data_9GNQ
# 
_entry.id   9GNQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9GNQ         pdb_00009gnq 10.2210/pdb9gnq/pdb 
WWPDB D_1292141499 ?            ?                   
EMDB  EMD-51477    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GNQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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  .                                                           8RHB      unspecified            
PDB  .                                                           8RHH      unspecified            
PDB  .                                                           8RIK      unspecified            
PDB  .                                                           8RIZ      unspecified            
EMDB 'Microtubule-associated Kif5B IAK tail mutant bound to ADP' EMD-51477 'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
3 roberto.steiner@kcl.ac.uk Steiner Roberto  ? 'principal investigator/group leader' 0000-0001-7084-9745 
4 joseph.atherton@kcl.ac.uk Joseph  Atherton ? 'principal investigator/group leader' 0000-0002-6362-2347 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Atherton, J.'   1 0000-0002-6362-2347 
'Chegkazi, M.S.' 2 0000-0002-0855-2681 
'Steiner, R.A.'  3 0000-0001-7084-9745 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.11.11.622991 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Atherton, J.'   1 ? 
primary 'Chegkazi, M.S.' 2 ? 
primary 'Peirano, E.'    3 ? 
primary 'Pozzer, L.S.'   4 ? 
primary 'Foran, T.'      5 ? 
primary 'Steiner, R.A.'  6 ? 
# 
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     nat 'Tubulin beta chain'        49907.770 1 ? ? ? Beta-tubulin  
2 polymer     nat 'Tubulin alpha-1B chain'    50204.445 1 ? ? ? Alpha-tubulin 
3 polymer     man 'Kinesin-1 heavy chain'     44772.059 1 ? ? ? ?             
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"  443.201   1 ? ? ? ?             
5 non-polymer syn TAXOL                       853.906   1 ? ? ? ?             
6 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE" 523.180   1 ? ? ? ?             
7 non-polymer syn 'MAGNESIUM ION'             24.305    1 ? ? ? ?             
8 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"  427.201   1 ? ? ? ?             
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 Beta-tubulin                                                                
2 'Alpha-tubulin ubiquitous,Tubulin K-alpha-1,Tubulin alpha-ubiquitous chain' 
3 'Conventional kinesin heavy chain,Ubiquitous kinesin heavy chain,UKHC'      
# 
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 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
B ? 
2 'polypeptide(L)' no no 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
A ? 
3 'polypeptide(L)' no no 
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTTGSTGSTGSTGSTGSTGSTGSTGSTGSARRGHSATGSTSGTPG
QHPAASPT
;
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNTTGSTGSTGSTGSTGSTGSTGSTGSTGSARRGHSATGSTSGTPG
QHPAASPT
;
K ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "GUANOSINE-5'-DIPHOSPHATE"  GDP 
5 TAXOL                       TA1 
6 "GUANOSINE-5'-TRIPHOSPHATE" GTP 
7 'MAGNESIUM ION'             MG  
8 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   GLU n 
1 4   ILE n 
1 5   VAL n 
1 6   HIS n 
1 7   ILE n 
1 8   GLN n 
1 9   ALA n 
1 10  GLY n 
1 11  GLN n 
1 12  CYS n 
1 13  GLY n 
1 14  ASN n 
1 15  GLN n 
1 16  ILE n 
1 17  GLY n 
1 18  ALA n 
1 19  LYS n 
1 20  PHE n 
1 21  TRP n 
1 22  GLU n 
1 23  VAL n 
1 24  ILE n 
1 25  SER n 
1 26  ASP n 
1 27  GLU n 
1 28  HIS n 
1 29  GLY n 
1 30  ILE n 
1 31  ASP n 
1 32  PRO n 
1 33  THR n 
1 34  GLY n 
1 35  SER n 
1 36  TYR n 
1 37  HIS n 
1 38  GLY n 
1 39  ASP n 
1 40  SER n 
1 41  ASP n 
1 42  LEU n 
1 43  GLN n 
1 44  LEU n 
1 45  GLU n 
1 46  ARG n 
1 47  ILE n 
1 48  ASN n 
1 49  VAL n 
1 50  TYR n 
1 51  TYR n 
1 52  ASN n 
1 53  GLU n 
1 54  ALA n 
1 55  ALA n 
1 56  GLY n 
1 57  ASN n 
1 58  LYS n 
1 59  TYR n 
1 60  VAL n 
1 61  PRO n 
1 62  ARG n 
1 63  ALA n 
1 64  ILE n 
1 65  LEU n 
1 66  VAL n 
1 67  ASP n 
1 68  LEU n 
1 69  GLU n 
1 70  PRO n 
1 71  GLY n 
1 72  THR n 
1 73  MET n 
1 74  ASP n 
1 75  SER n 
1 76  VAL n 
1 77  ARG n 
1 78  SER n 
1 79  GLY n 
1 80  PRO n 
1 81  PHE n 
1 82  GLY n 
1 83  GLN n 
1 84  ILE n 
1 85  PHE n 
1 86  ARG n 
1 87  PRO n 
1 88  ASP n 
1 89  ASN n 
1 90  PHE n 
1 91  VAL n 
1 92  PHE n 
1 93  GLY n 
1 94  GLN n 
1 95  SER n 
1 96  GLY n 
1 97  ALA n 
1 98  GLY n 
1 99  ASN n 
1 100 ASN n 
1 101 TRP n 
1 102 ALA n 
1 103 LYS n 
1 104 GLY n 
1 105 HIS n 
1 106 TYR n 
1 107 THR n 
1 108 GLU n 
1 109 GLY n 
1 110 ALA n 
1 111 GLU n 
1 112 LEU n 
1 113 VAL n 
1 114 ASP n 
1 115 SER n 
1 116 VAL n 
1 117 LEU n 
1 118 ASP n 
1 119 VAL n 
1 120 VAL n 
1 121 ARG n 
1 122 LYS n 
1 123 GLU n 
1 124 SER n 
1 125 GLU n 
1 126 SER n 
1 127 CYS n 
1 128 ASP n 
1 129 CYS n 
1 130 LEU n 
1 131 GLN n 
1 132 GLY n 
1 133 PHE n 
1 134 GLN n 
1 135 LEU n 
1 136 THR n 
1 137 HIS n 
1 138 SER n 
1 139 LEU n 
1 140 GLY n 
1 141 GLY n 
1 142 GLY n 
1 143 THR n 
1 144 GLY n 
1 145 SER n 
1 146 GLY n 
1 147 MET n 
1 148 GLY n 
1 149 THR n 
1 150 LEU n 
1 151 LEU n 
1 152 ILE n 
1 153 SER n 
1 154 LYS n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 GLU n 
1 159 TYR n 
1 160 PRO n 
1 161 ASP n 
1 162 ARG n 
1 163 ILE n 
1 164 MET n 
1 165 ASN n 
1 166 THR n 
1 167 PHE n 
1 168 SER n 
1 169 VAL n 
1 170 VAL n 
1 171 PRO n 
1 172 SER n 
1 173 PRO n 
1 174 LYS n 
1 175 VAL n 
1 176 SER n 
1 177 ASP n 
1 178 THR n 
1 179 VAL n 
1 180 VAL n 
1 181 GLU n 
1 182 PRO n 
1 183 TYR n 
1 184 ASN n 
1 185 ALA n 
1 186 THR n 
1 187 LEU n 
1 188 SER n 
1 189 VAL n 
1 190 HIS n 
1 191 GLN n 
1 192 LEU n 
1 193 VAL n 
1 194 GLU n 
1 195 ASN n 
1 196 THR n 
1 197 ASP n 
1 198 GLU n 
1 199 THR n 
1 200 TYR n 
1 201 CYS n 
1 202 ILE n 
1 203 ASP n 
1 204 ASN n 
1 205 GLU n 
1 206 ALA n 
1 207 LEU n 
1 208 TYR n 
1 209 ASP n 
1 210 ILE n 
1 211 CYS n 
1 212 PHE n 
1 213 ARG n 
1 214 THR n 
1 215 LEU n 
1 216 LYS n 
1 217 LEU n 
1 218 THR n 
1 219 THR n 
1 220 PRO n 
1 221 THR n 
1 222 TYR n 
1 223 GLY n 
1 224 ASP n 
1 225 LEU n 
1 226 ASN n 
1 227 HIS n 
1 228 LEU n 
1 229 VAL n 
1 230 SER n 
1 231 ALA n 
1 232 THR n 
1 233 MET n 
1 234 SER n 
1 235 GLY n 
1 236 VAL n 
1 237 THR n 
1 238 THR n 
1 239 CYS n 
1 240 LEU n 
1 241 ARG n 
1 242 PHE n 
1 243 PRO n 
1 244 GLY n 
1 245 GLN n 
1 246 LEU n 
1 247 ASN n 
1 248 ALA n 
1 249 ASP n 
1 250 LEU n 
1 251 ARG n 
1 252 LYS n 
1 253 LEU n 
1 254 ALA n 
1 255 VAL n 
1 256 ASN n 
1 257 MET n 
1 258 VAL n 
1 259 PRO n 
1 260 PHE n 
1 261 PRO n 
1 262 ARG n 
1 263 LEU n 
1 264 HIS n 
1 265 PHE n 
1 266 PHE n 
1 267 MET n 
1 268 PRO n 
1 269 GLY n 
1 270 PHE n 
1 271 ALA n 
1 272 PRO n 
1 273 LEU n 
1 274 THR n 
1 275 SER n 
1 276 ARG n 
1 277 GLY n 
1 278 SER n 
1 279 GLN n 
1 280 GLN n 
1 281 TYR n 
1 282 ARG n 
1 283 ALA n 
1 284 LEU n 
1 285 THR n 
1 286 VAL n 
1 287 PRO n 
1 288 GLU n 
1 289 LEU n 
1 290 THR n 
1 291 GLN n 
1 292 GLN n 
1 293 MET n 
1 294 PHE n 
1 295 ASP n 
1 296 ALA n 
1 297 LYS n 
1 298 ASN n 
1 299 MET n 
1 300 MET n 
1 301 ALA n 
1 302 ALA n 
1 303 CYS n 
1 304 ASP n 
1 305 PRO n 
1 306 ARG n 
1 307 HIS n 
1 308 GLY n 
1 309 ARG n 
1 310 TYR n 
1 311 LEU n 
1 312 THR n 
1 313 VAL n 
1 314 ALA n 
1 315 ALA n 
1 316 VAL n 
1 317 PHE n 
1 318 ARG n 
1 319 GLY n 
1 320 ARG n 
1 321 MET n 
1 322 SER n 
1 323 MET n 
1 324 LYS n 
1 325 GLU n 
1 326 VAL n 
1 327 ASP n 
1 328 GLU n 
1 329 GLN n 
1 330 MET n 
1 331 LEU n 
1 332 ASN n 
1 333 VAL n 
1 334 GLN n 
1 335 ASN n 
1 336 LYS n 
1 337 ASN n 
1 338 SER n 
1 339 SER n 
1 340 TYR n 
1 341 PHE n 
1 342 VAL n 
1 343 GLU n 
1 344 TRP n 
1 345 ILE n 
1 346 PRO n 
1 347 ASN n 
1 348 ASN n 
1 349 VAL n 
1 350 LYS n 
1 351 THR n 
1 352 ALA n 
1 353 VAL n 
1 354 CYS n 
1 355 ASP n 
1 356 ILE n 
1 357 PRO n 
1 358 PRO n 
1 359 ARG n 
1 360 GLY n 
1 361 LEU n 
1 362 LYS n 
1 363 MET n 
1 364 SER n 
1 365 ALA n 
1 366 THR n 
1 367 PHE n 
1 368 ILE n 
1 369 GLY n 
1 370 ASN n 
1 371 SER n 
1 372 THR n 
1 373 ALA n 
1 374 ILE n 
1 375 GLN n 
1 376 GLU n 
1 377 LEU n 
1 378 PHE n 
1 379 LYS n 
1 380 ARG n 
1 381 ILE n 
1 382 SER n 
1 383 GLU n 
1 384 GLN n 
1 385 PHE n 
1 386 THR n 
1 387 ALA n 
1 388 MET n 
1 389 PHE n 
1 390 ARG n 
1 391 ARG n 
1 392 LYS n 
1 393 ALA n 
1 394 PHE n 
1 395 LEU n 
1 396 HIS n 
1 397 TRP n 
1 398 TYR n 
1 399 THR n 
1 400 GLY n 
1 401 GLU n 
1 402 GLY n 
1 403 MET n 
1 404 ASP n 
1 405 GLU n 
1 406 MET n 
1 407 GLU n 
1 408 PHE n 
1 409 THR n 
1 410 GLU n 
1 411 ALA n 
1 412 GLU n 
1 413 SER n 
1 414 ASN n 
1 415 MET n 
1 416 ASN n 
1 417 ASP n 
1 418 LEU n 
1 419 VAL n 
1 420 SER n 
1 421 GLU n 
1 422 TYR n 
1 423 GLN n 
1 424 GLN n 
1 425 TYR n 
1 426 GLN n 
1 427 ASP n 
1 428 ALA n 
1 429 THR n 
1 430 ALA n 
1 431 ASP n 
1 432 GLU n 
1 433 GLN n 
1 434 GLY n 
1 435 GLU n 
1 436 PHE n 
1 437 GLU n 
1 438 GLU n 
1 439 GLU n 
1 440 GLY n 
1 441 GLU n 
1 442 GLU n 
1 443 ASP n 
1 444 GLU n 
1 445 ALA n 
2 1   MET n 
2 2   ARG n 
2 3   GLU n 
2 4   CYS n 
2 5   ILE n 
2 6   SER n 
2 7   ILE n 
2 8   HIS n 
2 9   VAL n 
2 10  GLY n 
2 11  GLN n 
2 12  ALA n 
2 13  GLY n 
2 14  VAL n 
2 15  GLN n 
2 16  ILE n 
2 17  GLY n 
2 18  ASN n 
2 19  ALA n 
2 20  CYS n 
2 21  TRP n 
2 22  GLU n 
2 23  LEU n 
2 24  TYR n 
2 25  CYS n 
2 26  LEU n 
2 27  GLU n 
2 28  HIS n 
2 29  GLY n 
2 30  ILE n 
2 31  GLN n 
2 32  PRO n 
2 33  ASP n 
2 34  GLY n 
2 35  GLN n 
2 36  MET n 
2 37  PRO n 
2 38  SER n 
2 39  ASP n 
2 40  LYS n 
2 41  THR n 
2 42  ILE n 
2 43  GLY n 
2 44  GLY n 
2 45  GLY n 
2 46  ASP n 
2 47  ASP n 
2 48  SER n 
2 49  PHE n 
2 50  ASN n 
2 51  THR n 
2 52  PHE n 
2 53  PHE n 
2 54  SER n 
2 55  GLU n 
2 56  THR n 
2 57  GLY n 
2 58  ALA n 
2 59  GLY n 
2 60  LYS n 
2 61  HIS n 
2 62  VAL n 
2 63  PRO n 
2 64  ARG n 
2 65  ALA n 
2 66  VAL n 
2 67  PHE n 
2 68  VAL n 
2 69  ASP n 
2 70  LEU n 
2 71  GLU n 
2 72  PRO n 
2 73  THR n 
2 74  VAL n 
2 75  ILE n 
2 76  ASP n 
2 77  GLU n 
2 78  VAL n 
2 79  ARG n 
2 80  THR n 
2 81  GLY n 
2 82  THR n 
2 83  TYR n 
2 84  ARG n 
2 85  GLN n 
2 86  LEU n 
2 87  PHE n 
2 88  HIS n 
2 89  PRO n 
2 90  GLU n 
2 91  GLN n 
2 92  LEU n 
2 93  ILE n 
2 94  THR n 
2 95  GLY n 
2 96  LYS n 
2 97  GLU n 
2 98  ASP n 
2 99  ALA n 
2 100 ALA n 
2 101 ASN n 
2 102 ASN n 
2 103 TYR n 
2 104 ALA n 
2 105 ARG n 
2 106 GLY n 
2 107 HIS n 
2 108 TYR n 
2 109 THR n 
2 110 ILE n 
2 111 GLY n 
2 112 LYS n 
2 113 GLU n 
2 114 ILE n 
2 115 ILE n 
2 116 ASP n 
2 117 LEU n 
2 118 VAL n 
2 119 LEU n 
2 120 ASP n 
2 121 ARG n 
2 122 ILE n 
2 123 ARG n 
2 124 LYS n 
2 125 LEU n 
2 126 ALA n 
2 127 ASP n 
2 128 GLN n 
2 129 CYS n 
2 130 THR n 
2 131 GLY n 
2 132 LEU n 
2 133 GLN n 
2 134 GLY n 
2 135 PHE n 
2 136 LEU n 
2 137 VAL n 
2 138 PHE n 
2 139 HIS n 
2 140 SER n 
2 141 PHE n 
2 142 GLY n 
2 143 GLY n 
2 144 GLY n 
2 145 THR n 
2 146 GLY n 
2 147 SER n 
2 148 GLY n 
2 149 PHE n 
2 150 THR n 
2 151 SER n 
2 152 LEU n 
2 153 LEU n 
2 154 MET n 
2 155 GLU n 
2 156 ARG n 
2 157 LEU n 
2 158 SER n 
2 159 VAL n 
2 160 ASP n 
2 161 TYR n 
2 162 GLY n 
2 163 LYS n 
2 164 LYS n 
2 165 SER n 
2 166 LYS n 
2 167 LEU n 
2 168 GLU n 
2 169 PHE n 
2 170 SER n 
2 171 ILE n 
2 172 TYR n 
2 173 PRO n 
2 174 ALA n 
2 175 PRO n 
2 176 GLN n 
2 177 VAL n 
2 178 SER n 
2 179 THR n 
2 180 ALA n 
2 181 VAL n 
2 182 VAL n 
2 183 GLU n 
2 184 PRO n 
2 185 TYR n 
2 186 ASN n 
2 187 SER n 
2 188 ILE n 
2 189 LEU n 
2 190 THR n 
2 191 THR n 
2 192 HIS n 
2 193 THR n 
2 194 THR n 
2 195 LEU n 
2 196 GLU n 
2 197 HIS n 
2 198 SER n 
2 199 ASP n 
2 200 CYS n 
2 201 ALA n 
2 202 PHE n 
2 203 MET n 
2 204 VAL n 
2 205 ASP n 
2 206 ASN n 
2 207 GLU n 
2 208 ALA n 
2 209 ILE n 
2 210 TYR n 
2 211 ASP n 
2 212 ILE n 
2 213 CYS n 
2 214 ARG n 
2 215 ARG n 
2 216 ASN n 
2 217 LEU n 
2 218 ASP n 
2 219 ILE n 
2 220 GLU n 
2 221 ARG n 
2 222 PRO n 
2 223 THR n 
2 224 TYR n 
2 225 THR n 
2 226 ASN n 
2 227 LEU n 
2 228 ASN n 
2 229 ARG n 
2 230 LEU n 
2 231 ILE n 
2 232 SER n 
2 233 GLN n 
2 234 ILE n 
2 235 VAL n 
2 236 SER n 
2 237 SER n 
2 238 ILE n 
2 239 THR n 
2 240 ALA n 
2 241 SER n 
2 242 LEU n 
2 243 ARG n 
2 244 PHE n 
2 245 ASP n 
2 246 GLY n 
2 247 ALA n 
2 248 LEU n 
2 249 ASN n 
2 250 VAL n 
2 251 ASP n 
2 252 LEU n 
2 253 THR n 
2 254 GLU n 
2 255 PHE n 
2 256 GLN n 
2 257 THR n 
2 258 ASN n 
2 259 LEU n 
2 260 VAL n 
2 261 PRO n 
2 262 TYR n 
2 263 PRO n 
2 264 ARG n 
2 265 ILE n 
2 266 HIS n 
2 267 PHE n 
2 268 PRO n 
2 269 LEU n 
2 270 ALA n 
2 271 THR n 
2 272 TYR n 
2 273 ALA n 
2 274 PRO n 
2 275 VAL n 
2 276 ILE n 
2 277 SER n 
2 278 ALA n 
2 279 GLU n 
2 280 LYS n 
2 281 ALA n 
2 282 TYR n 
2 283 HIS n 
2 284 GLU n 
2 285 GLN n 
2 286 LEU n 
2 287 SER n 
2 288 VAL n 
2 289 ALA n 
2 290 GLU n 
2 291 ILE n 
2 292 THR n 
2 293 ASN n 
2 294 ALA n 
2 295 CYS n 
2 296 PHE n 
2 297 GLU n 
2 298 PRO n 
2 299 ALA n 
2 300 ASN n 
2 301 GLN n 
2 302 MET n 
2 303 VAL n 
2 304 LYS n 
2 305 CYS n 
2 306 ASP n 
2 307 PRO n 
2 308 ARG n 
2 309 HIS n 
2 310 GLY n 
2 311 LYS n 
2 312 TYR n 
2 313 MET n 
2 314 ALA n 
2 315 CYS n 
2 316 CYS n 
2 317 LEU n 
2 318 LEU n 
2 319 TYR n 
2 320 ARG n 
2 321 GLY n 
2 322 ASP n 
2 323 VAL n 
2 324 VAL n 
2 325 PRO n 
2 326 LYS n 
2 327 ASP n 
2 328 VAL n 
2 329 ASN n 
2 330 ALA n 
2 331 ALA n 
2 332 ILE n 
2 333 ALA n 
2 334 THR n 
2 335 ILE n 
2 336 LYS n 
2 337 THR n 
2 338 LYS n 
2 339 ARG n 
2 340 SER n 
2 341 ILE n 
2 342 GLN n 
2 343 PHE n 
2 344 VAL n 
2 345 ASP n 
2 346 TRP n 
2 347 CYS n 
2 348 PRO n 
2 349 THR n 
2 350 GLY n 
2 351 PHE n 
2 352 LYS n 
2 353 VAL n 
2 354 GLY n 
2 355 ILE n 
2 356 ASN n 
2 357 TYR n 
2 358 GLN n 
2 359 PRO n 
2 360 PRO n 
2 361 THR n 
2 362 VAL n 
2 363 VAL n 
2 364 PRO n 
2 365 GLY n 
2 366 GLY n 
2 367 ASP n 
2 368 LEU n 
2 369 ALA n 
2 370 LYS n 
2 371 VAL n 
2 372 GLN n 
2 373 ARG n 
2 374 ALA n 
2 375 VAL n 
2 376 CYS n 
2 377 MET n 
2 378 LEU n 
2 379 SER n 
2 380 ASN n 
2 381 THR n 
2 382 THR n 
2 383 ALA n 
2 384 ILE n 
2 385 ALA n 
2 386 GLU n 
2 387 ALA n 
2 388 TRP n 
2 389 ALA n 
2 390 ARG n 
2 391 LEU n 
2 392 ASP n 
2 393 HIS n 
2 394 LYS n 
2 395 PHE n 
2 396 ASP n 
2 397 LEU n 
2 398 MET n 
2 399 TYR n 
2 400 ALA n 
2 401 LYS n 
2 402 ARG n 
2 403 ALA n 
2 404 PHE n 
2 405 VAL n 
2 406 HIS n 
2 407 TRP n 
2 408 TYR n 
2 409 VAL n 
2 410 GLY n 
2 411 GLU n 
2 412 GLY n 
2 413 MET n 
2 414 GLU n 
2 415 GLU n 
2 416 GLY n 
2 417 GLU n 
2 418 PHE n 
2 419 SER n 
2 420 GLU n 
2 421 ALA n 
2 422 ARG n 
2 423 GLU n 
2 424 ASP n 
2 425 MET n 
2 426 ALA n 
2 427 ALA n 
2 428 LEU n 
2 429 GLU n 
2 430 LYS n 
2 431 ASP n 
2 432 TYR n 
2 433 GLU n 
2 434 GLU n 
2 435 VAL n 
2 436 GLY n 
2 437 VAL n 
2 438 ASP n 
2 439 SER n 
2 440 VAL n 
2 441 GLU n 
2 442 GLY n 
2 443 GLU n 
2 444 GLY n 
2 445 GLU n 
2 446 GLU n 
2 447 GLU n 
2 448 GLY n 
2 449 GLU n 
2 450 GLU n 
2 451 TYR n 
3 1   MET n 
3 2   ALA n 
3 3   ASP n 
3 4   LEU n 
3 5   ALA n 
3 6   GLU n 
3 7   CYS n 
3 8   ASN n 
3 9   ILE n 
3 10  LYS n 
3 11  VAL n 
3 12  MET n 
3 13  CYS n 
3 14  ARG n 
3 15  PHE n 
3 16  ARG n 
3 17  PRO n 
3 18  LEU n 
3 19  ASN n 
3 20  GLU n 
3 21  SER n 
3 22  GLU n 
3 23  VAL n 
3 24  ASN n 
3 25  ARG n 
3 26  GLY n 
3 27  ASP n 
3 28  LYS n 
3 29  TYR n 
3 30  ILE n 
3 31  ALA n 
3 32  LYS n 
3 33  PHE n 
3 34  GLN n 
3 35  GLY n 
3 36  GLU n 
3 37  ASP n 
3 38  THR n 
3 39  VAL n 
3 40  VAL n 
3 41  ILE n 
3 42  ALA n 
3 43  SER n 
3 44  LYS n 
3 45  PRO n 
3 46  TYR n 
3 47  ALA n 
3 48  PHE n 
3 49  ASP n 
3 50  ARG n 
3 51  VAL n 
3 52  PHE n 
3 53  GLN n 
3 54  SER n 
3 55  SER n 
3 56  THR n 
3 57  SER n 
3 58  GLN n 
3 59  GLU n 
3 60  GLN n 
3 61  VAL n 
3 62  TYR n 
3 63  ASN n 
3 64  ASP n 
3 65  CYS n 
3 66  ALA n 
3 67  LYS n 
3 68  LYS n 
3 69  ILE n 
3 70  VAL n 
3 71  LYS n 
3 72  ASP n 
3 73  VAL n 
3 74  LEU n 
3 75  GLU n 
3 76  GLY n 
3 77  TYR n 
3 78  ASN n 
3 79  GLY n 
3 80  THR n 
3 81  ILE n 
3 82  PHE n 
3 83  ALA n 
3 84  TYR n 
3 85  GLY n 
3 86  GLN n 
3 87  THR n 
3 88  SER n 
3 89  SER n 
3 90  GLY n 
3 91  LYS n 
3 92  THR n 
3 93  HIS n 
3 94  THR n 
3 95  MET n 
3 96  GLU n 
3 97  GLY n 
3 98  LYS n 
3 99  LEU n 
3 100 HIS n 
3 101 ASP n 
3 102 PRO n 
3 103 GLU n 
3 104 GLY n 
3 105 MET n 
3 106 GLY n 
3 107 ILE n 
3 108 ILE n 
3 109 PRO n 
3 110 ARG n 
3 111 ILE n 
3 112 VAL n 
3 113 GLN n 
3 114 ASP n 
3 115 ILE n 
3 116 PHE n 
3 117 ASN n 
3 118 TYR n 
3 119 ILE n 
3 120 TYR n 
3 121 SER n 
3 122 MET n 
3 123 ASP n 
3 124 GLU n 
3 125 ASN n 
3 126 LEU n 
3 127 GLU n 
3 128 PHE n 
3 129 HIS n 
3 130 ILE n 
3 131 LYS n 
3 132 VAL n 
3 133 SER n 
3 134 TYR n 
3 135 PHE n 
3 136 GLU n 
3 137 ILE n 
3 138 TYR n 
3 139 LEU n 
3 140 ASP n 
3 141 LYS n 
3 142 ILE n 
3 143 ARG n 
3 144 ASP n 
3 145 LEU n 
3 146 LEU n 
3 147 ASP n 
3 148 VAL n 
3 149 SER n 
3 150 LYS n 
3 151 THR n 
3 152 ASN n 
3 153 LEU n 
3 154 SER n 
3 155 VAL n 
3 156 HIS n 
3 157 GLU n 
3 158 ASP n 
3 159 LYS n 
3 160 ASN n 
3 161 ARG n 
3 162 VAL n 
3 163 PRO n 
3 164 TYR n 
3 165 VAL n 
3 166 LYS n 
3 167 GLY n 
3 168 CYS n 
3 169 THR n 
3 170 GLU n 
3 171 ARG n 
3 172 PHE n 
3 173 VAL n 
3 174 CYS n 
3 175 SER n 
3 176 PRO n 
3 177 ASP n 
3 178 GLU n 
3 179 VAL n 
3 180 MET n 
3 181 ASP n 
3 182 THR n 
3 183 ILE n 
3 184 ASP n 
3 185 GLU n 
3 186 GLY n 
3 187 LYS n 
3 188 SER n 
3 189 ASN n 
3 190 ARG n 
3 191 HIS n 
3 192 VAL n 
3 193 ALA n 
3 194 VAL n 
3 195 THR n 
3 196 ASN n 
3 197 MET n 
3 198 ASN n 
3 199 GLU n 
3 200 HIS n 
3 201 SER n 
3 202 SER n 
3 203 ARG n 
3 204 SER n 
3 205 HIS n 
3 206 SER n 
3 207 ILE n 
3 208 PHE n 
3 209 LEU n 
3 210 ILE n 
3 211 ASN n 
3 212 VAL n 
3 213 LYS n 
3 214 GLN n 
3 215 GLU n 
3 216 ASN n 
3 217 THR n 
3 218 GLN n 
3 219 THR n 
3 220 GLU n 
3 221 GLN n 
3 222 LYS n 
3 223 LEU n 
3 224 SER n 
3 225 GLY n 
3 226 LYS n 
3 227 LEU n 
3 228 TYR n 
3 229 LEU n 
3 230 VAL n 
3 231 ASP n 
3 232 LEU n 
3 233 ALA n 
3 234 GLY n 
3 235 SER n 
3 236 GLU n 
3 237 LYS n 
3 238 VAL n 
3 239 SER n 
3 240 LYS n 
3 241 THR n 
3 242 GLY n 
3 243 ALA n 
3 244 GLU n 
3 245 GLY n 
3 246 ALA n 
3 247 VAL n 
3 248 LEU n 
3 249 ASP n 
3 250 GLU n 
3 251 ALA n 
3 252 LYS n 
3 253 ASN n 
3 254 ILE n 
3 255 ASN n 
3 256 LYS n 
3 257 SER n 
3 258 LEU n 
3 259 SER n 
3 260 ALA n 
3 261 LEU n 
3 262 GLY n 
3 263 ASN n 
3 264 VAL n 
3 265 ILE n 
3 266 SER n 
3 267 ALA n 
3 268 LEU n 
3 269 ALA n 
3 270 GLU n 
3 271 GLY n 
3 272 SER n 
3 273 THR n 
3 274 TYR n 
3 275 VAL n 
3 276 PRO n 
3 277 TYR n 
3 278 ARG n 
3 279 ASP n 
3 280 SER n 
3 281 LYS n 
3 282 MET n 
3 283 THR n 
3 284 ARG n 
3 285 ILE n 
3 286 LEU n 
3 287 GLN n 
3 288 ASP n 
3 289 SER n 
3 290 LEU n 
3 291 GLY n 
3 292 GLY n 
3 293 ASN n 
3 294 CYS n 
3 295 ARG n 
3 296 THR n 
3 297 THR n 
3 298 ILE n 
3 299 VAL n 
3 300 ILE n 
3 301 CYS n 
3 302 CYS n 
3 303 SER n 
3 304 PRO n 
3 305 SER n 
3 306 SER n 
3 307 TYR n 
3 308 ASN n 
3 309 GLU n 
3 310 SER n 
3 311 GLU n 
3 312 THR n 
3 313 LYS n 
3 314 SER n 
3 315 THR n 
3 316 LEU n 
3 317 LEU n 
3 318 PHE n 
3 319 GLY n 
3 320 GLN n 
3 321 ARG n 
3 322 ALA n 
3 323 LYS n 
3 324 THR n 
3 325 ILE n 
3 326 LYS n 
3 327 ASN n 
3 328 THR n 
3 329 VAL n 
3 330 CYS n 
3 331 VAL n 
3 332 ASN n 
3 333 VAL n 
3 334 GLU n 
3 335 LEU n 
3 336 THR n 
3 337 ALA n 
3 338 GLU n 
3 339 GLN n 
3 340 TRP n 
3 341 LYS n 
3 342 LYS n 
3 343 LYS n 
3 344 TYR n 
3 345 GLU n 
3 346 LYS n 
3 347 GLU n 
3 348 LYS n 
3 349 GLU n 
3 350 LYS n 
3 351 ASN n 
3 352 LYS n 
3 353 ILE n 
3 354 LEU n 
3 355 ARG n 
3 356 ASN n 
3 357 THR n 
3 358 THR n 
3 359 GLY n 
3 360 SER n 
3 361 THR n 
3 362 GLY n 
3 363 SER n 
3 364 THR n 
3 365 GLY n 
3 366 SER n 
3 367 THR n 
3 368 GLY n 
3 369 SER n 
3 370 THR n 
3 371 GLY n 
3 372 SER n 
3 373 THR n 
3 374 GLY n 
3 375 SER n 
3 376 THR n 
3 377 GLY n 
3 378 SER n 
3 379 THR n 
3 380 GLY n 
3 381 SER n 
3 382 THR n 
3 383 GLY n 
3 384 SER n 
3 385 ALA n 
3 386 ARG n 
3 387 ARG n 
3 388 GLY n 
3 389 HIS n 
3 390 SER n 
3 391 ALA n 
3 392 THR n 
3 393 GLY n 
3 394 SER n 
3 395 THR n 
3 396 SER n 
3 397 GLY n 
3 398 THR n 
3 399 PRO n 
3 400 GLY n 
3 401 GLN n 
3 402 HIS n 
3 403 PRO n 
3 404 ALA n 
3 405 ALA n 
3 406 SER n 
3 407 PRO n 
3 408 THR n 
# 
_entity_src_gen.entity_id                          3 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   408 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KIF5B, KNS, KNS1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 445 pig 'Sus scrofa' 9823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 1 451 pig 'Sus scrofa' 9823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
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  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
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 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
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 
TA1 non-polymer         . TAXOL                       ? 'C47 H51 N O14'     853.906 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET B . n 
A 1 2   ARG 2   2   2   ARG ARG B . n 
A 1 3   GLU 3   3   3   GLU GLU B . n 
A 1 4   ILE 4   4   4   ILE ILE B . n 
A 1 5   VAL 5   5   5   VAL VAL B . n 
A 1 6   HIS 6   6   6   HIS HIS B . n 
A 1 7   ILE 7   7   7   ILE ILE B . n 
A 1 8   GLN 8   8   8   GLN GLN B . n 
A 1 9   ALA 9   9   9   ALA ALA B . n 
A 1 10  GLY 10  10  10  GLY GLY B . n 
A 1 11  GLN 11  11  11  GLN GLN B . n 
A 1 12  CYS 12  12  12  CYS CYS B . n 
A 1 13  GLY 13  13  13  GLY GLY B . n 
A 1 14  ASN 14  14  14  ASN ASN B . n 
A 1 15  GLN 15  15  15  GLN GLN B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  GLY 17  17  17  GLY GLY B . n 
A 1 18  ALA 18  18  18  ALA ALA B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  PHE 20  20  20  PHE PHE B . n 
A 1 21  TRP 21  21  21  TRP TRP B . n 
A 1 22  GLU 22  22  22  GLU GLU B . n 
A 1 23  VAL 23  23  23  VAL VAL B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  SER 25  25  25  SER SER B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLU 27  27  27  GLU GLU B . n 
A 1 28  HIS 28  28  28  HIS HIS B . n 
A 1 29  GLY 29  29  29  GLY GLY B . n 
A 1 30  ILE 30  30  30  ILE ILE B . n 
A 1 31  ASP 31  31  31  ASP ASP B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  THR 33  33  33  THR THR B . n 
A 1 34  GLY 34  34  34  GLY GLY B . n 
A 1 35  SER 35  35  35  SER SER B . n 
A 1 36  TYR 36  36  36  TYR TYR B . n 
A 1 37  HIS 37  37  37  HIS HIS B . n 
A 1 38  GLY 38  38  38  GLY GLY B . n 
A 1 39  ASP 39  39  39  ASP ASP B . n 
A 1 40  SER 40  40  40  SER SER B . n 
A 1 41  ASP 41  41  41  ASP ASP B . n 
A 1 42  LEU 42  42  42  LEU LEU B . n 
A 1 43  GLN 43  43  43  GLN GLN B . n 
A 1 44  LEU 44  44  44  LEU LEU B . n 
A 1 45  GLU 45  47  47  GLU GLU B . n 
A 1 46  ARG 46  48  48  ARG ARG B . n 
A 1 47  ILE 47  49  49  ILE ILE B . n 
A 1 48  ASN 48  50  50  ASN ASN B . n 
A 1 49  VAL 49  51  51  VAL VAL B . n 
A 1 50  TYR 50  52  52  TYR TYR B . n 
A 1 51  TYR 51  53  53  TYR TYR B . n 
A 1 52  ASN 52  54  54  ASN ASN B . n 
A 1 53  GLU 53  55  55  GLU GLU B . n 
A 1 54  ALA 54  56  56  ALA ALA B . n 
A 1 55  ALA 55  57  57  ALA ALA B . n 
A 1 56  GLY 56  58  58  GLY GLY B . n 
A 1 57  ASN 57  59  59  ASN ASN B . n 
A 1 58  LYS 58  60  60  LYS LYS B . n 
A 1 59  TYR 59  61  61  TYR TYR B . n 
A 1 60  VAL 60  62  62  VAL VAL B . n 
A 1 61  PRO 61  63  63  PRO PRO B . n 
A 1 62  ARG 62  64  64  ARG ARG B . n 
A 1 63  ALA 63  65  65  ALA ALA B . n 
A 1 64  ILE 64  66  66  ILE ILE B . n 
A 1 65  LEU 65  67  67  LEU LEU B . n 
A 1 66  VAL 66  68  68  VAL VAL B . n 
A 1 67  ASP 67  69  69  ASP ASP B . n 
A 1 68  LEU 68  70  70  LEU LEU B . n 
A 1 69  GLU 69  71  71  GLU GLU B . n 
A 1 70  PRO 70  72  72  PRO PRO B . n 
A 1 71  GLY 71  73  73  GLY GLY B . n 
A 1 72  THR 72  74  74  THR THR B . n 
A 1 73  MET 73  75  75  MET MET B . n 
A 1 74  ASP 74  76  76  ASP ASP B . n 
A 1 75  SER 75  77  77  SER SER B . n 
A 1 76  VAL 76  78  78  VAL VAL B . n 
A 1 77  ARG 77  79  79  ARG ARG B . n 
