18  C  Y N 26  
A1BHC C19  C  Y N 27  
A1BHC O3   O  N N 28  
A1BHC H2   H  N N 29  
A1BHC H3   H  N N 30  
A1BHC H4   H  N N 31  
A1BHC H5   H  N N 32  
A1BHC H6   H  N N 33  
A1BHC H7   H  N N 34  
A1BHC H8   H  N N 35  
A1BHC H9   H  N N 36  
A1BHC H10  H  N N 37  
A1BHC H11  H  N N 38  
A1BHC H12  H  N N 39  
A1BHC H13  H  N N 40  
A1BHC H14  H  N N 41  
A1BHC H15  H  N N 42  
A1BHC H16  H  N N 43  
A1BHC H17  H  N N 44  
A1BHC H18  H  N N 45  
A1BHC H19  H  N N 46  
A1BHC H20  H  N N 47  
A1BHC H21  H  N N 48  
A1BHC H22  H  N N 49  
A1BHC H23  H  N N 50  
A1BHC H24  H  N N 51  
A1BHC H25  H  N N 52  
A1BHC H26  H  N N 53  
A1BHC H27  H  N N 54  
A1BHC H28  H  N N 55  
A1BHC H29  H  N N 56  
ALA   N    N  N N 57  
ALA   CA   C  N S 58  
ALA   C    C  N N 59  
ALA   O    O  N N 60  
ALA   CB   C  N N 61  
ALA   OXT  O  N N 62  
ALA   H    H  N N 63  
ALA   H2   H  N N 64  
ALA   HA   H  N N 65  
ALA   HB1  H  N N 66  
ALA   HB2  H  N N 67  
ALA   HB3  H  N N 68  
ALA   HXT  H  N N 69  
ARG   N    N  N N 70  
ARG   CA   C  N S 71  
ARG   C    C  N N 72  
ARG   O    O  N N 73  
ARG   CB   C  N N 74  
ARG   CG   C  N N 75  
ARG   CD   C  N N 76  
ARG   NE   N  N N 77  
ARG   CZ   C  N N 78  
ARG   NH1  N  N N 79  
ARG   NH2  N  N N 80  
ARG   OXT  O  N N 81  
ARG   H    H  N N 82  
ARG   H2   H  N N 83  
ARG   HA   H  N N 84  
ARG   HB2  H  N N 85  
ARG   HB3  H  N N 86  
ARG   HG2  H  N N 87  
ARG   HG3  H  N N 88  
ARG   HD2  H  N N 89  
ARG   HD3  H  N N 90  
ARG   HE   H  N N 91  
ARG   HH11 H  N N 92  
ARG   HH12 H  N N 93  
ARG   HH21 H  N N 94  
ARG   HH22 H  N N 95  
ARG   HXT  H  N N 96  
ASN   N    N  N N 97  
ASN   CA   C  N S 98  
ASN   C    C  N N 99  
ASN   O    O  N N 100 
ASN   CB   C  N N 101 
ASN   CG   C  N N 102 
ASN   OD1  O  N N 103 
ASN   ND2  N  N N 104 
ASN   OXT  O  N N 105 
ASN   H    H  N N 106 
ASN   H2   H  N N 107 
ASN   HA   H  N N 108 
ASN   HB2  H  N N 109 
ASN   HB3  H  N N 110 
ASN   HD21 H  N N 111 
ASN   HD22 H  N N 112 
ASN   HXT  H  N N 113 
ASP   N    N  N N 114 
ASP   CA   C  N S 115 
ASP   C    C  N N 116 
ASP   O    O  N N 117 
ASP   CB   C  N N 118 
ASP   CG   C  N N 119 
ASP   OD1  O  N N 120 
ASP   OD2  O  N N 121 
ASP   OXT  O  N N 122 
ASP   H    H  N N 123 
ASP   H2   H  N N 124 
ASP   HA   H  N N 125 
ASP   HB2  H  N N 126 
ASP   HB3  H  N N 127 
ASP   HD2  H  N N 128 
ASP   HXT  H  N N 129 
CYS   N    N  N N 130 
CYS   CA   C  N R 131 
CYS   C    C  N N 132 
CYS   O    O  N N 133 
CYS   CB   C  N N 134 
CYS   SG   S  N N 135 
CYS   OXT  O  N N 136 
CYS   H    H  N N 137 
CYS   H2   H  N N 138 
CYS   HA   H  N N 139 
CYS   HB2  H  N N 140 
CYS   HB3  H  N N 141 
CYS   HG   H  N N 142 
CYS   HXT  H  N N 143 
DMS   S    S  N N 144 
DMS   O    O  N N 145 
DMS   C1   C  N N 146 
DMS   C2   C  N N 147 
DMS   H11  H  N N 148 
DMS   H12  H  N N 149 
DMS   H13  H  N N 150 
DMS   H21  H  N N 151 
DMS   H22  H  N N 152 
DMS   H23  H  N N 153 
GLN   N    N  N N 154 
GLN   CA   C  N S 155 
GLN   C    C  N N 156 
GLN   O    O  N N 157 
GLN   CB   C  N N 158 
GLN   CG   C  N N 159 
GLN   CD   C  N N 160 
GLN   OE1  O  N N 161 
GLN   NE2  N  N N 162 
GLN   OXT  O  N N 163 
GLN   H    H  N N 164 
GLN   H2   H  N N 165 
GLN   HA   H  N N 166 
GLN   HB2  H  N N 167 
GLN   HB3  H  N N 168 
GLN   HG2  H  N N 169 
GLN   HG3  H  N N 170 
GLN   HE21 H  N N 171 
GLN   HE22 H  N N 172 
GLN   HXT  H  N N 173 
GLU   N    N  N N 174 
GLU   CA   C  N S 175 
GLU   C    C  N N 176 
GLU   O    O  N N 177 
GLU   CB   C  N N 178 
GLU   CG   C  N N 179 
GLU   CD   C  N N 180 
GLU   OE1  O  N N 181 
GLU   OE2  O  N N 182 
GLU   OXT  O  N N 183 
GLU   H    H  N N 184 
GLU   H2   H  N N 185 
GLU   HA   H  N N 186 
GLU   HB2  H  N N 187 
GLU   HB3  H  N N 188 
GLU   HG2  H  N N 189 
GLU   HG3  H  N N 190 
GLU   HE2  H  N N 191 
GLU   HXT  H  N N 192 
GLY   N    N  N N 193 
GLY   CA   C  N N 194 
GLY   C    C  N N 195 
GLY   O    O  N N 196 
GLY   OXT  O  N N 197 
GLY   H    H  N N 198 
GLY   H2   H  N N 199 
GLY   HA2  H  N N 200 
GLY   HA3  H  N N 201 
GLY   HXT  H  N N 202 
HIS   N    N  N N 203 
HIS   CA   C  N S 204 
HIS   C    C  N N 205 
HIS   O    O  N N 206 
HIS   CB   C  N N 207 
HIS   CG   C  Y N 208 
HIS   ND1  N  Y N 209 
HIS   CD2  C  Y N 210 
HIS   CE1  C  Y N 211 
HIS   NE2  N  Y N 212 
HIS   OXT  O  N N 213 
HIS   H    H  N N 214 
HIS   H2   H  N N 215 
HIS   HA   H  N N 216 
HIS   HB2  H  N N 217 
HIS   HB3  H  N N 218 
HIS   HD1  H  N N 219 
HIS   HD2  H  N N 220 
HIS   HE1  H  N N 221 
HIS   HE2  H  N N 222 
HIS   HXT  H  N N 223 
HOH   O    O  N N 224 
HOH   H1   H  N N 225 
HOH   H2   H  N N 226 
ILE   N    N  N N 227 
ILE   CA   C  N S 228 
ILE   C    C  N N 229 
ILE   O    O  N N 230 
ILE   CB   C  N S 231 
ILE   CG1  C  N N 232 
ILE   CG2  C  N N 233 
ILE   CD1  C  N N 234 
ILE   OXT  O  N N 235 
ILE   H    H  N N 236 
ILE   H2   H  N N 237 
ILE   HA   H  N N 238 
ILE   HB   H  N N 239 
ILE   HG12 H  N N 240 
ILE   HG13 H  N N 241 
ILE   HG21 H  N N 242 
ILE   HG22 H  N N 243 
ILE   HG23 H  N N 244 
ILE   HD11 H  N N 245 
ILE   HD12 H  N N 246 
ILE   HD13 H  N N 247 
ILE   HXT  H  N N 248 
LEU   N    N  N N 249 
LEU   CA   C  N S 250 
LEU   C    C  N N 251 
LEU   O    O  N N 252 
LEU   CB   C  N N 253 
LEU   CG   C  N N 254 
LEU   CD1  C  N N 255 
LEU   CD2  C  N N 256 
LEU   OXT  O  N N 257 
LEU   H    H  N N 258 
LEU   H2   H  N N 259 
LEU   HA   H  N N 260 
LEU   HB2  H  N N 261 
LEU   HB3  H  N N 262 
LEU   HG   H  N N 263 
LEU   HD11 H  N N 264 
LEU   HD12 H  N N 265 
LEU   HD13 H  N N 266 
LEU   HD21 H  N N 267 
LEU   HD22 H  N N 268 
LEU   HD23 H  N N 269 
LEU   HXT  H  N N 270 
LYS   N    N  N N 271 
LYS   CA   C  N S 272 
LYS   C    C  N N 273 
LYS   O    O  N N 274 
LYS   CB   C  N N 275 
LYS   CG   C  N N 276 
LYS   CD   C  N N 277 
LYS   CE   C  N N 278 
LYS   NZ   N  N N 279 
LYS   OXT  O  N N 280 
LYS   H    H  N N 281 
LYS   H2   H  N N 282 
LYS   HA   H  N N 283 
LYS   HB2  H  N N 284 
LYS   HB3  H  N N 285 
LYS   HG2  H  N N 286 
LYS   HG3  H  N N 287 
LYS   HD2  H  N N 288 
LYS   HD3  H  N N 289 
LYS   HE2  H  N N 290 
LYS   HE3  H  N N 291 
LYS   HZ1  H  N N 292 
LYS   HZ2  H  N N 293 
LYS   HZ3  H  N N 294 
LYS   HXT  H  N N 295 
MET   N    N  N N 296 
MET   CA   C  N S 297 
MET   C    C  N N 298 
MET   O    O  N N 299 
MET   CB   C  N N 300 
MET   CG   C  N N 301 
MET   SD   S  N N 302 
MET   CE   C  N N 303 
MET   OXT  O  N N 304 
MET   H    H  N N 305 
MET   H2   H  N N 306 
MET   HA   H  N N 307 
MET   HB2  H  N N 308 
MET   HB3  H  N N 309 
MET   HG2  H  N N 310 
MET   HG3  H  N N 311 
MET   HE1  H  N N 312 
MET   HE2  H  N N 313 
MET   HE3  H  N N 314 
MET   HXT  H  N N 315 
PHE   N    N  N N 316 
PHE   CA   C  N S 317 
PHE   C    C  N N 318 
PHE   O    O  N N 319 
PHE   CB   C  N N 320 
PHE   CG   C  Y N 321 
PHE   CD1  C  Y N 322 
PHE   CD2  C  Y N 323 
PHE   CE1  C  Y N 324 
PHE   CE2  C  Y N 325 
PHE   CZ   C  Y N 326 
PHE   OXT  O  N N 327 
PHE   H    H  N N 328 
PHE   H2   H  N N 329 
PHE   HA   H  N N 330 
PHE   HB2  H  N N 331 
PHE   HB3  H  N N 332 
PHE   HD1  H  N N 333 
PHE   HD2  H  N N 334 
PHE   HE1  H  N N 335 
PHE   HE2  H  N N 336 
PHE   HZ   H  N N 337 
PHE   HXT  H  N N 338 
PRO   N    N  N N 339 
PRO   CA   C  N S 340 
PRO   C    C  N N 341 
PRO   O    O  N N 342 
PRO   CB   C  N N 343 
PRO   CG   C  N N 344 
PRO   CD   C  N N 345 
PRO   OXT  O  N N 346 
PRO   H    H  N N 347 
PRO   HA   H  N N 348 
PRO   HB2  H  N N 349 
PRO   HB3  H  N N 350 
PRO   HG2  H  N N 351 
PRO   HG3  H  N N 352 
PRO   HD2  H  N N 353 
PRO   HD3  H  N N 354 
PRO   HXT  H  N N 355 
SER   N    N  N N 356 
SER   CA   C  N S 357 
SER   C    C  N N 358 
SER   O    O  N N 359 
SER   CB   C  N N 360 
SER   OG   O  N N 361 
SER   OXT  O  N N 362 
SER   H    H  N N 363 
SER   H2   H  N N 364 
SER   HA   H  N N 365 
SER   HB2  H  N N 366 
SER   HB3  H  N N 367 
SER   HG   H  N N 368 
SER   HXT  H  N N 369 
SO4   S    S  N N 370 
SO4   O1   O  N N 371 
SO4   O2   O  N N 372 
SO4   O3   O  N N 373 
SO4   O4   O  N N 374 
THR   N    N  N N 375 
THR   CA   C  N S 376 
THR   C    C  N N 377 
THR   O    O  N N 378 
THR   CB   C  N R 379 
THR   OG1  O  N N 380 
THR   CG2  C  N N 381 
THR   OXT  O  N N 382 
THR   H    H  N N 383 
THR   H2   H  N N 384 
THR   HA   H  N N 385 
THR   HB   H  N N 386 
THR   HG1  H  N N 387 
THR   HG21 H  N N 388 
THR   HG22 H  N N 389 
THR   HG23 H  N N 390 
THR   HXT  H  N N 391 
TRP   N    N  N N 392 
TRP   CA   C  N S 393 
TRP   C    C  N N 394 
TRP   O    O  N N 395 
TRP   CB   C  N N 396 
TRP   CG   C  Y N 397 
TRP   CD1  C  Y N 398 
TRP   CD2  C  Y N 399 
TRP   NE1  N  Y N 400 
TRP   CE2  C  Y N 401 
TRP   CE3  C  Y N 402 
TRP   CZ2  C  Y N 403 
TRP   CZ3  C  Y N 404 
TRP   CH2  C  Y N 405 
TRP   OXT  O  N N 406 
TRP   H    H  N N 407 
TRP   H2   H  N N 408 
TRP   HA   H  N N 409 
TRP   HB2  H  N N 410 
TRP   HB3  H  N N 411 
TRP   HD1  H  N N 412 
TRP   HE1  H  N N 413 
TRP   HE3  H  N N 414 
TRP   HZ2  H  N N 415 
TRP   HZ3  H  N N 416 
TRP   HH2  H  N N 417 
TRP   HXT  H  N N 418 
TYR   N    N  N N 419 
TYR   CA   C  N S 420 
TYR   C    C  N N 421 
TYR   O    O  N N 422 
TYR   CB   C  N N 423 
TYR   CG   C  Y N 424 
TYR   CD1  C  Y N 425 
TYR   CD2  C  Y N 426 
TYR   CE1  C  Y N 427 
TYR   CE2  C  Y N 428 
TYR   CZ   C  Y N 429 
TYR   OH   O  N N 430 
TYR   OXT  O  N N 431 
TYR   H    H  N N 432 
TYR   H2   H  N N 433 
TYR   HA   H  N N 434 
TYR   HB2  H  N N 435 
TYR   HB3  H  N N 436 
TYR   HD1  H  N N 437 
TYR   HD2  H  N N 438 
TYR   HE1  H  N N 439 
TYR   HE2  H  N N 440 
TYR   HH   H  N N 441 
TYR   HXT  H  N N 442 
VAL   N    N  N N 443 
VAL   CA   C  N S 444 
VAL   C    C  N N 445 
VAL   O    O  N N 446 
VAL   CB   C  N N 447 
VAL   CG1  C  N N 448 
VAL   CG2  C  N N 449 
VAL   OXT  O  N N 450 
VAL   H    H  N N 451 
VAL   H2   H  N N 452 
VAL   HA   H  N N 453 
VAL   HB   H  N N 454 
VAL   HG11 H  N N 455 
VAL   HG12 H  N N 456 
VAL   HG13 H  N N 457 
VAL   HG21 H  N N 458 
VAL   HG22 H  N N 459 
VAL   HG23 H  N N 460 
VAL   HXT  H  N N 461 
# 
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 
A1BHC C15 C14  sing N N 1   
A1BHC O2  C17  sing N N 2   
A1BHC C14 C17  sing N N 3   
A1BHC C14 C16  sing N N 4   
A1BHC C14 N3   sing N N 5   
A1BHC N3  C13  sing N N 6   
A1BHC CL1 C10  sing N N 7   
A1BHC C11 C10  doub Y N 8   
A1BHC C11 C12  sing Y N 9   
A1BHC C13 O1   doub N N 10  
A1BHC C13 C12  sing N N 11  
A1BHC C10 C9   sing Y N 12  
A1BHC C12 C18  doub Y N 13  
A1BHC C9  C8   doub Y N 14  
A1BHC C18 C8   sing Y N 15  
A1BHC C8  N2   sing N N 16  
A1BHC N2  C7   sing N N 17  
A1BHC C7  C6   sing N N 18  
A1BHC C6  C19  doub Y N 19  
A1BHC C6  C5   sing Y N 20  
A1BHC C19 C20  sing Y N 21  
A1BHC C5  C4   doub Y N 22  
A1BHC C20 C21  doub Y N 23  
A1BHC C4  C21  sing Y N 24  
A1BHC C4  C3   sing N N 25  
A1BHC C21 O3   sing N N 26  
A1BHC C3  N1   sing N N 27  
A1BHC C2  N1   sing N N 28  
A1BHC N1  C1   sing N N 29  
A1BHC N3  H2   sing N N 30  
A1BHC C5  H3   sing N N 31  
A1BHC C7  H4   sing N N 32  
A1BHC C7  H5   sing N N 33  
A1BHC C15 H6   sing N N 34  
A1BHC C15 H7   sing N N 35  
A1BHC C15 H8   sing N N 36  
A1BHC C17 H9   sing N N 37  
A1BHC C17 H10  sing N N 38  
A1BHC C20 H11  sing N N 39  
A1BHC C1  H12  sing N N 40  
A1BHC C1  H13  sing N N 41  
A1BHC C1  H14  sing N N 42  
A1BHC C2  H15  sing N N 43  
A1BHC C2  H16  sing N N 44  
A1BHC C2  H17  sing N N 45  
A1BHC C3  H18  sing N N 46  
A1BHC C3  H19  sing N N 47  
A1BHC N2  H20  sing N N 48  
A1BHC C9  H21  sing N N 49  
A1BHC C11 H22  sing N N 50  
A1BHC C16 H23  sing N N 51  
A1BHC C16 H24  sing N N 52  
A1BHC C16 H25  sing N N 53  
A1BHC O2  H26  sing N N 54  
A1BHC C18 H27  sing N N 55  
A1BHC C19 H28  sing N N 56  
A1BHC O3  H29  sing N N 57  
ALA   N   CA   sing N N 58  
ALA   N   H    sing N N 59  
ALA   N   H2   sing N N 60  
ALA   CA  C    sing N N 61  
ALA   CA  CB   sing N N 62  
ALA   CA  HA   sing N N 63  
ALA   C   O    doub N N 64  
ALA   C   OXT  sing N N 65  
ALA   CB  HB1  sing N N 66  
ALA   CB  HB2  sing N N 67  
ALA   CB  HB3  sing N N 68  
ALA   OXT HXT  sing N N 69  
ARG   N   CA   sing N N 70  
ARG   N   H    sing N N 71  
ARG   N   H2   sing N N 72  
ARG   CA  C    sing N N 73  
ARG   CA  CB   sing N N 74  
ARG   CA  HA   sing N N 75  
ARG   C   O    doub N N 76  
ARG   C   OXT  sing N N 77  
ARG   CB  CG   sing N N 78  
ARG   CB  HB2  sing N N 79  
ARG   CB  HB3  sing N N 80  
ARG   CG  CD   sing N N 81  
ARG   CG  HG2  sing N N 82  
ARG   CG  HG3  sing N N 83  
ARG   CD  NE   sing N N 84  
ARG   CD  HD2  sing N N 85  
ARG   CD  HD3  sing N N 86  
ARG   NE  CZ   sing N N 87  
ARG   NE  HE   sing N N 88  
ARG   CZ  NH1  sing N N 89  
ARG   CZ  NH2  doub N N 90  
ARG   NH1 HH11 sing N N 91  
ARG   NH1 HH12 sing N N 92  
ARG   NH2 HH21 sing N N 93  
ARG   NH2 HH22 sing N N 94  
ARG   OXT HXT  sing N N 95  
ASN   N   CA   sing N N 96  
ASN   N   H    sing N N 97  
ASN   N   H2   sing N N 98  
ASN   CA  C    sing N N 99  
ASN   CA  CB   sing N N 100 
ASN   CA  HA   sing N N 101 
ASN   C   O    doub N N 102 
ASN   C   OXT  sing N N 103 
ASN   CB  CG   sing N N 104 
ASN   CB  HB2  sing N N 105 
ASN   CB  HB3  sing N N 106 
ASN   CG  OD1  doub N N 107 
ASN   CG  ND2  sing N N 108 
ASN   ND2 HD21 sing N N 109 
ASN   ND2 HD22 sing N N 110 
ASN   OXT HXT  sing N N 111 
ASP   N   CA   sing N N 112 
ASP   N   H    sing N N 113 
ASP   N   H2   sing N N 114 
ASP   CA  C    sing N N 115 
ASP   CA  CB   sing N N 116 
ASP   CA  HA   sing N N 117 
ASP   C   O    doub N N 118 
ASP   C   OXT  sing N N 119 
ASP   CB  CG   sing N N 120 
ASP   CB  HB2  sing N N 121 
ASP   CB  HB3  sing N N 122 
ASP   CG  OD1  doub N N 123 
ASP   CG  OD2  sing N N 124 
ASP   OD2 HD2  sing N N 125 
ASP   OXT HXT  sing N N 126 
CYS   N   CA   sing N N 127 
CYS   N   H    sing N N 128 
CYS   N   H2   sing N N 129 
CYS   CA  C    sing N N 130 
CYS   CA  CB   sing N N 131 
CYS   CA  HA   sing N N 132 
CYS   C   O    doub N N 133 
CYS   C   OXT  sing N N 134 
CYS   CB  SG   sing N N 135 
CYS   CB  HB2  sing N N 136 
CYS   CB  HB3  sing N N 137 
CYS   SG  HG   sing N N 138 
CYS   OXT HXT  sing N N 139 
DMS   S   O    doub N N 140 
DMS   S   C1   sing N N 141 
DMS   S   C2   sing N N 142 
DMS   C1  H11  sing N N 143 
DMS   C1  H12  sing N N 144 
DMS   C1  H13  sing N N 145 
DMS   C2  H21  sing N N 146 
DMS   C2  H22  sing N N 147 
DMS   C2  H23  sing N N 148 
GLN   N   CA   sing N N 149 
GLN   N   H    sing N N 150 
GLN   N   H2   sing N N 151 
GLN   CA  C    sing N N 152 
GLN   CA  CB   sing N N 153 
GLN   CA  HA   sing N N 154 
GLN   C   O    doub N N 155 
GLN   C   OXT  sing N N 156 
GLN   CB  CG   sing N N 157 
GLN   CB  HB2  sing N N 158 
GLN   CB  HB3  sing N N 159 
GLN   CG  CD   sing N N 160 
GLN   CG  HG2  sing N N 161 
GLN   CG  HG3  sing N N 162 
GLN   CD  OE1  doub N N 163 
GLN   CD  NE2  sing N N 164 
GLN   NE2 HE21 sing N N 165 
GLN   NE2 HE22 sing N N 166 
GLN   OXT HXT  sing N N 167 
GLU   N   CA   sing N N 168 
GLU   N   H    sing N N 169 
GLU   N   H2   sing N N 170 
GLU   CA  C    sing N N 171 
GLU   CA  CB   sing N N 172 
GLU   CA  HA   sing N N 173 
GLU   C   O    doub N N 174 
GLU   C   OXT  sing N N 175 
GLU   CB  CG   sing N N 176 
GLU   CB  HB2  sing N N 177 
GLU   CB  HB3  sing N N 178 
GLU   CG  CD   sing N N 179 
GLU   CG  HG2  sing N N 180 
GLU   CG  HG3  sing N N 181 
GLU   CD  OE1  doub N N 182 
GLU   CD  OE2  sing N N 183 
GLU   OE2 HE2  sing N N 184 
GLU   OXT HXT  sing N N 185 
GLY   N   CA   sing N N 186 
GLY   N   H    sing N N 187 
GLY   N   H2   sing N N 188 
GLY   CA  C    sing N N 189 
GLY   CA  HA2  sing N N 190 
GLY   CA  HA3  sing N N 191 
GLY   C   O    doub N N 192 
GLY   C   OXT  sing N N 193 
GLY   OXT HXT  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
SO4   S   O1   doub N N 356 
SO4   S   O2   doub N N 357 
SO4   S   O3   sing N N 358 
SO4   S   O4   sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
_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                    7HP2 
_atom_sites.fract_transf_matrix[1][1]   0.023742 
_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]   0.023742 
_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]   0.004638 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? 0.555   38.719 -7.451  1.00 63.43  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -0.782  38.067 -7.507  1.00 62.50  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -0.944  37.438 -8.907  1.00 59.23  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -0.959  38.138 -9.929  1.00 61.32  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -1.847  39.062 -7.048  1.00 65.58  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -3.269  38.541 -7.001  1.00 66.35  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -3.757  38.205 -5.878  1.00 69.70  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -3.914  38.550 -8.072  1.00 69.56  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -0.948  36.124 -8.955  1.00 54.98  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -0.808  35.377 -10.216 1.00 52.05  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -2.202  35.125 -10.791 1.00 49.76  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -3.192  35.054 -10.036 1.00 47.13  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -0.063  34.063 -9.985  1.00 52.47  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? 1.321   34.274 -9.425  1.00 53.32  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? 2.181   32.720 -9.096  1.00 53.90  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? 3.677   33.419 -8.413  1.00 56.89  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -2.294  35.037 -12.118 1.00 44.65  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -3.573  34.793 -12.818 1.00 44.35  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -3.349  33.784 -13.940 1.00 42.05  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -2.229  33.656 -14.435 1.00 40.68  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -4.146  36.118 -13.310 1.00 45.76  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -3.289  36.884 -14.285 1.00 47.50  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -2.285  37.720 -13.830 1.00 48.37  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -3.468  36.778 -15.660 1.00 48.24  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -1.503  38.462 -14.692 1.00 49.88  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -2.701  37.533 -16.532 1.00 48.31  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -1.711  38.372 -16.053 1.00 49.23  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -0.913  39.102 -16.900 1.00 53.32  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -4.383  33.046 -14.315 1.00 41.74  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -4.204  32.031 -15.398 1.00 41.20  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -4.910  32.498 -16.696 1.00 41.51  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -5.905  33.229 -16.632 1.00 41.69  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -4.637  30.633 -14.941 1.00 40.09  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -6.113  30.571 -14.557 1.00 41.23  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -3.748  30.134 -13.814 1.00 39.99  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -6.635  29.150 -14.473 1.00 39.97  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -4.404  32.072 -17.861 1.00 42.87  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -4.965  32.401 -19.216 1.00 44.04  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -4.909  31.149 -20.085 1.00 40.61  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -3.862  30.499 -20.111 1.00 39.13  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -4.158  33.433 -19.992 1.00 48.45  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -3.728  34.658 -19.228 1.00 51.42  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -3.060  35.682 -20.142 1.00 54.45  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -2.140  35.295 -20.897 1.00 54.99  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -3.407  36.875 -20.041 1.00 59.99  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -6.033  30.761 -20.667 1.00 40.62  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -6.134  29.486 -21.427 1.00 40.83  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -5.204  29.605 -22.658 1.00 41.20  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -5.203  30.693 -23.285 1.00 42.14  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -7.593  29.207 -21.777 1.00 41.46  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -7.867  27.765 -22.166 1.00 41.26  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -9.343  27.492 -22.395 1.00 42.88  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -9.517  26.070 -22.642 1.00 42.77  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -9.294  25.450 -23.812 1.00 43.80  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -8.925  26.138 -24.885 1.00 44.62  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -9.446  24.143 -23.896 1.00 42.80  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -4.424  28.565 -22.912 1.00 39.98  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -3.406  28.506 -23.988 1.00 41.36  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -3.748  27.473 -25.072 1.00 41.24  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -3.116  27.572 -26.179 1.00 40.99  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -2.060  28.243 -23.391 1.00 40.09  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -4.705  26.569 -24.868 1.00 40.34  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -4.955  25.495 -25.841 1.00 41.55  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -5.753  24.353 -25.283 1.00 42.42  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -6.001  24.306 -24.016 1.00 41.29  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -6.133  23.450 -26.184 1.00 43.12  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -6.781  22.158 -25.874 1.00 44.41  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -5.669  21.144 -25.684 1.00 45.63  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -4.570  21.320 -26.262 1.00 46.32  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -7.675  21.616 -26.984 1.00 46.81  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -8.983  22.348 -27.188 1.00 48.36  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -9.151  23.462 -26.626 1.00 45.53  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -9.800  21.815 -27.996 1.00 50.71  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -5.964  20.100 -24.950 1.00 45.15  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -4.992  19.021 -24.690 1.00 43.93  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -5.387  17.894 -25.612 1.00 45.40  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -6.364  17.148 -25.341 1.00 44.97  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -4.952  18.673 -23.218 1.00 42.49  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -4.424  19.904 -22.493 1.00 43.43  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -4.090  17.459 -22.987 1.00 43.20  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -4.374  19.723 -21.021 1.00 41.11  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -4.643  17.803 -26.715 0.25 45.63  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -4.669  17.788 -26.729 0.25 46.05  ? 60  THR   A N   1 
ATOM   84   N  N   C THR   A 1 17  ? -4.643  17.803 -26.715 0.25 45.63  ? 60  THR   A N   1 
ATOM   85   N  N   D THR   A 1 17  ? -4.669  17.788 -26.729 0.25 46.05  ? 60  THR   A N   1 
ATOM   86   C  CA  A THR   A 1 17  ? -4.894  16.883 -27.850 0.25 47.58  ? 60  THR   A CA  1 
ATOM   87   C  CA  B THR   A 1 17  ? -4.949  16.812 -27.812 0.25 48.12  ? 60  THR   A CA  1 
ATOM   88   C  CA  C THR   A 1 17  ? -4.894  16.883 -27.850 0.25 47.58  ? 60  THR   A CA  1 
ATOM   89   C  CA  D THR   A 1 17  ? -4.949  16.812 -27.812 0.25 48.12  ? 60  THR   A CA  1 
ATOM   90   C  C   A THR   A 1 17  ? -3.541  16.399 -28.377 0.25 48.12  ? 60  THR   A C   1 
ATOM   91   C  C   B THR   A 1 17  ? -3.628  16.431 -28.491 0.25 48.70  ? 60  THR   A C   1 
ATOM   92   C  C   C THR   A 1 17  ? -3.541  16.399 -28.377 0.25 48.12  ? 60  THR   A C   1 
ATOM   93   C  C   D THR   A 1 17  ? -3.628  16.431 -28.491 0.25 48.70  ? 60  THR   A C   1 
ATOM   94   O  O   A THR   A 1 17  ? -2.553  17.176 -28.312 0.25 48.31  ? 60  THR   A O   1 
ATOM   95   O  O   B THR   A 1 17  ? -2.768  17.325 -28.685 0.25 49.48  ? 60  THR   A O   1 
ATOM   96   O  O   C THR   A 1 17  ? -2.553  17.176 -28.312 0.25 48.31  ? 60  THR   A O   1 
ATOM   97   O  O   D THR   A 1 17  ? -2.768  17.325 -28.685 0.25 49.48  ? 60  THR   A O   1 
ATOM   98   C  CB  A THR   A 1 17  ? -5.737  17.571 -28.936 0.25 48.90  ? 60  THR   A CB  1 
ATOM   99   C  CB  B THR   A 1 17  ? -5.978  17.376 -28.806 0.25 49.75  ? 60  THR   A CB  1 
ATOM   100  C  CB  C THR   A 1 17  ? -5.737  17.571 -28.936 0.25 48.90  ? 60  THR   A CB  1 
ATOM   101  C  CB  D THR   A 1 17  ? -5.978  17.376 -28.806 0.25 49.75  ? 60  THR   A CB  1 
ATOM   102  O  OG1 A THR   A 1 17  ? -4.859  18.398 -29.696 0.25 48.92  ? 60  THR   A OG1 1 
ATOM   103  O  OG1 B THR   A 1 17  ? -7.301  17.258 -28.270 0.25 50.35  ? 60  THR   A OG1 1 
ATOM   104  O  OG1 C THR   A 1 17  ? -4.859  18.398 -29.696 0.25 48.92  ? 60  THR   A OG1 1 
ATOM   105  O  OG1 D THR   A 1 17  ? -7.301  17.258 -28.270 0.25 50.35  ? 60  THR   A OG1 1 
ATOM   106  C  CG2 A THR   A 1 17  ? -6.876  18.393 -28.368 0.25 48.92  ? 60  THR   A CG2 1 
ATOM   107  C  CG2 B THR   A 1 17  ? -5.919  16.687 -30.148 0.25 50.70  ? 60  THR   A CG2 1 
ATOM   108  C  CG2 C THR   A 1 17  ? -6.876  18.393 -28.368 0.25 48.92  ? 60  THR   A CG2 1 
ATOM   109  C  CG2 D THR   A 1 17  ? -5.919  16.687 -30.148 0.25 50.70  ? 60  THR   A CG2 1 
ATOM   110  N  N   . TRP   A 1 18  ? -3.487  15.152 -28.841 1.00 48.71  ? 61  TRP   A N   1 
ATOM   111  C  CA  . TRP   A 1 18  ? -2.329  14.650 -29.600 1.00 49.21  ? 61  TRP   A CA  1 
ATOM   112  C  C   . TRP   A 1 18  ? -2.525  15.196 -31.009 1.00 50.65  ? 61  TRP   A C   1 
ATOM   113  O  O   . TRP   A 1 18  ? -3.602  15.032 -31.518 1.00 50.96  ? 61  TRP   A O   1 
ATOM   114  C  CB  . TRP   A 1 18  ? -2.347  13.125 -29.594 1.00 49.15  ? 61  TRP   A CB  1 
ATOM   115  C  CG  . TRP   A 1 18  ? -1.174  12.550 -30.301 1.00 49.80  ? 61  TRP   A CG  1 
ATOM   116  C  CD1 . TRP   A 1 18  ? -1.013  12.460 -31.642 1.00 50.12  ? 61  TRP   A CD1 1 
ATOM   117  C  CD2 . TRP   A 1 18  ? 0.006   11.985 -29.729 1.00 47.77  ? 61  TRP   A CD2 1 
ATOM   118  N  NE1 . TRP   A 1 18  ? 0.173   11.854 -31.939 1.00 50.33  ? 61  TRP   A NE1 1 
ATOM   119  C  CE2 . TRP   A 1 18  ? 0.833   11.558 -30.791 1.00 48.34  ? 61  TRP   A CE2 1 
ATOM   120  C  CE3 . TRP   A 1 18  ? 0.444   11.776 -28.434 1.00 43.81  ? 61  TRP   A CE3 1 
ATOM   121  C  CZ2 . TRP   A 1 18  ? 2.056   10.918 -30.589 1.00 48.64  ? 61  TRP   A CZ2 1 
ATOM   122  C  CZ3 . TRP   A 1 18  ? 1.655   11.173 -28.238 1.00 45.15  ? 61  TRP   A CZ3 1 
ATOM   123  C  CH2 . TRP   A 1 18  ? 2.490   10.811 -29.286 1.00 47.69  ? 61  TRP   A CH2 1 
ATOM   124  N  N   A GLU   A 1 19  ? -1.528  15.903 -31.552 0.25 50.71  ? 62  GLU   A N   1 
ATOM   125  N  N   B GLU   A 1 19  ? -1.528  15.903 -31.552 0.25 50.71  ? 62  GLU   A N   1 
ATOM   126  N  N   C GLU   A 1 19  ? -1.494  15.828 -31.570 0.25 51.75  ? 62  GLU   A N   1 
ATOM   127  N  N   D GLU   A 1 19  ? -1.494  15.828 -31.570 0.25 51.75  ? 62  GLU   A N   1 
ATOM   128  C  CA  A GLU   A 1 19  ? -1.551  16.448 -32.940 0.25 53.32  ? 62  GLU   A CA  1 
ATOM   129  C  CA  B GLU   A 1 19  ? -1.551  16.448 -32.940 0.25 53.32  ? 62  GLU   A CA  1 
ATOM   130  C  CA  C GLU   A 1 19  ? -1.520  16.403 -32.941 0.25 55.07  ? 62  GLU   A CA  1 
ATOM   131  C  CA  D GLU   A 1 19  ? -1.520  16.403 -32.941 0.25 55.07  ? 62  GLU   A CA  1 
ATOM   132  C  C   A GLU   A 1 19  ? -0.808  15.463 -33.851 0.25 54.72  ? 62  GLU   A C   1 
ATOM   133  C  C   B GLU   A 1 19  ? -0.808  15.463 -33.851 0.25 54.72  ? 62  GLU   A C   1 
ATOM   134  C  C   C GLU   A 1 19  ? -0.683  15.510 -33.862 0.25 56.70  ? 62  GLU   A C   1 
ATOM   135  C  C   D GLU   A 1 19  ? -0.683  15.510 -33.862 0.25 56.70  ? 62  GLU   A C   1 
ATOM   136  O  O   A GLU   A 1 19  ? 0.382   15.168 -33.585 0.25 53.00  ? 62  GLU   A O   1 
ATOM   137  O  O   B GLU   A 1 19  ? 0.382   15.168 -33.585 0.25 53.00  ? 62  GLU   A O   1 
ATOM   138  O  O   C GLU   A 1 19  ? 0.545   15.401 -33.646 0.25 55.14  ? 62  GLU   A O   1 
ATOM   139  O  O   D GLU   A 1 19  ? 0.545   15.401 -33.646 0.25 55.14  ? 62  GLU   A O   1 
ATOM   140  C  CB  A GLU   A 1 19  ? -0.950  17.858 -32.997 0.25 53.28  ? 62  GLU   A CB  1 
ATOM   141  C  CB  B GLU   A 1 19  ? -0.950  17.858 -32.997 0.25 53.28  ? 62  GLU   A CB  1 
ATOM   142  C  CB  C GLU   A 1 19  ? -1.012  17.844 -32.907 0.25 55.35  ? 62  GLU   A CB  1 
ATOM   143  C  CB  D GLU   A 1 19  ? -1.012  17.844 -32.907 0.25 55.35  ? 62  GLU   A CB  1 
ATOM   144  C  CG  A GLU   A 1 19  ? -1.836  18.927 -32.372 0.25 52.95  ? 62  GLU   A CG  1 
ATOM   145  C  CG  B GLU   A 1 19  ? -1.836  18.927 -32.372 0.25 52.95  ? 62  GLU   A CG  1 
ATOM   146  C  CG  C GLU   A 1 19  ? -1.244  18.596 -34.196 0.25 57.41  ? 62  GLU   A CG  1 
ATOM   147  C  CG  D GLU   A 1 19  ? -1.244  18.596 -34.196 0.25 57.41  ? 62  GLU   A CG  1 
ATOM   148  C  CD  A GLU   A 1 19  ? -3.250  18.985 -32.924 0.25 54.48  ? 62  GLU   A CD  1 
ATOM   149  C  CD  B GLU   A 1 19  ? -3.250  18.985 -32.924 0.25 54.48  ? 62  GLU   A CD  1 
ATOM   150  C  CD  C GLU   A 1 19  ? 0.034   18.914 -34.944 0.25 58.46  ? 62  GLU   A CD  1 
ATOM   151  C  CD  D GLU   A 1 19  ? 0.034   18.914 -34.944 0.25 58.46  ? 62  GLU   A CD  1 
ATOM   152  O  OE1 A GLU   A 1 19  ? -3.434  19.526 -34.044 0.25 55.80  ? 62  GLU   A OE1 1 
ATOM   153  O  OE1 B GLU   A 1 19  ? -3.434  19.526 -34.044 0.25 55.80  ? 62  GLU   A OE1 1 
ATOM   154  O  OE1 C GLU   A 1 19  ? 1.093   18.950 -34.290 0.25 57.26  ? 62  GLU   A OE1 1 
ATOM   155  O  OE1 D GLU   A 1 19  ? 1.093   18.950 -34.290 0.25 57.26  ? 62  GLU   A OE1 1 
ATOM   156  O  OE2 A GLU   A 1 19  ? -4.162  18.466 -32.240 0.25 54.07  ? 62  GLU   A OE2 1 
ATOM   157  O  OE2 B GLU   A 1 19  ? -4.162  18.466 -32.240 0.25 54.07  ? 62  GLU   A OE2 1 
ATOM   158  O  OE2 C GLU   A 1 19  ? -0.039  19.129 -36.159 0.25 59.03  ? 62  GLU   A OE2 1 
ATOM   159  O  OE2 D GLU   A 1 19  ? -0.039  19.129 -36.159 0.25 59.03  ? 62  GLU   A OE2 1 
ATOM   160  N  N   A LYS   A 1 20  ? -1.492  14.951 -34.880 0.25 57.70  ? 63  LYS   A N   1 
ATOM   161  N  N   B LYS   A 1 20  ? -1.492  14.951 -34.880 0.25 57.70  ? 63  LYS   A N   1 
ATOM   162  N  N   C LYS   A 1 20  ? -1.324  14.883 -34.852 0.25 60.08  ? 63  LYS   A N   1 
ATOM   163  N  N   D LYS   A 1 20  ? -1.324  14.883 -34.852 0.25 60.08  ? 63  LYS   A N   1 
ATOM   164  C  CA  A LYS   A 1 20  ? -0.882  14.034 -35.879 0.25 59.60  ? 63  LYS   A CA  1 
ATOM   165  C  CA  B LYS   A 1 20  ? -0.882  14.034 -35.879 0.25 59.60  ? 63  LYS   A CA  1 
ATOM   166  C  CA  C LYS   A 1 20  ? -0.631  13.998 -35.824 0.25 61.90  ? 63  LYS   A CA  1 
ATOM   167  C  CA  D LYS   A 1 20  ? -0.631  13.998 -35.824 0.25 61.90  ? 63  LYS   A CA  1 
ATOM   168  C  C   A LYS   A 1 20  ? 0.059   14.876 -36.737 0.25 60.77  ? 63  LYS   A C   1 
ATOM   169  C  C   B LYS   A 1 20  ? 0.059   14.876 -36.737 0.25 60.77  ? 63  LYS   A C   1 
ATOM   170  C  C   C LYS   A 1 20  ? 0.319   14.867 -36.644 0.25 63.08  ? 63  LYS   A C   1 
ATOM   171  C  C   D LYS   A 1 20  ? 0.319   14.867 -36.644 0.25 63.08  ? 63  LYS   A C   1 
ATOM   172  O  O   A LYS   A 1 20  ? -0.359  15.958 -37.162 0.25 61.52  ? 63  LYS   A O   1 
ATOM   173  O  O   B LYS   A 1 20  ? -0.359  15.958 -37.162 0.25 61.52  ? 63  LYS   A O   1 
ATOM   174  O  O   C LYS   A 1 20  ? -0.018  16.032 -36.892 0.25 62.56  ? 63  LYS   A O   1 
ATOM   175  O  O   D LYS   A 1 20  ? -0.018  16.032 -36.892 0.25 62.56  ? 63  LYS   A O   1 
ATOM   176  C  CB  A LYS   A 1 20  ? -1.969  13.341 -36.703 0.25 62.12  ? 63  LYS   A CB  1 
ATOM   177  C  CB  B LYS   A 1 20  ? -1.969  13.341 -36.703 0.25 62.12  ? 63  LYS   A CB  1 
ATOM   178  C  CB  C LYS   A 1 20  ? -1.640  13.278 -36.718 0.25 64.61  ? 63  LYS   A CB  1 
ATOM   179  C  CB  D LYS   A 1 20  ? -1.640  13.278 -36.718 0.25 64.61  ? 63  LYS   A CB  1 
ATOM   180  C  CG  A LYS   A 1 20  ? -2.943  12.515 -35.871 0.25 62.30  ? 63  LYS   A CG  1 
ATOM   181  C  CG  B LYS   A 1 20  ? -2.943  12.515 -35.871 0.25 62.30  ? 63  LYS   A CG  1 
ATOM   182  C  CG  C LYS   A 1 20  ? -2.509  12.257 -35.998 0.25 64.99  ? 63  LYS   A CG  1 
ATOM   183  C  CG  D LYS   A 1 20  ? -2.509  12.257 -35.998 0.25 64.99  ? 63  LYS   A CG  1 
ATOM   184  C  CD  A LYS   A 1 20  ? -4.033  11.844 -36.686 0.25 64.36  ? 63  LYS   A CD  1 
ATOM   185  C  CD  B LYS   A 1 20  ? -4.033  11.844 -36.686 0.25 64.36  ? 63  LYS   A CD  1 
ATOM   186  C  CD  C LYS   A 1 20  ? -3.530  11.604 -36.911 0.25 67.20  ? 63  LYS   A CD  1 
ATOM   187  C  CD  D LYS   A 1 20  ? -3.530  11.604 -36.911 0.25 67.20  ? 63  LYS   A CD  1 
ATOM   188  C  CE  A LYS   A 1 20  ? -4.974  11.038 -35.812 0.25 64.44  ? 63  LYS   A CE  1 
ATOM   189  C  CE  B LYS   A 1 20  ? -4.974  11.038 -35.812 0.25 64.44  ? 63  LYS   A CE  1 
ATOM   190  C  CE  C LYS   A 1 20  ? -4.371  10.565 -36.200 0.25 67.45  ? 63  LYS   A CE  1 
ATOM   191  C  CE  D LYS   A 1 20  ? -4.371  10.565 -36.200 0.25 67.45  ? 63  LYS   A CE  1 
ATOM   192  N  NZ  A LYS   A 1 20  ? -6.112  10.501 -36.592 0.25 66.50  ? 63  LYS   A NZ  1 
ATOM   193  N  NZ  B LYS   A 1 20  ? -6.112  10.501 -36.592 0.25 66.50  ? 63  LYS   A NZ  1 
ATOM   194  N  NZ  C LYS   A 1 20  ? -5.346  9.937  -37.120 0.25 69.50  ? 63  LYS   A NZ  1 
ATOM   195  N  NZ  D LYS   A 1 20  ? -5.346  9.937  -37.120 0.25 69.50  ? 63  LYS   A NZ  1 
ATOM   196  N  N   A ASP   A 1 21  ? 1.300   14.428 -36.917 0.25 62.23  ? 64  ASP   A N   1 
ATOM   197  N  N   B ASP   A 1 21  ? 1.300   14.428 -36.917 0.25 62.23  ? 64  ASP   A N   1 
ATOM   198  N  N   C ASP   A 1 21  ? 1.484   14.342 -37.011 0.25 65.19  ? 64  ASP   A N   1 
ATOM   199  N  N   D ASP   A 1 21  ? 1.484   14.342 -37.011 0.25 65.19  ? 64  ASP   A N   1 
ATOM   200  C  CA  A ASP   A 1 21  ? 2.356   15.219 -37.602 0.25 63.97  ? 64  ASP   A CA  1 
ATOM   201  C  CA  B ASP   A 1 21  ? 2.356   15.219 -37.602 0.25 63.97  ? 64  ASP   A CA  1 
ATOM   202  C  CA  C ASP   A 1 21  ? 2.482   15.126 -37.779 0.25 67.56  ? 64  ASP   A CA  1 
ATOM   203  C  CA  D ASP   A 1 21  ? 2.482   15.126 -37.779 0.25 67.56  ? 64  ASP   A CA  1 
ATOM   204  C  C   A ASP   A 1 21  ? 2.623   16.489 -36.785 0.25 62.45  ? 64  ASP   A C   1 
ATOM   205  C  C   B ASP   A 1 21  ? 2.623   16.489 -36.785 0.25 62.45  ? 64  ASP   A C   1 
ATOM   206  C  C   C ASP   A 1 21  ? 2.824   16.392 -36.979 0.25 65.51  ? 64  ASP   A C   1 
ATOM   207  C  C   D ASP   A 1 21  ? 2.824   16.392 -36.979 0.25 65.51  ? 64  ASP   A C   1 
ATOM   208  O  O   A ASP   A 1 21  ? 2.225   17.568 -37.223 0.25 62.04  ? 64  ASP   A O   1 
ATOM   209  O  O   B ASP   A 1 21  ? 2.225   17.568 -37.223 0.25 62.04  ? 64  ASP   A O   1 
ATOM   210  O  O   C ASP   A 1 21  ? 2.572   17.490 -37.480 0.25 66.44  ? 64  ASP   A O   1 
ATOM   211  O  O   D ASP   A 1 21  ? 2.572   17.490 -37.480 0.25 66.44  ? 64  ASP   A O   1 
ATOM   212  C  CB  A ASP   A 1 21  ? 1.958   15.540 -39.048 0.25 67.43  ? 64  ASP   A CB  1 
ATOM   213  C  CB  B ASP   A 1 21  ? 1.958   15.540 -39.048 0.25 67.43  ? 64  ASP   A CB  1 
ATOM   214  C  CB  C ASP   A 1 21  ? 1.949   15.473 -39.177 0.25 71.39  ? 64  ASP   A CB  1 
ATOM   215  C  CB  D ASP   A 1 21  ? 1.949   15.473 -39.177 0.25 71.39  ? 64  ASP   A CB  1 
ATOM   216  C  CG  A ASP   A 1 21  ? 2.285   14.441 -40.049 0.25 69.60  ? 64  ASP   A CG  1 
ATOM   217  C  CG  B ASP   A 1 21  ? 2.285   14.441 -40.049 0.25 69.60  ? 64  ASP   A CG  1 
ATOM   218  C  CG  C ASP   A 1 21  ? 0.974   14.459 -39.764 0.25 73.78  ? 64  ASP   A CG  1 
ATOM   219  C  CG  D ASP   A 1 21  ? 0.974   14.459 -39.764 0.25 73.78  ? 64  ASP   A CG  1 
ATOM   220  O  OD1 A ASP   A 1 21  ? 3.403   13.885 -39.970 0.25 69.49  ? 64  ASP   A OD1 1 
ATOM   221  O  OD1 B ASP   A 1 21  ? 3.403   13.885 -39.970 0.25 69.49  ? 64  ASP   A OD1 1 
ATOM   222  O  OD1 C ASP   A 1 21  ? 0.939   13.311 -39.223 0.25 74.10  ? 64  ASP   A OD1 1 
ATOM   223  O  OD1 D ASP   A 1 21  ? 0.939   13.311 -39.223 0.25 74.10  ? 64  ASP   A OD1 1 
ATOM   224  O  OD2 A ASP   A 1 21  ? 1.415   14.144 -40.892 0.25 71.25  ? 64  ASP   A OD2 1 
ATOM   225  O  OD2 B ASP   A 1 21  ? 1.415   14.144 -40.892 0.25 71.25  ? 64  ASP   A OD2 1 
ATOM   226  O  OD2 C ASP   A 1 21  ? 0.264   14.823 -40.769 0.25 76.18  ? 64  ASP   A OD2 1 
ATOM   227  O  OD2 D ASP   A 1 21  ? 0.264   14.823 -40.769 0.25 76.18  ? 64  ASP   A OD2 1 
ATOM   228  N  N   A ALA   A 1 22  ? 3.214   16.343 -35.592 0.25 61.33  ? 65  ALA   A N   1 
ATOM   229  N  N   B ALA   A 1 22  ? 3.214   16.343 -35.592 0.25 61.33  ? 65  ALA   A N   1 
ATOM   230  N  N   C ALA   A 1 22  ? 3.319   16.247 -35.743 0.25 64.39  ? 65  ALA   A N   1 
ATOM   231  N  N   D ALA   A 1 22  ? 3.319   16.247 -35.743 0.25 64.39  ? 65  ALA   A N   1 
ATOM   232  C  CA  A ALA   A 1 22  ? 3.864   17.442 -34.842 0.25 59.48  ? 65  ALA   A CA  1 
ATOM   233  C  CA  B ALA   A 1 22  ? 3.864   17.442 -34.842 0.25 59.48  ? 65  ALA   A CA  1 
ATOM   234  C  CA  C ALA   A 1 22  ? 3.890   17.361 -34.948 0.25 61.50  ? 65  ALA   A CA  1 
ATOM   235  C  CA  D ALA   A 1 22  ? 3.890   17.361 -34.948 0.25 61.50  ? 65  ALA   A CA  1 
ATOM   236  C  C   A ALA   A 1 22  ? 5.376   17.365 -35.101 0.25 59.10  ? 65  ALA   A C   1 
ATOM   237  C  C   B ALA   A 1 22  ? 5.376   17.365 -35.101 0.25 59.10  ? 65  ALA   A C   1 
ATOM   238  C  C   C ALA   A 1 22  ? 5.410   17.355 -35.156 0.25 60.30  ? 65  ALA   A C   1 
ATOM   239  C  C   D ALA   A 1 22  ? 5.410   17.355 -35.156 0.25 60.30  ? 65  ALA   A C   1 
ATOM   240  O  O   A ALA   A 1 22  ? 5.841   16.262 -35.528 0.25 59.62  ? 65  ALA   A O   1 
ATOM   241  O  O   B ALA   A 1 22  ? 5.841   16.262 -35.528 0.25 59.62  ? 65  ALA   A O   1 
ATOM   242  O  O   C ALA   A 1 22  ? 5.923   16.293 -35.617 0.25 61.06  ? 65  ALA   A O   1 
ATOM   243  O  O   D ALA   A 1 22  ? 5.923   16.293 -35.617 0.25 61.06  ? 65  ALA   A O   1 
ATOM   244  C  CB  A ALA   A 1 22  ? 3.537   17.321 -33.376 0.25 58.46  ? 65  ALA   A CB  1 
ATOM   245  C  CB  B ALA   A 1 22  ? 3.537   17.321 -33.376 0.25 58.46  ? 65  ALA   A CB  1 
ATOM   246  C  CB  C ALA   A 1 22  ? 3.515   17.209 -33.498 0.25 60.57  ? 65  ALA   A CB  1 
ATOM   247  C  CB  D ALA   A 1 22  ? 3.515   17.209 -33.498 0.25 60.57  ? 65  ALA   A CB  1 
ATOM   248  N  N   . GLU   A 1 23  ? 6.095   18.483 -34.875 1.00 59.56  ? 66  GLU   A N   1 
ATOM   249  C  CA  . GLU   A 1 23  ? 7.596   18.533 -34.919 1.00 59.42  ? 66  GLU   A CA  1 
ATOM   250  C  C   . GLU   A 1 23  ? 8.142   17.406 -34.036 1.00 57.48  ? 66  GLU   A C   1 
ATOM   251  O  O   . GLU   A 1 23  ? 7.597   17.207 -32.939 1.00 51.59  ? 66  GLU   A O   1 
ATOM   252  C  CB  . GLU   A 1 23  ? 8.155   19.845 -34.360 1.00 62.77  ? 66  GLU   A CB  1 
ATOM   253  C  CG  . GLU   A 1 23  ? 9.669   19.840 -34.163 1.00 65.10  ? 66  GLU   A CG  1 
ATOM   254  C  CD  . GLU   A 1 23  ? 10.312  21.208 -33.952 1.00 69.34  ? 66  GLU   A CD  1 
ATOM   255  O  OE1 . GLU   A 1 23  ? 9.899   22.194 -34.623 1.00 74.56  ? 66  GLU   A OE1 1 
ATOM   256  O  OE2 . GLU   A 1 23  ? 11.234  21.293 -33.117 1.00 72.18  ? 66  GLU   A OE2 1 
ATOM   257  N  N   . VAL   A 1 24  ? 9.103   16.618 -34.507 1.00 57.09  ? 67  VAL   A N   1 
ATOM   258  C  CA  . VAL   A 1 24  ? 9.652   15.474 -33.703 1.00 56.65  ? 67  VAL   A CA  1 
ATOM   259  C  C   . VAL   A 1 24  ? 11.133  15.751 -33.425 1.00 55.65  ? 67  VAL   A C   1 
ATOM   260  O  O   . VAL   A 1 24  ? 11.837  16.178 -34.311 1.00 59.58  ? 67  VAL   A O   1 
ATOM   261  C  CB  . VAL   A 1 24  ? 9.375   14.139 -34.422 1.00 57.85  ? 67  VAL   A CB  1 
ATOM   262  C  CG1 . VAL   A 1 24  ? 9.623   12.957 -33.517 1.00 56.34  ? 67  VAL   A CG1 1 
ATOM   263  C  CG2 . VAL   A 1 24  ? 7.953   14.098 -34.963 1.00 57.76  ? 67  VAL   A CG2 1 
ATOM   264  N  N   . THR   A 1 25  ? 11.583  15.685 -32.187 1.00 53.14  ? 68  THR   A N   1 
ATOM   265  C  CA  . THR   A 1 25  ? 12.971  16.113 -31.887 1.00 52.61  ? 68  THR   A CA  1 
ATOM   266  C  C   . THR   A 1 25  ? 13.312  15.665 -30.475 1.00 50.49  ? 68  THR   A C   1 
ATOM   267  O  O   . THR   A 1 25  ? 12.482  14.946 -29.863 1.00 47.97  ? 68  THR   A O   1 
ATOM   268  C  CB  . THR   A 1 25  ? 13.165  17.616 -32.137 1.00 52.42  ? 68  THR   A CB  1 
ATOM   269  O  OG1 . THR   A 1 25  ? 14.578  17.809 -32.310 1.00 53.81  ? 68  THR   A OG1 1 
ATOM   270  C  CG2 . THR   A 1 25  ? 12.597  18.490 -31.042 1.00 52.98  ? 68  THR   A CG2 1 
ATOM   271  N  N   . GLY   A 1 26  ? 14.539  15.959 -30.063 1.00 51.14  ? 69  GLY   A N   1 
ATOM   272  C  CA  . GLY   A 1 26  ? 15.055  15.531 -28.764 1.00 51.30  ? 69  GLY   A CA  1 
ATOM   273  C  C   . GLY   A 1 26  ? 15.523  14.078 -28.766 1.00 52.12  ? 69  GLY   A C   1 
ATOM   274  O  O   . GLY   A 1 26  ? 14.974  13.195 -29.509 1.00 50.86  ? 69  GLY   A O   1 
ATOM   275  N  N   . ASN   A 1 27  ? 16.477  13.837 -27.840 1.00 53.05  ? 70  ASN   A N   1 
ATOM   276  C  CA  . ASN   A 1 27  ? 17.119  12.529 -27.574 1.00 52.96  ? 70  ASN   A CA  1 
ATOM   277  C  C   . ASN   A 1 27  ? 16.465  11.880 -26.349 1.00 52.27  ? 70  ASN   A C   1 
ATOM   278  O  O   . ASN   A 1 27  ? 15.430  12.416 -25.833 1.00 49.14  ? 70  ASN   A O   1 
ATOM   279  C  CB  . ASN   A 1 27  ? 18.634  12.728 -27.580 1.00 55.27  ? 70  ASN   A CB  1 
ATOM   280  C  CG  . ASN   A 1 27  ? 19.182  13.352 -26.315 1.00 55.02  ? 70  ASN   A CG  1 
ATOM   281  O  OD1 . ASN   A 1 27  ? 18.789  14.449 -25.923 1.00 56.10  ? 70  ASN   A OD1 1 
ATOM   282  N  ND2 . ASN   A 1 27  ? 20.160  12.686 -25.724 1.00 56.53  ? 70  ASN   A ND2 1 
ATOM   283  N  N   . SER   A 1 28  ? 16.972  10.722 -25.900 1.00 52.85  ? 71  SER   A N   1 
ATOM   284  C  CA  . SER   A 1 28  ? 16.349  9.900  -24.840 1.00 51.27  ? 71  SER   A CA  1 
ATOM   285  C  C   . SER   A 1 28  ? 17.449  9.398  -23.922 1.00 50.60  ? 71  SER   A C   1 
ATOM   286  O  O   . SER   A 1 28  ? 17.674  8.164  -23.856 1.00 51.28  ? 71  SER   A O   1 
ATOM   287  C  CB  . SER   A 1 28  ? 15.609  8.690  -25.326 1.00 54.37  ? 71  SER   A CB  1 
ATOM   288  O  OG  . SER   A 1 28  ? 14.866  8.888  -26.475 1.00 58.55  ? 71  SER   A OG  1 
ATOM   289  N  N   . PRO   A 1 29  ? 18.124  10.291 -23.155 1.00 51.60  ? 72  PRO   A N   1 
ATOM   290  C  CA  . PRO   A 1 29  ? 19.296  9.883  -22.382 1.00 50.50  ? 72  PRO   A CA  1 
ATOM   291  C  C   . PRO   A 1 29  ? 18.830  9.050  -21.170 1.00 51.13  ? 72  PRO   A C   1 
ATOM   292  O  O   . PRO   A 1 29  ? 17.732  9.311  -20.672 1.00 48.54  ? 72  PRO   A O   1 
ATOM   293  C  CB  . PRO   A 1 29  ? 19.914  11.247 -22.030 1.00 50.82  ? 72  PRO   A CB  1 
ATOM   294  C  CG  . PRO   A 1 29  ? 18.692  12.130 -21.779 1.00 49.03  ? 72  PRO   A CG  1 
ATOM   295  C  CD  . PRO   A 1 29  ? 17.711  11.674 -22.858 1.00 50.94  ? 72  PRO   A CD  1 
ATOM   296  N  N   . ARG   A 1 30  ? 19.638  8.064  -20.765 1.00 53.23  ? 73  ARG   A N   1 
ATOM   297  C  CA  . ARG   A 1 30  ? 19.462  7.318  -19.485 1.00 55.13  ? 73  ARG   A CA  1 
ATOM   298  C  C   . ARG   A 1 30  ? 20.439  7.889  -18.462 1.00 53.33  ? 73  ARG   A C   1 
ATOM   299  O  O   . ARG   A 1 30  ? 21.640  7.691  -18.622 1.00 55.30  ? 73  ARG   A O   1 
ATOM   300  C  CB  . ARG   A 1 30  ? 19.675  5.821  -19.694 1.00 59.97  ? 73  ARG   A CB  1 
ATOM   301  C  CG  . ARG   A 1 30  ? 18.628  5.200  -20.611 1.00 60.63  ? 73  ARG   A CG  1 
ATOM   302  C  CD  . ARG   A 1 30  ? 18.836  3.707  -20.758 1.00 67.04  ? 73  ARG   A CD  1 
ATOM   303  N  NE  . ARG   A 1 30  ? 18.076  3.183  -21.871 1.00 74.03  ? 73  ARG   A NE  1 
ATOM   304  C  CZ  . ARG   A 1 30  ? 16.809  2.757  -21.856 1.00 74.23  ? 73  ARG   A CZ  1 
ATOM   305  N  NH1 . ARG   A 1 30  ? 16.121  2.742  -20.726 1.00 72.39  ? 73  ARG   A NH1 1 
ATOM   306  N  NH2 . ARG   A 1 30  ? 16.253  2.336  -22.998 1.00 70.06  ? 73  ARG   A NH2 1 
ATOM   307  N  N   . LEU   A 1 31  ? 19.931  8.589  -17.455 1.00 50.99  ? 74  LEU   A N   1 
ATOM   308  C  CA  . LEU   A 1 31  ? 20.785  9.354  -16.522 1.00 50.81  ? 74  LEU   A CA  1 
ATOM   309  C  C   . LEU   A 1 31  ? 20.571  8.804  -15.107 1.00 49.40  ? 74  LEU   A C   1 
ATOM   310  O  O   . LEU   A 1 31  ? 19.414  8.572  -14.714 1.00 47.62  ? 74  LEU   A O   1 
ATOM   311  C  CB  . LEU   A 1 31  ? 20.384  10.832 -16.566 1.00 49.76  ? 74  LEU   A CB  1 
ATOM   312  C  CG  . LEU   A 1 31  ? 20.503  11.538 -17.923 1.00 50.80  ? 74  LEU   A CG  1 
ATOM   313  C  CD1 . LEU   A 1 31  ? 19.581  12.736 -17.931 1.00 49.91  ? 74  LEU   A CD1 1 
ATOM   314  C  CD2 . LEU   A 1 31  ? 21.938  11.974 -18.176 1.00 52.01  ? 74  LEU   A CD2 1 
ATOM   315  N  N   A ASP   A 1 32  ? 21.665  8.603  -14.368 0.13 50.83  ? 75  ASP   A N   1 
ATOM   316  N  N   B ASP   A 1 32  ? 21.665  8.603  -14.369 0.14 50.84  ? 75  ASP   A N   1 
ATOM   317  N  N   C ASP   A 1 32  ? 21.661  8.569  -14.376 0.36 51.67  ? 75  ASP   A N   1 
ATOM   318  N  N   D ASP   A 1 32  ? 21.661  8.568  -14.376 0.37 51.67  ? 75  ASP   A N   1 
ATOM   319  C  CA  A ASP   A 1 32  ? 21.638  8.307  -12.910 0.13 50.87  ? 75  ASP   A CA  1 
ATOM   320  C  CA  B ASP   A 1 32  ? 21.638  8.307  -12.910 0.14 50.87  ? 75  ASP   A CA  1 
ATOM   321  C  CA  C ASP   A 1 32  ? 21.599  8.291  -12.915 0.36 51.90  ? 75  ASP   A CA  1 
ATOM   322  C  CA  D ASP   A 1 32  ? 21.598  8.291  -12.915 0.37 51.90  ? 75  ASP   A CA  1 
ATOM   323  C  C   A ASP   A 1 32  ? 21.445  9.635  -12.174 0.13 49.75  ? 75  ASP   A C   1 
ATOM   324  C  C   B ASP   A 1 32  ? 21.445  9.635  -12.175 0.14 49.75  ? 75  ASP   A C   1 
ATOM   325  C  C   C ASP   A 1 32  ? 21.415  9.633  -12.206 0.36 50.00  ? 75  ASP   A C   1 
ATOM   326  C  C   D ASP   A 1 32  ? 21.415  9.633  -12.206 0.37 50.00  ? 75  ASP   A C   1 
ATOM   327  O  O   A ASP   A 1 32  ? 22.286  10.535 -12.369 0.13 50.32  ? 75  ASP   A O   1 
ATOM   328  O  O   B ASP   A 1 32  ? 22.286  10.535 -12.370 0.14 50.31  ? 75  ASP   A O   1 
ATOM   329  O  O   C ASP   A 1 32  ? 22.241  10.538 -12.440 0.36 50.44  ? 75  ASP   A O   1 
ATOM   330  O  O   D ASP   A 1 32  ? 22.241  10.538 -12.440 0.37 50.44  ? 75  ASP   A O   1 
ATOM   331  C  CB  A ASP   A 1 32  ? 22.914  7.593  -12.452 0.13 53.18  ? 75  ASP   A CB  1 
ATOM   332  C  CB  B ASP   A 1 32  ? 22.914  7.592  -12.453 0.14 53.18  ? 75  ASP   A CB  1 
ATOM   333  C  CB  C ASP   A 1 32  ? 22.838  7.546  -12.403 0.36 55.19  ? 75  ASP   A CB  1 
ATOM   334  C  CB  D ASP   A 1 32  ? 22.838  7.546  -12.403 0.37 55.20  ? 75  ASP   A CB  1 
ATOM   335  C  CG  A ASP   A 1 32  ? 23.231  6.333  -13.249 0.13 54.56  ? 75  ASP   A CG  1 
ATOM   336  C  CG  B ASP   A 1 32  ? 23.231  6.333  -13.251 0.14 54.57  ? 75  ASP   A CG  1 
ATOM   337  C  CG  C ASP   A 1 32  ? 22.991  6.124  -12.948 0.36 57.53  ? 75  ASP   A CG  1 
ATOM   338  C  CG  D ASP   A 1 32  ? 22.990  6.125  -12.948 0.37 57.54  ? 75  ASP   A CG  1 
ATOM   339  O  OD1 A ASP   A 1 32  ? 22.324  5.429  -13.331 0.13 53.80  ? 75  ASP   A OD1 1 
ATOM   340  O  OD1 B ASP   A 1 32  ? 22.325  5.428  -13.334 0.14 53.81  ? 75  ASP   A OD1 1 
ATOM   341  O  OD1 C ASP   A 1 32  ? 21.959  5.542  -13.487 0.36 56.48  ? 75  ASP   A OD1 1 
ATOM   342  O  OD1 D ASP   A 1 32  ? 21.959  5.541  -13.487 0.37 56.48  ? 75  ASP   A OD1 1 
ATOM   343  O  OD2 A ASP   A 1 32  ? 24.377  6.272  -13.802 0.13 56.46  ? 75  ASP   A OD2 1 
ATOM   344  O  OD2 B ASP   A 1 32  ? 24.377  6.273  -13.805 0.14 56.47  ? 75  ASP   A OD2 1 
ATOM   345  O  OD2 C ASP   A 1 32  ? 24.147  5.609  -12.836 0.36 61.50  ? 75  ASP   A OD2 1 
ATOM   346  O  OD2 D ASP   A 1 32  ? 24.147  5.609  -12.836 0.37 61.51  ? 75  ASP   A OD2 1 
ATOM   347  N  N   A VAL   A 1 33  ? 20.380  9.761  -11.377 0.13 48.53  ? 76  VAL   A N   1 
ATOM   348  N  N   B VAL   A 1 33  ? 20.380  9.760  -11.377 0.14 48.53  ? 76  VAL   A N   1 
ATOM   349  N  N   C VAL   A 1 33  ? 20.375  9.757  -11.376 0.36 48.76  ? 76  VAL   A N   1 
ATOM   350  N  N   D VAL   A 1 33  ? 20.375  9.757  -11.376 0.37 48.76  ? 76  VAL   A N   1 
ATOM   351  C  CA  A VAL   A 1 33  ? 20.035  11.027 -10.663 0.13 47.39  ? 76  VAL   A CA  1 
ATOM   352  C  CA  B VAL   A 1 33  ? 20.035  11.027 -10.662 0.14 47.39  ? 76  VAL   A CA  1 
ATOM   353  C  CA  C VAL   A 1 33  ? 20.037  11.026 -10.663 0.36 47.41  ? 76  VAL   A CA  1 
ATOM   354  C  CA  D VAL   A 1 33  ? 20.037  11.026 -10.663 0.37 47.41  ? 76  VAL   A CA  1 
ATOM   355  C  C   A VAL   A 1 33  ? 19.641  10.721 -9.212  0.13 47.36  ? 76  VAL   A C   1 
ATOM   356  C  C   B VAL   A 1 33  ? 19.641  10.721 -9.212  0.14 47.36  ? 76  VAL   A C   1 
ATOM   357  C  C   C VAL   A 1 33  ? 19.641  10.722 -9.211  0.36 47.30  ? 76  VAL   A C   1 
ATOM   358  C  C   D VAL   A 1 33  ? 19.641  10.722 -9.211  0.37 47.30  ? 76  VAL   A C   1 
ATOM   359  O  O   A VAL   A 1 33  ? 19.239  9.568  -8.914  0.13 47.50  ? 76  VAL   A O   1 
ATOM   360  O  O   B VAL   A 1 33  ? 19.237  9.568  -8.914  0.14 47.50  ? 76  VAL   A O   1 
ATOM   361  O  O   C VAL   A 1 33  ? 19.233  9.565  -8.901  0.36 47.52  ? 76  VAL   A O   1 
ATOM   362  O  O   D VAL   A 1 33  ? 19.233  9.565  -8.901  0.37 47.52  ? 76  VAL   A O   1 
ATOM   363  C  CB  A VAL   A 1 33  ? 18.919  11.807 -11.389 0.13 45.43  ? 76  VAL   A CB  1 
ATOM   364  C  CB  B VAL   A 1 33  ? 18.919  11.807 -11.389 0.14 45.42  ? 76  VAL   A CB  1 
ATOM   365  C  CB  C VAL   A 1 33  ? 18.922  11.809 -11.391 0.36 45.33  ? 76  VAL   A CB  1 
ATOM   366  C  CB  D VAL   A 1 33  ? 18.922  11.809 -11.391 0.37 45.33  ? 76  VAL   A CB  1 
ATOM   367  C  CG1 A VAL   A 1 33  ? 19.326  12.214 -12.802 0.13 45.36  ? 76  VAL   A CG1 1 
ATOM   368  C  CG1 B VAL   A 1 33  ? 19.326  12.214 -12.802 0.14 45.36  ? 76  VAL   A CG1 1 
ATOM   369  C  CG1 C VAL   A 1 33  ? 19.326  12.218 -12.807 0.36 45.05  ? 76  VAL   A CG1 1 
ATOM   370  C  CG1 D VAL   A 1 33  ? 19.326  12.218 -12.807 0.37 45.05  ? 76  VAL   A CG1 1 
ATOM   371  C  CG2 A VAL   A 1 33  ? 17.609  11.034 -11.408 0.13 44.27  ? 76  VAL   A CG2 1 
ATOM   372  C  CG2 B VAL   A 1 33  ? 17.609  11.034 -11.408 0.14 44.27  ? 76  VAL   A CG2 1 
ATOM   373  C  CG2 C VAL   A 1 33  ? 17.612  11.033 -11.405 0.36 44.19  ? 76  VAL   A CG2 1 
ATOM   374  C  CG2 D VAL   A 1 33  ? 17.612  11.033 -11.405 0.37 44.18  ? 76  VAL   A CG2 1 
ATOM   375  N  N   A ALA   A 1 34  ? 19.759  11.733 -8.349  0.13 47.56  ? 77  ALA   A N   1 
ATOM   376  N  N   B ALA   A 1 34  ? 19.759  11.733 -8.350  0.14 47.57  ? 77  ALA   A N   1 
ATOM   377  N  N   C ALA   A 1 34  ? 19.759  11.736 -8.355  0.36 47.53  ? 77  ALA   A N   1 
ATOM   378  N  N   D ALA   A 1 34  ? 19.759  11.736 -8.355  0.37 47.53  ? 77  ALA   A N   1 
ATOM   379  C  CA  A ALA   A 1 34  ? 19.260  11.727 -6.955  0.13 47.40  ? 77  ALA   A CA  1 
ATOM   380  C  CA  B ALA   A 1 34  ? 19.260  11.727 -6.955  0.14 47.40  ? 77  ALA   A CA  1 
ATOM   381  C  CA  C ALA   A 1 34  ? 19.259  11.731 -6.959  0.36 47.23  ? 77  ALA   A CA  1 
ATOM   382  C  CA  D ALA   A 1 34  ? 19.259  11.731 -6.959  0.37 47.23  ? 77  ALA   A CA  1 
ATOM   383  C  C   A ALA   A 1 34  ? 18.184  12.807 -6.807  0.13 46.15  ? 77  ALA   A C   1 
ATOM   384  C  C   B ALA   A 1 34  ? 18.184  12.807 -6.807  0.14 46.15  ? 77  ALA   A C   1 
ATOM   385  C  C   C ALA   A 1 34  ? 18.187  12.812 -6.815  0.36 46.00  ? 77  ALA   A C   1 
ATOM   386  C  C   D ALA   A 1 34  ? 18.187  12.812 -6.815  0.37 46.00  ? 77  ALA   A C   1 
ATOM   387  O  O   A ALA   A 1 34  ? 18.231  13.808 -7.552  0.13 45.24  ? 77  ALA   A O   1 
ATOM   388  O  O   B ALA   A 1 34  ? 18.231  13.808 -7.553  0.14 45.24  ? 77  ALA   A O   1 
ATOM   389  O  O   C ALA   A 1 34  ? 18.234  13.814 -7.562  0.36 44.92  ? 77  ALA   A O   1 
ATOM   390  O  O   D ALA   A 1 34  ? 18.234  13.814 -7.562  0.37 44.91  ? 77  ALA   A O   1 
ATOM   391  C  CB  A ALA   A 1 34  ? 20.400  11.926 -5.985  0.13 49.39  ? 77  ALA   A CB  1 
ATOM   392  C  CB  B ALA   A 1 34  ? 20.400  11.926 -5.985  0.14 49.39  ? 77  ALA   A CB  1 
ATOM   393  C  CB  C ALA   A 1 34  ? 20.399  11.922 -5.983  0.36 49.50  ? 77  ALA   A CB  1 
ATOM   394  C  CB  D ALA   A 1 34  ? 20.399  11.922 -5.983  0.37 49.50  ? 77  ALA   A CB  1 
ATOM   395  N  N   A LEU   A 1 35  ? 17.236  12.585 -5.890  0.13 45.65  ? 78  LEU   A N   1 
ATOM   396  N  N   B LEU   A 1 35  ? 17.235  12.585 -5.890  0.14 45.65  ? 78  LEU   A N   1 
ATOM   397  N  N   C LEU   A 1 35  ? 17.226  12.598 -5.916  0.36 44.99  ? 78  LEU   A N   1 
ATOM   398  N  N   D LEU   A 1 35  ? 17.226  12.598 -5.916  0.37 44.99  ? 78  LEU   A N   1 
ATOM   399  C  CA  A LEU   A 1 35  ? 16.128  13.521 -5.561  0.13 44.93  ? 78  LEU   A CA  1 
ATOM   400  C  CA  B LEU   A 1 35  ? 16.128  13.521 -5.561  0.14 44.93  ? 78  LEU   A CA  1 
ATOM   401  C  CA  C LEU   A 1 35  ? 16.154  13.575 -5.599  0.36 44.27  ? 78  LEU   A CA  1 
ATOM   402  C  CA  D LEU   A 1 35  ? 16.154  13.575 -5.599  0.37 44.27  ? 78  LEU   A CA  1 
ATOM   403  C  C   A LEU   A 1 35  ? 16.200  13.851 -4.067  0.13 45.63  ? 78  LEU   A C   1 
ATOM   404  C  C   B LEU   A 1 35  ? 16.200  13.852 -4.068  0.14 45.63  ? 78  LEU   A C   1 
ATOM   405  C  C   C LEU   A 1 35  ? 16.289  13.929 -4.120  0.36 44.73  ? 78  LEU   A C   1 
ATOM   406  C  C   D LEU   A 1 35  ? 16.289  13.929 -4.120  0.37 44.73  ? 78  LEU   A C   1 
ATOM   407  O  O   A LEU   A 1 35  ? 15.920  12.945 -3.249  0.13 46.48  ? 78  LEU   A O   1 
ATOM   408  O  O   B LEU   A 1 35  ? 15.920  12.945 -3.249  0.14 46.49  ? 78  LEU   A O   1 
ATOM   409  O  O   C LEU   A 1 35  ? 16.248  12.983 -3.295  0.36 46.10  ? 78  LEU   A O   1 
ATOM   410  O  O   D LEU   A 1 35  ? 16.249  12.983 -3.295  0.37 46.10  ? 78  LEU   A O   1 
ATOM   411  C  CB  A LEU   A 1 35  ? 14.794  12.864 -5.931  0.13 44.08  ? 78  LEU   A CB  1 
ATOM   412  C  CB  B LEU   A 1 35  ? 14.794  12.864 -5.932  0.14 44.09  ? 78  LEU   A CB  1 
ATOM   413  C  CB  C LEU   A 1 35  ? 14.798  12.939 -5.922  0.36 43.69  ? 78  LEU   A CB  1 
ATOM   414  C  CB  D LEU   A 1 35  ? 14.798  12.940 -5.923  0.37 43.69  ? 78  LEU   A CB  1 
ATOM   415  C  CG  A LEU   A 1 35  ? 13.538  13.675 -5.608  0.13 43.58  ? 78  LEU   A CG  1 
ATOM   416  C  CG  B LEU   A 1 35  ? 13.538  13.676 -5.609  0.14 43.59  ? 78  LEU   A CG  1 
ATOM   417  C  CG  C LEU   A 1 35  ? 13.566  13.799 -5.634  0.36 43.70  ? 78  LEU   A CG  1 
ATOM   418  C  CG  D LEU   A 1 35  ? 13.566  13.799 -5.634  0.37 43.71  ? 78  LEU   A CG  1 
ATOM   419  C  CD1 A LEU   A 1 35  ? 13.495  14.963 -6.414  0.13 42.96  ? 78  LEU   A CD1 1 
ATOM   420  C  CD1 B LEU   A 1 35  ? 13.494  14.963 -6.415  0.14 42.97  ? 78  LEU   A CD1 1 
ATOM   421  C  CD1 C LEU   A 1 35  ? 13.550  15.049 -6.490  0.36 43.01  ? 78  LEU   A CD1 1 
ATOM   422  C  CD1 D LEU   A 1 35  ? 13.550  15.049 -6.490  0.37 43.01  ? 78  LEU   A CD1 1 
ATOM   423  C  CD2 A LEU   A 1 35  ? 12.279  12.859 -5.859  0.13 43.07  ? 78  LEU   A CD2 1 
ATOM   424  C  CD2 B LEU   A 1 35  ? 12.279  12.860 -5.859  0.14 43.09  ? 78  LEU   A CD2 1 
ATOM   425  C  CD2 C LEU   A 1 35  ? 12.277  13.017 -5.851  0.36 43.50  ? 78  LEU   A CD2 1 
ATOM   426  C  CD2 D LEU   A 1 35  ? 12.277  13.017 -5.851  0.37 43.50  ? 78  LEU   A CD2 1 
ATOM   427  N  N   A ASP   A 1 36  ? 16.584  15.088 -3.729  0.13 45.79  ? 79  ASP   A N   1 
ATOM   428  N  N   B ASP   A 1 36  ? 16.584  15.088 -3.729  0.14 45.78  ? 79  ASP   A N   1 
ATOM   429  N  N   C ASP   A 1 36  ? 16.529  15.204 -3.790  0.36 44.40  ? 79  ASP   A N   1 
ATOM   430  N  N   D ASP   A 1 36  ? 16.529  15.204 -3.791  0.37 44.40  ? 79  ASP   A N   1 
