data_9EAJ
# 
_entry.id   9EAJ 
# 
_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   9EAJ         pdb_00009eaj 10.2210/pdb9eaj/pdb 
WWPDB D_1000290012 ?            ?                   
EMDB  EMD-47833    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-03-05 ? 
2  'EM metadata'     1 0 2025-03-05 ? 
3  'Additional map'  1 0 2025-03-05 1 
4  'Additional map'  1 0 2025-03-05 2 
5  'Additional map'  1 0 2025-03-05 3 
6  'Half map'        1 0 2025-03-05 1 
7  'Half map'        1 0 2025-03-05 2 
8  Image             1 0 2025-03-05 ? 
9  'Primary map'     1 0 2025-03-05 ? 
10 'Structure model' 1 1 2025-03-19 ? 
11 'Structure model' 1 2 2025-03-26 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 'Additional map'  repository 'Initial release' ? ? 
5 5 'Additional map'  repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 'Half map'        repository 'Initial release' ? ? 
8 8 Image             repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'     
2 10 'Structure model' 'Database references' 
3 11 'Structure model' 'Data collection'     
4 11 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
4 11 'Structure model' citation        
5 11 'Structure model' citation_author 
6 11 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  10 'Structure model' '_citation.country'                 
2  10 'Structure model' '_citation.journal_abbrev'          
3  10 'Structure model' '_citation.journal_id_ASTM'         
4  10 'Structure model' '_citation.journal_id_CSD'          
5  10 'Structure model' '_citation.journal_id_ISSN'         
6  10 'Structure model' '_citation.journal_volume'          
7  10 'Structure model' '_citation.pdbx_database_id_DOI'    
8  10 'Structure model' '_citation.title'                   
9  10 'Structure model' '_citation.year'                    
10 10 'Structure model' '_citation_author.identifier_ORCID' 
11 10 'Structure model' '_em_admin.last_update'             
12 11 'Structure model' '_citation.page_first'              
13 11 'Structure model' '_citation.page_last'               
14 11 'Structure model' '_citation.pdbx_database_id_PubMed' 
15 11 'Structure model' '_citation.title'                   
16 11 'Structure model' '_citation_author.identifier_ORCID' 
17 11 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EAJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-11 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                       9EAH      unspecified            
PDB  .                                                                                       9EAI      unspecified            
EMDB 'Structure of nanobody AT206 in complex with the angiotensin II type I receptor (AT1R)' EMD-47833 'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              andrew_kruse@hms.harvard.edu 
_pdbx_contact_author.name_first         Andrew 
_pdbx_contact_author.name_last          Kruse 
_pdbx_contact_author.name_mi            C 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1467-1222 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Skiba, M.A.' 1 0000-0003-4615-6775 
'Kruse, A.C.' 2 0000-0002-1467-1222 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2423931122 
_citation.page_last                 e2423931122 
_citation.title                     'Epitope-directed selection of GPCR nanobody ligands with evolvable function.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2423931122 
_citation.pdbx_database_id_PubMed   40067891 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Skiba, M.A.'  1 0000-0003-4615-6775 
primary 'Canavan, C.'  2 0000-0003-0648-2373 
primary 'Nemeth, G.R.' 3 ?                   
primary 'Liu, J.'      4 ?                   
primary 'Kanso, A.'    5 0009-0003-6417-9556 
primary 'Kruse, A.C.'  6 0000-0002-1467-1222 
# 
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 'Nanobody AT206,Type-1 angiotensin II receptor,Soluble cytochrome b562' 65542.836 2 ? 'M232W,  H327I, R331L' ? ? 
2 polymer man 'BAG2 Anti-BRIL Fab Heavy Chain'                                        24539.314 1 ? ?                      ? ? 
3 polymer man 'BAG2 Anti-BRIL Fab Light Chain'                                        23541.164 1 ? ?                      ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'AT1AR,AT1BR,Angiotensin II type-1 receptor,AT1 receptor,Cytochrome b-562' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;QVQLQESGGGLVQAGGSLRLSCAASGSISYYRMGWYRQAPGKEREFVAGIGVGTTTNYADSVKGRFTISRDNAKNTVYLQ
MNSLKPEDTAVYYCAAYNYFPRSIVYYYVYWGQGTQVTVSSGGSGEDQVDPRLIDGKILNSSTEDGIKRIQDDCPKAGRH
NYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIA
SASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHY
ESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYDLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALD
AQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLERARSTLDKLNDD
IFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLL
KYGGSSLEVLFQGPTETSQVAPA
;
;QVQLQESGGGLVQAGGSLRLSCAASGSISYYRMGWYRQAPGKEREFVAGIGVGTTTNYADSVKGRFTISRDNAKNTVYLQ
MNSLKPEDTAVYYCAAYNYFPRSIVYYYVYWGQGTQVTVSSGGSGEDQVDPRLIDGKILNSSTEDGIKRIQDDCPKAGRH
NYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIA
SASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHY
ESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYDLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALD
AQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLERARSTLDKLNDD
IFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLL
KYGGSSLEVLFQGPTETSQVAPA
;
A,B ? 
2 'polypeptide(L)' no no 
;EISEVQLVESGGGLVQPGGSLRLSCAASGFNVVDFSLHWVRQAPGKGLEWVAYISSSSGSTSYADSVKGRFTISADTSKN
TAYLQMNSLRAEDTAVYYCARWGYWPGEPWWKAFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCD
;
;EISEVQLVESGGGLVQPGGSLRLSCAASGFNVVDFSLHWVRQAPGKGLEWVAYISSSSGSTSYADSVKGRFTISADTSKN
TAYLQMNSLRAEDTAVYYCARWGYWPGEPWWKAFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYF
PEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCD
;
C   ? 
3 'polypeptide(L)' no no 
;DIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQP
EDFATYYCQQYLYYSLVTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;DIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQP
EDFATYYCQQYLYYSLVTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
D   ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   GLN n 
1 4   LEU n 
1 5   GLN n 
1 6   GLU n 
1 7   SER n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  LEU n 
1 12  VAL n 
1 13  GLN n 
1 14  ALA n 
1 15  GLY n 
1 16  GLY n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  LEU n 
1 21  SER n 
1 22  CYS n 
1 23  ALA n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  SER n 
1 28  ILE n 
1 29  SER n 
1 30  TYR n 
1 31  TYR n 
1 32  ARG n 
1 33  MET n 
1 34  GLY n 
1 35  TRP n 
1 36  TYR n 
1 37  ARG n 
1 38  GLN n 
1 39  ALA n 
1 40  PRO n 
1 41  GLY n 
1 42  LYS n 
1 43  GLU n 
1 44  ARG n 
1 45  GLU n 
1 46  PHE n 
1 47  VAL n 
1 48  ALA n 
1 49  GLY n 
1 50  ILE n 
1 51  GLY n 
1 52  VAL n 
1 53  GLY n 
1 54  THR n 
1 55  THR n 
1 56  THR n 
1 57  ASN n 
1 58  TYR n 
1 59  ALA n 
1 60  ASP n 
1 61  SER n 
1 62  VAL n 
1 63  LYS n 
1 64  GLY n 
1 65  ARG n 
1 66  PHE n 
1 67  THR n 
1 68  ILE n 
1 69  SER n 
1 70  ARG n 
1 71  ASP n 
1 72  ASN n 
1 73  ALA n 
1 74  LYS n 
1 75  ASN n 
1 76  THR n 
1 77  VAL n 
1 78  TYR n 
1 79  LEU n 
1 80  GLN n 
1 81  MET n 
1 82  ASN n 
1 83  SER n 
1 84  LEU n 
1 85  LYS n 
1 86  PRO n 
1 87  GLU n 
1 88  ASP n 
1 89  THR n 
1 90  ALA n 
1 91  VAL n 
1 92  TYR n 
1 93  TYR n 
1 94  CYS n 
1 95  ALA n 
1 96  ALA n 
1 97  TYR n 
1 98  ASN n 
1 99  TYR n 
1 100 PHE n 
1 101 PRO n 
1 102 ARG n 
1 103 SER n 
1 104 ILE n 
1 105 VAL n 
1 106 TYR n 
1 107 TYR n 
1 108 TYR n 
1 109 VAL n 
1 110 TYR n 
1 111 TRP n 
1 112 GLY n 
1 113 GLN n 
1 114 GLY n 
1 115 THR n 
1 116 GLN n 
1 117 VAL n 
1 118 THR n 
1 119 VAL n 
1 120 SER n 
1 121 SER n 
1 122 GLY n 
1 123 GLY n 
1 124 SER n 
1 125 GLY n 
1 126 GLU n 
1 127 ASP n 
1 128 GLN n 
1 129 VAL n 
1 130 ASP n 
1 131 PRO n 
1 132 ARG n 
1 133 LEU n 
1 134 ILE n 
1 135 ASP n 
1 136 GLY n 
1 137 LYS n 
1 138 ILE n 
1 139 LEU n 
1 140 ASN n 
1 141 SER n 
1 142 SER n 
1 143 THR n 
1 144 GLU n 
1 145 ASP n 
1 146 GLY n 
1 147 ILE n 
1 148 LYS n 
1 149 ARG n 
1 150 ILE n 
1 151 GLN n 
1 152 ASP n 
1 153 ASP n 
1 154 CYS n 
1 155 PRO n 
1 156 LYS n 
1 157 ALA n 
1 158 GLY n 
1 159 ARG n 
1 160 HIS n 
1 161 ASN n 
1 162 TYR n 
1 163 ILE n 
1 164 PHE n 
1 165 VAL n 
1 166 MET n 
1 167 ILE n 
1 168 PRO n 
1 169 THR n 
1 170 LEU n 
1 171 TYR n 
1 172 SER n 
1 173 ILE n 
1 174 ILE n 
1 175 PHE n 
1 176 VAL n 
1 177 VAL n 
1 178 GLY n 
1 179 ILE n 
1 180 PHE n 
1 181 GLY n 
1 182 ASN n 
1 183 SER n 
1 184 LEU n 
1 185 VAL n 
1 186 VAL n 
1 187 ILE n 
1 188 VAL n 
1 189 ILE n 
1 190 TYR n 
1 191 PHE n 
1 192 TYR n 
1 193 MET n 
1 194 LYS n 
1 195 LEU n 
1 196 LYS n 
1 197 THR n 
1 198 VAL n 
1 199 ALA n 
1 200 SER n 
1 201 VAL n 
1 202 PHE n 
1 203 LEU n 
1 204 LEU n 
1 205 ASN n 
1 206 LEU n 
1 207 ALA n 
1 208 LEU n 
1 209 ALA n 
1 210 ASP n 
1 211 LEU n 
1 212 CYS n 
1 213 PHE n 
1 214 LEU n 
1 215 LEU n 
1 216 THR n 
1 217 LEU n 
1 218 PRO n 
1 219 LEU n 
1 220 TRP n 
1 221 ALA n 
1 222 VAL n 
1 223 TYR n 
1 224 THR n 
1 225 ALA n 
1 226 MET n 
1 227 GLU n 
1 228 TYR n 
1 229 ARG n 
1 230 TRP n 
1 231 PRO n 
1 232 PHE n 
1 233 GLY n 
1 234 ASN n 
1 235 TYR n 
1 236 LEU n 
1 237 CYS n 
1 238 LYS n 
1 239 ILE n 
1 240 ALA n 
1 241 SER n 
1 242 ALA n 
1 243 SER n 
1 244 VAL n 
1 245 SER n 
1 246 PHE n 
1 247 ASN n 
1 248 LEU n 
1 249 TYR n 
1 250 ALA n 
1 251 SER n 
1 252 VAL n 
1 253 PHE n 
1 254 LEU n 
1 255 LEU n 
1 256 THR n 
1 257 CYS n 
1 258 LEU n 
1 259 SER n 
1 260 ILE n 
1 261 ASP n 
1 262 ARG n 
1 263 TYR n 
1 264 LEU n 
1 265 ALA n 
1 266 ILE n 
1 267 VAL n 
1 268 HIS n 
1 269 PRO n 
1 270 MET n 
1 271 LYS n 
1 272 SER n 
1 273 ARG n 
1 274 LEU n 
1 275 ARG n 
1 276 ARG n 
1 277 THR n 
1 278 MET n 
1 279 LEU n 
1 280 VAL n 
1 281 ALA n 
1 282 LYS n 
1 283 VAL n 
1 284 THR n 
1 285 CYS n 
1 286 ILE n 
1 287 ILE n 
1 288 ILE n 
1 289 TRP n 
1 290 LEU n 
1 291 LEU n 
1 292 ALA n 
1 293 GLY n 
1 294 LEU n 
1 295 ALA n 
1 296 SER n 
1 297 LEU n 
1 298 PRO n 
1 299 ALA n 
1 300 ILE n 
1 301 ILE n 
1 302 HIS n 
1 303 ARG n 
1 304 ASN n 
1 305 VAL n 
1 306 PHE n 
1 307 PHE n 
1 308 ILE n 
1 309 GLU n 
1 310 ASN n 
1 311 THR n 
1 312 ASN n 
1 313 ILE n 
1 314 THR n 
1 315 VAL n 
1 316 CYS n 
1 317 ALA n 
1 318 PHE n 
1 319 HIS n 
1 320 TYR n 
1 321 GLU n 
1 322 SER n 
1 323 GLN n 
1 324 ASN n 
1 325 SER n 
1 326 THR n 
1 327 LEU n 
1 328 PRO n 
1 329 ILE n 
1 330 GLY n 
1 331 LEU n 
1 332 GLY n 
1 333 LEU n 
1 334 THR n 
1 335 LYS n 
1 336 ASN n 
1 337 ILE n 
1 338 LEU n 
1 339 GLY n 
1 340 PHE n 
1 341 LEU n 
1 342 PHE n 
1 343 PRO n 
1 344 PHE n 
1 345 LEU n 
1 346 ILE n 
1 347 ILE n 
1 348 LEU n 
1 349 THR n 
1 350 SER n 
1 351 TYR n 
1 352 THR n 
1 353 LEU n 
1 354 ILE n 
1 355 TRP n 
1 356 LYS n 
1 357 ALA n 
1 358 LEU n 
1 359 LYS n 
1 360 LYS n 
1 361 ALA n 
1 362 TYR n 
1 363 ASP n 
1 364 LEU n 
1 365 GLU n 
1 366 ASP n 
1 367 ASN n 
1 368 TRP n 
1 369 GLU n 
1 370 THR n 
1 371 LEU n 
1 372 ASN n 
1 373 ASP n 
1 374 ASN n 
1 375 LEU n 
1 376 LYS n 
1 377 VAL n 
1 378 ILE n 
1 379 GLU n 
1 380 LYS n 
1 381 ALA n 
1 382 ASP n 
1 383 ASN n 
1 384 ALA n 
1 385 ALA n 
1 386 GLN n 
1 387 VAL n 
1 388 LYS n 
1 389 ASP n 
1 390 ALA n 
1 391 LEU n 
1 392 THR n 
1 393 LYS n 
1 394 MET n 
1 395 ARG n 
1 396 ALA n 
1 397 ALA n 
1 398 ALA n 
1 399 LEU n 
1 400 ASP n 
1 401 ALA n 
1 402 GLN n 
1 403 LYS n 
1 404 ALA n 
1 405 THR n 
1 406 PRO n 
1 407 PRO n 
1 408 LYS n 
1 409 LEU n 
1 410 GLU n 
1 411 ASP n 
1 412 LYS n 
1 413 SER n 
1 414 PRO n 
1 415 ASP n 
1 416 SER n 
1 417 PRO n 
1 418 GLU n 
1 419 MET n 
1 420 LYS n 
1 421 ASP n 
1 422 PHE n 
1 423 ARG n 
1 424 HIS n 
1 425 GLY n 
1 426 PHE n 
1 427 ASP n 
1 428 ILE n 
1 429 LEU n 
1 430 VAL n 
1 431 GLY n 
1 432 GLN n 
1 433 ILE n 
1 434 ASP n 
1 435 ASP n 
1 436 ALA n 
1 437 LEU n 
1 438 LYS n 
1 439 LEU n 
1 440 ALA n 
1 441 ASN n 
1 442 GLU n 
1 443 GLY n 
1 444 LYS n 
1 445 VAL n 
1 446 LYS n 
1 447 GLU n 
1 448 ALA n 
1 449 GLN n 
1 450 ALA n 
1 451 ALA n 
1 452 ALA n 
1 453 GLU n 
1 454 GLN n 
1 455 LEU n 
1 456 LYS n 
1 457 THR n 
1 458 THR n 
1 459 ARG n 
1 460 ASN n 
1 461 ALA n 
1 462 TYR n 
1 463 ILE n 
1 464 GLN n 
1 465 LYS n 
1 466 TYR n 
1 467 LEU n 
1 468 GLU n 
1 469 ARG n 
1 470 ALA n 
1 471 ARG n 
1 472 SER n 
1 473 THR n 
1 474 LEU n 
1 475 ASP n 
1 476 LYS n 
1 477 LEU n 
1 478 ASN n 
1 479 ASP n 
1 480 ASP n 
1 481 ILE n 
1 482 PHE n 
1 483 LYS n 
1 484 ILE n 
1 485 ILE n 
1 486 MET n 
1 487 ALA n 
1 488 ILE n 
1 489 VAL n 
1 490 LEU n 
1 491 PHE n 
1 492 PHE n 
1 493 PHE n 
1 494 PHE n 
1 495 SER n 
1 496 TRP n 
1 497 ILE n 
1 498 PRO n 
1 499 HIS n 
1 500 GLN n 
1 501 ILE n 
1 502 PHE n 
1 503 THR n 
1 504 PHE n 
1 505 LEU n 
1 506 ASP n 
1 507 VAL n 
1 508 LEU n 
1 509 ILE n 
1 510 GLN n 
1 511 LEU n 
1 512 GLY n 
1 513 ILE n 
1 514 ILE n 
1 515 ARG n 
1 516 ASP n 
1 517 CYS n 
1 518 ARG n 
1 519 ILE n 
1 520 ALA n 
1 521 ASP n 
1 522 ILE n 
1 523 VAL n 
1 524 ASP n 
1 525 THR n 
1 526 ALA n 
1 527 MET n 
1 528 PRO n 
1 529 ILE n 
1 530 THR n 
1 531 ILE n 
1 532 CYS n 
1 533 ILE n 
1 534 ALA n 
1 535 TYR n 
1 536 PHE n 
1 537 ASN n 
1 538 ASN n 
1 539 CYS n 
1 540 LEU n 
1 541 ASN n 
1 542 PRO n 
1 543 LEU n 
1 544 PHE n 
1 545 TYR n 
1 546 GLY n 
1 547 PHE n 
1 548 LEU n 
1 549 GLY n 
1 550 LYS n 
1 551 LYS n 
1 552 PHE n 
1 553 LYS n 
1 554 ARG n 
1 555 TYR n 
1 556 PHE n 
1 557 LEU n 
1 558 GLN n 
1 559 LEU n 
1 560 LEU n 
1 561 LYS n 
1 562 TYR n 
1 563 GLY n 
1 564 GLY n 
1 565 SER n 
1 566 SER n 
1 567 LEU n 
1 568 GLU n 
1 569 VAL n 
1 570 LEU n 
1 571 PHE n 
1 572 GLN n 
1 573 GLY n 
1 574 PRO n 
1 575 THR n 
1 576 GLU n 
1 577 THR n 
1 578 SER n 
1 579 GLN n 
1 580 VAL n 
1 581 ALA n 
1 582 PRO n 
1 583 ALA n 
2 1   GLU n 
2 2   ILE n 
2 3   SER n 
2 4   GLU n 
2 5   VAL n 
2 6   GLN n 
2 7   LEU n 
2 8   VAL n 
2 9   GLU n 
2 10  SER n 
2 11  GLY n 
2 12  GLY n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  GLN n 
2 17  PRO n 
2 18  GLY n 
2 19  GLY n 
2 20  SER n 
2 21  LEU n 
2 22  ARG n 
2 23  LEU n 
2 24  SER n 
2 25  CYS n 
2 26  ALA n 
2 27  ALA n 
2 28  SER n 
2 29  GLY n 
2 30  PHE n 
2 31  ASN n 
2 32  VAL n 
2 33  VAL n 
2 34  ASP n 
2 35  PHE n 
2 36  SER n 
2 37  LEU n 
2 38  HIS n 
2 39  TRP n 
2 40  VAL n 
2 41  ARG n 
2 42  GLN n 
2 43  ALA n 
2 44  PRO n 
2 45  GLY n 
2 46  LYS n 
2 47  GLY n 
2 48  LEU n 
2 49  GLU n 
2 50  TRP n 
2 51  VAL n 
2 52  ALA n 
2 53  TYR n 
2 54  ILE n 
2 55  SER n 
2 56  SER n 
2 57  SER n 
2 58  SER n 
2 59  GLY n 
2 60  SER n 
2 61  THR n 
2 62  SER n 
2 63  TYR n 
2 64  ALA n 
2 65  ASP n 
2 66  SER n 
2 67  VAL n 
2 68  LYS n 
2 69  GLY n 
2 70  ARG n 
2 71  PHE n 
2 72  THR n 
2 73  ILE n 
2 74  SER n 
2 75  ALA n 
2 76  ASP n 
2 77  THR n 
2 78  SER n 
2 79  LYS n 
2 80  ASN n 
2 81  THR n 
2 82  ALA n 
2 83  TYR n 
2 84  LEU n 
2 85  GLN n 
2 86  MET n 
2 87  ASN n 
2 88  SER n 
2 89  LEU n 
2 90  ARG n 
2 91  ALA n 
2 92  GLU n 
2 93  ASP n 
2 94  THR n 
2 95  ALA n 
2 96  VAL n 
2 97  TYR n 
2 98  TYR n 
2 99  CYS n 
2 100 ALA n 
2 101 ARG n 
2 102 TRP n 
2 103 GLY n 
2 104 TYR n 
2 105 TRP n 
2 106 PRO n 
2 107 GLY n 
2 108 GLU n 
2 109 PRO n 
2 110 TRP n 
2 111 TRP n 
2 112 LYS n 
2 113 ALA n 
2 114 PHE n 
2 115 ASP n 
2 116 TYR n 
2 117 TRP n 
2 118 GLY n 
2 119 GLN n 
2 120 GLY n 
2 121 THR n 
2 122 LEU n 
2 123 VAL n 
2 124 THR n 
2 125 VAL n 
2 126 SER n 
2 127 SER n 
2 128 ALA n 
2 129 SER n 
2 130 THR n 
2 131 LYS n 
2 132 GLY n 
2 133 PRO n 
2 134 SER n 
2 135 VAL n 
2 136 PHE n 
2 137 PRO n 
2 138 LEU n 
2 139 ALA n 
2 140 PRO n 
2 141 SER n 
2 142 SER n 
2 143 LYS n 
2 144 SER n 
2 145 THR n 
2 146 SER n 
2 147 GLY n 
2 148 GLY n 
2 149 THR n 
2 150 ALA n 
2 151 ALA n 
2 152 LEU n 
2 153 GLY n 
2 154 CYS n 
2 155 LEU n 
2 156 VAL n 
2 157 LYS n 
2 158 ASP n 
2 159 TYR n 
2 160 PHE n 
2 161 PRO n 
2 162 GLU n 
2 163 PRO n 
2 164 VAL n 
2 165 THR n 
2 166 VAL n 
2 167 SER n 
2 168 TRP n 
2 169 ASN n 
2 170 SER n 
2 171 GLY n 
2 172 ALA n 
2 173 LEU n 
2 174 THR n 
2 175 SER n 
2 176 GLY n 
2 177 VAL n 
2 178 HIS n 
2 179 THR n 
2 180 PHE n 
2 181 PRO n 
2 182 ALA n 
2 183 VAL n 
2 184 LEU n 
2 185 GLN n 
2 186 SER n 
2 187 SER n 
2 188 GLY n 
2 189 LEU n 
2 190 TYR n 
2 191 SER n 
2 192 LEU n 
2 193 SER n 
2 194 SER n 
2 195 VAL n 
2 196 VAL n 
2 197 THR n 
2 198 VAL n 
2 199 PRO n 
2 200 SER n 
2 201 SER n 
2 202 SER n 
2 203 LEU n 
2 204 GLY n 
2 205 THR n 
2 206 GLN n 
2 207 THR n 
2 208 TYR n 
2 209 ILE n 
2 210 CYS n 
2 211 ASN n 
2 212 VAL n 
2 213 ASN n 
2 214 HIS n 
2 215 LYS n 
2 216 PRO n 
2 217 SER n 
2 218 ASN n 
2 219 THR n 
2 220 LYS n 
2 221 VAL n 
2 222 ASP n 
2 223 LYS n 
2 224 LYS n 
2 225 VAL n 
2 226 GLU n 
2 227 PRO n 
2 228 LYS n 
2 229 SER n 
2 230 CYS n 
2 231 ASP n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   SER n 
3 10  SER n 
3 11  LEU n 
3 12  SER n 
3 13  ALA n 
3 14  SER n 
3 15  VAL n 
3 16  GLY n 
3 17  ASP n 
3 18  ARG n 
3 19  VAL n 
3 20  THR n 
3 21  ILE n 
3 22  THR n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  SER n 
3 29  VAL n 
3 30  SER n 
3 31  SER n 
3 32  ALA n 
3 33  VAL n 
3 34  ALA n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  LYS n 
3 43  ALA n 
3 44  PRO n 
3 45  LYS n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  SER n 
3 51  ALA n 
3 52  SER n 
3 53  SER n 
3 54  LEU n 
3 55  TYR n 
3 56  SER n 
3 57  GLY n 
3 58  VAL n 
3 59  PRO n 
3 60  SER n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  ARG n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  ASP n 
3 71  PHE n 
3 72  THR n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  PRO n 
3 81  GLU n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  THR n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  TYR n 
3 92  LEU n 
3 93  TYR n 
3 94  TYR n 
3 95  SER n 
3 96  LEU n 
3 97  VAL n 
3 98  THR n 
3 99  PHE n 
3 100 GLY n 
3 101 GLN n 
3 102 GLY n 
3 103 THR n 
3 104 LYS n 
3 105 VAL n 
3 106 GLU n 
3 107 ILE n 
3 108 LYS n 
3 109 ARG n 
3 110 THR n 
3 111 VAL n 
3 112 ALA n 
3 113 ALA n 
3 114 PRO n 
3 115 SER n 
3 116 VAL n 
3 117 PHE n 
3 118 ILE n 
3 119 PHE n 
3 120 PRO n 
3 121 PRO n 
3 122 SER n 
3 123 ASP n 
3 124 GLU n 
3 125 GLN n 
3 126 LEU n 
3 127 LYS n 
3 128 SER n 
3 129 GLY n 
3 130 THR n 
3 131 ALA n 
3 132 SER n 
3 133 VAL n 
3 134 VAL n 
3 135 CYS n 
3 136 LEU n 
3 137 LEU n 
3 138 ASN n 
3 139 ASN n 
3 140 PHE n 
3 141 TYR n 
3 142 PRO n 
3 143 ARG n 
3 144 GLU n 
3 145 ALA n 
3 146 LYS n 
3 147 VAL n 
3 148 GLN n 
3 149 TRP n 
3 150 LYS n 
3 151 VAL n 
3 152 ASP n 
3 153 ASN n 
3 154 ALA n 
3 155 LEU n 
3 156 GLN n 
3 157 SER n 
3 158 GLY n 
3 159 ASN n 
3 160 SER n 
3 161 GLN n 
3 162 GLU n 
3 163 SER n 
3 164 VAL n 
3 165 THR n 
3 166 GLU n 
3 167 GLN n 
3 168 ASP n 
3 169 SER n 
3 170 LYS n 
3 171 ASP n 
3 172 SER n 
3 173 THR n 
3 174 TYR n 
3 175 SER n 
3 176 LEU n 
3 177 SER n 
3 178 SER n 
3 179 THR n 
3 180 LEU n 
3 181 THR n 
3 182 LEU n 
3 183 SER n 
3 184 LYS n 
3 185 ALA n 
3 186 ASP n 
3 187 TYR n 
3 188 GLU n 
3 189 LYS n 
3 190 HIS n 
3 191 LYS n 
3 192 VAL n 
3 193 TYR n 
3 194 ALA n 
3 195 CYS n 
3 196 GLU n 
3 197 VAL n 
3 198 THR n 
3 199 HIS n 
3 200 GLN n 
3 201 GLY n 
3 202 LEU n 
3 203 SER n 
3 204 SER n 
3 205 PRO n 
3 206 VAL n 
3 207 THR n 
3 208 LYS n 
3 209 SER n 
3 210 PHE n 
3 211 ASN n 
3 212 ARG n 
3 213 GLY n 
3 214 GLU n 
3 215 CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   121 ?     ? ?                                      ? ? ? ? ? ? Camelidae             9835  ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 122 362 human ? 'AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B' ? ? ? ? ? ? 'Homo sapiens'        9606  ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 363 477 ?     ? cybC                                   ? ? ? ? ? ? 'Escherichia coli'    562   ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 4 sample 'Biological sequence' 478 583 human ? 'AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B' ? ? ? ? ? ? 'Homo sapiens'        9606  ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   231 ?     ? ?                                      ? ? ? ? ? ? 'synthetic construct' 32630 ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1   215 ?     ? ?                                      ? ? ? ? ? ? 'synthetic construct' 32630 ? 
? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? Expi293F ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
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   GLN 1   -135 ?    ?   ?   A . n 
A 1 2   VAL 2   -134 ?    ?   ?   A . n 
A 1 3   GLN 3   -133 ?    ?   ?   A . n 
A 1 4   LEU 4   -132 ?    ?   ?   A . n 
A 1 5   GLN 5   -131 ?    ?   ?   A . n 
A 1 6   GLU 6   -130 ?    ?   ?   A . n 
A 1 7   SER 7   -129 ?    ?   ?   A . n 
A 1 8   GLY 8   -128 ?    ?   ?   A . n 
A 1 9   GLY 9   -127 ?    ?   ?   A . n 
A 1 10  GLY 10  -126 ?    ?   ?   A . n 
A 1 11  LEU 11  -125 ?    ?   ?   A . n 
A 1 12  VAL 12  -124 ?    ?   ?   A . n 
A 1 13  GLN 13  -123 ?    ?   ?   A . n 
A 1 14  ALA 14  -122 ?    ?   ?   A . n 
A 1 15  GLY 15  -121 ?    ?   ?   A . n 
A 1 16  GLY 16  -120 ?    ?   ?   A . n 
A 1 17  SER 17  -119 ?    ?   ?   A . n 
A 1 18  LEU 18  -118 ?    ?   ?   A . n 
A 1 19  ARG 19  -117 ?    ?   ?   A . n 
A 1 20  LEU 20  -116 ?    ?   ?   A . n 
A 1 21  SER 21  -115 ?    ?   ?   A . n 
A 1 22  CYS 22  -114 ?    ?   ?   A . n 
A 1 23  ALA 23  -113 ?    ?   ?   A . n 
A 1 24  ALA 24  -112 ?    ?   ?   A . n 
A 1 25  SER 25  -111 ?    ?   ?   A . n 
A 1 26  GLY 26  -110 ?    ?   ?   A . n 
A 1 27  SER 27  -109 ?    ?   ?   A . n 
A 1 28  ILE 28  -108 ?    ?   ?   A . n 
A 1 29  SER 29  -107 ?    ?   ?   A . n 
A 1 30  TYR 30  -106 ?    ?   ?   A . n 
A 1 31  TYR 31  -105 ?    ?   ?   A . n 
A 1 32  ARG 32  -104 ?    ?   ?   A . n 
A 1 33  MET 33  -103 ?    ?   ?   A . n 
A 1 34  GLY 34  -102 ?    ?   ?   A . n 
A 1 35  TRP 35  -101 ?    ?   ?   A . n 
A 1 36  TYR 36  -100 ?    ?   ?   A . n 
A 1 37  ARG 37  -99  ?    ?   ?   A . n 
A 1 38  GLN 38  -98  ?    ?   ?   A . n 
A 1 39  ALA 39  -97  ?    ?   ?   A . n 
A 1 40  PRO 40  -96  ?    ?   ?   A . n 
A 1 41  GLY 41  -95  ?    ?   ?   A . n 
A 1 42  LYS 42  -94  ?    ?   ?   A . n 
A 1 43  GLU 43  -93  ?    ?   ?   A . n 
A 1 44  ARG 44  -92  ?    ?   ?   A . n 
A 1 45  GLU 45  -91  ?    ?   ?   A . n 
A 1 46  PHE 46  -90  ?    ?   ?   A . n 
A 1 47  VAL 47  -89  ?    ?   ?   A . n 
A 1 48  ALA 48  -88  ?    ?   ?   A . n 
A 1 49  GLY 49  -87  ?    ?   ?   A . n 
A 1 50  ILE 50  -86  ?    ?   ?   A . n 
A 1 51  GLY 51  -85  ?    ?   ?   A . n 
A 1 52  VAL 52  -84  ?    ?   ?   A . n 
A 1 53  GLY 53  -83  ?    ?   ?   A . n 
A 1 54  THR 54  -82  ?    ?   ?   A . n 
A 1 55  THR 55  -81  ?    ?   ?   A . n 
A 1 56  THR 56  -80  ?    ?   ?   A . n 
A 1 57  ASN 57  -79  ?    ?   ?   A . n 
A 1 58  TYR 58  -78  ?    ?   ?   A . n 
A 1 59  ALA 59  -77  ?    ?   ?   A . n 
A 1 60  ASP 60  -76  ?    ?   ?   A . n 
A 1 61  SER 61  -75  ?    ?   ?   A . n 
A 1 62  VAL 62  -74  ?    ?   ?   A . n 
A 1 63  LYS 63  -73  ?    ?   ?   A . n 
A 1 64  GLY 64  -72  ?    ?   ?   A . n 
A 1 65  ARG 65  -71  ?    ?   ?   A . n 
A 1 66  PHE 66  -70  ?    ?   ?   A . n 
A 1 67  THR 67  -69  ?    ?   ?   A . n 
A 1 68  ILE 68  -68  ?    ?   ?   A . n 
A 1 69  SER 69  -67  ?    ?   ?   A . n 
A 1 70  ARG 70  -66  ?    ?   ?   A . n 
A 1 71  ASP 71  -65  ?    ?   ?   A . n 
A 1 72  ASN 72  -64  ?    ?   ?   A . n 
A 1 73  ALA 73  -63  ?    ?   ?   A . n 
A 1 74  LYS 74  -62  ?    ?   ?   A . n 
A 1 75  ASN 75  -61  ?    ?   ?   A . n 
A 1 76  THR 76  -60  ?    ?   ?   A . n 
A 1 77  VAL 77  -59  ?    ?   ?   A . n 
A 1 78  TYR 78  -58  ?    ?   ?   A . n 
A 1 79  LEU 79  -57  ?    ?   ?   A . n 
A 1 80  GLN 80  -56  ?    ?   ?   A . n 
A 1 81  MET 81  -55  ?    ?   ?   A . n 
A 1 82  ASN 82  -54  ?    ?   ?   A . n 
A 1 83  SER 83  -53  ?    ?   ?   A . n 
A 1 84  LEU 84  -52  ?    ?   ?   A . n 
A 1 85  LYS 85  -51  ?    ?   ?   A . n 
A 1 86  PRO 86  -50  ?    ?   ?   A . n 
A 1 87  GLU 87  -49  ?    ?   ?   A . n 
A 1 88  ASP 88  -48  ?    ?   ?   A . n 
A 1 89  THR 89  -47  ?    ?   ?   A . n 
A 1 90  ALA 90  -46  ?    ?   ?   A . n 
A 1 91  VAL 91  -45  ?    ?   ?   A . n 
A 1 92  TYR 92  -44  ?    ?   ?   A . n 
A 1 93  TYR 93  -43  ?    ?   ?   A . n 
A 1 94  CYS 94  -42  ?    ?   ?   A . n 
A 1 95  ALA 95  -41  ?    ?   ?   A . n 
A 1 96  ALA 96  -40  ?    ?   ?   A . n 
A 1 97  TYR 97  -39  ?    ?   ?   A . n 
A 1 98  ASN 98  -38  ?    ?   ?   A . n 
A 1 99  TYR 99  -37  ?    ?   ?   A . n 
A 1 100 PHE 100 -36  ?    ?   ?   A . n 
A 1 101 PRO 101 -35  ?    ?   ?   A . n 
A 1 102 ARG 102 -34  ?    ?   ?   A . n 
A 1 103 SER 103 -33  ?    ?   ?   A . n 
A 1 104 ILE 104 -32  ?    ?   ?   A . n 
A 1 105 VAL 105 -31  ?    ?   ?   A . n 
A 1 106 TYR 106 -30  ?    ?   ?   A . n 
A 1 107 TYR 107 -29  ?    ?   ?   A . n 
A 1 108 TYR 108 -28  ?    ?   ?   A . n 
A 1 109 VAL 109 -27  ?    ?   ?   A . n 
A 1 110 TYR 110 -26  ?    ?   ?   A . n 
A 1 111 TRP 111 -25  ?    ?   ?   A . n 
A 1 112 GLY 112 -24  ?    ?   ?   A . n 
A 1 113 GLN 113 -23  ?    ?   ?   A . n 
A 1 114 GLY 114 -22  ?    ?   ?   A . n 
A 1 115 THR 115 -21  ?    ?   ?   A . n 
A 1 116 GLN 116 -20  ?    ?   ?   A . n 
A 1 117 VAL 117 -19  ?    ?   ?   A . n 
A 1 118 THR 118 -18  ?    ?   ?   A . n 
A 1 119 VAL 119 -17  ?    ?   ?   A . n 
A 1 120 SER 120 -16  ?    ?   ?   A . n 
A 1 121 SER 121 -15  ?    ?   ?   A . n 
A 1 122 GLY 122 -14  ?    ?   ?   A . n 
A 1 123 GLY 123 -13  ?    ?   ?   A . n 
A 1 124 SER 124 -12  ?    ?   ?   A . n 
A 1 125 GLY 125 -11  ?    ?   ?   A . n 
A 1 126 GLU 126 -10  ?    ?   ?   A . n 
A 1 127 ASP 127 -9   ?    ?   ?   A . n 
A 1 128 GLN 128 -8   ?    ?   ?   A . n 
A 1 129 VAL 129 -7   ?    ?   ?   A . n 
A 1 130 ASP 130 -6   ?    ?   ?   A . n 
A 1 131 PRO 131 -5   ?    ?   ?   A . n 
A 1 132 ARG 132 -4   ?    ?   ?   A . n 
A 1 133 LEU 133 -3   ?    ?   ?   A . n 
A 1 134 ILE 134 -2   ?    ?   ?   A . n 
A 1 135 ASP 135 -1   ?    ?   ?   A . n 
A 1 136 GLY 136 0    ?    ?   ?   A . n 
A 1 137 LYS 137 1    ?    ?   ?   A . n 
A 1 138 ILE 138 2    ?    ?   ?   A . n 
A 1 139 LEU 139 3    ?    ?   ?   A . n 
A 1 140 ASN 140 4    ?    ?   ?   A . n 
A 1 141 SER 141 5    ?    ?   ?   A . n 
A 1 142 SER 142 6    ?    ?   ?   A . n 
A 1 143 THR 143 7    ?    ?   ?   A . n 
A 1 144 GLU 144 8    ?    ?   ?   A . n 
A 1 145 ASP 145 9    ?    ?   ?   A . n 
A 1 146 GLY 146 10   ?    ?   ?   A . n 
A 1 147 ILE 147 11   ?    ?   ?   A . n 
A 1 148 LYS 148 12   ?    ?   ?   A . n 
A 1 149 ARG 149 13   ?    ?   ?   A . n 
A 1 150 ILE 150 14   ?    ?   ?   A . n 
A 1 151 GLN 151 15   ?    ?   ?   A . n 
A 1 152 ASP 152 16   ?    ?   ?   A . n 
A 1 153 ASP 153 17   ?    ?   ?   A . n 
A 1 154 CYS 154 18   ?    ?   ?   A . n 
A 1 155 PRO 155 19   ?    ?   ?   A . n 
A 1 156 LYS 156 20   ?    ?   ?   A . n 
A 1 157 ALA 157 21   ?    ?   ?   A . n 
A 1 158 GLY 158 22   ?    ?   ?   A . n 
A 1 159 ARG 159 23   ?    ?   ?   A . n 
A 1 160 HIS 160 24   ?    ?   ?   A . n 
A 1 161 ASN 161 25   ?    ?   ?   A . n 
A 1 162 TYR 162 26   ?    ?   ?   A . n 
A 1 163 ILE 163 27   ?    ?   ?   A . n 
A 1 164 PHE 164 28   ?    ?   ?   A . n 
A 1 165 VAL 165 29   ?    ?   ?   A . n 
A 1 166 MET 166 30   30   MET MET A . n 
A 1 167 ILE 167 31   31   ILE ILE A . n 
A 1 168 PRO 168 32   32   PRO PRO A . n 
A 1 169 THR 169 33   33   THR THR A . n 
A 1 170 LEU 170 34   34   LEU LEU A . n 
A 1 171 TYR 171 35   35   TYR TYR A . n 
A 1 172 SER 172 36   36   SER SER A . n 
A 1 173 ILE 173 37   37   ILE ILE A . n 
A 1 174 ILE 174 38   38   ILE ILE A . n 
A 1 175 PHE 175 39   39   PHE PHE A . n 
A 1 176 VAL 176 40   40   VAL VAL A . n 
A 1 177 VAL 177 41   41   VAL VAL A . n 
A 1 178 GLY 178 42   42   GLY GLY A . n 
A 1 179 ILE 179 43   43   ILE ILE A . n 
A 1 180 PHE 180 44   44   PHE PHE A . n 
A 1 181 GLY 181 45   45   GLY GLY A . n 
A 1 182 ASN 182 46   46   ASN ASN A . n 
A 1 183 SER 183 47   47   SER SER A . n 
A 1 184 LEU 184 48   48   LEU LEU A . n 
A 1 185 VAL 185 49   49   VAL VAL A . n 
A 1 186 VAL 186 50   50   VAL VAL A . n 
A 1 187 ILE 187 51   51   ILE ILE A . n 
A 1 188 VAL 188 52   52   VAL VAL A . n 
A 1 189 ILE 189 53   53   ILE ILE A . n 
A 1 190 TYR 190 54   54   TYR TYR A . n 
A 1 191 PHE 191 55   55   PHE PHE A . n 
A 1 192 TYR 192 56   56   TYR TYR A . n 
A 1 193 MET 193 57   57   MET MET A . n 
A 1 194 LYS 194 58   58   LYS LYS A . n 
A 1 195 LEU 195 59   59   LEU LEU A . n 
A 1 196 LYS 196 60   60   LYS LYS A . n 
A 1 197 THR 197 61   61   THR THR A . n 
A 1 198 VAL 198 62   62   VAL VAL A . n 
A 1 199 ALA 199 63   63   ALA ALA A . n 
A 1 200 SER 200 64   64   SER SER A . n 
A 1 201 VAL 201 65   65   VAL VAL A . n 
A 1 202 PHE 202 66   66   PHE PHE A . n 
A 1 203 LEU 203 67   67   LEU LEU A . n 
A 1 204 LEU 204 68   68   LEU LEU A . n 
A 1 205 ASN 205 69   69   ASN ASN A . n 
A 1 206 LEU 206 70   70   LEU LEU A . n 
A 1 207 ALA 207 71   71   ALA ALA A . n 
A 1 208 LEU 208 72   72   LEU LEU A . n 
A 1 209 ALA 209 73   73   ALA ALA A . n 
A 1 210 ASP 210 74   74   ASP ASP A . n 
A 1 211 LEU 211 75   75   LEU LEU A . n 
A 1 212 CYS 212 76   76   CYS CYS A . n 
A 1 213 PHE 213 77   77   PHE PHE A . n 
A 1 214 LEU 214 78   78   LEU LEU A . n 
A 1 215 LEU 215 79   79   LEU LEU A . n 
A 1 216 THR 216 80   80   THR THR A . n 
A 1 217 LEU 217 81   81   LEU LEU A . n 
A 1 218 PRO 218 82   82   PRO PRO A . n 
A 1 219 LEU 219 83   83   LEU LEU A . n 
A 1 220 TRP 220 84   84   TRP TRP A . n 
A 1 221 ALA 221 85   85   ALA ALA A . n 
A 1 222 VAL 222 86   86   VAL VAL A . n 
A 1 223 TYR 223 87   87   TYR TYR A . n 
A 1 224 THR 224 88   88   THR THR A . n 
A 1 225 ALA 225 89   89   ALA ALA A . n 
A 1 226 MET 226 90   90   MET MET A . n 
A 1 227 GLU 227 91   91   GLU GLU A . n 
A 1 228 TYR 228 92   92   TYR TYR A . n 
A 1 229 ARG 229 93   93   ARG ARG A . n 
A 1 230 TRP 230 94   94   TRP TRP A . n 
A 1 231 PRO 231 95   95   PRO PRO A . n 
A 1 232 PHE 232 96   96   PHE PHE A . n 
A 1 233 GLY 233 97   97   GLY GLY A . n 
A 1 234 ASN 234 98   98   ASN ASN A . n 
A 1 235 TYR 235 99   99   TYR TYR A . n 
A 1 236 LEU 236 100  100  LEU LEU A . n 
A 1 237 CYS 237 101  101  CYS CYS A . n 
A 1 238 LYS 238 102  102  LYS LYS A . n 
A 1 239 ILE 239 103  103  ILE ILE A . n 
A 1 240 ALA 240 104  104  ALA ALA A . n 
A 1 241 SER 241 105  105  SER SER A . n 
A 1 242 ALA 242 106  106  ALA ALA A . n 
A 1 243 SER 243 107  107  SER SER A . n 
A 1 244 VAL 244 108  108  VAL VAL A . n 
A 1 245 SER 245 109  109  SER SER A . n 
A 1 246 PHE 246 110  110  PHE PHE A . n 
A 1 247 ASN 247 111  111  ASN ASN A . n 
A 1 248 LEU 248 112  112  LEU LEU A . n 
A 1 249 TYR 249 113  113  TYR TYR A . n 
A 1 250 ALA 250 114  114  ALA ALA A . n 
A 1 251 SER 251 115  115  SER SER A . n 
A 1 252 VAL 252 116  116  VAL VAL A . n 
A 1 253 PHE 253 117  117  PHE PHE A . n 
A 1 254 LEU 254 118  118  LEU LEU A . n 
A 1 255 LEU 255 119  119  LEU LEU A . n 
A 1 256 THR 256 120  120  THR THR A . n 
A 1 257 CYS 257 121  121  CYS CYS A . n 
A 1 258 LEU 258 122  122  LEU LEU A . n 
A 1 259 SER 259 123  123  SER SER A . n 
A 1 260 ILE 260 124  124  ILE ILE A . n 
A 1 261 ASP 261 125  125  ASP ASP A . n 
A 1 262 ARG 262 126  126  ARG ARG A . n 
A 1 263 TYR 263 127  127  TYR TYR A . n 
A 1 264 LEU 264 128  128  LEU LEU A . n 
A 1 265 ALA 265 129  129  ALA ALA A . n 
A 1 266 ILE 266 130  130  ILE ILE A . n 
A 1 267 VAL 267 131  131  VAL VAL A . n 
A 1 268 HIS 268 132  132  HIS HIS A . n 
A 1 269 PRO 269 133  133  PRO PRO A . n 
A 1 270 MET 270 134  ?    ?   ?   A . n 
A 1 271 LYS 271 135  ?    ?   ?   A . n 
A 1 272 SER 272 136  ?    ?   ?   A . n 
A 1 273 ARG 273 137  ?    ?   ?   A . n 
A 1 274 LEU 274 138  ?    ?   ?   A . n 
A 1 275 ARG 275 139  ?    ?   ?   A . n 
A 1 276 ARG 276 140  ?    ?   ?   A . n 
A 1 277 THR 277 141  141  THR THR A . n 
A 1 278 MET 278 142  142  MET MET A . n 
A 1 279 LEU 279 143  143  LEU LEU A . n 
A 1 280 VAL 280 144  144  VAL VAL A . n 
A 1 281 ALA 281 145  145  ALA ALA A . n 
A 1 282 LYS 282 146  146  LYS LYS A . n 
A 1 283 VAL 283 147  147  VAL VAL A . n 
A 1 284 THR 284 148  148  THR THR A . n 
A 1 285 CYS 285 149  149  CYS CYS A . n 
A 1 286 ILE 286 150  150  ILE ILE A . n 
A 1 287 ILE 287 151  151  ILE ILE A . n 
A 1 288 ILE 288 152  152  ILE ILE A . n 
A 1 289 TRP 289 153  153  TRP TRP A . n 
A 1 290 LEU 290 154  154  LEU LEU A . n 
A 1 291 LEU 291 155  155  LEU LEU A . n 
A 1 292 ALA 292 156  156  ALA ALA A . n 
A 1 293 GLY 293 157  157  GLY GLY A . n 
A 1 294 LEU 294 158  158  LEU LEU A . n 
A 1 295 ALA 295 159  159  ALA ALA A . n 
A 1 296 SER 296 160  160  SER SER A . n 
A 1 297 LEU 297 161  161  LEU LEU A . n 
A 1 298 PRO 298 162  162  PRO PRO A . n 
A 1 299 ALA 299 163  163  ALA ALA A . n 
A 1 300 ILE 300 164  164  ILE ILE A . n 
A 1 301 ILE 301 165  165  ILE ILE A . n 
A 1 302 HIS 302 166  166  HIS HIS A . n 
A 1 303 ARG 303 167  167  ARG ARG A . n 
A 1 304 ASN 304 168  168  ASN ASN A . n 
A 1 305 VAL 305 169  169  VAL VAL A . n 
A 1 306 PHE 306 170  170  PHE PHE A . n 
A 1 307 PHE 307 171  171  PHE PHE A . n 
A 1 308 ILE 308 172  172  ILE ILE A . n 
A 1 309 GLU 309 173  173  GLU GLU A . n 
A 1 310 ASN 310 174  174  ASN ASN A . n 
A 1 311 THR 311 175  175  THR THR A . n 
A 1 312 ASN 312 176  176  ASN ASN A . n 
A 1 313 ILE 313 177  177  ILE ILE A . n 
A 1 314 THR 314 178  178  THR THR A . n 
A 1 315 VAL 315 179  179  VAL VAL A . n 
A 1 316 CYS 316 180  180  CYS CYS A . n 
A 1 317 ALA 317 181  181  ALA ALA A . n 
A 1 318 PHE 318 182  182  PHE PHE A . n 
A 1 319 HIS 319 183  183  HIS HIS A . n 
A 1 320 TYR 320 184  184  TYR TYR A . n 
A 1 321 GLU 321 185  185  GLU GLU A . n 
A 1 322 SER 322 186  186  SER SER A . n 
A 1 323 GLN 323 187  187  GLN GLN A . n 
A 1 324 ASN 324 188  188  ASN ASN A . n 
A 1 325 SER 325 189  189  SER SER A . n 
A 1 326 THR 326 190  190  THR THR A . n 
A 1 327 LEU 327 191  191  LEU LEU A . n 
A 1 328 PRO 328 192  192  PRO PRO A . n 
A 1 329 ILE 329 193  193  ILE ILE A . n 
A 1 330 GLY 330 194  194  GLY GLY A . n 
A 1 331 LEU 331 195  195  LEU LEU A . n 
A 1 332 GLY 332 196  196  GLY GLY A . n 
A 1 333 LEU 333 197  197  LEU LEU A . n 
A 1 334 THR 334 198  198  THR THR A . n 
A 1 335 LYS 335 199  199  LYS LYS A . n 
A 1 336 ASN 336 200  200  ASN ASN A . n 
A 1 337 ILE 337 201  201  ILE ILE A . n 
A 1 338 LEU 338 202  202  LEU LEU A . n 
A 1 339 GLY 339 203  203  GLY GLY A . n 
A 1 340 PHE 340 204  204  PHE PHE A . n 
A 1 341 LEU 341 205  205  LEU LEU A . n 
A 1 342 PHE 342 206  206  PHE PHE A . n 
A 1 343 PRO 343 207  207  PRO PRO A . n 
A 1 344 PHE 344 208  208  PHE PHE A . n 
A 1 345 LEU 345 209  209  LEU LEU A . n 
A 1 346 ILE 346 210  210  ILE ILE A . n 
A 1 347 ILE 347 211  211  ILE ILE A . n 
A 1 348 LEU 348 212  212  LEU LEU A . n 
A 1 349 THR 349 213  213  THR THR A . n 
A 1 350 SER 350 214  214  SER SER A . n 
A 1 351 TYR 351 215  215  TYR TYR A . n 
A 1 352 THR 352 216  216  THR THR A . n 
A 1 353 LEU 353 217  217  LEU LEU A . n 
A 1 354 ILE 354 218  218  ILE ILE A . n 
A 1 355 TRP 355 219  219  TRP TRP A . n 
A 1 356 LYS 356 220  220  LYS LYS A . n 
A 1 357 ALA 357 221  221  ALA ALA A . n 
A 1 358 LEU 358 222  222  LEU LEU A . n 
A 1 359 LYS 359 223  223  LYS LYS A . n 
A 1 360 LYS 360 224  224  LYS LYS A . n 
A 1 361 ALA 361 225  225  ALA ALA A . n 
A 1 362 TYR 362 226  226  TYR TYR A . n 
A 1 363 ASP 363 227  227  ASP ASP A . n 
A 1 364 LEU 364 228  228  LEU LEU A . n 
A 1 365 GLU 365 229  229  GLU GLU A . n 
A 1 366 ASP 366 230  230  ASP ASP A . n 
A 1 367 ASN 367 231  231  ASN ASN A . n 
A 1 368 TRP 368 232  232  TRP TRP A . n 
A 1 369 GLU 369 233  233  GLU GLU A . n 
A 1 370 THR 370 234  234  THR THR A . n 
A 1 371 LEU 371 235  235  LEU LEU A . n 
A 1 372 ASN 372 236  236  ASN ASN A . n 
A 1 373 ASP 373 237  237  ASP ASP A . n 
A 1 374 ASN 374 238  238  ASN ASN A . n 
A 1 375 LEU 375 239  239  LEU LEU A . n 
A 1 376 LYS 376 240  240  LYS LYS A . n 
A 1 377 VAL 377 241  241  VAL VAL A . n 
A 1 378 ILE 378 242  242  ILE ILE A . n 
A 1 379 GLU 379 243  243  GLU GLU A . n 
A 1 380 LYS 380 244  244  LYS LYS A . n 
A 1 381 ALA 381 245  245  ALA ALA A . n 
A 1 382 ASP 382 246  246  ASP ASP A . n 
A 1 383 ASN 383 247  247  ASN ASN A . n 
A 1 384 ALA 384 248  248  ALA ALA A . n 
A 1 385 ALA 385 249  249  ALA ALA A . n 
A 1 386 GLN 386 250  250  GLN GLN A . n 
A 1 387 VAL 387 251  251  VAL VAL A . n 
A 1 388 LYS 388 252  252  LYS LYS A . n 
A 1 389 ASP 389 253  253  ASP ASP A . n 
A 1 390 ALA 390 254  254  ALA ALA A . n 
A 1 391 LEU 391 255  255  LEU LEU A . n 
A 1 392 THR 392 256  256  THR THR A . n 
A 1 393 LYS 393 257  257  LYS LYS A . n 
A 1 394 MET 394 258  258  MET MET A . n 
A 1 395 ARG 395 259  259  ARG ARG A . n 
A 1 396 ALA 396 260  260  ALA ALA A . n 
A 1 397 ALA 397 261  261  ALA ALA A . n 
A 1 398 ALA 398 262  262  ALA ALA A . n 
A 1 399 LEU 399 263  263  LEU LEU A . n 
A 1 400 ASP 400 264  264  ASP ASP A . n 
A 1 401 ALA 401 265  265  ALA ALA A . n 
A 1 402 GLN 402 266  266  GLN GLN A . n 
A 1 403 LYS 403 267  267  LYS LYS A . n 
A 1 404 ALA 404 268  268  ALA ALA A . n 
A 1 405 THR 405 269  269  THR THR A . n 
A 1 406 PRO 406 270  270  PRO PRO A . n 
A 1 407 PRO 407 271  271  PRO PRO A . n 
A 1 408 LYS 408 272  272  LYS LYS A . n 
A 1 409 LEU 409 273  ?    ?   ?   A . n 
A 1 410 GLU 410 274  ?    ?   ?   A . n 
A 1 411 ASP 411 275  ?    ?   ?   A . n 
A 1 412 LYS 412 276  ?    ?   ?   A . n 
A 1 413 SER 413 277  ?    ?   ?   A . n 
A 1 414 PRO 414 278  ?    ?   ?   A . n 
A 1 415 ASP 415 279  ?    ?   ?   A . n 
A 1 416 SER 416 280  280  SER SER A . n 
A 1 417 PRO 417 281  281  PRO PRO A . n 
A 1 418 GLU 418 282  282  GLU GLU A . n 
A 1 419 MET 419 283  283  MET MET A . n 
A 1 420 LYS 420 284  284  LYS LYS A . n 
A 1 421 ASP 421 285  285  ASP ASP A . n 
A 1 422 PHE 422 286  286  PHE PHE A . n 
A 1 423 ARG 423 287  287  ARG ARG A . n 
A 1 424 HIS 424 288  288  HIS HIS A . n 
A 1 425 GLY 425 289  289  GLY GLY A . n 
A 1 426 PHE 426 290  290  PHE PHE A . n 
A 1 427 ASP 427 291  291  ASP ASP A . n 
A 1 428 ILE 428 292  292  ILE ILE A . n 
A 1 429 LEU 429 293  293  LEU LEU A . n 
A 1 430 VAL 430 294  294  VAL VAL A . n 
A 1 431 GLY 431 295  295  GLY GLY A . n 
A 1 432 GLN 432 296  296  GLN GLN A . n 
A 1 433 ILE 433 297  297  ILE ILE A . n 
A 1 434 ASP 434 298  298  ASP ASP A . n 
A 1 435 ASP 435 299  299  ASP ASP A . n 
A 1 436 ALA 436 300  300  ALA ALA A . n 
A 1 437 LEU 437 301  301  LEU LEU A . n 
A 1 438 LYS 438 302  302  LYS LYS A . n 
A 1 439 LEU 439 303  303  LEU LEU A . n 
A 1 440 ALA 440 304  304  ALA ALA A . n 
A 1 441 ASN 441 305  305  ASN ASN A . n 
A 1 442 GLU 442 306  306  GLU GLU A . n 
A 1 443 GLY 443 307  307  GLY GLY A . n 
A 1 444 LYS 444 308  308  LYS LYS A . n 
A 1 445 VAL 445 309  309  VAL VAL A . n 
A 1 446 LYS 446 310  310  LYS LYS A . n 
A 1 447 GLU 447 311  311  GLU GLU A . n 
A 1 448 ALA 448 312  312  ALA ALA A . n 
A 1 449 GLN 449 313  313  GLN GLN A . n 
A 1 450 ALA 450 314  314  ALA ALA A . n 
A 1 451 ALA 451 315  315  ALA ALA A . n 
A 1 452 ALA 452 316  316  ALA ALA A . n 
A 1 453 GLU 453 317  317  GLU GLU A . n 
A 1 454 GLN 454 318  318  GLN GLN A . n 
A 1 455 LEU 455 319  319  LEU LEU A . n 
A 1 456 LYS 456 320  320  LYS LYS A . n 
A 1 457 THR 457 321  321  THR THR A . n 
A 1 458 THR 458 322  322  THR THR A . n 
A 1 459 ARG 459 323  323  ARG ARG A . n 
A 1 460 ASN 460 324  324  ASN ASN A . n 
A 1 461 ALA 461 325  325  ALA ALA A . n 
A 1 462 TYR 462 326  326  TYR TYR A . n 
A 1 463 ILE 463 327  327  ILE ILE A . n 
A 1 464 GLN 464 328  328  GLN GLN A . n 
A 1 465 LYS 465 329  329  LYS LYS A . n 
A 1 466 TYR 466 330  330  TYR TYR A . n 
A 1 467 LEU 467 331  331  LEU LEU A . n 
A 1 468 GLU 468 332  332  GLU GLU A . n 
A 1 469 ARG 469 333  333  ARG ARG A . n 
A 1 470 ALA 470 334  334  ALA ALA A . n 
A 1 471 ARG 471 335  335  ARG ARG A . n 
A 1 472 SER 472 336  336  SER SER A . n 
A 1 473 THR 473 337  337  THR THR A . n 
A 1 474 LEU 474 338  338  LEU LEU A . n 
A 1 475 ASP 475 339  339  ASP ASP A . n 
A 1 476 LYS 476 340  340  LYS LYS A . n 
A 1 477 LEU 477 341  341  LEU LEU A . n 
A 1 478 ASN 478 1235 1235 ASN ASN A . n 
A 1 479 ASP 479 1236 1236 ASP ASP A . n 
A 1 480 ASP 480 1237 1237 ASP ASP A . n 
A 1 481 ILE 481 1238 1238 ILE ILE A . n 
A 1 482 PHE 482 1239 1239 PHE PHE A . n 
A 1 483 LYS 483 1240 1240 LYS LYS A . n 
A 1 484 ILE 484 1241 1241 ILE ILE A . n 
A 1 485 ILE 485 1242 1242 ILE ILE A . n 
A 1 486 MET 486 1243 1243 MET MET A . n 
A 1 487 ALA 487 1244 1244 ALA ALA A . n 
A 1 488 ILE 488 1245 1245 ILE ILE A . n 
A 1 489 VAL 489 1246 1246 VAL VAL A . n 
A 1 490 LEU 490 1247 1247 LEU LEU A . n 
A 1 491 PHE 491 1248 1248 PHE PHE A . n 
A 1 492 PHE 492 1249 1249 PHE PHE A . n 
A 1 493 PHE 493 1250 1250 PHE PHE A . n 
A 1 494 PHE 494 1251 1251 PHE PHE A . n 
A 1 495 SER 495 1252 1252 SER SER A . n 
A 1 496 TRP 496 1253 1253 TRP TRP A . n 
A 1 497 ILE 497 1254 1254 ILE ILE A . n 
A 1 498 PRO 498 1255 1255 PRO PRO A . n 
A 1 499 HIS 499 1256 1256 HIS HIS A . n 
A 1 500 GLN 500 1257 1257 GLN GLN A . n 
A 1 501 ILE 501 1258 1258 ILE ILE A . n 
A 1 502 PHE 502 1259 1259 PHE PHE A . n 
A 1 503 THR 503 1260 1260 THR THR A . n 
A 1 504 PHE 504 1261 1261 PHE PHE A . n 
A 1 505 LEU 505 1262 1262 LEU LEU A . n 
A 1 506 ASP 506 1263 1263 ASP ASP A . n 
A 1 507 VAL 507 1264 1264 VAL VAL A . n 
A 1 508 LEU 508 1265 1265 LEU LEU A . n 
A 1 509 ILE 509 1266 1266 ILE ILE A . n 
A 1 510 GLN 510 1267 1267 GLN GLN A . n 
A 1 511 LEU 511 1268 1268 LEU LEU A . n 
A 1 512 GLY 512 1269 1269 GLY GLY A . n 
A 1 513 ILE 513 1270 1270 ILE ILE A . n 
A 1 514 ILE 514 1271 1271 ILE ILE A . n 
A 1 515 ARG 515 1272 ?    ?   ?   A . n 
A 1 516 ASP 516 1273 ?    ?   ?   A . n 
A 1 517 CYS 517 1274 ?    ?   ?   A . n 
A 1 518 ARG 518 1275 ?    ?   ?   A . n 
A 1 519 ILE 519 1276 ?    ?   ?   A . n 
A 1 520 ALA 520 1277 1277 ALA ALA A . n 
A 1 521 ASP 521 1278 1278 ASP ASP A . n 
A 1 522 ILE 522 1279 1279 ILE ILE A . n 
A 1 523 VAL 523 1280 1280 VAL VAL A . n 
A 1 524 ASP 524 1281 1281 ASP ASP A . n 
A 1 525 THR 525 1282 1282 THR THR A . n 
A 1 526 ALA 526 1283 1283 ALA ALA A . n 
A 1 527 MET 527 1284 1284 MET MET A . n 
A 1 528 PRO 528 1285 1285 PRO PRO A . n 
A 1 529 ILE 529 1286 1286 ILE ILE A . n 
A 1 530 THR 530 1287 1287 THR THR A . n 
A 1 531 ILE 531 1288 1288 ILE ILE A . n 
A 1 532 CYS 532 1289 1289 CYS CYS A . n 
A 1 533 ILE 533 1290 1290 ILE ILE A . n 
A 1 534 ALA 534 1291 1291 ALA ALA A . n 
A 1 535 TYR 535 1292 1292 TYR TYR A . n 
A 1 536 PHE 536 1293 1293 PHE PHE A . n 
A 1 537 ASN 537 1294 1294 ASN ASN A . n 
A 1 538 ASN 538 1295 1295 ASN ASN A . n 
A 1 539 CYS 539 1296 1296 CYS CYS A . n 
A 1 540 LEU 540 1297 1297 LEU LEU A . n 
A 1 541 ASN 541 1298 1298 ASN ASN A . n 
A 1 542 PRO 542 1299 1299 PRO PRO A . n 
A 1 543 LEU 543 1300 1300 LEU LEU A . n 
A 1 544 PHE 544 1301 1301 PHE PHE A . n 
A 1 545 TYR 545 1302 1302 TYR TYR A . n 
A 1 546 GLY 546 1303 1303 GLY GLY A . n 
A 1 547 PHE 547 1304 1304 PHE PHE A . n 
A 1 548 LEU 548 1305 1305 LEU LEU A . n 
A 1 549 GLY 549 1306 1306 GLY GLY A . n 
A 1 550 LYS 550 1307 ?    ?   ?   A . n 
A 1 551 LYS 551 1308 ?    ?   ?   A . n 
A 1 552 PHE 552 1309 ?    ?   ?   A . n 
A 1 553 LYS 553 1310 ?    ?   ?   A . n 
A 1 554 ARG 554 1311 ?    ?   ?   A . n 
A 1 555 TYR 555 1312 ?    ?   ?   A . n 
A 1 556 PHE 556 1313 ?    ?   ?   A . n 
A 1 557 LEU 557 1314 ?    ?   ?   A . n 
A 1 558 GLN 558 1315 ?    ?   ?   A . n 
A 1 559 LEU 559 1316 ?    ?   ?   A . n 
A 1 560 LEU 560 1317 ?    ?   ?   A . n 
A 1 561 LYS 561 1318 ?    ?   ?   A . n 
A 1 562 TYR 562 1319 ?    ?   ?   A . n 
A 1 563 GLY 563 1320 ?    ?   ?   A . n 
A 1 564 GLY 564 1321 ?    ?   ?   A . n 
A 1 565 SER 565 1322 ?    ?   ?   A . n 
A 1 566 SER 566 1323 ?    ?   ?   A . n 
A 1 567 LEU 567 1324 ?    ?   ?   A . n 
A 1 568 GLU 568 1325 ?    ?   ?   A . n 
A 1 569 VAL 569 1326 ?    ?   ?   A . n 
A 1 570 LEU 570 1327 ?    ?   ?   A . n 
A 1 571 PHE 571 1328 ?    ?   ?   A . n 
A 1 572 GLN 572 1329 ?    ?   ?   A . n 
A 1 573 GLY 573 1330 ?    ?   ?   A . n 
A 1 574 PRO 574 1331 ?    ?   ?   A . n 
A 1 575 THR 575 1332 ?    ?   ?   A . n 
A 1 576 GLU 576 1333 ?    ?   ?   A . n 
A 1 577 THR 577 1334 ?    ?   ?   A . n 
A 1 578 SER 578 1335 ?    ?   ?   A . n 
A 1 579 GLN 579 1336 ?    ?   ?   A . n 
A 1 580 VAL 580 1337 ?    ?   ?   A . n 
A 1 581 ALA 581 1338 ?    ?   ?   A . n 
A 1 582 PRO 582 1339 ?    ?   ?   A . n 
A 1 583 ALA 583 1340 ?    ?   ?   A . n 
B 1 1   GLN 1   1    ?    ?   ?   B . n 
B 1 2   VAL 2   2    ?    ?   ?   B . n 
B 1 3   GLN 3   3    ?    ?   ?   B . n 
B 1 4   LEU 4   4    ?    ?   ?   B . n 
B 1 5   GLN 5   5    ?    ?   ?   B . n 
B 1 6   GLU 6   6    ?    ?   ?   B . n 
B 1 7   SER 7   7    ?    ?   ?   B . n 
B 1 8   GLY 8   8    ?    ?   ?   B . n 
B 1 9   GLY 9   9    ?    ?   ?   B . n 
B 1 10  GLY 10  10   ?    ?   ?   B . n 
B 1 11  LEU 11  11   ?    ?   ?   B . n 
B 1 12  VAL 12  12   ?    ?   ?   B . n 
B 1 13  GLN 13  13   ?    ?   ?   B . n 
B 1 14  ALA 14  14   ?    ?   ?   B . n 
B 1 15  GLY 15  15   ?    ?   ?   B . n 
B 1 16  GLY 16  16   ?    ?   ?   B . n 
B 1 17  SER 17  17   ?    ?   ?   B . n 
B 1 18  LEU 18  18   ?    ?   ?   B . n 
B 1 19  ARG 19  19   ?    ?   ?   B . n 
B 1 20  LEU 20  20   ?    ?   ?   B . n 
B 1 21  SER 21  21   ?    ?   ?   B . n 
B 1 22  CYS 22  22   ?    ?   ?   B . n 
B 1 23  ALA 23  23   ?    ?   ?   B . n 
B 1 24  ALA 24  24   ?    ?   ?   B . n 
B 1 25  SER 25  25   ?    ?   ?   B . n 
B 1 26  GLY 26  26   ?    ?   ?   B . n 
B 1 27  SER 27  27   ?    ?   ?   B . n 
B 1 28  ILE 28  28   ?    ?   ?   B . n 
B 1 29  SER 29  29   29   SER SER B . n 
B 1 30  TYR 30  30   30   TYR TYR B . n 
B 1 31  TYR 31  31   31   TYR TYR B . n 
B 1 32  ARG 32  32   32   ARG ARG B . n 
B 1 33  MET 33  33   33   MET MET B . n 
B 1 34  GLY 34  34   34   GLY GLY B . n 
B 1 35  TRP 35  35   35   TRP TRP B . n 
B 1 36  TYR 36  36   36   TYR TYR B . n 
B 1 37  ARG 37  37   37   ARG ARG B . n 
B 1 38  GLN 38  38   38   GLN GLN B . n 
B 1 39  ALA 39  39   39   ALA ALA B . n 
B 1 40  PRO 40  40   ?    ?   ?   B . n 
B 1 41  GLY 41  41   ?    ?   ?   B . n 
B 1 42  LYS 42  42   ?    ?   ?   B . n 
B 1 43  GLU 43  43   43   GLU GLU B . n 
B 1 44  ARG 44  44   44   ARG ARG B . n 
B 1 45  GLU 45  45   45   GLU GLU B . n 
B 1 46  PHE 46  46   46   PHE PHE B . n 
B 1 47  VAL 47  47   47   VAL VAL B . n 
B 1 48  ALA 48  48   48   ALA ALA B . n 
B 1 49  GLY 49  49   49   GLY GLY B . n 
B 1 50  ILE 50  50   50   ILE ILE B . n 
B 1 51  GLY 51  51   51   GLY GLY B . n 
B 1 52  VAL 52  52   ?    ?   ?   B . n 
B 1 53  GLY 53  53   ?    ?   ?   B . n 
B 1 54  THR 54  54   ?    ?   ?   B . n 
B 1 55  THR 55  55   55   THR THR B . n 
B 1 56  THR 56  56   56   THR THR B . n 
B 1 57  ASN 57  57   57   ASN ASN B . n 
B 1 58  TYR 58  58   58   TYR TYR B . n 
B 1 59  ALA 59  59   59   ALA ALA B . n 
B 1 60  ASP 60  60   60   ASP ASP B . n 
B 1 61  SER 61  61   61   SER SER B . n 
B 1 62  VAL 62  62   62   VAL VAL B . n 
B 1 63  LYS 63  63   63   LYS LYS B . n 
B 1 64  GLY 64  64   64   GLY GLY B . n 
B 1 65  ARG 65  65   65   ARG ARG B . n 
B 1 66  PHE 66  66   66   PHE PHE B . n 
B 1 67  THR 67  67   ?    ?   ?   B . n 
B 1 68  ILE 68  68   ?    ?   ?   B . n 
B 1 69  SER 69  69   ?    ?   ?   B . n 
B 1 70  ARG 70  70   ?    ?   ?   B . n 
B 1 71  ASP 71  71   ?    ?   ?   B . n 
B 1 72  ASN 72  72   ?    ?   ?   B . n 
B 1 73  ALA 73  73   ?    ?   ?   B . n 
B 1 74  LYS 74  74   ?    ?   ?   B . n 
B 1 75  ASN 75  75   ?    ?   ?   B . n 
B 1 76  THR 76  76   ?    ?   ?   B . n 
B 1 77  VAL 77  77   ?    ?   ?   B . n 
B 1 78  TYR 78  78   ?    ?   ?   B . n 
B 1 79  LEU 79  79   79   LEU LEU B . n 
B 1 80  GLN 80  80   80   GLN GLN B . n 
B 1 81  MET 81  81   81   MET MET B . n 
B 1 82  ASN 82  82   82   ASN ASN B . n 
B 1 83  SER 83  83   83   SER SER B . n 
B 1 84  LEU 84  84   84   LEU LEU B . n 
B 1 85  LYS 85  85   85   LYS LYS B . n 
B 1 86  PRO 86  86   ?    ?   ?   B . n 
B 1 87  GLU 87  87   ?    ?   ?   B . n 
B 1 88  ASP 88  88   ?    ?   ?   B . n 
B 1 89  THR 89  89   ?    ?   ?   B . n 
B 1 90  ALA 90  90   ?    ?   ?   B . n 
B 1 91  VAL 91  91   91   VAL VAL B . n 
B 1 92  TYR 92  92   92   TYR TYR B . n 
B 1 93  TYR 93  93   93   TYR TYR B . n 
B 1 94  CYS 94  94   94   CYS CYS B . n 
B 1 95  ALA 95  95   95   ALA ALA B . n 
B 1 96  ALA 96  96   96   ALA ALA B . n 
B 1 97  TYR 97  97   97   TYR TYR B . n 
B 1 98  ASN 98  98   98   ASN ASN B . n 
B 1 99  TYR 99  99   99   TYR TYR B . n 
B 1 100 PHE 100 100  100  PHE PHE B . n 
B 1 101 PRO 101 101  101  PRO PRO B . n 
B 1 102 ARG 102 102  102  ARG ARG B . n 
B 1 103 SER 103 103  103  SER SER B . n 
B 1 104 ILE 104 104  104  ILE ILE B . n 
B 1 105 VAL 105 105  105  VAL VAL B . n 
B 1 106 TYR 106 106  106  TYR TYR B . n 
B 1 107 TYR 107 107  107  TYR TYR B . n 
B 1 108 TYR 108 108  108  TYR TYR B . n 
B 1 109 VAL 109 109  109  VAL VAL B . n 
B 1 110 TYR 110 110  110  TYR TYR B . n 
B 1 111 TRP 111 111  111  TRP TRP B . n 
B 1 112 GLY 112 112  112  GLY GLY B . n 
B 1 113 GLN 113 113  113  GLN GLN B . n 
B 1 114 GLY 114 114  114  GLY GLY B . n 
B 1 115 THR 115 115  115  THR THR B . n 
B 1 116 GLN 116 116  116  GLN GLN B . n 
B 1 117 VAL 117 117  117  VAL VAL B . n 
B 1 118 THR 118 118  ?    ?   ?   B . n 
B 1 119 VAL 119 119  ?    ?   ?   B . n 
B 1 120 SER 120 120  ?    ?   ?   B . n 
B 1 121 SER 121 121  ?    ?   ?   B . n 
B 1 122 GLY 122 122  ?    ?   ?   B . n 
B 1 123 GLY 123 123  ?    ?   ?   B . n 
B 1 124 SER 124 124  ?    ?   ?   B . n 
B 1 125 GLY 125 125  ?    ?   ?   B . n 
B 1 126 GLU 126 126  ?    ?   ?   B . n 
B 1 127 ASP 127 127  ?    ?   ?   B . n 
B 1 128 GLN 128 128  ?    ?   ?   B . n 
B 1 129 VAL 129 129  ?    ?   ?   B . n 
B 1 130 ASP 130 130  ?    ?   ?   B . n 
B 1 131 PRO 131 131  ?    ?   ?   B . n 
B 1 132 ARG 132 132  ?    ?   ?   B . n 
B 1 133 LEU 133 133  ?    ?   ?   B . n 
B 1 134 ILE 134 134  ?    ?   ?   B . n 
B 1 135 ASP 135 135  ?    ?   ?   B . n 
B 1 136 GLY 136 136  ?    ?   ?   B . n 
B 1 137 LYS 137 137  ?    ?   ?   B . n 
B 1 138 ILE 138 138  ?    ?   ?   B . n 
B 1 139 LEU 139 139  ?    ?   ?   B . n 
B 1 140 ASN 140 140  ?    ?   ?   B . n 
B 1 141 SER 141 141  ?    ?   ?   B . n 
B 1 142 SER 142 142  ?    ?   ?   B . n 
B 1 143 THR 143 143  ?    ?   ?   B . n 
B 1 144 GLU 144 144  ?    ?   ?   B . n 
B 1 145 ASP 145 145  ?    ?   ?   B . n 
B 1 146 GLY 146 146  ?    ?   ?   B . n 
B 1 147 ILE 147 147  ?    ?   ?   B . n 
B 1 148 LYS 148 148  ?    ?   ?   B . n 
B 1 149 ARG 149 149  ?    ?   ?   B . n 
B 1 150 ILE 150 150  ?    ?   ?   B . n 
B 1 151 GLN 151 151  ?    ?   ?   B . n 
B 1 152 ASP 152 152  ?    ?   ?   B . n 
B 1 153 ASP 153 153  ?    ?   ?   B . n 
B 1 154 CYS 154 154  ?    ?   ?   B . n 
B 1 155 PRO 155 155  ?    ?   ?   B . n 
B 1 156 LYS 156 156  ?    ?   ?   B . n 
B 1 157 ALA 157 157  ?    ?   ?   B . n 
B 1 158 GLY 158 158  ?    ?   ?   B . n 
B 1 159 ARG 159 159  ?    ?   ?   B . n 
B 1 160 HIS 160 160  ?    ?   ?   B . n 
B 1 161 ASN 161 161  ?    ?   ?   B . n 
B 1 162 TYR 162 162  ?    ?   ?   B . n 
B 1 163 ILE 163 163  ?    ?   ?   B . n 
B 1 164 PHE 164 164  ?    ?   ?   B . n 
B 1 165 VAL 165 165  ?    ?   ?   B . n 
B 1 166 MET 166 166  ?    ?   ?   B . n 
B 1 167 ILE 167 167  ?    ?   ?   B . n 
B 1 168 PRO 168 168  ?    ?   ?   B . n 
B 1 169 THR 169 169  ?    ?   ?   B . n 
B 1 170 LEU 170 170  ?    ?   ?   B . n 
B 1 171 TYR 171 171  ?    ?   ?   B . n 
B 1 172 SER 172 172  ?    ?   ?   B . n 
B 1 173 ILE 173 173  ?    ?   ?   B . n 
B 1 174 ILE 174 174  ?    ?   ?   B . n 
B 1 175 PHE 175 175  ?    ?   ?   B . n 
B 1 176 VAL 176 176  ?    ?   ?   B . n 
B 1 177 VAL 177 177  ?    ?   ?   B . n 
B 1 178 GLY 178 178  ?    ?   ?   B . n 
B 1 179 ILE 179 179  ?    ?   ?   B . n 
B 1 180 PHE 180 180  ?    ?   ?   B . n 
B 1 181 GLY 181 181  ?    ?   ?   B . n 
B 1 182 ASN 182 182  ?    ?   ?   B . n 
B 1 183 SER 183 183  ?    ?   ?   B . n 
B 1 184 LEU 184 184  ?    ?   ?   B . n 
B 1 185 VAL 185 185  ?    ?   ?   B . n 
B 1 186 VAL 186 186  ?    ?   ?   B . n 
B 1 187 ILE 187 187  ?    ?   ?   B . n 
B 1 188 VAL 188 188  ?    ?   ?   B . n 
B 1 189 ILE 189 189  ?    ?   ?   B . n 
B 1 190 TYR 190 190  ?    ?   ?   B . n 
B 1 191 PHE 191 191  ?    ?   ?   B . n 
B 1 192 TYR 192 192  ?    ?   ?   B . n 
B 1 193 MET 193 193  ?    ?   ?   B . n 
B 1 194 LYS 194 194  ?    ?   ?   B . n 
B 1 195 LEU 195 195  ?    ?   ?   B . n 
B 1 196 LYS 196 196  ?    ?   ?   B . n 
B 1 197 THR 197 197  ?    ?   ?   B . n 
B 1 198 VAL 198 198  ?    ?   ?   B . n 
B 1 199 ALA 199 199  ?    ?   ?   B . n 
B 1 200 SER 200 200  ?    ?   ?   B . n 
B 1 201 VAL 201 201  ?    ?   ?   B . n 
B 1 202 PHE 202 202  ?    ?   ?   B . n 
B 1 203 LEU 203 203  ?    ?   ?   B . n 
B 1 204 LEU 204 204  ?    ?   ?   B . n 
B 1 205 ASN 205 205  ?    ?   ?   B . n 
B 1 206 LEU 206 206  ?    ?   ?   B . n 
B 1 207 ALA 207 207  ?    ?   ?   B . n 
B 1 208 LEU 208 208  ?    ?   ?   B . n 
B 1 209 ALA 209 209  ?    ?   ?   B . n 
B 1 210 ASP 210 210  ?    ?   ?   B . n 
B 1 211 LEU 211 211  ?    ?   ?   B . n 
B 1 212 CYS 212 212  ?    ?   ?   B . n 
B 1 213 PHE 213 213  ?    ?   ?   B . n 
B 1 214 LEU 214 214  ?    ?   ?   B . n 
B 1 215 LEU 215 215  ?    ?   ?   B . n 
B 1 216 THR 216 216  ?    ?   ?   B . n 
B 1 217 LEU 217 217  ?    ?   ?   B . n 
B 1 218 PRO 218 218  ?    ?   ?   B . n 
B 1 219 LEU 219 219  ?    ?   ?   B . n 
B 1 220 TRP 220 220  ?    ?   ?   B . n 
B 1 221 ALA 221 221  ?    ?   ?   B . n 
B 1 222 VAL 222 222  ?    ?   ?   B . n 
B 1 223 TYR 223 223  ?    ?   ?   B . n 
B 1 224 THR 224 224  ?    ?   ?   B . n 
B 1 225 ALA 225 225  ?    ?   ?   B . n 
B 1 226 MET 226 226  ?    ?   ?   B . n 
B 1 227 GLU 227 227  ?    ?   ?   B . n 
B 1 228 TYR 228 228  ?    ?   ?   B . n 
B 1 229 ARG 229 229  ?    ?   ?   B . n 
B 1 230 TRP 230 230  ?    ?   ?   B . n 
B 1 231 PRO 231 231  ?    ?   ?   B . n 
B 1 232 PHE 232 232  ?    ?   ?   B . n 
B 1 233 GLY 233 233  ?    ?   ?   B . n 
B 1 234 ASN 234 234  ?    ?   ?   B . n 
B 1 235 TYR 235 235  ?    ?   ?   B . n 
B 1 236 LEU 236 236  ?    ?   ?   B . n 
B 1 237 CYS 237 237  ?    ?   ?   B . n 
B 1 238 LYS 238 238  ?    ?   ?   B . n 
B 1 239 ILE 239 239  ?    ?   ?   B . n 
B 1 240 ALA 240 240  ?    ?   ?   B . n 
B 1 241 SER 241 241  ?    ?   ?   B . n 
B 1 242 ALA 242 242  ?    ?   ?   B . n 
B 1 243 SER 243 243  ?    ?   ?   B . n 
B 1 244 VAL 244 244  ?    ?   ?   B . n 
B 1 245 SER 245 245  ?    ?   ?   B . n 
B 1 246 PHE 246 246  ?    ?   ?   B . n 
B 1 247 ASN 247 247  ?    ?   ?   B . n 
B 1 248 LEU 248 248  ?    ?   ?   B . n 
B 1 249 TYR 249 249  ?    ?   ?   B . n 
B 1 250 ALA 250 250  ?    ?   ?   B . n 
B 1 251 SER 251 251  ?    ?   ?   B . n 
B 1 252 VAL 252 252  ?    ?   ?   B . n 
B 1 253 PHE 253 253  ?    ?   ?   B . n 
B 1 254 LEU 254 254  ?    ?   ?   B . n 
B 1 255 LEU 255 255  ?    ?   ?   B . n 
B 1 256 THR 256 256  ?    ?   ?   B . n 
B 1 257 CYS 257 257  ?    ?   ?   B . n 
B 1 258 LEU 258 258  ?    ?   ?   B . n 
B 1 259 SER 259 259  ?    ?   ?   B . n 
B 1 260 ILE 260 260  ?    ?   ?   B . n 
B 1 261 ASP 261 261  ?    ?   ?   B . n 
B 1 262 ARG 262 262  ?    ?   ?   B . n 
B 1 263 TYR 263 263  ?    ?   ?   B . n 
B 1 264 LEU 264 264  ?    ?   ?   B . n 
B 1 265 ALA 265 265  ?    ?   ?   B . n 
B 1 266 ILE 266 266  ?    ?   ?   B . n 
B 1 267 VAL 267 267  ?    ?   ?   B . n 
B 1 268 HIS 268 268  ?    ?   ?   B . n 
B 1 269 PRO 269 269  ?    ?   ?   B . n 
B 1 270 MET 270 270  ?    ?   ?   B . n 
B 1 271 LYS 271 271  ?    ?   ?   B . n 
B 1 272 SER 272 272  ?    ?   ?   B . n 
B 1 273 ARG 273 273  ?    ?   ?   B . n 
B 1 274 LEU 274 274  ?    ?   ?   B . n 
B 1 275 ARG 275 275  ?    ?   ?   B . n 
B 1 276 ARG 276 276  ?    ?   ?   B . n 
B 1 277 THR 277 277  ?    ?   ?   B . n 
B 1 278 MET 278 278  ?    ?   ?   B . n 
B 1 279 LEU 279 279  ?    ?   ?   B . n 
B 1 280 VAL 280 280  ?    ?   ?   B . n 
B 1 281 ALA 281 281  ?    ?   ?   B . n 
B 1 282 LYS 282 282  ?    ?   ?   B . n 
B 1 283 VAL 283 283  ?    ?   ?   B . n 
B 1 284 THR 284 284  ?    ?   ?   B . n 
B 1 285 CYS 285 285  ?    ?   ?   B . n 
B 1 286 ILE 286 286  ?    ?   ?   B . n 
B 1 287 ILE 287 287  ?    ?   ?   B . n 
B 1 288 ILE 288 288  ?    ?   ?   B . n 
B 1 289 TRP 289 289  ?    ?   ?   B . n 
B 1 290 LEU 290 290  ?    ?   ?   B . n 
B 1 291 LEU 291 291  ?    ?   ?   B . n 
B 1 292 ALA 292 292  ?    ?   ?   B . n 
B 1 293 GLY 293 293  ?    ?   ?   B . n 
B 1 294 LEU 294 294  ?    ?   ?   B . n 
B 1 295 ALA 295 295  ?    ?   ?   B . n 
B 1 296 SER 296 296  ?    ?   ?   B . n 
B 1 297 LEU 297 297  ?    ?   ?   B . n 
B 1 298 PRO 298 298  ?    ?   ?   B . n 
B 1 299 ALA 299 299  ?    ?   ?   B . n 
B 1 300 ILE 300 300  ?    ?   ?   B . n 
B 1 301 ILE 301 301  ?    ?   ?   B . n 
B 1 302 HIS 302 302  ?    ?   ?   B . n 
B 1 303 ARG 303 303  ?    ?   ?   B . n 
B 1 304 ASN 304 304  ?    ?   ?   B . n 
B 1 305 VAL 305 305  ?    ?   ?   B . n 
B 1 306 PHE 306 306  ?    ?   ?   B . n 
B 1 307 PHE 307 307  ?    ?   ?   B . n 
B 1 308 ILE 308 308  ?    ?   ?   B . n 
B 1 309 GLU 309 309  ?    ?   ?   B . n 
B 1 310 ASN 310 310  ?    ?   ?   B . n 
B 1 311 THR 311 311  ?    ?   ?   B . n 
B 1 312 ASN 312 312  ?    ?   ?   B . n 
B 1 313 ILE 313 313  ?    ?   ?   B . n 
B 1 314 THR 314 314  ?    ?   ?   B . n 
B 1 315 VAL 315 315  ?    ?   ?   B . n 
B 1 316 CYS 316 316  ?    ?   ?   B . n 
B 1 317 ALA 317 317  ?    ?   ?   B . n 
B 1 318 PHE 318 318  ?    ?   ?   B . n 
B 1 319 HIS 319 319  ?    ?   ?   B . n 
B 1 320 TYR 320 320  ?    ?   ?   B . n 
B 1 321 GLU 321 321  ?    ?   ?   B . n 
B 1 322 SER 322 322  ?    ?   ?   B . n 
B 1 323 GLN 323 323  ?    ?   ?   B . n 
B 1 324 ASN 324 324  ?    ?   ?   B . n 
B 1 325 SER 325 325  ?    ?   ?   B . n 
B 1 326 THR 326 326  ?    ?   ?   B . n 
B 1 327 LEU 327 327  ?    ?   ?   B . n 
B 1 328 PRO 328 328  ?    ?   ?   B . n 
B 1 329 ILE 329 329  ?    ?   ?   B . n 
B 1 330 GLY 330 330  ?    ?   ?   B . n 
B 1 331 LEU 331 331  ?    ?   ?   B . n 
B 1 332 GLY 332 332  ?    ?   ?   B . n 
B 1 333 LEU 333 333  ?    ?   ?   B . n 
B 1 334 THR 334 334  ?    ?   ?   B . n 
B 1 335 LYS 335 335  ?    ?   ?   B . n 
B 1 336 ASN 336 336  ?    ?   ?   B . n 
B 1 337 ILE 337 337  ?    ?   ?   B . n 
B 1 338 LEU 338 338  ?    ?   ?   B . n 
B 1 339 GLY 339 339  ?    ?   ?   B . n 
B 1 340 PHE 340 340  ?    ?   ?   B . n 
B 1 341 LEU 341 341  ?    ?   ?   B . n 
B 1 342 PHE 342 342  ?    ?   ?   B . n 
B 1 343 PRO 343 343  ?    ?   ?   B . n 
B 1 344 PHE 344 344  ?    ?   ?   B . n 
B 1 345 LEU 345 345  ?    ?   ?   B . n 
B 1 346 ILE 346 346  ?    ?   ?   B . n 
B 1 347 ILE 347 347  ?    ?   ?   B . n 
B 1 348 LEU 348 348  ?    ?   ?   B . n 
B 1 349 THR 349 349  ?    ?   ?   B . n 
B 1 350 SER 350 350  ?    ?   ?   B . n 
B 1 351 TYR 351 351  ?    ?   ?   B . n 
B 1 352 THR 352 352  ?    ?   ?   B . n 
B 1 353 LEU 353 353  ?    ?   ?   B . n 
B 1 354 ILE 354 354  ?    ?   ?   B . n 
B 1 355 TRP 355 355  ?    ?   ?   B . n 
B 1 356 LYS 356 356  ?    ?   ?   B . n 
B 1 357 ALA 357 357  ?    ?   ?   B . n 
B 1 358 LEU 358 358  ?    ?   ?   B . n 
B 1 359 LYS 359 359  ?    ?   ?   B . n 
B 1 360 LYS 360 360  ?    ?   ?   B . n 
B 1 361 ALA 361 361  ?    ?   ?   B . n 
B 1 362 TYR 362 362  ?    ?   ?   B . n 
B 1 363 ASP 363 363  ?    ?   ?   B . n 
B 1 364 LEU 364 364  ?    ?   ?   B . n 
B 1 365 GLU 365 365  ?    ?   ?   B . n 
B 1 366 ASP 366 366  ?    ?   ?   B . n 
B 1 367 ASN 367 367  ?    ?   ?   B . n 
B 1 368 TRP 368 368  ?    ?   ?   B . n 
B 1 369 GLU 369 369  ?    ?   ?   B . n 
B 1 370 THR 370 370  ?    ?   ?   B . n 
B 1 371 LEU 371 371  ?    ?   ?   B . n 
B 1 372 ASN 372 372  ?    ?   ?   B . n 
B 1 373 ASP 373 373  ?    ?   ?   B . n 
B 1 374 ASN 374 374  ?    ?   ?   B . n 
B 1 375 LEU 375 375  ?    ?   ?   B . n 
B 1 376 LYS 376 376  ?    ?   ?   B . n 
B 1 377 VAL 377 377  ?    ?   ?   B . n 
B 1 378 ILE 378 378  ?    ?   ?   B . n 
B 1 379 GLU 379 379  ?    ?   ?   B . n 
B 1 380 LYS 380 380  ?    ?   ?   B . n 
B 1 381 ALA 381 381  ?    ?   ?   B . n 
B 1 382 ASP 382 382  ?    ?   ?   B . n 
B 1 383 ASN 383 383  ?    ?   ?   B . n 
B 1 384 ALA 384 384  ?    ?   ?   B . n 
B 1 385 ALA 385 385  ?    ?   ?   B . n 
B 1 386 GLN 386 386  ?    ?   ?   B . n 
B 1 387 VAL 387 387  ?    ?   ?   B . n 
B 1 388 LYS 388 388  ?    ?   ?   B . n 
B 1 389 ASP 389 389  ?    ?   ?   B . n 
B 1 390 ALA 390 390  ?    ?   ?   B . n 
B 1 391 LEU 391 391  ?    ?   ?   B . n 
B 1 392 THR 392 392  ?    ?   ?   B . n 
B 1 393 LYS 393 393  ?    ?   ?   B . n 
B 1 394 MET 394 394  ?    ?   ?   B . n 
B 1 395 ARG 395 395  ?    ?   ?   B . n 
B 1 396 ALA 396 396  ?    ?   ?   B . n 
B 1 397 ALA 397 397  ?    ?   ?   B . n 
B 1 398 ALA 398 398  ?    ?   ?   B . n 
B 1 399 LEU 399 399  ?    ?   ?   B . n 
B 1 400 ASP 400 400  ?    ?   ?   B . n 
B 1 401 ALA 401 401  ?    ?   ?   B . n 
B 1 402 GLN 402 402  ?    ?   ?   B . n 
B 1 403 LYS 403 403  ?    ?   ?   B . n 
B 1 404 ALA 404 404  ?    ?   ?   B . n 
B 1 405 THR 405 405  ?    ?   ?   B . n 
B 1 406 PRO 406 406  ?    ?   ?   B . n 
B 1 407 PRO 407 407  ?    ?   ?   B . n 
B 1 408 LYS 408 408  ?    ?   ?   B . n 
B 1 409 LEU 409 409  ?    ?   ?   B . n 
B 1 410 GLU 410 410  ?    ?   ?   B . n 
B 1 411 ASP 411 411  ?    ?   ?   B . n 
B 1 412 LYS 412 412  ?    ?   ?   B . n 
B 1 413 SER 413 413  ?    ?   ?   B . n 
B 1 414 PRO 414 414  ?    ?   ?   B . n 
B 1 415 ASP 415 415  ?    ?   ?   B . n 
B 1 416 SER 416 416  ?    ?   ?   B . n 
B 1 417 PRO 417 417  ?    ?   ?   B . n 
B 1 418 GLU 418 418  ?    ?   ?   B . n 
B 1 419 MET 419 419  ?    ?   ?   B . n 
B 1 420 LYS 420 420  ?    ?   ?   B . n 
B 1 421 ASP 421 421  ?    ?   ?   B . n 
B 1 422 PHE 422 422  ?    ?   ?   B . n 
B 1 423 ARG 423 423  ?    ?   ?   B . n 
B 1 424 HIS 424 424  ?    ?   ?   B . n 
B 1 425 GLY 425 425  ?    ?   ?   B . n 
B 1 426 PHE 426 426  ?    ?   ?   B . n 
B 1 427 ASP 427 427  ?    ?   ?   B . n 
B 1 428 ILE 428 428  ?    ?   ?   B . n 
B 1 429 LEU 429 429  ?    ?   ?   B . n 
B 1 430 VAL 430 430  ?    ?   ?   B . n 
B 1 431 GLY 431 431  ?    ?   ?   B . n 
B 1 432 GLN 432 432  ?    ?   ?   B . n 
B 1 433 ILE 433 433  ?    ?   ?   B . n 
B 1 434 ASP 434 434  ?    ?   ?   B . n 
B 1 435 ASP 435 435  ?    ?   ?   B . n 
B 1 436 ALA 436 436  ?    ?   ?   B . n 
B 1 437 LEU 437 437  ?    ?   ?   B . n 
B 1 438 LYS 438 438  ?    ?   ?   B . n 
B 1 439 LEU 439 439  ?    ?   ?   B . n 
B 1 440 ALA 440 440  ?    ?   ?   B . n 
B 1 441 ASN 441 441  ?    ?   ?   B . n 
B 1 442 GLU 442 442  ?    ?   ?   B . n 
B 1 443 GLY 443 443  ?    ?   ?   B . n 
B 1 444 LYS 444 444  ?    ?   ?   B . n 
B 1 445 VAL 445 445  ?    ?   ?   B . n 
B 1 446 LYS 446 446  ?    ?   ?   B . n 
B 1 447 GLU 447 447  ?    ?   ?   B . n 
B 1 448 ALA 448 448  ?    ?   ?   B . n 
B 1 449 GLN 449 449  ?    ?   ?   B . n 
B 1 450 ALA 450 450  ?    ?   ?   B . n 
B 1 451 ALA 451 451  ?    ?   ?   B . n 
B 1 452 ALA 452 452  ?    ?   ?   B . n 
B 1 453 GLU 453 453  ?    ?   ?   B . n 
B 1 454 GLN 454 454  ?    ?   ?   B . n 
B 1 455 LEU 455 455  ?    ?   ?   B . n 
B 1 456 LYS 456 456  ?    ?   ?   B . n 
B 1 457 THR 457 457  ?    ?   ?   B . n 
B 1 458 THR 458 458  ?    ?   ?   B . n 
B 1 459 ARG 459 459  ?    ?   ?   B . n 
B 1 460 ASN 460 460  ?    ?   ?   B . n 
B 1 461 ALA 461 461  ?    ?   ?   B . n 
B 1 462 TYR 462 462  ?    ?   ?   B . n 
B 1 463 ILE 463 463  ?    ?   ?   B . n 
B 1 464 GLN 464 464  ?    ?   ?   B . n 
B 1 465 LYS 465 465  ?    ?   ?   B . n 
B 1 466 TYR 466 466  ?    ?   ?   B . n 
B 1 467 LEU 467 467  ?    ?   ?   B . n 
B 1 468 GLU 468 468  ?    ?   ?   B . n 
B 1 469 ARG 469 469  ?    ?   ?   B . n 
B 1 470 ALA 470 470  ?    ?   ?   B . n 
B 1 471 ARG 471 471  ?    ?   ?   B . n 
B 1 472 SER 472 472  ?    ?   ?   B . n 
B 1 473 THR 473 473  ?    ?   ?   B . n 
B 1 474 LEU 474 474  ?    ?   ?   B . n 
B 1 475 ASP 475 475  ?    ?   ?   B . n 
B 1 476 LYS 476 476  ?    ?   ?   B . n 
B 1 477 LEU 477 477  ?    ?   ?   B . n 
B 1 478 ASN 478 478  ?    ?   ?   B . n 
B 1 479 ASP 479 479  ?    ?   ?   B . n 
B 1 480 ASP 480 480  ?    ?   ?   B . n 
B 1 481 ILE 481 481  ?    ?   ?   B . n 
B 1 482 PHE 482 482  ?    ?   ?   B . n 
B 1 483 LYS 483 483  ?    ?   ?   B . n 
B 1 484 ILE 484 484  ?    ?   ?   B . n 
B 1 485 ILE 485 485  ?    ?   ?   B . n 
B 1 486 MET 486 486  ?    ?   ?   B . n 
B 1 487 ALA 487 487  ?    ?   ?   B . n 
B 1 488 ILE 488 488  ?    ?   ?   B . n 
B 1 489 VAL 489 489  ?    ?   ?   B . n 
B 1 490 LEU 490 490  ?    ?   ?   B . n 
B 1 491 PHE 491 491  ?    ?   ?   B . n 
B 1 492 PHE 492 492  ?    ?   ?   B . n 
B 1 493 PHE 493 493  ?    ?   ?   B . n 
B 1 494 PHE 494 494  ?    ?   ?   B . n 
B 1 495 SER 495 495  ?    ?   ?   B . n 
B 1 496 TRP 496 496  ?    ?   ?   B . n 
B 1 497 ILE 497 497  ?    ?   ?   B . n 
B 1 498 PRO 498 498  ?    ?   ?   B . n 
B 1 499 HIS 499 499  ?    ?   ?   B . n 
B 1 500 GLN 500 500  ?    ?   ?   B . n 
B 1 501 ILE 501 501  ?    ?   ?   B . n 
B 1 502 PHE 502 502  ?    ?   ?   B . n 
B 1 503 THR 503 503  ?    ?   ?   B . n 
B 1 504 PHE 504 504  ?    ?   ?   B . n 
B 1 505 LEU 505 505  ?    ?   ?   B . n 
B 1 506 ASP 506 506  ?    ?   ?   B . n 
B 1 507 VAL 507 507  ?    ?   ?   B . n 
B 1 508 LEU 508 508  ?    ?   ?   B . n 
B 1 509 ILE 509 509  ?    ?   ?   B . n 
B 1 510 GLN 510 510  ?    ?   ?   B . n 
B 1 511 LEU 511 511  ?    ?   ?   B . n 
B 1 512 GLY 512 512  ?    ?   ?   B . n 
B 1 513 ILE 513 513  ?    ?   ?   B . n 
B 1 514 ILE 514 514  ?    ?   ?   B . n 
B 1 515 ARG 515 515  ?    ?   ?   B . n 
B 1 516 ASP 516 516  ?    ?   ?   B . n 
B 1 517 CYS 517 517  ?    ?   ?   B . n 
B 1 518 ARG 518 518  ?    ?   ?   B . n 
B 1 519 ILE 519 519  ?    ?   ?   B . n 
B 1 520 ALA 520 520  ?    ?   ?   B . n 
B 1 521 ASP 521 521  ?    ?   ?   B . n 
B 1 522 ILE 522 522  ?    ?   ?   B . n 
B 1 523 VAL 523 523  ?    ?   ?   B . n 
B 1 524 ASP 524 524  ?    ?   ?   B . n 
B 1 525 THR 525 525  ?    ?   ?   B . n 
B 1 526 ALA 526 526  ?    ?   ?   B . n 
B 1 527 MET 527 527  ?    ?   ?   B . n 
B 1 528 PRO 528 528  ?    ?   ?   B . n 
B 1 529 ILE 529 529  ?    ?   ?   B . n 
B 1 530 THR 530 530  ?    ?   ?   B . n 
B 1 531 ILE 531 531  ?    ?   ?   B . n 
B 1 532 CYS 532 532  ?    ?   ?   B . n 
B 1 533 ILE 533 533  ?    ?   ?   B . n 
B 1 534 ALA 534 534  ?    ?   ?   B . n 
B 1 535 TYR 535 535  ?    ?   ?   B . n 
B 1 536 PHE 536 536  ?    ?   ?   B . n 
B 1 537 ASN 537 537  ?    ?   ?   B . n 
B 1 538 ASN 538 538  ?    ?   ?   B . n 
B 1 539 CYS 539 539  ?    ?   ?   B . n 
B 1 540 LEU 540 540  ?    ?   ?   B . n 
B 1 541 ASN 541 541  ?    ?   ?   B . n 
B 1 542 PRO 542 542  ?    ?   ?   B . n 
B 1 543 LEU 543 543  ?    ?   ?   B . n 
B 1 544 PHE 544 544  ?    ?   ?   B . n 
B 1 545 TYR 545 545  ?    ?   ?   B . n 
B 1 546 GLY 546 546  ?    ?   ?   B . n 
B 1 547 PHE 547 547  ?    ?   ?   B . n 
B 1 548 LEU 548 548  ?    ?   ?   B . n 
B 1 549 GLY 549 549  ?    ?   ?   B . n 
B 1 550 LYS 550 550  ?    ?   ?   B . n 
B 1 551 LYS 551 551  ?    ?   ?   B . n 
B 1 552 PHE 552 552  ?    ?   ?   B . n 
B 1 553 LYS 553 553  ?    ?   ?   B . n 
B 1 554 ARG 554 554  ?    ?   ?   B . n 
B 1 555 TYR 555 555  ?    ?   ?   B . n 
B 1 556 PHE 556 556  ?    ?   ?   B . n 
B 1 557 LEU 557 557  ?    ?   ?   B . n 
B 1 558 GLN 558 558  ?    ?   ?   B . n 
B 1 559 LEU 559 559  ?    ?   ?   B . n 
B 1 560 LEU 560 560  ?    ?   ?   B . n 
B 1 561 LYS 561 561  ?    ?   ?   B . n 
B 1 562 TYR 562 562  ?    ?   ?   B . n 
B 1 563 GLY 563 563  ?    ?   ?   B . n 
B 1 564 GLY 564 564  ?    ?   ?   B . n 
B 1 565 SER 565 565  ?    ?   ?   B . n 
B 1 566 SER 566 566  ?    ?   ?   B . n 
B 1 567 LEU 567 567  ?    ?   ?   B . n 
B 1 568 GLU 568 568  ?    ?   ?   B . n 
B 1 569 VAL 569 569  ?    ?   ?   B . n 
B 1 570 LEU 570 570  ?    ?   ?   B . n 
B 1 571 PHE 571 571  ?    ?   ?   B . n 
B 1 572 GLN 572 572  ?    ?   ?   B . n 
B 1 573 GLY 573 573  ?    ?   ?   B . n 
B 1 574 PRO 574 574  ?    ?   ?   B . n 
B 1 575 THR 575 575  ?    ?   ?   B . n 
B 1 576 GLU 576 576  ?    ?   ?   B . n 
B 1 577 THR 577 577  ?    ?   ?   B . n 
B 1 578 SER 578 578  ?    ?   ?   B . n 
B 1 579 GLN 579 579  ?    ?   ?   B . n 
B 1 580 VAL 580 580  ?    ?   ?   B . n 
B 1 581 ALA 581 581  ?    ?   ?   B . n 
B 1 582 PRO 582 582  ?    ?   ?   B . n 
B 1 583 ALA 583 583  ?    ?   ?   B . n 
C 2 1   GLU 1   1    ?    ?   ?   C . n 
C 2 2   ILE 2   2    ?    ?   ?   C . n 
C 2 3   SER 3   3    ?    ?   ?   C . n 
C 2 4   GLU 4   4    4    GLU GLU C . n 
C 2 5   VAL 5   5    5    VAL VAL C . n 
C 2 6   GLN 6   6    6    GLN GLN C . n 
C 2 7   LEU 7   7    7    LEU LEU C . n 
C 2 8   VAL 8   8    8    VAL VAL C . n 
C 2 9   GLU 9   9    9    GLU GLU C . n 
C 2 10  SER 10  10   10   SER SER C . n 
C 2 11  GLY 11  11   11   GLY GLY C . n 
C 2 12  GLY 12  12   12   GLY GLY C . n 
C 2 13  GLY 13  13   13   GLY GLY C . n 
C 2 14  LEU 14  14   14   LEU LEU C . n 
C 2 15  VAL 15  15   15   VAL VAL C . n 
C 2 16  GLN 16  16   16   GLN GLN C . n 
C 2 17  PRO 17  17   17   PRO PRO C . n 
C 2 18  GLY 18  18   18   GLY GLY C . n 
C 2 19  GLY 19  19   19   GLY GLY C . n 
C 2 20  SER 20  20   20   SER SER C . n 
C 2 21  LEU 21  21   21   LEU LEU C . n 
C 2 22  ARG 22  22   22   ARG ARG C . n 
C 2 23  LEU 23  23   23   LEU LEU C . n 
C 2 24  SER 24  24   24   SER SER C . n 
C 2 25  CYS 25  25   25   CYS CYS C . n 
C 2 26  ALA 26  26   26   ALA ALA C . n 
C 2 27  ALA 27  27   27   ALA ALA C . n 
C 2 28  SER 28  28   28   SER SER C . n 
C 2 29  GLY 29  29   29   GLY GLY C . n 
C 2 30  PHE 30  30   30   PHE PHE C . n 
C 2 31  ASN 31  31   31   ASN ASN C . n 
C 2 32  VAL 32  32   32   VAL VAL C . n 
C 2 33  VAL 33  33   33   VAL VAL C . n 
C 2 34  ASP 34  34   34   ASP ASP C . n 
C 2 35  PHE 35  35   35   PHE PHE C . n 
C 2 36  SER 36  36   36   SER SER C . n 
C 2 37  LEU 37  37   37   LEU LEU C . n 
C 2 38  HIS 38  38   38   HIS HIS C . n 
C 2 39  TRP 39  39   39   TRP TRP C . n 
C 2 40  VAL 40  40   40   VAL VAL C . n 
C 2 41  ARG 41  41   41   ARG ARG C . n 
C 2 42  GLN 42  42   42   GLN GLN C . n 
C 2 43  ALA 43  43   43   ALA ALA C . n 
C 2 44  PRO 44  44   44   PRO PRO C . n 
C 2 45  GLY 45  45   45   GLY GLY C . n 
C 2 46  LYS 46  46   46   LYS LYS C . n 
C 2 47  GLY 47  47   47   GLY GLY C . n 
C 2 48  LEU 48  48   48   LEU LEU C . n 
C 2 49  GLU 49  49   49   GLU GLU C . n 
C 2 50  TRP 50  50   50   TRP TRP C . n 
C 2 51  VAL 51  51   51   VAL VAL C . n 
C 2 52  ALA 52  52   52   ALA ALA C . n 
C 2 53  TYR 53  53   53   TYR TYR C . n 
C 2 54  ILE 54  54   54   ILE ILE C . n 
C 2 55  SER 55  55   55   SER SER C . n 
C 2 56  SER 56  56   56   SER SER C . n 
C 2 57  SER 57  57   57   SER SER C . n 
C 2 58  SER 58  58   58   SER SER C . n 
C 2 59  GLY 59  59   59   GLY GLY C . n 
C 2 60  SER 60  60   60   SER SER C . n 
C 2 61  THR 61  61   61   THR THR C . n 
C 2 62  SER 62  62   62   SER SER C . n 
C 2 63  TYR 63  63   63   TYR TYR C . n 
C 2 64  ALA 64  64   64   ALA ALA C . n 
C 2 65  ASP 65  65   65   ASP ASP C . n 
C 2 66  SER 66  66   66   SER SER C . n 
C 2 67  VAL 67  67   67   VAL VAL C . n 
C 2 68  LYS 68  68   68   LYS LYS C . n 
C 2 69  GLY 69  69   69   GLY GLY C . n 
C 2 70  ARG 70  70   70   ARG ARG C . n 
C 2 71  PHE 71  71   71   PHE PHE C . n 
C 2 72  THR 72  72   72   THR THR C . n 
C 2 73  ILE 73  73   73   ILE ILE C . n 
C 2 74  SER 74  74   74   SER SER C . n 
C 2 75  ALA 75  75   75   ALA ALA C . n 
C 2 76  ASP 76  76   76   ASP ASP C . n 
C 2 77  THR 77  77   77   THR THR C . n 
C 2 78  SER 78  78   78   SER SER C . n 
C 2 79  LYS 79  79   79   LYS LYS C . n 
C 2 80  ASN 80  80   80   ASN ASN C . n 
C 2 81  THR 81  81   81   THR THR C . n 
C 2 82  ALA 82  82   82   ALA ALA C . n 
C 2 83  TYR 83  83   83   TYR TYR C . n 
C 2 84  LEU 84  84   84   LEU LEU C . n 
C 2 85  GLN 85  85   85   GLN GLN C . n 
C 2 86  MET 86  86   86   MET MET C . n 
C 2 87  ASN 87  87   87   ASN ASN C . n 
C 2 88  SER 88  88   88   SER SER C . n 
C 2 89  LEU 89  89   89   LEU LEU C . n 
C 2 90  ARG 90  90   90   ARG ARG C . n 
C 2 91  ALA 91  91   91   ALA ALA C . n 
C 2 92  GLU 92  92   92   GLU GLU C . n 
C 2 93  ASP 93  93   93   ASP ASP C . n 
C 2 94  THR 94  94   94   THR THR C . n 
C 2 95  ALA 95  95   95   ALA ALA C . n 
C 2 96  VAL 96  96   96   VAL VAL C . n 
C 2 97  TYR 97  97   97   TYR TYR C . n 
C 2 98  TYR 98  98   98   TYR TYR C . n 
C 2 99  CYS 99  99   99   CYS CYS C . n 
C 2 100 ALA 100 100  100  ALA ALA C . n 
C 2 101 ARG 101 101  101  ARG ARG C . n 
C 2 102 TRP 102 102  102  TRP TRP C . n 
C 2 103 GLY 103 103  103  GLY GLY C . n 
C 2 104 TYR 104 104  104  TYR TYR C . n 
C 2 105 TRP 105 105  105  TRP TRP C . n 
C 2 106 PRO 106 106  106  PRO PRO C . n 
C 2 107 GLY 107 107  107  GLY GLY C . n 
C 2 108 GLU 108 108  108  GLU GLU C . n 
C 2 109 PRO 109 109  109  PRO PRO C . n 
C 2 110 TRP 110 110  110  TRP TRP C . n 
C 2 111 TRP 111 111  111  TRP TRP C . n 
C 2 112 LYS 112 112  112  LYS LYS C . n 
C 2 113 ALA 113 113  113  ALA ALA C . n 
C 2 114 PHE 114 114  114  PHE PHE C . n 
C 2 115 ASP 115 115  115  ASP ASP C . n 
C 2 116 TYR 116 116  116  TYR TYR C . n 
C 2 117 TRP 117 117  117  TRP TRP C . n 
C 2 118 GLY 118 118  118  GLY GLY C . n 
C 2 119 GLN 119 119  119  GLN GLN C . n 
C 2 120 GLY 120 120  120  GLY GLY C . n 
C 2 121 THR 121 121  121  THR THR C . n 
C 2 122 LEU 122 122  122  LEU LEU C . n 
C 2 123 VAL 123 123  123  VAL VAL C . n 
C 2 124 THR 124 124  124  THR THR C . n 
C 2 125 VAL 125 125  125  VAL VAL C . n 
C 2 126 SER 126 126  ?    ?   ?   C . n 
C 2 127 SER 127 127  ?    ?   ?   C . n 
C 2 128 ALA 128 128  ?    ?   ?   C . n 
C 2 129 SER 129 129  ?    ?   ?   C . n 
C 2 130 THR 130 130  ?    ?   ?   C . n 
C 2 131 LYS 131 131  ?    ?   ?   C . n 
C 2 132 GLY 132 132  ?    ?   ?   C . n 
C 2 133 PRO 133 133  ?    ?   ?   C . n 
C 2 134 SER 134 134  ?    ?   ?   C . n 
C 2 135 VAL 135 135  ?    ?   ?   C . n 
C 2 136 PHE 136 136  ?    ?   ?   C . n 
C 2 137 PRO 137 137  ?    ?   ?   C . n 
C 2 138 LEU 138 138  ?    ?   ?   C . n 
C 2 139 ALA 139 139  ?    ?   ?   C . n 
C 2 140 PRO 140 140  ?    ?   ?   C . n 
C 2 141 SER 141 141  ?    ?   ?   C . n 
C 2 142 SER 142 142  ?    ?   ?   C . n 
C 2 143 LYS 143 143  ?    ?   ?   C . n 
C 2 144 SER 144 144  ?    ?   ?   C . n 
C 2 145 THR 145 145  ?    ?   ?   C . n 
C 2 146 SER 146 146  ?    ?   ?   C . n 
C 2 147 GLY 147 147  ?    ?   ?   C . n 
C 2 148 GLY 148 148  ?    ?   ?   C . n 
C 2 149 THR 149 149  ?    ?   ?   C . n 
C 2 150 ALA 150 150  ?    ?   ?   C . n 
C 2 151 ALA 151 151  ?    ?   ?   C . n 
C 2 152 LEU 152 152  ?    ?   ?   C . n 
C 2 153 GLY 153 153  ?    ?   ?   C . n 
C 2 154 CYS 154 154  ?    ?   ?   C . n 
C 2 155 LEU 155 155  ?    ?   ?   C . n 
