data_7HA9
# 
_entry.id   7HA9 
# 
_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   7HA9         pdb_00007ha9 10.2210/pdb7ha9/pdb 
WWPDB D_1001407220 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HA9 
_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   2024-07-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              yufeng@sari.ac.cn 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9502-3277 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, L.' 1  ? 
'Wang, W.'  2  ? 
'Zhu, Z.'   3  ? 
'Li, Q.'    4  ? 
'Li, M.'    5  ? 
'Zhou, H.'  6  ? 
'Xu, Q.'    7  ? 
'Wen, W.'   8  ? 
'Wang, Q.'  9  ? 
'Yu, F.'    10 ? 
# 
_citation.id                        primary 
_citation.title                     
;Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening.
;
_citation.journal_abbrev            Iucrj 
_citation.journal_volume            12 
_citation.page_first                177 
_citation.page_last                 187 
_citation.year                      2025 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2052-2525 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   39819741 
_citation.pdbx_database_id_DOI      10.1107/S2052252524012247 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Huang, L.' 0009-0001-8431-0182 1  
primary 'Wang, W.'  ?                   2  
primary 'Zhu, Z.'   ?                   3  
primary 'Li, Q.'    ?                   4  
primary 'Li, M.'    ?                   5  
primary 'Zhou, H.'  ?                   6  
primary 'Xu, Q.'    0000-0002-7137-0768 7  
primary 'Wen, W.'   ?                   8  
primary 'Wang, Q.'  ?                   9  
primary 'Yu, F.'    0000-0002-9502-3277 10 
# 
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 'Heat shock protein HSP 90-alpha'                                                26859.117 1   3.6.4.10 ? ? ? 
2 non-polymer syn "N-[(1R,2S,4R)-bicyclo[2.2.1]heptan-2-yl]-N'-[(2S)-1-hydroxybutan-2-yl]thiourea" 242.381   1   ?        ? ? ? 
3 water       nat water                                                                            18.015    117 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Heat shock 86 kDa,HSP 86,HSP86,Heat shock protein family C member 1,Lipopolysaccharide-associated protein 2,LAP-2,LPS-associated protein 2,Renal carcinoma antigen NY-REN-38
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDR
TLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAG
GSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "N-[(1R,2S,4R)-bicyclo[2.2.1]heptan-2-yl]-N'-[(2S)-1-hydroxybutan-2-yl]thiourea" A1AW9 
3 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLN n 
1 4   PRO n 
1 5   MET n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   GLU n 
1 10  VAL n 
1 11  GLU n 
1 12  THR n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  GLN n 
1 17  ALA n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLN n 
1 22  LEU n 
1 23  MET n 
1 24  SER n 
1 25  LEU n 
1 26  ILE n 
1 27  ILE n 
1 28  ASN n 
1 29  THR n 
1 30  PHE n 
1 31  TYR n 
1 32  SER n 
1 33  ASN n 
1 34  LYS n 
1 35  GLU n 
1 36  ILE n 
1 37  PHE n 
1 38  LEU n 
1 39  ARG n 
1 40  GLU n 
1 41  LEU n 
1 42  ILE n 
1 43  SER n 
1 44  ASN n 
1 45  SER n 
1 46  SER n 
1 47  ASP n 
1 48  ALA n 
1 49  LEU n 
1 50  ASP n 
1 51  LYS n 
1 52  ILE n 
1 53  ARG n 
1 54  TYR n 
1 55  GLU n 
1 56  SER n 
1 57  LEU n 
1 58  THR n 
1 59  ASP n 
1 60  PRO n 
1 61  SER n 
1 62  LYS n 
1 63  LEU n 
1 64  ASP n 
1 65  SER n 
1 66  GLY n 
1 67  LYS n 
1 68  GLU n 
1 69  LEU n 
1 70  HIS n 
1 71  ILE n 
1 72  ASN n 
1 73  LEU n 
1 74  ILE n 
1 75  PRO n 
1 76  ASN n 
1 77  LYS n 
1 78  GLN n 
1 79  ASP n 
1 80  ARG n 
1 81  THR n 
1 82  LEU n 
1 83  THR n 
1 84  ILE n 
1 85  VAL n 
1 86  ASP n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  GLY n 
1 91  MET n 
1 92  THR n 
1 93  LYS n 
1 94  ALA n 
1 95  ASP n 
1 96  LEU n 
1 97  ILE n 
1 98  ASN n 
1 99  ASN n 
1 100 LEU n 
1 101 GLY n 
1 102 THR n 
1 103 ILE n 
1 104 ALA n 
1 105 LYS n 
1 106 SER n 
1 107 GLY n 
1 108 THR n 
1 109 LYS n 
1 110 ALA n 
1 111 PHE n 
1 112 MET n 
1 113 GLU n 
1 114 ALA n 
1 115 LEU n 
1 116 GLN n 
1 117 ALA n 
1 118 GLY n 
1 119 ALA n 
1 120 ASP n 
1 121 ILE n 
1 122 SER n 
1 123 MET n 
1 124 ILE n 
1 125 GLY n 
1 126 GLN n 
1 127 PHE n 
1 128 GLY n 
1 129 VAL n 
1 130 GLY n 
1 131 PHE n 
1 132 TYR n 
1 133 SER n 
1 134 ALA n 
1 135 TYR n 
1 136 LEU n 
1 137 VAL n 
1 138 ALA n 
1 139 GLU n 
1 140 LYS n 
1 141 VAL n 
1 142 THR n 
1 143 VAL n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 HIS n 
1 148 ASN n 
1 149 ASP n 
1 150 ASP n 
1 151 GLU n 
1 152 GLN n 
1 153 TYR n 
1 154 ALA n 
1 155 TRP n 
1 156 GLU n 
1 157 SER n 
1 158 SER n 
1 159 ALA n 
1 160 GLY n 
1 161 GLY n 
1 162 SER n 
1 163 PHE n 
1 164 THR n 
1 165 VAL n 
1 166 ARG n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 GLY n 
1 171 GLU n 
1 172 PRO n 
1 173 MET n 
1 174 GLY n 
1 175 ARG n 
1 176 GLY n 
1 177 THR n 
1 178 LYS n 
1 179 VAL n 
1 180 ILE n 
1 181 LEU n 
1 182 HIS n 
1 183 LEU n 
1 184 LYS n 
1 185 GLU n 
1 186 ASP n 
1 187 GLN n 
1 188 THR n 
1 189 GLU n 
1 190 TYR n 
1 191 LEU n 
1 192 GLU n 
1 193 GLU n 
1 194 ARG n 
1 195 ARG n 
1 196 ILE n 
1 197 LYS n 
1 198 GLU n 
1 199 ILE n 
1 200 VAL n 
1 201 LYS n 
1 202 LYS n 
1 203 HIS n 
1 204 SER n 
1 205 GLN n 
1 206 PHE n 
1 207 ILE n 
1 208 GLY n 
1 209 TYR n 
1 210 PRO n 
1 211 ILE n 
1 212 THR n 
1 213 LEU n 
1 214 PHE n 
1 215 VAL n 
1 216 GLU n 
1 217 LYS n 
1 218 GLU n 
1 219 ARG n 
1 220 ASP n 
1 221 LYS n 
1 222 GLU n 
1 223 VAL n 
1 224 SER n 
1 225 ASP n 
1 226 ASP n 
1 227 GLU n 
1 228 ALA n 
1 229 GLU n 
1 230 LEU n 
1 231 GLU n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   237 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90AA1, HSP90A, HSPC1, HSPCA' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1AW9 non-polymer         . "N-[(1R,2S,4R)-bicyclo[2.2.1]heptan-2-yl]-N'-[(2S)-1-hydroxybutan-2-yl]thiourea" ? 'C12 H22 N2 O S' 
242.381 
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 
GLN   'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                            ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                       ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   8   ?   ?   ?   A . n 
A 1 2   ASP 2   9   ?   ?   ?   A . n 
A 1 3   GLN 3   10  ?   ?   ?   A . n 
A 1 4   PRO 4   11  ?   ?   ?   A . n 
A 1 5   MET 5   12  ?   ?   ?   A . n 
A 1 6   GLU 6   13  ?   ?   ?   A . n 
A 1 7   GLU 7   14  ?   ?   ?   A . n 
A 1 8   GLU 8   15  ?   ?   ?   A . n 
A 1 9   GLU 9   16  16  GLU GLU A . n 
A 1 10  VAL 10  17  17  VAL VAL A . n 
A 1 11  GLU 11  18  18  GLU GLU A . n 
A 1 12  THR 12  19  19  THR THR A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  ALA 14  21  21  ALA ALA A . n 
A 1 15  PHE 15  22  22  PHE PHE A . n 
A 1 16  GLN 16  23  23  GLN GLN A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  GLU 18  25  25  GLU GLU A . n 
A 1 19  ILE 19  26  26  ILE ILE A . n 
A 1 20  ALA 20  27  27  ALA ALA A . n 
A 1 21  GLN 21  28  28  GLN GLN A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  MET 23  30  30  MET MET A . n 
A 1 24  SER 24  31  31  SER SER A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  ILE 26  33  33  ILE ILE A . n 
A 1 27  ILE 27  34  34  ILE ILE A . n 
A 1 28  ASN 28  35  35  ASN ASN A . n 
A 1 29  THR 29  36  36  THR THR A . n 
A 1 30  PHE 30  37  37  PHE PHE A . n 
A 1 31  TYR 31  38  38  TYR TYR A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ASN 33  40  40  ASN ASN A . n 
A 1 34  LYS 34  41  41  LYS LYS A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  PHE 37  44  44  PHE PHE A . n 
A 1 38  LEU 38  45  45  LEU LEU A . n 
A 1 39  ARG 39  46  46  ARG ARG A . n 
A 1 40  GLU 40  47  47  GLU GLU A . n 
A 1 41  LEU 41  48  48  LEU LEU A . n 
A 1 42  ILE 42  49  49  ILE ILE A . n 
A 1 43  SER 43  50  50  SER SER A . n 
A 1 44  ASN 44  51  51  ASN ASN A . n 
A 1 45  SER 45  52  52  SER SER A . n 
A 1 46  SER 46  53  53  SER SER A . n 
A 1 47  ASP 47  54  54  ASP ASP A . n 
A 1 48  ALA 48  55  55  ALA ALA A . n 
A 1 49  LEU 49  56  56  LEU LEU A . n 
A 1 50  ASP 50  57  57  ASP ASP A . n 
A 1 51  LYS 51  58  58  LYS LYS A . n 
A 1 52  ILE 52  59  59  ILE ILE A . n 
A 1 53  ARG 53  60  60  ARG ARG A . n 
A 1 54  TYR 54  61  61  TYR TYR A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  SER 56  63  63  SER SER A . n 
A 1 57  LEU 57  64  64  LEU LEU A . n 
A 1 58  THR 58  65  65  THR THR A . n 
A 1 59  ASP 59  66  66  ASP ASP A . n 
A 1 60  PRO 60  67  67  PRO PRO A . n 
A 1 61  SER 61  68  68  SER SER A . n 
A 1 62  LYS 62  69  69  LYS LYS A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ASP 64  71  71  ASP ASP A . n 
A 1 65  SER 65  72  72  SER SER A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  LYS 67  74  74  LYS LYS A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  LEU 69  76  76  LEU LEU A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  ILE 71  78  78  ILE ILE A . n 
A 1 72  ASN 72  79  79  ASN ASN A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  ILE 74  81  81  ILE ILE A . n 
A 1 75  PRO 75  82  82  PRO PRO A . n 
A 1 76  ASN 76  83  83  ASN ASN A . n 
A 1 77  LYS 77  84  84  LYS LYS A . n 
A 1 78  GLN 78  85  85  GLN GLN A . n 
A 1 79  ASP 79  86  86  ASP ASP A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  THR 81  88  88  THR THR A . n 
A 1 82  LEU 82  89  89  LEU LEU A . n 
A 1 83  THR 83  90  90  THR THR A . n 
A 1 84  ILE 84  91  91  ILE ILE A . n 
A 1 85  VAL 85  92  92  VAL VAL A . n 
A 1 86  ASP 86  93  93  ASP ASP A . n 
A 1 87  THR 87  94  94  THR THR A . n 
A 1 88  GLY 88  95  95  GLY GLY A . n 
A 1 89  ILE 89  96  96  ILE ILE A . n 
A 1 90  GLY 90  97  97  GLY GLY A . n 
A 1 91  MET 91  98  98  MET MET A . n 
A 1 92  THR 92  99  99  THR THR A . n 
A 1 93  LYS 93  100 100 LYS LYS A . n 
A 1 94  ALA 94  101 101 ALA ALA A . n 
A 1 95  ASP 95  102 102 ASP ASP A . n 
A 1 96  LEU 96  103 103 LEU LEU A . n 
A 1 97  ILE 97  104 104 ILE ILE A . n 
A 1 98  ASN 98  105 105 ASN ASN A . n 
A 1 99  ASN 99  106 106 ASN ASN A . n 
A 1 100 LEU 100 107 107 LEU LEU A . n 
A 1 101 GLY 101 108 108 GLY GLY A . n 
A 1 102 THR 102 109 109 THR THR A . n 
A 1 103 ILE 103 110 110 ILE ILE A . n 
A 1 104 ALA 104 111 111 ALA ALA A . n 
A 1 105 LYS 105 112 112 LYS LYS A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 THR 108 115 115 THR THR A . n 
A 1 109 LYS 109 116 116 LYS LYS A . n 
A 1 110 ALA 110 117 117 ALA ALA A . n 
A 1 111 PHE 111 118 118 PHE PHE A . n 
A 1 112 MET 112 119 119 MET MET A . n 
A 1 113 GLU 113 120 120 GLU GLU A . n 
A 1 114 ALA 114 121 121 ALA ALA A . n 
A 1 115 LEU 115 122 122 LEU LEU A . n 
A 1 116 GLN 116 123 123 GLN GLN A . n 
A 1 117 ALA 117 124 124 ALA ALA A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 ALA 119 126 126 ALA ALA A . n 
A 1 120 ASP 120 127 127 ASP ASP A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 SER 122 129 129 SER SER A . n 
A 1 123 MET 123 130 130 MET MET A . n 
A 1 124 ILE 124 131 131 ILE ILE A . n 
A 1 125 GLY 125 132 132 GLY GLY A . n 
A 1 126 GLN 126 133 133 GLN GLN A . n 
A 1 127 PHE 127 134 134 PHE PHE A . n 
A 1 128 GLY 128 135 135 GLY GLY A . n 
A 1 129 VAL 129 136 136 VAL VAL A . n 
A 1 130 GLY 130 137 137 GLY GLY A . n 
A 1 131 PHE 131 138 138 PHE PHE A . n 
A 1 132 TYR 132 139 139 TYR TYR A . n 
A 1 133 SER 133 140 140 SER SER A . n 
A 1 134 ALA 134 141 141 ALA ALA A . n 
A 1 135 TYR 135 142 142 TYR TYR A . n 
A 1 136 LEU 136 143 143 LEU LEU A . n 
A 1 137 VAL 137 144 144 VAL VAL A . n 
A 1 138 ALA 138 145 145 ALA ALA A . n 
A 1 139 GLU 139 146 146 GLU GLU A . n 
A 1 140 LYS 140 147 147 LYS LYS A . n 
A 1 141 VAL 141 148 148 VAL VAL A . n 
A 1 142 THR 142 149 149 THR THR A . n 
A 1 143 VAL 143 150 150 VAL VAL A . n 
A 1 144 ILE 144 151 151 ILE ILE A . n 
A 1 145 THR 145 152 152 THR THR A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 HIS 147 154 154 HIS HIS A . n 
A 1 148 ASN 148 155 155 ASN ASN A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 ASP 150 157 157 ASP ASP A . n 
A 1 151 GLU 151 158 158 GLU GLU A . n 
A 1 152 GLN 152 159 159 GLN GLN A . n 
A 1 153 TYR 153 160 160 TYR TYR A . n 
A 1 154 ALA 154 161 161 ALA ALA A . n 
A 1 155 TRP 155 162 162 TRP TRP A . n 
A 1 156 GLU 156 163 163 GLU GLU A . n 
A 1 157 SER 157 164 164 SER SER A . n 
A 1 158 SER 158 165 165 SER SER A . n 
A 1 159 ALA 159 166 166 ALA ALA A . n 
A 1 160 GLY 160 167 167 GLY GLY A . n 
A 1 161 GLY 161 168 168 GLY GLY A . n 
A 1 162 SER 162 169 169 SER SER A . n 
A 1 163 PHE 163 170 170 PHE PHE A . n 
A 1 164 THR 164 171 171 THR THR A . n 
A 1 165 VAL 165 172 172 VAL VAL A . n 
A 1 166 ARG 166 173 173 ARG ARG A . n 
A 1 167 THR 167 174 174 THR THR A . n 
A 1 168 ASP 168 175 175 ASP ASP A . n 
A 1 169 THR 169 176 176 THR THR A . n 
A 1 170 GLY 170 177 177 GLY GLY A . n 
A 1 171 GLU 171 178 178 GLU GLU A . n 
A 1 172 PRO 172 179 179 PRO PRO A . n 
A 1 173 MET 173 180 180 MET MET A . n 
A 1 174 GLY 174 181 181 GLY GLY A . n 
A 1 175 ARG 175 182 182 ARG ARG A . n 
A 1 176 GLY 176 183 183 GLY GLY A . n 
A 1 177 THR 177 184 184 THR THR A . n 
A 1 178 LYS 178 185 185 LYS LYS A . n 
A 1 179 VAL 179 186 186 VAL VAL A . n 
A 1 180 ILE 180 187 187 ILE ILE A . n 
A 1 181 LEU 181 188 188 LEU LEU A . n 
A 1 182 HIS 182 189 189 HIS HIS A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 GLU 185 192 192 GLU GLU A . n 
A 1 186 ASP 186 193 193 ASP ASP A . n 
A 1 187 GLN 187 194 194 GLN GLN A . n 
A 1 188 THR 188 195 195 THR THR A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 TYR 190 197 197 TYR TYR A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 GLU 192 199 199 GLU GLU A . n 
A 1 193 GLU 193 200 200 GLU GLU A . n 
A 1 194 ARG 194 201 201 ARG ARG A . n 
A 1 195 ARG 195 202 202 ARG ARG A . n 
A 1 196 ILE 196 203 203 ILE ILE A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 GLU 198 205 205 GLU GLU A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 VAL 200 207 207 VAL VAL A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 LYS 202 209 209 LYS LYS A . n 
A 1 203 HIS 203 210 210 HIS HIS A . n 
A 1 204 SER 204 211 211 SER SER A . n 
A 1 205 GLN 205 212 212 GLN GLN A . n 
A 1 206 PHE 206 213 213 PHE PHE A . n 
A 1 207 ILE 207 214 214 ILE ILE A . n 
A 1 208 GLY 208 215 215 GLY GLY A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 PRO 210 217 217 PRO PRO A . n 
A 1 211 ILE 211 218 218 ILE ILE A . n 
A 1 212 THR 212 219 219 THR THR A . n 
A 1 213 LEU 213 220 220 LEU LEU A . n 
A 1 214 PHE 214 221 221 PHE PHE A . n 
A 1 215 VAL 215 222 222 VAL VAL A . n 
A 1 216 GLU 216 223 223 GLU GLU A . n 
A 1 217 LYS 217 224 224 LYS LYS A . n 
A 1 218 GLU 218 225 ?   ?   ?   A . n 
A 1 219 ARG 219 226 ?   ?   ?   A . n 
A 1 220 ASP 220 227 ?   ?   ?   A . n 
A 1 221 LYS 221 228 ?   ?   ?   A . n 
A 1 222 GLU 222 229 ?   ?   ?   A . n 
A 1 223 VAL 223 230 ?   ?   ?   A . n 
A 1 224 SER 224 231 ?   ?   ?   A . n 
A 1 225 ASP 225 232 ?   ?   ?   A . n 
A 1 226 ASP 226 233 ?   ?   ?   A . n 
A 1 227 GLU 227 234 ?   ?   ?   A . n 
A 1 228 ALA 228 235 ?   ?   ?   A . n 
A 1 229 GLU 229 236 ?   ?   ?   A . n 
A 1 230 LEU 230 237 ?   ?   ?   A . n 
A 1 231 GLU 231 238 ?   ?   ?   A . n 
A 1 232 HIS 232 239 ?   ?   ?   A . n 
A 1 233 HIS 233 240 ?   ?   ?   A . n 
A 1 234 HIS 234 241 ?   ?   ?   A . n 
A 1 235 HIS 235 242 ?   ?   ?   A . n 
A 1 236 HIS 236 243 ?   ?   ?   A . n 
A 1 237 HIS 237 244 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AW9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AW9 
_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 
B 2 A1AW9 1   301 301 A1AW9 DWR A . 
C 3 HOH   1   401 24  HOH   HOH A . 
C 3 HOH   2   402 106 HOH   HOH A . 
C 3 HOH   3   403 9   HOH   HOH A . 
C 3 HOH   4   404 90  HOH   HOH A . 
C 3 HOH   5   405 55  HOH   HOH A . 
C 3 HOH   6   406 77  HOH   HOH A . 
C 3 HOH   7   407 43  HOH   HOH A . 
C 3 HOH   8   408 35  HOH   HOH A . 
C 3 HOH   9   409 41  HOH   HOH A . 
C 3 HOH   10  410 37  HOH   HOH A . 
C 3 HOH   11  411 72  HOH   HOH A . 
C 3 HOH   12  412 19  HOH   HOH A . 
C 3 HOH   13  413 94  HOH   HOH A . 
C 3 HOH   14  414 97  HOH   HOH A . 
C 3 HOH   15  415 25  HOH   HOH A . 
C 3 HOH   16  416 8   HOH   HOH A . 
C 3 HOH   17  417 13  HOH   HOH A . 
C 3 HOH   18  418 93  HOH   HOH A . 
C 3 HOH   19  419 32  HOH   HOH A . 
C 3 HOH   20  420 59  HOH   HOH A . 
C 3 HOH   21  421 30  HOH   HOH A . 
C 3 HOH   22  422 2   HOH   HOH A . 
C 3 HOH   23  423 40  HOH   HOH A . 
C 3 HOH   24  424 7   HOH   HOH A . 
C 3 HOH   25  425 3   HOH   HOH A . 
C 3 HOH   26  426 46  HOH   HOH A . 
C 3 HOH   27  427 75  HOH   HOH A . 
C 3 HOH   28  428 57  HOH   HOH A . 
C 3 HOH   29  429 111 HOH   HOH A . 
C 3 HOH   30  430 6   HOH   HOH A . 
C 3 HOH   31  431 65  HOH   HOH A . 
C 3 HOH   32  432 20  HOH   HOH A . 
C 3 HOH   33  433 45  HOH   HOH A . 
C 3 HOH   34  434 22  HOH   HOH A . 
C 3 HOH   35  435 44  HOH   HOH A . 
C 3 HOH   36  436 47  HOH   HOH A . 
C 3 HOH   37  437 51  HOH   HOH A . 
C 3 HOH   38  438 56  HOH   HOH A . 
C 3 HOH   39  439 1   HOH   HOH A . 
C 3 HOH   40  440 4   HOH   HOH A . 
C 3 HOH   41  441 71  HOH   HOH A . 
C 3 HOH   42  442 109 HOH   HOH A . 
C 3 HOH   43  443 21  HOH   HOH A . 
C 3 HOH   44  444 83  HOH   HOH A . 
C 3 HOH   45  445 16  HOH   HOH A . 
C 3 HOH   46  446 11  HOH   HOH A . 
C 3 HOH   47  447 28  HOH   HOH A . 
C 3 HOH   48  448 17  HOH   HOH A . 
C 3 HOH   49  449 31  HOH   HOH A . 
C 3 HOH   50  450 50  HOH   HOH A . 
C 3 HOH   51  451 36  HOH   HOH A . 
C 3 HOH   52  452 79  HOH   HOH A . 
C 3 HOH   53  453 23  HOH   HOH A . 
C 3 HOH   54  454 52  HOH   HOH A . 
C 3 HOH   55  455 34  HOH   HOH A . 
C 3 HOH   56  456 67  HOH   HOH A . 
C 3 HOH   57  457 10  HOH   HOH A . 
C 3 HOH   58  458 18  HOH   HOH A . 
C 3 HOH   59  459 12  HOH   HOH A . 
C 3 HOH   60  460 26  HOH   HOH A . 
C 3 HOH   61  461 62  HOH   HOH A . 
C 3 HOH   62  462 29  HOH   HOH A . 
C 3 HOH   63  463 27  HOH   HOH A . 
C 3 HOH   64  464 66  HOH   HOH A . 
C 3 HOH   65  465 5   HOH   HOH A . 
C 3 HOH   66  466 74  HOH   HOH A . 
C 3 HOH   67  467 48  HOH   HOH A . 
C 3 HOH   68  468 98  HOH   HOH A . 
C 3 HOH   69  469 88  HOH   HOH A . 
C 3 HOH   70  470 84  HOH   HOH A . 
C 3 HOH   71  471 107 HOH   HOH A . 
C 3 HOH   72  472 91  HOH   HOH A . 
C 3 HOH   73  473 92  HOH   HOH A . 
C 3 HOH   74  474 60  HOH   HOH A . 
C 3 HOH   75  475 33  HOH   HOH A . 
C 3 HOH   76  476 103 HOH   HOH A . 
C 3 HOH   77  477 105 HOH   HOH A . 
C 3 HOH   78  478 110 HOH   HOH A . 
C 3 HOH   79  479 80  HOH   HOH A . 
C 3 HOH   80  480 61  HOH   HOH A . 
C 3 HOH   81  481 38  HOH   HOH A . 
C 3 HOH   82  482 102 HOH   HOH A . 
C 3 HOH   83  483 117 HOH   HOH A . 
C 3 HOH   84  484 15  HOH   HOH A . 
C 3 HOH   85  485 116 HOH   HOH A . 
C 3 HOH   86  486 54  HOH   HOH A . 
C 3 HOH   87  487 39  HOH   HOH A . 
C 3 HOH   88  488 108 HOH   HOH A . 
C 3 HOH   89  489 70  HOH   HOH A . 
C 3 HOH   90  490 82  HOH   HOH A . 
C 3 HOH   91  491 86  HOH   HOH A . 
C 3 HOH   92  492 76  HOH   HOH A . 
C 3 HOH   93  493 112 HOH   HOH A . 
C 3 HOH   94  494 14  HOH   HOH A . 
C 3 HOH   95  495 78  HOH   HOH A . 
C 3 HOH   96  496 63  HOH   HOH A . 
C 3 HOH   97  497 89  HOH   HOH A . 
C 3 HOH   98  498 69  HOH   HOH A . 
C 3 HOH   99  499 85  HOH   HOH A . 
C 3 HOH   100 500 49  HOH   HOH A . 
C 3 HOH   101 501 99  HOH   HOH A . 
C 3 HOH   102 502 113 HOH   HOH A . 
C 3 HOH   103 503 101 HOH   HOH A . 
C 3 HOH   104 504 53  HOH   HOH A . 
C 3 HOH   105 505 104 HOH   HOH A . 
C 3 HOH   106 506 58  HOH   HOH A . 
C 3 HOH   107 507 87  HOH   HOH A . 
C 3 HOH   108 508 73  HOH   HOH A . 
C 3 HOH   109 509 114 HOH   HOH A . 
C 3 HOH   110 510 42  HOH   HOH A . 
C 3 HOH   111 511 68  HOH   HOH A . 
C 3 HOH   112 512 115 HOH   HOH A . 
C 3 HOH   113 513 96  HOH   HOH A . 
C 3 HOH   114 514 95  HOH   HOH A . 
C 3 HOH   115 515 81  HOH   HOH A . 
C 3 HOH   116 516 100 HOH   HOH A . 
C 3 HOH   117 517 64  HOH   HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 XDS         .           ?               package 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/     ?   ? 
2 Aimless     0.7.7       23/04/21        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 DIMPLE      .           ?               program 'Marcin Wojdyr'   wojdyr@gmail.com                        phasing           
http://ccp4.github.io/dimple/                       ?   ? 
4 PHENIX      1.20.1_4487 ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                       C++ ? 
5 PDB_EXTRACT 3.28        'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
# 
_cell.volume             596196.301 
_cell.length_a           69.780 
_cell.length_b           88.410 
_cell.length_c           96.640 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           7HA9 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.entry_id                         7HA9 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HA9 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.88 
_exptl_crystal.density_percent_sol   57.23 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '100mM Tris-HCl pH 8.5, 22% PEG4000, 200mM MgCl2' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER X 16M' 
_diffrn_detector.pdbx_collection_date   2024-01-13 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    Si111 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97919 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.pdbx_wavelength_list        0.97919 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HA9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.270 
_reflns.d_resolution_high            2.000 
_reflns.number_obs                   20546 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.080 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        19.400 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              12.900 
_reflns.pdbx_Rrim_I_all              0.084 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     265330 
_reflns.pdbx_scaling_rejects         58 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 2.000 2.050  ? 20116 1520 ? 1.561 ? ? ? 13.200 ? 1.900  ? ? ? ? ? ? 99.800 1.623 0.440 0.642 
1 2 8.940 30.270 ? 2249  252  ? 0.039 ? ? ? 8.900  ? 44.300 ? ? ? ? ? ? 94.200 0.042 0.014 0.998 
# 
_refine.entry_id                                 7HA9 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.pdbx_overall_phase_error                 25.0707 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_R_factor_obs                          0.2016 
_refine.B_iso_mean                               51.55 
_refine.ls_number_reflns_R_free                  1016 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_R_factor_R_work                       0.2002 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            2.00 
_refine.ls_number_reflns_obs                     20534 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.ls_number_reflns_R_work                  19518 
_refine.ls_d_res_low                             27.39 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.2300 
_refine.overall_SU_ML                            0.2864 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               1777 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        27.39 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.dev_ideal_target 
'X-RAY DIFFRACTION' f_bond_d           1687 0.0016 ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2274 0.4681 ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     263  0.0386 ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      288  0.0026 ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 236  7.3085 ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' 2.00 2.11  2758 0.2871 99.83 0.3672 138 . . . . . 
'X-RAY DIFFRACTION' 2.11 2.24  2751 0.2468 99.86 0.2730 141 . . . . . 
'X-RAY DIFFRACTION' 2.24 2.41  2757 0.2331 99.93 0.2693 142 . . . . . 
'X-RAY DIFFRACTION' 2.41 2.65  2763 0.2350 99.97 0.2387 148 . . . . . 
'X-RAY DIFFRACTION' 2.65 3.04  2768 0.2291 99.86 0.2894 156 . . . . . 
'X-RAY DIFFRACTION' 3.04 3.82  2798 0.1989 99.97 0.2254 159 . . . . . 
'X-RAY DIFFRACTION' 3.82 27.39 2923 0.1687 99.29 0.1869 132 . . . . . 
# 
_struct.entry_id                  7HA9 
_struct.title                     'PanDDA analysis group deposition -- Crystal structure of HSP90N in complex with Fr13551' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HA9 
_struct_keywords.pdbx_keywords   CHAPERONE 
_struct_keywords.text            
'Crystallographic Fragment Screening; Fragment-Based Drug Discovery (FBDD); Heat shock protein 90 (HSP90), CHAPERONE' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HS90A_HUMAN 
_struct_ref.pdbx_db_accession          P07900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRT
LTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGG
SFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAE
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HA9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07900 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  236 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       236 
# 
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 7HA9 MET A 1   ? UNP P07900 ? ? 'initiating methionine' 8   1 
1 7HA9 LEU A 230 ? UNP P07900 ? ? 'expression tag'        237 2 
1 7HA9 GLU A 231 ? UNP P07900 ? ? 'expression tag'        238 3 
1 7HA9 HIS A 232 ? UNP P07900 ? ? 'expression tag'        239 4 
1 7HA9 HIS A 233 ? UNP P07900 ? ? 'expression tag'        240 5 
1 7HA9 HIS A 234 ? UNP P07900 ? ? 'expression tag'        241 6 
1 7HA9 HIS A 235 ? UNP P07900 ? ? 'expression tag'        242 7 
1 7HA9 HIS A 236 ? UNP P07900 ? ? 'expression tag'        243 8 
1 7HA9 HIS A 237 ? UNP P07900 ? ? 'expression tag'        244 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLN A 16  ? THR A 29  ? GLN A 23  THR A 36  1 ? 14 
HELX_P HELX_P2 AA2 GLU A 35  ? ASP A 59  ? GLU A 42  ASP A 66  1 ? 25 
HELX_P HELX_P3 AA3 PRO A 60  ? ASP A 64  ? PRO A 67  ASP A 71  5 ? 5  
HELX_P HELX_P4 AA4 THR A 92  ? ASN A 98  ? THR A 99  ASN A 105 1 ? 7  
HELX_P HELX_P5 AA5 ASN A 98  ? ALA A 117 ? ASN A 105 ALA A 124 1 ? 20 
HELX_P HELX_P6 AA6 ASP A 120 ? GLY A 128 ? ASP A 127 GLY A 135 5 ? 9  
HELX_P HELX_P7 AA7 VAL A 129 ? LEU A 136 ? VAL A 136 LEU A 143 5 ? 8  
HELX_P HELX_P8 AA8 GLU A 185 ? LEU A 191 ? GLU A 192 LEU A 198 5 ? 7  
HELX_P HELX_P9 AA9 GLU A 192 ? SER A 204 ? GLU A 199 SER A 211 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 VAL A 10  ? ALA A 14  ? VAL A 17  ALA A 21  
AA1 2 SER A 162 ? THR A 167 ? SER A 169 THR A 174 
AA1 3 GLN A 152 ? SER A 157 ? GLN A 159 SER A 164 
AA1 4 ALA A 138 ? LYS A 146 ? ALA A 145 LYS A 153 
AA1 5 GLY A 176 ? LEU A 183 ? GLY A 183 LEU A 190 
AA1 6 THR A 81  ? ASP A 86  ? THR A 88  ASP A 93  
AA1 7 ILE A 71  ? ASN A 76  ? ILE A 78  ASN A 83  
AA1 8 ILE A 211 ? LEU A 213 ? ILE A 218 LEU A 220 
# 
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 N PHE A 13  ? N PHE A 20  O PHE A 163 ? O PHE A 170 
AA1 2 3 O ARG A 166 ? O ARG A 173 N ALA A 154 ? N ALA A 161 
AA1 3 4 O TRP A 155 ? O TRP A 162 N VAL A 143 ? N VAL A 150 
AA1 4 5 N ILE A 144 ? N ILE A 151 O LYS A 178 ? O LYS A 185 
AA1 5 6 O VAL A 179 ? O VAL A 186 N ILE A 84  ? N ILE A 91  
AA1 6 7 O THR A 83  ? O THR A 90  N ILE A 74  ? N ILE A 81  
AA1 7 8 N LEU A 73  ? N LEU A 80  O THR A 212 ? O THR A 219 
# 
_pdbx_entry_details.entry_id                   7HA9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 499 ? ? O A HOH 507 ? ? 1.84 
2 1 O   A HOH 403 ? ? O A HOH 411 ? ? 2.10 
3 1 O   A HOH 464 ? ? O A HOH 476 ? ? 2.11 
4 1 ND2 A ASN 106 ? ? O A HOH 401 ? ? 2.13 
5 1 O   A HOH 497 ? ? O A HOH 503 ? ? 2.15 
# 
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 ASN A 105 ? ? -124.50 -62.90  
2 1 ALA A 166 ? ? 60.91   -146.63 
3 1 ARG A 182 ? ? -170.52 140.07  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.pdbx_refine_id 
_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] 
1 ? 'X-RAY DIFFRACTION' refined 13.7784583812  27.306879741  30.8992878999 0.408032458814 0.429011068562 0.441255302214 
0.0192389305685   -0.0949342524972 0.0211616411927  4.06899532577 3.18709203507 5.94013470931 -1.04551709953  -2.48311330701  
0.858161673905  0.0412693014883  -0.417110347604  -0.172501082149 0.3301785873    -0.12921932436   -0.279617906711   
0.022951749899   0.377827270357    0.119645557492    
2 ? 'X-RAY DIFFRACTION' refined -6.54024942895 37.3202050562 22.746520536  0.348223198295 0.377388467409 0.385484015288 
-0.00748234226812 -0.0278479107791 -0.0159565832004 1.86619351688 4.07909992342 4.22425561263 -1.24887911252  0.524359724229  
-3.33971268629  0.017697914151   0.167755851399   0.036537301156  0.242001666748  0.0380581547461  0.103236304746    
-0.232951233659  0.0622466580259   -0.00148485912839 
3 ? 'X-RAY DIFFRACTION' refined -2.67340640437 25.6798808427 24.7568207247 0.358806404546 0.318862795898 0.317033152707 
-0.00377772063396 -0.0844114365846 -0.0107769832635 3.68812362    3.46508049438 2.82926046508 -0.198874577885 -2.00473236249  
-0.917883160635 -0.0382601347119 -0.0995878885566 -0.151062066581 0.0173531905623 0.06627917975    -0.00881927801173 0.34949038185 
-0.00535769674052 -0.0500326083284  
4 ? 'X-RAY DIFFRACTION' refined 12.4264528383  38.8597379954 33.9294019811 0.517344933307 0.494732709612 0.542509385504 
-0.12804095622    -0.137780841979  -0.0304753288547 6.73514751692 7.12507431831 6.38028546876 -0.808677186298 0.535545568748  
-2.25953508027  -0.0450168028337 -0.745587798158  0.906249634868  0.904783759496  -0.26439418941   -0.420869012954   
-0.774243246415  1.04296560064     0.218382245038    
5 ? 'X-RAY DIFFRACTION' refined 2.8780340396   24.5959642864 21.7747305405 0.341161599048 0.274149243381 0.367354346055 
0.00128353600593  -0.0697721595594 -0.0446982364903 3.84978617138 3.01066552692 3.10682025521 -0.840927666799 -0.242121194285 
-1.03531718371  0.120177507661   0.206987028071   -0.352492757112 -0.32613135983  -0.0126936591654 0.116371315221    
0.377230129145   0.0737825573146   -0.132135052927   
6 ? 'X-RAY DIFFRACTION' refined -5.68582962387 24.3343284079 41.2921483998 0.530111953702 0.549708451115 0.359712650397 
0.0313267933427   0.0160006737197  0.134725214638   7.85886771351 5.4271004824  3.69767780838 -3.42026017933  -0.494602945347 
0.75747876763   -0.345292982134  -0.888767900334  -0.235810267916 0.696438245211  0.396924132619   0.255921050907    
-0.0530641262698 -0.248368275984   0.0117329829284   
7 ? 'X-RAY DIFFRACTION' refined -13.030413865  30.1825221516 32.378722366  0.439135525932 0.402008709838 0.379452392677 
0.0485602893052   0.00920286043587 0.0230991739425  4.83802748759 4.06406637363 4.66354271235 -1.1327161316   -0.206913259703 
-3.11232209884  -0.17209904125   -0.250885659428  -0.178581496773 0.936516540055  0.277731421837   -0.430122664148   
-0.485381647623  -0.461932609661   -0.10792323762    
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.pdbx_refine_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 
1 1 'X-RAY DIFFRACTION' A 16  A 1   A 40  A 25  . 
;chain 'A' and (resid 16 through 40 )
;
2 2 'X-RAY DIFFRACTION' A 41  A 26  A 76  A 61  . 
;chain 'A' and (resid 41 through 76 )
;
3 3 'X-RAY DIFFRACTION' A 77  A 62  A 105 A 90  . 
;chain 'A' and (resid 77 through 105 )
;
4 4 'X-RAY DIFFRACTION' A 106 A 91  A 136 A 121 . 
;chain 'A' and (resid 106 through 136 )
;
5 5 'X-RAY DIFFRACTION' A 137 A 122 A 190 A 175 . 
;chain 'A' and (resid 137 through 190 )
;
6 6 'X-RAY DIFFRACTION' A 191 A 176 A 210 A 195 . 
;chain 'A' and (resid 191 through 210 )
;
7 7 'X-RAY DIFFRACTION' A 211 A 196 A 224 A 209 . 
;chain 'A' and (resid 211 through 224 )
;
# 
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 MET 8   ? A MET 1   
2  1 Y 1 A ASP 9   ? A ASP 2   
3  1 Y 1 A GLN 10  ? A GLN 3   
4  1 Y 1 A PRO 11  ? A PRO 4   
5  1 Y 1 A MET 12  ? A MET 5   
6  1 Y 1 A GLU 13  ? A GLU 6   
7  1 Y 1 A GLU 14  ? A GLU 7   
8  1 Y 1 A GLU 15  ? A GLU 8   
9  1 Y 1 A GLU 225 ? A GLU 218 
10 1 Y 1 A ARG 226 ? A ARG 219 
11 1 Y 1 A ASP 227 ? A ASP 220 
12 1 Y 1 A LYS 228 ? A LYS 221 
13 1 Y 1 A GLU 229 ? A GLU 222 
14 1 Y 1 A VAL 230 ? A VAL 223 
15 1 Y 1 A SER 231 ? A SER 224 
16 1 Y 1 A ASP 232 ? A ASP 225 
17 1 Y 1 A ASP 233 ? A ASP 226 
18 1 Y 1 A GLU 234 ? A GLU 227 
19 1 Y 1 A ALA 235 ? A ALA 228 
20 1 Y 1 A GLU 236 ? A GLU 229 
21 1 Y 1 A LEU 237 ? A LEU 230 
22 1 Y 1 A GLU 238 ? A GLU 231 
23 1 Y 1 A HIS 239 ? A HIS 232 
24 1 Y 1 A HIS 240 ? A HIS 233 
25 1 Y 1 A HIS 241 ? A HIS 234 
26 1 Y 1 A HIS 242 ? A HIS 235 
27 1 Y 1 A HIS 243 ? A HIS 236 
28 1 Y 1 A HIS 244 ? A HIS 237 
# 
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 
A1AW9 C1   C N N 1   
A1AW9 C10  C N N 2   
A1AW9 C11  C N S 3   
A1AW9 C12  C N N 4   
A1AW9 C2   C N N 5   
A1AW9 C3   C N R 6   
A1AW9 C4   C N N 7   
A1AW9 C5   C N N 8   
A1AW9 C6   C N R 9   
A1AW9 C7   C N N 10  
A1AW9 C8   C N R 11  
A1AW9 C9   C N N 12  
A1AW9 O1   O N N 13  
A1AW9 N1   N N N 14  
A1AW9 N2   N N N 15  
A1AW9 S1   S N N 16  
A1AW9 H3   H N N 17  
A1AW9 H2   H N N 18  
A1AW9 H1   H N N 19  
A1AW9 H18  H N N 20  
A1AW9 H19  H N N 21  
A1AW9 H20  H N N 22  
A1AW9 H21  H N N 23  
A1AW9 H22  H N N 24  
A1AW9 H5   H N N 25  
A1AW9 H4   H N N 26  
A1AW9 H6   H N N 27  
A1AW9 H8   H N N 28  
A1AW9 H7   H N N 29  
A1AW9 H12  H N N 30  
A1AW9 H14  H N N 31  
A1AW9 H13  H N N 32  
A1AW9 H15  H N N 33  
A1AW9 H16  H N N 34  
A1AW9 H17  H N N 35  
A1AW9 H9   H N N 36  
A1AW9 H10  H N N 37  
A1AW9 H11  H N N 38  
ALA   N    N N N 39  
ALA   CA   C N S 40  
ALA   C    C N N 41  
ALA   O    O N N 42  
ALA   CB   C N N 43  
ALA   OXT  O N N 44  
ALA   H    H N N 45  
ALA   H2   H N N 46  
ALA   HA   H N N 47  
ALA   HB1  H N N 48  
ALA   HB2  H N N 49  
ALA   HB3  H N N 50  
ALA   HXT  H N N 51  
ARG   N    N N N 52  
ARG   CA   C N S 53  
ARG   C    C N N 54  
ARG   O    O N N 55  
ARG   CB   C N N 56  
ARG   CG   C N N 57  
ARG   CD   C N N 58  
ARG   NE   N N N 59  
ARG   CZ   C N N 60  
ARG   NH1  N N N 61  
ARG   NH2  N N N 62  
ARG   OXT  O N N 63  
ARG   H    H N N 64  
ARG   H2   H N N 65  
ARG   HA   H N N 66  
ARG   HB2  H N N 67  
ARG   HB3  H N N 68  
ARG   HG2  H N N 69  
ARG   HG3  H N N 70  
ARG   HD2  H N N 71  
ARG   HD3  H N N 72  
ARG   HE   H N N 73  
ARG   HH11 H N N 74  
ARG   HH12 H N N 75  
ARG   HH21 H N N 76  
ARG   HH22 H N N 77  
ARG   HXT  H N N 78  
ASN   N    N N N 79  
ASN   CA   C N S 80  
ASN   C    C N N 81  
ASN   O    O N N 82  
ASN   CB   C N N 83  
ASN   CG   C N N 84  
ASN   OD1  O N N 85  
ASN   ND2  N N N 86  
ASN   OXT  O N N 87  
ASN   H    H N N 88  
ASN   H2   H N N 89  
ASN   HA   H N N 90  
ASN   HB2  H N N 91  
ASN   HB3  H N N 92  
ASN   HD21 H N N 93  
ASN   HD22 H N N 94  
ASN   HXT  H N N 95  
ASP   N    N N N 96  
ASP   CA   C N S 97  
ASP   C    C N N 98  
ASP   O    O N N 99  
ASP   CB   C N N 100 
ASP   CG   C N N 101 
ASP   OD1  O N N 102 
ASP   OD2  O N N 103 
ASP   OXT  O N N 104 
ASP   H    H N N 105 
ASP   H2   H N N 106 
ASP   HA   H N N 107 
ASP   HB2  H N N 108 
ASP   HB3  H N N 109 
ASP   HD2  H N N 110 
ASP   HXT  H N N 111 
GLN   N    N N N 112 
GLN   CA   C N S 113 
GLN   C    C N N 114 
GLN   O    O N N 115 
GLN   CB   C N N 116 
GLN   CG   C N N 117 
GLN   CD   C N N 118 
GLN   OE1  O N N 119 
GLN   NE2  N N N 120 
GLN   OXT  O N N 121 
GLN   H    H N N 122 
GLN   H2   H N N 123 
GLN   HA   H N N 124 
GLN   HB2  H N N 125 
GLN   HB3  H N N 126 
GLN   HG2  H N N 127 
GLN   HG3  H N N 128 
GLN   HE21 H N N 129 
GLN   HE22 H N N 130 
GLN   HXT  H N N 131 
GLU   N    N N N 132 
GLU   CA   C N S 133 
GLU   C    C N N 134 
GLU   O    O N N 135 
GLU   CB   C N N 136 
GLU   CG   C N N 137 
GLU   CD   C N N 138 
GLU   OE1  O N N 139 
GLU   OE2  O N N 140 
GLU   OXT  O N N 141 
GLU   H    H N N 142 
GLU   H2   H N N 143 
GLU   HA   H N N 144 
GLU   HB2  H N N 145 
GLU   HB3  H N N 146 
GLU   HG2  H N N 147 
GLU   HG3  H N N 148 
GLU   HE2  H N N 149 
GLU   HXT  H N N 150 
GLY   N    N N N 151 
GLY   CA   C N N 152 
GLY   C    C N N 153 
GLY   O    O N N 154 
GLY   OXT  O N N 155 
GLY   H    H N N 156 
GLY   H2   H N N 157 
GLY   HA2  H N N 158 
GLY   HA3  H N N 159 
GLY   HXT  H N N 160 
HIS   N    N N N 161 
HIS   CA   C N S 162 
HIS   C    C N N 163 
HIS   O    O N N 164 
HIS   CB   C N N 165 
HIS   CG   C Y N 166 
HIS   ND1  N Y N 167 
HIS   CD2  C Y N 168 
HIS   CE1  C Y N 169 
HIS   NE2  N Y N 170 
HIS   OXT  O N N 171 
HIS   H    H N N 172 
HIS   H2   H N N 173 
HIS   HA   H N N 174 
HIS   HB2  H N N 175 
HIS   HB3  H N N 176 
HIS   HD1  H N N 177 
HIS   HD2  H N N 178 
HIS   HE1  H N N 179 
HIS   HE2  H N N 180 
HIS   HXT  H N N 181 
HOH   O    O N N 182 
HOH   H1   H N N 183 
HOH   H2   H N N 184 
ILE   N    N N N 185 
ILE   CA   C N S 186 
ILE   C    C N N 187 
ILE   O    O N N 188 
ILE   CB   C N S 189 
ILE   CG1  C N N 190 
ILE   CG2  C N N 191 
ILE   CD1  C N N 192 
ILE   OXT  O N N 193 
ILE   H    H N N 194 
ILE   H2   H N N 195 
ILE   HA   H N N 196 
ILE   HB   H N N 197 
ILE   HG12 H N N 198 
ILE   HG13 H N N 199 
ILE   HG21 H N N 200 
ILE   HG22 H N N 201 
ILE   HG23 H N N 202 
ILE   HD11 H N N 203 
ILE   HD12 H N N 204 
ILE   HD13 H N N 205 
ILE   HXT  H N N 206 
LEU   N    N N N 207 
LEU   CA   C N S 208 
LEU   C    C N N 209 
LEU   O    O N N 210 
LEU   CB   C N N 211 
LEU   CG   C N N 212 
LEU   CD1  C N N 213 
LEU   CD2  C N N 214 
LEU   OXT  O N N 215 
LEU   H    H N N 216 
LEU   H2   H N N 217 
LEU   HA   H N N 218 
LEU   HB2  H N N 219 
LEU   HB3  H N N 220 
LEU   HG   H N N 221 
LEU   HD11 H N N 222 
LEU   HD12 H N N 223 
LEU   HD13 H N N 224 
LEU   HD21 H N N 225 
LEU   HD22 H N N 226 
LEU   HD23 H N N 227 
LEU   HXT  H N N 228 
LYS   N    N N N 229 
LYS   CA   C N S 230 
LYS   C    C N N 231 
LYS   O    O N N 232 
LYS   CB   C N N 233 
LYS   CG   C N N 234 
LYS   CD   C N N 235 
LYS   CE   C N N 236 
LYS   NZ   N N N 237 
LYS   OXT  O N N 238 
LYS   H    H N N 239 
LYS   H2   H N N 240 
LYS   HA   H N N 241 
LYS   HB2  H N N 242 
LYS   HB3  H N N 243 
LYS   HG2  H N N 244 
LYS   HG3  H N N 245 
LYS   HD2  H N N 246 
LYS   HD3  H N N 247 
LYS   HE2  H N N 248 
LYS   HE3  H N N 249 
LYS   HZ1  H N N 250 
LYS   HZ2  H N N 251 
LYS   HZ3  H N N 252 
LYS   HXT  H N N 253 
MET   N    N N N 254 
MET   CA   C N S 255 
MET   C    C N N 256 
MET   O    O N N 257 
MET   CB   C N N 258 
MET   CG   C N N 259 
MET   SD   S N N 260 
MET   CE   C N N 261 
MET   OXT  O N N 262 
MET   H    H N N 263 
MET   H2   H N N 264 
MET   HA   H N N 265 
MET   HB2  H N N 266 
MET   HB3  H N N 267 
MET   HG2  H N N 268 
MET   HG3  H N N 269 
MET   HE1  H N N 270 
MET   HE2  H N N 271 
MET   HE3  H N N 272 
MET   HXT  H N N 273 
PHE   N    N N N 274 
PHE   CA   C N S 275 
PHE   C    C N N 276 
PHE   O    O N N 277 
PHE   CB   C N N 278 
PHE   CG   C Y N 279 
PHE   CD1  C Y N 280 
PHE   CD2  C Y N 281 
PHE   CE1  C Y N 282 
PHE   CE2  C Y N 283 
PHE   CZ   C Y N 284 
PHE   OXT  O N N 285 
PHE   H    H N N 286 
PHE   H2   H N N 287 
PHE   HA   H N N 288 
PHE   HB2  H N N 289 
PHE   HB3  H N N 290 
PHE   HD1  H N N 291 
PHE   HD2  H N N 292 
PHE   HE1  H N N 293 
PHE   HE2  H N N 294 
PHE   HZ   H N N 295 
PHE   HXT  H N N 296 
PRO   N    N N N 297 
PRO   CA   C N S 298 
PRO   C    C N N 299 
PRO   O    O N N 300 
PRO   CB   C N N 301 
PRO   CG   C N N 302 
PRO   CD   C N N 303 
PRO   OXT  O N N 304 
PRO   H    H N N 305 
PRO   HA   H N N 306 
PRO   HB2  H N N 307 
PRO   HB3  H N N 308 
PRO   HG2  H N N 309 
PRO   HG3  H N N 310 
PRO   HD2  H N N 311 
PRO   HD3  H N N 312 
PRO   HXT  H N N 313 
SER   N    N N N 314 
SER   CA   C N S 315 
SER   C    C N N 316 
SER   O    O N N 317 
SER   CB   C N N 318 
SER   OG   O N N 319 
SER   OXT  O N N 320 
SER   H    H N N 321 
SER   H2   H N N 322 
SER   HA   H N N 323 
SER   HB2  H N N 324 
SER   HB3  H N N 325 
SER   HG   H N N 326 
SER   HXT  H N N 327 
THR   N    N N N 328 
THR   CA   C N S 329 
THR   C    C N N 330 
THR   O    O N N 331 
THR   CB   C N R 332 
THR   OG1  O N N 333 
THR   CG2  C N N 334 
THR   OXT  O N N 335 
THR   H    H N N 336 
THR   H2   H N N 337 
THR   HA   H N N 338 
THR   HB   H N N 339 
THR   HG1  H N N 340 
THR   HG21 H N N 341 
THR   HG22 H N N 342 
THR   HG23 H N N 343 
THR   HXT  H N N 344 
TRP   N    N N N 345 
TRP   CA   C N S 346 
TRP   C    C N N 347 
TRP   O    O N N 348 
TRP   CB   C N N 349 
TRP   CG   C Y N 350 
TRP   CD1  C Y N 351 
TRP   CD2  C Y N 352 
TRP   NE1  N Y N 353 
TRP   CE2  C Y N 354 
TRP   CE3  C Y N 355 
TRP   CZ2  C Y N 356 
TRP   CZ3  C Y N 357 
TRP   CH2  C Y N 358 
TRP   OXT  O N N 359 
TRP   H    H N N 360 
TRP   H2   H N N 361 
TRP   HA   H N N 362 
TRP   HB2  H N N 363 
TRP   HB3  H N N 364 
TRP   HD1  H N N 365 
TRP   HE1  H N N 366 
TRP   HE3  H N N 367 
TRP   HZ2  H N N 368 
TRP   HZ3  H N N 369 
TRP   HH2  H N N 370 
TRP   HXT  H N N 371 
TYR   N    N N N 372 
TYR   CA   C N S 373 
TYR   C    C N N 374 
TYR   O    O N N 375 
TYR   CB   C N N 376 
TYR   CG   C Y N 377 
TYR   CD1  C Y N 378 
TYR   CD2  C Y N 379 
TYR   CE1  C Y N 380 
TYR   CE2  C Y N 381 
TYR   CZ   C Y N 382 
TYR   OH   O N N 383 
TYR   OXT  O N N 384 
TYR   H    H N N 385 
TYR   H2   H N N 386 
TYR   HA   H N N 387 
TYR   HB2  H N N 388 
TYR   HB3  H N N 389 
TYR   HD1  H N N 390 
TYR   HD2  H N N 391 
TYR   HE1  H N N 392 
TYR   HE2  H N N 393 
TYR   HH   H N N 394 
TYR   HXT  H N N 395 
VAL   N    N N N 396 
VAL   CA   C N S 397 
VAL   C    C N N 398 
VAL   O    O N N 399 
VAL   CB   C N N 400 
VAL   CG1  C N N 401 
VAL   CG2  C N N 402 
VAL   OXT  O N N 403 
VAL   H    H N N 404 
VAL   H2   H N N 405 
VAL   HA   H N N 406 
VAL   HB   H N N 407 
VAL   HG11 H N N 408 
VAL   HG12 H N N 409 
VAL   HG13 H N N 410 
VAL   HG21 H N N 411 
VAL   HG22 H N N 412 
VAL   HG23 H N N 413 
VAL   HXT  H N N 414 
# 
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 
A1AW9 C1  C2   sing N N 1   
A1AW9 C2  C3   sing N N 2   
A1AW9 C3  C4   sing N N 3   
A1AW9 C4  O1   sing N N 4   
A1AW9 C3  N1   sing N N 5   
A1AW9 N1  C5   sing N N 6   
A1AW9 C5  S1   doub N N 7   
A1AW9 C5  N2   sing N N 8   
A1AW9 N2  C6   sing N N 9   
A1AW9 C6  C7   sing N N 10  
A1AW9 C7  C8   sing N N 11  
A1AW9 C8  C9   sing N N 12  
A1AW9 C9  C10  sing N N 13  
A1AW9 C10 C11  sing N N 14  
A1AW9 C11 C12  sing N N 15  
A1AW9 C6  C11  sing N N 16  
A1AW9 C8  C12  sing N N 17  
A1AW9 C1  H3   sing N N 18  
A1AW9 C1  H2   sing N N 19  
A1AW9 C1  H1   sing N N 20  
A1AW9 C10 H18  sing N N 21  
A1AW9 C10 H19  sing N N 22  
A1AW9 C11 H20  sing N N 23  
A1AW9 C12 H21  sing N N 24  
A1AW9 C12 H22  sing N N 25  
A1AW9 C2  H5   sing N N 26  
A1AW9 C2  H4   sing N N 27  
A1AW9 C3  H6   sing N N 28  
A1AW9 C4  H8   sing N N 29  
A1AW9 C4  H7   sing N N 30  
A1AW9 C6  H12  sing N N 31  
A1AW9 C7  H14  sing N N 32  
A1AW9 C7  H13  sing N N 33  
A1AW9 C8  H15  sing N N 34  
A1AW9 C9  H16  sing N N 35  
A1AW9 C9  H17  sing N N 36  
A1AW9 O1  H9   sing N N 37  
A1AW9 N1  H10  sing N N 38  
A1AW9 N2  H11  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
GLN   N   CA   sing N N 109 
GLN   N   H    sing N N 110 
GLN   N   H2   sing N N 111 
GLN   CA  C    sing N N 112 
GLN   CA  CB   sing N N 113 
GLN   CA  HA   sing N N 114 
GLN   C   O    doub N N 115 
GLN   C   OXT  sing N N 116 
GLN   CB  CG   sing N N 117 
GLN   CB  HB2  sing N N 118 
GLN   CB  HB3  sing N N 119 
GLN   CG  CD   sing N N 120 
GLN   CG  HG2  sing N N 121 
GLN   CG  HG3  sing N N 122 
GLN   CD  OE1  doub N N 123 
GLN   CD  NE2  sing N N 124 
GLN   NE2 HE21 sing N N 125 
GLN   NE2 HE22 sing N N 126 
GLN   OXT HXT  sing N N 127 
GLU   N   CA   sing N N 128 
GLU   N   H    sing N N 129 
GLU   N   H2   sing N N 130 
GLU   CA  C    sing N N 131 
GLU   CA  CB   sing N N 132 
GLU   CA  HA   sing N N 133 
GLU   C   O    doub N N 134 
GLU   C   OXT  sing N N 135 
GLU   CB  CG   sing N N 136 
GLU   CB  HB2  sing N N 137 
GLU   CB  HB3  sing N N 138 
GLU   CG  CD   sing N N 139 
GLU   CG  HG2  sing N N 140 
GLU   CG  HG3  sing N N 141 
GLU   CD  OE1  doub N N 142 
GLU   CD  OE2  sing N N 143 
GLU   OE2 HE2  sing N N 144 
GLU   OXT HXT  sing N N 145 
GLY   N   CA   sing N N 146 
GLY   N   H    sing N N 147 
GLY   N   H2   sing N N 148 
GLY   CA  C    sing N N 149 
GLY   CA  HA2  sing N N 150 
GLY   CA  HA3  sing N N 151 
GLY   C   O    doub N N 152 
GLY   C   OXT  sing N N 153 
GLY   OXT HXT  sing N N 154 
HIS   N   CA   sing N N 155 
HIS   N   H    sing N N 156 
HIS   N   H2   sing N N 157 
HIS   CA  C    sing N N 158 
HIS   CA  CB   sing N N 159 
HIS   CA  HA   sing N N 160 
HIS   C   O    doub N N 161 
HIS   C   OXT  sing N N 162 
HIS   CB  CG   sing N N 163 
HIS   CB  HB2  sing N N 164 
HIS   CB  HB3  sing N N 165 
HIS   CG  ND1  sing Y N 166 
HIS   CG  CD2  doub Y N 167 
HIS   ND1 CE1  doub Y N 168 
HIS   ND1 HD1  sing N N 169 
HIS   CD2 NE2  sing Y N 170 
HIS   CD2 HD2  sing N N 171 
HIS   CE1 NE2  sing Y N 172 
HIS   CE1 HE1  sing N N 173 
HIS   NE2 HE2  sing N N 174 
HIS   OXT HXT  sing N N 175 
HOH   O   H1   sing N N 176 
HOH   O   H2   sing N N 177 
ILE   N   CA   sing N N 178 
ILE   N   H    sing N N 179 
ILE   N   H2   sing N N 180 
ILE   CA  C    sing N N 181 
ILE   CA  CB   sing N N 182 
ILE   CA  HA   sing N N 183 
ILE   C   O    doub N N 184 
ILE   C   OXT  sing N N 185 
ILE   CB  CG1  sing N N 186 
ILE   CB  CG2  sing N N 187 
ILE   CB  HB   sing N N 188 
ILE   CG1 CD1  sing N N 189 
ILE   CG1 HG12 sing N N 190 
ILE   CG1 HG13 sing N N 191 
ILE   CG2 HG21 sing N N 192 
ILE   CG2 HG22 sing N N 193 
ILE   CG2 HG23 sing N N 194 
ILE   CD1 HD11 sing N N 195 
ILE   CD1 HD12 sing N N 196 
ILE   CD1 HD13 sing N N 197 
ILE   OXT HXT  sing N N 198 
LEU   N   CA   sing N N 199 
LEU   N   H    sing N N 200 
LEU   N   H2   sing N N 201 
LEU   CA  C    sing N N 202 
LEU   CA  CB   sing N N 203 
LEU   CA  HA   sing N N 204 
LEU   C   O    doub N N 205 
LEU   C   OXT  sing N N 206 
LEU   CB  CG   sing N N 207 
LEU   CB  HB2  sing N N 208 
LEU   CB  HB3  sing N N 209 
LEU   CG  CD1  sing N N 210 
LEU   CG  CD2  sing N N 211 
LEU   CG  HG   sing N N 212 
LEU   CD1 HD11 sing N N 213 
LEU   CD1 HD12 sing N N 214 
LEU   CD1 HD13 sing N N 215 
LEU   CD2 HD21 sing N N 216 
LEU   CD2 HD22 sing N N 217 
LEU   CD2 HD23 sing N N 218 
LEU   OXT HXT  sing N N 219 
LYS   N   CA   sing N N 220 
LYS   N   H    sing N N 221 
LYS   N   H2   sing N N 222 
LYS   CA  C    sing N N 223 
LYS   CA  CB   sing N N 224 
LYS   CA  HA   sing N N 225 
LYS   C   O    doub N N 226 
LYS   C   OXT  sing N N 227 
LYS   CB  CG   sing N N 228 
LYS   CB  HB2  sing N N 229 
LYS   CB  HB3  sing N N 230 
LYS   CG  CD   sing N N 231 
LYS   CG  HG2  sing N N 232 
LYS   CG  HG3  sing N N 233 
LYS   CD  CE   sing N N 234 
LYS   CD  HD2  sing N N 235 
LYS   CD  HD3  sing N N 236 
LYS   CE  NZ   sing N N 237 
LYS   CE  HE2  sing N N 238 
LYS   CE  HE3  sing N N 239 
LYS   NZ  HZ1  sing N N 240 
LYS   NZ  HZ2  sing N N 241 
LYS   NZ  HZ3  sing N N 242 
LYS   OXT HXT  sing N N 243 
MET   N   CA   sing N N 244 
MET   N   H    sing N N 245 
MET   N   H2   sing N N 246 
MET   CA  C    sing N N 247 
MET   CA  CB   sing N N 248 
MET   CA  HA   sing N N 249 
MET   C   O    doub N N 250 
MET   C   OXT  sing N N 251 
MET   CB  CG   sing N N 252 
MET   CB  HB2  sing N N 253 
MET   CB  HB3  sing N N 254 
MET   CG  SD   sing N N 255 
MET   CG  HG2  sing N N 256 
MET   CG  HG3  sing N N 257 
MET   SD  CE   sing N N 258 
MET   CE  HE1  sing N N 259 
MET   CE  HE2  sing N N 260 
MET   CE  HE3  sing N N 261 
MET   OXT HXT  sing N N 262 
PHE   N   CA   sing N N 263 
PHE   N   H    sing N N 264 
PHE   N   H2   sing N N 265 
PHE   CA  C    sing N N 266 
PHE   CA  CB   sing N N 267 
PHE   CA  HA   sing N N 268 
PHE   C   O    doub N N 269 
PHE   C   OXT  sing N N 270 
PHE   CB  CG   sing N N 271 
PHE   CB  HB2  sing N N 272 
PHE   CB  HB3  sing N N 273 
PHE   CG  CD1  doub Y N 274 
PHE   CG  CD2  sing Y N 275 
PHE   CD1 CE1  sing Y N 276 
PHE   CD1 HD1  sing N N 277 
PHE   CD2 CE2  doub Y N 278 
PHE   CD2 HD2  sing N N 279 
PHE   CE1 CZ   doub Y N 280 
PHE   CE1 HE1  sing N N 281 
PHE   CE2 CZ   sing Y N 282 
PHE   CE2 HE2  sing N N 283 
PHE   CZ  HZ   sing N N 284 
PHE   OXT HXT  sing N N 285 
PRO   N   CA   sing N N 286 
PRO   N   CD   sing N N 287 
PRO   N   H    sing N N 288 
PRO   CA  C    sing N N 289 
PRO   CA  CB   sing N N 290 
PRO   CA  HA   sing N N 291 
PRO   C   O    doub N N 292 
PRO   C   OXT  sing N N 293 
PRO   CB  CG   sing N N 294 
PRO   CB  HB2  sing N N 295 
PRO   CB  HB3  sing N N 296 
PRO   CG  CD   sing N N 297 
PRO   CG  HG2  sing N N 298 
PRO   CG  HG3  sing N N 299 
PRO   CD  HD2  sing N N 300 
PRO   CD  HD3  sing N N 301 
PRO   OXT HXT  sing N N 302 
SER   N   CA   sing N N 303 
SER   N   H    sing N N 304 
SER   N   H2   sing N N 305 
SER   CA  C    sing N N 306 
SER   CA  CB   sing N N 307 
SER   CA  HA   sing N N 308 
SER   C   O    doub N N 309 
SER   C   OXT  sing N N 310 
SER   CB  OG   sing N N 311 
SER   CB  HB2  sing N N 312 
SER   CB  HB3  sing N N 313 
SER   OG  HG   sing N N 314 
SER   OXT HXT  sing N N 315 
THR   N   CA   sing N N 316 
THR   N   H    sing N N 317 
THR   N   H2   sing N N 318 
THR   CA  C    sing N N 319 
THR   CA  CB   sing N N 320 
THR   CA  HA   sing N N 321 
THR   C   O    doub N N 322 
THR   C   OXT  sing N N 323 
THR   CB  OG1  sing N N 324 
THR   CB  CG2  sing N N 325 
THR   CB  HB   sing N N 326 
THR   OG1 HG1  sing N N 327 
THR   CG2 HG21 sing N N 328 
THR   CG2 HG22 sing N N 329 
THR   CG2 HG23 sing N N 330 
THR   OXT HXT  sing N N 331 
TRP   N   CA   sing N N 332 
TRP   N   H    sing N N 333 
TRP   N   H2   sing N N 334 
TRP   CA  C    sing N N 335 
TRP   CA  CB   sing N N 336 
TRP   CA  HA   sing N N 337 
TRP   C   O    doub N N 338 
TRP   C   OXT  sing N N 339 
TRP   CB  CG   sing N N 340 
TRP   CB  HB2  sing N N 341 
TRP   CB  HB3  sing N N 342 
TRP   CG  CD1  doub Y N 343 
TRP   CG  CD2  sing Y N 344 
TRP   CD1 NE1  sing Y N 345 
TRP   CD1 HD1  sing N N 346 
TRP   CD2 CE2  doub Y N 347 
TRP   CD2 CE3  sing Y N 348 
TRP   NE1 CE2  sing Y N 349 
TRP   NE1 HE1  sing N N 350 
TRP   CE2 CZ2  sing Y N 351 
TRP   CE3 CZ3  doub Y N 352 
TRP   CE3 HE3  sing N N 353 
TRP   CZ2 CH2  doub Y N 354 
TRP   CZ2 HZ2  sing N N 355 
TRP   CZ3 CH2  sing Y N 356 
TRP   CZ3 HZ3  sing N N 357 
TRP   CH2 HH2  sing N N 358 
TRP   OXT HXT  sing N N 359 
TYR   N   CA   sing N N 360 
TYR   N   H    sing N N 361 
TYR   N   H2   sing N N 362 
TYR   CA  C    sing N N 363 
TYR   CA  CB   sing N N 364 
TYR   CA  HA   sing N N 365 
TYR   C   O    doub N N 366 
TYR   C   OXT  sing N N 367 
TYR   CB  CG   sing N N 368 
TYR   CB  HB2  sing N N 369 
TYR   CB  HB3  sing N N 370 
TYR   CG  CD1  doub Y N 371 
TYR   CG  CD2  sing Y N 372 
TYR   CD1 CE1  sing Y N 373 
TYR   CD1 HD1  sing N N 374 
TYR   CD2 CE2  doub Y N 375 
TYR   CD2 HD2  sing N N 376 
TYR   CE1 CZ   doub Y N 377 
TYR   CE1 HE1  sing N N 378 
TYR   CE2 CZ   sing Y N 379 
TYR   CE2 HE2  sing N N 380 
TYR   CZ  OH   sing N N 381 
TYR   OH  HH   sing N N 382 
TYR   OXT HXT  sing N N 383 
VAL   N   CA   sing N N 384 
VAL   N   H    sing N N 385 
VAL   N   H2   sing N N 386 
VAL   CA  C    sing N N 387 
VAL   CA  CB   sing N N 388 
VAL   CA  HA   sing N N 389 
VAL   C   O    doub N N 390 
VAL   C   OXT  sing N N 391 
VAL   CB  CG1  sing N N 392 
VAL   CB  CG2  sing N N 393 
VAL   CB  HB   sing N N 394 
VAL   CG1 HG11 sing N N 395 
VAL   CG1 HG12 sing N N 396 
VAL   CG1 HG13 sing N N 397 
VAL   CG2 HG21 sing N N 398 
VAL   CG2 HG22 sing N N 399 
VAL   CG2 HG23 sing N N 400 
VAL   OXT HXT  sing N N 401 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFC2301405 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         'Crystallographic fragment screening of Human heat shock protein 90' 
_pdbx_deposit_group.group_description   
;Heat shock protein 90 (HSP90) is one of the most active molecular chaperones in cells. It plays a vital role in the cell maturation process and serves as a molecular chaperone involved in many oncogenic proteins folding, assembly and stabilization. Many HSP90 client proteins are kinases or transcription factors involved in signal transduction pathways and are key regulatory factors in tumor growth and maintenance. Therefore, HSP90 inhibitors can be used as drugs for cancer treatment.