A 1 78  SER 78  80  80  SER SER B . n 
A 1 79  GLY 79  81  81  GLY GLY B . n 
A 1 80  PRO 80  82  82  PRO PRO B . n 
A 1 81  PHE 81  83  83  PHE PHE B . n 
A 1 82  GLY 82  84  84  GLY GLY B . n 
A 1 83  GLN 83  85  85  GLN GLN B . n 
A 1 84  ILE 84  86  86  ILE ILE B . n 
A 1 85  PHE 85  87  87  PHE PHE B . n 
A 1 86  ARG 86  88  88  ARG ARG B . n 
A 1 87  PRO 87  89  89  PRO PRO B . n 
A 1 88  ASP 88  90  90  ASP ASP B . n 
A 1 89  ASN 89  91  91  ASN ASN B . n 
A 1 90  PHE 90  92  92  PHE PHE B . n 
A 1 91  VAL 91  93  93  VAL VAL B . n 
A 1 92  PHE 92  94  94  PHE PHE B . n 
A 1 93  GLY 93  95  95  GLY GLY B . n 
A 1 94  GLN 94  96  96  GLN GLN B . n 
A 1 95  SER 95  97  97  SER SER B . n 
A 1 96  GLY 96  98  98  GLY GLY B . n 
A 1 97  ALA 97  99  99  ALA ALA B . n 
A 1 98  GLY 98  100 100 GLY GLY B . n 
A 1 99  ASN 99  101 101 ASN ASN B . n 
A 1 100 ASN 100 102 102 ASN ASN B . n 
A 1 101 TRP 101 103 103 TRP TRP B . n 
A 1 102 ALA 102 104 104 ALA ALA B . n 
A 1 103 LYS 103 105 105 LYS LYS B . n 
A 1 104 GLY 104 106 106 GLY GLY B . n 
A 1 105 HIS 105 107 107 HIS HIS B . n 
A 1 106 TYR 106 108 108 TYR TYR B . n 
A 1 107 THR 107 109 109 THR THR B . n 
A 1 108 GLU 108 110 110 GLU GLU B . n 
A 1 109 GLY 109 111 111 GLY GLY B . n 
A 1 110 ALA 110 112 112 ALA ALA B . n 
A 1 111 GLU 111 113 113 GLU GLU B . n 
A 1 112 LEU 112 114 114 LEU LEU B . n 
A 1 113 VAL 113 115 115 VAL VAL B . n 
A 1 114 ASP 114 116 116 ASP ASP B . n 
A 1 115 SER 115 117 117 SER SER B . n 
A 1 116 VAL 116 118 118 VAL VAL B . n 
A 1 117 LEU 117 119 119 LEU LEU B . n 
A 1 118 ASP 118 120 120 ASP ASP B . n 
A 1 119 VAL 119 121 121 VAL VAL B . n 
A 1 120 VAL 120 122 122 VAL VAL B . n 
A 1 121 ARG 121 123 123 ARG ARG B . n 
A 1 122 LYS 122 124 124 LYS LYS B . n 
A 1 123 GLU 123 125 125 GLU GLU B . n 
A 1 124 SER 124 126 126 SER SER B . n 
A 1 125 GLU 125 127 127 GLU GLU B . n 
A 1 126 SER 126 128 128 SER SER B . n 
A 1 127 CYS 127 129 129 CYS CYS B . n 
A 1 128 ASP 128 130 130 ASP ASP B . n 
A 1 129 CYS 129 131 131 CYS CYS B . n 
A 1 130 LEU 130 132 132 LEU LEU B . n 
A 1 131 GLN 131 133 133 GLN GLN B . n 
A 1 132 GLY 132 134 134 GLY GLY B . n 
A 1 133 PHE 133 135 135 PHE PHE B . n 
A 1 134 GLN 134 136 136 GLN GLN B . n 
A 1 135 LEU 135 137 137 LEU LEU B . n 
A 1 136 THR 136 138 138 THR THR B . n 
A 1 137 HIS 137 139 139 HIS HIS B . n 
A 1 138 SER 138 140 140 SER SER B . n 
A 1 139 LEU 139 141 141 LEU LEU B . n 
A 1 140 GLY 140 142 142 GLY GLY B . n 
A 1 141 GLY 141 143 143 GLY GLY B . n 
A 1 142 GLY 142 144 144 GLY GLY B . n 
A 1 143 THR 143 145 145 THR THR B . n 
A 1 144 GLY 144 146 146 GLY GLY B . n 
A 1 145 SER 145 147 147 SER SER B . n 
A 1 146 GLY 146 148 148 GLY GLY B . n 
A 1 147 MET 147 149 149 MET MET B . n 
A 1 148 GLY 148 150 150 GLY GLY B . n 
A 1 149 THR 149 151 151 THR THR B . n 
A 1 150 LEU 150 152 152 LEU LEU B . n 
A 1 151 LEU 151 153 153 LEU LEU B . n 
A 1 152 ILE 152 154 154 ILE ILE B . n 
A 1 153 SER 153 155 155 SER SER B . n 
A 1 154 LYS 154 156 156 LYS LYS B . n 
A 1 155 ILE 155 157 157 ILE ILE B . n 
A 1 156 ARG 156 158 158 ARG ARG B . n 
A 1 157 GLU 157 159 159 GLU GLU B . n 
A 1 158 GLU 158 160 160 GLU GLU B . n 
A 1 159 TYR 159 161 161 TYR TYR B . n 
A 1 160 PRO 160 162 162 PRO PRO B . n 
A 1 161 ASP 161 163 163 ASP ASP B . n 
A 1 162 ARG 162 164 164 ARG ARG B . n 
A 1 163 ILE 163 165 165 ILE ILE B . n 
A 1 164 MET 164 166 166 MET MET B . n 
A 1 165 ASN 165 167 167 ASN ASN B . n 
A 1 166 THR 166 168 168 THR THR B . n 
A 1 167 PHE 167 169 169 PHE PHE B . n 
A 1 168 SER 168 170 170 SER SER B . n 
A 1 169 VAL 169 171 171 VAL VAL B . n 
A 1 170 VAL 170 172 172 VAL VAL B . n 
A 1 171 PRO 171 173 173 PRO PRO B . n 
A 1 172 SER 172 174 174 SER SER B . n 
A 1 173 PRO 173 175 175 PRO PRO B . n 
A 1 174 LYS 174 176 176 LYS LYS B . n 
A 1 175 VAL 175 177 177 VAL VAL B . n 
A 1 176 SER 176 178 178 SER SER B . n 
A 1 177 ASP 177 179 179 ASP ASP B . n 
A 1 178 THR 178 180 180 THR THR B . n 
A 1 179 VAL 179 181 181 VAL VAL B . n 
A 1 180 VAL 180 182 182 VAL VAL B . n 
A 1 181 GLU 181 183 183 GLU GLU B . n 
A 1 182 PRO 182 184 184 PRO PRO B . n 
A 1 183 TYR 183 185 185 TYR TYR B . n 
A 1 184 ASN 184 186 186 ASN ASN B . n 
A 1 185 ALA 185 187 187 ALA ALA B . n 
A 1 186 THR 186 188 188 THR THR B . n 
A 1 187 LEU 187 189 189 LEU LEU B . n 
A 1 188 SER 188 190 190 SER SER B . n 
A 1 189 VAL 189 191 191 VAL VAL B . n 
A 1 190 HIS 190 192 192 HIS HIS B . n 
A 1 191 GLN 191 193 193 GLN GLN B . n 
A 1 192 LEU 192 194 194 LEU LEU B . n 
A 1 193 VAL 193 195 195 VAL VAL B . n 
A 1 194 GLU 194 196 196 GLU GLU B . n 
A 1 195 ASN 195 197 197 ASN ASN B . n 
A 1 196 THR 196 198 198 THR THR B . n 
A 1 197 ASP 197 199 199 ASP ASP B . n 
A 1 198 GLU 198 200 200 GLU GLU B . n 
A 1 199 THR 199 201 201 THR THR B . n 
A 1 200 TYR 200 202 202 TYR TYR B . n 
A 1 201 CYS 201 203 203 CYS CYS B . n 
A 1 202 ILE 202 204 204 ILE ILE B . n 
A 1 203 ASP 203 205 205 ASP ASP B . n 
A 1 204 ASN 204 206 206 ASN ASN B . n 
A 1 205 GLU 205 207 207 GLU GLU B . n 
A 1 206 ALA 206 208 208 ALA ALA B . n 
A 1 207 LEU 207 209 209 LEU LEU B . n 
A 1 208 TYR 208 210 210 TYR TYR B . n 
A 1 209 ASP 209 211 211 ASP ASP B . n 
A 1 210 ILE 210 212 212 ILE ILE B . n 
A 1 211 CYS 211 213 213 CYS CYS B . n 
A 1 212 PHE 212 214 214 PHE PHE B . n 
A 1 213 ARG 213 215 215 ARG ARG B . n 
A 1 214 THR 214 216 216 THR THR B . n 
A 1 215 LEU 215 217 217 LEU LEU B . n 
A 1 216 LYS 216 218 218 LYS LYS B . n 
A 1 217 LEU 217 219 219 LEU LEU B . n 
A 1 218 THR 218 220 220 THR THR B . n 
A 1 219 THR 219 221 221 THR THR B . n 
A 1 220 PRO 220 222 222 PRO PRO B . n 
A 1 221 THR 221 223 223 THR THR B . n 
A 1 222 TYR 222 224 224 TYR TYR B . n 
A 1 223 GLY 223 225 225 GLY GLY B . n 
A 1 224 ASP 224 226 226 ASP ASP B . n 
A 1 225 LEU 225 227 227 LEU LEU B . n 
A 1 226 ASN 226 228 228 ASN ASN B . n 
A 1 227 HIS 227 229 229 HIS HIS B . n 
A 1 228 LEU 228 230 230 LEU LEU B . n 
A 1 229 VAL 229 231 231 VAL VAL B . n 
A 1 230 SER 230 232 232 SER SER B . n 
A 1 231 ALA 231 233 233 ALA ALA B . n 
A 1 232 THR 232 234 234 THR THR B . n 
A 1 233 MET 233 235 235 MET MET B . n 
A 1 234 SER 234 236 236 SER SER B . n 
A 1 235 GLY 235 237 237 GLY GLY B . n 
A 1 236 VAL 236 238 238 VAL VAL B . n 
A 1 237 THR 237 239 239 THR THR B . n 
A 1 238 THR 238 240 240 THR THR B . n 
A 1 239 CYS 239 241 241 CYS CYS B . n 
A 1 240 LEU 240 242 242 LEU LEU B . n 
A 1 241 ARG 241 243 243 ARG ARG B . n 
A 1 242 PHE 242 244 244 PHE PHE B . n 
A 1 243 PRO 243 245 245 PRO PRO B . n 
A 1 244 GLY 244 246 246 GLY GLY B . n 
A 1 245 GLN 245 247 247 GLN GLN B . n 
A 1 246 LEU 246 248 248 LEU LEU B . n 
A 1 247 ASN 247 249 249 ASN ASN B . n 
A 1 248 ALA 248 250 250 ALA ALA B . n 
A 1 249 ASP 249 251 251 ASP ASP B . n 
A 1 250 LEU 250 252 252 LEU LEU B . n 
A 1 251 ARG 251 253 253 ARG ARG B . n 
A 1 252 LYS 252 254 254 LYS LYS B . n 
A 1 253 LEU 253 255 255 LEU LEU B . n 
A 1 254 ALA 254 256 256 ALA ALA B . n 
A 1 255 VAL 255 257 257 VAL VAL B . n 
A 1 256 ASN 256 258 258 ASN ASN B . n 
A 1 257 MET 257 259 259 MET MET B . n 
A 1 258 VAL 258 260 260 VAL VAL B . n 
A 1 259 PRO 259 261 261 PRO PRO B . n 
A 1 260 PHE 260 262 262 PHE PHE B . n 
A 1 261 PRO 261 263 263 PRO PRO B . n 
A 1 262 ARG 262 264 264 ARG ARG B . n 
A 1 263 LEU 263 265 265 LEU LEU B . n 
A 1 264 HIS 264 266 266 HIS HIS B . n 
A 1 265 PHE 265 267 267 PHE PHE B . n 
A 1 266 PHE 266 268 268 PHE PHE B . n 
A 1 267 MET 267 269 269 MET MET B . n 
A 1 268 PRO 268 270 270 PRO PRO B . n 
A 1 269 GLY 269 271 271 GLY GLY B . n 
A 1 270 PHE 270 272 272 PHE PHE B . n 
A 1 271 ALA 271 273 273 ALA ALA B . n 
A 1 272 PRO 272 274 274 PRO PRO B . n 
A 1 273 LEU 273 275 275 LEU LEU B . n 
A 1 274 THR 274 276 276 THR THR B . n 
A 1 275 SER 275 277 277 SER SER B . n 
A 1 276 ARG 276 278 278 ARG ARG B . n 
A 1 277 GLY 277 279 279 GLY GLY B . n 
A 1 278 SER 278 280 280 SER SER B . n 
A 1 279 GLN 279 281 281 GLN GLN B . n 
A 1 280 GLN 280 282 282 GLN GLN B . n 
A 1 281 TYR 281 283 283 TYR TYR B . n 
A 1 282 ARG 282 284 284 ARG ARG B . n 
A 1 283 ALA 283 285 285 ALA ALA B . n 
A 1 284 LEU 284 286 286 LEU LEU B . n 
A 1 285 THR 285 287 287 THR THR B . n 
A 1 286 VAL 286 288 288 VAL VAL B . n 
A 1 287 PRO 287 289 289 PRO PRO B . n 
A 1 288 GLU 288 290 290 GLU GLU B . n 
A 1 289 LEU 289 291 291 LEU LEU B . n 
A 1 290 THR 290 292 292 THR THR B . n 
A 1 291 GLN 291 293 293 GLN GLN B . n 
A 1 292 GLN 292 294 294 GLN GLN B . n 
A 1 293 MET 293 295 295 MET MET B . n 
A 1 294 PHE 294 296 296 PHE PHE B . n 
A 1 295 ASP 295 297 297 ASP ASP B . n 
A 1 296 ALA 296 298 298 ALA ALA B . n 
A 1 297 LYS 297 299 299 LYS LYS B . n 
A 1 298 ASN 298 300 300 ASN ASN B . n 
A 1 299 MET 299 301 301 MET MET B . n 
A 1 300 MET 300 302 302 MET MET B . n 
A 1 301 ALA 301 303 303 ALA ALA B . n 
A 1 302 ALA 302 304 304 ALA ALA B . n 
A 1 303 CYS 303 305 305 CYS CYS B . n 
A 1 304 ASP 304 306 306 ASP ASP B . n 
A 1 305 PRO 305 307 307 PRO PRO B . n 
A 1 306 ARG 306 308 308 ARG ARG B . n 
A 1 307 HIS 307 309 309 HIS HIS B . n 
A 1 308 GLY 308 310 310 GLY GLY B . n 
A 1 309 ARG 309 311 311 ARG ARG B . n 
A 1 310 TYR 310 312 312 TYR TYR B . n 
A 1 311 LEU 311 313 313 LEU LEU B . n 
A 1 312 THR 312 314 314 THR THR B . n 
A 1 313 VAL 313 315 315 VAL VAL B . n 
A 1 314 ALA 314 316 316 ALA ALA B . n 
A 1 315 ALA 315 317 317 ALA ALA B . n 
A 1 316 VAL 316 318 318 VAL VAL B . n 
A 1 317 PHE 317 319 319 PHE PHE B . n 
A 1 318 ARG 318 320 320 ARG ARG B . n 
A 1 319 GLY 319 321 321 GLY GLY B . n 
A 1 320 ARG 320 322 322 ARG ARG B . n 
A 1 321 MET 321 323 323 MET MET B . n 
A 1 322 SER 322 324 324 SER SER B . n 
A 1 323 MET 323 325 325 MET MET B . n 
A 1 324 LYS 324 326 326 LYS LYS B . n 
A 1 325 GLU 325 327 327 GLU GLU B . n 
A 1 326 VAL 326 328 328 VAL VAL B . n 
A 1 327 ASP 327 329 329 ASP ASP B . n 
A 1 328 GLU 328 330 330 GLU GLU B . n 
A 1 329 GLN 329 331 331 GLN GLN B . n 
A 1 330 MET 330 332 332 MET MET B . n 
A 1 331 LEU 331 333 333 LEU LEU B . n 
A 1 332 ASN 332 334 334 ASN ASN B . n 
A 1 333 VAL 333 335 335 VAL VAL B . n 
A 1 334 GLN 334 336 336 GLN GLN B . n 
A 1 335 ASN 335 337 337 ASN ASN B . n 
A 1 336 LYS 336 338 338 LYS LYS B . n 
A 1 337 ASN 337 339 339 ASN ASN B . n 
A 1 338 SER 338 340 340 SER SER B . n 
A 1 339 SER 339 341 341 SER SER B . n 
A 1 340 TYR 340 342 342 TYR TYR B . n 
A 1 341 PHE 341 343 343 PHE PHE B . n 
A 1 342 VAL 342 344 344 VAL VAL B . n 
A 1 343 GLU 343 345 345 GLU GLU B . n 
A 1 344 TRP 344 346 346 TRP TRP B . n 
A 1 345 ILE 345 347 347 ILE ILE B . n 
A 1 346 PRO 346 348 348 PRO PRO B . n 
A 1 347 ASN 347 349 349 ASN ASN B . n 
A 1 348 ASN 348 350 350 ASN ASN B . n 
A 1 349 VAL 349 351 351 VAL VAL B . n 
A 1 350 LYS 350 352 352 LYS LYS B . n 
A 1 351 THR 351 353 353 THR THR B . n 
A 1 352 ALA 352 354 354 ALA ALA B . n 
A 1 353 VAL 353 355 355 VAL VAL B . n 
A 1 354 CYS 354 356 356 CYS CYS B . n 
A 1 355 ASP 355 357 357 ASP ASP B . n 
A 1 356 ILE 356 358 358 ILE ILE B . n 
A 1 357 PRO 357 359 359 PRO PRO B . n 
A 1 358 PRO 358 360 360 PRO PRO B . n 
A 1 359 ARG 359 369 369 ARG ARG B . n 
A 1 360 GLY 360 370 370 GLY GLY B . n 
A 1 361 LEU 361 371 371 LEU LEU B . n 
A 1 362 LYS 362 372 372 LYS LYS B . n 
A 1 363 MET 363 373 373 MET MET B . n 
A 1 364 SER 364 374 374 SER SER B . n 
A 1 365 ALA 365 375 375 ALA ALA B . n 
A 1 366 THR 366 376 376 THR THR B . n 
A 1 367 PHE 367 377 377 PHE PHE B . n 
A 1 368 ILE 368 378 378 ILE ILE B . n 
A 1 369 GLY 369 379 379 GLY GLY B . n 
A 1 370 ASN 370 380 380 ASN ASN B . n 
A 1 371 SER 371 381 381 SER SER B . n 
A 1 372 THR 372 382 382 THR THR B . n 
A 1 373 ALA 373 383 383 ALA ALA B . n 
A 1 374 ILE 374 384 384 ILE ILE B . n 
A 1 375 GLN 375 385 385 GLN GLN B . n 
A 1 376 GLU 376 386 386 GLU GLU B . n 
A 1 377 LEU 377 387 387 LEU LEU B . n 
A 1 378 PHE 378 388 388 PHE PHE B . n 
A 1 379 LYS 379 389 389 LYS LYS B . n 
A 1 380 ARG 380 390 390 ARG ARG B . n 
A 1 381 ILE 381 391 391 ILE ILE B . n 
A 1 382 SER 382 392 392 SER SER B . n 
A 1 383 GLU 383 393 393 GLU GLU B . n 
A 1 384 GLN 384 394 394 GLN GLN B . n 
A 1 385 PHE 385 395 395 PHE PHE B . n 
A 1 386 THR 386 396 396 THR THR B . n 
A 1 387 ALA 387 397 397 ALA ALA B . n 
A 1 388 MET 388 398 398 MET MET B . n 
A 1 389 PHE 389 399 399 PHE PHE B . n 
A 1 390 ARG 390 400 400 ARG ARG B . n 
A 1 391 ARG 391 401 401 ARG ARG B . n 
A 1 392 LYS 392 402 402 LYS LYS B . n 
A 1 393 ALA 393 403 403 ALA ALA B . n 
A 1 394 PHE 394 404 404 PHE PHE B . n 
A 1 395 LEU 395 405 405 LEU LEU B . n 
A 1 396 HIS 396 406 406 HIS HIS B . n 
A 1 397 TRP 397 407 407 TRP TRP B . n 
A 1 398 TYR 398 408 408 TYR TYR B . n 
A 1 399 THR 399 409 409 THR THR B . n 
A 1 400 GLY 400 410 410 GLY GLY B . n 
A 1 401 GLU 401 411 411 GLU GLU B . n 
A 1 402 GLY 402 412 412 GLY GLY B . n 
A 1 403 MET 403 413 413 MET MET B . n 
A 1 404 ASP 404 414 414 ASP ASP B . n 
A 1 405 GLU 405 415 415 GLU GLU B . n 
A 1 406 MET 406 416 416 MET MET B . n 
A 1 407 GLU 407 417 417 GLU GLU B . n 
A 1 408 PHE 408 418 418 PHE PHE B . n 
A 1 409 THR 409 419 419 THR THR B . n 
A 1 410 GLU 410 420 420 GLU GLU B . n 
A 1 411 ALA 411 421 421 ALA ALA B . n 
A 1 412 GLU 412 422 422 GLU GLU B . n 
A 1 413 SER 413 423 423 SER SER B . n 
A 1 414 ASN 414 424 424 ASN ASN B . n 
A 1 415 MET 415 425 425 MET MET B . n 
A 1 416 ASN 416 426 426 ASN ASN B . n 
A 1 417 ASP 417 427 427 ASP ASP B . n 
A 1 418 LEU 418 428 428 LEU LEU B . n 
A 1 419 VAL 419 429 429 VAL VAL B . n 
A 1 420 SER 420 430 430 SER SER B . n 
A 1 421 GLU 421 431 431 GLU GLU B . n 
A 1 422 TYR 422 432 432 TYR TYR B . n 
A 1 423 GLN 423 433 433 GLN GLN B . n 
A 1 424 GLN 424 434 434 GLN GLN B . n 
A 1 425 TYR 425 435 435 TYR TYR B . n 
A 1 426 GLN 426 436 436 GLN GLN B . n 
A 1 427 ASP 427 437 ?   ?   ?   B . n 
A 1 428 ALA 428 438 ?   ?   ?   B . n 
A 1 429 THR 429 439 ?   ?   ?   B . n 
A 1 430 ALA 430 440 ?   ?   ?   B . n 
A 1 431 ASP 431 441 ?   ?   ?   B . n 
A 1 432 GLU 432 442 ?   ?   ?   B . n 
A 1 433 GLN 433 443 ?   ?   ?   B . n 
A 1 434 GLY 434 444 ?   ?   ?   B . n 
A 1 435 GLU 435 445 ?   ?   ?   B . n 
A 1 436 PHE 436 446 ?   ?   ?   B . n 
A 1 437 GLU 437 447 ?   ?   ?   B . n 
A 1 438 GLU 438 448 ?   ?   ?   B . n 
A 1 439 GLU 439 449 ?   ?   ?   B . n 
A 1 440 GLY 440 450 ?   ?   ?   B . n 
A 1 441 GLU 441 451 ?   ?   ?   B . n 
A 1 442 GLU 442 452 ?   ?   ?   B . n 
A 1 443 ASP 443 453 ?   ?   ?   B . n 
A 1 444 GLU 444 454 ?   ?   ?   B . n 
A 1 445 ALA 445 455 ?   ?   ?   B . n 
B 2 1   MET 1   1   1   MET MET A . n 
B 2 2   ARG 2   2   2   ARG ARG A . n 
B 2 3   GLU 3   3   3   GLU GLU A . n 
B 2 4   CYS 4   4   4   CYS CYS A . n 
B 2 5   ILE 5   5   5   ILE ILE A . n 
B 2 6   SER 6   6   6   SER SER A . n 
B 2 7   ILE 7   7   7   ILE ILE A . n 
B 2 8   HIS 8   8   8   HIS HIS A . n 
B 2 9   VAL 9   9   9   VAL VAL A . n 
B 2 10  GLY 10  10  10  GLY GLY A . n 
B 2 11  GLN 11  11  11  GLN GLN A . n 
B 2 12  ALA 12  12  12  ALA ALA A . n 
B 2 13  GLY 13  13  13  GLY GLY A . n 
B 2 14  VAL 14  14  14  VAL VAL A . n 
B 2 15  GLN 15  15  15  GLN GLN A . n 
B 2 16  ILE 16  16  16  ILE ILE A . n 
B 2 17  GLY 17  17  17  GLY GLY A . n 
B 2 18  ASN 18  18  18  ASN ASN A . n 
B 2 19  ALA 19  19  19  ALA ALA A . n 
B 2 20  CYS 20  20  20  CYS CYS A . n 
B 2 21  TRP 21  21  21  TRP TRP A . n 
B 2 22  GLU 22  22  22  GLU GLU A . n 
B 2 23  LEU 23  23  23  LEU LEU A . n 
B 2 24  TYR 24  24  24  TYR TYR A . n 
B 2 25  CYS 25  25  25  CYS CYS A . n 
B 2 26  LEU 26  26  26  LEU LEU A . n 
B 2 27  GLU 27  27  27  GLU GLU A . n 
B 2 28  HIS 28  28  28  HIS HIS A . n 
B 2 29  GLY 29  29  29  GLY GLY A . n 
B 2 30  ILE 30  30  30  ILE ILE A . n 
B 2 31  GLN 31  31  31  GLN GLN A . n 
B 2 32  PRO 32  32  32  PRO PRO A . n 
B 2 33  ASP 33  33  33  ASP ASP A . n 
B 2 34  GLY 34  34  34  GLY GLY A . n 
B 2 35  GLN 35  35  35  GLN GLN A . n 
B 2 36  MET 36  36  36  MET MET A . n 
B 2 37  PRO 37  37  37  PRO PRO A . n 
B 2 38  SER 38  38  ?   ?   ?   A . n 
B 2 39  ASP 39  39  ?   ?   ?   A . n 
B 2 40  LYS 40  40  ?   ?   ?   A . n 
B 2 41  THR 41  41  ?   ?   ?   A . n 
B 2 42  ILE 42  42  ?   ?   ?   A . n 
B 2 43  GLY 43  43  ?   ?   ?   A . n 
B 2 44  GLY 44  44  ?   ?   ?   A . n 
B 2 45  GLY 45  45  ?   ?   ?   A . n 
B 2 46  ASP 46  46  ?   ?   ?   A . n 
B 2 47  ASP 47  47  47  ASP ASP A . n 
B 2 48  SER 48  48  48  SER SER A . n 
B 2 49  PHE 49  49  49  PHE PHE A . n 
B 2 50  ASN 50  50  50  ASN ASN A . n 
B 2 51  THR 51  51  51  THR THR A . n 
B 2 52  PHE 52  52  52  PHE PHE A . n 
B 2 53  PHE 53  53  53  PHE PHE A . n 
B 2 54  SER 54  54  54  SER SER A . n 
B 2 55  GLU 55  55  55  GLU GLU A . n 
B 2 56  THR 56  56  56  THR THR A . n 
B 2 57  GLY 57  57  57  GLY GLY A . n 
B 2 58  ALA 58  58  58  ALA ALA A . n 
B 2 59  GLY 59  59  59  GLY GLY A . n 
B 2 60  LYS 60  60  60  LYS LYS A . n 
B 2 61  HIS 61  61  61  HIS HIS A . n 
B 2 62  VAL 62  62  62  VAL VAL A . n 
B 2 63  PRO 63  63  63  PRO PRO A . n 
B 2 64  ARG 64  64  64  ARG ARG A . n 
B 2 65  ALA 65  65  65  ALA ALA A . n 
B 2 66  VAL 66  66  66  VAL VAL A . n 
B 2 67  PHE 67  67  67  PHE PHE A . n 
B 2 68  VAL 68  68  68  VAL VAL A . n 
B 2 69  ASP 69  69  69  ASP ASP A . n 
B 2 70  LEU 70  70  70  LEU LEU A . n 
B 2 71  GLU 71  71  71  GLU GLU A . n 
B 2 72  PRO 72  72  72  PRO PRO A . n 
B 2 73  THR 73  73  73  THR THR A . n 
B 2 74  VAL 74  74  74  VAL VAL A . n 
B 2 75  ILE 75  75  75  ILE ILE A . n 
B 2 76  ASP 76  76  76  ASP ASP A . n 
B 2 77  GLU 77  77  77  GLU GLU A . n 
B 2 78  VAL 78  78  78  VAL VAL A . n 
B 2 79  ARG 79  79  79  ARG ARG A . n 
B 2 80  THR 80  80  80  THR THR A . n 
B 2 81  GLY 81  81  81  GLY GLY A . n 
B 2 82  THR 82  82  82  THR THR A . n 
B 2 83  TYR 83  83  83  TYR TYR A . n 
B 2 84  ARG 84  84  84  ARG ARG A . n 
B 2 85  GLN 85  85  85  GLN GLN A . n 
B 2 86  LEU 86  86  86  LEU LEU A . n 
B 2 87  PHE 87  87  87  PHE PHE A . n 
B 2 88  HIS 88  88  88  HIS HIS A . n 
B 2 89  PRO 89  89  89  PRO PRO A . n 
B 2 90  GLU 90  90  90  GLU GLU A . n 
B 2 91  GLN 91  91  91  GLN GLN A . n 
B 2 92  LEU 92  92  92  LEU LEU A . n 
B 2 93  ILE 93  93  93  ILE ILE A . n 
B 2 94  THR 94  94  94  THR THR A . n 
B 2 95  GLY 95  95  95  GLY GLY A . n 
B 2 96  LYS 96  96  96  LYS LYS A . n 
B 2 97  GLU 97  97  97  GLU GLU A . n 
B 2 98  ASP 98  98  98  ASP ASP A . n 
B 2 99  ALA 99  99  99  ALA ALA A . n 
B 2 100 ALA 100 100 100 ALA ALA A . n 
B 2 101 ASN 101 101 101 ASN ASN A . n 
B 2 102 ASN 102 102 102 ASN ASN A . n 
B 2 103 TYR 103 103 103 TYR TYR A . n 
B 2 104 ALA 104 104 104 ALA ALA A . n 
B 2 105 ARG 105 105 105 ARG ARG A . n 
B 2 106 GLY 106 106 106 GLY GLY A . n 
B 2 107 HIS 107 107 107 HIS HIS A . n 
B 2 108 TYR 108 108 108 TYR TYR A . n 
B 2 109 THR 109 109 109 THR THR A . n 
B 2 110 ILE 110 110 110 ILE ILE A . n 
B 2 111 GLY 111 111 111 GLY GLY A . n 
B 2 112 LYS 112 112 112 LYS LYS A . n 
B 2 113 GLU 113 113 113 GLU GLU A . n 
B 2 114 ILE 114 114 114 ILE ILE A . n 
B 2 115 ILE 115 115 115 ILE ILE A . n 
B 2 116 ASP 116 116 116 ASP ASP A . n 
B 2 117 LEU 117 117 117 LEU LEU A . n 
B 2 118 VAL 118 118 118 VAL VAL A . n 
B 2 119 LEU 119 119 119 LEU LEU A . n 
B 2 120 ASP 120 120 120 ASP ASP A . n 
B 2 121 ARG 121 121 121 ARG ARG A . n 
B 2 122 ILE 122 122 122 ILE ILE A . n 
B 2 123 ARG 123 123 123 ARG ARG A . n 
B 2 124 LYS 124 124 124 LYS LYS A . n 
B 2 125 LEU 125 125 125 LEU LEU A . n 
B 2 126 ALA 126 126 126 ALA ALA A . n 
B 2 127 ASP 127 127 127 ASP ASP A . n 
B 2 128 GLN 128 128 128 GLN GLN A . n 
B 2 129 CYS 129 129 129 CYS CYS A . n 
B 2 130 THR 130 130 130 THR THR A . n 
B 2 131 GLY 131 131 131 GLY GLY A . n 
B 2 132 LEU 132 132 132 LEU LEU A . n 
B 2 133 GLN 133 133 133 GLN GLN A . n 
B 2 134 GLY 134 134 134 GLY GLY A . n 
B 2 135 PHE 135 135 135 PHE PHE A . n 
B 2 136 LEU 136 136 136 LEU LEU A . n 
B 2 137 VAL 137 137 137 VAL VAL A . n 
B 2 138 PHE 138 138 138 PHE PHE A . n 
B 2 139 HIS 139 139 139 HIS HIS A . n 
B 2 140 SER 140 140 140 SER SER A . n 
B 2 141 PHE 141 141 141 PHE PHE A . n 
B 2 142 GLY 142 142 142 GLY GLY A . n 
B 2 143 GLY 143 143 143 GLY GLY A . n 
B 2 144 GLY 144 144 144 GLY GLY A . n 
B 2 145 THR 145 145 145 THR THR A . n 
B 2 146 GLY 146 146 146 GLY GLY A . n 
B 2 147 SER 147 147 147 SER SER A . n 
B 2 148 GLY 148 148 148 GLY GLY A . n 
B 2 149 PHE 149 149 149 PHE PHE A . n 
B 2 150 THR 150 150 150 THR THR A . n 
B 2 151 SER 151 151 151 SER SER A . n 
B 2 152 LEU 152 152 152 LEU LEU A . n 
B 2 153 LEU 153 153 153 LEU LEU A . n 
B 2 154 MET 154 154 154 MET MET A . n 
B 2 155 GLU 155 155 155 GLU GLU A . n 
B 2 156 ARG 156 156 156 ARG ARG A . n 
B 2 157 LEU 157 157 157 LEU LEU A . n 
B 2 158 SER 158 158 158 SER SER A . n 
B 2 159 VAL 159 159 159 VAL VAL A . n 
B 2 160 ASP 160 160 160 ASP ASP A . n 
B 2 161 TYR 161 161 161 TYR TYR A . n 
B 2 162 GLY 162 162 162 GLY GLY A . n 
B 2 163 LYS 163 163 163 LYS LYS A . n 
B 2 164 LYS 164 164 164 LYS LYS A . n 
B 2 165 SER 165 165 165 SER SER A . n 
B 2 166 LYS 166 166 166 LYS LYS A . n 
B 2 167 LEU 167 167 167 LEU LEU A . n 
B 2 168 GLU 168 168 168 GLU GLU A . n 
B 2 169 PHE 169 169 169 PHE PHE A . n 
B 2 170 SER 170 170 170 SER SER A . n 
B 2 171 ILE 171 171 171 ILE ILE A . n 
B 2 172 TYR 172 172 172 TYR TYR A . n 
B 2 173 PRO 173 173 173 PRO PRO A . n 
B 2 174 ALA 174 174 174 ALA ALA A . n 
B 2 175 PRO 175 175 175 PRO PRO A . n 
B 2 176 GLN 176 176 176 GLN GLN A . n 
B 2 177 VAL 177 177 177 VAL VAL A . n 
B 2 178 SER 178 178 178 SER SER A . n 
B 2 179 THR 179 179 179 THR THR A . n 
B 2 180 ALA 180 180 180 ALA ALA A . n 
B 2 181 VAL 181 181 181 VAL VAL A . n 
B 2 182 VAL 182 182 182 VAL VAL A . n 
B 2 183 GLU 183 183 183 GLU GLU A . n 
B 2 184 PRO 184 184 184 PRO PRO A . n 
B 2 185 TYR 185 185 185 TYR TYR A . n 
B 2 186 ASN 186 186 186 ASN ASN A . n 
B 2 187 SER 187 187 187 SER SER A . n 
B 2 188 ILE 188 188 188 ILE ILE A . n 
B 2 189 LEU 189 189 189 LEU LEU A . n 
B 2 190 THR 190 190 190 THR THR A . n 
B 2 191 THR 191 191 191 THR THR A . n 
B 2 192 HIS 192 192 192 HIS HIS A . n 
B 2 193 THR 193 193 193 THR THR A . n 
B 2 194 THR 194 194 194 THR THR A . n 
B 2 195 LEU 195 195 195 LEU LEU A . n 
B 2 196 GLU 196 196 196 GLU GLU A . n 
B 2 197 HIS 197 197 197 HIS HIS A . n 
B 2 198 SER 198 198 198 SER SER A . n 
B 2 199 ASP 199 199 199 ASP ASP A . n 
B 2 200 CYS 200 200 200 CYS CYS A . n 
B 2 201 ALA 201 201 201 ALA ALA A . n 
B 2 202 PHE 202 202 202 PHE PHE A . n 
B 2 203 MET 203 203 203 MET MET A . n 
B 2 204 VAL 204 204 204 VAL VAL A . n 
B 2 205 ASP 205 205 205 ASP ASP A . n 
B 2 206 ASN 206 206 206 ASN ASN A . n 
B 2 207 GLU 207 207 207 GLU GLU A . n 
B 2 208 ALA 208 208 208 ALA ALA A . n 
B 2 209 ILE 209 209 209 ILE ILE A . n 
B 2 210 TYR 210 210 210 TYR TYR A . n 
B 2 211 ASP 211 211 211 ASP ASP A . n 
B 2 212 ILE 212 212 212 ILE ILE A . n 
B 2 213 CYS 213 213 213 CYS CYS A . n 
B 2 214 ARG 214 214 214 ARG ARG A . n 
B 2 215 ARG 215 215 215 ARG ARG A . n 
B 2 216 ASN 216 216 216 ASN ASN A . n 
B 2 217 LEU 217 217 217 LEU LEU A . n 
B 2 218 ASP 218 218 218 ASP ASP A . n 
B 2 219 ILE 219 219 219 ILE ILE A . n 
B 2 220 GLU 220 220 220 GLU GLU A . n 
B 2 221 ARG 221 221 221 ARG ARG A . n 
B 2 222 PRO 222 222 222 PRO PRO A . n 
B 2 223 THR 223 223 223 THR THR A . n 
B 2 224 TYR 224 224 224 TYR TYR A . n 
B 2 225 THR 225 225 225 THR THR A . n 
B 2 226 ASN 226 226 226 ASN ASN A . n 
B 2 227 LEU 227 227 227 LEU LEU A . n 
B 2 228 ASN 228 228 228 ASN ASN A . n 
B 2 229 ARG 229 229 229 ARG ARG A . n 
B 2 230 LEU 230 230 230 LEU LEU A . n 
B 2 231 ILE 231 231 231 ILE ILE A . n 
B 2 232 SER 232 232 232 SER SER A . n 
B 2 233 GLN 233 233 233 GLN GLN A . n 
B 2 234 ILE 234 234 234 ILE ILE A . n 
B 2 235 VAL 235 235 235 VAL VAL A . n 
B 2 236 SER 236 236 236 SER SER A . n 
B 2 237 SER 237 237 237 SER SER A . n 
B 2 238 ILE 238 238 238 ILE ILE A . n 
B 2 239 THR 239 239 239 THR THR A . n 
B 2 240 ALA 240 240 240 ALA ALA A . n 
B 2 241 SER 241 241 241 SER SER A . n 
B 2 242 LEU 242 242 242 LEU LEU A . n 
B 2 243 ARG 243 243 243 ARG ARG A . n 
B 2 244 PHE 244 244 244 PHE PHE A . n 
B 2 245 ASP 245 245 245 ASP ASP A . n 
B 2 246 GLY 246 246 246 GLY GLY A . n 