ATOM   431  C  CA  A ASP   A 1 36  ? 16.755  15.550 -2.321  0.13 46.66  ? 79  ASP   A CA  1 
ATOM   432  C  CA  B ASP   A 1 36  ? 16.754  15.550 -2.321  0.14 46.66  ? 79  ASP   A CA  1 
ATOM   433  C  CA  C ASP   A 1 36  ? 16.715  15.639 -2.372  0.36 45.37  ? 79  ASP   A CA  1 
ATOM   434  C  CA  D ASP   A 1 36  ? 16.715  15.639 -2.373  0.37 45.37  ? 79  ASP   A CA  1 
ATOM   435  C  C   A ASP   A 1 36  ? 15.382  15.923 -1.744  0.13 45.67  ? 79  ASP   A C   1 
ATOM   436  C  C   B ASP   A 1 36  ? 15.382  15.923 -1.744  0.14 45.67  ? 79  ASP   A C   1 
ATOM   437  C  C   C ASP   A 1 36  ? 15.351  16.004 -1.778  0.36 44.12  ? 79  ASP   A C   1 
ATOM   438  C  C   D ASP   A 1 36  ? 15.351  16.004 -1.778  0.37 44.12  ? 79  ASP   A C   1 
ATOM   439  O  O   A ASP   A 1 36  ? 14.372  15.820 -2.472  0.13 43.83  ? 79  ASP   A O   1 
ATOM   440  O  O   B ASP   A 1 36  ? 14.372  15.820 -2.472  0.14 43.82  ? 79  ASP   A O   1 
ATOM   441  O  O   C ASP   A 1 36  ? 14.331  15.977 -2.499  0.36 41.26  ? 79  ASP   A O   1 
ATOM   442  O  O   D ASP   A 1 36  ? 14.331  15.977 -2.499  0.37 41.25  ? 79  ASP   A O   1 
ATOM   443  C  CB  A ASP   A 1 36  ? 17.766  16.700 -2.228  0.13 47.78  ? 79  ASP   A CB  1 
ATOM   444  C  CB  B ASP   A 1 36  ? 17.766  16.699 -2.227  0.14 47.78  ? 79  ASP   A CB  1 
ATOM   445  C  CB  C ASP   A 1 36  ? 17.739  16.775 -2.252  0.36 46.77  ? 79  ASP   A CB  1 
ATOM   446  C  CB  D ASP   A 1 36  ? 17.739  16.775 -2.252  0.37 46.77  ? 79  ASP   A CB  1 
ATOM   447  C  CG  A ASP   A 1 36  ? 17.273  18.056 -2.799  0.13 47.04  ? 79  ASP   A CG  1 
ATOM   448  C  CG  B ASP   A 1 36  ? 17.274  18.055 -2.801  0.14 47.04  ? 79  ASP   A CG  1 
ATOM   449  C  CG  C ASP   A 1 36  ? 17.279  18.193 -2.824  0.36 46.69  ? 79  ASP   A CG  1 
ATOM   450  C  CG  D ASP   A 1 36  ? 17.279  18.193 -2.824  0.37 46.69  ? 79  ASP   A CG  1 
ATOM   451  O  OD1 A ASP   A 1 36  ? 16.126  18.120 -3.342  0.13 45.74  ? 79  ASP   A OD1 1 
ATOM   452  O  OD1 B ASP   A 1 36  ? 16.128  18.118 -3.349  0.14 45.74  ? 79  ASP   A OD1 1 
ATOM   453  O  OD1 C ASP   A 1 36  ? 16.049  18.434 -3.146  0.36 45.78  ? 79  ASP   A OD1 1 
ATOM   454  O  OD1 D ASP   A 1 36  ? 16.049  18.434 -3.146  0.37 45.78  ? 79  ASP   A OD1 1 
ATOM   455  O  OD2 A ASP   A 1 36  ? 18.040  19.047 -2.689  0.13 48.16  ? 79  ASP   A OD2 1 
ATOM   456  O  OD2 B ASP   A 1 36  ? 18.040  19.046 -2.690  0.14 48.17  ? 79  ASP   A OD2 1 
ATOM   457  O  OD2 C ASP   A 1 36  ? 18.165  19.066 -2.936  0.36 48.41  ? 79  ASP   A OD2 1 
ATOM   458  O  OD2 D ASP   A 1 36  ? 18.166  19.065 -2.937  0.37 48.41  ? 79  ASP   A OD2 1 
ATOM   459  N  N   A GLU   A 1 37  ? 15.354  16.352 -0.481  0.13 46.49  ? 80  GLU   A N   1 
ATOM   460  N  N   B GLU   A 1 37  ? 15.355  16.352 -0.481  0.14 46.48  ? 80  GLU   A N   1 
ATOM   461  N  N   C GLU   A 1 37  ? 15.328  16.341 -0.492  0.36 44.93  ? 80  GLU   A N   1 
ATOM   462  N  N   D GLU   A 1 37  ? 15.328  16.341 -0.493  0.37 44.93  ? 80  GLU   A N   1 
ATOM   463  C  CA  A GLU   A 1 37  ? 14.111  16.669 0.270   0.13 46.59  ? 80  GLU   A CA  1 
ATOM   464  C  CA  B GLU   A 1 37  ? 14.111  16.668 0.270   0.14 46.59  ? 80  GLU   A CA  1 
ATOM   465  C  CA  C GLU   A 1 37  ? 14.071  16.651 0.229   0.36 46.11  ? 80  GLU   A CA  1 
ATOM   466  C  CA  D GLU   A 1 37  ? 14.071  16.651 0.229   0.37 46.11  ? 80  GLU   A CA  1 
ATOM   467  C  C   A GLU   A 1 37  ? 13.451  17.929 -0.311  0.13 45.56  ? 80  GLU   A C   1 
ATOM   468  C  C   B GLU   A 1 37  ? 13.451  17.929 -0.311  0.14 45.56  ? 80  GLU   A C   1 
ATOM   469  C  C   C GLU   A 1 37  ? 13.426  17.906 -0.382  0.36 45.34  ? 80  GLU   A C   1 
ATOM   470  C  C   D GLU   A 1 37  ? 13.426  17.906 -0.383  0.37 45.34  ? 80  GLU   A C   1 
ATOM   471  O  O   A GLU   A 1 37  ? 12.219  18.057 -0.182  0.13 45.28  ? 80  GLU   A O   1 
ATOM   472  O  O   B GLU   A 1 37  ? 12.219  18.058 -0.181  0.14 45.28  ? 80  GLU   A O   1 
ATOM   473  O  O   C GLU   A 1 37  ? 12.174  17.986 -0.399  0.36 45.64  ? 80  GLU   A O   1 
ATOM   474  O  O   D GLU   A 1 37  ? 12.174  17.986 -0.399  0.37 45.64  ? 80  GLU   A O   1 
ATOM   475  C  CB  A GLU   A 1 37  ? 14.444  16.819 1.755   0.13 48.35  ? 80  GLU   A CB  1 
ATOM   476  C  CB  B GLU   A 1 37  ? 14.444  16.818 1.755   0.14 48.34  ? 80  GLU   A CB  1 
ATOM   477  C  CB  C GLU   A 1 37  ? 14.394  16.774 1.717   0.36 47.92  ? 80  GLU   A CB  1 
ATOM   478  C  CB  D GLU   A 1 37  ? 14.394  16.773 1.716   0.37 47.92  ? 80  GLU   A CB  1 
ATOM   479  C  CG  A GLU   A 1 37  ? 13.229  16.881 2.660   0.13 49.03  ? 80  GLU   A CG  1 
ATOM   480  C  CG  B GLU   A 1 37  ? 13.229  16.880 2.660   0.14 49.04  ? 80  GLU   A CG  1 
ATOM   481  C  CG  C GLU   A 1 37  ? 13.180  16.930 2.601   0.36 49.72  ? 80  GLU   A CG  1 
ATOM   482  C  CG  D GLU   A 1 37  ? 13.180  16.931 2.601   0.37 49.72  ? 80  GLU   A CG  1 
ATOM   483  C  CD  A GLU   A 1 37  ? 13.580  16.913 4.138   0.13 50.98  ? 80  GLU   A CD  1 
ATOM   484  C  CD  B GLU   A 1 37  ? 13.580  16.913 4.137   0.14 50.98  ? 80  GLU   A CD  1 
ATOM   485  C  CD  C GLU   A 1 37  ? 13.541  16.894 4.073   0.36 51.91  ? 80  GLU   A CD  1 
ATOM   486  C  CD  D GLU   A 1 37  ? 13.541  16.894 4.072   0.37 51.92  ? 80  GLU   A CD  1 
ATOM   487  O  OE1 A GLU   A 1 37  ? 14.493  17.680 4.502   0.13 52.10  ? 80  GLU   A OE1 1 
ATOM   488  O  OE1 B GLU   A 1 37  ? 14.494  17.679 4.501   0.14 52.10  ? 80  GLU   A OE1 1 
ATOM   489  O  OE1 C GLU   A 1 37  ? 13.644  17.981 4.682   0.36 52.57  ? 80  GLU   A OE1 1 
ATOM   490  O  OE1 D GLU   A 1 37  ? 13.644  17.981 4.681   0.37 52.58  ? 80  GLU   A OE1 1 
ATOM   491  O  OE2 A GLU   A 1 37  ? 12.950  16.165 4.918   0.13 51.91  ? 80  GLU   A OE2 1 
ATOM   492  O  OE2 B GLU   A 1 37  ? 12.949  16.167 4.918   0.14 51.93  ? 80  GLU   A OE2 1 
ATOM   493  O  OE2 C GLU   A 1 37  ? 13.751  15.780 4.594   0.36 54.07  ? 80  GLU   A OE2 1 
ATOM   494  O  OE2 D GLU   A 1 37  ? 13.751  15.780 4.593   0.37 54.08  ? 80  GLU   A OE2 1 
ATOM   495  N  N   . SER   A 1 38  ? 14.235  18.819 -0.932  1.00 45.22  ? 81  SER   A N   1 
ATOM   496  C  CA  . SER   A 1 38  ? 13.730  20.073 -1.554  1.00 44.75  ? 81  SER   A CA  1 
ATOM   497  C  C   . SER   A 1 38  ? 13.164  19.822 -2.974  1.00 42.14  ? 81  SER   A C   1 
ATOM   498  O  O   . SER   A 1 38  ? 12.619  20.772 -3.545  1.00 41.45  ? 81  SER   A O   1 
ATOM   499  C  CB  . SER   A 1 38  ? 14.813  21.102 -1.509  1.00 47.22  ? 81  SER   A CB  1 
ATOM   500  O  OG  . SER   A 1 38  ? 15.199  21.302 -0.149  1.00 51.13  ? 81  SER   A OG  1 
ATOM   501  N  N   . GLY   A 1 39  ? 13.165  18.576 -3.447  1.00 39.94  ? 82  GLY   A N   1 
ATOM   502  C  CA  . GLY   A 1 39  ? 12.642  18.224 -4.783  1.00 41.13  ? 82  GLY   A CA  1 
ATOM   503  C  C   . GLY   A 1 39  ? 13.633  18.526 -5.888  1.00 41.28  ? 82  GLY   A C   1 
ATOM   504  O  O   . GLY   A 1 39  ? 13.209  18.498 -7.095  1.00 39.49  ? 82  GLY   A O   1 
ATOM   505  N  N   A ASP   A 1 40  ? 14.899  18.804 -5.554  0.13 42.41  ? 83  ASP   A N   1 
ATOM   506  N  N   B ASP   A 1 40  ? 14.899  18.804 -5.554  0.14 42.41  ? 83  ASP   A N   1 
ATOM   507  N  N   C ASP   A 1 40  ? 14.898  18.801 -5.526  0.36 42.50  ? 83  ASP   A N   1 
ATOM   508  N  N   D ASP   A 1 40  ? 14.898  18.801 -5.526  0.37 42.49  ? 83  ASP   A N   1 
ATOM   509  C  CA  A ASP   A 1 40  ? 15.950  19.141 -6.556  0.13 43.32  ? 83  ASP   A CA  1 
ATOM   510  C  CA  B ASP   A 1 40  ? 15.949  19.141 -6.557  0.14 43.32  ? 83  ASP   A CA  1 
ATOM   511  C  CA  C ASP   A 1 40  ? 16.003  19.087 -6.487  0.36 44.09  ? 83  ASP   A CA  1 
ATOM   512  C  CA  D ASP   A 1 40  ? 16.003  19.087 -6.487  0.37 44.09  ? 83  ASP   A CA  1 
ATOM   513  C  C   A ASP   A 1 40  ? 16.598  17.841 -7.049  0.13 43.22  ? 83  ASP   A C   1 
ATOM   514  C  C   B ASP   A 1 40  ? 16.598  17.841 -7.049  0.14 43.22  ? 83  ASP   A C   1 
ATOM   515  C  C   C ASP   A 1 40  ? 16.533  17.756 -7.034  0.36 43.30  ? 83  ASP   A C   1 
ATOM   516  C  C   D ASP   A 1 40  ? 16.533  17.756 -7.034  0.37 43.30  ? 83  ASP   A C   1 
ATOM   517  O  O   A ASP   A 1 40  ? 17.166  17.100 -6.208  0.13 43.57  ? 83  ASP   A O   1 
ATOM   518  O  O   B ASP   A 1 40  ? 17.166  17.099 -6.208  0.14 43.57  ? 83  ASP   A O   1 
ATOM   519  O  O   C ASP   A 1 40  ? 16.977  16.900 -6.207  0.36 42.75  ? 83  ASP   A O   1 
ATOM   520  O  O   D ASP   A 1 40  ? 16.977  16.900 -6.207  0.37 42.75  ? 83  ASP   A O   1 
ATOM   521  C  CB  A ASP   A 1 40  ? 16.983  20.116 -5.982  0.13 45.05  ? 83  ASP   A CB  1 
ATOM   522  C  CB  B ASP   A 1 40  ? 16.983  20.116 -5.983  0.14 45.06  ? 83  ASP   A CB  1 
ATOM   523  C  CB  C ASP   A 1 40  ? 17.170  19.836 -5.825  0.36 46.40  ? 83  ASP   A CB  1 
ATOM   524  C  CB  D ASP   A 1 40  ? 17.170  19.836 -5.825  0.37 46.40  ? 83  ASP   A CB  1 
ATOM   525  C  CG  A ASP   A 1 40  ? 16.499  21.558 -5.905  0.13 45.31  ? 83  ASP   A CG  1 
ATOM   526  C  CG  B ASP   A 1 40  ? 16.499  21.558 -5.905  0.14 45.32  ? 83  ASP   A CG  1 
ATOM   527  C  CG  C ASP   A 1 40  ? 16.836  21.167 -5.166  0.36 47.30  ? 83  ASP   A CG  1 
ATOM   528  C  CG  D ASP   A 1 40  ? 16.836  21.167 -5.166  0.37 47.31  ? 83  ASP   A CG  1 
ATOM   529  O  OD1 A ASP   A 1 40  ? 15.477  21.873 -6.555  0.13 44.51  ? 83  ASP   A OD1 1 
ATOM   530  O  OD1 B ASP   A 1 40  ? 15.477  21.873 -6.556  0.14 44.52  ? 83  ASP   A OD1 1 
ATOM   531  O  OD1 C ASP   A 1 40  ? 16.401  22.086 -5.881  0.36 47.19  ? 83  ASP   A OD1 1 
ATOM   532  O  OD1 D ASP   A 1 40  ? 16.402  22.086 -5.881  0.37 47.19  ? 83  ASP   A OD1 1 
ATOM   533  O  OD2 A ASP   A 1 40  ? 17.149  22.359 -5.199  0.13 46.80  ? 83  ASP   A OD2 1 
ATOM   534  O  OD2 B ASP   A 1 40  ? 17.149  22.359 -5.200  0.14 46.81  ? 83  ASP   A OD2 1 
ATOM   535  O  OD2 C ASP   A 1 40  ? 17.067  21.285 -3.943  0.36 48.03  ? 83  ASP   A OD2 1 
ATOM   536  O  OD2 D ASP   A 1 40  ? 17.067  21.285 -3.943  0.37 48.03  ? 83  ASP   A OD2 1 
ATOM   537  N  N   . PHE   A 1 41  ? 16.498  17.576 -8.356  1.00 42.30  ? 84  PHE   A N   1 
ATOM   538  C  CA  . PHE   A 1 41  ? 17.219  16.479 -9.033  1.00 43.85  ? 84  PHE   A CA  1 
ATOM   539  C  C   . PHE   A 1 41  ? 18.687  16.892 -9.250  1.00 47.65  ? 84  PHE   A C   1 
ATOM   540  O  O   . PHE   A 1 41  ? 18.959  18.072 -9.636  1.00 48.44  ? 84  PHE   A O   1 
ATOM   541  C  CB  . PHE   A 1 41  ? 16.593  16.166 -10.390 1.00 40.50  ? 84  PHE   A CB  1 
ATOM   542  C  CG  . PHE   A 1 41  ? 15.335  15.337 -10.331 1.00 38.21  ? 84  PHE   A CG  1 
ATOM   543  C  CD1 . PHE   A 1 41  ? 15.386  13.974 -10.067 1.00 38.90  ? 84  PHE   A CD1 1 
ATOM   544  C  CD2 . PHE   A 1 41  ? 14.101  15.901 -10.550 1.00 37.29  ? 84  PHE   A CD2 1 
ATOM   545  C  CE1 . PHE   A 1 41  ? 14.230  13.206 -10.038 1.00 38.14  ? 84  PHE   A CE1 1 
ATOM   546  C  CE2 . PHE   A 1 41  ? 12.942  15.145 -10.455 1.00 36.62  ? 84  PHE   A CE2 1 
ATOM   547  C  CZ  . PHE   A 1 41  ? 13.008  13.800 -10.234 1.00 36.19  ? 84  PHE   A CZ  1 
ATOM   548  N  N   A SER   A 1 42  ? 19.615  15.958 -9.010  0.13 49.43  ? 85  SER   A N   1 
ATOM   549  N  N   B SER   A 1 42  ? 19.615  15.958 -9.010  0.14 49.44  ? 85  SER   A N   1 
ATOM   550  N  N   C SER   A 1 42  ? 19.605  15.942 -9.038  0.36 49.36  ? 85  SER   A N   1 
ATOM   551  N  N   D SER   A 1 42  ? 19.605  15.942 -9.038  0.37 49.36  ? 85  SER   A N   1 
ATOM   552  C  CA  A SER   A 1 42  ? 21.082  16.140 -9.180  0.13 51.77  ? 85  SER   A CA  1 
ATOM   553  C  CA  B SER   A 1 42  ? 21.082  16.140 -9.181  0.14 51.77  ? 85  SER   A CA  1 
ATOM   554  C  CA  C SER   A 1 42  ? 21.072  16.107 -9.205  0.36 51.34  ? 85  SER   A CA  1 
ATOM   555  C  CA  D SER   A 1 42  ? 21.072  16.107 -9.205  0.37 51.34  ? 85  SER   A CA  1 
ATOM   556  C  C   A SER   A 1 42  ? 21.660  14.965 -9.976  0.13 53.07  ? 85  SER   A C   1 
ATOM   557  C  C   B SER   A 1 42  ? 21.660  14.965 -9.976  0.14 53.07  ? 85  SER   A C   1 
ATOM   558  C  C   C SER   A 1 42  ? 21.626  14.946 -10.030 0.36 52.14  ? 85  SER   A C   1 
ATOM   559  C  C   D SER   A 1 42  ? 21.626  14.946 -10.030 0.37 52.14  ? 85  SER   A C   1 
ATOM   560  O  O   A SER   A 1 42  ? 21.142  13.841 -9.828  0.13 52.36  ? 85  SER   A O   1 
ATOM   561  O  O   B SER   A 1 42  ? 21.143  13.841 -9.828  0.14 52.35  ? 85  SER   A O   1 
ATOM   562  O  O   C SER   A 1 42  ? 21.176  13.800 -9.819  0.36 51.04  ? 85  SER   A O   1 
ATOM   563  O  O   D SER   A 1 42  ? 21.176  13.800 -9.819  0.37 51.03  ? 85  SER   A O   1 
ATOM   564  C  CB  A SER   A 1 42  ? 21.777  16.298 -7.847  0.13 53.31  ? 85  SER   A CB  1 
ATOM   565  C  CB  B SER   A 1 42  ? 21.777  16.299 -7.847  0.14 53.32  ? 85  SER   A CB  1 
ATOM   566  C  CB  C SER   A 1 42  ? 21.778  16.214 -7.868  0.36 53.57  ? 85  SER   A CB  1 
ATOM   567  C  CB  D SER   A 1 42  ? 21.779  16.215 -7.868  0.37 53.57  ? 85  SER   A CB  1 
ATOM   568  O  OG  A SER   A 1 42  ? 21.500  15.204 -6.986  0.13 53.25  ? 85  SER   A OG  1 
ATOM   569  O  OG  B SER   A 1 42  ? 21.500  15.205 -6.985  0.14 53.26  ? 85  SER   A OG  1 
ATOM   570  O  OG  C SER   A 1 42  ? 21.535  15.080 -7.050  0.36 53.66  ? 85  SER   A OG  1 
ATOM   571  O  OG  D SER   A 1 42  ? 21.535  15.080 -7.049  0.37 53.66  ? 85  SER   A OG  1 
ATOM   572  N  N   A LEU   A 1 43  ? 22.700  15.223 -10.778 0.13 55.29  ? 86  LEU   A N   1 
ATOM   573  N  N   B LEU   A 1 43  ? 22.700  15.223 -10.779 0.14 55.29  ? 86  LEU   A N   1 
ATOM   574  N  N   C LEU   A 1 43  ? 22.585  15.235 -10.918 0.36 53.77  ? 86  LEU   A N   1 
ATOM   575  N  N   D LEU   A 1 43  ? 22.585  15.235 -10.919 0.37 53.77  ? 86  LEU   A N   1 
ATOM   576  C  CA  A LEU   A 1 43  ? 23.325  14.222 -11.687 0.13 56.95  ? 86  LEU   A CA  1 
ATOM   577  C  CA  B LEU   A 1 43  ? 23.325  14.222 -11.687 0.14 56.95  ? 86  LEU   A CA  1 
ATOM   578  C  CA  C LEU   A 1 43  ? 23.232  14.203 -11.767 0.36 55.17  ? 86  LEU   A CA  1 
ATOM   579  C  CA  D LEU   A 1 43  ? 23.232  14.203 -11.767 0.37 55.16  ? 86  LEU   A CA  1 
ATOM   580  C  C   A LEU   A 1 43  ? 24.250  13.286 -10.902 0.13 58.75  ? 86  LEU   A C   1 
ATOM   581  C  C   B LEU   A 1 43  ? 24.250  13.286 -10.902 0.14 58.74  ? 86  LEU   A C   1 
ATOM   582  C  C   C LEU   A 1 43  ? 24.254  13.441 -10.921 0.36 55.60  ? 86  LEU   A C   1 
ATOM   583  C  C   D LEU   A 1 43  ? 24.253  13.441 -10.921 0.37 55.59  ? 86  LEU   A C   1 
ATOM   584  O  O   A LEU   A 1 43  ? 24.932  13.758 -9.980  0.13 60.54  ? 86  LEU   A O   1 
ATOM   585  O  O   B LEU   A 1 43  ? 24.932  13.758 -9.981  0.14 60.55  ? 86  LEU   A O   1 
ATOM   586  O  O   C LEU   A 1 43  ? 25.244  14.068 -10.516 0.36 55.67  ? 86  LEU   A O   1 
ATOM   587  O  O   D LEU   A 1 43  ? 25.244  14.068 -10.516 0.37 55.66  ? 86  LEU   A O   1 
ATOM   588  C  CB  A LEU   A 1 43  ? 24.120  14.933 -12.788 0.13 58.04  ? 86  LEU   A CB  1 
ATOM   589  C  CB  B LEU   A 1 43  ? 24.121  14.933 -12.788 0.14 58.03  ? 86  LEU   A CB  1 
ATOM   590  C  CB  C LEU   A 1 43  ? 23.921  14.865 -12.966 0.36 56.97  ? 86  LEU   A CB  1 
ATOM   591  C  CB  D LEU   A 1 43  ? 23.921  14.865 -12.966 0.37 56.96  ? 86  LEU   A CB  1 
ATOM   592  C  CG  A LEU   A 1 43  ? 23.473  14.966 -14.171 0.13 57.47  ? 86  LEU   A CG  1 
ATOM   593  C  CG  B LEU   A 1 43  ? 23.473  14.967 -14.171 0.14 57.47  ? 86  LEU   A CG  1 
ATOM   594  C  CG  C LEU   A 1 43  ? 23.480  14.388 -14.349 0.36 57.73  ? 86  LEU   A CG  1 
ATOM   595  C  CG  D LEU   A 1 43  ? 23.481  14.387 -14.349 0.37 57.73  ? 86  LEU   A CG  1 
ATOM   596  C  CD1 A LEU   A 1 43  ? 24.340  15.758 -15.135 0.13 58.86  ? 86  LEU   A CD1 1 
ATOM   597  C  CD1 B LEU   A 1 43  ? 24.341  15.758 -15.134 0.14 58.87  ? 86  LEU   A CD1 1 
ATOM   598  C  CD1 C LEU   A 1 43  ? 24.613  14.567 -15.347 0.36 59.88  ? 86  LEU   A CD1 1 
ATOM   599  C  CD1 D LEU   A 1 43  ? 24.614  14.566 -15.347 0.37 59.87  ? 86  LEU   A CD1 1 
ATOM   600  C  CD2 A LEU   A 1 43  ? 23.233  13.560 -14.706 0.13 57.42  ? 86  LEU   A CD2 1 
ATOM   601  C  CD2 B LEU   A 1 43  ? 23.232  13.561 -14.707 0.14 57.42  ? 86  LEU   A CD2 1 
ATOM   602  C  CD2 C LEU   A 1 43  ? 23.024  12.936 -14.341 0.36 57.75  ? 86  LEU   A CD2 1 
ATOM   603  C  CD2 D LEU   A 1 43  ? 23.024  12.934 -14.341 0.37 57.75  ? 86  LEU   A CD2 1 
ATOM   604  N  N   A VAL   A 1 44  ? 24.283  12.014 -11.308 0.13 59.66  ? 87  VAL   A N   1 
ATOM   605  N  N   B VAL   A 1 44  ? 24.283  12.014 -11.307 0.14 59.66  ? 87  VAL   A N   1 
ATOM   606  N  N   C VAL   A 1 44  ? 24.028  12.143 -10.707 0.36 55.59  ? 87  VAL   A N   1 
ATOM   607  N  N   D VAL   A 1 44  ? 24.028  12.143 -10.707 0.37 55.58  ? 87  VAL   A N   1 
ATOM   608  C  CA  A VAL   A 1 44  ? 25.291  10.989 -10.905 0.13 61.76  ? 87  VAL   A CA  1 
ATOM   609  C  CA  B VAL   A 1 44  ? 25.291  10.989 -10.904 0.14 61.76  ? 87  VAL   A CA  1 
ATOM   610  C  CA  C VAL   A 1 44  ? 24.983  11.230 -10.011 0.36 58.80  ? 87  VAL   A CA  1 
ATOM   611  C  CA  D VAL   A 1 44  ? 24.983  11.230 -10.011 0.37 58.80  ? 87  VAL   A CA  1 
ATOM   612  C  C   A VAL   A 1 44  ? 25.886  10.400 -12.194 0.13 62.99  ? 87  VAL   A C   1 
ATOM   613  C  C   B VAL   A 1 44  ? 25.886  10.400 -12.194 0.14 63.00  ? 87  VAL   A C   1 
ATOM   614  C  C   C VAL   A 1 44  ? 26.130  10.908 -10.975 0.36 61.28  ? 87  VAL   A C   1 
ATOM   615  C  C   D VAL   A 1 44  ? 26.130  10.908 -10.974 0.37 61.28  ? 87  VAL   A C   1 
ATOM   616  O  O   A VAL   A 1 44  ? 25.126  10.270 -13.182 0.13 61.57  ? 87  VAL   A O   1 
ATOM   617  O  O   B VAL   A 1 44  ? 25.126  10.272 -13.182 0.14 61.57  ? 87  VAL   A O   1 
ATOM   618  O  O   C VAL   A 1 44  ? 27.286  10.980 -10.531 0.36 63.05  ? 87  VAL   A O   1 
ATOM   619  O  O   D VAL   A 1 44  ? 27.285  10.980 -10.531 0.37 63.04  ? 87  VAL   A O   1 
ATOM   620  C  CB  A VAL   A 1 44  ? 24.646  9.912  -10.010 0.13 61.55  ? 87  VAL   A CB  1 
ATOM   621  C  CB  B VAL   A 1 44  ? 24.646  9.911  -10.010 0.14 61.55  ? 87  VAL   A CB  1 
ATOM   622  C  CB  C VAL   A 1 44  ? 24.282  9.950  -9.518  0.36 58.12  ? 87  VAL   A CB  1 
ATOM   623  C  CB  D VAL   A 1 44  ? 24.282  9.951  -9.518  0.37 58.12  ? 87  VAL   A CB  1 
ATOM   624  C  CG1 A VAL   A 1 44  ? 25.660  8.887  -9.528  0.13 63.68  ? 87  VAL   A CG1 1 
ATOM   625  C  CG1 B VAL   A 1 44  ? 25.660  8.886  -9.529  0.14 63.68  ? 87  VAL   A CG1 1 
ATOM   626  C  CG1 C VAL   A 1 44  ? 25.246  9.004  -8.825  0.36 60.61  ? 87  VAL   A CG1 1 
ATOM   627  C  CG1 D VAL   A 1 44  ? 25.246  9.004  -8.825  0.37 60.61  ? 87  VAL   A CG1 1 
ATOM   628  C  CG2 A VAL   A 1 44  ? 23.906  10.528 -8.830  0.13 60.32  ? 87  VAL   A CG2 1 
ATOM   629  C  CG2 B VAL   A 1 44  ? 23.907  10.528 -8.829  0.14 60.30  ? 87  VAL   A CG2 1 
ATOM   630  C  CG2 C VAL   A 1 44  ? 23.107  10.267 -8.618  0.36 55.96  ? 87  VAL   A CG2 1 
ATOM   631  C  CG2 D VAL   A 1 44  ? 23.107  10.267 -8.618  0.37 55.95  ? 87  VAL   A CG2 1 
ATOM   632  N  N   A GLU   A 1 45  ? 27.193  10.103 -12.206 0.13 65.07  ? 88  GLU   A N   1 
ATOM   633  N  N   B GLU   A 1 45  ? 27.193  10.103 -12.206 0.14 65.07  ? 88  GLU   A N   1 
ATOM   634  N  N   C GLU   A 1 45  ? 25.803  10.553 -12.228 0.36 60.36  ? 88  GLU   A N   1 
ATOM   635  N  N   D GLU   A 1 45  ? 25.803  10.554 -12.228 0.37 60.36  ? 88  GLU   A N   1 
ATOM   636  C  CA  A GLU   A 1 45  ? 27.926  9.544  -13.380 0.13 66.39  ? 88  GLU   A CA  1 
ATOM   637  C  CA  B GLU   A 1 45  ? 27.926  9.544  -13.381 0.14 66.39  ? 88  GLU   A CA  1 
ATOM   638  C  CA  C GLU   A 1 45  ? 26.755  10.389 -13.367 0.36 62.30  ? 88  GLU   A CA  1 
ATOM   639  C  CA  D GLU   A 1 45  ? 26.755  10.389 -13.368 0.37 62.30  ? 88  GLU   A CA  1 
ATOM   640  C  C   A GLU   A 1 45  ? 28.839  8.402  -12.921 0.13 68.04  ? 88  GLU   A C   1 
ATOM   641  C  C   B GLU   A 1 45  ? 28.839  8.402  -12.922 0.14 68.04  ? 88  GLU   A C   1 
ATOM   642  C  C   C GLU   A 1 45  ? 26.006  10.597 -14.691 0.36 61.16  ? 88  GLU   A C   1 
ATOM   643  C  C   D GLU   A 1 45  ? 26.006  10.596 -14.691 0.37 61.16  ? 88  GLU   A C   1 
ATOM   644  O  O   A GLU   A 1 45  ? 28.970  7.384  -13.601 0.13 67.93  ? 88  GLU   A O   1 
ATOM   645  O  O   B GLU   A 1 45  ? 28.969  7.383  -13.601 0.14 67.91  ? 88  GLU   A O   1 
ATOM   646  O  O   C GLU   A 1 45  ? 26.343  11.541 -15.410 0.36 62.33  ? 88  GLU   A O   1 
ATOM   647  O  O   D GLU   A 1 45  ? 26.343  11.541 -15.410 0.37 62.33  ? 88  GLU   A O   1 
ATOM   648  C  CB  A GLU   A 1 45  ? 28.746  10.627 -14.088 0.13 67.41  ? 88  GLU   A CB  1 
ATOM   649  C  CB  B GLU   A 1 45  ? 28.746  10.627 -14.088 0.14 67.41  ? 88  GLU   A CB  1 
ATOM   650  C  CB  C GLU   A 1 45  ? 27.413  9.004  -13.386 0.36 64.63  ? 88  GLU   A CB  1 
ATOM   651  C  CB  D GLU   A 1 45  ? 27.413  9.004  -13.386 0.37 64.63  ? 88  GLU   A CB  1 
ATOM   652  C  CG  A GLU   A 1 45  ? 27.904  11.631 -14.858 0.13 65.83  ? 88  GLU   A CG  1 
ATOM   653  C  CG  B GLU   A 1 45  ? 27.905  11.631 -14.859 0.14 65.83  ? 88  GLU   A CG  1 
ATOM   654  C  CG  C GLU   A 1 45  ? 28.391  8.754  -12.253 0.36 66.95  ? 88  GLU   A CG  1 
ATOM   655  C  CG  D GLU   A 1 45  ? 28.391  8.754  -12.253 0.37 66.95  ? 88  GLU   A CG  1 
ATOM   656  C  CD  A GLU   A 1 45  ? 27.379  11.143 -16.199 0.13 65.52  ? 88  GLU   A CD  1 
ATOM   657  C  CD  B GLU   A 1 45  ? 27.380  11.143 -16.199 0.14 65.52  ? 88  GLU   A CD  1 
ATOM   658  C  CD  C GLU   A 1 45  ? 27.968  7.719  -11.220 0.36 67.58  ? 88  GLU   A CD  1 
ATOM   659  C  CD  D GLU   A 1 45  ? 27.968  7.719  -11.220 0.37 67.59  ? 88  GLU   A CD  1 
ATOM   660  O  OE1 A GLU   A 1 45  ? 27.989  10.215 -16.770 0.13 67.13  ? 88  GLU   A OE1 1 
ATOM   661  O  OE1 B GLU   A 1 45  ? 27.990  10.215 -16.771 0.14 67.15  ? 88  GLU   A OE1 1 
ATOM   662  O  OE1 C GLU   A 1 45  ? 27.080  6.895  -11.533 0.36 68.42  ? 88  GLU   A OE1 1 
ATOM   663  O  OE1 D GLU   A 1 45  ? 27.080  6.895  -11.533 0.37 68.43  ? 88  GLU   A OE1 1 
ATOM   664  O  OE2 A GLU   A 1 45  ? 26.373  11.704 -16.683 0.13 63.74  ? 88  GLU   A OE2 1 
ATOM   665  O  OE2 B GLU   A 1 45  ? 26.374  11.704 -16.684 0.14 63.75  ? 88  GLU   A OE2 1 
ATOM   666  O  OE2 C GLU   A 1 45  ? 28.537  7.726  -10.119 0.36 67.48  ? 88  GLU   A OE2 1 
ATOM   667  O  OE2 D GLU   A 1 45  ? 28.537  7.725  -10.119 0.37 67.47  ? 88  GLU   A OE2 1 
ATOM   668  N  N   . GLY   B 2 7   ? -14.519 32.172 -12.618 1.00 62.06  ? 16  GLY   B N   1 
ATOM   669  C  CA  . GLY   B 2 7   ? -13.985 32.496 -13.986 1.00 62.92  ? 16  GLY   B CA  1 
ATOM   670  C  C   . GLY   B 2 7   ? -13.982 31.280 -14.898 1.00 62.01  ? 16  GLY   B C   1 
ATOM   671  O  O   . GLY   B 2 7   ? -15.056 30.671 -15.064 1.00 62.77  ? 16  GLY   B O   1 
ATOM   672  N  N   . GLU   B 2 8   ? -12.808 30.909 -15.429 1.00 59.50  ? 17  GLU   B N   1 
ATOM   673  C  CA  . GLU   B 2 8   ? -12.637 29.867 -16.483 1.00 56.51  ? 17  GLU   B CA  1 
ATOM   674  C  C   . GLU   B 2 8   ? -12.310 28.511 -15.843 1.00 55.51  ? 17  GLU   B C   1 
ATOM   675  O  O   . GLU   B 2 8   ? -11.247 28.375 -15.172 1.00 56.16  ? 17  GLU   B O   1 
ATOM   676  C  CB  . GLU   B 2 8   ? -11.534 30.273 -17.459 1.00 55.72  ? 17  GLU   B CB  1 
ATOM   677  C  CG  . GLU   B 2 8   ? -11.773 29.731 -18.855 1.00 56.25  ? 17  GLU   B CG  1 
ATOM   678  C  CD  . GLU   B 2 8   ? -10.776 30.215 -19.894 1.00 54.76  ? 17  GLU   B CD  1 
ATOM   679  O  OE1 . GLU   B 2 8   ? -9.777  30.896 -19.508 1.00 51.18  ? 17  GLU   B OE1 1 
ATOM   680  O  OE2 . GLU   B 2 8   ? -11.014 29.930 -21.120 1.00 59.74  ? 17  GLU   B OE2 1 
ATOM   681  N  N   A THR   B 2 9   ? -13.204 27.533 -16.010 0.25 54.75  ? 18  THR   B N   1 
ATOM   682  N  N   B THR   B 2 9   ? -13.210 27.543 -16.032 0.25 54.03  ? 18  THR   B N   1 
ATOM   683  N  N   C THR   B 2 9   ? -13.204 27.533 -16.010 0.25 54.75  ? 18  THR   B N   1 
ATOM   684  N  N   D THR   B 2 9   ? -13.210 27.543 -16.032 0.25 54.03  ? 18  THR   B N   1 
ATOM   685  C  CA  A THR   B 2 9   ? -13.078 26.166 -15.436 0.25 54.04  ? 18  THR   B CA  1 
ATOM   686  C  CA  B THR   B 2 9   ? -13.147 26.181 -15.442 0.25 52.94  ? 18  THR   B CA  1 
ATOM   687  C  CA  C THR   B 2 9   ? -13.078 26.166 -15.436 0.25 54.04  ? 18  THR   B CA  1 
ATOM   688  C  CA  D THR   B 2 9   ? -13.147 26.181 -15.442 0.25 52.94  ? 18  THR   B CA  1 
ATOM   689  C  C   A THR   B 2 9   ? -13.087 25.142 -16.572 0.25 51.76  ? 18  THR   B C   1 
ATOM   690  C  C   B THR   B 2 9   ? -13.050 25.145 -16.566 0.25 51.11  ? 18  THR   B C   1 
ATOM   691  C  C   C THR   B 2 9   ? -13.087 25.142 -16.572 0.25 51.76  ? 18  THR   B C   1 
ATOM   692  C  C   D THR   B 2 9   ? -13.050 25.145 -16.566 0.25 51.11  ? 18  THR   B C   1 
ATOM   693  O  O   A THR   B 2 9   ? -13.263 23.942 -16.275 0.25 51.03  ? 18  THR   B O   1 
ATOM   694  O  O   B THR   B 2 9   ? -13.108 23.938 -16.254 0.25 50.51  ? 18  THR   B O   1 
ATOM   695  O  O   C THR   B 2 9   ? -13.263 23.942 -16.275 0.25 51.03  ? 18  THR   B O   1 
ATOM   696  O  O   D THR   B 2 9   ? -13.108 23.938 -16.254 0.25 50.51  ? 18  THR   B O   1 
ATOM   697  C  CB  A THR   B 2 9   ? -14.186 25.895 -14.408 0.25 55.34  ? 18  THR   B CB  1 
ATOM   698  C  CB  B THR   B 2 9   ? -14.369 25.921 -14.550 0.25 53.49  ? 18  THR   B CB  1 
ATOM   699  C  CB  C THR   B 2 9   ? -14.186 25.895 -14.408 0.25 55.34  ? 18  THR   B CB  1 
ATOM   700  C  CB  D THR   B 2 9   ? -14.369 25.921 -14.550 0.25 53.49  ? 18  THR   B CB  1 
ATOM   701  O  OG1 A THR   B 2 9   ? -14.220 27.002 -13.506 0.25 56.81  ? 18  THR   B OG1 1 
ATOM   702  O  OG1 B THR   B 2 9   ? -15.521 26.189 -15.349 0.25 53.03  ? 18  THR   B OG1 1 
ATOM   703  O  OG1 C THR   B 2 9   ? -14.220 27.002 -13.506 0.25 56.81  ? 18  THR   B OG1 1 
ATOM   704  O  OG1 D THR   B 2 9   ? -15.521 26.189 -15.349 0.25 53.03  ? 18  THR   B OG1 1 
ATOM   705  C  CG2 A THR   B 2 9   ? -13.986 24.610 -13.629 0.25 55.12  ? 18  THR   B CG2 1 
ATOM   706  C  CG2 B THR   B 2 9   ? -14.394 26.762 -13.290 0.25 53.95  ? 18  THR   B CG2 1 
ATOM   707  C  CG2 C THR   B 2 9   ? -13.986 24.610 -13.629 0.25 55.12  ? 18  THR   B CG2 1 
ATOM   708  C  CG2 D THR   B 2 9   ? -14.394 26.762 -13.290 0.25 53.95  ? 18  THR   B CG2 1 
ATOM   709  N  N   . THR   B 2 10  ? -12.914 25.597 -17.823 1.00 50.95  ? 19  THR   B N   1 
ATOM   710  C  CA  . THR   B 2 10  ? -12.857 24.714 -18.996 1.00 47.73  ? 19  THR   B CA  1 
ATOM   711  C  C   . THR   B 2 10  ? -11.603 23.865 -18.947 1.00 43.27  ? 19  THR   B C   1 
ATOM   712  O  O   . THR   B 2 10  ? -10.541 24.456 -18.676 1.00 45.89  ? 19  THR   B O   1 
ATOM   713  C  CB  . THR   B 2 10  ? -12.793 25.491 -20.343 1.00 47.51  ? 19  THR   B CB  1 
ATOM   714  O  OG1 . THR   B 2 10  ? -13.581 26.661 -20.242 1.00 48.50  ? 19  THR   B OG1 1 
ATOM   715  C  CG2 . THR   B 2 10  ? -13.323 24.672 -21.474 1.00 49.93  ? 19  THR   B CG2 1 
ATOM   716  N  N   . ASP   B 2 11  ? -11.712 22.594 -19.325 1.00 42.32  ? 20  ASP   B N   1 
ATOM   717  C  CA  . ASP   B 2 11  ? -10.558 21.682 -19.533 1.00 41.18  ? 20  ASP   B CA  1 
ATOM   718  C  C   . ASP   B 2 11  ? -9.594  22.326 -20.555 1.00 43.81  ? 20  ASP   B C   1 
ATOM   719  O  O   . ASP   B 2 11  ? -10.085 23.046 -21.485 1.00 40.96  ? 20  ASP   B O   1 
ATOM   720  C  CB  . ASP   B 2 11  ? -11.035 20.287 -19.934 1.00 43.29  ? 20  ASP   B CB  1 
ATOM   721  C  CG  . ASP   B 2 11  ? -11.630 19.300 -18.934 1.00 45.41  ? 20  ASP   B CG  1 
ATOM   722  O  OD1 . ASP   B 2 11  ? -11.893 19.665 -17.748 1.00 42.86  ? 20  ASP   B OD1 1 
ATOM   723  O  OD2 . ASP   B 2 11  ? -11.800 18.118 -19.366 1.00 48.18  ? 20  ASP   B OD2 1 
ATOM   724  N  N   . GLY   B 2 12  ? -8.280  22.156 -20.387 1.00 41.14  ? 21  GLY   B N   1 
ATOM   725  C  CA  . GLY   B 2 12  ? -7.300  22.754 -21.304 1.00 38.56  ? 21  GLY   B CA  1 
ATOM   726  C  C   . GLY   B 2 12  ? -6.010  23.087 -20.615 1.00 38.39  ? 21  GLY   B C   1 
ATOM   727  O  O   . GLY   B 2 12  ? -5.861  22.702 -19.393 1.00 35.85  ? 21  GLY   B O   1 
ATOM   728  N  N   . VAL   B 2 13  ? -5.071  23.664 -21.356 1.00 36.07  ? 22  VAL   B N   1 
ATOM   729  C  CA  . VAL   B 2 13  ? -3.712  24.047 -20.888 1.00 35.68  ? 22  VAL   B CA  1 
ATOM   730  C  C   . VAL   B 2 13  ? -3.707  25.549 -20.717 1.00 36.76  ? 22  VAL   B C   1 
ATOM   731  O  O   . VAL   B 2 13  ? -4.330  26.256 -21.491 1.00 35.83  ? 22  VAL   B O   1 
ATOM   732  C  CB  . VAL   B 2 13  ? -2.527  23.533 -21.697 1.00 34.43  ? 22  VAL   B CB  1 
ATOM   733  C  CG1 . VAL   B 2 13  ? -2.525  24.168 -23.098 1.00 33.17  ? 22  VAL   B CG1 1 
ATOM   734  C  CG2 . VAL   B 2 13  ? -1.161  23.771 -21.102 1.00 32.64  ? 22  VAL   B CG2 1 
ATOM   735  N  N   . TYR   B 2 14  ? -3.176  26.013 -19.578 1.00 34.84  ? 23  TYR   B N   1 
ATOM   736  C  CA  . TYR   B 2 14  ? -3.181  27.443 -19.258 1.00 35.35  ? 23  TYR   B CA  1 
ATOM   737  C  C   . TYR   B 2 14  ? -1.787  27.993 -19.039 1.00 36.45  ? 23  TYR   B C   1 
ATOM   738  O  O   . TYR   B 2 14  ? -0.956  27.313 -18.397 1.00 37.13  ? 23  TYR   B O   1 
ATOM   739  C  CB  . TYR   B 2 14  ? -4.039  27.671 -18.005 1.00 35.79  ? 23  TYR   B CB  1 
ATOM   740  C  CG  . TYR   B 2 14  ? -5.510  27.496 -18.229 1.00 35.58  ? 23  TYR   B CG  1 
ATOM   741  C  CD1 . TYR   B 2 14  ? -6.047  26.237 -18.402 1.00 36.44  ? 23  TYR   B CD1 1 
ATOM   742  C  CD2 . TYR   B 2 14  ? -6.371  28.584 -18.181 1.00 36.53  ? 23  TYR   B CD2 1 
ATOM   743  C  CE1 . TYR   B 2 14  ? -7.398  26.073 -18.633 1.00 37.81  ? 23  TYR   B CE1 1 
ATOM   744  C  CE2 . TYR   B 2 14  ? -7.722  28.436 -18.394 1.00 37.15  ? 23  TYR   B CE2 1 
ATOM   745  C  CZ  . TYR   B 2 14  ? -8.236  27.174 -18.606 1.00 37.84  ? 23  TYR   B CZ  1 
ATOM   746  O  OH  . TYR   B 2 14  ? -9.576  27.002 -18.760 1.00 40.06  ? 23  TYR   B OH  1 
ATOM   747  N  N   . ARG   B 2 15  ? -1.620  29.284 -19.314 1.00 37.12  ? 24  ARG   B N   1 
ATOM   748  C  CA  . ARG   B 2 15  ? -0.474  30.065 -18.776 1.00 38.48  ? 24  ARG   B CA  1 
ATOM   749  C  C   . ARG   B 2 15  ? -0.752  30.532 -17.342 1.00 39.02  ? 24  ARG   B C   1 
ATOM   750  O  O   . ARG   B 2 15  ? -1.905  30.917 -17.054 1.00 38.64  ? 24  ARG   B O   1 
ATOM   751  C  CB  . ARG   B 2 15  ? -0.214  31.327 -19.590 1.00 40.89  ? 24  ARG   B CB  1 
ATOM   752  C  CG  . ARG   B 2 15  ? 0.116   31.050 -21.048 1.00 41.71  ? 24  ARG   B CG  1 
ATOM   753  C  CD  . ARG   B 2 15  ? 0.216   32.339 -21.822 1.00 44.21  ? 24  ARG   B CD  1 
ATOM   754  N  NE  . ARG   B 2 15  ? 0.041   31.953 -23.212 1.00 45.05  ? 24  ARG   B NE  1 
ATOM   755  C  CZ  . ARG   B 2 15  ? 1.022   31.620 -24.055 1.00 46.73  ? 24  ARG   B CZ  1 
ATOM   756  N  NH1 . ARG   B 2 15  ? 2.293   31.671 -23.674 1.00 46.18  ? 24  ARG   B NH1 1 
ATOM   757  N  NH2 . ARG   B 2 15  ? 0.716   31.294 -25.302 1.00 46.92  ? 24  ARG   B NH2 1 
ATOM   758  N  N   . VAL   B 2 16  ? 0.311   30.536 -16.525 1.00 38.43  ? 25  VAL   B N   1 
ATOM   759  C  CA  . VAL   B 2 16  ? 0.350   31.200 -15.206 1.00 40.39  ? 25  VAL   B CA  1 
ATOM   760  C  C   . VAL   B 2 16  ? 1.222   32.445 -15.321 1.00 40.21  ? 25  VAL   B C   1 
ATOM   761  O  O   . VAL   B 2 16  ? 2.414   32.274 -15.563 1.00 41.25  ? 25  VAL   B O   1 
ATOM   762  C  CB  . VAL   B 2 16  ? 0.891   30.197 -14.179 1.00 39.37  ? 25  VAL   B CB  1 
ATOM   763  C  CG1 . VAL   B 2 16  ? 0.710   30.748 -12.794 1.00 39.08  ? 25  VAL   B CG1 1 
ATOM   764  C  CG2 . VAL   B 2 16  ? 0.237   28.830 -14.363 1.00 39.33  ? 25  VAL   B CG2 1 
ATOM   765  N  N   . MET   B 2 17  ? 0.636   33.609 -15.034 1.00 41.58  ? 26  MET   B N   1 
ATOM   766  C  CA  . MET   B 2 17  ? 1.216   34.955 -15.227 1.00 43.94  ? 26  MET   B CA  1 
ATOM   767  C  C   . MET   B 2 17  ? 1.329   35.665 -13.878 1.00 45.39  ? 26  MET   B C   1 
ATOM   768  O  O   . MET   B 2 17  ? 0.498   35.381 -12.993 1.00 42.93  ? 26  MET   B O   1 
ATOM   769  C  CB  . MET   B 2 17  ? 0.303   35.783 -16.131 1.00 44.76  ? 26  MET   B CB  1 
ATOM   770  C  CG  . MET   B 2 17  ? -0.015  35.087 -17.451 1.00 46.44  ? 26  MET   B CG  1 
ATOM   771  S  SD  . MET   B 2 17  ? 1.443   34.731 -18.477 1.00 45.86  ? 26  MET   B SD  1 
ATOM   772  C  CE  . MET   B 2 17  ? 1.947   36.401 -18.883 1.00 47.88  ? 26  MET   B CE  1 
ATOM   773  N  N   . THR   B 2 18  ? 2.290   36.580 -13.768 1.00 46.81  ? 27  THR   B N   1 
ATOM   774  C  CA  . THR   B 2 18  ? 2.418   37.481 -12.605 1.00 48.93  ? 27  THR   B CA  1 
ATOM   775  C  C   . THR   B 2 18  ? 2.630   38.908 -13.091 1.00 52.24  ? 27  THR   B C   1 
ATOM   776  O  O   . THR   B 2 18  ? 3.241   39.088 -14.201 1.00 49.18  ? 27  THR   B O   1 
ATOM   777  C  CB  . THR   B 2 18  ? 3.526   37.052 -11.630 1.00 48.93  ? 27  THR   B CB  1 
ATOM   778  O  OG1 . THR   B 2 18  ? 3.415   37.996 -10.562 1.00 46.94  ? 27  THR   B OG1 1 
ATOM   779  C  CG2 . THR   B 2 18  ? 4.916   37.073 -12.224 1.00 48.62  ? 27  THR   B CG2 1 
ATOM   780  N  N   . ARG   B 2 19  ? 2.138   39.877 -12.303 1.00 54.36  ? 28  ARG   B N   1 
ATOM   781  C  CA  . ARG   B 2 19  ? 2.385   41.312 -12.562 1.00 61.88  ? 28  ARG   B CA  1 
ATOM   782  C  C   . ARG   B 2 19  ? 3.401   41.862 -11.561 1.00 63.23  ? 28  ARG   B C   1 
ATOM   783  O  O   . ARG   B 2 19  ? 3.657   43.066 -11.645 1.00 63.31  ? 28  ARG   B O   1 
ATOM   784  C  CB  . ARG   B 2 19  ? 1.067   42.081 -12.587 1.00 65.84  ? 28  ARG   B CB  1 
ATOM   785  C  CG  . ARG   B 2 19  ? 0.165   41.634 -13.725 1.00 70.93  ? 28  ARG   B CG  1 
ATOM   786  C  CD  . ARG   B 2 19  ? -0.433  42.764 -14.538 1.00 77.01  ? 28  ARG   B CD  1 
ATOM   787  N  NE  . ARG   B 2 19  ? -1.447  42.290 -15.481 1.00 83.12  ? 28  ARG   B NE  1 
ATOM   788  C  CZ  . ARG   B 2 19  ? -2.695  41.934 -15.148 1.00 86.74  ? 28  ARG   B CZ  1 
ATOM   789  N  NH1 . ARG   B 2 19  ? -3.099  41.980 -13.886 1.00 86.22  ? 28  ARG   B NH1 1 
ATOM   790  N  NH2 . ARG   B 2 19  ? -3.537  41.519 -16.085 1.00 87.45  ? 28  ARG   B NH2 1 
ATOM   791  N  N   . ARG   B 2 20  ? 4.038   40.998 -10.763 1.00 66.75  ? 29  ARG   B N   1 
ATOM   792  C  CA  . ARG   B 2 20  ? 4.956   41.363 -9.647  1.00 73.68  ? 29  ARG   B CA  1 
ATOM   793  C  C   . ARG   B 2 20  ? 6.340   41.737 -10.193 1.00 73.87  ? 29  ARG   B C   1 
ATOM   794  O  O   . ARG   B 2 20  ? 7.055   42.482 -9.505  1.00 74.95  ? 29  ARG   B O   1 
ATOM   795  C  CB  . ARG   B 2 20  ? 5.052   40.197 -8.652  1.00 80.01  ? 29  ARG   B CB  1 
ATOM   796  C  CG  . ARG   B 2 20  ? 5.359   40.606 -7.217  1.00 86.89  ? 29  ARG   B CG  1 
ATOM   797  C  CD  . ARG   B 2 20  ? 5.637   39.413 -6.313  1.00 90.79  ? 29  ARG   B CD  1 
ATOM   798  N  NE  . ARG   B 2 20  ? 6.746   38.607 -6.829  1.00 92.72  ? 29  ARG   B NE  1 
ATOM   799  C  CZ  . ARG   B 2 20  ? 8.040   38.844 -6.613  1.00 94.19  ? 29  ARG   B CZ  1 
ATOM   800  N  NH1 . ARG   B 2 20  ? 8.417   39.875 -5.872  1.00 95.94  ? 29  ARG   B NH1 1 
ATOM   801  N  NH2 . ARG   B 2 20  ? 8.955   38.043 -7.136  1.00 92.93  ? 29  ARG   B NH2 1 
ATOM   802  N  N   . LEU   B 2 21  ? 6.698   41.239 -11.381 1.00 71.26  ? 30  LEU   B N   1 
ATOM   803  C  CA  . LEU   B 2 21  ? 7.962   41.572 -12.093 1.00 69.54  ? 30  LEU   B CA  1 
ATOM   804  C  C   . LEU   B 2 21  ? 7.669   42.663 -13.136 1.00 66.46  ? 30  LEU   B C   1 
ATOM   805  O  O   . LEU   B 2 21  ? 6.566   43.244 -13.099 1.00 68.13  ? 30  LEU   B O   1 
ATOM   806  C  CB  . LEU   B 2 21  ? 8.504   40.289 -12.730 1.00 70.99  ? 30  LEU   B CB  1 
ATOM   807  C  CG  . LEU   B 2 21  ? 9.363   39.380 -11.848 1.00 72.90  ? 30  LEU   B CG  1 
ATOM   808  C  CD1 . LEU   B 2 21  ? 8.969   39.446 -10.381 1.00 73.30  ? 30  LEU   B CD1 1 
ATOM   809  C  CD2 . LEU   B 2 21  ? 9.301   37.944 -12.350 1.00 72.69  ? 30  LEU   B CD2 1 
ATOM   810  N  N   . LEU   B 2 22  ? 8.618   42.957 -14.027 1.00 64.13  ? 31  LEU   B N   1 
ATOM   811  C  CA  . LEU   B 2 22  ? 8.404   43.911 -15.151 1.00 61.83  ? 31  LEU   B CA  1 
ATOM   812  C  C   . LEU   B 2 22  ? 7.258   43.403 -16.029 1.00 60.55  ? 31  LEU   B C   1 
ATOM   813  O  O   . LEU   B 2 22  ? 7.196   42.168 -16.244 1.00 59.74  ? 31  LEU   B O   1 
ATOM   814  C  CB  . LEU   B 2 22  ? 9.692   44.013 -15.962 1.00 62.41  ? 31  LEU   B CB  1 
ATOM   815  C  CG  . LEU   B 2 22  ? 9.691   45.071 -17.054 1.00 60.86  ? 31  LEU   B CG  1 
ATOM   816  C  CD1 . LEU   B 2 22  ? 9.777   46.456 -16.452 1.00 59.77  ? 31  LEU   B CD1 1 
ATOM   817  C  CD2 . LEU   B 2 22  ? 10.845  44.818 -18.018 1.00 61.88  ? 31  LEU   B CD2 1 
ATOM   818  N  N   . GLY   B 2 23  ? 6.387   44.300 -16.506 1.00 58.05  ? 32  GLY   B N   1 
ATOM   819  C  CA  . GLY   B 2 23  ? 5.238   43.936 -17.358 1.00 57.79  ? 32  GLY   B CA  1 
ATOM   820  C  C   . GLY   B 2 23  ? 4.470   42.740 -16.808 1.00 56.16  ? 32  GLY   B C   1 
ATOM   821  O  O   . GLY   B 2 23  ? 4.348   42.594 -15.577 1.00 56.36  ? 32  GLY   B O   1 
ATOM   822  N  N   . SER   B 2 24  ? 3.946   41.898 -17.692 1.00 54.48  ? 33  SER   B N   1 
ATOM   823  C  CA  . SER   B 2 24  ? 3.234   40.651 -17.333 1.00 54.09  ? 33  SER   B CA  1 
ATOM   824  C  C   . SER   B 2 24  ? 4.179   39.508 -17.654 1.00 52.19  ? 33  SER   B C   1 
ATOM   825  O  O   . SER   B 2 24  ? 4.526   39.403 -18.824 1.00 49.65  ? 33  SER   B O   1 
ATOM   826  C  CB  . SER   B 2 24  ? 1.961   40.503 -18.118 1.00 54.91  ? 33  SER   B CB  1 
ATOM   827  O  OG  . SER   B 2 24  ? 1.034   41.505 -17.765 1.00 57.18  ? 33  SER   B OG  1 
ATOM   828  N  N   . THR   B 2 25  ? 4.585   38.722 -16.669 1.00 47.76  ? 34  THR   B N   1 
ATOM   829  C  CA  . THR   B 2 25  ? 5.645   37.707 -16.850 1.00 48.28  ? 34  THR   B CA  1 
ATOM   830  C  C   . THR   B 2 25  ? 5.039   36.316 -16.726 1.00 46.72  ? 34  THR   B C   1 
ATOM   831  O  O   . THR   B 2 25  ? 4.277   36.068 -15.726 1.00 45.39  ? 34  THR   B O   1 
ATOM   832  C  CB  . THR   B 2 25  ? 6.801   37.882 -15.855 1.00 49.86  ? 34  THR   B CB  1 
ATOM   833  O  OG1 . THR   B 2 25  ? 7.256   39.234 -15.916 1.00 51.93  ? 34  THR   B OG1 1 
ATOM   834  C  CG2 . THR   B 2 25  ? 7.961   36.957 -16.161 1.00 50.48  ? 34  THR   B CG2 1 
ATOM   835  N  N   . GLN   B 2 26  ? 5.483   35.405 -17.586 1.00 43.68  ? 35  GLN   B N   1 
ATOM   836  C  CA  . GLN   B 2 26  ? 5.030   34.001 -17.484 1.00 43.48  ? 35  GLN   B CA  1 
ATOM   837  C  C   . GLN   B 2 26  ? 5.993   33.248 -16.566 1.00 42.91  ? 35  GLN   B C   1 
ATOM   838  O  O   . GLN   B 2 26  ? 7.182   33.136 -16.882 1.00 42.05  ? 35  GLN   B O   1 
ATOM   839  C  CB  . GLN   B 2 26  ? 4.863   33.322 -18.834 1.00 43.23  ? 35  GLN   B CB  1 
ATOM   840  C  CG  . GLN   B 2 26  ? 4.248   31.942 -18.736 1.00 41.95  ? 35  GLN   B CG  1 
ATOM   841  C  CD  . GLN   B 2 26  ? 4.016   31.321 -20.090 1.00 42.58  ? 35  GLN   B CD  1 
ATOM   842  O  OE1 . GLN   B 2 26  ? 3.383   31.935 -20.960 1.00 41.86  ? 35  GLN   B OE1 1 
ATOM   843  N  NE2 . GLN   B 2 26  ? 4.439   30.071 -20.221 1.00 41.42  ? 35  GLN   B NE2 1 
ATOM   844  N  N   . VAL   B 2 27  ? 5.460   32.742 -15.456 1.00 41.21  ? 36  VAL   B N   1 
ATOM   845  C  CA  . VAL   B 2 27  ? 6.233   31.979 -14.443 1.00 40.52  ? 36  VAL   B CA  1 
ATOM   846  C  C   . VAL   B 2 27  ? 5.971   30.493 -14.679 1.00 37.71  ? 36  VAL   B C   1 
ATOM   847  O  O   . VAL   B 2 27  ? 6.845   29.674 -14.334 1.00 37.88  ? 36  VAL   B O   1 
ATOM   848  C  CB  . VAL   B 2 27  ? 5.897   32.472 -13.020 1.00 41.24  ? 36  VAL   B CB  1 
ATOM   849  C  CG1 . VAL   B 2 27  ? 6.443   33.865 -12.771 1.00 42.85  ? 36  VAL   B CG1 1 
ATOM   850  C  CG2 . VAL   B 2 27  ? 4.421   32.444 -12.688 1.00 41.40  ? 36  VAL   B CG2 1 
ATOM   851  N  N   . GLY   B 2 28  ? 4.873   30.140 -15.350 1.00 36.68  ? 37  GLY   B N   1 
ATOM   852  C  CA  . GLY   B 2 28  ? 4.709   28.753 -15.812 1.00 34.56  ? 37  GLY   B CA  1 
ATOM   853  C  C   . GLY   B 2 28  ? 3.378   28.453 -16.419 1.00 35.30  ? 37  GLY   B C   1 
ATOM   854  O  O   . GLY   B 2 28  ? 2.782   29.368 -17.059 1.00 36.59  ? 37  GLY   B O   1 
ATOM   855  N  N   . VAL   B 2 29  ? 2.992   27.178 -16.325 1.00 35.00  ? 38  VAL   B N   1 
ATOM   856  C  CA  . VAL   B 2 29  ? 1.889   26.547 -17.120 1.00 35.43  ? 38  VAL   B CA  1 
ATOM   857  C  C   . VAL   B 2 29  ? 1.162   25.556 -16.219 1.00 34.95  ? 38  VAL   B C   1 
ATOM   858  O  O   . VAL   B 2 29  ? 1.844   24.953 -15.369 1.00 34.84  ? 38  VAL   B O   1 
ATOM   859  C  CB  . VAL   B 2 29  ? 2.474   25.817 -18.338 1.00 35.40  ? 38  VAL   B CB  1 
ATOM   860  C  CG1 . VAL   B 2 29  ? 1.430   25.215 -19.290 1.00 35.67  ? 38  VAL   B CG1 1 
ATOM   861  C  CG2 . VAL   B 2 29  ? 3.379   26.742 -19.133 1.00 36.05  ? 38  VAL   B CG2 1 
ATOM   862  N  N   . GLY   B 2 30  ? -0.075  25.221 -16.548 1.00 35.24  ? 39  GLY   B N   1 
ATOM   863  C  CA  . GLY   B 2 30  ? -0.698  24.049 -15.935 1.00 35.28  ? 39  GLY   B CA  1 
ATOM   864  C  C   . GLY   B 2 30  ? -1.908  23.584 -16.668 1.00 35.68  ? 39  GLY   B C   1 
ATOM   865  O  O   . GLY   B 2 30  ? -2.212  24.197 -17.731 1.00 34.80  ? 39  GLY   B O   1 
ATOM   866  N  N   . VAL   B 2 31  ? -2.582  22.588 -16.069 1.00 33.19  ? 40  VAL   B N   1 
ATOM   867  C  CA  . VAL   B 2 31  ? -3.674  21.782 -16.689 1.00 35.62  ? 40  VAL   B CA  1 
ATOM   868  C  C   . VAL   B 2 31  ? -4.934  21.924 -15.891 1.00 35.75  ? 40  VAL   B C   1 
ATOM   869  O  O   . VAL   B 2 31  ? -4.879  21.625 -14.587 1.00 33.30  ? 40  VAL   B O   1 
ATOM   870  C  CB  . VAL   B 2 31  ? -3.330  20.297 -16.797 1.00 36.07  ? 40  VAL   B CB  1 
ATOM   871  C  CG1 . VAL   B 2 31  ? -4.518  19.513 -17.291 1.00 36.54  ? 40  VAL   B CG1 1 
ATOM   872  C  CG2 . VAL   B 2 31  ? -2.114  20.077 -17.671 1.00 37.10  ? 40  VAL   B CG2 1 
ATOM   873  N  N   . MET   B 2 32  ? -6.028  22.308 -16.546 1.00 34.35  ? 41  MET   B N   1 
ATOM   874  C  CA  . MET   B 2 32  ? -7.371  22.316 -15.940 1.00 35.96  ? 41  MET   B CA  1 
ATOM   875  C  C   . MET   B 2 32  ? -8.073  21.027 -16.385 1.00 36.24  ? 41  MET   B C   1 
ATOM   876  O  O   . MET   B 2 32  ? -8.247  20.779 -17.605 1.00 35.88  ? 41  MET   B O   1 
ATOM   877  C  CB  . MET   B 2 32  ? -8.121  23.597 -16.293 1.00 36.15  ? 41  MET   B CB  1 
ATOM   878  C  CG  . MET   B 2 32  ? -9.444  23.762 -15.648 1.00 38.41  ? 41  MET   B CG  1 
ATOM   879  S  SD  . MET   B 2 32  ? -9.176  24.286 -13.916 1.00 39.09  ? 41  MET   B SD  1 
ATOM   880  C  CE  . MET   B 2 32  ? -8.408  25.894 -14.109 1.00 38.65  ? 41  MET   B CE  1 
ATOM   881  N  N   . GLN   B 2 33  ? -8.465  20.170 -15.445 1.00 36.48  ? 42  GLN   B N   1 
ATOM   882  C  CA  . GLN   B 2 33  ? -9.201  18.920 -15.735 1.00 38.07  ? 42  GLN   B CA  1 
ATOM   883  C  C   . GLN   B 2 33  ? -10.175 18.623 -14.605 1.00 40.33  ? 42  GLN   B C   1 
ATOM   884  O  O   . GLN   B 2 33  ? -9.730  18.726 -13.396 1.00 40.23  ? 42  GLN   B O   1 
ATOM   885  C  CB  . GLN   B 2 33  ? -8.255  17.734 -15.932 1.00 39.57  ? 42  GLN   B CB  1 
ATOM   886  C  CG  . GLN   B 2 33  ? -9.009  16.574 -16.567 1.00 43.16  ? 42  GLN   B CG  1 
ATOM   887  C  CD  . GLN   B 2 33  ? -8.147  15.364 -16.799 1.00 45.78  ? 42  GLN   B CD  1 
ATOM   888  O  OE1 . GLN   B 2 33  ? -8.409  14.295 -16.260 1.00 52.33  ? 42  GLN   B OE1 1 
ATOM   889  N  NE2 . GLN   B 2 33  ? -7.071  15.533 -17.540 1.00 44.61  ? 42  GLN   B NE2 1 
ATOM   890  N  N   . GLU   B 2 34  ? -11.432 18.312 -14.941 1.00 40.92  ? 43  GLU   B N   1 
ATOM   891  C  CA  . GLU   B 2 34  ? -12.509 18.034 -13.952 1.00 42.46  ? 43  GLU   B CA  1 
ATOM   892  C  C   . GLU   B 2 34  ? -12.579 19.158 -12.902 1.00 41.61  ? 43  GLU   B C   1 
ATOM   893  O  O   . GLU   B 2 34  ? -12.885 18.830 -11.689 1.00 40.37  ? 43  GLU   B O   1 
ATOM   894  C  CB  . GLU   B 2 34  ? -12.272 16.667 -13.311 1.00 44.35  ? 43  GLU   B CB  1 
ATOM   895  C  CG  . GLU   B 2 34  ? -12.429 15.508 -14.283 1.00 46.75  ? 43  GLU   B CG  1 
ATOM   896  C  CD  . GLU   B 2 34  ? -11.876 14.170 -13.822 1.00 49.07  ? 43  GLU   B CD  1 
ATOM   897  O  OE1 . GLU   B 2 34  ? -12.494 13.556 -12.946 1.00 51.30  ? 43  GLU   B OE1 1 
ATOM   898  O  OE2 . GLU   B 2 34  ? -10.815 13.754 -14.330 1.00 50.45  ? 43  GLU   B OE2 1 
ATOM   899  N  N   . GLY   B 2 35  ? -12.414 20.423 -13.316 1.00 40.06  ? 44  GLY   B N   1 
ATOM   900  C  CA  . GLY   B 2 35  ? -12.502 21.629 -12.467 1.00 39.44  ? 44  GLY   B CA  1 
ATOM   901  C  C   . GLY   B 2 35  ? -11.355 21.759 -11.446 1.00 38.54  ? 44  GLY   B C   1 
ATOM   902  O  O   . GLY   B 2 35  ? -11.445 22.639 -10.563 1.00 38.64  ? 44  GLY   B O   1 
ATOM   903  N  N   . VAL   B 2 36  ? -10.304 20.946 -11.555 1.00 36.88  ? 45  VAL   B N   1 
ATOM   904  C  CA  . VAL   B 2 36  ? -9.031  21.071 -10.796 1.00 34.78  ? 45  VAL   B CA  1 
ATOM   905  C  C   . VAL   B 2 36  ? -7.913  21.645 -11.629 1.00 34.34  ? 45  VAL   B C   1 
ATOM   906  O  O   . VAL   B 2 36  ? -7.749  21.167 -12.827 1.00 33.20  ? 45  VAL   B O   1 
ATOM   907  C  CB  . VAL   B 2 36  ? -8.664  19.701 -10.206 1.00 35.86  ? 45  VAL   B CB  1 
ATOM   908  C  CG1 . VAL   B 2 36  ? -7.381  19.762 -9.405  1.00 35.81  ? 45  VAL   B CG1 1 
ATOM   909  C  CG2 . VAL   B 2 36  ? -9.806  19.202 -9.329  1.00 36.36  ? 45  VAL   B CG2 1 
ATOM   910  N  N   . PHE   B 2 37  ? -7.191  22.623 -11.112 1.00 32.72  ? 46  PHE   B N   1 
ATOM   911  C  CA  . PHE   B 2 37  ? -5.973  23.167 -11.754 1.00 33.22  ? 46  PHE   B CA  1 
ATOM   912  C  C   . PHE   B 2 37  ? -4.710  22.492 -11.200 1.00 32.92  ? 46  PHE   B C   1 
ATOM   913  O  O   . PHE   B 2 37  ? -4.515  22.462 -9.935  1.00 32.93  ? 46  PHE   B O   1 
ATOM   914  C  CB  . PHE   B 2 37  ? -5.866  24.678 -11.656 1.00 33.32  ? 46  PHE   B CB  1 
ATOM   915  C  CG  . PHE   B 2 37  ? -4.817  25.246 -12.573 1.00 33.68  ? 46  PHE   B CG  1 
ATOM   916  C  CD1 . PHE   B 2 37  ? -4.946  25.119 -13.942 1.00 34.79  ? 46  PHE   B CD1 1 
ATOM   917  C  CD2 . PHE   B 2 37  ? -3.776  26.003 -12.073 1.00 34.07  ? 46  PHE   B CD2 1 
ATOM   918  C  CE1 . PHE   B 2 37  ? -3.995  25.658 -14.795 1.00 34.36  ? 46  PHE   B CE1 1 
ATOM   919  C  CE2 . PHE   B 2 37  ? -2.832  26.546 -12.922 1.00 34.97  ? 46  PHE   B CE2 1 
ATOM   920  C  CZ  . PHE   B 2 37  ? -2.930  26.353 -14.282 1.00 34.90  ? 46  PHE   B CZ  1 
ATOM   921  N  N   . HIS   B 2 38  ? -3.888  21.975 -12.106 1.00 31.43  ? 47  HIS   B N   1 
ATOM   922  C  CA  . HIS   B 2 38  ? -2.673  21.151 -11.847 1.00 32.04  ? 47  HIS   B CA  1 
ATOM   923  C  C   . HIS   B 2 38  ? -1.442  21.900 -12.345 1.00 33.11  ? 47  HIS   B C   1 
ATOM   924  O  O   . HIS   B 2 38  ? -1.417  22.278 -13.567 1.00 33.80  ? 47  HIS   B O   1 
ATOM   925  C  CB  . HIS   B 2 38  ? -2.729  19.776 -12.468 1.00 31.47  ? 47  HIS   B CB  1 
ATOM   926  C  CG  . HIS   B 2 38  ? -4.011  19.046 -12.279 1.00 31.86  ? 47  HIS   B CG  1 
ATOM   927  N  ND1 . HIS   B 2 38  ? -5.201  19.502 -12.787 1.00 32.01  ? 47  HIS   B ND1 1 
ATOM   928  C  CD2 . HIS   B 2 38  ? -4.294  17.930 -11.559 1.00 31.97  ? 47  HIS   B CD2 1 
ATOM   929  C  CE1 . HIS   B 2 38  ? -6.141  18.635 -12.458 1.00 32.48  ? 47  HIS   B CE1 1 
ATOM   930  N  NE2 . HIS   B 2 38  ? -5.616  17.686 -11.677 1.00 31.55  ? 47  HIS   B NE2 1 
ATOM   931  N  N   . THR   B 2 39  ? -0.465  22.173 -11.492 1.00 32.75  ? 48  THR   B N   1 
ATOM   932  C  CA  . THR   B 2 39  ? 0.805   22.825 -11.890 1.00 32.61  ? 48  THR   B CA  1 
ATOM   933  C  C   . THR   B 2 39  ? 1.921   22.328 -10.964 1.00 34.35  ? 48  THR   B C   1 
ATOM   934  O  O   . THR   B 2 39  ? 1.663   21.393 -10.131 1.00 32.94  ? 48  THR   B O   1 
ATOM   935  C  CB  . THR   B 2 39  ? 0.655   24.344 -12.010 1.00 32.51  ? 48  THR   B CB  1 
ATOM   936  O  OG1 . THR   B 2 39  ? 1.810   24.955 -12.612 1.00 33.65  ? 48  THR   B OG1 1 
ATOM   937  C  CG2 . THR   B 2 39  ? 0.394   25.041 -10.681 1.00 33.67  ? 48  THR   B CG2 1 
ATOM   938  N  N   . MET   B 2 40  ? 3.116   22.873 -11.163 1.00 34.82  ? 49  MET   B N   1 
ATOM   939  C  CA  . MET   B 2 40  ? 4.320   22.495 -10.408 1.00 34.86  ? 49  MET   B CA  1 
ATOM   940  C  C   . MET   B 2 40  ? 4.400   23.468 -9.218  1.00 34.74  ? 49  MET   B C   1 
ATOM   941  O  O   . MET   B 2 40  ? 4.096   24.664 -9.366  1.00 34.20  ? 49  MET   B O   1 
ATOM   942  C  CB  . MET   B 2 40  ? 5.600   22.426 -11.236 1.00 35.24  ? 49  MET   B CB  1 
ATOM   943  C  CG  . MET   B 2 40  ? 5.361   21.671 -12.558 1.00 37.21  ? 49  MET   B CG  1 
ATOM   944  S  SD  . MET   B 2 40  ? 6.865   20.964 -13.183 1.00 39.39  ? 49  MET   B SD  1 
ATOM   945  C  CE  . MET   B 2 40  ? 7.095   19.486 -12.182 1.00 39.19  ? 49  MET   B CE  1 
ATOM   946  N  N   A TRP   B 2 41  ? 4.789   22.952 -8.046  0.13 34.61  ? 50  TRP   B N   1 
ATOM   947  N  N   B TRP   B 2 41  ? 4.778   22.953 -8.044  0.14 34.01  ? 50  TRP   B N   1 
ATOM   948  N  N   C TRP   B 2 41  ? 4.776   22.950 -8.041  0.36 34.03  ? 50  TRP   B N   1 
ATOM   949  N  N   D TRP   B 2 41  ? 4.776   22.951 -8.043  0.37 33.72  ? 50  TRP   B N   1 
ATOM   950  C  CA  A TRP   B 2 41  ? 4.880   23.737 -6.783  0.13 35.06  ? 50  TRP   B CA  1 
ATOM   951  C  CA  B TRP   B 2 41  ? 4.856   23.756 -6.793  0.14 34.24  ? 50  TRP   B CA  1 
ATOM   952  C  CA  C TRP   B 2 41  ? 4.861   23.763 -6.794  0.36 34.86  ? 50  TRP   B CA  1 
ATOM   953  C  CA  D TRP   B 2 41  ? 4.852   23.757 -6.792  0.37 34.23  ? 50  TRP   B CA  1 
ATOM   954  C  C   A TRP   B 2 41  ? 5.742   24.987 -7.010  0.13 35.37  ? 50  TRP   B C   1 
ATOM   955  C  C   B TRP   B 2 41  ? 5.734   24.996 -7.022  0.14 34.88  ? 50  TRP   B C   1 
ATOM   956  C  C   C TRP   B 2 41  ? 5.721   25.009 -7.050  0.36 35.25  ? 50  TRP   B C   1 
ATOM   957  C  C   D TRP   B 2 41  ? 5.733   24.997 -7.024  0.37 34.86  ? 50  TRP   B C   1 
ATOM   958  O  O   A TRP   B 2 41  ? 5.349   26.063 -6.521  0.13 35.66  ? 50  TRP   B O   1 
ATOM   959  O  O   B TRP   B 2 41  ? 5.344   26.079 -6.549  0.14 35.26  ? 50  TRP   B O   1 
ATOM   960  O  O   C TRP   B 2 41  ? 5.309   26.098 -6.621  0.36 35.82  ? 50  TRP   B O   1 
ATOM   961  O  O   D TRP   B 2 41  ? 5.348   26.077 -6.553  0.37 35.34  ? 50  TRP   B O   1 
ATOM   962  C  CB  A TRP   B 2 41  ? 5.435   22.886 -5.634  0.13 34.87  ? 50  TRP   B CB  1 
ATOM   963  C  CB  B TRP   B 2 41  ? 5.376   22.922 -5.615  0.14 33.42  ? 50  TRP   B CB  1 
ATOM   964  C  CB  C TRP   B 2 41  ? 5.435   22.963 -5.621  0.36 34.19  ? 50  TRP   B CB  1 
ATOM   965  C  CB  D TRP   B 2 41  ? 5.380   22.920 -5.623  0.37 33.11  ? 50  TRP   B CB  1 
ATOM   966  C  CG  A TRP   B 2 41  ? 5.280   23.541 -4.291  0.13 35.22  ? 50  TRP   B CG  1 
ATOM   967  C  CG  B TRP   B 2 41  ? 5.473   23.739 -4.358  0.14 33.31  ? 50  TRP   B CG  1 
ATOM   968  C  CG  C TRP   B 2 41  ? 5.217   23.688 -4.315  0.36 34.79  ? 50  TRP   B CG  1 
ATOM   969  C  CG  D TRP   B 2 41  ? 5.475   23.732 -4.356  0.37 33.15  ? 50  TRP   B CG  1 
ATOM   970  C  CD1 A TRP   B 2 41  ? 4.281   23.331 -3.387  0.13 35.36  ? 50  TRP   B CD1 1 
ATOM   971  C  CD1 B TRP   B 2 41  ? 6.543   24.482 -3.949  0.14 33.39  ? 50  TRP   B CD1 1 
ATOM   972  C  CD1 C TRP   B 2 41  ? 4.078   23.680 -3.567  0.36 35.23  ? 50  TRP   B CD1 1 
ATOM   973  C  CD1 D TRP   B 2 41  ? 6.541   24.480 -3.949  0.37 33.42  ? 50  TRP   B CD1 1 
ATOM   974  C  CD2 A TRP   B 2 41  ? 6.129   24.554 -3.719  0.13 35.67  ? 50  TRP   B CD2 1 
ATOM   975  C  CD2 B TRP   B 2 41  ? 4.424   24.004 -3.408  0.14 33.33  ? 50  TRP   B CD2 1 
ATOM   976  C  CD2 C TRP   B 2 41  ? 6.095   24.640 -3.682  0.36 35.64  ? 50  TRP   B CD2 1 
ATOM   977  C  CD2 D TRP   B 2 41  ? 4.426   24.001 -3.408  0.37 33.32  ? 50  TRP   B CD2 1 
ATOM   978  N  NE1 A TRP   B 2 41  ? 4.451   24.136 -2.292  0.13 35.76  ? 50  TRP   B NE1 1 
ATOM   979  N  NE1 B TRP   B 2 41  ? 6.253   25.149 -2.789  0.14 32.92  ? 50  TRP   B NE1 1 
ATOM   980  N  NE1 C TRP   B 2 41  ? 4.187   24.550 -2.513  0.36 35.53  ? 50  TRP   B NE1 1 
ATOM   981  N  NE1 D TRP   B 2 41  ? 6.256   25.146 -2.788  0.37 32.41  ? 50  TRP   B NE1 1 
ATOM   982  C  CE2 A TRP   B 2 41  ? 5.579   24.895 -2.466  0.13 35.74  ? 50  TRP   B CE2 1 
ATOM   983  C  CE2 B TRP   B 2 41  ? 4.954   24.889 -2.442  0.14 33.33  ? 50  TRP   B CE2 1 
ATOM   984  C  CE2 C TRP   B 2 41  ? 5.423   25.137 -2.546  0.36 35.62  ? 50  TRP   B CE2 1 
ATOM   985  C  CE2 D TRP   B 2 41  ? 4.953   24.894 -2.446  0.37 33.30  ? 50  TRP   B CE2 1 
ATOM   986  C  CE3 A TRP   B 2 41  ? 7.296   25.206 -4.140  0.13 35.89  ? 50  TRP   B CE3 1 
ATOM   987  C  CE3 B TRP   B 2 41  ? 3.100   23.568 -3.260  0.14 33.43  ? 50  TRP   B CE3 1 
ATOM   988  C  CE3 C TRP   B 2 41  ? 7.378   25.124 -3.962  0.36 36.02  ? 50  TRP   B CE3 1 
ATOM   989  C  CE3 D TRP   B 2 41  ? 3.103   23.563 -3.256  0.37 33.50  ? 50  TRP   B CE3 1 
ATOM   990  C  CZ2 A TRP   B 2 41  ? 6.162   25.845 -1.628  0.13 36.20  ? 50  TRP   B CZ2 1 
ATOM   991  C  CZ2 B TRP   B 2 41  ? 4.208   25.328 -1.347  0.14 33.45  ? 50  TRP   B CZ2 1 
ATOM   992  C  CZ2 C TRP   B 2 41  ? 6.005   26.057 -1.675  0.36 36.60  ? 50  TRP   B CZ2 1 
ATOM   993  C  CZ2 D TRP   B 2 41  ? 4.206   25.331 -1.350  0.37 33.40  ? 50  TRP   B CZ2 1 
ATOM   994  C  CZ3 A TRP   B 2 41  ? 7.875   26.140 -3.308  0.13 36.07  ? 50  TRP   B CZ3 1 
ATOM   995  C  CZ3 B TRP   B 2 41  ? 2.360   24.019 -2.189  0.14 33.70  ? 50  TRP   B CZ3 1 
ATOM   996  C  CZ3 C TRP   B 2 41  ? 7.961   26.018 -3.090  0.36 36.05  ? 50  TRP   B CZ3 1 
ATOM   997  C  CZ3 D TRP   B 2 41  ? 2.359   24.021 -2.191  0.37 33.92  ? 50  TRP   B CZ3 1 
ATOM   998  C  CH2 A TRP   B 2 41  ? 7.312   26.457 -2.074  0.13 36.24  ? 50  TRP   B CH2 1 
ATOM   999  C  CH2 B TRP   B 2 41  ? 2.911   24.878 -1.236  0.14 33.55  ? 50  TRP   B CH2 1 
ATOM   1000 C  CH2 C TRP   B 2 41  ? 7.277   26.489 -1.974  0.36 36.57  ? 50  TRP   B CH2 1 
ATOM   1001 C  CH2 D TRP   B 2 41  ? 2.908   24.878 -1.233  0.37 33.56  ? 50  TRP   B CH2 1 
ATOM   1002 N  N   . HIS   B 2 42  ? 6.866   24.848 -7.726  1.00 35.56  ? 51  HIS   B N   1 
ATOM   1003 C  CA  . HIS   B 2 42  ? 7.872   25.941 -7.858  1.00 36.18  ? 51  HIS   B CA  1 
ATOM   1004 C  C   . HIS   B 2 42  ? 7.335   27.066 -8.782  1.00 36.90  ? 51  HIS   B C   1 
ATOM   1005 O  O   . HIS   B 2 42  ? 7.780   28.229 -8.652  1.00 37.45  ? 51  HIS   B O   1 
ATOM   1006 C  CB  . HIS   B 2 42  ? 9.198   25.440 -8.380  1.00 38.09  ? 51  HIS   B CB  1 
ATOM   1007 C  CG  . HIS   B 2 42  ? 9.211   25.183 -9.854  1.00 37.52  ? 51  HIS   B CG  1 
ATOM   1008 N  ND1 . HIS   B 2 42  ? 9.126   23.896 -10.324 1.00 38.24  ? 51  HIS   B ND1 1 
ATOM   1009 C  CD2 . HIS   B 2 42  ? 9.352   25.980 -10.957 1.00 39.16  ? 51  HIS   B CD2 1 
ATOM   1010 C  CE1 . HIS   B 2 42  ? 9.235   23.887 -11.652 1.00 39.12  ? 51  HIS   B CE1 1 
ATOM   1011 N  NE2 . HIS   B 2 42  ? 9.357   25.164 -12.068 1.00 39.49  ? 51  HIS   B NE2 1 
ATOM   1012 N  N   . VAL   B 2 43  ? 6.268   26.805 -9.507  1.00 36.08  ? 52  VAL   B N   1 
ATOM   1013 C  CA  . VAL   B 2 43  ? 5.576   27.869 -10.299 1.00 36.68  ? 52  VAL   B CA  1 
ATOM   1014 C  C   . VAL   B 2 43  ? 4.806   28.839 -9.398  1.00 37.35  ? 52  VAL   B C   1 
ATOM   1015 O  O   . VAL   B 2 43  ? 4.937   30.069 -9.611  1.00 37.32  ? 52  VAL   B O   1 
ATOM   1016 C  CB  . VAL   B 2 43  ? 4.664   27.230 -11.353 1.00 36.75  ? 52  VAL   B CB  1 
ATOM   1017 C  CG1 . VAL   B 2 43  ? 3.841   28.301 -12.054 1.00 37.46  ? 52  VAL   B CG1 1 
ATOM   1018 C  CG2 . VAL   B 2 43  ? 5.488   26.406 -12.353 1.00 36.53  ? 52  VAL   B CG2 1 
ATOM   1019 N  N   . THR   B 2 44  ? 4.029   28.342 -8.418  1.00 37.33  ? 53  THR   B N   1 
ATOM   1020 C  CA  . THR   B 2 44  ? 3.107   29.192 -7.624  1.00 38.00  ? 53  THR   B CA  1 
ATOM   1021 C  C   . THR   B 2 44  ? 3.615   29.350 -6.187  1.00 38.46  ? 53  THR   B C   1 
ATOM   1022 O  O   . THR   B 2 44  ? 3.158   30.333 -5.571  1.00 38.11  ? 53  THR   B O   1 
ATOM   1023 C  CB  . THR   B 2 44  ? 1.674   28.647 -7.607  1.00 37.24  ? 53  THR   B CB  1 
ATOM   1024 O  OG1 . THR   B 2 44  ? 1.644   27.399 -6.921  1.00 37.03  ? 53  THR   B OG1 1 
ATOM   1025 C  CG2 . THR   B 2 44  ? 1.101   28.479 -9.000  1.00 37.05  ? 53  THR   B CG2 1 
ATOM   1026 N  N   . LYS   B 2 45  ? 4.539   28.485 -5.748  1.00 40.29  ? 54  LYS   B N   1 
ATOM   1027 C  CA  . LYS   B 2 45  ? 4.949   28.347 -4.318  1.00 46.25  ? 54  LYS   B CA  1 
ATOM   1028 C  C   . LYS   B 2 45  ? 3.689   28.216 -3.446  1.00 43.17  ? 54  LYS   B C   1 
ATOM   1029 O  O   . LYS   B 2 45  ? 3.722   28.671 -2.278  1.00 42.83  ? 54  LYS   B O   1 
ATOM   1030 C  CB  . LYS   B 2 45  ? 5.774   29.534 -3.806  1.00 51.65  ? 54  LYS   B CB  1 