C 2 156 VAL 156 156  ?    ?   ?   C . n 
C 2 157 LYS 157 157  ?    ?   ?   C . n 
C 2 158 ASP 158 158  ?    ?   ?   C . n 
C 2 159 TYR 159 159  ?    ?   ?   C . n 
C 2 160 PHE 160 160  ?    ?   ?   C . n 
C 2 161 PRO 161 161  ?    ?   ?   C . n 
C 2 162 GLU 162 162  ?    ?   ?   C . n 
C 2 163 PRO 163 163  ?    ?   ?   C . n 
C 2 164 VAL 164 164  ?    ?   ?   C . n 
C 2 165 THR 165 165  ?    ?   ?   C . n 
C 2 166 VAL 166 166  ?    ?   ?   C . n 
C 2 167 SER 167 167  ?    ?   ?   C . n 
C 2 168 TRP 168 168  ?    ?   ?   C . n 
C 2 169 ASN 169 169  ?    ?   ?   C . n 
C 2 170 SER 170 170  ?    ?   ?   C . n 
C 2 171 GLY 171 171  ?    ?   ?   C . n 
C 2 172 ALA 172 172  ?    ?   ?   C . n 
C 2 173 LEU 173 173  ?    ?   ?   C . n 
C 2 174 THR 174 174  ?    ?   ?   C . n 
C 2 175 SER 175 175  ?    ?   ?   C . n 
C 2 176 GLY 176 176  ?    ?   ?   C . n 
C 2 177 VAL 177 177  ?    ?   ?   C . n 
C 2 178 HIS 178 178  ?    ?   ?   C . n 
C 2 179 THR 179 179  ?    ?   ?   C . n 
C 2 180 PHE 180 180  ?    ?   ?   C . n 
C 2 181 PRO 181 181  ?    ?   ?   C . n 
C 2 182 ALA 182 182  ?    ?   ?   C . n 
C 2 183 VAL 183 183  ?    ?   ?   C . n 
C 2 184 LEU 184 184  ?    ?   ?   C . n 
C 2 185 GLN 185 185  ?    ?   ?   C . n 
C 2 186 SER 186 186  ?    ?   ?   C . n 
C 2 187 SER 187 187  ?    ?   ?   C . n 
C 2 188 GLY 188 188  ?    ?   ?   C . n 
C 2 189 LEU 189 189  ?    ?   ?   C . n 
C 2 190 TYR 190 190  ?    ?   ?   C . n 
C 2 191 SER 191 191  ?    ?   ?   C . n 
C 2 192 LEU 192 192  ?    ?   ?   C . n 
C 2 193 SER 193 193  ?    ?   ?   C . n 
C 2 194 SER 194 194  ?    ?   ?   C . n 
C 2 195 VAL 195 195  ?    ?   ?   C . n 
C 2 196 VAL 196 196  ?    ?   ?   C . n 
C 2 197 THR 197 197  ?    ?   ?   C . n 
C 2 198 VAL 198 198  ?    ?   ?   C . n 
C 2 199 PRO 199 199  ?    ?   ?   C . n 
C 2 200 SER 200 200  ?    ?   ?   C . n 
C 2 201 SER 201 201  ?    ?   ?   C . n 
C 2 202 SER 202 202  ?    ?   ?   C . n 
C 2 203 LEU 203 203  ?    ?   ?   C . n 
C 2 204 GLY 204 204  ?    ?   ?   C . n 
C 2 205 THR 205 205  ?    ?   ?   C . n 
C 2 206 GLN 206 206  ?    ?   ?   C . n 
C 2 207 THR 207 207  ?    ?   ?   C . n 
C 2 208 TYR 208 208  ?    ?   ?   C . n 
C 2 209 ILE 209 209  ?    ?   ?   C . n 
C 2 210 CYS 210 210  ?    ?   ?   C . n 
C 2 211 ASN 211 211  ?    ?   ?   C . n 
C 2 212 VAL 212 212  ?    ?   ?   C . n 
C 2 213 ASN 213 213  ?    ?   ?   C . n 
C 2 214 HIS 214 214  ?    ?   ?   C . n 
C 2 215 LYS 215 215  ?    ?   ?   C . n 
C 2 216 PRO 216 216  ?    ?   ?   C . n 
C 2 217 SER 217 217  ?    ?   ?   C . n 
C 2 218 ASN 218 218  ?    ?   ?   C . n 
C 2 219 THR 219 219  ?    ?   ?   C . n 
C 2 220 LYS 220 220  ?    ?   ?   C . n 
C 2 221 VAL 221 221  ?    ?   ?   C . n 
C 2 222 ASP 222 222  ?    ?   ?   C . n 
C 2 223 LYS 223 223  ?    ?   ?   C . n 
C 2 224 LYS 224 224  ?    ?   ?   C . n 
C 2 225 VAL 225 225  ?    ?   ?   C . n 
C 2 226 GLU 226 226  ?    ?   ?   C . n 
C 2 227 PRO 227 227  ?    ?   ?   C . n 
C 2 228 LYS 228 228  ?    ?   ?   C . n 
C 2 229 SER 229 229  ?    ?   ?   C . n 
C 2 230 CYS 230 230  ?    ?   ?   C . n 
C 2 231 ASP 231 231  ?    ?   ?   C . n 
D 3 1   ASP 1   2    2    ASP ASP D . n 
D 3 2   ILE 2   3    3    ILE ILE D . n 
D 3 3   GLN 3   4    4    GLN GLN D . n 
D 3 4   MET 4   5    5    MET MET D . n 
D 3 5   THR 5   6    6    THR THR D . n 
D 3 6   GLN 6   7    7    GLN GLN D . n 
D 3 7   SER 7   8    8    SER SER D . n 
D 3 8   PRO 8   9    9    PRO PRO D . n 
D 3 9   SER 9   10   10   SER SER D . n 
D 3 10  SER 10  11   11   SER SER D . n 
D 3 11  LEU 11  12   12   LEU LEU D . n 
D 3 12  SER 12  13   13   SER SER D . n 
D 3 13  ALA 13  14   14   ALA ALA D . n 
D 3 14  SER 14  15   15   SER SER D . n 
D 3 15  VAL 15  16   16   VAL VAL D . n 
D 3 16  GLY 16  17   17   GLY GLY D . n 
D 3 17  ASP 17  18   18   ASP ASP D . n 
D 3 18  ARG 18  19   19   ARG ARG D . n 
D 3 19  VAL 19  20   20   VAL VAL D . n 
D 3 20  THR 20  21   21   THR THR D . n 
D 3 21  ILE 21  22   22   ILE ILE D . n 
D 3 22  THR 22  23   23   THR THR D . n 
D 3 23  CYS 23  24   24   CYS CYS D . n 
D 3 24  ARG 24  25   25   ARG ARG D . n 
D 3 25  ALA 25  26   26   ALA ALA D . n 
D 3 26  SER 26  27   27   SER SER D . n 
D 3 27  GLN 27  28   28   GLN GLN D . n 
D 3 28  SER 28  29   29   SER SER D . n 
D 3 29  VAL 29  30   30   VAL VAL D . n 
D 3 30  SER 30  31   31   SER SER D . n 
D 3 31  SER 31  32   32   SER SER D . n 
D 3 32  ALA 32  33   33   ALA ALA D . n 
D 3 33  VAL 33  34   34   VAL VAL D . n 
D 3 34  ALA 34  35   35   ALA ALA D . n 
D 3 35  TRP 35  36   36   TRP TRP D . n 
D 3 36  TYR 36  37   37   TYR TYR D . n 
D 3 37  GLN 37  38   38   GLN GLN D . n 
D 3 38  GLN 38  39   39   GLN GLN D . n 
D 3 39  LYS 39  40   40   LYS LYS D . n 
D 3 40  PRO 40  41   41   PRO PRO D . n 
D 3 41  GLY 41  42   42   GLY GLY D . n 
D 3 42  LYS 42  43   43   LYS LYS D . n 
D 3 43  ALA 43  44   44   ALA ALA D . n 
D 3 44  PRO 44  45   45   PRO PRO D . n 
D 3 45  LYS 45  46   46   LYS LYS D . n 
D 3 46  LEU 46  47   47   LEU LEU D . n 
D 3 47  LEU 47  48   48   LEU LEU D . n 
D 3 48  ILE 48  49   49   ILE ILE D . n 
D 3 49  TYR 49  50   50   TYR TYR D . n 
D 3 50  SER 50  51   51   SER SER D . n 
D 3 51  ALA 51  52   52   ALA ALA D . n 
D 3 52  SER 52  53   53   SER SER D . n 
D 3 53  SER 53  54   54   SER SER D . n 
D 3 54  LEU 54  55   55   LEU LEU D . n 
D 3 55  TYR 55  56   56   TYR TYR D . n 
D 3 56  SER 56  57   57   SER SER D . n 
D 3 57  GLY 57  58   58   GLY GLY D . n 
D 3 58  VAL 58  59   59   VAL VAL D . n 
D 3 59  PRO 59  60   60   PRO PRO D . n 
D 3 60  SER 60  61   61   SER SER D . n 
D 3 61  ARG 61  62   62   ARG ARG D . n 
D 3 62  PHE 62  63   63   PHE PHE D . n 
D 3 63  SER 63  64   64   SER SER D . n 
D 3 64  GLY 64  65   65   GLY GLY D . n 
D 3 65  SER 65  66   66   SER SER D . n 
D 3 66  ARG 66  67   67   ARG ARG D . n 
D 3 67  SER 67  68   68   SER SER D . n 
D 3 68  GLY 68  69   69   GLY GLY D . n 
D 3 69  THR 69  70   70   THR THR D . n 
D 3 70  ASP 70  71   71   ASP ASP D . n 
D 3 71  PHE 71  72   72   PHE PHE D . n 
D 3 72  THR 72  73   73   THR THR D . n 
D 3 73  LEU 73  74   74   LEU LEU D . n 
D 3 74  THR 74  75   75   THR THR D . n 
D 3 75  ILE 75  76   76   ILE ILE D . n 
D 3 76  SER 76  77   77   SER SER D . n 
D 3 77  SER 77  78   78   SER SER D . n 
D 3 78  LEU 78  79   79   LEU LEU D . n 
D 3 79  GLN 79  80   80   GLN GLN D . n 
D 3 80  PRO 80  81   81   PRO PRO D . n 
D 3 81  GLU 81  82   82   GLU GLU D . n 
D 3 82  ASP 82  83   83   ASP ASP D . n 
D 3 83  PHE 83  84   84   PHE PHE D . n 
D 3 84  ALA 84  85   85   ALA ALA D . n 
D 3 85  THR 85  86   86   THR THR D . n 
D 3 86  TYR 86  87   87   TYR TYR D . n 
D 3 87  TYR 87  88   88   TYR TYR D . n 
D 3 88  CYS 88  89   89   CYS CYS D . n 
D 3 89  GLN 89  90   90   GLN GLN D . n 
D 3 90  GLN 90  91   91   GLN GLN D . n 
D 3 91  TYR 91  92   92   TYR TYR D . n 
D 3 92  LEU 92  93   93   LEU LEU D . n 
D 3 93  TYR 93  94   94   TYR TYR D . n 
D 3 94  TYR 94  95   95   TYR TYR D . n 
D 3 95  SER 95  96   96   SER SER D . n 
D 3 96  LEU 96  97   97   LEU LEU D . n 
D 3 97  VAL 97  98   98   VAL VAL D . n 
D 3 98  THR 98  99   99   THR THR D . n 
D 3 99  PHE 99  100  100  PHE PHE D . n 
D 3 100 GLY 100 101  101  GLY GLY D . n 
D 3 101 GLN 101 102  102  GLN GLN D . n 
D 3 102 GLY 102 103  103  GLY GLY D . n 
D 3 103 THR 103 104  104  THR THR D . n 
D 3 104 LYS 104 105  105  LYS LYS D . n 
D 3 105 VAL 105 106  106  VAL VAL D . n 
D 3 106 GLU 106 107  107  GLU GLU D . n 
D 3 107 ILE 107 108  108  ILE ILE D . n 
D 3 108 LYS 108 109  109  LYS LYS D . n 
D 3 109 ARG 109 110  110  ARG ARG D . n 
D 3 110 THR 110 111  ?    ?   ?   D . n 
D 3 111 VAL 111 112  ?    ?   ?   D . n 
D 3 112 ALA 112 113  ?    ?   ?   D . n 
D 3 113 ALA 113 114  ?    ?   ?   D . n 
D 3 114 PRO 114 115  ?    ?   ?   D . n 
D 3 115 SER 115 116  ?    ?   ?   D . n 
D 3 116 VAL 116 117  ?    ?   ?   D . n 
D 3 117 PHE 117 118  ?    ?   ?   D . n 
D 3 118 ILE 118 119  ?    ?   ?   D . n 
D 3 119 PHE 119 120  ?    ?   ?   D . n 
D 3 120 PRO 120 121  ?    ?   ?   D . n 
D 3 121 PRO 121 122  ?    ?   ?   D . n 
D 3 122 SER 122 123  ?    ?   ?   D . n 
D 3 123 ASP 123 124  ?    ?   ?   D . n 
D 3 124 GLU 124 125  ?    ?   ?   D . n 
D 3 125 GLN 125 126  ?    ?   ?   D . n 
D 3 126 LEU 126 127  ?    ?   ?   D . n 
D 3 127 LYS 127 128  ?    ?   ?   D . n 
D 3 128 SER 128 129  ?    ?   ?   D . n 
D 3 129 GLY 129 130  ?    ?   ?   D . n 
D 3 130 THR 130 131  ?    ?   ?   D . n 
D 3 131 ALA 131 132  ?    ?   ?   D . n 
D 3 132 SER 132 133  ?    ?   ?   D . n 
D 3 133 VAL 133 134  ?    ?   ?   D . n 
D 3 134 VAL 134 135  ?    ?   ?   D . n 
D 3 135 CYS 135 136  ?    ?   ?   D . n 
D 3 136 LEU 136 137  ?    ?   ?   D . n 
D 3 137 LEU 137 138  ?    ?   ?   D . n 
D 3 138 ASN 138 139  ?    ?   ?   D . n 
D 3 139 ASN 139 140  ?    ?   ?   D . n 
D 3 140 PHE 140 141  ?    ?   ?   D . n 
D 3 141 TYR 141 142  ?    ?   ?   D . n 
D 3 142 PRO 142 143  ?    ?   ?   D . n 
D 3 143 ARG 143 144  ?    ?   ?   D . n 
D 3 144 GLU 144 145  ?    ?   ?   D . n 
D 3 145 ALA 145 146  ?    ?   ?   D . n 
D 3 146 LYS 146 147  ?    ?   ?   D . n 
D 3 147 VAL 147 148  ?    ?   ?   D . n 
D 3 148 GLN 148 149  ?    ?   ?   D . n 
D 3 149 TRP 149 150  ?    ?   ?   D . n 
D 3 150 LYS 150 151  ?    ?   ?   D . n 
D 3 151 VAL 151 152  ?    ?   ?   D . n 
D 3 152 ASP 152 153  ?    ?   ?   D . n 
D 3 153 ASN 153 154  ?    ?   ?   D . n 
D 3 154 ALA 154 155  ?    ?   ?   D . n 
D 3 155 LEU 155 156  ?    ?   ?   D . n 
D 3 156 GLN 156 157  ?    ?   ?   D . n 
D 3 157 SER 157 158  ?    ?   ?   D . n 
D 3 158 GLY 158 159  ?    ?   ?   D . n 
D 3 159 ASN 159 160  ?    ?   ?   D . n 
D 3 160 SER 160 161  ?    ?   ?   D . n 
D 3 161 GLN 161 162  ?    ?   ?   D . n 
D 3 162 GLU 162 163  ?    ?   ?   D . n 
D 3 163 SER 163 164  ?    ?   ?   D . n 
D 3 164 VAL 164 165  ?    ?   ?   D . n 
D 3 165 THR 165 166  ?    ?   ?   D . n 
D 3 166 GLU 166 167  ?    ?   ?   D . n 
D 3 167 GLN 167 168  ?    ?   ?   D . n 
D 3 168 ASP 168 169  ?    ?   ?   D . n 
D 3 169 SER 169 170  ?    ?   ?   D . n 
D 3 170 LYS 170 171  ?    ?   ?   D . n 
D 3 171 ASP 171 172  ?    ?   ?   D . n 
D 3 172 SER 172 173  ?    ?   ?   D . n 
D 3 173 THR 173 174  ?    ?   ?   D . n 
D 3 174 TYR 174 175  ?    ?   ?   D . n 
D 3 175 SER 175 176  ?    ?   ?   D . n 
D 3 176 LEU 176 177  ?    ?   ?   D . n 
D 3 177 SER 177 178  ?    ?   ?   D . n 
D 3 178 SER 178 179  ?    ?   ?   D . n 
D 3 179 THR 179 180  ?    ?   ?   D . n 
D 3 180 LEU 180 181  ?    ?   ?   D . n 
D 3 181 THR 181 182  ?    ?   ?   D . n 
D 3 182 LEU 182 183  ?    ?   ?   D . n 
D 3 183 SER 183 184  ?    ?   ?   D . n 
D 3 184 LYS 184 185  ?    ?   ?   D . n 
D 3 185 ALA 185 186  ?    ?   ?   D . n 
D 3 186 ASP 186 187  ?    ?   ?   D . n 
D 3 187 TYR 187 188  ?    ?   ?   D . n 
D 3 188 GLU 188 189  ?    ?   ?   D . n 
D 3 189 LYS 189 190  ?    ?   ?   D . n 
D 3 190 HIS 190 191  ?    ?   ?   D . n 
D 3 191 LYS 191 192  ?    ?   ?   D . n 
D 3 192 VAL 192 193  ?    ?   ?   D . n 
D 3 193 TYR 193 194  ?    ?   ?   D . n 
D 3 194 ALA 194 195  ?    ?   ?   D . n 
D 3 195 CYS 195 196  ?    ?   ?   D . n 
D 3 196 GLU 196 197  ?    ?   ?   D . n 
D 3 197 VAL 197 198  ?    ?   ?   D . n 
D 3 198 THR 198 199  ?    ?   ?   D . n 
D 3 199 HIS 199 200  ?    ?   ?   D . n 
D 3 200 GLN 200 201  ?    ?   ?   D . n 
D 3 201 GLY 201 202  ?    ?   ?   D . n 
D 3 202 LEU 202 203  ?    ?   ?   D . n 
D 3 203 SER 203 204  ?    ?   ?   D . n 
D 3 204 SER 204 205  ?    ?   ?   D . n 
D 3 205 PRO 205 206  ?    ?   ?   D . n 
D 3 206 VAL 206 207  ?    ?   ?   D . n 
D 3 207 THR 207 208  ?    ?   ?   D . n 
D 3 208 LYS 208 209  ?    ?   ?   D . n 
D 3 209 SER 209 210  ?    ?   ?   D . n 
D 3 210 PHE 210 211  ?    ?   ?   D . n 
D 3 211 ASN 211 212  ?    ?   ?   D . n 
D 3 212 ARG 212 213  ?    ?   ?   D . n 
D 3 213 GLY 213 214  ?    ?   ?   D . n 
D 3 214 GLU 214 215  ?    ?   ?   D . n 
D 3 215 CYS 215 216  ?    ?   ?   D . n 
# 
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 D LYS 43 ? CG ? D LYS 42 CG 
2 1 Y 1 D LYS 43 ? CD ? D LYS 42 CD 
3 1 Y 1 D LYS 43 ? CE ? D LYS 42 CE 
4 1 Y 1 D LYS 43 ? NZ ? D LYS 42 NZ 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EAJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9EAJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9EAJ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9EAJ 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.004  ? 5375 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.504  ? 7302 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 12.003 ? 1877 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.039  ? 826  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 898  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9EAJ 
_struct.title                        'Structure of nanobody AT206 in complex with the angiotensin II type I receptor (AT1R)' 
_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        9EAJ 
_struct_keywords.text            'GPCR, AT1R, nanobody, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9EAJ        9EAJ   ? 1 ? 1   
2 UNP AGTR1_HUMAN P30556 ? 1 
;ILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTL
PLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASL
PAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAY
;
2   
3 UNP C562_ECOLX  P0ABE7 ? 1 
;DLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANE
GKVKEAQAAAEQLKTTRNAYHQKYR
;
24  
4 UNP AGTR1_HUMAN P30556 ? 1 
;NDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFL
QLLKY
;
235 
5 PDB 9EAJ        9EAJ   ? 2 ? 1   
6 PDB 9EAJ        9EAJ   ? 3 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 9EAJ A 1   ? 121 ? 9EAJ   -135 ? -15 ? -135 -15  
2  2 9EAJ A 138 ? 362 ? P30556 2    ? 226 ? 2    226  
3  3 9EAJ A 363 ? 467 ? P0ABE7 24   ? 128 ? 227  331  
4  4 9EAJ A 478 ? 562 ? P30556 235  ? 319 ? 1235 1319 
5  1 9EAJ B 1   ? 121 ? 9EAJ   1    ? 121 ? 1    121  
6  2 9EAJ B 138 ? 362 ? P30556 2    ? 226 ? 138  362  
7  3 9EAJ B 363 ? 467 ? P0ABE7 24   ? 128 ? 363  467  
8  4 9EAJ B 478 ? 562 ? P30556 235  ? 319 ? 478  562  
9  5 9EAJ C 1   ? 231 ? 9EAJ   1    ? 231 ? 1    231  
10 6 9EAJ D 1   ? 215 ? 9EAJ   2    ? 216 ? 2    216  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9EAJ GLY A 122 ? PDB ?      ?   ?   linker                -14  1   
1 9EAJ GLY A 123 ? PDB ?      ?   ?   linker                -13  2   
1 9EAJ SER A 124 ? PDB ?      ?   ?   linker                -12  3   
1 9EAJ GLY A 125 ? PDB ?      ?   ?   linker                -11  4   
1 9EAJ GLU A 126 ? PDB ?      ?   ?   linker                -10  5   
1 9EAJ ASP A 127 ? PDB ?      ?   ?   linker                -9   6   
1 9EAJ GLN A 128 ? PDB ?      ?   ?   linker                -8   7   
1 9EAJ VAL A 129 ? PDB ?      ?   ?   linker                -7   8   
1 9EAJ ASP A 130 ? PDB ?      ?   ?   linker                -6   9   
1 9EAJ PRO A 131 ? PDB ?      ?   ?   linker                -5   10  
1 9EAJ ARG A 132 ? PDB ?      ?   ?   linker                -4   11  
1 9EAJ LEU A 133 ? PDB ?      ?   ?   linker                -3   12  
1 9EAJ ILE A 134 ? PDB ?      ?   ?   linker                -2   13  
1 9EAJ ASP A 135 ? PDB ?      ?   ?   linker                -1   14  
1 9EAJ GLY A 136 ? PDB ?      ?   ?   linker                0    15  
1 9EAJ LYS A 137 ? PDB ?      ?   ?   linker                1    16  
3 9EAJ TRP A 368 ? UNP P0ABE7 MET 29  'engineered mutation' 232  17  
3 9EAJ ILE A 463 ? UNP P0ABE7 HIS 124 'engineered mutation' 327  18  
3 9EAJ LEU A 467 ? UNP P0ABE7 ARG 128 'engineered mutation' 331  19  
3 9EAJ GLU A 468 ? UNP P0ABE7 ?   ?   linker                332  20  
3 9EAJ ARG A 469 ? UNP P0ABE7 ?   ?   linker                333  21  
3 9EAJ ALA A 470 ? UNP P0ABE7 ?   ?   linker                334  22  
3 9EAJ ARG A 471 ? UNP P0ABE7 ?   ?   linker                335  23  
3 9EAJ SER A 472 ? UNP P0ABE7 ?   ?   linker                336  24  
3 9EAJ THR A 473 ? UNP P0ABE7 ?   ?   linker                337  25  
3 9EAJ LEU A 474 ? UNP P0ABE7 ?   ?   linker                338  26  
3 9EAJ ASP A 475 ? UNP P0ABE7 ?   ?   linker                339  27  
3 9EAJ LYS A 476 ? UNP P0ABE7 ?   ?   linker                340  28  
3 9EAJ LEU A 477 ? UNP P0ABE7 ?   ?   linker                341  29  
4 9EAJ GLY A 563 ? UNP P30556 ?   ?   'expression tag'      1320 30  
4 9EAJ GLY A 564 ? UNP P30556 ?   ?   'expression tag'      1321 31  
4 9EAJ SER A 565 ? UNP P30556 ?   ?   'expression tag'      1322 32  
4 9EAJ SER A 566 ? UNP P30556 ?   ?   'expression tag'      1323 33  
4 9EAJ LEU A 567 ? UNP P30556 ?   ?   'expression tag'      1324 34  
4 9EAJ GLU A 568 ? UNP P30556 ?   ?   'expression tag'      1325 35  
4 9EAJ VAL A 569 ? UNP P30556 ?   ?   'expression tag'      1326 36  
4 9EAJ LEU A 570 ? UNP P30556 ?   ?   'expression tag'      1327 37  
4 9EAJ PHE A 571 ? UNP P30556 ?   ?   'expression tag'      1328 38  
4 9EAJ GLN A 572 ? UNP P30556 ?   ?   'expression tag'      1329 39  
4 9EAJ GLY A 573 ? UNP P30556 ?   ?   'expression tag'      1330 40  
4 9EAJ PRO A 574 ? UNP P30556 ?   ?   'expression tag'      1331 41  
4 9EAJ THR A 575 ? UNP P30556 ?   ?   'expression tag'      1332 42  
4 9EAJ GLU A 576 ? UNP P30556 ?   ?   'expression tag'      1333 43  
4 9EAJ THR A 577 ? UNP P30556 ?   ?   'expression tag'      1334 44  
4 9EAJ SER A 578 ? UNP P30556 ?   ?   'expression tag'      1335 45  
4 9EAJ GLN A 579 ? UNP P30556 ?   ?   'expression tag'      1336 46  
4 9EAJ VAL A 580 ? UNP P30556 ?   ?   'expression tag'      1337 47  
4 9EAJ ALA A 581 ? UNP P30556 ?   ?   'expression tag'      1338 48  
4 9EAJ PRO A 582 ? UNP P30556 ?   ?   'expression tag'      1339 49  
4 9EAJ ALA A 583 ? UNP P30556 ?   ?   'expression tag'      1340 50  
5 9EAJ GLY B 122 ? PDB ?      ?   ?   linker                122  51  
5 9EAJ GLY B 123 ? PDB ?      ?   ?   linker                123  52  
5 9EAJ SER B 124 ? PDB ?      ?   ?   linker                124  53  
5 9EAJ GLY B 125 ? PDB ?      ?   ?   linker                125  54  
5 9EAJ GLU B 126 ? PDB ?      ?   ?   linker                126  55  
5 9EAJ ASP B 127 ? PDB ?      ?   ?   linker                127  56  
5 9EAJ GLN B 128 ? PDB ?      ?   ?   linker                128  57  
5 9EAJ VAL B 129 ? PDB ?      ?   ?   linker                129  58  
5 9EAJ ASP B 130 ? PDB ?      ?   ?   linker                130  59  
5 9EAJ PRO B 131 ? PDB ?      ?   ?   linker                131  60  
5 9EAJ ARG B 132 ? PDB ?      ?   ?   linker                132  61  
5 9EAJ LEU B 133 ? PDB ?      ?   ?   linker                133  62  
5 9EAJ ILE B 134 ? PDB ?      ?   ?   linker                134  63  
5 9EAJ ASP B 135 ? PDB ?      ?   ?   linker                135  64  
5 9EAJ GLY B 136 ? PDB ?      ?   ?   linker                136  65  
5 9EAJ LYS B 137 ? PDB ?      ?   ?   linker                137  66  
7 9EAJ TRP B 368 ? UNP P0ABE7 MET 29  conflict              368  67  
7 9EAJ ILE B 463 ? UNP P0ABE7 HIS 124 conflict              463  68  
7 9EAJ LEU B 467 ? UNP P0ABE7 ARG 128 conflict              467  69  
7 9EAJ GLU B 468 ? UNP P0ABE7 ?   ?   linker                468  70  
7 9EAJ ARG B 469 ? UNP P0ABE7 ?   ?   linker                469  71  
7 9EAJ ALA B 470 ? UNP P0ABE7 ?   ?   linker                470  72  
7 9EAJ ARG B 471 ? UNP P0ABE7 ?   ?   linker                471  73  
7 9EAJ SER B 472 ? UNP P0ABE7 ?   ?   linker                472  74  
7 9EAJ THR B 473 ? UNP P0ABE7 ?   ?   linker                473  75  
7 9EAJ LEU B 474 ? UNP P0ABE7 ?   ?   linker                474  76  
7 9EAJ ASP B 475 ? UNP P0ABE7 ?   ?   linker                475  77  
7 9EAJ LYS B 476 ? UNP P0ABE7 ?   ?   linker                476  78  
7 9EAJ LEU B 477 ? UNP P0ABE7 ?   ?   linker                477  79  
8 9EAJ GLY B 563 ? UNP P30556 ?   ?   'expression tag'      563  80  
8 9EAJ GLY B 564 ? UNP P30556 ?   ?   'expression tag'      564  81  
8 9EAJ SER B 565 ? UNP P30556 ?   ?   'expression tag'      565  82  
8 9EAJ SER B 566 ? UNP P30556 ?   ?   'expression tag'      566  83  
8 9EAJ LEU B 567 ? UNP P30556 ?   ?   'expression tag'      567  84  
8 9EAJ GLU B 568 ? UNP P30556 ?   ?   'expression tag'      568  85  
8 9EAJ VAL B 569 ? UNP P30556 ?   ?   'expression tag'      569  86  
8 9EAJ LEU B 570 ? UNP P30556 ?   ?   'expression tag'      570  87  
8 9EAJ PHE B 571 ? UNP P30556 ?   ?   'expression tag'      571  88  
8 9EAJ GLN B 572 ? UNP P30556 ?   ?   'expression tag'      572  89  
8 9EAJ GLY B 573 ? UNP P30556 ?   ?   'expression tag'      573  90  
8 9EAJ PRO B 574 ? UNP P30556 ?   ?   'expression tag'      574  91  
8 9EAJ THR B 575 ? UNP P30556 ?   ?   'expression tag'      575  92  
8 9EAJ GLU B 576 ? UNP P30556 ?   ?   'expression tag'      576  93  
8 9EAJ THR B 577 ? UNP P30556 ?   ?   'expression tag'      577  94  
8 9EAJ SER B 578 ? UNP P30556 ?   ?   'expression tag'      578  95  
8 9EAJ GLN B 579 ? UNP P30556 ?   ?   'expression tag'      579  96  
8 9EAJ VAL B 580 ? UNP P30556 ?   ?   'expression tag'      580  97  
8 9EAJ ALA B 581 ? UNP P30556 ?   ?   'expression tag'      581  98  
8 9EAJ PRO B 582 ? UNP P30556 ?   ?   'expression tag'      582  99  
8 9EAJ ALA B 583 ? UNP P30556 ?   ?   'expression tag'      583  100 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 MET A 166 ? ILE A 189 ? MET A 30   ILE A 53   1 ? 24 
HELX_P HELX_P2  AA2 THR A 197 ? MET A 226 ? THR A 61   MET A 90   1 ? 30 
HELX_P HELX_P3  AA3 GLY A 233 ? HIS A 268 ? GLY A 97   HIS A 132  1 ? 36 
HELX_P HELX_P4  AA4 MET A 278 ? SER A 296 ? MET A 142  SER A 160  1 ? 19 
HELX_P HELX_P5  AA5 SER A 296 ? HIS A 302 ? SER A 160  HIS A 166  1 ? 7  
HELX_P HELX_P6  AA6 THR A 326 ? LEU A 338 ? THR A 190  LEU A 202  1 ? 13 
HELX_P HELX_P7  AA7 PHE A 340 ? LYS A 380 ? PHE A 204  LYS A 244  1 ? 41 
HELX_P HELX_P8  AA8 ASN A 383 ? ALA A 404 ? ASN A 247  ALA A 268  1 ? 22 
HELX_P HELX_P9  AA9 GLU A 418 ? GLU A 442 ? GLU A 282  GLU A 306  1 ? 25 
HELX_P HELX_P10 AB1 LYS A 444 ? ILE A 463 ? LYS A 308  ILE A 327  1 ? 20 
HELX_P HELX_P11 AB2 ILE A 463 ? ASP A 479 ? ILE A 327  ASP A 1236 1 ? 17 
HELX_P HELX_P12 AB3 ASP A 479 ? LEU A 511 ? ASP A 1236 LEU A 1268 1 ? 33 
HELX_P HELX_P13 AB4 ASP A 521 ? ALA A 526 ? ASP A 1278 ALA A 1283 1 ? 6  
HELX_P HELX_P14 AB5 ALA A 526 ? TYR A 535 ? ALA A 1283 TYR A 1292 1 ? 10 
HELX_P HELX_P15 AB6 PHE A 536 ? GLY A 549 ? PHE A 1293 GLY A 1306 1 ? 14 
HELX_P HELX_P16 AB7 ASN C 31  ? ASP C 34  ? ASN C 31   ASP C 34   5 ? 4  
HELX_P HELX_P17 AB8 GLY C 107 ? LYS C 112 ? GLY C 107  LYS C 112  1 ? 6  
HELX_P HELX_P18 AB9 TYR D 93  ? VAL D 97  ? TYR D 94   VAL D 98   5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 237 SG ? ? ? 1_555 A CYS 316 SG ? ? A CYS 101 A CYS 180 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
disulf2 disulf ? ? C CYS 25  SG ? ? ? 1_555 C CYS 99  SG ? ? C CYS 25  C CYS 99  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? D CYS 23  SG ? ? ? 1_555 D CYS 88  SG ? ? D CYS 24  D CYS 89  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 237 ? CYS A 316 ? CYS A 101 ? 1_555 CYS A 180 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS C 25  ? CYS C 99  ? CYS C 25  ? 1_555 CYS C 99  ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS D 23  ? CYS D 88  ? CYS D 24  ? 1_555 CYS D 89  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TRP 
_struct_mon_prot_cis.label_seq_id           105 
_struct_mon_prot_cis.label_asym_id          C 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TRP 
_struct_mon_prot_cis.auth_seq_id            105 
_struct_mon_prot_cis.auth_asym_id           C 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    106 
_struct_mon_prot_cis.pdbx_label_asym_id_2   C 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     106 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    C 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.25 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 5 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? 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 ARG A 303 ? PHE A 307 ? ARG A 167 PHE A 171 
AA1 2 THR A 314 ? HIS A 319 ? THR A 178 HIS A 183 
AA1 3 TYR B 108 ? VAL B 109 ? TYR B 108 VAL B 109 
AA2 1 GLU B 45  ? ILE B 50  ? GLU B 45  ILE B 50  
AA2 2 MET B 33  ? ARG B 37  ? MET B 33  ARG B 37  
AA2 3 TYR B 93  ? CYS B 94  ? TYR B 93  CYS B 94  
AA3 1 GLN C 6   ? SER C 10  ? GLN C 6   SER C 10  
AA3 2 LEU C 21  ? SER C 28  ? LEU C 21  SER C 28  
AA3 3 THR C 81  ? MET C 86  ? THR C 81  MET C 86  
AA3 4 PHE C 71  ? ASP C 76  ? PHE C 71  ASP C 76  
AA4 1 THR C 61  ? TYR C 63  ? THR C 61  TYR C 63  
AA4 2 LEU C 48  ? SER C 55  ? LEU C 48  SER C 55  
AA4 3 SER C 36  ? GLN C 42  ? SER C 36  GLN C 42  
AA4 4 ALA C 95  ? TRP C 102 ? ALA C 95  TRP C 102 
AA4 5 THR C 121 ? VAL C 123 ? THR C 121 VAL C 123 
AA5 1 MET D 4   ? GLN D 6   ? MET D 5   GLN D 7   
AA5 2 VAL D 19  ? ALA D 25  ? VAL D 20  ALA D 26  
AA5 3 ASP D 70  ? ILE D 75  ? ASP D 71  ILE D 76  
AA5 4 PHE D 62  ? SER D 67  ? PHE D 63  SER D 68  
AA6 1 SER D 10  ? ALA D 13  ? SER D 11  ALA D 14  
AA6 2 THR D 103 ? ILE D 107 ? THR D 104 ILE D 108 
AA6 3 THR D 85  ? GLN D 90  ? THR D 86  GLN D 91  
AA6 4 VAL D 33  ? GLN D 38  ? VAL D 34  GLN D 39  
AA6 5 LYS D 45  ? ILE D 48  ? LYS D 46  ILE D 49  
AA7 1 SER D 10  ? ALA D 13  ? SER D 11  ALA D 14  
AA7 2 THR D 103 ? ILE D 107 ? THR D 104 ILE D 108 
AA7 3 THR D 85  ? GLN D 90  ? THR D 86  GLN D 91  
AA7 4 THR D 98  ? PHE D 99  ? THR D 99  PHE D 100 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASN A 304 ? N ASN A 168 O ALA A 317 ? O ALA A 181 
AA1 2 3 N PHE A 318 ? N PHE A 182 O VAL B 109 ? O VAL B 109 
AA2 1 2 O GLU B 45  ? O GLU B 45  N ARG B 37  ? N ARG B 37  
AA2 2 3 N TYR B 36  ? N TYR B 36  O TYR B 93  ? O TYR B 93  
AA3 1 2 N GLN C 6   ? N GLN C 6   O SER C 28  ? O SER C 28  
AA3 2 3 N LEU C 23  ? N LEU C 23  O LEU C 84  ? O LEU C 84  
AA3 3 4 O TYR C 83  ? O TYR C 83  N SER C 74  ? N SER C 74  
AA4 1 2 O SER C 62  ? O SER C 62  N TYR C 53  ? N TYR C 53  
AA4 2 3 O GLU C 49  ? O GLU C 49  N ARG C 41  ? N ARG C 41  
AA4 3 4 N SER C 36  ? N SER C 36  O TRP C 102 ? O TRP C 102 
AA4 4 5 N TYR C 97  ? N TYR C 97  O THR C 121 ? O THR C 121 
AA5 1 2 N THR D 5   ? N THR D 6   O ARG D 24  ? O ARG D 25  
AA5 2 3 N CYS D 23  ? N CYS D 24  O PHE D 71  ? O PHE D 72  
AA5 3 4 O THR D 74  ? O THR D 75  N SER D 63  ? N SER D 64  
AA6 1 2 N ALA D 13  ? N ALA D 14  O GLU D 106 ? O GLU D 107 
AA6 2 3 O THR D 103 ? O THR D 104 N TYR D 86  ? N TYR D 87  
AA6 3 4 O THR D 85  ? O THR D 86  N GLN D 38  ? N GLN D 39  
AA6 4 5 N TRP D 35  ? N TRP D 36  O LEU D 47  ? O LEU D 48  
AA7 1 2 N ALA D 13  ? N ALA D 14  O GLU D 106 ? O GLU D 107 
AA7 2 3 O THR D 103 ? O THR D 104 N TYR D 86  ? N TYR D 87  
AA7 3 4 N GLN D 90  ? N GLN D 91  O THR D 98  ? O THR D 99  
# 
_pdbx_entry_details.entry_id                   9EAJ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 D GLN 91 ? ? OG1 D THR 99 ? ? 2.14 
2 1 O   D TYR 50 ? ? OH  D TYR 92 ? ? 2.16 
# 
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 MET A 90  ? ? -94.46  32.21   
2  1 GLU A 173 ? ? 57.86   -151.38 
3  1 ASN A 188 ? ? -99.03  37.01   
4  1 ILE A 201 ? ? -103.38 -63.86  
5  1 PHE A 204 ? ? -130.31 -36.10  
6  1 VAL B 47  ? ? -123.01 -63.36  
7  1 ALA B 59  ? ? -79.43  -165.62 
8  1 ASP B 60  ? ? -69.50  6.57    
9  1 TRP B 111 ? ? 49.64   -144.50 
10 1 SER D 31  ? ? 60.16   -149.14 
11 1 PRO D 81  ? ? -64.98  1.57    
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9EAJ 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9EAJ 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.2 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               120432 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Nanobody AT206 in complex with the angiotensin II type I receptor (AT1R)' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_imaging.entry_id                        9EAJ 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             1800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9EAJ 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9EAJ 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLN -135 ? A GLN 1   
2   1 Y 1 A VAL -134 ? A VAL 2   
3   1 Y 1 A GLN -133 ? A GLN 3   
4   1 Y 1 A LEU -132 ? A LEU 4   
5   1 Y 1 A GLN -131 ? A GLN 5   
6   1 Y 1 A GLU -130 ? A GLU 6   
7   1 Y 1 A SER -129 ? A SER 7   
8   1 Y 1 A GLY -128 ? A GLY 8   
9   1 Y 1 A GLY -127 ? A GLY 9   
10  1 Y 1 A GLY -126 ? A GLY 10  
11  1 Y 1 A LEU -125 ? A LEU 11  
12  1 Y 1 A VAL -124 ? A VAL 12  
13  1 Y 1 A GLN -123 ? A GLN 13  
14  1 Y 1 A ALA -122 ? A ALA 14  
15  1 Y 1 A GLY -121 ? A GLY 15  
16  1 Y 1 A GLY -120 ? A GLY 16  
17  1 Y 1 A SER -119 ? A SER 17  
18  1 Y 1 A LEU -118 ? A LEU 18  
19  1 Y 1 A ARG -117 ? A ARG 19  
20  1 Y 1 A LEU -116 ? A LEU 20  
21  1 Y 1 A SER -115 ? A SER 21  
22  1 Y 1 A CYS -114 ? A CYS 22  
23  1 Y 1 A ALA -113 ? A ALA 23  
24  1 Y 1 A ALA -112 ? A ALA 24  
25  1 Y 1 A SER -111 ? A SER 25  
26  1 Y 1 A GLY -110 ? A GLY 26  
27  1 Y 1 A SER -109 ? A SER 27  
28  1 Y 1 A ILE -108 ? A ILE 28  
29  1 Y 1 A SER -107 ? A SER 29  
30  1 Y 1 A TYR -106 ? A TYR 30  
31  1 Y 1 A TYR -105 ? A TYR 31  
32  1 Y 1 A ARG -104 ? A ARG 32  
33  1 Y 1 A MET -103 ? A MET 33  
34  1 Y 1 A GLY -102 ? A GLY 34  
35  1 Y 1 A TRP -101 ? A TRP 35  
36  1 Y 1 A TYR -100 ? A TYR 36  
37  1 Y 1 A ARG -99  ? A ARG 37  
38  1 Y 1 A GLN -98  ? A GLN 38  
39  1 Y 1 A ALA -97  ? A ALA 39  
40  1 Y 1 A PRO -96  ? A PRO 40  
41  1 Y 1 A GLY -95  ? A GLY 41  
42  1 Y 1 A LYS -94  ? A LYS 42  
43  1 Y 1 A GLU -93  ? A GLU 43  
44  1 Y 1 A ARG -92  ? A ARG 44  
45  1 Y 1 A GLU -91  ? A GLU 45  
46  1 Y 1 A PHE -90  ? A PHE 46  
47  1 Y 1 A VAL -89  ? A VAL 47  
48  1 Y 1 A ALA -88  ? A ALA 48  
49  1 Y 1 A GLY -87  ? A GLY 49  
50  1 Y 1 A ILE -86  ? A ILE 50  
51  1 Y 1 A GLY -85  ? A GLY 51  
52  1 Y 1 A VAL -84  ? A VAL 52  
53  1 Y 1 A GLY -83  ? A GLY 53  
54  1 Y 1 A THR -82  ? A THR 54  
55  1 Y 1 A THR -81  ? A THR 55  
56  1 Y 1 A THR -80  ? A THR 56  
57  1 Y 1 A ASN -79  ? A ASN 57  
58  1 Y 1 A TYR -78  ? A TYR 58  
59  1 Y 1 A ALA -77  ? A ALA 59  
60  1 Y 1 A ASP -76  ? A ASP 60  
61  1 Y 1 A SER -75  ? A SER 61  
62  1 Y 1 A VAL -74  ? A VAL 62  
63  1 Y 1 A LYS -73  ? A LYS 63  
64  1 Y 1 A GLY -72  ? A GLY 64  
65  1 Y 1 A ARG -71  ? A ARG 65  
66  1 Y 1 A PHE -70  ? A PHE 66  
67  1 Y 1 A THR -69  ? A THR 67  
68  1 Y 1 A ILE -68  ? A ILE 68  
69  1 Y 1 A SER -67  ? A SER 69  
70  1 Y 1 A ARG -66  ? A ARG 70  
71  1 Y 1 A ASP -65  ? A ASP 71  
72  1 Y 1 A ASN -64  ? A ASN 72  
73  1 Y 1 A ALA -63  ? A ALA 73  
74  1 Y 1 A LYS -62  ? A LYS 74  
75  1 Y 1 A ASN -61  ? A ASN 75  
76  1 Y 1 A THR -60  ? A THR 76  
77  1 Y 1 A VAL -59  ? A VAL 77  
78  1 Y 1 A TYR -58  ? A TYR 78  
79  1 Y 1 A LEU -57  ? A LEU 79  
80  1 Y 1 A GLN -56  ? A GLN 80  
81  1 Y 1 A MET -55  ? A MET 81  
82  1 Y 1 A ASN -54  ? A ASN 82  
83  1 Y 1 A SER -53  ? A SER 83  
84  1 Y 1 A LEU -52  ? A LEU 84  
85  1 Y 1 A LYS -51  ? A LYS 85  
86  1 Y 1 A PRO -50  ? A PRO 86  
87  1 Y 1 A GLU -49  ? A GLU 87  
88  1 Y 1 A ASP -48  ? A ASP 88  
89  1 Y 1 A THR -47  ? A THR 89  
90  1 Y 1 A ALA -46  ? A ALA 90  
91  1 Y 1 A VAL -45  ? A VAL 91  
92  1 Y 1 A TYR -44  ? A TYR 92  
93  1 Y 1 A TYR -43  ? A TYR 93  
94  1 Y 1 A CYS -42  ? A CYS 94  
95  1 Y 1 A ALA -41  ? A ALA 95  
96  1 Y 1 A ALA -40  ? A ALA 96  
97  1 Y 1 A TYR -39  ? A TYR 97  
98  1 Y 1 A ASN -38  ? A ASN 98  
99  1 Y 1 A TYR -37  ? A TYR 99  
100 1 Y 1 A PHE -36  ? A PHE 100 
101 1 Y 1 A PRO -35  ? A PRO 101 
102 1 Y 1 A ARG -34  ? A ARG 102 
103 1 Y 1 A SER -33  ? A SER 103 
104 1 Y 1 A ILE -32  ? A ILE 104 
105 1 Y 1 A VAL -31  ? A VAL 105 
106 1 Y 1 A TYR -30  ? A TYR 106 
107 1 Y 1 A TYR -29  ? A TYR 107 
108 1 Y 1 A TYR -28  ? A TYR 108 
109 1 Y 1 A VAL -27  ? A VAL 109 
110 1 Y 1 A TYR -26  ? A TYR 110 
111 1 Y 1 A TRP -25  ? A TRP 111 
112 1 Y 1 A GLY -24  ? A GLY 112 
113 1 Y 1 A GLN -23  ? A GLN 113 
114 1 Y 1 A GLY -22  ? A GLY 114 
115 1 Y 1 A THR -21  ? A THR 115 
116 1 Y 1 A GLN -20  ? A GLN 116 
117 1 Y 1 A VAL -19  ? A VAL 117 
118 1 Y 1 A THR -18  ? A THR 118 
119 1 Y 1 A VAL -17  ? A VAL 119 
120 1 Y 1 A SER -16  ? A SER 120 
121 1 Y 1 A SER -15  ? A SER 121 
122 1 Y 1 A GLY -14  ? A GLY 122 
123 1 Y 1 A GLY -13  ? A GLY 123 
124 1 Y 1 A SER -12  ? A SER 124 
125 1 Y 1 A GLY -11  ? A GLY 125 
126 1 Y 1 A GLU -10  ? A GLU 126 
127 1 Y 1 A ASP -9   ? A ASP 127 
128 1 Y 1 A GLN -8   ? A GLN 128 
129 1 Y 1 A VAL -7   ? A VAL 129 
130 1 Y 1 A ASP -6   ? A ASP 130 
131 1 Y 1 A PRO -5   ? A PRO 131 
132 1 Y 1 A ARG -4   ? A ARG 132 
133 1 Y 1 A LEU -3   ? A LEU 133 
134 1 Y 1 A ILE -2   ? A ILE 134 
135 1 Y 1 A ASP -1   ? A ASP 135 
136 1 Y 1 A GLY 0    ? A GLY 136 
137 1 Y 1 A LYS 1    ? A LYS 137 
138 1 Y 1 A ILE 2    ? A ILE 138 
139 1 Y 1 A LEU 3    ? A LEU 139 
140 1 Y 1 A ASN 4    ? A ASN 140 
141 1 Y 1 A SER 5    ? A SER 141 
142 1 Y 1 A SER 6    ? A SER 142 
143 1 Y 1 A THR 7    ? A THR 143 
144 1 Y 1 A GLU 8    ? A GLU 144 
145 1 Y 1 A ASP 9    ? A ASP 145 
146 1 Y 1 A GLY 10   ? A GLY 146 
147 1 Y 1 A ILE 11   ? A ILE 147 
148 1 Y 1 A LYS 12   ? A LYS 148 
149 1 Y 1 A ARG 13   ? A ARG 149 
150 1 Y 1 A ILE 14   ? A ILE 150 
151 1 Y 1 A GLN 15   ? A GLN 151 
152 1 Y 1 A ASP 16   ? A ASP 152 
153 1 Y 1 A ASP 17   ? A ASP 153 
154 1 Y 1 A CYS 18   ? A CYS 154 
155 1 Y 1 A PRO 19   ? A PRO 155 
156 1 Y 1 A LYS 20   ? A LYS 156 
157 1 Y 1 A ALA 21   ? A ALA 157 
158 1 Y 1 A GLY 22   ? A GLY 158 
159 1 Y 1 A ARG 23   ? A ARG 159 
160 1 Y 1 A HIS 24   ? A HIS 160 
161 1 Y 1 A ASN 25   ? A ASN 161 
162 1 Y 1 A TYR 26   ? A TYR 162 
163 1 Y 1 A ILE 27   ? A ILE 163 
164 1 Y 1 A PHE 28   ? A PHE 164 
165 1 Y 1 A VAL 29   ? A VAL 165 
166 1 Y 1 A MET 134  ? A MET 270 
167 1 Y 1 A LYS 135  ? A LYS 271 
168 1 Y 1 A SER 136  ? A SER 272 
169 1 Y 1 A ARG 137  ? A ARG 273 
170 1 Y 1 A LEU 138  ? A LEU 274 
171 1 Y 1 A ARG 139  ? A ARG 275 
172 1 Y 1 A ARG 140  ? A ARG 276 
173 1 Y 1 A LEU 273  ? A LEU 409 
174 1 Y 1 A GLU 274  ? A GLU 410 
175 1 Y 1 A ASP 275  ? A ASP 411 
176 1 Y 1 A LYS 276  ? A LYS 412 
177 1 Y 1 A SER 277  ? A SER 413 
178 1 Y 1 A PRO 278  ? A PRO 414 
179 1 Y 1 A ASP 279  ? A ASP 415 
180 1 Y 1 A ARG 1272 ? A ARG 515 
181 1 Y 1 A ASP 1273 ? A ASP 516 
182 1 Y 1 A CYS 1274 ? A CYS 517 
183 1 Y 1 A ARG 1275 ? A ARG 518 
184 1 Y 1 A ILE 1276 ? A ILE 519 
185 1 Y 1 A LYS 1307 ? A LYS 550 
186 1 Y 1 A LYS 1308 ? A LYS 551 
187 1 Y 1 A PHE 1309 ? A PHE 552 
188 1 Y 1 A LYS 1310 ? A LYS 553 
189 1 Y 1 A ARG 1311 ? A ARG 554 
190 1 Y 1 A TYR 1312 ? A TYR 555 
191 1 Y 1 A PHE 1313 ? A PHE 556 
192 1 Y 1 A LEU 1314 ? A LEU 557 
193 1 Y 1 A GLN 1315 ? A GLN 558 
194 1 Y 1 A LEU 1316 ? A LEU 559 
195 1 Y 1 A LEU 1317 ? A LEU 560 
196 1 Y 1 A LYS 1318 ? A LYS 561 
197 1 Y 1 A TYR 1319 ? A TYR 562 
198 1 Y 1 A GLY 1320 ? A GLY 563 
199 1 Y 1 A GLY 1321 ? A GLY 564 
200 1 Y 1 A SER 1322 ? A SER 565 
201 1 Y 1 A SER 1323 ? A SER 566 
202 1 Y 1 A LEU 1324 ? A LEU 567 
203 1 Y 1 A GLU 1325 ? A GLU 568 
204 1 Y 1 A VAL 1326 ? A VAL 569 
205 1 Y 1 A LEU 1327 ? A LEU 570 
206 1 Y 1 A PHE 1328 ? A PHE 571 
207 1 Y 1 A GLN 1329 ? A GLN 572 
208 1 Y 1 A GLY 1330 ? A GLY 573 
209 1 Y 1 A PRO 1331 ? A PRO 574 
210 1 Y 1 A THR 1332 ? A THR 575 
211 1 Y 1 A GLU 1333 ? A GLU 576 
212 1 Y 1 A THR 1334 ? A THR 577 
213 1 Y 1 A SER 1335 ? A SER 578 
214 1 Y 1 A GLN 1336 ? A GLN 579 
215 1 Y 1 A VAL 1337 ? A VAL 580 
216 1 Y 1 A ALA 1338 ? A ALA 581 
217 1 Y 1 A PRO 1339 ? A PRO 582 
218 1 Y 1 A ALA 1340 ? A ALA 583 
219 1 Y 1 B GLN 1    ? B GLN 1   
220 1 Y 1 B VAL 2    ? B VAL 2   
221 1 Y 1 B GLN 3    ? B GLN 3   
222 1 Y 1 B LEU 4    ? B LEU 4   
223 1 Y 1 B GLN 5    ? B GLN 5   
224 1 Y 1 B GLU 6    ? B GLU 6   
225 1 Y 1 B SER 7    ? B SER 7   
226 1 Y 1 B GLY 8    ? B GLY 8   
227 1 Y 1 B GLY 9    ? B GLY 9   
228 1 Y 1 B GLY 10   ? B GLY 10  
229 1 Y 1 B LEU 11   ? B LEU 11  
230 1 Y 1 B VAL 12   ? B VAL 12  
231 1 Y 1 B GLN 13   ? B GLN 13  
232 1 Y 1 B ALA 14   ? B ALA 14  
233 1 Y 1 B GLY 15   ? B GLY 15  
234 1 Y 1 B GLY 16   ? B GLY 16  
235 1 Y 1 B SER 17   ? B SER 17  
236 1 Y 1 B LEU 18   ? B LEU 18  
237 1 Y 1 B ARG 19   ? B ARG 19  
238 1 Y 1 B LEU 20   ? B LEU 20  
239 1 Y 1 B SER 21   ? B SER 21  
240 1 Y 1 B CYS 22   ? B CYS 22  
241 1 Y 1 B ALA 23   ? B ALA 23  
242 1 Y 1 B ALA 24   ? B ALA 24  
243 1 Y 1 B SER 25   ? B SER 25  
244 1 Y 1 B GLY 26   ? B GLY 26  
245 1 Y 1 B SER 27   ? B SER 27  
246 1 Y 1 B ILE 28   ? B ILE 28  
247 1 Y 1 B PRO 40   ? B PRO 40  
248 1 Y 1 B GLY 41   ? B GLY 41  
249 1 Y 1 B LYS 42   ? B LYS 42  
250 1 Y 1 B VAL 52   ? B VAL 52  
251 1 Y 1 B GLY 53   ? B GLY 53  
252 1 Y 1 B THR 54   ? B THR 54  
253 1 Y 1 B THR 67   ? B THR 67  
254 1 Y 1 B ILE 68   ? B ILE 68  
255 1 Y 1 B SER 69   ? B SER 69  
256 1 Y 1 B ARG 70   ? B ARG 70  
257 1 Y 1 B ASP 71   ? B ASP 71  
258 1 Y 1 B ASN 72   ? B ASN 72  
259 1 Y 1 B ALA 73   ? B ALA 73  
260 1 Y 1 B LYS 74   ? B LYS 74  
261 1 Y 1 B ASN 75   ? B ASN 75  
262 1 Y 1 B THR 76   ? B THR 76  
263 1 Y 1 B VAL 77   ? B VAL 77  
264 1 Y 1 B TYR 78   ? B TYR 78  
265 1 Y 1 B PRO 86   ? B PRO 86  
266 1 Y 1 B GLU 87   ? B GLU 87  
267 1 Y 1 B ASP 88   ? B ASP 88  
268 1 Y 1 B THR 89   ? B THR 89  
269 1 Y 1 B ALA 90   ? B ALA 90  
270 1 Y 1 B THR 118  ? B THR 118 
271 1 Y 1 B VAL 119  ? B VAL 119 
272 1 Y 1 B SER 120  ? B SER 120 
273 1 Y 1 B SER 121  ? B SER 121 
274 1 Y 1 B GLY 122  ? B GLY 122 
275 1 Y 1 B GLY 123  ? B GLY 123 
276 1 Y 1 B SER 124  ? B SER 124 
277 1 Y 1 B GLY 125  ? B GLY 125 
278 1 Y 1 B GLU 126  ? B GLU 126 
279 1 Y 1 B ASP 127  ? B ASP 127 
280 1 Y 1 B GLN 128  ? B GLN 128 
281 1 Y 1 B VAL 129  ? B VAL 129 
282 1 Y 1 B ASP 130  ? B ASP 130 
283 1 Y 1 B PRO 131  ? B PRO 131 
284 1 Y 1 B ARG 132  ? B ARG 132 
285 1 Y 1 B LEU 133  ? B LEU 133 
286 1 Y 1 B ILE 134  ? B ILE 134 
287 1 Y 1 B ASP 135  ? B ASP 135 
288 1 Y 1 B GLY 136  ? B GLY 136 
289 1 Y 1 B LYS 137  ? B LYS 137 
290 1 Y 1 B ILE 138  ? B ILE 138 
291 1 Y 1 B LEU 139  ? B LEU 139 
292 1 Y 1 B ASN 140  ? B ASN 140 
293 1 Y 1 B SER 141  ? B SER 141 
294 1 Y 1 B SER 142  ? B SER 142 
295 1 Y 1 B THR 143  ? B THR 143 
296 1 Y 1 B GLU 144  ? B GLU 144 
297 1 Y 1 B ASP 145  ? B ASP 145 
298 1 Y 1 B GLY 146  ? B GLY 146 
299 1 Y 1 B ILE 147  ? B ILE 147 
300 1 Y 1 B LYS 148  ? B LYS 148 
301 1 Y 1 B ARG 149  ? B ARG 149 
302 1 Y 1 B ILE 150  ? B ILE 150 
303 1 Y 1 B GLN 151  ? B GLN 151 
304 1 Y 1 B ASP 152  ? B ASP 152 
305 1 Y 1 B ASP 153  ? B ASP 153 
306 1 Y 1 B CYS 154  ? B CYS 154 
307 1 Y 1 B PRO 155  ? B PRO 155 
308 1 Y 1 B LYS 156  ? B LYS 156 
309 1 Y 1 B ALA 157  ? B ALA 157 
310 1 Y 1 B GLY 158  ? B GLY 158 
311 1 Y 1 B ARG 159  ? B ARG 159 
312 1 Y 1 B HIS 160  ? B HIS 160 
313 1 Y 1 B ASN 161  ? B ASN 161 
314 1 Y 1 B TYR 162  ? B TYR 162 
315 1 Y 1 B ILE 163  ? B ILE 163 
316 1 Y 1 B PHE 164  ? B PHE 164 
317 1 Y 1 B VAL 165  ? B VAL 165 
318 1 Y 1 B MET 166  ? B MET 166 
319 1 Y 1 B ILE 167  ? B ILE 167 
320 1 Y 1 B PRO 168  ? B PRO 168 
321 1 Y 1 B THR 169  ? B THR 169 
322 1 Y 1 B LEU 170  ? B LEU 170 
323 1 Y 1 B TYR 171  ? B TYR 171 
324 1 Y 1 B SER 172  ? B SER 172 
325 1 Y 1 B ILE 173  ? B ILE 173 
326 1 Y 1 B ILE 174  ? B ILE 174 
327 1 Y 1 B PHE 175  ? B PHE 175 
328 1 Y 1 B VAL 176  ? B VAL 176 
329 1 Y 1 B VAL 177  ? B VAL 177 
330 1 Y 1 B GLY 178  ? B GLY 178 
331 1 Y 1 B ILE 179  ? B ILE 179 
332 1 Y 1 B PHE 180  ? B PHE 180 
333 1 Y 1 B GLY 181  ? B GLY 181 
334 1 Y 1 B ASN 182  ? B ASN 182 
335 1 Y 1 B SER 183  ? B SER 183 
336 1 Y 1 B LEU 184  ? B LEU 184 
337 1 Y 1 B VAL 185  ? B VAL 185 
338 1 Y 1 B VAL 186  ? B VAL 186 
339 1 Y 1 B ILE 187  ? B ILE 187 
340 1 Y 1 B VAL 188  ? B VAL 188 
341 1 Y 1 B ILE 189  ? B ILE 189 
342 1 Y 1 B TYR 190  ? B TYR 190 
343 1 Y 1 B PHE 191  ? B PHE 191 
344 1 Y 1 B TYR 192  ? B TYR 192 
345 1 Y 1 B MET 193  ? B MET 193 
346 1 Y 1 B LYS 194  ? B LYS 194 
347 1 Y 1 B LEU 195  ? B LEU 195 
348 1 Y 1 B LYS 196  ? B LYS 196 
349 1 Y 1 B THR 197  ? B THR 197 
350 1 Y 1 B VAL 198  ? B VAL 198 
351 1 Y 1 B ALA 199  ? B ALA 199 
352 1 Y 1 B SER 200  ? B SER 200 
353 1 Y 1 B VAL 201  ? B VAL 201 
354 1 Y 1 B PHE 202  ? B PHE 202 
355 1 Y 1 B LEU 203  ? B LEU 203 
356 1 Y 1 B LEU 204  ? B LEU 204 
357 1 Y 1 B ASN 205  ? B ASN 205 
358 1 Y 1 B LEU 206  ? B LEU 206 
359 1 Y 1 B ALA 207  ? B ALA 207 
360 1 Y 1 B LEU 208  ? B LEU 208 
361 1 Y 1 B ALA 209  ? B ALA 209 
362 1 Y 1 B ASP 210  ? B ASP 210 
363 1 Y 1 B LEU 211  ? B LEU 211 
364 1 Y 1 B CYS 212  ? B CYS 212 
365 1 Y 1 B PHE 213  ? B PHE 213 
366 1 Y 1 B LEU 214  ? B LEU 214 
367 1 Y 1 B LEU 215  ? B LEU 215 
368 1 Y 1 B THR 216  ? B THR 216 
369 1 Y 1 B LEU 217  ? B LEU 217 
370 1 Y 1 B PRO 218  ? B PRO 218 
371 1 Y 1 B LEU 219  ? B LEU 219 
372 1 Y 1 B TRP 220  ? B TRP 220 
373 1 Y 1 B ALA 221  ? B ALA 221 
374 1 Y 1 B VAL 222  ? B VAL 222 
375 1 Y 1 B TYR 223  ? B TYR 223 
376 1 Y 1 B THR 224  ? B THR 224 
377 1 Y 1 B ALA 225  ? B ALA 225 
378 1 Y 1 B MET 226  ? B MET 226 
379 1 Y 1 B GLU 227  ? B GLU 227 
380 1 Y 1 B TYR 228  ? B TYR 228 
381 1 Y 1 B ARG 229  ? B ARG 229 
382 1 Y 1 B TRP 230  ? B TRP 230 
383 1 Y 1 B PRO 231  ? B PRO 231 
384 1 Y 1 B PHE 232  ? B PHE 232 
385 1 Y 1 B GLY 233  ? B GLY 233 
386 1 Y 1 B ASN 234  ? B ASN 234 
387 1 Y 1 B TYR 235  ? B TYR 235 
388 1 Y 1 B LEU 236  ? B LEU 236 
389 1 Y 1 B CYS 237  ? B CYS 237 
390 1 Y 1 B LYS 238  ? B LYS 238 
391 1 Y 1 B ILE 239  ? B ILE 239 
392 1 Y 1 B ALA 240  ? B ALA 240 
393 1 Y 1 B SER 241  ? B SER 241 
394 1 Y 1 B ALA 242  ? B ALA 242 
395 1 Y 1 B SER 243  ? B SER 243 
396 1 Y 1 B VAL 244  ? B VAL 244 
397 1 Y 1 B SER 245  ? B SER 245 
398 1 Y 1 B PHE 246  ? B PHE 246 
399 1 Y 1 B ASN 247  ? B ASN 247 
400 1 Y 1 B LEU 248  ? B LEU 248 
401 1 Y 1 B TYR 249  ? B TYR 249 
402 1 Y 1 B ALA 250  ? B ALA 250 
403 1 Y 1 B SER 251  ? B SER 251 
404 1 Y 1 B VAL 252  ? B VAL 252 
405 1 Y 1 B PHE 253  ? B PHE 253 
406 1 Y 1 B LEU 254  ? B LEU 254 
407 1 Y 1 B LEU 255  ? B LEU 255 
408 1 Y 1 B THR 256  ? B THR 256 
409 1 Y 1 B CYS 257  ? B CYS 257 
410 1 Y 1 B LEU 258  ? B LEU 258 
411 1 Y 1 B SER 259  ? B SER 259 
412 1 Y 1 B ILE 260  ? B ILE 260 
413 1 Y 1 B ASP 261  ? B ASP 261 
414 1 Y 1 B ARG 262  ? B ARG 262 
415 1 Y 1 B TYR 263  ? B TYR 263 
416 1 Y 1 B LEU 264  ? B LEU 264 
417 1 Y 1 B ALA 265  ? B ALA 265 
418 1 Y 1 B ILE 266  ? B ILE 266 
419 1 Y 1 B VAL 267  ? B VAL 267 
420 1 Y 1 B HIS 268  ? B HIS 268 
421 1 Y 1 B PRO 269  ? B PRO 269 
422 1 Y 1 B MET 270  ? B MET 270 
423 1 Y 1 B LYS 271  ? B LYS 271 
424 1 Y 1 B SER 272  ? B SER 272 
425 1 Y 1 B ARG 273  ? B ARG 273 
426 1 Y 1 B LEU 274  ? B LEU 274 
427 1 Y 1 B ARG 275  ? B ARG 275 
428 1 Y 1 B ARG 276  ? B ARG 276 
429 1 Y 1 B THR 277  ? B THR 277 
430 1 Y 1 B MET 278  ? B MET 278 
431 1 Y 1 B LEU 279  ? B LEU 279 
432 1 Y 1 B VAL 280  ? B VAL 280 
433 1 Y 1 B ALA 281  ? B ALA 281 
434 1 Y 1 B LYS 282  ? B LYS 282 
435 1 Y 1 B VAL 283  ? B VAL 283 
436 1 Y 1 B THR 284  ? B THR 284 
437 1 Y 1 B CYS 285  ? B CYS 285 
438 1 Y 1 B ILE 286  ? B ILE 286 
439 1 Y 1 B ILE 287  ? B ILE 287 
440 1 Y 1 B ILE 288  ? B ILE 288 
441 1 Y 1 B TRP 289  ? B TRP 289 
442 1 Y 1 B LEU 290  ? B LEU 290 
443 1 Y 1 B LEU 291  ? B LEU 291 
444 1 Y 1 B ALA 292  ? B ALA 292 
445 1 Y 1 B GLY 293  ? B GLY 293 
446 1 Y 1 B LEU 294  ? B LEU 294 
447 1 Y 1 B ALA 295  ? B ALA 295 
448 1 Y 1 B SER 296  ? B SER 296 
449 1 Y 1 B LEU 297  ? B LEU 297 
450 1 Y 1 B PRO 298  ? B PRO 298 
451 1 Y 1 B ALA 299  ? B ALA 299 
452 1 Y 1 B ILE 300  ? B ILE 300 
453 1 Y 1 B ILE 301  ? B ILE 301 
454 1 Y 1 B HIS 302  ? B HIS 302 
455 1 Y 1 B ARG 303  ? B ARG 303 
456 1 Y 1 B ASN 304  ? B ASN 304 
457 1 Y 1 B VAL 305  ? B VAL 305 
458 1 Y 1 B PHE 306  ? B PHE 306 
459 1 Y 1 B PHE 307  ? B PHE 307 
460 1 Y 1 B ILE 308  ? B ILE 308 
461 1 Y 1 B GLU 309  ? B GLU 309 
462 1 Y 1 B ASN 310  ? B ASN 310 
463 1 Y 1 B THR 311  ? B THR 311 
464 1 Y 1 B ASN 312  ? B ASN 312 
465 1 Y 1 B ILE 313  ? B ILE 313 
466 1 Y 1 B THR 314  ? B THR 314 
467 1 Y 1 B VAL 315  ? B VAL 315 
468 1 Y 1 B CYS 316  ? B CYS 316 
469 1 Y 1 B ALA 317  ? B ALA 317 
470 1 Y 1 B PHE 318  ? B PHE 318 
471 1 Y 1 B HIS 319  ? B HIS 319 
472 1 Y 1 B TYR 320  ? B TYR 320 
473 1 Y 1 B GLU 321  ? B GLU 321 
474 1 Y 1 B SER 322  ? B SER 322 
475 1 Y 1 B GLN 323  ? B GLN 323 
476 1 Y 1 B ASN 324  ? B ASN 324 
477 1 Y 1 B SER 325  ? B SER 325 
478 1 Y 1 B THR 326  ? B THR 326 
479 1 Y 1 B LEU 327  ? B LEU 327 
480 1 Y 1 B PRO 328  ? B PRO 328 
481 1 Y 1 B ILE 329  ? B ILE 329 
482 1 Y 1 B GLY 330  ? B GLY 330 
483 1 Y 1 B LEU 331  ? B LEU 331 
484 1 Y 1 B GLY 332  ? B GLY 332 
485 1 Y 1 B LEU 333  ? B LEU 333 
486 1 Y 1 B THR 334  ? B THR 334 
487 1 Y 1 B LYS 335  ? B LYS 335 
488 1 Y 1 B ASN 336  ? B ASN 336 
489 1 Y 1 B ILE 337  ? B ILE 337 
490 1 Y 1 B LEU 338  ? B LEU 338 
491 1 Y 1 B GLY 339  ? B GLY 339 
492 1 Y 1 B PHE 340  ? B PHE 340 
493 1 Y 1 B LEU 341  ? B LEU 341 
494 1 Y 1 B PHE 342  ? B PHE 342 
495 1 Y 1 B PRO 343  ? B PRO 343 
496 1 Y 1 B PHE 344  ? B PHE 344 
497 1 Y 1 B LEU 345  ? B LEU 345 
498 1 Y 1 B ILE 346  ? B ILE 346 
499 1 Y 1 B ILE 347  ? B ILE 347 
500 1 Y 1 B LEU 348  ? B LEU 348 
501 1 Y 1 B THR 349  ? B THR 349 
502 1 Y 1 B SER 350  ? B SER 350 
503 1 Y 1 B TYR 351  ? B TYR 351 
504 1 Y 1 B THR 352  ? B THR 352 
505 1 Y 1 B LEU 353  ? B LEU 353 
506 1 Y 1 B ILE 354  ? B ILE 354 
507 1 Y 1 B TRP 355  ? B TRP 355 
508 1 Y 1 B LYS 356  ? B LYS 356 
509 1 Y 1 B ALA 357  ? B ALA 357 
510 1 Y 1 B LEU 358  ? B LEU 358 
511 1 Y 1 B LYS 359  ? B LYS 359 
512 1 Y 1 B LYS 360  ? B LYS 360 
513 1 Y 1 B ALA 361  ? B ALA 361 
514 1 Y 1 B TYR 362  ? B TYR 362 
515 1 Y 1 B ASP 363  ? B ASP 363 
516 1 Y 1 B LEU 364  ? B LEU 364 
517 1 Y 1 B GLU 365  ? B GLU 365 
518 1 Y 1 B ASP 366  ? B ASP 366 
519 1 Y 1 B ASN 367  ? B ASN 367 
520 1 Y 1 B TRP 368  ? B TRP 368 
521 1 Y 1 B GLU 369  ? B GLU 369 
522 1 Y 1 B THR 370  ? B THR 370 
523 1 Y 1 B LEU 371  ? B LEU 371 
524 1 Y 1 B ASN 372  ? B ASN 372 
525 1 Y 1 B ASP 373  ? B ASP 373 
526 1 Y 1 B ASN 374  ? B ASN 374 
527 1 Y 1 B LEU 375  ? B LEU 375 
528 1 Y 1 B LYS 376  ? B LYS 376 
529 1 Y 1 B VAL 377  ? B VAL 377 
530 1 Y 1 B ILE 378  ? B ILE 378 
531 1 Y 1 B GLU 379  ? B GLU 379 
532 1 Y 1 B LYS 380  ? B LYS 380 
533 1 Y 1 B ALA 381  ? B ALA 381 
534 1 Y 1 B ASP 382  ? B ASP 382 
535 1 Y 1 B ASN 383  ? B ASN 383 
536 1 Y 1 B ALA 384  ? B ALA 384 
537 1 Y 1 B ALA 385  ? B ALA 385 
538 1 Y 1 B GLN 386  ? B GLN 386 
539 1 Y 1 B VAL 387  ? B VAL 387 
540 1 Y 1 B LYS 388  ? B LYS 388 
541 1 Y 1 B ASP 389  ? B ASP 389 
542 1 Y 1 B ALA 390  ? B ALA 390 
543 1 Y 1 B LEU 391  ? B LEU 391 
544 1 Y 1 B THR 392  ? B THR 392 
545 1 Y 1 B LYS 393  ? B LYS 393 
546 1 Y 1 B MET 394  ? B MET 394 
547 1 Y 1 B ARG 395  ? B ARG 395 
548 1 Y 1 B ALA 396  ? B ALA 396 
549 1 Y 1 B ALA 397  ? B ALA 397 
550 1 Y 1 B ALA 398  ? B ALA 398 
551 1 Y 1 B LEU 399  ? B LEU 399 
552 1 Y 1 B ASP 400  ? B ASP 400 
553 1 Y 1 B ALA 401  ? B ALA 401 
554 1 Y 1 B GLN 402  ? B GLN 402 
555 1 Y 1 B LYS 403  ? B LYS 403 
556 1 Y 1 B ALA 404  ? B ALA 404 
557 1 Y 1 B THR 405  ? B THR 405 
558 1 Y 1 B PRO 406  ? B PRO 406 
559 1 Y 1 B PRO 407  ? B PRO 407 
560 1 Y 1 B LYS 408  ? B LYS 408 
561 1 Y 1 B LEU 409  ? B LEU 409 
562 1 Y 1 B GLU 410  ? B GLU 410 
563 1 Y 1 B ASP 411  ? B ASP 411 
564 1 Y 1 B LYS 412  ? B LYS 412 
565 1 Y 1 B SER 413  ? B SER 413 
566 1 Y 1 B PRO 414  ? B PRO 414 
567 1 Y 1 B ASP 415  ? B ASP 415 
568 1 Y 1 B SER 416  ? B SER 416 
569 1 Y 1 B PRO 417  ? B PRO 417 
570 1 Y 1 B GLU 418  ? B GLU 418 
571 1 Y 1 B MET 419  ? B MET 419 
572 1 Y 1 B LYS 420  ? B LYS 420 
573 1 Y 1 B ASP 421  ? B ASP 421 
574 1 Y 1 B PHE 422  ? B PHE 422 
575 1 Y 1 B ARG 423  ? B ARG 423 
576 1 Y 1 B HIS 424  ? B HIS 424 
577 1 Y 1 B GLY 425  ? B GLY 425 
578 1 Y 1 B PHE 426  ? B PHE 426 
579 1 Y 1 B ASP 427  ? B ASP 427 
580 1 Y 1 B ILE 428  ? B ILE 428 
581 1 Y 1 B LEU 429  ? B LEU 429 
582 1 Y 1 B VAL 430  ? B VAL 430 
583 1 Y 1 B GLY 431  ? B GLY 431 
584 1 Y 1 B GLN 432  ? B GLN 432 
585 1 Y 1 B ILE 433  ? B ILE 433 
586 1 Y 1 B ASP 434  ? B ASP 434 
587 1 Y 1 B ASP 435  ? B ASP 435 
588 1 Y 1 B ALA 436  ? B ALA 436 
589 1 Y 1 B LEU 437  ? B LEU 437 
590 1 Y 1 B LYS 438  ? B LYS 438 
591 1 Y 1 B LEU 439  ? B LEU 439 
592 1 Y 1 B ALA 440  ? B ALA 440 
593 1 Y 1 B ASN 441  ? B ASN 441 
594 1 Y 1 B GLU 442  ? B GLU 442 
595 1 Y 1 B GLY 443  ? B GLY 443 
596 1 Y 1 B LYS 444  ? B LYS 444 
597 1 Y 1 B VAL 445  ? B VAL 445 
598 1 Y 1 B LYS 446  ? B LYS 446 
599 1 Y 1 B GLU 447  ? B GLU 447 
600 1 Y 1 B ALA 448  ? B ALA 448 
601 1 Y 1 B GLN 449  ? B GLN 449 
602 1 Y 1 B ALA 450  ? B ALA 450 
603 1 Y 1 B ALA 451  ? B ALA 451 
604 1 Y 1 B ALA 452  ? B ALA 452 
605 1 Y 1 B GLU 453  ? B GLU 453 
606 1 Y 1 B GLN 454  ? B GLN 454 
607 1 Y 1 B LEU 455  ? B LEU 455 
608 1 Y 1 B LYS 456  ? B LYS 456 
609 1 Y 1 B THR 457  ? B THR 457 
610 1 Y 1 B THR 458  ? B THR 458 
611 1 Y 1 B ARG 459  ? B ARG 459 
612 1 Y 1 B ASN 460  ? B ASN 460 
613 1 Y 1 B ALA 461  ? B ALA 461 
614 1 Y 1 B TYR 462  ? B TYR 462 
615 1 Y 1 B ILE 463  ? B ILE 463 
616 1 Y 1 B GLN 464  ? B GLN 464 
617 1 Y 1 B LYS 465  ? B LYS 465 
618 1 Y 1 B TYR 466  ? B TYR 466 
619 1 Y 1 B LEU 467  ? B LEU 467 
620 1 Y 1 B GLU 468  ? B GLU 468 
621 1 Y 1 B ARG 469  ? B ARG 469 
622 1 Y 1 B ALA 470  ? B ALA 470 
623 1 Y 1 B ARG 471  ? B ARG 471 
624 1 Y 1 B SER 472  ? B SER 472 
625 1 Y 1 B THR 473  ? B THR 473 
626 1 Y 1 B LEU 474  ? B LEU 474 
627 1 Y 1 B ASP 475  ? B ASP 475 
628 1 Y 1 B LYS 476  ? B LYS 476 
629 1 Y 1 B LEU 477  ? B LEU 477 
630 1 Y 1 B ASN 478  ? B ASN 478 
631 1 Y 1 B ASP 479  ? B ASP 479 
632 1 Y 1 B ASP 480  ? B ASP 480 
633 1 Y 1 B ILE 481  ? B ILE 481 
634 1 Y 1 B PHE 482  ? B PHE 482 
635 1 Y 1 B LYS 483  ? B LYS 483 
636 1 Y 1 B ILE 484  ? B ILE 484 
637 1 Y 1 B ILE 485  ? B ILE 485 
638 1 Y 1 B MET 486  ? B MET 486 
639 1 Y 1 B ALA 487  ? B ALA 487 
640 1 Y 1 B ILE 488  ? B ILE 488 
641 1 Y 1 B VAL 489  ? B VAL 489 
642 1 Y 1 B LEU 490  ? B LEU 490 
643 1 Y 1 B PHE 491  ? B PHE 491 
644 1 Y 1 B PHE 492  ? B PHE 492 
645 1 Y 1 B PHE 493  ? B PHE 493 
646 1 Y 1 B PHE 494  ? B PHE 494 
647 1 Y 1 B SER 495  ? B SER 495 
648 1 Y 1 B TRP 496  ? B TRP 496 
649 1 Y 1 B ILE 497  ? B ILE 497 
650 1 Y 1 B PRO 498  ? B PRO 498 
651 1 Y 1 B HIS 499  ? B HIS 499 
652 1 Y 1 B GLN 500  ? B GLN 500 
653 1 Y 1 B ILE 501  ? B ILE 501 
654 1 Y 1 B PHE 502  ? B PHE 502 
655 1 Y 1 B THR 503  ? B THR 503 
656 1 Y 1 B PHE 504  ? B PHE 504 
657 1 Y 1 B LEU 505  ? B LEU 505 
658 1 Y 1 B ASP 506  ? B ASP 506 
659 1 Y 1 B VAL 507  ? B VAL 507 
660 1 Y 1 B LEU 508  ? B LEU 508 
661 1 Y 1 B ILE 509  ? B ILE 509 
662 1 Y 1 B GLN 510  ? B GLN 510 
663 1 Y 1 B LEU 511  ? B LEU 511 
664 1 Y 1 B GLY 512  ? B GLY 512 
665 1 Y 1 B ILE 513  ? B ILE 513 
666 1 Y 1 B ILE 514  ? B ILE 514 
667 1 Y 1 B ARG 515  ? B ARG 515 
668 1 Y 1 B ASP 516  ? B ASP 516 
669 1 Y 1 B CYS 517  ? B CYS 517 
670 1 Y 1 B ARG 518  ? B ARG 518 
671 1 Y 1 B ILE 519  ? B ILE 519 
672 1 Y 1 B ALA 520  ? B ALA 520 
673 1 Y 1 B ASP 521  ? B ASP 521 
674 1 Y 1 B ILE 522  ? B ILE 522 
675 1 Y 1 B VAL 523  ? B VAL 523 
676 1 Y 1 B ASP 524  ? B ASP 524 
677 1 Y 1 B THR 525  ? B THR 525 
678 1 Y 1 B ALA 526  ? B ALA 526 
679 1 Y 1 B MET 527  ? B MET 527 
680 1 Y 1 B PRO 528  ? B PRO 528 
681 1 Y 1 B ILE 529  ? B ILE 529 
682 1 Y 1 B THR 530  ? B THR 530 
683 1 Y 1 B ILE 531  ? B ILE 531 
684 1 Y 1 B CYS 532  ? B CYS 532 
685 1 Y 1 B ILE 533  ? B ILE 533 
686 1 Y 1 B ALA 534  ? B ALA 534 
687 1 Y 1 B TYR 535  ? B TYR 535 
688 1 Y 1 B PHE 536  ? B PHE 536 
689 1 Y 1 B ASN 537  ? B ASN 537 
690 1 Y 1 B ASN 538  ? B ASN 538 
691 1 Y 1 B CYS 539  ? B CYS 539 
692 1 Y 1 B LEU 540  ? B LEU 540 
693 1 Y 1 B ASN 541  ? B ASN 541 
694 1 Y 1 B PRO 542  ? B PRO 542 
695 1 Y 1 B LEU 543  ? B LEU 543 
696 1 Y 1 B PHE 544  ? B PHE 544 
697 1 Y 1 B TYR 545  ? B TYR 545 
698 1 Y 1 B GLY 546  ? B GLY 546 
699 1 Y 1 B PHE 547  ? B PHE 547 
700 1 Y 1 B LEU 548  ? B LEU 548 
701 1 Y 1 B GLY 549  ? B GLY 549 
702 1 Y 1 B LYS 550  ? B LYS 550 
703 1 Y 1 B LYS 551  ? B LYS 551 
704 1 Y 1 B PHE 552  ? B PHE 552 
705 1 Y 1 B LYS 553  ? B LYS 553 
706 1 Y 1 B ARG 554  ? B ARG 554 
707 1 Y 1 B TYR 555  ? B TYR 555 
708 1 Y 1 B PHE 556  ? B PHE 556 
709 1 Y 1 B LEU 557  ? B LEU 557 
710 1 Y 1 B GLN 558  ? B GLN 558 
711 1 Y 1 B LEU 559  ? B LEU 559 
712 1 Y 1 B LEU 560  ? B LEU 560 
713 1 Y 1 B LYS 561  ? B LYS 561 
714 1 Y 1 B TYR 562  ? B TYR 562 
715 1 Y 1 B GLY 563  ? B GLY 563 
716 1 Y 1 B GLY 564  ? B GLY 564 
717 1 Y 1 B SER 565  ? B SER 565 
718 1 Y 1 B SER 566  ? B SER 566 
719 1 Y 1 B LEU 567  ? B LEU 567 
720 1 Y 1 B GLU 568  ? B GLU 568 
721 1 Y 1 B VAL 569  ? B VAL 569 
722 1 Y 1 B LEU 570  ? B LEU 570 
723 1 Y 1 B PHE 571  ? B PHE 571 
724 1 Y 1 B GLN 572  ? B GLN 572 
725 1 Y 1 B GLY 573  ? B GLY 573 
726 1 Y 1 B PRO 574  ? B PRO 574 
727 1 Y 1 B THR 575  ? B THR 575 
728 1 Y 1 B GLU 576  ? B GLU 576 
729 1 Y 1 B THR 577  ? B THR 577 
730 1 Y 1 B SER 578  ? B SER 578 
731 1 Y 1 B GLN 579  ? B GLN 579 
732 1 Y 1 B VAL 580  ? B VAL 580 
733 1 Y 1 B ALA 581  ? B ALA 581 
734 1 Y 1 B PRO 582  ? B PRO 582 
735 1 Y 1 B ALA 583  ? B ALA 583 
736 1 Y 1 C GLU 1    ? C GLU 1   
737 1 Y 1 C ILE 2    ? C ILE 2   
738 1 Y 1 C SER 3    ? C SER 3   
739 1 Y 1 C SER 126  ? C SER 126 
740 1 Y 1 C SER 127  ? C SER 127 
741 1 Y 1 C ALA 128  ? C ALA 128 
742 1 Y 1 C SER 129  ? C SER 129 
743 1 Y 1 C THR 130  ? C THR 130 
744 1 Y 1 C LYS 131  ? C LYS 131 
745 1 Y 1 C GLY 132  ? C GLY 132 
746 1 Y 1 C PRO 133  ? C PRO 133 
747 1 Y 1 C SER 134  ? C SER 134 
748 1 Y 1 C VAL 135  ? C VAL 135 
749 1 Y 1 C PHE 136  ? C PHE 136 
750 1 Y 1 C PRO 137  ? C PRO 137 
751 1 Y 1 C LEU 138  ? C LEU 138 
752 1 Y 1 C ALA 139  ? C ALA 139 
753 1 Y 1 C PRO 140  ? C PRO 140 
754 1 Y 1 C SER 141  ? C SER 141 
755 1 Y 1 C SER 142  ? C SER 142 
756 1 Y 1 C LYS 143  ? C LYS 143 
757 1 Y 1 C SER 144  ? C SER 144 
758 1 Y 1 C THR 145  ? C THR 145 
759 1 Y 1 C SER 146  ? C SER 146 
760 1 Y 1 C GLY 147  ? C GLY 147 
761 1 Y 1 C GLY 148  ? C GLY 148 
762 1 Y 1 C THR 149  ? C THR 149 
763 1 Y 1 C ALA 150  ? C ALA 150 
764 1 Y 1 C ALA 151  ? C ALA 151 
765 1 Y 1 C LEU 152  ? C LEU 152 
766 1 Y 1 C GLY 153  ? C GLY 153 
767 1 Y 1 C CYS 154  ? C CYS 154 
768 1 Y 1 C LEU 155  ? C LEU 155 
769 1 Y 1 C VAL 156  ? C VAL 156 
770 1 Y 1 C LYS 157  ? C LYS 157 
771 1 Y 1 C ASP 158  ? C ASP 158 
772 1 Y 1 C TYR 159  ? C TYR 159 
773 1 Y 1 C PHE 160  ? C PHE 160 
774 1 Y 1 C PRO 161  ? C PRO 161 
775 1 Y 1 C GLU 162  ? C GLU 162 
776 1 Y 1 C PRO 163  ? C PRO 163 
777 1 Y 1 C VAL 164  ? C VAL 164 
778 1 Y 1 C THR 165  ? C THR 165 
779 1 Y 1 C VAL 166  ? C VAL 166 
780 1 Y 1 C SER 167  ? C SER 167 
781 1 Y 1 C TRP 168  ? C TRP 168 
782 1 Y 1 C ASN 169  ? C ASN 169 
783 1 Y 1 C SER 170  ? C SER 170 
784 1 Y 1 C GLY 171  ? C GLY 171 
785 1 Y 1 C ALA 172  ? C ALA 172 
786 1 Y 1 C LEU 173  ? C LEU 173 
787 1 Y 1 C THR 174  ? C THR 174 
788 1 Y 1 C SER 175  ? C SER 175 
789 1 Y 1 C GLY 176  ? C GLY 176 
790 1 Y 1 C VAL 177  ? C VAL 177 
791 1 Y 1 C HIS 178  ? C HIS 178 
792 1 Y 1 C THR 179  ? C THR 179 
793 1 Y 1 C PHE 180  ? C PHE 180 
794 1 Y 1 C PRO 181  ? C PRO 181 
795 1 Y 1 C ALA 182  ? C ALA 182 
796 1 Y 1 C VAL 183  ? C VAL 183 
797 1 Y 1 C LEU 184  ? C LEU 184 
798 1 Y 1 C GLN 185  ? C GLN 185 
799 1 Y 1 C SER 186  ? C SER 186 
800 1 Y 1 C SER 187  ? C SER 187 
801 1 Y 1 C GLY 188  ? C GLY 188 
802 1 Y 1 C LEU 189  ? C LEU 189 
803 1 Y 1 C TYR 190  ? C TYR 190 
804 1 Y 1 C SER 191  ? C SER 191 
805 1 Y 1 C LEU 192  ? C LEU 192 
806 1 Y 1 C SER 193  ? C SER 193 
807 1 Y 1 C SER 194  ? C SER 194 
808 1 Y 1 C VAL 195  ? C VAL 195 
809 1 Y 1 C VAL 196  ? C VAL 196 
810 1 Y 1 C THR 197  ? C THR 197 
811 1 Y 1 C VAL 198  ? C VAL 198 
812 1 Y 1 C PRO 199  ? C PRO 199 
813 1 Y 1 C SER 200  ? C SER 200 
814 1 Y 1 C SER 201  ? C SER 201 
815 1 Y 1 C SER 202  ? C SER 202 
816 1 Y 1 C LEU 203  ? C LEU 203 
817 1 Y 1 C GLY 204  ? C GLY 204 
818 1 Y 1 C THR 205  ? C THR 205 
819 1 Y 1 C GLN 206  ? C GLN 206 
820 1 Y 1 C THR 207  ? C THR 207 
821 1 Y 1 C TYR 208  ? C TYR 208 
822 1 Y 1 C ILE 209  ? C ILE 209 
823 1 Y 1 C CYS 210  ? C CYS 210 
824 1 Y 1 C ASN 211  ? C ASN 211 
825 1 Y 1 C VAL 212  ? C VAL 212 
826 1 Y 1 C ASN 213  ? C ASN 213 
827 1 Y 1 C HIS 214  ? C HIS 214 
828 1 Y 1 C LYS 215  ? C LYS 215 
829 1 Y 1 C PRO 216  ? C PRO 216 
830 1 Y 1 C SER 217  ? C SER 217 
831 1 Y 1 C ASN 218  ? C ASN 218 
832 1 Y 1 C THR 219  ? C THR 219 
833 1 Y 1 C LYS 220  ? C LYS 220 
834 1 Y 1 C VAL 221  ? C VAL 221 
835 1 Y 1 C ASP 222  ? C ASP 222 
836 1 Y 1 C LYS 223  ? C LYS 223 
837 1 Y 1 C LYS 224  ? C LYS 224 
838 1 Y 1 C VAL 225  ? C VAL 225 
839 1 Y 1 C GLU 226  ? C GLU 226 
840 1 Y 1 C PRO 227  ? C PRO 227 
841 1 Y 1 C LYS 228  ? C LYS 228 
842 1 Y 1 C SER 229  ? C SER 229 
843 1 Y 1 C CYS 230  ? C CYS 230 
844 1 Y 1 C ASP 231  ? C ASP 231 
845 1 Y 1 D THR 111  ? D THR 110 
846 1 Y 1 D VAL 112  ? D VAL 111 
847 1 Y 1 D ALA 113  ? D ALA 112 
848 1 Y 1 D ALA 114  ? D ALA 113 
849 1 Y 1 D PRO 115  ? D PRO 114 
850 1 Y 1 D SER 116  ? D SER 115 
851 1 Y 1 D VAL 117  ? D VAL 116 
852 1 Y 1 D PHE 118  ? D PHE 117 
853 1 Y 1 D ILE 119  ? D ILE 118 
854 1 Y 1 D PHE 120  ? D PHE 119 
855 1 Y 1 D PRO 121  ? D PRO 120 
856 1 Y 1 D PRO 122  ? D PRO 121 
857 1 Y 1 D SER 123  ? D SER 122 
858 1 Y 1 D ASP 124  ? D ASP 123 
859 1 Y 1 D GLU 125  ? D GLU 124 
860 1 Y 1 D GLN 126  ? D GLN 125 
861 1 Y 1 D LEU 127  ? D LEU 126 
862 1 Y 1 D LYS 128  ? D LYS 127 
863 1 Y 1 D SER 129  ? D SER 128 
864 1 Y 1 D GLY 130  ? D GLY 129 
865 1 Y 1 D THR 131  ? D THR 130 
866 1 Y 1 D ALA 132  ? D ALA 131 
867 1 Y 1 D SER 133  ? D SER 132 
868 1 Y 1 D VAL 134  ? D VAL 133 
869 1 Y 1 D VAL 135  ? D VAL 134 
870 1 Y 1 D CYS 136  ? D CYS 135 
871 1 Y 1 D LEU 137  ? D LEU 136 
872 1 Y 1 D LEU 138  ? D LEU 137 
873 1 Y 1 D ASN 139  ? D ASN 138 
874 1 Y 1 D ASN 140  ? D ASN 139 
875 1 Y 1 D PHE 141  ? D PHE 140 
876 1 Y 1 D TYR 142  ? D TYR 141 
877 1 Y 1 D PRO 143  ? D PRO 142 
878 1 Y 1 D ARG 144  ? D ARG 143 
879 1 Y 1 D GLU 145  ? D GLU 144 
880 1 Y 1 D ALA 146  ? D ALA 145 
881 1 Y 1 D LYS 147  ? D LYS 146 
882 1 Y 1 D VAL 148  ? D VAL 147 
883 1 Y 1 D GLN 149  ? D GLN 148 
884 1 Y 1 D TRP 150  ? D TRP 149 
885 1 Y 1 D LYS 151  ? D LYS 150 
886 1 Y 1 D VAL 152  ? D VAL 151 
887 1 Y 1 D ASP 153  ? D ASP 152 
888 1 Y 1 D ASN 154  ? D ASN 153 
889 1 Y 1 D ALA 155  ? D ALA 154 
890 1 Y 1 D LEU 156  ? D LEU 155 
891 1 Y 1 D GLN 157  ? D GLN 156 
892 1 Y 1 D SER 158  ? D SER 157 
893 1 Y 1 D GLY 159  ? D GLY 158 
894 1 Y 1 D ASN 160  ? D ASN 159 
895 1 Y 1 D SER 161  ? D SER 160 
896 1 Y 1 D GLN 162  ? D GLN 161 
897 1 Y 1 D GLU 163  ? D GLU 162 
898 1 Y 1 D SER 164  ? D SER 163 
899 1 Y 1 D VAL 165  ? D VAL 164 
900 1 Y 1 D THR 166  ? D THR 165 
901 1 Y 1 D GLU 167  ? D GLU 166 
902 1 Y 1 D GLN 168  ? D GLN 167 
903 1 Y 1 D ASP 169  ? D ASP 168 
904 1 Y 1 D SER 170  ? D SER 169 
905 1 Y 1 D LYS 171  ? D LYS 170 
906 1 Y 1 D ASP 172  ? D ASP 171 
907 1 Y 1 D SER 173  ? D SER 172 
908 1 Y 1 D THR 174  ? D THR 173 
909 1 Y 1 D TYR 175  ? D TYR 174 
910 1 Y 1 D SER 176  ? D SER 175 
911 1 Y 1 D LEU 177  ? D LEU 176 
912 1 Y 1 D SER 178  ? D SER 177 
913 1 Y 1 D SER 179  ? D SER 178 
914 1 Y 1 D THR 180  ? D THR 179 
915 1 Y 1 D LEU 181  ? D LEU 180 
916 1 Y 1 D THR 182  ? D THR 181 
917 1 Y 1 D LEU 183  ? D LEU 182 
918 1 Y 1 D SER 184  ? D SER 183 
919 1 Y 1 D LYS 185  ? D LYS 184 
920 1 Y 1 D ALA 186  ? D ALA 185 
921 1 Y 1 D ASP 187  ? D ASP 186 
922 1 Y 1 D TYR 188  ? D TYR 187 
923 1 Y 1 D GLU 189  ? D GLU 188 
924 1 Y 1 D LYS 190  ? D LYS 189 
925 1 Y 1 D HIS 191  ? D HIS 190 
926 1 Y 1 D LYS 192  ? D LYS 191 
927 1 Y 1 D VAL 193  ? D VAL 192 
928 1 Y 1 D TYR 194  ? D TYR 193 
929 1 Y 1 D ALA 195  ? D ALA 194 
930 1 Y 1 D CYS 196  ? D CYS 195 
931 1 Y 1 D GLU 197  ? D GLU 196 
932 1 Y 1 D VAL 198  ? D VAL 197 
933 1 Y 1 D THR 199  ? D THR 198 
934 1 Y 1 D HIS 200  ? D HIS 199 
935 1 Y 1 D GLN 201  ? D GLN 200 
936 1 Y 1 D GLY 202  ? D GLY 201 
937 1 Y 1 D LEU 203  ? D LEU 202 
938 1 Y 1 D SER 204  ? D SER 203 
939 1 Y 1 D SER 205  ? D SER 204 
940 1 Y 1 D PRO 206  ? D PRO 205 
941 1 Y 1 D VAL 207  ? D VAL 206 
942 1 Y 1 D THR 208  ? D THR 207 
943 1 Y 1 D LYS 209  ? D LYS 208 
944 1 Y 1 D SER 210  ? D SER 209 
945 1 Y 1 D PHE 211  ? D PHE 210 
946 1 Y 1 D ASN 212  ? D ASN 211 
947 1 Y 1 D ARG 213  ? D ARG 212 
948 1 Y 1 D GLY 214  ? D GLY 213 
949 1 Y 1 D GLU 215  ? D GLU 214 
950 1 Y 1 D CYS 216  ? D CYS 215 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-11-11 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9EAJ 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'Structure of nanobody AT206 in complex with the angiotensin II type I receptor (AT1R)' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               Expi293R 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         63.5 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     7964 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   1417574 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.21.1_5286: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Helen Hay Whitney Foundation'                                                                                            
'United States' ?           1 
'National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)' 
'United States' K99HD110612 2 
'National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)' 
'United States' R21HD101596 3 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                                                       
'United States' R01CA260415 4 
# 
_atom_sites.entry_id                    9EAJ 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_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 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . MET A 1 166 ? 160.943 160.839 123.821 1.00 127.22 ? 30   MET A N   1 
ATOM 2    C CA  . MET A 1 166 ? 161.487 159.512 124.078 1.00 128.16 ? 30   MET A CA  1 
ATOM 3    C C   . MET A 1 166 ? 160.412 158.445 123.935 1.00 125.06 ? 30   MET A C   1 
ATOM 4    O O   . MET A 1 166 ? 160.713 157.270 123.715 1.00 122.55 ? 30   MET A O   1 
ATOM 5    C CB  . MET A 1 166 ? 162.120 159.451 125.471 1.00 129.70 ? 30   MET A CB  1 
ATOM 6    C CG  . MET A 1 166 ? 162.777 158.119 125.821 1.00 130.61 ? 30   MET A CG  1 
ATOM 7    S SD  . MET A 1 166 ? 163.837 157.440 124.523 1.00 135.57 ? 30   MET A SD  1 
ATOM 8    C CE  . MET A 1 166 ? 165.065 158.729 124.370 1.00 132.10 ? 30   MET A CE  1 
ATOM 9    N N   . ILE A 1 167 ? 159.156 158.869 124.057 1.00 125.26 ? 31   ILE A N   1 
ATOM 10   C CA  . ILE A 1 167 ? 158.034 157.956 123.829 1.00 122.51 ? 31   ILE A CA  1 
ATOM 11   C C   . ILE A 1 167 ? 158.133 157.252 122.479 1.00 120.89 ? 31   ILE A C   1 
ATOM 12   O O   . ILE A 1 167 ? 157.909 156.035 122.428 1.00 121.26 ? 31   ILE A O   1 
ATOM 13   C CB  . ILE A 1 167 ? 156.702 158.698 124.016 1.00 121.28 ? 31   ILE A CB  1 
ATOM 14   C CG1 . ILE A 1 167 ? 156.676 159.421 125.358 1.00 118.11 ? 31   ILE A CG1 1 
ATOM 15   C CG2 . ILE A 1 167 ? 155.532 157.743 123.884 1.00 115.97 ? 31   ILE A CG2 1 
ATOM 16   C CD1 . ILE A 1 167 ? 156.827 158.497 126.538 1.00 115.49 ? 31   ILE A CD1 1 
ATOM 17   N N   . PRO A 1 168 ? 158.440 157.928 121.367 1.00 120.19 ? 32   PRO A N   1 
ATOM 18   C CA  . PRO A 1 168 ? 158.617 157.191 120.108 1.00 118.90 ? 32   PRO A CA  1 
ATOM 19   C C   . PRO A 1 168 ? 159.737 156.171 120.156 1.00 119.69 ? 32   PRO A C   1 
ATOM 20   O O   . PRO A 1 168 ? 159.625 155.111 119.527 1.00 118.16 ? 32   PRO A O   1 
ATOM 21   C CB  . PRO A 1 168 ? 158.917 158.303 119.094 1.00 118.96 ? 32   PRO A CB  1 
ATOM 22   C CG  . PRO A 1 168 ? 158.324 159.517 119.675 1.00 119.16 ? 32   PRO A CG  1 
ATOM 23   C CD  . PRO A 1 168 ? 158.516 159.382 121.148 1.00 119.15 ? 32   PRO A CD  1 
ATOM 24   N N   . THR A 1 169 ? 160.817 156.456 120.881 1.00 121.52 ? 33   THR A N   1 
ATOM 25   C CA  . THR A 1 169 ? 161.947 155.538 120.931 1.00 122.48 ? 33   THR A CA  1 
ATOM 26   C C   . THR A 1 169 ? 161.815 154.504 122.039 1.00 120.97 ? 33   THR A C   1 
ATOM 27   O O   . THR A 1 169 ? 162.338 153.392 121.903 1.00 118.33 ? 33   THR A O   1 
ATOM 28   C CB  . THR A 1 169 ? 163.255 156.314 121.107 1.00 123.05 ? 33   THR A CB  1 
ATOM 29   O OG1 . THR A 1 169 ? 163.264 157.441 120.222 1.00 120.54 ? 33   THR A OG1 1 
ATOM 30   C CG2 . THR A 1 169 ? 164.445 155.424 120.779 1.00 121.04 ? 33   THR A CG2 1 
ATOM 31   N N   . LEU A 1 170 ? 161.120 154.839 123.128 1.00 121.03 ? 34   LEU A N   1 
ATOM 32   C CA  . LEU A 1 170 ? 160.880 153.854 124.178 1.00 120.59 ? 34   LEU A CA  1 
ATOM 33   C C   . LEU A 1 170 ? 160.016 152.709 123.664 1.00 116.75 ? 34   LEU A C   1 
ATOM 34   O O   . LEU A 1 170 ? 160.208 151.552 124.055 1.00 116.70 ? 34   LEU A O   1 
ATOM 35   C CB  . LEU A 1 170 ? 160.230 154.523 125.389 1.00 121.69 ? 34   LEU A CB  1 
ATOM 36   C CG  . LEU A 1 170 ? 159.943 153.633 126.598 1.00 118.40 ? 34   LEU A CG  1 
ATOM 37   C CD1 . LEU A 1 170 ? 161.159 152.796 126.949 1.00 118.51 ? 34   LEU A CD1 1 
ATOM 38   C CD2 . LEU A 1 170 ? 159.522 154.476 127.788 1.00 114.04 ? 34   LEU A CD2 1 
ATOM 39   N N   . TYR A 1 171 ? 159.062 153.012 122.782 1.00 114.54 ? 35   TYR A N   1 
ATOM 40   C CA  . TYR A 1 171 ? 158.273 151.957 122.156 1.00 112.59 ? 35   TYR A CA  1 
ATOM 41   C C   . TYR A 1 171 ? 159.152 151.036 121.321 1.00 114.26 ? 35   TYR A C   1 
ATOM 42   O O   . TYR A 1 171 ? 158.944 149.818 121.301 1.00 112.95 ? 35   TYR A O   1 
ATOM 43   C CB  . TYR A 1 171 ? 157.168 152.568 121.297 1.00 111.75 ? 35   TYR A CB  1 
ATOM 44   C CG  . TYR A 1 171 ? 155.955 153.021 122.073 1.00 113.16 ? 35   TYR A CG  1 
ATOM 45   C CD1 . TYR A 1 171 ? 155.599 152.405 123.264 1.00 110.94 ? 35   TYR A CD1 1 
ATOM 46   C CD2 . TYR A 1 171 ? 155.163 154.064 121.613 1.00 114.49 ? 35   TYR A CD2 1 
ATOM 47   C CE1 . TYR A 1 171 ? 154.487 152.816 123.976 1.00 107.86 ? 35   TYR A CE1 1 
ATOM 48   C CE2 . TYR A 1 171 ? 154.050 154.482 122.318 1.00 112.83 ? 35   TYR A CE2 1 
ATOM 49   C CZ  . TYR A 1 171 ? 153.718 153.855 123.499 1.00 110.42 ? 35   TYR A CZ  1 
ATOM 50   O OH  . TYR A 1 171 ? 152.612 154.268 124.205 1.00 107.75 ? 35   TYR A OH  1 
ATOM 51   N N   . SER A 1 172 ? 160.141 151.600 120.623 1.00 114.40 ? 36   SER A N   1 
ATOM 52   C CA  . SER A 1 172 ? 161.059 150.775 119.844 1.00 114.41 ? 36   SER A CA  1 
ATOM 53   C C   . SER A 1 172 ? 161.819 149.806 120.740 1.00 113.79 ? 36   SER A C   1 
ATOM 54   O O   . SER A 1 172 ? 162.086 148.664 120.348 1.00 112.87 ? 36   SER A O   1 
ATOM 55   C CB  . SER A 1 172 ? 162.028 151.661 119.065 1.00 113.51 ? 36   SER A CB  1 
ATOM 56   O OG  . SER A 1 172 ? 161.329 152.567 118.229 1.00 113.33 ? 36   SER A OG  1 
ATOM 57   N N   . ILE A 1 173 ? 162.177 150.245 121.948 1.00 114.82 ? 37   ILE A N   1 
ATOM 58   C CA  . ILE A 1 173 ? 162.842 149.359 122.899 1.00 116.82 ? 37   ILE A CA  1 
ATOM 59   C C   . ILE A 1 173 ? 161.912 148.225 123.311 1.00 113.06 ? 37   ILE A C   1 
ATOM 60   O O   . ILE A 1 173 ? 162.330 147.066 123.419 1.00 109.24 ? 37   ILE A O   1 
ATOM 61   C CB  . ILE A 1 173 ? 163.332 150.161 124.119 1.00 119.71 ? 37   ILE A CB  1 
ATOM 62   C CG1 . ILE A 1 173 ? 164.197 151.340 123.667 1.00 119.54 ? 37   ILE A CG1 1 
ATOM 63   C CG2 . ILE A 1 173 ? 164.103 149.263 125.075 1.00 118.04 ? 37   ILE A CG2 1 
ATOM 64   C CD1 . ILE A 1 173 ? 164.632 152.246 124.798 1.00 117.62 ? 37   ILE A CD1 1 
ATOM 65   N N   . ILE A 1 174 ? 160.636 148.542 123.549 1.00 113.05 ? 38   ILE A N   1 
ATOM 66   C CA  . ILE A 1 174 ? 159.675 147.532 123.984 1.00 108.33 ? 38   ILE A CA  1 
ATOM 67   C C   . ILE A 1 174 ? 159.495 146.464 122.913 1.00 106.59 ? 38   ILE A C   1 
ATOM 68   O O   . ILE A 1 174 ? 159.425 145.266 123.215 1.00 103.75 ? 38   ILE A O   1 
ATOM 69   C CB  . ILE A 1 174 ? 158.334 148.195 124.349 1.00 106.23 ? 38   ILE A CB  1 
ATOM 70   C CG1 . ILE A 1 174 ? 158.523 149.196 125.487 1.00 108.27 ? 38   ILE A CG1 1 
ATOM 71   C CG2 . ILE A 1 174 ? 157.301 147.146 124.728 1.00 101.41 ? 38   ILE A CG2 1 
ATOM 72   C CD1 . ILE A 1 174 ? 157.261 149.946 125.840 1.00 108.58 ? 38   ILE A CD1 1 
ATOM 73   N N   . PHE A 1 175 ? 159.406 146.878 121.648 1.00 106.18 ? 39   PHE A N   1 
ATOM 74   C CA  . PHE A 1 175 ? 159.193 145.918 120.570 1.00 103.80 ? 39   PHE A CA  1 
ATOM 75   C C   . PHE A 1 175 ? 160.372 144.963 120.434 1.00 108.59 ? 39   PHE A C   1 
ATOM 76   O O   . PHE A 1 175 ? 160.184 143.770 120.171 1.00 107.95 ? 39   PHE A O   1 
ATOM 77   C CB  . PHE A 1 175 ? 158.945 146.652 119.253 1.00 100.39 ? 39   PHE A CB  1 
ATOM 78   C CG  . PHE A 1 175 ? 158.621 145.741 118.104 1.00 100.39 ? 39   PHE A CG  1 
ATOM 79   C CD1 . PHE A 1 175 ? 157.325 145.303 117.896 1.00 97.60  ? 39   PHE A CD1 1 
ATOM 80   C CD2 . PHE A 1 175 ? 159.610 145.325 117.229 1.00 102.96 ? 39   PHE A CD2 1 
ATOM 81   C CE1 . PHE A 1 175 ? 157.020 144.467 116.839 1.00 95.46  ? 39   PHE A CE1 1 
ATOM 82   C CE2 . PHE A 1 175 ? 159.310 144.487 116.171 1.00 100.38 ? 39   PHE A CE2 1 
ATOM 83   C CZ  . PHE A 1 175 ? 158.013 144.058 115.977 1.00 95.40  ? 39   PHE A CZ  1 
ATOM 84   N N   . VAL A 1 176 ? 161.597 145.469 120.595 1.00 111.34 ? 40   VAL A N   1 
ATOM 85   C CA  . VAL A 1 176 ? 162.775 144.614 120.460 1.00 111.05 ? 40   VAL A CA  1 
ATOM 86   C C   . VAL A 1 176 ? 162.791 143.552 121.553 1.00 108.41 ? 40   VAL A C   1 
ATOM 87   O O   . VAL A 1 176 ? 162.922 142.354 121.279 1.00 105.42 ? 40   VAL A O   1 
ATOM 88   C CB  . VAL A 1 176 ? 164.061 145.462 120.482 1.00 111.19 ? 40   VAL A CB  1 
ATOM 89   C CG1 . VAL A 1 176 ? 165.287 144.566 120.454 1.00 111.13 ? 40   VAL A CG1 1 
ATOM 90   C CG2 . VAL A 1 176 ? 164.084 146.425 119.310 1.00 110.64 ? 40   VAL A CG2 1 
ATOM 91   N N   . VAL A 1 177 ? 162.643 143.977 122.808 1.00 108.09 ? 41   VAL A N   1 
ATOM 92   C CA  . VAL A 1 177 ? 162.689 143.034 123.921 1.00 106.97 ? 41   VAL A CA  1 
ATOM 93   C C   . VAL A 1 177 ? 161.424 142.188 123.966 1.00 106.21 ? 41   VAL A C   1 
ATOM 94   O O   . VAL A 1 177 ? 161.482 140.973 124.187 1.00 105.78 ? 41   VAL A O   1 
ATOM 95   C CB  . VAL A 1 177 ? 162.915 143.787 125.244 1.00 107.97 ? 41   VAL A CB  1 
ATOM 96   C CG1 . VAL A 1 177 ? 162.986 142.811 126.407 1.00 104.66 ? 41   VAL A CG1 1 
ATOM 97   C CG2 . VAL A 1 177 ? 164.178 144.625 125.167 1.00 110.25 ? 41   VAL A CG2 1 
ATOM 98   N N   . GLY A 1 178 ? 160.264 142.814 123.764 1.00 105.28 ? 42   GLY A N   1 
ATOM 99   C CA  . GLY A 1 178 ? 159.009 142.096 123.928 1.00 101.46 ? 42   GLY A CA  1 
ATOM 100  C C   . GLY A 1 178 ? 158.824 140.977 122.920 1.00 98.69  ? 42   GLY A C   1 
ATOM 101  O O   . GLY A 1 178 ? 158.435 139.863 123.279 1.00 97.35  ? 42   GLY A O   1 
ATOM 102  N N   . ILE A 1 179 ? 159.090 141.259 121.644 1.00 99.28  ? 43   ILE A N   1 
ATOM 103  C CA  . ILE A 1 179 ? 158.963 140.225 120.621 1.00 101.83 ? 43   ILE A CA  1 
ATOM 104  C C   . ILE A 1 179 ? 159.987 139.122 120.849 1.00 102.86 ? 43   ILE A C   1 
ATOM 105  O O   . ILE A 1 179 ? 159.673 137.931 120.738 1.00 100.90 ? 43   ILE A O   1 
ATOM 106  C CB  . ILE A 1 179 ? 159.093 140.842 119.217 1.00 103.49 ? 43   ILE A CB  1 
ATOM 107  C CG1 . ILE A 1 179 ? 157.922 141.782 118.938 1.00 100.97 ? 43   ILE A CG1 1 
ATOM 108  C CG2 . ILE A 1 179 ? 159.155 139.753 118.157 1.00 103.73 ? 43   ILE A CG2 1 
ATOM 109  C CD1 . ILE A 1 179 ? 156.588 141.082 118.869 1.00 96.01  ? 43   ILE A CD1 1 
ATOM 110  N N   . PHE A 1 180 ? 161.227 139.497 121.166 1.00 104.79 ? 44   PHE A N   1 
ATOM 111  C CA  . PHE A 1 180 ? 162.251 138.499 121.457 1.00 105.31 ? 44   PHE A CA  1 
ATOM 112  C C   . PHE A 1 180 ? 161.912 137.709 122.716 1.00 101.72 ? 44   PHE A C   1 
ATOM 113  O O   . PHE A 1 180 ? 162.085 136.486 122.756 1.00 98.73  ? 44   PHE A O   1 
ATOM 114  C CB  . PHE A 1 180 ? 163.612 139.181 121.592 1.00 108.06 ? 44   PHE A CB  1 
ATOM 115  C CG  . PHE A 1 180 ? 164.690 138.292 122.145 1.00 111.24 ? 44   PHE A CG  1 
ATOM 116  C CD1 . PHE A 1 180 ? 165.111 137.172 121.448 1.00 111.93 ? 44   PHE A CD1 1 
ATOM 117  C CD2 . PHE A 1 180 ? 165.298 138.592 123.353 1.00 110.20 ? 44   PHE A CD2 1 
ATOM 118  C CE1 . PHE A 1 180 ? 166.108 136.359 121.953 1.00 112.45 ? 44   PHE A CE1 1 
ATOM 119  C CE2 . PHE A 1 180 ? 166.297 137.784 123.863 1.00 110.88 ? 44   PHE A CE2 1 
ATOM 120  C CZ  . PHE A 1 180 ? 166.702 136.667 123.161 1.00 112.27 ? 44   PHE A CZ  1 
ATOM 121  N N   . GLY A 1 181 ? 161.421 138.391 123.751 1.00 100.15 ? 45   GLY A N   1 
ATOM 122  C CA  . GLY A 1 181 ? 161.125 137.704 124.998 1.00 95.69  ? 45   GLY A CA  1 
ATOM 123  C C   . GLY A 1 181 ? 159.905 136.807 124.904 1.00 93.76  ? 45   GLY A C   1 
ATOM 124  O O   . GLY A 1 181 ? 159.955 135.632 125.274 1.00 95.73  ? 45   GLY A O   1 
ATOM 125  N N   . ASN A 1 182 ? 158.790 137.349 124.407 1.00 93.19  ? 46   ASN A N   1 
ATOM 126  C CA  . ASN A 1 182 ? 157.544 136.590 124.389 1.00 91.26  ? 46   ASN A CA  1 
ATOM 127  C C   . ASN A 1 182 ? 157.596 135.421 123.415 1.00 90.49  ? 46   ASN A C   1 
ATOM 128  O O   . ASN A 1 182 ? 156.931 134.404 123.640 1.00 91.83  ? 46   ASN A O   1 
ATOM 129  C CB  . ASN A 1 182 ? 156.370 137.507 124.050 1.00 86.83  ? 46   ASN A CB  1 
ATOM 130  C CG  . ASN A 1 182 ? 155.930 138.350 125.230 1.00 86.13  ? 46   ASN A CG  1 
ATOM 131  O OD1 . ASN A 1 182 ? 155.016 137.977 125.963 1.00 83.65  ? 46   ASN A OD1 1 
ATOM 132  N ND2 . ASN A 1 182 ? 156.579 139.491 125.421 1.00 86.01  ? 46   ASN A ND2 1 
ATOM 133  N N   . SER A 1 183 ? 158.358 135.543 122.326 1.00 90.36  ? 47   SER A N   1 
ATOM 134  C CA  . SER A 1 183 ? 158.474 134.428 121.391 1.00 93.31  ? 47   SER A CA  1 
ATOM 135  C C   . SER A 1 183 ? 159.227 133.260 122.018 1.00 95.94  ? 47   SER A C   1 
ATOM 136  O O   . SER A 1 183 ? 158.899 132.096 121.766 1.00 94.43  ? 47   SER A O   1 
ATOM 137  C CB  . SER A 1 183 ? 159.155 134.884 120.102 1.00 98.01  ? 47   SER A CB  1 
ATOM 138  O OG  . SER A 1 183 ? 159.006 133.912 119.081 1.00 100.97 ? 47   SER A OG  1 
ATOM 139  N N   . LEU A 1 184 ? 160.250 133.550 122.825 1.00 97.90  ? 48   LEU A N   1 
ATOM 140  C CA  . LEU A 1 184 ? 160.883 132.496 123.611 1.00 95.56  ? 48   LEU A CA  1 
ATOM 141  C C   . LEU A 1 184 ? 159.927 131.953 124.664 1.00 94.17  ? 48   LEU A C   1 
ATOM 142  O O   . LEU A 1 184 ? 159.890 130.743 124.911 1.00 99.18  ? 48   LEU A O   1 
ATOM 143  C CB  . LEU A 1 184 ? 162.155 133.020 124.274 1.00 96.53  ? 48   LEU A CB  1 
ATOM 144  C CG  . LEU A 1 184 ? 163.282 133.520 123.370 1.00 103.19 ? 48   LEU A CG  1 
ATOM 145  C CD1 . LEU A 1 184 ? 164.449 134.019 124.205 1.00 101.31 ? 48   LEU A CD1 1 
ATOM 146  C CD2 . LEU A 1 184 ? 163.726 132.422 122.419 1.00 105.19 ? 48   LEU A CD2 1 
ATOM 147  N N   . VAL A 1 185 ? 159.151 132.835 125.295 1.00 90.74  ? 49   VAL A N   1 
ATOM 148  C CA  . VAL A 1 185 ? 158.230 132.411 126.345 1.00 86.63  ? 49   VAL A CA  1 