B 2 247 ALA 247 247 247 ALA ALA A . n 
B 2 248 LEU 248 248 248 LEU LEU A . n 
B 2 249 ASN 249 249 249 ASN ASN A . n 
B 2 250 VAL 250 250 250 VAL VAL A . n 
B 2 251 ASP 251 251 251 ASP ASP A . n 
B 2 252 LEU 252 252 252 LEU LEU A . n 
B 2 253 THR 253 253 253 THR THR A . n 
B 2 254 GLU 254 254 254 GLU GLU A . n 
B 2 255 PHE 255 255 255 PHE PHE A . n 
B 2 256 GLN 256 256 256 GLN GLN A . n 
B 2 257 THR 257 257 257 THR THR A . n 
B 2 258 ASN 258 258 258 ASN ASN A . n 
B 2 259 LEU 259 259 259 LEU LEU A . n 
B 2 260 VAL 260 260 260 VAL VAL A . n 
B 2 261 PRO 261 261 261 PRO PRO A . n 
B 2 262 TYR 262 262 262 TYR TYR A . n 
B 2 263 PRO 263 263 263 PRO PRO A . n 
B 2 264 ARG 264 264 264 ARG ARG A . n 
B 2 265 ILE 265 265 265 ILE ILE A . n 
B 2 266 HIS 266 266 266 HIS HIS A . n 
B 2 267 PHE 267 267 267 PHE PHE A . n 
B 2 268 PRO 268 268 268 PRO PRO A . n 
B 2 269 LEU 269 269 269 LEU LEU A . n 
B 2 270 ALA 270 270 270 ALA ALA A . n 
B 2 271 THR 271 271 271 THR THR A . n 
B 2 272 TYR 272 272 272 TYR TYR A . n 
B 2 273 ALA 273 273 273 ALA ALA A . n 
B 2 274 PRO 274 274 274 PRO PRO A . n 
B 2 275 VAL 275 275 275 VAL VAL A . n 
B 2 276 ILE 276 276 276 ILE ILE A . n 
B 2 277 SER 277 277 277 SER SER A . n 
B 2 278 ALA 278 278 278 ALA ALA A . n 
B 2 279 GLU 279 279 279 GLU GLU A . n 
B 2 280 LYS 280 280 280 LYS LYS A . n 
B 2 281 ALA 281 281 281 ALA ALA A . n 
B 2 282 TYR 282 282 282 TYR TYR A . n 
B 2 283 HIS 283 283 283 HIS HIS A . n 
B 2 284 GLU 284 284 284 GLU GLU A . n 
B 2 285 GLN 285 285 285 GLN GLN A . n 
B 2 286 LEU 286 286 286 LEU LEU A . n 
B 2 287 SER 287 287 287 SER SER A . n 
B 2 288 VAL 288 288 288 VAL VAL A . n 
B 2 289 ALA 289 289 289 ALA ALA A . n 
B 2 290 GLU 290 290 290 GLU GLU A . n 
B 2 291 ILE 291 291 291 ILE ILE A . n 
B 2 292 THR 292 292 292 THR THR A . n 
B 2 293 ASN 293 293 293 ASN ASN A . n 
B 2 294 ALA 294 294 294 ALA ALA A . n 
B 2 295 CYS 295 295 295 CYS CYS A . n 
B 2 296 PHE 296 296 296 PHE PHE A . n 
B 2 297 GLU 297 297 297 GLU GLU A . n 
B 2 298 PRO 298 298 298 PRO PRO A . n 
B 2 299 ALA 299 299 299 ALA ALA A . n 
B 2 300 ASN 300 300 300 ASN ASN A . n 
B 2 301 GLN 301 301 301 GLN GLN A . n 
B 2 302 MET 302 302 302 MET MET A . n 
B 2 303 VAL 303 303 303 VAL VAL A . n 
B 2 304 LYS 304 304 304 LYS LYS A . n 
B 2 305 CYS 305 305 305 CYS CYS A . n 
B 2 306 ASP 306 306 306 ASP ASP A . n 
B 2 307 PRO 307 307 307 PRO PRO A . n 
B 2 308 ARG 308 308 308 ARG ARG A . n 
B 2 309 HIS 309 309 309 HIS HIS A . n 
B 2 310 GLY 310 310 310 GLY GLY A . n 
B 2 311 LYS 311 311 311 LYS LYS A . n 
B 2 312 TYR 312 312 312 TYR TYR A . n 
B 2 313 MET 313 313 313 MET MET A . n 
B 2 314 ALA 314 314 314 ALA ALA A . n 
B 2 315 CYS 315 315 315 CYS CYS A . n 
B 2 316 CYS 316 316 316 CYS CYS A . n 
B 2 317 LEU 317 317 317 LEU LEU A . n 
B 2 318 LEU 318 318 318 LEU LEU A . n 
B 2 319 TYR 319 319 319 TYR TYR A . n 
B 2 320 ARG 320 320 320 ARG ARG A . n 
B 2 321 GLY 321 321 321 GLY GLY A . n 
B 2 322 ASP 322 322 322 ASP ASP A . n 
B 2 323 VAL 323 323 323 VAL VAL A . n 
B 2 324 VAL 324 324 324 VAL VAL A . n 
B 2 325 PRO 325 325 325 PRO PRO A . n 
B 2 326 LYS 326 326 326 LYS LYS A . n 
B 2 327 ASP 327 327 327 ASP ASP A . n 
B 2 328 VAL 328 328 328 VAL VAL A . n 
B 2 329 ASN 329 329 329 ASN ASN A . n 
B 2 330 ALA 330 330 330 ALA ALA A . n 
B 2 331 ALA 331 331 331 ALA ALA A . n 
B 2 332 ILE 332 332 332 ILE ILE A . n 
B 2 333 ALA 333 333 333 ALA ALA A . n 
B 2 334 THR 334 334 334 THR THR A . n 
B 2 335 ILE 335 335 335 ILE ILE A . n 
B 2 336 LYS 336 336 336 LYS LYS A . n 
B 2 337 THR 337 337 337 THR THR A . n 
B 2 338 LYS 338 338 338 LYS LYS A . n 
B 2 339 ARG 339 339 339 ARG ARG A . n 
B 2 340 SER 340 340 340 SER SER A . n 
B 2 341 ILE 341 341 341 ILE ILE A . n 
B 2 342 GLN 342 342 342 GLN GLN A . n 
B 2 343 PHE 343 343 343 PHE PHE A . n 
B 2 344 VAL 344 344 344 VAL VAL A . n 
B 2 345 ASP 345 345 345 ASP ASP A . n 
B 2 346 TRP 346 346 346 TRP TRP A . n 
B 2 347 CYS 347 347 347 CYS CYS A . n 
B 2 348 PRO 348 348 348 PRO PRO A . n 
B 2 349 THR 349 349 349 THR THR A . n 
B 2 350 GLY 350 350 350 GLY GLY A . n 
B 2 351 PHE 351 351 351 PHE PHE A . n 
B 2 352 LYS 352 352 352 LYS LYS A . n 
B 2 353 VAL 353 353 353 VAL VAL A . n 
B 2 354 GLY 354 354 354 GLY GLY A . n 
B 2 355 ILE 355 355 355 ILE ILE A . n 
B 2 356 ASN 356 356 356 ASN ASN A . n 
B 2 357 TYR 357 357 357 TYR TYR A . n 
B 2 358 GLN 358 358 358 GLN GLN A . n 
B 2 359 PRO 359 359 359 PRO PRO A . n 
B 2 360 PRO 360 360 360 PRO PRO A . n 
B 2 361 THR 361 361 361 THR THR A . n 
B 2 362 VAL 362 362 362 VAL VAL A . n 
B 2 363 VAL 363 363 363 VAL VAL A . n 
B 2 364 PRO 364 364 364 PRO PRO A . n 
B 2 365 GLY 365 365 365 GLY GLY A . n 
B 2 366 GLY 366 366 366 GLY GLY A . n 
B 2 367 ASP 367 367 367 ASP ASP A . n 
B 2 368 LEU 368 368 368 LEU LEU A . n 
B 2 369 ALA 369 369 369 ALA ALA A . n 
B 2 370 LYS 370 370 370 LYS LYS A . n 
B 2 371 VAL 371 371 371 VAL VAL A . n 
B 2 372 GLN 372 372 372 GLN GLN A . n 
B 2 373 ARG 373 373 373 ARG ARG A . n 
B 2 374 ALA 374 374 374 ALA ALA A . n 
B 2 375 VAL 375 375 375 VAL VAL A . n 
B 2 376 CYS 376 376 376 CYS CYS A . n 
B 2 377 MET 377 377 377 MET MET A . n 
B 2 378 LEU 378 378 378 LEU LEU A . n 
B 2 379 SER 379 379 379 SER SER A . n 
B 2 380 ASN 380 380 380 ASN ASN A . n 
B 2 381 THR 381 381 381 THR THR A . n 
B 2 382 THR 382 382 382 THR THR A . n 
B 2 383 ALA 383 383 383 ALA ALA A . n 
B 2 384 ILE 384 384 384 ILE ILE A . n 
B 2 385 ALA 385 385 385 ALA ALA A . n 
B 2 386 GLU 386 386 386 GLU GLU A . n 
B 2 387 ALA 387 387 387 ALA ALA A . n 
B 2 388 TRP 388 388 388 TRP TRP A . n 
B 2 389 ALA 389 389 389 ALA ALA A . n 
B 2 390 ARG 390 390 390 ARG ARG A . n 
B 2 391 LEU 391 391 391 LEU LEU A . n 
B 2 392 ASP 392 392 392 ASP ASP A . n 
B 2 393 HIS 393 393 393 HIS HIS A . n 
B 2 394 LYS 394 394 394 LYS LYS A . n 
B 2 395 PHE 395 395 395 PHE PHE A . n 
B 2 396 ASP 396 396 396 ASP ASP A . n 
B 2 397 LEU 397 397 397 LEU LEU A . n 
B 2 398 MET 398 398 398 MET MET A . n 
B 2 399 TYR 399 399 399 TYR TYR A . n 
B 2 400 ALA 400 400 400 ALA ALA A . n 
B 2 401 LYS 401 401 401 LYS LYS A . n 
B 2 402 ARG 402 402 402 ARG ARG A . n 
B 2 403 ALA 403 403 403 ALA ALA A . n 
B 2 404 PHE 404 404 404 PHE PHE A . n 
B 2 405 VAL 405 405 405 VAL VAL A . n 
B 2 406 HIS 406 406 406 HIS HIS A . n 
B 2 407 TRP 407 407 407 TRP TRP A . n 
B 2 408 TYR 408 408 408 TYR TYR A . n 
B 2 409 VAL 409 409 409 VAL VAL A . n 
B 2 410 GLY 410 410 410 GLY GLY A . n 
B 2 411 GLU 411 411 411 GLU GLU A . n 
B 2 412 GLY 412 412 412 GLY GLY A . n 
B 2 413 MET 413 413 413 MET MET A . n 
B 2 414 GLU 414 414 414 GLU GLU A . n 
B 2 415 GLU 415 415 415 GLU GLU A . n 
B 2 416 GLY 416 416 416 GLY GLY A . n 
B 2 417 GLU 417 417 417 GLU GLU A . n 
B 2 418 PHE 418 418 418 PHE PHE A . n 
B 2 419 SER 419 419 419 SER SER A . n 
B 2 420 GLU 420 420 420 GLU GLU A . n 
B 2 421 ALA 421 421 421 ALA ALA A . n 
B 2 422 ARG 422 422 422 ARG ARG A . n 
B 2 423 GLU 423 423 423 GLU GLU A . n 
B 2 424 ASP 424 424 424 ASP ASP A . n 
B 2 425 MET 425 425 425 MET MET A . n 
B 2 426 ALA 426 426 426 ALA ALA A . n 
B 2 427 ALA 427 427 427 ALA ALA A . n 
B 2 428 LEU 428 428 428 LEU LEU A . n 
B 2 429 GLU 429 429 429 GLU GLU A . n 
B 2 430 LYS 430 430 430 LYS LYS A . n 
B 2 431 ASP 431 431 431 ASP ASP A . n 
B 2 432 TYR 432 432 432 TYR TYR A . n 
B 2 433 GLU 433 433 433 GLU GLU A . n 
B 2 434 GLU 434 434 434 GLU GLU A . n 
B 2 435 VAL 435 435 435 VAL VAL A . n 
B 2 436 GLY 436 436 436 GLY GLY A . n 
B 2 437 VAL 437 437 437 VAL VAL A . n 
B 2 438 ASP 438 438 ?   ?   ?   A . n 
B 2 439 SER 439 439 ?   ?   ?   A . n 
B 2 440 VAL 440 440 ?   ?   ?   A . n 
B 2 441 GLU 441 441 ?   ?   ?   A . n 
B 2 442 GLY 442 442 ?   ?   ?   A . n 
B 2 443 GLU 443 443 ?   ?   ?   A . n 
B 2 444 GLY 444 444 ?   ?   ?   A . n 
B 2 445 GLU 445 445 ?   ?   ?   A . n 
B 2 446 GLU 446 446 ?   ?   ?   A . n 
B 2 447 GLU 447 447 ?   ?   ?   A . n 
B 2 448 GLY 448 448 ?   ?   ?   A . n 
B 2 449 GLU 449 449 ?   ?   ?   A . n 
B 2 450 GLU 450 450 ?   ?   ?   A . n 
B 2 451 TYR 451 451 ?   ?   ?   A . n 
C 3 1   MET 1   1   ?   ?   ?   K . n 
C 3 2   ALA 2   2   ?   ?   ?   K . n 
C 3 3   ASP 3   3   ?   ?   ?   K . n 
C 3 4   LEU 4   4   ?   ?   ?   K . n 
C 3 5   ALA 5   5   ?   ?   ?   K . n 
C 3 6   GLU 6   6   ?   ?   ?   K . n 
C 3 7   CYS 7   7   ?   ?   ?   K . n 
C 3 8   ASN 8   8   8   ASN ASN K . n 
C 3 9   ILE 9   9   9   ILE ILE K . n 
C 3 10  LYS 10  10  10  LYS LYS K . n 
C 3 11  VAL 11  11  11  VAL VAL K . n 
C 3 12  MET 12  12  12  MET MET K . n 
C 3 13  CYS 13  13  13  CYS CYS K . n 
C 3 14  ARG 14  14  14  ARG ARG K . n 
C 3 15  PHE 15  15  15  PHE PHE K . n 
C 3 16  ARG 16  16  16  ARG ARG K . n 
C 3 17  PRO 17  17  17  PRO PRO K . n 
C 3 18  LEU 18  18  18  LEU LEU K . n 
C 3 19  ASN 19  19  19  ASN ASN K . n 
C 3 20  GLU 20  20  20  GLU GLU K . n 
C 3 21  SER 21  21  21  SER SER K . n 
C 3 22  GLU 22  22  22  GLU GLU K . n 
C 3 23  VAL 23  23  23  VAL VAL K . n 
C 3 24  ASN 24  24  24  ASN ASN K . n 
C 3 25  ARG 25  25  25  ARG ARG K . n 
C 3 26  GLY 26  26  26  GLY GLY K . n 
C 3 27  ASP 27  27  27  ASP ASP K . n 
C 3 28  LYS 28  28  28  LYS LYS K . n 
C 3 29  TYR 29  29  29  TYR TYR K . n 
C 3 30  ILE 30  30  30  ILE ILE K . n 
C 3 31  ALA 31  31  31  ALA ALA K . n 
C 3 32  LYS 32  32  32  LYS LYS K . n 
C 3 33  PHE 33  33  33  PHE PHE K . n 
C 3 34  GLN 34  34  34  GLN GLN K . n 
C 3 35  GLY 35  35  35  GLY GLY K . n 
C 3 36  GLU 36  36  36  GLU GLU K . n 
C 3 37  ASP 37  37  37  ASP ASP K . n 
C 3 38  THR 38  38  38  THR THR K . n 
C 3 39  VAL 39  39  39  VAL VAL K . n 
C 3 40  VAL 40  40  40  VAL VAL K . n 
C 3 41  ILE 41  41  41  ILE ILE K . n 
C 3 42  ALA 42  42  42  ALA ALA K . n 
C 3 43  SER 43  43  43  SER SER K . n 
C 3 44  LYS 44  44  44  LYS LYS K . n 
C 3 45  PRO 45  45  45  PRO PRO K . n 
C 3 46  TYR 46  46  46  TYR TYR K . n 
C 3 47  ALA 47  47  47  ALA ALA K . n 
C 3 48  PHE 48  48  48  PHE PHE K . n 
C 3 49  ASP 49  49  49  ASP ASP K . n 
C 3 50  ARG 50  50  50  ARG ARG K . n 
C 3 51  VAL 51  51  51  VAL VAL K . n 
C 3 52  PHE 52  52  52  PHE PHE K . n 
C 3 53  GLN 53  53  53  GLN GLN K . n 
C 3 54  SER 54  54  54  SER SER K . n 
C 3 55  SER 55  55  55  SER SER K . n 
C 3 56  THR 56  56  56  THR THR K . n 
C 3 57  SER 57  57  57  SER SER K . n 
C 3 58  GLN 58  58  58  GLN GLN K . n 
C 3 59  GLU 59  59  59  GLU GLU K . n 
C 3 60  GLN 60  60  60  GLN GLN K . n 
C 3 61  VAL 61  61  61  VAL VAL K . n 
C 3 62  TYR 62  62  62  TYR TYR K . n 
C 3 63  ASN 63  63  63  ASN ASN K . n 
C 3 64  ASP 64  64  64  ASP ASP K . n 
C 3 65  CYS 65  65  65  CYS ALA K . n 
C 3 66  ALA 66  66  66  ALA ALA K . n 
C 3 67  LYS 67  67  67  LYS LYS K . n 
C 3 68  LYS 68  68  68  LYS LYS K . n 
C 3 69  ILE 69  69  69  ILE ILE K . n 
C 3 70  VAL 70  70  70  VAL VAL K . n 
C 3 71  LYS 71  71  71  LYS LYS K . n 
C 3 72  ASP 72  72  72  ASP ASP K . n 
C 3 73  VAL 73  73  73  VAL VAL K . n 
C 3 74  LEU 74  74  74  LEU LEU K . n 
C 3 75  GLU 75  75  75  GLU GLU K . n 
C 3 76  GLY 76  76  76  GLY GLY K . n 
C 3 77  TYR 77  77  77  TYR TYR K . n 
C 3 78  ASN 78  78  78  ASN ASN K . n 
C 3 79  GLY 79  79  79  GLY GLY K . n 
C 3 80  THR 80  80  80  THR THR K . n 
C 3 81  ILE 81  81  81  ILE ILE K . n 
C 3 82  PHE 82  82  82  PHE PHE K . n 
C 3 83  ALA 83  83  83  ALA ALA K . n 
C 3 84  TYR 84  84  84  TYR TYR K . n 
C 3 85  GLY 85  85  85  GLY GLY K . n 
C 3 86  GLN 86  86  86  GLN GLN K . n 
C 3 87  THR 87  87  87  THR THR K . n 
C 3 88  SER 88  88  88  SER SER K . n 
C 3 89  SER 89  89  89  SER SER K . n 
C 3 90  GLY 90  90  90  GLY GLY K . n 
C 3 91  LYS 91  91  91  LYS LYS K . n 
C 3 92  THR 92  92  92  THR THR K . n 
C 3 93  HIS 93  93  93  HIS HIS K . n 
C 3 94  THR 94  94  94  THR THR K . n 
C 3 95  MET 95  95  95  MET MET K . n 
C 3 96  GLU 96  96  96  GLU GLU K . n 
C 3 97  GLY 97  97  97  GLY GLY K . n 
C 3 98  LYS 98  98  98  LYS LYS K . n 
C 3 99  LEU 99  99  99  LEU LEU K . n 
C 3 100 HIS 100 100 100 HIS HIS K . n 
C 3 101 ASP 101 101 101 ASP ASP K . n 
C 3 102 PRO 102 102 102 PRO PRO K . n 
C 3 103 GLU 103 103 103 GLU GLU K . n 
C 3 104 GLY 104 104 104 GLY GLY K . n 
C 3 105 MET 105 105 105 MET MET K . n 
C 3 106 GLY 106 106 106 GLY GLY K . n 
C 3 107 ILE 107 107 107 ILE ILE K . n 
C 3 108 ILE 108 108 108 ILE ILE K . n 
C 3 109 PRO 109 109 109 PRO PRO K . n 
C 3 110 ARG 110 110 110 ARG ARG K . n 
C 3 111 ILE 111 111 111 ILE ILE K . n 
C 3 112 VAL 112 112 112 VAL VAL K . n 
C 3 113 GLN 113 113 113 GLN GLN K . n 
C 3 114 ASP 114 114 114 ASP ASP K . n 
C 3 115 ILE 115 115 115 ILE ILE K . n 
C 3 116 PHE 116 116 116 PHE PHE K . n 
C 3 117 ASN 117 117 117 ASN ASN K . n 
C 3 118 TYR 118 118 118 TYR TYR K . n 
C 3 119 ILE 119 119 119 ILE ILE K . n 
C 3 120 TYR 120 120 120 TYR TYR K . n 
C 3 121 SER 121 121 121 SER SER K . n 
C 3 122 MET 122 122 122 MET MET K . n 
C 3 123 ASP 123 123 123 ASP ASP K . n 
C 3 124 GLU 124 124 124 GLU GLU K . n 
C 3 125 ASN 125 125 125 ASN ASN K . n 
C 3 126 LEU 126 126 126 LEU LEU K . n 
C 3 127 GLU 127 127 127 GLU GLU K . n 
C 3 128 PHE 128 128 128 PHE PHE K . n 
C 3 129 HIS 129 129 129 HIS HIS K . n 
C 3 130 ILE 130 130 130 ILE ILE K . n 
C 3 131 LYS 131 131 131 LYS LYS K . n 
C 3 132 VAL 132 132 132 VAL VAL K . n 
C 3 133 SER 133 133 133 SER SER K . n 
C 3 134 TYR 134 134 134 TYR TYR K . n 
C 3 135 PHE 135 135 135 PHE PHE K . n 
C 3 136 GLU 136 136 136 GLU GLU K . n 
C 3 137 ILE 137 137 137 ILE ILE K . n 
C 3 138 TYR 138 138 138 TYR TYR K . n 
C 3 139 LEU 139 139 139 LEU LEU K . n 
C 3 140 ASP 140 140 140 ASP ASP K . n 
C 3 141 LYS 141 141 141 LYS LYS K . n 
C 3 142 ILE 142 142 142 ILE ILE K . n 
C 3 143 ARG 143 143 143 ARG ARG K . n 
C 3 144 ASP 144 144 144 ASP ASP K . n 
C 3 145 LEU 145 145 145 LEU LEU K . n 
C 3 146 LEU 146 146 146 LEU LEU K . n 
C 3 147 ASP 147 147 147 ASP ASP K . n 
C 3 148 VAL 148 148 148 VAL VAL K . n 
C 3 149 SER 149 149 149 SER SER K . n 
C 3 150 LYS 150 150 150 LYS LYS K . n 
C 3 151 THR 151 151 151 THR THR K . n 
C 3 152 ASN 152 152 152 ASN ASN K . n 
C 3 153 LEU 153 153 153 LEU LEU K . n 
C 3 154 SER 154 154 154 SER SER K . n 
C 3 155 VAL 155 155 155 VAL VAL K . n 
C 3 156 HIS 156 156 156 HIS HIS K . n 
C 3 157 GLU 157 157 157 GLU GLU K . n 
C 3 158 ASP 158 158 158 ASP ASP K . n 
C 3 159 LYS 159 159 159 LYS LYS K . n 
C 3 160 ASN 160 160 160 ASN ASN K . n 
C 3 161 ARG 161 161 161 ARG ARG K . n 
C 3 162 VAL 162 162 162 VAL VAL K . n 
C 3 163 PRO 163 163 163 PRO PRO K . n 
C 3 164 TYR 164 164 164 TYR TYR K . n 
C 3 165 VAL 165 165 165 VAL VAL K . n 
C 3 166 LYS 166 166 166 LYS LYS K . n 
C 3 167 GLY 167 167 167 GLY GLY K . n 
C 3 168 CYS 168 168 168 CYS CYS K . n 
C 3 169 THR 169 169 169 THR THR K . n 
C 3 170 GLU 170 170 170 GLU GLU K . n 
C 3 171 ARG 171 171 171 ARG ARG K . n 
C 3 172 PHE 172 172 172 PHE PHE K . n 
C 3 173 VAL 173 173 173 VAL VAL K . n 
C 3 174 CYS 174 174 174 CYS CYS K . n 
C 3 175 SER 175 175 175 SER SER K . n 
C 3 176 PRO 176 176 176 PRO PRO K . n 
C 3 177 ASP 177 177 177 ASP ASP K . n 
C 3 178 GLU 178 178 178 GLU GLU K . n 
C 3 179 VAL 179 179 179 VAL VAL K . n 
C 3 180 MET 180 180 180 MET MET K . n 
C 3 181 ASP 181 181 181 ASP ASP K . n 
C 3 182 THR 182 182 182 THR THR K . n 
C 3 183 ILE 183 183 183 ILE ILE K . n 
C 3 184 ASP 184 184 184 ASP ASP K . n 
C 3 185 GLU 185 185 185 GLU GLU K . n 
C 3 186 GLY 186 186 186 GLY GLY K . n 
C 3 187 LYS 187 187 187 LYS LYS K . n 
C 3 188 SER 188 188 188 SER SER K . n 
C 3 189 ASN 189 189 189 ASN ASN K . n 
C 3 190 ARG 190 190 190 ARG ARG K . n 
C 3 191 HIS 191 191 191 HIS HIS K . n 
C 3 192 VAL 192 192 192 VAL VAL K . n 
C 3 193 ALA 193 193 193 ALA ALA K . n 
C 3 194 VAL 194 194 194 VAL VAL K . n 
C 3 195 THR 195 195 ?   ?   ?   K . n 
C 3 196 ASN 196 196 ?   ?   ?   K . n 
C 3 197 MET 197 197 ?   ?   ?   K . n 
C 3 198 ASN 198 198 ?   ?   ?   K . n 
C 3 199 GLU 199 199 199 GLU GLU K . n 
C 3 200 HIS 200 200 200 HIS HIS K . n 
C 3 201 SER 201 201 201 SER SER K . n 
C 3 202 SER 202 202 202 SER SER K . n 
C 3 203 ARG 203 203 203 ARG ARG K . n 
C 3 204 SER 204 204 204 SER SER K . n 
C 3 205 HIS 205 205 205 HIS HIS K . n 
C 3 206 SER 206 206 206 SER SER K . n 
C 3 207 ILE 207 207 207 ILE ILE K . n 
C 3 208 PHE 208 208 208 PHE PHE K . n 
C 3 209 LEU 209 209 209 LEU LEU K . n 
C 3 210 ILE 210 210 210 ILE ILE K . n 
C 3 211 ASN 211 211 211 ASN ASN K . n 
C 3 212 VAL 212 212 212 VAL VAL K . n 
C 3 213 LYS 213 213 213 LYS LYS K . n 
C 3 214 GLN 214 214 214 GLN GLN K . n 
C 3 215 GLU 215 215 215 GLU GLU K . n 
C 3 216 ASN 216 216 216 ASN ASN K . n 
C 3 217 THR 217 217 217 THR THR K . n 
C 3 218 GLN 218 218 218 GLN GLN K . n 
C 3 219 THR 219 219 219 THR THR K . n 
C 3 220 GLU 220 220 220 GLU GLU K . n 
C 3 221 GLN 221 221 221 GLN GLN K . n 
C 3 222 LYS 222 222 222 LYS LYS K . n 
C 3 223 LEU 223 223 223 LEU LEU K . n 
C 3 224 SER 224 224 224 SER SER K . n 
C 3 225 GLY 225 225 225 GLY GLY K . n 
C 3 226 LYS 226 226 226 LYS LYS K . n 
C 3 227 LEU 227 227 227 LEU LEU K . n 
C 3 228 TYR 228 228 228 TYR TYR K . n 
C 3 229 LEU 229 229 229 LEU LEU K . n 
C 3 230 VAL 230 230 230 VAL VAL K . n 
C 3 231 ASP 231 231 231 ASP ASP K . n 
C 3 232 LEU 232 232 232 LEU LEU K . n 
C 3 233 ALA 233 233 233 ALA ALA K . n 
C 3 234 GLY 234 234 234 GLY GLY K . n 
C 3 235 SER 235 235 235 SER SER K . n 
C 3 236 GLU 236 236 236 GLU GLU K . n 
C 3 237 LYS 237 237 237 LYS LYS K . n 
C 3 238 VAL 238 238 238 VAL VAL K . n 
C 3 239 SER 239 239 239 SER SER K . n 
C 3 240 LYS 240 240 240 LYS LYS K . n 
C 3 241 THR 241 241 241 THR THR K . n 
C 3 242 GLY 242 242 242 GLY GLY K . n 
C 3 243 ALA 243 243 243 ALA ALA K . n 
C 3 244 GLU 244 244 244 GLU GLU K . n 
C 3 245 GLY 245 245 245 GLY GLY K . n 
C 3 246 ALA 246 246 246 ALA ALA K . n 
C 3 247 VAL 247 247 247 VAL VAL K . n 
C 3 248 LEU 248 248 248 LEU LEU K . n 
C 3 249 ASP 249 249 249 ASP ASP K . n 
C 3 250 GLU 250 250 250 GLU GLU K . n 
C 3 251 ALA 251 251 251 ALA ALA K . n 
C 3 252 LYS 252 252 252 LYS LYS K . n 
C 3 253 ASN 253 253 253 ASN ASN K . n 
C 3 254 ILE 254 254 254 ILE ILE K . n 
C 3 255 ASN 255 255 255 ASN ASN K . n 
C 3 256 LYS 256 256 256 LYS LYS K . n 
C 3 257 SER 257 257 257 SER SER K . n 
C 3 258 LEU 258 258 258 LEU LEU K . n 
C 3 259 SER 259 259 259 SER SER K . n 
C 3 260 ALA 260 260 260 ALA ALA K . n 
C 3 261 LEU 261 261 261 LEU LEU K . n 
C 3 262 GLY 262 262 262 GLY GLY K . n 
C 3 263 ASN 263 263 263 ASN ASN K . n 
C 3 264 VAL 264 264 264 VAL VAL K . n 
C 3 265 ILE 265 265 265 ILE ILE K . n 
C 3 266 SER 266 266 266 SER SER K . n 
C 3 267 ALA 267 267 267 ALA ALA K . n 
C 3 268 LEU 268 268 268 LEU LEU K . n 
C 3 269 ALA 269 269 269 ALA ALA K . n 
C 3 270 GLU 270 270 270 GLU GLU K . n 
C 3 271 GLY 271 271 271 GLY GLY K . n 
C 3 272 SER 272 272 272 SER SER K . n 
C 3 273 THR 273 273 273 THR THR K . n 
C 3 274 TYR 274 274 274 TYR TYR K . n 
C 3 275 VAL 275 275 275 VAL VAL K . n 
C 3 276 PRO 276 276 276 PRO PRO K . n 
C 3 277 TYR 277 277 277 TYR TYR K . n 
C 3 278 ARG 278 278 278 ARG ARG K . n 
C 3 279 ASP 279 279 279 ASP ASP K . n 
C 3 280 SER 280 280 280 SER SER K . n 
C 3 281 LYS 281 281 281 LYS LYS K . n 
C 3 282 MET 282 282 282 MET MET K . n 
C 3 283 THR 283 283 283 THR THR K . n 
C 3 284 ARG 284 284 284 ARG ARG K . n 
C 3 285 ILE 285 285 285 ILE ILE K . n 
C 3 286 LEU 286 286 286 LEU LEU K . n 
C 3 287 GLN 287 287 287 GLN GLN K . n 
C 3 288 ASP 288 288 288 ASP ASP K . n 
C 3 289 SER 289 289 289 SER SER K . n 
C 3 290 LEU 290 290 290 LEU LEU K . n 
C 3 291 GLY 291 291 291 GLY GLY K . n 
C 3 292 GLY 292 292 292 GLY GLY K . n 
C 3 293 ASN 293 293 293 ASN ASN K . n 
C 3 294 CYS 294 294 294 CYS CYS K . n 
C 3 295 ARG 295 295 295 ARG ARG K . n 
C 3 296 THR 296 296 296 THR THR K . n 
C 3 297 THR 297 297 297 THR THR K . n 
C 3 298 ILE 298 298 298 ILE ILE K . n 
C 3 299 VAL 299 299 299 VAL VAL K . n 
C 3 300 ILE 300 300 300 ILE ILE K . n 
C 3 301 CYS 301 301 301 CYS CYS K . n 
C 3 302 CYS 302 302 302 CYS CYS K . n 
C 3 303 SER 303 303 303 SER SER K . n 
C 3 304 PRO 304 304 304 PRO PRO K . n 
C 3 305 SER 305 305 305 SER SER K . n 
C 3 306 SER 306 306 306 SER SER K . n 
C 3 307 TYR 307 307 307 TYR TYR K . n 
C 3 308 ASN 308 308 308 ASN ASN K . n 
C 3 309 GLU 309 309 309 GLU GLU K . n 
C 3 310 SER 310 310 310 SER SER K . n 
C 3 311 GLU 311 311 311 GLU GLU K . n 
C 3 312 THR 312 312 312 THR THR K . n 
C 3 313 LYS 313 313 313 LYS LYS K . n 
C 3 314 SER 314 314 314 SER SER K . n 
C 3 315 THR 315 315 315 THR THR K . n 
C 3 316 LEU 316 316 316 LEU LEU K . n 
C 3 317 LEU 317 317 317 LEU LEU K . n 
C 3 318 PHE 318 318 318 PHE PHE K . n 
C 3 319 GLY 319 319 319 GLY GLY K . n 
C 3 320 GLN 320 320 320 GLN GLN K . n 
C 3 321 ARG 321 321 321 ARG ARG K . n 
C 3 322 ALA 322 322 322 ALA ALA K . n 
C 3 323 LYS 323 323 323 LYS LYS K . n 
C 3 324 THR 324 324 ?   ?   ?   K . n 
C 3 325 ILE 325 325 ?   ?   ?   K . n 
C 3 326 LYS 326 326 ?   ?   ?   K . n 
C 3 327 ASN 327 327 ?   ?   ?   K . n 
C 3 328 THR 328 328 ?   ?   ?   K . n 
C 3 329 VAL 329 329 ?   ?   ?   K . n 
C 3 330 CYS 330 330 ?   ?   ?   K . n 
C 3 331 VAL 331 331 ?   ?   ?   K . n 
C 3 332 ASN 332 332 ?   ?   ?   K . n 
C 3 333 VAL 333 333 ?   ?   ?   K . n 
C 3 334 GLU 334 334 ?   ?   ?   K . n 
C 3 335 LEU 335 335 ?   ?   ?   K . n 
C 3 336 THR 336 336 ?   ?   ?   K . n 
C 3 337 ALA 337 337 ?   ?   ?   K . n 
C 3 338 GLU 338 338 ?   ?   ?   K . n 
C 3 339 GLN 339 339 ?   ?   ?   K . n 
C 3 340 TRP 340 340 ?   ?   ?   K . n 
C 3 341 LYS 341 341 ?   ?   ?   K . n 
C 3 342 LYS 342 342 ?   ?   ?   K . n 
C 3 343 LYS 343 343 ?   ?   ?   K . n 
C 3 344 TYR 344 344 ?   ?   ?   K . n 
C 3 345 GLU 345 345 ?   ?   ?   K . n 
C 3 346 LYS 346 346 ?   ?   ?   K . n 
C 3 347 GLU 347 347 ?   ?   ?   K . n 
C 3 348 LYS 348 348 ?   ?   ?   K . n 
C 3 349 GLU 349 349 ?   ?   ?   K . n 
C 3 350 LYS 350 350 ?   ?   ?   K . n 
C 3 351 ASN 351 351 ?   ?   ?   K . n 
C 3 352 LYS 352 352 ?   ?   ?   K . n 
C 3 353 ILE 353 353 ?   ?   ?   K . n 
C 3 354 LEU 354 354 ?   ?   ?   K . n 
C 3 355 ARG 355 355 ?   ?   ?   K . n 
C 3 356 ASN 356 356 ?   ?   ?   K . n 
C 3 357 THR 357 357 ?   ?   ?   K . n 
C 3 358 THR 358 358 ?   ?   ?   K . n 
C 3 359 GLY 359 359 ?   ?   ?   K . n 
C 3 360 SER 360 360 ?   ?   ?   K . n 
C 3 361 THR 361 361 ?   ?   ?   K . n 
C 3 362 GLY 362 362 ?   ?   ?   K . n 
C 3 363 SER 363 363 ?   ?   ?   K . n 
C 3 364 THR 364 364 ?   ?   ?   K . n 
C 3 365 GLY 365 365 ?   ?   ?   K . n 
C 3 366 SER 366 366 ?   ?   ?   K . n 
C 3 367 THR 367 367 ?   ?   ?   K . n 
C 3 368 GLY 368 368 ?   ?   ?   K . n 
C 3 369 SER 369 369 ?   ?   ?   K . n 
C 3 370 THR 370 370 ?   ?   ?   K . n 
C 3 371 GLY 371 371 ?   ?   ?   K . n 
C 3 372 SER 372 372 ?   ?   ?   K . n 
C 3 373 THR 373 373 ?   ?   ?   K . n 
C 3 374 GLY 374 374 ?   ?   ?   K . n 
C 3 375 SER 375 375 ?   ?   ?   K . n 
C 3 376 THR 376 376 ?   ?   ?   K . n 
C 3 377 GLY 377 377 ?   ?   ?   K . n 
C 3 378 SER 378 378 ?   ?   ?   K . n 
C 3 379 THR 379 379 ?   ?   ?   K . n 
C 3 380 GLY 380 380 ?   ?   ?   K . n 
C 3 381 SER 381 381 ?   ?   ?   K . n 
C 3 382 THR 382 382 ?   ?   ?   K . n 
C 3 383 GLY 383 383 ?   ?   ?   K . n 
C 3 384 SER 384 384 ?   ?   ?   K . n 
C 3 385 ALA 385 385 ?   ?   ?   K . n 
C 3 386 ARG 386 386 ?   ?   ?   K . n 
C 3 387 ARG 387 387 ?   ?   ?   K . n 
C 3 388 GLY 388 388 ?   ?   ?   K . n 
C 3 389 HIS 389 389 ?   ?   ?   K . n 
C 3 390 SER 390 390 ?   ?   ?   K . n 
C 3 391 ALA 391 391 ?   ?   ?   K . n 
C 3 392 THR 392 392 ?   ?   ?   K . n 
C 3 393 GLY 393 393 ?   ?   ?   K . n 
C 3 394 SER 394 394 ?   ?   ?   K . n 
C 3 395 THR 395 395 ?   ?   ?   K . n 
C 3 396 SER 396 396 ?   ?   ?   K . n 
C 3 397 GLY 397 397 ?   ?   ?   K . n 
C 3 398 THR 398 398 ?   ?   ?   K . n 
C 3 399 PRO 399 399 ?   ?   ?   K . n 
C 3 400 GLY 400 400 ?   ?   ?   K . n 
C 3 401 GLN 401 401 ?   ?   ?   K . n 
C 3 402 HIS 402 402 ?   ?   ?   K . n 
C 3 403 PRO 403 403 ?   ?   ?   K . n 
C 3 404 ALA 404 404 ?   ?   ?   K . n 
C 3 405 ALA 405 405 ?   ?   ?   K . n 
C 3 406 SER 406 406 ?   ?   ?   K . n 
C 3 407 PRO 407 407 ?   ?   ?   K . n 
C 3 408 THR 408 408 ?   ?   ?   K . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 GDP 1 501 501 GDP GDP B . 