ATOM   1031 C  CG  . LYS   B 2 45  ? 6.734   30.164 -4.797  1.00 56.43  ? 54  LYS   B CG  1 
ATOM   1032 C  CD  . LYS   B 2 45  ? 8.070   29.512 -4.860  1.00 60.49  ? 54  LYS   B CD  1 
ATOM   1033 C  CE  . LYS   B 2 45  ? 9.058   30.392 -5.597  1.00 64.18  ? 54  LYS   B CE  1 
ATOM   1034 N  NZ  . LYS   B 2 45  ? 9.752   29.625 -6.653  1.00 67.88  ? 54  LYS   B NZ  1 
ATOM   1035 N  N   . GLY   B 2 46  ? 2.602   27.648 -3.988  1.00 41.74  ? 55  GLY   B N   1 
ATOM   1036 C  CA  . GLY   B 2 46  ? 1.328   27.372 -3.291  1.00 42.22  ? 55  GLY   B CA  1 
ATOM   1037 C  C   . GLY   B 2 46  ? 0.417   28.577 -3.186  1.00 42.96  ? 55  GLY   B C   1 
ATOM   1038 O  O   . GLY   B 2 46  ? -0.588  28.512 -2.391  1.00 42.13  ? 55  GLY   B O   1 
ATOM   1039 N  N   . ALA   B 2 47  ? 0.748   29.706 -3.811  1.00 41.15  ? 56  ALA   B N   1 
ATOM   1040 C  CA  . ALA   B 2 47  ? -0.072  30.937 -3.741  1.00 42.93  ? 56  ALA   B CA  1 
ATOM   1041 C  C   . ALA   B 2 47  ? -1.433  30.720 -4.419  1.00 44.27  ? 56  ALA   B C   1 
ATOM   1042 O  O   . ALA   B 2 47  ? -1.538  29.811 -5.243  1.00 42.95  ? 56  ALA   B O   1 
ATOM   1043 C  CB  . ALA   B 2 47  ? 0.639   32.087 -4.390  1.00 44.57  ? 56  ALA   B CB  1 
ATOM   1044 N  N   . ALA   B 2 48  ? -2.450  31.501 -4.034  1.00 43.85  ? 57  ALA   B N   1 
ATOM   1045 C  CA  . ALA   B 2 48  ? -3.756  31.617 -4.720  1.00 43.04  ? 57  ALA   B CA  1 
ATOM   1046 C  C   . ALA   B 2 48  ? -3.590  32.196 -6.130  1.00 44.09  ? 57  ALA   B C   1 
ATOM   1047 O  O   . ALA   B 2 48  ? -2.651  32.986 -6.354  1.00 46.37  ? 57  ALA   B O   1 
ATOM   1048 C  CB  . ALA   B 2 48  ? -4.714  32.486 -3.921  1.00 42.86  ? 57  ALA   B CB  1 
ATOM   1049 N  N   . LEU   B 2 49  ? -4.522  31.857 -7.023  1.00 44.59  ? 58  LEU   B N   1 
ATOM   1050 C  CA  . LEU   B 2 49  ? -4.519  32.221 -8.479  1.00 46.06  ? 58  LEU   B CA  1 
ATOM   1051 C  C   . LEU   B 2 49  ? -5.834  32.928 -8.831  1.00 47.34  ? 58  LEU   B C   1 
ATOM   1052 O  O   . LEU   B 2 49  ? -6.912  32.549 -8.298  1.00 49.71  ? 58  LEU   B O   1 
ATOM   1053 C  CB  . LEU   B 2 49  ? -4.396  30.962 -9.339  1.00 44.38  ? 58  LEU   B CB  1 
ATOM   1054 C  CG  . LEU   B 2 49  ? -3.124  30.137 -9.167  1.00 43.73  ? 58  LEU   B CG  1 
ATOM   1055 C  CD1 . LEU   B 2 49  ? -3.142  28.914 -10.044 1.00 44.41  ? 58  LEU   B CD1 1 
ATOM   1056 C  CD2 . LEU   B 2 49  ? -1.874  30.953 -9.452  1.00 44.75  ? 58  LEU   B CD2 1 
ATOM   1057 N  N   . ARG   B 2 50  ? -5.770  33.941 -9.681  1.00 48.36  ? 59  ARG   B N   1 
ATOM   1058 C  CA  . ARG   B 2 50  ? -6.982  34.590 -10.227 1.00 51.44  ? 59  ARG   B CA  1 
ATOM   1059 C  C   . ARG   B 2 50  ? -7.334  33.945 -11.577 1.00 51.85  ? 59  ARG   B C   1 
ATOM   1060 O  O   . ARG   B 2 50  ? -6.393  33.548 -12.344 1.00 46.98  ? 59  ARG   B O   1 
ATOM   1061 C  CB  . ARG   B 2 50  ? -6.706  36.092 -10.260 1.00 57.12  ? 59  ARG   B CB  1 
ATOM   1062 C  CG  . ARG   B 2 50  ? -7.788  36.932 -10.917 1.00 61.74  ? 59  ARG   B CG  1 
ATOM   1063 C  CD  . ARG   B 2 50  ? -7.511  38.415 -10.711 1.00 66.99  ? 59  ARG   B CD  1 
ATOM   1064 N  NE  . ARG   B 2 50  ? -6.103  38.809 -10.873 1.00 70.38  ? 59  ARG   B NE  1 
ATOM   1065 C  CZ  . ARG   B 2 50  ? -5.498  39.102 -12.034 1.00 72.61  ? 59  ARG   B CZ  1 
ATOM   1066 N  NH1 . ARG   B 2 50  ? -6.152  39.024 -13.185 1.00 74.43  ? 59  ARG   B NH1 1 
ATOM   1067 N  NH2 . ARG   B 2 50  ? -4.224  39.467 -12.041 1.00 73.19  ? 59  ARG   B NH2 1 
ATOM   1068 N  N   . SER   B 2 51  ? -8.622  33.743 -11.842 1.00 52.89  ? 60  SER   B N   1 
ATOM   1069 C  CA  . SER   B 2 51  ? -9.132  33.409 -13.206 1.00 57.13  ? 60  SER   B CA  1 
ATOM   1070 C  C   . SER   B 2 51  ? -10.388 34.231 -13.534 1.00 60.57  ? 60  SER   B C   1 
ATOM   1071 O  O   . SER   B 2 51  ? -11.517 33.768 -13.245 1.00 59.28  ? 60  SER   B O   1 
ATOM   1072 C  CB  . SER   B 2 51  ? -9.417  31.956 -13.351 1.00 55.64  ? 60  SER   B CB  1 
ATOM   1073 O  OG  . SER   B 2 51  ? -10.121 31.764 -14.570 1.00 59.40  ? 60  SER   B OG  1 
ATOM   1074 N  N   . GLY   B 2 52  ? -10.215 35.413 -14.127 1.00 66.49  ? 61  GLY   B N   1 
ATOM   1075 C  CA  . GLY   B 2 52  ? -11.286 36.432 -14.186 1.00 70.73  ? 61  GLY   B CA  1 
ATOM   1076 C  C   . GLY   B 2 52  ? -11.331 37.187 -12.877 1.00 72.45  ? 61  GLY   B C   1 
ATOM   1077 O  O   . GLY   B 2 52  ? -10.253 37.600 -12.424 1.00 72.07  ? 61  GLY   B O   1 
ATOM   1078 N  N   . GLU   B 2 53  ? -12.511 37.355 -12.271 1.00 78.94  ? 62  GLU   B N   1 
ATOM   1079 C  CA  . GLU   B 2 53  ? -12.607 37.706 -10.824 1.00 80.81  ? 62  GLU   B CA  1 
ATOM   1080 C  C   . GLU   B 2 53  ? -12.770 36.426 -9.999  1.00 74.30  ? 62  GLU   B C   1 
ATOM   1081 O  O   . GLU   B 2 53  ? -12.900 36.544 -8.775  1.00 80.82  ? 62  GLU   B O   1 
ATOM   1082 C  CB  . GLU   B 2 53  ? -13.711 38.724 -10.529 1.00 88.61  ? 62  GLU   B CB  1 
ATOM   1083 C  CG  . GLU   B 2 53  ? -13.146 40.092 -10.164 1.00 93.92  ? 62  GLU   B CG  1 
ATOM   1084 C  CD  . GLU   B 2 53  ? -14.161 41.155 -9.779  1.00 98.83  ? 62  GLU   B CD  1 
ATOM   1085 O  OE1 . GLU   B 2 53  ? -15.087 40.836 -9.006  1.00 104.28 ? 62  GLU   B OE1 1 
ATOM   1086 O  OE2 . GLU   B 2 53  ? -14.014 42.308 -10.243 1.00 101.70 ? 62  GLU   B OE2 1 
ATOM   1087 N  N   . GLY   B 2 54  ? -12.750 35.256 -10.643 1.00 66.07  ? 63  GLY   B N   1 
ATOM   1088 C  CA  . GLY   B 2 54  ? -12.636 33.952 -9.976  1.00 60.42  ? 63  GLY   B CA  1 
ATOM   1089 C  C   . GLY   B 2 54  ? -11.328 33.886 -9.220  1.00 57.73  ? 63  GLY   B C   1 
ATOM   1090 O  O   . GLY   B 2 54  ? -10.364 34.523 -9.663  1.00 56.38  ? 63  GLY   B O   1 
ATOM   1091 N  N   . ARG   B 2 55  ? -11.314 33.165 -8.102  1.00 54.31  ? 64  ARG   B N   1 
ATOM   1092 C  CA  . ARG   B 2 55  ? -10.100 32.846 -7.313  1.00 54.56  ? 64  ARG   B CA  1 
ATOM   1093 C  C   . ARG   B 2 55  ? -9.960  31.322 -7.296  1.00 53.38  ? 64  ARG   B C   1 
ATOM   1094 O  O   . ARG   B 2 55  ? -10.996 30.627 -7.251  1.00 55.25  ? 64  ARG   B O   1 
ATOM   1095 C  CB  . ARG   B 2 55  ? -10.235 33.401 -5.897  1.00 57.49  ? 64  ARG   B CB  1 
ATOM   1096 C  CG  . ARG   B 2 55  ? -8.989  33.327 -5.025  1.00 58.66  ? 64  ARG   B CG  1 
ATOM   1097 C  CD  . ARG   B 2 55  ? -9.361  33.796 -3.620  1.00 61.58  ? 64  ARG   B CD  1 
ATOM   1098 N  NE  . ARG   B 2 55  ? -8.437  33.285 -2.616  1.00 64.25  ? 64  ARG   B NE  1 
ATOM   1099 C  CZ  . ARG   B 2 55  ? -7.559  34.000 -1.907  1.00 70.77  ? 64  ARG   B CZ  1 
ATOM   1100 N  NH1 . ARG   B 2 55  ? -7.478  35.311 -2.038  1.00 74.40  ? 64  ARG   B NH1 1 
ATOM   1101 N  NH2 . ARG   B 2 55  ? -6.770  33.402 -1.027  1.00 73.36  ? 64  ARG   B NH2 1 
ATOM   1102 N  N   . LEU   B 2 56  ? -8.739  30.807 -7.400  1.00 49.65  ? 65  LEU   B N   1 
ATOM   1103 C  CA  . LEU   B 2 56  ? -8.470  29.361 -7.275  1.00 45.22  ? 65  LEU   B CA  1 
ATOM   1104 C  C   . LEU   B 2 56  ? -7.618  29.227 -6.028  1.00 42.41  ? 65  LEU   B C   1 
ATOM   1105 O  O   . LEU   B 2 56  ? -6.607  29.955 -5.960  1.00 41.69  ? 65  LEU   B O   1 
ATOM   1106 C  CB  . LEU   B 2 56  ? -7.697  28.846 -8.498  1.00 45.02  ? 65  LEU   B CB  1 
ATOM   1107 C  CG  . LEU   B 2 56  ? -8.322  29.036 -9.894  1.00 46.37  ? 65  LEU   B CG  1 
ATOM   1108 C  CD1 . LEU   B 2 56  ? -7.383  28.499 -10.916 1.00 46.80  ? 65  LEU   B CD1 1 
ATOM   1109 C  CD2 . LEU   B 2 56  ? -9.655  28.325 -10.017 1.00 47.52  ? 65  LEU   B CD2 1 
ATOM   1110 N  N   . ASP   B 2 57  ? -8.067  28.431 -5.052  1.00 39.76  ? 66  ASP   B N   1 
ATOM   1111 C  CA  . ASP   B 2 57  ? -7.278  28.204 -3.826  1.00 39.79  ? 66  ASP   B CA  1 
ATOM   1112 C  C   . ASP   B 2 57  ? -6.602  26.857 -3.861  1.00 35.51  ? 66  ASP   B C   1 
ATOM   1113 O  O   . ASP   B 2 57  ? -7.174  25.885 -4.311  1.00 35.82  ? 66  ASP   B O   1 
ATOM   1114 C  CB  . ASP   B 2 57  ? -8.164  28.347 -2.577  1.00 41.79  ? 66  ASP   B CB  1 
ATOM   1115 C  CG  . ASP   B 2 57  ? -8.607  29.780 -2.395  1.00 44.80  ? 66  ASP   B CG  1 
ATOM   1116 O  OD1 . ASP   B 2 57  ? -7.741  30.671 -2.531  1.00 46.96  ? 66  ASP   B OD1 1 
ATOM   1117 O  OD2 . ASP   B 2 57  ? -9.801  30.001 -2.076  1.00 50.13  ? 66  ASP   B OD2 1 
ATOM   1118 N  N   . PRO   B 2 58  ? -5.394  26.751 -3.302  1.00 34.80  ? 67  PRO   B N   1 
ATOM   1119 C  CA  . PRO   B 2 58  ? -4.672  25.475 -3.282  1.00 34.30  ? 67  PRO   B CA  1 
ATOM   1120 C  C   . PRO   B 2 58  ? -5.467  24.462 -2.463  1.00 34.88  ? 67  PRO   B C   1 
ATOM   1121 O  O   . PRO   B 2 58  ? -6.118  24.897 -1.487  1.00 35.05  ? 67  PRO   B O   1 
ATOM   1122 C  CB  . PRO   B 2 58  ? -3.300  25.812 -2.703  1.00 33.85  ? 67  PRO   B CB  1 
ATOM   1123 C  CG  . PRO   B 2 58  ? -3.486  27.147 -2.037  1.00 35.52  ? 67  PRO   B CG  1 
ATOM   1124 C  CD  . PRO   B 2 58  ? -4.635  27.853 -2.709  1.00 35.31  ? 67  PRO   B CD  1 
ATOM   1125 N  N   . TYR   B 2 59  ? -5.420  23.198 -2.863  1.00 33.50  ? 68  TYR   B N   1 
ATOM   1126 C  CA  . TYR   B 2 59  ? -6.092  22.065 -2.178  1.00 33.06  ? 68  TYR   B CA  1 
ATOM   1127 C  C   . TYR   B 2 59  ? -5.071  21.030 -1.692  1.00 32.68  ? 68  TYR   B C   1 
ATOM   1128 O  O   . TYR   B 2 59  ? -5.257  20.444 -0.539  1.00 31.58  ? 68  TYR   B O   1 
ATOM   1129 C  CB  . TYR   B 2 59  ? -7.132  21.456 -3.111  1.00 33.13  ? 68  TYR   B CB  1 
ATOM   1130 C  CG  . TYR   B 2 59  ? -7.938  20.314 -2.559  1.00 32.98  ? 68  TYR   B CG  1 
ATOM   1131 C  CD1 . TYR   B 2 59  ? -7.391  19.043 -2.445  1.00 33.39  ? 68  TYR   B CD1 1 
ATOM   1132 C  CD2 . TYR   B 2 59  ? -9.221  20.510 -2.053  1.00 32.89  ? 68  TYR   B CD2 1 
ATOM   1133 C  CE1 . TYR   B 2 59  ? -8.135  17.982 -1.939  1.00 32.58  ? 68  TYR   B CE1 1 
ATOM   1134 C  CE2 . TYR   B 2 59  ? -10.011 19.447 -1.638  1.00 32.79  ? 68  TYR   B CE2 1 
ATOM   1135 C  CZ  . TYR   B 2 59  ? -9.456  18.183 -1.568  1.00 33.11  ? 68  TYR   B CZ  1 
ATOM   1136 O  OH  . TYR   B 2 59  ? -10.217 17.135 -1.094  1.00 33.35  ? 68  TYR   B OH  1 
ATOM   1137 N  N   . TRP   B 2 60  ? -4.109  20.681 -2.530  1.00 32.22  ? 69  TRP   B N   1 
ATOM   1138 C  CA  . TRP   B 2 60  ? -3.065  19.658 -2.253  1.00 31.79  ? 69  TRP   B CA  1 
ATOM   1139 C  C   . TRP   B 2 60  ? -1.760  20.169 -2.789  1.00 32.21  ? 69  TRP   B C   1 
ATOM   1140 O  O   . TRP   B 2 60  ? -1.794  20.803 -3.883  1.00 31.51  ? 69  TRP   B O   1 
ATOM   1141 C  CB  . TRP   B 2 60  ? -3.432  18.257 -2.770  1.00 31.14  ? 69  TRP   B CB  1 
ATOM   1142 C  CG  . TRP   B 2 60  ? -2.291  17.287 -2.674  1.00 30.71  ? 69  TRP   B CG  1 
ATOM   1143 C  CD1 . TRP   B 2 60  ? -1.918  16.534 -1.598  1.00 30.47  ? 69  TRP   B CD1 1 
ATOM   1144 C  CD2 . TRP   B 2 60  ? -1.281  17.026 -3.682  1.00 30.33  ? 69  TRP   B CD2 1 
ATOM   1145 N  NE1 . TRP   B 2 60  ? -0.787  15.812 -1.836  1.00 30.39  ? 69  TRP   B NE1 1 
ATOM   1146 C  CE2 . TRP   B 2 60  ? -0.384  16.076 -3.153  1.00 30.69  ? 69  TRP   B CE2 1 
ATOM   1147 C  CE3 . TRP   B 2 60  ? -1.096  17.440 -5.015  1.00 30.93  ? 69  TRP   B CE3 1 
ATOM   1148 C  CZ2 . TRP   B 2 60  ? 0.702   15.583 -3.858  1.00 30.25  ? 69  TRP   B CZ2 1 
ATOM   1149 C  CZ3 . TRP   B 2 60  ? -0.029  16.922 -5.719  1.00 30.25  ? 69  TRP   B CZ3 1 
ATOM   1150 C  CH2 . TRP   B 2 60  ? 0.863   16.005 -5.185  1.00 30.93  ? 69  TRP   B CH2 1 
ATOM   1151 N  N   . GLY   B 2 61  ? -0.642  19.829 -2.145  1.00 32.11  ? 70  GLY   B N   1 
ATOM   1152 C  CA  . GLY   B 2 61  ? 0.709   20.064 -2.692  1.00 31.72  ? 70  GLY   B CA  1 
ATOM   1153 C  C   . GLY   B 2 61  ? 1.802   19.339 -1.938  1.00 32.97  ? 70  GLY   B C   1 
ATOM   1154 O  O   . GLY   B 2 61  ? 1.599   18.945 -0.681  1.00 31.21  ? 70  GLY   B O   1 
ATOM   1155 N  N   . ASP   B 2 62  ? 2.908   19.101 -2.603  1.00 32.52  ? 71  ASP   B N   1 
ATOM   1156 C  CA  . ASP   B 2 62  ? 4.101   18.449 -1.989  1.00 32.21  ? 71  ASP   B CA  1 
ATOM   1157 C  C   . ASP   B 2 62  ? 5.373   18.999 -2.622  1.00 34.63  ? 71  ASP   B C   1 
ATOM   1158 O  O   . ASP   B 2 62  ? 5.539   18.831 -3.914  1.00 32.80  ? 71  ASP   B O   1 
ATOM   1159 C  CB  . ASP   B 2 62  ? 3.902   16.960 -2.142  1.00 32.82  ? 71  ASP   B CB  1 
ATOM   1160 C  CG  . ASP   B 2 62  ? 4.988   16.152 -1.517  1.00 34.56  ? 71  ASP   B CG  1 
ATOM   1161 O  OD1 . ASP   B 2 62  ? 6.104   16.255 -1.933  1.00 37.59  ? 71  ASP   B OD1 1 
ATOM   1162 O  OD2 . ASP   B 2 62  ? 4.692   15.724 -0.374  1.00 40.08  ? 71  ASP   B OD2 1 
ATOM   1163 N  N   . VAL   B 2 63  ? 6.237   19.649 -1.850  1.00 33.37  ? 72  VAL   B N   1 
ATOM   1164 C  CA  . VAL   B 2 63  ? 7.478   20.286 -2.382  1.00 34.05  ? 72  VAL   B CA  1 
ATOM   1165 C  C   . VAL   B 2 63  ? 8.373   19.203 -2.998  1.00 34.26  ? 72  VAL   B C   1 
ATOM   1166 O  O   . VAL   B 2 63  ? 9.005   19.502 -4.039  1.00 34.09  ? 72  VAL   B O   1 
ATOM   1167 C  CB  . VAL   B 2 63  ? 8.217   21.108 -1.302  1.00 33.17  ? 72  VAL   B CB  1 
ATOM   1168 C  CG1 . VAL   B 2 63  ? 9.683   21.289 -1.605  1.00 33.34  ? 72  VAL   B CG1 1 
ATOM   1169 C  CG2 . VAL   B 2 63  ? 7.561   22.466 -1.095  1.00 33.28  ? 72  VAL   B CG2 1 
ATOM   1170 N  N   . LYS   B 2 64  ? 8.405   17.967 -2.474  1.00 33.88  ? 73  LYS   B N   1 
ATOM   1171 C  CA  . LYS   B 2 64  ? 9.435   16.986 -2.903  1.00 35.81  ? 73  LYS   B CA  1 
ATOM   1172 C  C   . LYS   B 2 64  ? 9.042   16.496 -4.317  1.00 34.81  ? 73  LYS   B C   1 
ATOM   1173 O  O   . LYS   B 2 64  ? 9.932   16.334 -5.227  1.00 36.21  ? 73  LYS   B O   1 
ATOM   1174 C  CB  . LYS   B 2 64  ? 9.546   15.755 -2.014  1.00 36.05  ? 73  LYS   B CB  1 
ATOM   1175 C  CG  . LYS   B 2 64  ? 10.682  14.839 -2.427  1.00 36.65  ? 73  LYS   B CG  1 
ATOM   1176 C  CD  . LYS   B 2 64  ? 11.177  13.919 -1.414  1.00 38.09  ? 73  LYS   B CD  1 
ATOM   1177 C  CE  . LYS   B 2 64  ? 12.256  13.000 -1.914  1.00 39.79  ? 73  LYS   B CE  1 
ATOM   1178 N  NZ  . LYS   B 2 64  ? 12.533  11.935 -0.900  1.00 39.63  ? 73  LYS   B NZ  1 
ATOM   1179 N  N   . GLN   B 2 65  ? 7.755   16.240 -4.476  1.00 34.88  ? 74  GLN   B N   1 
ATOM   1180 C  CA  . GLN   B 2 65  ? 7.172   15.885 -5.803  1.00 35.12  ? 74  GLN   B CA  1 
ATOM   1181 C  C   . GLN   B 2 65  ? 7.129   17.103 -6.708  1.00 35.97  ? 74  GLN   B C   1 
ATOM   1182 O  O   . GLN   B 2 65  ? 7.073   16.878 -7.959  1.00 33.30  ? 74  GLN   B O   1 
ATOM   1183 C  CB  . GLN   B 2 65  ? 5.768   15.322 -5.721  1.00 37.12  ? 74  GLN   B CB  1 
ATOM   1184 C  CG  . GLN   B 2 65  ? 5.651   14.056 -4.862  1.00 39.07  ? 74  GLN   B CG  1 
ATOM   1185 C  CD  . GLN   B 2 65  ? 4.202   13.617 -4.808  1.00 41.06  ? 74  GLN   B CD  1 
ATOM   1186 O  OE1 . GLN   B 2 65  ? 3.507   13.540 -5.840  1.00 42.47  ? 74  GLN   B OE1 1 
ATOM   1187 N  NE2 . GLN   B 2 65  ? 3.691   13.400 -3.612  1.00 42.45  ? 74  GLN   B NE2 1 
ATOM   1188 N  N   . ASP   B 2 66  ? 7.178   18.323 -6.183  1.00 34.16  ? 75  ASP   B N   1 
ATOM   1189 C  CA  . ASP   B 2 66  ? 7.077   19.588 -6.957  1.00 35.01  ? 75  ASP   B CA  1 
ATOM   1190 C  C   . ASP   B 2 66  ? 5.744   19.642 -7.717  1.00 34.29  ? 75  ASP   B C   1 
ATOM   1191 O  O   . ASP   B 2 66  ? 5.723   20.121 -8.914  1.00 34.21  ? 75  ASP   B O   1 
ATOM   1192 C  CB  . ASP   B 2 66  ? 8.268   19.760 -7.907  1.00 34.44  ? 75  ASP   B CB  1 
ATOM   1193 C  CG  . ASP   B 2 66  ? 8.434   21.203 -8.366  1.00 35.47  ? 75  ASP   B CG  1 
ATOM   1194 O  OD1 . ASP   B 2 66  ? 7.943   22.097 -7.694  1.00 33.88  ? 75  ASP   B OD1 1 
ATOM   1195 O  OD2 . ASP   B 2 66  ? 8.983   21.426 -9.506  1.00 34.64  ? 75  ASP   B OD2 1 
ATOM   1196 N  N   . LEU   B 2 67  ? 4.635   19.294 -7.043  1.00 32.28  ? 76  LEU   B N   1 
ATOM   1197 C  CA  . LEU   B 2 67  ? 3.268   19.355 -7.592  1.00 31.70  ? 76  LEU   B CA  1 
ATOM   1198 C  C   . LEU   B 2 67  ? 2.340   20.129 -6.685  1.00 32.02  ? 76  LEU   B C   1 
ATOM   1199 O  O   . LEU   B 2 67  ? 2.528   20.059 -5.420  1.00 30.90  ? 76  LEU   B O   1 
ATOM   1200 C  CB  . LEU   B 2 67  ? 2.758   17.946 -7.903  1.00 31.26  ? 76  LEU   B CB  1 
ATOM   1201 C  CG  . LEU   B 2 67  ? 3.473   17.198 -9.046  1.00 30.35  ? 76  LEU   B CG  1 
ATOM   1202 C  CD1 . LEU   B 2 67  ? 2.878   15.815 -9.162  1.00 30.40  ? 76  LEU   B CD1 1 
ATOM   1203 C  CD2 . LEU   B 2 67  ? 3.301   17.929 -10.434 1.00 31.33  ? 76  LEU   B CD2 1 
ATOM   1204 N  N   . VAL   B 2 68  ? 1.279   20.684 -7.254  1.00 32.02  ? 77  VAL   B N   1 
ATOM   1205 C  CA  . VAL   B 2 68  ? 0.194   21.396 -6.525  1.00 32.24  ? 77  VAL   B CA  1 
ATOM   1206 C  C   . VAL   B 2 68  ? -1.120  21.288 -7.291  1.00 33.54  ? 77  VAL   B C   1 
ATOM   1207 O  O   . VAL   B 2 68  ? -1.086  21.416 -8.597  1.00 31.70  ? 77  VAL   B O   1 
ATOM   1208 C  CB  . VAL   B 2 68  ? 0.630   22.843 -6.218  1.00 32.97  ? 77  VAL   B CB  1 
ATOM   1209 C  CG1 . VAL   B 2 68  ? 0.957   23.691 -7.468  1.00 32.75  ? 77  VAL   B CG1 1 
ATOM   1210 C  CG2 . VAL   B 2 68  ? -0.380  23.543 -5.310  1.00 33.47  ? 77  VAL   B CG2 1 
ATOM   1211 N  N   . SER   B 2 69  ? -2.243  21.057 -6.613  1.00 32.70  ? 78  SER   B N   1 
ATOM   1212 C  CA  . SER   B 2 69  ? -3.603  21.117 -7.224  1.00 30.59  ? 78  SER   B CA  1 
ATOM   1213 C  C   . SER   B 2 69  ? -4.381  22.253 -6.574  1.00 32.93  ? 78  SER   B C   1 
ATOM   1214 O  O   . SER   B 2 69  ? -4.221  22.474 -5.262  1.00 30.96  ? 78  SER   B O   1 
ATOM   1215 C  CB  . SER   B 2 69  ? -4.321  19.773 -7.157  1.00 30.58  ? 78  SER   B CB  1 
ATOM   1216 O  OG  . SER   B 2 69  ? -4.693  19.360 -5.792  1.00 31.24  ? 78  SER   B OG  1 
ATOM   1217 N  N   . TYR   B 2 70  ? -5.330  22.805 -7.290  1.00 31.70  ? 79  TYR   B N   1 
ATOM   1218 C  CA  . TYR   B 2 70  ? -6.230  23.918 -6.922  1.00 32.89  ? 79  TYR   B CA  1 
ATOM   1219 C  C   . TYR   B 2 70  ? -7.681  23.473 -7.102  1.00 34.11  ? 79  TYR   B C   1 
ATOM   1220 O  O   . TYR   B 2 70  ? -8.025  22.720 -8.075  1.00 33.20  ? 79  TYR   B O   1 
ATOM   1221 C  CB  . TYR   B 2 70  ? -5.946  25.206 -7.703  1.00 33.17  ? 79  TYR   B CB  1 
ATOM   1222 C  CG  . TYR   B 2 70  ? -4.631  25.866 -7.378  1.00 33.23  ? 79  TYR   B CG  1 
ATOM   1223 C  CD1 . TYR   B 2 70  ? -3.426  25.387 -7.878  1.00 32.74  ? 79  TYR   B CD1 1 
ATOM   1224 C  CD2 . TYR   B 2 70  ? -4.592  27.015 -6.604  1.00 34.01  ? 79  TYR   B CD2 1 
ATOM   1225 C  CE1 . TYR   B 2 70  ? -2.218  25.991 -7.570  1.00 33.29  ? 79  TYR   B CE1 1 
ATOM   1226 C  CE2 . TYR   B 2 70  ? -3.403  27.674 -6.346  1.00 33.94  ? 79  TYR   B CE2 1 
ATOM   1227 C  CZ  . TYR   B 2 70  ? -2.206  27.113 -6.748  1.00 33.93  ? 79  TYR   B CZ  1 
ATOM   1228 O  OH  . TYR   B 2 70  ? -1.022  27.731 -6.479  1.00 34.54  ? 79  TYR   B OH  1 
ATOM   1229 N  N   . CYS   B 2 71  ? -8.531  23.766 -6.072  1.00 34.97  ? 80  CYS   B N   1 
ATOM   1230 C  CA  . CYS   B 2 71  ? -10.010 23.580 -6.103  1.00 35.73  ? 80  CYS   B CA  1 
ATOM   1231 C  C   . CYS   B 2 71  ? -10.361 22.111 -5.885  1.00 35.22  ? 80  CYS   B C   1 
ATOM   1232 O  O   . CYS   B 2 71  ? -11.571 21.788 -5.748  1.00 35.40  ? 80  CYS   B O   1 
ATOM   1233 C  CB  . CYS   B 2 71  ? -10.709 24.017 -7.389  1.00 37.61  ? 80  CYS   B CB  1 
ATOM   1234 S  SG  . CYS   B 2 71  ? -10.130 25.629 -7.976  1.00 41.48  ? 80  CYS   B SG  1 
ATOM   1235 N  N   . GLY   B 2 72  ? -9.380  21.234 -5.764  1.00 33.76  ? 81  GLY   B N   1 
ATOM   1236 C  CA  . GLY   B 2 72  ? -9.752  19.824 -5.729  1.00 33.75  ? 81  GLY   B CA  1 
ATOM   1237 C  C   . GLY   B 2 72  ? -8.521  18.959 -5.689  1.00 33.02  ? 81  GLY   B C   1 
ATOM   1238 O  O   . GLY   B 2 72  ? -7.399  19.439 -5.836  1.00 33.32  ? 81  GLY   B O   1 
ATOM   1239 N  N   . PRO   B 2 73  ? -8.728  17.652 -5.455  1.00 34.10  ? 82  PRO   B N   1 
ATOM   1240 C  CA  . PRO   B 2 73  ? -7.636  16.688 -5.436  1.00 34.14  ? 82  PRO   B CA  1 
ATOM   1241 C  C   . PRO   B 2 73  ? -7.013  16.423 -6.802  1.00 35.61  ? 82  PRO   B C   1 
ATOM   1242 O  O   . PRO   B 2 73  ? -7.765  16.621 -7.797  1.00 34.79  ? 82  PRO   B O   1 
ATOM   1243 C  CB  . PRO   B 2 73  ? -8.273  15.387 -4.940  1.00 34.70  ? 82  PRO   B CB  1 
ATOM   1244 C  CG  . PRO   B 2 73  ? -9.744  15.539 -5.149  1.00 34.44  ? 82  PRO   B CG  1 
ATOM   1245 C  CD  . PRO   B 2 73  ? -10.031 17.020 -5.200  1.00 34.43  ? 82  PRO   B CD  1 
ATOM   1246 N  N   . TRP   B 2 74  ? -5.767  15.954 -6.799  1.00 35.54  ? 83  TRP   B N   1 
ATOM   1247 C  CA  . TRP   B 2 74  ? -5.031  15.692 -8.049  1.00 35.09  ? 83  TRP   B CA  1 
ATOM   1248 C  C   . TRP   B 2 74  ? -5.861  14.726 -8.901  1.00 36.48  ? 83  TRP   B C   1 
ATOM   1249 O  O   . TRP   B 2 74  ? -6.187  13.643 -8.410  1.00 35.67  ? 83  TRP   B O   1 
ATOM   1250 C  CB  . TRP   B 2 74  ? -3.623  15.160 -7.799  1.00 34.61  ? 83  TRP   B CB  1 
ATOM   1251 C  CG  . TRP   B 2 74  ? -2.777  15.022 -9.041  1.00 33.48  ? 83  TRP   B CG  1 
ATOM   1252 C  CD1 . TRP   B 2 74  ? -2.672  13.929 -9.858  1.00 33.32  ? 83  TRP   B CD1 1 
ATOM   1253 C  CD2 . TRP   B 2 74  ? -1.834  15.979 -9.538  1.00 32.30  ? 83  TRP   B CD2 1 
ATOM   1254 N  NE1 . TRP   B 2 74  ? -1.744  14.148 -10.838 1.00 32.56  ? 83  TRP   B NE1 1 
ATOM   1255 C  CE2 . TRP   B 2 74  ? -1.284  15.430 -10.726 1.00 32.62  ? 83  TRP   B CE2 1 
ATOM   1256 C  CE3 . TRP   B 2 74  ? -1.549  17.308 -9.241  1.00 32.08  ? 83  TRP   B CE3 1 
ATOM   1257 C  CZ2 . TRP   B 2 74  ? -0.316  16.120 -11.438 1.00 32.40  ? 83  TRP   B CZ2 1 
ATOM   1258 C  CZ3 . TRP   B 2 74  ? -0.616  18.002 -9.961  1.00 32.79  ? 83  TRP   B CZ3 1 
ATOM   1259 C  CH2 . TRP   B 2 74  ? -0.019  17.402 -11.080 1.00 32.96  ? 83  TRP   B CH2 1 
ATOM   1260 N  N   . LYS   B 2 75  ? -6.077  15.025 -10.208 1.00 37.30  ? 84  LYS   B N   1 
ATOM   1261 C  CA  . LYS   B 2 75  ? -6.979  14.152 -11.015 1.00 37.97  ? 84  LYS   B CA  1 
ATOM   1262 C  C   . LYS   B 2 75  ? -6.231  13.354 -12.106 1.00 40.14  ? 84  LYS   B C   1 
ATOM   1263 O  O   . LYS   B 2 75  ? -6.886  12.460 -12.678 1.00 40.79  ? 84  LYS   B O   1 
ATOM   1264 C  CB  . LYS   B 2 75  ? -8.082  14.980 -11.662 1.00 40.91  ? 84  LYS   B CB  1 
ATOM   1265 C  CG  . LYS   B 2 75  ? -8.933  15.775 -10.697 1.00 40.82  ? 84  LYS   B CG  1 
ATOM   1266 C  CD  . LYS   B 2 75  ? -10.070 14.980 -10.147 1.00 41.67  ? 84  LYS   B CD  1 
ATOM   1267 C  CE  . LYS   B 2 75  ? -10.904 15.898 -9.299  1.00 44.03  ? 84  LYS   B CE  1 
ATOM   1268 N  NZ  . LYS   B 2 75  ? -12.151 15.282 -8.817  1.00 46.28  ? 84  LYS   B NZ  1 
ATOM   1269 N  N   . LEU   B 2 76  ? -4.976  13.674 -12.439 1.00 39.32  ? 85  LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 76  ? -4.279  13.140 -13.660 1.00 41.62  ? 85  LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 76  ? -3.623  11.835 -13.199 1.00 43.16  ? 85  LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 76  ? -2.886  11.859 -12.192 1.00 40.22  ? 85  LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 76  ? -3.261  14.180 -14.138 1.00 40.00  ? 85  LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 76  ? -3.790  15.605 -14.306 1.00 40.11  ? 85  LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 76  ? -2.676  16.580 -14.629 1.00 40.36  ? 85  LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 76  ? -4.890  15.674 -15.334 1.00 41.37  ? 85  LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 77  ? -3.979  10.708 -13.800 1.00 45.04  ? 86  ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 77  ? -3.586  9.369  -13.276 1.00 47.93  ? 86  ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 77  ? -2.948  8.510  -14.377 1.00 47.42  ? 86  ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 77  ? -2.368  7.504  -14.063 1.00 47.59  ? 86  ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 77  ? -4.767  8.670  -12.592 1.00 51.82  ? 86  ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 77  ? -5.871  8.246  -13.534 1.00 57.19  ? 86  ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 77  ? -5.733  8.537  -14.741 1.00 60.74  ? 86  ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 77  ? -6.867  7.664  -13.050 1.00 62.67  ? 86  ASP   B OD2 1 
ATOM   1285 N  N   . ALA   B 2 78  ? -2.983  8.912  -15.639 1.00 44.28  ? 87  ALA   B N   1 
ATOM   1286 C  CA  . ALA   B 2 78  ? -2.311  8.137  -16.708 1.00 45.01  ? 87  ALA   B CA  1 
ATOM   1287 C  C   . ALA   B 2 78  ? -0.786  8.145  -16.535 1.00 44.80  ? 87  ALA   B C   1 
ATOM   1288 O  O   . ALA   B 2 78  ? -0.187  9.171  -16.084 1.00 42.81  ? 87  ALA   B O   1 
ATOM   1289 C  CB  . ALA   B 2 78  ? -2.699  8.707  -18.035 1.00 45.44  ? 87  ALA   B CB  1 
ATOM   1290 N  N   . ALA   B 2 79  ? -0.153  7.097  -17.064 1.00 44.94  ? 88  ALA   B N   1 
ATOM   1291 C  CA  . ALA   B 2 79  ? 1.287   6.823  -16.910 1.00 46.42  ? 88  ALA   B CA  1 
ATOM   1292 C  C   . ALA   B 2 79  ? 1.931   6.552  -18.276 1.00 46.53  ? 88  ALA   B C   1 
ATOM   1293 O  O   . ALA   B 2 79  ? 1.262   5.945  -19.150 1.00 46.91  ? 88  ALA   B O   1 
ATOM   1294 C  CB  . ALA   B 2 79  ? 1.442   5.647  -15.964 1.00 46.56  ? 88  ALA   B CB  1 
ATOM   1295 N  N   . TRP   B 2 80  ? 3.161   7.039  -18.509 1.00 45.17  ? 89  TRP   B N   1 
ATOM   1296 C  CA  . TRP   B 2 80  ? 4.006   6.557  -19.642 1.00 47.60  ? 89  TRP   B CA  1 
ATOM   1297 C  C   . TRP   B 2 80  ? 4.073   5.029  -19.597 1.00 48.60  ? 89  TRP   B C   1 
ATOM   1298 O  O   . TRP   B 2 80  ? 4.229   4.439  -18.475 1.00 47.37  ? 89  TRP   B O   1 
ATOM   1299 C  CB  . TRP   B 2 80  ? 5.399   7.207  -19.639 1.00 46.16  ? 89  TRP   B CB  1 
ATOM   1300 C  CG  . TRP   B 2 80  ? 6.260   6.860  -20.809 1.00 45.52  ? 89  TRP   B CG  1 
ATOM   1301 C  CD1 . TRP   B 2 80  ? 5.904   6.952  -22.133 1.00 45.78  ? 89  TRP   B CD1 1 
ATOM   1302 C  CD2 . TRP   B 2 80  ? 7.652   6.512  -20.798 1.00 44.99  ? 89  TRP   B CD2 1 
ATOM   1303 N  NE1 . TRP   B 2 80  ? 6.951   6.587  -22.926 1.00 46.68  ? 89  TRP   B NE1 1 
ATOM   1304 C  CE2 . TRP   B 2 80  ? 8.040   6.311  -22.142 1.00 46.99  ? 89  TRP   B CE2 1 
ATOM   1305 C  CE3 . TRP   B 2 80  ? 8.594   6.261  -19.785 1.00 45.19  ? 89  TRP   B CE3 1 
ATOM   1306 C  CZ2 . TRP   B 2 80  ? 9.323   5.901  -22.507 1.00 45.72  ? 89  TRP   B CZ2 1 
ATOM   1307 C  CZ3 . TRP   B 2 80  ? 9.869   5.859  -20.149 1.00 45.41  ? 89  TRP   B CZ3 1 
ATOM   1308 C  CH2 . TRP   B 2 80  ? 10.232  5.704  -21.504 1.00 46.40  ? 89  TRP   B CH2 1 
ATOM   1309 N  N   . ASP   B 2 81  ? 3.929   4.414  -20.764 1.00 52.31  ? 90  ASP   B N   1 
ATOM   1310 C  CA  . ASP   B 2 81  ? 3.908   2.936  -20.923 1.00 54.65  ? 90  ASP   B CA  1 
ATOM   1311 C  C   . ASP   B 2 81  ? 5.344   2.387  -20.821 1.00 53.90  ? 90  ASP   B C   1 
ATOM   1312 O  O   . ASP   B 2 81  ? 5.443   1.189  -20.585 1.00 54.81  ? 90  ASP   B O   1 
ATOM   1313 C  CB  . ASP   B 2 81  ? 3.220   2.527  -22.247 1.00 52.82  ? 90  ASP   B CB  1 
ATOM   1314 C  CG  . ASP   B 2 81  ? 3.843   3.074  -23.510 1.00 55.31  ? 90  ASP   B CG  1 
ATOM   1315 O  OD1 . ASP   B 2 81  ? 4.887   3.726  -23.431 1.00 56.65  ? 90  ASP   B OD1 1 
ATOM   1316 O  OD2 . ASP   B 2 81  ? 3.251   2.887  -24.589 1.00 59.11  ? 90  ASP   B OD2 1 
ATOM   1317 N  N   . GLY   B 2 82  ? 6.370   3.239  -21.020 1.00 54.22  ? 91  GLY   B N   1 
ATOM   1318 C  CA  . GLY   B 2 82  ? 7.821   2.945  -21.009 1.00 54.57  ? 91  GLY   B CA  1 
ATOM   1319 C  C   . GLY   B 2 82  ? 8.378   2.659  -22.409 1.00 56.91  ? 91  GLY   B C   1 
ATOM   1320 O  O   . GLY   B 2 82  ? 9.603   2.377  -22.540 1.00 56.71  ? 91  GLY   B O   1 
ATOM   1321 N  N   . LEU   B 2 83  ? 7.531   2.695  -23.437 1.00 55.84  ? 92  LEU   B N   1 
ATOM   1322 C  CA  . LEU   B 2 83  ? 7.880   2.275  -24.827 1.00 58.75  ? 92  LEU   B CA  1 
ATOM   1323 C  C   . LEU   B 2 83  ? 7.674   3.400  -25.825 1.00 58.46  ? 92  LEU   B C   1 
ATOM   1324 O  O   . LEU   B 2 83  ? 8.522   3.588  -26.755 1.00 59.70  ? 92  LEU   B O   1 
ATOM   1325 C  CB  . LEU   B 2 83  ? 6.941   1.142  -25.240 1.00 62.33  ? 92  LEU   B CB  1 
ATOM   1326 C  CG  . LEU   B 2 83  ? 7.300   -0.251 -24.750 1.00 64.52  ? 92  LEU   B CG  1 
ATOM   1327 C  CD1 . LEU   B 2 83  ? 6.264   -1.250 -25.243 1.00 67.50  ? 92  LEU   B CD1 1 
ATOM   1328 C  CD2 . LEU   B 2 83  ? 8.690   -0.660 -25.224 1.00 63.52  ? 92  LEU   B CD2 1 
ATOM   1329 N  N   . SER   B 2 84  ? 6.485   3.989  -25.782 1.00 57.04  ? 93  SER   B N   1 
ATOM   1330 C  CA  . SER   B 2 84  ? 5.957   4.802  -26.903 1.00 53.08  ? 93  SER   B CA  1 
ATOM   1331 C  C   . SER   B 2 84  ? 6.517   6.215  -26.814 1.00 51.92  ? 93  SER   B C   1 
ATOM   1332 O  O   . SER   B 2 84  ? 6.871   6.717  -25.679 1.00 48.53  ? 93  SER   B O   1 
ATOM   1333 C  CB  . SER   B 2 84  ? 4.477   4.831  -26.878 1.00 54.48  ? 93  SER   B CB  1 
ATOM   1334 O  OG  . SER   B 2 84  ? 3.973   3.522  -26.709 1.00 55.08  ? 93  SER   B OG  1 
ATOM   1335 N  N   . GLU   B 2 85  ? 6.442   6.890  -27.944 1.00 47.98  ? 94  GLU   B N   1 
ATOM   1336 C  CA  . GLU   B 2 85  ? 6.762   8.323  -28.089 1.00 47.54  ? 94  GLU   B CA  1 
ATOM   1337 C  C   . GLU   B 2 85  ? 5.652   9.075  -27.341 1.00 45.24  ? 94  GLU   B C   1 
ATOM   1338 O  O   . GLU   B 2 85  ? 4.510   8.511  -27.062 1.00 44.76  ? 94  GLU   B O   1 
ATOM   1339 C  CB  . GLU   B 2 85  ? 6.875   8.690  -29.589 1.00 48.74  ? 94  GLU   B CB  1 
ATOM   1340 C  CG  . GLU   B 2 85  ? 8.155   8.153  -30.252 1.00 51.17  ? 94  GLU   B CG  1 
ATOM   1341 C  CD  . GLU   B 2 85  ? 8.649   8.802  -31.559 1.00 53.52  ? 94  GLU   B CD  1 
ATOM   1342 O  OE1 . GLU   B 2 85  ? 7.960   9.640  -32.109 1.00 52.72  ? 94  GLU   B OE1 1 
ATOM   1343 O  OE2 . GLU   B 2 85  ? 9.757   8.476  -32.006 1.00 56.68  ? 94  GLU   B OE2 1 
ATOM   1344 N  N   . VAL   B 2 86  ? 5.971   10.286 -26.914 1.00 44.24  ? 95  VAL   B N   1 
ATOM   1345 C  CA  . VAL   B 2 86  ? 4.968   11.132 -26.225 1.00 43.16  ? 95  VAL   B CA  1 
ATOM   1346 C  C   . VAL   B 2 86  ? 4.967   12.495 -26.898 1.00 41.71  ? 95  VAL   B C   1 
ATOM   1347 O  O   . VAL   B 2 86  ? 5.852   12.747 -27.725 1.00 44.41  ? 95  VAL   B O   1 
ATOM   1348 C  CB  . VAL   B 2 86  ? 5.294   11.261 -24.716 1.00 40.27  ? 95  VAL   B CB  1 
ATOM   1349 C  CG1 . VAL   B 2 86  ? 5.559   9.920  -24.056 1.00 40.98  ? 95  VAL   B CG1 1 
ATOM   1350 C  CG2 . VAL   B 2 86  ? 6.500   12.168 -24.495 1.00 41.03  ? 95  VAL   B CG2 1 
ATOM   1351 N  N   . GLN   B 2 87  ? 4.033   13.377 -26.552 1.00 40.91  ? 96  GLN   B N   1 
ATOM   1352 C  CA  . GLN   B 2 87  ? 4.147   14.794 -26.957 1.00 41.20  ? 96  GLN   B CA  1 
ATOM   1353 C  C   . GLN   B 2 87  ? 4.185   15.754 -25.791 1.00 39.55  ? 96  GLN   B C   1 
ATOM   1354 O  O   . GLN   B 2 87  ? 3.281   15.686 -24.935 1.00 38.80  ? 96  GLN   B O   1 
ATOM   1355 C  CB  . GLN   B 2 87  ? 3.051   15.192 -27.938 1.00 41.93  ? 96  GLN   B CB  1 
ATOM   1356 C  CG  . GLN   B 2 87  ? 3.265   14.587 -29.279 1.00 42.10  ? 96  GLN   B CG  1 
ATOM   1357 C  CD  . GLN   B 2 87  ? 2.142   14.959 -30.209 1.00 43.15  ? 96  GLN   B CD  1 
ATOM   1358 O  OE1 . GLN   B 2 87  ? 1.255   15.770 -29.919 1.00 41.27  ? 96  GLN   B OE1 1 
ATOM   1359 N  NE2 . GLN   B 2 87  ? 2.184   14.317 -31.367 1.00 43.18  ? 96  GLN   B NE2 1 
ATOM   1360 N  N   . LEU   B 2 88  ? 5.194   16.623 -25.758 1.00 38.80  ? 97  LEU   B N   1 
ATOM   1361 C  CA  . LEU   B 2 88  ? 5.184   17.785 -24.826 1.00 36.97  ? 97  LEU   B CA  1 
ATOM   1362 C  C   . LEU   B 2 88  ? 4.305   18.841 -25.446 1.00 39.45  ? 97  LEU   B C   1 
ATOM   1363 O  O   . LEU   B 2 88  ? 4.582   19.204 -26.658 1.00 39.60  ? 97  LEU   B O   1 
ATOM   1364 C  CB  . LEU   B 2 88  ? 6.590   18.358 -24.639 1.00 38.00  ? 97  LEU   B CB  1 
ATOM   1365 C  CG  . LEU   B 2 88  ? 6.684   19.685 -23.909 1.00 38.07  ? 97  LEU   B CG  1 
ATOM   1366 C  CD1 . LEU   B 2 88  ? 6.208   19.501 -22.470 1.00 37.42  ? 97  LEU   B CD1 1 
ATOM   1367 C  CD2 . LEU   B 2 88  ? 8.107   20.197 -23.875 1.00 38.44  ? 97  LEU   B CD2 1 
ATOM   1368 N  N   . LEU   B 2 89  ? 3.254   19.262 -24.772 1.00 37.86  ? 98  LEU   B N   1 
ATOM   1369 C  CA  . LEU   B 2 89  ? 2.450   20.409 -25.239 1.00 38.58  ? 98  LEU   B CA  1 
ATOM   1370 C  C   . LEU   B 2 89  ? 3.103   21.658 -24.678 1.00 38.87  ? 98  LEU   B C   1 
ATOM   1371 O  O   . LEU   B 2 89  ? 2.714   22.087 -23.519 1.00 37.26  ? 98  LEU   B O   1 
ATOM   1372 C  CB  . LEU   B 2 89  ? 1.005   20.199 -24.798 1.00 40.35  ? 98  LEU   B CB  1 
ATOM   1373 C  CG  . LEU   B 2 89  ? -0.030  21.276 -25.138 1.00 41.80  ? 98  LEU   B CG  1 
ATOM   1374 C  CD1 . LEU   B 2 89  ? 0.362   22.141 -26.291 1.00 45.92  ? 98  LEU   B CD1 1 
ATOM   1375 C  CD2 . LEU   B 2 89  ? -1.397  20.632 -25.348 1.00 43.28  ? 98  LEU   B CD2 1 
ATOM   1376 N  N   . ALA   B 2 90  ? 4.168   22.118 -25.331 1.00 38.56  ? 99  ALA   B N   1 
ATOM   1377 C  CA  . ALA   B 2 90  ? 4.961   23.269 -24.853 1.00 39.01  ? 99  ALA   B CA  1 
ATOM   1378 C  C   . ALA   B 2 90  ? 4.135   24.537 -24.996 1.00 40.06  ? 99  ALA   B C   1 
ATOM   1379 O  O   . ALA   B 2 90  ? 3.552   24.789 -26.104 1.00 40.73  ? 99  ALA   B O   1 
ATOM   1380 C  CB  . ALA   B 2 90  ? 6.279   23.358 -25.580 1.00 40.76  ? 99  ALA   B CB  1 
ATOM   1381 N  N   . VAL   B 2 91  ? 4.096   25.326 -23.918 1.00 39.49  ? 100 VAL   B N   1 
ATOM   1382 C  CA  . VAL   B 2 91  ? 3.518   26.680 -23.892 1.00 39.65  ? 100 VAL   B CA  1 
ATOM   1383 C  C   . VAL   B 2 91  ? 4.626   27.639 -23.479 1.00 40.93  ? 100 VAL   B C   1 
ATOM   1384 O  O   . VAL   B 2 91  ? 4.688   28.048 -22.309 1.00 40.77  ? 100 VAL   B O   1 
ATOM   1385 C  CB  . VAL   B 2 91  ? 2.315   26.700 -22.941 1.00 38.26  ? 100 VAL   B CB  1 
ATOM   1386 C  CG1 . VAL   B 2 91  ? 1.564   28.031 -22.959 1.00 38.50  ? 100 VAL   B CG1 1 
ATOM   1387 C  CG2 . VAL   B 2 91  ? 1.378   25.534 -23.223 1.00 36.94  ? 100 VAL   B CG2 1 
ATOM   1388 N  N   . PRO   B 2 92  ? 5.522   28.061 -24.402 1.00 39.66  ? 101 PRO   B N   1 
ATOM   1389 C  CA  . PRO   B 2 92  ? 6.639   28.938 -24.044 1.00 40.95  ? 101 PRO   B CA  1 
ATOM   1390 C  C   . PRO   B 2 92  ? 6.185   30.365 -23.806 1.00 41.03  ? 101 PRO   B C   1 
ATOM   1391 O  O   . PRO   B 2 92  ? 5.112   30.746 -24.288 1.00 43.15  ? 101 PRO   B O   1 
ATOM   1392 C  CB  . PRO   B 2 92  ? 7.591   28.877 -25.250 1.00 41.85  ? 101 PRO   B CB  1 
ATOM   1393 C  CG  . PRO   B 2 92  ? 6.999   27.808 -26.152 1.00 40.97  ? 101 PRO   B CG  1 
ATOM   1394 C  CD  . PRO   B 2 92  ? 5.523   27.774 -25.856 1.00 41.72  ? 101 PRO   B CD  1 
ATOM   1395 N  N   . PRO   B 2 93  ? 6.903   31.177 -22.991 1.00 42.82  ? 102 PRO   B N   1 
ATOM   1396 C  CA  . PRO   B 2 93  ? 6.470   32.552 -22.754 1.00 44.26  ? 102 PRO   B CA  1 
ATOM   1397 C  C   . PRO   B 2 93  ? 6.300   33.300 -24.094 1.00 45.03  ? 102 PRO   B C   1 
ATOM   1398 O  O   . PRO   B 2 93  ? 7.213   33.216 -24.917 1.00 45.05  ? 102 PRO   B O   1 
ATOM   1399 C  CB  . PRO   B 2 93  ? 7.574   33.176 -21.901 1.00 44.88  ? 102 PRO   B CB  1 
ATOM   1400 C  CG  . PRO   B 2 93  ? 8.246   31.980 -21.221 1.00 44.38  ? 102 PRO   B CG  1 
ATOM   1401 C  CD  . PRO   B 2 93  ? 8.040   30.788 -22.139 1.00 44.00  ? 102 PRO   B CD  1 
ATOM   1402 N  N   . GLY   B 2 94  ? 5.148   33.962 -24.293 1.00 45.75  ? 103 GLY   B N   1 
ATOM   1403 C  CA  . GLY   B 2 94  ? 4.875   34.892 -25.409 1.00 46.73  ? 103 GLY   B CA  1 
ATOM   1404 C  C   . GLY   B 2 94  ? 4.696   34.185 -26.743 1.00 47.14  ? 103 GLY   B C   1 
ATOM   1405 O  O   . GLY   B 2 94  ? 4.635   34.913 -27.826 1.00 48.52  ? 103 GLY   B O   1 
ATOM   1406 N  N   . GLU   B 2 95  ? 4.596   32.852 -26.745 1.00 46.51  ? 104 GLU   B N   1 
ATOM   1407 C  CA  . GLU   B 2 95  ? 4.539   32.032 -27.985 1.00 47.22  ? 104 GLU   B CA  1 
ATOM   1408 C  C   . GLU   B 2 95  ? 3.365   31.072 -27.894 1.00 47.79  ? 104 GLU   B C   1 
ATOM   1409 O  O   . GLU   B 2 95  ? 2.983   30.684 -26.772 1.00 44.58  ? 104 GLU   B O   1 
ATOM   1410 C  CB  . GLU   B 2 95  ? 5.857   31.302 -28.215 1.00 47.12  ? 104 GLU   B CB  1 
ATOM   1411 C  CG  . GLU   B 2 95  ? 7.063   32.238 -28.296 1.00 48.59  ? 104 GLU   B CG  1 
ATOM   1412 C  CD  . GLU   B 2 95  ? 8.394   31.533 -28.543 1.00 50.30  ? 104 GLU   B CD  1 
ATOM   1413 O  OE1 . GLU   B 2 95  ? 8.408   30.277 -28.432 1.00 50.32  ? 104 GLU   B OE1 1 
ATOM   1414 O  OE2 . GLU   B 2 95  ? 9.426   32.230 -28.888 1.00 52.20  ? 104 GLU   B OE2 1 
ATOM   1415 N  N   . ARG   B 2 96  ? 2.813   30.697 -29.038 1.00 47.01  ? 105 ARG   B N   1 
ATOM   1416 C  CA  . ARG   B 2 96  ? 1.654   29.777 -29.136 1.00 48.59  ? 105 ARG   B CA  1 
ATOM   1417 C  C   . ARG   B 2 96  ? 2.005   28.380 -28.614 1.00 46.81  ? 105 ARG   B C   1 
ATOM   1418 O  O   . ARG   B 2 96  ? 3.178   27.932 -28.758 1.00 44.63  ? 105 ARG   B O   1 
ATOM   1419 C  CB  . ARG   B 2 96  ? 1.196   29.654 -30.587 1.00 53.24  ? 105 ARG   B CB  1 
ATOM   1420 C  CG  . ARG   B 2 96  ? -0.193  29.052 -30.753 1.00 57.76  ? 105 ARG   B CG  1 
ATOM   1421 C  CD  . ARG   B 2 96  ? -1.033  29.765 -31.815 1.00 61.27  ? 105 ARG   B CD  1 
ATOM   1422 N  NE  . ARG   B 2 96  ? -0.497  29.572 -33.144 1.00 64.96  ? 105 ARG   B NE  1 
ATOM   1423 C  CZ  . ARG   B 2 96  ? 0.431   30.344 -33.710 1.00 69.89  ? 105 ARG   B CZ  1 
ATOM   1424 N  NH1 . ARG   B 2 96  ? 0.932   31.378 -33.059 1.00 72.16  ? 105 ARG   B NH1 1 
ATOM   1425 N  NH2 . ARG   B 2 96  ? 0.856   30.091 -34.935 1.00 73.25  ? 105 ARG   B NH2 1 
ATOM   1426 N  N   . ALA   B 2 97  ? 1.000   27.695 -28.053 1.00 45.37  ? 106 ALA   B N   1 
ATOM   1427 C  CA  . ALA   B 2 97  ? 1.105   26.281 -27.641 1.00 44.69  ? 106 ALA   B CA  1 
ATOM   1428 C  C   . ALA   B 2 97  ? 1.559   25.475 -28.859 1.00 46.10  ? 106 ALA   B C   1 
ATOM   1429 O  O   . ALA   B 2 97  ? 1.086   25.753 -29.960 1.00 43.83  ? 106 ALA   B O   1 
ATOM   1430 C  CB  . ALA   B 2 97  ? -0.190  25.789 -27.053 1.00 45.11  ? 106 ALA   B CB  1 
ATOM   1431 N  N   . LYS   B 2 98  ? 2.452   24.522 -28.669 1.00 44.72  ? 107 LYS   B N   1 
ATOM   1432 C  CA  . LYS   B 2 98  ? 3.129   23.812 -29.778 1.00 46.74  ? 107 LYS   B CA  1 
ATOM   1433 C  C   . LYS   B 2 98  ? 3.391   22.393 -29.295 1.00 45.86  ? 107 LYS   B C   1 
ATOM   1434 O  O   . LYS   B 2 98  ? 4.069   22.200 -28.203 1.00 42.65  ? 107 LYS   B O   1 
ATOM   1435 C  CB  . LYS   B 2 98  ? 4.357   24.632 -30.194 1.00 48.80  ? 107 LYS   B CB  1 
ATOM   1436 C  CG  . LYS   B 2 98  ? 5.373   23.892 -31.035 1.00 52.85  ? 107 LYS   B CG  1 
ATOM   1437 C  CD  . LYS   B 2 98  ? 6.619   24.713 -31.317 1.00 54.59  ? 107 LYS   B CD  1 
ATOM   1438 C  CE  . LYS   B 2 98  ? 7.383   25.062 -30.044 1.00 54.15  ? 107 LYS   B CE  1 
ATOM   1439 N  NZ  . LYS   B 2 98  ? 8.849   24.873 -30.225 1.00 54.14  ? 107 LYS   B NZ  1 
ATOM   1440 N  N   . ASN   B 2 99  ? 2.810   21.417 -29.996 1.00 42.80  ? 108 ASN   B N   1 
ATOM   1441 C  CA  . ASN   B 2 99  ? 3.126   20.005 -29.702 1.00 42.73  ? 108 ASN   B CA  1 
ATOM   1442 C  C   . ASN   B 2 99  ? 4.513   19.637 -30.227 1.00 43.38  ? 108 ASN   B C   1 
ATOM   1443 O  O   . ASN   B 2 99  ? 4.762   19.652 -31.545 1.00 40.68  ? 108 ASN   B O   1 
ATOM   1444 C  CB  . ASN   B 2 99  ? 2.057   19.053 -30.222 1.00 42.72  ? 108 ASN   B CB  1 
ATOM   1445 C  CG  . ASN   B 2 99  ? 0.701   19.261 -29.607 1.00 44.60  ? 108 ASN   B CG  1 
ATOM   1446 O  OD1 . ASN   B 2 99  ? 0.071   20.291 -29.850 1.00 48.29  ? 108 ASN   B OD1 1 
ATOM   1447 N  ND2 . ASN   B 2 99  ? 0.187   18.245 -28.925 1.00 44.07  ? 108 ASN   B ND2 1 
ATOM   1448 N  N   . ILE   B 2 100 ? 5.343   19.088 -29.371 1.00 41.66  ? 109 ILE   B N   1 
ATOM   1449 C  CA  . ILE   B 2 100 ? 6.685   18.557 -29.700 1.00 42.76  ? 109 ILE   B CA  1 
ATOM   1450 C  C   . ILE   B 2 100 ? 6.708   17.083 -29.369 1.00 43.52  ? 109 ILE   B C   1 
ATOM   1451 O  O   . ILE   B 2 100 ? 6.627   16.708 -28.133 1.00 41.14  ? 109 ILE   B O   1 
ATOM   1452 C  CB  . ILE   B 2 100 ? 7.848   19.345 -29.079 1.00 44.49  ? 109 ILE   B CB  1 
ATOM   1453 C  CG1 . ILE   B 2 100 ? 7.699   20.839 -29.342 1.00 46.65  ? 109 ILE   B CG1 1 
ATOM   1454 C  CG2 . ILE   B 2 100 ? 9.196   18.868 -29.598 1.00 45.34  ? 109 ILE   B CG2 1 
ATOM   1455 C  CD1 . ILE   B 2 100 ? 8.027   21.240 -30.796 1.00 47.76  ? 109 ILE   B CD1 1 
ATOM   1456 N  N   . GLN   B 2 101 ? 6.999   16.248 -30.375 1.00 44.06  ? 110 GLN   B N   1 
ATOM   1457 C  CA  . GLN   B 2 101 ? 6.951   14.773 -30.205 1.00 44.87  ? 110 GLN   B CA  1 
ATOM   1458 C  C   . GLN   B 2 101 ? 8.367   14.241 -29.982 1.00 45.46  ? 110 GLN   B C   1 
ATOM   1459 O  O   . GLN   B 2 101 ? 9.350   14.857 -30.537 1.00 45.03  ? 110 GLN   B O   1 
ATOM   1460 C  CB  . GLN   B 2 101 ? 6.107   14.099 -31.267 1.00 46.70  ? 110 GLN   B CB  1 
ATOM   1461 C  CG  . GLN   B 2 101 ? 6.271   12.580 -31.310 1.00 48.01  ? 110 GLN   B CG  1 
ATOM   1462 C  CD  . GLN   B 2 101 ? 5.224   11.978 -32.222 1.00 48.75  ? 110 GLN   B CD  1 
ATOM   1463 O  OE1 . GLN   B 2 101 ? 4.319   12.650 -32.690 1.00 49.54  ? 110 GLN   B OE1 1 
ATOM   1464 N  NE2 . GLN   B 2 101 ? 5.321   10.691 -32.489 1.00 50.74  ? 110 GLN   B NE2 1 
ATOM   1465 N  N   . THR   B 2 102 ? 8.491   13.298 -28.995 1.00 44.58  ? 111 THR   B N   1 
ATOM   1466 C  CA  . THR   B 2 102 ? 9.803   12.809 -28.523 1.00 45.49  ? 111 THR   B CA  1 
ATOM   1467 C  C   . THR   B 2 102 ? 9.654   11.417 -27.902 1.00 43.99  ? 111 THR   B C   1 
ATOM   1468 O  O   . THR   B 2 102 ? 8.557   11.044 -27.496 1.00 46.65  ? 111 THR   B O   1 
ATOM   1469 C  CB  . THR   B 2 102 ? 10.447  13.910 -27.663 1.00 45.53  ? 111 THR   B CB  1 
ATOM   1470 O  OG1 . THR   B 2 102 ? 11.826  13.561 -27.511 1.00 46.51  ? 111 THR   B OG1 1 
ATOM   1471 C  CG2 . THR   B 2 102 ? 9.783   14.127 -26.314 1.00 45.49  ? 111 THR   B CG2 1 
ATOM   1472 N  N   . LEU   B 2 103 ? 10.714  10.630 -27.903 1.00 43.82  ? 112 LEU   B N   1 
ATOM   1473 C  CA  . LEU   B 2 103 ? 10.807  9.380  -27.110 1.00 43.25  ? 112 LEU   B CA  1 
ATOM   1474 C  C   . LEU   B 2 103 ? 11.498  9.716  -25.803 1.00 42.17  ? 112 LEU   B C   1 
ATOM   1475 O  O   . LEU   B 2 103 ? 12.675  10.166 -25.787 1.00 41.04  ? 112 LEU   B O   1 
ATOM   1476 C  CB  . LEU   B 2 103 ? 11.606  8.274  -27.792 1.00 44.04  ? 112 LEU   B CB  1 
ATOM   1477 C  CG  . LEU   B 2 103 ? 11.684  6.975  -26.976 1.00 44.27  ? 112 LEU   B CG  1 
ATOM   1478 C  CD1 . LEU   B 2 103 ? 10.354  6.216  -27.045 1.00 43.58  ? 112 LEU   B CD1 1 
ATOM   1479 C  CD2 . LEU   B 2 103 ? 12.853  6.089  -27.444 1.00 44.93  ? 112 LEU   B CD2 1 
ATOM   1480 N  N   . PRO   B 2 104 ? 10.784  9.564  -24.667 1.00 42.75  ? 113 PRO   B N   1 
ATOM   1481 C  CA  . PRO   B 2 104 ? 11.450  9.824  -23.396 1.00 41.64  ? 113 PRO   B CA  1 
ATOM   1482 C  C   . PRO   B 2 104 ? 12.659  8.895  -23.171 1.00 42.66  ? 113 PRO   B C   1 
ATOM   1483 O  O   . PRO   B 2 104 ? 12.621  7.706  -23.520 1.00 42.77  ? 113 PRO   B O   1 
ATOM   1484 C  CB  . PRO   B 2 104 ? 10.352  9.598  -22.338 1.00 41.54  ? 113 PRO   B CB  1 
ATOM   1485 C  CG  . PRO   B 2 104 ? 9.036   9.637  -23.086 1.00 41.37  ? 113 PRO   B CG  1 
ATOM   1486 C  CD  . PRO   B 2 104 ? 9.371   9.164  -24.520 1.00 41.47  ? 113 PRO   B CD  1 
ATOM   1487 N  N   . GLY   B 2 105 ? 13.671  9.453  -22.456 1.00 44.13  ? 114 GLY   B N   1 
ATOM   1488 C  CA  . GLY   B 2 105 ? 14.711  8.663  -21.793 1.00 44.11  ? 114 GLY   B CA  1 
ATOM   1489 C  C   . GLY   B 2 105 ? 14.271  8.286  -20.368 1.00 45.54  ? 114 GLY   B C   1 
ATOM   1490 O  O   . GLY   B 2 105 ? 13.035  8.107  -20.101 1.00 44.48  ? 114 GLY   B O   1 
ATOM   1491 N  N   . ILE   B 2 106 ? 15.249  8.079  -19.499 1.00 46.08  ? 115 ILE   B N   1 
ATOM   1492 C  CA  . ILE   B 2 106 ? 15.010  7.586  -18.101 1.00 45.72  ? 115 ILE   B CA  1 
ATOM   1493 C  C   . ILE   B 2 106 ? 15.926  8.340  -17.129 1.00 46.14  ? 115 ILE   B C   1 
ATOM   1494 O  O   . ILE   B 2 106 ? 17.145  8.399  -17.382 1.00 44.98  ? 115 ILE   B O   1 
ATOM   1495 C  CB  . ILE   B 2 106 ? 15.246  6.060  -18.009 1.00 48.02  ? 115 ILE   B CB  1 
ATOM   1496 C  CG1 . ILE   B 2 106 ? 14.484  5.265  -19.069 1.00 50.32  ? 115 ILE   B CG1 1 
ATOM   1497 C  CG2 . ILE   B 2 106 ? 14.932  5.497  -16.612 1.00 48.03  ? 115 ILE   B CG2 1 
ATOM   1498 C  CD1 . ILE   B 2 106 ? 13.011  5.257  -18.846 1.00 51.71  ? 115 ILE   B CD1 1 
ATOM   1499 N  N   . PHE   B 2 107 ? 15.341  8.778  -15.993 1.00 45.03  ? 116 PHE   B N   1 
ATOM   1500 C  CA  . PHE   B 2 107 ? 16.004  9.049  -14.691 1.00 46.35  ? 116 PHE   B CA  1 
ATOM   1501 C  C   . PHE   B 2 107 ? 16.078  7.734  -13.902 1.00 45.49  ? 116 PHE   B C   1 
ATOM   1502 O  O   . PHE   B 2 107 ? 15.034  7.095  -13.649 1.00 44.06  ? 116 PHE   B O   1 
ATOM   1503 C  CB  . PHE   B 2 107 ? 15.212  10.107 -13.923 1.00 44.00  ? 116 PHE   B CB  1 
ATOM   1504 C  CG  . PHE   B 2 107 ? 15.445  11.535 -14.345 1.00 45.17  ? 116 PHE   B CG  1 
ATOM   1505 C  CD1 . PHE   B 2 107 ? 16.205  11.867 -15.454 1.00 45.20  ? 116 PHE   B CD1 1 
ATOM   1506 C  CD2 . PHE   B 2 107 ? 14.850  12.560 -13.631 1.00 44.13  ? 116 PHE   B CD2 1 
ATOM   1507 C  CE1 . PHE   B 2 107 ? 16.441  13.193 -15.771 1.00 45.01  ? 116 PHE   B CE1 1 
ATOM   1508 C  CE2 . PHE   B 2 107 ? 15.055  13.885 -13.974 1.00 44.79  ? 116 PHE   B CE2 1 
ATOM   1509 C  CZ  . PHE   B 2 107 ? 15.843  14.197 -15.046 1.00 44.14  ? 116 PHE   B CZ  1 
ATOM   1510 N  N   . LYS   B 2 108 ? 17.288  7.269  -13.646 1.00 47.75  ? 117 LYS   B N   1 
ATOM   1511 C  CA  . LYS   B 2 108 ? 17.523  6.075  -12.788 1.00 50.43  ? 117 LYS   B CA  1 
ATOM   1512 C  C   . LYS   B 2 108 ? 17.766  6.593  -11.375 1.00 47.24  ? 117 LYS   B C   1 
ATOM   1513 O  O   . LYS   B 2 108 ? 18.713  7.375  -11.204 1.00 45.51  ? 117 LYS   B O   1 
ATOM   1514 C  CB  . LYS   B 2 108 ? 18.650  5.196  -13.338 1.00 54.80  ? 117 LYS   B CB  1 
ATOM   1515 C  CG  . LYS   B 2 108 ? 18.169  4.150  -14.351 1.00 60.31  ? 117 LYS   B CG  1 
ATOM   1516 C  CD  . LYS   B 2 108 ? 19.254  3.540  -15.229 1.00 66.28  ? 117 LYS   B CD  1 
ATOM   1517 C  CE  . LYS   B 2 108 ? 18.837  2.220  -15.869 1.00 72.12  ? 117 LYS   B CE  1 
ATOM   1518 N  NZ  . LYS   B 2 108 ? 19.539  1.910  -17.154 1.00 76.25  ? 117 LYS   B NZ  1 
ATOM   1519 N  N   . THR   B 2 109 ? 16.935  6.179  -10.432 1.00 47.93  ? 118 THR   B N   1 
ATOM   1520 C  CA  . THR   B 2 109 ? 17.026  6.649  -9.031  1.00 47.68  ? 118 THR   B CA  1 
ATOM   1521 C  C   . THR   B 2 109 ? 17.049  5.444  -8.085  1.00 47.90  ? 118 THR   B C   1 
ATOM   1522 O  O   . THR   B 2 109 ? 16.497  4.355  -8.431  1.00 44.87  ? 118 THR   B O   1 
ATOM   1523 C  CB  . THR   B 2 109 ? 15.858  7.546  -8.591  1.00 47.91  ? 118 THR   B CB  1 
ATOM   1524 O  OG1 . THR   B 2 109 ? 14.804  6.724  -8.063  1.00 47.21  ? 118 THR   B OG1 1 
ATOM   1525 C  CG2 . THR   B 2 109 ? 15.359  8.459  -9.684  1.00 47.50  ? 118 THR   B CG2 1 
ATOM   1526 N  N   . LYS   B 2 110 ? 17.580  5.671  -6.890  1.00 49.51  ? 119 LYS   B N   1 
ATOM   1527 C  CA  . LYS   B 2 110 ? 17.662  4.625  -5.842  1.00 54.33  ? 119 LYS   B CA  1 
ATOM   1528 C  C   . LYS   B 2 110 ? 16.260  4.106  -5.485  1.00 55.72  ? 119 LYS   B C   1 
ATOM   1529 O  O   . LYS   B 2 110 ? 16.190  3.033  -4.892  1.00 53.35  ? 119 LYS   B O   1 
ATOM   1530 C  CB  . LYS   B 2 110 ? 18.386  5.174  -4.617  1.00 52.88  ? 119 LYS   B CB  1 
ATOM   1531 C  CG  . LYS   B 2 110 ? 17.676  6.308  -3.899  1.00 56.57  ? 119 LYS   B CG  1 
ATOM   1532 C  CD  . LYS   B 2 110 ? 18.533  6.934  -2.779  1.00 57.80  ? 119 LYS   B CD  1 
ATOM   1533 C  CE  . LYS   B 2 110 ? 17.917  6.803  -1.415  1.00 61.98  ? 119 LYS   B CE  1 
ATOM   1534 N  NZ  . LYS   B 2 110 ? 16.726  7.679  -1.286  1.00 61.68  ? 119 LYS   B NZ  1 
ATOM   1535 N  N   . ASP   B 2 111 ? 15.187  4.810  -5.860  1.00 54.86  ? 120 ASP   B N   1 
ATOM   1536 C  CA  . ASP   B 2 111 ? 13.803  4.375  -5.555  1.00 54.60  ? 120 ASP   B CA  1 
ATOM   1537 C  C   . ASP   B 2 111 ? 13.069  3.946  -6.822  1.00 53.69  ? 120 ASP   B C   1 
ATOM   1538 O  O   . ASP   B 2 111 ? 11.862  3.728  -6.714  1.00 53.48  ? 120 ASP   B O   1 
ATOM   1539 C  CB  . ASP   B 2 111 ? 13.023  5.465  -4.823  1.00 55.41  ? 120 ASP   B CB  1 
ATOM   1540 C  CG  . ASP   B 2 111 ? 13.570  5.661  -3.425  1.00 56.20  ? 120 ASP   B CG  1 
ATOM   1541 O  OD1 . ASP   B 2 111 ? 13.424  4.736  -2.606  1.00 57.05  ? 120 ASP   B OD1 1 
ATOM   1542 O  OD2 . ASP   B 2 111 ? 14.246  6.669  -3.228  1.00 55.07  ? 120 ASP   B OD2 1 
ATOM   1543 N  N   . GLY   B 2 112 ? 13.746  3.826  -7.975  1.00 50.53  ? 121 GLY   B N   1 
ATOM   1544 C  CA  . GLY   B 2 112 ? 13.089  3.272  -9.163  1.00 51.59  ? 121 GLY   B CA  1 
ATOM   1545 C  C   . GLY   B 2 112 ? 13.251  4.244  -10.308 1.00 49.05  ? 121 GLY   B C   1 
ATOM   1546 O  O   . GLY   B 2 112 ? 13.914  5.275  -10.121 1.00 46.55  ? 121 GLY   B O   1 
ATOM   1547 N  N   . ASP   B 2 113 ? 12.737  3.912  -11.481 1.00 50.37  ? 122 ASP   B N   1 
ATOM   1548 C  CA  . ASP   B 2 113 ? 13.015  4.724  -12.685 1.00 51.52  ? 122 ASP   B CA  1 
ATOM   1549 C  C   . ASP   B 2 113 ? 11.787  5.555  -13.032 1.00 51.78  ? 122 ASP   B C   1 
ATOM   1550 O  O   . ASP   B 2 113 ? 10.673  5.017  -12.846 1.00 49.86  ? 122 ASP   B O   1 
ATOM   1551 C  CB  . ASP   B 2 113 ? 13.452  3.812  -13.832 1.00 54.31  ? 122 ASP   B CB  1 
ATOM   1552 C  CG  . ASP   B 2 113 ? 14.753  3.073  -13.529 1.00 56.96  ? 122 ASP   B CG  1 
ATOM   1553 O  OD1 . ASP   B 2 113 ? 15.385  3.384  -12.493 1.00 58.66  ? 122 ASP   B OD1 1 
ATOM   1554 O  OD2 . ASP   B 2 113 ? 15.116  2.195  -14.305 1.00 64.07  ? 122 ASP   B OD2 1 
ATOM   1555 N  N   . ILE   B 2 114 ? 12.030  6.767  -13.576 1.00 48.14  ? 123 ILE   B N   1 
ATOM   1556 C  CA  . ILE   B 2 114 ? 11.018  7.757  -14.032 1.00 47.55  ? 123 ILE   B CA  1 
ATOM   1557 C  C   . ILE   B 2 114 ? 11.362  8.079  -15.506 1.00 43.97  ? 123 ILE   B C   1 
ATOM   1558 O  O   . ILE   B 2 114 ? 12.568  8.162  -15.816 1.00 43.03  ? 123 ILE   B O   1 
ATOM   1559 C  CB  . ILE   B 2 114 ? 11.061  9.024  -13.152 1.00 48.19  ? 123 ILE   B CB  1 
ATOM   1560 C  CG1 . ILE   B 2 114 ? 11.359  8.714  -11.680 1.00 53.91  ? 123 ILE   B CG1 1 
ATOM   1561 C  CG2 . ILE   B 2 114 ? 9.771   9.795  -13.288 1.00 51.40  ? 123 ILE   B CG2 1 
ATOM   1562 C  CD1 . ILE   B 2 114 ? 11.790  9.921  -10.840 1.00 54.28  ? 123 ILE   B CD1 1 
ATOM   1563 N  N   . GLY   B 2 115 ? 10.355  8.297  -16.344 1.00 44.39  ? 124 GLY   B N   1 
ATOM   1564 C  CA  . GLY   B 2 115 ? 10.550  8.807  -17.715 1.00 43.72  ? 124 GLY   B CA  1 
ATOM   1565 C  C   . GLY   B 2 115 ? 11.101  10.206 -17.631 1.00 43.47  ? 124 GLY   B C   1 
ATOM   1566 O  O   . GLY   B 2 115 ? 10.830  10.892 -16.607 1.00 39.75  ? 124 GLY   B O   1 
ATOM   1567 N  N   . ALA   B 2 116 ? 11.860  10.604 -18.641 1.00 40.40  ? 125 ALA   B N   1 
ATOM   1568 C  CA  . ALA   B 2 116 ? 12.507  11.924 -18.746 1.00 40.92  ? 125 ALA   B CA  1 
ATOM   1569 C  C   . ALA   B 2 116 ? 12.345  12.403 -20.188 1.00 42.00  ? 125 ALA   B C   1 
ATOM   1570 O  O   . ALA   B 2 116 ? 12.445  11.558 -21.116 1.00 42.37  ? 125 ALA   B O   1 
ATOM   1571 C  CB  . ALA   B 2 116 ? 13.975  11.834 -18.453 1.00 41.54  ? 125 ALA   B CB  1 
ATOM   1572 N  N   A VAL   B 2 117 ? 12.164  13.712 -20.365 0.13 42.27  ? 126 VAL   B N   1 
ATOM   1573 N  N   B VAL   B 2 117 ? 12.115  13.710 -20.349 0.14 41.21  ? 126 VAL   B N   1 
ATOM   1574 N  N   C VAL   B 2 117 ? 12.164  13.711 -20.364 0.36 42.30  ? 126 VAL   B N   1 
ATOM   1575 N  N   D VAL   B 2 117 ? 12.113  13.709 -20.348 0.37 41.13  ? 126 VAL   B N   1 
ATOM   1576 C  CA  A VAL   B 2 117 ? 11.940  14.363 -21.686 0.13 42.89  ? 126 VAL   B CA  1 
ATOM   1577 C  CA  B VAL   B 2 117 ? 11.925  14.415 -21.649 0.14 41.20  ? 126 VAL   B CA  1 
ATOM   1578 C  CA  C VAL   B 2 117 ? 11.937  14.365 -21.682 0.36 42.90  ? 126 VAL   B CA  1 
ATOM   1579 C  CA  D VAL   B 2 117 ? 11.922  14.419 -21.644 0.37 40.97  ? 126 VAL   B CA  1 
ATOM   1580 C  C   A VAL   B 2 117 ? 13.047  15.400 -21.907 0.13 42.84  ? 126 VAL   B C   1 
ATOM   1581 C  C   B VAL   B 2 117 ? 13.117  15.358 -21.851 0.14 41.80  ? 126 VAL   B C   1 
ATOM   1582 C  C   C VAL   B 2 117 ? 13.045  15.399 -21.904 0.36 42.96  ? 126 VAL   B C   1 
ATOM   1583 C  C   D VAL   B 2 117 ? 13.116  15.358 -21.847 0.37 41.82  ? 126 VAL   B C   1 
ATOM   1584 O  O   A VAL   B 2 117 ? 13.146  16.335 -21.099 0.13 42.33  ? 126 VAL   B O   1 
ATOM   1585 O  O   B VAL   B 2 117 ? 13.362  16.180 -20.959 0.14 41.18  ? 126 VAL   B O   1 
ATOM   1586 O  O   C VAL   B 2 117 ? 13.143  16.327 -21.102 0.36 42.33  ? 126 VAL   B O   1 
ATOM   1587 O  O   D VAL   B 2 117 ? 13.368  16.174 -20.963 0.37 41.09  ? 126 VAL   B O   1 
ATOM   1588 C  CB  A VAL   B 2 117 ? 10.521  14.957 -21.785 0.13 43.40  ? 126 VAL   B CB  1 
ATOM   1589 C  CB  B VAL   B 2 117 ? 10.575  15.158 -21.679 0.14 40.61  ? 126 VAL   B CB  1 
ATOM   1590 C  CB  C VAL   B 2 117 ? 10.519  14.957 -21.781 0.36 43.63  ? 126 VAL   B CB  1 
ATOM   1591 C  CB  D VAL   B 2 117 ? 10.572  15.161 -21.679 0.37 40.39  ? 126 VAL   B CB  1 
ATOM   1592 C  CG1 A VAL   B 2 117 ? 9.515   13.897 -22.210 0.13 43.80  ? 126 VAL   B CG1 1 
ATOM   1593 C  CG1 B VAL   B 2 117 ? 10.390  15.969 -22.954 0.14 40.85  ? 126 VAL   B CG1 1 
ATOM   1594 C  CG1 C VAL   B 2 117 ? 9.516   13.893 -22.206 0.36 44.16  ? 126 VAL   B CG1 1 
ATOM   1595 C  CG1 D VAL   B 2 117 ? 10.391  15.967 -22.958 0.37 40.65  ? 126 VAL   B CG1 1 
ATOM   1596 C  CG2 A VAL   B 2 117 ? 10.074  15.619 -20.490 0.13 43.43  ? 126 VAL   B CG2 1 
ATOM   1597 C  CG2 B VAL   B 2 117 ? 9.409   14.198 -21.482 0.14 40.25  ? 126 VAL   B CG2 1 
ATOM   1598 C  CG2 C VAL   B 2 117 ? 10.072  15.616 -20.485 0.36 44.05  ? 126 VAL   B CG2 1 
ATOM   1599 C  CG2 D VAL   B 2 117 ? 9.402   14.203 -21.484 0.37 39.95  ? 126 VAL   B CG2 1 
ATOM   1600 N  N   . ALA   B 2 118 ? 13.855  15.207 -22.960 1.00 42.46  ? 127 ALA   B N   1 
ATOM   1601 C  CA  . ALA   B 2 118 ? 15.058  16.026 -23.256 1.00 43.68  ? 127 ALA   B CA  1 
ATOM   1602 C  C   . ALA   B 2 118 ? 14.711  17.099 -24.319 1.00 45.61  ? 127 ALA   B C   1 
ATOM   1603 O  O   . ALA   B 2 118 ? 15.030  16.868 -25.474 1.00 47.35  ? 127 ALA   B O   1 
ATOM   1604 C  CB  . ALA   B 2 118 ? 16.181  15.123 -23.772 1.00 43.92  ? 127 ALA   B CB  1 
ATOM   1605 N  N   . LEU   B 2 119 ? 14.061  18.215 -23.956 1.00 45.79  ? 128 LEU   B N   1 
ATOM   1606 C  CA  . LEU   B 2 119 ? 13.712  19.350 -24.858 1.00 44.82  ? 128 LEU   B CA  1 
ATOM   1607 C  C   . LEU   B 2 119 ? 14.106  20.654 -24.154 1.00 47.61  ? 128 LEU   B C   1 
ATOM   1608 O  O   . LEU   B 2 119 ? 13.874  20.736 -22.945 1.00 47.31  ? 128 LEU   B O   1 
ATOM   1609 C  CB  . LEU   B 2 119 ? 12.218  19.229 -25.141 1.00 43.29  ? 128 LEU   B CB  1 
ATOM   1610 C  CG  . LEU   B 2 119 ? 11.822  17.994 -25.951 1.00 43.43  ? 128 LEU   B CG  1 
ATOM   1611 C  CD1 . LEU   B 2 119 ? 10.318  17.807 -26.110 1.00 42.01  ? 128 LEU   B CD1 1 
ATOM   1612 C  CD2 . LEU   B 2 119 ? 12.466  18.128 -27.331 1.00 44.60  ? 128 LEU   B CD2 1 
ATOM   1613 N  N   . ASP   B 2 120 ? 14.704  21.628 -24.837 1.00 47.97  ? 129 ASP   B N   1 
ATOM   1614 C  CA  . ASP   B 2 120 ? 15.262  22.856 -24.198 1.00 50.40  ? 129 ASP   B CA  1 
ATOM   1615 C  C   . ASP   B 2 120 ? 14.265  24.021 -24.308 1.00 49.99  ? 129 ASP   B C   1 
ATOM   1616 O  O   . ASP   B 2 120 ? 14.258  24.683 -25.325 1.00 48.50  ? 129 ASP   B O   1 
ATOM   1617 C  CB  . ASP   B 2 120 ? 16.528  23.389 -24.883 1.00 53.84  ? 129 ASP   B CB  1 
ATOM   1618 C  CG  . ASP   B 2 120 ? 17.749  22.486 -24.841 1.00 56.12  ? 129 ASP   B CG  1 
ATOM   1619 O  OD1 . ASP   B 2 120 ? 17.871  21.657 -23.881 1.00 57.88  ? 129 ASP   B OD1 1 
ATOM   1620 O  OD2 . ASP   B 2 120 ? 18.590  22.637 -25.777 1.00 58.64  ? 129 ASP   B OD2 1 
ATOM   1621 N  N   . TYR   B 2 121 ? 13.465  24.294 -23.296 1.00 45.75  ? 130 TYR   B N   1 
ATOM   1622 C  CA  . TYR   B 2 121 ? 12.588  25.498 -23.197 1.00 45.38  ? 130 TYR   B CA  1 
ATOM   1623 C  C   . TYR   B 2 121 ? 12.987  26.305 -21.945 1.00 45.60  ? 130 TYR   B C   1 
ATOM   1624 O  O   . TYR   B 2 121 ? 13.693  25.776 -21.079 1.00 45.07  ? 130 TYR   B O   1 
ATOM   1625 C  CB  . TYR   B 2 121 ? 11.142  25.030 -23.136 1.00 44.42  ? 130 TYR   B CB  1 
ATOM   1626 C  CG  . TYR   B 2 121 ? 10.629  24.531 -24.456 1.00 45.16  ? 130 TYR   B CG  1 
ATOM   1627 C  CD1 . TYR   B 2 121 ? 10.179  25.445 -25.389 1.00 47.26  ? 130 TYR   B CD1 1 
ATOM   1628 C  CD2 . TYR   B 2 121 ? 10.644  23.188 -24.806 1.00 46.00  ? 130 TYR   B CD2 1 
ATOM   1629 C  CE1 . TYR   B 2 121 ? 9.692   25.036 -26.613 1.00 47.28  ? 130 TYR   B CE1 1 
