data_9BR0
# 
_entry.id   9BR0 
# 
_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   9BR0         pdb_00009br0 10.2210/pdb9br0/pdb 
WWPDB D_1000284004 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_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.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BR0 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wliu@chem.tamu.edu 
_pdbx_contact_author.name_first         Wenshe 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7078-6534 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Blankenship, L.R.' 1 0000-0002-1714-4399 
'Liu, W.R.'         2 0000-0002-7078-6534 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of the SARS-CoV-2 main protease' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Blankenship, L.R.' 1 ? 
primary 'Liu, W.R.'         2 ? 
# 
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 '3C-like proteinase nsp5' 33825.547 1 3.4.22.69 ? ? ? 
2 non-polymer syn 
'O-tert-butyl-N-(trifluoroacetyl)-L-threonyl-3-cyclohexyl-N-{(2R)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide' 
561.637   1 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        
'O-tert-butyl-N-(trifluoroacetyl)-L-threonyl-3-cyclohexyl-N-{(2R)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide' 
_pdbx_entity_nonpoly.comp_id     A1ARU 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1ARU non-polymer         . 
'O-tert-butyl-N-(trifluoroacetyl)-L-threonyl-3-cyclohexyl-N-{(2R)-1-imino-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide' 
? 'C26 H42 F3 N5 O5' 561.637 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'     121.158 
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 
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU ALA A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ARU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARU 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          A1ARU 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     401 
_pdbx_nonpoly_scheme.auth_seq_num    401 
_pdbx_nonpoly_scheme.pdb_mon_id      A1ARU 
_pdbx_nonpoly_scheme.auth_mon_id     r84 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLU 178 ? CG  ? A GLU 178 CG  
2 1 Y 1 A GLU 178 ? CD  ? A GLU 178 CD  
3 1 Y 1 A GLU 178 ? OE1 ? A GLU 178 OE1 
4 1 Y 1 A GLU 178 ? OE2 ? A GLU 178 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? 1.18.2_3874 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT    ? ? ? .           2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.950 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BR0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.242 
_cell.length_a_esd                 ? 
_cell.length_b                     81.708 
_cell.length_b_esd                 ? 
_cell.length_c                     86.822 
_cell.length_c_esd                 ? 
_cell.volume                       382721.422 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BR0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y (x,y,-x+z)' 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BR0 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M Ammonium phosphate dibasic, 17%
W/v PEG3350, pH8.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     120 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'Bruker PHOTON II' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54301 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-002' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54301 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          27.94 
_reflns.entry_id                                       9BR0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_reflns.d_resolution_low                               24.37 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     13059 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.39 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.41 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1431 
_reflns.pdbx_Rpim_I_all                                0.04101 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1366 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.5 
_reflns_shell.d_res_low                                     2.589 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.85 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1301 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.5457 
_reflns_shell.pdbx_Rpim_I_all                               0.1831 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.938 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.5122 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.14 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BR0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             24.37 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     13052 
_refine.ls_number_reflns_R_free                  632 
_refine.ls_number_reflns_R_work                  12420 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.51 
_refine.ls_percent_reflns_R_free                 4.84 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2377 
_refine.ls_R_factor_R_free                       0.2780 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2356 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.3737 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3823 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        24.37 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2402 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2363 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0107  ? 2456 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.3203  ? 3341 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0588  ? 379  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0096  ? 431  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.8691 ? 355  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.50 2.69  . . 120 2486 99.73 . . . . 0.2929 . . . . . . . . . . . 0.3493 
'X-RAY DIFFRACTION' 2.69 2.96  . . 138 2448 99.54 . . . . 0.3243 . . . . . . . . . . . 0.3263 
'X-RAY DIFFRACTION' 2.96 3.39  . . 120 2490 99.62 . . . . 0.2803 . . . . . . . . . . . 0.3516 
'X-RAY DIFFRACTION' 3.39 4.27  . . 136 2471 99.31 . . . . 0.2161 . . . . . . . . . . . 0.2856 
'X-RAY DIFFRACTION' 4.27 24.37 . . 118 2525 99.36 . . . . 0.1694 . . . . . . . . . . . 0.1844 
# 
_struct.entry_id                     9BR0 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor YR-B-84' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BR0 
_struct_keywords.text            'main protease, VIRAL PROTEIN, Hydrolase' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BR0 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3280  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  24680 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,y,-z -1.0000000000 0.0000000000 0.0000000000 -54.2420000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ARU 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C5 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ARU 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.816 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ARU 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ARU 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C5 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1ARU 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 18  O GLY A 29  ? O GLY A 29  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BR0 
_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   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              56 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              56 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              56 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                123.93 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.63 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 5   ? ? -64.07  98.73   
2 1 ASP A 33  ? ? 49.97   -122.87 
3 1 ASN A 84  ? ? 58.93   -117.34 
4 1 TYR A 154 ? ? 52.33   -85.79  
5 1 THR A 169 ? ? -68.64  4.95    
6 1 SER A 301 ? ? -130.33 -32.14  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    GLN 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     110 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.101 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -14.0608561234 
_pdbx_refine_tls.origin_y         -15.4499938655 
_pdbx_refine_tls.origin_z         -0.520947221269 
_pdbx_refine_tls.T[1][1]          0.168975696636 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0100736945137 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0209636233061 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.168158372272 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0271348786021 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.142067002594 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.13087974965 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.437961042388 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.347012282888 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.39202409333 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.533251530929 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.30692849416 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0118969818699 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0535984543222 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.137270586366 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.051867528284 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0042197175794 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0276462882 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0507014391848 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0486135780712 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0297622179344 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   B 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     401 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 
A1ARU N    N N N 1   
A1ARU C    C N S 2   
A1ARU O    O N N 3   
A1ARU C1   C N N 4   
A1ARU C10  C N N 5   
A1ARU C11  C N N 6   
A1ARU C12  C N N 7   
A1ARU C13  C N R 8   
A1ARU C14  C N N 9   
A1ARU C15  C N N 10  
A1ARU C16  C N N 11  
A1ARU C17  C N N 12  
A1ARU C18  C N N 13  
A1ARU C19  C N N 14  
A1ARU C2   C N S 15  
A1ARU C20  C N N 16  
A1ARU C21  C N N 17  
A1ARU C22  C N N 18  
A1ARU C23  C N N 19  
A1ARU C24  C N N 20  
A1ARU C25  C N N 21  
A1ARU C3   C N N 22  
A1ARU C4   C N S 23  
A1ARU C5   C N N 24  
A1ARU C6   C N N 25  
A1ARU C7   C N S 26  
A1ARU C8   C N N 27  
A1ARU C9   C N N 28  
A1ARU F17  F N N 29  
A1ARU F18  F N N 30  
A1ARU F19  F N N 31  
A1ARU N1   N N N 32  
A1ARU N2   N N N 33  
A1ARU N3   N N N 34  
A1ARU N4   N N N 35  
A1ARU O1   O N N 36  
A1ARU O3   O N N 37  
A1ARU O4   O N N 38  
A1ARU O6   O N N 39  
A1ARU HN   H N N 40  
A1ARU H0   H N N 41  
A1ARU H111 H N N 42  
A1ARU H112 H N N 43  
A1ARU H12  H N N 44  
A1ARU H13  H N N 45  
A1ARU H142 H N N 46  
A1ARU H141 H N N 47  
A1ARU H143 H N N 48  
A1ARU H181 H N N 49  
A1ARU H183 H N N 50  
A1ARU H182 H N N 51  
A1ARU H191 H N N 52  
A1ARU H192 H N N 53  
A1ARU H193 H N N 54  
A1ARU H2   H N N 55  
A1ARU H201 H N N 56  
A1ARU H203 H N N 57  
A1ARU H202 H N N 58  
A1ARU H212 H N N 59  
A1ARU H211 H N N 60  
A1ARU H221 H N N 61  
A1ARU H222 H N N 62  
A1ARU H231 H N N 63  
A1ARU H232 H N N 64  
A1ARU H241 H N N 65  
A1ARU H242 H N N 66  
A1ARU H251 H N N 67  
A1ARU H252 H N N 68  
A1ARU H4   H N N 69  
A1ARU H5   H N N 70  
A1ARU H62  H N N 71  
A1ARU H61  H N N 72  
A1ARU H7   H N N 73  
A1ARU H82  H N N 74  
A1ARU H81  H N N 75  
A1ARU H92  H N N 76  
A1ARU H91  H N N 77  
A1ARU HN1  H N N 78  
A1ARU HN2  H N N 79  
A1ARU HN3  H N N 80  
A1ARU HN4  H N N 81  
ALA   N    N N N 82  
ALA   CA   C N S 83  
ALA   C    C N N 84  
ALA   O    O N N 85  
ALA   CB   C N N 86  
ALA   OXT  O N N 87  
ALA   H    H N N 88  
ALA   H2   H N N 89  
ALA   HA   H N N 90  
ALA   HB1  H N N 91  
ALA   HB2  H N N 92  
ALA   HB3  H N N 93  
ALA   HXT  H N N 94  
ARG   N    N N N 95  
ARG   CA   C N S 96  
ARG   C    C N N 97  
ARG   O    O N N 98  
ARG   CB   C N N 99  
ARG   CG   C N N 100 
ARG   CD   C N N 101 
ARG   NE   N N N 102 
ARG   CZ   C N N 103 
ARG   NH1  N N N 104 
ARG   NH2  N N N 105 
ARG   OXT  O N N 106 
ARG   H    H N N 107 
ARG   H2   H N N 108 
ARG   HA   H N N 109 
ARG   HB2  H N N 110 
ARG   HB3  H N N 111 
ARG   HG2  H N N 112 
ARG   HG3  H N N 113 
ARG   HD2  H N N 114 
ARG   HD3  H N N 115 
ARG   HE   H N N 116 
ARG   HH11 H N N 117 
ARG   HH12 H N N 118 
ARG   HH21 H N N 119 
ARG   HH22 H N N 120 
ARG   HXT  H N N 121 
ASN   N    N N N 122 
ASN   CA   C N S 123 
ASN   C    C N N 124 
ASN   O    O N N 125 
ASN   CB   C N N 126 
ASN   CG   C N N 127 
ASN   OD1  O N N 128 
ASN   ND2  N N N 129 
ASN   OXT  O N N 130 
ASN   H    H N N 131 
ASN   H2   H N N 132 
ASN   HA   H N N 133 
ASN   HB2  H N N 134 
ASN   HB3  H N N 135 
ASN   HD21 H N N 136 
ASN   HD22 H N N 137 
ASN   HXT  H N N 138 
ASP   N    N N N 139 
ASP   CA   C N S 140 
ASP   C    C N N 141 
ASP   O    O N N 142 
ASP   CB   C N N 143 
ASP   CG   C N N 144 
ASP   OD1  O N N 145 
ASP   OD2  O N N 146 
ASP   OXT  O N N 147 
ASP   H    H N N 148 
ASP   H2   H N N 149 
ASP   HA   H N N 150 
ASP   HB2  H N N 151 
ASP   HB3  H N N 152 
ASP   HD2  H N N 153 
ASP   HXT  H N N 154 
CYS   N    N N N 155 
CYS   CA   C N R 156 
CYS   C    C N N 157 
CYS   O    O N N 158 
CYS   CB   C N N 159 
CYS   SG   S N N 160 
CYS   OXT  O N N 161 
CYS   H    H N N 162 
CYS   H2   H N N 163 
CYS   HA   H N N 164 
CYS   HB2  H N N 165 
CYS   HB3  H N N 166 
CYS   HG   H N N 167 
CYS   HXT  H N N 168 
GLN   N    N N N 169 
GLN   CA   C N S 170 
GLN   C    C N N 171 
GLN   O    O N N 172 
GLN   CB   C N N 173 
GLN   CG   C N N 174 
GLN   CD   C N N 175 
GLN   OE1  O N N 176 
GLN   NE2  N N N 177 
GLN   OXT  O N N 178 
GLN   H    H N N 179 
GLN   H2   H N N 180 
GLN   HA   H N N 181 
GLN   HB2  H N N 182 
GLN   HB3  H N N 183 
GLN   HG2  H N N 184 
GLN   HG3  H N N 185 
GLN   HE21 H N N 186 
GLN   HE22 H N N 187 
GLN   HXT  H N N 188 
GLU   N    N N N 189 
GLU   CA   C N S 190 
GLU   C    C N N 191 
GLU   O    O N N 192 
GLU   CB   C N N 193 
GLU   CG   C N N 194 
GLU   CD   C N N 195 
GLU   OE1  O N N 196 
GLU   OE2  O N N 197 
GLU   OXT  O N N 198 
GLU   H    H N N 199 
GLU   H2   H N N 200 
GLU   HA   H N N 201 
GLU   HB2  H N N 202 
GLU   HB3  H N N 203 
GLU   HG2  H N N 204 
GLU   HG3  H N N 205 
GLU   HE2  H N N 206 
GLU   HXT  H N N 207 
GLY   N    N N N 208 
GLY   CA   C N N 209 
GLY   C    C N N 210 
GLY   O    O N N 211 
GLY   OXT  O N N 212 
GLY   H    H N N 213 
GLY   H2   H N N 214 
GLY   HA2  H N N 215 
GLY   HA3  H N N 216 
GLY   HXT  H N N 217 
HIS   N    N N N 218 
HIS   CA   C N S 219 
HIS   C    C N N 220 
HIS   O    O N N 221 
HIS   CB   C N N 222 
HIS   CG   C Y N 223 
HIS   ND1  N Y N 224 
HIS   CD2  C Y N 225 
HIS   CE1  C Y N 226 
HIS   NE2  N Y N 227 
HIS   OXT  O N N 228 
HIS   H    H N N 229 
HIS   H2   H N N 230 
HIS   HA   H N N 231 
HIS   HB2  H N N 232 
HIS   HB3  H N N 233 
HIS   HD1  H N N 234 
HIS   HD2  H N N 235 
HIS   HE1  H N N 236 
HIS   HE2  H N N 237 
HIS   HXT  H N N 238 
ILE   N    N N N 239 
ILE   CA   C N S 240 
ILE   C    C N N 241 
ILE   O    O N N 242 
ILE   CB   C N S 243 
ILE   CG1  C N N 244 
ILE   CG2  C N N 245 
ILE   CD1  C N N 246 
ILE   OXT  O N N 247 
ILE   H    H N N 248 
ILE   H2   H N N 249 
ILE   HA   H N N 250 
ILE   HB   H N N 251 
ILE   HG12 H N N 252 
ILE   HG13 H N N 253 
ILE   HG21 H N N 254 
ILE   HG22 H N N 255 
ILE   HG23 H N N 256 
ILE   HD11 H N N 257 
ILE   HD12 H N N 258 
ILE   HD13 H N N 259 
ILE   HXT  H N N 260 
LEU   N    N N N 261 
LEU   CA   C N S 262 
LEU   C    C N N 263 
LEU   O    O N N 264 
LEU   CB   C N N 265 
LEU   CG   C N N 266 
LEU   CD1  C N N 267 
LEU   CD2  C N N 268 
LEU   OXT  O N N 269 
LEU   H    H N N 270 
LEU   H2   H N N 271 
LEU   HA   H N N 272 
LEU   HB2  H N N 273 
LEU   HB3  H N N 274 
LEU   HG   H N N 275 
LEU   HD11 H N N 276 
LEU   HD12 H N N 277 
LEU   HD13 H N N 278 
LEU   HD21 H N N 279 
LEU   HD22 H N N 280 
LEU   HD23 H N N 281 
LEU   HXT  H N N 282 
LYS   N    N N N 283 
LYS   CA   C N S 284 
LYS   C    C N N 285 
LYS   O    O N N 286 
LYS   CB   C N N 287 
LYS   CG   C N N 288 
LYS   CD   C N N 289 
LYS   CE   C N N 290 
LYS   NZ   N N N 291 
LYS   OXT  O N N 292 
LYS   H    H N N 293 
LYS   H2   H N N 294 
LYS   HA   H N N 295 
LYS   HB2  H N N 296 
LYS   HB3  H N N 297 
LYS   HG2  H N N 298 
LYS   HG3  H N N 299 
LYS   HD2  H N N 300 
LYS   HD3  H N N 301 
LYS   HE2  H N N 302 
LYS   HE3  H N N 303 
LYS   HZ1  H N N 304 
LYS   HZ2  H N N 305 
LYS   HZ3  H N N 306 
LYS   HXT  H N N 307 
MET   N    N N N 308 
MET   CA   C N S 309 
MET   C    C N N 310 
MET   O    O N N 311 
MET   CB   C N N 312 
MET   CG   C N N 313 
MET   SD   S N N 314 
MET   CE   C N N 315 
MET   OXT  O N N 316 
MET   H    H N N 317 
MET   H2   H N N 318 
MET   HA   H N N 319 
MET   HB2  H N N 320 
MET   HB3  H N N 321 
MET   HG2  H N N 322 
MET   HG3  H N N 323 
MET   HE1  H N N 324 
MET   HE2  H N N 325 
MET   HE3  H N N 326 
MET   HXT  H N N 327 
PHE   N    N N N 328 
PHE   CA   C N S 329 
PHE   C    C N N 330 
PHE   O    O N N 331 
PHE   CB   C N N 332 
PHE   CG   C Y N 333 
PHE   CD1  C Y N 334 
PHE   CD2  C Y N 335 
PHE   CE1  C Y N 336 
PHE   CE2  C Y N 337 
PHE   CZ   C Y N 338 
PHE   OXT  O N N 339 
PHE   H    H N N 340 
PHE   H2   H N N 341 
PHE   HA   H N N 342 
PHE   HB2  H N N 343 
PHE   HB3  H N N 344 
PHE   HD1  H N N 345 
PHE   HD2  H N N 346 
PHE   HE1  H N N 347 
PHE   HE2  H N N 348 
PHE   HZ   H N N 349 
PHE   HXT  H N N 350 
PRO   N    N N N 351 
PRO   CA   C N S 352 
PRO   C    C N N 353 
PRO   O    O N N 354 
PRO   CB   C N N 355 
PRO   CG   C N N 356 
PRO   CD   C N N 357 
PRO   OXT  O N N 358 
PRO   H    H N N 359 
PRO   HA   H N N 360 
PRO   HB2  H N N 361 
PRO   HB3  H N N 362 
PRO   HG2  H N N 363 
PRO   HG3  H N N 364 
PRO   HD2  H N N 365 
PRO   HD3  H N N 366 
PRO   HXT  H N N 367 
SER   N    N N N 368 
SER   CA   C N S 369 
SER   C    C N N 370 
SER   O    O N N 371 
SER   CB   C N N 372 
SER   OG   O N N 373 
SER   OXT  O N N 374 
SER   H    H N N 375 
SER   H2   H N N 376 
SER   HA   H N N 377 
SER   HB2  H N N 378 
SER   HB3  H N N 379 
SER   HG   H N N 380 
SER   HXT  H N N 381 
THR   N    N N N 382 
THR   CA   C N S 383 
THR   C    C N N 384 
THR   O    O N N 385 
THR   CB   C N R 386 
THR   OG1  O N N 387 
THR   CG2  C N N 388 
THR   OXT  O N N 389 
THR   H    H N N 390 
THR   H2   H N N 391 
THR   HA   H N N 392 
THR   HB   H N N 393 
THR   HG1  H N N 394 
THR   HG21 H N N 395 
THR   HG22 H N N 396 
THR   HG23 H N N 397 
THR   HXT  H N N 398 
TRP   N    N N N 399 
TRP   CA   C N S 400 
TRP   C    C N N 401 
TRP   O    O N N 402 
TRP   CB   C N N 403 
TRP   CG   C Y N 404 
TRP   CD1  C Y N 405 
TRP   CD2  C Y N 406 
TRP   NE1  N Y N 407 
TRP   CE2  C Y N 408 
TRP   CE3  C Y N 409 
TRP   CZ2  C Y N 410 
TRP   CZ3  C Y N 411 
TRP   CH2  C Y N 412 
TRP   OXT  O N N 413 
TRP   H    H N N 414 
TRP   H2   H N N 415 
TRP   HA   H N N 416 
TRP   HB2  H N N 417 
TRP   HB3  H N N 418 
TRP   HD1  H N N 419 
TRP   HE1  H N N 420 
TRP   HE3  H N N 421 
TRP   HZ2  H N N 422 
TRP   HZ3  H N N 423 
TRP   HH2  H N N 424 
TRP   HXT  H N N 425 
TYR   N    N N N 426 
TYR   CA   C N S 427 
TYR   C    C N N 428 
TYR   O    O N N 429 
TYR   CB   C N N 430 
TYR   CG   C Y N 431 
TYR   CD1  C Y N 432 
TYR   CD2  C Y N 433 
TYR   CE1  C Y N 434 
TYR   CE2  C Y N 435 
TYR   CZ   C Y N 436 
TYR   OH   O N N 437 
TYR   OXT  O N N 438 
TYR   H    H N N 439 
TYR   H2   H N N 440 
TYR   HA   H N N 441 
TYR   HB2  H N N 442 
TYR   HB3  H N N 443 
TYR   HD1  H N N 444 
TYR   HD2  H N N 445 
TYR   HE1  H N N 446 
TYR   HE2  H N N 447 
TYR   HH   H N N 448 
TYR   HXT  H N N 449 
VAL   N    N N N 450 
VAL   CA   C N S 451 
VAL   C    C N N 452 
VAL   O    O N N 453 
VAL   CB   C N N 454 
VAL   CG1  C N N 455 
VAL   CG2  C N N 456 
VAL   OXT  O N N 457 
VAL   H    H N N 458 
VAL   H2   H N N 459 
VAL   HA   H N N 460 
VAL   HB   H N N 461 
VAL   HG11 H N N 462 
VAL   HG12 H N N 463 
VAL   HG13 H N N 464 
VAL   HG21 H N N 465 
VAL   HG22 H N N 466 
VAL   HG23 H N N 467 
VAL   HXT  H N N 468 
# 
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 
A1ARU O6  C15  doub N N 1   
A1ARU N3  C15  sing N N 2   
A1ARU C15 C16  sing N N 3   
A1ARU C   N3   sing N N 4   
A1ARU C13 C    sing N N 5   
A1ARU C1  C    sing N N 6   
A1ARU C14 C13  sing N N 7   
A1ARU O4  C13  sing N N 8   
A1ARU C17 O4   sing N N 9   
A1ARU C18 C17  sing N N 10  
A1ARU C19 C17  sing N N 11  
A1ARU C20 C17  sing N N 12  
A1ARU O   C1   doub N N 13  
A1ARU N   C1   sing N N 14  
A1ARU C2  N    sing N N 15  
A1ARU C11 C2   sing N N 16  
A1ARU C3  C2   sing N N 17  
A1ARU C12 C11  sing N N 18  
A1ARU C12 C21  sing N N 19  
A1ARU C25 C12  sing N N 20  
A1ARU C21 C22  sing N N 21  
A1ARU C22 C23  sing N N 22  
A1ARU C23 C24  sing N N 23  
A1ARU C24 C25  sing N N 24  
A1ARU O1  C3   doub N N 25  
A1ARU N1  C3   sing N N 26  
A1ARU C4  N1   sing N N 27  
A1ARU C5  C4   sing N N 28  
A1ARU C6  C4   sing N N 29  
A1ARU N4  C5   doub N N 30  
A1ARU C7  C6   sing N N 31  
A1ARU C7  C10  sing N N 32  
A1ARU C8  C7   sing N N 33  
A1ARU O3  C10  doub N N 34  
A1ARU C10 N2   sing N N 35  
A1ARU C9  C8   sing N N 36  
A1ARU N2  C9   sing N N 37  
A1ARU F17 C16  sing N N 38  
A1ARU F18 C16  sing N N 39  
A1ARU C16 F19  sing N N 40  
A1ARU N   HN   sing N N 41  
A1ARU C   H0   sing N N 42  
A1ARU C11 H111 sing N N 43  
A1ARU C11 H112 sing N N 44  
A1ARU C12 H12  sing N N 45  
A1ARU C13 H13  sing N N 46  
A1ARU C14 H142 sing N N 47  
A1ARU C14 H141 sing N N 48  
A1ARU C14 H143 sing N N 49  
A1ARU C18 H181 sing N N 50  
A1ARU C18 H183 sing N N 51  
A1ARU C18 H182 sing N N 52  
A1ARU C19 H191 sing N N 53  
A1ARU C19 H192 sing N N 54  
A1ARU C19 H193 sing N N 55  
A1ARU C2  H2   sing N N 56  
A1ARU C20 H201 sing N N 57  
A1ARU C20 H203 sing N N 58  
A1ARU C20 H202 sing N N 59  
A1ARU C21 H212 sing N N 60  
A1ARU C21 H211 sing N N 61  
A1ARU C22 H221 sing N N 62  
A1ARU C22 H222 sing N N 63  
A1ARU C23 H231 sing N N 64  
A1ARU C23 H232 sing N N 65  
A1ARU C24 H241 sing N N 66  
A1ARU C24 H242 sing N N 67  
A1ARU C25 H251 sing N N 68  
A1ARU C25 H252 sing N N 69  
A1ARU C4  H4   sing N N 70  
A1ARU C5  H5   sing N N 71  
A1ARU C6  H62  sing N N 72  
A1ARU C6  H61  sing N N 73  
A1ARU C7  H7   sing N N 74  
A1ARU C8  H82  sing N N 75  
A1ARU C8  H81  sing N N 76  
A1ARU C9  H92  sing N N 77  
A1ARU C9  H91  sing N N 78  
A1ARU N1  HN1  sing N N 79  
A1ARU N2  HN2  sing N N 80  
A1ARU N3  HN3  sing N N 81  
A1ARU N4  HN4  sing N N 82  
ALA   N   CA   sing N N 83  
ALA   N   H    sing N N 84  
ALA   N   H2   sing N N 85  
ALA   CA  C    sing N N 86  
ALA   CA  CB   sing N N 87  
ALA   CA  HA   sing N N 88  
ALA   C   O    doub N N 89  
ALA   C   OXT  sing N N 90  
ALA   CB  HB1  sing N N 91  
ALA   CB  HB2  sing N N 92  
ALA   CB  HB3  sing N N 93  
ALA   OXT HXT  sing N N 94  
ARG   N   CA   sing N N 95  
ARG   N   H    sing N N 96  
ARG   N   H2   sing N N 97  
ARG   CA  C    sing N N 98  
ARG   CA  CB   sing N N 99  
ARG   CA  HA   sing N N 100 
ARG   C   O    doub N N 101 
ARG   C   OXT  sing N N 102 
ARG   CB  CG   sing N N 103 
ARG   CB  HB2  sing N N 104 
ARG   CB  HB3  sing N N 105 
ARG   CG  CD   sing N N 106 
ARG   CG  HG2  sing N N 107 
ARG   CG  HG3  sing N N 108 
ARG   CD  NE   sing N N 109 
ARG   CD  HD2  sing N N 110 
ARG   CD  HD3  sing N N 111 
ARG   NE  CZ   sing N N 112 
ARG   NE  HE   sing N N 113 
ARG   CZ  NH1  sing N N 114 
ARG   CZ  NH2  doub N N 115 
ARG   NH1 HH11 sing N N 116 
ARG   NH1 HH12 sing N N 117 
ARG   NH2 HH21 sing N N 118 
ARG   NH2 HH22 sing N N 119 
ARG   OXT HXT  sing N N 120 
ASN   N   CA   sing N N 121 
ASN   N   H    sing N N 122 
ASN   N   H2   sing N N 123 
ASN   CA  C    sing N N 124 
ASN   CA  CB   sing N N 125 
ASN   CA  HA   sing N N 126 
ASN   C   O    doub N N 127 
ASN   C   OXT  sing N N 128 
ASN   CB  CG   sing N N 129 
ASN   CB  HB2  sing N N 130 
ASN   CB  HB3  sing N N 131 
ASN   CG  OD1  doub N N 132 
ASN   CG  ND2  sing N N 133 
ASN   ND2 HD21 sing N N 134 
ASN   ND2 HD22 sing N N 135 
ASN   OXT HXT  sing N N 136 
ASP   N   CA   sing N N 137 
ASP   N   H    sing N N 138 
ASP   N   H2   sing N N 139 
ASP   CA  C    sing N N 140 
ASP   CA  CB   sing N N 141 
ASP   CA  HA   sing N N 142 
ASP   C   O    doub N N 143 
ASP   C   OXT  sing N N 144 
ASP   CB  CG   sing N N 145 
ASP   CB  HB2  sing N N 146 
ASP   CB  HB3  sing N N 147 
ASP   CG  OD1  doub N N 148 
ASP   CG  OD2  sing N N 149 
ASP   OD2 HD2  sing N N 150 
ASP   OXT HXT  sing N N 151 
CYS   N   CA   sing N N 152 
CYS   N   H    sing N N 153 
CYS   N   H2   sing N N 154 
CYS   CA  C    sing N N 155 
CYS   CA  CB   sing N N 156 
CYS   CA  HA   sing N N 157 
CYS   C   O    doub N N 158 
CYS   C   OXT  sing N N 159 
CYS   CB  SG   sing N N 160 
CYS   CB  HB2  sing N N 161 
CYS   CB  HB3  sing N N 162 
CYS   SG  HG   sing N N 163 
CYS   OXT HXT  sing N N 164 
GLN   N   CA   sing N N 165 
GLN   N   H    sing N N 166 
GLN   N   H2   sing N N 167 
GLN   CA  C    sing N N 168 
GLN   CA  CB   sing N N 169 
GLN   CA  HA   sing N N 170 
GLN   C   O    doub N N 171 
GLN   C   OXT  sing N N 172 
GLN   CB  CG   sing N N 173 
GLN   CB  HB2  sing N N 174 
GLN   CB  HB3  sing N N 175 
GLN   CG  CD   sing N N 176 
GLN   CG  HG2  sing N N 177 
GLN   CG  HG3  sing N N 178 
GLN   CD  OE1  doub N N 179 
GLN   CD  NE2  sing N N 180 
GLN   NE2 HE21 sing N N 181 
GLN   NE2 HE22 sing N N 182 
GLN   OXT HXT  sing N N 183 
GLU   N   CA   sing N N 184 
GLU   N   H    sing N N 185 
GLU   N   H2   sing N N 186 
GLU   CA  C    sing N N 187 
GLU   CA  CB   sing N N 188 
GLU   CA  HA   sing N N 189 
GLU   C   O    doub N N 190 
GLU   C   OXT  sing N N 191 
GLU   CB  CG   sing N N 192 
GLU   CB  HB2  sing N N 193 
GLU   CB  HB3  sing N N 194 
GLU   CG  CD   sing N N 195 
GLU   CG  HG2  sing N N 196 
GLU   CG  HG3  sing N N 197 
GLU   CD  OE1  doub N N 198 
GLU   CD  OE2  sing N N 199 
GLU   OE2 HE2  sing N N 200 
GLU   OXT HXT  sing N N 201 
GLY   N   CA   sing N N 202 
GLY   N   H    sing N N 203 
GLY   N   H2   sing N N 204 
GLY   CA  C    sing N N 205 
GLY   CA  HA2  sing N N 206 
GLY   CA  HA3  sing N N 207 
GLY   C   O    doub N N 208 
GLY   C   OXT  sing N N 209 
GLY   OXT HXT  sing N N 210 
HIS   N   CA   sing N N 211 
HIS   N   H    sing N N 212 
HIS   N   H2   sing N N 213 
HIS   CA  C    sing N N 214 
HIS   CA  CB   sing N N 215 
HIS   CA  HA   sing N N 216 
HIS   C   O    doub N N 217 
HIS   C   OXT  sing N N 218 
HIS   CB  CG   sing N N 219 
HIS   CB  HB2  sing N N 220 
HIS   CB  HB3  sing N N 221 
HIS   CG  ND1  sing Y N 222 
HIS   CG  CD2  doub Y N 223 
HIS   ND1 CE1  doub Y N 224 
HIS   ND1 HD1  sing N N 225 
HIS   CD2 NE2  sing Y N 226 
HIS   CD2 HD2  sing N N 227 
HIS   CE1 NE2  sing Y N 228 
HIS   CE1 HE1  sing N N 229 
HIS   NE2 HE2  sing N N 230 
HIS   OXT HXT  sing N N 231 
ILE   N   CA   sing N N 232 
ILE   N   H    sing N N 233 
ILE   N   H2   sing N N 234 
ILE   CA  C    sing N N 235 
ILE   CA  CB   sing N N 236 
ILE   CA  HA   sing N N 237 
ILE   C   O    doub N N 238 
ILE   C   OXT  sing N N 239 
ILE   CB  CG1  sing N N 240 
ILE   CB  CG2  sing N N 241 
ILE   CB  HB   sing N N 242 
ILE   CG1 CD1  sing N N 243 
ILE   CG1 HG12 sing N N 244 
ILE   CG1 HG13 sing N N 245 
ILE   CG2 HG21 sing N N 246 
ILE   CG2 HG22 sing N N 247 
ILE   CG2 HG23 sing N N 248 
ILE   CD1 HD11 sing N N 249 
ILE   CD1 HD12 sing N N 250 
ILE   CD1 HD13 sing N N 251 
ILE   OXT HXT  sing N N 252 
LEU   N   CA   sing N N 253 
LEU   N   H    sing N N 254 
LEU   N   H2   sing N N 255 
LEU   CA  C    sing N N 256 
LEU   CA  CB   sing N N 257 
LEU   CA  HA   sing N N 258 
LEU   C   O    doub N N 259 
LEU   C   OXT  sing N N 260 
LEU   CB  CG   sing N N 261 
LEU   CB  HB2  sing N N 262 
LEU   CB  HB3  sing N N 263 
LEU   CG  CD1  sing N N 264 
LEU   CG  CD2  sing N N 265 
LEU   CG  HG   sing N N 266 
LEU   CD1 HD11 sing N N 267 
LEU   CD1 HD12 sing N N 268 
LEU   CD1 HD13 sing N N 269 
LEU   CD2 HD21 sing N N 270 
LEU   CD2 HD22 sing N N 271 
LEU   CD2 HD23 sing N N 272 
LEU   OXT HXT  sing N N 273 
LYS   N   CA   sing N N 274 
LYS   N   H    sing N N 275 
LYS   N   H2   sing N N 276 
LYS   CA  C    sing N N 277 
LYS   CA  CB   sing N N 278 
LYS   CA  HA   sing N N 279 
LYS   C   O    doub N N 280 
LYS   C   OXT  sing N N 281 
LYS   CB  CG   sing N N 282 
LYS   CB  HB2  sing N N 283 
LYS   CB  HB3  sing N N 284 
LYS   CG  CD   sing N N 285 
LYS   CG  HG2  sing N N 286 
LYS   CG  HG3  sing N N 287 
LYS   CD  CE   sing N N 288 
LYS   CD  HD2  sing N N 289 
LYS   CD  HD3  sing N N 290 
LYS   CE  NZ   sing N N 291 
LYS   CE  HE2  sing N N 292 
LYS   CE  HE3  sing N N 293 
LYS   NZ  HZ1  sing N N 294 
LYS   NZ  HZ2  sing N N 295 
LYS   NZ  HZ3  sing N N 296 
LYS   OXT HXT  sing N N 297 
MET   N   CA   sing N N 298 
MET   N   H    sing N N 299 
MET   N   H2   sing N N 300 
MET   CA  C    sing N N 301 
MET   CA  CB   sing N N 302 
MET   CA  HA   sing N N 303 
MET   C   O    doub N N 304 
MET   C   OXT  sing N N 305 
MET   CB  CG   sing N N 306 
MET   CB  HB2  sing N N 307 
MET   CB  HB3  sing N N 308 
MET   CG  SD   sing N N 309 
MET   CG  HG2  sing N N 310 
MET   CG  HG3  sing N N 311 
MET   SD  CE   sing N N 312 
MET   CE  HE1  sing N N 313 
MET   CE  HE2  sing N N 314 
MET   CE  HE3  sing N N 315 
MET   OXT HXT  sing N N 316 
PHE   N   CA   sing N N 317 
PHE   N   H    sing N N 318 
PHE   N   H2   sing N N 319 
PHE   CA  C    sing N N 320 
PHE   CA  CB   sing N N 321 
PHE   CA  HA   sing N N 322 
PHE   C   O    doub N N 323 
PHE   C   OXT  sing N N 324 
PHE   CB  CG   sing N N 325 
PHE   CB  HB2  sing N N 326 
PHE   CB  HB3  sing N N 327 
PHE   CG  CD1  doub Y N 328 
PHE   CG  CD2  sing Y N 329 
PHE   CD1 CE1  sing Y N 330 
PHE   CD1 HD1  sing N N 331 
PHE   CD2 CE2  doub Y N 332 
PHE   CD2 HD2  sing N N 333 
PHE   CE1 CZ   doub Y N 334 
PHE   CE1 HE1  sing N N 335 
PHE   CE2 CZ   sing Y N 336 
PHE   CE2 HE2  sing N N 337 
PHE   CZ  HZ   sing N N 338 
PHE   OXT HXT  sing N N 339 
PRO   N   CA   sing N N 340 
PRO   N   CD   sing N N 341 
PRO   N   H    sing N N 342 
PRO   CA  C    sing N N 343 
PRO   CA  CB   sing N N 344 
PRO   CA  HA   sing N N 345 
PRO   C   O    doub N N 346 
PRO   C   OXT  sing N N 347 
PRO   CB  CG   sing N N 348 
PRO   CB  HB2  sing N N 349 
PRO   CB  HB3  sing N N 350 
PRO   CG  CD   sing N N 351 
PRO   CG  HG2  sing N N 352 
PRO   CG  HG3  sing N N 353 
PRO   CD  HD2  sing N N 354 
PRO   CD  HD3  sing N N 355 
PRO   OXT HXT  sing N N 356 
SER   N   CA   sing N N 357 
SER   N   H    sing N N 358 
SER   N   H2   sing N N 359 
SER   CA  C    sing N N 360 
SER   CA  CB   sing N N 361 
SER   CA  HA   sing N N 362 
SER   C   O    doub N N 363 
SER   C   OXT  sing N N 364 
SER   CB  OG   sing N N 365 
SER   CB  HB2  sing N N 366 
SER   CB  HB3  sing N N 367 
SER   OG  HG   sing N N 368 
SER   OXT HXT  sing N N 369 
THR   N   CA   sing N N 370 
THR   N   H    sing N N 371 
THR   N   H2   sing N N 372 
THR   CA  C    sing N N 373 
THR   CA  CB   sing N N 374 
THR   CA  HA   sing N N 375 
THR   C   O    doub N N 376 
THR   C   OXT  sing N N 377 
THR   CB  OG1  sing N N 378 
THR   CB  CG2  sing N N 379 
THR   CB  HB   sing N N 380 
THR   OG1 HG1  sing N N 381 
THR   CG2 HG21 sing N N 382 
THR   CG2 HG22 sing N N 383 
THR   CG2 HG23 sing N N 384 
THR   OXT HXT  sing N N 385 
TRP   N   CA   sing N N 386 
TRP   N   H    sing N N 387 
TRP   N   H2   sing N N 388 
TRP   CA  C    sing N N 389 
TRP   CA  CB   sing N N 390 
TRP   CA  HA   sing N N 391 
TRP   C   O    doub N N 392 
TRP   C   OXT  sing N N 393 
TRP   CB  CG   sing N N 394 
TRP   CB  HB2  sing N N 395 
TRP   CB  HB3  sing N N 396 
TRP   CG  CD1  doub Y N 397 
TRP   CG  CD2  sing Y N 398 
TRP   CD1 NE1  sing Y N 399 
TRP   CD1 HD1  sing N N 400 
TRP   CD2 CE2  doub Y N 401 
TRP   CD2 CE3  sing Y N 402 
TRP   NE1 CE2  sing Y N 403 
TRP   NE1 HE1  sing N N 404 
TRP   CE2 CZ2  sing Y N 405 
TRP   CE3 CZ3  doub Y N 406 
TRP   CE3 HE3  sing N N 407 
TRP   CZ2 CH2  doub Y N 408 
TRP   CZ2 HZ2  sing N N 409 
TRP   CZ3 CH2  sing Y N 410 
TRP   CZ3 HZ3  sing N N 411 
TRP   CH2 HH2  sing N N 412 
TRP   OXT HXT  sing N N 413 
TYR   N   CA   sing N N 414 
TYR   N   H    sing N N 415 
TYR   N   H2   sing N N 416 
TYR   CA  C    sing N N 417 
TYR   CA  CB   sing N N 418 
TYR   CA  HA   sing N N 419 
TYR   C   O    doub N N 420 
TYR   C   OXT  sing N N 421 
TYR   CB  CG   sing N N 422 
TYR   CB  HB2  sing N N 423 
TYR   CB  HB3  sing N N 424 
TYR   CG  CD1  doub Y N 425 
TYR   CG  CD2  sing Y N 426 
TYR   CD1 CE1  sing Y N 427 
TYR   CD1 HD1  sing N N 428 
TYR   CD2 CE2  doub Y N 429 
TYR   CD2 HD2  sing N N 430 
TYR   CE1 CZ   doub Y N 431 
TYR   CE1 HE1  sing N N 432 
TYR   CE2 CZ   sing Y N 433 
TYR   CE2 HE2  sing N N 434 
TYR   CZ  OH   sing N N 435 
TYR   OH  HH   sing N N 436 
TYR   OXT HXT  sing N N 437 
VAL   N   CA   sing N N 438 
VAL   N   H    sing N N 439 
VAL   N   H2   sing N N 440 
VAL   CA  C    sing N N 441 
VAL   CA  CB   sing N N 442 
VAL   CA  HA   sing N N 443 
VAL   C   O    doub N N 444 
VAL   C   OXT  sing N N 445 
VAL   CB  CG1  sing N N 446 
VAL   CB  CG2  sing N N 447 
VAL   CB  HB   sing N N 448 
VAL   CG1 HG11 sing N N 449 
VAL   CG1 HG12 sing N N 450 
VAL   CG1 HG13 sing N N 451 
VAL   CG2 HG21 sing N N 452 
VAL   CG2 HG22 sing N N 453 
VAL   CG2 HG23 sing N N 454 
VAL   OXT HXT  sing N N 455 
# 
_pdbx_audit_support.funding_organization   'Welch Foundation' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7JPY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 1 2 1' 
_space_group.name_Hall        'C 2y (x,y,-x+z)' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BR0 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.018436 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001921 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012239 
_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]   0.011580 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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.
;
? 
F ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-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   . SER   A 1 1   ? -34.98643 -19.52745 14.90076  1.000 26.72176  ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -34.67968 -20.83422 14.33956  1.000 29.14965  ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -34.51647 -20.80302 12.81298  1.000 29.46121  ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -34.90273 -19.81987 12.14314  1.000 23.80062  ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -35.76089 -21.83715 14.75879  1.000 27.61847  ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -35.67728 -23.05797 14.04770  1.000 35.35900  ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? -33.90644 -21.88336 12.29964  1.000 31.09849  ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? -33.48780 -22.01331 10.91820  1.000 26.98739  ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? -32.03408 -21.61696 10.72555  1.000 28.97864  ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? -31.43139 -20.93367 11.55285  1.000 33.74653  ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? -31.45959 -22.06478 9.60290   1.000 21.34018  ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? -30.03168 -21.88220 9.34530   1.000 19.88774  ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? -29.78054 -21.77790 7.84444   1.000 25.07480  ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? -30.02566 -22.73868 7.10161   1.000 31.35335  ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? -29.19978 -23.02204 9.94194   1.000 20.14337  ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? -27.74033 -22.64402 10.14036  1.000 26.31843  ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? -26.77457 -22.99129 9.19947   1.000 24.26551  ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? -27.35007 -21.86931 11.22461  1.000 24.02931  ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? -25.43967 -22.61192 9.37016   1.000 23.59775  ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? -26.04313 -21.48174 11.39463  1.000 24.28285  ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? -25.07410 -21.85944 10.46418  1.000 25.91591  ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? -29.26977 -20.62923 7.39564   1.000 19.65354  ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? -29.11636 -20.33698 5.97433   1.000 22.86250  ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? -27.68490 -19.90485 5.64379   1.000 20.48538  ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? -26.98409 -19.30761 6.47246   1.000 18.87814  ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? -30.11304 -19.22914 5.55248   1.000 26.77542  ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? -31.55396 -19.71994 5.30580   1.000 20.55951  ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? -31.69126 -20.20933 3.87142   1.000 22.60829  ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? -33.04584 -20.62892 3.54336   1.000 24.55505  ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? -33.37476 -21.35765 2.47601   1.000 28.01262  ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? -34.64894 -21.71849 2.27026   1.000 21.35580  ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? -32.43189 -21.73629 1.61124   1.000 24.99328  ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? -27.23359 -20.20424 4.42606   1.000 19.90045  ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? -26.00922 -19.54150 3.97361   1.000 21.62329  ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? -26.32676 -18.06215 3.88985   1.000 19.56448  ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? -26.95755 -17.59942 2.93858   1.000 19.68285  ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? -25.48942 -20.08003 2.64763   1.000 17.80636  ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? -25.02877 -21.50620 2.72430   1.000 24.18781  ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? -24.07801 -21.86059 1.62504   1.000 26.73013  ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? -22.64746 -21.66985 2.09463   1.000 26.69250  ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? -22.29947 -22.71439 3.10304   1.000 25.27698  ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? -25.93969 -17.32309 4.92285   1.000 18.69592  ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? -26.36174 -15.93991 5.06484   1.000 20.48642  ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? -25.19796 -15.00788 4.73193   1.000 18.38264  ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? -24.11412 -15.11266 5.31591   1.000 22.36950  ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? -26.89716 -15.68449 6.46844   1.000 16.56724  ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? -27.64089 -14.39008 6.56925   1.000 21.84577  ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? -28.20559 -14.09583 8.24645   1.000 26.57104  ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? -29.39528 -15.43051 8.41775   1.000 22.08175  ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? -25.42097 -14.12574 3.77946   1.000 16.74420  ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? -24.44317 -13.12826 3.39014   1.000 19.37155  ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? -24.69087 -11.82483 4.13394   1.000 20.21334  ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? -25.82147 -11.50235 4.50100   1.000 20.11324  ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? -24.49418 -12.88166 1.88238   1.000 20.37636  ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? -23.61283 -11.08363 4.36128   1.000 22.42899  ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? -23.72872 -9.74167  4.90324   1.000 23.70800  ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? -24.55160 -8.86368  3.96686   1.000 19.29063  ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? -24.51822 -9.03833  2.74329   1.000 15.65394  ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? -22.35123 -9.12812  5.10439   1.000 20.01107  ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? -21.57481 -9.80200  6.14788   1.000 26.39694  ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? -21.77493 -9.50425  7.47475   1.000 36.52912  ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? -20.67458 -10.78646 5.82077   1.000 26.59902  ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? -21.04829 -10.16648 8.45581   1.000 38.23378  ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? -19.96213 -11.44888 6.80788   1.000 27.59631  ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? -20.14751 -11.13448 8.12030   1.000 29.50615  ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? -25.32120 -7.92898  4.51294   1.000 18.05703  ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? -26.01291 -6.98558  3.63698   1.000 16.87787  ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? -24.94876 -6.27764  2.80969   1.000 16.22865  ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? -23.85636 -5.98520  3.29626   1.000 16.00618  ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? -26.73873 -6.04088  4.60628   1.000 17.65613  ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? -26.61372 -6.65894  5.97886   1.000 22.28820  ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? -25.37197 -7.52153  5.92653   1.000 21.13701  ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? -25.25060 -6.07193  1.53171   1.000 16.23797  ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? -24.26457 -5.63061  0.56307   1.000 15.87991  ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? -24.40335 -4.15301  0.19965   1.000 16.63314  ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? -23.74144 -3.69384  -0.73693  1.000 16.78582  ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? -24.36411 -6.50543  -0.69253  1.000 16.26878  ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? -25.55704 -6.25000  -1.40662  1.000 16.16097  ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? -25.27100 -3.40405  0.89675   1.000 21.25463  ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? -25.45114 -1.99044  0.57308   1.000 18.45886  ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? -24.15432 -1.20883  0.59320   1.000 18.49272  ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? -23.83054 -0.48585  -0.35511  1.000 21.77069  ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? -23.36909 -1.36206  1.65975   1.000 18.08050  ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? -22.11961 -0.60466  1.73768   1.000 19.88008  ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? -21.22597 -0.85225  0.51750   1.000 19.49088  ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? -20.58772 0.08871   0.01191   1.000 21.85229  ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? -21.39239 -0.93718  3.04036   1.000 19.31462  ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? -22.17196 -0.49836  4.24118   1.000 20.76612  ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? -21.38871 -0.61111  5.51807   1.000 31.47325  ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? -21.91697 0.37771   6.56282   1.000 39.49539  ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? -23.24219 -0.03293  7.10654   1.000 46.23681  ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? -21.20473 -2.09292  -0.00327  1.000 16.54364  ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? -20.35467 -2.42968  -1.16570  1.000 19.05935  ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? -20.98630 -2.05735  -2.52659  1.000 20.93491  ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? -20.24855 -1.69363  -3.46316  1.000 17.34122  ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? -19.97467 -3.92498  -1.15115  1.000 17.38109  ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? -19.16618 -4.28597  -2.37934  1.000 14.69591  ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? -19.23484 -4.27871  0.12663   1.000 17.20841  ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? -22.32901 -2.15815  -2.67268  1.000 16.83968  ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? -22.99065 -1.77099  -3.92669  1.000 17.45780  ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? -22.62201 -0.34929  -4.34985  1.000 22.06908  ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? -22.42977 -0.07417  -5.54663  1.000 24.61920  ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? -24.52143 -1.88528  -3.81403  1.000 18.08310  ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? -25.11906 -3.32739  -3.63075  1.000 17.51891  ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? -26.55642 -3.31414  -3.09635  1.000 18.23872  ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? -27.38153 -2.52352  -3.59398  1.000 19.25059  ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? -26.87749 -4.10007  -2.17755  1.000 17.91288  ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? -22.54017 0.57520   -3.38836  1.000 18.80873  ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? -22.22114 1.96051   -3.66607  1.000 19.77601  ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? -20.75655 2.22993   -3.94561  1.000 21.62226  ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? -20.34978 3.38317   -4.07430  1.000 21.66892  ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? -19.94486 1.18839   -4.02934  1.000 18.35112  ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? -18.55474 1.31049   -4.43579  1.000 21.27672  ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? -18.29877 0.69011   -5.79427  1.000 23.83326  ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? -17.16415 0.73223   -6.27535  1.000 26.52147  ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? -17.62624 0.65618   -3.41020  1.000 17.29963  ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? -17.94638 1.15044   -1.69387  1.000 18.24945  ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? -19.30608 0.10073   -6.42832  1.000 22.78731  ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? -19.02755 -0.64939  -7.63364  1.000 23.88148  ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? -19.14503 0.27293   -8.83251  1.000 25.86758  ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? -19.99999 1.15881   -8.87515  1.000 25.66315  ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? -19.94895 -1.85519  -7.76742  1.000 22.60757  ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? -19.75806 -2.89968  -6.67656  1.000 19.69780  ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? -18.06632 -3.37305  -6.41997  1.000 24.02424  ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? -17.65291 -4.02424  -8.05939  1.000 24.45519  ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? -18.23688 0.08137   -9.78410  1.000 29.62827  ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? -18.08969 0.95330   -10.93891 1.000 30.47645  ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? -17.62789 0.09017   -12.10389 1.000 30.09277  ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? -17.12434 -1.02339  -11.92062 1.000 26.79735  ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? -17.07815 2.09982   -10.67710 1.000 29.64923  ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? -17.49688 2.95904   -9.47932  1.000 26.01659  ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? -15.70142 1.52648   -10.44262 1.000 23.71301  ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? -17.81905 0.61522   -13.31381 1.000 34.31216  ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? -17.34633 0.00268   -14.54425 1.000 27.58969  ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? -15.98252 0.58161   -14.87388 1.000 28.16849  ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? -15.75132 1.77445   -14.68201 1.000 35.51433  ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? -18.33580 0.29429   -15.67204 1.000 36.94274  ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? -18.29182 -0.65056  -16.86051 1.000 37.44805  ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? -19.23113 -0.20690  -17.99417 1.000 44.61729  ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? -20.01706 -1.00543  -18.51904 1.000 47.16859  ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? -19.13127 1.06787   -18.38765 1.000 52.15117  ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? -15.06843 -0.25919  -15.34783 1.000 31.25431  ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? -13.75457 0.20012   -15.79300 1.000 32.90009  ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? -13.49871 -0.36709  -17.18817 1.000 35.92409  ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? -13.68403 -1.56678  -17.42483 1.000 35.36708  ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? -12.63876 -0.19966  -14.80321 1.000 29.08311  ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? -11.27629 0.03879   -15.39609 1.000 30.45392  ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? -12.77513 0.56996   -13.48287 1.000 31.22272  ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? -13.09172 0.49547   -18.11751 1.000 42.11408  ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? -12.97782 0.11437   -19.52151 1.000 44.16406  ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? -11.65257 0.59971   -20.09329 1.000 45.74793  ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? -11.37893 1.80471   -20.11916 1.000 45.81658  ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? -14.15536 0.66565   -20.33020 1.000 44.28674  ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? -15.38607 0.17978   -19.76568 1.000 44.12845  ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? -14.04988 0.23205   -21.78945 1.000 43.62223  ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? -10.83199 -0.34040  -20.54807 1.000 44.17788  ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? -9.61503  -0.03437  -21.28708 1.000 44.21791  ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? -9.72958  -0.76605  -22.61226 1.000 46.08757  ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? -9.92536  -1.98675  -22.63095 1.000 41.18697  ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? -8.36204  -0.46895  -20.50818 1.000 44.38238  ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? -6.79609  0.41401   -20.86929 1.000 47.32639  ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? -9.65272  -0.01988  -23.71002 1.000 48.75830  ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? -9.76984  -0.63523  -25.02500 1.000 48.96253  ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? -11.05993 -1.42634  -25.18618 1.000 51.53946  ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? -12.16494 -0.92744  -24.95085 1.000 52.78844  ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? -10.91485 -2.68651  -25.58441 1.000 53.79965  ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? -12.02797 -3.58899  -25.85164 1.000 52.93820  ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? -12.50765 -4.33099  -24.60796 1.000 53.48446  ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? -13.41939 -5.16121  -24.70971 1.000 50.66758  ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? -11.60935 -4.60730  -26.92182 1.000 60.17690  ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? -12.76199 -5.27920  -27.44282 1.000 59.86880  ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? -10.62654 -5.64022  -26.32718 1.000 59.31992  ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? -11.92414 -4.04931  -23.44275 1.000 51.00127  ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? -12.08300 -4.87154  -22.24443 1.000 44.16653  ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? -12.83997 -4.08669  -21.17555 1.000 41.83730  ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? -12.33201 -3.08208  -20.66490 1.000 40.15871  ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? -10.71506 -5.30803  -21.73039 1.000 42.04813  ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? -10.07175 -6.11683  -22.72726 1.000 42.18732  ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? -10.85115 -6.07335  -20.41133 1.000 38.16246  ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? -14.04681 -4.54206  -20.83324 1.000 36.27680  ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? -14.83692 -3.92871  -19.77330 1.000 35.09385  ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? -15.02167 -4.90067  -18.60924 1.000 31.16022  ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? -15.46922 -6.03368  -18.79830 1.000 33.85662  ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? -16.20125 -3.47629  -20.29280 1.000 37.35663  ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? -16.02696 -2.47132  -21.30711 1.000 40.67416  ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? -17.01352 -2.90890  -19.15066 1.000 30.10712  ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? -14.70516 -4.44023  -17.40981 1.000 25.78652  ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? -14.83870 -5.21495  -16.18513 1.000 24.52370  ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? -15.11584 -4.25590  -15.03825 1.000 25.10013  ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? -15.08104 -3.03272  -15.19902 1.000 26.25958  ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? -13.59368 -6.09053  -15.94681 1.000 27.21122  ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? -12.22714 -5.37310  -16.01359 1.000 32.39475  ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? -11.81755 -4.60926  -14.74253 1.000 30.67155  ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? -11.13138 -6.35710  -16.44729 1.000 31.58158  ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? -15.38028 -4.82715  -13.87440 1.000 23.83457  ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? -15.79035 -4.06703  -12.70143 1.000 27.85375  ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? -14.60428 -3.48770  -11.95960 1.000 22.70653  ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? -13.51525 -4.05770  -11.96334 1.000 22.16934  ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? -16.57278 -4.96296  -11.73800 1.000 29.05596  ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? -17.84958 -5.43370  -12.34012 1.000 24.95221  ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? -18.74406 -4.63253  -12.55726 1.000 22.80416  ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? -17.93092 -6.72388  -12.66333 1.000 24.56857  ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? -14.83930 -2.36028  -11.28692 1.000 23.90841  ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? -13.86972 -1.82299  -10.35532 1.000 27.65999  ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? -14.50482 -1.49486  -9.02350  1.000 22.56432  ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? -15.72767 -1.39161  -8.89628  1.000 26.94589  ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? -13.65133 -1.32228  -8.01557  1.000 22.79081  ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? -14.07008 -0.90948  -6.67633  1.000 25.88758  ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? -13.55879 0.49683   -6.40856  1.000 24.61078  ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? -12.36182 0.76456   -6.57883  1.000 21.82219  ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? -13.56243 -1.86953  -5.58324  1.000 22.03923  ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? -14.08618 -1.57775  -4.15893  1.000 23.53591  ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? -15.42298 -2.23487  -3.92699  1.000 19.88798  ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? -13.10570 -1.98685  -3.03927  1.000 18.56720  ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? -14.46264 1.37373   -5.94043  1.000 25.90229  ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? -14.21431 2.80911   -5.76508  1.000 26.46855  ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? -14.23756 3.19213   -4.27886  1.000 27.98351  ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? -15.31023 3.30414   -3.66907  1.000 22.54654  ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? -15.25796 3.59739   -6.54802  1.000 25.55946  ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? -15.04291 5.06520   -6.62564  1.000 28.42147  ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? -13.86714 5.74334   -6.44594  1.000 34.48402  ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? -16.03903 6.05530   -6.91895  1.000 30.75163  ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? -14.07365 7.09921   -6.61557  1.000 38.29345  ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? -15.39718 7.31342   -6.90637  1.000 32.04032  ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? -17.40985 5.99688   -7.19609  1.000 32.57857  ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? -16.07775 8.49644   -7.14618  1.000 34.59339  ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? -18.08819 7.17314   -7.43639  1.000 37.15396  ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? -17.42175 8.40984   -7.40874  1.000 40.43596  ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? -13.05353 3.42847   -3.71119  1.000 27.30514  ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? -12.89617 3.82291   -2.31556  1.000 26.65105  ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? -12.15426 5.14716   -2.24160  1.000 32.80205  ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? -11.05121 5.27624   -2.79014  1.000 29.96987  ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? -12.14317 2.76794   -1.52392  1.000 26.90433  ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? -12.91192 1.45346   -1.43411  1.000 29.20414  ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? -12.07948 0.39444   -0.74001  1.000 24.67179  ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? -14.26809 1.67099   -0.74091  1.000 25.53618  ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? -12.76044 6.12056   -1.55127  1.000 32.65504  ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? -12.28280 7.49566   -1.57004  1.000 31.41151  ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? -12.09049 7.90089   -3.02577  1.000 34.40135  ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? -13.03736 7.79334   -3.81594  1.000 31.47324  ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? -11.00999 7.62918   -0.72989  1.000 33.27371  ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? -11.21894 7.15152   0.72624   1.000 36.52725  ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? -12.08248 7.72888   1.42755   1.000 33.90296  ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? -10.54655 6.17708   1.15656   1.000 31.80043  ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? -10.88183 8.32525   -3.41206  1.000 34.33947  ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? -10.63236 8.79648   -4.77413  1.000 35.45200  ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? -9.80017  7.80510   -5.59060  1.000 34.92348  ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? -9.05161  8.21239   -6.48476  1.000 34.00460  ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? -9.97837  10.18746  -4.76900  1.000 35.69416  ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? -8.51832  10.18486  -4.26551  1.000 39.62560  ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? -8.07606  9.18338   -3.64776  1.000 36.92030  ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? -7.81720  11.21393  -4.48338  1.000 37.83175  ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? -9.94014  6.50337   -5.30456  1.000 34.07312  ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? -9.16018  5.43679   -5.93118  1.000 30.47098  ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? -10.10766 4.36740   -6.45816  1.000 28.10959  ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? -11.08915 4.01675   -5.79539  1.000 28.76410  ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? -8.16358  4.81039   -4.93176  1.000 29.33102  ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? -7.37061  3.66934   -5.58149  1.000 26.87817  ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? -7.25937  5.87422   -4.32268  1.000 26.57410  ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? -9.80104  3.82147   -7.63170  1.000 28.58710  ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? -10.58948 2.73896   -8.21356  1.000 26.45636  ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? -9.68820  1.52607   -8.37829  1.000 25.07650  ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? -8.71757  1.55458   -9.14346  1.000 27.77500  ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? -11.23414 3.12741   -9.55421  1.000 23.97333  ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? -11.96104 1.93644   -10.13764 1.000 24.73719  ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? -12.19755 4.25304   -9.34965  1.000 27.24589  ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? -10.01701 0.45985   -7.67230  1.000 25.75226  ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? -9.27236  -0.78002  -7.75929  1.000 23.21882  ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? -9.91814  -1.71069  -8.78640  1.000 23.80433  ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? -11.13615 -1.88149  -8.78699  1.000 27.53608  ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? -9.22794  -1.44189  -6.39034  1.000 19.59523  ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? -8.67096  -0.56273  -5.29794  1.000 20.22455  ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? -9.46398  0.41443   -4.68483  1.000 18.74415  ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? -7.33992  -0.72404  -4.85523  1.000 19.38965  ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? -8.95196  1.20829   -3.65517  1.000 22.88989  ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? -6.80783  0.06939   -3.83002  1.000 17.15769  ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? -7.61002  1.03135   -3.23743  1.000 21.11406  ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? -7.09030  1.81431   -2.23379  1.000 19.97921  ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? -9.10839  -2.30659  -9.64827  1.000 19.40593  ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? -9.62592  -3.28695  -10.59576 1.000 23.35726  ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? -8.49573  -4.23986  -10.94163 1.000 25.65451  ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? -7.32887  -3.96322  -10.64435 1.000 24.72684  ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? -10.20440 -2.59719  -11.84197 1.000 24.49545  ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? -8.95101  -1.93342  -12.99819 1.000 22.64229  ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? -8.81065  -5.40213  -11.53476 1.000 23.48701  ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? -7.74443  -6.32934  -11.92985 1.000 20.39574  ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? -6.88657  -5.74213  -13.03405 1.000 27.23473  ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? -7.38874  -5.14674  -13.99641 1.000 28.34298  ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? -8.50386  -7.56851  -12.41137 1.000 23.87442  ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? -9.90257  -7.44958  -11.79185 1.000 19.61783  ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? -10.14979 -5.96762  -11.79263 1.000 23.41710  ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? -5.57040  -5.91298  -12.89036 1.000 27.16997  ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? -4.67548  -5.29791  -13.85927 1.000 29.60457  ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? -4.84289  -5.89448  -15.25689 1.000 32.01331  ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? -4.44458  -5.24855  -16.23253 1.000 28.98709  ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? -3.21596  -5.38417  -13.37256 1.000 29.79002  ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? -2.55669  -6.76387  -13.43351 1.000 28.92377  ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? -1.12751  -6.72538  -12.91183 1.000 27.70370  ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? -0.51850  -8.05020  -12.89684 1.000 32.52721  ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? 