E 5 TA1 1 502 502 TA1 TA1 B . 
F 6 GTP 1 501 501 GTP GTP A . 
G 7 MG  1 502 502 MG  MG  A . 
H 8 ADP 1 501 401 ADP ADP K . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     K 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     CYS 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      65 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     SG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    C 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    CYS 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     65 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    SG 
# 
_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                     9GNQ 
_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                         9GNQ 
_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                   9GNQ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9GNQ 
_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' ? 0.005  ? 9510  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.576  ? 12907 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.139 ? 1310  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.046  ? 1418  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 1670  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9GNQ 
_struct.title                        'Microtubule-associated Kif5B IAK tail mutant bound to ADP' 
_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        9GNQ 
_struct_keywords.text            
'Kinesin autoinhibition motor microtubules mechanochemistry intracellular transport, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 8 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP TBB_PIG    P02554 ? 1 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
;
1 
2 UNP TBA1B_PIG  Q2XVP4 ? 2 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
1 
3 UNP KINH_HUMAN P33176 ? 3 
;MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQVYNDCAKKIVKDVLEGYNGT
IFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKN
RVPYVKGCTERFVCSPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVICCSPSSYNESETKSTLLFGQ
RAKTIKNTVCVNVELTAEQWKKKYEKEKEKNKILRNT
;
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 9GNQ B 1 ? 445 ? P02554 1 ? 445 ? 1 455 
2 2 9GNQ A 1 ? 451 ? Q2XVP4 1 ? 451 ? 1 451 
3 3 9GNQ K 1 ? 357 ? P33176 1 ? 357 ? 1 357 
# 
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 
3 9GNQ THR K 358 ? UNP P33176 ? ? 'expression tag' 358 1  
3 9GNQ GLY K 359 ? UNP P33176 ? ? 'expression tag' 359 2  
3 9GNQ SER K 360 ? UNP P33176 ? ? 'expression tag' 360 3  
3 9GNQ THR K 361 ? UNP P33176 ? ? 'expression tag' 361 4  
3 9GNQ GLY K 362 ? UNP P33176 ? ? 'expression tag' 362 5  
3 9GNQ SER K 363 ? UNP P33176 ? ? 'expression tag' 363 6  
3 9GNQ THR K 364 ? UNP P33176 ? ? 'expression tag' 364 7  
3 9GNQ GLY K 365 ? UNP P33176 ? ? 'expression tag' 365 8  
3 9GNQ SER K 366 ? UNP P33176 ? ? 'expression tag' 366 9  
3 9GNQ THR K 367 ? UNP P33176 ? ? 'expression tag' 367 10 
3 9GNQ GLY K 368 ? UNP P33176 ? ? 'expression tag' 368 11 
3 9GNQ SER K 369 ? UNP P33176 ? ? 'expression tag' 369 12 
3 9GNQ THR K 370 ? UNP P33176 ? ? 'expression tag' 370 13 
3 9GNQ GLY K 371 ? UNP P33176 ? ? 'expression tag' 371 14 
3 9GNQ SER K 372 ? UNP P33176 ? ? 'expression tag' 372 15 
3 9GNQ THR K 373 ? UNP P33176 ? ? 'expression tag' 373 16 
3 9GNQ GLY K 374 ? UNP P33176 ? ? 'expression tag' 374 17 
3 9GNQ SER K 375 ? UNP P33176 ? ? 'expression tag' 375 18 
3 9GNQ THR K 376 ? UNP P33176 ? ? 'expression tag' 376 19 
3 9GNQ GLY K 377 ? UNP P33176 ? ? 'expression tag' 377 20 
3 9GNQ SER K 378 ? UNP P33176 ? ? 'expression tag' 378 21 
3 9GNQ THR K 379 ? UNP P33176 ? ? 'expression tag' 379 22 
3 9GNQ GLY K 380 ? UNP P33176 ? ? 'expression tag' 380 23 
3 9GNQ SER K 381 ? UNP P33176 ? ? 'expression tag' 381 24 
3 9GNQ THR K 382 ? UNP P33176 ? ? 'expression tag' 382 25 
3 9GNQ GLY K 383 ? UNP P33176 ? ? 'expression tag' 383 26 
3 9GNQ SER K 384 ? UNP P33176 ? ? 'expression tag' 384 27 
3 9GNQ ALA K 385 ? UNP P33176 ? ? 'expression tag' 385 28 
3 9GNQ ARG K 386 ? UNP P33176 ? ? 'expression tag' 386 29 
3 9GNQ ARG K 387 ? UNP P33176 ? ? 'expression tag' 387 30 
3 9GNQ GLY K 388 ? UNP P33176 ? ? 'expression tag' 388 31 
3 9GNQ HIS K 389 ? UNP P33176 ? ? 'expression tag' 389 32 
3 9GNQ SER K 390 ? UNP P33176 ? ? 'expression tag' 390 33 
3 9GNQ ALA K 391 ? UNP P33176 ? ? 'expression tag' 391 34 
3 9GNQ THR K 392 ? UNP P33176 ? ? 'expression tag' 392 35 
3 9GNQ GLY K 393 ? UNP P33176 ? ? 'expression tag' 393 36 
3 9GNQ SER K 394 ? UNP P33176 ? ? 'expression tag' 394 37 
3 9GNQ THR K 395 ? UNP P33176 ? ? 'expression tag' 395 38 
3 9GNQ SER K 396 ? UNP P33176 ? ? 'expression tag' 396 39 
3 9GNQ GLY K 397 ? UNP P33176 ? ? 'expression tag' 397 40 
3 9GNQ THR K 398 ? UNP P33176 ? ? 'expression tag' 398 41 
3 9GNQ PRO K 399 ? UNP P33176 ? ? 'expression tag' 399 42 
3 9GNQ GLY K 400 ? UNP P33176 ? ? 'expression tag' 400 43 
3 9GNQ GLN K 401 ? UNP P33176 ? ? 'expression tag' 401 44 
3 9GNQ HIS K 402 ? UNP P33176 ? ? 'expression tag' 402 45 
3 9GNQ PRO K 403 ? UNP P33176 ? ? 'expression tag' 403 46 
3 9GNQ ALA K 404 ? UNP P33176 ? ? 'expression tag' 404 47 
3 9GNQ ALA K 405 ? UNP P33176 ? ? 'expression tag' 405 48 
3 9GNQ SER K 406 ? UNP P33176 ? ? 'expression tag' 406 49 
3 9GNQ PRO K 407 ? UNP P33176 ? ? 'expression tag' 407 50 
3 9GNQ THR K 408 ? UNP P33176 ? ? 'expression tag' 408 51 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 GLY A 10  ? GLY A 29  ? GLY B 10  GLY B 29  1 ? 20 
HELX_P HELX_P2  AA2 SER A 40  ? ARG A 46  ? SER B 40  ARG B 48  1 ? 7  
HELX_P HELX_P3  AA3 ILE A 47  ? VAL A 49  ? ILE B 49  VAL B 51  5 ? 3  
HELX_P HELX_P4  AA4 GLU A 69  ? SER A 78  ? GLU B 71  SER B 80  1 ? 10 
HELX_P HELX_P5  AA5 ARG A 86  ? ASP A 88  ? ARG B 88  ASP B 90  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 100 ? THR A 107 ? ASN B 102 THR B 109 1 ? 8  
HELX_P HELX_P7  AA7 LEU A 112 ? GLU A 125 ? LEU B 114 GLU B 127 1 ? 14 
HELX_P HELX_P8  AA8 GLY A 142 ? TYR A 159 ? GLY B 144 TYR B 161 1 ? 18 
HELX_P HELX_P9  AA9 VAL A 180 ? THR A 196 ? VAL B 182 THR B 198 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 203 ? THR A 214 ? ASP B 205 THR B 216 1 ? 12 
HELX_P HELX_P11 AB2 THR A 221 ? THR A 237 ? THR B 223 THR B 239 1 ? 17 
HELX_P HELX_P12 AB3 THR A 238 ? ARG A 241 ? THR B 240 ARG B 243 5 ? 4  
HELX_P HELX_P13 AB4 ASP A 249 ? VAL A 258 ? ASP B 251 VAL B 260 1 ? 10 
HELX_P HELX_P14 AB5 THR A 285 ? PHE A 294 ? THR B 287 PHE B 296 1 ? 10 
HELX_P HELX_P15 AB6 ASP A 295 ? MET A 299 ? ASP B 297 MET B 301 5 ? 5  
HELX_P HELX_P16 AB7 SER A 322 ? ASN A 337 ? SER B 324 ASN B 339 1 ? 16 
HELX_P HELX_P17 AB8 SER A 338 ? PHE A 341 ? SER B 340 PHE B 343 5 ? 4  
HELX_P HELX_P18 AB9 ILE A 374 ? ARG A 391 ? ILE B 384 ARG B 401 1 ? 18 
HELX_P HELX_P19 AC1 LEU A 395 ? GLY A 400 ? LEU B 405 GLY B 410 1 ? 6  
HELX_P HELX_P20 AC2 ASP A 404 ? TYR A 425 ? ASP B 414 TYR B 435 1 ? 22 
HELX_P HELX_P21 AC3 GLY B 10  ? GLY B 29  ? GLY A 10  GLY A 29  1 ? 20 
HELX_P HELX_P22 AC4 THR B 73  ? THR B 80  ? THR A 73  THR A 80  1 ? 8  
HELX_P HELX_P23 AC5 ASN B 102 ? TYR B 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P24 AC6 ILE B 114 ? GLN B 128 ? ILE A 114 GLN A 128 1 ? 15 
HELX_P HELX_P25 AC7 GLY B 144 ? TYR B 161 ? GLY A 144 TYR A 161 1 ? 18 
HELX_P HELX_P26 AC8 VAL B 182 ? SER B 198 ? VAL A 182 SER A 198 1 ? 17 
HELX_P HELX_P27 AC9 ASP B 205 ? ASN B 216 ? ASP A 205 ASN A 216 1 ? 12 
HELX_P HELX_P28 AD1 THR B 223 ? PHE B 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P29 AD2 ASP B 251 ? VAL B 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P30 AD3 SER B 277 ? TYR B 282 ? SER A 277 TYR A 282 1 ? 6  
HELX_P HELX_P31 AD4 SER B 287 ? CYS B 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P32 AD5 VAL B 324 ? LYS B 338 ? VAL A 324 LYS A 338 1 ? 15 
HELX_P HELX_P33 AD6 ILE B 384 ? LYS B 401 ? ILE A 384 LYS A 401 1 ? 18 
HELX_P HELX_P34 AD7 PHE B 404 ? GLY B 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P35 AD8 GLU B 415 ? VAL B 437 ? GLU A 415 VAL A 437 1 ? 23 
HELX_P HELX_P36 AD9 ASN C 19  ? VAL C 23  ? ASN K 19  VAL K 23  5 ? 5  
HELX_P HELX_P37 AE1 SER C 57  ? ALA C 66  ? SER K 57  ALA K 66  1 ? 10 
HELX_P HELX_P38 AE2 ALA C 66  ? LEU C 74  ? ALA K 66  LEU K 74  1 ? 9  
HELX_P HELX_P39 AE3 GLY C 90  ? MET C 95  ? GLY K 90  MET K 95  1 ? 6  
HELX_P HELX_P40 AE4 ILE C 107 ? TYR C 120 ? ILE K 107 TYR K 120 1 ? 14 
HELX_P HELX_P41 AE5 SER C 175 ? SER C 188 ? SER K 175 SER K 188 1 ? 14 
HELX_P HELX_P42 AE6 LYS C 237 ? THR C 241 ? LYS K 237 THR K 241 5 ? 5  
HELX_P HELX_P43 AE7 GLY C 245 ? GLU C 270 ? GLY K 245 GLU K 270 1 ? 26 
HELX_P HELX_P44 AE8 PRO C 276 ? ASP C 279 ? PRO K 276 ASP K 279 5 ? 4  
HELX_P HELX_P45 AE9 SER C 280 ? LEU C 286 ? SER K 280 LEU K 286 1 ? 7  
HELX_P HELX_P46 AF1 LEU C 286 ? GLY C 291 ? LEU K 286 GLY K 291 1 ? 6  
HELX_P HELX_P47 AF2 SER C 305 ? TYR C 307 ? SER K 305 TYR K 307 5 ? 3  
HELX_P HELX_P48 AF3 ASN C 308 ? LYS C 323 ? ASN K 308 LYS K 323 1 ? 16 
# 
_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 
metalc1 metalc ? ? F GTP . O3G ? ? ? 1_555 G MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc2 metalc ? ? F GTP . O1B ? ? ? 1_555 G MG . MG ? ? A GTP 501 A MG 502 1_555 ? ? ? ? ? ? ? 2.776 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O3G 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   GTP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    GTP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     501 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   G 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     502 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O1B 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   GTP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    GTP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     501 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 68.1 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 271 A . ? ALA 273 B PRO 272 A ? PRO 274 B 1 0.52 
2 ALA 273 B . ? ALA 273 A PRO 274 B ? PRO 274 A 1 0.55 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 2  ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 4  ? 
AA6 ? 8  ? 
AA7 ? 8  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 2  ? 
# 
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  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
AA3 5 6  ? parallel      
AA4 1 2  ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA5 3 4  ? parallel      
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA6 5 6  ? anti-parallel 
AA6 6 7  ? anti-parallel 
AA6 7 8  ? anti-parallel 
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? anti-parallel 
AA7 6 7  ? anti-parallel 
AA7 7 8  ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? 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  PHE A 90  ? PHE A 92  ? PHE B 92  PHE B 94  
AA1 2  ALA A 63  ? ASP A 67  ? ALA B 65  ASP B 69  
AA1 3  GLU A 3   ? ALA A 9   ? GLU B 3   ALA B 9   
AA1 4  LEU A 130 ? SER A 138 ? LEU B 132 SER B 140 
AA1 5  ILE A 163 ? VAL A 169 ? ILE B 165 VAL B 171 
AA1 6  GLU A 198 ? ILE A 202 ? GLU B 200 ILE B 204 
AA1 7  PHE A 265 ? ALA A 271 ? PHE B 267 ALA B 273 
AA1 8  MET A 363 ? SER A 371 ? MET B 373 SER B 381 
AA1 9  TYR A 310 ? GLY A 319 ? TYR B 312 GLY B 321 
AA1 10 VAL A 349 ? CYS A 354 ? VAL B 351 CYS B 356 
AA2 1  TYR A 51  ? ALA A 54  ? TYR B 53  ALA B 56  
AA2 2  LYS A 58  ? PRO A 61  ? LYS B 60  PRO B 63  
AA3 1  LEU B 92  ? THR B 94  ? LEU A 92  THR A 94  
AA3 2  ALA B 65  ? ASP B 69  ? ALA A 65  ASP A 69  
AA3 3  GLU B 3   ? VAL B 9   ? GLU A 3   VAL A 9   
AA3 4  LEU B 132 ? PHE B 138 ? LEU A 132 PHE A 138 
AA3 5  SER B 165 ? ILE B 171 ? SER A 165 ILE A 171 
AA3 6  CYS B 200 ? VAL B 204 ? CYS A 200 VAL A 204 
AA4 1  PHE B 53  ? GLU B 55  ? PHE A 53  GLU A 55  
AA4 2  HIS B 61  ? PRO B 63  ? HIS A 61  PRO A 63  
AA5 1  LEU B 269 ? ALA B 273 ? LEU A 269 ALA A 273 
AA5 2  ARG B 373 ? THR B 381 ? ARG A 373 THR A 381 
AA5 3  TYR B 312 ? GLY B 321 ? TYR A 312 GLY A 321 
AA5 4  PHE B 351 ? ASN B 356 ? PHE A 351 ASN A 356 
AA6 1  ARG C 50  ? VAL C 51  ? ARG K 50  VAL K 51  
AA6 2  ILE C 9   ? ARG C 14  ? ILE K 9   ARG K 14  
AA6 3  ARG C 295 ? CYS C 301 ? ARG K 295 CYS K 301 
AA6 4  GLY C 79  ? GLY C 85  ? GLY K 79  GLY K 85  
AA6 5  LYS C 222 ? ASP C 231 ? LYS K 222 ASP K 231 
AA6 6  HIS C 205 ? ASN C 216 ? HIS K 205 ASN K 216 
AA6 7  LEU C 126 ? ILE C 137 ? LEU K 126 ILE K 137 
AA6 8  ILE C 142 ? ASP C 144 ? ILE K 142 ASP K 144 
AA7 1  ARG C 50  ? VAL C 51  ? ARG K 50  VAL K 51  
AA7 2  ILE C 9   ? ARG C 14  ? ILE K 9   ARG K 14  
AA7 3  ARG C 295 ? CYS C 301 ? ARG K 295 CYS K 301 
AA7 4  GLY C 79  ? GLY C 85  ? GLY K 79  GLY K 85  
AA7 5  LYS C 222 ? ASP C 231 ? LYS K 222 ASP K 231 
AA7 6  HIS C 205 ? ASN C 216 ? HIS K 205 ASN K 216 
AA7 7  LEU C 126 ? ILE C 137 ? LEU K 126 ILE K 137 
AA7 8  ARG C 171 ? VAL C 173 ? ARG K 171 VAL K 173 
AA8 1  LYS C 32  ? GLN C 34  ? LYS K 32  GLN K 34  
AA8 2  THR C 38  ? VAL C 40  ? THR K 38  VAL K 40  
AA8 3  PRO C 45  ? ALA C 47  ? PRO K 45  ALA K 47  
AA9 1  SER C 154 ? HIS C 156 ? SER K 154 HIS K 156 
AA9 2  TYR C 164 ? LYS C 166 ? TYR K 164 LYS K 166 
AB1 1  VAL C 192 ? ALA C 193 ? VAL K 192 ALA K 193 
AB1 2  SER C 201 ? SER C 202 ? SER K 201 SER K 202 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O VAL A 91  ? O VAL B 93  N LEU A 65  ? N LEU B 67  
AA1 2 3  O VAL A 66  ? O VAL B 68  N GLN A 8   ? N GLN B 8   
AA1 3 4  N VAL A 5   ? N VAL B 5   O GLN A 134 ? O GLN B 136 
AA1 4 5  N PHE A 133 ? N PHE B 135 O ILE A 163 ? O ILE B 165 
AA1 5 6  N THR A 166 ? N THR B 168 O TYR A 200 ? O TYR B 202 
AA1 6 7  N CYS A 201 ? N CYS B 203 O PHE A 266 ? O PHE B 268 
AA1 7 8  N ALA A 271 ? N ALA B 273 O ALA A 365 ? O ALA B 375 
AA1 8 9  O ASN A 370 ? O ASN B 380 N LEU A 311 ? N LEU B 313 
AA1 9 10 N PHE A 317 ? N PHE B 319 O ALA A 352 ? O ALA B 354 
AA2 1 2  N ASN A 52  ? N ASN B 54  O VAL A 60  ? O VAL B 62  
AA3 1 2  O ILE B 93  ? O ILE A 93  N PHE B 67  ? N PHE A 67  
AA3 2 3  O VAL B 68  ? O VAL A 68  N HIS B 8   ? N HIS A 8   
AA3 3 4  N ILE B 7   ? N ILE A 7   O PHE B 138 ? O PHE A 138 
AA3 4 5  N VAL B 137 ? N VAL A 137 O PHE B 169 ? O PHE A 169 
AA3 5 6  N GLU B 168 ? N GLU A 168 O PHE B 202 ? O PHE A 202 
AA4 1 2  N SER B 54  ? N SER A 54  O VAL B 62  ? O VAL A 62  
AA5 1 2  N LEU B 269 ? N LEU A 269 O SER B 379 ? O SER A 379 
AA5 2 3  O LEU B 378 ? O LEU A 378 N CYS B 316 ? N CYS A 316 
AA5 3 4  N TYR B 319 ? N TYR A 319 O GLY B 354 ? O GLY A 354 
AA6 1 2  O ARG C 50  ? O ARG K 50  N CYS C 13  ? N CYS K 13  
AA6 2 3  N MET C 12  ? N MET K 12  O ILE C 298 ? O ILE K 298 
AA6 3 4  O CYS C 301 ? O CYS K 301 N TYR C 84  ? N TYR K 84  
AA6 4 5  N ILE C 81  ? N ILE K 81  O VAL C 230 ? O VAL K 230 
AA6 5 6  O ASP C 231 ? O ASP K 231 N SER C 206 ? N SER K 206 
AA6 6 7  O ASN C 211 ? O ASN K 211 N LYS C 131 ? N LYS K 131 
AA6 7 8  N GLU C 136 ? N GLU K 136 O ARG C 143 ? O ARG K 143 
AA7 1 2  O ARG C 50  ? O ARG K 50  N CYS C 13  ? N CYS K 13  
AA7 2 3  N MET C 12  ? N MET K 12  O ILE C 298 ? O ILE K 298 
AA7 3 4  O CYS C 301 ? O CYS K 301 N TYR C 84  ? N TYR K 84  
AA7 4 5  N ILE C 81  ? N ILE K 81  O VAL C 230 ? O VAL K 230 
AA7 5 6  O ASP C 231 ? O ASP K 231 N SER C 206 ? N SER K 206 
AA7 6 7  O ASN C 211 ? O ASN K 211 N LYS C 131 ? N LYS K 131 
AA7 7 8  N VAL C 132 ? N VAL K 132 O ARG C 171 ? O ARG K 171 
AA8 1 2  N LYS C 32  ? N LYS K 32  O VAL C 40  ? O VAL K 40  
AA8 2 3  N VAL C 39  ? N VAL K 39  O TYR C 46  ? O TYR K 46  
AA9 1 2  N HIS C 156 ? N HIS K 156 O TYR C 164 ? O TYR K 164 
AB1 1 2  N ALA C 193 ? N ALA K 193 O SER C 201 ? O SER K 201 
# 
_pdbx_entry_details.entry_id                   9GNQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NE2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    229 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O14 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   TA1 
_pdbx_validate_close_contact.auth_seq_id_2    502 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A PRO 268 ? ? N A LEU 269 ? ? 1.537 1.336 0.201 0.023 Y 
2 1 C A LEU 269 ? ? N A ALA 270 ? ? 1.479 1.336 0.143 0.023 Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             O 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              268 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              268 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             N 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              269 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                133.04 
_pdbx_validate_rmsd_angle.angle_target_value         122.70 
_pdbx_validate_rmsd_angle.angle_deviation            10.34 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS B 309 ? ? -92.74  52.14   
2  1 TYR B 435 ? ? -95.31  32.17   
3  1 SER A 48  ? ? 69.38   -4.77   
4  1 LYS A 112 ? ? -81.88  47.63   
5  1 ASP A 251 ? ? -102.91 -169.02 
6  1 GLU K 96  ? ? -173.52 -55.39  
7  1 TYR K 120 ? ? -69.02  4.51    
8  1 ASP K 123 ? ? 46.00   -150.31 
9  1 TYR K 134 ? ? -161.44 115.98  
10 1 ARG K 161 ? ? 38.97   59.39   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 156 ? ? 0.092 'SIDE CHAIN' 
2 1 ARG A 221 ? ? 0.260 'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9GNQ 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           'Phenix Real Space refine and Coot' 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_reconstruction.entry_id                    9GNQ 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     'Noise-substitution test corrected FSC' 
_em_3d_reconstruction.resolution                  2.9 
_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               268199 
_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       'BRB80 + 5mM AMPPNP' 
_em_buffer.pH            6.8 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX '13pf microtubule bound to Kif5bMoNeXXX in the presence of ADP' ? ? ? '1, 2, 3' 
2 1 NATURAL            COMPLEX 'Kif5bMoNeXXX bound with ADP'                                   ? ? ? 3         
3 1 NATURAL            COMPLEX Alpha-tubulin                                                   ? ? ? 2         
4 2 NATURAL            COMPLEX 'Beta tubulin'                                                  ? ? ? 1         
# 
_em_imaging.entry_id                        9GNQ 
_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           ? 
_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             700 
_em_imaging.nominal_defocus_max             2500 
_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_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    ? 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        C-flat-2/2 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9GNQ 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              80 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'LEICA EM GP' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9GNQ 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       FILAMENT 
_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 B ASP 437 ? A ASP 427 
2   1 Y 1 B ALA 438 ? A ALA 428 
3   1 Y 1 B THR 439 ? A THR 429 
4   1 Y 1 B ALA 440 ? A ALA 430 
5   1 Y 1 B ASP 441 ? A ASP 431 
6   1 Y 1 B GLU 442 ? A GLU 432 
7   1 Y 1 B GLN 443 ? A GLN 433 
8   1 Y 1 B GLY 444 ? A GLY 434 
9   1 Y 1 B GLU 445 ? A GLU 435 
10  1 Y 1 B PHE 446 ? A PHE 436 
11  1 Y 1 B GLU 447 ? A GLU 437 
12  1 Y 1 B GLU 448 ? A GLU 438 
13  1 Y 1 B GLU 449 ? A GLU 439 
14  1 Y 1 B GLY 450 ? A GLY 440 
15  1 Y 1 B GLU 451 ? A GLU 441 
16  1 Y 1 B GLU 452 ? A GLU 442 
17  1 Y 1 B ASP 453 ? A ASP 443 
18  1 Y 1 B GLU 454 ? A GLU 444 
19  1 Y 1 B ALA 455 ? A ALA 445 
20  1 Y 1 A SER 38  ? B SER 38  
21  1 Y 1 A ASP 39  ? B ASP 39  
22  1 Y 1 A LYS 40  ? B LYS 40  
23  1 Y 1 A THR 41  ? B THR 41  
24  1 Y 1 A ILE 42  ? B ILE 42  
25  1 Y 1 A GLY 43  ? B GLY 43  
26  1 Y 1 A GLY 44  ? B GLY 44  
27  1 Y 1 A GLY 45  ? B GLY 45  
28  1 Y 1 A ASP 46  ? B ASP 46  
29  1 Y 1 A ASP 438 ? B ASP 438 
30  1 Y 1 A SER 439 ? B SER 439 
31  1 Y 1 A VAL 440 ? B VAL 440 
32  1 Y 1 A GLU 441 ? B GLU 441 
33  1 Y 1 A GLY 442 ? B GLY 442 
34  1 Y 1 A GLU 443 ? B GLU 443 
35  1 Y 1 A GLY 444 ? B GLY 444 
36  1 Y 1 A GLU 445 ? B GLU 445 
37  1 Y 1 A GLU 446 ? B GLU 446 
38  1 Y 1 A GLU 447 ? B GLU 447 
39  1 Y 1 A GLY 448 ? B GLY 448 
40  1 Y 1 A GLU 449 ? B GLU 449 
41  1 Y 1 A GLU 450 ? B GLU 450 
42  1 Y 1 A TYR 451 ? B TYR 451 
43  1 Y 1 K MET 1   ? C MET 1   
44  1 Y 1 K ALA 2   ? C ALA 2   
45  1 Y 1 K ASP 3   ? C ASP 3   
46  1 Y 1 K LEU 4   ? C LEU 4   
47  1 Y 1 K ALA 5   ? C ALA 5   
48  1 Y 1 K GLU 6   ? C GLU 6   
49  1 Y 1 K CYS 7   ? C CYS 7   
50  1 Y 1 K THR 195 ? C THR 195 
51  1 Y 1 K ASN 196 ? C ASN 196 
52  1 Y 1 K MET 197 ? C MET 197 
53  1 Y 1 K ASN 198 ? C ASN 198 
54  1 Y 1 K THR 324 ? C THR 324 
55  1 Y 1 K ILE 325 ? C ILE 325 
56  1 Y 1 K LYS 326 ? C LYS 326 
57  1 Y 1 K ASN 327 ? C ASN 327 
58  1 Y 1 K THR 328 ? C THR 328 
59  1 Y 1 K VAL 329 ? C VAL 329 
60  1 Y 1 K CYS 330 ? C CYS 330 
61  1 Y 1 K VAL 331 ? C VAL 331 
62  1 Y 1 K ASN 332 ? C ASN 332 
63  1 Y 1 K VAL 333 ? C VAL 333 
64  1 Y 1 K GLU 334 ? C GLU 334 
65  1 Y 1 K LEU 335 ? C LEU 335 
66  1 Y 1 K THR 336 ? C THR 336 
67  1 Y 1 K ALA 337 ? C ALA 337 
68  1 Y 1 K GLU 338 ? C GLU 338 
69  1 Y 1 K GLN 339 ? C GLN 339 
70  1 Y 1 K TRP 340 ? C TRP 340 
71  1 Y 1 K LYS 341 ? C LYS 341 
72  1 Y 1 K LYS 342 ? C LYS 342 
73  1 Y 1 K LYS 343 ? C LYS 343 
74  1 Y 1 K TYR 344 ? C TYR 344 
75  1 Y 1 K GLU 345 ? C GLU 345 
76  1 Y 1 K LYS 346 ? C LYS 346 
77  1 Y 1 K GLU 347 ? C GLU 347 
78  1 Y 1 K LYS 348 ? C LYS 348 
79  1 Y 1 K GLU 349 ? C GLU 349 
80  1 Y 1 K LYS 350 ? C LYS 350 
81  1 Y 1 K ASN 351 ? C ASN 351 
82  1 Y 1 K LYS 352 ? C LYS 352 
83  1 Y 1 K ILE 353 ? C ILE 353 
84  1 Y 1 K LEU 354 ? C LEU 354 
85  1 Y 1 K ARG 355 ? C ARG 355 
86  1 Y 1 K ASN 356 ? C ASN 356 
87  1 Y 1 K THR 357 ? C THR 357 
88  1 Y 1 K THR 358 ? C THR 358 
89  1 Y 1 K GLY 359 ? C GLY 359 
90  1 Y 1 K SER 360 ? C SER 360 
91  1 Y 1 K THR 361 ? C THR 361 
92  1 Y 1 K GLY 362 ? C GLY 362 
93  1 Y 1 K SER 363 ? C SER 363 
94  1 Y 1 K THR 364 ? C THR 364 
95  1 Y 1 K GLY 365 ? C GLY 365 
96  1 Y 1 K SER 366 ? C SER 366 
97  1 Y 1 K THR 367 ? C THR 367 
98  1 Y 1 K GLY 368 ? C GLY 368 
99  1 Y 1 K SER 369 ? C SER 369 
100 1 Y 1 K THR 370 ? C THR 370 
101 1 Y 1 K GLY 371 ? C GLY 371 
102 1 Y 1 K SER 372 ? C SER 372 
103 1 Y 1 K THR 373 ? C THR 373 
104 1 Y 1 K GLY 374 ? C GLY 374 
105 1 Y 1 K SER 375 ? C SER 375 
106 1 Y 1 K THR 376 ? C THR 376 
107 1 Y 1 K GLY 377 ? C GLY 377 
108 1 Y 1 K SER 378 ? C SER 378 
109 1 Y 1 K THR 379 ? C THR 379 
110 1 Y 1 K GLY 380 ? C GLY 380 
111 1 Y 1 K SER 381 ? C SER 381 
112 1 Y 1 K THR 382 ? C THR 382 
113 1 Y 1 K GLY 383 ? C GLY 383 
114 1 Y 1 K SER 384 ? C SER 384 
115 1 Y 1 K ALA 385 ? C ALA 385 
116 1 Y 1 K ARG 386 ? C ARG 386 
117 1 Y 1 K ARG 387 ? C ARG 387 
118 1 Y 1 K GLY 388 ? C GLY 388 
119 1 Y 1 K HIS 389 ? C HIS 389 
120 1 Y 1 K SER 390 ? C SER 390 
121 1 Y 1 K ALA 391 ? C ALA 391 
122 1 Y 1 K THR 392 ? C THR 392 
123 1 Y 1 K GLY 393 ? C GLY 393 
124 1 Y 1 K SER 394 ? C SER 394 
125 1 Y 1 K THR 395 ? C THR 395 
126 1 Y 1 K SER 396 ? C SER 396 
127 1 Y 1 K GLY 397 ? C GLY 397 
128 1 Y 1 K THR 398 ? C THR 398 
129 1 Y 1 K PRO 399 ? C PRO 399 
130 1 Y 1 K GLY 400 ? C GLY 400 
131 1 Y 1 K GLN 401 ? C GLN 401 
132 1 Y 1 K HIS 402 ? C HIS 402 
133 1 Y 1 K PRO 403 ? C PRO 403 
134 1 Y 1 K ALA 404 ? C ALA 404 
135 1 Y 1 K ALA 405 ? C ALA 405 
136 1 Y 1 K SER 406 ? C SER 406 
137 1 Y 1 K PRO 407 ? C PRO 407 
138 1 Y 1 K THR 408 ? C THR 408 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CYS N      N  N N 116 
CYS CA     C  N R 117 
CYS C      C  N N 118 
CYS O      O  N N 119 
CYS CB     C  N N 120 
CYS SG     S  N N 121 
CYS OXT    O  N N 122 
CYS H      H  N N 123 
CYS H2     H  N N 124 
CYS HA     H  N N 125 
CYS HB2    H  N N 126 
CYS HB3    H  N N 127 
CYS HG     H  N N 128 
CYS HXT    H  N N 129 
GDP PB     P  N N 130 
GDP O1B    O  N N 131 
GDP O2B    O  N N 132 
GDP O3B    O  N N 133 
GDP O3A    O  N N 134 
GDP PA     P  N N 135 
GDP O1A    O  N N 136 
GDP O2A    O  N N 137 
GDP "O5'"  O  N N 138 
GDP "C5'"  C  N N 139 
GDP "C4'"  C  N R 140 
GDP "O4'"  O  N N 141 
GDP "C3'"  C  N S 142 
GDP "O3'"  O  N N 143 
GDP "C2'"  C  N R 144 
GDP "O2'"  O  N N 145 
GDP "C1'"  C  N R 146 
GDP N9     N  Y N 147 
GDP C8     C  Y N 148 
GDP N7     N  Y N 149 
GDP C5     C  Y N 150 
GDP C6     C  N N 151 
GDP O6     O  N N 152 
GDP N1     N  N N 153 
GDP C2     C  N N 154 
GDP N2     N  N N 155 
GDP N3     N  N N 156 
GDP C4     C  Y N 157 
GDP HOB2   H  N N 158 
GDP HOB3   H  N N 159 
GDP HOA2   H  N N 160 
GDP "H5'"  H  N N 161 
GDP "H5''" H  N N 162 
GDP "H4'"  H  N N 163 
GDP "H3'"  H  N N 164 
GDP "HO3'" H  N N 165 
GDP "H2'"  H  N N 166 
GDP "HO2'" H  N N 167 
GDP "H1'"  H  N N 168 
GDP H8     H  N N 169 
GDP HN1    H  N N 170 
GDP HN21   H  N N 171 
GDP HN22   H  N N 172 
GLN N      N  N N 173 
GLN CA     C  N S 174 
GLN C      C  N N 175 
GLN O      O  N N 176 
GLN CB     C  N N 177 
GLN CG     C  N N 178 
GLN CD     C  N N 179 
GLN OE1    O  N N 180 
GLN NE2    N  N N 181 
GLN OXT    O  N N 182 
GLN H      H  N N 183 
GLN H2     H  N N 184 
GLN HA     H  N N 185 
GLN HB2    H  N N 186 
GLN HB3    H  N N 187 
GLN HG2    H  N N 188 
GLN HG3    H  N N 189 
GLN HE21   H  N N 190 
GLN HE22   H  N N 191 
GLN HXT    H  N N 192 
GLU N      N  N N 193 
GLU CA     C  N S 194 
GLU C      C  N N 195 
GLU O      O  N N 196 
GLU CB     C  N N 197 
GLU CG     C  N N 198 
GLU CD     C  N N 199 
GLU OE1    O  N N 200 
GLU OE2    O  N N 201 
GLU OXT    O  N N 202 
GLU H      H  N N 203 
GLU H2     H  N N 204 
GLU HA     H  N N 205 
GLU HB2    H  N N 206 
GLU HB3    H  N N 207 
GLU HG2    H  N N 208 
GLU HG3    H  N N 209 
GLU HE2    H  N N 210 
GLU HXT    H  N N 211 
GLY N      N  N N 212 
GLY CA     C  N N 213 
GLY C      C  N N 214 
GLY O      O  N N 215 
GLY OXT    O  N N 216 
GLY H      H  N N 217 
GLY H2     H  N N 218 
GLY HA2    H  N N 219 
GLY HA3    H  N N 220 
GLY HXT    H  N N 221 
GTP PG     P  N N 222 
GTP O1G    O  N N 223 
GTP O2G    O  N N 224 
GTP O3G    O  N N 225 
GTP O3B    O  N N 226 
GTP PB     P  N N 227 
GTP O1B    O  N N 228 
GTP O2B    O  N N 229 
GTP O3A    O  N N 230 
GTP PA     P  N N 231 
GTP O1A    O  N N 232 
GTP O2A    O  N N 233 
GTP "O5'"  O  N N 234 
GTP "C5'"  C  N N 235 
GTP "C4'"  C  N R 236 
GTP "O4'"  O  N N 237 
GTP "C3'"  C  N S 238 
GTP "O3'"  O  N N 239 
GTP "C2'"  C  N R 240 
GTP "O2'"  O  N N 241 
GTP "C1'"  C  N R 242 
GTP N9     N  Y N 243 