;
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002298 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    7HA9 
_atom_sites.fract_transf_matrix[1][1]   0.014331 
_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]   0.011311 
_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]   0.010348 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU   A 1 9   ? 8.44831   15.96177 10.33436 1.000 78.20042  ? 16  GLU   A N   1 
ATOM   2    C CA  . GLU   A 1 9   ? 9.74139   16.63255 10.38820 1.000 78.09085  ? 16  GLU   A CA  1 
ATOM   3    C C   . GLU   A 1 9   ? 9.80458   17.57564 11.58537 1.000 70.81253  ? 16  GLU   A C   1 
ATOM   4    O O   . GLU   A 1 9   ? 9.04220   18.53869 11.67118 1.000 67.78391  ? 16  GLU   A O   1 
ATOM   5    C CB  . GLU   A 1 9   ? 10.00369  17.39808 9.08963  1.000 87.06065  ? 16  GLU   A CB  1 
ATOM   6    C CG  . GLU   A 1 9   ? 11.47221  17.68711 8.82464  1.000 90.98957  ? 16  GLU   A CG  1 
ATOM   7    C CD  . GLU   A 1 9   ? 11.87502  19.09184 9.22710  1.000 117.13942 ? 16  GLU   A CD  1 
ATOM   8    O OE1 . GLU   A 1 9   ? 11.00954  19.84349 9.72272  1.000 116.81367 ? 16  GLU   A OE1 1 
ATOM   9    O OE2 . GLU   A 1 9   ? 13.05920  19.44526 9.04675  1.000 109.66620 ? 16  GLU   A OE2 1 
ATOM   10   N N   . VAL   A 1 10  ? 10.72051  17.29281 12.50793 1.000 62.62263  ? 17  VAL   A N   1 
ATOM   11   C CA  . VAL   A 1 10  ? 10.85508  18.04112 13.75161 1.000 57.73853  ? 17  VAL   A CA  1 
ATOM   12   C C   . VAL   A 1 10  ? 12.20951  18.73475 13.75932 1.000 54.73494  ? 17  VAL   A C   1 
ATOM   13   O O   . VAL   A 1 10  ? 13.23812  18.10231 13.49485 1.000 52.82069  ? 17  VAL   A O   1 
ATOM   14   C CB  . VAL   A 1 10  ? 10.70659  17.12623 14.98120 1.000 53.30844  ? 17  VAL   A CB  1 
ATOM   15   C CG1 . VAL   A 1 10  ? 10.65640  17.95174 16.25656 1.000 50.60056  ? 17  VAL   A CG1 1 
ATOM   16   C CG2 . VAL   A 1 10  ? 9.46542   16.25617 14.84969 1.000 59.16926  ? 17  VAL   A CG2 1 
ATOM   17   N N   . GLU   A 1 11  ? 12.20744  20.02868 14.06489 1.000 50.40131  ? 18  GLU   A N   1 
ATOM   18   C CA  . GLU   A 1 11  ? 13.42531  20.81336 14.21555 1.000 46.98583  ? 18  GLU   A CA  1 
ATOM   19   C C   . GLU   A 1 11  ? 13.64887  21.10227 15.69252 1.000 44.29688  ? 18  GLU   A C   1 
ATOM   20   O O   . GLU   A 1 11  ? 12.71143  21.48022 16.40214 1.000 43.94162  ? 18  GLU   A O   1 
ATOM   21   C CB  . GLU   A 1 11  ? 13.34085  22.12515 13.43180 1.000 48.77059  ? 18  GLU   A CB  1 
ATOM   22   C CG  . GLU   A 1 11  ? 13.38106  21.96260 11.92362 1.000 55.56986  ? 18  GLU   A CG  1 
ATOM   23   C CD  . GLU   A 1 11  ? 13.34429  23.29348 11.19805 1.000 60.17533  ? 18  GLU   A CD  1 
ATOM   24   O OE1 . GLU   A 1 11  ? 12.40873  24.08202 11.44867 1.000 58.53781  ? 18  GLU   A OE1 1 
ATOM   25   O OE2 . GLU   A 1 11  ? 14.25134  23.55255 10.37903 1.000 66.44465  ? 18  GLU   A OE2 1 
ATOM   26   N N   . THR   A 1 12  ? 14.88424  20.92748 16.15036 1.000 39.27871  ? 19  THR   A N   1 
ATOM   27   C CA  . THR   A 1 12  ? 15.25489  21.17587 17.53687 1.000 38.95461  ? 19  THR   A CA  1 
ATOM   28   C C   . THR   A 1 12  ? 16.11961  22.42593 17.61257 1.000 41.44111  ? 19  THR   A C   1 
ATOM   29   O O   . THR   A 1 12  ? 17.08667  22.56424 16.85544 1.000 40.87018  ? 19  THR   A O   1 
ATOM   30   C CB  . THR   A 1 12  ? 16.00369  19.98113 18.13161 1.000 41.94154  ? 19  THR   A CB  1 
ATOM   31   O OG1 . THR   A 1 12  ? 15.18900  18.80622 18.03284 1.000 42.76441  ? 19  THR   A OG1 1 
ATOM   32   C CG2 . THR   A 1 12  ? 16.33676  20.23839 19.59259 1.000 43.53222  ? 19  THR   A CG2 1 
ATOM   33   N N   . PHE   A 1 13  ? 15.76769  23.33141 18.52231 1.000 36.68415  ? 20  PHE   A N   1 
ATOM   34   C CA  . PHE   A 1 13  ? 16.49487  24.57562 18.71140 1.000 41.72279  ? 20  PHE   A CA  1 
ATOM   35   C C   . PHE   A 1 13  ? 16.94113  24.68832 20.15996 1.000 43.62461  ? 20  PHE   A C   1 
ATOM   36   O O   . PHE   A 1 13  ? 16.34061  24.09616 21.06085 1.000 40.62708  ? 20  PHE   A O   1 
ATOM   37   C CB  . PHE   A 1 13  ? 15.64066  25.79793 18.34373 1.000 41.66726  ? 20  PHE   A CB  1 
ATOM   38   C CG  . PHE   A 1 13  ? 14.99821  25.70820 16.98878 1.000 38.96966  ? 20  PHE   A CG  1 
ATOM   39   C CD1 . PHE   A 1 13  ? 13.75448  25.11782 16.83369 1.000 40.79711  ? 20  PHE   A CD1 1 
ATOM   40   C CD2 . PHE   A 1 13  ? 15.63499  26.22074 15.87085 1.000 41.76589  ? 20  PHE   A CD2 1 
ATOM   41   C CE1 . PHE   A 1 13  ? 13.16044  25.03701 15.58858 1.000 42.25417  ? 20  PHE   A CE1 1 
ATOM   42   C CE2 . PHE   A 1 13  ? 15.04601  26.14287 14.62342 1.000 44.58730  ? 20  PHE   A CE2 1 
ATOM   43   C CZ  . PHE   A 1 13  ? 13.80742  25.55029 14.48236 1.000 44.76287  ? 20  PHE   A CZ  1 
ATOM   44   N N   . ALA   A 1 14  ? 18.00403  25.45629 20.37326 1.000 43.88227  ? 21  ALA   A N   1 
ATOM   45   C CA  . ALA   A 1 14  ? 18.47957  25.75345 21.71412 1.000 43.79329  ? 21  ALA   A CA  1 
ATOM   46   C C   . ALA   A 1 14  ? 17.86072  27.05321 22.20387 1.000 44.35685  ? 21  ALA   A C   1 
ATOM   47   O O   . ALA   A 1 14  ? 17.76599  28.03184 21.45662 1.000 41.91455  ? 21  ALA   A O   1 
ATOM   48   C CB  . ALA   A 1 14  ? 20.00489  25.85901 21.74529 1.000 46.87143  ? 21  ALA   A CB  1 
ATOM   49   N N   . PHE   A 1 15  ? 17.42673  27.05171 23.46083 1.000 43.13153  ? 22  PHE   A N   1 
ATOM   50   C CA  . PHE   A 1 15  ? 16.93561  28.27810 24.06783 1.000 45.32637  ? 22  PHE   A CA  1 
ATOM   51   C C   . PHE   A 1 15  ? 18.05140  29.31007 24.14043 1.000 48.03412  ? 22  PHE   A C   1 
ATOM   52   O O   . PHE   A 1 15  ? 19.23493  28.97455 24.23356 1.000 46.03478  ? 22  PHE   A O   1 
ATOM   53   C CB  . PHE   A 1 15  ? 16.39355  28.01354 25.47339 1.000 44.01679  ? 22  PHE   A CB  1 
ATOM   54   C CG  . PHE   A 1 15  ? 14.98927  27.49002 25.49668 1.000 42.82098  ? 22  PHE   A CG  1 
ATOM   55   C CD1 . PHE   A 1 15  ? 13.92630  28.29559 25.11932 1.000 44.28985  ? 22  PHE   A CD1 1 
ATOM   56   C CD2 . PHE   A 1 15  ? 14.72997  26.19582 25.90998 1.000 42.38369  ? 22  PHE   A CD2 1 
ATOM   57   C CE1 . PHE   A 1 15  ? 12.63115  27.81343 25.14517 1.000 41.76312  ? 22  PHE   A CE1 1 
ATOM   58   C CE2 . PHE   A 1 15  ? 13.44050  25.70870 25.93762 1.000 41.35120  ? 22  PHE   A CE2 1 
ATOM   59   C CZ  . PHE   A 1 15  ? 12.38877  26.51723 25.55526 1.000 41.59184  ? 22  PHE   A CZ  1 
ATOM   60   N N   . GLN   A 1 16  ? 17.66167  30.57888 24.08364 1.000 48.83430  ? 23  GLN   A N   1 
ATOM   61   C CA  . GLN   A 1 16  ? 18.60215  31.65525 24.34669 1.000 51.69667  ? 23  GLN   A CA  1 
ATOM   62   C C   . GLN   A 1 16  ? 19.12177  31.52946 25.77238 1.000 50.12534  ? 23  GLN   A C   1 
ATOM   63   O O   . GLN   A 1 16  ? 18.37655  31.16829 26.68728 1.000 46.37662  ? 23  GLN   A O   1 
ATOM   64   C CB  . GLN   A 1 16  ? 17.91562  32.99924 24.11198 1.000 55.49755  ? 23  GLN   A CB  1 
ATOM   65   C CG  . GLN   A 1 16  ? 17.61199  33.23432 22.62419 1.000 63.56945  ? 23  GLN   A CG  1 
ATOM   66   C CD  . GLN   A 1 16  ? 17.75634  34.68339 22.22072 1.000 74.84469  ? 23  GLN   A CD  1 
ATOM   67   O OE1 . GLN   A 1 16  ? 17.32311  35.57664 22.94646 1.000 92.79529  ? 23  GLN   A OE1 1 
ATOM   68   N NE2 . GLN   A 1 16  ? 18.36123  34.92796 21.06126 1.000 80.43237  ? 23  GLN   A NE2 1 
ATOM   69   N N   . ALA   A 1 17  ? 20.41746  31.80990 25.95006 1.000 50.00361  ? 24  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 17  ? 21.09428  31.49270 27.20656 1.000 49.61136  ? 24  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 17  ? 20.37123  32.08401 28.40987 1.000 51.53441  ? 24  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 17  ? 20.29434  31.45205 29.46985 1.000 53.22656  ? 24  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 17  ? 22.54243  31.98345 27.16075 1.000 51.02012  ? 24  ALA   A CB  1 
ATOM   74   N N   . GLU   A 1 18  ? 19.82598  33.29237 28.26303 1.000 49.68416  ? 25  GLU   A N   1 
ATOM   75   C CA  . GLU   A 1 18  ? 19.09915  33.91040 29.36665 1.000 52.37229  ? 25  GLU   A CA  1 
ATOM   76   C C   . GLU   A 1 18  ? 17.79062  33.18045 29.64479 1.000 50.46583  ? 25  GLU   A C   1 
ATOM   77   O O   . GLU   A 1 18  ? 17.40942  32.99917 30.80718 1.000 45.36800  ? 25  GLU   A O   1 
ATOM   78   C CB  . GLU   A 1 18  ? 18.83899  35.38559 29.06097 1.000 56.12099  ? 25  GLU   A CB  1 
ATOM   79   C CG  . GLU   A 1 18  ? 20.10048  36.21296 28.84698 1.000 64.48607  ? 25  GLU   A CG  1 
ATOM   80   C CD  . GLU   A 1 18  ? 20.62768  36.13195 27.42550 1.000 69.32732  ? 25  GLU   A CD  1 
ATOM   81   O OE1 . GLU   A 1 18  ? 20.07917  35.34329 26.62708 1.000 62.81075  ? 25  GLU   A OE1 1 
ATOM   82   O OE2 . GLU   A 1 18  ? 21.59483  36.85524 27.10748 1.000 84.29782  ? 25  GLU   A OE2 1 
ATOM   83   N N   . ILE   A 1 19  ? 17.09154  32.75001 28.59273 1.000 44.61882  ? 26  ILE   A N   1 
ATOM   84   C CA  . ILE   A 1 19  ? 15.82237  32.05492 28.78379 1.000 45.07212  ? 26  ILE   A CA  1 
ATOM   85   C C   . ILE   A 1 19  ? 16.05261  30.67623 29.39135 1.000 43.83133  ? 26  ILE   A C   1 
ATOM   86   O O   . ILE   A 1 19  ? 15.33707  30.26206 30.31211 1.000 41.67640  ? 26  ILE   A O   1 
ATOM   87   C CB  . ILE   A 1 19  ? 15.05389  31.97509 27.45216 1.000 43.00549  ? 26  ILE   A CB  1 
ATOM   88   C CG1 . ILE   A 1 19  ? 14.51082  33.35515 27.07441 1.000 42.51059  ? 26  ILE   A CG1 1 
ATOM   89   C CG2 . ILE   A 1 19  ? 13.91976  30.96433 27.54347 1.000 44.03630  ? 26  ILE   A CG2 1 
ATOM   90   C CD1 . ILE   A 1 19  ? 14.07321  33.46892 25.63187 1.000 51.69042  ? 26  ILE   A CD1 1 
ATOM   91   N N   . ALA   A 1 20  ? 17.05490  29.94607 28.89385 1.000 38.37127  ? 27  ALA   A N   1 
ATOM   92   C CA  . ALA   A 1 20  ? 17.38217  28.64898 29.47782 1.000 43.98101  ? 27  ALA   A CA  1 
ATOM   93   C C   . ALA   A 1 20  ? 17.79422  28.79547 30.93603 1.000 42.03124  ? 27  ALA   A C   1 
ATOM   94   O O   . ALA   A 1 20  ? 17.50245  27.92458 31.76455 1.000 41.03388  ? 27  ALA   A O   1 
ATOM   95   C CB  . ALA   A 1 20  ? 18.49145  27.97216 28.67305 1.000 44.26030  ? 27  ALA   A CB  1 
ATOM   96   N N   . GLN   A 1 21  ? 18.47307  29.89596 31.26770 1.000 43.83660  ? 28  GLN   A N   1 
ATOM   97   C CA  . GLN   A 1 21  ? 18.83451  30.15471 32.65683 1.000 48.90874  ? 28  GLN   A CA  1 
ATOM   98   C C   . GLN   A 1 21  ? 17.59943  30.43501 33.50180 1.000 45.76172  ? 28  GLN   A C   1 
ATOM   99   O O   . GLN   A 1 21  ? 17.50660  29.97763 34.64666 1.000 44.30673  ? 28  GLN   A O   1 
ATOM   100  C CB  . GLN   A 1 21  ? 19.81095  31.32675 32.73223 1.000 52.41836  ? 28  GLN   A CB  1 
ATOM   101  C CG  . GLN   A 1 21  ? 21.27109  30.92024 32.71260 1.000 58.93923  ? 28  GLN   A CG  1 
ATOM   102  C CD  . GLN   A 1 21  ? 22.19166  32.08864 32.43255 1.000 68.81497  ? 28  GLN   A CD  1 
ATOM   103  O OE1 . GLN   A 1 21  ? 21.89936  33.22441 32.80377 1.000 65.54536  ? 28  GLN   A OE1 1 
ATOM   104  N NE2 . GLN   A 1 21  ? 23.30870  31.81730 31.76634 1.000 78.15244  ? 28  GLN   A NE2 1 
ATOM   105  N N   . LEU   A 1 22  ? 16.64073  31.18571 32.95323 1.000 44.54734  ? 29  LEU   A N   1 
ATOM   106  C CA  . LEU   A 1 22  ? 15.41138  31.47130 33.68579 1.000 45.06453  ? 29  LEU   A CA  1 
ATOM   107  C C   . LEU   A 1 22  ? 14.59405  30.20635 33.91258 1.000 43.11717  ? 29  LEU   A C   1 
ATOM   108  O O   . LEU   A 1 22  ? 14.07540  29.98676 35.01392 1.000 43.97405  ? 29  LEU   A O   1 
ATOM   109  C CB  . LEU   A 1 22  ? 14.58134  32.51239 32.93594 1.000 46.87895  ? 29  LEU   A CB  1 
ATOM   110  C CG  . LEU   A 1 22  ? 13.18153  32.78262 33.49340 1.000 46.06112  ? 29  LEU   A CG  1 
ATOM   111  C CD1 . LEU   A 1 22  ? 13.25471  33.24853 34.94106 1.000 46.55523  ? 29  LEU   A CD1 1 
ATOM   112  C CD2 . LEU   A 1 22  ? 12.44344  33.79478 32.63224 1.000 47.58910  ? 29  LEU   A CD2 1 
ATOM   113  N N   . MET   A 1 23  ? 14.46065  29.36735 32.88125 1.000 41.82796  ? 30  MET   A N   1 
ATOM   114  C CA  . MET   A 1 23  ? 13.69095  28.13660 33.03041 1.000 44.11768  ? 30  MET   A CA  1 
ATOM   115  C C   . MET   A 1 23  ? 14.31403  27.22241 34.07658 1.000 46.61749  ? 30  MET   A C   1 
ATOM   116  O O   . MET   A 1 23  ? 13.60347  26.64840 34.90873 1.000 47.75842  ? 30  MET   A O   1 
ATOM   117  C CB  . MET   A 1 23  ? 13.57219  27.41670 31.68632 1.000 42.12630  ? 30  MET   A CB  1 
ATOM   118  C CG  . MET   A 1 23  ? 12.81102  28.20456 30.62852 1.000 39.40258  ? 30  MET   A CG  1 
ATOM   119  S SD  . MET   A 1 23  ? 12.90876  27.47828 28.98029 1.000 46.31996  ? 30  MET   A SD  1 
ATOM   120  C CE  . MET   A 1 23  ? 11.98315  25.96566 29.22133 1.000 40.89160  ? 30  MET   A CE  1 
ATOM   121  N N   . SER   A 1 24  ? 15.64260  27.08413 34.05934 1.000 47.07203  ? 31  SER   A N   1 
ATOM   122  C CA  . SER   A 1 24  ? 16.31017  26.27436 35.07350 1.000 45.98684  ? 31  SER   A CA  1 
ATOM   123  C C   . SER   A 1 24  ? 16.04938  26.82265 36.47031 1.000 51.91186  ? 31  SER   A C   1 
ATOM   124  O O   . SER   A 1 24  ? 15.88638  26.05660 37.42703 1.000 54.99314  ? 31  SER   A O   1 
ATOM   125  C CB  . SER   A 1 24  ? 17.81107  26.21019 34.79232 1.000 50.31052  ? 31  SER   A CB  1 
ATOM   126  O OG  . SER   A 1 24  ? 18.51951  25.70575 35.91153 1.000 57.85534  ? 31  SER   A OG  1 
ATOM   127  N N   . LEU   A 1 25  ? 15.99918  28.14923 36.60604 1.000 51.34558  ? 32  LEU   A N   1 
ATOM   128  C CA  . LEU   A 1 25  ? 15.66922  28.74424 37.89617 1.000 53.23766  ? 32  LEU   A CA  1 
ATOM   129  C C   . LEU   A 1 25  ? 14.23873  28.41191 38.30187 1.000 54.10168  ? 32  LEU   A C   1 
ATOM   130  O O   . LEU   A 1 25  ? 13.97250  28.10158 39.46794 1.000 57.01938  ? 32  LEU   A O   1 
ATOM   131  C CB  . LEU   A 1 25  ? 15.88034  30.25950 37.84147 1.000 54.69141  ? 32  LEU   A CB  1 
ATOM   132  C CG  . LEU   A 1 25  ? 15.85319  31.06526 39.14535 1.000 63.73663  ? 32  LEU   A CG  1 
ATOM   133  C CD1 . LEU   A 1 25  ? 16.71162  32.31079 39.00124 1.000 62.22344  ? 32  LEU   A CD1 1 
ATOM   134  C CD2 . LEU   A 1 25  ? 14.43433  31.45545 39.54174 1.000 62.04455  ? 32  LEU   A CD2 1 
ATOM   135  N N   . ILE   A 1 26  ? 13.30664  28.46017 37.34866 1.000 48.35712  ? 33  ILE   A N   1 
ATOM   136  C CA  . ILE   A 1 26  ? 11.89477  28.27877 37.67210 1.000 49.76953  ? 33  ILE   A CA  1 
ATOM   137  C C   . ILE   A 1 26  ? 11.62309  26.85309 38.14123 1.000 53.71199  ? 33  ILE   A C   1 
ATOM   138  O O   . ILE   A 1 26  ? 10.83361  26.63059 39.06749 1.000 52.34414  ? 33  ILE   A O   1 
ATOM   139  C CB  . ILE   A 1 26  ? 11.02782  28.66399 36.45880 1.000 47.55323  ? 33  ILE   A CB  1 
ATOM   140  C CG1 . ILE   A 1 26  ? 11.03062  30.18401 36.27506 1.000 46.51189  ? 33  ILE   A CG1 1 
ATOM   141  C CG2 . ILE   A 1 26  ? 9.60931   28.14086 36.61028 1.000 43.92294  ? 33  ILE   A CG2 1 
ATOM   142  C CD1 . ILE   A 1 26  ? 10.41908  30.64769 34.97471 1.000 49.21649  ? 33  ILE   A CD1 1 
ATOM   143  N N   . ILE   A 1 27  ? 12.28162  25.86785 37.53048 1.000 53.94757  ? 34  ILE   A N   1 
ATOM   144  C CA  . ILE   A 1 27  ? 12.03673  24.47795 37.90573 1.000 59.37799  ? 34  ILE   A CA  1 
ATOM   145  C C   . ILE   A 1 27  ? 12.73101  24.12667 39.21631 1.000 64.02336  ? 34  ILE   A C   1 
ATOM   146  O O   . ILE   A 1 27  ? 12.18763  23.37576 40.03402 1.000 70.70714  ? 34  ILE   A O   1 
ATOM   147  C CB  . ILE   A 1 27  ? 12.47454  23.53079 36.77439 1.000 60.59668  ? 34  ILE   A CB  1 
ATOM   148  C CG1 . ILE   A 1 27  ? 12.04782  24.08016 35.41636 1.000 51.39752  ? 34  ILE   A CG1 1 
ATOM   149  C CG2 . ILE   A 1 27  ? 11.91525  22.12985 36.99641 1.000 76.10627  ? 34  ILE   A CG2 1 
ATOM   150  C CD1 . ILE   A 1 27  ? 12.51319  23.23972 34.26670 1.000 51.88076  ? 34  ILE   A CD1 1 
ATOM   151  N N   . ASN   A 1 28  ? 13.93632  24.65079 39.44094 1.000 64.37876  ? 35  ASN   A N   1 
ATOM   152  C CA  . ASN   A 1 28  ? 14.78199  24.18085 40.53176 1.000 70.11686  ? 35  ASN   A CA  1 
ATOM   153  C C   . ASN   A 1 28  ? 14.68975  25.02330 41.79757 1.000 83.41277  ? 35  ASN   A C   1 
ATOM   154  O O   . ASN   A 1 28  ? 15.17662  24.58368 42.84595 1.000 90.15428  ? 35  ASN   A O   1 
ATOM   155  C CB  . ASN   A 1 28  ? 16.24426  24.11471 40.07536 1.000 72.34318  ? 35  ASN   A CB  1 
ATOM   156  C CG  . ASN   A 1 28  ? 16.43326  23.22493 38.86381 1.000 73.33224  ? 35  ASN   A CG  1 
ATOM   157  O OD1 . ASN   A 1 28  ? 17.16650  23.56457 37.93625 1.000 79.38017  ? 35  ASN   A OD1 1 
ATOM   158  N ND2 . ASN   A 1 28  ? 15.76591  22.07674 38.86525 1.000 71.22648  ? 35  ASN   A ND2 1 
ATOM   159  N N   . THR   A 1 29  ? 14.09012  26.20970 41.73483 1.000 72.24242  ? 36  THR   A N   1 
ATOM   160  C CA  . THR   A 1 29  ? 13.92388  27.03200 42.92618 1.000 79.69744  ? 36  THR   A CA  1 
ATOM   161  C C   . THR   A 1 29  ? 12.71842  26.55226 43.72556 1.000 71.38347  ? 36  THR   A C   1 
ATOM   162  O O   . THR   A 1 29  ? 11.64311  26.31637 43.16429 1.000 65.45607  ? 36  THR   A O   1 
ATOM   163  C CB  . THR   A 1 29  ? 13.75615  28.50528 42.54921 1.000 79.21751  ? 36  THR   A CB  1 
ATOM   164  O OG1 . THR   A 1 29  ? 15.00366  29.02296 42.06885 1.000 74.64030  ? 36  THR   A OG1 1 
ATOM   165  C CG2 . THR   A 1 29  ? 13.30709  29.32412 43.75267 1.000 75.10591  ? 36  THR   A CG2 1 
ATOM   166  N N   . PHE   A 1 30  ? 12.90461  26.39657 45.03554 1.000 69.79829  ? 37  PHE   A N   1 
ATOM   167  C CA  . PHE   A 1 30  ? 11.80779  26.02414 45.92193 1.000 69.87890  ? 37  PHE   A CA  1 
ATOM   168  C C   . PHE   A 1 30  ? 10.88670  27.22306 46.10650 1.000 69.27305  ? 37  PHE   A C   1 
ATOM   169  O O   . PHE   A 1 30  ? 11.24754  28.19948 46.77223 1.000 79.79911  ? 37  PHE   A O   1 
ATOM   170  C CB  . PHE   A 1 30  ? 12.34577  25.52901 47.26134 1.000 71.62314  ? 37  PHE   A CB  1 
ATOM   171  C CG  . PHE   A 1 30  ? 11.29238  24.91737 48.14408 1.000 85.87577  ? 37  PHE   A CG  1 
ATOM   172  C CD1 . PHE   A 1 30  ? 10.93103  23.58876 47.99376 1.000 84.48503  ? 37  PHE   A CD1 1 
ATOM   173  C CD2 . PHE   A 1 30  ? 10.66294  25.66981 49.12290 1.000 74.83103  ? 37  PHE   A CD2 1 
ATOM   174  C CE1 . PHE   A 1 30  ? 9.95580   23.02162 48.79749 1.000 90.87865  ? 37  PHE   A CE1 1 
ATOM   175  C CE2 . PHE   A 1 30  ? 9.68798   25.10805 49.93393 1.000 72.84125  ? 37  PHE   A CE2 1 
ATOM   176  C CZ  . PHE   A 1 30  ? 9.33511   23.78115 49.77051 1.000 75.02794  ? 37  PHE   A CZ  1 
ATOM   177  N N   . TYR   A 1 31  ? 9.69890   27.15305 45.50966 1.000 64.80679  ? 38  TYR   A N   1 
ATOM   178  C CA  . TYR   A 1 31  ? 8.74806   28.26053 45.55032 1.000 62.76497  ? 38  TYR   A CA  1 
ATOM   179  C C   . TYR   A 1 31  ? 7.35074   27.66168 45.60297 1.000 61.27379  ? 38  TYR   A C   1 
ATOM   180  O O   . TYR   A 1 31  ? 6.91743   27.01403 44.64586 1.000 57.05661  ? 38  TYR   A O   1 
ATOM   181  C CB  . TYR   A 1 31  ? 8.92108   29.17236 44.33936 1.000 62.48326  ? 38  TYR   A CB  1 
ATOM   182  C CG  . TYR   A 1 31  ? 8.02110   30.38627 44.33563 1.000 61.98679  ? 38  TYR   A CG  1 
ATOM   183  C CD1 . TYR   A 1 31  ? 8.30302   31.48479 45.13695 1.000 61.70518  ? 38  TYR   A CD1 1 
ATOM   184  C CD2 . TYR   A 1 31  ? 6.90400   30.44474 43.51424 1.000 58.68161  ? 38  TYR   A CD2 1 
ATOM   185  C CE1 . TYR   A 1 31  ? 7.48776   32.60214 45.13375 1.000 64.36177  ? 38  TYR   A CE1 1 
ATOM   186  C CE2 . TYR   A 1 31  ? 6.08483   31.55854 43.50131 1.000 59.14825  ? 38  TYR   A CE2 1 
ATOM   187  C CZ  . TYR   A 1 31  ? 6.37954   32.63368 44.31295 1.000 63.54887  ? 38  TYR   A CZ  1 
ATOM   188  O OH  . TYR   A 1 31  ? 5.56502   33.74339 44.30353 1.000 65.13370  ? 38  TYR   A OH  1 
ATOM   189  N N   . SER   A 1 32  ? 6.65010   27.88065 46.71671 1.000 62.32382  ? 39  SER   A N   1 
ATOM   190  C CA  . SER   A 1 32  ? 5.38856   27.19371 46.96248 1.000 63.06798  ? 39  SER   A CA  1 
ATOM   191  C C   . SER   A 1 32  ? 4.18975   27.87451 46.31216 1.000 62.60450  ? 39  SER   A C   1 
ATOM   192  O O   . SER   A 1 32  ? 3.16704   27.21505 46.09724 1.000 71.35707  ? 39  SER   A O   1 
ATOM   193  C CB  . SER   A 1 32  ? 5.15250   27.06649 48.46774 1.000 64.57896  ? 39  SER   A CB  1 
ATOM   194  O OG  . SER   A 1 32  ? 5.96018   26.04272 49.01936 1.000 61.31599  ? 39  SER   A OG  1 
ATOM   195  N N   . ASN   A 1 33  ? 4.28209   29.16674 45.99437 1.000 58.37851  ? 40  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 33  ? 3.16475   29.89669 45.39295 1.000 57.68402  ? 40  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 33  ? 3.12334   29.65597 43.88061 1.000 54.44046  ? 40  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 33  ? 3.23896   30.56631 43.06042 1.000 53.30240  ? 40  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 33  ? 3.26780   31.38038 45.72289 1.000 59.65080  ? 40  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 33  ? 2.03831   32.15984 45.29879 1.000 59.79148  ? 40  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 33  ? 0.91135   31.67894 45.41870 1.000 58.13545  ? 40  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 33  ? 2.25007   33.37297 44.80230 1.000 56.79883  ? 40  ASN   A ND2 1 
ATOM   203  N N   . LYS   A 1 34  ? 2.94012   28.38631 43.52023 1.000 51.31673  ? 41  LYS   A N   1 
ATOM   204  C CA  . LYS   A 1 34  ? 2.99279   27.97643 42.12349 1.000 48.48107  ? 41  LYS   A CA  1 
ATOM   205  C C   . LYS   A 1 34  ? 1.72293   28.30312 41.34868 1.000 45.31206  ? 41  LYS   A C   1 
ATOM   206  O O   . LYS   A 1 34  ? 1.75030   28.26430 40.11437 1.000 41.67671  ? 41  LYS   A O   1 
ATOM   207  C CB  . LYS   A 1 34  ? 3.27369   26.47473 42.03095 1.000 48.89400  ? 41  LYS   A CB  1 
ATOM   208  C CG  . LYS   A 1 34  ? 4.67091   26.08123 42.47920 1.000 49.68195  ? 41  LYS   A CG  1 
ATOM   209  C CD  . LYS   A 1 34  ? 4.88749   24.58214 42.37125 1.000 46.22834  ? 41  LYS   A CD  1 
ATOM   210  C CE  . LYS   A 1 34  ? 6.23541   24.17988 42.94725 1.000 58.92075  ? 41  LYS   A CE  1 
ATOM   211  N NZ  . LYS   A 1 34  ? 7.35214   24.48609 42.01105 1.000 59.17024  ? 41  LYS   A NZ  1 
ATOM   212  N N   . GLU   A 1 35  ? 0.62263   28.63276 42.03036 1.000 45.88728  ? 42  GLU   A N   1 
ATOM   213  C CA  . GLU   A 1 35  ? -0.64719  28.86543 41.34889 1.000 45.78394  ? 42  GLU   A CA  1 
ATOM   214  C C   . GLU   A 1 35  ? -0.61587  30.07191 40.41946 1.000 46.10890  ? 42  GLU   A C   1 
ATOM   215  O O   . GLU   A 1 35  ? -1.52245  30.21477 39.59039 1.000 43.66682  ? 42  GLU   A O   1 
ATOM   216  C CB  . GLU   A 1 35  ? -1.76926  29.04409 42.37310 1.000 49.52225  ? 42  GLU   A CB  1 
ATOM   217  C CG  . GLU   A 1 35  ? -1.71838  30.36297 43.12602 1.000 54.17252  ? 42  GLU   A CG  1 
ATOM   218  C CD  . GLU   A 1 35  ? -2.81856  30.48244 44.16193 1.000 59.73800  ? 42  GLU   A CD  1 
ATOM   219  O OE1 . GLU   A 1 35  ? -3.04804  29.50331 44.90251 1.000 58.69775  ? 42  GLU   A OE1 1 
ATOM   220  O OE2 . GLU   A 1 35  ? -3.45299  31.55568 44.23637 1.000 78.63254  ? 42  GLU   A OE2 1 
ATOM   221  N N   . ILE   A 1 36  ? 0.39602   30.93711 40.52988 1.000 43.28655  ? 43  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 36  ? 0.47829   32.11743 39.67667 1.000 45.34406  ? 43  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 36  ? 0.69651   31.77479 38.21165 1.000 43.00485  ? 43  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 36  ? 0.54007   32.65083 37.35376 1.000 41.16547  ? 43  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 36  ? 1.59817   33.06030 40.16371 1.000 48.27936  ? 43  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 36  ? 2.95612   32.35680 40.11187 1.000 48.53024  ? 43  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 36  ? 1.30425   33.55284 41.57112 1.000 51.26882  ? 43  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 36  ? 3.88258   32.88973 39.03981 1.000 50.60935  ? 43  ILE   A CD1 1 
ATOM   229  N N   . PHE   A 1 37  ? 1.05450   30.52502 37.90105 1.000 39.96797  ? 44  PHE   A N   1 
ATOM   230  C CA  . PHE   A 1 37  ? 1.22943   30.13051 36.50617 1.000 39.41716  ? 44  PHE   A CA  1 
ATOM   231  C C   . PHE   A 1 37  ? -0.06537  30.29551 35.72020 1.000 39.40316  ? 44  PHE   A C   1 
ATOM   232  O O   . PHE   A 1 37  ? -0.04340  30.68995 34.54850 1.000 37.77762  ? 44  PHE   A O   1 
ATOM   233  C CB  . PHE   A 1 37  ? 1.72505   28.68406 36.42423 1.000 40.24388  ? 44  PHE   A CB  1 
ATOM   234  C CG  . PHE   A 1 37  ? 0.62579   27.65991 36.50956 1.000 39.50974  ? 44  PHE   A CG  1 
ATOM   235  C CD1 . PHE   A 1 37  ? 0.15138   27.23989 37.73981 1.000 39.76852  ? 44  PHE   A CD1 1 
ATOM   236  C CD2 . PHE   A 1 37  ? 0.06168   27.12275 35.36233 1.000 39.10588  ? 44  PHE   A CD2 1 
ATOM   237  C CE1 . PHE   A 1 37  ? -0.86152  26.30536 37.82759 1.000 42.24637  ? 44  PHE   A CE1 1 
ATOM   238  C CE2 . PHE   A 1 37  ? -0.95518  26.19008 35.44598 1.000 39.01787  ? 44  PHE   A CE2 1 
ATOM   239  C CZ  . PHE   A 1 37  ? -1.41460  25.77938 36.67906 1.000 39.93699  ? 44  PHE   A CZ  1 
ATOM   240  N N   . LEU   A 1 38  ? -1.20534  29.99877 36.34935 1.000 39.09286  ? 45  LEU   A N   1 
ATOM   241  C CA  . LEU   A 1 38  ? -2.47832  30.06750 35.64062 1.000 39.23245  ? 45  LEU   A CA  1 
ATOM   242  C C   . LEU   A 1 38  ? -2.86760  31.51026 35.34912 1.000 40.00846  ? 45  LEU   A C   1 
ATOM   243  O O   . LEU   A 1 38  ? -3.43353  31.80404 34.28988 1.000 40.06970  ? 45  LEU   A O   1 
ATOM   244  C CB  . LEU   A 1 38  ? -3.56649  29.36425 36.45070 1.000 38.69452  ? 45  LEU   A CB  1 
ATOM   245  C CG  . LEU   A 1 38  ? -4.90342  29.13924 35.74262 1.000 43.38619  ? 45  LEU   A CG  1 
ATOM   246  C CD1 . LEU   A 1 38  ? -4.69205  28.42121 34.41885 1.000 36.92674  ? 45  LEU   A CD1 1 
ATOM   247  C CD2 . LEU   A 1 38  ? -5.85533  28.35673 36.63415 1.000 41.41853  ? 45  LEU   A CD2 1 
ATOM   248  N N   . ARG   A 1 39  ? -2.57053  32.42336 36.27669 1.000 39.17556  ? 46  ARG   A N   1 
ATOM   249  C CA  . ARG   A 1 39  ? -2.81188  33.84011 36.02582 1.000 44.97917  ? 46  ARG   A CA  1 
ATOM   250  C C   . ARG   A 1 39  ? -1.96880  34.34100 34.86118 1.000 42.58283  ? 46  ARG   A C   1 
ATOM   251  O O   . ARG   A 1 39  ? -2.45009  35.10908 34.01942 1.000 44.85711  ? 46  ARG   A O   1 
ATOM   252  C CB  . ARG   A 1 39  ? -2.51495  34.65110 37.28703 1.000 49.18597  ? 46  ARG   A CB  1 
ATOM   253  C CG  . ARG   A 1 39  ? -2.43527  36.15315 37.06379 1.000 53.74609  ? 46  ARG   A CG  1 
ATOM   254  C CD  . ARG   A 1 39  ? -1.92082  36.87039 38.30332 1.000 60.52048  ? 46  ARG   A CD  1 
ATOM   255  N NE  . ARG   A 1 39  ? -0.46835  36.79867 38.40912 1.000 66.64299  ? 46  ARG   A NE  1 
ATOM   256  C CZ  . ARG   A 1 39  ? 0.20427   36.84847 39.55096 1.000 73.97479  ? 46  ARG   A CZ  1 
ATOM   257  N NH1 . ARG   A 1 39  ? -0.41469  36.97920 40.71314 1.000 66.40997  ? 46  ARG   A NH1 1 
ATOM   258  N NH2 . ARG   A 1 39  ? 1.53156   36.76494 39.52623 1.000 58.37667  ? 46  ARG   A NH2 1 
ATOM   259  N N   . GLU   A 1 40  ? -0.70729  33.90874 34.79378 1.000 39.23631  ? 47  GLU   A N   1 
ATOM   260  C CA  . GLU   A 1 40  ? 0.18293   34.37112 33.73449 1.000 41.78359  ? 47  GLU   A CA  1 
ATOM   261  C C   . GLU   A 1 40  ? -0.26746  33.86673 32.36940 1.000 41.50750  ? 47  GLU   A C   1 
ATOM   262  O O   . GLU   A 1 40  ? -0.25142  34.61842 31.38722 1.000 37.17941  ? 47  GLU   A O   1 
ATOM   263  C CB  . GLU   A 1 40  ? 1.61557   33.92401 34.02491 1.000 42.71823  ? 47  GLU   A CB  1 
ATOM   264  C CG  . GLU   A 1 40  ? 2.22132   34.53428 35.27983 1.000 44.83256  ? 47  GLU   A CG  1 
ATOM   265  C CD  . GLU   A 1 40  ? 2.00882   36.03362 35.36350 1.000 55.07948  ? 47  GLU   A CD  1 
ATOM   266  O OE1 . GLU   A 1 40  ? 2.25497   36.72747 34.35518 1.000 51.08535  ? 47  GLU   A OE1 1 
ATOM   267  O OE2 . GLU   A 1 40  ? 1.59917   36.51905 36.43876 1.000 54.05414  ? 47  GLU   A OE2 1 
ATOM   268  N N   . LEU   A 1 41  ? -0.67437  32.59805 32.28762 1.000 36.14776  ? 48  LEU   A N   1 
ATOM   269  C CA  . LEU   A 1 41  ? -1.09302  32.04062 31.00668 1.000 36.80820  ? 48  LEU   A CA  1 
ATOM   270  C C   . LEU   A 1 41  ? -2.45163  32.57839 30.57511 1.000 35.01704  ? 48  LEU   A C   1 
ATOM   271  O O   . LEU   A 1 41  ? -2.69608  32.74531 29.37492 1.000 37.99609  ? 48  LEU   A O   1 
ATOM   272  C CB  . LEU   A 1 41  ? -1.11086  30.51465 31.08621 1.000 34.12935  ? 48  LEU   A CB  1 
ATOM   273  C CG  . LEU   A 1 41  ? 0.26416   29.89526 31.35720 1.000 35.25188  ? 48  LEU   A CG  1 
ATOM   274  C CD1 . LEU   A 1 41  ? 0.15848   28.40109 31.60588 1.000 33.36903  ? 48  LEU   A CD1 1 
ATOM   275  C CD2 . LEU   A 1 41  ? 1.21498   30.18113 30.20471 1.000 34.09596  ? 48  LEU   A CD2 1 
ATOM   276  N N   . ILE   A 1 42  ? -3.34374  32.85540 31.52799 1.000 36.51128  ? 49  ILE   A N   1 
ATOM   277  C CA  . ILE   A 1 42  ? -4.61405  33.48671 31.18440 1.000 35.73598  ? 49  ILE   A CA  1 
ATOM   278  C C   . ILE   A 1 42  ? -4.38460  34.92229 30.72729 1.000 37.32015  ? 49  ILE   A C   1 
ATOM   279  O O   . ILE   A 1 42  ? -5.01896  35.39543 29.77601 1.000 36.19424  ? 49  ILE   A O   1 
ATOM   280  C CB  . ILE   A 1 42  ? -5.58781  33.41185 32.37545 1.000 37.77607  ? 49  ILE   A CB  1 
ATOM   281  C CG1 . ILE   A 1 42  ? -6.10438  31.98175 32.54988 1.000 38.17002  ? 49  ILE   A CG1 1 
ATOM   282  C CG2 . ILE   A 1 42  ? -6.75056  34.37765 32.18890 1.000 39.63124  ? 49  ILE   A CG2 1 
ATOM   283  C CD1 . ILE   A 1 42  ? -6.95927  31.78571 33.78412 1.000 38.02431  ? 49  ILE   A CD1 1 
ATOM   284  N N   . SER   A 1 43  ? -3.46738  35.63441 31.38764 1.000 37.78147  ? 50  SER   A N   1 
ATOM   285  C CA  . SER   A 1 43  ? -3.12282  36.98305 30.94863 1.000 40.04635  ? 50  SER   A CA  1 
ATOM   286  C C   . SER   A 1 43  ? -2.50179  36.96401 29.55756 1.000 37.97571  ? 50  SER   A C   1 
ATOM   287  O O   . SER   A 1 43  ? -2.75299  37.86179 28.74443 1.000 36.01175  ? 50  SER   A O   1 
ATOM   288  C CB  . SER   A 1 43  ? -2.17396  37.63640 31.95320 1.000 42.70763  ? 50  SER   A CB  1 
ATOM   289  O OG  . SER   A 1 43  ? -2.89117  38.20503 33.03417 1.000 55.48655  ? 50  SER   A OG  1 
ATOM   290  N N   . ASN   A 1 44  ? -1.68429  35.94758 29.26749 1.000 37.30031  ? 51  ASN   A N   1 
ATOM   291  C CA  . ASN   A 1 44  ? -1.15635  35.78407 27.91676 1.000 37.04848  ? 51  ASN   A CA  1 
ATOM   292  C C   . ASN   A 1 44  ? -2.28236  35.57120 26.91423 1.000 37.50776  ? 51  ASN   A C   1 
ATOM   293  O O   . ASN   A 1 44  ? -2.27138  36.15017 25.82119 1.000 36.01418  ? 51  ASN   A O   1 
ATOM   294  C CB  . ASN   A 1 44  ? -0.17836  34.60963 27.87167 1.000 37.67701  ? 51  ASN   A CB  1 
ATOM   295  C CG  . ASN   A 1 44  ? 1.17720   34.95507 28.45058 1.000 40.41337  ? 51  ASN   A CG  1 
ATOM   296  O OD1 . ASN   A 1 44  ? 1.43630   36.10108 28.81679 1.000 43.25062  ? 51  ASN   A OD1 1 
ATOM   297  N ND2 . ASN   A 1 44  ? 2.05296   33.96102 28.53517 1.000 39.90508  ? 51  ASN   A ND2 1 
ATOM   298  N N   . SER   A 1 45  ? -3.26440  34.74027 27.27183 1.000 36.19899  ? 52  SER   A N   1 
ATOM   299  C CA  . SER   A 1 45  ? -4.39684  34.50032 26.38390 1.000 32.48156  ? 52  SER   A CA  1 
ATOM   300  C C   . SER   A 1 45  ? -5.21895  35.76704 26.18592 1.000 33.77282  ? 52  SER   A C   1 
ATOM   301  O O   . SER   A 1 45  ? -5.68186  36.04889 25.07416 1.000 35.64369  ? 52  SER   A O   1 
ATOM   302  C CB  . SER   A 1 45  ? -5.26855  33.37651 26.94361 1.000 34.26579  ? 52  SER   A CB  1 
ATOM   303  O OG  . SER   A 1 45  ? -4.59013  32.13361 26.89659 1.000 35.39560  ? 52  SER   A OG  1 
ATOM   304  N N   . SER   A 1 46  ? -5.41121  36.54297 27.25553 1.000 34.03282  ? 53  SER   A N   1 
ATOM   305  C CA  . SER   A 1 46  ? -6.15993  37.79033 27.14305 1.000 35.87850  ? 53  SER   A CA  1 
ATOM   306  C C   . SER   A 1 46  ? -5.46217  38.76986 26.20873 1.000 35.28668  ? 53  SER   A C   1 
ATOM   307  O O   . SER   A 1 46  ? -6.11886  39.46863 25.42747 1.000 34.01557  ? 53  SER   A O   1 
ATOM   308  C CB  . SER   A 1 46  ? -6.35064  38.41257 28.52603 1.000 41.25651  ? 53  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 46  ? -7.11258  39.60520 28.44978 1.000 43.49588  ? 53  SER   A OG  1 
ATOM   310  N N   . ASP   A 1 47  ? -4.12947  38.83734 26.27738 1.000 36.25808  ? 54  ASP   A N   1 
ATOM   311  C CA  . ASP   A 1 47  ? -3.38600  39.71509 25.37854 1.000 36.66264  ? 54  ASP   A CA  1 
ATOM   312  C C   . ASP   A 1 47  ? -3.52004  39.26307 23.92955 1.000 40.18351  ? 54  ASP   A C   1 
ATOM   313  O O   . ASP   A 1 47  ? -3.68954  40.09213 23.02831 1.000 35.81762  ? 54  ASP   A O   1 
ATOM   314  C CB  . ASP   A 1 47  ? -1.91329  39.76495 25.78526 1.000 39.65197  ? 54  ASP   A CB  1 
ATOM   315  C CG  . ASP   A 1 47  ? -1.69065  40.50794 27.08742 1.000 41.46461  ? 54  ASP   A CG  1 
ATOM   316  O OD1 . ASP   A 1 47  ? -2.61996  41.20623 27.54611 1.000 38.82818  ? 54  ASP   A OD1 1 
ATOM   317  O OD2 . ASP   A 1 47  ? -0.58387  40.39087 27.65384 1.000 41.39732  ? 54  ASP   A OD2 1 
ATOM   318  N N   . ALA   A 1 48  ? -3.44955  37.95197 23.68600 1.000 34.80974  ? 55  ALA   A N   1 
ATOM   319  C CA  . ALA   A 1 48  ? -3.58345  37.44388 22.32376 1.000 35.09814  ? 55  ALA   A CA  1 
ATOM   320  C C   . ALA   A 1 48  ? -4.98059  37.70103 21.77245 1.000 31.66447  ? 55  ALA   A C   1 
ATOM   321  O O   . ALA   A 1 48  ? -5.14632  37.96883 20.57593 1.000 32.70083  ? 55  ALA   A O   1 
ATOM   322  C CB  . ALA   A 1 48  ? -3.25415  35.95163 22.28577 1.000 33.34883  ? 55  ALA   A CB  1 
ATOM   323  N N   . LEU   A 1 49  ? -5.99999  37.62676 22.63119 1.000 31.49456  ? 56  LEU   A N   1 
ATOM   324  C CA  . LEU   A 1 49  ? -7.35586  37.93198 22.18819 1.000 32.59953  ? 56  LEU   A CA  1 
ATOM   325  C C   . LEU   A 1 49  ? -7.54170  39.42381 21.94191 1.000 33.45978  ? 56  LEU   A C   1 
ATOM   326  O O   . LEU   A 1 49  ? -8.29719  39.81246 21.04381 1.000 35.22250  ? 56  LEU   A O   1 
ATOM   327  C CB  . LEU   A 1 49  ? -8.37198  37.43256 23.21431 1.000 33.31778  ? 56  LEU   A CB  1 
ATOM   328  C CG  . LEU   A 1 49  ? -8.51831  35.91318 23.32215 1.000 34.80182  ? 56  LEU   A CG  1 
ATOM   329  C CD1 . LEU   A 1 49  ? -9.02555  35.52451 24.69888 1.000 33.36339  ? 56  LEU   A CD1 1 
ATOM   330  C CD2 . LEU   A 1 49  ? -9.44309  35.38145 22.23806 1.000 35.82825  ? 56  LEU   A CD2 1 
ATOM   331  N N   . ASP   A 1 50  ? -6.86507  40.27063 22.72256 1.000 35.33198  ? 57  ASP   A N   1 
ATOM   332  C CA  . ASP   A 1 50  ? -6.92691  41.70921 22.48128 1.000 34.93495  ? 57  ASP   A CA  1 
ATOM   333  C C   . ASP   A 1 50  ? -6.36152  42.06226 21.11191 1.000 32.87532  ? 57  ASP   A C   1 
ATOM   334  O O   . ASP   A 1 50  ? -6.88408  42.94795 20.42470 1.000 33.59938  ? 57  ASP   A O   1 
ATOM   335  C CB  . ASP   A 1 50  ? -6.16835  42.46310 23.57562 1.000 35.70270  ? 57  ASP   A CB  1 
ATOM   336  C CG  . ASP   A 1 50  ? -6.93678  42.53496 24.87898 1.000 38.87834  ? 57  ASP   A CG  1 
ATOM   337  O OD1 . ASP   A 1 50  ? -8.17754  42.39768 24.85078 1.000 39.49913  ? 57  ASP   A OD1 1 
ATOM   338  O OD2 . ASP   A 1 50  ? -6.29603  42.72897 25.93329 1.000 40.13750  ? 57  ASP   A OD2 1 
ATOM   339  N N   . LYS   A 1 51  ? -5.29712  41.37352 20.69495 1.000 32.88374  ? 58  LYS   A N   1 
ATOM   340  C CA  . LYS   A 1 51  ? -4.62779  41.72788 19.44781 1.000 35.25867  ? 58  LYS   A CA  1 
ATOM   341  C C   . LYS   A 1 51  ? -5.48441  41.37516 18.23735 1.000 35.42062  ? 58  LYS   A C   1 
ATOM   342  O O   . LYS   A 1 51  ? -5.63094  42.18394 17.31365 1.000 37.79512  ? 58  LYS   A O   1 
ATOM   343  C CB  . LYS   A 1 51  ? -3.26742  41.03607 19.36585 1.000 38.18710  ? 58  LYS   A CB  1 
ATOM   344  C CG  . LYS   A 1 51  ? -2.45788  41.44384 18.14892 1.000 55.64826  ? 58  LYS   A CG  1 
ATOM   345  C CD  . LYS   A 1 51  ? -0.96768  41.26339 18.37216 1.000 62.70135  ? 58  LYS   A CD  1 
ATOM   346  C CE  . LYS   A 1 51  ? -0.17439  41.87108 17.22682 1.000 57.63910  ? 58  LYS   A CE  1 
ATOM   347  N NZ  . LYS   A 1 51  ? 1.14851   41.21388 17.04894 1.000 61.68949  ? 58  LYS   A NZ  1 
ATOM   348  N N   . ILE   A 1 52  ? -6.05402  40.16718 18.21666 1.000 34.65120  ? 59  ILE   A N   1 
ATOM   349  C CA  . ILE   A 1 52  ? -6.88847  39.78374 17.08171 1.000 35.11474  ? 59  ILE   A CA  1 
ATOM   350  C C   . ILE   A 1 52  ? -8.16892  40.60827 17.05700 1.000 34.26861  ? 59  ILE   A C   1 
ATOM   351  O O   . ILE   A 1 52  ? -8.69292  40.92331 15.98127 1.000 36.66149  ? 59  ILE   A O   1 
ATOM   352  C CB  . ILE   A 1 52  ? -7.18090  38.26977 17.10588 1.000 31.28584  ? 59  ILE   A CB  1 
ATOM   353  C CG1 . ILE   A 1 52  ? -7.90138  37.84243 15.82403 1.000 35.61802  ? 59  ILE   A CG1 1 
ATOM   354  C CG2 . ILE   A 1 52  ? -7.99058  37.88269 18.33755 1.000 32.88059  ? 59  ILE   A CG2 1 
ATOM   355  C CD1 . ILE   A 1 52  ? -7.11738  38.12223 14.55898 1.000 34.67395  ? 59  ILE   A CD1 1 
ATOM   356  N N   . ARG   A 1 53  ? -8.68403  40.98598 18.22880 1.000 35.86396  ? 60  ARG   A N   1 
ATOM   357  C CA  . ARG   A 1 53  ? -9.86420  41.84090 18.27591 1.000 38.06157  ? 60  ARG   A CA  1 
ATOM   358  C C   . ARG   A 1 53  ? -9.54843  43.23632 17.75445 1.000 37.25547  ? 60  ARG   A C   1 
ATOM   359  O O   . ARG   A 1 53  ? -10.34326 43.82330 17.01102 1.000 38.83687  ? 60  ARG   A O   1 
ATOM   360  C CB  . ARG   A 1 53  ? -10.40195 41.90588 19.70450 1.000 38.90678  ? 60  ARG   A CB  1 
ATOM   361  C CG  . ARG   A 1 53  ? -11.62193 42.78917 19.87362 1.000 47.60689  ? 60  ARG   A CG  1 
ATOM   362  C CD  . ARG   A 1 53  ? -12.35582 42.45218 21.15806 1.000 60.83777  ? 60  ARG   A CD  1 
ATOM   363  N NE  . ARG   A 1 53  ? -13.11187 43.59325 21.65641 1.000 75.84802  ? 60  ARG   A NE  1 
ATOM   364  C CZ  . ARG   A 1 53  ? -12.90533 44.16777 22.83387 1.000 79.04500  ? 60  ARG   A CZ  1 
ATOM   365  N NH1 . ARG   A 1 53  ? -11.97582 43.72611 23.66751 1.000 59.56462  ? 60  ARG   A NH1 1 
ATOM   366  N NH2 . ARG   A 1 53  ? -13.64713 45.21382 23.18326 1.000 69.95558  ? 60  ARG   A NH2 1 
ATOM   367  N N   . TYR   A 1 54  ? -8.38852  43.77910 18.12971 1.000 37.41298  ? 61  TYR   A N   1 
ATOM   368  C CA  . TYR   A 1 54  ? -7.98560  45.09270 17.63881 1.000 38.16989  ? 61  TYR   A CA  1 
ATOM   369  C C   . TYR   A 1 54  ? -7.76068  45.06841 16.13174 1.000 37.88674  ? 61  TYR   A C   1 
ATOM   370  O O   . TYR   A 1 54  ? -8.20779  45.96740 15.40955 1.000 37.65389  ? 61  TYR   A O   1 
ATOM   371  C CB  . TYR   A 1 54  ? -6.72277  45.55413 18.36765 1.000 36.41544  ? 61  TYR   A CB  1 
ATOM   372  C CG  . TYR   A 1 54  ? -6.07980  46.77968 17.76226 1.000 35.99068  ? 61  TYR   A CG  1 
ATOM   373  C CD1 . TYR   A 1 54  ? -6.63569  48.03907 17.94130 1.000 38.50251  ? 61  TYR   A CD1 1 
ATOM   374  C CD2 . TYR   A 1 54  ? -4.91842  46.67681 17.00815 1.000 38.72947  ? 61  TYR   A CD2 1 
ATOM   375  C CE1 . TYR   A 1 54  ? -6.05134  49.16286 17.38829 1.000 36.76346  ? 61  TYR   A CE1 1 
ATOM   376  C CE2 . TYR   A 1 54  ? -4.32754  47.79378 16.45044 1.000 40.61173  ? 61  TYR   A CE2 1 
ATOM   377  C CZ  . TYR   A 1 54  ? -4.89800  49.03428 16.64362 1.000 39.79540  ? 61  TYR   A CZ  1 
ATOM   378  O OH  . TYR   A 1 54  ? -4.31144  50.14915 16.09017 1.000 43.99561  ? 61  TYR   A OH  1 
ATOM   379  N N   . GLU   A 1 55  ? -7.06738  44.03847 15.63859 1.000 35.29554  ? 62  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 55  ? -6.79138  43.94382 14.20923 1.000 40.97357  ? 62  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 55  ? -8.06863  43.76679 13.39960 1.000 39.93378  ? 62  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 55  ? -8.14957  44.24056 12.26060 1.000 40.20486  ? 62  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 55  ? -5.82828  42.78789 13.93721 1.000 42.48296  ? 62  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 55  ? -4.39750  43.06039 14.36736 1.000 47.70988  ? 62  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 55  ? -3.42297  42.02267 13.84668 1.000 60.88142  ? 62  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 55  ? -3.84517  41.15098 13.05834 1.000 55.78016  ? 62  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 55  ? -2.23458  42.07802 14.22744 1.000 68.23284  ? 62  GLU   A OE2 1 
ATOM   388  N N   . SER   A 1 56  ? -9.07331  43.09647 13.96741 1.000 37.24191  ? 63  SER   A N   1 
ATOM   389  C CA  . SER   A 1 56  ? -10.32389 42.87503 13.25247 1.000 41.03864  ? 63  SER   A CA  1 
ATOM   390  C C   . SER   A 1 56  ? -11.13032 44.15446 13.07626 1.000 42.16480  ? 63  SER   A C   1 
ATOM   391  O O   . SER   A 1 56  ? -12.01664 44.19769 12.21645 1.000 42.46830  ? 63  SER   A O   1 
ATOM   392  C CB  . SER   A 1 56  ? -11.16544 41.82901 13.98329 1.000 39.08056  ? 63  SER   A CB  1 
ATOM   393  O OG  . SER   A 1 56  ? -11.78683 42.38459 15.12910 1.000 38.49958  ? 63  SER   A OG  1 
ATOM   394  N N   . LEU   A 1 57  ? -10.84691 45.19263 13.86702 1.000 42.05129  ? 64  LEU   A N   1 
ATOM   395  C CA  . LEU   A 1 57  ? -11.60221 46.43587 13.75234 1.000 45.15512  ? 64  LEU   A CA  1 
ATOM   396  C C   . LEU   A 1 57  ? -11.33065 47.14137 12.43008 1.000 46.49245  ? 64  LEU   A C   1 
ATOM   397  O O   . LEU   A 1 57  ? -12.21218 47.83161 11.90631 1.000 51.53671  ? 64  LEU   A O   1 
ATOM   398  C CB  . LEU   A 1 57  ? -11.27708 47.35602 14.92852 1.000 46.03688  ? 64  LEU   A CB  1 
ATOM   399  C CG  . LEU   A 1 57  ? -11.61070 46.77783 16.30570 1.000 45.66316  ? 64  LEU   A CG  1 
ATOM   400  C CD1 . LEU   A 1 57  ? -11.37402 47.80304 17.40146 1.000 47.88594  ? 64  LEU   A CD1 1 
ATOM   401  C CD2 . LEU   A 1 57  ? -13.04491 46.26872 16.34243 1.000 47.38535  ? 64  LEU   A CD2 1 
ATOM   402  N N   . THR   A 1 58  ? -10.12851 46.98330 11.87761 1.000 42.20653  ? 65  THR   A N   1 
ATOM   403  C CA  . THR   A 1 58  ? -9.79928  47.52830 10.56841 1.000 47.63121  ? 65  THR   A CA  1 
ATOM   404  C C   . THR   A 1 58  ? -9.83920  46.48149 9.46304  1.000 52.55818  ? 65  THR   A C   1 
ATOM   405  O O   . THR   A 1 58  ? -9.84575  46.84919 8.28402  1.000 50.39701  ? 65  THR   A O   1 
ATOM   406  C CB  . THR   A 1 58  ? -8.41245  48.18527 10.59601 1.000 48.34592  ? 65  THR   A CB  1 
ATOM   407  O OG1 . THR   A 1 58  ? -7.44962  47.25509 11.10708 1.000 49.49948  ? 65  THR   A OG1 1 
ATOM   408  C CG2 . THR   A 1 58  ? -8.42873  49.42882 11.47336 1.000 49.96281  ? 65  THR   A CG2 1 
ATOM   409  N N   . ASP   A 1 59  ? -9.86797  45.19613 9.81197  1.000 50.17622  ? 66  ASP   A N   1 
ATOM   410  C CA  . ASP   A 1 59  ? -9.93091  44.11461 8.83099  1.000 50.97736  ? 66  ASP   A CA  1 
ATOM   411  C C   . ASP   A 1 59  ? -10.79217 43.00600 9.41257  1.000 49.82487  ? 66  ASP   A C   1 
ATOM   412  O O   . ASP   A 1 59  ? -10.28554 42.07100 10.04715 1.000 48.03416  ? 66  ASP   A O   1 
ATOM   413  C CB  . ASP   A 1 59  ? -8.53458  43.60370 8.47344  1.000 52.03640  ? 66  ASP   A CB  1 
ATOM   414  C CG  . ASP   A 1 59  ? -8.54966  42.60891 7.32546  1.000 58.33956  ? 66  ASP   A CG  1 
ATOM   415  O OD1 . ASP   A 1 59  ? -9.64128  42.31308 6.79300  1.000 58.81341  ? 66  ASP   A OD1 1 
ATOM   416  O OD2 . ASP   A 1 59  ? -7.46280  42.11856 6.95349  1.000 62.15165  ? 66  ASP   A OD2 1 
ATOM   417  N N   . PRO   A 1 60  ? -12.11120 43.07799 9.22196  1.000 49.37701  ? 67  PRO   A N   1 
ATOM   418  C CA  . PRO   A 1 60  ? -12.99382 42.04906 9.79372  1.000 49.55462  ? 67  PRO   A CA  1 
ATOM   419  C C   . PRO   A 1 60  ? -12.74511 40.65538 9.24616  1.000 47.83508  ? 67  PRO   A C   1 
ATOM   420  O O   . PRO   A 1 60  ? -13.15393 39.67722 9.88382  1.000 46.65918  ? 67  PRO   A O   1 
ATOM   421  C CB  . PRO   A 1 60  ? -14.39805 42.54994 9.42781  1.000 52.48991  ? 67  PRO   A CB  1 
ATOM   422  C CG  . PRO   A 1 60  ? -14.22699 44.02294 9.22680  1.000 51.68266  ? 67  PRO   A CG  1 
ATOM   423  C CD  . PRO   A 1 60  ? -12.87526 44.16800 8.59433  1.000 52.49510  ? 67  PRO   A CD  1 
ATOM   424  N N   . SER   A 1 61  ? -12.09143 40.52835 8.08867  1.000 47.85949  ? 68  SER   A N   1 
ATOM   425  C CA  . SER   A 1 61  ? -11.79964 39.21394 7.52928  1.000 48.34995  ? 68  SER   A CA  1 
ATOM   426  C C   . SER   A 1 61  ? -10.79461 38.42866 8.36191  1.000 49.72008  ? 68  SER   A C   1 
ATOM   427  O O   . SER   A 1 61  ? -10.64627 37.22140 8.14430  1.000 48.71617  ? 68  SER   A O   1 
ATOM   428  C CB  . SER   A 1 61  ? -11.28647 39.35459 6.09469  1.000 49.59019  ? 68  SER   A CB  1 
ATOM   429  O OG  . SER   A 1 61  ? -9.94852  39.81927 6.07440  1.000 54.05307  ? 68  SER   A OG  1 
ATOM   430  N N   . LYS   A 1 62  ? -10.10339 39.07699 9.30257  1.000 44.04324  ? 69  LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 62  ? -9.20989  38.35442 10.19894 1.000 47.17233  ? 69  LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 62  ? -9.96915  37.42983 11.14023 1.000 44.29835  ? 69  LYS   A C   1 
ATOM   433  O O   . LYS   A 1 62  ? -9.36095  36.53155 11.73165 1.000 42.87804  ? 69  LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 62  ? -8.36131  39.33973 11.00395 1.000 44.22919  ? 69  LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 62  ? -7.52530  40.27587 10.14716 1.000 46.21396  ? 69  LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 62  ? -6.16689  40.53959 10.77221 1.000 47.40616  ? 69  LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 62  ? -5.35000  41.49731 9.92109  1.000 49.24787  ? 69  LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 62  ? -3.89671  41.41619 10.22954 1.000 55.24911  ? 69  LYS   A NZ  1 
ATOM   439  N N   . LEU   A 1 63  ? -11.27680 37.62949 11.29104 1.000 41.12827  ? 70  LEU   A N   1 
ATOM   440  C CA  . LEU   A 1 63  ? -12.11920 36.76657 12.10526 1.000 43.70210  ? 70  LEU   A CA  1 
ATOM   441  C C   . LEU   A 1 63  ? -12.76924 35.65012 11.29789 1.000 46.80500  ? 70  LEU   A C   1 
ATOM   442  O O   . LEU   A 1 63  ? -13.60428 34.91776 11.83860 1.000 42.90928  ? 70  LEU   A O   1 
ATOM   443  C CB  . LEU   A 1 63  ? -13.19726 37.59509 12.80797 1.000 47.56913  ? 70  LEU   A CB  1 
ATOM   444  C CG  . LEU   A 1 63  ? -12.70285 38.59656 13.85316 1.000 44.99913  ? 70  LEU   A CG  1 
ATOM   445  C CD1 . LEU   A 1 63  ? -13.87430 39.26712 14.55079 1.000 49.27003  ? 70  LEU   A CD1 1 
ATOM   446  C CD2 . LEU   A 1 63  ? -11.78965 37.91936 14.86662 1.000 40.39720  ? 70  LEU   A CD2 1 
ATOM   447  N N   . ASP   A 1 64  ? -12.40940 35.50723 10.01852 1.000 46.01059  ? 71  ASP   A N   1 
ATOM   448  C CA  . ASP   A 1 64  ? -12.94524 34.41234 9.21596  1.000 48.99963  ? 71  ASP   A CA  1 
ATOM   449  C C   . ASP   A 1 64  ? -12.53739 33.05787 9.77802  1.000 46.58859  ? 71  ASP   A C   1 
ATOM   450  O O   . ASP   A 1 64  ? -13.24496 32.06358 9.57910  1.000 44.62536  ? 71  ASP   A O   1 
ATOM   451  C CB  . ASP   A 1 64  ? -12.47981 34.54488 7.76567  1.000 48.34621  ? 71  ASP   A CB  1 
ATOM   452  C CG  . ASP   A 1 64  ? -13.15478 35.69121 7.03863  1.000 53.27021  ? 71  ASP   A CG  1 
ATOM   453  O OD1 . ASP   A 1 64  ? -14.08893 36.29266 7.60964  1.000 49.31540  ? 71  ASP   A OD1 1 
ATOM   454  O OD2 . ASP   A 1 64  ? -12.74890 35.99140 5.89623  1.000 51.01940  ? 71  ASP   A OD2 1 
ATOM   455  N N   . SER   A 1 65  ? -11.40584 32.99904 10.47919 1.000 44.50739  ? 72  SER   A N   1 
ATOM   456  C CA  . SER   A 1 65  ? -10.93359 31.78457 11.12839 1.000 43.31341  ? 72  SER   A CA  1 
ATOM   457  C C   . SER   A 1 65  ? -11.56077 31.56501 12.49983 1.000 51.98544  ? 72  SER   A C   1 
ATOM   458  O O   . SER   A 1 65  ? -11.04427 30.75985 13.28384 1.000 46.26319  ? 72  SER   A O   1 
ATOM   459  C CB  . SER   A 1 65  ? -9.40880  31.81874 11.25410 1.000 43.93203  ? 72  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 65  ? -8.96512  33.09696 11.67872 1.000 39.74182  ? 72  SER   A OG  1 
ATOM   461  N N   . GLY   A 1 66  ? -12.65155 32.26045 12.81012 1.000 46.14388  ? 73  GLY   A N   1 