ATOM 149  C C   . VAL A 1 185 ? 157.155 131.493 125.783 1.00 87.91  ? 49   VAL A C   1 
ATOM 150  O O   . VAL A 1 185 ? 156.835 130.457 126.374 1.00 92.01  ? 49   VAL A O   1 
ATOM 151  C CB  . VAL A 1 185 ? 157.619 133.640 127.041 1.00 84.30  ? 49   VAL A CB  1 
ATOM 152  C CG1 . VAL A 1 185 ? 156.308 133.280 127.697 1.00 84.57  ? 49   VAL A CG1 1 
ATOM 153  C CG2 . VAL A 1 185 ? 158.584 134.192 128.066 1.00 84.09  ? 49   VAL A CG2 1 
ATOM 154  N N   . VAL A 1 186 ? 156.581 131.852 124.634 1.00 85.65  ? 50   VAL A N   1 
ATOM 155  C CA  . VAL A 1 186 ? 155.513 131.030 124.077 1.00 86.40  ? 50   VAL A CA  1 
ATOM 156  C C   . VAL A 1 186 ? 156.041 129.663 123.664 1.00 92.67  ? 50   VAL A C   1 
ATOM 157  O O   . VAL A 1 186 ? 155.320 128.663 123.747 1.00 98.23  ? 50   VAL A O   1 
ATOM 158  C CB  . VAL A 1 186 ? 154.819 131.756 122.909 1.00 89.31  ? 50   VAL A CB  1 
ATOM 159  C CG1 . VAL A 1 186 ? 155.774 131.972 121.757 1.00 94.79  ? 50   VAL A CG1 1 
ATOM 160  C CG2 . VAL A 1 186 ? 153.602 130.975 122.450 1.00 88.68  ? 50   VAL A CG2 1 
ATOM 161  N N   . ILE A 1 187 ? 157.296 129.585 123.217 1.00 93.20  ? 51   ILE A N   1 
ATOM 162  C CA  . ILE A 1 187 ? 157.869 128.289 122.865 1.00 98.15  ? 51   ILE A CA  1 
ATOM 163  C C   . ILE A 1 187 ? 158.107 127.452 124.116 1.00 96.43  ? 51   ILE A C   1 
ATOM 164  O O   . ILE A 1 187 ? 157.792 126.257 124.147 1.00 98.44  ? 51   ILE A O   1 
ATOM 165  C CB  . ILE A 1 187 ? 159.163 128.476 122.051 1.00 97.88  ? 51   ILE A CB  1 
ATOM 166  C CG1 . ILE A 1 187 ? 158.843 129.044 120.668 1.00 94.97  ? 51   ILE A CG1 1 
ATOM 167  C CG2 . ILE A 1 187 ? 159.905 127.159 121.912 1.00 100.14 ? 51   ILE A CG2 1 
ATOM 168  C CD1 . ILE A 1 187 ? 157.976 128.138 119.827 1.00 93.75  ? 51   ILE A CD1 1 
ATOM 169  N N   . VAL A 1 188 ? 158.651 128.068 125.169 1.00 89.64  ? 52   VAL A N   1 
ATOM 170  C CA  . VAL A 1 188 ? 158.984 127.330 126.385 1.00 89.57  ? 52   VAL A CA  1 
ATOM 171  C C   . VAL A 1 188 ? 157.735 126.710 126.995 1.00 96.15  ? 52   VAL A C   1 
ATOM 172  O O   . VAL A 1 188 ? 157.722 125.530 127.362 1.00 101.51 ? 52   VAL A O   1 
ATOM 173  C CB  . VAL A 1 188 ? 159.698 128.251 127.388 1.00 88.11  ? 52   VAL A CB  1 
ATOM 174  C CG1 . VAL A 1 188 ? 159.654 127.650 128.775 1.00 92.33  ? 52   VAL A CG1 1 
ATOM 175  C CG2 . VAL A 1 188 ? 161.132 128.489 126.956 1.00 91.75  ? 52   VAL A CG2 1 
ATOM 176  N N   . ILE A 1 189 ? 156.660 127.494 127.102 1.00 97.67  ? 53   ILE A N   1 
ATOM 177  C CA  . ILE A 1 189 ? 155.421 126.996 127.690 1.00 98.04  ? 53   ILE A CA  1 
ATOM 178  C C   . ILE A 1 189 ? 154.691 126.026 126.775 1.00 97.69  ? 53   ILE A C   1 
ATOM 179  O O   . ILE A 1 189 ? 153.733 125.379 127.207 1.00 97.04  ? 53   ILE A O   1 
ATOM 180  C CB  . ILE A 1 189 ? 154.523 128.188 128.076 1.00 89.71  ? 53   ILE A CB  1 
ATOM 181  C CG1 . ILE A 1 189 ? 155.352 129.242 128.804 1.00 90.34  ? 53   ILE A CG1 1 
ATOM 182  C CG2 . ILE A 1 189 ? 153.400 127.756 128.995 1.00 84.04  ? 53   ILE A CG2 1 
ATOM 183  C CD1 . ILE A 1 189 ? 154.557 130.435 129.246 1.00 86.93  ? 53   ILE A CD1 1 
ATOM 184  N N   . TYR A 1 190 ? 155.126 125.886 125.525 1.00 97.85  ? 54   TYR A N   1 
ATOM 185  C CA  . TYR A 1 190 ? 154.499 124.949 124.604 1.00 102.91 ? 54   TYR A CA  1 
ATOM 186  C C   . TYR A 1 190 ? 155.353 123.730 124.295 1.00 108.62 ? 54   TYR A C   1 
ATOM 187  O O   . TYR A 1 190 ? 154.799 122.666 124.013 1.00 108.55 ? 54   TYR A O   1 
ATOM 188  C CB  . TYR A 1 190 ? 154.141 125.650 123.287 1.00 104.06 ? 54   TYR A CB  1 
ATOM 189  C CG  . TYR A 1 190 ? 153.119 124.911 122.452 1.00 107.37 ? 54   TYR A CG  1 
ATOM 190  C CD1 . TYR A 1 190 ? 153.511 123.989 121.491 1.00 111.69 ? 54   TYR A CD1 1 
ATOM 191  C CD2 . TYR A 1 190 ? 151.761 125.139 122.622 1.00 104.15 ? 54   TYR A CD2 1 
ATOM 192  C CE1 . TYR A 1 190 ? 152.579 123.312 120.725 1.00 115.00 ? 54   TYR A CE1 1 
ATOM 193  C CE2 . TYR A 1 190 ? 150.821 124.468 121.861 1.00 111.19 ? 54   TYR A CE2 1 
ATOM 194  C CZ  . TYR A 1 190 ? 151.236 123.555 120.914 1.00 117.41 ? 54   TYR A CZ  1 
ATOM 195  O OH  . TYR A 1 190 ? 150.305 122.884 120.154 1.00 115.79 ? 54   TYR A OH  1 
ATOM 196  N N   . PHE A 1 191 ? 156.679 123.849 124.345 1.00 109.37 ? 55   PHE A N   1 
ATOM 197  C CA  . PHE A 1 191 ? 157.565 122.749 123.985 1.00 111.07 ? 55   PHE A CA  1 
ATOM 198  C C   . PHE A 1 191 ? 158.390 122.224 125.151 1.00 111.67 ? 55   PHE A C   1 
ATOM 199  O O   . PHE A 1 191 ? 158.346 121.025 125.442 1.00 112.89 ? 55   PHE A O   1 
ATOM 200  C CB  . PHE A 1 191 ? 158.490 123.182 122.841 1.00 107.19 ? 55   PHE A CB  1 
ATOM 201  C CG  . PHE A 1 191 ? 157.781 123.352 121.532 1.00 108.41 ? 55   PHE A CG  1 
ATOM 202  C CD1 . PHE A 1 191 ? 157.170 124.549 121.211 1.00 107.84 ? 55   PHE A CD1 1 
ATOM 203  C CD2 . PHE A 1 191 ? 157.713 122.308 120.628 1.00 111.06 ? 55   PHE A CD2 1 
ATOM 204  C CE1 . PHE A 1 191 ? 156.512 124.706 120.009 1.00 110.48 ? 55   PHE A CE1 1 
ATOM 205  C CE2 . PHE A 1 191 ? 157.056 122.459 119.424 1.00 111.56 ? 55   PHE A CE2 1 
ATOM 206  C CZ  . PHE A 1 191 ? 156.454 123.659 119.115 1.00 110.57 ? 55   PHE A CZ  1 
ATOM 207  N N   . TYR A 1 192 ? 159.152 123.083 125.829 1.00 109.35 ? 56   TYR A N   1 
ATOM 208  C CA  . TYR A 1 192 ? 160.000 122.601 126.915 1.00 110.04 ? 56   TYR A CA  1 
ATOM 209  C C   . TYR A 1 192 ? 159.165 122.153 128.108 1.00 111.99 ? 56   TYR A C   1 
ATOM 210  O O   . TYR A 1 192 ? 159.362 121.054 128.640 1.00 115.19 ? 56   TYR A O   1 
ATOM 211  C CB  . TYR A 1 192 ? 161.005 123.679 127.319 1.00 107.00 ? 56   TYR A CB  1 
ATOM 212  C CG  . TYR A 1 192 ? 162.008 123.996 126.235 1.00 111.76 ? 56   TYR A CG  1 
ATOM 213  C CD1 . TYR A 1 192 ? 162.169 123.152 125.146 1.00 114.00 ? 56   TYR A CD1 1 
ATOM 214  C CD2 . TYR A 1 192 ? 162.793 125.136 126.300 1.00 114.49 ? 56   TYR A CD2 1 
ATOM 215  C CE1 . TYR A 1 192 ? 163.079 123.435 124.151 1.00 117.66 ? 56   TYR A CE1 1 
ATOM 216  C CE2 . TYR A 1 192 ? 163.708 125.428 125.309 1.00 119.30 ? 56   TYR A CE2 1 
ATOM 217  C CZ  . TYR A 1 192 ? 163.847 124.572 124.237 1.00 122.31 ? 56   TYR A CZ  1 
ATOM 218  O OH  . TYR A 1 192 ? 164.758 124.854 123.245 1.00 122.62 ? 56   TYR A OH  1 
ATOM 219  N N   . MET A 1 193 ? 158.221 122.985 128.538 1.00 108.49 ? 57   MET A N   1 
ATOM 220  C CA  . MET A 1 193 ? 157.256 122.626 129.573 1.00 106.61 ? 57   MET A CA  1 
ATOM 221  C C   . MET A 1 193 ? 155.876 122.719 128.929 1.00 106.16 ? 57   MET A C   1 
ATOM 222  O O   . MET A 1 193 ? 155.222 123.764 128.965 1.00 107.40 ? 57   MET A O   1 
ATOM 223  C CB  . MET A 1 193 ? 157.382 123.523 130.809 1.00 103.18 ? 57   MET A CB  1 
ATOM 224  C CG  . MET A 1 193 ? 157.498 125.007 130.516 1.00 106.25 ? 57   MET A CG  1 
ATOM 225  S SD  . MET A 1 193 ? 156.751 126.012 131.810 1.00 122.97 ? 57   MET A SD  1 
ATOM 226  C CE  . MET A 1 193 ? 155.075 125.388 131.782 1.00 103.14 ? 57   MET A CE  1 
ATOM 227  N N   . LYS A 1 194 ? 155.435 121.613 128.337 1.00 104.57 ? 58   LYS A N   1 
ATOM 228  C CA  . LYS A 1 194 ? 154.208 121.607 127.559 1.00 105.75 ? 58   LYS A CA  1 
ATOM 229  C C   . LYS A 1 194 ? 153.004 121.883 128.458 1.00 103.58 ? 58   LYS A C   1 
ATOM 230  O O   . LYS A 1 194 ? 153.113 122.002 129.682 1.00 102.46 ? 58   LYS A O   1 
ATOM 231  C CB  . LYS A 1 194 ? 154.064 120.279 126.822 1.00 109.29 ? 58   LYS A CB  1 
ATOM 232  C CG  . LYS A 1 194 ? 155.217 119.980 125.878 1.00 110.19 ? 58   LYS A CG  1 
ATOM 233  C CD  . LYS A 1 194 ? 155.066 118.612 125.235 1.00 113.92 ? 58   LYS A CD  1 
ATOM 234  C CE  . LYS A 1 194 ? 156.222 118.312 124.297 1.00 113.90 ? 58   LYS A CE  1 
ATOM 235  N NZ  . LYS A 1 194 ? 156.088 116.970 123.670 1.00 111.61 ? 58   LYS A NZ  1 
ATOM 236  N N   . LEU A 1 195 ? 151.832 121.981 127.834 1.00 101.50 ? 59   LEU A N   1 
ATOM 237  C CA  . LEU A 1 195 ? 150.609 122.392 128.522 1.00 99.17  ? 59   LEU A CA  1 
ATOM 238  C C   . LEU A 1 195 ? 150.134 121.247 129.411 1.00 101.19 ? 59   LEU A C   1 
ATOM 239  O O   . LEU A 1 195 ? 149.193 120.514 129.097 1.00 104.00 ? 59   LEU A O   1 
ATOM 240  C CB  . LEU A 1 195 ? 149.535 122.798 127.519 1.00 98.03  ? 59   LEU A CB  1 
ATOM 241  C CG  . LEU A 1 195 ? 149.548 124.214 126.934 1.00 94.04  ? 59   LEU A CG  1 
ATOM 242  C CD1 . LEU A 1 195 ? 150.828 124.508 126.175 1.00 99.21  ? 59   LEU A CD1 1 
ATOM 243  C CD2 . LEU A 1 195 ? 148.344 124.414 126.031 1.00 92.30  ? 59   LEU A CD2 1 
ATOM 244  N N   . LYS A 1 196 ? 150.805 121.096 130.551 1.00 99.94  ? 60   LYS A N   1 
ATOM 245  C CA  . LYS A 1 196 ? 150.463 120.072 131.527 1.00 101.05 ? 60   LYS A CA  1 
ATOM 246  C C   . LYS A 1 196 ? 149.609 120.600 132.672 1.00 98.66  ? 60   LYS A C   1 
ATOM 247  O O   . LYS A 1 196 ? 149.020 119.799 133.403 1.00 102.09 ? 60   LYS A O   1 
ATOM 248  C CB  . LYS A 1 196 ? 151.738 119.438 132.099 1.00 103.84 ? 60   LYS A CB  1 
ATOM 249  C CG  . LYS A 1 196 ? 152.688 118.890 131.047 1.00 106.11 ? 60   LYS A CG  1 
ATOM 250  C CD  . LYS A 1 196 ? 152.014 117.834 130.188 1.00 103.68 ? 60   LYS A CD  1 
ATOM 251  C CE  . LYS A 1 196 ? 152.949 117.324 129.106 1.00 102.77 ? 60   LYS A CE  1 
ATOM 252  N NZ  . LYS A 1 196 ? 154.196 116.753 129.681 1.00 100.87 ? 60   LYS A NZ  1 
ATOM 253  N N   . THR A 1 197 ? 149.521 121.918 132.838 1.00 88.91  ? 61   THR A N   1 
ATOM 254  C CA  . THR A 1 197 ? 148.765 122.525 133.920 1.00 82.37  ? 61   THR A CA  1 
ATOM 255  C C   . THR A 1 197 ? 147.901 123.649 133.369 1.00 81.38  ? 61   THR A C   1 
ATOM 256  O O   . THR A 1 197 ? 148.153 124.178 132.285 1.00 86.51  ? 61   THR A O   1 
ATOM 257  C CB  . THR A 1 197 ? 149.685 123.067 135.020 1.00 81.69  ? 61   THR A CB  1 
ATOM 258  O OG1 . THR A 1 197 ? 150.731 123.845 134.427 1.00 81.41  ? 61   THR A OG1 1 
ATOM 259  C CG2 . THR A 1 197 ? 150.299 121.928 135.813 1.00 89.27  ? 61   THR A CG2 1 
ATOM 260  N N   . VAL A 1 198 ? 146.862 123.999 134.131 1.00 78.81  ? 62   VAL A N   1 
ATOM 261  C CA  . VAL A 1 198 ? 145.969 125.084 133.733 1.00 72.24  ? 62   VAL A CA  1 
ATOM 262  C C   . VAL A 1 198 ? 146.722 126.404 133.683 1.00 70.18  ? 62   VAL A C   1 
ATOM 263  O O   . VAL A 1 198 ? 146.542 127.209 132.758 1.00 73.28  ? 62   VAL A O   1 
ATOM 264  C CB  . VAL A 1 198 ? 144.768 125.160 134.691 1.00 71.42  ? 62   VAL A CB  1 
ATOM 265  C CG1 . VAL A 1 198 ? 143.799 126.229 134.238 1.00 68.27  ? 62   VAL A CG1 1 
ATOM 266  C CG2 . VAL A 1 198 ? 144.083 123.813 134.784 1.00 81.28  ? 62   VAL A CG2 1 
ATOM 267  N N   . ALA A 1 199 ? 147.569 126.654 134.683 1.00 68.64  ? 63   ALA A N   1 
ATOM 268  C CA  . ALA A 1 199 ? 148.335 127.892 134.709 1.00 64.23  ? 63   ALA A CA  1 
ATOM 269  C C   . ALA A 1 199 ? 149.260 128.001 133.509 1.00 67.62  ? 63   ALA A C   1 
ATOM 270  O O   . ALA A 1 199 ? 149.526 129.108 133.037 1.00 72.03  ? 63   ALA A O   1 
ATOM 271  C CB  . ALA A 1 199 ? 149.131 127.990 136.007 1.00 64.76  ? 63   ALA A CB  1 
ATOM 272  N N   . SER A 1 200 ? 149.753 126.874 132.995 1.00 67.84  ? 64   SER A N   1 
ATOM 273  C CA  . SER A 1 200 ? 150.542 126.917 131.768 1.00 67.19  ? 64   SER A CA  1 
ATOM 274  C C   . SER A 1 200 ? 149.699 127.385 130.590 1.00 64.88  ? 64   SER A C   1 
ATOM 275  O O   . SER A 1 200 ? 150.169 128.168 129.759 1.00 69.10  ? 64   SER A O   1 
ATOM 276  C CB  . SER A 1 200 ? 151.148 125.547 131.480 1.00 79.80  ? 64   SER A CB  1 
ATOM 277  O OG  . SER A 1 200 ? 150.145 124.619 131.108 1.00 84.81  ? 64   SER A OG  1 
ATOM 278  N N   . VAL A 1 201 ? 148.450 126.925 130.507 1.00 63.92  ? 65   VAL A N   1 
ATOM 279  C CA  . VAL A 1 201 ? 147.553 127.373 129.444 1.00 66.14  ? 65   VAL A CA  1 
ATOM 280  C C   . VAL A 1 201 ? 147.298 128.871 129.559 1.00 65.02  ? 65   VAL A C   1 
ATOM 281  O O   . VAL A 1 201 ? 147.333 129.608 128.564 1.00 64.79  ? 65   VAL A O   1 
ATOM 282  C CB  . VAL A 1 201 ? 146.239 126.576 129.484 1.00 66.32  ? 65   VAL A CB  1 
ATOM 283  C CG1 . VAL A 1 201 ? 145.236 127.162 128.518 1.00 64.72  ? 65   VAL A CG1 1 
ATOM 284  C CG2 . VAL A 1 201 ? 146.500 125.122 129.159 1.00 77.97  ? 65   VAL A CG2 1 
ATOM 285  N N   . PHE A 1 202 ? 147.037 129.344 130.777 1.00 64.76  ? 66   PHE A N   1 
ATOM 286  C CA  . PHE A 1 202 ? 146.757 130.764 130.962 1.00 57.68  ? 66   PHE A CA  1 
ATOM 287  C C   . PHE A 1 202 ? 147.984 131.623 130.676 1.00 57.97  ? 66   PHE A C   1 
ATOM 288  O O   . PHE A 1 202 ? 147.860 132.708 130.103 1.00 64.92  ? 66   PHE A O   1 
ATOM 289  C CB  . PHE A 1 202 ? 146.231 131.015 132.370 1.00 55.81  ? 66   PHE A CB  1 
ATOM 290  C CG  . PHE A 1 202 ? 144.803 130.607 132.557 1.00 58.71  ? 66   PHE A CG  1 
ATOM 291  C CD1 . PHE A 1 202 ? 143.883 130.788 131.545 1.00 58.44  ? 66   PHE A CD1 1 
ATOM 292  C CD2 . PHE A 1 202 ? 144.381 130.035 133.740 1.00 60.60  ? 66   PHE A CD2 1 
ATOM 293  C CE1 . PHE A 1 202 ? 142.571 130.415 131.712 1.00 63.84  ? 66   PHE A CE1 1 
ATOM 294  C CE2 . PHE A 1 202 ? 143.069 129.659 133.910 1.00 61.44  ? 66   PHE A CE2 1 
ATOM 295  C CZ  . PHE A 1 202 ? 142.164 129.849 132.894 1.00 65.94  ? 66   PHE A CZ  1 
ATOM 296  N N   . LEU A 1 203 ? 149.176 131.161 131.058 1.00 55.60  ? 67   LEU A N   1 
ATOM 297  C CA  . LEU A 1 203 ? 150.386 131.913 130.743 1.00 57.09  ? 67   LEU A CA  1 
ATOM 298  C C   . LEU A 1 203 ? 150.684 131.900 129.249 1.00 60.62  ? 67   LEU A C   1 
ATOM 299  O O   . LEU A 1 203 ? 151.177 132.897 128.708 1.00 63.21  ? 67   LEU A O   1 
ATOM 300  C CB  . LEU A 1 203 ? 151.573 131.360 131.528 1.00 59.69  ? 67   LEU A CB  1 
ATOM 301  C CG  . LEU A 1 203 ? 151.575 131.618 133.035 1.00 61.85  ? 67   LEU A CG  1 
ATOM 302  C CD1 . LEU A 1 203 ? 152.748 130.924 133.690 1.00 63.34  ? 67   LEU A CD1 1 
ATOM 303  C CD2 . LEU A 1 203 ? 151.610 133.103 133.330 1.00 64.29  ? 67   LEU A CD2 1 
ATOM 304  N N   . LEU A 1 204 ? 150.388 130.794 128.565 1.00 62.33  ? 68   LEU A N   1 
ATOM 305  C CA  . LEU A 1 204 ? 150.512 130.764 127.113 1.00 63.41  ? 68   LEU A CA  1 
ATOM 306  C C   . LEU A 1 204 ? 149.588 131.788 126.469 1.00 66.22  ? 68   LEU A C   1 
ATOM 307  O O   . LEU A 1 204 ? 149.996 132.537 125.573 1.00 69.63  ? 68   LEU A O   1 
ATOM 308  C CB  . LEU A 1 204 ? 150.198 129.361 126.598 1.00 66.30  ? 68   LEU A CB  1 
ATOM 309  C CG  . LEU A 1 204 ? 150.219 129.167 125.084 1.00 69.05  ? 68   LEU A CG  1 
ATOM 310  C CD1 . LEU A 1 204 ? 151.628 128.852 124.618 1.00 77.86  ? 68   LEU A CD1 1 
ATOM 311  C CD2 . LEU A 1 204 ? 149.245 128.081 124.665 1.00 71.44  ? 68   LEU A CD2 1 
ATOM 312  N N   . ASN A 1 205 ? 148.334 131.838 126.923 1.00 63.20  ? 69   ASN A N   1 
ATOM 313  C CA  . ASN A 1 205 ? 147.394 132.818 126.387 1.00 59.20  ? 69   ASN A CA  1 
ATOM 314  C C   . ASN A 1 205 ? 147.843 134.240 126.691 1.00 60.96  ? 69   ASN A C   1 
ATOM 315  O O   . ASN A 1 205 ? 147.677 135.140 125.861 1.00 69.00  ? 69   ASN A O   1 
ATOM 316  C CB  . ASN A 1 205 ? 145.999 132.568 126.948 1.00 59.00  ? 69   ASN A CB  1 
ATOM 317  C CG  . ASN A 1 205 ? 145.284 131.447 126.236 1.00 62.90  ? 69   ASN A CG  1 
ATOM 318  O OD1 . ASN A 1 205 ? 145.528 130.273 126.501 1.00 64.05  ? 69   ASN A OD1 1 
ATOM 319  N ND2 . ASN A 1 205 ? 144.390 131.803 125.326 1.00 67.86  ? 69   ASN A ND2 1 
ATOM 320  N N   . LEU A 1 206 ? 148.398 134.468 127.881 1.00 56.81  ? 70   LEU A N   1 
ATOM 321  C CA  . LEU A 1 206 ? 148.891 135.796 128.227 1.00 54.90  ? 70   LEU A CA  1 
ATOM 322  C C   . LEU A 1 206 ? 150.037 136.212 127.316 1.00 60.90  ? 70   LEU A C   1 
ATOM 323  O O   . LEU A 1 206 ? 150.088 137.358 126.850 1.00 66.54  ? 70   LEU A O   1 
ATOM 324  C CB  . LEU A 1 206 ? 149.331 135.818 129.688 1.00 52.67  ? 70   LEU A CB  1 
ATOM 325  C CG  . LEU A 1 206 ? 149.620 137.179 130.308 1.00 53.39  ? 70   LEU A CG  1 
ATOM 326  C CD1 . LEU A 1 206 ? 148.367 138.014 130.314 1.00 53.25  ? 70   LEU A CD1 1 
ATOM 327  C CD2 . LEU A 1 206 ? 150.145 137.002 131.712 1.00 56.07  ? 70   LEU A CD2 1 
ATOM 328  N N   . ALA A 1 207 ? 150.964 135.294 127.045 1.00 60.88  ? 71   ALA A N   1 
ATOM 329  C CA  . ALA A 1 207 ? 152.059 135.603 126.133 1.00 63.04  ? 71   ALA A CA  1 
ATOM 330  C C   . ALA A 1 207 ? 151.544 135.861 124.723 1.00 69.08  ? 71   ALA A C   1 
ATOM 331  O O   . ALA A 1 207 ? 152.051 136.746 124.026 1.00 75.04  ? 71   ALA A O   1 
ATOM 332  C CB  . ALA A 1 207 ? 153.083 134.472 126.134 1.00 69.52  ? 71   ALA A CB  1 
ATOM 333  N N   . LEU A 1 208 ? 150.538 135.100 124.285 1.00 66.92  ? 72   LEU A N   1 
ATOM 334  C CA  . LEU A 1 208 ? 149.958 135.338 122.967 1.00 67.95  ? 72   LEU A CA  1 
ATOM 335  C C   . LEU A 1 208 ? 149.291 136.706 122.889 1.00 69.67  ? 72   LEU A C   1 
ATOM 336  O O   . LEU A 1 208 ? 149.412 137.404 121.878 1.00 75.25  ? 72   LEU A O   1 
ATOM 337  C CB  . LEU A 1 208 ? 148.958 134.237 122.622 1.00 67.15  ? 72   LEU A CB  1 
ATOM 338  C CG  . LEU A 1 208 ? 149.553 132.862 122.333 1.00 71.64  ? 72   LEU A CG  1 
ATOM 339  C CD1 . LEU A 1 208 ? 148.465 131.876 121.944 1.00 70.54  ? 72   LEU A CD1 1 
ATOM 340  C CD2 . LEU A 1 208 ? 150.595 132.969 121.242 1.00 74.35  ? 72   LEU A CD2 1 
ATOM 341  N N   . ALA A 1 209 ? 148.575 137.105 123.942 1.00 66.16  ? 73   ALA A N   1 
ATOM 342  C CA  . ALA A 1 209 ? 147.945 138.422 123.950 1.00 64.03  ? 73   ALA A CA  1 
ATOM 343  C C   . ALA A 1 209 ? 148.988 139.532 123.923 1.00 66.97  ? 73   ALA A C   1 
ATOM 344  O O   . ALA A 1 209 ? 148.825 140.537 123.216 1.00 75.24  ? 73   ALA A O   1 
ATOM 345  C CB  . ALA A 1 209 ? 147.042 138.569 125.172 1.00 61.31  ? 73   ALA A CB  1 
ATOM 346  N N   . ASP A 1 210 ? 150.066 139.373 124.692 1.00 63.90  ? 74   ASP A N   1 
ATOM 347  C CA  . ASP A 1 210 ? 151.128 140.372 124.664 1.00 65.31  ? 74   ASP A CA  1 
ATOM 348  C C   . ASP A 1 210 ? 151.788 140.439 123.292 1.00 69.33  ? 74   ASP A C   1 
ATOM 349  O O   . ASP A 1 210 ? 152.128 141.526 122.819 1.00 74.17  ? 74   ASP A O   1 
ATOM 350  C CB  . ASP A 1 210 ? 152.159 140.083 125.752 1.00 71.41  ? 74   ASP A CB  1 
ATOM 351  C CG  . ASP A 1 210 ? 151.571 140.176 127.147 1.00 74.15  ? 74   ASP A CG  1 
ATOM 352  O OD1 . ASP A 1 210 ? 150.344 140.369 127.266 1.00 70.09  ? 74   ASP A OD1 1 
ATOM 353  O OD2 . ASP A 1 210 ? 152.336 140.054 128.126 1.00 78.13  ? 74   ASP A OD2 1 
ATOM 354  N N   . LEU A 1 211 ? 151.974 139.291 122.636 1.00 67.90  ? 75   LEU A N   1 
ATOM 355  C CA  . LEU A 1 211 ? 152.499 139.300 121.273 1.00 69.59  ? 75   LEU A CA  1 
ATOM 356  C C   . LEU A 1 211 ? 151.553 140.016 120.320 1.00 73.35  ? 75   LEU A C   1 
ATOM 357  O O   . LEU A 1 211 ? 151.994 140.775 119.449 1.00 79.44  ? 75   LEU A O   1 
ATOM 358  C CB  . LEU A 1 211 ? 152.746 137.874 120.788 1.00 71.60  ? 75   LEU A CB  1 
ATOM 359  C CG  . LEU A 1 211 ? 154.085 137.231 121.134 1.00 83.69  ? 75   LEU A CG  1 
ATOM 360  C CD1 . LEU A 1 211 ? 154.157 135.832 120.549 1.00 84.74  ? 75   LEU A CD1 1 
ATOM 361  C CD2 . LEU A 1 211 ? 155.224 138.088 120.620 1.00 87.59  ? 75   LEU A CD2 1 
ATOM 362  N N   . CYS A 1 212 ? 150.249 139.776 120.462 1.00 71.13  ? 76   CYS A N   1 
ATOM 363  C CA  . CYS A 1 212 ? 149.279 140.434 119.594 1.00 70.78  ? 76   CYS A CA  1 
ATOM 364  C C   . CYS A 1 212 ? 149.334 141.944 119.761 1.00 72.26  ? 76   CYS A C   1 
ATOM 365  O O   . CYS A 1 212 ? 149.260 142.687 118.776 1.00 76.15  ? 76   CYS A O   1 
ATOM 366  C CB  . CYS A 1 212 ? 147.872 139.915 119.882 1.00 69.50  ? 76   CYS A CB  1 
ATOM 367  S SG  . CYS A 1 212 ? 147.574 138.220 119.338 1.00 89.66  ? 76   CYS A SG  1 
ATOM 368  N N   . PHE A 1 213 ? 149.460 142.421 121.000 1.00 72.21  ? 77   PHE A N   1 
ATOM 369  C CA  . PHE A 1 213 ? 149.589 143.861 121.204 1.00 67.18  ? 77   PHE A CA  1 
ATOM 370  C C   . PHE A 1 213 ? 150.906 144.392 120.649 1.00 76.02  ? 77   PHE A C   1 
ATOM 371  O O   . PHE A 1 213 ? 150.940 145.456 120.016 1.00 81.92  ? 77   PHE A O   1 
ATOM 372  C CB  . PHE A 1 213 ? 149.469 144.211 122.680 1.00 61.04  ? 77   PHE A CB  1 
ATOM 373  C CG  . PHE A 1 213 ? 149.878 145.611 122.984 1.00 65.45  ? 77   PHE A CG  1 
ATOM 374  C CD1 . PHE A 1 213 ? 149.078 146.670 122.611 1.00 71.31  ? 77   PHE A CD1 1 
ATOM 375  C CD2 . PHE A 1 213 ? 151.072 145.873 123.621 1.00 73.42  ? 77   PHE A CD2 1 
ATOM 376  C CE1 . PHE A 1 213 ? 149.454 147.966 122.877 1.00 76.46  ? 77   PHE A CE1 1 
ATOM 377  C CE2 . PHE A 1 213 ? 151.453 147.167 123.889 1.00 78.01  ? 77   PHE A CE2 1 
ATOM 378  C CZ  . PHE A 1 213 ? 150.646 148.215 123.512 1.00 76.01  ? 77   PHE A CZ  1 
ATOM 379  N N   . LEU A 1 214 ? 152.006 143.677 120.885 1.00 77.23  ? 78   LEU A N   1 
ATOM 380  C CA  . LEU A 1 214 ? 153.302 144.135 120.404 1.00 80.45  ? 78   LEU A CA  1 
ATOM 381  C C   . LEU A 1 214 ? 153.386 144.145 118.887 1.00 82.57  ? 78   LEU A C   1 
ATOM 382  O O   . LEU A 1 214 ? 154.226 144.859 118.335 1.00 85.90  ? 78   LEU A O   1 
ATOM 383  C CB  . LEU A 1 214 ? 154.413 143.263 120.980 1.00 80.59  ? 78   LEU A CB  1 
ATOM 384  C CG  . LEU A 1 214 ? 154.655 143.422 122.476 1.00 79.01  ? 78   LEU A CG  1 
ATOM 385  C CD1 . LEU A 1 214 ? 155.599 142.350 122.963 1.00 84.33  ? 78   LEU A CD1 1 
ATOM 386  C CD2 . LEU A 1 214 ? 155.209 144.797 122.771 1.00 83.06  ? 78   LEU A CD2 1 
ATOM 387  N N   . LEU A 1 215 ? 152.555 143.358 118.204 1.00 78.53  ? 79   LEU A N   1 
ATOM 388  C CA  . LEU A 1 215 ? 152.528 143.425 116.747 1.00 80.48  ? 79   LEU A CA  1 
ATOM 389  C C   . LEU A 1 215 ? 152.088 144.803 116.270 1.00 87.07  ? 79   LEU A C   1 
ATOM 390  O O   . LEU A 1 215 ? 152.650 145.346 115.312 1.00 91.44  ? 79   LEU A O   1 
ATOM 391  C CB  . LEU A 1 215 ? 151.608 142.345 116.179 1.00 80.92  ? 79   LEU A CB  1 
ATOM 392  C CG  . LEU A 1 215 ? 152.112 140.904 116.245 1.00 82.60  ? 79   LEU A CG  1 
ATOM 393  C CD1 . LEU A 1 215 ? 151.200 139.982 115.453 1.00 75.54  ? 79   LEU A CD1 1 
ATOM 394  C CD2 . LEU A 1 215 ? 153.541 140.814 115.744 1.00 81.88  ? 79   LEU A CD2 1 
ATOM 395  N N   . THR A 1 216 ? 151.082 145.383 116.924 1.00 88.89  ? 80   THR A N   1 
ATOM 396  C CA  . THR A 1 216 ? 150.577 146.701 116.564 1.00 88.53  ? 80   THR A CA  1 
ATOM 397  C C   . THR A 1 216 ? 151.301 147.833 117.278 1.00 89.62  ? 80   THR A C   1 
ATOM 398  O O   . THR A 1 216 ? 151.067 149.000 116.948 1.00 91.39  ? 80   THR A O   1 
ATOM 399  C CB  . THR A 1 216 ? 149.081 146.798 116.871 1.00 79.41  ? 80   THR A CB  1 
ATOM 400  O OG1 . THR A 1 216 ? 148.891 146.949 118.282 1.00 78.54  ? 80   THR A OG1 1 
ATOM 401  C CG2 . THR A 1 216 ? 148.367 145.541 116.400 1.00 75.61  ? 80   THR A CG2 1 
ATOM 402  N N   . LEU A 1 217 ? 152.147 147.519 118.255 1.00 89.07  ? 81   LEU A N   1 
ATOM 403  C CA  . LEU A 1 217 ? 152.922 148.565 118.919 1.00 91.20  ? 81   LEU A CA  1 
ATOM 404  C C   . LEU A 1 217 ? 153.795 149.398 117.978 1.00 95.60  ? 81   LEU A C   1 
ATOM 405  O O   . LEU A 1 217 ? 153.821 150.630 118.148 1.00 99.57  ? 81   LEU A O   1 
ATOM 406  C CB  . LEU A 1 217 ? 153.770 147.944 120.036 1.00 89.09  ? 81   LEU A CB  1 
ATOM 407  C CG  . LEU A 1 217 ? 154.445 148.926 120.995 1.00 95.30  ? 81   LEU A CG  1 
ATOM 408  C CD1 . LEU A 1 217 ? 154.411 148.387 122.413 1.00 92.09  ? 81   LEU A CD1 1 
ATOM 409  C CD2 . LEU A 1 217 ? 155.876 149.203 120.571 1.00 100.13 ? 81   LEU A CD2 1 
ATOM 410  N N   . PRO A 1 218 ? 154.540 148.830 117.019 1.00 96.08  ? 82   PRO A N   1 
ATOM 411  C CA  . PRO A 1 218 ? 155.374 149.689 116.161 1.00 97.05  ? 82   PRO A CA  1 
ATOM 412  C C   . PRO A 1 218 ? 154.578 150.691 115.347 1.00 97.22  ? 82   PRO A C   1 
ATOM 413  O O   . PRO A 1 218 ? 155.119 151.740 114.976 1.00 96.05  ? 82   PRO A O   1 
ATOM 414  C CB  . PRO A 1 218 ? 156.108 148.684 115.260 1.00 96.45  ? 82   PRO A CB  1 
ATOM 415  C CG  . PRO A 1 218 ? 155.250 147.481 115.264 1.00 95.47  ? 82   PRO A CG  1 
ATOM 416  C CD  . PRO A 1 218 ? 154.697 147.412 116.654 1.00 94.71  ? 82   PRO A CD  1 
ATOM 417  N N   . LEU A 1 219 ? 153.308 150.405 115.058 1.00 97.49  ? 83   LEU A N   1 
ATOM 418  C CA  . LEU A 1 219 ? 152.456 151.408 114.429 1.00 94.92  ? 83   LEU A CA  1 
ATOM 419  C C   . LEU A 1 219 ? 152.342 152.641 115.313 1.00 96.97  ? 83   LEU A C   1 
ATOM 420  O O   . LEU A 1 219 ? 152.521 153.772 114.848 1.00 99.76  ? 83   LEU A O   1 
ATOM 421  C CB  . LEU A 1 219 ? 151.073 150.823 114.137 1.00 91.14  ? 83   LEU A CB  1 
ATOM 422  C CG  . LEU A 1 219 ? 150.875 150.054 112.829 1.00 92.35  ? 83   LEU A CG  1 
ATOM 423  C CD1 . LEU A 1 219 ? 151.754 148.816 112.759 1.00 91.17  ? 83   LEU A CD1 1 
ATOM 424  C CD2 . LEU A 1 219 ? 149.415 149.678 112.657 1.00 90.14  ? 83   LEU A CD2 1 
ATOM 425  N N   . TRP A 1 220 ? 152.072 152.438 116.603 1.00 96.40  ? 84   TRP A N   1 
ATOM 426  C CA  . TRP A 1 220 ? 152.020 153.560 117.532 1.00 96.46  ? 84   TRP A CA  1 
ATOM 427  C C   . TRP A 1 220 ? 153.375 154.240 117.650 1.00 100.54 ? 84   TRP A C   1 
ATOM 428  O O   . TRP A 1 220 ? 153.454 155.469 117.757 1.00 104.33 ? 84   TRP A O   1 
ATOM 429  C CB  . TRP A 1 220 ? 151.541 153.092 118.905 1.00 98.05  ? 84   TRP A CB  1 
ATOM 430  C CG  . TRP A 1 220 ? 150.092 152.710 118.966 1.00 100.03 ? 84   TRP A CG  1 
ATOM 431  C CD1 . TRP A 1 220 ? 149.573 151.560 119.482 1.00 96.58  ? 84   TRP A CD1 1 
ATOM 432  C CD2 . TRP A 1 220 ? 148.974 153.482 118.505 1.00 101.44 ? 84   TRP A CD2 1 
ATOM 433  N NE1 . TRP A 1 220 ? 148.204 151.567 119.370 1.00 97.46  ? 84   TRP A NE1 1 
ATOM 434  C CE2 . TRP A 1 220 ? 147.813 152.736 118.773 1.00 98.80  ? 84   TRP A CE2 1 
ATOM 435  C CE3 . TRP A 1 220 ? 148.844 154.732 117.890 1.00 99.95  ? 84   TRP A CE3 1 
ATOM 436  C CZ2 . TRP A 1 220 ? 146.538 153.198 118.452 1.00 94.61  ? 84   TRP A CZ2 1 
ATOM 437  C CZ3 . TRP A 1 220 ? 147.580 155.184 117.568 1.00 99.78  ? 84   TRP A CZ3 1 
ATOM 438  C CH2 . TRP A 1 220 ? 146.444 154.420 117.848 1.00 96.56  ? 84   TRP A CH2 1 
ATOM 439  N N   . ALA A 1 221 ? 154.454 153.456 117.644 1.00 102.57 ? 85   ALA A N   1 
ATOM 440  C CA  . ALA A 1 221 ? 155.791 154.035 117.746 1.00 105.69 ? 85   ALA A CA  1 
ATOM 441  C C   . ALA A 1 221 ? 156.072 154.979 116.583 1.00 108.07 ? 85   ALA A C   1 
ATOM 442  O O   . ALA A 1 221 ? 156.519 156.115 116.781 1.00 110.06 ? 85   ALA A O   1 
ATOM 443  C CB  . ALA A 1 221 ? 156.838 152.924 117.799 1.00 104.82 ? 85   ALA A CB  1 
ATOM 444  N N   . VAL A 1 222 ? 155.802 154.527 115.357 1.00 106.50 ? 86   VAL A N   1 
ATOM 445  C CA  . VAL A 1 222 ? 156.089 155.349 114.188 1.00 105.70 ? 86   VAL A CA  1 
ATOM 446  C C   . VAL A 1 222 ? 155.099 156.504 114.084 1.00 104.98 ? 86   VAL A C   1 
ATOM 447  O O   . VAL A 1 222 ? 155.431 157.566 113.546 1.00 108.21 ? 86   VAL A O   1 
ATOM 448  C CB  . VAL A 1 222 ? 156.104 154.480 112.914 1.00 106.01 ? 86   VAL A CB  1 
ATOM 449  C CG1 . VAL A 1 222 ? 154.699 154.062 112.516 1.00 103.74 ? 86   VAL A CG1 1 
ATOM 450  C CG2 . VAL A 1 222 ? 156.797 155.208 111.778 1.00 106.76 ? 86   VAL A CG2 1 
ATOM 451  N N   . TYR A 1 223 ? 153.881 156.328 114.600 1.00 104.03 ? 87   TYR A N   1 
ATOM 452  C CA  . TYR A 1 223 ? 152.913 157.418 114.611 1.00 104.49 ? 87   TYR A CA  1 
ATOM 453  C C   . TYR A 1 223 ? 153.331 158.521 115.575 1.00 106.33 ? 87   TYR A C   1 
ATOM 454  O O   . TYR A 1 223 ? 153.140 159.708 115.290 1.00 108.95 ? 87   TYR A O   1 
ATOM 455  C CB  . TYR A 1 223 ? 151.534 156.868 114.968 1.00 105.04 ? 87   TYR A CB  1 
ATOM 456  C CG  . TYR A 1 223 ? 150.566 157.870 115.545 1.00 102.02 ? 87   TYR A CG  1 
ATOM 457  C CD1 . TYR A 1 223 ? 150.025 158.876 114.761 1.00 101.80 ? 87   TYR A CD1 1 
ATOM 458  C CD2 . TYR A 1 223 ? 150.171 157.790 116.871 1.00 103.92 ? 87   TYR A CD2 1 
ATOM 459  C CE1 . TYR A 1 223 ? 149.132 159.784 115.287 1.00 103.71 ? 87   TYR A CE1 1 
ATOM 460  C CE2 . TYR A 1 223 ? 149.279 158.691 117.405 1.00 106.43 ? 87   TYR A CE2 1 
ATOM 461  C CZ  . TYR A 1 223 ? 148.762 159.686 116.610 1.00 106.36 ? 87   TYR A CZ  1 
ATOM 462  O OH  . TYR A 1 223 ? 147.871 160.588 117.142 1.00 108.35 ? 87   TYR A OH  1 
ATOM 463  N N   . THR A 1 224 ? 153.891 158.149 116.726 1.00 108.35 ? 88   THR A N   1 
ATOM 464  C CA  . THR A 1 224 ? 154.415 159.135 117.661 1.00 109.67 ? 88   THR A CA  1 
ATOM 465  C C   . THR A 1 224 ? 155.745 159.718 117.205 1.00 111.93 ? 88   THR A C   1 
ATOM 466  O O   . THR A 1 224 ? 156.092 160.831 117.614 1.00 113.52 ? 88   THR A O   1 
ATOM 467  C CB  . THR A 1 224 ? 154.580 158.512 119.048 1.00 111.34 ? 88   THR A CB  1 
ATOM 468  O OG1 . THR A 1 224 ? 153.475 157.642 119.313 1.00 113.81 ? 88   THR A OG1 1 
ATOM 469  C CG2 . THR A 1 224 ? 154.622 159.593 120.116 1.00 112.94 ? 88   THR A CG2 1 
ATOM 470  N N   . ALA A 1 225 ? 156.490 158.995 116.367 1.00 113.39 ? 89   ALA A N   1 
ATOM 471  C CA  . ALA A 1 225 ? 157.784 159.490 115.910 1.00 115.08 ? 89   ALA A CA  1 
ATOM 472  C C   . ALA A 1 225 ? 157.635 160.751 115.070 1.00 116.53 ? 89   ALA A C   1 
ATOM 473  O O   . ALA A 1 225 ? 158.472 161.657 115.144 1.00 118.71 ? 89   ALA A O   1 
ATOM 474  C CB  . ALA A 1 225 ? 158.514 158.404 115.121 1.00 111.43 ? 89   ALA A CB  1 
ATOM 475  N N   . MET A 1 226 ? 156.575 160.831 114.264 1.00 114.50 ? 90   MET A N   1 
ATOM 476  C CA  . MET A 1 226 ? 156.373 161.961 113.365 1.00 115.44 ? 90   MET A CA  1 
ATOM 477  C C   . MET A 1 226 ? 155.488 163.043 113.966 1.00 117.44 ? 90   MET A C   1 
ATOM 478  O O   . MET A 1 226 ? 154.756 163.714 113.228 1.00 117.23 ? 90   MET A O   1 
ATOM 479  C CB  . MET A 1 226 ? 155.799 161.482 112.032 1.00 112.93 ? 90   MET A CB  1 
ATOM 480  C CG  . MET A 1 226 ? 156.854 160.979 111.060 1.00 115.43 ? 90   MET A CG  1 
ATOM 481  S SD  . MET A 1 226 ? 157.292 159.255 111.320 1.00 122.51 ? 90   MET A SD  1 
ATOM 482  C CE  . MET A 1 226 ? 155.922 158.460 110.495 1.00 113.88 ? 90   MET A CE  1 
ATOM 483  N N   . GLU A 1 227 ? 155.538 163.229 115.286 1.00 118.36 ? 91   GLU A N   1 
ATOM 484  C CA  . GLU A 1 227 ? 154.799 164.291 115.969 1.00 117.76 ? 91   GLU A CA  1 
ATOM 485  C C   . GLU A 1 227 ? 153.291 164.104 115.806 1.00 115.63 ? 91   GLU A C   1 
ATOM 486  O O   . GLU A 1 227 ? 152.557 165.034 115.466 1.00 116.67 ? 91   GLU A O   1 
ATOM 487  C CB  . GLU A 1 227 ? 155.244 165.672 115.481 1.00 120.82 ? 91   GLU A CB  1 
ATOM 488  C CG  . GLU A 1 227 ? 156.729 165.939 115.667 1.00 122.85 ? 91   GLU A CG  1 
ATOM 489  C CD  . GLU A 1 227 ? 157.219 167.127 114.862 1.00 124.19 ? 91   GLU A CD  1 
ATOM 490  O OE1 . GLU A 1 227 ? 156.573 167.471 113.851 1.00 121.98 ? 91   GLU A OE1 1 
ATOM 491  O OE2 . GLU A 1 227 ? 158.252 167.716 115.242 1.00 122.41 ? 91   GLU A OE2 1 
ATOM 492  N N   . TYR A 1 228 ? 152.836 162.874 116.049 1.00 114.26 ? 92   TYR A N   1 
ATOM 493  C CA  . TYR A 1 228 ? 151.416 162.522 116.053 1.00 111.53 ? 92   TYR A CA  1 
ATOM 494  C C   . TYR A 1 228 ? 150.752 162.814 114.704 1.00 109.57 ? 92   TYR A C   1 
ATOM 495  O O   . TYR A 1 228 ? 149.861 163.657 114.585 1.00 107.42 ? 92   TYR A O   1 
ATOM 496  C CB  . TYR A 1 228 ? 150.682 163.231 117.196 1.00 111.87 ? 92   TYR A CB  1 
ATOM 497  C CG  . TYR A 1 228 ? 150.973 162.650 118.561 1.00 112.78 ? 92   TYR A CG  1 
ATOM 498  C CD1 . TYR A 1 228 ? 150.278 161.543 119.025 1.00 112.84 ? 92   TYR A CD1 1 
ATOM 499  C CD2 . TYR A 1 228 ? 151.941 163.208 119.386 1.00 113.99 ? 92   TYR A CD2 1 
ATOM 500  C CE1 . TYR A 1 228 ? 150.537 161.007 120.269 1.00 111.44 ? 92   TYR A CE1 1 
ATOM 501  C CE2 . TYR A 1 228 ? 152.206 162.679 120.634 1.00 114.86 ? 92   TYR A CE2 1 
ATOM 502  C CZ  . TYR A 1 228 ? 151.500 161.579 121.069 1.00 113.38 ? 92   TYR A CZ  1 
ATOM 503  O OH  . TYR A 1 228 ? 151.758 161.044 122.308 1.00 114.80 ? 92   TYR A OH  1 
ATOM 504  N N   . ARG A 1 229 ? 151.207 162.094 113.681 1.00 108.25 ? 93   ARG A N   1 
ATOM 505  C CA  . ARG A 1 229 ? 150.522 162.065 112.397 1.00 106.50 ? 93   ARG A CA  1 
ATOM 506  C C   . ARG A 1 229 ? 150.566 160.647 111.847 1.00 103.74 ? 93   ARG A C   1 
ATOM 507  O O   . ARG A 1 229 ? 151.598 159.975 111.917 1.00 107.09 ? 93   ARG A O   1 
ATOM 508  C CB  . ARG A 1 229 ? 151.126 163.062 111.400 1.00 110.17 ? 93   ARG A CB  1 
ATOM 509  C CG  . ARG A 1 229 ? 152.608 162.907 111.146 1.00 113.81 ? 93   ARG A CG  1 
ATOM 510  C CD  . ARG A 1 229 ? 153.158 164.138 110.442 1.00 117.32 ? 93   ARG A CD  1 
ATOM 511  N NE  . ARG A 1 229 ? 152.930 165.348 111.224 1.00 120.48 ? 93   ARG A NE  1 
ATOM 512  C CZ  . ARG A 1 229 ? 153.170 166.578 110.793 1.00 119.58 ? 93   ARG A CZ  1 
ATOM 513  N NH1 . ARG A 1 229 ? 153.646 166.805 109.580 1.00 117.35 ? 93   ARG A NH1 1 
ATOM 514  N NH2 . ARG A 1 229 ? 152.923 167.607 111.598 1.00 118.20 ? 93   ARG A NH2 1 
ATOM 515  N N   . TRP A 1 230 ? 149.435 160.200 111.300 1.00 100.63 ? 94   TRP A N   1 
ATOM 516  C CA  . TRP A 1 230 ? 149.224 158.800 110.968 1.00 98.68  ? 94   TRP A CA  1 
ATOM 517  C C   . TRP A 1 230 ? 149.427 158.579 109.479 1.00 100.85 ? 94   TRP A C   1 
ATOM 518  O O   . TRP A 1 230 ? 148.594 159.029 108.678 1.00 105.25 ? 94   TRP A O   1 
ATOM 519  C CB  . TRP A 1 230 ? 147.817 158.379 111.380 1.00 98.63  ? 94   TRP A CB  1 
ATOM 520  C CG  . TRP A 1 230 ? 147.546 156.921 111.307 1.00 96.35  ? 94   TRP A CG  1 
ATOM 521  C CD1 . TRP A 1 230 ? 146.913 156.257 110.303 1.00 95.72  ? 94   TRP A CD1 1 
ATOM 522  C CD2 . TRP A 1 230 ? 147.874 155.941 112.294 1.00 95.15  ? 94   TRP A CD2 1 
ATOM 523  N NE1 . TRP A 1 230 ? 146.833 154.920 110.597 1.00 93.76  ? 94   TRP A NE1 1 
ATOM 524  C CE2 . TRP A 1 230 ? 147.417 154.700 111.816 1.00 94.44  ? 94   TRP A CE2 1 
ATOM 525  C CE3 . TRP A 1 230 ? 148.514 155.991 113.533 1.00 95.52  ? 94   TRP A CE3 1 
ATOM 526  C CZ2 . TRP A 1 230 ? 147.581 153.519 112.532 1.00 94.01  ? 94   TRP A CZ2 1 
ATOM 527  C CZ3 . TRP A 1 230 ? 148.676 154.819 114.243 1.00 97.51  ? 94   TRP A CZ3 1 
ATOM 528  C CH2 . TRP A 1 230 ? 148.211 153.599 113.742 1.00 96.15  ? 94   TRP A CH2 1 
ATOM 529  N N   . PRO A 1 231 ? 150.496 157.898 109.056 1.00 101.72 ? 95   PRO A N   1 
ATOM 530  C CA  . PRO A 1 231 ? 150.695 157.649 107.622 1.00 101.76 ? 95   PRO A CA  1 
ATOM 531  C C   . PRO A 1 231 ? 149.853 156.519 107.060 1.00 98.52  ? 95   PRO A C   1 
ATOM 532  O O   . PRO A 1 231 ? 149.659 156.471 105.838 1.00 97.91  ? 95   PRO A O   1 
ATOM 533  C CB  . PRO A 1 231 ? 152.190 157.298 107.532 1.00 102.87 ? 95   PRO A CB  1 
ATOM 534  C CG  . PRO A 1 231 ? 152.777 157.679 108.853 1.00 103.86 ? 95   PRO A CG  1 
ATOM 535  C CD  . PRO A 1 231 ? 151.679 157.526 109.843 1.00 102.18 ? 95   PRO A CD  1 
ATOM 536  N N   . PHE A 1 232 ? 149.344 155.619 107.895 1.00 99.19  ? 96   PHE A N   1 
ATOM 537  C CA  . PHE A 1 232 ? 148.664 154.426 107.418 1.00 97.39  ? 96   PHE A CA  1 
ATOM 538  C C   . PHE A 1 232 ? 147.202 154.742 107.103 1.00 95.80  ? 96   PHE A C   1 
ATOM 539  O O   . PHE A 1 232 ? 146.750 155.884 107.210 1.00 97.48  ? 96   PHE A O   1 
ATOM 540  C CB  . PHE A 1 232 ? 148.787 153.303 108.445 1.00 95.82  ? 96   PHE A CB  1 
ATOM 541  C CG  . PHE A 1 232 ? 150.191 153.056 108.908 1.00 94.59  ? 96   PHE A CG  1 
ATOM 542  C CD1 . PHE A 1 232 ? 151.014 152.179 108.228 1.00 93.94  ? 96   PHE A CD1 1 
ATOM 543  C CD2 . PHE A 1 232 ? 150.686 153.699 110.028 1.00 96.58  ? 96   PHE A CD2 1 
ATOM 544  C CE1 . PHE A 1 232 ? 152.306 151.952 108.654 1.00 99.34  ? 96   PHE A CE1 1 
ATOM 545  C CE2 . PHE A 1 232 ? 151.975 153.478 110.457 1.00 96.40  ? 96   PHE A CE2 1 
ATOM 546  C CZ  . PHE A 1 232 ? 152.786 152.603 109.771 1.00 98.48  ? 96   PHE A CZ  1 
ATOM 547  N N   . GLY A 1 233 ? 146.447 153.721 106.710 1.00 92.66  ? 97   GLY A N   1 
ATOM 548  C CA  . GLY A 1 233 ? 145.047 153.882 106.389 1.00 95.29  ? 97   GLY A CA  1 
ATOM 549  C C   . GLY A 1 233 ? 144.174 153.851 107.627 1.00 94.04  ? 97   GLY A C   1 
ATOM 550  O O   . GLY A 1 233 ? 144.644 153.841 108.765 1.00 96.58  ? 97   GLY A O   1 
ATOM 551  N N   . ASN A 1 234 ? 142.862 153.852 107.386 1.00 90.73  ? 98   ASN A N   1 
ATOM 552  C CA  . ASN A 1 234 ? 141.915 153.779 108.492 1.00 89.19  ? 98   ASN A CA  1 
ATOM 553  C C   . ASN A 1 234 ? 142.018 152.448 109.222 1.00 89.29  ? 98   ASN A C   1 
ATOM 554  O O   . ASN A 1 234 ? 141.974 152.405 110.459 1.00 89.47  ? 98   ASN A O   1 
ATOM 555  C CB  . ASN A 1 234 ? 140.494 153.992 107.977 1.00 91.38  ? 98   ASN A CB  1 
ATOM 556  C CG  . ASN A 1 234 ? 140.388 155.170 107.038 1.00 94.84  ? 98   ASN A CG  1 
ATOM 557  O OD1 . ASN A 1 234 ? 141.354 155.531 106.367 1.00 97.47  ? 98   ASN A OD1 1 
ATOM 558  N ND2 . ASN A 1 234 ? 139.211 155.779 106.984 1.00 91.21  ? 98   ASN A ND2 1 
ATOM 559  N N   . TYR A 1 235 ? 142.163 151.353 108.472 1.00 88.82  ? 99   TYR A N   1 
ATOM 560  C CA  . TYR A 1 235 ? 142.130 150.026 109.077 1.00 88.44  ? 99   TYR A CA  1 
ATOM 561  C C   . TYR A 1 235 ? 143.278 149.828 110.056 1.00 84.21  ? 99   TYR A C   1 
ATOM 562  O O   . TYR A 1 235 ? 143.105 149.184 111.094 1.00 82.80  ? 99   TYR A O   1 
ATOM 563  C CB  . TYR A 1 235 ? 142.152 148.951 107.992 1.00 89.81  ? 99   TYR A CB  1 
ATOM 564  C CG  . TYR A 1 235 ? 140.782 148.648 107.432 1.00 93.43  ? 99   TYR A CG  1 
ATOM 565  C CD1 . TYR A 1 235 ? 139.651 148.765 108.227 1.00 95.31  ? 99   TYR A CD1 1 
ATOM 566  C CD2 . TYR A 1 235 ? 140.618 148.254 106.112 1.00 92.77  ? 99   TYR A CD2 1 
ATOM 567  C CE1 . TYR A 1 235 ? 138.395 148.494 107.725 1.00 98.19  ? 99   TYR A CE1 1 
ATOM 568  C CE2 . TYR A 1 235 ? 139.364 147.981 105.601 1.00 96.09  ? 99   TYR A CE2 1 
ATOM 569  C CZ  . TYR A 1 235 ? 138.257 148.103 106.413 1.00 99.83  ? 99   TYR A CZ  1 
ATOM 570  O OH  . TYR A 1 235 ? 137.003 147.834 105.915 1.00 102.42 ? 99   TYR A OH  1 
ATOM 571  N N   . LEU A 1 236 ? 144.456 150.368 109.749 1.00 84.60  ? 100  LEU A N   1 
ATOM 572  C CA  . LEU A 1 236 ? 145.562 150.265 110.693 1.00 86.07  ? 100  LEU A CA  1 
ATOM 573  C C   . LEU A 1 236 ? 145.251 151.008 111.986 1.00 85.97  ? 100  LEU A C   1 
ATOM 574  O O   . LEU A 1 236 ? 145.585 150.536 113.078 1.00 89.49  ? 100  LEU A O   1 
ATOM 575  C CB  . LEU A 1 236 ? 146.850 150.790 110.064 1.00 89.62  ? 100  LEU A CB  1 
ATOM 576  C CG  . LEU A 1 236 ? 147.551 149.891 109.042 1.00 90.59  ? 100  LEU A CG  1 
ATOM 577  C CD1 . LEU A 1 236 ? 147.629 148.462 109.550 1.00 85.27  ? 100  LEU A CD1 1 
ATOM 578  C CD2 . LEU A 1 236 ? 146.874 149.950 107.681 1.00 92.59  ? 100  LEU A CD2 1 
ATOM 579  N N   . CYS A 1 237 ? 144.604 152.169 111.884 1.00 83.88  ? 101  CYS A N   1 
ATOM 580  C CA  . CYS A 1 237 ? 144.211 152.914 113.077 1.00 83.61  ? 101  CYS A CA  1 
ATOM 581  C C   . CYS A 1 237 ? 143.214 152.125 113.916 1.00 82.75  ? 101  CYS A C   1 
ATOM 582  O O   . CYS A 1 237 ? 143.363 152.009 115.144 1.00 87.01  ? 101  CYS A O   1 
ATOM 583  C CB  . CYS A 1 237 ? 143.627 154.264 112.663 1.00 85.31  ? 101  CYS A CB  1 
ATOM 584  S SG  . CYS A 1 237 ? 142.428 154.976 113.794 1.00 88.37  ? 101  CYS A SG  1 
ATOM 585  N N   . LYS A 1 238 ? 142.191 151.568 113.268 1.00 77.09  ? 102  LYS A N   1 
ATOM 586  C CA  . LYS A 1 238 ? 141.209 150.779 114.001 1.00 76.01  ? 102  LYS A CA  1 
ATOM 587  C C   . LYS A 1 238 ? 141.864 149.572 114.654 1.00 76.64  ? 102  LYS A C   1 
ATOM 588  O O   . LYS A 1 238 ? 141.592 149.263 115.820 1.00 75.89  ? 102  LYS A O   1 
ATOM 589  C CB  . LYS A 1 238 ? 140.080 150.342 113.068 1.00 74.66  ? 102  LYS A CB  1 
ATOM 590  C CG  . LYS A 1 238 ? 139.570 151.445 112.164 1.00 79.50  ? 102  LYS A CG  1 
ATOM 591  C CD  . LYS A 1 238 ? 138.288 151.060 111.461 1.00 79.43  ? 102  LYS A CD  1 
ATOM 592  C CE  . LYS A 1 238 ? 137.117 151.093 112.419 1.00 77.94  ? 102  LYS A CE  1 
ATOM 593  N NZ  . LYS A 1 238 ? 135.813 150.937 111.722 1.00 76.97  ? 102  LYS A NZ  1 
ATOM 594  N N   . ILE A 1 239 ? 142.745 148.889 113.922 1.00 77.24  ? 103  ILE A N   1 
ATOM 595  C CA  . ILE A 1 239 ? 143.404 147.701 114.449 1.00 70.56  ? 103  ILE A CA  1 
ATOM 596  C C   . ILE A 1 239 ? 144.260 148.054 115.654 1.00 69.57  ? 103  ILE A C   1 
ATOM 597  O O   . ILE A 1 239 ? 144.243 147.351 116.666 1.00 74.08  ? 103  ILE A O   1 
ATOM 598  C CB  . ILE A 1 239 ? 144.233 147.020 113.346 1.00 71.68  ? 103  ILE A CB  1 
ATOM 599  C CG1 . ILE A 1 239 ? 143.317 146.323 112.339 1.00 72.81  ? 103  ILE A CG1 1 
ATOM 600  C CG2 . ILE A 1 239 ? 145.214 146.037 113.949 1.00 74.60  ? 103  ILE A CG2 1 
ATOM 601  C CD1 . ILE A 1 239 ? 142.472 145.231 112.937 1.00 70.04  ? 103  ILE A CD1 1 
ATOM 602  N N   . ALA A 1 240 ? 145.013 149.151 115.574 1.00 69.99  ? 104  ALA A N   1 
ATOM 603  C CA  . ALA A 1 240 ? 145.885 149.524 116.682 1.00 73.71  ? 104  ALA A CA  1 
ATOM 604  C C   . ALA A 1 240 ? 145.088 149.893 117.930 1.00 75.97  ? 104  ALA A C   1 
ATOM 605  O O   . ALA A 1 240 ? 145.422 149.453 119.041 1.00 80.17  ? 104  ALA A O   1 
ATOM 606  C CB  . ALA A 1 240 ? 146.798 150.670 116.255 1.00 79.23  ? 104  ALA A CB  1 
ATOM 607  N N   . SER A 1 241 ? 144.025 150.690 117.776 1.00 71.26  ? 105  SER A N   1 
ATOM 608  C CA  . SER A 1 241 ? 143.232 151.059 118.948 1.00 70.52  ? 105  SER A CA  1 
ATOM 609  C C   . SER A 1 241 ? 142.534 149.845 119.559 1.00 68.24  ? 105  SER A C   1 
ATOM 610  O O   . SER A 1 241 ? 142.534 149.661 120.791 1.00 64.40  ? 105  SER A O   1 
ATOM 611  C CB  . SER A 1 241 ? 142.218 152.130 118.567 1.00 76.11  ? 105  SER A CB  1 
ATOM 612  O OG  . SER A 1 241 ? 142.862 153.229 117.951 1.00 83.01  ? 105  SER A OG  1 
ATOM 613  N N   . ALA A 1 242 ? 141.932 149.006 118.712 1.00 68.98  ? 106  ALA A N   1 
ATOM 614  C CA  . ALA A 1 242 ? 141.308 147.790 119.209 1.00 63.73  ? 106  ALA A CA  1 
ATOM 615  C C   . ALA A 1 242 ? 142.325 146.885 119.877 1.00 62.46  ? 106  ALA A C   1 
ATOM 616  O O   . ALA A 1 242 ? 141.990 146.196 120.839 1.00 67.16  ? 106  ALA A O   1 
ATOM 617  C CB  . ALA A 1 242 ? 140.607 147.051 118.073 1.00 66.68  ? 106  ALA A CB  1 
ATOM 618  N N   . SER A 1 243 ? 143.568 146.878 119.394 1.00 61.39  ? 107  SER A N   1 
ATOM 619  C CA  . SER A 1 243 ? 144.595 146.051 120.014 1.00 59.52  ? 107  SER A CA  1 
ATOM 620  C C   . SER A 1 243 ? 144.962 146.572 121.392 1.00 58.69  ? 107  SER A C   1 
ATOM 621  O O   . SER A 1 243 ? 145.209 145.785 122.308 1.00 63.83  ? 107  SER A O   1 
ATOM 622  C CB  . SER A 1 243 ? 145.828 145.982 119.119 1.00 65.56  ? 107  SER A CB  1 
ATOM 623  O OG  . SER A 1 243 ? 145.548 145.255 117.937 1.00 69.42  ? 107  SER A OG  1 
ATOM 624  N N   . VAL A 1 244 ? 144.994 147.892 121.563 1.00 55.05  ? 108  VAL A N   1 
ATOM 625  C CA  . VAL A 1 244 ? 145.252 148.455 122.889 1.00 56.41  ? 108  VAL A CA  1 
ATOM 626  C C   . VAL A 1 244 ? 144.169 148.018 123.875 1.00 58.13  ? 108  VAL A C   1 
ATOM 627  O O   . VAL A 1 244 ? 144.455 147.482 124.962 1.00 58.54  ? 108  VAL A O   1 
ATOM 628  C CB  . VAL A 1 244 ? 145.358 149.988 122.797 1.00 67.09  ? 108  VAL A CB  1 
ATOM 629  C CG1 . VAL A 1 244 ? 145.110 150.635 124.137 1.00 64.83  ? 108  VAL A CG1 1 
ATOM 630  C CG2 . VAL A 1 244 ? 146.720 150.388 122.260 1.00 72.99  ? 108  VAL A CG2 1 
ATOM 631  N N   . SER A 1 245 ? 142.902 148.208 123.492 1.00 61.42  ? 109  SER A N   1 
ATOM 632  C CA  . SER A 1 245 ? 141.807 147.837 124.392 1.00 56.37  ? 109  SER A CA  1 
ATOM 633  C C   . SER A 1 245 ? 141.777 146.332 124.643 1.00 51.45  ? 109  SER A C   1 
ATOM 634  O O   . SER A 1 245 ? 141.560 145.877 125.778 1.00 52.03  ? 109  SER A O   1 
ATOM 635  C CB  . SER A 1 245 ? 140.475 148.307 123.817 1.00 60.49  ? 109  SER A CB  1 
ATOM 636  O OG  . SER A 1 245 ? 139.395 147.816 124.586 1.00 64.07  ? 109  SER A OG  1 
ATOM 637  N N   . PHE A 1 246 ? 141.994 145.547 123.588 1.00 51.87  ? 110  PHE A N   1 
ATOM 638  C CA  . PHE A 1 246 ? 142.003 144.099 123.697 1.00 51.02  ? 110  PHE A CA  1 
ATOM 639  C C   . PHE A 1 246 ? 143.107 143.627 124.624 1.00 50.84  ? 110  PHE A C   1 
ATOM 640  O O   . PHE A 1 246 ? 142.899 142.710 125.422 1.00 55.71  ? 110  PHE A O   1 
ATOM 641  C CB  . PHE A 1 246 ? 142.168 143.490 122.305 1.00 52.06  ? 110  PHE A CB  1 
ATOM 642  C CG  . PHE A 1 246 ? 142.227 141.997 122.295 1.00 53.15  ? 110  PHE A CG  1 
ATOM 643  C CD1 . PHE A 1 246 ? 143.432 141.336 122.434 1.00 54.75  ? 110  PHE A CD1 1 
ATOM 644  C CD2 . PHE A 1 246 ? 141.079 141.252 122.128 1.00 56.25  ? 110  PHE A CD2 1 
ATOM 645  C CE1 . PHE A 1 246 ? 143.486 139.968 122.427 1.00 60.31  ? 110  PHE A CE1 1 
ATOM 646  C CE2 . PHE A 1 246 ? 141.131 139.883 122.115 1.00 61.51  ? 110  PHE A CE2 1 
ATOM 647  C CZ  . PHE A 1 246 ? 142.335 139.241 122.266 1.00 59.58  ? 110  PHE A CZ  1 
ATOM 648  N N   . ASN A 1 247 ? 144.295 144.222 124.524 1.00 50.44  ? 111  ASN A N   1 
ATOM 649  C CA  . ASN A 1 247 ? 145.375 143.835 125.418 1.00 47.36  ? 111  ASN A CA  1 
ATOM 650  C C   . ASN A 1 247 ? 144.985 144.085 126.862 1.00 46.85  ? 111  ASN A C   1 
ATOM 651  O O   . ASN A 1 247 ? 145.150 143.208 127.716 1.00 51.74  ? 111  ASN A O   1 
ATOM 652  C CB  . ASN A 1 247 ? 146.653 144.592 125.076 1.00 54.14  ? 111  ASN A CB  1 
ATOM 653  C CG  . ASN A 1 247 ? 147.750 144.356 126.088 1.00 57.42  ? 111  ASN A CG  1 
ATOM 654  O OD1 . ASN A 1 247 ? 147.830 145.038 127.106 1.00 57.54  ? 111  ASN A OD1 1 
ATOM 655  N ND2 . ASN A 1 247 ? 148.601 143.383 125.814 1.00 64.34  ? 111  ASN A ND2 1 
ATOM 656  N N   . LEU A 1 248 ? 144.433 145.266 127.151 1.00 48.05  ? 112  LEU A N   1 
ATOM 657  C CA  . LEU A 1 248 ? 144.036 145.545 128.531 1.00 45.80  ? 112  LEU A CA  1 
ATOM 658  C C   . LEU A 1 248 ? 143.067 144.489 129.052 1.00 44.14  ? 112  LEU A C   1 
ATOM 659  O O   . LEU A 1 248 ? 143.297 143.879 130.108 1.00 44.47  ? 112  LEU A O   1 
ATOM 660  C CB  . LEU A 1 248 ? 143.412 146.935 128.635 1.00 51.71  ? 112  LEU A CB  1 
ATOM 661  C CG  . LEU A 1 248 ? 142.583 147.211 129.892 1.00 51.04  ? 112  LEU A CG  1 
ATOM 662  C CD1 . LEU A 1 248 ? 143.420 147.116 131.151 1.00 53.75  ? 112  LEU A CD1 1 
ATOM 663  C CD2 . LEU A 1 248 ? 141.924 148.570 129.797 1.00 55.53  ? 112  LEU A CD2 1 
ATOM 664  N N   . TYR A 1 249 ? 141.988 144.236 128.307 1.00 48.25  ? 113  TYR A N   1 
ATOM 665  C CA  . TYR A 1 249 ? 140.941 143.359 128.831 1.00 47.10  ? 113  TYR A CA  1 
ATOM 666  C C   . TYR A 1 249 ? 141.387 141.901 128.881 1.00 46.83  ? 113  TYR A C   1 
ATOM 667  O O   . TYR A 1 249 ? 141.123 141.200 129.867 1.00 49.07  ? 113  TYR A O   1 
ATOM 668  C CB  . TYR A 1 249 ? 139.668 143.503 128.007 1.00 49.03  ? 113  TYR A CB  1 
ATOM 669  C CG  . TYR A 1 249 ? 138.972 144.816 128.236 1.00 50.94  ? 113  TYR A CG  1 
ATOM 670  C CD1 . TYR A 1 249 ? 138.438 145.129 129.473 1.00 52.47  ? 113  TYR A CD1 1 
ATOM 671  C CD2 . TYR A 1 249 ? 138.852 145.743 127.218 1.00 53.73  ? 113  TYR A CD2 1 
ATOM 672  C CE1 . TYR A 1 249 ? 137.804 146.328 129.687 1.00 55.48  ? 113  TYR A CE1 1 
ATOM 673  C CE2 . TYR A 1 249 ? 138.219 146.942 127.423 1.00 57.40  ? 113  TYR A CE2 1 
ATOM 674  C CZ  . TYR A 1 249 ? 137.697 147.230 128.658 1.00 59.89  ? 113  TYR A CZ  1 
ATOM 675  O OH  . TYR A 1 249 ? 137.064 148.431 128.858 1.00 69.22  ? 113  TYR A OH  1 
ATOM 676  N N   . ALA A 1 250 ? 142.053 141.420 127.832 1.00 44.22  ? 114  ALA A N   1 
ATOM 677  C CA  . ALA A 1 250 ? 142.539 140.049 127.840 1.00 40.66  ? 114  ALA A CA  1 
ATOM 678  C C   . ALA A 1 250 ? 143.528 139.826 128.970 1.00 42.66  ? 114  ALA A C   1 
ATOM 679  O O   . ALA A 1 250 ? 143.467 138.802 129.658 1.00 46.87  ? 114  ALA A O   1 
ATOM 680  C CB  . ALA A 1 250 ? 143.176 139.707 126.495 1.00 42.95  ? 114  ALA A CB  1 
ATOM 681  N N   . SER A 1 251 ? 144.444 140.774 129.190 1.00 40.58  ? 115  SER A N   1 
ATOM 682  C CA  . SER A 1 251 ? 145.417 140.612 130.260 1.00 39.14  ? 115  SER A CA  1 
ATOM 683  C C   . SER A 1 251 ? 144.741 140.565 131.622 1.00 43.33  ? 115  SER A C   1 
ATOM 684  O O   . SER A 1 251 ? 145.064 139.707 132.450 1.00 48.13  ? 115  SER A O   1 
ATOM 685  C CB  . SER A 1 251 ? 146.446 141.735 130.206 1.00 41.50  ? 115  SER A CB  1 
ATOM 686  O OG  . SER A 1 251 ? 147.276 141.597 129.070 1.00 50.81  ? 115  SER A OG  1 
ATOM 687  N N   . VAL A 1 252 ? 143.791 141.470 131.881 1.00 41.79  ? 116  VAL A N   1 
ATOM 688  C CA  . VAL A 1 252 ? 143.180 141.467 133.209 1.00 40.84  ? 116  VAL A CA  1 
ATOM 689  C C   . VAL A 1 252 ? 142.374 140.192 133.432 1.00 42.85  ? 116  VAL A C   1 
ATOM 690  O O   . VAL A 1 252 ? 142.419 139.600 134.518 1.00 46.31  ? 116  VAL A O   1 
ATOM 691  C CB  . VAL A 1 252 ? 142.332 142.732 133.446 1.00 43.55  ? 116  VAL A CB  1 
ATOM 692  C CG1 . VAL A 1 252 ? 143.197 143.961 133.370 1.00 49.23  ? 116  VAL A CG1 1 
ATOM 693  C CG2 . VAL A 1 252 ? 141.189 142.833 132.466 1.00 47.19  ? 116  VAL A CG2 1 
ATOM 694  N N   . PHE A 1 253 ? 141.637 139.734 132.414 1.00 43.33  ? 117  PHE A N   1 
ATOM 695  C CA  . PHE A 1 253 ? 140.836 138.525 132.591 1.00 43.23  ? 117  PHE A CA  1 
ATOM 696  C C   . PHE A 1 253 ? 141.715 137.294 132.772 1.00 43.88  ? 117  PHE A C   1 
ATOM 697  O O   . PHE A 1 253 ? 141.427 136.437 133.617 1.00 47.45  ? 117  PHE A O   1 
ATOM 698  C CB  . PHE A 1 253 ? 139.888 138.344 131.411 1.00 44.16  ? 117  PHE A CB  1 
ATOM 699  C CG  . PHE A 1 253 ? 138.798 139.370 131.351 1.00 45.76  ? 117  PHE A CG  1 
ATOM 700  C CD1 . PHE A 1 253 ? 138.512 140.158 132.450 1.00 45.33  ? 117  PHE A CD1 1 
ATOM 701  C CD2 . PHE A 1 253 ? 138.055 139.543 130.200 1.00 50.58  ? 117  PHE A CD2 1 
ATOM 702  C CE1 . PHE A 1 253 ? 137.513 141.100 132.400 1.00 45.83  ? 117  PHE A CE1 1 
ATOM 703  C CE2 . PHE A 1 253 ? 137.053 140.485 130.144 1.00 52.96  ? 117  PHE A CE2 1 
ATOM 704  C CZ  . PHE A 1 253 ? 136.782 141.264 131.245 1.00 49.10  ? 117  PHE A CZ  1 
ATOM 705  N N   . LEU A 1 254 ? 142.795 137.187 131.996 1.00 43.75  ? 118  LEU A N   1 
ATOM 706  C CA  . LEU A 1 254 ? 143.698 136.055 132.155 1.00 42.42  ? 118  LEU A CA  1 
ATOM 707  C C   . LEU A 1 254 ? 144.375 136.079 133.518 1.00 44.64  ? 118  LEU A C   1 
ATOM 708  O O   . LEU A 1 254 ? 144.574 135.027 134.132 1.00 50.46  ? 118  LEU A O   1 
ATOM 709  C CB  . LEU A 1 254 ? 144.734 136.046 131.034 1.00 43.13  ? 118  LEU A CB  1 
ATOM 710  C CG  . LEU A 1 254 ? 144.199 135.671 129.653 1.00 46.52  ? 118  LEU A CG  1 
ATOM 711  C CD1 . LEU A 1 254 ? 145.239 135.929 128.591 1.00 49.94  ? 118  LEU A CD1 1 
ATOM 712  C CD2 . LEU A 1 254 ? 143.772 134.222 129.628 1.00 51.52  ? 118  LEU A CD2 1 
ATOM 713  N N   . LEU A 1 255 ? 144.730 137.265 134.017 1.00 43.83  ? 119  LEU A N   1 
ATOM 714  C CA  . LEU A 1 255 ? 145.343 137.344 135.339 1.00 42.74  ? 119  LEU A CA  1 
ATOM 715  C C   . LEU A 1 255 ? 144.362 136.951 136.438 1.00 45.61  ? 119  LEU A C   1 
ATOM 716  O O   . LEU A 1 255 ? 144.745 136.277 137.401 1.00 50.44  ? 119  LEU A O   1 
ATOM 717  C CB  . LEU A 1 255 ? 145.894 138.746 135.585 1.00 42.32  ? 119  LEU A CB  1 
ATOM 718  C CG  . LEU A 1 255 ? 147.161 139.090 134.805 1.00 45.00  ? 119  LEU A CG  1 
ATOM 719  C CD1 . LEU A 1 255 ? 147.674 140.452 135.201 1.00 49.08  ? 119  LEU A CD1 1 
ATOM 720  C CD2 . LEU A 1 255 ? 148.221 138.039 135.033 1.00 48.70  ? 119  LEU A CD2 1 
ATOM 721  N N   . THR A 1 256 ? 143.098 137.366 136.324 1.00 45.82  ? 120  THR A N   1 
ATOM 722  C CA  . THR A 1 256 ? 142.115 136.941 137.319 1.00 44.54  ? 120  THR A CA  1 
ATOM 723  C C   . THR A 1 256 ? 141.907 135.434 137.282 1.00 45.41  ? 120  THR A C   1 
ATOM 724  O O   . THR A 1 256 ? 141.782 134.795 138.332 1.00 51.42  ? 120  THR A O   1 
ATOM 725  C CB  . THR A 1 256 ? 140.781 137.653 137.117 1.00 45.20  ? 120  THR A CB  1 
ATOM 726  O OG1 . THR A 1 256 ? 140.268 137.360 135.815 1.00 51.56  ? 120  THR A OG1 1 
ATOM 727  C CG2 . THR A 1 256 ? 140.959 139.131 137.261 1.00 48.30  ? 120  THR A CG2 1 
ATOM 728  N N   . CYS A 1 257 ? 141.855 134.848 136.085 1.00 41.66  ? 121  CYS A N   1 
ATOM 729  C CA  . CYS A 1 257 ? 141.720 133.398 136.001 1.00 42.48  ? 121  CYS A CA  1 
ATOM 730  C C   . CYS A 1 257 ? 142.945 132.695 136.571 1.00 46.78  ? 121  CYS A C   1 
ATOM 731  O O   . CYS A 1 257 ? 142.823 131.647 137.210 1.00 52.79  ? 121  CYS A O   1 
ATOM 732  C CB  . CYS A 1 257 ? 141.467 132.974 134.558 1.00 46.91  ? 121  CYS A CB  1 
ATOM 733  S SG  . CYS A 1 257 ? 139.799 133.347 133.987 1.00 69.24  ? 121  CYS A SG  1 
ATOM 734  N N   . LEU A 1 258 ? 144.135 133.260 136.360 1.00 47.13  ? 122  LEU A N   1 
ATOM 735  C CA  . LEU A 1 258 ? 145.342 132.706 136.965 1.00 45.91  ? 122  LEU A CA  1 
ATOM 736  C C   . LEU A 1 258 ? 145.257 132.733 138.485 1.00 48.68  ? 122  LEU A C   1 
ATOM 737  O O   . LEU A 1 258 ? 145.600 131.753 139.155 1.00 54.00  ? 122  LEU A O   1 
ATOM 738  C CB  . LEU A 1 258 ? 146.569 133.484 136.493 1.00 45.52  ? 122  LEU A CB  1 
ATOM 739  C CG  . LEU A 1 258 ? 147.238 133.048 135.196 1.00 47.05  ? 122  LEU A CG  1 
ATOM 740  C CD1 . LEU A 1 258 ? 148.257 134.076 134.763 1.00 49.78  ? 122  LEU A CD1 1 
ATOM 741  C CD2 . LEU A 1 258 ? 147.901 131.713 135.403 1.00 53.36  ? 122  LEU A CD2 1 
ATOM 742  N N   . SER A 1 259 ? 144.812 133.857 139.047 1.00 46.56  ? 123  SER A N   1 
ATOM 743  C CA  . SER A 1 259 ? 144.704 133.962 140.499 1.00 45.23  ? 123  SER A CA  1 
ATOM 744  C C   . SER A 1 259 ? 143.676 132.985 141.050 1.00 50.35  ? 123  SER A C   1 
ATOM 745  O O   . SER A 1 259 ? 143.901 132.355 142.090 1.00 56.09  ? 123  SER A O   1 
ATOM 746  C CB  . SER A 1 259 ? 144.351 135.391 140.894 1.00 47.13  ? 123  SER A CB  1 
ATOM 747  O OG  . SER A 1 259 ? 145.347 136.290 140.449 1.00 51.45  ? 123  SER A OG  1 
ATOM 748  N N   . ILE A 1 260 ? 142.540 132.842 140.367 1.00 48.98  ? 124  ILE A N   1 
ATOM 749  C CA  . ILE A 1 260 ? 141.519 131.897 140.812 1.00 46.19  ? 124  ILE A CA  1 
ATOM 750  C C   . ILE A 1 260 ? 142.046 130.470 140.743 1.00 49.65  ? 124  ILE A C   1 
ATOM 751  O O   . ILE A 1 260 ? 141.798 129.657 141.640 1.00 55.61  ? 124  ILE A O   1 
ATOM 752  C CB  . ILE A 1 260 ? 140.235 132.070 139.984 1.00 43.79  ? 124  ILE A CB  1 
ATOM 753  C CG1 . ILE A 1 260 ? 139.577 133.411 140.304 1.00 45.30  ? 124  ILE A CG1 1 
ATOM 754  C CG2 . ILE A 1 260 ? 139.280 130.929 140.241 1.00 47.74  ? 124  ILE A CG2 1 
ATOM 755  C CD1 . ILE A 1 260 ? 138.343 133.686 139.488 1.00 51.70  ? 124  ILE A CD1 1 
ATOM 756  N N   . ASP A 1 261 ? 142.778 130.141 139.676 1.00 49.96  ? 125  ASP A N   1 
ATOM 757  C CA  . ASP A 1 261 ? 143.356 128.808 139.560 1.00 50.59  ? 125  ASP A CA  1 
ATOM 758  C C   . ASP A 1 261 ? 144.366 128.540 140.666 1.00 54.57  ? 125  ASP A C   1 
ATOM 759  O O   . ASP A 1 261 ? 144.405 127.438 141.221 1.00 58.98  ? 125  ASP A O   1 
ATOM 760  C CB  . ASP A 1 261 ? 144.013 128.636 138.195 1.00 54.79  ? 125  ASP A CB  1 
ATOM 761  C CG  . ASP A 1 261 ? 145.114 127.601 138.213 1.00 62.37  ? 125  ASP A CG  1 
ATOM 762  O OD1 . ASP A 1 261 ? 144.813 126.415 138.455 1.00 63.90  ? 125  ASP A OD1 1 
ATOM 763  O OD2 . ASP A 1 261 ? 146.284 127.976 137.991 1.00 64.23  ? 125  ASP A OD2 1 
ATOM 764  N N   . ARG A 1 262 ? 145.203 129.526 140.991 1.00 55.49  ? 126  ARG A N   1 
ATOM 765  C CA  . ARG A 1 262 ? 146.159 129.336 142.079 1.00 57.12  ? 126  ARG A CA  1 
ATOM 766  C C   . ARG A 1 262 ? 145.444 129.167 143.410 1.00 56.51  ? 126  ARG A C   1 
ATOM 767  O O   . ARG A 1 262 ? 145.857 128.355 144.246 1.00 62.24  ? 126  ARG A O   1 
ATOM 768  C CB  . ARG A 1 262 ? 147.144 130.502 142.145 1.00 57.24  ? 126  ARG A CB  1 
ATOM 769  C CG  . ARG A 1 262 ? 148.064 130.606 140.947 1.00 59.48  ? 126  ARG A CG  1 
ATOM 770  C CD  . ARG A 1 262 ? 148.569 129.244 140.518 1.00 61.79  ? 126  ARG A CD  1 
ATOM 771  N NE  . ARG A 1 262 ? 149.378 128.607 141.548 1.00 69.54  ? 126  ARG A NE  1 
ATOM 772  C CZ  . ARG A 1 262 ? 149.800 127.352 141.494 1.00 73.28  ? 126  ARG A CZ  1 
ATOM 773  N NH1 . ARG A 1 262 ? 149.497 126.565 140.475 1.00 71.95  ? 126  ARG A NH1 1 
ATOM 774  N NH2 . ARG A 1 262 ? 150.542 126.874 142.489 1.00 71.34  ? 126  ARG A NH2 1 
ATOM 775  N N   . TYR A 1 263 ? 144.370 129.926 143.630 1.00 52.20  ? 127  TYR A N   1 
ATOM 776  C CA  . TYR A 1 263 ? 143.606 129.774 144.862 1.00 52.52  ? 127  TYR A CA  1 
ATOM 777  C C   . TYR A 1 263 ? 142.997 128.384 144.966 1.00 57.54  ? 127  TYR A C   1 
ATOM 778  O O   . TYR A 1 263 ? 143.040 127.759 146.030 1.00 63.74  ? 127  TYR A O   1 
ATOM 779  C CB  . TYR A 1 263 ? 142.518 130.840 144.938 1.00 54.97  ? 127  TYR A CB  1 
ATOM 780  C CG  . TYR A 1 263 ? 141.425 130.519 145.924 1.00 61.37  ? 127  TYR A CG  1 
ATOM 781  C CD1 . TYR A 1 263 ? 141.668 130.545 147.287 1.00 64.74  ? 127  TYR A CD1 1 
ATOM 782  C CD2 . TYR A 1 263 ? 140.148 130.199 145.493 1.00 62.94  ? 127  TYR A CD2 1 
ATOM 783  C CE1 . TYR A 1 263 ? 140.674 130.253 148.193 1.00 68.34  ? 127  TYR A CE1 1 
ATOM 784  C CE2 . TYR A 1 263 ? 139.146 129.908 146.391 1.00 68.62  ? 127  TYR A CE2 1 
ATOM 785  C CZ  . TYR A 1 263 ? 139.415 129.937 147.741 1.00 71.83  ? 127  TYR A CZ  1 
ATOM 786  O OH  . TYR A 1 263 ? 138.422 129.647 148.645 1.00 73.04  ? 127  TYR A OH  1 
ATOM 787  N N   . LEU A 1 264 ? 142.429 127.881 143.871 1.00 57.57  ? 128  LEU A N   1 
ATOM 788  C CA  . LEU A 1 264 ? 141.870 126.533 143.892 1.00 57.76  ? 128  LEU A CA  1 
ATOM 789  C C   . LEU A 1 264 ? 142.956 125.487 144.106 1.00 59.12  ? 128  LEU A C   1 
ATOM 790  O O   . LEU A 1 264 ? 142.752 124.521 144.845 1.00 65.94  ? 128  LEU A O   1 
ATOM 791  C CB  . LEU A 1 264 ? 141.107 126.252 142.601 1.00 54.50  ? 128  LEU A CB  1 
ATOM 792  C CG  . LEU A 1 264 ? 139.867 127.107 142.354 1.00 55.68  ? 128  LEU A CG  1 
ATOM 793  C CD1 . LEU A 1 264 ? 139.079 126.563 141.178 1.00 57.67  ? 128  LEU A CD1 1 
ATOM 794  C CD2 . LEU A 1 264 ? 139.005 127.174 143.598 1.00 60.41  ? 128  LEU A CD2 1 
ATOM 795  N N   . ALA A 1 265 ? 144.112 125.655 143.465 1.00 55.73  ? 129  ALA A N   1 
ATOM 796  C CA  . ALA A 1 265 ? 145.186 124.680 143.611 1.00 57.27  ? 129  ALA A CA  1 
ATOM 797  C C   . ALA A 1 265 ? 145.717 124.643 145.037 1.00 63.54  ? 129  ALA A C   1 
ATOM 798  O O   . ALA A 1 265 ? 145.963 123.563 145.585 1.00 70.91  ? 129  ALA A O   1 
ATOM 799  C CB  . ALA A 1 265 ? 146.314 124.989 142.631 1.00 59.60  ? 129  ALA A CB  1 
ATOM 800  N N   . ILE A 1 266 ? 145.908 125.809 145.652 1.00 58.93  ? 130  ILE A N   1 
ATOM 801  C CA  . ILE A 1 266 ? 146.479 125.852 146.994 1.00 59.35  ? 130  ILE A CA  1 
ATOM 802  C C   . ILE A 1 266 ? 145.458 125.433 148.044 1.00 62.88  ? 130  ILE A C   1 
ATOM 803  O O   . ILE A 1 266 ? 145.778 124.676 148.965 1.00 66.36  ? 130  ILE A O   1 
ATOM 804  C CB  . ILE A 1 266 ? 147.048 127.251 147.280 1.00 59.30  ? 130  ILE A CB  1 
ATOM 805  C CG1 . ILE A 1 266 ? 148.265 127.515 146.395 1.00 63.09  ? 130  ILE A CG1 1 
ATOM 806  C CG2 . ILE A 1 266 ? 147.419 127.388 148.742 1.00 60.72  ? 130  ILE A CG2 1 
ATOM 807  C CD1 . ILE A 1 266 ? 148.996 128.787 146.729 1.00 67.09  ? 130  ILE A CD1 1 
ATOM 808  N N   . VAL A 1 267 ? 144.217 125.901 147.928 1.00 63.87  ? 131  VAL A N   1 
ATOM 809  C CA  . VAL A 1 267 ? 143.254 125.755 149.013 1.00 66.85  ? 131  VAL A CA  1 
ATOM 810  C C   . VAL A 1 267 ? 142.353 124.541 148.807 1.00 67.48  ? 131  VAL A C   1 
ATOM 811  O O   . VAL A 1 267 ? 141.928 123.905 149.777 1.00 72.64  ? 131  VAL A O   1 
ATOM 812  C CB  . VAL A 1 267 ? 142.428 127.044 149.171 1.00 66.49  ? 131  VAL A CB  1 
ATOM 813  C CG1 . VAL A 1 267 ? 141.474 126.930 150.340 1.00 68.36  ? 131  VAL A CG1 1 
ATOM 814  C CG2 . VAL A 1 267 ? 143.355 128.224 149.370 1.00 64.22  ? 131  VAL A CG2 1 
ATOM 815  N N   . HIS A 1 268 ? 142.067 124.189 147.552 1.00 66.53  ? 132  HIS A N   1 
ATOM 816  C CA  . HIS A 1 268 ? 141.195 123.061 147.226 1.00 68.38  ? 132  HIS A CA  1 
ATOM 817  C C   . HIS A 1 268 ? 141.927 122.097 146.297 1.00 70.06  ? 132  HIS A C   1 
ATOM 818  O O   . HIS A 1 268 ? 141.566 121.962 145.121 1.00 68.44  ? 132  HIS A O   1 
ATOM 819  C CB  . HIS A 1 268 ? 139.897 123.521 146.564 1.00 69.69  ? 132  HIS A CB  1 
ATOM 820  C CG  . HIS A 1 268 ? 139.134 124.543 147.345 1.00 75.37  ? 132  HIS A CG  1 
ATOM 821  N ND1 . HIS A 1 268 ? 139.369 124.797 148.678 1.00 76.94  ? 132  HIS A ND1 1 
ATOM 822  C CD2 . HIS A 1 268 ? 138.133 125.375 146.975 1.00 74.92  ? 132  HIS A CD2 1 
ATOM 823  C CE1 . HIS A 1 268 ? 138.546 125.743 149.095 1.00 78.33  ? 132  HIS A CE1 1 
ATOM 824  N NE2 . HIS A 1 268 ? 137.786 126.111 148.080 1.00 76.85  ? 132  HIS A NE2 1 
ATOM 825  N N   . PRO A 1 269 ? 142.958 121.400 146.793 1.00 70.64  ? 133  PRO A N   1 
ATOM 826  C CA  . PRO A 1 269 ? 143.675 120.474 145.913 1.00 72.89  ? 133  PRO A CA  1 
ATOM 827  C C   . PRO A 1 269 ? 142.840 119.246 145.564 1.00 74.78  ? 133  PRO A C   1 
ATOM 828  O O   . PRO A 1 269 ? 143.379 118.139 145.538 1.00 77.24  ? 133  PRO A O   1 
ATOM 829  C CB  . PRO A 1 269 ? 144.907 120.081 146.739 1.00 72.33  ? 133  PRO A CB  1 
ATOM 830  C CG  . PRO A 1 269 ? 144.996 121.107 147.829 1.00 69.16  ? 133  PRO A CG  1 
ATOM 831  C CD  . PRO A 1 269 ? 143.583 121.477 148.122 1.00 68.68  ? 133  PRO A CD  1 
ATOM 832  N N   . THR A 1 277 ? 141.102 119.429 134.396 1.00 100.67 ? 141  THR A N   1 
ATOM 833  C CA  . THR A 1 277 ? 140.471 120.708 134.092 1.00 99.76  ? 141  THR A CA  1 
ATOM 834  C C   . THR A 1 277 ? 141.181 121.421 132.946 1.00 96.13  ? 141  THR A C   1 
ATOM 835  O O   . THR A 1 277 ? 141.564 122.581 133.071 1.00 93.73  ? 141  THR A O   1 
ATOM 836  C CB  . THR A 1 277 ? 140.450 121.636 135.325 1.00 97.39  ? 141  THR A CB  1 
ATOM 837  O OG1 . THR A 1 277 ? 141.774 121.766 135.854 1.00 95.10  ? 141  THR A OG1 1 
ATOM 838  C CG2 . THR A 1 277 ? 139.530 121.081 136.399 1.00 95.12  ? 141  THR A CG2 1 
ATOM 839  N N   . MET A 1 278 ? 141.351 120.721 131.826 1.00 97.66  ? 142  MET A N   1 
ATOM 840  C CA  . MET A 1 278 ? 142.024 121.267 130.653 1.00 95.02  ? 142  MET A CA  1 
ATOM 841  C C   . MET A 1 278 ? 141.060 121.767 129.589 1.00 94.72  ? 142  MET A C   1 
ATOM 842  O O   . MET A 1 278 ? 141.274 122.844 129.024 1.00 94.39  ? 142  MET A O   1 
ATOM 843  C CB  . MET A 1 278 ? 142.950 120.217 130.037 1.00 96.65  ? 142  MET A CB  1 
ATOM 844  C CG  . MET A 1 278 ? 144.278 120.103 130.742 1.00 100.49 ? 142  MET A CG  1 
ATOM 845  S SD  . MET A 1 278 ? 144.999 121.731 130.999 1.00 99.21  ? 142  MET A SD  1 
ATOM 846  C CE  . MET A 1 278 ? 146.728 121.303 131.090 1.00 92.06  ? 142  MET A CE  1 
ATOM 847  N N   . LEU A 1 279 ? 140.012 121.000 129.287 1.00 95.10  ? 143  LEU A N   1 
ATOM 848  C CA  . LEU A 1 279 ? 139.012 121.477 128.340 1.00 95.79  ? 143  LEU A CA  1 
ATOM 849  C C   . LEU A 1 279 ? 138.307 122.716 128.873 1.00 93.48  ? 143  LEU A C   1 
ATOM 850  O O   . LEU A 1 279 ? 138.023 123.651 128.116 1.00 91.47  ? 143  LEU A O   1 
ATOM 851  C CB  . LEU A 1 279 ? 138.006 120.370 128.025 1.00 100.26 ? 143  LEU A CB  1 
ATOM 852  C CG  . LEU A 1 279 ? 138.429 119.367 126.949 1.00 105.18 ? 143  LEU A CG  1 
ATOM 853  C CD1 . LEU A 1 279 ? 138.953 120.099 125.720 1.00 101.93 ? 143  LEU A CD1 1 
ATOM 854  C CD2 . LEU A 1 279 ? 139.461 118.378 127.473 1.00 106.00 ? 143  LEU A CD2 1 
ATOM 855  N N   . VAL A 1 280 ? 138.023 122.747 130.177 1.00 92.68  ? 144  VAL A N   1 
ATOM 856  C CA  . VAL A 1 280 ? 137.444 123.948 130.766 1.00 91.21  ? 144  VAL A CA  1 
ATOM 857  C C   . VAL A 1 280 ? 138.429 125.109 130.699 1.00 89.15  ? 144  VAL A C   1 
ATOM 858  O O   . VAL A 1 280 ? 138.023 126.259 130.514 1.00 86.73  ? 144  VAL A O   1 
ATOM 859  C CB  . VAL A 1 280 ? 136.978 123.678 132.208 1.00 93.16  ? 144  VAL A CB  1 
ATOM 860  C CG1 . VAL A 1 280 ? 138.123 123.178 133.052 1.00 90.76  ? 144  VAL A CG1 1 
ATOM 861  C CG2 . VAL A 1 280 ? 136.375 124.934 132.818 1.00 84.79  ? 144  VAL A CG2 1 
ATOM 862  N N   . ALA A 1 281 ? 139.730 124.842 130.835 1.00 88.92  ? 145  ALA A N   1 
ATOM 863  C CA  . ALA A 1 281 ? 140.717 125.909 130.694 1.00 82.17  ? 145  ALA A CA  1 
ATOM 864  C C   . ALA A 1 281 ? 140.738 126.467 129.275 1.00 83.19  ? 145  ALA A C   1 
ATOM 865  O O   . ALA A 1 281 ? 140.809 127.686 129.084 1.00 85.05  ? 145  ALA A O   1 
ATOM 866  C CB  . ALA A 1 281 ? 142.101 125.402 131.091 1.00 80.11  ? 145  ALA A CB  1 
ATOM 867  N N   . LYS A 1 282 ? 140.683 125.593 128.267 1.00 81.74  ? 146  LYS A N   1 
ATOM 868  C CA  . LYS A 1 282 ? 140.640 126.068 126.885 1.00 81.45  ? 146  LYS A CA  1 
ATOM 869  C C   . LYS A 1 282 ? 139.358 126.842 126.606 1.00 80.84  ? 146  LYS A C   1 
ATOM 870  O O   . LYS A 1 282 ? 139.375 127.859 125.901 1.00 79.99  ? 146  LYS A O   1 
ATOM 871  C CB  . LYS A 1 282 ? 140.775 124.893 125.918 1.00 83.79  ? 146  LYS A CB  1 
ATOM 872  C CG  . LYS A 1 282 ? 142.167 124.298 125.850 1.00 89.77  ? 146  LYS A CG  1 
ATOM 873  C CD  . LYS A 1 282 ? 143.180 125.319 125.361 1.00 89.99  ? 146  LYS A CD  1 
ATOM 874  C CE  . LYS A 1 282 ? 144.520 124.666 125.068 1.00 89.98  ? 146  LYS A CE  1 
ATOM 875  N NZ  . LYS A 1 282 ? 145.024 123.899 126.238 1.00 91.58  ? 146  LYS A NZ  1 
ATOM 876  N N   . VAL A 1 283 ? 138.233 126.368 127.144 1.00 79.44  ? 147  VAL A N   1 
ATOM 877  C CA  . VAL A 1 283 ? 136.975 127.090 126.993 1.00 79.87  ? 147  VAL A CA  1 
ATOM 878  C C   . VAL A 1 283 ? 137.070 128.457 127.656 1.00 79.88  ? 147  VAL A C   1 
ATOM 879  O O   . VAL A 1 283 ? 136.600 129.461 127.112 1.00 79.21  ? 147  VAL A O   1 
ATOM 880  C CB  . VAL A 1 283 ? 135.811 126.256 127.559 1.00 84.62  ? 147  VAL A CB  1 
ATOM 881  C CG1 . VAL A 1 283 ? 134.557 127.109 127.709 1.00 83.15  ? 147  VAL A CG1 1 
ATOM 882  C CG2 . VAL A 1 283 ? 135.539 125.064 126.658 1.00 85.75  ? 147  VAL A CG2 1 
ATOM 883  N N   . THR A 1 284 ? 137.692 128.521 128.834 1.00 80.49  ? 148  THR A N   1 
ATOM 884  C CA  . THR A 1 284 ? 137.866 129.797 129.514 1.00 78.47  ? 148  THR A CA  1 
ATOM 885  C C   . THR A 1 284 ? 138.730 130.743 128.693 1.00 74.64  ? 148  THR A C   1 
ATOM 886  O O   . THR A 1 284 ? 138.435 131.936 128.600 1.00 75.81  ? 148  THR A O   1 
ATOM 887  C CB  . THR A 1 284 ? 138.481 129.578 130.894 1.00 76.84  ? 148  THR A CB  1 
ATOM 888  O OG1 . THR A 1 284 ? 137.682 128.646 131.631 1.00 84.08  ? 148  THR A OG1 1 
ATOM 889  C CG2 . THR A 1 284 ? 138.544 130.885 131.656 1.00 70.04  ? 148  THR A CG2 1 
ATOM 890  N N   . CYS A 1 285 ? 139.801 130.229 128.089 1.00 70.72  ? 149  CYS A N   1 
ATOM 891  C CA  . CYS A 1 285 ? 140.669 131.085 127.285 1.00 67.23  ? 149  CYS A CA  1 
ATOM 892  C C   . CYS A 1 285 ? 139.954 131.610 126.045 1.00 72.25  ? 149  CYS A C   1 
ATOM 893  O O   . CYS A 1 285 ? 140.074 132.795 125.710 1.00 73.91  ? 149  CYS A O   1 
ATOM 894  C CB  . CYS A 1 285 ? 141.935 130.332 126.896 1.00 66.64  ? 149  CYS A CB  1 
ATOM 895  S SG  . CYS A 1 285 ? 142.983 129.934 128.298 1.00 83.57  ? 149  CYS A SG  1 
ATOM 896  N N   . ILE A 1 286 ? 139.214 130.749 125.342 1.00 75.60  ? 150  ILE A N   1 
ATOM 897  C CA  . ILE A 1 286 ? 138.509 131.231 124.157 1.00 72.29  ? 150  ILE A CA  1 
ATOM 898  C C   . ILE A 1 286 ? 137.399 132.198 124.549 1.00 69.95  ? 150  ILE A C   1 
ATOM 899  O O   . ILE A 1 286 ? 137.142 133.175 123.837 1.00 70.93  ? 150  ILE A O   1 
ATOM 900  C CB  . ILE A 1 286 ? 137.981 130.064 123.299 1.00 71.62  ? 150  ILE A CB  1 
ATOM 901  C CG1 . ILE A 1 286 ? 136.949 129.234 124.056 1.00 76.12  ? 150  ILE A CG1 1 
ATOM 902  C CG2 . ILE A 1 286 ? 139.130 129.185 122.840 1.00 69.94  ? 150  ILE A CG2 1 
ATOM 903  C CD1 . ILE A 1 286 ? 136.426 128.055 123.271 1.00 75.26  ? 150  ILE A CD1 1 
ATOM 904  N N   . ILE A 1 287 ? 136.743 131.973 125.690 1.00 67.84  ? 151  ILE A N   1 
ATOM 905  C CA  . ILE A 1 287 ? 135.736 132.917 126.161 1.00 69.90  ? 151  ILE A CA  1 
ATOM 906  C C   . ILE A 1 287 ? 136.379 134.248 126.530 1.00 71.55  ? 151  ILE A C   1 
ATOM 907  O O   . ILE A 1 287 ? 135.807 135.315 126.290 1.00 71.74  ? 151  ILE A O   1 
ATOM 908  C CB  . ILE A 1 287 ? 134.954 132.314 127.341 1.00 71.16  ? 151  ILE A CB  1 
ATOM 909  C CG1 . ILE A 1 287 ? 134.030 131.204 126.845 1.00 75.26  ? 151  ILE A CG1 1 
ATOM 910  C CG2 . ILE A 1 287 ? 134.155 133.382 128.065 1.00 72.03  ? 151  ILE A CG2 1 
ATOM 911  C CD1 . ILE A 1 287 ? 133.037 131.664 125.806 1.00 71.05  ? 151  ILE A CD1 1 
ATOM 912  N N   . ILE A 1 288 ? 137.575 134.211 127.117 1.00 69.96  ? 152  ILE A N   1 
ATOM 913  C CA  . ILE A 1 288 ? 138.275 135.443 127.465 1.00 66.05  ? 152  ILE A CA  1 
ATOM 914  C C   . ILE A 1 288 ? 138.639 136.223 126.211 1.00 65.00  ? 152  ILE A C   1 
ATOM 915  O O   . ILE A 1 288 ? 138.479 137.447 126.158 1.00 66.51  ? 152  ILE A O   1 
ATOM 916  C CB  . ILE A 1 288 ? 139.517 135.127 128.314 1.00 63.63  ? 152  ILE A CB  1 
ATOM 917  C CG1 . ILE A 1 288 ? 139.110 134.823 129.753 1.00 61.89  ? 152  ILE A CG1 1 
ATOM 918  C CG2 . ILE A 1 288 ? 140.497 136.275 128.268 1.00 59.36  ? 152  ILE A CG2 1 
ATOM 919  C CD1 . ILE A 1 288 ? 140.265 134.460 130.635 1.00 59.67  ? 152  ILE A CD1 1 
ATOM 920  N N   . TRP A 1 289 ? 139.135 135.534 125.185 1.00 65.11  ? 153  TRP A N   1 
ATOM 921  C CA  . TRP A 1 289 ? 139.449 136.221 123.936 1.00 64.16  ? 153  TRP A CA  1 
ATOM 922  C C   . TRP A 1 289 ? 138.191 136.775 123.277 1.00 65.95  ? 153  TRP A C   1 
ATOM 923  O O   . TRP A 1 289 ? 138.212 137.879 122.723 1.00 68.02  ? 153  TRP A O   1 
ATOM 924  C CB  . TRP A 1 289 ? 140.207 135.287 122.995 1.00 64.07  ? 153  TRP A CB  1 
ATOM 925  C CG  . TRP A 1 289 ? 141.652 135.173 123.364 1.00 65.78  ? 153  TRP A CG  1 
ATOM 926  C CD1 . TRP A 1 289 ? 142.158 134.680 124.527 1.00 67.73  ? 153  TRP A CD1 1 
ATOM 927  C CD2 . TRP A 1 289 ? 142.777 135.574 122.575 1.00 66.85  ? 153  TRP A CD2 1 
ATOM 928  N NE1 . TRP A 1 289 ? 143.528 134.744 124.512 1.00 66.25  ? 153  TRP A NE1 1 
ATOM 929  C CE2 . TRP A 1 289 ? 143.933 135.289 123.324 1.00 67.72  ? 153  TRP A CE2 1 
ATOM 930  C CE3 . TRP A 1 289 ? 142.920 136.140 121.307 1.00 69.36  ? 153  TRP A CE3 1 
ATOM 931  C CZ2 . TRP A 1 289 ? 145.214 135.552 122.848 1.00 69.59  ? 153  TRP A CZ2 1 
ATOM 932  C CZ3 . TRP A 1 289 ? 144.192 136.403 120.837 1.00 70.88  ? 153  TRP A CZ3 1 
ATOM 933  C CH2 . TRP A 1 289 ? 145.322 136.108 121.606 1.00 71.00  ? 153  TRP A CH2 1 
ATOM 934  N N   . LEU A 1 290 ? 137.080 136.040 123.349 1.00 66.70  ? 154  LEU A N   1 
ATOM 935  C CA  . LEU A 1 290 ? 135.823 136.539 122.797 1.00 64.84  ? 154  LEU A CA  1 
ATOM 936  C C   . LEU A 1 290 ? 135.341 137.782 123.539 1.00 66.81  ? 154  LEU A C   1 
ATOM 937  O O   . LEU A 1 290 ? 134.916 138.762 122.919 1.00 70.11  ? 154  LEU A O   1 
ATOM 938  C CB  . LEU A 1 290 ? 134.763 135.442 122.843 1.00 63.82  ? 154  LEU A CB  1 
ATOM 939  C CG  . LEU A 1 290 ? 133.363 135.855 122.396 1.00 67.82  ? 154  LEU A CG  1 
ATOM 940  C CD1 . LEU A 1 290 ? 133.382 136.293 120.945 1.00 69.09  ? 154  LEU A CD1 1 
ATOM 941  C CD2 . LEU A 1 290 ? 132.378 134.718 122.604 1.00 68.60  ? 154  LEU A CD2 1 
ATOM 942  N N   . LEU A 1 291 ? 135.399 137.759 124.872 1.00 66.59  ? 155  LEU A N   1 
ATOM 943  C CA  . LEU A 1 291 ? 134.973 138.914 125.656 1.00 67.65  ? 155  LEU A CA  1 
ATOM 944  C C   . LEU A 1 291 ? 135.878 140.114 125.414 1.00 66.44  ? 155  LEU A C   1 
ATOM 945  O O   . LEU A 1 291 ? 135.400 141.251 125.344 1.00 68.12  ? 155  LEU A O   1 
ATOM 946  C CB  . LEU A 1 291 ? 134.945 138.567 127.143 1.00 66.44  ? 155  LEU A CB  1 
ATOM 947  C CG  . LEU A 1 291 ? 133.907 137.548 127.610 1.00 72.74  ? 155  LEU A CG  1 
ATOM 948  C CD1 . LEU A 1 291 ? 133.910 137.454 129.127 1.00 72.88  ? 155  LEU A CD1 1 
ATOM 949  C CD2 . LEU A 1 291 ? 132.526 137.908 127.090 1.00 77.06  ? 155  LEU A CD2 1 
ATOM 950  N N   . ALA A 1 292 ? 137.188 139.888 125.303 1.00 63.06  ? 156  ALA A N   1 
ATOM 951  C CA  . ALA A 1 292 ? 138.103 140.986 125.026 1.00 59.22  ? 156  ALA A CA  1 
ATOM 952  C C   . ALA A 1 292 ? 137.892 141.553 123.630 1.00 61.75  ? 156  ALA A C   1 
ATOM 953  O O   . ALA A 1 292 ? 138.043 142.762 123.426 1.00 64.10  ? 156  ALA A O   1 
ATOM 954  C CB  . ALA A 1 292 ? 139.545 140.523 125.207 1.00 56.83  ? 156  ALA A CB  1 
ATOM 955  N N   . GLY A 1 293 ? 137.554 140.704 122.658 1.00 60.52  ? 157  GLY A N   1 
ATOM 956  C CA  . GLY A 1 293 ? 137.203 141.210 121.342 1.00 59.86  ? 157  GLY A CA  1 
ATOM 957  C C   . GLY A 1 293 ? 135.913 142.007 121.352 1.00 64.27  ? 157  GLY A C   1 
ATOM 958  O O   . GLY A 1 293 ? 135.790 143.016 120.655 1.00 71.61  ? 157  GLY A O   1 
ATOM 959  N N   . LEU A 1 294 ? 134.930 141.562 122.135 1.00 62.45  ? 158  LEU A N   1 
ATOM 960  C CA  . LEU A 1 294 ? 133.678 142.304 122.241 1.00 65.75  ? 158  LEU A CA  1 
ATOM 961  C C   . LEU A 1 294 ? 133.882 143.643 122.938 1.00 69.05  ? 158  LEU A C   1 
ATOM 962  O O   . LEU A 1 294 ? 133.239 144.637 122.585 1.00 75.15  ? 158  LEU A O   1 
ATOM 963  C CB  . LEU A 1 294 ? 132.630 141.471 122.977 1.00 67.47  ? 158  LEU A CB  1 
ATOM 964  C CG  . LEU A 1 294 ? 131.562 140.801 122.113 1.00 71.88  ? 158  LEU A CG  1 
ATOM 965  C CD1 . LEU A 1 294 ? 132.191 139.895 121.069 1.00 70.09  ? 158  LEU A CD1 1 
ATOM 966  C CD2 . LEU A 1 294 ? 130.594 140.024 122.985 1.00 77.66  ? 158  LEU A CD2 1 
ATOM 967  N N   . ALA A 1 295 ? 134.761 143.688 123.940 1.00 67.36  ? 159  ALA A N   1 
ATOM 968  C CA  . ALA A 1 295 ? 135.010 144.934 124.653 1.00 66.49  ? 159  ALA A CA  1 
ATOM 969  C C   . ALA A 1 295 ? 135.815 145.923 123.823 1.00 66.30  ? 159  ALA A C   1 
ATOM 970  O O   . ALA A 1 295 ? 135.811 147.118 124.131 1.00 68.40  ? 159  ALA A O   1 
ATOM 971  C CB  . ALA A 1 295 ? 135.728 144.651 125.971 1.00 64.10  ? 159  ALA A CB  1 
ATOM 972  N N   . SER A 1 296 ? 136.503 145.456 122.785 1.00 62.64  ? 160  SER A N   1 
ATOM 973  C CA  . SER A 1 296 ? 137.210 146.325 121.859 1.00 63.87  ? 160  SER A CA  1 
ATOM 974  C C   . SER A 1 296 ? 136.376 146.655 120.630 1.00 67.51  ? 160  SER A C   1 
ATOM 975  O O   . SER A 1 296 ? 136.909 147.185 119.652 1.00 69.21  ? 160  SER A O   1 
ATOM 976  C CB  . SER A 1 296 ? 138.532 145.686 121.437 1.00 63.58  ? 160  SER A CB  1 
ATOM 977  O OG  . SER A 1 296 ? 138.307 144.480 120.733 1.00 67.11  ? 160  SER A OG  1 
ATOM 978  N N   . LEU A 1 297 ? 135.088 146.321 120.647 1.00 68.86  ? 161  LEU A N   1 
ATOM 979  C CA  . LEU A 1 297 ? 134.219 146.668 119.528 1.00 70.99  ? 161  LEU A CA  1 
ATOM 980  C C   . LEU A 1 297 ? 134.062 148.170 119.321 1.00 74.74  ? 161  LEU A C   1 
ATOM 981  O O   . LEU A 1 297 ? 134.092 148.603 118.156 1.00 79.34  ? 161  LEU A O   1 
ATOM 982  C CB  . LEU A 1 297 ? 132.852 145.998 119.707 1.00 73.17  ? 161  LEU A CB  1 
ATOM 983  C CG  . LEU A 1 297 ? 132.043 145.807 118.427 1.00 78.57  ? 161  LEU A CG  1 
ATOM 984  C CD1 . LEU A 1 297 ? 132.799 144.907 117.465 1.00 72.88  ? 161  LEU A CD1 1 
ATOM 985  C CD2 . LEU A 1 297 ? 130.672 145.232 118.744 1.00 78.00  ? 161  LEU A CD2 1 
ATOM 986  N N   . PRO A 1 298 ? 133.856 149.004 120.351 1.00 73.89  ? 162  PRO A N   1 
ATOM 987  C CA  . PRO A 1 298 ? 133.757 150.451 120.086 1.00 76.70  ? 162  PRO A CA  1 
ATOM 988  C C   . PRO A 1 298 ? 134.974 151.023 119.382 1.00 76.03  ? 162  PRO A C   1 
ATOM 989  O O   . PRO A 1 298 ? 134.829 151.847 118.470 1.00 78.02  ? 162  PRO A O   1 
ATOM 990  C CB  . PRO A 1 298 ? 133.583 151.047 121.488 1.00 74.84  ? 162  PRO A CB  1 
ATOM 991  C CG  . PRO A 1 298 ? 132.959 149.965 122.273 1.00 74.05  ? 162  PRO A CG  1 
ATOM 992  C CD  . PRO A 1 298 ? 133.563 148.696 121.763 1.00 71.78  ? 162  PRO A CD  1 
ATOM 993  N N   . ALA A 1 299 ? 136.175 150.588 119.761 1.00 70.82  ? 163  ALA A N   1 
ATOM 994  C CA  . ALA A 1 299 ? 137.378 151.099 119.122 1.00 67.12  ? 163  ALA A CA  1 
ATOM 995  C C   . ALA A 1 299 ? 137.546 150.574 117.706 1.00 69.46  ? 163  ALA A C   1 
ATOM 996  O O   . ALA A 1 299 ? 138.211 151.222 116.895 1.00 72.00  ? 163  ALA A O   1 
ATOM 997  C CB  . ALA A 1 299 ? 138.606 150.750 119.960 1.00 66.28  ? 163  ALA A CB  1 
ATOM 998  N N   . ILE A 1 300 ? 136.964 149.416 117.390 1.00 73.24  ? 164  ILE A N   1 