GTP C8     C  Y N 244 
GTP N7     N  Y N 245 
GTP C5     C  Y N 246 
GTP C6     C  N N 247 
GTP O6     O  N N 248 
GTP N1     N  N N 249 
GTP C2     C  N N 250 
GTP N2     N  N N 251 
GTP N3     N  N N 252 
GTP C4     C  Y N 253 
GTP HOG2   H  N N 254 
GTP HOG3   H  N N 255 
GTP HOB2   H  N N 256 
GTP HOA2   H  N N 257 
GTP "H5'"  H  N N 258 
GTP "H5''" H  N N 259 
GTP "H4'"  H  N N 260 
GTP "H3'"  H  N N 261 
GTP "HO3'" H  N N 262 
GTP "H2'"  H  N N 263 
GTP "HO2'" H  N N 264 
GTP "H1'"  H  N N 265 
GTP H8     H  N N 266 
GTP HN1    H  N N 267 
GTP HN21   H  N N 268 
GTP HN22   H  N N 269 
HIS N      N  N N 270 
HIS CA     C  N S 271 
HIS C      C  N N 272 
HIS O      O  N N 273 
HIS CB     C  N N 274 
HIS CG     C  Y N 275 
HIS ND1    N  Y N 276 
HIS CD2    C  Y N 277 
HIS CE1    C  Y N 278 
HIS NE2    N  Y N 279 
HIS OXT    O  N N 280 
HIS H      H  N N 281 
HIS H2     H  N N 282 
HIS HA     H  N N 283 
HIS HB2    H  N N 284 
HIS HB3    H  N N 285 
HIS HD1    H  N N 286 
HIS HD2    H  N N 287 
HIS HE1    H  N N 288 
HIS HE2    H  N N 289 
HIS HXT    H  N N 290 
ILE N      N  N N 291 
ILE CA     C  N S 292 
ILE C      C  N N 293 
ILE O      O  N N 294 
ILE CB     C  N S 295 
ILE CG1    C  N N 296 
ILE CG2    C  N N 297 
ILE CD1    C  N N 298 
ILE OXT    O  N N 299 
ILE H      H  N N 300 
ILE H2     H  N N 301 
ILE HA     H  N N 302 
ILE HB     H  N N 303 
ILE HG12   H  N N 304 
ILE HG13   H  N N 305 
ILE HG21   H  N N 306 
ILE HG22   H  N N 307 
ILE HG23   H  N N 308 
ILE HD11   H  N N 309 
ILE HD12   H  N N 310 
ILE HD13   H  N N 311 
ILE HXT    H  N N 312 
LEU N      N  N N 313 
LEU CA     C  N S 314 
LEU C      C  N N 315 
LEU O      O  N N 316 
LEU CB     C  N N 317 
LEU CG     C  N N 318 
LEU CD1    C  N N 319 
LEU CD2    C  N N 320 
LEU OXT    O  N N 321 
LEU H      H  N N 322 
LEU H2     H  N N 323 
LEU HA     H  N N 324 
LEU HB2    H  N N 325 
LEU HB3    H  N N 326 
LEU HG     H  N N 327 
LEU HD11   H  N N 328 
LEU HD12   H  N N 329 
LEU HD13   H  N N 330 
LEU HD21   H  N N 331 
LEU HD22   H  N N 332 
LEU HD23   H  N N 333 
LEU HXT    H  N N 334 
LYS N      N  N N 335 
LYS CA     C  N S 336 
LYS C      C  N N 337 
LYS O      O  N N 338 
LYS CB     C  N N 339 
LYS CG     C  N N 340 
LYS CD     C  N N 341 
LYS CE     C  N N 342 
LYS NZ     N  N N 343 
LYS OXT    O  N N 344 
LYS H      H  N N 345 
LYS H2     H  N N 346 
LYS HA     H  N N 347 
LYS HB2    H  N N 348 
LYS HB3    H  N N 349 
LYS HG2    H  N N 350 
LYS HG3    H  N N 351 
LYS HD2    H  N N 352 
LYS HD3    H  N N 353 
LYS HE2    H  N N 354 
LYS HE3    H  N N 355 
LYS HZ1    H  N N 356 
LYS HZ2    H  N N 357 
LYS HZ3    H  N N 358 
LYS HXT    H  N N 359 
MET N      N  N N 360 
MET CA     C  N S 361 
MET C      C  N N 362 
MET O      O  N N 363 
MET CB     C  N N 364 
MET CG     C  N N 365 
MET SD     S  N N 366 
MET CE     C  N N 367 
MET OXT    O  N N 368 
MET H      H  N N 369 
MET H2     H  N N 370 
MET HA     H  N N 371 
MET HB2    H  N N 372 
MET HB3    H  N N 373 
MET HG2    H  N N 374 
MET HG3    H  N N 375 
MET HE1    H  N N 376 
MET HE2    H  N N 377 
MET HE3    H  N N 378 
MET HXT    H  N N 379 
MG  MG     MG N N 380 
PHE N      N  N N 381 
PHE CA     C  N S 382 
PHE C      C  N N 383 
PHE O      O  N N 384 
PHE CB     C  N N 385 
PHE CG     C  Y N 386 
PHE CD1    C  Y N 387 
PHE CD2    C  Y N 388 
PHE CE1    C  Y N 389 
PHE CE2    C  Y N 390 
PHE CZ     C  Y N 391 
PHE OXT    O  N N 392 
PHE H      H  N N 393 
PHE H2     H  N N 394 
PHE HA     H  N N 395 
PHE HB2    H  N N 396 
PHE HB3    H  N N 397 
PHE HD1    H  N N 398 
PHE HD2    H  N N 399 
PHE HE1    H  N N 400 
PHE HE2    H  N N 401 
PHE HZ     H  N N 402 
PHE HXT    H  N N 403 
PRO N      N  N N 404 
PRO CA     C  N S 405 
PRO C      C  N N 406 
PRO O      O  N N 407 
PRO CB     C  N N 408 
PRO CG     C  N N 409 
PRO CD     C  N N 410 
PRO OXT    O  N N 411 
PRO H      H  N N 412 
PRO HA     H  N N 413 
PRO HB2    H  N N 414 
PRO HB3    H  N N 415 
PRO HG2    H  N N 416 
PRO HG3    H  N N 417 
PRO HD2    H  N N 418 
PRO HD3    H  N N 419 
PRO HXT    H  N N 420 
SER N      N  N N 421 
SER CA     C  N S 422 
SER C      C  N N 423 
SER O      O  N N 424 
SER CB     C  N N 425 
SER OG     O  N N 426 
SER OXT    O  N N 427 
SER H      H  N N 428 
SER H2     H  N N 429 
SER HA     H  N N 430 
SER HB2    H  N N 431 
SER HB3    H  N N 432 
SER HG     H  N N 433 
SER HXT    H  N N 434 
TA1 O01    O  N N 435 
TA1 C01    C  N S 436 
TA1 C02    C  N S 437 
TA1 O02    O  N N 438 
TA1 C03    C  N N 439 
TA1 O03    O  N N 440 
TA1 C04    C  Y N 441 
TA1 C05    C  Y N 442 
TA1 C06    C  Y N 443 
TA1 C07    C  Y N 444 
TA1 C08    C  Y N 445 
TA1 C09    C  Y N 446 
TA1 C10    C  N R 447 
TA1 C11    C  N S 448 
TA1 O04    O  N N 449 
TA1 C12    C  N N 450 
TA1 O05    O  N N 451 
TA1 C13    C  N N 452 
TA1 C14    C  N N 453 
TA1 O06    O  N N 454 
TA1 C15    C  N R 455 
TA1 C16    C  N N 456 
TA1 C17    C  N S 457 
TA1 O07    O  N N 458 
TA1 C18    C  N S 459 
TA1 C19    C  N N 460 
TA1 C20    C  N N 461 
TA1 O08    O  N N 462 
TA1 C21    C  N R 463 
TA1 O09    O  N N 464 
TA1 C22    C  N N 465 
TA1 O10    O  N N 466 
TA1 C23    C  N N 467 
TA1 C24    C  N N 468 
TA1 C25    C  N N 469 
TA1 C26    C  N S 470 
TA1 O11    O  N N 471 
TA1 C27    C  N N 472 
TA1 O12    O  N N 473 
TA1 C28    C  N R 474 
TA1 O13    O  N N 475 
TA1 C29    C  N S 476 
TA1 N01    N  N N 477 
TA1 C30    C  N N 478 
TA1 O14    O  N N 479 
TA1 C31    C  Y N 480 
TA1 C32    C  Y N 481 
TA1 C33    C  Y N 482 
TA1 C34    C  Y N 483 
TA1 C35    C  Y N 484 
TA1 C36    C  Y N 485 
TA1 C37    C  Y N 486 
TA1 C38    C  Y N 487 
TA1 C39    C  Y N 488 
TA1 C40    C  Y N 489 
TA1 C41    C  Y N 490 
TA1 C42    C  Y N 491 
TA1 C43    C  N N 492 
TA1 C44    C  N N 493 
TA1 C45    C  N N 494 
TA1 C46    C  N N 495 
TA1 C47    C  N N 496 
TA1 H011   H  N N 497 
TA1 H021   H  N N 498 
TA1 H051   H  N N 499 
TA1 H061   H  N N 500 
TA1 HC71   H  N N 501 
TA1 H081   H  N N 502 
TA1 H091   H  N N 503 
TA1 H101   H  N N 504 
TA1 H131   H  N N 505 
TA1 H132   H  N N 506 
TA1 H133   H  N N 507 
TA1 H141   H  N N 508 
TA1 H142   H  N N 509 
TA1 H151   H  N N 510 
TA1 H161   H  N N 511 
TA1 H162   H  N N 512 
TA1 H171   H  N N 513 
TA1 H071   H  N N 514 
TA1 H191   H  N N 515 
TA1 H192   H  N N 516 
TA1 H193   H  N N 517 
TA1 H211   H  N N 518 
TA1 H231   H  N N 519 
TA1 H232   H  N N 520 
TA1 H233   H  N N 521 
TA1 H261   H  N N 522 
TA1 H281   H  N N 523 
TA1 HO11   H  N N 524 
TA1 H291   H  N N 525 
TA1 HN01   H  N N 526 
TA1 H321   H  N N 527 
TA1 H331   H  N N 528 
TA1 H341   H  N N 529 
TA1 H351   H  N N 530 
TA1 H361   H  N N 531 
TA1 H381   H  N N 532 
TA1 H391   H  N N 533 
TA1 H401   H  N N 534 
TA1 H411   H  N N 535 
TA1 H421   H  N N 536 
TA1 H431   H  N N 537 
TA1 H432   H  N N 538 
TA1 H441   H  N N 539 
TA1 H442   H  N N 540 
TA1 H443   H  N N 541 
TA1 H461   H  N N 542 
TA1 H462   H  N N 543 
TA1 H463   H  N N 544 
TA1 H471   H  N N 545 
TA1 H472   H  N N 546 
TA1 H473   H  N N 547 
THR N      N  N N 548 
THR CA     C  N S 549 
THR C      C  N N 550 
THR O      O  N N 551 
THR CB     C  N R 552 
THR OG1    O  N N 553 
THR CG2    C  N N 554 
THR OXT    O  N N 555 
THR H      H  N N 556 
THR H2     H  N N 557 
THR HA     H  N N 558 
THR HB     H  N N 559 
THR HG1    H  N N 560 
THR HG21   H  N N 561 
THR HG22   H  N N 562 
THR HG23   H  N N 563 
THR HXT    H  N N 564 
TRP N      N  N N 565 
TRP CA     C  N S 566 
TRP C      C  N N 567 
TRP O      O  N N 568 
TRP CB     C  N N 569 
TRP CG     C  Y N 570 
TRP CD1    C  Y N 571 
TRP CD2    C  Y N 572 
TRP NE1    N  Y N 573 
TRP CE2    C  Y N 574 
TRP CE3    C  Y N 575 
TRP CZ2    C  Y N 576 
TRP CZ3    C  Y N 577 
TRP CH2    C  Y N 578 
TRP OXT    O  N N 579 
TRP H      H  N N 580 
TRP H2     H  N N 581 
TRP HA     H  N N 582 
TRP HB2    H  N N 583 
TRP HB3    H  N N 584 
TRP HD1    H  N N 585 
TRP HE1    H  N N 586 
TRP HE3    H  N N 587 
TRP HZ2    H  N N 588 
TRP HZ3    H  N N 589 
TRP HH2    H  N N 590 
TRP HXT    H  N N 591 
TYR N      N  N N 592 
TYR CA     C  N S 593 
TYR C      C  N N 594 
TYR O      O  N N 595 
TYR CB     C  N N 596 
TYR CG     C  Y N 597 
TYR CD1    C  Y N 598 
TYR CD2    C  Y N 599 
TYR CE1    C  Y N 600 
TYR CE2    C  Y N 601 
TYR CZ     C  Y N 602 
TYR OH     O  N N 603 
TYR OXT    O  N N 604 
TYR H      H  N N 605 
TYR H2     H  N N 606 
TYR HA     H  N N 607 
TYR HB2    H  N N 608 
TYR HB3    H  N N 609 
TYR HD1    H  N N 610 
TYR HD2    H  N N 611 
TYR HE1    H  N N 612 
TYR HE2    H  N N 613 
TYR HH     H  N N 614 
TYR HXT    H  N N 615 
VAL N      N  N N 616 
VAL CA     C  N S 617 
VAL C      C  N N 618 
VAL O      O  N N 619 
VAL CB     C  N N 620 
VAL CG1    C  N N 621 
VAL CG2    C  N N 622 
VAL OXT    O  N N 623 
VAL H      H  N N 624 
VAL H2     H  N N 625 
VAL HA     H  N N 626 
VAL HB     H  N N 627 
VAL HG11   H  N N 628 
VAL HG12   H  N N 629 
VAL HG13   H  N N 630 
VAL HG21   H  N N 631 
VAL HG22   H  N N 632 
VAL HG23   H  N N 633 
VAL HXT    H  N N 634 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GDP PB    O1B    doub N N 127 
GDP PB    O2B    sing N N 128 
GDP PB    O3B    sing N N 129 
GDP PB    O3A    sing N N 130 
GDP O2B   HOB2   sing N N 131 
GDP O3B   HOB3   sing N N 132 
GDP O3A   PA     sing N N 133 
GDP PA    O1A    doub N N 134 
GDP PA    O2A    sing N N 135 
GDP PA    "O5'"  sing N N 136 
GDP O2A   HOA2   sing N N 137 
GDP "O5'" "C5'"  sing N N 138 
GDP "C5'" "C4'"  sing N N 139 
GDP "C5'" "H5'"  sing N N 140 
GDP "C5'" "H5''" sing N N 141 
GDP "C4'" "O4'"  sing N N 142 
GDP "C4'" "C3'"  sing N N 143 
GDP "C4'" "H4'"  sing N N 144 
GDP "O4'" "C1'"  sing N N 145 
GDP "C3'" "O3'"  sing N N 146 
GDP "C3'" "C2'"  sing N N 147 
GDP "C3'" "H3'"  sing N N 148 
GDP "O3'" "HO3'" sing N N 149 
GDP "C2'" "O2'"  sing N N 150 
GDP "C2'" "C1'"  sing N N 151 
GDP "C2'" "H2'"  sing N N 152 
GDP "O2'" "HO2'" sing N N 153 
GDP "C1'" N9     sing N N 154 
GDP "C1'" "H1'"  sing N N 155 
GDP N9    C8     sing Y N 156 
GDP N9    C4     sing Y N 157 
GDP C8    N7     doub Y N 158 
GDP C8    H8     sing N N 159 
GDP N7    C5     sing Y N 160 
GDP C5    C6     sing N N 161 
GDP C5    C4     doub Y N 162 
GDP C6    O6     doub N N 163 
GDP C6    N1     sing N N 164 
GDP N1    C2     sing N N 165 
GDP N1    HN1    sing N N 166 
GDP C2    N2     sing N N 167 
GDP C2    N3     doub N N 168 
GDP N2    HN21   sing N N 169 
GDP N2    HN22   sing N N 170 
GDP N3    C4     sing N N 171 
GLN N     CA     sing N N 172 
GLN N     H      sing N N 173 
GLN N     H2     sing N N 174 
GLN CA    C      sing N N 175 
GLN CA    CB     sing N N 176 
GLN CA    HA     sing N N 177 
GLN C     O      doub N N 178 
GLN C     OXT    sing N N 179 
GLN CB    CG     sing N N 180 
GLN CB    HB2    sing N N 181 
GLN CB    HB3    sing N N 182 
GLN CG    CD     sing N N 183 
GLN CG    HG2    sing N N 184 
GLN CG    HG3    sing N N 185 
GLN CD    OE1    doub N N 186 
GLN CD    NE2    sing N N 187 
GLN NE2   HE21   sing N N 188 
GLN NE2   HE22   sing N N 189 
GLN OXT   HXT    sing N N 190 
GLU N     CA     sing N N 191 
GLU N     H      sing N N 192 
GLU N     H2     sing N N 193 
GLU CA    C      sing N N 194 
GLU CA    CB     sing N N 195 
GLU CA    HA     sing N N 196 
GLU C     O      doub N N 197 
GLU C     OXT    sing N N 198 
GLU CB    CG     sing N N 199 
GLU CB    HB2    sing N N 200 
GLU CB    HB3    sing N N 201 
GLU CG    CD     sing N N 202 
GLU CG    HG2    sing N N 203 
GLU CG    HG3    sing N N 204 
GLU CD    OE1    doub N N 205 
GLU CD    OE2    sing N N 206 
GLU OE2   HE2    sing N N 207 
GLU OXT   HXT    sing N N 208 
GLY N     CA     sing N N 209 
GLY N     H      sing N N 210 
GLY N     H2     sing N N 211 
GLY CA    C      sing N N 212 
GLY CA    HA2    sing N N 213 
GLY CA    HA3    sing N N 214 
GLY C     O      doub N N 215 
GLY C     OXT    sing N N 216 
GLY OXT   HXT    sing N N 217 
GTP PG    O1G    doub N N 218 
GTP PG    O2G    sing N N 219 
GTP PG    O3G    sing N N 220 
GTP PG    O3B    sing N N 221 
GTP O2G   HOG2   sing N N 222 
GTP O3G   HOG3   sing N N 223 
GTP O3B   PB     sing N N 224 
GTP PB    O1B    doub N N 225 
GTP PB    O2B    sing N N 226 
GTP PB    O3A    sing N N 227 
GTP O2B   HOB2   sing N N 228 
GTP O3A   PA     sing N N 229 
GTP PA    O1A    doub N N 230 
GTP PA    O2A    sing N N 231 
GTP PA    "O5'"  sing N N 232 
GTP O2A   HOA2   sing N N 233 
GTP "O5'" "C5'"  sing N N 234 
GTP "C5'" "C4'"  sing N N 235 
GTP "C5'" "H5'"  sing N N 236 
GTP "C5'" "H5''" sing N N 237 
GTP "C4'" "O4'"  sing N N 238 
GTP "C4'" "C3'"  sing N N 239 
GTP "C4'" "H4'"  sing N N 240 
GTP "O4'" "C1'"  sing N N 241 
GTP "C3'" "O3'"  sing N N 242 
GTP "C3'" "C2'"  sing N N 243 
GTP "C3'" "H3'"  sing N N 244 
GTP "O3'" "HO3'" sing N N 245 
GTP "C2'" "O2'"  sing N N 246 
GTP "C2'" "C1'"  sing N N 247 
GTP "C2'" "H2'"  sing N N 248 
GTP "O2'" "HO2'" sing N N 249 
GTP "C1'" N9     sing N N 250 
GTP "C1'" "H1'"  sing N N 251 
GTP N9    C8     sing Y N 252 
GTP N9    C4     sing Y N 253 
GTP C8    N7     doub Y N 254 
GTP C8    H8     sing N N 255 
GTP N7    C5     sing Y N 256 
GTP C5    C6     sing N N 257 
GTP C5    C4     doub Y N 258 
GTP C6    O6     doub N N 259 
GTP C6    N1     sing N N 260 
GTP N1    C2     sing N N 261 
GTP N1    HN1    sing N N 262 
GTP C2    N2     sing N N 263 
GTP C2    N3     doub N N 264 
GTP N2    HN21   sing N N 265 
GTP N2    HN22   sing N N 266 
GTP N3    C4     sing N N 267 
HIS N     CA     sing N N 268 
HIS N     H      sing N N 269 
HIS N     H2     sing N N 270 
HIS CA    C      sing N N 271 
HIS CA    CB     sing N N 272 
HIS CA    HA     sing N N 273 
HIS C     O      doub N N 274 
HIS C     OXT    sing N N 275 
HIS CB    CG     sing N N 276 
HIS CB    HB2    sing N N 277 
HIS CB    HB3    sing N N 278 
HIS CG    ND1    sing Y N 279 
HIS CG    CD2    doub Y N 280 
HIS ND1   CE1    doub Y N 281 
HIS ND1   HD1    sing N N 282 
HIS CD2   NE2    sing Y N 283 
HIS CD2   HD2    sing N N 284 
HIS CE1   NE2    sing Y N 285 
HIS CE1   HE1    sing N N 286 
HIS NE2   HE2    sing N N 287 
HIS OXT   HXT    sing N N 288 
ILE N     CA     sing N N 289 
ILE N     H      sing N N 290 
ILE N     H2     sing N N 291 
ILE CA    C      sing N N 292 
ILE CA    CB     sing N N 293 
ILE CA    HA     sing N N 294 
ILE C     O      doub N N 295 
ILE C     OXT    sing N N 296 
ILE CB    CG1    sing N N 297 
ILE CB    CG2    sing N N 298 
ILE CB    HB     sing N N 299 
ILE CG1   CD1    sing N N 300 
ILE CG1   HG12   sing N N 301 
ILE CG1   HG13   sing N N 302 
ILE CG2   HG21   sing N N 303 
ILE CG2   HG22   sing N N 304 
ILE CG2   HG23   sing N N 305 
ILE CD1   HD11   sing N N 306 
ILE CD1   HD12   sing N N 307 
ILE CD1   HD13   sing N N 308 
ILE OXT   HXT    sing N N 309 
LEU N     CA     sing N N 310 
LEU N     H      sing N N 311 
LEU N     H2     sing N N 312 
LEU CA    C      sing N N 313 
LEU CA    CB     sing N N 314 
LEU CA    HA     sing N N 315 
LEU C     O      doub N N 316 
LEU C     OXT    sing N N 317 
LEU CB    CG     sing N N 318 
LEU CB    HB2    sing N N 319 
LEU CB    HB3    sing N N 320 
LEU CG    CD1    sing N N 321 
LEU CG    CD2    sing N N 322 
LEU CG    HG     sing N N 323 
LEU CD1   HD11   sing N N 324 
LEU CD1   HD12   sing N N 325 
LEU CD1   HD13   sing N N 326 
LEU CD2   HD21   sing N N 327 
LEU CD2   HD22   sing N N 328 
LEU CD2   HD23   sing N N 329 
LEU OXT   HXT    sing N N 330 
LYS N     CA     sing N N 331 
LYS N     H      sing N N 332 
LYS N     H2     sing N N 333 
LYS CA    C      sing N N 334 
LYS CA    CB     sing N N 335 
LYS CA    HA     sing N N 336 
LYS C     O      doub N N 337 
LYS C     OXT    sing N N 338 
LYS CB    CG     sing N N 339 
LYS CB    HB2    sing N N 340 
LYS CB    HB3    sing N N 341 
LYS CG    CD     sing N N 342 
LYS CG    HG2    sing N N 343 
LYS CG    HG3    sing N N 344 
LYS CD    CE     sing N N 345 
LYS CD    HD2    sing N N 346 
LYS CD    HD3    sing N N 347 
LYS CE    NZ     sing N N 348 
LYS CE    HE2    sing N N 349 
LYS CE    HE3    sing N N 350 
LYS NZ    HZ1    sing N N 351 
LYS NZ    HZ2    sing N N 352 
LYS NZ    HZ3    sing N N 353 
LYS OXT   HXT    sing N N 354 
MET N     CA     sing N N 355 
MET N     H      sing N N 356 
MET N     H2     sing N N 357 
MET CA    C      sing N N 358 
MET CA    CB     sing N N 359 
MET CA    HA     sing N N 360 
MET C     O      doub N N 361 
MET C     OXT    sing N N 362 
MET CB    CG     sing N N 363 
MET CB    HB2    sing N N 364 
MET CB    HB3    sing N N 365 
MET CG    SD     sing N N 366 
MET CG    HG2    sing N N 367 
MET CG    HG3    sing N N 368 
MET SD    CE     sing N N 369 
MET CE    HE1    sing N N 370 
MET CE    HE2    sing N N 371 
MET CE    HE3    sing N N 372 
MET OXT   HXT    sing N N 373 
PHE N     CA     sing N N 374 
PHE N     H      sing N N 375 
PHE N     H2     sing N N 376 
PHE CA    C      sing N N 377 
PHE CA    CB     sing N N 378 
PHE CA    HA     sing N N 379 
PHE C     O      doub N N 380 
PHE C     OXT    sing N N 381 
PHE CB    CG     sing N N 382 
PHE CB    HB2    sing N N 383 
PHE CB    HB3    sing N N 384 
PHE CG    CD1    doub Y N 385 
PHE CG    CD2    sing Y N 386 
PHE CD1   CE1    sing Y N 387 
PHE CD1   HD1    sing N N 388 
PHE CD2   CE2    doub Y N 389 
PHE CD2   HD2    sing N N 390 
PHE CE1   CZ     doub Y N 391 
PHE CE1   HE1    sing N N 392 
PHE CE2   CZ     sing Y N 393 
PHE CE2   HE2    sing N N 394 
PHE CZ    HZ     sing N N 395 
PHE OXT   HXT    sing N N 396 
PRO N     CA     sing N N 397 
PRO N     CD     sing N N 398 
PRO N     H      sing N N 399 
PRO CA    C      sing N N 400 
PRO CA    CB     sing N N 401 
PRO CA    HA     sing N N 402 
PRO C     O      doub N N 403 
PRO C     OXT    sing N N 404 
PRO CB    CG     sing N N 405 
PRO CB    HB2    sing N N 406 
PRO CB    HB3    sing N N 407 
PRO CG    CD     sing N N 408 
PRO CG    HG2    sing N N 409 
PRO CG    HG3    sing N N 410 
PRO CD    HD2    sing N N 411 
PRO CD    HD3    sing N N 412 
PRO OXT   HXT    sing N N 413 
SER N     CA     sing N N 414 
SER N     H      sing N N 415 
SER N     H2     sing N N 416 
SER CA    C      sing N N 417 
SER CA    CB     sing N N 418 
SER CA    HA     sing N N 419 
SER C     O      doub N N 420 
SER C     OXT    sing N N 421 
SER CB    OG     sing N N 422 
SER CB    HB2    sing N N 423 
SER CB    HB3    sing N N 424 
SER OG    HG     sing N N 425 
SER OXT   HXT    sing N N 426 
TA1 O01   C01    sing N N 427 
TA1 O01   H011   sing N N 428 
TA1 C01   C02    sing N N 429 
TA1 C01   C43    sing N N 430 
TA1 C01   C45    sing N N 431 
TA1 C02   O02    sing N N 432 
TA1 C02   C10    sing N N 433 
TA1 C02   H021   sing N N 434 
TA1 O02   C03    sing N N 435 
TA1 C03   O03    doub N N 436 
TA1 C03   C04    sing N N 437 
TA1 C04   C05    doub Y N 438 
TA1 C04   C09    sing Y N 439 
TA1 C05   C06    sing Y N 440 
TA1 C05   H051   sing N N 441 
TA1 C06   C07    doub Y N 442 
TA1 C06   H061   sing N N 443 
TA1 C07   C08    sing Y N 444 
TA1 C07   HC71   sing N N 445 
TA1 C08   C09    doub Y N 446 
TA1 C08   H081   sing N N 447 
TA1 C09   H091   sing N N 448 
TA1 C10   C11    sing N N 449 
TA1 C10   C18    sing N N 450 
TA1 C10   H101   sing N N 451 
TA1 C11   O04    sing N N 452 
TA1 C11   C14    sing N N 453 
TA1 C11   C15    sing N N 454 
TA1 O04   C12    sing N N 455 
TA1 C12   O05    doub N N 456 
TA1 C12   C13    sing N N 457 
TA1 C13   H131   sing N N 458 
TA1 C13   H132   sing N N 459 
TA1 C13   H133   sing N N 460 
TA1 C14   O06    sing N N 461 
TA1 C14   H141   sing N N 462 
TA1 C14   H142   sing N N 463 
TA1 O06   C15    sing N N 464 
TA1 C15   C16    sing N N 465 
TA1 C15   H151   sing N N 466 
TA1 C16   C17    sing N N 467 
TA1 C16   H161   sing N N 468 
TA1 C16   H162   sing N N 469 
TA1 C17   O07    sing N N 470 
TA1 C17   C18    sing N N 471 
TA1 C17   H171   sing N N 472 
TA1 O07   H071   sing N N 473 
TA1 C18   C19    sing N N 474 
TA1 C18   C20    sing N N 475 
TA1 C19   H191   sing N N 476 
TA1 C19   H192   sing N N 477 
TA1 C19   H193   sing N N 478 
TA1 C20   O08    doub N N 479 
TA1 C20   C21    sing N N 480 
TA1 C21   O09    sing N N 481 
TA1 C21   C24    sing N N 482 
TA1 C21   H211   sing N N 483 
TA1 O09   C22    sing N N 484 
TA1 C22   O10    doub N N 485 
TA1 C22   C23    sing N N 486 
TA1 C23   H231   sing N N 487 
TA1 C23   H232   sing N N 488 
TA1 C23   H233   sing N N 489 
TA1 C24   C25    doub N N 490 
TA1 C24   C45    sing N N 491 
TA1 C25   C26    sing N N 492 
TA1 C25   C44    sing N N 493 
TA1 C26   O11    sing N N 494 
TA1 C26   C43    sing N N 495 
TA1 C26   H261   sing N N 496 
TA1 O11   C27    sing N N 497 
TA1 C27   O12    doub N N 498 
TA1 C27   C28    sing N N 499 
TA1 C28   O13    sing N N 500 
TA1 C28   C29    sing N N 501 
TA1 C28   H281   sing N N 502 
TA1 O13   HO11   sing N N 503 
TA1 C29   N01    sing N N 504 
TA1 C29   C37    sing N N 505 
TA1 C29   H291   sing N N 506 
TA1 N01   C30    sing N N 507 
TA1 N01   HN01   sing N N 508 
TA1 C30   O14    doub N N 509 
TA1 C30   C31    sing N N 510 
TA1 C31   C32    doub Y N 511 
TA1 C31   C36    sing Y N 512 
TA1 C32   C33    sing Y N 513 
TA1 C32   H321   sing N N 514 
TA1 C33   C34    doub Y N 515 
TA1 C33   H331   sing N N 516 
TA1 C34   C35    sing Y N 517 
TA1 C34   H341   sing N N 518 
TA1 C35   C36    doub Y N 519 
TA1 C35   H351   sing N N 520 
TA1 C36   H361   sing N N 521 
TA1 C37   C38    doub Y N 522 
TA1 C37   C42    sing Y N 523 
TA1 C38   C39    sing Y N 524 
TA1 C38   H381   sing N N 525 
TA1 C39   C40    doub Y N 526 
TA1 C39   H391   sing N N 527 
TA1 C40   C41    sing Y N 528 
TA1 C40   H401   sing N N 529 
TA1 C41   C42    doub Y N 530 
TA1 C41   H411   sing N N 531 
TA1 C42   H421   sing N N 532 
TA1 C43   H431   sing N N 533 
TA1 C43   H432   sing N N 534 
TA1 C44   H441   sing N N 535 
TA1 C44   H442   sing N N 536 
TA1 C44   H443   sing N N 537 
TA1 C45   C46    sing N N 538 
TA1 C45   C47    sing N N 539 
TA1 C46   H461   sing N N 540 
TA1 C46   H462   sing N N 541 
TA1 C46   H463   sing N N 542 
TA1 C47   H471   sing N N 543 
TA1 C47   H472   sing N N 544 
TA1 C47   H473   sing N N 545 
THR N     CA     sing N N 546 
THR N     H      sing N N 547 
THR N     H2     sing N N 548 
THR CA    C      sing N N 549 
THR CA    CB     sing N N 550 
THR CA    HA     sing N N 551 
THR C     O      doub N N 552 
THR C     OXT    sing N N 553 
THR CB    OG1    sing N N 554 
THR CB    CG2    sing N N 555 
THR CB    HB     sing N N 556 
THR OG1   HG1    sing N N 557 
THR CG2   HG21   sing N N 558 
THR CG2   HG22   sing N N 559 
THR CG2   HG23   sing N N 560 
THR OXT   HXT    sing N N 561 
TRP N     CA     sing N N 562 
TRP N     H      sing N N 563 
TRP N     H2     sing N N 564 
TRP CA    C      sing N N 565 
TRP CA    CB     sing N N 566 
TRP CA    HA     sing N N 567 
TRP C     O      doub N N 568 
TRP C     OXT    sing N N 569 
TRP CB    CG     sing N N 570 
TRP CB    HB2    sing N N 571 
TRP CB    HB3    sing N N 572 
TRP CG    CD1    doub Y N 573 
TRP CG    CD2    sing Y N 574 
TRP CD1   NE1    sing Y N 575 
TRP CD1   HD1    sing N N 576 
TRP CD2   CE2    doub Y N 577 
TRP CD2   CE3    sing Y N 578 
TRP NE1   CE2    sing Y N 579 
TRP NE1   HE1    sing N N 580 
TRP CE2   CZ2    sing Y N 581 
TRP CE3   CZ3    doub Y N 582 
TRP CE3   HE3    sing N N 583 
TRP CZ2   CH2    doub Y N 584 
TRP CZ2   HZ2    sing N N 585 
TRP CZ3   CH2    sing Y N 586 
TRP CZ3   HZ3    sing N N 587 
TRP CH2   HH2    sing N N 588 
TRP OXT   HXT    sing N N 589 
TYR N     CA     sing N N 590 
TYR N     H      sing N N 591 
TYR N     H2     sing N N 592 
TYR CA    C      sing N N 593 
TYR CA    CB     sing N N 594 
TYR CA    HA     sing N N 595 
TYR C     O      doub N N 596 
TYR C     OXT    sing N N 597 
TYR CB    CG     sing N N 598 
TYR CB    HB2    sing N N 599 
TYR CB    HB3    sing N N 600 
TYR CG    CD1    doub Y N 601 
TYR CG    CD2    sing Y N 602 
TYR CD1   CE1    sing Y N 603 
TYR CD1   HD1    sing N N 604 
TYR CD2   CE2    doub Y N 605 
TYR CD2   HD2    sing N N 606 
TYR CE1   CZ     doub Y N 607 
TYR CE1   HE1    sing N N 608 
TYR CE2   CZ     sing Y N 609 
TYR CE2   HE2    sing N N 610 
TYR CZ    OH     sing N N 611 
TYR OH    HH     sing N N 612 
TYR OXT   HXT    sing N N 613 
VAL N     CA     sing N N 614 
VAL N     H      sing N N 615 
VAL N     H2     sing N N 616 
VAL CA    C      sing N N 617 
VAL CA    CB     sing N N 618 
VAL CA    HA     sing N N 619 
VAL C     O      doub N N 620 
VAL C     OXT    sing N N 621 
VAL CB    CG1    sing N N 622 
VAL CB    CG2    sing N N 623 
VAL CB    HB     sing N N 624 
VAL CG1   HG11   sing N N 625 
VAL CG1   HG12   sing N N 626 
VAL CG1   HG13   sing N N 627 
VAL CG2   HG21   sing N N 628 
VAL CG2   HG22   sing N N 629 
VAL CG2   HG23   sing N N 630 
VAL OXT   HXT    sing N N 631 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-03 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9GNQ 
_em_admin.last_update        2024-11-20 
_em_admin.map_release_date   2024-11-20 
_em_admin.title              'Microtubule-associated Kif5B IAK tail mutant bound to ADP' 
# 
_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' 
# 
loop_
_em_entity_assembly_molwt.entity_assembly_id 
_em_entity_assembly_molwt.experimental_flag 
_em_entity_assembly_molwt.id 
_em_entity_assembly_molwt.units 
_em_entity_assembly_molwt.value 
1 NO 1 KILODALTONS/NANOMETER 246 
4 ?  2 ?                     ?   
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_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 
? ? 2 2 9606 'Homo sapiens' ? ? ? ? ? 
? ? 3 3 9823 'Sus scrofa'   ? ? ? ? ? 
? ? 4 4 9823 'Sus scrofa'   ? ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 2 2 562 'Escherichia coli' ? ? 
? 4 3 562 'Escherichia coli' ? ? 
# 
_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         52 
_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                     ? 
# 
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 
'PARTICLE SELECTION'       ? 1  1 ? ? RELION  3.0 
'IMAGE ACQUISITION'        ? 2  ? ? 1 EPU     ?   
MASKING                    ? 3  ? ? ? ?       ?   
'CTF CORRECTION'           ? 4  1 ? ? CTFFIND ?   
'LAYERLINE INDEXING'       ? 5  ? ? ? ?       ?   
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?       ?   
'MODEL FITTING'            ? 7  ? 1 ? ?       ?   
OTHER                      ? 8  ? ? ? ?       ?   
'MODEL REFINEMENT'         ? 9  ? 1 ? ?       ?   
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?       ?   
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? RELION  ?   
CLASSIFICATION             ? 12 1 ? ? RELION  ?   
RECONSTRUCTION             ? 13 1 ? ? RELION  ?   