ATOM   1630 C  CE2 . TYR   B 2 121 ? 10.204  22.769 -26.057 1.00 47.79  ? 130 TYR   B CE2 1 
ATOM   1631 C  CZ  . TYR   B 2 121 ? 9.731   23.700 -26.961 1.00 48.54  ? 130 TYR   B CZ  1 
ATOM   1632 O  OH  . TYR   B 2 121 ? 9.297   23.345 -28.214 1.00 47.69  ? 130 TYR   B OH  1 
ATOM   1633 N  N   . PRO   B 2 122 ? 12.690  27.631 -21.881 1.00 45.78  ? 131 PRO   B N   1 
ATOM   1634 C  CA  . PRO   B 2 122 ? 13.069  28.462 -20.731 1.00 47.44  ? 131 PRO   B CA  1 
ATOM   1635 C  C   . PRO   B 2 122 ? 12.201  28.111 -19.508 1.00 43.65  ? 131 PRO   B C   1 
ATOM   1636 O  O   . PRO   B 2 122 ? 11.218  27.463 -19.662 1.00 42.05  ? 131 PRO   B O   1 
ATOM   1637 C  CB  . PRO   B 2 122 ? 12.840  29.906 -21.180 1.00 47.71  ? 131 PRO   B CB  1 
ATOM   1638 C  CG  . PRO   B 2 122 ? 11.867  29.790 -22.337 1.00 47.36  ? 131 PRO   B CG  1 
ATOM   1639 C  CD  . PRO   B 2 122 ? 12.050  28.412 -22.941 1.00 46.86  ? 131 PRO   B CD  1 
ATOM   1640 N  N   . ALA   B 2 123 ? 12.593  28.521 -18.312 1.00 47.03  ? 132 ALA   B N   1 
ATOM   1641 C  CA  . ALA   B 2 123 ? 11.913  28.090 -17.068 1.00 44.52  ? 132 ALA   B CA  1 
ATOM   1642 C  C   . ALA   B 2 123 ? 10.394  28.336 -17.084 1.00 43.68  ? 132 ALA   B C   1 
ATOM   1643 O  O   . ALA   B 2 123 ? 9.630   27.566 -16.398 1.00 43.02  ? 132 ALA   B O   1 
ATOM   1644 C  CB  . ALA   B 2 123 ? 12.568  28.722 -15.831 1.00 45.05  ? 132 ALA   B CB  1 
ATOM   1645 N  N   . GLY   B 2 124 ? 9.934   29.412 -17.703 1.00 41.11  ? 133 GLY   B N   1 
ATOM   1646 C  CA  . GLY   B 2 124 ? 8.511   29.809 -17.751 1.00 40.28  ? 133 GLY   B CA  1 
ATOM   1647 C  C   . GLY   B 2 124 ? 7.630   28.785 -18.446 1.00 39.51  ? 133 GLY   B C   1 
ATOM   1648 O  O   . GLY   B 2 124 ? 6.395   28.956 -18.368 1.00 38.87  ? 133 GLY   B O   1 
ATOM   1649 N  N   . THR   B 2 125 ? 8.221   27.786 -19.116 1.00 38.29  ? 134 THR   B N   1 
ATOM   1650 C  CA  . THR   B 2 125 ? 7.489   26.646 -19.742 1.00 38.10  ? 134 THR   B CA  1 
ATOM   1651 C  C   . THR   B 2 125 ? 7.122   25.544 -18.723 1.00 37.22  ? 134 THR   B C   1 
ATOM   1652 O  O   . THR   B 2 125 ? 6.311   24.616 -19.089 1.00 36.29  ? 134 THR   B O   1 
ATOM   1653 C  CB  . THR   B 2 125 ? 8.313   26.125 -20.925 1.00 39.40  ? 134 THR   B CB  1 
ATOM   1654 O  OG1 . THR   B 2 125 ? 8.949   27.250 -21.569 1.00 40.09  ? 134 THR   B OG1 1 
ATOM   1655 C  CG2 . THR   B 2 125 ? 7.506   25.460 -22.024 1.00 41.26  ? 134 THR   B CG2 1 
ATOM   1656 N  N   . SER   B 2 126 ? 7.661   25.676 -17.491 1.00 36.87  ? 135 SER   B N   1 
ATOM   1657 C  CA  . SER   B 2 126 ? 7.451   24.739 -16.321 1.00 36.34  ? 135 SER   B CA  1 
ATOM   1658 C  C   . SER   B 2 126 ? 5.947   24.451 -16.183 1.00 34.91  ? 135 SER   B C   1 
ATOM   1659 O  O   . SER   B 2 126 ? 5.154   25.393 -16.124 1.00 35.35  ? 135 SER   B O   1 
ATOM   1660 C  CB  . SER   B 2 126 ? 7.984   25.309 -15.041 1.00 37.45  ? 135 SER   B CB  1 
ATOM   1661 O  OG  . SER   B 2 126 ? 9.406   25.276 -14.912 1.00 38.27  ? 135 SER   B OG  1 
ATOM   1662 N  N   . GLY   B 2 127 ? 5.543   23.192 -16.163 1.00 34.24  ? 136 GLY   B N   1 
ATOM   1663 C  CA  . GLY   B 2 127 ? 4.129   22.804 -15.958 1.00 34.33  ? 136 GLY   B CA  1 
ATOM   1664 C  C   . GLY   B 2 127 ? 3.409   22.456 -17.234 1.00 34.75  ? 136 GLY   B C   1 
ATOM   1665 O  O   . GLY   B 2 127 ? 2.191   22.046 -17.177 1.00 34.55  ? 136 GLY   B O   1 
ATOM   1666 N  N   . SER   B 2 128 ? 4.104   22.659 -18.378 1.00 34.86  ? 137 SER   B N   1 
ATOM   1667 C  CA  . SER   B 2 128 ? 3.496   22.209 -19.635 1.00 34.45  ? 137 SER   B CA  1 
ATOM   1668 C  C   . SER   B 2 128 ? 3.255   20.708 -19.548 1.00 33.74  ? 137 SER   B C   1 
ATOM   1669 O  O   . SER   B 2 128 ? 4.110   19.956 -19.074 1.00 35.38  ? 137 SER   B O   1 
ATOM   1670 C  CB  . SER   B 2 128 ? 4.335   22.563 -20.906 1.00 34.65  ? 137 SER   B CB  1 
ATOM   1671 O  OG  . SER   B 2 128 ? 4.560   23.983 -21.047 1.00 36.70  ? 137 SER   B OG  1 
ATOM   1672 N  N   . PRO   B 2 129 ? 2.094   20.223 -20.032 1.00 34.11  ? 138 PRO   B N   1 
ATOM   1673 C  CA  . PRO   B 2 129 ? 1.760   18.820 -19.937 1.00 33.33  ? 138 PRO   B CA  1 
ATOM   1674 C  C   . PRO   B 2 129 ? 2.430   17.897 -20.942 1.00 35.71  ? 138 PRO   B C   1 
ATOM   1675 O  O   . PRO   B 2 129 ? 2.625   18.342 -22.108 1.00 35.46  ? 138 PRO   B O   1 
ATOM   1676 C  CB  . PRO   B 2 129 ? 0.248   18.798 -20.129 1.00 34.66  ? 138 PRO   B CB  1 
ATOM   1677 C  CG  . PRO   B 2 129 ? -0.056  20.022 -21.006 1.00 34.80  ? 138 PRO   B CG  1 
ATOM   1678 C  CD  . PRO   B 2 129 ? 0.988   21.040 -20.571 1.00 34.57  ? 138 PRO   B CD  1 
ATOM   1679 N  N   . ILE   B 2 130 ? 2.641   16.648 -20.535 1.00 34.51  ? 139 ILE   B N   1 
ATOM   1680 C  CA  . ILE   B 2 130 ? 3.186   15.539 -21.373 1.00 36.10  ? 139 ILE   B CA  1 
ATOM   1681 C  C   . ILE   B 2 130 ? 2.043   14.570 -21.644 1.00 37.83  ? 139 ILE   B C   1 
ATOM   1682 O  O   . ILE   B 2 130 ? 1.294   14.360 -20.764 1.00 36.73  ? 139 ILE   B O   1 
ATOM   1683 C  CB  . ILE   B 2 130 ? 4.409   14.890 -20.750 1.00 35.14  ? 139 ILE   B CB  1 
ATOM   1684 C  CG1 . ILE   B 2 130 ? 5.487   15.946 -20.502 1.00 36.16  ? 139 ILE   B CG1 1 
ATOM   1685 C  CG2 . ILE   B 2 130 ? 4.943   13.715 -21.528 1.00 36.60  ? 139 ILE   B CG2 1 
ATOM   1686 C  CD1 . ILE   B 2 130 ? 6.430   15.549 -19.416 1.00 36.41  ? 139 ILE   B CD1 1 
ATOM   1687 N  N   . LEU   B 2 131 ? 1.756   14.318 -22.936 1.00 38.65  ? 140 LEU   B N   1 
ATOM   1688 C  CA  . LEU   B 2 131 ? 0.559   13.536 -23.407 1.00 41.03  ? 140 LEU   B CA  1 
ATOM   1689 C  C   . LEU   B 2 131 ? 0.933   12.159 -23.995 1.00 41.13  ? 140 LEU   B C   1 
ATOM   1690 O  O   . LEU   B 2 131 ? 2.035   11.995 -24.631 1.00 40.67  ? 140 LEU   B O   1 
ATOM   1691 C  CB  . LEU   B 2 131 ? -0.215  14.279 -24.525 1.00 42.68  ? 140 LEU   B CB  1 
ATOM   1692 C  CG  . LEU   B 2 131 ? -0.265  15.806 -24.444 1.00 43.71  ? 140 LEU   B CG  1 
ATOM   1693 C  CD1 . LEU   B 2 131 ? -1.147  16.397 -25.531 1.00 45.25  ? 140 LEU   B CD1 1 
ATOM   1694 C  CD2 . LEU   B 2 131 ? -0.747  16.244 -23.052 1.00 44.49  ? 140 LEU   B CD2 1 
ATOM   1695 N  N   . ASP   B 2 132 ? 0.032   11.191 -23.794 1.00 41.97  ? 141 ASP   B N   1 
ATOM   1696 C  CA  . ASP   B 2 132 ? 0.131   9.886  -24.475 1.00 45.98  ? 141 ASP   B CA  1 
ATOM   1697 C  C   . ASP   B 2 132 ? -0.702  9.988  -25.771 1.00 46.74  ? 141 ASP   B C   1 
ATOM   1698 O  O   . ASP   B 2 132 ? -1.205  11.072 -26.032 1.00 44.80  ? 141 ASP   B O   1 
ATOM   1699 C  CB  . ASP   B 2 132 ? -0.254  8.724  -23.570 1.00 45.85  ? 141 ASP   B CB  1 
ATOM   1700 C  CG  . ASP   B 2 132 ? -1.712  8.588  -23.196 1.00 47.30  ? 141 ASP   B CG  1 
ATOM   1701 O  OD1 . ASP   B 2 132 ? -2.577  9.207  -23.847 1.00 46.74  ? 141 ASP   B OD1 1 
ATOM   1702 O  OD2 . ASP   B 2 132 ? -1.957  7.892  -22.164 1.00 49.15  ? 141 ASP   B OD2 1 
ATOM   1703 N  N   . LYS   B 2 133 ? -0.934  8.879  -26.459 1.00 50.25  ? 142 LYS   B N   1 
ATOM   1704 C  CA  . LYS   B 2 133 ? -1.552  8.915  -27.822 1.00 53.48  ? 142 LYS   B CA  1 
ATOM   1705 C  C   . LYS   B 2 133 ? -3.072  9.009  -27.707 1.00 54.17  ? 142 LYS   B C   1 
ATOM   1706 O  O   . LYS   B 2 133 ? -3.691  9.368  -28.710 1.00 56.02  ? 142 LYS   B O   1 
ATOM   1707 C  CB  . LYS   B 2 133 ? -1.128  7.691  -28.636 1.00 58.02  ? 142 LYS   B CB  1 
ATOM   1708 C  CG  . LYS   B 2 133 ? 0.312   7.773  -29.115 1.00 62.61  ? 142 LYS   B CG  1 
ATOM   1709 C  CD  . LYS   B 2 133 ? 0.994   6.455  -29.505 1.00 65.99  ? 142 LYS   B CD  1 
ATOM   1710 C  CE  . LYS   B 2 133 ? 2.477   6.667  -29.752 1.00 68.53  ? 142 LYS   B CE  1 
ATOM   1711 N  NZ  . LYS   B 2 133 ? 3.191   5.428  -30.153 1.00 69.81  ? 142 LYS   B NZ  1 
ATOM   1712 N  N   . CYS   B 2 134 ? -3.646  8.673  -26.539 1.00 54.06  ? 143 CYS   B N   1 
ATOM   1713 C  CA  . CYS   B 2 134 ? -5.089  8.863  -26.270 1.00 53.60  ? 143 CYS   B CA  1 
ATOM   1714 C  C   . CYS   B 2 134 ? -5.389  10.310 -25.835 1.00 49.67  ? 143 CYS   B C   1 
ATOM   1715 O  O   . CYS   B 2 134 ? -6.544  10.590 -25.636 1.00 49.37  ? 143 CYS   B O   1 
ATOM   1716 C  CB  . CYS   B 2 134 ? -5.579  7.849  -25.256 1.00 56.16  ? 143 CYS   B CB  1 
ATOM   1717 S  SG  . CYS   B 2 134 ? -5.827  6.203  -25.967 1.00 60.46  ? 143 CYS   B SG  1 
ATOM   1718 N  N   . GLY   B 2 135 ? -4.415  11.222 -25.860 1.00 47.51  ? 144 GLY   B N   1 
ATOM   1719 C  CA  . GLY   B 2 135 ? -4.537  12.608 -25.377 1.00 47.21  ? 144 GLY   B CA  1 
ATOM   1720 C  C   . GLY   B 2 135 ? -4.445  12.754 -23.834 1.00 45.83  ? 144 GLY   B C   1 
ATOM   1721 O  O   . GLY   B 2 135 ? -4.698  13.884 -23.341 1.00 43.24  ? 144 GLY   B O   1 
ATOM   1722 N  N   . ARG   B 2 136 ? -4.178  11.676 -23.077 1.00 44.17  ? 145 ARG   B N   1 
ATOM   1723 C  CA  . ARG   B 2 136 ? -4.149  11.742 -21.588 1.00 44.82  ? 145 ARG   B CA  1 
ATOM   1724 C  C   . ARG   B 2 136 ? -2.841  12.344 -21.075 1.00 41.67  ? 145 ARG   B C   1 
ATOM   1725 O  O   . ARG   B 2 136 ? -1.727  12.053 -21.566 1.00 40.54  ? 145 ARG   B O   1 
ATOM   1726 C  CB  . ARG   B 2 136 ? -4.391  10.359 -20.984 1.00 46.19  ? 145 ARG   B CB  1 
ATOM   1727 C  CG  . ARG   B 2 136 ? -5.810  9.852  -21.193 1.00 47.64  ? 145 ARG   B CG  1 
ATOM   1728 C  CD  . ARG   B 2 136 ? -5.894  8.419  -20.784 1.00 50.83  ? 145 ARG   B CD  1 
ATOM   1729 N  NE  . ARG   B 2 136 ? -4.950  7.679  -21.568 1.00 58.68  ? 145 ARG   B NE  1 
ATOM   1730 C  CZ  . ARG   B 2 136 ? -4.507  6.461  -21.322 1.00 61.67  ? 145 ARG   B CZ  1 
ATOM   1731 N  NH1 . ARG   B 2 136 ? -4.878  5.825  -20.228 1.00 64.91  ? 145 ARG   B NH1 1 
ATOM   1732 N  NH2 . ARG   B 2 136 ? -3.703  5.881  -22.201 1.00 63.51  ? 145 ARG   B NH2 1 
ATOM   1733 N  N   . VAL   B 2 137 ? -2.965  13.079 -19.984 1.00 40.83  ? 146 VAL   B N   1 
ATOM   1734 C  CA  . VAL   B 2 137 ? -1.785  13.745 -19.401 1.00 40.53  ? 146 VAL   B CA  1 
ATOM   1735 C  C   . VAL   B 2 137 ? -1.084  12.714 -18.506 1.00 41.17  ? 146 VAL   B C   1 
ATOM   1736 O  O   . VAL   B 2 137 ? -1.715  12.194 -17.562 1.00 41.55  ? 146 VAL   B O   1 
ATOM   1737 C  CB  . VAL   B 2 137 ? -2.173  15.002 -18.617 1.00 39.28  ? 146 VAL   B CB  1 
ATOM   1738 C  CG1 . VAL   B 2 137 ? -0.910  15.643 -18.076 1.00 38.96  ? 146 VAL   B CG1 1 
ATOM   1739 C  CG2 . VAL   B 2 137 ? -2.927  15.975 -19.543 1.00 39.08  ? 146 VAL   B CG2 1 
ATOM   1740 N  N   . ILE   B 2 138 ? 0.157   12.388 -18.849 1.00 39.37  ? 147 ILE   B N   1 
ATOM   1741 C  CA  . ILE   B 2 138 ? 0.981   11.366 -18.136 1.00 37.73  ? 147 ILE   B CA  1 
ATOM   1742 C  C   . ILE   B 2 138 ? 1.955   12.079 -17.196 1.00 36.02  ? 147 ILE   B C   1 
ATOM   1743 O  O   . ILE   B 2 138 ? 2.720   11.341 -16.498 1.00 35.24  ? 147 ILE   B O   1 
ATOM   1744 C  CB  . ILE   B 2 138 ? 1.695   10.438 -19.161 1.00 39.14  ? 147 ILE   B CB  1 
ATOM   1745 C  CG1 . ILE   B 2 138 ? 2.598   11.191 -20.138 1.00 39.34  ? 147 ILE   B CG1 1 
ATOM   1746 C  CG2 . ILE   B 2 138 ? 0.665   9.603  -19.882 1.00 38.25  ? 147 ILE   B CG2 1 
ATOM   1747 C  CD1 . ILE   B 2 138 ? 3.581   10.305 -20.960 1.00 39.86  ? 147 ILE   B CD1 1 
ATOM   1748 N  N   . GLY   B 2 139 ? 1.963   13.412 -17.164 1.00 35.66  ? 148 GLY   B N   1 
ATOM   1749 C  CA  . GLY   B 2 139 ? 2.800   14.201 -16.232 1.00 34.52  ? 148 GLY   B CA  1 
ATOM   1750 C  C   . GLY   B 2 139 ? 3.073   15.594 -16.705 1.00 34.69  ? 148 GLY   B C   1 
ATOM   1751 O  O   . GLY   B 2 139 ? 2.605   15.990 -17.866 1.00 35.19  ? 148 GLY   B O   1 
ATOM   1752 N  N   A LEU   B 2 140 ? 3.795   16.362 -15.884 0.13 33.94  ? 149 LEU   B N   1 
ATOM   1753 N  N   B LEU   B 2 140 ? 3.795   16.361 -15.885 0.14 33.94  ? 149 LEU   B N   1 
ATOM   1754 N  N   C LEU   B 2 140 ? 3.830   16.350 -15.902 0.36 33.97  ? 149 LEU   B N   1 
ATOM   1755 N  N   D LEU   B 2 140 ? 3.830   16.350 -15.902 0.37 33.97  ? 149 LEU   B N   1 
ATOM   1756 C  CA  A LEU   B 2 140 ? 4.159   17.771 -16.167 0.13 33.88  ? 149 LEU   B CA  1 
ATOM   1757 C  CA  B LEU   B 2 140 ? 4.159   17.771 -16.167 0.14 33.88  ? 149 LEU   B CA  1 
ATOM   1758 C  CA  C LEU   B 2 140 ? 4.176   17.760 -16.185 0.36 34.51  ? 149 LEU   B CA  1 
ATOM   1759 C  CA  D LEU   B 2 140 ? 4.176   17.760 -16.185 0.37 34.51  ? 149 LEU   B CA  1 
ATOM   1760 C  C   A LEU   B 2 140 ? 5.670   17.862 -16.379 0.13 34.20  ? 149 LEU   B C   1 
ATOM   1761 C  C   B LEU   B 2 140 ? 5.669   17.862 -16.378 0.14 34.20  ? 149 LEU   B C   1 
ATOM   1762 C  C   C LEU   B 2 140 ? 5.683   17.891 -16.353 0.36 35.34  ? 149 LEU   B C   1 
ATOM   1763 C  C   D LEU   B 2 140 ? 5.683   17.891 -16.353 0.37 35.34  ? 149 LEU   B C   1 
ATOM   1764 O  O   A LEU   B 2 140 ? 6.421   17.292 -15.577 0.13 33.21  ? 149 LEU   B O   1 
ATOM   1765 O  O   B LEU   B 2 140 ? 6.421   17.291 -15.578 0.14 33.21  ? 149 LEU   B O   1 
ATOM   1766 O  O   C LEU   B 2 140 ? 6.428   17.102 -15.720 0.36 34.24  ? 149 LEU   B O   1 
ATOM   1767 O  O   D LEU   B 2 140 ? 6.428   17.102 -15.720 0.37 34.24  ? 149 LEU   B O   1 
ATOM   1768 C  CB  A LEU   B 2 140 ? 3.705   18.681 -15.024 0.13 33.72  ? 149 LEU   B CB  1 
ATOM   1769 C  CB  B LEU   B 2 140 ? 3.705   18.681 -15.024 0.14 33.73  ? 149 LEU   B CB  1 
ATOM   1770 C  CB  C LEU   B 2 140 ? 3.691   18.718 -15.102 0.36 34.68  ? 149 LEU   B CB  1 
ATOM   1771 C  CB  D LEU   B 2 140 ? 3.691   18.718 -15.102 0.37 34.68  ? 149 LEU   B CB  1 
ATOM   1772 C  CG  A LEU   B 2 140 ? 2.227   18.600 -14.642 0.13 33.48  ? 149 LEU   B CG  1 
ATOM   1773 C  CG  B LEU   B 2 140 ? 2.227   18.600 -14.642 0.14 33.48  ? 149 LEU   B CG  1 
ATOM   1774 C  CG  C LEU   B 2 140 ? 2.209   18.669 -14.733 0.36 34.57  ? 149 LEU   B CG  1 
ATOM   1775 C  CG  D LEU   B 2 140 ? 2.210   18.669 -14.733 0.37 34.57  ? 149 LEU   B CG  1 
ATOM   1776 C  CD1 A LEU   B 2 140 ? 1.896   19.654 -13.604 0.13 33.25  ? 149 LEU   B CD1 1 
ATOM   1777 C  CD1 B LEU   B 2 140 ? 1.896   19.655 -13.605 0.14 33.25  ? 149 LEU   B CD1 1 
ATOM   1778 C  CD1 C LEU   B 2 140 ? 1.884   19.814 -13.805 0.36 34.02  ? 149 LEU   B CD1 1 
ATOM   1779 C  CD1 D LEU   B 2 140 ? 1.884   19.815 -13.806 0.37 34.02  ? 149 LEU   B CD1 1 
ATOM   1780 C  CD2 A LEU   B 2 140 ? 1.326   18.767 -15.857 0.13 33.31  ? 149 LEU   B CD2 1 
ATOM   1781 C  CD2 B LEU   B 2 140 ? 1.326   18.766 -15.857 0.14 33.31  ? 149 LEU   B CD2 1 
ATOM   1782 C  CD2 C LEU   B 2 140 ? 1.322   18.747 -15.956 0.36 34.08  ? 149 LEU   B CD2 1 
ATOM   1783 C  CD2 D LEU   B 2 140 ? 1.321   18.746 -15.956 0.37 34.08  ? 149 LEU   B CD2 1 
ATOM   1784 N  N   A TYR   B 2 141 ? 6.076   18.501 -17.480 0.13 34.10  ? 150 TYR   B N   1 
ATOM   1785 N  N   B TYR   B 2 141 ? 6.075   18.501 -17.480 0.14 34.10  ? 150 TYR   B N   1 
ATOM   1786 N  N   C TYR   B 2 141 ? 6.073   18.800 -17.270 0.36 35.26  ? 150 TYR   B N   1 
ATOM   1787 N  N   D TYR   B 2 141 ? 6.073   18.800 -17.271 0.37 35.26  ? 150 TYR   B N   1 
ATOM   1788 C  CA  A TYR   B 2 141 ? 7.478   18.893 -17.775 0.13 34.88  ? 150 TYR   B CA  1 
ATOM   1789 C  CA  B TYR   B 2 141 ? 7.478   18.892 -17.775 0.14 34.88  ? 150 TYR   B CA  1 
ATOM   1790 C  CA  C TYR   B 2 141 ? 7.474   19.090 -17.665 0.36 36.15  ? 150 TYR   B CA  1 
ATOM   1791 C  CA  D TYR   B 2 141 ? 7.474   19.090 -17.665 0.37 36.15  ? 150 TYR   B CA  1 
ATOM   1792 C  C   A TYR   B 2 141 ? 7.808   20.153 -16.979 0.13 34.88  ? 150 TYR   B C   1 
ATOM   1793 C  C   B TYR   B 2 141 ? 7.808   20.152 -16.979 0.14 34.88  ? 150 TYR   B C   1 
ATOM   1794 C  C   C TYR   B 2 141 ? 7.979   20.299 -16.874 0.36 36.64  ? 150 TYR   B C   1 
ATOM   1795 C  C   D TYR   B 2 141 ? 7.979   20.298 -16.874 0.37 36.64  ? 150 TYR   B C   1 
ATOM   1796 O  O   A TYR   B 2 141 ? 7.020   21.108 -17.084 0.13 35.24  ? 150 TYR   B O   1 
ATOM   1797 O  O   B TYR   B 2 141 ? 7.021   21.106 -17.085 0.14 35.24  ? 150 TYR   B O   1 
ATOM   1798 O  O   C TYR   B 2 141 ? 7.203   21.259 -16.711 0.36 37.79  ? 150 TYR   B O   1 
ATOM   1799 O  O   D TYR   B 2 141 ? 7.204   21.259 -16.711 0.37 37.79  ? 150 TYR   B O   1 
ATOM   1800 C  CB  A TYR   B 2 141 ? 7.641   19.175 -19.275 0.13 35.31  ? 150 TYR   B CB  1 
ATOM   1801 C  CB  B TYR   B 2 141 ? 7.641   19.174 -19.274 0.14 35.30  ? 150 TYR   B CB  1 
ATOM   1802 C  CB  C TYR   B 2 141 ? 7.504   19.306 -19.191 0.36 36.66  ? 150 TYR   B CB  1 
ATOM   1803 C  CB  D TYR   B 2 141 ? 7.503   19.306 -19.191 0.37 36.66  ? 150 TYR   B CB  1 
ATOM   1804 C  CG  A TYR   B 2 141 ? 8.866   19.952 -19.699 0.13 35.97  ? 150 TYR   B CG  1 
ATOM   1805 C  CG  B TYR   B 2 141 ? 8.867   19.951 -19.698 0.14 35.96  ? 150 TYR   B CG  1 
ATOM   1806 C  CG  C TYR   B 2 141 ? 8.693   20.024 -19.776 0.36 37.58  ? 150 TYR   B CG  1 
ATOM   1807 C  CG  D TYR   B 2 141 ? 8.693   20.023 -19.776 0.37 37.58  ? 150 TYR   B CG  1 
ATOM   1808 C  CD1 A TYR   B 2 141 ? 8.908   21.340 -19.646 0.13 36.24  ? 150 TYR   B CD1 1 
ATOM   1809 C  CD1 B TYR   B 2 141 ? 8.908   21.339 -19.646 0.14 36.24  ? 150 TYR   B CD1 1 
ATOM   1810 C  CD1 C TYR   B 2 141 ? 9.699   19.321 -20.433 0.36 38.31  ? 150 TYR   B CD1 1 
ATOM   1811 C  CD1 D TYR   B 2 141 ? 9.699   19.320 -20.433 0.37 38.30  ? 150 TYR   B CD1 1 
ATOM   1812 C  CD2 A TYR   B 2 141 ? 9.960   19.302 -20.250 0.13 36.51  ? 150 TYR   B CD2 1 
ATOM   1813 C  CD2 B TYR   B 2 141 ? 9.961   19.300 -20.249 0.14 36.50  ? 150 TYR   B CD2 1 
ATOM   1814 C  CD2 C TYR   B 2 141 ? 8.752   21.412 -19.813 0.36 38.17  ? 150 TYR   B CD2 1 
ATOM   1815 C  CD2 D TYR   B 2 141 ? 8.752   21.411 -19.813 0.37 38.17  ? 150 TYR   B CD2 1 
ATOM   1816 C  CE1 A TYR   B 2 141 ? 10.014  22.052 -20.099 0.13 36.81  ? 150 TYR   B CE1 1 
ATOM   1817 C  CE1 B TYR   B 2 141 ? 10.014  22.051 -20.100 0.14 36.82  ? 150 TYR   B CE1 1 
ATOM   1818 C  CE1 C TYR   B 2 141 ? 10.746  19.971 -21.078 0.36 38.81  ? 150 TYR   B CE1 1 
ATOM   1819 C  CE1 D TYR   B 2 141 ? 10.746  19.970 -21.079 0.37 38.81  ? 150 TYR   B CE1 1 
ATOM   1820 C  CE2 A TYR   B 2 141 ? 11.070  19.997 -20.707 0.13 37.08  ? 150 TYR   B CE2 1 
ATOM   1821 C  CE2 B TYR   B 2 141 ? 11.071  19.996 -20.707 0.14 37.08  ? 150 TYR   B CE2 1 
ATOM   1822 C  CE2 C TYR   B 2 141 ? 9.796   22.077 -20.454 0.36 38.66  ? 150 TYR   B CE2 1 
ATOM   1823 C  CE2 D TYR   B 2 141 ? 9.796   22.077 -20.454 0.37 38.66  ? 150 TYR   B CE2 1 
ATOM   1824 C  CZ  A TYR   B 2 141 ? 11.106  21.379 -20.627 0.13 37.31  ? 150 TYR   B CZ  1 
ATOM   1825 C  CZ  B TYR   B 2 141 ? 11.106  21.378 -20.627 0.14 37.31  ? 150 TYR   B CZ  1 
ATOM   1826 C  CZ  C TYR   B 2 141 ? 10.804  21.358 -21.077 0.36 39.09  ? 150 TYR   B CZ  1 
ATOM   1827 C  CZ  D TYR   B 2 141 ? 10.804  21.357 -21.078 0.37 39.09  ? 150 TYR   B CZ  1 
ATOM   1828 O  OH  A TYR   B 2 141 ? 12.211  22.046 -21.094 0.13 37.74  ? 150 TYR   B OH  1 
ATOM   1829 O  OH  B TYR   B 2 141 ? 12.212  22.045 -21.095 0.14 37.73  ? 150 TYR   B OH  1 
ATOM   1830 O  OH  C TYR   B 2 141 ? 11.859  22.029 -21.648 0.36 39.36  ? 150 TYR   B OH  1 
ATOM   1831 O  OH  D TYR   B 2 141 ? 11.859  22.029 -21.648 0.37 39.36  ? 150 TYR   B OH  1 
ATOM   1832 N  N   A GLY   B 2 142 ? 8.929   20.174 -16.248 0.13 35.22  ? 151 GLY   B N   1 
ATOM   1833 N  N   B GLY   B 2 142 ? 8.928   20.173 -16.248 0.14 35.22  ? 151 GLY   B N   1 
ATOM   1834 N  N   C GLY   B 2 142 ? 9.222   20.264 -16.377 0.36 37.38  ? 151 GLY   B N   1 
ATOM   1835 N  N   D GLY   B 2 142 ? 9.223   20.263 -16.378 0.37 37.38  ? 151 GLY   B N   1 
ATOM   1836 C  CA  A GLY   B 2 142 ? 9.383   21.417 -15.589 0.13 35.63  ? 151 GLY   B CA  1 
ATOM   1837 C  CA  B GLY   B 2 142 ? 9.382   21.417 -15.590 0.14 35.63  ? 151 GLY   B CA  1 
ATOM   1838 C  CA  C GLY   B 2 142 ? 9.807   21.456 -15.718 0.36 37.92  ? 151 GLY   B CA  1 
ATOM   1839 C  CA  D GLY   B 2 142 ? 9.807   21.456 -15.718 0.37 37.92  ? 151 GLY   B CA  1 
ATOM   1840 C  C   A GLY   B 2 142 ? 10.259  21.234 -14.357 0.13 35.57  ? 151 GLY   B C   1 
ATOM   1841 C  C   B GLY   B 2 142 ? 10.258  21.234 -14.357 0.14 35.57  ? 151 GLY   B C   1 
ATOM   1842 C  C   C GLY   B 2 142 ? 10.543  21.190 -14.410 0.36 37.94  ? 151 GLY   B C   1 
ATOM   1843 C  C   D GLY   B 2 142 ? 10.543  21.190 -14.410 0.37 37.94  ? 151 GLY   B C   1 
ATOM   1844 O  O   A GLY   B 2 142 ? 10.710  22.290 -13.826 0.13 35.71  ? 151 GLY   B O   1 
ATOM   1845 O  O   B GLY   B 2 142 ? 10.708  22.291 -13.827 0.14 35.71  ? 151 GLY   B O   1 
ATOM   1846 O  O   C GLY   B 2 142 ? 11.130  22.189 -13.851 0.36 38.69  ? 151 GLY   B O   1 
ATOM   1847 O  O   D GLY   B 2 142 ? 11.130  22.189 -13.852 0.37 38.69  ? 151 GLY   B O   1 
ATOM   1848 N  N   A ASN   B 2 143 ? 10.498  19.993 -13.898 0.13 35.80  ? 152 ASN   B N   1 
ATOM   1849 N  N   B ASN   B 2 143 ? 10.498  19.993 -13.898 0.14 35.80  ? 152 ASN   B N   1 
ATOM   1850 N  N   C ASN   B 2 143 ? 10.564  19.932 -13.933 0.36 37.71  ? 152 ASN   B N   1 
ATOM   1851 N  N   D ASN   B 2 143 ? 10.564  19.932 -13.933 0.37 37.71  ? 152 ASN   B N   1 
ATOM   1852 C  CA  A ASN   B 2 143 ? 11.552  19.698 -12.877 0.13 35.79  ? 152 ASN   B CA  1 
ATOM   1853 C  CA  B ASN   B 2 143 ? 11.552  19.699 -12.877 0.14 35.79  ? 152 ASN   B CA  1 
ATOM   1854 C  CA  C ASN   B 2 143 ? 11.510  19.534 -12.842 0.36 37.06  ? 152 ASN   B CA  1 
ATOM   1855 C  CA  D ASN   B 2 143 ? 11.510  19.534 -12.842 0.37 37.06  ? 152 ASN   B CA  1 
ATOM   1856 C  C   A ASN   B 2 143 ? 12.515  18.645 -13.503 0.13 36.79  ? 152 ASN   B C   1 
ATOM   1857 C  C   B ASN   B 2 143 ? 12.514  18.646 -13.506 0.14 36.79  ? 152 ASN   B C   1 
ATOM   1858 C  C   C ASN   B 2 143 ? 12.534  18.534 -13.468 0.36 37.46  ? 152 ASN   B C   1 
ATOM   1859 C  C   D ASN   B 2 143 ? 12.534  18.534 -13.467 0.37 37.46  ? 152 ASN   B C   1 
ATOM   1860 O  O   A ASN   B 2 143 ? 11.995  17.484 -13.994 0.13 37.38  ? 152 ASN   B O   1 
ATOM   1861 O  O   B ASN   B 2 143 ? 11.993  17.484 -13.990 0.14 37.39  ? 152 ASN   B O   1 
ATOM   1862 O  O   C ASN   B 2 143 ? 12.096  17.280 -13.790 0.36 38.47  ? 152 ASN   B O   1 
ATOM   1863 O  O   D ASN   B 2 143 ? 12.097  17.281 -13.790 0.37 38.47  ? 152 ASN   B O   1 
ATOM   1864 C  CB  A ASN   B 2 143 ? 10.952  19.288 -11.515 0.13 34.96  ? 152 ASN   B CB  1 
ATOM   1865 C  CB  B ASN   B 2 143 ? 10.952  19.288 -11.515 0.14 34.96  ? 152 ASN   B CB  1 
ATOM   1866 C  CB  C ASN   B 2 143 ? 10.779  18.998 -11.593 0.36 36.16  ? 152 ASN   B CB  1 
ATOM   1867 C  CB  D ASN   B 2 143 ? 10.779  18.998 -11.593 0.37 36.16  ? 152 ASN   B CB  1 
ATOM   1868 C  CG  A ASN   B 2 143 ? 11.880  19.530 -10.335 0.13 34.66  ? 152 ASN   B CG  1 
ATOM   1869 C  CG  B ASN   B 2 143 ? 11.881  19.531 -10.335 0.14 34.65  ? 152 ASN   B CG  1 
ATOM   1870 C  CG  C ASN   B 2 143 ? 11.669  18.948 -10.367 0.36 36.03  ? 152 ASN   B CG  1 
ATOM   1871 C  CG  D ASN   B 2 143 ? 11.670  18.948 -10.367 0.37 36.03  ? 152 ASN   B CG  1 
ATOM   1872 O  OD1 A ASN   B 2 143 ? 12.756  20.397 -10.371 0.13 34.68  ? 152 ASN   B OD1 1 
ATOM   1873 O  OD1 B ASN   B 2 143 ? 12.756  20.398 -10.370 0.14 34.67  ? 152 ASN   B OD1 1 
ATOM   1874 O  OD1 C ASN   B 2 143 ? 12.617  19.739 -10.229 0.36 36.05  ? 152 ASN   B OD1 1 
ATOM   1875 O  OD1 D ASN   B 2 143 ? 12.616  19.740 -10.230 0.37 36.05  ? 152 ASN   B OD1 1 
ATOM   1876 N  ND2 A ASN   B 2 143 ? 11.682  18.783 -9.259  0.13 34.00  ? 152 ASN   B ND2 1 
ATOM   1877 N  ND2 B ASN   B 2 143 ? 11.683  18.783 -9.259  0.14 34.00  ? 152 ASN   B ND2 1 
ATOM   1878 N  ND2 C ASN   B 2 143 ? 11.334  18.050 -9.444  0.36 35.45  ? 152 ASN   B ND2 1 
ATOM   1879 N  ND2 D ASN   B 2 143 ? 11.335  18.050 -9.445  0.37 35.45  ? 152 ASN   B ND2 1 
ATOM   1880 N  N   . GLY   B 2 144 ? 13.853  19.020 -13.384 1.00 37.85  ? 153 GLY   B N   1 
ATOM   1881 C  CA  . GLY   B 2 144 ? 14.911  18.194 -13.970 1.00 39.25  ? 153 GLY   B CA  1 
ATOM   1882 C  C   . GLY   B 2 144 ? 16.286  18.745 -13.720 1.00 41.70  ? 153 GLY   B C   1 
ATOM   1883 O  O   . GLY   B 2 144 ? 16.535  19.406 -12.622 1.00 40.42  ? 153 GLY   B O   1 
ATOM   1884 N  N   A VAL   B 2 145 ? 17.196  18.510 -14.673 0.13 42.66  ? 154 VAL   B N   1 
ATOM   1885 N  N   B VAL   B 2 145 ? 17.196  18.510 -14.673 0.14 42.66  ? 154 VAL   B N   1 
ATOM   1886 N  N   C VAL   B 2 145 ? 17.196  18.506 -14.673 0.36 42.31  ? 154 VAL   B N   1 
ATOM   1887 N  N   D VAL   B 2 145 ? 17.170  18.508 -14.693 0.37 40.20  ? 154 VAL   B N   1 
ATOM   1888 C  CA  A VAL   B 2 145 ? 18.656  18.782 -14.529 0.13 44.30  ? 154 VAL   B CA  1 
ATOM   1889 C  CA  B VAL   B 2 145 ? 18.656  18.782 -14.529 0.14 44.30  ? 154 VAL   B CA  1 
ATOM   1890 C  CA  C VAL   B 2 145 ? 18.656  18.780 -14.530 0.36 44.01  ? 154 VAL   B CA  1 
ATOM   1891 C  CA  D VAL   B 2 145 ? 18.638  18.734 -14.602 0.37 40.74  ? 154 VAL   B CA  1 
ATOM   1892 C  C   A VAL   B 2 145 ? 19.207  19.355 -15.841 0.13 45.81  ? 154 VAL   B C   1 
ATOM   1893 C  C   B VAL   B 2 145 ? 19.207  19.355 -15.841 0.14 45.81  ? 154 VAL   B C   1 
ATOM   1894 C  C   C VAL   B 2 145 ? 19.197  19.369 -15.843 0.36 45.38  ? 154 VAL   B C   1 
ATOM   1895 C  C   D VAL   B 2 145 ? 19.072  19.512 -15.857 0.37 42.38  ? 154 VAL   B C   1 
ATOM   1896 O  O   A VAL   B 2 145 ? 18.643  19.043 -16.894 0.13 45.49  ? 154 VAL   B O   1 
ATOM   1897 O  O   B VAL   B 2 145 ? 18.643  19.043 -16.893 0.14 45.48  ? 154 VAL   B O   1 
ATOM   1898 O  O   C VAL   B 2 145 ? 18.650  19.033 -16.885 0.36 45.01  ? 154 VAL   B O   1 
ATOM   1899 O  O   D VAL   B 2 145 ? 18.334  19.454 -16.831 0.37 41.47  ? 154 VAL   B O   1 
ATOM   1900 C  CB  A VAL   B 2 145 ? 19.406  17.499 -14.119 0.13 45.06  ? 154 VAL   B CB  1 
ATOM   1901 C  CB  B VAL   B 2 145 ? 19.405  17.499 -14.119 0.14 45.07  ? 154 VAL   B CB  1 
ATOM   1902 C  CB  C VAL   B 2 145 ? 19.405  17.497 -14.123 0.36 45.28  ? 154 VAL   B CB  1 
ATOM   1903 C  CB  D VAL   B 2 145 ? 19.356  17.378 -14.441 0.37 40.14  ? 154 VAL   B CB  1 
ATOM   1904 C  CG1 A VAL   B 2 145 ? 19.408  16.446 -15.222 0.13 45.07  ? 154 VAL   B CG1 1 
ATOM   1905 C  CG1 B VAL   B 2 145 ? 19.408  16.446 -15.222 0.14 45.07  ? 154 VAL   B CG1 1 
ATOM   1906 C  CG1 C VAL   B 2 145 ? 19.408  16.443 -15.226 0.36 44.95  ? 154 VAL   B CG1 1 
ATOM   1907 C  CG1 D VAL   B 2 145 ? 20.868  17.509 -14.564 0.37 40.73  ? 154 VAL   B CG1 1 
ATOM   1908 C  CG2 A VAL   B 2 145 ? 20.822  17.802 -13.654 0.13 45.86  ? 154 VAL   B CG2 1 
ATOM   1909 C  CG2 B VAL   B 2 145 ? 20.822  17.802 -13.654 0.14 45.88  ? 154 VAL   B CG2 1 
ATOM   1910 C  CG2 C VAL   B 2 145 ? 20.819  17.805 -13.652 0.36 46.48  ? 154 VAL   B CG2 1 
ATOM   1911 C  CG2 D VAL   B 2 145 ? 18.989  16.715 -13.098 0.37 38.94  ? 154 VAL   B CG2 1 
ATOM   1912 N  N   A VAL   B 2 146 ? 20.300  20.123 -15.749 0.13 47.71  ? 155 VAL   B N   1 
ATOM   1913 N  N   B VAL   B 2 146 ? 20.300  20.122 -15.749 0.14 47.71  ? 155 VAL   B N   1 
ATOM   1914 N  N   C VAL   B 2 146 ? 20.128  20.327 -15.731 0.36 46.21  ? 155 VAL   B N   1 
ATOM   1915 N  N   D VAL   B 2 146 ? 20.129  20.324 -15.734 0.37 45.13  ? 155 VAL   B N   1 
ATOM   1916 C  CA  A VAL   B 2 146 ? 21.124  20.610 -16.895 0.13 49.82  ? 155 VAL   B CA  1 
ATOM   1917 C  CA  B VAL   B 2 146 ? 21.124  20.610 -16.896 0.14 49.82  ? 155 VAL   B CA  1 
ATOM   1918 C  CA  C VAL   B 2 146 ? 20.900  20.943 -16.849 0.36 48.25  ? 155 VAL   B CA  1 
ATOM   1919 C  CA  D VAL   B 2 146 ? 20.899  20.945 -16.849 0.37 47.67  ? 155 VAL   B CA  1 
ATOM   1920 C  C   A VAL   B 2 146 ? 22.276  19.617 -17.105 0.13 51.36  ? 155 VAL   B C   1 
ATOM   1921 C  C   B VAL   B 2 146 ? 22.276  19.616 -17.106 0.14 51.37  ? 155 VAL   B C   1 
ATOM   1922 C  C   C VAL   B 2 146 ? 22.197  20.151 -16.962 0.36 49.69  ? 155 VAL   B C   1 
ATOM   1923 C  C   D VAL   B 2 146 ? 22.197  20.153 -16.963 0.37 49.41  ? 155 VAL   B C   1 
ATOM   1924 O  O   A VAL   B 2 146 ? 23.166  19.548 -16.236 0.13 51.16  ? 155 VAL   B O   1 
ATOM   1925 O  O   B VAL   B 2 146 ? 23.166  19.547 -16.237 0.14 51.15  ? 155 VAL   B O   1 
ATOM   1926 O  O   C VAL   B 2 146 ? 22.802  19.885 -15.922 0.36 50.28  ? 155 VAL   B O   1 
ATOM   1927 O  O   D VAL   B 2 146 ? 22.801  19.887 -15.923 0.37 50.13  ? 155 VAL   B O   1 
ATOM   1928 C  CB  A VAL   B 2 146 ? 21.630  22.043 -16.638 0.13 50.43  ? 155 VAL   B CB  1 
ATOM   1929 C  CB  B VAL   B 2 146 ? 21.631  22.043 -16.638 0.14 50.44  ? 155 VAL   B CB  1 
ATOM   1930 C  CB  C VAL   B 2 146 ? 21.181  22.437 -16.594 0.36 49.10  ? 155 VAL   B CB  1 
ATOM   1931 C  CB  D VAL   B 2 146 ? 21.181  22.439 -16.594 0.37 48.81  ? 155 VAL   B CB  1 
ATOM   1932 C  CG1 A VAL   B 2 146 ? 22.441  22.582 -17.808 0.13 51.21  ? 155 VAL   B CG1 1 
ATOM   1933 C  CG1 B VAL   B 2 146 ? 22.442  22.582 -17.808 0.14 51.21  ? 155 VAL   B CG1 1 
ATOM   1934 C  CG1 C VAL   B 2 146 ? 22.018  23.056 -17.712 0.36 49.78  ? 155 VAL   B CG1 1 
ATOM   1935 C  CG1 D VAL   B 2 146 ? 22.018  23.057 -17.713 0.37 49.58  ? 155 VAL   B CG1 1 
ATOM   1936 C  CG2 A VAL   B 2 146 ? 20.486  22.993 -16.303 0.13 50.42  ? 155 VAL   B CG2 1 
ATOM   1937 C  CG2 B VAL   B 2 146 ? 20.487  22.992 -16.302 0.14 50.43  ? 155 VAL   B CG2 1 
ATOM   1938 C  CG2 C VAL   B 2 146 ? 19.896  23.234 -16.388 0.36 48.83  ? 155 VAL   B CG2 1 
ATOM   1939 C  CG2 D VAL   B 2 146 ? 19.896  23.236 -16.387 0.37 48.61  ? 155 VAL   B CG2 1 
ATOM   1940 N  N   A ILE   B 2 147 ? 22.262  18.874 -18.216 0.13 52.83  ? 156 ILE   B N   1 
ATOM   1941 N  N   B ILE   B 2 147 ? 22.262  18.874 -18.217 0.14 52.84  ? 156 ILE   B N   1 
ATOM   1942 N  N   C ILE   B 2 147 ? 22.607  19.774 -18.168 0.36 50.55  ? 156 ILE   B N   1 
ATOM   1943 N  N   D ILE   B 2 147 ? 22.606  19.773 -18.169 0.37 50.44  ? 156 ILE   B N   1 
ATOM   1944 C  CA  A ILE   B 2 147 ? 23.197  17.733 -18.473 0.13 53.97  ? 156 ILE   B CA  1 
ATOM   1945 C  CA  B ILE   B 2 147 ? 23.197  17.733 -18.474 0.14 53.97  ? 156 ILE   B CA  1 
ATOM   1946 C  CA  C ILE   B 2 147 ? 23.789  18.883 -18.364 0.36 51.37  ? 156 ILE   B CA  1 
ATOM   1947 C  CA  D ILE   B 2 147 ? 23.789  18.884 -18.365 0.37 51.31  ? 156 ILE   B CA  1 
ATOM   1948 C  C   A ILE   B 2 147 ? 24.518  18.252 -19.060 0.13 55.34  ? 156 ILE   B C   1 
ATOM   1949 C  C   B ILE   B 2 147 ? 24.518  18.252 -19.061 0.14 55.35  ? 156 ILE   B C   1 
ATOM   1950 C  C   C ILE   B 2 147 ? 24.655  19.450 -19.496 0.36 51.69  ? 156 ILE   B C   1 
ATOM   1951 C  C   D ILE   B 2 147 ? 24.655  19.451 -19.496 0.37 51.66  ? 156 ILE   B C   1 
ATOM   1952 O  O   A ILE   B 2 147 ? 24.584  19.450 -19.416 0.13 55.47  ? 156 ILE   B O   1 
ATOM   1953 O  O   B ILE   B 2 147 ? 24.585  19.450 -19.418 0.14 55.46  ? 156 ILE   B O   1 
ATOM   1954 O  O   C ILE   B 2 147 ? 24.107  20.192 -20.302 0.36 52.06  ? 156 ILE   B O   1 
ATOM   1955 O  O   D ILE   B 2 147 ? 24.107  20.193 -20.301 0.37 52.05  ? 156 ILE   B O   1 
ATOM   1956 C  CB  A ILE   B 2 147 ? 22.544  16.670 -19.381 0.13 54.14  ? 156 ILE   B CB  1 
ATOM   1957 C  CB  B ILE   B 2 147 ? 22.544  16.670 -19.381 0.14 54.13  ? 156 ILE   B CB  1 
ATOM   1958 C  CB  C ILE   B 2 147 ? 23.317  17.433 -18.594 0.36 51.86  ? 156 ILE   B CB  1 
ATOM   1959 C  CB  D ILE   B 2 147 ? 23.319  17.433 -18.596 0.37 51.82  ? 156 ILE   B CB  1 
ATOM   1960 C  CG1 A ILE   B 2 147 ? 22.181  17.228 -20.762 0.13 55.11  ? 156 ILE   B CG1 1 
ATOM   1961 C  CG1 B ILE   B 2 147 ? 22.181  17.227 -20.763 0.14 55.11  ? 156 ILE   B CG1 1 
ATOM   1962 C  CG1 C ILE   B 2 147 ? 22.389  17.299 -19.800 0.36 52.35  ? 156 ILE   B CG1 1 
ATOM   1963 C  CG1 D ILE   B 2 147 ? 22.391  17.298 -19.802 0.37 52.33  ? 156 ILE   B CG1 1 
ATOM   1964 C  CG2 A ILE   B 2 147 ? 21.345  16.044 -18.685 0.13 53.75  ? 156 ILE   B CG2 1 
ATOM   1965 C  CG2 B ILE   B 2 147 ? 21.345  16.044 -18.685 0.14 53.75  ? 156 ILE   B CG2 1 
ATOM   1966 C  CG2 C ILE   B 2 147 ? 22.657  16.898 -17.327 0.36 52.15  ? 156 ILE   B CG2 1 
ATOM   1967 C  CG2 D ILE   B 2 147 ? 22.657  16.897 -17.332 0.37 52.11  ? 156 ILE   B CG2 1 
ATOM   1968 C  CD1 A ILE   B 2 147 ? 21.980  16.166 -21.822 0.13 55.17  ? 156 ILE   B CD1 1 
ATOM   1969 C  CD1 B ILE   B 2 147 ? 21.981  16.163 -21.821 0.14 55.16  ? 156 ILE   B CD1 1 
ATOM   1970 C  CD1 C ILE   B 2 147 ? 21.855  15.897 -20.005 0.36 52.77  ? 156 ILE   B CD1 1 
ATOM   1971 C  CD1 D ILE   B 2 147 ? 21.855  15.897 -20.003 0.37 52.76  ? 156 ILE   B CD1 1 
ATOM   1972 N  N   A LYS   B 2 148 ? 25.512  17.358 -19.177 0.13 56.36  ? 157 LYS   B N   1 
ATOM   1973 N  N   B LYS   B 2 148 ? 25.513  17.358 -19.177 0.14 56.36  ? 157 LYS   B N   1 
ATOM   1974 N  N   C LYS   B 2 148 ? 25.971  19.210 -19.417 0.36 52.58  ? 157 LYS   B N   1 
ATOM   1975 N  N   D LYS   B 2 148 ? 25.971  19.211 -19.417 0.37 52.57  ? 157 LYS   B N   1 
ATOM   1976 C  CA  A LYS   B 2 148 ? 26.893  17.634 -19.671 0.13 57.42  ? 157 LYS   B CA  1 
ATOM   1977 C  CA  B LYS   B 2 148 ? 26.894  17.633 -19.671 0.14 57.42  ? 157 LYS   B CA  1 
ATOM   1978 C  CA  C LYS   B 2 148 ? 27.021  19.447 -20.454 0.36 53.63  ? 157 LYS   B CA  1 
ATOM   1979 C  CA  D LYS   B 2 148 ? 27.021  19.447 -20.454 0.37 53.62  ? 157 LYS   B CA  1 
ATOM   1980 C  C   A LYS   B 2 148 ? 26.864  18.632 -20.836 0.13 57.39  ? 157 LYS   B C   1 
ATOM   1981 C  C   B LYS   B 2 148 ? 26.864  18.631 -20.836 0.14 57.39  ? 157 LYS   B C   1 
ATOM   1982 C  C   C LYS   B 2 148 ? 27.015  20.885 -20.990 0.36 53.46  ? 157 LYS   B C   1 
ATOM   1983 C  C   D LYS   B 2 148 ? 27.016  20.884 -20.990 0.37 53.45  ? 157 LYS   B C   1 
ATOM   1984 O  O   A LYS   B 2 148 ? 27.736  19.521 -20.869 0.13 57.47  ? 157 LYS   B O   1 
ATOM   1985 O  O   B LYS   B 2 148 ? 27.736  19.520 -20.869 0.14 57.46  ? 157 LYS   B O   1 
ATOM   1986 O  O   C LYS   B 2 148 ? 27.667  21.745 -20.359 0.36 53.21  ? 157 LYS   B O   1 
ATOM   1987 O  O   D LYS   B 2 148 ? 27.667  21.745 -20.359 0.37 53.21  ? 157 LYS   B O   1 
ATOM   1988 C  CB  A LYS   B 2 148 ? 27.577  16.341 -20.135 0.13 58.61  ? 157 LYS   B CB  1 
ATOM   1989 C  CB  B LYS   B 2 148 ? 27.578  16.341 -20.135 0.14 58.61  ? 157 LYS   B CB  1 
ATOM   1990 C  CB  C LYS   B 2 148 ? 26.870  18.474 -21.625 0.36 55.44  ? 157 LYS   B CB  1 
ATOM   1991 C  CB  D LYS   B 2 148 ? 26.870  18.474 -21.625 0.37 55.44  ? 157 LYS   B CB  1 
ATOM   1992 C  CG  A LYS   B 2 148 ? 28.133  15.457 -19.025 0.13 59.16  ? 157 LYS   B CG  1 
ATOM   1993 C  CG  B LYS   B 2 148 ? 28.134  15.456 -19.025 0.14 59.18  ? 157 LYS   B CG  1 
ATOM   1994 C  CG  C LYS   B 2 148 ? 26.596  17.025 -21.269 0.36 56.10  ? 157 LYS   B CG  1 
ATOM   1995 C  CG  D LYS   B 2 148 ? 26.597  17.025 -21.269 0.37 56.10  ? 157 LYS   B CG  1 
ATOM   1996 C  CD  A LYS   B 2 148 ? 28.606  14.091 -19.496 0.13 59.55  ? 157 LYS   B CD  1 
ATOM   1997 C  CD  B LYS   B 2 148 ? 28.607  14.091 -19.496 0.14 59.55  ? 157 LYS   B CD  1 
ATOM   1998 C  CD  C LYS   B 2 148 ? 25.497  16.424 -22.109 0.36 57.95  ? 157 LYS   B CD  1 
ATOM   1999 C  CD  D LYS   B 2 148 ? 25.498  16.424 -22.109 0.37 57.95  ? 157 LYS   B CD  1 
ATOM   2000 C  CE  A LYS   B 2 148 ? 29.778  14.141 -20.455 0.13 60.39  ? 157 LYS   B CE  1 
ATOM   2001 C  CE  B LYS   B 2 148 ? 29.779  14.140 -20.455 0.14 60.39  ? 157 LYS   B CE  1 
ATOM   2002 C  CE  C LYS   B 2 148 ? 25.287  14.947 -21.852 0.36 59.23  ? 157 LYS   B CE  1 
ATOM   2003 C  CE  D LYS   B 2 148 ? 25.287  14.947 -21.852 0.37 59.24  ? 157 LYS   B CE  1 
ATOM   2004 N  NZ  A LYS   B 2 148 ? 31.018  14.615 -19.797 0.13 60.41  ? 157 LYS   B NZ  1 
ATOM   2005 N  NZ  B LYS   B 2 148 ? 31.019  14.615 -19.798 0.14 60.41  ? 157 LYS   B NZ  1 
ATOM   2006 N  NZ  C LYS   B 2 148 ? 25.125  14.652 -20.405 0.36 60.48  ? 157 LYS   B NZ  1 
ATOM   2007 N  NZ  D LYS   B 2 148 ? 25.125  14.651 -20.406 0.37 60.49  ? 157 LYS   B NZ  1 
ATOM   2008 N  N   A ASN   B 2 149 ? 25.907  18.475 -21.757 0.13 57.31  ? 158 ASN   B N   1 
ATOM   2009 N  N   B ASN   B 2 149 ? 25.907  18.474 -21.757 0.14 57.32  ? 158 ASN   B N   1 
ATOM   2010 N  N   C ASN   B 2 149 ? 26.338  21.107 -22.126 0.36 52.32  ? 158 ASN   B N   1 
ATOM   2011 N  N   D ASN   B 2 149 ? 26.338  21.107 -22.126 0.37 52.32  ? 158 ASN   B N   1 
ATOM   2012 C  CA  A ASN   B 2 149 ? 25.771  19.298 -22.991 0.13 57.38  ? 158 ASN   B CA  1 
ATOM   2013 C  CA  B ASN   B 2 149 ? 25.771  19.297 -22.991 0.14 57.39  ? 158 ASN   B CA  1 
ATOM   2014 C  CA  C ASN   B 2 149 ? 26.388  22.352 -22.944 0.36 52.53  ? 158 ASN   B CA  1 
ATOM   2015 C  CA  D ASN   B 2 149 ? 26.389  22.352 -22.945 0.37 52.53  ? 158 ASN   B CA  1 
ATOM   2016 C  C   A ASN   B 2 149 ? 25.557  20.771 -22.621 0.13 56.28  ? 158 ASN   B C   1 
ATOM   2017 C  C   B ASN   B 2 149 ? 25.557  20.769 -22.621 0.14 56.31  ? 158 ASN   B C   1 
ATOM   2018 C  C   C ASN   B 2 149 ? 25.304  23.340 -22.496 0.36 51.32  ? 158 ASN   B C   1 
ATOM   2019 C  C   D ASN   B 2 149 ? 25.304  23.340 -22.496 0.37 51.32  ? 158 ASN   B C   1 
ATOM   2020 O  O   A ASN   B 2 149 ? 26.143  21.638 -23.305 0.13 56.95  ? 158 ASN   B O   1 
ATOM   2021 O  O   B ASN   B 2 149 ? 26.144  21.637 -23.303 0.14 56.97  ? 158 ASN   B O   1 
ATOM   2022 O  O   C ASN   B 2 149 ? 25.215  24.423 -23.108 0.36 49.59  ? 158 ASN   B O   1 
ATOM   2023 O  O   D ASN   B 2 149 ? 25.215  24.423 -23.108 0.37 49.58  ? 158 ASN   B O   1 
ATOM   2024 C  CB  A ASN   B 2 149 ? 24.618  18.821 -23.879 0.13 58.11  ? 158 ASN   B CB  1 
ATOM   2025 C  CB  B ASN   B 2 149 ? 24.617  18.820 -23.878 0.14 58.12  ? 158 ASN   B CB  1 
ATOM   2026 C  CB  C ASN   B 2 149 ? 26.174  22.058 -24.431 0.36 53.60  ? 158 ASN   B CB  1 
ATOM   2027 C  CB  D ASN   B 2 149 ? 26.174  22.058 -24.431 0.37 53.60  ? 158 ASN   B CB  1 
ATOM   2028 C  CG  A ASN   B 2 149 ? 24.637  17.332 -24.156 0.13 58.61  ? 158 ASN   B CG  1 
ATOM   2029 C  CG  B ASN   B 2 149 ? 24.636  17.332 -24.156 0.14 58.62  ? 158 ASN   B CG  1 
ATOM   2030 C  CG  C ASN   B 2 149 ? 24.765  21.588 -24.744 0.36 53.68  ? 158 ASN   B CG  1 
ATOM   2031 C  CG  D ASN   B 2 149 ? 24.765  21.588 -24.744 0.37 53.68  ? 158 ASN   B CG  1 
ATOM   2032 O  OD1 A ASN   B 2 149 ? 25.341  16.573 -23.484 0.13 59.00  ? 158 ASN   B OD1 1 
ATOM   2033 O  OD1 B ASN   B 2 149 ? 25.340  16.573 -23.483 0.14 59.01  ? 158 ASN   B OD1 1 
ATOM   2034 O  OD1 C ASN   B 2 149 ? 24.277  20.617 -24.175 0.36 54.19  ? 158 ASN   B OD1 1 
ATOM   2035 O  OD1 D ASN   B 2 149 ? 24.277  20.617 -24.175 0.37 54.20  ? 158 ASN   B OD1 1 
ATOM   2036 N  ND2 A ASN   B 2 149 ? 23.844  16.903 -25.129 0.13 58.77  ? 158 ASN   B ND2 1 
ATOM   2037 N  ND2 B ASN   B 2 149 ? 23.844  16.903 -25.129 0.14 58.78  ? 158 ASN   B ND2 1 
ATOM   2038 N  ND2 C ASN   B 2 149 ? 24.087  22.274 -25.644 0.36 54.82  ? 158 ASN   B ND2 1 
ATOM   2039 N  ND2 D ASN   B 2 149 ? 24.087  22.274 -25.644 0.37 54.82  ? 158 ASN   B ND2 1 
ATOM   2040 N  N   A GLY   B 2 150 ? 24.756  21.027 -21.578 0.13 54.20  ? 159 GLY   B N   1 
ATOM   2041 N  N   B GLY   B 2 150 ? 24.753  21.023 -21.580 0.14 54.25  ? 159 GLY   B N   1 
ATOM   2042 N  N   C GLY   B 2 150 ? 24.514  22.984 -21.470 0.36 49.57  ? 159 GLY   B N   1 
ATOM   2043 N  N   D GLY   B 2 150 ? 24.514  22.984 -21.471 0.37 49.57  ? 159 GLY   B N   1 
ATOM   2044 C  CA  A GLY   B 2 150 ? 24.203  22.352 -21.224 0.13 52.91  ? 159 GLY   B CA  1 
ATOM   2045 C  CA  B GLY   B 2 150 ? 24.202  22.347 -21.220 0.14 52.97  ? 159 GLY   B CA  1 
ATOM   2046 C  CA  C GLY   B 2 150 ? 23.339  23.766 -21.047 0.36 49.37  ? 159 GLY   B CA  1 
ATOM   2047 C  CA  D GLY   B 2 150 ? 23.339  23.766 -21.048 0.37 49.37  ? 159 GLY   B CA  1 
ATOM   2048 C  C   A GLY   B 2 150 ? 22.700  22.420 -21.530 0.13 51.78  ? 159 GLY   B C   1 
ATOM   2049 C  C   B GLY   B 2 150 ? 22.702  22.429 -21.531 0.14 51.91  ? 159 GLY   B C   1 
ATOM   2050 C  C   C GLY   B 2 150 ? 22.009  23.199 -21.560 0.36 48.96  ? 159 GLY   B C   1 
ATOM   2051 C  C   D GLY   B 2 150 ? 22.010  23.199 -21.561 0.37 48.95  ? 159 GLY   B C   1 
ATOM   2052 O  O   A GLY   B 2 150 ? 22.056  23.515 -21.462 0.13 50.98  ? 159 GLY   B O   1 
ATOM   2053 O  O   B GLY   B 2 150 ? 22.068  23.525 -21.455 0.14 51.05  ? 159 GLY   B O   1 
ATOM   2054 O  O   C GLY   B 2 150 ? 20.974  24.003 -21.625 0.36 49.28  ? 159 GLY   B O   1 
ATOM   2055 O  O   D GLY   B 2 150 ? 20.974  24.003 -21.624 0.37 49.28  ? 159 GLY   B O   1 
ATOM   2056 N  N   A SER   B 2 151 ? 22.187  21.282 -22.069 0.13 51.32  ? 160 SER   B N   1 
ATOM   2057 N  N   B SER   B 2 151 ? 22.171  21.318 -22.094 0.14 51.78  ? 160 SER   B N   1 
ATOM   2058 N  N   C SER   B 2 151 ? 22.006  21.874 -21.886 0.36 50.21  ? 160 SER   B N   1 
ATOM   2059 N  N   D SER   B 2 151 ? 22.006  21.874 -21.885 0.37 50.20  ? 160 SER   B N   1 
ATOM   2060 C  CA  A SER   B 2 151 ? 20.765  21.065 -22.443 0.13 50.56  ? 160 SER   B CA  1 
ATOM   2061 C  CA  B SER   B 2 151 ? 20.738  21.167 -22.450 0.14 51.25  ? 160 SER   B CA  1 
ATOM   2062 C  CA  C SER   B 2 151 ? 20.786  21.179 -22.371 0.36 51.03  ? 160 SER   B CA  1 
ATOM   2063 C  CA  D SER   B 2 151 ? 20.786  21.179 -22.371 0.37 51.03  ? 160 SER   B CA  1 
ATOM   2064 C  C   A SER   B 2 151 ? 19.936  20.775 -21.185 0.13 49.82  ? 160 SER   B C   1 
ATOM   2065 C  C   B SER   B 2 151 ? 19.936  20.777 -21.201 0.14 50.24  ? 160 SER   B C   1 
ATOM   2066 C  C   C SER   B 2 151 ? 19.931  20.759 -21.166 0.36 50.49  ? 160 SER   B C   1 
ATOM   2067 C  C   D SER   B 2 151 ? 19.931  20.759 -21.166 0.37 50.50  ? 160 SER   B C   1 
ATOM   2068 O  O   A SER   B 2 151 ? 20.536  20.546 -20.107 0.13 49.16  ? 160 SER   B O   1 
ATOM   2069 O  O   B SER   B 2 151 ? 20.552  20.486 -20.148 0.14 49.61  ? 160 SER   B O   1 
ATOM   2070 O  O   C SER   B 2 151 ? 20.504  20.421 -20.095 0.36 49.24  ? 160 SER   B O   1 
ATOM   2071 O  O   D SER   B 2 151 ? 20.504  20.421 -20.095 0.37 49.24  ? 160 SER   B O   1 
ATOM   2072 C  CB  A SER   B 2 151 ? 20.647  19.955 -23.473 0.13 51.05  ? 160 SER   B CB  1 
ATOM   2073 C  CB  B SER   B 2 151 ? 20.561  20.178 -23.584 0.14 52.23  ? 160 SER   B CB  1 
ATOM   2074 C  CB  C SER   B 2 151 ? 21.119  20.012 -23.274 0.36 53.64  ? 160 SER   B CB  1 
ATOM   2075 C  CB  D SER   B 2 151 ? 21.119  20.012 -23.274 0.37 53.65  ? 160 SER   B CB  1 
ATOM   2076 O  OG  A SER   B 2 151 ? 19.289  19.684 -23.795 0.13 50.34  ? 160 SER   B OG  1 
ATOM   2077 O  OG  B SER   B 2 151 ? 21.073  18.902 -23.238 0.14 52.56  ? 160 SER   B OG  1 
ATOM   2078 O  OG  C SER   B 2 151 ? 21.697  18.958 -22.516 0.36 56.96  ? 160 SER   B OG  1 
ATOM   2079 O  OG  D SER   B 2 151 ? 21.696  18.958 -22.516 0.37 56.97  ? 160 SER   B OG  1 
ATOM   2080 N  N   . TYR   B 2 152 ? 18.608  20.800 -21.318 1.00 48.93  ? 161 TYR   B N   1 
ATOM   2081 C  CA  . TYR   B 2 152 ? 17.675  20.511 -20.211 1.00 48.55  ? 161 TYR   B CA  1 
ATOM   2082 C  C   . TYR   B 2 152 ? 17.067  19.122 -20.367 1.00 46.32  ? 161 TYR   B C   1 
ATOM   2083 O  O   . TYR   B 2 152 ? 16.649  18.783 -21.470 1.00 44.44  ? 161 TYR   B O   1 
ATOM   2084 C  CB  . TYR   B 2 152 ? 16.590  21.574 -20.177 1.00 49.48  ? 161 TYR   B CB  1 
ATOM   2085 C  CG  . TYR   B 2 152 ? 15.724  21.449 -18.948 1.00 48.50  ? 161 TYR   B CG  1 
ATOM   2086 C  CD1 . TYR   B 2 152 ? 16.223  21.699 -17.683 1.00 48.64  ? 161 TYR   B CD1 1 
ATOM   2087 C  CD2 . TYR   B 2 152 ? 14.398  21.073 -19.077 1.00 48.09  ? 161 TYR   B CD2 1 
ATOM   2088 C  CE1 . TYR   B 2 152 ? 15.418  21.585 -16.550 1.00 49.34  ? 161 TYR   B CE1 1 
ATOM   2089 C  CE2 . TYR   B 2 152 ? 13.575  20.985 -17.963 1.00 50.16  ? 161 TYR   B CE2 1 
ATOM   2090 C  CZ  . TYR   B 2 152 ? 14.099  21.194 -16.699 1.00 47.21  ? 161 TYR   B CZ  1 
ATOM   2091 O  OH  . TYR   B 2 152 ? 13.253  21.129 -15.626 1.00 48.99  ? 161 TYR   B OH  1 
ATOM   2092 N  N   . VAL   B 2 153 ? 16.985  18.374 -19.240 1.00 43.68  ? 162 VAL   B N   1 
ATOM   2093 C  CA  . VAL   B 2 153 ? 16.244  17.081 -19.215 1.00 43.40  ? 162 VAL   B CA  1 
ATOM   2094 C  C   . VAL   B 2 153 ? 15.320  17.120 -17.987 1.00 43.30  ? 162 VAL   B C   1 
ATOM   2095 O  O   . VAL   B 2 153 ? 15.867  17.230 -16.852 1.00 41.58  ? 162 VAL   B O   1 
ATOM   2096 C  CB  . VAL   B 2 153 ? 17.185  15.865 -19.160 1.00 43.55  ? 162 VAL   B CB  1 
ATOM   2097 C  CG1 . VAL   B 2 153 ? 16.400  14.578 -19.366 1.00 43.52  ? 162 VAL   B CG1 1 
ATOM   2098 C  CG2 . VAL   B 2 153 ? 18.315  15.949 -20.200 1.00 45.68  ? 162 VAL   B CG2 1 
ATOM   2099 N  N   . SER   B 2 154 ? 14.007  17.045 -18.245 1.00 42.82  ? 163 SER   B N   1 
ATOM   2100 C  CA  . SER   B 2 154 ? 12.915  17.127 -17.251 1.00 41.08  ? 163 SER   B CA  1 
ATOM   2101 C  C   . SER   B 2 154 ? 12.445  15.709 -16.892 1.00 39.31  ? 163 SER   B C   1 
ATOM   2102 O  O   . SER   B 2 154 ? 12.347  14.835 -17.770 1.00 39.37  ? 163 SER   B O   1 
ATOM   2103 C  CB  . SER   B 2 154 ? 11.789  18.020 -17.754 1.00 41.20  ? 163 SER   B CB  1 
ATOM   2104 O  OG  . SER   B 2 154 ? 10.530  17.822 -17.078 1.00 41.59  ? 163 SER   B OG  1 
ATOM   2105 N  N   . ALA   B 2 155 ? 12.163  15.452 -15.601 1.00 36.67  ? 164 ALA   B N   1 
ATOM   2106 C  CA  . ALA   B 2 155 ? 11.370  14.264 -15.214 1.00 35.58  ? 164 ALA   B CA  1 
ATOM   2107 C  C   . ALA   B 2 155 ? 9.966   14.390 -15.922 1.00 36.16  ? 164 ALA   B C   1 
ATOM   2108 O  O   . ALA   B 2 155 ? 9.405   15.513 -16.206 1.00 37.54  ? 164 ALA   B O   1 
ATOM   2109 C  CB  . ALA   B 2 155 ? 11.239  14.158 -13.675 1.00 36.64  ? 164 ALA   B CB  1 
ATOM   2110 N  N   . ILE   B 2 156 ? 9.371   13.230 -16.103 1.00 35.49  ? 165 ILE   B N   1 
ATOM   2111 C  CA  . ILE   B 2 156 ? 7.896   13.149 -16.301 1.00 36.06  ? 165 ILE   B CA  1 
ATOM   2112 C  C   . ILE   B 2 156 ? 7.287   13.080 -14.898 1.00 34.94  ? 165 ILE   B C   1 
ATOM   2113 O  O   . ILE   B 2 156 ? 7.331   12.006 -14.312 1.00 35.59  ? 165 ILE   B O   1 
ATOM   2114 C  CB  . ILE   B 2 156 ? 7.489   11.945 -17.160 1.00 37.13  ? 165 ILE   B CB  1 
ATOM   2115 C  CG1 . ILE   B 2 156 ? 8.222   11.955 -18.498 1.00 38.39  ? 165 ILE   B CG1 1 
ATOM   2116 C  CG2 . ILE   B 2 156 ? 5.980   11.903 -17.303 1.00 37.66  ? 165 ILE   B CG2 1 
ATOM   2117 C  CD1 . ILE   B 2 156 ? 7.721   10.874 -19.454 1.00 38.34  ? 165 ILE   B CD1 1 
ATOM   2118 N  N   . THR   B 2 157 ? 6.842   14.214 -14.400 1.00 34.35  ? 166 THR   B N   1 
ATOM   2119 C  CA  . THR   B 2 157 ? 6.374   14.299 -12.965 1.00 33.35  ? 166 THR   B CA  1 
ATOM   2120 C  C   . THR   B 2 157 ? 4.853   14.119 -12.944 1.00 34.34  ? 166 THR   B C   1 
ATOM   2121 O  O   . THR   B 2 157 ? 4.134   14.968 -13.585 1.00 34.28  ? 166 THR   B O   1 
ATOM   2122 C  CB  . THR   B 2 157 ? 6.731   15.634 -12.338 1.00 32.77  ? 166 THR   B CB  1 
ATOM   2123 O  OG1 . THR   B 2 157 ? 8.211   15.852 -12.332 1.00 33.29  ? 166 THR   B OG1 1 
ATOM   2124 C  CG2 . THR   B 2 157 ? 6.291   15.622 -10.866 1.00 32.24  ? 166 THR   B CG2 1 
ATOM   2125 N  N   . GLN   B 2 158 ? 4.375   13.017 -12.325 1.00 33.83  ? 167 GLN   B N   1 
ATOM   2126 C  CA  . GLN   B 2 158 ? 2.948   12.662 -12.235 1.00 33.87  ? 167 GLN   B CA  1 
ATOM   2127 C  C   . GLN   B 2 158 ? 2.555   12.566 -10.748 1.00 35.11  ? 167 GLN   B C   1 
ATOM   2128 O  O   . GLN   B 2 158 ? 3.385   12.079 -9.977  1.00 34.86  ? 167 GLN   B O   1 
ATOM   2129 C  CB  . GLN   B 2 158 ? 2.636   11.337 -12.916 1.00 34.75  ? 167 GLN   B CB  1 
ATOM   2130 C  CG  . GLN   B 2 158 ? 1.156   10.971 -12.963 1.00 33.74  ? 167 GLN   B CG  1 
ATOM   2131 C  CD  . GLN   B 2 158 ? 0.250   12.053 -13.480 1.00 34.72  ? 167 GLN   B CD  1 
ATOM   2132 O  OE1 . GLN   B 2 158 ? 0.183   13.173 -12.972 1.00 32.56  ? 167 GLN   B OE1 1 
ATOM   2133 N  NE2 . GLN   B 2 158 ? -0.333  11.783 -14.651 1.00 34.14  ? 167 GLN   B NE2 1 
ATOM   2134 N  N   . GLY   B 2 159 ? 1.353   12.981 -10.409 1.00 37.79  ? 168 GLY   B N   1 
ATOM   2135 C  CA  . GLY   B 2 159 ? 0.807   12.783 -9.042  1.00 40.53  ? 168 GLY   B CA  1 
ATOM   2136 C  C   . GLY   B 2 159 ? -0.006  11.501 -8.940  1.00 45.01  ? 168 GLY   B C   1 
ATOM   2137 O  O   . GLY   B 2 159 ? -0.072  10.731 -9.890  1.00 49.74  ? 168 GLY   B O   1 
ATOM   2138 N  N   . LYS   B 2 160 ? -0.677  11.318 -7.824  1.00 52.81  ? 169 LYS   B N   1 
ATOM   2139 C  CA  . LYS   B 2 160 ? -1.464  10.111 -7.467  1.00 59.20  ? 169 LYS   B CA  1 
ATOM   2140 C  C   . LYS   B 2 160 ? -2.928  10.541 -7.327  1.00 61.45  ? 169 LYS   B C   1 
ATOM   2141 O  O   . LYS   B 2 160 ? -3.163  11.509 -6.599  1.00 62.51  ? 169 LYS   B O   1 
ATOM   2142 C  CB  . LYS   B 2 160 ? -0.927  9.539  -6.141  1.00 60.66  ? 169 LYS   B CB  1 
ATOM   2143 C  CG  . LYS   B 2 160 ? -1.404  8.132  -5.807  1.00 64.86  ? 169 LYS   B CG  1 
ATOM   2144 C  CD  . LYS   B 2 160 ? -1.246  7.742  -4.352  1.00 68.67  ? 169 LYS   B CD  1 
ATOM   2145 C  CE  . LYS   B 2 160 ? -2.339  6.795  -3.898  1.00 72.80  ? 169 LYS   B CE  1 
ATOM   2146 N  NZ  . LYS   B 2 160 ? -2.621  6.959  -2.455  1.00 75.10  ? 169 LYS   B NZ  1 
ATOM   2147 N  N   . ARG   B 2 161 ? -3.868  9.845  -7.970  1.00 63.23  ? 170 ARG   B N   1 
ATOM   2148 C  CA  . ARG   B 2 161 ? -5.336  10.053 -7.810  1.00 67.95  ? 170 ARG   B CA  1 
ATOM   2149 C  C   . ARG   B 2 161 ? -5.879  9.050  -6.770  1.00 73.79  ? 170 ARG   B C   1 
ATOM   2150 O  O   . ARG   B 2 161 ? -5.423  7.896  -6.789  1.00 77.89  ? 170 ARG   B O   1 
ATOM   2151 C  CB  . ARG   B 2 161 ? -5.983  9.937  -9.195  1.00 68.45  ? 170 ARG   B CB  1 
ATOM   2152 C  CG  . ARG   B 2 161 ? -7.402  10.472 -9.282  1.00 67.06  ? 170 ARG   B CG  1 
ATOM   2153 C  CD  . ARG   B 2 161 ? -8.128  10.056 -10.550 1.00 69.61  ? 170 ARG   B CD  1 
ATOM   2154 N  NE  . ARG   B 2 161 ? -9.574  10.233 -10.407 1.00 71.03  ? 170 ARG   B NE  1 
ATOM   2155 C  CZ  . ARG   B 2 161 ? -10.357 11.025 -11.148 1.00 70.47  ? 170 ARG   B CZ  1 
ATOM   2156 N  NH1 . ARG   B 2 161 ? -9.866  11.717 -12.170 1.00 69.76  ? 170 ARG   B NH1 1 
ATOM   2157 N  NH2 . ARG   B 2 161 ? -11.652 11.086 -10.876 1.00 69.29  ? 170 ARG   B NH2 1 
ATOM   2158 N  N   . GLU   B 2 162 ? -6.798  9.473  -5.885  1.00 81.17  ? 171 GLU   B N   1 
ATOM   2159 C  CA  . GLU   B 2 162 ? -7.335  8.659  -4.750  1.00 85.31  ? 171 GLU   B CA  1 
ATOM   2160 C  C   . GLU   B 2 162 ? -8.660  7.985  -5.131  1.00 87.39  ? 171 GLU   B C   1 
ATOM   2161 O  O   . GLU   B 2 162 ? -9.303  7.335  -4.290  1.00 88.73  ? 171 GLU   B O   1 
ATOM   2162 C  CB  . GLU   B 2 162 ? -7.536  9.536  -3.512  1.00 89.40  ? 171 GLU   B CB  1 
ATOM   2163 C  CG  . GLU   B 2 162 ? -6.271  10.225 -3.035  1.00 90.23  ? 171 GLU   B CG  1 
ATOM   2164 C  CD  . GLU   B 2 162 ? -5.314  9.328  -2.272  1.00 94.85  ? 171 GLU   B CD  1 
ATOM   2165 O  OE1 . GLU   B 2 162 ? -4.869  9.741  -1.174  1.00 100.41 ? 171 GLU   B OE1 1 
ATOM   2166 O  OE2 . GLU   B 2 162 ? -5.010  8.224  -2.776  1.00 95.81  ? 171 GLU   B OE2 1 
HETATM 2167 S  S   C DMS   C 3 .   ? 5.426   22.732 -33.952 0.50 93.97  ? 101 DMS   A S   1 
HETATM 2168 S  S   D DMS   C 3 .   ? 5.426   22.732 -33.952 0.50 93.97  ? 101 DMS   A S   1 
HETATM 2169 O  O   C DMS   C 3 .   ? 5.400   21.220 -33.975 0.50 87.59  ? 101 DMS   A O   1 
HETATM 2170 O  O   D DMS   C 3 .   ? 5.400   21.220 -33.975 0.50 87.59  ? 101 DMS   A O   1 
HETATM 2171 C  C1  C DMS   C 3 .   ? 4.586   23.314 -35.415 0.50 96.10  ? 101 DMS   A C1  1 
HETATM 2172 C  C1  D DMS   C 3 .   ? 4.586   23.314 -35.415 0.50 96.10  ? 101 DMS   A C1  1 
HETATM 2173 C  C2  C DMS   C 3 .   ? 7.068   23.226 -34.394 0.50 95.49  ? 101 DMS   A C2  1 
HETATM 2174 C  C2  D DMS   C 3 .   ? 7.068   23.226 -34.394 0.50 95.49  ? 101 DMS   A C2  1 
HETATM 2175 S  S   C DMS   D 3 .   ? 27.108  14.835 -17.908 0.36 100.78 ? 102 DMS   A S   1 
HETATM 2176 S  S   D DMS   D 3 .   ? 27.109  14.835 -17.907 0.37 100.77 ? 102 DMS   A S   1 
HETATM 2177 O  O   C DMS   D 3 .   ? 27.518  13.769 -16.927 0.36 102.78 ? 102 DMS   A O   1 
HETATM 2178 O  O   D DMS   D 3 .   ? 27.518  13.769 -16.926 0.37 102.79 ? 102 DMS   A O   1 
HETATM 2179 C  C1  C DMS   D 3 .   ? 28.505  15.061 -18.982 0.36 103.51 ? 102 DMS   A C1  1 
HETATM 2180 C  C1  D DMS   D 3 .   ? 28.505  15.060 -18.982 0.37 103.52 ? 102 DMS   A C1  1 
HETATM 2181 C  C2  C DMS   D 3 .   ? 27.223  16.386 -17.049 0.36 99.35  ? 102 DMS   A C2  1 
HETATM 2182 C  C2  D DMS   D 3 .   ? 27.225  16.387 -17.049 0.37 99.34  ? 102 DMS   A C2  1 
HETATM 2183 S  S   C DMS   E 3 .   ? 9.907   24.068 -40.846 0.50 120.49 ? 103 DMS   A S   1 
HETATM 2184 S  S   D DMS   E 3 .   ? 9.907   24.068 -40.846 0.50 120.49 ? 103 DMS   A S   1 
HETATM 2185 O  O   C DMS   E 3 .   ? 11.070  23.253 -41.342 0.50 117.64 ? 103 DMS   A O   1 
HETATM 2186 O  O   D DMS   E 3 .   ? 11.070  23.253 -41.342 0.50 117.64 ? 103 DMS   A O   1 
HETATM 2187 C  C1  C DMS   E 3 .   ? 8.448   23.191 -41.347 0.50 116.95 ? 103 DMS   A C1  1 
HETATM 2188 C  C1  D DMS   E 3 .   ? 8.448   23.191 -41.347 0.50 116.95 ? 103 DMS   A C1  1 
HETATM 2189 C  C2  C DMS   E 3 .   ? 9.767   25.445 -41.956 0.50 117.89 ? 103 DMS   A C2  1 
HETATM 2190 C  C2  D DMS   E 3 .   ? 9.767   25.445 -41.956 0.50 117.89 ? 103 DMS   A C2  1 
HETATM 2191 S  S   A DMS   F 3 .   ? 13.574  25.119 -17.801 0.13 68.89  ? 201 DMS   B S   1 
HETATM 2192 S  S   B DMS   F 3 .   ? 13.575  25.119 -17.802 0.14 68.88  ? 201 DMS   B S   1 
HETATM 2193 O  O   A DMS   F 3 .   ? 14.780  24.365 -18.288 0.13 68.52  ? 201 DMS   B O   1 
HETATM 2194 O  O   B DMS   F 3 .   ? 14.780  24.365 -18.288 0.14 68.50  ? 201 DMS   B O   1 
HETATM 2195 C  C1  A DMS   F 3 .   ? 13.469  24.815 -16.053 0.13 68.74  ? 201 DMS   B C1  1 
HETATM 2196 C  C1  B DMS   F 3 .   ? 13.469  24.816 -16.053 0.14 68.74  ? 201 DMS   B C1  1 
HETATM 2197 C  C2  A DMS   F 3 .   ? 12.157  24.168 -18.291 0.13 68.88  ? 201 DMS   B C2  1 
HETATM 2198 C  C2  B DMS   F 3 .   ? 12.158  24.168 -18.291 0.14 68.88  ? 201 DMS   B C2  1 
HETATM 2199 S  S   A DMS   G 3 .   ? 2.593   31.447 0.025   0.50 76.99  ? 202 DMS   B S   1 
HETATM 2200 S  S   B DMS   G 3 .   ? 2.593   31.447 0.025   0.50 76.99  ? 202 DMS   B S   1 
HETATM 2201 O  O   A DMS   G 3 .   ? 2.220   30.031 -0.285  0.50 74.86  ? 202 DMS   B O   1 
HETATM 2202 O  O   B DMS   G 3 .   ? 2.220   30.031 -0.285  0.50 74.86  ? 202 DMS   B O   1 
HETATM 2203 C  C1  A DMS   G 3 .   ? 1.240   32.454 -0.518  0.50 75.49  ? 202 DMS   B C1  1 
HETATM 2204 C  C1  B DMS   G 3 .   ? 1.240   32.454 -0.518  0.50 75.49  ? 202 DMS   B C1  1 
HETATM 2205 C  C2  A DMS   G 3 .   ? 3.780   31.953 -1.191  0.50 74.74  ? 202 DMS   B C2  1 
HETATM 2206 C  C2  B DMS   G 3 .   ? 3.780   31.953 -1.191  0.50 74.74  ? 202 DMS   B C2  1 
HETATM 2207 S  S   A DMS   H 3 .   ? 14.954  22.914 -13.158 0.13 43.60  ? 203 DMS   B S   1 
HETATM 2208 S  S   B DMS   H 3 .   ? 14.954  22.914 -13.159 0.14 43.59  ? 203 DMS   B S   1 
HETATM 2209 O  O   A DMS   H 3 .   ? 14.525  21.505 -13.439 0.13 42.64  ? 203 DMS   B O   1 
HETATM 2210 O  O   B DMS   H 3 .   ? 14.524  21.505 -13.440 0.14 42.61  ? 203 DMS   B O   1 
HETATM 2211 C  C1  A DMS   H 3 .   ? 13.822  23.523 -11.921 0.13 43.48  ? 203 DMS   B C1  1 
HETATM 2212 C  C1  B DMS   H 3 .   ? 13.823  23.523 -11.921 0.14 43.48  ? 203 DMS   B C1  1 
HETATM 2213 C  C2  A DMS   H 3 .   ? 16.382  22.809 -12.098 0.13 43.88  ? 203 DMS   B C2  1 
HETATM 2214 C  C2  B DMS   H 3 .   ? 16.382  22.807 -12.098 0.14 43.89  ? 203 DMS   B C2  1 
HETATM 2215 N  N1  C A1BHC I 4 .   ? 13.021  22.790 -7.520  0.36 46.75  ? 204 A1BHC B N1  1 
HETATM 2216 N  N1  D A1BHC I 4 .   ? 13.021  22.791 -7.520  0.37 46.75  ? 204 A1BHC B N1  1 
HETATM 2217 N  N3  C A1BHC I 4 .   ? 16.184  25.562 -19.258 0.36 44.61  ? 204 A1BHC B N3  1 
HETATM 2218 N  N3  D A1BHC I 4 .   ? 16.185  25.562 -19.258 0.37 44.61  ? 204 A1BHC B N3  1 
HETATM 2219 C  C4  C A1BHC I 4 .   ? 12.532  24.254 -9.423  0.36 45.79  ? 204 A1BHC B C4  1 
HETATM 2220 C  C4  D A1BHC I 4 .   ? 12.532  24.254 -9.423  0.37 45.79  ? 204 A1BHC B C4  1 
HETATM 2221 C  C5  C A1BHC I 4 .   ? 12.385  24.266 -10.802 0.36 44.66  ? 204 A1BHC B C5  1 
HETATM 2222 C  C5  D A1BHC I 4 .   ? 12.385  24.266 -10.802 0.37 44.66  ? 204 A1BHC B C5  1 
HETATM 2223 C  C6  C A1BHC I 4 .   ? 12.731  25.375 -11.556 0.36 43.60  ? 204 A1BHC B C6  1 
HETATM 2224 C  C6  D A1BHC I 4 .   ? 12.731  25.376 -11.557 0.37 43.60  ? 204 A1BHC B C6  1 
HETATM 2225 C  C7  C A1BHC I 4 .   ? 12.553  25.355 -13.053 0.36 42.78  ? 204 A1BHC B C7  1 
HETATM 2226 C  C7  D A1BHC I 4 .   ? 12.553  25.355 -13.053 0.37 42.78  ? 204 A1BHC B C7  1 
HETATM 2227 C  C8  C A1BHC I 4 .   ? 13.714  24.816 -15.170 0.36 41.93  ? 204 A1BHC B C8  1 
HETATM 2228 C  C8  D A1BHC I 4 .   ? 13.714  24.816 -15.170 0.37 41.92  ? 204 A1BHC B C8  1 
HETATM 2229 C  C10 C A1BHC I 4 .   ? 12.624  24.407 -17.269 0.36 41.44  ? 204 A1BHC B C10 1 