0.78430   -8.28729  -12.76261 1.000 34.80612  ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? 1.64392   -7.28209  -12.63561 1.000 34.69509  ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 1.23319   -9.53760  -12.76855 1.000 33.36934  ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? -5.48482  -7.09420  -15.39350 1.000 30.78811  ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? -5.62679  -7.61159  -16.76506 1.000 33.72233  ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? -6.68036  -6.83721  -17.59927 1.000 33.03846  ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? -7.00284  -7.28529  -18.71477 1.000 35.08659  ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? -5.92514  -9.12388  -16.78317 1.000 34.59078  ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? -7.29417  -9.51026  -16.30065 1.000 35.50796  ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? -7.48870  -10.30651 -15.19094 1.000 33.74772  ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? -8.53271  -9.24337  -16.79300 1.000 37.19212  ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? -8.78645  -10.49676 -15.01003 1.000 34.60865  ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? -9.44337  -9.85903  -15.96512 1.000 31.00577  ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? -7.19207  -5.69511  -17.13157 1.000 34.65852  ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? -8.03299  -4.85641  -17.98560 1.000 35.89637  ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? -7.20402  -4.19887  -19.08580 1.000 36.99830  ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? -7.71741  -3.90599  -20.17566 1.000 37.53162  ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? -8.78131  -3.80352  -17.14273 1.000 33.65309  ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? -7.80369  -2.78240  -16.53969 1.000 34.24522  ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? -9.84431  -3.11337  -17.96792 1.000 34.38259  ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? -5.91296  -3.95816  -18.83062 1.000 35.88429  ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? -5.04061  -3.35982  -19.84166 1.000 39.72624  ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? -4.58113  -4.35893  -20.89177 1.000 40.74720  ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? -3.87907  -3.96720  -21.83193 1.000 45.12058  ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? -3.84283  -2.68506  -19.14263 1.000 38.36697  ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? -2.90156  -3.72201  -18.52748 1.000 37.55103  ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? -4.33577  -1.74796  -18.05297 1.000 33.34931  ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? -1.81702  -3.10767  -17.64696 1.000 35.81930  ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? -4.96777  -5.63207  -20.77300 1.000 41.67649  ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? -4.60288  -6.64142  -21.75720 1.000 52.71929  ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? -5.48680  -6.57214  -22.99100 1.000 69.23820  ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? -6.63328  -6.10470  -22.95232 1.000 67.99651  ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? -4.68818  -8.05864  -21.19156 1.000 55.92538  ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? -3.45123  -8.49263  -19.96749 1.000 58.27665  ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? -4.93308  -7.06041  -24.09427 1.000 81.96328  ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? -5.63857  -7.23765  -25.35035 1.000 90.32452  ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? -5.70481  -8.72949  -25.66351 1.000 94.04293  ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? -5.08335  -9.55269  -24.98621 1.000 91.37683  ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? -4.94067  -6.45390  -26.46689 1.000 94.51163  ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? -3.78488  -7.17657  -26.90661 1.000 101.06310 ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? -4.49658  -5.09277  -25.95055 1.000 87.61872  ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? -6.46831  -9.07741  -26.70438 1.000 99.14173  ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? -6.71484  -10.48576 -27.01474 1.000 101.21860 ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? -5.42305  -11.25255 -27.31177 1.000 101.00134 ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? -5.34734  -12.46213 -27.05504 1.000 98.72569  ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? -7.68937  -10.58603 -28.19197 1.000 100.80532 ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? -8.87613  -9.85178  -27.92898 1.000 92.71164  ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? -4.40087  -10.57258 -27.84147 1.000 102.08432 ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? -3.10855  -11.17654 -28.15672 1.000 101.39493 ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? -2.08176  -10.99629 -27.04453 1.000 103.29815 ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? -1.01579  -11.62338 -27.09207 1.000 99.17449  ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? -2.55194  -10.58038 -29.45241 1.000 102.42507 ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 47  ? -2.42502  -9.06392  -29.41663 1.000 102.56967 ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 47  ? -3.69117  -8.35535  -29.87334 1.000 104.27158 ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 47  ? -4.73439  -9.02660  -30.05137 1.000 100.28793 ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 47  ? -3.64220  -7.11987  -30.04359 1.000 107.42360 ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 48  ? -2.38173  -10.15972 -26.04901 1.000 111.60308 ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 48  ? -1.52100  -9.93219  -24.89549 1.000 109.02302 ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 48  ? -1.81855  -10.85994 -23.72435 1.000 102.77079 ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 48  ? -1.41901  -10.56314 -22.59855 1.000 103.38420 ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 48  ? -1.65857  -8.49299  -24.40100 1.000 102.76268 ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 48  ? -0.77560  -7.52405  -25.15202 1.000 107.39851 ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 48  ? -1.31032  -6.49202  -25.63134 1.000 106.88894 ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 48  ? 0.44990   -7.78463  -25.25071 1.000 102.85993 ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 49  ? -2.47608  -11.98097 -23.94577 1.000 94.38713  ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 49  ? -2.96278  -12.77687 -22.82677 1.000 87.38326  ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 49  ? -2.09449  -13.99624 -22.51145 1.000 87.16388  ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 49  ? -2.25789  -14.61999 -21.45175 1.000 80.16936  ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 49  ? -4.39945  -13.22019 -23.13751 1.000 86.50404  ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 49  ? -5.42236  -12.13287 -23.13076 1.000 89.39170  ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 49  ? -7.08494  -12.63974 -23.61646 1.000 90.86059  ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 49  ? -7.59041  -13.78449 -22.36261 1.000 70.89248  ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 50  ? -1.19397  -14.36983 -23.41208 1.000 97.47202  ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 50  ? -0.44408  -15.60181 -23.20521 1.000 99.20044  ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 50  ? 0.61493   -15.42967 -22.12501 1.000 92.39112  ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 50  ? 0.63128   -16.19292 -21.15165 1.000 86.89115  ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 50  ? 0.16325   -16.09740 -24.52030 1.000 98.38163  ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 50  ? -0.79114  -15.92216 -25.69781 1.000 104.86899 ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 50  ? -0.13489  -16.23243 -27.04347 1.000 109.36357 ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 50  ? -2.07486  -16.74892 -25.51156 1.000 103.00653 ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 51  ? 1.47875   -14.41812 -22.22415 1.000 80.78730  ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 51  ? 2.43934   -14.17590 -21.15265 1.000 71.20041  ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 51  ? 2.57064   -12.66829 -20.91273 1.000 65.82586  ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 51  ? 3.66204   -12.10863 -21.01673 1.000 60.13989  ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 51  ? 3.80812   -14.74355 -21.51302 1.000 70.13141  ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 51  ? 4.58359   -15.14188 -20.28063 1.000 69.23196  ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 51  ? 3.98915   -15.35239 -19.26537 1.000 71.82262  ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 51  ? 5.85378   -14.94519 -20.28766 1.000 78.05690  ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 52  ? 1.50335   -11.98978 -20.51002 1.000 66.54440  ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 52  ? 1.52520   -10.52290 -20.53080 1.000 57.29445  ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 52  ? 2.60800   -9.96053  -19.61872 1.000 50.62604  ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 52  ? 2.86701   -10.48441 -18.53262 1.000 51.01430  ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 52  ? 0.11670   -10.14124 -20.05866 1.000 56.18170  ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 52  ? -0.39162  -11.30126 -19.31094 1.000 57.22529  ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 52  ? 0.29700   -12.52629 -19.86710 1.000 63.06449  ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 53  ? 3.25300   -8.89769  -20.08786 1.000 47.36903  ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 53  ? 4.20156   -8.12731  -19.29227 1.000 50.98073  ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 53  ? 3.48751   -6.83303  -18.92951 1.000 54.09562  ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 53  ? 3.48601   -5.87232  -19.70669 1.000 54.36213  ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 53  ? 5.50210   -7.85551  -20.04566 1.000 56.65032  ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 53  ? 6.61239   -7.34560  -19.13489 1.000 57.17938  ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 53  ? 6.44810   -6.36364  -18.40573 1.000 57.23472  ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 53  ? 7.75203   -8.01713  -19.17797 1.000 53.01063  ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 54  ? 2.87170   -6.81237  -17.74836 1.000 52.92241  ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 54  ? 2.03130   -5.67702  -17.39229 1.000 49.22781  ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 54  ? 2.83061   -4.39270  -17.22687 1.000 46.68613  ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 54  ? 2.27208   -3.29969  -17.38223 1.000 44.82668  ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 54  ? 1.26127   -5.98995  -16.11920 1.000 43.07441  ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 54  ? 0.23554   -7.07528  -16.32460 1.000 41.15405  ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 54  ? -1.01165  -6.78601  -16.87145 1.000 35.19406  ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 54  ? 0.51968   -8.39875  -15.99091 1.000 40.71154  ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 54  ? -1.94892  -7.77867  -17.06841 1.000 34.61883  ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 54  ? -0.41080  -9.39619  -16.19187 1.000 42.08651  ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 54  ? -1.64319  -9.07936  -16.72997 1.000 36.40107  ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 54  ? -2.57379  -10.07036 -16.92964 1.000 37.39252  ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 55  ? 4.11621   -4.49724  -16.88149 1.000 52.43363  ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 55  ? 4.89754   -3.28013  -16.71457 1.000 55.57249  ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 55  ? 4.99881   -2.55626  -18.03899 1.000 54.94256  ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 55  ? 4.74007   -1.34806  -18.10496 1.000 47.58679  ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 55  ? 6.30230   -3.54973  -16.15412 1.000 60.27091  ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 55  ? 6.35881   -3.85502  -14.69459 1.000 58.18567  ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 55  ? 6.15690   -5.34035  -14.38011 1.000 69.34114  ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 55  ? 5.46093   -6.07578  -15.14309 1.000 63.38177  ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 55  ? 6.61797   -5.75944  -13.29146 1.000 81.15772  ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 56  ? 5.42027   -3.25909  -19.12527 1.000 67.28724  ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? 5.44895   -2.57427  -20.43855 1.000 67.29283  ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? 4.05117   -2.23616  -20.91502 1.000 65.86860  ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? 3.83422   -1.14987  -21.46547 1.000 64.90730  ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? 6.01791   -3.27645  -21.70701 1.000 68.62413  ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? 7.43263   -3.55061  -21.68316 1.000 73.62996  ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? 7.97568   -3.10043  -20.76061 1.000 73.24116  ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? 8.08452   -3.91545  -22.67440 1.000 82.97292  ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 57  ? 3.06961   -3.11030  -20.62970 1.000 50.44847  ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 57  ? 1.69258   -2.78944  -21.04600 1.000 46.53600  ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 57  ? 1.19671   -1.47528  -20.41368 1.000 44.49841  ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 57  ? 0.41081   -0.72593  -21.02288 1.000 46.22046  ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 57  ? 0.70433   -3.94863  -20.72721 1.000 48.50753  ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 57  ? 0.83227   -5.20155  -21.61280 1.000 52.21336  ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 57  ? -0.19439  -6.22462  -21.15544 1.000 54.58600  ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 57  ? 0.67195   -4.84129  -23.08951 1.000 52.53812  ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 58  ? 1.66810   -1.16255  -19.21528 1.000 44.96820  ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 58  ? 1.15463   -0.03369  -18.45539 1.000 41.27069  ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 58  ? 1.92481   1.25850   -18.70628 1.000 44.12520  ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 58  ? 1.32654   2.34017   -18.67098 1.000 41.21202  ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 58  ? 1.17753   -0.36220  -16.96267 1.000 35.41915  ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 58  ? 0.38171   0.62616   -16.11915 1.000 34.92393  ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 58  ? -0.99752  0.74776   -16.71859 1.000 37.53918  ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 58  ? 0.29390   0.18851   -14.65693 1.000 37.64230  ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 59  ? 3.23810   1.18040   -18.94798 1.000 41.52903  ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 59  ? 3.99899   2.36505   -19.36674 1.000 45.55842  ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 59  ? 3.43006   2.97055   -20.64684 1.000 40.67677  ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 59  ? 3.54912   4.18598   -20.87561 1.000 42.29923  ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 59  ? 5.49594   2.00708   -19.52908 1.000 43.50019  ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 59  ? 6.34766   3.25035   -19.70690 1.000 43.50359  ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 59  ? 5.72164   1.12752   -20.71850 1.000 46.96631  ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 59  ? 6.37557   4.12149   -18.51160 1.000 48.41845  ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 60  ? 2.79553   2.14265   -21.49317 1.000 42.53170  ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 60  ? 2.26316   2.54730   -22.79429 1.000 40.96143  ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 60  ? 0.86325   3.13931   -22.72091 1.000 42.41585  ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 60  ? 0.37712   3.67415   -23.72843 1.000 40.94722  ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 60  ? 2.24293   1.35571   -23.75692 1.000 37.94824  ? 60  ARG   A CB  1 
ATOM   461  C CG  . ARG   A 1 60  ? 3.60474   0.83563   -24.05170 1.000 39.66734  ? 60  ARG   A CG  1 
ATOM   462  C CD  . ARG   A 1 60  ? 3.60860   -0.57599  -24.57296 1.000 43.26825  ? 60  ARG   A CD  1 
ATOM   463  N NE  . ARG   A 1 60  ? 4.95782   -0.90457  -25.03276 1.000 49.50074  ? 60  ARG   A NE  1 
ATOM   464  C CZ  . ARG   A 1 60  ? 5.43317   -2.13501  -25.19658 1.000 52.79260  ? 60  ARG   A CZ  1 
ATOM   465  N NH1 . ARG   A 1 60  ? 4.67238   -3.19735  -24.92846 1.000 51.58345  ? 60  ARG   A NH1 1 
ATOM   466  N NH2 . ARG   A 1 60  ? 6.68269   -2.29777  -25.62420 1.000 47.34979  ? 60  ARG   A NH2 1 
ATOM   467  N N   . LYS   A 1 61  ? 0.20889   3.04023   -21.56774 1.000 42.15674  ? 61  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 61  ? -1.11388  3.60089   -21.35765 1.000 40.25857  ? 61  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 61  ? -0.99786  5.03864   -20.86974 1.000 43.02687  ? 61  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 61  ? -0.08177  5.37684   -20.11770 1.000 44.12023  ? 61  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 61  ? -1.88268  2.76795   -20.32896 1.000 37.09344  ? 61  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 61  ? -2.17663  1.35386   -20.77097 1.000 40.38544  ? 61  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 61  ? -3.19406  1.34376   -21.90127 1.000 46.35321  ? 61  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 61  ? -3.56085  -0.06107  -22.35296 1.000 38.95286  ? 61  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 61  ? -4.42243  0.02874   -23.56995 1.000 38.89635  ? 61  LYS   A NZ  1 
ATOM   476  N N   . SER   A 1 62  ? -1.92547  5.88575   -21.30645 1.000 55.75387  ? 62  SER   A N   1 
ATOM   477  C CA  . SER   A 1 62  ? -2.16072  7.17738   -20.67564 1.000 56.72709  ? 62  SER   A CA  1 
ATOM   478  C C   . SER   A 1 62  ? -3.52932  7.16758   -19.99613 1.000 57.52026  ? 62  SER   A C   1 
ATOM   479  O O   . SER   A 1 62  ? -4.37595  6.29936   -20.25570 1.000 54.68251  ? 62  SER   A O   1 
ATOM   480  C CB  . SER   A 1 62  ? -2.02539  8.32661   -21.68648 1.000 57.63418  ? 62  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 62  ? -2.85801  8.14582   -22.81724 1.000 60.25579  ? 62  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 63  ? -3.71434  8.11808   -19.07129 1.000 53.68241  ? 63  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 63  ? -4.87532  8.07942   -18.18174 1.000 45.79540  ? 63  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 63  ? -6.18361  7.99342   -18.95351 1.000 48.76235  ? 63  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 63  ? -7.07166  7.21066   -18.59172 1.000 49.35365  ? 63  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 63  ? -4.89273  9.30383   -17.26755 1.000 43.18749  ? 63  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 63  ? -3.77840  9.28453   -16.24439 1.000 45.69846  ? 63  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 63  ? -3.11241  8.27114   -16.05939 1.000 48.95639  ? 63  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 63  ? -3.58230  10.40379  -15.55684 1.000 42.69032  ? 63  ASN   A ND2 1 
ATOM   490  N N   . HIS   A 1 64  ? -6.32346  8.78313   -20.02524 1.000 48.67626  ? 64  HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 64  ? -7.58629  8.80308   -20.75588 1.000 49.07624  ? 64  HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 64  ? -7.88860  7.48354   -21.45510 1.000 49.60369  ? 64  HIS   A C   1 
ATOM   493  O O   . HIS   A 1 64  ? -9.00213  7.32551   -21.97579 1.000 46.76400  ? 64  HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 64  ? -7.61489  9.95318   -21.77033 1.000 43.84337  ? 64  HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 64  ? -6.42976  9.99722   -22.67910 1.000 49.71349  ? 64  HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 64  ? -6.40781  9.36399   -23.90428 1.000 49.73204  ? 64  HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 64  ? -5.23500  10.62685  -22.55718 1.000 50.82843  ? 64  HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 64  ? -5.24519  9.59331   -24.49310 1.000 51.23875  ? 64  HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 64  ? -4.51599  10.35644  -23.69706 1.000 50.03643  ? 64  HIS   A NE2 1 
ATOM   500  N N   . ASN   A 1 65  ? -6.94451  6.53378   -21.47084 1.000 46.47998  ? 65  ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 65  ? -7.27900  5.18860   -21.92154 1.000 47.21067  ? 65  ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 65  ? -8.21285  4.46458   -20.95648 1.000 44.97033  ? 65  ASN   A C   1 
ATOM   503  O O   . ASN   A 1 65  ? -8.77561  3.42950   -21.33231 1.000 44.71778  ? 65  ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 65  ? -6.01166  4.35151   -22.13586 1.000 44.90197  ? 65  ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 65  ? -5.11960  4.90382   -23.22332 1.000 49.35369  ? 65  ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 65  ? -3.90978  5.07836   -23.02676 1.000 47.18154  ? 65  ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 65  ? -5.70778  5.18480   -24.38524 1.000 49.09828  ? 65  ASN   A ND2 1 
ATOM   508  N N   . PHE   A 1 66  ? -8.41178  4.99132   -19.74361 1.000 43.54600  ? 66  PHE   A N   1 
ATOM   509  C CA  . PHE   A 1 66  ? -9.23575  4.33962   -18.71915 1.000 46.48054  ? 66  PHE   A CA  1 
ATOM   510  C C   . PHE   A 1 66  ? -10.58299 5.05268   -18.59976 1.000 43.91025  ? 66  PHE   A C   1 
ATOM   511  O O   . PHE   A 1 66  ? -10.68076 6.16081   -18.06373 1.000 43.80526  ? 66  PHE   A O   1 
ATOM   512  C CB  . PHE   A 1 66  ? -8.50642  4.29683   -17.38107 1.000 40.97324  ? 66  PHE   A CB  1 
ATOM   513  C CG  . PHE   A 1 66  ? -7.27484  3.44642   -17.40032 1.000 40.29797  ? 66  PHE   A CG  1 
ATOM   514  C CD1 . PHE   A 1 66  ? -7.37588  2.06242   -17.45129 1.000 40.41773  ? 66  PHE   A CD1 1 
ATOM   515  C CD2 . PHE   A 1 66  ? -6.01208  4.02869   -17.39249 1.000 39.49578  ? 66  PHE   A CD2 1 
ATOM   516  C CE1 . PHE   A 1 66  ? -6.23458  1.26328   -17.47327 1.000 39.75863  ? 66  PHE   A CE1 1 
ATOM   517  C CE2 . PHE   A 1 66  ? -4.86290  3.23878   -17.41612 1.000 39.19348  ? 66  PHE   A CE2 1 
ATOM   518  C CZ  . PHE   A 1 66  ? -4.97499  1.85512   -17.45587 1.000 39.13024  ? 66  PHE   A CZ  1 
ATOM   519  N N   . LEU   A 1 67  ? -11.62303 4.38977   -19.08263 1.000 43.83579  ? 67  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 67  ? -12.98371 4.88997   -19.01468 1.000 42.32359  ? 67  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 67  ? -13.62048 4.29384   -17.76121 1.000 41.32727  ? 67  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 67  ? -13.71446 3.06717   -17.64800 1.000 38.09227  ? 67  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 67  ? -13.74663 4.45994   -20.26967 1.000 43.18542  ? 67  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 67  ? -13.41533 5.09734   -21.62864 1.000 45.25696  ? 67  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 67  ? -12.07645 4.58922   -22.20239 1.000 45.48983  ? 67  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 67  ? -14.53381 4.87063   -22.63119 1.000 36.31908  ? 67  LEU   A CD2 1 
ATOM   527  N N   . VAL   A 1 68  ? -14.05244 5.14411   -16.82635 1.000 43.66034  ? 68  VAL   A N   1 
ATOM   528  C CA  . VAL   A 1 68  ? -14.65272 4.70882   -15.56320 1.000 41.52374  ? 68  VAL   A CA  1 
ATOM   529  C C   . VAL   A 1 68  ? -16.06502 5.29246   -15.45180 1.000 48.44413  ? 68  VAL   A C   1 
ATOM   530  O O   . VAL   A 1 68  ? -16.22296 6.51968   -15.36682 1.000 51.95390  ? 68  VAL   A O   1 
ATOM   531  C CB  . VAL   A 1 68  ? -13.79502 5.12753   -14.35735 1.000 41.74651  ? 68  VAL   A CB  1 
ATOM   532  C CG1 . VAL   A 1 68  ? -14.42594 4.66139   -13.05907 1.000 37.57147  ? 68  VAL   A CG1 1 
ATOM   533  C CG2 . VAL   A 1 68  ? -12.36707 4.59856   -14.49561 1.000 34.06241  ? 68  VAL   A CG2 1 
ATOM   534  N N   . GLN   A 1 69  ? -17.09049 4.41955   -15.44032 1.000 41.87582  ? 69  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 69  ? -18.46526 4.82115   -15.12679 1.000 46.13985  ? 69  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 69  ? -18.76915 4.55045   -13.65675 1.000 43.47864  ? 69  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 69  ? -18.53797 3.44201   -13.16695 1.000 39.40753  ? 69  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 69  ? -19.51938 4.05823   -15.93651 1.000 48.92108  ? 69  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 69  ? -19.51951 4.00461   -17.45159 1.000 57.39538  ? 69  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 69  ? -19.42299 5.32458   -18.16523 1.000 58.17314  ? 69  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 69  ? -20.21146 6.23720   -17.93481 1.000 65.98428  ? 69  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 69  ? -18.48160 5.41037   -19.09372 1.000 59.79741  ? 69  GLN   A NE2 1 
ATOM   543  N N   . ALA   A 1 70  ? -19.33370 5.53823   -12.97253 1.000 49.78649  ? 70  ALA   A N   1 
ATOM   544  C CA  . ALA   A 1 70  ? -20.06097 5.31440   -11.72424 1.000 47.43999  ? 70  ALA   A CA  1 
ATOM   545  C C   . ALA   A 1 70  ? -21.52451 5.60431   -12.05841 1.000 51.32818  ? 70  ALA   A C   1 
ATOM   546  O O   . ALA   A 1 70  ? -21.97932 6.74966   -11.99604 1.000 49.00294  ? 70  ALA   A O   1 
ATOM   547  C CB  . ALA   A 1 70  ? -19.53941 6.18102   -10.59005 1.000 43.15550  ? 70  ALA   A CB  1 
ATOM   548  N N   . GLY   A 1 71  ? -22.24390 4.55482   -12.45787 1.000 47.72423  ? 71  GLY   A N   1 
ATOM   549  C CA  . GLY   A 1 71  ? -23.59059 4.73601   -12.98807 1.000 55.10809  ? 71  GLY   A CA  1 
ATOM   550  C C   . GLY   A 1 71  ? -23.53871 5.34115   -14.38343 1.000 59.74634  ? 71  GLY   A C   1 
ATOM   551  O O   . GLY   A 1 71  ? -22.73342 4.94406   -15.23451 1.000 59.19133  ? 71  GLY   A O   1 
ATOM   552  N N   . ASN   A 1 72  ? -24.42560 6.30062   -14.63482 1.000 61.01157  ? 72  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 72  ? -24.40545 7.09630   -15.85387 1.000 65.90096  ? 72  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 72  ? -23.46751 8.28967   -15.74388 1.000 67.00959  ? 72  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 72  ? -23.51243 9.18156   -16.59777 1.000 65.46483  ? 72  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 72  ? -25.81800 7.58398   -16.20078 1.000 70.98541  ? 72  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 72  ? -26.66966 6.50771   -16.83894 1.000 74.27663  ? 72  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 72  ? -26.32942 5.31997   -16.80732 1.000 67.88372  ? 72  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 72  ? -27.79425 6.92078   -17.42540 1.000 79.11326  ? 72  ASN   A ND2 1 
ATOM   560  N N   . VAL   A 1 73  ? -22.64582 8.33360   -14.69830 1.000 64.47507  ? 73  VAL   A N   1 
ATOM   561  C CA  . VAL   A 1 73  ? -21.69869 9.41493   -14.45481 1.000 63.09351  ? 73  VAL   A CA  1 
ATOM   562  C C   . VAL   A 1 73  ? -20.31260 8.93581   -14.85619 1.000 61.01767  ? 73  VAL   A C   1 
ATOM   563  O O   . VAL   A 1 73  ? -19.94847 7.77641   -14.62334 1.000 61.13822  ? 73  VAL   A O   1 
ATOM   564  C CB  . VAL   A 1 73  ? -21.74865 9.86169   -12.98098 1.000 58.39446  ? 73  VAL   A CB  1 
ATOM   565  C CG1 . VAL   A 1 73  ? -20.63010 10.81700  -12.67573 1.000 55.61659  ? 73  VAL   A CG1 1 
ATOM   566  C CG2 . VAL   A 1 73  ? -23.08696 10.52737  -12.69802 1.000 61.15548  ? 73  VAL   A CG2 1 
ATOM   567  N N   . GLN   A 1 74  ? -19.54180 9.82070   -15.46871 1.000 64.69229  ? 74  GLN   A N   1 
ATOM   568  C CA  . GLN   A 1 74  ? -18.30564 9.45536   -16.14950 1.000 65.08913  ? 74  GLN   A CA  1 
ATOM   569  C C   . GLN   A 1 74  ? -17.14670 9.98982   -15.31275 1.000 63.22388  ? 74  GLN   A C   1 
ATOM   570  O O   . GLN   A 1 74  ? -16.92388 11.19788  -15.26192 1.000 66.62545  ? 74  GLN   A O   1 
ATOM   571  C CB  . GLN   A 1 74  ? -18.29992 10.02806  -17.56507 1.000 69.32663  ? 74  GLN   A CB  1 
ATOM   572  C CG  . GLN   A 1 74  ? -19.39054 9.48011   -18.52557 1.000 76.12579  ? 74  GLN   A CG  1 
ATOM   573  C CD  . GLN   A 1 74  ? -20.71578 10.27762  -18.44816 1.000 81.79018  ? 74  GLN   A CD  1 
ATOM   574  O OE1 . GLN   A 1 74  ? -21.00096 10.94803  -17.44558 1.000 78.39448  ? 74  GLN   A OE1 1 
ATOM   575  N NE2 . GLN   A 1 74  ? -21.50967 10.22125  -19.52013 1.000 80.35378  ? 74  GLN   A NE2 1 
ATOM   576  N N   . LEU   A 1 75  ? -16.41799 9.09700   -14.64661 1.000 54.99307  ? 75  LEU   A N   1 
ATOM   577  C CA  . LEU   A 1 75  ? -15.28057 9.51018   -13.83565 1.000 53.70215  ? 75  LEU   A CA  1 
ATOM   578  C C   . LEU   A 1 75  ? -14.03877 9.75440   -14.68966 1.000 54.06004  ? 75  LEU   A C   1 
ATOM   579  O O   . LEU   A 1 75  ? -13.86367 9.17432   -15.76872 1.000 56.51748  ? 75  LEU   A O   1 
ATOM   580  C CB  . LEU   A 1 75  ? -14.95928 8.46487   -12.77071 1.000 49.32901  ? 75  LEU   A CB  1 
ATOM   581  C CG  . LEU   A 1 75  ? -15.87151 8.44773   -11.55247 1.000 45.08179  ? 75  LEU   A CG  1 
ATOM   582  C CD1 . LEU   A 1 75  ? -15.46306 7.35607   -10.58029 1.000 35.37722  ? 75  LEU   A CD1 1 
ATOM   583  C CD2 . LEU   A 1 75  ? -15.81600 9.81808   -10.89056 1.000 47.48839  ? 75  LEU   A CD2 1 
ATOM   584  N N   . ARG   A 1 76  ? -13.15488 10.60523  -14.16387 1.000 51.01228  ? 76  ARG   A N   1 
ATOM   585  C CA  . ARG   A 1 76  ? -11.90366 10.98750  -14.81375 1.000 50.08677  ? 76  ARG   A CA  1 
ATOM   586  C C   . ARG   A 1 76  ? -10.72787 10.40397  -14.04293 1.000 45.09714  ? 76  ARG   A C   1 
ATOM   587  O O   . ARG   A 1 76  ? -10.56285 10.68863  -12.85090 1.000 44.30209  ? 76  ARG   A O   1 
ATOM   588  C CB  . ARG   A 1 76  ? -11.76450 12.51189  -14.89087 1.000 53.01217  ? 76  ARG   A CB  1 
ATOM   589  C CG  . ARG   A 1 76  ? -10.97436 13.01947  -16.09645 1.000 55.10642  ? 76  ARG   A CG  1 
ATOM   590  C CD  . ARG   A 1 76  ? -11.23192 14.49922  -16.37193 1.000 66.90891  ? 76  ARG   A CD  1 
ATOM   591  N NE  . ARG   A 1 76  ? -12.41349 14.70131  -17.21270 1.000 69.37431  ? 76  ARG   A NE  1 
ATOM   592  C CZ  . ARG   A 1 76  ? -12.49174 14.39647  -18.50842 1.000 70.79978  ? 76  ARG   A CZ  1 
ATOM   593  N NH1 . ARG   A 1 76  ? -11.44906 13.88065  -19.15302 1.000 67.33907  ? 76  ARG   A NH1 1 
ATOM   594  N NH2 . ARG   A 1 76  ? -13.62158 14.62001  -19.16768 1.000 74.62880  ? 76  ARG   A NH2 1 
ATOM   595  N N   . VAL   A 1 77  ? -9.89523  9.62271   -14.72474 1.000 45.19644  ? 77  VAL   A N   1 
ATOM   596  C CA  . VAL   A 1 77  ? -8.66545  9.12042   -14.11460 1.000 45.02049  ? 77  VAL   A CA  1 
ATOM   597  C C   . VAL   A 1 77  ? -7.58701  10.19253  -14.21111 1.000 42.38730  ? 77  VAL   A C   1 
ATOM   598  O O   . VAL   A 1 77  ? -7.36139  10.76428  -15.28194 1.000 47.81971  ? 77  VAL   A O   1 
ATOM   599  C CB  . VAL   A 1 77  ? -8.21075  7.81110   -14.78067 1.000 43.54573  ? 77  VAL   A CB  1 
ATOM   600  C CG1 . VAL   A 1 77  ? -6.89200  7.33428   -14.18371 1.000 38.60889  ? 77  VAL   A CG1 1 
ATOM   601  C CG2 . VAL   A 1 77  ? -9.28095  6.73515   -14.62017 1.000 40.29773  ? 77  VAL   A CG2 1 
ATOM   602  N N   . ILE   A 1 78  ? -6.92734  10.47067  -13.08795 1.000 40.46640  ? 78  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 78  ? -5.86676  11.47338  -13.01032 1.000 43.98865  ? 78  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 78  ? -4.50324  10.86000  -12.71018 1.000 46.68639  ? 78  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 78  ? -3.51849  11.59797  -12.55781 1.000 42.82210  ? 78  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 78  ? -6.21354  12.56933  -11.97946 1.000 42.79450  ? 78  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 78  ? -6.32727  11.97645  -10.57050 1.000 44.78776  ? 78  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 78  ? -7.53372  13.25279  -12.35635 1.000 41.45724  ? 78  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 78  ? -6.47355  12.99553  -9.47660  1.000 43.69718  ? 78  ILE   A CD1 1 
ATOM   610  N N   . GLY   A 1 79  ? -4.41238  9.53247   -12.65223 1.000 43.67237  ? 79  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 79  ? -3.17284  8.82736   -12.41119 1.000 43.60975  ? 79  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 79  ? -3.42610  7.34649   -12.22000 1.000 42.48432  ? 79  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 79  ? -4.50889  6.95078   -11.77386 1.000 39.75899  ? 79  GLY   A O   1 
ATOM   614  N N   . HIS   A 1 80  ? -2.44784  6.51200   -12.56458 1.000 42.85156  ? 80  HIS   A N   1 
ATOM   615  C CA  . HIS   A 1 80  ? -2.58054  5.07116   -12.41811 1.000 40.24567  ? 80  HIS   A CA  1 
ATOM   616  C C   . HIS   A 1 80  ? -1.33257  4.50295   -11.75888 1.000 38.73825  ? 80  HIS   A C   1 
ATOM   617  O O   . HIS   A 1 80  ? -0.23664  5.06940   -11.86339 1.000 35.17573  ? 80  HIS   A O   1 
ATOM   618  C CB  . HIS   A 1 80  ? -2.80287  4.38442   -13.76283 1.000 36.79807  ? 80  HIS   A CB  1 
ATOM   619  C CG  . HIS   A 1 80  ? -1.82201  4.79605   -14.81120 1.000 40.10348  ? 80  HIS   A CG  1 
ATOM   620  N ND1 . HIS   A 1 80  ? -2.01247  5.89998   -15.61548 1.000 47.37852  ? 80  HIS   A ND1 1 
ATOM   621  C CD2 . HIS   A 1 80  ? -0.63755  4.25859   -15.18434 1.000 34.96020  ? 80  HIS   A CD2 1 
ATOM   622  C CE1 . HIS   A 1 80  ? -0.99069  6.02019   -16.44572 1.000 47.33714  ? 80  HIS   A CE1 1 
ATOM   623  N NE2 . HIS   A 1 80  ? -0.13969  5.03972   -16.20011 1.000 48.22657  ? 80  HIS   A NE2 1 
ATOM   624  N N   . SER   A 1 81  ? -1.51804  3.37293   -11.07386 1.000 34.25091  ? 81  SER   A N   1 
ATOM   625  C CA  . SER   A 1 81  ? -0.42267  2.63926   -10.45481 1.000 34.06316  ? 81  SER   A CA  1 
ATOM   626  C C   . SER   A 1 81  ? -0.79639  1.16679   -10.35326 1.000 34.07911  ? 81  SER   A C   1 
ATOM   627  O O   . SER   A 1 81  ? -1.96401  0.81834   -10.17099 1.000 29.84741  ? 81  SER   A O   1 
ATOM   628  C CB  . SER   A 1 81  ? -0.08480  3.19772   -9.06449  1.000 30.52590  ? 81  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 81  ? -1.27752  3.48683   -8.35180  1.000 30.55865  ? 81  SER   A OG  1 
ATOM   630  N N   . MET   A 1 82  ? 0.21073   0.30769   -10.45575 1.000 32.11207  ? 82  MET   A N   1 
ATOM   631  C CA  . MET   A 1 82  ? 0.04955   -1.12422  -10.27030 1.000 27.14955  ? 82  MET   A CA  1 
ATOM   632  C C   . MET   A 1 82  ? 0.60992   -1.55442  -8.91943  1.000 31.02395  ? 82  MET   A C   1 
ATOM   633  O O   . MET   A 1 82  ? 1.76979   -1.27567  -8.60959  1.000 31.28830  ? 82  MET   A O   1 
ATOM   634  C CB  . MET   A 1 82  ? 0.75528   -1.87564  -11.39263 1.000 31.94621  ? 82  MET   A CB  1 
ATOM   635  C CG  . MET   A 1 82  ? 0.40355   -3.34161  -11.46302 1.000 31.22289  ? 82  MET   A CG  1 
ATOM   636  S SD  . MET   A 1 82  ? 0.84615   -3.97146  -13.07839 1.000 37.58475  ? 82  MET   A SD  1 
ATOM   637  C CE  . MET   A 1 82  ? 2.53961   -3.35150  -13.23999 1.000 38.08109  ? 82  MET   A CE  1 
ATOM   638  N N   . GLN   A 1 83  ? -0.20966  -2.24250  -8.12154  1.000 30.21184  ? 83  GLN   A N   1 
ATOM   639  C CA  . GLN   A 1 83  ? 0.22999   -2.87111  -6.87882  1.000 25.40828  ? 83  GLN   A CA  1 
ATOM   640  C C   . GLN   A 1 83  ? -0.05516  -4.36221  -7.00679  1.000 25.10020  ? 83  GLN   A C   1 
ATOM   641  O O   . GLN   A 1 83  ? -1.20301  -4.79027  -6.85550  1.000 26.59276  ? 83  GLN   A O   1 
ATOM   642  C CB  . GLN   A 1 83  ? -0.47515  -2.28193  -5.66114  1.000 27.48295  ? 83  GLN   A CB  1 
ATOM   643  C CG  . GLN   A 1 83  ? -0.01308  -2.91079  -4.32707  1.000 26.04971  ? 83  GLN   A CG  1 
ATOM   644  C CD  . GLN   A 1 83  ? -0.78611  -2.38831  -3.11639  1.000 22.25278  ? 83  GLN   A CD  1 
ATOM   645  O OE1 . GLN   A 1 83  ? -1.57046  -1.45073  -3.22756  1.000 24.42040  ? 83  GLN   A OE1 1 
ATOM   646  N NE2 . GLN   A 1 83  ? -0.54616  -2.98390  -1.95459  1.000 19.66363  ? 83  GLN   A NE2 1 
ATOM   647  N N   . ASN   A 1 84  ? 0.98623   -5.15255  -7.26303  1.000 24.83596  ? 84  ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 84  ? 0.85826   -6.59346  -7.48208  1.000 20.36196  ? 84  ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 84  ? -0.07321  -6.79709  -8.67176  1.000 24.72122  ? 84  ASN   A C   1 
ATOM   650  O O   . ASN   A 1 84  ? 0.24742   -6.31948  -9.77092  1.000 30.38781  ? 84  ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 84  ? 0.44879   -7.22485  -6.16325  1.000 18.74837  ? 84  ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 84  ? 1.35237   -6.78569  -5.03605  1.000 22.33303  ? 84  ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 84  ? 2.58348   -6.95721  -5.10959  1.000 22.68910  ? 84  ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 84  ? 0.76727   -6.18802  -3.99976  1.000 20.03246  ? 84  ASN   A ND2 1 
ATOM   655  N N   . CYS   A 1 85  ? -1.22690  -7.43168  -8.51898  1.000 22.51396  ? 85  CYS   A N   1 
ATOM   656  C CA  . CYS   A 1 85  ? -2.05413  -7.68191  -9.68549  1.000 23.31242  ? 85  CYS   A CA  1 
ATOM   657  C C   . CYS   A 1 85  ? -3.25950  -6.73919  -9.81831  1.000 23.92622  ? 85  CYS   A C   1 
ATOM   658  O O   . CYS   A 1 85  ? -4.13312  -7.00087  -10.65484 1.000 24.22632  ? 85  CYS   A O   1 
ATOM   659  C CB  . CYS   A 1 85  ? -2.48634  -9.14372  -9.68345  1.000 21.26073  ? 85  CYS   A CB  1 
ATOM   660  S SG  . CYS   A 1 85  ? -1.03848  -10.23742 -9.95411  1.000 21.37407  ? 85  CYS   A SG  1 
ATOM   661  N N   . VAL   A 1 86  ? -3.31870  -5.63530  -9.06649  1.000 20.64821  ? 86  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 86  ? -4.46254  -4.72500  -9.13884  1.000 28.32258  ? 86  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 86  ? -4.02776  -3.36553  -9.67382  1.000 31.74553  ? 86  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 86  ? -2.94289  -2.86286  -9.35196  1.000 29.00130  ? 86  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 86  ? -5.19322  -4.53925  -7.78650  1.000 24.20934  ? 86  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 86  ? -5.81803  -5.84920  -7.29232  1.000 23.11175  ? 86  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 86  ? -4.30280  -3.91261  -6.75201  1.000 21.32628  ? 86  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 87  ? -4.89711  -2.76899  -10.48591 1.000 32.12598  ? 87  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 87  ? -4.75250  -1.37725  -10.88287 1.000 30.63625  ? 87  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 87  ? -5.36772  -0.46387  -9.83704  1.000 32.16078  ? 87  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 87  ? -6.50025  -0.69449  -9.38866  1.000 31.30214  ? 87  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 87  ? -5.43969  -1.11965  -12.21178 1.000 32.01745  ? 87  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 87  ? -4.56819  -0.97928  -13.42988 1.000 35.38251  ? 87  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 87  ? -5.47236  -0.49537  -14.53901 1.000 38.07197  ? 87  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 87  ? -3.47978  0.02009   -13.13305 1.000 34.32881  ? 87  LEU   A CD2 1 
ATOM   676  N N   . LYS   A 1 88  ? -4.62844  0.58519   -9.46367  1.000 30.35554  ? 88  LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 88  ? -5.13102  1.63958   -8.58656  1.000 29.53489  ? 88  LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 88  ? -5.21859  2.90386   -9.43111  1.000 28.94727  ? 88  LYS   A C   1 
ATOM   679  O O   . LYS   A 1 88  ? -4.19490  3.48182   -9.81340  1.000 33.73039  ? 88  LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 88  ? -4.25108  1.81745   -7.34259  1.000 26.14991  ? 88  LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 88  ? -4.17950  0.56082   -6.43049  1.000 24.48373  ? 88  LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 88  ? -2.92457  0.49980   -5.51963  1.000 23.53182  ? 88  LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 88  ? -3.17935  1.24694   -4.23034  1.000 29.83585  ? 88  LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 88  ? -2.09516  1.22175   -3.19985  1.000 25.89245  ? 88  LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 89  ? -6.43948  3.30846   -9.74827  1.000 29.21114  ? 89  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -6.69940  4.42848   -10.64726 1.000 32.75084  ? 89  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -7.17182  5.59172   -9.78655  1.000 35.03284  ? 89  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -8.30027  5.57522   -9.28343  1.000 35.58764  ? 89  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -7.74144  4.05057   -11.69086 1.000 31.28332  ? 89  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -7.41378  2.89727   -12.62995 1.000 31.04489  ? 89  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -8.66603  2.43737   -13.33613 1.000 28.64746  ? 89  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -6.38937  3.35978   -13.64643 1.000 32.55725  ? 89  LEU   A CD2 1 
ATOM   693  N N   . LYS   A 1 90  ? -6.30160  6.58877   -9.59743  1.000 33.31642  ? 90  LYS   A N   1 
ATOM   694  C CA  . LYS   A 1 90  ? -6.66089  7.76215   -8.81363  1.000 35.71980  ? 90  LYS   A CA  1 
ATOM   695  C C   . LYS   A 1 90  ? -7.57596  8.62086   -9.68753  1.000 41.62567  ? 90  LYS   A C   1 
ATOM   696  O O   . LYS   A 1 90  ? -7.22159  8.93527   -10.82936 1.000 41.26625  ? 90  LYS   A O   1 
ATOM   697  C CB  . LYS   A 1 90  ? -5.40152  8.51030   -8.35673  1.000 39.92651  ? 90  LYS   A CB  1 
ATOM   698  C CG  . LYS   A 1 90  ? -5.63330  9.66152   -7.33504  1.000 44.44531  ? 90  LYS   A CG  1 
ATOM   699  C CD  . LYS   A 1 90  ? -4.50688  9.73249   -6.27133  1.000 44.92336  ? 90  LYS   A CD  1 
ATOM   700  C CE  . LYS   A 1 90  ? -4.98314  10.27804  -4.92097  1.000 48.79308  ? 90  LYS   A CE  1 
ATOM   701  N NZ  . LYS   A 1 90  ? -3.85265  10.83490  -4.08520  1.000 51.79281  ? 90  LYS   A NZ  1 
ATOM   702  N N   . VAL   A 1 91  ? -8.77750  8.93830   -9.18214  1.000 40.69696  ? 91  VAL   A N   1 
ATOM   703  C CA  . VAL   A 1 91  ? -9.79991  9.66231   -9.93753  1.000 40.71916  ? 91  VAL   A CA  1 
ATOM   704  C C   . VAL   A 1 91  ? -10.08300 10.99892  -9.25455  1.000 43.64285  ? 91  VAL   A C   1 
ATOM   705  O O   . VAL   A 1 91  ? -9.82606  11.18318  -8.05960  1.000 48.02000  ? 91  VAL   A O   1 
ATOM   706  C CB  . VAL   A 1 91  ? -11.10252 8.83849   -10.09991 1.000 43.15083  ? 91  VAL   A CB  1 
ATOM   707  C CG1 . VAL   A 1 91  ? -10.85054 7.61050   -10.96767 1.000 39.47800  ? 91  VAL   A CG1 1 
ATOM   708  C CG2 . VAL   A 1 91  ? -11.70062 8.44835   -8.74667  1.000 36.68207  ? 91  VAL   A CG2 1 
ATOM   709  N N   . ASP   A 1 92  ? -10.62951 11.94794  -10.02430 1.000 40.81051  ? 92  ASP   A N   1 
ATOM   710  C CA  . ASP   A 1 92  ? -10.79130 13.29716  -9.47562  1.000 49.32947  ? 92  ASP   A CA  1 
ATOM   711  C C   . ASP   A 1 92  ? -11.89695 13.38620  -8.42073  1.000 49.27975  ? 92  ASP   A C   1 
ATOM   712  O O   . ASP   A 1 92  ? -11.87760 14.30877  -7.59995  1.000 50.16248  ? 92  ASP   A O   1 
ATOM   713  C CB  . ASP   A 1 92  ? -11.05630 14.32987  -10.58133 1.000 49.31065  ? 92  ASP   A CB  1 
ATOM   714  C CG  . ASP   A 1 92  ? -12.21247 13.94323  -11.49448 1.000 55.20545  ? 92  ASP   A CG  1 
ATOM   715  O OD1 . ASP   A 1 92  ? -12.34778 14.57547  -12.56779 1.000 59.86755  ? 92  ASP   A OD1 1 
ATOM   716  O OD2 . ASP   A 1 92  ? -12.96840 13.00215  -11.15302 1.000 51.67546  ? 92  ASP   A OD2 1 
ATOM   717  N N   . THR   A 1 93  ? -12.84768 12.45872  -8.41015  1.000 47.38213  ? 93  THR   A N   1 
ATOM   718  C CA  . THR   A 1 93  ? -13.95085 12.48630  -7.45396  1.000 47.57613  ? 93  THR   A CA  1 
ATOM   719  C C   . THR   A 1 93  ? -13.72388 11.45638  -6.34799  1.000 38.81453  ? 93  THR   A C   1 
ATOM   720  O O   . THR   A 1 93  ? -13.42423 10.29323  -6.62892  1.000 36.95547  ? 93  THR   A O   1 
ATOM   721  C CB  . THR   A 1 93  ? -15.28754 12.21052  -8.15301  1.000 45.97175  ? 93  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 93  ? -15.38346 13.00317  -9.34366  1.000 48.70864  ? 93  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 93  ? -16.45077 12.53905  -7.23081  1.000 37.92737  ? 93  THR   A CG2 1 
ATOM   724  N N   . ALA   A 1 94  ? -13.86077 11.88457  -5.09489  1.000 39.09124  ? 94  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 94  ? -13.91477 10.94450  -3.98568  1.000 38.36441  ? 94  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 94  ? -15.31381 10.32975  -3.91505  1.000 39.71809  ? 94  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 94  ? -16.31666 11.04002  -4.01647  1.000 29.56153  ? 94  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 94  ? -13.56717 11.63911  -2.67148  1.000 34.38327  ? 94  ALA   A CB  1 
ATOM   729  N N   . ASN   A 1 95  ? -15.38202 9.01074   -3.78246  1.000 34.27703  ? 95  ASN   A N   1 
ATOM   730  C CA  . ASN   A 1 95  ? -16.67063 8.34564   -3.67207  1.000 32.33065  ? 95  ASN   A CA  1 
ATOM   731  C C   . ASN   A 1 95  ? -17.32356 8.80428   -2.37762  1.000 35.12039  ? 95  ASN   A C   1 
ATOM   732  O O   . ASN   A 1 95  ? -16.74403 8.60305   -1.30194  1.000 35.01429  ? 95  ASN   A O   1 
ATOM   733  C CB  . ASN   A 1 95  ? -16.48908 6.83261   -3.69551  1.000 32.64042  ? 95  ASN   A CB  1 
ATOM   734  C CG  . ASN   A 1 95  ? -17.82484 6.05553   -3.61180  1.000 33.24926  ? 95  ASN   A CG  1 
ATOM   735  O OD1 . ASN   A 1 95  ? -18.90938 6.63331   -3.50852  1.000 32.72042  ? 95  ASN   A OD1 1 
ATOM   736  N ND2 . ASN   A 1 95  ? -17.72463 4.72845   -3.65057  1.000 29.94682  ? 95  ASN   A ND2 1 
ATOM   737  N N   . PRO   A 1 96  ? -18.47183 9.48399   -2.42640  1.000 33.73169  ? 96  PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 96  ? -19.10762 9.90544   -1.17000  1.000 36.46583  ? 96  PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 96  ? -19.74767 8.74784   -0.42920  1.000 34.84184  ? 96  PRO   A C   1 
ATOM   740  O O   . PRO   A 1 96  ? -20.01775 8.86761   0.76642   1.000 33.83154  ? 96  PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 96  ? -20.13777 10.96378  -1.61869  1.000 32.92232  ? 96  PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 96  ? -20.42254 10.63415  -3.08272  1.000 33.10105  ? 96  PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 96  ? -19.21391 9.91203   -3.62919  1.000 30.69456  ? 96  PRO   A CD  1 
ATOM   744  N N   . LYS   A 1 97  ? -19.98605 7.63134   -1.08556  1.000 31.47189  ? 97  LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 97  ? -20.58657 6.50601   -0.41682  1.000 33.52335  ? 97  LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 97  ? -19.56709 5.52552   0.05517   1.000 32.58395  ? 97  LYS   A C   1 
ATOM   747  O O   . LYS   A 1 97  ? -19.94571 4.38202   0.31257   1.000 32.33132  ? 97  LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 97  ? -21.56097 5.83094   -1.35928  1.000 30.68813  ? 97  LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 97  ? -22.68452 6.79362   -1.76731  1.000 32.55185  ? 97  LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 97  ? -23.58254 6.10422   -2.82245  1.000 28.39105  ? 97  LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 97  ? -22.70062 5.74786   -4.05153  1.000 36.59611  ? 97  LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 97  ? -21.96921 6.83675   -4.78528  1.000 31.20649  ? 97  LYS   A NZ  1 
ATOM   753  N N   . THR   A 1 98  ? -18.29887 5.95976   0.21092   1.000 33.14361  ? 98  THR   A N   1 
ATOM   754  C CA  . THR   A 1 98  ? -17.23151 5.14817   0.79196   1.000 32.11342  ? 98  THR   A CA  1 
ATOM   755  C C   . THR   A 1 98  ? -17.57411 4.78689   2.23491   1.000 32.22725  ? 98  THR   A C   1 
ATOM   756  O O   . THR   A 1 98  ? -17.69071 5.69466   3.07856   1.000 29.93885  ? 98  THR   A O   1 
ATOM   757  C CB  . THR   A 1 98  ? -15.88128 5.88262   0.79894   1.000 34.19277  ? 98  THR   A CB  1 
ATOM   758  O OG1 . THR   A 1 98  ? -15.45838 6.22860   -0.52909  1.000 32.14408  ? 98  THR   A OG1 1 
ATOM   759  C CG2 . THR   A 1 98  ? -14.81193 5.00758   1.44492   1.000 29.19733  ? 98  THR   A CG2 1 
ATOM   760  N N   . PRO   A 1 99  ? -17.72300 3.50330   2.56694   1.000 32.74353  ? 99  PRO   A N   1 
ATOM   761  C CA  . PRO   A 1 99  ? -17.85434 3.10215   3.96999   1.000 27.10834  ? 99  PRO   A CA  1 
ATOM   762  C C   . PRO   A 1 99  ? -16.49880 3.11830   4.64963   1.000 29.13155  ? 99  PRO   A C   1 
ATOM   763  O O   . PRO   A 1 99  ? -15.45415 3.14936   3.99174   1.000 27.80979  ? 99  PRO   A O   1 
ATOM   764  C CB  . PRO   A 1 99  ? -18.38921 1.66782   3.87156   1.000 27.20169  ? 99  PRO   A CB  1 
ATOM   765  C CG  . PRO   A 1 99  ? -17.74473 1.13843   2.64025   1.000 24.43731  ? 99  PRO   A CG  1 
ATOM   766  C CD  . PRO   A 1 99  ? -17.64797 2.33207   1.67309   1.000 31.16707  ? 99  PRO   A CD  1 
ATOM   767  N N   . LYS   A 1 100 ? -16.52945 3.11130   5.98716   1.000 27.79530  ? 100 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 100 ? -15.35517 2.66997   6.72644   1.000 25.23641  ? 100 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 100 ? -14.97793 1.28153   6.23632   1.000 25.99070  ? 100 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 100 ? -15.83927 0.41553   6.06126   1.000 22.71098  ? 100 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 100 ? -15.60241 2.65392   8.23683   1.000 29.58437  ? 100 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 100 ? -14.40713 2.08594   9.05068   1.000 36.22730  ? 100 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 100 ? -13.07566 2.88004   8.86761   1.000 40.73951  ? 100 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 100 ? -11.95923 2.47406   9.87897   1.000 51.66083  ? 100 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 100 ? -11.48020 1.03291   9.84518   1.000 45.23851  ? 100 LYS   A NZ  1 
ATOM   776  N N   . TYR   A 1 101 ? -13.68534 1.08656   5.98583   1.000 25.46446  ? 101 TYR   A N   1 
ATOM   777  C CA  . TYR   A 1 101 ? -13.22710 -0.10889  5.30735   1.000 25.19539  ? 101 TYR   A CA  1 
ATOM   778  C C   . TYR   A 1 101 ? -11.77088 -0.39927  5.64040   1.000 25.41363  ? 101 TYR   A C   1 
ATOM   779  O O   . TYR   A 1 101 ? -10.98731 0.50892   5.92889   1.000 30.68134  ? 101 TYR   A O   1 
ATOM   780  C CB  . TYR   A 1 101 ? -13.39832 0.02904   3.79308   1.000 24.44988  ? 101 TYR   A CB  1 
ATOM   781  C CG  . TYR   A 1 101 ? -12.33806 0.85251   3.12045   1.000 21.22218  ? 101 TYR   A CG  1 
ATOM   782  C CD1 . TYR   A 1 101 ? -12.50082 2.22643   2.96417   1.000 26.17477  ? 101 TYR   A CD1 1 
ATOM   783  C CD2 . TYR   A 1 101 ? -11.17390 0.25738   2.61691   1.000 22.43029  ? 101 TYR   A CD2 1 
ATOM   784  C CE1 . TYR   A 1 101 ? -11.52370 3.00052   2.33671   1.000 26.33488  ? 101 TYR   A CE1 1 
ATOM   785  C CE2 . TYR   A 1 101 ? -10.18962 1.01698   1.98473   1.000 22.75807  ? 101 TYR   A CE2 1 
ATOM   786  C CZ  . TYR   A 1 101 ? -10.37232 2.38487   1.84779   1.000 27.68439  ? 101 TYR   A CZ  1 
ATOM   787  O OH  . TYR   A 1 101 ? -9.40936  3.13477   1.21560   1.000 32.25210  ? 101 TYR   A OH  1 
ATOM   788  N N   . LYS   A 1 102 ? -11.43992 -1.68601  5.56261   1.000 21.24737  ? 102 LYS   A N   1 
ATOM   789  C CA  . LYS   A 1 102 ? -10.12780 -2.26397  5.74774   1.000 22.35825  ? 102 LYS   A CA  1 
ATOM   790  C C   . LYS   A 1 102 ? -9.89588  -3.19638  4.57291   1.000 23.05858  ? 102 LYS   A C   1 
ATOM   791  O O   . LYS   A 1 102 ? -10.84895 -3.71948  3.99229   1.000 19.69303  ? 102 LYS   A O   1 
ATOM   792  C CB  . LYS   A 1 102 ? -10.03037 -3.09207  7.06197   1.000 27.61940  ? 102 LYS   A CB  1 
ATOM   793  C CG  . LYS   A 1 102 ? -9.85420  -2.29434  8.36114   1.000 32.69278  ? 102 LYS   A CG  1 
ATOM   794  C CD  . LYS   A 1 102 ? -10.13246 -3.17069  9.62307   1.000 34.75966  ? 102 LYS   A CD  1 
ATOM   795  C CE  . LYS   A 1 102 ? -9.98417  -2.37994  10.94985  1.000 39.25757  ? 102 LYS   A CE  1 
ATOM   796  N NZ  . LYS   A 1 102 ? -11.19662 -1.55477  11.35782  1.000 37.74506  ? 102 LYS   A NZ  1 
ATOM   797  N N   . PHE   A 1 103 ? -8.62922  -3.40255  4.21912   1.000 21.93939  ? 103 PHE   A N   1 
ATOM   798  C CA  . PHE   A 1 103 ? -8.23865  -4.52024  3.37148   1.000 17.57157  ? 103 PHE   A CA  1 
ATOM   799  C C   . PHE   A 1 103 ? -7.62877  -5.56960  4.28773   1.000 18.98346  ? 103 PHE   A C   1 
ATOM   800  O O   . PHE   A 1 103 ? -6.68071  -5.27356  5.04072   1.000 18.85870  ? 103 PHE   A O   1 
ATOM   801  C CB  . PHE   A 1 103 ? -7.23235  -4.12008  2.29547   1.000 19.94671  ? 103 PHE   A CB  1 
ATOM   802  C CG  . PHE   A 1 103 ? -7.76796  -3.20505  1.23516   1.000 17.24682  ? 103 PHE   A CG  1 
ATOM   803  C CD1 . PHE   A 1 103 ? -9.13353  -2.97253  1.09466   1.000 19.17238  ? 103 PHE   A CD1 1 
ATOM   804  C CD2 . PHE   A 1 103 ? -6.87422  -2.53456  0.38716   1.000 17.91981  ? 103 PHE   A CD2 1 
ATOM   805  C CE1 . PHE   A 1 103 ? -9.62158  -2.10518  0.09780   1.000 15.67136  ? 103 PHE   A CE1 1 
ATOM   806  C CE2 . PHE   A 1 103 ? -7.33940  -1.66998  -0.61661  1.000 16.38760  ? 103 PHE   A CE2 1 
ATOM   807  C CZ  . PHE   A 1 103 ? -8.72165  -1.45146  -0.75351  1.000 18.27767  ? 103 PHE   A CZ  1 
ATOM   808  N N   . VAL   A 1 104 ? -8.18273  -6.77874  4.25299   1.000 15.14998  ? 104 VAL   A N   1 
ATOM   809  C CA  . VAL   A 1 104 ? -7.60800  -7.87447  5.00858   1.000 15.52066  ? 104 VAL   A CA  1 
ATOM   810  C C   . VAL   A 1 104 ? -7.30190  -8.98156  4.01902   1.000 15.98293  ? 104 VAL   A C   1 
ATOM   811  O O   . VAL   A 1 104 ? -7.97278  -9.13658  2.99137   1.000 19.21139  ? 104 VAL   A O   1 
ATOM   812  C CB  . VAL   A 1 104 ? -8.53706  -8.41874  6.12078   1.000 21.46092  ? 104 VAL   A CB  1 
ATOM   813  C CG1 . VAL   A 1 104 ? -9.00082  -7.32146  7.02394   1.000 19.81088  ? 104 VAL   A CG1 1 
ATOM   814  C CG2 . VAL   A 1 104 ? -9.67168  -9.21742  5.54443   1.000 16.19539  ? 104 VAL   A CG2 1 
ATOM   815  N N   . ARG   A 1 105 ? -6.26957  -9.74587  4.33068   1.000 18.81354  ? 105 ARG   A N   1 
ATOM   816  C CA  . ARG   A 1 105 ? -5.94814  -10.96609 3.61306   1.000 15.52725  ? 105 ARG   A CA  1 
ATOM   817  C C   . ARG   A 1 105 ? -6.34390  -12.10170 4.54592   1.000 15.28228  ? 105 ARG   A C   1 
ATOM   818  O O   . ARG   A 1 105 ? -5.83079  -12.17505 5.66362   1.000 15.74168  ? 105 ARG   A O   1 
ATOM   819  C CB  . ARG   A 1 105 ? -4.46318  -11.00425 3.24420   1.000 15.50570  ? 105 ARG   A CB  1 
ATOM   820  C CG  . ARG   A 1 105 ? -4.02888  -12.25915 2.51822   1.000 15.51572  ? 105 ARG   A CG  1 
ATOM   821  C CD  . ARG   A 1 105 ? -2.65527  -12.08531 1.90776   1.000 16.08202  ? 105 ARG   A CD  1 
ATOM   822  N NE  . ARG   A 1 105 ? -2.19803  -13.28342 1.20021   1.000 16.29495  ? 105 ARG   A NE  1 
ATOM   823  C CZ  . ARG   A 1 105 ? -2.50924  -13.56385 -0.06962  1.000 15.97092  ? 105 ARG   A CZ  1 
ATOM   824  N NH1 . ARG   A 1 105 ? -3.29895  -12.74526 -0.77373  1.000 15.38278  ? 105 ARG   A NH1 1 
ATOM   825  N NH2 . ARG   A 1 105 ? -2.02945  -14.65856 -0.64705  1.000 16.39196  ? 105 ARG   A NH2 1 
ATOM   826  N N   . ILE   A 1 106 ? -7.29057  -12.94018 4.11006   1.000 14.58609  ? 106 ILE   A N   1 
ATOM   827  C CA  . ILE   A 1 106 ? -7.90817  -13.96142 4.94933   1.000 15.85762  ? 106 ILE   A CA  1 
ATOM   828  C C   . ILE   A 1 106 ? -7.16938  -15.26536 4.72468   1.000 15.07767  ? 106 ILE   A C   1 
ATOM   829  O O   . ILE   A 1 106 ? -6.64245  -15.50519 3.64202   1.000 15.00114  ? 106 ILE   A O   1 
ATOM   830  C CB  . ILE   A 1 106 ? -9.42385  -14.16120 4.65956   1.000 14.14051  ? 106 ILE   A CB  1 
ATOM   831  C CG1 . ILE   A 1 106 ? -9.63073  -14.57757 3.18584   1.000 16.81890  ? 106 ILE   A CG1 1 
ATOM   832  C CG2 . ILE   A 1 106 ? -10.19564 -12.93457 4.99062   1.000 13.98176  ? 106 ILE   A CG2 1 
ATOM   833  C CD1 . ILE   A 1 106 ? -10.99297 -15.15861 2.83853   1.000 20.39964  ? 106 ILE   A CD1 1 
ATOM   834  N N   . GLN   A 1 107 ? -7.16585  -16.12521 5.76490   1.000 15.61660  ? 107 GLN   A N   1 
ATOM   835  C CA  . GLN   A 1 107 ? -6.70083  -17.50387 5.78291   1.000 20.05963  ? 107 GLN   A CA  1 
ATOM   836  C C   . GLN   A 1 107 ? -7.72613  -18.42759 5.12714   1.000 20.72855  ? 107 GLN   A C   1 
ATOM   837  O O   . GLN   A 1 107 ? -8.94714  -18.21208 5.25528   1.000 15.41542  ? 107 GLN   A O   1 
ATOM   838  C CB  . GLN   A 1 107 ? -6.45314  -17.98098 7.22507   1.000 17.60474  ? 107 GLN   A CB  1 
ATOM   839  C CG  . GLN   A 1 107 ? -5.10119  -17.57144 7.86416   1.000 24.29512  ? 107 GLN   A CG  1 
ATOM   840  C CD  . GLN   A 1 107 ? -3.89274  -17.88392 6.97641   1.000 25.33796  ? 107 GLN   A CD  1 
ATOM   841  O OE1 . GLN   A 1 107 ? -3.46458  -19.03585 6.83852   1.000 28.64929  ? 107 GLN   A OE1 1 
ATOM   842  N NE2 . GLN   A 1 107 ? -3.34922  -16.84657 6.36102   1.000 27.72988  ? 107 GLN   A NE2 1 
ATOM   843  N N   . PRO   A 1 108 ? -7.24440  -19.46386 4.42182   1.000 22.19986  ? 108 PRO   A N   1 
ATOM   844  C CA  . PRO   A 1 108 ? -8.13854  -20.55059 3.98678   1.000 18.99016  ? 108 PRO   A CA  1 
ATOM   845  C C   . PRO   A 1 108 ? -9.00960  -20.99819 5.14113   1.000 19.14258  ? 108 PRO   A C   1 
ATOM   846  O O   . PRO   A 1 108 ? -8.59712  -21.03298 6.31019   1.000 18.79783  ? 108 PRO   A O   1 
ATOM   847  C CB  . PRO   A 1 108 ? -7.19230  -21.67784 3.55790   1.000 20.46214  ? 108 PRO   A CB  1 
ATOM   848  C CG  . PRO   A 1 108 ? -5.81259  -21.25154 3.97934   1.000 18.69180  ? 108 PRO   A CG  1 
ATOM   849  C CD  . PRO   A 1 108 ? -5.84049  -19.74382 4.12295   1.000 22.54219  ? 108 PRO   A CD  1 
ATOM   850  N N   . GLY   A 1 109 ? -10.25486 -21.28211 4.81966   1.000 18.97902  ? 109 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 109 ? -11.20377 -21.54209 5.85206   1.000 16.11274  ? 109 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 109 ? -12.09880 -20.35032 6.13732   1.000 21.01972  ? 109 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 109 ? -13.31237 -20.54634 6.44859   1.000 23.98618  ? 109 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 110 ? -11.55401 -19.11603 6.15448   1.000 23.82354  ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? -12.56844 -18.07796 6.32589   1.000 24.98217  ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? -13.55604 -17.96837 5.17435   1.000 23.51285  ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? -13.35138 -18.44979 4.07036   1.000 21.19281  ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? -12.14107 -16.64393 6.47585   1.000 23.51322  ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? -11.41787 -16.07125 7.66661   1.000 35.05475  ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? -11.76163 -16.58829 9.07725   1.000 38.75281  ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? -10.88597 -16.38210 9.87149   1.000 53.28595  ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? -12.53010 -17.68696 9.15628   1.000 42.44567  ? 110 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? -14.71080 -17.47951 5.52060   1.000 17.07316  ? 111 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? -15.74417 -17.22700 4.55937   1.000 19.04411  ? 111 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? -15.81826 -15.72813 4.36522   1.000 15.48738  ? 111 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? -15.34323 -14.93370 5.19400   1.000 14.21104  ? 111 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? -17.09188 -17.77029 5.05178   1.000 18.30552  ? 111 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? -17.40613 -17.08473 6.26065   1.000 19.85423  ? 111 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? -17.02912 -19.25577 5.29772   1.000 17.02777  ? 111 THR   A CG2 1 
ATOM   870  N N   . PHE   A 1 112 ? -16.48413 -15.36156 3.28077   1.000 17.00647  ? 112 PHE   A N   1 
ATOM   871  C CA  . PHE   A 1 112 ? -16.81839 -13.97432 3.00400   1.000 16.20622  ? 112 PHE   A CA  1 
ATOM   872  C C   . PHE   A 1 112 ? -18.05601 -14.00508 2.12750   1.000 19.39165  ? 112 PHE   A C   1 
ATOM   873  O O   . PHE   A 1 112 ? -18.55942 -15.08244 1.76262   1.000 17.69419  ? 112 PHE   A O   1 
ATOM   874  C CB  . PHE   A 1 112 ? -15.64426 -13.21595 2.35938   1.000 13.36459  ? 112 PHE   A CB  1 
ATOM   875  C CG  . PHE   A 1 112 ? -15.06861 -13.90602 1.14485   1.000 12.72411  ? 112 PHE   A CG  1 
ATOM   876  C CD1 . PHE   A 1 112 ? -14.15626 -14.94904 1.28847   1.000 14.23727  ? 112 PHE   A CD1 1 
ATOM   877  C CD2 . PHE   A 1 112 ? -15.44521 -13.53093 -0.12970  1.000 12.66401  ? 112 PHE   A CD2 1 
ATOM   878  C CE1 . PHE   A 1 112 ? -13.62111 -15.60651 0.15596   1.000 17.46941  ? 112 PHE   A CE1 1 
ATOM   879  C CE2 . PHE   A 1 112 ? -14.91940 -14.17260 -1.25059  1.000 13.58459  ? 112 PHE   A CE2 1 
ATOM   880  C CZ  . PHE   A 1 112 ? -14.01709 -15.20324 -1.12454  1.000 12.58215  ? 112 PHE   A CZ  1 
ATOM   881  N N   . SER   A 1 113 ? -18.56894 -12.80552 1.84731   1.000 15.56233  ? 113 SER   A N   1 
ATOM   882  C CA  . SER   A 1 113 ? -19.70362 -12.58292 0.97311   1.000 16.02212  ? 113 SER   A CA  1 
ATOM   883  C C   . SER   A 1 113 ? -19.19396 -11.96656 -0.32328  1.000 18.50331  ? 113 SER   A C   1 
ATOM   884  O O   . SER   A 1 113 ? -18.27876 -11.14410 -0.29731  1.000 14.70430  ? 113 SER   A O   1 
ATOM   885  C CB  . SER   A 1 113 ? -20.74195 -11.63898 1.62116   1.000 21.70409  ? 113 SER   A CB  1 
ATOM   886  O OG  . SER   A 1 113 ? -21.45008 -12.25989 2.68503   1.000 18.24212  ? 113 SER   A OG  1 
ATOM   887  N N   . VAL   A 1 114 ? -19.79303 -12.36380 -1.45183  1.000 17.94508  ? 114 VAL   A N   1 
ATOM   888  C CA  . VAL   A 1 114 ? -19.41357 -11.89246 -2.77865  1.000 16.82767  ? 114 VAL   A CA  1 
ATOM   889  C C   . VAL   A 1 114 ? -20.59688 -11.13188 -3.36461  1.000 15.97602  ? 114 VAL   A C   1 
ATOM   890  O O   . VAL   A 1 114 ? -21.72211 -11.63567 -3.39035  1.000 17.57854  ? 114 VAL   A O   1 
ATOM   891  C CB  . VAL   A 1 114 ? -19.00554 -13.04966 -3.72153  1.000 19.24148  ? 114 VAL   A CB  1 
ATOM   892  C CG1 . VAL   A 1 114 ? -18.73786 -12.51610 -5.15347  1.000 13.18784  ? 114 VAL   A CG1 1 
ATOM   893  C CG2 . VAL   A 1 114 ? -17.81182 -13.90883 -3.15268  1.000 13.42321  ? 114 VAL   A CG2 1 
ATOM   894  N N   . LEU   A 1 115 ? -20.33321 -9.95066  -3.86943  1.000 16.29355  ? 115 LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 115 ? -21.30973 -9.20243  -4.63918  1.000 14.40232  ? 115 LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 115 ? -20.91786 -9.31411  -6.12094  1.000 16.04664  ? 115 LEU   A C   1 
ATOM   897  O O   . LEU   A 1 115 ? -19.96154 -8.68066  -6.58678  1.000 19.97182  ? 115 LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 115 ? -21.35693 -7.77433  -4.11286  1.000 14.21318  ? 115 LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 115 ? -22.14227 -6.80246  -4.94434  1.000 15.12268  ? 115 LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 115 ? -23.67504 -7.10534  -4.84876  1.000 18.51109  ? 115 LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 115 ? -21.76646 -5.35902  -4.54373  1.000 16.05613  ? 115 LEU   A CD2 1 
ATOM   902  N N   . ALA   A 1 116 ? -21.63236 -10.16342 -6.84803  1.000 17.44682  ? 116 ALA   A N   1 
ATOM   903  C CA  . ALA   A 1 116 ? -21.38864 -10.36086 -8.27168  1.000 20.87227  ? 116 ALA   A CA  1 
ATOM   904  C C   . ALA   A 1 116 ? -21.91875 -9.17474  -9.07007  1.000 22.99765  ? 116 ALA   A C   1 
ATOM   905  O O   . ALA   A 1 116 ? -23.08791 -8.77523  -8.92360  1.000 19.77006  ? 116 ALA   A O   1 
ATOM   906  C CB  . ALA   A 1 116 ? -22.03869 -11.65698 -8.76423  1.000 19.70005  ? 116 ALA   A CB  1 
ATOM   907  N N   . CYS   A 1 117 ? -21.05946 -8.64564  -9.93911  1.000 17.64299  ? 117 CYS   A N   1 