ATOM   462  C CA  . GLY   A 1 66  ? -13.30271 32.11153 14.09579 1.000 45.77966  ? 73  GLY   A CA  1 
ATOM   463  C C   . GLY   A 1 66  ? -13.70367 33.43571 14.71047 1.000 46.79836  ? 73  GLY   A C   1 
ATOM   464  O O   . GLY   A 1 66  ? -12.85166 34.28885 14.97514 1.000 43.34288  ? 73  GLY   A O   1 
ATOM   465  N N   . LYS   A 1 67  ? -15.00508 33.61891 14.94159 1.000 50.06774  ? 74  LYS   A N   1 
ATOM   466  C CA  . LYS   A 1 67  ? -15.49514 34.86696 15.51593 1.000 51.91699  ? 74  LYS   A CA  1 
ATOM   467  C C   . LYS   A 1 67  ? -15.41848 34.86862 17.03838 1.000 52.51482  ? 74  LYS   A C   1 
ATOM   468  O O   . LYS   A 1 67  ? -15.16950 35.91970 17.63943 1.000 50.09756  ? 74  LYS   A O   1 
ATOM   469  C CB  . LYS   A 1 67  ? -16.93238 35.12177 15.05403 1.000 54.96166  ? 74  LYS   A CB  1 
ATOM   470  C CG  . LYS   A 1 67  ? -17.64605 36.26121 15.76954 1.000 82.04263  ? 74  LYS   A CG  1 
ATOM   471  C CD  . LYS   A 1 67  ? -16.96905 37.60091 15.51819 1.000 86.86663  ? 74  LYS   A CD  1 
ATOM   472  C CE  . LYS   A 1 67  ? -17.52633 38.68129 16.43471 1.000 77.18442  ? 74  LYS   A CE  1 
ATOM   473  N NZ  . LYS   A 1 67  ? -18.83171 38.28847 17.03705 1.000 73.93358  ? 74  LYS   A NZ  1 
ATOM   474  N N   . GLU   A 1 68  ? -15.60740 33.71411 17.67221 1.000 52.66189  ? 75  GLU   A N   1 
ATOM   475  C CA  . GLU   A 1 68  ? -15.63654 33.65055 19.12738 1.000 53.16205  ? 75  GLU   A CA  1 
ATOM   476  C C   . GLU   A 1 68  ? -14.26748 33.96648 19.71876 1.000 47.56589  ? 75  GLU   A C   1 
ATOM   477  O O   . GLU   A 1 68  ? -13.23754 33.48018 19.24390 1.000 44.91514  ? 75  GLU   A O   1 
ATOM   478  C CB  . GLU   A 1 68  ? -16.09807 32.26835 19.58722 1.000 57.20466  ? 75  GLU   A CB  1 
ATOM   479  C CG  . GLU   A 1 68  ? -17.27929 31.71964 18.80415 1.000 71.71313  ? 75  GLU   A CG  1 
ATOM   480  C CD  . GLU   A 1 68  ? -16.87887 30.61610 17.84408 1.000 107.21237 ? 75  GLU   A CD  1 
ATOM   481  O OE1 . GLU   A 1 68  ? -16.98072 29.43095 18.22468 1.000 113.82146 ? 75  GLU   A OE1 1 
ATOM   482  O OE2 . GLU   A 1 68  ? -16.46223 30.93282 16.70933 1.000 84.72706  ? 75  GLU   A OE2 1 
ATOM   483  N N   . LEU   A 1 69  ? -14.26545 34.78815 20.76621 1.000 44.48594  ? 76  LEU   A N   1 
ATOM   484  C CA  . LEU   A 1 69  ? -13.05352 35.18818 21.47921 1.000 42.73524  ? 76  LEU   A CA  1 
ATOM   485  C C   . LEU   A 1 69  ? -13.22566 34.76438 22.93453 1.000 40.84880  ? 76  LEU   A C   1 
ATOM   486  O O   . LEU   A 1 69  ? -13.94921 35.41557 23.69466 1.000 40.21942  ? 76  LEU   A O   1 
ATOM   487  C CB  . LEU   A 1 69  ? -12.81524 36.69109 21.35512 1.000 41.17669  ? 76  LEU   A CB  1 
ATOM   488  C CG  . LEU   A 1 69  ? -12.77693 37.26655 19.93752 1.000 42.45484  ? 76  LEU   A CG  1 
ATOM   489  C CD1 . LEU   A 1 69  ? -12.70609 38.78567 19.97899 1.000 42.50888  ? 76  LEU   A CD1 1 
ATOM   490  C CD2 . LEU   A 1 69  ? -11.60718 36.69245 19.15101 1.000 35.69889  ? 76  LEU   A CD2 1 
ATOM   491  N N   . HIS   A 1 70  ? -12.56729 33.67456 23.32478 1.000 39.10554  ? 77  HIS   A N   1 
ATOM   492  C CA  . HIS   A 1 70  ? -12.77516 33.10647 24.64821 1.000 37.19950  ? 77  HIS   A CA  1 
ATOM   493  C C   . HIS   A 1 70  ? -11.52216 32.36730 25.09520 1.000 38.52478  ? 77  HIS   A C   1 
ATOM   494  O O   . HIS   A 1 70  ? -10.58672 32.15255 24.32026 1.000 34.60006  ? 77  HIS   A O   1 
ATOM   495  C CB  . HIS   A 1 70  ? -13.98779 32.16854 24.66137 1.000 41.38028  ? 77  HIS   A CB  1 
ATOM   496  C CG  . HIS   A 1 70  ? -13.89886 31.05159 23.66743 1.000 42.89094  ? 77  HIS   A CG  1 
ATOM   497  N ND1 . HIS   A 1 70  ? -14.74840 30.94758 22.58734 1.000 43.71110  ? 77  HIS   A ND1 1 
ATOM   498  C CD2 . HIS   A 1 70  ? -13.06349 29.98833 23.59177 1.000 42.16717  ? 77  HIS   A CD2 1 
ATOM   499  C CE1 . HIS   A 1 70  ? -14.43850 29.87083 21.88753 1.000 46.06561  ? 77  HIS   A CE1 1 
ATOM   500  N NE2 . HIS   A 1 70  ? -13.41967 29.27087 22.47591 1.000 44.28382  ? 77  HIS   A NE2 1 
ATOM   501  N N   . ILE   A 1 71  ? -11.52113 31.97893 26.36865 1.000 36.26780  ? 78  ILE   A N   1 
ATOM   502  C CA  . ILE   A 1 71  ? -10.46825 31.16591 26.96510 1.000 35.26619  ? 78  ILE   A CA  1 
ATOM   503  C C   . ILE   A 1 71  ? -11.11812 29.93361 27.57648 1.000 37.42966  ? 78  ILE   A C   1 
ATOM   504  O O   . ILE   A 1 71  ? -12.11024 30.04866 28.30494 1.000 36.89675  ? 78  ILE   A O   1 
ATOM   505  C CB  . ILE   A 1 71  ? -9.67494  31.94534 28.03035 1.000 34.63942  ? 78  ILE   A CB  1 
ATOM   506  C CG1 . ILE   A 1 71  ? -9.16262  33.26859 27.46030 1.000 33.28807  ? 78  ILE   A CG1 1 
ATOM   507  C CG2 . ILE   A 1 71  ? -8.51738  31.10651 28.55412 1.000 36.31059  ? 78  ILE   A CG2 1 
ATOM   508  C CD1 . ILE   A 1 71  ? -8.55903  34.18741 28.50077 1.000 35.29661  ? 78  ILE   A CD1 1 
ATOM   509  N N   . ASN   A 1 72  ? -10.56419 28.76055 27.28018 1.000 34.62759  ? 79  ASN   A N   1 
ATOM   510  C CA  . ASN   A 1 72  ? -11.06834 27.49706 27.80245 1.000 37.57098  ? 79  ASN   A CA  1 
ATOM   511  C C   . ASN   A 1 72  ? -9.98855  26.82696 28.63966 1.000 37.27200  ? 79  ASN   A C   1 
ATOM   512  O O   . ASN   A 1 72  ? -8.83164  26.74014 28.21434 1.000 37.17720  ? 79  ASN   A O   1 
ATOM   513  C CB  . ASN   A 1 72  ? -11.51203 26.56371 26.67078 1.000 35.12829  ? 79  ASN   A CB  1 
ATOM   514  C CG  . ASN   A 1 72  ? -12.79542 27.02086 26.00404 1.000 41.06491  ? 79  ASN   A CG  1 
ATOM   515  O OD1 . ASN   A 1 72  ? -13.61140 27.71531 26.61020 1.000 40.80038  ? 79  ASN   A OD1 1 
ATOM   516  N ND2 . ASN   A 1 72  ? -12.98221 26.62766 24.74939 1.000 41.18537  ? 79  ASN   A ND2 1 
ATOM   517  N N   . LEU   A 1 73  ? -10.36853 26.35987 29.82589 1.000 34.80126  ? 80  LEU   A N   1 
ATOM   518  C CA  . LEU   A 1 73  ? -9.48086  25.62212 30.71644 1.000 37.15184  ? 80  LEU   A CA  1 
ATOM   519  C C   . LEU   A 1 73  ? -9.94260  24.17211 30.75849 1.000 39.92742  ? 80  LEU   A C   1 
ATOM   520  O O   . LEU   A 1 73  ? -11.08319 23.89275 31.14381 1.000 40.82432  ? 80  LEU   A O   1 
ATOM   521  C CB  . LEU   A 1 73  ? -9.47728  26.23018 32.11872 1.000 34.99995  ? 80  LEU   A CB  1 
ATOM   522  C CG  . LEU   A 1 73  ? -9.29746  27.74678 32.20770 1.000 38.78380  ? 80  LEU   A CG  1 
ATOM   523  C CD1 . LEU   A 1 73  ? -9.39836  28.21182 33.65184 1.000 38.68676  ? 80  LEU   A CD1 1 
ATOM   524  C CD2 . LEU   A 1 73  ? -7.97138  28.17016 31.59611 1.000 35.05206  ? 80  LEU   A CD2 1 
ATOM   525  N N   . ILE   A 1 74  ? -9.06193  23.25717 30.36389 1.000 36.63825  ? 81  ILE   A N   1 
ATOM   526  C CA  . ILE   A 1 74  ? -9.42859  21.85151 30.20873 1.000 39.33694  ? 81  ILE   A CA  1 
ATOM   527  C C   . ILE   A 1 74  ? -8.48916  20.96925 31.02328 1.000 40.30576  ? 81  ILE   A C   1 
ATOM   528  O O   . ILE   A 1 74  ? -7.41215  20.59736 30.53527 1.000 36.29732  ? 81  ILE   A O   1 
ATOM   529  C CB  . ILE   A 1 74  ? -9.41503  21.43819 28.72815 1.000 40.85882  ? 81  ILE   A CB  1 
ATOM   530  C CG1 . ILE   A 1 74  ? -10.22798 22.42636 27.88764 1.000 40.58742  ? 81  ILE   A CG1 1 
ATOM   531  C CG2 . ILE   A 1 74  ? -9.95238  20.02366 28.56335 1.000 41.44684  ? 81  ILE   A CG2 1 
ATOM   532  C CD1 . ILE   A 1 74  ? -9.96642  22.32791 26.40148 1.000 41.18780  ? 81  ILE   A CD1 1 
ATOM   533  N N   . PRO   A 1 75  ? -8.84282  20.61450 32.25494 1.000 38.32039  ? 82  PRO   A N   1 
ATOM   534  C CA  . PRO   A 1 75  ? -8.04223  19.64084 33.00051 1.000 41.68388  ? 82  PRO   A CA  1 
ATOM   535  C C   . PRO   A 1 75  ? -8.34771  18.21695 32.56457 1.000 47.74599  ? 82  PRO   A C   1 
ATOM   536  O O   . PRO   A 1 75  ? -9.47260  17.87969 32.18722 1.000 46.53069  ? 82  PRO   A O   1 
ATOM   537  C CB  . PRO   A 1 75  ? -8.46804  19.87800 34.45385 1.000 42.49926  ? 82  PRO   A CB  1 
ATOM   538  C CG  . PRO   A 1 75  ? -9.87209  20.36925 34.34308 1.000 43.05010  ? 82  PRO   A CG  1 
ATOM   539  C CD  . PRO   A 1 75  ? -9.93758  21.17338 33.06818 1.000 38.87176  ? 82  PRO   A CD  1 
ATOM   540  N N   . ASN   A 1 76  ? -7.31543  17.37542 32.62009 1.000 46.65835  ? 83  ASN   A N   1 
ATOM   541  C CA  . ASN   A 1 76  ? -7.43168  15.96914 32.23105 1.000 47.06205  ? 83  ASN   A CA  1 
ATOM   542  C C   . ASN   A 1 76  ? -6.66413  15.14257 33.25793 1.000 50.44014  ? 83  ASN   A C   1 
ATOM   543  O O   . ASN   A 1 76  ? -5.43541  15.04630 33.19181 1.000 47.75815  ? 83  ASN   A O   1 
ATOM   544  C CB  . ASN   A 1 76  ? -6.90508  15.73982 30.81843 1.000 47.86801  ? 83  ASN   A CB  1 
ATOM   545  C CG  . ASN   A 1 76  ? -7.27640  14.37379 30.26819 1.000 53.56820  ? 83  ASN   A CG  1 
ATOM   546  O OD1 . ASN   A 1 76  ? -7.09122  13.35100 30.92777 1.000 52.60103  ? 83  ASN   A OD1 1 
ATOM   547  N ND2 . ASN   A 1 76  ? -7.80578  14.35318 29.05053 1.000 53.72208  ? 83  ASN   A ND2 1 
ATOM   548  N N   . LYS   A 1 77  ? -7.39563  14.54590 34.20193 1.000 53.38427  ? 84  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 77  ? -6.75524  13.77116 35.26055 1.000 55.56142  ? 84  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 77  ? -6.07632  12.52400 34.70891 1.000 56.34869  ? 84  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 77  ? -5.02443  12.11162 35.21161 1.000 54.91474  ? 84  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 77  ? -7.78314  13.38912 36.32452 1.000 56.97608  ? 84  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 77  ? -7.86357  14.35434 37.49184 1.000 60.90984  ? 84  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 77  ? -9.21404  14.26059 38.17908 1.000 67.65068  ? 84  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 77  ? -9.11378  14.63584 39.64655 1.000 73.05188  ? 84  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 77  ? -10.17780 15.59634 40.04599 1.000 76.02661  ? 84  LYS   A NZ  1 
ATOM   557  N N   . GLN   A 1 78  ? -6.66373  11.90858 33.68002 1.000 57.10274  ? 85  GLN   A N   1 
ATOM   558  C CA  . GLN   A 1 78  ? -6.09852  10.68235 33.12503 1.000 62.33466  ? 85  GLN   A CA  1 
ATOM   559  C C   . GLN   A 1 78  ? -4.73709  10.94434 32.49368 1.000 60.72646  ? 85  GLN   A C   1 
ATOM   560  O O   . GLN   A 1 78  ? -3.75923  10.24599 32.78448 1.000 62.17865  ? 85  GLN   A O   1 
ATOM   561  C CB  . GLN   A 1 78  ? -7.06383  10.07827 32.10377 1.000 66.74575  ? 85  GLN   A CB  1 
ATOM   562  C CG  . GLN   A 1 78  ? -6.41459  9.12184  31.11682 1.000 75.60747  ? 85  GLN   A CG  1 
ATOM   563  C CD  . GLN   A 1 78  ? -6.84562  7.68479  31.32903 1.000 90.27212  ? 85  GLN   A CD  1 
ATOM   564  O OE1 . GLN   A 1 78  ? -7.25475  7.30178  32.42530 1.000 95.79707  ? 85  GLN   A OE1 1 
ATOM   565  N NE2 . GLN   A 1 78  ? -6.76007  6.88084  30.27601 1.000 94.13655  ? 85  GLN   A NE2 1 
ATOM   566  N N   . ASP   A 1 79  ? -4.65487  11.95146 31.62444 1.000 55.78134  ? 86  ASP   A N   1 
ATOM   567  C CA  . ASP   A 1 79  ? -3.39119  12.31744 30.99973 1.000 54.27103  ? 86  ASP   A CA  1 
ATOM   568  C C   . ASP   A 1 79  ? -2.51726  13.18402 31.89566 1.000 52.47590  ? 86  ASP   A C   1 
ATOM   569  O O   . ASP   A 1 79  ? -1.35869  13.43248 31.54348 1.000 50.30502  ? 86  ASP   A O   1 
ATOM   570  C CB  . ASP   A 1 79  ? -3.64885  13.05137 29.68103 1.000 55.20802  ? 86  ASP   A CB  1 
ATOM   571  C CG  . ASP   A 1 79  ? -4.46542  12.22837 28.70508 1.000 60.62285  ? 86  ASP   A CG  1 
ATOM   572  O OD1 . ASP   A 1 79  ? -4.55956  10.99739 28.89438 1.000 58.94172  ? 86  ASP   A OD1 1 
ATOM   573  O OD2 . ASP   A 1 79  ? -5.01453  12.81397 27.74831 1.000 58.88112  ? 86  ASP   A OD2 1 
ATOM   574  N N   . ARG   A 1 80  ? -3.04163  13.63989 33.03587 1.000 51.59586  ? 87  ARG   A N   1 
ATOM   575  C CA  . ARG   A 1 80  ? -2.33347  14.55366 33.93397 1.000 49.69951  ? 87  ARG   A CA  1 
ATOM   576  C C   . ARG   A 1 80  ? -1.88163  15.80888 33.18929 1.000 45.14031  ? 87  ARG   A C   1 
ATOM   577  O O   . ARG   A 1 80  ? -0.73173  16.24221 33.28729 1.000 42.87627  ? 87  ARG   A O   1 
ATOM   578  C CB  . ARG   A 1 80  ? -1.15120  13.86049 34.61547 1.000 52.21935  ? 87  ARG   A CB  1 
ATOM   579  C CG  . ARG   A 1 80  ? -0.86041  14.38232 36.01311 1.000 56.57143  ? 87  ARG   A CG  1 
ATOM   580  C CD  . ARG   A 1 80  ? 0.61851   14.28756 36.34182 1.000 55.07142  ? 87  ARG   A CD  1 
ATOM   581  N NE  . ARG   A 1 80  ? 1.01916   12.91733 36.63472 1.000 64.17716  ? 87  ARG   A NE  1 
ATOM   582  C CZ  . ARG   A 1 80  ? 2.26460   12.46876 36.56081 1.000 72.73070  ? 87  ARG   A CZ  1 
ATOM   583  N NH1 . ARG   A 1 80  ? 3.26544   13.26115 36.21283 1.000 62.43977  ? 87  ARG   A NH1 1 
ATOM   584  N NH2 . ARG   A 1 80  ? 2.51212   11.19300 36.84300 1.000 65.90839  ? 87  ARG   A NH2 1 
ATOM   585  N N   . THR   A 1 81  ? -2.80547  16.39238 32.42990 1.000 43.65231  ? 88  THR   A N   1 
ATOM   586  C CA  . THR   A 1 81  ? -2.53441  17.59311 31.65545 1.000 42.54950  ? 88  THR   A CA  1 
ATOM   587  C C   . THR   A 1 81  ? -3.58889  18.64776 31.94985 1.000 40.89318  ? 88  THR   A C   1 
ATOM   588  O O   . THR   A 1 81  ? -4.77528  18.33403 32.08566 1.000 41.40525  ? 88  THR   A O   1 
ATOM   589  C CB  . THR   A 1 81  ? -2.51106  17.30744 30.14581 1.000 42.84306  ? 88  THR   A CB  1 
ATOM   590  O OG1 . THR   A 1 81  ? -3.78420  16.79447 29.73414 1.000 44.09380  ? 88  THR   A OG1 1 
ATOM   591  C CG2 . THR   A 1 81  ? -1.42175  16.30235 29.80154 1.000 44.84828  ? 88  THR   A CG2 1 
ATOM   592  N N   . LEU   A 1 82  ? -3.14591  19.89660 32.05256 1.000 37.94264  ? 89  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 82  ? -4.03042  21.05140 32.12775 1.000 36.80230  ? 89  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 82  ? -3.83735  21.86770 30.85869 1.000 38.44394  ? 89  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 82  ? -2.72352  22.31963 30.57080 1.000 38.95296  ? 89  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 82  ? -3.74399  21.89733 33.36791 1.000 38.05827  ? 89  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 82  ? -4.55258  23.19219 33.47776 1.000 40.14415  ? 89  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 82  ? -6.04645  22.90091 33.43555 1.000 37.01944  ? 89  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 82  ? -4.18758  23.94692 34.74495 1.000 39.11458  ? 89  LEU   A CD2 1 
ATOM   600  N N   . THR   A 1 83  ? -4.91390  22.04424 30.10157 1.000 32.27220  ? 90  THR   A N   1 
ATOM   601  C CA  . THR   A 1 83  ? -4.86458  22.68877 28.79806 1.000 35.17684  ? 90  THR   A CA  1 
ATOM   602  C C   . THR   A 1 83  ? -5.57737  24.03216 28.86527 1.000 39.34284  ? 90  THR   A C   1 
ATOM   603  O O   . THR   A 1 83  ? -6.69333  24.12300 29.38763 1.000 37.66884  ? 90  THR   A O   1 
ATOM   604  C CB  . THR   A 1 83  ? -5.50201  21.79638 27.73039 1.000 38.87864  ? 90  THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 83  ? -4.72331  20.60326 27.57927 1.000 42.36622  ? 90  THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 83  ? -5.56056  22.51474 26.40087 1.000 36.50115  ? 90  THR   A CG2 1 
ATOM   607  N N   . ILE   A 1 84  ? -4.92706  25.06962 28.34543 1.000 33.08686  ? 91  ILE   A N   1 
ATOM   608  C CA  . ILE   A 1 84  ? -5.48610  26.41541 28.28263 1.000 36.42072  ? 91  ILE   A CA  1 
ATOM   609  C C   . ILE   A 1 84  ? -5.58935  26.79404 26.81247 1.000 38.45460  ? 91  ILE   A C   1 
ATOM   610  O O   . ILE   A 1 84  ? -4.56774  26.94450 26.12947 1.000 35.67323  ? 91  ILE   A O   1 
ATOM   611  C CB  . ILE   A 1 84  ? -4.63638  27.42831 29.06011 1.000 37.78315  ? 91  ILE   A CB  1 
ATOM   612  C CG1 . ILE   A 1 84  ? -4.47787  26.96853 30.51024 1.000 42.03212  ? 91  ILE   A CG1 1 
ATOM   613  C CG2 . ILE   A 1 84  ? -5.26152  28.81564 28.99513 1.000 37.74822  ? 91  ILE   A CG2 1 
ATOM   614  C CD1 . ILE   A 1 84  ? -3.05932  26.99775 31.00884 1.000 47.50708  ? 91  ILE   A CD1 1 
ATOM   615  N N   . VAL   A 1 85  ? -6.81777  26.94590 26.32381 1.000 34.14919  ? 92  VAL   A N   1 
ATOM   616  C CA  . VAL   A 1 85  ? -7.08993  27.23533 24.92071 1.000 35.85445  ? 92  VAL   A CA  1 
ATOM   617  C C   . VAL   A 1 85  ? -7.63636  28.65011 24.81271 1.000 36.30204  ? 92  VAL   A C   1 
ATOM   618  O O   . VAL   A 1 85  ? -8.54196  29.03161 25.56308 1.000 36.28904  ? 92  VAL   A O   1 
ATOM   619  C CB  . VAL   A 1 85  ? -8.08496  26.22840 24.31757 1.000 35.79020  ? 92  VAL   A CB  1 
ATOM   620  C CG1 . VAL   A 1 85  ? -8.29730  26.51180 22.83622 1.000 34.49933  ? 92  VAL   A CG1 1 
ATOM   621  C CG2 . VAL   A 1 85  ? -7.60577  24.80605 24.53264 1.000 36.53630  ? 92  VAL   A CG2 1 
ATOM   622  N N   . ASP   A 1 86  ? -7.09071  29.42388 23.87981 1.000 33.33843  ? 93  ASP   A N   1 
ATOM   623  C CA  . ASP   A 1 86  ? -7.64366  30.72022 23.52436 1.000 33.18042  ? 93  ASP   A CA  1 
ATOM   624  C C   . ASP   A 1 86  ? -7.76236  30.80957 22.01094 1.000 35.13887  ? 93  ASP   A C   1 
ATOM   625  O O   . ASP   A 1 86  ? -7.04249  30.13043 21.27329 1.000 34.79419  ? 93  ASP   A O   1 
ATOM   626  C CB  . ASP   A 1 86  ? -6.79120  31.88578 24.07195 1.000 32.65966  ? 93  ASP   A CB  1 
ATOM   627  C CG  . ASP   A 1 86  ? -5.42998  31.99806 23.39917 1.000 36.29002  ? 93  ASP   A CG  1 
ATOM   628  O OD1 . ASP   A 1 86  ? -5.36811  32.40359 22.21858 1.000 37.44623  ? 93  ASP   A OD1 1 
ATOM   629  O OD2 . ASP   A 1 86  ? -4.41588  31.69131 24.06197 1.000 33.95313  ? 93  ASP   A OD2 1 
ATOM   630  N N   . THR   A 1 87  ? -8.68851  31.64886 21.55547 1.000 33.90628  ? 94  THR   A N   1 
ATOM   631  C CA  . THR   A 1 87  ? -8.87828  31.91738 20.13256 1.000 36.24416  ? 94  THR   A CA  1 
ATOM   632  C C   . THR   A 1 87  ? -8.25927  33.24952 19.72999 1.000 34.87457  ? 94  THR   A C   1 
ATOM   633  O O   . THR   A 1 87  ? -8.82928  33.99310 18.92707 1.000 35.17087  ? 94  THR   A O   1 
ATOM   634  C CB  . THR   A 1 87  ? -10.36165 31.88129 19.78176 1.000 39.22273  ? 94  THR   A CB  1 
ATOM   635  O OG1 . THR   A 1 87  ? -11.08200 32.73373 20.67888 1.000 38.03885  ? 94  THR   A OG1 1 
ATOM   636  C CG2 . THR   A 1 87  ? -10.89667 30.46263 19.89910 1.000 36.66347  ? 94  THR   A CG2 1 
ATOM   637  N N   . GLY   A 1 88  ? -7.08804  33.56748 20.28083 1.000 34.95376  ? 95  GLY   A N   1 
ATOM   638  C CA  . GLY   A 1 88  ? -6.40828  34.81445 20.00442 1.000 35.32383  ? 95  GLY   A CA  1 
ATOM   639  C C   . GLY   A 1 88  ? -5.76082  34.82425 18.64214 1.000 35.30730  ? 95  GLY   A C   1 
ATOM   640  O O   . GLY   A 1 88  ? -6.09413  34.03473 17.75403 1.000 37.41389  ? 95  GLY   A O   1 
ATOM   641  N N   . ILE   A 1 89  ? -4.80141  35.73842 18.48191 1.000 31.61080  ? 96  ILE   A N   1 
ATOM   642  C CA  . ILE   A 1 89  ? -4.15538  35.92527 17.19094 1.000 34.77773  ? 96  ILE   A CA  1 
ATOM   643  C C   . ILE   A 1 89  ? -3.29719  34.73007 16.79509 1.000 35.00571  ? 96  ILE   A C   1 
ATOM   644  O O   . ILE   A 1 89  ? -3.07240  34.50321 15.59892 1.000 36.22351  ? 96  ILE   A O   1 
ATOM   645  C CB  . ILE   A 1 89  ? -3.31593  37.21655 17.20118 1.000 37.19850  ? 96  ILE   A CB  1 
ATOM   646  C CG1 . ILE   A 1 89  ? -2.83072  37.55384 15.78674 1.000 42.65894  ? 96  ILE   A CG1 1 
ATOM   647  C CG2 . ILE   A 1 89  ? -2.14432  37.09214 18.17076 1.000 36.20010  ? 96  ILE   A CG2 1 
ATOM   648  C CD1 . ILE   A 1 89  ? -2.57288  39.02115 15.56186 1.000 45.53967  ? 96  ILE   A CD1 1 
ATOM   649  N N   . GLY   A 1 90  ? -2.82162  33.94655 17.76105 1.000 32.37279  ? 97  GLY   A N   1 
ATOM   650  C CA  . GLY   A 1 90  ? -1.95062  32.83550 17.44714 1.000 34.04247  ? 97  GLY   A CA  1 
ATOM   651  C C   . GLY   A 1 90  ? -0.51438  33.28176 17.25083 1.000 36.26431  ? 97  GLY   A C   1 
ATOM   652  O O   . GLY   A 1 90  ? -0.15166  34.44487 17.44583 1.000 32.91436  ? 97  GLY   A O   1 
ATOM   653  N N   . MET   A 1 91  ? 0.31574   32.32613 16.84172 1.000 31.79341  ? 98  MET   A N   1 
ATOM   654  C CA  . MET   A 1 91  ? 1.74793   32.55557 16.72677 1.000 36.16183  ? 98  MET   A CA  1 
ATOM   655  C C   . MET   A 1 91  ? 2.25512   31.94884 15.42854 1.000 36.46585  ? 98  MET   A C   1 
ATOM   656  O O   . MET   A 1 91  ? 1.91533   30.80900 15.09804 1.000 36.70726  ? 98  MET   A O   1 
ATOM   657  C CB  . MET   A 1 91  ? 2.48573   31.95585 17.92860 1.000 38.10820  ? 98  MET   A CB  1 
ATOM   658  C CG  . MET   A 1 91  ? 2.37777   32.79910 19.19204 1.000 39.08416  ? 98  MET   A CG  1 
ATOM   659  S SD  . MET   A 1 91  ? 3.29792   32.11231 20.57983 1.000 35.86390  ? 98  MET   A SD  1 
ATOM   660  C CE  . MET   A 1 91  ? 2.10768   30.93220 21.20339 1.000 38.10295  ? 98  MET   A CE  1 
ATOM   661  N N   . THR   A 1 92  ? 3.05718   32.71499 14.69484 1.000 37.61770  ? 99  THR   A N   1 
ATOM   662  C CA  . THR   A 1 92  ? 3.67082   32.22706 13.47145 1.000 38.16388  ? 99  THR   A CA  1 
ATOM   663  C C   . THR   A 1 92  ? 4.88006   31.35265 13.79714 1.000 41.27042  ? 99  THR   A C   1 
ATOM   664  O O   . THR   A 1 92  ? 5.28565   31.20844 14.95373 1.000 33.55697  ? 99  THR   A O   1 
ATOM   665  C CB  . THR   A 1 92  ? 4.09511   33.39284 12.57957 1.000 39.07287  ? 99  THR   A CB  1 
ATOM   666  O OG1 . THR   A 1 92  ? 5.10498   34.16131 13.24697 1.000 40.89430  ? 99  THR   A OG1 1 
ATOM   667  C CG2 . THR   A 1 92  ? 2.90778   34.28896 12.27007 1.000 39.43886  ? 99  THR   A CG2 1 
ATOM   668  N N   . LYS   A 1 93  ? 5.46542   30.76265 12.75153 1.000 40.73366  ? 100 LYS   A N   1 
ATOM   669  C CA  . LYS   A 1 93  ? 6.68305   29.98224 12.94649 1.000 42.29605  ? 100 LYS   A CA  1 
ATOM   670  C C   . LYS   A 1 93  ? 7.83143   30.87025 13.40844 1.000 40.28031  ? 100 LYS   A C   1 
ATOM   671  O O   . LYS   A 1 93  ? 8.63596   30.46816 14.25744 1.000 43.11849  ? 100 LYS   A O   1 
ATOM   672  C CB  . LYS   A 1 93  ? 7.05769   29.24666 11.65962 1.000 44.34020  ? 100 LYS   A CB  1 
ATOM   673  C CG  . LYS   A 1 93  ? 8.21375   28.27498 11.83349 1.000 45.99192  ? 100 LYS   A CG  1 
ATOM   674  C CD  . LYS   A 1 93  ? 8.53322   27.53078 10.54909 1.000 48.77754  ? 100 LYS   A CD  1 
ATOM   675  C CE  . LYS   A 1 93  ? 9.49823   26.38598 10.81388 1.000 55.43819  ? 100 LYS   A CE  1 
ATOM   676  N NZ  . LYS   A 1 93  ? 10.13444  25.89029 9.56327  1.000 54.74879  ? 100 LYS   A NZ  1 
ATOM   677  N N   . ALA   A 1 94  ? 7.92038   32.08638 12.86402 1.000 41.49024  ? 101 ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 94  ? 8.95501   33.01651 13.30094 1.000 44.05836  ? 101 ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 94  ? 8.74767   33.44512 14.74757 1.000 44.30214  ? 101 ALA   A C   1 
ATOM   680  O O   . ALA   A 1 94  ? 9.72177   33.73257 15.45272 1.000 45.03972  ? 101 ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 94  ? 8.98675   34.23659 12.38140 1.000 42.95160  ? 101 ALA   A CB  1 
ATOM   682  N N   . ASP   A 1 95  ? 7.49322   33.49710 15.20385 1.000 38.37835  ? 102 ASP   A N   1 
ATOM   683  C CA  . ASP   A 1 95  ? 7.22543   33.81329 16.60317 1.000 39.29167  ? 102 ASP   A CA  1 
ATOM   684  C C   . ASP   A 1 95  ? 7.79113   32.74301 17.52674 1.000 43.44363  ? 102 ASP   A C   1 
ATOM   685  O O   . ASP   A 1 95  ? 8.41211   33.05695 18.54895 1.000 42.50627  ? 102 ASP   A O   1 
ATOM   686  C CB  . ASP   A 1 95  ? 5.72012   33.95871 16.83280 1.000 37.73303  ? 102 ASP   A CB  1 
ATOM   687  C CG  . ASP   A 1 95  ? 5.16567   35.25921 16.29044 1.000 39.89719  ? 102 ASP   A CG  1 
ATOM   688  O OD1 . ASP   A 1 95  ? 5.92343   36.24785 16.21712 1.000 35.68311  ? 102 ASP   A OD1 1 
ATOM   689  O OD2 . ASP   A 1 95  ? 3.96709   35.29359 15.94068 1.000 39.63529  ? 102 ASP   A OD2 1 
ATOM   690  N N   . LEU   A 1 96  ? 7.59296   31.47098 17.17529 1.000 40.17044  ? 103 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 96  ? 7.95513   30.38114 18.07424 1.000 41.98787  ? 103 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 96  ? 9.46603   30.22146 18.18692 1.000 43.81117  ? 103 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 96  ? 9.97816   29.87111 19.25604 1.000 48.27942  ? 103 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 96  ? 7.31902   29.07839 17.59184 1.000 38.92889  ? 103 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 96  ? 5.79315   29.05073 17.48655 1.000 38.40491  ? 103 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 96  ? 5.34641   27.82504 16.71268 1.000 39.05458  ? 103 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 96  ? 5.15092   29.07951 18.86080 1.000 36.22061  ? 103 LEU   A CD2 1 
ATOM   698  N N   . ILE   A 1 97  ? 10.19530  30.47214 17.10331 1.000 41.98852  ? 104 ILE   A N   1 
ATOM   699  C CA  . ILE   A 1 97  ? 11.62360  30.17067 17.07775 1.000 47.96844  ? 104 ILE   A CA  1 
ATOM   700  C C   . ILE   A 1 97  ? 12.46916  31.38013 17.45779 1.000 50.95740  ? 104 ILE   A C   1 
ATOM   701  O O   . ILE   A 1 97  ? 13.44460  31.24840 18.20042 1.000 52.57641  ? 104 ILE   A O   1 
ATOM   702  C CB  . ILE   A 1 97  ? 12.02257  29.62297 15.69212 1.000 50.56677  ? 104 ILE   A CB  1 
ATOM   703  C CG1 . ILE   A 1 97  ? 11.16040  28.41546 15.31618 1.000 46.76694  ? 104 ILE   A CG1 1 
ATOM   704  C CG2 . ILE   A 1 97  ? 13.49717  29.25393 15.66388 1.000 53.67645  ? 104 ILE   A CG2 1 
ATOM   705  C CD1 . ILE   A 1 97  ? 11.16774  28.10801 13.83617 1.000 46.84228  ? 104 ILE   A CD1 1 
ATOM   706  N N   . ASN   A 1 98  ? 12.11902  32.57207 16.97430 1.000 50.20781  ? 105 ASN   A N   1 
ATOM   707  C CA  . ASN   A 1 98  ? 13.02163  33.71736 17.04869 1.000 54.32430  ? 105 ASN   A CA  1 
ATOM   708  C C   . ASN   A 1 98  ? 12.40922  34.92622 17.74173 1.000 51.99133  ? 105 ASN   A C   1 
ATOM   709  O O   . ASN   A 1 98  ? 12.90754  35.34596 18.79140 1.000 53.25530  ? 105 ASN   A O   1 
ATOM   710  C CB  . ASN   A 1 98  ? 13.48001  34.10029 15.63508 1.000 55.95861  ? 105 ASN   A CB  1 
ATOM   711  C CG  . ASN   A 1 98  ? 14.86152  33.57867 15.30903 1.000 69.76701  ? 105 ASN   A CG  1 
ATOM   712  O OD1 . ASN   A 1 98  ? 15.05320  32.86973 14.32107 1.000 82.60613  ? 105 ASN   A OD1 1 
ATOM   713  N ND2 . ASN   A 1 98  ? 15.83900  33.94084 16.13233 1.000 67.38905  ? 105 ASN   A ND2 1 
ATOM   714  N N   . ASN   A 1 99  ? 11.34028  35.49939 17.18664 1.000 52.29590  ? 106 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 99  ? 10.98394  36.87808 17.50939 1.000 52.17680  ? 106 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 99  ? 10.47571  37.02531 18.93898 1.000 53.14925  ? 106 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 99  ? 10.79659  38.01050 19.61347 1.000 61.35282  ? 106 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 99  ? 9.95342   37.38922 16.50558 1.000 49.98851  ? 106 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 99  ? 10.44440  37.28792 15.07432 1.000 54.10026  ? 106 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 99  ? 11.64399  37.38147 14.81093 1.000 56.50206  ? 106 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 99  ? 9.52036   37.09333 14.14225 1.000 56.31912  ? 106 ASN   A ND2 1 
ATOM   722  N N   . LEU   A 1 100 ? 9.68356   36.06791 19.42326 1.000 49.58610  ? 107 LEU   A N   1 
ATOM   723  C CA  . LEU   A 1 100 ? 9.15530   36.19215 20.77835 1.000 51.67306  ? 107 LEU   A CA  1 
ATOM   724  C C   . LEU   A 1 100 ? 10.24561  35.97497 21.82036 1.000 52.82675  ? 107 LEU   A C   1 
ATOM   725  O O   . LEU   A 1 100 ? 10.23976  36.61956 22.87594 1.000 53.17813  ? 107 LEU   A O   1 
ATOM   726  C CB  . LEU   A 1 100 ? 7.99921   35.21707 20.98455 1.000 50.81330  ? 107 LEU   A CB  1 
ATOM   727  C CG  . LEU   A 1 100 ? 6.70637   35.64210 20.28696 1.000 46.54274  ? 107 LEU   A CG  1 
ATOM   728  C CD1 . LEU   A 1 100 ? 5.56462   34.72507 20.67493 1.000 49.17210  ? 107 LEU   A CD1 1 
ATOM   729  C CD2 . LEU   A 1 100 ? 6.37330   37.09228 20.61306 1.000 44.38212  ? 107 LEU   A CD2 1 
ATOM   730  N N   . GLY   A 1 101 ? 11.18922  35.07283 21.54439 1.000 52.08724  ? 108 GLY   A N   1 
ATOM   731  C CA  . GLY   A 1 101 ? 12.32798  34.91713 22.43132 1.000 53.77310  ? 108 GLY   A CA  1 
ATOM   732  C C   . GLY   A 1 101 ? 13.25639  36.11363 22.40939 1.000 57.68932  ? 108 GLY   A C   1 
ATOM   733  O O   . GLY   A 1 101 ? 13.88016  36.43844 23.42437 1.000 60.72425  ? 108 GLY   A O   1 
ATOM   734  N N   . THR   A 1 102 ? 13.36293  36.78388 21.25901 1.000 57.23596  ? 109 THR   A N   1 
ATOM   735  C CA  . THR   A 1 102 ? 14.16855  37.99789 21.17768 1.000 58.32912  ? 109 THR   A CA  1 
ATOM   736  C C   . THR   A 1 102 ? 13.56289  39.11412 22.01983 1.000 59.88064  ? 109 THR   A C   1 
ATOM   737  O O   . THR   A 1 102 ? 14.28539  39.84040 22.71299 1.000 65.19912  ? 109 THR   A O   1 
ATOM   738  C CB  . THR   A 1 102 ? 14.30702  38.43738 19.71928 1.000 57.68087  ? 109 THR   A CB  1 
ATOM   739  O OG1 . THR   A 1 102 ? 15.00052  37.42595 18.97800 1.000 59.65453  ? 109 THR   A OG1 1 
ATOM   740  C CG2 . THR   A 1 102 ? 15.07784  39.74645 19.62184 1.000 56.99807  ? 109 THR   A CG2 1 
ATOM   741  N N   . ILE   A 1 103 ? 12.23639  39.26243 21.97446 1.000 56.21060  ? 110 ILE   A N   1 
ATOM   742  C CA  . ILE   A 1 103 ? 11.56102  40.23663 22.82639 1.000 59.38544  ? 110 ILE   A CA  1 
ATOM   743  C C   . ILE   A 1 103 ? 11.73646  39.87503 24.29510 1.000 60.73712  ? 110 ILE   A C   1 
ATOM   744  O O   . ILE   A 1 103 ? 11.81904  40.75848 25.15826 1.000 65.03823  ? 110 ILE   A O   1 
ATOM   745  C CB  . ILE   A 1 103 ? 10.07050  40.33351 22.43688 1.000 58.37297  ? 110 ILE   A CB  1 
ATOM   746  C CG1 . ILE   A 1 103 ? 9.92371   40.84256 21.00110 1.000 55.37594  ? 110 ILE   A CG1 1 
ATOM   747  C CG2 . ILE   A 1 103 ? 9.31015   41.23898 23.39602 1.000 54.31634  ? 110 ILE   A CG2 1 
ATOM   748  C CD1 . ILE   A 1 103 ? 10.37709  42.27339 20.81034 1.000 54.97020  ? 110 ILE   A CD1 1 
ATOM   749  N N   . ALA   A 1 104 ? 11.82628  38.58086 24.60154 1.000 57.88343  ? 111 ALA   A N   1 
ATOM   750  C CA  . ALA   A 1 104 ? 11.88486  38.12163 25.98177 1.000 59.39996  ? 111 ALA   A CA  1 
ATOM   751  C C   . ALA   A 1 104 ? 13.27757  38.19841 26.59434 1.000 59.09554  ? 111 ALA   A C   1 
ATOM   752  O O   . ALA   A 1 104 ? 13.39249  38.06137 27.81661 1.000 58.50466  ? 111 ALA   A O   1 
ATOM   753  C CB  . ALA   A 1 104 ? 11.37022  36.68352 26.07848 1.000 51.87323  ? 111 ALA   A CB  1 
ATOM   754  N N   . LYS   A 1 105 ? 14.33012  38.40890 25.79542 1.000 61.27828  ? 112 LYS   A N   1 
ATOM   755  C CA  . LYS   A 1 105 ? 15.68133  38.42130 26.35361 1.000 61.89832  ? 112 LYS   A CA  1 
ATOM   756  C C   . LYS   A 1 105 ? 15.83850  39.52886 27.38631 1.000 61.63119  ? 112 LYS   A C   1 
ATOM   757  O O   . LYS   A 1 105 ? 16.34666  39.29671 28.48953 1.000 61.78449  ? 112 LYS   A O   1 
ATOM   758  C CB  . LYS   A 1 105 ? 16.73254  38.58533 25.25362 1.000 65.37789  ? 112 LYS   A CB  1 
ATOM   759  C CG  . LYS   A 1 105 ? 18.15164  38.67993 25.82439 1.000 71.02305  ? 112 LYS   A CG  1 
ATOM   760  C CD  . LYS   A 1 105 ? 19.21524  38.93041 24.76722 1.000 74.59190  ? 112 LYS   A CD  1 
ATOM   761  C CE  . LYS   A 1 105 ? 19.17052  37.90874 23.64867 1.000 77.76594  ? 112 LYS   A CE  1 
ATOM   762  N NZ  . LYS   A 1 105 ? 20.43757  37.12440 23.57697 1.000 79.08870  ? 112 LYS   A NZ  1 
ATOM   763  N N   . SER   A 1 106 ? 15.41391  40.74789 27.04054 1.000 64.03608  ? 113 SER   A N   1 
ATOM   764  C CA  . SER   A 1 106 ? 15.58287  41.87042 27.95728 1.000 63.99239  ? 113 SER   A CA  1 
ATOM   765  C C   . SER   A 1 106 ? 14.73278  41.68794 29.20524 1.000 62.45810  ? 113 SER   A C   1 
ATOM   766  O O   . SER   A 1 106 ? 15.19941  41.93906 30.32228 1.000 58.79812  ? 113 SER   A O   1 
ATOM   767  C CB  . SER   A 1 106 ? 15.23158  43.18790 27.26456 1.000 65.55852  ? 113 SER   A CB  1 
ATOM   768  O OG  . SER   A 1 106 ? 14.16527  43.02325 26.34606 1.000 69.99007  ? 113 SER   A OG  1 
ATOM   769  N N   . GLY   A 1 107 ? 13.48448  41.24877 29.03446 1.000 60.18672  ? 114 GLY   A N   1 
ATOM   770  C CA  . GLY   A 1 107 ? 12.63475  41.00403 30.18705 1.000 59.14317  ? 114 GLY   A CA  1 
ATOM   771  C C   . GLY   A 1 107 ? 13.16232  39.88840 31.06697 1.000 56.54191  ? 114 GLY   A C   1 
ATOM   772  O O   . GLY   A 1 107 ? 13.07513  39.96112 32.29582 1.000 56.65611  ? 114 GLY   A O   1 
ATOM   773  N N   . THR   A 1 108 ? 13.72067  38.84340 30.45203 1.000 55.59706  ? 115 THR   A N   1 
ATOM   774  C CA  . THR   A 1 108 ? 14.33406  37.76605 31.22143 1.000 54.57191  ? 115 THR   A CA  1 
ATOM   775  C C   . THR   A 1 108 ? 15.53392  38.27366 32.00983 1.000 56.40965  ? 115 THR   A C   1 
ATOM   776  O O   . THR   A 1 108 ? 15.66928  37.99247 33.20543 1.000 55.87713  ? 115 THR   A O   1 
ATOM   777  C CB  . THR   A 1 108 ? 14.75079  36.62645 30.29087 1.000 52.86226  ? 115 THR   A CB  1 
ATOM   778  O OG1 . THR   A 1 108 ? 13.60316  36.13677 29.58526 1.000 55.00704  ? 115 THR   A OG1 1 
ATOM   779  C CG2 . THR   A 1 108 ? 15.37993  35.49623 31.08252 1.000 51.95801  ? 115 THR   A CG2 1 
ATOM   780  N N   . LYS   A 1 109 ? 16.41769  39.02623 31.34944 1.000 58.93116  ? 116 LYS   A N   1 
ATOM   781  C CA  . LYS   A 1 109 ? 17.59983  39.56445 32.01582 1.000 61.84660  ? 116 LYS   A CA  1 
ATOM   782  C C   . LYS   A 1 109 ? 17.21662  40.40884 33.22480 1.000 63.10460  ? 116 LYS   A C   1 
ATOM   783  O O   . LYS   A 1 109 ? 17.77886  40.24999 34.31476 1.000 66.26972  ? 116 LYS   A O   1 
ATOM   784  C CB  . LYS   A 1 109 ? 18.42188  40.38812 31.02288 1.000 64.96453  ? 116 LYS   A CB  1 
ATOM   785  C CG  . LYS   A 1 109 ? 19.71222  39.72692 30.57226 1.000 69.70687  ? 116 LYS   A CG  1 
ATOM   786  C CD  . LYS   A 1 109 ? 20.89990  40.25705 31.36022 1.000 78.71076  ? 116 LYS   A CD  1 
ATOM   787  C CE  . LYS   A 1 109 ? 22.16706  39.47715 31.05273 1.000 83.86563  ? 116 LYS   A CE  1 
ATOM   788  N NZ  . LYS   A 1 109 ? 23.06731  39.39077 32.23609 1.000 80.00042  ? 116 LYS   A NZ  1 
ATOM   789  N N   . ALA   A 1 110 ? 16.24755  41.31013 33.04867 1.000 61.40183  ? 117 ALA   A N   1 
ATOM   790  C CA  . ALA   A 1 110 ? 15.83172  42.17219 34.14833 1.000 59.77900  ? 117 ALA   A CA  1 
ATOM   791  C C   . ALA   A 1 110 ? 15.15281  41.38369 35.26047 1.000 60.66788  ? 117 ALA   A C   1 
ATOM   792  O O   . ALA   A 1 110 ? 15.28954  41.73686 36.43725 1.000 61.55204  ? 117 ALA   A O   1 
ATOM   793  C CB  . ALA   A 1 110 ? 14.90300  43.27166 33.63148 1.000 61.02756  ? 117 ALA   A CB  1 
ATOM   794  N N   . PHE   A 1 111 ? 14.42104  40.32176 34.91377 1.000 56.61634  ? 118 PHE   A N   1 
ATOM   795  C CA  . PHE   A 1 111 ? 13.72723  39.54087 35.93257 1.000 58.26761  ? 118 PHE   A CA  1 
ATOM   796  C C   . PHE   A 1 111 ? 14.71128  38.84739 36.86682 1.000 60.24926  ? 118 PHE   A C   1 
ATOM   797  O O   . PHE   A 1 111 ? 14.48680  38.79499 38.08133 1.000 60.61451  ? 118 PHE   A O   1 
ATOM   798  C CB  . PHE   A 1 111 ? 12.80035  38.52122 35.27084 1.000 52.65087  ? 118 PHE   A CB  1 
ATOM   799  C CG  . PHE   A 1 111 ? 11.99428  37.71121 36.24724 1.000 52.47311  ? 118 PHE   A CG  1 
ATOM   800  C CD1 . PHE   A 1 111 ? 11.37533  38.31675 37.32790 1.000 53.70172  ? 118 PHE   A CD1 1 
ATOM   801  C CD2 . PHE   A 1 111 ? 11.85878  36.34268 36.08600 1.000 48.00295  ? 118 PHE   A CD2 1 
ATOM   802  C CE1 . PHE   A 1 111 ? 10.63502  37.57264 38.22942 1.000 55.70451  ? 118 PHE   A CE1 1 
ATOM   803  C CE2 . PHE   A 1 111 ? 11.12055  35.59255 36.98283 1.000 49.39103  ? 118 PHE   A CE2 1 
ATOM   804  C CZ  . PHE   A 1 111 ? 10.50785  36.20835 38.05667 1.000 54.00552  ? 118 PHE   A CZ  1 
ATOM   805  N N   . MET   A 1 112 ? 15.80793  38.31512 36.31892 1.000 61.03566  ? 119 MET   A N   1 
ATOM   806  C CA  . MET   A 1 112 ? 16.80063  37.61193 37.12600 1.000 65.14636  ? 119 MET   A CA  1 
ATOM   807  C C   . MET   A 1 112 ? 17.63361  38.57417 37.96225 1.000 64.53643  ? 119 MET   A C   1 
ATOM   808  O O   . MET   A 1 112 ? 18.03941  38.23269 39.07861 1.000 71.05135  ? 119 MET   A O   1 
ATOM   809  C CB  . MET   A 1 112 ? 17.69543  36.75912 36.22448 1.000 63.04855  ? 119 MET   A CB  1 
ATOM   810  C CG  . MET   A 1 112 ? 16.91458  35.97269 35.17882 1.000 63.06529  ? 119 MET   A CG  1 
ATOM   811  S SD  . MET   A 1 112 ? 17.52259  34.31394 34.83143 1.000 79.44438  ? 119 MET   A SD  1 
ATOM   812  C CE  . MET   A 1 112 ? 18.69691  34.66767 33.53146 1.000 61.38695  ? 119 MET   A CE  1 
ATOM   813  N N   . GLU   A 1 113 ? 17.90484  39.77319 37.43990 1.000 68.64564  ? 120 GLU   A N   1 
ATOM   814  C CA  . GLU   A 1 113 ? 18.53154  40.80417 38.25975 1.000 75.04709  ? 120 GLU   A CA  1 
ATOM   815  C C   . GLU   A 1 113 ? 17.63472  41.17759 39.43081 1.000 74.63013  ? 120 GLU   A C   1 
ATOM   816  O O   . GLU   A 1 113 ? 18.11732  41.41594 40.54409 1.000 80.90422  ? 120 GLU   A O   1 
ATOM   817  C CB  . GLU   A 1 113 ? 18.84506  42.03865 37.41300 1.000 78.98839  ? 120 GLU   A CB  1 
ATOM   818  C CG  . GLU   A 1 113 ? 19.82329  41.80706 36.27315 1.000 82.57786  ? 120 GLU   A CG  1 
ATOM   819  C CD  . GLU   A 1 113 ? 20.09512  43.07442 35.48138 1.000 98.66581  ? 120 GLU   A CD  1 
ATOM   820  O OE1 . GLU   A 1 113 ? 20.66075  44.02801 36.05708 1.000 111.21147 ? 120 GLU   A OE1 1 
ATOM   821  O OE2 . GLU   A 1 113 ? 19.74038  43.11820 34.28443 1.000 94.72404  ? 120 GLU   A OE2 1 
ATOM   822  N N   . ALA   A 1 114 ? 16.32217  41.23026 39.19536 1.000 69.95749  ? 121 ALA   A N   1 
ATOM   823  C CA  . ALA   A 1 114 ? 15.38128  41.51321 40.27222 1.000 71.18629  ? 121 ALA   A CA  1 
ATOM   824  C C   . ALA   A 1 114 ? 15.36148  40.38113 41.29104 1.000 72.86745  ? 121 ALA   A C   1 
ATOM   825  O O   . ALA   A 1 114 ? 15.40128  40.62385 42.50280 1.000 76.43487  ? 121 ALA   A O   1 
ATOM   826  C CB  . ALA   A 1 114 ? 13.98545  41.75035 39.69615 1.000 69.83706  ? 121 ALA   A CB  1 
ATOM   827  N N   . LEU   A 1 115 ? 15.30358  39.13280 40.81535 1.000 69.75798  ? 122 LEU   A N   1 
ATOM   828  C CA  . LEU   A 1 115 ? 15.31103  37.99016 41.72371 1.000 72.61695  ? 122 LEU   A CA  1 
ATOM   829  C C   . LEU   A 1 115 ? 16.56662  37.96701 42.58417 1.000 77.21077  ? 122 LEU   A C   1 
ATOM   830  O O   . LEU   A 1 115 ? 16.52283  37.51330 43.73331 1.000 80.93695  ? 122 LEU   A O   1 
ATOM   831  C CB  . LEU   A 1 115 ? 15.18303  36.68789 40.93284 1.000 66.28738  ? 122 LEU   A CB  1 
ATOM   832  C CG  . LEU   A 1 115 ? 13.85354  36.45767 40.21152 1.000 63.38756  ? 122 LEU   A CG  1 
ATOM   833  C CD1 . LEU   A 1 115 ? 13.81120  35.06917 39.59796 1.000 61.39089  ? 122 LEU   A CD1 1 
ATOM   834  C CD2 . LEU   A 1 115 ? 12.68390  36.66119 41.16142 1.000 66.11932  ? 122 LEU   A CD2 1 
ATOM   835  N N   . GLN   A 1 116 ? 17.69090  38.45032 42.05052 1.000 78.21994  ? 123 GLN   A N   1 
ATOM   836  C CA  . GLN   A 1 116 ? 18.89330  38.58376 42.86443 1.000 86.64128  ? 123 GLN   A CA  1 
ATOM   837  C C   . GLN   A 1 116 ? 18.75886  39.71639 43.87334 1.000 88.04285  ? 123 GLN   A C   1 
ATOM   838  O O   . GLN   A 1 116 ? 19.38074  39.67193 44.94111 1.000 92.62771  ? 123 GLN   A O   1 
ATOM   839  C CB  . GLN   A 1 116 ? 20.11143  38.81040 41.96985 1.000 90.29801  ? 123 GLN   A CB  1 
ATOM   840  C CG  . GLN   A 1 116 ? 20.56169  37.57406 41.21090 1.000 87.25324  ? 123 GLN   A CG  1 
ATOM   841  C CD  . GLN   A 1 116 ? 21.95186  37.12270 41.61076 1.000 102.42324 ? 123 GLN   A CD  1 
ATOM   842  O OE1 . GLN   A 1 116 ? 22.17435  36.68588 42.73993 1.000 104.30503 ? 123 GLN   A OE1 1 
ATOM   843  N NE2 . GLN   A 1 116 ? 22.89737  37.22710 40.68410 1.000 107.56808 ? 123 GLN   A NE2 1 
ATOM   844  N N   . ALA   A 1 117 ? 17.95456  40.73175 43.55737 1.000 87.24411  ? 124 ALA   A N   1 
ATOM   845  C CA  . ALA   A 1 117 ? 17.70854  41.85278 44.45208 1.000 90.36385  ? 124 ALA   A CA  1 
ATOM   846  C C   . ALA   A 1 117 ? 16.56257  41.58780 45.42271 1.000 94.04845  ? 124 ALA   A C   1 
ATOM   847  O O   . ALA   A 1 117 ? 15.99258  42.53846 45.97021 1.000 96.85868  ? 124 ALA   A O   1 
ATOM   848  C CB  . ALA   A 1 117 ? 17.42939  43.12144 43.64320 1.000 87.99210  ? 124 ALA   A CB  1 
ATOM   849  N N   . GLY   A 1 118 ? 16.21020  40.32438 45.64149 1.000 95.89851  ? 125 GLY   A N   1 
ATOM   850  C CA  . GLY   A 1 118 ? 15.17287  39.97189 46.58642 1.000 93.33089  ? 125 GLY   A CA  1 
ATOM   851  C C   . GLY   A 1 118 ? 13.76207  39.96972 46.04476 1.000 86.93981  ? 125 GLY   A C   1 
ATOM   852  O O   . GLY   A 1 118 ? 12.81931  39.81576 46.83048 1.000 87.71618  ? 125 GLY   A O   1 
ATOM   853  N N   . ALA   A 1 119 ? 13.58034  40.13196 44.73686 1.000 83.29507  ? 126 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 119 ? 12.23847  40.14055 44.17683 1.000 81.68211  ? 126 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 119 ? 11.62772  38.74253 44.21852 1.000 80.54442  ? 126 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 119 ? 12.31505  37.73499 44.40801 1.000 82.09696  ? 126 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 119 ? 12.25019  40.66362 42.74101 1.000 77.98776  ? 126 ALA   A CB  1 
ATOM   858  N N   . ASP   A 1 120 ? 10.31318  38.69343 44.03504 1.000 77.24969  ? 127 ASP   A N   1 
ATOM   859  C CA  . ASP   A 1 120 ? 9.55694   37.45408 44.11002 1.000 73.35274  ? 127 ASP   A CA  1 
ATOM   860  C C   . ASP   A 1 120 ? 9.27137   36.91634 42.71301 1.000 68.93431  ? 127 ASP   A C   1 
ATOM   861  O O   . ASP   A 1 120 ? 9.15511   37.67342 41.74565 1.000 69.71279  ? 127 ASP   A O   1 
ATOM   862  C CB  . ASP   A 1 120 ? 8.24424   37.66660 44.86772 1.000 71.84212  ? 127 ASP   A CB  1 
ATOM   863  C CG  . ASP   A 1 120 ? 7.77723   36.41677 45.58682 1.000 79.78315  ? 127 ASP   A CG  1 
ATOM   864  O OD1 . ASP   A 1 120 ? 8.58095   35.82748 46.33937 1.000 95.39787  ? 127 ASP   A OD1 1 
ATOM   865  O OD2 . ASP   A 1 120 ? 6.60614   36.02564 45.40284 1.000 89.17767  ? 127 ASP   A OD2 1 
ATOM   866  N N   . ILE   A 1 121 ? 9.16132   35.58822 42.62090 1.000 66.55570  ? 128 ILE   A N   1 
ATOM   867  C CA  . ILE   A 1 121 ? 8.87337   34.94137 41.34347 1.000 62.85414  ? 128 ILE   A CA  1 
ATOM   868  C C   . ILE   A 1 121 ? 7.50220   35.35803 40.82582 1.000 60.81596  ? 128 ILE   A C   1 
ATOM   869  O O   . ILE   A 1 121 ? 7.27730   35.41651 39.60997 1.000 59.07155  ? 128 ILE   A O   1 
ATOM   870  C CB  . ILE   A 1 121 ? 8.99559   33.40954 41.49699 1.000 61.58349  ? 128 ILE   A CB  1 
ATOM   871  C CG1 . ILE   A 1 121 ? 10.46278  33.00940 41.66876 1.000 63.82351  ? 128 ILE   A CG1 1 
ATOM   872  C CG2 . ILE   A 1 121 ? 8.39400   32.67842 40.30376 1.000 55.55957  ? 128 ILE   A CG2 1 
ATOM   873  C CD1 . ILE   A 1 121 ? 10.68988  31.51281 41.71509 1.000 64.41872  ? 128 ILE   A CD1 1 
ATOM   874  N N   . SER   A 1 122 ? 6.57767   35.68957 41.73127 1.000 61.77109  ? 129 SER   A N   1 
ATOM   875  C CA  . SER   A 1 122 ? 5.22687   36.07100 41.33250 1.000 61.31799  ? 129 SER   A CA  1 
ATOM   876  C C   . SER   A 1 122 ? 5.19690   37.33069 40.47536 1.000 61.10867  ? 129 SER   A C   1 
ATOM   877  O O   . SER   A 1 122 ? 4.17908   37.59923 39.82843 1.000 58.51246  ? 129 SER   A O   1 
ATOM   878  C CB  . SER   A 1 122 ? 4.35417   36.27160 42.57224 1.000 60.48657  ? 129 SER   A CB  1 
ATOM   879  O OG  . SER   A 1 122 ? 4.79899   37.38167 43.33213 1.000 64.21180  ? 129 SER   A OG  1 
ATOM   880  N N   . MET   A 1 123 ? 6.27827   38.10955 40.45531 1.000 61.53351  ? 130 MET   A N   1 
ATOM   881  C CA  . MET   A 1 123 ? 6.35873   39.31165 39.63815 1.000 64.14337  ? 130 MET   A CA  1 
ATOM   882  C C   . MET   A 1 123 ? 6.87098   39.03040 38.23020 1.000 57.92409  ? 130 MET   A C   1 
ATOM   883  O O   . MET   A 1 123 ? 7.29975   39.96164 37.53918 1.000 57.84813  ? 130 MET   A O   1 
ATOM   884  C CB  . MET   A 1 123 ? 7.24647   40.35435 40.32049 1.000 65.97584  ? 130 MET   A CB  1 
ATOM   885  C CG  . MET   A 1 123 ? 6.55901   41.11408 41.44276 1.000 75.10378  ? 130 MET   A CG  1 
ATOM   886  S SD  . MET   A 1 123 ? 7.72551   41.79935 42.63360 1.000 107.05794 ? 130 MET   A SD  1 
ATOM   887  C CE  . MET   A 1 123 ? 9.08417   42.24846 41.55716 1.000 75.92881  ? 130 MET   A CE  1 
ATOM   888  N N   . ILE   A 1 124 ? 6.82909   37.76969 37.79136 1.000 55.40887  ? 131 ILE   A N   1 
ATOM   889  C CA  . ILE   A 1 124 ? 7.35704   37.40990 36.47856 1.000 53.65092  ? 131 ILE   A CA  1 
ATOM   890  C C   . ILE   A 1 124 ? 6.56285   38.08301 35.36614 1.000 53.98952  ? 131 ILE   A C   1 
ATOM   891  O O   . ILE   A 1 124 ? 7.11098   38.39166 34.30031 1.000 45.25502  ? 131 ILE   A O   1 
ATOM   892  C CB  . ILE   A 1 124 ? 7.37469   35.87398 36.32484 1.000 50.04143  ? 131 ILE   A CB  1 
ATOM   893  C CG1 . ILE   A 1 124 ? 7.99994   35.46381 34.98969 1.000 47.56787  ? 131 ILE   A CG1 1 
ATOM   894  C CG2 . ILE   A 1 124 ? 5.97183   35.29837 36.47330 1.000 49.11044  ? 131 ILE   A CG2 1 
ATOM   895  C CD1 . ILE   A 1 124 ? 8.35656   33.99457 34.91025 1.000 43.56430  ? 131 ILE   A CD1 1 
ATOM   896  N N   . GLY   A 1 125 ? 5.27310   38.34188 35.59571 1.000 52.85340  ? 132 GLY   A N   1 
ATOM   897  C CA  . GLY   A 1 125 ? 4.45609   38.96327 34.56782 1.000 53.65092  ? 132 GLY   A CA  1 
ATOM   898  C C   . GLY   A 1 125 ? 4.82572   40.40566 34.29252 1.000 55.32217  ? 132 GLY   A C   1 
ATOM   899  O O   . GLY   A 1 125 ? 4.64344   40.89233 33.17228 1.000 57.24752  ? 132 GLY   A O   1 
ATOM   900  N N   . GLN   A 1 126 ? 5.34919   41.10806 35.30031 1.000 58.05826  ? 133 GLN   A N   1 
ATOM   901  C CA  . GLN   A 1 126 ? 5.76602   42.49161 35.10874 1.000 60.10412  ? 133 GLN   A CA  1 
ATOM   902  C C   . GLN   A 1 126 ? 6.91339   42.61451 34.11688 1.000 58.59275  ? 133 GLN   A C   1 
ATOM   903  O O   . GLN   A 1 126 ? 7.13251   43.70089 33.57030 1.000 59.64403  ? 133 GLN   A O   1 
ATOM   904  C CB  . GLN   A 1 126 ? 6.16757   43.10749 36.44879 1.000 63.56360  ? 133 GLN   A CB  1 
ATOM   905  C CG  . GLN   A 1 126 ? 5.73689   44.55171 36.62238 1.000 87.57575  ? 133 GLN   A CG  1 
ATOM   906  C CD  . GLN   A 1 126 ? 6.15100   45.11455 37.96501 1.000 85.23221  ? 133 GLN   A CD  1 
ATOM   907  O OE1 . GLN   A 1 126 ? 6.75873   46.18232 38.04517 1.000 102.18924 ? 133 GLN   A OE1 1 
ATOM   908  N NE2 . GLN   A 1 126 ? 5.82628   44.39324 39.03158 1.000 86.37750  ? 133 GLN   A NE2 1 
ATOM   909  N N   . PHE   A 1 127 ? 7.64514   41.52999 33.87112 1.000 54.91611  ? 134 PHE   A N   1 
ATOM   910  C CA  . PHE   A 1 127 ? 8.75180   41.52280 32.92663 1.000 52.23944  ? 134 PHE   A CA  1 
ATOM   911  C C   . PHE   A 1 127 ? 8.37606   40.89587 31.58963 1.000 52.66087  ? 134 PHE   A C   1 
ATOM   912  O O   . PHE   A 1 127 ? 9.25583   40.67245 30.75170 1.000 53.37671  ? 134 PHE   A O   1 
ATOM   913  C CB  . PHE   A 1 127 ? 9.95380   40.79568 33.53296 1.000 54.47021  ? 134 PHE   A CB  1 
ATOM   914  C CG  . PHE   A 1 127 ? 10.43483  41.39362 34.82615 1.000 56.23194  ? 134 PHE   A CG  1 
ATOM   915  C CD1 . PHE   A 1 127 ? 9.83065   41.06418 36.02948 1.000 56.11337  ? 134 PHE   A CD1 1 
ATOM   916  C CD2 . PHE   A 1 127 ? 11.48922  42.29081 34.83643 1.000 57.87216  ? 134 PHE   A CD2 1 
ATOM   917  C CE1 . PHE   A 1 127 ? 10.27302  41.61533 37.21827 1.000 60.95390  ? 134 PHE   A CE1 1 
ATOM   918  C CE2 . PHE   A 1 127 ? 11.93589  42.84499 36.02094 1.000 61.53913  ? 134 PHE   A CE2 1 
ATOM   919  C CZ  . PHE   A 1 127 ? 11.32750  42.50691 37.21309 1.000 62.55491  ? 134 PHE   A CZ  1 
ATOM   920  N N   . GLY   A 1 128 ? 7.09534   40.60434 31.37514 1.000 51.38000  ? 135 GLY   A N   1 
ATOM   921  C CA  . GLY   A 1 128 ? 6.64178   40.08993 30.09675 1.000 47.14888  ? 135 GLY   A CA  1 
ATOM   922  C C   . GLY   A 1 128 ? 7.15754   38.71575 29.73473 1.000 48.04991  ? 135 GLY   A C   1 
ATOM   923  O O   . GLY   A 1 128 ? 7.27753   38.40337 28.54700 1.000 51.02480  ? 135 GLY   A O   1 
ATOM   924  N N   . VAL   A 1 129 ? 7.46963   37.88192 30.72520 1.000 44.51678  ? 136 VAL   A N   1 
ATOM   925  C CA  . VAL   A 1 129 ? 7.95382   36.53034 30.46374 1.000 44.08606  ? 136 VAL   A CA  1 
ATOM   926  C C   . VAL   A 1 129 ? 7.16195   35.54022 31.30817 1.000 42.22390  ? 136 VAL   A C   1 