HETATM 2230 C  C10 D A1BHC I 4 .   ? 12.624  24.407 -17.269 0.37 41.44  ? 204 A1BHC B C10 1 
HETATM 2231 C  C13 C A1BHC I 4 .   ? 16.162  25.620 -17.931 0.36 43.82  ? 204 A1BHC B C13 1 
HETATM 2232 C  C13 D A1BHC I 4 .   ? 16.162  25.620 -17.931 0.37 43.82  ? 204 A1BHC B C13 1 
HETATM 2233 C  C15 C A1BHC I 4 .   ? 16.933  25.613 -21.568 0.36 45.30  ? 204 A1BHC B C15 1 
HETATM 2234 C  C15 D A1BHC I 4 .   ? 16.933  25.613 -21.567 0.37 45.30  ? 204 A1BHC B C15 1 
HETATM 2235 C  C17 C A1BHC I 4 .   ? 17.662  27.392 -19.971 0.36 45.52  ? 204 A1BHC B C17 1 
HETATM 2236 C  C17 D A1BHC I 4 .   ? 17.662  27.392 -19.971 0.37 45.52  ? 204 A1BHC B C17 1 
HETATM 2237 C  C20 C A1BHC I 4 .   ? 13.397  26.502 -9.530  0.36 45.35  ? 204 A1BHC B C20 1 
HETATM 2238 C  C20 D A1BHC I 4 .   ? 13.397  26.502 -9.530  0.37 45.36  ? 204 A1BHC B C20 1 
HETATM 2239 C  C21 C A1BHC I 4 .   ? 13.043  25.391 -8.794  0.36 45.58  ? 204 A1BHC B C21 1 
HETATM 2240 C  C21 D A1BHC I 4 .   ? 13.043  25.391 -8.794  0.37 45.58  ? 204 A1BHC B C21 1 
HETATM 2241 C  C1  C A1BHC I 4 .   ? 12.513  21.689 -6.708  0.36 46.97  ? 204 A1BHC B C1  1 
HETATM 2242 C  C1  D A1BHC I 4 .   ? 12.514  21.688 -6.709  0.37 46.97  ? 204 A1BHC B C1  1 
HETATM 2243 C  C2  C A1BHC I 4 .   ? 14.366  22.499 -8.020  0.36 47.10  ? 204 A1BHC B C2  1 
HETATM 2244 C  C2  D A1BHC I 4 .   ? 14.367  22.499 -8.021  0.37 47.10  ? 204 A1BHC B C2  1 
HETATM 2245 C  C3  C A1BHC I 4 .   ? 12.121  23.046 -8.628  0.36 46.71  ? 204 A1BHC B C3  1 
HETATM 2246 C  C3  D A1BHC I 4 .   ? 12.121  23.046 -8.629  0.37 46.72  ? 204 A1BHC B C3  1 
HETATM 2247 N  N2  C A1BHC I 4 .   ? 13.675  24.817 -13.782 0.36 42.03  ? 204 A1BHC B N2  1 
HETATM 2248 N  N2  D A1BHC I 4 .   ? 13.675  24.816 -13.782 0.37 42.02  ? 204 A1BHC B N2  1 
HETATM 2249 C  C9  C A1BHC I 4 .   ? 12.586  24.421 -15.884 0.36 41.00  ? 204 A1BHC B C9  1 
HETATM 2250 C  C9  D A1BHC I 4 .   ? 12.586  24.421 -15.884 0.37 40.99  ? 204 A1BHC B C9  1 
HETATM 2251 CL CL1 C A1BHC I 4 .   ? 11.187  23.892 -18.134 0.36 39.66  ? 204 A1BHC B CL1 1 
HETATM 2252 CL CL1 D A1BHC I 4 .   ? 11.186  23.892 -18.134 0.37 39.65  ? 204 A1BHC B CL1 1 
HETATM 2253 C  C11 C A1BHC I 4 .   ? 13.754  24.799 -17.953 0.36 41.35  ? 204 A1BHC B C11 1 
HETATM 2254 C  C11 D A1BHC I 4 .   ? 13.754  24.799 -17.953 0.37 41.35  ? 204 A1BHC B C11 1 
HETATM 2255 C  C12 C A1BHC I 4 .   ? 14.888  25.204 -17.249 0.36 42.65  ? 204 A1BHC B C12 1 
HETATM 2256 C  C12 D A1BHC I 4 .   ? 14.888  25.204 -17.249 0.37 42.65  ? 204 A1BHC B C12 1 
HETATM 2257 O  O1  C A1BHC I 4 .   ? 17.148  25.962 -17.270 0.36 45.02  ? 204 A1BHC B O1  1 
HETATM 2258 O  O1  D A1BHC I 4 .   ? 17.148  25.962 -17.270 0.37 45.02  ? 204 A1BHC B O1  1 
HETATM 2259 C  C14 C A1BHC I 4 .   ? 17.337  25.901 -20.124 0.36 45.25  ? 204 A1BHC B C14 1 
HETATM 2260 C  C14 D A1BHC I 4 .   ? 17.338  25.901 -20.123 0.37 45.25  ? 204 A1BHC B C14 1 
HETATM 2261 C  C16 C A1BHC I 4 .   ? 18.542  25.039 -19.732 0.36 45.57  ? 204 A1BHC B C16 1 
HETATM 2262 C  C16 D A1BHC I 4 .   ? 18.542  25.039 -19.732 0.37 45.57  ? 204 A1BHC B C16 1 
HETATM 2263 O  O2  C A1BHC I 4 .   ? 16.551  28.248 -20.206 0.36 45.01  ? 204 A1BHC B O2  1 
HETATM 2264 O  O2  D A1BHC I 4 .   ? 16.551  28.248 -20.206 0.37 45.01  ? 204 A1BHC B O2  1 
HETATM 2265 C  C18 C A1BHC I 4 .   ? 14.871  25.195 -15.848 0.36 42.19  ? 204 A1BHC B C18 1 
HETATM 2266 C  C18 D A1BHC I 4 .   ? 14.871  25.195 -15.848 0.37 42.19  ? 204 A1BHC B C18 1 
HETATM 2267 C  C19 C A1BHC I 4 .   ? 13.242  26.488 -10.906 0.36 44.03  ? 204 A1BHC B C19 1 
HETATM 2268 C  C19 D A1BHC I 4 .   ? 13.242  26.488 -10.907 0.37 44.02  ? 204 A1BHC B C19 1 
HETATM 2269 O  O3  C A1BHC I 4 .   ? 13.197  25.406 -7.438  0.36 47.66  ? 204 A1BHC B O3  1 
HETATM 2270 O  O3  D A1BHC I 4 .   ? 13.197  25.406 -7.438  0.37 47.68  ? 204 A1BHC B O3  1 
HETATM 2271 S  S   C SO4   J 5 .   ? 16.095  20.301 -27.947 0.36 81.54  ? 205 SO4   B S   1 
HETATM 2272 S  S   D SO4   J 5 .   ? 16.095  20.301 -27.947 0.37 81.55  ? 205 SO4   B S   1 
HETATM 2273 O  O1  C SO4   J 5 .   ? 16.770  19.109 -27.498 0.36 81.74  ? 205 SO4   B O1  1 
HETATM 2274 O  O1  D SO4   J 5 .   ? 16.770  19.109 -27.497 0.37 81.74  ? 205 SO4   B O1  1 
HETATM 2275 O  O2  C SO4   J 5 .   ? 16.253  21.341 -26.973 0.36 80.13  ? 205 SO4   B O2  1 
HETATM 2276 O  O2  D SO4   J 5 .   ? 16.253  21.341 -26.973 0.37 80.12  ? 205 SO4   B O2  1 
HETATM 2277 O  O3  C SO4   J 5 .   ? 16.656  20.734 -29.203 0.36 82.60  ? 205 SO4   B O3  1 
HETATM 2278 O  O3  D SO4   J 5 .   ? 16.655  20.734 -29.202 0.37 82.60  ? 205 SO4   B O3  1 
HETATM 2279 O  O4  C SO4   J 5 .   ? 14.695  20.031 -28.110 0.36 81.79  ? 205 SO4   B O4  1 
HETATM 2280 O  O4  D SO4   J 5 .   ? 14.695  20.031 -28.109 0.37 81.80  ? 205 SO4   B O4  1 
HETATM 2281 S  S   C DMS   K 3 .   ? 7.387   32.203 -8.733  0.50 95.67  ? 206 DMS   B S   1 
HETATM 2282 S  S   D DMS   K 3 .   ? 7.387   32.203 -8.733  0.50 95.67  ? 206 DMS   B S   1 
HETATM 2283 O  O   C DMS   K 3 .   ? 7.517   31.311 -9.933  0.50 92.18  ? 206 DMS   B O   1 
HETATM 2284 O  O   D DMS   K 3 .   ? 7.517   31.311 -9.933  0.50 92.18  ? 206 DMS   B O   1 
HETATM 2285 C  C1  C DMS   K 3 .   ? 6.762   33.750 -9.335  0.50 94.45  ? 206 DMS   B C1  1 
HETATM 2286 C  C1  D DMS   K 3 .   ? 6.762   33.750 -9.335  0.50 94.45  ? 206 DMS   B C1  1 
HETATM 2287 C  C2  C DMS   K 3 .   ? 9.038   32.745 -8.343  0.50 95.43  ? 206 DMS   B C2  1 
HETATM 2288 C  C2  D DMS   K 3 .   ? 9.038   32.745 -8.343  0.50 95.43  ? 206 DMS   B C2  1 
HETATM 2289 S  S   C DMS   L 3 .   ? 1.772   34.176 -34.009 0.50 92.27  ? 207 DMS   B S   1 
HETATM 2290 S  S   D DMS   L 3 .   ? 1.772   34.176 -34.009 0.50 92.27  ? 207 DMS   B S   1 
HETATM 2291 O  O   C DMS   L 3 .   ? 2.540   33.025 -33.436 0.50 89.15  ? 207 DMS   B O   1 
HETATM 2292 O  O   D DMS   L 3 .   ? 2.540   33.025 -33.436 0.50 89.15  ? 207 DMS   B O   1 
HETATM 2293 C  C1  C DMS   L 3 .   ? 0.942   33.544 -35.435 0.50 92.76  ? 207 DMS   B C1  1 
HETATM 2294 C  C1  D DMS   L 3 .   ? 0.942   33.544 -35.435 0.50 92.76  ? 207 DMS   B C1  1 
HETATM 2295 C  C2  C DMS   L 3 .   ? 0.352   34.390 -32.986 0.50 91.31  ? 207 DMS   B C2  1 
HETATM 2296 C  C2  D DMS   L 3 .   ? 0.352   34.390 -32.986 0.50 91.31  ? 207 DMS   B C2  1 
HETATM 2297 S  S   C DMS   M 3 .   ? -0.272  4.716  -25.378 0.50 89.66  ? 208 DMS   B S   1 
HETATM 2298 S  S   D DMS   M 3 .   ? -0.272  4.716  -25.378 0.50 89.66  ? 208 DMS   B S   1 
HETATM 2299 O  O   C DMS   M 3 .   ? -1.528  5.451  -25.003 0.50 86.92  ? 208 DMS   B O   1 
HETATM 2300 O  O   D DMS   M 3 .   ? -1.528  5.451  -25.003 0.50 86.92  ? 208 DMS   B O   1 
HETATM 2301 C  C1  C DMS   M 3 .   ? 0.934   5.949  -25.795 0.50 87.55  ? 208 DMS   B C1  1 
HETATM 2302 C  C1  D DMS   M 3 .   ? 0.934   5.949  -25.795 0.50 87.55  ? 208 DMS   B C1  1 
HETATM 2303 C  C2  C DMS   M 3 .   ? -0.541  4.060  -27.011 0.50 89.95  ? 208 DMS   B C2  1 
HETATM 2304 C  C2  D DMS   M 3 .   ? -0.541  4.060  -27.011 0.50 89.95  ? 208 DMS   B C2  1 
HETATM 2305 S  S   C DMS   N 3 .   ? 19.020  32.194 -16.312 0.36 110.79 ? 209 DMS   B S   1 
HETATM 2306 S  S   D DMS   N 3 .   ? 19.021  32.194 -16.312 0.37 110.79 ? 209 DMS   B S   1 
HETATM 2307 O  O   C DMS   N 3 .   ? 17.811  32.775 -16.988 0.36 105.41 ? 209 DMS   B O   1 
HETATM 2308 O  O   D DMS   N 3 .   ? 17.812  32.775 -16.989 0.37 105.39 ? 209 DMS   B O   1 
HETATM 2309 C  C1  C DMS   N 3 .   ? 18.575  31.973 -14.608 0.36 111.40 ? 209 DMS   B C1  1 
HETATM 2310 C  C1  D DMS   N 3 .   ? 18.576  31.973 -14.608 0.37 111.41 ? 209 DMS   B C1  1 
HETATM 2311 C  C2  C DMS   N 3 .   ? 20.153  33.542 -16.094 0.36 109.20 ? 209 DMS   B C2  1 
HETATM 2312 C  C2  D DMS   N 3 .   ? 20.153  33.542 -16.094 0.37 109.20 ? 209 DMS   B C2  1 
HETATM 2313 O  O   C HOH   O 6 .   ? 14.781  10.950 -2.683  0.36 42.22  ? 201 HOH   A O   1 
HETATM 2314 O  O   D HOH   O 6 .   ? 14.781  10.950 -2.683  0.37 42.27  ? 201 HOH   A O   1 
HETATM 2315 O  O   C HOH   O 6 .   ? 12.520  23.372 -3.369  0.36 52.69  ? 202 HOH   A O   1 
HETATM 2316 O  O   D HOH   O 6 .   ? 12.520  23.372 -3.370  0.37 52.71  ? 202 HOH   A O   1 
HETATM 2317 O  O   C HOH   O 6 .   ? -5.578  13.608 -28.546 0.50 51.89  ? 203 HOH   A O   1 
HETATM 2318 O  O   D HOH   O 6 .   ? -5.578  13.608 -28.546 0.50 51.89  ? 203 HOH   A O   1 
HETATM 2319 O  O   C HOH   O 6 .   ? 19.357  15.929 -5.673  0.36 47.87  ? 204 HOH   A O   1 
HETATM 2320 O  O   D HOH   O 6 .   ? 19.357  15.929 -5.673  0.37 47.90  ? 204 HOH   A O   1 
HETATM 2321 O  O   C HOH   O 6 .   ? -8.279  20.357 -23.646 0.50 68.66  ? 205 HOH   A O   1 
HETATM 2322 O  O   D HOH   O 6 .   ? -8.279  20.357 -23.646 0.50 68.66  ? 205 HOH   A O   1 
HETATM 2323 O  O   C HOH   O 6 .   ? -1.394  29.224 -27.507 0.50 54.45  ? 206 HOH   A O   1 
HETATM 2324 O  O   D HOH   O 6 .   ? -1.394  29.224 -27.507 0.50 54.45  ? 206 HOH   A O   1 
HETATM 2325 O  O   C HOH   O 6 .   ? -8.956  19.751 -29.647 0.50 66.46  ? 207 HOH   A O   1 
HETATM 2326 O  O   D HOH   O 6 .   ? -8.956  19.751 -29.647 0.50 66.46  ? 207 HOH   A O   1 
HETATM 2327 O  O   C HOH   O 6 .   ? 18.928  8.239  -6.403  0.36 44.84  ? 208 HOH   A O   1 
HETATM 2328 O  O   D HOH   O 6 .   ? 18.927  8.239  -6.403  0.37 44.89  ? 208 HOH   A O   1 
HETATM 2329 O  O   C HOH   O 6 .   ? 17.422  19.302 0.211   0.36 50.04  ? 209 HOH   A O   1 
HETATM 2330 O  O   D HOH   O 6 .   ? 17.423  19.302 0.211   0.37 50.07  ? 209 HOH   A O   1 
HETATM 2331 O  O   C HOH   O 6 .   ? 17.376  9.735  -4.859  0.36 42.00  ? 210 HOH   A O   1 
HETATM 2332 O  O   D HOH   O 6 .   ? 17.376  9.735  -4.860  0.37 42.04  ? 210 HOH   A O   1 
HETATM 2333 O  O   C HOH   O 6 .   ? -7.532  20.067 -30.070 0.50 106.98 ? 211 HOH   A O   1 
HETATM 2334 O  O   D HOH   O 6 .   ? -7.532  20.067 -30.070 0.50 106.98 ? 211 HOH   A O   1 
HETATM 2335 O  O   C HOH   O 6 .   ? -10.971 18.817 -26.251 0.50 63.09  ? 212 HOH   A O   1 
HETATM 2336 O  O   D HOH   O 6 .   ? -10.971 18.817 -26.251 0.50 63.09  ? 212 HOH   A O   1 
HETATM 2337 O  O   C HOH   P 6 .   ? 5.972   15.221 1.601   0.50 50.42  ? 301 HOH   B O   1 
HETATM 2338 O  O   D HOH   P 6 .   ? 5.972   15.221 1.601   0.50 50.42  ? 301 HOH   B O   1 
HETATM 2339 O  O   C HOH   P 6 .   ? 2.836   7.720  -25.486 0.50 61.87  ? 302 HOH   B O   1 
HETATM 2340 O  O   D HOH   P 6 .   ? 2.836   7.720  -25.486 0.50 61.87  ? 302 HOH   B O   1 
HETATM 2341 O  O   C HOH   P 6 .   ? 4.525   32.433 -5.320  0.50 59.28  ? 303 HOH   B O   1 
HETATM 2342 O  O   D HOH   P 6 .   ? 4.525   32.433 -5.320  0.50 59.28  ? 303 HOH   B O   1 
HETATM 2343 O  O   C HOH   P 6 .   ? -12.032 21.420 -15.937 0.50 48.65  ? 304 HOH   B O   1 
HETATM 2344 O  O   D HOH   P 6 .   ? -12.032 21.420 -15.937 0.50 48.65  ? 304 HOH   B O   1 
HETATM 2345 O  O   C HOH   P 6 .   ? -4.128  11.897 -16.756 0.50 69.43  ? 305 HOH   B O   1 
HETATM 2346 O  O   D HOH   P 6 .   ? -4.128  11.897 -16.756 0.50 69.43  ? 305 HOH   B O   1 
HETATM 2347 O  O   C HOH   P 6 .   ? 6.024   9.827  -14.753 0.50 66.49  ? 306 HOH   B O   1 
HETATM 2348 O  O   D HOH   P 6 .   ? 6.024   9.827  -14.753 0.50 66.49  ? 306 HOH   B O   1 
HETATM 2349 O  O   C HOH   P 6 .   ? -0.736  34.742 -6.501  0.50 52.84  ? 307 HOH   B O   1 
HETATM 2350 O  O   D HOH   P 6 .   ? -0.736  34.742 -6.501  0.50 52.84  ? 307 HOH   B O   1 
HETATM 2351 O  O   C HOH   P 6 .   ? 15.240  29.236 -18.167 0.36 54.55  ? 308 HOH   B O   1 
HETATM 2352 O  O   D HOH   P 6 .   ? 15.240  29.236 -18.167 0.37 54.58  ? 308 HOH   B O   1 
HETATM 2353 O  O   C HOH   P 6 .   ? -10.276 26.950 -4.988  0.50 63.98  ? 309 HOH   B O   1 
HETATM 2354 O  O   D HOH   P 6 .   ? -10.276 26.950 -4.988  0.50 63.98  ? 309 HOH   B O   1 
HETATM 2355 O  O   C HOH   P 6 .   ? 3.460   34.375 -22.032 0.50 49.02  ? 310 HOH   B O   1 
HETATM 2356 O  O   D HOH   P 6 .   ? 3.460   34.375 -22.032 0.50 49.02  ? 310 HOH   B O   1 
HETATM 2357 O  O   C HOH   P 6 .   ? 0.301   6.429  -21.606 0.50 63.04  ? 311 HOH   B O   1 
HETATM 2358 O  O   D HOH   P 6 .   ? 0.301   6.429  -21.606 0.50 63.04  ? 311 HOH   B O   1 
HETATM 2359 O  O   C HOH   P 6 .   ? 9.174   16.482 -9.747  0.36 34.17  ? 312 HOH   B O   1 
HETATM 2360 O  O   D HOH   P 6 .   ? 9.174   16.482 -9.748  0.37 34.23  ? 312 HOH   B O   1 
HETATM 2361 O  O   C HOH   P 6 .   ? 20.001  34.160 -16.269 0.50 108.66 ? 313 HOH   B O   1 
HETATM 2362 O  O   D HOH   P 6 .   ? 20.001  34.160 -16.269 0.50 108.66 ? 313 HOH   B O   1 
HETATM 2363 O  O   C HOH   P 6 .   ? 3.849   8.923  -16.165 0.50 50.44  ? 314 HOH   B O   1 
HETATM 2364 O  O   D HOH   P 6 .   ? 3.849   8.923  -16.165 0.50 50.44  ? 314 HOH   B O   1 
HETATM 2365 O  O   C HOH   P 6 .   ? 3.364   9.055  -15.158 0.50 107.50 ? 315 HOH   B O   1 
HETATM 2366 O  O   D HOH   P 6 .   ? 3.364   9.055  -15.158 0.50 107.50 ? 315 HOH   B O   1 
HETATM 2367 O  O   C HOH   P 6 .   ? 9.364   21.953 -5.208  0.36 39.22  ? 316 HOH   B O   1 
HETATM 2368 O  O   D HOH   P 6 .   ? 9.364   21.953 -5.207  0.37 39.27  ? 316 HOH   B O   1 
HETATM 2369 O  O   C HOH   P 6 .   ? 5.559   40.560 -14.102 0.50 57.49  ? 317 HOH   B O   1 
HETATM 2370 O  O   D HOH   P 6 .   ? 5.559   40.560 -14.102 0.50 57.49  ? 317 HOH   B O   1 
HETATM 2371 O  O   C HOH   P 6 .   ? 10.944  31.678 -18.898 0.36 44.06  ? 318 HOH   B O   1 
HETATM 2372 O  O   D HOH   P 6 .   ? 10.944  31.677 -18.898 0.37 44.09  ? 318 HOH   B O   1 
HETATM 2373 O  O   C HOH   P 6 .   ? -0.000  27.270 -0.000  0.39 61.59  ? 319 HOH   B O   1 
HETATM 2374 O  O   D HOH   P 6 .   ? -0.000  27.269 -0.000  0.37 61.47  ? 319 HOH   B O   1 
HETATM 2375 O  O   C HOH   P 6 .   ? 2.538   9.654  -8.951  0.50 97.48  ? 320 HOH   B O   1 
HETATM 2376 O  O   D HOH   P 6 .   ? 2.538   9.654  -8.951  0.50 97.48  ? 320 HOH   B O   1 
HETATM 2377 O  O   C HOH   P 6 .   ? 5.965   5.372  -30.488 0.50 59.78  ? 321 HOH   B O   1 
HETATM 2378 O  O   D HOH   P 6 .   ? 5.965   5.372  -30.488 0.50 59.78  ? 321 HOH   B O   1 
HETATM 2379 O  O   C HOH   P 6 .   ? 17.860  18.855 -23.995 0.36 57.85  ? 322 HOH   B O   1 
HETATM 2380 O  O   D HOH   P 6 .   ? 17.860  18.856 -23.994 0.37 57.88  ? 322 HOH   B O   1 
HETATM 2381 O  O   C HOH   P 6 .   ? 8.846   17.646 -14.392 0.36 35.69  ? 323 HOH   B O   1 
HETATM 2382 O  O   D HOH   P 6 .   ? 8.846   17.647 -14.392 0.37 35.76  ? 323 HOH   B O   1 
HETATM 2383 O  O   C HOH   P 6 .   ? 15.454  19.750 -10.016 0.36 39.51  ? 324 HOH   B O   1 
HETATM 2384 O  O   D HOH   P 6 .   ? 15.454  19.751 -10.016 0.37 39.56  ? 324 HOH   B O   1 
HETATM 2385 O  O   C HOH   P 6 .   ? -8.047  18.582 -19.404 0.50 48.57  ? 325 HOH   B O   1 
HETATM 2386 O  O   D HOH   P 6 .   ? -8.047  18.582 -19.404 0.50 48.57  ? 325 HOH   B O   1 
HETATM 2387 O  O   C HOH   P 6 .   ? -9.306  24.416 -3.085  0.50 57.93  ? 326 HOH   B O   1 
HETATM 2388 O  O   D HOH   P 6 .   ? -9.306  24.416 -3.085  0.50 57.93  ? 326 HOH   B O   1 
HETATM 2389 O  O   C HOH   P 6 .   ? 5.183   34.441 -30.690 0.50 59.50  ? 327 HOH   B O   1 
HETATM 2390 O  O   D HOH   P 6 .   ? 5.183   34.441 -30.690 0.50 59.50  ? 327 HOH   B O   1 
HETATM 2391 O  O   C HOH   P 6 .   ? -4.466  15.183 -4.219  0.50 42.35  ? 328 HOH   B O   1 
HETATM 2392 O  O   D HOH   P 6 .   ? -4.466  15.183 -4.219  0.50 42.35  ? 328 HOH   B O   1 
HETATM 2393 O  O   C HOH   P 6 .   ? 2.550   6.309  -22.788 0.50 53.11  ? 329 HOH   B O   1 
HETATM 2394 O  O   D HOH   P 6 .   ? 2.550   6.309  -22.788 0.50 53.11  ? 329 HOH   B O   1 
HETATM 2395 O  O   D HOH   P 6 .   ? -7.114  27.128 0.469   0.37 49.63  ? 330 HOH   B O   1 
HETATM 2396 O  O   C HOH   P 6 .   ? 21.276  20.922 -12.842 0.36 48.28  ? 331 HOH   B O   1 
HETATM 2397 O  O   D HOH   P 6 .   ? 21.262  20.760 -12.851 0.37 48.52  ? 331 HOH   B O   1 
HETATM 2398 O  O   C HOH   P 6 .   ? -1.532  32.765 -1.252  0.50 94.79  ? 332 HOH   B O   1 
HETATM 2399 O  O   D HOH   P 6 .   ? -1.532  32.765 -1.252  0.50 94.79  ? 332 HOH   B O   1 
HETATM 2400 O  O   C HOH   P 6 .   ? 12.037  3.907  -23.960 0.50 58.19  ? 333 HOH   B O   1 
HETATM 2401 O  O   D HOH   P 6 .   ? 12.037  3.907  -23.960 0.50 58.19  ? 333 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   ? 0.9310 0.7298 0.7491 -0.0081 0.2065  -0.0654 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9155 0.7254 0.7336 0.0048  0.2072  -0.0650 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.8665 0.6943 0.6894 0.0185  0.1989  -0.0443 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.8908 0.7110 0.7278 0.0279  0.2012  -0.0303 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.9567 0.7465 0.7884 0.0110  0.2209  -0.0747 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.9606 0.7628 0.7976 0.0234  0.2237  -0.0759 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.0059 0.8094 0.8328 0.0178  0.2287  -0.0919 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 0.9936 0.8036 0.8458 0.0386  0.2215  -0.0612 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.8103 0.6597 0.6188 0.0187  0.1891  -0.0423 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.7682 0.6344 0.5748 0.0286  0.1792  -0.0250 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.7333 0.6075 0.5497 0.0436  0.1786  -0.0198 51  MET   A C   
12   O  O   . MET   A 8   ? 0.6985 0.5729 0.5191 0.0438  0.1838  -0.0310 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.7747 0.6581 0.5605 0.0214  0.1686  -0.0260 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.7891 0.6692 0.5676 0.0073  0.1675  -0.0308 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.7976 0.6980 0.5524 0.0013  0.1547  -0.0316 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8367 0.7324 0.5924 -0.0148 0.1550  -0.0382 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.6647 0.5461 0.4856 0.0561  0.1728  -0.0031 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.6539 0.5459 0.4851 0.0711  0.1693  0.0032  52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.6233 0.5323 0.4421 0.0779  0.1562  0.0158  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6098 0.5186 0.4173 0.0753  0.1530  0.0237  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.6695 0.5469 0.5219 0.0828  0.1773  0.0103  52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.6953 0.5609 0.5485 0.0870  0.1782  0.0262  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7125 0.5589 0.5662 0.0756  0.1865  0.0231  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.7023 0.5757 0.5549 0.1015  0.1709  0.0443  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7347 0.5694 0.5911 0.0779  0.1893  0.0381  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7074 0.5685 0.5597 0.1053  0.1739  0.0599  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.7245 0.5662 0.5797 0.0932  0.1838  0.0573  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.7800 0.6096 0.6361 0.0951  0.1881  0.0734  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.6134 0.5377 0.4347 0.0859  0.1490  0.0168  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.6065 0.5453 0.4133 0.0923  0.1357  0.0269  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.6057 0.5485 0.4230 0.1097  0.1310  0.0412  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.6015 0.5427 0.4397 0.1173  0.1353  0.0408  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.5914 0.5442 0.3874 0.0863  0.1282  0.0176  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.5969 0.5584 0.4111 0.0890  0.1297  0.0104  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.5969 0.5450 0.3773 0.0710  0.1312  0.0071  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.5790 0.5553 0.3841 0.0848  0.1205  0.0051  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.6261 0.5744 0.4283 0.1170  0.1221  0.0537  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.6383 0.5912 0.4436 0.1343  0.1152  0.0688  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.5970 0.5647 0.3812 0.1384  0.1008  0.0722  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.5851 0.5520 0.3494 0.1320  0.0997  0.0719  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.6997 0.6382 0.5027 0.1408  0.1214  0.0846  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.7392 0.6575 0.5569 0.1338  0.1363  0.0823  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.7828 0.6861 0.5997 0.1410  0.1424  0.1003  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.7944 0.7015 0.5933 0.1415  0.1396  0.1103  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 0.8528 0.7392 0.6871 0.1455  0.1514  0.1042  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.5908 0.5722 0.3803 0.1478  0.0899  0.0732  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.5958 0.5904 0.3652 0.1505  0.0749  0.0732  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.6097 0.5992 0.3562 0.1601  0.0722  0.0883  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.6219 0.6044 0.3746 0.1707  0.0765  0.1018  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.5932 0.6045 0.3775 0.1578  0.0636  0.0708  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.5919 0.6158 0.3598 0.1549  0.0488  0.0643  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.5995 0.6426 0.3871 0.1592  0.0374  0.0602  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.6006 0.6522 0.3720 0.1530  0.0243  0.0520  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.6212 0.6750 0.3678 0.1604  0.0105  0.0568  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.6368 0.6870 0.3714 0.1751  0.0080  0.0711  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.6119 0.6698 0.3445 0.1531  0.0000  0.0471  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.6020 0.5935 0.3237 0.1564  0.0673  0.0862  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.6288 0.6166 0.3260 0.1643  0.0667  0.0988  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.6318 0.6291 0.3057 0.1734  0.0511  0.0997  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.6366 0.6314 0.2892 0.1839  0.0504  0.1122  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.6179 0.5996 0.3057 0.1536  0.0756  0.0957  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.6164 0.6235 0.2929 0.1701  0.0394  0.0880  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.6374 0.6513 0.2898 0.1765  0.0240  0.0863  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.6446 0.6658 0.3011 0.1667  0.0142  0.0703  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.6240 0.6448 0.3001 0.1538  0.0212  0.0605  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.6582 0.6848 0.2955 0.1720  -0.0011 0.0676  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.6738 0.7048 0.3088 0.1623  -0.0121 0.0526  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.7026 0.7205 0.3103 0.1569  -0.0090 0.0473  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.7209 0.7315 0.3073 0.1650  -0.0037 0.0559  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7039 0.7453 0.3293 0.1698  -0.0315 0.0506  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.7079 0.7669 0.3625 0.1750  -0.0391 0.0536  58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.6627 0.7236 0.3433 0.1763  -0.0278 0.0597  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.7356 0.8060 0.3851 0.1790  -0.0572 0.0499  58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.6971 0.7126 0.3056 0.1445  -0.0121 0.0343  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.6947 0.6965 0.2780 0.1399  -0.0101 0.0286  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.7215 0.7210 0.2821 0.1432  -0.0261 0.0217  59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.7124 0.7147 0.2815 0.1337  -0.0353 0.0110  59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.6737 0.6705 0.2702 0.1245  -0.0016 0.0203  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.6793 0.6772 0.2935 0.1233  0.0132  0.0273  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.6961 0.6786 0.2667 0.1210  -0.0020 0.0146  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.6477 0.6412 0.2730 0.1090  0.0220  0.0196  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.7357 0.7303 0.2677 0.1563  -0.0287 0.0278  60  THR   A N   
83   N  N   B THR   A 17  ? 0.7409 0.7356 0.2729 0.1562  -0.0291 0.0277  60  THR   A N   
84   N  N   C THR   A 17  ? 0.7357 0.7303 0.2677 0.1563  -0.0287 0.0278  60  THR   A N   
85   N  N   D THR   A 17  ? 0.7409 0.7356 0.2729 0.1562  -0.0291 0.0277  60  THR   A N   
86   C  CA  A THR   A 17  ? 0.7710 0.7619 0.2747 0.1631  -0.0441 0.0223  60  THR   A CA  
87   C  CA  B THR   A 17  ? 0.7778 0.7685 0.2819 0.1622  -0.0447 0.0213  60  THR   A CA  
88   C  CA  C THR   A 17  ? 0.7710 0.7619 0.2747 0.1631  -0.0441 0.0223  60  THR   A CA  
89   C  CA  D THR   A 17  ? 0.7778 0.7685 0.2819 0.1622  -0.0447 0.0213  60  THR   A CA  
90   C  C   A THR   A 17  ? 0.7938 0.7712 0.2632 0.1723  -0.0384 0.0252  60  THR   A C   
91   C  C   B THR   A 17  ? 0.8009 0.7793 0.2698 0.1732  -0.0397 0.0254  60  THR   A C   
92   C  C   C THR   A 17  ? 0.7938 0.7712 0.2632 0.1723  -0.0384 0.0252  60  THR   A C   
93   C  C   D THR   A 17  ? 0.8009 0.7793 0.2698 0.1732  -0.0397 0.0254  60  THR   A C   
94   O  O   A THR   A 17  ? 0.7958 0.7737 0.2658 0.1780  -0.0246 0.0365  60  THR   A O   
95   O  O   B THR   A 17  ? 0.8105 0.7910 0.2784 0.1814  -0.0278 0.0383  60  THR   A O   
96   O  O   C THR   A 17  ? 0.7958 0.7737 0.2658 0.1780  -0.0246 0.0365  60  THR   A O   
97   O  O   D THR   A 17  ? 0.8105 0.7910 0.2784 0.1814  -0.0278 0.0383  60  THR   A O   
98   C  CB  A THR   A 17  ? 0.7824 0.7870 0.2884 0.1738  -0.0555 0.0287  60  THR   A CB  
99   C  CB  B THR   A 17  ? 0.7919 0.7971 0.3013 0.1707  -0.0580 0.0253  60  THR   A CB  
100  C  CB  C THR   A 17  ? 0.7824 0.7870 0.2884 0.1738  -0.0555 0.0287  60  THR   A CB  
101  C  CB  D THR   A 17  ? 0.7919 0.7971 0.3013 0.1707  -0.0580 0.0253  60  THR   A CB  
102  O  OG1 A THR   A 17  ? 0.7883 0.7915 0.2786 0.1883  -0.0476 0.0434  60  THR   A OG1 
103  O  OG1 B THR   A 17  ? 0.7855 0.8027 0.3245 0.1596  -0.0664 0.0169  60  THR   A OG1 
104  O  OG1 C THR   A 17  ? 0.7883 0.7915 0.2786 0.1883  -0.0476 0.0434  60  THR   A OG1 
105  O  OG1 D THR   A 17  ? 0.7855 0.8027 0.3245 0.1596  -0.0664 0.0169  60  THR   A OG1 
106  C  CG2 A THR   A 17  ? 0.7641 0.7848 0.3098 0.1682  -0.0565 0.0300  60  THR   A CG2 
107  C  CG2 B THR   A 17  ? 0.8176 0.8180 0.2905 0.1814  -0.0718 0.0226  60  THR   A CG2 
108  C  CG2 C THR   A 17  ? 0.7641 0.7848 0.3098 0.1682  -0.0565 0.0300  60  THR   A CG2 
109  C  CG2 D THR   A 17  ? 0.8176 0.8180 0.2905 0.1814  -0.0718 0.0226  60  THR   A CG2 
110  N  N   . TRP   A 18  ? 0.8143 0.7799 0.2564 0.1732  -0.0479 0.0148  61  TRP   A N   
111  C  CA  . TRP   A 18  ? 0.8364 0.7902 0.2428 0.1855  -0.0441 0.0168  61  TRP   A CA  
112  C  C   . TRP   A 18  ? 0.8585 0.8193 0.2463 0.2005  -0.0511 0.0245  61  TRP   A C   
113  O  O   . TRP   A 18  ? 0.8608 0.8268 0.2483 0.1997  -0.0668 0.0188  61  TRP   A O   
114  C  CB  . TRP   A 18  ? 0.8492 0.7852 0.2330 0.1813  -0.0525 0.0015  61  TRP   A CB  
115  C  CG  . TRP   A 18  ? 0.8736 0.7967 0.2217 0.1948  -0.0476 0.0022  61  TRP   A CG  
116  C  CD1 . TRP   A 18  ? 0.8890 0.8098 0.2053 0.2094  -0.0531 0.0034  61  TRP   A CD1 
117  C  CD2 . TRP   A 18  ? 0.8545 0.7662 0.1942 0.1961  -0.0358 0.0019  61  TRP   A CD2 
118  N  NE1 . TRP   A 18  ? 0.9049 0.8132 0.1941 0.2197  -0.0444 0.0030  61  TRP   A NE1 
119  C  CE2 . TRP   A 18  ? 0.8764 0.7798 0.1806 0.2123  -0.0340 0.0025  61  TRP   A CE2 
120  C  CE3 . TRP   A 18  ? 0.7997 0.7077 0.1571 0.1861  -0.0272 0.0011  61  TRP   A CE3 
121  C  CZ2 . TRP   A 18  ? 0.8885 0.7814 0.1780 0.2191  -0.0235 0.0021  61  TRP   A CZ2 
122  C  CZ3 . TRP   A 18  ? 0.8251 0.7231 0.1672 0.1927  -0.0184 0.0015  61  TRP   A CZ3 
123  C  CH2 . TRP   A 18  ? 0.8695 0.7616 0.1809 0.2094  -0.0157 0.0028  61  TRP   A CH2 
124  N  N   A GLU   A 19  ? 0.8628 0.8253 0.2385 0.2129  -0.0391 0.0382  62  GLU   A N   
125  N  N   B GLU   A 19  ? 0.8628 0.8253 0.2385 0.2129  -0.0391 0.0382  62  GLU   A N   
126  N  N   C GLU   A 19  ? 0.8768 0.8385 0.2507 0.2131  -0.0392 0.0376  62  GLU   A N   
127  N  N   D GLU   A 19  ? 0.8768 0.8385 0.2507 0.2131  -0.0392 0.0376  62  GLU   A N   
128  C  CA  A GLU   A 19  ? 0.9021 0.8692 0.2545 0.2290  -0.0431 0.0482  62  GLU   A CA  
129  C  CA  B GLU   A 19  ? 0.9021 0.8692 0.2545 0.2290  -0.0431 0.0482  62  GLU   A CA  
130  C  CA  C GLU   A 19  ? 0.9248 0.8914 0.2761 0.2290  -0.0430 0.0479  62  GLU   A CA  
131  C  CA  D GLU   A 19  ? 0.9248 0.8914 0.2761 0.2290  -0.0430 0.0479  62  GLU   A CA  
132  C  C   A GLU   A 19  ? 0.9388 0.8928 0.2472 0.2402  -0.0444 0.0428  62  GLU   A C   
133  C  C   B GLU   A 19  ? 0.9388 0.8928 0.2472 0.2402  -0.0444 0.0428  62  GLU   A C   
134  C  C   C GLU   A 19  ? 0.9642 0.9182 0.2718 0.2410  -0.0426 0.0440  62  GLU   A C   
135  C  C   D GLU   A 19  ? 0.9642 0.9182 0.2718 0.2410  -0.0426 0.0440  62  GLU   A C   
136  O  O   A GLU   A 19  ? 0.9221 0.8693 0.2223 0.2428  -0.0303 0.0445  62  GLU   A O   
137  O  O   B GLU   A 19  ? 0.9221 0.8693 0.2223 0.2428  -0.0303 0.0445  62  GLU   A O   
138  O  O   C GLU   A 19  ? 0.9482 0.8973 0.2492 0.2446  -0.0272 0.0482  62  GLU   A O   
139  O  O   D GLU   A 19  ? 0.9482 0.8973 0.2492 0.2446  -0.0272 0.0482  62  GLU   A O   
140  C  CB  A GLU   A 19  ? 0.8942 0.8699 0.2603 0.2352  -0.0276 0.0676  62  GLU   A CB  
141  C  CB  B GLU   A 19  ? 0.8942 0.8699 0.2603 0.2352  -0.0276 0.0676  62  GLU   A CB  
142  C  CB  C GLU   A 19  ? 0.9195 0.8953 0.2881 0.2339  -0.0280 0.0668  62  GLU   A CB  
143  C  CB  D GLU   A 19  ? 0.9195 0.8953 0.2881 0.2339  -0.0280 0.0668  62  GLU   A CB  
144  C  CG  A GLU   A 19  ? 0.8733 0.8602 0.2781 0.2279  -0.0281 0.0733  62  GLU   A CG  
145  C  CG  B GLU   A 19  ? 0.8733 0.8602 0.2781 0.2279  -0.0281 0.0733  62  GLU   A CG  
146  C  CG  C GLU   A 19  ? 0.9499 0.9311 0.3003 0.2491  -0.0320 0.0798  62  GLU   A CG  
147  C  CG  D GLU   A 19  ? 0.9499 0.9311 0.3003 0.2491  -0.0320 0.0798  62  GLU   A CG  
148  C  CD  A GLU   A 19  ? 0.8887 0.8843 0.2969 0.2300  -0.0472 0.0699  62  GLU   A CD  
149  C  CD  B GLU   A 19  ? 0.8887 0.8843 0.2969 0.2300  -0.0472 0.0699  62  GLU   A CD  
150  C  CD  C GLU   A 19  ? 0.9729 0.9503 0.2978 0.2621  -0.0168 0.0931  62  GLU   A CD  
151  C  CD  D GLU   A 19  ? 0.9729 0.9503 0.2978 0.2621  -0.0168 0.0931  62  GLU   A CD  
152  O  OE1 A GLU   A 19  ? 0.9099 0.9095 0.3008 0.2439  -0.0525 0.0804  62  GLU   A OE1 
153  O  OE1 B GLU   A 19  ? 0.9099 0.9095 0.3008 0.2439  -0.0525 0.0804  62  GLU   A OE1 
154  O  OE1 C GLU   A 19  ? 0.9551 0.9306 0.2898 0.2578  -0.0006 0.0957  62  GLU   A OE1 
155  O  OE1 D GLU   A 19  ? 0.9551 0.9306 0.2898 0.2578  -0.0006 0.0957  62  GLU   A OE1 
156  O  OE2 A GLU   A 19  ? 0.8757 0.8749 0.3038 0.2179  -0.0569 0.0570  62  GLU   A OE2 
157  O  OE2 B GLU   A 19  ? 0.8757 0.8749 0.3038 0.2179  -0.0569 0.0570  62  GLU   A OE2 
158  O  OE2 C GLU   A 19  ? 0.9897 0.9672 0.2858 0.2761  -0.0210 0.1010  62  GLU   A OE2 
159  O  OE2 D GLU   A 19  ? 0.9897 0.9672 0.2858 0.2761  -0.0210 0.1010  62  GLU   A OE2 
160  N  N   A LYS   A 20  ? 0.9868 0.9378 0.2678 0.2467  -0.0612 0.0355  63  LYS   A N   
161  N  N   B LYS   A 20  ? 0.9868 0.9378 0.2678 0.2467  -0.0612 0.0355  63  LYS   A N   
162  N  N   C LYS   A 20  ? 1.0180 0.9674 0.2970 0.2472  -0.0593 0.0354  63  LYS   A N   
163  N  N   D LYS   A 20  ? 1.0180 0.9674 0.2970 0.2472  -0.0593 0.0354  63  LYS   A N   
164  C  CA  A LYS   A 20  ? 1.0312 0.9679 0.2654 0.2590  -0.0634 0.0288  63  LYS   A CA  
165  C  CA  B LYS   A 20  ? 1.0312 0.9679 0.2654 0.2590  -0.0634 0.0288  63  LYS   A CA  
166  C  CA  C LYS   A 20  ? 1.0612 0.9965 0.2940 0.2598  -0.0600 0.0296  63  LYS   A CA  
167  C  CA  D LYS   A 20  ? 1.0612 0.9965 0.2940 0.2598  -0.0600 0.0296  63  LYS   A CA  
168  C  C   A LYS   A 20  ? 1.0510 0.9923 0.2657 0.2757  -0.0491 0.0467  63  LYS   A C   
169  C  C   B LYS   A 20  ? 1.0510 0.9923 0.2657 0.2757  -0.0491 0.0467  63  LYS   A C   
170  C  C   C LYS   A 20  ? 1.0803 1.0208 0.2955 0.2760  -0.0451 0.0478  63  LYS   A C   
171  C  C   D LYS   A 20  ? 1.0803 1.0208 0.2955 0.2760  -0.0451 0.0478  63  LYS   A C   
172  O  O   A LYS   A 20  ? 1.0538 1.0070 0.2765 0.2804  -0.0502 0.0604  63  LYS   A O   
173  O  O   B LYS   A 20  ? 1.0538 1.0070 0.2765 0.2804  -0.0502 0.0604  63  LYS   A O   
174  O  O   C LYS   A 20  ? 1.0650 1.0181 0.2938 0.2791  -0.0437 0.0624  63  LYS   A O   
175  O  O   D LYS   A 20  ? 1.0650 1.0181 0.2938 0.2791  -0.0437 0.0624  63  LYS   A O   
176  C  CB  A LYS   A 20  ? 1.0718 1.0047 0.2835 0.2598  -0.0870 0.0152  63  LYS   A CB  
177  C  CB  B LYS   A 20  ? 1.0718 1.0047 0.2835 0.2598  -0.0870 0.0152  63  LYS   A CB  
178  C  CB  C LYS   A 20  ? 1.1059 1.0361 0.3126 0.2618  -0.0827 0.0161  63  LYS   A CB  
179  C  CB  D LYS   A 20  ? 1.1059 1.0361 0.3126 0.2618  -0.0827 0.0161  63  LYS   A CB  
180  C  CG  A LYS   A 20  ? 1.0680 0.9972 0.3017 0.2415  -0.1005 -0.0019 63  LYS   A CG  
181  C  CG  B LYS   A 20  ? 1.0680 0.9972 0.3017 0.2415  -0.1005 -0.0019 63  LYS   A CG  
182  C  CG  C LYS   A 20  ? 1.1085 1.0312 0.3296 0.2450  -0.0967 -0.0029 63  LYS   A CG  
183  C  CG  D LYS   A 20  ? 1.1085 1.0312 0.3296 0.2450  -0.0967 -0.0029 63  LYS   A CG  
184  C  CD  A LYS   A 20  ? 1.1010 1.0285 0.3160 0.2402  -0.1249 -0.0163 63  LYS   A CD  
185  C  CD  B LYS   A 20  ? 1.1010 1.0285 0.3160 0.2402  -0.1249 -0.0163 63  LYS   A CD  
186  C  CD  C LYS   A 20  ? 1.1451 1.0648 0.3432 0.2454  -0.1205 -0.0168 63  LYS   A CD  
187  C  CD  D LYS   A 20  ? 1.1451 1.0648 0.3432 0.2454  -0.1205 -0.0168 63  LYS   A CD  
188  C  CE  A LYS   A 20  ? 1.0943 1.0188 0.3351 0.2201  -0.1362 -0.0324 63  LYS   A CE  
189  C  CE  B LYS   A 20  ? 1.0943 1.0188 0.3351 0.2201  -0.1362 -0.0324 63  LYS   A CE  
190  C  CE  C LYS   A 20  ? 1.1458 1.0572 0.3597 0.2269  -0.1333 -0.0356 63  LYS   A CE  
191  C  CE  D LYS   A 20  ? 1.1458 1.0572 0.3597 0.2269  -0.1333 -0.0356 63  LYS   A CE  
192  N  NZ  A LYS   A 20  ? 1.1235 1.0506 0.3524 0.2169  -0.1612 -0.0460 63  LYS   A NZ  
193  N  NZ  B LYS   A 20  ? 1.1235 1.0506 0.3524 0.2169  -0.1612 -0.0460 63  LYS   A NZ  
194  N  NZ  C LYS   A 20  ? 1.1794 1.0889 0.3722 0.2260  -0.1575 -0.0500 63  LYS   A NZ  
195  N  NZ  D LYS   A 20  ? 1.1794 1.0889 0.3722 0.2260  -0.1575 -0.0500 63  LYS   A NZ  
196  N  N   A ASP   A 21  ? 1.0795 1.0121 0.2727 0.2839  -0.0348 0.0477  64  ASP   A N   
197  N  N   B ASP   A 21  ? 1.0795 1.0121 0.2727 0.2839  -0.0348 0.0477  64  ASP   A N   
198  N  N   C ASP   A 21  ? 1.1193 1.0503 0.3072 0.2860  -0.0330 0.0477  64  ASP   A N   
199  N  N   D ASP   A 21  ? 1.1193 1.0503 0.3072 0.2860  -0.0330 0.0477  64  ASP   A N   
200  C  CA  A ASP   A 21  ? 1.1043 1.0426 0.2836 0.2981  -0.0167 0.0658  64  ASP   A CA  
201  C  CA  B ASP   A 21  ? 1.1043 1.0426 0.2836 0.2981  -0.0167 0.0658  64  ASP   A CA  
202  C  CA  C ASP   A 21  ? 1.1527 1.0896 0.3246 0.3008  -0.0159 0.0657  64  ASP   A CA  
203  C  CA  D ASP   A 21  ? 1.1527 1.0896 0.3246 0.3008  -0.0159 0.0657  64  ASP   A CA  
204  C  C   A ASP   A 21  ? 1.0664 1.0184 0.2879 0.2904  -0.0028 0.0819  64  ASP   A C   
205  C  C   B ASP   A 21  ? 1.0664 1.0184 0.2879 0.2904  -0.0028 0.0819  64  ASP   A C   
206  C  C   C ASP   A 21  ? 1.1083 1.0589 0.3218 0.2935  -0.0010 0.0823  64  ASP   A C   
207  C  C   D ASP   A 21  ? 1.1083 1.0589 0.3218 0.2935  -0.0010 0.0823  64  ASP   A C   
208  O  O   A ASP   A 21  ? 1.0564 1.0168 0.2841 0.2943  -0.0028 0.0959  64  ASP   A O   
209  O  O   B ASP   A 21  ? 1.0564 1.0168 0.2841 0.2943  -0.0028 0.0959  64  ASP   A O   
210  O  O   C ASP   A 21  ? 1.1159 1.0750 0.3332 0.2986  0.0010  0.0977  64  ASP   A O   
211  O  O   D ASP   A 21  ? 1.1159 1.0750 0.3332 0.2986  0.0010  0.0977  64  ASP   A O   
212  C  CB  A ASP   A 21  ? 1.1601 1.0992 0.3027 0.3131  -0.0248 0.0721  64  ASP   A CB  
213  C  CB  B ASP   A 21  ? 1.1601 1.0992 0.3027 0.3131  -0.0248 0.0721  64  ASP   A CB  
214  C  CB  C ASP   A 21  ? 1.2122 1.1503 0.3498 0.3145  -0.0258 0.0715  64  ASP   A CB  
215  C  CB  D ASP   A 21  ? 1.2122 1.1503 0.3498 0.3145  -0.0258 0.0715  64  ASP   A CB  
216  C  CG  A ASP   A 21  ? 1.2095 1.1340 0.3009 0.3258  -0.0294 0.0602  64  ASP   A CG  
217  C  CG  B ASP   A 21  ? 1.2095 1.1340 0.3009 0.3258  -0.0294 0.0602  64  ASP   A CG  
218  C  CG  C ASP   A 21  ? 1.2553 1.1834 0.3646 0.3150  -0.0496 0.0525  64  ASP   A CG  
219  C  CG  D ASP   A 21  ? 1.2553 1.1834 0.3646 0.3150  -0.0496 0.0525  64  ASP   A CG  
220  O  OD1 A ASP   A 21  ? 1.2145 1.1318 0.2940 0.3313  -0.0144 0.0581  64  ASP   A OD1 
221  O  OD1 B ASP   A 21  ? 1.2145 1.1318 0.2940 0.3313  -0.0144 0.0581  64  ASP   A OD1 
222  O  OD1 C ASP   A 21  ? 1.2637 1.1793 0.3724 0.3068  -0.0551 0.0343  64  ASP   A OD1 
223  O  OD1 D ASP   A 21  ? 1.2637 1.1793 0.3724 0.3068  -0.0551 0.0343  64  ASP   A OD1 
224  O  OD2 A ASP   A 21  ? 1.2408 1.1614 0.3050 0.3305  -0.0482 0.0526  64  ASP   A OD2 
225  O  OD2 B ASP   A 21  ? 1.2408 1.1614 0.3050 0.3305  -0.0482 0.0526  64  ASP   A OD2 
226  O  OD2 C ASP   A 21  ? 1.2916 1.2239 0.3790 0.3236  -0.0628 0.0564  64  ASP   A OD2 
227  O  OD2 D ASP   A 21  ? 1.2916 1.2239 0.3790 0.3236  -0.0628 0.0564  64  ASP   A OD2 
228  N  N   A ALA   A 22  ? 1.0425 0.9953 0.2922 0.2795  0.0070  0.0791  65  ALA   A N   
229  N  N   B ALA   A 22  ? 1.0425 0.9953 0.2922 0.2795  0.0070  0.0791  65  ALA   A N   
230  N  N   C ALA   A 22  ? 1.0837 1.0354 0.3273 0.2817  0.0076  0.0789  65  ALA   A N   
231  N  N   D ALA   A 22  ? 1.0837 1.0354 0.3273 0.2817  0.0076  0.0789  65  ALA   A N   
232  C  CA  A ALA   A 22  ? 1.0040 0.9677 0.2882 0.2732  0.0239  0.0933  65  ALA   A CA  
233  C  CA  B ALA   A 22  ? 1.0040 0.9677 0.2882 0.2732  0.0239  0.0933  65  ALA   A CA  
234  C  CA  C ALA   A 22  ? 1.0311 0.9941 0.3113 0.2746  0.0235  0.0929  65  ALA   A CA  
235  C  CA  D ALA   A 22  ? 1.0311 0.9941 0.3113 0.2746  0.0235  0.0929  65  ALA   A CA  
236  C  C   A ALA   A 22  ? 1.0022 0.9682 0.2750 0.2821  0.0429  0.1011  65  ALA   A C   
237  C  C   B ALA   A 22  ? 1.0022 0.9682 0.2750 0.2821  0.0429  0.1011  65  ALA   A C   
238  C  C   C ALA   A 22  ? 1.0180 0.9839 0.2891 0.2829  0.0432  0.1014  65  ALA   A C   
239  C  C   D ALA   A 22  ? 1.0180 0.9839 0.2891 0.2829  0.0432  0.1014  65  ALA   A C   
240  O  O   A ALA   A 22  ? 1.0214 0.9789 0.2648 0.2907  0.0420  0.0916  65  ALA   A O   
241  O  O   B ALA   A 22  ? 1.0214 0.9789 0.2648 0.2907  0.0420  0.0916  65  ALA   A O   
242  O  O   C ALA   A 22  ? 1.0403 0.9981 0.2816 0.2921  0.0433  0.0927  65  ALA   A O   
243  O  O   D ALA   A 22  ? 1.0403 0.9981 0.2816 0.2921  0.0433  0.0927  65  ALA   A O   
244  C  CB  A ALA   A 22  ? 0.9787 0.9433 0.2990 0.2556  0.0215  0.0845  65  ALA   A CB  
245  C  CB  B ALA   A 22  ? 0.9787 0.9433 0.2990 0.2556  0.0215  0.0845  65  ALA   A CB  
246  C  CB  C ALA   A 22  ? 1.0073 0.9708 0.3230 0.2570  0.0203  0.0836  65  ALA   A CB  
247  C  CB  D ALA   A 22  ? 1.0073 0.9708 0.3230 0.2570  0.0203  0.0836  65  ALA   A CB  
248  N  N   . GLU   A 23  ? 0.9967 0.9737 0.2926 0.2801  0.0594  0.1174  66  GLU   A N   
249  C  CA  . GLU   A 23  ? 0.9922 0.9766 0.2886 0.2853  0.0793  0.1258  66  GLU   A CA  
250  C  C   . GLU   A 23  ? 0.9667 0.9485 0.2685 0.2806  0.0785  0.1114  66  GLU   A C   
251  O  O   . GLU   A 23  ? 0.8855 0.8646 0.2099 0.2669  0.0697  0.1018  66  GLU   A O   
252  C  CB  . GLU   A 23  ? 1.0185 1.0150 0.3513 0.2764  0.0944  0.1411  66  GLU   A CB  
253  C  CG  . GLU   A 23  ? 1.0409 1.0490 0.3837 0.2778  0.1131  0.1475  66  GLU   A CG  
254  C  CD  . GLU   A 23  ? 1.0806 1.1003 0.4538 0.2707  0.1296  0.1649  66  GLU   A CD  
255  O  OE1 . GLU   A 23  ? 1.1487 1.1657 0.5185 0.2736  0.1328  0.1786  66  GLU   A OE1 
256  O  OE2 . GLU   A 23  ? 1.1038 1.1346 0.5040 0.2621  0.1389  0.1649  66  GLU   A OE2 
257  N  N   . VAL   A 24  ? 0.9695 0.9506 0.2490 0.2927  0.0865  0.1092  67  VAL   A N   
258  C  CA  . VAL   A 24  ? 0.9643 0.9411 0.2469 0.2908  0.0853  0.0962  67  VAL   A CA  
259  C  C   . VAL   A 24  ? 0.9398 0.9338 0.2406 0.2937  0.1044  0.1062  67  VAL   A C   
260  O  O   . VAL   A 24  ? 0.9901 0.9931 0.2803 0.3047  0.1182  0.1180  67  VAL   A O   
261  C  CB  . VAL   A 24  ? 0.9995 0.9578 0.2406 0.3027  0.0754  0.0817  67  VAL   A CB  
262  C  CG1 . VAL   A 24  ? 0.9826 0.9307 0.2272 0.2992  0.0706  0.0676  67  VAL   A CG1 
263  C  CG2 . VAL   A 24  ? 1.0082 0.9547 0.2315 0.3006  0.0573  0.0749  67  VAL   A CG2 
264  N  N   . THR   A 25  ? 0.8954 0.8966 0.2269 0.2826  0.1057  0.1034  68  THR   A N   
265  C  CA  . THR   A 25  ? 0.8738 0.8961 0.2290 0.2834  0.1227  0.1138  68  THR   A CA  
266  C  C   . THR   A 25  ? 0.8373 0.8632 0.2179 0.2727  0.1183  0.1059  68  THR   A C   
267  O  O   . THR   A 25  ? 0.8129 0.8223 0.1874 0.2666  0.1036  0.0929  68  THR   A O   
268  C  CB  . THR   A 25  ? 0.8594 0.8959 0.2360 0.2774  0.1346  0.1309  68  THR   A CB  
269  O  OG1 . THR   A 25  ? 0.8662 0.9229 0.2551 0.2831  0.1527  0.1410  68  THR   A OG1 
270  C  CG2 . THR   A 25  ? 0.8548 0.8928 0.2655 0.2579  0.1292  0.1312  68  THR   A CG2 
271  N  N   . GLY   A 26  ? 0.8303 0.8772 0.2354 0.2720  0.1305  0.1133  69  GLY   A N   
272  C  CA  . GLY   A 26  ? 0.8224 0.8762 0.2505 0.2640  0.1267  0.1073  69  GLY   A CA  
273  C  C   . GLY   A 26  ? 0.8423 0.8880 0.2499 0.2781  0.1235  0.0979  69  GLY   A C   
274  O  O   . GLY   A 26  ? 0.8451 0.8698 0.2173 0.2894  0.1177  0.0898  69  GLY   A O   
275  N  N   . ASN   A 27  ? 0.8411 0.9024 0.2719 0.2761  0.1257  0.0982  70  ASN   A N   
276  C  CA  . ASN   A 27  ? 0.8451 0.9021 0.2648 0.2892  0.1233  0.0912  70  ASN   A CA  
277  C  C   . ASN   A 27  ? 0.8421 0.8814 0.2625 0.2783  0.1076  0.0804  70  ASN   A C   
278  O  O   . ASN   A 27  ? 0.8034 0.8334 0.2300 0.2616  0.0993  0.0775  70  ASN   A O   
279  C  CB  . ASN   A 27  ? 0.8559 0.9445 0.2994 0.2973  0.1373  0.1007  70  ASN   A CB  
280  C  CG  . ASN   A 27  ? 0.8318 0.9429 0.3156 0.2817  0.1354  0.1044  70  ASN   A CG  
281  O  OD1 . ASN   A 27  ? 0.8370 0.9536 0.3407 0.2641  0.1347  0.1082  70  ASN   A OD1 
282  N  ND2 . ASN   A 27  ? 0.8422 0.9675 0.3381 0.2892  0.1352  0.1037  70  ASN   A ND2 
283  N  N   . SER   A 28  ? 0.8545 0.8868 0.2667 0.2881  0.1038  0.0747  71  SER   A N   
284  C  CA  . SER   A 28  ? 0.8440 0.8543 0.2495 0.2805  0.0897  0.0650  71  SER   A CA  
285  C  C   . SER   A 28  ? 0.8256 0.8497 0.2471 0.2857  0.0896  0.0672  71  SER   A C   
286  O  O   . SER   A 28  ? 0.8465 0.8532 0.2487 0.2990  0.0859  0.0618  71  SER   A O   
287  C  CB  . SER   A 28  ? 0.9071 0.8829 0.2758 0.2892  0.0821  0.0539  71  SER   A CB  
288  O  OG  . SER   A 28  ? 0.9706 0.9355 0.3183 0.2919  0.0827  0.0515  71  SER   A OG  
289  N  N   . PRO   A 29  ? 0.8170 0.8705 0.2730 0.2754  0.0924  0.0746  72  PRO   A N   
290  C  CA  . PRO   A 29  ? 0.7907 0.8636 0.2644 0.2819  0.0920  0.0779  72  PRO   A CA  
291  C  C   . PRO   A 29  ? 0.8092 0.8603 0.2730 0.2761  0.0778  0.0709  72  PRO   A C   
292  O  O   . PRO   A 29  ? 0.7841 0.8177 0.2425 0.2597  0.0704  0.0658  72  PRO   A O   
293  C  CB  . PRO   A 29  ? 0.7701 0.8784 0.2822 0.2684  0.0980  0.0864  72  PRO   A CB  
294  C  CG  . PRO   A 29  ? 0.7519 0.8465 0.2643 0.2479  0.0935  0.0834  72  PRO   A CG  
295  C  CD  . PRO   A 29  ? 0.7966 0.8631 0.2758 0.2557  0.0937  0.0788  72  PRO   A CD  
296  N  N   . ARG   A 30  ? 0.8366 0.8884 0.2972 0.2905  0.0750  0.0712  73  ARG   A N   
297  C  CA  . ARG   A 30  ? 0.8680 0.9041 0.3225 0.2862  0.0624  0.0679  73  ARG   A CA  
298  C  C   . ARG   A 30  ? 0.8229 0.8936 0.3098 0.2802  0.0597  0.0744  73  ARG   A C   
299  O  O   . ARG   A 30  ? 0.8343 0.9303 0.3364 0.2952  0.0641  0.0802  73  ARG   A O   
300  C  CB  . ARG   A 30  ? 0.9468 0.9572 0.3743 0.3069  0.0600  0.0644  73  ARG   A CB  
301  C  CG  . ARG   A 30  ? 0.9791 0.9517 0.3726 0.3102  0.0602  0.0557  73  ARG   A CG  
302  C  CD  . ARG   A 30  ? 1.0792 1.0222 0.4455 0.3296  0.0578  0.0512  73  ARG   A CD  
303  N  NE  . ARG   A 30  ? 1.1881 1.1007 0.5238 0.3354  0.0597  0.0423  73  ARG   A NE  
304  C  CZ  . ARG   A 30  ? 1.2099 1.0873 0.5230 0.3239  0.0518  0.0333  73  ARG   A CZ  
305  N  NH1 . ARG   A 30  ? 1.1891 1.0552 0.5060 0.3061  0.0426  0.0326  73  ARG   A NH1 
306  N  NH2 . ARG   A 30  ? 1.1736 1.0282 0.4602 0.3305  0.0533  0.0248  73  ARG   A NH2 
307  N  N   . LEU   A 31  ? 0.7889 0.8618 0.2866 0.2591  0.0528  0.0729  74  LEU   A N   
308  C  CA  . LEU   A 31  ? 0.7645 0.8718 0.2940 0.2496  0.0497  0.0776  74  LEU   A CA  
309  C  C   . LEU   A 31  ? 0.7543 0.8484 0.2739 0.2431  0.0361  0.0749  74  LEU   A C   
310  O  O   . LEU   A 31  ? 0.7493 0.8123 0.2474 0.2326  0.0314  0.0690  74  LEU   A O   
311  C  CB  . LEU   A 31  ? 0.7399 0.8608 0.2900 0.2290  0.0544  0.0776  74  LEU   A CB  
312  C  CG  . LEU   A 31  ? 0.7461 0.8786 0.3051 0.2329  0.0683  0.0820  74  LEU   A CG  
313  C  CD1 . LEU   A 31  ? 0.7343 0.8615 0.3004 0.2129  0.0706  0.0801  74  LEU   A CD1 
314  C  CD2 . LEU   A 31  ? 0.7372 0.9109 0.3279 0.2397  0.0761  0.0904  74  LEU   A CD2 
315  N  N   A ASP   A 32  ? 0.7591 0.8777 0.2944 0.2493  0.0300  0.0796  75  ASP   A N   
316  N  N   B ASP   A 32  ? 0.7592 0.8778 0.2944 0.2493  0.0300  0.0796  75  ASP   A N   
317  N  N   C ASP   A 32  ? 0.7702 0.8881 0.3047 0.2498  0.0300  0.0795  75  ASP   A N   
318  N  N   D ASP   A 32  ? 0.7702 0.8881 0.3047 0.2498  0.0300  0.0795  75  ASP   A N   
319  C  CA  A ASP   A 32  ? 0.7632 0.8770 0.2926 0.2417  0.0164  0.0787  75  ASP   A CA  
320  C  CA  B ASP   A 32  ? 0.7633 0.8770 0.2926 0.2417  0.0164  0.0787  75  ASP   A CA  
321  C  CA  C ASP   A 32  ? 0.7771 0.8895 0.3054 0.2415  0.0165  0.0785  75  ASP   A CA  
322  C  CA  D ASP   A 32  ? 0.7771 0.8895 0.3054 0.2415  0.0165  0.0785  75  ASP   A CA  
323  C  C   A ASP   A 32  ? 0.7361 0.8678 0.2860 0.2173  0.0141  0.0760  75  ASP   A C   
324  C  C   B ASP   A 32  ? 0.7361 0.8678 0.2860 0.2173  0.0141  0.0760  75  ASP   A C   
325  C  C   C ASP   A 32  ? 0.7398 0.8707 0.2892 0.2173  0.0144  0.0759  75  ASP   A C   
326  C  C   D ASP   A 32  ? 0.7398 0.8707 0.2892 0.2173  0.0144  0.0759  75  ASP   A C   
327  O  O   A ASP   A 32  ? 0.7206 0.8884 0.3026 0.2135  0.0179  0.0791  75  ASP   A O   
328  O  O   B ASP   A 32  ? 0.7206 0.8884 0.3026 0.2135  0.0179  0.0791  75  ASP   A O   
329  O  O   C ASP   A 32  ? 0.7228 0.8894 0.3042 0.2136  0.0186  0.0790  75  ASP   A O   
330  O  O   D ASP   A 32  ? 0.7228 0.8894 0.3042 0.2136  0.0186  0.0790  75  ASP   A O   
331  C  CB  A ASP   A 32  ? 0.7823 0.9174 0.3207 0.2594  0.0096  0.0852  75  ASP   A CB  
332  C  CB  B ASP   A 32  ? 0.7824 0.9175 0.3208 0.2594  0.0096  0.0852  75  ASP   A CB  
333  C  CB  C ASP   A 32  ? 0.8096 0.9418 0.3456 0.2589  0.0091  0.0849  75  ASP   A CB  
334  C  CB  D ASP   A 32  ? 0.8096 0.9418 0.3457 0.2589  0.0091  0.0849  75  ASP   A CB  
335  C  CG  A ASP   A 32  ? 0.8111 0.9299 0.3320 0.2859  0.0137  0.0877  75  ASP   A CG  
336  C  CG  B ASP   A 32  ? 0.8113 0.9300 0.3322 0.2859  0.0138  0.0877  75  ASP   A CG  
337  C  CG  C ASP   A 32  ? 0.8552 0.9633 0.3673 0.2840  0.0104  0.0868  75  ASP   A CG  
338  C  CG  D ASP   A 32  ? 0.8552 0.9634 0.3674 0.2840  0.0104  0.0868  75  ASP   A CG  
339  O  OD1 A ASP   A 32  ? 0.8274 0.9026 0.3140 0.2894  0.0124  0.0837  75  ASP   A OD1 
340  O  OD1 B ASP   A 32  ? 0.8275 0.9027 0.3141 0.2894  0.0124  0.0837  75  ASP   A OD1 
341  O  OD1 C ASP   A 32  ? 0.8652 0.9330 0.3476 0.2852  0.0140  0.0816  75  ASP   A OD1 
342  O  OD1 D ASP   A 32  ? 0.8652 0.9330 0.3476 0.2852  0.0140  0.0817  75  ASP   A OD1 
343  O  OD2 A ASP   A 32  ? 0.8177 0.9672 0.3601 0.3025  0.0190  0.0933  75  ASP   A OD2 
344  O  OD2 B ASP   A 32  ? 0.8178 0.9673 0.3602 0.3025  0.0191  0.0933  75  ASP   A OD2 
345  O  OD2 C ASP   A 32  ? 0.8940 1.0242 0.4184 0.3025  0.0076  0.0931  75  ASP   A OD2 
346  O  OD2 D ASP   A 32  ? 0.8941 1.0243 0.4186 0.3025  0.0076  0.0931  75  ASP   A OD2 
347  N  N   A VAL   A 33  ? 0.7347 0.8416 0.2673 0.2011  0.0090  0.0701  76  VAL   A N   
348  N  N   B VAL   A 33  ? 0.7347 0.8417 0.2673 0.2011  0.0090  0.0701  76  VAL   A N   
349  N  N   C VAL   A 33  ? 0.7377 0.8445 0.2702 0.2011  0.0090  0.0701  76  VAL   A N   
350  N  N   D VAL   A 33  ? 0.7377 0.8445 0.2702 0.2011  0.0090  0.0701  76  VAL   A N   
351  C  CA  A VAL   A 33  ? 0.7116 0.8293 0.2595 0.1776  0.0078  0.0655  76  VAL   A CA  
352  C  CA  B VAL   A 33  ? 0.7116 0.8294 0.2595 0.1776  0.0078  0.0655  76  VAL   A CA  
353  C  CA  C VAL   A 33  ? 0.7118 0.8296 0.2597 0.1777  0.0078  0.0655  76  VAL   A CA  
354  C  CA  D VAL   A 33  ? 0.7118 0.8296 0.2597 0.1777  0.0078  0.0655  76  VAL   A CA  
355  C  C   A VAL   A 33  ? 0.7221 0.8254 0.2517 0.1679  -0.0035 0.0620  76  VAL   A C   
356  C  C   B VAL   A 33  ? 0.7221 0.8254 0.2517 0.1679  -0.0035 0.0620  76  VAL   A C   
357  C  C   C VAL   A 33  ? 0.7214 0.8247 0.2511 0.1679  -0.0035 0.0620  76  VAL   A C   
358  C  C   D VAL   A 33  ? 0.7214 0.8247 0.2511 0.1679  -0.0035 0.0620  76  VAL   A C   
359  O  O   A VAL   A 33  ? 0.7426 0.8182 0.2436 0.1764  -0.0079 0.0629  76  VAL   A O   
360  O  O   B VAL   A 33  ? 0.7427 0.8182 0.2437 0.1764  -0.0079 0.0628  76  VAL   A O   
361  O  O   C VAL   A 33  ? 0.7430 0.8184 0.2438 0.1763  -0.0080 0.0628  76  VAL   A O   
362  O  O   D VAL   A 33  ? 0.7430 0.8184 0.2438 0.1763  -0.0080 0.0628  76  VAL   A O   
363  C  CB  A VAL   A 33  ? 0.6920 0.7945 0.2393 0.1660  0.0176  0.0610  76  VAL   A CB  
364  C  CB  B VAL   A 33  ? 0.6920 0.7945 0.2393 0.1660  0.0176  0.0610  76  VAL   A CB  
365  C  CB  C VAL   A 33  ? 0.6907 0.7933 0.2382 0.1660  0.0176  0.0610  76  VAL   A CB  
366  C  CB  D VAL   A 33  ? 0.6907 0.7933 0.2381 0.1660  0.0176  0.0610  76  VAL   A CB  
367  C  CG1 A VAL   A 33  ? 0.6808 0.7983 0.2442 0.1749  0.0291  0.0656  76  VAL   A CG1 
368  C  CG1 B VAL   A 33  ? 0.6808 0.7982 0.2442 0.1749  0.0291  0.0656  76  VAL   A CG1 
369  C  CG1 C VAL   A 33  ? 0.6769 0.7944 0.2404 0.1749  0.0292  0.0656  76  VAL   A CG1 
370  C  CG1 D VAL   A 33  ? 0.6769 0.7944 0.2404 0.1749  0.0292  0.0656  76  VAL   A CG1 
371  C  CG2 A VAL   A 33  ? 0.7012 0.7639 0.2169 0.1655  0.0170  0.0564  76  VAL   A CG2 
372  C  CG2 B VAL   A 33  ? 0.7012 0.7638 0.2169 0.1655  0.0170  0.0564  76  VAL   A CG2 
373  C  CG2 C VAL   A 33  ? 0.7001 0.7628 0.2158 0.1655  0.0170  0.0564  76  VAL   A CG2 
374  C  CG2 D VAL   A 33  ? 0.7001 0.7628 0.2158 0.1655  0.0170  0.0564  76  VAL   A CG2 
375  N  N   A ALA   A 34  ? 0.7142 0.8342 0.2586 0.1503  -0.0074 0.0581  77  ALA   A N   
376  N  N   B ALA   A 34  ? 0.7143 0.8342 0.2587 0.1503  -0.0074 0.0581  77  ALA   A N   
377  N  N   C ALA   A 34  ? 0.7137 0.8337 0.2582 0.1503  -0.0074 0.0581  77  ALA   A N   
378  N  N   D ALA   A 34  ? 0.7137 0.8337 0.2582 0.1503  -0.0074 0.0581  77  ALA   A N   
379  C  CA  A ALA   A 34  ? 0.7227 0.8292 0.2490 0.1372  -0.0162 0.0532  77  ALA   A CA  
380  C  CA  B ALA   A 34  ? 0.7227 0.8292 0.2490 0.1372  -0.0162 0.0532  77  ALA   A CA  
381  C  CA  C ALA   A 34  ? 0.7204 0.8270 0.2468 0.1371  -0.0162 0.0531  77  ALA   A CA  
382  C  CA  D ALA   A 34  ? 0.7204 0.8270 0.2468 0.1371  -0.0162 0.0531  77  ALA   A CA  
383  C  C   A ALA   A 34  ? 0.7098 0.8050 0.2384 0.1166  -0.0094 0.0447  77  ALA   A C   
384  C  C   B ALA   A 34  ? 0.7098 0.8050 0.2384 0.1166  -0.0094 0.0447  77  ALA   A C   
385  C  C   C ALA   A 34  ? 0.7079 0.8032 0.2367 0.1166  -0.0094 0.0447  77  ALA   A C   
386  C  C   D ALA   A 34  ? 0.7079 0.8032 0.2367 0.1166  -0.0094 0.0447  77  ALA   A C   
387  O  O   A ALA   A 34  ? 0.6857 0.7945 0.2384 0.1107  -0.0012 0.0436  77  ALA   A O   
388  O  O   B ALA   A 34  ? 0.6857 0.7945 0.2384 0.1107  -0.0012 0.0436  77  ALA   A O   
389  O  O   C ALA   A 34  ? 0.6815 0.7905 0.2344 0.1107  -0.0011 0.0436  77  ALA   A O   
390  O  O   D ALA   A 34  ? 0.6815 0.7904 0.2344 0.1107  -0.0011 0.0436  77  ALA   A O   
391  C  CB  A ALA   A 34  ? 0.7336 0.8701 0.2727 0.1357  -0.0283 0.0547  77  ALA   A CB  
392  C  CB  B ALA   A 34  ? 0.7336 0.8701 0.2727 0.1357  -0.0283 0.0547  77  ALA   A CB  
393  C  CB  C ALA   A 34  ? 0.7351 0.8715 0.2741 0.1357  -0.0283 0.0547  77  ALA   A CB  
394  C  CB  D ALA   A 34  ? 0.7351 0.8715 0.2741 0.1357  -0.0283 0.0547  77  ALA   A CB  
395  N  N   A LEU   A 35  ? 0.7202 0.7901 0.2240 0.1069  -0.0119 0.0397  78  LEU   A N   
396  N  N   B LEU   A 35  ? 0.7202 0.7901 0.2240 0.1069  -0.0119 0.0397  78  LEU   A N   
397  N  N   C LEU   A 35  ? 0.7116 0.7816 0.2159 0.1069  -0.0116 0.0397  78  LEU   A N   
398  N  N   D LEU   A 35  ? 0.7116 0.7816 0.2159 0.1069  -0.0116 0.0397  78  LEU   A N   
399  C  CA  A LEU   A 35  ? 0.7154 0.7726 0.2189 0.0882  -0.0054 0.0310  78  LEU   A CA  
400  C  CA  B LEU   A 35  ? 0.7155 0.7726 0.2189 0.0882  -0.0054 0.0310  78  LEU   A CA  
401  C  CA  C LEU   A 35  ? 0.7062 0.7646 0.2112 0.0880  -0.0052 0.0310  78  LEU   A CA  
402  C  CA  D LEU   A 35  ? 0.7062 0.7646 0.2112 0.0880  -0.0052 0.0310  78  LEU   A CA  
403  C  C   A LEU   A 35  ? 0.7269 0.7862 0.2203 0.0752  -0.0133 0.0254  78  LEU   A C   
404  C  C   B LEU   A 35  ? 0.7269 0.7863 0.2203 0.0752  -0.0133 0.0254  78  LEU   A C   
405  C  C   C LEU   A 35  ? 0.7136 0.7757 0.2099 0.0752  -0.0133 0.0255  78  LEU   A C   
406  C  C   D LEU   A 35  ? 0.7136 0.7757 0.2099 0.0752  -0.0133 0.0255  78  LEU   A C   
407  O  O   A LEU   A 35  ? 0.7532 0.7946 0.2179 0.0777  -0.0190 0.0268  78  LEU   A O   
408  O  O   B LEU   A 35  ? 0.7534 0.7948 0.2181 0.0777  -0.0190 0.0268  78  LEU   A O   
409  O  O   C LEU   A 35  ? 0.7444 0.7931 0.2140 0.0795  -0.0207 0.0279  78  LEU   A O   
410  O  O   D LEU   A 35  ? 0.7444 0.7932 0.2140 0.0795  -0.0207 0.0279  78  LEU   A O   
411  C  CB  A LEU   A 35  ? 0.7230 0.7469 0.2049 0.0893  0.0009  0.0298  78  LEU   A CB  
412  C  CB  B LEU   A 35  ? 0.7231 0.7469 0.2050 0.0893  0.0009  0.0298  78  LEU   A CB  
413  C  CB  C LEU   A 35  ? 0.7173 0.7421 0.2004 0.0886  0.0011  0.0295  78  LEU   A CB  
414  C  CB  D LEU   A 35  ? 0.7173 0.7421 0.2005 0.0886  0.0011  0.0295  78  LEU   A CB  
415  C  CG  A LEU   A 35  ? 0.7215 0.7314 0.2027 0.0725  0.0082  0.0214  78  LEU   A CG  
416  C  CG  B LEU   A 35  ? 0.7216 0.7315 0.2028 0.0725  0.0082  0.0214  78  LEU   A CG  
417  C  CG  C LEU   A 35  ? 0.7216 0.7334 0.2053 0.0717  0.0086  0.0211  78  LEU   A CG  
418  C  CG  D LEU   A 35  ? 0.7217 0.7335 0.2054 0.0717  0.0086  0.0211  78  LEU   A CG  
419  C  CD1 A LEU   A 35  ? 0.6994 0.7237 0.2092 0.0666  0.0162  0.0190  78  LEU   A CD1 
420  C  CD1 B LEU   A 35  ? 0.6995 0.7238 0.2092 0.0666  0.0162  0.0190  78  LEU   A CD1 
421  C  CD1 C LEU   A 35  ? 0.6985 0.7247 0.2109 0.0667  0.0165  0.0191  78  LEU   A CD1 
422  C  CD1 D LEU   A 35  ? 0.6985 0.7248 0.2109 0.0667  0.0165  0.0191  78  LEU   A CD1 
423  C  CD2 A LEU   A 35  ? 0.7319 0.7119 0.1928 0.0736  0.0127  0.0207  78  LEU   A CD2 
424  C  CD2 B LEU   A 35  ? 0.7321 0.7121 0.1930 0.0736  0.0127  0.0207  78  LEU   A CD2 
425  C  CD2 C LEU   A 35  ? 0.7358 0.7176 0.1992 0.0723  0.0132  0.0201  78  LEU   A CD2 
426  C  CD2 D LEU   A 35  ? 0.7358 0.7176 0.1992 0.0723  0.0132  0.0201  78  LEU   A CD2 
427  N  N   A ASP   A 36  ? 0.7152 0.7945 0.2298 0.0619  -0.0137 0.0194  79  ASP   A N   
428  N  N   B ASP   A 36  ? 0.7152 0.7944 0.2298 0.0619  -0.0137 0.0194  79  ASP   A N   
429  N  N   C ASP   A 36  ? 0.6969 0.7762 0.2136 0.0608  -0.0126 0.0188  79  ASP   A N   
430  N  N   D ASP   A 36  ? 0.6969 0.7762 0.2136 0.0608  -0.0126 0.0188  79  ASP   A N   
431  C  CA  A ASP   A 36  ? 0.7276 0.8115 0.2334 0.0485  -0.0219 0.0120  79  ASP   A CA  
432  C  CA  B ASP   A 36  ? 0.7276 0.8115 0.2334 0.0485  -0.0219 0.0120  79  ASP   A CA  
433  C  CA  C ASP   A 36  ? 0.7108 0.7947 0.2182 0.0477  -0.0210 0.0116  79  ASP   A CA  
434  C  CA  D ASP   A 36  ? 0.7108 0.7947 0.2182 0.0477  -0.0210 0.0116  79  ASP   A CA  
435  C  C   A ASP   A 36  ? 0.7303 0.7871 0.2179 0.0350  -0.0141 0.0032  79  ASP   A C   
436  C  C   B ASP   A 36  ? 0.7303 0.7870 0.2178 0.0350  -0.0141 0.0032  79  ASP   A C   