ATOM 999  C CA  . ILE A 1 300 ? 137.038 148.860 116.045 1.00 76.87  ? 164  ILE A CA  1 
ATOM 1000 C C   . ILE A 1 300 ? 135.832 149.242 115.202 1.00 77.03  ? 164  ILE A C   1 
ATOM 1001 O O   . ILE A 1 300 ? 135.735 148.825 114.040 1.00 77.84  ? 164  ILE A O   1 
ATOM 1002 C CB  . ILE A 1 300 ? 137.205 147.325 116.096 1.00 77.24  ? 164  ILE A CB  1 
ATOM 1003 C CG1 . ILE A 1 300 ? 137.876 146.798 114.825 1.00 74.33  ? 164  ILE A CG1 1 
ATOM 1004 C CG2 . ILE A 1 300 ? 135.867 146.641 116.301 1.00 76.43  ? 164  ILE A CG2 1 
ATOM 1005 C CD1 . ILE A 1 300 ? 139.326 147.179 114.693 1.00 70.62  ? 164  ILE A CD1 1 
ATOM 1006 N N   . ILE A 1 301 ? 134.904 150.022 115.750 1.00 74.99  ? 165  ILE A N   1 
ATOM 1007 C CA  . ILE A 1 301 ? 133.745 150.481 114.995 1.00 79.16  ? 165  ILE A CA  1 
ATOM 1008 C C   . ILE A 1 301 ? 133.649 151.998 114.910 1.00 84.68  ? 165  ILE A C   1 
ATOM 1009 O O   . ILE A 1 301 ? 132.894 152.505 114.067 1.00 87.04  ? 165  ILE A O   1 
ATOM 1010 C CB  . ILE A 1 301 ? 132.434 149.899 115.568 1.00 81.94  ? 165  ILE A CB  1 
ATOM 1011 C CG1 . ILE A 1 301 ? 131.357 149.827 114.484 1.00 88.16  ? 165  ILE A CG1 1 
ATOM 1012 C CG2 . ILE A 1 301 ? 131.944 150.730 116.733 1.00 80.79  ? 165  ILE A CG2 1 
ATOM 1013 C CD1 . ILE A 1 301 ? 130.049 149.246 114.967 1.00 92.06  ? 165  ILE A CD1 1 
ATOM 1014 N N   . HIS A 1 302 ? 134.388 152.746 115.731 1.00 83.90  ? 166  HIS A N   1 
ATOM 1015 C CA  . HIS A 1 302 ? 134.349 154.205 115.699 1.00 77.33  ? 166  HIS A CA  1 
ATOM 1016 C C   . HIS A 1 302 ? 135.648 154.851 115.251 1.00 72.64  ? 166  HIS A C   1 
ATOM 1017 O O   . HIS A 1 302 ? 135.608 155.889 114.594 1.00 76.81  ? 166  HIS A O   1 
ATOM 1018 C CB  . HIS A 1 302 ? 133.971 154.756 117.075 1.00 76.66  ? 166  HIS A CB  1 
ATOM 1019 C CG  . HIS A 1 302 ? 132.532 154.555 117.428 1.00 82.40  ? 166  HIS A CG  1 
ATOM 1020 N ND1 . HIS A 1 302 ? 132.105 153.558 118.276 1.00 85.09  ? 166  HIS A ND1 1 
ATOM 1021 C CD2 . HIS A 1 302 ? 131.419 155.220 117.039 1.00 86.97  ? 166  HIS A CD2 1 
ATOM 1022 C CE1 . HIS A 1 302 ? 130.792 153.618 118.398 1.00 90.96  ? 166  HIS A CE1 1 
ATOM 1023 N NE2 . HIS A 1 302 ? 130.351 154.619 117.658 1.00 95.46  ? 166  HIS A NE2 1 
ATOM 1024 N N   . ARG A 1 303 ? 136.797 154.272 115.592 1.00 72.98  ? 167  ARG A N   1 
ATOM 1025 C CA  . ARG A 1 303 ? 138.076 154.857 115.209 1.00 72.48  ? 167  ARG A CA  1 
ATOM 1026 C C   . ARG A 1 303 ? 138.168 155.007 113.698 1.00 76.53  ? 167  ARG A C   1 
ATOM 1027 O O   . ARG A 1 303 ? 137.797 154.102 112.948 1.00 82.10  ? 167  ARG A O   1 
ATOM 1028 C CB  . ARG A 1 303 ? 139.229 153.992 115.716 1.00 74.40  ? 167  ARG A CB  1 
ATOM 1029 C CG  . ARG A 1 303 ? 139.527 154.152 117.184 1.00 72.04  ? 167  ARG A CG  1 
ATOM 1030 C CD  . ARG A 1 303 ? 139.992 155.555 117.470 1.00 76.47  ? 167  ARG A CD  1 
ATOM 1031 N NE  . ARG A 1 303 ? 139.874 155.888 118.882 1.00 78.27  ? 167  ARG A NE  1 
ATOM 1032 C CZ  . ARG A 1 303 ? 140.901 156.048 119.701 1.00 82.96  ? 167  ARG A CZ  1 
ATOM 1033 N NH1 . ARG A 1 303 ? 142.147 155.915 119.281 1.00 87.48  ? 167  ARG A NH1 1 
ATOM 1034 N NH2 . ARG A 1 303 ? 140.672 156.364 120.971 1.00 87.99  ? 167  ARG A NH2 1 
ATOM 1035 N N   . ASN A 1 304 ? 138.659 156.158 113.255 1.00 76.07  ? 168  ASN A N   1 
ATOM 1036 C CA  . ASN A 1 304 ? 138.828 156.422 111.835 1.00 79.13  ? 168  ASN A CA  1 
ATOM 1037 C C   . ASN A 1 304 ? 139.870 157.515 111.675 1.00 80.85  ? 168  ASN A C   1 
ATOM 1038 O O   . ASN A 1 304 ? 140.083 158.328 112.576 1.00 84.02  ? 168  ASN A O   1 
ATOM 1039 C CB  . ASN A 1 304 ? 137.509 156.835 111.179 1.00 84.54  ? 168  ASN A CB  1 
ATOM 1040 C CG  . ASN A 1 304 ? 137.080 155.887 110.080 1.00 90.65  ? 168  ASN A CG  1 
ATOM 1041 O OD1 . ASN A 1 304 ? 137.903 155.202 109.476 1.00 89.24  ? 168  ASN A OD1 1 
ATOM 1042 N ND2 . ASN A 1 304 ? 135.781 155.847 109.810 1.00 91.23  ? 168  ASN A ND2 1 
ATOM 1043 N N   . VAL A 1 305 ? 140.516 157.527 110.510 1.00 82.97  ? 169  VAL A N   1 
ATOM 1044 C CA  . VAL A 1 305 ? 141.496 158.564 110.228 1.00 87.80  ? 169  VAL A CA  1 
ATOM 1045 C C   . VAL A 1 305 ? 140.781 159.900 110.070 1.00 86.91  ? 169  VAL A C   1 
ATOM 1046 O O   . VAL A 1 305 ? 139.610 159.965 109.673 1.00 86.20  ? 169  VAL A O   1 
ATOM 1047 C CB  . VAL A 1 305 ? 142.323 158.211 108.978 1.00 91.11  ? 169  VAL A CB  1 
ATOM 1048 C CG1 . VAL A 1 305 ? 141.535 158.496 107.709 1.00 91.58  ? 169  VAL A CG1 1 
ATOM 1049 C CG2 . VAL A 1 305 ? 143.647 158.956 108.984 1.00 93.10  ? 169  VAL A CG2 1 
ATOM 1050 N N   . PHE A 1 306 ? 141.481 160.981 110.403 1.00 87.62  ? 170  PHE A N   1 
ATOM 1051 C CA  . PHE A 1 306 ? 140.870 162.305 110.405 1.00 88.50  ? 170  PHE A CA  1 
ATOM 1052 C C   . PHE A 1 306 ? 141.917 163.336 110.021 1.00 95.99  ? 170  PHE A C   1 
ATOM 1053 O O   . PHE A 1 306 ? 142.912 163.500 110.729 1.00 101.49 ? 170  PHE A O   1 
ATOM 1054 C CB  . PHE A 1 306 ? 140.276 162.623 111.777 1.00 87.77  ? 170  PHE A CB  1 
ATOM 1055 C CG  . PHE A 1 306 ? 139.541 163.929 111.836 1.00 92.90  ? 170  PHE A CG  1 
ATOM 1056 C CD1 . PHE A 1 306 ? 138.556 164.228 110.914 1.00 95.99  ? 170  PHE A CD1 1 
ATOM 1057 C CD2 . PHE A 1 306 ? 139.818 164.849 112.829 1.00 95.11  ? 170  PHE A CD2 1 
ATOM 1058 C CE1 . PHE A 1 306 ? 137.874 165.424 110.973 1.00 98.78  ? 170  PHE A CE1 1 
ATOM 1059 C CE2 . PHE A 1 306 ? 139.136 166.046 112.892 1.00 95.96  ? 170  PHE A CE2 1 
ATOM 1060 C CZ  . PHE A 1 306 ? 138.164 166.333 111.964 1.00 97.39  ? 170  PHE A CZ  1 
ATOM 1061 N N   . PHE A 1 307 ? 141.684 164.034 108.913 1.00 96.91  ? 171  PHE A N   1 
ATOM 1062 C CA  . PHE A 1 307 ? 142.580 165.093 108.465 1.00 98.50  ? 171  PHE A CA  1 
ATOM 1063 C C   . PHE A 1 307 ? 142.404 166.309 109.366 1.00 103.64 ? 171  PHE A C   1 
ATOM 1064 O O   . PHE A 1 307 ? 141.287 166.816 109.522 1.00 106.20 ? 171  PHE A O   1 
ATOM 1065 C CB  . PHE A 1 307 ? 142.291 165.447 107.009 1.00 100.07 ? 171  PHE A CB  1 
ATOM 1066 C CG  . PHE A 1 307 ? 142.399 164.281 106.064 1.00 102.51 ? 171  PHE A CG  1 
ATOM 1067 C CD1 . PHE A 1 307 ? 141.337 163.409 105.891 1.00 102.34 ? 171  PHE A CD1 1 
ATOM 1068 C CD2 . PHE A 1 307 ? 143.559 164.065 105.344 1.00 101.62 ? 171  PHE A CD2 1 
ATOM 1069 C CE1 . PHE A 1 307 ? 141.435 162.341 105.026 1.00 100.70 ? 171  PHE A CE1 1 
ATOM 1070 C CE2 . PHE A 1 307 ? 143.662 162.998 104.478 1.00 99.31  ? 171  PHE A CE2 1 
ATOM 1071 C CZ  . PHE A 1 307 ? 142.599 162.136 104.319 1.00 101.11 ? 171  PHE A CZ  1 
ATOM 1072 N N   . ILE A 1 308 ? 143.501 166.782 109.952 1.00 108.47 ? 172  ILE A N   1 
ATOM 1073 C CA  . ILE A 1 308 ? 143.453 167.846 110.951 1.00 113.10 ? 172  ILE A CA  1 
ATOM 1074 C C   . ILE A 1 308 ? 143.524 169.183 110.218 1.00 122.11 ? 172  ILE A C   1 
ATOM 1075 O O   . ILE A 1 308 ? 144.591 169.614 109.776 1.00 123.59 ? 172  ILE A O   1 
ATOM 1076 C CB  . ILE A 1 308 ? 144.571 167.709 111.983 1.00 112.64 ? 172  ILE A CB  1 
ATOM 1077 C CG1 . ILE A 1 308 ? 144.355 166.459 112.830 1.00 109.15 ? 172  ILE A CG1 1 
ATOM 1078 C CG2 . ILE A 1 308 ? 144.617 168.934 112.879 1.00 116.28 ? 172  ILE A CG2 1 
ATOM 1079 C CD1 . ILE A 1 308 ? 145.252 166.383 114.039 1.00 111.29 ? 172  ILE A CD1 1 
ATOM 1080 N N   . GLU A 1 309 ? 142.372 169.828 110.082 1.00 124.56 ? 173  GLU A N   1 
ATOM 1081 C CA  . GLU A 1 309 ? 142.226 171.167 109.500 1.00 125.82 ? 173  GLU A CA  1 
ATOM 1082 C C   . GLU A 1 309 ? 142.785 171.170 108.076 1.00 125.50 ? 173  GLU A C   1 
ATOM 1083 O O   . GLU A 1 309 ? 142.766 170.149 107.377 1.00 120.81 ? 173  GLU A O   1 
ATOM 1084 C CB  . GLU A 1 309 ? 142.858 172.199 110.415 1.00 128.90 ? 173  GLU A CB  1 
ATOM 1085 C CG  . GLU A 1 309 ? 142.296 172.230 111.825 1.00 126.68 ? 173  GLU A CG  1 
ATOM 1086 C CD  . GLU A 1 309 ? 142.930 173.324 112.662 1.00 129.41 ? 173  GLU A CD  1 
ATOM 1087 O OE1 . GLU A 1 309 ? 143.198 174.408 112.103 1.00 130.43 ? 173  GLU A OE1 1 
ATOM 1088 O OE2 . GLU A 1 309 ? 143.164 173.106 113.870 1.00 132.07 ? 173  GLU A OE2 1 
ATOM 1089 N N   . ASN A 1 310 ? 143.269 172.332 107.636 1.00 129.32 ? 174  ASN A N   1 
ATOM 1090 C CA  . ASN A 1 310 ? 143.790 172.489 106.288 1.00 130.79 ? 174  ASN A CA  1 
ATOM 1091 C C   . ASN A 1 310 ? 145.171 171.875 106.118 1.00 129.50 ? 174  ASN A C   1 
ATOM 1092 O O   . ASN A 1 310 ? 145.626 171.727 104.980 1.00 130.91 ? 174  ASN A O   1 
ATOM 1093 C CB  . ASN A 1 310 ? 143.830 173.970 105.920 1.00 132.22 ? 174  ASN A CB  1 
ATOM 1094 C CG  . ASN A 1 310 ? 143.591 174.211 104.448 1.00 135.84 ? 174  ASN A CG  1 
ATOM 1095 O OD1 . ASN A 1 310 ? 143.858 173.349 103.611 1.00 136.19 ? 174  ASN A OD1 1 
ATOM 1096 N ND2 . ASN A 1 310 ? 143.078 175.388 104.120 1.00 136.28 ? 174  ASN A ND2 1 
ATOM 1097 N N   . THR A 1 311 ? 145.844 171.521 107.209 1.00 127.44 ? 175  THR A N   1 
ATOM 1098 C CA  . THR A 1 311 ? 147.130 170.849 107.116 1.00 129.26 ? 175  THR A CA  1 
ATOM 1099 C C   . THR A 1 311 ? 146.934 169.419 106.614 1.00 128.10 ? 175  THR A C   1 
ATOM 1100 O O   . THR A 1 311 ? 145.819 168.970 106.336 1.00 127.98 ? 175  THR A O   1 
ATOM 1101 C CB  . THR A 1 311 ? 147.833 170.853 108.470 1.00 127.22 ? 175  THR A CB  1 
ATOM 1102 O OG1 . THR A 1 311 ? 147.041 170.131 109.420 1.00 123.50 ? 175  THR A OG1 1 
ATOM 1103 C CG2 . THR A 1 311 ? 148.021 172.275 108.964 1.00 126.22 ? 175  THR A CG2 1 
ATOM 1104 N N   . ASN A 1 312 ? 148.041 168.691 106.494 1.00 124.75 ? 176  ASN A N   1 
ATOM 1105 C CA  . ASN A 1 312 ? 148.009 167.296 106.084 1.00 124.97 ? 176  ASN A CA  1 
ATOM 1106 C C   . ASN A 1 312 ? 148.140 166.339 107.260 1.00 121.68 ? 176  ASN A C   1 
ATOM 1107 O O   . ASN A 1 312 ? 148.335 165.137 107.050 1.00 121.18 ? 176  ASN A O   1 
ATOM 1108 C CB  . ASN A 1 312 ? 149.107 167.021 105.055 1.00 129.03 ? 176  ASN A CB  1 
ATOM 1109 C CG  . ASN A 1 312 ? 148.841 167.701 103.725 1.00 133.41 ? 176  ASN A CG  1 
ATOM 1110 O OD1 . ASN A 1 312 ? 148.027 168.621 103.641 1.00 134.20 ? 176  ASN A OD1 1 
ATOM 1111 N ND2 . ASN A 1 312 ? 149.528 167.253 102.679 1.00 132.24 ? 176  ASN A ND2 1 
ATOM 1112 N N   . ILE A 1 313 ? 148.032 166.842 108.488 1.00 117.97 ? 177  ILE A N   1 
ATOM 1113 C CA  . ILE A 1 313 ? 148.150 165.990 109.665 1.00 114.28 ? 177  ILE A CA  1 
ATOM 1114 C C   . ILE A 1 313 ? 146.930 165.083 109.743 1.00 108.08 ? 177  ILE A C   1 
ATOM 1115 O O   . ILE A 1 313 ? 145.791 165.555 109.837 1.00 108.04 ? 177  ILE A O   1 
ATOM 1116 C CB  . ILE A 1 313 ? 148.295 166.832 110.937 1.00 113.56 ? 177  ILE A CB  1 
ATOM 1117 C CG1 . ILE A 1 313 ? 149.526 167.731 110.846 1.00 114.61 ? 177  ILE A CG1 1 
ATOM 1118 C CG2 . ILE A 1 313 ? 148.381 165.934 112.155 1.00 110.22 ? 177  ILE A CG2 1 
ATOM 1119 C CD1 . ILE A 1 313 ? 149.733 168.597 112.066 1.00 116.93 ? 177  ILE A CD1 1 
ATOM 1120 N N   . THR A 1 314 ? 147.164 163.776 109.695 1.00 101.24 ? 178  THR A N   1 
ATOM 1121 C CA  . THR A 1 314 ? 146.116 162.775 109.830 1.00 100.36 ? 178  THR A CA  1 
ATOM 1122 C C   . THR A 1 314 ? 146.373 161.970 111.094 1.00 99.96  ? 178  THR A C   1 
ATOM 1123 O O   . THR A 1 314 ? 147.512 161.573 111.356 1.00 103.71 ? 178  THR A O   1 
ATOM 1124 C CB  . THR A 1 314 ? 146.080 161.852 108.614 1.00 100.67 ? 178  THR A CB  1 
ATOM 1125 O OG1 . THR A 1 314 ? 147.231 161.002 108.631 1.00 105.59 ? 178  THR A OG1 1 
ATOM 1126 C CG2 . THR A 1 314 ? 146.093 162.668 107.339 1.00 102.87 ? 178  THR A CG2 1 
ATOM 1127 N N   . VAL A 1 315 ? 145.323 161.735 111.879 1.00 97.61  ? 179  VAL A N   1 
ATOM 1128 C CA  . VAL A 1 315 ? 145.457 161.064 113.164 1.00 94.25  ? 179  VAL A CA  1 
ATOM 1129 C C   . VAL A 1 315 ? 144.392 159.985 113.293 1.00 91.22  ? 179  VAL A C   1 
ATOM 1130 O O   . VAL A 1 315 ? 143.400 159.961 112.563 1.00 93.48  ? 179  VAL A O   1 
ATOM 1131 C CB  . VAL A 1 315 ? 145.365 162.052 114.343 1.00 93.97  ? 179  VAL A CB  1 
ATOM 1132 C CG1 . VAL A 1 315 ? 146.569 162.973 114.351 1.00 98.78  ? 179  VAL A CG1 1 
ATOM 1133 C CG2 . VAL A 1 315 ? 144.082 162.854 114.258 1.00 92.87  ? 179  VAL A CG2 1 
ATOM 1134 N N   . CYS A 1 316 ? 144.620 159.078 114.241 1.00 88.02  ? 180  CYS A N   1 
ATOM 1135 C CA  . CYS A 1 316 ? 143.700 157.981 114.539 1.00 85.31  ? 180  CYS A CA  1 
ATOM 1136 C C   . CYS A 1 316 ? 142.667 158.497 115.532 1.00 85.51  ? 180  CYS A C   1 
ATOM 1137 O O   . CYS A 1 316 ? 142.812 158.353 116.745 1.00 88.18  ? 180  CYS A O   1 
ATOM 1138 C CB  . CYS A 1 316 ? 144.468 156.784 115.080 1.00 87.71  ? 180  CYS A CB  1 
ATOM 1139 S SG  . CYS A 1 316 ? 143.490 155.329 115.482 1.00 88.33  ? 180  CYS A SG  1 
ATOM 1140 N N   . ALA A 1 317 ? 141.607 159.102 115.010 1.00 81.71  ? 181  ALA A N   1 
ATOM 1141 C CA  . ALA A 1 317 ? 140.639 159.822 115.821 1.00 78.37  ? 181  ALA A CA  1 
ATOM 1142 C C   . ALA A 1 317 ? 139.426 158.958 116.137 1.00 78.45  ? 181  ALA A C   1 
ATOM 1143 O O   . ALA A 1 317 ? 139.049 158.075 115.366 1.00 83.63  ? 181  ALA A O   1 
ATOM 1144 C CB  . ALA A 1 317 ? 140.186 161.095 115.110 1.00 81.67  ? 181  ALA A CB  1 
ATOM 1145 N N   . PHE A 1 318 ? 138.811 159.236 117.282 1.00 77.99  ? 182  PHE A N   1 
ATOM 1146 C CA  . PHE A 1 318 ? 137.584 158.578 117.706 1.00 76.46  ? 182  PHE A CA  1 
ATOM 1147 C C   . PHE A 1 318 ? 136.414 159.488 117.360 1.00 78.86  ? 182  PHE A C   1 
ATOM 1148 O O   . PHE A 1 318 ? 136.372 160.639 117.800 1.00 87.70  ? 182  PHE A O   1 
ATOM 1149 C CB  . PHE A 1 318 ? 137.616 158.287 119.206 1.00 80.34  ? 182  PHE A CB  1 
ATOM 1150 C CG  . PHE A 1 318 ? 136.507 157.391 119.680 1.00 82.70  ? 182  PHE A CG  1 
ATOM 1151 C CD1 . PHE A 1 318 ? 135.263 157.907 119.991 1.00 83.07  ? 182  PHE A CD1 1 
ATOM 1152 C CD2 . PHE A 1 318 ? 136.715 156.033 119.828 1.00 83.36  ? 182  PHE A CD2 1 
ATOM 1153 C CE1 . PHE A 1 318 ? 134.247 157.084 120.428 1.00 84.37  ? 182  PHE A CE1 1 
ATOM 1154 C CE2 . PHE A 1 318 ? 135.702 155.208 120.266 1.00 80.35  ? 182  PHE A CE2 1 
ATOM 1155 C CZ  . PHE A 1 318 ? 134.468 155.734 120.566 1.00 82.13  ? 182  PHE A CZ  1 
ATOM 1156 N N   . HIS A 1 319 ? 135.470 158.978 116.580 1.00 75.13  ? 183  HIS A N   1 
ATOM 1157 C CA  . HIS A 1 319 ? 134.336 159.763 116.101 1.00 76.03  ? 183  HIS A CA  1 
ATOM 1158 C C   . HIS A 1 319 ? 133.066 159.260 116.774 1.00 82.51  ? 183  HIS A C   1 
ATOM 1159 O O   . HIS A 1 319 ? 132.486 158.258 116.348 1.00 89.17  ? 183  HIS A O   1 
ATOM 1160 C CB  . HIS A 1 319 ? 134.217 159.671 114.586 1.00 76.11  ? 183  HIS A CB  1 
ATOM 1161 C CG  . HIS A 1 319 ? 135.462 160.055 113.856 1.00 76.74  ? 183  HIS A CG  1 
ATOM 1162 N ND1 . HIS A 1 319 ? 135.668 161.318 113.351 1.00 80.39  ? 183  HIS A ND1 1 
ATOM 1163 C CD2 . HIS A 1 319 ? 136.564 159.338 113.536 1.00 79.30  ? 183  HIS A CD2 1 
ATOM 1164 C CE1 . HIS A 1 319 ? 136.844 161.365 112.753 1.00 83.87  ? 183  HIS A CE1 1 
ATOM 1165 N NE2 . HIS A 1 319 ? 137.408 160.176 112.852 1.00 82.81  ? 183  HIS A NE2 1 
ATOM 1166 N N   . TYR A 1 320 ? 132.625 159.961 117.814 1.00 86.39  ? 184  TYR A N   1 
ATOM 1167 C CA  . TYR A 1 320 ? 131.377 159.644 118.499 1.00 91.36  ? 184  TYR A CA  1 
ATOM 1168 C C   . TYR A 1 320 ? 130.361 160.733 118.184 1.00 98.64  ? 184  TYR A C   1 
ATOM 1169 O O   . TYR A 1 320 ? 130.598 161.910 118.467 1.00 101.24 ? 184  TYR A O   1 
ATOM 1170 C CB  . TYR A 1 320 ? 131.589 159.505 120.007 1.00 91.13  ? 184  TYR A CB  1 
ATOM 1171 C CG  . TYR A 1 320 ? 132.011 160.768 120.715 1.00 93.23  ? 184  TYR A CG  1 
ATOM 1172 C CD1 . TYR A 1 320 ? 133.318 161.222 120.647 1.00 93.27  ? 184  TYR A CD1 1 
ATOM 1173 C CD2 . TYR A 1 320 ? 131.104 161.498 121.469 1.00 98.54  ? 184  TYR A CD2 1 
ATOM 1174 C CE1 . TYR A 1 320 ? 133.708 162.374 121.299 1.00 94.15  ? 184  TYR A CE1 1 
ATOM 1175 C CE2 . TYR A 1 320 ? 131.486 162.650 122.125 1.00 100.70 ? 184  TYR A CE2 1 
ATOM 1176 C CZ  . TYR A 1 320 ? 132.789 163.084 122.036 1.00 95.80  ? 184  TYR A CZ  1 
ATOM 1177 O OH  . TYR A 1 320 ? 133.176 164.231 122.687 1.00 92.14  ? 184  TYR A OH  1 
ATOM 1178 N N   . GLU A 1 321 ? 129.233 160.334 117.603 1.00 104.59 ? 185  GLU A N   1 
ATOM 1179 C CA  . GLU A 1 321 ? 128.240 161.272 117.098 1.00 108.23 ? 185  GLU A CA  1 
ATOM 1180 C C   . GLU A 1 321 ? 127.286 161.685 118.218 1.00 112.23 ? 185  GLU A C   1 
ATOM 1181 O O   . GLU A 1 321 ? 127.516 161.418 119.400 1.00 111.55 ? 185  GLU A O   1 
ATOM 1182 C CB  . GLU A 1 321 ? 127.502 160.652 115.915 1.00 108.72 ? 185  GLU A CB  1 
ATOM 1183 C CG  . GLU A 1 321 ? 127.065 159.218 116.157 1.00 112.13 ? 185  GLU A CG  1 
ATOM 1184 C CD  . GLU A 1 321 ? 126.928 158.425 114.873 1.00 115.79 ? 185  GLU A CD  1 
ATOM 1185 O OE1 . GLU A 1 321 ? 126.585 159.026 113.833 1.00 109.16 ? 185  GLU A OE1 1 
ATOM 1186 O OE2 . GLU A 1 321 ? 127.174 157.201 114.902 1.00 118.19 ? 185  GLU A OE2 1 
ATOM 1187 N N   . SER A 1 322 ? 126.197 162.363 117.847 1.00 113.47 ? 186  SER A N   1 
ATOM 1188 C CA  . SER A 1 322 ? 125.206 162.779 118.835 1.00 116.40 ? 186  SER A CA  1 
ATOM 1189 C C   . SER A 1 322 ? 124.403 161.597 119.366 1.00 118.06 ? 186  SER A C   1 
ATOM 1190 O O   . SER A 1 322 ? 124.009 161.598 120.537 1.00 114.81 ? 186  SER A O   1 
ATOM 1191 C CB  . SER A 1 322 ? 124.271 163.827 118.233 1.00 115.81 ? 186  SER A CB  1 
ATOM 1192 O OG  . SER A 1 322 ? 124.982 164.993 117.860 1.00 113.35 ? 186  SER A OG  1 
ATOM 1193 N N   . GLN A 1 323 ? 124.144 160.592 118.525 1.00 118.60 ? 187  GLN A N   1 
ATOM 1194 C CA  . GLN A 1 323 ? 123.407 159.417 118.981 1.00 118.31 ? 187  GLN A CA  1 
ATOM 1195 C C   . GLN A 1 323 ? 124.157 158.693 120.090 1.00 118.70 ? 187  GLN A C   1 
ATOM 1196 O O   . GLN A 1 323 ? 123.555 158.255 121.077 1.00 119.30 ? 187  GLN A O   1 
ATOM 1197 C CB  . GLN A 1 323 ? 123.149 158.466 117.813 1.00 119.78 ? 187  GLN A CB  1 
ATOM 1198 C CG  . GLN A 1 323 ? 122.110 158.947 116.818 1.00 124.26 ? 187  GLN A CG  1 
ATOM 1199 C CD  . GLN A 1 323 ? 121.747 157.877 115.803 1.00 127.80 ? 187  GLN A CD  1 
ATOM 1200 O OE1 . GLN A 1 323 ? 122.423 156.854 115.696 1.00 124.60 ? 187  GLN A OE1 1 
ATOM 1201 N NE2 . GLN A 1 323 ? 120.672 158.107 115.058 1.00 128.32 ? 187  GLN A NE2 1 
ATOM 1202 N N   . ASN A 1 324 ? 125.474 158.563 119.948 1.00 116.97 ? 188  ASN A N   1 
ATOM 1203 C CA  . ASN A 1 324 ? 126.320 157.841 120.894 1.00 113.31 ? 188  ASN A CA  1 
ATOM 1204 C C   . ASN A 1 324 ? 127.018 158.786 121.859 1.00 109.52 ? 188  ASN A C   1 
ATOM 1205 O O   . ASN A 1 324 ? 128.177 158.571 122.218 1.00 107.89 ? 188  ASN A O   1 
ATOM 1206 C CB  . ASN A 1 324 ? 127.341 156.994 120.144 1.00 109.86 ? 188  ASN A CB  1 
ATOM 1207 C CG  . ASN A 1 324 ? 126.775 156.389 118.880 1.00 114.17 ? 188  ASN A CG  1 
ATOM 1208 O OD1 . ASN A 1 324 ? 125.595 156.045 118.816 1.00 115.02 ? 188  ASN A OD1 1 
ATOM 1209 N ND2 . ASN A 1 324 ? 127.614 156.264 117.858 1.00 111.60 ? 188  ASN A ND2 1 
ATOM 1210 N N   . SER A 1 325 ? 126.339 159.849 122.280 1.00 109.83 ? 189  SER A N   1 
ATOM 1211 C CA  . SER A 1 325 ? 126.960 160.833 123.154 1.00 109.53 ? 189  SER A CA  1 
ATOM 1212 C C   . SER A 1 325 ? 127.356 160.198 124.483 1.00 106.87 ? 189  SER A C   1 
ATOM 1213 O O   . SER A 1 325 ? 126.768 159.208 124.925 1.00 107.01 ? 189  SER A O   1 
ATOM 1214 C CB  . SER A 1 325 ? 126.011 162.007 123.392 1.00 110.53 ? 189  SER A CB  1 
ATOM 1215 O OG  . SER A 1 325 ? 126.648 163.030 124.136 1.00 110.22 ? 189  SER A OG  1 
ATOM 1216 N N   . THR A 1 326 ? 128.385 160.774 125.107 1.00 104.08 ? 190  THR A N   1 
ATOM 1217 C CA  . THR A 1 326 ? 128.969 160.290 126.358 1.00 104.86 ? 190  THR A CA  1 
ATOM 1218 C C   . THR A 1 326 ? 129.529 158.876 126.232 1.00 102.05 ? 190  THR A C   1 
ATOM 1219 O O   . THR A 1 326 ? 129.734 158.196 127.242 1.00 99.92  ? 190  THR A O   1 
ATOM 1220 C CB  . THR A 1 326 ? 127.968 160.351 127.520 1.00 107.88 ? 190  THR A CB  1 
ATOM 1221 O OG1 . THR A 1 326 ? 126.907 159.415 127.296 1.00 109.13 ? 190  THR A OG1 1 
ATOM 1222 C CG2 . THR A 1 326 ? 127.387 161.750 127.655 1.00 106.10 ? 190  THR A CG2 1 
ATOM 1223 N N   . LEU A 1 327 ? 129.772 158.411 125.008 1.00 100.68 ? 191  LEU A N   1 
ATOM 1224 C CA  . LEU A 1 327 ? 130.439 157.124 124.834 1.00 94.60  ? 191  LEU A CA  1 
ATOM 1225 C C   . LEU A 1 327 ? 131.854 157.105 125.400 1.00 91.33  ? 191  LEU A C   1 
ATOM 1226 O O   . LEU A 1 327 ? 132.214 156.099 126.037 1.00 91.35  ? 191  LEU A O   1 
ATOM 1227 C CB  . LEU A 1 327 ? 130.438 156.725 123.354 1.00 92.29  ? 191  LEU A CB  1 
ATOM 1228 C CG  . LEU A 1 327 ? 131.024 155.354 123.021 1.00 85.71  ? 191  LEU A CG  1 
ATOM 1229 C CD1 . LEU A 1 327 ? 130.310 154.273 123.798 1.00 81.61  ? 191  LEU A CD1 1 
ATOM 1230 C CD2 . LEU A 1 327 ? 130.928 155.091 121.536 1.00 86.43  ? 191  LEU A CD2 1 
ATOM 1231 N N   . PRO A 1 328 ? 132.703 158.124 125.197 1.00 91.97  ? 192  PRO A N   1 
ATOM 1232 C CA  . PRO A 1 328 ? 134.026 158.087 125.842 1.00 94.43  ? 192  PRO A CA  1 
ATOM 1233 C C   . PRO A 1 328 ? 133.951 157.988 127.354 1.00 92.26  ? 192  PRO A C   1 
ATOM 1234 O O   . PRO A 1 328 ? 134.795 157.326 127.972 1.00 90.80  ? 192  PRO A O   1 
ATOM 1235 C CB  . PRO A 1 328 ? 134.669 159.403 125.388 1.00 97.02  ? 192  PRO A CB  1 
ATOM 1236 C CG  . PRO A 1 328 ? 134.002 159.713 124.107 1.00 95.52  ? 192  PRO A CG  1 
ATOM 1237 C CD  . PRO A 1 328 ? 132.586 159.270 124.279 1.00 93.83  ? 192  PRO A CD  1 
ATOM 1238 N N   . ILE A 1 329 ? 132.953 158.625 127.968 1.00 93.07  ? 193  ILE A N   1 
ATOM 1239 C CA  . ILE A 1 329 ? 132.760 158.496 129.409 1.00 94.08  ? 193  ILE A CA  1 
ATOM 1240 C C   . ILE A 1 329 ? 132.494 157.041 129.773 1.00 91.25  ? 193  ILE A C   1 
ATOM 1241 O O   . ILE A 1 329 ? 133.074 156.499 130.722 1.00 89.48  ? 193  ILE A O   1 
ATOM 1242 C CB  . ILE A 1 329 ? 131.617 159.413 129.883 1.00 95.20  ? 193  ILE A CB  1 
ATOM 1243 C CG1 . ILE A 1 329 ? 132.067 160.877 129.919 1.00 99.95  ? 193  ILE A CG1 1 
ATOM 1244 C CG2 . ILE A 1 329 ? 131.105 158.974 131.244 1.00 94.62  ? 193  ILE A CG2 1 
ATOM 1245 C CD1 . ILE A 1 329 ? 131.957 161.599 128.592 1.00 101.72 ? 193  ILE A CD1 1 
ATOM 1246 N N   . GLY A 1 330 ? 131.621 156.383 129.009 1.00 89.23  ? 194  GLY A N   1 
ATOM 1247 C CA  . GLY A 1 330 ? 131.330 154.985 129.275 1.00 87.48  ? 194  GLY A CA  1 
ATOM 1248 C C   . GLY A 1 330 ? 132.539 154.089 129.095 1.00 83.21  ? 194  GLY A C   1 
ATOM 1249 O O   . GLY A 1 330 ? 132.768 153.176 129.889 1.00 81.45  ? 194  GLY A O   1 
ATOM 1250 N N   . LEU A 1 331 ? 133.326 154.332 128.045 1.00 82.30  ? 195  LEU A N   1 
ATOM 1251 C CA  . LEU A 1 331 ? 134.514 153.515 127.817 1.00 79.58  ? 195  LEU A CA  1 
ATOM 1252 C C   . LEU A 1 331 ? 135.542 153.711 128.924 1.00 78.57  ? 195  LEU A C   1 
ATOM 1253 O O   . LEU A 1 331 ? 136.162 152.743 129.380 1.00 76.91  ? 195  LEU A O   1 
ATOM 1254 C CB  . LEU A 1 331 ? 135.121 153.836 126.453 1.00 77.28  ? 195  LEU A CB  1 
ATOM 1255 C CG  . LEU A 1 331 ? 134.215 153.587 125.249 1.00 77.31  ? 195  LEU A CG  1 
ATOM 1256 C CD1 . LEU A 1 331 ? 135.010 153.677 123.960 1.00 78.85  ? 195  LEU A CD1 1 
ATOM 1257 C CD2 . LEU A 1 331 ? 133.526 152.243 125.363 1.00 77.47  ? 195  LEU A CD2 1 
ATOM 1258 N N   . GLY A 1 332 ? 135.738 154.952 129.371 1.00 79.85  ? 196  GLY A N   1 
ATOM 1259 C CA  . GLY A 1 332 ? 136.642 155.189 130.483 1.00 76.15  ? 196  GLY A CA  1 
ATOM 1260 C C   . GLY A 1 332 ? 136.170 154.528 131.763 1.00 75.45  ? 196  GLY A C   1 
ATOM 1261 O O   . GLY A 1 332 ? 136.969 153.965 132.515 1.00 73.51  ? 196  GLY A O   1 
ATOM 1262 N N   . LEU A 1 333 ? 134.862 154.585 132.027 1.00 77.60  ? 197  LEU A N   1 
ATOM 1263 C CA  . LEU A 1 333 ? 134.323 153.925 133.212 1.00 77.87  ? 197  LEU A CA  1 
ATOM 1264 C C   . LEU A 1 333 ? 134.480 152.413 133.124 1.00 76.41  ? 197  LEU A C   1 
ATOM 1265 O O   . LEU A 1 333 ? 134.762 151.756 134.130 1.00 74.99  ? 197  LEU A O   1 
ATOM 1266 C CB  . LEU A 1 333 ? 132.857 154.306 133.407 1.00 83.25  ? 197  LEU A CB  1 
ATOM 1267 C CG  . LEU A 1 333 ? 132.597 155.748 133.844 1.00 88.28  ? 197  LEU A CG  1 
ATOM 1268 C CD1 . LEU A 1 333 ? 131.119 155.967 134.113 1.00 91.67  ? 197  LEU A CD1 1 
ATOM 1269 C CD2 . LEU A 1 333 ? 133.427 156.093 135.069 1.00 83.52  ? 197  LEU A CD2 1 
ATOM 1270 N N   . THR A 1 334 ? 134.290 151.840 131.934 1.00 74.87  ? 198  THR A N   1 
ATOM 1271 C CA  . THR A 1 334 ? 134.492 150.404 131.768 1.00 70.08  ? 198  THR A CA  1 
ATOM 1272 C C   . THR A 1 334 ? 135.951 150.024 131.981 1.00 67.24  ? 198  THR A C   1 
ATOM 1273 O O   . THR A 1 334 ? 136.245 149.001 132.608 1.00 67.30  ? 198  THR A O   1 
ATOM 1274 C CB  . THR A 1 334 ? 134.021 149.962 130.385 1.00 67.33  ? 198  THR A CB  1 
ATOM 1275 O OG1 . THR A 1 334 ? 132.655 150.350 130.200 1.00 74.38  ? 198  THR A OG1 1 
ATOM 1276 C CG2 . THR A 1 334 ? 134.126 148.457 130.247 1.00 63.67  ? 198  THR A CG2 1 
ATOM 1277 N N   . LYS A 1 335 ? 136.879 150.831 131.465 1.00 66.55  ? 199  LYS A N   1 
ATOM 1278 C CA  . LYS A 1 335 ? 138.296 150.553 131.681 1.00 63.14  ? 199  LYS A CA  1 
ATOM 1279 C C   . LYS A 1 335 ? 138.660 150.642 133.157 1.00 67.60  ? 199  LYS A C   1 
ATOM 1280 O O   . LYS A 1 335 ? 139.433 149.822 133.661 1.00 70.68  ? 199  LYS A O   1 
ATOM 1281 C CB  . LYS A 1 335 ? 139.158 151.513 130.865 1.00 67.88  ? 199  LYS A CB  1 
ATOM 1282 C CG  . LYS A 1 335 ? 139.294 151.154 129.397 1.00 65.18  ? 199  LYS A CG  1 
ATOM 1283 C CD  . LYS A 1 335 ? 140.320 152.051 128.725 1.00 67.76  ? 199  LYS A CD  1 
ATOM 1284 C CE  . LYS A 1 335 ? 140.629 151.592 127.312 1.00 70.20  ? 199  LYS A CE  1 
ATOM 1285 N NZ  . LYS A 1 335 ? 139.434 151.648 126.432 1.00 74.83  ? 199  LYS A NZ  1 
ATOM 1286 N N   . ASN A 1 336 ? 138.122 151.637 133.864 1.00 69.99  ? 200  ASN A N   1 
ATOM 1287 C CA  . ASN A 1 336 ? 138.470 151.814 135.271 1.00 72.11  ? 200  ASN A CA  1 
ATOM 1288 C C   . ASN A 1 336 ? 137.770 150.817 136.187 1.00 72.46  ? 200  ASN A C   1 
ATOM 1289 O O   . ASN A 1 336 ? 138.289 150.512 137.265 1.00 72.24  ? 200  ASN A O   1 
ATOM 1290 C CB  . ASN A 1 336 ? 138.147 153.238 135.719 1.00 74.84  ? 200  ASN A CB  1 
ATOM 1291 C CG  . ASN A 1 336 ? 139.313 154.180 135.535 1.00 83.32  ? 200  ASN A CG  1 
ATOM 1292 O OD1 . ASN A 1 336 ? 139.454 154.813 134.492 1.00 88.97  ? 200  ASN A OD1 1 
ATOM 1293 N ND2 . ASN A 1 336 ? 140.161 154.276 136.550 1.00 85.70  ? 200  ASN A ND2 1 
ATOM 1294 N N   . ILE A 1 337 ? 136.604 150.308 135.794 1.00 69.02  ? 201  ILE A N   1 
ATOM 1295 C CA  . ILE A 1 337 ? 135.815 149.446 136.666 1.00 66.06  ? 201  ILE A CA  1 
ATOM 1296 C C   . ILE A 1 337 ? 135.957 147.993 136.239 1.00 66.70  ? 201  ILE A C   1 
ATOM 1297 O O   . ILE A 1 337 ? 136.481 147.163 136.989 1.00 70.54  ? 201  ILE A O   1 
ATOM 1298 C CB  . ILE A 1 337 ? 134.336 149.869 136.666 1.00 69.75  ? 201  ILE A CB  1 
ATOM 1299 C CG1 . ILE A 1 337 ? 134.186 151.286 137.223 1.00 75.23  ? 201  ILE A CG1 1 
ATOM 1300 C CG2 . ILE A 1 337 ? 133.502 148.885 137.464 1.00 75.74  ? 201  ILE A CG2 1 
ATOM 1301 C CD1 . ILE A 1 337 ? 132.803 151.867 137.043 1.00 75.80  ? 201  ILE A CD1 1 
ATOM 1302 N N   . LEU A 1 338 ? 135.493 147.676 135.029 1.00 65.74  ? 202  LEU A N   1 
ATOM 1303 C CA  . LEU A 1 338 ? 135.556 146.299 134.553 1.00 61.03  ? 202  LEU A CA  1 
ATOM 1304 C C   . LEU A 1 338 ? 136.991 145.844 134.333 1.00 59.54  ? 202  LEU A C   1 
ATOM 1305 O O   . LEU A 1 338 ? 137.302 144.665 134.526 1.00 58.90  ? 202  LEU A O   1 
ATOM 1306 C CB  . LEU A 1 338 ? 134.756 146.152 133.260 1.00 60.26  ? 202  LEU A CB  1 
ATOM 1307 C CG  . LEU A 1 338 ? 134.713 144.752 132.650 1.00 59.08  ? 202  LEU A CG  1 
ATOM 1308 C CD1 . LEU A 1 338 ? 133.797 143.847 133.451 1.00 64.95  ? 202  LEU A CD1 1 
ATOM 1309 C CD2 . LEU A 1 338 ? 134.281 144.810 131.197 1.00 60.81  ? 202  LEU A CD2 1 
ATOM 1310 N N   . GLY A 1 339 ? 137.871 146.752 133.927 1.00 62.60  ? 203  GLY A N   1 
ATOM 1311 C CA  . GLY A 1 339 ? 139.244 146.391 133.649 1.00 57.00  ? 203  GLY A CA  1 
ATOM 1312 C C   . GLY A 1 339 ? 140.185 146.578 134.818 1.00 58.11  ? 203  GLY A C   1 
ATOM 1313 O O   . GLY A 1 339 ? 141.307 146.070 134.793 1.00 63.36  ? 203  GLY A O   1 
ATOM 1314 N N   . PHE A 1 340 ? 139.767 147.303 135.834 1.00 60.45  ? 204  PHE A N   1 
ATOM 1315 C CA  . PHE A 1 340 ? 140.687 147.479 136.951 1.00 63.94  ? 204  PHE A CA  1 
ATOM 1316 C C   . PHE A 1 340 ? 140.071 147.184 138.309 1.00 66.74  ? 204  PHE A C   1 
ATOM 1317 O O   . PHE A 1 340 ? 140.765 146.667 139.182 1.00 69.07  ? 204  PHE A O   1 
ATOM 1318 C CB  . PHE A 1 340 ? 141.259 148.898 136.956 1.00 68.92  ? 204  PHE A CB  1 
ATOM 1319 C CG  . PHE A 1 340 ? 142.281 149.127 138.028 1.00 70.56  ? 204  PHE A CG  1 
ATOM 1320 C CD1 . PHE A 1 340 ? 143.593 148.737 137.843 1.00 69.42  ? 204  PHE A CD1 1 
ATOM 1321 C CD2 . PHE A 1 340 ? 141.927 149.727 139.223 1.00 71.62  ? 204  PHE A CD2 1 
ATOM 1322 C CE1 . PHE A 1 340 ? 144.534 148.943 138.826 1.00 72.14  ? 204  PHE A CE1 1 
ATOM 1323 C CE2 . PHE A 1 340 ? 142.864 149.934 140.210 1.00 72.99  ? 204  PHE A CE2 1 
ATOM 1324 C CZ  . PHE A 1 340 ? 144.168 149.542 140.012 1.00 72.88  ? 204  PHE A CZ  1 
ATOM 1325 N N   . LEU A 1 341 ? 138.797 147.512 138.520 1.00 67.79  ? 205  LEU A N   1 
ATOM 1326 C CA  . LEU A 1 341 ? 138.227 147.359 139.855 1.00 67.94  ? 205  LEU A CA  1 
ATOM 1327 C C   . LEU A 1 341 ? 137.865 145.910 140.150 1.00 67.47  ? 205  LEU A C   1 
ATOM 1328 O O   . LEU A 1 341 ? 138.300 145.352 141.162 1.00 69.55  ? 205  LEU A O   1 
ATOM 1329 C CB  . LEU A 1 341 ? 137.007 148.264 140.021 1.00 71.72  ? 205  LEU A CB  1 
ATOM 1330 C CG  . LEU A 1 341 ? 137.317 149.714 140.395 1.00 75.13  ? 205  LEU A CG  1 
ATOM 1331 C CD1 . LEU A 1 341 ? 136.039 150.505 140.605 1.00 77.53  ? 205  LEU A CD1 1 
ATOM 1332 C CD2 . LEU A 1 341 ? 138.188 149.763 141.637 1.00 72.16  ? 205  LEU A CD2 1 
ATOM 1333 N N   . PHE A 1 342 ? 137.056 145.290 139.292 1.00 67.77  ? 206  PHE A N   1 
ATOM 1334 C CA  . PHE A 1 342 ? 136.700 143.889 139.507 1.00 70.52  ? 206  PHE A CA  1 
ATOM 1335 C C   . PHE A 1 342 ? 137.917 142.973 139.493 1.00 67.41  ? 206  PHE A C   1 
ATOM 1336 O O   . PHE A 1 342 ? 138.018 142.107 140.381 1.00 66.66  ? 206  PHE A O   1 
ATOM 1337 C CB  . PHE A 1 342 ? 135.656 143.442 138.476 1.00 71.15  ? 206  PHE A CB  1 
ATOM 1338 C CG  . PHE A 1 342 ? 134.315 144.103 138.629 1.00 79.33  ? 206  PHE A CG  1 
ATOM 1339 C CD1 . PHE A 1 342 ? 134.039 144.921 139.712 1.00 81.41  ? 206  PHE A CD1 1 
ATOM 1340 C CD2 . PHE A 1 342 ? 133.322 143.893 137.687 1.00 78.59  ? 206  PHE A CD2 1 
ATOM 1341 C CE1 . PHE A 1 342 ? 132.802 145.524 139.845 1.00 87.37  ? 206  PHE A CE1 1 
ATOM 1342 C CE2 . PHE A 1 342 ? 132.084 144.492 137.815 1.00 81.24  ? 206  PHE A CE2 1 
ATOM 1343 C CZ  . PHE A 1 342 ? 131.823 145.308 138.896 1.00 87.99  ? 206  PHE A CZ  1 
ATOM 1344 N N   . PRO A 1 343 ? 138.847 143.071 138.533 1.00 62.86  ? 207  PRO A N   1 
ATOM 1345 C CA  . PRO A 1 343 ? 140.056 142.241 138.624 1.00 60.04  ? 207  PRO A CA  1 
ATOM 1346 C C   . PRO A 1 343 ? 140.858 142.465 139.890 1.00 62.44  ? 207  PRO A C   1 
ATOM 1347 O O   . PRO A 1 343 ? 141.304 141.492 140.507 1.00 65.90  ? 207  PRO A O   1 
ATOM 1348 C CB  . PRO A 1 343 ? 140.843 142.651 137.375 1.00 56.99  ? 207  PRO A CB  1 
ATOM 1349 C CG  . PRO A 1 343 ? 139.806 143.027 136.414 1.00 61.37  ? 207  PRO A CG  1 
ATOM 1350 C CD  . PRO A 1 343 ? 138.775 143.748 137.226 1.00 64.99  ? 207  PRO A CD  1 
ATOM 1351 N N   . PHE A 1 344 ? 141.050 143.718 140.302 1.00 62.11  ? 208  PHE A N   1 
ATOM 1352 C CA  . PHE A 1 344 ? 141.817 143.980 141.514 1.00 60.88  ? 208  PHE A CA  1 
ATOM 1353 C C   . PHE A 1 344 ? 141.139 143.370 142.729 1.00 63.06  ? 208  PHE A C   1 
ATOM 1354 O O   . PHE A 1 344 ? 141.798 142.749 143.569 1.00 65.47  ? 208  PHE A O   1 
ATOM 1355 C CB  . PHE A 1 344 ? 142.000 145.484 141.699 1.00 66.07  ? 208  PHE A CB  1 
ATOM 1356 C CG  . PHE A 1 344 ? 142.930 145.858 142.814 1.00 72.32  ? 208  PHE A CG  1 
ATOM 1357 C CD1 . PHE A 1 344 ? 144.292 145.961 142.589 1.00 74.49  ? 208  PHE A CD1 1 
ATOM 1358 C CD2 . PHE A 1 344 ? 142.442 146.135 144.078 1.00 74.40  ? 208  PHE A CD2 1 
ATOM 1359 C CE1 . PHE A 1 344 ? 145.152 146.318 143.608 1.00 78.77  ? 208  PHE A CE1 1 
ATOM 1360 C CE2 . PHE A 1 344 ? 143.296 146.491 145.102 1.00 77.68  ? 208  PHE A CE2 1 
ATOM 1361 C CZ  . PHE A 1 344 ? 144.653 146.583 144.867 1.00 79.78  ? 208  PHE A CZ  1 
ATOM 1362 N N   . LEU A 1 345 ? 139.817 143.516 142.829 1.00 64.93  ? 209  LEU A N   1 
ATOM 1363 C CA  . LEU A 1 345 ? 139.097 142.957 143.968 1.00 66.95  ? 209  LEU A CA  1 
ATOM 1364 C C   . LEU A 1 345 ? 139.156 141.435 143.977 1.00 64.83  ? 209  LEU A C   1 
ATOM 1365 O O   . LEU A 1 345 ? 139.387 140.830 145.028 1.00 63.81  ? 209  LEU A O   1 
ATOM 1366 C CB  . LEU A 1 345 ? 137.647 143.438 143.966 1.00 64.69  ? 209  LEU A CB  1 
ATOM 1367 C CG  . LEU A 1 345 ? 137.440 144.913 144.306 1.00 66.78  ? 209  LEU A CG  1 
ATOM 1368 C CD1 . LEU A 1 345 ? 135.961 145.237 144.383 1.00 67.53  ? 209  LEU A CD1 1 
ATOM 1369 C CD2 . LEU A 1 345 ? 138.133 145.256 145.609 1.00 69.54  ? 209  LEU A CD2 1 
ATOM 1370 N N   . ILE A 1 346 ? 138.952 140.796 142.824 1.00 59.96  ? 210  ILE A N   1 
ATOM 1371 C CA  . ILE A 1 346 ? 138.959 139.337 142.789 1.00 57.34  ? 210  ILE A CA  1 
ATOM 1372 C C   . ILE A 1 346 ? 140.351 138.798 143.094 1.00 57.75  ? 210  ILE A C   1 
ATOM 1373 O O   . ILE A 1 346 ? 140.502 137.806 143.816 1.00 60.00  ? 210  ILE A O   1 
ATOM 1374 C CB  . ILE A 1 346 ? 138.433 138.826 141.437 1.00 55.17  ? 210  ILE A CB  1 
ATOM 1375 C CG1 . ILE A 1 346 ? 136.942 139.128 141.305 1.00 57.36  ? 210  ILE A CG1 1 
ATOM 1376 C CG2 . ILE A 1 346 ? 138.677 137.338 141.298 1.00 54.30  ? 210  ILE A CG2 1 
ATOM 1377 C CD1 . ILE A 1 346 ? 136.305 138.527 140.079 1.00 61.00  ? 210  ILE A CD1 1 
ATOM 1378 N N   . ILE A 1 347 ? 141.389 139.440 142.560 1.00 55.76  ? 211  ILE A N   1 
ATOM 1379 C CA  . ILE A 1 347 ? 142.748 138.990 142.829 1.00 52.94  ? 211  ILE A CA  1 
ATOM 1380 C C   . ILE A 1 347 ? 143.102 139.200 144.295 1.00 58.34  ? 211  ILE A C   1 
ATOM 1381 O O   . ILE A 1 347 ? 143.752 138.350 144.913 1.00 62.91  ? 211  ILE A O   1 
ATOM 1382 C CB  . ILE A 1 347 ? 143.735 139.702 141.890 1.00 53.13  ? 211  ILE A CB  1 
ATOM 1383 C CG1 . ILE A 1 347 ? 143.508 139.239 140.454 1.00 52.04  ? 211  ILE A CG1 1 
ATOM 1384 C CG2 . ILE A 1 347 ? 145.161 139.437 142.315 1.00 54.18  ? 211  ILE A CG2 1 
ATOM 1385 C CD1 . ILE A 1 347 ? 144.397 139.911 139.457 1.00 52.03  ? 211  ILE A CD1 1 
ATOM 1386 N N   . LEU A 1 348 ? 142.680 140.324 144.880 1.00 58.26  ? 212  LEU A N   1 
ATOM 1387 C CA  . LEU A 1 348 ? 142.928 140.549 146.300 1.00 60.72  ? 212  LEU A CA  1 
ATOM 1388 C C   . LEU A 1 348 ? 142.205 139.520 147.157 1.00 62.07  ? 212  LEU A C   1 
ATOM 1389 O O   . LEU A 1 348 ? 142.765 139.018 148.135 1.00 64.18  ? 212  LEU A O   1 
ATOM 1390 C CB  . LEU A 1 348 ? 142.506 141.964 146.689 1.00 62.69  ? 212  LEU A CB  1 
ATOM 1391 C CG  . LEU A 1 348 ? 143.654 142.930 146.972 1.00 65.08  ? 212  LEU A CG  1 
ATOM 1392 C CD1 . LEU A 1 348 ? 144.399 142.508 148.225 1.00 58.21  ? 212  LEU A CD1 1 
ATOM 1393 C CD2 . LEU A 1 348 ? 144.597 142.992 145.784 1.00 68.56  ? 212  LEU A CD2 1 
ATOM 1394 N N   . THR A 1 349 ? 140.963 139.189 146.802 1.00 58.25  ? 213  THR A N   1 
ATOM 1395 C CA  . THR A 1 349 ? 140.227 138.160 147.528 1.00 59.06  ? 213  THR A CA  1 
ATOM 1396 C C   . THR A 1 349 ? 140.941 136.817 147.453 1.00 60.13  ? 213  THR A C   1 
ATOM 1397 O O   . THR A 1 349 ? 141.164 136.155 148.476 1.00 62.69  ? 213  THR A O   1 
ATOM 1398 C CB  . THR A 1 349 ? 138.811 138.044 146.964 1.00 60.96  ? 213  THR A CB  1 
ATOM 1399 O OG1 . THR A 1 349 ? 138.058 139.211 147.311 1.00 61.84  ? 213  THR A OG1 1 
ATOM 1400 C CG2 . THR A 1 349 ? 138.113 136.811 147.504 1.00 63.62  ? 213  THR A CG2 1 
ATOM 1401 N N   . SER A 1 350 ? 141.322 136.403 146.242 1.00 57.61  ? 214  SER A N   1 
ATOM 1402 C CA  . SER A 1 350 ? 141.977 135.112 146.077 1.00 54.97  ? 214  SER A CA  1 
ATOM 1403 C C   . SER A 1 350 ? 143.302 135.065 146.821 1.00 59.53  ? 214  SER A C   1 
ATOM 1404 O O   . SER A 1 350 ? 143.608 134.076 147.494 1.00 65.84  ? 214  SER A O   1 
ATOM 1405 C CB  . SER A 1 350 ? 142.184 134.812 144.595 1.00 52.17  ? 214  SER A CB  1 
ATOM 1406 O OG  . SER A 1 350 ? 140.942 134.684 143.930 1.00 57.06  ? 214  SER A OG  1 
ATOM 1407 N N   . TYR A 1 351 ? 144.094 136.133 146.739 1.00 55.68  ? 215  TYR A N   1 
ATOM 1408 C CA  . TYR A 1 351 ? 145.399 136.114 147.382 1.00 54.93  ? 215  TYR A CA  1 
ATOM 1409 C C   . TYR A 1 351 ? 145.308 136.263 148.894 1.00 59.35  ? 215  TYR A C   1 
ATOM 1410 O O   . TYR A 1 351 ? 146.150 135.714 149.609 1.00 64.05  ? 215  TYR A O   1 
ATOM 1411 C CB  . TYR A 1 351 ? 146.297 137.191 146.780 1.00 56.87  ? 215  TYR A CB  1 
ATOM 1412 C CG  . TYR A 1 351 ? 147.074 136.685 145.590 1.00 57.49  ? 215  TYR A CG  1 
ATOM 1413 C CD1 . TYR A 1 351 ? 146.489 136.611 144.336 1.00 55.32  ? 215  TYR A CD1 1 
ATOM 1414 C CD2 . TYR A 1 351 ? 148.384 136.260 145.725 1.00 60.84  ? 215  TYR A CD2 1 
ATOM 1415 C CE1 . TYR A 1 351 ? 147.191 136.140 143.252 1.00 54.53  ? 215  TYR A CE1 1 
ATOM 1416 C CE2 . TYR A 1 351 ? 149.093 135.788 144.645 1.00 61.73  ? 215  TYR A CE2 1 
ATOM 1417 C CZ  . TYR A 1 351 ? 148.492 135.731 143.412 1.00 58.60  ? 215  TYR A CZ  1 
ATOM 1418 O OH  . TYR A 1 351 ? 149.200 135.259 142.335 1.00 66.94  ? 215  TYR A OH  1 
ATOM 1419 N N   . THR A 1 352 ? 144.294 136.956 149.415 1.00 59.54  ? 216  THR A N   1 
ATOM 1420 C CA  . THR A 1 352 ? 144.144 136.997 150.864 1.00 60.94  ? 216  THR A CA  1 
ATOM 1421 C C   . THR A 1 352 ? 143.634 135.666 151.405 1.00 63.44  ? 216  THR A C   1 
ATOM 1422 O O   . THR A 1 352 ? 144.035 135.254 152.498 1.00 67.51  ? 216  THR A O   1 
ATOM 1423 C CB  . THR A 1 352 ? 143.236 138.159 151.281 1.00 62.43  ? 216  THR A CB  1 
ATOM 1424 O OG1 . THR A 1 352 ? 143.442 138.450 152.668 1.00 71.17  ? 216  THR A OG1 1 
ATOM 1425 C CG2 . THR A 1 352 ? 141.768 137.838 151.060 1.00 58.39  ? 216  THR A CG2 1 
ATOM 1426 N N   . LEU A 1 353 ? 142.793 134.956 150.647 1.00 61.09  ? 217  LEU A N   1 
ATOM 1427 C CA  . LEU A 1 353 ? 142.417 133.606 151.060 1.00 63.05  ? 217  LEU A CA  1 
ATOM 1428 C C   . LEU A 1 353 ? 143.613 132.663 150.997 1.00 61.04  ? 217  LEU A C   1 
ATOM 1429 O O   . LEU A 1 353 ? 143.791 131.808 151.877 1.00 65.39  ? 217  LEU A O   1 
ATOM 1430 C CB  . LEU A 1 353 ? 141.270 133.091 150.193 1.00 62.66  ? 217  LEU A CB  1 
ATOM 1431 C CG  . LEU A 1 353 ? 139.846 133.355 150.687 1.00 64.67  ? 217  LEU A CG  1 
ATOM 1432 C CD1 . LEU A 1 353 ? 139.633 134.815 151.026 1.00 64.77  ? 217  LEU A CD1 1 
ATOM 1433 C CD2 . LEU A 1 353 ? 138.835 132.906 149.649 1.00 66.00  ? 217  LEU A CD2 1 
ATOM 1434 N N   . ILE A 1 354 ? 144.447 132.810 149.966 1.00 56.56  ? 218  ILE A N   1 
ATOM 1435 C CA  . ILE A 1 354 ? 145.675 132.029 149.878 1.00 57.94  ? 218  ILE A CA  1 
ATOM 1436 C C   . ILE A 1 354 ? 146.563 132.302 151.082 1.00 60.93  ? 218  ILE A C   1 
ATOM 1437 O O   . ILE A 1 354 ? 147.118 131.375 151.681 1.00 67.49  ? 218  ILE A O   1 
ATOM 1438 C CB  . ILE A 1 354 ? 146.406 132.332 148.558 1.00 56.42  ? 218  ILE A CB  1 
ATOM 1439 C CG1 . ILE A 1 354 ? 145.696 131.660 147.386 1.00 59.05  ? 218  ILE A CG1 1 
ATOM 1440 C CG2 . ILE A 1 354 ? 147.853 131.891 148.630 1.00 54.11  ? 218  ILE A CG2 1 
ATOM 1441 C CD1 . ILE A 1 354 ? 146.321 131.970 146.054 1.00 60.09  ? 218  ILE A CD1 1 
ATOM 1442 N N   . TRP A 1 355 ? 146.712 133.573 151.457 1.00 59.14  ? 219  TRP A N   1 
ATOM 1443 C CA  . TRP A 1 355 ? 147.555 133.904 152.599 1.00 59.90  ? 219  TRP A CA  1 
ATOM 1444 C C   . TRP A 1 355 ? 146.964 133.376 153.898 1.00 65.10  ? 219  TRP A C   1 
ATOM 1445 O O   . TRP A 1 355 ? 147.703 132.971 154.797 1.00 68.88  ? 219  TRP A O   1 
ATOM 1446 C CB  . TRP A 1 355 ? 147.768 135.412 152.687 1.00 64.50  ? 219  TRP A CB  1 
ATOM 1447 C CG  . TRP A 1 355 ? 148.691 135.793 153.792 1.00 71.35  ? 219  TRP A CG  1 
ATOM 1448 C CD1 . TRP A 1 355 ? 150.051 135.856 153.738 1.00 73.58  ? 219  TRP A CD1 1 
ATOM 1449 C CD2 . TRP A 1 355 ? 148.326 136.155 155.127 1.00 75.05  ? 219  TRP A CD2 1 
ATOM 1450 N NE1 . TRP A 1 355 ? 150.557 136.239 154.955 1.00 74.85  ? 219  TRP A NE1 1 
ATOM 1451 C CE2 . TRP A 1 355 ? 149.517 136.429 155.825 1.00 76.45  ? 219  TRP A CE2 1 
ATOM 1452 C CE3 . TRP A 1 355 ? 147.107 136.276 155.799 1.00 73.75  ? 219  TRP A CE3 1 
ATOM 1453 C CZ2 . TRP A 1 355 ? 149.525 136.816 157.161 1.00 80.11  ? 219  TRP A CZ2 1 
ATOM 1454 C CZ3 . TRP A 1 355 ? 147.117 136.660 157.125 1.00 77.54  ? 219  TRP A CZ3 1 
ATOM 1455 C CH2 . TRP A 1 355 ? 148.318 136.926 157.792 1.00 80.98  ? 219  TRP A CH2 1 
ATOM 1456 N N   . LYS A 1 356 ? 145.637 133.375 154.022 1.00 64.31  ? 220  LYS A N   1 
ATOM 1457 C CA  . LYS A 1 356 ? 145.006 132.778 155.196 1.00 64.54  ? 220  LYS A CA  1 
ATOM 1458 C C   . LYS A 1 356 ? 145.336 131.293 155.300 1.00 63.48  ? 220  LYS A C   1 
ATOM 1459 O O   . LYS A 1 356 ? 145.718 130.797 156.370 1.00 66.65  ? 220  LYS A O   1 
ATOM 1460 C CB  . LYS A 1 356 ? 143.495 132.993 155.128 1.00 63.17  ? 220  LYS A CB  1 
ATOM 1461 C CG  . LYS A 1 356 ? 142.692 132.089 156.037 1.00 67.33  ? 220  LYS A CG  1 
ATOM 1462 C CD  . LYS A 1 356 ? 141.221 132.119 155.663 1.00 71.39  ? 220  LYS A CD  1 
ATOM 1463 C CE  . LYS A 1 356 ? 140.688 133.539 155.629 1.00 70.61  ? 220  LYS A CE  1 
ATOM 1464 N NZ  . LYS A 1 356 ? 139.259 133.578 155.218 1.00 71.30  ? 220  LYS A NZ  1 
ATOM 1465 N N   . ALA A 1 357 ? 145.200 130.567 154.187 1.00 61.97  ? 221  ALA A N   1 
ATOM 1466 C CA  . ALA A 1 357 ? 145.518 129.141 154.193 1.00 60.66  ? 221  ALA A CA  1 
ATOM 1467 C C   . ALA A 1 357 ? 146.990 128.906 154.506 1.00 60.37  ? 221  ALA A C   1 
ATOM 1468 O O   . ALA A 1 357 ? 147.337 127.986 155.259 1.00 67.57  ? 221  ALA A O   1 
ATOM 1469 C CB  . ALA A 1 357 ? 145.151 128.513 152.852 1.00 60.26  ? 221  ALA A CB  1 
ATOM 1470 N N   . LEU A 1 358 ? 147.870 129.729 153.937 1.00 59.63  ? 222  LEU A N   1 
ATOM 1471 C CA  . LEU A 1 358 ? 149.294 129.604 154.224 1.00 60.64  ? 222  LEU A CA  1 
ATOM 1472 C C   . LEU A 1 358 ? 149.585 129.879 155.688 1.00 64.01  ? 222  LEU A C   1 
ATOM 1473 O O   . LEU A 1 358 ? 150.446 129.230 156.285 1.00 66.16  ? 222  LEU A O   1 
ATOM 1474 C CB  . LEU A 1 358 ? 150.098 130.554 153.344 1.00 61.84  ? 222  LEU A CB  1 
ATOM 1475 C CG  . LEU A 1 358 ? 150.016 130.312 151.844 1.00 64.52  ? 222  LEU A CG  1 
ATOM 1476 C CD1 . LEU A 1 358 ? 150.718 131.440 151.117 1.00 66.12  ? 222  LEU A CD1 1 
ATOM 1477 C CD2 . LEU A 1 358 ? 150.605 128.962 151.488 1.00 62.83  ? 222  LEU A CD2 1 
ATOM 1478 N N   . LYS A 1 359 ? 148.894 130.853 156.280 1.00 64.87  ? 223  LYS A N   1 
ATOM 1479 C CA  . LYS A 1 359 ? 149.110 131.153 157.689 1.00 65.37  ? 223  LYS A CA  1 
ATOM 1480 C C   . LYS A 1 359 ? 148.690 129.988 158.570 1.00 63.93  ? 223  LYS A C   1 
ATOM 1481 O O   . LYS A 1 359 ? 149.398 129.639 159.518 1.00 67.80  ? 223  LYS A O   1 
ATOM 1482 C CB  . LYS A 1 359 ? 148.355 132.421 158.082 1.00 68.85  ? 223  LYS A CB  1 
ATOM 1483 C CG  . LYS A 1 359 ? 148.703 132.928 159.467 1.00 75.13  ? 223  LYS A CG  1 
ATOM 1484 C CD  . LYS A 1 359 ? 150.198 133.168 159.595 1.00 79.27  ? 223  LYS A CD  1 
ATOM 1485 C CE  . LYS A 1 359 ? 150.568 133.614 160.999 1.00 85.66  ? 223  LYS A CE  1 
ATOM 1486 N NZ  . LYS A 1 359 ? 149.853 134.858 161.393 1.00 94.52  ? 223  LYS A NZ  1 
ATOM 1487 N N   . LYS A 1 360 ? 147.545 129.369 158.275 1.00 61.12  ? 224  LYS A N   1 
ATOM 1488 C CA  . LYS A 1 360 ? 147.131 128.212 159.067 1.00 59.86  ? 224  LYS A CA  1 
ATOM 1489 C C   . LYS A 1 360 ? 148.113 127.055 158.914 1.00 59.34  ? 224  LYS A C   1 
ATOM 1490 O O   . LYS A 1 360 ? 148.506 126.419 159.906 1.00 64.17  ? 224  LYS A O   1 
ATOM 1491 C CB  . LYS A 1 360 ? 145.722 127.778 158.676 1.00 63.31  ? 224  LYS A CB  1 
ATOM 1492 C CG  . LYS A 1 360 ? 144.715 128.905 158.688 1.00 66.62  ? 224  LYS A CG  1 
ATOM 1493 C CD  . LYS A 1 360 ? 143.420 128.494 159.353 1.00 73.36  ? 224  LYS A CD  1 
ATOM 1494 C CE  . LYS A 1 360 ? 143.599 128.345 160.850 1.00 74.56  ? 224  LYS A CE  1 
ATOM 1495 N NZ  . LYS A 1 360 ? 142.298 128.118 161.529 1.00 74.39  ? 224  LYS A NZ  1 
ATOM 1496 N N   . ALA A 1 361 ? 148.534 126.774 157.678 1.00 56.18  ? 225  ALA A N   1 
ATOM 1497 C CA  . ALA A 1 361 ? 149.483 125.690 157.454 1.00 55.32  ? 225  ALA A CA  1 
ATOM 1498 C C   . ALA A 1 361 ? 150.810 125.966 158.147 1.00 60.78  ? 225  ALA A C   1 
ATOM 1499 O O   . ALA A 1 361 ? 151.412 125.062 158.737 1.00 64.48  ? 225  ALA A O   1 
ATOM 1500 C CB  . ALA A 1 361 ? 149.692 125.478 155.957 1.00 57.77  ? 225  ALA A CB  1 
ATOM 1501 N N   . TYR A 1 362 ? 151.280 127.213 158.096 1.00 62.96  ? 226  TYR A N   1 
ATOM 1502 C CA  . TYR A 1 362 ? 152.533 127.564 158.745 1.00 64.63  ? 226  TYR A CA  1 
ATOM 1503 C C   . TYR A 1 362 ? 152.418 127.510 160.259 1.00 64.05  ? 226  TYR A C   1 
ATOM 1504 O O   . TYR A 1 362 ? 153.380 127.139 160.930 1.00 66.24  ? 226  TYR A O   1 
ATOM 1505 C CB  . TYR A 1 362 ? 152.987 128.951 158.302 1.00 68.66  ? 226  TYR A CB  1 
ATOM 1506 C CG  . TYR A 1 362 ? 154.130 129.501 159.119 1.00 74.46  ? 226  TYR A CG  1 
ATOM 1507 C CD1 . TYR A 1 362 ? 155.413 128.989 158.985 1.00 75.31  ? 226  TYR A CD1 1 
ATOM 1508 C CD2 . TYR A 1 362 ? 153.929 130.535 160.023 1.00 75.72  ? 226  TYR A CD2 1 
ATOM 1509 C CE1 . TYR A 1 362 ? 156.462 129.490 159.729 1.00 80.86  ? 226  TYR A CE1 1 
ATOM 1510 C CE2 . TYR A 1 362 ? 154.971 131.042 160.771 1.00 80.57  ? 226  TYR A CE2 1 
ATOM 1511 C CZ  . TYR A 1 362 ? 156.235 130.516 160.620 1.00 85.70  ? 226  TYR A CZ  1 
ATOM 1512 O OH  . TYR A 1 362 ? 157.277 131.020 161.365 1.00 88.45  ? 226  TYR A OH  1 
ATOM 1513 N N   . ASP A 1 363 ? 151.265 127.880 160.816 1.00 61.97  ? 227  ASP A N   1 
ATOM 1514 C CA  . ASP A 1 363 ? 151.065 127.745 162.254 1.00 59.66  ? 227  ASP A CA  1 
ATOM 1515 C C   . ASP A 1 363 ? 151.180 126.287 162.675 1.00 59.37  ? 227  ASP A C   1 
ATOM 1516 O O   . ASP A 1 363 ? 151.911 125.950 163.617 1.00 60.57  ? 227  ASP A O   1 
ATOM 1517 C CB  . ASP A 1 363 ? 149.705 128.317 162.652 1.00 57.64  ? 227  ASP A CB  1 
ATOM 1518 C CG  . ASP A 1 363 ? 149.683 129.832 162.643 1.00 69.90  ? 227  ASP A CG  1 
ATOM 1519 O OD1 . ASP A 1 363 ? 150.768 130.444 162.560 1.00 78.08  ? 227  ASP A OD1 1 
ATOM 1520 O OD2 . ASP A 1 363 ? 148.579 130.410 162.716 1.00 68.87  ? 227  ASP A OD2 1 
ATOM 1521 N N   . LEU A 1 364 ? 150.478 125.401 161.964 1.00 58.45  ? 228  LEU A N   1 
ATOM 1522 C CA  . LEU A 1 364 ? 150.558 123.978 162.284 1.00 53.75  ? 228  LEU A CA  1 
ATOM 1523 C C   . LEU A 1 364 ? 151.991 123.472 162.159 1.00 54.77  ? 228  LEU A C   1 
ATOM 1524 O O   . LEU A 1 364 ? 152.496 122.767 163.042 1.00 54.94  ? 228  LEU A O   1 
ATOM 1525 C CB  . LEU A 1 364 ? 149.625 123.183 161.371 1.00 54.28  ? 228  LEU A CB  1 
ATOM 1526 C CG  . LEU A 1 364 ? 148.897 121.965 161.944 1.00 51.03  ? 228  LEU A CG  1 
ATOM 1527 C CD1 . LEU A 1 364 ? 147.984 121.355 160.898 1.00 51.41  ? 228  LEU A CD1 1 
ATOM 1528 C CD2 . LEU A 1 364 ? 149.862 120.926 162.469 1.00 51.25  ? 228  LEU A CD2 1 
ATOM 1529 N N   . GLU A 1 365 ? 152.670 123.842 161.071 1.00 58.70  ? 229  GLU A N   1 
ATOM 1530 C CA  . GLU A 1 365 ? 154.020 123.345 160.834 1.00 58.21  ? 229  GLU A CA  1 
ATOM 1531 C C   . GLU A 1 365 ? 154.997 123.855 161.884 1.00 61.79  ? 229  GLU A C   1 
ATOM 1532 O O   . GLU A 1 365 ? 155.825 123.095 162.389 1.00 64.61  ? 229  GLU A O   1 
ATOM 1533 C CB  . GLU A 1 365 ? 154.486 123.736 159.434 1.00 59.02  ? 229  GLU A CB  1 
ATOM 1534 C CG  . GLU A 1 365 ? 153.920 122.852 158.355 1.00 65.36  ? 229  GLU A CG  1 
ATOM 1535 C CD  . GLU A 1 365 ? 154.193 121.389 158.619 1.00 73.18  ? 229  GLU A CD  1 
ATOM 1536 O OE1 . GLU A 1 365 ? 155.346 121.047 158.954 1.00 72.94  ? 229  GLU A OE1 1 
ATOM 1537 O OE2 . GLU A 1 365 ? 153.250 120.580 158.504 1.00 75.64  ? 229  GLU A OE2 1 
ATOM 1538 N N   . ASP A 1 366 ? 154.927 125.144 162.216 1.00 59.91  ? 230  ASP A N   1 
ATOM 1539 C CA  . ASP A 1 366 ? 155.845 125.706 163.199 1.00 60.12  ? 230  ASP A CA  1 
ATOM 1540 C C   . ASP A 1 366 ? 155.622 125.090 164.571 1.00 60.51  ? 230  ASP A C   1 
ATOM 1541 O O   . ASP A 1 366 ? 156.586 124.767 165.281 1.00 58.36  ? 230  ASP A O   1 
ATOM 1542 C CB  . ASP A 1 366 ? 155.677 127.222 163.261 1.00 65.58  ? 230  ASP A CB  1 
ATOM 1543 C CG  . ASP A 1 366 ? 156.685 127.882 164.178 1.00 75.68  ? 230  ASP A CG  1 
ATOM 1544 O OD1 . ASP A 1 366 ? 157.715 127.249 164.487 1.00 73.49  ? 230  ASP A OD1 1 
ATOM 1545 O OD2 . ASP A 1 366 ? 156.445 129.035 164.593 1.00 82.71  ? 230  ASP A OD2 1 
ATOM 1546 N N   . ASN A 1 367 ? 154.358 124.920 164.965 1.00 58.98  ? 231  ASN A N   1 
ATOM 1547 C CA  . ASN A 1 367 ? 154.077 124.306 166.255 1.00 48.48  ? 231  ASN A CA  1 
ATOM 1548 C C   . ASN A 1 367 ? 154.596 122.878 166.298 1.00 49.93  ? 231  ASN A C   1 
ATOM 1549 O O   . ASN A 1 367 ? 155.184 122.449 167.298 1.00 48.94  ? 231  ASN A O   1 
ATOM 1550 C CB  . ASN A 1 367 ? 152.582 124.361 166.541 1.00 40.08  ? 231  ASN A CB  1 
ATOM 1551 C CG  . ASN A 1 367 ? 152.080 125.774 166.688 1.00 43.00  ? 231  ASN A CG  1 
ATOM 1552 O OD1 . ASN A 1 367 ? 152.817 126.661 167.110 1.00 45.70  ? 231  ASN A OD1 1 
ATOM 1553 N ND2 . ASN A 1 367 ? 150.824 125.997 166.334 1.00 46.02  ? 231  ASN A ND2 1 
ATOM 1554 N N   . TRP A 1 368 ? 154.428 122.131 165.208 1.00 50.63  ? 232  TRP A N   1 
ATOM 1555 C CA  . TRP A 1 368 ? 154.936 120.768 165.242 1.00 49.57  ? 232  TRP A CA  1 
ATOM 1556 C C   . TRP A 1 368 ? 156.455 120.720 165.171 1.00 56.71  ? 232  TRP A C   1 
ATOM 1557 O O   . TRP A 1 368 ? 157.061 119.781 165.692 1.00 60.03  ? 232  TRP A O   1 
ATOM 1558 C CB  . TRP A 1 368 ? 154.342 119.922 164.130 1.00 48.66  ? 232  TRP A CB  1 
ATOM 1559 C CG  . TRP A 1 368 ? 154.396 118.513 164.537 1.00 50.13  ? 232  TRP A CG  1 
ATOM 1560 C CD1 . TRP A 1 368 ? 155.384 117.620 164.271 1.00 52.27  ? 232  TRP A CD1 1 
ATOM 1561 C CD2 . TRP A 1 368 ? 153.454 117.837 165.366 1.00 52.64  ? 232  TRP A CD2 1 
ATOM 1562 N NE1 . TRP A 1 368 ? 155.100 116.414 164.857 1.00 55.08  ? 232  TRP A NE1 1 
ATOM 1563 C CE2 . TRP A 1 368 ? 153.917 116.523 165.537 1.00 52.67  ? 232  TRP A CE2 1 
ATOM 1564 C CE3 . TRP A 1 368 ? 152.252 118.212 165.968 1.00 53.31  ? 232  TRP A CE3 1 
ATOM 1565 C CZ2 . TRP A 1 368 ? 153.223 115.584 166.283 1.00 52.63  ? 232  TRP A CZ2 1 
ATOM 1566 C CZ3 . TRP A 1 368 ? 151.565 117.279 166.705 1.00 53.16  ? 232  TRP A CZ3 1 
ATOM 1567 C CH2 . TRP A 1 368 ? 152.049 115.978 166.854 1.00 54.99  ? 232  TRP A CH2 1 
ATOM 1568 N N   . GLU A 1 369 ? 157.092 121.703 164.539 1.00 57.07  ? 233  GLU A N   1 
ATOM 1569 C CA  . GLU A 1 369 ? 158.551 121.730 164.537 1.00 60.86  ? 233  GLU A CA  1 
ATOM 1570 C C   . GLU A 1 369 ? 159.089 122.000 165.935 1.00 60.76  ? 233  GLU A C   1 
ATOM 1571 O O   . GLU A 1 369 ? 160.067 121.378 166.366 1.00 61.33  ? 233  GLU A O   1 
ATOM 1572 C CB  . GLU A 1 369 ? 159.065 122.770 163.541 1.00 63.23  ? 233  GLU A CB  1 
ATOM 1573 C CG  . GLU A 1 369 ? 158.802 122.412 162.084 1.00 68.10  ? 233  GLU A CG  1 
ATOM 1574 C CD  . GLU A 1 369 ? 159.162 120.974 161.749 1.00 80.04  ? 233  GLU A CD  1 
ATOM 1575 O OE1 . GLU A 1 369 ? 160.260 120.519 162.135 1.00 78.73  ? 233  GLU A OE1 1 
ATOM 1576 O OE2 . GLU A 1 369 ? 158.340 120.295 161.099 1.00 85.68  ? 233  GLU A OE2 1 
ATOM 1577 N N   . THR A 1 370 ? 158.456 122.922 166.665 1.00 58.28  ? 234  THR A N   1 
ATOM 1578 C CA  . THR A 1 370 ? 158.847 123.139 168.057 1.00 56.81  ? 234  THR A CA  1 
ATOM 1579 C C   . THR A 1 370 ? 158.604 121.890 168.895 1.00 54.75  ? 234  THR A C   1 
ATOM 1580 O O   . THR A 1 370 ? 159.423 121.535 169.754 1.00 57.21  ? 234  THR A O   1 
ATOM 1581 C CB  . THR A 1 370 ? 158.095 124.329 168.648 1.00 51.38  ? 234  THR A CB  1 
ATOM 1582 O OG1 . THR A 1 370 ? 156.693 124.057 168.641 1.00 54.95  ? 234  THR A OG1 1 
ATOM 1583 C CG2 . THR A 1 370 ? 158.364 125.585 167.840 1.00 57.14  ? 234  THR A CG2 1 
ATOM 1584 N N   . LEU A 1 371 ? 157.485 121.205 168.654 1.00 50.71  ? 235  LEU A N   1 
ATOM 1585 C CA  . LEU A 1 371 ? 157.202 119.970 169.376 1.00 46.91  ? 235  LEU A CA  1 
ATOM 1586 C C   . LEU A 1 371 ? 158.266 118.913 169.097 1.00 53.21  ? 235  LEU A C   1 
ATOM 1587 O O   . LEU A 1 371 ? 158.732 118.231 170.014 1.00 58.42  ? 235  LEU A O   1 
ATOM 1588 C CB  . LEU A 1 371 ? 155.812 119.467 169.000 1.00 42.84  ? 235  LEU A CB  1 
ATOM 1589 C CG  . LEU A 1 371 ? 154.998 118.709 170.040 1.00 37.18  ? 235  LEU A CG  1 
ATOM 1590 C CD1 . LEU A 1 371 ? 153.542 118.755 169.656 1.00 37.02  ? 235  LEU A CD1 1 
ATOM 1591 C CD2 . LEU A 1 371 ? 155.464 117.276 170.149 1.00 43.86  ? 235  LEU A CD2 1 
ATOM 1592 N N   . ASN A 1 372 ? 158.672 118.767 167.834 1.00 51.60  ? 236  ASN A N   1 
ATOM 1593 C CA  . ASN A 1 372 ? 159.704 117.791 167.491 1.00 55.67  ? 236  ASN A CA  1 
ATOM 1594 C C   . ASN A 1 372 ? 161.051 118.156 168.103 1.00 59.98  ? 236  ASN A C   1 
ATOM 1595 O O   . ASN A 1 372 ? 161.775 117.279 168.588 1.00 60.14  ? 236  ASN A O   1 
ATOM 1596 C CB  . ASN A 1 372 ? 159.831 117.663 165.974 1.00 58.83  ? 236  ASN A CB  1 
ATOM 1597 C CG  . ASN A 1 372 ? 158.780 116.755 165.376 1.00 61.54  ? 236  ASN A CG  1 
ATOM 1598 O OD1 . ASN A 1 372 ? 158.265 115.860 166.042 1.00 61.39  ? 236  ASN A OD1 1 
ATOM 1599 N ND2 . ASN A 1 372 ? 158.462 116.976 164.108 1.00 66.04  ? 236  ASN A ND2 1 
ATOM 1600 N N   . ASP A 1 373 ? 161.413 119.441 168.078 1.00 60.61  ? 237  ASP A N   1 
ATOM 1601 C CA  . ASP A 1 373 ? 162.673 119.862 168.681 1.00 60.71  ? 237  ASP A CA  1 
ATOM 1602 C C   . ASP A 1 373 ? 162.693 119.549 170.169 1.00 61.50  ? 237  ASP A C   1 
ATOM 1603 O O   . ASP A 1 373 ? 163.685 119.032 170.698 1.00 64.39  ? 237  ASP A O   1 
ATOM 1604 C CB  . ASP A 1 373 ? 162.895 121.356 168.451 1.00 56.69  ? 237  ASP A CB  1 
ATOM 1605 C CG  . ASP A 1 373 ? 163.043 121.704 166.989 1.00 67.39  ? 237  ASP A CG  1 
ATOM 1606 O OD1 . ASP A 1 373 ? 163.509 120.843 166.215 1.00 73.40  ? 237  ASP A OD1 1 
ATOM 1607 O OD2 . ASP A 1 373 ? 162.695 122.843 166.614 1.00 62.98  ? 237  ASP A OD2 1 
ATOM 1608 N N   . ASN A 1 374 ? 161.596 119.852 170.864 1.00 57.39  ? 238  ASN A N   1 
ATOM 1609 C CA  . ASN A 1 374 ? 161.556 119.588 172.295 1.00 53.83  ? 238  ASN A CA  1 
ATOM 1610 C C   . ASN A 1 374 ? 161.513 118.092 172.580 1.00 58.42  ? 238  ASN A C   1 
ATOM 1611 O O   . ASN A 1 374 ? 162.060 117.633 173.586 1.00 63.13  ? 238  ASN A O   1 
ATOM 1612 C CB  . ASN A 1 374 ? 160.372 120.310 172.921 1.00 45.20  ? 238  ASN A CB  1 
ATOM 1613 C CG  . ASN A 1 374 ? 160.480 121.807 172.784 1.00 48.81  ? 238  ASN A CG  1 
ATOM 1614 O OD1 . ASN A 1 374 ? 161.188 122.458 173.546 1.00 52.20  ? 238  ASN A OD1 1 
ATOM 1615 N ND2 . ASN A 1 374 ? 159.785 122.364 171.806 1.00 48.65  ? 238  ASN A ND2 1 
ATOM 1616 N N   . LEU A 1 375 ? 160.893 117.310 171.698 1.00 55.88  ? 239  LEU A N   1 
ATOM 1617 C CA  . LEU A 1 375 ? 160.938 115.859 171.841 1.00 58.30  ? 239  LEU A CA  1 
ATOM 1618 C C   . LEU A 1 375 ? 162.369 115.351 171.730 1.00 66.44  ? 239  LEU A C   1 
ATOM 1619 O O   . LEU A 1 375 ? 162.805 114.486 172.503 1.00 68.99  ? 239  LEU A O   1 
ATOM 1620 C CB  . LEU A 1 375 ? 160.049 115.215 170.778 1.00 57.39  ? 239  LEU A CB  1 
ATOM 1621 C CG  . LEU A 1 375 ? 159.561 113.789 170.993 1.00 57.51  ? 239  LEU A CG  1 
ATOM 1622 C CD1 . LEU A 1 375 ? 158.703 113.737 172.223 1.00 56.59  ? 239  LEU A CD1 1 
ATOM 1623 C CD2 . LEU A 1 375 ? 158.771 113.334 169.787 1.00 62.33  ? 239  LEU A CD2 1 
ATOM 1624 N N   . LYS A 1 376 ? 163.120 115.889 170.769 1.00 67.56  ? 240  LYS A N   1 
ATOM 1625 C CA  . LYS A 1 376 ? 164.511 115.487 170.597 1.00 70.46  ? 240  LYS A CA  1 
ATOM 1626 C C   . LYS A 1 376 ? 165.344 115.856 171.817 1.00 71.29  ? 240  LYS A C   1 
ATOM 1627 O O   . LYS A 1 376 ? 166.158 115.055 172.289 1.00 73.56  ? 240  LYS A O   1 
ATOM 1628 C CB  . LYS A 1 376 ? 165.082 116.120 169.330 1.00 70.24  ? 240  LYS A CB  1 
ATOM 1629 C CG  . LYS A 1 376 ? 164.560 115.486 168.051 1.00 70.34  ? 240  LYS A CG  1 
ATOM 1630 C CD  . LYS A 1 376 ? 164.530 116.476 166.901 1.00 73.62  ? 240  LYS A CD  1 
ATOM 1631 C CE  . LYS A 1 376 ? 165.910 117.028 166.593 1.00 78.12  ? 240  LYS A CE  1 
ATOM 1632 N NZ  . LYS A 1 376 ? 165.855 118.013 165.480 1.00 75.58  ? 240  LYS A NZ  1 
ATOM 1633 N N   . VAL A 1 377 ? 165.150 117.064 172.353 1.00 68.99  ? 241  VAL A N   1 
ATOM 1634 C CA  . VAL A 1 377 ? 165.930 117.455 173.527 1.00 70.03  ? 241  VAL A CA  1 
ATOM 1635 C C   . VAL A 1 377 ? 165.472 116.690 174.761 1.00 70.49  ? 241  VAL A C   1 
ATOM 1636 O O   . VAL A 1 377 ? 166.214 116.584 175.744 1.00 73.72  ? 241  VAL A O   1 
ATOM 1637 C CB  . VAL A 1 377 ? 165.878 118.979 173.756 1.00 68.01  ? 241  VAL A CB  1 
ATOM 1638 C CG1 . VAL A 1 377 ? 166.174 119.727 172.465 1.00 68.15  ? 241  VAL A CG1 1 
ATOM 1639 C CG2 . VAL A 1 377 ? 164.552 119.395 174.349 1.00 62.54  ? 241  VAL A CG2 1 
ATOM 1640 N N   . ILE A 1 378 ? 164.247 116.160 174.745 1.00 68.89  ? 242  ILE A N   1 
ATOM 1641 C CA  . ILE A 1 378 ? 163.833 115.220 175.781 1.00 69.73  ? 242  ILE A CA  1 
ATOM 1642 C C   . ILE A 1 378 ? 164.621 113.926 175.665 1.00 76.93  ? 242  ILE A C   1 
ATOM 1643 O O   . ILE A 1 378 ? 165.092 113.378 176.668 1.00 80.46  ? 242  ILE A O   1 
ATOM 1644 C CB  . ILE A 1 378 ? 162.319 114.956 175.702 1.00 62.67  ? 242  ILE A CB  1 
ATOM 1645 C CG1 . ILE A 1 378 ? 161.542 116.065 176.389 1.00 54.62  ? 242  ILE A CG1 1 
ATOM 1646 C CG2 . ILE A 1 378 ? 161.967 113.626 176.334 1.00 59.57  ? 242  ILE A CG2 1 
ATOM 1647 C CD1 . ILE A 1 378 ? 160.073 115.851 176.345 1.00 49.44  ? 242  ILE A CD1 1 
ATOM 1648 N N   . GLU A 1 379 ? 164.779 113.418 174.440 1.00 78.07  ? 243  GLU A N   1 
ATOM 1649 C CA  . GLU A 1 379 ? 165.462 112.140 174.259 1.00 80.79  ? 243  GLU A CA  1 
ATOM 1650 C C   . GLU A 1 379 ? 166.896 112.199 174.770 1.00 83.21  ? 243  GLU A C   1 
ATOM 1651 O O   . GLU A 1 379 ? 167.363 111.271 175.440 1.00 84.02  ? 243  GLU A O   1 
ATOM 1652 C CB  . GLU A 1 379 ? 165.433 111.732 172.788 1.00 82.11  ? 243  GLU A CB  1 
ATOM 1653 C CG  . GLU A 1 379 ? 166.111 110.404 172.506 1.00 90.34  ? 243  GLU A CG  1 
ATOM 1654 C CD  . GLU A 1 379 ? 166.039 110.015 171.044 1.00 95.71  ? 243  GLU A CD  1 
ATOM 1655 O OE1 . GLU A 1 379 ? 165.225 110.612 170.310 1.00 91.57  ? 243  GLU A OE1 1 
ATOM 1656 O OE2 . GLU A 1 379 ? 166.800 109.116 170.629 1.00 98.12  ? 243  GLU A OE2 1 
ATOM 1657 N N   . LYS A 1 380 ? 167.608 113.282 174.470 1.00 83.61  ? 244  LYS A N   1 
ATOM 1658 C CA  . LYS A 1 380 ? 168.982 113.462 174.937 1.00 86.31  ? 244  LYS A CA  1 
ATOM 1659 C C   . LYS A 1 380 ? 168.996 114.358 176.176 1.00 88.70  ? 244  LYS A C   1 
ATOM 1660 O O   . LYS A 1 380 ? 169.486 115.488 176.170 1.00 89.22  ? 244  LYS A O   1 
ATOM 1661 C CB  . LYS A 1 380 ? 169.848 114.026 173.813 1.00 85.46  ? 244  LYS A CB  1 
ATOM 1662 C CG  . LYS A 1 380 ? 169.250 115.235 173.112 1.00 84.57  ? 244  LYS A CG  1 
ATOM 1663 C CD  . LYS A 1 380 ? 170.057 115.622 171.888 1.00 84.04  ? 244  LYS A CD  1 
ATOM 1664 C CE  . LYS A 1 380 ? 169.978 114.545 170.823 1.00 84.78  ? 244  LYS A CE  1 
ATOM 1665 N NZ  . LYS A 1 380 ? 168.572 114.289 170.410 1.00 83.94  ? 244  LYS A NZ  1 
ATOM 1666 N N   . ALA A 1 381 ? 168.452 113.819 177.265 1.00 89.20  ? 245  ALA A N   1 
ATOM 1667 C CA  . ALA A 1 381 ? 168.323 114.557 178.511 1.00 90.83  ? 245  ALA A CA  1 
ATOM 1668 C C   . ALA A 1 381 ? 168.959 113.776 179.650 1.00 94.27  ? 245  ALA A C   1 
ATOM 1669 O O   . ALA A 1 381 ? 169.059 112.547 179.605 1.00 92.96  ? 245  ALA A O   1 
ATOM 1670 C CB  . ALA A 1 381 ? 166.858 114.856 178.845 1.00 83.99  ? 245  ALA A CB  1 
ATOM 1671 N N   . ASP A 1 382 ? 169.384 114.508 180.679 1.00 96.50  ? 246  ASP A N   1 
ATOM 1672 C CA  . ASP A 1 382 ? 170.071 113.932 181.827 1.00 101.56 ? 246  ASP A CA  1 
ATOM 1673 C C   . ASP A 1 382 ? 169.213 113.964 183.085 1.00 98.67  ? 246  ASP A C   1 
ATOM 1674 O O   . ASP A 1 382 ? 168.983 112.922 183.705 1.00 98.59  ? 246  ASP A O   1 
ATOM 1675 C CB  . ASP A 1 382 ? 171.395 114.672 182.061 1.00 102.99 ? 246  ASP A CB  1 
ATOM 1676 C CG  . ASP A 1 382 ? 172.142 114.163 183.276 1.00 106.23 ? 246  ASP A CG  1 
ATOM 1677 O OD1 . ASP A 1 382 ? 172.701 113.048 183.208 1.00 106.60 ? 246  ASP A OD1 1 
ATOM 1678 O OD2 . ASP A 1 382 ? 172.171 114.878 184.299 1.00 105.10 ? 246  ASP A OD2 1 
ATOM 1679 N N   . ASN A 1 383 ? 168.727 115.136 183.479 1.00 93.23  ? 247  ASN A N   1 
ATOM 1680 C CA  . ASN A 1 383 ? 167.916 115.290 184.676 1.00 90.20  ? 247  ASN A CA  1 
ATOM 1681 C C   . ASN A 1 383 ? 166.472 115.583 184.297 1.00 84.79  ? 247  ASN A C   1 
ATOM 1682 O O   . ASN A 1 383 ? 166.131 115.747 183.124 1.00 84.42  ? 247  ASN A O   1 
ATOM 1683 C CB  . ASN A 1 383 ? 168.473 116.402 185.573 1.00 93.60  ? 247  ASN A CB  1 
ATOM 1684 C CG  . ASN A 1 383 ? 168.669 117.705 184.830 1.00 94.02  ? 247  ASN A CG  1 
ATOM 1685 O OD1 . ASN A 1 383 ? 168.962 117.712 183.634 1.00 94.31  ? 247  ASN A OD1 1 
ATOM 1686 N ND2 . ASN A 1 383 ? 168.511 118.819 185.535 1.00 90.66  ? 247  ASN A ND2 1 
ATOM 1687 N N   . ALA A 1 384 ? 165.616 115.645 185.319 1.00 82.78  ? 248  ALA A N   1 
ATOM 1688 C CA  . ALA A 1 384 ? 164.193 115.864 185.099 1.00 78.22  ? 248  ALA A CA  1 
ATOM 1689 C C   . ALA A 1 384 ? 163.838 117.329 184.886 1.00 73.76  ? 248  ALA A C   1 
ATOM 1690 O O   . ALA A 1 384 ? 162.732 117.619 184.422 1.00 70.69  ? 248  ALA A O   1 
ATOM 1691 C CB  . ALA A 1 384 ? 163.388 115.308 186.273 1.00 73.95  ? 248  ALA A CB  1 
ATOM 1692 N N   . ALA A 1 385 ? 164.737 118.257 185.215 1.00 74.13  ? 249  ALA A N   1 
ATOM 1693 C CA  . ALA A 1 385 ? 164.446 119.671 185.002 1.00 70.88  ? 249  ALA A CA  1 
ATOM 1694 C C   . ALA A 1 385 ? 164.367 119.997 183.516 1.00 70.90  ? 249  ALA A C   1 
ATOM 1695 O O   . ALA A 1 385 ? 163.435 120.675 183.064 1.00 69.24  ? 249  ALA A O   1 
ATOM 1696 C CB  . ALA A 1 385 ? 165.502 120.534 185.689 1.00 77.11  ? 249  ALA A CB  1 
ATOM 1697 N N   . GLN A 1 386 ? 165.343 119.520 182.739 1.00 71.89  ? 250  GLN A N   1 
ATOM 1698 C CA  . GLN A 1 386 ? 165.308 119.727 181.295 1.00 70.15  ? 250  GLN A CA  1 
ATOM 1699 C C   . GLN A 1 386 ? 164.107 119.031 180.674 1.00 65.74  ? 250  GLN A C   1 
ATOM 1700 O O   . GLN A 1 386 ? 163.471 119.569 179.758 1.00 61.66  ? 250  GLN A O   1 
ATOM 1701 C CB  . GLN A 1 386 ? 166.602 119.224 180.662 1.00 76.75  ? 250  GLN A CB  1 
ATOM 1702 C CG  . GLN A 1 386 ? 167.861 119.809 181.269 1.00 82.68  ? 250  GLN A CG  1 
ATOM 1703 C CD  . GLN A 1 386 ? 169.119 119.195 180.692 1.00 91.59  ? 250  GLN A CD  1 
ATOM 1704 O OE1 . GLN A 1 386 ? 169.103 118.634 179.596 1.00 89.96  ? 250  GLN A OE1 1 
ATOM 1705 N NE2 . GLN A 1 386 ? 170.217 119.291 181.431 1.00 95.45  ? 250  GLN A NE2 1 
ATOM 1706 N N   . VAL A 1 387 ? 163.782 117.832 181.161 1.00 65.02  ? 251  VAL A N   1 
ATOM 1707 C CA  . VAL A 1 387 ? 162.610 117.117 180.666 1.00 59.17  ? 251  VAL A CA  1 
ATOM 1708 C C   . VAL A 1 387 ? 161.342 117.906 180.957 1.00 57.83  ? 251  VAL A C   1 
ATOM 1709 O O   . VAL A 1 387 ? 160.460 118.024 180.101 1.00 54.48  ? 251  VAL A O   1 
ATOM 1710 C CB  . VAL A 1 387 ? 162.549 115.707 181.276 1.00 56.61  ? 251  VAL A CB  1 
ATOM 1711 C CG1 . VAL A 1 387 ? 161.328 114.972 180.774 1.00 52.68  ? 251  VAL A CG1 1 
ATOM 1712 C CG2 . VAL A 1 387 ? 163.804 114.936 180.940 1.00 66.35  ? 251  VAL A CG2 1 
ATOM 1713 N N   . LYS A 1 388 ? 161.226 118.458 182.167 1.00 61.02  ? 252  LYS A N   1 
ATOM 1714 C CA  . LYS A 1 388 ? 160.043 119.243 182.507 1.00 55.50  ? 252  LYS A CA  1 
ATOM 1715 C C   . LYS A 1 388 ? 159.931 120.489 181.639 1.00 52.48  ? 252  LYS A C   1 
ATOM 1716 O O   . LYS A 1 388 ? 158.839 120.827 181.170 1.00 54.73  ? 252  LYS A O   1 
ATOM 1717 C CB  . LYS A 1 388 ? 160.071 119.622 183.985 1.00 61.49  ? 252  LYS A CB  1 
ATOM 1718 C CG  . LYS A 1 388 ? 159.687 118.490 184.918 1.00 66.77  ? 252  LYS A CG  1 
ATOM 1719 C CD  . LYS A 1 388 ? 160.188 118.744 186.329 1.00 71.91  ? 252  LYS A CD  1 
ATOM 1720 C CE  . LYS A 1 388 ? 159.676 120.065 186.869 1.00 74.74  ? 252  LYS A CE  1 
ATOM 1721 N NZ  . LYS A 1 388 ? 160.203 120.335 188.235 1.00 77.17  ? 252  LYS A NZ  1 
ATOM 1722 N N   . ASP A 1 389 ? 161.046 121.189 181.411 1.00 53.66  ? 253  ASP A N   1 
ATOM 1723 C CA  . ASP A 1 389 ? 160.995 122.386 180.574 1.00 56.48  ? 253  ASP A CA  1 
ATOM 1724 C C   . ASP A 1 389 ? 160.612 122.045 179.138 1.00 53.74  ? 253  ASP A C   1 
ATOM 1725 O O   . ASP A 1 389 ? 159.788 122.735 178.518 1.00 53.30  ? 253  ASP A O   1 
ATOM 1726 C CB  . ASP A 1 389 ? 162.339 123.108 180.610 1.00 65.02  ? 253  ASP A CB  1 
ATOM 1727 C CG  . ASP A 1 389 ? 162.795 123.417 182.019 1.00 73.02  ? 253  ASP A CG  1 
ATOM 1728 O OD1 . ASP A 1 389 ? 161.938 123.467 182.925 1.00 72.36  ? 253  ASP A OD1 1 
ATOM 1729 O OD2 . ASP A 1 389 ? 164.012 123.611 182.223 1.00 76.07  ? 253  ASP A OD2 1 
ATOM 1730 N N   . ALA A 1 390 ? 161.195 120.978 178.594 1.00 50.60  ? 254  ALA A N   1 
ATOM 1731 C CA  . ALA A 1 390 ? 160.870 120.581 177.232 1.00 48.07  ? 254  ALA A CA  1 
ATOM 1732 C C   . ALA A 1 390 ? 159.421 120.133 177.118 1.00 46.06  ? 254  ALA A C   1 
ATOM 1733 O O   . ALA A 1 390 ? 158.758 120.424 176.121 1.00 46.39  ? 254  ALA A O   1 
ATOM 1734 C CB  . ALA A 1 390 ? 161.818 119.480 176.772 1.00 50.76  ? 254  ALA A CB  1 
ATOM 1735 N N   . LEU A 1 391 ? 158.910 119.423 178.126 1.00 42.95  ? 255  LEU A N   1 
ATOM 1736 C CA  . LEU A 1 391 ? 157.510 119.016 178.106 1.00 37.25  ? 255  LEU A CA  1 
ATOM 1737 C C   . LEU A 1 391 ? 156.579 120.212 178.217 1.00 36.93  ? 255  LEU A C   1 
ATOM 1738 O O   . LEU A 1 391 ? 155.501 120.208 177.620 1.00 36.27  ? 255  LEU A O   1 
ATOM 1739 C CB  . LEU A 1 391 ? 157.234 118.025 179.231 1.00 33.74  ? 255  LEU A CB  1 
ATOM 1740 C CG  . LEU A 1 391 ? 157.716 116.601 178.988 1.00 37.44  ? 255  LEU A CG  1 
ATOM 1741 C CD1 . LEU A 1 391 ? 157.687 115.807 180.269 1.00 41.10  ? 255  LEU A CD1 1 
ATOM 1742 C CD2 . LEU A 1 391 ? 156.848 115.949 177.944 1.00 31.61  ? 255  LEU A CD2 1 
ATOM 1743 N N   . THR A 1 392 ? 156.970 121.236 178.974 1.00 37.37  ? 256  THR A N   1 
ATOM 1744 C CA  . THR A 1 392 ? 156.190 122.467 179.027 1.00 31.54  ? 256  THR A CA  1 
ATOM 1745 C C   . THR A 1 392 ? 156.099 123.115 177.652 1.00 32.43  ? 256  THR A C   1 
ATOM 1746 O O   . THR A 1 392 ? 155.013 123.504 177.197 1.00 37.61  ? 256  THR A O   1 
ATOM 1747 C CB  . THR A 1 392 ? 156.825 123.427 180.027 1.00 35.49  ? 256  THR A CB  1 
ATOM 1748 O OG1 . THR A 1 392 ? 156.796 122.846 181.335 1.00 38.20  ? 256  THR A OG1 1 
ATOM 1749 C CG2 . THR A 1 392 ? 156.089 124.745 180.035 1.00 38.29  ? 256  THR A CG2 1 
ATOM 1750 N N   . LYS A 1 393 ? 157.241 123.242 176.975 1.00 35.78  ? 257  LYS A N   1 
ATOM 1751 C CA  . LYS A 1 393 ? 157.234 123.832 175.640 1.00 35.85  ? 257  LYS A CA  1 
ATOM 1752 C C   . LYS A 1 393 ? 156.430 122.979 174.667 1.00 31.82  ? 257  LYS A C   1 
ATOM 1753 O O   . LYS A 1 393 ? 155.712 123.508 173.810 1.00 30.54  ? 257  LYS A O   1 
ATOM 1754 C CB  . LYS A 1 393 ? 158.662 124.027 175.142 1.00 39.89  ? 257  LYS A CB  1 
ATOM 1755 C CG  . LYS A 1 393 ? 159.461 125.025 175.960 1.00 43.34  ? 257  LYS A CG  1 
ATOM 1756 C CD  . LYS A 1 393 ? 160.792 125.330 175.306 1.00 49.95  ? 257  LYS A CD  1 
ATOM 1757 C CE  . LYS A 1 393 ? 161.608 126.298 176.140 1.00 56.68  ? 257  LYS A CE  1 
ATOM 1758 N NZ  . LYS A 1 393 ? 161.949 125.729 177.469 1.00 53.82  ? 257  LYS A NZ  1 
ATOM 1759 N N   . MET A 1 394 ? 156.528 121.655 174.792 1.00 30.49  ? 258  MET A N   1 
ATOM 1760 C CA  . MET A 1 394 ? 155.762 120.758 173.935 1.00 28.59  ? 258  MET A CA  1 
ATOM 1761 C C   . MET A 1 394 ? 154.266 120.898 174.168 1.00 27.91  ? 258  MET A C   1 
ATOM 1762 O O   . MET A 1 394 ? 153.483 120.866 173.218 1.00 32.39  ? 258  MET A O   1 
ATOM 1763 C CB  . MET A 1 394 ? 156.198 119.317 174.170 1.00 28.99  ? 258  MET A CB  1 
ATOM 1764 C CG  . MET A 1 394 ? 157.226 118.830 173.199 1.00 36.75  ? 258  MET A CG  1 
ATOM 1765 S SD  . MET A 1 394 ? 158.177 117.461 173.848 1.00 48.95  ? 258  MET A SD  1 
ATOM 1766 C CE  . MET A 1 394 ? 156.869 116.330 174.264 1.00 43.81  ? 258  MET A CE  1 
ATOM 1767 N N   . ARG A 1 395 ? 153.845 121.023 175.426 1.00 25.81  ? 259  ARG A N   1 
ATOM 1768 C CA  . ARG A 1 395 ? 152.424 121.171 175.713 1.00 19.22  ? 259  ARG A CA  1 
ATOM 1769 C C   . ARG A 1 395 ? 151.890 122.477 175.158 1.00 21.40  ? 259  ARG A C   1 
ATOM 1770 O O   . ARG A 1 395 ? 150.798 122.513 174.581 1.00 23.97  ? 259  ARG A O   1 
ATOM 1771 C CB  . ARG A 1 395 ? 152.173 121.089 177.214 1.00 17.13  ? 259  ARG A CB  1 
ATOM 1772 C CG  . ARG A 1 395 ? 150.740 120.814 177.550 1.00 17.10  ? 259  ARG A CG  1 
ATOM 1773 C CD  . ARG A 1 395 ? 150.543 120.583 179.024 1.00 17.93  ? 259  ARG A CD  1 
ATOM 1774 N NE  . ARG A 1 395 ? 149.296 119.873 179.278 1.00 17.63  ? 259  ARG A NE  1 
ATOM 1775 C CZ  . ARG A 1 395 ? 148.096 120.432 179.255 1.00 16.72  ? 259  ARG A CZ  1 
ATOM 1776 N NH1 . ARG A 1 395 ? 147.938 121.716 178.994 1.00 18.39  ? 259  ARG A NH1 1 
ATOM 1777 N NH2 . ARG A 1 395 ? 147.028 119.682 179.496 1.00 17.94  ? 259  ARG A NH2 1 
ATOM 1778 N N   . ALA A 1 396 ? 152.646 123.564 175.323 1.00 24.52  ? 260  ALA A N   1 
ATOM 1779 C CA  . ALA A 1 396 ? 152.225 124.833 174.741 1.00 22.93  ? 260  ALA A CA  1 
ATOM 1780 C C   . ALA A 1 396 ? 152.118 124.731 173.226 1.00 29.24  ? 260  ALA A C   1 
ATOM 1781 O O   . ALA A 1 396 ? 151.147 125.211 172.628 1.00 31.87  ? 260  ALA A O   1 
ATOM 1782 C CB  . ALA A 1 396 ? 153.200 125.937 175.136 1.00 24.00  ? 260  ALA A CB  1 
ATOM 1783 N N   . ALA A 1 397 ? 153.101 124.088 172.590 1.00 28.28  ? 261  ALA A N   1 
ATOM 1784 C CA  . ALA A 1 397 ? 153.085 123.939 171.140 1.00 26.30  ? 261  ALA A CA  1 
ATOM 1785 C C   . ALA A 1 397 ? 151.913 123.088 170.674 1.00 29.85  ? 261  ALA A C   1 
ATOM 1786 O O   . ALA A 1 397 ? 151.290 123.396 169.656 1.00 37.90  ? 261  ALA A O   1 
ATOM 1787 C CB  . ALA A 1 397 ? 154.401 123.335 170.669 1.00 31.87  ? 261  ALA A CB  1 
ATOM 1788 N N   . ALA A 1 398 ? 151.608 122.005 171.387 1.00 27.37  ? 262  ALA A N   1 
ATOM 1789 C CA  . ALA A 1 398 ? 150.492 121.152 170.996 1.00 26.11  ? 262  ALA A CA  1 
ATOM 1790 C C   . ALA A 1 398 ? 149.162 121.871 171.155 1.00 29.11  ? 262  ALA A C   1 
ATOM 1791 O O   . ALA A 1 398 ? 148.273 121.736 170.307 1.00 38.31  ? 262  ALA A O   1 
ATOM 1792 C CB  . ALA A 1 398 ? 150.503 119.862 171.810 1.00 24.89  ? 262  ALA A CB  1 
ATOM 1793 N N   . LEU A 1 399 ? 149.002 122.638 172.237 1.00 27.10  ? 263  LEU A N   1 
ATOM 1794 C CA  . LEU A 1 399 ? 147.783 123.422 172.401 1.00 26.58  ? 263  LEU A CA  1 
ATOM 1795 C C   . LEU A 1 399 ? 147.643 124.451 171.288 1.00 30.88  ? 263  LEU A C   1 
ATOM 1796 O O   . LEU A 1 399 ? 146.538 124.684 170.788 1.00 32.30  ? 263  LEU A O   1 
ATOM 1797 C CB  . LEU A 1 399 ? 147.770 124.106 173.766 1.00 24.00  ? 263  LEU A CB  1 
ATOM 1798 C CG  . LEU A 1 399 ? 147.653 123.251 175.025 1.00 20.53  ? 263  LEU A CG  1 
ATOM 1799 C CD1 . LEU A 1 399 ? 147.632 124.134 176.247 1.00 17.87  ? 263  LEU A CD1 1 
ATOM 1800 C CD2 . LEU A 1 399 ? 146.410 122.412 174.971 1.00 20.22  ? 263  LEU A CD2 1 
ATOM 1801 N N   . ASP A 1 400 ? 148.749 125.088 170.896 1.00 30.90  ? 264  ASP A N   1 
ATOM 1802 C CA  . ASP A 1 400 ? 148.701 126.037 169.787 1.00 33.51  ? 264  ASP A CA  1 
ATOM 1803 C C   . ASP A 1 400 ? 148.364 125.348 168.470 1.00 39.50  ? 264  ASP A C   1 
ATOM 1804 O O   . ASP A 1 400 ? 147.602 125.887 167.662 1.00 45.45  ? 264  ASP A O   1 
ATOM 1805 C CB  . ASP A 1 400 ? 150.031 126.776 169.666 1.00 36.49  ? 264  ASP A CB  1 
ATOM 1806 C CG  . ASP A 1 400 ? 150.099 128.000 170.546 1.00 43.27  ? 264  ASP A CG  1 
ATOM 1807 O OD1 . ASP A 1 400 ? 149.040 128.609 170.796 1.00 44.43  ? 264  ASP A OD1 1 
ATOM 1808 O OD2 . ASP A 1 400 ? 151.214 128.359 170.981 1.00 42.66  ? 264  ASP A OD2 1 
ATOM 1809 N N   . ALA A 1 401 ? 148.936 124.168 168.228 1.00 36.89  ? 265  ALA A N   1 
ATOM 1810 C CA  . ALA A 1 401 ? 148.692 123.461 166.975 1.00 36.17  ? 265  ALA A CA  1 
ATOM 1811 C C   . ALA A 1 401 ? 147.250 122.990 166.875 1.00 42.90  ? 265  ALA A C   1 
ATOM 1812 O O   . ALA A 1 401 ? 146.676 122.966 165.782 1.00 50.75  ? 265  ALA A O   1 
ATOM 1813 C CB  . ALA A 1 401 ? 149.648 122.280 166.841 1.00 34.48  ? 265  ALA A CB  1 
ATOM 1814 N N   . GLN A 1 402 ? 146.651 122.601 168.001 1.00 39.87  ? 266  GLN A N   1 
ATOM 1815 C CA  . GLN A 1 402 ? 145.250 122.195 167.981 1.00 39.75  ? 266  GLN A CA  1 
ATOM 1816 C C   . GLN A 1 402 ? 144.343 123.343 167.567 1.00 48.11  ? 266  GLN A C   1 
ATOM 1817 O O   . GLN A 1 402 ? 143.274 123.113 166.992 1.00 58.28  ? 266  GLN A O   1 
ATOM 1818 C CB  . GLN A 1 402 ? 144.844 121.662 169.352 1.00 38.29  ? 266  GLN A CB  1 
ATOM 1819 C CG  . GLN A 1 402 ? 143.442 121.111 169.419 1.00 46.71  ? 266  GLN A CG  1 
ATOM 1820 C CD  . GLN A 1 402 ? 143.072 120.658 170.811 1.00 52.06  ? 266  GLN A CD  1 
ATOM 1821 O OE1 . GLN A 1 402 ? 143.753 120.983 171.780 1.00 46.78  ? 266  GLN A OE1 1 
ATOM 1822 N NE2 . GLN A 1 402 ? 141.990 119.902 170.920 1.00 55.71  ? 266  GLN A NE2 1 
ATOM 1823 N N   . LYS A 1 403 ? 144.743 124.582 167.856 1.00 47.76  ? 267  LYS A N   1 
ATOM 1824 C CA  . LYS A 1 403 ? 143.955 125.736 167.440 1.00 48.94  ? 267  LYS A CA  1 
ATOM 1825 C C   . LYS A 1 403 ? 143.961 125.894 165.926 1.00 57.66  ? 267  LYS A C   1 
ATOM 1826 O O   . LYS A 1 403 ? 142.937 126.239 165.328 1.00 64.21  ? 267  LYS A O   1 
ATOM 1827 C CB  . LYS A 1 403 ? 144.489 127.005 168.104 1.00 50.00  ? 267  LYS A CB  1 
ATOM 1828 C CG  . LYS A 1 403 ? 144.484 126.987 169.623 1.00 49.73  ? 267  LYS A CG  1 
ATOM 1829 C CD  . LYS A 1 403 ? 143.074 127.000 170.172 1.00 52.50  ? 267  LYS A CD  1 
ATOM 1830 C CE  . LYS A 1 403 ? 143.073 127.218 171.673 1.00 44.12  ? 267  LYS A CE  1 
ATOM 1831 N NZ  . LYS A 1 403 ? 141.689 127.332 172.213 1.00 46.32  ? 267  LYS A NZ  1 
ATOM 1832 N N   . ALA A 1 404 ? 145.107 125.645 165.291 1.00 59.49  ? 268  ALA A N   1 
ATOM 1833 C CA  . ALA A 1 404 ? 145.280 125.867 163.856 1.00 64.55  ? 268  ALA A CA  1 
ATOM 1834 C C   . ALA A 1 404 ? 144.608 124.739 163.071 1.00 67.39  ? 268  ALA A C   1 
ATOM 1835 O O   . ALA A 1 404 ? 145.249 123.842 162.522 1.00 64.55  ? 268  ALA A O   1 
ATOM 1836 C CB  . ALA A 1 404 ? 146.757 125.980 163.510 1.00 58.35  ? 268  ALA A CB  1 
ATOM 1837 N N   . THR A 1 405 ? 143.282 124.802 163.029 1.00 71.75  ? 269  THR A N   1 
ATOM 1838 C CA  . THR A 1 405 ? 142.526 123.856 162.225 1.00 75.06  ? 269  THR A CA  1 
ATOM 1839 C C   . THR A 1 405 ? 142.783 124.118 160.743 1.00 78.12  ? 269  THR A C   1 
ATOM 1840 O O   . THR A 1 405 ? 142.819 125.275 160.317 1.00 75.03  ? 269  THR A O   1 
ATOM 1841 C CB  . THR A 1 405 ? 141.032 123.966 162.516 1.00 74.16  ? 269  THR A CB  1 
ATOM 1842 O OG1 . THR A 1 405 ? 140.577 125.282 162.184 1.00 70.68  ? 269  THR A OG1 1 
ATOM 1843 C CG2 . THR A 1 405 ? 140.756 123.698 163.982 1.00 70.67  ? 269  THR A CG2 1 
ATOM 1844 N N   . PRO A 1 406 ? 142.976 123.075 159.941 1.00 79.01  ? 270  PRO A N   1 
ATOM 1845 C CA  . PRO A 1 406 ? 143.219 123.270 158.513 1.00 79.57  ? 270  PRO A CA  1 
ATOM 1846 C C   . PRO A 1 406 ? 142.045 123.969 157.855 1.00 85.95  ? 270  PRO A C   1 
ATOM 1847 O O   . PRO A 1 406 ? 140.884 123.714 158.210 1.00 87.65  ? 270  PRO A O   1 
ATOM 1848 C CB  . PRO A 1 406 ? 143.382 121.838 157.982 1.00 76.78  ? 270  PRO A CB  1 