ATOM   908  C CA  . CYS   A 1 117 ? -21.31146 -7.41575  -10.65862 1.000 22.50316  ? 117 CYS   A CA  1 
ATOM   909  C C   . CYS   A 1 117 ? -20.92844 -7.56834  -12.12320 1.000 26.18699  ? 117 CYS   A C   1 
ATOM   910  O O   . CYS   A 1 117 ? -20.03967 -8.34138  -12.49086 1.000 23.72329  ? 117 CYS   A O   1 
ATOM   911  C CB  . CYS   A 1 117 ? -20.54078 -6.23837  -10.04754 1.000 24.11243  ? 117 CYS   A CB  1 
ATOM   912  S SG  . CYS   A 1 117 ? -21.10900 -5.71134  -8.40959  1.000 27.96974  ? 117 CYS   A SG  1 
ATOM   913  N N   . TYR   A 1 118 ? -21.62831 -6.80496  -12.95467 1.000 29.84474  ? 118 TYR   A N   1 
ATOM   914  C CA  . TYR   A 1 118 ? -21.43894 -6.78756  -14.39584 1.000 28.43995  ? 118 TYR   A CA  1 
ATOM   915  C C   . TYR   A 1 118 ? -21.65428 -5.34722  -14.83189 1.000 33.52277  ? 118 TYR   A C   1 
ATOM   916  O O   . TYR   A 1 118 ? -22.69830 -4.75763  -14.52212 1.000 34.87644  ? 118 TYR   A O   1 
ATOM   917  C CB  . TYR   A 1 118 ? -22.40440 -7.76610  -15.09561 1.000 27.93900  ? 118 TYR   A CB  1 
ATOM   918  C CG  . TYR   A 1 118 ? -22.16460 -9.19695  -14.63244 1.000 29.59451  ? 118 TYR   A CG  1 
ATOM   919  C CD1 . TYR   A 1 118 ? -22.94261 -9.77137  -13.62443 1.000 32.25733  ? 118 TYR   A CD1 1 
ATOM   920  C CD2 . TYR   A 1 118 ? -21.09811 -9.94505  -15.14055 1.000 26.09718  ? 118 TYR   A CD2 1 
ATOM   921  C CE1 . TYR   A 1 118 ? -22.68878 -11.07106 -13.16476 1.000 26.39298  ? 118 TYR   A CE1 1 
ATOM   922  C CE2 . TYR   A 1 118 ? -20.84559 -11.23258 -14.69292 1.000 24.07143  ? 118 TYR   A CE2 1 
ATOM   923  C CZ  . TYR   A 1 118 ? -21.64006 -11.79240 -13.70550 1.000 24.76213  ? 118 TYR   A CZ  1 
ATOM   924  O OH  . TYR   A 1 118 ? -21.37595 -13.07483 -13.25469 1.000 22.67986  ? 118 TYR   A OH  1 
ATOM   925  N N   . ASN   A 1 119 ? -20.63756 -4.75900  -15.47394 1.000 32.22550  ? 119 ASN   A N   1 
ATOM   926  C CA  . ASN   A 1 119 ? -20.70893 -3.38150  -15.96979 1.000 33.73523  ? 119 ASN   A CA  1 
ATOM   927  C C   . ASN   A 1 119 ? -20.84381 -2.36835  -14.83154 1.000 34.00485  ? 119 ASN   A C   1 
ATOM   928  O O   . ASN   A 1 119 ? -21.41214 -1.28539  -15.00850 1.000 33.13855  ? 119 ASN   A O   1 
ATOM   929  C CB  . ASN   A 1 119 ? -21.85588 -3.23109  -16.96387 1.000 31.20212  ? 119 ASN   A CB  1 
ATOM   930  C CG  . ASN   A 1 119 ? -21.76121 -4.21837  -18.09788 1.000 40.33324  ? 119 ASN   A CG  1 
ATOM   931  O OD1 . ASN   A 1 119 ? -20.92265 -4.06664  -18.99830 1.000 46.98152  ? 119 ASN   A OD1 1 
ATOM   932  N ND2 . ASN   A 1 119 ? -22.60626 -5.25213  -18.06156 1.000 37.45616  ? 119 ASN   A ND2 1 
ATOM   933  N N   . GLY   A 1 120 ? -20.32584 -2.72036  -13.65210 1.000 33.31268  ? 120 GLY   A N   1 
ATOM   934  C CA  . GLY   A 1 120 ? -20.45403 -1.91024  -12.45899 1.000 30.06560  ? 120 GLY   A CA  1 
ATOM   935  C C   . GLY   A 1 120 ? -21.77467 -2.03107  -11.73397 1.000 30.23465  ? 120 GLY   A C   1 
ATOM   936  O O   . GLY   A 1 120 ? -21.96514 -1.36160  -10.70924 1.000 30.87862  ? 120 GLY   A O   1 
ATOM   937  N N   . SER   A 1 121 ? -22.69161 -2.85516  -12.22822 1.000 34.14175  ? 121 SER   A N   1 
ATOM   938  C CA  . SER   A 1 121 ? -24.01782 -2.96958  -11.65484 1.000 35.06174  ? 121 SER   A CA  1 
ATOM   939  C C   . SER   A 1 121 ? -24.12122 -4.28762  -10.92236 1.000 36.48921  ? 121 SER   A C   1 
ATOM   940  O O   . SER   A 1 121 ? -24.00599 -5.35223  -11.55365 1.000 34.24465  ? 121 SER   A O   1 
ATOM   941  C CB  . SER   A 1 121 ? -25.09851 -2.88058  -12.72805 1.000 46.05030  ? 121 SER   A CB  1 
ATOM   942  O OG  . SER   A 1 121 ? -25.24838 -1.55239  -13.19192 1.000 52.83347  ? 121 SER   A OG  1 
ATOM   943  N N   . PRO   A 1 122 ? -24.34573 -4.26714  -9.61200  1.000 30.69048  ? 122 PRO   A N   1 
ATOM   944  C CA  . PRO   A 1 122 ? -24.42500 -5.52653  -8.86721  1.000 28.22559  ? 122 PRO   A CA  1 
ATOM   945  C C   . PRO   A 1 122 ? -25.57385 -6.39013  -9.36843  1.000 32.92518  ? 122 PRO   A C   1 
ATOM   946  O O   . PRO   A 1 122 ? -26.67798 -5.90220  -9.62362  1.000 41.32760  ? 122 PRO   A O   1 
ATOM   947  C CB  . PRO   A 1 122 ? -24.62714 -5.06367  -7.41755  1.000 26.19340  ? 122 PRO   A CB  1 
ATOM   948  C CG  . PRO   A 1 122 ? -24.03913 -3.69366  -7.37287  1.000 26.49751  ? 122 PRO   A CG  1 
ATOM   949  C CD  . PRO   A 1 122 ? -24.42141 -3.09837  -8.72239  1.000 27.44503  ? 122 PRO   A CD  1 
ATOM   950  N N   . SER   A 1 123 ? -25.27984 -7.67944  -9.54344  1.000 30.79643  ? 123 SER   A N   1 
ATOM   951  C CA  . SER   A 1 123 ? -26.22209 -8.69455  -9.99801  1.000 34.62413  ? 123 SER   A CA  1 
ATOM   952  C C   . SER   A 1 123 ? -26.80257 -9.51251  -8.84609  1.000 31.61905  ? 123 SER   A C   1 
ATOM   953  O O   . SER   A 1 123 ? -28.01711 -9.75182  -8.80469  1.000 33.71015  ? 123 SER   A O   1 
ATOM   954  C CB  . SER   A 1 123 ? -25.51435 -9.61328  -11.00225 1.000 37.34982  ? 123 SER   A CB  1 
ATOM   955  O OG  . SER   A 1 123 ? -26.40294 -10.48510 -11.67042 1.000 53.30551  ? 123 SER   A OG  1 
ATOM   956  N N   . GLY   A 1 124 ? -25.95187 -9.94371  -7.91123  1.000 25.64948  ? 124 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 124 ? -26.35729 -10.79998 -6.80768  1.000 23.29451  ? 124 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 124 ? -25.29779 -10.86394 -5.72547  1.000 20.77698  ? 124 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 124 ? -24.15340 -10.43463 -5.90593  1.000 16.71481  ? 124 GLY   A O   1 
ATOM   960  N N   . VAL   A 1 125 ? -25.70453 -11.40872 -4.58330  1.000 18.42021  ? 125 VAL   A N   1 
ATOM   961  C CA  . VAL   A 1 125 ? -24.83112 -11.53959 -3.41667  1.000 17.54168  ? 125 VAL   A CA  1 
ATOM   962  C C   . VAL   A 1 125 ? -24.97085 -12.94562 -2.83353  1.000 17.73350  ? 125 VAL   A C   1 
ATOM   963  O O   . VAL   A 1 125 ? -26.08831 -13.40795 -2.56927  1.000 16.96594  ? 125 VAL   A O   1 
ATOM   964  C CB  . VAL   A 1 125 ? -25.14174 -10.45692 -2.36412  1.000 19.09776  ? 125 VAL   A CB  1 
ATOM   965  C CG1 . VAL   A 1 125 ? -26.65219 -10.38487 -2.11377  1.000 16.28661  ? 125 VAL   A CG1 1 
ATOM   966  C CG2 . VAL   A 1 125 ? -24.40959 -10.75126 -1.04774  1.000 14.35919  ? 125 VAL   A CG2 1 
ATOM   967  N N   . TYR   A 1 126 ? -23.84089 -13.64587 -2.68804  1.000 16.73655  ? 126 TYR   A N   1 
ATOM   968  C CA  . TYR   A 1 126 ? -23.81427 -14.98598 -2.09455  1.000 18.48928  ? 126 TYR   A CA  1 
ATOM   969  C C   . TYR   A 1 126 ? -22.59958 -15.12607 -1.17294  1.000 19.25873  ? 126 TYR   A C   1 
ATOM   970  O O   . TYR   A 1 126 ? -21.65754 -14.31355 -1.20617  1.000 15.59225  ? 126 TYR   A O   1 
ATOM   971  C CB  . TYR   A 1 126 ? -23.79284 -16.09943 -3.16662  1.000 18.11596  ? 126 TYR   A CB  1 
ATOM   972  C CG  . TYR   A 1 126 ? -22.73040 -15.87126 -4.23167  1.000 19.39611  ? 126 TYR   A CG  1 
ATOM   973  C CD1 . TYR   A 1 126 ? -21.42540 -16.32121 -4.06522  1.000 19.25888  ? 126 TYR   A CD1 1 
ATOM   974  C CD2 . TYR   A 1 126 ? -23.03550 -15.17142 -5.38846  1.000 20.10413  ? 126 TYR   A CD2 1 
ATOM   975  C CE1 . TYR   A 1 126 ? -20.45902 -16.09594 -5.05056  1.000 18.20930  ? 126 TYR   A CE1 1 
ATOM   976  C CE2 . TYR   A 1 126 ? -22.08475 -14.91820 -6.34562  1.000 19.89251  ? 126 TYR   A CE2 1 
ATOM   977  C CZ  . TYR   A 1 126 ? -20.80466 -15.37179 -6.17483  1.000 18.11165  ? 126 TYR   A CZ  1 
ATOM   978  O OH  . TYR   A 1 126 ? -19.91510 -15.11749 -7.18671  1.000 19.30780  ? 126 TYR   A OH  1 
ATOM   979  N N   . GLN   A 1 127 ? -22.61738 -16.21660 -0.39086  1.000 16.61353  ? 127 GLN   A N   1 
ATOM   980  C CA  . GLN   A 1 127 ? -21.62326 -16.52614 0.63757   1.000 17.03568  ? 127 GLN   A CA  1 
ATOM   981  C C   . GLN   A 1 127 ? -20.63654 -17.56963 0.11152   1.000 20.80487  ? 127 GLN   A C   1 
ATOM   982  O O   . GLN   A 1 127 ? -21.05785 -18.63194 -0.36295  1.000 27.76363  ? 127 GLN   A O   1 
ATOM   983  C CB  . GLN   A 1 127 ? -22.32984 -17.04721 1.90602   1.000 15.49137  ? 127 GLN   A CB  1 
ATOM   984  C CG  . GLN   A 1 127 ? -21.52451 -16.97159 3.17743   1.000 17.19442  ? 127 GLN   A CG  1 
ATOM   985  C CD  . GLN   A 1 127 ? -21.21629 -15.52468 3.54946   1.000 19.09789  ? 127 GLN   A CD  1 
ATOM   986  O OE1 . GLN   A 1 127 ? -21.85629 -14.60237 3.03202   1.000 22.87996  ? 127 GLN   A OE1 1 
ATOM   987  N NE2 . GLN   A 1 127 ? -20.21476 -15.31270 4.39342   1.000 14.80251  ? 127 GLN   A NE2 1 
ATOM   988  N N   . CYS   A 1 128 ? -19.33748 -17.27134 0.20696   1.000 16.17789  ? 128 CYS   A N   1 
ATOM   989  C CA  . CYS   A 1 128 ? -18.23730 -18.14253 -0.21969  1.000 20.94261  ? 128 CYS   A CA  1 
ATOM   990  C C   . CYS   A 1 128 ? -17.28513 -18.46092 0.92953   1.000 14.61894  ? 128 CYS   A C   1 
ATOM   991  O O   . CYS   A 1 128 ? -17.10677 -17.66009 1.83979   1.000 13.14505  ? 128 CYS   A O   1 
ATOM   992  C CB  . CYS   A 1 128 ? -17.37085 -17.48792 -1.32688  1.000 15.41052  ? 128 CYS   A CB  1 
ATOM   993  S SG  . CYS   A 1 128 ? -17.99727 -17.75713 -3.00077  1.000 36.36574  ? 128 CYS   A SG  1 
ATOM   994  N N   . ALA   A 1 129 ? -16.61223 -19.60500 0.84076   1.000 15.90223  ? 129 ALA   A N   1 
ATOM   995  C CA  . ALA   A 1 129 ? -15.40162 -19.83109 1.62797   1.000 21.01563  ? 129 ALA   A CA  1 
ATOM   996  C C   . ALA   A 1 129 ? -14.15352 -19.77402 0.74261   1.000 15.08811  ? 129 ALA   A C   1 
ATOM   997  O O   . ALA   A 1 129 ? -14.19578 -20.05716 -0.45988  1.000 15.43336  ? 129 ALA   A O   1 
ATOM   998  C CB  . ALA   A 1 129 ? -15.44171 -21.17298 2.36501   1.000 17.55766  ? 129 ALA   A CB  1 
ATOM   999  N N   . MET   A 1 130 ? -13.04168 -19.39566 1.34094   1.000 14.29011  ? 130 MET   A N   1 
ATOM   1000 C CA  . MET   A 1 130 ? -11.75519 -19.57960 0.68896   1.000 14.51960  ? 130 MET   A CA  1 
ATOM   1001 C C   . MET   A 1 130 ? -11.33842 -21.02015 0.94413   1.000 18.73970  ? 130 MET   A C   1 
ATOM   1002 O O   . MET   A 1 130 ? -11.04924 -21.39034 2.08711   1.000 21.11687  ? 130 MET   A O   1 
ATOM   1003 C CB  . MET   A 1 130 ? -10.73809 -18.58693 1.24116   1.000 18.99952  ? 130 MET   A CB  1 
ATOM   1004 C CG  . MET   A 1 130 ? -9.31110  -18.87059 0.85605   1.000 19.69143  ? 130 MET   A CG  1 
ATOM   1005 S SD  . MET   A 1 130 ? -9.13139  -18.47547 -0.88099  1.000 23.01352  ? 130 MET   A SD  1 
ATOM   1006 C CE  . MET   A 1 130 ? -9.67727  -16.75787 -0.89769  1.000 17.41818  ? 130 MET   A CE  1 
ATOM   1007 N N   . ARG   A 1 131 ? -11.35544 -21.85399 -0.09678  1.000 19.40960  ? 131 ARG   A N   1 
ATOM   1008 C CA  . ARG   A 1 131 ? -11.08759 -23.26648 0.09057   1.000 20.01834  ? 131 ARG   A CA  1 
ATOM   1009 C C   . ARG   A 1 131 ? -9.62829  -23.46479 0.52596   1.000 24.42011  ? 131 ARG   A C   1 
ATOM   1010 O O   . ARG   A 1 131 ? -8.82045  -22.54865 0.41979   1.000 22.97955  ? 131 ARG   A O   1 
ATOM   1011 C CB  . ARG   A 1 131 ? -11.38064 -24.02758 -1.19428  1.000 22.30161  ? 131 ARG   A CB  1 
ATOM   1012 C CG  . ARG   A 1 131 ? -12.72931 -23.75749 -1.83537  1.000 23.78024  ? 131 ARG   A CG  1 
ATOM   1013 C CD  . ARG   A 1 131 ? -13.91580 -24.26324 -1.01374  1.000 24.10231  ? 131 ARG   A CD  1 
ATOM   1014 N NE  . ARG   A 1 131 ? -13.67705 -25.58706 -0.46589  1.000 25.65708  ? 131 ARG   A NE  1 
ATOM   1015 C CZ  . ARG   A 1 131 ? -14.30786 -26.06050 0.60306   1.000 27.25968  ? 131 ARG   A CZ  1 
ATOM   1016 N NH1 . ARG   A 1 131 ? -15.21200 -25.30484 1.21571   1.000 25.59465  ? 131 ARG   A NH1 1 
ATOM   1017 N NH2 . ARG   A 1 131 ? -14.03608 -27.27535 1.06853   1.000 26.86002  ? 131 ARG   A NH2 1 
ATOM   1018 N N   . PRO   A 1 132 ? -9.27965  -24.63083 1.08745   1.000 25.16146  ? 132 PRO   A N   1 
ATOM   1019 C CA  . PRO   A 1 132 ? -7.86980  -24.85296 1.44862   1.000 28.02395  ? 132 PRO   A CA  1 
ATOM   1020 C C   . PRO   A 1 132 ? -6.90835  -24.69947 0.28195   1.000 26.08326  ? 132 PRO   A C   1 
ATOM   1021 O O   . PRO   A 1 132 ? -5.74887  -24.33469 0.50608   1.000 28.18380  ? 132 PRO   A O   1 
ATOM   1022 C CB  . PRO   A 1 132 ? -7.87430  -26.28324 1.99882   1.000 22.95032  ? 132 PRO   A CB  1 
ATOM   1023 C CG  . PRO   A 1 132 ? -9.20277  -26.39060 2.61037   1.000 29.48252  ? 132 PRO   A CG  1 
ATOM   1024 C CD  . PRO   A 1 132 ? -10.15032 -25.63350 1.71897   1.000 21.22200  ? 132 PRO   A CD  1 
ATOM   1025 N N   . ASN   A 1 133 ? -7.35270  -24.93221 -0.95327  1.000 26.44473  ? 133 ASN   A N   1 
ATOM   1026 C CA  . ASN   A 1 133 ? -6.51162  -24.74881 -2.12438  1.000 24.24270  ? 133 ASN   A CA  1 
ATOM   1027 C C   . ASN   A 1 133 ? -6.54430  -23.31377 -2.66640  1.000 24.98326  ? 133 ASN   A C   1 
ATOM   1028 O O   . ASN   A 1 133 ? -6.22150  -23.10312 -3.83909  1.000 23.24146  ? 133 ASN   A O   1 
ATOM   1029 C CB  . ASN   A 1 133 ? -6.93284  -25.73521 -3.21748  1.000 29.03645  ? 133 ASN   A CB  1 
ATOM   1030 C CG  . ASN   A 1 133 ? -8.32448  -25.43406 -3.76782  1.000 27.54164  ? 133 ASN   A CG  1 
ATOM   1031 O OD1 . ASN   A 1 133 ? -9.11366  -24.75814 -3.12313  1.000 26.00926  ? 133 ASN   A OD1 1 
ATOM   1032 N ND2 . ASN   A 1 133 ? -8.61698  -25.92595 -4.96248  1.000 27.35569  ? 133 ASN   A ND2 1 
ATOM   1033 N N   . PHE   A 1 134 ? -6.96394  -22.33515 -1.85524  1.000 24.01310  ? 134 PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 134 ? -7.02465  -20.91739 -2.25535  1.000 22.28537  ? 134 PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 134 ? -7.77964  -20.69831 -3.56787  1.000 21.26594  ? 134 PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 134 ? -7.42326  -19.82785 -4.36477  1.000 22.52998  ? 134 PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 134 ? -5.62625  -20.29167 -2.35625  1.000 19.79254  ? 134 PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 134 ? -4.84178  -20.33593 -1.07278  1.000 19.27263  ? 134 PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 134 ? -5.03293  -19.37057 -0.09794  1.000 19.83883  ? 134 PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 134 ? -3.94292  -21.37512 -0.82315  1.000 18.61037  ? 134 PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 134 ? -4.32317  -19.42106 1.11930   1.000 20.13256  ? 134 PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 134 ? -3.22406  -21.44238 0.38538   1.000 18.42588  ? 134 PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 134 ? -3.42667  -20.45111 1.36217   1.000 20.37957  ? 134 PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 135 ? -8.81960  -21.49606 -3.80680  1.000 22.17747  ? 135 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 135 ? -9.82438  -21.18485 -4.82272  1.000 25.59254  ? 135 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 135 ? -11.15509 -20.93631 -4.12115  1.000 20.03550  ? 135 THR   A C   1 
ATOM   1047 O O   . THR   A 1 135 ? -11.32121 -21.22175 -2.93180  1.000 15.65019  ? 135 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 135 ? -10.02300 -22.32031 -5.84145  1.000 20.65025  ? 135 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 135 ? -10.46710 -23.47988 -5.13687  1.000 22.31771  ? 135 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 135 ? -8.75585  -22.65585 -6.62953  1.000 20.70978  ? 135 THR   A CG2 1 
ATOM   1051 N N   . ILE   A 1 136 ? -12.12658 -20.42858 -4.87009  1.000 18.22840  ? 136 ILE   A N   1 
ATOM   1052 C CA  . ILE   A 1 136 ? -13.48403 -20.30237 -4.34924  1.000 24.77531  ? 136 ILE   A CA  1 
ATOM   1053 C C   . ILE   A 1 136 ? -14.47595 -20.92032 -5.32426  1.000 20.50633  ? 136 ILE   A C   1 
ATOM   1054 O O   . ILE   A 1 136 ? -14.43116 -20.65055 -6.52784  1.000 18.70570  ? 136 ILE   A O   1 
ATOM   1055 C CB  . ILE   A 1 136 ? -13.86485 -18.84085 -4.03923  1.000 17.46663  ? 136 ILE   A CB  1 
ATOM   1056 C CG1 . ILE   A 1 136 ? -13.73710 -17.98156 -5.27803  1.000 20.38395  ? 136 ILE   A CG1 1 
ATOM   1057 C CG2 . ILE   A 1 136 ? -13.00739 -18.30998 -2.89031  1.000 18.00429  ? 136 ILE   A CG2 1 
ATOM   1058 C CD1 . ILE   A 1 136 ? -14.38729 -16.63571 -5.11046  1.000 24.21267  ? 136 ILE   A CD1 1 
ATOM   1059 N N   . LYS   A 1 137 ? -15.37434 -21.74353 -4.79631  1.000 22.80396  ? 137 LYS   A N   1 
ATOM   1060 C CA  . LYS   A 1 137 ? -16.52982 -22.23105 -5.54776  1.000 21.21323  ? 137 LYS   A CA  1 
ATOM   1061 C C   . LYS   A 1 137 ? -17.54181 -21.09044 -5.63831  1.000 23.57043  ? 137 LYS   A C   1 
ATOM   1062 O O   . LYS   A 1 137 ? -18.46022 -20.96889 -4.82539  1.000 27.05096  ? 137 LYS   A O   1 
ATOM   1063 C CB  . LYS   A 1 137 ? -17.11698 -23.46093 -4.87277  1.000 19.52824  ? 137 LYS   A CB  1 
ATOM   1064 C CG  . LYS   A 1 137 ? -16.16411 -24.62777 -4.75608  1.000 27.09361  ? 137 LYS   A CG  1 
ATOM   1065 C CD  . LYS   A 1 137 ? -16.84184 -25.86285 -4.17153  1.000 29.87860  ? 137 LYS   A CD  1 
ATOM   1066 C CE  . LYS   A 1 137 ? -15.92086 -27.07661 -4.28917  1.000 37.14790  ? 137 LYS   A CE  1 
ATOM   1067 N NZ  . LYS   A 1 137 ? -16.09036 -28.04669 -3.15918  1.000 40.68892  ? 137 LYS   A NZ  1 
ATOM   1068 N N   . GLY   A 1 138 ? -17.36631 -20.22731 -6.63609  1.000 25.09056  ? 138 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 138 ? -18.21811 -19.07859 -6.82751  1.000 23.68365  ? 138 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 138 ? -19.12570 -19.22849 -8.03869  1.000 24.27026  ? 138 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 138 ? -19.17382 -20.26382 -8.70191  1.000 26.40919  ? 138 GLY   A O   1 
ATOM   1072 N N   . SER   A 1 139 ? -19.87298 -18.15587 -8.30251  1.000 21.81448  ? 139 SER   A N   1 
ATOM   1073 C CA  . SER   A 1 139 ? -20.72808 -18.06081 -9.48009  1.000 24.41565  ? 139 SER   A CA  1 
ATOM   1074 C C   . SER   A 1 139 ? -20.35800 -16.78763 -10.23152 1.000 22.71162  ? 139 SER   A C   1 
ATOM   1075 O O   . SER   A 1 139 ? -20.68980 -15.67609 -9.79294  1.000 20.34546  ? 139 SER   A O   1 
ATOM   1076 C CB  . SER   A 1 139 ? -22.20354 -18.07040 -9.10612  1.000 17.46288  ? 139 SER   A CB  1 
ATOM   1077 O OG  . SER   A 1 139 ? -23.00444 -17.89899 -10.26550 1.000 17.50615  ? 139 SER   A OG  1 
ATOM   1078 N N   . PHE   A 1 140 ? -19.69985 -16.95804 -11.37516 1.000 19.60543  ? 140 PHE   A N   1 
ATOM   1079 C CA  . PHE   A 1 140 ? -19.08176 -15.84845 -12.08063 1.000 21.49760  ? 140 PHE   A CA  1 
ATOM   1080 C C   . PHE   A 1 140 ? -19.17914 -16.07007 -13.57180 1.000 23.26070  ? 140 PHE   A C   1 
ATOM   1081 O O   . PHE   A 1 140 ? -18.77891 -17.12814 -14.06400 1.000 26.13461  ? 140 PHE   A O   1 
ATOM   1082 C CB  . PHE   A 1 140 ? -17.61621 -15.71233 -11.68264 1.000 23.04227  ? 140 PHE   A CB  1 
ATOM   1083 C CG  . PHE   A 1 140 ? -17.43844 -15.13334 -10.34097 1.000 19.36918  ? 140 PHE   A CG  1 
ATOM   1084 C CD1 . PHE   A 1 140 ? -18.03561 -13.93746 -10.02876 1.000 17.38721  ? 140 PHE   A CD1 1 
ATOM   1085 C CD2 . PHE   A 1 140 ? -16.71804 -15.79994 -9.37974  1.000 18.53029  ? 140 PHE   A CD2 1 
ATOM   1086 C CE1 . PHE   A 1 140 ? -17.89848 -13.40511 -8.78850  1.000 19.59862  ? 140 PHE   A CE1 1 
ATOM   1087 C CE2 . PHE   A 1 140 ? -16.56087 -15.26235 -8.13535  1.000 18.93834  ? 140 PHE   A CE2 1 
ATOM   1088 C CZ  . PHE   A 1 140 ? -17.15056 -14.07402 -7.83011  1.000 19.85490  ? 140 PHE   A CZ  1 
ATOM   1089 N N   . LEU   A 1 141 ? -19.70430 -15.07916 -14.28127 1.000 23.71979  ? 141 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 141 ? -19.81341 -15.12850 -15.72926 1.000 26.27645  ? 141 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 141 ? -18.80174 -14.16381 -16.32527 1.000 24.76000  ? 141 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 141 ? -18.01520 -13.54615 -15.61240 1.000 26.94481  ? 141 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 141 ? -21.23307 -14.79745 -16.18669 1.000 22.33251  ? 141 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 141 ? -22.30900 -15.84883 -15.89684 1.000 34.80345  ? 141 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 141 ? -23.49720 -15.64660 -16.83657 1.000 39.39055  ? 141 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 141 ? -21.79665 -17.27776 -15.96538 1.000 21.29207  ? 141 LEU   A CD2 1 
ATOM   1097 N N   . ASN   A 1 142 ? -18.81831 -14.04978 -17.64610 1.000 24.76847  ? 142 ASN   A N   1 
ATOM   1098 C CA  . ASN   A 1 142 ? -17.95566 -13.09105 -18.31335 1.000 25.69521  ? 142 ASN   A CA  1 
ATOM   1099 C C   . ASN   A 1 142 ? -18.19101 -11.70075 -17.73754 1.000 26.75829  ? 142 ASN   A C   1 
ATOM   1100 O O   . ASN   A 1 142 ? -19.27030 -11.39591 -17.21755 1.000 26.04846  ? 142 ASN   A O   1 
ATOM   1101 C CB  . ASN   A 1 142 ? -18.21834 -13.11689 -19.81708 1.000 27.46296  ? 142 ASN   A CB  1 
ATOM   1102 C CG  . ASN   A 1 142 ? -17.39395 -14.18811 -20.52878 1.000 37.86130  ? 142 ASN   A CG  1 
ATOM   1103 O OD1 . ASN   A 1 142 ? -16.31352 -14.57417 -20.05178 1.000 31.30947  ? 142 ASN   A OD1 1 
ATOM   1104 N ND2 . ASN   A 1 142 ? -17.89859 -14.67872 -21.67201 1.000 29.51822  ? 142 ASN   A ND2 1 
ATOM   1105 N N   . GLY   A 1 143 ? -17.16080 -10.86117 -17.79812 1.000 25.90828  ? 143 GLY   A N   1 
ATOM   1106 C CA  . GLY   A 1 143 ? -17.25672 -9.54044  -17.20768 1.000 24.15040  ? 143 GLY   A CA  1 
ATOM   1107 C C   . GLY   A 1 143 ? -17.47055 -9.48766  -15.69954 1.000 22.91507  ? 143 GLY   A C   1 
ATOM   1108 O O   . GLY   A 1 143 ? -17.77532 -8.42138  -15.16428 1.000 26.57983  ? 143 GLY   A O   1 
ATOM   1109 N N   . SER   A 1 144 ? -17.32825 -10.58849 -14.97820 1.000 22.41057  ? 144 SER   A N   1 
ATOM   1110 C CA  . SER   A 1 144 ? -17.48871 -10.46738 -13.53291 1.000 28.34205  ? 144 SER   A CA  1 
ATOM   1111 C C   . SER   A 1 144 ? -16.21448 -10.01765 -12.82913 1.000 22.23260  ? 144 SER   A C   1 
ATOM   1112 O O   . SER   A 1 144 ? -16.23775 -9.79044  -11.62054 1.000 22.48359  ? 144 SER   A O   1 
ATOM   1113 C CB  . SER   A 1 144 ? -17.97970 -11.79109 -12.90686 1.000 21.66297  ? 144 SER   A CB  1 
ATOM   1114 O OG  . SER   A 1 144 ? -17.22849 -12.91795 -13.35222 1.000 23.66186  ? 144 SER   A OG  1 
ATOM   1115 N N   . CYS   A 1 145 ? -15.10957 -9.88085  -13.53595 1.000 24.90857  ? 145 CYS   A N   1 
ATOM   1116 C CA  . CYS   A 1 145 ? -13.87309 -9.52440  -12.86015 1.000 24.35243  ? 145 CYS   A CA  1 
ATOM   1117 C C   . CYS   A 1 145 ? -13.99307 -8.16993  -12.18956 1.000 24.46338  ? 145 CYS   A C   1 
ATOM   1118 O O   . CYS   A 1 145 ? -14.72101 -7.28022  -12.64639 1.000 25.48247  ? 145 CYS   A O   1 
ATOM   1119 C CB  . CYS   A 1 145 ? -12.70929 -9.56181  -13.83029 1.000 23.87903  ? 145 CYS   A CB  1 
ATOM   1120 S SG  . CYS   A 1 145 ? -12.44961 -11.25000 -14.35087 1.000 31.45129  ? 145 CYS   A SG  1 
ATOM   1121 N N   . GLY   A 1 146 ? -13.32934 -8.05021  -11.04979 1.000 19.16351  ? 146 GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 146 ? -13.42681 -6.86330  -10.24961 1.000 21.75370  ? 146 GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 146 ? -14.47541 -6.90730  -9.16334  1.000 20.47366  ? 146 GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 146 ? -14.39287 -6.09512  -8.23188  1.000 16.08591  ? 146 GLY   A O   1 
ATOM   1125 N N   . SER   A 1 147 ? -15.46271 -7.81830  -9.26427  1.000 19.10848  ? 147 SER   A N   1 
ATOM   1126 C CA  . SER   A 1 147 ? -16.36466 -8.07996  -8.14892  1.000 17.17153  ? 147 SER   A CA  1 
ATOM   1127 C C   . SER   A 1 147 ? -15.52901 -8.44488  -6.92763  1.000 17.42717  ? 147 SER   A C   1 
ATOM   1128 O O   . SER   A 1 147 ? -14.50064 -9.11716  -7.04949  1.000 20.01298  ? 147 SER   A O   1 
ATOM   1129 C CB  . SER   A 1 147 ? -17.34112 -9.22473  -8.48226  1.000 19.39812  ? 147 SER   A CB  1 
ATOM   1130 O OG  . SER   A 1 147 ? -18.12521 -8.97095  -9.64919  1.000 18.92803  ? 147 SER   A OG  1 
ATOM   1131 N N   . VAL   A 1 148 ? -15.94861 -7.98218  -5.75034  1.000 14.35329  ? 148 VAL   A N   1 
ATOM   1132 C CA  . VAL   A 1 148 ? -15.16798 -8.17315  -4.53892  1.000 16.64271  ? 148 VAL   A CA  1 
ATOM   1133 C C   . VAL   A 1 148 ? -15.88971 -9.14331  -3.61123  1.000 16.43303  ? 148 VAL   A C   1 
ATOM   1134 O O   . VAL   A 1 148 ? -17.09264 -9.38810  -3.72984  1.000 22.73731  ? 148 VAL   A O   1 
ATOM   1135 C CB  . VAL   A 1 148 ? -14.84983 -6.84014  -3.80266  1.000 16.09622  ? 148 VAL   A CB  1 
ATOM   1136 C CG1 . VAL   A 1 148 ? -14.10842 -5.87930  -4.73090  1.000 14.59670  ? 148 VAL   A CG1 1 
ATOM   1137 C CG2 . VAL   A 1 148 ? -16.12444 -6.19802  -3.24146  1.000 13.47604  ? 148 VAL   A CG2 1 
ATOM   1138 N N   . GLY   A 1 149 ? -15.12119 -9.71757  -2.68755  1.000 14.86559  ? 149 GLY   A N   1 
ATOM   1139 C CA  . GLY   A 1 149 ? -15.63649 -10.41249 -1.52298  1.000 16.34342  ? 149 GLY   A CA  1 
ATOM   1140 C C   . GLY   A 1 149 ? -15.30497 -9.65426  -0.25068  1.000 16.57986  ? 149 GLY   A C   1 
ATOM   1141 O O   . GLY   A 1 149 ? -14.30912 -8.90382  -0.21533  1.000 13.56264  ? 149 GLY   A O   1 
ATOM   1142 N N   . PHE   A 1 150 ? -16.09682 -9.84814  0.80719   1.000 12.63731  ? 150 PHE   A N   1 
ATOM   1143 C CA  . PHE   A 1 150 ? -15.97994 -8.97190  1.96538   1.000 16.26996  ? 150 PHE   A CA  1 
ATOM   1144 C C   . PHE   A 1 150 ? -16.68723 -9.53832  3.19109   1.000 17.98004  ? 150 PHE   A C   1 
ATOM   1145 O O   . PHE   A 1 150 ? -17.60068 -10.35653 3.10459   1.000 18.14369  ? 150 PHE   A O   1 
ATOM   1146 C CB  . PHE   A 1 150 ? -16.54135 -7.57488  1.66446   1.000 15.38175  ? 150 PHE   A CB  1 
ATOM   1147 C CG  . PHE   A 1 150 ? -17.99962 -7.57180  1.29296   1.000 17.81751  ? 150 PHE   A CG  1 
ATOM   1148 C CD1 . PHE   A 1 150 ? -18.40004 -7.92035  0.00052   1.000 15.50592  ? 150 PHE   A CD1 1 
ATOM   1149 C CD2 . PHE   A 1 150 ? -18.97598 -7.20425  2.23278   1.000 17.76146  ? 150 PHE   A CD2 1 
ATOM   1150 C CE1 . PHE   A 1 150 ? -19.74647 -7.92345  -0.36086  1.000 17.72518  ? 150 PHE   A CE1 1 
ATOM   1151 C CE2 . PHE   A 1 150 ? -20.33789 -7.19232  1.88595   1.000 18.39111  ? 150 PHE   A CE2 1 
ATOM   1152 C CZ  . PHE   A 1 150 ? -20.73004 -7.55773  0.58413   1.000 19.42570  ? 150 PHE   A CZ  1 
ATOM   1153 N N   . ASN   A 1 151 ? -16.28535 -9.02529  4.33628   1.000 18.79098  ? 151 ASN   A N   1 
ATOM   1154 C CA  . ASN   A 1 151 ? -16.96744 -9.25567  5.58713   1.000 19.47818  ? 151 ASN   A CA  1 
ATOM   1155 C C   . ASN   A 1 151 ? -17.36813 -7.90468  6.14985   1.000 24.64423  ? 151 ASN   A C   1 
ATOM   1156 O O   . ASN   A 1 151 ? -16.78956 -6.86811  5.79421   1.000 25.03939  ? 151 ASN   A O   1 
ATOM   1157 C CB  . ASN   A 1 151 ? -16.06338 -10.03013 6.55438   1.000 18.61126  ? 151 ASN   A CB  1 
ATOM   1158 C CG  . ASN   A 1 151 ? -16.01876 -11.51110 6.22333   1.000 19.89900  ? 151 ASN   A CG  1 
ATOM   1159 O OD1 . ASN   A 1 151 ? -15.06517 -12.01795 5.60654   1.000 14.05549  ? 151 ASN   A OD1 1 
ATOM   1160 N ND2 . ASN   A 1 151 ? -17.09343 -12.20895 6.57966   1.000 20.04801  ? 151 ASN   A ND2 1 
ATOM   1161 N N   . ILE   A 1 152 ? -18.38847 -7.89654  7.00138   1.000 27.36388  ? 152 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 152 ? -18.76115 -6.66873  7.68134   1.000 37.75487  ? 152 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 152 ? -18.63665 -6.86673  9.18089   1.000 43.58847  ? 152 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 152 ? -18.96185 -7.93079  9.70949   1.000 49.97326  ? 152 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 152 ? -20.16444 -6.20691  7.27627   1.000 42.19956  ? 152 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 152 ? -20.18113 -6.03574  5.74922   1.000 27.08178  ? 152 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 152 ? -20.52806 -4.89027  8.00992   1.000 48.08937  ? 152 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 152 ? -21.41110 -5.33436  5.22778   1.000 26.99452  ? 152 ILE   A CD1 1 
ATOM   1169 N N   . ASP   A 1 153 ? -18.11831 -5.85755  9.85891   1.000 38.37300  ? 153 ASP   A N   1 
ATOM   1170 C CA  . ASP   A 1 153 ? -17.86849 -5.97958  11.28338  1.000 54.81974  ? 153 ASP   A CA  1 
ATOM   1171 C C   . ASP   A 1 153 ? -18.24053 -4.64752  11.94666  1.000 56.01362  ? 153 ASP   A C   1 
ATOM   1172 O O   . ASP   A 1 153 ? -17.49258 -3.66050  11.86472  1.000 53.42570  ? 153 ASP   A O   1 
ATOM   1173 C CB  . ASP   A 1 153 ? -16.41798 -6.38709  11.50180  1.000 52.86124  ? 153 ASP   A CB  1 
ATOM   1174 C CG  . ASP   A 1 153 ? -16.20720 -7.00146  12.85180  1.000 58.94622  ? 153 ASP   A CG  1 
ATOM   1175 O OD1 . ASP   A 1 153 ? -17.19499 -7.07279  13.63179  1.000 59.33986  ? 153 ASP   A OD1 1 
ATOM   1176 O OD2 . ASP   A 1 153 ? -15.13225 -7.58625  13.05419  1.000 63.49852  ? 153 ASP   A OD2 1 
ATOM   1177 N N   . TYR   A 1 154 ? -19.41367 -4.64075  12.59338  1.000 66.65282  ? 154 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 154 ? -20.18223 -3.46211  12.98335  1.000 71.24878  ? 154 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 154 ? -20.42339 -2.51383  11.81530  1.000 66.03249  ? 154 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 154 ? -21.46980 -2.58367  11.16680  1.000 75.83572  ? 154 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 154 ? -19.52073 -2.73522  14.15195  1.000 62.34832  ? 154 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 154 ? -19.28647 -3.62942  15.34796  1.000 68.53206  ? 154 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 154 ? -18.09187 -4.31161  15.49939  1.000 66.95669  ? 154 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 154 ? -20.29412 -3.84966  16.29178  1.000 69.19516  ? 154 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 154 ? -17.87620 -5.14874  16.58278  1.000 73.16593  ? 154 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 154 ? -20.09065 -4.69159  17.37392  1.000 70.18774  ? 154 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 154 ? -18.87944 -5.33737  17.51564  1.000 73.49793  ? 154 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 154 ? -18.66529 -6.17446  18.58987  1.000 74.92598  ? 154 TYR   A OH  1 
ATOM   1189 N N   . ASP   A 1 155 ? -19.49171 -1.61590  11.53470  1.000 51.18109  ? 155 ASP   A N   1 
ATOM   1190 C CA  . ASP   A 1 155 ? -19.70091 -0.64515  10.46806  1.000 57.03986  ? 155 ASP   A CA  1 
ATOM   1191 C C   . ASP   A 1 155 ? -18.64474 -0.70801  9.37595   1.000 47.81972  ? 155 ASP   A C   1 
ATOM   1192 O O   . ASP   A 1 155 ? -18.76327 0.01008   8.37037   1.000 41.52734  ? 155 ASP   A O   1 
ATOM   1193 C CB  . ASP   A 1 155 ? -19.74560 0.76652   11.05824  1.000 64.01036  ? 155 ASP   A CB  1 
ATOM   1194 C CG  . ASP   A 1 155 ? -18.56791 1.03810   11.97537  1.000 67.32903  ? 155 ASP   A CG  1 
ATOM   1195 O OD1 . ASP   A 1 155 ? -18.06821 2.19262   11.99884  1.000 69.93305  ? 155 ASP   A OD1 1 
ATOM   1196 O OD2 . ASP   A 1 155 ? -18.14606 0.08040   12.66951  1.000 65.25394  ? 155 ASP   A OD2 1 
ATOM   1197 N N   . CYS   A 1 156 ? -17.62786 -1.54591  9.54891   1.000 42.72639  ? 156 CYS   A N   1 
ATOM   1198 C CA  . CYS   A 1 156 ? -16.44807 -1.56480  8.70515   1.000 34.88859  ? 156 CYS   A CA  1 
ATOM   1199 C C   . CYS   A 1 156 ? -16.57223 -2.69288  7.69111   1.000 28.23288  ? 156 CYS   A C   1 
ATOM   1200 O O   . CYS   A 1 156 ? -16.84289 -3.83987  8.06587   1.000 27.63469  ? 156 CYS   A O   1 
ATOM   1201 C CB  . CYS   A 1 156 ? -15.19608 -1.75069  9.56583   1.000 31.55507  ? 156 CYS   A CB  1 
ATOM   1202 S SG  . CYS   A 1 156 ? -13.62948 -1.74498  8.66710   1.000 25.32322  ? 156 CYS   A SG  1 
ATOM   1203 N N   . VAL   A 1 157 ? -16.37461 -2.37017  6.41426   1.000 20.21587  ? 157 VAL   A N   1 
ATOM   1204 C CA  . VAL   A 1 157 ? -16.26448 -3.38972  5.37593   1.000 26.71076  ? 157 VAL   A CA  1 
ATOM   1205 C C   . VAL   A 1 157 ? -14.79764 -3.81379  5.26157   1.000 28.57180  ? 157 VAL   A C   1 
ATOM   1206 O O   . VAL   A 1 157 ? -13.94902 -3.04978  4.79001   1.000 27.17699  ? 157 VAL   A O   1 
ATOM   1207 C CB  . VAL   A 1 157 ? -16.80775 -2.89493  4.03074   1.000 26.19779  ? 157 VAL   A CB  1 
ATOM   1208 C CG1 . VAL   A 1 157 ? -16.56318 -3.96580  2.94143   1.000 18.20357  ? 157 VAL   A CG1 1 
ATOM   1209 C CG2 . VAL   A 1 157 ? -18.30223 -2.52691  4.15620   1.000 16.49214  ? 157 VAL   A CG2 1 
ATOM   1210 N N   . SER   A 1 158 ? -14.49706 -5.03650  5.70552   1.000 24.64715  ? 158 SER   A N   1 
ATOM   1211 C CA  . SER   A 1 158 ? -13.21386 -5.69268  5.44898   1.000 24.59129  ? 158 SER   A CA  1 
ATOM   1212 C C   . SER   A 1 158 ? -13.31346 -6.39222  4.09829   1.000 19.99617  ? 158 SER   A C   1 
ATOM   1213 O O   . SER   A 1 158 ? -13.80386 -7.51441  3.99220   1.000 18.69353  ? 158 SER   A O   1 
ATOM   1214 C CB  . SER   A 1 158 ? -12.86350 -6.68100  6.55776   1.000 23.63361  ? 158 SER   A CB  1 
ATOM   1215 O OG  . SER   A 1 158 ? -12.79120 -6.05347  7.82635   1.000 30.67281  ? 158 SER   A OG  1 
ATOM   1216 N N   . PHE   A 1 159 ? -12.88498 -5.69331  3.04693   1.000 19.70566  ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 159 ? -12.73182 -6.29883  1.72889   1.000 19.05985  ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 159 ? -11.58821 -7.30190  1.76014   1.000 17.86741  ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 159 ? -10.45953 -6.92964  2.08598   1.000 18.85399  ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 159 ? -12.40635 -5.23438  0.68254   1.000 17.05582  ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 159 ? -13.51155 -4.28118  0.42897   1.000 19.51513  ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 159 ? -14.56914 -4.63999  -0.40781  1.000 16.08921  ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 159 ? -13.49752 -3.01879  1.00899   1.000 15.62487  ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 159 ? -15.59114 -3.77083  -0.64005  1.000 14.41305  ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 159 ? -14.51681 -2.13765  0.76758   1.000 16.60635  ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 159 ? -15.56661 -2.50192  -0.04943  1.000 16.41209  ? 159 PHE   A CZ  1 
ATOM   1227 N N   . CYS   A 1 160 ? -11.86249 -8.54918  1.35196   1.000 13.89653  ? 160 CYS   A N   1 
ATOM   1228 C CA  . CYS   A 1 160 ? -10.84886 -9.59388  1.31672   1.000 14.07607  ? 160 CYS   A CA  1 
ATOM   1229 C C   . CYS   A 1 160 ? -10.63294 -10.25429 -0.04375  1.000 15.56345  ? 160 CYS   A C   1 
ATOM   1230 O O   . CYS   A 1 160 ? -9.74176  -11.10202 -0.14823  1.000 20.48347  ? 160 CYS   A O   1 
ATOM   1231 C CB  . CYS   A 1 160 ? -11.19923 -10.69831 2.31296   1.000 15.33761  ? 160 CYS   A CB  1 
ATOM   1232 S SG  . CYS   A 1 160 ? -12.71960 -11.50176 1.85389   1.000 12.71664  ? 160 CYS   A SG  1 
ATOM   1233 N N   . TYR   A 1 161 ? -11.39378 -9.92144  -1.08841  1.000 13.82435  ? 161 TYR   A N   1 
ATOM   1234 C CA  . TYR   A 1 161 ? -11.25831 -10.68519 -2.33141  1.000 13.32892  ? 161 TYR   A CA  1 
ATOM   1235 C C   . TYR   A 1 161 ? -11.58587 -9.80855  -3.52034  1.000 14.27353  ? 161 TYR   A C   1 
ATOM   1236 O O   . TYR   A 1 161 ? -12.53929 -9.03087  -3.48011  1.000 16.81367  ? 161 TYR   A O   1 
ATOM   1237 C CB  . TYR   A 1 161 ? -12.18556 -11.91388 -2.35384  1.000 14.68816  ? 161 TYR   A CB  1 
ATOM   1238 C CG  . TYR   A 1 161 ? -12.08883 -12.74415 -3.61759  1.000 13.54749  ? 161 TYR   A CG  1 
ATOM   1239 C CD1 . TYR   A 1 161 ? -10.93251 -13.48538 -3.87893  1.000 16.61708  ? 161 TYR   A CD1 1 
ATOM   1240 C CD2 . TYR   A 1 161 ? -13.14488 -12.80801 -4.55174  1.000 12.75449  ? 161 TYR   A CD2 1 
ATOM   1241 C CE1 . TYR   A 1 161 ? -10.80081 -14.26369 -5.02992  1.000 16.64711  ? 161 TYR   A CE1 1 
ATOM   1242 C CE2 . TYR   A 1 161 ? -13.03240 -13.58848 -5.70969  1.000 13.10756  ? 161 TYR   A CE2 1 
ATOM   1243 C CZ  . TYR   A 1 161 ? -11.85671 -14.31394 -5.93692  1.000 18.92434  ? 161 TYR   A CZ  1 
ATOM   1244 O OH  . TYR   A 1 161 ? -11.67476 -15.10539 -7.04470  1.000 16.63885  ? 161 TYR   A OH  1 
ATOM   1245 N N   . MET   A 1 162 ? -10.79334 -9.92666  -4.57290  1.000 15.95307  ? 162 MET   A N   1 
ATOM   1246 C CA  . MET   A 1 162 ? -11.19729 -9.45197  -5.88577  1.000 17.08838  ? 162 MET   A CA  1 
ATOM   1247 C C   . MET   A 1 162 ? -11.18222 -10.61320 -6.87352  1.000 14.91870  ? 162 MET   A C   1 
ATOM   1248 O O   . MET   A 1 162 ? -10.31252 -11.48400 -6.79862  1.000 13.58228  ? 162 MET   A O   1 
ATOM   1249 C CB  . MET   A 1 162 ? -10.29849 -8.35200  -6.36812  1.000 15.22930  ? 162 MET   A CB  1 
ATOM   1250 C CG  . MET   A 1 162 ? -10.81615 -7.70897  -7.60513  1.000 14.57497  ? 162 MET   A CG  1 
ATOM   1251 S SD  . MET   A 1 162 ? -9.96895  -6.17339  -7.82468  1.000 21.24340  ? 162 MET   A SD  1 
ATOM   1252 C CE  . MET   A 1 162 ? -11.16879 -5.01412  -7.11107  1.000 21.67396  ? 162 MET   A CE  1 
ATOM   1253 N N   . HIS   A 1 163 ? -12.14217 -10.63883 -7.79502  1.000 17.26150  ? 163 HIS   A N   1 
ATOM   1254 C CA  . HIS   A 1 163 ? -12.24745 -11.76444 -8.72845  1.000 24.15706  ? 163 HIS   A CA  1 
ATOM   1255 C C   . HIS   A 1 163 ? -11.49656 -11.48571 -10.02723 1.000 16.91398  ? 163 HIS   A C   1 
ATOM   1256 O O   . HIS   A 1 163 ? -11.64157 -10.40940 -10.61520 1.000 16.33605  ? 163 HIS   A O   1 
ATOM   1257 C CB  . HIS   A 1 163 ? -13.70430 -12.09764 -9.03026  1.000 18.47120  ? 163 HIS   A CB  1 
ATOM   1258 C CG  . HIS   A 1 163 ? -13.85782 -13.26199 -9.94548  1.000 19.19631  ? 163 HIS   A CG  1 
ATOM   1259 N ND1 . HIS   A 1 163 ? -13.35022 -14.50743 -9.64690  1.000 17.07757  ? 163 HIS   A ND1 1 
ATOM   1260 C CD2 . HIS   A 1 163 ? -14.45680 -13.37261 -11.15749 1.000 18.84973  ? 163 HIS   A CD2 1 
ATOM   1261 C CE1 . HIS   A 1 163 ? -13.63426 -15.33679 -10.63761 1.000 21.32815  ? 163 HIS   A CE1 1 
ATOM   1262 N NE2 . HIS   A 1 163 ? -14.30302 -14.67357 -11.56591 1.000 18.84875  ? 163 HIS   A NE2 1 
ATOM   1263 N N   . HIS   A 1 164 ? -10.69395 -12.46721 -10.46569 1.000 19.53751  ? 164 HIS   A N   1 
ATOM   1264 C CA  . HIS   A 1 164 ? -9.82660  -12.34758 -11.64570 1.000 22.94831  ? 164 HIS   A CA  1 
ATOM   1265 C C   . HIS   A 1 164 ? -10.08626 -13.40195 -12.70766 1.000 24.07534  ? 164 HIS   A C   1 
ATOM   1266 O O   . HIS   A 1 164 ? -10.02203 -13.09047 -13.90167 1.000 22.04775  ? 164 HIS   A O   1 
ATOM   1267 C CB  . HIS   A 1 164 ? -8.33193  -12.42380 -11.26471 1.000 19.24264  ? 164 HIS   A CB  1 
ATOM   1268 C CG  . HIS   A 1 164 ? -7.83162  -11.23229 -10.50876 1.000 20.55057  ? 164 HIS   A CG  1 
ATOM   1269 N ND1 . HIS   A 1 164 ? -6.75766  -10.47973 -10.93243 1.000 23.24126  ? 164 HIS   A ND1 1 
ATOM   1270 C CD2 . HIS   A 1 164 ? -8.24864  -10.67130 -9.34880  1.000 17.23037  ? 164 HIS   A CD2 1 
ATOM   1271 C CE1 . HIS   A 1 164 ? -6.54338  -9.49729  -10.07509 1.000 18.73910  ? 164 HIS   A CE1 1 
ATOM   1272 N NE2 . HIS   A 1 164 ? -7.44567  -9.58125  -9.11471  1.000 17.68604  ? 164 HIS   A NE2 1 
ATOM   1273 N N   . MET   A 1 165 ? -10.36404 -14.64697 -12.32479 1.000 26.52093  ? 165 MET   A N   1 
ATOM   1274 C CA  . MET   A 1 165 ? -10.35718 -15.68034 -13.35123 1.000 30.06069  ? 165 MET   A CA  1 
ATOM   1275 C C   . MET   A 1 165 ? -11.12203 -16.92433 -12.92769 1.000 27.17815  ? 165 MET   A C   1 
ATOM   1276 O O   . MET   A 1 165 ? -11.26107 -17.23957 -11.74413 1.000 26.28462  ? 165 MET   A O   1 
ATOM   1277 C CB  . MET   A 1 165 ? -8.92576  -16.06853 -13.71753 1.000 31.22165  ? 165 MET   A CB  1 
ATOM   1278 C CG  . MET   A 1 165 ? -8.16416  -16.72652 -12.60065 1.000 27.73665  ? 165 MET   A CG  1 
ATOM   1279 S SD  . MET   A 1 165 ? -6.45996  -16.90480 -13.16935 1.000 41.97658  ? 165 MET   A SD  1 
ATOM   1280 C CE  . MET   A 1 165 ? -6.26006  -15.27516 -13.87560 1.000 30.25811  ? 165 MET   A CE  1 
ATOM   1281 N N   . GLU   A 1 166 ? -11.57168 -17.65325 -13.93137 1.000 30.01796  ? 166 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 166 ? -12.12486 -18.97776 -13.73357 1.000 31.78228  ? 166 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 166 ? -11.10489 -20.02473 -14.18419 1.000 34.36436  ? 166 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 166 ? -10.48913 -19.88892 -15.24817 1.000 30.28174  ? 166 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 166 ? -13.43829 -19.12882 -14.49575 1.000 26.35303  ? 166 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 166 ? -14.05310 -20.50639 -14.33335 1.000 29.82931  ? 166 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 166 ? -15.44346 -20.56638 -14.91056 1.000 30.14398  ? 166 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 166 ? -16.32236 -19.81351 -14.42095 1.000 24.11695  ? 166 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 166 ? -15.63609 -21.34605 -15.87398 1.000 28.70629  ? 166 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 167 ? -10.91273 -21.04525 -13.35578 1.000 29.82484  ? 167 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 167 ? -10.02303 -22.14831 -13.65822 1.000 32.55931  ? 167 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 167 ? -10.76932 -23.17955 -14.49410 1.000 37.05459  ? 167 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 167 ? -12.00422 -23.20370 -14.48838 1.000 36.90267  ? 167 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 167 ? -9.52516  -22.77321 -12.36032 1.000 32.96028  ? 167 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 167 ? -8.54445  -21.95617 -11.53361 1.000 29.28236  ? 167 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 167 ? -8.04878  -22.77019 -10.36315 1.000 29.96202  ? 167 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 167 ? -7.37756  -21.51994 -12.39440 1.000 37.40586  ? 167 LEU   A CD2 1 
ATOM   1298 N N   . PRO   A 1 168 ? -10.04519 -24.04392 -15.23179 1.000 41.42944  ? 168 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 168 ? -10.74107 -25.07648 -16.02873 1.000 39.31514  ? 168 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 168 ? -11.74544 -25.89076 -15.22164 1.000 40.16722  ? 168 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 168 ? -12.84986 -26.15607 -15.71650 1.000 40.79311  ? 168 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 168 ? -9.59179  -25.94539 -16.55935 1.000 36.14226  ? 168 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 168 ? -8.40372  -25.08004 -16.53873 1.000 37.66366  ? 168 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 168 ? -8.57781  -24.14633 -15.36937 1.000 41.57388  ? 168 PRO   A CD  1 
ATOM   1305 N N   . THR   A 1 169 ? -11.41352 -26.26667 -13.96995 1.000 37.28237  ? 169 THR   A N   1 
ATOM   1306 C CA  . THR   A 1 169 ? -12.40294 -26.99293 -13.16242 1.000 34.14953  ? 169 THR   A CA  1 
ATOM   1307 C C   . THR   A 1 169 ? -13.61193 -26.12489 -12.75101 1.000 33.79358  ? 169 THR   A C   1 
ATOM   1308 O O   . THR   A 1 169 ? -14.44097 -26.62311 -11.97775 1.000 33.34415  ? 169 THR   A O   1 
ATOM   1309 C CB  . THR   A 1 169 ? -11.75563 -27.57301 -11.90476 1.000 35.80376  ? 169 THR   A CB  1 
ATOM   1310 O OG1 . THR   A 1 169 ? -11.12129 -26.51906 -11.17348 1.000 36.06947  ? 169 THR   A OG1 1 
ATOM   1311 C CG2 . THR   A 1 169 ? -10.72088 -28.65261 -12.26126 1.000 30.66239  ? 169 THR   A CG2 1 
ATOM   1312 N N   . GLY   A 1 170 ? -13.77151 -24.87193 -13.18674 1.000 33.05556  ? 170 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 170 ? -14.94653 -24.09291 -12.85577 1.000 27.60516  ? 170 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 170 ? -14.88411 -23.34178 -11.54530 1.000 27.31125  ? 170 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 170 ? -15.77152 -22.52635 -11.27561 1.000 27.65587  ? 170 GLY   A O   1 
ATOM   1316 N N   . VAL   A 1 171 ? -13.88796 -23.59756 -10.70588 1.000 29.02453  ? 171 VAL   A N   1 
ATOM   1317 C CA  . VAL   A 1 171 ? -13.68733 -22.78500 -9.51538  1.000 24.84776  ? 171 VAL   A CA  1 
ATOM   1318 C C   . VAL   A 1 171 ? -13.00021 -21.49494 -9.92446  1.000 23.99051  ? 171 VAL   A C   1 
ATOM   1319 O O   . VAL   A 1 171 ? -12.58703 -21.31541 -11.08211 1.000 21.36527  ? 171 VAL   A O   1 
ATOM   1320 C CB  . VAL   A 1 171 ? -12.86371 -23.52188 -8.44404  1.000 26.90506  ? 171 VAL   A CB  1 
ATOM   1321 C CG1 . VAL   A 1 171 ? -13.63746 -24.73576 -7.93176  1.000 29.93273  ? 171 VAL   A CG1 1 
ATOM   1322 C CG2 . VAL   A 1 171 ? -11.49043 -23.92385 -9.00643  1.000 19.04422  ? 171 VAL   A CG2 1 
ATOM   1323 N N   . HIS   A 1 172 ? -12.83670 -20.60927 -8.95633  1.000 21.91400  ? 172 HIS   A N   1 
ATOM   1324 C CA  . HIS   A 1 172 ? -12.48050 -19.23282 -9.22677  1.000 20.56595  ? 172 HIS   A CA  1 
ATOM   1325 C C   . HIS   A 1 172 ? -11.26330 -18.82856 -8.41322  1.000 21.32410  ? 172 HIS   A C   1 
ATOM   1326 O O   . HIS   A 1 172 ? -11.02105 -19.34073 -7.31182  1.000 20.46361  ? 172 HIS   A O   1 
ATOM   1327 C CB  . HIS   A 1 172 ? -13.67833 -18.34830 -8.95587  1.000 19.86903  ? 172 HIS   A CB  1 
ATOM   1328 C CG  . HIS   A 1 172 ? -14.82473 -18.63840 -9.87045  1.000 24.71120  ? 172 HIS   A CG  1 
ATOM   1329 N ND1 . HIS   A 1 172 ? -15.88767 -19.44795 -9.50934  1.000 20.51038  ? 172 HIS   A ND1 1 
ATOM   1330 C CD2 . HIS   A 1 172 ? -15.05396 -18.25721 -11.15176 1.000 21.72754  ? 172 HIS   A CD2 1 
ATOM   1331 C CE1 . HIS   A 1 172 ? -16.72427 -19.53761 -10.52791 1.000 21.71738  ? 172 HIS   A CE1 1 
ATOM   1332 N NE2 . HIS   A 1 172 ? -16.24316 -18.82682 -11.53518 1.000 21.74433  ? 172 HIS   A NE2 1 
ATOM   1333 N N   . ALA   A 1 173 ? -10.48944 -17.91150 -8.99236  1.000 20.20722  ? 173 ALA   A N   1 
ATOM   1334 C CA  . ALA   A 1 173 ? -9.23155  -17.44571 -8.42729  1.000 17.61118  ? 173 ALA   A CA  1 
ATOM   1335 C C   . ALA   A 1 173 ? -9.17589  -15.93007 -8.52442  1.000 19.33364  ? 173 ALA   A C   1 
ATOM   1336 O O   . ALA   A 1 173 ? -9.62836  -15.33590 -9.50835  1.000 17.40688  ? 173 ALA   A O   1 
ATOM   1337 C CB  . ALA   A 1 173 ? -8.01329  -18.04935 -9.14638  1.000 17.57759  ? 173 ALA   A CB  1 
ATOM   1338 N N   . GLY   A 1 174 ? -8.61865  -15.32045 -7.50068  1.000 17.95661  ? 174 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 174 ? -8.44092  -13.89413 -7.48223  1.000 18.83025  ? 174 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 174 ? -7.50160  -13.51715 -6.36991  1.000 15.17849  ? 174 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 174 ? -6.69463  -14.33119 -5.91617  1.000 14.62656  ? 174 GLY   A O   1 
ATOM   1342 N N   . THR   A 1 175 ? -7.62926  -12.26902 -5.92140  1.000 14.01870  ? 175 THR   A N   1 
ATOM   1343 C CA  . THR   A 1 175 ? -6.60563  -11.65214 -5.09626  1.000 15.62831  ? 175 THR   A CA  1 
ATOM   1344 C C   . THR   A 1 175 ? -7.23635  -10.98291 -3.89653  1.000 14.99779  ? 175 THR   A C   1 
ATOM   1345 O O   . THR   A 1 175 ? -8.44009  -10.70343 -3.87703  1.000 13.37508  ? 175 THR   A O   1 
ATOM   1346 C CB  . THR   A 1 175 ? -5.75483  -10.59291 -5.88056  1.000 14.54752  ? 175 THR   A CB  1 
ATOM   1347 O OG1 . THR   A 1 175 ? -6.57400  -9.54874  -6.42411  1.000 14.41109  ? 175 THR   A OG1 1 
ATOM   1348 C CG2 . THR   A 1 175 ? -4.99693  -11.25313 -6.97772  1.000 15.12829  ? 175 THR   A CG2 1 
ATOM   1349 N N   . ASP   A 1 176 ? -6.38697  -10.69016 -2.90827  1.000 15.45480  ? 176 ASP   A N   1 
ATOM   1350 C CA  . ASP   A 1 176 ? -6.74916  -9.66681  -1.94539  1.000 14.90984  ? 176 ASP   A CA  1 
ATOM   1351 C C   . ASP   A 1 176 ? -6.74923  -8.30604  -2.64523  1.000 14.28765  ? 176 ASP   A C   1 
ATOM   1352 O O   . ASP   A 1 176 ? -6.41536  -8.18616  -3.82426  1.000 14.17972  ? 176 ASP   A O   1 
ATOM   1353 C CB  . ASP   A 1 176 ? -5.81979  -9.70411  -0.71632  1.000 14.43636  ? 176 ASP   A CB  1 
ATOM   1354 C CG  . ASP   A 1 176 ? -4.35927  -9.34332  -1.02189  1.000 17.98528  ? 176 ASP   A CG  1 
ATOM   1355 O OD1 . ASP   A 1 176 ? -4.06647  -8.39184  -1.80215  1.000 19.33297  ? 176 ASP   A OD1 1 
ATOM   1356 O OD2 . ASP   A 1 176 ? -3.48555  -10.01895 -0.43390  1.000 18.79039  ? 176 ASP   A OD2 1 
ATOM   1357 N N   . LEU   A 1 177 ? -7.16164  -7.27845  -1.91429  1.000 14.06059  ? 177 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 177 ? -7.35839  -5.95808  -2.48389  1.000 14.32423  ? 177 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 177 ? -6.06572  -5.18193  -2.55924  1.000 16.52123  ? 177 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 177 ? -6.06690  -3.97403  -2.82023  1.000 20.21447  ? 177 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 177 ? -8.41403  -5.18330  -1.68375  1.000 14.96528  ? 177 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 177 ? -9.85440  -5.29637  -2.19663  1.000 16.01392  ? 177 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 177 ? -10.06387 -4.69868  -3.60383  1.000 14.17687  ? 177 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 177 ? -10.32617 -6.77448  -2.12874  1.000 15.35513  ? 177 LEU   A CD2 1 
ATOM   1365 N N   . GLU   A 1 178 ? -4.94845  -5.84450  -2.29382  1.000 21.49401  ? 178 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 178 ? -3.65087  -5.28660  -2.60973  1.000 20.34909  ? 178 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 178 ? -3.03721  -6.03045  -3.78578  1.000 20.24734  ? 178 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 178 ? -1.91297  -5.72390  -4.19712  1.000 22.62236  ? 178 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 178 ? -2.76118  -5.29656  -1.36609  1.000 17.33223  ? 178 GLU   A CB  1 
ATOM   1370 N N   . GLY   A 1 179 ? -3.77020  -6.98685  -4.34927  1.000 15.43715  ? 179 GLY   A N   1 
ATOM   1371 C CA  . GLY   A 1 179 ? -3.42329  -7.59409  -5.61592  1.000 16.34687  ? 179 GLY   A CA  1 
ATOM   1372 C C   . GLY   A 1 179 ? -2.59110  -8.85412  -5.53921  1.000 19.60472  ? 179 GLY   A C   1 
ATOM   1373 O O   . GLY   A 1 179 ? -2.10115  -9.32060  -6.57644  1.000 16.40476  ? 179 GLY   A O   1 
ATOM   1374 N N   . ASN   A 1 180 ? -2.38712  -9.40457  -4.35092  1.000 20.18439  ? 180 ASN   A N   1 
ATOM   1375 C CA  . ASN   A 1 180 ? -1.70166  -10.67714 -4.20021  1.000 16.73493  ? 180 ASN   A CA  1 
ATOM   1376 C C   . ASN   A 1 180 ? -2.73121  -11.77861 -4.37878  1.000 17.26543  ? 180 ASN   A C   1 
ATOM   1377 O O   . ASN   A 1 180 ? -3.75263  -11.80208 -3.67768  1.000 19.54183  ? 180 ASN   A O   1 
ATOM   1378 C CB  . ASN   A 1 180 ? -1.02680  -10.76299 -2.83626  1.000 16.69827  ? 180 ASN   A CB  1 
ATOM   1379 C CG  . ASN   A 1 180 ? -0.19779  -9.50280  -2.51571  1.000 17.79751  ? 180 ASN   A CG  1 
ATOM   1380 O OD1 . ASN   A 1 180 ? 0.84714   -9.24784  -3.15006  1.000 17.63901  ? 180 ASN   A OD1 1 
ATOM   1381 N ND2 . ASN   A 1 180 ? -0.68076  -8.69683  -1.54771  1.000 16.77198  ? 180 ASN   A ND2 1 
ATOM   1382 N N   . PHE   A 1 181 ? -2.48861  -12.65406 -5.34819  1.000 18.96347  ? 181 PHE   A N   1 
ATOM   1383 C CA  . PHE   A 1 181 ? -3.34902  -13.80835 -5.52528  1.000 17.61533  ? 181 PHE   A CA  1 
ATOM   1384 C C   . PHE   A 1 181 ? -3.38436  -14.63141 -4.25393  1.000 15.87331  ? 181 PHE   A C   1 
ATOM   1385 O O   . PHE   A 1 181 ? -2.37345  -14.80500 -3.57449  1.000 16.27686  ? 181 PHE   A O   1 
ATOM   1386 C CB  . PHE   A 1 181 ? -2.87235  -14.65653 -6.71241  1.000 16.56812  ? 181 PHE   A CB  1 
ATOM   1387 C CG  . PHE   A 1 181 ? -3.56912  -14.30490 -8.00477  1.000 21.03044  ? 181 PHE   A CG  1 
ATOM   1388 C CD1 . PHE   A 1 181 ? -4.80270  -14.89054 -8.33236  1.000 21.91835  ? 181 PHE   A CD1 1 
ATOM   1389 C CD2 . PHE   A 1 181 ? -3.03752  -13.35654 -8.86002  1.000 16.90106  ? 181 PHE   A CD2 1 
ATOM   1390 C CE1 . PHE   A 1 181 ? -5.47616  -14.54574 -9.48898  1.000 19.69306  ? 181 PHE   A CE1 1 
ATOM   1391 C CE2 . PHE   A 1 181 ? -3.69520  -13.01809 -10.01380 1.000 18.60884  ? 181 PHE   A CE2 1 
ATOM   1392 C CZ  . PHE   A 1 181 ? -4.91225  -13.62023 -10.34036 1.000 23.21618  ? 181 PHE   A CZ  1 
ATOM   1393 N N   . TYR   A 1 182 ? -4.57108  -15.09498 -3.90962  1.000 16.85531  ? 182 TYR   A N   1 
ATOM   1394 C CA  . TYR   A 1 182 ? -4.67830  -16.27327 -3.06835  1.000 15.45361  ? 182 TYR   A CA  1 
ATOM   1395 C C   . TYR   A 1 182 ? -4.19288  -17.48696 -3.87219  1.000 16.20406  ? 182 TYR   A C   1 
ATOM   1396 O O   . TYR   A 1 182 ? -4.51135  -17.63437 -5.05512  1.000 18.41372  ? 182 TYR   A O   1 
ATOM   1397 C CB  . TYR   A 1 182 ? -6.12800  -16.42198 -2.59518  1.000 14.82156  ? 182 TYR   A CB  1 
ATOM   1398 C CG  . TYR   A 1 182 ? -6.57021  -15.31852 -1.64423  1.000 14.30768  ? 182 TYR   A CG  1 
ATOM   1399 C CD1 . TYR   A 1 182 ? -6.25021  -15.38047 -0.28158  1.000 16.03640  ? 182 TYR   A CD1 1 
ATOM   1400 C CD2 . TYR   A 1 182 ? -7.29614  -14.21620 -2.09867  1.000 16.77121  ? 182 TYR   A CD2 1 
ATOM   1401 C CE1 . TYR   A 1 182 ? -6.64281  -14.39212 0.61233   1.000 16.42026  ? 182 TYR   A CE1 1 
ATOM   1402 C CE2 . TYR   A 1 182 ? -7.69903  -13.19788 -1.21622  1.000 16.32934  ? 182 TYR   A CE2 1 
ATOM   1403 C CZ  . TYR   A 1 182 ? -7.35719  -13.28985 0.14298   1.000 19.75501  ? 182 TYR   A CZ  1 
ATOM   1404 O OH  . TYR   A 1 182 ? -7.74050  -12.31127 1.04416   1.000 14.49915  ? 182 TYR   A OH  1 
ATOM   1405 N N   . GLY   A 1 183 ? -3.38120  -18.33143 -3.26063  1.000 16.88316  ? 183 GLY   A N   1 
ATOM   1406 C CA  . GLY   A 1 183 ? -2.84835  -19.49349 -3.94800  1.000 17.81627  ? 183 GLY   A CA  1 
ATOM   1407 C C   . GLY   A 1 183 ? -1.75274  -19.15872 -4.93398  1.000 18.86316  ? 183 GLY   A C   1 
ATOM   1408 O O   . GLY   A 1 183 ? -1.29503  -18.01058 -5.02121  1.000 22.10427  ? 183 GLY   A O   1 
ATOM   1409 N N   . PRO   A 1 184 ? -1.32926  -20.15543 -5.71959  1.000 19.45097  ? 184 PRO   A N   1 
ATOM   1410 C CA  . PRO   A 1 184 ? -0.14781  -19.98251 -6.58533  1.000 22.49671  ? 184 PRO   A CA  1 
ATOM   1411 C C   . PRO   A 1 184 ? -0.49823  -19.51531 -7.98895  1.000 26.56655  ? 184 PRO   A C   1 
ATOM   1412 O O   . PRO   A 1 184 ? 0.27824   -19.72781 -8.92909  1.000 30.09729  ? 184 PRO   A O   1 
ATOM   1413 C CB  . PRO   A 1 184 ? 0.44764   -21.39045 -6.63418  1.000 21.64988  ? 184 PRO   A CB  1 
ATOM   1414 C CG  . PRO   A 1 184 ? -0.81872  -22.27064 -6.65347  1.000 23.40663  ? 184 PRO   A CG  1 
ATOM   1415 C CD  . PRO   A 1 184 ? -1.89693  -21.51076 -5.83930  1.000 21.44899  ? 184 PRO   A CD  1 
ATOM   1416 N N   . PHE   A 1 185 ? -1.66451  -18.90610 -8.15350  1.000 22.40265  ? 185 PHE   A N   1 
ATOM   1417 C CA  . PHE   A 1 185 ? -2.14016  -18.56651 -9.48261  1.000 25.24397  ? 185 PHE   A CA  1 
ATOM   1418 C C   . PHE   A 1 185 ? -1.58447  -17.22111 -9.94033  1.000 27.45592  ? 185 PHE   A C   1 
ATOM   1419 O O   . PHE   A 1 185 ? -1.23028  -16.35134 -9.13151  1.000 23.60029  ? 185 PHE   A O   1 
ATOM   1420 C CB  . PHE   A 1 185 ? -3.66951  -18.55512 -9.51810  1.000 26.11501  ? 185 PHE   A CB  1 
ATOM   1421 C CG  . PHE   A 1 185 ? -4.27744  -19.78948 -8.94619  1.000 23.16041  ? 185 PHE   A CG  1 
ATOM   1422 C CD1 . PHE   A 1 185 ? -3.99099  -21.03275 -9.49741  1.000 26.67501  ? 185 PHE   A CD1 1 
ATOM   1423 C CD2 . PHE   A 1 185 ? -5.10416  -19.71848 -7.85409  1.000 19.97708  ? 185 PHE   A CD2 1 
ATOM   1424 C CE1 . PHE   A 1 185 ? -4.53056  -22.19232 -8.97777  1.000 26.25921  ? 185 PHE   A CE1 1 
ATOM   1425 C CE2 . PHE   A 1 185 ? -5.66373  -20.86983 -7.31785  1.000 23.10014  ? 185 PHE   A CE2 1 
ATOM   1426 C CZ  . PHE   A 1 185 ? -5.36859  -22.11575 -7.88106  1.000 27.85386  ? 185 PHE   A CZ  1 
ATOM   1427 N N   . VAL   A 1 186 ? -1.50485  -17.06967 -11.26532 1.000 27.18728  ? 186 VAL   A N   1 
ATOM   1428 C CA  . VAL   A 1 186 ? -1.01368  -15.85978 -11.89535 1.000 31.16623  ? 186 VAL   A CA  1 
ATOM   1429 C C   . VAL   A 1 186 ? -2.06214  -15.36928 -12.88730 1.000 33.77362  ? 186 VAL   A C   1 
ATOM   1430 O O   . VAL   A 1 186 ? -2.89898  -16.13374 -13.36929 1.000 37.28833  ? 186 VAL   A O   1 
ATOM   1431 C CB  . VAL   A 1 186 ? 0.35648   -16.11227 -12.57224 1.000 35.06152  ? 186 VAL   A CB  1 
ATOM   1432 C CG1 . VAL   A 1 186 ? 1.37237   -16.50415 -11.51620 1.000 21.72617  ? 186 VAL   A CG1 1 
ATOM   1433 C CG2 . VAL   A 1 186 ? 0.24796   -17.19279 -13.64985 1.000 36.06078  ? 186 VAL   A CG2 1 
ATOM   1434 N N   . ASP   A 1 187 ? -2.03680  -14.06975 -13.17595 1.000 29.30318  ? 187 ASP   A N   1 
ATOM   1435 C CA  . ASP   A 1 187 ? -2.96914  -13.53591 -14.17215 1.000 31.36932  ? 187 ASP   A CA  1 
ATOM   1436 C C   . ASP   A 1 187 ? -2.34259  -13.66764 -15.56255 1.000 39.26678  ? 187 ASP   A C   1 
ATOM   1437 O O   . ASP   A 1 187 ? -1.99823  -12.69674 -16.23955 1.000 36.59455  ? 187 ASP   A O   1 
ATOM   1438 C CB  . ASP   A 1 187 ? -3.38259  -12.10390 -13.83896 1.000 29.76542  ? 187 ASP   A CB  1 
ATOM   1439 C CG  . ASP   A 1 187 ? -2.22812  -11.24425 -13.35986 1.000 31.59120  ? 187 ASP   A CG  1 
ATOM   1440 O OD1 . ASP   A 1 187 ? -1.12048  -11.78815 -13.16454 1.000 35.03482  ? 187 ASP   A OD1 1 
ATOM   1441 O OD2 . ASP   A 1 187 ? -2.44074  -10.02853 -13.15678 1.000 28.39895  ? 187 ASP   A OD2 1 
ATOM   1442 N N   . ARG   A 1 188 ? -2.17548  -14.92956 -15.96298 1.000 41.41274  ? 188 ARG   A N   1 
ATOM   1443 C CA  . ARG   A 1 188 ? -1.77866  -15.31458 -17.30974 1.000 48.69879  ? 188 ARG   A CA  1 
ATOM   1444 C C   . ARG   A 1 188 ? -2.72366  -16.38777 -17.81227 1.000 54.91451  ? 188 ARG   A C   1 
ATOM   1445 O O   . ARG   A 1 188 ? -3.19276  -17.23233 -17.04270 1.000 47.46455  ? 188 ARG   A O   1 
ATOM   1446 C CB  . ARG   A 1 188 ? -0.36075  -15.90227 -17.40289 1.000 47.48346  ? 188 ARG   A CB  1 
ATOM   1447 C CG  . ARG   A 1 188 ? 0.75452   -14.96133 -17.14123 1.000 49.08127  ? 188 ARG   A CG  1 
ATOM   1448 C CD  . ARG   A 1 188 ? 2.03233   -15.71650 -17.33834 1.000 58.93529  ? 188 ARG   A CD  1 
ATOM   1449 N NE  . ARG   A 1 188 ? 2.48777   -16.59773 -16.28624 1.000 54.19441  ? 188 ARG   A NE  1 
ATOM   1450 C CZ  . ARG   A 1 188 ? 3.36402   -17.58961 -16.48780 1.000 54.58206  ? 188 ARG   A CZ  1 
ATOM   1451 N NH1 . ARG   A 1 188 ? 3.79837   -17.91817 -17.71415 1.000 52.44786  ? 188 ARG   A NH1 1 
ATOM   1452 N NH2 . ARG   A 1 188 ? 3.76193   -18.32609 -15.45991 1.000 54.76832  ? 188 ARG   A NH2 1 
ATOM   1453 N N   . GLN   A 1 189 ? -2.96146  -16.37524 -19.12398 1.000 79.23020  ? 189 GLN   A N   1 
ATOM   1454 C CA  . GLN   A 1 189 ? -3.75140  -17.42456 -19.76875 1.000 77.95676  ? 189 GLN   A CA  1 
ATOM   1455 C C   . GLN   A 1 189 ? -2.81908  -18.55910 -20.19404 1.000 79.79061  ? 189 GLN   A C   1 
ATOM   1456 O O   . GLN   A 1 189 ? -2.50599  -18.75485 -21.37040 1.000 83.77308  ? 189 GLN   A O   1 
ATOM   1457 C CB  . GLN   A 1 189 ? -4.52834  -16.87127 -20.95148 1.000 80.06714  ? 189 GLN   A CB  1 
ATOM   1458 C CG  . GLN   A 1 189 ? -5.64403  -17.78849 -21.36338 1.000 84.81073  ? 189 GLN   A CG  1 
ATOM   1459 C CD  . GLN   A 1 189 ? -6.15781  -17.49695 -22.75087 1.000 95.98447  ? 189 GLN   A CD  1 
ATOM   1460 O OE1 . GLN   A 1 189 ? -6.00969  -16.38225 -23.26954 1.000 98.03126  ? 189 GLN   A OE1 1 
ATOM   1461 N NE2 . GLN   A 1 189 ? -6.75407  -18.51600 -23.37965 1.000 101.04511 ? 189 GLN   A NE2 1 
ATOM   1462 N N   . THR   A 1 190 ? -2.34838  -19.28862 -19.18110 1.000 64.41588  ? 190 THR   A N   1 
ATOM   1463 C CA  . THR   A 1 190 ? -1.55251  -20.49695 -19.33006 1.000 57.36132  ? 190 THR   A CA  1 
ATOM   1464 C C   . THR   A 1 190 ? -2.18761  -21.58085 -18.47781 1.000 53.85432  ? 190 THR   A C   1 
ATOM   1465 O O   . THR   A 1 190 ? -3.12927  -21.33078 -17.71957 1.000 47.91976  ? 190 THR   A O   1 
ATOM   1466 C CB  . THR   A 1 190 ? -0.09564  -20.29311 -18.89587 1.000 56.46636  ? 190 THR   A CB  1 
ATOM   1467 O OG1 . THR   A 1 190 ? -0.04231  -20.20058 -17.46554 1.000 51.90304  ? 190 THR   A OG1 1 
ATOM   1468 C CG2 . THR   A 1 190 ? 0.48446   -19.01872 -19.51577 1.000 57.71065  ? 190 THR   A CG2 1 
ATOM   1469 N N   . ALA   A 1 191 ? -1.64820  -22.79123 -18.59206 1.000 50.69826  ? 191 ALA   A N   1 
ATOM   1470 C CA  . ALA   A 1 191 ? -2.20320  -23.92622 -17.86552 1.000 49.64978  ? 191 ALA   A CA  1 
ATOM   1471 C C   . ALA   A 1 191 ? -1.98026  -23.74935 -16.36314 1.000 49.97159  ? 191 ALA   A C   1 
ATOM   1472 O O   . ALA   A 1 191 ? -0.84092  -23.65267 -15.89822 1.000 54.07001  ? 191 ALA   A O   1 
ATOM   1473 C CB  . ALA   A 1 191 ? -1.57783  -25.22853 -18.36468 1.000 38.72546  ? 191 ALA   A CB  1 
ATOM   1474 N N   . GLN   A 1 192 ? -3.06697  -23.66857 -15.61057 1.000 48.03741  ? 192 GLN   A N   1 
ATOM   1475 C CA  . GLN   A 1 192 ? -3.01893  -23.70239 -14.15762 1.000 52.78290  ? 192 GLN   A CA  1 
ATOM   1476 C C   . GLN   A 1 192 ? -4.18222  -24.54020 -13.66087 1.000 51.22086  ? 192 GLN   A C   1 
ATOM   1477 O O   . GLN   A 1 192 ? -5.30035  -24.41413 -14.16811 1.000 49.68272  ? 192 GLN   A O   1 
ATOM   1478 C CB  . GLN   A 1 192 ? -3.13829  -22.31512 -13.52135 1.000 49.65848  ? 192 GLN   A CB  1 
ATOM   1479 C CG  . GLN   A 1 192 ? -2.35234  -21.21593 -14.14610 1.000 45.30155  ? 192 GLN   A CG  1 
ATOM   1480 C CD  . GLN   A 1 192 ? -2.84217  -19.88868 -13.63815 1.000 45.22145  ? 192 GLN   A CD  1 
ATOM   1481 O OE1 . GLN   A 1 192 ? -2.76677  -19.61507 -12.43830 1.000 40.68153  ? 192 GLN   A OE1 1 
ATOM   1482 N NE2 . GLN   A 1 192 ? -3.37152  -19.05760 -14.53724 1.000 49.31286  ? 192 GLN   A NE2 1 
ATOM   1483 N N   . ALA   A 1 193 ? -3.93288  -25.36552 -12.65511 1.000 45.55925  ? 193 ALA   A N   1 
ATOM   1484 C CA  . ALA   A 1 193 ? -5.00129  -26.15240 -12.06522 1.000 43.86443  ? 193 ALA   A CA  1 
ATOM   1485 C C   . ALA   A 1 193 ? -5.14016  -25.81538 -10.58904 1.000 43.18380  ? 193 ALA   A C   1 
ATOM   1486 O O   . ALA   A 1 193 ? -4.26017  -25.20698 -9.96982  1.000 44.22659  ? 193 ALA   A O   1 
ATOM   1487 C CB  . ALA   A 1 193 ? -4.76857  -27.65612 -12.24598 1.000 47.19800  ? 193 ALA   A CB  1 
ATOM   1488 N N   . ALA   A 1 194 ? -6.25852  -26.27317 -10.02925 1.000 39.37305  ? 194 ALA   A N   1 
ATOM   1489 C CA  . ALA   A 1 194 ? -6.68238  -25.83200 -8.70757  1.000 34.66892  ? 194 ALA   A CA  1 
ATOM   1490 C C   . ALA   A 1 194 ? -5.83299  -26.45093 -7.60523  1.000 34.43124  ? 194 ALA   A C   1 
ATOM   1491 O O   . ALA   A 1 194 ? -5.57183  -25.80631 -6.57906  1.000 37.57829  ? 194 ALA   A O   1 
ATOM   1492 C CB  . ALA   A 1 194 ? -8.16051  -26.17426 -8.50134  1.000 32.42026  ? 194 ALA   A CB  1 
ATOM   1493 N N   . GLY   A 1 195 ? -5.39599  -27.69252 -7.78720  1.000 33.24611  ? 195 GLY   A N   1 
ATOM   1494 C CA  . GLY   A 1 195 ? -4.74742  -28.38251 -6.69128  1.000 35.00000  ? 195 GLY   A CA  1 
ATOM   1495 C C   . GLY   A 1 195 ? -5.74682  -29.06383 -5.77985  1.000 36.58909  ? 195 GLY   A C   1 
ATOM   1496 O O   . GLY   A 1 195 ? -6.85376  -28.55108 -5.56766  1.000 38.18305  ? 195 GLY   A O   1 
ATOM   1497 N N   . THR   A 1 196 ? -5.36512  -30.21826 -5.23904  1.000 35.74259  ? 196 THR   A N   1 
ATOM   1498 C CA  . THR   A 1 196 ? -6.24387  -31.00546 -4.38386  1.000 39.11232  ? 196 THR   A CA  1 
ATOM   1499 C C   . THR   A 1 196 ? -6.87166  -30.14350 -3.30232  1.000 34.51240  ? 196 THR   A C   1 
ATOM   1500 O O   . THR   A 1 196 ? -6.18481  -29.39131 -2.61050  1.000 36.46272  ? 196 THR   A O   1 
ATOM   1501 C CB  . THR   A 1 196 ? -5.45191  -32.15774 -3.75512  1.000 39.51033  ? 196 THR   A CB  1 
ATOM   1502 O OG1 . THR   A 1 196 ? -5.27985  -33.19152 -4.73667  1.000 40.37659  ? 196 THR   A OG1 1 
ATOM   1503 C CG2 . THR   A 1 196 ? -6.16182  -32.72606 -2.50060  1.000 42.24218  ? 196 THR   A CG2 1 
ATOM   1504 N N   . ASP   A 1 197 ? -8.18185  -30.23277 -3.18093  1.000 40.74785  ? 197 ASP   A N   1 
ATOM   1505 C CA  . ASP   A 1 197 ? -8.86885  -29.54719 -2.10486  1.000 39.87454  ? 197 ASP   A CA  1 
ATOM   1506 C C   . ASP   A 1 197 ? -9.14313  -30.51988 -0.96917  1.000 43.51868  ? 197 ASP   A C   1 
ATOM   1507 O O   . ASP   A 1 197 ? -9.23807  -31.73175 -1.17344  1.000 48.80484  ? 197 ASP   A O   1 
ATOM   1508 C CB  . ASP   A 1 197 ? -10.17634 -28.92145 -2.58609  1.000 38.33115  ? 197 ASP   A CB  1 
ATOM   1509 C CG  . ASP   A 1 197 ? -10.64640 -27.79934 -1.67399  1.000 39.05221  ? 197 ASP   A CG  1 
ATOM   1510 O OD1 . ASP   A 1 197 ? -9.77853  -27.10670 -1.08912  1.000 36.62911  ? 197 ASP   A OD1 1 
ATOM   1511 O OD2 . ASP   A 1 197 ? -11.87828 -27.62883 -1.52810  1.000 40.30117  ? 197 ASP   A OD2 1 
ATOM   1512 N N   . THR   A 1 198 ? -9.24940  -29.97593 0.23516   1.000 37.69455  ? 198 THR   A N   1 
ATOM   1513 C CA  . THR   A 1 198 ? -9.65599  -30.71820 1.41810   1.000 38.03586  ? 198 THR   A CA  1 
ATOM   1514 C C   . THR   A 1 198 ? -10.88935 -30.05387 2.02857   1.000 38.77854  ? 198 THR   A C   1 
ATOM   1515 O O   . THR   A 1 198 ? -11.26529 -28.91917 1.67644   1.000 34.15129  ? 198 THR   A O   1 
ATOM   1516 C CB  . THR   A 1 198 ? -8.50401  -30.81068 2.43604   1.000 37.09440  ? 198 THR   A CB  1 
ATOM   1517 O OG1 . THR   A 1 198 ? -8.12499  -29.49618 2.87581   1.000 31.01948  ? 198 THR   A OG1 1 
ATOM   1518 C CG2 . THR   A 1 198 ? -7.28755  -31.49619 1.80084   1.000 42.47309  ? 198 THR   A CG2 1 
ATOM   1519 N N   . THR   A 1 199 ? -11.53414 -30.77762 2.94295   1.000 31.95406  ? 199 THR   A N   1 
ATOM   1520 C CA  . THR   A 1 199 ? -12.68248 -30.24146 3.65188   1.000 32.29244  ? 199 THR   A CA  1 
ATOM   1521 C C   . THR   A 1 199 ? -12.22918 -29.46834 4.89106   1.000 33.28624  ? 199 THR   A C   1 
ATOM   1522 O O   . THR   A 1 199 ? -11.30999 -29.90846 5.60122   1.000 30.98236  ? 199 THR   A O   1 
ATOM   1523 C CB  . THR   A 1 199 ? -13.64055 -31.36138 4.04006   1.000 33.32067  ? 199 THR   A CB  1 