437  C  C   C ASP   A 36  ? 0.7101 0.7670 0.1991 0.0342  -0.0134 0.0028  79  ASP   A C   
438  C  C   D ASP   A 36  ? 0.7101 0.7670 0.1991 0.0342  -0.0134 0.0028  79  ASP   A C   
439  O  O   A ASP   A 36  ? 0.7136 0.7518 0.1997 0.0364  -0.0034 0.0036  79  ASP   A O   
440  O  O   B ASP   A 36  ? 0.7135 0.7517 0.1996 0.0364  -0.0034 0.0036  79  ASP   A O   
441  O  O   C ASP   A 36  ? 0.6800 0.7188 0.1687 0.0349  -0.0025 0.0027  79  ASP   A O   
442  O  O   D ASP   A 36  ? 0.6800 0.7188 0.1686 0.0349  -0.0025 0.0027  79  ASP   A O   
443  C  CB  A ASP   A 36  ? 0.7209 0.8366 0.2578 0.0391  -0.0259 0.0080  79  ASP   A CB  
444  C  CB  B ASP   A 36  ? 0.7210 0.8366 0.2579 0.0391  -0.0259 0.0080  79  ASP   A CB  
445  C  CB  C ASP   A 36  ? 0.7077 0.8233 0.2458 0.0383  -0.0253 0.0076  79  ASP   A CB  
446  C  CB  D ASP   A 36  ? 0.7077 0.8233 0.2458 0.0383  -0.0253 0.0076  79  ASP   A CB  
447  C  CG  A ASP   A 36  ? 0.7039 0.8187 0.2645 0.0259  -0.0137 0.0014  79  ASP   A CG  
448  C  CG  B ASP   A 36  ? 0.7039 0.8187 0.2645 0.0259  -0.0137 0.0014  79  ASP   A CG  
449  C  CG  C ASP   A 36  ? 0.6983 0.8141 0.2616 0.0246  -0.0131 0.0008  79  ASP   A CG  
450  C  CG  D ASP   A 36  ? 0.6983 0.8141 0.2616 0.0246  -0.0131 0.0008  79  ASP   A CG  
451  O  OD1 A ASP   A 36  ? 0.6972 0.7889 0.2514 0.0256  -0.0024 0.0004  79  ASP   A OD1 
452  O  OD1 B ASP   A 36  ? 0.6972 0.7890 0.2515 0.0256  -0.0023 0.0005  79  ASP   A OD1 
453  O  OD1 C ASP   A 36  ? 0.6973 0.7887 0.2532 0.0207  -0.0019 -0.0024 79  ASP   A OD1 
454  O  OD1 D ASP   A 36  ? 0.6973 0.7887 0.2532 0.0207  -0.0019 -0.0024 79  ASP   A OD1 
455  O  OD2 A ASP   A 36  ? 0.7022 0.8394 0.2883 0.0159  -0.0160 -0.0025 79  ASP   A OD2 
456  O  OD2 B ASP   A 36  ? 0.7023 0.8395 0.2884 0.0159  -0.0160 -0.0025 79  ASP   A OD2 
457  O  OD2 C ASP   A 36  ? 0.7022 0.8430 0.2938 0.0176  -0.0150 -0.0007 79  ASP   A OD2 
458  O  OD2 D ASP   A 36  ? 0.7023 0.8430 0.2939 0.0177  -0.0150 -0.0007 79  ASP   A OD2 
459  N  N   A GLU   A 37  ? 0.7452 0.8013 0.2197 0.0225  -0.0193 -0.0047 80  GLU   A N   
460  N  N   B GLU   A 37  ? 0.7451 0.8012 0.2196 0.0225  -0.0193 -0.0047 80  GLU   A N   
461  N  N   C GLU   A 37  ? 0.7258 0.7812 0.2000 0.0226  -0.0190 -0.0047 80  GLU   A N   
462  N  N   D GLU   A 37  ? 0.7257 0.7812 0.1999 0.0226  -0.0190 -0.0047 80  GLU   A N   
463  C  CA  A GLU   A 37  ? 0.7615 0.7930 0.2157 0.0101  -0.0115 -0.0137 80  GLU   A CA  
464  C  CA  B GLU   A 37  ? 0.7615 0.7930 0.2157 0.0101  -0.0115 -0.0137 80  GLU   A CA  
465  C  CA  C GLU   A 37  ? 0.7556 0.7863 0.2099 0.0104  -0.0110 -0.0135 80  GLU   A CA  
466  C  CA  D GLU   A 37  ? 0.7555 0.7863 0.2099 0.0104  -0.0110 -0.0135 80  GLU   A CA  
467  C  C   A GLU   A 37  ? 0.7410 0.7706 0.2193 -0.0001 0.0010  -0.0215 80  GLU   A C   
468  C  C   B GLU   A 37  ? 0.7410 0.7706 0.2193 -0.0001 0.0010  -0.0215 80  GLU   A C   
469  C  C   C GLU   A 37  ? 0.7382 0.7674 0.2171 0.0004  0.0014  -0.0210 80  GLU   A C   
470  C  C   D GLU   A 37  ? 0.7382 0.7674 0.2171 0.0004  0.0014  -0.0210 80  GLU   A C   
471  O  O   A GLU   A 37  ? 0.7478 0.7563 0.2161 -0.0056 0.0113  -0.0263 80  GLU   A O   
472  O  O   B GLU   A 37  ? 0.7479 0.7564 0.2162 -0.0056 0.0113  -0.0263 80  GLU   A O   
473  O  O   C GLU   A 37  ? 0.7518 0.7599 0.2223 -0.0038 0.0122  -0.0249 80  GLU   A O   
474  O  O   D GLU   A 37  ? 0.7518 0.7599 0.2223 -0.0038 0.0122  -0.0249 80  GLU   A O   
475  C  CB  A GLU   A 37  ? 0.7901 0.8240 0.2227 0.0009  -0.0212 -0.0204 80  GLU   A CB  
476  C  CB  B GLU   A 37  ? 0.7900 0.8239 0.2226 0.0009  -0.0212 -0.0204 80  GLU   A CB  
477  C  CB  C GLU   A 37  ? 0.7852 0.8180 0.2174 0.0014  -0.0206 -0.0200 80  GLU   A CB  
478  C  CB  D GLU   A 37  ? 0.7852 0.8179 0.2174 0.0014  -0.0206 -0.0200 80  GLU   A CB  
479  C  CG  A GLU   A 37  ? 0.8167 0.8246 0.2214 -0.0092 -0.0130 -0.0281 80  GLU   A CG  
480  C  CG  B GLU   A 37  ? 0.8168 0.8247 0.2215 -0.0091 -0.0130 -0.0281 80  GLU   A CG  
481  C  CG  C GLU   A 37  ? 0.8251 0.8326 0.2314 -0.0094 -0.0121 -0.0284 80  GLU   A CG  
482  C  CG  D GLU   A 37  ? 0.8251 0.8326 0.2314 -0.0094 -0.0121 -0.0284 80  GLU   A CG  
483  C  CD  A GLU   A 37  ? 0.8505 0.8591 0.2272 -0.0166 -0.0229 -0.0340 80  GLU   A CD  
484  C  CD  B GLU   A 37  ? 0.8505 0.8591 0.2273 -0.0166 -0.0229 -0.0340 80  GLU   A CD  
485  C  CD  C GLU   A 37  ? 0.8623 0.8703 0.2398 -0.0162 -0.0223 -0.0336 80  GLU   A CD  
486  C  CD  D GLU   A 37  ? 0.8623 0.8703 0.2398 -0.0161 -0.0223 -0.0336 80  GLU   A CD  
487  O  OE1 A GLU   A 37  ? 0.8535 0.8833 0.2426 -0.0231 -0.0325 -0.0404 80  GLU   A OE1 
488  O  OE1 B GLU   A 37  ? 0.8534 0.8833 0.2427 -0.0231 -0.0325 -0.0404 80  GLU   A OE1 
489  O  OE1 C GLU   A 37  ? 0.8671 0.8814 0.2489 -0.0295 -0.0227 -0.0461 80  GLU   A OE1 
490  O  OE1 D GLU   A 37  ? 0.8671 0.8814 0.2490 -0.0295 -0.0227 -0.0461 80  GLU   A OE1 
491  O  OE2 A GLU   A 37  ? 0.8807 0.8687 0.2228 -0.0162 -0.0212 -0.0319 80  GLU   A OE2 
492  O  OE2 B GLU   A 37  ? 0.8809 0.8689 0.2230 -0.0162 -0.0212 -0.0319 80  GLU   A OE2 
493  O  OE2 C GLU   A 37  ? 0.9010 0.9023 0.2510 -0.0076 -0.0302 -0.0251 80  GLU   A OE2 
494  O  OE2 D GLU   A 37  ? 0.9011 0.9024 0.2511 -0.0076 -0.0302 -0.0251 80  GLU   A OE2 
495  N  N   . SER   A 38  ? 0.7191 0.7701 0.2288 -0.0023 0.0007  -0.0219 81  SER   A N   
496  C  CA  . SER   A 38  ? 0.7057 0.7544 0.2400 -0.0110 0.0124  -0.0275 81  SER   A CA  
497  C  C   . SER   A 38  ? 0.6710 0.7132 0.2167 -0.0002 0.0219  -0.0191 81  SER   A C   
498  O  O   . SER   A 38  ? 0.6579 0.6956 0.2213 -0.0052 0.0318  -0.0219 81  SER   A O   
499  C  CB  . SER   A 38  ? 0.7204 0.7924 0.2810 -0.0195 0.0081  -0.0312 81  SER   A CB  
500  O  OG  . SER   A 38  ? 0.7736 0.8493 0.3196 -0.0301 -0.0017 -0.0407 81  SER   A OG  
501  N  N   . GLY   A 39  ? 0.6489 0.6870 0.1814 0.0138  0.0190  -0.0101 82  GLY   A N   
502  C  CA  . GLY   A 39  ? 0.6642 0.6952 0.2030 0.0245  0.0262  -0.0031 82  GLY   A CA  
503  C  C   . GLY   A 39  ? 0.6508 0.7031 0.2144 0.0325  0.0268  0.0043  82  GLY   A C   
504  O  O   . GLY   A 39  ? 0.6275 0.6751 0.1979 0.0404  0.0339  0.0094  82  GLY   A O   
505  N  N   A ASP   A 40  ? 0.6526 0.7287 0.2297 0.0309  0.0199  0.0054  83  ASP   A N   
506  N  N   B ASP   A 40  ? 0.6526 0.7287 0.2297 0.0309  0.0199  0.0054  83  ASP   A N   
507  N  N   C ASP   A 40  ? 0.6539 0.7299 0.2307 0.0307  0.0197  0.0052  83  ASP   A N   
508  N  N   D ASP   A 40  ? 0.6539 0.7299 0.2307 0.0307  0.0197  0.0052  83  ASP   A N   
509  C  CA  A ASP   A 40  ? 0.6471 0.7475 0.2512 0.0374  0.0219  0.0130  83  ASP   A CA  
510  C  CA  B ASP   A 40  ? 0.6472 0.7475 0.2513 0.0374  0.0219  0.0130  83  ASP   A CA  
511  C  CA  C ASP   A 40  ? 0.6569 0.7580 0.2602 0.0376  0.0210  0.0130  83  ASP   A CA  
512  C  CA  D ASP   A 40  ? 0.6570 0.7580 0.2602 0.0376  0.0210  0.0130  83  ASP   A CA  
513  C  C   A ASP   A 40  ? 0.6465 0.7539 0.2416 0.0561  0.0168  0.0224  83  ASP   A C   
514  C  C   B ASP   A 40  ? 0.6465 0.7539 0.2416 0.0561  0.0168  0.0224  83  ASP   A C   
515  C  C   C ASP   A 40  ? 0.6490 0.7545 0.2418 0.0567  0.0166  0.0224  83  ASP   A C   
516  C  C   D ASP   A 40  ? 0.6490 0.7545 0.2418 0.0567  0.0166  0.0224  83  ASP   A C   
517  O  O   A ASP   A 40  ? 0.6532 0.7663 0.2359 0.0598  0.0059  0.0228  83  ASP   A O   
518  O  O   B ASP   A 40  ? 0.6531 0.7663 0.2358 0.0598  0.0059  0.0228  83  ASP   A O   
519  O  O   C ASP   A 40  ? 0.6465 0.7542 0.2234 0.0612  0.0061  0.0229  83  ASP   A O   
520  O  O   D ASP   A 40  ? 0.6465 0.7541 0.2234 0.0612  0.0061  0.0229  83  ASP   A O   
521  C  CB  A ASP   A 40  ? 0.6531 0.7779 0.2807 0.0251  0.0175  0.0091  83  ASP   A CB  
522  C  CB  B ASP   A 40  ? 0.6532 0.7779 0.2808 0.0251  0.0175  0.0091  83  ASP   A CB  
523  C  CB  C ASP   A 40  ? 0.6704 0.7979 0.2945 0.0273  0.0143  0.0098  83  ASP   A CB  
524  C  CB  D ASP   A 40  ? 0.6704 0.7979 0.2945 0.0273  0.0143  0.0098  83  ASP   A CB  
525  C  CG  A ASP   A 40  ? 0.6532 0.7714 0.2968 0.0087  0.0257  0.0014  83  ASP   A CG  
526  C  CG  B ASP   A 40  ? 0.6533 0.7714 0.2969 0.0087  0.0257  0.0014  83  ASP   A CG  
527  C  CG  C ASP   A 40  ? 0.6800 0.8030 0.3141 0.0077  0.0173  -0.0010 83  ASP   A CG  
528  C  CG  D ASP   A 40  ? 0.6801 0.8030 0.3142 0.0077  0.0173  -0.0010 83  ASP   A CG  
529  O  OD1 A ASP   A 40  ? 0.6499 0.7492 0.2920 0.0096  0.0360  0.0018  83  ASP   A OD1 
530  O  OD1 B ASP   A 40  ? 0.6500 0.7493 0.2921 0.0096  0.0360  0.0018  83  ASP   A OD1 
531  O  OD1 C ASP   A 40  ? 0.6752 0.7920 0.3256 0.0029  0.0284  -0.0011 83  ASP   A OD1 
532  O  OD1 D ASP   A 40  ? 0.6752 0.7921 0.3257 0.0029  0.0284  -0.0011 83  ASP   A OD1 
533  O  OD2 A ASP   A 40  ? 0.6629 0.7945 0.3207 -0.0046 0.0211  -0.0051 83  ASP   A OD2 
534  O  OD2 B ASP   A 40  ? 0.6630 0.7946 0.3208 -0.0046 0.0211  -0.0051 83  ASP   A OD2 
535  O  OD2 C ASP   A 40  ? 0.6914 0.8170 0.3164 -0.0021 0.0082  -0.0094 83  ASP   A OD2 
536  O  OD2 D ASP   A 40  ? 0.6914 0.8170 0.3164 -0.0021 0.0082  -0.0094 83  ASP   A OD2 
537  N  N   . PHE   A 41  ? 0.6341 0.7397 0.2335 0.0683  0.0243  0.0294  84  PHE   A N   
538  C  CA  . PHE   A 41  ? 0.6526 0.7661 0.2472 0.0874  0.0220  0.0380  84  PHE   A CA  
539  C  C   . PHE   A 41  ? 0.6792 0.8286 0.3027 0.0902  0.0209  0.0433  84  PHE   A C   
540  O  O   . PHE   A 41  ? 0.6755 0.8395 0.3253 0.0804  0.0279  0.0436  84  PHE   A O   
541  C  CB  . PHE   A 41  ? 0.6170 0.7164 0.2052 0.0985  0.0310  0.0422  84  PHE   A CB  
542  C  CG  . PHE   A 41  ? 0.6082 0.6757 0.1678 0.1006  0.0300  0.0386  84  PHE   A CG  
543  C  CD1 . PHE   A 41  ? 0.6293 0.6835 0.1652 0.1117  0.0234  0.0401  84  PHE   A CD1 
544  C  CD2 . PHE   A 41  ? 0.6028 0.6533 0.1604 0.0916  0.0359  0.0340  84  PHE   A CD2 
545  C  CE1 . PHE   A 41  ? 0.6377 0.6621 0.1492 0.1119  0.0231  0.0368  84  PHE   A CE1 
546  C  CE2 . PHE   A 41  ? 0.6108 0.6349 0.1457 0.0919  0.0348  0.0304  84  PHE   A CE2 
547  C  CZ  . PHE   A 41  ? 0.6172 0.6282 0.1295 0.1013  0.0288  0.0318  84  PHE   A CZ  
548  N  N   A SER   A 42  ? 0.6980 0.8616 0.3186 0.1030  0.0127  0.0480  85  SER   A N   
549  N  N   B SER   A 42  ? 0.6980 0.8616 0.3186 0.1030  0.0127  0.0480  85  SER   A N   
550  N  N   C SER   A 42  ? 0.6973 0.8606 0.3176 0.1034  0.0129  0.0481  85  SER   A N   
551  N  N   D SER   A 42  ? 0.6973 0.8606 0.3176 0.1034  0.0129  0.0481  85  SER   A N   
552  C  CA  A SER   A 42  ? 0.7051 0.9070 0.3547 0.1083  0.0106  0.0539  85  SER   A CA  
553  C  CA  B SER   A 42  ? 0.7050 0.9070 0.3547 0.1083  0.0106  0.0539  85  SER   A CA  
554  C  CA  C SER   A 42  ? 0.7001 0.9015 0.3491 0.1088  0.0107  0.0540  85  SER   A CA  
555  C  CA  D SER   A 42  ? 0.7001 0.9015 0.3491 0.1088  0.0107  0.0540  85  SER   A CA  
556  C  C   A SER   A 42  ? 0.7221 0.9288 0.3656 0.1323  0.0119  0.0624  85  SER   A C   
557  C  C   B SER   A 42  ? 0.7221 0.9287 0.3656 0.1323  0.0119  0.0624  85  SER   A C   
558  C  C   C SER   A 42  ? 0.7108 0.9164 0.3537 0.1328  0.0124  0.0625  85  SER   A C   
559  C  C   D SER   A 42  ? 0.7108 0.9164 0.3537 0.1328  0.0124  0.0625  85  SER   A C   
560  O  O   A SER   A 42  ? 0.7315 0.9129 0.3450 0.1432  0.0078  0.0623  85  SER   A O   
561  O  O   B SER   A 42  ? 0.7314 0.9128 0.3449 0.1432  0.0078  0.0623  85  SER   A O   
562  O  O   C SER   A 42  ? 0.7146 0.8964 0.3279 0.1438  0.0075  0.0625  85  SER   A O   
563  O  O   D SER   A 42  ? 0.7146 0.8964 0.3279 0.1438  0.0075  0.0625  85  SER   A O   
564  C  CB  A SER   A 42  ? 0.7161 0.9369 0.3725 0.0990  -0.0032 0.0498  85  SER   A CB  
565  C  CB  B SER   A 42  ? 0.7162 0.9370 0.3726 0.0990  -0.0032 0.0498  85  SER   A CB  
566  C  CB  C SER   A 42  ? 0.7200 0.9402 0.3751 0.1003  -0.0033 0.0502  85  SER   A CB  
567  C  CB  D SER   A 42  ? 0.7200 0.9402 0.3752 0.1003  -0.0033 0.0502  85  SER   A CB  
568  O  OG  A SER   A 42  ? 0.7316 0.9348 0.3569 0.1061  -0.0140 0.0489  85  SER   A OG  
569  O  OG  B SER   A 42  ? 0.7316 0.9349 0.3569 0.1061  -0.0141 0.0489  85  SER   A OG  
570  O  OG  C SER   A 42  ? 0.7371 0.9402 0.3614 0.1084  -0.0140 0.0498  85  SER   A OG  
571  O  OG  D SER   A 42  ? 0.7372 0.9402 0.3615 0.1084  -0.0140 0.0498  85  SER   A OG  
572  N  N   A LEU   A 43  ? 0.7307 0.9679 0.4020 0.1400  0.0183  0.0693  86  LEU   A N   
573  N  N   B LEU   A 43  ? 0.7307 0.9679 0.4020 0.1400  0.0184  0.0693  86  LEU   A N   
574  N  N   C LEU   A 43  ? 0.7130 0.9472 0.3828 0.1404  0.0200  0.0694  86  LEU   A N   
575  N  N   D LEU   A 43  ? 0.7129 0.9471 0.3828 0.1404  0.0200  0.0694  86  LEU   A N   
576  C  CA  A LEU   A 43  ? 0.7502 0.9945 0.4189 0.1643  0.0228  0.0772  86  LEU   A CA  
577  C  CA  B LEU   A 43  ? 0.7502 0.9945 0.4188 0.1643  0.0228  0.0772  86  LEU   A CA  
578  C  CA  C LEU   A 43  ? 0.7293 0.9707 0.3959 0.1647  0.0236  0.0771  86  LEU   A CA  
579  C  CA  D LEU   A 43  ? 0.7292 0.9707 0.3959 0.1647  0.0236  0.0771  86  LEU   A CA  
580  C  C   A LEU   A 43  ? 0.7676 1.0283 0.4361 0.1768  0.0099  0.0800  86  LEU   A C   
581  C  C   B LEU   A 43  ? 0.7676 1.0283 0.4360 0.1768  0.0099  0.0800  86  LEU   A C   
582  C  C   C LEU   A 43  ? 0.7261 0.9887 0.3975 0.1747  0.0106  0.0797  86  LEU   A C   
583  C  C   D LEU   A 43  ? 0.7260 0.9886 0.3975 0.1747  0.0106  0.0797  86  LEU   A C   
584  O  O   A LEU   A 43  ? 0.7750 1.0618 0.4633 0.1666  0.0000  0.0786  86  LEU   A O   
585  O  O   B LEU   A 43  ? 0.7751 1.0620 0.4635 0.1666  0.0001  0.0786  86  LEU   A O   
586  O  O   C LEU   A 43  ? 0.7041 1.0036 0.4075 0.1677  0.0065  0.0812  86  LEU   A O   
587  O  O   D LEU   A 43  ? 0.7040 1.0035 0.4074 0.1677  0.0065  0.0812  86  LEU   A O   
588  C  CB  A LEU   A 43  ? 0.7436 1.0174 0.4440 0.1670  0.0362  0.0841  86  LEU   A CB  
589  C  CB  B LEU   A 43  ? 0.7436 1.0173 0.4439 0.1670  0.0362  0.0841  86  LEU   A CB  
590  C  CB  C LEU   A 43  ? 0.7341 1.0013 0.4291 0.1685  0.0380  0.0840  86  LEU   A CB  
591  C  CB  D LEU   A 43  ? 0.7340 1.0012 0.4290 0.1685  0.0380  0.0840  86  LEU   A CB  
592  C  CG  A LEU   A 43  ? 0.7471 1.0016 0.4348 0.1747  0.0510  0.0870  86  LEU   A CG  
593  C  CG  B LEU   A 43  ? 0.7470 1.0016 0.4348 0.1747  0.0510  0.0870  86  LEU   A CG  
594  C  CG  C LEU   A 43  ? 0.7558 1.0045 0.4331 0.1843  0.0506  0.0878  86  LEU   A CG  
595  C  CG  D LEU   A 43  ? 0.7558 1.0044 0.4330 0.1843  0.0506  0.0878  86  LEU   A CG  
596  C  CD1 A LEU   A 43  ? 0.7437 1.0294 0.4633 0.1757  0.0650  0.0951  86  LEU   A CD1 
597  C  CD1 B LEU   A 43  ? 0.7437 1.0294 0.4633 0.1757  0.0650  0.0951  86  LEU   A CD1 
598  C  CD1 C LEU   A 43  ? 0.7633 1.0450 0.4666 0.1961  0.0627  0.0968  86  LEU   A CD1 
599  C  CD1 D LEU   A 43  ? 0.7633 1.0450 0.4666 0.1961  0.0627  0.0968  86  LEU   A CD1 
600  C  CD2 A LEU   A 43  ? 0.7642 0.9965 0.4209 0.1974  0.0510  0.0880  86  LEU   A CD2 
601  C  CD2 B LEU   A 43  ? 0.7643 0.9965 0.4209 0.1974  0.0510  0.0880  86  LEU   A CD2 
602  C  CD2 C LEU   A 43  ? 0.7778 0.9972 0.4191 0.2017  0.0449  0.0859  86  LEU   A CD2 
603  C  CD2 D LEU   A 43  ? 0.7777 0.9971 0.4191 0.2017  0.0449  0.0859  86  LEU   A CD2 
604  N  N   A VAL   A 44  ? 0.7914 1.0369 0.4383 0.1988  0.0099  0.0837  87  VAL   A N   
605  N  N   B VAL   A 44  ? 0.7914 1.0369 0.4383 0.1988  0.0099  0.0837  87  VAL   A N   
606  N  N   C VAL   A 44  ? 0.7433 0.9834 0.3853 0.1906  0.0044  0.0807  87  VAL   A N   
607  N  N   D VAL   A 44  ? 0.7433 0.9833 0.3852 0.1906  0.0044  0.0807  87  VAL   A N   
608  C  CA  A VAL   A 44  ? 0.8121 1.0738 0.4605 0.2181  0.0006  0.0891  87  VAL   A CA  
609  C  CA  B VAL   A 44  ? 0.8121 1.0738 0.4604 0.2181  0.0006  0.0891  87  VAL   A CA  
610  C  CA  C VAL   A 44  ? 0.7784 1.0346 0.4209 0.2055  -0.0078 0.0852  87  VAL   A CA  
611  C  CA  D VAL   A 44  ? 0.7784 1.0346 0.4209 0.2055  -0.0078 0.0852  87  VAL   A CA  
612  C  C   A VAL   A 44  ? 0.8231 1.0932 0.4770 0.2415  0.0127  0.0955  87  VAL   A C   
613  C  C   B VAL   A 44  ? 0.8231 1.0932 0.4771 0.2415  0.0127  0.0955  87  VAL   A C   
614  C  C   C VAL   A 44  ? 0.7919 1.0783 0.4580 0.2260  -0.0001 0.0932  87  VAL   A C   
615  C  C   D VAL   A 44  ? 0.7918 1.0783 0.4580 0.2260  -0.0001 0.0932  87  VAL   A C   
616  O  O   A VAL   A 44  ? 0.8199 1.0637 0.4554 0.2453  0.0238  0.0939  87  VAL   A O   
617  O  O   B VAL   A 44  ? 0.8199 1.0637 0.4554 0.2453  0.0238  0.0939  87  VAL   A O   
618  O  O   C VAL   A 44  ? 0.7921 1.1174 0.4859 0.2299  -0.0073 0.0973  87  VAL   A O   
619  O  O   D VAL   A 44  ? 0.7921 1.1173 0.4858 0.2300  -0.0073 0.0973  87  VAL   A O   
620  C  CB  A VAL   A 44  ? 0.8340 1.0602 0.4443 0.2229  -0.0110 0.0869  87  VAL   A CB  
621  C  CB  B VAL   A 44  ? 0.8340 1.0602 0.4443 0.2229  -0.0110 0.0869  87  VAL   A CB  
622  C  CB  C VAL   A 44  ? 0.7970 1.0132 0.3980 0.2159  -0.0152 0.0844  87  VAL   A CB  
623  C  CB  D VAL   A 44  ? 0.7970 1.0132 0.3980 0.2159  -0.0152 0.0844  87  VAL   A CB  
624  C  CG1 A VAL   A 44  ? 0.8559 1.0967 0.4666 0.2434  -0.0214 0.0936  87  VAL   A CG1 
625  C  CG1 B VAL   A 44  ? 0.8560 1.0967 0.4666 0.2434  -0.0214 0.0936  87  VAL   A CG1 
626  C  CG1 C VAL   A 44  ? 0.8243 1.0545 0.4242 0.2331  -0.0278 0.0905  87  VAL   A CG1 
627  C  CG1 D VAL   A 44  ? 0.8243 1.0545 0.4242 0.2331  -0.0278 0.0905  87  VAL   A CG1 
628  C  CG2 A VAL   A 44  ? 0.8257 1.0399 0.4260 0.1995  -0.0196 0.0800  87  VAL   A CG2 
629  C  CG2 B VAL   A 44  ? 0.8256 1.0397 0.4258 0.1995  -0.0196 0.0800  87  VAL   A CG2 
630  C  CG2 C VAL   A 44  ? 0.7869 0.9741 0.3650 0.1957  -0.0201 0.0770  87  VAL   A CG2 
631  C  CG2 D VAL   A 44  ? 0.7868 0.9740 0.3650 0.1957  -0.0201 0.0770  87  VAL   A CG2 
632  N  N   A GLU   A 45  ? 0.8285 1.1357 0.5078 0.2564  0.0108  0.1021  88  GLU   A N   
633  N  N   B GLU   A 45  ? 0.8285 1.1357 0.5078 0.2564  0.0108  0.1021  88  GLU   A N   
634  N  N   C GLU   A 45  ? 0.7895 1.0593 0.4445 0.2387  0.0136  0.0950  88  GLU   A N   
635  N  N   D GLU   A 45  ? 0.7895 1.0594 0.4445 0.2387  0.0136  0.0950  88  GLU   A N   
636  C  CA  A GLU   A 45  ? 0.8379 1.1587 0.5258 0.2807  0.0234  0.1083  88  GLU   A CA  
637  C  CA  B GLU   A 45  ? 0.8379 1.1587 0.5258 0.2807  0.0234  0.1083  88  GLU   A CA  
638  C  CA  C GLU   A 45  ? 0.7985 1.0944 0.4739 0.2575  0.0260  0.1019  88  GLU   A CA  
639  C  CA  D GLU   A 45  ? 0.7985 1.0945 0.4739 0.2575  0.0260  0.1019  88  GLU   A CA  
640  C  C   A GLU   A 45  ? 0.8545 1.1876 0.5431 0.3042  0.0139  0.1134  88  GLU   A C   
641  C  C   B GLU   A 45  ? 0.8544 1.1875 0.5431 0.3042  0.0139  0.1134  88  GLU   A C   
642  C  C   C GLU   A 45  ? 0.7964 1.0700 0.4574 0.2591  0.0421  0.1009  88  GLU   A C   
643  C  C   D GLU   A 45  ? 0.7964 1.0700 0.4574 0.2591  0.0421  0.1009  88  GLU   A C   
644  O  O   A GLU   A 45  ? 0.8637 1.1814 0.5357 0.3283  0.0201  0.1158  88  GLU   A O   
645  O  O   B GLU   A 45  ? 0.8635 1.1812 0.5354 0.3283  0.0201  0.1158  88  GLU   A O   
646  O  O   C GLU   A 45  ? 0.7952 1.0919 0.4810 0.2528  0.0540  0.1042  88  GLU   A O   
647  O  O   D GLU   A 45  ? 0.7952 1.0919 0.4810 0.2528  0.0540  0.1042  88  GLU   A O   
648  C  CB  A GLU   A 45  ? 0.8222 1.1865 0.5525 0.2744  0.0359  0.1128  88  GLU   A CB  
649  C  CB  B GLU   A 45  ? 0.8222 1.1865 0.5525 0.2744  0.0360  0.1128  88  GLU   A CB  
650  C  CB  C GLU   A 45  ? 0.8320 1.1268 0.4965 0.2853  0.0219  0.1063  88  GLU   A CB  
651  C  CB  D GLU   A 45  ? 0.8321 1.1269 0.4965 0.2853  0.0219  0.1063  88  GLU   A CB  
652  C  CG  A GLU   A 45  ? 0.8083 1.1574 0.5354 0.2577  0.0489  0.1103  88  GLU   A CG  
653  C  CG  B GLU   A 45  ? 0.8083 1.1574 0.5354 0.2577  0.0489  0.1103  88  GLU   A CG  
654  C  CG  C GLU   A 45  ? 0.8452 1.1701 0.5283 0.2891  0.0065  0.1099  88  GLU   A CG  
655  C  CG  D GLU   A 45  ? 0.8452 1.1702 0.5284 0.2892  0.0065  0.1099  88  GLU   A CG  
656  C  CD  A GLU   A 45  ? 0.8218 1.1443 0.5231 0.2731  0.0636  0.1111  88  GLU   A CD  
657  C  CD  B GLU   A 45  ? 0.8219 1.1444 0.5232 0.2731  0.0636  0.1111  88  GLU   A CD  
658  C  CD  C GLU   A 45  ? 0.8749 1.1684 0.5244 0.2952  -0.0089 0.1088  88  GLU   A CD  
659  C  CD  D GLU   A 45  ? 0.8750 1.1685 0.5245 0.2952  -0.0089 0.1088  88  GLU   A CD  
660  O  OE1 A GLU   A 45  ? 0.8423 1.1694 0.5388 0.2976  0.0687  0.1147  88  GLU   A OE1 
661  O  OE1 B GLU   A 45  ? 0.8425 1.1696 0.5390 0.2977  0.0687  0.1147  88  GLU   A OE1 
662  O  OE1 C GLU   A 45  ? 0.9131 1.1611 0.5253 0.3027  -0.0059 0.1062  88  GLU   A OE1 
663  O  OE1 D GLU   A 45  ? 0.9132 1.1613 0.5255 0.3027  -0.0059 0.1062  88  GLU   A OE1 
664  O  OE2 A GLU   A 45  ? 0.8127 1.1104 0.4986 0.2612  0.0697  0.1078  88  GLU   A OE2 
665  O  OE2 B GLU   A 45  ? 0.8128 1.1104 0.4987 0.2612  0.0697  0.1078  88  GLU   A OE2 
666  O  OE2 C GLU   A 45  ? 0.8630 1.1774 0.5232 0.2922  -0.0239 0.1107  88  GLU   A OE2 
667  O  OE2 D GLU   A 45  ? 0.8630 1.1774 0.5232 0.2922  -0.0239 0.1107  88  GLU   A OE2 
668  N  N   . GLY   B 7   ? 0.8617 0.8842 0.6117 0.0943  0.0734  -0.0260 16  GLY   B N   
669  C  CA  . GLY   B 7   ? 0.8754 0.8918 0.6235 0.1026  0.0729  -0.0170 16  GLY   B CA  
670  C  C   . GLY   B 7   ? 0.8692 0.8839 0.6029 0.1067  0.0684  -0.0122 16  GLY   B C   
671  O  O   . GLY   B 7   ? 0.8791 0.8959 0.6096 0.1072  0.0650  -0.0149 16  GLY   B O   
672  N  N   . GLU   B 8   ? 0.8413 0.8526 0.5666 0.1094  0.0683  -0.0057 17  GLU   B N   
673  C  CA  . GLU   B 8   ? 0.8086 0.8178 0.5204 0.1151  0.0640  -0.0005 17  GLU   B CA  
674  C  C   . GLU   B 8   ? 0.7997 0.8093 0.4999 0.1102  0.0611  -0.0032 17  GLU   B C   
675  O  O   . GLU   B 8   ? 0.8088 0.8182 0.5067 0.1060  0.0631  -0.0029 17  GLU   B O   
676  C  CB  . GLU   B 8   ? 0.8002 0.8070 0.5100 0.1214  0.0655  0.0079  17  GLU   B CB  
677  C  CG  . GLU   B 8   ? 0.8100 0.8160 0.5111 0.1300  0.0616  0.0131  17  GLU   B CG  
678  C  CD  . GLU   B 8   ? 0.7917 0.7974 0.4915 0.1367  0.0632  0.0221  17  GLU   B CD  
679  O  OE1 . GLU   B 8   ? 0.7446 0.7501 0.4496 0.1342  0.0672  0.0248  17  GLU   B OE1 
680  O  OE2 . GLU   B 8   ? 0.8565 0.8629 0.5503 0.1444  0.0603  0.0266  17  GLU   B OE2 
681  N  N   A THR   B 9   ? 0.7923 0.8023 0.4857 0.1102  0.0563  -0.0057 18  THR   B N   
682  N  N   B THR   B 9   ? 0.7831 0.7932 0.4766 0.1104  0.0563  -0.0056 18  THR   B N   
683  N  N   C THR   B 9   ? 0.7923 0.8023 0.4857 0.1102  0.0563  -0.0057 18  THR   B N   
684  N  N   D THR   B 9   ? 0.7831 0.7932 0.4766 0.1104  0.0563  -0.0056 18  THR   B N   
685  C  CA  A THR   B 9   ? 0.7868 0.7966 0.4696 0.1054  0.0523  -0.0081 18  THR   B CA  
686  C  CA  B THR   B 9   ? 0.7728 0.7827 0.4559 0.1054  0.0523  -0.0083 18  THR   B CA  
687  C  CA  C THR   B 9   ? 0.7868 0.7966 0.4696 0.1054  0.0523  -0.0081 18  THR   B CA  
688  C  CA  D THR   B 9   ? 0.7728 0.7827 0.4559 0.1054  0.0523  -0.0083 18  THR   B CA  
689  C  C   A THR   B 9   ? 0.7632 0.7694 0.4339 0.1121  0.0467  -0.0045 18  THR   B C   
690  C  C   B THR   B 9   ? 0.7551 0.7612 0.4257 0.1121  0.0468  -0.0045 18  THR   B C   
691  C  C   C THR   B 9   ? 0.7632 0.7694 0.4339 0.1121  0.0467  -0.0045 18  THR   B C   
692  C  C   D THR   B 9   ? 0.7551 0.7612 0.4257 0.1121  0.0468  -0.0045 18  THR   B C   
693  O  O   A THR   B 9   ? 0.7572 0.7622 0.4194 0.1090  0.0419  -0.0067 18  THR   B O   
694  O  O   B THR   B 9   ? 0.7508 0.7557 0.4126 0.1090  0.0422  -0.0063 18  THR   B O   
695  O  O   C THR   B 9   ? 0.7572 0.7622 0.4194 0.1090  0.0419  -0.0067 18  THR   B O   
696  O  O   D THR   B 9   ? 0.7508 0.7557 0.4126 0.1090  0.0422  -0.0063 18  THR   B O   
697  C  CB  A THR   B 9   ? 0.8005 0.8149 0.4871 0.0977  0.0512  -0.0151 18  THR   B CB  
698  C  CB  B THR   B 9   ? 0.7769 0.7913 0.4639 0.0985  0.0508  -0.0151 18  THR   B CB  
699  C  CB  C THR   B 9   ? 0.8005 0.8149 0.4871 0.0977  0.0512  -0.0151 18  THR   B CB  
700  C  CB  D THR   B 9   ? 0.7769 0.7913 0.4639 0.0985  0.0508  -0.0151 18  THR   B CB  
701  O  OG1 A THR   B 9   ? 0.8137 0.8321 0.5125 0.0931  0.0566  -0.0188 18  THR   B OG1 
702  O  OG1 B THR   B 9   ? 0.7697 0.7849 0.4601 0.1034  0.0490  -0.0153 18  THR   B OG1 
703  O  OG1 C THR   B 9   ? 0.8137 0.8321 0.5125 0.0931  0.0566  -0.0188 18  THR   B OG1 
704  O  OG1 D THR   B 9   ? 0.7697 0.7849 0.4601 0.1034  0.0490  -0.0153 18  THR   B OG1 
705  C  CG2 A THR   B 9   ? 0.8007 0.8153 0.4782 0.0911  0.0475  -0.0171 18  THR   B CG2 
706  C  CG2 B THR   B 9   ? 0.7776 0.7969 0.4754 0.0913  0.0558  -0.0201 18  THR   B CG2 
707  C  CG2 C THR   B 9   ? 0.8007 0.8153 0.4782 0.0911  0.0475  -0.0171 18  THR   B CG2 
708  C  CG2 D THR   B 9   ? 0.7776 0.7969 0.4754 0.0913  0.0558  -0.0201 18  THR   B CG2 
709  N  N   . THR   B 10  ? 0.7536 0.7584 0.4238 0.1209  0.0469  0.0006  19  THR   B N   
710  C  CA  . THR   B 10  ? 0.7173 0.7197 0.3763 0.1284  0.0418  0.0039  19  THR   B CA  
711  C  C   . THR   B 10  ? 0.6652 0.6651 0.3137 0.1289  0.0404  0.0059  19  THR   B C   
712  O  O   . THR   B 10  ? 0.6972 0.6978 0.3485 0.1281  0.0449  0.0088  19  THR   B O   
713  C  CB  . THR   B 10  ? 0.7137 0.7168 0.3747 0.1379  0.0431  0.0098  19  THR   B CB  
714  O  OG1 . THR   B 10  ? 0.7213 0.7264 0.3950 0.1372  0.0464  0.0091  19  THR   B OG1 
715  C  CG2 . THR   B 10  ? 0.7477 0.7500 0.3995 0.1449  0.0373  0.0108  19  THR   B CG2 
716  N  N   . ASP   B 11  ? 0.6578 0.6550 0.2952 0.1311  0.0341  0.0050  20  ASP   B N   
717  C  CA  . ASP   B 11  ? 0.6479 0.6424 0.2742 0.1338  0.0315  0.0070  20  ASP   B CA  
718  C  C   . ASP   B 11  ? 0.6808 0.6774 0.3061 0.1422  0.0347  0.0133  20  ASP   B C   
719  O  O   . ASP   B 11  ? 0.6426 0.6415 0.2719 0.1481  0.0358  0.0162  20  ASP   B O   
720  C  CB  . ASP   B 11  ? 0.6794 0.6702 0.2951 0.1359  0.0234  0.0044  20  ASP   B CB  
721  C  CG  . ASP   B 11  ? 0.7079 0.6960 0.3213 0.1274  0.0188  -0.0004 20  ASP   B CG  
722  O  OD1 . ASP   B 11  ? 0.6723 0.6628 0.2931 0.1184  0.0220  -0.0029 20  ASP   B OD1 
723  O  OD2 . ASP   B 11  ? 0.7475 0.7314 0.3517 0.1300  0.0116  -0.0017 20  ASP   B OD2 
724  N  N   . GLY   B 12  ? 0.6484 0.6452 0.2695 0.1427  0.0363  0.0159  21  GLY   B N   
725  C  CA  . GLY   B 12  ? 0.6148 0.6150 0.2351 0.1501  0.0395  0.0224  21  GLY   B CA  
726  C  C   . GLY   B 12  ? 0.6116 0.6133 0.2337 0.1464  0.0440  0.0246  21  GLY   B C   
727  O  O   . GLY   B 12  ? 0.5800 0.5795 0.2026 0.1382  0.0440  0.0206  21  GLY   B O   
728  N  N   . VAL   B 13  ? 0.5808 0.5865 0.2029 0.1522  0.0472  0.0310  22  VAL   B N   
729  C  CA  . VAL   B 13  ? 0.5744 0.5827 0.1982 0.1498  0.0516  0.0344  22  VAL   B CA  
730  C  C   . VAL   B 13  ? 0.5830 0.5934 0.2201 0.1470  0.0578  0.0378  22  VAL   B C   
731  O  O   . VAL   B 13  ? 0.5691 0.5808 0.2112 0.1511  0.0585  0.0407  22  VAL   B O   
732  C  CB  . VAL   B 13  ? 0.5606 0.5727 0.1748 0.1573  0.0506  0.0389  22  VAL   B CB  
733  C  CG1 . VAL   B 13  ? 0.5427 0.5602 0.1573 0.1663  0.0517  0.0454  22  VAL   B CG1 
734  C  CG2 . VAL   B 13  ? 0.5366 0.5515 0.1518 0.1542  0.0545  0.0417  22  VAL   B CG2 
735  N  N   . TYR   B 14  ? 0.5566 0.5667 0.2003 0.1391  0.0616  0.0364  23  TYR   B N   
736  C  CA  . TYR   B 14  ? 0.5581 0.5692 0.2157 0.1355  0.0671  0.0386  23  TYR   B CA  
737  C  C   . TYR   B 14  ? 0.5701 0.5843 0.2304 0.1339  0.0713  0.0435  23  TYR   B C   
738  O  O   . TYR   B 14  ? 0.5805 0.5952 0.2349 0.1308  0.0710  0.0419  23  TYR   B O   
739  C  CB  . TYR   B 14  ? 0.5620 0.5703 0.2274 0.1266  0.0679  0.0311  23  TYR   B CB  
740  C  CG  . TYR   B 14  ? 0.5597 0.5660 0.2261 0.1277  0.0648  0.0270  23  TYR   B CG  
741  C  CD1 . TYR   B 14  ? 0.5746 0.5793 0.2305 0.1292  0.0593  0.0237  23  TYR   B CD1 
742  C  CD2 . TYR   B 14  ? 0.5677 0.5739 0.2462 0.1265  0.0671  0.0259  23  TYR   B CD2 
743  C  CE1 . TYR   B 14  ? 0.5920 0.5955 0.2490 0.1300  0.0563  0.0202  23  TYR   B CE1 
744  C  CE2 . TYR   B 14  ? 0.5754 0.5807 0.2552 0.1276  0.0643  0.0222  23  TYR   B CE2 
745  C  CZ  . TYR   B 14  ? 0.5881 0.5924 0.2571 0.1291  0.0590  0.0194  23  TYR   B CZ  
746  O  OH  . TYR   B 14  ? 0.6159 0.6198 0.2863 0.1295  0.0561  0.0157  23  TYR   B OH  
747  N  N   . ARG   B 15  ? 0.5745 0.5902 0.2457 0.1342  0.0754  0.0485  24  ARG   B N   
748  C  CA  . ARG   B 15  ? 0.5887 0.6065 0.2667 0.1298  0.0799  0.0519  24  ARG   B CA  
749  C  C   . ARG   B 15  ? 0.5934 0.6082 0.2808 0.1201  0.0822  0.0450  24  ARG   B C   
750  O  O   . ARG   B 15  ? 0.5872 0.5992 0.2816 0.1179  0.0819  0.0402  24  ARG   B O   
751  C  CB  . ARG   B 15  ? 0.6153 0.6354 0.3027 0.1331  0.0830  0.0602  24  ARG   B CB  
752  C  CG  . ARG   B 15  ? 0.6266 0.6519 0.3061 0.1427  0.0814  0.0681  24  ARG   B CG  
753  C  CD  . ARG   B 15  ? 0.6540 0.6816 0.3438 0.1453  0.0841  0.0767  24  ARG   B CD  
754  N  NE  . ARG   B 15  ? 0.6658 0.6982 0.3475 0.1547  0.0815  0.0821  24  ARG   B NE  
755  C  CZ  . ARG   B 15  ? 0.6871 0.7274 0.3608 0.1605  0.0816  0.0890  24  ARG   B CZ  
756  N  NH1 . ARG   B 15  ? 0.6791 0.7232 0.3523 0.1578  0.0842  0.0921  24  ARG   B NH1 
757  N  NH2 . ARG   B 15  ? 0.6903 0.7353 0.3569 0.1692  0.0791  0.0930  24  ARG   B NH2 
758  N  N   . VAL   B 16  ? 0.5852 0.6017 0.2730 0.1148  0.0846  0.0448  25  VAL   B N   
759  C  CA  . VAL   B 16  ? 0.6071 0.6224 0.3051 0.1057  0.0876  0.0395  25  VAL   B CA  
760  C  C   . VAL   B 16  ? 0.6009 0.6176 0.3093 0.1047  0.0918  0.0455  25  VAL   B C   
761  O  O   . VAL   B 16  ? 0.6143 0.6347 0.3183 0.1059  0.0928  0.0511  25  VAL   B O   
762  C  CB  . VAL   B 16  ? 0.5965 0.6129 0.2864 0.1003  0.0866  0.0348  25  VAL   B CB  
763  C  CG1 . VAL   B 16  ? 0.5897 0.6059 0.2891 0.0910  0.0892  0.0280  25  VAL   B CG1 
764  C  CG2 . VAL   B 16  ? 0.6004 0.6154 0.2782 0.1029  0.0816  0.0314  25  VAL   B CG2 
765  N  N   . MET   B 17  ? 0.6144 0.6285 0.3367 0.1018  0.0938  0.0436  26  MET   B N   
766  C  CA  . MET   B 17  ? 0.6402 0.6540 0.3751 0.1009  0.0970  0.0494  26  MET   B CA  
767  C  C   . MET   B 17  ? 0.6555 0.6677 0.4013 0.0921  0.0995  0.0426  26  MET   B C   
768  O  O   . MET   B 17  ? 0.6246 0.6355 0.3710 0.0880  0.0988  0.0333  26  MET   B O   
769  C  CB  . MET   B 17  ? 0.6489 0.6599 0.3919 0.1059  0.0964  0.0527  26  MET   B CB  
770  C  CG  . MET   B 17  ? 0.6730 0.6860 0.4053 0.1148  0.0935  0.0582  26  MET   B CG  
771  S  SD  . MET   B 17  ? 0.6666 0.6864 0.3895 0.1203  0.0940  0.0695  26  MET   B SD  
772  C  CE  . MET   B 17  ? 0.6867 0.7065 0.4258 0.1195  0.0972  0.0787  26  MET   B CE  
773  N  N   . THR   B 18  ? 0.6704 0.6831 0.4248 0.0894  0.1023  0.0473  27  THR   B N   
774  C  CA  . THR   B 18  ? 0.6937 0.7046 0.4608 0.0816  0.1046  0.0413  27  THR   B CA  
775  C  C   . THR   B 18  ? 0.7318 0.7395 0.5135 0.0823  0.1060  0.0474  27  THR   B C   
776  O  O   . THR   B 18  ? 0.6929 0.7024 0.4730 0.0873  0.1061  0.0584  27  THR   B O   
777  C  CB  . THR   B 18  ? 0.6938 0.7085 0.4567 0.0754  0.1062  0.0391  27  THR   B CB  
778  O  OG1 . THR   B 18  ? 0.6648 0.6775 0.4409 0.0684  0.1080  0.0322  27  THR   B OG1 
779  C  CG2 . THR   B 18  ? 0.6897 0.7082 0.4493 0.0772  0.1074  0.0491  27  THR   B CG2 
780  N  N   . ARG   B 19  ? 0.7553 0.7591 0.5510 0.0776  0.1069  0.0406  28  ARG   B N   
781  C  CA  . ARG   B 19  ? 0.8466 0.8461 0.6582 0.0770  0.1079  0.0453  28  ARG   B CA  
782  C  C   . ARG   B 19  ? 0.8611 0.8612 0.6801 0.0693  0.1101  0.0430  28  ARG   B C   
783  O  O   . ARG   B 19  ? 0.8587 0.8548 0.6919 0.0677  0.1105  0.0461  28  ARG   B O   
784  C  CB  . ARG   B 19  ? 0.8948 0.8887 0.7178 0.0786  0.1066  0.0401  28  ARG   B CB  
785  C  CG  . ARG   B 19  ? 0.9615 0.9553 0.7780 0.0866  0.1044  0.0443  28  ARG   B CG  
786  C  CD  . ARG   B 19  ? 1.0360 1.0246 0.8654 0.0908  0.1033  0.0494  28  ARG   B CD  
787  N  NE  . ARG   B 19  ? 1.1154 1.1043 0.9384 0.0979  0.1011  0.0514  28  ARG   B NE  
788  C  CZ  . ARG   B 19  ? 1.1618 1.1500 0.9837 0.0988  0.0997  0.0423  28  ARG   B CZ  
789  N  NH1 . ARG   B 19  ? 1.1538 1.1416 0.9802 0.0931  0.1005  0.0305  28  ARG   B NH1 
790  N  NH2 . ARG   B 19  ? 1.1724 1.1613 0.9887 0.1054  0.0975  0.0451  28  ARG   B NH2 
791  N  N   . ARG   B 20  ? 0.9073 0.9123 0.7167 0.0650  0.1110  0.0390  29  ARG   B N   
792  C  CA  . ARG   B 20  ? 0.9926 0.9993 0.8075 0.0571  0.1130  0.0350  29  ARG   B CA  
793  C  C   . ARG   B 20  ? 0.9938 1.0027 0.8101 0.0570  0.1142  0.0463  29  ARG   B C   
794  O  O   . ARG   B 20  ? 1.0044 1.0129 0.8303 0.0509  0.1156  0.0450  29  ARG   B O   
795  C  CB  . ARG   B 20  ? 1.0750 1.0869 0.8780 0.0532  0.1132  0.0272  29  ARG   B CB  
796  C  CG  . ARG   B 20  ? 1.1592 1.1726 0.9695 0.0446  0.1148  0.0180  29  ARG   B CG  
797  C  CD  . ARG   B 20  ? 1.2106 1.2303 1.0084 0.0406  0.1149  0.0125  29  ARG   B CD  
798  N  NE  . ARG   B 20  ? 1.2378 1.2613 1.0238 0.0426  0.1149  0.0213  29  ARG   B NE  
799  C  CZ  . ARG   B 20  ? 1.2548 1.2814 1.0423 0.0393  0.1166  0.0257  29  ARG   B CZ  
800  N  NH1 . ARG   B 20  ? 1.2730 1.2987 1.0734 0.0333  0.1182  0.0222  29  ARG   B NH1 
801  N  NH2 . ARG   B 20  ? 1.2412 1.2720 1.0175 0.0421  0.1164  0.0333  29  ARG   B NH2 
802  N  N   . LEU   B 21  ? 0.9628 0.9747 0.7700 0.0633  0.1137  0.0568  30  LEU   B N   
803  C  CA  . LEU   B 21  ? 0.9395 0.9553 0.7475 0.0642  0.1148  0.0690  30  LEU   B CA  
804  C  C   . LEU   B 21  ? 0.8980 0.9097 0.7173 0.0680  0.1141  0.0778  30  LEU   B C   
805  O  O   . LEU   B 21  ? 0.9185 0.9236 0.7465 0.0689  0.1128  0.0729  30  LEU   B O   
806  C  CB  . LEU   B 21  ? 0.9612 0.9843 0.7517 0.0693  0.1144  0.0743  30  LEU   B CB  
807  C  CG  . LEU   B 21  ? 0.9868 1.0152 0.7677 0.0651  0.1153  0.0702  30  LEU   B CG  
808  C  CD1 . LEU   B 21  ? 0.9913 1.0170 0.7768 0.0575  0.1158  0.0577  30  LEU   B CD1 
809  C  CD2 . LEU   B 21  ? 0.9886 1.0213 0.7519 0.0711  0.1137  0.0710  30  LEU   B CD2 
810  N  N   . LEU   B 22  ? 0.8669 0.8830 0.6866 0.0701  0.1147  0.0904  31  LEU   B N   
811  C  CA  . LEU   B 22  ? 0.8354 0.8492 0.6647 0.0741  0.1138  0.1009  31  LEU   B CA  
812  C  C   . LEU   B 22  ? 0.8219 0.8347 0.6439 0.0821  0.1118  0.1011  31  LEU   B C   
813  O  O   . LEU   B 22  ? 0.8152 0.8331 0.6213 0.0861  0.1115  0.0994  31  LEU   B O   
814  C  CB  . LEU   B 22  ? 0.8408 0.8627 0.6678 0.0752  0.1149  0.1148  31  LEU   B CB  
815  C  CG  . LEU   B 22  ? 0.8178 0.8388 0.6558 0.0778  0.1140  0.1273  31  LEU   B CG  
816  C  CD1 . LEU   B 22  ? 0.8002 0.8129 0.6578 0.0710  0.1137  0.1266  31  LEU   B CD1 
817  C  CD2 . LEU   B 22  ? 0.8292 0.8617 0.6601 0.0808  0.1151  0.1411  31  LEU   B CD2 
818  N  N   . GLY   B 23  ? 0.7886 0.7950 0.6218 0.0843  0.1103  0.1030  32  GLY   B N   
819  C  CA  . GLY   B 23  ? 0.7874 0.7929 0.6154 0.0918  0.1083  0.1034  32  GLY   B CA  
820  C  C   . GLY   B 23  ? 0.7709 0.7766 0.5863 0.0929  0.1077  0.0918  32  GLY   B C   
821  O  O   . GLY   B 23  ? 0.7736 0.7769 0.5906 0.0871  0.1084  0.0809  32  GLY   B O   
822  N  N   . SER   B 24  ? 0.7524 0.7615 0.5559 0.1001  0.1061  0.0942  33  SER   B N   
823  C  CA  . SER   B 24  ? 0.7516 0.7613 0.5419 0.1017  0.1048  0.0848  33  SER   B CA  
824  C  C   . SER   B 24  ? 0.7303 0.7478 0.5048 0.1041  0.1050  0.0886  33  SER   B C   
825  O  O   . SER   B 24  ? 0.6980 0.7207 0.4675 0.1103  0.1045  0.0985  33  SER   B O   
826  C  CB  . SER   B 24  ? 0.7634 0.7711 0.5519 0.1082  0.1024  0.0843  33  SER   B CB  
827  O  OG  . SER   B 24  ? 0.7896 0.7902 0.5927 0.1062  0.1020  0.0797  33  SER   B OG  
828  N  N   . THR   B 25  ? 0.6761 0.6950 0.4435 0.0997  0.1056  0.0814  34  THR   B N   
829  C  CA  . THR   B 25  ? 0.6848 0.7109 0.4386 0.1014  0.1058  0.0849  34  THR   B CA  
830  C  C   . THR   B 25  ? 0.6699 0.6961 0.4092 0.1042  0.1032  0.0778  34  THR   B C   
831  O  O   . THR   B 25  ? 0.6541 0.6759 0.3945 0.0996  0.1025  0.0675  34  THR   B O   
832  C  CB  . THR   B 25  ? 0.7031 0.7312 0.4599 0.0941  0.1082  0.0837  34  THR   B CB  
833  O  OG1 . THR   B 25  ? 0.7248 0.7516 0.4964 0.0908  0.1101  0.0896  34  THR   B OG1 
834  C  CG2 . THR   B 25  ? 0.7125 0.7488 0.4565 0.0966  0.1085  0.0886  34  THR   B CG2 
835  N  N   . GLN   B 26  ? 0.6338 0.6656 0.3601 0.1107  0.1018  0.0827  35  GLN   B N   
836  C  CA  . GLN   B 26  ? 0.6360 0.6676 0.3482 0.1134  0.0986  0.0764  35  GLN   B CA  
837  C  C   . GLN   B 26  ? 0.6302 0.6643 0.3357 0.1088  0.0992  0.0730  35  GLN   B C   
838  O  O   . GLN   B 26  ? 0.6185 0.6588 0.3203 0.1105  0.1004  0.0793  35  GLN   B O   
839  C  CB  . GLN   B 26  ? 0.6352 0.6707 0.3366 0.1231  0.0960  0.0815  35  GLN   B CB  
840  C  CG  . GLN   B 26  ? 0.6239 0.6575 0.3123 0.1257  0.0920  0.0744  35  GLN   B CG  
841  C  CD  . GLN   B 26  ? 0.6341 0.6712 0.3125 0.1356  0.0891  0.0787  35  GLN   B CD  
842  O  OE1 . GLN   B 26  ? 0.6233 0.6606 0.3063 0.1399  0.0889  0.0829  35  GLN   B OE1 
843  N  NE2 . GLN   B 26  ? 0.6231 0.6627 0.2880 0.1392  0.0863  0.0768  35  GLN   B NE2 
844  N  N   . VAL   B 27  ? 0.6104 0.6407 0.3146 0.1033  0.0981  0.0634  36  VAL   B N   
845  C  CA  . VAL   B 27  ? 0.6031 0.6353 0.3011 0.0982  0.0982  0.0593  36  VAL   B CA  
846  C  C   . VAL   B 27  ? 0.5725 0.6047 0.2556 0.1026  0.0940  0.0564  36  VAL   B C   
847  O  O   . VAL   B 27  ? 0.5764 0.6116 0.2512 0.1020  0.0932  0.0562  36  VAL   B O   
848  C  CB  . VAL   B 27  ? 0.6101 0.6392 0.3174 0.0886  0.0999  0.0511  36  VAL   B CB  
849  C  CG1 . VAL   B 27  ? 0.6257 0.6551 0.3471 0.0843  0.1037  0.0542  36  VAL   B CG1 
850  C  CG2 . VAL   B 27  ? 0.6128 0.6370 0.3229 0.0872  0.0982  0.0435  36  VAL   B CG2 
851  N  N   . GLY   B 28  ? 0.5617 0.5907 0.2411 0.1076  0.0910  0.0549  37  GLY   B N   
852  C  CA  . GLY   B 28  ? 0.5396 0.5685 0.2048 0.1132  0.0864  0.0534  37  GLY   B CA  
853  C  C   . GLY   B 28  ? 0.5511 0.5762 0.2139 0.1174  0.0830  0.0508  37  GLY   B C   
854  O  O   . GLY   B 28  ? 0.5651 0.5896 0.2356 0.1200  0.0844  0.0537  37  GLY   B O   
855  N  N   . VAL   B 29  ? 0.5516 0.5744 0.2036 0.1188  0.0784  0.0462  38  VAL   B N   
856  C  CA  . VAL   B 29  ? 0.5600 0.5799 0.2060 0.1247  0.0739  0.0443  38  VAL   B CA  
857  C  C   . VAL   B 29  ? 0.5569 0.5724 0.1983 0.1195  0.0700  0.0365  38  VAL   B C   
858  O  O   . VAL   B 29  ? 0.5568 0.5725 0.1942 0.1150  0.0695  0.0344  38  VAL   B O   
859  C  CB  . VAL   B 29  ? 0.5623 0.5856 0.1970 0.1345  0.0711  0.0490  38  VAL   B CB  
860  C  CG1 . VAL   B 29  ? 0.5685 0.5896 0.1969 0.1414  0.0663  0.0476  38  VAL   B CG1 
861  C  CG2 . VAL   B 29  ? 0.5669 0.5967 0.2058 0.1388  0.0751  0.0577  38  VAL   B CG2 
862  N  N   . GLY   B 30  ? 0.5623 0.5745 0.2022 0.1214  0.0666  0.0332  39  GLY   B N   
863  C  CA  . GLY   B 30  ? 0.5663 0.5747 0.1993 0.1179  0.0617  0.0270  39  GLY   B CA  
864  C  C   . GLY   B 30  ? 0.5735 0.5790 0.2030 0.1224  0.0572  0.0251  39  GLY   B C   
865  O  O   . GLY   B 30  ? 0.5611 0.5680 0.1931 0.1290  0.0581  0.0288  39  GLY   B O   
866  N  N   . VAL   B 31  ? 0.5447 0.5469 0.1695 0.1183  0.0525  0.0197  40  VAL   B N   
867  C  CA  . VAL   B 31  ? 0.5786 0.5773 0.1975 0.1221  0.0465  0.0172  40  VAL   B CA  
868  C  C   . VAL   B 31  ? 0.5783 0.5762 0.2037 0.1147  0.0462  0.0120  40  VAL   B C   
869  O  O   . VAL   B 31  ? 0.5467 0.5449 0.1736 0.1056  0.0464  0.0084  40  VAL   B O   
870  C  CB  . VAL   B 31  ? 0.5895 0.5848 0.1960 0.1244  0.0400  0.0159  40  VAL   B CB  
871  C  CG1 . VAL   B 31  ? 0.5984 0.5897 0.2003 0.1267  0.0336  0.0128  40  VAL   B CG1 
872  C  CG2 . VAL   B 31  ? 0.6043 0.6014 0.2036 0.1328  0.0398  0.0205  40  VAL   B CG2 
873  N  N   . MET   B 32  ? 0.5594 0.5571 0.1884 0.1180  0.0455  0.0114  41  MET   B N   
874  C  CA  . MET   B 32  ? 0.5781 0.5758 0.2123 0.1121  0.0442  0.0063  41  MET   B CA  
875  C  C   . MET   B 32  ? 0.5860 0.5800 0.2107 0.1144  0.0366  0.0043  41  MET   B C   
876  O  O   . MET   B 32  ? 0.5837 0.5762 0.2032 0.1230  0.0335  0.0065  41  MET   B O   
877  C  CB  . MET   B 32  ? 0.5760 0.5760 0.2213 0.1138  0.0482  0.0067  41  MET   B CB  
878  C  CG  . MET   B 32  ? 0.6019 0.6035 0.2539 0.1081  0.0478  0.0012  41  MET   B CG  
879  S  SD  . MET   B 32  ? 0.6063 0.6118 0.2669 0.0966  0.0526  -0.0032 41  MET   B SD  
880  C  CE  . MET   B 32  ? 0.5967 0.6035 0.2683 0.0991  0.0598  0.0002  41  MET   B CE  
881  N  N   . GLN   B 33  ? 0.5903 0.5831 0.2126 0.1070  0.0330  0.0003  42  GLN   B N   
882  C  CA  . GLN   B 33  ? 0.6144 0.6032 0.2287 0.1077  0.0252  -0.0016 42  GLN   B CA  
883  C  C   . GLN   B 33  ? 0.6410 0.6316 0.2594 0.0976  0.0237  -0.0060 42  GLN   B C   
884  O  O   . GLN   B 33  ? 0.6378 0.6313 0.2593 0.0894  0.0265  -0.0072 42  GLN   B O   
885  C  CB  . GLN   B 33  ? 0.6388 0.6228 0.2417 0.1106  0.0201  -0.0003 42  GLN   B CB  
886  C  CG  . GLN   B 33  ? 0.6886 0.6676 0.2837 0.1139  0.0115  -0.0021 42  GLN   B CG  
887  C  CD  . GLN   B 33  ? 0.7271 0.7006 0.3114 0.1174  0.0056  -0.0015 42  GLN   B CD  
888  O  OE1 . GLN   B 33  ? 0.8130 0.7822 0.3931 0.1125  -0.0005 -0.0036 42  GLN   B OE1 
889  N  NE2 . GLN   B 33  ? 0.7135 0.6876 0.2936 0.1255  0.0074  0.0013  42  GLN   B NE2 
890  N  N   . GLU   B 34  ? 0.6486 0.6389 0.2673 0.0977  0.0196  -0.0082 43  GLU   B N   
891  C  CA  . GLU   B 34  ? 0.6656 0.6592 0.2885 0.0883  0.0179  -0.0121 43  GLU   B CA  
892  C  C   . GLU   B 34  ? 0.6487 0.6497 0.2827 0.0815  0.0253  -0.0142 43  GLU   B C   
893  O  O   . GLU   B 34  ? 0.6308 0.6360 0.2669 0.0718  0.0249  -0.0170 43  GLU   B O   
894  C  CB  . GLU   B 34  ? 0.6932 0.6833 0.3083 0.0826  0.0116  -0.0125 43  GLU   B CB  
895  C  CG  . GLU   B 34  ? 0.7295 0.7121 0.3346 0.0886  0.0032  -0.0116 43  GLU   B CG  
896  C  CD  . GLU   B 34  ? 0.7635 0.7405 0.3603 0.0851  -0.0033 -0.0111 43  GLU   B CD  
897  O  OE1 . GLU   B 34  ? 0.7911 0.7692 0.3888 0.0762  -0.0068 -0.0125 43  GLU   B OE1 
898  O  OE2 . GLU   B 34  ? 0.7850 0.7570 0.3747 0.0913  -0.0050 -0.0092 43  GLU   B OE2 
899  N  N   . GLY   B 35  ? 0.6259 0.6289 0.2672 0.0861  0.0313  -0.0133 44  GLY   B N   
900  C  CA  . GLY   B 35  ? 0.6120 0.6213 0.2650 0.0811  0.0382  -0.0159 44  GLY   B CA  
901  C  C   . GLY   B 35  ? 0.6000 0.6109 0.2535 0.0755  0.0419  -0.0158 44  GLY   B C   
902  O  O   . GLY   B 35  ? 0.5961 0.6127 0.2590 0.0701  0.0470  -0.0190 44  GLY   B O   
903  N  N   . VAL   B 36  ? 0.5835 0.5900 0.2277 0.0768  0.0394  -0.0127 45  VAL   B N   
904  C  CA  . VAL   B 36  ? 0.5566 0.5642 0.2004 0.0731  0.0427  -0.0115 45  VAL   B CA  
905  C  C   . VAL   B 36  ? 0.5523 0.5571 0.1952 0.0808  0.0458  -0.0069 45  VAL   B C   
906  O  O   . VAL   B 36  ? 0.5419 0.5421 0.1774 0.0893  0.0423  -0.0035 45  VAL   B O   
907  C  CB  . VAL   B 36  ? 0.5741 0.5796 0.2086 0.0683  0.0373  -0.0113 45  VAL   B CB  
908  C  CG1 . VAL   B 36  ? 0.5733 0.5803 0.2070 0.0644  0.0404  -0.0101 45  VAL   B CG1 
909  C  CG2 . VAL   B 36  ? 0.5785 0.5881 0.2148 0.0598  0.0344  -0.0152 45  VAL   B CG2 
910  N  N   . PHE   B 37  ? 0.5283 0.5363 0.1783 0.0784  0.0519  -0.0066 46  PHE   B N   
911  C  CA  . PHE   B 37  ? 0.5354 0.5419 0.1849 0.0842  0.0551  -0.0015 46  PHE   B CA  
912  C  C   . PHE   B 37  ? 0.5339 0.5401 0.1766 0.0816  0.0545  0.0000  46  PHE   B C   
913  O  O   . PHE   B 37  ? 0.5320 0.5416 0.1774 0.0729  0.0561  -0.0029 46  PHE   B O   
914  C  CB  . PHE   B 37  ? 0.5317 0.5410 0.1934 0.0839  0.0616  -0.0014 46  PHE   B CB  
915  C  CG  . PHE   B 37  ? 0.5366 0.5446 0.1982 0.0909  0.0641  0.0048  46  PHE   B CG  
916  C  CD1 . PHE   B 37  ? 0.5530 0.5587 0.2100 0.1001  0.0619  0.0092  46  PHE   B CD1 
917  C  CD2 . PHE   B 37  ? 0.5391 0.5492 0.2061 0.0881  0.0690  0.0064  46  PHE   B CD2 
918  C  CE1 . PHE   B 37  ? 0.5474 0.5535 0.2043 0.1064  0.0643  0.0156  46  PHE   B CE1 
919  C  CE2 . PHE   B 37  ? 0.5504 0.5603 0.2178 0.0941  0.0713  0.0129  46  PHE   B CE2 
920  C  CZ  . PHE   B 37  ? 0.5518 0.5601 0.2139 0.1032  0.0690  0.0177  46  PHE   B CZ  
921  N  N   . HIS   B 38  ? 0.5188 0.5219 0.1531 0.0889  0.0523  0.0046  47  HIS   B N   
922  C  CA  . HIS   B 38  ? 0.5297 0.5319 0.1557 0.0888  0.0505  0.0067  47  HIS   B CA  
923  C  C   . HIS   B 38  ? 0.5420 0.5464 0.1697 0.0935  0.0551  0.0116  47  HIS   B C   
924  O  O   . HIS   B 38  ? 0.5509 0.5550 0.1781 0.1020  0.0555  0.0154  47  HIS   B O   
925  C  CB  . HIS   B 38  ? 0.5280 0.5253 0.1423 0.0937  0.0431  0.0072  47  HIS   B CB  
926  C  CG  . HIS   B 38  ? 0.5344 0.5292 0.1470 0.0905  0.0379  0.0034  47  HIS   B CG  
927  N  ND1 . HIS   B 38  ? 0.5347 0.5296 0.1518 0.0924  0.0379  0.0019  47  HIS   B ND1 
928  C  CD2 . HIS   B 38  ? 0.5382 0.5307 0.1456 0.0848  0.0325  0.0011  47  HIS   B CD2 
929  C  CE1 . HIS   B 38  ? 0.5423 0.5352 0.1565 0.0884  0.0325  -0.0011 47  HIS   B CE1 
930  N  NE2 . HIS   B 38  ? 0.5329 0.5243 0.1415 0.0833  0.0291  -0.0015 47  HIS   B NE2 
931  N  N   . THR   B 39  ? 0.5355 0.5429 0.1657 0.0884  0.0586  0.0121  48  THR   B N   
932  C  CA  . THR   B 39  ? 0.5324 0.5426 0.1641 0.0921  0.0627  0.0172  48  THR   B CA  
933  C  C   . THR   B 39  ? 0.5549 0.5671 0.1831 0.0871  0.0630  0.0173  48  THR   B C   
934  O  O   . THR   B 39  ? 0.5390 0.5498 0.1627 0.0816  0.0592  0.0138  48  THR   B O   
935  C  CB  . THR   B 39  ? 0.5262 0.5388 0.1702 0.0915  0.0687  0.0185  48  THR   B CB  
936  O  OG1 . THR   B 39  ? 0.5393 0.5546 0.1846 0.0959  0.0720  0.0246  48  THR   B OG1 
937  C  CG2 . THR   B 39  ? 0.5367 0.5517 0.1906 0.0816  0.0723  0.0136  48  THR   B CG2 
938  N  N   . MET   B 40  ? 0.5592 0.5748 0.1890 0.0892  0.0667  0.0217  49  MET   B N   
939  C  CA  . MET   B 40  ? 0.5597 0.5781 0.1865 0.0855  0.0674  0.0226  49  MET   B CA  
940  C  C   . MET   B 40  ? 0.5535 0.5755 0.1909 0.0760  0.0725  0.0199  49  MET   B C   
941  O  O   . MET   B 40  ? 0.5430 0.5660 0.1904 0.0755  0.0768  0.0201  49  MET   B O   
942  C  CB  . MET   B 40  ? 0.5653 0.5865 0.1872 0.0929  0.0681  0.0286  49  MET   B CB  
943  C  CG  . MET   B 40  ? 0.5941 0.6126 0.2068 0.1034  0.0634  0.0306  49  MET   B CG  
944  S  SD  . MET   B 40  ? 0.6237 0.6460 0.2268 0.1111  0.0619  0.0352  49  MET   B SD  
945  C  CE  . MET   B 40  ? 0.6252 0.6437 0.2198 0.1067  0.0560  0.0311  49  MET   B CE  
946  N  N   A TRP   B 41  ? 0.5518 0.5758 0.1874 0.0687  0.0719  0.0172  50  TRP   B N   
947  N  N   B TRP   B 41  ? 0.5441 0.5680 0.1798 0.0687  0.0719  0.0172  50  TRP   B N   
948  N  N   C TRP   B 41  ? 0.5444 0.5683 0.1800 0.0686  0.0719  0.0172  50  TRP   B N   
949  N  N   D TRP   B 41  ? 0.5405 0.5644 0.1761 0.0687  0.0719  0.0172  50  TRP   B N   
950  C  CA  A TRP   B 41  ? 0.5530 0.5813 0.1977 0.0591  0.0762  0.0137  50  TRP   B CA  
951  C  CA  B TRP   B 41  ? 0.5426 0.5708 0.1875 0.0591  0.0763  0.0136  50  TRP   B CA  
952  C  CA  C TRP   B 41  ? 0.5503 0.5786 0.1953 0.0591  0.0763  0.0136  50  TRP   B CA  
953  C  CA  D TRP   B 41  ? 0.5424 0.5707 0.1873 0.0591  0.0763  0.0136  50  TRP   B CA  
954  C  C   A TRP   B 41  ? 0.5531 0.5845 0.2062 0.0600  0.0819  0.0171  50  TRP   B C   
955  C  C   B TRP   B 41  ? 0.5469 0.5782 0.2000 0.0601  0.0819  0.0171  50  TRP   B C   
956  C  C   C TRP   B 41  ? 0.5516 0.5829 0.2048 0.0603  0.0819  0.0171  50  TRP   B C   
957  C  C   D TRP   B 41  ? 0.5467 0.5780 0.1998 0.0601  0.0819  0.0171  50  TRP   B C   
958  O  O   A TRP   B 41  ? 0.5527 0.5856 0.2166 0.0554  0.0857  0.0140  50  TRP   B O   
959  O  O   B TRP   B 41  ? 0.5476 0.5804 0.2116 0.0555  0.0858  0.0141  50  TRP   B O   
960  O  O   C TRP   B 41  ? 0.5547 0.5873 0.2187 0.0560  0.0857  0.0142  50  TRP   B O   
961  O  O   D TRP   B 41  ? 0.5486 0.5814 0.2126 0.0556  0.0858  0.0141  50  TRP   B O   
962  C  CB  A TRP   B 41  ? 0.5514 0.5824 0.1911 0.0523  0.0743  0.0119  50  TRP   B CB  
963  C  CB  B TRP   B 41  ? 0.5328 0.5638 0.1729 0.0521  0.0744  0.0117  50  TRP   B CB  
964  C  CB  C TRP   B 41  ? 0.5424 0.5736 0.1828 0.0522  0.0747  0.0118  50  TRP   B CB  
965  C  CB  D TRP   B 41  ? 0.5289 0.5599 0.1690 0.0522  0.0744  0.0117  50  TRP   B CB  
966  C  CG  A TRP   B 41  ? 0.5512 0.5874 0.1994 0.0422  0.0779  0.0070  50  TRP   B CG  
967  C  CG  B TRP   B 41  ? 0.5265 0.5631 0.1758 0.0427  0.0789  0.0076  50  TRP   B CG  
968  C  CG  C TRP   B 41  ? 0.5454 0.5817 0.1948 0.0422  0.0784  0.0068  50  TRP   B CG  
969  C  CG  D TRP   B 41  ? 0.5246 0.5612 0.1738 0.0427  0.0788  0.0076  50  TRP   B CG  
970  C  CD1 A TRP   B 41  ? 0.5518 0.5898 0.2018 0.0352  0.0767  0.0014  50  TRP   B CD1 
971  C  CD1 B TRP   B 41  ? 0.5244 0.5653 0.1789 0.0400  0.0832  0.0090  50  TRP   B CD1 
972  C  CD1 C TRP   B 41  ? 0.5493 0.5870 0.2021 0.0361  0.0778  0.0010  50  TRP   B CD1 
973  C  CD1 D TRP   B 41  ? 0.5247 0.5656 0.1792 0.0400  0.0832  0.0090  50  TRP   B CD1 
974  C  CD2 A TRP   B 41  ? 0.5526 0.5937 0.2089 0.0381  0.0832  0.0069  50  TRP   B CD2 
975  C  CD2 B TRP   B 41  ? 0.5240 0.5632 0.1791 0.0351  0.0796  0.0012  50  TRP   B CD2 
976  C  CD2 C TRP   B 41  ? 0.5519 0.5932 0.2090 0.0377  0.0836  0.0066  50  TRP   B CD2 
977  C  CD2 D TRP   B 41  ? 0.5239 0.5631 0.1790 0.0351  0.0796  0.0012  50  TRP   B CD2 
978  N  NE1 A TRP   B 41  ? 0.5519 0.5962 0.2104 0.0274  0.0810  -0.0024 50  TRP   B NE1 
979  N  NE1 B TRP   B 41  ? 0.5141 0.5596 0.1770 0.0313  0.0863  0.0036  50  TRP   B NE1 
980  N  NE1 C TRP   B 41  ? 0.5481 0.5917 0.2100 0.0285  0.0822  -0.0030 50  TRP   B NE1 
981  N  NE1 D TRP   B 41  ? 0.5076 0.5532 0.1705 0.0313  0.0863  0.0036  50  TRP   B NE1 
982  C  CE2 A TRP   B 41  ? 0.5499 0.5956 0.2124 0.0289  0.0849  0.0006  50  TRP   B CE2 
983  C  CE2 B TRP   B 41  ? 0.5192 0.5643 0.1827 0.0284  0.0843  -0.0013 50  TRP   B CE2 
984  C  CE2 C TRP   B 41  ? 0.5477 0.5931 0.2123 0.0292  0.0856  0.0001  50  TRP   B CE2 
985  C  CE2 D TRP   B 41  ? 0.5188 0.5638 0.1823 0.0284  0.0843  -0.0013 50  TRP   B CE2 
986  C  CE3 A TRP   B 41  ? 0.5539 0.5965 0.2129 0.0411  0.0866  0.0116  50  TRP   B CE3 
987  C  CE3 B TRP   B 41  ? 0.5259 0.5639 0.1802 0.0332  0.0766  -0.0026 50  TRP   B CE3 
988  C  CE3 C TRP   B 41  ? 0.5555 0.5988 0.2140 0.0400  0.0865  0.0113  50  TRP   B CE3 
989  C  CE3 D TRP   B 41  ? 0.5269 0.5649 0.1811 0.0332  0.0765  -0.0026 50  TRP   B CE3 
990  C  CZ2 A TRP   B 41  ? 0.5511 0.6021 0.2222 0.0230  0.0896  -0.0017 50  TRP   B CZ2 
991  C  CZ2 B TRP   B 41  ? 0.5167 0.5668 0.1872 0.0204  0.0861  -0.0081 50  TRP   B CZ2 
992  C  CZ2 C TRP   B 41  ? 0.5555 0.6064 0.2286 0.0231  0.0902  -0.0023 50  TRP   B CZ2 
993  C  CZ2 D TRP   B 41  ? 0.5161 0.5662 0.1866 0.0204  0.0861  -0.0081 50  TRP   B CZ2 
994  C  CZ3 A TRP   B 41  ? 0.5517 0.5992 0.2195 0.0348  0.0911  0.0099  50  TRP   B CZ3 
995  C  CZ3 B TRP   B 41  ? 0.5251 0.5686 0.1865 0.0252  0.0786  -0.0088 50  TRP   B CZ3 
996  C  CZ3 C TRP   B 41  ? 0.5514 0.5998 0.2185 0.0335  0.0909  0.0094  50  TRP   B CZ3 
997  C  CZ3 D TRP   B 41  ? 0.5279 0.5714 0.1893 0.0252  0.0786  -0.0088 50  TRP   B CZ3 
998  C  CH2 A TRP   B 41  ? 0.5506 0.6019 0.2244 0.0260  0.0925  0.0029  50  TRP   B CH2 
999  C  CH2 B TRP   B 41  ? 0.5186 0.5683 0.1878 0.0190  0.0833  -0.0117 50  TRP   B CH2 
1000 C  CH2 C TRP   B 41  ? 0.5544 0.6061 0.2287 0.0253  0.0927  0.0024  50  TRP   B CH2 
1001 C  CH2 D TRP   B 41  ? 0.5187 0.5684 0.1879 0.0190  0.0833  -0.0118 50  TRP   B CH2 
1002 N  N   . HIS   B 42  ? 0.5566 0.5892 0.2052 0.0659  0.0822  0.0231  51  HIS   B N   
1003 C  CA  . HIS   B 42  ? 0.5606 0.5971 0.2166 0.0658  0.0872  0.0273  51  HIS   B CA  
1004 C  C   . HIS   B 42  ? 0.5676 0.6024 0.2320 0.0701  0.0898  0.0298  51  HIS   B C   
1005 O  O   . HIS   B 42  ? 0.5704 0.6073 0.2449 0.0676  0.0941  0.0316  51  HIS   B O   
1006 C  CB  . HIS   B 42  ? 0.5862 0.6260 0.2349 0.0709  0.0867  0.0332  51  HIS   B CB  
1007 C  CG  . HIS   B 42  ? 0.5813 0.6200 0.2241 0.0816  0.0848  0.0384  51  HIS   B CG  
1008 N  ND1 . HIS   B 42  ? 0.5951 0.6315 0.2261 0.0873  0.0795  0.0382  51  HIS   B ND1 
1009 C  CD2 . HIS   B 42  ? 0.6003 0.6406 0.2470 0.0877  0.0871  0.0440  51  HIS   B CD2 
1010 C  CE1 . HIS   B 42  ? 0.6072 0.6444 0.2345 0.0968  0.0787  0.0428  51  HIS   B CE1 
1011 N  NE2 . HIS   B 42  ? 0.6079 0.6478 0.2446 0.0970  0.0835  0.0468  51  HIS   B NE2 
1012 N  N   . VAL   B 43  ? 0.5594 0.5901 0.2213 0.0750  0.0871  0.0289  52  VAL   B N   
1013 C  CA  . VAL   B 43  ? 0.5648 0.5936 0.2352 0.0785  0.0891  0.0308  52  VAL   B CA  
1014 C  C   . VAL   B 43  ? 0.5694 0.5974 0.2522 0.0712  0.0918  0.0249  52  VAL   B C   
1015 O  O   . VAL   B 43  ? 0.5654 0.5934 0.2590 0.0711  0.0953  0.0271  52  VAL   B O   
1016 C  CB  . VAL   B 43  ? 0.5691 0.5944 0.2326 0.0861  0.0851  0.0315  52  VAL   B CB  
1017 C  CG1 . VAL   B 43  ? 0.5757 0.5991 0.2484 0.0891  0.0868  0.0329  52  VAL   B CG1 
1018 C  CG2 . VAL   B 43  ? 0.5696 0.5965 0.2218 0.0944  0.0825  0.0372  52  VAL   B CG2 
1019 N  N   . THR   B 44  ? 0.5695 0.5972 0.2513 0.0653  0.0902  0.0176  53  THR   B N   
1020 C  CA  . THR   B 44  ? 0.5743 0.6021 0.2672 0.0593  0.0924  0.0109  53  THR   B CA  
1021 C  C   . THR   B 44  ? 0.5773 0.6097 0.2741 0.0500  0.0946  0.0060  53  THR   B C   
1022 O  O   . THR   B 44  ? 0.5688 0.6023 0.2769 0.0455  0.0973  0.0010  53  THR   B O   
1023 C  CB  . THR   B 44  ? 0.5661 0.5920 0.2566 0.0595  0.0891  0.0059  53  THR   B CB  
1024 O  OG1 . THR   B 44  ? 0.5661 0.5935 0.2471 0.0557  0.0857  0.0032  53  THR   B OG1 
1025 C  CG2 . THR   B 44  ? 0.5664 0.5882 0.2532 0.0685  0.0866  0.0102  53  THR   B CG2 
1026 N  N   . LYS   B 45  ? 0.6025 0.6375 0.2909 0.0479  0.0934  0.0075  54  LYS   B N   
1027 C  CA  . LYS   B 45  ? 0.6759 0.7160 0.3653 0.0387  0.0945  0.0027  54  LYS   B CA  
1028 C  C   . LYS   B 45  ? 0.6354 0.6773 0.3275 0.0330  0.0936  -0.0052 54  LYS   B C   
1029 O  O   . LYS   B 45  ? 0.6272 0.6744 0.3256 0.0254  0.0959  -0.0108 54  LYS   B O   
1030 C  CB  . LYS   B 45  ? 0.7397 0.7828 0.4397 0.0346  0.0992  0.0024  54  LYS   B CB  
1031 C  CG  . LYS   B 45  ? 0.8000 0.8415 0.5025 0.0402  0.1012  0.0103  54  LYS   B CG  
1032 C  CD  . LYS   B 45  ? 0.8531 0.8976 0.5475 0.0412  0.1008  0.0156  54  LYS   B CD  
1033 C  CE  . LYS   B 45  ? 0.8978 0.9430 0.5977 0.0445  0.1037  0.0228  54  LYS   B CE  
1034 N  NZ  . LYS   B 45  ? 0.9479 0.9937 0.6374 0.0524  0.1017  0.0303  54  LYS   B NZ  
1035 N  N   . GLY   B 46  ? 0.6198 0.6585 0.3075 0.0366  0.0902  -0.0059 55  GLY   B N   
1036 C  CA  . GLY   B 46  ? 0.6246 0.6658 0.3137 0.0318  0.0886  -0.0127 55  GLY   B CA  
1037 C  C   . GLY   B 46  ? 0.6294 0.6715 0.3311 0.0310  0.0916  -0.0178 55  GLY   B C   
1038 O  O   . GLY   B 46  ? 0.6165 0.6631 0.3210 0.0259  0.0912  -0.0246 55  GLY   B O   
1039 N  N   . ALA   B 47  ? 0.6047 0.6437 0.3148 0.0350  0.0947  -0.0154 56  ALA   B N   
1040 C  CA  . ALA   B 47  ? 0.6229 0.6618 0.3462 0.0348  0.0973  -0.0202 56  ALA   B CA  
1041 C  C   . ALA   B 47  ? 0.6410 0.6774 0.3636 0.0393  0.0947  -0.0214 56  ALA   B C   
1042 O  O   . ALA   B 47  ? 0.6287 0.6618 0.3413 0.0443  0.0913  -0.0166 56  ALA   B O   
1043 C  CB  . ALA   B 47  ? 0.6422 0.6773 0.3740 0.0385  0.1002  -0.0157 56  ALA   B CB  
1044 N  N   . ALA   B 48  ? 0.6315 0.6700 0.3644 0.0376  0.0961  -0.0281 57  ALA   B N   
1045 C  CA  . ALA   B 48  ? 0.6211 0.6574 0.3565 0.0423  0.0943  -0.0293 57  ALA   B CA  
1046 C  C   . ALA   B 48  ? 0.6361 0.6651 0.3738 0.0510  0.0944  -0.0221 57  ALA   B C   
1047 O  O   . ALA   B 48  ? 0.6639 0.6906 0.4070 0.0521  0.0969  -0.0182 57  ALA   B O   
1048 C  CB  . ALA   B 48  ? 0.6133 0.6543 0.3608 0.0385  0.0963  -0.0385 57  ALA   B CB  
1049 N  N   . LEU   B 49  ? 0.6444 0.6707 0.3790 0.0566  0.0916  -0.0203 58  LEU   B N   
1050 C  CA  . LEU   B 49  ? 0.6649 0.6854 0.3998 0.0655  0.0909  -0.0129 58  LEU   B CA  
1051 C  C   . LEU   B 49  ? 0.6783 0.6978 0.4223 0.0685  0.0906  -0.0162 58  LEU   B C   
1052 O  O   . LEU   B 49  ? 0.7072 0.7303 0.4511 0.0657  0.0892  -0.0227 58  LEU   B O   
1053 C  CB  . LEU   B 49  ? 0.6492 0.6676 0.3695 0.0704  0.0869  -0.0074 58  LEU   B CB  
1054 C  CG  . LEU   B 49  ? 0.6440 0.6630 0.3542 0.0690  0.0863  -0.0035 58  LEU   B CG  
1055 C  CD1 . LEU   B 49  ? 0.6580 0.6746 0.3547 0.0746  0.0818  0.0006  58  LEU   B CD1 
1056 C  CD2 . LEU   B 49  ? 0.6557 0.6739 0.3704 0.0705  0.0897  0.0020  58  LEU   B CD2 