# 
_em_specimen.concentration           1.16 
_em_specimen.details                 
;Kinesin 1mg/ml 
Microtubules at 0.16mg/ml
;
_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 
'Wellcome Trust'                                                 'United Kingdom' 206175/Z/17/Z 1 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/V006568/1  2 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/S000828/1  3 
# 
_atom_sites.entry_id                    9GNQ 
_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  
MG 
N  
O  
P  
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 1   ? 114.191 163.055 129.861 1.00 62.74  ? 1   MET B N     1 
ATOM   2    C  CA    . MET A 1 1   ? 115.237 162.678 128.922 1.00 60.80  ? 1   MET B CA    1 
ATOM   3    C  C     . MET A 1 1   ? 116.545 162.450 129.659 1.00 62.63  ? 1   MET B C     1 
ATOM   4    O  O     . MET A 1 1   ? 117.271 163.395 129.952 1.00 68.90  ? 1   MET B O     1 
ATOM   5    C  CB    . MET A 1 1   ? 115.413 163.756 127.855 1.00 66.37  ? 1   MET B CB    1 
ATOM   6    C  CG    . MET A 1 1   ? 115.972 163.245 126.544 1.00 68.39  ? 1   MET B CG    1 
ATOM   7    S  SD    . MET A 1 1   ? 114.798 162.212 125.654 1.00 79.12  ? 1   MET B SD    1 
ATOM   8    C  CE    . MET A 1 1   ? 113.436 163.353 125.444 1.00 64.96  ? 1   MET B CE    1 
ATOM   9    N  N     . ARG A 1 2   ? 116.834 161.186 129.960 1.00 55.96  ? 2   ARG B N     1 
ATOM   10   C  CA    . ARG A 1 2   ? 118.062 160.789 130.644 1.00 56.43  ? 2   ARG B CA    1 
ATOM   11   C  C     . ARG A 1 2   ? 118.196 161.495 131.994 1.00 53.75  ? 2   ARG B C     1 
ATOM   12   O  O     . ARG A 1 2   ? 119.107 162.288 132.230 1.00 57.32  ? 2   ARG B O     1 
ATOM   13   C  CB    . ARG A 1 2   ? 119.279 161.037 129.751 1.00 55.53  ? 2   ARG B CB    1 
ATOM   14   C  CG    . ARG A 1 2   ? 119.296 160.145 128.533 1.00 53.85  ? 2   ARG B CG    1 
ATOM   15   C  CD    . ARG A 1 2   ? 120.450 160.468 127.625 1.00 54.25  ? 2   ARG B CD    1 
ATOM   16   N  NE    . ARG A 1 2   ? 120.444 161.868 127.230 1.00 55.89  ? 2   ARG B NE    1 
ATOM   17   C  CZ    . ARG A 1 2   ? 121.340 162.420 126.425 1.00 54.33  ? 2   ARG B CZ    1 
ATOM   18   N  NH1   . ARG A 1 2   ? 122.327 161.712 125.901 1.00 54.19  ? 2   ARG B NH1   1 
ATOM   19   N  NH2   . ARG A 1 2   ? 121.243 163.714 126.138 1.00 52.60  ? 2   ARG B NH2   1 
ATOM   20   N  N     . GLU A 1 3   ? 117.258 161.188 132.881 1.00 50.54  ? 3   GLU B N     1 
ATOM   21   C  CA    . GLU A 1 3   ? 117.209 161.785 134.204 1.00 46.73  ? 3   GLU B CA    1 
ATOM   22   C  C     . GLU A 1 3   ? 118.047 160.986 135.192 1.00 53.54  ? 3   GLU B C     1 
ATOM   23   O  O     . GLU A 1 3   ? 118.228 159.776 135.048 1.00 59.00  ? 3   GLU B O     1 
ATOM   24   C  CB    . GLU A 1 3   ? 115.767 161.869 134.699 1.00 52.62  ? 3   GLU B CB    1 
ATOM   25   C  CG    . GLU A 1 3   ? 114.898 162.823 133.909 1.00 58.72  ? 3   GLU B CG    1 
ATOM   26   C  CD    . GLU A 1 3   ? 114.042 162.118 132.886 1.00 63.62  ? 3   GLU B CD    1 
ATOM   27   O  OE1   . GLU A 1 3   ? 114.134 160.878 132.789 1.00 67.38  ? 3   GLU B OE1   1 
ATOM   28   O  OE2   . GLU A 1 3   ? 113.274 162.802 132.179 1.00 61.13  ? 3   GLU B OE2   1 
ATOM   29   N  N     . ILE A 1 4   ? 118.552 161.679 136.208 1.00 51.58  ? 4   ILE B N     1 
ATOM   30   C  CA    . ILE A 1 4   ? 119.376 161.080 137.249 1.00 43.05  ? 4   ILE B CA    1 
ATOM   31   C  C     . ILE A 1 4   ? 118.704 161.309 138.594 1.00 47.41  ? 4   ILE B C     1 
ATOM   32   O  O     . ILE A 1 4   ? 118.376 162.448 138.944 1.00 56.75  ? 4   ILE B O     1 
ATOM   33   C  CB    . ILE A 1 4   ? 120.800 161.657 137.247 1.00 40.01  ? 4   ILE B CB    1 
ATOM   34   C  CG1   . ILE A 1 4   ? 121.582 161.125 136.052 1.00 49.24  ? 4   ILE B CG1   1 
ATOM   35   C  CG2   . ILE A 1 4   ? 121.514 161.314 138.531 1.00 46.11  ? 4   ILE B CG2   1 
ATOM   36   C  CD1   . ILE A 1 4   ? 123.028 161.507 136.060 1.00 49.12  ? 4   ILE B CD1   1 
ATOM   37   N  N     . VAL A 1 5   ? 118.502 160.229 139.343 1.00 38.33  ? 5   VAL B N     1 
ATOM   38   C  CA    . VAL A 1 5   ? 117.966 160.283 140.697 1.00 34.74  ? 5   VAL B CA    1 
ATOM   39   C  C     . VAL A 1 5   ? 119.130 160.248 141.674 1.00 41.85  ? 5   VAL B C     1 
ATOM   40   O  O     . VAL A 1 5   ? 120.012 159.389 141.566 1.00 51.38  ? 5   VAL B O     1 
ATOM   41   C  CB    . VAL A 1 5   ? 116.994 159.121 140.955 1.00 38.74  ? 5   VAL B CB    1 
ATOM   42   C  CG1   . VAL A 1 5   ? 116.472 159.174 142.367 1.00 41.29  ? 5   VAL B CG1   1 
ATOM   43   C  CG2   . VAL A 1 5   ? 115.850 159.164 139.971 1.00 45.70  ? 5   VAL B CG2   1 
ATOM   44   N  N     . HIS A 1 6   ? 119.138 161.172 142.628 1.00 44.45  ? 6   HIS B N     1 
ATOM   45   C  CA    . HIS A 1 6   ? 120.252 161.334 143.551 1.00 36.67  ? 6   HIS B CA    1 
ATOM   46   C  C     . HIS A 1 6   ? 119.837 160.932 144.959 1.00 46.12  ? 6   HIS B C     1 
ATOM   47   O  O     . HIS A 1 6   ? 118.753 161.301 145.419 1.00 58.04  ? 6   HIS B O     1 
ATOM   48   C  CB    . HIS A 1 6   ? 120.751 162.775 143.539 1.00 34.98  ? 6   HIS B CB    1 
ATOM   49   C  CG    . HIS A 1 6   ? 122.050 162.968 144.250 1.00 39.90  ? 6   HIS B CG    1 
ATOM   50   N  ND1   . HIS A 1 6   ? 123.214 162.353 143.851 1.00 54.34  ? 6   HIS B ND1   1 
ATOM   51   C  CD2   . HIS A 1 6   ? 122.368 163.708 145.336 1.00 44.79  ? 6   HIS B CD2   1 
ATOM   52   C  CE1   . HIS A 1 6   ? 124.195 162.703 144.662 1.00 55.08  ? 6   HIS B CE1   1 
ATOM   53   N  NE2   . HIS A 1 6   ? 123.709 163.526 145.571 1.00 54.54  ? 6   HIS B NE2   1 
ATOM   54   N  N     . ILE A 1 7   ? 120.698 160.173 145.635 1.00 34.70  ? 7   ILE B N     1 
ATOM   55   C  CA    . ILE A 1 7   ? 120.479 159.741 147.010 1.00 29.24  ? 7   ILE B CA    1 
ATOM   56   C  C     . ILE A 1 7   ? 121.698 160.119 147.839 1.00 38.17  ? 7   ILE B C     1 
ATOM   57   O  O     . ILE A 1 7   ? 122.835 159.906 147.407 1.00 50.02  ? 7   ILE B O     1 
ATOM   58   C  CB    . ILE A 1 7   ? 120.221 158.226 147.104 1.00 32.33  ? 7   ILE B CB    1 
ATOM   59   C  CG1   . ILE A 1 7   ? 119.130 157.803 146.130 1.00 37.60  ? 7   ILE B CG1   1 
ATOM   60   C  CG2   . ILE A 1 7   ? 119.835 157.841 148.517 1.00 40.00  ? 7   ILE B CG2   1 
ATOM   61   C  CD1   . ILE A 1 7   ? 118.867 156.334 146.137 1.00 44.35  ? 7   ILE B CD1   1 
ATOM   62   N  N     . GLN A 1 8   ? 121.465 160.681 149.021 1.00 39.06  ? 8   GLN B N     1 
ATOM   63   C  CA    . GLN A 1 8   ? 122.525 161.018 149.962 1.00 37.28  ? 8   GLN B CA    1 
ATOM   64   C  C     . GLN A 1 8   ? 122.290 160.284 151.272 1.00 41.23  ? 8   GLN B C     1 
ATOM   65   O  O     . GLN A 1 8   ? 121.211 160.395 151.861 1.00 49.39  ? 8   GLN B O     1 
ATOM   66   C  CB    . GLN A 1 8   ? 122.582 162.520 150.216 1.00 35.10  ? 8   GLN B CB    1 
ATOM   67   C  CG    . GLN A 1 8   ? 122.377 163.363 148.991 1.00 41.27  ? 8   GLN B CG    1 
ATOM   68   C  CD    . GLN A 1 8   ? 121.846 164.731 149.325 1.00 48.35  ? 8   GLN B CD    1 
ATOM   69   O  OE1   . GLN A 1 8   ? 121.725 165.092 150.492 1.00 46.20  ? 8   GLN B OE1   1 
ATOM   70   N  NE2   . GLN A 1 8   ? 121.523 165.506 148.298 1.00 47.83  ? 8   GLN B NE2   1 
ATOM   71   N  N     . ALA A 1 9   ? 123.299 159.553 151.737 1.00 36.53  ? 9   ALA B N     1 
ATOM   72   C  CA    . ALA A 1 9   ? 123.193 158.752 152.948 1.00 33.58  ? 9   ALA B CA    1 
ATOM   73   C  C     . ALA A 1 9   ? 124.271 159.160 153.938 1.00 40.61  ? 9   ALA B C     1 
ATOM   74   O  O     . ALA A 1 9   ? 125.440 159.289 153.570 1.00 52.77  ? 9   ALA B O     1 
ATOM   75   C  CB    . ALA A 1 9   ? 123.309 157.263 152.633 1.00 39.87  ? 9   ALA B CB    1 
ATOM   76   N  N     . GLY A 1 10  ? 123.875 159.349 155.190 1.00 36.54  ? 10  GLY B N     1 
ATOM   77   C  CA    . GLY A 1 10  ? 124.815 159.668 156.242 1.00 36.60  ? 10  GLY B CA    1 
ATOM   78   C  C     . GLY A 1 10  ? 125.197 161.131 156.273 1.00 43.92  ? 10  GLY B C     1 
ATOM   79   O  O     . GLY A 1 10  ? 124.730 161.955 155.487 1.00 53.60  ? 10  GLY B O     1 
ATOM   80   N  N     . GLN A 1 11  ? 126.077 161.458 157.218 1.00 37.62  ? 11  GLN B N     1 
ATOM   81   C  CA    . GLN A 1 11  ? 126.515 162.840 157.375 1.00 40.25  ? 11  GLN B CA    1 
ATOM   82   C  C     . GLN A 1 11  ? 127.414 163.271 156.223 1.00 44.76  ? 11  GLN B C     1 
ATOM   83   O  O     . GLN A 1 11  ? 127.204 164.333 155.618 1.00 54.11  ? 11  GLN B O     1 
ATOM   84   C  CB    . GLN A 1 11  ? 127.228 163.015 158.714 1.00 41.39  ? 11  GLN B CB    1 
ATOM   85   C  CG    . GLN A 1 11  ? 127.696 164.430 158.979 1.00 43.89  ? 11  GLN B CG    1 
ATOM   86   C  CD    . GLN A 1 11  ? 128.590 164.538 160.191 1.00 49.78  ? 11  GLN B CD    1 
ATOM   87   O  OE1   . GLN A 1 11  ? 128.997 163.533 160.767 1.00 51.12  ? 11  GLN B OE1   1 
ATOM   88   N  NE2   . GLN A 1 11  ? 128.903 165.764 160.586 1.00 52.02  ? 11  GLN B NE2   1 
ATOM   89   N  N     . CYS A 1 12  ? 128.412 162.450 155.894 1.00 38.70  ? 12  CYS B N     1 
ATOM   90   C  CA    . CYS A 1 12  ? 129.332 162.797 154.818 1.00 42.11  ? 12  CYS B CA    1 
ATOM   91   C  C     . CYS A 1 12  ? 128.594 162.950 153.496 1.00 50.93  ? 12  CYS B C     1 
ATOM   92   O  O     . CYS A 1 12  ? 128.794 163.931 152.766 1.00 58.01  ? 12  CYS B O     1 
ATOM   93   C  CB    . CYS A 1 12  ? 130.422 161.735 154.703 1.00 45.04  ? 12  CYS B CB    1 
ATOM   94   S  SG    . CYS A 1 12  ? 131.595 162.031 153.376 1.00 65.83  ? 12  CYS B SG    1 
ATOM   95   N  N     . GLY A 1 13  ? 127.729 161.989 153.178 1.00 40.61  ? 13  GLY B N     1 
ATOM   96   C  CA    . GLY A 1 13  ? 126.993 162.053 151.931 1.00 36.12  ? 13  GLY B CA    1 
ATOM   97   C  C     . GLY A 1 13  ? 126.076 163.253 151.858 1.00 43.89  ? 13  GLY B C     1 
ATOM   98   O  O     . GLY A 1 13  ? 125.999 163.922 150.829 1.00 54.40  ? 13  GLY B O     1 
ATOM   99   N  N     . ASN A 1 14  ? 125.376 163.548 152.952 1.00 39.87  ? 14  ASN B N     1 
ATOM   100  C  CA    . ASN A 1 14  ? 124.464 164.685 152.955 1.00 34.06  ? 14  ASN B CA    1 
ATOM   101  C  C     . ASN A 1 14  ? 125.213 165.995 152.761 1.00 39.01  ? 14  ASN B C     1 
ATOM   102  O  O     . ASN A 1 14  ? 124.758 166.872 152.018 1.00 46.41  ? 14  ASN B O     1 
ATOM   103  C  CB    . ASN A 1 14  ? 123.663 164.712 154.252 1.00 34.05  ? 14  ASN B CB    1 
ATOM   104  C  CG    . ASN A 1 14  ? 122.528 163.716 154.258 1.00 41.76  ? 14  ASN B CG    1 
ATOM   105  O  OD1   . ASN A 1 14  ? 122.395 162.905 153.350 1.00 48.16  ? 14  ASN B OD1   1 
ATOM   106  N  ND2   . ASN A 1 14  ? 121.706 163.767 155.292 1.00 45.42  ? 14  ASN B ND2   1 
ATOM   107  N  N     . GLN A 1 15  ? 126.365 166.151 153.415 1.00 39.10  ? 15  GLN B N     1 
ATOM   108  C  CA    . GLN A 1 15  ? 127.108 167.399 153.267 1.00 43.07  ? 15  GLN B CA    1 
ATOM   109  C  C     . GLN A 1 15  ? 127.698 167.545 151.864 1.00 48.45  ? 15  GLN B C     1 
ATOM   110  O  O     . GLN A 1 15  ? 127.607 168.625 151.252 1.00 52.18  ? 15  GLN B O     1 
ATOM   111  C  CB    . GLN A 1 15  ? 128.188 167.488 154.339 1.00 39.94  ? 15  GLN B CB    1 
ATOM   112  C  CG    . GLN A 1 15  ? 127.687 168.117 155.627 1.00 40.96  ? 15  GLN B CG    1 
ATOM   113  C  CD    . GLN A 1 15  ? 128.659 167.979 156.770 1.00 49.36  ? 15  GLN B CD    1 
ATOM   114  O  OE1   . GLN A 1 15  ? 128.836 166.897 157.320 1.00 54.12  ? 15  GLN B OE1   1 
ATOM   115  N  NE2   . GLN A 1 15  ? 129.300 169.080 157.136 1.00 48.14  ? 15  GLN B NE2   1 
ATOM   116  N  N     . ILE A 1 16  ? 128.285 166.471 151.326 1.00 40.87  ? 16  ILE B N     1 
ATOM   117  C  CA    . ILE A 1 16  ? 128.783 166.517 149.954 1.00 36.07  ? 16  ILE B CA    1 
ATOM   118  C  C     . ILE A 1 16  ? 127.645 166.834 148.993 1.00 44.18  ? 16  ILE B C     1 
ATOM   119  O  O     . ILE A 1 16  ? 127.813 167.608 148.044 1.00 52.98  ? 16  ILE B O     1 
ATOM   120  C  CB    . ILE A 1 16  ? 129.475 165.195 149.579 1.00 32.07  ? 16  ILE B CB    1 
ATOM   121  C  CG1   . ILE A 1 16  ? 130.683 164.924 150.476 1.00 40.90  ? 16  ILE B CG1   1 
ATOM   122  C  CG2   . ILE A 1 16  ? 129.885 165.211 148.120 1.00 44.13  ? 16  ILE B CG2   1 
ATOM   123  C  CD1   . ILE A 1 16  ? 132.000 165.355 149.893 1.00 47.57  ? 16  ILE B CD1   1 
ATOM   124  N  N     . GLY A 1 17  ? 126.467 166.256 149.229 1.00 41.18  ? 17  GLY B N     1 
ATOM   125  C  CA    . GLY A 1 17  ? 125.338 166.504 148.348 1.00 42.05  ? 17  GLY B CA    1 
ATOM   126  C  C     . GLY A 1 17  ? 124.820 167.926 148.420 1.00 43.13  ? 17  GLY B C     1 
ATOM   127  O  O     . GLY A 1 17  ? 124.408 168.494 147.409 1.00 51.71  ? 17  GLY B O     1 
ATOM   128  N  N     . ALA A 1 18  ? 124.814 168.516 149.614 1.00 32.04  ? 18  ALA B N     1 
ATOM   129  C  CA    . ALA A 1 18  ? 124.411 169.911 149.739 1.00 33.37  ? 18  ALA B CA    1 
ATOM   130  C  C     . ALA A 1 18  ? 125.353 170.822 148.966 1.00 43.71  ? 18  ALA B C     1 
ATOM   131  O  O     . ALA A 1 18  ? 124.912 171.713 148.222 1.00 50.74  ? 18  ALA B O     1 
ATOM   132  C  CB    . ALA A 1 18  ? 124.361 170.310 151.211 1.00 35.99  ? 18  ALA B CB    1 
ATOM   133  N  N     . LYS A 1 19  ? 126.661 170.598 149.109 1.00 45.48  ? 19  LYS B N     1 
ATOM   134  C  CA    . LYS A 1 19  ? 127.612 171.385 148.327 1.00 41.71  ? 19  LYS B CA    1 
ATOM   135  C  C     . LYS A 1 19  ? 127.414 171.158 146.832 1.00 47.11  ? 19  LYS B C     1 
ATOM   136  O  O     . LYS A 1 19  ? 127.477 172.103 146.031 1.00 55.09  ? 19  LYS B O     1 
ATOM   137  C  CB    . LYS A 1 19  ? 129.040 171.046 148.740 1.00 42.83  ? 19  LYS B CB    1 
ATOM   138  C  CG    . LYS A 1 19  ? 130.098 171.821 147.986 1.00 52.08  ? 19  LYS B CG    1 
ATOM   139  C  CD    . LYS A 1 19  ? 129.960 173.308 148.219 1.00 49.05  ? 19  LYS B CD    1 
ATOM   140  C  CE    . LYS A 1 19  ? 130.291 173.669 149.646 1.00 50.44  ? 19  LYS B CE    1 
ATOM   141  N  NZ    . LYS A 1 19  ? 130.384 175.140 149.824 1.00 54.50  ? 19  LYS B NZ    1 
ATOM   142  N  N     . PHE A 1 20  ? 127.143 169.913 146.444 1.00 37.85  ? 20  PHE B N     1 
ATOM   143  C  CA    . PHE A 1 20  ? 126.932 169.585 145.042 1.00 33.22  ? 20  PHE B CA    1 
ATOM   144  C  C     . PHE A 1 20  ? 125.718 170.306 144.480 1.00 35.94  ? 20  PHE B C     1 
ATOM   145  O  O     . PHE A 1 20  ? 125.745 170.794 143.345 1.00 49.28  ? 20  PHE B O     1 
ATOM   146  C  CB    . PHE A 1 20  ? 126.778 168.075 144.898 1.00 38.15  ? 20  PHE B CB    1 
ATOM   147  C  CG    . PHE A 1 20  ? 126.348 167.631 143.541 1.00 40.92  ? 20  PHE B CG    1 
ATOM   148  C  CD1   . PHE A 1 20  ? 127.235 167.628 142.489 1.00 43.05  ? 20  PHE B CD1   1 
ATOM   149  C  CD2   . PHE A 1 20  ? 125.064 167.191 143.321 1.00 42.15  ? 20  PHE B CD2   1 
ATOM   150  C  CE1   . PHE A 1 20  ? 126.844 167.209 141.248 1.00 41.38  ? 20  PHE B CE1   1 
ATOM   151  C  CE2   . PHE A 1 20  ? 124.672 166.775 142.077 1.00 39.35  ? 20  PHE B CE2   1 
ATOM   152  C  CZ    . PHE A 1 20  ? 125.563 166.782 141.045 1.00 39.24  ? 20  PHE B CZ    1 
ATOM   153  N  N     . TRP A 1 21  ? 124.642 170.383 145.257 1.00 42.96  ? 21  TRP B N     1 
ATOM   154  C  CA    . TRP A 1 21  ? 123.429 171.020 144.762 1.00 43.39  ? 21  TRP B CA    1 
ATOM   155  C  C     . TRP A 1 21  ? 123.594 172.527 144.682 1.00 41.62  ? 21  TRP B C     1 
ATOM   156  O  O     . TRP A 1 21  ? 123.088 173.160 143.749 1.00 49.87  ? 21  TRP B O     1 
ATOM   157  C  CB    . TRP A 1 21  ? 122.242 170.632 145.633 1.00 36.79  ? 21  TRP B CB    1 
ATOM   158  C  CG    . TRP A 1 21  ? 121.724 169.294 145.262 1.00 34.47  ? 21  TRP B CG    1 
ATOM   159  C  CD1   . TRP A 1 21  ? 121.802 168.157 145.996 1.00 41.21  ? 21  TRP B CD1   1 
ATOM   160  C  CD2   . TRP A 1 21  ? 121.073 168.941 144.043 1.00 34.85  ? 21  TRP B CD2   1 
ATOM   161  N  NE1   . TRP A 1 21  ? 121.231 167.116 145.318 1.00 43.19  ? 21  TRP B NE1   1 
ATOM   162  C  CE2   . TRP A 1 21  ? 120.772 167.575 144.114 1.00 35.16  ? 21  TRP B CE2   1 
ATOM   163  C  CE3   . TRP A 1 21  ? 120.702 169.651 142.904 1.00 41.43  ? 21  TRP B CE3   1 
ATOM   164  C  CZ2   . TRP A 1 21  ? 120.124 166.905 143.091 1.00 35.27  ? 21  TRP B CZ2   1 
ATOM   165  C  CZ3   . TRP A 1 21  ? 120.063 168.984 141.892 1.00 40.34  ? 21  TRP B CZ3   1 
ATOM   166  C  CH2   . TRP A 1 21  ? 119.779 167.628 141.989 1.00 38.18  ? 21  TRP B CH2   1 
ATOM   167  N  N     . GLU A 1 22  ? 124.339 173.116 145.617 1.00 45.72  ? 22  GLU B N     1 
ATOM   168  C  CA    . GLU A 1 22  ? 124.669 174.530 145.483 1.00 45.23  ? 22  GLU B CA    1 
ATOM   169  C  C     . GLU A 1 22  ? 125.457 174.792 144.203 1.00 49.88  ? 22  GLU B C     1 
ATOM   170  O  O     . GLU A 1 22  ? 125.153 175.731 143.455 1.00 54.39  ? 22  GLU B O     1 
ATOM   171  C  CB    . GLU A 1 22  ? 125.454 175.001 146.703 1.00 49.30  ? 22  GLU B CB    1 
ATOM   172  C  CG    . GLU A 1 22  ? 125.884 176.445 146.638 1.00 54.76  ? 22  GLU B CG    1 
ATOM   173  C  CD    . GLU A 1 22  ? 126.651 176.871 147.869 1.00 63.26  ? 22  GLU B CD    1 
ATOM   174  O  OE1   . GLU A 1 22  ? 126.877 176.018 148.752 1.00 62.85  ? 22  GLU B OE1   1 
ATOM   175  O  OE2   . GLU A 1 22  ? 127.027 178.059 147.957 1.00 65.38  ? 22  GLU B OE2   1 
ATOM   176  N  N     . VAL A 1 23  ? 126.450 173.948 143.917 1.00 49.46  ? 23  VAL B N     1 
ATOM   177  C  CA    . VAL A 1 23  ? 127.276 174.139 142.726 1.00 44.49  ? 23  VAL B CA    1 
ATOM   178  C  C     . VAL A 1 23  ? 126.447 173.980 141.454 1.00 47.86  ? 23  VAL B C     1 
ATOM   179  O  O     . VAL A 1 23  ? 126.541 174.792 140.524 1.00 54.60  ? 23  VAL B O     1 
ATOM   180  C  CB    . VAL A 1 23  ? 128.465 173.163 142.749 1.00 50.16  ? 23  VAL B CB    1 
ATOM   181  C  CG1   . VAL A 1 23  ? 128.927 172.861 141.351 1.00 51.29  ? 23  VAL B CG1   1 
ATOM   182  C  CG2   . VAL A 1 23  ? 129.597 173.729 143.579 1.00 54.93  ? 23  VAL B CG2   1 
ATOM   183  N  N     . ILE A 1 24  ? 125.625 172.930 141.390 1.00 46.19  ? 24  ILE B N     1 
ATOM   184  C  CA    . ILE A 1 24  ? 124.823 172.674 140.196 1.00 43.08  ? 24  ILE B CA    1 
ATOM   185  C  C     . ILE A 1 24  ? 123.816 173.795 139.977 1.00 46.58  ? 24  ILE B C     1 
ATOM   186  O  O     . ILE A 1 24  ? 123.613 174.254 138.846 1.00 50.77  ? 24  ILE B O     1 
ATOM   187  C  CB    . ILE A 1 24  ? 124.136 171.299 140.300 1.00 41.59  ? 24  ILE B CB    1 
ATOM   188  C  CG1   . ILE A 1 24  ? 125.094 170.184 139.889 1.00 47.00  ? 24  ILE B CG1   1 
ATOM   189  C  CG2   . ILE A 1 24  ? 122.904 171.244 139.436 1.00 44.69  ? 24  ILE B CG2   1 
ATOM   190  C  CD1   . ILE A 1 24  ? 125.505 170.232 138.447 1.00 52.52  ? 24  ILE B CD1   1 
ATOM   191  N  N     . SER A 1 25  ? 123.171 174.258 141.051 1.00 50.51  ? 25  SER B N     1 
ATOM   192  C  CA    . SER A 1 25  ? 122.218 175.352 140.917 1.00 45.59  ? 25  SER B CA    1 
ATOM   193  C  C     . SER A 1 25  ? 122.904 176.620 140.438 1.00 41.24  ? 25  SER B C     1 
ATOM   194  O  O     . SER A 1 25  ? 122.342 177.368 139.632 1.00 49.84  ? 25  SER B O     1 
ATOM   195  C  CB    . SER A 1 25  ? 121.506 175.589 142.246 1.00 50.42  ? 25  SER B CB    1 
ATOM   196  O  OG    . SER A 1 25  ? 120.865 174.409 142.692 1.00 54.21  ? 25  SER B OG    1 
ATOM   197  N  N     . ASP A 1 26  ? 124.119 176.883 140.921 1.00 46.86  ? 26  ASP B N     1 
ATOM   198  C  CA    . ASP A 1 26  ? 124.864 178.030 140.415 1.00 49.93  ? 26  ASP B CA    1 
ATOM   199  C  C     . ASP A 1 26  ? 125.161 177.878 138.930 1.00 52.37  ? 26  ASP B C     1 
ATOM   200  O  O     . ASP A 1 26  ? 125.084 178.849 138.171 1.00 55.70  ? 26  ASP B O     1 
ATOM   201  C  CB    . ASP A 1 26  ? 126.158 178.209 141.205 1.00 58.63  ? 26  ASP B CB    1 
ATOM   202  C  CG    . ASP A 1 26  ? 126.974 179.390 140.723 1.00 64.34  ? 26  ASP B CG    1 
ATOM   203  O  OD1   . ASP A 1 26  ? 126.374 180.369 140.232 1.00 64.74  ? 26  ASP B OD1   1 
ATOM   204  O  OD2   . ASP A 1 26  ? 128.217 179.342 140.836 1.00 63.14  ? 26  ASP B OD2   1 
ATOM   205  N  N     . GLU A 1 27  ? 125.510 176.665 138.500 1.00 58.03  ? 27  GLU B N     1 
ATOM   206  C  CA    . GLU A 1 27  ? 125.793 176.435 137.086 1.00 52.83  ? 27  GLU B CA    1 
ATOM   207  C  C     . GLU A 1 27  ? 124.557 176.648 136.223 1.00 54.92  ? 27  GLU B C     1 
ATOM   208  O  O     . GLU A 1 27  ? 124.654 177.170 135.108 1.00 57.30  ? 27  GLU B O     1 
ATOM   209  C  CB    . GLU A 1 27  ? 126.344 175.025 136.883 1.00 54.36  ? 27  GLU B CB    1 
ATOM   210  C  CG    . GLU A 1 27  ? 126.801 174.739 135.471 1.00 56.87  ? 27  GLU B CG    1 
ATOM   211  C  CD    . GLU A 1 27  ? 127.620 173.473 135.376 1.00 66.50  ? 27  GLU B CD    1 
ATOM   212  O  OE1   . GLU A 1 27  ? 127.843 172.832 136.423 1.00 68.27  ? 27  GLU B OE1   1 
ATOM   213  O  OE2   . GLU A 1 27  ? 128.045 173.119 134.256 1.00 65.30  ? 27  GLU B OE2   1 
ATOM   214  N  N     . HIS A 1 28  ? 123.390 176.243 136.710 1.00 52.95  ? 28  HIS B N     1 
ATOM   215  C  CA    . HIS A 1 28  ? 122.163 176.343 135.933 1.00 44.19  ? 28  HIS B CA    1 
ATOM   216  C  C     . HIS A 1 28  ? 121.389 177.630 136.191 1.00 47.00  ? 28  HIS B C     1 
ATOM   217  O  O     . HIS A 1 28  ? 120.298 177.798 135.642 1.00 47.06  ? 28  HIS B O     1 
ATOM   218  C  CB    . HIS A 1 28  ? 121.272 175.135 136.214 1.00 46.15  ? 28  HIS B CB    1 
ATOM   219  C  CG    . HIS A 1 28  ? 121.597 173.942 135.375 1.00 47.16  ? 28  HIS B CG    1 
ATOM   220  N  ND1   . HIS A 1 28  ? 121.056 173.739 134.126 1.00 48.96  ? 28  HIS B ND1   1 
ATOM   221  C  CD2   . HIS A 1 28  ? 122.432 172.901 135.596 1.00 48.60  ? 28  HIS B CD2   1 
ATOM   222  C  CE1   . HIS A 1 28  ? 121.527 172.614 133.622 1.00 45.35  ? 28  HIS B CE1   1 
ATOM   223  N  NE2   . HIS A 1 28  ? 122.369 172.089 134.492 1.00 47.90  ? 28  HIS B NE2   1 
ATOM   224  N  N     . GLY A 1 29  ? 121.926 178.538 136.999 1.00 51.04  ? 29  GLY B N     1 
ATOM   225  C  CA    . GLY A 1 29  ? 121.287 179.815 137.239 1.00 45.70  ? 29  GLY B CA    1 
ATOM   226  C  C     . GLY A 1 29  ? 119.982 179.737 137.999 1.00 50.43  ? 29  GLY B C     1 
ATOM   227  O  O     . GLY A 1 29  ? 118.985 180.331 137.584 1.00 57.93  ? 29  GLY B O     1 
ATOM   228  N  N     . ILE A 1 30  ? 119.968 179.012 139.114 1.00 46.37  ? 30  ILE B N     1 
ATOM   229  C  CA    . ILE A 1 30  ? 118.765 178.815 139.909 1.00 37.26  ? 30  ILE B CA    1 
ATOM   230  C  C     . ILE A 1 30  ? 118.969 179.443 141.281 1.00 43.23  ? 30  ILE B C     1 
ATOM   231  O  O     . ILE A 1 30  ? 119.946 179.139 141.973 1.00 50.98  ? 30  ILE B O     1 
ATOM   232  C  CB    . ILE A 1 30  ? 118.402 177.326 140.033 1.00 45.92  ? 30  ILE B CB    1 
ATOM   233  C  CG1   . ILE A 1 30  ? 117.873 176.798 138.704 1.00 48.12  ? 30  ILE B CG1   1 
ATOM   234  C  CG2   . ILE A 1 30  ? 117.374 177.120 141.117 1.00 48.94  ? 30  ILE B CG2   1 
ATOM   235  C  CD1   . ILE A 1 30  ? 117.312 175.408 138.784 1.00 49.51  ? 30  ILE B CD1   1 
ATOM   236  N  N     . ASP A 1 31  ? 118.039 180.311 141.666 1.00 56.54  ? 31  ASP B N     1 
ATOM   237  C  CA    . ASP A 1 31  ? 118.047 180.965 142.962 1.00 53.27  ? 31  ASP B CA    1 
ATOM   238  C  C     . ASP A 1 31  ? 117.729 179.955 144.065 1.00 57.48  ? 31  ASP B C     1 
ATOM   239  O  O     . ASP A 1 31  ? 117.159 178.895 143.801 1.00 64.41  ? 31  ASP B O     1 
ATOM   240  C  CB    . ASP A 1 31  ? 117.022 182.100 142.956 1.00 56.59  ? 31  ASP B CB    1 
ATOM   241  C  CG    . ASP A 1 31  ? 117.140 183.018 144.152 1.00 63.55  ? 31  ASP B CG    1 
ATOM   242  O  OD1   . ASP A 1 31  ? 116.523 182.719 145.196 1.00 66.52  ? 31  ASP B OD1   1 
ATOM   243  O  OD2   . ASP A 1 31  ? 117.848 184.041 144.050 1.00 64.19  ? 31  ASP B OD2   1 
ATOM   244  N  N     . PRO A 1 32  ? 118.106 180.253 145.311 1.00 50.61  ? 32  PRO B N     1 
ATOM   245  C  CA    . PRO A 1 32  ? 117.717 179.373 146.424 1.00 47.54  ? 32  PRO B CA    1 
ATOM   246  C  C     . PRO A 1 32  ? 116.226 179.119 146.538 1.00 56.32  ? 32  PRO B C     1 
ATOM   247  O  O     . PRO A 1 32  ? 115.828 178.027 146.958 1.00 62.36  ? 32  PRO B O     1 
ATOM   248  C  CB    . PRO A 1 32  ? 118.241 180.118 147.656 1.00 48.03  ? 32  PRO B CB    1 
ATOM   249  C  CG    . PRO A 1 32  ? 119.242 181.095 147.155 1.00 53.08  ? 32  PRO B CG    1 
ATOM   250  C  CD    . PRO A 1 32  ? 119.267 181.081 145.663 1.00 54.54  ? 32  PRO B CD    1 
ATOM   251  N  N     . THR A 1 33  ? 115.382 180.090 146.191 1.00 58.12  ? 33  THR B N     1 
ATOM   252  C  CA    . THR A 1 33  ? 113.942 179.882 146.265 1.00 57.80  ? 33  THR B CA    1 
ATOM   253  C  C     . THR A 1 33  ? 113.426 178.937 145.192 1.00 52.59  ? 33  THR B C     1 
ATOM   254  O  O     . THR A 1 33  ? 112.255 178.552 145.245 1.00 55.65  ? 33  THR B O     1 
ATOM   255  C  CB    . THR A 1 33  ? 113.205 181.217 146.157 1.00 59.89  ? 33  THR B CB    1 
ATOM   256  O  OG1   . THR A 1 33  ? 113.358 181.743 144.833 1.00 60.09  ? 33  THR B OG1   1 
ATOM   257  C  CG2   . THR A 1 33  ? 113.761 182.216 147.158 1.00 58.10  ? 33  THR B CG2   1 
ATOM   258  N  N     . GLY A 1 34  ? 114.255 178.562 144.228 1.00 50.05  ? 34  GLY B N     1 
ATOM   259  C  CA    . GLY A 1 34  ? 113.824 177.730 143.130 1.00 51.23  ? 34  GLY B CA    1 
ATOM   260  C  C     . GLY A 1 34  ? 113.517 178.465 141.849 1.00 56.47  ? 34  GLY B C     1 
ATOM   261  O  O     . GLY A 1 34  ? 113.033 177.838 140.901 1.00 63.14  ? 34  GLY B O     1 
ATOM   262  N  N     . SER A 1 35  ? 113.771 179.765 141.788 1.00 56.58  ? 35  SER B N     1 
ATOM   263  C  CA    . SER A 1 35  ? 113.483 180.559 140.606 1.00 55.46  ? 35  SER B CA    1 
ATOM   264  C  C     . SER A 1 35  ? 114.691 180.615 139.679 1.00 58.37  ? 35  SER B C     1 