ATOM   927  O O   . VAL   A 1 129 ? 7.68301   34.49635 31.71627 1.000 38.59174  ? 136 VAL   A O   1 
ATOM   928  C CB  . VAL   A 1 129 ? 9.46529   36.41552 30.73753 1.000 44.53124  ? 136 VAL   A CB  1 
ATOM   929  C CG1 . VAL   A 1 129 ? 10.25245  37.19570 29.69466 1.000 46.93733  ? 136 VAL   A CG1 1 
ATOM   930  C CG2 . VAL   A 1 129 ? 9.79307   36.91847 32.13492 1.000 45.61405  ? 136 VAL   A CG2 1 
ATOM   931  N N   . GLY   A 1 130 ? 5.88825   35.85364 31.55612 1.000 40.09392  ? 137 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 130 ? 5.06398   35.04150 32.43434 1.000 41.48449  ? 137 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 130 ? 4.78783   33.63873 31.93290 1.000 37.45758  ? 137 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 130 ? 4.41024   32.77691 32.73335 1.000 40.35278  ? 137 GLY   A O   1 
ATOM   935  N N   . PHE   A 1 131 ? 4.95866   33.38960 30.63013 1.000 35.74432  ? 138 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 131 ? 4.69433   32.05636 30.09339 1.000 38.83916  ? 138 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 131 ? 5.57186   31.00719 30.75904 1.000 37.69694  ? 138 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 131 ? 5.10894   29.90253 31.06497 1.000 36.66082  ? 138 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 131 ? 4.91631   32.03092 28.58009 1.000 39.66589  ? 138 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 131 ? 5.05416   30.64087 28.00926 1.000 39.21916  ? 138 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 131 ? 3.93205   29.91138 27.64957 1.000 38.18467  ? 138 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 131 ? 6.30513   30.05985 27.84436 1.000 40.59016  ? 138 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 131 ? 4.05339   28.63465 27.12882 1.000 36.73414  ? 138 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 131 ? 6.43200   28.78182 27.33136 1.000 37.60503  ? 138 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 131 ? 5.30498   28.06988 26.96959 1.000 37.93245  ? 138 PHE   A CZ  1 
ATOM   946  N N   . TYR   A 1 132 ? 6.84685   31.32825 30.97807 1.000 38.40103  ? 139 TYR   A N   1 
ATOM   947  C CA  . TYR   A 1 132 ? 7.78892   30.34542 31.49465 1.000 41.49373  ? 139 TYR   A CA  1 
ATOM   948  C C   . TYR   A 1 132 ? 7.50143   29.95306 32.93687 1.000 37.99135  ? 139 TYR   A C   1 
ATOM   949  O O   . TYR   A 1 132 ? 8.10706   28.99556 33.42954 1.000 41.46635  ? 139 TYR   A O   1 
ATOM   950  C CB  . TYR   A 1 132 ? 9.21470   30.87825 31.34770 1.000 39.52591  ? 139 TYR   A CB  1 
ATOM   951  C CG  . TYR   A 1 132 ? 9.55238   31.23790 29.91740 1.000 40.81317  ? 139 TYR   A CG  1 
ATOM   952  C CD1 . TYR   A 1 132 ? 9.93560   30.26075 29.00696 1.000 39.42205  ? 139 TYR   A CD1 1 
ATOM   953  C CD2 . TYR   A 1 132 ? 9.46478   32.55044 29.47127 1.000 42.14337  ? 139 TYR   A CD2 1 
ATOM   954  C CE1 . TYR   A 1 132 ? 10.23456  30.58293 27.69506 1.000 40.22675  ? 139 TYR   A CE1 1 
ATOM   955  C CE2 . TYR   A 1 132 ? 9.76132   32.88224 28.16218 1.000 45.84716  ? 139 TYR   A CE2 1 
ATOM   956  C CZ  . TYR   A 1 132 ? 10.14576  31.89534 27.27879 1.000 46.79128  ? 139 TYR   A CZ  1 
ATOM   957  O OH  . TYR   A 1 132 ? 10.44204  32.22294 25.97518 1.000 51.37041  ? 139 TYR   A OH  1 
ATOM   958  N N   . SER   A 1 133 ? 6.58758   30.65105 33.61615 1.000 38.86492  ? 140 SER   A N   1 
ATOM   959  C CA  . SER   A 1 133 ? 6.11126   30.19854 34.91688 1.000 38.36848  ? 140 SER   A CA  1 
ATOM   960  C C   . SER   A 1 133 ? 5.30954   28.90867 34.82190 1.000 39.17363  ? 140 SER   A C   1 
ATOM   961  O O   . SER   A 1 133 ? 5.00486   28.30975 35.85892 1.000 37.97260  ? 140 SER   A O   1 
ATOM   962  C CB  . SER   A 1 133 ? 5.25967   31.28411 35.57736 1.000 38.79388  ? 140 SER   A CB  1 
ATOM   963  O OG  . SER   A 1 133 ? 4.01912   31.43678 34.90922 1.000 39.69747  ? 140 SER   A OG  1 
ATOM   964  N N   . ALA   A 1 134 ? 4.95600   28.47606 33.60866 1.000 36.13369  ? 141 ALA   A N   1 
ATOM   965  C CA  . ALA   A 1 134 ? 4.26910   27.20140 33.44312 1.000 35.90816  ? 141 ALA   A CA  1 
ATOM   966  C C   . ALA   A 1 134 ? 5.12481   26.03959 33.92580 1.000 37.90951  ? 141 ALA   A C   1 
ATOM   967  O O   . ALA   A 1 134 ? 4.59033   25.00161 34.33101 1.000 35.98586  ? 141 ALA   A O   1 
ATOM   968  C CB  . ALA   A 1 134 ? 3.88235   27.00242 31.97832 1.000 37.47205  ? 141 ALA   A CB  1 
ATOM   969  N N   . TYR   A 1 135 ? 6.44741   26.19291 33.89618 1.000 35.53454  ? 142 TYR   A N   1 
ATOM   970  C CA  . TYR   A 1 135 ? 7.34590   25.14299 34.35519 1.000 41.44494  ? 142 TYR   A CA  1 
ATOM   971  C C   . TYR   A 1 135 ? 7.45395   25.07810 35.87251 1.000 42.72318  ? 142 TYR   A C   1 
ATOM   972  O O   . TYR   A 1 135 ? 8.19868   24.23771 36.38871 1.000 43.21306  ? 142 TYR   A O   1 
ATOM   973  C CB  . TYR   A 1 135 ? 8.72655   25.32885 33.72185 1.000 36.77253  ? 142 TYR   A CB  1 
ATOM   974  C CG  . TYR   A 1 135 ? 8.71988   25.02320 32.24135 1.000 41.07273  ? 142 TYR   A CG  1 
ATOM   975  C CD1 . TYR   A 1 135 ? 8.91924   23.72809 31.77928 1.000 38.24120  ? 142 TYR   A CD1 1 
ATOM   976  C CD2 . TYR   A 1 135 ? 8.48130   26.02281 31.30728 1.000 35.68851  ? 142 TYR   A CD2 1 
ATOM   977  C CE1 . TYR   A 1 135 ? 8.90077   23.44076 30.42696 1.000 40.05897  ? 142 TYR   A CE1 1 
ATOM   978  C CE2 . TYR   A 1 135 ? 8.45922   25.74532 29.95269 1.000 36.23763  ? 142 TYR   A CE2 1 
ATOM   979  C CZ  . TYR   A 1 135 ? 8.66971   24.45278 29.51825 1.000 39.95496  ? 142 TYR   A CZ  1 
ATOM   980  O OH  . TYR   A 1 135 ? 8.64898   24.17015 28.17118 1.000 37.61459  ? 142 TYR   A OH  1 
ATOM   981  N N   . LEU   A 1 136 ? 6.73443   25.94003 36.59589 1.000 40.33705  ? 143 LEU   A N   1 
ATOM   982  C CA  . LEU   A 1 136 ? 6.57360   25.73600 38.03074 1.000 43.49176  ? 143 LEU   A CA  1 
ATOM   983  C C   . LEU   A 1 136 ? 5.78422   24.46913 38.31858 1.000 45.89486  ? 143 LEU   A C   1 
ATOM   984  O O   . LEU   A 1 136 ? 6.01301   23.81054 39.33965 1.000 41.61121  ? 143 LEU   A O   1 
ATOM   985  C CB  . LEU   A 1 136 ? 5.87481   26.93955 38.66601 1.000 42.54632  ? 143 LEU   A CB  1 
ATOM   986  C CG  . LEU   A 1 136 ? 6.61387   28.27706 38.72350 1.000 43.15921  ? 143 LEU   A CG  1 
ATOM   987  C CD1 . LEU   A 1 136 ? 5.63727   29.40485 39.01660 1.000 41.51700  ? 143 LEU   A CD1 1 
ATOM   988  C CD2 . LEU   A 1 136 ? 7.71067   28.23727 39.77488 1.000 43.80027  ? 143 LEU   A CD2 1 
ATOM   989  N N   . VAL   A 1 137 ? 4.85807   24.10721 37.43060 1.000 41.25564  ? 144 VAL   A N   1 
ATOM   990  C CA  . VAL   A 1 137 ? 3.99674   22.96005 37.63813 1.000 42.24108  ? 144 VAL   A CA  1 
ATOM   991  C C   . VAL   A 1 137 ? 4.11937   21.90665 36.54518 1.000 42.81951  ? 144 VAL   A C   1 
ATOM   992  O O   . VAL   A 1 137 ? 3.66968   20.76930 36.74780 1.000 41.63514  ? 144 VAL   A O   1 
ATOM   993  C CB  . VAL   A 1 137 ? 2.52114   23.39636 37.77841 1.000 41.70505  ? 144 VAL   A CB  1 
ATOM   994  C CG1 . VAL   A 1 137 ? 2.35273   24.31192 38.97917 1.000 43.33625  ? 144 VAL   A CG1 1 
ATOM   995  C CG2 . VAL   A 1 137 ? 2.05359   24.08564 36.50347 1.000 39.59582  ? 144 VAL   A CG2 1 
ATOM   996  N N   . ALA   A 1 138 ? 4.70934   22.23099 35.39659 1.000 40.62905  ? 145 ALA   A N   1 
ATOM   997  C CA  . ALA   A 1 138 ? 4.76076   21.32736 34.25606 1.000 40.85209  ? 145 ALA   A CA  1 
ATOM   998  C C   . ALA   A 1 138 ? 6.18824   20.85439 34.02498 1.000 41.70921  ? 145 ALA   A C   1 
ATOM   999  O O   . ALA   A 1 138 ? 7.12157   21.66407 34.00646 1.000 41.04889  ? 145 ALA   A O   1 
ATOM   1000 C CB  . ALA   A 1 138 ? 4.22536   22.00972 32.99525 1.000 39.06594  ? 145 ALA   A CB  1 
ATOM   1001 N N   . GLU   A 1 139 ? 6.35211   19.54174 33.85304 1.000 43.89514  ? 146 GLU   A N   1 
ATOM   1002 C CA  . GLU   A 1 139 ? 7.62946   18.99372 33.41855 1.000 44.04928  ? 146 GLU   A CA  1 
ATOM   1003 C C   . GLU   A 1 139 ? 7.81341   19.09644 31.91112 1.000 43.45525  ? 146 GLU   A C   1 
ATOM   1004 O O   . GLU   A 1 139 ? 8.95052   19.03765 31.43096 1.000 42.91945  ? 146 GLU   A O   1 
ATOM   1005 C CB  . GLU   A 1 139 ? 7.75454   17.53355 33.85918 1.000 52.62944  ? 146 GLU   A CB  1 
ATOM   1006 C CG  . GLU   A 1 139 ? 6.64820   16.63332 33.33565 1.000 56.87015  ? 146 GLU   A CG  1 
ATOM   1007 C CD  . GLU   A 1 139 ? 6.79335   15.19912 33.80397 1.000 76.65815  ? 146 GLU   A CD  1 
ATOM   1008 O OE1 . GLU   A 1 139 ? 6.89634   14.29911 32.94418 1.000 91.21568  ? 146 GLU   A OE1 1 
ATOM   1009 O OE2 . GLU   A 1 139 ? 6.80346   14.97152 35.03219 1.000 77.42316  ? 146 GLU   A OE2 1 
ATOM   1010 N N   . LYS   A 1 140 ? 6.72283   19.24840 31.16255 1.000 42.69198  ? 147 LYS   A N   1 
ATOM   1011 C CA  . LYS   A 1 140 ? 6.77192   19.42837 29.71976 1.000 40.98977  ? 147 LYS   A CA  1 
ATOM   1012 C C   . LYS   A 1 140 ? 5.59669   20.30076 29.30729 1.000 38.89165  ? 147 LYS   A C   1 
ATOM   1013 O O   . LYS   A 1 140 ? 4.49318   20.15529 29.83954 1.000 37.41581  ? 147 LYS   A O   1 
ATOM   1014 C CB  . LYS   A 1 140 ? 6.72406   18.08674 28.97795 1.000 42.29488  ? 147 LYS   A CB  1 
ATOM   1015 C CG  . LYS   A 1 140 ? 6.82356   18.21043 27.46370 1.000 43.48753  ? 147 LYS   A CG  1 
ATOM   1016 C CD  . LYS   A 1 140 ? 6.99154   16.85204 26.80255 1.000 45.00740  ? 147 LYS   A CD  1 
ATOM   1017 C CE  . LYS   A 1 140 ? 5.64431   16.20457 26.53008 1.000 46.00868  ? 147 LYS   A CE  1 
ATOM   1018 N NZ  . LYS   A 1 140 ? 5.78875   14.83048 25.97543 1.000 49.05376  ? 147 LYS   A NZ  1 
ATOM   1019 N N   . VAL   A 1 141 ? 5.83949   21.20992 28.36720 1.000 35.37143  ? 148 VAL   A N   1 
ATOM   1020 C CA  . VAL   A 1 141 ? 4.81436   22.11331 27.85990 1.000 35.23422  ? 148 VAL   A CA  1 
ATOM   1021 C C   . VAL   A 1 141 ? 4.73961   21.95848 26.34866 1.000 37.88554  ? 148 VAL   A C   1 
ATOM   1022 O O   . VAL   A 1 141 ? 5.75746   22.07570 25.65658 1.000 39.24761  ? 148 VAL   A O   1 
ATOM   1023 C CB  . VAL   A 1 141 ? 5.09938   23.57705 28.24375 1.000 34.89810  ? 148 VAL   A CB  1 
ATOM   1024 C CG1 . VAL   A 1 141 ? 4.05017   24.49503 27.63574 1.000 34.35016  ? 148 VAL   A CG1 1 
ATOM   1025 C CG2 . VAL   A 1 141 ? 5.13542   23.73314 29.75573 1.000 36.84424  ? 148 VAL   A CG2 1 
ATOM   1026 N N   . THR   A 1 142 ? 3.53896   21.69154 25.84292 1.000 34.65440  ? 149 THR   A N   1 
ATOM   1027 C CA  . THR   A 1 142 ? 3.27475   21.62480 24.41243 1.000 37.18112  ? 149 THR   A CA  1 
ATOM   1028 C C   . THR   A 1 142 ? 2.36946   22.78453 24.02402 1.000 42.55649  ? 149 THR   A C   1 
ATOM   1029 O O   . THR   A 1 142 ? 1.33836   23.01333 24.66551 1.000 36.63467  ? 149 THR   A O   1 
ATOM   1030 C CB  . THR   A 1 142 ? 2.62337   20.29421 24.02864 1.000 39.03390  ? 149 THR   A CB  1 
ATOM   1031 O OG1 . THR   A 1 142 ? 3.41123   19.20981 24.53592 1.000 40.60683  ? 149 THR   A OG1 1 
ATOM   1032 C CG2 . THR   A 1 142 ? 2.51379   20.17190 22.51476 1.000 38.22300  ? 149 THR   A CG2 1 
ATOM   1033 N N   . VAL   A 1 143 ? 2.75641   23.51438 22.98211 1.000 31.13955  ? 150 VAL   A N   1 
ATOM   1034 C CA  . VAL   A 1 143 ? 2.01507   24.68043 22.51605 1.000 36.42579  ? 150 VAL   A CA  1 
ATOM   1035 C C   . VAL   A 1 143 ? 1.60330   24.43062 21.07253 1.000 38.78667  ? 150 VAL   A C   1 
ATOM   1036 O O   . VAL   A 1 143 ? 2.45699   24.34338 20.18000 1.000 36.14383  ? 150 VAL   A O   1 
ATOM   1037 C CB  . VAL   A 1 143 ? 2.83156   25.97363 22.64084 1.000 37.40482  ? 150 VAL   A CB  1 
ATOM   1038 C CG1 . VAL   A 1 143 ? 2.04662   27.14819 22.07960 1.000 33.62230  ? 150 VAL   A CG1 1 
ATOM   1039 C CG2 . VAL   A 1 143 ? 3.19461   26.22771 24.09418 1.000 34.35271  ? 150 VAL   A CG2 1 
ATOM   1040 N N   . ILE   A 1 144 ? 0.29838   24.30959 20.84429 1.000 36.19345  ? 151 ILE   A N   1 
ATOM   1041 C CA  . ILE   A 1 144 ? -0.27394  24.24120 19.50548 1.000 35.45970  ? 151 ILE   A CA  1 
ATOM   1042 C C   . ILE   A 1 144 ? -0.85957  25.60701 19.18306 1.000 38.98894  ? 151 ILE   A C   1 
ATOM   1043 O O   . ILE   A 1 144 ? -1.67351  26.13747 19.94987 1.000 38.96515  ? 151 ILE   A O   1 
ATOM   1044 C CB  . ILE   A 1 144 ? -1.34570  23.14210 19.40798 1.000 41.80645  ? 151 ILE   A CB  1 
ATOM   1045 C CG1 . ILE   A 1 144 ? -0.91998  21.90543 20.20147 1.000 38.66410  ? 151 ILE   A CG1 1 
ATOM   1046 C CG2 . ILE   A 1 144 ? -1.60130  22.77748 17.95414 1.000 43.84052  ? 151 ILE   A CG2 1 
ATOM   1047 C CD1 . ILE   A 1 144 ? 0.20797   21.12606 19.56442 1.000 47.00866  ? 151 ILE   A CD1 1 
ATOM   1048 N N   . THR   A 1 145 ? -0.44497  26.18445 18.05849 1.000 35.44629  ? 152 THR   A N   1 
ATOM   1049 C CA  . THR   A 1 145 ? -0.83591  27.54418 17.72247 1.000 37.60999  ? 152 THR   A CA  1 
ATOM   1050 C C   . THR   A 1 145 ? -1.09634  27.65639 16.22800 1.000 36.79987  ? 152 THR   A C   1 
ATOM   1051 O O   . THR   A 1 145 ? -0.53229  26.91145 15.42204 1.000 37.57914  ? 152 THR   A O   1 
ATOM   1052 C CB  . THR   A 1 145 ? 0.23491   28.55873 18.15623 1.000 34.45640  ? 152 THR   A CB  1 
ATOM   1053 O OG1 . THR   A 1 145 ? -0.26999  29.89031 17.99855 1.000 37.72801  ? 152 THR   A OG1 1 
ATOM   1054 C CG2 . THR   A 1 145 ? 1.50600   28.39233 17.33363 1.000 37.09171  ? 152 THR   A CG2 1 
ATOM   1055 N N   . LYS   A 1 146 ? -1.96684  28.59827 15.87011 1.000 36.34045  ? 153 LYS   A N   1 
ATOM   1056 C CA  . LYS   A 1 146 ? -2.34493  28.83274 14.48145 1.000 35.10402  ? 153 LYS   A CA  1 
ATOM   1057 C C   . LYS   A 1 146 ? -2.56072  30.32347 14.28117 1.000 36.13250  ? 153 LYS   A C   1 
ATOM   1058 O O   . LYS   A 1 146 ? -3.46737  30.90765 14.88279 1.000 35.24306  ? 153 LYS   A O   1 
ATOM   1059 C CB  . LYS   A 1 146 ? -3.60978  28.05234 14.11037 1.000 37.35693  ? 153 LYS   A CB  1 
ATOM   1060 C CG  . LYS   A 1 146 ? -4.15815  28.37224 12.72714 1.000 37.90069  ? 153 LYS   A CG  1 
ATOM   1061 C CD  . LYS   A 1 146 ? -3.16130  28.02429 11.63240 1.000 37.89544  ? 153 LYS   A CD  1 
ATOM   1062 C CE  . LYS   A 1 146 ? -3.78784  28.16472 10.25131 1.000 41.42750  ? 153 LYS   A CE  1 
ATOM   1063 N NZ  . LYS   A 1 146 ? -3.81423  29.58274 9.79061  1.000 39.00313  ? 153 LYS   A NZ  1 
ATOM   1064 N N   . HIS   A 1 147 ? -1.72553  30.93247 13.44716 1.000 35.43447  ? 154 HIS   A N   1 
ATOM   1065 C CA  . HIS   A 1 147 ? -1.86186  32.32960 13.06902 1.000 36.94201  ? 154 HIS   A CA  1 
ATOM   1066 C C   . HIS   A 1 147 ? -2.49843  32.42088 11.68756 1.000 41.78107  ? 154 HIS   A C   1 
ATOM   1067 O O   . HIS   A 1 147 ? -2.39004  31.49954 10.87455 1.000 41.72251  ? 154 HIS   A O   1 
ATOM   1068 C CB  . HIS   A 1 147 ? -0.49886  33.02882 13.07722 1.000 40.59492  ? 154 HIS   A CB  1 
ATOM   1069 C CG  . HIS   A 1 147 ? -0.57552  34.51878 12.94403 1.000 39.94642  ? 154 HIS   A CG  1 
ATOM   1070 N ND1 . HIS   A 1 147 ? -0.66553  35.15430 11.72451 1.000 42.24127  ? 154 HIS   A ND1 1 
ATOM   1071 C CD2 . HIS   A 1 147 ? -0.56644  35.49893 13.87839 1.000 40.66777  ? 154 HIS   A CD2 1 
ATOM   1072 C CE1 . HIS   A 1 147 ? -0.71345  36.46100 11.91285 1.000 45.80049  ? 154 HIS   A CE1 1 
ATOM   1073 N NE2 . HIS   A 1 147 ? -0.65492  36.69669 13.21112 1.000 45.41532  ? 154 HIS   A NE2 1 
ATOM   1074 N N   . ASN   A 1 148 ? -3.17639  33.54340 11.43266 1.000 39.12390  ? 155 ASN   A N   1 
ATOM   1075 C CA  . ASN   A 1 148 ? -3.85897  33.72310 10.15443 1.000 44.35271  ? 155 ASN   A CA  1 
ATOM   1076 C C   . ASN   A 1 148 ? -2.88742  33.68566 8.98096  1.000 45.95318  ? 155 ASN   A C   1 
ATOM   1077 O O   . ASN   A 1 148 ? -3.27007  33.29719 7.87130  1.000 46.36598  ? 155 ASN   A O   1 
ATOM   1078 C CB  . ASN   A 1 148 ? -4.63062  35.04430 10.15112 1.000 42.11450  ? 155 ASN   A CB  1 
ATOM   1079 C CG  . ASN   A 1 148 ? -6.00938  34.92070 10.77194 1.000 49.08111  ? 155 ASN   A CG  1 
ATOM   1080 O OD1 . ASN   A 1 148 ? -6.56639  33.82678 10.86822 1.000 44.18701  ? 155 ASN   A OD1 1 
ATOM   1081 N ND2 . ASN   A 1 148 ? -6.56890  36.04873 11.19535 1.000 40.66049  ? 155 ASN   A ND2 1 
ATOM   1082 N N   . ASP   A 1 149 ? -1.63303  34.07385 9.20332  1.000 45.60315  ? 156 ASP   A N   1 
ATOM   1083 C CA  . ASP   A 1 149 ? -0.64991  34.20769 8.13780  1.000 52.23234  ? 156 ASP   A CA  1 
ATOM   1084 C C   . ASP   A 1 149 ? 0.30144   33.02000 8.04747  1.000 47.54720  ? 156 ASP   A C   1 
ATOM   1085 O O   . ASP   A 1 149 ? 1.26303   33.07129 7.27450  1.000 48.43145  ? 156 ASP   A O   1 
ATOM   1086 C CB  . ASP   A 1 149 ? 0.15490   35.49613 8.32678  1.000 50.59093  ? 156 ASP   A CB  1 
ATOM   1087 C CG  . ASP   A 1 149 ? -0.71129  36.74074 8.27621  1.000 53.83005  ? 156 ASP   A CG  1 
ATOM   1088 O OD1 . ASP   A 1 149 ? -1.82192  36.67657 7.70816  1.000 70.56326  ? 156 ASP   A OD1 1 
ATOM   1089 O OD2 . ASP   A 1 149 ? -0.27958  37.78513 8.80769  1.000 52.53450  ? 156 ASP   A OD2 1 
ATOM   1090 N N   . ASP   A 1 150 ? 0.06381   31.95538 8.81156  1.000 44.86769  ? 157 ASP   A N   1 
ATOM   1091 C CA  . ASP   A 1 150 ? 0.97371   30.81935 8.84000  1.000 48.44519  ? 157 ASP   A CA  1 
ATOM   1092 C C   . ASP   A 1 150 ? 0.17258   29.53583 9.01698  1.000 47.02126  ? 157 ASP   A C   1 
ATOM   1093 O O   . ASP   A 1 150 ? -1.05634  29.55365 9.13572  1.000 45.96070  ? 157 ASP   A O   1 
ATOM   1094 C CB  . ASP   A 1 150 ? 2.01767   30.97931 9.95215  1.000 44.98706  ? 157 ASP   A CB  1 
ATOM   1095 C CG  . ASP   A 1 150 ? 3.35134   30.35682 9.59295  1.000 48.58900  ? 157 ASP   A CG  1 
ATOM   1096 O OD1 . ASP   A 1 150 ? 3.37896   29.47950 8.70423  1.000 46.37889  ? 157 ASP   A OD1 1 
ATOM   1097 O OD2 . ASP   A 1 150 ? 4.37149   30.74098 10.20287 1.000 45.70777  ? 157 ASP   A OD2 1 
ATOM   1098 N N   . GLU   A 1 151 ? 0.88349   28.41050 9.02740  1.000 47.14891  ? 158 GLU   A N   1 
ATOM   1099 C CA  . GLU   A 1 151 ? 0.27586   27.10798 9.23695  1.000 48.96767  ? 158 GLU   A CA  1 
ATOM   1100 C C   . GLU   A 1 151 ? 0.17200   26.81182 10.73155 1.000 45.55058  ? 158 GLU   A C   1 
ATOM   1101 O O   . GLU   A 1 151 ? 0.62454   27.58296 11.58105 1.000 44.91297  ? 158 GLU   A O   1 
ATOM   1102 C CB  . GLU   A 1 151 ? 1.07907   26.01921 8.52594  1.000 52.92478  ? 158 GLU   A CB  1 
ATOM   1103 C CG  . GLU   A 1 151 ? 1.28554   26.25045 7.03927  1.000 65.46467  ? 158 GLU   A CG  1 
ATOM   1104 C CD  . GLU   A 1 151 ? 2.44081   25.43912 6.48363  1.000 93.12475  ? 158 GLU   A CD  1 
ATOM   1105 O OE1 . GLU   A 1 151 ? 2.49518   24.21940 6.74946  1.000 84.48696  ? 158 GLU   A OE1 1 
ATOM   1106 O OE2 . GLU   A 1 151 ? 3.29587   26.02126 5.78394  1.000 96.08808  ? 158 GLU   A OE2 1 
ATOM   1107 N N   . GLN   A 1 152 ? -0.43181  25.67272 11.05781 1.000 43.66984  ? 159 GLN   A N   1 
ATOM   1108 C CA  . GLN   A 1 152 ? -0.53073  25.23629 12.44288 1.000 41.56436  ? 159 GLN   A CA  1 
ATOM   1109 C C   . GLN   A 1 152 ? 0.76848   24.55817 12.85923 1.000 43.79729  ? 159 GLN   A C   1 
ATOM   1110 O O   . GLN   A 1 152 ? 1.26713   23.67136 12.15946 1.000 41.79412  ? 159 GLN   A O   1 
ATOM   1111 C CB  . GLN   A 1 152 ? -1.71200  24.28355 12.61773 1.000 44.37777  ? 159 GLN   A CB  1 
ATOM   1112 C CG  . GLN   A 1 152 ? -2.02815  23.94225 14.06257 1.000 45.83704  ? 159 GLN   A CG  1 
ATOM   1113 C CD  . GLN   A 1 152 ? -3.43456  23.40655 14.23290 1.000 53.11032  ? 159 GLN   A CD  1 
ATOM   1114 O OE1 . GLN   A 1 152 ? -4.40821  24.05437 13.84791 1.000 53.24933  ? 159 GLN   A OE1 1 
ATOM   1115 N NE2 . GLN   A 1 152 ? -3.54893  22.21580 14.80932 1.000 55.53402  ? 159 GLN   A NE2 1 
ATOM   1116 N N   . TYR   A 1 153 ? 1.31751   24.97683 13.99691 1.000 38.54712  ? 160 TYR   A N   1 
ATOM   1117 C CA  . TYR   A 1 153 ? 2.60481   24.48562 14.46209 1.000 42.02467  ? 160 TYR   A CA  1 
ATOM   1118 C C   . TYR   A 1 153 ? 2.48046   23.94297 15.87764 1.000 41.75842  ? 160 TYR   A C   1 
ATOM   1119 O O   . TYR   A 1 153 ? 1.55436   24.27999 16.61988 1.000 39.45204  ? 160 TYR   A O   1 
ATOM   1120 C CB  . TYR   A 1 153 ? 3.67449   25.58448 14.42151 1.000 41.32569  ? 160 TYR   A CB  1 
ATOM   1121 C CG  . TYR   A 1 153 ? 4.09632   25.97051 13.02475 1.000 46.53358  ? 160 TYR   A CG  1 
ATOM   1122 C CD1 . TYR   A 1 153 ? 3.63601   27.14115 12.43985 1.000 43.77994  ? 160 TYR   A CD1 1 
ATOM   1123 C CD2 . TYR   A 1 153 ? 4.95544   25.16408 12.29049 1.000 47.70419  ? 160 TYR   A CD2 1 
ATOM   1124 C CE1 . TYR   A 1 153 ? 4.01700   27.49751 11.16298 1.000 47.72157  ? 160 TYR   A CE1 1 
ATOM   1125 C CE2 . TYR   A 1 153 ? 5.34311   25.51304 11.01191 1.000 48.69150  ? 160 TYR   A CE2 1 
ATOM   1126 C CZ  . TYR   A 1 153 ? 4.87087   26.68122 10.45313 1.000 51.64770  ? 160 TYR   A CZ  1 
ATOM   1127 O OH  . TYR   A 1 153 ? 5.25326   27.03522 9.17962  1.000 64.56845  ? 160 TYR   A OH  1 
ATOM   1128 N N   . ALA   A 1 154 ? 3.44029   23.09645 16.24301 1.000 40.49796  ? 161 ALA   A N   1 
ATOM   1129 C CA  . ALA   A 1 154 ? 3.51333   22.49991 17.56992 1.000 38.80377  ? 161 ALA   A CA  1 
ATOM   1130 C C   . ALA   A 1 154 ? 4.86357   22.83648 18.18480 1.000 40.95610  ? 161 ALA   A C   1 
ATOM   1131 O O   . ALA   A 1 154 ? 5.90583   22.40995 17.67562 1.000 41.89392  ? 161 ALA   A O   1 
ATOM   1132 C CB  . ALA   A 1 154 ? 3.31098   20.98487 17.50742 1.000 41.83909  ? 161 ALA   A CB  1 
ATOM   1133 N N   . TRP   A 1 155 ? 4.83974   23.60646 19.26722 1.000 34.88449  ? 162 TRP   A N   1 
ATOM   1134 C CA  . TRP   A 1 155 ? 6.02834   23.94274 20.03697 1.000 37.52427  ? 162 TRP   A CA  1 
ATOM   1135 C C   . TRP   A 1 155 ? 6.04486   23.09893 21.30343 1.000 39.04235  ? 162 TRP   A C   1 
ATOM   1136 O O   . TRP   A 1 155 ? 5.00801   22.91316 21.94673 1.000 39.16742  ? 162 TRP   A O   1 
ATOM   1137 C CB  . TRP   A 1 155 ? 6.03661   25.43549 20.38147 1.000 36.05978  ? 162 TRP   A CB  1 
ATOM   1138 C CG  . TRP   A 1 155 ? 7.19869   25.91289 21.21172 1.000 38.44983  ? 162 TRP   A CG  1 
ATOM   1139 C CD1 . TRP   A 1 155 ? 8.30381   26.57619 20.76157 1.000 36.51785  ? 162 TRP   A CD1 1 
ATOM   1140 C CD2 . TRP   A 1 155 ? 7.34762   25.81053 22.63677 1.000 39.19302  ? 162 TRP   A CD2 1 
ATOM   1141 N NE1 . TRP   A 1 155 ? 9.13978   26.87203 21.81050 1.000 38.33917  ? 162 TRP   A NE1 1 
ATOM   1142 C CE2 . TRP   A 1 155 ? 8.57646   26.41384 22.97189 1.000 37.00454  ? 162 TRP   A CE2 1 
ATOM   1143 C CE3 . TRP   A 1 155 ? 6.56769   25.25858 23.65840 1.000 36.92587  ? 162 TRP   A CE3 1 
ATOM   1144 C CZ2 . TRP   A 1 155 ? 9.04344   26.47971 24.28354 1.000 37.45972  ? 162 TRP   A CZ2 1 
ATOM   1145 C CZ3 . TRP   A 1 155 ? 7.03338   25.32410 24.96038 1.000 34.12306  ? 162 TRP   A CZ3 1 
ATOM   1146 C CH2 . TRP   A 1 155 ? 8.25919   25.93194 25.26129 1.000 36.99160  ? 162 TRP   A CH2 1 
ATOM   1147 N N   . GLU   A 1 156 ? 7.21896   22.58033 21.65669 1.000 37.37426  ? 163 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 156 ? 7.32035   21.70090 22.81199 1.000 39.61588  ? 163 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 156 ? 8.70143   21.81642 23.43723 1.000 41.50147  ? 163 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 156 ? 9.70451   21.94150 22.72954 1.000 36.93693  ? 163 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 156 ? 7.04103   20.24425 22.42689 1.000 39.73288  ? 163 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 156 ? 6.89647   19.30656 23.61201 1.000 43.92378  ? 163 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 156 ? 6.37312   17.94351 23.20992 1.000 49.61017  ? 163 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 156 ? 7.18810   17.09207 22.79764 1.000 51.36238  ? 163 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 156 ? 5.14731   17.72413 23.30476 1.000 57.15269  ? 163 GLU   A OE2 1 
ATOM   1156 N N   . SER   A 1 157 ? 8.74221   21.76282 24.76778 1.000 38.08094  ? 164 SER   A N   1 
ATOM   1157 C CA  . SER   A 1 157 ? 10.00458  21.78663 25.49441 1.000 38.97313  ? 164 SER   A CA  1 
ATOM   1158 C C   . SER   A 1 157 ? 9.80409   21.18313 26.87477 1.000 40.58665  ? 164 SER   A C   1 
ATOM   1159 O O   . SER   A 1 157 ? 8.85639   21.54259 27.58074 1.000 39.07534  ? 164 SER   A O   1 
ATOM   1160 C CB  . SER   A 1 157 ? 10.54835  23.21225 25.62317 1.000 39.74439  ? 164 SER   A CB  1 
ATOM   1161 O OG  . SER   A 1 157 ? 11.71374  23.22993 26.42955 1.000 38.42352  ? 164 SER   A OG  1 
ATOM   1162 N N   . SER   A 1 158 ? 10.69316  20.26274 27.24763 1.000 40.26820  ? 165 SER   A N   1 
ATOM   1163 C CA  . SER   A 1 158 ? 10.82707  19.79807 28.62165 1.000 44.77404  ? 165 SER   A CA  1 
ATOM   1164 C C   . SER   A 1 158 ? 11.95057  20.52705 29.34763 1.000 50.34174  ? 165 SER   A C   1 
ATOM   1165 O O   . SER   A 1 158 ? 12.55327  19.97712 30.27704 1.000 46.28866  ? 165 SER   A O   1 
ATOM   1166 C CB  . SER   A 1 158 ? 11.06255  18.28802 28.65502 1.000 44.53831  ? 165 SER   A CB  1 
ATOM   1167 O OG  . SER   A 1 158 ? 10.00016  17.59133 28.02836 1.000 45.63952  ? 165 SER   A OG  1 
ATOM   1168 N N   . ALA   A 1 159 ? 12.23933  21.75454 28.92721 1.000 44.27783  ? 166 ALA   A N   1 
ATOM   1169 C CA  . ALA   A 1 159 ? 13.36894  22.55839 29.40899 1.000 44.83867  ? 166 ALA   A CA  1 
ATOM   1170 C C   . ALA   A 1 159 ? 14.65922  21.80330 29.08155 1.000 46.37056  ? 166 ALA   A C   1 
ATOM   1171 O O   . ALA   A 1 159 ? 14.74047  21.10850 28.06038 1.000 47.55142  ? 166 ALA   A O   1 
ATOM   1172 C CB  . ALA   A 1 159 ? 13.18486  22.90493 30.87129 1.000 43.08601  ? 166 ALA   A CB  1 
ATOM   1173 N N   . GLY   A 1 160 ? 15.67381  21.92482 29.93352 1.000 46.60917  ? 167 GLY   A N   1 
ATOM   1174 C CA  . GLY   A 1 160 ? 16.95896  21.33412 29.62349 1.000 48.83596  ? 167 GLY   A CA  1 
ATOM   1175 C C   . GLY   A 1 160 ? 17.77012  22.08823 28.59715 1.000 47.57187  ? 167 GLY   A C   1 
ATOM   1176 O O   . GLY   A 1 160 ? 18.84909  21.62373 28.21742 1.000 46.81882  ? 167 GLY   A O   1 
ATOM   1177 N N   . GLY   A 1 161 ? 17.27985  23.23431 28.12789 1.000 46.54718  ? 168 GLY   A N   1 
ATOM   1178 C CA  . GLY   A 1 161 ? 18.01246  24.07726 27.20848 1.000 49.28557  ? 168 GLY   A CA  1 
ATOM   1179 C C   . GLY   A 1 161 ? 17.60560  23.97319 25.75505 1.000 45.40145  ? 168 GLY   A C   1 
ATOM   1180 O O   . GLY   A 1 161 ? 18.24856  24.60484 24.90804 1.000 44.60295  ? 168 GLY   A O   1 
ATOM   1181 N N   . SER   A 1 162 ? 16.56160  23.21122 25.43373 1.000 42.58046  ? 169 SER   A N   1 
ATOM   1182 C CA  . SER   A 1 162 ? 16.17529  23.00902 24.04621 1.000 41.13078  ? 169 SER   A CA  1 
ATOM   1183 C C   . SER   A 1 162 ? 14.66041  22.94420 23.92210 1.000 45.19832  ? 169 SER   A C   1 
ATOM   1184 O O   . SER   A 1 162 ? 13.95200  22.60426 24.87374 1.000 41.56267  ? 169 SER   A O   1 
ATOM   1185 C CB  . SER   A 1 162 ? 16.79946  21.72974 23.46831 1.000 45.96057  ? 169 SER   A CB  1 
ATOM   1186 O OG  . SER   A 1 162 ? 16.18270  20.57185 24.00471 1.000 44.66681  ? 169 SER   A OG  1 
ATOM   1187 N N   . PHE   A 1 163 ? 14.17493  23.28338 22.72989 1.000 39.87539  ? 170 PHE   A N   1 
ATOM   1188 C CA  . PHE   A 1 163 ? 12.76906  23.14685 22.38437 1.000 39.41458  ? 170 PHE   A CA  1 
ATOM   1189 C C   . PHE   A 1 163 ? 12.66609  22.68376 20.93864 1.000 40.53903  ? 170 PHE   A C   1 
ATOM   1190 O O   . PHE   A 1 163 ? 13.62156  22.78235 20.16456 1.000 39.23138  ? 170 PHE   A O   1 
ATOM   1191 C CB  . PHE   A 1 163 ? 11.99469  24.45913 22.58894 1.000 39.28958  ? 170 PHE   A CB  1 
ATOM   1192 C CG  . PHE   A 1 163 ? 12.44611  25.58362 21.69767 1.000 39.27719  ? 170 PHE   A CG  1 
ATOM   1193 C CD1 . PHE   A 1 163 ? 13.48303  26.41678 22.08204 1.000 39.77166  ? 170 PHE   A CD1 1 
ATOM   1194 C CD2 . PHE   A 1 163 ? 11.82308  25.81650 20.48172 1.000 40.73120  ? 170 PHE   A CD2 1 
ATOM   1195 C CE1 . PHE   A 1 163 ? 13.89564  27.45592 21.26732 1.000 40.31219  ? 170 PHE   A CE1 1 
ATOM   1196 C CE2 . PHE   A 1 163 ? 12.23088  26.85324 19.66335 1.000 39.89947  ? 170 PHE   A CE2 1 
ATOM   1197 C CZ  . PHE   A 1 163 ? 13.26780  27.67427 20.05740 1.000 41.88960  ? 170 PHE   A CZ  1 
ATOM   1198 N N   . THR   A 1 164 ? 11.49197  22.17030 20.58132 1.000 38.05099  ? 171 THR   A N   1 
ATOM   1199 C CA  . THR   A 1 164 ? 11.23527  21.66954 19.24035 1.000 39.50974  ? 171 THR   A CA  1 
ATOM   1200 C C   . THR   A 1 164 ? 10.06942  22.42000 18.61183 1.000 40.84867  ? 171 THR   A C   1 
ATOM   1201 O O   . THR   A 1 164 ? 9.15956   22.88516 19.30507 1.000 37.55232  ? 171 THR   A O   1 
ATOM   1202 C CB  . THR   A 1 164 ? 10.92574  20.16544 19.24633 1.000 41.32420  ? 171 THR   A CB  1 
ATOM   1203 O OG1 . THR   A 1 164 ? 9.71801   19.92659 19.98044 1.000 41.16015  ? 171 THR   A OG1 1 
ATOM   1204 C CG2 . THR   A 1 164 ? 12.06720  19.38423 19.88096 1.000 41.16142  ? 171 THR   A CG2 1 
ATOM   1205 N N   . VAL   A 1 165 ? 10.11029  22.53521 17.28642 1.000 40.37638  ? 172 VAL   A N   1 
ATOM   1206 C CA  . VAL   A 1 165 ? 9.03629   23.13226 16.50236 1.000 41.20866  ? 172 VAL   A CA  1 
ATOM   1207 C C   . VAL   A 1 165 ? 8.75679   22.21923 15.31776 1.000 43.89429  ? 172 VAL   A C   1 
ATOM   1208 O O   . VAL   A 1 165 ? 9.68882   21.76951 14.64157 1.000 43.43783  ? 172 VAL   A O   1 
ATOM   1209 C CB  . VAL   A 1 165 ? 9.38862   24.55392 16.02053 1.000 41.54019  ? 172 VAL   A CB  1 
ATOM   1210 C CG1 . VAL   A 1 165 ? 8.28554   25.10243 15.12722 1.000 43.51423  ? 172 VAL   A CG1 1 
ATOM   1211 C CG2 . VAL   A 1 165 ? 9.61804   25.47838 17.20497 1.000 39.81654  ? 172 VAL   A CG2 1 
ATOM   1212 N N   . ARG   A 1 166 ? 7.47868   21.94054 15.07366 1.000 43.99159  ? 173 ARG   A N   1 
ATOM   1213 C CA  . ARG   A 1 166 ? 7.07689   21.08886 13.96523 1.000 46.67889  ? 173 ARG   A CA  1 
ATOM   1214 C C   . ARG   A 1 166 ? 5.71386   21.53983 13.46474 1.000 47.14781  ? 173 ARG   A C   1 
ATOM   1215 O O   . ARG   A 1 166 ? 4.94873   22.18664 14.18473 1.000 44.09871  ? 173 ARG   A O   1 
ATOM   1216 C CB  . ARG   A 1 166 ? 7.02361   19.61303 14.37720 1.000 50.58747  ? 173 ARG   A CB  1 
ATOM   1217 C CG  . ARG   A 1 166 ? 5.86132   19.28926 15.30253 1.000 51.81897  ? 173 ARG   A CG  1 
ATOM   1218 C CD  . ARG   A 1 166 ? 5.77667   17.80677 15.62263 1.000 56.21603  ? 173 ARG   A CD  1 
ATOM   1219 N NE  . ARG   A 1 166 ? 4.92363   17.56064 16.77946 1.000 79.05201  ? 173 ARG   A NE  1 
ATOM   1220 C CZ  . ARG   A 1 166 ? 3.59812   17.52833 16.74041 1.000 83.35730  ? 173 ARG   A CZ  1 
ATOM   1221 N NH1 . ARG   A 1 166 ? 2.93429   17.71238 15.61039 1.000 72.58372  ? 173 ARG   A NH1 1 
ATOM   1222 N NH2 . ARG   A 1 166 ? 2.92098   17.30933 17.86403 1.000 70.62370  ? 173 ARG   A NH2 1 
ATOM   1223 N N   . THR   A 1 167 ? 5.41852   21.19288 12.21537 1.000 45.15081  ? 174 THR   A N   1 
ATOM   1224 C CA  . THR   A 1 167 ? 4.08154   21.41434 11.68330 1.000 50.29503  ? 174 THR   A CA  1 
ATOM   1225 C C   . THR   A 1 167 ? 3.11324   20.42777 12.32341 1.000 53.08135  ? 174 THR   A C   1 
ATOM   1226 O O   . THR   A 1 167 ? 3.34972   19.21609 12.31379 1.000 57.23564  ? 174 THR   A O   1 
ATOM   1227 C CB  . THR   A 1 167 ? 4.07353   21.25917 10.16310 1.000 53.85780  ? 174 THR   A CB  1 
ATOM   1228 O OG1 . THR   A 1 167 ? 5.07319   22.10969 9.58780  1.000 55.06404  ? 174 THR   A OG1 1 
ATOM   1229 C CG2 . THR   A 1 167 ? 2.71173   21.63541 9.59784  1.000 58.44117  ? 174 THR   A CG2 1 
ATOM   1230 N N   . ASP   A 1 168 ? 2.02781   20.94642 12.89111 1.000 49.56317  ? 175 ASP   A N   1 
ATOM   1231 C CA  . ASP   A 1 168 ? 1.08219   20.10787 13.61423 1.000 58.69606  ? 175 ASP   A CA  1 
ATOM   1232 C C   . ASP   A 1 168 ? 0.15608   19.39226 12.63943 1.000 68.40403  ? 175 ASP   A C   1 
ATOM   1233 O O   . ASP   A 1 168 ? -0.45470  20.02239 11.77011 1.000 66.55265  ? 175 ASP   A O   1 
ATOM   1234 C CB  . ASP   A 1 168 ? 0.26726   20.94233 14.60097 1.000 54.35261  ? 175 ASP   A CB  1 
ATOM   1235 C CG  . ASP   A 1 168 ? -0.65376  20.09318 15.45515 1.000 59.58012  ? 175 ASP   A CG  1 
ATOM   1236 O OD1 . ASP   A 1 168 ? -0.21549  19.01643 15.91277 1.000 68.56396  ? 175 ASP   A OD1 1 
ATOM   1237 O OD2 . ASP   A 1 168 ? -1.81649  20.49663 15.66326 1.000 64.76262  ? 175 ASP   A OD2 1 
ATOM   1238 N N   . THR   A 1 169 ? 0.05160   18.07226 12.79182 1.000 79.29867  ? 176 THR   A N   1 
ATOM   1239 C CA  . THR   A 1 169 ? -0.79284  17.24733 11.93989 1.000 86.74567  ? 176 THR   A CA  1 
ATOM   1240 C C   . THR   A 1 169 ? -2.15438  16.95052 12.55298 1.000 82.63777  ? 176 THR   A C   1 
ATOM   1241 O O   . THR   A 1 169 ? -3.02448  16.41563 11.85735 1.000 81.26019  ? 176 THR   A O   1 
ATOM   1242 C CB  . THR   A 1 169 ? -0.09120  15.92006 11.62298 1.000 94.48608  ? 176 THR   A CB  1 
ATOM   1243 O OG1 . THR   A 1 169 ? 0.42684   15.35184 12.83288 1.000 84.38009  ? 176 THR   A OG1 1 
ATOM   1244 C CG2 . THR   A 1 169 ? 1.05186   16.14027 10.64478 1.000 84.12721  ? 176 THR   A CG2 1 
ATOM   1245 N N   . GLY   A 1 170 ? -2.36045  17.28469 13.82478 1.000 79.01729  ? 177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 170 ? -3.58138  16.92824 14.52117 1.000 79.31065  ? 177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 170 ? -4.80133  17.73579 14.12764 1.000 78.43483  ? 177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 170 ? -4.91731  18.19074 12.98572 1.000 77.51248  ? 177 GLY   A O   1 
ATOM   1249 N N   . GLU   A 1 171 ? -5.71706  17.91594 15.07346 1.000 79.44149  ? 178 GLU   A N   1 
ATOM   1250 C CA  . GLU   A 1 171 ? -6.96455  18.61051 14.79231 1.000 75.98717  ? 178 GLU   A CA  1 
ATOM   1251 C C   . GLU   A 1 171 ? -6.68961  20.07134 14.45528 1.000 66.44661  ? 178 GLU   A C   1 
ATOM   1252 O O   . GLU   A 1 171 ? -5.95286  20.74571 15.19125 1.000 61.27922  ? 178 GLU   A O   1 
ATOM   1253 C CB  . GLU   A 1 171 ? -7.90717  18.51898 15.99184 1.000 81.33535  ? 178 GLU   A CB  1 
ATOM   1254 C CG  . GLU   A 1 171 ? -7.97244  17.14027 16.63402 1.000 94.13815  ? 178 GLU   A CG  1 
ATOM   1255 C CD  . GLU   A 1 171 ? -9.12538  16.30483 16.11230 1.000 115.61886 ? 178 GLU   A CD  1 
ATOM   1256 O OE1 . GLU   A 1 171 ? -9.69876  15.52418 16.90087 1.000 102.79551 ? 178 GLU   A OE1 1 
ATOM   1257 O OE2 . GLU   A 1 171 ? -9.45855  16.42649 14.91468 1.000 115.54853 ? 178 GLU   A OE2 1 
ATOM   1258 N N   . PRO   A 1 172 ? -7.24726  20.59790 13.36619 1.000 63.16876  ? 179 PRO   A N   1 
ATOM   1259 C CA  . PRO   A 1 172 ? -7.05876  22.02101 13.05996 1.000 61.08462  ? 179 PRO   A CA  1 
ATOM   1260 C C   . PRO   A 1 172 ? -7.76368  22.89770 14.08398 1.000 58.04432  ? 179 PRO   A C   1 
ATOM   1261 O O   . PRO   A 1 172 ? -8.87275  22.59596 14.53107 1.000 61.44478  ? 179 PRO   A O   1 
ATOM   1262 C CB  . PRO   A 1 172 ? -7.67219  22.19022 11.66338 1.000 58.56788  ? 179 PRO   A CB  1 
ATOM   1263 C CG  . PRO   A 1 172 ? -8.23921  20.87990 11.27143 1.000 63.09836  ? 179 PRO   A CG  1 
ATOM   1264 C CD  . PRO   A 1 172 ? -8.05089  19.88175 12.35949 1.000 64.89144  ? 179 PRO   A CD  1 
ATOM   1265 N N   . MET   A 1 173 ? -7.10272  23.99405 14.45500 1.000 55.28377  ? 180 MET   A N   1 
ATOM   1266 C CA  . MET   A 1 173 ? -7.62027  24.89768 15.47252 1.000 55.04718  ? 180 MET   A CA  1 
ATOM   1267 C C   . MET   A 1 173 ? -8.40036  26.07216 14.90360 1.000 51.95860  ? 180 MET   A C   1 
ATOM   1268 O O   . MET   A 1 173 ? -9.19432  26.67628 15.63285 1.000 54.67771  ? 180 MET   A O   1 
ATOM   1269 C CB  . MET   A 1 173 ? -6.47410  25.44930 16.32626 1.000 54.69376  ? 180 MET   A CB  1 
ATOM   1270 C CG  . MET   A 1 173 ? -5.81400  24.43261 17.23099 1.000 61.71339  ? 180 MET   A CG  1 
ATOM   1271 S SD  . MET   A 1 173 ? -4.28785  25.08772 17.92493 1.000 67.80108  ? 180 MET   A SD  1 
ATOM   1272 C CE  . MET   A 1 173 ? -4.90679  26.52512 18.79271 1.000 48.31928  ? 180 MET   A CE  1 
ATOM   1273 N N   . GLY   A 1 174 ? -8.19536  26.41096 13.63411 1.000 48.48491  ? 181 GLY   A N   1 
ATOM   1274 C CA  . GLY   A 1 174 ? -8.78059  27.61382 13.07781 1.000 47.17603  ? 181 GLY   A CA  1 
ATOM   1275 C C   . GLY   A 1 174 ? -7.90254  28.82097 13.33301 1.000 44.08036  ? 181 GLY   A C   1 
ATOM   1276 O O   . GLY   A 1 174 ? -7.32641  29.38594 12.39858 1.000 42.97629  ? 181 GLY   A O   1 
ATOM   1277 N N   . ARG   A 1 175 ? -7.78609  29.21475 14.60067 1.000 39.22484  ? 182 ARG   A N   1 
ATOM   1278 C CA  . ARG   A 1 175 ? -6.92938  30.31788 15.01450 1.000 40.37153  ? 182 ARG   A CA  1 
ATOM   1279 C C   . ARG   A 1 175 ? -6.85963  30.33447 16.53344 1.000 36.59814  ? 182 ARG   A C   1 
ATOM   1280 O O   . ARG   A 1 175 ? -7.86785  30.10245 17.20483 1.000 38.91174  ? 182 ARG   A O   1 
ATOM   1281 C CB  . ARG   A 1 175 ? -7.45161  31.66590 14.49587 1.000 37.15489  ? 182 ARG   A CB  1 
ATOM   1282 C CG  . ARG   A 1 175 ? -6.47774  32.82054 14.68040 1.000 36.09555  ? 182 ARG   A CG  1 
ATOM   1283 C CD  . ARG   A 1 175 ? -7.19398  34.16384 14.68231 1.000 37.45967  ? 182 ARG   A CD  1 
ATOM   1284 N NE  . ARG   A 1 175 ? -8.17952  34.26308 15.75252 1.000 35.61053  ? 182 ARG   A NE  1 
ATOM   1285 C CZ  . ARG   A 1 175 ? -9.49166  34.28840 15.56344 1.000 41.48391  ? 182 ARG   A CZ  1 
ATOM   1286 N NH1 . ARG   A 1 175 ? -10.01640 34.22257 14.35111 1.000 37.41532  ? 182 ARG   A NH1 1 
ATOM   1287 N NH2 . ARG   A 1 175 ? -10.29740 34.38194 16.61746 1.000 36.73276  ? 182 ARG   A NH2 1 
ATOM   1288 N N   . GLY   A 1 176 ? -5.66886  30.60478 17.06714 1.000 34.88709  ? 183 GLY   A N   1 
ATOM   1289 C CA  . GLY   A 1 176 ? -5.48937  30.72288 18.49490 1.000 32.92894  ? 183 GLY   A CA  1 
ATOM   1290 C C   . GLY   A 1 176 ? -4.28596  29.93580 18.95792 1.000 38.70517  ? 183 GLY   A C   1 
ATOM   1291 O O   . GLY   A 1 176 ? -3.42128  29.55416 18.16107 1.000 37.02194  ? 183 GLY   A O   1 
ATOM   1292 N N   . THR   A 1 177 ? -4.23709  29.68770 20.26515 1.000 33.08860  ? 184 THR   A N   1 
ATOM   1293 C CA  . THR   A 1 177 ? -3.11448  29.00454 20.88848 1.000 31.87381  ? 184 THR   A CA  1 
ATOM   1294 C C   . THR   A 1 177 ? -3.62827  28.04395 21.94907 1.000 40.27869  ? 184 THR   A C   1 
ATOM   1295 O O   . THR   A 1 177 ? -4.50894  28.39155 22.74118 1.000 38.15596  ? 184 THR   A O   1 
ATOM   1296 C CB  . THR   A 1 177 ? -2.13142  30.00299 21.51579 1.000 38.20603  ? 184 THR   A CB  1 
ATOM   1297 O OG1 . THR   A 1 177 ? -1.60175  30.85632 20.49447 1.000 36.72407  ? 184 THR   A OG1 1 
ATOM   1298 C CG2 . THR   A 1 177 ? -0.98633  29.27354 22.20583 1.000 35.75695  ? 184 THR   A CG2 1 
ATOM   1299 N N   . LYS   A 1 178 ? -3.07513  26.83348 21.94988 1.000 35.04499  ? 185 LYS   A N   1 
ATOM   1300 C CA  . LYS   A 1 178 ? -3.39001  25.80600 22.93368 1.000 38.09584  ? 185 LYS   A CA  1 
ATOM   1301 C C   . LYS   A 1 178 ? -2.12265  25.47883 23.70951 1.000 38.17065  ? 185 LYS   A C   1 
ATOM   1302 O O   . LYS   A 1 178 ? -1.13886  25.01228 23.12578 1.000 36.44772  ? 185 LYS   A O   1 
ATOM   1303 C CB  . LYS   A 1 178 ? -3.94827  24.55268 22.25644 1.000 39.46223  ? 185 LYS   A CB  1 
ATOM   1304 C CG  . LYS   A 1 178 ? -4.24673  23.41016 23.21011 1.000 49.19742  ? 185 LYS   A CG  1 
ATOM   1305 C CD  . LYS   A 1 178 ? -5.40732  22.54661 22.72520 1.000 57.44296  ? 185 LYS   A CD  1 
ATOM   1306 C CE  . LYS   A 1 178 ? -5.49600  22.50586 21.20721 1.000 58.91960  ? 185 LYS   A CE  1 
ATOM   1307 N NZ  . LYS   A 1 178 ? -4.45448  21.62078 20.61508 1.000 66.66987  ? 185 LYS   A NZ  1 
ATOM   1308 N N   . VAL   A 1 179 ? -2.14494  25.72464 25.01561 1.000 34.60258  ? 186 VAL   A N   1 
ATOM   1309 C CA  . VAL   A 1 179 ? -1.00448  25.47147 25.88940 1.000 30.80312  ? 186 VAL   A CA  1 
ATOM   1310 C C   . VAL   A 1 179 ? -1.32129  24.22877 26.71034 1.000 36.89910  ? 186 VAL   A C   1 
ATOM   1311 O O   . VAL   A 1 179 ? -2.19282  24.25746 27.58816 1.000 32.94502  ? 186 VAL   A O   1 
ATOM   1312 C CB  . VAL   A 1 179 ? -0.69716  26.67299 26.79338 1.000 34.73298  ? 186 VAL   A CB  1 
ATOM   1313 C CG1 . VAL   A 1 179 ? 0.43048   26.33550 27.75872 1.000 32.62199  ? 186 VAL   A CG1 1 
ATOM   1314 C CG2 . VAL   A 1 179 ? -0.34347  27.89497 25.95462 1.000 33.86876  ? 186 VAL   A CG2 1 
ATOM   1315 N N   . ILE   A 1 180 ? -0.61637  23.13696 26.42966 1.000 34.13392  ? 187 ILE   A N   1 
ATOM   1316 C CA  . ILE   A 1 180 ? -0.81407  21.86842 27.12136 1.000 35.29425  ? 187 ILE   A CA  1 
ATOM   1317 C C   . ILE   A 1 180 ? 0.29069   21.71231 28.15595 1.000 37.04663  ? 187 ILE   A C   1 
ATOM   1318 O O   . ILE   A 1 180 ? 1.47502   21.63619 27.80668 1.000 37.68881  ? 187 ILE   A O   1 
ATOM   1319 C CB  . ILE   A 1 180 ? -0.82298  20.68658 26.14000 1.000 37.05430  ? 187 ILE   A CB  1 
ATOM   1320 C CG1 . ILE   A 1 180 ? -1.83679  20.92931 25.02062 1.000 39.30864  ? 187 ILE   A CG1 1 
ATOM   1321 C CG2 . ILE   A 1 180 ? -1.13250  19.38831 26.87296 1.000 38.31945  ? 187 ILE   A CG2 1 
ATOM   1322 C CD1 . ILE   A 1 180 ? -1.60563  20.07265 23.79408 1.000 42.59344  ? 187 ILE   A CD1 1 
ATOM   1323 N N   . LEU   A 1 181 ? -0.09520  21.66038 29.42778 1.000 35.01599  ? 188 LEU   A N   1 
ATOM   1324 C CA  . LEU   A 1 181 ? 0.84415   21.53482 30.53622 1.000 36.78514  ? 188 LEU   A CA  1 
ATOM   1325 C C   . LEU   A 1 181 ? 0.85045   20.08952 31.01677 1.000 39.12360  ? 188 LEU   A C   1 
ATOM   1326 O O   . LEU   A 1 181 ? -0.13578  19.61537 31.58837 1.000 38.78895  ? 188 LEU   A O   1 
ATOM   1327 C CB  . LEU   A 1 181 ? 0.46892   22.48188 31.67249 1.000 37.01611  ? 188 LEU   A CB  1 
ATOM   1328 C CG  . LEU   A 1 181 ? 0.22336   23.93029 31.25876 1.000 35.64018  ? 188 LEU   A CG  1 
ATOM   1329 C CD1 . LEU   A 1 181 ? -0.38597  24.71050 32.40268 1.000 38.61826  ? 188 LEU   A CD1 1 
ATOM   1330 C CD2 . LEU   A 1 181 ? 1.52205   24.56666 30.80609 1.000 35.13861  ? 188 LEU   A CD2 1 
ATOM   1331 N N   . HIS   A 1 182 ? 1.95931   19.39257 30.78455 1.000 37.10422  ? 189 HIS   A N   1 
ATOM   1332 C CA  . HIS   A 1 182 ? 2.14955   18.04447 31.31454 1.000 42.07613  ? 189 HIS   A CA  1 
ATOM   1333 C C   . HIS   A 1 182 ? 2.65767   18.18714 32.74297 1.000 43.75300  ? 189 HIS   A C   1 
ATOM   1334 O O   . HIS   A 1 182 ? 3.85155   18.38822 32.97716 1.000 42.05154  ? 189 HIS   A O   1 
ATOM   1335 C CB  . HIS   A 1 182 ? 3.10992   17.25224 30.43574 1.000 40.12181  ? 189 HIS   A CB  1 
ATOM   1336 C CG  . HIS   A 1 182 ? 2.73641   17.25819 28.98567 1.000 41.72272  ? 189 HIS   A CG  1 
ATOM   1337 N ND1 . HIS   A 1 182 ? 2.04871   16.22347 28.38923 1.000 43.81044  ? 189 HIS   A ND1 1 
ATOM   1338 C CD2 . HIS   A 1 182 ? 2.94085   18.18184 28.01651 1.000 42.14265  ? 189 HIS   A CD2 1 
ATOM   1339 C CE1 . HIS   A 1 182 ? 1.85286   16.50543 27.11343 1.000 45.65554  ? 189 HIS   A CE1 1 
ATOM   1340 N NE2 . HIS   A 1 182 ? 2.38401   17.68835 26.86184 1.000 43.49327  ? 189 HIS   A NE2 1 
ATOM   1341 N N   . LEU   A 1 183 ? 1.74163   18.08458 33.70167 1.000 44.55658  ? 190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 183 ? 2.02536   18.48071 35.07269 1.000 42.35305  ? 190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 183 ? 3.00421   17.52570 35.74485 1.000 50.60972  ? 190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 183 ? 3.07686   16.33685 35.42086 1.000 50.03155  ? 190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 183 ? 0.73109   18.54154 35.88303 1.000 42.52968  ? 190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 183 ? -0.30303  19.57944 35.44456 1.000 41.69876  ? 190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 183 ? -1.47700  19.59357 36.40764 1.000 42.65109  ? 190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 183 ? 0.32570   20.96020 35.33846 1.000 38.01114  ? 190 LEU   A CD2 1 
ATOM   1349 N N   . LYS   A 1 184 ? 3.76094   18.06587 36.69692 1.000 48.78568  ? 191 LYS   A N   1 
ATOM   1350 C CA  . LYS   A 1 184 ? 4.61327   17.24212 37.53622 1.000 50.87473  ? 191 LYS   A CA  1 
ATOM   1351 C C   . LYS   A 1 184 ? 3.75870   16.33847 38.42109 1.000 52.93336  ? 191 LYS   A C   1 
ATOM   1352 O O   . LYS   A 1 184 ? 2.55468   16.54984 38.59306 1.000 50.14342  ? 191 LYS   A O   1 
ATOM   1353 C CB  . LYS   A 1 184 ? 5.52949   18.11593 38.39341 1.000 49.63441  ? 191 LYS   A CB  1 
ATOM   1354 C CG  . LYS   A 1 184 ? 6.43831   19.03620 37.59122 1.000 48.86420  ? 191 LYS   A CG  1 
ATOM   1355 C CD  . LYS   A 1 184 ? 7.00514   20.15143 38.45789 1.000 48.09527  ? 191 LYS   A CD  1 
ATOM   1356 C CE  . LYS   A 1 184 ? 7.98726   21.01304 37.67859 1.000 49.46595  ? 191 LYS   A CE  1 
ATOM   1357 N NZ  . LYS   A 1 184 ? 8.61512   22.06039 38.53235 1.000 55.56604  ? 191 LYS   A NZ  1 
ATOM   1358 N N   . GLU   A 1 185 ? 4.40431   15.31784 38.99058 1.000 57.14829  ? 192 GLU   A N   1 
ATOM   1359 C CA  . GLU   A 1 185 ? 3.67352   14.31035 39.75405 1.000 59.19660  ? 192 GLU   A CA  1 
ATOM   1360 C C   . GLU   A 1 185 ? 2.98454   14.91643 40.97137 1.000 56.76247  ? 192 GLU   A C   1 
ATOM   1361 O O   . GLU   A 1 185 ? 1.86124   14.52912 41.31466 1.000 56.26804  ? 192 GLU   A O   1 
ATOM   1362 C CB  . GLU   A 1 185 ? 4.62169   13.18935 40.18010 1.000 62.47279  ? 192 GLU   A CB  1 
ATOM   1363 C CG  . GLU   A 1 185 ? 4.38833   11.87292 39.45945 1.000 80.31369  ? 192 GLU   A CG  1 
ATOM   1364 C CD  . GLU   A 1 185 ? 4.77814   10.67161 40.29746 1.000 101.41610 ? 192 GLU   A CD  1 
ATOM   1365 O OE1 . GLU   A 1 185 ? 5.96777   10.55887 40.66101 1.000 95.90335  ? 192 GLU   A OE1 1 
ATOM   1366 O OE2 . GLU   A 1 185 ? 3.89417   9.83997  40.59263 1.000 119.28770 ? 192 GLU   A OE2 1 
ATOM   1367 N N   . ASP   A 1 186 ? 3.63611   15.86830 41.63379 1.000 54.63617  ? 193 ASP   A N   1 
ATOM   1368 C CA  . ASP   A 1 186 ? 3.12110   16.45265 42.86417 1.000 55.04173  ? 193 ASP   A CA  1 
ATOM   1369 C C   . ASP   A 1 186 ? 2.28966   17.70816 42.62887 1.000 53.63220  ? 193 ASP   A C   1 
ATOM   1370 O O   . ASP   A 1 186 ? 1.96770   18.41047 43.59256 1.000 54.36672  ? 193 ASP   A O   1 
ATOM   1371 C CB  . ASP   A 1 186 ? 4.27719   16.77096 43.81594 1.000 60.63751  ? 193 ASP   A CB  1 
ATOM   1372 C CG  . ASP   A 1 186 ? 5.29211   17.71757 43.20397 1.000 71.12419  ? 193 ASP   A CG  1 
ATOM   1373 O OD1 . ASP   A 1 186 ? 5.34537   17.81244 41.95945 1.000 60.57821  ? 193 ASP   A OD1 1 
ATOM   1374 O OD2 . ASP   A 1 186 ? 6.03717   18.36689 43.96782 1.000 81.20739  ? 193 ASP   A OD2 1 
ATOM   1375 N N   . GLN   A 1 187 ? 1.93121   18.00537 41.38040 1.000 52.34930  ? 194 GLN   A N   1 
ATOM   1376 C CA  . GLN   A 1 187 ? 1.19728   19.22042 41.04701 1.000 51.97148  ? 194 GLN   A CA  1 
ATOM   1377 C C   . GLN   A 1 187 ? -0.17536  18.90841 40.45868 1.000 49.01358  ? 194 GLN   A C   1 
ATOM   1378 O O   . GLN   A 1 187 ? -0.71447  19.69213 39.67492 1.000 47.51713  ? 194 GLN   A O   1 
ATOM   1379 C CB  . GLN   A 1 187 ? 2.00583   20.09021 40.08479 1.000 47.96038  ? 194 GLN   A CB  1 
ATOM   1380 C CG  . GLN   A 1 187 ? 3.38180   20.48064 40.60451 1.000 49.70201  ? 194 GLN   A CG  1 
ATOM   1381 C CD  . GLN   A 1 187 ? 3.31665   21.28757 41.88659 1.000 49.73717  ? 194 GLN   A CD  1 
ATOM   1382 O OE1 . GLN   A 1 187 ? 2.41375   22.10288 42.07643 1.000 50.13867  ? 194 GLN   A OE1 1 
ATOM   1383 N NE2 . GLN   A 1 187 ? 4.27913   21.06554 42.77432 1.000 52.07382  ? 194 GLN   A NE2 1 
ATOM   1384 N N   . THR   A 1 188 ? -0.75706  17.76924 40.83520 1.000 48.66252  ? 195 THR   A N   1 
ATOM   1385 C CA  . THR   A 1 188 ? -2.05651  17.37259 40.30823 1.000 51.99541  ? 195 THR   A CA  1 
ATOM   1386 C C   . THR   A 1 188 ? -3.21402  18.15156 40.91942 1.000 52.04847  ? 195 THR   A C   1 
ATOM   1387 O O   . THR   A 1 188 ? -4.35363  17.98043 40.47339 1.000 51.98337  ? 195 THR   A O   1 
ATOM   1388 C CB  . THR   A 1 188 ? -2.28298  15.87416 40.52693 1.000 51.83339  ? 195 THR   A CB  1 
ATOM   1389 O OG1 . THR   A 1 188 ? -2.27885  15.58729 41.93092 1.000 56.22682  ? 195 THR   A OG1 1 
ATOM   1390 C CG2 . THR   A 1 188 ? -1.18887  15.06626 39.84440 1.000 52.59122  ? 195 THR   A CG2 1 
ATOM   1391 N N   . GLU   A 1 189 ? -2.95704  18.99562 41.92226 1.000 51.56053  ? 196 GLU   A N   1 