1057 N  N   . ARG   B 50  ? 0.6899 0.7053 0.4421 0.0739  0.0919  -0.0117 59  ARG   B N   
1058 C  CA  . ARG   B 50  ? 0.7267 0.7404 0.4871 0.0782  0.0912  -0.0133 59  ARG   B CA  
1059 C  C   . ARG   B 50  ? 0.7358 0.7469 0.4871 0.0860  0.0879  -0.0066 59  ARG   B C   
1060 O  O   . ARG   B 50  ? 0.6775 0.6868 0.4207 0.0898  0.0873  0.0012  59  ARG   B O   
1061 C  CB  . ARG   B 50  ? 0.7946 0.8054 0.5701 0.0789  0.0941  -0.0126 59  ARG   B CB  
1062 C  CG  . ARG   B 50  ? 0.8507 0.8588 0.6363 0.0841  0.0934  -0.0130 59  ARG   B CG  
1063 C  CD  . ARG   B 50  ? 0.9128 0.9176 0.7147 0.0834  0.0959  -0.0137 59  ARG   B CD  
1064 N  NE  . ARG   B 50  ? 0.9564 0.9585 0.7591 0.0825  0.0978  -0.0067 59  ARG   B NE  
1065 C  CZ  . ARG   B 50  ? 0.9861 0.9846 0.7881 0.0879  0.0975  0.0041  59  ARG   B CZ  
1066 N  NH1 . ARG   B 50  ? 1.0104 1.0072 0.8102 0.0950  0.0954  0.0094  59  ARG   B NH1 
1067 N  NH2 . ARG   B 50  ? 0.9933 0.9908 0.7967 0.0861  0.0994  0.0098  59  ARG   B NH2 
1068 N  N   . SER   B 51  ? 0.7486 0.7605 0.5003 0.0883  0.0855  -0.0098 60  SER   B N   
1069 C  CA  . SER   B 51  ? 0.8050 0.8145 0.5512 0.0964  0.0825  -0.0040 60  SER   B CA  
1070 C  C   . SER   B 51  ? 0.8450 0.8542 0.6020 0.0996  0.0822  -0.0066 60  SER   B C   
1071 O  O   . SER   B 51  ? 0.8280 0.8402 0.5840 0.0983  0.0801  -0.0125 60  SER   B O   
1072 C  CB  . SER   B 51  ? 0.7904 0.8012 0.5224 0.0967  0.0784  -0.0044 60  SER   B CB  
1073 O  OG  . SER   B 51  ? 0.8397 0.8487 0.5684 0.1042  0.0754  -0.0006 60  SER   B OG  
1074 N  N   . GLY   B 52  ? 0.9177 0.9235 0.6851 0.1036  0.0840  -0.0022 61  GLY   B N   
1075 C  CA  . GLY   B 52  ? 0.9671 0.9723 0.7480 0.1056  0.0843  -0.0057 61  GLY   B CA  
1076 C  C   . GLY   B 52  ? 0.9843 0.9913 0.7769 0.0990  0.0871  -0.0144 61  GLY   B C   
1077 O  O   . GLY   B 52  ? 0.9790 0.9845 0.7745 0.0956  0.0896  -0.0131 61  GLY   B O   
1078 N  N   . GLU   B 53  ? 1.0631 1.0739 0.8622 0.0972  0.0867  -0.0232 62  GLU   B N   
1079 C  CA  . GLU   B 53  ? 1.0828 1.0982 0.8894 0.0899  0.0891  -0.0335 62  GLU   B CA  
1080 C  C   . GLU   B 53  ? 1.0019 1.0240 0.7969 0.0839  0.0881  -0.0383 62  GLU   B C   
1081 O  O   . GLU   B 53  ? 1.0811 1.1091 0.8805 0.0775  0.0898  -0.0468 62  GLU   B O   
1082 C  CB  . GLU   B 53  ? 1.1760 1.1929 0.9976 0.0912  0.0895  -0.0409 62  GLU   B CB  
1083 C  CG  . GLU   B 53  ? 1.2398 1.2525 1.0762 0.0904  0.0921  -0.0426 62  GLU   B CG  
1084 C  CD  . GLU   B 53  ? 1.2962 1.3102 1.1486 0.0918  0.0923  -0.0510 62  GLU   B CD  
1085 O  OE1 . GLU   B 53  ? 1.3624 1.3845 1.2153 0.0890  0.0922  -0.0604 62  GLU   B OE1 
1086 O  OE2 . GLU   B 53  ? 1.3308 1.3379 1.1954 0.0956  0.0925  -0.0481 62  GLU   B OE2 
1087 N  N   . GLY   B 54  ? 0.9026 0.9241 0.6837 0.0859  0.0852  -0.0331 63  GLY   B N   
1088 C  CA  . GLY   B 54  ? 0.8335 0.8596 0.6024 0.0803  0.0836  -0.0354 63  GLY   B CA  
1089 C  C   . GLY   B 54  ? 0.8002 0.8264 0.5666 0.0749  0.0860  -0.0349 63  GLY   B C   
1090 O  O   . GLY   B 54  ? 0.7839 0.8050 0.5533 0.0775  0.0878  -0.0294 63  GLY   B O   
1091 N  N   . ARG   B 55  ? 0.7565 0.7889 0.5182 0.0675  0.0859  -0.0403 64  ARG   B N   
1092 C  CA  . ARG   B 55  ? 0.7607 0.7942 0.5177 0.0618  0.0876  -0.0399 64  ARG   B CA  
1093 C  C   . ARG   B 55  ? 0.7506 0.7851 0.4924 0.0597  0.0840  -0.0372 64  ARG   B C   
1094 O  O   . ARG   B 55  ? 0.7744 0.8123 0.5125 0.0588  0.0810  -0.0399 64  ARG   B O   
1095 C  CB  . ARG   B 55  ? 0.7925 0.8334 0.5583 0.0543  0.0905  -0.0492 64  ARG   B CB  
1096 C  CG  . ARG   B 55  ? 0.8075 0.8502 0.5712 0.0484  0.0927  -0.0494 64  ARG   B CG  
1097 C  CD  . ARG   B 55  ? 0.8386 0.8905 0.6106 0.0412  0.0951  -0.0598 64  ARG   B CD  
1098 N  NE  . ARG   B 55  ? 0.8727 0.9293 0.6392 0.0340  0.0961  -0.0609 64  ARG   B NE  
1099 C  CZ  . ARG   B 55  ? 0.9527 1.0106 0.7254 0.0303  0.0993  -0.0635 64  ARG   B CZ  
1100 N  NH1 . ARG   B 55  ? 0.9955 1.0500 0.7813 0.0328  0.1017  -0.0659 64  ARG   B NH1 
1101 N  NH2 . ARG   B 55  ? 0.9860 1.0488 0.7524 0.0238  0.0998  -0.0641 64  ARG   B NH2 
1102 N  N   . LEU   B 56  ? 0.7070 0.7385 0.4406 0.0594  0.0838  -0.0319 65  LEU   B N   
1103 C  CA  . LEU   B 56  ? 0.6554 0.6873 0.3751 0.0572  0.0801  -0.0297 65  LEU   B CA  
1104 C  C   . LEU   B 56  ? 0.6185 0.6550 0.3376 0.0492  0.0822  -0.0324 65  LEU   B C   
1105 O  O   . LEU   B 56  ? 0.6084 0.6434 0.3320 0.0494  0.0855  -0.0305 65  LEU   B O   
1106 C  CB  . LEU   B 56  ? 0.6584 0.6834 0.3687 0.0644  0.0779  -0.0211 65  LEU   B CB  
1107 C  CG  . LEU   B 56  ? 0.6770 0.6975 0.3872 0.0733  0.0760  -0.0170 65  LEU   B CG  
1108 C  CD1 . LEU   B 56  ? 0.6873 0.7031 0.3878 0.0796  0.0742  -0.0092 65  LEU   B CD1 
1109 C  CD2 . LEU   B 56  ? 0.6922 0.7142 0.3991 0.0734  0.0719  -0.0202 65  LEU   B CD2 
1110 N  N   . ASP   B 57  ? 0.5842 0.6271 0.2994 0.0422  0.0804  -0.0369 66  ASP   B N   
1111 C  CA  . ASP   B 57  ? 0.5831 0.6315 0.2969 0.0342  0.0821  -0.0392 66  ASP   B CA  
1112 C  C   . ASP   B 57  ? 0.5342 0.5802 0.2346 0.0331  0.0782  -0.0343 66  ASP   B C   
1113 O  O   . ASP   B 57  ? 0.5415 0.5853 0.2341 0.0347  0.0736  -0.0323 66  ASP   B O   
1114 C  CB  . ASP   B 57  ? 0.6030 0.6620 0.3227 0.0264  0.0832  -0.0477 66  ASP   B CB  
1115 C  CG  . ASP   B 57  ? 0.6355 0.6970 0.3695 0.0274  0.0874  -0.0536 66  ASP   B CG  
1116 O  OD1 . ASP   B 57  ? 0.6622 0.7198 0.4020 0.0294  0.0905  -0.0524 66  ASP   B OD1 
1117 O  OD2 . ASP   B 57  ? 0.6991 0.7668 0.4388 0.0260  0.0873  -0.0596 66  ASP   B OD2 
1118 N  N   . PRO   B 58  ? 0.5258 0.5727 0.2235 0.0297  0.0797  -0.0326 67  PRO   B N   
1119 C  CA  . PRO   B 58  ? 0.5244 0.5690 0.2097 0.0287  0.0759  -0.0280 67  PRO   B CA  
1120 C  C   . PRO   B 58  ? 0.5315 0.5815 0.2121 0.0218  0.0721  -0.0310 67  PRO   B C   
1121 O  O   . PRO   B 58  ? 0.5284 0.5872 0.2161 0.0154  0.0743  -0.0372 67  PRO   B O   
1122 C  CB  . PRO   B 58  ? 0.5178 0.5640 0.2040 0.0258  0.0792  -0.0268 67  PRO   B CB  
1123 C  CG  . PRO   B 58  ? 0.5328 0.5844 0.2321 0.0224  0.0844  -0.0327 67  PRO   B CG  
1124 C  CD  . PRO   B 58  ? 0.5283 0.5780 0.2350 0.0271  0.0849  -0.0350 67  PRO   B CD  
1125 N  N   . TYR   B 59  ? 0.5191 0.5646 0.1889 0.0233  0.0665  -0.0268 68  TYR   B N   
1126 C  CA  . TYR   B 59  ? 0.5141 0.5635 0.1784 0.0167  0.0617  -0.0279 68  TYR   B CA  
1127 C  C   . TYR   B 59  ? 0.5127 0.5608 0.1679 0.0132  0.0586  -0.0241 68  TYR   B C   
1128 O  O   . TYR   B 59  ? 0.4969 0.5523 0.1507 0.0041  0.0571  -0.0258 68  TYR   B O   
1129 C  CB  . TYR   B 59  ? 0.5181 0.5623 0.1784 0.0214  0.0567  -0.0266 68  TYR   B CB  
1130 C  CG  . TYR   B 59  ? 0.5167 0.5641 0.1720 0.0150  0.0512  -0.0271 68  TYR   B CG  
1131 C  CD1 . TYR   B 59  ? 0.5266 0.5698 0.1720 0.0131  0.0456  -0.0230 68  TYR   B CD1 
1132 C  CD2 . TYR   B 59  ? 0.5109 0.5664 0.1720 0.0100  0.0514  -0.0317 68  TYR   B CD2 
1133 C  CE1 . TYR   B 59  ? 0.5169 0.5625 0.1582 0.0068  0.0399  -0.0227 68  TYR   B CE1 
1134 C  CE2 . TYR   B 59  ? 0.5101 0.5688 0.1668 0.0042  0.0459  -0.0313 68  TYR   B CE2 
1135 C  CZ  . TYR   B 59  ? 0.5192 0.5727 0.1661 0.0022  0.0401  -0.0266 68  TYR   B CZ  
1136 O  OH  . TYR   B 59  ? 0.5224 0.5790 0.1657 -0.0043 0.0343  -0.0257 68  TYR   B OH  
1137 N  N   . TRP   B 60  ? 0.5118 0.5517 0.1604 0.0200  0.0570  -0.0190 69  TRP   B N   
1138 C  CA  . TRP   B 60  ? 0.5103 0.5476 0.1499 0.0186  0.0535  -0.0150 69  TRP   B CA  
1139 C  C   . TRP   B 60  ? 0.5168 0.5507 0.1560 0.0245  0.0568  -0.0117 69  TRP   B C   
1140 O  O   . TRP   B 60  ? 0.5087 0.5382 0.1501 0.0326  0.0586  -0.0103 69  TRP   B O   
1141 C  CB  . TRP   B 60  ? 0.5076 0.5380 0.1373 0.0208  0.0455  -0.0120 69  TRP   B CB  
1142 C  CG  . TRP   B 60  ? 0.5064 0.5327 0.1274 0.0214  0.0417  -0.0079 69  TRP   B CG  
1143 C  CD1 . TRP   B 60  ? 0.5033 0.5331 0.1210 0.0135  0.0392  -0.0071 69  TRP   B CD1 
1144 C  CD2 . TRP   B 60  ? 0.5061 0.5250 0.1210 0.0307  0.0403  -0.0038 69  TRP   B CD2 
1145 N  NE1 . TRP   B 60  ? 0.5066 0.5310 0.1169 0.0171  0.0361  -0.0030 69  TRP   B NE1 
1146 C  CE2 . TRP   B 60  ? 0.5134 0.5310 0.1215 0.0281  0.0367  -0.0012 69  TRP   B CE2 
1147 C  CE3 . TRP   B 60  ? 0.5158 0.5293 0.1298 0.0411  0.0414  -0.0020 69  TRP   B CE3 
1148 C  CZ2 . TRP   B 60  ? 0.5120 0.5239 0.1133 0.0356  0.0344  0.0024  69  TRP   B CZ2 
1149 C  CZ3 . TRP   B 60  ? 0.5113 0.5199 0.1181 0.0484  0.0391  0.0018  69  TRP   B CZ3 
1150 C  CH2 . TRP   B 60  ? 0.5223 0.5299 0.1227 0.0461  0.0356  0.0038  69  TRP   B CH2 
1151 N  N   . GLY   B 61  ? 0.5160 0.5519 0.1518 0.0212  0.0571  -0.0098 70  GLY   B N   
1152 C  CA  . GLY   B 61  ? 0.5129 0.5457 0.1465 0.0270  0.0591  -0.0057 70  GLY   B CA  
1153 C  C   . GLY   B 61  ? 0.5299 0.5646 0.1579 0.0230  0.0575  -0.0035 70  GLY   B C   
1154 O  O   . GLY   B 61  ? 0.5056 0.5464 0.1338 0.0134  0.0565  -0.0058 70  GLY   B O   
1155 N  N   . ASP   B 62  ? 0.5273 0.5581 0.1501 0.0295  0.0568  0.0008  71  ASP   B N   
1156 C  CA  . ASP   B 62  ? 0.5245 0.5570 0.1421 0.0270  0.0554  0.0034  71  ASP   B CA  
1157 C  C   . ASP   B 62  ? 0.5552 0.5876 0.1730 0.0334  0.0590  0.0070  71  ASP   B C   
1158 O  O   . ASP   B 62  ? 0.5352 0.5621 0.1487 0.0433  0.0573  0.0101  71  ASP   B O   
1159 C  CB  . ASP   B 62  ? 0.5375 0.5642 0.1452 0.0283  0.0473  0.0053  71  ASP   B CB  
1160 C  CG  . ASP   B 62  ? 0.5611 0.5887 0.1631 0.0258  0.0446  0.0079  71  ASP   B CG  
1161 O  OD1 . ASP   B 62  ? 0.6004 0.6275 0.2003 0.0311  0.0460  0.0108  71  ASP   B OD1 
1162 O  OD2 . ASP   B 62  ? 0.6296 0.6614 0.2319 0.0166  0.0429  0.0066  71  ASP   B OD2 
1163 N  N   . VAL   B 63  ? 0.5354 0.5743 0.1580 0.0285  0.0637  0.0068  72  VAL   B N   
1164 C  CA  . VAL   B 63  ? 0.5432 0.5833 0.1673 0.0336  0.0676  0.0106  72  VAL   B CA  
1165 C  C   . VAL   B 63  ? 0.5504 0.5870 0.1642 0.0404  0.0630  0.0152  72  VAL   B C   
1166 O  O   . VAL   B 63  ? 0.5490 0.5845 0.1616 0.0487  0.0644  0.0188  72  VAL   B O   
1167 C  CB  . VAL   B 63  ? 0.5270 0.5750 0.1583 0.0259  0.0729  0.0091  72  VAL   B CB  
1168 C  CG1 . VAL   B 63  ? 0.5289 0.5790 0.1589 0.0296  0.0750  0.0137  72  VAL   B CG1 
1169 C  CG2 . VAL   B 63  ? 0.5235 0.5742 0.1664 0.0226  0.0783  0.0050  72  VAL   B CG2 
1170 N  N   . LYS   B 64  ? 0.5487 0.5834 0.1550 0.0378  0.0572  0.0152  73  LYS   B N   
1171 C  CA  . LYS   B 64  ? 0.5769 0.6091 0.1743 0.0440  0.0529  0.0191  73  LYS   B CA  
1172 C  C   . LYS   B 64  ? 0.5687 0.5935 0.1602 0.0548  0.0489  0.0204  73  LYS   B C   
1173 O  O   . LYS   B 64  ? 0.5881 0.6124 0.1752 0.0638  0.0484  0.0237  73  LYS   B O   
1174 C  CB  . LYS   B 64  ? 0.5824 0.6135 0.1738 0.0388  0.0470  0.0190  73  LYS   B CB  
1175 C  CG  . LYS   B 64  ? 0.5936 0.6222 0.1768 0.0455  0.0428  0.0226  73  LYS   B CG  
1176 C  CD  . LYS   B 64  ? 0.6127 0.6424 0.1920 0.0398  0.0387  0.0235  73  LYS   B CD  
1177 C  CE  . LYS   B 64  ? 0.6378 0.6646 0.2094 0.0476  0.0340  0.0267  73  LYS   B CE  
1178 N  NZ  . LYS   B 64  ? 0.6373 0.6634 0.2049 0.0417  0.0284  0.0277  73  LYS   B NZ  
1179 N  N   . GLN   B 65  ? 0.5712 0.5914 0.1626 0.0539  0.0458  0.0177  74  GLN   B N   
1180 C  CA  . GLN   B 65  ? 0.5779 0.5915 0.1647 0.0635  0.0421  0.0181  74  GLN   B CA  
1181 C  C   . GLN   B 65  ? 0.5859 0.6019 0.1785 0.0689  0.0480  0.0193  74  GLN   B C   
1182 O  O   . GLN   B 65  ? 0.5549 0.5674 0.1429 0.0788  0.0458  0.0209  74  GLN   B O   
1183 C  CB  . GLN   B 65  ? 0.6053 0.6138 0.1911 0.0606  0.0373  0.0151  74  GLN   B CB  
1184 C  CG  . GLN   B 65  ? 0.6328 0.6383 0.2132 0.0547  0.0305  0.0146  74  GLN   B CG  
1185 C  CD  . GLN   B 65  ? 0.6593 0.6608 0.2398 0.0513  0.0261  0.0120  74  GLN   B CD  
1186 O  OE1 . GLN   B 65  ? 0.6793 0.6759 0.2581 0.0580  0.0238  0.0113  74  GLN   B OE1 
1187 N  NE2 . GLN   B 65  ? 0.6750 0.6799 0.2580 0.0407  0.0252  0.0105  74  GLN   B NE2 
1188 N  N   . ASP   B 66  ? 0.5581 0.5796 0.1601 0.0635  0.0549  0.0186  75  ASP   B N   
1189 C  CA  . ASP   B 66  ? 0.5658 0.5892 0.1750 0.0675  0.0604  0.0200  75  ASP   B CA  
1190 C  C   . ASP   B 66  ? 0.5580 0.5767 0.1678 0.0712  0.0584  0.0182  75  ASP   B C   
1191 O  O   . ASP   B 66  ? 0.5571 0.5751 0.1674 0.0794  0.0597  0.0210  75  ASP   B O   
1192 C  CB  . ASP   B 66  ? 0.5588 0.5845 0.1651 0.0761  0.0620  0.0253  75  ASP   B CB  
1193 C  CG  . ASP   B 66  ? 0.5674 0.5969 0.1831 0.0773  0.0686  0.0277  75  ASP   B CG  
1194 O  OD1 . ASP   B 66  ? 0.5437 0.5746 0.1686 0.0705  0.0724  0.0250  75  ASP   B OD1 
1195 O  OD2 . ASP   B 66  ? 0.5572 0.5882 0.1708 0.0859  0.0695  0.0324  75  ASP   B OD2 
1196 N  N   . LEU   B 67  ? 0.5328 0.5497 0.1436 0.0649  0.0559  0.0139  76  LEU   B N   
1197 C  CA  . LEU   B 67  ? 0.5263 0.5396 0.1386 0.0669  0.0540  0.0116  76  LEU   B CA  
1198 C  C   . LEU   B 67  ? 0.5259 0.5428 0.1477 0.0583  0.0574  0.0072  76  LEU   B C   
1199 O  O   . LEU   B 67  ? 0.5096 0.5308 0.1335 0.0494  0.0585  0.0048  76  LEU   B O   
1200 C  CB  . LEU   B 67  ? 0.5260 0.5332 0.1286 0.0695  0.0459  0.0110  76  LEU   B CB  
1201 C  CG  . LEU   B 67  ? 0.5188 0.5220 0.1121 0.0801  0.0418  0.0143  76  LEU   B CG  
1202 C  CD1 . LEU   B 67  ? 0.5245 0.5210 0.1095 0.0811  0.0333  0.0127  76  LEU   B CD1 
1203 C  CD2 . LEU   B 67  ? 0.5307 0.5339 0.1255 0.0896  0.0442  0.0165  76  LEU   B CD2 
1204 N  N   . VAL   B 68  ? 0.5248 0.5403 0.1513 0.0608  0.0582  0.0056  77  VAL   B N   
1205 C  CA  . VAL   B 68  ? 0.5233 0.5423 0.1590 0.0540  0.0609  0.0006  77  VAL   B CA  
1206 C  C   . VAL   B 68  ? 0.5410 0.5565 0.1766 0.0579  0.0580  -0.0007 77  VAL   B C   
1207 O  O   . VAL   B 68  ? 0.5198 0.5314 0.1531 0.0673  0.0573  0.0026  77  VAL   B O   
1208 C  CB  . VAL   B 68  ? 0.5275 0.5509 0.1741 0.0519  0.0681  0.0000  77  VAL   B CB  
1209 C  CG1 . VAL   B 68  ? 0.5246 0.5455 0.1743 0.0606  0.0708  0.0044  77  VAL   B CG1 
1210 C  CG2 . VAL   B 68  ? 0.5291 0.5571 0.1853 0.0446  0.0707  -0.0060 77  VAL   B CG2 
1211 N  N   . SER   B 69  ? 0.5289 0.5466 0.1669 0.0517  0.0563  -0.0051 78  SER   B N   
1212 C  CA  . SER   B 69  ? 0.5022 0.5180 0.1421 0.0544  0.0543  -0.0070 78  SER   B CA  
1213 C  C   . SER   B 69  ? 0.5257 0.5476 0.1776 0.0493  0.0593  -0.0118 78  SER   B C   
1214 O  O   . SER   B 69  ? 0.4972 0.5256 0.1534 0.0404  0.0619  -0.0153 78  SER   B O   
1215 C  CB  . SER   B 69  ? 0.5056 0.5187 0.1376 0.0525  0.0471  -0.0078 78  SER   B CB  
1216 O  OG  . SER   B 69  ? 0.5116 0.5303 0.1449 0.0418  0.0462  -0.0110 78  SER   B OG  
1217 N  N   . TYR   B 70  ? 0.5090 0.5298 0.1656 0.0537  0.0597  -0.0128 79  TYR   B N   
1218 C  CA  . TYR   B 70  ? 0.5185 0.5441 0.1869 0.0510  0.0637  -0.0176 79  TYR   B CA  
1219 C  C   . TYR   B 70  ? 0.5338 0.5601 0.2018 0.0507  0.0600  -0.0204 79  TYR   B C   
1220 O  O   . TYR   B 70  ? 0.5266 0.5475 0.1873 0.0564  0.0551  -0.0175 79  TYR   B O   
1221 C  CB  . TYR   B 70  ? 0.5201 0.5436 0.1965 0.0574  0.0683  -0.0155 79  TYR   B CB  
1222 C  CG  . TYR   B 70  ? 0.5196 0.5438 0.1991 0.0563  0.0727  -0.0135 79  TYR   B CG  
1223 C  CD1 . TYR   B 70  ? 0.5170 0.5380 0.1887 0.0601  0.0718  -0.0077 79  TYR   B CD1 
1224 C  CD2 . TYR   B 70  ? 0.5242 0.5527 0.2152 0.0517  0.0777  -0.0175 79  TYR   B CD2 
1225 C  CE1 . TYR   B 70  ? 0.5225 0.5450 0.1974 0.0588  0.0758  -0.0056 79  TYR   B CE1 
1226 C  CE2 . TYR   B 70  ? 0.5219 0.5509 0.2167 0.0506  0.0815  -0.0155 79  TYR   B CE2 
1227 C  CZ  . TYR   B 70  ? 0.5254 0.5518 0.2117 0.0534  0.0806  -0.0096 79  TYR   B CZ  
1228 O  OH  . TYR   B 70  ? 0.5315 0.5592 0.2214 0.0520  0.0842  -0.0074 79  TYR   B OH  
1229 N  N   . CYS   B 71  ? 0.5399 0.5738 0.2148 0.0432  0.0615  -0.0262 80  CYS   B N   
1230 C  CA  . CYS   B 71  ? 0.5477 0.5848 0.2250 0.0420  0.0590  -0.0297 80  CYS   B CA  
1231 C  C   . CYS   B 71  ? 0.5446 0.5812 0.2120 0.0381  0.0525  -0.0286 80  CYS   B C   
1232 O  O   . CYS   B 71  ? 0.5452 0.5857 0.2139 0.0353  0.0498  -0.0312 80  CYS   B O   
1233 C  CB  . CYS   B 71  ? 0.5723 0.6047 0.2519 0.0507  0.0582  -0.0282 80  CYS   B CB  
1234 S  SG  . CYS   B 71  ? 0.6187 0.6488 0.3084 0.0571  0.0645  -0.0269 80  CYS   B SG  
1235 N  N   . GLY   B 72  ? 0.5304 0.5631 0.1890 0.0371  0.0497  -0.0249 81  GLY   B N   
1236 C  CA  . GLY   B 72  ? 0.5341 0.5643 0.1836 0.0345  0.0425  -0.0233 81  GLY   B CA  
1237 C  C   . GLY   B 72  ? 0.5297 0.5546 0.1701 0.0349  0.0397  -0.0191 81  GLY   B C   
1238 O  O   . GLY   B 72  ? 0.5342 0.5572 0.1746 0.0382  0.0433  -0.0171 81  GLY   B O   
1239 N  N   . PRO   B 73  ? 0.5468 0.5693 0.1795 0.0313  0.0328  -0.0176 82  PRO   B N   
1240 C  CA  . PRO   B 73  ? 0.5522 0.5688 0.1759 0.0320  0.0289  -0.0138 82  PRO   B CA  
1241 C  C   . PRO   B 73  ? 0.5763 0.5832 0.1933 0.0433  0.0264  -0.0104 82  PRO   B C   
1242 O  O   . PRO   B 73  ? 0.5667 0.5707 0.1844 0.0495  0.0253  -0.0109 82  PRO   B O   
1243 C  CB  . PRO   B 73  ? 0.5613 0.5772 0.1798 0.0255  0.0213  -0.0132 82  PRO   B CB  
1244 C  CG  . PRO   B 73  ? 0.5555 0.5746 0.1784 0.0243  0.0201  -0.0159 82  PRO   B CG  
1245 C  CD  . PRO   B 73  ? 0.5500 0.5753 0.1827 0.0262  0.0282  -0.0193 82  PRO   B CD  
1246 N  N   . TRP   B 74  ? 0.5787 0.5819 0.1896 0.0453  0.0253  -0.0075 83  TRP   B N   
1247 C  CA  . TRP   B 74  ? 0.5777 0.5734 0.1819 0.0563  0.0232  -0.0044 83  TRP   B CA  
1248 C  C   . TRP   B 74  ? 0.5997 0.5886 0.1978 0.0607  0.0154  -0.0045 83  TRP   B C   
1249 O  O   . TRP   B 74  ? 0.5916 0.5779 0.1855 0.0556  0.0089  -0.0046 83  TRP   B O   
1250 C  CB  . TRP   B 74  ? 0.5743 0.5679 0.1725 0.0571  0.0223  -0.0016 83  TRP   B CB  
1251 C  CG  . TRP   B 74  ? 0.5638 0.5522 0.1560 0.0686  0.0212  0.0011  83  TRP   B CG  
1252 C  CD1 . TRP   B 74  ? 0.5673 0.5482 0.1504 0.0753  0.0138  0.0021  83  TRP   B CD1 
1253 C  CD2 . TRP   B 74  ? 0.5472 0.5382 0.1418 0.0743  0.0274  0.0033  83  TRP   B CD2 
1254 N  NE1 . TRP   B 74  ? 0.5592 0.5390 0.1387 0.0852  0.0154  0.0045  83  TRP   B NE1 
1255 C  CE2 . TRP   B 74  ? 0.5554 0.5416 0.1421 0.0849  0.0238  0.0056  83  TRP   B CE2 
1256 C  CE3 . TRP   B 74  ? 0.5394 0.5365 0.1429 0.0723  0.0355  0.0034  83  TRP   B CE3 
1257 C  CZ2 . TRP   B 74  ? 0.5518 0.5404 0.1388 0.0920  0.0283  0.0087  83  TRP   B CZ2 
1258 C  CZ3 . TRP   B 74  ? 0.5477 0.5461 0.1520 0.0792  0.0397  0.0067  83  TRP   B CZ3 
1259 C  CH2 . TRP   B 74  ? 0.5540 0.5486 0.1498 0.0890  0.0362  0.0096  83  TRP   B CH2 
1260 N  N   . LYS   B 75  ? 0.6116 0.5971 0.2084 0.0705  0.0152  -0.0039 84  LYS   B N   
1261 C  CA  . LYS   B 75  ? 0.6238 0.6033 0.2153 0.0745  0.0076  -0.0047 84  LYS   B CA  
1262 C  C   . LYS   B 75  ? 0.6570 0.6292 0.2388 0.0847  0.0024  -0.0028 84  LYS   B C   
1263 O  O   . LYS   B 75  ? 0.6689 0.6352 0.2455 0.0874  -0.0050 -0.0039 84  LYS   B O   
1264 C  CB  . LYS   B 75  ? 0.6582 0.6404 0.2558 0.0774  0.0102  -0.0063 84  LYS   B CB  
1265 C  CG  . LYS   B 75  ? 0.6511 0.6412 0.2587 0.0687  0.0150  -0.0090 84  LYS   B CG  
1266 C  CD  . LYS   B 75  ? 0.6616 0.6524 0.2689 0.0613  0.0094  -0.0111 84  LYS   B CD  
1267 C  CE  . LYS   B 75  ? 0.6849 0.6852 0.3026 0.0540  0.0149  -0.0142 84  LYS   B CE  
1268 N  NZ  . LYS   B 75  ? 0.7120 0.7154 0.3308 0.0470  0.0103  -0.0162 84  LYS   B NZ  
1269 N  N   . LEU   B 76  ? 0.6472 0.6199 0.2268 0.0904  0.0058  -0.0004 85  LEU   B N   
1270 C  CA  . LEU   B 76  ? 0.6808 0.6488 0.2518 0.1020  0.0021  0.0009  85  LEU   B CA  
1271 C  C   . LEU   B 76  ? 0.7046 0.6669 0.2680 0.1003  -0.0047 0.0009  85  LEU   B C   
1272 O  O   . LEU   B 76  ? 0.6661 0.6309 0.2311 0.0941  -0.0022 0.0020  85  LEU   B O   
1273 C  CB  . LEU   B 76  ? 0.6577 0.6309 0.2310 0.1079  0.0096  0.0039  85  LEU   B CB  
1274 C  CG  . LEU   B 76  ? 0.6541 0.6330 0.2369 0.1074  0.0170  0.0045  85  LEU   B CG  
1275 C  CD1 . LEU   B 76  ? 0.6547 0.6384 0.2403 0.1117  0.0240  0.0082  85  LEU   B CD1 
1276 C  CD2 . LEU   B 76  ? 0.6706 0.6479 0.2533 0.1130  0.0145  0.0035  85  LEU   B CD2 
1277 N  N   . ASP   B 77  ? 0.7334 0.6882 0.2897 0.1046  -0.0135 -0.0004 86  ASP   B N   
1278 C  CA  . ASP   B 77  ? 0.7743 0.7223 0.3245 0.1019  -0.0216 -0.0007 86  ASP   B CA  
1279 C  C   . ASP   B 77  ? 0.7730 0.7147 0.3139 0.1136  -0.0280 -0.0014 86  ASP   B C   
1280 O  O   . ASP   B 77  ? 0.7787 0.7148 0.3146 0.1134  -0.0341 -0.0015 86  ASP   B O   
1281 C  CB  . ASP   B 77  ? 0.8242 0.7687 0.3760 0.0926  -0.0276 -0.0022 86  ASP   B CB  
1282 C  CG  . ASP   B 77  ? 0.8945 0.8341 0.4441 0.0971  -0.0337 -0.0045 86  ASP   B CG  
1283 O  OD1 . ASP   B 77  ? 0.9405 0.8799 0.4872 0.1078  -0.0328 -0.0052 86  ASP   B OD1 
1284 O  OD2 . ASP   B 77  ? 0.9643 0.9013 0.5153 0.0896  -0.0389 -0.0054 86  ASP   B OD2 
1285 N  N   . ALA   B 78  ? 0.7334 0.6766 0.2722 0.1240  -0.0267 -0.0019 87  ALA   B N   
1286 C  CA  . ALA   B 78  ? 0.7471 0.6861 0.2769 0.1359  -0.0324 -0.0031 87  ALA   B CA  
1287 C  C   . ALA   B 78  ? 0.7443 0.6864 0.2713 0.1394  -0.0296 -0.0010 87  ALA   B C   
1288 O  O   . ALA   B 78  ? 0.7148 0.6646 0.2471 0.1364  -0.0207 0.0019  87  ALA   B O   
1289 C  CB  . ALA   B 78  ? 0.7516 0.6941 0.2805 0.1455  -0.0305 -0.0036 87  ALA   B CB  
1290 N  N   . ALA   B 79  ? 0.7505 0.6873 0.2694 0.1474  -0.0368 -0.0028 88  ALA   B N   
1291 C  CA  . ALA   B 79  ? 0.7700 0.7086 0.2851 0.1514  -0.0362 -0.0015 88  ALA   B CA  
1292 C  C   . ALA   B 79  ? 0.7733 0.7137 0.2809 0.1661  -0.0386 -0.0031 88  ALA   B C   
1293 O  O   . ALA   B 79  ? 0.7813 0.7166 0.2844 0.1725  -0.0454 -0.0067 88  ALA   B O   
1294 C  CB  . ALA   B 79  ? 0.7754 0.7053 0.2882 0.1452  -0.0440 -0.0025 88  ALA   B CB  
1295 N  N   . TRP   B 80  ? 0.7536 0.7023 0.2602 0.1717  -0.0329 -0.0005 89  TRP   B N   
1296 C  CA  . TRP   B 80  ? 0.7861 0.7374 0.2848 0.1856  -0.0361 -0.0022 89  TRP   B CA  
1297 C  C   . TRP   B 80  ? 0.8048 0.7450 0.2966 0.1887  -0.0478 -0.0069 89  TRP   B C   
1298 O  O   . TRP   B 80  ? 0.7909 0.7246 0.2842 0.1804  -0.0512 -0.0066 89  TRP   B O   
1299 C  CB  . TRP   B 80  ? 0.7642 0.7263 0.2633 0.1890  -0.0287 0.0016  89  TRP   B CB  
1300 C  CG  . TRP   B 80  ? 0.7567 0.7245 0.2483 0.2033  -0.0307 0.0003  89  TRP   B CG  
1301 C  CD1 . TRP   B 80  ? 0.7599 0.7317 0.2476 0.2135  -0.0318 -0.0013 89  TRP   B CD1 
1302 C  CD2 . TRP   B 80  ? 0.7496 0.7224 0.2373 0.2091  -0.0307 0.0009  89  TRP   B CD2 
1303 N  NE1 . TRP   B 80  ? 0.7712 0.7498 0.2523 0.2254  -0.0332 -0.0023 89  TRP   B NE1 
1304 C  CE2 . TRP   B 80  ? 0.7750 0.7543 0.2560 0.2231  -0.0326 -0.0010 89  TRP   B CE2 
1305 C  CE3 . TRP   B 80  ? 0.7519 0.7243 0.2407 0.2041  -0.0301 0.0025  89  TRP   B CE3 
1306 C  CZ2 . TRP   B 80  ? 0.7584 0.7445 0.2341 0.2324  -0.0335 -0.0016 89  TRP   B CZ2 
1307 C  CZ3 . TRP   B 80  ? 0.7544 0.7328 0.2380 0.2132  -0.0310 0.0022  89  TRP   B CZ3 
1308 C  CH2 . TRP   B 80  ? 0.7666 0.7523 0.2439 0.2273  -0.0325 0.0001  89  TRP   B CH2 
1309 N  N   . ASP   B 81  ? 0.8547 0.7929 0.3398 0.2001  -0.0541 -0.0111 90  ASP   B N   
1310 C  CA  . ASP   B 81  ? 0.8903 0.8170 0.3690 0.2048  -0.0665 -0.0166 90  ASP   B CA  
1311 C  C   . ASP   B 81  ? 0.8817 0.8103 0.3560 0.2111  -0.0682 -0.0171 90  ASP   B C   
1312 O  O   . ASP   B 81  ? 0.8979 0.8159 0.3686 0.2123  -0.0781 -0.0207 90  ASP   B O   
1313 C  CB  . ASP   B 81  ? 0.8696 0.7943 0.3429 0.2151  -0.0725 -0.0217 90  ASP   B CB  
1314 C  CG  . ASP   B 81  ? 0.8984 0.8356 0.3675 0.2282  -0.0679 -0.0218 90  ASP   B CG  
1315 O  OD1 . ASP   B 81  ? 0.9115 0.8591 0.3816 0.2300  -0.0604 -0.0179 90  ASP   B OD1 
1316 O  OD2 . ASP   B 81  ? 0.9477 0.8852 0.4129 0.2362  -0.0718 -0.0255 90  ASP   B OD2 
1317 N  N   . GLY   B 82  ? 0.8812 0.8227 0.3561 0.2151  -0.0593 -0.0134 91  GLY   B N   
1318 C  CA  . GLY   B 82  ? 0.8850 0.8321 0.3563 0.2217  -0.0589 -0.0131 91  GLY   B CA  
1319 C  C   . GLY   B 82  ? 0.9148 0.8689 0.3786 0.2380  -0.0614 -0.0168 91  GLY   B C   
1320 O  O   . GLY   B 82  ? 0.9114 0.8715 0.3717 0.2452  -0.0614 -0.0171 91  GLY   B O   
1321 N  N   . LEU   B 83  ? 0.9020 0.8562 0.3633 0.2439  -0.0636 -0.0198 92  LEU   B N   
1322 C  CA  . LEU   B 83  ? 0.9395 0.8998 0.3929 0.2598  -0.0676 -0.0246 92  LEU   B CA  
1323 C  C   . LEU   B 83  ? 0.9309 0.9052 0.3850 0.2646  -0.0595 -0.0214 92  LEU   B C   
1324 O  O   . LEU   B 83  ? 0.9437 0.9314 0.3932 0.2761  -0.0569 -0.0213 92  LEU   B O   
1325 C  CB  . LEU   B 83  ? 0.9908 0.9375 0.4398 0.2632  -0.0797 -0.0321 92  LEU   B CB  
1326 C  CG  . LEU   B 83  ? 1.0240 0.9576 0.4697 0.2645  -0.0908 -0.0372 92  LEU   B CG  
1327 C  CD1 . LEU   B 83  ? 1.0673 0.9878 0.5096 0.2675  -0.1025 -0.0442 92  LEU   B CD1 
1328 C  CD2 . LEU   B 83  ? 1.0106 0.9522 0.4505 0.2770  -0.0920 -0.0398 92  LEU   B CD2 
1329 N  N   . SER   B 84  ? 0.9124 0.8835 0.3711 0.2574  -0.0571 -0.0196 93  SER   B N   
1330 C  CA  . SER   B 84  ? 0.8590 0.8401 0.3174 0.2631  -0.0526 -0.0180 93  SER   B CA  
1331 C  C   . SER   B 84  ? 0.8378 0.8326 0.3020 0.2599  -0.0403 -0.0097 93  SER   B C   
1332 O  O   . SER   B 84  ? 0.7930 0.7868 0.2638 0.2493  -0.0347 -0.0052 93  SER   B O   
1333 C  CB  . SER   B 84  ? 0.8788 0.8509 0.3402 0.2570  -0.0555 -0.0195 93  SER   B CB  
1334 O  OG  . SER   B 84  ? 0.8926 0.8502 0.3500 0.2572  -0.0670 -0.0264 93  SER   B OG  
1335 N  N   . GLU   B 85  ? 0.7844 0.7912 0.2473 0.2675  -0.0363 -0.0075 94  GLU   B N   
1336 C  CA  . GLU   B 85  ? 0.7724 0.7924 0.2414 0.2651  -0.0251 0.0007  94  GLU   B CA  
1337 C  C   . GLU   B 85  ? 0.7426 0.7554 0.2207 0.2523  -0.0214 0.0036  94  GLU   B C   
1338 O  O   . GLU   B 85  ? 0.7406 0.7408 0.2189 0.2478  -0.0275 -0.0008 94  GLU   B O   
1339 C  CB  . GLU   B 85  ? 0.7843 0.8188 0.2487 0.2774  -0.0234 0.0020  94  GLU   B CB  
1340 C  CG  . GLU   B 85  ? 0.8139 0.8596 0.2705 0.2896  -0.0251 0.0002  94  GLU   B CG  
1341 C  CD  . GLU   B 85  ? 0.8382 0.9036 0.2917 0.3003  -0.0203 0.0043  94  GLU   B CD  
1342 O  OE1 . GLU   B 85  ? 0.8253 0.8957 0.2820 0.2995  -0.0163 0.0085  94  GLU   B OE1 
1343 O  OE2 . GLU   B 85  ? 0.8763 0.9529 0.3244 0.3094  -0.0205 0.0036  94  GLU   B OE2 
1344 N  N   . VAL   B 86  ? 0.7250 0.7447 0.2110 0.2458  -0.0119 0.0108  95  VAL   B N   
1345 C  CA  . VAL   B 86  ? 0.7100 0.7244 0.2053 0.2343  -0.0076 0.0135  95  VAL   B CA  
1346 C  C   . VAL   B 86  ? 0.6859 0.7122 0.1866 0.2359  0.0007  0.0204  95  VAL   B C   
1347 O  O   . VAL   B 86  ? 0.7170 0.7557 0.2144 0.2445  0.0034  0.0238  95  VAL   B O   
1348 C  CB  . VAL   B 86  ? 0.6733 0.6819 0.1748 0.2221  -0.0047 0.0147  95  VAL   B CB  
1349 C  CG1 . VAL   B 86  ? 0.6874 0.6860 0.1835 0.2210  -0.0127 0.0092  95  VAL   B CG1 
1350 C  CG2 . VAL   B 86  ? 0.6779 0.6975 0.1835 0.2210  0.0037  0.0212  95  VAL   B CG2 
1351 N  N   . GLN   B 87  ? 0.6739 0.6973 0.1831 0.2279  0.0047  0.0229  96  GLN   B N   
1352 C  CA  . GLN   B 87  ? 0.6717 0.7054 0.1881 0.2275  0.0132  0.0306  96  GLN   B CA  
1353 C  C   . GLN   B 87  ? 0.6479 0.6793 0.1753 0.2154  0.0200  0.0342  96  GLN   B C   
1354 O  O   . GLN   B 87  ? 0.6401 0.6618 0.1720 0.2067  0.0186  0.0309  96  GLN   B O   
1355 C  CB  . GLN   B 87  ? 0.6802 0.7157 0.1973 0.2316  0.0125  0.0312  96  GLN   B CB  
1356 C  CG  . GLN   B 87  ? 0.6832 0.7260 0.1904 0.2448  0.0081  0.0296  96  GLN   B CG  
1357 C  CD  . GLN   B 87  ? 0.6956 0.7403 0.2036 0.2485  0.0071  0.0301  96  GLN   B CD  
1358 O  OE1 . GLN   B 87  ? 0.6701 0.7114 0.1864 0.2418  0.0103  0.0324  96  GLN   B OE1 
1359 N  NE2 . GLN   B 87  ? 0.6972 0.7476 0.1958 0.2600  0.0022  0.0274  96  GLN   B NE2 
1360 N  N   . LEU   B 88  ? 0.6339 0.6747 0.1656 0.2149  0.0269  0.0407  97  LEU   B N   
1361 C  CA  . LEU   B 88  ? 0.6069 0.6471 0.1505 0.2041  0.0340  0.0448  97  LEU   B CA  
1362 C  C   . LEU   B 88  ? 0.6352 0.6779 0.1857 0.2043  0.0373  0.0487  97  LEU   B C   
1363 O  O   . LEU   B 88  ? 0.6345 0.6872 0.1826 0.2131  0.0386  0.0536  97  LEU   B O   
1364 C  CB  . LEU   B 88  ? 0.6160 0.6656 0.1621 0.2037  0.0398  0.0507  97  LEU   B CB  
1365 C  CG  . LEU   B 88  ? 0.6124 0.6631 0.1710 0.1942  0.0472  0.0557  97  LEU   B CG  
1366 C  CD1 . LEU   B 88  ? 0.6061 0.6462 0.1693 0.1830  0.0466  0.0505  97  LEU   B CD1 
1367 C  CD2 . LEU   B 88  ? 0.6130 0.6739 0.1735 0.1947  0.0523  0.0619  97  LEU   B CD2 
1368 N  N   . LEU   B 89  ? 0.6152 0.6501 0.1732 0.1962  0.0381  0.0466  98  LEU   B N   
1369 C  CA  . LEU   B 89  ? 0.6207 0.6578 0.1872 0.1956  0.0418  0.0506  98  LEU   B CA  
1370 C  C   . LEU   B 89  ? 0.6195 0.6606 0.1967 0.1892  0.0494  0.0565  98  LEU   B C   
1371 O  O   . LEU   B 89  ? 0.5985 0.6332 0.1840 0.1792  0.0516  0.0541  98  LEU   B O   
1372 C  CB  . LEU   B 89  ? 0.6454 0.6728 0.2146 0.1905  0.0385  0.0448  98  LEU   B CB  
1373 C  CG  . LEU   B 89  ? 0.6606 0.6884 0.2390 0.1892  0.0414  0.0474  98  LEU   B CG  
1374 C  CD1 . LEU   B 89  ? 0.7090 0.7465 0.2892 0.1963  0.0449  0.0553  98  LEU   B CD1 
1375 C  CD2 . LEU   B 89  ? 0.6825 0.7038 0.2578 0.1900  0.0356  0.0416  98  LEU   B CD2 
1376 N  N   . ALA   B 90  ? 0.6123 0.6636 0.1890 0.1942  0.0528  0.0634  99  ALA   B N   
1377 C  CA  . ALA   B 90  ? 0.6132 0.6691 0.1998 0.1885  0.0597  0.0697  99  ALA   B CA  
1378 C  C   . ALA   B 90  ? 0.6229 0.6776 0.2212 0.1852  0.0632  0.0734  99  ALA   B C   
1379 O  O   . ALA   B 90  ? 0.6306 0.6889 0.2280 0.1918  0.0622  0.0766  99  ALA   B O   
1380 C  CB  . ALA   B 90  ? 0.6326 0.7007 0.2152 0.1950  0.0619  0.0764  99  ALA   B CB  
1381 N  N   . VAL   B 91  ? 0.6137 0.6638 0.2228 0.1755  0.0671  0.0730  100 VAL   B N   
1382 C  CA  . VAL   B 91  ? 0.6117 0.6606 0.2340 0.1715  0.0711  0.0768  100 VAL   B CA  
1383 C  C   . VAL   B 91  ? 0.6236 0.6771 0.2543 0.1668  0.0766  0.0830  100 VAL   B C   
1384 O  O   . VAL   B 91  ? 0.6206 0.6692 0.2590 0.1578  0.0790  0.0798  100 VAL   B O   
1385 C  CB  . VAL   B 91  ? 0.5957 0.6345 0.2235 0.1642  0.0699  0.0691  100 VAL   B CB  
1386 C  CG1 . VAL   B 91  ? 0.5948 0.6317 0.2362 0.1611  0.0731  0.0718  100 VAL   B CG1 
1387 C  CG2 . VAL   B 91  ? 0.5835 0.6180 0.2017 0.1680  0.0638  0.0627  100 VAL   B CG2 
1388 N  N   . PRO   B 92  ? 0.6043 0.6680 0.2344 0.1722  0.0788  0.0919  101 PRO   B N   
1389 C  CA  . PRO   B 92  ? 0.6164 0.6850 0.2544 0.1676  0.0837  0.0983  101 PRO   B CA  
1390 C  C   . PRO   B 92  ? 0.6135 0.6786 0.2669 0.1618  0.0872  0.1020  101 PRO   B C   
1391 O  O   . PRO   B 92  ? 0.6402 0.7019 0.2974 0.1638  0.0861  0.1020  101 PRO   B O   
1392 C  CB  . PRO   B 92  ? 0.6254 0.7073 0.2572 0.1761  0.0844  0.1070  101 PRO   B CB  
1393 C  CG  . PRO   B 92  ? 0.6180 0.7013 0.2373 0.1854  0.0793  0.1034  101 PRO   B CG  
1394 C  CD  . PRO   B 92  ? 0.6302 0.7023 0.2524 0.1829  0.0767  0.0968  101 PRO   B CD  
1395 N  N   . PRO   B 93  ? 0.6329 0.6977 0.2962 0.1541  0.0912  0.1042  102 PRO   B N   
1396 C  CA  . PRO   B 93  ? 0.6474 0.7079 0.3262 0.1488  0.0939  0.1071  102 PRO   B CA  
1397 C  C   . PRO   B 93  ? 0.6540 0.7203 0.3364 0.1550  0.0943  0.1172  102 PRO   B C   
1398 O  O   . PRO   B 93  ? 0.6524 0.7293 0.3298 0.1601  0.0951  0.1253  102 PRO   B O   
1399 C  CB  . PRO   B 93  ? 0.6522 0.7142 0.3387 0.1413  0.0977  0.1094  102 PRO   B CB  
1400 C  CG  . PRO   B 93  ? 0.6491 0.7124 0.3245 0.1402  0.0965  0.1035  102 PRO   B CG  
1401 C  CD  . PRO   B 93  ? 0.6480 0.7150 0.3086 0.1497  0.0926  0.1026  102 PRO   B CD  
1402 N  N   . GLY   B 94  ? 0.6625 0.7227 0.3530 0.1549  0.0936  0.1167  103 GLY   B N   
1403 C  CA  . GLY   B 94  ? 0.6714 0.7356 0.3686 0.1592  0.0941  0.1265  103 GLY   B CA  
1404 C  C   . GLY   B 94  ? 0.6778 0.7503 0.3629 0.1695  0.0914  0.1303  103 GLY   B C   
1405 O  O   . GLY   B 94  ? 0.6918 0.7706 0.3811 0.1740  0.0919  0.1404  103 GLY   B O   
1406 N  N   . GLU   B 95  ? 0.6743 0.7473 0.3454 0.1735  0.0884  0.1231  104 GLU   B N   
1407 C  CA  . GLU   B 95  ? 0.6848 0.7664 0.3429 0.1838  0.0855  0.1254  104 GLU   B CA  
1408 C  C   . GLU   B 95  ? 0.6970 0.7711 0.3475 0.1862  0.0809  0.1152  104 GLU   B C   
1409 O  O   . GLU   B 95  ? 0.6593 0.7240 0.3106 0.1801  0.0801  0.1061  104 GLU   B O   
1410 C  CB  . GLU   B 95  ? 0.6835 0.7753 0.3312 0.1875  0.0859  0.1277  104 GLU   B CB  
1411 C  CG  . GLU   B 95  ? 0.6968 0.7972 0.3522 0.1847  0.0903  0.1382  104 GLU   B CG  
1412 C  CD  . GLU   B 95  ? 0.7178 0.8299 0.3632 0.1886  0.0909  0.1408  104 GLU   B CD  
1413 O  OE1 . GLU   B 95  ? 0.7225 0.8338 0.3555 0.1925  0.0877  0.1328  104 GLU   B OE1 
1414 O  OE2 . GLU   B 95  ? 0.7368 0.8594 0.3869 0.1880  0.0943  0.1510  104 GLU   B OE2 
1415 N  N   . ARG   B 96  ? 0.6878 0.7668 0.3312 0.1947  0.0780  0.1169  105 ARG   B N   
1416 C  CA  . ARG   B 96  ? 0.7124 0.7853 0.3482 0.1978  0.0731  0.1081  105 ARG   B CA  
1417 C  C   . ARG   B 96  ? 0.6948 0.7652 0.3184 0.1983  0.0699  0.0995  105 ARG   B C   
1418 O  O   . ARG   B 96  ? 0.6670 0.7447 0.2837 0.2010  0.0706  0.1018  105 ARG   B O   
1419 C  CB  . ARG   B 96  ? 0.7707 0.8515 0.4005 0.2076  0.0705  0.1126  105 ARG   B CB  
1420 C  CG  . ARG   B 96  ? 0.8314 0.9056 0.4573 0.2100  0.0658  0.1050  105 ARG   B CG  
1421 C  CD  . ARG   B 96  ? 0.8732 0.9512 0.5035 0.2149  0.0653  0.1110  105 ARG   B CD  
1422 N  NE  . ARG   B 96  ? 0.9182 1.0098 0.5403 0.2244  0.0645  0.1180  105 ARG   B NE  
1423 C  CZ  . ARG   B 96  ? 0.9759 1.0781 0.6016 0.2260  0.0681  0.1290  105 ARG   B CZ  
1424 N  NH1 . ARG   B 96  ? 1.0013 1.1011 0.6393 0.2187  0.0726  0.1343  105 ARG   B NH1 
1425 N  NH2 . ARG   B 96  ? 1.0166 1.1326 0.6339 0.2349  0.0671  0.1349  105 ARG   B NH2 
1426 N  N   . ALA   B 97  ? 0.6807 0.7415 0.3017 0.1959  0.0663  0.0900  106 ALA   B N   
1427 C  CA  . ALA   B 97  ? 0.6772 0.7343 0.2866 0.1967  0.0619  0.0817  106 ALA   B CA  
1428 C  C   . ALA   B 97  ? 0.6962 0.7623 0.2928 0.2076  0.0586  0.0835  106 ALA   B C   
1429 O  O   . ALA   B 97  ? 0.6660 0.7376 0.2616 0.2142  0.0577  0.0876  106 ALA   B O   
1430 C  CB  . ALA   B 97  ? 0.6859 0.7326 0.2955 0.1929  0.0582  0.0729  106 ALA   B CB  
1431 N  N   . LYS   B 98  ? 0.6812 0.7493 0.2685 0.2098  0.0568  0.0806  107 LYS   B N   
1432 C  CA  . LYS   B 98  ? 0.7073 0.7858 0.2828 0.2205  0.0543  0.0824  107 LYS   B CA  
1433 C  C   . LYS   B 98  ? 0.7015 0.7746 0.2665 0.2216  0.0491  0.0737  107 LYS   B C   
1434 O  O   . LYS   B 98  ? 0.6616 0.7306 0.2282 0.2150  0.0506  0.0715  107 LYS   B O   
1435 C  CB  . LYS   B 98  ? 0.7279 0.8190 0.3069 0.2221  0.0597  0.0924  107 LYS   B CB  
1436 C  CG  . LYS   B 98  ? 0.7790 0.8824 0.3465 0.2318  0.0581  0.0939  107 LYS   B CG  
1437 C  CD  . LYS   B 98  ? 0.7953 0.9119 0.3669 0.2321  0.0637  0.1041  107 LYS   B CD  
1438 C  CE  . LYS   B 98  ? 0.7890 0.9008 0.3676 0.2224  0.0675  0.1044  107 LYS   B CE  
1439 N  NZ  . LYS   B 98  ? 0.7861 0.9104 0.3604 0.2258  0.0696  0.1087  107 LYS   B NZ  
1440 N  N   . ASN   B 99  ? 0.6662 0.7383 0.2215 0.2289  0.0429  0.0684  108 ASN   B N   
1441 C  CA  . ASN   B 99  ? 0.6704 0.7379 0.2151 0.2315  0.0371  0.0605  108 ASN   B CA  
1442 C  C   . ASN   B 99  ? 0.6773 0.7562 0.2145 0.2390  0.0376  0.0632  108 ASN   B C   
1443 O  O   . ASN   B 99  ? 0.6409 0.7323 0.1724 0.2495  0.0371  0.0668  108 ASN   B O   
1444 C  CB  . ASN   B 99  ? 0.6748 0.7364 0.2120 0.2364  0.0296  0.0533  108 ASN   B CB  
1445 C  CG  . ASN   B 99  ? 0.7001 0.7505 0.2440 0.2287  0.0285  0.0498  108 ASN   B CG  
1446 O  OD1 . ASN   B 99  ? 0.7434 0.7957 0.2955 0.2268  0.0321  0.0543  108 ASN   B OD1 
1447 N  ND2 . ASN   B 99  ? 0.6982 0.7378 0.2384 0.2251  0.0228  0.0419  108 ASN   B ND2 
1448 N  N   . ILE   B 100 ? 0.6572 0.7331 0.1923 0.2357  0.0373  0.0604  109 ILE   B N   
1449 C  CA  . ILE   B 100 ? 0.6704 0.7562 0.1980 0.2425  0.0370  0.0614  109 ILE   B CA  
1450 C  C   . ILE   B 100 ? 0.6860 0.7634 0.2041 0.2452  0.0295  0.0520  109 ILE   B C   
1451 O  O   . ILE   B 100 ? 0.6589 0.7248 0.1795 0.2365  0.0282  0.0479  109 ILE   B O   
1452 C  CB  . ILE   B 100 ? 0.6880 0.7801 0.2223 0.2370  0.0439  0.0680  109 ILE   B CB  
1453 C  CG1 . ILE   B 100 ? 0.7097 0.8078 0.2550 0.2332  0.0506  0.0773  109 ILE   B CG1 
1454 C  CG2 . ILE   B 100 ? 0.6969 0.8019 0.2236 0.2452  0.0438  0.0698  109 ILE   B CG2 
1455 C  CD1 . ILE   B 100 ? 0.7195 0.8336 0.2616 0.2432  0.0521  0.0844  109 ILE   B CD1 
1456 N  N   . GLN   B 101 ? 0.6941 0.7782 0.2017 0.2569  0.0246  0.0490  110 GLN   B N   
1457 C  CA  . GLN   B 101 ? 0.7104 0.7858 0.2086 0.2608  0.0161  0.0395  110 GLN   B CA  
1458 C  C   . GLN   B 101 ? 0.7174 0.7990 0.2109 0.2645  0.0161  0.0391  110 GLN   B C   
1459 O  O   . GLN   B 101 ? 0.7066 0.8038 0.2004 0.2691  0.0215  0.0458  110 GLN   B O   
1460 C  CB  . GLN   B 101 ? 0.7363 0.8110 0.2269 0.2699  0.0094  0.0342  110 GLN   B CB  
1461 C  CG  . GLN   B 101 ? 0.7585 0.8266 0.2389 0.2763  0.0002  0.0248  110 GLN   B CG  
1462 C  CD  . GLN   B 101 ? 0.7709 0.8358 0.2454 0.2832  -0.0067 0.0191  110 GLN   B CD  
1463 O  OE1 . GLN   B 101 ? 0.7792 0.8456 0.2574 0.2821  -0.0047 0.0219  110 GLN   B OE1 
1464 N  NE2 . GLN   B 101 ? 0.8007 0.8610 0.2662 0.2904  -0.0153 0.0108  110 GLN   B NE2 
1465 N  N   . THR   B 102 ? 0.7109 0.7804 0.2023 0.2602  0.0113  0.0329  111 THR   B N   
1466 C  CA  . THR   B 102 ? 0.7223 0.7955 0.2106 0.2617  0.0113  0.0325  111 THR   B CA  
1467 C  C   . THR   B 102 ? 0.7099 0.7691 0.1924 0.2614  0.0025  0.0237  111 THR   B C   
1468 O  O   . THR   B 102 ? 0.7475 0.7934 0.2312 0.2561  -0.0019 0.0195  111 THR   B O   
1469 C  CB  . THR   B 102 ? 0.7182 0.7955 0.2161 0.2519  0.0201  0.0401  111 THR   B CB  
1470 O  OG1 . THR   B 102 ? 0.7291 0.8144 0.2236 0.2556  0.0208  0.0409  111 THR   B OG1 
1471 C  CG2 . THR   B 102 ? 0.7197 0.7831 0.2254 0.2383  0.0210  0.0389  111 THR   B CG2 
1472 N  N   . LEU   B 103 ? 0.7084 0.7713 0.1849 0.2677  -0.0005 0.0211  112 LEU   B N   
1473 C  CA  . LEU   B 103 ? 0.7069 0.7566 0.1795 0.2660  -0.0083 0.0141  112 LEU   B CA  
1474 C  C   . LEU   B 103 ? 0.6918 0.7395 0.1706 0.2555  -0.0037 0.0179  112 LEU   B C   
1475 O  O   . LEU   B 103 ? 0.6731 0.7329 0.1530 0.2573  0.0017  0.0226  112 LEU   B O   
1476 C  CB  . LEU   B 103 ? 0.7188 0.7728 0.1815 0.2791  -0.0150 0.0085  112 LEU   B CB  
1477 C  CG  . LEU   B 103 ? 0.7278 0.7670 0.1872 0.2774  -0.0238 0.0016  112 LEU   B CG  
1478 C  CD1 . LEU   B 103 ? 0.7249 0.7486 0.1821 0.2762  -0.0324 -0.0047 112 LEU   B CD1 
1479 C  CD2 . LEU   B 103 ? 0.7364 0.7825 0.1880 0.2896  -0.0284 -0.0024 112 LEU   B CD2 
1480 N  N   . PRO   B 104 ? 0.7023 0.7360 0.1859 0.2439  -0.0054 0.0162  113 PRO   B N   
1481 C  CA  . PRO   B 104 ? 0.6869 0.7192 0.1759 0.2340  -0.0014 0.0193  113 PRO   B CA  
1482 C  C   . PRO   B 104 ? 0.7011 0.7352 0.1844 0.2394  -0.0054 0.0169  113 PRO   B C   
1483 O  O   . PRO   B 104 ? 0.7071 0.7350 0.1829 0.2469  -0.0143 0.0106  113 PRO   B O   
1484 C  CB  . PRO   B 104 ? 0.6892 0.7065 0.1826 0.2222  -0.0044 0.0167  113 PRO   B CB  
1485 C  CG  . PRO   B 104 ? 0.6888 0.7016 0.1814 0.2244  -0.0072 0.0142  113 PRO   B CG  
1486 C  CD  . PRO   B 104 ? 0.6905 0.7107 0.1744 0.2395  -0.0109 0.0118  113 PRO   B CD  
1487 N  N   . GLY   B 105 ? 0.7158 0.7569 0.2037 0.2342  0.0007  0.0218  114 GLY   B N   
1488 C  CA  . GLY   B 105 ? 0.7169 0.7571 0.2018 0.2348  -0.0023 0.0202  114 GLY   B CA  
1489 C  C   . GLY   B 105 ? 0.7383 0.7648 0.2271 0.2223  -0.0050 0.0187  114 GLY   B C   
1490 O  O   . GLY   B 105 ? 0.7282 0.7432 0.2185 0.2165  -0.0084 0.0161  114 GLY   B O   
1491 N  N   . ILE   B 106 ? 0.7443 0.7724 0.2341 0.2186  -0.0042 0.0201  115 ILE   B N   
1492 C  CA  . ILE   B 106 ? 0.7426 0.7592 0.2353 0.2073  -0.0075 0.0189  115 ILE   B CA  
1493 C  C   . ILE   B 106 ? 0.7433 0.7676 0.2421 0.1989  0.0000  0.0242  115 ILE   B C   
1494 O  O   . ILE   B 106 ? 0.7257 0.7606 0.2227 0.2049  0.0024  0.0263  115 ILE   B O   
1495 C  CB  . ILE   B 106 ? 0.7773 0.7845 0.2627 0.2128  -0.0183 0.0134  115 ILE   B CB  
1496 C  CG1 . ILE   B 106 ? 0.8109 0.8113 0.2898 0.2225  -0.0264 0.0077  115 ILE   B CG1 
1497 C  CG2 . ILE   B 106 ? 0.7804 0.7758 0.2686 0.2010  -0.0224 0.0129  115 ILE   B CG2 
1498 C  CD1 . ILE   B 106 ? 0.8314 0.8204 0.3129 0.2150  -0.0290 0.0060  115 ILE   B CD1 
1499 N  N   . PHE   B 107 ? 0.7288 0.7475 0.2344 0.1855  0.0026  0.0255  116 PHE   B N   
1500 C  CA  . PHE   B 107 ? 0.7432 0.7640 0.2538 0.1753  0.0063  0.0283  116 PHE   B CA  
1501 C  C   . PHE   B 107 ? 0.7370 0.7476 0.2435 0.1731  -0.0024 0.0250  116 PHE   B C   
1502 O  O   . PHE   B 107 ? 0.7232 0.7221 0.2286 0.1694  -0.0085 0.0218  116 PHE   B O   
1503 C  CB  . PHE   B 107 ? 0.7108 0.7307 0.2303 0.1627  0.0126  0.0303  116 PHE   B CB  
1504 C  CG  . PHE   B 107 ? 0.7199 0.7505 0.2457 0.1623  0.0222  0.0349  116 PHE   B CG  
1505 C  CD1 . PHE   B 107 ? 0.7176 0.7587 0.2409 0.1726  0.0250  0.0376  116 PHE   B CD1 
1506 C  CD2 . PHE   B 107 ? 0.7038 0.7343 0.2384 0.1514  0.0281  0.0364  116 PHE   B CD2 
1507 C  CE1 . PHE   B 107 ? 0.7097 0.7606 0.2397 0.1711  0.0335  0.0427  116 PHE   B CE1 
1508 C  CE2 . PHE   B 107 ? 0.7070 0.7462 0.2483 0.1506  0.0363  0.0407  116 PHE   B CE2 
1509 C  CZ  . PHE   B 107 ? 0.6963 0.7454 0.2354 0.1602  0.0388  0.0442  116 PHE   B CZ  
1510 N  N   . LYS   B 108 ? 0.7650 0.7802 0.2689 0.1765  -0.0036 0.0258  117 LYS   B N   
1511 C  CA  . LYS   B 108 ? 0.8029 0.8092 0.3038 0.1738  -0.0117 0.0238  117 LYS   B CA  
1512 C  C   . LYS   B 108 ? 0.7596 0.7683 0.2670 0.1602  -0.0068 0.0272  117 LYS   B C   
1513 O  O   . LYS   B 108 ? 0.7328 0.7529 0.2435 0.1592  0.0004  0.0309  117 LYS   B O   
1514 C  CB  . LYS   B 108 ? 0.8594 0.8689 0.3536 0.1860  -0.0168 0.0221  117 LYS   B CB  
1515 C  CG  . LYS   B 108 ? 0.9345 0.9355 0.4214 0.1974  -0.0262 0.0164  117 LYS   B CG  
1516 C  CD  . LYS   B 108 ? 1.0101 1.0177 0.4905 0.2121  -0.0296 0.0141  117 LYS   B CD  
1517 C  CE  . LYS   B 108 ? 1.0902 1.0862 0.5637 0.2217  -0.0414 0.0074  117 LYS   B CE  
1518 N  NZ  . LYS   B 108 ? 1.1417 1.1463 0.6088 0.2381  -0.0433 0.0040  117 LYS   B NZ  
1519 N  N   . THR   B 109 ? 0.7709 0.7699 0.2801 0.1502  -0.0107 0.0262  118 THR   B N   
1520 C  CA  . THR   B 109 ? 0.7648 0.7663 0.2802 0.1365  -0.0064 0.0289  118 THR   B CA  
1521 C  C   . THR   B 109 ? 0.7713 0.7642 0.2842 0.1317  -0.0149 0.0283  118 THR   B C   
1522 O  O   . THR   B 109 ? 0.7384 0.7201 0.2463 0.1360  -0.0243 0.0253  118 THR   B O   
1523 C  CB  . THR   B 109 ? 0.7659 0.7665 0.2879 0.1261  -0.0013 0.0291  118 THR   B CB  
1524 O  OG1 . THR   B 109 ? 0.7610 0.7506 0.2819 0.1202  -0.0085 0.0268  118 THR   B OG1 
1525 C  CG2 . THR   B 109 ? 0.7589 0.7630 0.2826 0.1315  0.0038  0.0288  118 THR   B CG2 
1526 N  N   . LYS   B 110 ? 0.7889 0.7865 0.3056 0.1222  -0.0119 0.0310  119 LYS   B N   
1527 C  CA  . LYS   B 110 ? 0.8526 0.8437 0.3678 0.1160  -0.0193 0.0316  119 LYS   B CA  
1528 C  C   . LYS   B 110 ? 0.8738 0.8540 0.3893 0.1089  -0.0251 0.0300  119 LYS   B C   
1529 O  O   . LYS   B 110 ? 0.8471 0.8195 0.3603 0.1058  -0.0334 0.0304  119 LYS   B O   
1530 C  CB  . LYS   B 110 ? 0.8296 0.8299 0.3497 0.1060  -0.0135 0.0350  119 LYS   B CB  
1531 C  CG  . LYS   B 110 ? 0.8722 0.8776 0.3996 0.0941  -0.0056 0.0357  119 LYS   B CG  
1532 C  CD  . LYS   B 110 ? 0.8826 0.8986 0.4148 0.0854  0.0005  0.0386  119 LYS   B CD  
1533 C  CE  . LYS   B 110 ? 0.9347 0.9499 0.4702 0.0717  -0.0005 0.0391  119 LYS   B CE  
1534 N  NZ  . LYS   B 110 ? 0.9289 0.9447 0.4697 0.0647  0.0044  0.0372  119 LYS   B NZ  
1535 N  N   . ASP   B 111 ? 0.8620 0.8416 0.3805 0.1066  -0.0212 0.0285  120 ASP   B N   
1536 C  CA  . ASP   B 111 ? 0.8615 0.8321 0.3807 0.0997  -0.0263 0.0271  120 ASP   B CA  
1537 C  C   . ASP   B 111 ? 0.8542 0.8165 0.3691 0.1094  -0.0316 0.0236  120 ASP   B C   
1538 O  O   . ASP   B 111 ? 0.8534 0.8091 0.3694 0.1042  -0.0349 0.0223  120 ASP   B O   
1539 C  CB  . ASP   B 111 ? 0.8673 0.8440 0.3938 0.0880  -0.0185 0.0277  120 ASP   B CB  
1540 C  CG  . ASP   B 111 ? 0.8738 0.8574 0.4041 0.0771  -0.0154 0.0305  120 ASP   B CG  
1541 O  OD1 . ASP   B 111 ? 0.8867 0.8654 0.4155 0.0710  -0.0222 0.0317  120 ASP   B OD1 
1542 O  OD2 . ASP   B 111 ? 0.8548 0.8484 0.3890 0.0757  -0.0069 0.0316  120 ASP   B OD2 
1543 N  N   . GLY   B 112 ? 0.8154 0.7787 0.3257 0.1227  -0.0323 0.0221  121 GLY   B N   
1544 C  CA  . GLY   B 112 ? 0.8331 0.7884 0.3386 0.1324  -0.0385 0.0183  121 GLY   B CA  
1545 C  C   . GLY   B 112 ? 0.7981 0.7618 0.3036 0.1411  -0.0311 0.0178  121 GLY   B C   
1546 O  O   . GLY   B 112 ? 0.7613 0.7361 0.2709 0.1392  -0.0220 0.0207  121 GLY   B O   
1547 N  N   . ASP   B 113 ? 0.8178 0.7770 0.3191 0.1507  -0.0353 0.0144  122 ASP   B N   
1548 C  CA  . ASP   B 113 ? 0.8296 0.7977 0.3300 0.1606  -0.0292 0.0143  122 ASP   B CA  
1549 C  C   . ASP   B 113 ? 0.8316 0.7996 0.3359 0.1569  -0.0250 0.0140  122 ASP   B C   
1550 O  O   . ASP   B 113 ? 0.8106 0.7688 0.3148 0.1525  -0.0308 0.0117  122 ASP   B O   
1551 C  CB  . ASP   B 113 ? 0.8685 0.8340 0.3608 0.1754  -0.0365 0.0105  122 ASP   B CB  
1552 C  CG  . ASP   B 113 ? 0.9027 0.8696 0.3916 0.1800  -0.0401 0.0106  122 ASP   B CG  
1553 O  OD1 . ASP   B 113 ? 0.9215 0.8930 0.4143 0.1719  -0.0360 0.0143  122 ASP   B OD1 
1554 O  OD2 . ASP   B 113 ? 0.9960 0.9598 0.4785 0.1915  -0.0472 0.0068  122 ASP   B OD2 
1555 N  N   . ILE   B 114 ? 0.7808 0.7595 0.2885 0.1594  -0.0158 0.0165  123 ILE   B N   
1556 C  CA  . ILE   B 114 ? 0.7712 0.7520 0.2834 0.1574  -0.0105 0.0169  123 ILE   B CA  
1557 C  C   . ILE   B 114 ? 0.7247 0.7125 0.2332 0.1706  -0.0086 0.0170  123 ILE   B C   
1558 O  O   . ILE   B 114 ? 0.7107 0.7069 0.2170 0.1770  -0.0062 0.0189  123 ILE   B O   
1559 C  CB  . ILE   B 114 ? 0.7739 0.7618 0.2952 0.1466  -0.0008 0.0206  123 ILE   B CB  
1560 C  CG1 . ILE   B 114 ? 0.8461 0.8321 0.3699 0.1356  -0.0015 0.0214  123 ILE   B CG1 
1561 C  CG2 . ILE   B 114 ? 0.8133 0.7998 0.3399 0.1419  0.0023  0.0200  123 ILE   B CG2 
1562 C  CD1 . ILE   B 114 ? 0.8451 0.8401 0.3771 0.1268  0.0079  0.0246  123 ILE   B CD1 
1563 N  N   . GLY   B 115 ? 0.7309 0.7166 0.2391 0.1740  -0.0093 0.0154  124 GLY   B N   
1564 C  CA  . GLY   B 115 ? 0.7204 0.7144 0.2262 0.1851  -0.0063 0.0164  124 GLY   B CA  
1565 C  C   . GLY   B 115 ? 0.7111 0.7167 0.2238 0.1820  0.0043  0.0221  124 GLY   B C   
1566 O  O   . GLY   B 115 ? 0.6617 0.6666 0.1820 0.1705  0.0091  0.0240  124 GLY   B O   
1567 N  N   . ALA   B 116 ? 0.6694 0.6857 0.1797 0.1916  0.0076  0.0246  125 ALA   B N   
1568 C  CA  . ALA   B 116 ? 0.6698 0.6984 0.1865 0.1901  0.0173  0.0309  125 ALA   B CA  
1569 C  C   . ALA   B 116 ? 0.6815 0.7179 0.1961 0.2001  0.0192  0.0328  125 ALA   B C   
1570 O  O   . ALA   B 116 ? 0.6888 0.7259 0.1950 0.2112  0.0134  0.0296  125 ALA   B O   
1571 C  CB  . ALA   B 116 ? 0.6752 0.7121 0.1907 0.1919  0.0195  0.0335  125 ALA   B CB  
1572 N  N   A VAL   B 117 ? 0.6803 0.7231 0.2025 0.1966  0.0268  0.0380  126 VAL   B N   
1573 N  N   B VAL   B 117 ? 0.6670 0.7094 0.1893 0.1964  0.0268  0.0379  126 VAL   B N   
1574 N  N   C VAL   B 117 ? 0.6806 0.7235 0.2029 0.1966  0.0268  0.0380  126 VAL   B N   
1575 N  N   D VAL   B 117 ? 0.6660 0.7084 0.1884 0.1964  0.0267  0.0379  126 VAL   B N   
1576 C  CA  A VAL   B 117 ? 0.6854 0.7366 0.2073 0.2047  0.0295  0.0413  126 VAL   B CA  
1577 C  CA  B VAL   B 117 ? 0.6638 0.7151 0.1863 0.2041  0.0298  0.0415  126 VAL   B CA  
1578 C  CA  C VAL   B 117 ? 0.6856 0.7368 0.2076 0.2046  0.0295  0.0413  126 VAL   B CA  
1579 C  CA  D VAL   B 117 ? 0.6609 0.7121 0.1834 0.2041  0.0298  0.0415  126 VAL   B CA  
1580 C  C   A VAL   B 117 ? 0.6785 0.7439 0.2051 0.2053  0.0374  0.0489  126 VAL   B C   
1581 C  C   B VAL   B 117 ? 0.6654 0.7309 0.1919 0.2051  0.0373  0.0488  126 VAL   B C   
1582 C  C   C VAL   B 117 ? 0.6801 0.7454 0.2067 0.2053  0.0374  0.0488  126 VAL   B C   
1583 C  C   D VAL   B 117 ? 0.6657 0.7310 0.1921 0.2051  0.0374  0.0488  126 VAL   B C   
1584 O  O   A VAL   B 117 ? 0.6689 0.7346 0.2047 0.1955  0.0433  0.0524  126 VAL   B O   
1585 O  O   B VAL   B 117 ? 0.6546 0.7204 0.1895 0.1954  0.0429  0.0521  126 VAL   B O   
1586 O  O   C VAL   B 117 ? 0.6690 0.7346 0.2047 0.1956  0.0433  0.0524  126 VAL   B O   
1587 O  O   D VAL   B 117 ? 0.6534 0.7193 0.1883 0.1955  0.0429  0.0521  126 VAL   B O   
1588 C  CB  A VAL   B 117 ? 0.6922 0.7371 0.2195 0.2001  0.0304  0.0408  126 VAL   B CB  
1589 C  CB  B VAL   B 117 ? 0.6561 0.7017 0.1850 0.1987  0.0317  0.0417  126 VAL   B CB  
1590 C  CB  C VAL   B 117 ? 0.6951 0.7400 0.2224 0.2000  0.0304  0.0408  126 VAL   B CB  
1591 C  CB  D VAL   B 117 ? 0.6533 0.6989 0.1823 0.1986  0.0317  0.0417  126 VAL   B CB  
1592 C  CG1 A VAL   B 117 ? 0.7028 0.7381 0.2231 0.2046  0.0220  0.0342  126 VAL   B CG1 
1593 C  CG1 B VAL   B 117 ? 0.6557 0.7106 0.1857 0.2058  0.0351  0.0464  126 VAL   B CG1 
1594 C  CG1 C VAL   B 117 ? 0.7074 0.7427 0.2276 0.2046  0.0219  0.0342  126 VAL   B CG1 
1595 C  CG1 D VAL   B 117 ? 0.6532 0.7081 0.1831 0.2058  0.0351  0.0463  126 VAL   B CG1 
1596 C  CG2 A VAL   B 117 ? 0.6914 0.7301 0.2283 0.1864  0.0343  0.0412  126 VAL   B CG2 
1597 C  CG2 B VAL   B 117 ? 0.6573 0.6898 0.1823 0.1974  0.0241  0.0348  126 VAL   B CG2 
1598 C  CG2 C VAL   B 117 ? 0.6993 0.7380 0.2362 0.1864  0.0342  0.0412  126 VAL   B CG2 
1599 C  CG2 D VAL   B 117 ? 0.6535 0.6860 0.1785 0.1974  0.0241  0.0348  126 VAL   B CG2 
1600 N  N   . ALA   B 118 ? 0.6718 0.7490 0.1924 0.2164  0.0372  0.0510  127 ALA   B N   
1601 C  CA  . ALA   B 118 ? 0.6811 0.7736 0.2049 0.2182  0.0439  0.0585  127 ALA   B CA  
1602 C  C   . ALA   B 118 ? 0.7012 0.8027 0.2289 0.2215  0.0486  0.0649  127 ALA   B C   
1603 O  O   . ALA   B 118 ? 0.7219 0.8339 0.2432 0.2324  0.0474  0.0661  127 ALA   B O   
1604 C  CB  . ALA   B 118 ? 0.6841 0.7858 0.1987 0.2288  0.0407  0.0570  127 ALA   B CB  
1605 N  N   . LEU   B 119 ? 0.7013 0.7993 0.2392 0.2127  0.0534  0.0685  128 LEU   B N   
1606 C  CA  . LEU   B 119 ? 0.6846 0.7902 0.2280 0.2145  0.0580  0.0755  128 LEU   B CA  
1607 C  C   . LEU   B 119 ? 0.7150 0.8229 0.2707 0.2043  0.0653  0.0822  128 LEU   B C   
1608 O  O   . LEU   B 119 ? 0.7128 0.8108 0.2737 0.1945  0.0659  0.0789  128 LEU   B O   
1609 C  CB  . LEU   B 119 ? 0.6688 0.7639 0.2118 0.2146  0.0544  0.0712  128 LEU   B CB  
1610 C  CG  . LEU   B 119 ? 0.6751 0.7685 0.2063 0.2251  0.0469  0.0649  128 LEU   B CG  
1611 C  CD1 . LEU   B 119 ? 0.6609 0.7431 0.1920 0.2241  0.0429  0.0601  128 LEU   B CD1 
1612 C  CD2 . LEU   B 119 ? 0.6862 0.7961 0.2122 0.2366  0.0480  0.0698  128 LEU   B CD2 
1613 N  N   . ASP   B 120 ? 0.7137 0.8345 0.2741 0.2062  0.0704  0.0911  129 ASP   B N   
1614 C  CA  . ASP   B 120 ? 0.7395 0.8634 0.3120 0.1969  0.0770  0.0979  129 ASP   B CA  
1615 C  C   . ASP   B 120 ? 0.7325 0.8513 0.3154 0.1917  0.0799  0.1013  129 ASP   B C   
1616 O  O   . ASP   B 120 ? 0.7101 0.8376 0.2951 0.1963  0.0820  0.1085  129 ASP   B O   
1617 C  CB  . ASP   B 120 ? 0.7768 0.9184 0.3502 0.2010  0.0812  0.1072  129 ASP   B CB  
1618 C  CG  . ASP   B 120 ? 0.8056 0.9560 0.3705 0.2064  0.0797  0.1057  129 ASP   B CG  
1619 O  OD1 . ASP   B 120 ? 0.8320 0.9737 0.3934 0.2032  0.0767  0.0986  129 ASP   B OD1 
1620 O  OD2 . ASP   B 120 ? 0.8330 0.9999 0.3951 0.2136  0.0816  0.1122  129 ASP   B OD2 
1621 N  N   . TYR   B 121 ? 0.6809 0.7867 0.2706 0.1825  0.0800  0.0967  130 TYR   B N   
1622 C  CA  . TYR   B 121 ? 0.6741 0.7744 0.2756 0.1764  0.0831  0.0994  130 TYR   B CA  
1623 C  C   . TYR   B 121 ? 0.6744 0.7710 0.2870 0.1649  0.0873  0.1000  130 TYR   B C   
1624 O  O   . TYR   B 121 ? 0.6687 0.7648 0.2788 0.1612  0.0871  0.0966  130 TYR   B O   
1625 C  CB  . TYR   B 121 ? 0.6666 0.7552 0.2658 0.1766  0.0789  0.0920  130 TYR   B CB  
1626 C  CG  . TYR   B 121 ? 0.6776 0.7700 0.2683 0.1873  0.0753  0.0925  130 TYR   B CG  
1627 C  CD1 . TYR   B 121 ? 0.7008 0.7979 0.2968 0.1903  0.0774  0.0991  130 TYR   B CD1 
1628 C  CD2 . TYR   B 121 ? 0.6925 0.7846 0.2704 0.1948  0.0697  0.0867  130 TYR   B CD2 
1629 C  CE1 . TYR   B 121 ? 0.7021 0.8037 0.2906 0.2001  0.0742  0.0996  130 TYR   B CE1 
1630 C  CE2 . TYR   B 121 ? 0.7162 0.8129 0.2866 0.2050  0.0664  0.0869  130 TYR   B CE2 
1631 C  CZ  . TYR   B 121 ? 0.7223 0.8242 0.2978 0.2076  0.0688  0.0934  130 TYR   B CZ  
1632 O  OH  . TYR   B 121 ? 0.7120 0.8196 0.2802 0.2176  0.0657  0.0940  130 TYR   B OH  
1633 N  N   . PRO   B 122 ? 0.6728 0.7682 0.2982 0.1594  0.0913  0.1048  131 PRO   B N   
1634 C  CA  . PRO   B 122 ? 0.6912 0.7834 0.3278 0.1487  0.0951  0.1049  131 PRO   B CA  
1635 C  C   . PRO   B 122 ? 0.6469 0.7265 0.2850 0.1413  0.0932  0.0948  131 PRO   B C   
1636 O  O   . PRO   B 122 ? 0.6305 0.7038 0.2631 0.1442  0.0895  0.0894  131 PRO   B O   
1637 C  CB  . PRO   B 122 ? 0.6900 0.7835 0.3393 0.1464  0.0986  0.1126  131 PRO   B CB  
1638 C  CG  . PRO   B 122 ? 0.6868 0.7801 0.3323 0.1544  0.0961  0.1139  131 PRO   B CG  
1639 C  CD  . PRO   B 122 ? 0.6842 0.7820 0.3141 0.1635  0.0921  0.1108  131 PRO   B CD  
1640 N  N   . ALA   B 123 ? 0.6882 0.7651 0.3335 0.1320  0.0957  0.0926  132 ALA   B N   
1641 C  CA  . ALA   B 123 ? 0.6595 0.7268 0.3052 0.1249  0.0940  0.0830  132 ALA   B CA  
1642 C  C   . ALA   B 123 ? 0.6504 0.7090 0.3000 0.1238  0.0925  0.0784  132 ALA   B C   
1643 O  O   . ALA   B 123 ? 0.6457 0.6975 0.2912 0.1211  0.0894  0.0703  132 ALA   B O   
1644 C  CB  . ALA   B 123 ? 0.6633 0.7306 0.3178 0.1148  0.0976  0.0819  132 ALA   B CB  
1645 N  N   . GLY   B 124 ? 0.6149 0.6734 0.2735 0.1248  0.0946  0.0830  133 GLY   B N   
1646 C  CA  . GLY   B 124 ? 0.6051 0.6561 0.2692 0.1239  0.0936  0.0791  133 GLY   B CA  
1647 C  C   . GLY   B 124 ? 0.5998 0.6483 0.2531 0.1310  0.0888  0.0759  133 GLY   B C   
1648 O  O   . GLY   B 124 ? 0.5925 0.6348 0.2495 0.1299  0.0875  0.0716  133 GLY   B O   
1649 N  N   . THR   B 125 ? 0.5867 0.6402 0.2278 0.1383  0.0862  0.0776  134 THR   B N   
1650 C  CA  . THR   B 125 ? 0.5889 0.6399 0.2186 0.1453  0.0808  0.0736  134 THR   B CA  
1651 C  C   . THR   B 125 ? 0.5821 0.6261 0.2058 0.1409  0.0770  0.0647  134 THR   B C   
1652 O  O   . THR   B 125 ? 0.5744 0.6142 0.1900 0.1451  0.0720  0.0604  134 THR   B O   
1653 C  CB  . THR   B 125 ? 0.6056 0.6656 0.2256 0.1554  0.0795  0.0791  134 THR   B CB  
1654 O  OG1 . THR   B 125 ? 0.6093 0.6774 0.2365 0.1568  0.0840  0.0884  134 THR   B OG1 
1655 C  CG2 . THR   B 125 ? 0.6322 0.6917 0.2437 0.1645  0.0750  0.0778  134 THR   B CG2 
1656 N  N   . SER   B 126 ? 0.5766 0.6196 0.2044 0.1324  0.0792  0.0623  135 SER   B N   
1657 C  CA  . SER   B 126 ? 0.5732 0.6107 0.1968 0.1263  0.0763  0.0548  135 SER   B CA  
1658 C  C   . SER   B 126 ? 0.5574 0.5876 0.1812 0.1248  0.0730  0.0488  135 SER   B C   
1659 O  O   . SER   B 126 ? 0.5605 0.5888 0.1938 0.1218  0.0754  0.0484  135 SER   B O   
1660 C  CB  . SER   B 126 ? 0.5844 0.6225 0.2159 0.1165  0.0801  0.0534  135 SER   B CB  
1661 O  OG  . SER   B 126 ? 0.5932 0.6377 0.2229 0.1166  0.0821  0.0575  135 SER   B OG  
1662 N  N   . GLY   B 127 ? 0.5535 0.5797 0.1675 0.1268  0.0673  0.0444  136 GLY   B N   
1663 C  CA  . GLY   B 127 ? 0.5570 0.5766 0.1708 0.1246  0.0637  0.0387  136 GLY   B CA  
1664 C  C   . GLY   B 127 ? 0.5645 0.5829 0.1728 0.1336  0.0600  0.0396  136 GLY   B C   
1665 O  O   . GLY   B 127 ? 0.5640 0.5772 0.1715 0.1324  0.0564  0.0350  136 GLY   B O   
1666 N  N   . SER   B 128 ? 0.5651 0.5891 0.1702 0.1422  0.0610  0.0454  137 SER   B N   
1667 C  CA  . SER   B 128 ? 0.5621 0.5860 0.1606 0.1515  0.0570  0.0459  137 SER   B CA  
1668 C  C   . SER   B 128 ? 0.5585 0.5772 0.1459 0.1536  0.0498  0.0404  137 SER   B C   
1669 O  O   . SER   B 128 ? 0.5812 0.5999 0.1630 0.1529  0.0480  0.0393  137 SER   B O   
1670 C  CB  . SER   B 128 ? 0.5627 0.5954 0.1584 0.1610  0.0588  0.0531  137 SER   B CB  
1671 O  OG  . SER   B 128 ? 0.5834 0.6207 0.1900 0.1589  0.0650  0.0593  137 SER   B OG  
1672 N  N   . PRO   B 129 ? 0.5659 0.5800 0.1501 0.1565  0.0451  0.0369  138 PRO   B N   
1673 C  CA  . PRO   B 129 ? 0.5611 0.5692 0.1359 0.1578  0.0376  0.0316  138 PRO   B CA  
1674 C  C   . PRO   B 129 ? 0.5943 0.6046 0.1577 0.1685  0.0330  0.0321  138 PRO   B C   
1675 O  O   . PRO   B 129 ? 0.5895 0.6063 0.1516 0.1769  0.0346  0.0361  138 PRO   B O   
1676 C  CB  . PRO   B 129 ? 0.5788 0.5821 0.1557 0.1567  0.0348  0.0282  138 PRO   B CB  