ATOM   1524 O OG1 . THR   A 1 199 ? -14.13595 -31.98516 2.85125   1.000 34.40482  ? 199 THR   A OG1 1 
ATOM   1525 C CG2 . THR   A 1 199 ? -14.79895 -30.79898 4.81714   1.000 31.26944  ? 199 THR   A CG2 1 
ATOM   1526 N N   . ILE   A 1 200 ? -12.86663 -28.32568 5.13660   1.000 28.07763  ? 200 ILE   A N   1 
ATOM   1527 C CA  . ILE   A 1 200 ? -12.50986 -27.42759 6.24636   1.000 28.79066  ? 200 ILE   A CA  1 
ATOM   1528 C C   . ILE   A 1 200 ? -13.10573 -28.01343 7.53010   1.000 30.46443  ? 200 ILE   A C   1 
ATOM   1529 O O   . ILE   A 1 200 ? -14.26458 -27.76249 7.85634   1.000 25.27559  ? 200 ILE   A O   1 
ATOM   1530 C CB  . ILE   A 1 200 ? -12.98791 -25.99681 6.01512   1.000 26.83289  ? 200 ILE   A CB  1 
ATOM   1531 C CG1 . ILE   A 1 200 ? -12.57226 -25.50765 4.62545   1.000 26.64649  ? 200 ILE   A CG1 1 
ATOM   1532 C CG2 . ILE   A 1 200 ? -12.48219 -25.09004 7.12862   1.000 25.08719  ? 200 ILE   A CG2 1 
ATOM   1533 C CD1 . ILE   A 1 200 ? -13.58210 -24.56513 3.99906   1.000 20.68585  ? 200 ILE   A CD1 1 
ATOM   1534 N N   . THR   A 1 201 ? -12.29388 -28.76372 8.27503   1.000 29.14791  ? 201 THR   A N   1 
ATOM   1535 C CA  . THR   A 1 201 ? -12.83370 -29.59132 9.34880   1.000 29.76734  ? 201 THR   A CA  1 
ATOM   1536 C C   . THR   A 1 201 ? -13.53469 -28.74600 10.41204  1.000 27.85386  ? 201 THR   A C   1 
ATOM   1537 O O   . THR   A 1 201 ? -14.68601 -29.02257 10.77797  1.000 27.33908  ? 201 THR   A O   1 
ATOM   1538 C CB  . THR   A 1 201 ? -11.71552 -30.42122 9.97478   1.000 34.27132  ? 201 THR   A CB  1 
ATOM   1539 O OG1 . THR   A 1 201 ? -10.95484 -31.07340 8.94730   1.000 33.89013  ? 201 THR   A OG1 1 
ATOM   1540 C CG2 . THR   A 1 201 ? -12.32202 -31.45912 10.87567  1.000 33.16811  ? 201 THR   A CG2 1 
ATOM   1541 N N   . VAL   A 1 202 ? -12.86407 -27.69590 10.90251  1.000 24.08944  ? 202 VAL   A N   1 
ATOM   1542 C CA  . VAL   A 1 202 ? -13.39795 -26.91812 12.01843  1.000 22.53316  ? 202 VAL   A CA  1 
ATOM   1543 C C   . VAL   A 1 202 ? -14.76672 -26.34664 11.66106  1.000 25.52881  ? 202 VAL   A C   1 
ATOM   1544 O O   . VAL   A 1 202 ? -15.67538 -26.31271 12.50675  1.000 22.33321  ? 202 VAL   A O   1 
ATOM   1545 C CB  . VAL   A 1 202 ? -12.37765 -25.83000 12.45309  1.000 29.21136  ? 202 VAL   A CB  1 
ATOM   1546 C CG1 . VAL   A 1 202 ? -12.03742 -24.86542 11.31756  1.000 20.83962  ? 202 VAL   A CG1 1 
ATOM   1547 C CG2 . VAL   A 1 202 ? -12.84712 -25.07260 13.71398  1.000 27.81439  ? 202 VAL   A CG2 1 
ATOM   1548 N N   . ASN   A 1 203 ? -14.95953 -25.97121 10.38819  1.000 24.94298  ? 203 ASN   A N   1 
ATOM   1549 C CA  . ASN   A 1 203 ? -16.24201 -25.45874 9.92692   1.000 20.29542  ? 203 ASN   A CA  1 
ATOM   1550 C C   . ASN   A 1 203 ? -17.31466 -26.54821 9.94923   1.000 24.00923  ? 203 ASN   A C   1 
ATOM   1551 O O   . ASN   A 1 203 ? -18.44409 -26.30639 10.39901  1.000 19.61519  ? 203 ASN   A O   1 
ATOM   1552 C CB  . ASN   A 1 203 ? -16.09090 -24.86915 8.52627   1.000 21.32334  ? 203 ASN   A CB  1 
ATOM   1553 C CG  . ASN   A 1 203 ? -15.29993 -23.56228 8.51225   1.000 24.11765  ? 203 ASN   A CG  1 
ATOM   1554 O OD1 . ASN   A 1 203 ? -14.83648 -23.08221 9.55308   1.000 26.09196  ? 203 ASN   A OD1 1 
ATOM   1555 N ND2 . ASN   A 1 203 ? -15.12202 -22.99251 7.32265   1.000 21.16657  ? 203 ASN   A ND2 1 
ATOM   1556 N N   . VAL   A 1 204 ? -16.97979 -27.75884 9.48542   1.000 26.23790  ? 204 VAL   A N   1 
ATOM   1557 C CA  . VAL   A 1 204 ? -17.92667 -28.86922 9.58024   1.000 24.28463  ? 204 VAL   A CA  1 
ATOM   1558 C C   . VAL   A 1 204 ? -18.36792 -29.05922 11.01713  1.000 22.30383  ? 204 VAL   A C   1 
ATOM   1559 O O   . VAL   A 1 204 ? -19.55616 -29.27306 11.29780  1.000 22.20636  ? 204 VAL   A O   1 
ATOM   1560 C CB  . VAL   A 1 204 ? -17.32454 -30.16891 9.02048   1.000 22.00196  ? 204 VAL   A CB  1 
ATOM   1561 C CG1 . VAL   A 1 204 ? -18.27128 -31.32265 9.30645   1.000 23.89198  ? 204 VAL   A CG1 1 
ATOM   1562 C CG2 . VAL   A 1 204 ? -17.12140 -30.05425 7.54652   1.000 25.46319  ? 204 VAL   A CG2 1 
ATOM   1563 N N   . LEU   A 1 205 ? -17.41518 -28.98938 11.95061  1.000 24.09561  ? 205 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 205 ? -17.75665 -29.07127 13.36587  1.000 23.32708  ? 205 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 205 ? -18.67140 -27.92289 13.79175  1.000 22.70207  ? 205 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 205 ? -19.65822 -28.14494 14.49040  1.000 23.32451  ? 205 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 205 ? -16.47684 -29.10404 14.20579  1.000 26.48192  ? 205 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 205 ? -15.60190 -30.33768 13.97874  1.000 25.06527  ? 205 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 205 ? -14.27845 -30.17635 14.66334  1.000 29.78851  ? 205 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 205 ? -16.29409 -31.58026 14.48388  1.000 26.39422  ? 205 LEU   A CD2 1 
ATOM   1571 N N   . ALA   A 1 206 ? -18.36023 -26.68870 13.38319  1.000 21.60728  ? 206 ALA   A N   1 
ATOM   1572 C CA  . ALA   A 1 206 ? -19.16951 -25.54967 13.79449  1.000 21.17980  ? 206 ALA   A CA  1 
ATOM   1573 C C   . ALA   A 1 206 ? -20.58407 -25.66304 13.24870  1.000 20.92138  ? 206 ALA   A C   1 
ATOM   1574 O O   . ALA   A 1 206 ? -21.55456 -25.28983 13.92503  1.000 21.25158  ? 206 ALA   A O   1 
ATOM   1575 C CB  . ALA   A 1 206 ? -18.51302 -24.25279 13.33106  1.000 20.16546  ? 206 ALA   A CB  1 
ATOM   1576 N N   . TRP   A 1 207 ? -20.71833 -26.18638 12.02507  1.000 20.48306  ? 207 TRP   A N   1 
ATOM   1577 C CA  . TRP   A 1 207 ? -22.03449 -26.42267 11.43864  1.000 21.94409  ? 207 TRP   A CA  1 
ATOM   1578 C C   . TRP   A 1 207 ? -22.81560 -27.48446 12.22948  1.000 24.16156  ? 207 TRP   A C   1 
ATOM   1579 O O   . TRP   A 1 207 ? -24.00302 -27.29898 12.51797  1.000 26.15699  ? 207 TRP   A O   1 
ATOM   1580 C CB  . TRP   A 1 207 ? -21.84922 -26.80611 9.96936   1.000 19.92502  ? 207 TRP   A CB  1 
ATOM   1581 C CG  . TRP   A 1 207 ? -23.05141 -27.27797 9.20933   1.000 26.81982  ? 207 TRP   A CG  1 
ATOM   1582 C CD1 . TRP   A 1 207 ? -24.08967 -26.50960 8.72196   1.000 26.27866  ? 207 TRP   A CD1 1 
ATOM   1583 C CD2 . TRP   A 1 207 ? -23.30953 -28.61398 8.77493   1.000 24.25370  ? 207 TRP   A CD2 1 
ATOM   1584 N NE1 . TRP   A 1 207 ? -24.98239 -27.30236 8.03515   1.000 20.22830  ? 207 TRP   A NE1 1 
ATOM   1585 C CE2 . TRP   A 1 207 ? -24.52607 -28.59442 8.04575   1.000 25.37407  ? 207 TRP   A CE2 1 
ATOM   1586 C CE3 . TRP   A 1 207 ? -22.62916 -29.82412 8.91913   1.000 23.99196  ? 207 TRP   A CE3 1 
ATOM   1587 C CZ2 . TRP   A 1 207 ? -25.08344 -29.74766 7.48478   1.000 27.49461  ? 207 TRP   A CZ2 1 
ATOM   1588 C CZ3 . TRP   A 1 207 ? -23.19074 -30.97466 8.36598   1.000 31.47108  ? 207 TRP   A CZ3 1 
ATOM   1589 C CH2 . TRP   A 1 207 ? -24.41137 -30.92484 7.65989   1.000 29.02604  ? 207 TRP   A CH2 1 
ATOM   1590 N N   . LEU   A 1 208 ? -22.15369 -28.57892 12.62649  1.000 22.56927  ? 208 LEU   A N   1 
ATOM   1591 C CA  . LEU   A 1 208 ? -22.77055 -29.57090 13.51317  1.000 24.91889  ? 208 LEU   A CA  1 
ATOM   1592 C C   . LEU   A 1 208 ? -23.20510 -28.96396 14.84507  1.000 27.50073  ? 208 LEU   A C   1 
ATOM   1593 O O   . LEU   A 1 208 ? -24.22433 -29.38043 15.40969  1.000 27.81444  ? 208 LEU   A O   1 
ATOM   1594 C CB  . LEU   A 1 208 ? -21.80418 -30.73333 13.76364  1.000 24.91685  ? 208 LEU   A CB  1 
ATOM   1595 C CG  . LEU   A 1 208 ? -21.39103 -31.48883 12.48759  1.000 27.61442  ? 208 LEU   A CG  1 
ATOM   1596 C CD1 . LEU   A 1 208 ? -20.21098 -32.43853 12.70876  1.000 25.74430  ? 208 LEU   A CD1 1 
ATOM   1597 C CD2 . LEU   A 1 208 ? -22.58550 -32.23648 11.91250  1.000 27.33367  ? 208 LEU   A CD2 1 
ATOM   1598 N N   . TYR   A 1 209 ? -22.45199 -27.98988 15.37142  1.000 24.71184  ? 209 TYR   A N   1 
ATOM   1599 C CA  . TYR   A 1 209 ? -22.93319 -27.25771 16.54094  1.000 24.75171  ? 209 TYR   A CA  1 
ATOM   1600 C C   . TYR   A 1 209 ? -24.17607 -26.44286 16.20052  1.000 27.26937  ? 209 TYR   A C   1 
ATOM   1601 O O   . TYR   A 1 209 ? -25.15651 -26.45438 16.95508  1.000 27.04599  ? 209 TYR   A O   1 
ATOM   1602 C CB  . TYR   A 1 209 ? -21.83678 -26.36013 17.10577  1.000 24.83533  ? 209 TYR   A CB  1 
ATOM   1603 C CG  . TYR   A 1 209 ? -20.90983 -27.07602 18.04969  1.000 26.86340  ? 209 TYR   A CG  1 
ATOM   1604 C CD1 . TYR   A 1 209 ? -21.34180 -27.46857 19.30186  1.000 26.98092  ? 209 TYR   A CD1 1 
ATOM   1605 C CD2 . TYR   A 1 209 ? -19.59751 -27.37622 17.67262  1.000 27.51709  ? 209 TYR   A CD2 1 
ATOM   1606 C CE1 . TYR   A 1 209 ? -20.49365 -28.13524 20.17174  1.000 32.21153  ? 209 TYR   A CE1 1 
ATOM   1607 C CE2 . TYR   A 1 209 ? -18.74322 -28.04290 18.52841  1.000 30.65318  ? 209 TYR   A CE2 1 
ATOM   1608 C CZ  . TYR   A 1 209 ? -19.19289 -28.42367 19.77848  1.000 34.42515  ? 209 TYR   A CZ  1 
ATOM   1609 O OH  . TYR   A 1 209 ? -18.34064 -29.08772 20.63470  1.000 34.69640  ? 209 TYR   A OH  1 
ATOM   1610 N N   . ALA   A 1 210 ? -24.15376 -25.72535 15.06340  1.000 25.98017  ? 210 ALA   A N   1 
ATOM   1611 C CA  . ALA   A 1 210 ? -25.35587 -25.03869 14.61440  1.000 24.87315  ? 210 ALA   A CA  1 
ATOM   1612 C C   . ALA   A 1 210 ? -26.54736 -25.98483 14.60760  1.000 29.65567  ? 210 ALA   A C   1 
ATOM   1613 O O   . ALA   A 1 210 ? -27.63717 -25.62506 15.05886  1.000 28.29718  ? 210 ALA   A O   1 
ATOM   1614 C CB  . ALA   A 1 210 ? -25.15403 -24.43882 13.22842  1.000 22.42553  ? 210 ALA   A CB  1 
ATOM   1615 N N   . ALA   A 1 211 ? -26.35063 -27.20884 14.12067  1.000 27.08107  ? 211 ALA   A N   1 
ATOM   1616 C CA  . ALA   A 1 211 ? -27.43432 -28.18085 14.11979  1.000 33.58209  ? 211 ALA   A CA  1 
ATOM   1617 C C   . ALA   A 1 211 ? -27.95095 -28.43160 15.53462  1.000 34.43712  ? 211 ALA   A C   1 
ATOM   1618 O O   . ALA   A 1 211 ? -29.15879 -28.36429 15.78466  1.000 36.60506  ? 211 ALA   A O   1 
ATOM   1619 C CB  . ALA   A 1 211 ? -26.96307 -29.47709 13.46185  1.000 34.85455  ? 211 ALA   A CB  1 
ATOM   1620 N N   . VAL   A 1 212 ? -27.04778 -28.68549 16.48598  1.000 29.20803  ? 212 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 212 ? -27.48707 -28.93485 17.85874  1.000 35.91139  ? 212 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 212 ? -28.25352 -27.73071 18.40933  1.000 32.89078  ? 212 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 212 ? -29.24535 -27.89627 19.13731  1.000 31.38235  ? 212 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 212 ? -26.28984 -29.33031 18.75548  1.000 36.42090  ? 212 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 212 ? -26.66300 -29.25971 20.26075  1.000 30.87897  ? 212 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 212 ? -25.80035 -30.73950 18.40497  1.000 32.43235  ? 212 VAL   A CG2 1 
ATOM   1627 N N   . ILE   A 1 213 ? -27.82566 -26.50666 18.04918  1.000 33.62273  ? 213 ILE   A N   1 
ATOM   1628 C CA  . ILE   A 1 213 ? -28.49069 -25.28099 18.49890  1.000 27.18124  ? 213 ILE   A CA  1 
ATOM   1629 C C   . ILE   A 1 213 ? -29.88736 -25.18113 17.91000  1.000 30.00279  ? 213 ILE   A C   1 
ATOM   1630 O O   . ILE   A 1 213 ? -30.80393 -24.66133 18.57258  1.000 36.65174  ? 213 ILE   A O   1 
ATOM   1631 C CB  . ILE   A 1 213 ? -27.64344 -24.04600 18.13568  1.000 32.18248  ? 213 ILE   A CB  1 
ATOM   1632 C CG1 . ILE   A 1 213 ? -26.39879 -23.95572 19.01154  1.000 31.47285  ? 213 ILE   A CG1 1 
ATOM   1633 C CG2 . ILE   A 1 213 ? -28.47407 -22.75382 18.17902  1.000 28.36087  ? 213 ILE   A CG2 1 
ATOM   1634 C CD1 . ILE   A 1 213 ? -25.34889 -22.98603 18.46923  1.000 24.64702  ? 213 ILE   A CD1 1 
ATOM   1635 N N   . ASN   A 1 214 ? -30.08713 -25.72642 16.68889  1.000 27.50542  ? 214 ASN   A N   1 
ATOM   1636 C CA  . ASN   A 1 214 ? -31.35497 -25.68522 15.94595  1.000 33.27936  ? 214 ASN   A CA  1 
ATOM   1637 C C   . ASN   A 1 214 ? -32.21227 -26.93548 16.02629  1.000 39.77795  ? 214 ASN   A C   1 
ATOM   1638 O O   . ASN   A 1 214 ? -33.19846 -27.04831 15.27988  1.000 38.90455  ? 214 ASN   A O   1 
ATOM   1639 C CB  . ASN   A 1 214 ? -31.12350 -25.36016 14.48304  1.000 28.31182  ? 214 ASN   A CB  1 
ATOM   1640 C CG  . ASN   A 1 214 ? -30.89429 -23.87887 14.24571  1.000 33.76609  ? 214 ASN   A CG  1 
ATOM   1641 O OD1 . ASN   A 1 214 ? -29.79201 -23.44304 13.95770  1.000 26.82063  ? 214 ASN   A OD1 1 
ATOM   1642 N ND2 . ASN   A 1 214 ? -32.00461 -23.13792 14.14520  1.000 41.08260  ? 214 ASN   A ND2 1 
ATOM   1643 N N   . GLY   A 1 215 ? -31.90600 -27.85358 16.93318  1.000 39.63016  ? 215 GLY   A N   1 
ATOM   1644 C CA  . GLY   A 1 215 ? -32.79567 -28.94267 17.24397  1.000 42.58349  ? 215 GLY   A CA  1 
ATOM   1645 C C   . GLY   A 1 215 ? -32.32900 -30.31931 16.76680  1.000 50.27285  ? 215 GLY   A C   1 
ATOM   1646 O O   . GLY   A 1 215 ? -32.63759 -31.31723 17.44126  1.000 57.87212  ? 215 GLY   A O   1 
ATOM   1647 N N   . ASP   A 1 216 ? -31.53126 -30.42598 15.66291  1.000 61.37440  ? 216 ASP   A N   1 
ATOM   1648 C CA  . ASP   A 1 216 ? -31.05520 -31.78423 15.31846  1.000 66.89639  ? 216 ASP   A CA  1 
ATOM   1649 C C   . ASP   A 1 216 ? -30.09935 -32.28738 16.39289  1.000 65.65849  ? 216 ASP   A C   1 
ATOM   1650 O O   . ASP   A 1 216 ? -29.30037 -31.54035 16.95966  1.000 63.55451  ? 216 ASP   A O   1 
ATOM   1651 C CB  . ASP   A 1 216 ? -30.29657 -32.02323 13.98585  1.000 66.70968  ? 216 ASP   A CB  1 
ATOM   1652 C CG  . ASP   A 1 216 ? -31.05934 -31.71465 12.74614  1.000 72.59379  ? 216 ASP   A CG  1 
ATOM   1653 O OD1 . ASP   A 1 216 ? -32.19462 -31.37273 12.86803  1.000 82.42770  ? 216 ASP   A OD1 1 
ATOM   1654 O OD2 . ASP   A 1 216 ? -30.60315 -32.10094 11.64682  1.000 68.05005  ? 216 ASP   A OD2 1 
ATOM   1655 N N   . ARG   A 1 217 ? -30.24758 -33.51432 16.72232  1.000 48.24029  ? 217 ARG   A N   1 
ATOM   1656 C CA  . ARG   A 1 217 ? -29.37566 -34.08474 17.72708  1.000 40.77951  ? 217 ARG   A CA  1 
ATOM   1657 C C   . ARG   A 1 217 ? -29.09324 -35.55548 17.48158  1.000 43.65782  ? 217 ARG   A C   1 
ATOM   1658 O O   . ARG   A 1 217 ? -28.39199 -36.17084 18.28896  1.000 44.19076  ? 217 ARG   A O   1 
ATOM   1659 C CB  . ARG   A 1 217 ? -30.03060 -33.84685 19.05501  1.000 43.66493  ? 217 ARG   A CB  1 
ATOM   1660 C CG  . ARG   A 1 217 ? -29.07497 -33.63685 20.20484  1.000 45.44293  ? 217 ARG   A CG  1 
ATOM   1661 C CD  . ARG   A 1 217 ? -29.81412 -33.34592 21.52257  1.000 40.25167  ? 217 ARG   A CD  1 
ATOM   1662 N NE  . ARG   A 1 217 ? -29.02528 -33.91164 22.60025  1.000 41.84973  ? 217 ARG   A NE  1 
ATOM   1663 C CZ  . ARG   A 1 217 ? -28.00005 -33.29492 23.17070  1.000 43.13768  ? 217 ARG   A CZ  1 
ATOM   1664 N NH1 . ARG   A 1 217 ? -27.31501 -33.91001 24.11983  1.000 40.46339  ? 217 ARG   A NH1 1 
ATOM   1665 N NH2 . ARG   A 1 217 ? -27.64110 -32.07634 22.77571  1.000 40.29173  ? 217 ARG   A NH2 1 
ATOM   1666 N N   . TRP   A 1 218 ? -29.52815 -36.11019 16.34365  1.000 45.11308  ? 218 TRP   A N   1 
ATOM   1667 C CA  . TRP   A 1 218 ? -29.43213 -37.52940 16.04747  1.000 36.32451  ? 218 TRP   A CA  1 
ATOM   1668 C C   . TRP   A 1 218 ? -28.00258 -38.00462 15.83434  1.000 42.19235  ? 218 TRP   A C   1 
ATOM   1669 O O   . TRP   A 1 218 ? -27.73283 -39.19952 16.01557  1.000 41.97105  ? 218 TRP   A O   1 
ATOM   1670 C CB  . TRP   A 1 218 ? -30.26731 -37.82723 14.81442  1.000 36.86642  ? 218 TRP   A CB  1 
ATOM   1671 C CG  . TRP   A 1 218 ? -29.76819 -37.24157 13.46541  1.000 46.26666  ? 218 TRP   A CG  1 
ATOM   1672 C CD1 . TRP   A 1 218 ? -30.23997 -36.11763 12.83232  1.000 44.08002  ? 218 TRP   A CD1 1 
ATOM   1673 C CD2 . TRP   A 1 218 ? -28.77545 -37.80449 12.57592  1.000 45.30949  ? 218 TRP   A CD2 1 
ATOM   1674 N NE1 . TRP   A 1 218 ? -29.60686 -35.94712 11.62732  1.000 45.32867  ? 218 TRP   A NE1 1 
ATOM   1675 C CE2 . TRP   A 1 218 ? -28.70023 -36.95593 11.44433  1.000 47.43677  ? 218 TRP   A CE2 1 
ATOM   1676 C CE3 . TRP   A 1 218 ? -27.93812 -38.93042 12.62996  1.000 42.26148  ? 218 TRP   A CE3 1 
ATOM   1677 C CZ2 . TRP   A 1 218 ? -27.81827 -37.19010 10.37750  1.000 46.22281  ? 218 TRP   A CZ2 1 
ATOM   1678 C CZ3 . TRP   A 1 218 ? -27.05781 -39.16325 11.55858  1.000 45.53822  ? 218 TRP   A CZ3 1 
ATOM   1679 C CH2 . TRP   A 1 218 ? -27.00998 -38.29176 10.45123  1.000 44.36779  ? 218 TRP   A CH2 1 
ATOM   1680 N N   . PHE   A 1 219 ? -27.08048 -37.10816 15.47722  1.000 37.84557  ? 219 PHE   A N   1 
ATOM   1681 C CA  . PHE   A 1 219 ? -25.74365 -37.52464 15.06802  1.000 37.51038  ? 219 PHE   A CA  1 
ATOM   1682 C C   . PHE   A 1 219 ? -24.75793 -37.66181 16.22391  1.000 36.27179  ? 219 PHE   A C   1 
ATOM   1683 O O   . PHE   A 1 219 ? -23.59833 -38.01715 15.98304  1.000 36.19548  ? 219 PHE   A O   1 
ATOM   1684 C CB  . PHE   A 1 219 ? -25.17970 -36.55321 14.02835  1.000 31.45506  ? 219 PHE   A CB  1 
ATOM   1685 C CG  . PHE   A 1 219 ? -25.36710 -35.11021 14.39166  1.000 38.66155  ? 219 PHE   A CG  1 
ATOM   1686 C CD1 . PHE   A 1 219 ? -24.43457 -34.45348 15.18316  1.000 36.82318  ? 219 PHE   A CD1 1 
ATOM   1687 C CD2 . PHE   A 1 219 ? -26.49185 -34.40501 13.96028  1.000 40.94259  ? 219 PHE   A CD2 1 
ATOM   1688 C CE1 . PHE   A 1 219 ? -24.60759 -33.11894 15.52399  1.000 36.04089  ? 219 PHE   A CE1 1 
ATOM   1689 C CE2 . PHE   A 1 219 ? -26.67199 -33.07385 14.30452  1.000 39.47233  ? 219 PHE   A CE2 1 
ATOM   1690 C CZ  . PHE   A 1 219 ? -25.73091 -32.43015 15.09261  1.000 36.37135  ? 219 PHE   A CZ  1 
ATOM   1691 N N   . LEU   A 1 220 ? -25.18175 -37.42093 17.46163  1.000 38.47614  ? 220 LEU   A N   1 
ATOM   1692 C CA  . LEU   A 1 220 ? -24.29282 -37.48551 18.61918  1.000 40.88122  ? 220 LEU   A CA  1 
ATOM   1693 C C   . LEU   A 1 220 ? -24.11941 -38.92872 19.12932  1.000 41.03355  ? 220 LEU   A C   1 
ATOM   1694 O O   . LEU   A 1 220 ? -24.78459 -39.86647 18.67954  1.000 40.29111  ? 220 LEU   A O   1 
ATOM   1695 C CB  . LEU   A 1 220 ? -24.82625 -36.57706 19.73344  1.000 38.70493  ? 220 LEU   A CB  1 
ATOM   1696 C CG  . LEU   A 1 220 ? -25.08046 -35.11299 19.35337  1.000 40.21482  ? 220 LEU   A CG  1 
ATOM   1697 C CD1 . LEU   A 1 220 ? -25.60212 -34.31141 20.54381  1.000 40.13733  ? 220 LEU   A CD1 1 
ATOM   1698 C CD2 . LEU   A 1 220 ? -23.82328 -34.47167 18.77974  1.000 37.96682  ? 220 LEU   A CD2 1 
ATOM   1699 N N   . ASN   A 1 221 ? -23.20510 -39.09456 20.08798  1.000 44.00630  ? 221 ASN   A N   1 
ATOM   1700 C CA  . ASN   A 1 221 ? -22.89016 -40.39582 20.67944  1.000 52.52482  ? 221 ASN   A CA  1 
ATOM   1701 C C   . ASN   A 1 221 ? -22.27926 -40.18187 22.05787  1.000 52.17109  ? 221 ASN   A C   1 
ATOM   1702 O O   . ASN   A 1 221 ? -21.96083 -39.04730 22.43062  1.000 46.86802  ? 221 ASN   A O   1 
ATOM   1703 C CB  . ASN   A 1 221 ? -21.97890 -41.22838 19.75239  1.000 53.80120  ? 221 ASN   A CB  1 
ATOM   1704 C CG  . ASN   A 1 221 ? -20.68381 -40.50654 19.34599  1.000 52.33726  ? 221 ASN   A CG  1 
ATOM   1705 O OD1 . ASN   A 1 221 ? -20.28901 -39.50228 19.93659  1.000 53.80115  ? 221 ASN   A OD1 1 
ATOM   1706 N ND2 . ASN   A 1 221 ? -20.06426 -40.98787 18.27284  1.000 51.93154  ? 221 ASN   A ND2 1 
ATOM   1707 N N   . ARG   A 1 222 ? -22.17834 -41.27395 22.85188  1.000 57.14956  ? 222 ARG   A N   1 
ATOM   1708 C CA  . ARG   A 1 222 ? -21.41279 -41.11515 24.08562  1.000 58.21584  ? 222 ARG   A CA  1 
ATOM   1709 C C   . ARG   A 1 222 ? -19.92947 -41.36472 23.85840  1.000 60.24535  ? 222 ARG   A C   1 
ATOM   1710 O O   . ARG   A 1 222 ? -19.13189 -41.12575 24.77008  1.000 64.13444  ? 222 ARG   A O   1 
ATOM   1711 C CB  . ARG   A 1 222 ? -21.90628 -41.97451 25.29751  1.000 60.55651  ? 222 ARG   A CB  1 
ATOM   1712 C CG  . ARG   A 1 222 ? -21.39510 -43.43944 25.63508  1.000 61.91132  ? 222 ARG   A CG  1 
ATOM   1713 C CD  . ARG   A 1 222 ? -22.05915 -44.53388 24.86276  1.000 62.95806  ? 222 ARG   A CD  1 
ATOM   1714 N NE  . ARG   A 1 222 ? -21.78358 -45.92209 25.28121  1.000 64.87507  ? 222 ARG   A NE  1 
ATOM   1715 C CZ  . ARG   A 1 222 ? -20.88807 -46.71869 24.71187  1.000 67.18408  ? 222 ARG   A CZ  1 
ATOM   1716 N NH1 . ARG   A 1 222 ? -20.23444 -46.30134 23.64034  1.000 68.33423  ? 222 ARG   A NH1 1 
ATOM   1717 N NH2 . ARG   A 1 222 ? -20.70905 -47.95348 25.15628  1.000 74.14671  ? 222 ARG   A NH2 1 
ATOM   1718 N N   . PHE   A 1 223 ? -19.53296 -41.76272 22.65164  1.000 64.67804  ? 223 PHE   A N   1 
ATOM   1719 C CA  . PHE   A 1 223 ? -18.11474 -41.84996 22.33867  1.000 61.85863  ? 223 PHE   A CA  1 
ATOM   1720 C C   . PHE   A 1 223 ? -17.43332 -40.50560 22.55096  1.000 60.28601  ? 223 PHE   A C   1 
ATOM   1721 O O   . PHE   A 1 223 ? -18.05531 -39.44321 22.47762  1.000 57.09165  ? 223 PHE   A O   1 
ATOM   1722 C CB  . PHE   A 1 223 ? -17.91151 -42.29056 20.89402  1.000 61.42326  ? 223 PHE   A CB  1 
ATOM   1723 C CG  . PHE   A 1 223 ? -18.46801 -43.64286 20.59164  1.000 71.63459  ? 223 PHE   A CG  1 
ATOM   1724 C CD1 . PHE   A 1 223 ? -18.03715 -44.76012 21.29120  1.000 76.75721  ? 223 PHE   A CD1 1 
ATOM   1725 C CD2 . PHE   A 1 223 ? -19.43943 -43.79694 19.61376  1.000 72.09588  ? 223 PHE   A CD2 1 
ATOM   1726 C CE1 . PHE   A 1 223 ? -18.55799 -46.00984 21.00658  1.000 80.40248  ? 223 PHE   A CE1 1 
ATOM   1727 C CE2 . PHE   A 1 223 ? -19.96761 -45.03982 19.32851  1.000 75.54108  ? 223 PHE   A CE2 1 
ATOM   1728 C CZ  . PHE   A 1 223 ? -19.52697 -46.14864 20.02521  1.000 79.63066  ? 223 PHE   A CZ  1 
ATOM   1729 N N   . THR   A 1 224 ? -16.14304 -40.56740 22.84050  1.000 57.49676  ? 224 THR   A N   1 
ATOM   1730 C CA  . THR   A 1 224 ? -15.25273 -39.42673 22.72600  1.000 49.23233  ? 224 THR   A CA  1 
ATOM   1731 C C   . THR   A 1 224 ? -14.00539 -39.92402 22.01455  1.000 53.63114  ? 224 THR   A C   1 
ATOM   1732 O O   . THR   A 1 224 ? -13.86233 -41.12072 21.74605  1.000 60.35398  ? 224 THR   A O   1 
ATOM   1733 C CB  . THR   A 1 224 ? -14.93306 -38.81086 24.09750  1.000 50.63856  ? 224 THR   A CB  1 
ATOM   1734 O OG1 . THR   A 1 224 ? -14.41451 -37.48964 23.91738  1.000 48.56117  ? 224 THR   A OG1 1 
ATOM   1735 C CG2 . THR   A 1 224 ? -13.92380 -39.67266 24.87476  1.000 46.01555  ? 224 THR   A CG2 1 
ATOM   1736 N N   . THR   A 1 225 ? -13.09917 -39.00668 21.69225  1.000 52.10747  ? 225 THR   A N   1 
ATOM   1737 C CA  . THR   A 1 225 ? -11.86242 -39.40666 21.04014  1.000 49.94304  ? 225 THR   A CA  1 
ATOM   1738 C C   . THR   A 1 225 ? -10.79037 -38.37240 21.34583  1.000 46.52672  ? 225 THR   A C   1 
ATOM   1739 O O   . THR   A 1 225 ? -11.08486 -37.24643 21.75294  1.000 47.52884  ? 225 THR   A O   1 
ATOM   1740 C CB  . THR   A 1 225 ? -12.05105 -39.58729 19.52180  1.000 48.65948  ? 225 THR   A CB  1 
ATOM   1741 O OG1 . THR   A 1 225 ? -10.92330 -40.28627 18.97227  1.000 53.38304  ? 225 THR   A OG1 1 
ATOM   1742 C CG2 . THR   A 1 225 ? -12.20035 -38.25589 18.82952  1.000 41.10583  ? 225 THR   A CG2 1 
ATOM   1743 N N   . THR   A 1 226 ? -9.53591  -38.78695 21.19211  1.000 47.58854  ? 226 THR   A N   1 
ATOM   1744 C CA  . THR   A 1 226 ? -8.42719  -37.86046 21.34459  1.000 53.57057  ? 226 THR   A CA  1 
ATOM   1745 C C   . THR   A 1 226 ? -8.25279  -37.07201 20.05821  1.000 49.77613  ? 226 THR   A C   1 
ATOM   1746 O O   . THR   A 1 226 ? -8.69837  -37.48641 18.98392  1.000 45.19141  ? 226 THR   A O   1 
ATOM   1747 C CB  . THR   A 1 226 ? -7.11110  -38.58703 21.68896  1.000 54.60376  ? 226 THR   A CB  1 
ATOM   1748 O OG1 . THR   A 1 226 ? -6.76871  -39.51237 20.64872  1.000 55.70641  ? 226 THR   A OG1 1 
ATOM   1749 C CG2 . THR   A 1 226 ? -7.21801  -39.34667 23.01493  1.000 46.88881  ? 226 THR   A CG2 1 
ATOM   1750 N N   . LEU   A 1 227 ? -7.59841  -35.91382 20.18113  1.000 49.71182  ? 227 LEU   A N   1 
ATOM   1751 C CA  . LEU   A 1 227 ? -7.27825  -35.11840 18.99790  1.000 51.96070  ? 227 LEU   A CA  1 
ATOM   1752 C C   . LEU   A 1 227 ? -6.42367  -35.91730 18.02386  1.000 51.84682  ? 227 LEU   A C   1 
ATOM   1753 O O   . LEU   A 1 227 ? -6.73877  -35.99834 16.82956  1.000 51.79442  ? 227 LEU   A O   1 
ATOM   1754 C CB  . LEU   A 1 227 ? -6.56426  -33.82906 19.39681  1.000 53.07298  ? 227 LEU   A CB  1 
ATOM   1755 C CG  . LEU   A 1 227 ? -6.46108  -32.80569 18.26855  1.000 47.79814  ? 227 LEU   A CG  1 
ATOM   1756 C CD1 . LEU   A 1 227 ? -7.81851  -32.63075 17.59614  1.000 43.23265  ? 227 LEU   A CD1 1 
ATOM   1757 C CD2 . LEU   A 1 227 ? -5.90198  -31.48544 18.78545  1.000 46.99034  ? 227 LEU   A CD2 1 
ATOM   1758 N N   . ASN   A 1 228 ? -5.33841  -36.51842 18.52696  1.000 49.72484  ? 228 ASN   A N   1 
ATOM   1759 C CA  . ASN   A 1 228 ? -4.49452  -37.37780 17.70735  1.000 53.27785  ? 228 ASN   A CA  1 
ATOM   1760 C C   . ASN   A 1 228 ? -5.32689  -38.37777 16.90891  1.000 53.46527  ? 228 ASN   A C   1 
ATOM   1761 O O   . ASN   A 1 228 ? -5.18336  -38.47948 15.68554  1.000 53.22740  ? 228 ASN   A O   1 
ATOM   1762 C CB  . ASN   A 1 228 ? -3.47622  -38.11006 18.59193  1.000 63.09950  ? 228 ASN   A CB  1 
ATOM   1763 C CG  . ASN   A 1 228 ? -2.22320  -37.27619 18.87343  1.000 66.29452  ? 228 ASN   A CG  1 
ATOM   1764 O OD1 . ASN   A 1 228 ? -1.88068  -36.37705 18.11334  1.000 64.83153  ? 228 ASN   A OD1 1 
ATOM   1765 N ND2 . ASN   A 1 228 ? -1.51855  -37.60500 19.95023  1.000 70.11952  ? 228 ASN   A ND2 1 
ATOM   1766 N N   . ASP   A 1 229 ? -6.22213  -39.11355 17.58463  1.000 50.93127  ? 229 ASP   A N   1 
ATOM   1767 C CA  . ASP   A 1 229 ? -6.97702  -40.16624 16.90552  1.000 50.09858  ? 229 ASP   A CA  1 
ATOM   1768 C C   . ASP   A 1 229 ? -7.99740  -39.58185 15.94134  1.000 50.95892  ? 229 ASP   A C   1 
ATOM   1769 O O   . ASP   A 1 229 ? -8.32310  -40.20592 14.92144  1.000 50.75608  ? 229 ASP   A O   1 
ATOM   1770 C CB  . ASP   A 1 229 ? -7.69172  -41.07640 17.91653  1.000 49.09523  ? 229 ASP   A CB  1 
ATOM   1771 C CG  . ASP   A 1 229 ? -6.74123  -42.00568 18.66167  1.000 51.53522  ? 229 ASP   A CG  1 
ATOM   1772 O OD1 . ASP   A 1 229 ? -5.63822  -42.30491 18.15108  1.000 49.59980  ? 229 ASP   A OD1 1 
ATOM   1773 O OD2 . ASP   A 1 229 ? -7.11159  -42.44611 19.76859  1.000 50.86468  ? 229 ASP   A OD2 1 
ATOM   1774 N N   . PHE   A 1 230 ? -8.53344  -38.40330 16.25208  1.000 51.29135  ? 230 PHE   A N   1 
ATOM   1775 C CA  . PHE   A 1 230 ? -9.47647  -37.79277 15.32782  1.000 48.22867  ? 230 PHE   A CA  1 
ATOM   1776 C C   . PHE   A 1 230 ? -8.78985  -37.44704 14.01505  1.000 47.73707  ? 230 PHE   A C   1 
ATOM   1777 O O   . PHE   A 1 230 ? -9.31698  -37.73988 12.93518  1.000 48.63528  ? 230 PHE   A O   1 
ATOM   1778 C CB  . PHE   A 1 230 ? -10.11804 -36.54641 15.93682  1.000 45.08394  ? 230 PHE   A CB  1 
ATOM   1779 C CG  . PHE   A 1 230 ? -10.99357 -35.81477 14.97083  1.000 45.59668  ? 230 PHE   A CG  1 
ATOM   1780 C CD1 . PHE   A 1 230 ? -12.29492 -36.23505 14.74691  1.000 43.10884  ? 230 PHE   A CD1 1 
ATOM   1781 C CD2 . PHE   A 1 230 ? -10.49944 -34.75190 14.23148  1.000 39.40791  ? 230 PHE   A CD2 1 
ATOM   1782 C CE1 . PHE   A 1 230 ? -13.09007 -35.58380 13.83531  1.000 38.34804  ? 230 PHE   A CE1 1 
ATOM   1783 C CE2 . PHE   A 1 230 ? -11.28951 -34.10829 13.31850  1.000 38.93329  ? 230 PHE   A CE2 1 
ATOM   1784 C CZ  . PHE   A 1 230 ? -12.58427 -34.52074 13.11822  1.000 39.89743  ? 230 PHE   A CZ  1 
ATOM   1785 N N   . ASN   A 1 231 ? -7.60333  -36.82734 14.09159  1.000 50.85257  ? 231 ASN   A N   1 
ATOM   1786 C CA  . ASN   A 1 231 ? -6.88169  -36.42729 12.88279  1.000 48.04467  ? 231 ASN   A CA  1 
ATOM   1787 C C   . ASN   A 1 231 ? -6.53906  -37.63023 12.00478  1.000 48.72332  ? 231 ASN   A C   1 
ATOM   1788 O O   . ASN   A 1 231 ? -6.48061  -37.50047 10.77649  1.000 50.91011  ? 231 ASN   A O   1 
ATOM   1789 C CB  . ASN   A 1 231 ? -5.61325  -35.65877 13.26057  1.000 43.09370  ? 231 ASN   A CB  1 
ATOM   1790 C CG  . ASN   A 1 231 ? -5.90119  -34.26700 13.80627  1.000 44.17189  ? 231 ASN   A CG  1 
ATOM   1791 O OD1 . ASN   A 1 231 ? -6.88982  -33.62822 13.44580  1.000 45.41816  ? 231 ASN   A OD1 1 
ATOM   1792 N ND2 . ASN   A 1 231 ? -5.02885  -33.79061 14.68282  1.000 49.13230  ? 231 ASN   A ND2 1 
ATOM   1793 N N   . LEU   A 1 232 ? -6.32965  -38.80569 12.61199  1.000 48.03686  ? 232 LEU   A N   1 
ATOM   1794 C CA  . LEU   A 1 232 ? -6.03546  -40.01572 11.84271  1.000 50.43114  ? 232 LEU   A CA  1 
ATOM   1795 C C   . LEU   A 1 232 ? -7.20808  -40.39983 10.94477  1.000 50.73059  ? 232 LEU   A C   1 
ATOM   1796 O O   . LEU   A 1 232 ? -7.00904  -40.83216 9.79954   1.000 46.74265  ? 232 LEU   A O   1 
ATOM   1797 C CB  . LEU   A 1 232 ? -5.69435  -41.17437 12.79037  1.000 49.97002  ? 232 LEU   A CB  1 
ATOM   1798 C CG  . LEU   A 1 232 ? -4.23044  -41.50806 13.10958  1.000 48.78491  ? 232 LEU   A CG  1 
ATOM   1799 C CD1 . LEU   A 1 232 ? -3.55108  -40.32675 13.77371  1.000 46.63936  ? 232 LEU   A CD1 1 
ATOM   1800 C CD2 . LEU   A 1 232 ? -4.11349  -42.76300 13.98512  1.000 46.01728  ? 232 LEU   A CD2 1 
ATOM   1801 N N   . VAL   A 1 233 ? -8.43918  -40.26088 11.45861  1.000 51.24593  ? 233 VAL   A N   1 
ATOM   1802 C CA  . VAL   A 1 233 ? -9.63600  -40.53039 10.66134  1.000 50.52476  ? 233 VAL   A CA  1 
ATOM   1803 C C   . VAL   A 1 233 ? -9.87195  -39.41974 9.64267   1.000 52.87942  ? 233 VAL   A C   1 
ATOM   1804 O O   . VAL   A 1 233 ? -10.25324 -39.68034 8.49496   1.000 52.31612  ? 233 VAL   A O   1 
ATOM   1805 C CB  . VAL   A 1 233 ? -10.85350 -40.72043 11.58471  1.000 50.57825  ? 233 VAL   A CB  1 
ATOM   1806 C CG1 . VAL   A 1 233 ? -12.12398 -41.01783 10.75507  1.000 43.15701  ? 233 VAL   A CG1 1 
ATOM   1807 C CG2 . VAL   A 1 233 ? -10.57072 -41.83630 12.59413  1.000 46.34623  ? 233 VAL   A CG2 1 
ATOM   1808 N N   . ALA   A 1 234 ? -9.65746  -38.16817 10.05137  1.000 63.80349  ? 234 ALA   A N   1 
ATOM   1809 C CA  . ALA   A 1 234 ? -9.86291  -37.02493 9.17053   1.000 63.87506  ? 234 ALA   A CA  1 
ATOM   1810 C C   . ALA   A 1 234 ? -9.05593  -37.17637 7.88482   1.000 63.73185  ? 234 ALA   A C   1 
ATOM   1811 O O   . ALA   A 1 234 ? -9.62306  -37.25466 6.78111   1.000 65.46895  ? 234 ALA   A O   1 
ATOM   1812 C CB  . ALA   A 1 234 ? -9.49375  -35.73656 9.91770   1.000 63.02597  ? 234 ALA   A CB  1 
ATOM   1813 N N   . MET   A 1 235 ? -7.73113  -37.31293 8.02482   1.000 54.04171  ? 235 MET   A N   1 
ATOM   1814 C CA  . MET   A 1 235 ? -6.88029  -37.29666 6.85351   1.000 52.83444  ? 235 MET   A CA  1 
ATOM   1815 C C   . MET   A 1 235 ? -7.25691  -38.38763 5.89038   1.000 53.24918  ? 235 MET   A C   1 
ATOM   1816 O O   . MET   A 1 235 ? -7.14767  -38.16858 4.68636   1.000 50.83671  ? 235 MET   A O   1 
ATOM   1817 C CB  . MET   A 1 235 ? -5.42692  -37.38707 7.27035   1.000 58.11317  ? 235 MET   A CB  1 
ATOM   1818 C CG  . MET   A 1 235 ? -4.44054  -37.40437 6.18892   1.000 68.25510  ? 235 MET   A CG  1 
ATOM   1819 S SD  . MET   A 1 235 ? -2.78253  -37.36354 6.86374   1.000 89.84303  ? 235 MET   A SD  1 
ATOM   1820 C CE  . MET   A 1 235 ? -2.60672  -38.77630 7.92131   1.000 64.71706  ? 235 MET   A CE  1 
ATOM   1821 N N   . LYS   A 1 236 ? -7.74892  -39.53341 6.38033   1.000 53.44081  ? 236 LYS   A N   1 
ATOM   1822 C CA  . LYS   A 1 236 ? -8.25505  -40.55849 5.46618   1.000 50.71530  ? 236 LYS   A CA  1 
ATOM   1823 C C   . LYS   A 1 236 ? -9.34859  -39.99677 4.55356   1.000 50.96012  ? 236 LYS   A C   1 
ATOM   1824 O O   . LYS   A 1 236 ? -9.28935  -40.13368 3.32209   1.000 49.04488  ? 236 LYS   A O   1 
ATOM   1825 C CB  . LYS   A 1 236 ? -8.77662  -41.75619 6.25446   1.000 48.25924  ? 236 LYS   A CB  1 
ATOM   1826 C CG  . LYS   A 1 236 ? -9.36654  -42.80174 5.36276   1.000 44.38633  ? 236 LYS   A CG  1 
ATOM   1827 C CD  . LYS   A 1 236 ? -10.23672 -43.76460 6.13110   1.000 53.33920  ? 236 LYS   A CD  1 
ATOM   1828 C CE  . LYS   A 1 236 ? -11.43847 -44.23016 5.30952   1.000 54.11558  ? 236 LYS   A CE  1 
ATOM   1829 N NZ  . LYS   A 1 236 ? -11.13617 -45.36186 4.38875   1.000 56.46180  ? 236 LYS   A NZ  1 
ATOM   1830 N N   . TYR   A 1 237 ? -10.33146 -39.31651 5.14108   1.000 50.97166  ? 237 TYR   A N   1 
ATOM   1831 C CA  . TYR   A 1 237 ? -11.45852 -38.74158 4.42007   1.000 48.41899  ? 237 TYR   A CA  1 
ATOM   1832 C C   . TYR   A 1 237 ? -11.16241 -37.37641 3.83168   1.000 46.71054  ? 237 TYR   A C   1 
ATOM   1833 O O   . TYR   A 1 237 ? -12.11287 -36.65661 3.51410   1.000 40.33906  ? 237 TYR   A O   1 
ATOM   1834 C CB  . TYR   A 1 237 ? -12.67289 -38.65613 5.34380   1.000 44.63920  ? 237 TYR   A CB  1 
ATOM   1835 C CG  . TYR   A 1 237 ? -13.24442 -40.00870 5.66554   1.000 47.93956  ? 237 TYR   A CG  1 
ATOM   1836 C CD1 . TYR   A 1 237 ? -14.16351 -40.60867 4.81532   1.000 44.97863  ? 237 TYR   A CD1 1 
ATOM   1837 C CD2 . TYR   A 1 237 ? -12.85059 -40.70112 6.80513   1.000 47.74339  ? 237 TYR   A CD2 1 
ATOM   1838 C CE1 . TYR   A 1 237 ? -14.68450 -41.84770 5.09115   1.000 43.02926  ? 237 TYR   A CE1 1 
ATOM   1839 C CE2 . TYR   A 1 237 ? -13.36899 -41.94949 7.09086   1.000 48.30740  ? 237 TYR   A CE2 1 
ATOM   1840 C CZ  . TYR   A 1 237 ? -14.29296 -42.51855 6.22983   1.000 48.04574  ? 237 TYR   A CZ  1 
ATOM   1841 O OH  . TYR   A 1 237 ? -14.83200 -43.76315 6.49964   1.000 46.55374  ? 237 TYR   A OH  1 
ATOM   1842 N N   . ASN   A 1 238 ? -9.88559  -37.01285 3.68420   1.000 44.89654  ? 238 ASN   A N   1 
ATOM   1843 C CA  . ASN   A 1 238 ? -9.47793  -35.76474 3.03725   1.000 41.63557  ? 238 ASN   A CA  1 
ATOM   1844 C C   . ASN   A 1 238 ? -9.94323  -34.53642 3.81814   1.000 41.47993  ? 238 ASN   A C   1 
ATOM   1845 O O   . ASN   A 1 238 ? -10.26542 -33.49799 3.23524   1.000 38.65786  ? 238 ASN   A O   1 
ATOM   1846 C CB  . ASN   A 1 238 ? -9.98108  -35.69649 1.59487   1.000 37.24153  ? 238 ASN   A CB  1 
ATOM   1847 C CG  . ASN   A 1 238 ? -9.20002  -34.70035 0.75510   1.000 51.94040  ? 238 ASN   A CG  1 
ATOM   1848 O OD1 . ASN   A 1 238 ? -7.97461  -34.56514 0.90224   1.000 54.11004  ? 238 ASN   A OD1 1 
ATOM   1849 N ND2 . ASN   A 1 238 ? -9.91174  -33.96479 -0.11317  1.000 50.86149  ? 238 ASN   A ND2 1 
ATOM   1850 N N   . TYR   A 1 239 ? -9.99885  -34.63839 5.14085   1.000 43.61296  ? 239 TYR   A N   1 
ATOM   1851 C CA  . TYR   A 1 239 ? -10.30351 -33.48020 5.96325   1.000 39.93400  ? 239 TYR   A CA  1 
ATOM   1852 C C   . TYR   A 1 239 ? -9.00312  -32.80648 6.40533   1.000 38.45679  ? 239 TYR   A C   1 
ATOM   1853 O O   . TYR   A 1 239 ? -7.94204  -33.43094 6.49928   1.000 40.71977  ? 239 TYR   A O   1 
ATOM   1854 C CB  . TYR   A 1 239 ? -11.16499 -33.87940 7.17924   1.000 39.35863  ? 239 TYR   A CB  1 
ATOM   1855 C CG  . TYR   A 1 239 ? -12.65900 -33.87010 6.91007   1.000 38.47465  ? 239 TYR   A CG  1 
ATOM   1856 C CD1 . TYR   A 1 239 ? -13.18715 -34.50317 5.79098   1.000 39.51328  ? 239 TYR   A CD1 1 
ATOM   1857 C CD2 . TYR   A 1 239 ? -13.54492 -33.21017 7.76187   1.000 39.16332  ? 239 TYR   A CD2 1 
ATOM   1858 C CE1 . TYR   A 1 239 ? -14.55125 -34.48891 5.52302   1.000 34.25880  ? 239 TYR   A CE1 1 
ATOM   1859 C CE2 . TYR   A 1 239 ? -14.92401 -33.18797 7.50051   1.000 34.58908  ? 239 TYR   A CE2 1 
ATOM   1860 C CZ  . TYR   A 1 239 ? -15.41488 -33.83407 6.37401   1.000 34.76991  ? 239 TYR   A CZ  1 
ATOM   1861 O OH  . TYR   A 1 239 ? -16.76910 -33.82384 6.08296   1.000 34.88086  ? 239 TYR   A OH  1 
ATOM   1862 N N   . GLU   A 1 240 ? -9.09089  -31.50823 6.65433   1.000 41.23041  ? 240 GLU   A N   1 
ATOM   1863 C CA  . GLU   A 1 240 ? -7.97057  -30.81730 7.26405   1.000 41.35663  ? 240 GLU   A CA  1 
ATOM   1864 C C   . GLU   A 1 240 ? -7.70789  -31.37052 8.65485   1.000 39.22068  ? 240 GLU   A C   1 
ATOM   1865 O O   . GLU   A 1 240 ? -8.64452  -31.75533 9.36260   1.000 39.16449  ? 240 GLU   A O   1 
ATOM   1866 C CB  . GLU   A 1 240 ? -8.23965  -29.33338 7.42133   1.000 35.83013  ? 240 GLU   A CB  1 
ATOM   1867 C CG  . GLU   A 1 240 ? -8.01155  -28.49148 6.26661   1.000 37.11056  ? 240 GLU   A CG  1 
ATOM   1868 C CD  . GLU   A 1 240 ? -7.97298  -27.06323 6.72731   1.000 45.02440  ? 240 GLU   A CD  1 
ATOM   1869 O OE1 . GLU   A 1 240 ? -6.92410  -26.68217 7.29863   1.000 48.76907  ? 240 GLU   A OE1 1 
ATOM   1870 O OE2 . GLU   A 1 240 ? -8.98668  -26.34119 6.57586   1.000 42.95458  ? 240 GLU   A OE2 1 
ATOM   1871 N N   . PRO   A 1 241 ? -6.44949  -31.37033 9.08822   1.000 49.20421  ? 241 PRO   A N   1 
ATOM   1872 C CA  . PRO   A 1 241 ? -6.18071  -31.54980 10.51581  1.000 44.51158  ? 241 PRO   A CA  1 
ATOM   1873 C C   . PRO   A 1 241 ? -6.90883  -30.48336 11.31654  1.000 43.33990  ? 241 PRO   A C   1 
ATOM   1874 O O   . PRO   A 1 241 ? -7.16854  -29.37474 10.84286  1.000 41.38733  ? 241 PRO   A O   1 
ATOM   1875 C CB  . PRO   A 1 241 ? -4.65825  -31.39822 10.61494  1.000 40.15222  ? 241 PRO   A CB  1 
ATOM   1876 C CG  . PRO   A 1 241 ? -4.16943  -31.82441 9.26716   1.000 41.78082  ? 241 PRO   A CG  1 
ATOM   1877 C CD  . PRO   A 1 241 ? -5.20487  -31.30212 8.29882   1.000 45.97587  ? 241 PRO   A CD  1 
ATOM   1878 N N   . LEU   A 1 242 ? -7.28529  -30.85467 12.52415  1.000 44.49060  ? 242 LEU   A N   1 
ATOM   1879 C CA  . LEU   A 1 242 ? -7.86981  -29.94421 13.49143  1.000 41.58638  ? 242 LEU   A CA  1 
ATOM   1880 C C   . LEU   A 1 242 ? -6.79895  -29.67187 14.53822  1.000 45.11804  ? 242 LEU   A C   1 
ATOM   1881 O O   . LEU   A 1 242 ? -6.21852  -30.61274 15.09590  1.000 42.69139  ? 242 LEU   A O   1 
ATOM   1882 C CB  . LEU   A 1 242 ? -9.12159  -30.56493 14.11221  1.000 39.81141  ? 242 LEU   A CB  1 
ATOM   1883 C CG  . LEU   A 1 242 ? -9.95499  -29.73014 15.06837  1.000 36.68156  ? 242 LEU   A CG  1 
ATOM   1884 C CD1 . LEU   A 1 242 ? -10.95656 -28.91938 14.26599  1.000 37.31367  ? 242 LEU   A CD1 1 
ATOM   1885 C CD2 . LEU   A 1 242 ? -10.64226 -30.63476 16.09266  1.000 36.94750  ? 242 LEU   A CD2 1 
ATOM   1886 N N   . THR   A 1 243 ? -6.50391  -28.39986 14.76920  1.000 43.19986  ? 243 THR   A N   1 
ATOM   1887 C CA  . THR   A 1 243 ? -5.46507  -28.04190 15.72344  1.000 43.78126  ? 243 THR   A CA  1 
ATOM   1888 C C   . THR   A 1 243 ? -6.07534  -27.80815 17.09997  1.000 44.15759  ? 243 THR   A C   1 
ATOM   1889 O O   . THR   A 1 243 ? -7.29750  -27.80684 17.27439  1.000 46.91584  ? 243 THR   A O   1 
ATOM   1890 C CB  . THR   A 1 243 ? -4.70903  -26.79439 15.25577  1.000 47.39545  ? 243 THR   A CB  1 
ATOM   1891 O OG1 . THR   A 1 243 ? -5.57224  -25.64279 15.30965  1.000 43.68518  ? 243 THR   A OG1 1 
ATOM   1892 C CG2 . THR   A 1 243 ? -4.19226  -26.98862 13.82746  1.000 40.51561  ? 243 THR   A CG2 1 
ATOM   1893 N N   . GLN   A 1 244 ? -5.20546  -27.61046 18.09291  1.000 46.12916  ? 244 GLN   A N   1 
ATOM   1894 C CA  . GLN   A 1 244 ? -5.69194  -27.17407 19.39612  1.000 46.26068  ? 244 GLN   A CA  1 
ATOM   1895 C C   . GLN   A 1 244 ? -6.28247  -25.77427 19.31306  1.000 47.02707  ? 244 GLN   A C   1 
ATOM   1896 O O   . GLN   A 1 244 ? -7.22765  -25.45716 20.04367  1.000 47.95153  ? 244 GLN   A O   1 
ATOM   1897 C CB  . GLN   A 1 244 ? -4.57172  -27.22074 20.43405  1.000 48.63168  ? 244 GLN   A CB  1 
ATOM   1898 C CG  . GLN   A 1 244 ? -5.04791  -26.96099 21.85648  1.000 53.87460  ? 244 GLN   A CG  1 
ATOM   1899 C CD  . GLN   A 1 244 ? -5.83248  -28.13349 22.44313  1.000 59.48352  ? 244 GLN   A CD  1 
ATOM   1900 O OE1 . GLN   A 1 244 ? -5.29825  -29.23625 22.59958  1.000 58.71779  ? 244 GLN   A OE1 1 
ATOM   1901 N NE2 . GLN   A 1 244 ? -7.10204  -27.89352 22.78074  1.000 53.77385  ? 244 GLN   A NE2 1 
ATOM   1902 N N   . ASP   A 1 245 ? -5.75391  -24.93549 18.41826  1.000 45.59917  ? 245 ASP   A N   1 
ATOM   1903 C CA  . ASP   A 1 245 ? -6.29326  -23.59351 18.24454  1.000 45.25246  ? 245 ASP   A CA  1 
ATOM   1904 C C   . ASP   A 1 245 ? -7.70813  -23.63725 17.67364  1.000 46.69010  ? 245 ASP   A C   1 
ATOM   1905 O O   . ASP   A 1 245 ? -8.55372  -22.79314 18.00691  1.000 41.52439  ? 245 ASP   A O   1 
ATOM   1906 C CB  . ASP   A 1 245 ? -5.37143  -22.79661 17.33244  1.000 43.23766  ? 245 ASP   A CB  1 
ATOM   1907 C CG  . ASP   A 1 245 ? -5.75117  -21.34471 17.26029  1.000 44.25269  ? 245 ASP   A CG  1 
ATOM   1908 O OD1 . ASP   A 1 245 ? -6.04217  -20.86650 16.14330  1.000 45.01034  ? 245 ASP   A OD1 1 
ATOM   1909 O OD2 . ASP   A 1 245 ? -5.76122  -20.68574 18.32289  1.000 47.41297  ? 245 ASP   A OD2 1 
ATOM   1910 N N   . HIS   A 1 246 ? -7.96440  -24.59937 16.78361  1.000 44.75322  ? 246 HIS   A N   1 
ATOM   1911 C CA  . HIS   A 1 246 ? -9.31912  -24.87695 16.32288  1.000 41.68888  ? 246 HIS   A CA  1 
ATOM   1912 C C   . HIS   A 1 246 ? -10.23063 -25.25050 17.48747  1.000 39.83956  ? 246 HIS   A C   1 
ATOM   1913 O O   . HIS   A 1 246 ? -11.32064 -24.68824 17.64412  1.000 35.84835  ? 246 HIS   A O   1 
ATOM   1914 C CB  . HIS   A 1 246 ? -9.28773  -26.00800 15.29615  1.000 38.96487  ? 246 HIS   A CB  1 
ATOM   1915 C CG  . HIS   A 1 246 ? -8.70716  -25.61904 13.97436  1.000 35.48615  ? 246 HIS   A CG  1 
ATOM   1916 N ND1 . HIS   A 1 246 ? -8.15732  -26.53823 13.10691  1.000 41.06829  ? 246 HIS   A ND1 1 
ATOM   1917 C CD2 . HIS   A 1 246 ? -8.60821  -24.41701 13.35925  1.000 34.50190  ? 246 HIS   A CD2 1 
ATOM   1918 C CE1 . HIS   A 1 246 ? -7.74555  -25.92034 12.01256  1.000 39.55635  ? 246 HIS   A CE1 1 
ATOM   1919 N NE2 . HIS   A 1 246 ? -8.00923  -24.63262 12.14034  1.000 35.39171  ? 246 HIS   A NE2 1 
ATOM   1920 N N   . VAL   A 1 247 ? -9.80065  -26.21809 18.30506  1.000 38.50030  ? 247 VAL   A N   1 
ATOM   1921 C CA  . VAL   A 1 247 ? -10.56788 -26.62189 19.48358  1.000 41.81980  ? 247 VAL   A CA  1 
ATOM   1922 C C   . VAL   A 1 247 ? -10.95377 -25.40506 20.32760  1.000 43.97300  ? 247 VAL   A C   1 
ATOM   1923 O O   . VAL   A 1 247 ? -12.08743 -25.30671 20.82239  1.000 43.61657  ? 247 VAL   A O   1 
ATOM   1924 C CB  . VAL   A 1 247 ? -9.76893  -27.65737 20.30621  1.000 42.81384  ? 247 VAL   A CB  1 
ATOM   1925 C CG1 . VAL   A 1 247 ? -10.44395 -27.92752 21.65777  1.000 36.98704  ? 247 VAL   A CG1 1 
ATOM   1926 C CG2 . VAL   A 1 247 ? -9.58508  -28.95173 19.51373  1.000 37.91691  ? 247 VAL   A CG2 1 
ATOM   1927 N N   . ASP   A 1 248 ? -10.02423 -24.45032 20.49061  1.000 40.28900  ? 248 ASP   A N   1 
ATOM   1928 C CA  . ASP   A 1 248 ? -10.28381 -23.28260 21.33681  1.000 40.20282  ? 248 ASP   A CA  1 
ATOM   1929 C C   . ASP   A 1 248 ? -11.29611 -22.33497 20.70421  1.000 42.09981  ? 248 ASP   A C   1 
ATOM   1930 O O   . ASP   A 1 248 ? -12.18587 -21.82483 21.39753  1.000 38.64249  ? 248 ASP   A O   1 
ATOM   1931 C CB  . ASP   A 1 248 ? -8.98677  -22.53796 21.62136  1.000 40.72014  ? 248 ASP   A CB  1 
ATOM   1932 C CG  . ASP   A 1 248 ? -7.91022  -23.44092 22.16918  1.000 48.58337  ? 248 ASP   A CG  1 
ATOM   1933 O OD1 . ASP   A 1 248 ? -8.20980  -24.28938 23.05022  1.000 49.11848  ? 248 ASP   A OD1 1 
ATOM   1934 O OD2 . ASP   A 1 248 ? -6.75875  -23.29898 21.70422  1.000 50.51025  ? 248 ASP   A OD2 1 
ATOM   1935 N N   . ILE   A 1 249 ? -11.15620 -22.05765 19.40062  1.000 41.25997  ? 249 ILE   A N   1 
ATOM   1936 C CA  . ILE   A 1 249 ? -12.15891 -21.26017 18.69285  1.000 40.16037  ? 249 ILE   A CA  1 
ATOM   1937 C C   . ILE   A 1 249 ? -13.54446 -21.86281 18.87727  1.000 37.44300  ? 249 ILE   A C   1 
ATOM   1938 O O   . ILE   A 1 249 ? -14.51549 -21.14929 19.15792  1.000 38.66369  ? 249 ILE   A O   1 
ATOM   1939 C CB  . ILE   A 1 249 ? -11.79350 -21.12702 17.20055  1.000 39.19767  ? 249 ILE   A CB  1 
ATOM   1940 C CG1 . ILE   A 1 249 ? -10.40646 -20.50224 17.03575  1.000 41.95713  ? 249 ILE   A CG1 1 
ATOM   1941 C CG2 . ILE   A 1 249 ? -12.83830 -20.32489 16.46589  1.000 42.06350  ? 249 ILE   A CG2 1 
ATOM   1942 C CD1 . ILE   A 1 249 ? -9.90765  -20.49417 15.60546  1.000 41.45411  ? 249 ILE   A CD1 1 
ATOM   1943 N N   . LEU   A 1 250 ? -13.65319 -23.19080 18.75951  1.000 39.24146  ? 250 LEU   A N   1 
ATOM   1944 C CA  . LEU   A 1 250 ? -14.91734 -23.89947 18.96051  1.000 37.69729  ? 250 LEU   A CA  1 
ATOM   1945 C C   . LEU   A 1 250 ? -15.35451 -23.96444 20.45737  1.000 37.64921  ? 250 LEU   A C   1 
ATOM   1946 O O   . LEU   A 1 250 ? -16.31784 -24.68591 20.77399  1.000 37.29216  ? 250 LEU   A O   1 
ATOM   1947 C CB  . LEU   A 1 250 ? -14.82152 -25.30981 18.37130  1.000 35.86165  ? 250 LEU   A CB  1 
ATOM   1948 C CG  . LEU   A 1 250 ? -14.82328 -25.46821 16.83744  1.000 35.28403  ? 250 LEU   A CG  1 
ATOM   1949 C CD1 . LEU   A 1 250 ? -14.43809 -26.90195 16.43022  1.000 33.07897  ? 250 LEU   A CD1 1 
ATOM   1950 C CD2 . LEU   A 1 250 ? -16.14930 -25.06561 16.20630  1.000 22.98767  ? 250 LEU   A CD2 1 
ATOM   1951 N N   . GLY   A 1 251 ? -14.68201 -23.23297 21.34623  1.000 34.77217  ? 251 GLY   A N   1 
ATOM   1952 C CA  . GLY   A 1 251 ? -15.02383 -23.18937 22.74906  1.000 34.36195  ? 251 GLY   A CA  1 
ATOM   1953 C C   . GLY   A 1 251 ? -16.40610 -22.63868 23.06654  1.000 35.64559  ? 251 GLY   A C   1 
ATOM   1954 O O   . GLY   A 1 251 ? -17.23025 -23.32204 23.67862  1.000 36.05157  ? 251 GLY   A O   1 
ATOM   1955 N N   . PRO   A 1 252 ? -16.67452 -21.37860 22.69881  1.000 34.11466  ? 252 PRO   A N   1 
ATOM   1956 C CA  . PRO   A 1 252 ? -18.01272 -20.81276 22.95535  1.000 34.81211  ? 252 PRO   A CA  1 
ATOM   1957 C C   . PRO   A 1 252 ? -19.15784 -21.71837 22.52362  1.000 33.96806  ? 252 PRO   A C   1 
ATOM   1958 O O   . PRO   A 1 252 ? -20.13966 -21.87405 23.26717  1.000 33.62288  ? 252 PRO   A O   1 
ATOM   1959 C CB  . PRO   A 1 252 ? -17.99111 -19.50477 22.15099  1.000 31.32188  ? 252 PRO   A CB  1 
ATOM   1960 C CG  . PRO   A 1 252 ? -16.57497 -19.09972 22.12787  1.000 32.99189  ? 252 PRO   A CG  1 
ATOM   1961 C CD  . PRO   A 1 252 ? -15.73777 -20.36620 22.17139  1.000 35.89002  ? 252 PRO   A CD  1 
ATOM   1962 N N   . LEU   A 1 253 ? -19.03680 -22.33210 21.34128  1.000 33.72930  ? 253 LEU   A N   1 
ATOM   1963 C CA  . LEU   A 1 253 ? -20.05357 -23.25027 20.83678  1.000 32.55051  ? 253 LEU   A CA  1 
ATOM   1964 C C   . LEU   A 1 253 ? -20.12487 -24.51233 21.68647  1.000 33.34656  ? 253 LEU   A C   1 
ATOM   1965 O O   . LEU   A 1 253 ? -21.21655 -24.97935 22.03789  1.000 34.47704  ? 253 LEU   A O   1 
ATOM   1966 C CB  . LEU   A 1 253 ? -19.75518 -23.61182 19.38389  1.000 26.92493  ? 253 LEU   A CB  1 
ATOM   1967 C CG  . LEU   A 1 253 ? -20.15103 -22.61740 18.31411  1.000 27.80983  ? 253 LEU   A CG  1 
ATOM   1968 C CD1 . LEU   A 1 253 ? -19.44768 -22.96578 16.98735  1.000 24.17975  ? 253 LEU   A CD1 1 
ATOM   1969 C CD2 . LEU   A 1 253 ? -21.67492 -22.60475 18.15806  1.000 26.32649  ? 253 LEU   A CD2 1 
ATOM   1970 N N   . SER   A 1 254 ? -18.96971 -25.09815 21.99844  1.000 33.57905  ? 254 SER   A N   1 
ATOM   1971 C CA  . SER   A 1 254 ? -18.94190 -26.20964 22.93912  1.000 34.96134  ? 254 SER   A CA  1 
ATOM   1972 C C   . SER   A 1 254 ? -19.72853 -25.86362 24.19817  1.000 36.14205  ? 254 SER   A C   1 
ATOM   1973 O O   . SER   A 1 254 ? -20.60528 -26.62188 24.62921  1.000 37.01152  ? 254 SER   A O   1 
ATOM   1974 C CB  . SER   A 1 254 ? -17.49556 -26.55759 23.28470  1.000 33.92789  ? 254 SER   A CB  1 
ATOM   1975 O OG  . SER   A 1 254 ? -17.41888 -27.73776 24.06530  1.000 35.27427  ? 254 SER   A OG  1 
ATOM   1976 N N   . ALA   A 1 255 ? -19.45740 -24.68812 24.77196  1.000 34.03867  ? 255 ALA   A N   1 
ATOM   1977 C CA  . ALA   A 1 255 ? -20.03332 -24.33394 26.06180  1.000 37.80825  ? 255 ALA   A CA  1 
ATOM   1978 C C   . ALA   A 1 255 ? -21.50386 -23.94857 25.94930  1.000 41.83929  ? 255 ALA   A C   1 
ATOM   1979 O O   . ALA   A 1 255 ? -22.26863 -24.17552 26.89560  1.000 42.63462  ? 255 ALA   A O   1 
ATOM   1980 C CB  . ALA   A 1 255 ? -19.23031 -23.20143 26.70493  1.000 37.78951  ? 255 ALA   A CB  1 
ATOM   1981 N N   . GLN   A 1 256 ? -21.92418 -23.38363 24.81326  1.000 36.93902  ? 256 GLN   A N   1 
ATOM   1982 C CA  . GLN   A 1 256 ? -23.33936 -23.06706 24.64912  1.000 35.22801  ? 256 GLN   A CA  1 
ATOM   1983 C C   . GLN   A 1 256 ? -24.18267 -24.32882 24.53296  1.000 36.13805  ? 256 GLN   A C   1 
ATOM   1984 O O   . GLN   A 1 256 ? -25.36974 -24.31582 24.87140  1.000 39.33512  ? 256 GLN   A O   1 
ATOM   1985 C CB  . GLN   A 1 256 ? -23.55901 -22.18126 23.41873  1.000 30.88529  ? 256 GLN   A CB  1 
ATOM   1986 C CG  . GLN   A 1 256 ? -24.93667 -21.55558 23.39851  1.000 30.39306  ? 256 GLN   A CG  1 
ATOM   1987 C CD  . GLN   A 1 256 ? -25.45041 -21.20246 21.99699  1.000 31.27466  ? 256 GLN   A CD  1 
ATOM   1988 O OE1 . GLN   A 1 256 ? -24.68113 -20.85223 21.08955  1.000 27.84612  ? 256 GLN   A OE1 1 
ATOM   1989 N NE2 . GLN   A 1 256 ? -26.77207 -21.28887 21.82543  1.000 28.83860  ? 256 GLN   A NE2 1 
ATOM   1990 N N   . THR   A 1 257 ? -23.60001 -25.42422 24.06005  1.000 37.44810  ? 257 THR   A N   1 
ATOM   1991 C CA  . THR   A 1 257 ? -24.36221 -26.63925 23.83948  1.000 39.10596  ? 257 THR   A CA  1 
ATOM   1992 C C   . THR   A 1 257 ? -24.05026 -27.73563 24.84481  1.000 33.62991  ? 257 THR   A C   1 
ATOM   1993 O O   . THR   A 1 257 ? -24.76753 -28.73713 24.87698  1.000 34.36468  ? 257 THR   A O   1 
ATOM   1994 C CB  . THR   A 1 257 ? -24.12399 -27.17190 22.41310  1.000 36.65483  ? 257 THR   A CB  1 
ATOM   1995 O OG1 . THR   A 1 257 ? -22.71825 -27.34048 22.18249  1.000 30.04705  ? 257 THR   A OG1 1 
ATOM   1996 C CG2 . THR   A 1 257 ? -24.71339 -26.22089 21.36632  1.000 28.82509  ? 257 THR   A CG2 1 
ATOM   1997 N N   . GLY   A 1 258 ? -23.01693 -27.56995 25.66727  1.000 35.85150  ? 258 GLY   A N   1 
ATOM   1998 C CA  . GLY   A 1 258 ? -22.61363 -28.60160 26.60492  1.000 36.32830  ? 258 GLY   A CA  1 
ATOM   1999 C C   . GLY   A 1 258 ? -22.06608 -29.85826 25.97122  1.000 36.34938  ? 258 GLY   A C   1 
ATOM   2000 O O   . GLY   A 1 258 ? -21.97427 -30.88564 26.65041  1.000 41.45362  ? 258 GLY   A O   1 
ATOM   2001 N N   . ILE   A 1 259 ? -21.72378 -29.81093 24.68530  1.000 39.08372  ? 259 ILE   A N   1 
ATOM   2002 C CA  . ILE   A 1 259 ? -21.07399 -30.90657 23.97624  1.000 38.34370  ? 259 ILE   A CA  1 
ATOM   2003 C C   . ILE   A 1 259 ? -19.58786 -30.55386 23.89156  1.000 40.72620  ? 259 ILE   A C   1 
ATOM   2004 O O   . ILE   A 1 259 ? -19.19868 -29.59690 23.20814  1.000 36.48712  ? 259 ILE   A O   1 
ATOM   2005 C CB  . ILE   A 1 259 ? -21.69087 -31.12664 22.58348  1.000 37.22994  ? 259 ILE   A CB  1 
ATOM   2006 C CG1 . ILE   A 1 259 ? -23.19251 -31.35876 22.68673  1.000 36.20222  ? 259 ILE   A CG1 1 
ATOM   2007 C CG2 . ILE   A 1 259 ? -21.06988 -32.34025 21.88087  1.000 33.33997  ? 259 ILE   A CG2 1 
ATOM   2008 C CD1 . ILE   A 1 259 ? -23.50877 -32.64998 23.34827  1.000 35.22907  ? 259 ILE   A CD1 1 
ATOM   2009 N N   . ALA   A 1 260 ? -18.75521 -31.31373 24.60282  1.000 42.15182  ? 260 ALA   A N   1 
ATOM   2010 C CA  . ALA   A 1 260 ? -17.31846 -31.07418 24.57753  1.000 41.78320  ? 260 ALA   A CA  1 
ATOM   2011 C C   . ALA   A 1 260 ? -16.80065 -31.14104 23.14141  1.000 41.38919  ? 260 ALA   A C   1 
ATOM   2012 O O   . ALA   A 1 260 ? -17.34107 -31.86911 22.29997  1.000 40.91874  ? 260 ALA   A O   1 
ATOM   2013 C CB  . ALA   A 1 260 ? -16.59934 -32.09033 25.46587  1.000 42.42568  ? 260 ALA   A CB  1 
ATOM   2014 N N   . VAL   A 1 261 ? -15.76669 -30.33950 22.85064  1.000 35.31008  ? 261 VAL   A N   1 
ATOM   2015 C CA  . VAL   A 1 261 ? -15.28160 -30.25078 21.47626  1.000 34.95260  ? 261 VAL   A CA  1 
ATOM   2016 C C   . VAL   A 1 261 ? -14.85083 -31.62101 20.97664  1.000 37.06660  ? 261 VAL   A C   1 
ATOM   2017 O O   . VAL   A 1 261 ? -15.18279 -32.02470 19.85239  1.000 31.60541  ? 261 VAL   A O   1 
ATOM   2018 C CB  . VAL   A 1 261 ? -14.14259 -29.22233 21.36187  1.000 37.64026  ? 261 VAL   A CB  1 
ATOM   2019 C CG1 . VAL   A 1 261 ? -13.40429 -29.39594 20.02935  1.000 30.08563  ? 261 VAL   A CG1 1 
ATOM   2020 C CG2 . VAL   A 1 261 ? -14.70013 -27.82169 21.44544  1.000 33.82055  ? 261 VAL   A CG2 1 
ATOM   2021 N N   . LEU   A 1 262 ? -14.12056 -32.36792 21.80866  1.000 36.38647  ? 262 LEU   A N   1 
ATOM   2022 C CA  . LEU   A 1 262 ? -13.67985 -33.69620 21.39949  1.000 38.98197  ? 262 LEU   A CA  1 
ATOM   2023 C C   . LEU   A 1 262 ? -14.84076 -34.68712 21.34036  1.000 39.18116  ? 262 LEU   A C   1 
ATOM   2024 O O   . LEU   A 1 262 ? -14.65657 -35.80735 20.84842  1.000 40.67313  ? 262 LEU   A O   1 
ATOM   2025 C CB  . LEU   A 1 262 ? -12.60869 -34.25679 22.34407  1.000 43.59411  ? 262 LEU   A CB  1 
ATOM   2026 C CG  . LEU   A 1 262 ? -11.20911 -33.61504 22.28301  1.000 47.52016  ? 262 LEU   A CG  1 
ATOM   2027 C CD1 . LEU   A 1 262 ? -10.63588 -33.55628 20.85981  1.000 39.86057  ? 262 LEU   A CD1 1 
ATOM   2028 C CD2 . LEU   A 1 262 ? -11.12212 -32.28140 23.04080  1.000 46.68621  ? 262 LEU   A CD2 1 
ATOM   2029 N N   . ASP   A 1 263 ? -16.02077 -34.30846 21.84265  1.000 38.84430  ? 263 ASP   A N   1 
ATOM   2030 C CA  . ASP   A 1 263 ? -17.20570 -35.14291 21.68458  1.000 41.34747  ? 263 ASP   A CA  1 
ATOM   2031 C C   . ASP   A 1 263 ? -17.81935 -34.95455 20.30834  1.000 38.37264  ? 263 ASP   A C   1 
ATOM   2032 O O   . ASP   A 1 263 ? -18.15130 -35.93290 19.63194  1.000 37.74258  ? 263 ASP   A O   1 
ATOM   2033 C CB  . ASP   A 1 263 ? -18.23197 -34.82328 22.76770  1.000 42.18897  ? 263 ASP   A CB  1 
ATOM   2034 C CG  . ASP   A 1 263 ? -17.82125 -35.34865 24.13125  1.000 43.08699  ? 263 ASP   A CG  1 
ATOM   2035 O OD1 . ASP   A 1 263 ? -16.81681 -36.08847 24.20570  1.000 40.05305  ? 263 ASP   A OD1 1 
ATOM   2036 O OD2 . ASP   A 1 263 ? -18.51078 -35.01164 25.12018  1.000 45.24883  ? 263 ASP   A OD2 1 
ATOM   2037 N N   . MET   A 1 264 ? -17.98316 -33.69824 19.87922  1.000 39.04330  ? 264 MET   A N   1 
ATOM   2038 C CA  . MET   A 1 264 ? -18.44843 -33.44238 18.51797  1.000 32.87720  ? 264 MET   A CA  1 
ATOM   2039 C C   . MET   A 1 264 ? -17.47973 -34.00545 17.48406  1.000 35.24424  ? 264 MET   A C   1 
ATOM   2040 O O   . MET   A 1 264 ? -17.89709 -34.39292 16.38552  1.000 30.31342  ? 264 MET   A O   1 
ATOM   2041 C CB  . MET   A 1 264 ? -18.66059 -31.95041 18.31808  1.000 31.93433  ? 264 MET   A CB  1 
ATOM   2042 C CG  . MET   A 1 264 ? -19.42251 -31.62448 17.07349  1.000 33.38907  ? 264 MET   A CG  1 
ATOM   2043 S SD  . MET   A 1 264 ? -21.12637 -32.15692 17.25949  1.000 30.72365  ? 264 MET   A SD  1 
ATOM   2044 C CE  . MET   A 1 264 ? -21.83145 -30.74178 18.09837  1.000 32.25119  ? 264 MET   A CE  1 
ATOM   2045 N N   . CYS   A 1 265 ? -16.19100 -34.10338 17.83553  1.000 38.25445  ? 265 CYS   A N   1 
ATOM   2046 C CA  . CYS   A 1 265 ? -15.23297 -34.80021 16.97989  1.000 38.72770  ? 265 CYS   A CA  1 
ATOM   2047 C C   . CYS   A 1 265 ? -15.57536 -36.28158 16.84212  1.000 36.02704  ? 265 CYS   A C   1 
ATOM   2048 O O   . CYS   A 1 265 ? -15.48961 -36.84691 15.74351  1.000 35.94978  ? 265 CYS   A O   1 
ATOM   2049 C CB  . CYS   A 1 265 ? -13.81895 -34.62777 17.53040  1.000 38.30407  ? 265 CYS   A CB  1 
ATOM   2050 S SG  . CYS   A 1 265 ? -13.14113 -32.97336 17.31548  1.000 30.73012  ? 265 CYS   A SG  1 
ATOM   2051 N N   . ALA   A 1 266 ? -15.95883 -36.93395 17.94467  1.000 36.47840  ? 266 ALA   A N   1 
ATOM   2052 C CA  . ALA   A 1 266 ? -16.41396 -38.32185 17.84519  1.000 36.40415  ? 266 ALA   A CA  1 
ATOM   2053 C C   . ALA   A 1 266 ? -17.68854 -38.44558 17.00866  1.000 38.09043  ? 266 ALA   A C   1 
ATOM   2054 O O   . ALA   A 1 266 ? -17.88449 -39.47055 16.34251  1.000 39.61814  ? 266 ALA   A O   1 
ATOM   2055 C CB  . ALA   A 1 266 ? -16.63750 -38.92010 19.23189  1.000 38.19017  ? 266 ALA   A CB  1 
ATOM   2056 N N   . SER   A 1 267 ? -18.56706 -37.42547 17.02537  1.000 34.91199  ? 267 SER   A N   1 
ATOM   2057 C CA  . SER   A 1 267 ? -19.76581 -37.47728 16.18725  1.000 33.44508  ? 267 SER   A CA  1 
ATOM   2058 C C   . SER   A 1 267 ? -19.39568 -37.42641 14.71993  1.000 37.02778  ? 267 SER   A C   1 
ATOM   2059 O O   . SER   A 1 267 ? -19.90422 -38.21176 13.91009  1.000 35.83816  ? 267 SER   A O   1 
ATOM   2060 C CB  . SER   A 1 267 ? -20.72690 -36.33120 16.50385  1.000 32.29496  ? 267 SER   A CB  1 
ATOM   2061 O OG  . SER   A 1 267 ? -21.16549 -36.36098 17.84105  1.000 46.76899  ? 267 SER   A OG  1 
ATOM   2062 N N   . LEU   A 1 268 ? -18.52452 -36.48127 14.35620  1.000 34.98931  ? 268 LEU   A N   1 
ATOM   2063 C CA  . LEU   A 1 268 ? -18.08577 -36.37220 12.97469  1.000 34.35769  ? 268 LEU   A CA  1 
ATOM   2064 C C   . LEU   A 1 268 ? -17.36727 -37.64418 12.53673  1.000 36.85484  ? 268 LEU   A C   1 
ATOM   2065 O O   . LEU   A 1 268 ? -17.64066 -38.18169 11.45785  1.000 38.97335  ? 268 LEU   A O   1 
ATOM   2066 C CB  . LEU   A 1 268 ? -17.19252 -35.13661 12.80735  1.000 32.61597  ? 268 LEU   A CB  1 
ATOM   2067 C CG  . LEU   A 1 268 ? -16.64864 -34.85359 11.41303  1.000 34.64319  ? 268 LEU   A CG  1 
ATOM   2068 C CD1 . LEU   A 1 268 ? -17.77885 -35.00076 10.39811  1.000 30.71143  ? 268 LEU   A CD1 1 
ATOM   2069 C CD2 . LEU   A 1 268 ? -16.02120 -33.45661 11.34234  1.000 34.28647  ? 268 LEU   A CD2 1 
ATOM   2070 N N   . LYS   A 1 269 ? -16.44934 -38.15148 13.36376  1.000 35.72800  ? 269 LYS   A N   1 
ATOM   2071 C CA  . LYS   A 1 269 ? -15.78261 -39.40896 13.02002  1.000 39.15959  ? 269 LYS   A CA  1 
ATOM   2072 C C   . LYS   A 1 269 ? -16.79652 -40.47459 12.58226  1.000 41.20190  ? 269 LYS   A C   1 
ATOM   2073 O O   . LYS   A 1 269 ? -16.68369 -41.05914 11.49383  1.000 41.19851  ? 269 LYS   A O   1 
ATOM   2074 C CB  . LYS   A 1 269 ? -14.94734 -39.91919 14.20073  1.000 36.13455  ? 269 LYS   A CB  1 
ATOM   2075 C CG  . LYS   A 1 269 ? -14.25885 -41.24741 13.88095  1.000 41.22404  ? 269 LYS   A CG  1 
ATOM   2076 C CD  . LYS   A 1 269 ? -13.64473 -41.96579 15.09252  1.000 48.33502  ? 269 LYS   A CD  1 
ATOM   2077 C CE  . LYS   A 1 269 ? -12.36626 -41.36495 15.62703  1.000 48.06765  ? 269 LYS   A CE  1 
ATOM   2078 N NZ  . LYS   A 1 269 ? -11.81208 -42.29279 16.63771  1.000 53.57415  ? 269 LYS   A NZ  1 
ATOM   2079 N N   . GLU   A 1 270 ? -17.82760 -40.69875 13.40567  1.000 38.55087  ? 270 GLU   A N   1 
ATOM   2080 C CA  . GLU   A 1 270 ? -18.86425 -41.67738 13.07073  1.000 44.17210  ? 270 GLU   A CA  1 
ATOM   2081 C C   . GLU   A 1 270 ? -19.62530 -41.28042 11.79879  1.000 44.21899  ? 270 GLU   A C   1 
ATOM   2082 O O   . GLU   A 1 270 ? -19.96852 -42.14534 10.97891  1.000 46.38207  ? 270 GLU   A O   1 
ATOM   2083 C CB  . GLU   A 1 270 ? -19.81925 -41.84521 14.26098  1.000 38.00465  ? 270 GLU   A CB  1 
ATOM   2084 C CG  . GLU   A 1 270 ? -20.79317 -43.01169 14.16166  1.000 48.69875  ? 270 GLU   A CG  1 
ATOM   2085 C CD  . GLU   A 1 270 ? -21.73888 -43.11738 15.36948  1.000 53.73703  ? 270 GLU   A CD  1 
ATOM   2086 O OE1 . GLU   A 1 270 ? -21.65359 -44.13733 16.08923  1.000 52.95900  ? 270 GLU   A OE1 1 
ATOM   2087 O OE2 . GLU   A 1 270 ? -22.57251 -42.20508 15.59465  1.000 49.93838  ? 270 GLU   A OE2 1 
ATOM   2088 N N   . LEU   A 1 271 ? -19.86820 -39.97322 11.60087  1.000 39.95995  ? 271 LEU   A N   1 
ATOM   2089 C CA  . LEU   A 1 271 ? -20.56295 -39.51154 10.39957  1.000 43.20407  ? 271 LEU   A CA  1 
ATOM   2090 C C   . LEU   A 1 271 ? -19.74195 -39.77270 9.14019   1.000 45.76039  ? 271 LEU   A C   1 
ATOM   2091 O O   . LEU   A 1 271 ? -20.28628 -40.18960 8.10996   1.000 45.13833  ? 271 LEU   A O   1 
ATOM   2092 C CB  . LEU   A 1 271 ? -20.88552 -38.02364 10.51882  1.000 40.99785  ? 271 LEU   A CB  1 
ATOM   2093 C CG  . LEU   A 1 271 ? -22.09561 -37.58542 11.33540  1.000 36.16659  ? 271 LEU   A CG  1 
ATOM   2094 C CD1 . LEU   A 1 271 ? -22.10129 -36.08207 11.43551  1.000 28.99071  ? 271 LEU   A CD1 1 
ATOM   2095 C CD2 . LEU   A 1 271 ? -23.36589 -38.08198 10.68416  1.000 41.12840  ? 271 LEU   A CD2 1 
ATOM   2096 N N   . LEU   A 1 272 ? -18.43159 -39.51363 9.19654   1.000 38.85712  ? 272 LEU   A N   1 
ATOM   2097 C CA  . LEU   A 1 272 ? -17.57080 -39.84511 8.06506   1.000 44.87861  ? 272 LEU   A CA  1 
ATOM   2098 C C   . LEU   A 1 272 ? -17.48664 -41.35055 7.85559   1.000 44.15724  ? 272 LEU   A C   1 
ATOM   2099 O O   . LEU   A 1 272 ? -17.38249 -41.81098 6.71292   1.000 45.76051  ? 272 LEU   A O   1 
ATOM   2100 C CB  . LEU   A 1 272 ? -16.16768 -39.25936 8.26726   1.000 45.86128  ? 272 LEU   A CB  1 
ATOM   2101 C CG  . LEU   A 1 272 ? -16.12010 -37.72827 8.32661   1.000 41.70206  ? 272 LEU   A CG  1 
ATOM   2102 C CD1 . LEU   A 1 272 ? -14.75882 -37.24691 8.77356   1.000 38.43599  ? 272 LEU   A CD1 1 
ATOM   2103 C CD2 . LEU   A 1 272 ? -16.49788 -37.12919 6.98497   1.000 38.37249  ? 272 LEU   A CD2 1 
ATOM   2104 N N   . GLN   A 1 273 ? -17.54756 -42.12924 8.93744   1.000 45.77036  ? 273 GLN   A N   1 
ATOM   2105 C CA  . GLN   A 1 273 ? -17.40090 -43.57336 8.81723   1.000 46.44805  ? 273 GLN   A CA  1 
ATOM   2106 C C   . GLN   A 1 273 ? -18.68065 -44.21818 8.31022   1.000 50.08294  ? 273 GLN   A C   1 
ATOM   2107 O O   . GLN   A 1 273 ? -18.64966 -45.02657 7.37641   1.000 52.47398  ? 273 GLN   A O   1 
ATOM   2108 C CB  . GLN   A 1 273 ? -16.98445 -44.16952 10.16012  1.000 44.87271  ? 273 GLN   A CB  1 
ATOM   2109 C CG  . GLN   A 1 273 ? -15.47794 -44.11351 10.38517  1.000 49.31714  ? 273 GLN   A CG  1 
ATOM   2110 C CD  . GLN   A 1 273 ? -15.08585 -44.30803 11.83029  1.000 47.99639  ? 273 GLN   A CD  1 
ATOM   2111 O OE1 . GLN   A 1 273 ? -15.91486 -44.65973 12.66643  1.000 53.06202  ? 273 GLN   A OE1 1 
ATOM   2112 N NE2 . GLN   A 1 273 ? -13.81586 -44.07034 12.13681  1.000 48.71314  ? 273 GLN   A NE2 1 
ATOM   2113 N N   . ASN   A 1 274 ? -19.81792 -43.85470 8.89443   1.000 52.02387  ? 274 ASN   A N   1 
ATOM   2114 C CA  . ASN   A 1 274 ? -21.07992 -44.51812 8.60589   1.000 50.45313  ? 274 ASN   A CA  1 
ATOM   2115 C C   . ASN   A 1 274 ? -21.96893 -43.74064 7.63982   1.000 51.02965  ? 274 ASN   A C   1 
ATOM   2116 O O   . ASN   A 1 274 ? -23.03398 -44.23349 7.26371   1.000 49.42364  ? 274 ASN   A O   1 
ATOM   2117 C CB  . ASN   A 1 274 ? -21.82570 -44.79133 9.91697   1.000 52.53110  ? 274 ASN   A CB  1 
ATOM   2118 C CG  . ASN   A 1 274 ? -20.95296 -45.51802 10.95095  1.000 60.34896  ? 274 ASN   A CG  1 
ATOM   2119 O OD1 . ASN   A 1 274 ? -21.17046 -45.40586 12.16084  1.000 58.20992  ? 274 ASN   A OD1 1 
ATOM   2120 N ND2 . ASN   A 1 274 ? -19.96048 -46.26548 10.47054  1.000 59.38354  ? 274 ASN   A ND2 1 
ATOM   2121 N N   . GLY   A 1 275 ? -21.55926 -42.56033 7.20968   1.000 51.69886  ? 275 GLY   A N   1 
ATOM   2122 C CA  . GLY   A 1 275 ? -22.44805 -41.78116 6.37284   1.000 55.86588  ? 275 GLY   A CA  1 
ATOM   2123 C C   . GLY   A 1 275 ? -23.59732 -41.18457 7.17628   1.000 56.65759  ? 275 GLY   A C   1 
ATOM   2124 O O   . GLY   A 1 275 ? -23.64310 -41.23828 8.40416   1.000 56.31566  ? 275 GLY   A O   1 
ATOM   2125 N N   . MET   A 1 276 ? -24.54369 -40.60128 6.44816   1.000 63.75793  ? 276 MET   A N   1 
ATOM   2126 C CA  . MET   A 1 276 ? -25.70429 -39.98188 7.07292   1.000 64.43276  ? 276 MET   A CA  1 
ATOM   2127 C C   . MET   A 1 276 ? -26.93414 -40.87276 7.02013   1.000 68.29300  ? 276 MET   A C   1 
ATOM   2128 O O   . MET   A 1 276 ? -27.96960 -40.51268 7.59187   1.000 66.87846  ? 276 MET   A O   1 
ATOM   2129 C CB  . MET   A 1 276 ? -25.97942 -38.61104 6.43218   1.000 60.51363  ? 276 MET   A CB  1 
ATOM   2130 C CG  . MET   A 1 276 ? -24.93126 -37.57177 6.86173   1.000 56.19371  ? 276 MET   A CG  1 
ATOM   2131 S SD  . MET   A 1 276 ? -25.00395 -35.89411 6.16095   1.000 56.61751  ? 276 MET   A SD  1 
ATOM   2132 C CE  . MET   A 1 276 ? -26.75805 -35.58746 6.21630   1.000 45.12693  ? 276 MET   A CE  1 
ATOM   2133 N N   . ASN   A 1 277 ? -26.81490 -42.05233 6.40465   1.000 78.27799  ? 277 ASN   A N   1 
ATOM   2134 C CA  . ASN   A 1 277 ? -27.92623 -42.99097 6.23435   1.000 82.07705  ? 277 ASN   A CA  1 
ATOM   2135 C C   . ASN   A 1 277 ? -29.12356 -42.30486 5.59210   1.000 81.80476  ? 277 ASN   A C   1 
ATOM   2136 O O   . ASN   A 1 277 ? -30.27482 -42.50687 5.98845   1.000 83.14968  ? 277 ASN   A O   1 
ATOM   2137 C CB  . ASN   A 1 277 ? -28.32150 -43.64623 7.55669   1.000 88.25939  ? 277 ASN   A CB  1 
ATOM   2138 C CG  . ASN   A 1 277 ? -29.18245 -44.87899 7.35412   1.000 92.64941  ? 277 ASN   A CG  1 
ATOM   2139 O OD1 . ASN   A 1 277 ? -29.05565 -45.57846 6.34853   1.000 97.40499  ? 277 ASN   A OD1 1 
ATOM   2140 N ND2 . ASN   A 1 277 ? -30.07086 -45.14553 8.30520   1.000 95.47569  ? 277 ASN   A ND2 1 
ATOM   2141 N N   . GLY   A 1 278 ? -28.84186 -41.47849 4.58873   1.000 79.63406  ? 278 GLY   A N   1 
ATOM   2142 C CA  . GLY   A 1 278 ? -29.89563 -40.74424 3.91712   1.000 80.08872  ? 278 GLY   A CA  1 
ATOM   2143 C C   . GLY   A 1 278 ? -30.73461 -39.88393 4.83515   1.000 72.59586  ? 278 GLY   A C   1 
ATOM   2144 O O   . GLY   A 1 278 ? -31.93539 -39.71730 4.59064   1.000 73.12743  ? 278 GLY   A O   1 
ATOM   2145 N N   . ARG   A 1 279 ? -30.14758 -39.35677 5.90878   1.000 68.51654  ? 279 ARG   A N   1 
ATOM   2146 C CA  . ARG   A 1 279 ? -30.80882 -38.30408 6.65172   1.000 58.86506  ? 279 ARG   A CA  1 