ATOM 1849 C CG  . PRO A 1 406 ? 143.760 121.037 159.164 1.00 74.95  ? 270  PRO A CG  1 
ATOM 1850 C CD  . PRO A 1 406 ? 143.037 121.654 160.317 1.00 76.88  ? 270  PRO A CD  1 
ATOM 1851 N N   . PRO A 1 407 ? 142.301 124.860 156.899 1.00 88.14  ? 271  PRO A N   1 
ATOM 1852 C CA  . PRO A 1 407 ? 141.194 125.526 156.202 1.00 88.20  ? 271  PRO A CA  1 
ATOM 1853 C C   . PRO A 1 407 ? 140.358 124.541 155.404 1.00 91.88  ? 271  PRO A C   1 
ATOM 1854 O O   . PRO A 1 407 ? 140.845 123.943 154.439 1.00 90.27  ? 271  PRO A O   1 
ATOM 1855 C CB  . PRO A 1 407 ? 141.906 126.537 155.295 1.00 84.05  ? 271  PRO A CB  1 
ATOM 1856 C CG  . PRO A 1 407 ? 143.285 125.994 155.128 1.00 81.52  ? 271  PRO A CG  1 
ATOM 1857 C CD  . PRO A 1 407 ? 143.616 125.320 156.422 1.00 83.04  ? 271  PRO A CD  1 
ATOM 1858 N N   . LYS A 1 408 ? 139.103 124.366 155.811 1.00 95.57  ? 272  LYS A N   1 
ATOM 1859 C CA  . LYS A 1 408 ? 138.186 123.424 155.173 1.00 100.84 ? 272  LYS A CA  1 
ATOM 1860 C C   . LYS A 1 408 ? 138.754 122.008 155.162 1.00 97.16  ? 272  LYS A C   1 
ATOM 1861 O O   . LYS A 1 408 ? 138.255 121.125 155.858 1.00 92.93  ? 272  LYS A O   1 
ATOM 1862 C CB  . LYS A 1 408 ? 137.859 123.872 153.746 1.00 102.13 ? 272  LYS A CB  1 
ATOM 1863 C CG  . LYS A 1 408 ? 137.213 125.244 153.655 1.00 99.25  ? 272  LYS A CG  1 
ATOM 1864 C CD  . LYS A 1 408 ? 136.957 125.635 152.209 1.00 97.06  ? 272  LYS A CD  1 
ATOM 1865 C CE  . LYS A 1 408 ? 136.196 126.945 152.117 1.00 101.69 ? 272  LYS A CE  1 
ATOM 1866 N NZ  . LYS A 1 408 ? 134.847 126.848 152.745 1.00 104.65 ? 272  LYS A NZ  1 
ATOM 1867 N N   . SER A 1 416 ? 130.855 116.464 161.507 1.00 110.03 ? 280  SER A N   1 
ATOM 1868 C CA  . SER A 1 416 ? 132.169 117.093 161.560 1.00 109.02 ? 280  SER A CA  1 
ATOM 1869 C C   . SER A 1 416 ? 133.281 116.050 161.506 1.00 106.73 ? 280  SER A C   1 
ATOM 1870 O O   . SER A 1 416 ? 133.915 115.764 162.519 1.00 101.29 ? 280  SER A O   1 
ATOM 1871 C CB  . SER A 1 416 ? 132.301 117.939 162.825 1.00 101.52 ? 280  SER A CB  1 
ATOM 1872 O OG  . SER A 1 416 ? 132.007 117.172 163.979 1.00 100.37 ? 280  SER A OG  1 
ATOM 1873 N N   . PRO A 1 417 ? 133.511 115.477 160.321 1.00 109.50 ? 281  PRO A N   1 
ATOM 1874 C CA  . PRO A 1 417 ? 134.543 114.434 160.203 1.00 107.82 ? 281  PRO A CA  1 
ATOM 1875 C C   . PRO A 1 417 ? 135.936 114.912 160.563 1.00 102.02 ? 281  PRO A C   1 
ATOM 1876 O O   . PRO A 1 417 ? 136.732 114.128 161.095 1.00 100.56 ? 281  PRO A O   1 
ATOM 1877 C CB  . PRO A 1 417 ? 134.455 114.021 158.726 1.00 112.25 ? 281  PRO A CB  1 
ATOM 1878 C CG  . PRO A 1 417 ? 133.102 114.477 158.272 1.00 110.42 ? 281  PRO A CG  1 
ATOM 1879 C CD  . PRO A 1 417 ? 132.833 115.731 159.040 1.00 110.36 ? 281  PRO A CD  1 
ATOM 1880 N N   . GLU A 1 418 ? 136.260 116.176 160.287 1.00 99.49  ? 282  GLU A N   1 
ATOM 1881 C CA  . GLU A 1 418 ? 137.606 116.675 160.542 1.00 95.26  ? 282  GLU A CA  1 
ATOM 1882 C C   . GLU A 1 418 ? 137.785 117.081 162.000 1.00 93.26  ? 282  GLU A C   1 
ATOM 1883 O O   . GLU A 1 418 ? 138.728 116.637 162.664 1.00 86.54  ? 282  GLU A O   1 
ATOM 1884 C CB  . GLU A 1 418 ? 137.907 117.857 159.619 1.00 94.31  ? 282  GLU A CB  1 
ATOM 1885 C CG  . GLU A 1 418 ? 139.289 118.454 159.803 1.00 91.03  ? 282  GLU A CG  1 
ATOM 1886 C CD  . GLU A 1 418 ? 139.431 119.806 159.132 1.00 96.59  ? 282  GLU A CD  1 
ATOM 1887 O OE1 . GLU A 1 418 ? 138.397 120.425 158.805 1.00 98.38  ? 282  GLU A OE1 1 
ATOM 1888 O OE2 . GLU A 1 418 ? 140.578 120.252 158.932 1.00 95.67  ? 282  GLU A OE2 1 
ATOM 1889 N N   . MET A 1 419 ? 136.886 117.926 162.512 1.00 94.33  ? 283  MET A N   1 
ATOM 1890 C CA  . MET A 1 419 ? 137.024 118.424 163.877 1.00 87.22  ? 283  MET A CA  1 
ATOM 1891 C C   . MET A 1 419 ? 136.946 117.294 164.895 1.00 87.33  ? 283  MET A C   1 
ATOM 1892 O O   . MET A 1 419 ? 137.594 117.351 165.945 1.00 86.27  ? 283  MET A O   1 
ATOM 1893 C CB  . MET A 1 419 ? 135.957 119.478 164.158 1.00 89.12  ? 283  MET A CB  1 
ATOM 1894 C CG  . MET A 1 419 ? 136.072 120.726 163.299 1.00 93.56  ? 283  MET A CG  1 
ATOM 1895 S SD  . MET A 1 419 ? 137.585 121.659 163.602 1.00 98.90  ? 283  MET A SD  1 
ATOM 1896 C CE  . MET A 1 419 ? 138.583 121.171 162.199 1.00 88.95  ? 283  MET A CE  1 
ATOM 1897 N N   . LYS A 1 420 ? 136.152 116.265 164.610 1.00 90.28  ? 284  LYS A N   1 
ATOM 1898 C CA  . LYS A 1 420 ? 136.095 115.110 165.495 1.00 90.41  ? 284  LYS A CA  1 
ATOM 1899 C C   . LYS A 1 420 ? 137.347 114.245 165.410 1.00 85.69  ? 284  LYS A C   1 
ATOM 1900 O O   . LYS A 1 420 ? 137.499 113.327 166.221 1.00 85.17  ? 284  LYS A O   1 
ATOM 1901 C CB  . LYS A 1 420 ? 134.854 114.272 165.178 1.00 95.89  ? 284  LYS A CB  1 
ATOM 1902 C CG  . LYS A 1 420 ? 134.402 113.352 166.300 1.00 97.89  ? 284  LYS A CG  1 
ATOM 1903 C CD  . LYS A 1 420 ? 133.222 112.499 165.867 1.00 100.18 ? 284  LYS A CD  1 
ATOM 1904 C CE  . LYS A 1 420 ? 132.827 111.512 166.951 1.00 104.13 ? 284  LYS A CE  1 
ATOM 1905 N NZ  . LYS A 1 420 ? 131.710 110.631 166.515 1.00 105.82 ? 284  LYS A NZ  1 
ATOM 1906 N N   . ASP A 1 421 ? 138.235 114.504 164.455 1.00 82.02  ? 285  ASP A N   1 
ATOM 1907 C CA  . ASP A 1 421 ? 139.461 113.729 164.303 1.00 78.06  ? 285  ASP A CA  1 
ATOM 1908 C C   . ASP A 1 421 ? 140.723 114.555 164.483 1.00 75.67  ? 285  ASP A C   1 
ATOM 1909 O O   . ASP A 1 421 ? 141.687 114.072 165.079 1.00 76.26  ? 285  ASP A O   1 
ATOM 1910 C CB  . ASP A 1 421 ? 139.493 113.052 162.929 1.00 83.37  ? 285  ASP A CB  1 
ATOM 1911 C CG  . ASP A 1 421 ? 140.500 111.925 162.863 1.00 88.11  ? 285  ASP A CG  1 
ATOM 1912 O OD1 . ASP A 1 421 ? 141.029 111.541 163.926 1.00 81.95  ? 285  ASP A OD1 1 
ATOM 1913 O OD2 . ASP A 1 421 ? 140.762 111.423 161.750 1.00 91.95  ? 285  ASP A OD2 1 
ATOM 1914 N N   . PHE A 1 422 ? 140.753 115.783 163.964 1.00 72.76  ? 286  PHE A N   1 
ATOM 1915 C CA  . PHE A 1 422 ? 141.890 116.669 164.200 1.00 68.35  ? 286  PHE A CA  1 
ATOM 1916 C C   . PHE A 1 422 ? 142.000 117.023 165.680 1.00 65.97  ? 286  PHE A C   1 
ATOM 1917 O O   . PHE A 1 422 ? 143.039 116.796 166.323 1.00 65.36  ? 286  PHE A O   1 
ATOM 1918 C CB  . PHE A 1 422 ? 141.717 117.924 163.340 1.00 70.49  ? 286  PHE A CB  1 
ATOM 1919 C CG  . PHE A 1 422 ? 142.839 118.914 163.442 1.00 68.25  ? 286  PHE A CG  1 
ATOM 1920 C CD1 . PHE A 1 422 ? 144.029 118.705 162.771 1.00 66.88  ? 286  PHE A CD1 1 
ATOM 1921 C CD2 . PHE A 1 422 ? 142.686 120.079 164.169 1.00 66.32  ? 286  PHE A CD2 1 
ATOM 1922 C CE1 . PHE A 1 422 ? 145.054 119.624 162.850 1.00 63.29  ? 286  PHE A CE1 1 
ATOM 1923 C CE2 . PHE A 1 422 ? 143.707 120.998 164.249 1.00 62.37  ? 286  PHE A CE2 1 
ATOM 1924 C CZ  . PHE A 1 422 ? 144.891 120.770 163.589 1.00 59.58  ? 286  PHE A CZ  1 
ATOM 1925 N N   . ARG A 1 423 ? 140.907 117.527 166.250 1.00 66.20  ? 287  ARG A N   1 
ATOM 1926 C CA  . ARG A 1 423 ? 140.910 117.887 167.658 1.00 60.06  ? 287  ARG A CA  1 
ATOM 1927 C C   . ARG A 1 423 ? 141.059 116.665 168.548 1.00 59.21  ? 287  ARG A C   1 
ATOM 1928 O O   . ARG A 1 423 ? 141.693 116.755 169.597 1.00 59.19  ? 287  ARG A O   1 
ATOM 1929 C CB  . ARG A 1 423 ? 139.639 118.653 168.010 1.00 64.69  ? 287  ARG A CB  1 
ATOM 1930 C CG  . ARG A 1 423 ? 139.473 119.945 167.236 1.00 73.92  ? 287  ARG A CG  1 
ATOM 1931 C CD  . ARG A 1 423 ? 138.292 120.745 167.749 1.00 81.84  ? 287  ARG A CD  1 
ATOM 1932 N NE  . ARG A 1 423 ? 138.477 121.151 169.137 1.00 80.19  ? 287  ARG A NE  1 
ATOM 1933 C CZ  . ARG A 1 423 ? 139.131 122.240 169.515 1.00 80.73  ? 287  ARG A CZ  1 
ATOM 1934 N NH1 . ARG A 1 423 ? 139.686 123.055 168.633 1.00 79.67  ? 287  ARG A NH1 1 
ATOM 1935 N NH2 . ARG A 1 423 ? 139.231 122.519 170.812 1.00 76.26  ? 287  ARG A NH2 1 
ATOM 1936 N N   . HIS A 1 424 ? 140.486 115.524 168.162 1.00 59.46  ? 288  HIS A N   1 
ATOM 1937 C CA  . HIS A 1 424 ? 140.661 114.315 168.964 1.00 57.27  ? 288  HIS A CA  1 
ATOM 1938 C C   . HIS A 1 424 ? 142.110 113.848 168.957 1.00 54.02  ? 288  HIS A C   1 
ATOM 1939 O O   . HIS A 1 424 ? 142.639 113.418 169.992 1.00 57.58  ? 288  HIS A O   1 
ATOM 1940 C CB  . HIS A 1 424 ? 139.745 113.207 168.460 1.00 61.68  ? 288  HIS A CB  1 
ATOM 1941 C CG  . HIS A 1 424 ? 139.912 111.914 169.190 1.00 62.06  ? 288  HIS A CG  1 
ATOM 1942 N ND1 . HIS A 1 424 ? 139.702 111.793 170.546 1.00 64.45  ? 288  HIS A ND1 1 
ATOM 1943 C CD2 . HIS A 1 424 ? 140.271 110.684 168.753 1.00 64.37  ? 288  HIS A CD2 1 
ATOM 1944 C CE1 . HIS A 1 424 ? 139.924 110.544 170.914 1.00 65.05  ? 288  HIS A CE1 1 
ATOM 1945 N NE2 . HIS A 1 424 ? 140.270 109.850 169.845 1.00 66.19  ? 288  HIS A NE2 1 
ATOM 1946 N N   . GLY A 1 425 ? 142.768 113.922 167.802 1.00 51.28  ? 289  GLY A N   1 
ATOM 1947 C CA  . GLY A 1 425 ? 144.175 113.571 167.748 1.00 51.25  ? 289  GLY A CA  1 
ATOM 1948 C C   . GLY A 1 425 ? 145.019 114.452 168.643 1.00 49.87  ? 289  GLY A C   1 
ATOM 1949 O O   . GLY A 1 425 ? 145.883 113.965 169.379 1.00 50.75  ? 289  GLY A O   1 
ATOM 1950 N N   . PHE A 1 426 ? 144.758 115.761 168.629 1.00 47.01  ? 290  PHE A N   1 
ATOM 1951 C CA  . PHE A 1 426 ? 145.546 116.629 169.498 1.00 40.22  ? 290  PHE A CA  1 
ATOM 1952 C C   . PHE A 1 426 ? 145.157 116.492 170.966 1.00 39.14  ? 290  PHE A C   1 
ATOM 1953 O O   . PHE A 1 426 ? 146.001 116.699 171.843 1.00 41.56  ? 290  PHE A O   1 
ATOM 1954 C CB  . PHE A 1 426 ? 145.439 118.072 169.034 1.00 42.88  ? 290  PHE A CB  1 
ATOM 1955 C CG  . PHE A 1 426 ? 146.381 118.399 167.929 1.00 44.63  ? 290  PHE A CG  1 
ATOM 1956 C CD1 . PHE A 1 426 ? 147.709 118.649 168.198 1.00 43.64  ? 290  PHE A CD1 1 
ATOM 1957 C CD2 . PHE A 1 426 ? 145.950 118.422 166.620 1.00 48.84  ? 290  PHE A CD2 1 
ATOM 1958 C CE1 . PHE A 1 426 ? 148.584 118.935 167.187 1.00 47.86  ? 290  PHE A CE1 1 
ATOM 1959 C CE2 . PHE A 1 426 ? 146.823 118.708 165.605 1.00 49.38  ? 290  PHE A CE2 1 
ATOM 1960 C CZ  . PHE A 1 426 ? 148.142 118.969 165.889 1.00 50.52  ? 290  PHE A CZ  1 
ATOM 1961 N N   . ASP A 1 427 ? 143.905 116.140 171.259 1.00 39.70  ? 291  ASP A N   1 
ATOM 1962 C CA  . ASP A 1 427 ? 143.522 115.858 172.637 1.00 34.68  ? 291  ASP A CA  1 
ATOM 1963 C C   . ASP A 1 427 ? 144.295 114.670 173.181 1.00 36.15  ? 291  ASP A C   1 
ATOM 1964 O O   . ASP A 1 427 ? 144.795 114.708 174.312 1.00 39.93  ? 291  ASP A O   1 
ATOM 1965 C CB  . ASP A 1 427 ? 142.020 115.594 172.724 1.00 39.21  ? 291  ASP A CB  1 
ATOM 1966 C CG  . ASP A 1 427 ? 141.192 116.838 172.483 1.00 49.45  ? 291  ASP A CG  1 
ATOM 1967 O OD1 . ASP A 1 427 ? 141.774 117.886 172.138 1.00 49.29  ? 291  ASP A OD1 1 
ATOM 1968 O OD2 . ASP A 1 427 ? 139.957 116.769 172.640 1.00 53.00  ? 291  ASP A OD2 1 
ATOM 1969 N N   . ILE A 1 428 ? 144.417 113.609 172.383 1.00 39.36  ? 292  ILE A N   1 
ATOM 1970 C CA  . ILE A 1 428 ? 145.220 112.462 172.799 1.00 38.33  ? 292  ILE A CA  1 
ATOM 1971 C C   . ILE A 1 428 ? 146.683 112.859 172.949 1.00 39.56  ? 292  ILE A C   1 
ATOM 1972 O O   . ILE A 1 428 ? 147.373 112.416 173.878 1.00 42.64  ? 292  ILE A O   1 
ATOM 1973 C CB  . ILE A 1 428 ? 145.043 111.301 171.805 1.00 39.87  ? 292  ILE A CB  1 
ATOM 1974 C CG1 . ILE A 1 428 ? 143.591 110.833 171.805 1.00 45.61  ? 292  ILE A CG1 1 
ATOM 1975 C CG2 . ILE A 1 428 ? 145.960 110.155 172.159 1.00 43.68  ? 292  ILE A CG2 1 
ATOM 1976 C CD1 . ILE A 1 428 ? 143.354 109.609 170.972 1.00 55.64  ? 292  ILE A CD1 1 
ATOM 1977 N N   . LEU A 1 429 ? 147.181 113.704 172.043 1.00 37.89  ? 293  LEU A N   1 
ATOM 1978 C CA  . LEU A 1 429 ? 148.576 114.128 172.120 1.00 33.06  ? 293  LEU A CA  1 
ATOM 1979 C C   . LEU A 1 429 ? 148.863 114.861 173.423 1.00 31.44  ? 293  LEU A C   1 
ATOM 1980 O O   . LEU A 1 429 ? 149.832 114.552 174.127 1.00 36.10  ? 293  LEU A O   1 
ATOM 1981 C CB  . LEU A 1 429 ? 148.913 115.019 170.931 1.00 35.69  ? 293  LEU A CB  1 
ATOM 1982 C CG  . LEU A 1 429 ? 150.389 115.132 170.583 1.00 34.47  ? 293  LEU A CG  1 
ATOM 1983 C CD1 . LEU A 1 429 ? 150.736 114.081 169.562 1.00 45.17  ? 293  LEU A CD1 1 
ATOM 1984 C CD2 . LEU A 1 429 ? 150.690 116.512 170.060 1.00 36.91  ? 293  LEU A CD2 1 
ATOM 1985 N N   . VAL A 1 430 ? 148.032 115.847 173.761 1.00 30.52  ? 294  VAL A N   1 
ATOM 1986 C CA  . VAL A 1 430 ? 148.260 116.595 174.990 1.00 24.71  ? 294  VAL A CA  1 
ATOM 1987 C C   . VAL A 1 430 ? 147.995 115.737 176.220 1.00 28.28  ? 294  VAL A C   1 
ATOM 1988 O O   . VAL A 1 430 ? 148.606 115.963 177.265 1.00 29.85  ? 294  VAL A O   1 
ATOM 1989 C CB  . VAL A 1 430 ? 147.422 117.883 175.014 1.00 18.90  ? 294  VAL A CB  1 
ATOM 1990 C CG1 . VAL A 1 430 ? 147.801 118.717 176.197 1.00 22.03  ? 294  VAL A CG1 1 
ATOM 1991 C CG2 . VAL A 1 430 ? 147.652 118.677 173.756 1.00 22.70  ? 294  VAL A CG2 1 
ATOM 1992 N N   . GLY A 1 431 ? 147.116 114.739 176.130 1.00 31.60  ? 295  GLY A N   1 
ATOM 1993 C CA  . GLY A 1 431 ? 146.994 113.792 177.227 1.00 31.71  ? 295  GLY A CA  1 
ATOM 1994 C C   . GLY A 1 431 ? 148.274 113.012 177.461 1.00 33.80  ? 295  GLY A C   1 
ATOM 1995 O O   . GLY A 1 431 ? 148.664 112.762 178.604 1.00 38.44  ? 295  GLY A O   1 
ATOM 1996 N N   . GLN A 1 432 ? 148.949 112.623 176.381 1.00 32.55  ? 296  GLN A N   1 
ATOM 1997 C CA  . GLN A 1 432 ? 150.234 111.945 176.533 1.00 36.43  ? 296  GLN A CA  1 
ATOM 1998 C C   . GLN A 1 432 ? 151.300 112.885 177.082 1.00 36.68  ? 296  GLN A C   1 
ATOM 1999 O O   . GLN A 1 432 ? 152.156 112.468 177.872 1.00 42.36  ? 296  GLN A O   1 
ATOM 2000 C CB  . GLN A 1 432 ? 150.669 111.344 175.201 1.00 39.03  ? 296  GLN A CB  1 
ATOM 2001 C CG  . GLN A 1 432 ? 149.805 110.181 174.772 1.00 40.49  ? 296  GLN A CG  1 
ATOM 2002 C CD  . GLN A 1 432 ? 149.968 109.851 173.315 1.00 45.40  ? 296  GLN A CD  1 
ATOM 2003 O OE1 . GLN A 1 432 ? 150.640 110.567 172.582 1.00 48.52  ? 296  GLN A OE1 1 
ATOM 2004 N NE2 . GLN A 1 432 ? 149.351 108.762 172.882 1.00 49.25  ? 296  GLN A NE2 1 
ATOM 2005 N N   . ILE A 1 433 ? 151.266 114.158 176.681 1.00 31.90  ? 297  ILE A N   1 
ATOM 2006 C CA  . ILE A 1 433 ? 152.192 115.129 177.265 1.00 28.46  ? 297  ILE A CA  1 
ATOM 2007 C C   . ILE A 1 433 ? 151.936 115.274 178.761 1.00 31.27  ? 297  ILE A C   1 
ATOM 2008 O O   . ILE A 1 433 ? 152.873 115.385 179.556 1.00 36.85  ? 297  ILE A O   1 
ATOM 2009 C CB  . ILE A 1 433 ? 152.098 116.489 176.551 1.00 23.80  ? 297  ILE A CB  1 
ATOM 2010 C CG1 . ILE A 1 433 ? 152.382 116.343 175.063 1.00 24.71  ? 297  ILE A CG1 1 
ATOM 2011 C CG2 . ILE A 1 433 ? 153.091 117.450 177.140 1.00 24.03  ? 297  ILE A CG2 1 
ATOM 2012 C CD1 . ILE A 1 433 ? 152.496 117.647 174.333 1.00 18.66  ? 297  ILE A CD1 1 
ATOM 2013 N N   . ASP A 1 434 ? 150.666 115.286 179.165 1.00 29.82  ? 298  ASP A N   1 
ATOM 2014 C CA  . ASP A 1 434 ? 150.340 115.368 180.586 1.00 27.47  ? 298  ASP A CA  1 
ATOM 2015 C C   . ASP A 1 434 ? 150.823 114.138 181.340 1.00 34.43  ? 298  ASP A C   1 
ATOM 2016 O O   . ASP A 1 434 ? 151.292 114.249 182.475 1.00 40.31  ? 298  ASP A O   1 
ATOM 2017 C CB  . ASP A 1 434 ? 148.838 115.545 180.777 1.00 28.78  ? 298  ASP A CB  1 
ATOM 2018 C CG  . ASP A 1 434 ? 148.342 116.868 180.259 1.00 31.56  ? 298  ASP A CG  1 
ATOM 2019 O OD1 . ASP A 1 434 ? 149.134 117.580 179.613 1.00 30.16  ? 298  ASP A OD1 1 
ATOM 2020 O OD2 . ASP A 1 434 ? 147.165 117.202 180.504 1.00 31.35  ? 298  ASP A OD2 1 
ATOM 2021 N N   . ASP A 1 435 ? 150.693 112.953 180.740 1.00 37.34  ? 299  ASP A N   1 
ATOM 2022 C CA  . ASP A 1 435 ? 151.220 111.750 181.384 1.00 38.85  ? 299  ASP A CA  1 
ATOM 2023 C C   . ASP A 1 435 ? 152.733 111.834 181.551 1.00 41.31  ? 299  ASP A C   1 
ATOM 2024 O O   . ASP A 1 435 ? 153.275 111.473 182.606 1.00 45.77  ? 299  ASP A O   1 
ATOM 2025 C CB  . ASP A 1 435 ? 150.843 110.510 180.578 1.00 44.83  ? 299  ASP A CB  1 
ATOM 2026 C CG  . ASP A 1 435 ? 149.349 110.291 180.513 1.00 52.48  ? 299  ASP A CG  1 
ATOM 2027 O OD1 . ASP A 1 435 ? 148.602 111.127 181.059 1.00 51.30  ? 299  ASP A OD1 1 
ATOM 2028 O OD2 . ASP A 1 435 ? 148.922 109.280 179.918 1.00 55.24  ? 299  ASP A OD2 1 
ATOM 2029 N N   . ALA A 1 436 ? 153.429 112.319 180.522 1.00 39.20  ? 300  ALA A N   1 
ATOM 2030 C CA  . ALA A 1 436 ? 154.874 112.494 180.623 1.00 40.11  ? 300  ALA A CA  1 
ATOM 2031 C C   . ALA A 1 436 ? 155.237 113.497 181.709 1.00 40.26  ? 300  ALA A C   1 
ATOM 2032 O O   . ALA A 1 436 ? 156.209 113.299 182.441 1.00 43.05  ? 300  ALA A O   1 
ATOM 2033 C CB  . ALA A 1 436 ? 155.442 112.936 179.278 1.00 41.24  ? 300  ALA A CB  1 
ATOM 2034 N N   . LEU A 1 437 ? 154.478 114.588 181.818 1.00 37.83  ? 301  LEU A N   1 
ATOM 2035 C CA  . LEU A 1 437 ? 154.747 115.589 182.847 1.00 32.97  ? 301  LEU A CA  1 
ATOM 2036 C C   . LEU A 1 437 ? 154.488 115.040 184.243 1.00 39.77  ? 301  LEU A C   1 
ATOM 2037 O O   . LEU A 1 437 ? 155.228 115.346 185.184 1.00 49.19  ? 301  LEU A O   1 
ATOM 2038 C CB  . LEU A 1 437 ? 153.906 116.836 182.596 1.00 27.03  ? 301  LEU A CB  1 
ATOM 2039 C CG  . LEU A 1 437 ? 154.575 117.927 181.769 1.00 29.93  ? 301  LEU A CG  1 
ATOM 2040 C CD1 . LEU A 1 437 ? 153.550 118.871 181.195 1.00 26.96  ? 301  LEU A CD1 1 
ATOM 2041 C CD2 . LEU A 1 437 ? 155.558 118.683 182.628 1.00 37.35  ? 301  LEU A CD2 1 
ATOM 2042 N N   . LYS A 1 438 ? 153.436 114.237 184.401 1.00 38.91  ? 302  LYS A N   1 
ATOM 2043 C CA  . LYS A 1 438 ? 153.182 113.592 185.684 1.00 40.38  ? 302  LYS A CA  1 
ATOM 2044 C C   . LYS A 1 438 ? 154.327 112.671 186.068 1.00 51.59  ? 302  LYS A C   1 
ATOM 2045 O O   . LYS A 1 438 ? 154.732 112.625 187.235 1.00 56.79  ? 302  LYS A O   1 
ATOM 2046 C CB  . LYS A 1 438 ? 151.871 112.811 185.630 1.00 38.22  ? 302  LYS A CB  1 
ATOM 2047 C CG  . LYS A 1 438 ? 150.630 113.673 185.571 1.00 45.29  ? 302  LYS A CG  1 
ATOM 2048 C CD  . LYS A 1 438 ? 149.433 112.872 185.107 1.00 50.56  ? 302  LYS A CD  1 
ATOM 2049 C CE  . LYS A 1 438 ? 149.270 111.603 185.920 1.00 55.48  ? 302  LYS A CE  1 
ATOM 2050 N NZ  . LYS A 1 438 ? 148.192 110.741 185.365 1.00 59.88  ? 302  LYS A NZ  1 
ATOM 2051 N N   . LEU A 1 439 ? 154.859 111.919 185.101 1.00 55.94  ? 303  LEU A N   1 
ATOM 2052 C CA  . LEU A 1 439 ? 155.974 111.025 185.404 1.00 60.43  ? 303  LEU A CA  1 
ATOM 2053 C C   . LEU A 1 439 ? 157.259 111.801 185.677 1.00 61.40  ? 303  LEU A C   1 
ATOM 2054 O O   . LEU A 1 439 ? 158.071 111.389 186.512 1.00 68.95  ? 303  LEU A O   1 
ATOM 2055 C CB  . LEU A 1 439 ? 156.174 110.033 184.261 1.00 58.74  ? 303  LEU A CB  1 
ATOM 2056 C CG  . LEU A 1 439 ? 154.982 109.104 184.040 1.00 59.27  ? 303  LEU A CG  1 
ATOM 2057 C CD1 . LEU A 1 439 ? 155.166 108.269 182.790 1.00 64.86  ? 303  LEU A CD1 1 
ATOM 2058 C CD2 . LEU A 1 439 ? 154.780 108.220 185.253 1.00 64.79  ? 303  LEU A CD2 1 
ATOM 2059 N N   . ALA A 1 440 ? 157.464 112.922 184.985 1.00 55.19  ? 304  ALA A N   1 
ATOM 2060 C CA  . ALA A 1 440 ? 158.696 113.683 185.153 1.00 55.77  ? 304  ALA A CA  1 
ATOM 2061 C C   . ALA A 1 440 ? 158.709 114.472 186.454 1.00 62.48  ? 304  ALA A C   1 
ATOM 2062 O O   . ALA A 1 440 ? 159.778 114.670 187.040 1.00 68.60  ? 304  ALA A O   1 
ATOM 2063 C CB  . ALA A 1 440 ? 158.899 114.625 183.968 1.00 54.19  ? 304  ALA A CB  1 
ATOM 2064 N N   . ASN A 1 441 ? 157.547 114.942 186.914 1.00 61.52  ? 305  ASN A N   1 
ATOM 2065 C CA  . ASN A 1 441 ? 157.503 115.680 188.174 1.00 64.00  ? 305  ASN A CA  1 
ATOM 2066 C C   . ASN A 1 441 ? 157.926 114.800 189.343 1.00 71.43  ? 305  ASN A C   1 
ATOM 2067 O O   . ASN A 1 441 ? 158.610 115.263 190.263 1.00 70.29  ? 305  ASN A O   1 
ATOM 2068 C CB  . ASN A 1 441 ? 156.103 116.246 188.409 1.00 60.61  ? 305  ASN A CB  1 
ATOM 2069 C CG  . ASN A 1 441 ? 155.803 117.439 187.530 1.00 60.67  ? 305  ASN A CG  1 
ATOM 2070 O OD1 . ASN A 1 441 ? 156.483 117.678 186.535 1.00 61.95  ? 305  ASN A OD1 1 
ATOM 2071 N ND2 . ASN A 1 441 ? 154.777 118.196 187.893 1.00 51.20  ? 305  ASN A ND2 1 
ATOM 2072 N N   . GLU A 1 442 ? 157.527 113.527 189.325 1.00 72.91  ? 306  GLU A N   1 
ATOM 2073 C CA  . GLU A 1 442 ? 157.902 112.611 190.395 1.00 74.57  ? 306  GLU A CA  1 
ATOM 2074 C C   . GLU A 1 442 ? 159.402 112.359 190.443 1.00 75.88  ? 306  GLU A C   1 
ATOM 2075 O O   . GLU A 1 442 ? 159.905 111.868 191.459 1.00 79.20  ? 306  GLU A O   1 
ATOM 2076 C CB  . GLU A 1 442 ? 157.161 111.284 190.232 1.00 72.14  ? 306  GLU A CB  1 
ATOM 2077 C CG  . GLU A 1 442 ? 155.652 111.418 190.190 1.00 72.62  ? 306  GLU A CG  1 
ATOM 2078 C CD  . GLU A 1 442 ? 154.955 110.084 190.024 1.00 82.79  ? 306  GLU A CD  1 
ATOM 2079 O OE1 . GLU A 1 442 ? 155.655 109.056 189.927 1.00 84.21  ? 306  GLU A OE1 1 
ATOM 2080 O OE2 . GLU A 1 442 ? 153.707 110.060 189.988 1.00 89.71  ? 306  GLU A OE2 1 
ATOM 2081 N N   . GLY A 1 443 ? 160.127 112.685 189.376 1.00 75.44  ? 307  GLY A N   1 
ATOM 2082 C CA  . GLY A 1 443 ? 161.545 112.416 189.292 1.00 79.29  ? 307  GLY A CA  1 
ATOM 2083 C C   . GLY A 1 443 ? 161.916 111.199 188.477 1.00 79.92  ? 307  GLY A C   1 
ATOM 2084 O O   . GLY A 1 443 ? 163.098 110.841 188.436 1.00 82.37  ? 307  GLY A O   1 
ATOM 2085 N N   . LYS A 1 444 ? 160.951 110.553 187.828 1.00 77.12  ? 308  LYS A N   1 
ATOM 2086 C CA  . LYS A 1 444 ? 161.206 109.363 187.021 1.00 76.56  ? 308  LYS A CA  1 
ATOM 2087 C C   . LYS A 1 444 ? 161.490 109.808 185.593 1.00 79.80  ? 308  LYS A C   1 
ATOM 2088 O O   . LYS A 1 444 ? 160.570 110.045 184.809 1.00 79.83  ? 308  LYS A O   1 
ATOM 2089 C CB  . LYS A 1 444 ? 160.019 108.411 187.085 1.00 79.53  ? 308  LYS A CB  1 
ATOM 2090 C CG  . LYS A 1 444 ? 159.545 108.126 188.496 1.00 79.73  ? 308  LYS A CG  1 
ATOM 2091 C CD  . LYS A 1 444 ? 158.440 107.091 188.511 1.00 81.78  ? 308  LYS A CD  1 
ATOM 2092 C CE  . LYS A 1 444 ? 157.997 106.797 189.931 1.00 83.29  ? 308  LYS A CE  1 
ATOM 2093 N NZ  . LYS A 1 444 ? 159.143 106.405 190.794 1.00 81.69  ? 308  LYS A NZ  1 
ATOM 2094 N N   . VAL A 1 445 ? 162.774 109.923 185.252 1.00 82.12  ? 309  VAL A N   1 
ATOM 2095 C CA  . VAL A 1 445 ? 163.148 110.407 183.928 1.00 84.15  ? 309  VAL A CA  1 
ATOM 2096 C C   . VAL A 1 445 ? 162.820 109.374 182.858 1.00 86.10  ? 309  VAL A C   1 
ATOM 2097 O O   . VAL A 1 445 ? 162.283 109.713 181.795 1.00 88.01  ? 309  VAL A O   1 
ATOM 2098 C CB  . VAL A 1 445 ? 164.638 110.786 183.906 1.00 85.40  ? 309  VAL A CB  1 
ATOM 2099 C CG1 . VAL A 1 445 ? 165.016 111.360 182.556 1.00 84.47  ? 309  VAL A CG1 1 
ATOM 2100 C CG2 . VAL A 1 445 ? 164.945 111.772 185.016 1.00 87.55  ? 309  VAL A CG2 1 
ATOM 2101 N N   . LYS A 1 446 ? 163.128 108.102 183.119 1.00 85.05  ? 310  LYS A N   1 
ATOM 2102 C CA  . LYS A 1 446 ? 162.986 107.075 182.092 1.00 83.12  ? 310  LYS A CA  1 
ATOM 2103 C C   . LYS A 1 446 ? 161.537 106.927 181.650 1.00 81.33  ? 310  LYS A C   1 
ATOM 2104 O O   . LYS A 1 446 ? 161.256 106.735 180.460 1.00 81.16  ? 310  LYS A O   1 
ATOM 2105 C CB  . LYS A 1 446 ? 163.531 105.744 182.607 1.00 87.67  ? 310  LYS A CB  1 
ATOM 2106 C CG  . LYS A 1 446 ? 164.956 105.821 183.126 1.00 93.17  ? 310  LYS A CG  1 
ATOM 2107 C CD  . LYS A 1 446 ? 165.904 106.343 182.059 1.00 94.54  ? 310  LYS A CD  1 
ATOM 2108 C CE  . LYS A 1 446 ? 167.331 106.428 182.578 1.00 93.71  ? 310  LYS A CE  1 
ATOM 2109 N NZ  . LYS A 1 446 ? 167.449 107.349 183.741 1.00 97.12  ? 310  LYS A NZ  1 
ATOM 2110 N N   . GLU A 1 447 ? 160.599 107.010 182.593 1.00 80.46  ? 311  GLU A N   1 
ATOM 2111 C CA  . GLU A 1 447 ? 159.192 106.946 182.222 1.00 80.66  ? 311  GLU A CA  1 
ATOM 2112 C C   . GLU A 1 447 ? 158.770 108.174 181.422 1.00 79.49  ? 311  GLU A C   1 
ATOM 2113 O O   . GLU A 1 447 ? 157.904 108.072 180.545 1.00 77.65  ? 311  GLU A O   1 
ATOM 2114 C CB  . GLU A 1 447 ? 158.332 106.779 183.472 1.00 80.65  ? 311  GLU A CB  1 
ATOM 2115 C CG  . GLU A 1 447 ? 158.739 105.595 184.333 1.00 83.45  ? 311  GLU A CG  1 
ATOM 2116 C CD  . GLU A 1 447 ? 157.626 105.127 185.247 1.00 86.11  ? 311  GLU A CD  1 
ATOM 2117 O OE1 . GLU A 1 447 ? 156.446 105.296 184.881 1.00 88.91  ? 311  GLU A OE1 1 
ATOM 2118 O OE2 . GLU A 1 447 ? 157.931 104.591 186.332 1.00 83.76  ? 311  GLU A OE2 1 
ATOM 2119 N N   . ALA A 1 448 ? 159.375 109.332 181.695 1.00 75.88  ? 312  ALA A N   1 
ATOM 2120 C CA  . ALA A 1 448 ? 159.131 110.502 180.858 1.00 68.29  ? 312  ALA A CA  1 
ATOM 2121 C C   . ALA A 1 448 ? 159.604 110.263 179.431 1.00 73.05  ? 312  ALA A C   1 
ATOM 2122 O O   . ALA A 1 448 ? 158.912 110.621 178.468 1.00 77.09  ? 312  ALA A O   1 
ATOM 2123 C CB  . ALA A 1 448 ? 159.819 111.729 181.451 1.00 63.98  ? 312  ALA A CB  1 
ATOM 2124 N N   . GLN A 1 449 ? 160.781 109.650 179.274 1.00 71.86  ? 313  GLN A N   1 
ATOM 2125 C CA  . GLN A 1 449 ? 161.260 109.313 177.936 1.00 72.94  ? 313  GLN A CA  1 
ATOM 2126 C C   . GLN A 1 449 ? 160.307 108.350 177.241 1.00 74.33  ? 313  GLN A C   1 
ATOM 2127 O O   . GLN A 1 449 ? 159.997 108.513 176.053 1.00 74.98  ? 313  GLN A O   1 
ATOM 2128 C CB  . GLN A 1 449 ? 162.658 108.699 178.011 1.00 77.86  ? 313  GLN A CB  1 
ATOM 2129 C CG  . GLN A 1 449 ? 163.586 109.314 179.043 1.00 79.74  ? 313  GLN A CG  1 
ATOM 2130 C CD  . GLN A 1 449 ? 164.161 110.643 178.613 1.00 82.79  ? 313  GLN A CD  1 
ATOM 2131 O OE1 . GLN A 1 449 ? 163.661 111.279 177.690 1.00 82.77  ? 313  GLN A OE1 1 
ATOM 2132 N NE2 . GLN A 1 449 ? 165.226 111.068 179.278 1.00 83.87  ? 313  GLN A NE2 1 
ATOM 2133 N N   . ALA A 1 450 ? 159.836 107.336 177.968 1.00 72.74  ? 314  ALA A N   1 
ATOM 2134 C CA  . ALA A 1 450 ? 158.917 106.368 177.380 1.00 71.92  ? 314  ALA A CA  1 
ATOM 2135 C C   . ALA A 1 450 ? 157.624 107.034 176.925 1.00 73.86  ? 314  ALA A C   1 
ATOM 2136 O O   . ALA A 1 450 ? 157.122 106.753 175.830 1.00 76.89  ? 314  ALA A O   1 
ATOM 2137 C CB  . ALA A 1 450 ? 158.624 105.252 178.381 1.00 73.76  ? 314  ALA A CB  1 
ATOM 2138 N N   . ALA A 1 451 ? 157.071 107.925 177.751 1.00 70.19  ? 315  ALA A N   1 
ATOM 2139 C CA  . ALA A 1 451 ? 155.844 108.619 177.373 1.00 67.91  ? 315  ALA A CA  1 
ATOM 2140 C C   . ALA A 1 451 ? 156.066 109.526 176.168 1.00 68.13  ? 315  ALA A C   1 
ATOM 2141 O O   . ALA A 1 451 ? 155.192 109.641 175.299 1.00 69.95  ? 315  ALA A O   1 
ATOM 2142 C CB  . ALA A 1 451 ? 155.305 109.413 178.558 1.00 65.01  ? 315  ALA A CB  1 
ATOM 2143 N N   . ALA A 1 452 ? 157.231 110.173 176.090 1.00 64.46  ? 316  ALA A N   1 
ATOM 2144 C CA  . ALA A 1 452 ? 157.544 110.974 174.911 1.00 62.97  ? 316  ALA A CA  1 
ATOM 2145 C C   . ALA A 1 452 ? 157.609 110.108 173.655 1.00 66.78  ? 316  ALA A C   1 
ATOM 2146 O O   . ALA A 1 452 ? 157.154 110.518 172.577 1.00 65.05  ? 316  ALA A O   1 
ATOM 2147 C CB  . ALA A 1 452 ? 158.858 111.718 175.128 1.00 65.68  ? 316  ALA A CB  1 
ATOM 2148 N N   . GLU A 1 453 ? 158.174 108.906 173.769 1.00 66.71  ? 317  GLU A N   1 
ATOM 2149 C CA  . GLU A 1 453 ? 158.196 108.005 172.619 1.00 68.00  ? 317  GLU A CA  1 
ATOM 2150 C C   . GLU A 1 453 ? 156.787 107.576 172.223 1.00 67.09  ? 317  GLU A C   1 
ATOM 2151 O O   . GLU A 1 453 ? 156.481 107.446 171.030 1.00 69.15  ? 317  GLU A O   1 
ATOM 2152 C CB  . GLU A 1 453 ? 159.070 106.789 172.917 1.00 74.70  ? 317  GLU A CB  1 
ATOM 2153 C CG  . GLU A 1 453 ? 160.496 107.141 173.295 1.00 77.59  ? 317  GLU A CG  1 
ATOM 2154 C CD  . GLU A 1 453 ? 161.114 108.155 172.356 1.00 80.73  ? 317  GLU A CD  1 
ATOM 2155 O OE1 . GLU A 1 453 ? 161.046 107.952 171.126 1.00 82.35  ? 317  GLU A OE1 1 
ATOM 2156 O OE2 . GLU A 1 453 ? 161.662 109.163 172.848 1.00 79.91  ? 317  GLU A OE2 1 
ATOM 2157 N N   . GLN A 1 454 ? 155.917 107.340 173.207 1.00 67.19  ? 318  GLN A N   1 
ATOM 2158 C CA  . GLN A 1 454 ? 154.527 107.025 172.882 1.00 65.34  ? 318  GLN A CA  1 
ATOM 2159 C C   . GLN A 1 454 ? 153.855 108.188 172.167 1.00 62.04  ? 318  GLN A C   1 
ATOM 2160 O O   . GLN A 1 454 ? 153.007 107.982 171.292 1.00 62.97  ? 318  GLN A O   1 
ATOM 2161 C CB  . GLN A 1 454 ? 153.741 106.660 174.142 1.00 68.55  ? 318  GLN A CB  1 
ATOM 2162 C CG  . GLN A 1 454 ? 154.392 105.611 175.034 1.00 78.28  ? 318  GLN A CG  1 
ATOM 2163 C CD  . GLN A 1 454 ? 155.237 104.609 174.269 1.00 82.79  ? 318  GLN A CD  1 
ATOM 2164 O OE1 . GLN A 1 454 ? 154.746 103.903 173.389 1.00 87.36  ? 318  GLN A OE1 1 
ATOM 2165 N NE2 . GLN A 1 454 ? 156.521 104.544 174.605 1.00 76.44  ? 318  GLN A NE2 1 
ATOM 2166 N N   . LEU A 1 455 ? 154.217 109.415 172.534 1.00 61.23  ? 319  LEU A N   1 
ATOM 2167 C CA  . LEU A 1 455 ? 153.734 110.588 171.809 1.00 56.60  ? 319  LEU A CA  1 
ATOM 2168 C C   . LEU A 1 455 ? 154.206 110.568 170.360 1.00 57.33  ? 319  LEU A C   1 
ATOM 2169 O O   . LEU A 1 455 ? 153.442 110.882 169.434 1.00 55.80  ? 319  LEU A O   1 
ATOM 2170 C CB  . LEU A 1 455 ? 154.229 111.842 172.524 1.00 56.30  ? 319  LEU A CB  1 
ATOM 2171 C CG  . LEU A 1 455 ? 153.637 113.229 172.336 1.00 48.98  ? 319  LEU A CG  1 
ATOM 2172 C CD1 . LEU A 1 455 ? 154.299 114.090 173.360 1.00 42.82  ? 319  LEU A CD1 1 
ATOM 2173 C CD2 . LEU A 1 455 ? 153.914 113.776 170.961 1.00 55.96  ? 319  LEU A CD2 1 
ATOM 2174 N N   . LYS A 1 456 ? 155.476 110.222 170.154 1.00 62.03  ? 320  LYS A N   1 
ATOM 2175 C CA  . LYS A 1 456 ? 156.000 110.083 168.798 1.00 62.07  ? 320  LYS A CA  1 
ATOM 2176 C C   . LYS A 1 456 ? 155.191 109.066 168.005 1.00 58.90  ? 320  LYS A C   1 
ATOM 2177 O O   . LYS A 1 456 ? 154.903 109.271 166.822 1.00 57.41  ? 320  LYS A O   1 
ATOM 2178 C CB  . LYS A 1 456 ? 157.473 109.678 168.854 1.00 66.14  ? 320  LYS A CB  1 
ATOM 2179 C CG  . LYS A 1 456 ? 158.159 109.562 167.514 1.00 63.43  ? 320  LYS A CG  1 
ATOM 2180 C CD  . LYS A 1 456 ? 159.598 109.120 167.692 1.00 72.45  ? 320  LYS A CD  1 
ATOM 2181 C CE  . LYS A 1 456 ? 160.345 110.047 168.637 1.00 77.47  ? 320  LYS A CE  1 
ATOM 2182 N NZ  . LYS A 1 456 ? 161.709 109.542 168.955 1.00 80.22  ? 320  LYS A NZ  1 
ATOM 2183 N N   . THR A 1 457 ? 154.819 107.959 168.648 1.00 61.90  ? 321  THR A N   1 
ATOM 2184 C CA  . THR A 1 457 ? 153.966 106.966 167.999 1.00 59.12  ? 321  THR A CA  1 
ATOM 2185 C C   . THR A 1 457 ? 152.594 107.541 167.658 1.00 56.79  ? 321  THR A C   1 
ATOM 2186 O O   . THR A 1 457 ? 152.064 107.297 166.570 1.00 58.43  ? 321  THR A O   1 
ATOM 2187 C CB  . THR A 1 457 ? 153.822 105.734 168.895 1.00 63.76  ? 321  THR A CB  1 
ATOM 2188 O OG1 . THR A 1 457 ? 154.997 104.921 168.786 1.00 65.26  ? 321  THR A OG1 1 
ATOM 2189 C CG2 . THR A 1 457 ? 152.605 104.915 168.505 1.00 62.97  ? 321  THR A CG2 1 
ATOM 2190 N N   . THR A 1 458 ? 152.003 108.306 168.579 1.00 59.70  ? 322  THR A N   1 
ATOM 2191 C CA  . THR A 1 458 ? 150.674 108.870 168.345 1.00 60.25  ? 322  THR A CA  1 
ATOM 2192 C C   . THR A 1 458 ? 150.673 109.874 167.197 1.00 54.97  ? 322  THR A C   1 
ATOM 2193 O O   . THR A 1 458 ? 149.643 110.053 166.538 1.00 53.46  ? 322  THR A O   1 
ATOM 2194 C CB  . THR A 1 458 ? 150.144 109.527 169.624 1.00 62.59  ? 322  THR A CB  1 
ATOM 2195 O OG1 . THR A 1 458 ? 149.958 108.527 170.632 1.00 64.30  ? 322  THR A OG1 1 
ATOM 2196 C CG2 . THR A 1 458 ? 148.816 110.236 169.383 1.00 54.39  ? 322  THR A CG2 1 
ATOM 2197 N N   . ARG A 1 459 ? 151.805 110.532 166.940 1.00 54.77  ? 323  ARG A N   1 
ATOM 2198 C CA  . ARG A 1 459 ? 151.854 111.486 165.831 1.00 52.32  ? 323  ARG A CA  1 
ATOM 2199 C C   . ARG A 1 459 ? 151.390 110.855 164.523 1.00 52.78  ? 323  ARG A C   1 
ATOM 2200 O O   . ARG A 1 459 ? 150.609 111.451 163.775 1.00 54.39  ? 323  ARG A O   1 
ATOM 2201 C CB  . ARG A 1 459 ? 153.263 112.043 165.649 1.00 55.70  ? 323  ARG A CB  1 
ATOM 2202 C CG  . ARG A 1 459 ? 153.410 112.828 164.349 1.00 50.60  ? 323  ARG A CG  1 
ATOM 2203 C CD  . ARG A 1 459 ? 154.857 113.119 164.000 1.00 50.28  ? 323  ARG A CD  1 
ATOM 2204 N NE  . ARG A 1 459 ? 155.515 111.960 163.413 1.00 54.44  ? 323  ARG A NE  1 
ATOM 2205 C CZ  . ARG A 1 459 ? 156.289 111.122 164.086 1.00 56.68  ? 323  ARG A CZ  1 
ATOM 2206 N NH1 . ARG A 1 459 ? 156.545 111.301 165.370 1.00 58.55  ? 323  ARG A NH1 1 
ATOM 2207 N NH2 . ARG A 1 459 ? 156.820 110.079 163.455 1.00 57.02  ? 323  ARG A NH2 1 
ATOM 2208 N N   . ASN A 1 460 ? 151.869 109.644 164.230 1.00 53.54  ? 324  ASN A N   1 
ATOM 2209 C CA  . ASN A 1 460 ? 151.558 109.006 162.953 1.00 55.42  ? 324  ASN A CA  1 
ATOM 2210 C C   . ASN A 1 460 ? 150.072 108.697 162.823 1.00 57.99  ? 324  ASN A C   1 
ATOM 2211 O O   . ASN A 1 460 ? 149.490 108.854 161.743 1.00 57.40  ? 324  ASN A O   1 
ATOM 2212 C CB  . ASN A 1 460 ? 152.374 107.726 162.797 1.00 54.38  ? 324  ASN A CB  1 
ATOM 2213 C CG  . ASN A 1 460 ? 153.852 107.954 162.991 1.00 57.76  ? 324  ASN A CG  1 
ATOM 2214 O OD1 . ASN A 1 460 ? 154.373 109.022 162.680 1.00 57.71  ? 324  ASN A OD1 1 
ATOM 2215 N ND2 . ASN A 1 460 ? 154.542 106.946 163.510 1.00 57.42  ? 324  ASN A ND2 1 
ATOM 2216 N N   . ALA A 1 461 ? 149.443 108.247 163.909 1.00 56.50  ? 325  ALA A N   1 
ATOM 2217 C CA  . ALA A 1 461 ? 148.074 107.749 163.823 1.00 51.70  ? 325  ALA A CA  1 
ATOM 2218 C C   . ALA A 1 461 ? 147.088 108.847 163.441 1.00 56.96  ? 325  ALA A C   1 
ATOM 2219 O O   . ALA A 1 461 ? 146.179 108.612 162.637 1.00 65.20  ? 325  ALA A O   1 
ATOM 2220 C CB  . ALA A 1 461 ? 147.671 107.104 165.146 1.00 50.84  ? 325  ALA A CB  1 
ATOM 2221 N N   . TYR A 1 462 ? 147.240 110.043 164.001 1.00 54.94  ? 326  TYR A N   1 
ATOM 2222 C CA  . TYR A 1 462 ? 146.238 111.091 163.829 1.00 55.98  ? 326  TYR A CA  1 
ATOM 2223 C C   . TYR A 1 462 ? 146.760 112.353 163.163 1.00 55.38  ? 326  TYR A C   1 
ATOM 2224 O O   . TYR A 1 462 ? 146.041 112.962 162.371 1.00 59.56  ? 326  TYR A O   1 
ATOM 2225 C CB  . TYR A 1 462 ? 145.633 111.475 165.184 1.00 57.76  ? 326  TYR A CB  1 
ATOM 2226 C CG  . TYR A 1 462 ? 144.821 110.394 165.851 1.00 59.27  ? 326  TYR A CG  1 
ATOM 2227 C CD1 . TYR A 1 462 ? 143.459 110.285 165.625 1.00 61.34  ? 326  TYR A CD1 1 
ATOM 2228 C CD2 . TYR A 1 462 ? 145.413 109.498 166.725 1.00 58.13  ? 326  TYR A CD2 1 
ATOM 2229 C CE1 . TYR A 1 462 ? 142.713 109.306 166.239 1.00 60.19  ? 326  TYR A CE1 1 
ATOM 2230 C CE2 . TYR A 1 462 ? 144.675 108.515 167.344 1.00 60.51  ? 326  TYR A CE2 1 
ATOM 2231 C CZ  . TYR A 1 462 ? 143.326 108.423 167.097 1.00 62.64  ? 326  TYR A CZ  1 
ATOM 2232 O OH  . TYR A 1 462 ? 142.588 107.442 167.714 1.00 65.81  ? 326  TYR A OH  1 
ATOM 2233 N N   . ILE A 1 463 ? 147.982 112.779 163.472 1.00 53.70  ? 327  ILE A N   1 
ATOM 2234 C CA  . ILE A 1 463 ? 148.436 114.106 163.074 1.00 53.27  ? 327  ILE A CA  1 
ATOM 2235 C C   . ILE A 1 463 ? 149.259 114.103 161.790 1.00 54.57  ? 327  ILE A C   1 
ATOM 2236 O O   . ILE A 1 463 ? 149.420 115.168 161.172 1.00 58.54  ? 327  ILE A O   1 
ATOM 2237 C CB  . ILE A 1 463 ? 149.246 114.769 164.210 1.00 57.06  ? 327  ILE A CB  1 
ATOM 2238 C CG1 . ILE A 1 463 ? 148.661 114.417 165.577 1.00 56.37  ? 327  ILE A CG1 1 
ATOM 2239 C CG2 . ILE A 1 463 ? 149.262 116.272 164.043 1.00 54.51  ? 327  ILE A CG2 1 
ATOM 2240 C CD1 . ILE A 1 463 ? 147.287 114.966 165.810 1.00 53.36  ? 327  ILE A CD1 1 
ATOM 2241 N N   . GLN A 1 464 ? 149.776 112.950 161.364 1.00 55.24  ? 328  GLN A N   1 
ATOM 2242 C CA  . GLN A 1 464 ? 150.706 112.940 160.240 1.00 55.23  ? 328  GLN A CA  1 
ATOM 2243 C C   . GLN A 1 464 ? 150.033 113.337 158.933 1.00 58.25  ? 328  GLN A C   1 
ATOM 2244 O O   . GLN A 1 464 ? 150.664 113.983 158.090 1.00 60.71  ? 328  GLN A O   1 
ATOM 2245 C CB  . GLN A 1 464 ? 151.357 111.567 160.105 1.00 55.37  ? 328  GLN A CB  1 
ATOM 2246 C CG  . GLN A 1 464 ? 152.486 111.529 159.095 1.00 60.04  ? 328  GLN A CG  1 
ATOM 2247 C CD  . GLN A 1 464 ? 153.538 112.591 159.353 1.00 57.54  ? 328  GLN A CD  1 
ATOM 2248 O OE1 . GLN A 1 464 ? 154.335 112.480 160.282 1.00 54.38  ? 328  GLN A OE1 1 
ATOM 2249 N NE2 . GLN A 1 464 ? 153.545 113.627 158.526 1.00 58.84  ? 328  GLN A NE2 1 
ATOM 2250 N N   . LYS A 1 465 ? 148.766 112.965 158.739 1.00 59.73  ? 329  LYS A N   1 
ATOM 2251 C CA  . LYS A 1 465 ? 148.081 113.339 157.505 1.00 60.77  ? 329  LYS A CA  1 
ATOM 2252 C C   . LYS A 1 465 ? 147.952 114.852 157.383 1.00 61.75  ? 329  LYS A C   1 
ATOM 2253 O O   . LYS A 1 465 ? 148.229 115.423 156.322 1.00 65.07  ? 329  LYS A O   1 
ATOM 2254 C CB  . LYS A 1 465 ? 146.711 112.662 157.433 1.00 60.40  ? 329  LYS A CB  1 
ATOM 2255 C CG  . LYS A 1 465 ? 145.795 112.956 158.597 1.00 61.04  ? 329  LYS A CG  1 
ATOM 2256 C CD  . LYS A 1 465 ? 144.618 112.005 158.632 1.00 66.05  ? 329  LYS A CD  1 
ATOM 2257 C CE  . LYS A 1 465 ? 145.062 110.612 159.030 1.00 70.73  ? 329  LYS A CE  1 
ATOM 2258 N NZ  . LYS A 1 465 ? 143.903 109.711 159.264 1.00 80.60  ? 329  LYS A NZ  1 
ATOM 2259 N N   . TYR A 1 466 ? 147.567 115.526 158.468 1.00 59.49  ? 330  TYR A N   1 
ATOM 2260 C CA  . TYR A 1 466 ? 147.453 116.978 158.421 1.00 55.30  ? 330  TYR A CA  1 
ATOM 2261 C C   . TYR A 1 466 ? 148.819 117.641 158.344 1.00 57.14  ? 330  TYR A C   1 
ATOM 2262 O O   . TYR A 1 466 ? 148.960 118.686 157.702 1.00 62.36  ? 330  TYR A O   1 
ATOM 2263 C CB  . TYR A 1 466 ? 146.668 117.479 159.629 1.00 54.68  ? 330  TYR A CB  1 
ATOM 2264 C CG  . TYR A 1 466 ? 145.307 116.844 159.742 1.00 61.47  ? 330  TYR A CG  1 
ATOM 2265 C CD1 . TYR A 1 466 ? 144.237 117.312 158.996 1.00 66.02  ? 330  TYR A CD1 1 
ATOM 2266 C CD2 . TYR A 1 466 ? 145.093 115.766 160.585 1.00 64.97  ? 330  TYR A CD2 1 
ATOM 2267 C CE1 . TYR A 1 466 ? 142.992 116.729 159.092 1.00 67.81  ? 330  TYR A CE1 1 
ATOM 2268 C CE2 . TYR A 1 466 ? 143.852 115.176 160.686 1.00 66.56  ? 330  TYR A CE2 1 
ATOM 2269 C CZ  . TYR A 1 466 ? 142.806 115.662 159.938 1.00 68.92  ? 330  TYR A CZ  1 
ATOM 2270 O OH  . TYR A 1 466 ? 141.569 115.076 160.039 1.00 75.65  ? 330  TYR A OH  1 
ATOM 2271 N N   . LEU A 1 467 ? 149.836 117.046 158.969 1.00 54.57  ? 331  LEU A N   1 
ATOM 2272 C CA  . LEU A 1 467 ? 151.187 117.579 158.843 1.00 54.26  ? 331  LEU A CA  1 
ATOM 2273 C C   . LEU A 1 467 ? 151.655 117.547 157.396 1.00 59.69  ? 331  LEU A C   1 
ATOM 2274 O O   . LEU A 1 467 ? 152.197 118.532 156.883 1.00 66.61  ? 331  LEU A O   1 
ATOM 2275 C CB  . LEU A 1 467 ? 152.151 116.792 159.728 1.00 53.56  ? 331  LEU A CB  1 
ATOM 2276 C CG  . LEU A 1 467 ? 152.091 117.038 161.230 1.00 52.16  ? 331  LEU A CG  1 
ATOM 2277 C CD1 . LEU A 1 467 ? 153.139 116.202 161.931 1.00 53.33  ? 331  LEU A CD1 1 
ATOM 2278 C CD2 . LEU A 1 467 ? 152.310 118.500 161.507 1.00 55.15  ? 331  LEU A CD2 1 
ATOM 2279 N N   . GLU A 1 468 ? 151.447 116.419 156.714 1.00 59.60  ? 332  GLU A N   1 
ATOM 2280 C CA  . GLU A 1 468 ? 151.892 116.324 155.328 1.00 61.15  ? 332  GLU A CA  1 
ATOM 2281 C C   . GLU A 1 468 ? 151.044 117.196 154.413 1.00 62.71  ? 332  GLU A C   1 
ATOM 2282 O O   . GLU A 1 468 ? 151.559 117.742 153.433 1.00 64.44  ? 332  GLU A O   1 
ATOM 2283 C CB  . GLU A 1 468 ? 151.887 114.867 154.862 1.00 63.35  ? 332  GLU A CB  1 
ATOM 2284 C CG  . GLU A 1 468 ? 150.519 114.284 154.572 1.00 68.17  ? 332  GLU A CG  1 
ATOM 2285 C CD  . GLU A 1 468 ? 150.561 112.788 154.351 1.00 74.93  ? 332  GLU A CD  1 
ATOM 2286 O OE1 . GLU A 1 468 ? 151.500 112.137 154.854 1.00 70.14  ? 332  GLU A OE1 1 
ATOM 2287 O OE2 . GLU A 1 468 ? 149.654 112.261 153.673 1.00 78.79  ? 332  GLU A OE2 1 
ATOM 2288 N N   . ARG A 1 469 ? 149.755 117.359 154.723 1.00 64.49  ? 333  ARG A N   1 
ATOM 2289 C CA  . ARG A 1 469 ? 148.918 118.273 153.952 1.00 61.98  ? 333  ARG A CA  1 
ATOM 2290 C C   . ARG A 1 469 ? 149.403 119.713 154.086 1.00 62.54  ? 333  ARG A C   1 
ATOM 2291 O O   . ARG A 1 469 ? 149.481 120.446 153.093 1.00 68.53  ? 333  ARG A O   1 
ATOM 2292 C CB  . ARG A 1 469 ? 147.469 118.141 154.410 1.00 60.26  ? 333  ARG A CB  1 
ATOM 2293 C CG  . ARG A 1 469 ? 146.460 118.853 153.550 1.00 60.96  ? 333  ARG A CG  1 
ATOM 2294 C CD  . ARG A 1 469 ? 145.062 118.582 154.070 1.00 69.27  ? 333  ARG A CD  1 
ATOM 2295 N NE  . ARG A 1 469 ? 144.807 117.153 154.207 1.00 74.42  ? 333  ARG A NE  1 
ATOM 2296 C CZ  . ARG A 1 469 ? 143.693 116.634 154.704 1.00 77.77  ? 333  ARG A CZ  1 
ATOM 2297 N NH1 . ARG A 1 469 ? 142.706 117.402 155.136 1.00 74.65  ? 333  ARG A NH1 1 
ATOM 2298 N NH2 . ARG A 1 469 ? 143.566 115.312 154.771 1.00 73.19  ? 333  ARG A NH2 1 
ATOM 2299 N N   . ALA A 1 470 ? 149.741 120.133 155.306 1.00 61.83  ? 334  ALA A N   1 
ATOM 2300 C CA  . ALA A 1 470 ? 150.273 121.476 155.506 1.00 62.30  ? 334  ALA A CA  1 
ATOM 2301 C C   . ALA A 1 470 ? 151.616 121.645 154.812 1.00 66.30  ? 334  ALA A C   1 
ATOM 2302 O O   . ALA A 1 470 ? 151.899 122.704 154.241 1.00 70.74  ? 334  ALA A O   1 
ATOM 2303 C CB  . ALA A 1 470 ? 150.402 121.774 156.998 1.00 58.34  ? 334  ALA A CB  1 
ATOM 2304 N N   . ARG A 1 471 ? 152.464 120.617 154.860 1.00 66.17  ? 335  ARG A N   1 
ATOM 2305 C CA  . ARG A 1 471 ? 153.749 120.690 154.173 1.00 67.69  ? 335  ARG A CA  1 
ATOM 2306 C C   . ARG A 1 471 ? 153.564 120.819 152.668 1.00 71.40  ? 335  ARG A C   1 
ATOM 2307 O O   . ARG A 1 471 ? 154.277 121.584 152.011 1.00 76.18  ? 335  ARG A O   1 
ATOM 2308 C CB  . ARG A 1 471 ? 154.592 119.461 154.506 1.00 69.77  ? 335  ARG A CB  1 
ATOM 2309 C CG  . ARG A 1 471 ? 155.880 119.343 153.708 1.00 76.38  ? 335  ARG A CG  1 
ATOM 2310 C CD  . ARG A 1 471 ? 156.961 120.283 154.217 1.00 80.38  ? 335  ARG A CD  1 
ATOM 2311 N NE  . ARG A 1 471 ? 156.812 121.640 153.707 1.00 83.14  ? 335  ARG A NE  1 
ATOM 2312 C CZ  . ARG A 1 471 ? 157.619 122.645 154.017 1.00 89.05  ? 335  ARG A CZ  1 
ATOM 2313 N NH1 . ARG A 1 471 ? 158.643 122.480 154.837 1.00 93.01  ? 335  ARG A NH1 1 
ATOM 2314 N NH2 . ARG A 1 471 ? 157.394 123.844 153.491 1.00 88.18  ? 335  ARG A NH2 1 
ATOM 2315 N N   . SER A 1 472 ? 152.612 120.074 152.101 1.00 69.52  ? 336  SER A N   1 
ATOM 2316 C CA  . SER A 1 472 ? 152.336 120.189 150.673 1.00 68.90  ? 336  SER A CA  1 
ATOM 2317 C C   . SER A 1 472 ? 151.814 121.575 150.322 1.00 69.48  ? 336  SER A C   1 
ATOM 2318 O O   . SER A 1 472 ? 152.208 122.152 149.304 1.00 74.38  ? 336  SER A O   1 
ATOM 2319 C CB  . SER A 1 472 ? 151.336 119.118 150.243 1.00 66.31  ? 336  SER A CB  1 
ATOM 2320 O OG  . SER A 1 472 ? 151.846 117.821 150.490 1.00 74.31  ? 336  SER A OG  1 
ATOM 2321 N N   . THR A 1 473 ? 150.927 122.125 151.154 1.00 67.44  ? 337  THR A N   1 
ATOM 2322 C CA  . THR A 1 473 ? 150.420 123.471 150.901 1.00 65.02  ? 337  THR A CA  1 
ATOM 2323 C C   . THR A 1 473 ? 151.538 124.504 150.959 1.00 65.66  ? 337  THR A C   1 
ATOM 2324 O O   . THR A 1 473 ? 151.584 125.427 150.139 1.00 69.61  ? 337  THR A O   1 
ATOM 2325 C CB  . THR A 1 473 ? 149.314 123.815 151.897 1.00 66.82  ? 337  THR A CB  1 
ATOM 2326 O OG1 . THR A 1 473 ? 148.169 122.994 151.638 1.00 65.40  ? 337  THR A OG1 1 
ATOM 2327 C CG2 . THR A 1 473 ? 148.918 125.271 151.772 1.00 66.06  ? 337  THR A CG2 1 
ATOM 2328 N N   . LEU A 1 474 ? 152.453 124.367 151.918 1.00 69.60  ? 338  LEU A N   1 
ATOM 2329 C CA  . LEU A 1 474 ? 153.588 125.279 151.987 1.00 74.34  ? 338  LEU A CA  1 
ATOM 2330 C C   . LEU A 1 474 ? 154.590 125.047 150.865 1.00 76.41  ? 338  LEU A C   1 
ATOM 2331 O O   . LEU A 1 474 ? 155.380 125.947 150.563 1.00 78.87  ? 338  LEU A O   1 
ATOM 2332 C CB  . LEU A 1 474 ? 154.298 125.150 153.334 1.00 74.72  ? 338  LEU A CB  1 
ATOM 2333 C CG  . LEU A 1 474 ? 153.561 125.651 154.571 1.00 70.33  ? 338  LEU A CG  1 
ATOM 2334 C CD1 . LEU A 1 474 ? 154.434 125.461 155.789 1.00 73.03  ? 338  LEU A CD1 1 
ATOM 2335 C CD2 . LEU A 1 474 ? 153.187 127.106 154.406 1.00 67.89  ? 338  LEU A CD2 1 
ATOM 2336 N N   . ASP A 1 475 ? 154.588 123.861 150.254 1.00 74.25  ? 339  ASP A N   1 
ATOM 2337 C CA  . ASP A 1 475 ? 155.517 123.593 149.161 1.00 76.49  ? 339  ASP A CA  1 
ATOM 2338 C C   . ASP A 1 475 ? 155.192 124.422 147.929 1.00 79.74  ? 339  ASP A C   1 
ATOM 2339 O O   . ASP A 1 475 ? 156.088 124.726 147.134 1.00 81.07  ? 339  ASP A O   1 
ATOM 2340 C CB  . ASP A 1 475 ? 155.507 122.106 148.810 1.00 79.64  ? 339  ASP A CB  1 
ATOM 2341 C CG  . ASP A 1 475 ? 156.674 121.357 149.415 1.00 87.48  ? 339  ASP A CG  1 
ATOM 2342 O OD1 . ASP A 1 475 ? 157.761 121.956 149.544 1.00 94.64  ? 339  ASP A OD1 1 
ATOM 2343 O OD2 . ASP A 1 475 ? 156.507 120.168 149.758 1.00 86.13  ? 339  ASP A OD2 1 
ATOM 2344 N N   . LYS A 1 476 ? 153.925 124.796 147.752 1.00 79.14  ? 340  LYS A N   1 
ATOM 2345 C CA  . LYS A 1 476 ? 153.511 125.538 146.570 1.00 79.99  ? 340  LYS A CA  1 
ATOM 2346 C C   . LYS A 1 476 ? 154.051 126.960 146.541 1.00 80.55  ? 340  LYS A C   1 
ATOM 2347 O O   . LYS A 1 476 ? 153.975 127.609 145.494 1.00 81.90  ? 340  LYS A O   1 
ATOM 2348 C CB  . LYS A 1 476 ? 151.987 125.547 146.482 1.00 70.86  ? 340  LYS A CB  1 
ATOM 2349 C CG  . LYS A 1 476 ? 151.385 124.157 146.489 1.00 64.85  ? 340  LYS A CG  1 
ATOM 2350 C CD  . LYS A 1 476 ? 149.879 124.206 146.379 1.00 67.53  ? 340  LYS A CD  1 
ATOM 2351 C CE  . LYS A 1 476 ? 149.267 122.836 146.601 1.00 66.99  ? 340  LYS A CE  1 
ATOM 2352 N NZ  . LYS A 1 476 ? 149.773 121.836 145.629 1.00 65.67  ? 340  LYS A NZ  1 
ATOM 2353 N N   . LEU A 1 477 ? 154.585 127.463 147.652 1.00 77.47  ? 341  LEU A N   1 
ATOM 2354 C CA  . LEU A 1 477 ? 155.206 128.782 147.631 1.00 80.13  ? 341  LEU A CA  1 
ATOM 2355 C C   . LEU A 1 477 ? 156.566 128.750 146.949 1.00 85.09  ? 341  LEU A C   1 
ATOM 2356 O O   . LEU A 1 477 ? 156.888 129.647 146.163 1.00 85.81  ? 341  LEU A O   1 
ATOM 2357 C CB  . LEU A 1 477 ? 155.336 129.327 149.050 1.00 81.21  ? 341  LEU A CB  1 
ATOM 2358 C CG  . LEU A 1 477 ? 154.225 130.271 149.496 1.00 75.30  ? 341  LEU A CG  1 
ATOM 2359 C CD1 . LEU A 1 477 ? 152.905 129.823 148.912 1.00 74.50  ? 341  LEU A CD1 1 
ATOM 2360 C CD2 . LEU A 1 477 ? 154.163 130.310 151.010 1.00 73.98  ? 341  LEU A CD2 1 
ATOM 2361 N N   . ASN A 1 478 ? 157.375 127.729 147.231 1.00 88.27  ? 1235 ASN A N   1 
ATOM 2362 C CA  . ASN A 1 478 ? 158.655 127.595 146.550 1.00 92.64  ? 1235 ASN A CA  1 
ATOM 2363 C C   . ASN A 1 478 ? 158.492 127.221 145.086 1.00 92.15  ? 1235 ASN A C   1 
ATOM 2364 O O   . ASN A 1 478 ? 159.481 127.236 144.347 1.00 93.23  ? 1235 ASN A O   1 
ATOM 2365 C CB  . ASN A 1 478 ? 159.530 126.561 147.259 1.00 92.04  ? 1235 ASN A CB  1 
ATOM 2366 C CG  . ASN A 1 478 ? 160.092 127.077 148.568 1.00 95.28  ? 1235 ASN A CG  1 
ATOM 2367 O OD1 . ASN A 1 478 ? 159.539 127.993 149.176 1.00 92.97  ? 1235 ASN A OD1 1 
ATOM 2368 N ND2 . ASN A 1 478 ? 161.201 126.494 149.007 1.00 100.53 ? 1235 ASN A ND2 1 
ATOM 2369 N N   . ASP A 1 479 ? 157.279 126.876 144.662 1.00 89.86  ? 1236 ASP A N   1 
ATOM 2370 C CA  . ASP A 1 479 ? 157.006 126.653 143.252 1.00 90.38  ? 1236 ASP A CA  1 
ATOM 2371 C C   . ASP A 1 479 ? 157.316 127.917 142.464 1.00 91.34  ? 1236 ASP A C   1 
ATOM 2372 O O   . ASP A 1 479 ? 156.930 129.020 142.859 1.00 91.57  ? 1236 ASP A O   1 
ATOM 2373 C CB  . ASP A 1 479 ? 155.545 126.252 143.062 1.00 85.19  ? 1236 ASP A CB  1 
ATOM 2374 C CG  . ASP A 1 479 ? 155.288 125.596 141.728 1.00 87.06  ? 1236 ASP A CG  1 
ATOM 2375 O OD1 . ASP A 1 479 ? 156.143 125.716 140.826 1.00 88.02  ? 1236 ASP A OD1 1 
ATOM 2376 O OD2 . ASP A 1 479 ? 154.224 124.960 141.581 1.00 87.75  ? 1236 ASP A OD2 1 
ATOM 2377 N N   . ASP A 1 480 ? 158.030 127.756 141.349 1.00 90.95  ? 1237 ASP A N   1 
ATOM 2378 C CA  . ASP A 1 480 ? 158.408 128.916 140.552 1.00 90.22  ? 1237 ASP A CA  1 
ATOM 2379 C C   . ASP A 1 480 ? 157.205 129.548 139.868 1.00 85.82  ? 1237 ASP A C   1 
ATOM 2380 O O   . ASP A 1 480 ? 157.173 130.769 139.684 1.00 83.25  ? 1237 ASP A O   1 
ATOM 2381 C CB  . ASP A 1 480 ? 159.464 128.524 139.520 1.00 93.46  ? 1237 ASP A CB  1 
ATOM 2382 C CG  . ASP A 1 480 ? 160.839 128.352 140.133 1.00 97.73  ? 1237 ASP A CG  1 
ATOM 2383 O OD1 . ASP A 1 480 ? 161.093 128.950 141.199 1.00 96.59  ? 1237 ASP A OD1 1 
ATOM 2384 O OD2 . ASP A 1 480 ? 161.669 127.624 139.548 1.00 100.58 ? 1237 ASP A OD2 1 
ATOM 2385 N N   . ILE A 1 481 ? 156.212 128.743 139.487 1.00 83.03  ? 1238 ILE A N   1 
ATOM 2386 C CA  . ILE A 1 481 ? 155.067 129.284 138.762 1.00 78.87  ? 1238 ILE A CA  1 
ATOM 2387 C C   . ILE A 1 481 ? 154.227 130.189 139.655 1.00 74.84  ? 1238 ILE A C   1 
ATOM 2388 O O   . ILE A 1 481 ? 153.676 131.189 139.184 1.00 75.03  ? 1238 ILE A O   1 
ATOM 2389 C CB  . ILE A 1 481 ? 154.238 128.143 138.144 1.00 77.97  ? 1238 ILE A CB  1 
ATOM 2390 C CG1 . ILE A 1 481 ? 153.259 128.696 137.114 1.00 73.24  ? 1238 ILE A CG1 1 
ATOM 2391 C CG2 . ILE A 1 481 ? 153.498 127.359 139.210 1.00 82.46  ? 1238 ILE A CG2 1 
ATOM 2392 C CD1 . ILE A 1 481 ? 152.683 127.634 136.218 1.00 75.09  ? 1238 ILE A CD1 1 
ATOM 2393 N N   . PHE A 1 482 ? 154.115 129.873 140.947 1.00 75.37  ? 1239 PHE A N   1 
ATOM 2394 C CA  . PHE A 1 482 ? 153.395 130.760 141.854 1.00 72.94  ? 1239 PHE A CA  1 
ATOM 2395 C C   . PHE A 1 482 ? 154.079 132.116 141.949 1.00 72.03  ? 1239 PHE A C   1 
ATOM 2396 O O   . PHE A 1 482 ? 153.418 133.161 141.902 1.00 74.19  ? 1239 PHE A O   1 
ATOM 2397 C CB  . PHE A 1 482 ? 153.279 130.120 143.237 1.00 75.18  ? 1239 PHE A CB  1 
ATOM 2398 C CG  . PHE A 1 482 ? 152.583 130.985 144.250 1.00 73.39  ? 1239 PHE A CG  1 
ATOM 2399 C CD1 . PHE A 1 482 ? 151.205 130.997 144.336 1.00 72.58  ? 1239 PHE A CD1 1 
ATOM 2400 C CD2 . PHE A 1 482 ? 153.308 131.778 145.120 1.00 74.80  ? 1239 PHE A CD2 1 
ATOM 2401 C CE1 . PHE A 1 482 ? 150.563 131.787 145.266 1.00 68.77  ? 1239 PHE A CE1 1 
ATOM 2402 C CE2 . PHE A 1 482 ? 152.669 132.570 146.051 1.00 74.64  ? 1239 PHE A CE2 1 
ATOM 2403 C CZ  . PHE A 1 482 ? 151.295 132.573 146.123 1.00 67.89  ? 1239 PHE A CZ  1 
ATOM 2404 N N   . LYS A 1 483 ? 155.407 132.119 142.081 1.00 72.61  ? 1240 LYS A N   1 
ATOM 2405 C CA  . LYS A 1 483 ? 156.144 133.376 142.132 1.00 74.77  ? 1240 LYS A CA  1 
ATOM 2406 C C   . LYS A 1 483 ? 156.003 134.146 140.828 1.00 75.21  ? 1240 LYS A C   1 
ATOM 2407 O O   . LYS A 1 483 ? 155.849 135.372 140.837 1.00 73.52  ? 1240 LYS A O   1 
ATOM 2408 C CB  . LYS A 1 483 ? 157.617 133.112 142.438 1.00 79.55  ? 1240 LYS A CB  1 
ATOM 2409 C CG  . LYS A 1 483 ? 157.863 132.339 143.719 1.00 85.19  ? 1240 LYS A CG  1 
ATOM 2410 C CD  . LYS A 1 483 ? 159.341 132.031 143.887 1.00 91.35  ? 1240 LYS A CD  1 
ATOM 2411 C CE  . LYS A 1 483 ? 159.601 131.222 145.144 1.00 92.52  ? 1240 LYS A CE  1 
ATOM 2412 N NZ  . LYS A 1 483 ? 161.043 130.879 145.289 1.00 96.67  ? 1240 LYS A NZ  1 
ATOM 2413 N N   . ILE A 1 484 ? 156.055 133.442 139.695 1.00 73.81  ? 1241 ILE A N   1 
ATOM 2414 C CA  . ILE A 1 484 ? 155.905 134.097 138.398 1.00 68.13  ? 1241 ILE A CA  1 
ATOM 2415 C C   . ILE A 1 484 ? 154.546 134.769 138.299 1.00 65.35  ? 1241 ILE A C   1 
ATOM 2416 O O   . ILE A 1 484 ? 154.437 135.933 137.899 1.00 67.62  ? 1241 ILE A O   1 
ATOM 2417 C CB  . ILE A 1 484 ? 156.109 133.084 137.258 1.00 70.52  ? 1241 ILE A CB  1 
ATOM 2418 C CG1 . ILE A 1 484 ? 157.586 132.729 137.110 1.00 79.45  ? 1241 ILE A CG1 1 
ATOM 2419 C CG2 . ILE A 1 484 ? 155.562 133.630 135.961 1.00 69.93  ? 1241 ILE A CG2 1 
ATOM 2420 C CD1 . ILE A 1 484 ? 157.849 131.692 136.050 1.00 80.81  ? 1241 ILE A CD1 1 
ATOM 2421 N N   . ILE A 1 485 ? 153.488 134.048 138.673 1.00 64.70  ? 1242 ILE A N   1 
ATOM 2422 C CA  . ILE A 1 485 ? 152.141 134.597 138.570 1.00 59.47  ? 1242 ILE A CA  1 
ATOM 2423 C C   . ILE A 1 485 ? 151.973 135.788 139.501 1.00 62.18  ? 1242 ILE A C   1 
ATOM 2424 O O   . ILE A 1 485 ? 151.394 136.812 139.119 1.00 65.56  ? 1242 ILE A O   1 
ATOM 2425 C CB  . ILE A 1 485 ? 151.098 133.504 138.854 1.00 61.12  ? 1242 ILE A CB  1 
ATOM 2426 C CG1 . ILE A 1 485 ? 151.137 132.448 137.752 1.00 63.67  ? 1242 ILE A CG1 1 
ATOM 2427 C CG2 . ILE A 1 485 ? 149.718 134.110 138.966 1.00 57.62  ? 1242 ILE A CG2 1 
ATOM 2428 C CD1 . ILE A 1 485 ? 150.331 131.223 138.059 1.00 66.10  ? 1242 ILE A CD1 1 
ATOM 2429 N N   . MET A 1 486 ? 152.470 135.681 140.736 1.00 63.65  ? 1243 MET A N   1 
ATOM 2430 C CA  . MET A 1 486 ? 152.325 136.790 141.673 1.00 64.49  ? 1243 MET A CA  1 
ATOM 2431 C C   . MET A 1 486 ? 153.094 138.018 141.203 1.00 65.98  ? 1243 MET A C   1 
ATOM 2432 O O   . MET A 1 486 ? 152.587 139.143 141.290 1.00 67.11  ? 1243 MET A O   1 
ATOM 2433 C CB  . MET A 1 486 ? 152.782 136.372 143.068 1.00 67.06  ? 1243 MET A CB  1 
ATOM 2434 C CG  . MET A 1 486 ? 152.393 137.361 144.151 1.00 70.83  ? 1243 MET A CG  1 
ATOM 2435 S SD  . MET A 1 486 ? 152.819 136.811 145.812 1.00 104.67 ? 1243 MET A SD  1 
ATOM 2436 C CE  . MET A 1 486 ? 154.607 136.815 145.726 1.00 94.97  ? 1243 MET A CE  1 
ATOM 2437 N N   . ALA A 1 487 ? 154.316 137.826 140.702 1.00 62.57  ? 1244 ALA A N   1 
ATOM 2438 C CA  . ALA A 1 487 ? 155.093 138.951 140.197 1.00 62.40  ? 1244 ALA A CA  1 
ATOM 2439 C C   . ALA A 1 487 ? 154.416 139.592 138.996 1.00 62.63  ? 1244 ALA A C   1 
ATOM 2440 O O   . ALA A 1 487 ? 154.363 140.821 138.890 1.00 65.61  ? 1244 ALA A O   1 
ATOM 2441 C CB  . ALA A 1 487 ? 156.504 138.497 139.834 1.00 65.90  ? 1244 ALA A CB  1 
ATOM 2442 N N   . ILE A 1 488 ? 153.886 138.777 138.082 1.00 62.13  ? 1245 ILE A N   1 
ATOM 2443 C CA  . ILE A 1 488 ? 153.200 139.319 136.915 1.00 57.36  ? 1245 ILE A CA  1 
ATOM 2444 C C   . ILE A 1 488 ? 151.980 140.122 137.338 1.00 56.99  ? 1245 ILE A C   1 
ATOM 2445 O O   . ILE A 1 488 ? 151.750 141.226 136.838 1.00 62.68  ? 1245 ILE A O   1 
ATOM 2446 C CB  . ILE A 1 488 ? 152.824 138.189 135.941 1.00 54.27  ? 1245 ILE A CB  1 
ATOM 2447 C CG1 . ILE A 1 488 ? 154.067 137.662 135.233 1.00 60.72  ? 1245 ILE A CG1 1 
ATOM 2448 C CG2 . ILE A 1 488 ? 151.823 138.678 134.926 1.00 50.84  ? 1245 ILE A CG2 1 
ATOM 2449 C CD1 . ILE A 1 488 ? 153.781 136.540 134.275 1.00 61.81  ? 1245 ILE A CD1 1 
ATOM 2450 N N   . VAL A 1 489 ? 151.187 139.595 138.272 1.00 55.75  ? 1246 VAL A N   1 
ATOM 2451 C CA  . VAL A 1 489 ? 149.986 140.303 138.711 1.00 55.25  ? 1246 VAL A CA  1 
ATOM 2452 C C   . VAL A 1 489 ? 150.355 141.627 139.370 1.00 60.01  ? 1246 VAL A C   1 
ATOM 2453 O O   . VAL A 1 489 ? 149.791 142.683 139.047 1.00 64.91  ? 1246 VAL A O   1 
ATOM 2454 C CB  . VAL A 1 489 ? 149.155 139.419 139.656 1.00 52.48  ? 1246 VAL A CB  1 
ATOM 2455 C CG1 . VAL A 1 489 ? 148.051 140.228 140.288 1.00 52.53  ? 1246 VAL A CG1 1 
ATOM 2456 C CG2 . VAL A 1 489 ? 148.572 138.241 138.905 1.00 53.37  ? 1246 VAL A CG2 1 
ATOM 2457 N N   . LEU A 1 490 ? 151.315 141.593 140.299 1.00 59.74  ? 1247 LEU A N   1 
ATOM 2458 C CA  . LEU A 1 490 ? 151.702 142.809 141.008 1.00 62.76  ? 1247 LEU A CA  1 
ATOM 2459 C C   . LEU A 1 490 ? 152.261 143.851 140.053 1.00 66.54  ? 1247 LEU A C   1 
ATOM 2460 O O   . LEU A 1 490 ? 151.896 145.030 140.120 1.00 70.28  ? 1247 LEU A O   1 
ATOM 2461 C CB  . LEU A 1 490 ? 152.727 142.485 142.093 1.00 62.64  ? 1247 LEU A CB  1 
ATOM 2462 C CG  . LEU A 1 490 ? 152.209 142.033 143.455 1.00 69.14  ? 1247 LEU A CG  1 
ATOM 2463 C CD1 . LEU A 1 490 ? 153.374 141.817 144.405 1.00 68.05  ? 1247 LEU A CD1 1 
ATOM 2464 C CD2 . LEU A 1 490 ? 151.237 143.054 144.020 1.00 69.11  ? 1247 LEU A CD2 1 
ATOM 2465 N N   . PHE A 1 491 ? 153.149 143.436 139.150 1.00 63.84  ? 1248 PHE A N   1 
ATOM 2466 C CA  . PHE A 1 491 ? 153.757 144.391 138.237 1.00 62.91  ? 1248 PHE A CA  1 
ATOM 2467 C C   . PHE A 1 491 ? 152.743 144.928 137.239 1.00 66.07  ? 1248 PHE A C   1 
ATOM 2468 O O   . PHE A 1 491 ? 152.791 146.107 136.880 1.00 71.19  ? 1248 PHE A O   1 
ATOM 2469 C CB  . PHE A 1 491 ? 154.934 143.748 137.517 1.00 64.42  ? 1248 PHE A CB  1 
ATOM 2470 C CG  . PHE A 1 491 ? 155.588 144.649 136.530 1.00 73.52  ? 1248 PHE A CG  1 
ATOM 2471 C CD1 . PHE A 1 491 ? 156.104 145.869 136.928 1.00 76.66  ? 1248 PHE A CD1 1 
ATOM 2472 C CD2 . PHE A 1 491 ? 155.686 144.287 135.203 1.00 78.96  ? 1248 PHE A CD2 1 
ATOM 2473 C CE1 . PHE A 1 491 ? 156.707 146.710 136.019 1.00 78.92  ? 1248 PHE A CE1 1 
ATOM 2474 C CE2 . PHE A 1 491 ? 156.280 145.128 134.293 1.00 82.69  ? 1248 PHE A CE2 1 
ATOM 2475 C CZ  . PHE A 1 491 ? 156.799 146.337 134.700 1.00 82.92  ? 1248 PHE A CZ  1 
ATOM 2476 N N   . PHE A 1 492 ? 151.817 144.083 136.782 1.00 64.01  ? 1249 PHE A N   1 
ATOM 2477 C CA  . PHE A 1 492 ? 150.769 144.540 135.880 1.00 59.83  ? 1249 PHE A CA  1 
ATOM 2478 C C   . PHE A 1 492 ? 149.922 145.615 136.538 1.00 61.11  ? 1249 PHE A C   1 
ATOM 2479 O O   . PHE A 1 492 ? 149.650 146.661 135.940 1.00 65.87  ? 1249 PHE A O   1 
ATOM 2480 C CB  . PHE A 1 492 ? 149.906 143.351 135.459 1.00 56.19  ? 1249 PHE A CB  1 
ATOM 2481 C CG  . PHE A 1 492 ? 148.753 143.715 134.573 1.00 56.28  ? 1249 PHE A CG  1 
ATOM 2482 C CD1 . PHE A 1 492 ? 147.532 144.073 135.112 1.00 58.01  ? 1249 PHE A CD1 1 
ATOM 2483 C CD2 . PHE A 1 492 ? 148.883 143.679 133.200 1.00 60.21  ? 1249 PHE A CD2 1 
ATOM 2484 C CE1 . PHE A 1 492 ? 146.476 144.406 134.302 1.00 54.84  ? 1249 PHE A CE1 1 
ATOM 2485 C CE2 . PHE A 1 492 ? 147.825 144.009 132.386 1.00 57.50  ? 1249 PHE A CE2 1 
ATOM 2486 C CZ  . PHE A 1 492 ? 146.623 144.372 132.937 1.00 54.78  ? 1249 PHE A CZ  1 
ATOM 2487 N N   . PHE A 1 493 ? 149.505 145.384 137.783 1.00 60.98  ? 1250 PHE A N   1 
ATOM 2488 C CA  . PHE A 1 493 ? 148.665 146.381 138.435 1.00 65.09  ? 1250 PHE A CA  1 
ATOM 2489 C C   . PHE A 1 493 ? 149.446 147.640 138.789 1.00 69.88  ? 1250 PHE A C   1 
ATOM 2490 O O   . PHE A 1 493 ? 148.900 148.744 138.694 1.00 72.06  ? 1250 PHE A O   1 
ATOM 2491 C CB  . PHE A 1 493 ? 147.982 145.777 139.658 1.00 64.80  ? 1250 PHE A CB  1 
ATOM 2492 C CG  . PHE A 1 493 ? 146.746 145.001 139.315 1.00 67.97  ? 1250 PHE A CG  1 
ATOM 2493 C CD1 . PHE A 1 493 ? 146.826 143.674 138.944 1.00 64.81  ? 1250 PHE A CD1 1 
ATOM 2494 C CD2 . PHE A 1 493 ? 145.508 145.612 139.322 1.00 70.15  ? 1250 PHE A CD2 1 
ATOM 2495 C CE1 . PHE A 1 493 ? 145.693 142.968 138.608 1.00 61.81  ? 1250 PHE A CE1 1 
ATOM 2496 C CE2 . PHE A 1 493 ? 144.371 144.908 138.989 1.00 68.63  ? 1250 PHE A CE2 1 
ATOM 2497 C CZ  . PHE A 1 493 ? 144.465 143.586 138.631 1.00 62.51  ? 1250 PHE A CZ  1 
ATOM 2498 N N   . PHE A 1 494 ? 150.721 147.513 139.163 1.00 70.37  ? 1251 PHE A N   1 
ATOM 2499 C CA  . PHE A 1 494 ? 151.532 148.706 139.395 1.00 69.57  ? 1251 PHE A CA  1 
ATOM 2500 C C   . PHE A 1 494 ? 151.701 149.516 138.116 1.00 69.56  ? 1251 PHE A C   1 
ATOM 2501 O O   . PHE A 1 494 ? 151.655 150.751 138.145 1.00 74.94  ? 1251 PHE A O   1 
ATOM 2502 C CB  . PHE A 1 494 ? 152.897 148.325 139.967 1.00 69.70  ? 1251 PHE A CB  1 
ATOM 2503 C CG  . PHE A 1 494 ? 152.889 148.088 141.449 1.00 76.61  ? 1251 PHE A CG  1 
ATOM 2504 C CD1 . PHE A 1 494 ? 154.048 147.718 142.109 1.00 79.34  ? 1251 PHE A CD1 1 
ATOM 2505 C CD2 . PHE A 1 494 ? 151.724 148.232 142.182 1.00 80.25  ? 1251 PHE A CD2 1 
ATOM 2506 C CE1 . PHE A 1 494 ? 154.047 147.499 143.474 1.00 80.84  ? 1251 PHE A CE1 1 
ATOM 2507 C CE2 . PHE A 1 494 ? 151.715 148.012 143.547 1.00 80.29  ? 1251 PHE A CE2 1 
ATOM 2508 C CZ  . PHE A 1 494 ? 152.878 147.647 144.193 1.00 79.91  ? 1251 PHE A CZ  1 
ATOM 2509 N N   . SER A 1 495 ? 151.905 148.842 136.983 1.00 66.29  ? 1252 SER A N   1 
ATOM 2510 C CA  . SER A 1 495 ? 152.055 149.547 135.718 1.00 66.27  ? 1252 SER A CA  1 
ATOM 2511 C C   . SER A 1 495 ? 150.754 150.198 135.277 1.00 71.32  ? 1252 SER A C   1 
ATOM 2512 O O   . SER A 1 495 ? 150.778 151.275 134.673 1.00 77.16  ? 1252 SER A O   1 
ATOM 2513 C CB  . SER A 1 495 ? 152.550 148.590 134.638 1.00 70.43  ? 1252 SER A CB  1 
ATOM 2514 O OG  . SER A 1 495 ? 153.742 147.945 135.041 1.00 76.72  ? 1252 SER A OG  1 
ATOM 2515 N N   . TRP A 1 496 ? 149.619 149.564 135.554 1.00 69.66  ? 1253 TRP A N   1 
ATOM 2516 C CA  . TRP A 1 496 ? 148.344 150.073 135.071 1.00 67.38  ? 1253 TRP A CA  1 
ATOM 2517 C C   . TRP A 1 496 ? 147.666 151.053 136.018 1.00 73.33  ? 1253 TRP A C   1 
ATOM 2518 O O   . TRP A 1 496 ? 146.720 151.725 135.600 1.00 78.28  ? 1253 TRP A O   1 
ATOM 2519 C CB  . TRP A 1 496 ? 147.396 148.913 134.782 1.00 63.89  ? 1253 TRP A CB  1 
ATOM 2520 C CG  . TRP A 1 496 ? 147.530 148.388 133.402 1.00 64.68  ? 1253 TRP A CG  1 
ATOM 2521 C CD1 . TRP A 1 496 ? 148.313 147.355 132.988 1.00 65.29  ? 1253 TRP A CD1 1 
ATOM 2522 C CD2 . TRP A 1 496 ? 146.862 148.876 132.242 1.00 64.97  ? 1253 TRP A CD2 1 
ATOM 2523 N NE1 . TRP A 1 496 ? 148.169 147.165 131.638 1.00 57.38  ? 1253 TRP A NE1 1 
ATOM 2524 C CE2 . TRP A 1 496 ? 147.282 148.090 131.157 1.00 61.58  ? 1253 TRP A CE2 1 
ATOM 2525 C CE3 . TRP A 1 496 ? 145.945 149.903 132.015 1.00 68.31  ? 1253 TRP A CE3 1 
ATOM 2526 C CZ2 . TRP A 1 496 ? 146.818 148.298 129.868 1.00 64.28  ? 1253 TRP A CZ2 1 
ATOM 2527 C CZ3 . TRP A 1 496 ? 145.487 150.108 130.738 1.00 67.73  ? 1253 TRP A CZ3 1 
ATOM 2528 C CH2 . TRP A 1 496 ? 145.921 149.311 129.681 1.00 64.82  ? 1253 TRP A CH2 1 
ATOM 2529 N N   . ILE A 1 497 ? 148.107 151.154 137.274 1.00 74.11  ? 1254 ILE A N   1 
ATOM 2530 C CA  . ILE A 1 497 ? 147.490 152.113 138.194 1.00 75.80  ? 1254 ILE A CA  1 
ATOM 2531 C C   . ILE A 1 497 ? 147.572 153.546 137.678 1.00 80.61  ? 1254 ILE A C   1 
ATOM 2532 O O   . ILE A 1 497 ? 146.540 154.238 137.684 1.00 84.10  ? 1254 ILE A O   1 
ATOM 2533 C CB  . ILE A 1 497 ? 148.085 151.953 139.604 1.00 74.12  ? 1254 ILE A CB  1 
ATOM 2534 C CG1 . ILE A 1 497 ? 147.367 150.836 140.358 1.00 73.61  ? 1254 ILE A CG1 1 
ATOM 2535 C CG2 . ILE A 1 497 ? 147.984 153.254 140.379 1.00 75.83  ? 1254 ILE A CG2 1 
ATOM 2536 C CD1 . ILE A 1 497 ? 147.926 150.572 141.733 1.00 75.49  ? 1254 ILE A CD1 1 
ATOM 2537 N N   . PRO A 1 498 ? 148.730 154.055 137.229 1.00 79.46  ? 1255 PRO A N   1 
ATOM 2538 C CA  . PRO A 1 498 ? 148.748 155.442 136.727 1.00 85.18  ? 1255 PRO A CA  1 
ATOM 2539 C C   . PRO A 1 498 ? 147.784 155.680 135.579 1.00 84.98  ? 1255 PRO A C   1 
ATOM 2540 O O   . PRO A 1 498 ? 147.069 156.691 135.569 1.00 87.61  ? 1255 PRO A O   1 
ATOM 2541 C CB  . PRO A 1 498 ? 150.209 155.634 136.297 1.00 84.01  ? 1255 PRO A CB  1 
ATOM 2542 C CG  . PRO A 1 498 ? 150.970 154.665 137.105 1.00 77.76  ? 1255 PRO A CG  1 
ATOM 2543 C CD  . PRO A 1 498 ? 150.084 153.471 137.230 1.00 74.94  ? 1255 PRO A CD  1 
ATOM 2544 N N   . HIS A 1 499 ? 147.727 154.761 134.616 1.00 82.34  ? 1256 HIS A N   1 
ATOM 2545 C CA  . HIS A 1 499 ? 146.839 154.959 133.479 1.00 83.34  ? 1256 HIS A CA  1 
ATOM 2546 C C   . HIS A 1 499 ? 145.379 154.922 133.905 1.00 82.71  ? 1256 HIS A C   1 
ATOM 2547 O O   . HIS A 1 499 ? 144.567 155.710 133.412 1.00 87.50  ? 1256 HIS A O   1 
ATOM 2548 C CB  . HIS A 1 499 ? 147.110 153.913 132.404 1.00 81.58  ? 1256 HIS A CB  1 
ATOM 2549 C CG  . HIS A 1 499 ? 146.306 154.112 131.159 1.00 83.26  ? 1256 HIS A CG  1 
ATOM 2550 N ND1 . HIS A 1 499 ? 145.197 153.352 130.860 1.00 85.39  ? 1256 HIS A ND1 1 
ATOM 2551 C CD2 . HIS A 1 499 ? 146.444 154.993 130.141 1.00 86.80  ? 1256 HIS A CD2 1 
ATOM 2552 C CE1 . HIS A 1 499 ? 144.690 153.751 129.707 1.00 88.90  ? 1256 HIS A CE1 1 
ATOM 2553 N NE2 . HIS A 1 499 ? 145.427 154.747 129.251 1.00 89.56  ? 1256 HIS A NE2 1 
ATOM 2554 N N   . GLN A 1 500 ? 145.022 154.016 134.817 1.00 80.03  ? 1257 GLN A N   1 
ATOM 2555 C CA  . GLN A 1 500 ? 143.636 153.945 135.269 1.00 81.23  ? 1257 GLN A CA  1 
ATOM 2556 C C   . GLN A 1 500 ? 143.231 155.203 136.027 1.00 87.94  ? 1257 GLN A C   1 
ATOM 2557 O O   . GLN A 1 500 ? 142.140 155.744 135.802 1.00 90.96  ? 1257 GLN A O   1 
ATOM 2558 C CB  . GLN A 1 500 ? 143.424 152.707 136.137 1.00 77.54  ? 1257 GLN A CB  1 
ATOM 2559 C CG  . GLN A 1 500 ? 143.649 151.388 135.418 1.00 77.70  ? 1257 GLN A CG  1 
ATOM 2560 C CD  . GLN A 1 500 ? 142.657 151.139 134.303 1.00 77.85  ? 1257 GLN A CD  1 
ATOM 2561 O OE1 . GLN A 1 500 ? 141.574 151.719 134.277 1.00 78.81  ? 1257 GLN A OE1 1 
ATOM 2562 N NE2 . GLN A 1 500 ? 143.022 150.267 133.375 1.00 70.50  ? 1257 GLN A NE2 1 
ATOM 2563 N N   . ILE A 1 501 ? 144.091 155.692 136.925 1.00 88.23  ? 1258 ILE A N   1 
ATOM 2564 C CA  . ILE A 1 501 ? 143.717 156.884 137.682 1.00 88.93  ? 1258 ILE A CA  1 
ATOM 2565 C C   . ILE A 1 501 ? 143.685 158.113 136.781 1.00 90.78  ? 1258 ILE A C   1 
ATOM 2566 O O   . ILE A 1 501 ? 142.856 159.009 136.976 1.00 94.94  ? 1258 ILE A O   1 
ATOM 2567 C CB  . ILE A 1 501 ? 144.639 157.086 138.900 1.00 88.33  ? 1258 ILE A CB  1 
ATOM 2568 C CG1 . ILE A 1 501 ? 146.100 157.225 138.477 1.00 88.11  ? 1258 ILE A CG1 1 
ATOM 2569 C CG2 . ILE A 1 501 ? 144.467 155.942 139.889 1.00 86.76  ? 1258 ILE A CG2 1 
ATOM 2570 C CD1 . ILE A 1 501 ? 147.074 157.253 139.639 1.00 84.99  ? 1258 ILE A CD1 1 
ATOM 2571 N N   . PHE A 1 502 ? 144.556 158.179 135.770 1.00 89.52  ? 1259 PHE A N   1 
ATOM 2572 C CA  . PHE A 1 502 ? 144.483 159.307 134.847 1.00 93.21  ? 1259 PHE A CA  1 
ATOM 2573 C C   . PHE A 1 502 ? 143.266 159.218 133.937 1.00 93.19  ? 1259 PHE A C   1 
ATOM 2574 O O   . PHE A 1 502 ? 142.693 160.249 133.578 1.00 95.64  ? 1259 PHE A O   1 
ATOM 2575 C CB  . PHE A 1 502 ? 145.766 159.412 134.030 1.00 93.09  ? 1259 PHE A CB  1 
ATOM 2576 C CG  . PHE A 1 502 ? 146.830 160.220 134.701 1.00 96.55  ? 1259 PHE A CG  1 
ATOM 2577 C CD1 . PHE A 1 502 ? 146.970 160.190 136.076 1.00 97.07  ? 1259 PHE A CD1 1 
ATOM 2578 C CD2 . PHE A 1 502 ? 147.667 161.036 133.966 1.00 104.14 ? 1259 PHE A CD2 1 
ATOM 2579 C CE1 . PHE A 1 502 ? 147.939 160.940 136.703 1.00 104.50 ? 1259 PHE A CE1 1 
ATOM 2580 C CE2 . PHE A 1 502 ? 148.638 161.790 134.589 1.00 109.99 ? 1259 PHE A CE2 1 
ATOM 2581 C CZ  . PHE A 1 502 ? 148.776 161.742 135.959 1.00 109.71 ? 1259 PHE A CZ  1 
ATOM 2582 N N   . THR A 1 503 ? 142.848 158.008 133.563 1.00 91.17  ? 1260 THR A N   1 
ATOM 2583 C CA  . THR A 1 503 ? 141.588 157.862 132.844 1.00 91.11  ? 1260 THR A CA  1 
ATOM 2584 C C   . THR A 1 503 ? 140.422 158.324 133.705 1.00 92.99  ? 1260 THR A C   1 
ATOM 2585 O O   . THR A 1 503 ? 139.481 158.952 133.206 1.00 99.53  ? 1260 THR A O   1 
ATOM 2586 C CB  . THR A 1 503 ? 141.391 156.410 132.409 1.00 89.85  ? 1260 THR A CB  1 
ATOM 2587 O OG1 . THR A 1 503 ? 142.495 155.998 131.596 1.00 91.88  ? 1260 THR A OG1 1 
ATOM 2588 C CG2 . THR A 1 503 ? 140.106 156.260 131.613 1.00 84.53  ? 1260 THR A CG2 1 
ATOM 2589 N N   . PHE A 1 504 ? 140.466 158.020 135.003 1.00 89.60  ? 1261 PHE A N   1 
ATOM 2590 C CA  . PHE A 1 504 ? 139.421 158.498 135.903 1.00 93.46  ? 1261 PHE A CA  1 
ATOM 2591 C C   . PHE A 1 504 ? 139.427 160.021 136.002 1.00 99.58  ? 1261 PHE A C   1 
ATOM 2592 O O   . PHE A 1 504 ? 138.365 160.653 135.999 1.00 101.22 ? 1261 PHE A O   1 
ATOM 2593 C CB  . PHE A 1 504 ? 139.584 157.866 137.282 1.00 92.87  ? 1261 PHE A CB  1 
ATOM 2594 C CG  . PHE A 1 504 ? 138.390 158.044 138.169 1.00 95.35  ? 1261 PHE A CG  1 
ATOM 2595 C CD1 . PHE A 1 504 ? 137.172 157.476 137.831 1.00 95.10  ? 1261 PHE A CD1 1 
ATOM 2596 C CD2 . PHE A 1 504 ? 138.483 158.770 139.343 1.00 97.83  ? 1261 PHE A CD2 1 
ATOM 2597 C CE1 . PHE A 1 504 ? 136.068 157.634 138.642 1.00 97.59  ? 1261 PHE A CE1 1 
ATOM 2598 C CE2 . PHE A 1 504 ? 137.381 158.931 140.161 1.00 103.09 ? 1261 PHE A CE2 1 
ATOM 2599 C CZ  . PHE A 1 504 ? 136.172 158.361 139.809 1.00 102.09 ? 1261 PHE A CZ  1 
ATOM 2600 N N   . LEU A 1 505 ? 140.612 160.629 136.081 1.00 99.06  ? 1262 LEU A N   1 
ATOM 2601 C CA  . LEU A 1 505 ? 140.686 162.089 136.101 1.00 99.36  ? 1262 LEU A CA  1 
ATOM 2602 C C   . LEU A 1 505 ? 140.148 162.687 134.807 1.00 101.99 ? 1262 LEU A C   1 
ATOM 2603 O O   . LEU A 1 505 ? 139.426 163.692 134.828 1.00 105.19 ? 1262 LEU A O   1 
ATOM 2604 C CB  . LEU A 1 505 ? 142.123 162.545 136.342 1.00 97.61  ? 1262 LEU A CB  1 
ATOM 2605 C CG  . LEU A 1 505 ? 142.643 162.375 137.769 1.00 101.15 ? 1262 LEU A CG  1 
ATOM 2606 C CD1 . LEU A 1 505 ? 144.048 162.938 137.902 1.00 102.80 ? 1262 LEU A CD1 1 
ATOM 2607 C CD2 . LEU A 1 505 ? 141.700 163.038 138.758 1.00 98.35  ? 1262 LEU A CD2 1 
ATOM 2608 N N   . ASP A 1 506 ? 140.485 162.082 133.669 1.00 101.44 ? 1263 ASP A N   1 
ATOM 2609 C CA  . ASP A 1 506 ? 140.024 162.603 132.389 1.00 102.83 ? 1263 ASP A CA  1 
ATOM 2610 C C   . ASP A 1 506 ? 138.514 162.467 132.245 1.00 103.41 ? 1263 ASP A C   1 
ATOM 2611 O O   . ASP A 1 506 ? 137.856 163.367 131.714 1.00 108.01 ? 1263 ASP A O   1 
ATOM 2612 C CB  . ASP A 1 506 ? 140.744 161.892 131.246 1.00 103.92 ? 1263 ASP A CB  1 
ATOM 2613 C CG  . ASP A 1 506 ? 140.752 162.704 129.970 1.00 111.80 ? 1263 ASP A CG  1 
ATOM 2614 O OD1 . ASP A 1 506 ? 139.671 163.159 129.544 1.00 114.43 ? 1263 ASP A OD1 1 
ATOM 2615 O OD2 . ASP A 1 506 ? 141.843 162.898 129.397 1.00 115.95 ? 1263 ASP A OD2 1 
ATOM 2616 N N   . VAL A 1 507 ? 137.941 161.351 132.704 1.00 100.89 ? 1264 VAL A N   1 
ATOM 2617 C CA  . VAL A 1 507 ? 136.491 161.209 132.621 1.00 101.98 ? 1264 VAL A CA  1 
ATOM 2618 C C   . VAL A 1 507 ? 135.804 162.147 133.606 1.00 104.92 ? 1264 VAL A C   1 
ATOM 2619 O O   . VAL A 1 507 ? 134.690 162.616 133.346 1.00 106.29 ? 1264 VAL A O   1 
ATOM 2620 C CB  . VAL A 1 507 ? 136.058 159.743 132.824 1.00 99.25  ? 1264 VAL A CB  1 
ATOM 2621 C CG1 . VAL A 1 507 ? 136.238 159.303 134.260 1.00 96.80  ? 1264 VAL A CG1 1 
ATOM 2622 C CG2 . VAL A 1 507 ? 134.613 159.556 132.393 1.00 94.73  ? 1264 VAL A CG2 1 
ATOM 2623 N N   . LEU A 1 508 ? 136.444 162.449 134.740 1.00 105.49 ? 1265 LEU A N   1 
ATOM 2624 C CA  . LEU A 1 508 ? 135.902 163.466 135.635 1.00 107.70 ? 1265 LEU A CA  1 
ATOM 2625 C C   . LEU A 1 508 ? 135.901 164.836 134.972 1.00 108.67 ? 1265 LEU A C   1 
ATOM 2626 O O   . LEU A 1 508 ? 134.942 165.604 135.113 1.00 111.32 ? 1265 LEU A O   1 
ATOM 2627 C CB  . LEU A 1 508 ? 136.696 163.508 136.940 1.00 104.47 ? 1265 LEU A CB  1 
ATOM 2628 C CG  . LEU A 1 508 ? 136.413 162.402 137.957 1.00 102.89 ? 1265 LEU A CG  1 
ATOM 2629 C CD1 . LEU A 1 508 ? 137.103 162.710 139.274 1.00 102.70 ? 1265 LEU A CD1 1 
ATOM 2630 C CD2 . LEU A 1 508 ? 134.915 162.221 138.160 1.00 103.01 ? 1265 LEU A CD2 1 
ATOM 2631 N N   . ILE A 1 509 ? 136.974 165.165 134.252 1.00 105.23 ? 1266 ILE A N   1 
ATOM 2632 C CA  . ILE A 1 509 ? 137.027 166.439 133.542 1.00 107.23 ? 1266 ILE A CA  1 
ATOM 2633 C C   . ILE A 1 509 ? 135.962 166.494 132.453 1.00 110.16 ? 1266 ILE A C   1 
ATOM 2634 O O   . ILE A 1 509 ? 135.257 167.499 132.305 1.00 113.01 ? 1266 ILE A O   1 
ATOM 2635 C CB  . ILE A 1 509 ? 138.437 166.676 132.970 1.00 105.76 ? 1266 ILE A CB  1 
ATOM 2636 C CG1 . ILE A 1 509 ? 139.366 167.223 134.054 1.00 106.99 ? 1266 ILE A CG1 1 
ATOM 2637 C CG2 . ILE A 1 509 ? 138.386 167.621 131.784 1.00 104.94 ? 1266 ILE A CG2 1 
ATOM 2638 C CD1 . ILE A 1 509 ? 140.728 167.630 133.536 1.00 108.97 ? 1266 ILE A CD1 1 
ATOM 2639 N N   . GLN A 1 510 ? 135.823 165.416 131.678 1.00 110.27 ? 1267 GLN A N   1 
ATOM 2640 C CA  . GLN A 1 510 ? 134.836 165.399 130.602 1.00 111.39 ? 1267 GLN A CA  1 
ATOM 2641 C C   . GLN A 1 510 ? 133.416 165.484 131.148 1.00 112.77 ? 1267 GLN A C   1 
ATOM 2642 O O   . GLN A 1 510 ? 132.558 166.156 130.564 1.00 116.44 ? 1267 GLN A O   1 
ATOM 2643 C CB  . GLN A 1 510 ? 135.005 164.143 129.748 1.00 109.05 ? 1267 GLN A CB  1 
ATOM 2644 C CG  . GLN A 1 510 ? 136.315 164.080 128.987 1.00 111.26 ? 1267 GLN A CG  1 
ATOM 2645 C CD  . GLN A 1 510 ? 136.402 162.870 128.078 1.00 112.25 ? 1267 GLN A CD  1 
ATOM 2646 O OE1 . GLN A 1 510 ? 137.491 162.400 127.754 1.00 114.99 ? 1267 GLN A OE1 1 
ATOM 2647 N NE2 . GLN A 1 510 ? 135.250 162.363 127.657 1.00 108.27 ? 1267 GLN A NE2 1 
ATOM 2648 N N   . LEU A 1 511 ? 133.145 164.810 132.267 1.00 110.45 ? 1268 LEU A N   1 
ATOM 2649 C CA  . LEU A 1 511 ? 131.805 164.818 132.835 1.00 112.45 ? 1268 LEU A CA  1 
ATOM 2650 C C   . LEU A 1 511 ? 131.468 166.133 133.524 1.00 115.00 ? 1268 LEU A C   1 
ATOM 2651 O O   . LEU A 1 511 ? 130.320 166.316 133.944 1.00 115.76 ? 1268 LEU A O   1 
ATOM 2652 C CB  . LEU A 1 511 ? 131.645 163.653 133.813 1.00 111.56 ? 1268 LEU A CB  1 
ATOM 2653 C CG  . LEU A 1 511 ? 130.231 163.079 133.949 1.00 111.51 ? 1268 LEU A CG  1 
ATOM 2654 C CD1 . LEU A 1 511 ? 129.689 162.669 132.590 1.00 106.68 ? 1268 LEU A CD1 1 
ATOM 2655 C CD2 . LEU A 1 511 ? 130.211 161.900 134.909 1.00 109.21 ? 1268 LEU A CD2 1 
ATOM 2656 N N   . GLY A 1 512 ? 132.430 167.045 133.652 1.00 113.66 ? 1269 GLY A N   1 
ATOM 2657 C CA  . GLY A 1 512 ? 132.180 168.354 134.215 1.00 114.38 ? 1269 GLY A CA  1 
ATOM 2658 C C   . GLY A 1 512 ? 132.380 168.474 135.709 1.00 113.27 ? 1269 GLY A C   1 
ATOM 2659 O O   . GLY A 1 512 ? 132.219 169.577 136.249 1.00 113.88 ? 1269 GLY A O   1 
ATOM 2660 N N   . ILE A 1 513 ? 132.714 167.383 136.399 1.00 110.58 ? 1270 ILE A N   1 
ATOM 2661 C CA  . ILE A 1 513 ? 132.936 167.461 137.840 1.00 111.13 ? 1270 ILE A CA  1 
ATOM 2662 C C   . ILE A 1 513 ? 134.145 168.336 138.144 1.00 111.99 ? 1270 ILE A C   1 
ATOM 2663 O O   . ILE A 1 513 ? 134.117 169.159 139.067 1.00 114.34 ? 1270 ILE A O   1 
ATOM 2664 C CB  . ILE A 1 513 ? 133.080 166.049 138.441 1.00 112.10 ? 1270 ILE A CB  1 
ATOM 2665 C CG1 . ILE A 1 513 ? 131.733 165.548 138.972 1.00 110.51 ? 1270 ILE A CG1 1 
ATOM 2666 C CG2 . ILE A 1 513 ? 134.103 166.035 139.561 1.00 112.43 ? 1270 ILE A CG2 1 
ATOM 2667 C CD1 . ILE A 1 513 ? 130.667 165.374 137.915 1.00 111.16 ? 1270 ILE A CD1 1 
ATOM 2668 N N   . ILE A 1 514 ? 135.215 168.186 137.371 1.00 111.44 ? 1271 ILE A N   1 
ATOM 2669 C CA  . ILE A 1 514 ? 136.416 168.987 137.577 1.00 113.05 ? 1271 ILE A CA  1 
ATOM 2670 C C   . ILE A 1 514 ? 136.592 169.994 136.446 1.00 110.02 ? 1271 ILE A C   1 
ATOM 2671 O O   . ILE A 1 514 ? 135.618 170.433 135.835 1.00 107.41 ? 1271 ILE A O   1 
ATOM 2672 C CB  . ILE A 1 514 ? 137.661 168.097 137.707 1.00 109.39 ? 1271 ILE A CB  1 
ATOM 2673 C CG1 . ILE A 1 514 ? 137.518 167.155 138.903 1.00 109.42 ? 1271 ILE A CG1 1 
ATOM 2674 C CG2 . ILE A 1 514 ? 138.910 168.948 137.835 1.00 105.38 ? 1271 ILE A CG2 1 
ATOM 2675 C CD1 . ILE A 1 514 ? 137.261 167.862 140.212 1.00 106.97 ? 1271 ILE A CD1 1 
ATOM 2676 N N   . ALA A 1 520 ? 144.429 170.151 135.440 1.00 124.13 ? 1277 ALA A N   1 
ATOM 2677 C CA  . ALA A 1 520 ? 143.850 169.683 134.186 1.00 127.52 ? 1277 ALA A CA  1 
ATOM 2678 C C   . ALA A 1 520 ? 144.929 169.482 133.129 1.00 130.23 ? 1277 ALA A C   1 
ATOM 2679 O O   . ALA A 1 520 ? 144.906 168.505 132.382 1.00 130.66 ? 1277 ALA A O   1 
ATOM 2680 C CB  . ALA A 1 520 ? 142.797 170.661 133.691 1.00 126.07 ? 1277 ALA A CB  1 
ATOM 2681 N N   . ASP A 1 521 ? 145.873 170.422 133.066 1.00 131.94 ? 1278 ASP A N   1 
ATOM 2682 C CA  . ASP A 1 521 ? 146.973 170.299 132.116 1.00 132.64 ? 1278 ASP A CA  1 
ATOM 2683 C C   . ASP A 1 521 ? 147.858 169.105 132.449 1.00 129.87 ? 1278 ASP A C   1 
ATOM 2684 O O   . ASP A 1 521 ? 148.363 168.429 131.545 1.00 127.72 ? 1278 ASP A O   1 
ATOM 2685 C CB  . ASP A 1 521 ? 147.794 171.588 132.093 1.00 135.96 ? 1278 ASP A CB  1 
ATOM 2686 C CG  . ASP A 1 521 ? 146.979 172.789 131.655 1.00 138.28 ? 1278 ASP A CG  1 
ATOM 2687 O OD1 . ASP A 1 521 ? 145.773 172.622 131.376 1.00 133.58 ? 1278 ASP A OD1 1 
ATOM 2688 O OD2 . ASP A 1 521 ? 147.546 173.900 131.589 1.00 139.59 ? 1278 ASP A OD2 1 
ATOM 2689 N N   . ILE A 1 522 ? 148.060 168.834 133.741 1.00 130.15 ? 1279 ILE A N   1 
ATOM 2690 C CA  . ILE A 1 522 ? 148.888 167.703 134.152 1.00 131.54 ? 1279 ILE A CA  1 
ATOM 2691 C C   . ILE A 1 522 ? 148.253 166.387 133.727 1.00 128.30 ? 1279 ILE A C   1 
ATOM 2692 O O   . ILE A 1 522 ? 148.959 165.429 133.389 1.00 126.25 ? 1279 ILE A O   1 
ATOM 2693 C CB  . ILE A 1 522 ? 149.136 167.748 135.672 1.00 131.66 ? 1279 ILE A CB  1 
ATOM 2694 C CG1 . ILE A 1 522 ? 149.651 169.128 136.083 1.00 130.46 ? 1279 ILE A CG1 1 
ATOM 2695 C CG2 . ILE A 1 522 ? 150.129 166.670 136.085 1.00 127.58 ? 1279 ILE A CG2 1 
ATOM 2696 C CD1 . ILE A 1 522 ? 150.925 169.537 135.379 1.00 130.08 ? 1279 ILE A CD1 1 
ATOM 2697 N N   . VAL A 1 523 ? 146.920 166.313 133.741 1.00 126.51 ? 1280 VAL A N   1 