ATOM   265  O  O     . SER A 1 35  ? 115.823 180.335 140.073 1.00 64.69  ? 35  SER B O     1 
ATOM   266  C  CB    . SER A 1 35  ? 113.062 181.973 140.998 1.00 58.57  ? 35  SER B CB    1 
ATOM   267  O  OG    . SER A 1 35  ? 111.967 181.944 141.892 1.00 62.97  ? 35  SER B OG    1 
ATOM   268  N  N     . TYR A 1 36  ? 114.431 180.988 138.432 1.00 57.02  ? 36  TYR B N     1 
ATOM   269  C  CA    . TYR A 1 36  ? 115.445 181.048 137.390 1.00 54.07  ? 36  TYR B CA    1 
ATOM   270  C  C     . TYR A 1 36  ? 115.853 182.497 137.164 1.00 56.73  ? 36  TYR B C     1 
ATOM   271  O  O     . TYR A 1 36  ? 115.012 183.336 136.828 1.00 59.88  ? 36  TYR B O     1 
ATOM   272  C  CB    . TYR A 1 36  ? 114.925 180.436 136.093 1.00 54.60  ? 36  TYR B CB    1 
ATOM   273  C  CG    . TYR A 1 36  ? 115.881 180.586 134.941 1.00 55.34  ? 36  TYR B CG    1 
ATOM   274  C  CD1   . TYR A 1 36  ? 117.010 179.794 134.850 1.00 56.20  ? 36  TYR B CD1   1 
ATOM   275  C  CD2   . TYR A 1 36  ? 115.659 181.519 133.948 1.00 58.97  ? 36  TYR B CD2   1 
ATOM   276  C  CE1   . TYR A 1 36  ? 117.888 179.929 133.808 1.00 59.10  ? 36  TYR B CE1   1 
ATOM   277  C  CE2   . TYR A 1 36  ? 116.534 181.659 132.899 1.00 57.42  ? 36  TYR B CE2   1 
ATOM   278  C  CZ    . TYR A 1 36  ? 117.646 180.861 132.834 1.00 58.01  ? 36  TYR B CZ    1 
ATOM   279  O  OH    . TYR A 1 36  ? 118.521 180.999 131.785 1.00 60.55  ? 36  TYR B OH    1 
ATOM   280  N  N     . HIS A 1 37  ? 117.137 182.785 137.339 1.00 64.24  ? 37  HIS B N     1 
ATOM   281  C  CA    . HIS A 1 37  ? 117.690 184.110 137.103 1.00 62.05  ? 37  HIS B CA    1 
ATOM   282  C  C     . HIS A 1 37  ? 118.961 184.016 136.277 1.00 66.75  ? 37  HIS B C     1 
ATOM   283  O  O     . HIS A 1 37  ? 119.959 184.685 136.556 1.00 72.01  ? 37  HIS B O     1 
ATOM   284  C  CB    . HIS A 1 37  ? 117.953 184.835 138.418 1.00 65.08  ? 37  HIS B CB    1 
ATOM   285  C  CG    . HIS A 1 37  ? 116.732 185.455 139.018 1.00 72.18  ? 37  HIS B CG    1 
ATOM   286  N  ND1   . HIS A 1 37  ? 115.658 184.711 139.455 1.00 77.88  ? 37  HIS B ND1   1 
ATOM   287  C  CD2   . HIS A 1 37  ? 116.415 186.749 139.256 1.00 72.79  ? 37  HIS B CD2   1 
ATOM   288  C  CE1   . HIS A 1 37  ? 114.731 185.521 139.936 1.00 75.98  ? 37  HIS B CE1   1 
ATOM   289  N  NE2   . HIS A 1 37  ? 115.166 186.763 139.826 1.00 75.70  ? 37  HIS B NE2   1 
ATOM   290  N  N     . GLY A 1 38  ? 118.943 183.181 135.245 1.00 66.00  ? 38  GLY B N     1 
ATOM   291  C  CA    . GLY A 1 38  ? 120.096 182.986 134.398 1.00 69.44  ? 38  GLY B CA    1 
ATOM   292  C  C     . GLY A 1 38  ? 120.179 184.017 133.291 1.00 71.63  ? 38  GLY B C     1 
ATOM   293  O  O     . GLY A 1 38  ? 119.451 185.010 133.255 1.00 72.50  ? 38  GLY B O     1 
ATOM   294  N  N     . ASP A 1 39  ? 121.099 183.761 132.362 1.00 70.63  ? 39  ASP B N     1 
ATOM   295  C  CA    . ASP A 1 39  ? 121.301 184.660 131.235 1.00 68.57  ? 39  ASP B CA    1 
ATOM   296  C  C     . ASP A 1 39  ? 121.484 183.920 129.915 1.00 70.59  ? 39  ASP B C     1 
ATOM   297  O  O     . ASP A 1 39  ? 121.926 184.536 128.938 1.00 70.92  ? 39  ASP B O     1 
ATOM   298  C  CB    . ASP A 1 39  ? 122.508 185.562 131.490 1.00 71.34  ? 39  ASP B CB    1 
ATOM   299  C  CG    . ASP A 1 39  ? 123.726 184.787 131.936 1.00 73.89  ? 39  ASP B CG    1 
ATOM   300  O  OD1   . ASP A 1 39  ? 123.585 183.583 132.230 1.00 71.67  ? 39  ASP B OD1   1 
ATOM   301  O  OD2   . ASP A 1 39  ? 124.823 185.378 131.993 1.00 75.54  ? 39  ASP B OD2   1 
ATOM   302  N  N     . SER A 1 40  ? 121.163 182.631 129.850 1.00 70.37  ? 40  SER B N     1 
ATOM   303  C  CA    . SER A 1 40  ? 121.332 181.863 128.627 1.00 67.65  ? 40  SER B CA    1 
ATOM   304  C  C     . SER A 1 40  ? 120.264 180.783 128.555 1.00 69.70  ? 40  SER B C     1 
ATOM   305  O  O     . SER A 1 40  ? 119.768 180.311 129.581 1.00 71.47  ? 40  SER B O     1 
ATOM   306  C  CB    . SER A 1 40  ? 122.724 181.231 128.554 1.00 68.12  ? 40  SER B CB    1 
ATOM   307  O  OG    . SER A 1 40  ? 122.873 180.472 127.370 1.00 72.19  ? 40  SER B OG    1 
ATOM   308  N  N     . ASP A 1 41  ? 119.915 180.396 127.327 1.00 64.80  ? 41  ASP B N     1 
ATOM   309  C  CA    . ASP A 1 41  ? 118.911 179.359 127.124 1.00 67.15  ? 41  ASP B CA    1 
ATOM   310  C  C     . ASP A 1 41  ? 119.465 177.963 127.371 1.00 72.06  ? 41  ASP B C     1 
ATOM   311  O  O     . ASP A 1 41  ? 118.713 177.057 127.759 1.00 79.33  ? 41  ASP B O     1 
ATOM   312  C  CB    . ASP A 1 41  ? 118.346 179.452 125.708 1.00 70.29  ? 41  ASP B CB    1 
ATOM   313  C  CG    . ASP A 1 41  ? 117.907 180.852 125.352 1.00 75.06  ? 41  ASP B CG    1 
ATOM   314  O  OD1   . ASP A 1 41  ? 118.091 181.760 126.188 1.00 77.76  ? 41  ASP B OD1   1 
ATOM   315  O  OD2   . ASP A 1 41  ? 117.378 181.047 124.237 1.00 73.95  ? 41  ASP B OD2   1 
ATOM   316  N  N     . LEU A 1 42  ? 120.766 177.767 127.147 1.00 59.91  ? 42  LEU B N     1 
ATOM   317  C  CA    . LEU A 1 42  ? 121.370 176.462 127.366 1.00 56.31  ? 42  LEU B CA    1 
ATOM   318  C  C     . LEU A 1 42  ? 121.279 176.025 128.817 1.00 61.42  ? 42  LEU B C     1 
ATOM   319  O  O     . LEU A 1 42  ? 121.337 174.824 129.097 1.00 62.97  ? 42  LEU B O     1 
ATOM   320  C  CB    . LEU A 1 42  ? 122.830 176.475 126.921 1.00 54.18  ? 42  LEU B CB    1 
ATOM   321  C  CG    . LEU A 1 42  ? 123.087 176.673 125.432 1.00 55.81  ? 42  LEU B CG    1 
ATOM   322  C  CD1   . LEU A 1 42  ? 123.401 178.125 125.142 1.00 58.64  ? 42  LEU B CD1   1 
ATOM   323  C  CD2   . LEU A 1 42  ? 124.211 175.778 124.961 1.00 59.14  ? 42  LEU B CD2   1 
ATOM   324  N  N     . GLN A 1 43  ? 121.142 176.971 129.745 1.00 53.77  ? 43  GLN B N     1 
ATOM   325  C  CA    . GLN A 1 43  ? 120.959 176.609 131.143 1.00 48.70  ? 43  GLN B CA    1 
ATOM   326  C  C     . GLN A 1 43  ? 119.642 175.874 131.358 1.00 54.01  ? 43  GLN B C     1 
ATOM   327  O  O     . GLN A 1 43  ? 119.590 174.893 132.107 1.00 59.59  ? 43  GLN B O     1 
ATOM   328  C  CB    . GLN A 1 43  ? 121.031 177.858 132.018 1.00 52.40  ? 43  GLN B CB    1 
ATOM   329  C  CG    . GLN A 1 43  ? 122.379 178.542 131.997 1.00 50.68  ? 43  GLN B CG    1 
ATOM   330  C  CD    . GLN A 1 43  ? 122.469 179.682 132.978 1.00 54.05  ? 43  GLN B CD    1 
ATOM   331  O  OE1   . GLN A 1 43  ? 121.458 180.203 133.435 1.00 62.51  ? 43  GLN B OE1   1 
ATOM   332  N  NE2   . GLN A 1 43  ? 123.687 180.076 133.311 1.00 51.29  ? 43  GLN B NE2   1 
ATOM   333  N  N     . LEU A 1 44  ? 118.572 176.328 130.715 1.00 50.77  ? 44  LEU B N     1 
ATOM   334  C  CA    . LEU A 1 44  ? 117.264 175.706 130.864 1.00 49.44  ? 44  LEU B CA    1 
ATOM   335  C  C     . LEU A 1 44  ? 116.993 174.613 129.843 1.00 48.14  ? 44  LEU B C     1 
ATOM   336  O  O     . LEU A 1 44  ? 115.975 173.925 129.960 1.00 52.49  ? 44  LEU B O     1 
ATOM   337  C  CB    . LEU A 1 44  ? 116.161 176.762 130.755 1.00 50.77  ? 44  LEU B CB    1 
ATOM   338  C  CG    . LEU A 1 44  ? 115.880 177.631 131.976 1.00 56.50  ? 44  LEU B CG    1 
ATOM   339  C  CD1   . LEU A 1 44  ? 114.891 178.726 131.626 1.00 53.16  ? 44  LEU B CD1   1 
ATOM   340  C  CD2   . LEU A 1 44  ? 115.356 176.784 133.119 1.00 58.13  ? 44  LEU B CD2   1 
ATOM   341  N  N     . GLU A 1 45  ? 117.865 174.437 128.848 1.00 55.73  ? 47  GLU B N     1 
ATOM   342  C  CA    . GLU A 1 45  ? 117.571 173.496 127.769 1.00 57.98  ? 47  GLU B CA    1 
ATOM   343  C  C     . GLU A 1 45  ? 117.465 172.061 128.272 1.00 56.45  ? 47  GLU B C     1 
ATOM   344  O  O     . GLU A 1 45  ? 116.565 171.321 127.861 1.00 55.78  ? 47  GLU B O     1 
ATOM   345  C  CB    . GLU A 1 45  ? 118.633 173.600 126.678 1.00 63.27  ? 47  GLU B CB    1 
ATOM   346  C  CG    . GLU A 1 45  ? 118.296 172.826 125.418 1.00 66.13  ? 47  GLU B CG    1 
ATOM   347  C  CD    . GLU A 1 45  ? 119.257 173.113 124.283 1.00 70.51  ? 47  GLU B CD    1 
ATOM   348  O  OE1   . GLU A 1 45  ? 120.158 173.959 124.464 1.00 67.75  ? 47  GLU B OE1   1 
ATOM   349  O  OE2   . GLU A 1 45  ? 119.114 172.491 123.209 1.00 67.42  ? 47  GLU B OE2   1 
ATOM   350  N  N     . ARG A 1 46  ? 118.373 171.641 129.148 1.00 51.41  ? 48  ARG B N     1 
ATOM   351  C  CA    . ARG A 1 46  ? 118.404 170.277 129.666 1.00 49.09  ? 48  ARG B CA    1 
ATOM   352  C  C     . ARG A 1 46  ? 118.321 170.259 131.186 1.00 51.76  ? 48  ARG B C     1 
ATOM   353  O  O     . ARG A 1 46  ? 119.033 169.510 131.854 1.00 55.13  ? 48  ARG B O     1 
ATOM   354  C  CB    . ARG A 1 46  ? 119.661 169.540 129.215 1.00 48.86  ? 48  ARG B CB    1 
ATOM   355  C  CG    . ARG A 1 46  ? 119.917 169.529 127.727 1.00 48.68  ? 48  ARG B CG    1 
ATOM   356  C  CD    . ARG A 1 46  ? 119.093 168.480 127.023 1.00 50.23  ? 48  ARG B CD    1 
ATOM   357  N  NE    . ARG A 1 46  ? 119.365 168.468 125.592 1.00 48.40  ? 48  ARG B NE    1 
ATOM   358  C  CZ    . ARG A 1 46  ? 118.605 167.865 124.692 1.00 51.19  ? 48  ARG B CZ    1 
ATOM   359  N  NH1   . ARG A 1 46  ? 117.513 167.206 125.040 1.00 50.40  ? 48  ARG B NH1   1 
ATOM   360  N  NH2   . ARG A 1 46  ? 118.950 167.922 123.409 1.00 53.38  ? 48  ARG B NH2   1 
ATOM   361  N  N     . ILE A 1 47  ? 117.448 171.091 131.757 1.00 48.94  ? 49  ILE B N     1 
ATOM   362  C  CA    . ILE A 1 47  ? 117.296 171.134 133.209 1.00 41.02  ? 49  ILE B CA    1 
ATOM   363  C  C     . ILE A 1 47  ? 116.531 169.943 133.758 1.00 44.18  ? 49  ILE B C     1 
ATOM   364  O  O     . ILE A 1 47  ? 116.538 169.724 134.974 1.00 47.58  ? 49  ILE B O     1 
ATOM   365  C  CB    . ILE A 1 47  ? 116.611 172.447 133.625 1.00 32.77  ? 49  ILE B CB    1 
ATOM   366  C  CG1   . ILE A 1 47  ? 117.041 172.854 135.028 1.00 40.51  ? 49  ILE B CG1   1 
ATOM   367  C  CG2   . ILE A 1 47  ? 115.111 172.314 133.547 1.00 43.37  ? 49  ILE B CG2   1 
ATOM   368  C  CD1   . ILE A 1 47  ? 116.531 174.194 135.445 1.00 47.40  ? 49  ILE B CD1   1 
ATOM   369  N  N     . ASN A 1 48  ? 115.881 169.156 132.902 1.00 44.11  ? 50  ASN B N     1 
ATOM   370  C  CA    . ASN A 1 48  ? 115.130 168.004 133.374 1.00 37.69  ? 50  ASN B CA    1 
ATOM   371  C  C     . ASN A 1 48  ? 116.023 166.867 133.842 1.00 47.67  ? 50  ASN B C     1 
ATOM   372  O  O     . ASN A 1 48  ? 115.519 165.933 134.472 1.00 57.27  ? 50  ASN B O     1 
ATOM   373  C  CB    . ASN A 1 48  ? 114.190 167.501 132.280 1.00 50.14  ? 50  ASN B CB    1 
ATOM   374  C  CG    . ASN A 1 48  ? 114.920 167.129 131.013 1.00 58.91  ? 50  ASN B CG    1 
ATOM   375  O  OD1   . ASN A 1 48  ? 115.150 167.970 130.145 1.00 58.85  ? 50  ASN B OD1   1 
ATOM   376  N  ND2   . ASN A 1 48  ? 115.290 165.861 130.896 1.00 57.96  ? 50  ASN B ND2   1 
ATOM   377  N  N     . VAL A 1 49  ? 117.323 166.914 133.547 1.00 45.35  ? 51  VAL B N     1 
ATOM   378  C  CA    . VAL A 1 49  ? 118.225 165.854 133.986 1.00 38.07  ? 51  VAL B CA    1 
ATOM   379  C  C     . VAL A 1 49  ? 118.306 165.822 135.503 1.00 43.65  ? 51  VAL B C     1 
ATOM   380  O  O     . VAL A 1 49  ? 118.269 164.752 136.120 1.00 50.49  ? 51  VAL B O     1 
ATOM   381  C  CB    . VAL A 1 49  ? 119.611 166.036 133.342 1.00 36.24  ? 51  VAL B CB    1 
ATOM   382  C  CG1   . VAL A 1 49  ? 120.615 165.097 133.962 1.00 44.89  ? 51  VAL B CG1   1 
ATOM   383  C  CG2   . VAL A 1 49  ? 119.529 165.802 131.854 1.00 42.20  ? 51  VAL B CG2   1 
ATOM   384  N  N     . TYR A 1 50  ? 118.398 166.993 136.131 1.00 47.00  ? 52  TYR B N     1 
ATOM   385  C  CA    . TYR A 1 50  ? 118.613 167.092 137.564 1.00 38.00  ? 52  TYR B CA    1 
ATOM   386  C  C     . TYR A 1 50  ? 117.470 167.727 138.340 1.00 42.97  ? 52  TYR B C     1 
ATOM   387  O  O     . TYR A 1 50  ? 117.469 167.632 139.569 1.00 54.21  ? 52  TYR B O     1 
ATOM   388  C  CB    . TYR A 1 50  ? 119.885 167.900 137.854 1.00 34.81  ? 52  TYR B CB    1 
ATOM   389  C  CG    . TYR A 1 50  ? 121.142 167.080 137.912 1.00 35.71  ? 52  TYR B CG    1 
ATOM   390  C  CD1   . TYR A 1 50  ? 121.237 165.985 138.744 1.00 44.78  ? 52  TYR B CD1   1 
ATOM   391  C  CD2   . TYR A 1 50  ? 122.239 167.410 137.143 1.00 41.50  ? 52  TYR B CD2   1 
ATOM   392  C  CE1   . TYR A 1 50  ? 122.385 165.239 138.801 1.00 45.57  ? 52  TYR B CE1   1 
ATOM   393  C  CE2   . TYR A 1 50  ? 123.388 166.670 137.193 1.00 40.79  ? 52  TYR B CE2   1 
ATOM   394  C  CZ    . TYR A 1 50  ? 123.457 165.586 138.023 1.00 43.49  ? 52  TYR B CZ    1 
ATOM   395  O  OH    . TYR A 1 50  ? 124.606 164.840 138.080 1.00 43.65  ? 52  TYR B OH    1 
ATOM   396  N  N     . TYR A 1 51  ? 116.509 168.365 137.680 1.00 41.48  ? 53  TYR B N     1 
ATOM   397  C  CA    . TYR A 1 51  ? 115.493 169.140 138.375 1.00 30.30  ? 53  TYR B CA    1 
ATOM   398  C  C     . TYR A 1 51  ? 114.100 168.760 137.901 1.00 42.24  ? 53  TYR B C     1 
ATOM   399  O  O     . TYR A 1 51  ? 113.906 168.316 136.769 1.00 44.70  ? 53  TYR B O     1 
ATOM   400  C  CB    . TYR A 1 51  ? 115.691 170.632 138.164 1.00 33.14  ? 53  TYR B CB    1 
ATOM   401  C  CG    . TYR A 1 51  ? 116.922 171.197 138.810 1.00 39.95  ? 53  TYR B CG    1 
ATOM   402  C  CD1   . TYR A 1 51  ? 118.152 171.114 138.192 1.00 43.19  ? 53  TYR B CD1   1 
ATOM   403  C  CD2   . TYR A 1 51  ? 116.848 171.838 140.029 1.00 39.82  ? 53  TYR B CD2   1 
ATOM   404  C  CE1   . TYR A 1 51  ? 119.270 171.639 138.777 1.00 42.90  ? 53  TYR B CE1   1 
ATOM   405  C  CE2   . TYR A 1 51  ? 117.960 172.363 140.619 1.00 35.00  ? 53  TYR B CE2   1 
ATOM   406  C  CZ    . TYR A 1 51  ? 119.166 172.262 139.991 1.00 41.86  ? 53  TYR B CZ    1 
ATOM   407  O  OH    . TYR A 1 51  ? 120.280 172.792 140.590 1.00 50.39  ? 53  TYR B OH    1 
ATOM   408  N  N     . ASN A 1 52  ? 113.130 168.948 138.790 1.00 51.71  ? 54  ASN B N     1 
ATOM   409  C  CA    . ASN A 1 52  ? 111.722 168.715 138.510 1.00 42.15  ? 54  ASN B CA    1 
ATOM   410  C  C     . ASN A 1 52  ? 110.983 170.045 138.483 1.00 50.39  ? 54  ASN B C     1 
ATOM   411  O  O     . ASN A 1 52  ? 111.185 170.896 139.353 1.00 57.42  ? 54  ASN B O     1 
ATOM   412  C  CB    . ASN A 1 52  ? 111.097 167.801 139.561 1.00 37.82  ? 54  ASN B CB    1 
ATOM   413  C  CG    . ASN A 1 52  ? 110.788 166.434 139.028 1.00 39.17  ? 54  ASN B CG    1 
ATOM   414  O  OD1   . ASN A 1 52  ? 110.482 166.271 137.853 1.00 44.19  ? 54  ASN B OD1   1 
ATOM   415  N  ND2   . ASN A 1 52  ? 110.853 165.437 139.894 1.00 46.06  ? 54  ASN B ND2   1 
ATOM   416  N  N     . GLU A 1 53  ? 110.133 170.224 137.480 1.00 47.85  ? 55  GLU B N     1 
ATOM   417  C  CA    . GLU A 1 53  ? 109.382 171.460 137.352 1.00 44.56  ? 55  GLU B CA    1 
ATOM   418  C  C     . GLU A 1 53  ? 108.288 171.541 138.410 1.00 54.26  ? 55  GLU B C     1 
ATOM   419  O  O     . GLU A 1 53  ? 107.859 170.535 138.981 1.00 61.42  ? 55  GLU B O     1 
ATOM   420  C  CB    . GLU A 1 53  ? 108.766 171.569 135.962 1.00 49.62  ? 55  GLU B CB    1 
ATOM   421  C  CG    . GLU A 1 53  ? 109.533 172.463 135.014 1.00 58.95  ? 55  GLU B CG    1 
ATOM   422  C  CD    . GLU A 1 53  ? 109.032 173.890 135.039 1.00 63.89  ? 55  GLU B CD    1 
ATOM   423  O  OE1   . GLU A 1 53  ? 108.049 174.161 135.758 1.00 62.94  ? 55  GLU B OE1   1 
ATOM   424  O  OE2   . GLU A 1 53  ? 109.620 174.741 134.338 1.00 63.97  ? 55  GLU B OE2   1 
ATOM   425  N  N     . ALA A 1 54  ? 107.833 172.763 138.669 1.00 47.03  ? 56  ALA B N     1 
ATOM   426  C  CA    . ALA A 1 54  ? 106.763 173.006 139.623 1.00 43.88  ? 56  ALA B CA    1 
ATOM   427  C  C     . ALA A 1 54  ? 105.914 174.166 139.124 1.00 44.94  ? 56  ALA B C     1 
ATOM   428  O  O     . ALA A 1 54  ? 106.212 174.789 138.102 1.00 50.26  ? 56  ALA B O     1 
ATOM   429  C  CB    . ALA A 1 54  ? 107.318 173.280 141.023 1.00 48.99  ? 56  ALA B CB    1 
ATOM   430  N  N     . ALA A 1 55  ? 104.841 174.451 139.852 1.00 47.99  ? 57  ALA B N     1 
ATOM   431  C  CA    . ALA A 1 55  ? 103.942 175.527 139.470 1.00 49.18  ? 57  ALA B CA    1 
ATOM   432  C  C     . ALA A 1 55  ? 104.622 176.882 139.611 1.00 52.78  ? 57  ALA B C     1 
ATOM   433  O  O     . ALA A 1 55  ? 105.343 177.137 140.578 1.00 62.17  ? 57  ALA B O     1 
ATOM   434  C  CB    . ALA A 1 55  ? 102.676 175.487 140.322 1.00 52.18  ? 57  ALA B CB    1 
ATOM   435  N  N     . GLY A 1 56  ? 104.380 177.754 138.640 1.00 57.85  ? 58  GLY B N     1 
ATOM   436  C  CA    . GLY A 1 56  ? 104.933 179.098 138.662 1.00 59.02  ? 58  GLY B CA    1 
ATOM   437  C  C     . GLY A 1 56  ? 106.433 179.189 138.482 1.00 62.65  ? 58  GLY B C     1 
ATOM   438  O  O     . GLY A 1 56  ? 107.080 180.009 139.143 1.00 58.84  ? 58  GLY B O     1 
ATOM   439  N  N     . ASN A 1 57  ? 107.000 178.368 137.595 1.00 65.46  ? 59  ASN B N     1 
ATOM   440  C  CA    . ASN A 1 57  ? 108.425 178.397 137.258 1.00 60.08  ? 59  ASN B CA    1 
ATOM   441  C  C     . ASN A 1 57  ? 109.298 178.218 138.501 1.00 62.46  ? 59  ASN B C     1 
ATOM   442  O  O     . ASN A 1 57  ? 110.093 179.081 138.872 1.00 67.06  ? 59  ASN B O     1 
ATOM   443  C  CB    . ASN A 1 57  ? 108.788 179.685 136.512 1.00 63.98  ? 59  ASN B CB    1 
ATOM   444  C  CG    . ASN A 1 57  ? 107.859 179.965 135.350 1.00 68.80  ? 59  ASN B CG    1 
ATOM   445  O  OD1   . ASN A 1 57  ? 107.280 181.047 135.250 1.00 65.79  ? 59  ASN B OD1   1 
ATOM   446  N  ND2   . ASN A 1 57  ? 107.712 178.990 134.461 1.00 68.68  ? 59  ASN B ND2   1 
ATOM   447  N  N     . LYS A 1 58  ? 109.133 177.068 139.141 1.00 48.88  ? 60  LYS B N     1 
ATOM   448  C  CA    . LYS A 1 58  ? 109.922 176.682 140.298 1.00 41.66  ? 60  LYS B CA    1 
ATOM   449  C  C     . LYS A 1 58  ? 110.533 175.319 140.027 1.00 51.91  ? 60  LYS B C     1 
ATOM   450  O  O     . LYS A 1 58  ? 109.908 174.472 139.383 1.00 63.16  ? 60  LYS B O     1 
ATOM   451  C  CB    . LYS A 1 58  ? 109.065 176.640 141.561 1.00 42.00  ? 60  LYS B CB    1 
ATOM   452  C  CG    . LYS A 1 58  ? 109.850 176.529 142.843 1.00 53.91  ? 60  LYS B CG    1 
ATOM   453  C  CD    . LYS A 1 58  ? 108.928 176.360 144.033 1.00 54.12  ? 60  LYS B CD    1 
ATOM   454  C  CE    . LYS A 1 58  ? 109.707 176.347 145.335 1.00 54.48  ? 60  LYS B CE    1 
ATOM   455  N  NZ    . LYS A 1 58  ? 110.766 175.303 145.335 1.00 54.53  ? 60  LYS B NZ    1 
ATOM   456  N  N     . TYR A 1 59  ? 111.752 175.107 140.508 1.00 45.15  ? 61  TYR B N     1 
ATOM   457  C  CA    . TYR A 1 59  ? 112.486 173.879 140.243 1.00 42.31  ? 61  TYR B CA    1 
ATOM   458  C  C     . TYR A 1 59  ? 112.878 173.217 141.554 1.00 52.47  ? 61  TYR B C     1 
ATOM   459  O  O     . TYR A 1 59  ? 113.418 173.875 142.449 1.00 61.02  ? 61  TYR B O     1 
ATOM   460  C  CB    . TYR A 1 59  ? 113.715 174.164 139.382 1.00 42.92  ? 61  TYR B CB    1 
ATOM   461  C  CG    . TYR A 1 59  ? 113.347 174.651 138.008 1.00 42.11  ? 61  TYR B CG    1 
ATOM   462  C  CD1   . TYR A 1 59  ? 112.979 173.762 137.015 1.00 46.19  ? 61  TYR B CD1   1 
ATOM   463  C  CD2   . TYR A 1 59  ? 113.335 176.000 137.710 1.00 44.81  ? 61  TYR B CD2   1 
ATOM   464  C  CE1   . TYR A 1 59  ? 112.629 174.201 135.764 1.00 45.68  ? 61  TYR B CE1   1 
ATOM   465  C  CE2   . TYR A 1 59  ? 112.982 176.448 136.459 1.00 47.68  ? 61  TYR B CE2   1 
ATOM   466  C  CZ    . TYR A 1 59  ? 112.632 175.544 135.490 1.00 44.99  ? 61  TYR B CZ    1 
ATOM   467  O  OH    . TYR A 1 59  ? 112.281 175.989 134.239 1.00 49.22  ? 61  TYR B OH    1 
ATOM   468  N  N     . VAL A 1 60  ? 112.547 171.915 141.663 1.00 36.88  ? 62  VAL B N     1 
ATOM   469  C  CA    . VAL A 1 60  ? 112.872 171.151 142.885 1.00 34.10  ? 62  VAL B CA    1 
ATOM   470  C  C     . VAL A 1 60  ? 113.833 170.043 142.465 1.00 34.46  ? 62  VAL B C     1 
ATOM   471  O  O     . VAL A 1 60  ? 113.575 169.430 141.444 1.00 47.22  ? 62  VAL B O     1 
ATOM   472  C  CB    . VAL A 1 60  ? 111.550 170.615 143.442 1.00 41.62  ? 62  VAL B CB    1 
ATOM   473  C  CG1   . VAL A 1 60  ? 111.764 169.499 144.453 1.00 45.93  ? 62  VAL B CG1   1 
ATOM   474  C  CG2   . VAL A 1 60  ? 110.693 171.723 144.037 1.00 45.89  ? 62  VAL B CG2   1 
ATOM   475  N  N     . PRO A 1 61  ? 114.977 169.831 143.167 1.00 27.64  ? 63  PRO B N     1 
ATOM   476  C  CA    . PRO A 1 61  ? 115.913 168.763 142.816 1.00 33.31  ? 63  PRO B CA    1 
ATOM   477  C  C     . PRO A 1 61  ? 115.307 167.378 142.956 1.00 38.40  ? 63  PRO B C     1 
ATOM   478  O  O     . PRO A 1 61  ? 114.382 167.148 143.736 1.00 46.51  ? 63  PRO B O     1 
ATOM   479  C  CB    . PRO A 1 61  ? 117.058 168.962 143.814 1.00 42.06  ? 63  PRO B CB    1 
ATOM   480  C  CG    . PRO A 1 61  ? 116.964 170.369 144.208 1.00 40.85  ? 63  PRO B CG    1 
ATOM   481  C  CD    . PRO A 1 61  ? 115.513 170.693 144.227 1.00 40.47  ? 63  PRO B CD    1 
ATOM   482  N  N     . ARG A 1 62  ? 115.848 166.446 142.177 1.00 37.95  ? 64  ARG B N     1 
ATOM   483  C  CA    . ARG A 1 62  ? 115.476 165.038 142.276 1.00 38.32  ? 64  ARG B CA    1 
ATOM   484  C  C     . ARG A 1 62  ? 116.421 164.310 143.232 1.00 41.46  ? 64  ARG B C     1 
ATOM   485  O  O     . ARG A 1 62  ? 117.132 163.377 142.871 1.00 51.74  ? 64  ARG B O     1 
ATOM   486  C  CB    . ARG A 1 62  ? 115.474 164.394 140.897 1.00 38.90  ? 64  ARG B CB    1 
ATOM   487  C  CG    . ARG A 1 62  ? 114.139 163.810 140.505 1.00 41.62  ? 64  ARG B CG    1 
ATOM   488  C  CD    . ARG A 1 62  ? 114.260 162.913 139.296 1.00 42.06  ? 64  ARG B CD    1 
ATOM   489  N  NE    . ARG A 1 62  ? 115.053 163.533 138.245 1.00 44.65  ? 64  ARG B NE    1 
ATOM   490  C  CZ    . ARG A 1 62  ? 114.564 164.323 137.303 1.00 40.52  ? 64  ARG B CZ    1 
ATOM   491  N  NH1   . ARG A 1 62  ? 113.276 164.605 137.238 1.00 40.71  ? 64  ARG B NH1   1 
ATOM   492  N  NH2   . ARG A 1 62  ? 115.389 164.846 136.405 1.00 47.41  ? 64  ARG B NH2   1 
ATOM   493  N  N     . ALA A 1 63  ? 116.409 164.761 144.480 1.00 38.87  ? 65  ALA B N     1 
ATOM   494  C  CA    . ALA A 1 63  ? 117.289 164.242 145.511 1.00 41.05  ? 65  ALA B CA    1 
ATOM   495  C  C     . ALA A 1 63  ? 116.474 163.611 146.627 1.00 40.20  ? 65  ALA B C     1 
ATOM   496  O  O     . ALA A 1 63  ? 115.364 164.052 146.933 1.00 52.97  ? 65  ALA B O     1 
ATOM   497  C  CB    . ALA A 1 63  ? 118.182 165.343 146.084 1.00 46.16  ? 65  ALA B CB    1 
ATOM   498  N  N     . ILE A 1 64  ? 117.035 162.571 147.234 1.00 32.90  ? 66  ILE B N     1 
ATOM   499  C  CA    . ILE A 1 64  ? 116.416 161.885 148.357 1.00 34.08  ? 66  ILE B CA    1 
ATOM   500  C  C     . ILE A 1 64  ? 117.436 161.811 149.480 1.00 42.38  ? 66  ILE B C     1 
ATOM   501  O  O     . ILE A 1 64  ? 118.485 161.177 149.331 1.00 53.07  ? 66  ILE B O     1 
ATOM   502  C  CB    . ILE A 1 64  ? 115.916 160.488 147.965 1.00 40.22  ? 66  ILE B CB    1 
ATOM   503  C  CG1   . ILE A 1 64  ? 114.800 160.634 146.936 1.00 46.55  ? 66  ILE B CG1   1 
ATOM   504  C  CG2   . ILE A 1 64  ? 115.443 159.731 149.181 1.00 41.25  ? 66  ILE B CG2   1 
ATOM   505  C  CD1   . ILE A 1 64  ? 114.218 159.353 146.472 1.00 50.02  ? 66  ILE B CD1   1 
ATOM   506  N  N     . LEU A 1 65  ? 117.128 162.456 150.599 1.00 37.27  ? 67  LEU B N     1 
ATOM   507  C  CA    . LEU A 1 65  ? 118.047 162.591 151.720 1.00 34.94  ? 67  LEU B CA    1 
ATOM   508  C  C     . LEU A 1 65  ? 117.627 161.632 152.824 1.00 37.95  ? 67  LEU B C     1 
ATOM   509  O  O     . LEU A 1 65  ? 116.513 161.738 153.347 1.00 46.79  ? 67  LEU B O     1 
ATOM   510  C  CB    . LEU A 1 65  ? 118.055 164.032 152.227 1.00 37.40  ? 67  LEU B CB    1 
ATOM   511  C  CG    . LEU A 1 65  ? 118.047 165.150 151.181 1.00 40.77  ? 67  LEU B CG    1 
ATOM   512  C  CD1   . LEU A 1 65  ? 116.646 165.661 150.910 1.00 44.40  ? 67  LEU B CD1   1 
ATOM   513  C  CD2   . LEU A 1 65  ? 118.943 166.284 151.620 1.00 40.18  ? 67  LEU B CD2   1 
ATOM   514  N  N     . VAL A 1 66  ? 118.513 160.707 153.186 1.00 38.92  ? 68  VAL B N     1 
ATOM   515  C  CA    . VAL A 1 66  ? 118.191 159.631 154.117 1.00 33.77  ? 68  VAL B CA    1 
ATOM   516  C  C     . VAL A 1 66  ? 119.266 159.561 155.195 1.00 39.91  ? 68  VAL B C     1 
ATOM   517  O  O     . VAL A 1 66  ? 120.460 159.651 154.894 1.00 46.84  ? 68  VAL B O     1 
ATOM   518  C  CB    . VAL A 1 66  ? 118.047 158.279 153.390 1.00 37.22  ? 68  VAL B CB    1 
ATOM   519  C  CG1   . VAL A 1 66  ? 119.215 158.040 152.464 1.00 43.13  ? 68  VAL B CG1   1 
ATOM   520  C  CG2   . VAL A 1 66  ? 117.912 157.149 154.382 1.00 43.62  ? 68  VAL B CG2   1 
ATOM   521  N  N     . ASP A 1 67  ? 118.839 159.417 156.448 1.00 50.72  ? 69  ASP B N     1 
ATOM   522  C  CA    . ASP A 1 67  ? 119.742 159.324 157.588 1.00 47.42  ? 69  ASP B CA    1 
ATOM   523  C  C     . ASP A 1 67  ? 119.012 158.631 158.730 1.00 50.84  ? 69  ASP B C     1 
ATOM   524  O  O     . ASP A 1 67  ? 117.797 158.430 158.684 1.00 61.57  ? 69  ASP B O     1 
ATOM   525  C  CB    . ASP A 1 67  ? 120.240 160.704 158.016 1.00 48.22  ? 69  ASP B CB    1 
ATOM   526  C  CG    . ASP A 1 67  ? 121.412 160.633 158.966 1.00 56.91  ? 69  ASP B CG    1 
ATOM   527  O  OD1   . ASP A 1 67  ? 121.886 159.514 159.241 1.00 58.92  ? 69  ASP B OD1   1 
ATOM   528  O  OD2   . ASP A 1 67  ? 121.860 161.697 159.438 1.00 57.49  ? 69  ASP B OD2   1 
ATOM   529  N  N     . LEU A 1 68  ? 119.771 158.251 159.754 1.00 42.81  ? 70  LEU B N     1 
ATOM   530  C  CA    . LEU A 1 68  ? 119.215 157.644 160.954 1.00 39.95  ? 70  LEU B CA    1 
ATOM   531  C  C     . LEU A 1 68  ? 119.139 158.612 162.128 1.00 48.56  ? 70  LEU B C     1 
ATOM   532  O  O     . LEU A 1 68  ? 118.609 158.248 163.180 1.00 53.06  ? 70  LEU B O     1 
ATOM   533  C  CB    . LEU A 1 68  ? 120.035 156.413 161.349 1.00 42.92  ? 70  LEU B CB    1 
ATOM   534  C  CG    . LEU A 1 68  ? 119.924 155.221 160.397 1.00 45.01  ? 70  LEU B CG    1 