ATOM   2147 C C   . ARG   A 1 279 ? -30.19362 -36.98871 6.22556   1.000 57.93671  ? 279 ARG   A C   1 
ATOM   2148 O O   . ARG   A 1 279 ? -29.27944 -36.94674 5.40421   1.000 58.46669  ? 279 ARG   A O   1 
ATOM   2149 C CB  . ARG   A 1 279 ? -30.64534 -38.40899 8.15940   1.000 61.08281  ? 279 ARG   A CB  1 
ATOM   2150 C CG  . ARG   A 1 279 ? -31.02561 -39.69825 8.78537   1.000 66.91641  ? 279 ARG   A CG  1 
ATOM   2151 C CD  . ARG   A 1 279 ? -31.19494 -39.38076 10.21167  1.000 64.51286  ? 279 ARG   A CD  1 
ATOM   2152 N NE  . ARG   A 1 279 ? -31.30441 -40.50179 11.11783  1.000 67.11682  ? 279 ARG   A NE  1 
ATOM   2153 C CZ  . ARG   A 1 279 ? -31.58078 -40.30713 12.39477  1.000 66.81939  ? 279 ARG   A CZ  1 
ATOM   2154 N NH1 . ARG   A 1 279 ? -31.92764 -39.08165 12.77884  1.000 64.06657  ? 279 ARG   A NH1 1 
ATOM   2155 N NH2 . ARG   A 1 279 ? -31.63328 -41.32331 13.24647  1.000 69.20320  ? 279 ARG   A NH2 1 
ATOM   2156 N N   . THR   A 1 280 ? -30.64803 -35.90717 6.84446   1.000 49.98678  ? 280 THR   A N   1 
ATOM   2157 C CA  . THR   A 1 280 ? -30.14483 -34.57956 6.53650   1.000 39.67704  ? 280 THR   A CA  1 
ATOM   2158 C C   . THR   A 1 280 ? -29.87234 -33.81378 7.81778   1.000 38.00093  ? 280 THR   A C   1 
ATOM   2159 O O   . THR   A 1 280 ? -30.65466 -33.87955 8.76925   1.000 38.92150  ? 280 THR   A O   1 
ATOM   2160 C CB  . THR   A 1 280 ? -31.12906 -33.79530 5.68014   1.000 40.20676  ? 280 THR   A CB  1 
ATOM   2161 O OG1 . THR   A 1 280 ? -32.36601 -33.65625 6.39203   1.000 41.48250  ? 280 THR   A OG1 1 
ATOM   2162 C CG2 . THR   A 1 280 ? -31.35934 -34.51604 4.33482   1.000 38.71501  ? 280 THR   A CG2 1 
ATOM   2163 N N   . ILE   A 1 281 ? -28.75244 -33.09635 7.83497   1.000 38.17864  ? 281 ILE   A N   1 
ATOM   2164 C CA  . ILE   A 1 281 ? -28.42896 -32.16110 8.90263   1.000 33.53428  ? 281 ILE   A CA  1 
ATOM   2165 C C   . ILE   A 1 281 ? -28.67997 -30.74502 8.40087   1.000 34.41722  ? 281 ILE   A C   1 
ATOM   2166 O O   . ILE   A 1 281 ? -28.08059 -30.30857 7.40805   1.000 32.59153  ? 281 ILE   A O   1 
ATOM   2167 C CB  . ILE   A 1 281 ? -26.97945 -32.32527 9.37270   1.000 33.57196  ? 281 ILE   A CB  1 
ATOM   2168 C CG1 . ILE   A 1 281 ? -26.73774 -33.73985 9.90707   1.000 29.91988  ? 281 ILE   A CG1 1 
ATOM   2169 C CG2 . ILE   A 1 281 ? -26.65194 -31.26238 10.40486  1.000 32.49602  ? 281 ILE   A CG2 1 
ATOM   2170 C CD1 . ILE   A 1 281 ? -25.40679 -33.91165 10.54874  1.000 28.50125  ? 281 ILE   A CD1 1 
ATOM   2171 N N   . LEU   A 1 282 ? -29.56356 -30.02079 9.08614   1.000 34.12321  ? 282 LEU   A N   1 
ATOM   2172 C CA  . LEU   A 1 282 ? -29.87215 -28.63598 8.72259   1.000 28.51064  ? 282 LEU   A CA  1 
ATOM   2173 C C   . LEU   A 1 282 ? -30.34659 -28.53838 7.27175   1.000 30.18016  ? 282 LEU   A C   1 
ATOM   2174 O O   . LEU   A 1 282 ? -29.94219 -27.64451 6.52562   1.000 26.78131  ? 282 LEU   A O   1 
ATOM   2175 C CB  . LEU   A 1 282 ? -28.66911 -27.73125 8.96692   1.000 23.93460  ? 282 LEU   A CB  1 
ATOM   2176 C CG  . LEU   A 1 282 ? -28.53729 -27.33732 10.42303  1.000 25.77346  ? 282 LEU   A CG  1 
ATOM   2177 C CD1 . LEU   A 1 282 ? -27.43098 -26.31933 10.57676  1.000 24.71539  ? 282 LEU   A CD1 1 
ATOM   2178 C CD2 . LEU   A 1 282 ? -29.86453 -26.79803 10.93686  1.000 25.28130  ? 282 LEU   A CD2 1 
ATOM   2179 N N   . GLY   A 1 283 ? -31.21234 -29.47521 6.87896   1.000 28.33280  ? 283 GLY   A N   1 
ATOM   2180 C CA  . GLY   A 1 283 ? -31.67505 -29.59357 5.51344   1.000 30.93653  ? 283 GLY   A CA  1 
ATOM   2181 C C   . GLY   A 1 283 ? -30.60150 -29.91169 4.49496   1.000 32.79769  ? 283 GLY   A C   1 
ATOM   2182 O O   . GLY   A 1 283 ? -30.79484 -29.62505 3.30747   1.000 27.89956  ? 283 GLY   A O   1 
ATOM   2183 N N   . SER   A 1 284 ? -29.46826 -30.48655 4.91058   1.000 31.30215  ? 284 SER   A N   1 
ATOM   2184 C CA  . SER   A 1 284 ? -28.38288 -30.79788 3.97986   1.000 34.46577  ? 284 SER   A CA  1 
ATOM   2185 C C   . SER   A 1 284 ? -28.03579 -32.27885 4.03489   1.000 32.98369  ? 284 SER   A C   1 
ATOM   2186 O O   . SER   A 1 284 ? -27.84200 -32.83482 5.11875   1.000 33.41685  ? 284 SER   A O   1 
ATOM   2187 C CB  . SER   A 1 284 ? -27.12856 -29.96978 4.26875   1.000 27.62341  ? 284 SER   A CB  1 
ATOM   2188 O OG  . SER   A 1 284 ? -26.07279 -30.36308 3.40394   1.000 31.64773  ? 284 SER   A OG  1 
ATOM   2189 N N   . ALA   A 1 285 ? -27.93244 -32.91038 2.86642   1.000 32.78035  ? 285 ALA   A N   1 
ATOM   2190 C CA  . ALA   A 1 285 ? -27.50953 -34.30113 2.78755   1.000 33.41739  ? 285 ALA   A CA  1 
ATOM   2191 C C   . ALA   A 1 285 ? -26.00092 -34.45381 2.65613   1.000 33.28069  ? 285 ALA   A C   1 
ATOM   2192 O O   . ALA   A 1 285 ? -25.52516 -35.52862 2.26859   1.000 33.56902  ? 285 ALA   A O   1 
ATOM   2193 C CB  . ALA   A 1 285 ? -28.20170 -35.00186 1.62466   1.000 35.12762  ? 285 ALA   A CB  1 
ATOM   2194 N N   . LEU   A 1 286 ? -25.23759 -33.40693 2.95945   1.000 31.89271  ? 286 LEU   A N   1 
ATOM   2195 C CA  . LEU   A 1 286 ? -23.78603 -33.48556 2.92637   1.000 31.31349  ? 286 LEU   A CA  1 
ATOM   2196 C C   . LEU   A 1 286 ? -23.22110 -32.75392 4.13368   1.000 32.68479  ? 286 LEU   A C   1 
ATOM   2197 O O   . LEU   A 1 286 ? -23.83360 -31.80736 4.64525   1.000 30.77862  ? 286 LEU   A O   1 
ATOM   2198 C CB  . LEU   A 1 286 ? -23.20608 -32.86652 1.65421   1.000 29.51939  ? 286 LEU   A CB  1 
ATOM   2199 C CG  . LEU   A 1 286 ? -23.53251 -33.44599 0.28713   1.000 29.75269  ? 286 LEU   A CG  1 
ATOM   2200 C CD1 . LEU   A 1 286 ? -22.99275 -32.49346 -0.80308  1.000 26.81965  ? 286 LEU   A CD1 1 
ATOM   2201 C CD2 . LEU   A 1 286 ? -22.98513 -34.86064 0.12193   1.000 26.10435  ? 286 LEU   A CD2 1 
ATOM   2202 N N   . LEU   A 1 287 ? -22.03872 -33.18383 4.57475   1.000 27.75218  ? 287 LEU   A N   1 
ATOM   2203 C CA  . LEU   A 1 287 ? -21.34309 -32.44354 5.61212   1.000 28.68347  ? 287 LEU   A CA  1 
ATOM   2204 C C   . LEU   A 1 287 ? -20.92941 -31.07354 5.06590   1.000 29.99774  ? 287 LEU   A C   1 
ATOM   2205 O O   . LEU   A 1 287 ? -20.11636 -30.96576 4.14492   1.000 28.10258  ? 287 LEU   A O   1 
ATOM   2206 C CB  . LEU   A 1 287 ? -20.15212 -33.24245 6.12911   1.000 28.53350  ? 287 LEU   A CB  1 
ATOM   2207 C CG  . LEU   A 1 287 ? -20.67376 -34.48653 6.85563   1.000 35.52751  ? 287 LEU   A CG  1 
ATOM   2208 C CD1 . LEU   A 1 287 ? -19.56916 -35.42692 7.29769   1.000 26.96768  ? 287 LEU   A CD1 1 
ATOM   2209 C CD2 . LEU   A 1 287 ? -21.57440 -34.09390 8.03973   1.000 34.61239  ? 287 LEU   A CD2 1 
ATOM   2210 N N   . GLU   A 1 288 ? -21.51317 -30.02967 5.62568   1.000 23.01726  ? 288 GLU   A N   1 
ATOM   2211 C CA  . GLU   A 1 288 ? -21.33862 -28.68502 5.12796   1.000 24.38072  ? 288 GLU   A CA  1 
ATOM   2212 C C   . GLU   A 1 288 ? -20.14114 -28.01884 5.80349   1.000 23.25664  ? 288 GLU   A C   1 
ATOM   2213 O O   . GLU   A 1 288 ? -20.04178 -28.00259 7.03617   1.000 24.72291  ? 288 GLU   A O   1 
ATOM   2214 C CB  . GLU   A 1 288 ? -22.63010 -27.89518 5.36764   1.000 26.22785  ? 288 GLU   A CB  1 
ATOM   2215 C CG  . GLU   A 1 288 ? -22.48920 -26.44554 5.04744   1.000 30.81663  ? 288 GLU   A CG  1 
ATOM   2216 C CD  . GLU   A 1 288 ? -22.51579 -26.21886 3.55026   1.000 34.47829  ? 288 GLU   A CD  1 
ATOM   2217 O OE1 . GLU   A 1 288 ? -21.57110 -25.55237 3.03950   1.000 26.44314  ? 288 GLU   A OE1 1 
ATOM   2218 O OE2 . GLU   A 1 288 ? -23.47087 -26.73435 2.90807   1.000 41.73535  ? 288 GLU   A OE2 1 
ATOM   2219 N N   . ASP   A 1 289 ? -19.24140 -27.44987 5.00319   1.000 18.75747  ? 289 ASP   A N   1 
ATOM   2220 C CA  . ASP   A 1 289 ? -18.01398 -26.87927 5.54495   1.000 22.61512  ? 289 ASP   A CA  1 
ATOM   2221 C C   . ASP   A 1 289 ? -17.81891 -25.40459 5.24694   1.000 24.90352  ? 289 ASP   A C   1 
ATOM   2222 O O   . ASP   A 1 289 ? -16.70406 -24.90330 5.46946   1.000 22.79766  ? 289 ASP   A O   1 
ATOM   2223 C CB  . ASP   A 1 289 ? -16.77531 -27.63326 5.04221   1.000 23.12070  ? 289 ASP   A CB  1 
ATOM   2224 C CG  . ASP   A 1 289 ? -16.41867 -27.33551 3.57077   1.000 23.32092  ? 289 ASP   A CG  1 
ATOM   2225 O OD1 . ASP   A 1 289 ? -15.27706 -27.68529 3.18044   1.000 27.27208  ? 289 ASP   A OD1 1 
ATOM   2226 O OD2 . ASP   A 1 289 ? -17.25837 -26.82832 2.77734   1.000 22.98679  ? 289 ASP   A OD2 1 
ATOM   2227 N N   . GLU   A 1 290 ? -18.82050 -24.69643 4.70577   1.000 19.95319  ? 290 GLU   A N   1 
ATOM   2228 C CA  . GLU   A 1 290 ? -18.60558 -23.28569 4.39175   1.000 22.23768  ? 290 GLU   A CA  1 
ATOM   2229 C C   . GLU   A 1 290 ? -19.23573 -22.35806 5.42873   1.000 21.34779  ? 290 GLU   A C   1 
ATOM   2230 O O   . GLU   A 1 290 ? -19.67335 -21.24671 5.09723   1.000 20.07707  ? 290 GLU   A O   1 
ATOM   2231 C CB  . GLU   A 1 290 ? -19.07631 -22.94449 2.97791   1.000 20.07801  ? 290 GLU   A CB  1 
ATOM   2232 C CG  . GLU   A 1 290 ? -18.14329 -23.48494 1.88208   1.000 19.69200  ? 290 GLU   A CG  1 
ATOM   2233 C CD  . GLU   A 1 290 ? -18.19044 -22.69721 0.58332   1.000 20.99759  ? 290 GLU   A CD  1 
ATOM   2234 O OE1 . GLU   A 1 290 ? -17.17161 -22.72279 -0.15855  1.000 22.70439  ? 290 GLU   A OE1 1 
ATOM   2235 O OE2 . GLU   A 1 290 ? -19.23440 -22.04731 0.30183   1.000 20.56945  ? 290 GLU   A OE2 1 
ATOM   2236 N N   . PHE   A 1 291 ? -19.24279 -22.78804 6.68905   1.000 18.16065  ? 291 PHE   A N   1 
ATOM   2237 C CA  . PHE   A 1 291 ? -19.69048 -21.98063 7.81426   1.000 23.25759  ? 291 PHE   A CA  1 
ATOM   2238 C C   . PHE   A 1 291 ? -18.60766 -22.01205 8.88625   1.000 19.34222  ? 291 PHE   A C   1 
ATOM   2239 O O   . PHE   A 1 291 ? -18.32079 -23.07490 9.44095   1.000 20.12716  ? 291 PHE   A O   1 
ATOM   2240 C CB  . PHE   A 1 291 ? -20.99631 -22.52734 8.40304   1.000 22.89942  ? 291 PHE   A CB  1 
ATOM   2241 C CG  . PHE   A 1 291 ? -22.20386 -22.37686 7.53225   1.000 25.71081  ? 291 PHE   A CG  1 
ATOM   2242 C CD1 . PHE   A 1 291 ? -22.80276 -21.12450 7.34178   1.000 25.74738  ? 291 PHE   A CD1 1 
ATOM   2243 C CD2 . PHE   A 1 291 ? -22.82550 -23.49963 6.99162   1.000 25.47201  ? 291 PHE   A CD2 1 
ATOM   2244 C CE1 . PHE   A 1 291 ? -23.97021 -20.99273 6.58909   1.000 16.41160  ? 291 PHE   A CE1 1 
ATOM   2245 C CE2 . PHE   A 1 291 ? -23.99934 -23.37066 6.24097   1.000 23.30238  ? 291 PHE   A CE2 1 
ATOM   2246 C CZ  . PHE   A 1 291 ? -24.57179 -22.11193 6.04476   1.000 16.74730  ? 291 PHE   A CZ  1 
ATOM   2247 N N   . THR   A 1 292 ? -18.03855 -20.86071 9.20522   1.000 21.76821  ? 292 THR   A N   1 
ATOM   2248 C CA  . THR   A 1 292 ? -17.05533 -20.75940 10.28084  1.000 24.13601  ? 292 THR   A CA  1 
ATOM   2249 C C   . THR   A 1 292 ? -17.74303 -20.76516 11.64738  1.000 22.65364  ? 292 THR   A C   1 
ATOM   2250 O O   . THR   A 1 292 ? -18.96047 -20.58384 11.75618  1.000 19.76363  ? 292 THR   A O   1 
ATOM   2251 C CB  . THR   A 1 292 ? -16.22827 -19.48869 10.10953  1.000 22.19754  ? 292 THR   A CB  1 
ATOM   2252 O OG1 . THR   A 1 292 ? -17.08969 -18.35132 10.14961  1.000 21.03296  ? 292 THR   A OG1 1 
ATOM   2253 C CG2 . THR   A 1 292 ? -15.51569 -19.50324 8.81168   1.000 21.86341  ? 292 THR   A CG2 1 
ATOM   2254 N N   . PRO   A 1 293 ? -16.98104 -20.97032 12.72615  1.000 21.37699  ? 293 PRO   A N   1 
ATOM   2255 C CA  . PRO   A 1 293 ? -17.57865 -20.82283 14.06014  1.000 23.80257  ? 293 PRO   A CA  1 
ATOM   2256 C C   . PRO   A 1 293 ? -18.11674 -19.42411 14.30042  1.000 24.56034  ? 293 PRO   A C   1 
ATOM   2257 O O   . PRO   A 1 293 ? -19.17911 -19.26646 14.92740  1.000 21.27971  ? 293 PRO   A O   1 
ATOM   2258 C CB  . PRO   A 1 293 ? -16.41998 -21.17886 15.01173  1.000 20.74600  ? 293 PRO   A CB  1 
ATOM   2259 C CG  . PRO   A 1 293 ? -15.46141 -21.94985 14.19270  1.000 22.65233  ? 293 PRO   A CG  1 
ATOM   2260 C CD  . PRO   A 1 293 ? -15.55605 -21.33952 12.81967  1.000 28.28216  ? 293 PRO   A CD  1 
ATOM   2261 N N   . PHE   A 1 294 ? -17.42957 -18.40543 13.77438  1.000 24.56926  ? 294 PHE   A N   1 
ATOM   2262 C CA  . PHE   A 1 294 ? -17.97663 -17.05659 13.80057  1.000 25.06731  ? 294 PHE   A CA  1 
ATOM   2263 C C   . PHE   A 1 294 ? -19.35185 -17.00081 13.14968  1.000 25.05723  ? 294 PHE   A C   1 
ATOM   2264 O O   . PHE   A 1 294 ? -20.29981 -16.47531 13.74630  1.000 26.09709  ? 294 PHE   A O   1 
ATOM   2265 C CB  . PHE   A 1 294 ? -17.04394 -16.08688 13.10845  1.000 24.94250  ? 294 PHE   A CB  1 
ATOM   2266 C CG  . PHE   A 1 294 ? -17.51180 -14.68050 13.19270  1.000 29.59753  ? 294 PHE   A CG  1 
ATOM   2267 C CD1 . PHE   A 1 294 ? -17.29979 -13.94100 14.34460  1.000 28.80314  ? 294 PHE   A CD1 1 
ATOM   2268 C CD2 . PHE   A 1 294 ? -18.20206 -14.09872 12.13537  1.000 34.41980  ? 294 PHE   A CD2 1 
ATOM   2269 C CE1 . PHE   A 1 294 ? -17.73020 -12.63114 14.42974  1.000 30.32486  ? 294 PHE   A CE1 1 
ATOM   2270 C CE2 . PHE   A 1 294 ? -18.64964 -12.78415 12.21415  1.000 33.84863  ? 294 PHE   A CE2 1 
ATOM   2271 C CZ  . PHE   A 1 294 ? -18.40713 -12.05294 13.36344  1.000 37.41257  ? 294 PHE   A CZ  1 
ATOM   2272 N N   . ASP   A 1 295 ? -19.47339 -17.53573 11.92182  1.000 23.06869  ? 295 ASP   A N   1 
ATOM   2273 C CA  . ASP   A 1 295 ? -20.74139 -17.54103 11.18715  1.000 23.36741  ? 295 ASP   A CA  1 
ATOM   2274 C C   . ASP   A 1 295 ? -21.88066 -18.13423 12.01233  1.000 30.03167  ? 295 ASP   A C   1 
ATOM   2275 O O   . ASP   A 1 295 ? -22.94206 -17.51538 12.16676  1.000 28.20403  ? 295 ASP   A O   1 
ATOM   2276 C CB  . ASP   A 1 295 ? -20.60764 -18.34011 9.89344   1.000 23.07699  ? 295 ASP   A CB  1 
ATOM   2277 C CG  . ASP   A 1 295 ? -19.72810 -17.66951 8.88718   1.000 21.33140  ? 295 ASP   A CG  1 
ATOM   2278 O OD1 . ASP   A 1 295 ? -19.49065 -16.45474 9.03986   1.000 28.46732  ? 295 ASP   A OD1 1 
ATOM   2279 O OD2 . ASP   A 1 295 ? -19.30227 -18.35610 7.93621   1.000 17.85834  ? 295 ASP   A OD2 1 
ATOM   2280 N N   . VAL   A 1 296 ? -21.68700 -19.36887 12.50097  1.000 25.87662  ? 296 VAL   A N   1 
ATOM   2281 C CA  . VAL   A 1 296 ? -22.69699 -20.01885 13.33494  1.000 29.96211  ? 296 VAL   A CA  1 
ATOM   2282 C C   . VAL   A 1 296 ? -23.14286 -19.09413 14.46594  1.000 31.78875  ? 296 VAL   A C   1 
ATOM   2283 O O   . VAL   A 1 296 ? -24.34368 -18.92620 14.71520  1.000 32.73348  ? 296 VAL   A O   1 
ATOM   2284 C CB  . VAL   A 1 296 ? -22.17128 -21.36262 13.87617  1.000 21.00576  ? 296 VAL   A CB  1 
ATOM   2285 C CG1 . VAL   A 1 296 ? -23.10145 -21.88596 14.92262  1.000 25.82602  ? 296 VAL   A CG1 1 
ATOM   2286 C CG2 . VAL   A 1 296 ? -22.09054 -22.36138 12.76791  1.000 19.26084  ? 296 VAL   A CG2 1 
ATOM   2287 N N   . VAL   A 1 297 ? -22.18455 -18.47724 15.16432  1.000 29.54340  ? 297 VAL   A N   1 
ATOM   2288 C CA  . VAL   A 1 297 ? -22.52902 -17.59619 16.27938  1.000 29.97256  ? 297 VAL   A CA  1 
ATOM   2289 C C   . VAL   A 1 297 ? -23.25628 -16.34462 15.78112  1.000 35.57678  ? 297 VAL   A C   1 
ATOM   2290 O O   . VAL   A 1 297 ? -24.25198 -15.92546 16.37577  1.000 40.71314  ? 297 VAL   A O   1 
ATOM   2291 C CB  . VAL   A 1 297 ? -21.27207 -17.24914 17.10691  1.000 31.14103  ? 297 VAL   A CB  1 
ATOM   2292 C CG1 . VAL   A 1 297 ? -21.56935 -16.16944 18.15267  1.000 25.02202  ? 297 VAL   A CG1 1 
ATOM   2293 C CG2 . VAL   A 1 297 ? -20.69968 -18.50396 17.77661  1.000 30.29170  ? 297 VAL   A CG2 1 
ATOM   2294 N N   . ARG   A 1 298 ? -22.78546 -15.73287 14.68494  1.000 33.78935  ? 298 ARG   A N   1 
ATOM   2295 C CA  . ARG   A 1 298 ? -23.52396 -14.61454 14.09413  1.000 38.18279  ? 298 ARG   A CA  1 
ATOM   2296 C C   . ARG   A 1 298 ? -24.98399 -14.98369 13.83782  1.000 40.20226  ? 298 ARG   A C   1 
ATOM   2297 O O   . ARG   A 1 298 ? -25.89271 -14.24357 14.22469  1.000 50.88970  ? 298 ARG   A O   1 
ATOM   2298 C CB  . ARG   A 1 298 ? -22.83972 -14.11144 12.79667  1.000 37.60233  ? 298 ARG   A CB  1 
ATOM   2299 C CG  . ARG   A 1 298 ? -23.68178 -12.99046 12.01714  1.000 56.60756  ? 298 ARG   A CG  1 
ATOM   2300 C CD  . ARG   A 1 298 ? -22.95952 -12.28831 10.85713  1.000 50.65506  ? 298 ARG   A CD  1 
ATOM   2301 N NE  . ARG   A 1 298 ? -22.56847 -13.00032 9.63267   1.000 40.47989  ? 298 ARG   A NE  1 
ATOM   2302 C CZ  . ARG   A 1 298 ? -23.29230 -13.07976 8.52041   1.000 36.17105  ? 298 ARG   A CZ  1 
ATOM   2303 N NH1 . ARG   A 1 298 ? -24.40362 -12.34379 8.38896   1.000 35.72886  ? 298 ARG   A NH1 1 
ATOM   2304 N NH2 . ARG   A 1 298 ? -22.82834 -13.79475 7.48550   1.000 33.00715  ? 298 ARG   A NH2 1 
ATOM   2305 N N   . GLN   A 1 299 ? -25.23394 -16.14792 13.23739  1.000 32.84370  ? 299 GLN   A N   1 
ATOM   2306 C CA  . GLN   A 1 299 ? -26.58253 -16.48036 12.79415  1.000 36.51450  ? 299 GLN   A CA  1 
ATOM   2307 C C   . GLN   A 1 299 ? -27.45845 -17.01581 13.93475  1.000 38.62788  ? 299 GLN   A C   1 
ATOM   2308 O O   . GLN   A 1 299 ? -28.62803 -16.64419 14.03127  1.000 38.78355  ? 299 GLN   A O   1 
ATOM   2309 C CB  . GLN   A 1 299 ? -26.48725 -17.46793 11.62381  1.000 28.08972  ? 299 GLN   A CB  1 
ATOM   2310 C CG  . GLN   A 1 299 ? -27.80517 -17.75428 10.95593  1.000 29.19500  ? 299 GLN   A CG  1 
ATOM   2311 C CD  . GLN   A 1 299 ? -27.66640 -18.41065 9.58546   1.000 25.56105  ? 299 GLN   A CD  1 
ATOM   2312 O OE1 . GLN   A 1 299 ? -28.64625 -18.93376 9.04761   1.000 25.53138  ? 299 GLN   A OE1 1 
ATOM   2313 N NE2 . GLN   A 1 299 ? -26.46465 -18.37443 9.00849   1.000 21.12176  ? 299 GLN   A NE2 1 
ATOM   2314 N N   . CYS   A 1 300 ? -26.92825 -17.88841 14.80006  1.000 37.71644  ? 300 CYS   A N   1 
ATOM   2315 C CA  . CYS   A 1 300 ? -27.70562 -18.50465 15.87667  1.000 39.08274  ? 300 CYS   A CA  1 
ATOM   2316 C C   . CYS   A 1 300 ? -27.80033 -17.63672 17.13095  1.000 47.38587  ? 300 CYS   A C   1 
ATOM   2317 O O   . CYS   A 1 300 ? -28.37276 -18.08858 18.14027  1.000 50.87493  ? 300 CYS   A O   1 
ATOM   2318 C CB  . CYS   A 1 300 ? -27.10563 -19.86475 16.24365  1.000 32.80973  ? 300 CYS   A CB  1 
ATOM   2319 S SG  . CYS   A 1 300 ? -27.04266 -21.03908 14.86234  1.000 30.90852  ? 300 CYS   A SG  1 
ATOM   2320 N N   . SER   A 1 301 ? -27.26276 -16.41230 17.08156  1.000 52.38829  ? 301 SER   A N   1 
ATOM   2321 C CA  . SER   A 1 301 ? -27.25393 -15.47686 18.20207  1.000 56.57925  ? 301 SER   A CA  1 
ATOM   2322 C C   . SER   A 1 301 ? -27.76256 -14.10245 17.75869  1.000 58.14891  ? 301 SER   A C   1 
ATOM   2323 O O   . SER   A 1 301 ? -28.38161 -13.38183 18.55043  1.000 61.74733  ? 301 SER   A O   1 
ATOM   2324 C CB  . SER   A 1 301 ? -25.84193 -15.39424 18.80900  1.000 59.03522  ? 301 SER   A CB  1 
ATOM   2325 O OG  . SER   A 1 301 ? -25.63530 -14.21341 19.56654  1.000 68.34954  ? 301 SER   A OG  1 
ATOM   2326 N N   . GLY   A 1 302 ? -27.51088 -13.72526 16.50122  1.000 64.63545  ? 302 GLY   A N   1 
ATOM   2327 C CA  . GLY   A 1 302 ? -28.23701 -12.62311 15.87938  1.000 65.30489  ? 302 GLY   A CA  1 
ATOM   2328 C C   . GLY   A 1 302 ? -27.51162 -11.29788 15.75356  1.000 77.22625  ? 302 GLY   A C   1 
ATOM   2329 O O   . GLY   A 1 302 ? -28.10662 -10.24431 16.00561  1.000 74.08355  ? 302 GLY   A O   1 
ATOM   2330 N N   . VAL   A 1 303 ? -26.24640 -11.33657 15.32564  1.000 93.08718  ? 303 VAL   A N   1 
ATOM   2331 C CA  . VAL   A 1 303 ? -25.36924 -10.16460 15.34027  1.000 98.69818  ? 303 VAL   A CA  1 
ATOM   2332 C C   . VAL   A 1 303 ? -25.64699 -9.29531  14.11193  1.000 95.45284  ? 303 VAL   A C   1 
ATOM   2333 O O   . VAL   A 1 303 ? -25.70424 -9.79921  12.98069  1.000 91.35464  ? 303 VAL   A O   1 
ATOM   2334 C CB  . VAL   A 1 303 ? -23.89073 -10.60374 15.41114  1.000 95.02291  ? 303 VAL   A CB  1 
ATOM   2335 C CG1 . VAL   A 1 303 ? -22.93447 -9.40595  15.25149  1.000 96.85093  ? 303 VAL   A CG1 1 
ATOM   2336 C CG2 . VAL   A 1 303 ? -23.61867 -11.37154 16.71932  1.000 84.08708  ? 303 VAL   A CG2 1 
ATOM   2337 N N   . THR   A 1 304 ? -25.80520 -7.97082  14.33736  1.000 97.56287  ? 304 THR   A N   1 
ATOM   2338 C CA  . THR   A 1 304 ? -26.17941 -6.96241  13.34224  1.000 96.05697  ? 304 THR   A CA  1 
ATOM   2339 C C   . THR   A 1 304 ? -25.01028 -6.00806  13.05020  1.000 111.77531 ? 304 THR   A C   1 
ATOM   2340 O O   . THR   A 1 304 ? -23.89185 -6.17753  13.56683  1.000 109.05173 ? 304 THR   A O   1 
ATOM   2341 C CB  . THR   A 1 304 ? -27.41446 -6.17343  13.81360  1.000 88.90056  ? 304 THR   A CB  1 
ATOM   2342 O OG1 . THR   A 1 304 ? -27.06731 -5.34618  14.93562  1.000 95.87751  ? 304 THR   A OG1 1 
ATOM   2343 C CG2 . THR   A 1 304 ? -28.54856 -7.11362  14.21304  1.000 80.70218  ? 304 THR   A CG2 1 
ATOM   2344 N N   . PHE   A 1 305 ? -25.28577 -4.97918  12.23417  1.000 130.19861 ? 305 PHE   A N   1 
ATOM   2345 C CA  . PHE   A 1 305 ? -24.25887 -4.06979  11.72120  1.000 133.08584 ? 305 PHE   A CA  1 
ATOM   2346 C C   . PHE   A 1 305 ? -24.82587 -2.67141  11.50408  1.000 133.99702 ? 305 PHE   A C   1 
ATOM   2347 O O   . PHE   A 1 305 ? -26.02826 -2.48824  11.29120  1.000 139.22666 ? 305 PHE   A O   1 
ATOM   2348 C CB  . PHE   A 1 305 ? -23.65792 -4.59524  10.40806  1.000 128.70441 ? 305 PHE   A CB  1 
ATOM   2349 C CG  . PHE   A 1 305 ? -23.13717 -5.98156  10.52627  1.000 123.92840 ? 305 PHE   A CG  1 
ATOM   2350 C CD1 . PHE   A 1 305 ? -21.98118 -6.22708  11.24533  1.000 122.51874 ? 305 PHE   A CD1 1 
ATOM   2351 C CD2 . PHE   A 1 305 ? -23.83642 -7.04916  9.98917   1.000 121.22577 ? 305 PHE   A CD2 1 
ATOM   2352 C CE1 . PHE   A 1 305 ? -21.50794 -7.50351  11.40228  1.000 122.87114 ? 305 PHE   A CE1 1 
ATOM   2353 C CE2 . PHE   A 1 305 ? -23.36959 -8.33065  10.14389  1.000 121.38034 ? 305 PHE   A CE2 1 
ATOM   2354 C CZ  . PHE   A 1 305 ? -22.20107 -8.55504  10.85850  1.000 122.13301 ? 305 PHE   A CZ  1 
ATOM   2355 N N   . GLN   A 1 306 ? -23.93118 -1.68535  11.54264  1.000 93.30546  ? 306 GLN   A N   1 
ATOM   2356 C CA  . GLN   A 1 306 ? -24.29416 -0.29257  11.28821  1.000 91.34989  ? 306 GLN   A CA  1 
ATOM   2357 C C   . GLN   A 1 306 ? -23.19636 0.41127   10.49162  1.000 80.17024  ? 306 GLN   A C   1 
ATOM   2358 O O   . GLN   A 1 306 ? -23.45222 0.98042   9.42702   1.000 79.35796  ? 306 GLN   A O   1 
ATOM   2359 C CB  . GLN   A 1 306 ? -24.55839 0.46037   12.60279  1.000 89.15304  ? 306 GLN   A CB  1 
ATOM   2360 C CG  . GLN   A 1 306 ? -25.91384 0.16867   13.27005  1.000 82.48092  ? 306 GLN   A CG  1 
ATOM   2361 C CD  . GLN   A 1 306 ? -27.11535 0.71853   12.49196  1.000 81.12463  ? 306 GLN   A CD  1 
ATOM   2362 O OE1 . GLN   A 1 306 ? -27.55560 1.85257   12.71786  1.000 78.31235  ? 306 GLN   A OE1 1 
ATOM   2363 N NE2 . GLN   A 1 306 ? -27.66094 -0.09558  11.58466  1.000 73.07733  ? 306 GLN   A NE2 1 
HETATM 2364 N N   . A1ARU B 2 .   ? -9.46822  -15.74164 -17.62392 1.000 34.29130  ? 401 A1ARU A N   1 
HETATM 2365 C C   . A1ARU B 2 .   ? -9.84905  -18.04725 -17.97906 1.000 39.04156  ? 401 A1ARU A C   1 
HETATM 2366 O O   . A1ARU B 2 .   ? -10.85673 -16.78996 -16.20415 1.000 33.28851  ? 401 A1ARU A O   1 
HETATM 2367 C C1  . A1ARU B 2 .   ? -10.12002 -16.80136 -17.18186 1.000 35.30224  ? 401 A1ARU A C1  1 
HETATM 2368 C C10 . A1ARU B 2 .   ? -14.93219 -16.03594 -14.95064 1.000 27.49594  ? 401 A1ARU A C10 1 
HETATM 2369 C C11 . A1ARU B 2 .   ? -9.15703  -13.48647 -18.38072 1.000 40.88145  ? 401 A1ARU A C11 1 
HETATM 2370 C C12 . A1ARU B 2 .   ? -7.80746  -12.91174 -17.95906 1.000 40.75236  ? 401 A1ARU A C12 1 
HETATM 2371 C C13 . A1ARU B 2 .   ? -11.14298 -18.65334 -18.51835 1.000 37.72535  ? 401 A1ARU A C13 1 
HETATM 2372 C C14 . A1ARU B 2 .   ? -11.71180 -17.75128 -19.61328 1.000 39.98238  ? 401 A1ARU A C14 1 
HETATM 2373 C C15 . A1ARU B 2 .   ? -7.77559  -19.17183 -17.43926 1.000 41.74910  ? 401 A1ARU A C15 1 
HETATM 2374 C C16 . A1ARU B 2 .   ? -6.96220  -19.96253 -16.42140 1.000 42.31996  ? 401 A1ARU A C16 1 
HETATM 2375 C C17 . A1ARU B 2 .   ? -11.95512 -20.92949 -18.92366 1.000 44.41223  ? 401 A1ARU A C17 1 
HETATM 2376 C C18 . A1ARU B 2 .   ? -12.99364 -20.54830 -17.87345 1.000 34.95950  ? 401 A1ARU A C18 1 
HETATM 2377 C C19 . A1ARU B 2 .   ? -11.38780 -22.29523 -18.53790 1.000 42.42072  ? 401 A1ARU A C19 1 
HETATM 2378 C C2  . A1ARU B 2 .   ? -9.83270  -14.37263 -17.33769 1.000 35.48389  ? 401 A1ARU A C2  1 
HETATM 2379 C C20 . A1ARU B 2 .   ? -12.63334 -21.03585 -20.28818 1.000 37.05428  ? 401 A1ARU A C20 1 
HETATM 2380 C C21 . A1ARU B 2 .   ? -6.93061  -12.82139 -19.20338 1.000 46.42072  ? 401 A1ARU A C21 1 
HETATM 2381 C C22 . A1ARU B 2 .   ? -5.47833  -12.44733 -18.93040 1.000 51.66938  ? 401 A1ARU A C22 1 
HETATM 2382 C C23 . A1ARU B 2 .   ? -4.87970  -13.39430 -17.90116 1.000 43.82960  ? 401 A1ARU A C23 1 
HETATM 2383 C C24 . A1ARU B 2 .   ? -5.70640  -13.31598 -16.62937 1.000 41.29057  ? 401 A1ARU A C24 1 
HETATM 2384 C C25 . A1ARU B 2 .   ? -7.13439  -13.78013 -16.90167 1.000 42.10722  ? 401 A1ARU A C25 1 
HETATM 2385 C C3  . A1ARU B 2 .   ? -11.30921 -14.11684 -17.40617 1.000 34.05839  ? 401 A1ARU A C3  1 
HETATM 2386 C C4  . A1ARU B 2 .   ? -13.19990 -12.91724 -16.39468 1.000 32.29980  ? 401 A1ARU A C4  1 
HETATM 2387 C C5  . A1ARU B 2 .   ? -13.14339 -11.44733 -16.01776 1.000 27.38909  ? 401 A1ARU A C5  1 
HETATM 2388 C C6  . A1ARU B 2 .   ? -14.10804 -13.69671 -15.43796 1.000 27.25395  ? 401 A1ARU A C6  1 
HETATM 2389 C C7  . A1ARU B 2 .   ? -14.15063 -15.15331 -15.87827 1.000 27.98416  ? 401 A1ARU A C7  1 
HETATM 2390 C C8  . A1ARU B 2 .   ? -14.88530 -15.29198 -17.20929 1.000 29.25803  ? 401 A1ARU A C8  1 
HETATM 2391 C C9  . A1ARU B 2 .   ? -15.89828 -16.42338 -17.02540 1.000 29.53273  ? 401 A1ARU A C9  1 
HETATM 2392 F F17 . A1ARU B 2 .   ? -5.66302  -19.77842 -16.62160 1.000 45.21152  ? 401 A1ARU A F17 1 
HETATM 2393 F F18 . A1ARU B 2 .   ? -7.22092  -21.25726 -16.51213 1.000 48.21061  ? 401 A1ARU A F18 1 
HETATM 2394 F F19 . A1ARU B 2 .   ? -7.26554  -19.56363 -15.19795 1.000 39.35203  ? 401 A1ARU A F19 1 
HETATM 2395 N N1  . A1ARU B 2 .   ? -11.86307 -13.49401 -16.36688 1.000 31.16490  ? 401 A1ARU A N1  1 
HETATM 2396 N N2  . A1ARU B 2 .   ? -15.86150 -16.72930 -15.60933 1.000 28.34942  ? 401 A1ARU A N2  1 
HETATM 2397 N N3  . A1ARU B 2 .   ? -9.08223  -19.02097 -17.21454 1.000 41.42153  ? 401 A1ARU A N3  1 
HETATM 2398 N N4  . A1ARU B 2 .   ? -14.16550 -10.71814 -16.07613 1.000 27.41867  ? 401 A1ARU A N4  1 
HETATM 2399 O O1  . A1ARU B 2 .   ? -11.94306 -14.45896 -18.38834 1.000 39.70700  ? 401 A1ARU A O1  1 
HETATM 2400 O O3  . A1ARU B 2 .   ? -14.70548 -16.09723 -13.75674 1.000 26.56519  ? 401 A1ARU A O3  1 
HETATM 2401 O O4  . A1ARU B 2 .   ? -10.87000 -19.97715 -18.99846 1.000 38.90437  ? 401 A1ARU A O4  1 
HETATM 2402 O O6  . A1ARU B 2 .   ? -7.24685  -18.68326 -18.43056 1.000 49.39109  ? 401 A1ARU A O6  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   . SER   A 1   ? 0.24961 0.43628 0.32941 -0.01368 0.06701  0.13520  1   SER   A N   
2    C CA  . SER   A 1   ? 0.28097 0.45897 0.36762 -0.02102 0.05485  0.14347  1   SER   A CA  
3    C C   . SER   A 1   ? 0.28591 0.45071 0.38278 -0.02073 0.04284  0.13769  1   SER   A C   
4    O O   . SER   A 1   ? 0.21141 0.37772 0.31518 -0.01529 0.04368  0.13060  1   SER   A O   
5    C CB  . SER   A 1   ? 0.25064 0.44333 0.35540 -0.02791 0.05827  0.15837  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.34808 0.53093 0.46447 -0.03547 0.04687  0.16528  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.31098 0.46262 0.40800 -0.02646 0.03226  0.14099  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.26270 0.39938 0.36332 -0.02727 0.02078  0.13449  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.29985 0.42076 0.38045 -0.02294 0.01680  0.12504  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.36503 0.48762 0.42956 -0.01857 0.02261  0.12130  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.20779 0.31369 0.28934 -0.02487 0.00685  0.12073  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.19963 0.29094 0.26508 -0.02150 0.00271  0.11320  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.26835 0.34803 0.33635 -0.02157 -0.00555 0.10512  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.34701 0.41998 0.42429 -0.02733 -0.01175 0.10681  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.20694 0.29086 0.26755 -0.02444 0.00062  0.12006  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.29340 0.36945 0.33713 -0.01990 -0.00091 0.11458  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.27303 0.33374 0.31522 -0.01903 -0.00779 0.10921  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.26622 0.35118 0.29561 -0.01686 0.00483  0.11378  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.27047 0.32645 0.29969 -0.01497 -0.00908 0.10496  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.27587 0.35570 0.29107 -0.01393 0.00255  0.10886  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.30079 0.36677 0.31712 -0.01281 -0.00458 0.10516  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.20369 0.28042 0.26263 -0.01588 -0.00546 0.09614  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.24664 0.31540 0.30663 -0.01565 -0.01231 0.08921  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.22563 0.28222 0.27050 -0.01172 -0.01426 0.08126  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.20856 0.26596 0.24277 -0.00787 -0.00972 0.07940  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.28973 0.36939 0.35822 -0.01255 -0.01034 0.08825  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.20043 0.29256 0.28818 -0.01764 -0.01200 0.09566  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.22680 0.31330 0.31892 -0.02327 -0.02256 0.09323  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.24074 0.34056 0.35168 -0.02946 -0.02587 0.09998  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.28368 0.38082 0.39985 -0.03776 -0.03544 0.09900  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.18828 0.30010 0.32304 -0.04443 -0.03879 0.10589  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.25544 0.33590 0.35830 -0.03994 -0.04146 0.09073  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.22218 0.26826 0.26569 -0.01334 -0.02089 0.07625  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.25096 0.28851 0.28212 -0.00912 -0.02180 0.06877  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.22331 0.26716 0.25290 -0.00450 -0.01855 0.06581  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.22218 0.26846 0.25722 -0.00458 -0.02145 0.06497  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.20717 0.23327 0.23612 -0.01151 -0.02803 0.06343  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.29054 0.30686 0.32163 -0.01492 -0.02986 0.06500  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.32914 0.33242 0.35406 -0.01487 -0.03301 0.05740  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.33250 0.33176 0.34994 -0.00940 -0.03027 0.05616  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 0.31361 0.31050 0.33630 -0.00948 -0.02872 0.06334  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.21362 0.26046 0.23628 -0.00081 -0.01244 0.06471  6   MET   A N   
43   C CA  . MET   A 6   ? 0.23459 0.28612 0.25768 0.00374  -0.00722 0.06189  6   MET   A CA  
44   C C   . MET   A 6   ? 0.21455 0.25734 0.22657 0.00668  -0.00743 0.05462  6   MET   A C   
45   O O   . MET   A 6   ? 0.26976 0.30878 0.27140 0.00624  -0.00701 0.05204  6   MET   A O   
46   C CB  . MET   A 6   ? 0.18189 0.24274 0.20485 0.00501  0.00127  0.06420  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.24542 0.31102 0.27360 0.01008  0.00813  0.06170  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.30280 0.37880 0.32798 0.01149  0.02014  0.06217  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.23669 0.32536 0.27696 0.00700  0.01905  0.07380  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.19335 0.23410 0.20875 0.00918  -0.00857 0.05257  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.23203 0.26478 0.23922 0.01158  -0.00820 0.04676  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.24250 0.27588 0.24963 0.01567  -0.00018 0.04354  7   ALA   A C   
53   O O   . ALA   A 7   ? 0.23573 0.27604 0.25245 0.01826  0.00477  0.04627  7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.24484 0.27441 0.25496 0.01166  -0.01381 0.04736  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.27637 0.30236 0.27346 0.01601  0.00158  0.03731  8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.29397 0.31653 0.29030 0.01924  0.00923  0.03214  8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.23428 0.25536 0.24332 0.02394  0.01031  0.03516  8   PHE   A C   
58   O O   . PHE   A 8   ? 0.18721 0.20756 0.20001 0.02355  0.00363  0.03938  8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.25393 0.26811 0.23829 0.01708  0.00917  0.02504  8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.33733 0.35527 0.31036 0.01286  0.00832  0.02302  8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.46681 0.48838 0.43275 0.01186  0.01479  0.01889  8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.34069 0.35958 0.31036 0.01002  0.00131  0.02589  8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.49019 0.51771 0.44481 0.00733  0.01284  0.01886  8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.35435 0.37849 0.31570 0.00663  -0.00011 0.02639  8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.37948 0.40869 0.33292 0.00497  0.00498  0.02353  8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.21622 0.23752 0.23235 0.02859  0.01891  0.03357  9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.19717 0.21665 0.22746 0.03408  0.02012  0.03784  9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.19484 0.20264 0.21914 0.03315  0.01663  0.03554  9   PRO   A C   
69   O O   . PRO   A 9   ? 0.19889 0.19843 0.21084 0.03008  0.01816  0.02785  9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.20511 0.22355 0.24220 0.03963  0.03242  0.03385  9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.26615 0.28918 0.29151 0.03615  0.03715  0.02823  9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.25750 0.27850 0.26711 0.02907  0.02852  0.02653  9   PRO   A CD  
73   N N   . SER   A 10  ? 0.19172 0.20074 0.22451 0.03485  0.01115  0.04312  10  SER   A N   
74   C CA  . SER   A 10  ? 0.19198 0.19275 0.21864 0.03297  0.00666  0.04329  10  SER   A CA  
75   C C   . SER   A 10  ? 0.20135 0.19330 0.23733 0.03804  0.01157  0.04541  10  SER   A C   
76   O O   . SER   A 10  ? 0.20601 0.19234 0.23944 0.03679  0.00800  0.04824  10  SER   A O   
77   C CB  . SER   A 10  ? 0.19466 0.20285 0.22064 0.02995  -0.00336 0.05023  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.18568 0.20227 0.22609 0.03342  -0.00572 0.05978  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.25643 0.24694 0.30421 0.04401  0.02038  0.04472  11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.22059 0.20067 0.28009 0.04977  0.02608  0.04727  11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.22987 0.19379 0.27898 0.04612  0.02800  0.04001  11  GLY   A C   
82   O O   . GLY   A 11  ? 0.27206 0.22946 0.32567 0.04691  0.02586  0.04613  11  GLY   A O   
83   N N   . LYS   A 12  ? 0.23111 0.18973 0.26614 0.04121  0.03143  0.02777  12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.26149 0.20611 0.28775 0.03640  0.03283  0.02052  12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.25760 0.20363 0.27933 0.03231  0.02388  0.02707  12  LYS   A C   
86   O O   . LYS   A 12  ? 0.29051 0.22555 0.31423 0.03107  0.02504  0.02799  12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.25992 0.20355 0.27040 0.03024  0.03529  0.00764  12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.27876 0.21917 0.29108 0.03358  0.04591  -0.00043 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 0.42085 0.35955 0.41544 0.02633  0.04840  -0.01353 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 0.52591 0.45379 0.52094 0.02874  0.06148  -0.02494 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 0.60568 0.54367 0.60743 0.03538  0.06808  -0.02277 12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.21779 0.17672 0.23408 0.03017  0.01570  0.03181  13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.25092 0.21205 0.26119 0.02634  0.00841  0.03673  13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.27067 0.23467 0.29010 0.02982  0.00484  0.04914  13  VAL   A C   
95   O O   . VAL   A 13  ? 0.22723 0.18828 0.24338 0.02737  0.00229  0.05333  13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.22965 0.20115 0.22961 0.02239  0.00218  0.03504  13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.19693 0.17064 0.19081 0.01921  -0.00359 0.03904  13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.23073 0.20130 0.22181 0.01866  0.00447  0.02539  13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.21236 0.18409 0.24339 0.03504  0.00426  0.05614  14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.21521 0.19234 0.25577 0.03809  -0.00021 0.06951  14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.27540 0.24009 0.32304 0.04050  0.00401  0.07435  14  GLU   A C   
102  O O   . GLU   A 14  ? 0.30702 0.27416 0.35424 0.03949  -0.00085 0.08443  14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.21427 0.20213 0.27067 0.04392  -0.00028 0.07663  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.20351 0.20581 0.25632 0.04090  -0.00585 0.07536  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.20345 0.21541 0.27413 0.04663  -0.00271 0.08002  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.20928 0.22523 0.29692 0.05257  -0.00224 0.09068  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.19823 0.21498 0.26740 0.04541  -0.00048 0.07419  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.23660 0.18751 0.29054 0.04327  0.01336  0.06740  15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.25094 0.18678 0.31367 0.04536  0.01861  0.07101  15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.28124 0.20831 0.33199 0.03785  0.01774  0.06692  15  GLY   A C   
111  O O   . GLY   A 15  ? 0.28442 0.19702 0.34188 0.03792  0.02259  0.06860  15  GLY   A O   
112  N N   . CYS   A 16  ? 0.24235 0.17775 0.27716 0.03137  0.01216  0.06187  16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.28397 0.21547 0.30898 0.02442  0.01077  0.05985  16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.31485 0.25807 0.33264 0.02222  0.00345  0.06928  16  CYS   A C   
115  O O   . CYS   A 16  ? 0.35169 0.29412 0.36189 0.01689  0.00276  0.06901  16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.23740 0.16936 0.25055 0.01863  0.01125  0.04613  16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.25209 0.17364 0.26767 0.01952  0.01928  0.03269  16  CYS   A SG  
118  N N   . MET   A 17  ? 0.29710 0.25209 0.31662 0.02552  -0.00184 0.07715  17  MET   A N   
119  C CA  . MET   A 17  ? 0.31082 0.27725 0.31932 0.02198  -0.00872 0.08283  17  MET   A CA  
120  C C   . MET   A 17  ? 0.33438 0.30097 0.34750 0.02291  -0.01010 0.09743  17  MET   A C   
121  O O   . MET   A 17  ? 0.32793 0.29117 0.35597 0.02841  -0.00856 0.10653  17  MET   A O   
122  C CB  . MET   A 17  ? 0.29132 0.27096 0.29671 0.02264  -0.01485 0.08288  17  MET   A CB  
123  C CG  . MET   A 17  ? 0.25606 0.23638 0.25599 0.02109  -0.01393 0.07032  17  MET   A CG  
124  S SD  . MET   A 17  ? 0.31657 0.29291 0.30333 0.01538  -0.01209 0.06024  17  MET   A SD  
125  C CE  . MET   A 17  ? 0.32315 0.30837 0.29767 0.01167  -0.01750 0.06562  17  MET   A CE  
126  N N   . VAL   A 18  ? 0.38472 0.35534 0.38568 0.01774  -0.01224 0.10013  18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.39482 0.36601 0.39714 0.01706  -0.01298 0.11441  18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.39165 0.37598 0.37576 0.01177  -0.01801 0.11639  18  VAL   A C   
129  O O   . VAL   A 18  ? 0.35249 0.34097 0.32472 0.00862  -0.01875 0.10502  18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.38733 0.34366 0.39555 0.01506  -0.00583 0.11432  18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.34107 0.28195 0.36549 0.01952  0.00029  0.10943  18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.31610 0.27266 0.31223 0.00866  -0.00375 0.10295  18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.44364 0.43442 0.42564 0.01095  -0.02105 0.13129  19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.36080 0.36377 0.32371 0.00533  -0.02457 0.13417  19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.37141 0.36896 0.32991 0.00132  -0.01816 0.13533  19  GLN   A C   
136  O O   . GLN   A 19  ? 0.46361 0.45074 0.43504 0.00259  -0.01384 0.14276  19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.47539 0.49085 0.43742 0.00583  -0.03198 0.15119  19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.48410 0.51533 0.42342 -0.00040 -0.03793 0.15136  19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.57056 0.61468 0.51001 -0.00088 -0.04507 0.16610  19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.60147 0.65811 0.53262 -0.00366 -0.05247 0.16343  19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.66371 0.70379 0.61401 0.00123  -0.04207 0.17826  19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.41388 0.41800 0.35564 -0.00357 -0.01680 0.12773  20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.43659 0.43945 0.37402 -0.00789 -0.01046 0.12982  20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.47700 0.49424 0.39372 -0.01233 -0.01193 0.13398  20  VAL   A C   
145  O O   . VAL   A 20  ? 0.47203 0.49672 0.37504 -0.01347 -0.01476 0.12447  20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.38940 0.38600 0.32963 -0.00922 -0.00471 0.11485  20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.40734 0.40737 0.34240 -0.01422 0.00149  0.11675  20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.41526 0.39750 0.37356 -0.00660 -0.00257 0.11129  20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.55518 0.57584 0.46912 -0.01527 -0.00963 0.14809  21  THR   A N   
150  C CA  . THR   A 21  ? 0.58331 0.61893 0.47580 -0.01990 -0.01106 0.15429  21  THR   A CA  
151  C C   . THR   A 21  ? 0.60421 0.64190 0.49211 -0.02442 -0.00246 0.15885  21  THR   A C   
152  O O   . THR   A 21  ? 0.60290 0.63455 0.50337 -0.02495 0.00048  0.17185  21  THR   A O   
153  C CB  . THR   A 21  ? 0.58247 0.62490 0.47532 -0.01892 -0.01892 0.16918  21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.57827 0.62099 0.47742 -0.01501 -0.02659 0.16557  21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.57671 0.63344 0.44729 -0.02406 -0.02033 0.16949  21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.58716 0.63301 0.45839 -0.02765 0.00227  0.14820  22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.58788 0.64024 0.45196 -0.03227 0.01105  0.15283  22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.61558 0.68253 0.45301 -0.03586 0.01053  0.15184  22  CYS   A C   
159  O O   . CYS   A 22  ? 0.55685 0.62753 0.38053 -0.03579 0.00921  0.13802  22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.58851 0.63698 0.46084 -0.03205 0.01937  0.13863  22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.62216 0.67446 0.50157 -0.03722 0.03069  0.14717  22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.64932 0.72127 0.48200 -0.03839 0.01132  0.16266  23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.65608 0.73980 0.46448 -0.04176 0.01082  0.15914  23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.69105 0.77763 0.48959 -0.04110 0.00023  0.15292  23  GLY   A C   
165  O O   . GLY   A 23  ? 0.70372 0.78783 0.51417 -0.03853 -0.00894 0.16107  23  GLY   A O   
166  N N   . THR   A 24  ? 0.72481 0.81654 0.50279 -0.04351 0.00209  0.13776  24  THR   A N   
167  C CA  . THR   A 24  ? 0.71676 0.81166 0.48300 -0.04480 -0.00724 0.12953  24  THR   A CA  
168  C C   . THR   A 24  ? 0.72309 0.81034 0.49874 -0.04168 -0.01123 0.11946  24  THR   A C   
169  O O   . THR   A 24  ? 0.68939 0.77843 0.45732 -0.04326 -0.01884 0.11154  24  THR   A O   
170  C CB  . THR   A 24  ? 0.81526 0.91709 0.55409 -0.04957 -0.00240 0.11648  24  THR   A CB  
171  O OG1 . THR   A 24  ? 0.81386 0.92012 0.54076 -0.05273 -0.01263 0.11129  24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.80752 0.90445 0.54192 -0.04835 0.00795  0.09915  24  THR   A CG2 
173  N N   . THR   A 25  ? 0.68874 0.76802 0.48106 -0.03796 -0.00649 0.11991  25  THR   A N   
174  C CA  . THR   A 25  ? 0.60188 0.67196 0.40429 -0.03426 -0.00753 0.10635  25  THR   A CA  
175  C C   . THR   A 25  ? 0.56698 0.62843 0.39421 -0.02925 -0.01356 0.11435  25  THR   A C   
176  O O   . THR   A 25  ? 0.54235 0.59740 0.38610 -0.02685 -0.00941 0.12199  25  THR   A O   
177  C CB  . THR   A 25  ? 0.57512 0.63948 0.38304 -0.03199 0.00401  0.09404  25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.58184 0.65380 0.36728 -0.03565 0.01100  0.08515  25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.52456 0.57780 0.34764 -0.02705 0.00272  0.08061  25  THR   A CG2 
180  N N   . THR   A 26  ? 0.49566 0.55681 0.32588 -0.02808 -0.02270 0.11203  26  THR   A N   
181  C CA  . THR   A 26  ? 0.47549 0.52891 0.32901 -0.02268 -0.02719 0.11752  26  THR   A CA  
182  C C   . THR   A 26  ? 0.42571 0.47071 0.28753 -0.01957 -0.02736 0.10167  26  THR   A C   
183  O O   . THR   A 26  ? 0.46237 0.51057 0.31345 -0.02199 -0.03116 0.09191  26  THR   A O   
184  C CB  . THR   A 26  ? 0.50063 0.56317 0.35558 -0.02313 -0.03772 0.13209  26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.54156 0.60883 0.39505 -0.02445 -0.03651 0.14498  26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.40308 0.45737 0.28348 -0.01648 -0.04037 0.13614  26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.35499 0.38921 0.23557 -0.01492 -0.02347 0.09957  27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.33843 0.36516 0.22820 -0.01180 -0.02329 0.08694  27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.34181 0.35960 0.25228 -0.00714 -0.02245 0.09121  27  LEU   A C   
190  O O   . LEU   A 27  ? 0.35469 0.36998 0.27308 -0.00626 -0.02104 0.10253  27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.37525 0.39915 0.25950 -0.01244 -0.01618 0.07358  27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.44028 0.46302 0.32756 -0.01304 -0.00795 0.07608  27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.41509 0.42899 0.32130 -0.01042 -0.00534 0.07619  27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.43240 0.45878 0.30878 -0.01447 -0.00130 0.06579  27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.32483 0.33713 0.24365 -0.00439 -0.02271 0.08186  28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.37271 0.37675 0.30885 -0.00020 -0.02162 0.08329  28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.30820 0.30389 0.25066 -0.00044 -0.01480 0.07912  28  ASN   A C   
198  O O   . ASN   A 28  ? 0.30296 0.30006 0.23931 -0.00272 -0.01141 0.07204  28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.38658 0.38999 0.32742 0.00201  -0.02443 0.07527  28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.33252 0.34463 0.27091 0.00152  -0.03181 0.07995  28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.30142 0.31646 0.24857 0.00381  -0.03478 0.09079  28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.32986 0.34640 0.25724 -0.00179 -0.03487 0.07230  28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.32181 0.30888 0.27772 0.00185  -0.01266 0.08314  29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.36993 0.34834 0.33268 0.00053  -0.00726 0.07723  29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.30458 0.27457 0.27819 0.00373  -0.00628 0.07208  29  GLY   A C   
206  O O   . GLY   A 29  ? 0.35821 0.32802 0.33759 0.00794  -0.00849 0.07573  29  GLY   A O   
207  N N   . LEU   A 30  ? 0.30841 0.27270 0.28484 0.00135  -0.00274 0.06355  30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.34794 0.30362 0.33205 0.00300  -0.00049 0.05691  30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.33322 0.27634 0.32554 0.00037  0.00444  0.05768  30  LEU   A C   
210  O O   . LEU   A 30  ? 0.29841 0.24135 0.28939 -0.00518 0.00600  0.05679  30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.29943 0.25910 0.27886 0.00123  -0.00114 0.04574  30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.31915 0.27223 0.30288 0.00246  0.00118  0.03826  30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.27123 0.22838 0.25604 0.00774  -0.00068 0.03914  30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.25681 0.21231 0.23635 -0.00216 0.00127  0.02864  30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.34988 0.28228 0.35201 0.00423  0.00744  0.05877  31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.35895 0.27563 0.37111 0.00259  0.01294  0.06011  31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.38093 0.28671 0.39561 0.00133  0.01745  0.04667  31  TRP   A C   
218  O O   . TRP   A 31  ? 0.31183 0.21333 0.33151 0.00709  0.02003  0.04407  31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.34541 0.25721 0.36852 0.00886  0.01385  0.07342  31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.38332 0.27784 0.41872 0.00793  0.01963  0.07805  31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.46310 0.34796 0.49917 0.00020  0.02298  0.07397  31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.41101 0.29537 0.46205 0.01490  0.02292  0.08852  31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.51242 0.37964 0.56291 0.00142  0.02842  0.08069  31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.43025 0.29657 0.49057 0.01108  0.02874  0.09001  31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.42947 0.31896 0.48941 0.02396  0.02142  0.09759  31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 0.46160 0.31293 0.53986 0.01683  0.03374  0.10011  31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.48535 0.36246 0.56387 0.03015  0.02601  0.10837  31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 0.53053 0.38770 0.61815 0.02699  0.03245  0.10958  31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.37464 0.27689 0.38594 -0.00667 0.01863  0.03829  32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.36979 0.26263 0.38020 -0.01038 0.02227  0.02441  32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.45079 0.32737 0.46817 -0.01723 0.02679  0.02207  32  LEU   A C   
232  O O   . LEU   A 32  ? 0.41372 0.29392 0.43109 -0.02398 0.02489  0.02574  32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.37235 0.27842 0.37147 -0.01535 0.01795  0.01552  32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.39899 0.31843 0.39221 -0.00917 0.01422  0.01677  32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.34028 0.27272 0.32441 -0.01365 0.00984  0.01060  32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.35363 0.26651 0.35012 -0.00281 0.01837  0.01350  32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.45276 0.31114 0.47684 -0.01568 0.03349  0.01558  33  ASP   A N   
238  C CA  . ASP   A 33  ? 0.44057 0.27884 0.47409 -0.02122 0.03898  0.01410  33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.47539 0.31386 0.51785 -0.01983 0.03790  0.03167  33  ASP   A C   
240  O O   . ASP   A 33  ? 0.43537 0.27725 0.48322 -0.01058 0.03737  0.04405  33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.46680 0.30433 0.49312 -0.03420 0.03768  0.00108  33  ASP   A CB  
242  C CG  . ASP   A 33  ? 0.51100 0.35139 0.52548 -0.03609 0.03788  -0.01533 33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 0.48209 0.30749 0.49857 -0.03227 0.04495  -0.02360 33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.44878 0.30718 0.45232 -0.04082 0.03142  -0.01912 33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.47454 0.31180 0.51840 -0.02934 0.03713  0.03388  34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.48601 0.32338 0.53763 -0.02913 0.03711  0.05116  34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.47481 0.33516 0.51696 -0.03211 0.03121  0.05784  34  ASP   A C   
248  O O   . ASP   A 34  ? 0.46129 0.32351 0.50722 -0.03694 0.03179  0.06809  34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.49197 0.30856 0.55568 -0.03724 0.04262  0.05155  34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.54179 0.36253 0.60128 -0.05119 0.04077  0.04173  34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.50588 0.34325 0.55368 -0.05393 0.03586  0.03221  34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.52012 0.32760 0.58971 -0.05968 0.04414  0.04450  34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.46224 0.33964 0.49274 -0.02903 0.02641  0.05241  35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.41269 0.31081 0.43426 -0.03099 0.02195  0.05579  35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.38134 0.29151 0.39518 -0.02209 0.01821  0.06047  35  VAL   A C   
256  O O   . VAL   A 35  ? 0.39071 0.29892 0.40328 -0.01645 0.01740  0.05511  35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.39702 0.30416 0.41327 -0.03780 0.01950  0.04308  35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.36113 0.28920 0.37091 -0.03816 0.01619  0.04679  35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.36338 0.25935 0.38697 -0.04839 0.02211  0.03702  35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.38493 0.30814 0.39311 -0.02158 0.01623  0.06974  36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.35695 0.29211 0.35616 -0.01516 0.01216  0.07300  36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.33755 0.28812 0.32712 -0.01752 0.01026  0.06813  36  VAL   A C   
263  O O   . VAL   A 36  ? 0.37002 0.32749 0.35781 -0.02158 0.01213  0.07273  36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.32492 0.26179 0.32416 -0.01188 0.01143  0.08838  36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.33375 0.28414 0.32202 -0.00745 0.00636  0.08978  36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.36705 0.28917 0.37899 -0.00777 0.01346  0.09429  36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.34598 0.30196 0.33053 -0.01460 0.00732  0.05953  37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.31187 0.28091 0.28943 -0.01527 0.00591  0.05497  37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.31988 0.29669 0.28788 -0.01102 0.00357  0.05893  37  TYR   A C   
270  O O   . TYR   A 37  ? 0.36835 0.34289 0.33501 -0.00687 0.00061  0.06037  37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.26544 0.23565 0.24343 -0.01500 0.00390  0.04448  37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.27353 0.23675 0.25815 -0.02044 0.00532  0.03881  37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.25803 0.20730 0.24686 -0.02002 0.00703  0.03673  37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.25946 0.23061 0.24664 -0.02632 0.00510  0.03501  37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.31180 0.25330 0.30461 -0.02619 0.00865  0.02923  37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.23135 0.19725 0.22331 -0.03318 0.00529  0.02889  37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.28618 0.23641 0.27965 -0.03357 0.00715  0.02516  37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.27307 0.21676 0.26929 -0.04141 0.00769  0.01718  37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.26309 0.24949 0.22476 -0.01248 0.00520  0.06016  38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.31465 0.30794 0.26488 -0.00978 0.00333  0.06112  38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.34219 0.34472 0.28784 -0.01067 0.00674  0.05623  38  CYS   A C   
282  O O   . CYS   A 38  ? 0.32711 0.33272 0.27968 -0.01345 0.01040  0.05532  38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.33064 0.32448 0.27559 -0.01026 0.00279  0.07242  38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.30620 0.30605 0.24806 -0.01528 0.00892  0.08069  38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.31665 0.32378 0.25197 -0.00842 0.00587  0.05250  39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.27609 0.29076 0.20809 -0.00814 0.01083  0.04735  39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.36188 0.38305 0.28987 -0.01133 0.01682  0.05340  39  PRO   A C   
288  O O   . PRO   A 39  ? 0.37869 0.40025 0.29797 -0.01327 0.01627  0.06094  39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.32396 0.33860 0.24456 -0.00576 0.00863  0.04170  39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.27154 0.27983 0.19402 -0.00457 0.00136  0.04274  39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.31884 0.32424 0.24666 -0.00626 0.00057  0.05193  39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.35635 0.38433 0.29166 -0.01197 0.02261  0.05128  40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.38520 0.42077 0.31887 -0.01547 0.02937  0.05778  40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.41998 0.46085 0.33553 -0.01499 0.03332  0.05739  40  ARG   A C   
295  O O   . ARG   A 40  ? 0.38165 0.42843 0.29130 -0.01847 0.03806  0.06507  40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.37985 0.42415 0.32788 -0.01633 0.03480  0.05602  40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.36617 0.41793 0.31487 -0.01143 0.03970  0.04791  40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.34095 0.40399 0.30767 -0.01217 0.04424  0.04873  40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.39840 0.46811 0.36937 -0.00599 0.04925  0.04204  40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.41763 0.50072 0.40413 -0.00476 0.05540  0.04307  40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.40911 0.50139 0.40776 -0.01062 0.05678  0.05025  40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.39631 0.48371 0.38787 0.00230  0.06046  0.03728  40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.40867 0.44711 0.31403 -0.01162 0.03131  0.04866  41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.45084 0.49406 0.33640 -0.01275 0.03521  0.04683  41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.44672 0.48974 0.31885 -0.01661 0.02951  0.05633  41  HIS   A C   
306  O O   . HIS   A 41  ? 0.47764 0.52518 0.33031 -0.01871 0.03052  0.05469  41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.46551 0.50522 0.34356 -0.00932 0.03559  0.03381  41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.48081 0.51200 0.35633 -0.00883 0.02565  0.03115  41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.45702 0.48169 0.34355 -0.00504 0.02270  0.02440  41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.50635 0.53621 0.37057 -0.01182 0.01810  0.03527  41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.47115 0.49042 0.35341 -0.00593 0.01440  0.02406  41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.42857 0.45133 0.29817 -0.00990 0.01123  0.03053  41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.46552 0.50399 0.34735 -0.01772 0.02398  0.06631  42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.48372 0.52387 0.35630 -0.02070 0.01955  0.07844  42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.49720 0.54643 0.36214 -0.02485 0.02666  0.08778  42  VAL   A C   
316  O O   . VAL   A 42  ? 0.50704 0.56233 0.35666 -0.02793 0.02470  0.09643  42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.45313 0.48431 0.34122 -0.01953 0.01327  0.08652  42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.45634 0.48378 0.36104 -0.02105 0.01814  0.09101  42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.46402 0.49733 0.34502 -0.02094 0.00742  0.09958  42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.47859 0.53066 0.35419 -0.02554 0.03480  0.08719  43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.52581 0.58783 0.39578 -0.02983 0.04291  0.09640  43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.54177 0.61445 0.39198 -0.03019 0.05054  0.08897  43  ILE   A C   
323  O O   . ILE   A 43  ? 0.59634 0.67929 0.43875 -0.03383 0.05846  0.09610  43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.50142 0.56372 0.39263 -0.03137 0.04852  0.09903  43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.48697 0.55348 0.38632 -0.02799 0.05387  0.08573  43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.43631 0.48579 0.34502 -0.03156 0.04145  0.10332  43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.45681 0.52496 0.37920 -0.03016 0.05669  0.08782  43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.55731 0.62726 0.39895 -0.02682 0.04909  0.07469  44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.70135 0.77852 0.52322 -0.02712 0.05703  0.06501  44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.91773 1.00006 0.71294 -0.03214 0.05303  0.06963  44  CYS   A C   
331  O O   . CYS   A 44  ? 0.90385 0.98292 0.69679 -0.03382 0.04179  0.07748  44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.74382 0.81396 0.56713 -0.02210 0.05740  0.04764  44  CYS   A CB  
333  S SG  . CYS   A 44  ? 0.76482 0.83372 0.61570 -0.01586 0.06399  0.04105  44  CYS   A SG  
334  N N   . THR   A 45  ? 1.08249 1.17421 0.85753 -0.03457 0.06263  0.06468  45  THR   A N   
335  C CA  . THR   A 45  ? 1.19610 1.29488 0.94093 -0.04037 0.06002  0.06565  45  THR   A CA  
336  C C   . THR   A 45  ? 1.24994 1.34520 0.97806 -0.03957 0.06421  0.04470  45  THR   A C   
337  O O   . THR   A 45  ? 1.21408 1.30226 0.95556 -0.03371 0.07081  0.03166  45  THR   A O   
338  C CB  . THR   A 45  ? 1.24864 1.35800 0.98437 -0.04410 0.06776  0.07662  45  THR   A CB  
339  O OG1 . THR   A 45  ? 1.33193 1.44665 1.06136 -0.04254 0.08322  0.06493  45  THR   A OG1 
340  C CG2 . THR   A 45  ? 1.15340 1.26406 0.91165 -0.04435 0.06762  0.09463  45  THR   A CG2 
341  N N   . SER   A 46  ? 1.32228 1.41937 1.02528 -0.04455 0.05942  0.04116  46  SER   A N   
342  C CA  . SER   A 46  ? 1.35616 1.44682 1.04287 -0.04498 0.06164  0.02046  46  SER   A CA  
343  C C   . SER   A 46  ? 1.35433 1.44555 1.03771 -0.04134 0.07982  0.00645  46  SER   A C   
344  O O   . SER   A 46  ? 1.32925 1.41166 1.01021 -0.03888 0.08487  -0.01194 46  SER   A O   
345  C CB  . SER   A 46  ? 1.35781 1.45011 1.02222 -0.05082 0.05250  0.02036  46  SER   A CB  
346  O OG  . SER   A 46  ? 1.25249 1.34605 0.92408 -0.05309 0.03646  0.03437  46  SER   A OG  
347  N N   . GLU   A 47  ? 1.36420 1.46492 1.04962 -0.04059 0.09031  0.01504  47  GLU   A N   
348  C CA  . GLU   A 47  ? 1.35434 1.45798 1.04023 -0.03620 0.10871  0.00422  47  GLU   A CA  
349  C C   . GLU   A 47  ? 1.36717 1.47569 1.08200 -0.03055 0.11726  0.00713  47  GLU   A C   
350  O O   . GLU   A 47  ? 1.31172 1.42256 1.03390 -0.02508 0.13239  -0.00261 47  GLU   A O   
351  C CB  . GLU   A 47  ? 1.36910 1.48201 1.04058 -0.03900 0.11606  0.01203  47  GLU   A CB  
352  C CG  . GLU   A 47  ? 1.36425 1.48563 1.04730 -0.04216 0.11140  0.03514  47  GLU   A CG  
353  C CD  . GLU   A 47  ? 1.38983 1.51034 1.06167 -0.04785 0.09484  0.04722  47  GLU   A CD  
354  O OE1 . GLU   A 47  ? 1.34601 1.46070 1.00377 -0.04973 0.08522  0.03838  47  GLU   A OE1 
355  O OE2 . GLU   A 47  ? 1.42544 1.55131 1.10486 -0.05039 0.09146  0.06589  47  GLU   A OE2 
356  N N   . ASP   A 48  ? 1.46576 1.57082 1.20383 -0.02949 0.10584  0.02039  48  ASP   A N   
357  C CA  . ASP   A 48  ? 1.42220 1.52597 1.19421 -0.02319 0.10849  0.02388  48  ASP   A CA  
358  C C   . ASP   A 48  ? 1.34200 1.43166 1.13117 -0.01668 0.10290  0.01255  48  ASP   A C   
359  O O   . ASP   A 48  ? 1.34135 1.42923 1.15755 -0.01281 0.09997  0.01741  48  ASP   A O   
360  C CB  . ASP   A 48  ? 1.33697 1.44327 1.12428 -0.02641 0.09971  0.04320  48  ASP   A CB  
361  C CG  . ASP   A 48  ? 1.39116 1.51228 1.17721 -0.03066 0.10907  0.05660  48  ASP   A CG  
362  O OD1 . ASP   A 48  ? 1.38660 1.51091 1.16378 -0.03669 0.10276  0.07170  48  ASP   A OD1 
363  O OD2 . ASP   A 48  ? 1.32744 1.45756 1.12321 -0.02782 0.12287  0.05318  48  ASP   A OD2 
364  N N   . MET   A 49  ? 1.24402 1.32393 1.01833 -0.01601 0.10150  -0.00225 49  MET   A N   
365  C CA  . MET   A 49  ? 1.15483 1.22067 0.94467 -0.01106 0.09411  -0.01020 49  MET   A CA  
366  C C   . MET   A 49  ? 1.14953 1.21040 0.95190 -0.00294 0.10591  -0.02409 49  MET   A C   
367  O O   . MET   A 49  ? 1.05822 1.10905 0.87880 0.00224  0.10115  -0.02807 49  MET   A O   
368  C CB  . MET   A 49  ? 1.15357 1.21033 0.92286 -0.01623 0.08274  -0.01610 49  MET   A CB  
369  C CG  . MET   A 49  ? 1.19057 1.25051 0.95540 -0.02202 0.06871  -0.00149 49  MET   A CG  
370  S SD  . MET   A 49  ? 1.21874 1.27301 0.96054 -0.02898 0.05518  -0.00683 49  MET   A SD  
371  C CE  . MET   A 49  ? 0.96539 1.00296 0.72525 -0.02382 0.04986  -0.01863 49  MET   A CE  
372  N N   . LEU   A 50  ? 1.28076 1.34856 1.07418 -0.00137 0.12172  -0.03111 50  LEU   A N   
373  C CA  . LEU   A 50  ? 1.30066 1.36237 1.10614 0.00728  0.13401  -0.04501 50  LEU   A CA  