ATOM   1392 C CA  . GLU   A 1 189 ? -4.02495  19.79792 42.50778 1.000 50.97493  ? 196 GLU   A CA  1 
ATOM   1393 C C   . GLU   A 1 189 ? -4.62628  20.77216 41.50461 1.000 51.41098  ? 196 GLU   A C   1 
ATOM   1394 O O   . GLU   A 1 189 ? -5.77854  21.18573 41.67174 1.000 50.49693  ? 196 GLU   A O   1 
ATOM   1395 C CB  . GLU   A 1 189 ? -3.50508  20.56316 43.72643 1.000 52.81908  ? 196 GLU   A CB  1 
ATOM   1396 C CG  . GLU   A 1 189 ? -2.70636  21.81092 43.38092 1.000 49.84995  ? 196 GLU   A CG  1 
ATOM   1397 C CD  . GLU   A 1 189 ? -2.01932  22.41768 44.58631 1.000 60.10349  ? 196 GLU   A CD  1 
ATOM   1398 O OE1 . GLU   A 1 189 ? -0.98298  21.87167 45.01838 1.000 63.02317  ? 196 GLU   A OE1 1 
ATOM   1399 O OE2 . GLU   A 1 189 ? -2.51623  23.44150 45.10093 1.000 54.93372  ? 196 GLU   A OE2 1 
ATOM   1400 N N   . TYR   A 1 190 ? -3.87910  21.14129 40.46727 1.000 45.03047  ? 197 TYR   A N   1 
ATOM   1401 C CA  . TYR   A 1 190 ? -4.35883  22.06247 39.44839 1.000 47.99636  ? 197 TYR   A CA  1 
ATOM   1402 C C   . TYR   A 1 190 ? -5.20462  21.37171 38.38869 1.000 46.85678  ? 197 TYR   A C   1 
ATOM   1403 O O   . TYR   A 1 190 ? -5.57784  22.00602 37.39613 1.000 44.42975  ? 197 TYR   A O   1 
ATOM   1404 C CB  . TYR   A 1 190 ? -3.16995  22.78818 38.81626 1.000 45.25884  ? 197 TYR   A CB  1 
ATOM   1405 C CG  . TYR   A 1 190 ? -2.33189  23.50291 39.85185 1.000 48.10962  ? 197 TYR   A CG  1 
ATOM   1406 C CD1 . TYR   A 1 190 ? -2.81489  24.63091 40.50108 1.000 48.89003  ? 197 TYR   A CD1 1 
ATOM   1407 C CD2 . TYR   A 1 190 ? -1.07686  23.02924 40.20942 1.000 48.66401  ? 197 TYR   A CD2 1 
ATOM   1408 C CE1 . TYR   A 1 190 ? -2.06286  25.28266 41.45968 1.000 49.84520  ? 197 TYR   A CE1 1 
ATOM   1409 C CE2 . TYR   A 1 190 ? -0.31738  23.67372 41.16887 1.000 48.54296  ? 197 TYR   A CE2 1 
ATOM   1410 C CZ  . TYR   A 1 190 ? -0.81517  24.80029 41.78978 1.000 48.59536  ? 197 TYR   A CZ  1 
ATOM   1411 O OH  . TYR   A 1 190 ? -0.06361  25.44574 42.74473 1.000 48.35991  ? 197 TYR   A OH  1 
ATOM   1412 N N   . LEU   A 1 191 ? -5.50529  20.08788 38.57948 1.000 46.43670  ? 198 LEU   A N   1 
ATOM   1413 C CA  . LEU   A 1 191 ? -6.51865  19.39391 37.80135 1.000 47.04410  ? 198 LEU   A CA  1 
ATOM   1414 C C   . LEU   A 1 191 ? -7.86271  19.34655 38.51316 1.000 51.14027  ? 198 LEU   A C   1 
ATOM   1415 O O   . LEU   A 1 191 ? -8.84383  18.87891 37.92495 1.000 51.51469  ? 198 LEU   A O   1 
ATOM   1416 C CB  . LEU   A 1 191 ? -6.05795  17.96601 37.48127 1.000 47.64444  ? 198 LEU   A CB  1 
ATOM   1417 C CG  . LEU   A 1 191 ? -4.73793  17.84914 36.71719 1.000 47.81647  ? 198 LEU   A CG  1 
ATOM   1418 C CD1 . LEU   A 1 191 ? -4.31570  16.39356 36.59147 1.000 52.05811  ? 198 LEU   A CD1 1 
ATOM   1419 C CD2 . LEU   A 1 191 ? -4.85443  18.50068 35.34998 1.000 45.15680  ? 198 LEU   A CD2 1 
ATOM   1420 N N   . GLU   A 1 192 ? -7.92575  19.81875 39.75607 1.000 49.58265  ? 199 GLU   A N   1 
ATOM   1421 C CA  . GLU   A 1 192 ? -9.16543  19.82507 40.51682 1.000 54.62354  ? 199 GLU   A CA  1 
ATOM   1422 C C   . GLU   A 1 192 ? -10.03608 21.00090 40.09697 1.000 53.09653  ? 199 GLU   A C   1 
ATOM   1423 O O   . GLU   A 1 192 ? -9.53707  22.09670 39.82619 1.000 51.35689  ? 199 GLU   A O   1 
ATOM   1424 C CB  . GLU   A 1 192 ? -8.87151  19.90344 42.01529 1.000 58.75695  ? 199 GLU   A CB  1 
ATOM   1425 C CG  . GLU   A 1 192 ? -8.17539  18.67946 42.58740 1.000 62.38732  ? 199 GLU   A CG  1 
ATOM   1426 C CD  . GLU   A 1 192 ? -9.07600  17.46324 42.63113 1.000 79.87069  ? 199 GLU   A CD  1 
ATOM   1427 O OE1 . GLU   A 1 192 ? -10.25894 17.60989 43.00388 1.000 100.88641 ? 199 GLU   A OE1 1 
ATOM   1428 O OE2 . GLU   A 1 192 ? -8.60051  16.35863 42.29625 1.000 80.98586  ? 199 GLU   A OE2 1 
ATOM   1429 N N   . GLU   A 1 193 ? -11.34841 20.76628 40.04891 1.000 55.14450  ? 200 GLU   A N   1 
ATOM   1430 C CA  . GLU   A 1 193 ? -12.27232 21.80756 39.61053 1.000 56.30981  ? 200 GLU   A CA  1 
ATOM   1431 C C   . GLU   A 1 193 ? -12.29802 22.97357 40.59213 1.000 54.77785  ? 200 GLU   A C   1 
ATOM   1432 O O   . GLU   A 1 193 ? -12.18479 24.13801 40.19110 1.000 51.28486  ? 200 GLU   A O   1 
ATOM   1433 C CB  . GLU   A 1 193 ? -13.67308 21.22135 39.43179 1.000 61.40207  ? 200 GLU   A CB  1 
ATOM   1434 C CG  . GLU   A 1 193 ? -14.79682 22.23408 39.58522 1.000 70.16626  ? 200 GLU   A CG  1 
ATOM   1435 C CD  . GLU   A 1 193 ? -16.12860 21.70323 39.09434 1.000 87.17216  ? 200 GLU   A CD  1 
ATOM   1436 O OE1 . GLU   A 1 193 ? -16.96876 22.51587 38.65350 1.000 97.08407  ? 200 GLU   A OE1 1 
ATOM   1437 O OE2 . GLU   A 1 193 ? -16.33473 20.47239 39.14830 1.000 75.92206  ? 200 GLU   A OE2 1 
ATOM   1438 N N   . ARG   A 1 194 ? -12.44429 22.68104 41.88705 1.000 55.04276  ? 201 ARG   A N   1 
ATOM   1439 C CA  . ARG   A 1 194 ? -12.53725 23.74704 42.87768 1.000 56.35126  ? 201 ARG   A CA  1 
ATOM   1440 C C   . ARG   A 1 194 ? -11.22046 24.49123 43.05656 1.000 55.68922  ? 201 ARG   A C   1 
ATOM   1441 O O   . ARG   A 1 194 ? -11.23365 25.65220 43.47935 1.000 52.82598  ? 201 ARG   A O   1 
ATOM   1442 C CB  . ARG   A 1 194 ? -13.01560 23.18379 44.21802 1.000 60.31653  ? 201 ARG   A CB  1 
ATOM   1443 C CG  . ARG   A 1 194 ? -12.06899 22.18780 44.86026 1.000 73.09638  ? 201 ARG   A CG  1 
ATOM   1444 C CD  . ARG   A 1 194 ? -12.68238 21.59200 46.11555 1.000 80.43341  ? 201 ARG   A CD  1 
ATOM   1445 N NE  . ARG   A 1 194 ? -11.81554 20.59429 46.73078 1.000 103.53578 ? 201 ARG   A NE  1 
ATOM   1446 C CZ  . ARG   A 1 194 ? -12.13304 19.88874 47.80778 1.000 108.76078 ? 201 ARG   A CZ  1 
ATOM   1447 N NH1 . ARG   A 1 194 ? -13.29809 20.04185 48.41596 1.000 101.76221 ? 201 ARG   A NH1 1 
ATOM   1448 N NH2 . ARG   A 1 194 ? -11.25939 19.00807 48.28739 1.000 116.87224 ? 201 ARG   A NH2 1 
ATOM   1449 N N   . ARG   A 1 195 ? -10.08858 23.85783 42.74040 1.000 53.25020  ? 202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 195 ? -8.81062  24.55854 42.81718 1.000 53.01373  ? 202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 195 ? -8.64930  25.53691 41.66084 1.000 49.73901  ? 202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 195 ? -8.17781  26.66348 41.85499 1.000 49.86525  ? 202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 195 ? -7.65730  23.55610 42.83417 1.000 53.15208  ? 202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 195 ? -6.28065  24.19565 42.95080 1.000 52.05763  ? 202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 195 ? -6.01221  24.68607 44.36554 1.000 55.42657  ? 202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 195 ? -4.62926  25.11502 44.53898 1.000 54.30798  ? 202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 195 ? -4.24570  26.37791 44.66930 1.000 55.21108  ? 202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 195 ? -5.12038  27.37052 44.66319 1.000 54.62470  ? 202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 195 ? -2.95156  26.65195 44.80863 1.000 53.23571  ? 202 ARG   A NH2 1 
ATOM   1460 N N   . ILE   A 1 196 ? -9.03267  25.12399 40.45031 1.000 49.17582  ? 203 ILE   A N   1 
ATOM   1461 C CA  . ILE   A 1 196 ? -8.95553  26.02007 39.29963 1.000 47.70233  ? 203 ILE   A CA  1 
ATOM   1462 C C   . ILE   A 1 196 ? -9.90158  27.20013 39.48136 1.000 47.68707  ? 203 ILE   A C   1 
ATOM   1463 O O   . ILE   A 1 196 ? -9.56672  28.34188 39.14191 1.000 45.63476  ? 203 ILE   A O   1 
ATOM   1464 C CB  . ILE   A 1 196 ? -9.25263  25.24831 37.99992 1.000 46.29820  ? 203 ILE   A CB  1 
ATOM   1465 C CG1 . ILE   A 1 196 ? -8.20016  24.16256 37.76697 1.000 43.95109  ? 203 ILE   A CG1 1 
ATOM   1466 C CG2 . ILE   A 1 196 ? -9.30524  26.19548 36.81113 1.000 41.55133  ? 203 ILE   A CG2 1 
ATOM   1467 C CD1 . ILE   A 1 196 ? -8.62356  23.11116 36.76090 1.000 44.75452  ? 203 ILE   A CD1 1 
ATOM   1468 N N   . LYS   A 1 197 ? -11.09391 26.94636 40.02834 1.000 48.79748  ? 204 LYS   A N   1 
ATOM   1469 C CA  . LYS   A 1 197 ? -12.05173 28.02480 40.25444 1.000 49.53014  ? 204 LYS   A CA  1 
ATOM   1470 C C   . LYS   A 1 197 ? -11.50592 29.05240 41.23735 1.000 50.60866  ? 204 LYS   A C   1 
ATOM   1471 O O   . LYS   A 1 197 ? -11.67459 30.26185 41.04125 1.000 50.06274  ? 204 LYS   A O   1 
ATOM   1472 C CB  . LYS   A 1 197 ? -13.37467 27.45376 40.76395 1.000 50.37300  ? 204 LYS   A CB  1 
ATOM   1473 C CG  . LYS   A 1 197 ? -14.32812 27.00287 39.67227 1.000 57.70461  ? 204 LYS   A CG  1 
ATOM   1474 C CD  . LYS   A 1 197 ? -15.74757 26.89343 40.20601 1.000 73.80799  ? 204 LYS   A CD  1 
ATOM   1475 C CE  . LYS   A 1 197 ? -16.47884 25.70749 39.60231 1.000 80.63260  ? 204 LYS   A CE  1 
ATOM   1476 N NZ  . LYS   A 1 197 ? -17.37100 25.04808 40.59558 1.000 83.54985  ? 204 LYS   A NZ  1 
ATOM   1477 N N   . GLU   A 1 198 ? -10.84941 28.58840 42.30322 1.000 50.77960  ? 205 GLU   A N   1 
ATOM   1478 C CA  . GLU   A 1 198 ? -10.29587 29.50743 43.29230 1.000 52.55904  ? 205 GLU   A CA  1 
ATOM   1479 C C   . GLU   A 1 198 ? -9.19023  30.36558 42.69025 1.000 51.81853  ? 205 GLU   A C   1 
ATOM   1480 O O   . GLU   A 1 198 ? -9.09524  31.56329 42.98189 1.000 53.90179  ? 205 GLU   A O   1 
ATOM   1481 C CB  . GLU   A 1 198 ? -9.77564  28.72300 44.49803 1.000 56.15374  ? 205 GLU   A CB  1 
ATOM   1482 C CG  . GLU   A 1 198 ? -8.82781  29.50139 45.39805 1.000 59.14484  ? 205 GLU   A CG  1 
ATOM   1483 C CD  . GLU   A 1 198 ? -8.17746  28.62679 46.45248 1.000 77.01576  ? 205 GLU   A CD  1 
ATOM   1484 O OE1 . GLU   A 1 198 ? -7.61252  27.57569 46.08387 1.000 74.24149  ? 205 GLU   A OE1 1 
ATOM   1485 O OE2 . GLU   A 1 198 ? -8.22779  28.99052 47.64688 1.000 64.73631  ? 205 GLU   A OE2 1 
ATOM   1486 N N   . ILE   A 1 199 ? -8.35083  29.77338 41.83859 1.000 50.73081  ? 206 ILE   A N   1 
ATOM   1487 C CA  . ILE   A 1 199 ? -7.25014  30.52183 41.23991 1.000 52.22772  ? 206 ILE   A CA  1 
ATOM   1488 C C   . ILE   A 1 199 ? -7.77784  31.56371 40.26082 1.000 52.60699  ? 206 ILE   A C   1 
ATOM   1489 O O   . ILE   A 1 199 ? -7.30204  32.70550 40.23263 1.000 56.32097  ? 206 ILE   A O   1 
ATOM   1490 C CB  . ILE   A 1 199 ? -6.25815  29.55714 40.56533 1.000 49.17466  ? 206 ILE   A CB  1 
ATOM   1491 C CG1 . ILE   A 1 199 ? -5.62668  28.63331 41.60752 1.000 51.11837  ? 206 ILE   A CG1 1 
ATOM   1492 C CG2 . ILE   A 1 199 ? -5.18121  30.32897 39.81714 1.000 51.21260  ? 206 ILE   A CG2 1 
ATOM   1493 C CD1 . ILE   A 1 199 ? -4.88223  27.46300 41.01187 1.000 50.55242  ? 206 ILE   A CD1 1 
ATOM   1494 N N   . VAL   A 1 200 ? -8.77049  31.19283 39.44889 1.000 49.80561  ? 207 VAL   A N   1 
ATOM   1495 C CA  . VAL   A 1 200 ? -9.31544  32.12279 38.46408 1.000 51.90326  ? 207 VAL   A CA  1 
ATOM   1496 C C   . VAL   A 1 200 ? -10.02375 33.28268 39.15391 1.000 55.07685  ? 207 VAL   A C   1 
ATOM   1497 O O   . VAL   A 1 200 ? -9.87458  34.44400 38.75550 1.000 56.52694  ? 207 VAL   A O   1 
ATOM   1498 C CB  . VAL   A 1 200 ? -10.25099 31.37896 37.49328 1.000 50.13926  ? 207 VAL   A CB  1 
ATOM   1499 C CG1 . VAL   A 1 200 ? -11.01501 32.36480 36.62244 1.000 49.84829  ? 207 VAL   A CG1 1 
ATOM   1500 C CG2 . VAL   A 1 200 ? -9.45494  30.41120 36.63307 1.000 45.73003  ? 207 VAL   A CG2 1 
ATOM   1501 N N   . LYS   A 1 201 ? -10.80031 32.99138 40.19953 1.000 55.05291  ? 208 LYS   A N   1 
ATOM   1502 C CA  . LYS   A 1 201 ? -11.48812 34.05251 40.92852 1.000 58.30382  ? 208 LYS   A CA  1 
ATOM   1503 C C   . LYS   A 1 201 ? -10.49745 34.96712 41.64020 1.000 61.19588  ? 208 LYS   A C   1 
ATOM   1504 O O   . LYS   A 1 201 ? -10.71489 36.18149 41.72835 1.000 65.60067  ? 208 LYS   A O   1 
ATOM   1505 C CB  . LYS   A 1 201 ? -12.47321 33.44185 41.92646 1.000 56.25572  ? 208 LYS   A CB  1 
ATOM   1506 C CG  . LYS   A 1 201 ? -13.05256 34.42888 42.92752 1.000 65.72385  ? 208 LYS   A CG  1 
ATOM   1507 C CD  . LYS   A 1 201 ? -14.05438 33.75390 43.85055 1.000 73.86206  ? 208 LYS   A CD  1 
ATOM   1508 C CE  . LYS   A 1 201 ? -15.32269 34.57918 43.99272 1.000 83.04219  ? 208 LYS   A CE  1 
ATOM   1509 N NZ  . LYS   A 1 201 ? -16.44138 34.02085 43.18347 1.000 88.12291  ? 208 LYS   A NZ  1 
ATOM   1510 N N   . LYS   A 1 202 ? -9.39580  34.40467 42.13874 1.000 62.75019  ? 209 LYS   A N   1 
ATOM   1511 C CA  . LYS   A 1 202 ? -8.43619  35.18497 42.91211 1.000 63.18352  ? 209 LYS   A CA  1 
ATOM   1512 C C   . LYS   A 1 202 ? -7.52978  36.02349 42.01739 1.000 66.84376  ? 209 LYS   A C   1 
ATOM   1513 O O   . LYS   A 1 202 ? -7.17528  37.15235 42.37518 1.000 69.41631  ? 209 LYS   A O   1 
ATOM   1514 C CB  . LYS   A 1 202 ? -7.60379  34.25055 43.79301 1.000 68.58151  ? 209 LYS   A CB  1 
ATOM   1515 C CG  . LYS   A 1 202 ? -6.49313  34.92515 44.58030 1.000 71.60713  ? 209 LYS   A CG  1 
ATOM   1516 C CD  . LYS   A 1 202 ? -5.68623  33.89680 45.35983 1.000 72.37394  ? 209 LYS   A CD  1 
ATOM   1517 C CE  . LYS   A 1 202 ? -4.55593  34.54577 46.14061 1.000 76.07134  ? 209 LYS   A CE  1 
ATOM   1518 N NZ  . LYS   A 1 202 ? -3.83287  33.55570 46.98691 1.000 73.22754  ? 209 LYS   A NZ  1 
ATOM   1519 N N   . HIS   A 1 203 ? -7.15265  35.49896 40.84938 1.000 65.99894  ? 210 HIS   A N   1 
ATOM   1520 C CA  . HIS   A 1 203 ? -6.15778  36.14584 40.00643 1.000 68.03294  ? 210 HIS   A CA  1 
ATOM   1521 C C   . HIS   A 1 203 ? -6.69899  36.68861 38.69182 1.000 63.68807  ? 210 HIS   A C   1 
ATOM   1522 O O   . HIS   A 1 203 ? -6.08619  37.59907 38.12584 1.000 65.46161  ? 210 HIS   A O   1 
ATOM   1523 C CB  . HIS   A 1 203 ? -5.01593  35.16902 39.68789 1.000 68.78414  ? 210 HIS   A CB  1 
ATOM   1524 C CG  . HIS   A 1 203 ? -4.24075  34.72404 40.88891 1.000 77.56261  ? 210 HIS   A CG  1 
ATOM   1525 N ND1 . HIS   A 1 203 ? -3.35767  35.54784 41.55272 1.000 75.45692  ? 210 HIS   A ND1 1 
ATOM   1526 C CD2 . HIS   A 1 203 ? -4.20721  33.53587 41.53766 1.000 72.00098  ? 210 HIS   A CD2 1 
ATOM   1527 C CE1 . HIS   A 1 203 ? -2.81811  34.88863 42.56275 1.000 73.40265  ? 210 HIS   A CE1 1 
ATOM   1528 N NE2 . HIS   A 1 203 ? -3.31664  33.66571 42.57565 1.000 70.34162  ? 210 HIS   A NE2 1 
ATOM   1529 N N   . SER   A 1 204 ? -7.81612  36.16176 38.18900 1.000 62.82247  ? 211 SER   A N   1 
ATOM   1530 C CA  . SER   A 1 204 ? -8.26539  36.47844 36.83789 1.000 65.57778  ? 211 SER   A CA  1 
ATOM   1531 C C   . SER   A 1 204 ? -9.73267  36.89184 36.80914 1.000 65.44214  ? 211 SER   A C   1 
ATOM   1532 O O   . SER   A 1 204 ? -10.44137 36.61097 35.83911 1.000 65.34740  ? 211 SER   A O   1 
ATOM   1533 C CB  . SER   A 1 204 ? -8.02980  35.29265 35.90225 1.000 61.22361  ? 211 SER   A CB  1 
ATOM   1534 O OG  . SER   A 1 204 ? -6.65459  34.95471 35.84461 1.000 63.26542  ? 211 SER   A OG  1 
ATOM   1535 N N   . GLN   A 1 205 ? -10.20463 37.56931 37.85675 1.000 69.83493  ? 212 GLN   A N   1 
ATOM   1536 C CA  . GLN   A 1 205 ? -11.60313 37.97909 37.90179 1.000 78.14168  ? 212 GLN   A CA  1 
ATOM   1537 C C   . GLN   A 1 205 ? -11.90811 39.15831 36.98716 1.000 75.39951  ? 212 GLN   A C   1 
ATOM   1538 O O   . GLN   A 1 205 ? -13.08601 39.47932 36.79665 1.000 77.18857  ? 212 GLN   A O   1 
ATOM   1539 C CB  . GLN   A 1 205 ? -12.00626 38.33034 39.33563 1.000 76.23322  ? 212 GLN   A CB  1 
ATOM   1540 C CG  . GLN   A 1 205 ? -10.94226 39.08077 40.11764 1.000 81.28399  ? 212 GLN   A CG  1 
ATOM   1541 C CD  . GLN   A 1 205 ? -11.49418 39.73503 41.36934 1.000 97.27342  ? 212 GLN   A CD  1 
ATOM   1542 O OE1 . GLN   A 1 205 ? -12.70665 39.77669 41.57905 1.000 106.09317 ? 212 GLN   A OE1 1 
ATOM   1543 N NE2 . GLN   A 1 205 ? -10.60426 40.25237 42.20836 1.000 97.73366  ? 212 GLN   A NE2 1 
ATOM   1544 N N   . PHE   A 1 206 ? -10.89078 39.80377 36.41600 1.000 81.83677  ? 213 PHE   A N   1 
ATOM   1545 C CA  . PHE   A 1 206 ? -11.07854 41.00165 35.60600 1.000 72.51928  ? 213 PHE   A CA  1 
ATOM   1546 C C   . PHE   A 1 206 ? -10.57637 40.80928 34.17789 1.000 69.36059  ? 213 PHE   A C   1 
ATOM   1547 O O   . PHE   A 1 206 ? -10.07151 41.74773 33.55856 1.000 66.84104  ? 213 PHE   A O   1 
ATOM   1548 C CB  . PHE   A 1 206 ? -10.39157 42.20040 36.25756 1.000 75.33737  ? 213 PHE   A CB  1 
ATOM   1549 C CG  . PHE   A 1 206 ? -10.90578 42.51862 37.63173 1.000 76.33236  ? 213 PHE   A CG  1 
ATOM   1550 C CD1 . PHE   A 1 206 ? -12.26283 42.47179 37.90580 1.000 77.60127  ? 213 PHE   A CD1 1 
ATOM   1551 C CD2 . PHE   A 1 206 ? -10.03257 42.86294 38.65011 1.000 80.10336  ? 213 PHE   A CD2 1 
ATOM   1552 C CE1 . PHE   A 1 206 ? -12.73982 42.76469 39.16941 1.000 81.85277  ? 213 PHE   A CE1 1 
ATOM   1553 C CE2 . PHE   A 1 206 ? -10.50320 43.15673 39.91590 1.000 81.72493  ? 213 PHE   A CE2 1 
ATOM   1554 C CZ  . PHE   A 1 206 ? -11.85858 43.10757 40.17569 1.000 79.33814  ? 213 PHE   A CZ  1 
ATOM   1555 N N   . ILE   A 1 207 ? -10.70972 39.60045 33.64381 1.000 63.82877  ? 214 ILE   A N   1 
ATOM   1556 C CA  . ILE   A 1 207 ? -10.34273 39.31367 32.26205 1.000 56.35868  ? 214 ILE   A CA  1 
ATOM   1557 C C   . ILE   A 1 207 ? -11.53854 39.62331 31.37168 1.000 53.15092  ? 214 ILE   A C   1 
ATOM   1558 O O   . ILE   A 1 207 ? -12.66378 39.19528 31.65564 1.000 56.02687  ? 214 ILE   A O   1 
ATOM   1559 C CB  . ILE   A 1 207 ? -9.89296  37.85145 32.10466 1.000 54.62523  ? 214 ILE   A CB  1 
ATOM   1560 C CG1 . ILE   A 1 207 ? -8.58015  37.61729 32.85576 1.000 53.53186  ? 214 ILE   A CG1 1 
ATOM   1561 C CG2 . ILE   A 1 207 ? -9.74650  37.48611 30.63467 1.000 47.74234  ? 214 ILE   A CG2 1 
ATOM   1562 C CD1 . ILE   A 1 207 ? -7.38677  38.31055 32.23422 1.000 49.88036  ? 214 ILE   A CD1 1 
ATOM   1563 N N   . GLY   A 1 208 ? -11.29846 40.36812 30.29451 1.000 50.66384  ? 215 GLY   A N   1 
ATOM   1564 C CA  . GLY   A 1 208 ? -12.37293 40.82961 29.43652 1.000 50.10155  ? 215 GLY   A CA  1 
ATOM   1565 C C   . GLY   A 1 208 ? -12.84496 39.82775 28.40230 1.000 49.72738  ? 215 GLY   A C   1 
ATOM   1566 O O   . GLY   A 1 208 ? -13.33289 40.21727 27.33700 1.000 47.34354  ? 215 GLY   A O   1 
ATOM   1567 N N   . TYR   A 1 209 ? -12.70998 38.53748 28.69896 1.000 45.78094  ? 216 TYR   A N   1 
ATOM   1568 C CA  . TYR   A 1 209 ? -13.16612 37.48457 27.79972 1.000 44.81953  ? 216 TYR   A CA  1 
ATOM   1569 C C   . TYR   A 1 209 ? -13.68355 36.32720 28.64080 1.000 43.55792  ? 216 TYR   A C   1 
ATOM   1570 O O   . TYR   A 1 209 ? -13.20760 36.11420 29.75540 1.000 41.91703  ? 216 TYR   A O   1 
ATOM   1571 C CB  . TYR   A 1 209 ? -12.04262 37.01277 26.86294 1.000 46.71257  ? 216 TYR   A CB  1 
ATOM   1572 C CG  . TYR   A 1 209 ? -11.49284 38.11478 25.98477 1.000 42.32887  ? 216 TYR   A CG  1 
ATOM   1573 C CD1 . TYR   A 1 209 ? -12.13478 38.47530 24.80671 1.000 42.09521  ? 216 TYR   A CD1 1 
ATOM   1574 C CD2 . TYR   A 1 209 ? -10.33700 38.79920 26.33608 1.000 43.28972  ? 216 TYR   A CD2 1 
ATOM   1575 C CE1 . TYR   A 1 209 ? -11.64081 39.48680 24.00077 1.000 44.06058  ? 216 TYR   A CE1 1 
ATOM   1576 C CE2 . TYR   A 1 209 ? -9.83454  39.81189 25.53599 1.000 42.32535  ? 216 TYR   A CE2 1 
ATOM   1577 C CZ  . TYR   A 1 209 ? -10.49102 40.15144 24.36948 1.000 41.45805  ? 216 TYR   A CZ  1 
ATOM   1578 O OH  . TYR   A 1 209 ? -9.99866  41.15751 23.56784 1.000 43.38142  ? 216 TYR   A OH  1 
ATOM   1579 N N   . PRO   A 1 210 ? -14.67082 35.57655 28.13309 1.000 42.52401  ? 217 PRO   A N   1 
ATOM   1580 C CA  . PRO   A 1 210 ? -15.22624 34.47104 28.93226 1.000 42.06608  ? 217 PRO   A CA  1 
ATOM   1581 C C   . PRO   A 1 210 ? -14.19318 33.37962 29.15388 1.000 40.05050  ? 217 PRO   A C   1 
ATOM   1582 O O   . PRO   A 1 210 ? -13.57095 32.88630 28.21019 1.000 40.57310  ? 217 PRO   A O   1 
ATOM   1583 C CB  . PRO   A 1 210 ? -16.40578 33.96785 28.08318 1.000 43.59549  ? 217 PRO   A CB  1 
ATOM   1584 C CG  . PRO   A 1 210 ? -16.25900 34.59069 26.74474 1.000 42.32734  ? 217 PRO   A CG  1 
ATOM   1585 C CD  . PRO   A 1 210 ? -15.38139 35.78936 26.86728 1.000 44.98319  ? 217 PRO   A CD  1 
ATOM   1586 N N   . ILE   A 1 211 ? -14.00427 33.01375 30.41983 1.000 40.24036  ? 218 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -13.14738 31.90220 30.81239 1.000 42.15315  ? 218 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -14.05518 30.75276 31.22270 1.000 42.14899  ? 218 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -14.81402 30.86923 32.19316 1.000 44.93627  ? 218 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -12.19310 32.28798 31.95285 1.000 42.28637  ? 218 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -11.41783 33.55863 31.59931 1.000 42.64201  ? 218 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -11.23851 31.14445 32.25369 1.000 40.81435  ? 218 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.63246 34.13332 32.75842 1.000 43.87525  ? 218 ILE   A CD1 1 
ATOM   1594 N N   . THR   A 1 212 ? -13.98345 29.64778 30.48586 1.000 39.48266  ? 219 THR   A N   1 
ATOM   1595 C CA  . THR   A 1 212 ? -14.84830 28.49426 30.70569 1.000 42.02725  ? 219 THR   A CA  1 
ATOM   1596 C C   . THR   A 1 212 ? -14.01702 27.32032 31.20637 1.000 38.45089  ? 219 THR   A C   1 
ATOM   1597 O O   . THR   A 1 212 ? -13.05467 26.90974 30.54844 1.000 39.46651  ? 219 THR   A O   1 
ATOM   1598 C CB  . THR   A 1 212 ? -15.58853 28.11204 29.42367 1.000 40.69466  ? 219 THR   A CB  1 
ATOM   1599 O OG1 . THR   A 1 212 ? -16.31662 29.24564 28.93554 1.000 39.47519  ? 219 THR   A OG1 1 
ATOM   1600 C CG2 . THR   A 1 212 ? -16.55536 26.96927 29.68778 1.000 45.10540  ? 219 THR   A CG2 1 
ATOM   1601 N N   . LEU   A 1 213 ? -14.39421 26.77992 32.36207 1.000 42.13901  ? 220 LEU   A N   1 
ATOM   1602 C CA  . LEU   A 1 213 ? -13.75512 25.59032 32.90928 1.000 43.26856  ? 220 LEU   A CA  1 
ATOM   1603 C C   . LEU   A 1 213 ? -14.50331 24.35745 32.41706 1.000 43.06029  ? 220 LEU   A C   1 
ATOM   1604 O O   . LEU   A 1 213 ? -15.71464 24.23421 32.62924 1.000 41.52464  ? 220 LEU   A O   1 
ATOM   1605 C CB  . LEU   A 1 213 ? -13.73531 25.63467 34.43690 1.000 42.88896  ? 220 LEU   A CB  1 
ATOM   1606 C CG  . LEU   A 1 213 ? -13.16013 24.40892 35.15300 1.000 49.58564  ? 220 LEU   A CG  1 
ATOM   1607 C CD1 . LEU   A 1 213 ? -11.81442 24.00379 34.56242 1.000 45.12057  ? 220 LEU   A CD1 1 
ATOM   1608 C CD2 . LEU   A 1 213 ? -13.04214 24.66390 36.64902 1.000 52.01530  ? 220 LEU   A CD2 1 
ATOM   1609 N N   . PHE   A 1 214 ? -13.78453 23.45110 31.76085 1.000 40.52314  ? 221 PHE   A N   1 
ATOM   1610 C CA  . PHE   A 1 214 ? -14.36692 22.21517 31.24964 1.000 43.69756  ? 221 PHE   A CA  1 
ATOM   1611 C C   . PHE   A 1 214 ? -14.33355 21.16843 32.35715 1.000 44.94606  ? 221 PHE   A C   1 
ATOM   1612 O O   . PHE   A 1 214 ? -13.26072 20.68361 32.73142 1.000 45.41175  ? 221 PHE   A O   1 
ATOM   1613 C CB  . PHE   A 1 214 ? -13.61294 21.73163 30.01367 1.000 44.79463  ? 221 PHE   A CB  1 
ATOM   1614 C CG  . PHE   A 1 214 ? -14.05421 22.38756 28.73531 1.000 45.96919  ? 221 PHE   A CG  1 
ATOM   1615 C CD1 . PHE   A 1 214 ? -14.21600 23.76137 28.66174 1.000 47.94324  ? 221 PHE   A CD1 1 
ATOM   1616 C CD2 . PHE   A 1 214 ? -14.30314 21.62911 27.60506 1.000 55.30364  ? 221 PHE   A CD2 1 
ATOM   1617 C CE1 . PHE   A 1 214 ? -14.62001 24.36489 27.48581 1.000 47.57976  ? 221 PHE   A CE1 1 
ATOM   1618 C CE2 . PHE   A 1 214 ? -14.70748 22.22597 26.42615 1.000 54.02466  ? 221 PHE   A CE2 1 
ATOM   1619 C CZ  . PHE   A 1 214 ? -14.86595 23.59591 26.36669 1.000 45.90641  ? 221 PHE   A CZ  1 
ATOM   1620 N N   . VAL   A 1 215 ? -15.50408 20.82347 32.88178 1.000 45.33118  ? 222 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 215 ? -15.60669 19.80762 33.92219 1.000 47.56299  ? 222 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 215 ? -15.49833 18.42941 33.28620 1.000 49.19432  ? 222 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 215 ? -16.11729 18.15428 32.25115 1.000 49.22135  ? 222 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 215 ? -16.92545 19.96453 34.70027 1.000 49.52789  ? 222 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 215 ? -17.02299 18.92387 35.80686 1.000 51.93239  ? 222 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 215 ? -17.04605 21.37199 35.26466 1.000 51.27758  ? 222 VAL   A CG2 1 
ATOM   1627 N N   . GLU   A 1 216 ? -14.70430 17.55731 33.90018 1.000 48.86137  ? 223 GLU   A N   1 
ATOM   1628 C CA  . GLU   A 1 216 ? -14.53285 16.20749 33.38713 1.000 51.26775  ? 223 GLU   A CA  1 
ATOM   1629 C C   . GLU   A 1 216 ? -15.75627 15.35464 33.69695 1.000 51.58946  ? 223 GLU   A C   1 
ATOM   1630 O O   . GLU   A 1 216 ? -16.49002 15.60480 34.65781 1.000 52.34297  ? 223 GLU   A O   1 
ATOM   1631 C CB  . GLU   A 1 216 ? -13.28304 15.55784 33.98041 1.000 53.14322  ? 223 GLU   A CB  1 
ATOM   1632 C CG  . GLU   A 1 216 ? -12.00410 16.33719 33.73234 1.000 51.81887  ? 223 GLU   A CG  1 
ATOM   1633 C CD  . GLU   A 1 216 ? -10.76698 15.46702 33.83970 1.000 54.06092  ? 223 GLU   A CD  1 
ATOM   1634 O OE1 . GLU   A 1 216 ? -10.60975 14.55477 33.00154 1.000 54.44145  ? 223 GLU   A OE1 1 
ATOM   1635 O OE2 . GLU   A 1 216 ? -9.95399  15.69108 34.76138 1.000 58.42741  ? 223 GLU   A OE2 1 
ATOM   1636 N N   . LYS   A 1 217 ? -15.96597 14.33486 32.87069 1.000 55.51403  ? 224 LYS   A N   1 
ATOM   1637 C CA  . LYS   A 1 217 ? -17.11066 13.44469 33.02181 1.000 62.60651  ? 224 LYS   A CA  1 
ATOM   1638 C C   . LYS   A 1 217 ? -16.68861 12.10017 33.60678 1.000 65.31773  ? 224 LYS   A C   1 
ATOM   1639 O O   . LYS   A 1 217 ? -16.56978 11.95154 34.82314 1.000 75.33168  ? 224 LYS   A O   1 
ATOM   1640 C CB  . LYS   A 1 217 ? -17.80662 13.23989 31.67492 1.000 61.08589  ? 224 LYS   A CB  1 
ATOM   1641 C CG  . LYS   A 1 217 ? -18.11020 14.52936 30.92932 1.000 57.72542  ? 224 LYS   A CG  1 
ATOM   1642 C CD  . LYS   A 1 217 ? -18.48442 14.25692 29.48063 1.000 55.62300  ? 224 LYS   A CD  1 
ATOM   1643 C CE  . LYS   A 1 217 ? -17.47076 13.34517 28.80739 1.000 56.48447  ? 224 LYS   A CE  1 
ATOM   1644 N NZ  . LYS   A 1 217 ? -16.24388 14.08845 28.40326 1.000 55.30701  ? 224 LYS   A NZ  1 
HETATM 1645 C C1  . A1AW9 B 2 .   ? 5.10496   35.45616 28.07621 0.973 44.42814  ? 301 A1AW9 A C1  1 
HETATM 1646 C C10 . A1AW9 B 2 .   ? 5.41448   30.00746 23.53398 0.973 48.19297  ? 301 A1AW9 A C10 1 
HETATM 1647 C C11 . A1AW9 B 2 .   ? 6.51595   30.60007 24.42128 0.973 49.10500  ? 301 A1AW9 A C11 1 
HETATM 1648 C C12 . A1AW9 B 2 .   ? 7.73428   29.82048 23.93489 0.973 47.10971  ? 301 A1AW9 A C12 1 
HETATM 1649 C C2  . A1AW9 B 2 .   ? 5.85994   36.10878 26.94522 0.973 66.23475  ? 301 A1AW9 A C2  1 
HETATM 1650 C C3  . A1AW9 B 2 .   ? 6.98822   35.26527 26.34265 0.973 50.23597  ? 301 A1AW9 A C3  1 
HETATM 1651 C C4  . A1AW9 B 2 .   ? 7.86371   36.08753 25.40853 0.973 63.77486  ? 301 A1AW9 A C4  1 
HETATM 1652 C C5  . A1AW9 B 2 .   ? 5.61078   34.04078 24.59064 0.973 64.42592  ? 301 A1AW9 A C5  1 
HETATM 1653 C C6  . A1AW9 B 2 .   ? 6.87476   32.03043 23.95860 0.973 56.29384  ? 301 A1AW9 A C6  1 
HETATM 1654 C C7  . A1AW9 B 2 .   ? 7.63933   31.77277 22.63124 0.973 54.78108  ? 301 A1AW9 A C7  1 
HETATM 1655 C C8  . A1AW9 B 2 .   ? 7.57916   30.25666 22.48220 0.973 50.24088  ? 301 A1AW9 A C8  1 
HETATM 1656 C C9  . A1AW9 B 2 .   ? 6.13045   29.85174 22.18142 0.973 47.37130  ? 301 A1AW9 A C9  1 
HETATM 1657 O O1  . A1AW9 B 2 .   ? 8.84463   35.26739 24.78798 0.973 78.14353  ? 301 A1AW9 A O1  1 
HETATM 1658 N N1  . A1AW9 B 2 .   ? 6.53349   34.09223 25.58578 0.973 61.89966  ? 301 A1AW9 A N1  1 
HETATM 1659 N N2  . A1AW9 B 2 .   ? 5.74389   32.93661 23.83475 0.973 64.78737  ? 301 A1AW9 A N2  1 
HETATM 1660 S S1  . A1AW9 B 2 .   ? 4.51280   35.22534 24.12689 0.973 96.60367  ? 301 A1AW9 A S1  1 
HETATM 1661 O O   . HOH   C 3 .   ? 7.48007   37.46362 14.64280 1.000 45.67214  ? 401 HOH   A O   1 
HETATM 1662 O O   . HOH   C 3 .   ? 7.48135   19.77018 10.61102 1.000 58.86058  ? 402 HOH   A O   1 
HETATM 1663 O O   . HOH   C 3 .   ? -5.02566  36.32018 34.96457 1.000 51.88950  ? 403 HOH   A O   1 
HETATM 1664 O O   . HOH   C 3 .   ? 13.24168  32.69134 12.87324 1.000 60.56167  ? 404 HOH   A O   1 
HETATM 1665 O O   . HOH   C 3 .   ? 10.98540  30.32261 47.70155 1.000 65.97577  ? 405 HOH   A O   1 
HETATM 1666 O O   . HOH   C 3 .   ? -11.66526 14.63142 30.88124 1.000 54.99349  ? 406 HOH   A O   1 
HETATM 1667 O O   . HOH   C 3 .   ? -10.69885 17.21456 36.44301 1.000 52.97326  ? 407 HOH   A O   1 
HETATM 1668 O O   . HOH   C 3 .   ? -3.57811  12.80820 37.01635 1.000 54.99400  ? 408 HOH   A O   1 
HETATM 1669 O O   . HOH   C 3 .   ? 10.57240  17.06286 25.68993 1.000 52.07980  ? 409 HOH   A O   1 
HETATM 1670 O O   . HOH   C 3 .   ? -8.66456  41.19894 29.51383 1.000 51.92926  ? 410 HOH   A O   1 
HETATM 1671 O O   . HOH   C 3 .   ? -5.27807  38.20069 35.86665 1.000 59.38617  ? 411 HOH   A O   1 
HETATM 1672 O O   . HOH   C 3 .   ? 1.40124   23.78466 43.91037 1.000 51.70125  ? 412 HOH   A O   1 
HETATM 1673 O O   . HOH   C 3 .   ? -3.70415  29.97154 47.27343 1.000 63.98104  ? 413 HOH   A O   1 
HETATM 1674 O O   . HOH   C 3 .   ? -14.94548 44.96329 20.63968 1.000 68.47384  ? 414 HOH   A O   1 
HETATM 1675 O O   . HOH   C 3 .   ? -15.41787 17.33545 29.96015 1.000 47.74971  ? 415 HOH   A O   1 
HETATM 1676 O O   . HOH   C 3 .   ? -17.95227 24.54777 33.80662 1.000 40.87596  ? 416 HOH   A O   1 
HETATM 1677 O O   . HOH   C 3 .   ? -14.75539 30.43342 27.30754 1.000 39.31158  ? 417 HOH   A O   1 
HETATM 1678 O O   . HOH   C 3 .   ? 11.59233  31.05154 24.02071 1.000 48.30506  ? 418 HOH   A O   1 
HETATM 1679 O O   . HOH   C 3 .   ? -5.79383  31.08222 11.25440 1.000 42.85010  ? 419 HOH   A O   1 
HETATM 1680 O O   . HOH   C 3 .   ? -1.44614  33.00248 45.01141 1.000 62.45484  ? 420 HOH   A O   1 
HETATM 1681 O O   . HOH   C 3 .   ? 17.15540  25.42973 31.12513 1.000 48.22780  ? 421 HOH   A O   1 
HETATM 1682 O O   . HOH   C 3 .   ? -5.77221  18.74717 29.06694 1.000 41.19841  ? 422 HOH   A O   1 
HETATM 1683 O O   . HOH   C 3 .   ? -11.64360 19.09192 31.41896 1.000 47.98597  ? 423 HOH   A O   1 
HETATM 1684 O O   . HOH   C 3 .   ? -5.26910  41.60349 28.04650 1.000 41.55132  ? 424 HOH   A O   1 
HETATM 1685 O O   . HOH   C 3 .   ? -4.14568  35.42869 13.40735 1.000 40.88277  ? 425 HOH   A O   1 
HETATM 1686 O O   . HOH   C 3 .   ? 14.01104  19.44160 23.06130 1.000 45.47825  ? 426 HOH   A O   1 
HETATM 1687 O O   . HOH   C 3 .   ? -14.60130 14.21585 30.62911 1.000 55.31449  ? 427 HOH   A O   1 
HETATM 1688 O O   . HOH   C 3 .   ? 11.31384  18.63777 32.50818 1.000 50.74426  ? 428 HOH   A O   1 
HETATM 1689 O O   . HOH   C 3 .   ? -9.34469  12.25375 32.88229 1.000 57.26133  ? 429 HOH   A O   1 
HETATM 1690 O O   . HOH   C 3 .   ? 0.62204   29.92451 12.79713 1.000 41.54707  ? 430 HOH   A O   1 
HETATM 1691 O O   . HOH   C 3 .   ? -3.50563  38.25053 8.99633  1.000 54.54805  ? 431 HOH   A O   1 
HETATM 1692 O O   . HOH   C 3 .   ? 15.26342  17.48826 15.73835 1.000 46.15937  ? 432 HOH   A O   1 
HETATM 1693 O O   . HOH   C 3 .   ? 5.87955   36.54011 12.34898 1.000 45.10378  ? 433 HOH   A O   1 
HETATM 1694 O O   . HOH   C 3 .   ? -0.50666  19.31066 43.99007 1.000 54.49487  ? 434 HOH   A O   1 
HETATM 1695 O O   . HOH   C 3 .   ? 8.12835   24.50126 8.44455  1.000 50.29395  ? 435 HOH   A O   1 
HETATM 1696 O O   . HOH   C 3 .   ? 0.82449   38.96695 33.94960 1.000 55.94932  ? 436 HOH   A O   1 
HETATM 1697 O O   . HOH   C 3 .   ? 10.75393  32.98233 19.87896 1.000 47.53627  ? 437 HOH   A O   1 
HETATM 1698 O O   . HOH   C 3 .   ? 1.60004   36.48422 17.14494 1.000 45.24753  ? 438 HOH   A O   1 
HETATM 1699 O O   . HOH   C 3 .   ? -3.29522  33.01390 20.59084 1.000 31.22682  ? 439 HOH   A O   1 
HETATM 1700 O O   . HOH   C 3 .   ? 7.28282   20.25553 18.57203 1.000 35.40496  ? 440 HOH   A O   1 
HETATM 1701 O O   . HOH   C 3 .   ? -9.29954  42.99155 27.25536 1.000 52.65988  ? 441 HOH   A O   1 
HETATM 1702 O O   . HOH   C 3 .   ? 9.80937   17.94223 21.84783 1.000 55.36437  ? 442 HOH   A O   1 
HETATM 1703 O O   . HOH   C 3 .   ? -5.84414  44.71247 10.87249 1.000 44.61123  ? 443 HOH   A O   1 
HETATM 1704 O O   . HOH   C 3 .   ? 9.46551   24.56983 40.24376 1.000 57.36019  ? 444 HOH   A O   1 
HETATM 1705 O O   . HOH   C 3 .   ? -6.76288  47.70231 13.72953 1.000 43.79771  ? 445 HOH   A O   1 
HETATM 1706 O O   . HOH   C 3 .   ? 4.11353   37.81454 30.78877 1.000 43.12890  ? 446 HOH   A O   1 
HETATM 1707 O O   . HOH   C 3 .   ? 10.87150  29.23746 21.78531 1.000 45.38712  ? 447 HOH   A O   1 
HETATM 1708 O O   . HOH   C 3 .   ? -12.91524 31.58144 17.26464 1.000 47.41073  ? 448 HOH   A O   1 
HETATM 1709 O O   . HOH   C 3 .   ? 13.19214  19.88275 26.11520 1.000 46.64808  ? 449 HOH   A O   1 
HETATM 1710 O O   . HOH   C 3 .   ? -16.02565 37.25437 23.69756 1.000 47.02709  ? 450 HOH   A O   1 
HETATM 1711 O O   . HOH   C 3 .   ? -8.01539  28.40129 9.89681  1.000 50.81722  ? 451 HOH   A O   1 
HETATM 1712 O O   . HOH   C 3 .   ? -10.33342 32.77249 45.15445 1.000 58.41486  ? 452 HOH   A O   1 
HETATM 1713 O O   . HOH   C 3 .   ? 6.58720   32.41671 10.21716 1.000 43.46148  ? 453 HOH   A O   1 
HETATM 1714 O O   . HOH   C 3 .   ? 19.61599  29.51618 36.40589 1.000 54.19737  ? 454 HOH   A O   1 
HETATM 1715 O O   . HOH   C 3 .   ? 2.10425   36.55605 31.56952 1.000 43.89863  ? 455 HOH   A O   1 
HETATM 1716 O O   . HOH   C 3 .   ? 6.92637   14.63127 37.98934 1.000 59.44820  ? 456 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? -1.81295  32.70289 24.25215 1.000 39.65296  ? 457 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? -1.99442  30.84889 27.43089 1.000 38.43996  ? 458 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? -3.42201  29.43152 25.41842 1.000 32.43267  ? 459 HOH   A O   1 
HETATM 1720 O O   . HOH   C 3 .   ? 0.25049   38.78303 29.81160 1.000 50.45583  ? 460 HOH   A O   1 
HETATM 1721 O O   . HOH   C 3 .   ? 14.70480  17.09497 20.23682 1.000 47.98856  ? 461 HOH   A O   1 
HETATM 1722 O O   . HOH   C 3 .   ? -17.23530 32.10052 23.30285 1.000 44.71747  ? 462 HOH   A O   1 
HETATM 1723 O O   . HOH   C 3 .   ? 9.74398   23.16186 11.95970 1.000 54.96113  ? 463 HOH   A O   1 
HETATM 1724 O O   . HOH   C 3 .   ? 3.12596   14.86766 32.94552 1.000 55.97081  ? 464 HOH   A O   1 
HETATM 1725 O O   . HOH   C 3 .   ? 15.35344  25.15907 29.07608 1.000 39.70808  ? 465 HOH   A O   1 
HETATM 1726 O O   . HOH   C 3 .   ? -0.53029  33.38184 21.51016 1.000 50.51295  ? 466 HOH   A O   1 
HETATM 1727 O O   . HOH   C 3 .   ? 0.54582   39.23403 14.05493 1.000 54.97638  ? 467 HOH   A O   1 
HETATM 1728 O O   . HOH   C 3 .   ? -12.47213 18.08428 40.44995 1.000 62.01363  ? 468 HOH   A O   1 
HETATM 1729 O O   . HOH   C 3 .   ? 18.40816  19.34093 25.47200 1.000 57.95998  ? 469 HOH   A O   1 
HETATM 1730 O O   . HOH   C 3 .   ? -5.23294  18.99975 25.15964 1.000 51.82332  ? 470 HOH   A O   1 
HETATM 1731 O O   . HOH   C 3 .   ? -5.93809  25.25344 11.63100 1.000 58.05959  ? 471 HOH   A O   1 
HETATM 1732 O O   . HOH   C 3 .   ? -2.11607  24.41992 8.98039  1.000 55.02730  ? 472 HOH   A O   1 
HETATM 1733 O O   . HOH   C 3 .   ? 9.55559   15.08552 29.52745 1.000 52.05005  ? 473 HOH   A O   1 
HETATM 1734 O O   . HOH   C 3 .   ? -16.81415 36.18888 21.30396 1.000 51.43643  ? 474 HOH   A O   1 
HETATM 1735 O O   . HOH   C 3 .   ? -10.61820 30.63721 16.23971 1.000 42.58125  ? 475 HOH   A O   1 
HETATM 1736 O O   . HOH   C 3 .   ? 1.41884   14.43827 31.78726 1.000 51.80782  ? 476 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 2.13765   42.94922 14.83031 1.000 58.81955  ? 477 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? 2.68502   40.79929 30.90689 1.000 61.74898  ? 478 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 0.37937   36.83251 24.57379 1.000 48.72221  ? 479 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? 0.03798   28.07317 44.94378 1.000 54.87267  ? 480 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? -16.86946 27.82695 33.75691 1.000 48.19905  ? 481 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -7.82587  27.91606 19.35478 1.000 44.58339  ? 482 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 15.74920  34.39884 19.29025 1.000 62.06685  ? 483 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -11.42987 24.43197 23.30746 1.000 42.73678  ? 484 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? -15.96478 36.34447 10.04830 1.000 66.71696  ? 485 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 4.68011   22.62010 45.41307 1.000 55.32228  ? 486 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? -12.07271 26.70090 21.30334 1.000 51.46790  ? 487 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -15.17479 34.94347 32.59934 1.000 53.97933  ? 488 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 14.79464  31.41441 23.11950 1.000 37.50737  ? 489 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? -17.95706 24.58104 36.48681 1.000 54.82974  ? 490 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? -2.44722  42.91691 23.67403 1.000 46.17943  ? 491 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? -7.40175  16.95289 27.30689 1.000 55.50645  ? 492 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? 14.57349  17.56844 30.58444 1.000 61.45415  ? 493 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -4.16531  38.00539 11.83437 1.000 40.88913  ? 494 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? -13.13150 18.44580 36.52205 1.000 54.75495  ? 495 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? -12.90983 19.60025 42.63554 1.000 61.31329  ? 496 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? -15.43664 39.70095 24.94129 1.000 59.10066  ? 497 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 11.38538  19.23650 23.61042 1.000 48.19893  ? 498 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? -2.06176  30.89017 5.73125  1.000 62.00781  ? 499 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 16.23240  23.28423 33.07300 1.000 48.54278  ? 500 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 8.319     43.770   29.482   1.000 56.25143  ? 501 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 19.64484  24.57852 30.46828 1.000 55.16561  ? 502 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? -15.25717 41.12177 23.34439 1.000 63.07046  ? 503 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? -17.09476 31.17657 25.44816 1.000 44.73618  ? 504 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 11.14828  31.04306 11.01619 1.000 53.24005  ? 505 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? 0.14224   37.97259 22.12811 1.000 56.82425  ? 506 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? -0.53827  29.97141 5.26672  1.000 62.16846  ? 507 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 6.05578   35.29052 9.60057  1.000 58.42802  ? 508 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? -5.02177  13.65038 39.63895 1.000 56.47512  ? 509 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 8.95618   31.70752 8.93615  1.000 52.76917  ? 510 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? -12.637   17.619   29.530   1.000 51.04792  ? 511 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 11.12542  15.57698 32.47117 1.000 66.06449  ? 512 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 14.30269  17.15791 26.26708 1.000 56.32571  ? 513 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 1.76991   37.07902 20.49643 1.000 62.68312  ? 514 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? -16.31987 27.42188 36.50970 1.000 56.13275  ? 515 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? 1.46904   35.37458 21.99190 1.000 72.01649  ? 516 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? -11.480   17.208   27.013   1.000 53.54389  ? 517 HOH   A 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   . GLU A 9   ? 0.96352 1.06264 0.94510 0.03056  -0.02217 -0.35563 16  GLU A N   
2    C CA  . GLU A 9   ? 0.97460 1.04761 0.94489 0.06109  -0.01554 -0.31279 16  GLU A CA  
3    C C   . GLU A 9   ? 0.87555 0.94952 0.86548 0.06602  -0.02248 -0.27199 16  GLU A C   
4    O O   . GLU A 9   ? 0.82254 0.94240 0.81054 0.07126  -0.03976 -0.26610 16  GLU A O   
5    C CB  . GLU A 9   ? 1.08835 1.19886 1.02071 0.08983  -0.02338 -0.31277 16  GLU A CB  
6    C CG  . GLU A 9   ? 1.15345 1.23044 1.07329 0.11517  -0.00734 -0.28160 16  GLU A CG  
7    C CD  . GLU A 9   ? 1.48057 1.57021 1.39999 0.13454  -0.01312 -0.23809 16  GLU A CD  
8    O OE1 . GLU A 9   ? 1.46464 1.58376 1.38999 0.13157  -0.02928 -0.23097 16  GLU A OE1 
9    O OE2 . GLU A 9   ? 1.39425 1.46412 1.30844 0.15183  0.00052  -0.21248 16  GLU A OE2 
10   N N   . VAL A 10  ? 0.78263 0.80715 0.78959 0.06648  -0.00880 -0.24470 17  VAL A N   
11   C CA  . VAL A 10  ? 0.71597 0.73695 0.74088 0.06775  -0.01410 -0.20972 17  VAL A CA  
12   C C   . VAL A 10  ? 0.68316 0.69248 0.70404 0.09126  -0.00907 -0.17548 17  VAL A C   
13   O O   . VAL A 10  ? 0.66842 0.64867 0.68985 0.10027  0.00585  -0.17168 17  VAL A O   
14   C CB  . VAL A 10  ? 0.66553 0.64584 0.71411 0.04682  -0.00377 -0.20685 17  VAL A CB  
15   C CG1 . VAL A 10  ? 0.62502 0.61055 0.68702 0.04702  -0.01204 -0.17564 17  VAL A CG1 
16   C CG2 . VAL A 10  ? 0.73568 0.72155 0.79093 0.01788  -0.00161 -0.24585 17  VAL A CG2 
17   N N   . GLU A 11  ? 0.62152 0.65367 0.63983 0.10050  -0.01944 -0.15208 18  GLU A N   
18   C CA  . GLU A 11  ? 0.58019 0.60494 0.60011 0.11566  -0.01392 -0.12106 18  GLU A CA  
19   C C   . GLU A 11  ? 0.54237 0.55532 0.58539 0.10669  -0.01755 -0.09813 18  GLU A C   
20   O O   . GLU A 11  ? 0.53351 0.55641 0.57966 0.09621  -0.02790 -0.09874 18  GLU A O   
21   C CB  . GLU A 11  ? 0.60255 0.65321 0.59730 0.13182  -0.01829 -0.11175 18  GLU A CB  
22   C CG  . GLU A 11  ? 0.69438 0.75802 0.65900 0.14688  -0.01314 -0.12832 18  GLU A CG  
23   C CD  . GLU A 11  ? 0.75692 0.83892 0.69055 0.16704  -0.01386 -0.11268 18  GLU A CD  
24   O OE1 . GLU A 11  ? 0.73283 0.83344 0.65790 0.16985  -0.02631 -0.10918 18  GLU A OE1 
25   O OE2 . GLU A 11  ? 0.84419 0.91975 0.76066 0.18176  0.00063  -0.10261 18  GLU A OE2 
26   N N   . THR A 12  ? 0.47879 0.47602 0.53760 0.11225  -0.00932 -0.07902 19  THR A N   
27   C CA  . THR A 12  ? 0.47006 0.46193 0.54811 0.10614  -0.01411 -0.05782 19  THR A CA  
28   C C   . THR A 12  ? 0.49473 0.50344 0.57640 0.11161  -0.01503 -0.03770 19  THR A C   
29   O O   . THR A 12  ? 0.48492 0.49974 0.56821 0.12231  -0.00479 -0.03281 19  THR A O   
30   C CB  . THR A 12  ? 0.51050 0.47778 0.60531 0.10967  -0.00535 -0.05136 19  THR A CB  
31   O OG1 . THR A 12  ? 0.53162 0.47239 0.62084 0.10109  0.00096  -0.07158 19  THR A OG1 
32   C CG2 . THR A 12  ? 0.52535 0.49390 0.63478 0.10594  -0.01304 -0.02961 19  THR A CG2 
33   N N   . PHE A 13  ? 0.43211 0.44677 0.51495 0.10252  -0.02464 -0.02782 20  PHE A N   
34   C CA  . PHE A 13  ? 0.49157 0.51629 0.57742 0.10150  -0.02364 -0.01239 20  PHE A CA  
35   C C   . PHE A 13  ? 0.50825 0.53625 0.61304 0.09130  -0.03158 -0.00051 20  PHE A C   
36   O O   . PHE A 13  ? 0.47250 0.49246 0.57869 0.08594  -0.03901 -0.00199 20  PHE A O   
37   C CB  . PHE A 13  ? 0.49893 0.52419 0.56005 0.10214  -0.02551 -0.01341 20  PHE A CB  
38   C CG  . PHE A 13  ? 0.47159 0.50117 0.50790 0.11556  -0.02196 -0.02553 20  PHE A CG  
39   C CD1 . PHE A 13  ? 0.49498 0.53229 0.52283 0.11523  -0.03086 -0.04365 20  PHE A CD1 
40   C CD2 . PHE A 13  ? 0.51198 0.54207 0.53286 0.12780  -0.00915 -0.01986 20  PHE A CD2 
41   C CE1 . PHE A 13  ? 0.51656 0.56793 0.52097 0.12782  -0.03079 -0.05800 20  PHE A CE1 
42   C CE2 . PHE A 13  ? 0.55486 0.59255 0.54669 0.14317  -0.00723 -0.03078 20  PHE A CE2 
43   C CZ  . PHE A 13  ? 0.55532 0.60663 0.53883 0.14367  -0.01995 -0.05092 20  PHE A CZ  
44   N N   . ALA A 14  ? 0.50227 0.54433 0.62073 0.08753  -0.02888 0.01023  21  ALA A N   
45   C CA  . ALA A 14  ? 0.49187 0.54615 0.62593 0.07670  -0.03864 0.01845  21  ALA A CA  
46   C C   . ALA A 14  ? 0.50716 0.55319 0.62500 0.06343  -0.04228 0.01730  21  ALA A C   
47   O O   . ALA A 14  ? 0.48394 0.52067 0.58796 0.06265  -0.03253 0.01670  21  ALA A O   
48   C CB  . ALA A 14  ? 0.51128 0.59501 0.67461 0.07659  -0.03462 0.02615  21  ALA A CB  
49   N N   . PHE A 15  ? 0.49275 0.53784 0.60821 0.05529  -0.05390 0.01797  22  PHE A N   
50   C CA  . PHE A 15  ? 0.52891 0.56435 0.62893 0.04312  -0.05601 0.01566  22  PHE A CA  
51   C C   . PHE A 15  ? 0.55585 0.60155 0.66768 0.02960  -0.05058 0.01716  22  PHE A C   
52   O O   . PHE A 15  ? 0.51212 0.58611 0.65088 0.02685  -0.05187 0.02033  22  PHE A O   
53   C CB  . PHE A 15  ? 0.51414 0.54962 0.60868 0.03700  -0.06824 0.01568  22  PHE A CB  
54   C CG  . PHE A 15  ? 0.50908 0.52980 0.58812 0.04253  -0.06895 0.01091  22  PHE A CG  
55   C CD1 . PHE A 15  ? 0.53780 0.54695 0.59806 0.04445  -0.06496 0.00436  22  PHE A CD1 
56   C CD2 . PHE A 15  ? 0.50234 0.52165 0.58639 0.04620  -0.07166 0.01304  22  PHE A CD2 
57   C CE1 . PHE A 15  ? 0.50865 0.51672 0.56144 0.04809  -0.06609 -0.00259 22  PHE A CE1 
58   C CE2 . PHE A 15  ? 0.49580 0.50486 0.57049 0.04571  -0.06955 0.00578  22  PHE A CE2 
59   C CZ  . PHE A 15  ? 0.50298 0.51226 0.56505 0.04565  -0.06800 -0.00338 22  PHE A CZ  
60   N N   . GLN A 16  ? 0.58006 0.60289 0.67253 0.02125  -0.04250 0.01406  23  GLN A N   
61   C CA  . GLN A 16  ? 0.61254 0.63744 0.71426 0.00100  -0.03475 0.01150  23  GLN A CA  
62   C C   . GLN A 16  ? 0.57802 0.63099 0.69553 -0.01445 -0.05127 0.00627  23  GLN A C   
63   O O   . GLN A 16  ? 0.53594 0.58612 0.64004 -0.01109 -0.06412 0.00517  23  GLN A O   
64   C CB  . GLN A 16  ? 0.68559 0.66713 0.75593 -0.00250 -0.02006 0.00951  23  GLN A CB  
65   C CG  . GLN A 16  ? 0.80158 0.76053 0.85324 0.01581  -0.00254 0.01750  23  GLN A CG  
66   C CD  . GLN A 16  ? 0.96534 0.88307 0.99535 0.00830  0.02122  0.02042  23  GLN A CD  
67   O OE1 . GLN A 16  ? 1.20807 1.09724 1.22048 -0.00073 0.02442  0.01549  23  GLN A OE1 
68   N NE2 . GLN A 16  ? 1.03966 0.94883 1.06758 0.01265  0.04117  0.02881  23  GLN A NE2 
69   N N   . ALA A 17  ? 0.55603 0.64144 0.70243 -0.03110 -0.05056 0.00260  24  ALA A N   
70   C CA  . ALA A 17  ? 0.53001 0.65948 0.69551 -0.04088 -0.07007 -0.00209 24  ALA A CA  
71   C C   . ALA A 17  ? 0.56919 0.68136 0.70753 -0.05252 -0.07945 -0.01134 24  ALA A C   
72   O O   . ALA A 17  ? 0.58406 0.71905 0.71926 -0.04741 -0.09790 -0.00984 24  ALA A O   
73   C CB  . ALA A 17  ? 0.52072 0.69415 0.72366 -0.06202 -0.06637 -0.00989 24  ALA A CB  
74   N N   . GLU A 18  ? 0.56829 0.63667 0.68282 -0.06548 -0.06473 -0.01973 25  GLU A N   
75   C CA  . GLU A 18  ? 0.61900 0.66612 0.70479 -0.07492 -0.07019 -0.03019 25  GLU A CA  
76   C C   . GLU A 18  ? 0.60841 0.63887 0.67019 -0.05204 -0.07723 -0.02146 25  GLU A C   
77   O O   . GLU A 18  ? 0.54632 0.58391 0.59354 -0.05366 -0.08964 -0.02512 25  GLU A O   
78   C CB  . GLU A 18  ? 0.69071 0.68664 0.75500 -0.09064 -0.04789 -0.04025 25  GLU A CB  
79   C CG  . GLU A 18  ? 0.78542 0.79143 0.87332 -0.12096 -0.03547 -0.05214 25  GLU A CG  
80   C CD  . GLU A 18  ? 0.84172 0.84474 0.94767 -0.11444 -0.01707 -0.03999 25  GLU A CD  
81   O OE1 . GLU A 18  ? 0.76248 0.76124 0.86280 -0.08540 -0.01779 -0.02387 25  GLU A OE1 
82   O OE2 . GLU A 18  ? 1.02389 1.02978 1.14926 -0.14014 -0.00048 -0.04825 25  GLU A OE2 
83   N N   . ILE A 19  ? 0.54215 0.55375 0.59941 -0.03190 -0.06866 -0.01137 26  ILE A N   
84   C CA  . ILE A 19  ? 0.55683 0.55832 0.59739 -0.01463 -0.07327 -0.00663 26  ILE A CA  
85   C C   . ILE A 19  ? 0.52698 0.55766 0.58076 -0.00778 -0.08789 0.00095  26  ILE A C   
86   O O   . ILE A 19  ? 0.50538 0.53390 0.54423 -0.00503 -0.09421 0.00211  26  ILE A O   
87   C CB  . ILE A 19  ? 0.53909 0.52181 0.57312 0.00326  -0.06183 -0.00195 26  ILE A CB  