ATOM 2698 C CA  . VAL A 1 523 ? 146.234 165.102 133.298 1.00 125.34 ? 1280 VAL A CA  1 
ATOM 2699 C C   . VAL A 1 523 ? 146.571 164.807 131.843 1.00 125.00 ? 1280 VAL A C   1 
ATOM 2700 O O   . VAL A 1 523 ? 146.875 163.667 131.474 1.00 124.22 ? 1280 VAL A O   1 
ATOM 2701 C CB  . VAL A 1 523 ? 144.715 165.238 133.507 1.00 123.44 ? 1280 VAL A CB  1 
ATOM 2702 C CG1 . VAL A 1 523 ? 143.995 164.025 132.951 1.00 115.73 ? 1280 VAL A CG1 1 
ATOM 2703 C CG2 . VAL A 1 523 ? 144.396 165.422 134.978 1.00 121.61 ? 1280 VAL A CG2 1 
ATOM 2704 N N   . ASP A 1 524 ? 146.525 165.834 130.996 1.00 126.20 ? 1281 ASP A N   1 
ATOM 2705 C CA  . ASP A 1 524 ? 146.864 165.658 129.589 1.00 127.48 ? 1281 ASP A CA  1 
ATOM 2706 C C   . ASP A 1 524 ? 148.367 165.568 129.367 1.00 123.65 ? 1281 ASP A C   1 
ATOM 2707 O O   . ASP A 1 524 ? 148.807 164.935 128.401 1.00 119.68 ? 1281 ASP A O   1 
ATOM 2708 C CB  . ASP A 1 524 ? 146.280 166.804 128.766 1.00 130.10 ? 1281 ASP A CB  1 
ATOM 2709 C CG  . ASP A 1 524 ? 144.790 166.970 128.979 1.00 128.98 ? 1281 ASP A CG  1 
ATOM 2710 O OD1 . ASP A 1 524 ? 144.166 166.049 129.549 1.00 126.57 ? 1281 ASP A OD1 1 
ATOM 2711 O OD2 . ASP A 1 524 ? 144.245 168.023 128.586 1.00 128.39 ? 1281 ASP A OD2 1 
ATOM 2712 N N   . THR A 1 525 ? 149.163 166.193 130.236 1.00 123.99 ? 1282 THR A N   1 
ATOM 2713 C CA  . THR A 1 525 ? 150.609 166.213 130.038 1.00 125.29 ? 1282 THR A CA  1 
ATOM 2714 C C   . THR A 1 525 ? 151.199 164.810 130.115 1.00 122.69 ? 1282 THR A C   1 
ATOM 2715 O O   . THR A 1 525 ? 152.022 164.422 129.278 1.00 120.81 ? 1282 THR A O   1 
ATOM 2716 C CB  . THR A 1 525 ? 151.268 167.124 131.075 1.00 129.31 ? 1282 THR A CB  1 
ATOM 2717 O OG1 . THR A 1 525 ? 150.680 168.429 131.011 1.00 131.03 ? 1282 THR A OG1 1 
ATOM 2718 C CG2 . THR A 1 525 ? 152.762 167.232 130.813 1.00 127.58 ? 1282 THR A CG2 1 
ATOM 2719 N N   . ALA A 1 526 ? 150.782 164.030 131.110 1.00 121.38 ? 1283 ALA A N   1 
ATOM 2720 C CA  . ALA A 1 526 ? 151.342 162.709 131.353 1.00 116.78 ? 1283 ALA A CA  1 
ATOM 2721 C C   . ALA A 1 526 ? 150.484 161.586 130.785 1.00 111.57 ? 1283 ALA A C   1 
ATOM 2722 O O   . ALA A 1 526 ? 150.771 160.414 131.046 1.00 108.81 ? 1283 ALA A O   1 
ATOM 2723 C CB  . ALA A 1 526 ? 151.557 162.496 132.852 1.00 113.29 ? 1283 ALA A CB  1 
ATOM 2724 N N   . MET A 1 527 ? 149.440 161.912 130.024 1.00 111.67 ? 1284 MET A N   1 
ATOM 2725 C CA  . MET A 1 527 ? 148.633 160.869 129.393 1.00 108.51 ? 1284 MET A CA  1 
ATOM 2726 C C   . MET A 1 527 ? 149.450 159.977 128.464 1.00 105.68 ? 1284 MET A C   1 
ATOM 2727 O O   . MET A 1 527 ? 149.325 158.743 128.565 1.00 104.27 ? 1284 MET A O   1 
ATOM 2728 C CB  . MET A 1 527 ? 147.446 161.508 128.665 1.00 112.22 ? 1284 MET A CB  1 
ATOM 2729 C CG  . MET A 1 527 ? 146.361 160.528 128.266 1.00 111.32 ? 1284 MET A CG  1 
ATOM 2730 S SD  . MET A 1 527 ? 145.411 159.940 129.679 1.00 114.36 ? 1284 MET A SD  1 
ATOM 2731 C CE  . MET A 1 527 ? 144.307 158.781 128.879 1.00 106.40 ? 1284 MET A CE  1 
ATOM 2732 N N   . PRO A 1 528 ? 150.280 160.500 127.551 1.00 107.34 ? 1285 PRO A N   1 
ATOM 2733 C CA  . PRO A 1 528 ? 151.172 159.601 126.803 1.00 104.77 ? 1285 PRO A CA  1 
ATOM 2734 C C   . PRO A 1 528 ? 152.143 158.851 127.694 1.00 101.61 ? 1285 PRO A C   1 
ATOM 2735 O O   . PRO A 1 528 ? 152.464 157.691 127.410 1.00 99.51  ? 1285 PRO A O   1 
ATOM 2736 C CB  . PRO A 1 528 ? 151.899 160.547 125.839 1.00 105.41 ? 1285 PRO A CB  1 
ATOM 2737 C CG  . PRO A 1 528 ? 151.810 161.878 126.480 1.00 105.73 ? 1285 PRO A CG  1 
ATOM 2738 C CD  . PRO A 1 528 ? 150.475 161.903 127.146 1.00 108.96 ? 1285 PRO A CD  1 
ATOM 2739 N N   . ILE A 1 529 ? 152.611 159.474 128.776 1.00 102.53 ? 1286 ILE A N   1 
ATOM 2740 C CA  . ILE A 1 529 ? 153.492 158.779 129.711 1.00 102.95 ? 1286 ILE A CA  1 
ATOM 2741 C C   . ILE A 1 529 ? 152.773 157.582 130.318 1.00 100.35 ? 1286 ILE A C   1 
ATOM 2742 O O   . ILE A 1 529 ? 153.328 156.480 130.413 1.00 100.31 ? 1286 ILE A O   1 
ATOM 2743 C CB  . ILE A 1 529 ? 153.990 159.748 130.798 1.00 102.86 ? 1286 ILE A CB  1 
ATOM 2744 C CG1 . ILE A 1 529 ? 154.648 160.973 130.164 1.00 105.81 ? 1286 ILE A CG1 1 
ATOM 2745 C CG2 . ILE A 1 529 ? 154.964 159.050 131.730 1.00 100.70 ? 1286 ILE A CG2 1 
ATOM 2746 C CD1 . ILE A 1 529 ? 155.895 160.655 129.371 1.00 107.35 ? 1286 ILE A CD1 1 
ATOM 2747 N N   . THR A 1 530 ? 151.522 157.783 130.738 1.00 99.41  ? 1287 THR A N   1 
ATOM 2748 C CA  . THR A 1 530 ? 150.756 156.690 131.326 1.00 96.05  ? 1287 THR A CA  1 
ATOM 2749 C C   . THR A 1 530 ? 150.485 155.590 130.310 1.00 94.76  ? 1287 THR A C   1 
ATOM 2750 O O   . THR A 1 530 ? 150.611 154.405 130.632 1.00 93.40  ? 1287 THR A O   1 
ATOM 2751 C CB  . THR A 1 530 ? 149.443 157.211 131.902 1.00 95.47  ? 1287 THR A CB  1 
ATOM 2752 O OG1 . THR A 1 530 ? 148.708 157.889 130.877 1.00 97.86  ? 1287 THR A OG1 1 
ATOM 2753 C CG2 . THR A 1 530 ? 149.710 158.163 133.054 1.00 97.62  ? 1287 THR A CG2 1 
ATOM 2754 N N   . ILE A 1 531 ? 150.109 155.954 129.082 1.00 94.96  ? 1288 ILE A N   1 
ATOM 2755 C CA  . ILE A 1 531 ? 149.830 154.915 128.094 1.00 90.88  ? 1288 ILE A CA  1 
ATOM 2756 C C   . ILE A 1 531 ? 151.104 154.162 127.729 1.00 93.63  ? 1288 ILE A C   1 
ATOM 2757 O O   . ILE A 1 531 ? 151.049 152.979 127.374 1.00 92.51  ? 1288 ILE A O   1 
ATOM 2758 C CB  . ILE A 1 531 ? 149.142 155.501 126.847 1.00 93.23  ? 1288 ILE A CB  1 
ATOM 2759 C CG1 . ILE A 1 531 ? 148.472 154.390 126.042 1.00 88.03  ? 1288 ILE A CG1 1 
ATOM 2760 C CG2 . ILE A 1 531 ? 150.132 156.213 125.953 1.00 100.89 ? 1288 ILE A CG2 1 
ATOM 2761 C CD1 . ILE A 1 531 ? 147.293 153.778 126.733 1.00 87.52  ? 1288 ILE A CD1 1 
ATOM 2762 N N   . CYS A 1 532 ? 152.265 154.816 127.801 1.00 98.90  ? 1289 CYS A N   1 
ATOM 2763 C CA  . CYS A 1 532 ? 153.509 154.123 127.493 1.00 98.39  ? 1289 CYS A CA  1 
ATOM 2764 C C   . CYS A 1 532 ? 153.936 153.195 128.622 1.00 95.93  ? 1289 CYS A C   1 
ATOM 2765 O O   . CYS A 1 532 ? 154.361 152.063 128.366 1.00 95.53  ? 1289 CYS A O   1 
ATOM 2766 C CB  . CYS A 1 532 ? 154.615 155.133 127.192 1.00 102.59 ? 1289 CYS A CB  1 
ATOM 2767 S SG  . CYS A 1 532 ? 156.158 154.380 126.638 1.00 119.56 ? 1289 CYS A SG  1 
ATOM 2768 N N   . ILE A 1 533 ? 153.837 153.648 129.874 1.00 94.23  ? 1290 ILE A N   1 
ATOM 2769 C CA  . ILE A 1 533 ? 154.301 152.810 130.976 1.00 91.57  ? 1290 ILE A CA  1 
ATOM 2770 C C   . ILE A 1 533 ? 153.306 151.696 131.263 1.00 89.53  ? 1290 ILE A C   1 
ATOM 2771 O O   . ILE A 1 533 ? 153.686 150.633 131.765 1.00 90.18  ? 1290 ILE A O   1 
ATOM 2772 C CB  . ILE A 1 533 ? 154.575 153.649 132.238 1.00 88.67  ? 1290 ILE A CB  1 
ATOM 2773 C CG1 . ILE A 1 533 ? 153.282 154.255 132.779 1.00 89.62  ? 1290 ILE A CG1 1 
ATOM 2774 C CG2 . ILE A 1 533 ? 155.601 154.733 131.949 1.00 93.38  ? 1290 ILE A CG2 1 
ATOM 2775 C CD1 . ILE A 1 533 ? 153.460 154.985 134.086 1.00 92.23  ? 1290 ILE A CD1 1 
ATOM 2776 N N   . ALA A 1 534 ? 152.025 151.913 130.956 1.00 87.08  ? 1291 ALA A N   1 
ATOM 2777 C CA  . ALA A 1 534 ? 151.020 150.887 131.205 1.00 81.82  ? 1291 ALA A CA  1 
ATOM 2778 C C   . ALA A 1 534 ? 151.277 149.652 130.358 1.00 82.09  ? 1291 ALA A C   1 
ATOM 2779 O O   . ALA A 1 534 ? 151.140 148.520 130.836 1.00 83.41  ? 1291 ALA A O   1 
ATOM 2780 C CB  . ALA A 1 534 ? 149.624 151.442 130.932 1.00 80.87  ? 1291 ALA A CB  1 
ATOM 2781 N N   . TYR A 1 535 ? 151.655 149.848 129.101 1.00 82.07  ? 1292 TYR A N   1 
ATOM 2782 C CA  . TYR A 1 535 ? 151.945 148.753 128.192 1.00 82.44  ? 1292 TYR A CA  1 
ATOM 2783 C C   . TYR A 1 535 ? 153.426 148.419 128.144 1.00 85.63  ? 1292 TYR A C   1 
ATOM 2784 O O   . TYR A 1 535 ? 153.850 147.638 127.288 1.00 87.67  ? 1292 TYR A O   1 
ATOM 2785 C CB  . TYR A 1 535 ? 151.417 149.086 126.800 1.00 79.77  ? 1292 TYR A CB  1 
ATOM 2786 C CG  . TYR A 1 535 ? 149.909 149.116 126.754 1.00 75.61  ? 1292 TYR A CG  1 
ATOM 2787 C CD1 . TYR A 1 535 ? 149.207 150.268 127.077 1.00 76.96  ? 1292 TYR A CD1 1 
ATOM 2788 C CD2 . TYR A 1 535 ? 149.186 147.984 126.416 1.00 72.82  ? 1292 TYR A CD2 1 
ATOM 2789 C CE1 . TYR A 1 535 ? 147.832 150.292 127.048 1.00 74.87  ? 1292 TYR A CE1 1 
ATOM 2790 C CE2 . TYR A 1 535 ? 147.816 148.002 126.379 1.00 70.59  ? 1292 TYR A CE2 1 
ATOM 2791 C CZ  . TYR A 1 535 ? 147.143 149.156 126.695 1.00 72.19  ? 1292 TYR A CZ  1 
ATOM 2792 O OH  . TYR A 1 535 ? 145.770 149.161 126.666 1.00 67.14  ? 1292 TYR A OH  1 
ATOM 2793 N N   . PHE A 1 536 ? 154.222 148.998 129.043 1.00 86.58  ? 1293 PHE A N   1 
ATOM 2794 C CA  . PHE A 1 536 ? 155.621 148.617 129.164 1.00 90.35  ? 1293 PHE A CA  1 
ATOM 2795 C C   . PHE A 1 536 ? 155.784 147.234 129.775 1.00 90.64  ? 1293 PHE A C   1 
ATOM 2796 O O   . PHE A 1 536 ? 156.837 146.612 129.598 1.00 93.21  ? 1293 PHE A O   1 
ATOM 2797 C CB  . PHE A 1 536 ? 156.372 149.653 130.003 1.00 93.40  ? 1293 PHE A CB  1 
ATOM 2798 C CG  . PHE A 1 536 ? 157.858 149.442 130.046 1.00 101.39 ? 1293 PHE A CG  1 
ATOM 2799 C CD1 . PHE A 1 536 ? 158.662 149.889 129.013 1.00 106.12 ? 1293 PHE A CD1 1 
ATOM 2800 C CD2 . PHE A 1 536 ? 158.452 148.812 131.124 1.00 102.80 ? 1293 PHE A CD2 1 
ATOM 2801 C CE1 . PHE A 1 536 ? 160.029 149.702 129.047 1.00 106.89 ? 1293 PHE A CE1 1 
ATOM 2802 C CE2 . PHE A 1 536 ? 159.819 148.625 131.164 1.00 105.47 ? 1293 PHE A CE2 1 
ATOM 2803 C CZ  . PHE A 1 536 ? 160.608 149.069 130.125 1.00 105.24 ? 1293 PHE A CZ  1 
ATOM 2804 N N   . ASN A 1 537 ? 154.762 146.737 130.479 1.00 87.79  ? 1294 ASN A N   1 
ATOM 2805 C CA  . ASN A 1 537 ? 154.872 145.438 131.133 1.00 86.88  ? 1294 ASN A CA  1 
ATOM 2806 C C   . ASN A 1 537 ? 155.103 144.319 130.128 1.00 85.27  ? 1294 ASN A C   1 
ATOM 2807 O O   . ASN A 1 537 ? 155.869 143.389 130.406 1.00 86.43  ? 1294 ASN A O   1 
ATOM 2808 C CB  . ASN A 1 537 ? 153.625 145.158 131.973 1.00 80.99  ? 1294 ASN A CB  1 
ATOM 2809 C CG  . ASN A 1 537 ? 152.364 145.094 131.145 1.00 79.30  ? 1294 ASN A CG  1 
ATOM 2810 O OD1 . ASN A 1 537 ? 152.047 144.064 130.557 1.00 79.15  ? 1294 ASN A OD1 1 
ATOM 2811 N ND2 . ASN A 1 537 ? 151.629 146.196 131.105 1.00 79.36  ? 1294 ASN A ND2 1 
ATOM 2812 N N   . ASN A 1 538 ? 154.478 144.403 128.949 1.00 82.67  ? 1295 ASN A N   1 
ATOM 2813 C CA  . ASN A 1 538 ? 154.699 143.388 127.925 1.00 82.68  ? 1295 ASN A CA  1 
ATOM 2814 C C   . ASN A 1 538 ? 156.173 143.271 127.572 1.00 87.52  ? 1295 ASN A C   1 
ATOM 2815 O O   . ASN A 1 538 ? 156.621 142.215 127.113 1.00 89.00  ? 1295 ASN A O   1 
ATOM 2816 C CB  . ASN A 1 538 ? 153.896 143.714 126.666 1.00 79.07  ? 1295 ASN A CB  1 
ATOM 2817 C CG  . ASN A 1 538 ? 152.496 144.177 126.972 1.00 76.31  ? 1295 ASN A CG  1 
ATOM 2818 O OD1 . ASN A 1 538 ? 151.588 143.371 127.152 1.00 75.68  ? 1295 ASN A OD1 1 
ATOM 2819 N ND2 . ASN A 1 538 ? 152.307 145.487 127.021 1.00 76.65  ? 1295 ASN A ND2 1 
ATOM 2820 N N   . CYS A 1 539 ? 156.938 144.345 127.771 1.00 89.93  ? 1296 CYS A N   1 
ATOM 2821 C CA  . CYS A 1 539 ? 158.369 144.284 127.508 1.00 94.75  ? 1296 CYS A CA  1 
ATOM 2822 C C   . CYS A 1 539 ? 159.063 143.306 128.445 1.00 93.35  ? 1296 CYS A C   1 
ATOM 2823 O O   . CYS A 1 539 ? 159.916 142.523 128.013 1.00 92.98  ? 1296 CYS A O   1 
ATOM 2824 C CB  . CYS A 1 539 ? 158.985 145.675 127.639 1.00 101.26 ? 1296 CYS A CB  1 
ATOM 2825 S SG  . CYS A 1 539 ? 160.781 145.713 127.463 1.00 115.37 ? 1296 CYS A SG  1 
ATOM 2826 N N   . LEU A 1 540 ? 158.709 143.324 129.732 1.00 91.49  ? 1297 LEU A N   1 
ATOM 2827 C CA  . LEU A 1 540 ? 159.464 142.565 130.720 1.00 90.74  ? 1297 LEU A CA  1 
ATOM 2828 C C   . LEU A 1 540 ? 158.651 141.480 131.410 1.00 88.79  ? 1297 LEU A C   1 
ATOM 2829 O O   . LEU A 1 540 ? 159.132 140.897 132.387 1.00 90.49  ? 1297 LEU A O   1 
ATOM 2830 C CB  . LEU A 1 540 ? 160.083 143.505 131.759 1.00 90.16  ? 1297 LEU A CB  1 
ATOM 2831 C CG  . LEU A 1 540 ? 159.217 144.237 132.777 1.00 87.44  ? 1297 LEU A CG  1 
ATOM 2832 C CD1 . LEU A 1 540 ? 159.251 143.522 134.114 1.00 87.73  ? 1297 LEU A CD1 1 
ATOM 2833 C CD2 . LEU A 1 540 ? 159.723 145.649 132.928 1.00 92.68  ? 1297 LEU A CD2 1 
ATOM 2834 N N   . ASN A 1 541 ? 157.448 141.175 130.932 1.00 88.81  ? 1298 ASN A N   1 
ATOM 2835 C CA  . ASN A 1 541 ? 156.786 139.957 131.387 1.00 84.46  ? 1298 ASN A CA  1 
ATOM 2836 C C   . ASN A 1 541 ? 157.635 138.715 131.142 1.00 86.34  ? 1298 ASN A C   1 
ATOM 2837 O O   . ASN A 1 541 ? 157.695 137.861 132.044 1.00 88.78  ? 1298 ASN A O   1 
ATOM 2838 C CB  . ASN A 1 541 ? 155.407 139.821 130.730 1.00 82.40  ? 1298 ASN A CB  1 
ATOM 2839 C CG  . ASN A 1 541 ? 154.310 140.455 131.550 1.00 81.84  ? 1298 ASN A CG  1 
ATOM 2840 O OD1 . ASN A 1 541 ? 154.572 141.132 132.541 1.00 83.53  ? 1298 ASN A OD1 1 
ATOM 2841 N ND2 . ASN A 1 541 ? 153.069 140.240 131.140 1.00 74.73  ? 1298 ASN A ND2 1 
ATOM 2842 N N   . PRO A 1 542 ? 158.296 138.539 129.992 1.00 87.38  ? 1299 PRO A N   1 
ATOM 2843 C CA  . PRO A 1 542 ? 159.227 137.407 129.863 1.00 87.06  ? 1299 PRO A CA  1 
ATOM 2844 C C   . PRO A 1 542 ? 160.358 137.424 130.873 1.00 87.42  ? 1299 PRO A C   1 
ATOM 2845 O O   . PRO A 1 542 ? 160.807 136.353 131.300 1.00 90.55  ? 1299 PRO A O   1 
ATOM 2846 C CB  . PRO A 1 542 ? 159.758 137.558 128.432 1.00 88.18  ? 1299 PRO A CB  1 
ATOM 2847 C CG  . PRO A 1 542 ? 158.686 138.275 127.718 1.00 89.84  ? 1299 PRO A CG  1 
ATOM 2848 C CD  . PRO A 1 542 ? 158.122 139.238 128.707 1.00 89.02  ? 1299 PRO A CD  1 
ATOM 2849 N N   . LEU A 1 543 ? 160.831 138.607 131.274 1.00 88.26  ? 1300 LEU A N   1 
ATOM 2850 C CA  . LEU A 1 543 ? 161.986 138.681 132.164 1.00 91.40  ? 1300 LEU A CA  1 
ATOM 2851 C C   . LEU A 1 543 ? 161.727 137.981 133.490 1.00 91.19  ? 1300 LEU A C   1 
ATOM 2852 O O   . LEU A 1 543 ? 162.646 137.387 134.064 1.00 93.91  ? 1300 LEU A O   1 
ATOM 2853 C CB  . LEU A 1 543 ? 162.380 140.139 132.399 1.00 91.10  ? 1300 LEU A CB  1 
ATOM 2854 C CG  . LEU A 1 543 ? 162.936 140.874 131.179 1.00 92.05  ? 1300 LEU A CG  1 
ATOM 2855 C CD1 . LEU A 1 543 ? 163.501 142.225 131.578 1.00 91.22  ? 1300 LEU A CD1 1 
ATOM 2856 C CD2 . LEU A 1 543 ? 163.993 140.031 130.483 1.00 90.93  ? 1300 LEU A CD2 1 
ATOM 2857 N N   . PHE A 1 544 ? 160.489 138.028 133.986 1.00 86.72  ? 1301 PHE A N   1 
ATOM 2858 C CA  . PHE A 1 544 ? 160.162 137.291 135.201 1.00 87.67  ? 1301 PHE A CA  1 
ATOM 2859 C C   . PHE A 1 544 ? 160.431 135.805 135.022 1.00 91.27  ? 1301 PHE A C   1 
ATOM 2860 O O   . PHE A 1 544 ? 161.036 135.166 135.893 1.00 94.87  ? 1301 PHE A O   1 
ATOM 2861 C CB  . PHE A 1 544 ? 158.705 137.535 135.585 1.00 82.48  ? 1301 PHE A CB  1 
ATOM 2862 C CG  . PHE A 1 544 ? 158.426 138.938 136.025 1.00 80.21  ? 1301 PHE A CG  1 
ATOM 2863 C CD1 . PHE A 1 544 ? 159.365 139.647 136.749 1.00 81.43  ? 1301 PHE A CD1 1 
ATOM 2864 C CD2 . PHE A 1 544 ? 157.230 139.552 135.709 1.00 77.83  ? 1301 PHE A CD2 1 
ATOM 2865 C CE1 . PHE A 1 544 ? 159.114 140.939 137.156 1.00 80.63  ? 1301 PHE A CE1 1 
ATOM 2866 C CE2 . PHE A 1 544 ? 156.973 140.845 136.112 1.00 75.51  ? 1301 PHE A CE2 1 
ATOM 2867 C CZ  . PHE A 1 544 ? 157.916 141.539 136.836 1.00 77.47  ? 1301 PHE A CZ  1 
ATOM 2868 N N   . TYR A 1 545 ? 160.019 135.243 133.883 1.00 87.38  ? 1302 TYR A N   1 
ATOM 2869 C CA  . TYR A 1 545 ? 160.335 133.851 133.587 1.00 87.84  ? 1302 TYR A CA  1 
ATOM 2870 C C   . TYR A 1 545 ? 161.839 133.618 133.626 1.00 94.15  ? 1302 TYR A C   1 
ATOM 2871 O O   . TYR A 1 545 ? 162.302 132.559 134.064 1.00 98.40  ? 1302 TYR A O   1 
ATOM 2872 C CB  . TYR A 1 545 ? 159.777 133.459 132.218 1.00 85.10  ? 1302 TYR A CB  1 
ATOM 2873 C CG  . TYR A 1 545 ? 158.274 133.574 132.063 1.00 83.60  ? 1302 TYR A CG  1 
ATOM 2874 C CD1 . TYR A 1 545 ? 157.645 134.809 132.083 1.00 84.06  ? 1302 TYR A CD1 1 
ATOM 2875 C CD2 . TYR A 1 545 ? 157.492 132.449 131.856 1.00 84.80  ? 1302 TYR A CD2 1 
ATOM 2876 C CE1 . TYR A 1 545 ? 156.283 134.920 131.931 1.00 84.64  ? 1302 TYR A CE1 1 
ATOM 2877 C CE2 . TYR A 1 545 ? 156.126 132.551 131.699 1.00 82.90  ? 1302 TYR A CE2 1 
ATOM 2878 C CZ  . TYR A 1 545 ? 155.529 133.790 131.736 1.00 84.79  ? 1302 TYR A CZ  1 
ATOM 2879 O OH  . TYR A 1 545 ? 154.169 133.904 131.578 1.00 82.49  ? 1302 TYR A OH  1 
ATOM 2880 N N   . GLY A 1 546 ? 162.618 134.600 133.177 1.00 95.21  ? 1303 GLY A N   1 
ATOM 2881 C CA  . GLY A 1 546 ? 164.061 134.480 133.199 1.00 98.11  ? 1303 GLY A CA  1 
ATOM 2882 C C   . GLY A 1 546 ? 164.711 134.776 134.530 1.00 101.74 ? 1303 GLY A C   1 
ATOM 2883 O O   . GLY A 1 546 ? 165.922 134.579 134.667 1.00 103.69 ? 1303 GLY A O   1 
ATOM 2884 N N   . PHE A 1 547 ? 163.946 135.248 135.512 1.00 100.75 ? 1304 PHE A N   1 
ATOM 2885 C CA  . PHE A 1 547 ? 164.473 135.515 136.845 1.00 99.15  ? 1304 PHE A CA  1 
ATOM 2886 C C   . PHE A 1 547 ? 163.905 134.591 137.906 1.00 98.25  ? 1304 PHE A C   1 
ATOM 2887 O O   . PHE A 1 547 ? 164.626 134.200 138.826 1.00 98.84  ? 1304 PHE A O   1 
ATOM 2888 C CB  . PHE A 1 547 ? 164.197 136.968 137.248 1.00 99.73  ? 1304 PHE A CB  1 
ATOM 2889 C CG  . PHE A 1 547 ? 165.099 137.969 136.581 1.00 106.81 ? 1304 PHE A CG  1 
ATOM 2890 C CD1 . PHE A 1 547 ? 166.157 137.553 135.789 1.00 107.14 ? 1304 PHE A CD1 1 
ATOM 2891 C CD2 . PHE A 1 547 ? 164.895 139.327 136.758 1.00 109.54 ? 1304 PHE A CD2 1 
ATOM 2892 C CE1 . PHE A 1 547 ? 166.988 138.474 135.178 1.00 107.15 ? 1304 PHE A CE1 1 
ATOM 2893 C CE2 . PHE A 1 547 ? 165.723 140.251 136.151 1.00 109.91 ? 1304 PHE A CE2 1 
ATOM 2894 C CZ  . PHE A 1 547 ? 166.771 139.823 135.360 1.00 109.05 ? 1304 PHE A CZ  1 
ATOM 2895 N N   . LEU A 1 548 ? 162.629 134.234 137.801 1.00 96.74  ? 1305 LEU A N   1 
ATOM 2896 C CA  . LEU A 1 548 ? 161.971 133.367 138.765 1.00 94.94  ? 1305 LEU A CA  1 
ATOM 2897 C C   . LEU A 1 548 ? 161.831 131.936 138.267 1.00 95.52  ? 1305 LEU A C   1 
ATOM 2898 O O   . LEU A 1 548 ? 161.184 131.122 138.929 1.00 96.21  ? 1305 LEU A O   1 
ATOM 2899 C CB  . LEU A 1 548 ? 160.599 133.936 139.122 1.00 89.62  ? 1305 LEU A CB  1 
ATOM 2900 C CG  . LEU A 1 548 ? 160.605 135.404 139.544 1.00 87.40  ? 1305 LEU A CG  1 
ATOM 2901 C CD1 . LEU A 1 548 ? 159.192 135.908 139.747 1.00 81.89  ? 1305 LEU A CD1 1 
ATOM 2902 C CD2 . LEU A 1 548 ? 161.424 135.584 140.806 1.00 89.90  ? 1305 LEU A CD2 1 
ATOM 2903 N N   . GLY A 1 549 ? 162.419 131.610 137.122 1.00 94.95  ? 1306 GLY A N   1 
ATOM 2904 C CA  . GLY A 1 549 ? 162.313 130.273 136.571 1.00 96.40  ? 1306 GLY A CA  1 
ATOM 2905 C C   . GLY A 1 549 ? 163.356 129.314 137.108 1.00 99.95  ? 1306 GLY A C   1 
ATOM 2906 O O   . GLY A 1 549 ? 164.230 128.855 136.372 1.00 101.88 ? 1306 GLY A O   1 
ATOM 2907 N N   . SER B 1 29  ? 135.244 169.110 127.505 1.00 128.63 ? 29   SER B N   1 
ATOM 2908 C CA  . SER B 1 29  ? 134.758 170.106 126.559 1.00 132.65 ? 29   SER B CA  1 
ATOM 2909 C C   . SER B 1 29  ? 135.893 171.005 126.080 1.00 132.65 ? 29   SER B C   1 
ATOM 2910 O O   . SER B 1 29  ? 137.041 170.570 125.983 1.00 131.64 ? 29   SER B O   1 
ATOM 2911 C CB  . SER B 1 29  ? 133.652 170.950 127.192 1.00 133.09 ? 29   SER B CB  1 
ATOM 2912 O OG  . SER B 1 29  ? 132.612 170.130 127.694 1.00 132.52 ? 29   SER B OG  1 
ATOM 2913 N N   . TYR B 1 30  ? 135.555 172.262 125.784 1.00 132.75 ? 30   TYR B N   1 
ATOM 2914 C CA  . TYR B 1 30  ? 136.526 173.273 125.359 1.00 131.58 ? 30   TYR B CA  1 
ATOM 2915 C C   . TYR B 1 30  ? 137.325 172.806 124.144 1.00 128.68 ? 30   TYR B C   1 
ATOM 2916 O O   . TYR B 1 30  ? 138.533 173.031 124.048 1.00 126.30 ? 30   TYR B O   1 
ATOM 2917 C CB  . TYR B 1 30  ? 137.467 173.655 126.505 1.00 131.53 ? 30   TYR B CB  1 
ATOM 2918 C CG  . TYR B 1 30  ? 136.792 173.763 127.853 1.00 134.31 ? 30   TYR B CG  1 
ATOM 2919 C CD1 . TYR B 1 30  ? 135.995 174.855 128.169 1.00 134.83 ? 30   TYR B CD1 1 
ATOM 2920 C CD2 . TYR B 1 30  ? 136.962 172.777 128.816 1.00 133.72 ? 30   TYR B CD2 1 
ATOM 2921 C CE1 . TYR B 1 30  ? 135.380 174.957 129.403 1.00 135.61 ? 30   TYR B CE1 1 
ATOM 2922 C CE2 . TYR B 1 30  ? 136.352 172.870 130.051 1.00 133.08 ? 30   TYR B CE2 1 
ATOM 2923 C CZ  . TYR B 1 30  ? 135.563 173.962 130.339 1.00 134.48 ? 30   TYR B CZ  1 
ATOM 2924 O OH  . TYR B 1 30  ? 134.956 174.057 131.569 1.00 131.51 ? 30   TYR B OH  1 
ATOM 2925 N N   . TYR B 1 31  ? 136.648 172.151 123.209 1.00 127.65 ? 31   TYR B N   1 
ATOM 2926 C CA  . TYR B 1 31  ? 137.299 171.647 122.011 1.00 124.53 ? 31   TYR B CA  1 
ATOM 2927 C C   . TYR B 1 31  ? 137.227 172.670 120.883 1.00 125.91 ? 31   TYR B C   1 
ATOM 2928 O O   . TYR B 1 31  ? 136.367 173.554 120.861 1.00 127.99 ? 31   TYR B O   1 
ATOM 2929 C CB  . TYR B 1 31  ? 136.664 170.330 121.562 1.00 119.18 ? 31   TYR B CB  1 
ATOM 2930 C CG  . TYR B 1 31  ? 137.177 169.113 122.294 1.00 116.22 ? 31   TYR B CG  1 
ATOM 2931 C CD1 . TYR B 1 31  ? 138.159 169.227 123.268 1.00 120.68 ? 31   TYR B CD1 1 
ATOM 2932 C CD2 . TYR B 1 31  ? 136.692 167.846 121.998 1.00 111.65 ? 31   TYR B CD2 1 
ATOM 2933 C CE1 . TYR B 1 31  ? 138.635 168.116 123.936 1.00 122.48 ? 31   TYR B CE1 1 
ATOM 2934 C CE2 . TYR B 1 31  ? 137.162 166.729 122.659 1.00 112.45 ? 31   TYR B CE2 1 
ATOM 2935 C CZ  . TYR B 1 31  ? 138.135 166.870 123.627 1.00 120.63 ? 31   TYR B CZ  1 
ATOM 2936 O OH  . TYR B 1 31  ? 138.610 165.763 124.291 1.00 116.41 ? 31   TYR B OH  1 
ATOM 2937 N N   . ARG B 1 32  ? 138.158 172.541 119.941 1.00 124.31 ? 32   ARG B N   1 
ATOM 2938 C CA  . ARG B 1 32  ? 138.140 173.365 118.741 1.00 122.05 ? 32   ARG B CA  1 
ATOM 2939 C C   . ARG B 1 32  ? 136.958 172.982 117.859 1.00 119.12 ? 32   ARG B C   1 
ATOM 2940 O O   . ARG B 1 32  ? 136.701 171.800 117.620 1.00 118.00 ? 32   ARG B O   1 
ATOM 2941 C CB  . ARG B 1 32  ? 139.453 173.198 117.979 1.00 120.97 ? 32   ARG B CB  1 
ATOM 2942 C CG  . ARG B 1 32  ? 139.555 173.996 116.702 1.00 123.19 ? 32   ARG B CG  1 
ATOM 2943 C CD  . ARG B 1 32  ? 140.922 173.825 116.069 1.00 126.34 ? 32   ARG B CD  1 
ATOM 2944 N NE  . ARG B 1 32  ? 141.098 174.688 114.908 1.00 130.72 ? 32   ARG B NE  1 
ATOM 2945 C CZ  . ARG B 1 32  ? 141.589 175.918 114.960 1.00 132.82 ? 32   ARG B CZ  1 
ATOM 2946 N NH1 . ARG B 1 32  ? 141.965 176.465 116.104 1.00 131.18 ? 32   ARG B NH1 1 
ATOM 2947 N NH2 . ARG B 1 32  ? 141.705 176.618 113.835 1.00 132.33 ? 32   ARG B NH2 1 
ATOM 2948 N N   . MET B 1 33  ? 136.233 173.987 117.378 1.00 119.60 ? 33   MET B N   1 
ATOM 2949 C CA  . MET B 1 33  ? 135.023 173.773 116.596 1.00 117.00 ? 33   MET B CA  1 
ATOM 2950 C C   . MET B 1 33  ? 135.313 173.899 115.105 1.00 117.02 ? 33   MET B C   1 
ATOM 2951 O O   . MET B 1 33  ? 136.343 174.438 114.692 1.00 119.66 ? 33   MET B O   1 
ATOM 2952 C CB  . MET B 1 33  ? 133.934 174.766 117.005 1.00 116.44 ? 33   MET B CB  1 
ATOM 2953 C CG  . MET B 1 33  ? 133.778 174.916 118.509 1.00 120.44 ? 33   MET B CG  1 
ATOM 2954 S SD  . MET B 1 33  ? 133.542 173.343 119.358 1.00 118.59 ? 33   MET B SD  1 
ATOM 2955 C CE  . MET B 1 33  ? 131.938 172.857 118.735 1.00 115.17 ? 33   MET B CE  1 
ATOM 2956 N N   . GLY B 1 34  ? 134.387 173.392 114.296 1.00 114.40 ? 34   GLY B N   1 
ATOM 2957 C CA  . GLY B 1 34  ? 134.582 173.410 112.856 1.00 115.56 ? 34   GLY B CA  1 
ATOM 2958 C C   . GLY B 1 34  ? 133.316 173.047 112.113 1.00 113.31 ? 34   GLY B C   1 
ATOM 2959 O O   . GLY B 1 34  ? 132.316 172.631 112.704 1.00 114.12 ? 34   GLY B O   1 
ATOM 2960 N N   . TRP B 1 35  ? 133.376 173.221 110.793 1.00 113.28 ? 35   TRP B N   1 
ATOM 2961 C CA  . TRP B 1 35  ? 132.268 172.914 109.898 1.00 114.57 ? 35   TRP B CA  1 
ATOM 2962 C C   . TRP B 1 35  ? 132.820 172.261 108.640 1.00 116.98 ? 35   TRP B C   1 
ATOM 2963 O O   . TRP B 1 35  ? 133.782 172.764 108.054 1.00 121.35 ? 35   TRP B O   1 
ATOM 2964 C CB  . TRP B 1 35  ? 131.477 174.178 109.536 1.00 115.54 ? 35   TRP B CB  1 
ATOM 2965 C CG  . TRP B 1 35  ? 130.910 174.897 110.721 1.00 117.76 ? 35   TRP B CG  1 
ATOM 2966 C CD1 . TRP B 1 35  ? 131.555 175.794 111.523 1.00 118.41 ? 35   TRP B CD1 1 
ATOM 2967 C CD2 . TRP B 1 35  ? 129.579 174.783 111.237 1.00 118.78 ? 35   TRP B CD2 1 
ATOM 2968 N NE1 . TRP B 1 35  ? 130.710 176.241 112.509 1.00 119.50 ? 35   TRP B NE1 1 
ATOM 2969 C CE2 . TRP B 1 35  ? 129.490 175.636 112.355 1.00 120.28 ? 35   TRP B CE2 1 
ATOM 2970 C CE3 . TRP B 1 35  ? 128.455 174.041 110.864 1.00 117.92 ? 35   TRP B CE3 1 
ATOM 2971 C CZ2 . TRP B 1 35  ? 128.322 175.766 113.102 1.00 120.65 ? 35   TRP B CZ2 1 
ATOM 2972 C CZ3 . TRP B 1 35  ? 127.297 174.173 111.608 1.00 118.73 ? 35   TRP B CZ3 1 
ATOM 2973 C CH2 . TRP B 1 35  ? 127.239 175.028 112.712 1.00 119.82 ? 35   TRP B CH2 1 
ATOM 2974 N N   . TYR B 1 36  ? 132.208 171.154 108.222 1.00 113.75 ? 36   TYR B N   1 
ATOM 2975 C CA  . TYR B 1 36  ? 132.687 170.367 107.095 1.00 112.22 ? 36   TYR B CA  1 
ATOM 2976 C C   . TYR B 1 36  ? 131.558 170.151 106.098 1.00 116.87 ? 36   TYR B C   1 
ATOM 2977 O O   . TYR B 1 36  ? 130.381 170.150 106.463 1.00 120.38 ? 36   TYR B O   1 
ATOM 2978 C CB  . TYR B 1 36  ? 133.233 169.007 107.553 1.00 112.74 ? 36   TYR B CB  1 
ATOM 2979 C CG  . TYR B 1 36  ? 134.522 169.070 108.342 1.00 109.84 ? 36   TYR B CG  1 
ATOM 2980 C CD1 . TYR B 1 36  ? 134.565 169.653 109.599 1.00 109.57 ? 36   TYR B CD1 1 
ATOM 2981 C CD2 . TYR B 1 36  ? 135.690 168.522 107.840 1.00 110.58 ? 36   TYR B CD2 1 
ATOM 2982 C CE1 . TYR B 1 36  ? 135.735 169.709 110.320 1.00 109.39 ? 36   TYR B CE1 1 
ATOM 2983 C CE2 . TYR B 1 36  ? 136.864 168.572 108.556 1.00 108.36 ? 36   TYR B CE2 1 
ATOM 2984 C CZ  . TYR B 1 36  ? 136.879 169.166 109.795 1.00 107.71 ? 36   TYR B CZ  1 
ATOM 2985 O OH  . TYR B 1 36  ? 138.046 169.219 110.517 1.00 110.46 ? 36   TYR B OH  1 
ATOM 2986 N N   . ARG B 1 37  ? 131.926 169.960 104.834 1.00 119.01 ? 37   ARG B N   1 
ATOM 2987 C CA  . ARG B 1 37  ? 130.973 169.665 103.773 1.00 121.20 ? 37   ARG B CA  1 
ATOM 2988 C C   . ARG B 1 37  ? 130.932 168.169 103.489 1.00 123.91 ? 37   ARG B C   1 
ATOM 2989 O O   . ARG B 1 37  ? 131.910 167.450 103.703 1.00 125.47 ? 37   ARG B O   1 
ATOM 2990 C CB  . ARG B 1 37  ? 131.326 170.412 102.484 1.00 124.60 ? 37   ARG B CB  1 
ATOM 2991 C CG  . ARG B 1 37  ? 130.867 171.855 102.450 1.00 128.88 ? 37   ARG B CG  1 
ATOM 2992 C CD  . ARG B 1 37  ? 131.238 172.527 101.138 1.00 126.11 ? 37   ARG B CD  1 
ATOM 2993 N NE  . ARG B 1 37  ? 130.799 173.917 101.102 1.00 127.32 ? 37   ARG B NE  1 
ATOM 2994 C CZ  . ARG B 1 37  ? 130.925 174.715 100.051 1.00 132.27 ? 37   ARG B CZ  1 
ATOM 2995 N NH1 . ARG B 1 37  ? 131.480 174.295 98.927  1.00 134.66 ? 37   ARG B NH1 1 
ATOM 2996 N NH2 . ARG B 1 37  ? 130.480 175.965 100.129 1.00 134.81 ? 37   ARG B NH2 1 
ATOM 2997 N N   . GLN B 1 38  ? 129.787 167.709 102.994 1.00 125.65 ? 38   GLN B N   1 
ATOM 2998 C CA  . GLN B 1 38  ? 129.572 166.312 102.628 1.00 127.15 ? 38   GLN B CA  1 
ATOM 2999 C C   . GLN B 1 38  ? 128.937 166.229 101.245 1.00 126.53 ? 38   GLN B C   1 
ATOM 3000 O O   . GLN B 1 38  ? 127.886 165.619 101.039 1.00 127.72 ? 38   GLN B O   1 
ATOM 3001 C CB  . GLN B 1 38  ? 128.729 165.603 103.688 1.00 126.48 ? 38   GLN B CB  1 
ATOM 3002 C CG  . GLN B 1 38  ? 128.615 164.087 103.524 1.00 127.80 ? 38   GLN B CG  1 
ATOM 3003 C CD  . GLN B 1 38  ? 129.950 163.411 103.282 1.00 128.24 ? 38   GLN B CD  1 
ATOM 3004 O OE1 . GLN B 1 38  ? 130.946 163.714 103.938 1.00 128.55 ? 38   GLN B OE1 1 
ATOM 3005 N NE2 . GLN B 1 38  ? 129.976 162.486 102.330 1.00 126.88 ? 38   GLN B NE2 1 
ATOM 3006 N N   . ALA B 1 39  ? 129.568 166.877 100.273 1.00 125.90 ? 39   ALA B N   1 
ATOM 3007 C CA  . ALA B 1 39  ? 129.091 166.842 98.897  1.00 123.53 ? 39   ALA B CA  1 
ATOM 3008 C C   . ALA B 1 39  ? 129.893 165.840 98.073  1.00 117.59 ? 39   ALA B C   1 
ATOM 3009 O O   . ALA B 1 39  ? 130.424 166.176 97.015  1.00 111.55 ? 39   ALA B O   1 
ATOM 3010 C CB  . ALA B 1 39  ? 129.167 168.225 98.272  1.00 122.82 ? 39   ALA B CB  1 
ATOM 3011 N N   . GLU B 1 43  ? 132.864 162.044 102.792 1.00 128.67 ? 43   GLU B N   1 
ATOM 3012 C CA  . GLU B 1 43  ? 133.773 163.004 102.182 1.00 127.93 ? 43   GLU B CA  1 
ATOM 3013 C C   . GLU B 1 43  ? 134.413 163.887 103.244 1.00 126.09 ? 43   GLU B C   1 
ATOM 3014 O O   . GLU B 1 43  ? 135.632 163.883 103.412 1.00 126.62 ? 43   GLU B O   1 
ATOM 3015 C CB  . GLU B 1 43  ? 133.037 163.863 101.151 1.00 126.77 ? 43   GLU B CB  1 
ATOM 3016 C CG  . GLU B 1 43  ? 133.939 164.795 100.359 1.00 127.49 ? 43   GLU B CG  1 
ATOM 3017 C CD  . GLU B 1 43  ? 134.871 164.052 99.419  1.00 131.28 ? 43   GLU B CD  1 
ATOM 3018 O OE1 . GLU B 1 43  ? 134.597 162.875 99.106  1.00 131.88 ? 43   GLU B OE1 1 
ATOM 3019 O OE2 . GLU B 1 43  ? 135.881 164.648 98.991  1.00 130.56 ? 43   GLU B OE2 1 
ATOM 3020 N N   . ARG B 1 44  ? 133.575 164.639 103.959 1.00 124.00 ? 44   ARG B N   1 
ATOM 3021 C CA  . ARG B 1 44  ? 134.015 165.533 105.030 1.00 121.40 ? 44   ARG B CA  1 
ATOM 3022 C C   . ARG B 1 44  ? 135.081 166.511 104.532 1.00 121.90 ? 44   ARG B C   1 
ATOM 3023 O O   . ARG B 1 44  ? 136.232 166.507 104.978 1.00 123.17 ? 44   ARG B O   1 
ATOM 3024 C CB  . ARG B 1 44  ? 134.523 164.740 106.236 1.00 120.25 ? 44   ARG B CB  1 
ATOM 3025 C CG  . ARG B 1 44  ? 133.469 163.893 106.923 1.00 118.92 ? 44   ARG B CG  1 
ATOM 3026 C CD  . ARG B 1 44  ? 132.280 164.730 107.350 1.00 118.22 ? 44   ARG B CD  1 
ATOM 3027 N NE  . ARG B 1 44  ? 131.387 163.983 108.226 1.00 121.69 ? 44   ARG B NE  1 
ATOM 3028 C CZ  . ARG B 1 44  ? 130.443 163.153 107.806 1.00 127.94 ? 44   ARG B CZ  1 
ATOM 3029 N NH1 . ARG B 1 44  ? 130.239 162.931 106.518 1.00 129.61 ? 44   ARG B NH1 1 
ATOM 3030 N NH2 . ARG B 1 44  ? 129.683 162.528 108.702 1.00 125.24 ? 44   ARG B NH2 1 
ATOM 3031 N N   . GLU B 1 45  ? 134.674 167.354 103.586 1.00 121.04 ? 45   GLU B N   1 
ATOM 3032 C CA  . GLU B 1 45  ? 135.564 168.378 103.053 1.00 120.09 ? 45   GLU B CA  1 
ATOM 3033 C C   . GLU B 1 45  ? 135.617 169.549 104.027 1.00 120.20 ? 45   GLU B C   1 
ATOM 3034 O O   . GLU B 1 45  ? 134.585 170.149 104.346 1.00 121.92 ? 45   GLU B O   1 
ATOM 3035 C CB  . GLU B 1 45  ? 135.098 168.838 101.675 1.00 121.92 ? 45   GLU B CB  1 
ATOM 3036 C CG  . GLU B 1 45  ? 136.212 169.304 100.746 1.00 127.51 ? 45   GLU B CG  1 
ATOM 3037 C CD  . GLU B 1 45  ? 136.915 170.562 101.224 1.00 128.30 ? 45   GLU B CD  1 
ATOM 3038 O OE1 . GLU B 1 45  ? 137.796 170.465 102.104 1.00 126.77 ? 45   GLU B OE1 1 
ATOM 3039 O OE2 . GLU B 1 45  ? 136.580 171.654 100.720 1.00 127.80 ? 45   GLU B OE2 1 
ATOM 3040 N N   . PHE B 1 46  ? 136.820 169.871 104.494 1.00 118.78 ? 46   PHE B N   1 
ATOM 3041 C CA  . PHE B 1 46  ? 136.991 170.897 105.513 1.00 118.96 ? 46   PHE B CA  1 
ATOM 3042 C C   . PHE B 1 46  ? 136.679 172.276 104.953 1.00 122.10 ? 46   PHE B C   1 
ATOM 3043 O O   . PHE B 1 46  ? 137.173 172.654 103.887 1.00 125.61 ? 46   PHE B O   1 
ATOM 3044 C CB  . PHE B 1 46  ? 138.419 170.848 106.049 1.00 120.40 ? 46   PHE B CB  1 
ATOM 3045 C CG  . PHE B 1 46  ? 138.734 171.921 107.038 1.00 123.24 ? 46   PHE B CG  1 
ATOM 3046 C CD1 . PHE B 1 46  ? 139.807 172.764 106.840 1.00 128.04 ? 46   PHE B CD1 1 
ATOM 3047 C CD2 . PHE B 1 46  ? 137.965 172.081 108.174 1.00 123.02 ? 46   PHE B CD2 1 
ATOM 3048 C CE1 . PHE B 1 46  ? 140.102 173.752 107.762 1.00 129.76 ? 46   PHE B CE1 1 
ATOM 3049 C CE2 . PHE B 1 46  ? 138.259 173.068 109.090 1.00 126.35 ? 46   PHE B CE2 1 
ATOM 3050 C CZ  . PHE B 1 46  ? 139.336 173.900 108.879 1.00 130.22 ? 46   PHE B CZ  1 
ATOM 3051 N N   . VAL B 1 47  ? 135.866 173.034 105.689 1.00 121.44 ? 47   VAL B N   1 
ATOM 3052 C CA  . VAL B 1 47  ? 135.464 174.365 105.252 1.00 122.41 ? 47   VAL B CA  1 
ATOM 3053 C C   . VAL B 1 47  ? 135.836 175.408 106.294 1.00 125.21 ? 47   VAL B C   1 
ATOM 3054 O O   . VAL B 1 47  ? 136.666 176.285 106.036 1.00 129.46 ? 47   VAL B O   1 
ATOM 3055 C CB  . VAL B 1 47  ? 133.958 174.412 104.950 1.00 119.10 ? 47   VAL B CB  1 
ATOM 3056 C CG1 . VAL B 1 47  ? 133.501 175.846 104.767 1.00 121.89 ? 47   VAL B CG1 1 
ATOM 3057 C CG2 . VAL B 1 47  ? 133.652 173.597 103.710 1.00 120.56 ? 47   VAL B CG2 1 
ATOM 3058 N N   . ALA B 1 48  ? 135.249 175.311 107.482 1.00 123.06 ? 48   ALA B N   1 
ATOM 3059 C CA  . ALA B 1 48  ? 135.435 176.305 108.528 1.00 125.07 ? 48   ALA B CA  1 
ATOM 3060 C C   . ALA B 1 48  ? 136.155 175.677 109.710 1.00 122.48 ? 48   ALA B C   1 
ATOM 3061 O O   . ALA B 1 48  ? 135.775 174.597 110.172 1.00 118.78 ? 48   ALA B O   1 
ATOM 3062 C CB  . ALA B 1 48  ? 134.094 176.895 108.977 1.00 125.76 ? 48   ALA B CB  1 
ATOM 3063 N N   . GLY B 1 49  ? 137.196 176.352 110.189 1.00 124.71 ? 49   GLY B N   1 
ATOM 3064 C CA  . GLY B 1 49  ? 137.872 175.947 111.405 1.00 126.37 ? 49   GLY B CA  1 
ATOM 3065 C C   . GLY B 1 49  ? 138.144 177.130 112.311 1.00 128.39 ? 49   GLY B C   1 
ATOM 3066 O O   . GLY B 1 49  ? 138.879 178.048 111.935 1.00 129.70 ? 49   GLY B O   1 
ATOM 3067 N N   . ILE B 1 50  ? 137.563 177.119 113.509 1.00 128.17 ? 50   ILE B N   1 
ATOM 3068 C CA  . ILE B 1 50  ? 137.664 178.234 114.441 1.00 128.03 ? 50   ILE B CA  1 
ATOM 3069 C C   . ILE B 1 50  ? 138.025 177.698 115.818 1.00 127.87 ? 50   ILE B C   1 
ATOM 3070 O O   . ILE B 1 50  ? 137.840 176.514 116.113 1.00 126.23 ? 50   ILE B O   1 
ATOM 3071 C CB  . ILE B 1 50  ? 136.356 179.057 114.506 1.00 128.75 ? 50   ILE B CB  1 
ATOM 3072 C CG1 . ILE B 1 50  ? 135.163 178.156 114.837 1.00 125.86 ? 50   ILE B CG1 1 
ATOM 3073 C CG2 . ILE B 1 50  ? 136.128 179.801 113.200 1.00 130.12 ? 50   ILE B CG2 1 
ATOM 3074 C CD1 . ILE B 1 50  ? 133.863 178.910 115.034 1.00 124.52 ? 50   ILE B CD1 1 
ATOM 3075 N N   . GLY B 1 51  ? 138.547 178.581 116.662 1.00 128.91 ? 51   GLY B N   1 
ATOM 3076 C CA  . GLY B 1 51  ? 138.901 178.216 118.020 1.00 129.49 ? 51   GLY B CA  1 
ATOM 3077 C C   . GLY B 1 51  ? 137.691 178.064 118.919 1.00 128.24 ? 51   GLY B C   1 
ATOM 3078 O O   . GLY B 1 51  ? 136.564 178.340 118.508 1.00 126.11 ? 51   GLY B O   1 
ATOM 3079 N N   . THR B 1 55  ? 142.084 179.765 115.020 1.00 136.43 ? 55   THR B N   1 
ATOM 3080 C CA  . THR B 1 55  ? 142.266 180.649 113.872 1.00 137.24 ? 55   THR B CA  1 
ATOM 3081 C C   . THR B 1 55  ? 141.028 180.637 112.988 1.00 137.01 ? 55   THR B C   1 
ATOM 3082 O O   . THR B 1 55  ? 139.940 180.332 113.461 1.00 137.43 ? 55   THR B O   1 
ATOM 3083 C CB  . THR B 1 55  ? 143.496 180.256 113.039 1.00 135.96 ? 55   THR B CB  1 
ATOM 3084 O OG1 . THR B 1 55  ? 143.346 178.920 112.541 1.00 135.08 ? 55   THR B OG1 1 
ATOM 3085 C CG2 . THR B 1 55  ? 144.747 180.349 113.887 1.00 134.04 ? 55   THR B CG2 1 
ATOM 3086 N N   . THR B 1 56  ? 141.194 180.980 111.711 1.00 135.24 ? 56   THR B N   1 
ATOM 3087 C CA  . THR B 1 56  ? 140.084 181.029 110.765 1.00 135.17 ? 56   THR B CA  1 
ATOM 3088 C C   . THR B 1 56  ? 140.502 180.425 109.431 1.00 134.19 ? 56   THR B C   1 
ATOM 3089 O O   . THR B 1 56  ? 140.236 180.982 108.360 1.00 134.50 ? 56   THR B O   1 
ATOM 3090 C CB  . THR B 1 56  ? 139.582 182.460 110.589 1.00 135.52 ? 56   THR B CB  1 
ATOM 3091 O OG1 . THR B 1 56  ? 139.632 183.130 111.854 1.00 136.02 ? 56   THR B OG1 1 
ATOM 3092 C CG2 . THR B 1 56  ? 138.145 182.459 110.114 1.00 134.43 ? 56   THR B CG2 1 
ATOM 3093 N N   . ASN B 1 57  ? 141.165 179.276 109.479 1.00 131.97 ? 57   ASN B N   1 
ATOM 3094 C CA  . ASN B 1 57  ? 141.679 178.651 108.268 1.00 131.28 ? 57   ASN B CA  1 
ATOM 3095 C C   . ASN B 1 57  ? 140.505 178.097 107.478 1.00 131.57 ? 57   ASN B C   1 
ATOM 3096 O O   . ASN B 1 57  ? 140.072 176.963 107.690 1.00 132.69 ? 57   ASN B O   1 
ATOM 3097 C CB  . ASN B 1 57  ? 142.684 177.563 108.622 1.00 134.70 ? 57   ASN B CB  1 
ATOM 3098 C CG  . ASN B 1 57  ? 142.261 176.751 109.829 1.00 134.47 ? 57   ASN B CG  1 
ATOM 3099 O OD1 . ASN B 1 57  ? 141.101 176.779 110.237 1.00 134.47 ? 57   ASN B OD1 1 
ATOM 3100 N ND2 . ASN B 1 57  ? 143.208 176.027 110.411 1.00 133.36 ? 57   ASN B ND2 1 
ATOM 3101 N N   . TYR B 1 58  ? 139.992 178.896 106.550 1.00 132.52 ? 58   TYR B N   1 
ATOM 3102 C CA  . TYR B 1 58  ? 138.900 178.472 105.694 1.00 132.85 ? 58   TYR B CA  1 
ATOM 3103 C C   . TYR B 1 58  ? 139.440 177.791 104.437 1.00 132.85 ? 58   TYR B C   1 
ATOM 3104 O O   . TYR B 1 58  ? 140.637 177.814 104.144 1.00 135.01 ? 58   TYR B O   1 
ATOM 3105 C CB  . TYR B 1 58  ? 138.012 179.660 105.332 1.00 133.60 ? 58   TYR B CB  1 
ATOM 3106 C CG  . TYR B 1 58  ? 137.120 180.137 106.454 1.00 135.89 ? 58   TYR B CG  1 
ATOM 3107 C CD1 . TYR B 1 58  ? 136.920 179.367 107.590 1.00 134.38 ? 58   TYR B CD1 1 
ATOM 3108 C CD2 . TYR B 1 58  ? 136.466 181.356 106.369 1.00 138.60 ? 58   TYR B CD2 1 
ATOM 3109 C CE1 . TYR B 1 58  ? 136.097 179.804 108.613 1.00 135.87 ? 58   TYR B CE1 1 
ATOM 3110 C CE2 . TYR B 1 58  ? 135.640 181.801 107.387 1.00 138.86 ? 58   TYR B CE2 1 
ATOM 3111 C CZ  . TYR B 1 58  ? 135.458 181.021 108.506 1.00 138.79 ? 58   TYR B CZ  1 
ATOM 3112 O OH  . TYR B 1 58  ? 134.640 181.453 109.526 1.00 137.75 ? 58   TYR B OH  1 
ATOM 3113 N N   . ALA B 1 59  ? 138.536 177.189 103.675 1.00 131.46 ? 59   ALA B N   1 
ATOM 3114 C CA  . ALA B 1 59  ? 138.893 176.528 102.430 1.00 134.25 ? 59   ALA B CA  1 
ATOM 3115 C C   . ALA B 1 59  ? 139.056 177.581 101.334 1.00 138.11 ? 59   ALA B C   1 
ATOM 3116 O O   . ALA B 1 59  ? 139.164 178.781 101.599 1.00 138.23 ? 59   ALA B O   1 
ATOM 3117 C CB  . ALA B 1 59  ? 137.851 175.472 102.074 1.00 132.40 ? 59   ALA B CB  1 
ATOM 3118 N N   . ASP B 1 60  ? 139.090 177.137 100.085 1.00 137.68 ? 60   ASP B N   1 
ATOM 3119 C CA  . ASP B 1 60  ? 139.213 178.032 98.939  1.00 137.06 ? 60   ASP B CA  1 
ATOM 3120 C C   . ASP B 1 60  ? 137.966 178.880 98.701  1.00 138.23 ? 60   ASP B C   1 
ATOM 3121 O O   . ASP B 1 60  ? 137.915 179.582 97.685  1.00 136.96 ? 60   ASP B O   1 
ATOM 3122 C CB  . ASP B 1 60  ? 139.536 177.216 97.687  1.00 137.97 ? 60   ASP B CB  1 
ATOM 3123 C CG  . ASP B 1 60  ? 138.565 176.071 97.475  1.00 137.65 ? 60   ASP B CG  1 
ATOM 3124 O OD1 . ASP B 1 60  ? 138.018 175.559 98.475  1.00 135.02 ? 60   ASP B OD1 1 
ATOM 3125 O OD2 . ASP B 1 60  ? 138.350 175.682 96.308  1.00 137.74 ? 60   ASP B OD2 1 
ATOM 3126 N N   . SER B 1 61  ? 136.975 178.840 99.588  1.00 140.32 ? 61   SER B N   1 
ATOM 3127 C CA  . SER B 1 61  ? 135.758 179.626 99.463  1.00 139.88 ? 61   SER B CA  1 
ATOM 3128 C C   . SER B 1 61  ? 135.673 180.635 100.601 1.00 140.77 ? 61   SER B C   1 
ATOM 3129 O O   . SER B 1 61  ? 136.298 180.472 101.652 1.00 139.50 ? 61   SER B O   1 
ATOM 3130 C CB  . SER B 1 61  ? 134.517 178.726 99.463  1.00 137.80 ? 61   SER B CB  1 
ATOM 3131 O OG  . SER B 1 61  ? 134.509 177.872 100.594 1.00 134.95 ? 61   SER B OG  1 
ATOM 3132 N N   . VAL B 1 62  ? 134.887 181.689 100.379 1.00 142.23 ? 62   VAL B N   1 
ATOM 3133 C CA  . VAL B 1 62  ? 134.738 182.757 101.363 1.00 144.22 ? 62   VAL B CA  1 
ATOM 3134 C C   . VAL B 1 62  ? 133.919 182.255 102.544 1.00 145.67 ? 62   VAL B C   1 
ATOM 3135 O O   . VAL B 1 62  ? 134.420 182.175 103.672 1.00 144.77 ? 62   VAL B O   1 
ATOM 3136 C CB  . VAL B 1 62  ? 134.085 184.002 100.735 1.00 141.96 ? 62   VAL B CB  1 
ATOM 3137 C CG1 . VAL B 1 62  ? 134.028 185.139 101.744 1.00 138.90 ? 62   VAL B CG1 1 
ATOM 3138 C CG2 . VAL B 1 62  ? 134.840 184.422 99.485  1.00 141.27 ? 62   VAL B CG2 1 
ATOM 3139 N N   . LYS B 1 63  ? 132.657 181.912 102.285 1.00 147.75 ? 63   LYS B N   1 
ATOM 3140 C CA  . LYS B 1 63  ? 131.763 181.328 103.287 1.00 147.70 ? 63   LYS B CA  1 
ATOM 3141 C C   . LYS B 1 63  ? 131.657 182.195 104.538 1.00 147.36 ? 63   LYS B C   1 
ATOM 3142 O O   . LYS B 1 63  ? 131.528 181.686 105.653 1.00 146.40 ? 63   LYS B O   1 
ATOM 3143 C CB  . LYS B 1 63  ? 132.200 179.906 103.650 1.00 143.59 ? 63   LYS B CB  1 
ATOM 3144 C CG  . LYS B 1 63  ? 132.090 178.920 102.498 1.00 141.17 ? 63   LYS B CG  1 
ATOM 3145 C CD  . LYS B 1 63  ? 130.686 178.917 101.907 1.00 140.77 ? 63   LYS B CD  1 
ATOM 3146 C CE  . LYS B 1 63  ? 129.662 178.427 102.915 1.00 139.22 ? 63   LYS B CE  1 
ATOM 3147 N NZ  . LYS B 1 63  ? 128.268 178.669 102.457 1.00 139.77 ? 63   LYS B NZ  1 
ATOM 3148 N N   . GLY B 1 64  ? 131.700 183.513 104.360 1.00 147.81 ? 64   GLY B N   1 
ATOM 3149 C CA  . GLY B 1 64  ? 131.593 184.405 105.496 1.00 146.66 ? 64   GLY B CA  1 
ATOM 3150 C C   . GLY B 1 64  ? 132.767 184.245 106.444 1.00 146.62 ? 64   GLY B C   1 
ATOM 3151 O O   . GLY B 1 64  ? 133.882 183.884 106.050 1.00 146.42 ? 64   GLY B O   1 
ATOM 3152 N N   . ARG B 1 65  ? 132.509 184.517 107.722 1.00 144.68 ? 65   ARG B N   1 
ATOM 3153 C CA  . ARG B 1 65  ? 133.516 184.365 108.763 1.00 142.53 ? 65   ARG B CA  1 
ATOM 3154 C C   . ARG B 1 65  ? 132.814 184.276 110.111 1.00 141.15 ? 65   ARG B C   1 
ATOM 3155 O O   . ARG B 1 65  ? 131.684 184.745 110.274 1.00 142.51 ? 65   ARG B O   1 
ATOM 3156 C CB  . ARG B 1 65  ? 134.520 185.525 108.748 1.00 141.91 ? 65   ARG B CB  1 
ATOM 3157 C CG  . ARG B 1 65  ? 135.799 185.261 109.526 1.00 141.18 ? 65   ARG B CG  1 
ATOM 3158 C CD  . ARG B 1 65  ? 136.501 186.562 109.885 1.00 141.89 ? 65   ARG B CD  1 
ATOM 3159 N NE  . ARG B 1 65  ? 135.664 187.395 110.739 1.00 142.10 ? 65   ARG B NE  1 
ATOM 3160 C CZ  . ARG B 1 65  ? 135.999 188.599 111.181 1.00 140.72 ? 65   ARG B CZ  1 
ATOM 3161 N NH1 . ARG B 1 65  ? 137.159 189.152 110.868 1.00 139.26 ? 65   ARG B NH1 1 
ATOM 3162 N NH2 . ARG B 1 65  ? 135.148 189.264 111.956 1.00 137.96 ? 65   ARG B NH2 1 
ATOM 3163 N N   . PHE B 1 66  ? 133.497 183.665 111.074 1.00 137.49 ? 66   PHE B N   1 
ATOM 3164 C CA  . PHE B 1 66  ? 133.001 183.608 112.445 1.00 134.22 ? 66   PHE B CA  1 
ATOM 3165 C C   . PHE B 1 66  ? 133.429 184.846 113.226 1.00 136.14 ? 66   PHE B C   1 
ATOM 3166 O O   . PHE B 1 66  ? 132.592 185.584 113.745 1.00 134.60 ? 66   PHE B O   1 
ATOM 3167 C CB  . PHE B 1 66  ? 133.496 182.346 113.150 1.00 129.51 ? 66   PHE B CB  1 
ATOM 3168 C CG  . PHE B 1 66  ? 133.545 182.468 114.646 1.00 129.47 ? 66   PHE B CG  1 
ATOM 3169 C CD1 . PHE B 1 66  ? 132.381 182.573 115.387 1.00 130.15 ? 66   PHE B CD1 1 
ATOM 3170 C CD2 . PHE B 1 66  ? 134.759 182.469 115.311 1.00 130.18 ? 66   PHE B CD2 1 
ATOM 3171 C CE1 . PHE B 1 66  ? 132.430 182.687 116.763 1.00 130.04 ? 66   PHE B CE1 1 
ATOM 3172 C CE2 . PHE B 1 66  ? 134.812 182.579 116.684 1.00 129.75 ? 66   PHE B CE2 1 
ATOM 3173 C CZ  . PHE B 1 66  ? 133.646 182.688 117.411 1.00 129.36 ? 66   PHE B CZ  1 
ATOM 3174 N N   . LEU B 1 79  ? 125.008 181.696 108.792 1.00 143.46 ? 79   LEU B N   1 
ATOM 3175 C CA  . LEU B 1 79  ? 125.680 182.990 108.794 1.00 146.95 ? 79   LEU B CA  1 
ATOM 3176 C C   . LEU B 1 79  ? 126.678 183.072 107.641 1.00 149.09 ? 79   LEU B C   1 
ATOM 3177 O O   . LEU B 1 79  ? 127.317 184.102 107.419 1.00 149.22 ? 79   LEU B O   1 
ATOM 3178 C CB  . LEU B 1 79  ? 126.377 183.225 110.138 1.00 145.34 ? 79   LEU B CB  1 
ATOM 3179 C CG  . LEU B 1 79  ? 126.905 184.632 110.423 1.00 141.43 ? 79   LEU B CG  1 
ATOM 3180 C CD1 . LEU B 1 79  ? 125.859 185.671 110.062 1.00 138.28 ? 79   LEU B CD1 1 
ATOM 3181 C CD2 . LEU B 1 79  ? 127.315 184.766 111.881 1.00 139.57 ? 79   LEU B CD2 1 
ATOM 3182 N N   . GLN B 1 80  ? 126.792 181.976 106.895 1.00 149.05 ? 80   GLN B N   1 
ATOM 3183 C CA  . GLN B 1 80  ? 127.680 181.932 105.746 1.00 148.35 ? 80   GLN B CA  1 
ATOM 3184 C C   . GLN B 1 80  ? 127.113 182.797 104.619 1.00 148.10 ? 80   GLN B C   1 
ATOM 3185 O O   . GLN B 1 80  ? 126.070 183.442 104.755 1.00 148.01 ? 80   GLN B O   1 
ATOM 3186 C CB  . GLN B 1 80  ? 127.877 180.489 105.290 1.00 148.06 ? 80   GLN B CB  1 
ATOM 3187 C CG  . GLN B 1 80  ? 128.001 179.483 106.429 1.00 147.18 ? 80   GLN B CG  1 
ATOM 3188 C CD  . GLN B 1 80  ? 129.269 179.659 107.244 1.00 146.48 ? 80   GLN B CD  1 
ATOM 3189 O OE1 . GLN B 1 80  ? 130.370 179.377 106.770 1.00 145.17 ? 80   GLN B OE1 1 
ATOM 3190 N NE2 . GLN B 1 80  ? 129.119 180.121 108.481 1.00 144.49 ? 80   GLN B NE2 1 
ATOM 3191 N N   . MET B 1 81  ? 127.814 182.812 103.486 1.00 147.68 ? 81   MET B N   1 
ATOM 3192 C CA  . MET B 1 81  ? 127.370 183.599 102.342 1.00 149.33 ? 81   MET B CA  1 
ATOM 3193 C C   . MET B 1 81  ? 126.056 183.050 101.801 1.00 150.25 ? 81   MET B C   1 
ATOM 3194 O O   . MET B 1 81  ? 125.987 181.893 101.377 1.00 151.23 ? 81   MET B O   1 
ATOM 3195 C CB  . MET B 1 81  ? 128.435 183.612 101.243 1.00 148.79 ? 81   MET B CB  1 
ATOM 3196 C CG  . MET B 1 81  ? 128.483 184.910 100.447 1.00 148.71 ? 81   MET B CG  1 
ATOM 3197 S SD  . MET B 1 81  ? 129.538 184.820 98.992  1.00 147.06 ? 81   MET B SD  1 
ATOM 3198 C CE  . MET B 1 81  ? 128.534 183.821 97.904  1.00 146.91 ? 81   MET B CE  1 
ATOM 3199 N N   . ASN B 1 82  ? 125.011 183.876 101.809 1.00 149.55 ? 82   ASN B N   1 
ATOM 3200 C CA  . ASN B 1 82  ? 123.677 183.446 101.414 1.00 149.30 ? 82   ASN B CA  1 
ATOM 3201 C C   . ASN B 1 82  ? 123.439 183.530 99.912  1.00 149.49 ? 82   ASN B C   1 
ATOM 3202 O O   . ASN B 1 82  ? 122.327 183.234 99.462  1.00 148.42 ? 82   ASN B O   1 
ATOM 3203 C CB  . ASN B 1 82  ? 122.618 184.271 102.152 1.00 148.14 ? 82   ASN B CB  1 
ATOM 3204 C CG  . ASN B 1 82  ? 122.629 184.027 103.649 1.00 146.95 ? 82   ASN B CG  1 
ATOM 3205 O OD1 . ASN B 1 82  ? 122.726 184.963 104.442 1.00 146.42 ? 82   ASN B OD1 1 
ATOM 3206 N ND2 . ASN B 1 82  ? 122.530 182.763 104.043 1.00 145.29 ? 82   ASN B ND2 1 
ATOM 3207 N N   . SER B 1 83  ? 124.439 183.940 99.132  1.00 149.88 ? 83   SER B N   1 
ATOM 3208 C CA  . SER B 1 83  ? 124.350 183.940 97.679  1.00 148.93 ? 83   SER B CA  1 
ATOM 3209 C C   . SER B 1 83  ? 125.091 182.766 97.050  1.00 150.53 ? 83   SER B C   1 
ATOM 3210 O O   . SER B 1 83  ? 125.357 182.788 95.843  1.00 150.79 ? 83   SER B O   1 
ATOM 3211 C CB  . SER B 1 83  ? 124.880 185.261 97.116  1.00 146.15 ? 83   SER B CB  1 
ATOM 3212 O OG  . SER B 1 83  ? 124.805 185.281 95.702  1.00 142.86 ? 83   SER B OG  1 
ATOM 3213 N N   . LEU B 1 84  ? 125.433 181.751 97.841  1.00 149.71 ? 84   LEU B N   1 
ATOM 3214 C CA  . LEU B 1 84  ? 126.171 180.607 97.325  1.00 148.73 ? 84   LEU B CA  1 
ATOM 3215 C C   . LEU B 1 84  ? 125.338 179.846 96.300  1.00 151.23 ? 84   LEU B C   1 
ATOM 3216 O O   . LEU B 1 84  ? 124.106 179.814 96.365  1.00 151.63 ? 84   LEU B O   1 
ATOM 3217 C CB  . LEU B 1 84  ? 126.574 179.678 98.469  1.00 147.32 ? 84   LEU B CB  1 
ATOM 3218 C CG  . LEU B 1 84  ? 127.452 178.481 98.106  1.00 147.34 ? 84   LEU B CG  1 
ATOM 3219 C CD1 . LEU B 1 84  ? 128.813 178.937 97.596  1.00 146.22 ? 84   LEU B CD1 1 
ATOM 3220 C CD2 . LEU B 1 84  ? 127.600 177.555 99.298  1.00 145.44 ? 84   LEU B CD2 1 
ATOM 3221 N N   . LYS B 1 85  ? 126.029 179.235 95.341  1.00 150.23 ? 85   LYS B N   1 
ATOM 3222 C CA  . LYS B 1 85  ? 125.397 178.474 94.266  1.00 148.89 ? 85   LYS B CA  1 
ATOM 3223 C C   . LYS B 1 85  ? 124.444 177.402 94.792  1.00 147.75 ? 85   LYS B C   1 
ATOM 3224 O O   . LYS B 1 85  ? 124.575 176.939 95.925  1.00 148.20 ? 85   LYS B O   1 
ATOM 3225 C CB  . LYS B 1 85  ? 126.467 177.824 93.386  1.00 147.89 ? 85   LYS B CB  1 
ATOM 3226 C CG  . LYS B 1 85  ? 127.282 176.759 94.101  1.00 146.95 ? 85   LYS B CG  1 
ATOM 3227 C CD  . LYS B 1 85  ? 128.391 176.213 93.221  1.00 142.22 ? 85   LYS B CD  1 
ATOM 3228 C CE  . LYS B 1 85  ? 129.053 175.007 93.867  1.00 140.68 ? 85   LYS B CE  1 
ATOM 3229 N NZ  . LYS B 1 85  ? 129.500 175.294 95.257  1.00 139.46 ? 85   LYS B NZ  1 
ATOM 3230 N N   . VAL B 1 91  ? 125.301 169.252 103.436 1.00 124.91 ? 91   VAL B N   1 
ATOM 3231 C CA  . VAL B 1 91  ? 125.095 169.175 104.876 1.00 126.31 ? 91   VAL B CA  1 
ATOM 3232 C C   . VAL B 1 91  ? 126.391 169.517 105.600 1.00 124.86 ? 91   VAL B C   1 
ATOM 3233 O O   . VAL B 1 91  ? 127.462 169.036 105.234 1.00 124.33 ? 91   VAL B O   1 
ATOM 3234 C CB  . VAL B 1 91  ? 124.569 167.786 105.290 1.00 126.62 ? 91   VAL B CB  1 
ATOM 3235 C CG1 . VAL B 1 91  ? 125.442 166.685 104.709 1.00 124.40 ? 91   VAL B CG1 1 
ATOM 3236 C CG2 . VAL B 1 91  ? 124.487 167.672 106.804 1.00 124.82 ? 91   VAL B CG2 1 
ATOM 3237 N N   . TYR B 1 92  ? 126.290 170.360 106.623 1.00 123.32 ? 92   TYR B N   1 
ATOM 3238 C CA  . TYR B 1 92  ? 127.445 170.838 107.370 1.00 120.34 ? 92   TYR B CA  1 
ATOM 3239 C C   . TYR B 1 92  ? 127.445 170.216 108.757 1.00 119.42 ? 92   TYR B C   1 
ATOM 3240 O O   . TYR B 1 92  ? 126.422 170.233 109.450 1.00 120.67 ? 92   TYR B O   1 
ATOM 3241 C CB  . TYR B 1 92  ? 127.437 172.364 107.467 1.00 120.36 ? 92   TYR B CB  1 
ATOM 3242 C CG  . TYR B 1 92  ? 127.411 173.058 106.125 1.00 122.24 ? 92   TYR B CG  1 
ATOM 3243 C CD1 . TYR B 1 92  ? 127.898 172.431 104.986 1.00 121.67 ? 92   TYR B CD1 1 
ATOM 3244 C CD2 . TYR B 1 92  ? 126.900 174.340 105.997 1.00 124.70 ? 92   TYR B CD2 1 
ATOM 3245 C CE1 . TYR B 1 92  ? 127.873 173.057 103.762 1.00 121.81 ? 92   TYR B CE1 1 
ATOM 3246 C CE2 . TYR B 1 92  ? 126.874 174.976 104.774 1.00 128.74 ? 92   TYR B CE2 1 
ATOM 3247 C CZ  . TYR B 1 92  ? 127.362 174.329 103.661 1.00 126.11 ? 92   TYR B CZ  1 
ATOM 3248 O OH  . TYR B 1 92  ? 127.338 174.957 102.439 1.00 129.25 ? 92   TYR B OH  1 
ATOM 3249 N N   . TYR B 1 93  ? 128.591 169.673 109.159 1.00 116.68 ? 93   TYR B N   1 
ATOM 3250 C CA  . TYR B 1 93  ? 128.736 168.975 110.429 1.00 115.99 ? 93   TYR B CA  1 
ATOM 3251 C C   . TYR B 1 93  ? 129.615 169.785 111.370 1.00 116.60 ? 93   TYR B C   1 
ATOM 3252 O O   . TYR B 1 93  ? 130.674 170.278 110.969 1.00 118.53 ? 93   TYR B O   1 
ATOM 3253 C CB  . TYR B 1 93  ? 129.328 167.581 110.220 1.00 115.24 ? 93   TYR B CB  1 
ATOM 3254 C CG  . TYR B 1 93  ? 128.455 166.670 109.389 1.00 122.23 ? 93   TYR B CG  1 
ATOM 3255 C CD1 . TYR B 1 93  ? 127.379 166.003 109.958 1.00 123.57 ? 93   TYR B CD1 1 
ATOM 3256 C CD2 . TYR B 1 93  ? 128.707 166.476 108.039 1.00 123.83 ? 93   TYR B CD2 1 
ATOM 3257 C CE1 . TYR B 1 93  ? 126.579 165.171 109.206 1.00 123.73 ? 93   TYR B CE1 1 
ATOM 3258 C CE2 . TYR B 1 93  ? 127.912 165.645 107.279 1.00 125.53 ? 93   TYR B CE2 1 
ATOM 3259 C CZ  . TYR B 1 93  ? 126.850 164.995 107.868 1.00 126.52 ? 93   TYR B CZ  1 
ATOM 3260 O OH  . TYR B 1 93  ? 126.054 164.165 107.115 1.00 129.07 ? 93   TYR B OH  1 
ATOM 3261 N N   . CYS B 1 94  ? 129.172 169.920 112.617 1.00 114.77 ? 94   CYS B N   1 
ATOM 3262 C CA  . CYS B 1 94  ? 129.920 170.649 113.633 1.00 113.03 ? 94   CYS B CA  1 
ATOM 3263 C C   . CYS B 1 94  ? 130.906 169.693 114.292 1.00 111.17 ? 94   CYS B C   1 
ATOM 3264 O O   . CYS B 1 94  ? 130.503 168.778 115.015 1.00 111.75 ? 94   CYS B O   1 
ATOM 3265 C CB  . CYS B 1 94  ? 128.967 171.257 114.656 1.00 115.45 ? 94   CYS B CB  1 
ATOM 3266 S SG  . CYS B 1 94  ? 129.775 172.114 116.021 1.00 126.03 ? 94   CYS B SG  1 
ATOM 3267 N N   . ALA B 1 95  ? 132.197 169.909 114.057 1.00 109.98 ? 95   ALA B N   1 
ATOM 3268 C CA  . ALA B 1 95  ? 133.251 169.018 114.527 1.00 104.48 ? 95   ALA B CA  1 
ATOM 3269 C C   . ALA B 1 95  ? 133.938 169.625 115.741 1.00 103.08 ? 95   ALA B C   1 
ATOM 3270 O O   . ALA B 1 95  ? 134.452 170.746 115.671 1.00 108.14 ? 95   ALA B O   1 
ATOM 3271 C CB  . ALA B 1 95  ? 134.271 168.754 113.422 1.00 105.80 ? 95   ALA B CB  1 
ATOM 3272 N N   . ALA B 1 96  ? 133.974 168.871 116.833 1.00 97.80  ? 96   ALA B N   1 
ATOM 3273 C CA  . ALA B 1 96  ? 134.600 169.292 118.081 1.00 102.83 ? 96   ALA B CA  1 
ATOM 3274 C C   . ALA B 1 96  ? 135.814 168.398 118.320 1.00 102.10 ? 96   ALA B C   1 
ATOM 3275 O O   . ALA B 1 96  ? 135.716 167.352 118.962 1.00 103.24 ? 96   ALA B O   1 
ATOM 3276 C CB  . ALA B 1 96  ? 133.611 169.214 119.234 1.00 106.65 ? 96   ALA B CB  1 
ATOM 3277 N N   . TYR B 1 97  ? 136.964 168.826 117.808 1.00 103.61 ? 97   TYR B N   1 
ATOM 3278 C CA  . TYR B 1 97  ? 138.195 168.050 117.860 1.00 104.25 ? 97   TYR B CA  1 
ATOM 3279 C C   . TYR B 1 97  ? 139.291 168.854 118.543 1.00 110.25 ? 97   TYR B C   1 
ATOM 3280 O O   . TYR B 1 97  ? 139.402 170.066 118.339 1.00 112.49 ? 97   TYR B O   1 
ATOM 3281 C CB  . TYR B 1 97  ? 138.650 167.643 116.453 1.00 104.28 ? 97   TYR B CB  1 
ATOM 3282 C CG  . TYR B 1 97  ? 138.793 168.803 115.494 1.00 106.37 ? 97   TYR B CG  1 
ATOM 3283 C CD1 . TYR B 1 97  ? 139.994 169.487 115.372 1.00 108.27 ? 97   TYR B CD1 1 
ATOM 3284 C CD2 . TYR B 1 97  ? 137.724 169.215 114.713 1.00 107.25 ? 97   TYR B CD2 1 
ATOM 3285 C CE1 . TYR B 1 97  ? 140.125 170.547 114.504 1.00 113.07 ? 97   TYR B CE1 1 
ATOM 3286 C CE2 . TYR B 1 97  ? 137.846 170.274 113.841 1.00 110.43 ? 97   TYR B CE2 1 
ATOM 3287 C CZ  . TYR B 1 97  ? 139.048 170.938 113.741 1.00 115.69 ? 97   TYR B CZ  1 
ATOM 3288 O OH  . TYR B 1 97  ? 139.178 171.997 112.874 1.00 121.39 ? 97   TYR B OH  1 
ATOM 3289 N N   . ASN B 1 98  ? 140.095 168.176 119.355 1.00 111.88 ? 98   ASN B N   1 
ATOM 3290 C CA  . ASN B 1 98  ? 141.220 168.832 119.999 1.00 118.28 ? 98   ASN B CA  1 
ATOM 3291 C C   . ASN B 1 98  ? 142.315 169.143 118.982 1.00 119.51 ? 98   ASN B C   1 
ATOM 3292 O O   . ASN B 1 98  ? 142.435 168.498 117.937 1.00 118.84 ? 98   ASN B O   1 
ATOM 3293 C CB  . ASN B 1 98  ? 141.773 167.965 121.128 1.00 117.33 ? 98   ASN B CB  1 
ATOM 3294 C CG  . ASN B 1 98  ? 141.853 166.502 120.751 1.00 114.60 ? 98   ASN B CG  1 
ATOM 3295 O OD1 . ASN B 1 98  ? 141.823 166.149 119.573 1.00 112.32 ? 98   ASN B OD1 1 
ATOM 3296 N ND2 . ASN B 1 98  ? 141.950 165.639 121.754 1.00 114.69 ? 98   ASN B ND2 1 
ATOM 3297 N N   . TYR B 1 99  ? 143.121 170.157 119.304 1.00 120.89 ? 99   TYR B N   1 
ATOM 3298 C CA  . TYR B 1 99  ? 144.142 170.627 118.372 1.00 120.45 ? 99   TYR B CA  1 
ATOM 3299 C C   . TYR B 1 99  ? 145.180 169.545 118.096 1.00 119.29 ? 99   TYR B C   1 
ATOM 3300 O O   . TYR B 1 99  ? 145.545 169.298 116.941 1.00 118.01 ? 99   TYR B O   1 
ATOM 3301 C CB  . TYR B 1 99  ? 144.810 171.886 118.927 1.00 124.79 ? 99   TYR B CB  1 
ATOM 3302 C CG  . TYR B 1 99  ? 143.847 172.864 119.564 1.00 130.28 ? 99   TYR B CG  1 
ATOM 3303 C CD1 . TYR B 1 99  ? 143.540 172.785 120.916 1.00 130.02 ? 99   TYR B CD1 1 
ATOM 3304 C CD2 . TYR B 1 99  ? 143.251 173.870 118.816 1.00 131.12 ? 99   TYR B CD2 1 
ATOM 3305 C CE1 . TYR B 1 99  ? 142.660 173.674 121.503 1.00 132.74 ? 99   TYR B CE1 1 
ATOM 3306 C CE2 . TYR B 1 99  ? 142.371 174.765 119.395 1.00 131.56 ? 99   TYR B CE2 1 
ATOM 3307 C CZ  . TYR B 1 99  ? 142.080 174.661 120.738 1.00 133.45 ? 99   TYR B CZ  1 
ATOM 3308 O OH  . TYR B 1 99  ? 141.205 175.549 121.320 1.00 132.21 ? 99   TYR B OH  1 
ATOM 3309 N N   . PHE B 1 100 ? 145.665 168.889 119.145 1.00 119.35 ? 100  PHE B N   1 
ATOM 3310 C CA  . PHE B 1 100 ? 146.662 167.838 119.033 1.00 118.47 ? 100  PHE B CA  1 
ATOM 3311 C C   . PHE B 1 100 ? 146.240 166.631 119.855 1.00 117.93 ? 100  PHE B C   1 
ATOM 3312 O O   . PHE B 1 100 ? 145.544 166.776 120.866 1.00 116.75 ? 100  PHE B O   1 
ATOM 3313 C CB  . PHE B 1 100 ? 148.040 168.322 119.510 1.00 120.88 ? 100  PHE B CB  1 
ATOM 3314 C CG  . PHE B 1 100 ? 148.832 169.039 118.454 1.00 123.31 ? 100  PHE B CG  1 
ATOM 3315 C CD1 . PHE B 1 100 ? 149.578 168.327 117.528 1.00 120.25 ? 100  PHE B CD1 1 
ATOM 3316 C CD2 . PHE B 1 100 ? 148.838 170.423 118.390 1.00 123.28 ? 100  PHE B CD2 1 
ATOM 3317 C CE1 . PHE B 1 100 ? 150.310 168.980 116.557 1.00 120.73 ? 100  PHE B CE1 1 
ATOM 3318 C CE2 . PHE B 1 100 ? 149.569 171.082 117.420 1.00 119.50 ? 100  PHE B CE2 1 
ATOM 3319 C CZ  . PHE B 1 100 ? 150.306 170.359 116.503 1.00 120.57 ? 100  PHE B CZ  1 
ATOM 3320 N N   . PRO B 1 101 ? 146.646 165.428 119.448 1.00 118.14 ? 101  PRO B N   1 
ATOM 3321 C CA  . PRO B 1 101 ? 146.303 164.233 120.232 1.00 114.10 ? 101  PRO B CA  1 
ATOM 3322 C C   . PRO B 1 101 ? 147.008 164.255 121.580 1.00 115.06 ? 101  PRO B C   1 
ATOM 3323 O O   . PRO B 1 101 ? 148.228 164.416 121.655 1.00 114.59 ? 101  PRO B O   1 
ATOM 3324 C CB  . PRO B 1 101 ? 146.797 163.073 119.359 1.00 109.68 ? 101  PRO B CB  1 
ATOM 3325 C CG  . PRO B 1 101 ? 147.026 163.661 118.003 1.00 109.84 ? 101  PRO B CG  1 
ATOM 3326 C CD  . PRO B 1 101 ? 147.384 165.092 118.221 1.00 115.37 ? 101  PRO B CD  1 
ATOM 3327 N N   . ARG B 1 102 ? 146.226 164.099 122.649 1.00 114.92 ? 102  ARG B N   1 
ATOM 3328 C CA  . ARG B 1 102 ? 146.809 164.055 123.985 1.00 116.98 ? 102  ARG B CA  1 
ATOM 3329 C C   . ARG B 1 102 ? 147.741 162.860 124.129 1.00 117.15 ? 102  ARG B C   1 
ATOM 3330 O O   . ARG B 1 102 ? 148.856 162.983 124.647 1.00 118.06 ? 102  ARG B O   1 
ATOM 3331 C CB  . ARG B 1 102 ? 145.703 164.015 125.038 1.00 118.42 ? 102  ARG B CB  1 
ATOM 3332 C CG  . ARG B 1 102 ? 144.770 165.208 124.981 1.00 121.64 ? 102  ARG B CG  1 
ATOM 3333 C CD  . ARG B 1 102 ? 143.798 165.207 126.141 1.00 122.86 ? 102  ARG B CD  1 
ATOM 3334 N NE  . ARG B 1 102 ? 142.919 166.368 126.104 1.00 126.65 ? 102  ARG B NE  1 
ATOM 3335 C CZ  . ARG B 1 102 ? 141.982 166.624 127.006 1.00 129.93 ? 102  ARG B CZ  1 
ATOM 3336 N NH1 . ARG B 1 102 ? 141.775 165.818 128.034 1.00 128.07 ? 102  ARG B NH1 1 
ATOM 3337 N NH2 . ARG B 1 102 ? 141.236 167.717 126.874 1.00 132.09 ? 102  ARG B NH2 1 
ATOM 3338 N N   . SER B 1 103 ? 147.302 161.694 123.659 1.00 115.98 ? 103  SER B N   1 
ATOM 3339 C CA  . SER B 1 103 ? 148.146 160.507 123.623 1.00 114.42 ? 103  SER B CA  1 
ATOM 3340 C C   . SER B 1 103 ? 148.042 159.865 122.248 1.00 112.35 ? 103  SER B C   1 
ATOM 3341 O O   . SER B 1 103 ? 147.461 160.452 121.330 1.00 112.44 ? 103  SER B O   1 
ATOM 3342 C CB  . SER B 1 103 ? 147.744 159.514 124.715 1.00 110.01 ? 103  SER B CB  1 
ATOM 3343 O OG  . SER B 1 103 ? 146.466 158.962 124.458 1.00 108.97 ? 103  SER B OG  1 
ATOM 3344 N N   . ILE B 1 104 ? 148.607 158.667 122.091 1.00 110.52 ? 104  ILE B N   1 
ATOM 3345 C CA  . ILE B 1 104 ? 148.475 157.962 120.821 1.00 108.18 ? 104  ILE B CA  1 
ATOM 3346 C C   . ILE B 1 104 ? 147.021 157.592 120.565 1.00 107.96 ? 104  ILE B C   1 
ATOM 3347 O O   . ILE B 1 104 ? 146.587 157.507 119.410 1.00 105.03 ? 104  ILE B O   1 
ATOM 3348 C CB  . ILE B 1 104 ? 149.388 156.723 120.798 1.00 106.19 ? 104  ILE B CB  1 
ATOM 3349 C CG1 . ILE B 1 104 ? 148.927 155.692 121.829 1.00 102.94 ? 104  ILE B CG1 1 
ATOM 3350 C CG2 . ILE B 1 104 ? 150.825 157.120 121.073 1.00 109.50 ? 104  ILE B CG2 1 
ATOM 3351 C CD1 . ILE B 1 104 ? 149.836 154.494 121.940 1.00 99.38  ? 104  ILE B CD1 1 
ATOM 3352 N N   . VAL B 1 105 ? 146.245 157.386 121.624 1.00 110.00 ? 105  VAL B N   1 
ATOM 3353 C CA  . VAL B 1 105 ? 144.877 156.904 121.515 1.00 107.69 ? 105  VAL B CA  1 
ATOM 3354 C C   . VAL B 1 105 ? 143.865 158.027 121.709 1.00 105.31 ? 105  VAL B C   1 
ATOM 3355 O O   . VAL B 1 105 ? 142.866 158.093 120.992 1.00 101.37 ? 105  VAL B O   1 
ATOM 3356 C CB  . VAL B 1 105 ? 144.655 155.760 122.529 1.00 106.11 ? 105  VAL B CB  1 
ATOM 3357 C CG1 . VAL B 1 105 ? 143.179 155.503 122.755 1.00 105.83 ? 105  VAL B CG1 1 
ATOM 3358 C CG2 . VAL B 1 105 ? 145.348 154.494 122.052 1.00 97.08  ? 105  VAL B CG2 1 
ATOM 3359 N N   . TYR B 1 106 ? 144.117 158.927 122.654 1.00 106.09 ? 106  TYR B N   1 
ATOM 3360 C CA  . TYR B 1 106 ? 143.143 159.946 123.038 1.00 106.75 ? 106  TYR B CA  1 
ATOM 3361 C C   . TYR B 1 106 ? 143.063 161.017 121.957 1.00 109.28 ? 106  TYR B C   1 
ATOM 3362 O O   . TYR B 1 106 ? 143.872 161.945 121.920 1.00 113.66 ? 106  TYR B O   1 
ATOM 3363 C CB  . TYR B 1 106 ? 143.521 160.556 124.382 1.00 108.96 ? 106  TYR B CB  1 
ATOM 3364 C CG  . TYR B 1 106 ? 142.399 161.315 125.057 1.00 111.84 ? 106  TYR B CG  1 
ATOM 3365 C CD1 . TYR B 1 106 ? 141.985 162.554 124.584 1.00 115.42 ? 106  TYR B CD1 1 
ATOM 3366 C CD2 . TYR B 1 106 ? 141.761 160.798 126.176 1.00 112.22 ? 106  TYR B CD2 1 
ATOM 3367 C CE1 . TYR B 1 106 ? 140.963 163.251 125.200 1.00 116.21 ? 106  TYR B CE1 1 
ATOM 3368 C CE2 . TYR B 1 106 ? 140.739 161.489 126.798 1.00 114.18 ? 106  TYR B CE2 1 
ATOM 3369 C CZ  . TYR B 1 106 ? 140.345 162.715 126.306 1.00 115.37 ? 106  TYR B CZ  1 
ATOM 3370 O OH  . TYR B 1 106 ? 139.329 163.408 126.921 1.00 113.84 ? 106  TYR B OH  1 
ATOM 3371 N N   . TYR B 1 107 ? 142.075 160.890 121.073 1.00 103.05 ? 107  TYR B N   1 
ATOM 3372 C CA  . TYR B 1 107 ? 141.746 161.943 120.115 1.00 96.17  ? 107  TYR B CA  1 
ATOM 3373 C C   . TYR B 1 107 ? 140.299 161.715 119.707 1.00 94.43  ? 107  TYR B C   1 
ATOM 3374 O O   . TYR B 1 107 ? 139.994 160.706 119.065 1.00 95.91  ? 107  TYR B O   1 
ATOM 3375 C CB  . TYR B 1 107 ? 142.671 161.908 118.906 1.00 96.11  ? 107  TYR B CB  1 
ATOM 3376 C CG  . TYR B 1 107 ? 142.580 163.136 118.022 1.00 100.05 ? 107  TYR B CG  1 
ATOM 3377 C CD1 . TYR B 1 107 ? 141.442 163.401 117.276 1.00 95.88  ? 107  TYR B CD1 1 
ATOM 3378 C CD2 . TYR B 1 107 ? 143.638 164.025 117.927 1.00 105.81 ? 107  TYR B CD2 1 
ATOM 3379 C CE1 . TYR B 1 107 ? 141.358 164.516 116.469 1.00 97.15  ? 107  TYR B CE1 1 
ATOM 3380 C CE2 . TYR B 1 107 ? 143.565 165.142 117.120 1.00 105.79 ? 107  TYR B CE2 1 
ATOM 3381 C CZ  . TYR B 1 107 ? 142.422 165.382 116.395 1.00 100.74 ? 107  TYR B CZ  1 
ATOM 3382 O OH  . TYR B 1 107 ? 142.343 166.494 115.591 1.00 105.11 ? 107  TYR B OH  1 
ATOM 3383 N N   . TYR B 1 108 ? 139.419 162.642 120.067 1.00 90.72  ? 108  TYR B N   1 
ATOM 3384 C CA  . TYR B 1 108 ? 137.991 162.468 119.863 1.00 85.44  ? 108  TYR B CA  1 
ATOM 3385 C C   . TYR B 1 108 ? 137.446 163.549 118.943 1.00 85.00  ? 108  TYR B C   1 
ATOM 3386 O O   . TYR B 1 108 ? 137.967 164.664 118.889 1.00 95.32  ? 108  TYR B O   1 
ATOM 3387 C CB  . TYR B 1 108 ? 137.244 162.489 121.196 1.00 89.46  ? 108  TYR B CB  1 
ATOM 3388 C CG  . TYR B 1 108 ? 137.678 161.396 122.140 1.00 93.34  ? 108  TYR B CG  1 
ATOM 3389 C CD1 . TYR B 1 108 ? 138.750 161.581 122.999 1.00 99.67  ? 108  TYR B CD1 1 
ATOM 3390 C CD2 . TYR B 1 108 ? 137.020 160.176 122.170 1.00 92.38  ? 108  TYR B CD2 1 
ATOM 3391 C CE1 . TYR B 1 108 ? 139.153 160.586 123.861 1.00 101.43 ? 108  TYR B CE1 1 
ATOM 3392 C CE2 . TYR B 1 108 ? 137.416 159.173 123.029 1.00 96.34  ? 108  TYR B CE2 1 
ATOM 3393 C CZ  . TYR B 1 108 ? 138.484 159.385 123.873 1.00 102.33 ? 108  TYR B CZ  1 
ATOM 3394 O OH  . TYR B 1 108 ? 138.886 158.390 124.734 1.00 107.70 ? 108  TYR B OH  1 
ATOM 3395 N N   . VAL B 1 109 ? 136.401 163.195 118.202 1.00 77.42  ? 109  VAL B N   1 
ATOM 3396 C CA  . VAL B 1 109 ? 135.675 164.120 117.344 1.00 79.34  ? 109  VAL B CA  1 
ATOM 3397 C C   . VAL B 1 109 ? 134.189 163.917 117.597 1.00 85.66  ? 109  VAL B C   1 
ATOM 3398 O O   . VAL B 1 109 ? 133.715 162.777 117.638 1.00 88.20  ? 109  VAL B O   1 
ATOM 3399 C CB  . VAL B 1 109 ? 136.012 163.907 115.858 1.00 81.49  ? 109  VAL B CB  1 
ATOM 3400 C CG1 . VAL B 1 109 ? 135.072 164.704 114.978 1.00 91.70  ? 109  VAL B CG1 1 
ATOM 3401 C CG2 . VAL B 1 109 ? 137.449 164.296 115.585 1.00 80.89  ? 109  VAL B CG2 1 
ATOM 3402 N N   . TYR B 1 110 ? 133.457 165.015 117.778 1.00 90.84  ? 110  TYR B N   1 
ATOM 3403 C CA  . TYR B 1 110 ? 132.049 164.927 118.147 1.00 94.23  ? 110  TYR B CA  1 
ATOM 3404 C C   . TYR B 1 110 ? 131.128 164.802 116.940 1.00 96.85  ? 110  TYR B C   1 
ATOM 3405 O O   . TYR B 1 110 ? 130.116 164.099 117.011 1.00 101.46 ? 110  TYR B O   1 
ATOM 3406 C CB  . TYR B 1 110 ? 131.646 166.150 118.976 1.00 99.70  ? 110  TYR B CB  1 
ATOM 3407 C CG  . TYR B 1 110 ? 130.326 165.999 119.700 1.00 104.01 ? 110  TYR B CG  1 
ATOM 3408 C CD1 . TYR B 1 110 ? 129.124 166.282 119.065 1.00 107.12 ? 110  TYR B CD1 1 
ATOM 3409 C CD2 . TYR B 1 110 ? 130.283 165.582 121.021 1.00 102.52 ? 110  TYR B CD2 1 
ATOM 3410 C CE1 . TYR B 1 110 ? 127.919 166.143 119.722 1.00 108.80 ? 110  TYR B CE1 1 
ATOM 3411 C CE2 . TYR B 1 110 ? 129.083 165.442 121.686 1.00 106.26 ? 110  TYR B CE2 1 
ATOM 3412 C CZ  . TYR B 1 110 ? 127.904 165.724 121.032 1.00 109.42 ? 110  TYR B CZ  1 
ATOM 3413 O OH  . TYR B 1 110 ? 126.705 165.585 121.693 1.00 110.26 ? 110  TYR B OH  1 
ATOM 3414 N N   . TRP B 1 111 ? 131.451 165.478 115.839 1.00 98.00  ? 111  TRP B N   1 
ATOM 3415 C CA  . TRP B 1 111 ? 130.582 165.532 114.667 1.00 105.50 ? 111  TRP B CA  1 
ATOM 3416 C C   . TRP B 1 111 ? 129.149 165.901 115.033 1.00 107.51 ? 111  TRP B C   1 
ATOM 3417 O O   . TRP B 1 111 ? 128.915 166.697 115.947 1.00 108.12 ? 111  TRP B O   1 
ATOM 3418 C CB  . TRP B 1 111 ? 130.594 164.205 113.909 1.00 100.78 ? 111  TRP B CB  1 
ATOM 3419 C CG  . TRP B 1 111 ? 131.837 163.959 113.118 1.00 100.62 ? 111  TRP B CG  1 
ATOM 3420 C CD1 . TRP B 1 111 ? 132.585 162.824 113.113 1.00 98.24  ? 111  TRP B CD1 1 
ATOM 3421 C CD2 . TRP B 1 111 ? 132.479 164.866 112.213 1.00 104.71 ? 111  TRP B CD2 1 
ATOM 3422 N NE1 . TRP B 1 111 ? 133.649 162.962 112.260 1.00 99.31  ? 111  TRP B NE1 1 
ATOM 3423 C CE2 . TRP B 1 111 ? 133.608 164.209 111.698 1.00 102.46 ? 111  TRP B CE2 1 
ATOM 3424 C CE3 . TRP B 1 111 ? 132.206 166.169 111.786 1.00 108.08 ? 111  TRP B CE3 1 
ATOM 3425 C CZ2 . TRP B 1 111 ? 134.462 164.805 110.783 1.00 103.33 ? 111  TRP B CZ2 1 
ATOM 3426 C CZ3 . TRP B 1 111 ? 133.053 166.756 110.874 1.00 109.06 ? 111  TRP B CZ3 1 
ATOM 3427 C CH2 . TRP B 1 111 ? 134.171 166.079 110.387 1.00 106.95 ? 111  TRP B CH2 1 
ATOM 3428 N N   . GLY B 1 112 ? 128.189 165.322 114.327 1.00 108.80 ? 112  GLY B N   1 
ATOM 3429 C CA  . GLY B 1 112 ? 126.801 165.632 114.566 1.00 113.50 ? 112  GLY B CA  1 
ATOM 3430 C C   . GLY B 1 112 ? 126.401 166.970 113.977 1.00 117.31 ? 112  GLY B C   1 
ATOM 3431 O O   . GLY B 1 112 ? 127.095 167.562 113.146 1.00 118.94 ? 112  GLY B O   1 
ATOM 3432 N N   . GLN B 1 113 ? 125.243 167.449 114.433 1.00 119.90 ? 113  GLN B N   1 
ATOM 3433 C CA  . GLN B 1 113 ? 124.683 168.726 113.992 1.00 122.82 ? 113  GLN B CA  1 
ATOM 3434 C C   . GLN B 1 113 ? 124.537 168.771 112.471 1.00 123.16 ? 113  GLN B C   1 
ATOM 3435 O O   . GLN B 1 113 ? 124.903 169.749 111.816 1.00 123.94 ? 113  GLN B O   1 
ATOM 3436 C CB  . GLN B 1 113 ? 125.525 169.901 114.498 1.00 119.38 ? 113  GLN B CB  1 
ATOM 3437 C CG  . GLN B 1 113 ? 125.677 169.959 116.010 1.00 117.17 ? 113  GLN B CG  1 
ATOM 3438 C CD  . GLN B 1 113 ? 124.382 170.302 116.720 1.00 120.44 ? 113  GLN B CD  1 
ATOM 3439 O OE1 . GLN B 1 113 ? 123.425 170.773 116.103 1.00 121.54 ? 113  GLN B OE1 1 
ATOM 3440 N NE2 . GLN B 1 113 ? 124.345 170.069 118.027 1.00 118.82 ? 113  GLN B NE2 1 
ATOM 3441 N N   . GLY B 1 114 ? 124.001 167.691 111.907 1.00 121.33 ? 114  GLY B N   1 
ATOM 3442 C CA  . GLY B 1 114 ? 123.768 167.634 110.477 1.00 124.15 ? 114  GLY B CA  1 
ATOM 3443 C C   . GLY B 1 114 ? 122.672 168.579 110.032 1.00 128.70 ? 114  GLY B C   1 
ATOM 3444 O O   . GLY B 1 114 ? 121.492 168.343 110.309 1.00 128.19 ? 114  GLY B O   1 
ATOM 3445 N N   . THR B 1 115 ? 123.048 169.655 109.339 1.00 129.55 ? 115  THR B N   1 
ATOM 3446 C CA  . THR B 1 115 ? 122.107 170.704 108.939 1.00 128.95 ? 115  THR B CA  1 
ATOM 3447 C C   . THR B 1 115 ? 122.443 171.136 107.515 1.00 127.77 ? 115  THR B C   1 
ATOM 3448 O O   . THR B 1 115 ? 123.338 171.961 107.307 1.00 126.49 ? 115  THR B O   1 
ATOM 3449 C CB  . THR B 1 115 ? 122.158 171.891 109.897 1.00 126.17 ? 115  THR B CB  1 
ATOM 3450 O OG1 . THR B 1 115 ? 123.524 172.246 110.146 1.00 125.55 ? 115  THR B OG1 1 
ATOM 3451 C CG2 . THR B 1 115 ? 121.468 171.555 111.215 1.00 123.11 ? 115  THR B CG2 1 
ATOM 3452 N N   . GLN B 1 116 ? 121.723 170.583 106.544 1.00 128.00 ? 116  GLN B N   1 
ATOM 3453 C CA  . GLN B 1 116 ? 121.907 170.979 105.156 1.00 127.52 ? 116  GLN B CA  1 
ATOM 3454 C C   . GLN B 1 116 ? 121.434 172.411 104.943 1.00 129.80 ? 116  GLN B C   1 
ATOM 3455 O O   . GLN B 1 116 ? 120.409 172.832 105.486 1.00 130.21 ? 116  GLN B O   1 
ATOM 3456 C CB  . GLN B 1 116 ? 121.152 170.025 104.227 1.00 126.44 ? 116  GLN B CB  1 
ATOM 3457 C CG  . GLN B 1 116 ? 120.939 170.541 102.807 1.00 127.30 ? 116  GLN B CG  1 
ATOM 3458 C CD  . GLN B 1 116 ? 122.233 170.722 102.034 1.00 127.83 ? 116  GLN B CD  1 
ATOM 3459 O OE1 . GLN B 1 116 ? 123.278 170.192 102.410 1.00 129.61 ? 116  GLN B OE1 1 
ATOM 3460 N NE2 . GLN B 1 116 ? 122.167 171.475 100.942 1.00 124.72 ? 116  GLN B NE2 1 
ATOM 3461 N N   . VAL B 1 117 ? 122.194 173.162 104.153 1.00 128.76 ? 117  VAL B N   1 
ATOM 3462 C CA  . VAL B 1 117 ? 121.845 174.541 103.842 1.00 129.08 ? 117  VAL B CA  1 
ATOM 3463 C C   . VAL B 1 117 ? 120.917 174.596 102.634 1.00 128.75 ? 117  VAL B C   1 
ATOM 3464 O O   . VAL B 1 117 ? 119.915 173.883 102.573 1.00 127.34 ? 117  VAL B O   1 
ATOM 3465 C CB  . VAL B 1 117 ? 123.102 175.384 103.596 1.00 125.95 ? 117  VAL B CB  1 
ATOM 3466 C CG1 . VAL B 1 117 ? 123.915 174.793 102.457 1.00 124.77 ? 117  VAL B CG1 1 
ATOM 3467 C CG2 . VAL B 1 117 ? 122.721 176.825 103.298 1.00 123.61 ? 117  VAL B CG2 1 
ATOM 3468 N N   . GLU C 2 4   ? 124.397 125.387 193.129 1.00 126.15 ? 4    GLU C N   1 
ATOM 3469 C CA  . GLU C 2 4   ? 124.630 124.893 194.481 1.00 128.58 ? 4    GLU C CA  1 
ATOM 3470 C C   . GLU C 2 4   ? 126.055 124.374 194.632 1.00 129.10 ? 4    GLU C C   1 
ATOM 3471 O O   . GLU C 2 4   ? 126.463 123.955 195.715 1.00 128.11 ? 4    GLU C O   1 
ATOM 3472 C CB  . GLU C 2 4   ? 123.628 123.792 194.830 1.00 130.89 ? 4    GLU C CB  1 
ATOM 3473 C CG  . GLU C 2 4   ? 123.712 122.570 193.930 1.00 132.92 ? 4    GLU C CG  1 
ATOM 3474 C CD  . GLU C 2 4   ? 122.684 121.514 194.285 1.00 134.90 ? 4    GLU C CD  1 
ATOM 3475 O OE1 . GLU C 2 4   ? 121.797 121.803 195.115 1.00 136.92 ? 4    GLU C OE1 1 
ATOM 3476 O OE2 . GLU C 2 4   ? 122.763 120.396 193.736 1.00 134.08 ? 4    GLU C OE2 1 
ATOM 3477 N N   . VAL C 2 5   ? 126.809 124.407 193.533 1.00 129.19 ? 5    VAL C N   1 
ATOM 3478 C CA  . VAL C 2 5   ? 128.183 123.919 193.547 1.00 125.51 ? 5    VAL C CA  1 
ATOM 3479 C C   . VAL C 2 5   ? 129.072 124.933 194.251 1.00 122.60 ? 5    VAL C C   1 
ATOM 3480 O O   . VAL C 2 5   ? 129.093 126.118 193.894 1.00 122.31 ? 5    VAL C O   1 
ATOM 3481 C CB  . VAL C 2 5   ? 128.670 123.652 192.115 1.00 120.23 ? 5    VAL C CB  1 
ATOM 3482 C CG1 . VAL C 2 5   ? 130.098 123.153 192.133 1.00 111.31 ? 5    VAL C CG1 1 
ATOM 3483 C CG2 . VAL C 2 5   ? 127.758 122.652 191.423 1.00 120.44 ? 5    VAL C CG2 1 
ATOM 3484 N N   . GLN C 2 6   ? 129.816 124.471 195.254 1.00 121.92 ? 6    GLN C N   1 
ATOM 3485 C CA  . GLN C 2 6   ? 130.678 125.361 196.018 1.00 122.41 ? 6    GLN C CA  1 
ATOM 3486 C C   . GLN C 2 6   ? 131.752 124.549 196.725 1.00 117.34 ? 6    GLN C C   1 
ATOM 3487 O O   . GLN C 2 6   ? 131.669 123.322 196.830 1.00 116.30 ? 6    GLN C O   1 
ATOM 3488 C CB  . GLN C 2 6   ? 129.876 126.184 197.032 1.00 127.34 ? 6    GLN C CB  1 
ATOM 3489 C CG  . GLN C 2 6   ? 129.068 125.346 198.006 1.00 129.42 ? 6    GLN C CG  1 
ATOM 3490 C CD  . GLN C 2 6   ? 128.280 126.191 198.983 1.00 132.78 ? 6    GLN C CD  1 
ATOM 3491 O OE1 . GLN C 2 6   ? 128.512 127.394 199.109 1.00 135.56 ? 6    GLN C OE1 1 
ATOM 3492 N NE2 . GLN C 2 6   ? 127.338 125.567 199.680 1.00 130.15 ? 6    GLN C NE2 1 
ATOM 3493 N N   . LEU C 2 7   ? 132.775 125.259 197.193 1.00 113.29 ? 7    LEU C N   1 
ATOM 3494 C CA  . LEU C 2 7   ? 133.830 124.686 198.016 1.00 110.48 ? 7    LEU C CA  1 
ATOM 3495 C C   . LEU C 2 7   ? 133.997 125.552 199.254 1.00 111.55 ? 7    LEU C C   1 
ATOM 3496 O O   . LEU C 2 7   ? 134.099 126.778 199.147 1.00 109.08 ? 7    LEU C O   1 
ATOM 3497 C CB  . LEU C 2 7   ? 135.158 124.590 197.253 1.00 102.41 ? 7    LEU C CB  1 
ATOM 3498 C CG  . LEU C 2 7   ? 135.193 123.731 195.988 1.00 101.06 ? 7    LEU C CG  1 
ATOM 3499 C CD1 . LEU C 2 7   ? 134.903 124.563 194.750 1.00 89.87  ? 7    LEU C CD1 1 
ATOM 3500 C CD2 . LEU C 2 7   ? 136.529 123.027 195.861 1.00 91.57  ? 7    LEU C CD2 1 
ATOM 3501 N N   . VAL C 2 8   ? 134.021 124.917 200.421 1.00 114.65 ? 8    VAL C N   1 
ATOM 3502 C CA  . VAL C 2 8   ? 134.181 125.619 201.686 1.00 113.68 ? 8    VAL C CA  1 
ATOM 3503 C C   . VAL C 2 8   ? 135.480 125.162 202.332 1.00 114.71 ? 8    VAL C C   1 
ATOM 3504 O O   . VAL C 2 8   ? 135.950 124.043 202.105 1.00 115.36 ? 8    VAL C O   1 
ATOM 3505 C CB  . VAL C 2 8   ? 132.982 125.389 202.634 1.00 114.89 ? 8    VAL C CB  1 
ATOM 3506 C CG1 . VAL C 2 8   ? 131.672 125.617 201.896 1.00 116.01 ? 8    VAL C CG1 1 
ATOM 3507 C CG2 . VAL C 2 8   ? 133.026 123.996 203.235 1.00 114.43 ? 8    VAL C CG2 1 
ATOM 3508 N N   . GLU C 2 9   ? 136.069 126.044 203.134 1.00 116.46 ? 9    GLU C N   1 
ATOM 3509 C CA  . GLU C 2 9   ? 137.324 125.766 203.812 1.00 118.47 ? 9    GLU C CA  1 
ATOM 3510 C C   . GLU C 2 9   ? 137.112 125.742 205.319 1.00 120.32 ? 9    GLU C C   1 
ATOM 3511 O O   . GLU C 2 9   ? 136.243 126.437 205.854 1.00 119.95 ? 9    GLU C O   1 
ATOM 3512 C CB  . GLU C 2 9   ? 138.399 126.802 203.458 1.00 114.96 ? 9    GLU C CB  1 
ATOM 3513 C CG  . GLU C 2 9   ? 139.077 126.585 202.116 1.00 108.67 ? 9    GLU C CG  1 
ATOM 3514 C CD  . GLU C 2 9   ? 138.331 127.226 200.963 1.00 106.62 ? 9    GLU C CD  1 
ATOM 3515 O OE1 . GLU C 2 9   ? 137.096 127.375 201.053 1.00 110.43 ? 9    GLU C OE1 1 
ATOM 3516 O OE2 . GLU C 2 9   ? 138.986 127.589 199.966 1.00 99.87  ? 9    GLU C OE2 1 
ATOM 3517 N N   . SER C 2 10  ? 137.917 124.928 205.996 1.00 122.09 ? 10   SER C N   1 
ATOM 3518 C CA  . SER C 2 10  ? 137.827 124.776 207.439 1.00 125.26 ? 10   SER C CA  1 
ATOM 3519 C C   . SER C 2 10  ? 139.211 124.467 207.988 1.00 126.14 ? 10   SER C C   1 
ATOM 3520 O O   . SER C 2 10  ? 140.110 124.047 207.257 1.00 124.38 ? 10   SER C O   1 
ATOM 3521 C CB  . SER C 2 10  ? 136.840 123.669 207.829 1.00 125.26 ? 10   SER C CB  1 
ATOM 3522 O OG  . SER C 2 10  ? 135.570 123.884 207.239 1.00 127.68 ? 10   SER C OG  1 
ATOM 3523 N N   . GLY C 2 11  ? 139.370 124.671 209.294 1.00 129.46 ? 11   GLY C N   1 
ATOM 3524 C CA  . GLY C 2 11  ? 140.615 124.378 209.970 1.00 127.18 ? 11   GLY C CA  1 
ATOM 3525 C C   . GLY C 2 11  ? 141.579 125.538 210.086 1.00 126.02 ? 11   GLY C C   1 
ATOM 3526 O O   . GLY C 2 11  ? 142.607 125.399 210.761 1.00 125.24 ? 11   GLY C O   1 
ATOM 3527 N N   . GLY C 2 12  ? 141.290 126.672 209.453 1.00 126.59 ? 12   GLY C N   1 
ATOM 3528 C CA  . GLY C 2 12  ? 142.146 127.831 209.596 1.00 130.42 ? 12   GLY C CA  1 
ATOM 3529 C C   . GLY C 2 12  ? 141.967 128.513 210.940 1.00 136.01 ? 12   GLY C C   1 
ATOM 3530 O O   . GLY C 2 12  ? 140.883 128.527 211.523 1.00 136.74 ? 12   GLY C O   1 
ATOM 3531 N N   . GLY C 2 13  ? 143.055 129.089 211.434 1.00 136.06 ? 13   GLY C N   1 
ATOM 3532 C CA  . GLY C 2 13  ? 143.016 129.776 212.708 1.00 135.98 ? 13   GLY C CA  1 
ATOM 3533 C C   . GLY C 2 13  ? 144.404 130.202 213.134 1.00 136.37 ? 13   GLY C C   1 
ATOM 3534 O O   . GLY C 2 13  ? 145.385 130.051 212.400 1.00 130.79 ? 13   GLY C O   1 
ATOM 3535 N N   . LEU C 2 14  ? 144.463 130.745 214.348 1.00 139.82 ? 14   LEU C N   1 
ATOM 3536 C CA  . LEU C 2 14  ? 145.721 131.204 214.923 1.00 139.50 ? 14   LEU C CA  1 
ATOM 3537 C C   . LEU C 2 14  ? 146.450 130.030 215.564 1.00 139.23 ? 14   LEU C C   1 
ATOM 3538 O O   . LEU C 2 14  ? 145.937 129.409 216.501 1.00 138.61 ? 14   LEU C O   1 
ATOM 3539 C CB  . LEU C 2 14  ? 145.468 132.305 215.950 1.00 140.43 ? 14   LEU C CB  1 
ATOM 3540 C CG  . LEU C 2 14  ? 146.670 132.740 216.795 1.00 141.31 ? 14   LEU C CG  1 
ATOM 3541 C CD1 . LEU C 2 14  ? 147.799 133.254 215.916 1.00 139.49 ? 14   LEU C CD1 1 
ATOM 3542 C CD2 . LEU C 2 14  ? 146.260 133.794 217.813 1.00 138.21 ? 14   LEU C CD2 1 
ATOM 3543 N N   . VAL C 2 15  ? 147.645 129.725 215.057 1.00 138.65 ? 15   VAL C N   1 
ATOM 3544 C CA  . VAL C 2 15  ? 148.475 128.656 215.591 1.00 138.43 ? 15   VAL C CA  1 
ATOM 3545 C C   . VAL C 2 15  ? 149.897 129.175 215.752 1.00 138.82 ? 15   VAL C C   1 
ATOM 3546 O O   . VAL C 2 15  ? 150.320 130.123 215.087 1.00 136.74 ? 15   VAL C O   1 
ATOM 3547 C CB  . VAL C 2 15  ? 148.460 127.396 214.700 1.00 137.07 ? 15   VAL C CB  1 