374  C C   . LEU   A 50  ? 1.20013 1.26862 1.04169 0.01510  0.13709  -0.03691 50  LEU   A C   
375  O O   . LEU   A 50  ? 1.12696 1.18626 0.98825 0.02165  0.13433  -0.04098 50  LEU   A O   
376  C CB  . LEU   A 50  ? 1.29568 1.36230 1.08008 0.00706  0.15154  -0.05660 50  LEU   A CB  
377  C CG  . LEU   A 50  ? 1.39090 1.45726 1.13639 -0.00347 0.14726  -0.06047 50  LEU   A CG  
378  C CD1 . LEU   A 50  ? 1.45327 1.52744 1.17460 -0.00501 0.16515  -0.07062 50  LEU   A CD1 
379  C CD2 . LEU   A 50  ? 1.37729 1.42573 1.11076 -0.00677 0.13536  -0.07183 50  LEU   A CD2 
380  N N   . ASN   A 51  ? 1.04426 1.12944 0.89586 0.01378  0.14161  -0.02427 51  ASN   A N   
381  C CA  . ASN   A 51  ? 0.90853 1.00213 0.79463 0.01928  0.14215  -0.01569 51  ASN   A CA  
382  C C   . ASN   A 51  ? 0.83455 0.93917 0.72736 0.01236  0.13484  0.00139  51  ASN   A C   
383  O O   . ASN   A 51  ? 0.75247 0.87279 0.65978 0.01229  0.14306  0.00937  51  ASN   A O   
384  C CB  . ASN   A 51  ? 0.88643 0.99152 0.78673 0.02678  0.16077  -0.02005 51  ASN   A CB  
385  C CG  . ASN   A 51  ? 0.86162 0.97057 0.79831 0.03507  0.16008  -0.01645 51  ASN   A CG  
386  O OD1 . ASN   A 51  ? 0.89485 0.99367 0.84042 0.03605  0.14741  -0.01549 51  ASN   A OD1 
387  N ND2 . ASN   A 51  ? 0.96028 1.08713 0.91839 0.03879  0.17083  -0.01044 51  ASN   A ND2 
388  N N   . PRO   A 52  ? 0.84870 0.94513 0.73456 0.00669  0.11968  0.00753  52  PRO   A N   
389  C CA  . PRO   A 52  ? 0.72837 0.83231 0.61624 -0.00054 0.11439  0.02278  52  PRO   A CA  
390  C C   . PRO   A 52  ? 0.63028 0.74462 0.54866 0.00043  0.11535  0.03137  52  PRO   A C   
391  O O   . PRO   A 52  ? 0.62916 0.74142 0.56773 0.00549  0.11179  0.02837  52  PRO   A O   
392  C CB  . PRO   A 52  ? 0.72156 0.81212 0.60097 -0.00420 0.09827  0.02539  52  PRO   A CB  
393  C CG  . PRO   A 52  ? 0.73732 0.81589 0.62108 0.00145  0.09362  0.01408  52  PRO   A CG  
394  C CD  . PRO   A 52  ? 0.81166 0.89172 0.69278 0.00735  0.10712  0.00166  52  PRO   A CD  
395  N N   . ASN   A 53  ? 0.58391 0.71049 0.50541 -0.00520 0.12001  0.04271  53  ASN   A N   
396  C CA  . ASN   A 53  ? 0.61702 0.75396 0.56606 -0.00750 0.11918  0.05236  53  ASN   A CA  
397  C C   . ASN   A 53  ? 0.65968 0.78866 0.60704 -0.01541 0.10712  0.06265  53  ASN   A C   
398  O O   . ASN   A 53  ? 0.66470 0.79741 0.60340 -0.02186 0.10950  0.07259  53  ASN   A O   
399  C CB  . ASN   A 53  ? 0.67953 0.83609 0.63684 -0.00873 0.13403  0.05806  53  ASN   A CB  
400  C CG  . ASN   A 53  ? 0.67096 0.84068 0.66091 -0.01049 0.13347  0.06592  53  ASN   A CG  
401  O OD1 . ASN   A 53  ? 0.66968 0.83573 0.66924 -0.01719 0.12299  0.07368  53  ASN   A OD1 
402  N ND2 . ASN   A 53  ? 0.60700 0.79245 0.61471 -0.00465 0.14499  0.06361  53  ASN   A ND2 
403  N N   . TYR   A 54  ? 0.64574 0.76343 0.60165 -0.01467 0.09487  0.06056  54  TYR   A N   
404  C CA  . TYR   A 54  ? 0.60341 0.71039 0.55664 -0.02077 0.08420  0.06811  54  TYR   A CA  
405  C C   . TYR   A 54  ? 0.56354 0.67754 0.53278 -0.02835 0.08539  0.07963  54  TYR   A C   
406  O O   . TYR   A 54  ? 0.54410 0.65018 0.50893 -0.03407 0.08071  0.08817  54  TYR   A O   
407  C CB  . TYR   A 54  ? 0.52766 0.62216 0.48681 -0.01805 0.07263  0.06219  54  TYR   A CB  
408  C CG  . TYR   A 54  ? 0.51210 0.59708 0.45449 -0.01256 0.06981  0.05268  54  TYR   A CG  
409  C CD1 . TYR   A 54  ? 0.44611 0.52156 0.36955 -0.01458 0.06412  0.05442  54  TYR   A CD1 
410  C CD2 . TYR   A 54  ? 0.50465 0.59056 0.45165 -0.00562 0.07280  0.04268  54  TYR   A CD2 
411  C CE1 . TYR   A 54  ? 0.44618 0.51404 0.35513 -0.01105 0.06091  0.04568  54  TYR   A CE1 
412  C CE2 . TYR   A 54  ? 0.53028 0.60610 0.46272 -0.00177 0.07041  0.03365  54  TYR   A CE2 
413  C CZ  . TYR   A 54  ? 0.46759 0.53481 0.38067 -0.00511 0.06423  0.03479  54  TYR   A CZ  
414  O OH  . TYR   A 54  ? 0.48769 0.54592 0.38714 -0.00270 0.06115  0.02577  54  TYR   A OH  
415  N N   . GLU   A 55  ? 0.62466 0.75321 0.61438 -0.02866 0.09128  0.08051  55  GLU   A N   
416  C CA  . GLU   A 55  ? 0.65661 0.79215 0.66275 -0.03744 0.09203  0.09118  55  GLU   A CA  
417  C C   . GLU   A 55  ? 0.65105 0.79121 0.64531 -0.04232 0.10015  0.10144  55  GLU   A C   
418  O O   . GLU   A 55  ? 0.55989 0.69301 0.55518 -0.04979 0.09649  0.11139  55  GLU   A O   
419  C CB  . GLU   A 55  ? 0.70131 0.85540 0.73331 -0.03761 0.09661  0.09135  55  GLU   A CB  
420  C CG  . GLU   A 55  ? 0.67035 0.82242 0.71803 -0.03647 0.08658  0.08585  55  GLU   A CG  
421  C CD  . GLU   A 55  ? 0.81242 0.96433 0.85789 -0.02543 0.08669  0.07565  55  GLU   A CD  
422  O OE1 . GLU   A 55  ? 0.74609 0.89020 0.77192 -0.01917 0.09066  0.06986  55  GLU   A OE1 
423  O OE2 . GLU   A 55  ? 0.95405 1.11240 1.01717 -0.02370 0.08150  0.07351  55  GLU   A OE2 
424  N N   . ASP   A 56  ? 0.80708 0.95929 0.79023 -0.03842 0.11217  0.09965  56  ASP   A N   
425  C CA  . ASP   A 56  ? 0.81035 0.96809 0.77838 -0.04362 0.11988  0.11034  56  ASP   A CA  
426  C C   . ASP   A 56  ? 0.80545 0.94783 0.74942 -0.04466 0.11199  0.11312  56  ASP   A C   
427  O O   . ASP   A 56  ? 0.79540 0.93603 0.73475 -0.05128 0.11135  0.12660  56  ASP   A O   
428  C CB  . ASP   A 56  ? 0.82684 1.00002 0.78055 -0.04048 0.13532  0.10817  56  ASP   A CB  
429  C CG  . ASP   A 56  ? 0.87672 1.06951 0.85138 -0.03923 0.14722  0.10845  56  ASP   A CG  
430  O OD1 . ASP   A 56  ? 0.86257 1.05821 0.86205 -0.04232 0.14248  0.11213  56  ASP   A OD1 
431  O OD2 . ASP   A 56  ? 0.99245 1.20010 0.96005 -0.03761 0.16192  0.10848  56  ASP   A OD2 
432  N N   . LEU   A 57  ? 0.61814 0.74921 0.54947 -0.03846 0.10500  0.10177  57  LEU   A N   
433  C CA  . LEU   A 57  ? 0.57954 0.69817 0.49045 -0.03959 0.09638  0.10529  57  LEU   A CA  
434  C C   . LEU   A 57  ? 0.55370 0.66041 0.47662 -0.04461 0.08690  0.11622  57  LEU   A C   
435  O O   . LEU   A 57  ? 0.58106 0.68240 0.49271 -0.04767 0.08307  0.12696  57  LEU   A O   
436  C CB  . LEU   A 57  ? 0.61190 0.72056 0.51061 -0.03296 0.08968  0.09123  57  LEU   A CB  
437  C CG  . LEU   A 57  ? 0.66297 0.77835 0.54255 -0.02886 0.09838  0.08003  57  LEU   A CG  
438  C CD1 . LEU   A 57  ? 0.69993 0.80286 0.57123 -0.02385 0.09020  0.06725  57  LEU   A CD1 
439  C CD2 . LEU   A 57  ? 0.67261 0.79621 0.52739 -0.03372 0.10401  0.08770  57  LEU   A CD2 
440  N N   . LEU   A 58  ? 0.55325 0.65608 0.49926 -0.04572 0.08341  0.11397  58  LEU   A N   
441  C CA  . LEU   A 58  ? 0.50746 0.59580 0.46484 -0.04988 0.07485  0.12022  58  LEU   A CA  
442  C C   . LEU   A 58  ? 0.53820 0.62941 0.50895 -0.05863 0.07931  0.13398  58  LEU   A C   
443  O O   . LEU   A 58  ? 0.50477 0.58300 0.47810 -0.06240 0.07476  0.14340  58  LEU   A O   
444  C CB  . LEU   A 58  ? 0.43054 0.51204 0.40319 -0.04772 0.06800  0.10923  58  LEU   A CB  
445  C CG  . LEU   A 58  ? 0.42787 0.49134 0.40774 -0.05049 0.05917  0.11165  58  LEU   A CG  
446  C CD1 . LEU   A 58  ? 0.46991 0.52333 0.43307 -0.04708 0.05468  0.11597  58  LEU   A CD1 
447  C CD2 . LEU   A 58  ? 0.46082 0.51856 0.45086 -0.04830 0.05244  0.09971  58  LEU   A CD2 
448  N N   . ILE   A 59  ? 0.49629 0.60404 0.47758 -0.06192 0.08851  0.13588  59  ILE   A N   
449  C CA  . ILE   A 59  ? 0.54178 0.65431 0.53493 -0.07123 0.09401  0.15040  59  ILE   A CA  
450  C C   . ILE   A 59  ? 0.48626 0.59753 0.46174 -0.07332 0.09693  0.16479  59  ILE   A C   
451  O O   . ILE   A 59  ? 0.50565 0.61181 0.48972 -0.08074 0.09766  0.17919  59  ILE   A O   
452  C CB  . ILE   A 59  ? 0.50369 0.63845 0.51066 -0.07354 0.10457  0.15016  59  ILE   A CB  
453  C CG1 . ILE   A 59  ? 0.49629 0.63579 0.52086 -0.08468 0.10905  0.16440  59  ILE   A CG1 
454  C CG2 . ILE   A 59  ? 0.54851 0.69876 0.53724 -0.06847 0.11533  0.14915  59  ILE   A CG2 
455  C CD1 . ILE   A 59  ? 0.55646 0.68201 0.60122 -0.09151 0.10023  0.16353  59  ILE   A CD1 
456  N N   . ARG   A 60  ? 0.51655 0.63229 0.46718 -0.06744 0.09824  0.16158  60  ARG   A N   
457  C CA  . ARG   A 60  ? 0.50307 0.62000 0.43328 -0.06882 0.09971  0.17300  60  ARG   A CA  
458  C C   . ARG   A 60  ? 0.52940 0.62895 0.45326 -0.06744 0.08829  0.17913  60  ARG   A C   
459  O O   . ARG   A 60  ? 0.51569 0.61298 0.42714 -0.06806 0.08646  0.18798  60  ARG   A O   
460  C CB  . ARG   A 60  ? 0.46915 0.59824 0.37446 -0.06393 0.10561  0.16382  60  ARG   A CB  
461  C CG  . ARG   A 60  ? 0.48328 0.62942 0.39448 -0.06410 0.11865  0.15871  60  ARG   A CG  
462  C CD  . ARG   A 60  ? 0.53247 0.68749 0.42404 -0.05773 0.12519  0.14454  60  ARG   A CD  
463  N NE  . ARG   A 60  ? 0.60378 0.77470 0.50232 -0.05766 0.13932  0.14157  60  ARG   A NE  
464  C CZ  . ARG   A 60  ? 0.64399 0.82444 0.53745 -0.05147 0.14882  0.12800  60  ARG   A CZ  
465  N NH1 . ARG   A 60  ? 0.63482 0.81002 0.51510 -0.04522 0.14549  0.11535  60  ARG   A NH1 
466  N NH2 . ARG   A 60  ? 0.56713 0.76182 0.47013 -0.05136 0.16207  0.12694  60  ARG   A NH2 
467  N N   . LYS   A 61  ? 0.52744 0.61366 0.46067 -0.06438 0.07986  0.17207  61  LYS   A N   
468  C CA  . LYS   A 61  ? 0.50936 0.57941 0.44087 -0.06218 0.06986  0.17763  61  LYS   A CA  
469  C C   . LYS   A 61  ? 0.54192 0.59787 0.49503 -0.06757 0.06869  0.18917  61  LYS   A C   
470  O O   . LYS   A 61  ? 0.55019 0.60403 0.52215 -0.07210 0.07160  0.18508  61  LYS   A O   
471  C CB  . LYS   A 61  ? 0.47232 0.53295 0.40411 -0.05529 0.06172  0.16101  61  LYS   A CB  
472  C CG  . LYS   A 61  ? 0.51763 0.58794 0.42889 -0.05010 0.06184  0.14928  61  LYS   A CG  
473  C CD  . LYS   A 61  ? 0.59944 0.67322 0.48855 -0.04964 0.05819  0.15830  61  LYS   A CD  
474  C CE  . LYS   A 61  ? 0.51043 0.59186 0.37774 -0.04593 0.05777  0.14503  61  LYS   A CE  
475  N NZ  . LYS   A 61  ? 0.51520 0.60277 0.35991 -0.04770 0.05398  0.15459  61  LYS   A NZ  
476  N N   . SER   A 62  ? 0.70747 0.75208 0.65884 -0.06619 0.06337  0.19973  62  SER   A N   
477  C CA  . SER   A 62  ? 0.71950 0.74437 0.69151 -0.06856 0.06064  0.20656  62  SER   A CA  
478  C C   . SER   A 62  ? 0.73386 0.74417 0.70748 -0.06202 0.05209  0.20424  62  SER   A C   
479  O O   . SER   A 62  ? 0.70112 0.71783 0.65874 -0.05616 0.04724  0.20051  62  SER   A O   
480  C CB  . SER   A 62  ? 0.73116 0.75354 0.70514 -0.07158 0.06272  0.22097  62  SER   A CB  
481  O OG  . SER   A 62  ? 0.76826 0.79781 0.72337 -0.06704 0.05900  0.22756  62  SER   A OG  
482  N N   . ASN   A 63  ? 0.68518 0.67547 0.67903 -0.06342 0.05072  0.20504  63  ASN   A N   
483  C CA  . ASN   A 63  ? 0.58862 0.56410 0.58730 -0.05677 0.04414  0.19850  63  ASN   A CA  
484  C C   . ASN   A 63  ? 0.62910 0.60712 0.61653 -0.04932 0.03810  0.20687  63  ASN   A C   
485  O O   . ASN   A 63  ? 0.63840 0.61787 0.61895 -0.04336 0.03264  0.20031  63  ASN   A O   
486  C CB  . ASN   A 63  ? 0.55591 0.50766 0.57736 -0.05958 0.04523  0.19886  63  ASN   A CB  
487  C CG  . ASN   A 63  ? 0.58521 0.53407 0.61705 -0.06657 0.04805  0.18384  63  ASN   A CG  
488  O OD1 . ASN   A 63  ? 0.62393 0.58829 0.64790 -0.06729 0.04830  0.17241  63  ASN   A OD1 
489  N ND2 . ASN   A 63  ? 0.54763 0.47646 0.59795 -0.07190 0.05001  0.18372  63  ASN   A ND2 
490  N N   . HIS   A 64  ? 0.62794 0.60776 0.61377 -0.04955 0.03819  0.21955  64  HIS   A N   
491  C CA  . HIS   A 64  ? 0.63435 0.61804 0.61228 -0.04293 0.03125  0.22689  64  HIS   A CA  
492  C C   . HIS   A 64  ? 0.64257 0.64605 0.59609 -0.04123 0.02762  0.22190  64  HIS   A C   
493  O O   . HIS   A 64  ? 0.60723 0.61582 0.55377 -0.03656 0.02055  0.22586  64  HIS   A O   
494  C CB  . HIS   A 64  ? 0.56690 0.54974 0.54921 -0.04422 0.03206  0.24283  64  HIS   A CB  
495  C CG  . HIS   A 64  ? 0.64027 0.63536 0.61326 -0.05141 0.03837  0.24762  64  HIS   A CG  
496  N ND1 . HIS   A 64  ? 0.64134 0.65610 0.59215 -0.05215 0.03768  0.25086  64  HIS   A ND1 
497  C CD2 . HIS   A 64  ? 0.65242 0.64306 0.63577 -0.05851 0.04583  0.24952  64  HIS   A CD2 
498  C CE1 . HIS   A 64  ? 0.65902 0.68102 0.60680 -0.05862 0.04522  0.25473  64  HIS   A CE1 
499  N NE2 . HIS   A 64  ? 0.64157 0.64994 0.60965 -0.06262 0.05002  0.25448  64  HIS   A NE2 
500  N N   . ASN   A 65  ? 0.60322 0.61809 0.54472 -0.04506 0.03240  0.21269  65  ASN   A N   
501  C CA  . ASN   A 65  ? 0.61495 0.64475 0.53409 -0.04310 0.02944  0.20413  65  ASN   A CA  
502  C C   . ASN   A 65  ? 0.58783 0.61237 0.50846 -0.03778 0.02297  0.19482  65  ASN   A C   
503  O O   . ASN   A 65  ? 0.58701 0.62163 0.49043 -0.03585 0.01854  0.18824  65  ASN   A O   
504  C CB  . ASN   A 65  ? 0.58514 0.62778 0.49315 -0.04747 0.03774  0.19564  65  ASN   A CB  
505  C CG  . ASN   A 65  ? 0.64022 0.69120 0.54379 -0.05251 0.04461  0.20420  65  ASN   A CG  
506  O OD1 . ASN   A 65  ? 0.60909 0.66261 0.52098 -0.05703 0.05287  0.20323  65  ASN   A OD1 
507  N ND2 . ASN   A 65  ? 0.63920 0.69588 0.53043 -0.05215 0.04111  0.21313  65  ASN   A ND2 
508  N N   . PHE   A 66  ? 0.56854 0.57694 0.50907 -0.03579 0.02246  0.19350  66  PHE   A N   
509  C CA  . PHE   A 66  ? 0.60669 0.60842 0.55095 -0.02987 0.01694  0.17905  66  PHE   A CA  
510  C C   . PHE   A 66  ? 0.57341 0.56638 0.52860 -0.02442 0.01100  0.19005  66  PHE   A C   
511  O O   . PHE   A 66  ? 0.57093 0.54802 0.54545 -0.02335 0.01320  0.19600  66  PHE   A O   
512  C CB  . PHE   A 66  ? 0.53612 0.52699 0.49369 -0.03069 0.02055  0.16333  66  PHE   A CB  
513  C CG  . PHE   A 66  ? 0.52657 0.52828 0.47629 -0.03443 0.02550  0.15229  66  PHE   A CG  
514  C CD1 . PHE   A 66  ? 0.52949 0.54128 0.46492 -0.03172 0.02366  0.14006  66  PHE   A CD1 
515  C CD2 . PHE   A 66  ? 0.51340 0.51547 0.47179 -0.04066 0.03237  0.15479  66  PHE   A CD2 
516  C CE1 . PHE   A 66  ? 0.51945 0.54094 0.45026 -0.03382 0.02921  0.13044  66  PHE   A CE1 
517  C CE2 . PHE   A 66  ? 0.50693 0.52120 0.46104 -0.04328 0.03742  0.14570  66  PHE   A CE2 
518  C CZ  . PHE   A 66  ? 0.50743 0.53119 0.44815 -0.03918 0.03616  0.13364  66  PHE   A CZ  
519  N N   . LEU   A 67  ? 0.57278 0.57600 0.51678 -0.02094 0.00370  0.19106  67  LEU   A N   
520  C CA  . LEU   A 67  ? 0.55118 0.55024 0.50668 -0.01467 -0.00256 0.19714  67  LEU   A CA  
521  C C   . LEU   A 67  ? 0.53843 0.53059 0.50122 -0.00988 -0.00499 0.18625  67  LEU   A C   
522  O O   . LEU   A 67  ? 0.49900 0.49983 0.44851 -0.01024 -0.00792 0.17307  67  LEU   A O   
523  C CB  . LEU   A 67  ? 0.56137 0.57781 0.50167 -0.01482 -0.00966 0.20201  67  LEU   A CB  
524  C CG  . LEU   A 67  ? 0.58721 0.61222 0.52013 -0.01864 -0.00874 0.21403  67  LEU   A CG  
525  C CD1 . LEU   A 67  ? 0.59374 0.62635 0.50831 -0.02544 -0.00219 0.20928  67  LEU   A CD1 
526  C CD2 . LEU   A 67  ? 0.47192 0.51172 0.39632 -0.01770 -0.01752 0.22024  67  LEU   A CD2 
527  N N   . VAL   A 68  ? 0.56637 0.54204 0.55048 -0.00523 -0.00296 0.18673  68  VAL   A N   
528  C CA  . VAL   A 68  ? 0.53910 0.50725 0.53136 -0.00037 -0.00372 0.17178  68  VAL   A CA  
529  C C   . VAL   A 68  ? 0.62246 0.58742 0.63078 0.00739  -0.00721 0.18274  68  VAL   A C   
530  O O   . VAL   A 68  ? 0.66539 0.61759 0.69102 0.01017  -0.00337 0.19143  68  VAL   A O   
531  C CB  . VAL   A 68  ? 0.54417 0.49555 0.54645 -0.00232 0.00346  0.15840  68  VAL   A CB  
532  C CG1 . VAL   A 68  ? 0.49140 0.43669 0.49945 0.00223  0.00295  0.14350  68  VAL   A CG1 
533  C CG2 . VAL   A 68  ? 0.44898 0.40617 0.43907 -0.00968 0.00675  0.14988  68  VAL   A CG2 
534  N N   . GLN   A 69  ? 0.53676 0.51348 0.54084 0.01080  -0.01400 0.18018  69  GLN   A N   
535  C CA  . GLN   A 69  ? 0.58514 0.56112 0.60685 0.01864  -0.01663 0.18577  69  GLN   A CA  
536  C C   . GLN   A 69  ? 0.55183 0.51690 0.58327 0.02289  -0.01280 0.17096  69  GLN   A C   
537  O O   . GLN   A 69  ? 0.50271 0.47265 0.52195 0.02017  -0.01409 0.15558  69  GLN   A O   
538  C CB  . GLN   A 69  ? 0.61596 0.61301 0.62980 0.01885  -0.02619 0.18907  69  GLN   A CB  
539  C CG  . GLN   A 69  ? 0.72257 0.73583 0.72236 0.01383  -0.03174 0.19783  69  GLN   A CG  
540  C CD  . GLN   A 69  ? 0.73017 0.74015 0.74000 0.01464  -0.02929 0.21171  69  GLN   A CD  
541  O OE1 . GLN   A 69  ? 0.82367 0.82862 0.85480 0.02093  -0.02827 0.21938  69  GLN   A OE1 
542  N NE2 . GLN   A 69  ? 0.75445 0.76855 0.74903 0.00830  -0.02811 0.21544  69  GLN   A NE2 
543  N N   . ALA   A 70  ? 0.62922 0.58014 0.68230 0.02960  -0.00763 0.17415  70  ALA   A N   
544  C CA  . ALA   A 70  ? 0.59798 0.54320 0.66133 0.03517  -0.00456 0.16199  70  ALA   A CA  
545  C C   . ALA   A 70  ? 0.63856 0.59304 0.71864 0.04330  -0.00832 0.17590  70  ALA   A C   
546  O O   . ALA   A 70  ? 0.60596 0.55146 0.70446 0.04855  -0.00340 0.18139  70  ALA   A O   
547  C CB  . ALA   A 70  ? 0.54798 0.46999 0.62174 0.03594  0.00577  0.15086  70  ALA   A CB  
548  N N   . GLY   A 71  ? 0.58884 0.56363 0.66083 0.04245  -0.01698 0.17673  71  GLY   A N   
549  C CA  . GLY   A 71  ? 0.67315 0.66306 0.75765 0.04669  -0.02199 0.18614  71  GLY   A CA  
550  C C   . GLY   A 71  ? 0.72995 0.72880 0.81134 0.04351  -0.02639 0.19957  71  GLY   A C   
551  O O   . GLY   A 71  ? 0.72767 0.73239 0.78894 0.03607  -0.03023 0.20042  71  GLY   A O   
552  N N   . ASN   A 72  ? 0.73848 0.73942 0.84026 0.04936  -0.02539 0.21051  72  ASN   A N   
553  C CA  . ASN   A 72  ? 0.79779 0.80517 0.90097 0.04762  -0.02824 0.22514  72  ASN   A CA  
554  C C   . ASN   A 72  ? 0.81677 0.80316 0.92613 0.04818  -0.01964 0.22751  72  ASN   A C   
555  O O   . ASN   A 72  ? 0.79423 0.78280 0.91033 0.04837  -0.02016 0.24087  72  ASN   A O   
556  C CB  . ASN   A 72  ? 0.85067 0.87147 0.97498 0.05358  -0.03141 0.23758  72  ASN   A CB  
557  C CG  . ASN   A 72  ? 0.88683 0.93299 1.00236 0.04955  -0.04250 0.23978  72  ASN   A CG  
558  O OD1 . ASN   A 72  ? 0.81075 0.86246 0.90606 0.04350  -0.04698 0.22948  72  ASN   A OD1 
559  N ND2 . ASN   A 72  ? 0.93759 0.99923 1.06912 0.05249  -0.04694 0.25334  72  ASN   A ND2 
560  N N   . VAL   A 73  ? 0.79178 0.75806 0.89992 0.04798  -0.01183 0.21511  73  VAL   A N   
561  C CA  . VAL   A 73  ? 0.77962 0.72389 0.89376 0.04692  -0.00327 0.21474  73  VAL   A CA  
562  C C   . VAL   A 73  ? 0.76094 0.70467 0.85278 0.03738  -0.00417 0.21119  73  VAL   A C   
563  O O   . VAL   A 73  ? 0.76580 0.71623 0.84094 0.03350  -0.00718 0.20209  73  VAL   A O   
564  C CB  . VAL   A 73  ? 0.72269 0.64430 0.85173 0.05217  0.00681  0.20225  73  VAL   A CB  
565  C CG1 . VAL   A 73  ? 0.69443 0.59249 0.82626 0.04831  0.01507  0.19855  73  VAL   A CG1 
566  C CG2 . VAL   A 73  ? 0.74946 0.67161 0.90257 0.06205  0.00966  0.20724  73  VAL   A CG2 
567  N N   . GLN   A 74  ? 0.80965 0.74626 0.90211 0.03360  -0.00117 0.21884  74  GLN   A N   
568  C CA  . GLN   A 74  ? 0.81982 0.76107 0.89220 0.02442  -0.00212 0.21924  74  GLN   A CA  
569  C C   . GLN   A 74  ? 0.80230 0.72107 0.87885 0.02039  0.00682  0.21078  74  GLN   A C   
570  O O   . GLN   A 74  ? 0.84570 0.74902 0.93674 0.02077  0.01243  0.21530  74  GLN   A O   
571  C CB  . GLN   A 74  ? 0.87053 0.82350 0.94006 0.02210  -0.00560 0.23539  74  GLN   A CB  
572  C CG  . GLN   A 74  ? 0.95049 0.92782 1.01412 0.02386  -0.01537 0.24402  74  GLN   A CG  
573  C CD  . GLN   A 74  ? 1.01384 0.99181 1.10201 0.03258  -0.01635 0.25370  74  GLN   A CD  
574  O OE1 . GLN   A 74  ? 0.97002 0.93048 1.07814 0.03880  -0.00964 0.24968  74  GLN   A OE1 
575  N NE2 . GLN   A 74  ? 0.98923 0.98771 1.07614 0.03271  -0.02419 0.26634  74  GLN   A NE2 
576  N N   . LEU   A 75  ? 0.70256 0.61960 0.76733 0.01597  0.00803  0.19848  75  LEU   A N   
577  C CA  . LEU   A 75  ? 0.69129 0.58925 0.75990 0.01033  0.01579  0.18976  75  LEU   A CA  
578  C C   . LEU   A 75  ? 0.69753 0.59961 0.75690 0.00133  0.01727  0.19596  75  LEU   A C   
579  O O   . LEU   A 75  ? 0.72752 0.64905 0.77083 -0.00136 0.01262  0.20276  75  LEU   A O   
580  C CB  . LEU   A 75  ? 0.63885 0.53764 0.69779 0.00834  0.01602  0.16976  75  LEU   A CB  
581  C CG  . LEU   A 75  ? 0.58481 0.47380 0.65429 0.01529  0.01816  0.15789  75  LEU   A CG  
582  C CD1 . LEU   A 75  ? 0.46463 0.35877 0.52077 0.01202  0.01736  0.13669  75  LEU   A CD1 
583  C CD2 . LEU   A 75  ? 0.61740 0.48036 0.70658 0.01652  0.02683  0.15697  75  LEU   A CD2 
584  N N   . ARG   A 76  ? 0.66174 0.54532 0.73118 -0.00401 0.02435  0.19210  76  ARG   A N   
585  C CA  . ARG   A 76  ? 0.65087 0.53635 0.71585 -0.01325 0.02727  0.19736  76  ARG   A CA  
586  C C   . ARG   A 76  ? 0.58998 0.47430 0.64921 -0.02153 0.03035  0.18298  76  ARG   A C   
587  O O   . ARG   A 76  ? 0.58232 0.45097 0.64999 -0.02297 0.03359  0.16767  76  ARG   A O   
588  C CB  . ARG   A 76  ? 0.68823 0.55545 0.77054 -0.01432 0.03226  0.20349  76  ARG   A CB  
589  C CG  . ARG   A 76  ? 0.71345 0.58907 0.79127 -0.02050 0.03301  0.21677  76  ARG   A CG  
590  C CD  . ARG   A 76  ? 0.86221 0.72241 0.95761 -0.01867 0.03613  0.22676  76  ARG   A CD  
591  N NE  . ARG   A 76  ? 0.88926 0.75980 0.98685 -0.00990 0.03112  0.24031  76  ARG   A NE  
592  C CZ  . ARG   A 76  ? 0.90442 0.79639 0.98926 -0.01041 0.02624  0.25335  76  ARG   A CZ  
593  N NH1 . ARG   A 76  ? 0.86178 0.76681 0.92998 -0.01849 0.02674  0.25449  76  ARG   A NH1 
594  N NH2 . ARG   A 76  ? 0.94836 0.84963 1.03756 -0.00308 0.02118  0.26505  76  ARG   A NH2 
595  N N   . VAL   A 77  ? 0.59021 0.49378 0.63326 -0.02685 0.02898  0.18322  77  VAL   A N   
596  C CA  . VAL   A 77  ? 0.58829 0.49591 0.62638 -0.03439 0.03132  0.16740  77  VAL   A CA  
597  C C   . VAL   A 77  ? 0.55427 0.45183 0.60443 -0.04371 0.03733  0.17335  77  VAL   A C   
598  O O   . VAL   A 77  ? 0.62154 0.52227 0.67312 -0.04628 0.03946  0.19157  77  VAL   A O   
599  C CB  . VAL   A 77  ? 0.56816 0.50005 0.58633 -0.03526 0.02880  0.16449  77  VAL   A CB  
600  C CG1 . VAL   A 77  ? 0.50415 0.44175 0.52106 -0.04220 0.03160  0.15062  77  VAL   A CG1 
601  C CG2 . VAL   A 77  ? 0.52794 0.46786 0.53533 -0.02736 0.02266  0.15745  77  VAL   A CG2 
602  N N   . ILE   A 78  ? 0.53094 0.41703 0.58957 -0.04961 0.03977  0.15845  78  ILE   A N   
603  C CA  . ILE   A 78  ? 0.57469 0.45031 0.64636 -0.06032 0.04497  0.16132  78  ILE   A CA  
604  C C   . ILE   A 78  ? 0.60523 0.49611 0.67254 -0.06927 0.04537  0.15081  78  ILE   A C   
605  O O   . ILE   A 78  ? 0.55438 0.43955 0.63312 -0.07976 0.04900  0.15156  78  ILE   A O   
606  C CB  . ILE   A 78  ? 0.56364 0.41035 0.65201 -0.06173 0.04794  0.15385  78  ILE   A CB  
607  C CG1 . ILE   A 78  ? 0.59131 0.43535 0.67507 -0.06116 0.04554  0.13049  78  ILE   A CG1 
608  C CG2 . ILE   A 78  ? 0.54871 0.38073 0.64575 -0.05173 0.04878  0.16693  78  ILE   A CG2 
609  C CD1 . ILE   A 78  ? 0.58224 0.39891 0.67915 -0.06480 0.04943  0.11921  78  ILE   A CD1 
610  N N   . GLY   A 79  ? 0.56534 0.47587 0.61814 -0.06551 0.04186  0.14203  79  GLY   A N   
611  C CA  . GLY   A 79  ? 0.55971 0.48734 0.60992 -0.07185 0.04225  0.13349  79  GLY   A CA  
612  C C   . GLY   A 79  ? 0.54494 0.48873 0.58054 -0.06466 0.03818  0.12327  79  GLY   A C   
613  O O   . GLY   A 79  ? 0.51428 0.45211 0.54427 -0.05694 0.03430  0.11731  79  GLY   A O   
614  N N   . HIS   A 80  ? 0.54444 0.50854 0.57519 -0.06688 0.03967  0.12159  80  HIS   A N   
615  C CA  . HIS   A 80  ? 0.51074 0.48904 0.52938 -0.06027 0.03679  0.11212  80  HIS   A CA  
616  C C   . HIS   A 80  ? 0.48508 0.47683 0.50997 -0.06511 0.03731  0.10296  80  HIS   A C   
617  O O   . HIS   A 80  ? 0.43449 0.43156 0.47046 -0.07361 0.04092  0.10707  80  HIS   A O   
618  C CB  . HIS   A 80  ? 0.46749 0.45925 0.47142 -0.05533 0.03880  0.12044  80  HIS   A CB  
619  C CG  . HIS   A 80  ? 0.50521 0.50781 0.51074 -0.06126 0.04555  0.13222  80  HIS   A CG  
620  N ND1 . HIS   A 80  ? 0.59873 0.59443 0.60701 -0.06455 0.04819  0.14803  80  HIS   A ND1 
621  C CD2 . HIS   A 80  ? 0.43391 0.45454 0.43988 -0.06429 0.05089  0.13143  80  HIS   A CD2 
622  C CE1 . HIS   A 80  ? 0.59347 0.60285 0.60227 -0.07004 0.05484  0.15651  80  HIS   A CE1 
623  N NE2 . HIS   A 80  ? 0.59989 0.62481 0.60769 -0.06983 0.05696  0.14620  80  HIS   A NE2 
624  N N   . SER   A 81  ? 0.42803 0.42615 0.44719 -0.05973 0.03341  0.09167  81  SER   A N   
625  C CA  . SER   A 81  ? 0.41848 0.43197 0.44379 -0.06225 0.03301  0.08427  81  SER   A CA  
626  C C   . SER   A 81  ? 0.41917 0.44145 0.43423 -0.05316 0.03080  0.07726  81  SER   A C   
627  O O   . SER   A 81  ? 0.37177 0.38492 0.37738 -0.04695 0.02716  0.07380  81  SER   A O   
628  C CB  . SER   A 81  ? 0.37233 0.37905 0.40846 -0.06949 0.02873  0.07592  81  SER   A CB  
629  O OG  . SER   A 81  ? 0.38050 0.36917 0.41141 -0.06625 0.02489  0.06998  81  SER   A OG  
630  N N   . MET   A 82  ? 0.38704 0.42708 0.40599 -0.05245 0.03341  0.07554  82  MET   A N   
631  C CA  . MET   A 82  ? 0.32363 0.37146 0.33647 -0.04434 0.03208  0.06865  82  MET   A CA  
632  C C   . MET   A 82  ? 0.36702 0.42133 0.39042 -0.04583 0.02714  0.06153  82  MET   A C   
633  O O   . MET   A 82  ? 0.36185 0.42789 0.39907 -0.05200 0.02799  0.06320  82  MET   A O   
634  C CB  . MET   A 82  ? 0.38026 0.44311 0.39044 -0.04095 0.03975  0.07183  82  MET   A CB  
635  C CG  . MET   A 82  ? 0.37276 0.43909 0.37447 -0.03192 0.03982  0.06482  82  MET   A CG  
636  S SD  . MET   A 82  ? 0.45302 0.53034 0.44468 -0.02831 0.05048  0.06762  82  MET   A SD  
637  C CE  . MET   A 82  ? 0.44695 0.54209 0.45787 -0.03477 0.05797  0.07470  82  MET   A CE  
638  N N   . GLN   A 83  ? 0.36077 0.40914 0.37800 -0.04068 0.02167  0.05460  83  GLN   A N   
639  C CA  . GLN   A 83  ? 0.29479 0.35127 0.31934 -0.04085 0.01657  0.04903  83  GLN   A CA  
640  C C   . GLN   A 83  ? 0.29091 0.35238 0.31040 -0.03115 0.01696  0.04626  83  GLN   A C   
641  O O   . GLN   A 83  ? 0.31691 0.36779 0.32570 -0.02629 0.01422  0.04275  83  GLN   A O   
642  C CB  . GLN   A 83  ? 0.32602 0.37025 0.34796 -0.04464 0.01010  0.04337  83  GLN   A CB  
643  C CG  . GLN   A 83  ? 0.30259 0.35722 0.32996 -0.04595 0.00403  0.03858  83  GLN   A CG  
644  C CD  . GLN   A 83  ? 0.26053 0.30328 0.28170 -0.04966 -0.00135 0.03169  83  GLN   A CD  
645  O OE1 . GLN   A 83  ? 0.29531 0.32140 0.31115 -0.05148 0.00009  0.03006  83  GLN   A OE1 
646  N NE2 . GLN   A 83  ? 0.22430 0.27622 0.24660 -0.05066 -0.00705 0.02812  83  GLN   A NE2 
647  N N   . ASN   A 84  ? 0.27914 0.35652 0.30799 -0.02838 0.02074  0.04794  84  ASN   A N   
648  C CA  . ASN   A 84  ? 0.22211 0.30302 0.24853 -0.01899 0.02287  0.04523  84  ASN   A CA  
649  C C   . ASN   A 84  ? 0.28644 0.35652 0.29633 -0.01487 0.02705  0.04411  84  ASN   A C   
650  O O   . ASN   A 84  ? 0.35847 0.43107 0.36506 -0.01677 0.03336  0.04796  84  ASN   A O   
651  C CB  . ASN   A 84  ? 0.20165 0.28105 0.22966 -0.01686 0.01520  0.04156  84  ASN   A CB  
652  C CG  . ASN   A 84  ? 0.23854 0.32986 0.28016 -0.02348 0.00994  0.04332  84  ASN   A CG  
653  O OD1 . ASN   A 84  ? 0.23231 0.34070 0.28908 -0.02435 0.01232  0.04745  84  ASN   A OD1 
654  N ND2 . ASN   A 84  ? 0.21366 0.29726 0.25023 -0.02870 0.00300  0.04010  84  ASN   A ND2 
655  N N   . CYS   A 85  ? 0.26574 0.32495 0.26474 -0.01035 0.02348  0.03973  85  CYS   A N   
656  C CA  . CYS   A 85  ? 0.28352 0.33522 0.26703 -0.00760 0.02652  0.03874  85  CYS   A CA  
657  C C   . CYS   A 85  ? 0.29873 0.33820 0.27216 -0.01063 0.02208  0.04105  85  CYS   A C   
658  O O   . CYS   A 85  ? 0.30865 0.34280 0.26904 -0.00865 0.02220  0.04073  85  CYS   A O   
659  C CB  . CYS   A 85  ? 0.25990 0.30890 0.23900 -0.00073 0.02663  0.03258  85  CYS   A CB  
660  S SG  . CYS   A 85  ? 0.25264 0.31515 0.24433 0.00470  0.03530  0.03094  85  CYS   A SG  
661  N N   . VAL   A 86  ? 0.25659 0.29178 0.23617 -0.01554 0.01848  0.04346  86  VAL   A N   
662  C CA  . VAL   A 86  ? 0.35997 0.38284 0.33332 -0.01706 0.01531  0.04609  86  VAL   A CA  
663  C C   . VAL   A 86  ? 0.40263 0.42384 0.37971 -0.02291 0.01837  0.05342  86  VAL   A C   
664  O O   . VAL   A 86  ? 0.36246 0.38932 0.35014 -0.02800 0.02034  0.05460  86  VAL   A O   
665  C CB  . VAL   A 86  ? 0.30961 0.32433 0.28591 -0.01708 0.00952  0.04178  86  VAL   A CB  
666  C CG1 . VAL   A 86  ? 0.29688 0.31210 0.26916 -0.01156 0.00634  0.03643  86  VAL   A CG1 
667  C CG2 . VAL   A 86  ? 0.26864 0.28602 0.25564 -0.02277 0.00849  0.04007  86  VAL   A CG2 
668  N N   . LEU   A 87  ? 0.41239 0.42639 0.38187 -0.02256 0.01833  0.05934  87  LEU   A N   
669  C CA  . LEU   A 87  ? 0.39379 0.40233 0.36792 -0.02763 0.02044  0.06785  87  LEU   A CA  
670  C C   . LEU   A 87  ? 0.41527 0.40988 0.39681 -0.02923 0.01702  0.06603  87  LEU   A C   
671  O O   . LEU   A 87  ? 0.40791 0.39550 0.38593 -0.02475 0.01324  0.06288  87  LEU   A O   
672  C CB  . LEU   A 87  ? 0.41505 0.42290 0.37856 -0.02623 0.02151  0.07697  87  LEU   A CB  
673  C CG  . LEU   A 87  ? 0.45564 0.47381 0.41493 -0.02934 0.02780  0.08432  87  LEU   A CG  
674  C CD1 . LEU   A 87  ? 0.49400 0.50983 0.44273 -0.02877 0.02675  0.09493  87  LEU   A CD1 
675  C CD2 . LEU   A 87  ? 0.43749 0.45584 0.41101 -0.03609 0.03153  0.08842  87  LEU   A CD2 
676  N N   . LYS   A 88  ? 0.39026 0.38072 0.38239 -0.03601 0.01898  0.06765  88  LYS   A N   
677  C CA  . LYS   A 88  ? 0.38286 0.35742 0.38191 -0.03861 0.01760  0.06534  88  LYS   A CA  
678  C C   . LYS   A 88  ? 0.37691 0.34214 0.38081 -0.04160 0.02115  0.07667  88  LYS   A C   
679  O O   . LYS   A 88  ? 0.43420 0.40269 0.44471 -0.04841 0.02466  0.08169  88  LYS   A O   
680  C CB  . LYS   A 88  ? 0.33703 0.31251 0.34404 -0.04531 0.01631  0.05641  88  LYS   A CB  
681  C CG  . LYS   A 88  ? 0.31389 0.29949 0.31689 -0.04213 0.01220  0.04725  88  LYS   A CG  
682  C CD  . LYS   A 88  ? 0.29580 0.29156 0.30674 -0.04951 0.01033  0.04198  88  LYS   A CD  
683  C CE  . LYS   A 88  ? 0.37895 0.36332 0.39136 -0.05503 0.00765  0.03361  88  LYS   A CE  
684  N NZ  . LYS   A 88  ? 0.32362 0.31844 0.34174 -0.06357 0.00392  0.02776  88  LYS   A NZ  
685  N N   . LEU   A 89  ? 0.38433 0.33924 0.38632 -0.03642 0.02026  0.08207  89  LEU   A N   
686  C CA  . LEU   A 89  ? 0.43034 0.37689 0.43716 -0.03747 0.02306  0.09572  89  LEU   A CA  
687  C C   . LEU   A 89  ? 0.46213 0.38793 0.48102 -0.03863 0.02434  0.09323  89  LEU   A C   
688  O O   . LEU   A 89  ? 0.47177 0.38937 0.49103 -0.03228 0.02264  0.08987  89  LEU   A O   
689  C CB  . LEU   A 89  ? 0.41317 0.36489 0.41056 -0.03060 0.02073  0.10532  89  LEU   A CB  
690  C CG  . LEU   A 89  ? 0.40888 0.37897 0.39171 -0.02954 0.02013  0.10636  89  LEU   A CG  
691  C CD1 . LEU   A 89  ? 0.38062 0.35446 0.35339 -0.02348 0.01573  0.11188  89  LEU   A CD1 
692  C CD2 . LEU   A 89  ? 0.42576 0.40320 0.40806 -0.03532 0.02523  0.11650  89  LEU   A CD2 
693  N N   . LYS   A 90  ? 0.43976 0.35694 0.46917 -0.04703 0.02796  0.09417  90  LYS   A N   
694  C CA  . LYS   A 90  ? 0.47383 0.36846 0.51490 -0.04920 0.03048  0.09042  90  LYS   A CA  
695  C C   . LYS   A 90  ? 0.55026 0.43340 0.59793 -0.04376 0.03276  0.10598  90  LYS   A C   
696  O O   . LYS   A 90  ? 0.54361 0.43217 0.59214 -0.04573 0.03425  0.12093  90  LYS   A O   
697  C CB  . LYS   A 90  ? 0.52583 0.41503 0.57617 -0.06147 0.03308  0.08594  90  LYS   A CB  
698  C CG  . LYS   A 90  ? 0.58797 0.45194 0.64880 -0.06589 0.03603  0.07690  90  LYS   A CG  
699  C CD  . LYS   A 90  ? 0.59295 0.45849 0.65545 -0.07803 0.03470  0.06247  90  LYS   A CD  
700  C CE  . LYS   A 90  ? 0.64818 0.49408 0.71165 -0.08024 0.03582  0.04615  90  LYS   A CE  
701  N NZ  . LYS   A 90  ? 0.68595 0.52789 0.75406 -0.09542 0.03522  0.03491  90  LYS   A NZ  
702  N N   . VAL   A 91  ? 0.54145 0.41103 0.59382 -0.03633 0.03309  0.10361  91  VAL   A N   
703  C CA  . VAL   A 91  ? 0.54185 0.40251 0.60278 -0.02912 0.03446  0.11935  91  VAL   A CA  
704  C C   . VAL   A 91  ? 0.58229 0.41555 0.66040 -0.02968 0.04055  0.11681  91  VAL   A C   
705  O O   . VAL   A 91  ? 0.64102 0.46279 0.72074 -0.03384 0.04294  0.09971  91  VAL   A O   
706  C CB  . VAL   A 91  ? 0.57142 0.44221 0.62591 -0.01828 0.02988  0.12148  91  VAL   A CB  
707  C CG1 . VAL   A 91  ? 0.52240 0.41751 0.56007 -0.01837 0.02453  0.12514  91  VAL   A CG1 
708  C CG2 . VAL   A 91  ? 0.49154 0.35657 0.54563 -0.01456 0.03004  0.10419  91  VAL   A CG2 
709  N N   . ASP   A 92  ? 0.54574 0.36812 0.63675 -0.02552 0.04329  0.13415  92  ASP   A N   
710  C CA  . ASP   A 92  ? 0.65708 0.45047 0.76675 -0.02637 0.05053  0.13262  92  ASP   A CA  
711  C C   . ASP   A 92  ? 0.65900 0.43907 0.77433 -0.01773 0.05353  0.12021  92  ASP   A C   
712  O O   . ASP   A 92  ? 0.67469 0.42997 0.80129 -0.02007 0.06049  0.11015  92  ASP   A O   
713  C CB  . ASP   A 92  ? 0.65476 0.44301 0.77581 -0.02339 0.05189  0.15303  92  ASP   A CB  
714  C CG  . ASP   A 92  ? 0.72474 0.53023 0.84259 -0.01181 0.04644  0.16755  92  ASP   A CG  
715  O OD1 . ASP   A 92  ? 0.78092 0.59173 0.90205 -0.01012 0.04500  0.18330  92  ASP   A OD1 
716  O OD2 . ASP   A 92  ? 0.67890 0.49362 0.79092 -0.00525 0.04326  0.16328  92  ASP   A OD2 
717  N N   . THR   A 93  ? 0.63228 0.42788 0.74015 -0.00843 0.04911  0.12000  93  THR   A N   
718  C CA  . THR   A 93  ? 0.63589 0.42206 0.74972 0.00036  0.05262  0.10965  93  THR   A CA  
719  C C   . THR   A 93  ? 0.52714 0.32306 0.62457 -0.00292 0.05028  0.08845  93  THR   A C   
720  O O   . THR   A 93  ? 0.50119 0.31951 0.58344 -0.00464 0.04321  0.08807  93  THR   A O   
721  C CB  . THR   A 93  ? 0.60966 0.40729 0.72977 0.01307  0.04939  0.12552  93  THR   A CB  
722  O OG1 . THR   A 93  ? 0.64092 0.43929 0.77050 0.01486  0.04825  0.14578  93  THR   A OG1 
723  C CG2 . THR   A 93  ? 0.50777 0.29266 0.64064 0.02298  0.05561  0.11777  93  THR   A CG2 
724  N N   . ALA   A 94  ? 0.53543 0.31418 0.63567 -0.00393 0.05659  0.07100  94  ALA   A N   
725  C CA  . ALA   A 94  ? 0.52789 0.31624 0.61355 -0.00512 0.05478  0.05298  94  ALA   A CA  
726  C C   . ALA   A 94  ? 0.54116 0.33931 0.62863 0.00743  0.05417  0.05636  94  ALA   A C   
727  O O   . ALA   A 94  ? 0.41100 0.19753 0.51467 0.01674  0.05982  0.06308  94  ALA   A O   
728  C CB  . ALA   A 94  ? 0.48439 0.25213 0.56989 -0.01180 0.06184  0.03276  94  ALA   A CB  
729  N N   . ASN   A 95  ? 0.46983 0.28977 0.54277 0.00777  0.04740  0.05297  95  ASN   A N   
730  C CA  . ASN   A 95  ? 0.44095 0.27184 0.51563 0.01799  0.04628  0.05569  95  ASN   A CA  
731  C C   . ASN   A 95  ? 0.47941 0.29587 0.55914 0.02168  0.05530  0.04129  95  ASN   A C   
732  O O   . ASN   A 95  ? 0.48304 0.29658 0.55077 0.01465  0.05699  0.02418  95  ASN   A O   
733  C CB  . ASN   A 95  ? 0.44263 0.29700 0.50056 0.01587  0.03783  0.05317  95  ASN   A CB  
734  C CG  . ASN   A 95  ? 0.44534 0.31254 0.50544 0.02500  0.03587  0.05650  95  ASN   A CG  
735  O OD1 . ASN   A 95  ? 0.43587 0.29663 0.51073 0.03350  0.04088  0.06093  95  ASN   A OD1 
736  N ND2 . ASN   A 95  ? 0.40180 0.28735 0.44869 0.02307  0.02886  0.05458  95  ASN   A ND2 
737  N N   . PRO   A 96  ? 0.45900 0.26608 0.55657 0.03223  0.06183  0.04756  96  PRO   A N   
738  C CA  . PRO   A 96  ? 0.49674 0.29017 0.59863 0.03628  0.07234  0.03243  96  PRO   A CA  
739  C C   . PRO   A 96  ? 0.47363 0.28526 0.56494 0.03913  0.07044  0.02503  96  PRO   A C   
740  O O   . PRO   A 96  ? 0.46462 0.26876 0.55206 0.03938  0.07838  0.00932  96  PRO   A O   
741  C CB  . PRO   A 96  ? 0.44778 0.22740 0.57571 0.04816  0.08011  0.04463  96  PRO   A CB  
742  C CG  . PRO   A 96  ? 0.44202 0.23902 0.57665 0.05226  0.07032  0.06852  96  PRO   A CG  
743  C CD  . PRO   A 96  ? 0.41392 0.22347 0.52886 0.04088  0.06019  0.06923  96  PRO   A CD  
744  N N   . LYS   A 97  ? 0.42507 0.25986 0.51086 0.04056  0.06060  0.03536  97  LYS   A N   
745  C CA  . LYS   A 97  ? 0.44835 0.29986 0.52552 0.04256  0.05864  0.02965  97  LYS   A CA  
746  C C   . LYS   A 97  ? 0.44037 0.30184 0.49584 0.03250  0.05226  0.01971  97  LYS   A C   
747  O O   . LYS   A 97  ? 0.43408 0.31240 0.48195 0.03335  0.04782  0.01925  97  LYS   A O   
748  C CB  . LYS   A 97  ? 0.40332 0.27373 0.48895 0.04981  0.05181  0.04631  97  LYS   A CB  
749  C CG  . LYS   A 97  ? 0.42090 0.28448 0.53144 0.06108  0.05791  0.05819  97  LYS   A CG  
750  C CD  . LYS   A 97  ? 0.35822 0.24400 0.47651 0.06635  0.04860  0.07638  97  LYS   A CD  
751  C CE  . LYS   A 97  ? 0.46347 0.35691 0.57011 0.05912  0.03761  0.08605  97  LYS   A CE  
752  N NZ  . LYS   A 97  ? 0.39839 0.27715 0.51016 0.05705  0.03899  0.09386  97  LYS   A NZ  
753  N N   . THR   A 98  ? 0.45350 0.30512 0.50069 0.02296  0.05191  0.01229  98  THR   A N   
754  C CA  . THR   A 98  ? 0.44348 0.30438 0.47231 0.01320  0.04643  0.00256  98  THR   A CA  
755  C C   . THR   A 98  ? 0.44757 0.31017 0.46676 0.01239  0.05081  -0.01192 98  THR   A C   
756  O O   . THR   A 98  ? 0.42363 0.27001 0.44390 0.01134  0.05977  -0.02363 98  THR   A O   
757  C CB  . THR   A 98  ? 0.47474 0.32433 0.50010 0.00283  0.04637  -0.00297 98  THR   A CB  
758  O OG1 . THR   A 98  ? 0.44643 0.29532 0.47958 0.00252  0.04295  0.01097  98  THR   A OG1 
759  C CG2 . THR   A 98  ? 0.41271 0.27516 0.42149 -0.00662 0.04014  -0.01161 98  THR   A CG2 
760  N N   . PRO   A 99  ? 0.45132 0.33227 0.46051 0.01235  0.04535  -0.01188 99  PRO   A N   
761  C CA  . PRO   A 99  ? 0.38272 0.26741 0.37987 0.00966  0.04866  -0.02469 99  PRO   A CA  
762  C C   . PRO   A 99  ? 0.41335 0.29756 0.39595 -0.00218 0.04537  -0.03523 99  PRO   A C   
763  O O   . PRO   A 99  ? 0.39629 0.28168 0.37867 -0.00780 0.03933  -0.03122 99  PRO   A O   
764  C CB  . PRO   A 99  ? 0.37825 0.28325 0.37204 0.01319  0.04247  -0.01729 99  PRO   A CB  
765  C CG  . PRO   A 99  ? 0.34033 0.25286 0.33532 0.01166  0.03324  -0.00643 99  PRO   A CG  
766  C CD  . PRO   A 99  ? 0.42620 0.32482 0.43319 0.01342  0.03575  -0.00051 99  PRO   A CD  
767  N N   . LYS   A 100 ? 0.40055 0.28451 0.37103 -0.00630 0.04953  -0.04848 100 LYS   A N   
768  C CA  . LYS   A 100 ? 0.37045 0.26332 0.32510 -0.01745 0.04324  -0.05573 100 LYS   A CA  
769  C C   . LYS   A 100 ? 0.37393 0.28717 0.32643 -0.01677 0.03292  -0.04446 100 LYS   A C   
770  O O   . LYS   A 100 ? 0.32831 0.25119 0.28341 -0.00953 0.03209  -0.03716 100 LYS   A O   
771  C CB  . LYS   A 100 ? 0.43014 0.32435 0.36958 -0.02151 0.04832  -0.06965 100 LYS   A CB  
772  C CG  . LYS   A 100 ? 0.51534 0.42322 0.43791 -0.03340 0.03997  -0.07495 100 LYS   A CG  
773  C CD  . LYS   A 100 ? 0.57509 0.47546 0.49737 -0.04451 0.03598  -0.08009 100 LYS   A CD  
774  C CE  . LYS   A 100 ? 0.71401 0.62903 0.61983 -0.05735 0.02813  -0.08681 100 LYS   A CE  
775  N NZ  . LYS   A 100 ? 0.62534 0.56505 0.52847 -0.05669 0.01769  -0.07512 100 LYS   A NZ  
776  N N   . TYR   A 101 ? 0.36627 0.28559 0.31567 -0.02439 0.02554  -0.04303 101 TYR   A N   
777  C CA  . TYR   A 101 ? 0.35710 0.29251 0.30769 -0.02285 0.01715  -0.03218 101 TYR   A CA  
778  C C   . TYR   A 101 ? 0.35842 0.30412 0.30306 -0.03238 0.01023  -0.03410 101 TYR   A C   
779  O O   . TYR   A 101 ? 0.42787 0.36674 0.37114 -0.04079 0.01079  -0.04125 101 TYR   A O   
780  C CB  . TYR   A 101 ? 0.34492 0.27639 0.30768 -0.01714 0.01648  -0.02122 101 TYR   A CB  
781  C CG  . TYR   A 101 ? 0.30465 0.22941 0.27229 -0.02297 0.01560  -0.02019 101 TYR   A CG  
782  C CD1 . TYR   A 101 ? 0.37124 0.27763 0.34566 -0.02400 0.02187  -0.02339 101 TYR   A CD1 
783  C CD2 . TYR   A 101 ? 0.31611 0.25276 0.28338 -0.02717 0.00926  -0.01529 101 TYR   A CD2 
784  C CE1 . TYR   A 101 ? 0.37354 0.27348 0.35359 -0.03020 0.02132  -0.02134 101 TYR   A CE1 
785  C CE2 . TYR   A 101 ? 0.31986 0.25205 0.29280 -0.03296 0.00908  -0.01343 101 TYR   A CE2 
786  C CZ  . TYR   A 101 ? 0.38633 0.30023 0.36532 -0.03494 0.01482  -0.01618 101 TYR   A CZ  
787  O OH  . TYR   A 101 ? 0.44349 0.35286 0.42909 -0.04135 0.01484  -0.01324 101 TYR   A OH  
788  N N   . LYS   A 102 ? 0.30071 0.26290 0.24369 -0.03084 0.00378  -0.02702 102 LYS   A N   
789  C CA  . LYS   A 102 ? 0.31062 0.28703 0.25186 -0.03711 -0.00345 -0.02491 102 LYS   A CA  
790  C C   . LYS   A 102 ? 0.31427 0.29813 0.26372 -0.03114 -0.00675 -0.01386 102 LYS   A C   
791  O O   . LYS   A 102 ? 0.27151 0.25329 0.22344 -0.02331 -0.00516 -0.00890 102 LYS   A O   
792  C CB  . LYS   A 102 ? 0.37617 0.36661 0.30664 -0.04023 -0.00734 -0.02706 102 LYS   A CB  
793  C CG  . LYS   A 102 ? 0.44527 0.43341 0.36351 -0.04953 -0.00596 -0.03922 102 LYS   A CG  
794  C CD  . LYS   A 102 ? 0.47100 0.47316 0.37656 -0.05080 -0.00848 -0.03957 102 LYS   A CD  
795  C CE  . LYS   A 102 ? 0.53375 0.53461 0.42325 -0.06116 -0.00684 -0.05307 102 LYS   A CE  
796  N NZ  . LYS   A 102 ? 0.52227 0.50636 0.40551 -0.05842 0.00423  -0.06390 102 LYS   A NZ  
797  N N   . PHE   A 103 ? 0.29554 0.28862 0.24944 -0.03524 -0.01103 -0.01046 103 PHE   A N   
798  C CA  . PHE   A 103 ? 0.23491 0.23796 0.19477 -0.03010 -0.01387 -0.00164 103 PHE   A CA  
799  C C   . PHE   A 103 ? 0.24803 0.26723 0.20603 -0.03169 -0.01941 0.00042  103 PHE   A C   
800  O O   . PHE   A 103 ? 0.24386 0.27176 0.20093 -0.03945 -0.02310 -0.00203 103 PHE   A O   
801  C CB  . PHE   A 103 ? 0.26186 0.26600 0.23002 -0.03223 -0.01350 0.00211  103 PHE   A CB  
802  C CG  . PHE   A 103 ? 0.23142 0.22154 0.20234 -0.03014 -0.00861 0.00346  103 PHE   A CG  
803  C CD1 . PHE   A 103 ? 0.26037 0.23935 0.22875 -0.02462 -0.00540 0.00301  103 PHE   A CD1 
804  C CD2 . PHE   A 103 ? 0.23797 0.22745 0.21545 -0.03401 -0.00723 0.00651  103 PHE   A CD2 
805  C CE1 . PHE   A 103 ? 0.21844 0.18599 0.19101 -0.02236 -0.00158 0.00650  103 PHE   A CE1 
806  C CE2 . PHE   A 103 ? 0.22168 0.19899 0.20198 -0.03229 -0.00297 0.00995  103 PHE   A CE2 
807  C CZ  . PHE   A 103 ? 0.25009 0.21640 0.22798 -0.02626 -0.00051 0.01026  103 PHE   A CZ  
808  N N   . VAL   A 104 ? 0.19803 0.22155 0.15605 -0.02499 -0.02041 0.00547  104 VAL   A N   
809  C CA  . VAL   A 104 ? 0.19746 0.23591 0.15634 -0.02515 -0.02550 0.01017  104 VAL   A CA  
810  C C   . VAL   A 104 ? 0.19904 0.24097 0.16726 -0.01829 -0.02565 0.01739  104 VAL   A C   
811  O O   . VAL   A 104 ? 0.24269 0.27529 0.21197 -0.01313 -0.02220 0.01790  104 VAL   A O   
812  C CB  . VAL   A 104 ? 0.27489 0.31532 0.22520 -0.02414 -0.02614 0.00994  104 VAL   A CB  
813  C CG1 . VAL   A 104 ? 0.25949 0.29427 0.19896 -0.03001 -0.02375 0.00091  104 VAL   A CG1 
814  C CG2 . VAL   A 104 ? 0.20977 0.24359 0.16198 -0.01626 -0.02345 0.01353  104 VAL   A CG2 
815  N N   . ARG   A 105 ? 0.22791 0.28378 0.20314 -0.01842 -0.02958 0.02290  105 ARG   A N   
816  C CA  . ARG   A 105 ? 0.18197 0.24119 0.16681 -0.01127 -0.02895 0.02925  105 ARG   A CA  
817  C C   . ARG   A 105 ? 0.17722 0.24185 0.16159 -0.00847 -0.03211 0.03455  105 ARG   A C   
818  O O   . ARG   A 105 ? 0.17905 0.25625 0.16281 -0.01249 -0.03702 0.03776  105 ARG   A O   
819  C CB  . ARG   A 105 ? 0.17361 0.24500 0.17053 -0.01223 -0.02985 0.03300  105 ARG   A CB  
820  C CG  . ARG   A 105 ? 0.16895 0.24338 0.17720 -0.00412 -0.02755 0.03861  105 ARG   A CG  
821  C CD  . ARG   A 105 ? 0.16829 0.25353 0.18922 -0.00444 -0.02586 0.04122  105 ARG   A CD  
822  N NE  . ARG   A 105 ? 0.16636 0.25377 0.19900 0.00416  -0.02183 0.04547  105 ARG   A NE  
823  C CZ  . ARG   A 105 ? 0.16660 0.24296 0.19726 0.00900  -0.01506 0.04187  105 ARG   A CZ  
824  N NH1 . ARG   A 105 ? 0.16736 0.23152 0.18559 0.00625  -0.01267 0.03600  105 ARG   A NH1 
825  N NH2 . ARG   A 105 ? 0.16803 0.24566 0.20913 0.01653  -0.01047 0.04419  105 ARG   A NH2 
826  N N   . ILE   A 106 ? 0.17153 0.22711 0.15557 -0.00263 -0.02968 0.03577  106 ILE   A N   
827  C CA  . ILE   A 106 ? 0.18715 0.24494 0.17042 -0.00044 -0.03174 0.04105  106 ILE   A CA  
828  C C   . ILE   A 106 ? 0.17115 0.23408 0.16765 0.00516  -0.03257 0.04886  106 ILE   A C   
829  O O   . ILE   A 106 ? 0.16881 0.22822 0.17294 0.00899  -0.02934 0.04778  106 ILE   A O   
830  C CB  . ILE   A 106 ? 0.17153 0.21678 0.14897 0.00182  -0.02873 0.03843  106 ILE   A CB  
831  C CG1 . ILE   A 106 ? 0.20736 0.24227 0.18941 0.00638  -0.02539 0.03650  106 ILE   A CG1 
832  C CG2 . ILE   A 106 ? 0.17445 0.21520 0.14159 -0.00223 -0.02699 0.03186  106 ILE   A CG2 
833  C CD1 . ILE   A 106 ? 0.25659 0.28198 0.23652 0.00845  -0.02404 0.03600  106 ILE   A CD1 
834  N N   . GLN   A 107 ? 0.17435 0.24536 0.17365 0.00590  -0.03622 0.05713  107 GLN   A N   
835  C CA  . GLN   A 107 ? 0.22495 0.29904 0.23818 0.01203  -0.03685 0.06654  107 GLN   A CA  
836  C C   . GLN   A 107 ? 0.23828 0.29639 0.25292 0.01667  -0.03282 0.06541  107 GLN   A C   
837  O O   . GLN   A 107 ? 0.17684 0.22739 0.18148 0.01423  -0.03202 0.06178  107 GLN   A O   
838  C CB  . GLN   A 107 ? 0.18854 0.27750 0.20286 0.01008  -0.04285 0.07738  107 GLN   A CB  
839  C CG  . GLN   A 107 ? 0.26480 0.37396 0.28434 0.00654  -0.04860 0.08265  107 GLN   A CG  
840  C CD  . GLN   A 107 ? 0.27055 0.38378 0.30840 0.01203  -0.04668 0.08519  107 GLN   A CD  
841  O OE1 . GLN   A 107 ? 0.30658 0.42132 0.36064 0.01953  -0.04573 0.09415  107 GLN   A OE1 
842  N NE2 . GLN   A 107 ? 0.30094 0.41544 0.33723 0.00849  -0.04518 0.07742  107 GLN   A NE2 
843  N N   . PRO   A 108 ? 0.25421 0.30720 0.28209 0.02311  -0.02993 0.06812  108 PRO   A N   
844  C CA  . PRO   A 108 ? 0.21758 0.25568 0.24828 0.02645  -0.02700 0.06798  108 PRO   A CA  
845  C C   . PRO   A 108 ? 0.21985 0.26000 0.24747 0.02405  -0.03035 0.07541  108 PRO   A C   
846  O O   . PRO   A 108 ? 0.21047 0.26446 0.23930 0.02262  -0.03471 0.08459  108 PRO   A O   
847  C CB  . PRO   A 108 ? 0.23103 0.26713 0.27931 0.03383  -0.02398 0.07271  108 PRO   A CB  
848  C CG  . PRO   A 108 ? 0.19982 0.25387 0.25651 0.03477  -0.02640 0.07843  108 PRO   A CG  
849  C CD  . PRO   A 108 ? 0.25082 0.31242 0.29326 0.02745  -0.02903 0.07210  108 PRO   A CD  
850  N N   . GLY   A 109 ? 0.22346 0.25151 0.24615 0.02270  -0.02852 0.07166  109 GLY   A N   
851  C CA  . GLY   A 109 ? 0.18760 0.21839 0.20621 0.01957  -0.03058 0.07788  109 GLY   A CA  
852  C C   . GLY   A 109 ? 0.25371 0.28737 0.25758 0.01432  -0.03059 0.07154  109 GLY   A C   
853  O O   . GLY   A 109 ? 0.29342 0.32397 0.29397 0.01207  -0.02973 0.07258  109 GLY   A O   
854  N N   . GLN   A 110 ? 0.28959 0.32978 0.28581 0.01209  -0.03116 0.06578  110 GLN   A N   
855  C CA  . GLN   A 110 ? 0.30856 0.34753 0.29312 0.00826  -0.02957 0.05929  110 GLN   A CA  
856  C C   . GLN   A 110 ? 0.29408 0.32077 0.27853 0.00912  -0.02674 0.05283  110 GLN   A C   
857  O O   . GLN   A 110 ? 0.26567 0.28417 0.25539 0.01159  -0.02593 0.05037  110 GLN   A O   
858  C CB  . GLN   A 110 ? 0.29138 0.33493 0.26708 0.00493  -0.02947 0.05239  110 GLN   A CB  
859  C CG  . GLN   A 110 ? 0.43540 0.49205 0.40447 0.00058  -0.03237 0.05389  110 GLN   A CG  
860  C CD  . GLN   A 110 ? 0.48054 0.54748 0.44441 -0.00189 -0.03432 0.06155  110 GLN   A CD  
861  O OE1 . GLN   A 110 ? 0.66164 0.74092 0.62206 -0.00528 -0.03827 0.06442  110 GLN   A OE1 
862  N NE2 . GLN   A 110 ? 0.52659 0.59022 0.49593 0.00078  -0.03343 0.06864  110 GLN   A NE2 
863  N N   . THR   A 111 ? 0.21439 0.24102 0.19329 0.00695  -0.02521 0.05110  111 THR   A N   
864  C CA  . THR   A 111 ? 0.24189 0.26058 0.22111 0.00712  -0.02354 0.04643  111 THR   A CA  
865  C C   . THR   A 111 ? 0.19899 0.21788 0.17158 0.00626  -0.02166 0.03991  111 THR   A C   
866  O O   . THR   A 111 ? 0.18294 0.20729 0.14972 0.00452  -0.02099 0.03824  111 THR   A O   
867  C CB  . THR   A 111 ? 0.23142 0.25101 0.21309 0.00578  -0.02267 0.05062  111 THR   A CB  
868  O OG1 . THR   A 111 ? 0.25037 0.27850 0.22551 0.00414  -0.02053 0.05151  111 THR   A OG1 
869  C CG2 . THR   A 111 ? 0.21326 0.23100 0.20272 0.00603  -0.02425 0.05800  111 THR   A CG2 
870  N N   . PHE   A 112 ? 0.21991 0.23267 0.19359 0.00696  -0.02096 0.03655  112 PHE   A N   
871  C CA  . PHE   A 112 ? 0.21140 0.22271 0.18165 0.00690  -0.01873 0.03217  112 PHE   A CA  
872  C C   . PHE   A 112 ? 0.25139 0.25973 0.22567 0.00763  -0.01900 0.03285  112 PHE   A C   
873  O O   . PHE   A 112 ? 0.22887 0.23621 0.20722 0.00702  -0.02121 0.03541  112 PHE   A O   
874  C CB  . PHE   A 112 ? 0.17708 0.18596 0.14476 0.00675  -0.01880 0.02850  112 PHE   A CB  
875  C CG  . PHE   A 112 ? 0.16944 0.17467 0.13934 0.00790  -0.02037 0.02848  112 PHE   A CG  
876  C CD1 . PHE   A 112 ? 0.18697 0.19385 0.16013 0.00884  -0.02145 0.03043  112 PHE   A CD1 
877  C CD2 . PHE   A 112 ? 0.17058 0.17122 0.13938 0.00821  -0.02032 0.02680  112 PHE   A CD2 
878  C CE1 . PHE   A 112 ? 0.22873 0.23114 0.20389 0.01043  -0.02110 0.02889  112 PHE   A CE1 
879  C CE2 . PHE   A 112 ? 0.18349 0.18099 0.15167 0.00869  -0.02080 0.02542  112 PHE   A CE2 
880  C CZ  . PHE   A 112 ? 0.16976 0.16734 0.14097 0.00995  -0.02052 0.02553  112 PHE   A CZ  
881  N N   . SER   A 113 ? 0.20330 0.21051 0.17748 0.00859  -0.01686 0.03101  113 SER   A N   
882  C CA  . SER   A 113 ? 0.20754 0.21446 0.18677 0.00951  -0.01775 0.03301  113 SER   A CA  
883  C C   . SER   A 113 ? 0.24124 0.24384 0.21796 0.00975  -0.01929 0.03176  113 SER   A C   
884  O O   . SER   A 113 ? 0.19530 0.19497 0.16842 0.00993  -0.01735 0.02920  113 SER   A O   
885  C CB  . SER   A 113 ? 0.27702 0.28684 0.26080 0.01163  -0.01335 0.03381  113 SER   A CB  
886  O OG  . SER   A 113 ? 0.23031 0.24607 0.21675 0.01118  -0.01133 0.03602  113 SER   A OG  
887  N N   . VAL   A 114 ? 0.23355 0.23658 0.21170 0.00887  -0.02296 0.03384  114 VAL   A N   
888  C CA  . VAL   A 114 ? 0.22156 0.22232 0.19550 0.00841  -0.02475 0.03379  114 VAL   A CA  
889  C C   . VAL   A 114 ? 0.20765 0.21224 0.18712 0.00944  -0.02636 0.03898  114 VAL   A C   
890  O O   . VAL   A 114 ? 0.22418 0.23418 0.20955 0.00856  -0.02915 0.04207  114 VAL   A O   
891  C CB  . VAL   A 114 ? 0.25461 0.25346 0.22302 0.00569  -0.02792 0.03130  114 VAL   A CB  
892  C CG1 . VAL   A 114 ? 0.18028 0.17877 0.14202 0.00458  -0.02939 0.03167  114 VAL   A CG1 
893  C CG2 . VAL   A 114 ? 0.18267 0.17815 0.14920 0.00600  -0.02587 0.02757  114 VAL   A CG2 
894  N N   . LEU   A 115 ? 0.21250 0.21501 0.19156 0.01108  -0.02490 0.04099  115 LEU   A N   
895  C CA  . LEU   A 115 ? 0.18516 0.19181 0.17025 0.01255  -0.02709 0.04800  115 LEU   A CA  
896  C C   . LEU   A 115 ? 0.20852 0.21638 0.18479 0.00951  -0.03152 0.04992  115 LEU   A C   
897  O O   . LEU   A 115 ? 0.26153 0.26516 0.23215 0.00944  -0.02939 0.04967  115 LEU   A O   
898  C CB  . LEU   A 115 ? 0.18186 0.18417 0.17401 0.01682  -0.02155 0.04990  115 LEU   A CB  
899  C CG  . LEU   A 115 ? 0.18970 0.19481 0.19009 0.01963  -0.02292 0.05891  115 LEU   A CG  
900  C CD1 . LEU   A 115 ? 0.22506 0.24059 0.23769 0.02157  -0.02557 0.06486  115 LEU   A CD1 
901  C CD2 . LEU   A 115 ? 0.20291 0.19855 0.20860 0.02329  -0.01623 0.05914  115 LEU   A CD2 
902  N N   . ALA   A 116 ? 0.22485 0.23895 0.19910 0.00608  -0.03750 0.05136  116 ALA   A N   
903  C CA  . ALA   A 116 ? 0.27108 0.28771 0.23425 0.00209  -0.04192 0.05225  116 ALA   A CA  
904  C C   . ALA   A 116 ? 0.29487 0.31734 0.26160 0.00358  -0.04435 0.06260  116 ALA   A C   
905  O O   . ALA   A 116 ? 0.24750 0.27709 0.22659 0.00572  -0.04697 0.07009  116 ALA   A O   
906  C CB  . ALA   A 116 ? 0.25617 0.27715 0.21519 -0.00350 -0.04797 0.04927  116 ALA   A CB  
907  N N   . CYS   A 117 ? 0.23095 0.25142 0.18798 0.00256  -0.04330 0.06407  117 CYS   A N   
908  C CA  . CYS   A 117 ? 0.29017 0.31431 0.25055 0.00435  -0.04446 0.07528  117 CYS   A CA  
909  C C   . CYS   A 117 ? 0.34034 0.37000 0.28464 -0.00082 -0.04836 0.07777  117 CYS   A C   
910  O O   . CYS   A 117 ? 0.31482 0.34150 0.24506 -0.00447 -0.04658 0.06901  117 CYS   A O   
911  C CB  . CYS   A 117 ? 0.31167 0.32601 0.27848 0.00870  -0.03695 0.07632  117 CYS   A CB  
912  S SG  . CYS   A 117 ? 0.35675 0.36490 0.34108 0.01474  -0.03143 0.07424  117 CYS   A SG  
913  N N   . TYR   A 118 ? 0.38281 0.42133 0.32983 -0.00079 -0.05330 0.09049  118 TYR   A N   
914  C CA  . TYR   A 118 ? 0.36760 0.41433 0.29866 -0.00611 -0.05784 0.09568  118 TYR   A CA  
915  C C   . TYR   A 118 ? 0.42796 0.47781 0.36795 -0.00245 -0.05811 0.11191  118 TYR   A C   
916  O O   . TYR   A 118 ? 0.43772 0.49213 0.39530 0.00203  -0.06096 0.12184  118 TYR   A O   
917  C CB  . TYR   A 118 ? 0.35976 0.41884 0.28295 -0.01261 -0.06758 0.09499  118 TYR   A CB  
918  C CG  . TYR   A 118 ? 0.38515 0.43793 0.30138 -0.01615 -0.06633 0.07891  118 TYR   A CG  
919  C CD1 . TYR   A 118 ? 0.41457 0.46648 0.34458 -0.01471 -0.06758 0.07555  118 TYR   A CD1 
920  C CD2 . TYR   A 118 ? 0.34904 0.39585 0.24669 -0.02016 -0.06245 0.06756  118 TYR   A CD2 
921  C CE1 . TYR   A 118 ? 0.34425 0.38902 0.26954 -0.01774 -0.06601 0.06239  118 TYR   A CE1 
922  C CE2 . TYR   A 118 ? 0.32715 0.36630 0.22116 -0.02231 -0.06042 0.05377  118 TYR   A CE2 
923  C CZ  . TYR   A 118 ? 0.33174 0.36945 0.23966 -0.02126 -0.06256 0.05171  118 TYR   A CZ  
924  O OH  . TYR   A 118 ? 0.30899 0.33815 0.21460 -0.02336 -0.06039 0.03959  118 TYR   A OH  
925  N N   . ASN   A 119 ? 0.41583 0.46249 0.34611 -0.00373 -0.05400 0.11499  119 ASN   A N   
926  C CA  . ASN   A 119 ? 0.43183 0.47982 0.37014 -0.00085 -0.05362 0.13158  119 ASN   A CA  
927  C C   . ASN   A 119 ? 0.43168 0.46744 0.39290 0.00691  -0.04744 0.13434  119 ASN   A C   
928  O O   . ASN   A 119 ? 0.41564 0.45214 0.39133 0.01134  -0.04812 0.14898  119 ASN   A O   
929  C CB  . ASN   A 119 ? 0.39418 0.45852 0.33284 -0.00267 -0.06341 0.14513  119 ASN   A CB  
930  C CG  . ASN   A 119 ? 0.51426 0.58914 0.42907 -0.01143 -0.06862 0.13874  119 ASN   A CG  
931  O OD1 . ASN   A 119 ? 0.60355 0.67936 0.50217 -0.01530 -0.06588 0.13915  119 ASN   A OD1 
932  N ND2 . ASN   A 119 ? 0.47610 0.55855 0.38851 -0.01507 -0.07550 0.13216  119 ASN   A ND2 
933  N N   . GLY   A 120 ? 0.42559 0.44995 0.39018 0.00854  -0.04118 0.12027  120 GLY   A N   
934  C CA  . GLY   A 120 ? 0.38236 0.39472 0.36527 0.01466  -0.03486 0.11903  120 GLY   A CA  
935  C C   . GLY   A 120 ? 0.37811 0.39414 0.37652 0.01965  -0.03688 0.12027  120 GLY   A C   
936  O O   . GLY   A 120 ? 0.38470 0.39077 0.39778 0.02507  -0.03054 0.11819  120 GLY   A O   
937  N N   . SER   A 121 ? 0.42373 0.45407 0.41943 0.01748  -0.04506 0.12315  121 SER   A N   
938  C CA  . SER   A 121 ? 0.42746 0.46479 0.43994 0.02178  -0.04740 0.12655  121 SER   A CA  
939  C C   . SER   A 121 ? 0.44705 0.48551 0.45387 0.01864  -0.04804 0.11298  121 SER   A C   
940  O O   . SER   A 121 ? 0.42137 0.46650 0.41328 0.01188  -0.05400 0.10842  121 SER   A O   
941  C CB  . SER   A 121 ? 0.55904 0.61427 0.57639 0.02096  -0.05729 0.14207  121 SER   A CB  
942  O OG  . SER   A 121 ? 0.64120 0.69553 0.67069 0.02611  -0.05604 0.15753  121 SER   A OG  
943  N N   . PRO   A 122 ? 0.37217 0.40394 0.38999 0.02302  -0.04173 0.10635  122 PRO   A N   
944  C CA  . PRO   A 122 ? 0.34217 0.37504 0.35524 0.01996  -0.04208 0.09516  122 PRO   A CA  
945  C C   . PRO   A 122 ? 0.39551 0.44391 0.41159 0.01639  -0.05095 0.09973  122 PRO   A C   
946  O O   . PRO   A 122 ? 0.49321 0.55262 0.52442 0.01946  -0.05442 0.11120  122 PRO   A O   
947  C CB  . PRO   A 122 ? 0.31476 0.33989 0.34058 0.02592  -0.03335 0.09060  122 PRO   A CB  
948  C CG  . PRO   A 122 ? 0.32105 0.33469 0.35105 0.03003  -0.02702 0.09325  122 PRO   A CG  
949  C CD  . PRO   A 122 ? 0.32942 0.35069 0.36268 0.03040  -0.03298 0.10766  122 PRO   A CD  
950  N N   . SER   A 123 ? 0.37279 0.42204 0.37529 0.00958  -0.05470 0.09090  123 SER   A N   
951  C CA  . SER   A 123 ? 0.41709 0.47879 0.41968 0.00362  -0.06334 0.09207  123 SER   A CA  
952  C C   . SER   A 123 ? 0.37565 0.43775 0.38798 0.00374  -0.06114 0.08676  123 SER   A C   
953  O O   . SER   A 123 ? 0.39343 0.46836 0.41904 0.00271  -0.06578 0.09302  123 SER   A O   
954  C CB  . SER   A 123 ? 0.45942 0.51955 0.44015 -0.00468 -0.06803 0.08473  123 SER   A CB  
955  O OG  . SER   A 123 ? 0.65837 0.73023 0.63676 -0.01226 -0.07751 0.08567  123 SER   A OG  
956  N N   . GLY   A 124 ? 0.30600 0.35586 0.31270 0.00468  -0.05432 0.07653  124 GLY   A N   
957  C CA  . GLY   A 124 ? 0.27401 0.32374 0.28734 0.00411  -0.05189 0.07198  124 GLY   A CA  
958  C C   . GLY   A 124 ? 0.24815 0.28533 0.25595 0.00686  -0.04377 0.06362  124 GLY   A C   
959  O O   . GLY   A 124 ? 0.20291 0.23134 0.20084 0.00792  -0.04082 0.05980  124 GLY   A O   
960  N N   . VAL   A 125 ? 0.21566 0.25380 0.23043 0.00747  -0.04045 0.06172  125 VAL   A N   
961  C CA  . VAL   A 125 ? 0.20902 0.23844 0.21904 0.00939  -0.03368 0.05517  125 VAL   A CA  
962  C C   . VAL   A 125 ? 0.21138 0.24128 0.22114 0.00528  -0.03487 0.05247  125 VAL   A C   
963  O O   . VAL   A 125 ? 0.19540 0.23369 0.21553 0.00363  -0.03644 0.05668  125 VAL   A O   
964  C CB  . VAL   A 125 ? 0.22585 0.25531 0.24446 0.01551  -0.02593 0.05647  125 VAL   A CB  
965  C CG1 . VAL   A 125 ? 0.18086 0.22211 0.21584 0.01749  -0.02563 0.06346  125 VAL   A CG1 
966  C CG2 . VAL   A 125 ? 0.16972 0.19358 0.18228 0.01570  -0.02019 0.05002  125 VAL   A CG2 
967  N N   . TYR   A 126 ? 0.20496 0.22635 0.20460 0.00355  -0.03419 0.04649  126 TYR   A N   
968  C CA  . TYR   A 126 ? 0.22760 0.24709 0.22782 0.00032  -0.03465 0.04485  126 TYR   A CA  
969  C C   . TYR   A 126 ? 0.24143 0.25462 0.23569 0.00249  -0.03015 0.04132  126 TYR   A C   
970  O O   . TYR   A 126 ? 0.19817 0.20787 0.18640 0.00509  -0.02773 0.03861  126 TYR   A O   
971  C CB  . TYR   A 126 ? 0.22554 0.24132 0.22147 -0.00545 -0.04049 0.04189  126 TYR   A CB  
972  C CG  . TYR   A 126 ? 0.24793 0.25724 0.23180 -0.00543 -0.04123 0.03682  126 TYR   A CG  
973  C CD1 . TYR   A 126 ? 0.25122 0.25195 0.22857 -0.00403 -0.03796 0.03168  126 TYR   A CD1 
974  C CD2 . TYR   A 126 ? 0.25676 0.27033 0.23677 -0.00657 -0.04489 0.03845  126 TYR   A CD2 
975  C CE1 . TYR   A 126 ? 0.24269 0.23912 0.21006 -0.00383 -0.03741 0.02734  126 TYR   A CE1 
976  C CE2 . TYR   A 126 ? 0.25946 0.26857 0.22779 -0.00679 -0.04466 0.03469  126 TYR   A CE2 
977  C CZ  . TYR   A 126 ? 0.24182 0.24239 0.20395 -0.00540 -0.04044 0.02873  126 TYR   A CZ  
978  O OH  . TYR   A 126 ? 0.26147 0.25934 0.21280 -0.00575 -0.03940 0.02535  126 TYR   A OH  
979  N N   . GLN   A 127 ? 0.20730 0.21979 0.20415 0.00071  -0.02969 0.04232  127 GLN   A N   
980  C CA  . GLN   A 127 ? 0.21469 0.22456 0.20803 0.00228  -0.02655 0.04167  127 GLN   A CA  
981  C C   . GLN   A 127 ? 0.26617 0.26784 0.25648 0.00118  -0.02846 0.03883  127 GLN   A C   
982  O O   . GLN   A 127 ? 0.35449 0.35215 0.34825 -0.00207 -0.03107 0.03875  127 GLN   A O   
983  C CB  . GLN   A 127 ? 0.19120 0.20700 0.19040 0.00141  -0.02428 0.04693  127 GLN   A CB  
984  C CG  . GLN   A 127 ? 0.21372 0.23149 0.20810 0.00300  -0.02089 0.04789  127 GLN   A CG  
985  C CD  . GLN   A 127 ? 0.23909 0.25903 0.22751 0.00560  -0.01722 0.04407  127 GLN   A CD  
986  O OE1 . GLN   A 127 ? 0.28602 0.30647 0.27684 0.00711  -0.01602 0.04254  127 GLN   A OE1 
987  N NE2 . GLN   A 127 ? 0.18667 0.20763 0.16813 0.00581  -0.01579 0.04273  127 GLN   A NE2 
988  N N   . CYS   A 128 ? 0.21013 0.20932 0.19523 0.00372  -0.02674 0.03631  128 CYS   A N   
989  C CA  . CYS   A 128 ? 0.27301 0.26552 0.25719 0.00442  -0.02684 0.03386  128 CYS   A CA  
990  C C   . CYS   A 128 ? 0.19132 0.18648 0.17765 0.00666  -0.02527 0.03744  128 CYS   A C   
991  O O   . CYS   A 128 ? 0.17123 0.17320 0.15503 0.00723  -0.02416 0.03916  128 CYS   A O   
992  C CB  . CYS   A 128 ? 0.20599 0.19587 0.18367 0.00560  -0.02614 0.02864  128 CYS   A CB  
993  S SG  . CYS   A 128 ? 0.47467 0.45960 0.44746 0.00225  -0.02875 0.02389  128 CYS   A SG  
994  N N   . ALA   A 129 ? 0.20783 0.19758 0.19880 0.00785  -0.02514 0.03834  129 ALA   A N   
995  C CA  . ALA   A 129 ? 0.27028 0.26390 0.26432 0.01083  -0.02432 0.04226  129 ALA   A CA  
996  C C   . ALA   A 129 ? 0.19618 0.18687 0.19022 0.01372  -0.02254 0.03773  129 ALA   A C   
997  O O   . ALA   A 129 ? 0.20382 0.18650 0.19608 0.01364  -0.02126 0.03176  129 ALA   A O   
998  C CB  . ALA   A 129 ? 0.22421 0.21566 0.22724 0.01146  -0.02474 0.04956  129 ALA   A CB  
999  N N   . MET   A 130 ? 0.18290 0.18146 0.17860 0.01568  -0.02235 0.04054  130 MET   A N   
1000 C CA  . MET   A 130 ? 0.18450 0.18261 0.18457 0.01913  -0.01998 0.03856  130 MET   A CA  
1001 C C   . MET   A 130 ? 0.23540 0.22931 0.24732 0.02298  -0.01897 0.04353  130 MET   A C   
1002 O O   . MET   A 130 ? 0.26096 0.26213 0.27926 0.02401  -0.02116 0.05234  130 MET   A O   
1003 C CB  . MET   A 130 ? 0.23752 0.24748 0.23690 0.01881  -0.02083 0.04038  130 MET   A CB  
1004 C CG  . MET   A 130 ? 0.24206 0.25599 0.25013 0.02265  -0.01853 0.04126  130 MET   A CG  
1005 S SD  . MET   A 130 ? 0.28857 0.29476 0.29108 0.02314  -0.01352 0.03193  130 MET   A SD  
1006 C CE  . MET   A 130 ? 0.22064 0.23005 0.21112 0.01759  -0.01557 0.02909  130 MET   A CE  
1007 N N   . ARG   A 131 ? 0.24702 0.22878 0.26167 0.02482  -0.01555 0.03812  131 ARG   A N   
1008 C CA  . ARG   A 131 ? 0.25313 0.22699 0.28049 0.02867  -0.01356 0.04209  131 ARG   A CA  
1009 C C   . ARG   A 131 ? 0.30187 0.28444 0.34154 0.03479  -0.01190 0.04858  131 ARG   A C   
1010 O O   . ARG   A 131 ? 0.28085 0.27411 0.31816 0.03520  -0.01176 0.04755  131 ARG   A O   
1011 C CB  . ARG   A 131 ? 0.28797 0.24546 0.31393 0.02859  -0.00936 0.03220  131 ARG   A CB  
1012 C CG  . ARG   A 131 ? 0.31270 0.26430 0.32654 0.02178  -0.01189 0.02542  131 ARG   A CG  
1013 C CD  . ARG   A 131 ? 0.31625 0.26598 0.33355 0.01777  -0.01588 0.03146  131 ARG   A CD  
1014 N NE  . ARG   A 131 ? 0.33405 0.27548 0.36532 0.02061  -0.01419 0.03741  131 ARG   A NE  
1015 C CZ  . ARG   A 131 ? 0.35148 0.29491 0.38935 0.01880  -0.01692 0.04728  131 ARG   A CZ  
1016 N NH1 . ARG   A 131 ? 0.32917 0.28304 0.36027 0.01440  -0.02067 0.05078  131 ARG   A NH1 
1017 N NH2 . ARG   A 131 ? 0.34449 0.27965 0.39643 0.02168  -0.01518 0.05423  131 ARG   A NH2 
1018 N N   . PRO   A 132 ? 0.30729 0.28681 0.36192 0.03932  -0.01109 0.05684  132 PRO   A N   
1019 C CA  . PRO   A 132 ? 0.33519 0.32501 0.40458 0.04590  -0.00975 0.06448  132 PRO   A CA  
1020 C C   . PRO   A 132 ? 0.31024 0.29822 0.38259 0.05025  -0.00303 0.05606  132 PRO   A C   
1021 O O   . PRO   A 132 ? 0.32909 0.33152 0.41024 0.05367  -0.00278 0.06105  132 PRO   A O   
1022 C CB  . PRO   A 132 ? 0.26800 0.24990 0.35411 0.05059  -0.00884 0.07421  132 PRO   A CB  
1023 C CG  . PRO   A 132 ? 0.35487 0.33275 0.43258 0.04424  -0.01316 0.07687  132 PRO   A CG  
1024 C CD  . PRO   A 132 ? 0.25833 0.22957 0.31844 0.03805  -0.01281 0.06331  132 PRO   A CD  
1025 N N   . ASN   A 133 ? 0.32257 0.29498 0.38722 0.04945  0.00229  0.04357  133 ASN   A N   
1026 C CA  . ASN   A 133 ? 0.29527 0.26634 0.35950 0.05285  0.00976  0.03470  133 ASN   A CA  
1027 C C   . ASN   A 133 ? 0.30702 0.28716 0.35506 0.04744  0.00826  0.02901  133 ASN   A C   
1028 O O   . ASN   A 133 ? 0.28828 0.26488 0.32991 0.04791  0.01435  0.01993  133 ASN   A O   
1029 C CB  . ASN   A 133 ? 0.36390 0.31372 0.42563 0.05388  0.01670  0.02320  133 ASN   A CB  
1030 C CG  . ASN   A 133 ? 0.35456 0.29517 0.39673 0.04505  0.01298  0.01453  133 ASN   A CG  
1031 O OD1 . ASN   A 133 ? 0.33519 0.28290 0.37014 0.03966  0.00555  0.01926  133 ASN   A OD1 
1032 N ND2 . ASN   A 133 ? 0.35991 0.28576 0.39372 0.04346  0.01831  0.00178  133 ASN   A ND2 
1033 N N   . PHE   A 134 ? 0.29359 0.28432 0.33448 0.04216  0.00093  0.03398  134 PHE   A N   
1034 C CA  . PHE   A 134 ? 0.27373 0.27162 0.30140 0.03707  -0.00058 0.02992  134 PHE   A CA  
1035 C C   . PHE   A 134 ? 0.26943 0.25635 0.28223 0.03380  0.00214  0.01948  134 PHE   A C   
1036 O O   . PHE   A 134 ? 0.28661 0.27753 0.29189 0.03214  0.00457  0.01557  134 PHE   A O   
1037 C CB  . PHE   A 134 ? 0.23503 0.24679 0.27020 0.03928  0.00205  0.03231  134 PHE   A CB  
1038 C CG  . PHE   A 134 ? 0.21896 0.24556 0.26776 0.04088  -0.00238 0.04325  134 PHE   A CG  
1039 C CD1 . PHE   A 134 ? 0.22474 0.26157 0.26748 0.03495  -0.00938 0.04718  134 PHE   A CD1 
1040 C CD2 . PHE   A 134 ? 0.20299 0.23332 0.27080 0.04826  0.00043  0.04976  134 PHE   A CD2 
1041 C CE1 . PHE   A 134 ? 0.21991 0.27220 0.27283 0.03497  -0.01458 0.05717  134 PHE   A CE1 
1042 C CE2 . PHE   A 134 ? 0.19082 0.23761 0.27167 0.04935  -0.00507 0.06184  134 PHE   A CE2 
1043 C CZ  . PHE   A 134 ? 0.21467 0.27314 0.28652 0.04192  -0.01316 0.06533  134 PHE   A CZ  
1044 N N   . THR   A 135 ? 0.28664 0.26064 0.29536 0.03215  0.00138  0.01568  135 THR   A N   
1045 C CA  . THR   A 135 ? 0.33749 0.30422 0.33069 0.02682  0.00059  0.00773  135 THR   A CA  
1046 C C   . THR   A 135 ? 0.26834 0.23515 0.25777 0.02201  -0.00644 0.01145  135 THR   A C   
1047 O O   . THR   A 135 ? 0.20906 0.17892 0.20665 0.02284  -0.00940 0.01876  135 THR   A O   
1048 C CB  . THR   A 135 ? 0.28076 0.23270 0.27116 0.02708  0.00538  -0.00163 135 THR   A CB  
1049 O OG1 . THR   A 135 ? 0.30148 0.24427 0.30223 0.02811  0.00407  0.00119  135 THR   A OG1 