88   C CG1 . ILE A 19  ? 0.55329 0.49955 0.56237 0.00444  -0.04650 -0.00553 26  ILE A CG1 
89   C CG2 . ILE A 19  ? 0.55210 0.53941 0.58166 0.01697  -0.06773 -0.00006 26  ILE A CG2 
90   C CD1 . ILE A 19  ? 0.67675 0.61016 0.67709 0.02409  -0.03491 0.00089  26  ILE A CD1 
91   N N   . ALA A 20  ? 0.44090 0.49631 0.52072 -0.00297 -0.09058 0.00764  27  ALA A N   
92   C CA  . ALA A 20  ? 0.50143 0.57874 0.59091 0.00806  -0.10165 0.01771  27  ALA A CA  
93   C C   . ALA A 20  ? 0.47129 0.57196 0.55374 0.00010  -0.11639 0.01680  27  ALA A C   
94   O O   . ALA A 20  ? 0.46183 0.56480 0.53247 0.01060  -0.12353 0.02633  27  ALA A O   
95   C CB  . ALA A 20  ? 0.48719 0.58818 0.60632 0.01765  -0.09996 0.02448  27  ALA A CB  
96   N N   . GLN A 21  ? 0.48721 0.60420 0.57418 -0.01927 -0.11963 0.00453  28  GLN A N   
97   C CA  . GLN A 21  ? 0.54604 0.68979 0.62248 -0.02928 -0.13529 -0.00172 28  GLN A CA  
98   C C   . GLN A 21  ? 0.52968 0.64129 0.56777 -0.03063 -0.13392 -0.00541 28  GLN A C   
99   O O   . GLN A 21  ? 0.51252 0.63856 0.53237 -0.02549 -0.14564 -0.00089 28  GLN A O   
100  C CB  . GLN A 21  ? 0.57737 0.74478 0.66951 -0.05580 -0.13644 -0.02023 28  GLN A CB  
101  C CG  . GLN A 21  ? 0.62576 0.85677 0.75689 -0.05633 -0.14823 -0.01889 28  GLN A CG  
102  C CD  . GLN A 21  ? 0.73599 0.98710 0.89156 -0.08771 -0.14184 -0.03927 28  GLN A CD  
103  O OE1 . GLN A 21  ? 0.70963 0.93447 0.84633 -0.11248 -0.13540 -0.05789 28  GLN A OE1 
104  N NE2 . GLN A 21  ? 0.82542 1.12062 1.02340 -0.08761 -0.14040 -0.03668 28  GLN A NE2 
105  N N   . LEU A 22  ? 0.53299 0.60285 0.55675 -0.03454 -0.11857 -0.01233 29  LEU A N   
106  C CA  . LEU A 22  ? 0.55953 0.60232 0.55040 -0.03328 -0.11455 -0.01625 29  LEU A CA  
107  C C   . LEU A 22  ? 0.53797 0.57789 0.52240 -0.01587 -0.11489 -0.00136 29  LEU A C   
108  O O   . LEU A 22  ? 0.55714 0.59599 0.51768 -0.01463 -0.11797 0.00048  29  LEU A O   
109  C CB  . LEU A 22  ? 0.59941 0.60259 0.57918 -0.03466 -0.09712 -0.02455 29  LEU A CB  
110  C CG  . LEU A 22  ? 0.60683 0.58548 0.55781 -0.02792 -0.08981 -0.02789 29  LEU A CG  
111  C CD1 . LEU A 22  ? 0.62069 0.60214 0.54606 -0.04006 -0.09619 -0.03872 29  LEU A CD1 
112  C CD2 . LEU A 22  ? 0.64085 0.58493 0.58239 -0.02172 -0.07274 -0.03303 29  LEU A CD2 
113  N N   . MET A 23  ? 0.51657 0.55260 0.52010 -0.00400 -0.10925 0.00804  30  MET A N   
114  C CA  . MET A 23  ? 0.54971 0.57729 0.54927 0.00758  -0.10539 0.01913  30  MET A CA  
115  C C   . MET A 23  ? 0.57847 0.62174 0.57105 0.01450  -0.11503 0.03312  30  MET A C   
116  O O   . MET A 23  ? 0.60384 0.63530 0.57546 0.01831  -0.11108 0.04076  30  MET A O   
117  C CB  . MET A 23  ? 0.51961 0.54036 0.54064 0.01622  -0.09754 0.02190  30  MET A CB  
118  C CG  . MET A 23  ? 0.48885 0.49750 0.51077 0.01558  -0.08856 0.01077  30  MET A CG  
119  S SD  . MET A 23  ? 0.56955 0.57803 0.61238 0.02560  -0.08223 0.01063  30  MET A SD  
120  C CE  . MET A 23  ? 0.50312 0.50333 0.54724 0.02798  -0.07696 0.01266  30  MET A CE  
121  N N   . SER A 24  ? 0.56898 0.64138 0.57816 0.01806  -0.12648 0.03777  31  SER A N   
122  C CA  . SER A 24  ? 0.55100 0.64529 0.55100 0.03094  -0.13782 0.05312  31  SER A CA  
123  C C   . SER A 24  ? 0.63455 0.73697 0.60089 0.02399  -0.14635 0.04887  31  SER A C   
124  O O   . SER A 24  ? 0.68250 0.78329 0.62370 0.03701  -0.14819 0.06447  31  SER A O   
125  C CB  . SER A 24  ? 0.58162 0.71955 0.61040 0.03666  -0.15041 0.05554  31  SER A CB  
126  O OG  . SER A 24  ? 0.66975 0.84172 0.68678 0.05080  -0.16597 0.06812  31  SER A OG  
127  N N   . LEU A 25  ? 0.62779 0.73412 0.58899 0.00426  -0.14908 0.02793  32  LEU A N   
128  C CA  . LEU A 25  ? 0.66268 0.77214 0.58797 -0.00378 -0.15492 0.01926  32  LEU A CA  
129  C C   . LEU A 25  ? 0.69512 0.76784 0.59266 0.00134  -0.13947 0.02548  32  LEU A C   
130  O O   . LEU A 25  ? 0.74244 0.81734 0.60670 0.00697  -0.14178 0.03281  32  LEU A O   
131  C CB  . LEU A 25  ? 0.68081 0.79090 0.60632 -0.02762 -0.15581 -0.00737 32  LEU A CB  
132  C CG  . LEU A 25  ? 0.80422 0.92317 0.69431 -0.04067 -0.16395 -0.02439 32  LEU A CG  
133  C CD1 . LEU A 25  ? 0.77589 0.90918 0.67914 -0.06680 -0.16866 -0.05093 32  LEU A CD1 
134  C CD2 . LEU A 25  ? 0.80809 0.88429 0.66502 -0.04035 -0.14746 -0.02895 32  LEU A CD2 
135  N N   . ILE A 26  ? 0.62759 0.67129 0.53847 0.00006  -0.12318 0.02250  33  ILE A N   
136  C CA  . ILE A 26  ? 0.66001 0.67865 0.55236 0.00153  -0.10740 0.02370  33  ILE A CA  
137  C C   . ILE A 26  ? 0.71546 0.72642 0.59893 0.01316  -0.10087 0.04519  33  ILE A C   
138  O O   . ILE A 26  ? 0.71110 0.71100 0.56674 0.01375  -0.09130 0.05025  33  ILE A O   
139  C CB  . ILE A 26  ? 0.63053 0.63267 0.54361 -0.00046 -0.09446 0.01396  33  ILE A CB  
140  C CG1 . ILE A 26  ? 0.62155 0.61710 0.52859 -0.00888 -0.09407 -0.00447 33  ILE A CG1 
141  C CG2 . ILE A 26  ? 0.59067 0.58009 0.49811 0.00193  -0.07824 0.01625  33  ILE A CG2 
142  C CD1 . ILE A 26  ? 0.65424 0.63705 0.57871 -0.00454 -0.08372 -0.01060 33  ILE A CD1 
143  N N   . ILE A 27  ? 0.71102 0.72334 0.61540 0.02313  -0.10269 0.05870  34  ILE A N   
144  C CA  . ILE A 27  ? 0.78999 0.78237 0.68373 0.03487  -0.09128 0.08018  34  ILE A CA  
145  C C   . ILE A 27  ? 0.85577 0.86088 0.71595 0.04877  -0.10149 0.09814  34  ILE A C   
146  O O   . ILE A 27  ? 0.95764 0.94048 0.78842 0.05597  -0.08828 0.11500  34  ILE A O   
147  C CB  . ILE A 27  ? 0.79880 0.78075 0.72285 0.04300  -0.08644 0.08717  34  ILE A CB  
148  C CG1 . ILE A 27  ? 0.67226 0.65415 0.62647 0.03176  -0.08281 0.06724  34  ILE A CG1 
149  C CG2 . ILE A 27  ? 1.01114 0.95598 0.92457 0.04978  -0.06586 0.10468  34  ILE A CG2 
150  C CD1 . ILE A 27  ? 0.67235 0.64601 0.65288 0.03908  -0.07841 0.07013  34  ILE A CD1 
151  N N   . ASN A 28  ? 0.84632 0.89023 0.70955 0.05291  -0.12422 0.09481  35  ASN A N   
152  C CA  . ASN A 28  ? 0.91978 0.98866 0.75568 0.07212  -0.13840 0.11308  35  ASN A CA  
153  C C   . ASN A 28  ? 1.09415 1.18438 0.89077 0.06525  -0.14983 0.10309  35  ASN A C   
154  O O   . ASN A 28  ? 1.18406 1.29427 0.94713 0.08353  -0.16032 0.11963  35  ASN A O   
155  C CB  . ASN A 28  ? 0.92320 1.03609 0.78942 0.08310  -0.15831 0.11484  35  ASN A CB  
156  C CG  . ASN A 28  ? 0.93142 1.02294 0.83193 0.09345  -0.14618 0.12484  35  ASN A CG  
157  O OD1 . ASN A 28  ? 0.98769 1.10274 0.92566 0.08920  -0.15323 0.11407  35  ASN A OD1 
158  N ND2 . ASN A 28  ? 0.92530 0.96934 0.81165 0.10549  -0.12513 0.14418  35  ASN A ND2 
159  N N   . THR A 29  ? 0.95442 1.03994 0.75052 0.04224  -0.14739 0.07685  36  THR A N   
160  C CA  . THR A 29  ? 1.05801 1.15686 0.81327 0.03442  -0.15484 0.06349  36  THR A CA  
161  C C   . THR A 29  ? 0.97729 1.04218 0.69278 0.04034  -0.13388 0.07668  36  THR A C   
162  O O   . THR A 29  ? 0.90929 0.93944 0.63830 0.03484  -0.11109 0.07781  36  THR A O   
163  C CB  . THR A 29  ? 1.04832 1.14608 0.81550 0.00931  -0.15575 0.03023  36  THR A CB  
164  O OG1 . THR A 29  ? 0.96815 1.10218 0.76566 0.00019  -0.17452 0.01684  36  THR A OG1 
165  C CG2 . THR A 29  ? 1.01203 1.10922 0.73243 0.00064  -0.15614 0.01384  36  THR A CG2 
166  N N   . PHE A 30  ? 0.96856 1.04833 0.63512 0.05154  -0.14122 0.08612  37  PHE A N   
167  C CA  . PHE A 30  ? 0.99430 1.04366 0.61711 0.05635  -0.11906 0.09865  37  PHE A CA  
168  C C   . PHE A 30  ? 0.99328 1.03225 0.60653 0.03606  -0.10925 0.06981  37  PHE A C   
169  O O   . PHE A 30  ? 1.12767 1.18862 0.71572 0.02822  -0.12404 0.04813  37  PHE A O   
170  C CB  . PHE A 30  ? 1.02839 1.09794 0.59502 0.07823  -0.13000 0.11899  37  PHE A CB  
171  C CG  . PHE A 30  ? 1.23700 1.26994 0.75595 0.08661  -0.10220 0.13967  37  PHE A CG  
172  C CD1 . PHE A 30  ? 1.23294 1.22655 0.75056 0.10101  -0.07820 0.17306  37  PHE A CD1 
173  C CD2 . PHE A 30  ? 1.11149 1.14581 0.58594 0.07882  -0.09660 0.12480  37  PHE A CD2 
174  C CE1 . PHE A 30  ? 1.34027 1.29738 0.81532 0.10522  -0.04774 0.19240  37  PHE A CE1 
175  C CE2 . PHE A 30  ? 1.11148 1.11370 0.54246 0.08588  -0.06754 0.14447  37  PHE A CE2 
176  C CZ  . PHE A 30  ? 1.15145 1.11553 0.58374 0.09803  -0.04246 0.17897  37  PHE A CZ  
177  N N   . TYR A 31  ? 0.94032 0.94778 0.57427 0.02811  -0.08384 0.06775  38  TYR A N   
178  C CA  . TYR A 31  ? 0.91904 0.91651 0.54923 0.01455  -0.07169 0.04243  38  TYR A CA  
179  C C   . TYR A 31  ? 0.90802 0.88149 0.53861 0.01490  -0.04035 0.05304  38  TYR A C   
180  O O   . TYR A 31  ? 0.84473 0.80771 0.51545 0.01245  -0.02881 0.05988  38  TYR A O   
181  C CB  . TYR A 31  ? 0.90052 0.89898 0.57458 0.00289  -0.07839 0.02004  38  TYR A CB  
182  C CG  . TYR A 31  ? 0.90102 0.88523 0.56896 -0.00530 -0.06537 -0.00453 38  TYR A CG  
183  C CD1 . TYR A 31  ? 0.90872 0.89432 0.54148 -0.01229 -0.07231 -0.02658 38  TYR A CD1 
184  C CD2 . TYR A 31  ? 0.85383 0.82489 0.55091 -0.00464 -0.04605 -0.00724 38  TYR A CD2 
185  C CE1 . TYR A 31  ? 0.95224 0.91694 0.57628 -0.01617 -0.05704 -0.04843 38  TYR A CE1 
186  C CE2 . TYR A 31  ? 0.86565 0.82521 0.55650 -0.00548 -0.03338 -0.02727 38  TYR A CE2 
187  C CZ  . TYR A 31  ? 0.93660 0.88823 0.58974 -0.01014 -0.03734 -0.04673 38  TYR A CZ  
188  O OH  . TYR A 31  ? 0.96618 0.89859 0.61002 -0.00754 -0.02134 -0.06599 38  TYR A OH  
189  N N   . SER A 32  ? 0.93771 0.90587 0.52445 0.01628  -0.02576 0.05206  39  SER A N   
190  C CA  . SER A 32  ? 0.95374 0.90455 0.53801 0.01543  0.00679  0.06460  39  SER A CA  
191  C C   . SER A 32  ? 0.93592 0.88826 0.55450 0.00605  0.02416  0.04340  39  SER A C   
192  O O   . SER A 32  ? 1.04105 0.98921 0.68098 0.00107  0.04940  0.05029  39  SER A O   
193  C CB  . SER A 32  ? 0.99597 0.94229 0.51544 0.02322  0.01829  0.07559  39  SER A CB  
194  O OG  . SER A 32  ? 0.96653 0.90800 0.45519 0.03750  0.01134  0.10534  39  SER A OG  
195  N N   . ASN A 33  ? 0.87816 0.83715 0.50280 0.00407  0.01283  0.01772  40  ASN A N   
196  C CA  . ASN A 33  ? 0.85895 0.82105 0.51173 0.00282  0.02867  -0.00047 40  ASN A CA  
197  C C   . ASN A 33  ? 0.79618 0.76532 0.50700 0.00059  0.02341  -0.00173 40  ASN A C   
198  O O   . ASN A 33  ? 0.77507 0.74489 0.50529 0.00311  0.01466  -0.01727 40  ASN A O   
199  C CB  . ASN A 33  ? 0.89460 0.84998 0.52188 0.00511  0.02336  -0.02542 40  ASN A CB  
200  C CG  . ASN A 33  ? 0.88938 0.84638 0.53605 0.01177  0.04328  -0.04102 40  ASN A CG  
201  O OD1 . ASN A 33  ? 0.85929 0.83031 0.51928 0.01413  0.06571  -0.03563 40  ASN A OD1 
202  N ND2 . ASN A 33  ? 0.85531 0.79874 0.50405 0.01566  0.03701  -0.06017 40  ASN A ND2 
203  N N   . LYS A 34  ? 0.78921 0.65123 0.50936 0.01422  -0.14261 0.03760  41  LYS A N   
204  C CA  . LYS A 34  ? 0.71497 0.62455 0.50254 0.01141  -0.12915 0.03960  41  LYS A CA  
205  C C   . LYS A 34  ? 0.67730 0.57383 0.47052 0.01968  -0.10516 0.02669  41  LYS A C   
206  O O   . LYS A 34  ? 0.60673 0.53273 0.44407 0.01458  -0.09898 0.02544  41  LYS A O   
207  C CB  . LYS A 34  ? 0.69231 0.64214 0.52331 0.02375  -0.11456 0.05180  41  LYS A CB  
208  C CG  . LYS A 34  ? 0.68784 0.66780 0.53205 0.01594  -0.13656 0.06985  41  LYS A CG  
209  C CD  . LYS A 34  ? 0.62009 0.63360 0.50277 0.03261  -0.11848 0.08192  41  LYS A CD  
210  C CE  . LYS A 34  ? 0.76624 0.81149 0.66099 0.02834  -0.13875 0.10372  41  LYS A CE  
211  N NZ  . LYS A 34  ? 0.73868 0.83063 0.67889 0.01568  -0.15168 0.11804  41  LYS A NZ  
212  N N   . GLU A 35  ? 0.71330 0.56782 0.46240 0.03395  -0.09114 0.01953  42  GLU A N   
213  C CA  . GLU A 35  ? 0.70991 0.55899 0.47068 0.04347  -0.06717 0.01285  42  GLU A CA  
214  C C   . GLU A 35  ? 0.71582 0.55823 0.47788 0.02969  -0.07639 0.00369  42  GLU A C   
215  O O   . GLU A 35  ? 0.67501 0.52464 0.45949 0.03453  -0.05908 0.00009  42  GLU A O   
216  C CB  . GLU A 35  ? 0.78718 0.59536 0.49909 0.06523  -0.04857 0.01305  42  GLU A CB  
217  C CG  . GLU A 35  ? 0.89079 0.64028 0.52724 0.06626  -0.06218 0.00429  42  GLU A CG  
218  C CD  . GLU A 35  ? 0.99336 0.70089 0.57552 0.09517  -0.03865 0.00722  42  GLU A CD  
219  O OE1 . GLU A 35  ? 0.97632 0.69357 0.56035 0.11018  -0.02494 0.01838  42  GLU A OE1 
220  O OE2 . GLU A 35  ? 1.26216 0.92659 0.79893 0.10517  -0.03207 0.00044  42  GLU A OE2 
221  N N   . ILE A 36  ? 0.69147 0.52111 0.43211 0.01123  -0.10484 0.00213  43  ILE A N   
222  C CA  . ILE A 36  ? 0.72001 0.54118 0.46168 -0.00327 -0.11497 -0.00433 43  ILE A CA  
223  C C   . ILE A 36  ? 0.65052 0.52463 0.45884 -0.01031 -0.10818 -0.00086 43  ILE A C   
224  O O   . ILE A 36  ? 0.62555 0.49750 0.44105 -0.01840 -0.10983 -0.00539 43  ILE A O   
225  C CB  . ILE A 36  ? 0.77735 0.57278 0.48426 -0.02579 -0.15184 -0.00276 43  ILE A CB  
226  C CG1 . ILE A 36  ? 0.74962 0.59515 0.49916 -0.04069 -0.17113 0.01337  43  ILE A CG1 
227  C CG2 . ILE A 36  ? 0.86589 0.59265 0.48945 -0.01731 -0.16060 -0.00982 43  ILE A CG2 
228  C CD1 . ILE A 36  ? 0.74824 0.63124 0.54344 -0.06314 -0.18790 0.02319  43  ILE A CD1 
229  N N   . PHE A 37  ? 0.58327 0.50019 0.43514 -0.00535 -0.10004 0.00724  44  PHE A N   
230  C CA  . PHE A 37  ? 0.54519 0.50356 0.44892 -0.00703 -0.09172 0.00955  44  PHE A CA  
231  C C   . PHE A 37  ? 0.54531 0.49569 0.45614 0.00098  -0.07214 -0.00016 44  PHE A C   
232  O O   . PHE A 37  ? 0.51152 0.47849 0.44537 -0.00459 -0.07123 -0.00216 44  PHE A O   
233  C CB  . PHE A 37  ? 0.53376 0.52553 0.46979 0.00230  -0.08402 0.01874  44  PHE A CB  
234  C CG  . PHE A 37  ? 0.52559 0.50934 0.46625 0.01834  -0.06215 0.01450  44  PHE A CG  
235  C CD1 . PHE A 37  ? 0.54463 0.50664 0.45975 0.02770  -0.05680 0.01654  44  PHE A CD1 
236  C CD2 . PHE A 37  ? 0.50689 0.50302 0.47594 0.02313  -0.04874 0.01037  44  PHE A CD2 
237  C CE1 . PHE A 37  ? 0.57383 0.53188 0.49946 0.04011  -0.03775 0.01755  44  PHE A CE1 
238  C CE2 . PHE A 37  ? 0.50651 0.49363 0.48236 0.03302  -0.03373 0.00939  44  PHE A CE2 
239  C CZ  . PHE A 37  ? 0.52950 0.50028 0.48764 0.04080  -0.02785 0.01449  44  PHE A CZ  
240  N N   . LEU A 38  ? 0.55469 0.48279 0.44787 0.01453  -0.05637 -0.00308 45  LEU A N   
241  C CA  . LEU A 38  ? 0.55189 0.47945 0.45931 0.02140  -0.03900 -0.00675 45  LEU A CA  
242  C C   . LEU A 38  ? 0.57655 0.48173 0.46186 0.01747  -0.04144 -0.01269 45  LEU A C   
243  O O   . LEU A 38  ? 0.56593 0.48314 0.47339 0.01607  -0.03501 -0.01492 45  LEU A O   
244  C CB  . LEU A 38  ? 0.55081 0.46727 0.45214 0.03696  -0.02112 -0.00116 45  LEU A CB  
245  C CG  . LEU A 38  ? 0.59764 0.52400 0.52683 0.04223  -0.00489 0.00206  45  LEU A CG  
246  C CD1 . LEU A 38  ? 0.49315 0.44684 0.46306 0.03328  -0.00924 -0.00079 45  LEU A CD1 
247  C CD2 . LEU A 38  ? 0.57353 0.49589 0.50430 0.05612  0.01174  0.01446  45  LEU A CD2 
248  N N   . ARG A 39  ? 0.59453 0.46229 0.43167 0.01594  -0.05210 -0.01526 46  ARG A N   
249  C CA  . ARG A 39  ? 0.68753 0.52481 0.49666 0.01189  -0.05680 -0.02121 46  ARG A CA  
250  C C   . ARG A 39  ? 0.63882 0.50114 0.47799 -0.00727 -0.07179 -0.02136 46  ARG A C   
251  O O   . ARG A 39  ? 0.66612 0.52647 0.51178 -0.00861 -0.06704 -0.02411 46  ARG A O   
252  C CB  . ARG A 39  ? 0.78215 0.56322 0.52347 0.01273  -0.07024 -0.02507 46  ARG A CB  
253  C CG  . ARG A 39  ? 0.86574 0.60550 0.57087 0.00387  -0.08290 -0.03171 46  ARG A CG  
254  C CD  . ARG A 39  ? 0.99774 0.67343 0.62833 0.00027  -0.10446 -0.03674 46  ARG A CD  
255  N NE  . ARG A 39  ? 1.06665 0.75719 0.70830 -0.02669 -0.13783 -0.03195 46  ARG A NE  
256  C CZ  . ARG A 39  ? 1.18739 0.84250 0.78081 -0.03347 -0.16127 -0.03194 46  ARG A CZ  
257  N NH1 . ARG A 39  ? 1.13503 0.73114 0.65710 -0.01308 -0.15410 -0.03899 46  ARG A NH1 
258  N NH2 . ARG A 39  ? 0.97361 0.65416 0.59027 -0.06013 -0.19266 -0.02216 46  ARG A NH2 
259  N N   . GLU A 40  ? 0.58049 0.46990 0.44041 -0.02044 -0.08845 -0.01511 47  GLU A N   
260  C CA  . GLU A 40  ? 0.59263 0.51114 0.48381 -0.03659 -0.10091 -0.00947 47  GLU A CA  
261  C C   . GLU A 40  ? 0.56307 0.51751 0.49652 -0.02943 -0.08366 -0.00998 47  GLU A C   
262  O O   . GLU A 40  ? 0.50143 0.46395 0.44726 -0.03579 -0.08482 -0.00955 47  GLU A O   
263  C CB  . GLU A 40  ? 0.58910 0.53584 0.49815 -0.04861 -0.11972 0.00358  47  GLU A CB  
264  C CG  . GLU A 40  ? 0.64232 0.55278 0.50833 -0.06175 -0.14542 0.00582  47  GLU A CG  
265  C CD  . GLU A 40  ? 0.80222 0.66314 0.62740 -0.07397 -0.15980 -0.00098 47  GLU A CD  
266  O OE1 . GLU A 40  ? 0.73810 0.61479 0.58812 -0.08547 -0.16384 0.00344  47  GLU A OE1 
267  O OE2 . GLU A 40  ? 0.82917 0.63145 0.59319 -0.07026 -0.16636 -0.01017 47  GLU A OE2 
268  N N   . LEU A 41  ? 0.48316 0.45501 0.43528 -0.01667 -0.06927 -0.01057 48  LEU A N   
269  C CA  . LEU A 41  ? 0.47304 0.46950 0.45601 -0.01074 -0.05725 -0.01233 48  LEU A CA  
270  C C   . LEU A 41  ? 0.45704 0.43825 0.43520 -0.00640 -0.04661 -0.01869 48  LEU A C   
271  O O   . LEU A 41  ? 0.48397 0.47991 0.47980 -0.00721 -0.04358 -0.02010 48  LEU A O   
272  C CB  . LEU A 41  ? 0.42969 0.43917 0.42790 -0.00032 -0.04896 -0.01096 48  LEU A CB  
273  C CG  . LEU A 41  ? 0.43329 0.46448 0.44164 -0.00062 -0.05648 -0.00124 48  LEU A CG  
274  C CD1 . LEU A 41  ? 0.40607 0.43989 0.42191 0.01186  -0.04722 -0.00024 48  LEU A CD1 
275  C CD2 . LEU A 41  ? 0.40115 0.46271 0.43163 -0.00355 -0.05975 0.00629  48  LEU A CD2 
276  N N   . ILE A 42  ? 0.49349 0.44663 0.44714 0.00037  -0.03988 -0.02014 49  ILE A N   
277  C CA  . ILE A 42  ? 0.48812 0.43045 0.43923 0.00674  -0.02842 -0.02092 49  ILE A CA  
278  C C   . ILE A 42  ? 0.51790 0.44618 0.45392 -0.00048 -0.03540 -0.02336 49  ILE A C   
279  O O   . ILE A 42  ? 0.49630 0.43290 0.44601 0.00045  -0.02983 -0.02306 49  ILE A O   
280  C CB  . ILE A 42  ? 0.52980 0.44774 0.45777 0.02103  -0.01526 -0.01687 49  ILE A CB  
281  C CG1 . ILE A 42  ? 0.51951 0.45672 0.47405 0.02688  -0.00645 -0.01061 49  ILE A CG1 
282  C CG2 . ILE A 42  ? 0.56125 0.46481 0.47974 0.03063  -0.00269 -0.01355 49  ILE A CG2 
283  C CD1 . ILE A 42  ? 0.52951 0.44936 0.46588 0.04247  0.00845  -0.00148 49  ILE A CD1 
284  N N   . SER A 43  ? 0.54096 0.44624 0.44832 -0.00934 -0.05005 -0.02448 50  SER A N   
285  C CA  . SER A 43  ? 0.57993 0.46815 0.47349 -0.01998 -0.06056 -0.02516 50  SER A CA  
286  C C   . SER A 43  ? 0.52660 0.45572 0.46059 -0.02997 -0.06490 -0.02068 50  SER A C   
287  O O   . SER A 43  ? 0.50134 0.42851 0.43844 -0.03288 -0.06394 -0.01997 50  SER A O   
288  C CB  . SER A 43  ? 0.63826 0.49116 0.49327 -0.03227 -0.08177 -0.02538 50  SER A CB  
289  O OG  . SER A 43  ? 0.83722 0.63424 0.63677 -0.02025 -0.07711 -0.03130 50  SER A OG  
290  N N   . ASN A 44  ? 0.49665 0.46161 0.45899 -0.03231 -0.06783 -0.01612 51  ASN A N   
291  C CA  . ASN A 44  ? 0.46969 0.47260 0.46538 -0.03464 -0.06677 -0.01047 51  ASN A CA  
292  C C   . ASN A 44  ? 0.46955 0.47942 0.47616 -0.02444 -0.05275 -0.01606 51  ASN A C   
293  O O   . ASN A 44  ? 0.44287 0.46528 0.46022 -0.02638 -0.05192 -0.01354 51  ASN A O   
294  C CB  . ASN A 44  ? 0.45997 0.49447 0.47712 -0.03179 -0.06782 -0.00366 51  ASN A CB  
295  C CG  . ASN A 44  ? 0.49015 0.53462 0.51075 -0.04534 -0.08509 0.00944  51  ASN A CG  
296  O OD1 . ASN A 44  ? 0.53786 0.56215 0.54332 -0.06034 -0.09986 0.01250  51  ASN A OD1 
297  N ND2 . ASN A 44  ? 0.46741 0.54135 0.50745 -0.04053 -0.08487 0.01909  51  ASN A ND2 
298  N N   . SER A 45  ? 0.45568 0.45868 0.46103 -0.01467 -0.04328 -0.02120 52  SER A N   
299  C CA  . SER A 45  ? 0.40210 0.41197 0.42008 -0.00860 -0.03487 -0.02347 52  SER A CA  
300  C C   . SER A 45  ? 0.42601 0.42206 0.43514 -0.00828 -0.03113 -0.02210 52  SER A C   
301  O O   . SER A 45  ? 0.44140 0.45007 0.46283 -0.00780 -0.02941 -0.02107 52  SER A O   
302  C CB  . SER A 45  ? 0.42425 0.43038 0.44732 -0.00180 -0.02843 -0.02404 52  SER A CB  
303  O OG  . SER A 45  ? 0.43265 0.44874 0.46348 -0.00041 -0.03113 -0.02557 52  SER A OG  
304  N N   . SER A 46  ? 0.44807 0.41418 0.43085 -0.00650 -0.02968 -0.02174 53  SER A N   
305  C CA  . SER A 46  ? 0.48345 0.42886 0.45091 -0.00222 -0.02401 -0.01964 53  SER A CA  
306  C C   . SER A 46  ? 0.47367 0.42318 0.44388 -0.01266 -0.03278 -0.01853 53  SER A C   
307  O O   . SER A 46  ? 0.45517 0.40679 0.43048 -0.00924 -0.02730 -0.01544 53  SER A O   
308  C CB  . SER A 46  ? 0.58049 0.48132 0.50575 0.00495  -0.02100 -0.02069 53  SER A CB  
309  O OG  . SER A 46  ? 0.62479 0.49886 0.52900 0.01385  -0.01263 -0.01801 53  SER A OG  
310  N N   . ASP A 47  ? 0.48443 0.43848 0.45473 -0.02545 -0.04643 -0.01750 54  ASP A N   
311  C CA  . ASP A 47  ? 0.48301 0.44719 0.46281 -0.03650 -0.05467 -0.01120 54  ASP A CA  
312  C C   . ASP A 47  ? 0.50464 0.50777 0.51438 -0.03174 -0.04787 -0.00842 54  ASP A C   
313  O O   . ASP A 47  ? 0.44631 0.45377 0.46082 -0.03281 -0.04639 -0.00391 54  ASP A O   
314  C CB  . ASP A 47  ? 0.51807 0.48797 0.50055 -0.05203 -0.07154 -0.00430 54  ASP A CB  
315  C CG  . ASP A 47  ? 0.57026 0.49156 0.51364 -0.06105 -0.08520 -0.00681 54  ASP A CG  
316  O OD1 . ASP A 47  ? 0.56260 0.44089 0.47181 -0.05294 -0.07916 -0.01375 54  ASP A OD1 
317  O OD2 . ASP A 47  ? 0.56825 0.49248 0.51218 -0.07500 -0.10239 -0.00052 54  ASP A OD2 
318  N N   . ALA A 48  ? 0.42388 0.45023 0.44850 -0.02544 -0.04428 -0.01118 55  ALA A N   
319  C CA  . ALA A 48  ? 0.41366 0.46591 0.45400 -0.01893 -0.03974 -0.01071 55  ALA A CA  
320  C C   . ALA A 48  ? 0.37199 0.41892 0.41219 -0.01350 -0.03430 -0.01342 55  ALA A C   
321  O O   . ALA A 48  ? 0.37866 0.43924 0.42459 -0.01114 -0.03351 -0.01088 55  ALA A O   
322  C CB  . ALA A 48  ? 0.38558 0.45015 0.43138 -0.01201 -0.03839 -0.01457 55  ALA A CB  
323  N N   . LEU A 49  ? 0.37738 0.40722 0.41205 -0.01020 -0.03004 -0.01550 56  LEU A N   
324  C CA  . LEU A 49  ? 0.38877 0.41989 0.42998 -0.00479 -0.02461 -0.01186 56  LEU A CA  
325  C C   . LEU A 49  ? 0.40641 0.42615 0.43876 -0.00411 -0.02129 -0.00631 56  LEU A C   
326  O O   . LEU A 49  ? 0.42173 0.45287 0.46369 -0.00064 -0.01894 -0.00098 56  LEU A O   
327  C CB  . LEU A 49  ? 0.40042 0.42232 0.44318 0.00124  -0.01787 -0.00925 56  LEU A CB  
328  C CG  . LEU A 49  ? 0.41133 0.44368 0.46730 -0.00013 -0.02168 -0.01189 56  LEU A CG  
329  C CD1 . LEU A 49  ? 0.39804 0.41839 0.45123 0.00535  -0.01383 -0.00755 56  LEU A CD1 
330  C CD2 . LEU A 49  ? 0.41234 0.46159 0.48738 -0.00224 -0.02752 -0.00821 56  LEU A CD2 
331  N N   . ASP A 50  ? 0.44562 0.43951 0.45732 -0.00816 -0.02313 -0.00678 57  ASP A N   
332  C CA  . ASP A 50  ? 0.45170 0.42582 0.44984 -0.00885 -0.02210 -0.00180 57  ASP A CA  
333  C C   . ASP A 50  ? 0.41156 0.41110 0.42645 -0.01496 -0.02661 0.00336  57  ASP A C   
334  O O   . ASP A 50  ? 0.42111 0.41907 0.43645 -0.01138 -0.02248 0.00950  57  ASP A O   
335  C CB  . ASP A 50  ? 0.48553 0.41873 0.45228 -0.01612 -0.02951 -0.00413 57  ASP A CB  
336  C CG  . ASP A 50  ? 0.54876 0.44395 0.48449 -0.00375 -0.02107 -0.00757 57  ASP A CG  
337  O OD1 . ASP A 50  ? 0.55270 0.45357 0.49452 0.01200  -0.00608 -0.00312 57  ASP A OD1 
338  O OD2 . ASP A 50  ? 0.58663 0.44703 0.49138 -0.00909 -0.02974 -0.01238 57  ASP A OD2 
339  N N   . LYS A 51  ? 0.39916 0.42315 0.42712 -0.02129 -0.03302 0.00326  58  LYS A N   
340  C CA  . LYS A 51  ? 0.41665 0.46528 0.45773 -0.02383 -0.03453 0.01165  58  LYS A CA  
341  C C   . LYS A 51  ? 0.40968 0.47795 0.45819 -0.01363 -0.02934 0.01109  58  LYS A C   
342  O O   . LYS A 51  ? 0.43655 0.51192 0.48757 -0.01205 -0.02733 0.01871  58  LYS A O   
343  C CB  . LYS A 51  ? 0.44219 0.51401 0.49474 -0.02808 -0.03905 0.01591  58  LYS A CB  
344  C CG  . LYS A 51  ? 0.64917 0.74932 0.71589 -0.02775 -0.03740 0.02993  58  LYS A CG  
345  C CD  . LYS A 51  ? 0.72603 0.84775 0.80859 -0.03493 -0.04220 0.04343  58  LYS A CD  
346  C CE  . LYS A 51  ? 0.64576 0.79799 0.74628 -0.03422 -0.03841 0.06397  58  LYS A CE  
347  N NZ  . LYS A 51  ? 0.67776 0.86727 0.79889 -0.03015 -0.03560 0.08069  58  LYS A NZ  
348  N N   . ILE A 52  ? 0.39707 0.47192 0.44759 -0.00796 -0.02947 0.00310  59  ILE A N   
349  C CA  . ILE A 52  ? 0.39773 0.48561 0.45087 -0.00168 -0.03066 0.00261  59  ILE A CA  
350  C C   . ILE A 52  ? 0.38702 0.47007 0.44496 0.00034  -0.02768 0.00892  59  ILE A C   
351  O O   . ILE A 52  ? 0.41231 0.50762 0.47304 0.00363  -0.02933 0.01422  59  ILE A O   
352  C CB  . ILE A 52  ? 0.34962 0.43801 0.40109 0.00044  -0.03607 -0.00654 59  ILE A CB  
353  C CG1 . ILE A 52  ? 0.40394 0.49900 0.45038 0.00401  -0.04356 -0.00754 59  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.37136 0.44806 0.42989 -0.00222 -0.03517 -0.00814 59  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.39334 0.49810 0.42601 0.01133  -0.04214 -0.00524 59  ILE A CD1 
356  N N   . ARG A 53  ? 0.41382 0.47860 0.47025 0.00102  -0.02212 0.01032  60  ARG A N   
357  C CA  . ARG A 53  ? 0.44210 0.50205 0.50201 0.00813  -0.01482 0.02025  60  ARG A CA  
358  C C   . ARG A 53  ? 0.43770 0.48873 0.48910 0.00893  -0.01146 0.02691  60  ARG A C   
359  O O   . ARG A 53  ? 0.45200 0.51300 0.51062 0.01507  -0.00829 0.03664  60  ARG A O   
360  C CB  . ARG A 53  ? 0.46283 0.50035 0.51510 0.01428  -0.00577 0.02154  60  ARG A CB  
361  C CG  . ARG A 53  ? 0.57470 0.60593 0.62822 0.02776  0.00678  0.03542  60  ARG A CG  
362  C CD  . ARG A 53  ? 0.74739 0.76647 0.79769 0.03869  0.01821  0.04036  60  ARG A CD  
363  N NE  . ARG A 53  ? 0.95101 0.94624 0.98462 0.05715  0.03534  0.05238  60  ARG A NE  
364  C CZ  . ARG A 53  ? 1.01980 0.96896 1.01459 0.06774  0.04529  0.04858  60  ARG A CZ  
365  N NH1 . ARG A 53  ? 0.78801 0.71434 0.76084 0.05915  0.03783  0.03416  60  ARG A NH1 
366  N NH2 . ARG A 53  ? 0.92097 0.84292 0.89410 0.08896  0.06274  0.06016  60  ARG A NH2 
367  N N   . TYR A 54  ? 0.45018 0.48314 0.48820 0.00140  -0.01386 0.02420  61  TYR A N   
368  C CA  . TYR A 54  ? 0.46576 0.48742 0.49710 -0.00134 -0.01327 0.03251  61  TYR A CA  
369  C C   . TYR A 54  ? 0.44622 0.50122 0.49208 -0.00087 -0.01518 0.03902  61  TYR A C   
370  O O   . TYR A 54  ? 0.44244 0.49886 0.48937 0.00375  -0.01128 0.04871  61  TYR A O   
371  C CB  . TYR A 54  ? 0.45600 0.45343 0.47419 -0.01459 -0.02099 0.03123  61  TYR A CB  
372  C CG  . TYR A 54  ? 0.45356 0.44315 0.47078 -0.02275 -0.02458 0.04275  61  TYR A CG  
373  C CD1 . TYR A 54  ? 0.50454 0.45632 0.50206 -0.01904 -0.02065 0.04760  61  TYR A CD1 
374  C CD2 . TYR A 54  ? 0.47204 0.49147 0.50803 -0.03239 -0.03047 0.05161  61  TYR A CD2 
375  C CE1 . TYR A 54  ? 0.48629 0.42729 0.48326 -0.02824 -0.02528 0.05957  61  TYR A CE1 
376  C CE2 . TYR A 54  ? 0.49555 0.51146 0.53605 -0.04120 -0.03381 0.06657  61  TYR A CE2 
377  C CZ  . TYR A 54  ? 0.50521 0.48044 0.52640 -0.04086 -0.03260 0.06981  61  TYR A CZ  
378  O OH  . TYR A 54  ? 0.55920 0.52733 0.58510 -0.05133 -0.03727 0.08601  61  TYR A OH  
379  N N   . GLU A 55  ? 0.40302 0.48227 0.45578 -0.00283 -0.01991 0.03455  62  GLU A N   
380  C CA  . GLU A 55  ? 0.46480 0.57054 0.52147 0.00196  -0.02015 0.04042  62  GLU A CA  
381  C C   . GLU A 55  ? 0.44813 0.56392 0.50525 0.01016  -0.02141 0.04100  62  GLU A C   
382  O O   . GLU A 55  ? 0.44761 0.57683 0.50317 0.01522  -0.02075 0.04932  62  GLU A O   
383  C CB  . GLU A 55  ? 0.47890 0.60103 0.53422 0.00375  -0.02234 0.03541  62  GLU A CB  
384  C CG  . GLU A 55  ? 0.54100 0.66777 0.60398 -0.00394 -0.02181 0.04349  62  GLU A CG  
385  C CD  . GLU A 55  ? 0.70017 0.84984 0.76321 0.00438  -0.01907 0.04496  62  GLU A CD  
386  O OE1 . GLU A 55  ? 0.63918 0.79267 0.68753 0.01701  -0.01806 0.03709  62  GLU A OE1 
387  O OE2 . GLU A 55  ? 0.78504 0.94672 0.86078 -0.00109 -0.01874 0.05548  62  GLU A OE2 
388  N N   . SER A 56  ? 0.41403 0.52573 0.47526 0.01085  -0.02435 0.03526  63  SER A N   
389  C CA  . SER A 56  ? 0.45533 0.58068 0.52327 0.01486  -0.02997 0.04008  63  SER A CA  
390  C C   . SER A 56  ? 0.46674 0.59293 0.54240 0.02055  -0.02268 0.05484  63  SER A C   
391  O O   . SER A 56  ? 0.46224 0.60611 0.54525 0.02398  -0.02822 0.06359  63  SER A O   
392  C CB  . SER A 56  ? 0.42731 0.55215 0.50543 0.01181  -0.03569 0.03588  63  SER A CB  
393  O OG  . SER A 56  ? 0.42016 0.53473 0.50791 0.01509  -0.02497 0.04281  63  SER A OG  
394  N N   . LEU A 57  ? 0.47439 0.57817 0.54520 0.02187  -0.01190 0.05845  64  LEU A N   
395  C CA  . LEU A 57  ? 0.51563 0.61211 0.58795 0.03074  -0.00270 0.07274  64  LEU A CA  
396  C C   . LEU A 57  ? 0.52811 0.63860 0.59979 0.03223  -0.00402 0.08185  64  LEU A C   
397  O O   . LEU A 57  ? 0.58708 0.70571 0.66536 0.04098  0.00001  0.09561  64  LEU A O   
398  C CB  . LEU A 57  ? 0.54653 0.60150 0.60116 0.03231  0.00705  0.07192  64  LEU A CB  
399  C CG  . LEU A 57  ? 0.54980 0.58669 0.59850 0.03510  0.01118  0.06484  64  LEU A CG  
400  C CD1 . LEU A 57  ? 0.60547 0.59050 0.62348 0.03972  0.01959  0.06376  64  LEU A CD1 
401  C CD2 . LEU A 57  ? 0.55655 0.61747 0.62641 0.04594  0.01603  0.07546  64  LEU A CD2 
402  N N   . THR A 58  ? 0.47406 0.59033 0.53927 0.02585  -0.00803 0.07757  65  THR A N   
403  C CA  . THR A 58  ? 0.53768 0.67082 0.60127 0.02935  -0.00776 0.08810  65  THR A CA  
404  C C   . THR A 58  ? 0.59389 0.75205 0.65103 0.03326  -0.01692 0.08349  65  THR A C   
405  O O   . THR A 58  ? 0.56375 0.73646 0.61465 0.03992  -0.01716 0.09282  65  THR A O   
406  C CB  . THR A 58  ? 0.55018 0.67515 0.61159 0.02212  -0.00411 0.09338  65  THR A CB  
407  O OG1 . THR A 58  ? 0.56410 0.69162 0.62504 0.01521  -0.00798 0.08315  65  THR A OG1 
408  C CG2 . THR A 58  ? 0.58383 0.67287 0.64165 0.01734  0.00066  0.09925  65  THR A CG2 
409  N N   . ASP A 59  ? 0.56507 0.72315 0.61824 0.03021  -0.02497 0.06942  66  ASP A N   
410  C CA  . ASP A 59  ? 0.57779 0.74553 0.61359 0.03419  -0.03649 0.06218  66  ASP A CA  
411  C C   . ASP A 59  ? 0.56344 0.72581 0.60386 0.02785  -0.04880 0.05222  66  ASP A C   
412  O O   . ASP A 59  ? 0.54589 0.69779 0.58140 0.02430  -0.05047 0.03982  66  ASP A O   
413  C CB  . ASP A 59  ? 0.59685 0.76511 0.61518 0.03907  -0.03190 0.05701  66  ASP A CB  
414  C CG  . ASP A 59  ? 0.68784 0.85515 0.67364 0.04905  -0.04150 0.04964  66  ASP A CG  
415  O OD1 . ASP A 59  ? 0.69753 0.86254 0.67458 0.04773  -0.05649 0.04768  66  ASP A OD1 
416  O OD2 . ASP A 59  ? 0.74269 0.90959 0.70920 0.05910  -0.03470 0.04737  66  ASP A OD2 
417  N N   . PRO A 60  ? 0.55015 0.72219 0.60376 0.02588  -0.05796 0.06070  67  PRO A N   
418  C CA  . PRO A 60  ? 0.54837 0.71997 0.61451 0.01729  -0.07096 0.05723  67  PRO A CA  
419  C C   . PRO A 60  ? 0.53953 0.69841 0.57957 0.01288  -0.08937 0.04217  67  PRO A C   
420  O O   . PRO A 60  ? 0.52431 0.67603 0.57250 0.00389  -0.09927 0.03686  67  PRO A O   
421  C CB  . PRO A 60  ? 0.57066 0.76370 0.66001 0.01682  -0.07806 0.07675  67  PRO A CB  
422  C CG  . PRO A 60  ? 0.55792 0.75545 0.65034 0.02732  -0.06057 0.08874  67  PRO A CG  
423  C CD  . PRO A 60  ? 0.58114 0.76811 0.64532 0.03113  -0.05570 0.07837  67  PRO A CD  
424  N N   . SER A 61  ? 0.55379 0.70572 0.55894 0.02076  -0.09344 0.03616  68  SER A N   
425  C CA  . SER A 61  ? 0.58075 0.70869 0.54764 0.02132  -0.10955 0.02039  68  SER A CA  
426  C C   . SER A 61  ? 0.60583 0.71761 0.56569 0.02348  -0.09975 0.00687  68  SER A C   
427  O O   . SER A 61  ? 0.61192 0.69769 0.54138 0.02396  -0.11241 -0.00662 68  SER A O   
428  C CB  . SER A 61  ? 0.61338 0.73430 0.53652 0.03578  -0.11135 0.01896  68  SER A CB  
429  O OG  . SER A 61  ? 0.67053 0.79660 0.58664 0.04998  -0.08738 0.02010  68  SER A OG  
430  N N   . LYS A 62  ? 0.52228 0.64499 0.50617 0.02463  -0.07943 0.01071  69  LYS A N   
431  C CA  . LYS A 62  ? 0.56600 0.67779 0.54854 0.02509  -0.07190 0.00089  69  LYS A CA  
432  C C   . LYS A 62  ? 0.52856 0.62958 0.52499 0.01326  -0.08272 -0.00514 69  LYS A C   
433  O O   . LYS A 62  ? 0.51785 0.60490 0.50643 0.01400  -0.08107 -0.01493 69  LYS A O   
434  C CB  . LYS A 62  ? 0.51726 0.64150 0.52175 0.02520  -0.05318 0.00856  69  LYS A CB  
435  C CG  . LYS A 62  ? 0.53990 0.67791 0.53811 0.03440  -0.04229 0.01932  69  LYS A CG  
436  C CD  . LYS A 62  ? 0.54906 0.69418 0.55797 0.03464  -0.02953 0.02444  69  LYS A CD  
437  C CE  . LYS A 62  ? 0.56577 0.72937 0.57606 0.04174  -0.01912 0.04100  69  LYS A CE  
438  N NZ  . LYS A 62  ? 0.63400 0.81132 0.65390 0.04402  -0.00939 0.05026  69  LYS A NZ  
439  N N   . LEU A 63  ? 0.47750 0.58787 0.49732 0.00341  -0.09268 0.00397  70  LEU A N   
440  C CA  . LEU A 63  ? 0.50506 0.61119 0.54423 -0.00833 -0.10337 0.00457  70  LEU A CA  
441  C C   . LEU A 63  ? 0.55630 0.64556 0.57652 -0.01743 -0.13122 -0.00021 70  LEU A C   
442  O O   . LEU A 63  ? 0.50047 0.58848 0.54141 -0.03080 -0.14465 0.00480  70  LEU A O   
443  C CB  . LEU A 63  ? 0.53275 0.66214 0.61252 -0.01206 -0.09661 0.02326  70  LEU A CB  
444  C CG  . LEU A 63  ? 0.49581 0.62745 0.58650 -0.00433 -0.07225 0.02652  70  LEU A CG  
445  C CD1 . LEU A 63  ? 0.53442 0.68137 0.65625 -0.00246 -0.06384 0.04562  70  LEU A CD1 
446  C CD2 . LEU A 63  ? 0.44570 0.56083 0.52838 -0.00476 -0.06557 0.01390  70  LEU A CD2 
447  N N   . ASP A 64  ? 0.56542 0.63870 0.54407 -0.01055 -0.14127 -0.00833 71  ASP A N   
448  C CA  . ASP A 64  ? 0.62416 0.66734 0.57027 -0.01929 -0.17185 -0.01598 71  ASP A CA  
449  C C   . ASP A 64  ? 0.61145 0.61996 0.53874 -0.02228 -0.17792 -0.03069 71  ASP A C   
450  O O   . ASP A 64  ? 0.59942 0.58148 0.51467 -0.03734 -0.20629 -0.03354 71  ASP A O   
451  C CB  . ASP A 64  ? 0.64034 0.66462 0.53197 -0.00536 -0.17769 -0.02377 71  ASP A CB  
452  C CG  . ASP A 64  ? 0.68768 0.74170 0.59464 -0.00601 -0.18052 -0.00772 71  ASP A CG  
453  O OD1 . ASP A 64  ? 0.60927 0.69626 0.56824 -0.01763 -0.18051 0.00995  71  ASP A OD1 
454  O OD2 . ASP A 64  ? 0.67614 0.72059 0.54177 0.00776  -0.18088 -0.01093 71  ASP A OD2 
455  N N   . SER A 65  ? 0.58620 0.59347 0.51141 -0.00942 -0.15364 -0.03822 72  SER A N   
456  C CA  . SER A 65  ? 0.58552 0.56358 0.49661 -0.00933 -0.15485 -0.05002 72  SER A CA  
457  C C   . SER A 65  ? 0.67352 0.66775 0.63395 -0.02461 -0.15353 -0.04089 72  SER A C   
458  O O   . SER A 65  ? 0.60722 0.58573 0.56483 -0.02281 -0.14779 -0.04790 72  SER A O   
459  C CB  . SER A 65  ? 0.60120 0.57668 0.49133 0.01257  -0.12940 -0.05763 72  SER A CB  
460  O OG  . SER A 65  ? 0.52389 0.53880 0.44731 0.01662  -0.10736 -0.04646 72  SER A OG  
461  N N   . GLY A 66  ? 0.57425 0.60027 0.57873 -0.03664 -0.15655 -0.02318 73  GLY A N   
462  C CA  . GLY A 66  ? 0.54862 0.59230 0.59850 -0.04658 -0.15155 -0.01034 73  GLY A CA  
463  C C   . GLY A 66  ? 0.53630 0.61760 0.62423 -0.04181 -0.13117 0.00653  73  GLY A C   
464  O O   . GLY A 66  ? 0.49318 0.57956 0.57409 -0.02907 -0.10992 0.00199  73  GLY A O   
465  N N   . LYS A 67  ? 0.55619 0.66233 0.68383 -0.05156 -0.13805 0.02839  74  LYS A N   
466  C CA  . LYS A 67  ? 0.55923 0.69573 0.71764 -0.04240 -0.11671 0.04651  74  LYS A CA  
467  C C   . LYS A 67  ? 0.56043 0.69895 0.73594 -0.03568 -0.09517 0.05147  74  LYS A C   
468  O O   . LYS A 67  ? 0.52903 0.67096 0.70348 -0.02201 -0.07249 0.05418  74  LYS A O   
469  C CB  . LYS A 67  ? 0.57532 0.74272 0.77025 -0.05109 -0.13041 0.07302  74  LYS A CB  
470  C CG  . LYS A 67  ? 0.89659 1.09470 1.12595 -0.03792 -0.10610 0.09725  74  LYS A CG  
471  C CD  . LYS A 67  ? 0.96740 1.15969 1.17344 -0.02132 -0.08639 0.08920  74  LYS A CD  
472  C CE  . LYS A 67  ? 0.83356 1.03946 1.05964 -0.00406 -0.05905 0.10894  74  LYS A CE  
473  N NZ  . LYS A 67  ? 0.76698 1.00329 1.03887 -0.00515 -0.05812 0.13889  74  LYS A NZ  
474  N N   . GLU A 68  ? 0.56126 0.69240 0.74725 -0.04467 -0.10279 0.05252  75  GLU A N   
475  C CA  . GLU A 68  ? 0.56171 0.69549 0.76272 -0.03714 -0.08272 0.05994  75  GLU A CA  
476  C C   . GLU A 68  ? 0.50961 0.62061 0.67707 -0.02554 -0.06606 0.03902  75  GLU A C   
477  O O   . GLU A 68  ? 0.49187 0.58342 0.63128 -0.02747 -0.07358 0.01917  75  GLU A O   
478  C CB  . GLU A 68  ? 0.60764 0.73817 0.82771 -0.05076 -0.09644 0.06700  75  GLU A CB  
479  C CG  . GLU A 68  ? 0.77598 0.92285 1.02594 -0.07016 -0.12398 0.08602  75  GLU A CG  
480  C CD  . GLU A 68  ? 1.24779 1.35957 1.46622 -0.08627 -0.15478 0.06631  75  GLU A CD  
481  O OE1 . GLU A 68  ? 1.33603 1.43006 1.55861 -0.09861 -0.16798 0.06673  75  GLU A OE1 
482  O OE2 . GLU A 68  ? 0.97868 1.07659 1.16398 -0.08481 -0.16510 0.05100  75  GLU A OE2 
483  N N   . LEU A 69  ? 0.46987 0.58198 0.63842 -0.01247 -0.04387 0.04571  76  LEU A N   
484  C CA  . LEU A 69  ? 0.46506 0.55506 0.60363 -0.00436 -0.03149 0.02997  76  LEU A CA  
485  C C   . LEU A 69  ? 0.44227 0.52546 0.58433 0.00177  -0.01923 0.03634  76  LEU A C   
486  O O   . LEU A 69  ? 0.43133 0.51760 0.57923 0.01409  -0.00281 0.05179  76  LEU A O   
487  C CB  . LEU A 69  ? 0.45210 0.53693 0.57550 0.00513  -0.01992 0.03023  76  LEU A CB  
488  C CG  . LEU A 69  ? 0.46524 0.56030 0.58755 0.00171  -0.02880 0.02876  76  LEU A CG  
489  C CD1 . LEU A 69  ? 0.47251 0.55975 0.58288 0.01154  -0.01572 0.03324  76  LEU A CD1 
490  C CD2 . LEU A 69  ? 0.38824 0.47633 0.49182 -0.00483 -0.04052 0.01121  76  LEU A CD2 
491  N N   . HIS A 70  ? 0.41709 0.52554 0.54321 0.00533  -0.03574 0.07551  77  HIS A N   
492  C CA  . HIS A 70  ? 0.39962 0.49406 0.51973 -0.00006 -0.02911 0.06784  77  HIS A CA  
493  C C   . HIS A 70  ? 0.43602 0.50431 0.52343 -0.00605 -0.03610 0.04872  77  HIS A C   
494  O O   . HIS A 70  ? 0.39287 0.45579 0.46599 -0.00732 -0.04667 0.04160  77  HIS A O   
495  C CB  . HIS A 70  ? 0.43939 0.55616 0.57672 -0.00901 -0.03699 0.07757  77  HIS A CB  
496  C CG  . HIS A 70  ? 0.45839 0.58497 0.58630 -0.02154 -0.05988 0.07338  77  HIS A CG  
497  N ND1 . HIS A 70  ? 0.45094 0.61175 0.59813 -0.02614 -0.07359 0.08508  77  HIS A ND1 
498  C CD2 . HIS A 70  ? 0.46530 0.57124 0.56563 -0.03053 -0.07048 0.05819  77  HIS A CD2 
499  C CE1 . HIS A 70  ? 0.48811 0.64593 0.61624 -0.03949 -0.09155 0.07401  77  HIS A CE1 
500  N NE2 . HIS A 70  ? 0.48637 0.60898 0.58723 -0.04143 -0.08816 0.05823  77  HIS A NE2 
501  N N   . ILE A 71  ? 0.41616 0.46970 0.49215 -0.00824 -0.02885 0.04247  78  ILE A N   
502  C CA  . ILE A 71  ? 0.41961 0.45335 0.46700 -0.01222 -0.03560 0.02887  78  ILE A CA  
503  C C   . ILE A 71  ? 0.44866 0.48090 0.49260 -0.01897 -0.03755 0.03301  78  ILE A C   
504  O O   . ILE A 71  ? 0.43651 0.47341 0.49199 -0.01827 -0.02529 0.04121  78  ILE A O   
505  C CB  . ILE A 71  ? 0.42262 0.43950 0.45402 -0.00759 -0.02473 0.01733  78  ILE A CB  
506  C CG1 . ILE A 71  ? 0.40247 0.41834 0.44399 -0.00246 -0.01801 0.01370  78  ILE A CG1 
507  C CG2 . ILE A 71  ? 0.45670 0.46136 0.46158 -0.01016 -0.03517 0.00653  78  ILE A CG2 
508  C CD1 . ILE A 71  ? 0.43727 0.43667 0.46717 -0.00134 -0.00520 -0.00019 78  ILE A CD1 
509  N N   . ASN A 72  ? 0.42076 0.44437 0.45056 -0.02486 -0.04982 0.02824  79  ASN A N   
510  C CA  . ASN A 72  ? 0.46130 0.47803 0.48820 -0.03178 -0.04973 0.03226  79  ASN A CA  
511  C C   . ASN A 72  ? 0.47393 0.46933 0.47291 -0.02784 -0.05014 0.02631  79  ASN A C   
512  O O   . ASN A 72  ? 0.47919 0.46773 0.46564 -0.02487 -0.05850 0.01839  79  ASN A O   
513  C CB  . ASN A 72  ? 0.42469 0.44797 0.46206 -0.04346 -0.06177 0.03302  79  ASN A CB  
514  C CG  . ASN A 72  ? 0.47995 0.53234 0.54799 -0.04882 -0.06366 0.04266  79  ASN A CG  
515  O OD1 . ASN A 72  ? 0.46610 0.53126 0.55287 -0.04416 -0.05182 0.05261  79  ASN A OD1 
516  N ND2 . ASN A 72  ? 0.47586 0.54029 0.54871 -0.05818 -0.07826 0.04021  79  ASN A ND2 
517  N N   . LEU A 73  ? 0.44823 0.43539 0.43867 -0.02654 -0.04027 0.03231  80  LEU A N   
518  C CA  . LEU A 73  ? 0.49236 0.46309 0.45615 -0.02107 -0.04052 0.03180  80  LEU A CA  
519  C C   . LEU A 73  ? 0.53079 0.48884 0.49743 -0.02685 -0.03794 0.04052  80  LEU A C   
520  O O   . LEU A 73  ? 0.53707 0.49698 0.51709 -0.03208 -0.02739 0.04968  80  LEU A O   
521  C CB  . LEU A 73  ? 0.47210 0.44115 0.41660 -0.01375 -0.02973 0.03259  80  LEU A CB  
522  C CG  . LEU A 73  ? 0.51738 0.49429 0.46193 -0.01084 -0.02632 0.02249  80  LEU A CG  
523  C CD1 . LEU A 73  ? 0.52649 0.49740 0.44604 -0.00589 -0.01375 0.02071  80  LEU A CD1 
524  C CD2 . LEU A 73  ? 0.47069 0.44999 0.41114 -0.00945 -0.03961 0.01061  80  LEU A CD2 
525  N N   . ILE A 74  ? 0.49707 0.44096 0.45406 -0.02587 -0.04502 0.03812  81  ILE A N   
526  C CA  . ILE A 74  ? 0.53573 0.46140 0.49749 -0.03284 -0.04066 0.04402  81  ILE A CA  
527  C C   . ILE A 74  ? 0.56173 0.46808 0.50162 -0.02127 -0.03663 0.05160  81  ILE A C   
528  O O   . ILE A 74  ? 0.51622 0.41408 0.44884 -0.01576 -0.04323 0.04732  81  ILE A O   
529  C CB  . ILE A 74  ? 0.55225 0.47467 0.52553 -0.04397 -0.04995 0.03395  81  ILE A CB  
530  C CG1 . ILE A 74  ? 0.53368 0.48198 0.52648 -0.05221 -0.05685 0.02939  81  ILE A CG1 
531  C CG2 . ILE A 74  ? 0.56455 0.46516 0.54508 -0.05547 -0.04321 0.03661  81  ILE A CG2 
532  C CD1 . ILE A 74  ? 0.54030 0.49032 0.53433 -0.05976 -0.06884 0.01825  81  ILE A CD1 
533  N N   . PRO A 75  ? 0.54218 0.44237 0.47145 -0.01560 -0.02473 0.06498  82  PRO A N   
534  C CA  . PRO A 75  ? 0.59706 0.47992 0.50681 -0.00310 -0.02004 0.07716  82  PRO A CA  
535  C C   . PRO A 75  ? 0.67910 0.53395 0.60108 -0.00967 -0.01010 0.08341  82  PRO A C   
536  O O   . PRO A 75  ? 0.65857 0.50793 0.60145 -0.02527 -0.00294 0.08228  82  PRO A O   
537  C CB  . PRO A 75  ? 0.61217 0.49952 0.50309 0.00482  -0.00924 0.08988  82  PRO A CB  
538  C CG  . PRO A 75  ? 0.60973 0.50465 0.52133 -0.00769 -0.00030 0.08809  82  PRO A CG  
539  C CD  . PRO A 75  ? 0.54468 0.45485 0.47743 -0.01762 -0.01344 0.07142  82  PRO A CD  
540  N N   . ASN A 76  ? 0.67471 0.51216 0.58593 0.00208  -0.00891 0.09009  83  ASN A N   
541  C CA  . ASN A 76  ? 0.68809 0.49121 0.60885 -0.00224 0.00422  0.09545  83  ASN A CA  
542  C C   . ASN A 76  ? 0.74154 0.52979 0.64517 0.01873  0.01466  0.11799  83  ASN A C   
543  O O   . ASN A 76  ? 0.70967 0.50039 0.60453 0.03406  0.00789  0.12087  83  ASN A O   
544  C CB  . ASN A 76  ? 0.69916 0.49128 0.62832 -0.00952 -0.00298 0.07801  83  ASN A CB  
545  C CG  . ASN A 76  ? 0.78082 0.53365 0.72088 -0.02072 0.01222  0.07667  83  ASN A CG  
546  O OD1 . ASN A 76  ? 0.77857 0.50441 0.71562 -0.01117 0.02916  0.09351  83  ASN A OD1 
547  N ND2 . ASN A 76  ? 0.78021 0.52904 0.73195 -0.04143 0.00681  0.05652  83  ASN A ND2 
548  N N   . LYS A 77  ? 0.78415 0.55914 0.68507 0.02039  0.03201  0.13622  84  LYS A N   
549  C CA  . LYS A 77  ? 0.82199 0.58490 0.70419 0.04254  0.04318  0.16243  84  LYS A CA  
550  C C   . LYS A 77  ? 0.84040 0.56856 0.73203 0.04923  0.05429  0.16897  84  LYS A C   
551  O O   . LYS A 77  ? 0.82656 0.55438 0.70557 0.07232  0.05516  0.18716  84  LYS A O   
552  C CB  . LYS A 77  ? 0.84479 0.59778 0.72226 0.04234  0.06325  0.18175  84  LYS A CB  
553  C CG  . LYS A 77  ? 0.89407 0.67710 0.74312 0.05246  0.05762  0.18871  84  LYS A CG  
554  C CD  . LYS A 77  ? 0.98062 0.75633 0.83347 0.04444  0.07824  0.19909  84  LYS A CD  
555  C CE  . LYS A 77  ? 1.05762 0.84742 0.87060 0.06244  0.08300  0.21699  84  LYS A CE  
556  N NZ  . LYS A 77  ? 1.09066 0.89586 0.90215 0.05257  0.08869  0.20910  84  LYS A NZ  
557  N N   . GLN A 78  ? 0.85212 0.55145 0.76608 0.02934  0.06336  0.15436  85  GLN A N   
558  C CA  . GLN A 78  ? 0.92951 0.58746 0.85146 0.03382  0.07887  0.15764  85  GLN A CA  
559  C C   . GLN A 78  ? 0.90773 0.57547 0.82413 0.04788  0.06551  0.15030  85  GLN A C   
560  O O   . GLN A 78  ? 0.93192 0.58568 0.84491 0.07036  0.07493  0.16882  85  GLN A O   
561  C CB  . GLN A 78  ? 0.98846 0.61530 0.93227 0.00464  0.08906  0.13723  85  GLN A CB  
562  C CG  . GLN A 78  ? 1.11288 0.69824 1.06162 0.00348  0.10030  0.12677  85  GLN A CG  
563  C CD  . GLN A 78  ? 1.31240 0.84407 1.27346 -0.00112 0.13192  0.13824  85  GLN A CD  
564  O OE1 . GLN A 78  ? 1.38397 0.90958 1.34630 0.00744  0.14742  0.16384  85  GLN A OE1 
565  N NE2 . GLN A 78  ? 1.37280 0.86248 1.34148 -0.01509 0.14376  0.11886  85  GLN A NE2 
566  N N   . ASP A 79  ? 0.83615 0.52907 0.75421 0.03618  0.04515  0.12569  86  ASP A N   
567  C CA  . ASP A 79  ? 0.81366 0.51914 0.72926 0.04828  0.03337  0.11837  86  ASP A CA  
568  C C   . ASP A 79  ? 0.78049 0.52873 0.68463 0.06796  0.01680  0.13086  86  ASP A C   
569  O O   . ASP A 79  ? 0.74736 0.50996 0.65403 0.08041  0.00806  0.12940  86  ASP A O   
570  C CB  . ASP A 79  ? 0.82085 0.53509 0.74172 0.02825  0.02017  0.08866  86  ASP A CB  
571  C CG  . ASP A 79  ? 0.89927 0.57584 0.82828 0.00582  0.03237  0.07224  86  ASP A CG  
572  O OD1 . ASP A 79  ? 0.89021 0.52625 0.82306 0.00734  0.05397  0.08156  86  ASP A OD1 
573  O OD2 . ASP A 79  ? 0.87268 0.56045 0.80408 -0.01376 0.02053  0.05013  86  ASP A OD2 
574  N N   . ARG A 80  ? 0.76661 0.53548 0.65832 0.07001  0.01312  0.14209  87  ARG A N   
575  C CA  . ARG A 80  ? 0.73392 0.54456 0.60988 0.08384  -0.00439 0.14907  87  ARG A CA  
576  C C   . ARG A 80  ? 0.66455 0.50434 0.54624 0.07552  -0.02450 0.12537  87  ARG A C   
577  O O   . ARG A 80  ? 0.62727 0.49300 0.50883 0.08748  -0.03772 0.12661  87  ARG A O   
578  C CB  . ARG A 80  ? 0.76609 0.58167 0.63634 0.11075  -0.00272 0.17489  87  ARG A CB  
579  C CG  . ARG A 80  ? 0.81743 0.66912 0.66290 0.12404  -0.01484 0.19061  87  ARG A CG  
580  C CD  . ARG A 80  ? 0.78849 0.66919 0.63479 0.14676  -0.02767 0.20605  87  ARG A CD  
581  N NE  . ARG A 80  ? 0.91015 0.76722 0.76107 0.16870  -0.00954 0.23689  87  ARG A NE  
582  C CZ  . ARG A 80  ? 1.00947 0.87977 0.87419 0.19024  -0.01262 0.25350  87  ARG A CZ  
583  N NH1 . ARG A 80  ? 0.86209 0.77147 0.73886 0.19156  -0.03415 0.24185  87  ARG A NH1 
584  N NH2 . ARG A 80  ? 0.93014 0.77387 0.80021 0.21154  0.00837  0.28404  87  ARG A NH2 
585  N N   . THR A 81  ? 0.64395 0.48104 0.53360 0.05486  -0.02617 0.10519  88  THR A N   
586  C CA  . THR A 81  ? 0.62007 0.48051 0.51611 0.04655  -0.04145 0.08455  88  THR A CA  
587  C C   . THR A 81  ? 0.59455 0.47150 0.48771 0.03342  -0.04557 0.07545  88  THR A C   
588  O O   . THR A 81  ? 0.60426 0.46837 0.50058 0.02322  -0.03543 0.07800  88  THR A O   
589  C CB  . THR A 81  ? 0.62560 0.46684 0.53540 0.03650  -0.03880 0.06919  88  THR A CB  
590  O OG1 . THR A 81  ? 0.64716 0.46599 0.56222 0.01925  -0.02928 0.06396  88  THR A OG1 
591  C CG2 . THR A 81  ? 0.65641 0.47777 0.56985 0.05097  -0.03071 0.07713  88  THR A CG2 
592  N N   . LEU A 82  ? 0.54880 0.45371 0.43914 0.03371  -0.05850 0.06529  89  LEU A N   
593  C CA  . LEU A 82  ? 0.52944 0.44812 0.42076 0.02247  -0.06036 0.05455  89  LEU A CA  
594  C C   . LEU A 82  ? 0.54222 0.46901 0.44947 0.01452  -0.06778 0.03809  89  LEU A C   
595  O O   . LEU A 82  ? 0.54383 0.48273 0.45347 0.02012  -0.07635 0.03234  89  LEU A O   
596  C CB  . LEU A 82  ? 0.54490 0.48438 0.41677 0.02852  -0.06543 0.05526  89  LEU A CB  
597  C CG  . LEU A 82  ? 0.56744 0.51752 0.44034 0.01885  -0.06366 0.04313  89  LEU A CG  
598  C CD1 . LEU A 82  ? 0.52901 0.46671 0.41085 0.01062  -0.04977 0.04881  89  LEU A CD1 
599  C CD2 . LEU A 82  ? 0.55777 0.52302 0.40538 0.02363  -0.06707 0.04046  89  LEU A CD2 
600  N N   . THR A 83  ? 0.46135 0.38393 0.38092 0.00189  -0.06429 0.03231  90  THR A N   
601  C CA  . THR A 83  ? 0.49180 0.42085 0.42391 -0.00485 -0.07013 0.02014  90  THR A CA  
602  C C   . THR A 83  ? 0.53589 0.48347 0.47548 -0.00978 -0.07055 0.01546  90  THR A C   
603  O O   . THR A 83  ? 0.51277 0.46246 0.45601 -0.01448 -0.06381 0.02068  90  THR A O   
604  C CB  . THR A 83  ? 0.54176 0.45419 0.48126 -0.01550 -0.06760 0.01748  90  THR A CB  
605  O OG1 . THR A 83  ? 0.59582 0.48532 0.52858 -0.00973 -0.06351 0.02013  90  THR A OG1 
606  C CG2 . THR A 83  ? 0.50578 0.42832 0.45278 -0.02189 -0.07434 0.00669  90  THR A CG2 