ATOM 3548 C CG1 . VAL C 2 15  ? 147.080 126.758 214.706 1.00 135.91 ? 15   VAL C CG1 1 
ATOM 3549 C CG2 . VAL C 2 15  ? 148.887 127.748 213.286 1.00 136.94 ? 15   VAL C CG2 1 
ATOM 3550 N N   . GLN C 2 16  ? 150.634 128.534 216.654 1.00 140.79 ? 16   GLN C N   1 
ATOM 3551 C CA  . GLN C 2 16  ? 151.997 128.950 216.932 1.00 140.89 ? 16   GLN C CA  1 
ATOM 3552 C C   . GLN C 2 16  ? 152.911 128.616 215.754 1.00 140.06 ? 16   GLN C C   1 
ATOM 3553 O O   . GLN C 2 16  ? 152.677 127.643 215.032 1.00 139.27 ? 16   GLN C O   1 
ATOM 3554 C CB  . GLN C 2 16  ? 152.511 128.275 218.200 1.00 140.92 ? 16   GLN C CB  1 
ATOM 3555 C CG  . GLN C 2 16  ? 151.712 128.617 219.448 1.00 142.78 ? 16   GLN C CG  1 
ATOM 3556 C CD  . GLN C 2 16  ? 151.750 130.097 219.778 1.00 143.63 ? 16   GLN C CD  1 
ATOM 3557 O OE1 . GLN C 2 16  ? 152.764 130.765 219.578 1.00 141.34 ? 16   GLN C OE1 1 
ATOM 3558 N NE2 . GLN C 2 16  ? 150.638 130.619 220.283 1.00 143.63 ? 16   GLN C NE2 1 
ATOM 3559 N N   . PRO C 2 17  ? 153.952 129.419 215.531 1.00 138.01 ? 17   PRO C N   1 
ATOM 3560 C CA  . PRO C 2 17  ? 154.903 129.111 214.458 1.00 137.14 ? 17   PRO C CA  1 
ATOM 3561 C C   . PRO C 2 17  ? 155.631 127.802 214.719 1.00 135.69 ? 17   PRO C C   1 
ATOM 3562 O O   . PRO C 2 17  ? 155.871 127.414 215.864 1.00 135.67 ? 17   PRO C O   1 
ATOM 3563 C CB  . PRO C 2 17  ? 155.868 130.303 214.483 1.00 136.05 ? 17   PRO C CB  1 
ATOM 3564 C CG  . PRO C 2 17  ? 155.105 131.398 215.155 1.00 135.93 ? 17   PRO C CG  1 
ATOM 3565 C CD  . PRO C 2 17  ? 154.237 130.716 216.166 1.00 136.76 ? 17   PRO C CD  1 
ATOM 3566 N N   . GLY C 2 18  ? 155.982 127.118 213.633 1.00 132.99 ? 18   GLY C N   1 
ATOM 3567 C CA  . GLY C 2 18  ? 156.658 125.843 213.718 1.00 130.94 ? 18   GLY C CA  1 
ATOM 3568 C C   . GLY C 2 18  ? 155.760 124.655 213.975 1.00 132.44 ? 18   GLY C C   1 
ATOM 3569 O O   . GLY C 2 18  ? 156.269 123.535 214.111 1.00 131.34 ? 18   GLY C O   1 
ATOM 3570 N N   . GLY C 2 19  ? 154.448 124.855 214.046 1.00 134.28 ? 19   GLY C N   1 
ATOM 3571 C CA  . GLY C 2 19  ? 153.508 123.786 214.303 1.00 134.48 ? 19   GLY C CA  1 
ATOM 3572 C C   . GLY C 2 19  ? 152.966 123.167 213.033 1.00 131.17 ? 19   GLY C C   1 
ATOM 3573 O O   . GLY C 2 19  ? 153.536 123.300 211.947 1.00 129.16 ? 19   GLY C O   1 
ATOM 3574 N N   . SER C 2 20  ? 151.839 122.475 213.179 1.00 130.06 ? 20   SER C N   1 
ATOM 3575 C CA  . SER C 2 20  ? 151.184 121.790 212.076 1.00 127.48 ? 20   SER C CA  1 
ATOM 3576 C C   . SER C 2 20  ? 149.743 122.265 211.951 1.00 127.19 ? 20   SER C C   1 
ATOM 3577 O O   . SER C 2 20  ? 149.084 122.575 212.948 1.00 127.15 ? 20   SER C O   1 
ATOM 3578 C CB  . SER C 2 20  ? 151.215 120.269 212.269 1.00 125.02 ? 20   SER C CB  1 
ATOM 3579 O OG  . SER C 2 20  ? 150.591 119.607 211.184 1.00 124.15 ? 20   SER C OG  1 
ATOM 3580 N N   . LEU C 2 21  ? 149.261 122.320 210.712 1.00 122.98 ? 21   LEU C N   1 
ATOM 3581 C CA  . LEU C 2 21  ? 147.898 122.735 210.418 1.00 120.49 ? 21   LEU C CA  1 
ATOM 3582 C C   . LEU C 2 21  ? 147.246 121.725 209.488 1.00 117.25 ? 21   LEU C C   1 
ATOM 3583 O O   . LEU C 2 21  ? 147.915 121.084 208.677 1.00 116.16 ? 21   LEU C O   1 
ATOM 3584 C CB  . LEU C 2 21  ? 147.857 124.126 209.776 1.00 122.77 ? 21   LEU C CB  1 
ATOM 3585 C CG  . LEU C 2 21  ? 147.727 125.317 210.723 1.00 126.37 ? 21   LEU C CG  1 
ATOM 3586 C CD1 . LEU C 2 21  ? 147.892 126.617 209.958 1.00 126.70 ? 21   LEU C CD1 1 
ATOM 3587 C CD2 . LEU C 2 21  ? 146.381 125.276 211.425 1.00 122.60 ? 21   LEU C CD2 1 
ATOM 3588 N N   . ARG C 2 22  ? 145.928 121.588 209.616 1.00 117.14 ? 22   ARG C N   1 
ATOM 3589 C CA  . ARG C 2 22  ? 145.137 120.712 208.753 1.00 115.90 ? 22   ARG C CA  1 
ATOM 3590 C C   . ARG C 2 22  ? 144.000 121.539 208.165 1.00 118.95 ? 22   ARG C C   1 
ATOM 3591 O O   . ARG C 2 22  ? 142.970 121.740 208.815 1.00 121.24 ? 22   ARG C O   1 
ATOM 3592 C CB  . ARG C 2 22  ? 144.601 119.509 209.520 1.00 116.16 ? 22   ARG C CB  1 
ATOM 3593 C CG  . ARG C 2 22  ? 143.686 118.619 208.694 1.00 112.87 ? 22   ARG C CG  1 
ATOM 3594 C CD  . ARG C 2 22  ? 143.110 117.493 209.532 1.00 116.83 ? 22   ARG C CD  1 
ATOM 3595 N NE  . ARG C 2 22  ? 142.255 116.610 208.748 1.00 117.45 ? 22   ARG C NE  1 
ATOM 3596 C CZ  . ARG C 2 22  ? 142.695 115.580 208.039 1.00 116.20 ? 22   ARG C CZ  1 
ATOM 3597 N NH1 . ARG C 2 22  ? 143.983 115.285 207.976 1.00 114.31 ? 22   ARG C NH1 1 
ATOM 3598 N NH2 . ARG C 2 22  ? 141.822 114.827 207.377 1.00 114.65 ? 22   ARG C NH2 1 
ATOM 3599 N N   . LEU C 2 23  ? 144.185 122.016 206.938 1.00 114.78 ? 23   LEU C N   1 
ATOM 3600 C CA  . LEU C 2 23  ? 143.161 122.790 206.250 1.00 113.23 ? 23   LEU C CA  1 
ATOM 3601 C C   . LEU C 2 23  ? 142.315 121.854 205.400 1.00 113.10 ? 23   LEU C C   1 
ATOM 3602 O O   . LEU C 2 23  ? 142.830 121.194 204.493 1.00 111.06 ? 23   LEU C O   1 
ATOM 3603 C CB  . LEU C 2 23  ? 143.792 123.883 205.391 1.00 108.77 ? 23   LEU C CB  1 
ATOM 3604 C CG  . LEU C 2 23  ? 143.595 125.296 205.937 1.00 115.77 ? 23   LEU C CG  1 
ATOM 3605 C CD1 . LEU C 2 23  ? 144.199 125.423 207.326 1.00 119.36 ? 23   LEU C CD1 1 
ATOM 3606 C CD2 . LEU C 2 23  ? 144.181 126.329 204.997 1.00 109.83 ? 23   LEU C CD2 1 
ATOM 3607 N N   . SER C 2 24  ? 141.023 121.794 205.694 1.00 115.41 ? 24   SER C N   1 
ATOM 3608 C CA  . SER C 2 24  ? 140.099 120.936 204.974 1.00 115.45 ? 24   SER C CA  1 
ATOM 3609 C C   . SER C 2 24  ? 139.291 121.751 203.973 1.00 114.75 ? 24   SER C C   1 
ATOM 3610 O O   . SER C 2 24  ? 138.980 122.922 204.203 1.00 115.82 ? 24   SER C O   1 
ATOM 3611 C CB  . SER C 2 24  ? 139.157 120.214 205.939 1.00 118.39 ? 24   SER C CB  1 
ATOM 3612 O OG  . SER C 2 24  ? 138.255 119.376 205.240 1.00 116.22 ? 24   SER C OG  1 
ATOM 3613 N N   . CYS C 2 25  ? 138.954 121.113 202.856 1.00 111.68 ? 25   CYS C N   1 
ATOM 3614 C CA  . CYS C 2 25  ? 138.176 121.727 201.787 1.00 110.87 ? 25   CYS C CA  1 
ATOM 3615 C C   . CYS C 2 25  ? 137.038 120.781 201.433 1.00 112.78 ? 25   CYS C C   1 
ATOM 3616 O O   . CYS C 2 25  ? 137.275 119.705 200.876 1.00 112.68 ? 25   CYS C O   1 
ATOM 3617 C CB  . CYS C 2 25  ? 139.049 122.012 200.567 1.00 108.25 ? 25   CYS C CB  1 
ATOM 3618 S SG  . CYS C 2 25  ? 138.137 122.459 199.078 1.00 110.52 ? 25   CYS C SG  1 
ATOM 3619 N N   . ALA C 2 26  ? 135.814 121.180 201.756 1.00 113.92 ? 26   ALA C N   1 
ATOM 3620 C CA  . ALA C 2 26  ? 134.630 120.374 201.493 1.00 115.85 ? 26   ALA C CA  1 
ATOM 3621 C C   . ALA C 2 26  ? 133.960 120.857 200.215 1.00 116.00 ? 26   ALA C C   1 
ATOM 3622 O O   . ALA C 2 26  ? 133.748 122.060 200.035 1.00 114.61 ? 26   ALA C O   1 
ATOM 3623 C CB  . ALA C 2 26  ? 133.651 120.440 202.665 1.00 115.17 ? 26   ALA C CB  1 
ATOM 3624 N N   . ALA C 2 27  ? 133.625 119.917 199.338 1.00 116.90 ? 27   ALA C N   1 
ATOM 3625 C CA  . ALA C 2 27  ? 133.052 120.217 198.034 1.00 114.95 ? 27   ALA C CA  1 
ATOM 3626 C C   . ALA C 2 27  ? 131.596 119.776 198.001 1.00 120.31 ? 27   ALA C C   1 
ATOM 3627 O O   . ALA C 2 27  ? 131.269 118.669 198.441 1.00 121.49 ? 27   ALA C O   1 
ATOM 3628 C CB  . ALA C 2 27  ? 133.841 119.521 196.924 1.00 107.29 ? 27   ALA C CB  1 
ATOM 3629 N N   . SER C 2 28  ? 130.726 120.641 197.481 1.00 122.09 ? 28   SER C N   1 
ATOM 3630 C CA  . SER C 2 28  ? 129.308 120.345 197.359 1.00 121.85 ? 28   SER C CA  1 
ATOM 3631 C C   . SER C 2 28  ? 128.851 120.638 195.938 1.00 120.96 ? 28   SER C C   1 
ATOM 3632 O O   . SER C 2 28  ? 129.276 121.626 195.332 1.00 121.70 ? 28   SER C O   1 
ATOM 3633 C CB  . SER C 2 28  ? 128.479 121.165 198.355 1.00 124.57 ? 28   SER C CB  1 
ATOM 3634 O OG  . SER C 2 28  ? 128.905 120.932 199.686 1.00 122.78 ? 28   SER C OG  1 
ATOM 3635 N N   . GLY C 2 29  ? 127.981 119.779 195.414 1.00 120.29 ? 29   GLY C N   1 
ATOM 3636 C CA  . GLY C 2 29  ? 127.442 119.953 194.083 1.00 120.44 ? 29   GLY C CA  1 
ATOM 3637 C C   . GLY C 2 29  ? 128.214 119.275 192.973 1.00 118.12 ? 29   GLY C C   1 
ATOM 3638 O O   . GLY C 2 29  ? 127.766 119.313 191.820 1.00 116.68 ? 29   GLY C O   1 
ATOM 3639 N N   . PHE C 2 30  ? 129.354 118.660 193.274 1.00 115.11 ? 30   PHE C N   1 
ATOM 3640 C CA  . PHE C 2 30  ? 130.131 117.958 192.262 1.00 110.64 ? 30   PHE C CA  1 
ATOM 3641 C C   . PHE C 2 30  ? 130.964 116.887 192.949 1.00 106.58 ? 30   PHE C C   1 
ATOM 3642 O O   . PHE C 2 30  ? 131.126 116.885 194.172 1.00 107.37 ? 30   PHE C O   1 
ATOM 3643 C CB  . PHE C 2 30  ? 131.019 118.920 191.462 1.00 104.70 ? 30   PHE C CB  1 
ATOM 3644 C CG  . PHE C 2 30  ? 132.225 119.408 192.216 1.00 102.12 ? 30   PHE C CG  1 
ATOM 3645 C CD1 . PHE C 2 30  ? 132.135 120.498 193.061 1.00 103.38 ? 30   PHE C CD1 1 
ATOM 3646 C CD2 . PHE C 2 30  ? 133.451 118.781 192.071 1.00 94.61  ? 30   PHE C CD2 1 
ATOM 3647 C CE1 . PHE C 2 30  ? 133.240 120.950 193.750 1.00 99.68  ? 30   PHE C CE1 1 
ATOM 3648 C CE2 . PHE C 2 30  ? 134.558 119.227 192.760 1.00 89.23  ? 30   PHE C CE2 1 
ATOM 3649 C CZ  . PHE C 2 30  ? 134.452 120.313 193.599 1.00 92.28  ? 30   PHE C CZ  1 
ATOM 3650 N N   . ASN C 2 31  ? 131.492 115.972 192.142 1.00 103.31 ? 31   ASN C N   1 
ATOM 3651 C CA  . ASN C 2 31  ? 132.336 114.897 192.642 1.00 102.44 ? 31   ASN C CA  1 
ATOM 3652 C C   . ASN C 2 31  ? 133.801 115.296 192.530 1.00 97.95  ? 31   ASN C C   1 
ATOM 3653 O O   . ASN C 2 31  ? 134.249 115.750 191.473 1.00 90.82  ? 31   ASN C O   1 
ATOM 3654 C CB  . ASN C 2 31  ? 132.080 113.602 191.870 1.00 105.21 ? 31   ASN C CB  1 
ATOM 3655 C CG  . ASN C 2 31  ? 130.706 113.027 192.140 1.00 112.53 ? 31   ASN C CG  1 
ATOM 3656 O OD1 . ASN C 2 31  ? 130.515 112.269 193.090 1.00 113.50 ? 31   ASN C OD1 1 
ATOM 3657 N ND2 . ASN C 2 31  ? 129.740 113.384 191.301 1.00 114.10 ? 31   ASN C ND2 1 
ATOM 3658 N N   . VAL C 2 32  ? 134.541 115.124 193.627 1.00 99.71  ? 32   VAL C N   1 
ATOM 3659 C CA  . VAL C 2 32  ? 135.967 115.422 193.632 1.00 93.81  ? 32   VAL C CA  1 
ATOM 3660 C C   . VAL C 2 32  ? 136.731 114.529 192.664 1.00 86.24  ? 32   VAL C C   1 
ATOM 3661 O O   . VAL C 2 32  ? 137.760 114.946 192.123 1.00 83.51  ? 32   VAL C O   1 
ATOM 3662 C CB  . VAL C 2 32  ? 136.504 115.309 195.073 1.00 94.89  ? 32   VAL C CB  1 
ATOM 3663 C CG1 . VAL C 2 32  ? 138.007 115.094 195.097 1.00 85.91  ? 32   VAL C CG1 1 
ATOM 3664 C CG2 . VAL C 2 32  ? 136.149 116.560 195.849 1.00 99.12  ? 32   VAL C CG2 1 
ATOM 3665 N N   . VAL C 2 33  ? 136.235 113.319 192.397 1.00 86.02  ? 33   VAL C N   1 
ATOM 3666 C CA  . VAL C 2 33  ? 136.932 112.423 191.481 1.00 85.27  ? 33   VAL C CA  1 
ATOM 3667 C C   . VAL C 2 33  ? 137.006 113.017 190.079 1.00 80.69  ? 33   VAL C C   1 
ATOM 3668 O O   . VAL C 2 33  ? 137.923 112.700 189.313 1.00 76.16  ? 33   VAL C O   1 
ATOM 3669 C CB  . VAL C 2 33  ? 136.257 111.039 191.472 1.00 91.11  ? 33   VAL C CB  1 
ATOM 3670 C CG1 . VAL C 2 33  ? 136.227 110.459 192.873 1.00 93.69  ? 33   VAL C CG1 1 
ATOM 3671 C CG2 . VAL C 2 33  ? 134.850 111.129 190.901 1.00 92.08  ? 33   VAL C CG2 1 
ATOM 3672 N N   . ASP C 2 34  ? 136.062 113.883 189.719 1.00 77.59  ? 34   ASP C N   1 
ATOM 3673 C CA  . ASP C 2 34  ? 136.002 114.455 188.382 1.00 76.60  ? 34   ASP C CA  1 
ATOM 3674 C C   . ASP C 2 34  ? 136.752 115.773 188.254 1.00 71.91  ? 34   ASP C C   1 
ATOM 3675 O O   . ASP C 2 34  ? 136.755 116.360 187.167 1.00 66.99  ? 34   ASP C O   1 
ATOM 3676 C CB  . ASP C 2 34  ? 134.543 114.660 187.961 1.00 82.24  ? 34   ASP C CB  1 
ATOM 3677 C CG  . ASP C 2 34  ? 133.849 113.360 187.611 1.00 88.52  ? 34   ASP C CG  1 
ATOM 3678 O OD1 . ASP C 2 34  ? 134.519 112.455 187.073 1.00 86.87  ? 34   ASP C OD1 1 
ATOM 3679 O OD2 . ASP C 2 34  ? 132.633 113.245 187.872 1.00 96.80  ? 34   ASP C OD2 1 
ATOM 3680 N N   . PHE C 2 35  ? 137.378 116.257 189.322 1.00 66.78  ? 35   PHE C N   1 
ATOM 3681 C CA  . PHE C 2 35  ? 138.079 117.530 189.287 1.00 55.27  ? 35   PHE C CA  1 
ATOM 3682 C C   . PHE C 2 35  ? 139.352 117.434 190.110 1.00 51.87  ? 35   PHE C C   1 
ATOM 3683 O O   . PHE C 2 35  ? 139.516 116.541 190.941 1.00 58.71  ? 35   PHE C O   1 
ATOM 3684 C CB  . PHE C 2 35  ? 137.206 118.673 189.812 1.00 56.95  ? 35   PHE C CB  1 
ATOM 3685 C CG  . PHE C 2 35  ? 136.087 119.053 188.891 1.00 60.87  ? 35   PHE C CG  1 
ATOM 3686 C CD1 . PHE C 2 35  ? 134.863 118.418 188.966 1.00 68.20  ? 35   PHE C CD1 1 
ATOM 3687 C CD2 . PHE C 2 35  ? 136.259 120.052 187.953 1.00 58.56  ? 35   PHE C CD2 1 
ATOM 3688 C CE1 . PHE C 2 35  ? 133.836 118.768 188.120 1.00 66.39  ? 35   PHE C CE1 1 
ATOM 3689 C CE2 . PHE C 2 35  ? 135.236 120.406 187.105 1.00 60.23  ? 35   PHE C CE2 1 
ATOM 3690 C CZ  . PHE C 2 35  ? 134.023 119.763 187.188 1.00 60.57  ? 35   PHE C CZ  1 
ATOM 3691 N N   . SER C 2 36  ? 140.260 118.366 189.859 1.00 45.00  ? 36   SER C N   1 
ATOM 3692 C CA  . SER C 2 36  ? 141.490 118.489 190.622 1.00 40.58  ? 36   SER C CA  1 
ATOM 3693 C C   . SER C 2 36  ? 141.359 119.664 191.574 1.00 42.99  ? 36   SER C C   1 
ATOM 3694 O O   . SER C 2 36  ? 140.931 120.751 191.170 1.00 48.76  ? 36   SER C O   1 
ATOM 3695 C CB  . SER C 2 36  ? 142.684 118.698 189.702 1.00 34.18  ? 36   SER C CB  1 
ATOM 3696 O OG  . SER C 2 36  ? 142.620 119.988 189.142 1.00 31.84  ? 36   SER C OG  1 
ATOM 3697 N N   . LEU C 2 37  ? 141.727 119.449 192.828 1.00 42.40  ? 37   LEU C N   1 
ATOM 3698 C CA  . LEU C 2 37  ? 141.572 120.467 193.856 1.00 43.21  ? 37   LEU C CA  1 
ATOM 3699 C C   . LEU C 2 37  ? 142.927 121.097 194.139 1.00 41.08  ? 37   LEU C C   1 
ATOM 3700 O O   . LEU C 2 37  ? 143.859 120.409 194.566 1.00 44.73  ? 37   LEU C O   1 
ATOM 3701 C CB  . LEU C 2 37  ? 140.962 119.874 195.123 1.00 52.21  ? 37   LEU C CB  1 
ATOM 3702 C CG  . LEU C 2 37  ? 139.548 119.325 194.923 1.00 64.80  ? 37   LEU C CG  1 
ATOM 3703 C CD1 . LEU C 2 37  ? 138.940 118.891 196.238 1.00 82.45  ? 37   LEU C CD1 1 
ATOM 3704 C CD2 . LEU C 2 37  ? 138.659 120.350 194.241 1.00 63.13  ? 37   LEU C CD2 1 
ATOM 3705 N N   . HIS C 2 38  ? 143.031 122.397 193.889 1.00 38.32  ? 38   HIS C N   1 
ATOM 3706 C CA  . HIS C 2 38  ? 144.259 123.152 194.061 1.00 39.29  ? 38   HIS C CA  1 
ATOM 3707 C C   . HIS C 2 38  ? 144.145 124.043 195.286 1.00 47.21  ? 38   HIS C C   1 
ATOM 3708 O O   . HIS C 2 38  ? 143.058 124.503 195.637 1.00 58.59  ? 38   HIS C O   1 
ATOM 3709 C CB  . HIS C 2 38  ? 144.551 124.014 192.835 1.00 33.93  ? 38   HIS C CB  1 
ATOM 3710 C CG  . HIS C 2 38  ? 144.763 123.234 191.579 1.00 29.03  ? 38   HIS C CG  1 
ATOM 3711 N ND1 . HIS C 2 38  ? 145.865 123.409 190.776 1.00 27.21  ? 38   HIS C ND1 1 
ATOM 3712 C CD2 . HIS C 2 38  ? 144.015 122.276 190.987 1.00 28.58  ? 38   HIS C CD2 1 
ATOM 3713 C CE1 . HIS C 2 38  ? 145.789 122.592 189.743 1.00 24.56  ? 38   HIS C CE1 1 
ATOM 3714 N NE2 . HIS C 2 38  ? 144.675 121.894 189.847 1.00 25.65  ? 38   HIS C NE2 1 
ATOM 3715 N N   . TRP C 2 39  ? 145.273 124.280 195.937 1.00 42.77  ? 39   TRP C N   1 
ATOM 3716 C CA  . TRP C 2 39  ? 145.362 125.196 197.062 1.00 51.03  ? 39   TRP C CA  1 
ATOM 3717 C C   . TRP C 2 39  ? 146.223 126.374 196.643 1.00 52.12  ? 39   TRP C C   1 
ATOM 3718 O O   . TRP C 2 39  ? 147.381 126.186 196.251 1.00 55.13  ? 39   TRP C O   1 
ATOM 3719 C CB  . TRP C 2 39  ? 145.944 124.509 198.294 1.00 57.07  ? 39   TRP C CB  1 
ATOM 3720 C CG  . TRP C 2 39  ? 144.972 123.616 198.975 1.00 67.85  ? 39   TRP C CG  1 
ATOM 3721 C CD1 . TRP C 2 39  ? 144.728 122.309 198.695 1.00 69.64  ? 39   TRP C CD1 1 
ATOM 3722 C CD2 . TRP C 2 39  ? 144.100 123.965 200.054 1.00 76.90  ? 39   TRP C CD2 1 
ATOM 3723 N NE1 . TRP C 2 39  ? 143.759 121.818 199.532 1.00 78.68  ? 39   TRP C NE1 1 
ATOM 3724 C CE2 . TRP C 2 39  ? 143.357 122.817 200.377 1.00 85.91  ? 39   TRP C CE2 1 
ATOM 3725 C CE3 . TRP C 2 39  ? 143.876 125.139 200.779 1.00 85.31  ? 39   TRP C CE3 1 
ATOM 3726 C CZ2 . TRP C 2 39  ? 142.407 122.805 201.393 1.00 97.34  ? 39   TRP C CZ2 1 
ATOM 3727 C CZ3 . TRP C 2 39  ? 142.932 125.126 201.786 1.00 93.54  ? 39   TRP C CZ3 1 
ATOM 3728 C CH2 . TRP C 2 39  ? 142.209 123.967 202.084 1.00 99.23  ? 39   TRP C CH2 1 
ATOM 3729 N N   . VAL C 2 40  ? 145.654 127.573 196.733 1.00 58.73  ? 40   VAL C N   1 
ATOM 3730 C CA  . VAL C 2 40  ? 146.297 128.815 196.319 1.00 62.28  ? 40   VAL C CA  1 
ATOM 3731 C C   . VAL C 2 40  ? 146.327 129.745 197.524 1.00 73.55  ? 40   VAL C C   1 
ATOM 3732 O O   . VAL C 2 40  ? 145.281 130.028 198.118 1.00 79.18  ? 40   VAL C O   1 
ATOM 3733 C CB  . VAL C 2 40  ? 145.551 129.471 195.146 1.00 59.12  ? 40   VAL C CB  1 
ATOM 3734 C CG1 . VAL C 2 40  ? 146.230 130.757 194.735 1.00 62.72  ? 40   VAL C CG1 1 
ATOM 3735 C CG2 . VAL C 2 40  ? 145.449 128.517 193.977 1.00 49.11  ? 40   VAL C CG2 1 
ATOM 3736 N N   . ARG C 2 41  ? 147.510 130.228 197.883 1.00 74.35  ? 41   ARG C N   1 
ATOM 3737 C CA  . ARG C 2 41  ? 147.636 131.142 199.007 1.00 82.23  ? 41   ARG C CA  1 
ATOM 3738 C C   . ARG C 2 41  ? 147.683 132.582 198.519 1.00 86.09  ? 41   ARG C C   1 
ATOM 3739 O O   . ARG C 2 41  ? 148.081 132.865 197.386 1.00 83.91  ? 41   ARG C O   1 
ATOM 3740 C CB  . ARG C 2 41  ? 148.883 130.847 199.841 1.00 81.09  ? 41   ARG C CB  1 
ATOM 3741 C CG  . ARG C 2 41  ? 150.173 131.342 199.221 1.00 77.60  ? 41   ARG C CG  1 
ATOM 3742 C CD  . ARG C 2 41  ? 151.192 131.711 200.284 1.00 83.24  ? 41   ARG C CD  1 
ATOM 3743 N NE  . ARG C 2 41  ? 151.489 130.602 201.181 1.00 89.28  ? 41   ARG C NE  1 
ATOM 3744 C CZ  . ARG C 2 41  ? 152.494 129.754 201.016 1.00 90.41  ? 41   ARG C CZ  1 
ATOM 3745 N NH1 . ARG C 2 41  ? 153.314 129.847 199.982 1.00 82.98  ? 41   ARG C NH1 1 
ATOM 3746 N NH2 . ARG C 2 41  ? 152.683 128.791 201.911 1.00 94.91  ? 41   ARG C NH2 1 
ATOM 3747 N N   . GLN C 2 42  ? 147.260 133.493 199.391 1.00 92.41  ? 42   GLN C N   1 
ATOM 3748 C CA  . GLN C 2 42  ? 147.321 134.927 199.128 1.00 97.74  ? 42   GLN C CA  1 
ATOM 3749 C C   . GLN C 2 42  ? 147.775 135.608 200.410 1.00 107.01 ? 42   GLN C C   1 
ATOM 3750 O O   . GLN C 2 42  ? 147.053 135.591 201.411 1.00 111.80 ? 42   GLN C O   1 
ATOM 3751 C CB  . GLN C 2 42  ? 145.967 135.467 198.670 1.00 98.47  ? 42   GLN C CB  1 
ATOM 3752 C CG  . GLN C 2 42  ? 145.967 136.950 198.350 1.00 101.06 ? 42   GLN C CG  1 
ATOM 3753 C CD  . GLN C 2 42  ? 144.611 137.449 197.896 1.00 101.67 ? 42   GLN C CD  1 
ATOM 3754 O OE1 . GLN C 2 42  ? 143.579 136.879 198.246 1.00 102.05 ? 42   GLN C OE1 1 
ATOM 3755 N NE2 . GLN C 2 42  ? 144.607 138.515 197.106 1.00 100.08 ? 42   GLN C NE2 1 
ATOM 3756 N N   . ALA C 2 43  ? 148.977 136.173 200.389 1.00 110.99 ? 43   ALA C N   1 
ATOM 3757 C CA  . ALA C 2 43  ? 149.477 136.894 201.544 1.00 117.78 ? 43   ALA C CA  1 
ATOM 3758 C C   . ALA C 2 43  ? 148.695 138.194 201.727 1.00 123.32 ? 43   ALA C C   1 
ATOM 3759 O O   . ALA C 2 43  ? 148.180 138.757 200.757 1.00 122.66 ? 43   ALA C O   1 
ATOM 3760 C CB  . ALA C 2 43  ? 150.965 137.190 201.382 1.00 117.91 ? 43   ALA C CB  1 
ATOM 3761 N N   . PRO C 2 44  ? 148.577 138.683 202.961 1.00 124.60 ? 44   PRO C N   1 
ATOM 3762 C CA  . PRO C 2 44  ? 147.842 139.935 203.186 1.00 125.75 ? 44   PRO C CA  1 
ATOM 3763 C C   . PRO C 2 44  ? 148.488 141.096 202.443 1.00 125.44 ? 44   PRO C C   1 
ATOM 3764 O O   . PRO C 2 44  ? 149.695 141.327 202.541 1.00 123.09 ? 44   PRO C O   1 
ATOM 3765 C CB  . PRO C 2 44  ? 147.914 140.121 204.707 1.00 126.46 ? 44   PRO C CB  1 
ATOM 3766 C CG  . PRO C 2 44  ? 149.082 139.294 205.140 1.00 124.32 ? 44   PRO C CG  1 
ATOM 3767 C CD  . PRO C 2 44  ? 149.096 138.118 204.218 1.00 120.54 ? 44   PRO C CD  1 
ATOM 3768 N N   . GLY C 2 45  ? 147.665 141.829 201.697 1.00 126.27 ? 45   GLY C N   1 
ATOM 3769 C CA  . GLY C 2 45  ? 148.168 142.920 200.879 1.00 126.29 ? 45   GLY C CA  1 
ATOM 3770 C C   . GLY C 2 45  ? 149.094 142.478 199.769 1.00 125.33 ? 45   GLY C C   1 
ATOM 3771 O O   . GLY C 2 45  ? 150.036 143.202 199.431 1.00 125.35 ? 45   GLY C O   1 
ATOM 3772 N N   . LYS C 2 46  ? 148.848 141.306 199.186 1.00 123.23 ? 46   LYS C N   1 
ATOM 3773 C CA  . LYS C 2 46  ? 149.701 140.772 198.136 1.00 119.14 ? 46   LYS C CA  1 
ATOM 3774 C C   . LYS C 2 46  ? 148.869 139.877 197.228 1.00 113.57 ? 46   LYS C C   1 
ATOM 3775 O O   . LYS C 2 46  ? 147.718 139.551 197.525 1.00 111.30 ? 46   LYS C O   1 
ATOM 3776 C CB  . LYS C 2 46  ? 150.898 140.013 198.719 1.00 118.01 ? 46   LYS C CB  1 
ATOM 3777 C CG  . LYS C 2 46  ? 152.172 140.841 198.790 1.00 120.81 ? 46   LYS C CG  1 
ATOM 3778 C CD  . LYS C 2 46  ? 153.215 140.196 199.685 1.00 123.32 ? 46   LYS C CD  1 
ATOM 3779 C CE  . LYS C 2 46  ? 152.805 140.276 201.145 1.00 125.66 ? 46   LYS C CE  1 
ATOM 3780 N NZ  . LYS C 2 46  ? 152.566 141.681 201.578 1.00 128.33 ? 46   LYS C NZ  1 
ATOM 3781 N N   . GLY C 2 47  ? 149.472 139.483 196.108 1.00 109.94 ? 47   GLY C N   1 
ATOM 3782 C CA  . GLY C 2 47  ? 148.774 138.723 195.094 1.00 99.70  ? 47   GLY C CA  1 
ATOM 3783 C C   . GLY C 2 47  ? 148.642 137.252 195.434 1.00 93.67  ? 47   GLY C C   1 
ATOM 3784 O O   . GLY C 2 47  ? 149.079 136.771 196.479 1.00 93.82  ? 47   GLY C O   1 
ATOM 3785 N N   . LEU C 2 48  ? 148.014 136.525 194.512 1.00 85.97  ? 48   LEU C N   1 
ATOM 3786 C CA  . LEU C 2 48  ? 147.768 135.103 194.692 1.00 75.10  ? 48   LEU C CA  1 
ATOM 3787 C C   . LEU C 2 48  ? 149.007 134.292 194.340 1.00 69.27  ? 48   LEU C C   1 
ATOM 3788 O O   . LEU C 2 48  ? 149.715 134.597 193.378 1.00 68.36  ? 48   LEU C O   1 
ATOM 3789 C CB  . LEU C 2 48  ? 146.589 134.659 193.828 1.00 69.66  ? 48   LEU C CB  1 
ATOM 3790 C CG  . LEU C 2 48  ? 145.214 135.196 194.220 1.00 76.19  ? 48   LEU C CG  1 
ATOM 3791 C CD1 . LEU C 2 48  ? 144.277 135.195 193.031 1.00 71.13  ? 48   LEU C CD1 1 
ATOM 3792 C CD2 . LEU C 2 48  ? 144.636 134.361 195.340 1.00 79.15  ? 48   LEU C CD2 1 
ATOM 3793 N N   . GLU C 2 49  ? 149.268 133.256 195.134 1.00 70.26  ? 49   GLU C N   1 
ATOM 3794 C CA  . GLU C 2 49  ? 150.380 132.344 194.904 1.00 68.51  ? 49   GLU C CA  1 
ATOM 3795 C C   . GLU C 2 49  ? 149.869 130.915 194.956 1.00 63.91  ? 49   GLU C C   1 
ATOM 3796 O O   . GLU C 2 49  ? 149.193 130.530 195.914 1.00 66.29  ? 49   GLU C O   1 
ATOM 3797 C CB  . GLU C 2 49  ? 151.489 132.535 195.939 1.00 71.55  ? 49   GLU C CB  1 
ATOM 3798 C CG  . GLU C 2 49  ? 152.558 131.459 195.884 1.00 73.29  ? 49   GLU C CG  1 
ATOM 3799 C CD  . GLU C 2 49  ? 153.363 131.366 197.160 1.00 79.18  ? 49   GLU C CD  1 
ATOM 3800 O OE1 . GLU C 2 49  ? 153.560 132.409 197.816 1.00 84.39  ? 49   GLU C OE1 1 
ATOM 3801 O OE2 . GLU C 2 49  ? 153.792 130.248 197.515 1.00 75.30  ? 49   GLU C OE2 1 
ATOM 3802 N N   . TRP C 2 50  ? 150.201 130.133 193.935 1.00 54.09  ? 50   TRP C N   1 
ATOM 3803 C CA  . TRP C 2 50  ? 149.791 128.738 193.870 1.00 46.19  ? 50   TRP C CA  1 
ATOM 3804 C C   . TRP C 2 50  ? 150.632 127.910 194.831 1.00 46.77  ? 50   TRP C C   1 
ATOM 3805 O O   . TRP C 2 50  ? 151.861 128.014 194.836 1.00 52.27  ? 50   TRP C O   1 
ATOM 3806 C CB  . TRP C 2 50  ? 149.939 128.229 192.440 1.00 38.01  ? 50   TRP C CB  1 
ATOM 3807 C CG  . TRP C 2 50  ? 149.450 126.847 192.220 1.00 34.72  ? 50   TRP C CG  1 
ATOM 3808 C CD1 . TRP C 2 50  ? 148.164 126.457 192.024 1.00 32.33  ? 50   TRP C CD1 1 
ATOM 3809 C CD2 . TRP C 2 50  ? 150.245 125.664 192.142 1.00 32.79  ? 50   TRP C CD2 1 
ATOM 3810 N NE1 . TRP C 2 50  ? 148.105 125.102 191.842 1.00 29.88  ? 50   TRP C NE1 1 
ATOM 3811 C CE2 . TRP C 2 50  ? 149.373 124.592 191.911 1.00 28.32  ? 50   TRP C CE2 1 
ATOM 3812 C CE3 . TRP C 2 50  ? 151.611 125.409 192.253 1.00 34.57  ? 50   TRP C CE3 1 
ATOM 3813 C CZ2 . TRP C 2 50  ? 149.820 123.289 191.791 1.00 28.59  ? 50   TRP C CZ2 1 
ATOM 3814 C CZ3 . TRP C 2 50  ? 152.049 124.119 192.132 1.00 34.29  ? 50   TRP C CZ3 1 
ATOM 3815 C CH2 . TRP C 2 50  ? 151.159 123.074 191.903 1.00 32.09  ? 50   TRP C CH2 1 
ATOM 3816 N N   . VAL C 2 51  ? 149.975 127.088 195.647 1.00 42.33  ? 51   VAL C N   1 
ATOM 3817 C CA  . VAL C 2 51  ? 150.638 126.329 196.707 1.00 39.37  ? 51   VAL C CA  1 
ATOM 3818 C C   . VAL C 2 51  ? 150.749 124.853 196.353 1.00 40.31  ? 51   VAL C C   1 
ATOM 3819 O O   . VAL C 2 51  ? 151.842 124.290 196.351 1.00 50.25  ? 51   VAL C O   1 
ATOM 3820 C CB  . VAL C 2 51  ? 149.928 126.525 198.064 1.00 47.60  ? 51   VAL C CB  1 
ATOM 3821 C CG1 . VAL C 2 51  ? 150.324 125.430 199.027 1.00 53.64  ? 51   VAL C CG1 1 
ATOM 3822 C CG2 . VAL C 2 51  ? 150.291 127.856 198.643 1.00 65.16  ? 51   VAL C CG2 1 
ATOM 3823 N N   . ALA C 2 52  ? 149.628 124.204 196.065 1.00 38.12  ? 52   ALA C N   1 
ATOM 3824 C CA  . ALA C 2 52  ? 149.655 122.761 195.863 1.00 33.52  ? 52   ALA C CA  1 
ATOM 3825 C C   . ALA C 2 52  ? 148.455 122.355 195.025 1.00 34.67  ? 52   ALA C C   1 
ATOM 3826 O O   . ALA C 2 52  ? 147.591 123.173 194.714 1.00 42.54  ? 52   ALA C O   1 
ATOM 3827 C CB  . ALA C 2 52  ? 149.669 122.024 197.201 1.00 40.39  ? 52   ALA C CB  1 
ATOM 3828 N N   . TYR C 2 53  ? 148.398 121.076 194.666 1.00 34.43  ? 53   TYR C N   1 
ATOM 3829 C CA  . TYR C 2 53  ? 147.224 120.546 193.987 1.00 36.31  ? 53   TYR C CA  1 
ATOM 3830 C C   . TYR C 2 53  ? 147.181 119.043 194.178 1.00 38.22  ? 53   TYR C C   1 
ATOM 3831 O O   . TYR C 2 53  ? 148.200 118.407 194.452 1.00 47.16  ? 53   TYR C O   1 
ATOM 3832 C CB  . TYR C 2 53  ? 147.217 120.906 192.498 1.00 34.50  ? 53   TYR C CB  1 
ATOM 3833 C CG  . TYR C 2 53  ? 147.640 119.814 191.543 1.00 32.17  ? 53   TYR C CG  1 
ATOM 3834 C CD1 . TYR C 2 53  ? 146.714 118.937 191.006 1.00 33.90  ? 53   TYR C CD1 1 
ATOM 3835 C CD2 . TYR C 2 53  ? 148.955 119.694 191.140 1.00 33.71  ? 53   TYR C CD2 1 
ATOM 3836 C CE1 . TYR C 2 53  ? 147.094 117.956 190.122 1.00 35.80  ? 53   TYR C CE1 1 
ATOM 3837 C CE2 . TYR C 2 53  ? 149.341 118.716 190.255 1.00 34.85  ? 53   TYR C CE2 1 
ATOM 3838 C CZ  . TYR C 2 53  ? 148.409 117.852 189.750 1.00 37.12  ? 53   TYR C CZ  1 
ATOM 3839 O OH  . TYR C 2 53  ? 148.797 116.875 188.868 1.00 42.56  ? 53   TYR C OH  1 
ATOM 3840 N N   . ILE C 2 54  ? 145.984 118.484 194.046 1.00 36.30  ? 54   ILE C N   1 
ATOM 3841 C CA  . ILE C 2 54  ? 145.811 117.037 194.040 1.00 43.91  ? 54   ILE C CA  1 
ATOM 3842 C C   . ILE C 2 54  ? 144.798 116.665 192.970 1.00 47.23  ? 54   ILE C C   1 
ATOM 3843 O O   . ILE C 2 54  ? 143.729 117.278 192.871 1.00 53.50  ? 54   ILE C O   1 
ATOM 3844 C CB  . ILE C 2 54  ? 145.375 116.488 195.412 1.00 51.25  ? 54   ILE C CB  1 
ATOM 3845 C CG1 . ILE C 2 54  ? 145.165 114.979 195.322 1.00 56.70  ? 54   ILE C CG1 1 
ATOM 3846 C CG2 . ILE C 2 54  ? 144.110 117.164 195.898 1.00 53.82  ? 54   ILE C CG2 1 
ATOM 3847 C CD1 . ILE C 2 54  ? 144.996 114.307 196.652 1.00 70.98  ? 54   ILE C CD1 1 
ATOM 3848 N N   . SER C 2 55  ? 145.143 115.668 192.163 1.00 48.42  ? 55   SER C N   1 
ATOM 3849 C CA  . SER C 2 55  ? 144.223 115.052 191.215 1.00 48.04  ? 55   SER C CA  1 
ATOM 3850 C C   . SER C 2 55  ? 143.770 113.741 191.845 1.00 57.96  ? 55   SER C C   1 
ATOM 3851 O O   . SER C 2 55  ? 144.510 112.757 191.849 1.00 62.46  ? 55   SER C O   1 
ATOM 3852 C CB  . SER C 2 55  ? 144.899 114.835 189.868 1.00 48.92  ? 55   SER C CB  1 
ATOM 3853 O OG  . SER C 2 55  ? 143.997 114.288 188.929 1.00 49.70  ? 55   SER C OG  1 
ATOM 3854 N N   . SER C 2 56  ? 142.551 113.735 192.387 1.00 61.44  ? 56   SER C N   1 
ATOM 3855 C CA  . SER C 2 56  ? 142.103 112.607 193.198 1.00 63.24  ? 56   SER C CA  1 
ATOM 3856 C C   . SER C 2 56  ? 142.034 111.319 192.387 1.00 65.72  ? 56   SER C C   1 
ATOM 3857 O O   . SER C 2 56  ? 142.406 110.248 192.881 1.00 65.69  ? 56   SER C O   1 
ATOM 3858 C CB  . SER C 2 56  ? 140.745 112.919 193.821 1.00 71.07  ? 56   SER C CB  1 
ATOM 3859 O OG  . SER C 2 56  ? 139.802 113.270 192.826 1.00 74.64  ? 56   SER C OG  1 
ATOM 3860 N N   . SER C 2 57  ? 141.550 111.397 191.146 1.00 62.97  ? 57   SER C N   1 
ATOM 3861 C CA  . SER C 2 57  ? 141.433 110.196 190.324 1.00 63.76  ? 57   SER C CA  1 
ATOM 3862 C C   . SER C 2 57  ? 142.800 109.584 190.050 1.00 65.77  ? 57   SER C C   1 
ATOM 3863 O O   . SER C 2 57  ? 143.025 108.395 190.301 1.00 69.93  ? 57   SER C O   1 
ATOM 3864 C CB  . SER C 2 57  ? 140.724 110.526 189.012 1.00 64.33  ? 57   SER C CB  1 
ATOM 3865 O OG  . SER C 2 57  ? 141.591 111.215 188.130 1.00 62.57  ? 57   SER C OG  1 
ATOM 3866 N N   . SER C 2 58  ? 143.734 110.389 189.544 1.00 63.32  ? 58   SER C N   1 
ATOM 3867 C CA  . SER C 2 58  ? 145.077 109.902 189.262 1.00 60.74  ? 58   SER C CA  1 
ATOM 3868 C C   . SER C 2 58  ? 145.908 109.715 190.523 1.00 59.16  ? 58   SER C C   1 
ATOM 3869 O O   . SER C 2 58  ? 146.838 108.903 190.522 1.00 63.06  ? 58   SER C O   1 
ATOM 3870 C CB  . SER C 2 58  ? 145.798 110.862 188.314 1.00 59.32  ? 58   SER C CB  1 
ATOM 3871 O OG  . SER C 2 58  ? 145.014 111.128 187.164 1.00 57.59  ? 58   SER C OG  1 
ATOM 3872 N N   . GLY C 2 59  ? 145.599 110.447 191.589 1.00 58.29  ? 59   GLY C N   1 
ATOM 3873 C CA  . GLY C 2 59  ? 146.378 110.398 192.805 1.00 58.37  ? 59   GLY C CA  1 
ATOM 3874 C C   . GLY C 2 59  ? 147.631 111.241 192.788 1.00 57.65  ? 59   GLY C C   1 
ATOM 3875 O O   . GLY C 2 59  ? 148.334 111.294 193.804 1.00 59.94  ? 59   GLY C O   1 
ATOM 3876 N N   . SER C 2 60  ? 147.928 111.909 191.677 1.00 54.60  ? 60   SER C N   1 
ATOM 3877 C CA  . SER C 2 60  ? 149.149 112.691 191.561 1.00 53.76  ? 60   SER C CA  1 
ATOM 3878 C C   . SER C 2 60  ? 148.980 114.047 192.228 1.00 49.33  ? 60   SER C C   1 
ATOM 3879 O O   . SER C 2 60  ? 147.959 114.716 192.058 1.00 51.00  ? 60   SER C O   1 
ATOM 3880 C CB  . SER C 2 60  ? 149.527 112.878 190.093 1.00 54.80  ? 60   SER C CB  1 
ATOM 3881 O OG  . SER C 2 60  ? 148.535 113.614 189.404 1.00 49.83  ? 60   SER C OG  1 
ATOM 3882 N N   . THR C 2 61  ? 149.990 114.446 192.993 1.00 46.08  ? 61   THR C N   1 
ATOM 3883 C CA  . THR C 2 61  ? 150.004 115.725 193.680 1.00 42.44  ? 61   THR C CA  1 
ATOM 3884 C C   . THR C 2 61  ? 151.285 116.461 193.330 1.00 44.18  ? 61   THR C C   1 
ATOM 3885 O O   . THR C 2 61  ? 152.302 115.852 192.995 1.00 49.88  ? 61   THR C O   1 
ATOM 3886 C CB  . THR C 2 61  ? 149.915 115.562 195.200 1.00 44.35  ? 61   THR C CB  1 
ATOM 3887 O OG1 . THR C 2 61  ? 151.124 114.972 195.687 1.00 52.52  ? 61   THR C OG1 1 
ATOM 3888 C CG2 . THR C 2 61  ? 148.748 114.675 195.579 1.00 47.10  ? 61   THR C CG2 1 
ATOM 3889 N N   . SER C 2 62  ? 151.228 117.785 193.412 1.00 40.41  ? 62   SER C N   1 
ATOM 3890 C CA  . SER C 2 62  ? 152.398 118.615 193.182 1.00 38.27  ? 62   SER C CA  1 
ATOM 3891 C C   . SER C 2 62  ? 152.391 119.755 194.186 1.00 40.60  ? 62   SER C C   1 
ATOM 3892 O O   . SER C 2 62  ? 151.371 120.052 194.808 1.00 45.19  ? 62   SER C O   1 
ATOM 3893 C CB  . SER C 2 62  ? 152.437 119.159 191.754 1.00 38.51  ? 62   SER C CB  1 
ATOM 3894 O OG  . SER C 2 62  ? 153.667 119.808 191.500 1.00 47.29  ? 62   SER C OG  1 
ATOM 3895 N N   . TYR C 2 63  ? 153.548 120.388 194.349 1.00 41.03  ? 63   TYR C N   1 
ATOM 3896 C CA  . TYR C 2 63  ? 153.691 121.483 195.294 1.00 44.29  ? 63   TYR C CA  1 
ATOM 3897 C C   . TYR C 2 63  ? 154.507 122.595 194.660 1.00 46.04  ? 63   TYR C C   1 
ATOM 3898 O O   . TYR C 2 63  ? 155.256 122.378 193.706 1.00 51.06  ? 63   TYR C O   1 
ATOM 3899 C CB  . TYR C 2 63  ? 154.356 121.028 196.594 1.00 49.95  ? 63   TYR C CB  1 
ATOM 3900 C CG  . TYR C 2 63  ? 153.648 119.882 197.262 1.00 50.11  ? 63   TYR C CG  1 
ATOM 3901 C CD1 . TYR C 2 63  ? 154.157 118.597 197.201 1.00 55.75  ? 63   TYR C CD1 1 
ATOM 3902 C CD2 . TYR C 2 63  ? 152.465 120.083 197.946 1.00 51.54  ? 63   TYR C CD2 1 
ATOM 3903 C CE1 . TYR C 2 63  ? 153.510 117.548 197.807 1.00 57.76  ? 63   TYR C CE1 1 
ATOM 3904 C CE2 . TYR C 2 63  ? 151.811 119.043 198.553 1.00 62.24  ? 63   TYR C CE2 1 
ATOM 3905 C CZ  . TYR C 2 63  ? 152.335 117.778 198.480 1.00 64.76  ? 63   TYR C CZ  1 
ATOM 3906 O OH  . TYR C 2 63  ? 151.677 116.740 199.090 1.00 73.24  ? 63   TYR C OH  1 
ATOM 3907 N N   . ALA C 2 64  ? 154.341 123.798 195.194 1.00 44.92  ? 64   ALA C N   1 
ATOM 3908 C CA  . ALA C 2 64  ? 155.170 124.917 194.789 1.00 53.00  ? 64   ALA C CA  1 
ATOM 3909 C C   . ALA C 2 64  ? 156.556 124.782 195.402 1.00 65.46  ? 64   ALA C C   1 
ATOM 3910 O O   . ALA C 2 64  ? 156.731 124.177 196.462 1.00 69.12  ? 64   ALA C O   1 
ATOM 3911 C CB  . ALA C 2 64  ? 154.538 126.240 195.209 1.00 54.14  ? 64   ALA C CB  1 
ATOM 3912 N N   . ASP C 2 65  ? 157.548 125.356 194.720 1.00 68.95  ? 65   ASP C N   1 
ATOM 3913 C CA  . ASP C 2 65  ? 158.927 125.224 195.176 1.00 70.90  ? 65   ASP C CA  1 
ATOM 3914 C C   . ASP C 2 65  ? 159.114 125.814 196.567 1.00 72.41  ? 65   ASP C C   1 
ATOM 3915 O O   . ASP C 2 65  ? 159.906 125.302 197.365 1.00 73.99  ? 65   ASP C O   1 
ATOM 3916 C CB  . ASP C 2 65  ? 159.872 125.888 194.175 1.00 78.74  ? 65   ASP C CB  1 
ATOM 3917 C CG  . ASP C 2 65  ? 159.283 127.143 193.565 1.00 83.42  ? 65   ASP C CG  1 
ATOM 3918 O OD1 . ASP C 2 65  ? 158.069 127.148 193.273 1.00 76.29  ? 65   ASP C OD1 1 
ATOM 3919 O OD2 . ASP C 2 65  ? 160.033 128.124 193.378 1.00 89.52  ? 65   ASP C OD2 1 
ATOM 3920 N N   . SER C 2 66  ? 158.390 126.890 196.878 1.00 74.26  ? 66   SER C N   1 
ATOM 3921 C CA  . SER C 2 66  ? 158.529 127.519 198.187 1.00 76.55  ? 66   SER C CA  1 
ATOM 3922 C C   . SER C 2 66  ? 157.965 126.648 199.302 1.00 76.81  ? 66   SER C C   1 
ATOM 3923 O O   . SER C 2 66  ? 158.429 126.734 200.444 1.00 81.57  ? 66   SER C O   1 
ATOM 3924 C CB  . SER C 2 66  ? 157.847 128.886 198.186 1.00 79.58  ? 66   SER C CB  1 
ATOM 3925 O OG  . SER C 2 66  ? 156.476 128.772 197.854 1.00 80.61  ? 66   SER C OG  1 
ATOM 3926 N N   . VAL C 2 67  ? 156.971 125.813 199.001 1.00 74.28  ? 67   VAL C N   1 
ATOM 3927 C CA  . VAL C 2 67  ? 156.340 124.954 199.996 1.00 75.59  ? 67   VAL C CA  1 
ATOM 3928 C C   . VAL C 2 67  ? 156.657 123.486 199.786 1.00 75.20  ? 67   VAL C C   1 
ATOM 3929 O O   . VAL C 2 67  ? 156.109 122.638 200.505 1.00 76.78  ? 67   VAL C O   1 
ATOM 3930 C CB  . VAL C 2 67  ? 154.816 125.162 200.030 1.00 73.05  ? 67   VAL C CB  1 
ATOM 3931 C CG1 . VAL C 2 67  ? 154.491 126.634 200.171 1.00 78.47  ? 67   VAL C CG1 1 
ATOM 3932 C CG2 . VAL C 2 67  ? 154.183 124.593 198.781 1.00 63.85  ? 67   VAL C CG2 1 
ATOM 3933 N N   . LYS C 2 68  ? 157.515 123.153 198.827 1.00 73.30  ? 68   LYS C N   1 
ATOM 3934 C CA  . LYS C 2 68  ? 157.826 121.758 198.555 1.00 70.27  ? 68   LYS C CA  1 
ATOM 3935 C C   . LYS C 2 68  ? 158.568 121.138 199.730 1.00 74.40  ? 68   LYS C C   1 
ATOM 3936 O O   . LYS C 2 68  ? 159.471 121.748 200.308 1.00 79.72  ? 68   LYS C O   1 
ATOM 3937 C CB  . LYS C 2 68  ? 158.663 121.640 197.284 1.00 70.31  ? 68   LYS C CB  1 
ATOM 3938 C CG  . LYS C 2 68  ? 158.946 120.213 196.852 1.00 72.64  ? 68   LYS C CG  1 
ATOM 3939 C CD  . LYS C 2 68  ? 157.699 119.547 196.310 1.00 68.89  ? 68   LYS C CD  1 
ATOM 3940 C CE  . LYS C 2 68  ? 157.935 118.077 196.025 1.00 70.47  ? 68   LYS C CE  1 
ATOM 3941 N NZ  . LYS C 2 68  ? 158.224 117.317 197.270 1.00 73.51  ? 68   LYS C NZ  1 
ATOM 3942 N N   . GLY C 2 69  ? 158.180 119.917 200.085 1.00 74.76  ? 69   GLY C N   1 
ATOM 3943 C CA  . GLY C 2 69  ? 158.822 119.196 201.162 1.00 79.92  ? 69   GLY C CA  1 
ATOM 3944 C C   . GLY C 2 69  ? 158.300 119.505 202.547 1.00 83.30  ? 69   GLY C C   1 
ATOM 3945 O O   . GLY C 2 69  ? 158.764 118.892 203.516 1.00 86.37  ? 69   GLY C O   1 
ATOM 3946 N N   . ARG C 2 70  ? 157.357 120.430 202.675 1.00 85.15  ? 70   ARG C N   1 
ATOM 3947 C CA  . ARG C 2 70  ? 156.760 120.768 203.957 1.00 89.79  ? 70   ARG C CA  1 
ATOM 3948 C C   . ARG C 2 70  ? 155.274 120.468 204.032 1.00 92.46  ? 70   ARG C C   1 
ATOM 3949 O O   . ARG C 2 70  ? 154.767 120.214 205.126 1.00 99.59  ? 70   ARG C O   1 
ATOM 3950 C CB  . ARG C 2 70  ? 156.975 122.256 204.271 1.00 91.46  ? 70   ARG C CB  1 
ATOM 3951 C CG  . ARG C 2 70  ? 158.429 122.665 204.388 1.00 88.84  ? 70   ARG C CG  1 
ATOM 3952 C CD  . ARG C 2 70  ? 158.612 124.113 203.976 1.00 94.01  ? 70   ARG C CD  1 
ATOM 3953 N NE  . ARG C 2 70  ? 157.634 124.987 204.611 1.00 100.99 ? 70   ARG C NE  1 
ATOM 3954 C CZ  . ARG C 2 70  ? 157.453 126.261 204.294 1.00 108.44 ? 70   ARG C CZ  1 
ATOM 3955 N NH1 . ARG C 2 70  ? 158.166 126.846 203.346 1.00 107.41 ? 70   ARG C NH1 1 
ATOM 3956 N NH2 . ARG C 2 70  ? 156.531 126.966 204.943 1.00 113.00 ? 70   ARG C NH2 1 
ATOM 3957 N N   . PHE C 2 71  ? 154.567 120.487 202.907 1.00 88.57  ? 71   PHE C N   1 
ATOM 3958 C CA  . PHE C 2 71  ? 153.129 120.278 202.877 1.00 86.66  ? 71   PHE C CA  1 
ATOM 3959 C C   . PHE C 2 71  ? 152.812 118.882 202.358 1.00 83.92  ? 71   PHE C C   1 
ATOM 3960 O O   . PHE C 2 71  ? 153.603 118.272 201.635 1.00 84.17  ? 71   PHE C O   1 
ATOM 3961 C CB  . PHE C 2 71  ? 152.430 121.321 201.999 1.00 84.86  ? 71   PHE C CB  1 
ATOM 3962 C CG  . PHE C 2 71  ? 152.466 122.718 202.557 1.00 91.19  ? 71   PHE C CG  1 
ATOM 3963 C CD1 . PHE C 2 71  ? 153.024 122.978 203.796 1.00 96.75  ? 71   PHE C CD1 1 
ATOM 3964 C CD2 . PHE C 2 71  ? 151.924 123.770 201.843 1.00 89.88  ? 71   PHE C CD2 1 
ATOM 3965 C CE1 . PHE C 2 71  ? 153.053 124.262 204.303 1.00 100.57 ? 71   PHE C CE1 1 
ATOM 3966 C CE2 . PHE C 2 71  ? 151.946 125.054 202.347 1.00 89.05  ? 71   PHE C CE2 1 
ATOM 3967 C CZ  . PHE C 2 71  ? 152.512 125.300 203.577 1.00 96.44  ? 71   PHE C CZ  1 
ATOM 3968 N N   . THR C 2 72  ? 151.644 118.383 202.748 1.00 85.24  ? 72   THR C N   1 
ATOM 3969 C CA  . THR C 2 72  ? 151.150 117.084 202.299 1.00 86.71  ? 72   THR C CA  1 
ATOM 3970 C C   . THR C 2 72  ? 149.678 117.244 201.958 1.00 84.50  ? 72   THR C C   1 
ATOM 3971 O O   . THR C 2 72  ? 148.856 117.465 202.850 1.00 88.25  ? 72   THR C O   1 
ATOM 3972 C CB  . THR C 2 72  ? 151.348 116.009 203.366 1.00 92.42  ? 72   THR C CB  1 
ATOM 3973 O OG1 . THR C 2 72  ? 152.747 115.748 203.532 1.00 93.04  ? 72   THR C OG1 1 
ATOM 3974 C CG2 . THR C 2 72  ? 150.641 114.723 202.967 1.00 91.27  ? 72   THR C CG2 1 
ATOM 3975 N N   . ILE C 2 73  ? 149.340 117.145 200.680 1.00 79.55  ? 73   ILE C N   1 
ATOM 3976 C CA  . ILE C 2 73  ? 147.966 117.312 200.229 1.00 79.13  ? 73   ILE C CA  1 
ATOM 3977 C C   . ILE C 2 73  ? 147.385 115.937 199.926 1.00 83.88  ? 73   ILE C C   1 
ATOM 3978 O O   . ILE C 2 73  ? 148.020 115.114 199.255 1.00 87.90  ? 73   ILE C O   1 
ATOM 3979 C CB  . ILE C 2 73  ? 147.889 118.250 199.012 1.00 68.19  ? 73   ILE C CB  1 
ATOM 3980 C CG1 . ILE C 2 73  ? 146.441 118.477 198.593 1.00 65.70  ? 73   ILE C CG1 1 
ATOM 3981 C CG2 . ILE C 2 73  ? 148.704 117.720 197.855 1.00 62.92  ? 73   ILE C CG2 1 
ATOM 3982 C CD1 . ILE C 2 73  ? 146.291 119.541 197.548 1.00 55.87  ? 73   ILE C CD1 1 
ATOM 3983 N N   . SER C 2 74  ? 146.195 115.673 200.458 1.00 87.01  ? 74   SER C N   1 
ATOM 3984 C CA  . SER C 2 74  ? 145.517 114.400 200.272 1.00 91.57  ? 74   SER C CA  1 
ATOM 3985 C C   . SER C 2 74  ? 144.048 114.676 199.993 1.00 95.27  ? 74   SER C C   1 
ATOM 3986 O O   . SER C 2 74  ? 143.594 115.821 200.038 1.00 97.75  ? 74   SER C O   1 
ATOM 3987 C CB  . SER C 2 74  ? 145.694 113.494 201.494 1.00 91.46  ? 74   SER C CB  1 
ATOM 3988 O OG  . SER C 2 74  ? 145.173 114.105 202.660 1.00 93.75  ? 74   SER C OG  1 
ATOM 3989 N N   . ALA C 2 75  ? 143.292 113.622 199.703 1.00 97.02  ? 75   ALA C N   1 
ATOM 3990 C CA  . ALA C 2 75  ? 141.872 113.787 199.439 1.00 104.16 ? 75   ALA C CA  1 
ATOM 3991 C C   . ALA C 2 75  ? 141.136 112.497 199.758 1.00 109.52 ? 75   ALA C C   1 
ATOM 3992 O O   . ALA C 2 75  ? 141.651 111.397 199.545 1.00 109.95 ? 75   ALA C O   1 
ATOM 3993 C CB  . ALA C 2 75  ? 141.610 114.194 197.985 1.00 96.99  ? 75   ALA C CB  1 
ATOM 3994 N N   . ASP C 2 76  ? 139.922 112.650 200.276 1.00 112.24 ? 76   ASP C N   1 
ATOM 3995 C CA  . ASP C 2 76  ? 138.997 111.544 200.482 1.00 115.42 ? 76   ASP C CA  1 
ATOM 3996 C C   . ASP C 2 76  ? 137.823 111.729 199.533 1.00 117.23 ? 76   ASP C C   1 
ATOM 3997 O O   . ASP C 2 76  ? 137.128 112.751 199.588 1.00 117.30 ? 76   ASP C O   1 
ATOM 3998 C CB  . ASP C 2 76  ? 138.518 111.482 201.932 1.00 118.81 ? 76   ASP C CB  1 
ATOM 3999 C CG  . ASP C 2 76  ? 139.624 111.101 202.894 1.00 121.34 ? 76   ASP C CG  1 
ATOM 4000 O OD1 . ASP C 2 76  ? 140.777 110.937 202.442 1.00 123.48 ? 76   ASP C OD1 1 
ATOM 4001 O OD2 . ASP C 2 76  ? 139.341 110.964 204.103 1.00 121.25 ? 76   ASP C OD2 1 
ATOM 4002 N N   . THR C 2 77  ? 137.613 110.745 198.661 1.00 120.84 ? 77   THR C N   1 
ATOM 4003 C CA  . THR C 2 77  ? 136.543 110.809 197.677 1.00 123.74 ? 77   THR C CA  1 
ATOM 4004 C C   . THR C 2 77  ? 135.194 110.382 198.237 1.00 125.22 ? 77   THR C C   1 
ATOM 4005 O O   . THR C 2 77  ? 134.168 110.644 197.600 1.00 121.02 ? 77   THR C O   1 
ATOM 4006 C CB  . THR C 2 77  ? 136.895 109.937 196.470 1.00 122.96 ? 77   THR C CB  1 
ATOM 4007 O OG1 . THR C 2 77  ? 136.955 108.564 196.875 1.00 127.00 ? 77   THR C OG1 1 
ATOM 4008 C CG2 . THR C 2 77  ? 138.245 110.344 195.904 1.00 112.94 ? 77   THR C CG2 1 
ATOM 4009 N N   . SER C 2 78  ? 135.170 109.728 199.401 1.00 127.49 ? 78   SER C N   1 
ATOM 4010 C CA  . SER C 2 78  ? 133.900 109.335 200.002 1.00 128.65 ? 78   SER C CA  1 
ATOM 4011 C C   . SER C 2 78  ? 133.077 110.552 200.403 1.00 128.46 ? 78   SER C C   1 
ATOM 4012 O O   . SER C 2 78  ? 131.864 110.594 200.170 1.00 129.43 ? 78   SER C O   1 
ATOM 4013 C CB  . SER C 2 78  ? 134.151 108.433 201.210 1.00 127.42 ? 78   SER C CB  1 
ATOM 4014 O OG  . SER C 2 78  ? 134.952 109.091 202.175 1.00 127.47 ? 78   SER C OG  1 
ATOM 4015 N N   . LYS C 2 79  ? 133.718 111.551 201.006 1.00 125.98 ? 79   LYS C N   1 
ATOM 4016 C CA  . LYS C 2 79  ? 133.053 112.780 201.414 1.00 123.52 ? 79   LYS C CA  1 
ATOM 4017 C C   . LYS C 2 79  ? 133.328 113.942 200.471 1.00 121.79 ? 79   LYS C C   1 
ATOM 4018 O O   . LYS C 2 79  ? 132.883 115.060 200.747 1.00 120.50 ? 79   LYS C O   1 
ATOM 4019 C CB  . LYS C 2 79  ? 133.479 113.162 202.834 1.00 124.27 ? 79   LYS C CB  1 
ATOM 4020 C CG  . LYS C 2 79  ? 133.191 112.096 203.876 1.00 127.94 ? 79   LYS C CG  1 
ATOM 4021 C CD  . LYS C 2 79  ? 133.780 112.474 205.223 1.00 129.07 ? 79   LYS C CD  1 
ATOM 4022 C CE  . LYS C 2 79  ? 135.277 112.711 205.114 1.00 126.45 ? 79   LYS C CE  1 
ATOM 4023 N NZ  . LYS C 2 79  ? 135.980 111.541 204.518 1.00 125.55 ? 79   LYS C NZ  1 
ATOM 4024 N N   . ASN C 2 80  ? 134.042 113.703 199.369 1.00 121.06 ? 80   ASN C N   1 
ATOM 4025 C CA  . ASN C 2 80  ? 134.417 114.751 198.420 1.00 116.62 ? 80   ASN C CA  1 
ATOM 4026 C C   . ASN C 2 80  ? 135.166 115.885 199.119 1.00 116.11 ? 80   ASN C C   1 
ATOM 4027 O O   . ASN C 2 80  ? 134.803 117.058 199.014 1.00 115.51 ? 80   ASN C O   1 
ATOM 4028 C CB  . ASN C 2 80  ? 133.192 115.286 197.673 1.00 114.30 ? 80   ASN C CB  1 
ATOM 4029 C CG  . ASN C 2 80  ? 132.567 114.253 196.760 1.00 114.93 ? 80   ASN C CG  1 
ATOM 4030 O OD1 . ASN C 2 80  ? 132.916 113.074 196.806 1.00 119.90 ? 80   ASN C OD1 1 
ATOM 4031 N ND2 . ASN C 2 80  ? 131.634 114.691 195.924 1.00 108.95 ? 80   ASN C ND2 1 
ATOM 4032 N N   . THR C 2 81  ? 136.225 115.527 199.842 1.00 116.58 ? 81   THR C N   1 
ATOM 4033 C CA  . THR C 2 81  ? 136.983 116.498 200.616 1.00 114.28 ? 81   THR C CA  1 
ATOM 4034 C C   . THR C 2 81  ? 138.464 116.410 200.281 1.00 111.23 ? 81   THR C C   1 
ATOM 4035 O O   . THR C 2 81  ? 138.976 115.351 199.911 1.00 114.12 ? 81   THR C O   1 
ATOM 4036 C CB  . THR C 2 81  ? 136.793 116.294 202.126 1.00 117.07 ? 81   THR C CB  1 
ATOM 4037 O OG1 . THR C 2 81  ? 137.130 114.946 202.474 1.00 120.20 ? 81   THR C OG1 1 
ATOM 4038 C CG2 . THR C 2 81  ? 135.353 116.574 202.527 1.00 117.25 ? 81   THR C CG2 1 
ATOM 4039 N N   . ALA C 2 82  ? 139.144 117.544 200.414 1.00 109.25 ? 82   ALA C N   1 
ATOM 4040 C CA  . ALA C 2 82  ? 140.588 117.635 200.278 1.00 107.40 ? 82   ALA C CA  1 
ATOM 4041 C C   . ALA C 2 82  ? 141.187 118.107 201.594 1.00 109.07 ? 82   ALA C C   1 
ATOM 4042 O O   . ALA C 2 82  ? 140.525 118.762 202.399 1.00 111.45 ? 82   ALA C O   1 
ATOM 4043 C CB  . ALA C 2 82  ? 140.993 118.591 199.152 1.00 99.85  ? 82   ALA C CB  1 
ATOM 4044 N N   . TYR C 2 83  ? 142.451 117.763 201.813 1.00 104.82 ? 83   TYR C N   1 
ATOM 4045 C CA  . TYR C 2 83  ? 143.141 118.125 203.040 1.00 103.35 ? 83   TYR C CA  1 
ATOM 4046 C C   . TYR C 2 83  ? 144.544 118.594 202.702 1.00 99.29  ? 83   TYR C C   1 
ATOM 4047 O O   . TYR C 2 83  ? 145.207 118.016 201.838 1.00 100.16 ? 83   TYR C O   1 
ATOM 4048 C CB  . TYR C 2 83  ? 143.208 116.947 204.018 1.00 104.66 ? 83   TYR C CB  1 
ATOM 4049 C CG  . TYR C 2 83  ? 141.903 116.203 204.169 1.00 110.24 ? 83   TYR C CG  1 
ATOM 4050 C CD1 . TYR C 2 83  ? 140.882 116.706 204.963 1.00 114.96 ? 83   TYR C CD1 1 
ATOM 4051 C CD2 . TYR C 2 83  ? 141.691 114.998 203.515 1.00 110.92 ? 83   TYR C CD2 1 
ATOM 4052 C CE1 . TYR C 2 83  ? 139.688 116.029 205.101 1.00 116.01 ? 83   TYR C CE1 1 
ATOM 4053 C CE2 . TYR C 2 83  ? 140.501 114.314 203.647 1.00 113.36 ? 83   TYR C CE2 1 
ATOM 4054 C CZ  . TYR C 2 83  ? 139.503 114.833 204.441 1.00 117.63 ? 83   TYR C CZ  1 
ATOM 4055 O OH  . TYR C 2 83  ? 138.315 114.153 204.575 1.00 121.97 ? 83   TYR C OH  1 
ATOM 4056 N N   . LEU C 2 84  ? 144.988 119.642 203.386 1.00 98.23  ? 84   LEU C N   1 
ATOM 4057 C CA  . LEU C 2 84  ? 146.350 120.141 203.274 1.00 94.42  ? 84   LEU C CA  1 
ATOM 4058 C C   . LEU C 2 84  ? 146.966 120.131 204.664 1.00 99.01  ? 84   LEU C C   1 
ATOM 4059 O O   . LEU C 2 84  ? 146.444 120.775 205.580 1.00 104.96 ? 84   LEU C O   1 
ATOM 4060 C CB  . LEU C 2 84  ? 146.375 121.546 202.673 1.00 92.11  ? 84   LEU C CB  1 
ATOM 4061 C CG  . LEU C 2 84  ? 147.750 122.159 202.429 1.00 88.21  ? 84   LEU C CG  1 
ATOM 4062 C CD1 . LEU C 2 84  ? 148.579 121.245 201.559 1.00 84.31  ? 84   LEU C CD1 1 
ATOM 4063 C CD2 . LEU C 2 84  ? 147.612 123.519 201.781 1.00 83.08  ? 84   LEU C CD2 1 
ATOM 4064 N N   . GLN C 2 85  ? 148.062 119.396 204.820 1.00 96.06  ? 85   GLN C N   1 
ATOM 4065 C CA  . GLN C 2 85  ? 148.760 119.261 206.089 1.00 101.16 ? 85   GLN C CA  1 
ATOM 4066 C C   . GLN C 2 85  ? 150.041 120.074 206.007 1.00 102.85 ? 85   GLN C C   1 
ATOM 4067 O O   . GLN C 2 85  ? 150.877 119.830 205.132 1.00 101.28 ? 85   GLN C O   1 
ATOM 4068 C CB  . GLN C 2 85  ? 149.068 117.794 206.387 1.00 102.00 ? 85   GLN C CB  1 
ATOM 4069 C CG  . GLN C 2 85  ? 149.170 117.462 207.863 1.00 105.37 ? 85   GLN C CG  1 
ATOM 4070 C CD  . GLN C 2 85  ? 147.813 117.389 208.532 1.00 109.09 ? 85   GLN C CD  1 
ATOM 4071 O OE1 . GLN C 2 85  ? 147.553 118.087 209.511 1.00 109.97 ? 85   GLN C OE1 1 
ATOM 4072 N NE2 . GLN C 2 85  ? 146.941 116.536 208.009 1.00 110.32 ? 85   GLN C NE2 1 
ATOM 4073 N N   . MET C 2 86  ? 150.190 121.031 206.912 1.00 110.95 ? 86   MET C N   1 
ATOM 4074 C CA  . MET C 2 86  ? 151.327 121.937 206.928 1.00 111.90 ? 86   MET C CA  1 
ATOM 4075 C C   . MET C 2 86  ? 152.189 121.643 208.145 1.00 117.95 ? 86   MET C C   1 
ATOM 4076 O O   . MET C 2 86  ? 151.685 121.593 209.273 1.00 120.72 ? 86   MET C O   1 
ATOM 4077 C CB  . MET C 2 86  ? 150.861 123.391 206.945 1.00 109.65 ? 86   MET C CB  1 
ATOM 4078 C CG  . MET C 2 86  ? 149.850 123.714 205.867 1.00 106.90 ? 86   MET C CG  1 
ATOM 4079 S SD  . MET C 2 86  ? 149.115 125.340 206.083 1.00 117.82 ? 86   MET C SD  1 
ATOM 4080 C CE  . MET C 2 86  ? 147.415 124.968 205.680 1.00 108.91 ? 86   MET C CE  1 
ATOM 4081 N N   . ASN C 2 87  ? 153.482 121.446 207.912 1.00 117.74 ? 87   ASN C N   1 
ATOM 4082 C CA  . ASN C 2 87  ? 154.439 121.172 208.970 1.00 120.84 ? 87   ASN C CA  1 
ATOM 4083 C C   . ASN C 2 87  ? 155.568 122.187 208.893 1.00 122.41 ? 87   ASN C C   1 
ATOM 4084 O O   . ASN C 2 87  ? 155.936 122.647 207.808 1.00 118.88 ? 87   ASN C O   1 
ATOM 4085 C CB  . ASN C 2 87  ? 154.998 119.749 208.863 1.00 119.39 ? 87   ASN C CB  1 
ATOM 4086 C CG  . ASN C 2 87  ? 153.906 118.699 208.805 1.00 119.05 ? 87   ASN C CG  1 
ATOM 4087 O OD1 . ASN C 2 87  ? 152.838 118.864 209.393 1.00 118.84 ? 87   ASN C OD1 1 
ATOM 4088 N ND2 . ASN C 2 87  ? 154.169 117.611 208.091 1.00 118.49 ? 87   ASN C ND2 1 
ATOM 4089 N N   . SER C 2 88  ? 156.112 122.533 210.058 1.00 125.93 ? 88   SER C N   1 
ATOM 4090 C CA  . SER C 2 88  ? 157.173 123.530 210.181 1.00 126.43 ? 88   SER C CA  1 
ATOM 4091 C C   . SER C 2 88  ? 156.749 124.854 209.545 1.00 127.69 ? 88   SER C C   1 
ATOM 4092 O O   . SER C 2 88  ? 157.342 125.338 208.579 1.00 125.33 ? 88   SER C O   1 
ATOM 4093 C CB  . SER C 2 88  ? 158.483 123.019 209.574 1.00 123.25 ? 88   SER C CB  1 
ATOM 4094 O OG  . SER C 2 88  ? 158.376 122.872 208.170 1.00 121.43 ? 88   SER C OG  1 
ATOM 4095 N N   . LEU C 2 89  ? 155.693 125.434 210.112 1.00 129.06 ? 89   LEU C N   1 
ATOM 4096 C CA  . LEU C 2 89  ? 155.167 126.694 209.609 1.00 127.83 ? 89   LEU C CA  1 
ATOM 4097 C C   . LEU C 2 89  ? 156.182 127.815 209.799 1.00 129.60 ? 89   LEU C C   1 
ATOM 4098 O O   . LEU C 2 89  ? 157.003 127.795 210.718 1.00 131.04 ? 89   LEU C O   1 
ATOM 4099 C CB  . LEU C 2 89  ? 153.859 127.045 210.317 1.00 128.97 ? 89   LEU C CB  1 
ATOM 4100 C CG  . LEU C 2 89  ? 152.660 126.164 209.972 1.00 127.37 ? 89   LEU C CG  1 
ATOM 4101 C CD1 . LEU C 2 89  ? 151.470 126.519 210.844 1.00 128.81 ? 89   LEU C CD1 1 
ATOM 4102 C CD2 . LEU C 2 89  ? 152.313 126.317 208.504 1.00 125.98 ? 89   LEU C CD2 1 
ATOM 4103 N N   . ARG C 2 90  ? 156.117 128.801 208.910 1.00 127.64 ? 90   ARG C N   1 
ATOM 4104 C CA  . ARG C 2 90  ? 157.042 129.923 208.898 1.00 127.41 ? 90   ARG C CA  1 
ATOM 4105 C C   . ARG C 2 90  ? 156.249 131.225 208.871 1.00 130.85 ? 90   ARG C C   1 
ATOM 4106 O O   . ARG C 2 90  ? 155.015 131.229 208.902 1.00 131.28 ? 90   ARG C O   1 
ATOM 4107 C CB  . ARG C 2 90  ? 157.997 129.831 207.702 1.00 124.91 ? 90   ARG C CB  1 
ATOM 4108 C CG  . ARG C 2 90  ? 158.895 128.607 207.730 1.00 122.74 ? 90   ARG C CG  1 
ATOM 4109 C CD  . ARG C 2 90  ? 159.473 128.314 206.358 1.00 120.16 ? 90   ARG C CD  1 
ATOM 4110 N NE  . ARG C 2 90  ? 160.113 129.485 205.772 1.00 127.39 ? 90   ARG C NE  1 
ATOM 4111 C CZ  . ARG C 2 90  ? 160.704 129.498 204.586 1.00 126.97 ? 90   ARG C CZ  1 
ATOM 4112 N NH1 . ARG C 2 90  ? 160.763 128.414 203.831 1.00 118.20 ? 90   ARG C NH1 1 
ATOM 4113 N NH2 . ARG C 2 90  ? 161.251 130.628 204.146 1.00 128.89 ? 90   ARG C NH2 1 
ATOM 4114 N N   . ALA C 2 91  ? 156.974 132.344 208.822 1.00 133.64 ? 91   ALA C N   1 
ATOM 4115 C CA  . ALA C 2 91  ? 156.318 133.647 208.807 1.00 134.53 ? 91   ALA C CA  1 
ATOM 4116 C C   . ALA C 2 91  ? 155.609 133.898 207.482 1.00 133.27 ? 91   ALA C C   1 
ATOM 4117 O O   . ALA C 2 91  ? 154.544 134.525 207.452 1.00 131.51 ? 91   ALA C O   1 
ATOM 4118 C CB  . ALA C 2 91  ? 157.337 134.750 209.090 1.00 134.37 ? 91   ALA C CB  1 
ATOM 4119 N N   . GLU C 2 92  ? 156.185 133.419 206.377 1.00 134.00 ? 92   GLU C N   1 
ATOM 4120 C CA  . GLU C 2 92  ? 155.595 133.656 205.065 1.00 133.94 ? 92   GLU C CA  1 
ATOM 4121 C C   . GLU C 2 92  ? 154.288 132.901 204.866 1.00 129.70 ? 92   GLU C C   1 
ATOM 4122 O O   . GLU C 2 92  ? 153.472 133.310 204.034 1.00 122.86 ? 92   GLU C O   1 
ATOM 4123 C CB  . GLU C 2 92  ? 156.583 133.271 203.961 1.00 135.61 ? 92   GLU C CB  1 
ATOM 4124 C CG  . GLU C 2 92  ? 157.928 133.979 204.038 1.00 137.35 ? 92   GLU C CG  1 
ATOM 4125 C CD  . GLU C 2 92  ? 158.900 133.289 204.975 1.00 137.38 ? 92   GLU C CD  1 
ATOM 4126 O OE1 . GLU C 2 92  ? 158.606 132.157 205.409 1.00 134.44 ? 92   GLU C OE1 1 
ATOM 4127 O OE2 . GLU C 2 92  ? 159.958 133.880 205.277 1.00 139.78 ? 92   GLU C OE2 1 
ATOM 4128 N N   . ASP C 2 93  ? 154.069 131.814 205.608 1.00 127.86 ? 93   ASP C N   1 
ATOM 4129 C CA  . ASP C 2 93  ? 152.852 131.028 205.452 1.00 122.28 ? 93   ASP C CA  1 
ATOM 4130 C C   . ASP C 2 93  ? 151.615 131.734 205.991 1.00 121.79 ? 93   ASP C C   1 
ATOM 4131 O O   . ASP C 2 93  ? 150.502 131.249 205.765 1.00 122.08 ? 93   ASP C O   1 
ATOM 4132 C CB  . ASP C 2 93  ? 153.015 129.671 206.136 1.00 122.72 ? 93   ASP C CB  1 
ATOM 4133 C CG  . ASP C 2 93  ? 154.143 128.856 205.543 1.00 120.66 ? 93   ASP C CG  1 
ATOM 4134 O OD1 . ASP C 2 93  ? 154.895 129.402 204.710 1.00 118.46 ? 93   ASP C OD1 1 
ATOM 4135 O OD2 . ASP C 2 93  ? 154.277 127.668 205.903 1.00 120.09 ? 93   ASP C OD2 1 
ATOM 4136 N N   . THR C 2 94  ? 151.778 132.852 206.695 1.00 123.56 ? 94   THR C N   1 
ATOM 4137 C CA  . THR C 2 94  ? 150.637 133.632 207.163 1.00 126.21 ? 94   THR C CA  1 
ATOM 4138 C C   . THR C 2 94  ? 149.917 134.222 205.958 1.00 124.23 ? 94   THR C C   1 
ATOM 4139 O O   . THR C 2 94  ? 150.399 135.182 205.349 1.00 125.64 ? 94   THR C O   1 
ATOM 4140 C CB  . THR C 2 94  ? 151.102 134.732 208.112 1.00 129.01 ? 94   THR C CB  1 
ATOM 4141 O OG1 . THR C 2 94  ? 151.628 134.144 209.309 1.00 131.41 ? 94   THR C OG1 1 
ATOM 4142 C CG2 . THR C 2 94  ? 149.948 135.657 208.468 1.00 125.95 ? 94   THR C CG2 1 
ATOM 4143 N N   . ALA C 2 95  ? 148.766 133.654 205.611 1.00 120.58 ? 95   ALA C N   1 
ATOM 4144 C CA  . ALA C 2 95  ? 148.069 134.049 204.393 1.00 113.77 ? 95   ALA C CA  1 
ATOM 4145 C C   . ALA C 2 95  ? 146.664 133.466 204.418 1.00 112.52 ? 95   ALA C C   1 
ATOM 4146 O O   . ALA C 2 95  ? 146.298 132.709 205.320 1.00 115.28 ? 95   ALA C O   1 
ATOM 4147 C CB  . ALA C 2 95  ? 148.823 133.587 203.144 1.00 109.14 ? 95   ALA C CB  1 
ATOM 4148 N N   . VAL C 2 96  ? 145.879 133.830 203.407 1.00 112.06 ? 96   VAL C N   1 
ATOM 4149 C CA  . VAL C 2 96  ? 144.546 133.279 203.203 1.00 111.70 ? 96   VAL C CA  1 
ATOM 4150 C C   . VAL C 2 96  ? 144.644 132.196 202.139 1.00 106.25 ? 96   VAL C C   1 
ATOM 4151 O O   . VAL C 2 96  ? 145.138 132.446 201.034 1.00 101.57 ? 96   VAL C O   1 
ATOM 4152 C CB  . VAL C 2 96  ? 143.548 134.372 202.788 1.00 109.34 ? 96   VAL C CB  1 
ATOM 4153 C CG1 . VAL C 2 96  ? 142.120 133.870 202.932 1.00 106.49 ? 96   VAL C CG1 1 
ATOM 4154 C CG2 . VAL C 2 96  ? 143.769 135.630 203.607 1.00 110.35 ? 96   VAL C CG2 1 
ATOM 4155 N N   . TYR C 2 97  ? 144.182 130.996 202.468 1.00 104.70 ? 97   TYR C N   1 
ATOM 4156 C CA  . TYR C 2 97  ? 144.259 129.854 201.569 1.00 97.69  ? 97   TYR C CA  1 
ATOM 4157 C C   . TYR C 2 97  ? 142.901 129.609 200.928 1.00 96.05  ? 97   TYR C C   1 
ATOM 4158 O O   . TYR C 2 97  ? 141.877 129.570 201.620 1.00 99.42  ? 97   TYR C O   1 
ATOM 4159 C CB  . TYR C 2 97  ? 144.729 128.606 202.315 1.00 98.07  ? 97   TYR C CB  1 
ATOM 4160 C CG  . TYR C 2 97  ? 146.216 128.578 202.572 1.00 99.95  ? 97   TYR C CG  1 
ATOM 4161 C CD1 . TYR C 2 97  ? 146.791 129.403 203.526 1.00 104.26 ? 97   TYR C CD1 1 
ATOM 4162 C CD2 . TYR C 2 97  ? 147.045 127.725 201.861 1.00 94.04  ? 97   TYR C CD2 1 
ATOM 4163 C CE1 . TYR C 2 97  ? 148.150 129.381 203.760 1.00 103.74 ? 97   TYR C CE1 1 
ATOM 4164 C CE2 . TYR C 2 97  ? 148.405 127.696 202.092 1.00 94.52  ? 97   TYR C CE2 1 
ATOM 4165 C CZ  . TYR C 2 97  ? 148.951 128.526 203.043 1.00 98.52  ? 97   TYR C CZ  1 
ATOM 4166 O OH  . TYR C 2 97  ? 150.305 128.503 203.278 1.00 98.06  ? 97   TYR C OH  1 
ATOM 4167 N N   . TYR C 2 98  ? 142.902 129.449 199.606 1.00 89.24  ? 98   TYR C N   1 
ATOM 4168 C CA  . TYR C 2 98  ? 141.707 129.197 198.820 1.00 87.20  ? 98   TYR C CA  1 
ATOM 4169 C C   . TYR C 2 98  ? 141.812 127.824 198.177 1.00 77.71  ? 98   TYR C C   1 
ATOM 4170 O O   . TYR C 2 98  ? 142.889 127.417 197.726 1.00 71.52  ? 98   TYR C O   1 
ATOM 4171 C CB  . TYR C 2 98  ? 141.517 130.257 197.732 1.00 88.44  ? 98   TYR C CB  1 
ATOM 4172 C CG  . TYR C 2 98  ? 141.551 131.681 198.231 1.00 95.33  ? 98   TYR C CG  1 
ATOM 4173 C CD1 . TYR C 2 98  ? 142.745 132.384 198.296 1.00 95.50  ? 98   TYR C CD1 1 
ATOM 4174 C CD2 . TYR C 2 98  ? 140.388 132.327 198.627 1.00 97.77  ? 98   TYR C CD2 1 
ATOM 4175 C CE1 . TYR C 2 98  ? 142.782 133.685 198.747 1.00 101.46 ? 98   TYR C CE1 1 
ATOM 4176 C CE2 . TYR C 2 98  ? 140.416 133.629 199.079 1.00 102.06 ? 98   TYR C CE2 1 
ATOM 4177 C CZ  . TYR C 2 98  ? 141.616 134.303 199.138 1.00 105.96 ? 98   TYR C CZ  1 
ATOM 4178 O OH  . TYR C 2 98  ? 141.651 135.602 199.588 1.00 110.50 ? 98   TYR C OH  1 
ATOM 4179 N N   . CYS C 2 99  ? 140.687 127.119 198.137 1.00 83.77  ? 99   CYS C N   1 
ATOM 4180 C CA  . CYS C 2 99  ? 140.595 125.788 197.546 1.00 79.54  ? 99   CYS C CA  1 
ATOM 4181 C C   . CYS C 2 99  ? 139.887 125.931 196.204 1.00 73.92  ? 99   CYS C C   1 
ATOM 4182 O O   . CYS C 2 99  ? 138.658 125.950 196.125 1.00 78.52  ? 99   CYS C O   1 
ATOM 4183 C CB  . CYS C 2 99  ? 139.854 124.841 198.480 1.00 86.85  ? 99   CYS C CB  1 
ATOM 4184 S SG  . CYS C 2 99  ? 139.571 123.184 197.839 1.00 92.45  ? 99   CYS C SG  1 
ATOM 4185 N N   . ALA C 2 100 ? 140.673 126.036 195.142 1.00 57.63  ? 100  ALA C N   1 
ATOM 4186 C CA  . ALA C 2 100 ? 140.137 126.182 193.800 1.00 51.68  ? 100  ALA C CA  1 
ATOM 4187 C C   . ALA C 2 100 ? 139.905 124.817 193.166 1.00 51.17  ? 100  ALA C C   1 
ATOM 4188 O O   . ALA C 2 100 ? 140.537 123.823 193.522 1.00 54.44  ? 100  ALA C O   1 
ATOM 4189 C CB  . ALA C 2 100 ? 141.080 127.011 192.937 1.00 48.85  ? 100  ALA C CB  1 
ATOM 4190 N N   . ARG C 2 101 ? 138.980 124.782 192.213 1.00 49.45  ? 101  ARG C N   1 
ATOM 4191 C CA  . ARG C 2 101 ? 138.609 123.563 191.509 1.00 44.85  ? 101  ARG C CA  1 
ATOM 4192 C C   . ARG C 2 101 ? 138.922 123.729 190.032 1.00 40.47  ? 101  ARG C C   1 
ATOM 4193 O O   . ARG C 2 101 ? 138.506 124.714 189.419 1.00 46.92  ? 101  ARG C O   1 
ATOM 4194 C CB  . ARG C 2 101 ? 137.123 123.258 191.692 1.00 57.03  ? 101  ARG C CB  1 
ATOM 4195 C CG  . ARG C 2 101 ? 136.630 122.092 190.869 1.00 59.69  ? 101  ARG C CG  1 
ATOM 4196 C CD  . ARG C 2 101 ? 135.122 122.119 190.708 1.00 65.63  ? 101  ARG C CD  1 
ATOM 4197 N NE  . ARG C 2 101 ? 134.695 123.005 189.632 1.00 65.37  ? 101  ARG C NE  1 
ATOM 4198 C CZ  . ARG C 2 101 ? 133.442 123.124 189.216 1.00 71.76  ? 101  ARG C CZ  1 
ATOM 4199 N NH1 . ARG C 2 101 ? 132.460 122.435 189.774 1.00 78.88  ? 101  ARG C NH1 1 
ATOM 4200 N NH2 . ARG C 2 101 ? 133.167 123.951 188.213 1.00 71.05  ? 101  ARG C NH2 1 
ATOM 4201 N N   . TRP C 2 102 ? 139.633 122.764 189.456 1.00 33.42  ? 102  TRP C N   1 
ATOM 4202 C CA  . TRP C 2 102 ? 140.032 122.840 188.059 1.00 29.41  ? 102  TRP C CA  1 
ATOM 4203 C C   . TRP C 2 102 ? 139.697 121.528 187.367 1.00 35.19  ? 102  TRP C C   1 
ATOM 4204 O O   . TRP C 2 102 ? 139.972 120.454 187.906 1.00 40.68  ? 102  TRP C O   1 
ATOM 4205 C CB  . TRP C 2 102 ? 141.519 123.148 187.960 1.00 25.88  ? 102  TRP C CB  1 
ATOM 4206 C CG  . TRP C 2 102 ? 142.012 123.450 186.605 1.00 23.88  ? 102  TRP C CG  1 
ATOM 4207 C CD1 . TRP C 2 102 ? 141.296 123.500 185.459 1.00 24.97  ? 102  TRP C CD1 1 
ATOM 4208 C CD2 . TRP C 2 102 ? 143.355 123.749 186.253 1.00 20.90  ? 102  TRP C CD2 1 
ATOM 4209 N NE1 . TRP C 2 102 ? 142.110 123.809 184.407 1.00 22.04  ? 102  TRP C NE1 1 
ATOM 4210 C CE2 . TRP C 2 102 ? 143.385 123.967 184.874 1.00 18.21  ? 102  TRP C CE2 1 
ATOM 4211 C CE3 . TRP C 2 102 ? 144.539 123.858 186.976 1.00 22.46  ? 102  TRP C CE3 1 
ATOM 4212 C CZ2 . TRP C 2 102 ? 144.548 124.280 184.205 1.00 19.39  ? 102  TRP C CZ2 1 
ATOM 4213 C CZ3 . TRP C 2 102 ? 145.684 124.171 186.312 1.00 21.77  ? 102  TRP C CZ3 1 
ATOM 4214 C CH2 . TRP C 2 102 ? 145.687 124.378 184.942 1.00 21.35  ? 102  TRP C CH2 1 
ATOM 4215 N N   . GLY C 2 103 ? 139.113 121.616 186.175 1.00 30.24  ? 103  GLY C N   1 
ATOM 4216 C CA  . GLY C 2 103 ? 138.628 120.449 185.465 1.00 32.50  ? 103  GLY C CA  1 
ATOM 4217 C C   . GLY C 2 103 ? 139.692 119.492 184.972 1.00 33.13  ? 103  GLY C C   1 
ATOM 4218 O O   . GLY C 2 103 ? 140.833 119.524 185.436 1.00 35.14  ? 103  GLY C O   1 
ATOM 4219 N N   . TYR C 2 104 ? 139.328 118.630 184.028 1.00 35.81  ? 104  TYR C N   1 
ATOM 4220 C CA  . TYR C 2 104 ? 140.213 117.588 183.531 1.00 32.07  ? 104  TYR C CA  1 
ATOM 4221 C C   . TYR C 2 104 ? 140.314 117.651 182.016 1.00 32.22  ? 104  TYR C C   1 
ATOM 4222 O O   . TYR C 2 104 ? 139.315 117.859 181.324 1.00 36.71  ? 104  TYR C O   1 
ATOM 4223 C CB  . TYR C 2 104 ? 139.725 116.204 183.949 1.00 33.87  ? 104  TYR C CB  1 
ATOM 4224 C CG  . TYR C 2 104 ? 140.276 115.742 185.269 1.00 37.63  ? 104  TYR C CG  1 
ATOM 4225 C CD1 . TYR C 2 104 ? 141.591 115.992 185.613 1.00 36.76  ? 104  TYR C CD1 1 
ATOM 4226 C CD2 . TYR C 2 104 ? 139.482 115.061 186.170 1.00 45.09  ? 104  TYR C CD2 1 
ATOM 4227 C CE1 . TYR C 2 104 ? 142.100 115.575 186.815 1.00 40.77  ? 104  TYR C CE1 1 
ATOM 4228 C CE2 . TYR C 2 104 ? 139.983 114.641 187.376 1.00 49.49  ? 104  TYR C CE2 1 
ATOM 4229 C CZ  . TYR C 2 104 ? 141.291 114.901 187.694 1.00 50.30  ? 104  TYR C CZ  1 
ATOM 4230 O OH  . TYR C 2 104 ? 141.795 114.483 188.899 1.00 56.27  ? 104  TYR C OH  1 
ATOM 4231 N N   . TRP C 2 105 ? 141.525 117.468 181.511 1.00 30.44  ? 105  TRP C N   1 
ATOM 4232 C CA  . TRP C 2 105 ? 141.725 117.368 180.077 1.00 31.50  ? 105  TRP C CA  1 
ATOM 4233 C C   . TRP C 2 105 ? 141.077 116.084 179.561 1.00 36.24  ? 105  TRP C C   1 
ATOM 4234 O O   . TRP C 2 105 ? 141.123 115.052 180.237 1.00 41.39  ? 105  TRP C O   1 
ATOM 4235 C CB  . TRP C 2 105 ? 143.221 117.384 179.756 1.00 28.42  ? 105  TRP C CB  1 
ATOM 4236 C CG  . TRP C 2 105 ? 143.544 117.433 178.302 1.00 25.53  ? 105  TRP C CG  1 
ATOM 4237 C CD1 . TRP C 2 105 ? 143.924 116.391 177.513 1.00 28.92  ? 105  TRP C CD1 1 
ATOM 4238 C CD2 . TRP C 2 105 ? 143.512 118.584 177.458 1.00 24.30  ? 105  TRP C CD2 1 
ATOM 4239 N NE1 . TRP C 2 105 ? 144.131 116.822 176.229 1.00 31.04  ? 105  TRP C NE1 1 
ATOM 4240 C CE2 . TRP C 2 105 ? 143.881 118.167 176.170 1.00 28.85  ? 105  TRP C CE2 1 
ATOM 4241 C CE3 . TRP C 2 105 ? 143.202 119.927 177.664 1.00 26.41  ? 105  TRP C CE3 1 
ATOM 4242 C CZ2 . TRP C 2 105 ? 143.952 119.043 175.099 1.00 29.84  ? 105  TRP C CZ2 1 
ATOM 4243 C CZ3 . TRP C 2 105 ? 143.273 120.791 176.602 1.00 23.36  ? 105  TRP C CZ3 1 
ATOM 4244 C CH2 . TRP C 2 105 ? 143.642 120.350 175.336 1.00 24.54  ? 105  TRP C CH2 1 
ATOM 4245 N N   . PRO C 2 106 ? 140.460 116.110 178.374 1.00 33.13  ? 106  PRO C N   1 
ATOM 4246 C CA  . PRO C 2 106 ? 140.295 117.229 177.448 1.00 32.66  ? 106  PRO C CA  1 
ATOM 4247 C C   . PRO C 2 106 ? 138.980 117.955 177.628 1.00 35.79  ? 106  PRO C C   1 
ATOM 4248 O O   . PRO C 2 106 ? 138.177 117.613 178.488 1.00 38.33  ? 106  PRO C O   1 
ATOM 4249 C CB  . PRO C 2 106 ? 140.352 116.535 176.091 1.00 33.84  ? 106  PRO C CB  1 
ATOM 4250 C CG  . PRO C 2 106 ? 139.626 115.252 176.350 1.00 36.66  ? 106  PRO C CG  1 
ATOM 4251 C CD  . PRO C 2 106 ? 139.977 114.858 177.770 1.00 35.46  ? 106  PRO C CD  1 
ATOM 4252 N N   . GLY C 2 107 ? 138.735 118.967 176.809 1.00 36.71  ? 107  GLY C N   1 
ATOM 4253 C CA  . GLY C 2 107 ? 137.449 119.631 176.783 1.00 38.52  ? 107  GLY C CA  1 
ATOM 4254 C C   . GLY C 2 107 ? 137.470 120.961 177.501 1.00 37.60  ? 107  GLY C C   1 
ATOM 4255 O O   . GLY C 2 107 ? 138.492 121.427 178.010 1.00 37.13  ? 107  GLY C O   1 
ATOM 4256 N N   . GLU C 2 108 ? 136.296 121.575 177.523 1.00 41.23  ? 108  GLU C N   1 
ATOM 4257 C CA  . GLU C 2 108 ? 136.057 122.865 178.153 1.00 39.75  ? 108  GLU C CA  1 
ATOM 4258 C C   . GLU C 2 108 ? 136.193 122.839 179.675 1.00 39.81  ? 108  GLU C C   1 
ATOM 4259 O O   . GLU C 2 108 ? 136.498 123.883 180.262 1.00 41.74  ? 108  GLU C O   1 
ATOM 4260 C CB  . GLU C 2 108 ? 134.672 123.384 177.765 1.00 41.76  ? 108  GLU C CB  1 
ATOM 4261 C CG  . GLU C 2 108 ? 134.630 124.879 177.495 1.00 48.20  ? 108  GLU C CG  1 
ATOM 4262 C CD  . GLU C 2 108 ? 135.471 125.283 176.297 1.00 56.36  ? 108  GLU C CD  1 
ATOM 4263 O OE1 . GLU C 2 108 ? 135.731 124.424 175.428 1.00 57.74  ? 108  GLU C OE1 1 
ATOM 4264 O OE2 . GLU C 2 108 ? 135.876 126.461 176.223 1.00 60.31  ? 108  GLU C OE2 1 
ATOM 4265 N N   . PRO C 2 109 ? 135.954 121.714 180.363 1.00 37.88  ? 109  PRO C N   1 
ATOM 4266 C CA  . PRO C 2 109 ? 136.250 121.697 181.805 1.00 39.39  ? 109  PRO C CA  1 
ATOM 4267 C C   . PRO C 2 109 ? 137.681 122.074 182.139 1.00 34.77  ? 109  PRO C C   1 
ATOM 4268 O O   . PRO C 2 109 ? 137.917 122.716 183.168 1.00 36.94  ? 109  PRO C O   1 
ATOM 4269 C CB  . PRO C 2 109 ? 135.936 120.252 182.199 1.00 37.41  ? 109  PRO C CB  1 
ATOM 4270 C CG  . PRO C 2 109 ? 134.839 119.883 181.312 1.00 38.57  ? 109  PRO C CG  1 
ATOM 4271 C CD  . PRO C 2 109 ? 135.105 120.565 179.995 1.00 35.96  ? 109  PRO C CD  1 
ATOM 4272 N N   . TRP C 2 110 ? 138.647 121.690 181.306 1.00 28.80  ? 110  TRP C N   1 
ATOM 4273 C CA  . TRP C 2 110 ? 140.029 122.066 181.573 1.00 24.95  ? 110  TRP C CA  1 
ATOM 4274 C C   . TRP C 2 110 ? 140.255 123.550 181.329 1.00 25.97  ? 110  TRP C C   1 
ATOM 4275 O O   . TRP C 2 110 ? 140.964 124.209 182.095 1.00 28.24  ? 110  TRP C O   1 
ATOM 4276 C CB  . TRP C 2 110 ? 140.982 121.236 180.717 1.00 23.17  ? 110  TRP C CB  1 
ATOM 4277 C CG  . TRP C 2 110 ? 142.411 121.443 181.076 1.00 20.90  ? 110  TRP C CG  1 
ATOM 4278 C CD1 . TRP C 2 110 ? 143.117 120.780 182.031 1.00 22.92  ? 110  TRP C CD1 1 
ATOM 4279 C CD2 . TRP C 2 110 ? 143.314 122.384 180.493 1.00 17.44  ? 110  TRP C CD2 1 
ATOM 4280 N NE1 . TRP C 2 110 ? 144.403 121.248 182.078 1.00 19.35  ? 110  TRP C NE1 1 
ATOM 4281 C CE2 . TRP C 2 110 ? 144.546 122.236 181.143 1.00 15.94  ? 110  TRP C CE2 1 
ATOM 4282 C CE3 . TRP C 2 110 ? 143.199 123.338 179.485 1.00 20.24  ? 110  TRP C CE3 1 
ATOM 4283 C CZ2 . TRP C 2 110 ? 145.649 123.004 180.818 1.00 15.43  ? 110  TRP C CZ2 1 
ATOM 4284 C CZ3 . TRP C 2 110 ? 144.297 124.099 179.168 1.00 19.10  ? 110  TRP C CZ3 1 
ATOM 4285 C CH2 . TRP C 2 110 ? 145.501 123.929 179.827 1.00 15.47  ? 110  TRP C CH2 1 
ATOM 4286 N N   . TRP C 2 111 ? 139.654 124.099 180.273 1.00 26.80  ? 111  TRP C N   1 
ATOM 4287 C CA  . TRP C 2 111 ? 139.892 125.489 179.912 1.00 26.06  ? 111  TRP C CA  1 
ATOM 4288 C C   . TRP C 2 111 ? 139.255 126.475 180.877 1.00 29.06  ? 111  TRP C C   1 
ATOM 4289 O O   . TRP C 2 111 ? 139.604 127.656 180.839 1.00 32.88  ? 111  TRP C O   1 
ATOM 4290 C CB  . TRP C 2 111 ? 139.393 125.759 178.497 1.00 27.28  ? 111  TRP C CB  1 
ATOM 4291 C CG  . TRP C 2 111 ? 140.211 125.094 177.445 1.00 28.99  ? 111  TRP C CG  1 
ATOM 4292 C CD1 . TRP C 2 111 ? 139.968 123.892 176.863 1.00 30.94  ? 111  TRP C CD1 1 
ATOM 4293 C CD2 . TRP C 2 111 ? 141.411 125.593 176.848 1.00 26.44  ? 111  TRP C CD2 1 
ATOM 4294 N NE1 . TRP C 2 111 ? 140.939 123.608 175.940 1.00 29.04  ? 111  TRP C NE1 1 
ATOM 4295 C CE2 . TRP C 2 111 ? 141.838 124.640 175.913 1.00 25.92  ? 111  TRP C CE2 1 
ATOM 4296 C CE3 . TRP C 2 111 ? 142.165 126.754 177.014 1.00 27.17  ? 111  TRP C CE3 1 
ATOM 4297 C CZ2 . TRP C 2 111 ? 142.983 124.811 175.147 1.00 25.12  ? 111  TRP C CZ2 1 
ATOM 4298 C CZ3 . TRP C 2 111 ? 143.300 126.919 176.255 1.00 27.69  ? 111  TRP C CZ3 1 
ATOM 4299 C CH2 . TRP C 2 111 ? 143.698 125.956 175.334 1.00 25.02  ? 111  TRP C CH2 1 
ATOM 4300 N N   . LYS C 2 112 ? 138.333 126.033 181.728 1.00 32.43  ? 112  LYS C N   1 
ATOM 4301 C CA  . LYS C 2 112 ? 137.761 126.894 182.761 1.00 35.62  ? 112  LYS C CA  1 
ATOM 4302 C C   . LYS C 2 112 ? 138.596 126.728 184.026 1.00 34.63  ? 112  LYS C C   1 
ATOM 4303 O O   . LYS C 2 112 ? 138.218 126.052 184.983 1.00 37.74  ? 112  LYS C O   1 
ATOM 4304 C CB  . LYS C 2 112 ? 136.297 126.551 182.994 1.00 39.87  ? 112  LYS C CB  1 
ATOM 4305 C CG  . LYS C 2 112 ? 135.444 126.660 181.752 1.00 44.59  ? 112  LYS C CG  1 
ATOM 4306 C CD  . LYS C 2 112 ? 134.043 126.147 181.998 1.00 49.23  ? 112  LYS C CD  1 
ATOM 4307 C CE  . LYS C 2 112 ? 133.228 126.160 180.720 1.00 52.11  ? 112  LYS C CE  1 
ATOM 4308 N NZ  . LYS C 2 112 ? 131.866 125.607 180.936 1.00 53.40  ? 112  LYS C NZ  1 
ATOM 4309 N N   . ALA C 2 113 ? 139.760 127.360 184.019 1.00 30.09  ? 113  ALA C N   1 
ATOM 4310 C CA  . ALA C 2 113 ? 140.707 127.208 185.111 1.00 28.34  ? 113  ALA C CA  1 
ATOM 4311 C C   . ALA C 2 113 ? 140.174 127.875 186.363 1.00 34.07  ? 113  ALA C C   1 
ATOM 4312 O O   . ALA C 2 113 ? 139.900 129.077 186.356 1.00 49.39  ? 113  ALA C O   1 
ATOM 4313 C CB  . ALA C 2 113 ? 142.046 127.821 184.733 1.00 32.16  ? 113  ALA C CB  1 
ATOM 4314 N N   . PHE C 2 114 ? 140.062 127.112 187.443 1.00 33.06  ? 114  PHE C N   1 
ATOM 4315 C CA  . PHE C 2 114 ? 139.636 127.642 188.735 1.00 39.75  ? 114  PHE C CA  1 
ATOM 4316 C C   . PHE C 2 114 ? 138.321 128.400 188.603 1.00 48.21  ? 114  PHE C C   1 
ATOM 4317 O O   . PHE C 2 114 ? 138.189 129.548 189.030 1.00 54.59  ? 114  PHE C O   1 
ATOM 4318 C CB  . PHE C 2 114 ? 140.713 128.535 189.351 1.00 35.41  ? 114  PHE C CB  1 
ATOM 4319 C CG  . PHE C 2 114 ? 141.992 127.824 189.668 1.00 31.77  ? 114  PHE C CG  1 
ATOM 4320 C CD1 . PHE C 2 114 ? 142.064 126.455 189.659 1.00 34.28  ? 114  PHE C CD1 1 
ATOM 4321 C CD2 . PHE C 2 114 ? 143.123 128.538 189.986 1.00 35.85  ? 114  PHE C CD2 1 
ATOM 4322 C CE1 . PHE C 2 114 ? 143.237 125.819 189.952 1.00 33.13  ? 114  PHE C CE1 1 
ATOM 4323 C CE2 . PHE C 2 114 ? 144.294 127.900 190.280 1.00 32.21  ? 114  PHE C CE2 1 
ATOM 4324 C CZ  . PHE C 2 114 ? 144.350 126.543 190.262 1.00 29.82  ? 114  PHE C CZ  1 
ATOM 4325 N N   . ASP C 2 115 ? 137.342 127.752 187.973 1.00 47.36  ? 115  ASP C N   1 
ATOM 4326 C CA  . ASP C 2 115 ? 136.045 128.390 187.790 1.00 53.34  ? 115  ASP C CA  1 
ATOM 4327 C C   . ASP C 2 115 ? 135.373 128.667 189.128 1.00 62.90  ? 115  ASP C C   1 
ATOM 4328 O O   . ASP C 2 115 ? 134.807 129.747 189.333 1.00 69.77  ? 115  ASP C O   1 
ATOM 4329 C CB  . ASP C 2 115 ? 135.154 127.525 186.903 1.00 58.41  ? 115  ASP C CB  1 
ATOM 4330 C CG  . ASP C 2 115 ? 135.222 126.059 187.265 1.00 65.33  ? 115  ASP C CG  1 
ATOM 4331 O OD1 . ASP C 2 115 ? 135.032 125.730 188.453 1.00 68.73  ? 115  ASP C OD1 1 
ATOM 4332 O OD2 . ASP C 2 115 ? 135.455 125.229 186.362 1.00 63.41  ? 115  ASP C OD2 1 
ATOM 4333 N N   . TYR C 2 116 ? 135.429 127.712 190.053 1.00 59.57  ? 116  TYR C N   1 
ATOM 4334 C CA  . TYR C 2 116 ? 134.816 127.857 191.371 1.00 65.41  ? 116  TYR C CA  1 
ATOM 4335 C C   . TYR C 2 116 ? 135.907 127.803 192.430 1.00 66.66  ? 116  TYR C C   1 
ATOM 4336 O O   . TYR C 2 116 ? 136.527 126.756 192.636 1.00 67.32  ? 116  TYR C O   1 
ATOM 4337 C CB  . TYR C 2 116 ? 133.768 126.774 191.616 1.00 71.31  ? 116  TYR C CB  1 
ATOM 4338 C CG  . TYR C 2 116 ? 132.554 126.878 190.725 1.00 78.52  ? 116  TYR C CG  1 
ATOM 4339 C CD1 . TYR C 2 116 ? 132.211 128.079 190.121 1.00 76.07  ? 116  TYR C CD1 1 
ATOM 4340 C CD2 . TYR C 2 116 ? 131.750 125.776 190.487 1.00 84.21  ? 116  TYR C CD2 1 
ATOM 4341 C CE1 . TYR C 2 116 ? 131.104 128.176 189.304 1.00 79.41  ? 116  TYR C CE1 1 
ATOM 4342 C CE2 . TYR C 2 116 ? 130.640 125.863 189.672 1.00 87.65  ? 116  TYR C CE2 1 
ATOM 4343 C CZ  . TYR C 2 116 ? 130.322 127.065 189.084 1.00 87.83  ? 116  TYR C CZ  1 
ATOM 4344 O OH  . TYR C 2 116 ? 129.216 127.156 188.271 1.00 94.04  ? 116  TYR C OH  1 
ATOM 4345 N N   . TRP C 2 117 ? 136.130 128.925 193.105 1.00 69.10  ? 117  TRP C N   1 
ATOM 4346 C CA  . TRP C 2 117 ? 137.075 128.996 194.205 1.00 72.86  ? 117  TRP C CA  1 
ATOM 4347 C C   . TRP C 2 117 ? 136.379 128.700 195.529 1.00 82.99  ? 117  TRP C C   1 
ATOM 4348 O O   . TRP C 2 117 ? 135.152 128.636 195.621 1.00 87.46  ? 117  TRP C O   1 
ATOM 4349 C CB  . TRP C 2 117 ? 137.729 130.373 194.268 1.00 67.50  ? 117  TRP C CB  1 
ATOM 4350 C CG  . TRP C 2 117 ? 138.601 130.699 193.115 1.00 59.86  ? 117  TRP C CG  1 
ATOM 4351 C CD1 . TRP C 2 117 ? 138.230 130.804 191.813 1.00 58.00  ? 117  TRP C CD1 1 
ATOM 4352 C CD2 . TRP C 2 117 ? 139.997 131.001 193.162 1.00 59.36  ? 117  TRP C CD2 1 
ATOM 4353 N NE1 . TRP C 2 117 ? 139.311 131.138 191.039 1.00 57.00  ? 117  TRP C NE1 1 
ATOM 4354 C CE2 . TRP C 2 117 ? 140.410 131.265 191.846 1.00 56.65  ? 117  TRP C CE2 1 
ATOM 4355 C CE3 . TRP C 2 117 ? 140.940 131.066 194.189 1.00 64.51  ? 117  TRP C CE3 1 
ATOM 4356 C CZ2 . TRP C 2 117 ? 141.723 131.589 191.530 1.00 55.50  ? 117  TRP C CZ2 1 
ATOM 4357 C CZ3 . TRP C 2 117 ? 142.240 131.387 193.873 1.00 61.31  ? 117  TRP C CZ3 1 
ATOM 4358 C CH2 . TRP C 2 117 ? 142.620 131.645 192.555 1.00 55.36  ? 117  TRP C CH2 1 
ATOM 4359 N N   . GLY C 2 118 ? 137.189 128.522 196.570 1.00 87.03  ? 118  GLY C N   1 
ATOM 4360 C CA  . GLY C 2 118 ? 136.667 128.384 197.911 1.00 92.13  ? 118  GLY C CA  1 
ATOM 4361 C C   . GLY C 2 118 ? 136.612 129.711 198.644 1.00 100.50 ? 118  GLY C C   1 
ATOM 4362 O O   . GLY C 2 118 ? 137.123 130.727 198.180 1.00 101.88 ? 118  GLY C O   1 
ATOM 4363 N N   . GLN C 2 119 ? 135.972 129.685 199.815 1.00 108.55 ? 119  GLN C N   1 
ATOM 4364 C CA  . GLN C 2 119 ? 135.845 130.902 200.612 1.00 110.02 ? 119  GLN C CA  1 
ATOM 4365 C C   . GLN C 2 119 ? 137.204 131.387 201.103 1.00 107.72 ? 119  GLN C C   1 
ATOM 4366 O O   . GLN C 2 119 ? 137.448 132.597 201.174 1.00 104.35 ? 119  GLN C O   1 
ATOM 4367 C CB  . GLN C 2 119 ? 134.896 130.661 201.786 1.00 110.76 ? 119  GLN C CB  1 
ATOM 4368 C CG  . GLN C 2 119 ? 135.289 129.499 202.682 1.00 113.39 ? 119  GLN C CG  1 
ATOM 4369 C CD  . GLN C 2 119 ? 134.221 129.160 203.698 1.00 118.31 ? 119  GLN C CD  1 
ATOM 4370 O OE1 . GLN C 2 119 ? 133.063 129.550 203.552 1.00 121.10 ? 119  GLN C OE1 1 
ATOM 4371 N NE2 . GLN C 2 119 ? 134.605 128.428 204.737 1.00 117.80 ? 119  GLN C NE2 1 
ATOM 4372 N N   . GLY C 2 120 ? 138.098 130.464 201.445 1.00 107.51 ? 120  GLY C N   1 
ATOM 4373 C CA  . GLY C 2 120 ? 139.422 130.826 201.908 1.00 107.73 ? 120  GLY C CA  1 
ATOM 4374 C C   . GLY C 2 120 ? 139.488 131.028 203.405 1.00 110.99 ? 120  GLY C C   1 
ATOM 4375 O O   . GLY C 2 120 ? 138.639 131.713 203.982 1.00 112.65 ? 120  GLY C O   1 
ATOM 4376 N N   . THR C 2 121 ? 140.492 130.438 204.048 1.00 114.01 ? 121  THR C N   1 
ATOM 4377 C CA  . THR C 2 121 ? 140.685 130.562 205.486 1.00 119.61 ? 121  THR C CA  1 
ATOM 4378 C C   . THR C 2 121 ? 142.029 131.214 205.768 1.00 119.06 ? 121  THR C C   1 
ATOM 4379 O O   . THR C 2 121 ? 143.024 130.918 205.102 1.00 115.00 ? 121  THR C O   1 
ATOM 4380 C CB  . THR C 2 121 ? 140.614 129.200 206.186 1.00 122.95 ? 121  THR C CB  1 
ATOM 4381 O OG1 . THR C 2 121 ? 141.343 128.228 205.426 1.00 120.47 ? 121  THR C OG1 1 
ATOM 4382 C CG2 . THR C 2 121 ? 139.170 128.753 206.337 1.00 123.97 ? 121  THR C CG2 1 
ATOM 4383 N N   . LEU C 2 122 ? 142.049 132.111 206.749 1.00 121.41 ? 122  LEU C N   1 
ATOM 4384 C CA  . LEU C 2 122 ? 143.258 132.837 207.110 1.00 122.52 ? 122  LEU C CA  1 
ATOM 4385 C C   . LEU C 2 122 ? 144.037 132.059 208.161 1.00 124.55 ? 122  LEU C C   1 
ATOM 4386 O O   . LEU C 2 122 ? 143.465 131.605 209.157 1.00 125.41 ? 122  LEU C O   1 
ATOM 4387 C CB  . LEU C 2 122 ? 142.912 134.231 207.635 1.00 120.34 ? 122  LEU C CB  1 
ATOM 4388 C CG  . LEU C 2 122 ? 144.067 135.046 208.216 1.00 120.77 ? 122  LEU C CG  1 
ATOM 4389 C CD1 . LEU C 2 122 ? 145.148 135.274 207.174 1.00 120.35 ? 122  LEU C CD1 1 
ATOM 4390 C CD2 . LEU C 2 122 ? 143.562 136.370 208.764 1.00 122.60 ? 122  LEU C CD2 1 
ATOM 4391 N N   . VAL C 2 123 ? 145.339 131.902 207.935 1.00 123.94 ? 123  VAL C N   1 
ATOM 4392 C CA  . VAL C 2 123 ? 146.235 131.263 208.889 1.00 125.66 ? 123  VAL C CA  1 
ATOM 4393 C C   . VAL C 2 123 ? 147.360 132.236 209.211 1.00 127.53 ? 123  VAL C C   1 
ATOM 4394 O O   . VAL C 2 123 ? 147.936 132.857 208.308 1.00 126.47 ? 123  VAL C O   1 
ATOM 4395 C CB  . VAL C 2 123 ? 146.783 129.925 208.358 1.00 122.77 ? 123  VAL C CB  1 
ATOM 4396 C CG1 . VAL C 2 123 ? 145.652 128.922 208.202 1.00 123.11 ? 123  VAL C CG1 1 