1050 C CG2 . THR   A 135 ? 0.28073 0.23145 0.27470 0.03255  0.01458  -0.00693 135 THR   A CG2 
1051 N N   . ILE   A 136 ? 0.25015 0.21485 0.22760 0.01698  -0.00891 0.00713  136 ILE   A N   
1052 C CA  . ILE   A 136 ? 0.33346 0.29850 0.30939 0.01277  -0.01461 0.01029  136 ILE   A CA  
1053 C C   . ILE   A 136 ? 0.28454 0.24089 0.25372 0.00791  -0.01624 0.00389  136 ILE   A C   
1054 O O   . ILE   A 136 ? 0.26577 0.22074 0.22423 0.00572  -0.01517 -0.00242 136 ILE   A O   
1055 C CB  . ILE   A 136 ? 0.23926 0.21402 0.21037 0.01106  -0.01754 0.01405  136 ILE   A CB  
1056 C CG1 . ILE   A 136 ? 0.27920 0.25529 0.24001 0.00943  -0.01654 0.01007  136 ILE   A CG1 
1057 C CG2 . ILE   A 136 ? 0.24132 0.22423 0.21853 0.01389  -0.01695 0.01953  136 ILE   A CG2 
1058 C CD1 . ILE   A 136 ? 0.32664 0.30905 0.28429 0.00762  -0.01945 0.01401  136 ILE   A CD1 
1059 N N   . LYS   A 137 ? 0.31327 0.26483 0.28835 0.00534  -0.01911 0.00594  137 LYS   A N   
1060 C CA  . LYS   A 137 ? 0.29673 0.24257 0.26670 -0.00134 -0.02266 0.00106  137 LYS   A CA  
1061 C C   . LYS   A 137 ? 0.32459 0.28148 0.28950 -0.00479 -0.02793 0.00492  137 LYS   A C   
1062 O O   . LYS   A 137 ? 0.36472 0.32685 0.33624 -0.00629 -0.03115 0.01123  137 LYS   A O   
1063 C CB  . LYS   A 137 ? 0.27454 0.21226 0.25519 -0.00337 -0.02373 0.00336  137 LYS   A CB  
1064 C CG  . LYS   A 137 ? 0.37179 0.29709 0.36055 0.00093  -0.01813 0.00096  137 LYS   A CG  
1065 C CD  . LYS   A 137 ? 0.40664 0.32194 0.40667 -0.00204 -0.01929 0.00399  137 LYS   A CD  
1066 C CE  . LYS   A 137 ? 0.50096 0.40055 0.50994 0.00252  -0.01286 0.00042  137 LYS   A CE  
1067 N NZ  . LYS   A 137 ? 0.54216 0.43626 0.56758 0.00383  -0.01290 0.01043  137 LYS   A NZ  
1068 N N   . GLY   A 138 ? 0.34606 0.30713 0.30013 -0.00563 -0.02817 0.00197  138 GLY   A N   
1069 C CA  . GLY   A 138 ? 0.32592 0.29710 0.27685 -0.00767 -0.03258 0.00675  138 GLY   A CA  
1070 C C   . GLY   A 138 ? 0.33590 0.30819 0.27807 -0.01454 -0.03772 0.00324  138 GLY   A C   
1071 O O   . GLY   A 138 ? 0.36740 0.33157 0.30446 -0.01896 -0.03803 -0.00448 138 GLY   A O   
1072 N N   . SER   A 139 ? 0.30169 0.28446 0.24271 -0.01564 -0.04194 0.00928  139 SER   A N   
1073 C CA  . SER   A 139 ? 0.33558 0.32392 0.26818 -0.02222 -0.04827 0.00865  139 SER   A CA  
1074 C C   . SER   A 139 ? 0.31442 0.30981 0.23871 -0.02030 -0.04801 0.01263  139 SER   A C   
1075 O O   . SER   A 139 ? 0.27960 0.28213 0.21130 -0.01663 -0.04862 0.02130  139 SER   A O   
1076 C CB  . SER   A 139 ? 0.24116 0.23800 0.18435 -0.02582 -0.05486 0.01515  139 SER   A CB  
1077 O OG  . SER   A 139 ? 0.24136 0.24666 0.17714 -0.03252 -0.06225 0.01607  139 SER   A OG  
1078 N N   . PHE   A 140 ? 0.28099 0.27387 0.19006 -0.02296 -0.04648 0.00635  140 PHE   A N   
1079 C CA  . PHE   A 140 ? 0.30601 0.30423 0.20657 -0.02102 -0.04443 0.01023  140 PHE   A CA  
1080 C C   . PHE   A 140 ? 0.33348 0.33494 0.21538 -0.02787 -0.04732 0.00584  140 PHE   A C   
1081 O O   . PHE   A 140 ? 0.37585 0.36934 0.24781 -0.03127 -0.04457 -0.00552 140 PHE   A O   
1082 C CB  . PHE   A 140 ? 0.32728 0.31935 0.22887 -0.01510 -0.03551 0.00725  140 PHE   A CB  
1083 C CG  . PHE   A 140 ? 0.27583 0.26792 0.19219 -0.00937 -0.03342 0.01292  140 PHE   A CG  
1084 C CD1 . PHE   A 140 ? 0.24648 0.24498 0.16917 -0.00774 -0.03596 0.02193  140 PHE   A CD1 
1085 C CD2 . PHE   A 140 ? 0.26473 0.25057 0.18877 -0.00579 -0.02897 0.00936  140 PHE   A CD2 
1086 C CE1 . PHE   A 140 ? 0.27096 0.26860 0.20510 -0.00331 -0.03344 0.02520  140 PHE   A CE1 
1087 C CE2 . PHE   A 140 ? 0.26578 0.25303 0.20077 -0.00177 -0.02764 0.01414  140 PHE   A CE2 
1088 C CZ  . PHE   A 140 ? 0.27428 0.26685 0.21327 -0.00089 -0.02959 0.02097  140 PHE   A CZ  
1089 N N   . LEU   A 141 ? 0.33708 0.35000 0.21416 -0.02989 -0.05251 0.01489  141 LEU   A N   
1090 C CA  . LEU   A 141 ? 0.37400 0.39328 0.23110 -0.03707 -0.05611 0.01286  141 LEU   A CA  
1091 C C   . LEU   A 141 ? 0.35677 0.37895 0.20505 -0.03401 -0.05032 0.01724  141 LEU   A C   
1092 O O   . LEU   A 141 ? 0.38233 0.40061 0.24084 -0.02706 -0.04386 0.02055  141 LEU   A O   
1093 C CB  . LEU   A 141 ? 0.31905 0.35217 0.17731 -0.04278 -0.06778 0.02201  141 LEU   A CB  
1094 C CG  . LEU   A 141 ? 0.47506 0.50799 0.33933 -0.04893 -0.07468 0.01724  141 LEU   A CG  
1095 C CD1 . LEU   A 141 ? 0.52955 0.57916 0.38794 -0.05752 -0.08688 0.02430  141 LEU   A CD1 
1096 C CD2 . LEU   A 141 ? 0.31182 0.33005 0.16713 -0.05299 -0.07025 0.00043  141 LEU   A CD2 
1097 N N   . ASN   A 142 ? 0.36091 0.39070 0.18947 -0.04020 -0.05278 0.01730  142 ASN   A N   
1098 C CA  . ASN   A 142 ? 0.37401 0.40861 0.19368 -0.03839 -0.04765 0.02361  142 ASN   A CA  
1099 C C   . ASN   A 142 ? 0.38019 0.41953 0.21697 -0.03256 -0.04932 0.03964  142 ASN   A C   
1100 O O   . ASN   A 142 ? 0.36522 0.40865 0.21585 -0.03150 -0.05639 0.04737  142 ASN   A O   
1101 C CB  . ASN   A 142 ? 0.40101 0.44633 0.19613 -0.04708 -0.05215 0.02396  142 ASN   A CB  
1102 C CG  . ASN   A 142 ? 0.54191 0.58020 0.31644 -0.05116 -0.04450 0.00674  142 ASN   A CG  
1103 O OD1 . ASN   A 142 ? 0.46086 0.48830 0.24045 -0.04549 -0.03369 -0.00167 142 ASN   A OD1 
1104 N ND2 . ASN   A 142 ? 0.44169 0.48663 0.19324 -0.06111 -0.04991 0.00122  142 ASN   A ND2 
1105 N N   . GLY   A 143 ? 0.36965 0.40780 0.20694 -0.02873 -0.04194 0.04422  143 GLY   A N   
1106 C CA  . GLY   A 143 ? 0.34155 0.38048 0.19558 -0.02340 -0.04193 0.05754  143 GLY   A CA  
1107 C C   . GLY   A 143 ? 0.32155 0.35229 0.19683 -0.01745 -0.04077 0.05609  143 GLY   A C   
1108 O O   . GLY   A 143 ? 0.36333 0.39376 0.25282 -0.01338 -0.04116 0.06586  143 GLY   A O   
1109 N N   . SER   A 144 ? 0.31660 0.34032 0.19458 -0.01681 -0.03890 0.04445  144 SER   A N   
1110 C CA  . SER   A 144 ? 0.38766 0.40534 0.28387 -0.01162 -0.03752 0.04426  144 SER   A CA  
1111 C C   . SER   A 144 ? 0.31036 0.32172 0.21266 -0.00758 -0.02946 0.04226  144 SER   A C   
1112 O O   . SER   A 144 ? 0.31065 0.31767 0.22595 -0.00398 -0.02805 0.04209  144 SER   A O   
1113 C CB  . SER   A 144 ? 0.30340 0.31710 0.20259 -0.01269 -0.03963 0.03533  144 SER   A CB  
1114 O OG  . SER   A 144 ? 0.33415 0.34285 0.22205 -0.01510 -0.03599 0.02414  144 SER   A OG  
1115 N N   . CYS   A 145 ? 0.34707 0.35906 0.24028 -0.00866 -0.02414 0.04078  145 CYS   A N   
1116 C CA  . CYS   A 145 ? 0.33880 0.34693 0.23955 -0.00578 -0.01718 0.03900  145 CYS   A CA  
1117 C C   . CYS   A 145 ? 0.33674 0.34294 0.24981 -0.00373 -0.01719 0.04733  145 CYS   A C   
1118 O O   . CYS   A 145 ? 0.34858 0.35703 0.26261 -0.00411 -0.02039 0.05669  145 CYS   A O   
1119 C CB  . CYS   A 145 ? 0.33525 0.34660 0.22545 -0.00754 -0.01089 0.03718  145 CYS   A CB  
1120 S SG  . CYS   A 145 ? 0.43565 0.44530 0.31405 -0.00866 -0.00831 0.02394  145 CYS   A SG  
1121 N N   . GLY   A 146 ? 0.26771 0.26951 0.19091 -0.00160 -0.01382 0.04379  146 GLY   A N   
1122 C CA  . GLY   A 146 ? 0.29820 0.29578 0.23257 -0.00031 -0.01312 0.04846  146 GLY   A CA  
1123 C C   . GLY   A 146 ? 0.28023 0.27458 0.22310 0.00228  -0.01607 0.04739  146 GLY   A C   
1124 O O   . GLY   A 146 ? 0.22341 0.21276 0.17502 0.00339  -0.01392 0.04754  146 GLY   A O   
1125 N N   . SER   A 147 ? 0.26281 0.26000 0.20322 0.00265  -0.02049 0.04594  147 SER   A N   
1126 C CA  . SER   A 147 ? 0.23595 0.23175 0.18474 0.00489  -0.02222 0.04428  147 SER   A CA  
1127 C C   . SER   A 147 ? 0.23915 0.23179 0.19121 0.00552  -0.01889 0.03758  147 SER   A C   
1128 O O   . SER   A 147 ? 0.27303 0.26638 0.22099 0.00451  -0.01716 0.03327  147 SER   A O   
1129 C CB  . SER   A 147 ? 0.26377 0.26384 0.20943 0.00363  -0.02732 0.04296  147 SER   A CB  
1130 O OG  . SER   A 147 ? 0.25728 0.26310 0.19879 0.00180  -0.03198 0.04945  147 SER   A OG  
1131 N N   . VAL   A 148 ? 0.19856 0.18865 0.15815 0.00726  -0.01771 0.03703  148 VAL   A N   
1132 C CA  . VAL   A 148 ? 0.22737 0.21624 0.18874 0.00688  -0.01535 0.03172  148 VAL   A CA  
1133 C C   . VAL   A 148 ? 0.22330 0.21434 0.18674 0.00798  -0.01696 0.02965  148 VAL   A C   
1134 O O   . VAL   A 148 ? 0.30174 0.29442 0.26776 0.00910  -0.01905 0.03221  148 VAL   A O   
1135 C CB  . VAL   A 148 ? 0.22068 0.20456 0.18634 0.00634  -0.01181 0.03100  148 VAL   A CB  
1136 C CG1 . VAL   A 148 ? 0.20274 0.18394 0.16793 0.00452  -0.01000 0.03434  148 VAL   A CG1 
1137 C CG2 . VAL   A 148 ? 0.18657 0.16725 0.15821 0.00912  -0.01058 0.03249  148 VAL   A CG2 
1138 N N   . GLY   A 149 ? 0.20304 0.19553 0.16625 0.00730  -0.01625 0.02615  149 GLY   A N   
1139 C CA  . GLY   A 149 ? 0.22029 0.21511 0.18558 0.00784  -0.01681 0.02531  149 GLY   A CA  
1140 C C   . GLY   A 149 ? 0.22321 0.21821 0.18854 0.00677  -0.01431 0.02275  149 GLY   A C   
1141 O O   . GLY   A 149 ? 0.18579 0.17958 0.14994 0.00469  -0.01304 0.02070  149 GLY   A O   
1142 N N   . PHE   A 150 ? 0.17232 0.16941 0.13843 0.00730  -0.01340 0.02249  150 PHE   A N   
1143 C CA  . PHE   A 150 ? 0.21934 0.21579 0.18306 0.00574  -0.01011 0.01853  150 PHE   A CA  
1144 C C   . PHE   A 150 ? 0.23976 0.24136 0.20204 0.00584  -0.00896 0.01865  150 PHE   A C   
1145 O O   . PHE   A 150 ? 0.23967 0.24412 0.20558 0.00769  -0.00985 0.02256  150 PHE   A O   
1146 C CB  . PHE   A 150 ? 0.20959 0.19864 0.17621 0.00711  -0.00609 0.01705  150 PHE   A CB  
1147 C CG  . PHE   A 150 ? 0.23821 0.22739 0.21138 0.01123  -0.00502 0.02108  150 PHE   A CG  
1148 C CD1 . PHE   A 150 ? 0.20741 0.19770 0.18404 0.01270  -0.00868 0.02654  150 PHE   A CD1 
1149 C CD2 . PHE   A 150 ? 0.23644 0.22603 0.21239 0.01328  -0.00017 0.01943  150 PHE   A CD2 
1150 C CE1 . PHE   A 150 ? 0.23207 0.22525 0.21616 0.01569  -0.00902 0.03137  150 PHE   A CE1 
1151 C CE2 . PHE   A 150 ? 0.24047 0.23267 0.22564 0.01741  0.00092  0.02437  150 PHE   A CE2 
1152 C CZ  . PHE   A 150 ? 0.25113 0.24583 0.24113 0.01839  -0.00425 0.03091  150 PHE   A CZ  
1153 N N   . ASN   A 151 ? 0.25148 0.25456 0.20793 0.00300  -0.00675 0.01417  151 ASN   A N   
1154 C CA  . ASN   A 151 ? 0.25980 0.26794 0.21234 0.00250  -0.00396 0.01335  151 ASN   A CA  
1155 C C   . ASN   A 151 ? 0.32822 0.33039 0.27776 0.00211  0.00265  0.00603  151 ASN   A C   
1156 O O   . ASN   A 151 ? 0.33590 0.33026 0.28523 0.00060  0.00384  0.00141  151 ASN   A O   
1157 C CB  . ASN   A 151 ? 0.24804 0.26518 0.19392 -0.00135 -0.00755 0.01474  151 ASN   A CB  
1158 C CG  . ASN   A 151 ? 0.26103 0.28285 0.21220 0.00043  -0.01203 0.02274  151 ASN   A CG  
1159 O OD1 . ASN   A 151 ? 0.18584 0.20798 0.14023 0.00059  -0.01593 0.02502  151 ASN   A OD1 
1160 N ND2 . ASN   A 151 ? 0.26116 0.28588 0.21469 0.00194  -0.01064 0.02691  151 ASN   A ND2 
1161 N N   . ILE   A 152 ? 0.36214 0.36718 0.31038 0.00357  0.00791  0.00490  152 ILE   A N   
1162 C CA  . ILE   A 152 ? 0.49707 0.49570 0.44175 0.00347  0.01593  -0.00370 152 ILE   A CA  
1163 C C   . ILE   A 152 ? 0.57297 0.57904 0.50415 -0.00107 0.01851  -0.00845 152 ILE   A C   
1164 O O   . ILE   A 152 ? 0.65097 0.66782 0.57997 -0.00129 0.01683  -0.00247 152 ILE   A O   
1165 C CB  . ILE   A 152 ? 0.55066 0.54558 0.50715 0.01025  0.02226  -0.00178 152 ILE   A CB  
1166 C CG1 . ILE   A 152 ? 0.35717 0.34690 0.32491 0.01352  0.01795  0.00426  152 ILE   A CG1 
1167 C CG2 . ILE   A 152 ? 0.62899 0.61500 0.58319 0.01117  0.03252  -0.01183 152 ILE   A CG2 
1168 C CD1 . ILE   A 152 ? 0.35272 0.33888 0.33408 0.02012  0.02312  0.00731  152 ILE   A CD1 
1169 N N   . ASP   A 153 ? 0.51206 0.51247 0.43347 -0.00561 0.02224  -0.01899 153 ASP   A N   
1170 C CA  . ASP   A 153 ? 0.72310 0.73165 0.62815 -0.01166 0.02384  -0.02449 153 ASP   A CA  
1171 C C   . ASP   A 153 ? 0.74413 0.74195 0.64219 -0.01300 0.03425  -0.03838 153 ASP   A C   
1172 O O   . ASP   A 153 ? 0.71596 0.70324 0.61073 -0.01752 0.03449  -0.04727 153 ASP   A O   
1173 C CB  . ASP   A 153 ? 0.69839 0.71453 0.59557 -0.01901 0.01424  -0.02305 153 ASP   A CB  
1174 C CG  . ASP   A 153 ? 0.77573 0.80635 0.65761 -0.02470 0.01251  -0.02247 153 ASP   A CG  
1175 O OD1 . ASP   A 153 ? 0.78166 0.81561 0.65737 -0.02330 0.01978  -0.02419 153 ASP   A OD1 
1176 O OD2 . ASP   A 153 ? 0.83118 0.87200 0.70948 -0.02952 0.00368  -0.01747 153 ASP   A OD2 
1177 N N   . TYR   A 154 ? 0.87845 0.87867 0.77539 -0.00908 0.04358  -0.04027 154 TYR   A N   
1178 C CA  . TYR   A 154 ? 0.94057 0.92897 0.83759 -0.00612 0.05660  -0.05182 154 TYR   A CA  
1179 C C   . TYR   A 154 ? 0.87399 0.84600 0.78894 0.00016  0.05928  -0.05193 154 TYR   A C   
1180 O O   . TYR   A 154 ? 0.99259 0.96453 0.92429 0.00893  0.06274  -0.04444 154 TYR   A O   
1181 C CB  . TYR   A 154 ? 0.83610 0.82095 0.71190 -0.01530 0.06046  -0.06727 154 TYR   A CB  
1182 C CG  . TYR   A 154 ? 0.91478 0.91788 0.77125 -0.02207 0.05742  -0.06591 154 TYR   A CG  
1183 C CD1 . TYR   A 154 ? 0.89401 0.90827 0.74177 -0.02983 0.04470  -0.06053 154 TYR   A CD1 
1184 C CD2 . TYR   A 154 ? 0.92310 0.93412 0.77188 -0.02005 0.06738  -0.06785 154 TYR   A CD2 
1185 C CE1 . TYR   A 154 ? 0.97215 1.00441 0.80341 -0.03574 0.04114  -0.05672 154 TYR   A CE1 
1186 C CE2 . TYR   A 154 ? 0.93574 0.96472 0.76635 -0.02651 0.06441  -0.06451 154 TYR   A CE2 
1187 C CZ  . TYR   A 154 ? 0.97710 1.01653 0.79895 -0.03435 0.05083  -0.05847 154 TYR   A CZ  
1188 O OH  . TYR   A 154 ? 0.99459 1.05293 0.79933 -0.04060 0.04718  -0.05296 154 TYR   A OH  
1189 N N   . ASP   A 155 ? 0.69098 0.65005 0.60363 -0.00456 0.05751  -0.05925 155 ASP   A N   
1190 C CA  . ASP   A 155 ? 0.76494 0.70784 0.69447 0.00105  0.06059  -0.05826 155 ASP   A CA  
1191 C C   . ASP   A 155 ? 0.64717 0.58800 0.58176 -0.00203 0.04997  -0.05152 155 ASP   A C   
1192 O O   . ASP   A 155 ? 0.56670 0.49594 0.51521 0.00226  0.05119  -0.04788 155 ASP   A O   
1193 C CB  . ASP   A 155 ? 0.86060 0.78489 0.78661 -0.00061 0.07197  -0.07395 155 ASP   A CB  
1194 C CG  . ASP   A 155 ? 0.91008 0.83296 0.81515 -0.01346 0.06917  -0.08685 155 ASP   A CG  
1195 O OD1 . ASP   A 155 ? 0.94930 0.85439 0.85345 -0.01808 0.07312  -0.09794 155 ASP   A OD1 
1196 O OD2 . ASP   A 155 ? 0.88297 0.82310 0.77328 -0.01934 0.06255  -0.08508 155 ASP   A OD2 
1197 N N   . CYS   A 156 ? 0.58208 0.53473 0.50661 -0.00898 0.04015  -0.04885 156 CYS   A N   
1198 C CA  . CYS   A 156 ? 0.48202 0.43409 0.40949 -0.01318 0.03141  -0.04457 156 CYS   A CA  
1199 C C   . CYS   A 156 ? 0.39135 0.35359 0.32778 -0.00804 0.02417  -0.03057 156 CYS   A C   
1200 O O   . CYS   A 156 ? 0.38062 0.35581 0.31356 -0.00703 0.02098  -0.02539 156 CYS   A O   
1201 C CB  . CYS   A 156 ? 0.44210 0.40212 0.35473 -0.02403 0.02549  -0.05048 156 CYS   A CB  
1202 S SG  . CYS   A 156 ? 0.36076 0.32298 0.27843 -0.02997 0.01571  -0.04563 156 CYS   A SG  
1203 N N   . VAL   A 157 ? 0.28829 0.24421 0.23560 -0.00535 0.02190  -0.02462 157 VAL   A N   
1204 C CA  . VAL   A 157 ? 0.36579 0.33029 0.31880 -0.00236 0.01478  -0.01354 157 VAL   A CA  
1205 C C   . VAL   A 157 ? 0.38885 0.35974 0.33700 -0.00869 0.00776  -0.01288 157 VAL   A C   
1206 O O   . VAL   A 157 ? 0.37255 0.33729 0.32277 -0.01243 0.00720  -0.01459 157 VAL   A O   
1207 C CB  . VAL   A 157 ? 0.35761 0.31481 0.32297 0.00334  0.01568  -0.00662 157 VAL   A CB  
1208 C CG1 . VAL   A 157 ? 0.25268 0.21862 0.22035 0.00470  0.00830  0.00266  157 VAL   A CG1 
1209 C CG2 . VAL   A 157 ? 0.23304 0.18688 0.20671 0.01046  0.02229  -0.00541 157 VAL   A CG2 
1210 N N   . SER   A 158 ? 0.33640 0.32019 0.27989 -0.00976 0.00273  -0.00947 158 SER   A N   
1211 C CA  . SER   A 158 ? 0.33292 0.32533 0.27611 -0.01328 -0.00396 -0.00588 158 SER   A CA  
1212 C C   . SER   A 158 ? 0.27186 0.26485 0.22305 -0.00809 -0.00640 0.00214  158 SER   A C   
1213 O O   . SER   A 158 ? 0.25310 0.25153 0.20565 -0.00454 -0.00842 0.00714  158 SER   A O   
1214 C CB  . SER   A 158 ? 0.31869 0.32434 0.25494 -0.01606 -0.00790 -0.00457 158 SER   A CB  
1215 O OG  . SER   A 158 ? 0.41104 0.41767 0.33671 -0.02195 -0.00588 -0.01261 158 SER   A OG  
1216 N N   . PHE   A 159 ? 0.26871 0.25539 0.22463 -0.00827 -0.00579 0.00311  159 PHE   A N   
1217 C CA  . PHE   A 159 ? 0.25845 0.24681 0.21893 -0.00500 -0.00802 0.00953  159 PHE   A CA  
1218 C C   . PHE   A 159 ? 0.23991 0.23844 0.20053 -0.00655 -0.01201 0.01165  159 PHE   A C   
1219 O O   . PHE   A 159 ? 0.25095 0.25348 0.21193 -0.01131 -0.01312 0.00983  159 PHE   A O   
1220 C CB  . PHE   A 159 ? 0.23434 0.21513 0.19857 -0.00584 -0.00597 0.01082  159 PHE   A CB  
1221 C CG  . PHE   A 159 ? 0.26774 0.23844 0.23530 -0.00281 -0.00208 0.01135  159 PHE   A CG  
1222 C CD1 . PHE   A 159 ? 0.22321 0.19425 0.19385 0.00250  -0.00276 0.01730  159 PHE   A CD1 
1223 C CD2 . PHE   A 159 ? 0.22135 0.18225 0.19007 -0.00543 0.00226  0.00605  159 PHE   A CD2 
1224 C CE1 . PHE   A 159 ? 0.20238 0.16632 0.17893 0.00606  0.00048  0.01966  159 PHE   A CE1 
1225 C CE2 . PHE   A 159 ? 0.23513 0.18605 0.20979 -0.00132 0.00677  0.00739  159 PHE   A CE2 
1226 C CZ  . PHE   A 159 ? 0.23023 0.18359 0.20976 0.00489  0.00578  0.01506  159 PHE   A CZ  
1227 N N   . CYS   A 160 ? 0.18785 0.19029 0.14986 -0.00263 -0.01396 0.01573  160 CYS   A N   
1228 C CA  . CYS   A 160 ? 0.18641 0.19714 0.15127 -0.00233 -0.01658 0.01841  160 CYS   A CA  
1229 C C   . CYS   A 160 ? 0.20473 0.21421 0.17240 0.00099  -0.01595 0.02084  160 CYS   A C   
1230 O O   . CYS   A 160 ? 0.26370 0.27902 0.23555 0.00223  -0.01663 0.02264  160 CYS   A O   
1231 C CB  . CYS   A 160 ? 0.20070 0.21700 0.16506 -0.00103 -0.01888 0.02070  160 CYS   A CB  
1232 S SG  . CYS   A 160 ? 0.16933 0.17993 0.13391 0.00322  -0.01828 0.02273  160 CYS   A SG  
1233 N N   . TYR   A 161 ? 0.18562 0.18846 0.15119 0.00248  -0.01451 0.02109  161 TYR   A N   
1234 C CA  . TYR   A 161 ? 0.17973 0.18199 0.14472 0.00474  -0.01399 0.02213  161 TYR   A CA  
1235 C C   . TYR   A 161 ? 0.19425 0.19229 0.15579 0.00411  -0.01253 0.02331  161 TYR   A C   
1236 O O   . TYR   A 161 ? 0.22797 0.22191 0.18895 0.00405  -0.01288 0.02457  161 TYR   A O   
1237 C CB  . TYR   A 161 ? 0.19774 0.19817 0.16218 0.00713  -0.01582 0.02239  161 TYR   A CB  
1238 C CG  . TYR   A 161 ? 0.18489 0.18303 0.14682 0.00841  -0.01498 0.02118  161 TYR   A CG  
1239 C CD1 . TYR   A 161 ? 0.22200 0.22243 0.18694 0.01008  -0.01257 0.01996  161 TYR   A CD1 
1240 C CD2 . TYR   A 161 ? 0.17781 0.17227 0.13453 0.00778  -0.01641 0.02098  161 TYR   A CD2 
1241 C CE1 . TYR   A 161 ? 0.22466 0.22175 0.18610 0.01126  -0.01022 0.01689  161 TYR   A CE1 
1242 C CE2 . TYR   A 161 ? 0.18473 0.17697 0.13633 0.00763  -0.01559 0.01812  161 TYR   A CE2 
1243 C CZ  . TYR   A 161 ? 0.25776 0.25026 0.21102 0.00947  -0.01183 0.01524  161 TYR   A CZ  
1244 O OH  . TYR   A 161 ? 0.23190 0.22096 0.17935 0.00953  -0.00931 0.01056  161 TYR   A OH  
1245 N N   . MET   A 162 ? 0.21546 0.21532 0.17536 0.00396  -0.01043 0.02369  162 MET   A N   
1246 C CA  . MET   A 162 ? 0.23252 0.23005 0.18671 0.00346  -0.00962 0.02601  162 MET   A CA  
1247 C C   . MET   A 162 ? 0.20671 0.20513 0.15500 0.00466  -0.00906 0.02375  162 MET   A C   
1248 O O   . MET   A 162 ? 0.18821 0.18897 0.13888 0.00614  -0.00670 0.02079  162 MET   A O   
1249 C CB  . MET   A 162 ? 0.20825 0.20696 0.16344 0.00093  -0.00649 0.02863  162 MET   A CB  
1250 C CG  . MET   A 162 ? 0.20251 0.19941 0.15186 0.00016  -0.00614 0.03335  162 MET   A CG  
1251 S SD  . MET   A 162 ? 0.28588 0.28164 0.23963 -0.00341 -0.00264 0.03821  162 MET   A SD  
1252 C CE  . MET   A 162 ? 0.29266 0.27902 0.25183 -0.00278 -0.00455 0.04082  162 MET   A CE  
1253 N N   . HIS   A 163 ? 0.23934 0.23610 0.18042 0.00390  -0.01117 0.02500  163 HIS   A N   
1254 C CA  . HIS   A 163 ? 0.32947 0.32578 0.26260 0.00362  -0.01093 0.02086  163 HIS   A CA  
1255 C C   . HIS   A 163 ? 0.23966 0.23901 0.16398 0.00209  -0.00680 0.02094  163 HIS   A C   
1256 O O   . HIS   A 163 ? 0.23276 0.23432 0.15361 0.00019  -0.00717 0.02681  163 HIS   A O   
1257 C CB  . HIS   A 163 ? 0.25930 0.25420 0.18832 0.00206  -0.01642 0.02149  163 HIS   A CB  
1258 C CG  . HIS   A 163 ? 0.27217 0.26527 0.19192 0.00012  -0.01667 0.01553  163 HIS   A CG  
1259 N ND1 . HIS   A 163 ? 0.24608 0.23456 0.16823 0.00171  -0.01387 0.00887  163 HIS   A ND1 
1260 C CD2 . HIS   A 163 ? 0.27118 0.26609 0.17893 -0.00373 -0.01932 0.01487  163 HIS   A CD2 
1261 C CE1 . HIS   A 163 ? 0.30435 0.28978 0.21624 -0.00114 -0.01397 0.00283  163 HIS   A CE1 
1262 N NE2 . HIS   A 163 ? 0.27476 0.26484 0.17656 -0.00505 -0.01766 0.00599  163 HIS   A NE2 
1263 N N   . HIS   A 164 ? 0.27387 0.27322 0.19525 0.00324  -0.00211 0.01489  164 HIS   A N   
1264 C CA  . HIS   A 164 ? 0.31857 0.32189 0.23148 0.00224  0.00401  0.01372  164 HIS   A CA  
1265 C C   . HIS   A 164 ? 0.33826 0.33886 0.23764 0.00094  0.00585  0.00606  164 HIS   A C   
1266 O O   . HIS   A 164 ? 0.31587 0.32023 0.20161 -0.00213 0.00805  0.00636  164 HIS   A O   
1267 C CB  . HIS   A 164 ? 0.26675 0.27441 0.18998 0.00515  0.01080  0.01292  164 HIS   A CB  
1268 C CG  . HIS   A 164 ? 0.27849 0.29029 0.21206 0.00414  0.00993  0.01962  164 HIS   A CG  
1269 N ND1 . HIS   A 164 ? 0.30941 0.32799 0.24566 0.00262  0.01516  0.02322  164 HIS   A ND1 
1270 C CD2 . HIS   A 164 ? 0.23444 0.24420 0.17603 0.00368  0.00493  0.02254  164 HIS   A CD2 
1271 C CE1 . HIS   A 164 ? 0.24891 0.26844 0.19465 0.00064  0.01271  0.02779  164 HIS   A CE1 
1272 N NE2 . HIS   A 164 ? 0.23668 0.25054 0.18477 0.00136  0.00675  0.02687  164 HIS   A NE2 
1273 N N   . MET   A 165 ? 0.37061 0.36443 0.27263 0.00257  0.00530  -0.00097 165 MET   A N   
1274 C CA  . MET   A 165 ? 0.42114 0.41045 0.31057 0.00105  0.00916  -0.01064 165 MET   A CA  
1275 C C   . MET   A 165 ? 0.38704 0.36649 0.27911 0.00077  0.00580  -0.01713 165 MET   A C   
1276 O O   . MET   A 165 ? 0.37194 0.34841 0.27835 0.00374  0.00327  -0.01450 165 MET   A O   
1277 C CB  . MET   A 165 ? 0.43462 0.42540 0.32627 0.00509  0.02013  -0.01545 165 MET   A CB  
1278 C CG  . MET   A 165 ? 0.38480 0.37322 0.29584 0.01146  0.02324  -0.01577 165 MET   A CG  
1279 S SD  . MET   A 165 ? 0.56134 0.55615 0.47743 0.01646  0.03655  -0.01872 165 MET   A SD  
1280 C CE  . MET   A 165 ? 0.41217 0.41883 0.31867 0.01145  0.03627  -0.01044 165 MET   A CE  
1281 N N   . GLU   A 166 ? 0.42958 0.40407 0.30690 -0.00357 0.00618  -0.02586 166 GLU   A N   
1282 C CA  . GLU   A 166 ? 0.45522 0.41808 0.33428 -0.00479 0.00493  -0.03424 166 GLU   A CA  
1283 C C   . GLU   A 166 ? 0.49115 0.44527 0.36928 -0.00117 0.01594  -0.04548 166 GLU   A C   
1284 O O   . GLU   A 166 ? 0.44301 0.39987 0.30768 -0.00202 0.02289  -0.05097 166 GLU   A O   
1285 C CB  . GLU   A 166 ? 0.39156 0.35402 0.25572 -0.01355 -0.00311 -0.03735 166 GLU   A CB  
1286 C CG  . GLU   A 166 ? 0.43924 0.38869 0.30545 -0.01658 -0.00469 -0.04657 166 GLU   A CG  
1287 C CD  . GLU   A 166 ? 0.44612 0.39816 0.30106 -0.02633 -0.01477 -0.04763 166 GLU   A CD  
1288 O OE1 . GLU   A 166 ? 0.36446 0.32580 0.22607 -0.02759 -0.02327 -0.03667 166 GLU   A OE1 
1289 O OE2 . GLU   A 166 ? 0.43524 0.38070 0.27477 -0.03290 -0.01388 -0.05968 166 GLU   A OE2 
1290 N N   . LEU   A 167 ? 0.43193 0.37598 0.32530 0.00333  0.01823  -0.04803 167 LEU   A N   
1291 C CA  . LEU   A 167 ? 0.46885 0.40234 0.36592 0.00815  0.02912  -0.05820 167 LEU   A CA  
1292 C C   . LEU   A 167 ? 0.53526 0.45456 0.41808 0.00155  0.02934  -0.07207 167 LEU   A C   
1293 O O   . LEU   A 167 ? 0.53592 0.45385 0.41237 -0.00612 0.01942  -0.07156 167 LEU   A O   
1294 C CB  . LEU   A 167 ? 0.46718 0.39638 0.38878 0.01597  0.03068  -0.05258 167 LEU   A CB  
1295 C CG  . LEU   A 167 ? 0.41104 0.35397 0.34758 0.02235  0.03179  -0.04100 167 LEU   A CG  
1296 C CD1 . LEU   A 167 ? 0.41335 0.35249 0.37258 0.02952  0.03316  -0.03587 167 LEU   A CD1 
1297 C CD2 . LEU   A 167 ? 0.51278 0.46350 0.44498 0.02534  0.04160  -0.04383 167 LEU   A CD2 
1298 N N   . PRO   A 168 ? 0.59576 0.50456 0.47381 0.00399  0.04090  -0.08517 168 PRO   A N   
1299 C CA  . PRO   A 168 ? 0.57919 0.47212 0.44248 -0.00352 0.04155  -0.10079 168 PRO   A CA  
1300 C C   . PRO   A 168 ? 0.59017 0.47100 0.46501 -0.00695 0.03348  -0.09988 168 PRO   A C   
1301 O O   . PRO   A 168 ? 0.60408 0.48061 0.46527 -0.01759 0.02596  -0.10613 168 PRO   A O   
1302 C CB  . PRO   A 168 ? 0.54233 0.42363 0.40728 0.00329  0.05780  -0.11368 168 PRO   A CB  
1303 C CG  . PRO   A 168 ? 0.55428 0.45135 0.42541 0.01127  0.06483  -0.10550 168 PRO   A CG  
1304 C CD  . PRO   A 168 ? 0.59402 0.50478 0.48082 0.01344  0.05440  -0.08700 168 PRO   A CD  
1305 N N   . THR   A 169 ? 0.54647 0.42362 0.44647 0.00107  0.03416  -0.09092 169 THR   A N   
1306 C CA  . THR   A 169 ? 0.50636 0.37357 0.41759 -0.00269 0.02654  -0.08799 169 THR   A CA  
1307 C C   . THR   A 169 ? 0.49847 0.37930 0.40623 -0.00979 0.01269  -0.07728 169 THR   A C   
1308 O O   . THR   A 169 ? 0.49078 0.36660 0.40954 -0.01269 0.00649  -0.07266 169 THR   A O   
1309 C CB  . THR   A 169 ? 0.52004 0.38216 0.45819 0.00744  0.03030  -0.07888 169 THR   A CB  
1310 O OG1 . THR   A 169 ? 0.51436 0.39500 0.46112 0.01393  0.02867  -0.06495 169 THR   A OG1 
1311 C CG2 . THR   A 169 ? 0.45765 0.30333 0.40405 0.01496  0.04416  -0.08920 169 THR   A CG2 
1312 N N   . GLY   A 170 ? 0.48773 0.38535 0.38289 -0.01231 0.00810  -0.07215 170 GLY   A N   
1313 C CA  . GLY   A 170 ? 0.41516 0.32463 0.30908 -0.01811 -0.00380 -0.06244 170 GLY   A CA  
1314 C C   . GLY   A 170 ? 0.40247 0.32219 0.31304 -0.01195 -0.00696 -0.04744 170 GLY   A C   
1315 O O   . GLY   A 170 ? 0.40335 0.33394 0.31351 -0.01528 -0.01510 -0.03915 170 GLY   A O   
1316 N N   . VAL   A 171 ? 0.42003 0.33719 0.34558 -0.00326 -0.00081 -0.04365 171 VAL   A N   
1317 C CA  . VAL   A 171 ? 0.35926 0.28769 0.29715 0.00170  -0.00351 -0.03065 171 VAL   A CA  
1318 C C   . VAL   A 171 ? 0.34663 0.28752 0.27738 0.00377  -0.00170 -0.02748 171 VAL   A C   
1319 O O   . VAL   A 171 ? 0.31765 0.25893 0.23521 0.00231  0.00250  -0.03422 171 VAL   A O   
1320 C CB  . VAL   A 171 ? 0.38070 0.30444 0.33714 0.00930  0.00101  -0.02625 171 VAL   A CB  
1321 C CG1 . VAL   A 171 ? 0.42026 0.33153 0.38552 0.00679  -0.00128 -0.02673 171 VAL   A CG1 
1322 C CG2 . VAL   A 171 ? 0.28182 0.20140 0.24038 0.01568  0.01128  -0.03239 171 VAL   A CG2 
1323 N N   . HIS   A 172 ? 0.31419 0.26496 0.25348 0.00676  -0.00428 -0.01740 172 HIS   A N   
1324 C CA  . HIS   A 172 ? 0.29528 0.25715 0.22898 0.00687  -0.00447 -0.01292 172 HIS   A CA  
1325 C C   . HIS   A 172 ? 0.29891 0.26706 0.24425 0.01269  -0.00061 -0.00759 172 HIS   A C   
1326 O O   . HIS   A 172 ? 0.28392 0.25146 0.24214 0.01609  -0.00104 -0.00373 172 HIS   A O   
1327 C CB  . HIS   A 172 ? 0.28529 0.25305 0.21659 0.00289  -0.01227 -0.00666 172 HIS   A CB  
1328 C CG  . HIS   A 172 ? 0.35098 0.31649 0.27144 -0.00359 -0.01708 -0.01057 172 HIS   A CG  
1329 N ND1 . HIS   A 172 ? 0.29792 0.25878 0.22260 -0.00710 -0.02190 -0.01138 172 HIS   A ND1 
1330 C CD2 . HIS   A 172 ? 0.31717 0.28579 0.22258 -0.00806 -0.01822 -0.01345 172 HIS   A CD2 
1331 C CE1 . HIS   A 172 ? 0.31674 0.27838 0.23004 -0.01382 -0.02639 -0.01506 172 HIS   A CE1 
1332 N NE2 . HIS   A 172 ? 0.31964 0.28626 0.22028 -0.01447 -0.02450 -0.01626 172 HIS   A NE2 
1333 N N   . ALA   A 173 ? 0.28391 0.25926 0.22462 0.01309  0.00283  -0.00670 173 ALA   A N   
1334 C CA  . ALA   A 173 ? 0.24485 0.22816 0.19614 0.01713  0.00653  -0.00218 173 ALA   A CA  
1335 C C   . ALA   A 173 ? 0.26532 0.25679 0.21248 0.01421  0.00458  0.00309  173 ALA   A C   
1336 O O   . ALA   A 173 ? 0.24487 0.23660 0.17991 0.01071  0.00412  0.00241  173 ALA   A O   
1337 C CB  . ALA   A 173 ? 0.24358 0.22697 0.19731 0.02122  0.01578  -0.00715 173 ALA   A CB  
1338 N N   . GLY   A 174 ? 0.24233 0.24029 0.19965 0.01520  0.00327  0.00862  174 GLY   A N   
1339 C CA  . GLY   A 174 ? 0.25200 0.25561 0.20785 0.01221  0.00222  0.01302  174 GLY   A CA  
1340 C C   . GLY   A 174 ? 0.19922 0.21032 0.16717 0.01284  0.00184  0.01685  174 GLY   A C   
1341 O O   . GLY   A 174 ? 0.18765 0.20266 0.16544 0.01630  0.00370  0.01711  174 GLY   A O   
1342 N N   . THR   A 175 ? 0.18394 0.19703 0.15168 0.00921  -0.00080 0.02001  175 THR   A N   
1343 C CA  . THR   A 175 ? 0.19854 0.21979 0.17547 0.00737  -0.00108 0.02274  175 THR   A CA  
1344 C C   . THR   A 175 ? 0.19122 0.21065 0.16798 0.00445  -0.00606 0.02350  175 THR   A C   
1345 O O   . THR   A 175 ? 0.17522 0.18732 0.14565 0.00409  -0.00801 0.02279  175 THR   A O   
1346 C CB  . THR   A 175 ? 0.18320 0.20893 0.16061 0.00411  0.00286  0.02470  175 THR   A CB  
1347 O OG1 . THR   A 175 ? 0.18654 0.20541 0.15560 0.00111  0.00215  0.02596  175 THR   A OG1 
1348 C CG2 . THR   A 175 ? 0.18913 0.21886 0.16682 0.00706  0.00929  0.02363  175 THR   A CG2 
1349 N N   . ASP   A 176 ? 0.19196 0.21932 0.17593 0.00202  -0.00782 0.02488  176 ASP   A N   
1350 C CA  . ASP   A 176 ? 0.18645 0.21193 0.16813 -0.00271 -0.01085 0.02389  176 ASP   A CA  
1351 C C   . ASP   A 176 ? 0.18118 0.20122 0.16046 -0.00650 -0.00836 0.02371  176 ASP   A C   
1352 O O   . ASP   A 176 ? 0.17994 0.19997 0.15886 -0.00581 -0.00483 0.02554  176 ASP   A O   
1353 C CB  . ASP   A 176 ? 0.17462 0.21116 0.16274 -0.00596 -0.01427 0.02491  176 ASP   A CB  
1354 C CG  . ASP   A 176 ? 0.21289 0.26014 0.21033 -0.00896 -0.01298 0.02714  176 ASP   A CG  
1355 O OD1 . ASP   A 176 ? 0.23092 0.27537 0.22828 -0.01217 -0.00982 0.02685  176 ASP   A OD1 
1356 O OD2 . ASP   A 176 ? 0.21589 0.27578 0.22228 -0.00825 -0.01532 0.03042  176 ASP   A OD2 
1357 N N   . LEU   A 177 ? 0.18075 0.19544 0.15806 -0.01051 -0.00959 0.02158  177 LEU   A N   
1358 C CA  . LEU   A 177 ? 0.18718 0.19346 0.16361 -0.01352 -0.00703 0.02208  177 LEU   A CA  
1359 C C   . LEU   A 177 ? 0.21125 0.22244 0.19404 -0.01967 -0.00579 0.02292  177 LEU   A C   
1360 O O   . LEU   A 177 ? 0.26020 0.26368 0.24417 -0.02373 -0.00371 0.02341  177 LEU   A O   
1361 C CB  . LEU   A 177 ? 0.19974 0.19592 0.17296 -0.01442 -0.00735 0.01867  177 LEU   A CB  
1362 C CG  . LEU   A 177 ? 0.21664 0.20543 0.18639 -0.00903 -0.00670 0.02059  177 LEU   A CG  
1363 C CD1 . LEU   A 177 ? 0.19481 0.17910 0.16475 -0.00797 -0.00456 0.02620  177 LEU   A CD1 
1364 C CD2 . LEU   A 177 ? 0.20729 0.20168 0.17445 -0.00456 -0.00919 0.02094  177 LEU   A CD2 
1365 N N   . GLU   A 178 ? 0.26785 0.29212 0.25671 -0.02062 -0.00705 0.02380  178 GLU   A N   
1366 C CA  . GLU   A 178 ? 0.24780 0.28024 0.24513 -0.02598 -0.00544 0.02623  178 GLU   A CA  
1367 C C   . GLU   A 178 ? 0.24267 0.28305 0.24359 -0.02139 -0.00113 0.03051  178 GLU   A C   
1368 O O   . GLU   A 178 ? 0.26677 0.31656 0.27622 -0.02474 0.00154  0.03365  178 GLU   A O   
1369 C CB  . GLU   A 178 ? 0.20365 0.24758 0.20732 -0.03174 -0.01020 0.02451  178 GLU   A CB  
1370 N N   . GLY   A 179 ? 0.18513 0.22180 0.17960 -0.01429 0.00014  0.03016  179 GLY   A N   
1371 C CA  . GLY   A 179 ? 0.19576 0.23601 0.18933 -0.01019 0.00556  0.03210  179 GLY   A CA  
1372 C C   . GLY   A 179 ? 0.23067 0.28182 0.23240 -0.00533 0.00737  0.03205  179 GLY   A C   
1373 O O   . GLY   A 179 ? 0.18870 0.24372 0.19088 -0.00212 0.01360  0.03256  179 GLY   A O   
1374 N N   . ASN   A 180 ? 0.23389 0.29055 0.24247 -0.00456 0.00268  0.03190  180 ASN   A N   
1375 C CA  . ASN   A 180 ? 0.18375 0.24969 0.20240 0.00141  0.00410  0.03338  180 ASN   A CA  
1376 C C   . ASN   A 180 ? 0.19664 0.25179 0.20759 0.00755  0.00426  0.03025  180 ASN   A C   
1377 O O   . ASN   A 180 ? 0.23023 0.27785 0.23441 0.00673  -0.00076 0.02892  180 ASN   A O   
1378 C CB  . ASN   A 180 ? 0.17544 0.25375 0.20526 -0.00105 -0.00201 0.03673  180 ASN   A CB  
1379 C CG  . ASN   A 180 ? 0.18453 0.27175 0.21995 -0.01005 -0.00405 0.03839  180 ASN   A CG  
1380 O OD1 . ASN   A 180 ? 0.17571 0.27322 0.22128 -0.01129 0.00032  0.04143  180 ASN   A OD1 
1381 N ND2 . ASN   A 180 ? 0.17523 0.25800 0.20403 -0.01683 -0.01001 0.03581  180 ASN   A ND2 
1382 N N   . PHE   A 181 ? 0.21827 0.27229 0.22996 0.01310  0.01067  0.02849  181 PHE   A N   
1383 C CA  . PHE   A 181 ? 0.20659 0.25002 0.21269 0.01806  0.01101  0.02477  181 PHE   A CA  
1384 C C   . PHE   A 181 ? 0.18062 0.22645 0.19604 0.02079  0.00605  0.02789  181 PHE   A C   
1385 O O   . PHE   A 181 ? 0.17684 0.23517 0.20644 0.02204  0.00509  0.03298  181 PHE   A O   
1386 C CB  . PHE   A 181 ? 0.19369 0.23564 0.20019 0.02325  0.01988  0.02093  181 PHE   A CB  
1387 C CG  . PHE   A 181 ? 0.25882 0.29237 0.24786 0.02079  0.02304  0.01611  181 PHE   A CG  
1388 C CD1 . PHE   A 181 ? 0.27834 0.29933 0.25512 0.02085  0.02073  0.01117  181 PHE   A CD1 
1389 C CD2 . PHE   A 181 ? 0.20593 0.24534 0.19089 0.01748  0.02743  0.01765  181 PHE   A CD2 
1390 C CE1 . PHE   A 181 ? 0.25737 0.27318 0.21769 0.01765  0.02197  0.00790  181 PHE   A CE1 
1391 C CE2 . PHE   A 181 ? 0.23512 0.26865 0.20328 0.01482  0.02936  0.01508  181 PHE   A CE2 
1392 C CZ  . PHE   A 181 ? 0.30145 0.32378 0.25688 0.01490  0.02628  0.01015  181 PHE   A CZ  
1393 N N   . TYR   A 182 ? 0.19904 0.23446 0.20692 0.02110  0.00238  0.02608  182 TYR   A N   
1394 C CA  . TYR   A 182 ? 0.17875 0.21352 0.19490 0.02529  0.00010  0.02904  182 TYR   A CA  
1395 C C   . TYR   A 182 ? 0.18728 0.21770 0.21070 0.03214  0.00723  0.02661  182 TYR   A C   
1396 O O   . TYR   A 182 ? 0.22132 0.24281 0.23551 0.03253  0.01238  0.01974  182 TYR   A O   
1397 C CB  . TYR   A 182 ? 0.17731 0.20211 0.18374 0.02315  -0.00466 0.02779  182 TYR   A CB  
1398 C CG  . TYR   A 182 ? 0.17127 0.20015 0.17221 0.01756  -0.01019 0.02965  182 TYR   A CG  
1399 C CD1 . TYR   A 182 ? 0.18821 0.22634 0.19476 0.01637  -0.01485 0.03496  182 TYR   A CD1 
1400 C CD2 . TYR   A 182 ? 0.20782 0.23141 0.19800 0.01351  -0.01040 0.02619  182 TYR   A CD2 
1401 C CE1 . TYR   A 182 ? 0.19442 0.23537 0.19411 0.01080  -0.01884 0.03468  182 TYR   A CE1 
1402 C CE2 . TYR   A 182 ? 0.20306 0.22824 0.18914 0.00900  -0.01389 0.02659  182 TYR   A CE2 
1403 C CZ  . TYR   A 182 ? 0.24241 0.27584 0.23235 0.00739  -0.01771 0.02976  182 TYR   A CZ  
1404 O OH  . TYR   A 182 ? 0.17754 0.21179 0.16157 0.00244  -0.02018 0.02823  182 TYR   A OH  
1405 N N   . GLY   A 183 ? 0.18809 0.22525 0.22814 0.03750  0.00795  0.03223  183 GLY   A N   
1406 C CA  . GLY   A 183 ? 0.19833 0.23033 0.24828 0.04515  0.01610  0.02982  183 GLY   A CA  
1407 C C   . GLY   A 183 ? 0.20752 0.24720 0.26200 0.04737  0.02458  0.02723  183 GLY   A C   
1408 O O   . GLY   A 183 ? 0.24568 0.29636 0.29782 0.04257  0.02341  0.02900  183 GLY   A O   
1409 N N   . PRO   A 184 ? 0.21494 0.24812 0.27599 0.05444  0.03417  0.02252  184 PRO   A N   
1410 C CA  . PRO   A 184 ? 0.24772 0.29056 0.31649 0.05804  0.04420  0.02092  184 PRO   A CA  
1411 C C   . PRO   A 184 ? 0.30856 0.34400 0.35685 0.05428  0.05063  0.01072  184 PRO   A C   
1412 O O   . PRO   A 184 ? 0.35138 0.38968 0.40250 0.05829  0.06180  0.00635  184 PRO   A O   
1413 C CB  . PRO   A 184 ? 0.23225 0.27065 0.31969 0.06867  0.05240  0.02079  184 PRO   A CB  
1414 C CG  . PRO   A 184 ? 0.26579 0.28179 0.34176 0.06811  0.05025  0.01417  184 PRO   A CG  
1415 C CD  . PRO   A 184 ? 0.24542 0.26144 0.30810 0.05937  0.03724  0.01802  184 PRO   A CD  
1416 N N   . PHE   A 185 ? 0.26541 0.29238 0.29341 0.04686  0.04411  0.00743  185 PHE   A N   
1417 C CA  . PHE   A 185 ? 0.31062 0.33065 0.31789 0.04294  0.04871  -0.00102 185 PHE   A CA  
1418 C C   . PHE   A 185 ? 0.33572 0.36869 0.33879 0.03817  0.04999  0.00291  185 PHE   A C   
1419 O O   . PHE   A 185 ? 0.28043 0.32411 0.29217 0.03518  0.04421  0.01098  185 PHE   A O   
1420 C CB  . PHE   A 185 ? 0.33197 0.33869 0.32159 0.03739  0.04090  -0.00486 185 PHE   A CB  
1421 C CG  . PHE   A 185 ? 0.29686 0.29122 0.29191 0.04050  0.03855  -0.00716 185 PHE   A CG  
1422 C CD1 . PHE   A 185 ? 0.34356 0.32761 0.34236 0.04594  0.04720  -0.01490 185 PHE   A CD1 
1423 C CD2 . PHE   A 185 ? 0.25643 0.24900 0.25361 0.03801  0.02876  -0.00163 185 PHE   A CD2 
1424 C CE1 . PHE   A 185 ? 0.34043 0.31131 0.34600 0.04847  0.04547  -0.01642 185 PHE   A CE1 
1425 C CE2 . PHE   A 185 ? 0.29767 0.27923 0.30080 0.04035  0.02688  -0.00232 185 PHE   A CE2 
1426 C CZ  . PHE   A 185 ? 0.36004 0.33020 0.36808 0.04545  0.03498  -0.00933 185 PHE   A CZ  
1427 N N   . VAL   A 186 ? 0.33747 0.36907 0.32645 0.03677  0.05790  -0.00308 186 VAL   A N   
1428 C CA  . VAL   A 186 ? 0.38597 0.42863 0.36958 0.03197  0.06057  0.00103  186 VAL   A CA  
1429 C C   . VAL   A 186 ? 0.43003 0.46488 0.38834 0.02570  0.05853  -0.00269 186 VAL   A C   
1430 O O   . VAL   A 186 ? 0.48299 0.50600 0.42779 0.02563  0.05828  -0.01076 186 VAL   A O   
1431 C CB  . VAL   A 186 ? 0.42811 0.48216 0.42191 0.03681  0.07392  0.00018  186 VAL   A CB  
1432 C CG1 . VAL   A 186 ? 0.24622 0.31120 0.26807 0.04279  0.07406  0.00655  186 VAL   A CG1 
1433 C CG2 . VAL   A 186 ? 0.44802 0.49201 0.43012 0.04100  0.08456  -0.01179 186 VAL   A CG2 
1434 N N   . ASP   A 187 ? 0.37295 0.41474 0.32569 0.01983  0.05640  0.00402  187 ASP   A N   
1435 C CA  . ASP   A 187 ? 0.40821 0.44529 0.33840 0.01414  0.05426  0.00320  187 ASP   A CA  
1436 C C   . ASP   A 187 ? 0.51045 0.55306 0.42845 0.01391  0.06588  -0.00074 187 ASP   A C   
1437 O O   . ASP   A 187 ? 0.47576 0.52691 0.38775 0.00971  0.06892  0.00554  187 ASP   A O   
1438 C CB  . ASP   A 187 ? 0.38714 0.42660 0.31721 0.00839  0.04650  0.01301  187 ASP   A CB  
1439 C CG  . ASP   A 187 ? 0.40097 0.45164 0.34771 0.00728  0.04900  0.02051  187 ASP   A CG  
1440 O OD1 . ASP   A 187 ? 0.43724 0.49608 0.39785 0.01139  0.05556  0.01924  187 ASP   A OD1 
1441 O OD2 . ASP   A 187 ? 0.36014 0.41132 0.30756 0.00216  0.04430  0.02782  187 ASP   A OD2 
1442 N N   . ARG   A 188 ? 0.54054 0.57757 0.45538 0.01861  0.07328  -0.01154 188 ARG   A N   
1443 C CA  . ARG   A 188 ? 0.63745 0.67654 0.53634 0.01855  0.08519  -0.01928 188 ARG   A CA  
1444 C C   . ARG   A 188 ? 0.72698 0.75148 0.60804 0.01769  0.08429  -0.03212 188 ARG   A C   
1445 O O   . ARG   A 188 ? 0.63344 0.64676 0.52323 0.02077  0.07953  -0.03647 188 ARG   A O   
1446 C CB  . ARG   A 188 ? 0.61406 0.66095 0.52914 0.02605  0.09948  -0.02242 188 ARG   A CB  
1447 C CG  . ARG   A 188 ? 0.62276 0.68681 0.55529 0.02612  0.10288  -0.01109 188 ARG   A CG  
1448 C CD  . ARG   A 188 ? 0.73951 0.81168 0.68809 0.03426  0.11765  -0.01511 188 ARG   A CD  
1449 N NE  . ARG   A 188 ? 0.67143 0.74203 0.64567 0.04267  0.11733  -0.01549 188 ARG   A NE  
1450 C CZ  . ARG   A 188 ? 0.67102 0.74372 0.65913 0.05186  0.13054  -0.02133 188 ARG   A CZ  
1451 N NH1 . ARG   A 188 ? 0.64750 0.72171 0.62356 0.05378  0.14596  -0.03013 188 ARG   A NH1 
1452 N NH2 . ARG   A 188 ? 0.66489 0.73738 0.67868 0.05963  0.12881  -0.01869 188 ARG   A NH2 
1453 N N   . GLN   A 189 ? 1.04312 1.06837 0.89890 0.01281  0.08922  -0.03813 189 GLN   A N   
1454 C CA  . GLN   A 189 ? 1.03788 1.05005 0.87407 0.01035  0.08962  -0.05252 189 GLN   A CA  
1455 C C   . GLN   A 189 ? 1.06178 1.06905 0.90085 0.01704  0.10582  -0.06606 189 GLN   A C   
1456 O O   . GLN   A 189 ? 1.11806 1.12757 0.93737 0.01496  0.11665  -0.07497 189 GLN   A O   
1457 C CB  . GLN   A 189 ? 1.07334 1.08968 0.87916 0.00073  0.08570  -0.05250 189 GLN   A CB  
1458 C CG  . GLN   A 189 ? 1.14393 1.14740 0.93110 -0.00448 0.08023  -0.06505 189 GLN   A CG  
1459 C CD  . GLN   A 189 ? 1.29439 1.30402 1.04857 -0.01398 0.07955  -0.06813 189 GLN   A CD  
1460 O OE1 . GLN   A 189 ? 1.31837 1.34214 1.06424 -0.01751 0.07865  -0.05623 189 GLN   A OE1 
1461 N NE2 . GLN   A 189 ? 1.36852 1.36756 1.10318 -0.01886 0.07999  -0.08409 189 GLN   A NE2 
1462 N N   . THR   A 190 ? 0.86038 0.86159 0.72554 0.02557  0.10786  -0.06675 190 THR   A N   
1463 C CA  . THR   A 190 ? 0.77032 0.76374 0.64540 0.03406  0.12234  -0.07857 190 THR   A CA  
1464 C C   . THR   A 190 ? 0.72808 0.70335 0.61479 0.03715  0.11634  -0.08368 190 THR   A C   
1465 O O   . THR   A 190 ? 0.65349 0.62527 0.54198 0.03302  0.10167  -0.07698 190 THR   A O   
1466 C CB  . THR   A 190 ? 0.74506 0.75286 0.64755 0.04316  0.13233  -0.07048 190 THR   A CB  
1467 O OG1 . THR   A 190 ? 0.67774 0.68743 0.60691 0.04706  0.12225  -0.05897 190 THR   A OG1 
1468 C CG2 . THR   A 190 ? 0.75664 0.78419 0.65191 0.03876  0.13560  -0.06120 190 THR   A CG2 
1469 N N   . ALA   A 191 ? 0.68886 0.65245 0.58500 0.04483  0.12872  -0.09508 191 ALA   A N   
1470 C CA  . ALA   A 191 ? 0.67810 0.62238 0.58599 0.04783  0.12474  -0.10010 191 ALA   A CA  
1471 C C   . ALA   A 191 ? 0.67003 0.62069 0.60797 0.05355  0.11582  -0.08392 191 ALA   A C   
1472 O O   . ALA   A 191 ? 0.71013 0.67267 0.67161 0.06211  0.12217  -0.07587 191 ALA   A O   
1473 C CB  . ALA   A 191 ? 0.54295 0.47217 0.45627 0.05566  0.14183  -0.11566 191 ALA   A CB  
1474 N N   . GLN   A 192 ? 0.64789 0.59274 0.58457 0.04823  0.10096  -0.07868 192 GLN   A N   
1475 C CA  . GLN   A 192 ? 0.69861 0.64661 0.66030 0.05271  0.09244  -0.06543 192 GLN   A CA  
1476 C C   . GLN   A 192 ? 0.68525 0.61530 0.64561 0.04946  0.08417  -0.06885 192 GLN   A C   
1477 O O   . GLN   A 192 ? 0.67515 0.59855 0.61402 0.04017  0.07744  -0.07488 192 GLN   A O   
1478 C CB  . GLN   A 192 ? 0.65291 0.61837 0.61551 0.04824  0.08112  -0.05104 192 GLN   A CB  
1479 C CG  . GLN   A 192 ? 0.59377 0.57633 0.55116 0.04687  0.08600  -0.04714 192 GLN   A CG  
1480 C CD  . GLN   A 192 ? 0.59062 0.58366 0.54393 0.04014  0.07369  -0.03584 192 GLN   A CD  
1481 O OE1 . GLN   A 192 ? 0.52590 0.52426 0.49555 0.04160  0.06614  -0.02601 192 GLN   A OE1 
1482 N NE2 . GLN   A 192 ? 0.64890 0.64466 0.58011 0.03261  0.07163  -0.03704 192 GLN   A NE2 
1483 N N   . ALA   A 193 ? 0.60761 0.53152 0.59191 0.05666  0.08408  -0.06347 193 ALA   A N   
1484 C CA  . ALA   A 193 ? 0.59089 0.49882 0.57694 0.05347  0.07626  -0.06430 193 ALA   A CA  
1485 C C   . ALA   A 193 ? 0.57325 0.49099 0.57654 0.05496  0.06529  -0.04748 193 ALA   A C   
1486 O O   . ALA   A 193 ? 0.57616 0.51083 0.59342 0.05975  0.06486  -0.03634 193 ALA   A O   
1487 C CB  . ALA   A 193 ? 0.63648 0.52314 0.63368 0.05961  0.08660  -0.07425 193 ALA   A CB  
1488 N N   . ALA   A 194 ? 0.52894 0.43603 0.53103 0.05017  0.05668  -0.04617 194 ALA   A N   
1489 C CA  . ALA   A 194 ? 0.46310 0.37975 0.47441 0.04889  0.04538  -0.03167 194 ALA   A CA  
1490 C C   . ALA   A 194 ? 0.45004 0.37006 0.48812 0.05821  0.04713  -0.02027 194 ALA   A C   
1491 O O   . ALA   A 194 ? 0.48175 0.41770 0.52835 0.05901  0.04038  -0.00729 194 ALA   A O   
1492 C CB  . ALA   A 194 ? 0.44130 0.34678 0.44374 0.04076  0.03681  -0.03354 194 ALA   A CB  
1493 N N   . GLY   A 195 ? 0.43536 0.34072 0.48712 0.06511  0.05604  -0.02463 195 GLY   A N   
1494 C CA  . GLY   A 195 ? 0.44773 0.35556 0.52655 0.07389  0.05638  -0.01150 195 GLY   A CA  
1495 C C   . GLY   A 195 ? 0.46972 0.36701 0.55349 0.07059  0.04851  -0.00479 195 GLY   A C   
1496 O O   . GLY   A 195 ? 0.49457 0.39313 0.56309 0.06135  0.03931  -0.00461 195 GLY   A O   
1497 N N   . THR   A 196 ? 0.45470 0.34210 0.56126 0.07839  0.05257  0.00172  196 THR   A N   
1498 C CA  . THR   A 196 ? 0.49869 0.37483 0.61257 0.07568  0.04652  0.00940  196 THR   A CA  
1499 C C   . THR   A 196 ? 0.43673 0.33073 0.54386 0.06923  0.03361  0.02203  196 THR   A C   
1500 O O   . THR   A 196 ? 0.45259 0.36813 0.56470 0.07188  0.02960  0.03295  196 THR   A O   
1501 C CB  . THR   A 196 ? 0.49590 0.36550 0.63981 0.08698  0.05211  0.02041  196 THR   A CB  
1502 O OG1 . THR   A 196 ? 0.51358 0.35800 0.66255 0.09122  0.06460  0.00602  196 THR   A OG1 
1503 C CG2 . THR   A 196 ? 0.52782 0.39503 0.68216 0.08472  0.04361  0.03602  196 THR   A CG2 
1504 N N   . ASP   A 197 ? 0.52241 0.40788 0.61794 0.06021  0.02751  0.01969  197 ASP   A N   
1505 C CA  . ASP   A 197 ? 0.50810 0.40850 0.59845 0.05462  0.01697  0.03121  197 ASP   A CA  
1506 C C   . ASP   A 197 ? 0.55013 0.44594 0.65744 0.05639  0.01422  0.04550  197 ASP   A C   
1507 O O   . ASP   A 197 ? 0.61968 0.49553 0.73916 0.05884  0.01929  0.04385  197 ASP   A O   
1508 C CB  . ASP   A 197 ? 0.49641 0.39472 0.56528 0.04384  0.01176  0.02226  197 ASP   A CB  
1509 C CG  . ASP   A 197 ? 0.50175 0.41940 0.56265 0.03947  0.00319  0.03130  197 ASP   A CG  
1510 O OD1 . ASP   A 197 ? 0.46436 0.39870 0.52869 0.04335  0.00187  0.03879  197 ASP   A OD1 
1511 O OD2 . ASP   A 197 ? 0.52097 0.43722 0.57307 0.03198  -0.00189 0.03067  197 ASP   A OD2 
1512 N N   . THR   A 198 ? 0.47012 0.38423 0.57787 0.05487  0.00657  0.05959  198 THR   A N   
1513 C CA  . THR   A 198 ? 0.47051 0.38447 0.59021 0.05468  0.00262  0.07512  198 THR   A CA  
1514 C C   . THR   A 198 ? 0.48218 0.40465 0.58657 0.04512  -0.00479 0.07756  198 THR   A C   
1515 O O   . THR   A 198 ? 0.42653 0.35760 0.51346 0.04016  -0.00734 0.06929  198 THR   A O   
1516 C CB  . THR   A 198 ? 0.44740 0.37826 0.58376 0.06258  0.00091  0.09233  198 THR   A CB  
1517 O OG1 . THR   A 198 ? 0.36638 0.32112 0.49110 0.06021  -0.00461 0.09450  198 THR   A OG1 
1518 C CG2 . THR   A 198 ? 0.51178 0.43501 0.66700 0.07330  0.00944  0.09053  198 THR   A CG2 
1519 N N   . THR   A 199 ? 0.39397 0.31388 0.50626 0.04286  -0.00751 0.08964  199 THR   A N   
1520 C CA  . THR   A 199 ? 0.39897 0.32852 0.49947 0.03467  -0.01320 0.09378  199 THR   A CA  
1521 C C   . THR   A 199 ? 0.40468 0.35852 0.50152 0.03559  -0.01815 0.10639  199 THR   A C   
1522 O O   . THR   A 199 ? 0.36872 0.33007 0.47840 0.04141  -0.01889 0.11949  199 THR   A O   
1523 C CB  . THR   A 199 ? 0.41319 0.32966 0.52318 0.03058  -0.01321 0.10090  199 THR   A CB  
1524 O OG1 . THR   A 199 ? 0.43419 0.32817 0.54487 0.02751  -0.00938 0.08674  199 THR   A OG1 
1525 C CG2 . THR   A 199 ? 0.38658 0.31563 0.48589 0.02272  -0.01791 0.10609  199 THR   A CG2 
1526 N N   . ILE   A 200 ? 0.34030 0.30642 0.42011 0.02975  -0.02147 0.10235  200 ILE   A N   
1527 C CA  . ILE   A 200 ? 0.34458 0.33282 0.41652 0.02885  -0.02576 0.11037  200 ILE   A CA  
1528 C C   . ILE   A 200 ? 0.36252 0.35733 0.43766 0.02607  -0.02825 0.12594  200 ILE   A C   
1529 O O   . ILE   A 200 ? 0.29915 0.29564 0.36557 0.02004  -0.02863 0.12526  200 ILE   A O   
1530 C CB  . ILE   A 200 ? 0.32331 0.31937 0.37685 0.02405  -0.02688 0.09934  200 ILE   A CB  
1531 C CG1 . ILE   A 200 ? 0.32481 0.31267 0.37496 0.02589  -0.02405 0.08491  200 ILE   A CG1 
1532 C CG2 . ILE   A 200 ? 0.29713 0.31376 0.34231 0.02271  -0.03060 0.10541  200 ILE   A CG2 
1533 C CD1 . ILE   A 200 ? 0.25463 0.24059 0.29075 0.02064  -0.02409 0.07385  200 ILE   A CD1 
1534 N N   . THR   A 201 ? 0.33960 0.34002 0.42788 0.03065  -0.02977 0.14112  201 THR   A N   
1535 C CA  . THR   A 201 ? 0.34442 0.34781 0.43880 0.02853  -0.03133 0.15787  201 THR   A CA  
1536 C C   . THR   A 201 ? 0.31999 0.34186 0.39646 0.02163  -0.03427 0.16149  201 THR   A C   
1537 O O   . THR   A 201 ? 0.31513 0.33471 0.38892 0.01647  -0.03299 0.16489  201 THR   A O   
1538 C CB  . THR   A 201 ? 0.39396 0.40358 0.50461 0.03465  -0.03263 0.17268  201 THR   A CB  
1539 O OG1 . THR   A 201 ? 0.38892 0.38201 0.51674 0.04254  -0.02855 0.16837  201 THR   A OG1 
1540 C CG2 . THR   A 201 ? 0.37806 0.38704 0.49514 0.03142  -0.03194 0.18423  201 THR   A CG2 
1541 N N   . VAL   A 202 ? 0.27030 0.31048 0.33451 0.02098  -0.03761 0.15994  202 VAL   A N   
1542 C CA  . VAL   A 202 ? 0.25065 0.30850 0.29701 0.01461  -0.03959 0.16300  202 VAL   A CA  
1543 C C   . VAL   A 202 ? 0.29441 0.34560 0.32997 0.00963  -0.03557 0.15105  202 VAL   A C   
1544 O O   . VAL   A 202 ? 0.25387 0.31283 0.28186 0.00487  -0.03436 0.15670  202 VAL   A O   
1545 C CB  . VAL   A 202 ? 0.33304 0.40896 0.36790 0.01382  -0.04377 0.15997  202 VAL   A CB  
1546 C CG1 . VAL   A 202 ? 0.23078 0.29947 0.26156 0.01505  -0.04201 0.14181  202 VAL   A CG1 
1547 C CG2 . VAL   A 202 ? 0.31620 0.40951 0.33111 0.00648  -0.04469 0.16046  202 VAL   A CG2 
1548 N N   . ASN   A 203 ? 0.29136 0.32881 0.32755 0.01083  -0.03318 0.13576  203 ASN   A N   
1549 C CA  . ASN   A 203 ? 0.23667 0.26863 0.26583 0.00674  -0.03012 0.12560  203 ASN   A CA  
1550 C C   . ASN   A 203 ? 0.28327 0.30623 0.32274 0.00402  -0.02829 0.13254  203 ASN   A C   
1551 O O   . ASN   A 203 ? 0.22739 0.25608 0.26181 -0.00060 -0.02630 0.13367  203 ASN   A O   
1552 C CB  . ASN   A 203 ? 0.25380 0.27472 0.28167 0.00852  -0.02908 0.10985  203 ASN   A CB  
1553 C CG  . ASN   A 203 ? 0.28990 0.32010 0.30636 0.00933  -0.03012 0.10207  203 ASN   A CG  
1554 O OD1 . ASN   A 203 ? 0.31261 0.35727 0.32150 0.00801  -0.03201 0.10702  203 ASN   A OD1 
1555 N ND2 . ASN   A 203 ? 0.25580 0.27782 0.27061 0.01069  -0.02905 0.08999  203 ASN   A ND2 
1556 N N   . VAL   A 204 ? 0.31100 0.31973 0.36619 0.00670  -0.02832 0.13730  204 VAL   A N   
1557 C CA  . VAL   A 204 ? 0.28566 0.28472 0.35232 0.00309  -0.02682 0.14498  204 VAL   A CA  
1558 C C   . VAL   A 204 ? 0.25628 0.27066 0.32050 -0.00016 -0.02690 0.16115  204 VAL   A C   
1559 O O   . VAL   A 204 ? 0.25427 0.26991 0.31957 -0.00570 -0.02480 0.16459  204 VAL   A O   
1560 C CB  . VAL   A 204 ? 0.25698 0.23722 0.34177 0.00703  -0.02615 0.14858  204 VAL   A CB  
1561 C CG1 . VAL   A 204 ? 0.27994 0.25048 0.37737 0.00222  -0.02477 0.15857  204 VAL   A CG1 
1562 C CG2 . VAL   A 204 ? 0.30600 0.27036 0.39113 0.00866  -0.02473 0.13119  204 VAL   A CG2 
1563 N N   . LEU   A 205 ? 0.27555 0.30351 0.33646 0.00274  -0.02943 0.17192  205 LEU   A N   
1564 C CA  . LEU   A 205 ? 0.26216 0.30767 0.31649 -0.00104 -0.02924 0.18452  205 LEU   A CA  
1565 C C   . LEU   A 205 ? 0.25594 0.31460 0.29204 -0.00598 -0.02687 0.17918  205 LEU   A C   
1566 O O   . LEU   A 205 ? 0.26206 0.32760 0.29657 -0.01064 -0.02360 0.18552  205 LEU   A O   
1567 C CB  . LEU   A 205 ? 0.29816 0.35748 0.35055 0.00196  -0.03258 0.19011  205 LEU   A CB  
1568 C CG  . LEU   A 205 ? 0.27681 0.32591 0.34965 0.00740  -0.03356 0.19747  205 LEU   A CG  
1569 C CD1 . LEU   A 205 ? 0.33174 0.39668 0.40340 0.01030  -0.03747 0.20225  205 LEU   A CD1 
1570 C CD2 . LEU   A 205 ? 0.29122 0.33515 0.37649 0.00499  -0.03126 0.20890  205 LEU   A CD2 
1571 N N   . ALA   A 206 ? 0.24519 0.30709 0.26870 -0.00486 -0.02706 0.16384  206 ALA   A N   
1572 C CA  . ALA   A 206 ? 0.24147 0.31422 0.24904 -0.00851 -0.02331 0.15557  206 ALA   A CA  
1573 C C   . ALA   A 206 ? 0.23836 0.30388 0.25268 -0.01124 -0.01898 0.15116  206 ALA   A C   
1574 O O   . ALA   A 206 ? 0.24109 0.31740 0.24897 -0.01473 -0.01433 0.15276  206 ALA   A O   
1575 C CB  . ALA   A 206 ? 0.23208 0.30592 0.22820 -0.00655 -0.02427 0.14014  206 ALA   A CB  
1576 N N   . TRP   A 207 ? 0.23414 0.28249 0.26163 -0.01004 -0.02027 0.14553  207 TRP   A N   
1577 C CA  . TRP   A 207 ? 0.25182 0.29412 0.28784 -0.01383 -0.01787 0.14242  207 TRP   A CA  
1578 C C   . TRP   A 207 ? 0.27554 0.32120 0.32129 -0.01845 -0.01587 0.15807  207 TRP   A C   
1579 O O   . TRP   A 207 ? 0.29775 0.35161 0.34449 -0.02261 -0.01199 0.15958  207 TRP   A O   
1580 C CB  . TRP   A 207 ? 0.22938 0.25288 0.27480 -0.01262 -0.02061 0.13259  207 TRP   A CB  
1581 C CG  . TRP   A 207 ? 0.31583 0.33133 0.37186 -0.01774 -0.02033 0.12963  207 TRP   A CG  
1582 C CD1 . TRP   A 207 ? 0.30779 0.32859 0.36209 -0.02035 -0.01933 0.12178  207 TRP   A CD1 
1583 C CD2 . TRP   A 207 ? 0.28329 0.28379 0.35445 -0.02128 -0.02159 0.13399  207 TRP   A CD2 
1584 N NE1 . TRP   A 207 ? 0.22971 0.24211 0.29677 -0.02608 -0.02086 0.12165  207 TRP   A NE1 
1585 C CE2 . TRP   A 207 ? 0.29622 0.29488 0.37300 -0.02727 -0.02209 0.12805  207 TRP   A CE2 
1586 C CE3 . TRP   A 207 ? 0.28061 0.26858 0.36239 -0.02002 -0.02227 0.14243  207 TRP   A CE3 
1587 C CZ2 . TRP   A 207 ? 0.32305 0.30764 0.41399 -0.03348 -0.02364 0.12921  207 TRP   A CZ2 
1588 C CZ3 . TRP   A 207 ? 0.37584 0.34745 0.47247 -0.02522 -0.02266 0.14348  207 TRP   A CZ3 
1589 C CH2 . TRP   A 207 ? 0.34423 0.31418 0.44445 -0.03261 -0.02354 0.13623  207 TRP   A CH2 
1590 N N   . LEU   A 208 ? 0.25425 0.29481 0.30847 -0.01754 -0.01800 0.17104  208 LEU   A N   
1591 C CA  . LEU   A 208 ? 0.27967 0.32443 0.34270 -0.02197 -0.01603 0.18871  208 LEU   A CA  
1592 C C   . LEU   A 208 ? 0.30950 0.37729 0.35811 -0.02449 -0.01214 0.19603  208 LEU   A C   
1593 O O   . LEU   A 208 ? 0.30954 0.38416 0.36312 -0.02924 -0.00812 0.20303  208 LEU   A O   
1594 C CB  . LEU   A 208 ? 0.27871 0.31505 0.35297 -0.01874 -0.01884 0.19895  208 LEU   A CB  
1595 C CG  . LEU   A 208 ? 0.31607 0.32723 0.40592 -0.01632 -0.02094 0.19390  208 LEU   A CG  
1596 C CD1 . LEU   A 208 ? 0.29114 0.29568 0.39135 -0.01049 -0.02246 0.19985  208 LEU   A CD1 
1597 C CD2 . LEU   A 208 ? 0.31237 0.31009 0.41609 -0.02321 -0.01925 0.19367  208 LEU   A CD2 
1598 N N   . TYR   A 209 ? 0.27610 0.35613 0.30671 -0.02166 -0.01285 0.19140  209 TYR   A N   
1599 C CA  . TYR   A 209 ? 0.27535 0.37567 0.28943 -0.02442 -0.00795 0.19210  209 TYR   A CA  
1600 C C   . TYR   A 209 ? 0.30682 0.41045 0.31884 -0.02646 -0.00165 0.18269  209 TYR   A C   
1601 O O   . TYR   A 209 ? 0.30037 0.41661 0.31064 -0.03028 0.00471  0.18929  209 TYR   A O   
1602 C CB  . TYR   A 209 ? 0.27926 0.38991 0.27446 -0.02219 -0.01047 0.18622  209 TYR   A CB  
1603 C CG  . TYR   A 209 ? 0.30251 0.42011 0.29807 -0.02180 -0.01468 0.19555  209 TYR   A CG  
1604 C CD1 . TYR   A 209 ? 0.30092 0.43236 0.29187 -0.02553 -0.01195 0.20488  209 TYR   A CD1 
1605 C CD2 . TYR   A 209 ? 0.31077 0.42210 0.31266 -0.01753 -0.02117 0.19581  209 TYR   A CD2 
1606 C CE1 . TYR   A 209 ? 0.36419 0.50342 0.35628 -0.02540 -0.01635 0.21495  209 TYR   A CE1 
1607 C CE2 . TYR   A 209 ? 0.34676 0.46634 0.35157 -0.01702 -0.02500 0.20581  209 TYR   A CE2 
1608 C CZ  . TYR   A 209 ? 0.39154 0.52513 0.39133 -0.02111 -0.02300 0.21572  209 TYR   A CZ  
1609 O OH  . TYR   A 209 ? 0.39063 0.53379 0.39388 -0.02082 -0.02735 0.22701  209 TYR   A OH  
1610 N N   . ALA   A 210 ? 0.29342 0.38661 0.30710 -0.02344 -0.00300 0.16621  210 ALA   A N   
1611 C CA  . ALA   A 210 ? 0.27756 0.37308 0.29442 -0.02438 0.00208  0.15705  210 ALA   A CA  
1612 C C   . ALA   A 210 ? 0.33221 0.42850 0.36607 -0.02944 0.00448  0.16734  210 ALA   A C   
1613 O O   . ALA   A 210 ? 0.31043 0.41950 0.34523 -0.03166 0.01130  0.16882  210 ALA   A O   
1614 C CB  . ALA   A 210 ? 0.24981 0.33216 0.27010 -0.02104 -0.00150 0.14175  210 ALA   A CB  
1615 N N   . ALA   A 211 ? 0.29927 0.38192 0.34777 -0.03149 -0.00043 0.17458  211 ALA   A N   
1616 C CA  . ALA   A 211 ? 0.37604 0.45798 0.44195 -0.03779 0.00128  0.18479  211 ALA   A CA  
1617 C C   . ALA   A 211 ? 0.38201 0.48205 0.44439 -0.04127 0.00765  0.20049  211 ALA   A C   
1618 O O   . ALA   A 211 ? 0.40343 0.51473 0.47267 -0.04536 0.01344  0.20390  211 ALA   A O   
1619 C CB  . ALA   A 211 ? 0.39400 0.45547 0.47484 -0.03941 -0.00452 0.18949  211 ALA   A CB  
1620 N N   . VAL   A 212 ? 0.31781 0.42254 0.36943 -0.03918 0.00652  0.20783  212 VAL   A N   
1621 C CA  . VAL   A 212 ? 0.39897 0.52046 0.44504 -0.04147 0.01151  0.21673  212 VAL   A CA  
1622 C C   . VAL   A 212 ? 0.35926 0.49910 0.39134 -0.04181 0.02024  0.21092  212 VAL   A C   
1623 O O   . VAL   A 212 ? 0.33505 0.48760 0.36973 -0.04504 0.02692  0.21664  212 VAL   A O   
1624 C CB  . VAL   A 212 ? 0.40771 0.53206 0.44406 -0.03887 0.00727  0.22255  212 VAL   A CB  
1625 C CG1 . VAL   A 212 ? 0.33495 0.47965 0.35865 -0.04140 0.01257  0.22964  212 VAL   A CG1 
1626 C CG2 . VAL   A 212 ? 0.35626 0.46455 0.41147 -0.03853 0.00150  0.23123  212 VAL   A CG2 
1627 N N   . ILE   A 213 ? 0.37283 0.51382 0.39086 -0.03822 0.02111  0.19911  213 ILE   A N   
1628 C CA  . ILE   A 213 ? 0.29051 0.44639 0.29587 -0.03729 0.03059  0.19061  213 ILE   A CA  
1629 C C   . ILE   A 213 ? 0.31941 0.47744 0.34311 -0.03844 0.03581  0.18792  213 ILE   A C   
1630 O O   . ILE   A 213 ? 0.39917 0.57336 0.42007 -0.03900 0.04617  0.18819  213 ILE   A O   
1631 C CB  . ILE   A 213 ? 0.36081 0.51131 0.35067 -0.03196 0.02844  0.17261  213 ILE   A CB  
1632 C CG1 . ILE   A 213 ? 0.35696 0.51275 0.32611 -0.03221 0.02491  0.17559  213 ILE   A CG1 
1633 C CG2 . ILE   A 213 ? 0.31160 0.46980 0.29619 -0.02933 0.03800  0.15920  213 ILE   A CG2 
1634 C CD1 . ILE   A 213 ? 0.27697 0.42403 0.23548 -0.02810 0.01996  0.15969  213 ILE   A CD1 
1635 N N   . ASN   A 214 ? 0.28624 0.42942 0.32942 -0.03928 0.02897  0.18598  214 ASN   A N   
1636 C CA  . ASN   A 214 ? 0.35212 0.49741 0.41493 -0.04132 0.03102  0.18358  214 ASN   A CA  
1637 C C   . ASN   A 214 ? 0.42694 0.57443 0.51001 -0.04911 0.03109  0.19874  214 ASN   A C   
1638 O O   . ASN   A 214 ? 0.40933 0.55774 0.51112 -0.05232 0.03036  0.19728  214 ASN   A O   
1639 C CB  . ASN   A 214 ? 0.29219 0.42177 0.36176 -0.03868 0.02314  0.17019  214 ASN   A CB  
1640 C CG  . ASN   A 214 ? 0.36475 0.49630 0.42191 -0.03169 0.02581  0.15503  214 ASN   A CG  
1641 O OD1 . ASN   A 214 ? 0.28443 0.40579 0.32884 -0.02780 0.02137  0.14652  214 ASN   A OD1 
1642 N ND2 . ASN   A 214 ? 0.45074 0.59392 0.51628 -0.03020 0.03235  0.15163  214 ASN   A ND2 
1643 N N   . GLY   A 215 ? 0.42541 0.57447 0.50589 -0.05227 0.03144  0.21252  215 GLY   A N   
1644 C CA  . GLY   A 215 ? 0.45628 0.60783 0.55386 -0.05814 0.03219  0.22295  215 GLY   A CA  
1645 C C   . GLY   A 215 ? 0.55608 0.68737 0.66669 -0.06165 0.02341  0.22880  215 GLY   A C   
1646 O O   . GLY   A 215 ? 0.64941 0.78203 0.76744 -0.06511 0.02410  0.23946  215 GLY   A O   
1647 N N   . ASP   A 216 ? 0.70245 0.81403 0.81547 -0.06043 0.01578  0.22205  216 ASP   A N   
1648 C CA  . ASP   A 216 ? 0.77513 0.86632 0.90031 -0.06289 0.00933  0.22675  216 ASP   A CA  
1649 C C   . ASP   A 216 ? 0.76243 0.85463 0.87767 -0.05865 0.00904  0.23503  216 ASP   A C   
1650 O O   . ASP   A 216 ? 0.73920 0.83977 0.83581 -0.05313 0.00980  0.23275  216 ASP   A O   
1651 C CB  . ASP   A 216 ? 0.77916 0.84614 0.90937 -0.06221 0.00186  0.21793  216 ASP   A CB  
1652 C CG  . ASP   A 216 ? 0.85187 0.91402 0.99234 -0.06705 -0.00081 0.20786  216 ASP   A CG  
1653 O OD1 . ASP   A 216 ? 0.96896 1.04674 1.11618 -0.07115 0.00278  0.20943  216 ASP   A OD1 
1654 O OD2 . ASP   A 216 ? 0.79979 0.84138 0.94443 -0.06737 -0.00706 0.19773  216 ASP   A OD2 
1655 N N   . ARG   A 217 ? 0.53977 0.62547 0.66767 -0.06189 0.00803  0.24487  217 ARG   A N   
1656 C CA  . ARG   A 217 ? 0.44663 0.53445 0.56835 -0.05828 0.00718  0.25459  217 ARG   A CA  
1657 C C   . ARG   A 217 ? 0.48347 0.55192 0.62341 -0.05990 0.00351  0.26187  217 ARG   A C   
1658 O O   . ARG   A 217 ? 0.49005 0.56008 0.62891 -0.05697 0.00255  0.27189  217 ARG   A O   
1659 C CB  . ARG   A 217 ? 0.47833 0.58962 0.59112 -0.06009 0.01351  0.26321  217 ARG   A CB  
1660 C CG  . ARG   A 217 ? 0.50293 0.62602 0.59768 -0.05570 0.01324  0.26845  217 ARG   A CG  
1661 C CD  . ARG   A 217 ? 0.43314 0.57959 0.51665 -0.05838 0.02041  0.27556  217 ARG   A CD  
1662 N NE  . ARG   A 217 ? 0.45358 0.60640 0.53011 -0.05711 0.01804  0.28694  217 ARG   A NE  
1663 C CZ  . ARG   A 217 ? 0.47356 0.63462 0.53086 -0.05335 0.01564  0.28417  217 ARG   A CZ  
1664 N NH1 . ARG   A 217 ? 0.43850 0.60640 0.49252 -0.05295 0.01260  0.29609  217 ARG   A NH1 
1665 N NH2 . ARG   A 217 ? 0.44199 0.60462 0.48429 -0.05038 0.01585  0.26982  217 ARG   A NH2 
1666 N N   . TRP   A 218 ? 0.50283 0.55219 0.65907 -0.06435 0.00118  0.25614  218 TRP   A N   
1667 C CA  . TRP   A 218 ? 0.39235 0.42102 0.56680 -0.06704 -0.00098 0.26121  218 TRP   A CA  
1668 C C   . TRP   A 218 ? 0.47207 0.48433 0.64671 -0.05954 -0.00440 0.26048  218 TRP   A C   
1669 O O   . TRP   A 218 ? 0.46911 0.46860 0.65699 -0.05954 -0.00473 0.26856  218 TRP   A O   
1670 C CB  . TRP   A 218 ? 0.39974 0.41270 0.58831 -0.07474 -0.00277 0.25178  218 TRP   A CB  
1671 C CG  . TRP   A 218 ? 0.52506 0.52290 0.70996 -0.07299 -0.00679 0.23547  218 TRP   A CG  
1672 C CD1 . TRP   A 218 ? 0.49666 0.50318 0.67500 -0.07478 -0.00749 0.22565  218 TRP   A CD1 
1673 C CD2 . TRP   A 218 ? 0.52034 0.49185 0.70936 -0.06955 -0.01011 0.22755  218 TRP   A CD2 
1674 N NE1 . TRP   A 218 ? 0.51914 0.50683 0.69631 -0.07335 -0.01175 0.21280  218 TRP   A NE1 
1675 C CE2 . TRP   A 218 ? 0.55116 0.51702 0.73420 -0.06996 -0.01301 0.21298  218 TRP   A CE2 
1676 C CE3 . TRP   A 218 ? 0.48514 0.43777 0.68284 -0.06572 -0.01030 0.23144  218 TRP   A CE3 
1677 C CZ2 . TRP   A 218 ? 0.54347 0.48536 0.72742 -0.06690 -0.01584 0.20145  218 TRP   A CZ2 
1678 C CZ3 . TRP   A 218 ? 0.53398 0.46261 0.73366 -0.06192 -0.01235 0.21954  218 TRP   A CZ3 
1679 C CH2 . TRP   A 218 ? 0.52339 0.44688 0.71551 -0.06266 -0.01495 0.20434  218 TRP   A CH2 
1680 N N   . PHE   A 219 ? 0.42120 0.43414 0.58263 -0.05293 -0.00651 0.25158  219 PHE   A N   
1681 C CA  . PHE   A 219 ? 0.42146 0.41815 0.58562 -0.04563 -0.00948 0.24903  219 PHE   A CA  
1682 C C   . PHE   A 219 ? 0.40327 0.41335 0.56155 -0.03929 -0.01007 0.26063  219 PHE   A C   
1683 O O   . PHE   A 219 ? 0.40431 0.40421 0.56674 -0.03260 -0.01230 0.26017  219 PHE   A O   
1684 C CB  . PHE   A 219 ? 0.35015 0.34016 0.50484 -0.04180 -0.01181 0.23385  219 PHE   A CB  
1685 C CG  . PHE   A 219 ? 0.44051 0.45243 0.57602 -0.04105 -0.01103 0.23011  219 PHE   A CG  
1686 C CD1 . PHE   A 219 ? 0.41719 0.44443 0.53749 -0.03491 -0.01176 0.23257  219 PHE   A CD1 
1687 C CD2 . PHE   A 219 ? 0.46813 0.48605 0.60145 -0.04691 -0.00941 0.22395  219 PHE   A CD2 
1688 C CE1 . PHE   A 219 ? 0.40740 0.45293 0.50906 -0.03459 -0.01032 0.22753  219 PHE   A CE1 
1689 C CE2 . PHE   A 219 ? 0.44872 0.48590 0.56515 -0.04551 -0.00738 0.22024  219 PHE   A CE2 
1690 C CZ  . PHE   A 219 ? 0.41079 0.46067 0.51049 -0.03937 -0.00751 0.22141  219 PHE   A CZ  
1691 N N   . LEU   A 220 ? 0.42645 0.45950 0.57597 -0.04148 -0.00806 0.27100  220 LEU   A N   
1692 C CA  . LEU   A 220 ? 0.45416 0.50278 0.59636 -0.03705 -0.00944 0.28203  220 LEU   A CA  
1693 C C   . LEU   A 220 ? 0.45246 0.49405 0.61258 -0.03702 -0.00959 0.29742  220 LEU   A C   
1694 O O   . LEU   A 220 ? 0.44293 0.46793 0.62002 -0.04107 -0.00794 0.29949  220 LEU   A O   
1695 C CB  . LEU   A 220 ? 0.42395 0.49979 0.54687 -0.04000 -0.00677 0.28526  220 LEU   A CB  
1696 C CG  . LEU   A 220 ? 0.44629 0.53028 0.55141 -0.04003 -0.00536 0.27085  220 LEU   A CG  
1697 C CD1 . LEU   A 220 ? 0.44311 0.55259 0.52933 -0.04272 -0.00119 0.27374  220 LEU   A CD1 
1698 C CD2 . LEU   A 220 ? 0.42221 0.50087 0.51948 -0.03356 -0.00972 0.26102  220 LEU   A CD2 
1699 N N   . ASN   A 221 ? 0.48689 0.54172 0.64343 -0.03285 -0.01181 0.30845  221 ASN   A N   
1700 C CA  . ASN   A 221 ? 0.59041 0.64154 0.76376 -0.03177 -0.01228 0.32507  221 ASN   A CA  
1701 C C   . ASN   A 221 ? 0.58105 0.65829 0.74293 -0.03034 -0.01451 0.33808  221 ASN   A C   
1702 O O   . ASN   A 221 ? 0.51495 0.60974 0.65607 -0.02979 -0.01595 0.33191  221 ASN   A O   
1703 C CB  . ASN   A 221 ? 0.60867 0.63475 0.80078 -0.02553 -0.01374 0.32225  221 ASN   A CB  
1704 C CG  . ASN   A 221 ? 0.59206 0.62001 0.77651 -0.01785 -0.01708 0.31338  221 ASN   A CG  
1705 O OD1 . ASN   A 221 ? 0.60961 0.65892 0.77567 -0.01709 -0.01937 0.31216  221 ASN   A OD1 
1706 N ND2 . ASN   A 221 ? 0.59019 0.59467 0.78830 -0.01268 -0.01685 0.30566  221 ASN   A ND2 
1707 N N   . ARG   A 222 ? 0.63877 0.71893 0.81372 -0.03064 -0.01473 0.35638  222 ARG   A N   
1708 C CA  . ARG   A 222 ? 0.64740 0.75204 0.81250 -0.02906 -0.01807 0.36898  222 ARG   A CA  
1709 C C   . ARG   A 222 ? 0.67126 0.77218 0.84560 -0.02111 -0.02272 0.37102  222 ARG   A C   
1710 O O   . ARG   A 222 ? 0.71621 0.83818 0.88242 -0.01976 -0.02669 0.37987  222 ARG   A O   
1711 C CB  . ARG   A 222 ? 0.67093 0.78845 0.84149 -0.03333 -0.01682 0.39007  222 ARG   A CB  
1712 C CG  . ARG   A 222 ? 0.68228 0.79231 0.87776 -0.03038 -0.01821 0.40970  222 ARG   A CG  
1713 C CD  . ARG   A 222 ? 0.69690 0.77943 0.91579 -0.03170 -0.01451 0.41057  222 ARG   A CD  
1714 N NE  . ARG   A 222 ? 0.71581 0.79115 0.95800 -0.02996 -0.01456 0.43001  222 ARG   A NE  
1715 C CZ  . ARG   A 222 ? 0.74443 0.80096 1.00730 -0.02300 -0.01551 0.43206  222 ARG   A CZ  
1716 N NH1 . ARG   A 222 ? 0.76381 0.80571 1.02687 -0.01750 -0.01620 0.41512  222 ARG   A NH1 
1717 N NH2 . ARG   A 222 ? 0.82741 0.87817 1.11166 -0.02158 -0.01496 0.45059  222 ARG   A NH2 
1718 N N   . PHE   A 223 ? 0.73056 0.80635 0.92057 -0.01613 -0.02218 0.36204  223 PHE   A N   
1719 C CA  . PHE   A 223 ? 0.69305 0.76614 0.89116 -0.00798 -0.02560 0.36173  223 PHE   A CA  
1720 C C   . PHE   A 223 ? 0.67398 0.76666 0.84996 -0.00703 -0.02944 0.35283  223 PHE   A C   
1721 O O   . PHE   A 223 ? 0.63806 0.73735 0.79381 -0.01131 -0.02851 0.34088  223 PHE   A O   
1722 C CB  . PHE   A 223 ? 0.69248 0.73473 0.90660 -0.00321 -0.02309 0.34925  223 PHE   A CB  
1723 C CG  . PHE   A 223 ? 0.82189 0.84140 1.05850 -0.00424 -0.01927 0.35593  223 PHE   A CG  
1724 C CD1 . PHE   A 223 ? 0.88020 0.90116 1.13506 -0.00156 -0.01951 0.37500  223 PHE   A CD1 
1725 C CD2 . PHE   A 223 ? 0.83423 0.83102 1.07406 -0.00858 -0.01560 0.34333  223 PHE   A CD2 
1726 C CE1 . PHE   A 223 ? 0.92692 0.92521 1.20280 -0.00284 -0.01566 0.38073  223 PHE   A CE1 