607  N N   . ILE A 84  ? 0.45105 0.41066 0.39544 -0.00784 -0.07566 0.00698  91  ILE A N   
608  C CA  . ILE A 84  ? 0.48551 0.45882 0.43950 -0.01071 -0.07301 0.00303  91  ILE A CA  
609  C C   . ILE A 84  ? 0.50537 0.48340 0.47233 -0.01438 -0.07619 -0.00034 91  ILE A C   
610  O O   . ILE A 84  ? 0.47047 0.44795 0.43700 -0.01086 -0.07999 -0.00556 91  ILE A O   
611  C CB  . ILE A 84  ? 0.50208 0.48361 0.44990 -0.00589 -0.07350 -0.00401 91  ILE A CB  
612  C CG1 . ILE A 84  ? 0.56333 0.54276 0.49094 -0.00178 -0.07281 -0.00025 91  ILE A CG1 
613  C CG2 . ILE A 84  ? 0.49559 0.48424 0.45444 -0.00850 -0.06579 -0.00823 91  ILE A CG2 
614  C CD1 . ILE A 84  ? 0.63301 0.62090 0.55114 0.00385  -0.08224 -0.00471 91  ILE A CD1 
615  N N   . VAL A 85  ? 0.44440 0.42972 0.42339 -0.02080 -0.07444 0.00415  92  VAL A N   
616  C CA  . VAL A 85  ? 0.46017 0.45420 0.44793 -0.02430 -0.07923 0.00363  92  VAL A CA  
617  C C   . VAL A 85  ? 0.45503 0.46560 0.45869 -0.02099 -0.07366 0.00810  92  VAL A C   
618  O O   . VAL A 85  ? 0.44928 0.46639 0.46314 -0.02113 -0.06617 0.01407  92  VAL A O   
619  C CB  . VAL A 85  ? 0.45805 0.45258 0.44924 -0.03548 -0.08428 0.00615  92  VAL A CB  
620  C CG1 . VAL A 85  ? 0.43689 0.44363 0.43030 -0.03930 -0.09213 0.00481  92  VAL A CG1 
621  C CG2 . VAL A 85  ? 0.47998 0.45121 0.45701 -0.03850 -0.08464 0.00215  92  VAL A CG2 
622  N N   . ASP A 86  ? 0.41490 0.43030 0.42151 -0.01675 -0.07431 0.00668  93  ASP A N   
623  C CA  . ASP A 86  ? 0.40247 0.43186 0.42638 -0.01211 -0.06719 0.01421  93  ASP A CA  
624  C C   . ASP A 86  ? 0.42316 0.46396 0.44799 -0.01170 -0.07389 0.01960  93  ASP A C   
625  O O   . ASP A 86  ? 0.42691 0.45954 0.43557 -0.01366 -0.08094 0.01320  93  ASP A O   
626  C CB  . ASP A 86  ? 0.39732 0.41916 0.42444 -0.00571 -0.05622 0.00836  93  ASP A CB  
627  C CG  . ASP A 86  ? 0.44743 0.46282 0.46860 -0.00316 -0.05868 0.00137  93  ASP A CG  
628  O OD1 . ASP A 86  ? 0.45877 0.47970 0.48432 0.00030  -0.05792 0.00713  93  ASP A OD1 
629  O OD2 . ASP A 86  ? 0.42335 0.43040 0.43632 -0.00384 -0.06088 -0.00832 93  ASP A OD2 
630  N N   . THR A 87  ? 0.39514 0.45532 0.43782 -0.00790 -0.07054 0.03265  94  THR A N   
631  C CA  . THR A 87  ? 0.41960 0.49591 0.46160 -0.00524 -0.07689 0.04147  94  THR A CA  
632  C C   . THR A 87  ? 0.40062 0.47444 0.45001 0.00704  -0.06382 0.04760  94  THR A C   
633  O O   . THR A 87  ? 0.39452 0.48675 0.45507 0.01454  -0.06157 0.06366  94  THR A O   
634  C CB  . THR A 87  ? 0.44145 0.54776 0.50108 -0.00844 -0.08411 0.05597  94  THR A CB  
635  O OG1 . THR A 87  ? 0.41541 0.52853 0.50137 -0.00174 -0.06998 0.06628  94  THR A OG1 
636  C CG2 . THR A 87  ? 0.41088 0.51883 0.46333 -0.02401 -0.09782 0.04824  94  THR A CG2 
637  N N   . GLY A 88  ? 0.40999 0.46266 0.45543 0.00912  -0.05478 0.03616  95  GLY A N   
638  C CA  . GLY A 88  ? 0.41330 0.45945 0.46939 0.01794  -0.03979 0.03939  95  GLY A CA  
639  C C   . GLY A 88  ? 0.41641 0.46406 0.46105 0.02255  -0.04175 0.04387  95  GLY A C   
640  O O   . GLY A 88  ? 0.44547 0.50322 0.47286 0.01999  -0.05491 0.04687  95  GLY A O   
641  N N   . ILE A 89  ? 0.37050 0.40664 0.42393 0.02838  -0.02710 0.04314  96  ILE A N   
642  C CA  . ILE A 89  ? 0.41375 0.44971 0.45793 0.03509  -0.02342 0.05020  96  ILE A CA  
643  C C   . ILE A 89  ? 0.42728 0.45542 0.44736 0.03006  -0.03390 0.03773  96  ILE A C   
644  O O   . ILE A 89  ? 0.44831 0.47818 0.44984 0.03434  -0.03489 0.04315  96  ILE A O   
645  C CB  . ILE A 89  ? 0.44153 0.46496 0.50689 0.04132  -0.00161 0.05258  96  ILE A CB  
646  C CG1 . ILE A 89  ? 0.51307 0.53753 0.57025 0.05114  0.00648  0.06592  96  ILE A CG1 
647  C CG2 . ILE A 89  ? 0.43122 0.44022 0.50400 0.03280  0.00048  0.03220  96  ILE A CG2 
648  C CD1 . ILE A 89  ? 0.54391 0.56014 0.62625 0.06044  0.03132  0.07868  96  ILE A CD1 
649  N N   . GLY A 90  ? 0.39767 0.41657 0.41578 0.02237  -0.04028 0.02232  97  GLY A N   
650  C CA  . GLY A 90  ? 0.42820 0.43719 0.42807 0.02016  -0.04622 0.01239  97  GLY A CA  
651  C C   . GLY A 90  ? 0.45544 0.45644 0.46600 0.02505  -0.03401 0.00903  97  GLY A C   
652  O O   . GLY A 90  ? 0.40527 0.40701 0.43832 0.02756  -0.02154 0.01195  97  GLY A O   
653  N N   . MET A 91  ? 0.40636 0.39863 0.40302 0.02605  -0.03571 0.00278  98  MET A N   
654  C CA  . MET A 91  ? 0.45812 0.44617 0.46969 0.03053  -0.02455 -0.00009 98  MET A CA  
655  C C   . MET A 91  ? 0.47261 0.45098 0.46195 0.03706  -0.01816 0.00203  98  MET A C   
656  O O   . MET A 91  ? 0.48769 0.45712 0.44990 0.03508  -0.02596 -0.00285 98  MET A O   
657  C CB  . MET A 91  ? 0.47810 0.46725 0.50259 0.02676  -0.03126 -0.01023 98  MET A CB  
658  C CG  . MET A 91  ? 0.48011 0.47833 0.52658 0.02048  -0.03339 -0.01475 98  MET A CG  
659  S SD  . MET A 91  ? 0.43318 0.43942 0.49006 0.01696  -0.04424 -0.02459 98  MET A SD  
660  C CE  . MET A 91  ? 0.47283 0.47234 0.50256 0.01466  -0.05736 -0.02409 98  MET A CE  
661  N N   . THR A 92  ? 0.48389 0.46150 0.48392 0.04421  -0.00175 0.00862  99  THR A N   
662  C CA  . THR A 92  ? 0.50182 0.46844 0.47980 0.05200  0.00885  0.01088  99  THR A CA  
663  C C   . THR A 92  ? 0.54005 0.49969 0.52835 0.05429  0.01279  0.00268  99  THR A C   
664  O O   . THR A 92  ? 0.43112 0.39879 0.44510 0.05021  0.00570  -0.00288 99  THR A O   
665  C CB  . THR A 92  ? 0.50972 0.47779 0.49708 0.06040  0.02845  0.02401  99  THR A CB  
666  O OG1 . THR A 92  ? 0.51620 0.48962 0.54797 0.05928  0.03938  0.02306  99  THR A OG1 
667  C CG2 . THR A 92  ? 0.51366 0.49041 0.49443 0.06146  0.02618  0.03651  99  THR A CG2 
668  N N   . LYS A 93  ? 0.54511 0.49059 0.51200 0.06210  0.02510  0.00307  100 LYS A N   
669  C CA  . LYS A 93  ? 0.56212 0.50144 0.54349 0.06783  0.03357  -0.00112 100 LYS A CA  
670  C C   . LYS A 93  ? 0.51408 0.47089 0.54550 0.07019  0.04383  0.00395  100 LYS A C   
671  O O   . LYS A 93  ? 0.53683 0.50410 0.59738 0.07041  0.04016  0.00097  100 LYS A O   
672  C CB  . LYS A 93  ? 0.60713 0.52405 0.55354 0.07666  0.04944  -0.00204 100 LYS A CB  
673  C CG  . LYS A 93  ? 0.62671 0.53391 0.58686 0.08488  0.06057  -0.00519 100 LYS A CG  
674  C CD  . LYS A 93  ? 0.68454 0.56354 0.60525 0.09376  0.08000  -0.00826 100 LYS A CD  
675  C CE  . LYS A 93  ? 0.76939 0.63445 0.70255 0.10293  0.09155  -0.01128 100 LYS A CE  
676  N NZ  . LYS A 93  ? 0.77934 0.61709 0.68378 0.11467  0.11888  -0.01268 100 LYS A NZ  
677  N N   . ALA A 94  ? 0.52362 0.48540 0.56742 0.07157  0.05675  0.01246  101 ALA A N   
678  C CA  . ALA A 94  ? 0.53366 0.51152 0.62884 0.06993  0.06724  0.01533  101 ALA A CA  
679  C C   . ALA A 94  ? 0.52158 0.51660 0.64509 0.05741  0.04968  0.00710  101 ALA A C   
680  O O   . ALA A 94  ? 0.51112 0.52385 0.67633 0.05283  0.04979  0.00346  101 ALA A O   
681  C CB  . ALA A 94  ? 0.51896 0.49315 0.61985 0.07387  0.08797  0.02733  101 ALA A CB  
682  N N   . ASP A 95  ? 0.45497 0.44682 0.55641 0.05133  0.03472  0.00386  102 ASP A N   
683  C CA  . ASP A 95  ? 0.45616 0.46064 0.57611 0.04019  0.01949  -0.00508 102 ASP A CA  
684  C C   . ASP A 95  ? 0.50345 0.51804 0.62917 0.03933  0.00502  -0.01190 102 ASP A C   
685  O O   . ASP A 95  ? 0.47547 0.50882 0.63076 0.03227  -0.00235 -0.01817 102 ASP A O   
686  C CB  . ASP A 95  ? 0.44717 0.44527 0.54124 0.03631  0.00939  -0.00488 102 ASP A CB  
687  C CG  . ASP A 95  ? 0.47398 0.46817 0.57376 0.03720  0.02281  0.00381  102 ASP A CG  
688  O OD1 . ASP A 95  ? 0.40959 0.40565 0.54056 0.03583  0.03817  0.00521  102 ASP A OD1 
689  O OD2 . ASP A 95  ? 0.47988 0.47019 0.55589 0.03936  0.01874  0.01045  102 ASP A OD2 
690  N N   . LEU A 96  ? 0.47558 0.47793 0.57278 0.04637  0.00128  -0.01052 103 LEU A N   
691  C CA  . LEU A 96  ? 0.49578 0.50418 0.59539 0.04799  -0.01104 -0.01339 103 LEU A CA  
692  C C   . LEU A 96  ? 0.50090 0.52667 0.63705 0.05433  -0.00472 -0.01008 103 LEU A C   
693  O O   . LEU A 96  ? 0.54440 0.59019 0.69981 0.05342  -0.01739 -0.01090 103 LEU A O   
694  C CB  . LEU A 96  ? 0.47771 0.46255 0.53885 0.05315  -0.01234 -0.01315 103 LEU A CB  
695  C CG  . LEU A 96  ? 0.48593 0.45876 0.51452 0.04570  -0.02104 -0.01586 103 LEU A CG  
696  C CD1 . LEU A 96  ? 0.51420 0.46255 0.50715 0.04833  -0.01885 -0.01814 103 LEU A CD1 
697  C CD2 . LEU A 96  ? 0.45330 0.43647 0.48644 0.03783  -0.03695 -0.01892 103 LEU A CD2 
698  N N   . ILE A 97  ? 0.47571 0.49698 0.62269 0.06154  0.01498  -0.00465 104 ILE A N   
699  C CA  . ILE A 97  ? 0.53341 0.57152 0.71765 0.06983  0.02397  0.00098  104 ILE A CA  
700  C C   . ILE A 97  ? 0.54467 0.61199 0.77948 0.06095  0.02600  -0.00001 104 ILE A C   
701  O O   . ILE A 97  ? 0.54203 0.63963 0.81601 0.06019  0.01832  0.00098  104 ILE A O   
702  C CB  . ILE A 97  ? 0.57948 0.59448 0.74735 0.08380  0.04790  0.00751  104 ILE A CB  
703  C CG1 . ILE A 97  ? 0.55922 0.54243 0.67528 0.08871  0.04577  0.00413  104 ILE A CG1 
704  C CG2 . ILE A 97  ? 0.59855 0.63164 0.80927 0.09476  0.06026  0.01566  104 ILE A CG2 
705  C CD1 . ILE A 97  ? 0.58100 0.53509 0.66370 0.09767  0.06800  0.00542  104 ILE A CD1 
706  N N   . ASN A 98  ? 0.53681 0.59700 0.77386 0.05364  0.03634  -0.00146 105 ASN A N   
707  C CA  . ASN A 98  ? 0.56532 0.64591 0.85284 0.04519  0.04621  -0.00213 105 ASN A CA  
708  C C   . ASN A 98  ? 0.53263 0.61530 0.82751 0.02827  0.03927  -0.01244 105 ASN A C   
709  O O   . ASN A 98  ? 0.52949 0.63727 0.85670 0.01484  0.02661  -0.02263 105 ASN A O   
710  C CB  . ASN A 98  ? 0.58918 0.65518 0.88181 0.05482  0.07604  0.00906  105 ASN A CB  
711  C CG  . ASN A 98  ? 0.74630 0.82900 1.07552 0.06461  0.08908  0.01699  105 ASN A CG  
712  O OD1 . ASN A 98  ? 0.92234 0.98652 1.22980 0.08028  0.10628  0.02557  105 ASN A OD1 
713  N ND2 . ASN A 98  ? 0.68520 0.80426 1.07102 0.05503  0.08159  0.01380  105 ASN A ND2 
714  N N   . ASN A 99  ? 0.71980 0.70517 0.56203 0.07053  -0.03454 0.14870  106 ASN A N   
715  C CA  . ASN A 99  ? 0.70371 0.68525 0.59352 0.04026  -0.04416 0.16989  106 ASN A CA  
716  C C   . ASN A 99  ? 0.70237 0.66839 0.64867 0.02187  -0.05877 0.15055  106 ASN A C   
717  O O   . ASN A 99  ? 0.78703 0.76265 0.78144 -0.00202 -0.05634 0.16205  106 ASN A O   
718  C CB  . ASN A 99  ? 0.69989 0.64610 0.55335 0.04110  -0.06433 0.18111  106 ASN A CB  
719  C CG  . ASN A 99  ? 0.77108 0.73118 0.55330 0.06018  -0.04922 0.20156  106 ASN A CG  
720  O OD1 . ASN A 99  ? 0.78714 0.79197 0.56772 0.06475  -0.01643 0.22226  106 ASN A OD1 
721  N ND2 . ASN A 99  ? 0.83035 0.75660 0.55291 0.07174  -0.07307 0.19716  106 ASN A ND2 
722  N N   . LEU A 100 ? 0.66869 0.60803 0.60732 0.03156  -0.07352 0.12137  107 LEU A N   
723  C CA  . LEU A 100 ? 0.68366 0.61123 0.66845 0.01683  -0.08220 0.10571  107 LEU A CA  
724  C C   . LEU A 100 ? 0.67824 0.64044 0.68850 0.01172  -0.06816 0.10288  107 LEU A C   
725  O O   . LEU A 100 ? 0.67061 0.63341 0.71650 -0.00741 -0.07095 0.09894  107 LEU A O   
726  C CB  . LEU A 100 ? 0.68660 0.58198 0.66209 0.02584  -0.09952 0.08260  107 LEU A CB  
727  C CG  . LEU A 100 ? 0.64234 0.50973 0.61634 0.02359  -0.12188 0.08613  107 LEU A CG  
728  C CD1 . LEU A 100 ? 0.67928 0.52456 0.66448 0.02517  -0.13970 0.06645  107 LEU A CD1 
729  C CD2 . LEU A 100 ? 0.60188 0.46604 0.61840 0.00816  -0.12206 0.10135  107 LEU A CD2 
730  N N   . GLY A 101 ? 0.66595 0.65678 0.65634 0.03082  -0.05422 0.10413  108 GLY A N   
731  C CA  . GLY A 101 ? 0.66210 0.69769 0.68334 0.02751  -0.04380 0.10849  108 GLY A CA  
732  C C   . GLY A 101 ? 0.68582 0.76215 0.74396 0.00370  -0.03598 0.13334  108 GLY A C   
733  O O   . GLY A 101 ? 0.70248 0.80618 0.79858 -0.01470 -0.04025 0.13421  108 GLY A O   
734  N N   . THR A 102 ? 0.68283 0.76275 0.72912 0.00139  -0.02675 0.15557  109 THR A N   
735  C CA  . THR A 102 ? 0.67221 0.78443 0.75960 -0.02701 -0.01987 0.18465  109 THR A CA  
736  C C   . THR A 102 ? 0.69485 0.76704 0.81330 -0.05923 -0.03991 0.17646  109 THR A C   
737  O O   . THR A 102 ? 0.74090 0.83364 0.90273 -0.08806 -0.04426 0.18317  109 THR A O   
738  C CB  . THR A 102 ? 0.67065 0.78989 0.73107 -0.02070 -0.00344 0.21519  109 THR A CB  
739  O OG1 . THR A 102 ? 0.69387 0.85218 0.72054 0.01275  0.02072  0.21991  109 THR A OG1 
740  C CG2 . THR A 102 ? 0.63627 0.78339 0.74601 -0.05533 0.00368  0.25144  109 THR A CG2 
741  N N   . ILE A 103 ? 0.67426 0.68894 0.77255 -0.05402 -0.05317 0.16080  110 ILE A N   
742  C CA  . ILE A 103 ? 0.72026 0.69167 0.84445 -0.07532 -0.06765 0.14788  110 ILE A CA  
743  C C   . ILE A 103 ? 0.73113 0.70869 0.86792 -0.08225 -0.07410 0.12043  110 ILE A C   
744  O O   . ILE A 103 ? 0.78471 0.74317 0.94329 -0.10600 -0.08276 0.11039  110 ILE A O   
745  C CB  . ILE A 103 ? 0.72979 0.65080 0.83732 -0.06114 -0.07783 0.13986  110 ILE A CB  
746  C CG1 . ILE A 103 ? 0.70005 0.61399 0.78999 -0.05645 -0.07670 0.17127  110 ILE A CG1 
747  C CG2 . ILE A 103 ? 0.68413 0.56078 0.81887 -0.07385 -0.08681 0.12277  110 ILE A CG2 
748  C CD1 . ILE A 103 ? 0.68903 0.59040 0.80918 -0.08207 -0.07458 0.19909  110 ILE A CD1 
749  N N   . ALA A 104 ? 0.69383 0.69354 0.81194 -0.06146 -0.07098 0.10824  111 ALA A N   
750  C CA  . ALA A 104 ? 0.71069 0.71500 0.83123 -0.06408 -0.07743 0.08659  111 ALA A CA  
751  C C   . ALA A 104 ? 0.68155 0.73809 0.82572 -0.07998 -0.08058 0.09467  111 ALA A C   
752  O O   . ALA A 104 ? 0.67361 0.73306 0.81624 -0.08759 -0.09115 0.07823  111 ALA A O   
753  C CB  . ALA A 104 ? 0.62527 0.62606 0.71961 -0.03630 -0.07453 0.07549  111 ALA A CB  
754  N N   . LYS A 105 ? 0.68622 0.78909 0.85299 -0.08519 -0.07204 0.12176  112 LYS A N   
755  C CA  . LYS A 105 ? 0.66058 0.82729 0.86398 -0.10061 -0.07717 0.13397  112 LYS A CA  
756  C C   . LYS A 105 ? 0.65576 0.80562 0.88033 -0.14051 -0.09985 0.12135  112 LYS A C   
757  O O   . LYS A 105 ? 0.64765 0.82239 0.87749 -0.14989 -0.11677 0.11013  112 LYS A O   
758  C CB  . LYS A 105 ? 0.67474 0.90039 0.90894 -0.10108 -0.05906 0.17033  112 LYS A CB  
759  C CG  . LYS A 105 ? 0.70113 1.00582 0.99161 -0.12074 -0.06648 0.18823  112 LYS A CG  
760  C CD  . LYS A 105 ? 0.70876 1.08308 1.04231 -0.12353 -0.04329 0.22996  112 LYS A CD  
761  C CE  . LYS A 105 ? 0.75614 1.14513 1.05349 -0.07468 -0.01054 0.23933  112 LYS A CE  
762  N NZ  . LYS A 105 ? 0.72860 1.21055 1.06585 -0.05164 0.00715  0.26156  112 LYS A NZ  
763  N N   . SER A 106 ? 0.69917 0.80197 0.93194 -0.16363 -0.10263 0.12265  113 SER A N   
764  C CA  . SER A 106 ? 0.70341 0.77594 0.95206 -0.20227 -0.12506 0.10636  113 SER A CA  
765  C C   . SER A 106 ? 0.71367 0.73893 0.92053 -0.19446 -0.13585 0.06536  113 SER A C   
766  O O   . SER A 106 ? 0.66746 0.69615 0.87045 -0.21607 -0.15710 0.04622  113 SER A O   
767  C CB  . SER A 106 ? 0.73558 0.75457 1.00078 -0.22371 -0.12362 0.11790  113 SER A CB  
768  O OG  . SER A 106 ? 0.81194 0.79537 1.05199 -0.19427 -0.10670 0.12399  113 SER A OG  
769  N N   . GLY A 107 ? 0.70919 0.69375 0.88388 -0.16444 -0.12186 0.05291  114 GLY A N   
770  C CA  . GLY A 107 ? 0.72027 0.66887 0.85803 -0.15375 -0.12423 0.01966  114 GLY A CA  
771  C C   . GLY A 107 ? 0.67808 0.67313 0.79713 -0.14423 -0.13013 0.01584  114 GLY A C   
772  O O   . GLY A 107 ? 0.69398 0.67526 0.78343 -0.15090 -0.14078 -0.00811 114 GLY A O   
773  N N   . THR A 108 ? 0.64458 0.69205 0.77581 -0.12579 -0.12281 0.03984  115 THR A N   
774  C CA  . THR A 108 ? 0.61996 0.71289 0.74064 -0.11364 -0.12952 0.04305  115 THR A CA  
775  C C   . THR A 108 ? 0.62298 0.75806 0.76227 -0.14328 -0.15526 0.04414  115 THR A C   
776  O O   . THR A 108 ? 0.62339 0.76511 0.73458 -0.14599 -0.17155 0.03081  115 THR A O   
777  C CB  . THR A 108 ? 0.58047 0.71386 0.71419 -0.08437 -0.11483 0.06770  115 THR A CB  
778  O OG1 . THR A 108 ? 0.62951 0.71890 0.74160 -0.06142 -0.09843 0.06288  115 THR A OG1 
779  C CG2 . THR A 108 ? 0.55717 0.73237 0.68463 -0.06717 -0.12182 0.07471  115 THR A CG2 
780  N N   . LYS A 109 ? 0.62847 0.79507 0.81557 -0.16776 -0.16089 0.06263  116 LYS A N   
781  C CA  . LYS A 109 ? 0.63939 0.85241 0.85809 -0.20304 -0.19055 0.06665  116 LYS A CA  
782  C C   . LYS A 109 ? 0.68744 0.84374 0.86651 -0.23043 -0.21574 0.02856  116 LYS A C   
783  O O   . LYS A 109 ? 0.72396 0.90699 0.88699 -0.24291 -0.24378 0.01827  116 LYS A O   
784  C CB  . LYS A 109 ? 0.64636 0.89299 0.92901 -0.23021 -0.18833 0.09529  116 LYS A CB  
785  C CG  . LYS A 109 ? 0.65272 1.00293 0.99289 -0.22257 -0.18421 0.13387  116 LYS A CG  
786  C CD  . LYS A 109 ? 0.73051 1.13991 1.12023 -0.26513 -0.22169 0.14092  116 LYS A CD  
787  C CE  . LYS A 109 ? 0.73519 1.26076 1.19057 -0.25054 -0.21724 0.18137  116 LYS A CE  
788  N NZ  . LYS A 109 ? 0.66896 1.23627 1.13442 -0.26435 -0.25293 0.17552  116 LYS A NZ  
789  N N   . ALA A 110 ? 0.69950 0.77535 0.85814 -0.23695 -0.20640 0.00667  117 ALA A N   
790  C CA  . ALA A 110 ? 0.71546 0.72605 0.82981 -0.25750 -0.22500 -0.03479 117 ALA A CA  
791  C C   . ALA A 110 ? 0.75382 0.75091 0.80037 -0.23081 -0.22070 -0.05862 117 ALA A C   
792  O O   . ALA A 110 ? 0.78717 0.76392 0.78761 -0.24693 -0.24359 -0.08849 117 ALA A O   
793  C CB  . ALA A 110 ? 0.75966 0.68575 0.87336 -0.26160 -0.21076 -0.04949 117 ALA A CB  
794  N N   . PHE A 111 ? 0.70299 0.70885 0.73932 -0.19192 -0.19252 -0.04532 118 PHE A N   
795  C CA  . PHE A 111 ? 0.74727 0.74165 0.72498 -0.16799 -0.18393 -0.06013 118 PHE A CA  
796  C C   . PHE A 111 ? 0.75970 0.81126 0.71824 -0.17238 -0.20990 -0.05188 118 PHE A C   
797  O O   . PHE A 111 ? 0.79071 0.82555 0.68681 -0.17203 -0.21882 -0.07333 118 PHE A O   
798  C CB  . PHE A 111 ? 0.67460 0.66759 0.65830 -0.13180 -0.15235 -0.04266 118 PHE A CB  
799  C CG  . PHE A 111 ? 0.69322 0.67419 0.62633 -0.10955 -0.13860 -0.05060 118 PHE A CG  
800  C CD1 . PHE A 111 ? 0.74051 0.67933 0.62058 -0.11307 -0.13502 -0.08217 118 PHE A CD1 
801  C CD2 . PHE A 111 ? 0.62631 0.63470 0.56289 -0.08448 -0.12711 -0.02562 118 PHE A CD2 
802  C CE1 . PHE A 111 ? 0.78321 0.71722 0.61609 -0.09240 -0.11689 -0.08384 118 PHE A CE1 
803  C CE2 . PHE A 111 ? 0.66134 0.65901 0.55628 -0.06749 -0.11294 -0.02601 118 PHE A CE2 
804  C CZ  . PHE A 111 ? 0.74761 0.71299 0.59137 -0.07168 -0.10616 -0.05270 118 PHE A CZ  
805  N N   . MET A 112 ? 0.72894 0.85100 0.73914 -0.17376 -0.22136 -0.01907 119 MET A N   
806  C CA  . MET A 112 ? 0.76125 0.94772 0.76629 -0.17382 -0.24848 -0.00397 119 MET A CA  
807  C C   . MET A 112 ? 0.75236 0.94997 0.74975 -0.21639 -0.29215 -0.02279 119 MET A C   
808  O O   . MET A 112 ? 0.84051 1.06291 0.79620 -0.21924 -0.31994 -0.02693 119 MET A O   
809  C CB  . MET A 112 ? 0.68800 0.94867 0.75889 -0.15609 -0.24301 0.03754  119 MET A CB  
810  C CG  . MET A 112 ? 0.69343 0.93119 0.77158 -0.11980 -0.20370 0.05005  119 MET A CG  
811  S SD  . MET A 112 ? 0.87391 1.16904 0.97558 -0.07622 -0.19316 0.08682  119 MET A SD  
812  C CE  . MET A 112 ? 0.59610 0.95804 0.77828 -0.08182 -0.18771 0.11313  119 MET A CE  
813  N N   . GLU A 113 ? 0.79850 0.97570 0.83402 -0.25154 -0.30184 -0.03287 120 GLU A N   
814  C CA  . GLU A 113 ? 0.88795 1.05364 0.90986 -0.29779 -0.34627 -0.05933 120 GLU A CA  
815  C C   . GLU A 113 ? 0.94309 1.02866 0.86386 -0.29533 -0.34929 -0.10807 120 GLU A C   
816  O O   . GLU A 113 ? 1.03656 1.12511 0.91233 -0.31056 -0.38175 -0.13007 120 GLU A O   
817  C CB  . GLU A 113 ? 0.92570 1.06690 1.00860 -0.33111 -0.34618 -0.05941 120 GLU A CB  
818  C CG  . GLU A 113 ? 0.91166 1.13497 1.09095 -0.33373 -0.33719 -0.01027 120 GLU A CG  
819  C CD  . GLU A 113 ? 1.10861 1.30153 1.33870 -0.36350 -0.33027 -0.00659 120 GLU A CD  
820  O OE1 . GLU A 113 ? 1.27287 1.44651 1.50615 -0.39478 -0.35413 -0.02671 120 GLU A OE1 
821  O OE2 . GLU A 113 ? 1.04914 1.23635 1.31359 -0.35536 -0.30170 0.01762  120 GLU A OE2 
822  N N   . ALA A 114 ? 0.91768 0.93497 0.80541 -0.26720 -0.30752 -0.12431 121 ALA A N   
823  C CA  . ALA A 114 ? 0.98799 0.93521 0.78155 -0.25604 -0.29882 -0.16760 121 ALA A CA  
824  C C   . ALA A 114 ? 1.01739 1.00295 0.74829 -0.23196 -0.30072 -0.15896 121 ALA A C   
825  O O   . ALA A 114 ? 1.09751 1.06116 0.74551 -0.24036 -0.32185 -0.18961 121 ALA A O   
826  C CB  . ALA A 114 ? 0.99278 0.87541 0.78531 -0.22784 -0.25072 -0.17770 121 ALA A CB  
827  N N   . LEU A 115 ? 0.94956 0.98730 0.71363 -0.20143 -0.27950 -0.11704 122 LEU A N   
828  C CA  . LEU A 115 ? 0.99176 1.06384 0.70351 -0.17778 -0.28073 -0.09987 122 LEU A CA  
829  C C   . LEU A 115 ? 1.03854 1.16451 0.73061 -0.20116 -0.33467 -0.09607 122 LEU A C   
830  O O   . LEU A 115 ? 1.11037 1.24154 0.72333 -0.19182 -0.34657 -0.09916 122 LEU A O   
831  C CB  . LEU A 115 ? 0.88123 0.99316 0.64423 -0.14462 -0.25412 -0.05468 122 LEU A CB  
832  C CG  . LEU A 115 ? 0.85602 0.92127 0.63114 -0.11990 -0.20593 -0.05470 122 LEU A CG  
833  C CD1 . LEU A 115 ? 0.80762 0.90536 0.61959 -0.09025 -0.18831 -0.01433 122 LEU A CD1 
834  C CD2 . LEU A 115 ? 0.93376 0.94555 0.63292 -0.10908 -0.18189 -0.08156 122 LEU A CD2 
835  N N   . GLN A 116 ? 1.01201 1.18332 0.77668 -0.23236 -0.36855 -0.08586 123 GLN A N   
836  C CA  . GLN A 116 ? 1.10138 1.32394 0.86665 -0.25184 -0.41621 -0.08452 123 GLN A CA  
837  C C   . GLN A 116 ? 1.16393 1.32338 0.85791 -0.27405 -0.43538 -0.13876 123 GLN A C   
838  O O   . GLN A 116 ? 1.22728 1.41053 0.88163 -0.27634 -0.46722 -0.14705 123 GLN A O   
839  C CB  . GLN A 116 ? 1.08658 1.37592 0.96841 -0.26925 -0.42984 -0.05595 123 GLN A CB  
840  C CG  . GLN A 116 ? 0.99976 1.36654 0.94893 -0.23868 -0.41486 -0.00220 123 GLN A CG  
841  C CD  . GLN A 116 ? 1.14787 1.59839 1.14536 -0.23463 -0.44332 0.02588  123 GLN A CD  
842  O OE1 . GLN A 116 ? 1.18596 1.64747 1.12968 -0.22416 -0.46659 0.02421  123 GLN A OE1 
843  N NE2 . GLN A 116 ? 1.15939 1.67008 1.25763 -0.24164 -0.44007 0.05362  123 GLN A NE2 
844  N N   . ALA A 117 ? 1.18703 1.26393 0.86392 -0.28700 -0.41637 -0.17652 124 ALA A N   
845  C CA  . ALA A 117 ? 1.27285 1.27870 0.88186 -0.30146 -0.42711 -0.23263 124 ALA A CA  
846  C C   . ALA A 117 ? 1.37858 1.32872 0.86610 -0.27240 -0.40180 -0.26177 124 ALA A C   
847  O O   . ALA A 117 ? 1.45903 1.33389 0.88727 -0.27405 -0.39293 -0.31227 124 ALA A O   
848  C CB  . ALA A 117 ? 1.24889 1.18909 0.90532 -0.32368 -0.41480 -0.25671 124 ALA A CB  
849  N N   . GLY A 118 ? 1.40192 1.38815 0.85365 -0.24361 -0.38560 -0.22902 125 GLY A N   
850  C CA  . GLY A 118 ? 1.42102 1.36610 0.75903 -0.21470 -0.35544 -0.24694 125 GLY A CA  
851  C C   . GLY A 118 ? 1.35996 1.24849 0.69487 -0.18835 -0.29439 -0.25328 125 GLY A C   
852  O O   . GLY A 118 ? 1.40941 1.26370 0.65970 -0.16136 -0.25911 -0.26942 125 GLY A O   
853  N N   . ALA A 119 ? 1.27977 1.16730 0.71777 -0.18859 -0.27499 -0.23654 126 ALA A N   
854  C CA  . ALA A 119 ? 1.26626 1.11221 0.72507 -0.15825 -0.21716 -0.23758 126 ALA A CA  
855  C C   . ALA A 119 ? 1.23726 1.12454 0.69851 -0.12315 -0.18195 -0.19474 126 ALA A C   
856  O O   . ALA A 119 ? 1.23572 1.18234 0.70125 -0.12050 -0.20089 -0.15820 126 ALA A O   
857  C CB  . ALA A 119 ? 1.18811 1.02450 0.75056 -0.16883 -0.21174 -0.22735 126 ALA A CB  
858  N N   . ASP A 120 ? 1.20528 1.05985 0.67000 -0.09625 -0.13109 -0.19748 127 ASP A N   
859  C CA  . ASP A 120 ? 1.14461 1.02803 0.61443 -0.06719 -0.09472 -0.15907 127 ASP A CA  
860  C C   . ASP A 120 ? 1.04801 0.94963 0.62154 -0.06028 -0.08094 -0.12601 127 ASP A C   
861  O O   . ASP A 120 ? 1.04657 0.92540 0.67680 -0.06857 -0.08132 -0.13811 127 ASP A O   
862  C CB  . ASP A 120 ? 1.15719 1.00368 0.56880 -0.04256 -0.04587 -0.17895 127 ASP A CB  
863  C CG  . ASP A 120 ? 1.25868 1.13920 0.63352 -0.02132 -0.01902 -0.14112 127 ASP A CG  
864  O OD1 . ASP A 120 ? 1.46508 1.37540 0.78421 -0.02641 -0.04613 -0.12478 127 ASP A OD1 
865  O OD2 . ASP A 120 ? 1.36769 1.24716 0.77349 -0.00070 0.02767  -0.12419 127 ASP A OD2 
866  N N   . ILE A 121 ? 0.99949 0.93747 0.59185 -0.04490 -0.07033 -0.08367 128 ILE A N   
867  C CA  . ILE A 121 ? 0.92044 0.86993 0.59780 -0.03721 -0.05965 -0.05529 128 ILE A CA  
868  C C   . ILE A 121 ? 0.89433 0.81073 0.60567 -0.02652 -0.02323 -0.06589 128 ILE A C   
869  O O   . ILE A 121 ? 0.85107 0.76361 0.62977 -0.02710 -0.02273 -0.05861 128 ILE A O   
870  C CB  . ILE A 121 ? 0.89249 0.87381 0.57359 -0.02254 -0.05668 -0.01144 128 ILE A CB  
871  C CG1 . ILE A 121 ? 0.90929 0.93144 0.58427 -0.02914 -0.09678 0.00474  128 ILE A CG1 
872  C CG2 . ILE A 121 ? 0.79326 0.77062 0.54713 -0.01261 -0.04058 0.01118  128 ILE A CG2 
873  C CD1 . ILE A 121 ? 0.90517 0.95153 0.59092 -0.01054 -0.09625 0.04944  128 ILE A CD1 
874  N N   . SER A 122 ? 0.92898 0.82442 0.59361 -0.01484 0.00761  -0.08264 129 SER A N   
875  C CA  . SER A 122 ? 0.91664 0.79108 0.62208 -0.00054 0.04446  -0.08894 129 SER A CA  
876  C C   . SER A 122 ? 0.91215 0.75246 0.65724 -0.00757 0.03495  -0.11655 129 SER A C   
877  O O   . SER A 122 ? 0.86473 0.69423 0.66425 0.00441  0.05693  -0.11422 129 SER A O   
878  C CB  . SER A 122 ? 0.93056 0.79430 0.57335 0.01723  0.08368  -0.10300 129 SER A CB  
879  O OG  . SER A 122 ? 1.01429 0.84254 0.58293 0.01290  0.07371  -0.14829 129 SER A OG  
880  N N   . MET A 123 ? 0.92977 0.75448 0.65373 -0.02795 0.00103  -0.13881 130 MET A N   
881  C CA  . MET A 123 ? 0.96249 0.75008 0.72459 -0.03851 -0.01029 -0.15928 130 MET A CA  
882  C C   . MET A 123 ? 0.85195 0.66309 0.68582 -0.04958 -0.03037 -0.13089 130 MET A C   
883  O O   . MET A 123 ? 0.84926 0.63790 0.71081 -0.06507 -0.04728 -0.13969 130 MET A O   
884  C CB  . MET A 123 ? 1.01544 0.76894 0.72240 -0.06027 -0.03771 -0.19713 130 MET A CB  
885  C CG  . MET A 123 ? 1.17204 0.87454 0.80702 -0.04584 -0.01448 -0.23976 130 MET A CG  
886  S SD  . MET A 123 ? 1.61894 1.29265 1.15612 -0.07350 -0.05506 -0.28294 130 MET A SD  
887  C CE  . MET A 123 ? 1.19639 0.88335 0.80521 -0.11566 -0.10711 -0.26960 130 MET A CE  
888  N N   . ILE A 124 ? 0.79784 0.64911 0.65834 -0.04134 -0.02745 -0.09691 131 ILE A N   
889  C CA  . ILE A 124 ? 0.75071 0.62295 0.66482 -0.04730 -0.04393 -0.07304 131 ILE A CA  
890  C C   . ILE A 124 ? 0.74690 0.59351 0.71095 -0.04289 -0.03561 -0.07304 131 ILE A C   
891  O O   . ILE A 124 ? 0.62465 0.47447 0.62037 -0.05259 -0.05110 -0.06279 131 ILE A O   
892  C CB  . ILE A 124 ? 0.69080 0.59704 0.61351 -0.03534 -0.04094 -0.04242 131 ILE A CB  
893  C CG1 . ILE A 124 ? 0.63951 0.56365 0.60420 -0.03676 -0.05582 -0.02290 131 ILE A CG1 
894  C CG2 . ILE A 124 ? 0.67765 0.57554 0.61278 -0.01899 -0.01253 -0.03395 131 ILE A CG2 
895  C CD1 . ILE A 124 ? 0.58044 0.52964 0.54516 -0.02452 -0.05827 0.00197  131 ILE A CD1 
896  N N   . GLY A 125 ? 0.73656 0.56193 0.70970 -0.02678 -0.01037 -0.08120 132 GLY A N   
897  C CA  . GLY A 125 ? 0.73592 0.54176 0.76081 -0.01945 -0.00565 -0.07703 132 GLY A CA  
898  C C   . GLY A 125 ? 0.76980 0.53443 0.79776 -0.03000 -0.01643 -0.09508 132 GLY A C   
899  O O   . GLY A 125 ? 0.78430 0.53744 0.85340 -0.03039 -0.02408 -0.08208 132 GLY A O   
900  N N   . GLN A 126 ? 0.82901 0.56658 0.81036 -0.04001 -0.01957 -0.12435 133 GLN A N   
901  C CA  . GLN A 126 ? 0.87091 0.55819 0.85459 -0.05520 -0.03324 -0.14336 133 GLN A CA  
902  C C   . GLN A 126 ? 0.83642 0.54161 0.84822 -0.08154 -0.06131 -0.12116 133 GLN A C   
903  O O   . GLN A 126 ? 0.85528 0.52176 0.88916 -0.09500 -0.07137 -0.12260 133 GLN A O   
904  C CB  . GLN A 126 ? 0.94836 0.59981 0.86695 -0.06460 -0.03678 -0.18373 133 GLN A CB  
905  C CG  . GLN A 126 ? 1.28047 0.85344 1.19356 -0.06088 -0.03089 -0.21656 133 GLN A CG  
906  C CD  . GLN A 126 ? 1.29143 0.82097 1.12604 -0.07070 -0.03764 -0.26339 133 GLN A CD  
907  O OE1 . GLN A 126 ? 1.52922 1.00182 1.35169 -0.09470 -0.06078 -0.28837 133 GLN A OE1 
908  N NE2 . GLN A 126 ? 1.31717 0.87055 1.09423 -0.05394 -0.01899 -0.27489 133 GLN A NE2 
909  N N   . PHE A 127 ? 0.77034 0.53251 0.78371 -0.08722 -0.07131 -0.09828 134 PHE A N   
910  C CA  . PHE A 127 ? 0.71699 0.50901 0.75886 -0.10673 -0.09062 -0.07380 134 PHE A CA  
911  C C   . PHE A 127 ? 0.70357 0.51812 0.77918 -0.09134 -0.08362 -0.04314 134 PHE A C   
912  O O   . PHE A 127 ? 0.69607 0.54329 0.78872 -0.10024 -0.09261 -0.02024 134 PHE A O   
913  C CB  . PHE A 127 ? 0.73491 0.57748 0.75723 -0.11981 -0.10705 -0.06940 134 PHE A CB  
914  C CG  . PHE A 127 ? 0.77712 0.60112 0.75832 -0.13908 -0.12285 -0.09989 134 PHE A CG  
915  C CD1 . PHE A 127 ? 0.79821 0.60838 0.72546 -0.12442 -0.11201 -0.12283 134 PHE A CD1 
916  C CD2 . PHE A 127 ? 0.79486 0.61508 0.78894 -0.17376 -0.14950 -0.10495 134 PHE A CD2 
917  C CE1 . PHE A 127 ? 0.88419 0.67323 0.75855 -0.14114 -0.12899 -0.15455 134 PHE A CE1 
918  C CE2 . PHE A 127 ? 0.86316 0.66131 0.81374 -0.19502 -0.17112 -0.13733 134 PHE A CE2 
919  C CZ  . PHE A 127 ? 0.90401 0.68447 0.78832 -0.17727 -0.16164 -0.16438 134 PHE A CZ  
920  N N   . GLY A 128 ? 0.68889 0.48947 0.77385 -0.06839 -0.06818 -0.04233 135 GLY A N   
921  C CA  . GLY A 128 ? 0.62207 0.43651 0.73286 -0.05617 -0.06820 -0.01771 135 GLY A CA  
922  C C   . GLY A 128 ? 0.62265 0.47920 0.72383 -0.05041 -0.07152 -0.00247 135 GLY A C   
923  O O   . GLY A 128 ? 0.65380 0.52124 0.76367 -0.04565 -0.07652 0.01580  135 GLY A O   
924  N N   . VAL A 129 ? 0.57895 0.45529 0.65720 -0.04830 -0.06866 -0.00935 136 VAL A N   
925  C CA  . VAL A 129 ? 0.56581 0.47332 0.63594 -0.03857 -0.07097 0.00495  136 VAL A CA  
926  C C   . VAL A 129 ? 0.54693 0.45209 0.60530 -0.02679 -0.06078 0.00213  136 VAL A C   
927  O O   . VAL A 129 ? 0.49984 0.42419 0.54228 -0.02071 -0.06214 0.01027  136 VAL A O   
928  C CB  . VAL A 129 ? 0.56220 0.50598 0.62380 -0.04810 -0.08085 0.01104  136 VAL A CB  
929  C CG1 . VAL A 129 ? 0.58156 0.53727 0.66458 -0.05996 -0.08671 0.02351  136 VAL A CG1 
930  C CG2 . VAL A 129 ? 0.58311 0.52650 0.62351 -0.06207 -0.08625 -0.00591 136 VAL A CG2 
931  N N   . GLY A 130 ? 0.50452 0.48216 0.53671 -0.04105 -0.04459 -0.08515 137 GLY A N   
932  C CA  . GLY A 130 ? 0.52607 0.51007 0.54008 -0.03056 -0.04322 -0.08172 137 GLY A CA  
933  C C   . GLY A 130 ? 0.46887 0.46546 0.48888 -0.02415 -0.04308 -0.06551 137 GLY A C   
934  O O   . GLY A 130 ? 0.50622 0.51196 0.51504 -0.01758 -0.04367 -0.05988 137 GLY A O   
935  N N   . PHE A 131 ? 0.44221 0.43774 0.47817 -0.02566 -0.04191 -0.05792 138 PHE A N   
936  C CA  . PHE A 131 ? 0.47803 0.47975 0.51794 -0.02010 -0.04282 -0.04618 138 PHE A CA  
937  C C   . PHE A 131 ? 0.45908 0.47663 0.49660 -0.01762 -0.05008 -0.04345 138 PHE A C   
938  O O   . PHE A 131 ? 0.44646 0.46579 0.48069 -0.01167 -0.05041 -0.03449 138 PHE A O   
939  C CB  . PHE A 131 ? 0.48586 0.48389 0.53737 -0.02124 -0.04119 -0.04204 138 PHE A CB  
940  C CG  . PHE A 131 ? 0.47816 0.48035 0.53164 -0.01618 -0.04425 -0.03525 138 PHE A CG  
941  C CD1 . PHE A 131 ? 0.46802 0.46250 0.52033 -0.01296 -0.04408 -0.02937 138 PHE A CD1 
942  C CD2 . PHE A 131 ? 0.49010 0.50353 0.54861 -0.01456 -0.04750 -0.03518 138 PHE A CD2 
943  C CE1 . PHE A 131 ? 0.45015 0.44210 0.50347 -0.00932 -0.04776 -0.02600 138 PHE A CE1 
944  C CE2 . PHE A 131 ? 0.45271 0.46459 0.51152 -0.00771 -0.04909 -0.03072 138 PHE A CE2 
945  C CZ  . PHE A 131 ? 0.46278 0.46090 0.51758 -0.00563 -0.04956 -0.02736 138 PHE A CZ  
946  N N   . TYR A 132 ? 0.46222 0.49233 0.50451 -0.02228 -0.05619 -0.04934 139 TYR A N   
947  C CA  . TYR A 132 ? 0.49443 0.54368 0.53846 -0.01802 -0.06379 -0.04449 139 TYR A CA  
948  C C   . TYR A 132 ? 0.45364 0.51031 0.47955 -0.01327 -0.06784 -0.04275 139 TYR A C   
949  O O   . TYR A 132 ? 0.49266 0.56445 0.51842 -0.00696 -0.07371 -0.03457 139 TYR A O   
950  C CB  . TYR A 132 ? 0.45861 0.52555 0.51764 -0.02505 -0.06998 -0.04993 139 TYR A CB  
951  C CG  . TYR A 132 ? 0.47060 0.53336 0.54675 -0.02831 -0.06327 -0.04822 139 TYR A CG  
952  C CD1 . TYR A 132 ? 0.44861 0.51627 0.53297 -0.01987 -0.05995 -0.03978 139 TYR A CD1 
953  C CD2 . TYR A 132 ? 0.48915 0.54103 0.57108 -0.03836 -0.05907 -0.05447 139 TYR A CD2 
954  C CE1 . TYR A 132 ? 0.45601 0.52173 0.55070 -0.02077 -0.05235 -0.03772 139 TYR A CE1 
955  C CE2 . TYR A 132 ? 0.53223 0.58201 0.62774 -0.04018 -0.05150 -0.04945 139 TYR A CE2 
956  C CZ  . TYR A 132 ? 0.53970 0.59828 0.63988 -0.03105 -0.04800 -0.04111 139 TYR A CZ  
957  O OH  . TYR A 132 ? 0.59490 0.65336 0.70358 -0.03094 -0.03913 -0.03574 139 TYR A OH  
958  N N   . SER A 133 ? 0.47333 0.52027 0.48309 -0.01403 -0.06358 -0.04876 140 SER A N   
959  C CA  . SER A 133 ? 0.47176 0.52567 0.46040 -0.00685 -0.06364 -0.04423 140 SER A CA  
960  C C   . SER A 133 ? 0.48182 0.53281 0.47379 0.00101  -0.05774 -0.02589 140 SER A C   
961  O O   . SER A 133 ? 0.46866 0.52796 0.44616 0.00788  -0.05665 -0.01632 140 SER A O   
962  C CB  . SER A 133 ? 0.48703 0.52997 0.45699 -0.00711 -0.05713 -0.05563 140 SER A CB  
963  O OG  . SER A 133 ? 0.50108 0.52828 0.47896 -0.00502 -0.04519 -0.05044 140 SER A OG  
964  N N   . ALA A 134 ? 0.44135 0.48030 0.45127 -0.00037 -0.05424 -0.02069 141 ALA A N   
965  C CA  . ALA A 134 ? 0.43825 0.47109 0.45501 0.00411  -0.05112 -0.00527 141 ALA A CA  
966  C C   . ALA A 134 ? 0.46054 0.50237 0.47748 0.01089  -0.05697 0.00534  141 ALA A C   
967  O O   . ALA A 134 ? 0.43722 0.47505 0.45503 0.01549  -0.05414 0.02058  141 ALA A O   
968  C CB  . ALA A 134 ? 0.45770 0.47551 0.49056 0.00047  -0.04979 -0.00617 141 ALA A CB  
969  N N   . TYR A 135 ? 0.42529 0.48028 0.44458 0.01179  -0.06474 -0.00045 142 TYR A N   
970  C CA  . TYR A 135 ? 0.49527 0.56230 0.51714 0.02082  -0.07068 0.01093  142 TYR A CA  
971  C C   . TYR A 135 ? 0.51186 0.59724 0.51419 0.02607  -0.07476 0.01815  142 TYR A C   
972  O O   . TYR A 135 ? 0.51334 0.61213 0.51643 0.03526  -0.08059 0.03040  142 TYR A O   
973  C CB  . TYR A 135 ? 0.42678 0.50730 0.46312 0.02096  -0.07694 0.00408  142 TYR A CB  
974  C CG  . TYR A 135 ? 0.48192 0.54543 0.53323 0.02101  -0.07156 0.00124  142 TYR A CG  
975  C CD1 . TYR A 135 ? 0.44701 0.49954 0.50644 0.03116  -0.07001 0.01032  142 TYR A CD1 
976  C CD2 . TYR A 135 ? 0.41507 0.47124 0.46969 0.01209  -0.06769 -0.01049 142 TYR A CD2 
977  C CE1 . TYR A 135 ? 0.47324 0.50870 0.54012 0.03242  -0.06544 0.00472  142 TYR A CE1 
978  C CE2 . TYR A 135 ? 0.42391 0.46655 0.48641 0.01356  -0.06302 -0.01283 142 TYR A CE2 
979  C CZ  . TYR A 135 ? 0.47292 0.50551 0.53967 0.02372  -0.06223 -0.00671 142 TYR A CZ  
980  O OH  . TYR A 135 ? 0.44755 0.46536 0.51627 0.02636  -0.05799 -0.01201 142 TYR A OH  
981  N N   . LEU A 136 ? 0.48763 0.57427 0.47073 0.02244  -0.07140 0.01126  143 LEU A N   
982  C CA  . LEU A 136 ? 0.53093 0.63247 0.48909 0.02984  -0.07227 0.02019  143 LEU A CA  
983  C C   . LEU A 136 ? 0.56311 0.65708 0.52360 0.03767  -0.06357 0.04465  143 LEU A C   
984  O O   . LEU A 136 ? 0.50883 0.61700 0.45521 0.04722  -0.06552 0.06069  143 LEU A O   
985  C CB  . LEU A 136 ? 0.52708 0.62762 0.46186 0.02638  -0.06747 0.00565  143 LEU A CB  
986  C CG  . LEU A 136 ? 0.53574 0.64111 0.46300 0.01783  -0.07685 -0.01931 143 LEU A CG  
987  C CD1 . LEU A 136 ? 0.52560 0.61675 0.43510 0.01575  -0.06729 -0.03381 143 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.54085 0.67295 0.45041 0.02074  -0.09238 -0.02188 143 LEU A CD2 
989  N N   . VAL A 137 ? 0.50536 0.57766 0.48451 0.03313  -0.05479 0.04892  144 VAL A N   
990  C CA  . VAL A 137 ? 0.51849 0.58076 0.50572 0.03648  -0.04654 0.07155  144 VAL A CA  
991  C C   . VAL A 137 ? 0.52444 0.56478 0.53773 0.03486  -0.04845 0.07702  144 VAL A C   
992  O O   . VAL A 137 ? 0.51004 0.53888 0.53303 0.03748  -0.04422 0.09686  144 VAL A O   
993  C CB  . VAL A 137 ? 0.51320 0.57152 0.49988 0.03178  -0.03394 0.07400  144 VAL A CB  
994  C CG1 . VAL A 137 ? 0.53788 0.61491 0.49379 0.03718  -0.02945 0.06911  144 VAL A CG1 
995  C CG2 . VAL A 137 ? 0.48560 0.52980 0.48906 0.02191  -0.03363 0.05754  144 VAL A CG2 
996  N N   . ALA A 138 ? 0.49571 0.52824 0.51977 0.03094  -0.05393 0.06030  145 ALA A N   
997  C CA  . ALA A 138 ? 0.50001 0.50898 0.54320 0.03027  -0.05506 0.06056  145 ALA A CA  
998  C C   . ALA A 138 ? 0.50802 0.52159 0.55515 0.04024  -0.06143 0.05941  145 ALA A C   
999  O O   . ALA A 138 ? 0.49430 0.52791 0.53746 0.04101  -0.06628 0.04830  145 ALA A O   
1000 C CB  . ALA A 138 ? 0.47890 0.47607 0.52936 0.02038  -0.05443 0.04375  145 ALA A CB  
1001 N N   . GLU A 139 ? 0.53839 0.53324 0.59618 0.04791  -0.06097 0.07155  146 GLU A N   
1002 C CA  . GLU A 139 ? 0.53753 0.53303 0.60311 0.06006  -0.06466 0.07025  146 GLU A CA  
1003 C C   . GLU A 139 ? 0.53314 0.51181 0.60614 0.05769  -0.06375 0.05187  146 GLU A C   
1004 O O   . GLU A 139 ? 0.52155 0.50914 0.60006 0.06732  -0.06478 0.04662  146 GLU A O   
1005 C CB  . GLU A 139 ? 0.64950 0.62746 0.72271 0.07217  -0.06317 0.09110  146 GLU A CB  
1006 C CG  . GLU A 139 ? 0.71322 0.65125 0.79633 0.06524  -0.05872 0.09491  146 GLU A CG  
1007 C CD  . GLU A 139 ? 0.96807 0.88361 1.06098 0.07664  -0.05651 0.11693  146 GLU A CD  
1008 O OE1 . GLU A 139 ? 1.16057 1.04077 1.26444 0.08054  -0.05596 0.11169  146 GLU A OE1 
1009 O OE2 . GLU A 139 ? 0.97411 0.90561 1.06200 0.08255  -0.05504 0.13955  146 GLU A OE2 
1010 N N   . LYS A 140 ? 0.53033 0.48829 0.60349 0.04607  -0.06172 0.04318  147 LYS A N   
1011 C CA  . LYS A 140 ? 0.51324 0.45693 0.58725 0.04363  -0.06154 0.02556  147 LYS A CA  
1012 C C   . LYS A 140 ? 0.48832 0.43054 0.55885 0.02876  -0.06151 0.01752  147 LYS A C   
1013 O O   . LYS A 140 ? 0.47025 0.40740 0.54398 0.02092  -0.06090 0.02622  147 LYS A O   
1014 C CB  . LYS A 140 ? 0.53993 0.44789 0.61920 0.04999  -0.06149 0.02414  147 LYS A CB  
1015 C CG  . LYS A 140 ? 0.56191 0.45527 0.63515 0.05003  -0.06146 0.00432  147 LYS A CG  
1016 C CD  . LYS A 140 ? 0.59335 0.44920 0.66753 0.05965  -0.06144 -0.00050 147 LYS A CD  
1017 C CE  . LYS A 140 ? 0.61597 0.43885 0.69330 0.04583  -0.06704 -0.00278 147 LYS A CE  
1018 N NZ  . LYS A 140 ? 0.66875 0.44807 0.74699 0.05387  -0.06818 -0.00921 147 LYS A NZ  
1019 N N   . VAL A 141 ? 0.44299 0.39196 0.50900 0.02597  -0.06116 0.00341  148 VAL A N   
1020 C CA  . VAL A 141 ? 0.44210 0.39114 0.50550 0.01455  -0.06122 -0.00320 148 VAL A CA  
1021 C C   . VAL A 141 ? 0.48247 0.41545 0.54155 0.01454  -0.06302 -0.01575 148 VAL A C   
1022 O O   . VAL A 141 ? 0.50006 0.43693 0.55424 0.02241  -0.06050 -0.02293 148 VAL A O   
1023 C CB  . VAL A 141 ? 0.43127 0.40412 0.49058 0.01104  -0.05874 -0.00648 148 VAL A CB  
1024 C CG1 . VAL A 141 ? 0.42550 0.39601 0.48364 0.00233  -0.05771 -0.01157 148 VAL A CG1 
1025 C CG2 . VAL A 141 ? 0.45166 0.43969 0.50856 0.01173  -0.05823 0.00276  148 VAL A CG2 
1026 N N   . THR A 142 ? 0.44597 0.36385 0.50689 0.00602  -0.06750 -0.01781 149 THR A N   
1027 C CA  . THR A 142 ? 0.48535 0.38987 0.53749 0.00475  -0.07189 -0.03080 149 THR A CA  
1028 C C   . THR A 142 ? 0.54909 0.46710 0.60077 -0.00386 -0.07325 -0.03148 149 THR A C   
1029 O O   . THR A 142 ? 0.46810 0.39255 0.53130 -0.01194 -0.07428 -0.02301 149 THR A O   
1030 C CB  . THR A 142 ? 0.51758 0.39252 0.57302 0.00108  -0.07971 -0.03449 149 THR A CB  
1031 O OG1 . THR A 142 ? 0.54168 0.40096 0.60023 0.01063  -0.07703 -0.03069 149 THR A OG1 
1032 C CG2 . THR A 142 ? 0.51748 0.37812 0.55670 0.00181  -0.08590 -0.05169 149 THR A CG2 
1033 N N   . VAL A 143 ? 0.40677 0.33030 0.44610 -0.00053 -0.07180 -0.03941 150 VAL A N   
1034 C CA  . VAL A 143 ? 0.47001 0.40568 0.50833 -0.00582 -0.07225 -0.03807 150 VAL A CA  
1035 C C   . VAL A 143 ? 0.50770 0.43400 0.53201 -0.00563 -0.08003 -0.04738 150 VAL A C   
1036 O O   . VAL A 143 ? 0.48119 0.40374 0.48837 0.00284  -0.07716 -0.05532 150 VAL A O   
1037 C CB  . VAL A 143 ? 0.47752 0.42977 0.51391 -0.00263 -0.06291 -0.03570 150 VAL A CB  
1038 C CG1 . VAL A 143 ? 0.42737 0.38707 0.46306 -0.00613 -0.06256 -0.03270 150 VAL A CG1 
1039 C CG2 . VAL A 143 ? 0.43243 0.39403 0.47879 -0.00373 -0.05839 -0.02969 150 VAL A CG2 
1040 N N   . ILE A 144 ? 0.47283 0.39816 0.50420 -0.01443 -0.08998 -0.04607 151 ILE A N   
1041 C CA  . ILE A 144 ? 0.46935 0.39126 0.48669 -0.01580 -0.10084 -0.05445 151 ILE A CA  
1042 C C   . ILE A 144 ? 0.50637 0.44932 0.52571 -0.01618 -0.09924 -0.04553 151 ILE A C   
1043 O O   . ILE A 144 ? 0.49514 0.45032 0.53504 -0.02136 -0.09777 -0.03460 151 ILE A O   
1044 C CB  . ILE A 144 ? 0.55063 0.45937 0.57846 -0.02695 -0.11623 -0.05895 151 ILE A CB  
1045 C CG1 . ILE A 144 ? 0.51521 0.40209 0.55176 -0.02784 -0.11453 -0.06051 151 ILE A CG1 
1046 C CG2 . ILE A 144 ? 0.58717 0.48652 0.59205 -0.02689 -0.13005 -0.07417 151 ILE A CG2 
1047 C CD1 . ILE A 144 ? 0.63623 0.50009 0.64980 -0.01665 -0.11266 -0.07536 151 ILE A CD1 
1048 N N   . THR A 145 ? 0.46732 0.41435 0.46513 -0.00895 -0.09789 -0.04869 152 THR A N   
1049 C CA  . THR A 145 ? 0.48855 0.45272 0.48773 -0.00686 -0.09408 -0.03752 152 THR A CA  
1050 C C   . THR A 145 ? 0.48521 0.45310 0.45991 -0.00227 -0.10284 -0.04105 152 THR A C   
1051 O O   . THR A 145 ? 0.50700 0.46400 0.45683 0.00264  -0.10610 -0.05382 152 THR A O   
1052 C CB  . THR A 145 ? 0.44651 0.41538 0.44730 -0.00152 -0.07706 -0.03093 152 THR A CB  
1053 O OG1 . THR A 145 ? 0.48225 0.46200 0.48924 -0.00035 -0.07278 -0.01884 152 THR A OG1 
1054 C CG2 . THR A 145 ? 0.48809 0.45378 0.46744 0.00696  -0.07008 -0.03685 152 THR A CG2 
1055 N N   . LYS A 146 ? 0.47225 0.45600 0.45251 -0.00207 -0.10632 -0.02933 153 LYS A N   
1056 C CA  . LYS A 146 ? 0.46159 0.45412 0.41808 0.00319  -0.11620 -0.02891 153 LYS A CA  
1057 C C   . LYS A 146 ? 0.46772 0.47534 0.42981 0.00965  -0.10733 -0.00959 153 LYS A C   
1058 O O   . LYS A 146 ? 0.44443 0.46196 0.43269 0.00685  -0.10820 0.00166  153 LYS A O   
1059 C CB  . LYS A 146 ? 0.48699 0.48449 0.44792 -0.00557 -0.13940 -0.03537 153 LYS A CB  
1060 C CG  . LYS A 146 ? 0.49711 0.50930 0.43364 -0.00037 -0.15339 -0.03374 153 LYS A CG  
1061 C CD  . LYS A 146 ? 0.51583 0.51688 0.40715 0.00982  -0.15100 -0.04660 153 LYS A CD  
1062 C CE  . LYS A 146 ? 0.56573 0.58183 0.42650 0.01486  -0.16841 -0.04735 153 LYS A CE  
1063 N NZ  . LYS A 146 ? 0.52948 0.56614 0.38632 0.02608  -0.15828 -0.02321 153 LYS A NZ  
1064 N N   . HIS A 147 ? 0.46629 0.47495 0.40511 0.01930  -0.09719 -0.00453 154 HIS A N   
1065 C CA  . HIS A 147 ? 0.48110 0.50009 0.42244 0.02636  -0.08833 0.01570  154 HIS A CA  
1066 C C   . HIS A 147 ? 0.54627 0.57970 0.46151 0.03380  -0.10151 0.02130  154 HIS A C   
1067 O O   . HIS A 147 ? 0.55575 0.58820 0.44132 0.03528  -0.11287 0.00687  154 HIS A O   
1068 C CB  . HIS A 147 ? 0.53094 0.54352 0.46797 0.03084  -0.06707 0.02203  154 HIS A CB  
1069 C CG  . HIS A 147 ? 0.51809 0.53392 0.46577 0.03550  -0.05539 0.04377  154 HIS A CG  
1070 N ND1 . HIS A 147 ? 0.55078 0.57625 0.47794 0.04554  -0.05386 0.05951  154 HIS A ND1 
1071 C CD2 . HIS A 147 ? 0.52066 0.52849 0.49604 0.03216  -0.04437 0.05232  154 HIS A CD2 
1072 C CE1 . HIS A 147 ? 0.59105 0.61288 0.53628 0.04793  -0.04179 0.07879  154 HIS A CE1 
1073 N NE2 . HIS A 147 ? 0.58062 0.59004 0.55492 0.03965  -0.03611 0.07304  154 HIS A NE2 
1074 N N   . ASN A 148 ? 0.50514 0.55121 0.43018 0.03963  -0.10042 0.04205  155 ASN A N   
1075 C CA  . ASN A 148 ? 0.57315 0.63772 0.47434 0.04804  -0.11455 0.05110  155 ASN A CA  
1076 C C   . ASN A 148 ? 0.60822 0.67218 0.46561 0.05813  -0.10769 0.05080  155 ASN A C   
1077 O O   . ASN A 148 ? 0.62051 0.69686 0.44433 0.06395  -0.12338 0.04721  155 ASN A O   
1078 C CB  . ASN A 148 ? 0.53364 0.61058 0.45594 0.05564  -0.11074 0.07759  155 ASN A CB  
1079 C CG  . ASN A 148 ? 0.60585 0.69703 0.56198 0.05038  -0.12546 0.07946  155 ASN A CG  
1080 O OD1 . ASN A 148 ? 0.54066 0.63839 0.49986 0.04042  -0.14390 0.06341  155 ASN A OD1 
1081 N ND2 . ASN A 148 ? 0.48848 0.58405 0.47238 0.05735  -0.11635 0.09983  155 ASN A ND2 
1082 N N   . ASP A 149 ? 0.60792 0.65997 0.46481 0.06038  -0.08470 0.05444  156 ASP A N   
1083 C CA  . ASP A 149 ? 0.70284 0.75825 0.52350 0.07153  -0.07240 0.05978  156 ASP A CA  
1084 C C   . ASP A 149 ? 0.65404 0.69968 0.45286 0.07149  -0.06958 0.03579  156 ASP A C   
1085 O O   . ASP A 149 ? 0.67317 0.72250 0.44450 0.08186  -0.05512 0.03934  156 ASP A O   
1086 C CB  . ASP A 149 ? 0.67711 0.72935 0.51577 0.07418  -0.04719 0.08350  156 ASP A CB  
1087 C CG  . ASP A 149 ? 0.71043 0.76768 0.56718 0.07806  -0.04718 0.10919  156 ASP A CG  
1088 O OD1 . ASP A 149 ? 0.92127 0.99303 0.76677 0.08351  -0.06552 0.11368  156 ASP A OD1 
1089 O OD2 . ASP A 149 ? 0.68871 0.73501 0.57235 0.07577  -0.02945 0.12469  156 ASP A OD2 
1090 N N   . ASP A 150 ? 0.61997 0.65345 0.43135 0.06152  -0.08137 0.01335  157 ASP A N   
1091 C CA  . ASP A 150 ? 0.67503 0.69522 0.47044 0.06297  -0.07753 -0.00853 157 ASP A CA  
1092 C C   . ASP A 150 ? 0.66207 0.67036 0.45416 0.05480  -0.10095 -0.03251 157 ASP A C   
1093 O O   . ASP A 150 ? 0.64210 0.65675 0.44745 0.04663  -0.11973 -0.03097 157 ASP A O   
1094 C CB  . ASP A 150 ? 0.62319 0.63581 0.45030 0.05818  -0.05858 -0.00641 157 ASP A CB  
1095 C CG  . ASP A 150 ? 0.67625 0.68580 0.48410 0.06766  -0.04408 -0.01597 157 ASP A CG  
1096 O OD1 . ASP A 150 ? 0.66243 0.66728 0.43247 0.07682  -0.05072 -0.03187 157 ASP A OD1 
1097 O OD2 . ASP A 150 ? 0.63104 0.64357 0.46208 0.06635  -0.02640 -0.00832 157 ASP A OD2 
1098 N N   . GLU A 151 ? 0.67442 0.66544 0.45158 0.05719  -0.09925 -0.05372 158 GLU A N   
1099 C CA  . GLU A 151 ? 0.70395 0.67646 0.48014 0.04848  -0.11939 -0.07726 158 GLU A CA  
1100 C C   . GLU A 151 ? 0.64881 0.61137 0.47054 0.03552  -0.11768 -0.07636 158 GLU A C   
1101 O O   . GLU A 151 ? 0.62928 0.59892 0.47829 0.03423  -0.10192 -0.06097 158 GLU A O   
1102 C CB  . GLU A 151 ? 0.77352 0.72693 0.51045 0.05959  -0.11734 -0.10087 158 GLU A CB  
1103 C CG  . GLU A 151 ? 0.94655 0.91009 0.63073 0.07535  -0.11643 -0.10317 158 GLU A CG  
1104 C CD  . GLU A 151 ? 1.31403 1.26179 0.96250 0.09187  -0.10263 -0.12151 158 GLU A CD  
1105 O OE1 . GLU A 151 ? 1.21486 1.13440 0.86086 0.08955  -0.11072 -0.14594 158 GLU A OE1 
1106 O OE2 . GLU A 151 ? 1.35437 1.31769 0.97885 0.10801  -0.08228 -0.11017 158 GLU A OE2 
1107 N N   . GLN A 152 ? 0.62835 0.57356 0.45735 0.02542  -0.13447 -0.09310 159 GLN A N   
1108 C CA  . GLN A 152 ? 0.59207 0.52723 0.45996 0.01444  -0.13251 -0.09147 159 GLN A CA  
1109 C C   . GLN A 152 ? 0.62759 0.54466 0.49184 0.02245  -0.11740 -0.10001 159 GLN A C   
1110 O O   . GLN A 152 ? 0.61798 0.51661 0.45340 0.03090  -0.11903 -0.11821 159 GLN A O   
1111 C CB  . GLN A 152 ? 0.62660 0.55125 0.50830 -0.00064 -0.15546 -0.10215 159 GLN A CB  
1112 C CG  . GLN A 152 ? 0.63270 0.55235 0.55655 -0.01240 -0.15293 -0.09464 159 GLN A CG  
1113 C CD  . GLN A 152 ? 0.71604 0.63802 0.66388 -0.02947 -0.17397 -0.09565 159 GLN A CD  
1114 O OE1 . GLN A 152 ? 0.70725 0.65321 0.66277 -0.03378 -0.18479 -0.08675 159 GLN A OE1 
1115 N NE2 . GLN A 152 ? 0.74955 0.64795 0.71254 -0.03920 -0.17967 -0.10453 159 GLN A NE2 
1116 N N   . TYR A 153 ? 0.54967 0.47260 0.44234 0.02101  -0.10311 -0.08741 160 TYR A N   
1117 C CA  . TYR A 153 ? 0.59611 0.51004 0.49060 0.02957  -0.08867 -0.09107 160 TYR A CA  
1118 C C   . TYR A 153 ? 0.58502 0.49042 0.51119 0.02082  -0.08979 -0.08777 160 TYR A C   
1119 O O   . TYR A 153 ? 0.54587 0.45819 0.49493 0.00907  -0.09583 -0.07850 160 TYR A O   
1120 C CB  . TYR A 153 ? 0.57973 0.51442 0.47604 0.03780  -0.06919 -0.07752 160 TYR A CB  
1121 C CG  . TYR A 153 ? 0.65406 0.59710 0.51690 0.05010  -0.06268 -0.07840 160 TYR A CG  
1122 C CD1 . TYR A 153 ? 0.61536 0.57562 0.47245 0.04912  -0.06186 -0.06447 160 TYR A CD1 
1123 C CD2 . TYR A 153 ? 0.68103 0.61467 0.51684 0.06476  -0.05585 -0.09179 160 TYR A CD2 
1124 C CE1 . TYR A 153 ? 0.67311 0.64279 0.49731 0.06146  -0.05476 -0.06202 160 TYR A CE1 
1125 C CE2 . TYR A 153 ? 0.70172 0.64525 0.50308 0.07792  -0.04775 -0.09156 160 TYR A CE2 