ATOM 4397 C CG2 . VAL C 2 123 ? 147.499 130.118 207.040 1.00 118.18 ? 123  VAL C CG2 1 
ATOM 4398 N N   . THR C 2 124 ? 147.647 132.388 210.502 1.00 132.35 ? 124  THR C N   1 
ATOM 4399 C CA  . THR C 2 124 ? 148.666 133.303 210.988 1.00 134.19 ? 124  THR C CA  1 
ATOM 4400 C C   . THR C 2 124 ? 149.596 132.564 211.938 1.00 136.93 ? 124  THR C C   1 
ATOM 4401 O O   . THR C 2 124 ? 149.205 131.584 212.577 1.00 138.16 ? 124  THR C O   1 
ATOM 4402 C CB  . THR C 2 124 ? 148.046 134.510 211.708 1.00 133.35 ? 124  THR C CB  1 
ATOM 4403 O OG1 . THR C 2 124 ? 147.258 134.052 212.814 1.00 135.73 ? 124  THR C OG1 1 
ATOM 4404 C CG2 . THR C 2 124 ? 147.158 135.303 210.762 1.00 128.85 ? 124  THR C CG2 1 
ATOM 4405 N N   . VAL C 2 125 ? 150.832 133.043 212.025 1.00 135.83 ? 125  VAL C N   1 
ATOM 4406 C CA  . VAL C 2 125 ? 151.821 132.437 212.907 1.00 136.24 ? 125  VAL C CA  1 
ATOM 4407 C C   . VAL C 2 125 ? 152.273 133.438 213.963 1.00 135.78 ? 125  VAL C C   1 
ATOM 4408 O O   . VAL C 2 125 ? 151.662 133.553 215.026 1.00 134.34 ? 125  VAL C O   1 
ATOM 4409 C CB  . VAL C 2 125 ? 153.025 131.907 212.111 1.00 133.98 ? 125  VAL C CB  1 
ATOM 4410 C CG1 . VAL C 2 125 ? 152.563 130.933 211.038 1.00 132.52 ? 125  VAL C CG1 1 
ATOM 4411 C CG2 . VAL C 2 125 ? 153.805 133.059 211.500 1.00 131.67 ? 125  VAL C CG2 1 
ATOM 4412 N N   . ASP D 3 1   ? 158.667 126.921 184.834 1.00 74.01  ? 2    ASP D N   1 
ATOM 4413 C CA  . ASP D 3 1   ? 158.645 128.217 185.502 1.00 71.27  ? 2    ASP D CA  1 
ATOM 4414 C C   . ASP D 3 1   ? 158.342 129.329 184.508 1.00 67.90  ? 2    ASP D C   1 
ATOM 4415 O O   . ASP D 3 1   ? 159.247 129.891 183.894 1.00 67.27  ? 2    ASP D O   1 
ATOM 4416 C CB  . ASP D 3 1   ? 159.978 128.484 186.203 1.00 73.08  ? 2    ASP D CB  1 
ATOM 4417 C CG  . ASP D 3 1   ? 159.923 129.688 187.123 1.00 80.17  ? 2    ASP D CG  1 
ATOM 4418 O OD1 . ASP D 3 1   ? 158.836 130.287 187.269 1.00 76.59  ? 2    ASP D OD1 1 
ATOM 4419 O OD2 . ASP D 3 1   ? 160.971 130.036 187.706 1.00 84.50  ? 2    ASP D OD2 1 
ATOM 4420 N N   . ILE D 3 2   ? 157.059 129.642 184.359 1.00 64.60  ? 3    ILE D N   1 
ATOM 4421 C CA  . ILE D 3 2   ? 156.588 130.679 183.451 1.00 60.37  ? 3    ILE D CA  1 
ATOM 4422 C C   . ILE D 3 2   ? 156.099 131.846 184.290 1.00 58.14  ? 3    ILE D C   1 
ATOM 4423 O O   . ILE D 3 2   ? 155.259 131.668 185.178 1.00 58.37  ? 3    ILE D O   1 
ATOM 4424 C CB  . ILE D 3 2   ? 155.477 130.152 182.530 1.00 49.33  ? 3    ILE D CB  1 
ATOM 4425 C CG1 . ILE D 3 2   ? 155.937 128.869 181.841 1.00 50.62  ? 3    ILE D CG1 1 
ATOM 4426 C CG2 . ILE D 3 2   ? 155.091 131.203 181.516 1.00 48.08  ? 3    ILE D CG2 1 
ATOM 4427 C CD1 . ILE D 3 2   ? 154.872 128.194 181.023 1.00 42.26  ? 3    ILE D CD1 1 
ATOM 4428 N N   . GLN D 3 3   ? 156.622 133.034 184.015 1.00 59.90  ? 4    GLN D N   1 
ATOM 4429 C CA  . GLN D 3 3   ? 156.346 134.214 184.820 1.00 63.03  ? 4    GLN D CA  1 
ATOM 4430 C C   . GLN D 3 3   ? 155.394 135.139 184.079 1.00 62.25  ? 4    GLN D C   1 
ATOM 4431 O O   . GLN D 3 3   ? 155.625 135.472 182.913 1.00 65.93  ? 4    GLN D O   1 
ATOM 4432 C CB  . GLN D 3 3   ? 157.643 134.946 185.160 1.00 65.84  ? 4    GLN D CB  1 
ATOM 4433 C CG  . GLN D 3 3   ? 158.583 134.134 186.029 1.00 72.30  ? 4    GLN D CG  1 
ATOM 4434 C CD  . GLN D 3 3   ? 160.032 134.532 185.852 1.00 80.58  ? 4    GLN D CD  1 
ATOM 4435 O OE1 . GLN D 3 3   ? 160.740 133.982 185.009 1.00 80.02  ? 4    GLN D OE1 1 
ATOM 4436 N NE2 . GLN D 3 3   ? 160.484 135.491 186.651 1.00 84.20  ? 4    GLN D NE2 1 
ATOM 4437 N N   . MET D 3 4   ? 154.327 135.549 184.757 1.00 57.47  ? 5    MET D N   1 
ATOM 4438 C CA  . MET D 3 4   ? 153.365 136.495 184.213 1.00 62.33  ? 5    MET D CA  1 
ATOM 4439 C C   . MET D 3 4   ? 153.629 137.868 184.813 1.00 74.02  ? 5    MET D C   1 
ATOM 4440 O O   . MET D 3 4   ? 153.808 137.994 186.028 1.00 78.46  ? 5    MET D O   1 
ATOM 4441 C CB  . MET D 3 4   ? 151.932 136.059 184.512 1.00 59.22  ? 5    MET D CB  1 
ATOM 4442 C CG  . MET D 3 4   ? 151.602 134.662 184.052 1.00 51.25  ? 5    MET D CG  1 
ATOM 4443 S SD  . MET D 3 4   ? 151.602 134.506 182.265 1.00 53.03  ? 5    MET D SD  1 
ATOM 4444 C CE  . MET D 3 4   ? 149.996 135.162 181.856 1.00 48.73  ? 5    MET D CE  1 
ATOM 4445 N N   . THR D 3 5   ? 153.658 138.890 183.961 1.00 74.47  ? 6    THR D N   1 
ATOM 4446 C CA  . THR D 3 5   ? 153.913 140.258 184.388 1.00 77.12  ? 6    THR D CA  1 
ATOM 4447 C C   . THR D 3 5   ? 152.801 141.161 183.880 1.00 80.04  ? 6    THR D C   1 
ATOM 4448 O O   . THR D 3 5   ? 152.462 141.121 182.695 1.00 78.91  ? 6    THR D O   1 
ATOM 4449 C CB  . THR D 3 5   ? 155.265 140.754 183.872 1.00 77.28  ? 6    THR D CB  1 
ATOM 4450 O OG1 . THR D 3 5   ? 155.307 140.619 182.447 1.00 74.24  ? 6    THR D OG1 1 
ATOM 4451 C CG2 . THR D 3 5   ? 156.397 139.949 184.485 1.00 74.85  ? 6    THR D CG2 1 
ATOM 4452 N N   . GLN D 3 6   ? 152.245 141.976 184.771 1.00 85.67  ? 7    GLN D N   1 
ATOM 4453 C CA  . GLN D 3 6   ? 151.221 142.950 184.418 1.00 94.33  ? 7    GLN D CA  1 
ATOM 4454 C C   . GLN D 3 6   ? 151.817 144.349 184.477 1.00 105.90 ? 7    GLN D C   1 
ATOM 4455 O O   . GLN D 3 6   ? 152.458 144.714 185.469 1.00 109.60 ? 7    GLN D O   1 
ATOM 4456 C CB  . GLN D 3 6   ? 150.016 142.853 185.355 1.00 94.59  ? 7    GLN D CB  1 
ATOM 4457 C CG  . GLN D 3 6   ? 149.481 141.452 185.532 1.00 86.32  ? 7    GLN D CG  1 
ATOM 4458 C CD  . GLN D 3 6   ? 148.135 141.427 186.219 1.00 87.16  ? 7    GLN D CD  1 
ATOM 4459 O OE1 . GLN D 3 6   ? 147.963 140.779 187.248 1.00 84.61  ? 7    GLN D OE1 1 
ATOM 4460 N NE2 . GLN D 3 6   ? 147.167 142.129 185.648 1.00 90.42  ? 7    GLN D NE2 1 
ATOM 4461 N N   . SER D 3 7   ? 151.605 145.126 183.419 1.00 106.50 ? 8    SER D N   1 
ATOM 4462 C CA  . SER D 3 7   ? 152.151 146.475 183.334 1.00 113.11 ? 8    SER D CA  1 
ATOM 4463 C C   . SER D 3 7   ? 151.365 147.467 184.192 1.00 118.96 ? 8    SER D C   1 
ATOM 4464 O O   . SER D 3 7   ? 151.974 148.178 185.003 1.00 121.87 ? 8    SER D O   1 
ATOM 4465 C CB  . SER D 3 7   ? 152.201 146.941 181.875 1.00 111.87 ? 8    SER D CB  1 
ATOM 4466 O OG  . SER D 3 7   ? 152.960 146.047 181.081 1.00 108.48 ? 8    SER D OG  1 
ATOM 4467 N N   . PRO D 3 8   ? 150.023 147.564 184.063 1.00 118.04 ? 9    PRO D N   1 
ATOM 4468 C CA  . PRO D 3 8   ? 149.300 148.553 184.876 1.00 121.64 ? 9    PRO D CA  1 
ATOM 4469 C C   . PRO D 3 8   ? 149.148 148.121 186.326 1.00 122.78 ? 9    PRO D C   1 
ATOM 4470 O O   . PRO D 3 8   ? 148.131 147.530 186.701 1.00 123.53 ? 9    PRO D O   1 
ATOM 4471 C CB  . PRO D 3 8   ? 147.942 148.658 184.172 1.00 119.00 ? 9    PRO D CB  1 
ATOM 4472 C CG  . PRO D 3 8   ? 147.746 147.329 183.566 1.00 112.74 ? 9    PRO D CG  1 
ATOM 4473 C CD  . PRO D 3 8   ? 149.106 146.840 183.159 1.00 109.81 ? 9    PRO D CD  1 
ATOM 4474 N N   . SER D 3 9   ? 150.162 148.405 187.147 1.00 124.22 ? 10   SER D N   1 
ATOM 4475 C CA  . SER D 3 9   ? 150.108 148.017 188.554 1.00 126.82 ? 10   SER D CA  1 
ATOM 4476 C C   . SER D 3 9   ? 148.930 148.672 189.265 1.00 128.03 ? 10   SER D C   1 
ATOM 4477 O O   . SER D 3 9   ? 148.249 148.031 190.074 1.00 124.85 ? 10   SER D O   1 
ATOM 4478 C CB  . SER D 3 9   ? 151.421 148.380 189.248 1.00 130.34 ? 10   SER D CB  1 
ATOM 4479 O OG  . SER D 3 9   ? 152.522 147.746 188.622 1.00 131.09 ? 10   SER D OG  1 
ATOM 4480 N N   . SER D 3 10  ? 148.678 149.947 188.981 1.00 131.07 ? 11   SER D N   1 
ATOM 4481 C CA  . SER D 3 10  ? 147.538 150.666 189.529 1.00 131.29 ? 11   SER D CA  1 
ATOM 4482 C C   . SER D 3 10  ? 146.783 151.343 188.396 1.00 132.21 ? 11   SER D C   1 
ATOM 4483 O O   . SER D 3 10  ? 147.389 151.963 187.518 1.00 131.97 ? 11   SER D O   1 
ATOM 4484 C CB  . SER D 3 10  ? 147.978 151.706 190.566 1.00 129.89 ? 11   SER D CB  1 
ATOM 4485 O OG  . SER D 3 10  ? 146.861 152.372 191.126 1.00 132.55 ? 11   SER D OG  1 
ATOM 4486 N N   . LEU D 3 11  ? 145.459 151.220 188.418 1.00 131.67 ? 12   LEU D N   1 
ATOM 4487 C CA  . LEU D 3 11  ? 144.605 151.794 187.390 1.00 134.20 ? 12   LEU D CA  1 
ATOM 4488 C C   . LEU D 3 11  ? 143.478 152.577 188.045 1.00 138.19 ? 12   LEU D C   1 
ATOM 4489 O O   . LEU D 3 11  ? 142.879 152.121 189.024 1.00 137.73 ? 12   LEU D O   1 
ATOM 4490 C CB  . LEU D 3 11  ? 144.035 150.703 186.472 1.00 135.06 ? 12   LEU D CB  1 
ATOM 4491 C CG  . LEU D 3 11  ? 143.115 151.127 185.325 1.00 135.51 ? 12   LEU D CG  1 
ATOM 4492 C CD1 . LEU D 3 11  ? 143.399 150.293 184.088 1.00 127.10 ? 12   LEU D CD1 1 
ATOM 4493 C CD2 . LEU D 3 11  ? 141.656 150.989 185.728 1.00 135.29 ? 12   LEU D CD2 1 
ATOM 4494 N N   . SER D 3 12  ? 143.192 153.756 187.497 1.00 142.22 ? 13   SER D N   1 
ATOM 4495 C CA  . SER D 3 12  ? 142.130 154.621 187.991 1.00 143.77 ? 13   SER D CA  1 
ATOM 4496 C C   . SER D 3 12  ? 141.322 155.142 186.813 1.00 143.87 ? 13   SER D C   1 
ATOM 4497 O O   . SER D 3 12  ? 141.893 155.641 185.838 1.00 143.41 ? 13   SER D O   1 
ATOM 4498 C CB  . SER D 3 12  ? 142.702 155.787 188.803 1.00 142.15 ? 13   SER D CB  1 
ATOM 4499 O OG  . SER D 3 12  ? 143.671 156.498 188.053 1.00 140.38 ? 13   SER D OG  1 
ATOM 4500 N N   . ALA D 3 13  ? 139.999 155.027 186.905 1.00 143.48 ? 14   ALA D N   1 
ATOM 4501 C CA  . ALA D 3 13  ? 139.122 155.484 185.837 1.00 144.93 ? 14   ALA D CA  1 
ATOM 4502 C C   . ALA D 3 13  ? 137.742 155.761 186.413 1.00 146.04 ? 14   ALA D C   1 
ATOM 4503 O O   . ALA D 3 13  ? 137.404 155.309 187.510 1.00 145.47 ? 14   ALA D O   1 
ATOM 4504 C CB  . ALA D 3 13  ? 139.036 154.461 184.699 1.00 143.27 ? 14   ALA D CB  1 
ATOM 4505 N N   . SER D 3 14  ? 136.949 156.507 185.651 1.00 146.78 ? 15   SER D N   1 
ATOM 4506 C CA  . SER D 3 14  ? 135.605 156.877 186.063 1.00 146.29 ? 15   SER D CA  1 
ATOM 4507 C C   . SER D 3 14  ? 134.579 155.898 185.498 1.00 144.47 ? 15   SER D C   1 
ATOM 4508 O O   . SER D 3 14  ? 134.889 155.025 184.686 1.00 143.75 ? 15   SER D O   1 
ATOM 4509 C CB  . SER D 3 14  ? 135.283 158.302 185.616 1.00 146.42 ? 15   SER D CB  1 
ATOM 4510 O OG  . SER D 3 14  ? 135.323 158.414 184.203 1.00 145.97 ? 15   SER D OG  1 
ATOM 4511 N N   . VAL D 3 15  ? 133.333 156.059 185.943 1.00 142.98 ? 16   VAL D N   1 
ATOM 4512 C CA  . VAL D 3 15  ? 132.253 155.191 185.490 1.00 142.50 ? 16   VAL D CA  1 
ATOM 4513 C C   . VAL D 3 15  ? 131.985 155.442 184.013 1.00 143.60 ? 16   VAL D C   1 
ATOM 4514 O O   . VAL D 3 15  ? 131.873 156.593 183.571 1.00 143.52 ? 16   VAL D O   1 
ATOM 4515 C CB  . VAL D 3 15  ? 130.991 155.420 186.334 1.00 141.67 ? 16   VAL D CB  1 
ATOM 4516 C CG1 . VAL D 3 15  ? 129.847 154.551 185.833 1.00 139.66 ? 16   VAL D CG1 1 
ATOM 4517 C CG2 . VAL D 3 15  ? 131.277 155.137 187.800 1.00 141.21 ? 16   VAL D CG2 1 
ATOM 4518 N N   . GLY D 3 16  ? 131.882 154.362 183.241 1.00 143.76 ? 17   GLY D N   1 
ATOM 4519 C CA  . GLY D 3 16  ? 131.634 154.456 181.819 1.00 142.93 ? 17   GLY D CA  1 
ATOM 4520 C C   . GLY D 3 16  ? 132.870 154.528 180.949 1.00 143.85 ? 17   GLY D C   1 
ATOM 4521 O O   . GLY D 3 16  ? 132.738 154.563 179.719 1.00 142.10 ? 17   GLY D O   1 
ATOM 4522 N N   . ASP D 3 17  ? 134.060 154.553 181.539 1.00 145.01 ? 18   ASP D N   1 
ATOM 4523 C CA  . ASP D 3 17  ? 135.299 154.626 180.782 1.00 145.13 ? 18   ASP D CA  1 
ATOM 4524 C C   . ASP D 3 17  ? 135.774 153.228 180.390 1.00 143.92 ? 18   ASP D C   1 
ATOM 4525 O O   . ASP D 3 17  ? 135.333 152.215 180.937 1.00 141.09 ? 18   ASP D O   1 
ATOM 4526 C CB  . ASP D 3 17  ? 136.379 155.346 181.592 1.00 143.70 ? 18   ASP D CB  1 
ATOM 4527 C CG  . ASP D 3 17  ? 137.526 155.840 180.729 1.00 144.67 ? 18   ASP D CG  1 
ATOM 4528 O OD1 . ASP D 3 17  ? 137.474 155.644 179.497 1.00 144.90 ? 18   ASP D OD1 1 
ATOM 4529 O OD2 . ASP D 3 17  ? 138.478 156.427 181.284 1.00 143.23 ? 18   ASP D OD2 1 
ATOM 4530 N N   . ARG D 3 18  ? 136.687 153.189 179.425 1.00 143.05 ? 19   ARG D N   1 
ATOM 4531 C CA  . ARG D 3 18  ? 137.254 151.946 178.919 1.00 137.92 ? 19   ARG D CA  1 
ATOM 4532 C C   . ARG D 3 18  ? 138.665 151.771 179.462 1.00 135.68 ? 19   ARG D C   1 
ATOM 4533 O O   . ARG D 3 18  ? 139.482 152.695 179.390 1.00 135.30 ? 19   ARG D O   1 
ATOM 4534 C CB  . ARG D 3 18  ? 137.271 151.944 177.390 1.00 136.24 ? 19   ARG D CB  1 
ATOM 4535 C CG  . ARG D 3 18  ? 138.158 150.879 176.772 1.00 133.44 ? 19   ARG D CG  1 
ATOM 4536 C CD  . ARG D 3 18  ? 138.234 151.046 175.265 1.00 137.35 ? 19   ARG D CD  1 
ATOM 4537 N NE  . ARG D 3 18  ? 139.214 150.152 174.661 1.00 138.72 ? 19   ARG D NE  1 
ATOM 4538 C CZ  . ARG D 3 18  ? 139.514 150.134 173.369 1.00 140.79 ? 19   ARG D CZ  1 
ATOM 4539 N NH1 . ARG D 3 18  ? 138.925 150.951 172.512 1.00 141.19 ? 19   ARG D NH1 1 
ATOM 4540 N NH2 . ARG D 3 18  ? 140.429 149.276 172.927 1.00 141.37 ? 19   ARG D NH2 1 
ATOM 4541 N N   . VAL D 3 19  ? 138.948 150.586 180.006 1.00 133.27 ? 20   VAL D N   1 
ATOM 4542 C CA  . VAL D 3 19  ? 140.247 150.284 180.587 1.00 128.88 ? 20   VAL D CA  1 
ATOM 4543 C C   . VAL D 3 19  ? 140.782 148.996 179.978 1.00 122.06 ? 20   VAL D C   1 
ATOM 4544 O O   . VAL D 3 19  ? 140.032 148.149 179.487 1.00 117.48 ? 20   VAL D O   1 
ATOM 4545 C CB  . VAL D 3 19  ? 140.189 150.169 182.124 1.00 128.33 ? 20   VAL D CB  1 
ATOM 4546 C CG1 . VAL D 3 19  ? 139.742 151.484 182.731 1.00 132.19 ? 20   VAL D CG1 1 
ATOM 4547 C CG2 . VAL D 3 19  ? 139.257 149.045 182.536 1.00 124.87 ? 20   VAL D CG2 1 
ATOM 4548 N N   . THR D 3 20  ? 142.106 148.859 180.022 1.00 117.05 ? 21   THR D N   1 
ATOM 4549 C CA  . THR D 3 20  ? 142.803 147.740 179.404 1.00 109.57 ? 21   THR D CA  1 
ATOM 4550 C C   . THR D 3 20  ? 143.972 147.325 180.282 1.00 107.76 ? 21   THR D C   1 
ATOM 4551 O O   . THR D 3 20  ? 144.784 148.166 180.679 1.00 107.12 ? 21   THR D O   1 
ATOM 4552 C CB  . THR D 3 20  ? 143.296 148.110 177.999 1.00 111.79 ? 21   THR D CB  1 
ATOM 4553 O OG1 . THR D 3 20  ? 142.206 148.030 177.072 1.00 114.48 ? 21   THR D OG1 1 
ATOM 4554 C CG2 . THR D 3 20  ? 144.413 147.181 177.550 1.00 106.81 ? 21   THR D CG2 1 
ATOM 4555 N N   . ILE D 3 21  ? 144.053 146.030 180.578 1.00 105.91 ? 22   ILE D N   1 
ATOM 4556 C CA  . ILE D 3 21  ? 145.137 145.453 181.364 1.00 101.30 ? 22   ILE D CA  1 
ATOM 4557 C C   . ILE D 3 21  ? 145.898 144.483 180.474 1.00 92.76  ? 22   ILE D C   1 
ATOM 4558 O O   . ILE D 3 21  ? 145.298 143.582 179.877 1.00 89.13  ? 22   ILE D O   1 
ATOM 4559 C CB  . ILE D 3 21  ? 144.617 144.740 182.625 1.00 99.58  ? 22   ILE D CB  1 
ATOM 4560 C CG1 . ILE D 3 21  ? 143.692 145.656 183.427 1.00 103.90 ? 22   ILE D CG1 1 
ATOM 4561 C CG2 . ILE D 3 21  ? 145.777 144.283 183.489 1.00 97.37  ? 22   ILE D CG2 1 
ATOM 4562 C CD1 . ILE D 3 21  ? 142.219 145.392 183.202 1.00 99.06  ? 22   ILE D CD1 1 
ATOM 4563 N N   . THR D 3 22  ? 147.212 144.667 180.386 1.00 92.71  ? 23   THR D N   1 
ATOM 4564 C CA  . THR D 3 22  ? 148.078 143.848 179.550 1.00 86.71  ? 23   THR D CA  1 
ATOM 4565 C C   . THR D 3 22  ? 148.942 142.958 180.430 1.00 85.61  ? 23   THR D C   1 
ATOM 4566 O O   . THR D 3 22  ? 149.560 143.434 181.388 1.00 90.67  ? 23   THR D O   1 
ATOM 4567 C CB  . THR D 3 22  ? 148.958 144.720 178.651 1.00 86.13  ? 23   THR D CB  1 
ATOM 4568 O OG1 . THR D 3 22  ? 148.165 145.265 177.589 1.00 88.96  ? 23   THR D OG1 1 
ATOM 4569 C CG2 . THR D 3 22  ? 150.099 143.909 178.057 1.00 79.82  ? 23   THR D CG2 1 
ATOM 4570 N N   . CYS D 3 23  ? 148.982 141.669 180.102 1.00 78.19  ? 24   CYS D N   1 
ATOM 4571 C CA  . CYS D 3 23  ? 149.729 140.673 180.853 1.00 73.86  ? 24   CYS D CA  1 
ATOM 4572 C C   . CYS D 3 23  ? 150.600 139.899 179.878 1.00 65.91  ? 24   CYS D C   1 
ATOM 4573 O O   . CYS D 3 23  ? 150.125 139.470 178.823 1.00 67.72  ? 24   CYS D O   1 
ATOM 4574 C CB  . CYS D 3 23  ? 148.768 139.749 181.609 1.00 75.50  ? 24   CYS D CB  1 
ATOM 4575 S SG  . CYS D 3 23  ? 149.504 138.483 182.651 1.00 79.95  ? 24   CYS D SG  1 
ATOM 4576 N N   . ARG D 3 24  ? 151.875 139.744 180.213 1.00 65.24  ? 25   ARG D N   1 
ATOM 4577 C CA  . ARG D 3 24  ? 152.841 139.104 179.333 1.00 67.91  ? 25   ARG D CA  1 
ATOM 4578 C C   . ARG D 3 24  ? 153.453 137.904 180.034 1.00 69.29  ? 25   ARG D C   1 
ATOM 4579 O O   . ARG D 3 24  ? 153.838 137.995 181.204 1.00 73.44  ? 25   ARG D O   1 
ATOM 4580 C CB  . ARG D 3 24  ? 153.940 140.078 178.912 1.00 70.63  ? 25   ARG D CB  1 
ATOM 4581 C CG  . ARG D 3 24  ? 154.098 140.202 177.414 1.00 72.07  ? 25   ARG D CG  1 
ATOM 4582 C CD  . ARG D 3 24  ? 155.460 140.743 177.041 1.00 74.74  ? 25   ARG D CD  1 
ATOM 4583 N NE  . ARG D 3 24  ? 156.503 139.745 177.238 1.00 75.65  ? 25   ARG D NE  1 
ATOM 4584 C CZ  . ARG D 3 24  ? 156.904 138.891 176.307 1.00 75.43  ? 25   ARG D CZ  1 
ATOM 4585 N NH1 . ARG D 3 24  ? 156.376 138.894 175.094 1.00 71.70  ? 25   ARG D NH1 1 
ATOM 4586 N NH2 . ARG D 3 24  ? 157.858 138.012 176.599 1.00 72.52  ? 25   ARG D NH2 1 
ATOM 4587 N N   . ALA D 3 25  ? 153.551 136.792 179.316 1.00 60.41  ? 26   ALA D N   1 
ATOM 4588 C CA  . ALA D 3 25  ? 154.109 135.568 179.862 1.00 57.25  ? 26   ALA D CA  1 
ATOM 4589 C C   . ALA D 3 25  ? 155.586 135.455 179.518 1.00 58.77  ? 26   ALA D C   1 
ATOM 4590 O O   . ALA D 3 25  ? 156.046 135.967 178.496 1.00 65.26  ? 26   ALA D O   1 
ATOM 4591 C CB  . ALA D 3 25  ? 153.358 134.351 179.327 1.00 52.94  ? 26   ALA D CB  1 
ATOM 4592 N N   . SER D 3 26  ? 156.331 134.771 180.387 1.00 55.62  ? 27   SER D N   1 
ATOM 4593 C CA  . SER D 3 26  ? 157.750 134.558 180.137 1.00 57.19  ? 27   SER D CA  1 
ATOM 4594 C C   . SER D 3 26  ? 157.996 133.732 178.885 1.00 62.35  ? 27   SER D C   1 
ATOM 4595 O O   . SER D 3 26  ? 159.074 133.837 178.291 1.00 68.80  ? 27   SER D O   1 
ATOM 4596 C CB  . SER D 3 26  ? 158.402 133.879 181.337 1.00 61.09  ? 27   SER D CB  1 
ATOM 4597 O OG  . SER D 3 26  ? 159.736 133.512 181.041 1.00 62.34  ? 27   SER D OG  1 
ATOM 4598 N N   . GLN D 3 27  ? 157.032 132.915 178.475 1.00 58.28  ? 28   GLN D N   1 
ATOM 4599 C CA  . GLN D 3 27  ? 157.148 132.120 177.261 1.00 53.65  ? 28   GLN D CA  1 
ATOM 4600 C C   . GLN D 3 27  ? 155.745 131.831 176.749 1.00 50.07  ? 28   GLN D C   1 
ATOM 4601 O O   . GLN D 3 27  ? 154.750 132.247 177.344 1.00 50.08  ? 28   GLN D O   1 
ATOM 4602 C CB  . GLN D 3 27  ? 157.937 130.834 177.510 1.00 47.14  ? 28   GLN D CB  1 
ATOM 4603 C CG  . GLN D 3 27  ? 157.446 130.017 178.681 1.00 48.75  ? 28   GLN D CG  1 
ATOM 4604 C CD  . GLN D 3 27  ? 158.159 128.688 178.793 1.00 55.04  ? 28   GLN D CD  1 
ATOM 4605 O OE1 . GLN D 3 27  ? 158.880 128.436 179.755 1.00 54.39  ? 28   GLN D OE1 1 
ATOM 4606 N NE2 . GLN D 3 27  ? 157.958 127.826 177.806 1.00 55.69  ? 28   GLN D NE2 1 
ATOM 4607 N N   . SER D 3 28  ? 155.672 131.121 175.629 1.00 48.92  ? 29   SER D N   1 
ATOM 4608 C CA  . SER D 3 28  ? 154.381 130.797 175.038 1.00 42.05  ? 29   SER D CA  1 
ATOM 4609 C C   . SER D 3 28  ? 153.618 129.832 175.932 1.00 40.80  ? 29   SER D C   1 
ATOM 4610 O O   . SER D 3 28  ? 154.146 128.793 176.339 1.00 42.57  ? 29   SER D O   1 
ATOM 4611 C CB  . SER D 3 28  ? 154.567 130.191 173.651 1.00 41.92  ? 29   SER D CB  1 
ATOM 4612 O OG  . SER D 3 28  ? 153.327 129.759 173.120 1.00 42.10  ? 29   SER D OG  1 
ATOM 4613 N N   . VAL D 3 29  ? 152.371 130.180 176.236 1.00 38.18  ? 30   VAL D N   1 
ATOM 4614 C CA  . VAL D 3 29  ? 151.485 129.355 177.042 1.00 33.56  ? 30   VAL D CA  1 
ATOM 4615 C C   . VAL D 3 29  ? 150.192 129.048 176.297 1.00 30.74  ? 30   VAL D C   1 
ATOM 4616 O O   . VAL D 3 29  ? 149.213 128.650 176.904 1.00 33.94  ? 30   VAL D O   1 
ATOM 4617 C CB  . VAL D 3 29  ? 151.194 130.012 178.405 1.00 29.54  ? 30   VAL D CB  1 
ATOM 4618 C CG1 . VAL D 3 29  ? 152.478 130.261 179.147 1.00 35.17  ? 30   VAL D CG1 1 
ATOM 4619 C CG2 . VAL D 3 29  ? 150.441 131.307 178.216 1.00 28.04  ? 30   VAL D CG2 1 
ATOM 4620 N N   . SER D 3 30  ? 150.191 129.230 174.983 1.00 29.77  ? 31   SER D N   1 
ATOM 4621 C CA  . SER D 3 30  ? 148.998 129.056 174.148 1.00 31.39  ? 31   SER D CA  1 
ATOM 4622 C C   . SER D 3 30  ? 147.937 130.041 174.638 1.00 35.83  ? 31   SER D C   1 
ATOM 4623 O O   . SER D 3 30  ? 148.264 131.128 175.130 1.00 43.52  ? 31   SER D O   1 
ATOM 4624 C CB  . SER D 3 30  ? 148.563 127.610 174.150 1.00 29.37  ? 31   SER D CB  1 
ATOM 4625 O OG  . SER D 3 30  ? 147.310 127.467 173.514 1.00 33.63  ? 31   SER D OG  1 
ATOM 4626 N N   . SER D 3 31  ? 146.662 129.683 174.510 1.00 32.06  ? 32   SER D N   1 
ATOM 4627 C CA  . SER D 3 31  ? 145.574 130.493 175.029 1.00 26.16  ? 32   SER D CA  1 
ATOM 4628 C C   . SER D 3 31  ? 145.257 130.169 176.474 1.00 25.58  ? 32   SER D C   1 
ATOM 4629 O O   . SER D 3 31  ? 144.145 130.441 176.930 1.00 31.55  ? 32   SER D O   1 
ATOM 4630 C CB  . SER D 3 31  ? 144.324 130.310 174.171 1.00 33.41  ? 32   SER D CB  1 
ATOM 4631 O OG  . SER D 3 31  ? 144.581 130.630 172.817 1.00 47.60  ? 32   SER D OG  1 
ATOM 4632 N N   . ALA D 3 32  ? 146.205 129.580 177.201 1.00 24.37  ? 33   ALA D N   1 
ATOM 4633 C CA  . ALA D 3 32  ? 145.995 129.169 178.585 1.00 23.72  ? 33   ALA D CA  1 
ATOM 4634 C C   . ALA D 3 32  ? 146.304 130.337 179.518 1.00 29.62  ? 33   ALA D C   1 
ATOM 4635 O O   . ALA D 3 32  ? 147.273 130.337 180.278 1.00 33.08  ? 33   ALA D O   1 
ATOM 4636 C CB  . ALA D 3 32  ? 146.852 127.957 178.914 1.00 22.00  ? 33   ALA D CB  1 
ATOM 4637 N N   . VAL D 3 33  ? 145.455 131.360 179.445 1.00 28.83  ? 34   VAL D N   1 
ATOM 4638 C CA  . VAL D 3 33  ? 145.554 132.523 180.321 1.00 27.46  ? 34   VAL D CA  1 
ATOM 4639 C C   . VAL D 3 33  ? 144.146 132.920 180.735 1.00 29.06  ? 34   VAL D C   1 
ATOM 4640 O O   . VAL D 3 33  ? 143.361 133.383 179.904 1.00 35.19  ? 34   VAL D O   1 
ATOM 4641 C CB  . VAL D 3 33  ? 146.265 133.705 179.657 1.00 31.91  ? 34   VAL D CB  1 
ATOM 4642 C CG1 . VAL D 3 33  ? 146.115 134.947 180.511 1.00 40.27  ? 34   VAL D CG1 1 
ATOM 4643 C CG2 . VAL D 3 33  ? 147.721 133.388 179.468 1.00 34.84  ? 34   VAL D CG2 1 
ATOM 4644 N N   . ALA D 3 34  ? 143.832 132.757 182.011 1.00 29.88  ? 35   ALA D N   1 
ATOM 4645 C CA  . ALA D 3 34  ? 142.531 133.110 182.551 1.00 34.41  ? 35   ALA D CA  1 
ATOM 4646 C C   . ALA D 3 34  ? 142.608 134.445 183.275 1.00 45.37  ? 35   ALA D C   1 
ATOM 4647 O O   . ALA D 3 34  ? 143.655 134.834 183.790 1.00 50.97  ? 35   ALA D O   1 
ATOM 4648 C CB  . ALA D 3 34  ? 142.021 132.029 183.503 1.00 35.51  ? 35   ALA D CB  1 
ATOM 4649 N N   . TRP D 3 35  ? 141.482 135.148 183.298 1.00 51.45  ? 36   TRP D N   1 
ATOM 4650 C CA  . TRP D 3 35  ? 141.360 136.443 183.956 1.00 53.49  ? 36   TRP D CA  1 
ATOM 4651 C C   . TRP D 3 35  ? 140.344 136.327 185.080 1.00 60.18  ? 36   TRP D C   1 
ATOM 4652 O O   . TRP D 3 35  ? 139.189 135.955 184.832 1.00 62.78  ? 36   TRP D O   1 
ATOM 4653 C CB  . TRP D 3 35  ? 140.935 137.529 182.966 1.00 57.86  ? 36   TRP D CB  1 
ATOM 4654 C CG  . TRP D 3 35  ? 141.990 137.889 181.980 1.00 57.81  ? 36   TRP D CG  1 
ATOM 4655 C CD1 . TRP D 3 35  ? 142.111 137.433 180.704 1.00 53.71  ? 36   TRP D CD1 1 
ATOM 4656 C CD2 . TRP D 3 35  ? 143.079 138.788 182.191 1.00 62.47  ? 36   TRP D CD2 1 
ATOM 4657 N NE1 . TRP D 3 35  ? 143.210 137.990 180.105 1.00 56.26  ? 36   TRP D NE1 1 
ATOM 4658 C CE2 . TRP D 3 35  ? 143.823 138.827 181.000 1.00 63.87  ? 36   TRP D CE2 1 
ATOM 4659 C CE3 . TRP D 3 35  ? 143.499 139.563 183.273 1.00 65.24  ? 36   TRP D CE3 1 
ATOM 4660 C CZ2 . TRP D 3 35  ? 144.962 139.611 180.860 1.00 70.19  ? 36   TRP D CZ2 1 
ATOM 4661 C CZ3 . TRP D 3 35  ? 144.628 140.340 183.132 1.00 69.81  ? 36   TRP D CZ3 1 
ATOM 4662 C CH2 . TRP D 3 35  ? 145.347 140.359 181.936 1.00 70.40  ? 36   TRP D CH2 1 
ATOM 4663 N N   . TYR D 3 36  ? 140.779 136.663 186.300 1.00 64.38  ? 37   TYR D N   1 
ATOM 4664 C CA  . TYR D 3 36  ? 139.960 136.626 187.504 1.00 71.15  ? 37   TYR D CA  1 
ATOM 4665 C C   . TYR D 3 36  ? 139.809 138.025 188.083 1.00 83.46  ? 37   TYR D C   1 
ATOM 4666 O O   . TYR D 3 36  ? 140.716 138.858 187.982 1.00 89.22  ? 37   TYR D O   1 
ATOM 4667 C CB  . TYR D 3 36  ? 140.568 135.733 188.598 1.00 68.84  ? 37   TYR D CB  1 
ATOM 4668 C CG  . TYR D 3 36  ? 140.898 134.331 188.171 1.00 59.68  ? 37   TYR D CG  1 
ATOM 4669 C CD1 . TYR D 3 36  ? 142.109 134.044 187.580 1.00 52.68  ? 37   TYR D CD1 1 
ATOM 4670 C CD2 . TYR D 3 36  ? 140.007 133.291 188.377 1.00 55.20  ? 37   TYR D CD2 1 
ATOM 4671 C CE1 . TYR D 3 36  ? 142.417 132.777 187.190 1.00 46.64  ? 37   TYR D CE1 1 
ATOM 4672 C CE2 . TYR D 3 36  ? 140.312 132.013 187.987 1.00 46.46  ? 37   TYR D CE2 1 
ATOM 4673 C CZ  . TYR D 3 36  ? 141.522 131.765 187.393 1.00 42.94  ? 37   TYR D CZ  1 
ATOM 4674 O OH  . TYR D 3 36  ? 141.853 130.497 186.994 1.00 42.81  ? 37   TYR D OH  1 
ATOM 4675 N N   . GLN D 3 37  ? 138.663 138.261 188.720 1.00 89.93  ? 38   GLN D N   1 
ATOM 4676 C CA  . GLN D 3 37  ? 138.386 139.497 189.441 1.00 97.52  ? 38   GLN D CA  1 
ATOM 4677 C C   . GLN D 3 37  ? 138.186 139.172 190.913 1.00 98.22  ? 38   GLN D C   1 
ATOM 4678 O O   . GLN D 3 37  ? 137.326 138.357 191.259 1.00 98.95  ? 38   GLN D O   1 
ATOM 4679 C CB  . GLN D 3 37  ? 137.148 140.199 188.882 1.00 101.18 ? 38   GLN D CB  1 
ATOM 4680 C CG  . GLN D 3 37  ? 136.721 141.423 189.674 1.00 108.08 ? 38   GLN D CG  1 
ATOM 4681 C CD  . GLN D 3 37  ? 135.449 142.048 189.140 1.00 112.61 ? 38   GLN D CD  1 
ATOM 4682 O OE1 . GLN D 3 37  ? 135.459 143.174 188.645 1.00 118.55 ? 38   GLN D OE1 1 
ATOM 4683 N NE2 . GLN D 3 37  ? 134.344 141.319 189.241 1.00 110.91 ? 38   GLN D NE2 1 
ATOM 4684 N N   . GLN D 3 38  ? 138.966 139.819 191.775 1.00 102.82 ? 39   GLN D N   1 
ATOM 4685 C CA  . GLN D 3 38  ? 138.890 139.622 193.216 1.00 107.43 ? 39   GLN D CA  1 
ATOM 4686 C C   . GLN D 3 38  ? 138.501 140.935 193.878 1.00 115.98 ? 39   GLN D C   1 
ATOM 4687 O O   . GLN D 3 38  ? 139.234 141.927 193.777 1.00 118.25 ? 39   GLN D O   1 
ATOM 4688 C CB  . GLN D 3 38  ? 140.220 139.120 193.778 1.00 105.40 ? 39   GLN D CB  1 
ATOM 4689 C CG  . GLN D 3 38  ? 140.198 138.897 195.280 1.00 104.89 ? 39   GLN D CG  1 
ATOM 4690 C CD  . GLN D 3 38  ? 141.559 138.552 195.843 1.00 104.38 ? 39   GLN D CD  1 
ATOM 4691 O OE1 . GLN D 3 38  ? 142.585 138.789 195.206 1.00 100.36 ? 39   GLN D OE1 1 
ATOM 4692 N NE2 . GLN D 3 38  ? 141.576 137.988 197.043 1.00 104.04 ? 39   GLN D NE2 1 
ATOM 4693 N N   . LYS D 3 39  ? 137.348 140.940 194.541 1.00 118.31 ? 40   LYS D N   1 
ATOM 4694 C CA  . LYS D 3 39  ? 136.942 142.058 195.372 1.00 122.48 ? 40   LYS D CA  1 
ATOM 4695 C C   . LYS D 3 39  ? 137.657 141.988 196.720 1.00 124.99 ? 40   LYS D C   1 
ATOM 4696 O O   . LYS D 3 39  ? 137.992 140.899 197.194 1.00 123.93 ? 40   LYS D O   1 
ATOM 4697 C CB  . LYS D 3 39  ? 135.432 142.044 195.582 1.00 123.75 ? 40   LYS D CB  1 
ATOM 4698 C CG  . LYS D 3 39  ? 134.628 142.178 194.299 1.00 129.23 ? 40   LYS D CG  1 
ATOM 4699 C CD  . LYS D 3 39  ? 133.137 142.038 194.563 1.00 133.16 ? 40   LYS D CD  1 
ATOM 4700 C CE  . LYS D 3 39  ? 132.335 142.150 193.276 1.00 126.65 ? 40   LYS D CE  1 
ATOM 4701 N NZ  . LYS D 3 39  ? 130.880 141.937 193.507 1.00 123.74 ? 40   LYS D NZ  1 
ATOM 4702 N N   . PRO D 3 40  ? 137.906 143.132 197.356 1.00 127.94 ? 41   PRO D N   1 
ATOM 4703 C CA  . PRO D 3 40  ? 138.614 143.115 198.643 1.00 128.65 ? 41   PRO D CA  1 
ATOM 4704 C C   . PRO D 3 40  ? 137.819 142.366 199.702 1.00 129.08 ? 41   PRO D C   1 
ATOM 4705 O O   . PRO D 3 40  ? 136.652 142.669 199.960 1.00 128.41 ? 41   PRO D O   1 
ATOM 4706 C CB  . PRO D 3 40  ? 138.763 144.602 198.985 1.00 126.11 ? 41   PRO D CB  1 
ATOM 4707 C CG  . PRO D 3 40  ? 137.686 145.280 198.206 1.00 125.02 ? 41   PRO D CG  1 
ATOM 4708 C CD  . PRO D 3 40  ? 137.562 144.500 196.935 1.00 124.93 ? 41   PRO D CD  1 
ATOM 4709 N N   . GLY D 3 41  ? 138.465 141.379 200.317 1.00 126.40 ? 42   GLY D N   1 
ATOM 4710 C CA  . GLY D 3 41  ? 137.818 140.560 201.321 1.00 126.32 ? 42   GLY D CA  1 
ATOM 4711 C C   . GLY D 3 41  ? 136.950 139.446 200.785 1.00 126.17 ? 42   GLY D C   1 
ATOM 4712 O O   . GLY D 3 41  ? 136.179 138.862 201.555 1.00 127.43 ? 42   GLY D O   1 
ATOM 4713 N N   . LYS D 3 42  ? 137.044 139.131 199.495 1.00 125.69 ? 43   LYS D N   1 
ATOM 4714 C CA  . LYS D 3 42  ? 136.235 138.082 198.894 1.00 122.76 ? 43   LYS D CA  1 
ATOM 4715 C C   . LYS D 3 42  ? 137.101 137.240 197.968 1.00 120.08 ? 43   LYS D C   1 
ATOM 4716 O O   . LYS D 3 42  ? 138.149 137.680 197.490 1.00 115.66 ? 43   LYS D O   1 
ATOM 4717 C CB  . LYS D 3 42  ? 135.040 138.664 198.125 1.00 119.72 ? 43   LYS D CB  1 
ATOM 4718 N N   . ALA D 3 43  ? 136.650 136.011 197.728 1.00 117.51 ? 44   ALA D N   1 
ATOM 4719 C CA  . ALA D 3 43  ? 137.378 135.103 196.859 1.00 107.85 ? 44   ALA D CA  1 
ATOM 4720 C C   . ALA D 3 43  ? 137.319 135.583 195.409 1.00 102.58 ? 44   ALA D C   1 
ATOM 4721 O O   . ALA D 3 43  ? 136.359 136.244 195.004 1.00 103.18 ? 44   ALA D O   1 
ATOM 4722 C CB  . ALA D 3 43  ? 136.804 133.693 196.960 1.00 102.40 ? 44   ALA D CB  1 
ATOM 4723 N N   . PRO D 3 44  ? 138.338 135.274 194.611 1.00 92.63  ? 45   PRO D N   1 
ATOM 4724 C CA  . PRO D 3 44  ? 138.323 135.681 193.203 1.00 87.71  ? 45   PRO D CA  1 
ATOM 4725 C C   . PRO D 3 44  ? 137.236 134.960 192.422 1.00 80.11  ? 45   PRO D C   1 
ATOM 4726 O O   . PRO D 3 44  ? 136.777 133.877 192.786 1.00 79.30  ? 45   PRO D O   1 
ATOM 4727 C CB  . PRO D 3 44  ? 139.717 135.291 192.703 1.00 81.12  ? 45   PRO D CB  1 
ATOM 4728 C CG  . PRO D 3 44  ? 140.553 135.219 193.931 1.00 85.59  ? 45   PRO D CG  1 
ATOM 4729 C CD  . PRO D 3 44  ? 139.639 134.708 195.000 1.00 90.60  ? 45   PRO D CD  1 
ATOM 4730 N N   . LYS D 3 45  ? 136.812 135.600 191.336 1.00 82.80  ? 46   LYS D N   1 
ATOM 4731 C CA  . LYS D 3 45  ? 135.816 135.045 190.431 1.00 81.22  ? 46   LYS D CA  1 
ATOM 4732 C C   . LYS D 3 45  ? 136.398 135.001 189.028 1.00 77.23  ? 46   LYS D C   1 
ATOM 4733 O O   . LYS D 3 45  ? 136.978 135.988 188.565 1.00 77.77  ? 46   LYS D O   1 
ATOM 4734 C CB  . LYS D 3 45  ? 134.527 135.872 190.443 1.00 86.61  ? 46   LYS D CB  1 
ATOM 4735 C CG  . LYS D 3 45  ? 133.825 135.905 191.789 1.00 91.08  ? 46   LYS D CG  1 
ATOM 4736 C CD  . LYS D 3 45  ? 132.524 136.684 191.719 1.00 92.24  ? 46   LYS D CD  1 
ATOM 4737 C CE  . LYS D 3 45  ? 131.828 136.706 193.070 1.00 98.90  ? 46   LYS D CE  1 
ATOM 4738 N NZ  . LYS D 3 45  ? 130.535 137.441 193.023 1.00 99.24  ? 46   LYS D NZ  1 
ATOM 4739 N N   . LEU D 3 46  ? 136.244 133.864 188.356 1.00 68.35  ? 47   LEU D N   1 
ATOM 4740 C CA  . LEU D 3 46  ? 136.750 133.731 186.998 1.00 65.85  ? 47   LEU D CA  1 
ATOM 4741 C C   . LEU D 3 46  ? 135.914 134.572 186.044 1.00 69.59  ? 47   LEU D C   1 
ATOM 4742 O O   . LEU D 3 46  ? 134.683 134.476 186.029 1.00 72.34  ? 47   LEU D O   1 
ATOM 4743 C CB  . LEU D 3 46  ? 136.737 132.267 186.564 1.00 62.32  ? 47   LEU D CB  1 
ATOM 4744 C CG  . LEU D 3 46  ? 137.089 131.957 185.107 1.00 53.50  ? 47   LEU D CG  1 
ATOM 4745 C CD1 . LEU D 3 46  ? 138.518 132.330 184.804 1.00 47.90  ? 47   LEU D CD1 1 
ATOM 4746 C CD2 . LEU D 3 46  ? 136.853 130.498 184.813 1.00 50.44  ? 47   LEU D CD2 1 
ATOM 4747 N N   . LEU D 3 47  ? 136.586 135.399 185.247 1.00 67.03  ? 48   LEU D N   1 
ATOM 4748 C CA  . LEU D 3 47  ? 135.933 136.209 184.228 1.00 68.74  ? 48   LEU D CA  1 
ATOM 4749 C C   . LEU D 3 47  ? 136.157 135.671 182.825 1.00 66.22  ? 48   LEU D C   1 
ATOM 4750 O O   . LEU D 3 47  ? 135.210 135.572 182.041 1.00 69.24  ? 48   LEU D O   1 
ATOM 4751 C CB  . LEU D 3 47  ? 136.425 137.659 184.301 1.00 69.99  ? 48   LEU D CB  1 
ATOM 4752 C CG  . LEU D 3 47  ? 136.086 138.469 185.549 1.00 79.37  ? 48   LEU D CG  1 
ATOM 4753 C CD1 . LEU D 3 47  ? 136.569 139.889 185.366 1.00 93.18  ? 48   LEU D CD1 1 
ATOM 4754 C CD2 . LEU D 3 47  ? 134.594 138.442 185.829 1.00 83.56  ? 48   LEU D CD2 1 
ATOM 4755 N N   . ILE D 3 48  ? 137.395 135.327 182.482 1.00 61.93  ? 49   ILE D N   1 
ATOM 4756 C CA  . ILE D 3 48  ? 137.722 134.852 181.140 1.00 55.10  ? 49   ILE D CA  1 
ATOM 4757 C C   . ILE D 3 48  ? 138.506 133.557 181.273 1.00 50.46  ? 49   ILE D C   1 
ATOM 4758 O O   . ILE D 3 48  ? 139.557 133.538 181.919 1.00 52.42  ? 49   ILE D O   1 
ATOM 4759 C CB  . ILE D 3 48  ? 138.521 135.898 180.349 1.00 53.47  ? 49   ILE D CB  1 
ATOM 4760 C CG1 . ILE D 3 48  ? 137.666 137.143 180.130 1.00 62.20  ? 49   ILE D CG1 1 
ATOM 4761 C CG2 . ILE D 3 48  ? 138.975 135.338 179.028 1.00 50.90  ? 49   ILE D CG2 1 
ATOM 4762 C CD1 . ILE D 3 48  ? 138.285 138.140 179.209 1.00 73.13  ? 49   ILE D CD1 1 
ATOM 4763 N N   . TYR D 3 49  ? 138.009 132.479 180.667 1.00 45.81  ? 50   TYR D N   1 
ATOM 4764 C CA  . TYR D 3 49  ? 138.610 131.175 180.919 1.00 41.33  ? 50   TYR D CA  1 
ATOM 4765 C C   . TYR D 3 49  ? 139.628 130.751 179.870 1.00 37.37  ? 50   TYR D C   1 
ATOM 4766 O O   . TYR D 3 49  ? 140.661 130.185 180.229 1.00 43.12  ? 50   TYR D O   1 
ATOM 4767 C CB  . TYR D 3 49  ? 137.538 130.092 181.081 1.00 44.00  ? 50   TYR D CB  1 
ATOM 4768 C CG  . TYR D 3 49  ? 136.516 129.951 179.984 1.00 47.06  ? 50   TYR D CG  1 
ATOM 4769 C CD1 . TYR D 3 49  ? 136.816 129.290 178.806 1.00 47.35  ? 50   TYR D CD1 1 
ATOM 4770 C CD2 . TYR D 3 49  ? 135.227 130.419 180.160 1.00 53.13  ? 50   TYR D CD2 1 
ATOM 4771 C CE1 . TYR D 3 49  ? 135.877 129.140 177.819 1.00 50.09  ? 50   TYR D CE1 1 
ATOM 4772 C CE2 . TYR D 3 49  ? 134.281 130.274 179.179 1.00 58.53  ? 50   TYR D CE2 1 
ATOM 4773 C CZ  . TYR D 3 49  ? 134.608 129.634 178.010 1.00 58.72  ? 50   TYR D CZ  1 
ATOM 4774 O OH  . TYR D 3 49  ? 133.658 129.489 177.026 1.00 71.45  ? 50   TYR D OH  1 
ATOM 4775 N N   . SER D 3 50  ? 139.393 130.995 178.590 1.00 36.02  ? 51   SER D N   1 
ATOM 4776 C CA  . SER D 3 50  ? 140.481 130.887 177.629 1.00 34.44  ? 51   SER D CA  1 
ATOM 4777 C C   . SER D 3 50  ? 141.225 132.213 177.654 1.00 37.92  ? 51   SER D C   1 
ATOM 4778 O O   . SER D 3 50  ? 141.031 133.032 178.552 1.00 44.91  ? 51   SER D O   1 
ATOM 4779 C CB  . SER D 3 50  ? 139.963 130.531 176.241 1.00 38.05  ? 51   SER D CB  1 
ATOM 4780 O OG  . SER D 3 50  ? 139.421 129.226 176.214 1.00 42.44  ? 51   SER D OG  1 
ATOM 4781 N N   . ALA D 3 51  ? 142.099 132.449 176.680 1.00 35.10  ? 52   ALA D N   1 
ATOM 4782 C CA  . ALA D 3 51  ? 142.697 133.774 176.577 1.00 33.47  ? 52   ALA D CA  1 
ATOM 4783 C C   . ALA D 3 51  ? 141.636 134.824 176.288 1.00 43.24  ? 52   ALA D C   1 
ATOM 4784 O O   . ALA D 3 51  ? 141.692 135.936 176.822 1.00 51.35  ? 52   ALA D O   1 
ATOM 4785 C CB  . ALA D 3 51  ? 143.772 133.793 175.495 1.00 40.46  ? 52   ALA D CB  1 
ATOM 4786 N N   . SER D 3 52  ? 140.655 134.483 175.452 1.00 52.99  ? 53   SER D N   1 
ATOM 4787 C CA  . SER D 3 52  ? 139.671 135.440 174.959 1.00 54.89  ? 53   SER D CA  1 
ATOM 4788 C C   . SER D 3 52  ? 138.274 134.837 174.921 1.00 47.80  ? 53   SER D C   1 
ATOM 4789 O O   . SER D 3 52  ? 137.513 135.066 173.977 1.00 50.54  ? 53   SER D O   1 
ATOM 4790 C CB  . SER D 3 52  ? 140.057 135.940 173.569 1.00 58.85  ? 53   SER D CB  1 
ATOM 4791 O OG  . SER D 3 52  ? 140.148 134.862 172.654 1.00 51.56  ? 53   SER D OG  1 
ATOM 4792 N N   . SER D 3 53  ? 137.902 134.065 175.938 1.00 45.19  ? 54   SER D N   1 
ATOM 4793 C CA  . SER D 3 53  ? 136.582 133.447 175.991 1.00 46.73  ? 54   SER D CA  1 
ATOM 4794 C C   . SER D 3 53  ? 135.904 133.832 177.293 1.00 57.01  ? 54   SER D C   1 
ATOM 4795 O O   . SER D 3 53  ? 136.434 133.560 178.373 1.00 62.44  ? 54   SER D O   1 
ATOM 4796 C CB  . SER D 3 53  ? 136.671 131.928 175.864 1.00 47.10  ? 54   SER D CB  1 
ATOM 4797 O OG  . SER D 3 53  ? 137.160 131.556 174.589 1.00 52.15  ? 54   SER D OG  1 
ATOM 4798 N N   . LEU D 3 54  ? 134.730 134.442 177.192 1.00 61.56  ? 55   LEU D N   1 
ATOM 4799 C CA  . LEU D 3 54  ? 134.054 134.992 178.358 1.00 67.18  ? 55   LEU D CA  1 
ATOM 4800 C C   . LEU D 3 54  ? 133.388 133.886 179.164 1.00 70.52  ? 55   LEU D C   1 
ATOM 4801 O O   . LEU D 3 54  ? 132.698 133.028 178.605 1.00 73.29  ? 55   LEU D O   1 
ATOM 4802 C CB  . LEU D 3 54  ? 133.019 136.027 177.924 1.00 74.94  ? 55   LEU D CB  1 
ATOM 4803 C CG  . LEU D 3 54  ? 132.484 136.946 179.019 1.00 83.21  ? 55   LEU D CG  1 
ATOM 4804 C CD1 . LEU D 3 54  ? 133.588 137.864 179.514 1.00 84.94  ? 55   LEU D CD1 1 
ATOM 4805 C CD2 . LEU D 3 54  ? 131.295 137.745 178.517 1.00 94.54  ? 55   LEU D CD2 1 
ATOM 4806 N N   . TYR D 3 55  ? 133.591 133.911 180.478 1.00 69.70  ? 56   TYR D N   1 
ATOM 4807 C CA  . TYR D 3 55  ? 132.980 132.919 181.349 1.00 73.63  ? 56   TYR D CA  1 
ATOM 4808 C C   . TYR D 3 55  ? 131.484 133.175 181.481 1.00 80.80  ? 56   TYR D C   1 
ATOM 4809 O O   . TYR D 3 55  ? 131.017 134.315 181.421 1.00 83.80  ? 56   TYR D O   1 
ATOM 4810 C CB  . TYR D 3 55  ? 133.644 132.937 182.725 1.00 71.19  ? 56   TYR D CB  1 
ATOM 4811 C CG  . TYR D 3 55  ? 133.180 131.843 183.656 1.00 73.08  ? 56   TYR D CG  1 
ATOM 4812 C CD1 . TYR D 3 55  ? 133.171 130.518 183.251 1.00 70.40  ? 56   TYR D CD1 1 
ATOM 4813 C CD2 . TYR D 3 55  ? 132.769 132.133 184.948 1.00 76.65  ? 56   TYR D CD2 1 
ATOM 4814 C CE1 . TYR D 3 55  ? 132.753 129.516 184.101 1.00 72.75  ? 56   TYR D CE1 1 
ATOM 4815 C CE2 . TYR D 3 55  ? 132.351 131.137 185.805 1.00 73.40  ? 56   TYR D CE2 1 
ATOM 4816 C CZ  . TYR D 3 55  ? 132.344 129.832 185.376 1.00 75.32  ? 56   TYR D CZ  1 
ATOM 4817 O OH  . TYR D 3 55  ? 131.928 128.837 186.227 1.00 79.19  ? 56   TYR D OH  1 
ATOM 4818 N N   . SER D 3 56  ? 130.729 132.095 181.656 1.00 84.32  ? 57   SER D N   1 
ATOM 4819 C CA  . SER D 3 56  ? 129.280 132.205 181.744 1.00 89.69  ? 57   SER D CA  1 
ATOM 4820 C C   . SER D 3 56  ? 128.866 132.893 183.039 1.00 94.19  ? 57   SER D C   1 
ATOM 4821 O O   . SER D 3 56  ? 129.409 132.617 184.112 1.00 90.95  ? 57   SER D O   1 
ATOM 4822 C CB  . SER D 3 56  ? 128.634 130.822 181.658 1.00 89.24  ? 57   SER D CB  1 
ATOM 4823 O OG  . SER D 3 56  ? 128.975 130.027 182.779 1.00 89.78  ? 57   SER D OG  1 
ATOM 4824 N N   . GLY D 3 57  ? 127.894 133.797 182.931 1.00 98.88  ? 58   GLY D N   1 
ATOM 4825 C CA  . GLY D 3 57  ? 127.322 134.477 184.068 1.00 98.59  ? 58   GLY D CA  1 
ATOM 4826 C C   . GLY D 3 57  ? 127.891 135.854 184.342 1.00 100.41 ? 58   GLY D C   1 
ATOM 4827 O O   . GLY D 3 57  ? 127.234 136.655 185.016 1.00 102.84 ? 58   GLY D O   1 
ATOM 4828 N N   . VAL D 3 58  ? 129.086 136.152 183.843 1.00 100.76 ? 59   VAL D N   1 
ATOM 4829 C CA  . VAL D 3 58  ? 129.693 137.464 184.054 1.00 103.92 ? 59   VAL D CA  1 
ATOM 4830 C C   . VAL D 3 58  ? 129.129 138.426 183.015 1.00 107.86 ? 59   VAL D C   1 
ATOM 4831 O O   . VAL D 3 58  ? 128.650 137.983 181.961 1.00 104.99 ? 59   VAL D O   1 
ATOM 4832 C CB  . VAL D 3 58  ? 131.227 137.390 183.990 1.00 98.54  ? 59   VAL D CB  1 
ATOM 4833 C CG1 . VAL D 3 58  ? 131.737 136.226 184.824 1.00 89.09  ? 59   VAL D CG1 1 
ATOM 4834 C CG2 . VAL D 3 58  ? 131.700 137.280 182.556 1.00 92.47  ? 59   VAL D CG2 1 
ATOM 4835 N N   . PRO D 3 59  ? 129.137 139.735 183.272 1.00 112.94 ? 60   PRO D N   1 
ATOM 4836 C CA  . PRO D 3 59  ? 128.612 140.682 182.282 1.00 114.78 ? 60   PRO D CA  1 
ATOM 4837 C C   . PRO D 3 59  ? 129.411 140.646 180.989 1.00 114.05 ? 60   PRO D C   1 
ATOM 4838 O O   . PRO D 3 59  ? 130.616 140.385 180.981 1.00 112.16 ? 60   PRO D O   1 
ATOM 4839 C CB  . PRO D 3 59  ? 128.744 142.037 182.984 1.00 116.97 ? 60   PRO D CB  1 
ATOM 4840 C CG  . PRO D 3 59  ? 128.751 141.706 184.439 1.00 115.13 ? 60   PRO D CG  1 
ATOM 4841 C CD  . PRO D 3 59  ? 129.473 140.399 184.543 1.00 109.26 ? 60   PRO D CD  1 
ATOM 4842 N N   . SER D 3 60  ? 128.718 140.924 179.883 1.00 112.93 ? 61   SER D N   1 
ATOM 4843 C CA  . SER D 3 60  ? 129.317 140.837 178.557 1.00 112.73 ? 61   SER D CA  1 
ATOM 4844 C C   . SER D 3 60  ? 130.295 141.966 178.264 1.00 112.15 ? 61   SER D C   1 
ATOM 4845 O O   . SER D 3 60  ? 130.956 141.929 177.221 1.00 108.78 ? 61   SER D O   1 
ATOM 4846 C CB  . SER D 3 60  ? 128.219 140.820 177.492 1.00 116.58 ? 61   SER D CB  1 
ATOM 4847 O OG  . SER D 3 60  ? 127.312 139.754 177.711 1.00 117.06 ? 61   SER D OG  1 
ATOM 4848 N N   . ARG D 3 61  ? 130.396 142.967 179.141 1.00 115.48 ? 62   ARG D N   1 
ATOM 4849 C CA  . ARG D 3 61  ? 131.284 144.096 178.879 1.00 118.68 ? 62   ARG D CA  1 
ATOM 4850 C C   . ARG D 3 61  ? 132.750 143.681 178.877 1.00 118.46 ? 62   ARG D C   1 
ATOM 4851 O O   . ARG D 3 61  ? 133.572 144.322 178.211 1.00 114.75 ? 62   ARG D O   1 
ATOM 4852 C CB  . ARG D 3 61  ? 131.045 145.198 179.911 1.00 122.83 ? 62   ARG D CB  1 
ATOM 4853 C CG  . ARG D 3 61  ? 132.136 145.310 180.958 1.00 123.78 ? 62   ARG D CG  1 
ATOM 4854 C CD  . ARG D 3 61  ? 131.658 146.046 182.190 1.00 126.67 ? 62   ARG D CD  1 
ATOM 4855 N NE  . ARG D 3 61  ? 130.579 145.341 182.868 1.00 127.58 ? 62   ARG D NE  1 
ATOM 4856 C CZ  . ARG D 3 61  ? 130.103 145.680 184.057 1.00 130.33 ? 62   ARG D CZ  1 
ATOM 4857 N NH1 . ARG D 3 61  ? 130.597 146.703 184.731 1.00 132.94 ? 62   ARG D NH1 1 
ATOM 4858 N NH2 . ARG D 3 61  ? 129.107 144.973 184.582 1.00 128.33 ? 62   ARG D NH2 1 
ATOM 4859 N N   . PHE D 3 62  ? 133.100 142.624 179.608 1.00 118.35 ? 63   PHE D N   1 
ATOM 4860 C CA  . PHE D 3 62  ? 134.482 142.173 179.679 1.00 113.76 ? 63   PHE D CA  1 
ATOM 4861 C C   . PHE D 3 62  ? 134.863 141.425 178.410 1.00 108.72 ? 63   PHE D C   1 
ATOM 4862 O O   . PHE D 3 62  ? 134.095 140.603 177.903 1.00 106.63 ? 63   PHE D O   1 
ATOM 4863 C CB  . PHE D 3 62  ? 134.690 141.269 180.894 1.00 112.41 ? 63   PHE D CB  1 
ATOM 4864 C CG  . PHE D 3 62  ? 134.427 141.944 182.208 1.00 114.66 ? 63   PHE D CG  1 
ATOM 4865 C CD1 . PHE D 3 62  ? 135.428 142.646 182.854 1.00 116.45 ? 63   PHE D CD1 1 
ATOM 4866 C CD2 . PHE D 3 62  ? 133.179 141.868 182.802 1.00 112.72 ? 63   PHE D CD2 1 
ATOM 4867 C CE1 . PHE D 3 62  ? 135.190 143.264 184.064 1.00 116.77 ? 63   PHE D CE1 1 
ATOM 4868 C CE2 . PHE D 3 62  ? 132.936 142.484 184.012 1.00 113.96 ? 63   PHE D CE2 1 
ATOM 4869 C CZ  . PHE D 3 62  ? 133.943 143.182 184.644 1.00 116.80 ? 63   PHE D CZ  1 
ATOM 4870 N N   . SER D 3 63  ? 136.054 141.715 177.895 1.00 105.15 ? 64   SER D N   1 
ATOM 4871 C CA  . SER D 3 63  ? 136.553 141.031 176.712 1.00 100.01 ? 64   SER D CA  1 
ATOM 4872 C C   . SER D 3 63  ? 138.018 140.683 176.913 1.00 94.64  ? 64   SER D C   1 
ATOM 4873 O O   . SER D 3 63  ? 138.723 141.324 177.694 1.00 96.57  ? 64   SER D O   1 
ATOM 4874 C CB  . SER D 3 63  ? 136.386 141.883 175.447 1.00 101.50 ? 64   SER D CB  1 
ATOM 4875 O OG  . SER D 3 63  ? 137.217 143.028 175.489 1.00 103.22 ? 64   SER D OG  1 
ATOM 4876 N N   . GLY D 3 64  ? 138.468 139.652 176.201 1.00 84.70  ? 65   GLY D N   1 
ATOM 4877 C CA  . GLY D 3 64  ? 139.858 139.267 176.227 1.00 74.47  ? 65   GLY D CA  1 
ATOM 4878 C C   . GLY D 3 64  ? 140.412 139.182 174.820 1.00 71.83  ? 65   GLY D C   1 
ATOM 4879 O O   . GLY D 3 64  ? 139.676 139.067 173.841 1.00 74.55  ? 65   GLY D O   1 
ATOM 4880 N N   . SER D 3 65  ? 141.734 139.265 174.734 1.00 68.92  ? 66   SER D N   1 
ATOM 4881 C CA  . SER D 3 65  ? 142.402 139.149 173.447 1.00 67.28  ? 66   SER D CA  1 
ATOM 4882 C C   . SER D 3 65  ? 143.794 138.582 173.655 1.00 65.01  ? 66   SER D C   1 
ATOM 4883 O O   . SER D 3 65  ? 144.445 138.874 174.659 1.00 63.52  ? 66   SER D O   1 
ATOM 4884 C CB  . SER D 3 65  ? 142.488 140.501 172.730 1.00 71.30  ? 66   SER D CB  1 
ATOM 4885 O OG  . SER D 3 65  ? 143.474 141.329 173.317 1.00 74.84  ? 66   SER D OG  1 
ATOM 4886 N N   . ARG D 3 66  ? 144.242 137.772 172.702 1.00 61.48  ? 67   ARG D N   1 
ATOM 4887 C CA  . ARG D 3 66  ? 145.579 137.199 172.715 1.00 56.02  ? 67   ARG D CA  1 
ATOM 4888 C C   . ARG D 3 66  ? 146.326 137.647 171.469 1.00 57.81  ? 67   ARG D C   1 
ATOM 4889 O O   . ARG D 3 66  ? 145.782 137.590 170.362 1.00 61.22  ? 67   ARG D O   1 
ATOM 4890 C CB  . ARG D 3 66  ? 145.532 135.672 172.775 1.00 53.11  ? 67   ARG D CB  1 
ATOM 4891 C CG  . ARG D 3 66  ? 146.905 135.043 172.787 1.00 49.94  ? 67   ARG D CG  1 
ATOM 4892 C CD  . ARG D 3 66  ? 146.881 133.598 172.352 1.00 45.68  ? 67   ARG D CD  1 
ATOM 4893 N NE  . ARG D 3 66  ? 148.232 133.058 172.291 1.00 47.14  ? 67   ARG D NE  1 
ATOM 4894 C CZ  . ARG D 3 66  ? 148.563 131.936 171.670 1.00 44.53  ? 67   ARG D CZ  1 
ATOM 4895 N NH1 . ARG D 3 66  ? 147.660 131.204 171.041 1.00 44.45  ? 67   ARG D NH1 1 
ATOM 4896 N NH2 . ARG D 3 66  ? 149.833 131.544 171.674 1.00 42.77  ? 67   ARG D NH2 1 
ATOM 4897 N N   . SER D 3 67  ? 147.567 138.094 171.652 1.00 56.95  ? 68   SER D N   1 
ATOM 4898 C CA  . SER D 3 67  ? 148.452 138.467 170.547 1.00 60.37  ? 68   SER D CA  1 
ATOM 4899 C C   . SER D 3 67  ? 149.825 137.903 170.901 1.00 60.23  ? 68   SER D C   1 
ATOM 4900 O O   . SER D 3 67  ? 150.614 138.550 171.595 1.00 63.04  ? 68   SER D O   1 
ATOM 4901 C CB  . SER D 3 67  ? 148.491 139.975 170.339 1.00 62.29  ? 68   SER D CB  1 
ATOM 4902 O OG  . SER D 3 67  ? 147.197 140.488 170.082 1.00 68.45  ? 68   SER D OG  1 
ATOM 4903 N N   . GLY D 3 68  ? 150.098 136.690 170.432 1.00 57.87  ? 69   GLY D N   1 
ATOM 4904 C CA  . GLY D 3 68  ? 151.338 136.032 170.783 1.00 55.09  ? 69   GLY D CA  1 
ATOM 4905 C C   . GLY D 3 68  ? 151.423 135.756 172.267 1.00 54.43  ? 69   GLY D C   1 
ATOM 4906 O O   . GLY D 3 68  ? 150.736 134.871 172.781 1.00 54.57  ? 69   GLY D O   1 
ATOM 4907 N N   . THR D 3 69  ? 152.267 136.506 172.968 1.00 55.96  ? 70   THR D N   1 
ATOM 4908 C CA  . THR D 3 69  ? 152.408 136.384 174.410 1.00 56.41  ? 70   THR D CA  1 
ATOM 4909 C C   . THR D 3 69  ? 151.816 137.577 175.153 1.00 61.96  ? 70   THR D C   1 
ATOM 4910 O O   . THR D 3 69  ? 152.073 137.741 176.348 1.00 65.84  ? 70   THR D O   1 
ATOM 4911 C CB  . THR D 3 69  ? 153.882 136.204 174.775 1.00 60.12  ? 70   THR D CB  1 
ATOM 4912 O OG1 . THR D 3 69  ? 154.564 135.570 173.689 1.00 64.99  ? 70   THR D OG1 1 
ATOM 4913 C CG2 . THR D 3 69  ? 154.022 135.319 175.975 1.00 56.80  ? 70   THR D CG2 1 
ATOM 4914 N N   . ASP D 3 70  ? 151.032 138.413 174.478 1.00 60.41  ? 71   ASP D N   1 
ATOM 4915 C CA  . ASP D 3 70  ? 150.400 139.572 175.095 1.00 59.25  ? 71   ASP D CA  1 
ATOM 4916 C C   . ASP D 3 70  ? 148.911 139.296 175.248 1.00 58.44  ? 71   ASP D C   1 
ATOM 4917 O O   . ASP D 3 70  ? 148.201 139.149 174.250 1.00 59.90  ? 71   ASP D O   1 
ATOM 4918 C CB  . ASP D 3 70  ? 150.629 140.825 174.251 1.00 67.63  ? 71   ASP D CB  1 
ATOM 4919 C CG  . ASP D 3 70  ? 152.059 141.317 174.308 1.00 75.64  ? 71   ASP D CG  1 
ATOM 4920 O OD1 . ASP D 3 70  ? 152.463 141.845 175.364 1.00 79.87  ? 71   ASP D OD1 1 
ATOM 4921 O OD2 . ASP D 3 70  ? 152.781 141.169 173.301 1.00 74.70  ? 71   ASP D OD2 1 
ATOM 4922 N N   . PHE D 3 71  ? 148.435 139.240 176.487 1.00 59.76  ? 72   PHE D N   1 
ATOM 4923 C CA  . PHE D 3 71  ? 147.038 138.955 176.778 1.00 61.16  ? 72   PHE D CA  1 
ATOM 4924 C C   . PHE D 3 71  ? 146.397 140.199 177.371 1.00 67.82  ? 72   PHE D C   1 
ATOM 4925 O O   . PHE D 3 71  ? 146.891 140.746 178.360 1.00 70.54  ? 72   PHE D O   1 
ATOM 4926 C CB  . PHE D 3 71  ? 146.913 137.770 177.738 1.00 54.51  ? 72   PHE D CB  1 
ATOM 4927 C CG  . PHE D 3 71  ? 147.575 136.518 177.239 1.00 49.28  ? 72   PHE D CG  1 
ATOM 4928 C CD1 . PHE D 3 71  ? 148.929 136.312 177.421 1.00 47.92  ? 72   PHE D CD1 1 
ATOM 4929 C CD2 . PHE D 3 71  ? 146.845 135.551 176.579 1.00 47.38  ? 72   PHE D CD2 1 
ATOM 4930 C CE1 . PHE D 3 71  ? 149.537 135.167 176.953 1.00 45.76  ? 72   PHE D CE1 1 
ATOM 4931 C CE2 . PHE D 3 71  ? 147.450 134.407 176.114 1.00 41.56  ? 72   PHE D CE2 1 
ATOM 4932 C CZ  . PHE D 3 71  ? 148.796 134.216 176.299 1.00 41.47  ? 72   PHE D CZ  1 
ATOM 4933 N N   . THR D 3 72  ? 145.303 140.646 176.767 1.00 69.21  ? 73   THR D N   1 
ATOM 4934 C CA  . THR D 3 72  ? 144.681 141.915 177.112 1.00 78.27  ? 73   THR D CA  1 
ATOM 4935 C C   . THR D 3 72  ? 143.269 141.679 177.622 1.00 81.36  ? 73   THR D C   1 
ATOM 4936 O O   . THR D 3 72  ? 142.476 140.993 176.971 1.00 82.47  ? 73   THR D O   1 
ATOM 4937 C CB  . THR D 3 72  ? 144.659 142.855 175.903 1.00 85.36  ? 73   THR D CB  1 
ATOM 4938 O OG1 . THR D 3 72  ? 145.961 143.420 175.707 1.00 86.66  ? 73   THR D OG1 1 
ATOM 4939 C CG2 . THR D 3 72  ? 143.649 143.969 176.099 1.00 90.95  ? 73   THR D CG2 1 
ATOM 4940 N N   . LEU D 3 73  ? 142.967 142.243 178.788 1.00 83.84  ? 74   LEU D N   1 
ATOM 4941 C CA  . LEU D 3 73  ? 141.615 142.279 179.327 1.00 87.49  ? 74   LEU D CA  1 
ATOM 4942 C C   . LEU D 3 73  ? 141.074 143.692 179.158 1.00 97.75  ? 74   LEU D C   1 
ATOM 4943 O O   . LEU D 3 73  ? 141.694 144.655 179.621 1.00 102.08 ? 74   LEU D O   1 
ATOM 4944 C CB  . LEU D 3 73  ? 141.596 141.871 180.799 1.00 82.76  ? 74   LEU D CB  1 
ATOM 4945 C CG  . LEU D 3 73  ? 140.270 142.070 181.535 1.00 85.65  ? 74   LEU D CG  1 
ATOM 4946 C CD1 . LEU D 3 73  ? 139.219 141.113 181.013 1.00 84.58  ? 74   LEU D CD1 1 
ATOM 4947 C CD2 . LEU D 3 73  ? 140.451 141.907 183.033 1.00 84.14  ? 74   LEU D CD2 1 
ATOM 4948 N N   . THR D 3 74  ? 139.926 143.815 178.502 1.00 101.64 ? 75   THR D N   1 
ATOM 4949 C CA  . THR D 3 74  ? 139.345 145.106 178.171 1.00 110.48 ? 75   THR D CA  1 
ATOM 4950 C C   . THR D 3 74  ? 137.963 145.232 178.794 1.00 113.64 ? 75   THR D C   1 
ATOM 4951 O O   . THR D 3 74  ? 137.151 144.302 178.730 1.00 110.28 ? 75   THR D O   1 
ATOM 4952 C CB  . THR D 3 74  ? 139.254 145.292 176.653 1.00 111.22 ? 75   THR D CB  1 
ATOM 4953 O OG1 . THR D 3 74  ? 140.551 145.112 176.071 1.00 108.50 ? 75   THR D OG1 1 
ATOM 4954 C CG2 . THR D 3 74  ? 138.741 146.683 176.311 1.00 115.52 ? 75   THR D CG2 1 
ATOM 4955 N N   . ILE D 3 75  ? 137.708 146.389 179.402 1.00 121.23 ? 76   ILE D N   1 
ATOM 4956 C CA  . ILE D 3 75  ? 136.411 146.729 179.973 1.00 124.91 ? 76   ILE D CA  1 
ATOM 4957 C C   . ILE D 3 75  ? 135.918 147.997 179.290 1.00 130.02 ? 76   ILE D C   1 
ATOM 4958 O O   . ILE D 3 75  ? 136.625 149.011 179.273 1.00 131.24 ? 76   ILE D O   1 
ATOM 4959 C CB  . ILE D 3 75  ? 136.496 146.924 181.497 1.00 124.66 ? 76   ILE D CB  1 
ATOM 4960 C CG1 . ILE D 3 75  ? 137.192 145.729 182.149 1.00 119.67 ? 76   ILE D CG1 1 
ATOM 4961 C CG2 . ILE D 3 75  ? 135.111 147.123 182.085 1.00 127.82 ? 76   ILE D CG2 1 
ATOM 4962 C CD1 . ILE D 3 75  ? 137.502 145.927 183.616 1.00 118.23 ? 76   ILE D CD1 1 
ATOM 4963 N N   . SER D 3 76  ? 134.712 147.939 178.726 1.00 132.10 ? 77   SER D N   1 
ATOM 4964 C CA  . SER D 3 76  ? 134.177 149.063 177.963 1.00 136.41 ? 77   SER D CA  1 
ATOM 4965 C C   . SER D 3 76  ? 133.291 149.967 178.819 1.00 140.52 ? 77   SER D C   1 
ATOM 4966 O O   . SER D 3 76  ? 133.577 151.158 178.976 1.00 140.22 ? 77   SER D O   1 
ATOM 4967 C CB  . SER D 3 76  ? 133.399 148.547 176.747 1.00 135.94 ? 77   SER D CB  1 
ATOM 4968 O OG  . SER D 3 76  ? 132.289 147.764 177.147 1.00 134.02 ? 77   SER D OG  1 
ATOM 4969 N N   . SER D 3 77  ? 132.217 149.413 179.378 1.00 140.09 ? 78   SER D N   1 
ATOM 4970 C CA  . SER D 3 77  ? 131.253 150.178 180.168 1.00 140.00 ? 78   SER D CA  1 
ATOM 4971 C C   . SER D 3 77  ? 131.555 149.941 181.644 1.00 139.91 ? 78   SER D C   1 
ATOM 4972 O O   . SER D 3 77  ? 130.948 149.091 182.293 1.00 139.37 ? 78   SER D O   1 
ATOM 4973 C CB  . SER D 3 77  ? 129.825 149.778 179.815 1.00 137.15 ? 78   SER D CB  1 
ATOM 4974 O OG  . SER D 3 77  ? 128.890 150.429 180.656 1.00 139.88 ? 78   SER D OG  1 
ATOM 4975 N N   . LEU D 3 78  ? 132.490 150.723 182.182 1.00 139.82 ? 79   LEU D N   1 
ATOM 4976 C CA  . LEU D 3 78  ? 132.949 150.522 183.550 1.00 139.70 ? 79   LEU D CA  1 
ATOM 4977 C C   . LEU D 3 78  ? 131.881 150.949 184.548 1.00 140.60 ? 79   LEU D C   1 
ATOM 4978 O O   . LEU D 3 78  ? 131.821 152.116 184.943 1.00 141.72 ? 79   LEU D O   1 
ATOM 4979 C CB  . LEU D 3 78  ? 134.249 151.297 183.787 1.00 139.40 ? 79   LEU D CB  1 
ATOM 4980 C CG  . LEU D 3 78  ? 135.218 150.853 184.887 1.00 137.81 ? 79   LEU D CG  1 
ATOM 4981 C CD1 . LEU D 3 78  ? 136.576 151.496 184.667 1.00 138.58 ? 79   LEU D CD1 1 
ATOM 4982 C CD2 . LEU D 3 78  ? 134.700 151.191 186.274 1.00 139.29 ? 79   LEU D CD2 1 
ATOM 4983 N N   . GLN D 3 79  ? 131.039 150.009 184.966 1.00 139.62 ? 80   GLN D N   1 
ATOM 4984 C CA  . GLN D 3 79  ? 130.049 150.282 185.991 1.00 139.97 ? 80   GLN D CA  1 
ATOM 4985 C C   . GLN D 3 79  ? 130.726 150.357 187.359 1.00 142.72 ? 80   GLN D C   1 
ATOM 4986 O O   . GLN D 3 79  ? 131.864 149.911 187.521 1.00 142.34 ? 80   GLN D O   1 
ATOM 4987 C CB  . GLN D 3 79  ? 128.967 149.204 185.975 1.00 140.01 ? 80   GLN D CB  1 
ATOM 4988 C CG  . GLN D 3 79  ? 128.170 149.157 184.681 1.00 140.59 ? 80   GLN D CG  1 
ATOM 4989 C CD  . GLN D 3 79  ? 127.019 148.174 184.742 1.00 141.77 ? 80   GLN D CD  1 
ATOM 4990 O OE1 . GLN D 3 79  ? 126.764 147.562 185.779 1.00 143.79 ? 80   GLN D OE1 1 
ATOM 4991 N NE2 . GLN D 3 79  ? 126.315 148.018 183.626 1.00 138.82 ? 80   GLN D NE2 1 
ATOM 4992 N N   . PRO D 3 80  ? 130.055 150.935 188.363 1.00 146.47 ? 81   PRO D N   1 
ATOM 4993 C CA  . PRO D 3 80  ? 130.685 151.071 189.687 1.00 145.59 ? 81   PRO D CA  1 
ATOM 4994 C C   . PRO D 3 80  ? 130.979 149.754 190.391 1.00 145.48 ? 81   PRO D C   1 
ATOM 4995 O O   . PRO D 3 80  ? 131.485 149.782 191.519 1.00 144.29 ? 81   PRO D O   1 
ATOM 4996 C CB  . PRO D 3 80  ? 129.656 151.896 190.479 1.00 143.98 ? 81   PRO D CB  1 
ATOM 4997 C CG  . PRO D 3 80  ? 128.368 151.704 189.756 1.00 145.17 ? 81   PRO D CG  1 
ATOM 4998 C CD  . PRO D 3 80  ? 128.747 151.611 188.314 1.00 145.39 ? 81   PRO D CD  1 
ATOM 4999 N N   . GLU D 3 81  ? 130.691 148.606 189.779 1.00 145.67 ? 82   GLU D N   1 
ATOM 5000 C CA  . GLU D 3 81  ? 130.984 147.308 190.369 1.00 143.35 ? 82   GLU D CA  1 
ATOM 5001 C C   . GLU D 3 81  ? 132.279 146.699 189.844 1.00 139.56 ? 82   GLU D C   1 
ATOM 5002 O O   . GLU D 3 81  ? 132.565 145.533 190.132 1.00 136.80 ? 82   GLU D O   1 
ATOM 5003 C CB  . GLU D 3 81  ? 129.822 146.342 190.126 1.00 144.21 ? 82   GLU D CB  1 
ATOM 5004 C CG  . GLU D 3 81  ? 128.499 146.799 190.714 1.00 147.92 ? 82   GLU D CG  1 
ATOM 5005 C CD  . GLU D 3 81  ? 127.403 145.766 190.548 1.00 150.54 ? 82   GLU D CD  1 
ATOM 5006 O OE1 . GLU D 3 81  ? 127.702 144.651 190.071 1.00 149.08 ? 82   GLU D OE1 1 
ATOM 5007 O OE2 . GLU D 3 81  ? 126.241 146.067 190.895 1.00 150.05 ? 82   GLU D OE2 1 
ATOM 5008 N N   . ASP D 3 82  ? 133.067 147.459 189.081 1.00 139.43 ? 83   ASP D N   1 
ATOM 5009 C CA  . ASP D 3 82  ? 134.305 146.968 188.488 1.00 135.19 ? 83   ASP D CA  1 
ATOM 5010 C C   . ASP D 3 82  ? 135.542 147.484 189.214 1.00 135.60 ? 83   ASP D C   1 
ATOM 5011 O O   . ASP D 3 82  ? 136.643 147.442 188.657 1.00 134.28 ? 83   ASP D O   1 
ATOM 5012 C CB  . ASP D 3 82  ? 134.374 147.348 187.009 1.00 132.42 ? 83   ASP D CB  1 
ATOM 5013 C CG  . ASP D 3 82  ? 133.224 146.780 186.210 1.00 133.62 ? 83   ASP D CG  1 
ATOM 5014 O OD1 . ASP D 3 82  ? 132.337 146.139 186.811 1.00 134.01 ? 83   ASP D OD1 1 
ATOM 5015 O OD2 . ASP D 3 82  ? 133.203 146.975 184.977 1.00 133.31 ? 83   ASP D OD2 1 
ATOM 5016 N N   . PHE D 3 83  ? 135.386 147.979 190.440 1.00 137.27 ? 84   PHE D N   1 
ATOM 5017 C CA  . PHE D 3 83  ? 136.507 148.527 191.202 1.00 136.76 ? 84   PHE D CA  1 
ATOM 5018 C C   . PHE D 3 83  ? 137.026 147.447 192.147 1.00 135.76 ? 84   PHE D C   1 
ATOM 5019 O O   . PHE D 3 83  ? 136.770 147.448 193.352 1.00 138.66 ? 84   PHE D O   1 
ATOM 5020 C CB  . PHE D 3 83  ? 136.084 149.792 191.941 1.00 137.73 ? 84   PHE D CB  1 
ATOM 5021 C CG  . PHE D 3 83  ? 135.704 150.921 191.027 1.00 139.60 ? 84   PHE D CG  1 
ATOM 5022 C CD1 . PHE D 3 83  ? 136.670 151.779 190.528 1.00 139.60 ? 84   PHE D CD1 1 
ATOM 5023 C CD2 . PHE D 3 83  ? 134.384 151.119 190.657 1.00 140.08 ? 84   PHE D CD2 1 
ATOM 5024 C CE1 . PHE D 3 83  ? 136.327 152.815 189.682 1.00 139.72 ? 84   PHE D CE1 1 
ATOM 5025 C CE2 . PHE D 3 83  ? 134.036 152.154 189.812 1.00 140.97 ? 84   PHE D CE2 1 
ATOM 5026 C CZ  . PHE D 3 83  ? 135.009 153.003 189.325 1.00 141.68 ? 84   PHE D CZ  1 
ATOM 5027 N N   . ALA D 3 84  ? 137.774 146.510 191.573 1.00 131.11 ? 85   ALA D N   1 
ATOM 5028 C CA  . ALA D 3 84  ? 138.389 145.420 192.316 1.00 124.42 ? 85   ALA D CA  1 
ATOM 5029 C C   . ALA D 3 84  ? 139.752 145.140 191.693 1.00 123.03 ? 85   ALA D C   1 
ATOM 5030 O O   . ALA D 3 84  ? 140.223 145.889 190.832 1.00 124.54 ? 85   ALA D O   1 
ATOM 5031 C CB  . ALA D 3 84  ? 137.480 144.185 192.318 1.00 119.06 ? 85   ALA D CB  1 
ATOM 5032 N N   . THR D 3 85  ? 140.390 144.057 192.125 1.00 119.80 ? 86   THR D N   1 
ATOM 5033 C CA  . THR D 3 85  ? 141.691 143.676 191.598 1.00 113.02 ? 86   THR D CA  1 
ATOM 5034 C C   . THR D 3 85  ? 141.519 142.629 190.505 1.00 109.16 ? 86   THR D C   1 
ATOM 5035 O O   . THR D 3 85  ? 140.594 141.817 190.541 1.00 107.14 ? 86   THR D O   1 
ATOM 5036 C CB  . THR D 3 85  ? 142.597 143.136 192.706 1.00 112.26 ? 86   THR D CB  1 
ATOM 5037 O OG1 . THR D 3 85  ? 142.363 143.870 193.913 1.00 113.45 ? 86   THR D OG1 1 
ATOM 5038 C CG2 . THR D 3 85  ? 144.058 143.292 192.317 1.00 108.86 ? 86   THR D CG2 1 
ATOM 5039 N N   . TYR D 3 86  ? 142.410 142.662 189.518 1.00 106.67 ? 87   TYR D N   1 
ATOM 5040 C CA  . TYR D 3 86  ? 142.339 141.763 188.375 1.00 98.84  ? 87   TYR D CA  1 
ATOM 5041 C C   . TYR D 3 86  ? 143.641 140.988 188.246 1.00 94.45  ? 87   TYR D C   1 
ATOM 5042 O O   . TYR D 3 86  ? 144.726 141.573 188.319 1.00 93.11  ? 87   TYR D O   1 
ATOM 5043 C CB  . TYR D 3 86  ? 142.044 142.537 187.090 1.00 100.42 ? 87   TYR D CB  1 
ATOM 5044 C CG  . TYR D 3 86  ? 140.622 143.036 187.022 1.00 106.42 ? 87   TYR D CG  1 
ATOM 5045 C CD1 . TYR D 3 86  ? 139.595 142.196 186.622 1.00 105.86 ? 87   TYR D CD1 1 
ATOM 5046 C CD2 . TYR D 3 86  ? 140.303 144.341 187.369 1.00 111.16 ? 87   TYR D CD2 1 
ATOM 5047 C CE1 . TYR D 3 86  ? 138.293 142.641 186.563 1.00 109.29 ? 87   TYR D CE1 1 
ATOM 5048 C CE2 . TYR D 3 86  ? 139.001 144.795 187.312 1.00 114.77 ? 87   TYR D CE2 1 
ATOM 5049 C CZ  . TYR D 3 86  ? 138.000 143.940 186.908 1.00 114.48 ? 87   TYR D CZ  1 
ATOM 5050 O OH  . TYR D 3 86  ? 136.700 144.380 186.846 1.00 114.70 ? 87   TYR D OH  1 
ATOM 5051 N N   . TYR D 3 87  ? 143.526 139.675 188.050 1.00 89.40  ? 88   TYR D N   1 
ATOM 5052 C CA  . TYR D 3 87  ? 144.682 138.795 187.957 1.00 81.61  ? 88   TYR D CA  1 
ATOM 5053 C C   . TYR D 3 87  ? 144.640 137.998 186.663 1.00 71.94  ? 88   TYR D C   1 
ATOM 5054 O O   . TYR D 3 87  ? 143.579 137.520 186.249 1.00 67.70  ? 88   TYR D O   1 
ATOM 5055 C CB  . TYR D 3 87  ? 144.746 137.829 189.142 1.00 79.05  ? 88   TYR D CB  1 
ATOM 5056 C CG  . TYR D 3 87  ? 145.006 138.491 190.472 1.00 87.40  ? 88   TYR D CG  1 
ATOM 5057 C CD1 . TYR D 3 87  ? 146.301 138.747 190.899 1.00 88.27  ? 88   TYR D CD1 1 
ATOM 5058 C CD2 . TYR D 3 87  ? 143.958 138.847 191.308 1.00 91.56  ? 88   TYR D CD2 1 
ATOM 5059 C CE1 . TYR D 3 87  ? 146.544 139.347 192.116 1.00 92.48  ? 88   TYR D CE1 1 
ATOM 5060 C CE2 . TYR D 3 87  ? 144.192 139.447 192.528 1.00 94.67  ? 88   TYR D CE2 1 
ATOM 5061 C CZ  . TYR D 3 87  ? 145.486 139.695 192.927 1.00 94.31  ? 88   TYR D CZ  1 
ATOM 5062 O OH  . TYR D 3 87  ? 145.724 140.292 194.141 1.00 97.55  ? 88   TYR D OH  1 
ATOM 5063 N N   . CYS D 3 88  ? 145.804 137.861 186.031 1.00 65.98  ? 89   CYS D N   1 
ATOM 5064 C CA  . CYS D 3 88  ? 145.999 136.951 184.912 1.00 56.93  ? 89   CYS D CA  1 
ATOM 5065 C C   . CYS D 3 88  ? 146.734 135.720 185.413 1.00 50.85  ? 89   CYS D C   1 
ATOM 5066 O O   . CYS D 3 88  ? 147.799 135.835 186.028 1.00 56.40  ? 89   CYS D O   1 
ATOM 5067 C CB  . CYS D 3 88  ? 146.792 137.607 183.780 1.00 62.59  ? 89   CYS D CB  1 
ATOM 5068 S SG  . CYS D 3 88  ? 148.315 138.433 184.300 1.00 87.70  ? 89   CYS D SG  1 
ATOM 5069 N N   . GLN D 3 89  ? 146.164 134.549 185.159 1.00 41.07  ? 90   GLN D N   1 
ATOM 5070 C CA  . GLN D 3 89  ? 146.741 133.283 185.582 1.00 36.35  ? 90   GLN D CA  1 
ATOM 5071 C C   . GLN D 3 89  ? 147.096 132.473 184.351 1.00 31.83  ? 90   GLN D C   1 
ATOM 5072 O O   . GLN D 3 89  ? 146.219 132.145 183.550 1.00 36.93  ? 90   GLN D O   1 
ATOM 5073 C CB  . GLN D 3 89  ? 145.769 132.501 186.460 1.00 36.25  ? 90   GLN D CB  1 
ATOM 5074 C CG  . GLN D 3 89  ? 146.208 131.088 186.749 1.00 29.03  ? 90   GLN D CG  1 
ATOM 5075 C CD  . GLN D 3 89  ? 145.050 130.129 186.793 1.00 30.91  ? 90   GLN D CD  1 
ATOM 5076 O OE1 . GLN D 3 89  ? 143.982 130.407 186.262 1.00 35.04  ? 90   GLN D OE1 1 
ATOM 5077 N NE2 . GLN D 3 89  ? 145.252 128.989 187.425 1.00 30.14  ? 90   GLN D NE2 1 
ATOM 5078 N N   . GLN D 3 90  ? 148.372 132.159 184.199 1.00 29.39  ? 91   GLN D N   1 
ATOM 5079 C CA  . GLN D 3 90  ? 148.783 131.163 183.226 1.00 26.01  ? 91   GLN D CA  1 
ATOM 5080 C C   . GLN D 3 90  ? 148.559 129.791 183.835 1.00 27.94  ? 91   GLN D C   1 
ATOM 5081 O O   . GLN D 3 90  ? 149.125 129.474 184.890 1.00 34.70  ? 91   GLN D O   1 
ATOM 5082 C CB  . GLN D 3 90  ? 150.242 131.357 182.835 1.00 26.47  ? 91   GLN D CB  1 
ATOM 5083 C CG  . GLN D 3 90  ? 150.917 130.111 182.333 1.00 25.63  ? 91   GLN D CG  1 
ATOM 5084 C CD  . GLN D 3 90  ? 151.715 129.432 183.408 1.00 27.07  ? 91   GLN D CD  1 
ATOM 5085 O OE1 . GLN D 3 90  ? 151.932 129.996 184.471 1.00 30.55  ? 91   GLN D OE1 1 
ATOM 5086 N NE2 . GLN D 3 90  ? 152.150 128.211 183.146 1.00 29.23  ? 91   GLN D NE2 1 
ATOM 5087 N N   . TYR D 3 91  ? 147.715 128.993 183.185 1.00 24.19  ? 92   TYR D N   1 
ATOM 5088 C CA  . TYR D 3 91  ? 147.365 127.671 183.676 1.00 22.20  ? 92   TYR D CA  1 
ATOM 5089 C C   . TYR D 3 91  ? 147.724 126.606 182.650 1.00 19.34  ? 92   TYR D C   1 
ATOM 5090 O O   . TYR D 3 91  ? 146.939 125.694 182.393 1.00 21.88  ? 92   TYR D O   1 
ATOM 5091 C CB  . TYR D 3 91  ? 145.877 127.614 184.044 1.00 21.77  ? 92   TYR D CB  1 
ATOM 5092 C CG  . TYR D 3 91  ? 144.885 127.896 182.931 1.00 21.05  ? 92   TYR D CG  1 
ATOM 5093 C CD1 . TYR D 3 91  ? 144.526 129.187 182.602 1.00 24.25  ? 92   TYR D CD1 1 
ATOM 5094 C CD2 . TYR D 3 91  ? 144.267 126.866 182.251 1.00 21.02  ? 92   TYR D CD2 1 
ATOM 5095 C CE1 . TYR D 3 91  ? 143.611 129.436 181.609 1.00 22.58  ? 92   TYR D CE1 1 
ATOM 5096 C CE2 . TYR D 3 91  ? 143.360 127.109 181.263 1.00 20.19  ? 92   TYR D CE2 1 
ATOM 5097 C CZ  . TYR D 3 91  ? 143.036 128.390 180.945 1.00 21.61  ? 92   TYR D CZ  1 
ATOM 5098 O OH  . TYR D 3 91  ? 142.125 128.618 179.950 1.00 29.65  ? 92   TYR D OH  1 
ATOM 5099 N N   . LEU D 3 92  ? 148.922 126.704 182.075 1.00 19.00  ? 93   LEU D N   1 
ATOM 5100 C CA  . LEU D 3 92  ? 149.319 125.779 181.020 1.00 19.09  ? 93   LEU D CA  1 
ATOM 5101 C C   . LEU D 3 92  ? 149.278 124.334 181.497 1.00 19.04  ? 93   LEU D C   1 
ATOM 5102 O O   . LEU D 3 92  ? 148.909 123.434 180.738 1.00 24.05  ? 93   LEU D O   1 
ATOM 5103 C CB  . LEU D 3 92  ? 150.715 126.131 180.517 1.00 22.19  ? 93   LEU D CB  1 
ATOM 5104 C CG  . LEU D 3 92  ? 151.236 125.267 179.376 1.00 21.08  ? 93   LEU D CG  1 
ATOM 5105 C CD1 . LEU D 3 92  ? 150.416 125.493 178.135 1.00 20.26  ? 93   LEU D CD1 1 
ATOM 5106 C CD2 . LEU D 3 92  ? 152.683 125.571 179.115 1.00 26.00  ? 93   LEU D CD2 1 
ATOM 5107 N N   . TYR D 3 93  ? 149.656 124.091 182.746 1.00 16.90  ? 94   TYR D N   1 
ATOM 5108 C CA  . TYR D 3 93  ? 149.616 122.752 183.307 1.00 17.06  ? 94   TYR D CA  1 
ATOM 5109 C C   . TYR D 3 93  ? 149.302 122.876 184.788 1.00 19.04  ? 94   TYR D C   1 
ATOM 5110 O O   . TYR D 3 93  ? 149.432 123.948 185.378 1.00 22.39  ? 94   TYR D O   1 
ATOM 5111 C CB  . TYR D 3 93  ? 150.931 121.996 183.061 1.00 18.07  ? 94   TYR D CB  1 
ATOM 5112 C CG  . TYR D 3 93  ? 150.975 120.621 183.682 1.00 17.49  ? 94   TYR D CG  1 
ATOM 5113 C CD1 . TYR D 3 93  ? 150.133 119.618 183.245 1.00 18.73  ? 94   TYR D CD1 1 
ATOM 5114 C CD2 . TYR D 3 93  ? 151.848 120.334 184.713 1.00 20.79  ? 94   TYR D CD2 1 
ATOM 5115 C CE1 . TYR D 3 93  ? 150.160 118.374 183.815 1.00 19.26  ? 94   TYR D CE1 1 
ATOM 5116 C CE2 . TYR D 3 93  ? 151.879 119.093 185.289 1.00 22.66  ? 94   TYR D CE2 1 
ATOM 5117 C CZ  . TYR D 3 93  ? 151.033 118.119 184.835 1.00 20.78  ? 94   TYR D CZ  1 
ATOM 5118 O OH  . TYR D 3 93  ? 151.060 116.876 185.405 1.00 28.50  ? 94   TYR D OH  1 
ATOM 5119 N N   . TYR D 3 94  ? 148.874 121.764 185.383 1.00 18.93  ? 95   TYR D N   1 
ATOM 5120 C CA  . TYR D 3 94  ? 148.375 121.793 186.753 1.00 19.72  ? 95   TYR D CA  1 
ATOM 5121 C C   . TYR D 3 94  ? 149.427 122.303 187.726 1.00 21.06  ? 95   TYR D C   1 
ATOM 5122 O O   . TYR D 3 94  ? 149.118 123.099 188.616 1.00 28.66  ? 95   TYR D O   1 
ATOM 5123 C CB  . TYR D 3 94  ? 147.896 120.403 187.161 1.00 23.71  ? 95   TYR D CB  1 
ATOM 5124 C CG  . TYR D 3 94  ? 146.579 120.013 186.539 1.00 22.61  ? 95   TYR D CG  1 
ATOM 5125 C CD1 . TYR D 3 94  ? 146.472 119.788 185.184 1.00 21.22  ? 95   TYR D CD1 1 
ATOM 5126 C CD2 . TYR D 3 94  ? 145.446 119.870 187.310 1.00 24.43  ? 95   TYR D CD2 1 
ATOM 5127 C CE1 . TYR D 3 94  ? 145.277 119.439 184.619 1.00 20.89  ? 95   TYR D CE1 1 
ATOM 5128 C CE2 . TYR D 3 94  ? 144.253 119.521 186.752 1.00 21.72  ? 95   TYR D CE2 1 
ATOM 5129 C CZ  . TYR D 3 94  ? 144.170 119.306 185.412 1.00 22.68  ? 95   TYR D CZ  1 
ATOM 5130 O OH  . TYR D 3 94  ? 142.964 118.955 184.861 1.00 33.54  ? 95   TYR D OH  1 
ATOM 5131 N N   . SER D 3 95  ? 150.669 121.868 187.577 1.00 19.76  ? 96   SER D N   1 
ATOM 5132 C CA  . SER D 3 95  ? 151.741 122.284 188.469 1.00 22.27  ? 96   SER D CA  1 
ATOM 5133 C C   . SER D 3 95  ? 152.479 123.518 187.973 1.00 26.22  ? 96   SER D C   1 
ATOM 5134 O O   . SER D 3 95  ? 153.489 123.899 188.569 1.00 35.93  ? 96   SER D O   1 
ATOM 5135 C CB  . SER D 3 95  ? 152.733 121.140 188.672 1.00 24.97  ? 96   SER D CB  1 
ATOM 5136 O OG  . SER D 3 95  ? 153.423 120.844 187.472 1.00 28.81  ? 96   SER D OG  1 
ATOM 5137 N N   . LEU D 3 96  ? 152.009 124.141 186.895 1.00 22.44  ? 97   LEU D N   1 
ATOM 5138 C CA  . LEU D 3 96  ? 152.671 125.287 186.286 1.00 20.96  ? 97   LEU D CA  1 
ATOM 5139 C C   . LEU D 3 96  ? 151.830 126.552 186.393 1.00 26.02  ? 97   LEU D C   1 
ATOM 5140 O O   . LEU D 3 96  ? 151.967 127.461 185.576 1.00 27.83  ? 97   LEU D O   1 
ATOM 5141 C CB  . LEU D 3 96  ? 152.990 125.008 184.818 1.00 19.32  ? 97   LEU D CB  1 
ATOM 5142 C CG  . LEU D 3 96  ? 154.281 124.310 184.402 1.00 22.51  ? 97   LEU D CG  1 
ATOM 5143 C CD1 . LEU D 3 96  ? 154.587 123.111 185.265 1.00 20.87  ? 97   LEU D CD1 1 
ATOM 5144 C CD2 . LEU D 3 96  ? 154.152 123.885 182.962 1.00 24.05  ? 97   LEU D CD2 1 
ATOM 5145 N N   . VAL D 3 97  ? 150.951 126.620 187.386 1.00 24.98  ? 98   VAL D N   1 
ATOM 5146 C CA  . VAL D 3 97  ? 150.015 127.731 187.508 1.00 22.00  ? 98   VAL D CA  1 
ATOM 5147 C C   . VAL D 3 97  ? 150.739 128.933 188.095 1.00 28.27  ? 98   VAL D C   1 
ATOM 5148 O O   . VAL D 3 97  ? 151.339 128.841 189.170 1.00 35.37  ? 98   VAL D O   1 
ATOM 5149 C CB  . VAL D 3 97  ? 148.815 127.341 188.375 1.00 22.61  ? 98   VAL D CB  1 
ATOM 5150 C CG1 . VAL D 3 97  ? 148.104 128.575 188.851 1.00 31.02  ? 98   VAL D CG1 1 
ATOM 5151 C CG2 . VAL D 3 97  ? 147.879 126.467 187.591 1.00 24.89  ? 98   VAL D CG2 1 
ATOM 5152 N N   . THR D 3 98  ? 150.684 130.065 187.396 1.00 29.46  ? 99   THR D N   1 
ATOM 5153 C CA  . THR D 3 98  ? 151.307 131.289 187.897 1.00 28.14  ? 99   THR D CA  1 
ATOM 5154 C C   . THR D 3 98  ? 150.376 132.466 187.684 1.00 33.48  ? 99   THR D C   1 
ATOM 5155 O O   . THR D 3 98  ? 149.961 132.733 186.555 1.00 36.77  ? 99   THR D O   1 
ATOM 5156 C CB  . THR D 3 98  ? 152.648 131.567 187.220 1.00 32.02  ? 99   THR D CB  1 
ATOM 5157 O OG1 . THR D 3 98  ? 152.473 131.577 185.802 1.00 38.07  ? 99   THR D OG1 1 
ATOM 5158 C CG2 . THR D 3 98  ? 153.673 130.520 187.604 1.00 35.99  ? 99   THR D CG2 1 
ATOM 5159 N N   . PHE D 3 99  ? 150.078 133.181 188.760 1.00 37.26  ? 100  PHE D N   1 
ATOM 5160 C CA  . PHE D 3 99  ? 149.227 134.356 188.708 1.00 42.45  ? 100  PHE D CA  1 
ATOM 5161 C C   . PHE D 3 99  ? 150.061 135.609 188.469 1.00 51.87  ? 100  PHE D C   1 
ATOM 5162 O O   . PHE D 3 99  ? 151.270 135.638 188.708 1.00 58.09  ? 100  PHE D O   1 
ATOM 5163 C CB  . PHE D 3 99  ? 148.433 134.500 190.005 1.00 47.81  ? 100  PHE D CB  1 
ATOM 5164 C CG  . PHE D 3 99  ? 147.482 133.371 190.268 1.00 44.79  ? 100  PHE D CG  1 
ATOM 5165 C CD1 . PHE D 3 99  ? 147.926 132.193 190.834 1.00 45.19  ? 100  PHE D CD1 1 
ATOM 5166 C CD2 . PHE D 3 99  ? 146.142 133.497 189.967 1.00 42.31  ? 100  PHE D CD2 1 
ATOM 5167 C CE1 . PHE D 3 99  ? 147.054 131.158 191.080 1.00 41.82  ? 100  PHE D CE1 1 
ATOM 5168 C CE2 . PHE D 3 99  ? 145.268 132.464 190.214 1.00 39.65  ? 100  PHE D CE2 1 
ATOM 5169 C CZ  . PHE D 3 99  ? 145.726 131.294 190.772 1.00 39.58  ? 100  PHE D CZ  1 
ATOM 5170 N N   . GLY D 3 100 ? 149.394 136.656 187.995 1.00 59.31  ? 101  GLY D N   1 
ATOM 5171 C CA  . GLY D 3 100 ? 150.053 137.928 187.803 1.00 69.43  ? 101  GLY D CA  1 
ATOM 5172 C C   . GLY D 3 100 ? 150.169 138.724 189.092 1.00 79.45  ? 101  GLY D C   1 
ATOM 5173 O O   . GLY D 3 100 ? 149.644 138.352 190.141 1.00 78.58  ? 101  GLY D O   1 
ATOM 5174 N N   . GLN D 3 101 ? 150.881 139.849 188.997 1.00 87.95  ? 102  GLN D N   1 
ATOM 5175 C CA  . GLN D 3 101 ? 151.090 140.695 190.169 1.00 90.03  ? 102  GLN D CA  1 
ATOM 5176 C C   . GLN D 3 101 ? 149.789 141.332 190.638 1.00 91.53  ? 102  GLN D C   1 
ATOM 5177 O O   . GLN D 3 101 ? 149.549 141.448 191.845 1.00 92.73  ? 102  GLN D O   1 
ATOM 5178 C CB  . GLN D 3 101 ? 152.135 141.768 189.866 1.00 89.56  ? 102  GLN D CB  1 
ATOM 5179 C CG  . GLN D 3 101 ? 153.570 141.261 189.863 1.00 88.72  ? 102  GLN D CG  1 
ATOM 5180 C CD  . GLN D 3 101 ? 153.869 140.343 188.695 1.00 88.32  ? 102  GLN D CD  1 
ATOM 5181 O OE1 . GLN D 3 101 ? 153.162 140.352 187.687 1.00 92.16  ? 102  GLN D OE1 1 
ATOM 5182 N NE2 . GLN D 3 101 ? 154.919 139.541 188.827 1.00 84.62  ? 102  GLN D NE2 1 
ATOM 5183 N N   . GLY D 3 102 ? 148.941 141.758 189.707 1.00 92.67  ? 103  GLY D N   1 
ATOM 5184 C CA  . GLY D 3 102 ? 147.664 142.336 190.071 1.00 97.41  ? 103  GLY D CA  1 
ATOM 5185 C C   . GLY D 3 102 ? 147.424 143.713 189.488 1.00 104.50 ? 103  GLY D C   1 
ATOM 5186 O O   . GLY D 3 102 ? 148.368 144.416 189.116 1.00 105.97 ? 103  GLY D O   1 
ATOM 5187 N N   . THR D 3 103 ? 146.155 144.106 189.404 1.00 106.42 ? 104  THR D N   1 
ATOM 5188 C CA  . THR D 3 103 ? 145.779 145.421 188.893 1.00 112.60 ? 104  THR D CA  1 
ATOM 5189 C C   . THR D 3 103 ? 144.426 145.785 189.478 1.00 117.20 ? 104  THR D C   1 
ATOM 5190 O O   . THR D 3 103 ? 143.431 145.107 189.205 1.00 116.76 ? 104  THR D O   1 
ATOM 5191 C CB  . THR D 3 103 ? 145.726 145.432 187.365 1.00 111.04 ? 104  THR D CB  1 
ATOM 5192 O OG1 . THR D 3 103 ? 147.059 145.402 186.840 1.00 110.21 ? 104  THR D OG1 1 
ATOM 5193 C CG2 . THR D 3 103 ? 145.014 146.677 186.863 1.00 113.62 ? 104  THR D CG2 1 
ATOM 5194 N N   . LYS D 3 104 ? 144.390 146.846 190.277 1.00 121.11 ? 105  LYS D N   1 
ATOM 5195 C CA  . LYS D 3 104 ? 143.175 147.269 190.959 1.00 122.12 ? 105  LYS D CA  1 
ATOM 5196 C C   . LYS D 3 104 ? 142.610 148.512 190.286 1.00 127.88 ? 105  LYS D C   1 
ATOM 5197 O O   . LYS D 3 104 ? 143.349 149.455 189.985 1.00 129.18 ? 105  LYS D O   1 
ATOM 5198 C CB  . LYS D 3 104 ? 143.448 147.534 192.440 1.00 121.25 ? 105  LYS D CB  1 
ATOM 5199 C CG  . LYS D 3 104 ? 144.622 148.456 192.713 1.00 124.21 ? 105  LYS D CG  1 
ATOM 5200 C CD  . LYS D 3 104 ? 145.196 148.204 194.097 1.00 123.92 ? 105  LYS D CD  1 
ATOM 5201 C CE  . LYS D 3 104 ? 144.110 148.221 195.161 1.00 124.67 ? 105  LYS D CE  1 
ATOM 5202 N NZ  . LYS D 3 104 ? 144.635 147.802 196.489 1.00 123.83 ? 105  LYS D NZ  1 
ATOM 5203 N N   . VAL D 3 105 ? 141.304 148.502 190.043 1.00 130.97 ? 106  VAL D N   1 
ATOM 5204 C CA  . VAL D 3 105 ? 140.619 149.620 189.406 1.00 134.83 ? 106  VAL D CA  1 
ATOM 5205 C C   . VAL D 3 105 ? 140.145 150.572 190.495 1.00 137.82 ? 106  VAL D C   1 
ATOM 5206 O O   . VAL D 3 105 ? 139.402 150.176 191.399 1.00 136.60 ? 106  VAL D O   1 
ATOM 5207 C CB  . VAL D 3 105 ? 139.444 149.135 188.545 1.00 132.30 ? 106  VAL D CB  1 
ATOM 5208 C CG1 . VAL D 3 105 ? 138.707 150.316 187.942 1.00 136.40 ? 106  VAL D CG1 1 
ATOM 5209 C CG2 . VAL D 3 105 ? 139.941 148.205 187.455 1.00 127.46 ? 106  VAL D CG2 1 
ATOM 5210 N N   . GLU D 3 106 ? 140.576 151.826 190.409 1.00 139.51 ? 107  GLU D N   1 
ATOM 5211 C CA  . GLU D 3 106 ? 140.241 152.843 191.390 1.00 140.21 ? 107  GLU D CA  1 
ATOM 5212 C C   . GLU D 3 106 ? 139.385 153.921 190.742 1.00 143.52 ? 107  GLU D C   1 
ATOM 5213 O O   . GLU D 3 106 ? 139.299 154.024 189.515 1.00 143.19 ? 107  GLU D O   1 
ATOM 5214 C CB  . GLU D 3 106 ? 141.507 153.462 191.994 1.00 140.60 ? 107  GLU D CB  1 
ATOM 5215 C CG  . GLU D 3 106 ? 142.448 152.444 192.613 1.00 139.86 ? 107  GLU D CG  1 
ATOM 5216 C CD  . GLU D 3 106 ? 143.748 153.061 193.083 1.00 139.92 ? 107  GLU D CD  1 
ATOM 5217 O OE1 . GLU D 3 106 ? 143.941 154.276 192.875 1.00 140.93 ? 107  GLU D OE1 1 
ATOM 5218 O OE2 . GLU D 3 106 ? 144.579 152.329 193.661 1.00 137.44 ? 107  GLU D OE2 1 
ATOM 5219 N N   . ILE D 3 107 ? 138.745 154.726 191.583 1.00 144.76 ? 108  ILE D N   1 
ATOM 5220 C CA  . ILE D 3 107 ? 137.878 155.802 191.120 1.00 145.66 ? 108  ILE D CA  1 
ATOM 5221 C C   . ILE D 3 107 ? 138.741 157.024 190.834 1.00 146.06 ? 108  ILE D C   1 
ATOM 5222 O O   . ILE D 3 107 ? 139.432 157.530 191.725 1.00 145.82 ? 108  ILE D O   1 
ATOM 5223 C CB  . ILE D 3 107 ? 136.788 156.123 192.152 1.00 145.55 ? 108  ILE D CB  1 
ATOM 5224 C CG1 . ILE D 3 107 ? 136.063 154.842 192.570 1.00 142.13 ? 108  ILE D CG1 1 
ATOM 5225 C CG2 . ILE D 3 107 ? 135.801 157.128 191.584 1.00 143.91 ? 108  ILE D CG2 1 
ATOM 5226 C CD1 . ILE D 3 107 ? 134.975 155.061 193.595 1.00 139.26 ? 108  ILE D CD1 1 
ATOM 5227 N N   . LYS D 3 108 ? 138.706 157.495 189.591 1.00 147.02 ? 109  LYS D N   1 
ATOM 5228 C CA  . LYS D 3 108 ? 139.506 158.641 189.186 1.00 146.96 ? 109  LYS D CA  1 
ATOM 5229 C C   . LYS D 3 108 ? 138.889 159.926 189.722 1.00 148.62 ? 109  LYS D C   1 
ATOM 5230 O O   . LYS D 3 108 ? 137.677 160.137 189.611 1.00 148.96 ? 109  LYS D O   1 
ATOM 5231 C CB  . LYS D 3 108 ? 139.621 158.700 187.664 1.00 144.16 ? 109  LYS D CB  1 
ATOM 5232 C CG  . LYS D 3 108 ? 140.587 159.753 187.152 1.00 140.61 ? 109  LYS D CG  1 
ATOM 5233 C CD  . LYS D 3 108 ? 140.693 159.706 185.637 1.00 137.29 ? 109  LYS D CD  1 
ATOM 5234 C CE  . LYS D 3 108 ? 141.713 160.706 185.121 1.00 131.40 ? 109  LYS D CE  1 
ATOM 5235 N NZ  . LYS D 3 108 ? 141.826 160.665 183.638 1.00 126.22 ? 109  LYS D NZ  1 
ATOM 5236 N N   . ARG D 3 109 ? 139.723 160.782 190.302 1.00 149.34 ? 110  ARG D N   1 
ATOM 5237 C CA  . ARG D 3 109 ? 139.258 162.051 190.847 1.00 149.76 ? 110  ARG D CA  1 
ATOM 5238 C C   . ARG D 3 109 ? 140.089 163.212 190.315 1.00 148.08 ? 110  ARG D C   1 
ATOM 5239 O O   . ARG D 3 109 ? 140.646 163.138 189.220 1.00 146.28 ? 110  ARG D O   1 
ATOM 5240 C CB  . ARG D 3 109 ? 139.305 162.027 192.375 1.00 149.74 ? 110  ARG D CB  1 
ATOM 5241 C CG  . ARG D 3 109 ? 138.770 163.291 193.025 1.00 150.86 ? 110  ARG D CG  1 
ATOM 5242 C CD  . ARG D 3 109 ? 138.841 163.206 194.539 1.00 152.26 ? 110  ARG D CD  1 
ATOM 5243 N NE  . ARG D 3 109 ? 138.225 164.364 195.175 1.00 157.31 ? 110  ARG D NE  1 
ATOM 5244 C CZ  . ARG D 3 109 ? 136.941 164.448 195.491 1.00 158.17 ? 110  ARG D CZ  1 
ATOM 5245 N NH1 . ARG D 3 109 ? 136.101 163.456 195.243 1.00 156.53 ? 110  ARG D NH1 1 
ATOM 5246 N NH2 . ARG D 3 109 ? 136.486 165.555 196.071 1.00 156.41 ? 110  ARG D NH2 1 
# 