1727 C CE2 . PHE   A 223 ? 0.87852 0.85323 1.13846 -0.01077 -0.01219 0.34827  223 PHE   A CE2 
1728 C CZ  . PHE   A 223 ? 0.92436 0.89898 1.20226 -0.00776 -0.01196 0.36674  223 PHE   A CZ  
1729 N N   . THR   A 224 ? 0.63376 0.73617 0.81469 -0.00162 -0.03366 0.35927  224 THR   A N   
1730 C CA  . THR   A 224 ? 0.53001 0.64478 0.69581 0.00048  -0.03753 0.34896  224 THR   A CA  
1731 C C   . THR   A 224 ? 0.58281 0.68634 0.76858 0.00930  -0.03874 0.34926  224 THR   A C   
1732 O O   . THR   A 224 ? 0.66527 0.75312 0.87478 0.01357  -0.03636 0.35795  224 THR   A O   
1733 C CB  . THR   A 224 ? 0.54346 0.68985 0.69072 -0.00397 -0.04215 0.35768  224 THR   A CB  
1734 O OG1 . THR   A 224 ? 0.52042 0.67658 0.64811 -0.00446 -0.04498 0.34326  224 THR   A OG1 
1735 C CG2 . THR   A 224 ? 0.47540 0.63438 0.63861 -0.00068 -0.04633 0.37771  224 THR   A CG2 
1736 N N   . THR   A 225 ? 0.56398 0.67501 0.74085 0.01212  -0.04186 0.33948  225 THR   A N   
1737 C CA  . THR   A 225 ? 0.53292 0.63597 0.72872 0.02077  -0.04246 0.33983  225 THR   A CA  
1738 C C   . THR   A 225 ? 0.48647 0.61142 0.66992 0.02119  -0.04806 0.33671  225 THR   A C   
1739 O O   . THR   A 225 ? 0.50246 0.64203 0.66139 0.01509  -0.05056 0.32896  225 THR   A O   
1740 C CB  . THR   A 225 ? 0.52361 0.59621 0.72902 0.02546  -0.03723 0.32414  225 THR   A CB  
1741 O OG1 . THR   A 225 ? 0.57908 0.64197 0.80726 0.03457  -0.03597 0.32724  225 THR   A OG1 
1742 C CG2 . THR   A 225 ? 0.43485 0.50710 0.61989 0.02360  -0.03773 0.30494  225 THR   A CG2 
1743 N N   . THR   A 226 ? 0.49300 0.62062 0.69453 0.02817  -0.04978 0.34339  226 THR   A N   
1744 C CA  . THR   A 226 ? 0.56504 0.71202 0.75838 0.02866  -0.05508 0.34016  226 THR   A CA  
1745 C C   . THR   A 226 ? 0.52360 0.65577 0.71190 0.03194  -0.05268 0.31990  226 THR   A C   
1746 O O   . THR   A 226 ? 0.47113 0.57738 0.66855 0.03599  -0.04693 0.31087  226 THR   A O   
1747 C CB  . THR   A 226 ? 0.56667 0.72491 0.78312 0.03481  -0.05786 0.35644  226 THR   A CB  
1748 O OG1 . THR   A 226 ? 0.58007 0.71401 0.82251 0.04434  -0.05193 0.35530  226 THR   A OG1 
1749 C CG2 . THR   A 226 ? 0.46144 0.63699 0.68313 0.03141  -0.06102 0.37847  226 THR   A CG2 
1750 N N   . LEU   A 227 ? 0.52217 0.67127 0.69537 0.02953  -0.05731 0.31269  227 LEU   A N   
1751 C CA  . LEU   A 227 ? 0.55560 0.69365 0.72502 0.03285  -0.05562 0.29508  227 LEU   A CA  
1752 C C   . LEU   A 227 ? 0.55043 0.67300 0.74651 0.04322  -0.05165 0.29591  227 LEU   A C   
1753 O O   . LEU   A 227 ? 0.55616 0.65524 0.75655 0.04742  -0.04616 0.28327  227 LEU   A O   
1754 C CB  . LEU   A 227 ? 0.56802 0.72858 0.71993 0.02832  -0.06171 0.28958  227 LEU   A CB  
1755 C CG  . LEU   A 227 ? 0.50744 0.65819 0.65048 0.02976  -0.06020 0.27060  227 LEU   A CG  
1756 C CD1 . LEU   A 227 ? 0.46009 0.59011 0.59244 0.02800  -0.05513 0.25848  227 LEU   A CD1 
1757 C CD2 . LEU   A 227 ? 0.49633 0.66909 0.62000 0.02336  -0.06632 0.26484  227 LEU   A CD2 
1758 N N   . ASN   A 228 ? 0.51303 0.64892 0.72737 0.04739  -0.05405 0.31082  228 ASN   A N   
1759 C CA  . ASN   A 228 ? 0.55337 0.67560 0.79535 0.05795  -0.04919 0.31327  228 ASN   A CA  
1760 C C   . ASN   A 228 ? 0.56227 0.65296 0.81621 0.06204  -0.04120 0.30885  228 ASN   A C   
1761 O O   . ASN   A 228 ? 0.56362 0.63332 0.82546 0.06816  -0.03528 0.29613  228 ASN   A O   
1762 C CB  . ASN   A 228 ? 0.66481 0.80607 0.92661 0.06105  -0.05258 0.33431  228 ASN   A CB  
1763 C CG  . ASN   A 228 ? 0.69731 0.86433 0.95725 0.06049  -0.05874 0.33633  228 ASN   A CG  
1764 O OD1 . ASN   A 228 ? 0.68193 0.84739 0.93399 0.06119  -0.05839 0.32175  228 ASN   A OD1 
1765 N ND2 . ASN   A 228 ? 0.73486 0.92593 1.00343 0.05906  -0.06447 0.35518  228 ASN   A ND2 
1766 N N   . ASP   A 229 ? 0.53111 0.61811 0.78593 0.05807  -0.04082 0.31875  229 ASP   A N   
1767 C CA  . ASP   A 229 ? 0.52603 0.58319 0.79429 0.06097  -0.03363 0.31594  229 ASP   A CA  
1768 C C   . ASP   A 229 ? 0.54891 0.58644 0.80086 0.05740  -0.03043 0.29610  229 ASP   A C   
1769 O O   . ASP   A 229 ? 0.55208 0.56189 0.81452 0.06103  -0.02395 0.28692  229 ASP   A O   
1770 C CB  . ASP   A 229 ? 0.51061 0.57037 0.78442 0.05678  -0.03434 0.33264  229 ASP   A CB  
1771 C CG  . ASP   A 229 ? 0.52967 0.60159 0.82685 0.06204  -0.03574 0.35366  229 ASP   A CG  
1772 O OD1 . ASP   A 229 ? 0.49986 0.56895 0.81576 0.07074  -0.03348 0.35450  229 ASP   A OD1 
1773 O OD2 . ASP   A 229 ? 0.51672 0.60174 0.81416 0.05750  -0.03884 0.37005  229 ASP   A OD2 
1774 N N   . PHE   A 230 ? 0.55709 0.60821 0.78354 0.04994  -0.03467 0.28920  230 PHE   A N   
1775 C CA  . PHE   A 230 ? 0.52870 0.56301 0.74076 0.04670  -0.03195 0.27150  230 PHE   A CA  
1776 C C   . PHE   A 230 ? 0.52541 0.54625 0.74213 0.05346  -0.02868 0.25682  230 PHE   A C   
1777 O O   . PHE   A 230 ? 0.54411 0.53959 0.76422 0.05491  -0.02337 0.24490  230 PHE   A O   
1778 C CB  . PHE   A 230 ? 0.49190 0.54441 0.67667 0.03812  -0.03652 0.26721  230 PHE   A CB  
1779 C CG  . PHE   A 230 ? 0.50787 0.54567 0.67893 0.03528  -0.03413 0.24999  230 PHE   A CG  
1780 C CD1 . PHE   A 230 ? 0.48197 0.50406 0.65191 0.03063  -0.03087 0.24757  230 PHE   A CD1 
1781 C CD2 . PHE   A 230 ? 0.43218 0.47157 0.59357 0.03722  -0.03510 0.23686  230 PHE   A CD2 
1782 C CE1 . PHE   A 230 ? 0.42949 0.43899 0.58857 0.02773  -0.02907 0.23282  230 PHE   A CE1 
1783 C CE2 . PHE   A 230 ? 0.43429 0.46043 0.58457 0.03486  -0.03308 0.22236  230 PHE   A CE2 
1784 C CZ  . PHE   A 230 ? 0.45178 0.46320 0.60094 0.03009  -0.03021 0.22046  230 PHE   A CZ  
1785 N N   . ASN   A 231 ? 0.55898 0.59713 0.77605 0.05715  -0.03173 0.25747  231 ASN   A N   
1786 C CA  . ASN   A 231 ? 0.52511 0.55371 0.74665 0.06370  -0.02835 0.24422  231 ASN   A CA  
1787 C C   . ASN   A 231 ? 0.53391 0.53786 0.77949 0.07237  -0.02033 0.24241  231 ASN   A C   
1788 O O   . ASN   A 231 ? 0.56727 0.55294 0.81414 0.07639  -0.01492 0.22738  231 ASN   A O   
1789 C CB  . ASN   A 231 ? 0.45414 0.50830 0.67492 0.06551  -0.03323 0.24803  231 ASN   A CB  
1790 C CG  . ASN   A 231 ? 0.47000 0.54381 0.66452 0.05698  -0.03989 0.24338  231 ASN   A CG  
1791 O OD1 . ASN   A 231 ? 0.49436 0.55982 0.67150 0.05217  -0.03938 0.23226  231 ASN   A OD1 
1792 N ND2 . ASN   A 231 ? 0.52496 0.62495 0.71689 0.05475  -0.04604 0.25174  231 ASN   A ND2 
1793 N N   . LEU   A 232 ? 0.51940 0.52201 0.78378 0.07515  -0.01898 0.25709  232 LEU   A N   
1794 C CA  . LEU   A 232 ? 0.55025 0.52794 0.83796 0.08319  -0.01058 0.25523  232 LEU   A CA  
1795 C C   . LEU   A 232 ? 0.56590 0.51273 0.84890 0.08003  -0.00515 0.24106  232 LEU   A C   
1796 O O   . LEU   A 232 ? 0.52028 0.44345 0.81228 0.08550  0.00247  0.22817  232 LEU   A O   
1797 C CB  . LEU   A 232 ? 0.53564 0.51893 0.84407 0.08584  -0.01082 0.27553  232 LEU   A CB  
1798 C CG  . LEU   A 232 ? 0.50831 0.50745 0.83784 0.09431  -0.01081 0.28811  232 LEU   A CG  
1799 C CD1 . LEU   A 232 ? 0.47456 0.50663 0.79089 0.09104  -0.01924 0.29266  232 LEU   A CD1 
1800 C CD2 . LEU   A 232 ? 0.46563 0.46625 0.81657 0.09653  -0.01046 0.30856  232 LEU   A CD2 
1801 N N   . VAL   A 233 ? 0.57700 0.52420 0.84591 0.07067  -0.00871 0.24302  233 VAL   A N   
1802 C CA  . VAL   A 233 ? 0.57858 0.49922 0.84192 0.06559  -0.00485 0.23012  233 VAL   A CA  
1803 C C   . VAL   A 233 ? 0.61590 0.53140 0.86187 0.06387  -0.00461 0.21142  233 VAL   A C   
1804 O O   . VAL   A 233 ? 0.61702 0.50687 0.86388 0.06394  0.00086  0.19615  233 VAL   A O   
1805 C CB  . VAL   A 233 ? 0.58007 0.50588 0.83579 0.05603  -0.00854 0.23979  233 VAL   A CB  
1806 C CG1 . VAL   A 233 ? 0.49630 0.39563 0.74784 0.04946  -0.00504 0.22697  233 VAL   A CG1 
1807 C CG2 . VAL   A 233 ? 0.51848 0.45000 0.79246 0.05808  -0.00865 0.25951  233 VAL   A CG2 
1808 N N   . ALA   A 234 ? 0.75172 0.69126 0.98127 0.06172  -0.01054 0.21206  234 ALA   A N   
1809 C CA  . ALA   A 234 ? 0.75881 0.69610 0.97206 0.06012  -0.01093 0.19629  234 ALA   A CA  
1810 C C   . ALA   A 234 ? 0.75932 0.67984 0.98236 0.06839  -0.00418 0.18311  234 ALA   A C   
1811 O O   . ALA   A 234 ? 0.79014 0.68735 1.01003 0.06702  0.00045  0.16789  234 ALA   A O   
1812 C CB  . ALA   A 234 ? 0.74345 0.71070 0.94055 0.05765  -0.01803 0.20054  234 ALA   A CB  
1813 N N   . MET   A 235 ? 0.62840 0.56038 0.86456 0.07666  -0.00296 0.18894  235 MET   A N   
1814 C CA  . MET   A 235 ? 0.61413 0.53496 0.85838 0.08483  0.00409  0.17641  235 MET   A CA  
1815 C C   . MET   A 235 ? 0.62712 0.51485 0.88126 0.08692  0.01313  0.16512  235 MET   A C   
1816 O O   . MET   A 235 ? 0.60284 0.47516 0.85356 0.08944  0.01929  0.14796  235 MET   A O   
1817 C CB  . MET   A 235 ? 0.66936 0.60953 0.92915 0.09286  0.00410  0.18686  235 MET   A CB  
1818 C CG  . MET   A 235 ? 0.79672 0.72956 1.06710 0.10189  0.01214  0.17613  235 MET   A CG  
1819 S SD  . MET   A 235 ? 1.05436 1.01620 1.34307 0.10940  0.01019  0.19147  235 MET   A SD  
1820 C CE  . MET   A 235 ? 0.72879 0.69116 1.03900 0.11171  0.00980  0.21144  235 MET   A CE  
1821 N N   . LYS   A 236 ? 0.62986 0.50596 0.89469 0.08493  0.01419  0.17335  236 LYS   A N   
1822 C CA  . LYS   A 236 ? 0.60421 0.44684 0.87589 0.08459  0.02227  0.16078  236 LYS   A CA  
1823 C C   . LYS   A 236 ? 0.61898 0.44552 0.87175 0.07624  0.02233  0.14279  236 LYS   A C   
1824 O O   . LYS   A 236 ? 0.60249 0.40772 0.85327 0.07770  0.02952  0.12406  236 LYS   A O   
1825 C CB  . LYS   A 236 ? 0.57150 0.40623 0.85589 0.08174  0.02189  0.17389  236 LYS   A CB  
1826 C CG  . LYS   A 236 ? 0.53213 0.33204 0.82230 0.07960  0.02945  0.16046  236 LYS   A CG  
1827 C CD  . LYS   A 236 ? 0.64547 0.43780 0.94337 0.07329  0.02750  0.17236  236 LYS   A CD  
1828 C CE  . LYS   A 236 ? 0.66741 0.43038 0.95836 0.06371  0.03027  0.15654  236 LYS   A CE  
1829 N NZ  . LYS   A 236 ? 0.70334 0.43515 1.00680 0.06759  0.04001  0.14368  236 LYS   A NZ  
1830 N N   . TYR   A 237 ? 0.62017 0.45823 0.85830 0.06714  0.01455  0.14793  237 TYR   A N   
1831 C CA  . TYR   A 237 ? 0.59722 0.42358 0.81890 0.05803  0.01318  0.13397  237 TYR   A CA  
1832 C C   . TYR   A 237 ? 0.57683 0.41385 0.78411 0.05939  0.01155  0.12449  237 TYR   A C   
1833 O O   . TYR   A 237 ? 0.50151 0.33692 0.69427 0.05129  0.00798  0.11752  237 TYR   A O   
1834 C CB  . TYR   A 237 ? 0.54874 0.38400 0.76334 0.04782  0.00635  0.14490  237 TYR   A CB  
1835 C CG  . TYR   A 237 ? 0.59154 0.41081 0.81914 0.04416  0.00870  0.15068  237 TYR   A CG  
1836 C CD1 . TYR   A 237 ? 0.56308 0.35556 0.79035 0.03652  0.01182  0.13719  237 TYR   A CD1 
1837 C CD2 . TYR   A 237 ? 0.58084 0.41186 0.82134 0.04766  0.00761  0.16942  237 TYR   A CD2 
1838 C CE1 . TYR   A 237 ? 0.53940 0.31664 0.77888 0.03260  0.01395  0.14219  237 TYR   A CE1 
1839 C CE2 . TYR   A 237 ? 0.58871 0.40446 0.84229 0.04451  0.01004  0.17546  237 TYR   A CE2 
1840 C CZ  . TYR   A 237 ? 0.59467 0.38306 0.84779 0.03702  0.01331  0.16174  237 TYR   A CZ  
1841 O OH  . TYR   A 237 ? 0.57673 0.34911 0.84299 0.03307  0.01565  0.16741  237 TYR   A OH  
1842 N N   . ASN   A 238 ? 0.54834 0.39698 0.76055 0.06901  0.01402  0.12472  238 ASN   A N   
1843 C CA  . ASN   A 238 ? 0.50774 0.36572 0.70850 0.07125  0.01372  0.11537  238 ASN   A CA  
1844 C C   . ASN   A 238 ? 0.50331 0.38832 0.68442 0.06396  0.00399  0.12113  238 ASN   A C   
1845 O O   . ASN   A 238 ? 0.47226 0.36404 0.63253 0.05848  0.00230  0.10716  238 ASN   A O   
1846 C CB  . ASN   A 238 ? 0.46357 0.30182 0.64962 0.06599  0.01918  0.09009  238 ASN   A CB  
1847 C CG  . ASN   A 238 ? 0.65012 0.49971 0.82367 0.06916  0.02187  0.07698  238 ASN   A CG  
1848 O OD1 . ASN   A 238 ? 0.66962 0.53095 0.85536 0.07900  0.02473  0.08339  238 ASN   A OD1 
1849 N ND2 . ASN   A 238 ? 0.64477 0.49296 0.79477 0.06048  0.02053  0.06000  238 ASN   A ND2 
1850 N N   . TYR   A 239 ? 0.52334 0.42439 0.70937 0.06325  -0.00203 0.14080  239 TYR   A N   
1851 C CA  . TYR   A 239 ? 0.47408 0.40040 0.64283 0.05759  -0.01007 0.14680  239 TYR   A CA  
1852 C C   . TYR   A 239 ? 0.44669 0.39714 0.61736 0.06350  -0.01290 0.15343  239 TYR   A C   
1853 O O   . TYR   A 239 ? 0.46903 0.42240 0.65574 0.07060  -0.01001 0.15845  239 TYR   A O   
1854 C CB  . TYR   A 239 ? 0.46498 0.39889 0.63158 0.05079  -0.01450 0.16064  239 TYR   A CB  
1855 C CG  . TYR   A 239 ? 0.46108 0.38220 0.61858 0.04164  -0.01490 0.15496  239 TYR   A CG  
1856 C CD1 . TYR   A 239 ? 0.48172 0.37689 0.64272 0.03930  -0.00984 0.14045  239 TYR   A CD1 
1857 C CD2 . TYR   A 239 ? 0.46919 0.40697 0.61187 0.03384  -0.01978 0.16048  239 TYR   A CD2 
1858 C CE1 . TYR   A 239 ? 0.42081 0.30848 0.57239 0.02904  -0.01093 0.13295  239 TYR   A CE1 
1859 C CE2 . TYR   A 239 ? 0.41652 0.34666 0.55105 0.02477  -0.01956 0.15319  239 TYR   A CE2 
1860 C CZ  . TYR   A 239 ? 0.42516 0.33097 0.56497 0.02221  -0.01577 0.14003  239 TYR   A CZ  
1861 O OH  . TYR   A 239 ? 0.43050 0.33086 0.56395 0.01248  -0.01659 0.13341  239 TYR   A OH  
1862 N N   . GLU   A 240 ? 0.48191 0.45125 0.63341 0.05843  -0.01805 0.14958  240 GLU   A N   
1863 C CA  . GLU   A 240 ? 0.47482 0.46908 0.62746 0.06158  -0.02262 0.15790  240 GLU   A CA  
1864 C C   . GLU   A 240 ? 0.44088 0.45113 0.59819 0.05960  -0.02670 0.17355  240 GLU   A C   
1865 O O   . GLU   A 240 ? 0.44247 0.45117 0.59443 0.05390  -0.02830 0.17943  240 GLU   A O   
1866 C CB  . GLU   A 240 ? 0.40756 0.41784 0.53599 0.05385  -0.02713 0.14887  240 GLU   A CB  
1867 C CG  . GLU   A 240 ? 0.42830 0.43432 0.54741 0.05353  -0.02357 0.13067  240 GLU   A CG  
1868 C CD  . GLU   A 240 ? 0.52828 0.55348 0.62896 0.04721  -0.02883 0.12722  240 GLU   A CD  
1869 O OE1 . GLU   A 240 ? 0.56777 0.61212 0.67311 0.04885  -0.03279 0.13505  240 GLU   A OE1 
1870 O OE2 . GLU   A 240 ? 0.50914 0.53087 0.59207 0.04046  -0.02919 0.11752  240 GLU   A OE2 
1871 N N   . PRO   A 241 ? 0.55831 0.58584 0.72538 0.06357  -0.02850 0.18077  241 PRO   A N   
1872 C CA  . PRO   A 241 ? 0.49213 0.54053 0.65857 0.05963  -0.03422 0.19526  241 PRO   A CA  
1873 C C   . PRO   A 241 ? 0.48061 0.54381 0.62230 0.04983  -0.04023 0.19393  241 PRO   A C   
1874 O O   . PRO   A 241 ? 0.46045 0.52490 0.58717 0.04697  -0.04136 0.18305  241 PRO   A O   
1875 C CB  . PRO   A 241 ? 0.42690 0.49275 0.60596 0.06460  -0.03575 0.20024  241 PRO   A CB  
1876 C CG  . PRO   A 241 ? 0.44823 0.49581 0.64344 0.07399  -0.02765 0.19168  241 PRO   A CG  
1877 C CD  . PRO   A 241 ? 0.51222 0.54129 0.69336 0.07181  -0.02479 0.17683  241 PRO   A CD  
1878 N N   . LEU   A 242 ? 0.49306 0.56661 0.63077 0.04480  -0.04325 0.20490  242 LEU   A N   
1879 C CA  . LEU   A 242 ? 0.45845 0.54827 0.57337 0.03565  -0.04794 0.20462  242 LEU   A CA  
1880 C C   . LEU   A 242 ? 0.49486 0.61019 0.60923 0.03338  -0.05381 0.21354  242 LEU   A C   
1881 O O   . LEU   A 242 ? 0.45687 0.57818 0.58702 0.03625  -0.05458 0.22695  242 LEU   A O   
1882 C CB  . LEU   A 242 ? 0.43940 0.52337 0.54988 0.03111  -0.04630 0.21039  242 LEU   A CB  
1883 C CG  . LEU   A 242 ? 0.40294 0.50078 0.49001 0.02212  -0.04873 0.20913  242 LEU   A CG  
1884 C CD1 . LEU   A 242 ? 0.41935 0.50541 0.49299 0.01973  -0.04605 0.19540  242 LEU   A CD1 
1885 C CD2 . LEU   A 242 ? 0.40431 0.50567 0.49385 0.01878  -0.04804 0.22203  242 LEU   A CD2 
1886 N N   . THR   A 243 ? 0.47134 0.60130 0.56876 0.02805  -0.05798 0.20619  243 THR   A N   
1887 C CA  . THR   A 243 ? 0.47112 0.62549 0.56687 0.02435  -0.06420 0.21314  243 THR   A CA  
1888 C C   . THR   A 243 ? 0.47731 0.64593 0.55455 0.01536  -0.06751 0.21788  243 THR   A C   
1889 O O   . THR   A 243 ? 0.51895 0.67937 0.58427 0.01222  -0.06451 0.21486  243 THR   A O   
1890 C CB  . THR   A 243 ? 0.51649 0.67935 0.60497 0.02243  -0.06707 0.20231  243 THR   A CB  
1891 O OG1 . THR   A 243 ? 0.47815 0.63976 0.54193 0.01528  -0.06737 0.18968  243 THR   A OG1 
1892 C CG2 . THR   A 243 ? 0.42821 0.57704 0.53415 0.03156  -0.06265 0.19690  243 THR   A CG2 
1893 N N   . GLN   A 244 ? 0.49545 0.68662 0.57063 0.01098  -0.07353 0.22558  244 GLN   A N   
1894 C CA  . GLN   A 244 ? 0.49904 0.70556 0.55309 0.00149  -0.07676 0.22748  244 GLN   A CA  
1895 C C   . GLN   A 244 ? 0.51759 0.72307 0.54616 -0.00525 -0.07630 0.21034  244 GLN   A C   
1896 O O   . GLN   A 244 ? 0.53473 0.74273 0.54448 -0.01130 -0.07486 0.20756  244 GLN   A O   
1897 C CB  . GLN   A 244 ? 0.51981 0.75127 0.57670 -0.00249 -0.08391 0.23889  244 GLN   A CB  
1898 C CG  . GLN   A 244 ? 0.58764 0.83560 0.62375 -0.01209 -0.08701 0.24270  244 GLN   A CG  
1899 C CD  . GLN   A 244 ? 0.65753 0.90274 0.69983 -0.01041 -0.08421 0.25646  244 GLN   A CD  
1900 O OE1 . GLN   A 244 ? 0.63957 0.88806 0.70338 -0.00541 -0.08534 0.27239  244 GLN   A OE1 
1901 N NE2 . GLN   A 244 ? 0.59306 0.83270 0.61741 -0.01465 -0.08020 0.25079  244 GLN   A NE2 
1902 N N   . ASP   A 245 ? 0.50083 0.70246 0.52927 -0.00408 -0.07682 0.19890  245 ASP   A N   
1903 C CA  . ASP   A 245 ? 0.50480 0.70366 0.51093 -0.01002 -0.07592 0.18244  245 ASP   A CA  
1904 C C   . ASP   A 245 ? 0.53149 0.71136 0.53116 -0.00789 -0.06921 0.17584  245 ASP   A C   
1905 O O   . ASP   A 245 ? 0.47312 0.65265 0.45197 -0.01368 -0.06708 0.16629  245 ASP   A O   
1906 C CB  . ASP   A 245 ? 0.47766 0.67645 0.48873 -0.00876 -0.07791 0.17358  245 ASP   A CB  
1907 C CG  . ASP   A 245 ? 0.49823 0.69618 0.48699 -0.01599 -0.07776 0.15720  245 ASP   A CG  
1908 O OD1 . ASP   A 245 ? 0.51213 0.69656 0.50150 -0.01278 -0.07457 0.14756  245 ASP   A OD1 
1909 O OD2 . ASP   A 245 ? 0.54015 0.75062 0.51071 -0.02502 -0.08056 0.15383  245 ASP   A OD2 
1910 N N   . HIS   A 246 ? 0.50626 0.66996 0.52419 0.00026  -0.06547 0.18036  246 HIS   A N   
1911 C CA  . HIS   A 246 ? 0.47405 0.62079 0.48914 0.00174  -0.05967 0.17720  246 HIS   A CA  
1912 C C   . HIS   A 246 ? 0.45172 0.60498 0.45702 -0.00328 -0.05821 0.18420  246 HIS   A C   
1913 O O   . HIS   A 246 ? 0.40732 0.55787 0.39688 -0.00727 -0.05457 0.17730  246 HIS   A O   
1914 C CB  . HIS   A 246 ? 0.43783 0.56671 0.47594 0.01043  -0.05651 0.18201  246 HIS   A CB  
1915 C CG  . HIS   A 246 ? 0.39440 0.51353 0.44038 0.01582  -0.05578 0.17320  246 HIS   A CG  
1916 N ND1 . HIS   A 246 ? 0.46172 0.56892 0.52977 0.02419  -0.05343 0.17680  246 HIS   A ND1 
1917 C CD2 . HIS   A 246 ? 0.38552 0.50489 0.42051 0.01409  -0.05643 0.16088  246 HIS   A CD2 
1918 C CE1 . HIS   A 246 ? 0.44386 0.54530 0.51380 0.02756  -0.05252 0.16721  246 HIS   A CE1 
1919 N NE2 . HIS   A 246 ? 0.39508 0.50415 0.44549 0.02137  -0.05473 0.15808  246 HIS   A NE2 
1920 N N   . VAL   A 247 ? 0.42820 0.59084 0.44379 -0.00284 -0.06054 0.19868  247 VAL   A N   
1921 C CA  . VAL   A 247 ? 0.47014 0.64158 0.47724 -0.00777 -0.05948 0.20713  247 VAL   A CA  
1922 C C   . VAL   A 247 ? 0.50221 0.68657 0.48200 -0.01622 -0.05971 0.19780  247 VAL   A C   
1923 O O   . VAL   A 247 ? 0.50182 0.68611 0.46930 -0.01982 -0.05520 0.19661  247 VAL   A O   
1924 C CB  . VAL   A 247 ? 0.47383 0.65781 0.49508 -0.00668 -0.06351 0.22447  247 VAL   A CB  
1925 C CG1 . VAL   A 247 ? 0.39946 0.59685 0.40903 -0.01293 -0.06330 0.23347  247 VAL   A CG1 
1926 C CG2 . VAL   A 247 ? 0.40803 0.57615 0.45650 0.00186  -0.06125 0.23322  247 VAL   A CG2 
1927 N N   . ASP   A 248 ? 0.45508 0.65026 0.42546 -0.01971 -0.06434 0.19046  248 ASP   A N   
1928 C CA  . ASP   A 248 ? 0.45903 0.66538 0.40311 -0.02836 -0.06440 0.18020  248 ASP   A CA  
1929 C C   . ASP   A 248 ? 0.49191 0.68533 0.42235 -0.02905 -0.05814 0.16462  248 ASP   A C   
1930 O O   . ASP   A 248 ? 0.45321 0.65008 0.36495 -0.03406 -0.05366 0.15913  248 ASP   A O   
1931 C CB  . ASP   A 248 ? 0.46256 0.68258 0.40204 -0.03276 -0.07129 0.17614  248 ASP   A CB  
1932 C CG  . ASP   A 248 ? 0.55209 0.78651 0.50735 -0.03169 -0.07764 0.19244  248 ASP   A CG  
1933 O OD1 . ASP   A 248 ? 0.55562 0.79809 0.51257 -0.03260 -0.07780 0.20555  248 ASP   A OD1 
1934 O OD2 . ASP   A 248 ? 0.57129 0.80966 0.53821 -0.02985 -0.08225 0.19277  248 ASP   A OD2 
1935 N N   . ILE   A 249 ? 0.48295 0.66236 0.42239 -0.02402 -0.05738 0.15742  249 ILE   A N   
1936 C CA  . ILE   A 249 ? 0.47648 0.64343 0.40600 -0.02384 -0.05141 0.14475  249 ILE   A CA  
1937 C C   . ILE   A 249 ? 0.44398 0.60524 0.37344 -0.02298 -0.04490 0.14982  249 ILE   A C   
1938 O O   . ILE   A 249 ? 0.46467 0.62612 0.37825 -0.02637 -0.03903 0.14183  249 ILE   A O   
1939 C CB  . ILE   A 249 ? 0.46456 0.61755 0.40722 -0.01777 -0.05208 0.13967  249 ILE   A CB  
1940 C CG1 . ILE   A 249 ? 0.49653 0.65712 0.44053 -0.01915 -0.05811 0.13523  249 ILE   A CG1 
1941 C CG2 . ILE   A 249 ? 0.50778 0.64935 0.44109 -0.01765 -0.04638 0.12828  249 ILE   A CG2 
1942 C CD1 . ILE   A 249 ? 0.48899 0.63815 0.44793 -0.01272 -0.05875 0.13218  249 ILE   A CD1 
1943 N N   . LEU   A 250 ? 0.46213 0.61867 0.41020 -0.01873 -0.04524 0.16325  250 LEU   A N   
1944 C CA  . LEU   A 250 ? 0.44306 0.59492 0.39435 -0.01875 -0.03964 0.16992  250 LEU   A CA  
1945 C C   . LEU   A 250 ? 0.44168 0.60975 0.37907 -0.02475 -0.03785 0.17566  250 LEU   A C   
1946 O O   . LEU   A 250 ? 0.43600 0.60299 0.37795 -0.02520 -0.03352 0.18380  250 LEU   A O   
1947 C CB  . LEU   A 250 ? 0.41541 0.55563 0.39155 -0.01316 -0.04061 0.18162  250 LEU   A CB  
1948 C CG  . LEU   A 250 ? 0.40992 0.53048 0.40023 -0.00737 -0.03994 0.17628  250 LEU   A CG  
1949 C CD1 . LEU   A 250 ? 0.37762 0.48729 0.39194 -0.00215 -0.04101 0.18712  250 LEU   A CD1 
1950 C CD2 . LEU   A 250 ? 0.25902 0.36960 0.24481 -0.00851 -0.03442 0.16932  250 LEU   A CD2 
1951 N N   . GLY   A 251 ? 0.40584 0.58857 0.32678 -0.02980 -0.04102 0.17137  251 GLY   A N   
1952 C CA  . GLY   A 251 ? 0.40073 0.59902 0.30584 -0.03594 -0.03944 0.17509  251 GLY   A CA  
1953 C C   . GLY   A 251 ? 0.42237 0.61991 0.31210 -0.03873 -0.02998 0.16778  251 GLY   A C   
1954 O O   . GLY   A 251 ? 0.42562 0.62747 0.31670 -0.03979 -0.02584 0.17723  251 GLY   A O   
1955 N N   . PRO   A 252 ? 0.40930 0.60225 0.28465 -0.04003 -0.02575 0.15106  252 PRO   A N   
1956 C CA  . PRO   A 252 ? 0.42255 0.61497 0.28518 -0.04170 -0.01497 0.14361  252 PRO   A CA  
1957 C C   . PRO   A 252 ? 0.40856 0.59459 0.28748 -0.03815 -0.00965 0.15364  252 PRO   A C   
1958 O O   . PRO   A 252 ? 0.40384 0.59683 0.27685 -0.04050 -0.00239 0.15694  252 PRO   A O   
1959 C CB  . PRO   A 252 ? 0.38417 0.56767 0.23825 -0.04103 -0.01202 0.12578  252 PRO   A CB  
1960 C CG  . PRO   A 252 ? 0.40551 0.59144 0.25659 -0.04304 -0.02117 0.12138  252 PRO   A CG  
1961 C CD  . PRO   A 252 ? 0.43478 0.62466 0.30422 -0.04069 -0.02999 0.13820  252 PRO   A CD  
1962 N N   . LEU   A 253 ? 0.40298 0.57585 0.30274 -0.03299 -0.01306 0.15835  253 LEU   A N   
1963 C CA  . LEU   A 253 ? 0.38474 0.54975 0.30228 -0.03064 -0.00924 0.16755  253 LEU   A CA  
1964 C C   . LEU   A 253 ? 0.38964 0.56133 0.31605 -0.03216 -0.01092 0.18386  253 LEU   A C   
1965 O O   . LEU   A 253 ? 0.40182 0.57614 0.33201 -0.03390 -0.00487 0.19031  253 LEU   A O   
1966 C CB  . LEU   A 253 ? 0.31292 0.46089 0.24921 -0.02551 -0.01334 0.16733  253 LEU   A CB  
1967 C CG  . LEU   A 253 ? 0.32800 0.46726 0.26139 -0.02356 -0.01010 0.15485  253 LEU   A CG  
1968 C CD1 . LEU   A 253 ? 0.28197 0.40403 0.23272 -0.01845 -0.01613 0.15129  253 LEU   A CD1 
1969 C CD2 . LEU   A 253 ? 0.30793 0.44488 0.24748 -0.02410 -0.00133 0.15272  253 LEU   A CD2 
1970 N N   . SER   A 254 ? 0.38968 0.56474 0.32143 -0.03143 -0.01887 0.19150  254 SER   A N   
1971 C CA  . SER   A 254 ? 0.40201 0.58587 0.34049 -0.03310 -0.02059 0.20758  254 SER   A CA  
1972 C C   . SER   A 254 ? 0.41811 0.61746 0.33766 -0.03874 -0.01459 0.20819  254 SER   A C   
1973 O O   . SER   A 254 ? 0.42610 0.62813 0.35204 -0.04017 -0.01031 0.21857  254 SER   A O   
1974 C CB  . SER   A 254 ? 0.38537 0.57595 0.32778 -0.03218 -0.02947 0.21400  254 SER   A CB  
1975 O OG  . SER   A 254 ? 0.39653 0.59447 0.34926 -0.03286 -0.03147 0.23137  254 SER   A OG  
1976 N N   . ALA   A 255 ? 0.39620 0.60496 0.29215 -0.04225 -0.01350 0.19607  255 ALA   A N   
1977 C CA  . ALA   A 255 ? 0.44582 0.66950 0.32121 -0.04781 -0.00778 0.19541  255 ALA   A CA  
1978 C C   . ALA   A 255 ? 0.49906 0.72001 0.37063 -0.04794 0.00415  0.18949  255 ALA   A C   
1979 O O   . ALA   A 255 ? 0.50822 0.73958 0.37212 -0.05122 0.01037  0.19494  255 ALA   A O   
1980 C CB  . ALA   A 255 ? 0.45058 0.68337 0.30188 -0.05218 -0.01025 0.18276  255 ALA   A CB  
1981 N N   . GLN   A 256 ? 0.43909 0.64749 0.31694 -0.04440 0.00779  0.17928  256 GLN   A N   
1982 C CA  . GLN   A 256 ? 0.41740 0.62499 0.29611 -0.04405 0.01939  0.17523  256 GLN   A CA  
1983 C C   . GLN   A 256 ? 0.42230 0.62840 0.32238 -0.04369 0.02090  0.19100  256 GLN   A C   
1984 O O   . GLN   A 256 ? 0.46073 0.67262 0.36120 -0.04513 0.03046  0.19235  256 GLN   A O   
1985 C CB  . GLN   A 256 ? 0.36499 0.56101 0.24750 -0.04030 0.02234  0.16207  256 GLN   A CB  
1986 C CG  . GLN   A 256 ? 0.35827 0.55736 0.23917 -0.03983 0.03569  0.15537  256 GLN   A CG  
1987 C CD  . GLN   A 256 ? 0.36776 0.55617 0.26437 -0.03551 0.03814  0.15034  256 GLN   A CD  
1988 O OE1 . GLN   A 256 ? 0.32705 0.50545 0.22553 -0.03304 0.03173  0.14463  256 GLN   A OE1 
1989 N NE2 . GLN   A 256 ? 0.33167 0.52353 0.24054 -0.03478 0.04748  0.15303  256 GLN   A NE2 
1990 N N   . THR   A 257 ? 0.43524 0.63331 0.35431 -0.04186 0.01224  0.20252  257 THR   A N   
1991 C CA  . THR   A 257 ? 0.45049 0.64387 0.39149 -0.04203 0.01329  0.21613  257 THR   A CA  
1992 C C   . THR   A 257 ? 0.37720 0.57895 0.32164 -0.04434 0.00958  0.23241  257 THR   A C   
1993 O O   . THR   A 257 ? 0.38177 0.58141 0.34252 -0.04555 0.01151  0.24424  257 THR   A O   
1994 C CB  . THR   A 257 ? 0.41841 0.59261 0.38169 -0.03823 0.00798  0.21651  257 THR   A CB  
1995 O OG1 . THR   A 257 ? 0.33610 0.50503 0.30052 -0.03530 -0.00114 0.21666  257 THR   A OG1 
1996 C CG2 . THR   A 257 ? 0.32165 0.48855 0.28503 -0.03653 0.01245  0.20335  257 THR   A CG2 
1997 N N   . GLY   A 258 ? 0.40666 0.61852 0.33701 -0.04546 0.00419  0.23374  258 GLY   A N   
1998 C CA  . GLY   A 258 ? 0.40813 0.62942 0.34276 -0.04737 -0.00017 0.25052  258 GLY   A CA  
1999 C C   . GLY   A 258 ? 0.40363 0.61267 0.36481 -0.04372 -0.00690 0.26271  258 GLY   A C   
2000 O O   . GLY   A 258 ? 0.46340 0.67827 0.43338 -0.04492 -0.00900 0.27878  258 GLY   A O   
2001 N N   . ILE   A 259 ? 0.43971 0.63140 0.41389 -0.03924 -0.00964 0.25540  259 ILE   A N   
2002 C CA  . ILE   A 259 ? 0.42706 0.60443 0.42540 -0.03500 -0.01524 0.26373  259 ILE   A CA  
2003 C C   . ILE   A 259 ? 0.45767 0.63744 0.45230 -0.03177 -0.02268 0.26025  259 ILE   A C   
2004 O O   . ILE   A 259 ? 0.40821 0.58321 0.39493 -0.02995 -0.02370 0.24614  259 ILE   A O   
2005 C CB  . ILE   A 259 ? 0.41449 0.57058 0.42950 -0.03270 -0.01291 0.25745  259 ILE   A CB  
2006 C CG1 . ILE   A 259 ? 0.39998 0.55655 0.41898 -0.03694 -0.00564 0.26034  259 ILE   A CG1 
2007 C CG2 . ILE   A 259 ? 0.36270 0.50175 0.40232 -0.02855 -0.01732 0.26508  259 ILE   A CG2 
2008 C CD1 . ILE   A 259 ? 0.38241 0.54096 0.41518 -0.03915 -0.00541 0.27747  259 ILE   A CD1 
2009 N N   . ALA   A 260 ? 0.47064 0.65910 0.47183 -0.03126 -0.02785 0.27383  260 ALA   A N   
2010 C CA  . ALA   A 260 ? 0.46444 0.65771 0.46542 -0.02850 -0.03505 0.27272  260 ALA   A CA  
2011 C C   . ALA   A 260 ? 0.46092 0.63398 0.47769 -0.02215 -0.03654 0.26479  260 ALA   A C   
2012 O O   . ALA   A 260 ? 0.45529 0.61008 0.48935 -0.01944 -0.03364 0.26605  260 ALA   A O   
2013 C CB  . ALA   A 260 ? 0.46516 0.67009 0.47674 -0.02832 -0.03989 0.29150  260 ALA   A CB  
2014 N N   . VAL   A 261 ? 0.38510 0.56143 0.39509 -0.02041 -0.04090 0.25577  261 VAL   A N   
2015 C CA  . VAL   A 261 ? 0.38253 0.54091 0.40460 -0.01452 -0.04169 0.24679  261 VAL   A CA  
2016 C C   . VAL   A 261 ? 0.40466 0.54981 0.45389 -0.00874 -0.04254 0.25783  261 VAL   A C   
2017 O O   . VAL   A 261 ? 0.33806 0.46224 0.40056 -0.00508 -0.03971 0.25306  261 VAL   A O   
2018 C CB  . VAL   A 261 ? 0.41727 0.58389 0.42899 -0.01402 -0.04653 0.23731  261 VAL   A CB  
2019 C CG1 . VAL   A 261 ? 0.32150 0.47163 0.34999 -0.00691 -0.04778 0.23211  261 VAL   A CG1 
2020 C CG2 . VAL   A 261 ? 0.37550 0.54678 0.36274 -0.01873 -0.04402 0.22219  261 VAL   A CG2 
2021 N N   . LEU   A 262 ? 0.38919 0.54610 0.44724 -0.00805 -0.04619 0.27272  262 LEU   A N   
2022 C CA  . LEU   A 262 ? 0.41730 0.56156 0.50228 -0.00208 -0.04617 0.28378  262 LEU   A CA  
2023 C C   . LEU   A 262 ? 0.42060 0.55146 0.51665 -0.00341 -0.04124 0.29057  262 LEU   A C   
2024 O O   . LEU   A 262 ? 0.43717 0.55230 0.55592 0.00122  -0.03992 0.29726  262 LEU   A O   
2025 C CB  . LEU   A 262 ? 0.46705 0.62891 0.56042 -0.00093 -0.05131 0.29983  262 LEU   A CB  
2026 C CG  . LEU   A 262 ? 0.51339 0.68699 0.60516 0.00144  -0.05683 0.29650  262 LEU   A CG  
2027 C CD1 . LEU   A 262 ? 0.41837 0.57289 0.52326 0.00881  -0.05526 0.28569  262 LEU   A CD1 
2028 C CD2 . LEU   A 262 ? 0.50524 0.69942 0.56921 -0.00582 -0.06032 0.28854  262 LEU   A CD2 
2029 N N   . ASP   A 263 ? 0.41928 0.55607 0.50056 -0.00977 -0.03806 0.28893  263 ASP   A N   
2030 C CA  . ASP   A 263 ? 0.45165 0.57576 0.54360 -0.01198 -0.03318 0.29388  263 ASP   A CA  
2031 C C   . ASP   A 263 ? 0.41990 0.52144 0.51664 -0.01085 -0.02976 0.27976  263 ASP   A C   
2032 O O   . ASP   A 263 ? 0.41220 0.49394 0.52790 -0.00940 -0.02757 0.28203  263 ASP   A O   
2033 C CB  . ASP   A 263 ? 0.46213 0.60310 0.53775 -0.01916 -0.03042 0.29835  263 ASP   A CB  
2034 C CG  . ASP   A 263 ? 0.46725 0.62810 0.54176 -0.02109 -0.03331 0.31559  263 ASP   A CG  
2035 O OD1 . ASP   A 263 ? 0.42378 0.58432 0.51373 -0.01675 -0.03736 0.32580  263 ASP   A OD1 
2036 O OD2 . ASP   A 263 ? 0.49458 0.67178 0.55289 -0.02689 -0.03117 0.31904  263 ASP   A OD2 
2037 N N   . MET   A 264 ? 0.43330 0.53728 0.51289 -0.01195 -0.02933 0.26498  264 MET   A N   
2038 C CA  . MET   A 264 ? 0.36045 0.44444 0.44429 -0.01077 -0.02705 0.25183  264 MET   A CA  
2039 C C   . MET   A 264 ? 0.39097 0.45652 0.49163 -0.00390 -0.02886 0.24881  264 MET   A C   
2040 O O   . MET   A 264 ? 0.33204 0.37617 0.44356 -0.00309 -0.02662 0.24218  264 MET   A O   
2041 C CB  . MET   A 264 ? 0.35292 0.44484 0.41559 -0.01254 -0.02656 0.23800  264 MET   A CB  
2042 C CG  . MET   A 264 ? 0.37599 0.45126 0.44138 -0.01301 -0.02392 0.22651  264 MET   A CG  
2043 S SD  . MET   A 264 ? 0.34088 0.41405 0.41243 -0.01990 -0.01852 0.23181  264 MET   A SD  
2044 C CE  . MET   A 264 ? 0.36096 0.45691 0.40753 -0.02402 -0.01475 0.22662  264 MET   A CE  
2045 N N   . CYS   A 265 ? 0.42523 0.49916 0.52910 0.00078  -0.03260 0.25384  265 CYS   A N   
2046 C CA  . CYS   A 265 ? 0.43026 0.48813 0.55309 0.00815  -0.03299 0.25321  265 CYS   A CA  
2047 C C   . CYS   A 265 ? 0.39443 0.43515 0.53929 0.00927  -0.02999 0.26245  265 CYS   A C   
2048 O O   . CYS   A 265 ? 0.39660 0.41392 0.55541 0.01301  -0.02734 0.25583  265 CYS   A O   
2049 C CB  . CYS   A 265 ? 0.41914 0.49345 0.54279 0.01230  -0.03745 0.25907  265 CYS   A CB  
2050 S SG  . CYS   A 265 ? 0.32569 0.41344 0.42848 0.01204  -0.04100 0.24519  265 CYS   A SG  
2051 N N   . ALA   A 266 ? 0.39551 0.44694 0.54357 0.00583  -0.03008 0.27737  266 ALA   A N   
2052 C CA  . ALA   A 266 ? 0.39330 0.42786 0.56203 0.00582  -0.02697 0.28625  266 ALA   A CA  
2053 C C   . ALA   A 266 ? 0.42071 0.43585 0.59070 0.00078  -0.02310 0.27668  266 ALA   A C   
2054 O O   . ALA   A 266 ? 0.44180 0.43387 0.62964 0.00169  -0.02029 0.27623  266 ALA   A O   
2055 C CB  . ALA   A 266 ? 0.40949 0.46128 0.58028 0.00248  -0.02797 0.30498  266 ALA   A CB  
2056 N N   . SER   A 267 ? 0.38350 0.40750 0.53549 -0.00492 -0.02274 0.26877  267 SER   A N   
2057 C CA  . SER   A 267 ? 0.36951 0.37736 0.52389 -0.01032 -0.01970 0.25992  267 SER   A CA  
2058 C C   . SER   A 267 ? 0.42066 0.40534 0.58088 -0.00671 -0.01933 0.24514  267 SER   A C   
2059 O O   . SER   A 267 ? 0.40876 0.37076 0.58216 -0.00904 -0.01705 0.24071  267 SER   A O   
2060 C CB  . SER   A 267 ? 0.35588 0.38002 0.49117 -0.01630 -0.01889 0.25500  267 SER   A CB  
2061 O OG  . SER   A 267 ? 0.53450 0.57954 0.66297 -0.02007 -0.01806 0.26724  267 SER   A OG  
2062 N N   . LEU   A 268 ? 0.39653 0.38666 0.54624 -0.00169 -0.02148 0.23664  268 LEU   A N   
2063 C CA  . LEU   A 268 ? 0.39388 0.36356 0.54800 0.00232  -0.02083 0.22267  268 LEU   A CA  
2064 C C   . LEU   A 268 ? 0.42527 0.37485 0.60019 0.00799  -0.01857 0.22492  268 LEU   A C   
2065 O O   . LEU   A 268 ? 0.45737 0.38197 0.64147 0.00731  -0.01576 0.21508  268 LEU   A O   
2066 C CB  . LEU   A 268 ? 0.37243 0.35459 0.51223 0.00698  -0.02354 0.21530  268 LEU   A CB  
2067 C CG  . LEU   A 268 ? 0.40318 0.36765 0.54545 0.01171  -0.02279 0.20099  268 LEU   A CG  
2068 C CD1 . LEU   A 268 ? 0.35937 0.30369 0.50384 0.00571  -0.02079 0.19105  268 LEU   A CD1 
2069 C CD2 . LEU   A 268 ? 0.39898 0.37900 0.52474 0.01429  -0.02573 0.19429  268 LEU   A CD2 
2070 N N   . LYS   A 269 ? 0.40488 0.36494 0.58768 0.01325  -0.01951 0.23748  269 LYS   A N   
2071 C CA  . LYS   A 269 ? 0.44724 0.38886 0.65179 0.01923  -0.01644 0.24098  269 LYS   A CA  
2072 C C   . LYS   A 269 ? 0.47708 0.39466 0.69374 0.01385  -0.01269 0.23947  269 LYS   A C   
2073 O O   . LYS   A 269 ? 0.48241 0.37375 0.70920 0.01585  -0.00893 0.22844  269 LYS   A O   
2074 C CB  . LYS   A 269 ? 0.40014 0.35947 0.61333 0.02343  -0.01839 0.25900  269 LYS   A CB  
2075 C CG  . LYS   A 269 ? 0.46262 0.40324 0.70047 0.03030  -0.01454 0.26391  269 LYS   A CG  
2076 C CD  . LYS   A 269 ? 0.54317 0.49987 0.79347 0.03327  -0.01636 0.28482  269 LYS   A CD  
2077 C CE  . LYS   A 269 ? 0.53265 0.51345 0.78026 0.03886  -0.02050 0.29092  269 LYS   A CE  
2078 N NZ  . LYS   A 269 ? 0.59317 0.58494 0.85747 0.04172  -0.02168 0.31154  269 LYS   A NZ  
2079 N N   . GLU   A 270 ? 0.44118 0.36764 0.65593 0.00619  -0.01340 0.24936  270 GLU   A N   
2080 C CA  . GLU   A 270 ? 0.51537 0.42134 0.74163 -0.00055 -0.01040 0.24874  270 GLU   A CA  
2081 C C   . GLU   A 270 ? 0.52383 0.41190 0.74439 -0.00629 -0.00945 0.23010  270 GLU   A C   
2082 O O   . GLU   A 270 ? 0.55619 0.41800 0.78811 -0.00930 -0.00651 0.22227  270 GLU   A O   
2083 C CB  . GLU   A 270 ? 0.43211 0.35559 0.65630 -0.00775 -0.01131 0.26360  270 GLU   A CB  
2084 C CG  . GLU   A 270 ? 0.56856 0.47402 0.80776 -0.01472 -0.00845 0.26735  270 GLU   A CG  
2085 C CD  . GLU   A 270 ? 0.62651 0.55181 0.86345 -0.02166 -0.00885 0.28270  270 GLU   A CD  
2086 O OE1 . GLU   A 270 ? 0.61238 0.53688 0.86294 -0.02109 -0.00778 0.29781  270 GLU   A OE1 
2087 O OE2 . GLU   A 270 ? 0.57782 0.51937 0.80024 -0.02749 -0.00968 0.27996  270 GLU   A OE2 
2088 N N   . LEU   A 271 ? 0.47123 0.37292 0.67415 -0.00822 -0.01200 0.22233  271 LEU   A N   
2089 C CA  . LEU   A 271 ? 0.51883 0.40625 0.71648 -0.01397 -0.01198 0.20565  271 LEU   A CA  
2090 C C   . LEU   A 271 ? 0.55759 0.42061 0.76049 -0.00844 -0.00978 0.19088  271 LEU   A C   
2091 O O   . LEU   A 271 ? 0.55589 0.39620 0.76296 -0.01418 -0.00824 0.17798  271 LEU   A O   
2092 C CB  . LEU   A 271 ? 0.49017 0.39873 0.66883 -0.01590 -0.01496 0.20218  271 LEU   A CB  
2093 C CG  . LEU   A 271 ? 0.42477 0.35314 0.59626 -0.02398 -0.01560 0.20975  271 LEU   A CG  
2094 C CD1 . LEU   A 271 ? 0.33371 0.28161 0.48620 -0.02310 -0.01747 0.20525  271 LEU   A CD1 
2095 C CD2 . LEU   A 271 ? 0.48938 0.40383 0.66948 -0.03431 -0.01488 0.20440  271 LEU   A CD2 
2096 N N   . LEU   A 272 ? 0.46855 0.33699 0.67086 0.00210  -0.00946 0.19171  272 LEU   A N   
2097 C CA  . LEU   A 272 ? 0.54998 0.39638 0.75883 0.00862  -0.00576 0.17838  272 LEU   A CA  
2098 C C   . LEU   A 272 ? 0.54270 0.36506 0.77001 0.00948  -0.00087 0.17898  272 LEU   A C   
2099 O O   . LEU   A 272 ? 0.57023 0.36690 0.80156 0.00954  0.00328  0.16329  272 LEU   A O   
2100 C CB  . LEU   A 272 ? 0.55831 0.41936 0.76485 0.01975  -0.00625 0.18107  272 LEU   A CB  
2101 C CG  . LEU   A 272 ? 0.50499 0.38689 0.69261 0.01936  -0.01065 0.17789  272 LEU   A CG  
2102 C CD1 . LEU   A 272 ? 0.45788 0.35797 0.64454 0.02871  -0.01201 0.18344  272 LEU   A CD1 
2103 C CD2 . LEU   A 272 ? 0.47058 0.33696 0.65045 0.01632  -0.00990 0.15950  272 LEU   A CD2 
2104 N N   . GLN   A 273 ? 0.55709 0.38695 0.79502 0.00971  -0.00100 0.19629  273 GLN   A N   
2105 C CA  . GLN   A 273 ? 0.56687 0.37417 0.82378 0.01131  0.00379  0.19868  273 GLN   A CA  
2106 C C   . GLN   A 273 ? 0.61905 0.40541 0.87847 -0.00048 0.00497  0.19105  273 GLN   A C   
2107 O O   . GLN   A 273 ? 0.65638 0.41408 0.92332 -0.00141 0.00952  0.17821  273 GLN   A O   
2108 C CB  . GLN   A 273 ? 0.53765 0.36122 0.80610 0.01560  0.00285  0.22111  273 GLN   A CB  
2109 C CG  . GLN   A 273 ? 0.58831 0.42189 0.86363 0.02810  0.00359  0.22683  273 GLN   A CG  
2110 C CD  . GLN   A 273 ? 0.56120 0.42004 0.84241 0.03072  0.00023  0.24955  273 GLN   A CD  
2111 O OE1 . GLN   A 273 ? 0.62271 0.48867 0.90473 0.02403  -0.00150 0.26158  273 GLN   A OE1 
2112 N NE2 . GLN   A 273 ? 0.56390 0.43770 0.84928 0.03992  -0.00078 0.25569  273 GLN   A NE2 
2113 N N   . ASN   A 274 ? 0.64102 0.44193 0.89372 -0.01011 0.00113  0.19787  274 ASN   A N   
2114 C CA  . ASN   A 274 ? 0.62458 0.41033 0.88207 -0.02237 0.00158  0.19411  274 ASN   A CA  
2115 C C   . ASN   A 274 ? 0.63722 0.41948 0.88219 -0.03215 -0.00101 0.17724  274 ASN   A C   
2116 O O   . ASN   A 274 ? 0.61962 0.39003 0.86822 -0.04374 -0.00138 0.17191  274 ASN   A O   
2117 C CB  . ASN   A 274 ? 0.64310 0.44781 0.90503 -0.02724 -0.00019 0.21417  274 ASN   A CB  
2118 C CG  . ASN   A 274 ? 0.73573 0.54727 1.00998 -0.01828 0.00133  0.23262  274 ASN   A CG  
2119 O OD1 . ASN   A 274 ? 0.70116 0.53618 0.97438 -0.01895 -0.00074 0.24996  274 ASN   A OD1 
2120 N ND2 . ASN   A 274 ? 0.72613 0.51791 1.01227 -0.00999 0.00518  0.22879  274 ASN   A ND2 
2121 N N   . GLY   A 275 ? 0.64683 0.43935 0.87814 -0.02837 -0.00314 0.16892  275 GLY   A N   
2122 C CA  . GLY   A 275 ? 0.70321 0.49559 0.92385 -0.03809 -0.00646 0.15519  275 GLY   A CA  
2123 C C   . GLY   A 275 ? 0.70642 0.52367 0.92265 -0.04619 -0.01029 0.16624  275 GLY   A C   
2124 O O   . GLY   A 275 ? 0.69520 0.53124 0.91330 -0.04366 -0.01009 0.18354  275 GLY   A O   
2125 N N   . MET   A 276 ? 0.79794 0.61636 1.00821 -0.05631 -0.01369 0.15548  276 MET   A N   
2126 C CA  . MET   A 276 ? 0.79941 0.64207 1.00666 -0.06408 -0.01654 0.16422  276 MET   A CA  
2127 C C   . MET   A 276 ? 0.84660 0.68267 1.06555 -0.07680 -0.01686 0.16521  276 MET   A C   
2128 O O   . MET   A 276 ? 0.82154 0.67837 1.04117 -0.08332 -0.01820 0.17359  276 MET   A O   
2129 C CB  . MET   A 276 ? 0.75006 0.60475 0.94443 -0.06654 -0.02065 0.15467  276 MET   A CB  
2130 C CG  . MET   A 276 ? 0.69474 0.56408 0.87628 -0.05447 -0.02027 0.15845  276 MET   A CG  
2131 S SD  . MET   A 276 ? 0.70136 0.59064 0.85921 -0.05186 -0.02347 0.14087  276 MET   A SD  
2132 C CE  . MET   A 276 ? 0.54941 0.45516 0.71005 -0.06459 -0.02605 0.14243  276 MET   A CE  
2133 N N   . ASN   A 277 ? 0.97922 0.78735 1.20764 -0.08002 -0.01489 0.15725  277 ASN   A N   
2134 C CA  . ASN   A 277 ? 1.02698 0.82514 1.26644 -0.09314 -0.01530 0.15619  277 ASN   A CA  
2135 C C   . ASN   A 277 ? 1.02084 0.83089 1.25648 -0.10588 -0.02085 0.14741  277 ASN   A C   
2136 O O   . ASN   A 277 ? 1.03121 0.85360 1.27451 -0.11545 -0.02213 0.15480  277 ASN   A O   
2137 C CB  . ASN   A 277 ? 1.09793 0.90741 1.34812 -0.09308 -0.01268 0.17697  277 ASN   A CB  
2138 C CG  . ASN   A 277 ? 1.15480 0.94681 1.41864 -0.10495 -0.01183 0.17598  277 ASN   A CG  
2139 O OD1 . ASN   A 277 ? 1.22358 0.98764 1.48972 -0.10966 -0.01130 0.16067  277 ASN   A OD1 
2140 N ND2 . ASN   A 277 ? 1.18241 0.99078 1.45446 -0.11028 -0.01133 0.19165  277 ASN   A ND2 
2141 N N   . GLY   A 278 ? 0.99778 0.80569 1.22226 -0.10584 -0.02435 0.13199  278 GLY   A N   
2142 C CA  . GLY   A 278 ? 1.00016 0.82192 1.22093 -0.11729 -0.03088 0.12376  278 GLY   A CA  
2143 C C   . GLY   A 278 ? 0.89363 0.74921 1.11547 -0.11812 -0.03205 0.13885  278 GLY   A C   
2144 O O   . GLY   A 278 ? 0.89422 0.76333 1.12096 -0.12930 -0.03612 0.13769  278 GLY   A O   
2145 N N   . ARG   A 279 ? 0.83843 0.70923 1.05565 -0.10657 -0.02817 0.15277  279 ARG   A N   
2146 C CA  . ARG   A 279 ? 0.70680 0.60949 0.92032 -0.10599 -0.02817 0.16322  279 ARG   A CA  
2147 C C   . ARG   A 279 ? 0.69754 0.60943 0.89436 -0.09820 -0.02999 0.15452  279 ARG   A C   
2148 O O   . ARG   A 279 ? 0.71280 0.60838 0.90029 -0.09276 -0.03116 0.14053  279 ARG   A O   
2149 C CB  . ARG   A 279 ? 0.72963 0.64791 0.94333 -0.09857 -0.02256 0.18172  279 ARG   A CB  
2150 C CG  . ARG   A 279 ? 0.80150 0.71248 1.02854 -0.10251 -0.01976 0.19164  279 ARG   A CG  
2151 C CD  . ARG   A 279 ? 0.76368 0.69982 0.98770 -0.09762 -0.01560 0.20865  279 ARG   A CD  
2152 N NE  . ARG   A 279 ? 0.79426 0.72739 1.02848 -0.09835 -0.01233 0.22228  279 ARG   A NE  
2153 C CZ  . ARG   A 279 ? 0.78375 0.73984 1.01524 -0.09581 -0.00871 0.23719  279 ARG   A CZ  
2154 N NH1 . ARG   A 279 ? 0.74425 0.72567 0.96432 -0.09376 -0.00740 0.23790  279 ARG   A NH1 
2155 N NH2 . ARG   A 279 ? 0.81160 0.76568 1.05212 -0.09642 -0.00607 0.25071  279 ARG   A NH2 
2156 N N   . THR   A 280 ? 0.58991 0.53011 0.77926 -0.09479 -0.02871 0.16013  280 THR   A N   
2157 C CA  . THR   A 280 ? 0.46160 0.41400 0.63195 -0.08530 -0.02946 0.14963  280 THR   A CA  
2158 C C   . THR   A 280 ? 0.43622 0.40957 0.59808 -0.07672 -0.02432 0.16163  280 THR   A C   
2159 O O   . THR   A 280 ? 0.44012 0.42958 0.60914 -0.08034 -0.02072 0.17549  280 THR   A O   
2160 C CB  . THR   A 280 ? 0.46449 0.43030 0.63288 -0.09087 -0.03396 0.13916  280 THR   A CB  
2161 O OG1 . THR   A 280 ? 0.46951 0.45719 0.64945 -0.09680 -0.03200 0.15124  280 THR   A OG1 
2162 C CG2 . THR   A 280 ? 0.45066 0.39666 0.62367 -0.10073 -0.04017 0.12538  280 THR   A CG2 
2163 N N   . ILE   A 281 ? 0.44368 0.41709 0.58985 -0.06607 -0.02374 0.15587  281 ILE   A N   
2164 C CA  . ILE   A 281 ? 0.38228 0.37573 0.51614 -0.05852 -0.01977 0.16275  281 ILE   A CA  
2165 C C   . ILE   A 281 ? 0.39310 0.39988 0.51472 -0.05511 -0.02047 0.15026  281 ILE   A C   
2166 O O   . ILE   A 281 ? 0.37572 0.37328 0.48933 -0.05160 -0.02383 0.13656  281 ILE   A O   
2167 C CB  . ILE   A 281 ? 0.38770 0.37384 0.51404 -0.04981 -0.01907 0.16660  281 ILE   A CB  
2168 C CG1 . ILE   A 281 ? 0.34091 0.31390 0.48201 -0.05220 -0.01811 0.18149  281 ILE   A CG1 
2169 C CG2 . ILE   A 281 ? 0.37210 0.37964 0.48297 -0.04370 -0.01599 0.17107  281 ILE   A CG2 
2170 C CD1 . ILE   A 281 ? 0.32509 0.29608 0.46174 -0.04352 -0.01761 0.18962  281 ILE   A CD1 
2171 N N   . LEU   A 282 ? 0.38244 0.41082 0.50326 -0.05582 -0.01653 0.15544  282 LEU   A N   
2172 C CA  . LEU   A 282 ? 0.31006 0.35135 0.42186 -0.05174 -0.01596 0.14542  282 LEU   A CA  
2173 C C   . LEU   A 282 ? 0.33176 0.36619 0.44876 -0.05584 -0.02217 0.13365  282 LEU   A C   
2174 O O   . LEU   A 282 ? 0.29250 0.32573 0.39933 -0.05104 -0.02445 0.12241  282 LEU   A O   
2175 C CB  . LEU   A 282 ? 0.25822 0.29953 0.35166 -0.04231 -0.01474 0.13938  282 LEU   A CB  
2176 C CG  . LEU   A 282 ? 0.27925 0.33602 0.36400 -0.03912 -0.00835 0.14877  282 LEU   A CG  
2177 C CD1 . LEU   A 282 ? 0.27151 0.32929 0.33827 -0.03146 -0.00803 0.14081  282 LEU   A CD1 
2178 C CD2 . LEU   A 282 ? 0.26487 0.34100 0.35470 -0.04157 -0.00243 0.15266  282 LEU   A CD2 
2179 N N   . GLY   A 283 ? 0.30442 0.33493 0.43716 -0.06568 -0.02523 0.13686  283 GLY   A N   
2180 C CA  . GLY   A 283 ? 0.33810 0.36191 0.47544 -0.07207 -0.03237 0.12636  283 GLY   A CA  
2181 C C   . GLY   A 283 ? 0.37245 0.37378 0.49994 -0.07041 -0.03667 0.11372  283 GLY   A C   
2182 O O   . GLY   A 283 ? 0.31246 0.31113 0.43647 -0.07347 -0.04226 0.10260  283 GLY   A O   
2183 N N   . SER   A 284 ? 0.35994 0.34634 0.48306 -0.06547 -0.03403 0.11560  284 SER   A N   
2184 C CA  . SER   A 284 ? 0.40963 0.37518 0.52473 -0.06262 -0.03629 0.10368  284 SER   A CA  
2185 C C   . SER   A 284 ? 0.39456 0.33814 0.52052 -0.06658 -0.03554 0.10689  284 SER   A C   
2186 O O   . SER   A 284 ? 0.39755 0.34121 0.53092 -0.06476 -0.03175 0.12060  284 SER   A O   
2187 C CB  . SER   A 284 ? 0.32715 0.29467 0.42774 -0.05089 -0.03348 0.10131  284 SER   A CB  
2188 O OG  . SER   A 284 ? 0.38628 0.33455 0.48164 -0.04795 -0.03443 0.09096  284 SER   A OG  
2189 N N   . ALA   A 285 ? 0.39825 0.32256 0.52469 -0.07191 -0.03878 0.09428  285 ALA   A N   
2190 C CA  . ALA   A 285 ? 0.41125 0.31028 0.54818 -0.07485 -0.03702 0.09460  285 ALA   A CA  
2191 C C   . ALA   A 285 ? 0.41668 0.30051 0.54732 -0.06393 -0.03325 0.09006  285 ALA   A C   
2192 O O   . ALA   A 285 ? 0.42595 0.28542 0.56410 -0.06497 -0.03119 0.08578  285 ALA   A O   
2193 C CB  . ALA   A 285 ? 0.43649 0.32065 0.57755 -0.08746 -0.04159 0.08202  285 ALA   A CB  
2194 N N   . LEU   A 286 ? 0.39866 0.29607 0.51705 -0.05364 -0.03190 0.09069  286 LEU   A N   
2195 C CA  . LEU   A 286 ? 0.39594 0.28333 0.51050 -0.04309 -0.02843 0.08842  286 LEU   A CA  
2196 C C   . LEU   A 286 ? 0.40837 0.31475 0.51876 -0.03453 -0.02672 0.10119  286 LEU   A C   
2197 O O   . LEU   A 286 ? 0.37964 0.30659 0.48322 -0.03546 -0.02785 0.10502  286 LEU   A O   
2198 C CB  . LEU   A 286 ? 0.37961 0.26216 0.47984 -0.04034 -0.02923 0.07057  286 LEU   A CB  
2199 C CG  . LEU   A 286 ? 0.38937 0.25364 0.48746 -0.04831 -0.03088 0.05424  286 LEU   A CG  
2200 C CD1 . LEU   A 286 ? 0.35704 0.22497 0.43702 -0.04486 -0.03170 0.03966  286 LEU   A CD1 
2201 C CD2 . LEU   A 286 ? 0.34829 0.18498 0.45858 -0.04821 -0.02639 0.05196  286 LEU   A CD2 
2202 N N   . LEU   A 287 ? 0.34666 0.24642 0.46138 -0.02625 -0.02387 0.10738  287 LEU   A N   
2203 C CA  . LEU   A 287 ? 0.35437 0.27273 0.46275 -0.01879 -0.02337 0.11754  287 LEU   A CA  
2204 C C   . LEU   A 287 ? 0.37297 0.30229 0.46452 -0.01492 -0.02452 0.10543  287 LEU   A C   
2205 O O   . LEU   A 287 ? 0.35339 0.27322 0.44116 -0.01081 -0.02377 0.09422  287 LEU   A O   
2206 C CB  . LEU   A 287 ? 0.35159 0.26199 0.47056 -0.01107 -0.02114 0.12784  287 LEU   A CB  
2207 C CG  . LEU   A 287 ? 0.43724 0.33936 0.57329 -0.01522 -0.02001 0.14340  287 LEU   A CG  
2208 C CD1 . LEU   A 287 ? 0.32733 0.21919 0.47812 -0.00736 -0.01776 0.15545  287 LEU   A CD1 
2209 C CD2 . LEU   A 287 ? 0.41969 0.34348 0.55195 -0.02013 -0.02104 0.15713  287 LEU   A CD2 
2210 N N   . GLU   A 288 ? 0.28123 0.23001 0.36332 -0.01636 -0.02552 0.10774  288 GLU   A N   
2211 C CA  . GLU   A 288 ? 0.30008 0.25842 0.36785 -0.01392 -0.02642 0.09710  288 GLU   A CA  
2212 C C   . GLU   A 288 ? 0.28492 0.25335 0.34538 -0.00660 -0.02568 0.10060  288 GLU   A C   
2213 O O   . GLU   A 288 ? 0.29962 0.27989 0.35984 -0.00572 -0.02519 0.11253  288 GLU   A O   
2214 C CB  . GLU   A 288 ? 0.31999 0.29280 0.38374 -0.01888 -0.02698 0.09742  288 GLU   A CB  
2215 C CG  . GLU   A 288 ? 0.37904 0.36206 0.42979 -0.01574 -0.02720 0.08898  288 GLU   A CG  
2216 C CD  . GLU   A 288 ? 0.42969 0.40345 0.47688 -0.01705 -0.02963 0.07582  288 GLU   A CD  
2217 O OE1 . GLU   A 288 ? 0.33131 0.30369 0.36972 -0.01223 -0.02942 0.06870  288 GLU   A OE1 
2218 O OE2 . GLU   A 288 ? 0.52128 0.49011 0.57436 -0.02365 -0.03192 0.07322  288 GLU   A OE2 
2219 N N   . ASP   A 289 ? 0.23120 0.19641 0.28509 -0.00223 -0.02577 0.09043  289 ASP   A N   
2220 C CA  . ASP   A 289 ? 0.27856 0.25309 0.32763 0.00379  -0.02567 0.09333  289 ASP   A CA  
2221 C C   . ASP   A 289 ? 0.30888 0.29304 0.34430 0.00468  -0.02609 0.08432  289 ASP   A C   
2222 O O   . ASP   A 289 ? 0.28133 0.27168 0.31319 0.00878  -0.02632 0.08441  289 ASP   A O   
2223 C CB  . ASP   A 289 ? 0.28585 0.24898 0.34366 0.00959  -0.02438 0.09250  289 ASP   A CB  
2224 C CG  . ASP   A 289 ? 0.29340 0.24611 0.34658 0.01084  -0.02290 0.07711  289 ASP   A CG  
2225 O OD1 . ASP   A 289 ? 0.34352 0.29045 0.40225 0.01665  -0.02056 0.07534  289 ASP   A OD1 
2226 O OD2 . ASP   A 289 ? 0.29254 0.24324 0.33761 0.00620  -0.02377 0.06758  289 ASP   A OD2 
2227 N N   . GLU   A 290 ? 0.24774 0.23330 0.27709 0.00099  -0.02633 0.07708  290 GLU   A N   
2228 C CA  . GLU   A 290 ? 0.27801 0.27070 0.29623 0.00234  -0.02624 0.06945  290 GLU   A CA  
2229 C C   . GLU   A 290 ? 0.26423 0.27078 0.27611 0.00095  -0.02509 0.07283  290 GLU   A C   
2230 O O   . GLU   A 290 ? 0.24897 0.25923 0.25464 0.00067  -0.02430 0.06662  290 GLU   A O   
2231 C CB  . GLU   A 290 ? 0.25402 0.23953 0.26932 0.00055  -0.02708 0.05910  290 GLU   A CB  
2232 C CG  . GLU   A 290 ? 0.25292 0.22624 0.26905 0.00276  -0.02667 0.05232  290 GLU   A CG  
2233 C CD  . GLU   A 290 ? 0.27303 0.24423 0.28055 0.00193  -0.02722 0.04222  290 GLU   A CD  
2234 O OE1 . GLU   A 290 ? 0.29733 0.26314 0.30220 0.00488  -0.02547 0.03665  290 GLU   A OE1 
2235 O OE2 . GLU   A 290 ? 0.26709 0.24319 0.27126 -0.00143 -0.02913 0.04081  290 GLU   A OE2 
2236 N N   . PHE   A 291 ? 0.22087 0.23506 0.23409 0.00034  -0.02442 0.08281  291 PHE   A N   
2237 C CA  . PHE   A 291 ? 0.28361 0.31141 0.28866 -0.00101 -0.02210 0.08555  291 PHE   A CA  
2238 C C   . PHE   A 291 ? 0.23290 0.26940 0.23261 0.00015  -0.02322 0.09199  291 PHE   A C   
2239 O O   . PHE   A 291 ? 0.24040 0.27766 0.24668 0.00019  -0.02462 0.10280  291 PHE   A O   
2240 C CB  . PHE   A 291 ? 0.27573 0.30804 0.28630 -0.00469 -0.01987 0.09296  291 PHE   A CB  
2241 C CG  . PHE   A 291 ? 0.31050 0.33941 0.32698 -0.00689 -0.01933 0.08807  291 PHE   A CG  
2242 C CD1 . PHE   A 291 ? 0.31066 0.34539 0.32223 -0.00602 -0.01691 0.08134  291 PHE   A CD1 
2243 C CD2 . PHE   A 291 ? 0.30620 0.32713 0.33449 -0.01039 -0.02122 0.09126  291 PHE   A CD2 
2244 C CE1 . PHE   A 291 ? 0.18982 0.22471 0.20904 -0.00795 -0.01713 0.07920  291 PHE   A CE1 
2245 C CE2 . PHE   A 291 ? 0.27668 0.29771 0.31100 -0.01377 -0.02190 0.08780  291 PHE   A CE2 
2246 C CZ  . PHE   A 291 ? 0.19225 0.22162 0.22245 -0.01225 -0.02016 0.08256  291 PHE   A CZ  
2247 N N   . THR   A 292 ? 0.26502 0.30854 0.25353 0.00050  -0.02292 0.08620  292 THR   A N   
2248 C CA  . THR   A 292 ? 0.29353 0.34840 0.27512 -0.00010 -0.02502 0.09173  292 THR   A CA  
2249 C C   . THR   A 292 ? 0.27331 0.34065 0.24678 -0.00374 -0.02259 0.09871  292 THR   A C   
2250 O O   . THR   A 292 ? 0.23682 0.30454 0.20957 -0.00524 -0.01803 0.09722  292 THR   A O   
2251 C CB  . THR   A 292 ? 0.27127 0.32865 0.24349 -0.00012 -0.02569 0.08178  292 THR   A CB  
2252 O OG1 . THR   A 292 ? 0.25937 0.31672 0.22306 -0.00174 -0.02124 0.07283  292 THR   A OG1 
2253 C CG2 . THR   A 292 ? 0.26795 0.31517 0.24759 0.00321  -0.02728 0.07627  292 THR   A CG2 
2254 N N   . PRO   A 293 ? 0.25514 0.33470 0.22239 -0.00542 -0.02545 0.10706  293 PRO   A N   
2255 C CA  . PRO   A 293 ? 0.28534 0.37862 0.24042 -0.00971 -0.02253 0.11236  293 PRO   A CA  
2256 C C   . PRO   A 293 ? 0.29886 0.39482 0.23950 -0.01186 -0.01705 0.09898  293 PRO   A C   
2257 O O   . PRO   A 293 ? 0.25732 0.35872 0.19249 -0.01383 -0.01089 0.09945  293 PRO   A O   
2258 C CB  . PRO   A 293 ? 0.24386 0.35069 0.19370 -0.01144 -0.02845 0.12289  293 PRO   A CB  
2259 C CG  . PRO   A 293 ? 0.26517 0.36404 0.23147 -0.00667 -0.03354 0.12765  293 PRO   A CG  
2260 C CD  . PRO   A 293 ? 0.33995 0.42373 0.31091 -0.00374 -0.03142 0.11291  293 PRO   A CD  
2261 N N   . PHE   A 294 ? 0.30200 0.39344 0.23807 -0.01125 -0.01827 0.08713  294 PHE   A N   
2262 C CA  . PHE   A 294 ? 0.31237 0.40164 0.23844 -0.01227 -0.01224 0.07362  294 PHE   A CA  
2263 C C   . PHE   A 294 ? 0.31169 0.39333 0.24704 -0.00933 -0.00634 0.07101  294 PHE   A C   
2264 O O   . PHE   A 294 ? 0.32531 0.41144 0.25481 -0.01019 0.00087  0.06776  294 PHE   A O   
2265 C CB  . PHE   A 294 ? 0.31363 0.39621 0.23786 -0.01187 -0.01474 0.06290  294 PHE   A CB  
2266 C CG  . PHE   A 294 ? 0.37700 0.45557 0.29200 -0.01293 -0.00836 0.04955  294 PHE   A CG  
2267 C CD1 . PHE   A 294 ? 0.37004 0.45666 0.26769 -0.01815 -0.00589 0.04372  294 PHE   A CD1 
2268 C CD2 . PHE   A 294 ? 0.43916 0.50581 0.36283 -0.00887 -0.00455 0.04295  294 PHE   A CD2 
2269 C CE1 . PHE   A 294 ? 0.39397 0.47417 0.28406 -0.01881 0.00128  0.03023  294 PHE   A CE1 
2270 C CE2 . PHE   A 294 ? 0.43553 0.49720 0.35337 -0.00882 0.00209  0.03166  294 PHE   A CE2 
2271 C CZ  . PHE   A 294 ? 0.48426 0.55143 0.38581 -0.01354 0.00556  0.02473  294 PHE   A CZ  
2272 N N   . ASP   A 295 ? 0.28515 0.35623 0.23513 -0.00608 -0.00917 0.07224  295 ASP   A N   
2273 C CA  . ASP   A 295 ? 0.28734 0.35289 0.24762 -0.00419 -0.00559 0.07074  295 ASP   A CA  
2274 C C   . ASP   A 295 ? 0.36797 0.44232 0.33078 -0.00608 -0.00098 0.07893  295 ASP   A C   
2275 O O   . ASP   A 295 ? 0.34341 0.42120 0.30702 -0.00544 0.00562  0.07547  295 ASP   A O   
2276 C CB  . ASP   A 295 ? 0.28288 0.33769 0.25625 -0.00241 -0.01062 0.07252  295 ASP   A CB  
2277 C CG  . ASP   A 295 ? 0.26395 0.31048 0.23606 -0.00027 -0.01342 0.06409  295 ASP   A CG  
2278 O OD1 . ASP   A 295 ? 0.35678 0.40422 0.32063 -0.00008 -0.01103 0.05643  295 ASP   A OD1 
2279 O OD2 . ASP   A 295 ? 0.22016 0.25873 0.19965 0.00096  -0.01727 0.06487  295 ASP   A OD2 
2280 N N   . VAL   A 296 ? 0.31293 0.39096 0.27930 -0.00809 -0.00400 0.09087  296 VAL   A N   
2281 C CA  . VAL   A 296 ? 0.36066 0.44797 0.32980 -0.01074 0.00039  0.10074  296 VAL   A CA  
2282 C C   . VAL   A 296 ? 0.38460 0.48417 0.33906 -0.01214 0.00826  0.09686  296 VAL   A C   
2283 O O   . VAL   A 296 ? 0.39336 0.49865 0.35172 -0.01227 0.01552  0.09741  296 VAL   A O   
2284 C CB  . VAL   A 296 ? 0.24515 0.33500 0.21798 -0.01279 -0.00408 0.11533  296 VAL   A CB  
2285 C CG1 . VAL   A 296 ? 0.30233 0.40414 0.27480 -0.01633 0.00112  0.12638  296 VAL   A CG1 
2286 C CG2 . VAL   A 296 ? 0.22205 0.29797 0.21181 -0.01156 -0.00900 0.11828  296 VAL   A CG2 
2287 N N   . VAL   A 297 ? 0.36021 0.46448 0.29783 -0.01354 0.00730  0.09237  297 VAL   A N   
2288 C CA  . VAL   A 297 ? 0.36784 0.48258 0.28840 -0.01582 0.01527  0.08655  297 VAL   A CA  
2289 C C   . VAL   A 297 ? 0.44040 0.54861 0.36274 -0.01233 0.02278  0.07263  297 VAL   A C   
2290 O O   . VAL   A 297 ? 0.50410 0.61907 0.42374 -0.01200 0.03261  0.07028  297 VAL   A O   
2291 C CB  . VAL   A 297 ? 0.38678 0.50822 0.28821 -0.01976 0.01103  0.08431  297 VAL   A CB  
2292 C CG1 . VAL   A 297 ? 0.31348 0.44284 0.19441 -0.02294 0.01972  0.07381  297 VAL   A CG1 
2293 C CG2 . VAL   A 297 ? 0.37286 0.50439 0.27370 -0.02276 0.00445  0.10127  297 VAL   A CG2 
2294 N N   . ARG   A 298 ? 0.42009 0.51561 0.34814 -0.00927 0.01895  0.06412  298 ARG   A N   
2295 C CA  . ARG   A 298 ? 0.47617 0.56482 0.40978 -0.00514 0.02546  0.05373  298 ARG   A CA  
2296 C C   . ARG   A 298 ? 0.49505 0.58786 0.44459 -0.00262 0.03070  0.05963  298 ARG   A C   
2297 O O   . ARG   A 298 ? 0.62878 0.72573 0.57906 -0.00026 0.04063  0.05496  298 ARG   A O   
2298 C CB  . ARG   A 298 ? 0.47123 0.54630 0.41119 -0.00249 0.01937  0.04750  298 ARG   A CB  
2299 C CG  . ARG   A 298 ? 0.71123 0.77890 0.66071 0.00258  0.02523  0.03971  298 ARG   A CG  
2300 C CD  . ARG   A 298 ? 0.63898 0.69414 0.59154 0.00457  0.02040  0.03357  298 ARG   A CD  
2301 N NE  . ARG   A 298 ? 0.50883 0.55857 0.47065 0.00505  0.01160  0.03848  298 ARG   A NE  
2302 C CZ  . ARG   A 298 ? 0.45090 0.49738 0.42605 0.00778  0.00987  0.04097  298 ARG   A CZ  
2303 N NH1 . ARG   A 298 ? 0.44197 0.49004 0.42552 0.01133  0.01590  0.03976  298 ARG   A NH1 
2304 N NH2 . ARG   A 298 ? 0.41094 0.45245 0.39073 0.00707  0.00223  0.04393  298 ARG   A NH2 
2305 N N   . GLN   A 299 ? 0.39746 0.48983 0.36062 -0.00344 0.02463  0.06989  299 GLN   A N   
2306 C CA  . GLN   A 299 ? 0.43678 0.53302 0.41759 -0.00217 0.02766  0.07521  299 GLN   A CA  
2307 C C   . GLN   A 299 ? 0.45864 0.56946 0.43958 -0.00477 0.03512  0.08378  299 GLN   A C   
2308 O O   . GLN   A 299 ? 0.45491 0.57324 0.44545 -0.00266 0.04314  0.08392  299 GLN   A O   
2309 C CB  . GLN   A 299 ? 0.32818 0.41652 0.32259 -0.00339 0.01802  0.08074  299 GLN   A CB  
2310 C CG  . GLN   A 299 ? 0.33466 0.42667 0.34795 -0.00343 0.01871  0.08512  299 GLN   A CG  
2311 C CD  . GLN   A 299 ? 0.28858 0.37048 0.31214 -0.00497 0.00909  0.08584  299 GLN   A CD  
2312 O OE1 . GLN   A 299 ? 0.28207 0.36736 0.32064 -0.00741 0.00727  0.09070  299 GLN   A OE1 
2313 N NE2 . GLN   A 299 ? 0.23889 0.30928 0.25436 -0.00411 0.00320  0.08058  299 GLN   A NE2 
2314 N N   . CYS   A 300 ? 0.44836 0.56463 0.42007 -0.00913 0.03295  0.09222  300 CYS   A N   
2315 C CA  . CYS   A 300 ? 0.46094 0.59182 0.43221 -0.01243 0.03969  0.10262  300 CYS   A CA  
2316 C C   . CYS   A 300 ? 0.56893 0.71055 0.52097 -0.01265 0.05033  0.09654  300 CYS   A C   
2317 O O   . CYS   A 300 ? 0.60984 0.76545 0.55773 -0.01576 0.05707  0.10500  300 CYS   A O   
2318 C CB  . CYS   A 300 ? 0.38129 0.51329 0.35204 -0.01705 0.03254  0.11648  300 CYS   A CB  
2319 S SG  . CYS   A 300 ? 0.35467 0.47220 0.34751 -0.01766 0.02186  0.12270  300 CYS   A SG  
2320 N N   . SER   A 301 ? 0.63850 0.77351 0.57850 -0.01001 0.05244  0.08185  301 SER   A N   
2321 C CA  . SER   A 301 ? 0.69613 0.83793 0.61569 -0.01082 0.06266  0.07231  301 SER   A CA  
2322 C C   . SER   A 301 ? 0.71711 0.85099 0.64130 -0.00479 0.07115  0.05758  301 SER   A C   
2323 O O   . SER   A 301 ? 0.76322 0.90323 0.67967 -0.00345 0.08422  0.05038  301 SER   A O   
2324 C CB  . SER   A 301 ? 0.73499 0.87630 0.63178 -0.01570 0.05589  0.06911  301 SER   A CB  
2325 O OG  . SER   A 301 ? 0.85953 1.00153 0.73592 -0.01690 0.06386  0.05434  301 SER   A OG  
2326 N N   . GLY   A 302 ? 0.79957 0.91976 0.73653 -0.00091 0.06457  0.05331  302 GLY   A N   
2327 C CA  . GLY   A 302 ? 0.80609 0.91975 0.75545 0.00587  0.07180  0.04458  302 GLY   A CA  
2328 C C   . GLY   A 302 ? 0.96512 1.06529 0.90384 0.00778  0.07377  0.02924  302 GLY   A C   
2329 O O   . GLY   A 302 ? 0.92577 1.02337 0.86570 0.01230  0.08554  0.01981  302 GLY   A O   
2330 N N   . VAL   A 303 ? 1.17178 1.26280 1.10230 0.00461  0.06288  0.02692  303 VAL   A N   
2331 C CA  . VAL   A 303 ? 1.25096 1.32996 1.16916 0.00396  0.06363  0.01295  303 VAL   A CA  
2332 C C   . VAL   A 303 ? 1.20861 1.27435 1.14382 0.01048  0.06399  0.00881  303 VAL   A C   
2333 O O   . VAL   A 303 ? 1.15249 1.21589 1.10268 0.01251  0.05565  0.01681  303 VAL   A O   
2334 C CB  . VAL   A 303 ? 1.20933 1.28711 1.11400 -0.00249 0.05175  0.01398  303 VAL   A CB  
2335 C CG1 . VAL   A 303 ? 1.23985 1.30497 1.13508 -0.00420 0.05099  0.00033  303 VAL   A CG1 
2336 C CG2 . VAL   A 303 ? 1.07171 1.16432 0.95890 -0.00896 0.05140  0.01935  303 VAL   A CG2 
2337 N N   . THR   A 304 ? 1.23937 1.29590 1.17168 0.01346  0.07389  -0.00382 304 THR   A N   
2338 C CA  . THR   A 304 ? 1.21894 1.26292 1.16787 0.02045  0.07679  -0.00735 304 THR   A CA  
2339 C C   . THR   A 304 ? 1.42647 1.45439 1.36610 0.01773  0.07351  -0.01789 304 THR   A C   
2340 O O   . THR   A 304 ? 1.39804 1.42601 1.31942 0.01012  0.06792  -0.02223 304 THR   A O   
2341 C CB  . THR   A 304 ? 1.12491 1.16993 1.08297 0.02741  0.09269  -0.01225 304 THR   A CB  
2342 O OG1 . THR   A 304 ? 1.22180 1.26094 1.16017 0.02451  0.10296  -0.02749 304 THR   A OG1 
2343 C CG2 . THR   A 304 ? 1.01190 1.07521 0.97920 0.02902  0.09675  -0.00157 304 THR   A CG2 
2344 N N   . PHE   A 305 ? 1.65941 1.67450 1.61305 0.02377  0.07705  -0.02102 305 PHE   A N   
2345 C CA  . PHE   A 305 ? 1.70262 1.70163 1.65241 0.02152  0.07353  -0.02849 305 PHE   A CA  
2346 C C   . PHE   A 305 ? 1.71521 1.69940 1.67666 0.02835  0.08473  -0.03584 305 PHE   A C   
2347 O O   . PHE   A 305 ? 1.77454 1.76175 1.75368 0.03682  0.09216  -0.03102 305 PHE   A O   
2348 C CB  . PHE   A 305 ? 1.64462 1.64289 1.60267 0.02094  0.06006  -0.01845 305 PHE   A CB  
2349 C CG  . PHE   A 305 ? 1.58259 1.59319 1.53294 0.01569  0.05003  -0.01084 305 PHE   A CG  
2350 C CD1 . PHE   A 305 ? 1.57003 1.58273 1.50239 0.00794  0.04555  -0.01545 305 PHE   A CD1 
2351 C CD2 . PHE   A 305 ? 1.54118 1.56174 1.50310 0.01820  0.04537  0.00111  305 PHE   A CD2 
2352 C CE1 . PHE   A 305 ? 1.57236 1.59625 1.49993 0.00415  0.03701  -0.00717 305 PHE   A CE1 
2353 C CE2 . PHE   A 305 ? 1.54208 1.57159 1.49823 0.01368  0.03729  0.00788  305 PHE   A CE2 
2354 C CZ  . PHE   A 305 ? 1.55663 1.58762 1.49624 0.00732  0.03344  0.00425  305 PHE   A CZ  
2355 N N   . GLN   A 306 ? 1.20790 1.17610 1.16118 0.02451  0.08575  -0.04682 306 GLN   A N   
2356 C CA  . GLN   A 306 ? 1.18530 1.13533 1.15026 0.03043  0.09609  -0.05402 306 GLN   A CA  
2357 C C   . GLN   A 306 ? 1.04872 0.98336 1.01402 0.02644  0.08930  -0.05601 306 GLN   A C   
2358 O O   . GLN   A 306 ? 1.03519 0.96120 1.01885 0.03262  0.08879  -0.04899 306 GLN   A O   
2359 C CB  . GLN   A 306 ? 1.16402 1.10676 1.11663 0.02935  0.11114  -0.07094 306 GLN   A CB  
2360 C CG  . GLN   A 306 ? 1.07344 1.02801 1.03244 0.03660  0.12320  -0.06946 306 GLN   A CG  
2361 C CD  . GLN   A 306 ? 1.04732 0.99849 1.03656 0.04985  0.13087  -0.06142 306 GLN   A CD  
2362 O OE1 . GLN   A 306 ? 1.01387 0.95009 1.01155 0.05606  0.14478  -0.07080 306 GLN   A OE1 
2363 N NE2 . GLN   A 306 ? 0.93497 0.90038 0.94125 0.05407  0.12184  -0.04390 306 GLN   A NE2 
2364 N N   . A1ARU B .   ? 0.49078 0.49025 0.32189 -0.00958 0.02550  -0.02535 401 A1ARU A N   
2365 C C   . A1ARU B .   ? 0.56056 0.54072 0.38212 -0.01081 0.02972  -0.04896 401 A1ARU A C   
2366 O O   . A1ARU B .   ? 0.47745 0.46324 0.32412 -0.00902 0.01385  -0.02855 401 A1ARU A O   
2367 C C1  . A1ARU B .   ? 0.50606 0.49494 0.34032 -0.00969 0.02189  -0.03320 401 A1ARU A C1  
2368 C C10 . A1ARU B .   ? 0.39904 0.38952 0.25617 -0.01918 -0.01933 -0.01032 401 A1ARU A C10 
2369 C C11 . A1ARU B .   ? 0.57036 0.58830 0.39465 -0.01331 0.02436  -0.00526 401 A1ARU A C11 
2370 C C12 . A1ARU B .   ? 0.56209 0.58495 0.40137 -0.00871 0.03279  -0.00038 401 A1ARU A C12 
2371 C C13 . A1ARU B .   ? 0.55107 0.52565 0.35667 -0.01927 0.02136  -0.05608 401 A1ARU A C13 
2372 C C14 . A1ARU B .   ? 0.58265 0.56983 0.36667 -0.02717 0.01557  -0.05032 401 A1ARU A C14 
2373 C C15 . A1ARU B .   ? 0.58973 0.56240 0.43414 0.00280  0.04982  -0.05832 401 A1ARU A C15 
2374 C C16 . A1ARU B .   ? 0.59076 0.55715 0.46006 0.01209  0.05572  -0.05932 401 A1ARU A C16 
2375 C C17 . A1ARU B .   ? 0.64753 0.59792 0.44202 -0.02590 0.02208  -0.08126 401 A1ARU A C17 
2376 C C18 . A1ARU B .   ? 0.52162 0.47492 0.33176 -0.02668 0.00917  -0.06918 401 A1ARU A C18 
2377 C C19 . A1ARU B .   ? 0.62461 0.55688 0.43030 -0.02057 0.03160  -0.09396 401 A1ARU A C19 
2378 C C2  . A1ARU B .   ? 0.50154 0.50905 0.33763 -0.01092 0.01862  -0.01097 401 A1ARU A C2  
2379 C C20 . A1ARU B .   ? 0.56321 0.51665 0.32803 -0.03732 0.01843  -0.08977 401 A1ARU A C20 
2380 C C21 . A1ARU B .   ? 0.63611 0.66711 0.46056 -0.01054 0.04341  -0.00223 401 A1ARU A C21 
2381 C C22 . A1ARU B .   ? 0.69517 0.73302 0.53501 -0.00638 0.05355  0.00122  401 A1ARU A C22 
2382 C C23 . A1ARU B .   ? 0.59121 0.62336 0.45076 0.00067  0.05702  -0.00609 401 A1ARU A C23 
2383 C C24 . A1ARU B .   ? 0.55709 0.58201 0.42975 0.00159  0.04548  -0.00261 401 A1ARU A C24 
2384 C C25 . A1ARU B .   ? 0.57496 0.59183 0.43309 -0.00210 0.03690  -0.00694 401 A1ARU A C25 
2385 C C3  . A1ARU B .   ? 0.48527 0.49328 0.31551 -0.01593 0.00662  -0.00629 401 A1ARU A C3  
2386 C C4  . A1ARU B .   ? 0.45695 0.46826 0.30204 -0.01720 -0.01053 0.01059  401 A1ARU A C4  
2387 C C5  . A1ARU B .   ? 0.38973 0.40566 0.24527 -0.01507 -0.01185 0.02405  401 A1ARU A C5  
2388 C C6  . A1ARU B .   ? 0.39169 0.39648 0.24736 -0.01646 -0.01640 0.00685  401 A1ARU A C6  
2389 C C7  . A1ARU B .   ? 0.40654 0.40438 0.25235 -0.01940 -0.01467 -0.00676 401 A1ARU A C7  
2390 C C8  . A1ARU B .   ? 0.42788 0.43121 0.25258 -0.02761 -0.01974 -0.00903 401 A1ARU A C8  
2391 C C9  . A1ARU B .   ? 0.43341 0.43045 0.25825 -0.03219 -0.02605 -0.01687 401 A1ARU A C9  
2392 F F17 . A1ARU B .   ? 0.62224 0.59648 0.49911 0.01782  0.06681  -0.05835 401 A1ARU A F17 
2393 F F18 . A1ARU B .   ? 0.67070 0.62180 0.53929 0.01285  0.05889  -0.07125 401 A1ARU A F18 
2394 F F19 . A1ARU B .   ? 0.54684 0.51567 0.43268 0.01375  0.04693  -0.04863 401 A1ARU A F19 
2395 N N1  . A1ARU B .   ? 0.44347 0.45112 0.28954 -0.01379 -0.00003 0.00236  401 A1ARU A N1  
2396 N N2  . A1ARU B .   ? 0.41374 0.40341 0.26000 -0.02616 -0.02509 -0.01580 401 A1ARU A N2  
2397 N N3  . A1ARU B .   ? 0.58801 0.55844 0.42739 -0.00316 0.03728  -0.05516 401 A1ARU A N3  
2398 N N4  . A1ARU B .   ? 0.38809 0.40801 0.24569 -0.01652 -0.01930 0.03353  401 A1ARU A N4  
2399 O O1  . A1ARU B .   ? 0.56239 0.57214 0.37415 -0.02191 0.00351  -0.01040 401 A1ARU A O1  
2400 O O3  . A1ARU B .   ? 0.38304 0.36971 0.25661 -0.01400 -0.01798 -0.00814 401 A1ARU A O3  
2401 O O4  . A1ARU B .   ? 0.57292 0.53458 0.37069 -0.01985 0.02930  -0.07301 401 A1ARU A O4  
2402 O O6  . A1ARU B .   ? 0.68842 0.66941 0.51880 0.00093  0.05642  -0.05916 401 A1ARU A O6  
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