1677 C  CG  . PRO   B 129 ? 0.5766 0.5852 0.1602 0.1608  0.0395  0.0329  138 PRO   B CG  
1678 C  CD  . PRO   B 129 ? 0.5696 0.5836 0.1604 0.1574  0.0466  0.0378  138 PRO   B CD  
1679 N  N   . ILE   B 130 ? 0.5835 0.5884 0.1392 0.1683  0.0270  0.0278  139 ILE   B N   
1680 C  CA  . ILE   B 130 ? 0.6073 0.6125 0.1516 0.1784  0.0209  0.0263  139 ILE   B CA  
1681 C  C   . ILE   B 130 ? 0.6338 0.6306 0.1730 0.1800  0.0128  0.0207  139 ILE   B C   
1682 O  O   . ILE   B 130 ? 0.6210 0.6112 0.1634 0.1715  0.0111  0.0178  139 ILE   B O   
1683 C  CB  . ILE   B 130 ? 0.5965 0.6021 0.1365 0.1777  0.0198  0.0260  139 ILE   B CB  
1684 C  CG1 . ILE   B 130 ? 0.6044 0.6190 0.1505 0.1756  0.0280  0.0319  139 ILE   B CG1 
1685 C  CG2 . ILE   B 130 ? 0.6187 0.6240 0.1476 0.1881  0.0130  0.0234  139 ILE   B CG2 
1686 C  CD1 . ILE   B 130 ? 0.6080 0.6218 0.1536 0.1700  0.0283  0.0314  139 ILE   B CD1 
1687 N  N   . LEU   B 131 ? 0.6453 0.6444 0.1787 0.1903  0.0095  0.0202  140 LEU   B N   
1688 C  CA  . LEU   B 131 ? 0.6792 0.6712 0.2083 0.1927  0.0020  0.0152  140 LEU   B CA  
1689 C  C   . LEU   B 131 ? 0.6854 0.6740 0.2032 0.2014  -0.0066 0.0107  140 LEU   B C   
1690 O  O   . LEU   B 131 ? 0.6792 0.6746 0.1913 0.2101  -0.0062 0.0121  140 LEU   B O   
1691 C  CB  . LEU   B 131 ? 0.6977 0.6949 0.2288 0.1984  0.0040  0.0173  140 LEU   B CB  
1692 C  CG  . LEU   B 131 ? 0.7051 0.7089 0.2467 0.1946  0.0130  0.0232  140 LEU   B CG  
1693 C  CD1 . LEU   B 131 ? 0.7228 0.7304 0.2660 0.2001  0.0136  0.0250  140 LEU   B CD1 
1694 C  CD2 . LEU   B 131 ? 0.7136 0.7122 0.2643 0.1817  0.0161  0.0222  140 LEU   B CD2 
1695 N  N   . ASP   B 132 ? 0.7004 0.6790 0.2152 0.1991  -0.0145 0.0054  141 ASP   B N   
1696 C  CA  . ASP   B 132 ? 0.7560 0.7299 0.2608 0.2078  -0.0240 0.0002  141 ASP   B CA  
1697 C  C   . ASP   B 132 ? 0.7657 0.7424 0.2676 0.2161  -0.0264 -0.0011 141 ASP   B C   
1698 O  O   . ASP   B 132 ? 0.7372 0.7196 0.2452 0.2145  -0.0202 0.0026  141 ASP   B O   
1699 C  CB  . ASP   B 132 ? 0.7592 0.7206 0.2622 0.2011  -0.0321 -0.0043 141 ASP   B CB  
1700 C  CG  . ASP   B 132 ? 0.7787 0.7328 0.2857 0.1933  -0.0355 -0.0065 141 ASP   B CG  
1701 O  OD1 . ASP   B 132 ? 0.7696 0.7270 0.2792 0.1951  -0.0334 -0.0060 141 ASP   B OD1 
1702 O  OD2 . ASP   B 132 ? 0.8046 0.7503 0.3126 0.1846  -0.0399 -0.0083 141 ASP   B OD2 
1703 N  N   . LYS   B 133 ? 0.8146 0.7864 0.3083 0.2235  -0.0355 -0.0066 142 LYS   B N   
1704 C  CA  . LYS   B 133 ? 0.8553 0.8316 0.3449 0.2332  -0.0380 -0.0083 142 LYS   B CA  
1705 C  C   . LYS   B 133 ? 0.8646 0.8348 0.3587 0.2270  -0.0404 -0.0099 142 LYS   B C   
1706 O  O   . LYS   B 133 ? 0.8867 0.8619 0.3799 0.2329  -0.0403 -0.0097 142 LYS   B O   
1707 C  CB  . LYS   B 133 ? 0.9171 0.8913 0.3960 0.2445  -0.0471 -0.0143 142 LYS   B CB  
1708 C  CG  . LYS   B 133 ? 0.9733 0.9579 0.4474 0.2535  -0.0439 -0.0125 142 LYS   B CG  
1709 C  CD  . LYS   B 133 ? 1.0205 1.0017 0.4850 0.2629  -0.0528 -0.0191 142 LYS   B CD  
1710 C  CE  . LYS   B 133 ? 1.0499 1.0427 0.5113 0.2700  -0.0482 -0.0163 142 LYS   B CE  
1711 N  NZ  . LYS   B 133 ? 1.0698 1.0604 0.5221 0.2800  -0.0567 -0.0231 142 LYS   B NZ  
1712 N  N   . CYS   B 134 ? 0.8649 0.8255 0.3635 0.2156  -0.0426 -0.0113 143 CYS   B N   
1713 C  CA  . CYS   B 134 ? 0.8587 0.8149 0.3629 0.2082  -0.0439 -0.0123 143 CYS   B CA  
1714 C  C   . CYS   B 134 ? 0.8033 0.7662 0.3177 0.2015  -0.0336 -0.0068 143 CYS   B C   
1715 O  O   . CYS   B 134 ? 0.7983 0.7594 0.3180 0.1960  -0.0337 -0.0074 143 CYS   B O   
1716 C  CB  . CYS   B 134 ? 0.8950 0.8394 0.3994 0.1992  -0.0511 -0.0159 143 CYS   B CB  
1717 S  SG  . CYS   B 134 ? 0.9561 0.8905 0.4504 0.2066  -0.0651 -0.0232 143 CYS   B SG  
1718 N  N   . GLY   B 135 ? 0.7722 0.7436 0.2892 0.2034  -0.0254 -0.0018 144 GLY   B N   
1719 C  CA  . GLY   B 135 ? 0.7631 0.7401 0.2904 0.1970  -0.0159 0.0032  144 GLY   B CA  
1720 C  C   . GLY   B 135 ? 0.7447 0.7177 0.2787 0.1844  -0.0129 0.0034  144 GLY   B C   
1721 O  O   . GLY   B 135 ? 0.7076 0.6844 0.2509 0.1783  -0.0056 0.0065  144 GLY   B O   
1722 N  N   . ARG   B 136 ? 0.7276 0.6931 0.2575 0.1802  -0.0185 0.0002  145 ARG   B N   
1723 C  CA  . ARG   B 136 ? 0.7348 0.6973 0.2706 0.1679  -0.0162 0.0004  145 ARG   B CA  
1724 C  C   . ARG   B 136 ? 0.6925 0.6603 0.2305 0.1666  -0.0093 0.0042  145 ARG   B C   
1725 O  O   . ARG   B 136 ? 0.6793 0.6497 0.2113 0.1741  -0.0097 0.0053  145 ARG   B O   
1726 C  CB  . ARG   B 136 ? 0.7570 0.7098 0.2879 0.1636  -0.0253 -0.0036 145 ARG   B CB  
1727 C  CG  . ARG   B 136 ? 0.7772 0.7247 0.3082 0.1615  -0.0318 -0.0070 145 ARG   B CG  
1728 C  CD  . ARG   B 136 ? 0.8227 0.7604 0.3481 0.1589  -0.0417 -0.0105 145 ARG   B CD  
1729 N  NE  . ARG   B 136 ? 0.9258 0.8613 0.4423 0.1695  -0.0465 -0.0120 145 ARG   B NE  
1730 C  CZ  . ARG   B 136 ? 0.9683 0.8957 0.4789 0.1701  -0.0546 -0.0146 145 ARG   B CZ  
1731 N  NH1 . ARG   B 136 ? 1.0109 0.9314 0.5237 0.1597  -0.0589 -0.0150 145 ARG   B NH1 
1732 N  NH2 . ARG   B 136 ? 0.9945 0.9212 0.4972 0.1815  -0.0587 -0.0166 145 ARG   B NH2 
1733 N  N   . VAL   B 137 ? 0.6783 0.6478 0.2249 0.1565  -0.0035 0.0056  146 VAL   B N   
1734 C  CA  . VAL   B 137 ? 0.6717 0.6465 0.2217 0.1540  0.0033  0.0092  146 VAL   B CA  
1735 C  C   . VAL   B 137 ? 0.6829 0.6529 0.2282 0.1498  -0.0009 0.0075  146 VAL   B C   
1736 O  O   . VAL   B 137 ? 0.6890 0.6538 0.2359 0.1409  -0.0043 0.0051  146 VAL   B O   
1737 C  CB  . VAL   B 137 ? 0.6507 0.6295 0.2120 0.1453  0.0112  0.0109  146 VAL   B CB  
1738 C  CG1 . VAL   B 137 ? 0.6440 0.6279 0.2085 0.1431  0.0177  0.0144  146 VAL   B CG1 
1739 C  CG2 . VAL   B 137 ? 0.6453 0.6279 0.2115 0.1498  0.0145  0.0126  146 VAL   B CG2 
1740 N  N   . ILE   B 138 ? 0.6614 0.6335 0.2010 0.1563  -0.0012 0.0090  147 ILE   B N   
1741 C  CA  . ILE   B 138 ? 0.6437 0.6116 0.1782 0.1542  -0.0057 0.0078  147 ILE   B CA  
1742 C  C   . ILE   B 138 ? 0.6183 0.5918 0.1581 0.1480  0.0015  0.0111  147 ILE   B C   
1743 O  O   . ILE   B 138 ? 0.6105 0.5815 0.1469 0.1455  -0.0013 0.0107  147 ILE   B O   
1744 C  CB  . ILE   B 138 ? 0.6654 0.6320 0.1898 0.1664  -0.0118 0.0064  147 ILE   B CB  
1745 C  CG1 . ILE   B 138 ? 0.6649 0.6416 0.1881 0.1758  -0.0060 0.0099  147 ILE   B CG1 
1746 C  CG2 . ILE   B 138 ? 0.6581 0.6177 0.1775 0.1708  -0.0202 0.0021  147 ILE   B CG2 
1747 C  CD1 . ILE   B 138 ? 0.6742 0.6523 0.1877 0.1875  -0.0110 0.0085  147 ILE   B CD1 
1748 N  N   . GLY   B 139 ? 0.6088 0.5892 0.1565 0.1456  0.0100  0.0142  148 GLY   B N   
1749 C  CA  . GLY   B 139 ? 0.5905 0.5763 0.1445 0.1389  0.0171  0.0171  148 GLY   B CA  
1750 C  C   . GLY   B 139 ? 0.5878 0.5814 0.1486 0.1410  0.0253  0.0212  148 GLY   B C   
1751 O  O   . GLY   B 139 ? 0.5936 0.5892 0.1541 0.1485  0.0257  0.0224  148 GLY   B O   
1752 N  N   A LEU   B 140 ? 0.5747 0.5730 0.1418 0.1348  0.0316  0.0235  149 LEU   B N   
1753 N  N   B LEU   B 140 ? 0.5747 0.5729 0.1418 0.1348  0.0316  0.0235  149 LEU   B N   
1754 N  N   C LEU   B 140 ? 0.5750 0.5734 0.1420 0.1350  0.0315  0.0236  149 LEU   B N   
1755 N  N   D LEU   B 140 ? 0.5750 0.5734 0.1420 0.1350  0.0315  0.0236  149 LEU   B N   
1756 C  CA  A LEU   B 140 ? 0.5688 0.5742 0.1440 0.1352  0.0396  0.0279  149 LEU   B CA  
1757 C  CA  B LEU   B 140 ? 0.5688 0.5742 0.1440 0.1352  0.0396  0.0279  149 LEU   B CA  
1758 C  CA  C LEU   B 140 ? 0.5768 0.5822 0.1519 0.1354  0.0395  0.0280  149 LEU   B CA  
1759 C  CA  D LEU   B 140 ? 0.5768 0.5822 0.1519 0.1354  0.0395  0.0280  149 LEU   B CA  
1760 C  C   A LEU   B 140 ? 0.5715 0.5834 0.1442 0.1394  0.0423  0.0322  149 LEU   B C   
1761 C  C   B LEU   B 140 ? 0.5715 0.5834 0.1442 0.1394  0.0423  0.0322  149 LEU   B C   
1762 C  C   C LEU   B 140 ? 0.5859 0.5979 0.1588 0.1392  0.0424  0.0322  149 LEU   B C   
1763 C  C   D LEU   B 140 ? 0.5859 0.5979 0.1588 0.1392  0.0424  0.0322  149 LEU   B C   
1764 O  O   A LEU   B 140 ? 0.5601 0.5716 0.1300 0.1358  0.0411  0.0313  149 LEU   B O   
1765 O  O   B LEU   B 140 ? 0.5601 0.5716 0.1301 0.1358  0.0411  0.0313  149 LEU   B O   
1766 O  O   C LEU   B 140 ? 0.5738 0.5848 0.1420 0.1373  0.0399  0.0311  149 LEU   B O   
1767 O  O   D LEU   B 140 ? 0.5738 0.5848 0.1420 0.1373  0.0399  0.0311  149 LEU   B O   
1768 C  CB  A LEU   B 140 ? 0.5632 0.5689 0.1492 0.1241  0.0446  0.0267  149 LEU   B CB  
1769 C  CB  B LEU   B 140 ? 0.5632 0.5689 0.1492 0.1241  0.0446  0.0267  149 LEU   B CB  
1770 C  CB  C LEU   B 140 ? 0.5751 0.5810 0.1612 0.1246  0.0447  0.0269  149 LEU   B CB  
1771 C  CB  D LEU   B 140 ? 0.5751 0.5810 0.1612 0.1246  0.0447  0.0269  149 LEU   B CB  
1772 C  CG  A LEU   B 140 ? 0.5606 0.5614 0.1499 0.1188  0.0423  0.0222  149 LEU   B CG  
1773 C  CG  B LEU   B 140 ? 0.5606 0.5615 0.1499 0.1188  0.0423  0.0222  149 LEU   B CG  
1774 C  CG  C LEU   B 140 ? 0.5742 0.5753 0.1637 0.1194  0.0425  0.0225  149 LEU   B CG  
1775 C  CG  D LEU   B 140 ? 0.5742 0.5753 0.1637 0.1194  0.0425  0.0225  149 LEU   B CG  
1776 C  CD1 A LEU   B 140 ? 0.5530 0.5564 0.1537 0.1092  0.0481  0.0210  149 LEU   B CD1 
1777 C  CD1 B LEU   B 140 ? 0.5531 0.5564 0.1537 0.1092  0.0481  0.0210  149 LEU   B CD1 
1778 C  CD1 C LEU   B 140 ? 0.5625 0.5662 0.1637 0.1105  0.0486  0.0216  149 LEU   B CD1 
1779 C  CD1 D LEU   B 140 ? 0.5625 0.5662 0.1637 0.1105  0.0486  0.0216  149 LEU   B CD1 
1780 C  CD2 A LEU   B 140 ? 0.5591 0.5587 0.1476 0.1263  0.0406  0.0226  149 LEU   B CD2 
1781 C  CD2 B LEU   B 140 ? 0.5591 0.5587 0.1475 0.1263  0.0406  0.0226  149 LEU   B CD2 
1782 C  CD2 C LEU   B 140 ? 0.5690 0.5687 0.1571 0.1270  0.0404  0.0228  149 LEU   B CD2 
1783 C  CD2 D LEU   B 140 ? 0.5690 0.5687 0.1571 0.1270  0.0404  0.0228  149 LEU   B CD2 
1784 N  N   A TYR   B 141 ? 0.5681 0.5863 0.1411 0.1472  0.0453  0.0368  150 TYR   B N   
1785 N  N   B TYR   B 141 ? 0.5681 0.5863 0.1410 0.1472  0.0453  0.0368  150 TYR   B N   
1786 N  N   C TYR   B 141 ? 0.5816 0.6004 0.1574 0.1449  0.0470  0.0372  150 TYR   B N   
1787 N  N   D TYR   B 141 ? 0.5816 0.6004 0.1574 0.1449  0.0470  0.0372  150 TYR   B N   
1788 C  CA  A TYR   B 141 ? 0.5752 0.6021 0.1479 0.1510  0.0494  0.0421  150 TYR   B CA  
1789 C  CA  B TYR   B 141 ? 0.5752 0.6021 0.1479 0.1510  0.0494  0.0421  150 TYR   B CA  
1790 C  CA  C TYR   B 141 ? 0.5905 0.6178 0.1650 0.1496  0.0504  0.0425  150 TYR   B CA  
1791 C  CA  D TYR   B 141 ? 0.5905 0.6178 0.1650 0.1496  0.0504  0.0425  150 TYR   B CA  
1792 C  C   A TYR   B 141 ? 0.5702 0.6006 0.1543 0.1424  0.0566  0.0450  150 TYR   B C   
1793 C  C   B TYR   B 141 ? 0.5702 0.6005 0.1543 0.1424  0.0566  0.0450  150 TYR   B C   
1794 C  C   C TYR   B 141 ? 0.5918 0.6232 0.1771 0.1415  0.0577  0.0457  150 TYR   B C   
1795 C  C   D TYR   B 141 ? 0.5918 0.6232 0.1771 0.1415  0.0577  0.0457  150 TYR   B C   
1796 O  O   A TYR   B 141 ? 0.5723 0.6019 0.1646 0.1398  0.0598  0.0458  150 TYR   B O   
1797 O  O   B TYR   B 141 ? 0.5724 0.6020 0.1646 0.1398  0.0598  0.0458  150 TYR   B O   
1798 O  O   C TYR   B 141 ? 0.6038 0.6338 0.1981 0.1369  0.0610  0.0458  150 TYR   B O   
1799 O  O   D TYR   B 141 ? 0.6038 0.6338 0.1982 0.1369  0.0610  0.0458  150 TYR   B O   
1800 C  CB  A TYR   B 141 ? 0.5794 0.6129 0.1490 0.1619  0.0499  0.0465  150 TYR   B CB  
1801 C  CB  B TYR   B 141 ? 0.5794 0.6129 0.1489 0.1619  0.0499  0.0465  150 TYR   B CB  
1802 C  CB  C TYR   B 141 ? 0.5962 0.6292 0.1673 0.1607  0.0504  0.0464  150 TYR   B CB  
1803 C  CB  D TYR   B 141 ? 0.5962 0.6291 0.1672 0.1607  0.0504  0.0464  150 TYR   B CB  
1804 C  CG  A TYR   B 141 ? 0.5833 0.6277 0.1555 0.1650  0.0555  0.0535  150 TYR   B CG  
1805 C  CG  B TYR   B 141 ? 0.5832 0.6276 0.1554 0.1650  0.0555  0.0535  150 TYR   B CG  
1806 C  CG  C TYR   B 141 ? 0.6037 0.6476 0.1764 0.1651  0.0555  0.0534  150 TYR   B CG  
1807 C  CG  D TYR   B 141 ? 0.6037 0.6476 0.1764 0.1651  0.0555  0.0534  150 TYR   B CG  
1808 C  CD1 A TYR   B 141 ? 0.5818 0.6302 0.1649 0.1607  0.0620  0.0586  150 TYR   B CD1 
1809 C  CD1 B TYR   B 141 ? 0.5818 0.6302 0.1648 0.1607  0.0620  0.0586  150 TYR   B CD1 
1810 C  CD1 C TYR   B 141 ? 0.6137 0.6642 0.1775 0.1738  0.0533  0.0549  150 TYR   B CD1 
1811 C  CD1 D TYR   B 141 ? 0.6137 0.6641 0.1775 0.1738  0.0533  0.0549  150 TYR   B CD1 
1812 C  CD2 A TYR   B 141 ? 0.5906 0.6418 0.1546 0.1729  0.0538  0.0552  150 TYR   B CD2 
1813 C  CD2 B TYR   B 141 ? 0.5906 0.6417 0.1545 0.1729  0.0538  0.0552  150 TYR   B CD2 
1814 C  CD2 C TYR   B 141 ? 0.6061 0.6545 0.1894 0.1615  0.0620  0.0588  150 TYR   B CD2 
1815 C  CD2 D TYR   B 141 ? 0.6061 0.6545 0.1894 0.1615  0.0620  0.0588  150 TYR   B CD2 
1816 C  CE1 A TYR   B 141 ? 0.5847 0.6435 0.1705 0.1633  0.0667  0.0658  150 TYR   B CE1 
1817 C  CE1 B TYR   B 141 ? 0.5847 0.6435 0.1705 0.1633  0.0667  0.0658  150 TYR   B CE1 
1818 C  CE1 C TYR   B 141 ? 0.6157 0.6780 0.1809 0.1783  0.0578  0.0619  150 TYR   B CE1 
1819 C  CE1 D TYR   B 141 ? 0.6157 0.6780 0.1808 0.1783  0.0578  0.0619  150 TYR   B CE1 
1820 C  CE2 A TYR   B 141 ? 0.5933 0.6559 0.1595 0.1759  0.0588  0.0621  150 TYR   B CE2 
1821 C  CE2 B TYR   B 141 ? 0.5933 0.6559 0.1595 0.1759  0.0587  0.0621  150 TYR   B CE2 
1822 C  CE2 C TYR   B 141 ? 0.6082 0.6673 0.1933 0.1656  0.0663  0.0662  150 TYR   B CE2 
1823 C  CE2 D TYR   B 141 ? 0.6082 0.6673 0.1932 0.1656  0.0663  0.0662  150 TYR   B CE2 
1824 C  CZ  A TYR   B 141 ? 0.5912 0.6577 0.1685 0.1708  0.0653  0.0677  150 TYR   B CZ  
1825 C  CZ  B TYR   B 141 ? 0.5913 0.6578 0.1685 0.1708  0.0653  0.0677  150 TYR   B CZ  
1826 C  CZ  C TYR   B 141 ? 0.6142 0.6809 0.1901 0.1738  0.0644  0.0679  150 TYR   B CZ  
1827 C  CZ  D TYR   B 141 ? 0.6142 0.6809 0.1901 0.1738  0.0644  0.0679  150 TYR   B CZ  
1828 O  OH  A TYR   B 141 ? 0.5919 0.6701 0.1717 0.1734  0.0698  0.0752  150 TYR   B OH  
1829 O  OH  B TYR   B 141 ? 0.5919 0.6701 0.1716 0.1734  0.0698  0.0752  150 TYR   B OH  
1830 O  OH  C TYR   B 141 ? 0.6129 0.6915 0.1909 0.1771  0.0688  0.0756  150 TYR   B OH  
1831 O  OH  D TYR   B 141 ? 0.6129 0.6915 0.1909 0.1772  0.0688  0.0756  150 TYR   B OH  
1832 N  N   A GLY   B 142 ? 0.5729 0.6071 0.1579 0.1385  0.0590  0.0465  151 GLY   B N   
1833 N  N   B GLY   B 142 ? 0.5729 0.6071 0.1579 0.1385  0.0590  0.0465  151 GLY   B N   
1834 N  N   C GLY   B 142 ? 0.5996 0.6359 0.1845 0.1397  0.0598  0.0479  151 GLY   B N   
1835 N  N   D GLY   B 142 ? 0.5996 0.6359 0.1845 0.1397  0.0598  0.0479  151 GLY   B N   
1836 C  CA  A GLY   B 142 ? 0.5731 0.6114 0.1690 0.1311  0.0659  0.0496  151 GLY   B CA  
1837 C  CA  B GLY   B 142 ? 0.5731 0.6114 0.1690 0.1311  0.0659  0.0496  151 GLY   B CA  
1838 C  CA  C GLY   B 142 ? 0.6015 0.6424 0.1968 0.1325  0.0666  0.0512  151 GLY   B CA  
1839 C  CA  D GLY   B 142 ? 0.6015 0.6424 0.1968 0.1325  0.0666  0.0512  151 GLY   B CA  
1840 C  C   A GLY   B 142 ? 0.5716 0.6112 0.1686 0.1236  0.0672  0.0484  151 GLY   B C   
1841 C  C   B GLY   B 142 ? 0.5715 0.6112 0.1686 0.1236  0.0672  0.0484  151 GLY   B C   
1842 C  C   C GLY   B 142 ? 0.6014 0.6425 0.1976 0.1244  0.0674  0.0493  151 GLY   B C   
1843 C  C   D GLY   B 142 ? 0.6015 0.6425 0.1976 0.1244  0.0674  0.0493  151 GLY   B C   
1844 O  O   A GLY   B 142 ? 0.5690 0.6124 0.1753 0.1175  0.0728  0.0508  151 GLY   B O   
1845 O  O   B GLY   B 142 ? 0.5690 0.6124 0.1753 0.1175  0.0728  0.0508  151 GLY   B O   
1846 O  O   C GLY   B 142 ? 0.6065 0.6520 0.2114 0.1185  0.0730  0.0519  151 GLY   B O   
1847 O  O   D GLY   B 142 ? 0.6065 0.6520 0.2115 0.1185  0.0730  0.0519  151 GLY   B O   
1848 N  N   A ASN   B 143 ? 0.5784 0.6149 0.1670 0.1236  0.0621  0.0450  152 ASN   B N   
1849 N  N   B ASN   B 143 ? 0.5783 0.6149 0.1670 0.1236  0.0621  0.0450  152 ASN   B N   
1850 N  N   C ASN   B 143 ? 0.6026 0.6394 0.1906 0.1241  0.0619  0.0451  152 ASN   B N   
1851 N  N   D ASN   B 143 ? 0.6026 0.6394 0.1906 0.1241  0.0619  0.0451  152 ASN   B N   
1852 C  CA  A ASN   B 143 ? 0.5774 0.6168 0.1655 0.1183  0.0629  0.0450  152 ASN   B CA  
1853 C  CA  B ASN   B 143 ? 0.5774 0.6168 0.1655 0.1183  0.0629  0.0450  152 ASN   B CA  
1854 C  CA  C ASN   B 143 ? 0.5941 0.6327 0.1811 0.1183  0.0620  0.0444  152 ASN   B CA  
1855 C  CA  D ASN   B 143 ? 0.5941 0.6327 0.1811 0.1184  0.0620  0.0444  152 ASN   B CA  
1856 C  C   A ASN   B 143 ? 0.5926 0.6349 0.1701 0.1274  0.0588  0.0464  152 ASN   B C   
1857 C  C   B ASN   B 143 ? 0.5927 0.6349 0.1701 0.1274  0.0588  0.0464  152 ASN   B C   
1858 C  C   C ASN   B 143 ? 0.6015 0.6435 0.1783 0.1274  0.0582  0.0461  152 ASN   B C   
1859 C  C   D ASN   B 143 ? 0.6015 0.6435 0.1782 0.1274  0.0582  0.0461  152 ASN   B C   
1860 O  O   A ASN   B 143 ? 0.6052 0.6415 0.1736 0.1335  0.0517  0.0430  152 ASN   B O   
1861 O  O   B ASN   B 143 ? 0.6053 0.6416 0.1737 0.1334  0.0517  0.0430  152 ASN   B O   
1862 O  O   C ASN   B 143 ? 0.6194 0.6551 0.1869 0.1326  0.0509  0.0425  152 ASN   B O   
1863 O  O   D ASN   B 143 ? 0.6194 0.6551 0.1869 0.1326  0.0510  0.0425  152 ASN   B O   
1864 C  CB  A ASN   B 143 ? 0.5683 0.6020 0.1580 0.1081  0.0609  0.0396  152 ASN   B CB  
1865 C  CB  B ASN   B 143 ? 0.5683 0.6020 0.1580 0.1081  0.0609  0.0396  152 ASN   B CB  
1866 C  CB  C ASN   B 143 ? 0.5847 0.6167 0.1723 0.1091  0.0592  0.0388  152 ASN   B CB  
1867 C  CB  D ASN   B 143 ? 0.5847 0.6167 0.1723 0.1091  0.0592  0.0388  152 ASN   B CB  
1868 C  CG  A ASN   B 143 ? 0.5617 0.5997 0.1552 0.1000  0.0640  0.0400  152 ASN   B CG  
1869 C  CG  B ASN   B 143 ? 0.5616 0.5997 0.1552 0.1000  0.0641  0.0400  152 ASN   B CG  
1870 C  CG  C ASN   B 143 ? 0.5813 0.6166 0.1708 0.1013  0.0609  0.0386  152 ASN   B CG  
1871 C  CG  D ASN   B 143 ? 0.5813 0.6166 0.1708 0.1013  0.0609  0.0386  152 ASN   B CG  
1872 O  OD1 A ASN   B 143 ? 0.5579 0.6027 0.1568 0.0994  0.0693  0.0439  152 ASN   B OD1 
1873 O  OD1 B ASN   B 143 ? 0.5578 0.6027 0.1567 0.0994  0.0693  0.0439  152 ASN   B OD1 
1874 O  OD1 C ASN   B 143 ? 0.5776 0.6198 0.1721 0.0998  0.0661  0.0421  152 ASN   B OD1 
1875 O  OD1 D ASN   B 143 ? 0.5776 0.6198 0.1721 0.0998  0.0661  0.0421  152 ASN   B OD1 
1876 N  ND2 A ASN   B 143 ? 0.5553 0.5899 0.1465 0.0933  0.0608  0.0362  152 ASN   B ND2 
1877 N  ND2 B ASN   B 143 ? 0.5552 0.5899 0.1465 0.0933  0.0608  0.0362  152 ASN   B ND2 
1878 N  ND2 C ASN   B 143 ? 0.5767 0.6073 0.1627 0.0957  0.0565  0.0347  152 ASN   B ND2 
1879 N  ND2 D ASN   B 143 ? 0.5766 0.6073 0.1627 0.0957  0.0565  0.0347  152 ASN   B ND2 
1880 N  N   . GLY   B 144 ? 0.6026 0.6536 0.1817 0.1276  0.0626  0.0508  153 GLY   B N   
1881 C  CA  . GLY   B 144 ? 0.6216 0.6778 0.1919 0.1364  0.0598  0.0525  153 GLY   B CA  
1882 C  C   . GLY   B 144 ? 0.6480 0.7144 0.2217 0.1350  0.0647  0.0574  153 GLY   B C   
1883 O  O   . GLY   B 144 ? 0.6290 0.6963 0.2105 0.1248  0.0688  0.0577  153 GLY   B O   
1884 N  N   A VAL   B 145 ? 0.6592 0.7341 0.2275 0.1447  0.0645  0.0611  154 VAL   B N   
1885 N  N   B VAL   B 145 ? 0.6591 0.7340 0.2275 0.1447  0.0645  0.0611  154 VAL   B N   
1886 N  N   C VAL   B 145 ? 0.6548 0.7297 0.2231 0.1448  0.0645  0.0610  154 VAL   B N   
1887 N  N   D VAL   B 145 ? 0.6280 0.7028 0.1963 0.1449  0.0645  0.0610  154 VAL   B N   
1888 C  CA  A VAL   B 145 ? 0.6758 0.7620 0.2454 0.1451  0.0681  0.0658  154 VAL   B CA  
1889 C  CA  B VAL   B 145 ? 0.6758 0.7620 0.2454 0.1451  0.0681  0.0658  154 VAL   B CA  
1890 C  CA  C VAL   B 145 ? 0.6721 0.7582 0.2417 0.1451  0.0681  0.0658  154 VAL   B CA  
1891 C  CA  D VAL   B 145 ? 0.6309 0.7170 0.1999 0.1458  0.0678  0.0657  154 VAL   B CA  
1892 C  C   A VAL   B 145 ? 0.6911 0.7888 0.2606 0.1539  0.0713  0.0721  154 VAL   B C   
1893 C  C   B VAL   B 145 ? 0.6911 0.7888 0.2606 0.1539  0.0713  0.0721  154 VAL   B C   
1894 C  C   C VAL   B 145 ? 0.6856 0.7832 0.2552 0.1538  0.0713  0.0721  154 VAL   B C   
1895 C  C   D VAL   B 145 ? 0.6474 0.7446 0.2181 0.1531  0.0718  0.0723  154 VAL   B C   
1896 O  O   A VAL   B 145 ? 0.6890 0.7859 0.2533 0.1623  0.0685  0.0715  154 VAL   B O   
1897 O  O   B VAL   B 145 ? 0.6889 0.7858 0.2532 0.1623  0.0685  0.0715  154 VAL   B O   
1898 O  O   C VAL   B 145 ? 0.6830 0.7799 0.2472 0.1623  0.0685  0.0715  154 VAL   B O   
1899 O  O   D VAL   B 145 ? 0.6374 0.7329 0.2052 0.1597  0.0700  0.0721  154 VAL   B O   
1900 C  CB  A VAL   B 145 ? 0.6883 0.7742 0.2494 0.1481  0.0629  0.0628  154 VAL   B CB  
1901 C  CB  B VAL   B 145 ? 0.6884 0.7743 0.2495 0.1481  0.0629  0.0628  154 VAL   B CB  
1902 C  CB  C VAL   B 145 ? 0.6910 0.7770 0.2521 0.1482  0.0629  0.0628  154 VAL   B CB  
1903 C  CB  D VAL   B 145 ? 0.6264 0.7127 0.1857 0.1511  0.0621  0.0628  154 VAL   B CB  
1904 C  CG1 A VAL   B 145 ? 0.6919 0.7781 0.2424 0.1610  0.0570  0.0609  154 VAL   B CG1 
1905 C  CG1 B VAL   B 145 ? 0.6919 0.7781 0.2424 0.1610  0.0570  0.0609  154 VAL   B CG1 
1906 C  CG1 C VAL   B 145 ? 0.6904 0.7766 0.2408 0.1611  0.0570  0.0609  154 VAL   B CG1 
1907 C  CG1 D VAL   B 145 ? 0.6297 0.7291 0.1886 0.1543  0.0651  0.0676  154 VAL   B CG1 
1908 C  CG2 A VAL   B 145 ? 0.6940 0.7906 0.2578 0.1459  0.0668  0.0670  154 VAL   B CG2 
1909 C  CG2 B VAL   B 145 ? 0.6943 0.7908 0.2581 0.1459  0.0668  0.0669  154 VAL   B CG2 
1910 C  CG2 C VAL   B 145 ? 0.7019 0.7984 0.2657 0.1458  0.0668  0.0669  154 VAL   B CG2 
1911 C  CG2 D VAL   B 145 ? 0.6146 0.6910 0.1736 0.1422  0.0586  0.0576  154 VAL   B CG2 
1912 N  N   A VAL   B 146 ? 0.7097 0.8183 0.2846 0.1517  0.0766  0.0781  155 VAL   B N   
1913 N  N   B VAL   B 146 ? 0.7097 0.8183 0.2846 0.1517  0.0766  0.0781  155 VAL   B N   
1914 N  N   C VAL   B 146 ? 0.6905 0.7981 0.2671 0.1504  0.0773  0.0783  155 VAL   B N   
1915 N  N   D VAL   B 146 ? 0.6768 0.7845 0.2534 0.1505  0.0773  0.0783  155 VAL   B N   
1916 C  CA  A VAL   B 146 ? 0.7317 0.8545 0.3064 0.1595  0.0798  0.0853  155 VAL   B CA  
1917 C  CA  B VAL   B 146 ? 0.7318 0.8545 0.3064 0.1595  0.0798  0.0853  155 VAL   B CA  
1918 C  CA  C VAL   B 146 ? 0.7113 0.8328 0.2888 0.1574  0.0809  0.0859  155 VAL   B CA  
1919 C  CA  D VAL   B 146 ? 0.7040 0.8255 0.2816 0.1574  0.0809  0.0859  155 VAL   B CA  
1920 C  C   A VAL   B 146 ? 0.7514 0.8828 0.3172 0.1673  0.0770  0.0851  155 VAL   B C   
1921 C  C   B VAL   B 146 ? 0.7515 0.8829 0.3173 0.1673  0.0770  0.0851  155 VAL   B C   
1922 C  C   C VAL   B 146 ? 0.7286 0.8601 0.2990 0.1636  0.0794  0.0869  155 VAL   B C   
1923 C  C   D VAL   B 146 ? 0.7251 0.8566 0.2955 0.1636  0.0794  0.0869  155 VAL   B C   
1924 O  O   A VAL   B 146 ? 0.7471 0.8818 0.3147 0.1623  0.0782  0.0856  155 VAL   B O   
1925 O  O   B VAL   B 146 ? 0.7471 0.8817 0.3147 0.1623  0.0782  0.0856  155 VAL   B O   
1926 O  O   C VAL   B 146 ? 0.7361 0.8668 0.3074 0.1578  0.0793  0.0851  155 VAL   B O   
1927 O  O   D VAL   B 146 ? 0.7342 0.8649 0.3055 0.1578  0.0793  0.0852  155 VAL   B O   
1928 C  CB  A VAL   B 146 ? 0.7333 0.8629 0.3199 0.1518  0.0869  0.0923  155 VAL   B CB  
1929 C  CB  B VAL   B 146 ? 0.7333 0.8630 0.3199 0.1518  0.0869  0.0923  155 VAL   B CB  
1930 C  CB  C VAL   B 146 ? 0.7162 0.8426 0.3064 0.1492  0.0878  0.0923  155 VAL   B CB  
1931 C  CB  D VAL   B 146 ? 0.7126 0.8389 0.3028 0.1492  0.0879  0.0923  155 VAL   B CB  
1932 C  CG1 A VAL   B 146 ? 0.7378 0.8828 0.3249 0.1590  0.0901  0.1008  155 VAL   B CG1 
1933 C  CG1 B VAL   B 146 ? 0.7379 0.8829 0.3249 0.1590  0.0901  0.1008  155 VAL   B CG1 
1934 C  CG1 C VAL   B 146 ? 0.7195 0.8610 0.3109 0.1556  0.0914  0.1012  155 VAL   B CG1 
1935 C  CG1 D VAL   B 146 ? 0.7169 0.8584 0.3084 0.1556  0.0914  0.1012  155 VAL   B CG1 
1936 C  CG2 A VAL   B 146 ? 0.7332 0.8533 0.3292 0.1439  0.0891  0.0914  155 VAL   B CG2 
1937 C  CG2 B VAL   B 146 ? 0.7333 0.8534 0.3293 0.1439  0.0891  0.0914  155 VAL   B CG2 
1938 C  CG2 C VAL   B 146 ? 0.7137 0.8297 0.3118 0.1429  0.0892  0.0907  155 VAL   B CG2 
1939 C  CG2 D VAL   B 146 ? 0.7109 0.8269 0.3090 0.1429  0.0892  0.0907  155 VAL   B CG2 
1940 N  N   A ILE   B 147 ? 0.7718 0.9071 0.3283 0.1794  0.0732  0.0841  156 ILE   B N   
1941 N  N   B ILE   B 147 ? 0.7718 0.9071 0.3284 0.1794  0.0732  0.0841  156 ILE   B N   
1942 N  N   C ILE   B 147 ? 0.7386 0.8798 0.3020 0.1753  0.0780  0.0892  156 ILE   B N   
1943 N  N   D ILE   B 147 ? 0.7372 0.8785 0.3006 0.1753  0.0780  0.0892  156 ILE   B N   
1944 C  CA  A ILE   B 147 ? 0.7873 0.9291 0.3342 0.1886  0.0690  0.0818  156 ILE   B CA  
1945 C  CA  B ILE   B 147 ? 0.7872 0.9291 0.3342 0.1886  0.0690  0.0818  156 ILE   B CA  
1946 C  CA  C ILE   B 147 ? 0.7484 0.8995 0.3039 0.1831  0.0757  0.0890  156 ILE   B CA  
1947 C  CA  D ILE   B 147 ? 0.7476 0.8987 0.3032 0.1831  0.0757  0.0890  156 ILE   B CA  
1948 C  C   A ILE   B 147 ? 0.7978 0.9587 0.3461 0.1931  0.0737  0.0893  156 ILE   B C   
1949 C  C   B ILE   B 147 ? 0.7978 0.9588 0.3461 0.1931  0.0737  0.0893  156 ILE   B C   
1950 C  C   C ILE   B 147 ? 0.7462 0.9157 0.3020 0.1905  0.0797  0.0969  156 ILE   B C   
1951 C  C   D ILE   B 147 ? 0.7458 0.9154 0.3016 0.1905  0.0797  0.0969  156 ILE   B C   
1952 O  O   A ILE   B 147 ? 0.7943 0.9626 0.3504 0.1898  0.0795  0.0965  156 ILE   B O   
1953 O  O   B ILE   B 147 ? 0.7942 0.9625 0.3503 0.1898  0.0795  0.0965  156 ILE   B O   
1954 O  O   C ILE   B 147 ? 0.7490 0.9210 0.3080 0.1920  0.0821  0.1010  156 ILE   B O   
1955 O  O   D ILE   B 147 ? 0.7488 0.9208 0.3078 0.1920  0.0821  0.1010  156 ILE   B O   
1956 C  CB  A ILE   B 147 ? 0.7944 0.9316 0.3310 0.1998  0.0622  0.0762  156 ILE   B CB  
1957 C  CB  B ILE   B 147 ? 0.7943 0.9315 0.3309 0.1998  0.0622  0.0762  156 ILE   B CB  
1958 C  CB  C ILE   B 147 ? 0.7611 0.9038 0.3054 0.1913  0.0676  0.0809  156 ILE   B CB  
1959 C  CB  D ILE   B 147 ? 0.7606 0.9033 0.3049 0.1913  0.0676  0.0809  156 ILE   B CB  
1960 C  CG1 A ILE   B 147 ? 0.8041 0.9494 0.3401 0.2074  0.0641  0.0802  156 ILE   B CG1 
1961 C  CG1 B ILE   B 147 ? 0.8042 0.9495 0.3401 0.2074  0.0641  0.0802  156 ILE   B CG1 
1962 C  CG1 C ILE   B 147 ? 0.7694 0.9104 0.3091 0.1998  0.0651  0.0796  156 ILE   B CG1 
1963 C  CG1 D ILE   B 147 ? 0.7692 0.9102 0.3089 0.1998  0.0651  0.0796  156 ILE   B CG1 
1964 C  CG2 A ILE   B 147 ? 0.7960 0.9148 0.3313 0.1947  0.0569  0.0690  156 ILE   B CG2 
1965 C  CG2 B ILE   B 147 ? 0.7960 0.9147 0.3312 0.1947  0.0569  0.0690  156 ILE   B CG2 
1966 C  CG2 C ILE   B 147 ? 0.7699 0.8965 0.3149 0.1824  0.0640  0.0745  156 ILE   B CG2 
1967 C  CG2 D ILE   B 147 ? 0.7694 0.8960 0.3144 0.1825  0.0640  0.0745  156 ILE   B CG2 
1968 C  CD1 A ILE   B 147 ? 0.8082 0.9549 0.3330 0.2209  0.0579  0.0755  156 ILE   B CD1 
1969 C  CD1 B ILE   B 147 ? 0.8080 0.9548 0.3328 0.2209  0.0578  0.0754  156 ILE   B CD1 
1970 C  CD1 C ILE   B 147 ? 0.7814 0.9128 0.3108 0.2072  0.0566  0.0713  156 ILE   B CD1 
1971 C  CD1 D ILE   B 147 ? 0.7812 0.9125 0.3106 0.2072  0.0566  0.0713  156 ILE   B CD1 
1972 N  N   A LYS   B 148 ? 0.8104 0.9793 0.3516 0.2006  0.0708  0.0878  157 LYS   B N   
1973 N  N   B LYS   B 148 ? 0.8105 0.9793 0.3516 0.2006  0.0708  0.0878  157 LYS   B N   
1974 N  N   C LYS   B 148 ? 0.7538 0.9360 0.3078 0.1933  0.0807  0.0995  157 LYS   B N   
1975 N  N   D LYS   B 148 ? 0.7537 0.9359 0.3076 0.1933  0.0807  0.0995  157 LYS   B N   
1976 C  CA  A LYS   B 148 ? 0.8172 1.0058 0.3584 0.2057  0.0745  0.0942  157 LYS   B CA  
1977 C  CA  B LYS   B 148 ? 0.8172 1.0059 0.3584 0.2057  0.0745  0.0942  157 LYS   B CA  
1978 C  CA  C LYS   B 148 ? 0.7609 0.9635 0.3130 0.2019  0.0836  0.1063  157 LYS   B CA  
1979 C  CA  D LYS   B 148 ? 0.7608 0.9634 0.3129 0.2019  0.0836  0.1063  157 LYS   B CA  
1980 C  C   A LYS   B 148 ? 0.8115 1.0127 0.3561 0.2093  0.0794  0.1019  157 LYS   B C   
1981 C  C   B LYS   B 148 ? 0.8115 1.0127 0.3561 0.2093  0.0794  0.1019  157 LYS   B C   
1982 C  C   C LYS   B 148 ? 0.7527 0.9640 0.3142 0.1978  0.0901  0.1160  157 LYS   B C   
1983 C  C   D LYS   B 148 ? 0.7527 0.9640 0.3142 0.1978  0.0901  0.1160  157 LYS   B C   
1984 O  O   A LYS   B 148 ? 0.8059 1.0204 0.3570 0.2059  0.0851  0.1100  157 LYS   B O   
1985 O  O   B LYS   B 148 ? 0.8058 1.0203 0.3570 0.2059  0.0851  0.1099  157 LYS   B O   
1986 O  O   C LYS   B 148 ? 0.7450 0.9609 0.3156 0.1889  0.0949  0.1215  157 LYS   B O   
1987 O  O   D LYS   B 148 ? 0.7449 0.9609 0.3156 0.1889  0.0949  0.1215  157 LYS   B O   
1988 C  CB  A LYS   B 148 ? 0.8339 1.0287 0.3641 0.2181  0.0690  0.0896  157 LYS   B CB  
1989 C  CB  B LYS   B 148 ? 0.8339 1.0287 0.3641 0.2181  0.0690  0.0896  157 LYS   B CB  
1990 C  CB  C LYS   B 148 ? 0.7861 0.9934 0.3268 0.2164  0.0785  0.1026  157 LYS   B CB  
1991 C  CB  D LYS   B 148 ? 0.7861 0.9934 0.3267 0.2164  0.0785  0.1026  157 LYS   B CB  
1992 C  CG  A LYS   B 148 ? 0.8437 1.0324 0.3716 0.2152  0.0652  0.0848  157 LYS   B CG  
1993 C  CG  B LYS   B 148 ? 0.8439 1.0327 0.3718 0.2153  0.0652  0.0848  157 LYS   B CG  
1994 C  CG  C LYS   B 148 ? 0.8015 0.9971 0.3327 0.2214  0.0708  0.0925  157 LYS   B CG  
1995 C  CG  D LYS   B 148 ? 0.8014 0.9971 0.3327 0.2214  0.0708  0.0925  157 LYS   B CG  
1996 C  CD  A LYS   B 148 ? 0.8513 1.0428 0.3684 0.2281  0.0583  0.0789  157 LYS   B CD  
1997 C  CD  B LYS   B 148 ? 0.8513 1.0428 0.3684 0.2281  0.0583  0.0789  157 LYS   B CD  
1998 C  CD  C LYS   B 148 ? 0.8299 1.0176 0.3541 0.2294  0.0655  0.0870  157 LYS   B CD  
1999 C  CD  D LYS   B 148 ? 0.8299 1.0177 0.3541 0.2294  0.0655  0.0870  157 LYS   B CD  
2000 C  CE  A LYS   B 148 ? 0.8556 1.0692 0.3697 0.2388  0.0606  0.0831  157 LYS   B CE  
2001 C  CE  B LYS   B 148 ? 0.8557 1.0692 0.3697 0.2388  0.0606  0.0831  157 LYS   B CE  
2002 C  CE  C LYS   B 148 ? 0.8529 1.0296 0.3679 0.2350  0.0571  0.0773  157 LYS   B CE  
2003 C  CE  D LYS   B 148 ? 0.8530 1.0297 0.3679 0.2350  0.0571  0.0773  157 LYS   B CE  
2004 N  NZ  A LYS   B 148 ? 0.8501 1.0756 0.3696 0.2333  0.0655  0.0887  157 LYS   B NZ  
2005 N  NZ  B LYS   B 148 ? 0.8500 1.0755 0.3695 0.2333  0.0655  0.0887  157 LYS   B NZ  
2006 N  NZ  C LYS   B 148 ? 0.8725 1.0346 0.3907 0.2243  0.0553  0.0737  157 LYS   B NZ  
2007 N  NZ  D LYS   B 148 ? 0.8726 1.0348 0.3909 0.2243  0.0553  0.0737  157 LYS   B NZ  
2008 N  N   A ASN   B 149 ? 0.8132 1.0106 0.3536 0.2158  0.0768  0.0999  158 ASN   B N   
2009 N  N   B ASN   B 149 ? 0.8133 1.0107 0.3536 0.2158  0.0768  0.0999  158 ASN   B N   
2010 N  N   C ASN   B 149 ? 0.7381 0.9520 0.2976 0.2043  0.0898  0.1180  158 ASN   B N   
2011 N  N   D ASN   B 149 ? 0.7381 0.9520 0.2976 0.2043  0.0898  0.1180  158 ASN   B N   
2012 C  CA  A ASN   B 149 ? 0.8095 1.0189 0.3517 0.2206  0.0804  0.1071  158 ASN   B CA  
2013 C  CA  B ASN   B 149 ? 0.8096 1.0190 0.3518 0.2206  0.0804  0.1071  158 ASN   B CA  
2014 C  CA  C ASN   B 149 ? 0.7347 0.9597 0.3015 0.2034  0.0951  0.1283  158 ASN   B CA  
2015 C  CA  D ASN   B 149 ? 0.7346 0.9597 0.3015 0.2034  0.0951  0.1283  158 ASN   B CA  
2016 C  C   A ASN   B 149 ? 0.7916 1.0000 0.3468 0.2089  0.0869  0.1147  158 ASN   B C   
2017 C  C   B ASN   B 149 ? 0.7919 1.0003 0.3471 0.2090  0.0869  0.1147  158 ASN   B C   
2018 C  C   C ASN   B 149 ? 0.7207 0.9316 0.2977 0.1931  0.0972  0.1292  158 ASN   B C   
2019 C  C   D ASN   B 149 ? 0.7207 0.9316 0.2977 0.1931  0.0972  0.1292  158 ASN   B C   
2020 O  O   A ASN   B 149 ? 0.7934 1.0171 0.3531 0.2100  0.0917  0.1239  158 ASN   B O   
2021 O  O   B ASN   B 149 ? 0.7936 1.0173 0.3533 0.2100  0.0917  0.1239  158 ASN   B O   
2022 O  O   C ASN   B 149 ? 0.6941 0.9115 0.2784 0.1914  0.1012  0.1377  158 ASN   B O   
2023 O  O   D ASN   B 149 ? 0.6940 0.9115 0.2783 0.1914  0.1012  0.1377  158 ASN   B O   
2024 C  CB  A ASN   B 149 ? 0.8232 1.0258 0.3588 0.2283  0.0759  0.1024  158 ASN   B CB  
2025 C  CB  B ASN   B 149 ? 0.8234 1.0260 0.3590 0.2283  0.0759  0.1024  158 ASN   B CB  
2026 C  CB  C ASN   B 149 ? 0.7471 0.9829 0.3062 0.2162  0.0934  0.1300  158 ASN   B CB  
2027 C  CB  D ASN   B 149 ? 0.7471 0.9829 0.3062 0.2162  0.0934  0.1300  158 ASN   B CB  
2028 C  CG  A ASN   B 149 ? 0.8345 1.0342 0.3579 0.2391  0.0684  0.0934  158 ASN   B CG  
2029 C  CG  B ASN   B 149 ? 0.8346 1.0344 0.3581 0.2390  0.0684  0.0934  158 ASN   B CG  
2030 C  CG  C ASN   B 149 ? 0.7547 0.9757 0.3090 0.2194  0.0888  0.1230  158 ASN   B CG  
2031 C  CG  D ASN   B 149 ? 0.7547 0.9757 0.3090 0.2194  0.0888  0.1230  158 ASN   B CG  
2032 O  OD1 A ASN   B 149 ? 0.8409 1.0395 0.3612 0.2394  0.0659  0.0895  158 ASN   B OD1 
2033 O  OD1 B ASN   B 149 ? 0.8411 1.0396 0.3613 0.2394  0.0659  0.0895  158 ASN   B OD1 
2034 O  OD1 C ASN   B 149 ? 0.7677 0.9750 0.3163 0.2199  0.0837  0.1135  158 ASN   B OD1 
2035 O  OD1 D ASN   B 149 ? 0.7677 0.9751 0.3164 0.2199  0.0837  0.1135  158 ASN   B OD1 
2036 N  ND2 A ASN   B 149 ? 0.8393 1.0374 0.3562 0.2478  0.0645  0.0899  158 ASN   B ND2 
2037 N  ND2 B ASN   B 149 ? 0.8394 1.0374 0.3563 0.2478  0.0645  0.0899  158 ASN   B ND2 
2038 N  ND2 C ASN   B 149 ? 0.7673 0.9911 0.3243 0.2214  0.0903  0.1278  158 ASN   B ND2 
2039 N  ND2 D ASN   B 149 ? 0.7674 0.9911 0.3243 0.2214  0.0903  0.1278  158 ASN   B ND2 
2040 N  N   A GLY   B 150 ? 0.7689 0.9603 0.3300 0.1983  0.0867  0.1109  159 GLY   B N   
2041 N  N   B GLY   B 150 ? 0.7695 0.9608 0.3306 0.1984  0.0867  0.1109  159 GLY   B N   
2042 N  N   C GLY   B 150 ? 0.7043 0.8971 0.2820 0.1866  0.0946  0.1211  159 GLY   B N   
2043 N  N   D GLY   B 150 ? 0.7042 0.8970 0.2819 0.1866  0.0946  0.1211  159 GLY   B N   
2044 C  CA  A GLY   B 150 ? 0.7503 0.9362 0.3236 0.1878  0.0915  0.1157  159 GLY   B CA  
2045 C  CA  B GLY   B 150 ? 0.7511 0.9371 0.3244 0.1878  0.0915  0.1157  159 GLY   B CA  
2046 C  CA  C GLY   B 150 ? 0.7037 0.8823 0.2898 0.1781  0.0957  0.1201  159 GLY   B CA  
2047 C  CA  D GLY   B 150 ? 0.7036 0.8823 0.2898 0.1781  0.0957  0.1201  159 GLY   B CA  
2048 C  C   A GLY   B 150 ? 0.7404 0.9132 0.3137 0.1879  0.0892  0.1119  159 GLY   B C   
2049 C  C   B GLY   B 150 ? 0.7420 0.9148 0.3154 0.1879  0.0892  0.1120  159 GLY   B C   
2050 C  C   C GLY   B 150 ? 0.7041 0.8718 0.2841 0.1834  0.0911  0.1140  159 GLY   B C   
2051 C  C   D GLY   B 150 ? 0.7040 0.8718 0.2841 0.1834  0.0911  0.1140  159 GLY   B C   
2052 O  O   A GLY   B 150 ? 0.7286 0.8967 0.3116 0.1811  0.0925  0.1156  159 GLY   B O   
2053 O  O   B GLY   B 150 ? 0.7293 0.8976 0.3125 0.1810  0.0926  0.1157  159 GLY   B O   
2054 O  O   C GLY   B 150 ? 0.7085 0.8681 0.2957 0.1788  0.0925  0.1151  159 GLY   B O   
2055 O  O   D GLY   B 150 ? 0.7084 0.8681 0.2956 0.1788  0.0925  0.1151  159 GLY   B O   
2056 N  N   A SER   B 151 ? 0.7396 0.9084 0.3019 0.1972  0.0833  0.1054  160 SER   B N   
2057 N  N   B SER   B 151 ? 0.7453 0.9142 0.3078 0.1972  0.0834  0.1056  160 SER   B N   
2058 N  N   C SER   B 151 ? 0.7242 0.8913 0.2920 0.1925  0.0856  0.1076  160 SER   B N   
2059 N  N   D SER   B 151 ? 0.7241 0.8912 0.2920 0.1925  0.0856  0.1076  160 SER   B N   
2060 C  CA  A SER   B 151 ? 0.7347 0.8915 0.2946 0.1991  0.0798  0.1006  160 SER   B CA  
2061 C  CA  B SER   B 151 ? 0.7431 0.9000 0.3039 0.1986  0.0802  0.1011  160 SER   B CA  
2062 C  CA  C SER   B 151 ? 0.7402 0.8970 0.3014 0.1980  0.0803  0.1011  160 SER   B CA  
2063 C  CA  D SER   B 151 ? 0.7402 0.8970 0.3013 0.1980  0.0803  0.1011  160 SER   B CA  
2064 C  C   A SER   B 151 ? 0.7306 0.8693 0.2931 0.1897  0.0774  0.0932  160 SER   B C   
2065 C  C   B SER   B 151 ? 0.7359 0.8747 0.2983 0.1899  0.0774  0.0932  160 SER   B C   
2066 C  C   C SER   B 151 ? 0.7392 0.8777 0.3016 0.1897  0.0773  0.0930  160 SER   B C   
2067 C  C   D SER   B 151 ? 0.7392 0.8777 0.3016 0.1897  0.0773  0.0930  160 SER   B C   
2068 O  O   A SER   B 151 ? 0.7224 0.8588 0.2864 0.1835  0.0777  0.0912  160 SER   B O   
2069 O  O   B SER   B 151 ? 0.7283 0.8649 0.2917 0.1841  0.0774  0.0910  160 SER   B O   
2070 O  O   C SER   B 151 ? 0.7240 0.8596 0.2871 0.1839  0.0771  0.0904  160 SER   B O   
2071 O  O   D SER   B 151 ? 0.7240 0.8596 0.2871 0.1839  0.0771  0.0904  160 SER   B O   
2072 C  CB  A SER   B 151 ? 0.7438 0.9042 0.2913 0.2124  0.0742  0.0964  160 SER   B CB  
2073 C  CB  B SER   B 151 ? 0.7581 0.9193 0.3070 0.2120  0.0750  0.0977  160 SER   B CB  
2074 C  CB  C SER   B 151 ? 0.7753 0.9391 0.3237 0.2113  0.0754  0.0977  160 SER   B CB  
2075 C  CB  D SER   B 151 ? 0.7754 0.9391 0.3238 0.2113  0.0754  0.0977  160 SER   B CB  
2076 O  OG  A SER   B 151 ? 0.7396 0.8883 0.2846 0.2140  0.0703  0.0914  160 SER   B OG  
2077 O  OG  B SER   B 151 ? 0.7658 0.9251 0.3059 0.2166  0.0700  0.0909  160 SER   B OG  
2078 O  OG  C SER   B 151 ? 0.8204 0.9804 0.3631 0.2117  0.0716  0.0916  160 SER   B OG  
2079 O  OG  D SER   B 151 ? 0.8206 0.9807 0.3634 0.2117  0.0716  0.0916  160 SER   B OG  
2080 N  N   . TYR   B 152 ? 0.7228 0.8503 0.2859 0.1887  0.0752  0.0895  161 TYR   B N   
2081 C  CA  . TYR   B 152 ? 0.7227 0.8340 0.2879 0.1802  0.0726  0.0825  161 TYR   B CA  
2082 C  C   . TYR   B 152 ? 0.7008 0.8036 0.2554 0.1863  0.0650  0.0745  161 TYR   B C   
2083 O  O   . TYR   B 152 ? 0.6783 0.7833 0.2269 0.1956  0.0621  0.0739  161 TYR   B O   
2084 C  CB  . TYR   B 152 ? 0.7333 0.8384 0.3080 0.1740  0.0756  0.0840  161 TYR   B CB  
2085 C  CG  . TYR   B 152 ? 0.7243 0.8154 0.3028 0.1642  0.0742  0.0775  161 TYR   B CG  
2086 C  CD1 . TYR   B 152 ? 0.7247 0.8142 0.3089 0.1544  0.0766  0.0766  161 TYR   B CD1 
2087 C  CD2 . TYR   B 152 ? 0.7232 0.8041 0.2996 0.1647  0.0702  0.0723  161 TYR   B CD2 
2088 C  CE1 . TYR   B 152 ? 0.7363 0.8146 0.3238 0.1454  0.0753  0.0706  161 TYR   B CE1 
2089 C  CE2 . TYR   B 152 ? 0.7520 0.8217 0.3321 0.1556  0.0691  0.0666  161 TYR   B CE2 
2090 C  CZ  . TYR   B 152 ? 0.7132 0.7820 0.2984 0.1461  0.0715  0.0657  161 TYR   B CZ  
2091 O  OH  . TYR   B 152 ? 0.7376 0.7971 0.3265 0.1372  0.0705  0.0602  161 TYR   B OH  
2092 N  N   . VAL   B 153 ? 0.6711 0.7642 0.2240 0.1804  0.0616  0.0686  162 VAL   B N   
2093 C  CA  . VAL   B 153 ? 0.6741 0.7563 0.2184 0.1840  0.0537  0.0609  162 VAL   B CA  
2094 C  C   . VAL   B 153 ? 0.6753 0.7447 0.2249 0.1723  0.0529  0.0568  162 VAL   B C   
2095 O  O   . VAL   B 153 ? 0.6524 0.7213 0.2060 0.1640  0.0549  0.0569  162 VAL   B O   
2096 C  CB  . VAL   B 153 ? 0.6783 0.7627 0.2136 0.1904  0.0487  0.0580  162 VAL   B CB  
2097 C  CG1 . VAL   B 153 ? 0.6844 0.7578 0.2111 0.1955  0.0400  0.0506  162 VAL   B CG1 
2098 C  CG2 . VAL   B 153 ? 0.7013 0.8015 0.2327 0.2009  0.0507  0.0626  162 VAL   B CG2 
2099 N  N   . SER   B 154 ? 0.6721 0.7329 0.2217 0.1721  0.0502  0.0535  163 SER   B N   
2100 C  CA  . SER   B 154 ? 0.6521 0.7019 0.2067 0.1618  0.0494  0.0495  163 SER   B CA  
2101 C  C   . SER   B 154 ? 0.6357 0.6754 0.1824 0.1625  0.0411  0.0430  163 SER   B C   
2102 O  O   . SER   B 154 ? 0.6398 0.6781 0.1779 0.1721  0.0354  0.0407  163 SER   B O   
2103 C  CB  . SER   B 154 ? 0.6523 0.7001 0.2129 0.1608  0.0519  0.0505  163 SER   B CB  
2104 O  OG  . SER   B 154 ? 0.6599 0.6972 0.2229 0.1538  0.0493  0.0454  163 SER   B OG  
2105 N  N   . ALA   B 155 ? 0.6035 0.6365 0.1530 0.1523  0.0399  0.0401  164 ALA   B N   
2106 C  CA  . ALA   B 155 ? 0.5953 0.6172 0.1393 0.1508  0.0320  0.0345  164 ALA   B CA  
2107 C  C   . ALA   B 155 ? 0.6042 0.6208 0.1486 0.1529  0.0301  0.0323  164 ALA   B C   
2108 O  O   . ALA   B 155 ? 0.6185 0.6379 0.1700 0.1510  0.0355  0.0345  164 ALA   B O   
2109 C  CB  . ALA   B 155 ? 0.6086 0.6263 0.1570 0.1383  0.0322  0.0327  164 ALA   B CB  
2110 N  N   . ILE   B 156 ? 0.6008 0.6091 0.1384 0.1560  0.0220  0.0279  165 ILE   B N   
2111 C  CA  . ILE   B 156 ? 0.6101 0.6112 0.1487 0.1541  0.0189  0.0248  165 ILE   B CA  
2112 C  C   . ILE   B 156 ? 0.5960 0.5915 0.1397 0.1412  0.0186  0.0227  165 ILE   B C   
2113 O  O   . ILE   B 156 ? 0.6078 0.5971 0.1470 0.1387  0.0124  0.0203  165 ILE   B O   
2114 C  CB  . ILE   B 156 ? 0.6288 0.6236 0.1581 0.1630  0.0100  0.0209  165 ILE   B CB  
2115 C  CG1 . ILE   B 156 ? 0.6442 0.6464 0.1679 0.1761  0.0102  0.0225  165 ILE   B CG1 
2116 C  CG2 . ILE   B 156 ? 0.6373 0.6252 0.1684 0.1602  0.0070  0.0180  165 ILE   B CG2 
2117 C  CD1 . ILE   B 156 ? 0.6484 0.6450 0.1633 0.1856  0.0015  0.0179  165 ILE   B CD1 
2118 N  N   . THR   B 157 ? 0.5846 0.5831 0.1374 0.1337  0.0252  0.0240  166 THR   B N   
2119 C  CA  . THR   B 157 ? 0.5708 0.5669 0.1293 0.1209  0.0262  0.0221  166 THR   B CA  
2120 C  C   . THR   B 157 ? 0.5848 0.5750 0.1449 0.1175  0.0228  0.0187  166 THR   B C   
2121 O  O   . THR   B 157 ? 0.5820 0.5738 0.1467 0.1196  0.0262  0.0191  166 THR   B O   
2122 C  CB  . THR   B 157 ? 0.5579 0.5610 0.1261 0.1143  0.0350  0.0245  166 THR   B CB  
2123 O  OG1 . THR   B 157 ? 0.5625 0.5722 0.1299 0.1169  0.0384  0.0281  166 THR   B OG1 
2124 C  CG2 . THR   B 157 ? 0.5499 0.5518 0.1231 0.1017  0.0355  0.0218  166 THR   B CG2 
2125 N  N   . GLN   B 158 ? 0.5819 0.5653 0.1380 0.1129  0.0159  0.0158  167 GLN   B N   
2126 C  CA  . GLN   B 158 ? 0.5839 0.5618 0.1409 0.1091  0.0116  0.0127  167 GLN   B CA  
2127 C  C   . GLN   B 158 ? 0.5980 0.5762 0.1596 0.0960  0.0118  0.0115  167 GLN   B C   
2128 O  O   . GLN   B 158 ? 0.5955 0.5740 0.1550 0.0924  0.0106  0.0124  167 GLN   B O   
2129 C  CB  . GLN   B 158 ? 0.6008 0.5705 0.1489 0.1155  0.0019  0.0107  167 GLN   B CB  
2130 C  CG  . GLN   B 158 ? 0.5895 0.5538 0.1385 0.1121  -0.0028 0.0078  167 GLN   B CG  
2131 C  CD  . GLN   B 158 ? 0.5986 0.5666 0.1537 0.1129  0.0023  0.0075  167 GLN   B CD  
2132 O  OE1 . GLN   B 158 ? 0.5666 0.5407 0.1299 0.1075  0.0099  0.0085  167 GLN   B OE1 
2133 N  NE2 . GLN   B 158 ? 0.5937 0.5585 0.1448 0.1212  -0.0015 0.0063  167 GLN   B NE2 
2134 N  N   . GLY   B 159 ? 0.6298 0.6085 0.1972 0.0899  0.0130  0.0094  168 GLY   B N   
2135 C  CA  . GLY   B 159 ? 0.6629 0.6429 0.2341 0.0776  0.0124  0.0079  168 GLY   B CA  
2136 C  C   . GLY   B 159 ? 0.7237 0.6965 0.2898 0.0753  0.0031  0.0065  168 GLY   B C   
2137 O  O   . GLY   B 159 ? 0.7881 0.7541 0.3475 0.0833  -0.0030 0.0062  168 GLY   B O   
2138 N  N   . LYS   B 160 ? 0.8207 0.7956 0.3903 0.0644  0.0022  0.0055  169 LYS   B N   
2139 C  CA  . LYS   B 160 ? 0.9047 0.8739 0.4707 0.0594  -0.0065 0.0049  169 LYS   B CA  
2140 C  C   . LYS   B 160 ? 0.9301 0.9025 0.5020 0.0541  -0.0054 0.0026  169 LYS   B C   
2141 O  O   . LYS   B 160 ? 0.9381 0.9191 0.5176 0.0477  0.0015  0.0015  169 LYS   B O   
2142 C  CB  . LYS   B 160 ? 0.9226 0.8939 0.4882 0.0500  -0.0083 0.0066  169 LYS   B CB  
2143 C  CG  . LYS   B 160 ? 0.9797 0.9440 0.5406 0.0456  -0.0186 0.0075  169 LYS   B CG  
2144 C  CD  . LYS   B 160 ? 1.0258 0.9947 0.5884 0.0337  -0.0196 0.0095  169 LYS   B CD  
2145 C  CE  . LYS   B 160 ? 1.0793 1.0452 0.6415 0.0259  -0.0275 0.0102  169 LYS   B CE  
2146 N  NZ  . LYS   B 160 ? 1.1034 1.0793 0.6705 0.0127  -0.0250 0.0113  169 LYS   B NZ  
2147 N  N   . ARG   B 161 ? 0.9558 0.9219 0.5247 0.0566  -0.0123 0.0015  170 ARG   B N   
2148 C  CA  . ARG   B 161 ? 1.0129 0.9820 0.5869 0.0511  -0.0127 -0.0004 170 ARG   B CA  
2149 C  C   . ARG   B 161 ? 1.0871 1.0558 0.6604 0.0402  -0.0191 0.0004  170 ARG   B C   
2150 O  O   . ARG   B 161 ? 1.1439 1.1047 0.7107 0.0411  -0.0269 0.0022  170 ARG   B O   
2151 C  CB  . ARG   B 161 ? 1.0221 0.9853 0.5933 0.0606  -0.0161 -0.0018 170 ARG   B CB  
2152 C  CG  . ARG   B 161 ? 1.0011 0.9685 0.5784 0.0575  -0.0146 -0.0040 170 ARG   B CG  
2153 C  CD  . ARG   B 161 ? 1.0368 0.9977 0.6103 0.0656  -0.0202 -0.0052 170 ARG   B CD  
2154 N  NE  . ARG   B 161 ? 1.0518 1.0164 0.6306 0.0603  -0.0209 -0.0071 170 ARG   B NE  
2155 C  CZ  . ARG   B 161 ? 1.0423 1.0098 0.6253 0.0649  -0.0176 -0.0088 170 ARG   B CZ  
2156 N  NH1 . ARG   B 161 ? 1.0339 1.0007 0.6160 0.0751  -0.0137 -0.0084 170 ARG   B NH1 
2157 N  NH2 . ARG   B 161 ? 1.0244 0.9960 0.6122 0.0591  -0.0187 -0.0105 170 ARG   B NH2 
2158 N  N   . GLU   B 162 ? 1.1755 1.1529 0.7556 0.0304  -0.0162 -0.0007 171 GLU   B N   
2159 C  CA  . GLU   B 162 ? 1.2268 1.2072 0.8074 0.0186  -0.0212 0.0007  171 GLU   B CA  
2160 C  C   . GLU   B 162 ? 1.2544 1.2313 0.8346 0.0168  -0.0284 0.0002  171 GLU   B C   
2161 O  O   . GLU   B 162 ? 1.2699 1.2499 0.8513 0.0068  -0.0329 0.0018  171 GLU   B O   
2162 C  CB  . GLU   B 162 ? 1.2713 1.2656 0.8597 0.0087  -0.0136 -0.0004 171 GLU   B CB  
2163 C  CG  . GLU   B 162 ? 1.2800 1.2785 0.8696 0.0092  -0.0066 -0.0001 171 GLU   B CG  
2164 C  CD  . GLU   B 162 ? 1.3409 1.3373 0.9255 0.0047  -0.0107 0.0034  171 GLU   B CD  
2165 O  OE1 . GLU   B 162 ? 1.4070 1.4128 0.9951 -0.0025 -0.0060 0.0035  171 GLU   B OE1 
2166 O  OE2 . GLU   B 162 ? 1.3590 1.3447 0.9366 0.0088  -0.0189 0.0058  171 GLU   B OE2 
2167 S  S   C DMS   C .   ? 1.3975 1.3902 0.7825 0.2604  0.0795  0.1590  101 DMS   A S   
2168 S  S   D DMS   C .   ? 1.3975 1.3902 0.7825 0.2604  0.0795  0.1590  101 DMS   A S   
2169 O  O   C DMS   C .   ? 1.3258 1.3149 0.6873 0.2632  0.0688  0.1415  101 DMS   A O   
2170 O  O   D DMS   C .   ? 1.3258 1.3149 0.6873 0.2632  0.0688  0.1415  101 DMS   A O   
2171 C  C1  C DMS   C .   ? 1.4352 1.4238 0.7922 0.2764  0.0722  0.1723  101 DMS   A C1  
2172 C  C1  D DMS   C .   ? 1.4352 1.4238 0.7922 0.2764  0.0722  0.1723  101 DMS   A C1  
2173 C  C2  C DMS   C .   ? 1.4154 1.4149 0.7977 0.2654  0.1036  0.1755  101 DMS   A C2  
2174 C  C2  D DMS   C .   ? 1.4154 1.4149 0.7977 0.2654  0.1036  0.1755  101 DMS   A C2  
2175 S  S   C DMS   D .   ? 1.3783 1.5447 0.9059 0.2072  0.0601  0.0775  102 DMS   A S   
2176 S  S   D DMS   D .   ? 1.3782 1.5447 0.9058 0.2072  0.0601  0.0775  102 DMS   A S   
2177 O  O   C DMS   D .   ? 1.4073 1.5666 0.9311 0.2057  0.0547  0.0723  102 DMS   A O   
2178 O  O   D DMS   D .   ? 1.4074 1.5667 0.9313 0.2057  0.0547  0.0724  102 DMS   A O   
2179 C  C1  C DMS   D .   ? 1.4056 1.5965 0.9309 0.2180  0.0636  0.0836  102 DMS   A C1  
2180 C  C1  D DMS   D .   ? 1.4057 1.5966 0.9310 0.2180  0.0636  0.0836  102 DMS   A C1  
2181 C  C2  C DMS   D .   ? 1.3550 1.5237 0.8960 0.1920  0.0688  0.0845  102 DMS   A C2  
2182 C  C2  D DMS   D .   ? 1.3548 1.5236 0.8958 0.1920  0.0688  0.0845  102 DMS   A C2  
2191 S  S   A DMS   F .   ? 0.9749 1.0528 0.5898 0.1404  0.0861  0.0814  201 DMS   B S   
2192 S  S   B DMS   F .   ? 0.9748 1.0526 0.5896 0.1404  0.0861  0.0814  201 DMS   B S   
2193 O  O   A DMS   F .   ? 0.9702 1.0574 0.5758 0.1474  0.0849  0.0843  201 DMS   B O   
2194 O  O   B DMS   F .   ? 0.9698 1.0571 0.5755 0.1474  0.0849  0.0843  201 DMS   B O   
2195 C  C1  A DMS   F .   ? 0.9747 1.0446 0.5923 0.1289  0.0857  0.0737  201 DMS   B C1  
2196 C  C1  B DMS   F .   ? 0.9746 1.0446 0.5923 0.1289  0.0857  0.0737  201 DMS   B C1  
2197 C  C2  A DMS   F .   ? 0.9804 1.0494 0.5871 0.1458  0.0800  0.0749  201 DMS   B C2  
2198 C  C2  B DMS   F .   ? 0.9804 1.0494 0.5870 0.1458  0.0800  0.0749  201 DMS   B C2  
2199 S  S   A DMS   G .   ? 1.0456 1.1035 0.7758 0.0109  0.1044  -0.0307 202 DMS   B S   
2200 S  S   B DMS   G .   ? 1.0456 1.1035 0.7758 0.0109  0.1044  -0.0307 202 DMS   B S   
2201 O  O   A DMS   G .   ? 1.0233 1.0804 0.7404 0.0128  0.1001  -0.0276 202 DMS   B O   
2202 O  O   B DMS   G .   ? 1.0233 1.0804 0.7404 0.0128  0.1001  -0.0276 202 DMS   B O   
2203 C  C1  A DMS   G .   ? 1.0242 1.0784 0.7656 0.0150  0.1051  -0.0350 202 DMS   B C1  
2204 C  C1  B DMS   G .   ? 1.0242 1.0784 0.7656 0.0150  0.1051  -0.0350 202 DMS   B C1  
2205 C  C2  A DMS   G .   ? 1.0192 1.0702 0.7502 0.0177  0.1056  -0.0209 202 DMS   B C2  
2206 C  C2  B DMS   G .   ? 1.0192 1.0702 0.7502 0.0177  0.1056  -0.0209 202 DMS   B C2  
2207 S  S   A DMS   H .   ? 0.6601 0.7275 0.2687 0.1155  0.0818  0.0635  203 DMS   B S   
2208 S  S   B DMS   H .   ? 0.6600 0.7274 0.2686 0.1155  0.0818  0.0635  203 DMS   B S   
2209 O  O   A DMS   H .   ? 0.6535 0.7158 0.2505 0.1214  0.0751  0.0593  203 DMS   B O   
2210 O  O   B DMS   H .   ? 0.6532 0.7155 0.2502 0.1214  0.0751  0.0593  203 DMS   B O   
2211 C  C1  A DMS   H .   ? 0.6581 0.7175 0.2763 0.1037  0.0833  0.0575  203 DMS   B C1  
2212 C  C1  B DMS   H .   ? 0.6581 0.7175 0.2763 0.1037  0.0833  0.0575  203 DMS   B C1  
2213 C  C2  A DMS   H .   ? 0.6613 0.7351 0.2708 0.1096  0.0839  0.0646  203 DMS   B C2  
2214 C  C2  B DMS   H .   ? 0.6613 0.7352 0.2708 0.1096  0.0839  0.0646  203 DMS   B C2  
2215 N  N1  C A1BHC I .   ? 0.7000 0.7515 0.3244 0.0732  0.0816  0.0402  204 A1BHC B N1  
2216 N  N1  D A1BHC I .   ? 0.7001 0.7516 0.3244 0.0732  0.0816  0.0402  204 A1BHC B N1  
2217 N  N3  C A1BHC I .   ? 0.6595 0.7642 0.2713 0.1509  0.0912  0.0975  204 A1BHC B N3  
2218 N  N3  D A1BHC I .   ? 0.6595 0.7642 0.2713 0.1509  0.0912  0.0975  204 A1BHC B N3  
2219 C  C4  C A1BHC I .   ? 0.6853 0.7368 0.3174 0.0829  0.0858  0.0464  204 A1BHC B C4  
2220 C  C4  D A1BHC I .   ? 0.6853 0.7369 0.3174 0.0829  0.0858  0.0464  204 A1BHC B C4  
2221 C  C5  C A1BHC I .   ? 0.6720 0.7237 0.3009 0.0925  0.0849  0.0506  204 A1BHC B C5  
2222 C  C5  D A1BHC I .   ? 0.6720 0.7237 0.3009 0.0925  0.0849  0.0506  204 A1BHC B C5  
2223 C  C6  C A1BHC I .   ? 0.6550 0.7108 0.2909 0.0952  0.0891  0.0565  204 A1BHC B C6  
2224 C  C6  D A1BHC I .   ? 0.6549 0.7108 0.2908 0.0952  0.0891  0.0565  204 A1BHC B C6  
2225 C  C7  C A1BHC I .   ? 0.6454 0.7027 0.2773 0.1056  0.0880  0.0614  204 A1BHC B C7  
2226 C  C7  D A1BHC I .   ? 0.6454 0.7027 0.2773 0.1056  0.0880  0.0614  204 A1BHC B C7  
2227 C  C8  C A1BHC I .   ? 0.6347 0.7034 0.2547 0.1228  0.0865  0.0714  204 A1BHC B C8  
2228 C  C8  D A1BHC I .   ? 0.6347 0.7034 0.2547 0.1228  0.0865  0.0714  204 A1BHC B C8  
2229 C  C10 C A1BHC I .   ? 0.6316 0.7000 0.2430 0.1382  0.0823  0.0738  204 A1BHC B C10 
2230 C  C10 D A1BHC I .   ? 0.6316 0.6999 0.2430 0.1382  0.0823  0.0738  204 A1BHC B C10 
2231 C  C13 C A1BHC I .   ? 0.6501 0.7479 0.2667 0.1413  0.0919  0.0927  204 A1BHC B C13 
2232 C  C13 D A1BHC I .   ? 0.6501 0.7479 0.2667 0.1413  0.0919  0.0927  204 A1BHC B C13 
2233 C  C15 C A1BHC I .   ? 0.6641 0.7889 0.2682 0.1676  0.0917  0.1091  204 A1BHC B C15 
2234 C  C15 D A1BHC I .   ? 0.6641 0.7889 0.2682 0.1676  0.0917  0.1091  204 A1BHC B C15 
2235 C  C17 C A1BHC I .   ? 0.6604 0.7834 0.2855 0.1493  0.0994  0.1139  204 A1BHC B C17 
2236 C  C17 D A1BHC I .   ? 0.6605 0.7834 0.2855 0.1493  0.0994  0.1139  204 A1BHC B C17 
2237 C  C20 C A1BHC I .   ? 0.6714 0.7300 0.3217 0.0787  0.0949  0.0530  204 A1BHC B C20 
2238 C  C20 D A1BHC I .   ? 0.6714 0.7300 0.3217 0.0787  0.0949  0.0530  204 A1BHC B C20 
2239 C  C21 C A1BHC I .   ? 0.6778 0.7332 0.3205 0.0762  0.0910  0.0474  204 A1BHC B C21 
2240 C  C21 D A1BHC I .   ? 0.6778 0.7333 0.3206 0.0762  0.0910  0.0474  204 A1BHC B C21 
2241 C  C1  C A1BHC I .   ? 0.7062 0.7538 0.3244 0.0692  0.0768  0.0354  204 A1BHC B C1  
2242 C  C1  D A1BHC I .   ? 0.7062 0.7538 0.3245 0.0692  0.0768  0.0354  204 A1BHC B C1  
2243 C  C2  C A1BHC I .   ? 0.7042 0.7614 0.3237 0.0788  0.0818  0.0455  204 A1BHC B C2  
2244 C  C2  D A1BHC I .   ? 0.7042 0.7614 0.3237 0.0788  0.0818  0.0455  204 A1BHC B C2  
2245 C  C3  C A1BHC I .   ? 0.7008 0.7484 0.3255 0.0797  0.0809  0.0410  204 A1BHC B C3  
2246 C  C3  D A1BHC I .   ? 0.7009 0.7484 0.3255 0.0797  0.0809  0.0410  204 A1BHC B C3  
2247 N  N2  C A1BHC I .   ? 0.6360 0.7005 0.2601 0.1130  0.0872  0.0664  204 A1BHC B N2  
2248 N  N2  D A1BHC I .   ? 0.6360 0.7005 0.2600 0.1130  0.0872  0.0664  204 A1BHC B N2  
2249 C  C9  C A1BHC I .   ? 0.6262 0.6894 0.2419 0.1282  0.0830  0.0690  204 A1BHC B C9  
2250 C  C9  D A1BHC I .   ? 0.6261 0.6894 0.2418 0.1282  0.0830  0.0690  204 A1BHC B C9  
2251 CL CL1 C A1BHC I .   ? 0.6130 0.6747 0.2189 0.1447  0.0775  0.0703  204 A1BHC B CL1 
2252 CL CL1 D A1BHC I .   ? 0.6129 0.6746 0.2188 0.1447  0.0775  0.0703  204 A1BHC B CL1 
2253 C  C11 C A1BHC I .   ? 0.6268 0.7060 0.2382 0.1427  0.0851  0.0814  204 A1BHC B C11 
2254 C  C11 D A1BHC I .   ? 0.6267 0.7060 0.2381 0.1427  0.0851  0.0814  204 A1BHC B C11 
2255 C  C12 C A1BHC I .   ? 0.6399 0.7246 0.2559 0.1371  0.0887  0.0842  204 A1BHC B C12 
2256 C  C12 D A1BHC I .   ? 0.6399 0.7246 0.2559 0.1371  0.0887  0.0842  204 A1BHC B C12 
2257 O  O1  C A1BHC I .   ? 0.6623 0.7649 0.2831 0.1360  0.0949  0.0950  204 A1BHC B O1  
2258 O  O1  D A1BHC I .   ? 0.6624 0.7649 0.2832 0.1360  0.0949  0.0950  204 A1BHC B O1  
2259 C  C14 C A1BHC I .   ? 0.6628 0.7823 0.2740 0.1565  0.0939  0.1064  204 A1BHC B C14 
2260 C  C14 D A1BHC I .   ? 0.6628 0.7823 0.2740 0.1564  0.0939  0.1064  204 A1BHC B C14 
2261 C  C16 C A1BHC I .   ? 0.6670 0.7931 0.2710 0.1582  0.0929  0.1052  204 A1BHC B C16 
2262 C  C16 D A1BHC I .   ? 0.6670 0.7932 0.2710 0.1582  0.0929  0.1052  204 A1BHC B C16 
2263 O  O2  C A1BHC I .   ? 0.6537 0.7694 0.2869 0.1469  0.1002  0.1148  204 A1BHC B O2  
2264 O  O2  D A1BHC I .   ? 0.6537 0.7694 0.2869 0.1469  0.1002  0.1148  204 A1BHC B O2  
2265 C  C18 C A1BHC I .   ? 0.6345 0.7135 0.2547 0.1273  0.0893  0.0790  204 A1BHC B C18 
2266 C  C18 D A1BHC I .   ? 0.6345 0.7135 0.2547 0.1273  0.0893  0.0790  204 A1BHC B C18 
2267 C  C19 C A1BHC I .   ? 0.6556 0.7146 0.3024 0.0881  0.0939  0.0579  204 A1BHC B C19 
2268 C  C19 D A1BHC I .   ? 0.6556 0.7145 0.3024 0.0881  0.0939  0.0579  204 A1BHC B C19 
2269 O  O3  C A1BHC I .   ? 0.7028 0.7592 0.3488 0.0668  0.0919  0.0429  204 A1BHC B O3  
2270 O  O3  D A1BHC I .   ? 0.7030 0.7594 0.3489 0.0668  0.0919  0.0429  204 A1BHC B O3  
2271 S  S   C SO4   J .   ? 1.1353 1.2909 0.6720 0.2380  0.0656  0.0952  205 SO4   B S   
2272 S  S   D SO4   J .   ? 1.1354 1.2909 0.6720 0.2380  0.0656  0.0952  205 SO4   B S   
2273 O  O1  C SO4   J .   ? 1.1411 1.2950 0.6696 0.2414  0.0614  0.0884  205 SO4   B O1  
2274 O  O1  D SO4   J .   ? 1.1411 1.2950 0.6696 0.2414  0.0614  0.0884  205 SO4   B O1  
2275 O  O2  C SO4   J .   ? 1.1147 1.2661 0.6634 0.2258  0.0711  0.0999  205 SO4   B O2  
2276 O  O2  D SO4   J .   ? 1.1147 1.2661 0.6634 0.2258  0.0711  0.0999  205 SO4   B O2  
2277 O  O3  C SO4   J .   ? 1.1431 1.3175 0.6777 0.2464  0.0682  0.1029  205 SO4   B O3  
2278 O  O3  D SO4   J .   ? 1.1431 1.3175 0.6778 0.2464  0.0682  0.1029  205 SO4   B O3  
2279 O  O4  C SO4   J .   ? 1.1432 1.2861 0.6783 0.2383  0.0615  0.0896  205 SO4   B O4  
2280 O  O4  D SO4   J .   ? 1.1432 1.2862 0.6784 0.2383  0.0615  0.0896  205 SO4   B O4  
2281 S  S   C DMS   K .   ? 1.2958 1.3304 1.0087 0.0620  0.1042  0.0333  206 DMS   B S   
2282 S  S   D DMS   K .   ? 1.2958 1.3304 1.0087 0.0620  0.1042  0.0333  206 DMS   B S   
2283 O  O   C DMS   K .   ? 1.2554 1.2903 0.9565 0.0708  0.1014  0.0394  206 DMS   B O   
2284 O  O   D DMS   K .   ? 1.2554 1.2903 0.9565 0.0708  0.1014  0.0394  206 DMS   B O   
2285 C  C1  C DMS   K .   ? 1.2766 1.3071 1.0047 0.0636  0.1063  0.0353  206 DMS   B C1  
2286 C  C1  D DMS   K .   ? 1.2766 1.3071 1.0047 0.0636  0.1063  0.0353  206 DMS   B C1  
2287 C  C2  C DMS   K .   ? 1.2897 1.3295 1.0068 0.0579  0.1075  0.0381  206 DMS   B C2  
2288 C  C2  D DMS   K .   ? 1.2897 1.3295 1.0068 0.0579  0.1075  0.0381  206 DMS   B C2  
2289 S  S   C DMS   L .   ? 1.2436 1.3559 0.9060 0.2157  0.0800  0.1611  207 DMS   B S   
2290 S  S   D DMS   L .   ? 1.2436 1.3559 0.9060 0.2157  0.0800  0.1611  207 DMS   B S   
2291 O  O   C DMS   L .   ? 1.2078 1.3207 0.8588 0.2156  0.0795  0.1533  207 DMS   B O   
2292 O  O   D DMS   L .   ? 1.2078 1.3207 0.8588 0.2156  0.0795  0.1533  207 DMS   B O   
2293 C  C1  C DMS   L .   ? 1.2507 1.3717 0.9019 0.2269  0.0757  0.1617  207 DMS   B C1  
2294 C  C1  D DMS   L .   ? 1.2507 1.3717 0.9019 0.2269  0.0757  0.1617  207 DMS   B C1  
2295 C  C2  C DMS   L .   ? 1.2346 1.3288 0.9060 0.2093  0.0785  0.1506  207 DMS   B C2  
2296 C  C2  D DMS   L .   ? 1.2346 1.3288 0.9060 0.2093  0.0785  0.1506  207 DMS   B C2  
2297 S  S   C DMS   M .   ? 1.3301 1.2697 0.8069 0.2250  -0.0648 -0.0226 208 DMS   B S   
2298 S  S   D DMS   M .   ? 1.3301 1.2697 0.8069 0.2250  -0.0648 -0.0226 208 DMS   B S   
2299 O  O   C DMS   M .   ? 1.2931 1.2319 0.7775 0.2153  -0.0611 -0.0202 208 DMS   B O   
2300 O  O   D DMS   M .   ? 1.2931 1.2319 0.7775 0.2153  -0.0611 -0.0202 208 DMS   B O   
2301 C  C1  C DMS   M .   ? 1.2974 1.2536 0.7753 0.2307  -0.0530 -0.0166 208 DMS   B C1  
2302 C  C1  D DMS   M .   ? 1.2974 1.2536 0.7753 0.2307  -0.0530 -0.0166 208 DMS   B C1  
2303 C  C2  C DMS   M .   ? 1.3363 1.2771 0.8041 0.2402  -0.0725 -0.0287 208 DMS   B C2  
2304 C  C2  D DMS   M .   ? 1.3363 1.2771 0.8041 0.2402  -0.0725 -0.0287 208 DMS   B C2  
# 