1126 C CZ  . TYR A 153 ? 0.73494 0.69740 0.53004 0.07573  -0.04739 -0.07570 160 TYR A CZ  
1127 O OH  . TYR A 153 ? 0.90686 0.88093 0.66551 0.08984  -0.03822 -0.07226 160 TYR A OH  
1128 N N   . ALA A 154 ? 0.57335 0.46533 0.50006 0.02875  -0.08261 -0.09385 161 ALA A N   
1129 C CA  . ALA A 154 ? 0.54573 0.43006 0.49858 0.02390  -0.08209 -0.08862 161 ALA A CA  
1130 C C   . ALA A 154 ? 0.56487 0.46394 0.52734 0.03334  -0.06650 -0.08051 161 ALA A C   
1131 O O   . ALA A 154 ? 0.58183 0.47775 0.53220 0.04736  -0.05802 -0.08677 161 ALA A O   
1132 C CB  . ALA A 154 ? 0.59658 0.44789 0.54522 0.02427  -0.09112 -0.10214 161 ALA A CB  
1133 N N   . TRP A 155 ? 0.47486 0.39148 0.45911 0.02610  -0.06307 -0.06724 162 TRP A N   
1134 C CA  . TRP A 155 ? 0.49818 0.43169 0.49589 0.03126  -0.05256 -0.05961 162 TRP A CA  
1135 C C   . TRP A 155 ? 0.51463 0.44087 0.52793 0.03012  -0.05580 -0.05518 162 TRP A C   
1136 O O   . TRP A 155 ? 0.51604 0.43493 0.53721 0.02038  -0.06291 -0.05130 162 TRP A O   
1137 C CB  . TRP A 155 ? 0.46884 0.42458 0.47669 0.02369  -0.04774 -0.05001 162 TRP A CB  
1138 C CG  . TRP A 155 ? 0.48720 0.46254 0.51118 0.02486  -0.04034 -0.04359 162 TRP A CG  
1139 C CD1 . TRP A 155 ? 0.45526 0.44895 0.48330 0.02878  -0.03062 -0.04050 162 TRP A CD1 
1140 C CD2 . TRP A 155 ? 0.48949 0.47118 0.52849 0.02091  -0.04316 -0.03872 162 TRP A CD2 
1141 N NE1 . TRP A 155 ? 0.46593 0.47735 0.51344 0.02593  -0.02935 -0.03545 162 TRP A NE1 
1142 C CE2 . TRP A 155 ? 0.45014 0.45433 0.50153 0.02194  -0.03752 -0.03502 162 TRP A CE2 
1143 C CE3 . TRP A 155 ? 0.46245 0.43511 0.50546 0.01667  -0.04974 -0.03595 162 TRP A CE3 
1144 C CZ2 . TRP A 155 ? 0.44716 0.46479 0.51135 0.01903  -0.04090 -0.03103 162 TRP A CZ2 
1145 C CZ3 . TRP A 155 ? 0.41938 0.40483 0.47232 0.01571  -0.05041 -0.03023 162 TRP A CZ3 
1146 C CH2 . TRP A 155 ? 0.44540 0.45299 0.50713 0.01696  -0.04729 -0.02899 162 TRP A CH2 
1147 N N   . GLU A 156 ? 0.49004 0.42094 0.50907 0.04116  -0.04984 -0.05345 163 GLU A N   
1148 C CA  . GLU A 156 ? 0.51641 0.44063 0.54818 0.04307  -0.05267 -0.04661 163 GLU A CA  
1149 C C   . GLU A 156 ? 0.52825 0.47638 0.57225 0.05266  -0.04631 -0.03932 163 GLU A C   
1150 O O   . GLU A 156 ? 0.46692 0.42674 0.50977 0.06295  -0.03862 -0.04237 163 GLU A O   
1151 C CB  . GLU A 156 ? 0.53151 0.42141 0.55676 0.04939  -0.05670 -0.05386 163 GLU A CB  
1152 C CG  . GLU A 156 ? 0.58373 0.46194 0.62323 0.04966  -0.05970 -0.04299 163 GLU A CG  
1153 C CD  . GLU A 156 ? 0.67053 0.50786 0.70656 0.05119  -0.06495 -0.05020 163 GLU A CD  
1154 O OE1 . GLU A 156 ? 0.70034 0.51992 0.73128 0.06700  -0.06070 -0.05653 163 GLU A OE1 
1155 O OE2 . GLU A 156 ? 0.76951 0.59215 0.80988 0.03656  -0.07314 -0.04965 163 GLU A OE2 
1156 N N   . SER A 157 ? 0.47751 0.43591 0.53348 0.04971  -0.04966 -0.02870 164 SER A N   
1157 C CA  . SER A 157 ? 0.47573 0.46018 0.54490 0.05810  -0.04755 -0.02080 164 SER A CA  
1158 C C   . SER A 157 ? 0.49433 0.47864 0.56914 0.05863  -0.05317 -0.00887 164 SER A C   
1159 O O   . SER A 157 ? 0.47709 0.45934 0.54826 0.04738  -0.05693 -0.00538 164 SER A O   
1160 C CB  . SER A 157 ? 0.47261 0.48850 0.54899 0.04956  -0.04601 -0.02069 164 SER A CB  
1161 O OG  . SER A 157 ? 0.44099 0.48584 0.53308 0.05489  -0.04760 -0.01318 164 SER A OG  
1162 N N   . SER A 158 ? 0.48627 0.47405 0.56969 0.07361  -0.05248 -0.00100 165 SER A N   
1163 C CA  . SER A 158 ? 0.53822 0.53572 0.62727 0.07728  -0.05746 0.01426  165 SER A CA  
1164 C C   . SER A 158 ? 0.59094 0.63167 0.69014 0.07893  -0.06117 0.01940  165 SER A C   
1165 O O   . SER A 158 ? 0.53219 0.58842 0.63814 0.08898  -0.06550 0.03272  165 SER A O   
1166 C CB  . SER A 158 ? 0.54178 0.51492 0.63555 0.09376  -0.05558 0.02271  165 SER A CB  
1167 O OG  . SER A 158 ? 0.57233 0.50320 0.65856 0.08911  -0.05464 0.01632  165 SER A OG  
1168 N N   . ALA A 159 ? 0.50675 0.56725 0.60836 0.06865  -0.06047 0.00983  166 ALA A N   
1169 C CA  . ALA A 159 ? 0.49532 0.59700 0.61134 0.06632  -0.06507 0.01156  166 ALA A CA  
1170 C C   . ALA A 159 ? 0.50217 0.62231 0.63739 0.08467  -0.06174 0.01875  166 ALA A C   
1171 O O   . ALA A 159 ? 0.52388 0.62423 0.65863 0.09667  -0.05216 0.01578  166 ALA A O   
1172 C CB  . ALA A 159 ? 0.47003 0.58764 0.57941 0.05948  -0.07568 0.01692  166 ALA A CB  
1173 N N   . GLY A 160 ? 0.48671 0.64577 0.63846 0.08813  -0.06984 0.02765  167 GLY A N   
1174 C CA  . GLY A 160 ? 0.49831 0.68303 0.67421 0.10627  -0.06617 0.03614  167 GLY A CA  
1175 C C   . GLY A 160 ? 0.46807 0.67638 0.66306 0.10323  -0.05767 0.03031  167 GLY A C   
1176 O O   . GLY A 160 ? 0.44283 0.67552 0.66055 0.11984  -0.05143 0.03782  167 GLY A O   
1177 N N   . GLY A 161 ? 0.45944 0.66182 0.64731 0.08380  -0.05568 0.01921  168 GLY A N   
1178 C CA  . GLY A 161 ? 0.48000 0.70570 0.68692 0.07826  -0.04685 0.01687  168 GLY A CA  
1179 C C   . GLY A 161 ? 0.44471 0.64315 0.63719 0.08425  -0.03054 0.01015  168 GLY A C   
1180 O O   . GLY A 161 ? 0.42288 0.64179 0.63003 0.08240  -0.02010 0.01131  168 GLY A O   
1181 N N   . SER A 162 ? 0.43294 0.58755 0.59737 0.09062  -0.02846 0.00374  169 SER A N   
1182 C CA  . SER A 162 ? 0.42929 0.55808 0.57542 0.09764  -0.01571 -0.00465 169 SER A CA  
1183 C C   . SER A 162 ? 0.50452 0.59098 0.62184 0.08789  -0.02086 -0.01405 169 SER A C   
1184 O O   . SER A 162 ? 0.46513 0.53701 0.57705 0.08254  -0.03100 -0.01240 169 SER A O   
1185 C CB  . SER A 162 ? 0.49307 0.61412 0.63910 0.12412  -0.00567 -0.00395 169 SER A CB  
1186 O OG  . SER A 162 ? 0.49212 0.57916 0.62585 0.13214  -0.01233 -0.00483 169 SER A OG  
1187 N N   . PHE A 163 ? 0.44824 0.51877 0.54807 0.08609  -0.01352 -0.02221 170 PHE A N   
1188 C CA  . PHE A 163 ? 0.46291 0.49697 0.53769 0.07868  -0.01862 -0.03114 170 PHE A CA  
1189 C C   . PHE A 163 ? 0.49096 0.50567 0.54367 0.09048  -0.01009 -0.04113 170 PHE A C   
1190 O O   . PHE A 163 ? 0.46770 0.50017 0.52275 0.10243  0.00241  -0.04008 170 PHE A O   
1191 C CB  . PHE A 163 ? 0.46048 0.49851 0.53384 0.05861  -0.02315 -0.03073 170 PHE A CB  
1192 C CG  . PHE A 163 ? 0.45334 0.50931 0.52970 0.05448  -0.01375 -0.02898 170 PHE A CG  
1193 C CD1 . PHE A 163 ? 0.44020 0.52921 0.54173 0.04873  -0.01053 -0.02122 170 PHE A CD1 
1194 C CD2 . PHE A 163 ? 0.48396 0.52471 0.53893 0.05546  -0.00895 -0.03380 170 PHE A CD2 
1195 C CE1 . PHE A 163 ? 0.43978 0.54399 0.54791 0.04343  -0.00056 -0.01662 170 PHE A CE1 
1196 C CE2 . PHE A 163 ? 0.46719 0.52440 0.52441 0.05259  0.00119  -0.02833 170 PHE A CE2 
1197 C CZ  . PHE A 163 ? 0.47286 0.56064 0.55811 0.04621  0.00644  -0.01888 170 PHE A CZ  
1198 N N   . THR A 164 ? 0.47825 0.45820 0.50932 0.08706  -0.01709 -0.05087 171 THR A N   
1199 C CA  . THR A 164 ? 0.51339 0.47066 0.51715 0.09688  -0.01311 -0.06413 171 THR A CA  
1200 C C   . THR A 164 ? 0.53899 0.48802 0.52505 0.08281  -0.01953 -0.06870 171 THR A C   
1201 O O   . THR A 164 ? 0.49503 0.44258 0.48920 0.06688  -0.02908 -0.06421 171 THR A O   
1202 C CB  . THR A 164 ? 0.55248 0.47163 0.54602 0.10681  -0.01822 -0.07444 171 THR A CB  
1203 O OG1 . THR A 164 ? 0.55589 0.45492 0.55308 0.09079  -0.03225 -0.07349 171 THR A OG1 
1204 C CG2 . THR A 164 ? 0.54171 0.46819 0.55405 0.12389  -0.01148 -0.06733 171 THR A CG2 
1205 N N   . VAL A 165 ? 0.54246 0.48828 0.50338 0.09078  -0.01350 -0.07666 172 VAL A N   
1206 C CA  . VAL A 165 ? 0.56220 0.50116 0.50238 0.08126  -0.02044 -0.08072 172 VAL A CA  
1207 C C   . VAL A 165 ? 0.61680 0.52952 0.52146 0.09277  -0.02316 -0.09908 172 VAL A C   
1208 O O   . VAL A 165 ? 0.61578 0.52889 0.50577 0.11139  -0.01067 -0.10521 172 VAL A O   
1209 C CB  . VAL A 165 ? 0.55592 0.52409 0.49834 0.07808  -0.01019 -0.06832 172 VAL A CB  
1210 C CG1 . VAL A 165 ? 0.59100 0.55248 0.50986 0.07196  -0.01750 -0.07054 172 VAL A CG1 
1211 C CG2 . VAL A 165 ? 0.51615 0.50471 0.49198 0.06485  -0.00972 -0.05427 172 VAL A CG2 
1212 N N   . ARG A 166 ? 0.62972 0.52078 0.52098 0.08201  -0.03966 -0.10852 173 ARG A N   
1213 C CA  . ARG A 166 ? 0.68484 0.54850 0.54024 0.08944  -0.04706 -0.12943 173 ARG A CA  
1214 C C   . ARG A 166 ? 0.69528 0.55770 0.53842 0.07461  -0.06412 -0.13213 173 ARG A C   
1215 O O   . ARG A 166 ? 0.64449 0.51895 0.51211 0.05871  -0.07124 -0.11922 173 ARG A O   
1216 C CB  . ARG A 166 ? 0.74588 0.57214 0.60407 0.09267  -0.05397 -0.14350 173 ARG A CB  
1217 C CG  . ARG A 166 ? 0.75830 0.57014 0.64045 0.07204  -0.07104 -0.13998 173 ARG A CG  
1218 C CD  . ARG A 166 ? 0.82665 0.59714 0.71216 0.07424  -0.07748 -0.15218 173 ARG A CD  
1219 N NE  . ARG A 166 ? 1.10713 0.87180 1.02469 0.05604  -0.08767 -0.14044 173 ARG A NE  
1220 C CZ  . ARG A 166 ? 1.16210 0.91966 1.08544 0.03663  -0.10448 -0.14265 173 ARG A CZ  
1221 N NH1 . ARG A 166 ? 1.03473 0.78964 0.93349 0.03189  -0.11626 -0.15723 173 ARG A NH1 
1222 N NH2 . ARG A 166 ? 0.99059 0.74714 0.94565 0.02218  -0.10955 -0.12850 173 ARG A NH2 
1223 N N   . THR A 167 ? 0.68742 0.53679 0.49132 0.08141  -0.07073 -0.14926 174 THR A N   
1224 C CA  . THR A 167 ? 0.75710 0.60510 0.54878 0.06788  -0.09119 -0.15407 174 THR A CA  
1225 C C   . THR A 167 ? 0.79514 0.61581 0.60590 0.05172  -0.11065 -0.16383 174 THR A C   
1226 O O   . THR A 167 ? 0.86152 0.64847 0.66471 0.05624  -0.11369 -0.18141 174 THR A O   
1227 C CB  . THR A 167 ? 0.82125 0.66388 0.56122 0.08021  -0.09492 -0.17130 174 THR A CB  
1228 O OG1 . THR A 167 ? 0.83309 0.70192 0.55718 0.09661  -0.07296 -0.15905 174 THR A OG1 
1229 C CG2 . THR A 167 ? 0.88038 0.73051 0.60961 0.06646  -0.11782 -0.17286 174 THR A CG2 
1230 N N   . ASP A 168 ? 0.73689 0.57160 0.57469 0.03349  -0.12238 -0.15109 175 ASP A N   
1231 C CA  . ASP A 168 ? 0.85020 0.66560 0.71438 0.01627  -0.13828 -0.15443 175 ASP A CA  
1232 C C   . ASP A 168 ? 0.98692 0.78278 0.82934 0.00787  -0.16195 -0.17602 175 ASP A C   
1233 O O   . ASP A 168 ? 0.96327 0.77820 0.78723 0.00576  -0.17280 -0.17708 175 ASP A O   
1234 C CB  . ASP A 168 ? 0.77374 0.61526 0.67615 0.00175  -0.13963 -0.13180 175 ASP A CB  
1235 C CG  . ASP A 168 ? 0.83433 0.66081 0.76863 -0.01547 -0.15188 -0.13033 175 ASP A CG  
1236 O OD1 . ASP A 168 ? 0.95593 0.75353 0.89566 -0.01397 -0.14961 -0.13706 175 ASP A OD1 
1237 O OD2 . ASP A 168 ? 0.88676 0.73119 0.84273 -0.02971 -0.16275 -0.12054 175 ASP A OD2 
1238 N N   . THR A 169 ? 1.13688 0.89402 0.98209 0.00280  -0.17100 -0.19292 176 THR A N   
1239 C CA  . THR A 169 ? 1.24569 0.97766 1.07259 -0.00808 -0.19599 -0.21742 176 THR A CA  
1240 C C   . THR A 169 ? 1.17911 0.91287 1.04787 -0.03508 -0.21597 -0.21015 176 THR A C   
1241 O O   . THR A 169 ? 1.16859 0.88966 1.02926 -0.04899 -0.24078 -0.22821 176 THR A O   
1242 C CB  . THR A 169 ? 1.36846 1.04968 1.17190 0.00247  -0.19454 -0.24371 176 THR A CB  
1243 O OG1 . THR A 169 ? 1.23486 0.89897 1.07223 0.00381  -0.18074 -0.23138 176 THR A OG1 
1244 C CG2 . THR A 169 ? 1.25374 0.93518 1.00753 0.02973  -0.17872 -0.25636 176 THR A CG2 
1245 N N   . GLY A 170 ? 1.11273 0.86391 1.02565 -0.04283 -0.20601 -0.18436 177 GLY A N   
1246 C CA  . GLY A 170 ? 1.10075 0.85509 1.05760 -0.06682 -0.22024 -0.17406 177 GLY A CA  
1247 C C   . GLY A 170 ? 1.07263 0.86549 1.04204 -0.07998 -0.23671 -0.16567 177 GLY A C   
1248 O O   . GLY A 170 ? 1.06785 0.87290 1.00437 -0.07464 -0.24742 -0.17710 177 GLY A O   
1249 N N   . GLU A 171 ? 1.06236 0.87680 1.07925 -0.09546 -0.23796 -0.14402 178 GLU A N   
1250 C CA  . GLU A 171 ? 0.99860 0.85240 1.03618 -0.10764 -0.25343 -0.13340 178 GLU A CA  
1251 C C   . GLU A 171 ? 0.87246 0.76118 0.89103 -0.09068 -0.24193 -0.12135 178 GLU A C   
1252 O O   . GLU A 171 ? 0.80413 0.69973 0.82448 -0.07791 -0.21815 -0.10703 178 GLU A O   
1253 C CB  . GLU A 171 ? 1.04127 0.91313 1.13597 -0.12421 -0.25120 -0.10972 178 GLU A CB  
1254 C CG  . GLU A 171 ? 1.20761 1.04271 1.32650 -0.13884 -0.25399 -0.11338 178 GLU A CG  
1255 C CD  . GLU A 171 ? 1.47322 1.30817 1.61160 -0.15999 -0.27405 -0.12039 178 GLU A CD  
1256 O OE1 . GLU A 171 ? 1.29985 1.12862 1.47730 -0.17487 -0.27095 -0.10781 178 GLU A OE1 
1257 O OE2 . GLU A 171 ? 1.47781 1.32158 1.59092 -0.16055 -0.29026 -0.13674 178 GLU A OE2 
1258 N N   . PRO A 172 ? 0.82968 0.74029 0.83016 -0.09026 -0.25865 -0.12601 179 PRO A N   
1259 C CA  . PRO A 172 ? 0.79734 0.73978 0.78382 -0.07434 -0.24701 -0.11042 179 PRO A CA  
1260 C C   . PRO A 172 ? 0.73303 0.70766 0.76472 -0.07749 -0.23660 -0.08244 179 PRO A C   
1261 O O   . PRO A 172 ? 0.75753 0.74751 0.82958 -0.09342 -0.24821 -0.07403 179 PRO A O   
1262 C CB  . PRO A 172 ? 0.76923 0.72770 0.72838 -0.07490 -0.27156 -0.12076 179 PRO A CB  
1263 C CG  . PRO A 172 ? 0.83353 0.76997 0.79395 -0.09331 -0.29825 -0.14410 179 PRO A CG  
1264 C CD  . PRO A 172 ? 0.85637 0.76183 0.84738 -0.10454 -0.29018 -0.14611 179 PRO A CD  
1265 N N   . MET A 173 ? 0.69683 0.68137 0.72232 -0.06200 -0.21384 -0.06830 180 MET A N   
1266 C CA  . MET A 173 ? 0.67363 0.68267 0.73524 -0.06116 -0.20032 -0.04474 180 MET A CA  
1267 C C   . MET A 173 ? 0.62146 0.66448 0.68824 -0.05478 -0.20512 -0.02959 180 MET A C   
1268 O O   . MET A 173 ? 0.63631 0.70253 0.73866 -0.05565 -0.19918 -0.01119 180 MET A O   
1269 C CB  . MET A 173 ? 0.67521 0.67281 0.73010 -0.04932 -0.17365 -0.03909 180 MET A CB  
1270 C CG  . MET A 173 ? 0.77097 0.74263 0.83122 -0.05376 -0.16598 -0.04613 180 MET A CG  
1271 S SD  . MET A 173 ? 0.85629 0.81871 0.90113 -0.03903 -0.14011 -0.04314 180 MET A SD  
1272 C CE  . MET A 173 ? 0.59236 0.58146 0.66210 -0.03595 -0.12728 -0.02218 180 MET A CE  
1273 N N   . GLY A 174 ? 0.58790 0.63489 0.61941 -0.04642 -0.21443 -0.03551 181 GLY A N   
1274 C CA  . GLY A 174 ? 0.56068 0.63808 0.59371 -0.03656 -0.21630 -0.01774 181 GLY A CA  
1275 C C   . GLY A 174 ? 0.52664 0.59962 0.54860 -0.02027 -0.19014 -0.00501 181 GLY A C   
1276 O O   . GLY A 174 ? 0.52399 0.59652 0.51239 -0.00841 -0.18700 -0.00359 181 GLY A O   
1277 N N   . ARG A 175 ? 0.45722 0.52650 0.50664 -0.02012 -0.17126 0.00425  182 ARG A N   
1278 C CA  . ARG A 175 ? 0.47657 0.53743 0.51994 -0.00822 -0.14737 0.01346  182 ARG A CA  
1279 C C   . ARG A 175 ? 0.42206 0.47583 0.49266 -0.01202 -0.13209 0.01612  182 ARG A C   
1280 O O   . ARG A 175 ? 0.43629 0.50415 0.53803 -0.01824 -0.13603 0.02257  182 ARG A O   
1281 C CB  . ARG A 175 ? 0.42824 0.50822 0.47526 0.00382  -0.14432 0.03328  182 ARG A CB  
1282 C CG  . ARG A 175 ? 0.42272 0.48868 0.46006 0.01463  -0.12142 0.04155  182 ARG A CG  
1283 C CD  . ARG A 175 ? 0.42950 0.50861 0.48518 0.02566  -0.11448 0.06328  182 ARG A CD  
1284 N NE  . ARG A 175 ? 0.39011 0.47995 0.48298 0.02375  -0.11209 0.06913  182 ARG A NE  
1285 C CZ  . ARG A 175 ? 0.44712 0.56511 0.56397 0.02532  -0.12459 0.08059  182 ARG A CZ  
1286 N NH1 . ARG A 175 ? 0.39208 0.53068 0.49885 0.02788  -0.14349 0.08662  182 ARG A NH1 
1287 N NH2 . ARG A 175 ? 0.37173 0.50051 0.52344 0.02502  -0.11802 0.08676  182 ARG A NH2 
1288 N N   . GLY A 176 ? 0.41058 0.44551 0.46946 -0.00813 -0.11490 0.01188  183 GLY A N   
1289 C CA  . GLY A 176 ? 0.38169 0.41038 0.45908 -0.00999 -0.10080 0.01350  183 GLY A CA  
1290 C C   . GLY A 176 ? 0.46581 0.47503 0.52978 -0.01325 -0.09554 0.00059  183 GLY A C   
1291 O O   . GLY A 176 ? 0.45572 0.45503 0.49592 -0.01115 -0.09789 -0.00860 183 GLY A O   
1292 N N   . THR A 177 ? 0.39086 0.39669 0.46966 -0.01657 -0.08765 0.00108  184 THR A N   
1293 C CA  . THR A 177 ? 0.38344 0.37439 0.45323 -0.01798 -0.08227 -0.00781 184 THR A CA  
1294 C C   . THR A 177 ? 0.48419 0.47482 0.57139 -0.02485 -0.08391 -0.00581 184 THR A C   
1295 O O   . THR A 177 ? 0.44689 0.44973 0.55314 -0.02573 -0.07926 0.00398  184 THR A O   
1296 C CB  . THR A 177 ? 0.46648 0.45386 0.53132 -0.01272 -0.06746 -0.00725 184 THR A CB  
1297 O OG1 . THR A 177 ? 0.45229 0.43908 0.50398 -0.00756 -0.06447 -0.00622 184 THR A OG1 
1298 C CG2 . THR A 177 ? 0.44048 0.41886 0.49926 -0.01365 -0.06398 -0.01465 184 THR A CG2 
1299 N N   . LYS A 178 ? 0.42482 0.40108 0.50566 -0.02829 -0.08899 -0.01372 185 LYS A N   
1300 C CA  . LYS A 178 ? 0.45981 0.43159 0.55606 -0.03452 -0.08949 -0.00966 185 LYS A CA  
1301 C C   . LYS A 178 ? 0.46784 0.42900 0.55347 -0.02920 -0.08091 -0.01265 185 LYS A C   
1302 O O   . LYS A 178 ? 0.45550 0.40366 0.52570 -0.02511 -0.08287 -0.02229 185 LYS A O   
1303 C CB  . LYS A 178 ? 0.47893 0.43946 0.58099 -0.04390 -0.10489 -0.01506 185 LYS A CB  
1304 C CG  . LYS A 178 ? 0.59888 0.55068 0.71972 -0.05154 -0.10487 -0.00836 185 LYS A CG  
1305 C CD  . LYS A 178 ? 0.69692 0.64683 0.83883 -0.06604 -0.12047 -0.00785 185 LYS A CD  
1306 C CE  . LYS A 178 ? 0.72324 0.66704 0.84840 -0.06791 -0.13676 -0.02367 185 LYS A CE  
1307 N NZ  . LYS A 178 ? 0.84061 0.75264 0.93990 -0.06371 -0.14060 -0.04133 185 LYS A NZ  
1308 N N   . VAL A 179 ? 0.41755 0.38659 0.51060 -0.02784 -0.07142 -0.00412 186 VAL A N   
1309 C CA  . VAL A 179 ? 0.37383 0.33870 0.45785 -0.02262 -0.06518 -0.00493 186 VAL A CA  
1310 C C   . VAL A 179 ? 0.44945 0.40819 0.54436 -0.02589 -0.06611 0.00417  186 VAL A C   
1311 O O   . VAL A 179 ? 0.39165 0.36105 0.49906 -0.02867 -0.06117 0.01608  186 VAL A O   
1312 C CB  . VAL A 179 ? 0.42120 0.39843 0.50006 -0.01820 -0.05523 -0.00345 186 VAL A CB  
1313 C CG1 . VAL A 179 ? 0.39714 0.37485 0.46749 -0.01389 -0.05231 -0.00380 186 VAL A CG1 
1314 C CG2 . VAL A 179 ? 0.41217 0.39099 0.48370 -0.01610 -0.05354 -0.01040 186 VAL A CG2 
1315 N N   . ILE A 180 ? 0.42167 0.36277 0.51249 -0.02428 -0.07080 0.00006  187 ILE A N   
1316 C CA  . ILE A 180 ? 0.43658 0.36583 0.53861 -0.02682 -0.07155 0.01016  187 ILE A CA  
1317 C C   . ILE A 180 ? 0.46057 0.39350 0.55353 -0.01690 -0.06488 0.01579  187 ILE A C   
1318 O O   . ILE A 180 ? 0.47394 0.40231 0.55575 -0.00875 -0.06560 0.00746  187 ILE A O   
1319 C CB  . ILE A 180 ? 0.46725 0.36913 0.57152 -0.03063 -0.08175 0.00156  187 ILE A CB  
1320 C CG1 . ILE A 180 ? 0.49399 0.39631 0.60325 -0.04052 -0.09196 -0.00656 187 ILE A CG1 
1321 C CG2 . ILE A 180 ? 0.48341 0.36863 0.60393 -0.03494 -0.08197 0.01439  187 ILE A CG2 
1322 C CD1 . ILE A 180 ? 0.54799 0.42340 0.64696 -0.04171 -0.10341 -0.02332 187 ILE A CD1 
1323 N N   . LEU A 181 ? 0.42937 0.37387 0.52721 -0.01668 -0.05831 0.03102  188 LEU A N   
1324 C CA  . LEU A 181 ? 0.45255 0.40539 0.53973 -0.00711 -0.05378 0.03837  188 LEU A CA  
1325 C C   . LEU A 181 ? 0.48430 0.42118 0.58104 -0.00548 -0.05398 0.05350  188 LEU A C   
1326 O O   . LEU A 181 ? 0.47572 0.41238 0.58571 -0.01151 -0.05004 0.06932  188 LEU A O   
1327 C CB  . LEU A 181 ? 0.45041 0.42650 0.52954 -0.00547 -0.04583 0.04464  188 LEU A CB  
1328 C CG  . LEU A 181 ? 0.43150 0.41784 0.50483 -0.00756 -0.04408 0.03158  188 LEU A CG  
1329 C CD1 . LEU A 181 ? 0.46607 0.46942 0.53183 -0.00486 -0.03469 0.03735  188 LEU A CD1 
1330 C CD2 . LEU A 181 ? 0.42864 0.41626 0.49020 -0.00381 -0.04798 0.01703  188 LEU A CD2 
1331 N N   . HIS A 182 ? 0.46449 0.38834 0.55696 0.00338  -0.05729 0.05047  189 HIS A N   
1332 C CA  . HIS A 182 ? 0.53065 0.43671 0.63135 0.00840  -0.05653 0.06642  189 HIS A CA  
1333 C C   . HIS A 182 ? 0.54746 0.47701 0.63795 0.01808  -0.05141 0.08296  189 HIS A C   
1334 O O   . HIS A 182 ? 0.52526 0.46758 0.60493 0.02926  -0.05358 0.07969  189 HIS A O   
1335 C CB  . HIS A 182 ? 0.51424 0.39575 0.61446 0.01707  -0.06108 0.05589  189 HIS A CB  
1336 C CG  . HIS A 182 ? 0.54092 0.40249 0.64187 0.00964  -0.06695 0.03563  189 HIS A CG  
1337 N ND1 . HIS A 182 ? 0.57479 0.40252 0.68728 0.00172  -0.07213 0.03318  189 HIS A ND1 
1338 C CD2 . HIS A 182 ? 0.54672 0.41770 0.63681 0.00867  -0.06917 0.01731  189 HIS A CD2 
1339 C CE1 . HIS A 182 ? 0.60355 0.42233 0.70883 -0.00307 -0.07862 0.01239  189 HIS A CE1 
1340 N NE2 . HIS A 182 ? 0.57193 0.41733 0.66328 0.00191  -0.07595 0.00414  189 HIS A NE2 
1341 N N   . LEU A 183 ? 0.55351 0.49187 0.64757 0.01397  -0.04477 0.10144  190 LEU A N   
1342 C CA  . LEU A 183 ? 0.52228 0.48797 0.59896 0.02264  -0.03957 0.11455  190 LEU A CA  
1343 C C   . LEU A 183 ? 0.62889 0.59236 0.70169 0.03639  -0.04112 0.13095  190 LEU A C   
1344 O O   . LEU A 183 ? 0.62545 0.56152 0.71400 0.03829  -0.04181 0.14070  190 LEU A O   
1345 C CB  . LEU A 183 ? 0.51958 0.49595 0.60040 0.01677  -0.02913 0.13220  190 LEU A CB  
1346 C CG  . LEU A 183 ? 0.50433 0.49028 0.58976 0.00664  -0.02578 0.12011  190 LEU A CG  
1347 C CD1 . LEU A 183 ? 0.50928 0.51181 0.59945 0.00485  -0.01255 0.14100  190 LEU A CD1 
1348 C CD2 . LEU A 183 ? 0.45956 0.46119 0.52350 0.01061  -0.02877 0.09791  190 LEU A CD2 
1349 N N   . LYS A 184 ? 0.63020 0.62077 0.60266 0.01022  -0.05321 0.10369  191 LYS A N   
1350 C CA  . LYS A 184 ? 0.65486 0.64699 0.63116 0.02642  -0.06269 0.11171  191 LYS A CA  
1351 C C   . LYS A 184 ? 0.69241 0.66265 0.65617 0.03466  -0.05752 0.13709  191 LYS A C   
1352 O O   . LYS A 184 ? 0.66366 0.62474 0.61682 0.02653  -0.04711 0.14673  191 LYS A O   
1353 C CB  . LYS A 184 ? 0.63331 0.65061 0.60196 0.03353  -0.07670 0.10366  191 LYS A CB  
1354 C CG  . LYS A 184 ? 0.60723 0.64631 0.60307 0.02250  -0.07759 0.08233  191 LYS A CG  
1355 C CD  . LYS A 184 ? 0.58983 0.65041 0.58716 0.02280  -0.09198 0.06852  191 LYS A CD  
1356 C CE  . LYS A 184 ? 0.58563 0.66705 0.62680 0.00900  -0.08895 0.05078  191 LYS A CE  
1357 N NZ  . LYS A 184 ? 0.64990 0.75238 0.70897 0.00699  -0.10652 0.03049  191 LYS A NZ  
1358 N N   . GLU A 185 ? 0.74649 0.70946 0.71543 0.05259  -0.06269 0.15085  192 GLU A N   
1359 C CA  . GLU A 185 ? 0.78271 0.71943 0.74706 0.06178  -0.05203 0.18263  192 GLU A CA  
1360 C C   . GLU A 185 ? 0.76297 0.70809 0.68566 0.06930  -0.04658 0.20224  192 GLU A C   
1361 O O   . GLU A 185 ? 0.76247 0.69076 0.68470 0.06555  -0.02802 0.22619  192 GLU A O   
1362 C CB  . GLU A 185 ? 0.82433 0.75069 0.79866 0.08523  -0.05889 0.19740  192 GLU A CB  
1363 C CG  . GLU A 185 ? 1.04794 0.93784 1.06577 0.08144  -0.04961 0.20167  192 GLU A CG  
1364 C CD  . GLU A 185 ? 1.32216 1.18660 1.34459 0.10714  -0.04742 0.23523  192 GLU A CD  
1365 O OE1 . GLU A 185 ? 1.24970 1.13086 1.26334 0.13087  -0.06322 0.23428  192 GLU A OE1 
1366 O OE2 . GLU A 185 ? 1.55473 1.38319 1.59447 0.10440  -0.02915 0.26414  192 GLU A OE2 
1367 N N   . ASP A 186 ? 0.73680 0.71041 0.62872 0.08061  -0.06205 0.18992  193 ASP A N   
1368 C CA  . ASP A 186 ? 0.75352 0.73959 0.59823 0.09519  -0.06027 0.20231  193 ASP A CA  
1369 C C   . ASP A 186 ? 0.73571 0.73005 0.57203 0.07771  -0.05499 0.18395  193 ASP A C   
1370 O O   . ASP A 186 ? 0.75326 0.76231 0.55011 0.09106  -0.05647 0.18376  193 ASP A O   
1371 C CB  . ASP A 186 ? 0.82439 0.83942 0.64015 0.12220  -0.08551 0.19239  193 ASP A CB  
1372 C CG  . ASP A 186 ? 0.94000 0.97913 0.78326 0.10962  -0.10667 0.15084  193 ASP A CG  
1373 O OD1 . ASP A 186 ? 0.79615 0.82637 0.67918 0.08534  -0.09950 0.13779  193 ASP A OD1 
1374 O OD2 . ASP A 186 ? 1.06303 1.13208 0.89039 0.12516  -0.12995 0.13090  193 ASP A OD2 
1375 N N   . GLN A 187 ? 0.71126 0.69732 0.58046 0.05253  -0.04937 0.16814  194 GLN A N   
1376 C CA  . GLN A 187 ? 0.70622 0.69799 0.57046 0.03874  -0.04525 0.15229  194 GLN A CA  
1377 C C   . GLN A 187 ? 0.66742 0.64595 0.54892 0.02457  -0.02648 0.16378  194 GLN A C   
1378 O O   . GLN A 187 ? 0.64470 0.62549 0.53525 0.01138  -0.02447 0.14934  194 GLN A O   
1379 C CB  . GLN A 187 ? 0.64567 0.64533 0.53127 0.02554  -0.05594 0.12405  194 GLN A CB  
1380 C CG  . GLN A 187 ? 0.66094 0.68002 0.54749 0.03533  -0.07582 0.10713  194 GLN A CG  
1381 C CD  . GLN A 187 ? 0.66804 0.70109 0.52066 0.05025  -0.08705 0.09815  194 GLN A CD  
1382 O OE1 . GLN A 187 ? 0.68015 0.70877 0.51611 0.04704  -0.07961 0.09431  194 GLN A OE1 
1383 N NE2 . GLN A 187 ? 0.69474 0.74761 0.53622 0.07025  -0.10703 0.09172  194 GLN A NE2 
1384 N N   . THR A 188 ? 0.66401 0.62965 0.55530 0.02808  -0.01268 0.19053  195 THR A N   
1385 C CA  . THR A 188 ? 0.69823 0.65570 0.62165 0.01265  0.00341  0.19834  195 THR A CA  
1386 C C   . THR A 188 ? 0.69977 0.67160 0.60624 0.01421  0.01733  0.20608  195 THR A C   
1387 O O   . THR A 188 ? 0.68743 0.66084 0.62686 0.00114  0.02923  0.20904  195 THR A O   
1388 C CB  . THR A 188 ? 0.69291 0.62860 0.64792 0.01305  0.01628  0.22505  195 THR A CB  
1389 O OG1 . THR A 188 ? 0.75929 0.69512 0.68195 0.03387  0.02915  0.25929  195 THR A OG1 
1390 C CG2 . THR A 188 ? 0.70070 0.62056 0.67697 0.01384  0.00248  0.21360  195 THR A CG2 
1391 N N   . GLU A 189 ? 0.70462 0.69022 0.56423 0.03155  0.01460  0.20551  196 GLU A N   
1392 C CA  . GLU A 189 ? 0.69835 0.69920 0.53926 0.03719  0.02826  0.20869  196 GLU A CA  
1393 C C   . GLU A 189 ? 0.69589 0.70105 0.55644 0.02212  0.02379  0.18445  196 GLU A C   
1394 O O   . GLU A 189 ? 0.67871 0.69588 0.54406 0.02267  0.03783  0.18871  196 GLU A O   
1395 C CB  . GLU A 189 ? 0.73603 0.75114 0.51972 0.06254  0.02073  0.20276  196 GLU A CB  
1396 C CG  . GLU A 189 ? 0.70034 0.71830 0.47543 0.05993  -0.00352 0.16436  196 GLU A CG  
1397 C CD  . GLU A 189 ? 0.84098 0.87422 0.56846 0.08526  -0.01849 0.14980  196 GLU A CD  
1398 O OE1 . GLU A 189 ? 0.88067 0.91849 0.59544 0.09750  -0.03307 0.15180  196 GLU A OE1 
1399 O OE2 . GLU A 189 ? 0.78026 0.82284 0.48413 0.09546  -0.01789 0.13311  196 GLU A OE2 
1400 N N   . TYR A 190 ? 0.61369 0.61147 0.48579 0.01159  0.00665  0.16208  197 TYR A N   
1401 C CA  . TYR A 190 ? 0.64629 0.64610 0.53125 0.00211  0.00304  0.14456  197 TYR A CA  
1402 C C   . TYR A 190 ? 0.61814 0.61973 0.54247 -0.01080 0.00671  0.14599  197 TYR A C   
1403 O O   . TYR A 190 ? 0.58327 0.58930 0.51556 -0.01470 0.00122  0.13272  197 TYR A O   
1404 C CB  . TYR A 190 ? 0.61560 0.60850 0.49553 -0.00102 -0.01194 0.12527  197 TYR A CB  
1405 C CG  . TYR A 190 ? 0.65974 0.65465 0.51356 0.00997  -0.02074 0.11543  197 TYR A CG  
1406 C CD1 . TYR A 190 ? 0.67511 0.67281 0.50967 0.01891  -0.01974 0.10529  197 TYR A CD1 
1407 C CD2 . TYR A 190 ? 0.66694 0.66376 0.51831 0.01401  -0.03252 0.11225  197 TYR A CD2 
1408 C CE1 . TYR A 190 ? 0.69289 0.69449 0.50651 0.03053  -0.03239 0.08778  197 TYR A CE1 
1409 C CE2 . TYR A 190 ? 0.66901 0.67428 0.50113 0.02574  -0.04616 0.09682  197 TYR A CE2 
1410 C CZ  . TYR A 190 ? 0.67528 0.68263 0.48850 0.03351  -0.04706 0.08252  197 TYR A CZ  
1411 O OH  . TYR A 190 ? 0.67432 0.69185 0.47128 0.04656  -0.06510 0.05884  197 TYR A OH  
1412 N N   . LEU A 191 ? 0.60505 0.60308 0.55626 -0.01571 0.01480  0.16106  198 LEU A N   
1413 C CA  . LEU A 191 ? 0.59453 0.59821 0.59472 -0.02840 0.01771  0.15842  198 LEU A CA  
1414 C C   . LEU A 191 ? 0.63342 0.65373 0.65595 -0.02915 0.03742  0.17549  198 LEU A C   
1415 O O   . LEU A 191 ? 0.61684 0.64911 0.69137 -0.04092 0.03905  0.17026  198 LEU A O   
1416 C CB  . LEU A 191 ? 0.59694 0.58284 0.63049 -0.03617 0.01517  0.16077  198 LEU A CB  
1417 C CG  . LEU A 191 ? 0.60793 0.58213 0.62675 -0.03367 -0.00154 0.14328  198 LEU A CG  
1418 C CD1 . LEU A 191 ? 0.65720 0.61081 0.70996 -0.03709 -0.00220 0.14639  198 LEU A CD1 
1419 C CD2 . LEU A 191 ? 0.57070 0.55711 0.58795 -0.03582 -0.01469 0.11698  198 LEU A CD2 
1420 N N   . GLU A 192 ? 0.62372 0.64946 0.61073 -0.01526 0.05200  0.19311  199 GLU A N   
1421 C CA  . GLU A 192 ? 0.67494 0.72146 0.67905 -0.01199 0.07653  0.21238  199 GLU A CA  
1422 C C   . GLU A 192 ? 0.64750 0.71623 0.65370 -0.00882 0.07290  0.19407  199 GLU A C   
1423 O O   . GLU A 192 ? 0.63972 0.70289 0.60872 -0.00046 0.05773  0.17510  199 GLU A O   
1424 C CB  . GLU A 192 ? 0.74360 0.79141 0.69749 0.00903  0.09402  0.23698  199 GLU A CB  
1425 C CG  . GLU A 192 ? 0.79696 0.82517 0.74830 0.01215  0.10206  0.26461  199 GLU A CG  
1426 C CD  . GLU A 192 ? 0.99725 1.02343 1.01404 -0.00200 0.12798  0.29395  199 GLU A CD  
1427 O OE1 . GLU A 192 ? 1.24682 1.29713 1.28928 -0.00307 0.15254  0.30813  199 GLU A OE1 
1428 O OE2 . GLU A 192 ? 1.00907 1.00954 1.05848 -0.01214 0.12492  0.30215  199 GLU A OE2 
1429 N N   . GLU A 193 ? 0.64802 0.74207 0.70515 -0.01519 0.08788  0.20089  200 GLU A N   
1430 C CA  . GLU A 193 ? 0.65126 0.77042 0.71784 -0.00919 0.08356  0.18433  200 GLU A CA  
1431 C C   . GLU A 193 ? 0.64826 0.77237 0.66068 0.01378  0.09393  0.18617  200 GLU A C   
1432 O O   . GLU A 193 ? 0.61399 0.73358 0.60102 0.02368  0.07933  0.16621  200 GLU A O   
1433 C CB  . GLU A 193 ? 0.67871 0.83149 0.82280 -0.02071 0.09733  0.19008  200 GLU A CB  
1434 C CG  . GLU A 193 ? 0.77492 0.96296 0.92812 -0.00692 0.10552  0.18478  200 GLU A CG  
1435 C CD  . GLU A 193 ? 0.94662 1.17507 1.19046 -0.02037 0.11002  0.18119  200 GLU A CD  
1436 O OE1 . GLU A 193 ? 1.05623 1.31531 1.31721 -0.01000 0.10170  0.16543  200 GLU A OE1 
1437 O OE2 . GLU A 193 ? 0.78363 1.01335 1.08771 -0.04084 0.12103  0.19321  200 GLU A OE2 
1438 N N   . ARG A 194 ? 0.65525 0.78747 0.64866 0.02513  0.11994  0.21005  201 ARG A N   
1439 C CA  . ARG A 194 ? 0.68656 0.82794 0.62659 0.05139  0.12928  0.20611  201 ARG A CA  
1440 C C   . ARG A 194 ? 0.70814 0.82124 0.58655 0.06192  0.10601  0.18546  201 ARG A C   
1441 O O   . ARG A 194 ? 0.68310 0.79697 0.52707 0.08050  0.10208  0.16646  201 ARG A O   
1442 C CB  . ARG A 194 ? 0.73386 0.89612 0.66177 0.06601  0.16517  0.23873  201 ARG A CB  
1443 C CG  . ARG A 194 ? 0.91201 1.05461 0.81070 0.06789  0.17002  0.26328  201 ARG A CG  
1444 C CD  . ARG A 194 ? 1.00080 1.16614 0.88917 0.08524  0.21178  0.30453  201 ARG A CD  
1445 N NE  . ARG A 194 ? 1.30982 1.45505 1.16901 0.09161  0.21767  0.33442  201 ARG A NE  
1446 C CZ  . ARG A 194 ? 1.37675 1.53255 1.22311 0.10809  0.25205  0.37520  201 ARG A CZ  
1447 N NH1 . ARG A 194 ? 1.27165 1.45920 1.13565 0.11766  0.28385  0.38810  201 ARG A NH1 
1448 N NH2 . ARG A 194 ? 1.49512 1.62584 1.31965 0.11457  0.24557  0.39038  201 ARG A NH2 
1449 N N   . ARG A 195 ? 0.68752 0.77678 0.55897 0.05055  0.09021  0.18605  202 ARG A N   
1450 C CA  . ARG A 195 ? 0.70571 0.77361 0.53495 0.05701  0.06701  0.16399  202 ARG A CA  
1451 C C   . ARG A 195 ? 0.66406 0.71784 0.50795 0.04790  0.04825  0.13938  202 ARG A C   
1452 O O   . ARG A 195 ? 0.67762 0.71959 0.49744 0.05737  0.03730  0.11819  202 ARG A O   
1453 C CB  . ARG A 195 ? 0.71453 0.76700 0.53801 0.04998  0.05756  0.17349  202 ARG A CB  
1454 C CG  . ARG A 195 ? 0.71589 0.75405 0.50801 0.05534  0.03324  0.14984  202 ARG A CG  
1455 C CD  . ARG A 195 ? 0.77238 0.82196 0.51161 0.08254  0.03242  0.14292  202 ARG A CD  
1456 N NE  . ARG A 195 ? 0.76688 0.80825 0.48832 0.08626  0.00563  0.11768  202 ARG A NE  
1457 C CZ  . ARG A 195 ? 0.78261 0.81934 0.49582 0.09125  -0.01082 0.08314  202 ARG A CZ  
1458 N NH1 . ARG A 195 ? 0.77546 0.81086 0.48917 0.09644  -0.00341 0.07025  202 ARG A NH1 
1459 N NH2 . ARG A 195 ? 0.75910 0.79250 0.47111 0.09113  -0.03552 0.05963  202 ARG A NH2 
1460 N N   . ILE A 196 ? 0.64322 0.69770 0.52754 0.03141  0.04439  0.14168  203 ILE A N   
1461 C CA  . ILE A 196 ? 0.62563 0.66927 0.51756 0.02821  0.03009  0.12559  203 ILE A CA  
1462 C C   . ILE A 196 ? 0.62364 0.67542 0.51283 0.04376  0.03570  0.11801  203 ILE A C   
1463 O O   . ILE A 196 ? 0.60811 0.64033 0.48547 0.05000  0.02704  0.10490  203 ILE A O   
1464 C CB  . ILE A 196 ? 0.59352 0.64381 0.52179 0.01407  0.02306  0.12745  203 ILE A CB  
1465 C CG1 . ILE A 196 ? 0.56735 0.60463 0.49796 0.00166  0.01652  0.13036  203 ILE A CG1 
1466 C CG2 . ILE A 196 ? 0.53583 0.58004 0.46290 0.01821  0.01128  0.11681  203 ILE A CG2 
1467 C CD1 . ILE A 196 ? 0.56105 0.60777 0.53165 -0.01037 0.01101  0.12838  203 ILE A CD1 
1468 N N   . LYS A 197 ? 0.62275 0.70289 0.52845 0.05094  0.05261  0.12751  204 LYS A N   
1469 C CA  . LYS A 197 ? 0.62779 0.72010 0.53403 0.06946  0.05953  0.11952  204 LYS A CA  
1470 C C   . LYS A 197 ? 0.66222 0.73623 0.52445 0.08750  0.05908  0.10349  204 LYS A C   
1471 O O   . LYS A 197 ? 0.66139 0.72088 0.51989 0.09994  0.05346  0.08770  204 LYS A O   
1472 C CB  . LYS A 197 ? 0.61406 0.74729 0.55260 0.07362  0.08205  0.13404  204 LYS A CB  
1473 C CG  . LYS A 197 ? 0.67871 0.83769 0.67610 0.06251  0.07725  0.13633  204 LYS A CG  
1474 C CD  . LYS A 197 ? 0.85372 1.05806 0.89259 0.07084  0.10021  0.14512  204 LYS A CD  
1475 C CE  . LYS A 197 ? 0.90574 1.14065 1.01729 0.04961  0.10174  0.15287  204 LYS A CE  
1476 N NZ  . LYS A 197 ? 0.91737 1.18808 1.06906 0.04807  0.13648  0.17473  204 LYS A NZ  
1477 N N   . GLU A 198 ? 0.67517 0.74926 0.50496 0.09160  0.06328  0.10562  205 GLU A N   
1478 C CA  . GLU A 198 ? 0.71577 0.77794 0.50329 0.11127  0.05745  0.08233  205 GLU A CA  
1479 C C   . GLU A 198 ? 0.71827 0.74319 0.50740 0.10227  0.03385  0.05963  205 GLU A C   
1480 O O   . GLU A 198 ? 0.75319 0.76054 0.53429 0.11528  0.02692  0.03403  205 GLU A O   
1481 C CB  . GLU A 198 ? 0.76991 0.84566 0.51802 0.12145  0.06332  0.09068  205 GLU A CB  
1482 C CG  . GLU A 198 ? 0.82632 0.89059 0.53032 0.13950  0.04555  0.05889  205 GLU A CG  
1483 C CD  . GLU A 198 ? 1.06180 1.14200 0.72245 0.15258  0.04582  0.06943  205 GLU A CD  
1484 O OE1 . GLU A 198 ? 1.02378 1.09999 0.69707 0.13572  0.04343  0.09177  205 GLU A OE1 
1485 O OE2 . GLU A 198 ? 0.91706 1.01429 0.52833 0.18340  0.04783  0.05484  205 GLU A OE2 
1486 N N   . ILE A 199 ? 0.70341 0.71553 0.50860 0.08031  0.02338  0.06841  206 ILE A N   
1487 C CA  . ILE A 199 ? 0.72962 0.71047 0.54432 0.06989  0.00681  0.05236  206 ILE A CA  
1488 C C   . ILE A 199 ? 0.73337 0.69485 0.57060 0.07101  0.00836  0.05159  206 ILE A C   
1489 O O   . ILE A 199 ? 0.78777 0.72002 0.63215 0.07353  0.00185  0.03405  206 ILE A O   
1490 C CB  . ILE A 199 ? 0.68801 0.66642 0.51399 0.04967  -0.00037 0.06423  206 ILE A CB  
1491 C CG1 . ILE A 199 ? 0.71555 0.70868 0.51803 0.05361  -0.00394 0.06557  206 ILE A CG1 
1492 C CG2 . ILE A 199 ? 0.71647 0.66780 0.56157 0.03776  -0.01089 0.05314  206 ILE A CG2 
1493 C CD1 . ILE A 199 ? 0.70355 0.69779 0.51942 0.03784  -0.00771 0.08055  206 ILE A CD1 
1494 N N   . VAL A 200 ? 0.68746 0.66485 0.54008 0.07062  0.01609  0.07023  207 VAL A N   
1495 C CA  . VAL A 200 ? 0.71348 0.67650 0.58210 0.07768  0.01616  0.07394  207 VAL A CA  
1496 C C   . VAL A 200 ? 0.75753 0.71216 0.62297 0.09994  0.02102  0.05873  207 VAL A C   
1497 O O   . VAL A 200 ? 0.78408 0.70501 0.65867 0.10689  0.01855  0.05291  207 VAL A O   
1498 C CB  . VAL A 200 ? 0.67582 0.66758 0.56166 0.07617  0.01768  0.09159  207 VAL A CB  
1499 C CG1 . VAL A 200 ? 0.67094 0.65621 0.56686 0.09290  0.01653  0.09640  207 VAL A CG1 
1500 C CG2 . VAL A 200 ? 0.61874 0.61119 0.50761 0.05754  0.01060  0.10045  207 VAL A CG2 
1501 N N   . LYS A 201 ? 0.75125 0.73506 0.60545 0.11327  0.03061  0.05344  208 LYS A N   
1502 C CA  . LYS A 201 ? 0.79562 0.77573 0.64393 0.13879  0.03651  0.03489  208 LYS A CA  
1503 C C   . LYS A 201 ? 0.84927 0.79325 0.68265 0.14319  0.02569  0.00414  208 LYS A C   
1504 O O   . LYS A 201 ? 0.91133 0.82777 0.75343 0.15901  0.02400  -0.01483 208 LYS A O   
1505 C CB  . LYS A 201 ? 0.75801 0.78397 0.59548 0.15349  0.05399  0.03854  208 LYS A CB  
1506 C CG  . LYS A 201 ? 0.88272 0.91078 0.70371 0.18437  0.06202  0.01426  208 LYS A CG  
1507 C CD  . LYS A 201 ? 0.97154 1.05188 0.78301 0.20009  0.08634  0.02499  208 LYS A CD  
1508 C CE  . LYS A 201 ? 1.07597 1.17499 0.90426 0.22828  0.09992  0.01669  208 LYS A CE  
1509 N NZ  . LYS A 201 ? 1.11114 1.24833 0.98880 0.22140  0.11018  0.04280  208 LYS A NZ  
1510 N N   . LYS A 202 ? 0.87461 0.81819 0.69142 0.13020  0.01623  -0.00364 209 LYS A N   
1511 C CA  . LYS A 202 ? 0.89105 0.80988 0.69976 0.13457  0.00096  -0.04008 209 LYS A CA  
1512 C C   . LYS A 202 ? 0.93987 0.81250 0.78739 0.11634  -0.00927 -0.04561 209 LYS A C   
1513 O O   . LYS A 202 ? 0.97777 0.81803 0.84171 0.12256  -0.01820 -0.07718 209 LYS A O   
1514 C CB  . LYS A 202 ? 0.96166 0.90432 0.73980 0.13158  -0.00782 -0.04614 209 LYS A CB  
1515 C CG  . LYS A 202 ? 1.00677 0.93349 0.78049 0.13562  -0.03075 -0.08917 209 LYS A CG  
1516 C CD  . LYS A 202 ? 1.01756 0.97397 0.75835 0.13685  -0.04158 -0.08998 209 LYS A CD  
1517 C CE  . LYS A 202 ? 1.06668 1.01602 0.80767 0.14265  -0.07068 -0.13883 209 LYS A CE  
1518 N NZ  . LYS A 202 ? 1.03227 1.01647 0.73357 0.15242  -0.08375 -0.13946 209 LYS A NZ  
1519 N N   . HIS A 203 ? 0.92440 0.79314 0.79012 0.09489  -0.00629 -0.01567 210 HIS A N   
1520 C CA  . HIS A 203 ? 0.95081 0.78150 0.85263 0.07674  -0.00999 -0.01358 210 HIS A CA  
1521 C C   . HIS A 203 ? 0.89708 0.70533 0.81745 0.07873  0.00260  0.01613  210 HIS A C   
1522 O O   . HIS A 203 ? 0.92231 0.68996 0.87498 0.07123  0.00569  0.01906  210 HIS A O   
1523 C CB  . HIS A 203 ? 0.95431 0.79910 0.86007 0.05377  -0.01559 -0.00366 210 HIS A CB  
1524 C CG  . HIS A 203 ? 1.06401 0.92791 0.95511 0.05356  -0.03156 -0.03152 210 HIS A CG  
1525 N ND1 . HIS A 203 ? 1.03573 0.88218 0.94911 0.05152  -0.04769 -0.06918 210 HIS A ND1 
1526 C CD2 . HIS A 203 ? 0.99272 0.89239 0.85059 0.05751  -0.03509 -0.02691 210 HIS A CD2 
1527 C CE1 . HIS A 203 ? 1.00831 0.88430 0.89636 0.05729  -0.06350 -0.08857 210 HIS A CE1 
1528 N NE2 . HIS A 203 ? 0.97157 0.87786 0.82323 0.06192  -0.05418 -0.05975 210 HIS A NE2 
1529 N N   . SER A 204 ? 1.05843 0.63061 0.69793 0.03465  -0.20338 -0.05770 211 SER A N   
1530 C CA  . SER A 204 ? 1.06523 0.66796 0.75847 0.03629  -0.17140 -0.05152 211 SER A CA  
1531 C C   . SER A 204 ? 1.08498 0.67658 0.72494 0.06911  -0.13223 -0.05447 211 SER A C   
1532 O O   . SER A 204 ? 1.05296 0.69494 0.73501 0.07621  -0.09849 -0.04216 211 SER A O   
1533 C CB  . SER A 204 ? 0.95440 0.63517 0.73665 0.02520  -0.15552 -0.03227 211 SER A CB  
1534 O OG  . SER A 204 ? 0.95648 0.65240 0.79492 -0.00084 -0.18704 -0.02503 211 SER A OG  
1535 N N   . GLN A 205 ? 1.19349 0.72066 0.73926 0.09066  -0.13615 -0.06980 212 GLN A N   
1536 C CA  . GLN A 205 ? 1.31862 0.83727 0.81313 0.12722  -0.09597 -0.06833 212 GLN A CA  
1537 C C   . GLN A 205 ? 1.28710 0.78408 0.79366 0.13311  -0.07930 -0.07154 212 GLN A C   
1538 O O   . GLN A 205 ? 1.31553 0.81996 0.79732 0.16378  -0.04177 -0.06388 212 GLN A O   
1539 C CB  . GLN A 205 ? 1.35336 0.80718 0.73598 0.15471  -0.10132 -0.08327 212 GLN A CB  
1540 C CG  . GLN A 205 ? 1.46191 0.83443 0.79207 0.13798  -0.14974 -0.10981 212 GLN A CG  
1541 C CD  . GLN A 205 ? 1.73338 1.02613 0.93644 0.17168  -0.14938 -0.13101 212 GLN A CD  
1542 O OE1 . GLN A 205 ? 1.85892 1.15617 1.01597 0.21181  -0.10757 -0.12361 212 GLN A OE1 
1543 N NE2 . GLN A 205 ? 1.78296 1.00326 0.92722 0.15615  -0.19637 -0.15665 212 GLN A NE2 
1544 N N   . PHE A 206 ? 1.36199 0.83701 0.91043 0.10544  -0.10502 -0.07795 213 PHE A N   
1545 C CA  . PHE A 206 ? 1.24953 0.69656 0.80931 0.11001  -0.09197 -0.07863 213 PHE A CA  
1546 C C   . PHE A 206 ? 1.15292 0.66631 0.81616 0.08625  -0.08641 -0.05988 213 PHE A C   
1547 O O   . PHE A 206 ? 1.11975 0.60805 0.81185 0.07370  -0.09448 -0.05883 213 PHE A O   
1548 C CB  . PHE A 206 ? 1.33722 0.68226 0.84299 0.10105  -0.12671 -0.10272 213 PHE A CB  
1549 C CG  . PHE A 206 ? 1.41394 0.68309 0.80325 0.12888  -0.13070 -0.12549 213 PHE A CG  
1550 C CD1 . PHE A 206 ? 1.44609 0.72132 0.78108 0.17337  -0.08720 -0.12022 213 PHE A CD1 
1551 C CD2 . PHE A 206 ? 1.50531 0.70010 0.83815 0.11137  -0.17821 -0.15050 213 PHE A CD2 
1552 C CE1 . PHE A 206 ? 1.56006 0.76688 0.78308 0.20431  -0.08653 -0.13952 213 PHE A CE1 
1553 C CE2 . PHE A 206 ? 1.58935 0.71158 0.80425 0.13973  -0.18154 -0.17383 213 PHE A CE2 
1554 C CZ  . PHE A 206 ? 1.57631 0.70372 0.73446 0.18850  -0.13339 -0.16836 213 PHE A CZ  
1555 N N   . ILE A 207 ? 1.03746 0.63287 0.75488 0.08073  -0.07203 -0.04457 214 ILE A N   
1556 C CA  . ILE A 207 ? 0.89160 0.55301 0.69676 0.06400  -0.06170 -0.02825 214 ILE A CA  
1557 C C   . ILE A 207 ? 0.83703 0.53462 0.64784 0.08649  -0.02117 -0.01561 214 ILE A C   
1558 O O   . ILE A 207 ? 0.87697 0.59578 0.65602 0.10859  0.00275  -0.01146 214 ILE A O   
1559 C CB  . ILE A 207 ? 0.83261 0.55584 0.68706 0.04845  -0.06623 -0.02112 214 ILE A CB  
1560 C CG1 . ILE A 207 ? 0.82484 0.52178 0.68735 0.02539  -0.10748 -0.02701 214 ILE A CG1 
1561 C CG2 . ILE A 207 ? 0.69730 0.48891 0.62779 0.03914  -0.04774 -0.00683 214 ILE A CG2 
1562 C CD1 . ILE A 207 ? 0.76196 0.45311 0.68016 0.00083  -0.12930 -0.02139 214 ILE A CD1 
1563 N N   . GLY A 208 ? 0.78679 0.49675 0.64146 0.08084  -0.01367 -0.00532 215 GLY A N   
1564 C CA  . GLY A 208 ? 0.76696 0.51003 0.62664 0.10258  0.02190  0.00971  215 GLY A CA  
1565 C C   . GLY A 208 ? 0.71487 0.55075 0.62379 0.09956  0.04315  0.02393  215 GLY A C   
1566 O O   . GLY A 208 ? 0.66180 0.53939 0.59765 0.10727  0.06515  0.03978  215 GLY A O   
1567 N N   . TYR A 209 ? 0.65131 0.51785 0.57031 0.08824  0.03583  0.01855  216 TYR A N   
1568 C CA  . TYR A 209 ? 0.60032 0.54395 0.55867 0.08279  0.05239  0.02690  216 TYR A CA  
1569 C C   . TYR A 209 ? 0.58860 0.54148 0.52492 0.08394  0.05190  0.02258  216 TYR A C   
1570 O O   . TYR A 209 ? 0.59176 0.50102 0.49987 0.08170  0.03292  0.01300  216 TYR A O   
1571 C CB  . TYR A 209 ? 0.59311 0.56937 0.61238 0.06041  0.04283  0.02729  216 TYR A CB  
1572 C CG  . TYR A 209 ? 0.52808 0.50333 0.57690 0.05858  0.04494  0.03776  216 TYR A CG  
1573 C CD1 . TYR A 209 ? 0.50272 0.52704 0.56967 0.06800  0.06914  0.05237  216 TYR A CD1 
1574 C CD2 . TYR A 209 ? 0.55186 0.48004 0.61291 0.04611  0.02134  0.03628  216 TYR A CD2 
1575 C CE1 . TYR A 209 ? 0.51729 0.54327 0.61354 0.06783  0.07310  0.06686  216 TYR A CE1 
1576 C CE2 . TYR A 209 ? 0.52854 0.45650 0.62313 0.04272  0.02364  0.05062  216 TYR A CE2 
1577 C CZ  . TYR A 209 ? 0.49554 0.47219 0.60748 0.05503  0.05125  0.06670  216 TYR A CZ  
1578 O OH  . TYR A 209 ? 0.50722 0.48636 0.65471 0.05312  0.05554  0.08564  216 TYR A OH  
1579 N N   . PRO A 210 ? 0.55193 0.56251 0.50127 0.08624  0.07113  0.03168  217 PRO A N   
1580 C CA  . PRO A 210 ? 0.54777 0.56838 0.48216 0.08591  0.07181  0.03261  217 PRO A CA  
1581 C C   . PRO A 210 ? 0.51557 0.53008 0.47608 0.06483  0.05179  0.02225  217 PRO A C   
1582 O O   . PRO A 210 ? 0.49829 0.53961 0.50369 0.04886  0.04914  0.01809  217 PRO A O   
1583 C CB  . PRO A 210 ? 0.53708 0.62589 0.49345 0.08574  0.09291  0.04629  217 PRO A CB  
1584 C CG  . PRO A 210 ? 0.50111 0.62026 0.48687 0.08271  0.09992  0.04894  217 PRO A CG  
1585 C CD  . PRO A 210 ? 0.55508 0.62335 0.53073 0.08928  0.09160  0.04424  217 PRO A CD  
1586 N N   . ILE A 211 ? 0.54009 0.51920 0.46966 0.06804  0.03921  0.01970  218 ILE A N   
1587 C CA  . ILE A 211 ? 0.55833 0.53296 0.51034 0.05225  0.02196  0.01540  218 ILE A CA  
1588 C C   . ILE A 211 ? 0.55044 0.55058 0.50045 0.05297  0.03331  0.02545  218 ILE A C   
1589 O O   . ILE A 211 ? 0.60393 0.59251 0.51093 0.06920  0.03978  0.03461  218 ILE A O   
1590 C CB  . ILE A 211 ? 0.58820 0.50849 0.51001 0.05305  -0.00437 0.00895  218 ILE A CB  
1591 C CG1 . ILE A 211 ? 0.60194 0.49274 0.52552 0.04983  -0.01720 0.00153  218 ILE A CG1 
1592 C CG2 . ILE A 211 ? 0.55740 0.48152 0.51184 0.03793  -0.02152 0.00970  218 ILE A CG2 
1593 C CD1 . ILE A 211 ? 0.65059 0.48207 0.53440 0.04871  -0.04707 -0.00673 218 ILE A CD1 
1594 N N   . THR A 212 ? 0.49070 0.52334 0.48612 0.03620  0.03656  0.02463  219 THR A N   
1595 C CA  . THR A 212 ? 0.51177 0.56893 0.51615 0.03076  0.04597  0.03517  219 THR A CA  
1596 C C   . THR A 212 ? 0.46536 0.50455 0.49105 0.01979  0.03270  0.03398  219 THR A C   
1597 O O   . THR A 212 ? 0.46735 0.50409 0.52811 0.00863  0.02561  0.02304  219 THR A O   
1598 C CB  . THR A 212 ? 0.46853 0.57307 0.50460 0.01827  0.05938  0.03432  219 THR A CB  
1599 O OG1 . THR A 212 ? 0.45118 0.57752 0.47118 0.03060  0.07187  0.03984  219 THR A OG1 
1600 C CG2 . THR A 212 ? 0.51251 0.64056 0.56073 0.00826  0.06593  0.04742  219 THR A CG2 
1601 N N   . LEU A 213 ? 0.52228 0.55128 0.52753 0.02593  0.03185  0.04845  220 LEU A N   
1602 C CA  . LEU A 213 ? 0.53402 0.54911 0.56088 0.01773  0.02188  0.05372  220 LEU A CA  
1603 C C   . LEU A 213 ? 0.51120 0.55090 0.57399 0.00226  0.03390  0.06045  220 LEU A C   
1604 O O   . LEU A 213 ? 0.48661 0.55028 0.54086 0.00338  0.04654  0.07614  220 LEU A O   
1605 C CB  . LEU A 213 ? 0.55113 0.54305 0.53541 0.03290  0.01384  0.06871  220 LEU A CB  
1606 C CG  . LEU A 213 ? 0.63273 0.61393 0.63737 0.02783  0.00456  0.08159  220 LEU A CG  
1607 C CD1 . LEU A 213 ? 0.56501 0.53561 0.61376 0.01624  -0.00900 0.06967  220 LEU A CD1 
1608 C CD2 . LEU A 213 ? 0.68802 0.64809 0.64024 0.04543  -0.00621 0.09540  220 LEU A CD2 
1609 N N   . PHE A 214 ? 0.46789 0.50046 0.57135 -0.01196 0.03001  0.04962  221 PHE A N   
1610 C CA  . PHE A 214 ? 0.49399 0.53622 0.63010 -0.02990 0.03770  0.05065  221 PHE A CA  
1611 C C   . PHE A 214 ? 0.51316 0.53690 0.65769 -0.02997 0.03500  0.07180  221 PHE A C   
1612 O O   . PHE A 214 ? 0.52334 0.52070 0.68140 -0.02608 0.02621  0.07221  221 PHE A O   
1613 C CB  . PHE A 214 ? 0.49993 0.53460 0.66747 -0.04084 0.03751  0.02671  221 PHE A CB  
1614 C CG  . PHE A 214 ? 0.50620 0.56977 0.67066 -0.04630 0.04418  0.01007  221 PHE A CG  
1615 C CD1 . PHE A 214 ? 0.53341 0.61513 0.67308 -0.03408 0.04562  0.01172  221 PHE A CD1 
1616 C CD2 . PHE A 214 ? 0.61612 0.68577 0.79940 -0.06303 0.04845  -0.00723 221 PHE A CD2 
1617 C CE1 . PHE A 214 ? 0.51885 0.63118 0.65778 -0.03734 0.05258  0.00114  221 PHE A CE1 
1618 C CE2 . PHE A 214 ? 0.59170 0.69276 0.76823 -0.06729 0.05317  -0.02081 221 PHE A CE2 
1619 C CZ  . PHE A 214 ? 0.48712 0.61306 0.64406 -0.05386 0.05593  -0.01425 221 PHE A CZ  
1620 N N   . VAL A 215 ? 0.51318 0.55556 0.65364 -0.03331 0.04345  0.09391  222 VAL A N   
1621 C CA  . VAL A 215 ? 0.54185 0.57205 0.69328 -0.03351 0.04365  0.12016  222 VAL A CA  
1622 C C   . VAL A 215 ? 0.55214 0.56478 0.75224 -0.05629 0.04402  0.11434  222 VAL A C   
1623 O O   . VAL A 215 ? 0.54215 0.56679 0.76124 -0.07648 0.04747  0.10032  222 VAL A O   
1624 C CB  . VAL A 215 ? 0.56246 0.62404 0.69533 -0.02721 0.05552  0.15109  222 VAL A CB  
1625 C CG1 . VAL A 215 ? 0.59169 0.64445 0.73706 -0.02587 0.05742  0.18368  222 VAL A CG1 
1626 C CG2 . VAL A 215 ? 0.60095 0.67013 0.67724 -0.00059 0.05787  0.15207  222 VAL A CG2 
1627 N N   . GLU A 216 ? 0.55227 0.53382 0.77041 -0.05270 0.03958  0.12484  223 GLU A N   
1628 C CA  . GLU A 216 ? 0.57795 0.53023 0.83977 -0.07062 0.04154  0.11960  223 GLU A CA  
1629 C C   . GLU A 216 ? 0.57159 0.53333 0.85524 -0.08972 0.04779  0.14492  223 GLU A C   
1630 O O   . GLU A 216 ? 0.57671 0.56615 0.84593 -0.08205 0.05236  0.17704  223 GLU A O   
1631 C CB  . GLU A 216 ? 0.60774 0.52536 0.88609 -0.05714 0.03684  0.12831  223 GLU A CB  
1632 C CG  . GLU A 216 ? 0.59591 0.50974 0.86323 -0.04045 0.02863  0.11011  223 GLU A CG  
1633 C CD  . GLU A 216 ? 0.62380 0.50588 0.92439 -0.03151 0.02686  0.11444  223 GLU A CD  
1634 O OE1 . GLU A 216 ? 0.62803 0.48186 0.95864 -0.03999 0.03584  0.09904  223 GLU A OE1 
1635 O OE2 . GLU A 216 ? 0.68011 0.56473 0.97514 -0.01511 0.01618  0.13354  223 GLU A OE2 
1636 N N   . LYS A 217 ? 0.61805 0.55511 0.93611 -0.11462 0.04808  0.13089  224 LYS A N   
1637 C CA  . LYS A 217 ? 0.69586 0.63856 1.04434 -0.14048 0.05036  0.15394  224 LYS A CA  
1638 C C   . LYS A 217 ? 0.73412 0.62937 1.11829 -0.14438 0.05187  0.17338  224 LYS A C   
1639 O O   . LYS A 217 ? 0.85896 0.75974 1.24356 -0.12784 0.05571  0.21070  224 LYS A O   
1640 C CB  . LYS A 217 ? 0.67141 0.61775 1.03182 -0.17182 0.04531  0.12484  224 LYS A CB  
1641 C CG  . LYS A 217 ? 0.62440 0.61607 0.95284 -0.16663 0.04439  0.10459  224 LYS A CG  
1642 C CD  . LYS A 217 ? 0.59680 0.58522 0.93140 -0.19477 0.03673  0.06955  224 LYS A CD  
1643 C CE  . LYS A 217 ? 0.62759 0.54907 0.96949 -0.19824 0.03473  0.03529  224 LYS A CE  
1644 N NZ  . LYS A 217 ? 0.62393 0.53717 0.94032 -0.16934 0.03964  0.01051  224 LYS A NZ  
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