ATOM   535  C  CD1   . LEU A 1 68  ? 120.792 154.069 160.852 1.00 48.33  ? 70  LEU B CD1   1 
ATOM   536  C  CD2   . LEU A 1 68  ? 118.489 154.780 160.283 1.00 47.56  ? 70  LEU B CD2   1 
ATOM   537  N  N     . GLU A 1 69  ? 119.657 159.826 161.976 1.00 56.01  ? 71  GLU B N     1 
ATOM   538  C  CA    . GLU A 1 69  ? 119.599 160.881 162.972 1.00 51.01  ? 71  GLU B CA    1 
ATOM   539  C  C     . GLU A 1 69  ? 119.115 162.164 162.318 1.00 60.35  ? 71  GLU B C     1 
ATOM   540  O  O     . GLU A 1 69  ? 119.315 162.364 161.116 1.00 67.60  ? 71  GLU B O     1 
ATOM   541  C  CB    . GLU A 1 69  ? 120.973 161.130 163.607 1.00 52.51  ? 71  GLU B CB    1 
ATOM   542  C  CG    . GLU A 1 69  ? 121.713 159.880 164.026 1.00 62.16  ? 71  GLU B CG    1 
ATOM   543  C  CD    . GLU A 1 69  ? 123.114 160.175 164.521 1.00 66.61  ? 71  GLU B CD    1 
ATOM   544  O  OE1   . GLU A 1 69  ? 123.471 161.367 164.618 1.00 65.48  ? 71  GLU B OE1   1 
ATOM   545  O  OE2   . GLU A 1 69  ? 123.858 159.215 164.813 1.00 62.82  ? 71  GLU B OE2   1 
ATOM   546  N  N     . PRO A 1 70  ? 118.478 163.052 163.078 1.00 48.90  ? 72  PRO B N     1 
ATOM   547  C  CA    . PRO A 1 70  ? 117.976 164.307 162.508 1.00 47.49  ? 72  PRO B CA    1 
ATOM   548  C  C     . PRO A 1 70  ? 118.949 165.477 162.521 1.00 47.11  ? 72  PRO B C     1 
ATOM   549  O  O     . PRO A 1 70  ? 118.618 166.525 161.955 1.00 55.54  ? 72  PRO B O     1 
ATOM   550  C  CB    . PRO A 1 70  ? 116.769 164.602 163.404 1.00 49.85  ? 72  PRO B CB    1 
ATOM   551  C  CG    . PRO A 1 70  ? 117.144 164.042 164.714 1.00 48.56  ? 72  PRO B CG    1 
ATOM   552  C  CD    . PRO A 1 70  ? 117.990 162.835 164.449 1.00 47.94  ? 72  PRO B CD    1 
ATOM   553  N  N     . GLY A 1 71  ? 120.122 165.339 163.137 1.00 49.95  ? 73  GLY B N     1 
ATOM   554  C  CA    . GLY A 1 71  ? 121.031 166.472 163.234 1.00 50.46  ? 73  GLY B CA    1 
ATOM   555  C  C     . GLY A 1 71  ? 121.541 166.940 161.884 1.00 54.72  ? 73  GLY B C     1 
ATOM   556  O  O     . GLY A 1 71  ? 121.531 168.137 161.582 1.00 60.16  ? 73  GLY B O     1 
ATOM   557  N  N     . THR A 1 72  ? 121.986 166.039 161.032 1.00 51.11  ? 74  THR B N     1 
ATOM   558  C  CA    . THR A 1 72  ? 122.425 166.494 159.704 1.00 53.84  ? 74  THR B CA    1 
ATOM   559  C  C     . THR A 1 72  ? 121.229 167.012 158.941 1.00 55.81  ? 74  THR B C     1 
ATOM   560  O  O     . THR A 1 72  ? 121.386 168.013 158.220 1.00 61.73  ? 74  THR B O     1 
ATOM   561  C  CB    . THR A 1 72  ? 123.178 165.412 158.942 1.00 59.11  ? 74  THR B CB    1 
ATOM   562  O  OG1   . THR A 1 72  ? 123.893 164.687 159.936 1.00 63.50  ? 74  THR B OG1   1 
ATOM   563  C  CG2   . THR A 1 72  ? 124.148 165.983 157.925 1.00 57.32  ? 74  THR B CG2   1 
ATOM   564  N  N     . MET A 1 73  ? 120.070 166.362 159.073 1.00 54.29  ? 75  MET B N     1 
ATOM   565  C  CA    . MET A 1 73  ? 118.904 166.818 158.329 1.00 56.24  ? 75  MET B CA    1 
ATOM   566  C  C     . MET A 1 73  ? 118.590 168.274 158.638 1.00 59.07  ? 75  MET B C     1 
ATOM   567  O  O     . MET A 1 73  ? 118.419 169.091 157.726 1.00 62.48  ? 75  MET B O     1 
ATOM   568  C  CB    . MET A 1 73  ? 117.701 165.937 158.655 1.00 60.17  ? 75  MET B CB    1 
ATOM   569  C  CG    . MET A 1 73  ? 117.823 164.520 158.159 1.00 59.76  ? 75  MET B CG    1 
ATOM   570  S  SD    . MET A 1 73  ? 118.303 164.456 156.431 1.00 71.00  ? 75  MET B SD    1 
ATOM   571  C  CE    . MET A 1 73  ? 117.963 162.741 156.078 1.00 58.56  ? 75  MET B CE    1 
ATOM   572  N  N     . ASP A 1 74  ? 118.508 168.623 159.920 1.00 54.34  ? 76  ASP B N     1 
ATOM   573  C  CA    . ASP A 1 74  ? 118.159 169.993 160.262 1.00 52.16  ? 76  ASP B CA    1 
ATOM   574  C  C     . ASP A 1 74  ? 119.351 170.934 160.206 1.00 53.23  ? 76  ASP B C     1 
ATOM   575  O  O     . ASP A 1 74  ? 119.167 172.145 160.354 1.00 60.17  ? 76  ASP B O     1 
ATOM   576  C  CB    . ASP A 1 74  ? 117.475 170.058 161.634 1.00 57.12  ? 76  ASP B CB    1 
ATOM   577  C  CG    . ASP A 1 74  ? 118.271 169.393 162.734 1.00 62.33  ? 76  ASP B CG    1 
ATOM   578  O  OD1   . ASP A 1 74  ? 119.510 169.351 162.647 1.00 63.68  ? 76  ASP B OD1   1 
ATOM   579  O  OD2   . ASP A 1 74  ? 117.647 168.903 163.698 1.00 63.23  ? 76  ASP B OD2   1 
ATOM   580  N  N     . SER A 1 75  ? 120.563 170.418 160.001 1.00 50.85  ? 77  SER B N     1 
ATOM   581  C  CA    . SER A 1 75  ? 121.656 171.289 159.589 1.00 51.07  ? 77  SER B CA    1 
ATOM   582  C  C     . SER A 1 75  ? 121.561 171.635 158.107 1.00 54.53  ? 77  SER B C     1 
ATOM   583  O  O     . SER A 1 75  ? 121.835 172.774 157.715 1.00 58.07  ? 77  SER B O     1 
ATOM   584  C  CB    . SER A 1 75  ? 122.998 170.630 159.898 1.00 54.20  ? 77  SER B CB    1 
ATOM   585  O  OG    . SER A 1 75  ? 123.325 169.657 158.922 1.00 56.31  ? 77  SER B OG    1 
ATOM   586  N  N     . VAL A 1 76  ? 121.180 170.666 157.272 1.00 55.23  ? 78  VAL B N     1 
ATOM   587  C  CA    . VAL A 1 76  ? 121.040 170.922 155.840 1.00 52.25  ? 78  VAL B CA    1 
ATOM   588  C  C     . VAL A 1 76  ? 119.838 171.816 155.568 1.00 51.94  ? 78  VAL B C     1 
ATOM   589  O  O     . VAL A 1 76  ? 119.890 172.710 154.715 1.00 54.60  ? 78  VAL B O     1 
ATOM   590  C  CB    . VAL A 1 76  ? 120.940 169.591 155.072 1.00 50.68  ? 78  VAL B CB    1 
ATOM   591  C  CG1   . VAL A 1 76  ? 120.313 169.800 153.707 1.00 51.26  ? 78  VAL B CG1   1 
ATOM   592  C  CG2   . VAL A 1 76  ? 122.305 168.948 154.939 1.00 52.38  ? 78  VAL B CG2   1 
ATOM   593  N  N     . ARG A 1 77  ? 118.740 171.595 156.290 1.00 58.92  ? 79  ARG B N     1 
ATOM   594  C  CA    . ARG A 1 77  ? 117.496 172.300 156.002 1.00 55.47  ? 79  ARG B CA    1 
ATOM   595  C  C     . ARG A 1 77  ? 117.611 173.796 156.252 1.00 55.22  ? 79  ARG B C     1 
ATOM   596  O  O     . ARG A 1 77  ? 116.938 174.588 155.584 1.00 59.09  ? 79  ARG B O     1 
ATOM   597  C  CB    . ARG A 1 77  ? 116.366 171.713 156.846 1.00 56.12  ? 79  ARG B CB    1 
ATOM   598  C  CG    . ARG A 1 77  ? 114.994 171.843 156.228 1.00 57.71  ? 79  ARG B CG    1 
ATOM   599  C  CD    . ARG A 1 77  ? 113.914 171.647 157.267 1.00 57.65  ? 79  ARG B CD    1 
ATOM   600  N  NE    . ARG A 1 77  ? 114.152 170.464 158.083 1.00 66.49  ? 79  ARG B NE    1 
ATOM   601  C  CZ    . ARG A 1 77  ? 113.548 169.299 157.904 1.00 65.96  ? 79  ARG B CZ    1 
ATOM   602  N  NH1   . ARG A 1 77  ? 112.652 169.125 156.948 1.00 62.29  ? 79  ARG B NH1   1 
ATOM   603  N  NH2   . ARG A 1 77  ? 113.845 168.284 158.710 1.00 62.22  ? 79  ARG B NH2   1 
ATOM   604  N  N     . SER A 1 78  ? 118.444 174.205 157.202 1.00 54.96  ? 80  SER B N     1 
ATOM   605  C  CA    . SER A 1 78  ? 118.560 175.603 157.590 1.00 53.80  ? 80  SER B CA    1 
ATOM   606  C  C     . SER A 1 78  ? 119.733 176.313 156.927 1.00 57.84  ? 80  SER B C     1 
ATOM   607  O  O     . SER A 1 78  ? 120.053 177.441 157.311 1.00 63.53  ? 80  SER B O     1 
ATOM   608  C  CB    . SER A 1 78  ? 118.682 175.716 159.109 1.00 56.46  ? 80  SER B CB    1 
ATOM   609  O  OG    . SER A 1 78  ? 119.841 175.050 159.576 1.00 63.37  ? 80  SER B OG    1 
ATOM   610  N  N     . GLY A 1 79  ? 120.379 175.685 155.951 1.00 55.00  ? 81  GLY B N     1 
ATOM   611  C  CA    . GLY A 1 79  ? 121.506 176.282 155.278 1.00 51.25  ? 81  GLY B CA    1 
ATOM   612  C  C     . GLY A 1 79  ? 121.086 177.252 154.195 1.00 56.87  ? 81  GLY B C     1 
ATOM   613  O  O     . GLY A 1 79  ? 119.914 177.624 154.082 1.00 60.69  ? 81  GLY B O     1 
ATOM   614  N  N     . PRO A 1 80  ? 122.048 177.695 153.383 1.00 53.41  ? 82  PRO B N     1 
ATOM   615  C  CA    . PRO A 1 80  ? 121.712 178.651 152.314 1.00 54.14  ? 82  PRO B CA    1 
ATOM   616  C  C     . PRO A 1 80  ? 120.743 178.095 151.288 1.00 56.57  ? 82  PRO B C     1 
ATOM   617  O  O     . PRO A 1 80  ? 119.896 178.834 150.774 1.00 56.89  ? 82  PRO B O     1 
ATOM   618  C  CB    . PRO A 1 80  ? 123.080 178.962 151.693 1.00 54.84  ? 82  PRO B CB    1 
ATOM   619  C  CG    . PRO A 1 80  ? 123.897 177.748 151.976 1.00 53.67  ? 82  PRO B CG    1 
ATOM   620  C  CD    . PRO A 1 80  ? 123.454 177.264 153.321 1.00 53.22  ? 82  PRO B CD    1 
ATOM   621  N  N     . PHE A 1 81  ? 120.844 176.805 150.978 1.00 55.77  ? 83  PHE B N     1 
ATOM   622  C  CA    . PHE A 1 81  ? 120.049 176.176 149.933 1.00 44.86  ? 83  PHE B CA    1 
ATOM   623  C  C     . PHE A 1 81  ? 119.146 175.088 150.497 1.00 48.10  ? 83  PHE B C     1 
ATOM   624  O  O     . PHE A 1 81  ? 118.758 174.163 149.784 1.00 53.81  ? 83  PHE B O     1 
ATOM   625  C  CB    . PHE A 1 81  ? 120.949 175.606 148.840 1.00 46.53  ? 83  PHE B CB    1 
ATOM   626  C  CG    . PHE A 1 81  ? 121.407 176.627 147.847 1.00 52.04  ? 83  PHE B CG    1 
ATOM   627  C  CD1   . PHE A 1 81  ? 122.423 177.508 148.161 1.00 54.12  ? 83  PHE B CD1   1 
ATOM   628  C  CD2   . PHE A 1 81  ? 120.818 176.715 146.602 1.00 54.09  ? 83  PHE B CD2   1 
ATOM   629  C  CE1   . PHE A 1 81  ? 122.843 178.452 147.251 1.00 56.17  ? 83  PHE B CE1   1 
ATOM   630  C  CE2   . PHE A 1 81  ? 121.236 177.656 145.693 1.00 51.99  ? 83  PHE B CE2   1 
ATOM   631  C  CZ    . PHE A 1 81  ? 122.247 178.525 146.016 1.00 53.77  ? 83  PHE B CZ    1 
ATOM   632  N  N     . GLY A 1 82  ? 118.807 175.179 151.780 1.00 50.40  ? 84  GLY B N     1 
ATOM   633  C  CA    . GLY A 1 82  ? 117.924 174.188 152.359 1.00 54.15  ? 84  GLY B CA    1 
ATOM   634  C  C     . GLY A 1 82  ? 116.479 174.333 151.952 1.00 57.24  ? 84  GLY B C     1 
ATOM   635  O  O     . GLY A 1 82  ? 115.707 173.381 152.094 1.00 58.42  ? 84  GLY B O     1 
ATOM   636  N  N     . GLN A 1 83  ? 116.097 175.499 151.445 1.00 48.08  ? 85  GLN B N     1 
ATOM   637  C  CA    . GLN A 1 83  ? 114.723 175.755 151.045 1.00 49.14  ? 85  GLN B CA    1 
ATOM   638  C  C     . GLN A 1 83  ? 114.404 175.236 149.651 1.00 53.38  ? 85  GLN B C     1 
ATOM   639  O  O     . GLN A 1 83  ? 113.260 175.369 149.208 1.00 57.80  ? 85  GLN B O     1 
ATOM   640  C  CB    . GLN A 1 83  ? 114.433 177.254 151.113 1.00 49.17  ? 85  GLN B CB    1 
ATOM   641  C  CG    . GLN A 1 83  ? 113.702 177.681 152.366 1.00 51.06  ? 85  GLN B CG    1 
ATOM   642  C  CD    . GLN A 1 83  ? 114.386 177.198 153.627 1.00 58.56  ? 85  GLN B CD    1 
ATOM   643  O  OE1   . GLN A 1 83  ? 115.579 177.424 153.823 1.00 61.87  ? 85  GLN B OE1   1 
ATOM   644  N  NE2   . GLN A 1 83  ? 113.632 176.529 154.490 1.00 51.49  ? 85  GLN B NE2   1 
ATOM   645  N  N     . ILE A 1 84  ? 115.377 174.652 148.953 1.00 45.99  ? 86  ILE B N     1 
ATOM   646  C  CA    . ILE A 1 84  ? 115.151 174.188 147.590 1.00 45.55  ? 86  ILE B CA    1 
ATOM   647  C  C     . ILE A 1 84  ? 114.666 172.745 147.533 1.00 46.03  ? 86  ILE B C     1 
ATOM   648  O  O     . ILE A 1 84  ? 114.016 172.358 146.554 1.00 53.85  ? 86  ILE B O     1 
ATOM   649  C  CB    . ILE A 1 84  ? 116.431 174.358 146.752 1.00 45.16  ? 86  ILE B CB    1 
ATOM   650  C  CG1   . ILE A 1 84  ? 116.103 174.397 145.265 1.00 48.62  ? 86  ILE B CG1   1 
ATOM   651  C  CG2   . ILE A 1 84  ? 117.415 173.237 147.023 1.00 46.87  ? 86  ILE B CG2   1 
ATOM   652  C  CD1   . ILE A 1 84  ? 117.317 174.562 144.395 1.00 49.47  ? 86  ILE B CD1   1 
ATOM   653  N  N     . PHE A 1 85  ? 114.938 171.947 148.558 1.00 40.62  ? 87  PHE B N     1 
ATOM   654  C  CA    . PHE A 1 85  ? 114.587 170.539 148.538 1.00 41.06  ? 87  PHE B CA    1 
ATOM   655  C  C     . PHE A 1 85  ? 113.125 170.334 148.905 1.00 48.26  ? 87  PHE B C     1 
ATOM   656  O  O     . PHE A 1 85  ? 112.535 171.111 149.659 1.00 55.94  ? 87  PHE B O     1 
ATOM   657  C  CB    . PHE A 1 85  ? 115.466 169.756 149.508 1.00 39.70  ? 87  PHE B CB    1 
ATOM   658  C  CG    . PHE A 1 85  ? 116.900 169.693 149.107 1.00 37.01  ? 87  PHE B CG    1 
ATOM   659  C  CD1   . PHE A 1 85  ? 117.290 168.948 148.017 1.00 42.82  ? 87  PHE B CD1   1 
ATOM   660  C  CD2   . PHE A 1 85  ? 117.862 170.359 149.827 1.00 44.37  ? 87  PHE B CD2   1 
ATOM   661  C  CE1   . PHE A 1 85  ? 118.605 168.884 147.649 1.00 42.43  ? 87  PHE B CE1   1 
ATOM   662  C  CE2   . PHE A 1 85  ? 119.181 170.294 149.460 1.00 45.66  ? 87  PHE B CE2   1 
ATOM   663  C  CZ    . PHE A 1 85  ? 119.550 169.557 148.371 1.00 42.99  ? 87  PHE B CZ    1 
ATOM   664  N  N     . ARG A 1 86  ? 112.547 169.270 148.371 1.00 42.28  ? 88  ARG B N     1 
ATOM   665  C  CA    . ARG A 1 86  ? 111.181 168.924 148.721 1.00 35.04  ? 88  ARG B CA    1 
ATOM   666  C  C     . ARG A 1 86  ? 111.138 168.402 150.149 1.00 52.09  ? 88  ARG B C     1 
ATOM   667  O  O     . ARG A 1 86  ? 111.899 167.490 150.491 1.00 58.10  ? 88  ARG B O     1 
ATOM   668  C  CB    . ARG A 1 86  ? 110.625 167.877 147.769 1.00 39.22  ? 88  ARG B CB    1 
ATOM   669  C  CG    . ARG A 1 86  ? 109.241 167.418 148.134 1.00 47.03  ? 88  ARG B CG    1 
ATOM   670  C  CD    . ARG A 1 86  ? 108.779 166.293 147.241 1.00 50.36  ? 88  ARG B CD    1 
ATOM   671  N  NE    . ARG A 1 86  ? 108.252 166.782 145.976 1.00 44.13  ? 88  ARG B NE    1 
ATOM   672  C  CZ    . ARG A 1 86  ? 108.830 166.590 144.800 1.00 49.43  ? 88  ARG B CZ    1 
ATOM   673  N  NH1   . ARG A 1 86  ? 109.958 165.909 144.689 1.00 51.57  ? 88  ARG B NH1   1 
ATOM   674  N  NH2   . ARG A 1 86  ? 108.262 167.090 143.708 1.00 52.47  ? 88  ARG B NH2   1 
ATOM   675  N  N     . PRO A 1 87  ? 110.279 168.948 151.010 1.00 50.28  ? 89  PRO B N     1 
ATOM   676  C  CA    . PRO A 1 87  ? 110.238 168.478 152.403 1.00 43.39  ? 89  PRO B CA    1 
ATOM   677  C  C     . PRO A 1 87  ? 109.827 167.024 152.555 1.00 42.79  ? 89  PRO B C     1 
ATOM   678  O  O     . PRO A 1 87  ? 110.125 166.421 153.592 1.00 50.81  ? 89  PRO B O     1 
ATOM   679  C  CB    . PRO A 1 87  ? 109.223 169.422 153.060 1.00 44.31  ? 89  PRO B CB    1 
ATOM   680  C  CG    . PRO A 1 87  ? 108.456 170.015 151.936 1.00 38.08  ? 89  PRO B CG    1 
ATOM   681  C  CD    . PRO A 1 87  ? 109.383 170.090 150.785 1.00 41.39  ? 89  PRO B CD    1 
ATOM   682  N  N     . ASP A 1 88  ? 109.164 166.437 151.563 1.00 45.93  ? 90  ASP B N     1 
ATOM   683  C  CA    . ASP A 1 88  ? 108.737 165.047 151.650 1.00 47.51  ? 90  ASP B CA    1 
ATOM   684  C  C     . ASP A 1 88  ? 109.859 164.057 151.378 1.00 50.82  ? 90  ASP B C     1 
ATOM   685  O  O     . ASP A 1 88  ? 109.679 162.864 151.635 1.00 55.67  ? 90  ASP B O     1 
ATOM   686  C  CB    . ASP A 1 88  ? 107.589 164.788 150.674 1.00 55.74  ? 90  ASP B CB    1 
ATOM   687  C  CG    . ASP A 1 88  ? 106.238 165.164 151.251 1.00 64.10  ? 90  ASP B CG    1 
ATOM   688  O  OD1   . ASP A 1 88  ? 106.171 165.483 152.456 1.00 63.40  ? 90  ASP B OD1   1 
ATOM   689  O  OD2   . ASP A 1 88  ? 105.241 165.141 150.498 1.00 63.74  ? 90  ASP B OD2   1 
ATOM   690  N  N     . ASN A 1 89  ? 110.998 164.511 150.862 1.00 49.41  ? 91  ASN B N     1 
ATOM   691  C  CA    . ASN A 1 89  ? 112.114 163.635 150.537 1.00 38.79  ? 91  ASN B CA    1 
ATOM   692  C  C     . ASN A 1 89  ? 113.127 163.510 151.667 1.00 45.20  ? 91  ASN B C     1 
ATOM   693  O  O     . ASN A 1 89  ? 114.140 162.828 151.494 1.00 52.16  ? 91  ASN B O     1 
ATOM   694  C  CB    . ASN A 1 89  ? 112.817 164.128 149.274 1.00 38.09  ? 91  ASN B CB    1 
ATOM   695  C  CG    . ASN A 1 89  ? 112.063 163.775 148.017 1.00 48.89  ? 91  ASN B CG    1 
ATOM   696  O  OD1   . ASN A 1 89  ? 110.895 163.405 148.069 1.00 52.40  ? 91  ASN B OD1   1 
ATOM   697  N  ND2   . ASN A 1 89  ? 112.725 163.891 146.877 1.00 48.90  ? 91  ASN B ND2   1 
ATOM   698  N  N     . PHE A 1 90  ? 112.891 164.154 152.807 1.00 46.33  ? 92  PHE B N     1 
ATOM   699  C  CA    . PHE A 1 90  ? 113.715 163.949 153.993 1.00 41.00  ? 92  PHE B CA    1 
ATOM   700  C  C     . PHE A 1 90  ? 113.184 162.735 154.746 1.00 45.55  ? 92  PHE B C     1 
ATOM   701  O  O     . PHE A 1 90  ? 112.082 162.775 155.298 1.00 50.03  ? 92  PHE B O     1 
ATOM   702  C  CB    . PHE A 1 90  ? 113.688 165.177 154.897 1.00 43.26  ? 92  PHE B CB    1 
ATOM   703  C  CG    . PHE A 1 90  ? 114.417 166.367 154.354 1.00 41.69  ? 92  PHE B CG    1 
ATOM   704  C  CD1   . PHE A 1 90  ? 113.880 167.124 153.337 1.00 44.80  ? 92  PHE B CD1   1 
ATOM   705  C  CD2   . PHE A 1 90  ? 115.616 166.762 154.902 1.00 46.98  ? 92  PHE B CD2   1 
ATOM   706  C  CE1   . PHE A 1 90  ? 114.542 168.227 152.858 1.00 40.59  ? 92  PHE B CE1   1 
ATOM   707  C  CE2   . PHE A 1 90  ? 116.277 167.865 154.423 1.00 48.54  ? 92  PHE B CE2   1 
ATOM   708  C  CZ    . PHE A 1 90  ? 115.739 168.596 153.403 1.00 42.98  ? 92  PHE B CZ    1 
ATOM   709  N  N     . VAL A 1 91  ? 113.975 161.637 154.734 1.00 37.69  ? 93  VAL B N     1 
ATOM   710  C  CA    . VAL A 1 91  ? 113.624 160.391 155.460 1.00 32.00  ? 93  VAL B CA    1 
ATOM   711  C  C     . VAL A 1 91  ? 114.660 160.203 156.569 1.00 45.82  ? 93  VAL B C     1 
ATOM   712  O  O     . VAL A 1 91  ? 115.833 160.025 156.236 1.00 51.64  ? 93  VAL B O     1 
ATOM   713  C  CB    . VAL A 1 91  ? 113.604 159.182 154.521 1.00 34.69  ? 93  VAL B CB    1 
ATOM   714  C  CG1   . VAL A 1 91  ? 113.346 157.886 155.274 1.00 38.74  ? 93  VAL B CG1   1 
ATOM   715  C  CG2   . VAL A 1 91  ? 112.590 159.352 153.402 1.00 47.84  ? 93  VAL B CG2   1 
ATOM   716  N  N     . PHE A 1 92  ? 114.215 160.233 157.850 1.00 52.31  ? 94  PHE B N     1 
ATOM   717  C  CA    . PHE A 1 92  ? 115.139 160.087 158.963 1.00 44.98  ? 94  PHE B CA    1 
ATOM   718  C  C     . PHE A 1 92  ? 114.475 159.325 160.097 1.00 44.77  ? 94  PHE B C     1 
ATOM   719  O  O     . PHE A 1 92  ? 113.252 159.338 160.244 1.00 48.82  ? 94  PHE B O     1 
ATOM   720  C  CB    . PHE A 1 92  ? 115.636 161.446 159.463 1.00 41.80  ? 94  PHE B CB    1 
ATOM   721  C  CG    . PHE A 1 92  ? 114.542 162.426 159.747 1.00 43.84  ? 94  PHE B CG    1 
ATOM   722  C  CD1   . PHE A 1 92  ? 113.921 162.450 160.977 1.00 41.64  ? 94  PHE B CD1   1 
ATOM   723  C  CD2   . PHE A 1 92  ? 114.138 163.327 158.786 1.00 50.39  ? 94  PHE B CD2   1 
ATOM   724  C  CE1   . PHE A 1 92  ? 112.918 163.350 161.239 1.00 45.49  ? 94  PHE B CE1   1 
ATOM   725  C  CE2   . PHE A 1 92  ? 113.134 164.228 159.045 1.00 51.55  ? 94  PHE B CE2   1 
ATOM   726  C  CZ    . PHE A 1 92  ? 112.525 164.238 160.273 1.00 50.98  ? 94  PHE B CZ    1 
ATOM   727  N  N     . GLY A 1 93  ? 115.300 158.657 160.895 1.00 48.32  ? 95  GLY B N     1 
ATOM   728  C  CA    . GLY A 1 93  ? 114.868 158.001 162.104 1.00 51.56  ? 95  GLY B CA    1 
ATOM   729  C  C     . GLY A 1 93  ? 115.273 158.776 163.339 1.00 56.07  ? 95  GLY B C     1 
ATOM   730  O  O     . GLY A 1 93  ? 115.479 159.995 163.304 1.00 61.13  ? 95  GLY B O     1 
ATOM   731  N  N     . GLN A 1 94  ? 115.396 158.065 164.443 1.00 50.30  ? 96  GLN B N     1 
ATOM   732  C  CA    . GLN A 1 94  ? 115.742 158.731 165.693 1.00 48.67  ? 96  GLN B CA    1 
ATOM   733  C  C     . GLN A 1 94  ? 116.962 158.135 166.376 1.00 50.99  ? 96  GLN B C     1 
ATOM   734  O  O     . GLN A 1 94  ? 117.717 158.870 167.014 1.00 57.35  ? 96  GLN B O     1 
ATOM   735  C  CB    . GLN A 1 94  ? 114.545 158.702 166.647 1.00 49.82  ? 96  GLN B CB    1 
ATOM   736  C  CG    . GLN A 1 94  ? 113.335 159.446 166.124 1.00 51.43  ? 96  GLN B CG    1 
ATOM   737  C  CD    . GLN A 1 94  ? 113.625 160.903 165.845 1.00 53.59  ? 96  GLN B CD    1 
ATOM   738  O  OE1   . GLN A 1 94  ? 114.427 161.531 166.533 1.00 54.12  ? 96  GLN B OE1   1 
ATOM   739  N  NE2   . GLN A 1 94  ? 112.966 161.452 164.833 1.00 51.93  ? 96  GLN B NE2   1 
ATOM   740  N  N     . SER A 1 95  ? 117.174 156.831 166.263 1.00 51.73  ? 97  SER B N     1 
ATOM   741  C  CA    . SER A 1 95  ? 118.348 156.191 166.835 1.00 53.17  ? 97  SER B CA    1 
ATOM   742  C  C     . SER A 1 95  ? 119.393 155.980 165.749 1.00 56.29  ? 97  SER B C     1 
ATOM   743  O  O     . SER A 1 95  ? 119.118 155.338 164.731 1.00 64.28  ? 97  SER B O     1 
ATOM   744  C  CB    . SER A 1 95  ? 117.973 154.859 167.480 1.00 56.97  ? 97  SER B CB    1 
ATOM   745  O  OG    . SER A 1 95  ? 117.351 154.003 166.541 1.00 57.24  ? 97  SER B OG    1 
ATOM   746  N  N     . GLY A 1 96  ? 120.585 156.514 165.971 1.00 45.37  ? 98  GLY B N     1 
ATOM   747  C  CA    . GLY A 1 96  ? 121.620 156.461 164.965 1.00 47.48  ? 98  GLY B CA    1 
ATOM   748  C  C     . GLY A 1 96  ? 122.214 155.079 164.806 1.00 51.08  ? 98  GLY B C     1 
ATOM   749  O  O     . GLY A 1 96  ? 121.924 154.142 165.549 1.00 55.73  ? 98  GLY B O     1 
ATOM   750  N  N     . ALA A 1 97  ? 123.070 154.956 163.795 1.00 47.82  ? 99  ALA B N     1 
ATOM   751  C  CA    . ALA A 1 97  ? 123.737 153.687 163.551 1.00 43.11  ? 99  ALA B CA    1 
ATOM   752  C  C     . ALA A 1 97  ? 124.779 153.389 164.616 1.00 41.81  ? 99  ALA B C     1 
ATOM   753  O  O     . ALA A 1 97  ? 125.105 152.220 164.849 1.00 52.53  ? 99  ALA B O     1 
ATOM   754  C  CB    . ALA A 1 97  ? 124.378 153.687 162.166 1.00 50.08  ? 99  ALA B CB    1 
ATOM   755  N  N     . GLY A 1 98  ? 125.311 154.417 165.267 1.00 37.76  ? 100 GLY B N     1 
ATOM   756  C  CA    . GLY A 1 98  ? 126.327 154.208 166.283 1.00 37.62  ? 100 GLY B CA    1 
ATOM   757  C  C     . GLY A 1 98  ? 127.621 153.639 165.747 1.00 42.42  ? 100 GLY B C     1 
ATOM   758  O  O     . GLY A 1 98  ? 128.278 152.847 166.433 1.00 46.85  ? 100 GLY B O     1 
ATOM   759  N  N     . ASN A 1 99  ? 128.002 154.027 164.532 1.00 36.47  ? 101 ASN B N     1 
ATOM   760  C  CA    . ASN A 1 99  ? 129.220 153.546 163.884 1.00 31.45  ? 101 ASN B CA    1 
ATOM   761  C  C     . ASN A 1 99  ? 129.232 152.025 163.773 1.00 40.28  ? 101 ASN B C     1 
ATOM   762  O  O     . ASN A 1 99  ? 130.276 151.384 163.891 1.00 48.30  ? 101 ASN B O     1 
ATOM   763  C  CB    . ASN A 1 99  ? 130.462 154.048 164.616 1.00 34.73  ? 101 ASN B CB    1 
ATOM   764  C  CG    . ASN A 1 99  ? 130.797 155.473 164.269 1.00 46.17  ? 101 ASN B CG    1 
ATOM   765  O  OD1   . ASN A 1 99  ? 130.220 156.049 163.350 1.00 50.34  ? 101 ASN B OD1   1 
ATOM   766  N  ND2   . ASN A 1 99  ? 131.726 156.060 165.011 1.00 49.95  ? 101 ASN B ND2   1 
ATOM   767  N  N     . ASN A 1 100 ? 128.063 151.443 163.533 1.00 47.05  ? 102 ASN B N     1 
ATOM   768  C  CA    . ASN A 1 100 ? 127.892 149.999 163.465 1.00 38.61  ? 102 ASN B CA    1 
ATOM   769  C  C     . ASN A 1 100 ? 127.336 149.631 162.100 1.00 42.15  ? 102 ASN B C     1 
ATOM   770  O  O     . ASN A 1 100 ? 126.225 150.041 161.750 1.00 51.70  ? 102 ASN B O     1 
ATOM   771  C  CB    . ASN A 1 100 ? 126.958 149.509 164.567 1.00 38.36  ? 102 ASN B CB    1 
ATOM   772  C  CG    . ASN A 1 100 ? 127.204 148.076 164.934 1.00 42.44  ? 102 ASN B CG    1 
ATOM   773  O  OD1   . ASN A 1 100 ? 127.813 147.329 164.175 1.00 49.34  ? 102 ASN B OD1   1 
ATOM   774  N  ND2   . ASN A 1 100 ? 126.720 147.673 166.098 1.00 44.92  ? 102 ASN B ND2   1 
ATOM   775  N  N     . TRP A 1 101 ? 128.107 148.863 161.331 1.00 38.24  ? 103 TRP B N     1 
ATOM   776  C  CA    . TRP A 1 101 ? 127.620 148.398 160.039 1.00 38.39  ? 103 TRP B CA    1 
ATOM   777  C  C     . TRP A 1 101 ? 126.419 147.483 160.208 1.00 36.02  ? 103 TRP B C     1 
ATOM   778  O  O     . TRP A 1 101 ? 125.427 147.601 159.479 1.00 51.24  ? 103 TRP B O     1 
ATOM   779  C  CB    . TRP A 1 101 ? 128.737 147.678 159.288 1.00 42.70  ? 103 TRP B CB    1 
ATOM   780  C  CG    . TRP A 1 101 ? 128.373 147.299 157.896 1.00 41.50  ? 103 TRP B CG    1 
ATOM   781  C  CD1   . TRP A 1 101 ? 128.587 148.031 156.776 1.00 45.11  ? 103 TRP B CD1   1 
ATOM   782  C  CD2   . TRP A 1 101 ? 127.736 146.095 157.473 1.00 38.92  ? 103 TRP B CD2   1 
ATOM   783  N  NE1   . TRP A 1 101 ? 128.118 147.363 155.677 1.00 47.83  ? 103 TRP B NE1   1 
ATOM   784  C  CE2   . TRP A 1 101 ? 127.591 146.168 156.081 1.00 39.06  ? 103 TRP B CE2   1 
ATOM   785  C  CE3   . TRP A 1 101 ? 127.268 144.961 158.139 1.00 42.34  ? 103 TRP B CE3   1 
ATOM   786  C  CZ2   . TRP A 1 101 ? 127.000 145.158 155.342 1.00 39.89  ? 103 TRP B CZ2   1 
ATOM   787  C  CZ3   . TRP A 1 101 ? 126.686 143.959 157.401 1.00 44.79  ? 103 TRP B CZ3   1 
ATOM   788  C  CH2   . TRP A 1 101 ? 126.557 144.063 156.018 1.00 43.34  ? 103 TRP B CH2   1 
ATOM   789  N  N     . ALA A 1 102 ? 126.488 146.573 161.177 1.00 33.96  ? 104 ALA B N     1 
ATOM   790  C  CA    . ALA A 1 102 ? 125.414 145.610 161.367 1.00 38.71  ? 104 ALA B CA    1 
ATOM   791  C  C     . ALA A 1 102 ? 124.116 146.304 161.730 1.00 38.74  ? 104 ALA B C     1 
ATOM   792  O  O     . ALA A 1 102 ? 123.047 145.931 161.239 1.00 42.47  ? 104 ALA B O     1 
ATOM   793  C  CB    . ALA A 1 102 ? 125.800 144.605 162.449 1.00 45.78  ? 104 ALA B CB    1 
ATOM   794  N  N     . LYS A 1 103 ? 124.187 147.322 162.585 1.00 43.02  ? 105 LYS B N     1 
ATOM   795  C  CA    . LYS A 1 103 ? 122.978 148.001 163.028 1.00 39.29  ? 105 LYS B CA    1 
ATOM   796  C  C     . LYS A 1 103 ? 122.259 148.652 161.857 1.00 36.13  ? 105 LYS B C     1 
ATOM   797  O  O     . LYS A 1 103 ? 121.075 148.390 161.616 1.00 49.92  ? 105 LYS B O     1 
ATOM   798  C  CB    . LYS A 1 103 ? 123.332 149.037 164.093 1.00 42.76  ? 105 LYS B CB    1 
ATOM   799  C  CG    . LYS A 1 103 ? 122.138 149.723 164.705 1.00 49.53  ? 105 LYS B CG    1 
ATOM   800  C  CD    . LYS A 1 103 ? 122.529 150.485 165.956 1.00 48.47  ? 105 LYS B CD    1 
ATOM   801  C  CE    . LYS A 1 103 ? 123.067 149.551 167.017 1.00 48.55  ? 105 LYS B CE    1 
ATOM   802  N  NZ    . LYS A 1 103 ? 123.346 150.273 168.284 1.00 50.48  ? 105 LYS B NZ    1 
ATOM   803  N  N     . GLY A 1 104 ? 122.979 149.461 161.082 1.00 39.13  ? 106 GLY B N     1 
ATOM   804  C  CA    . GLY A 1 104 ? 122.379 150.159 159.964 1.00 44.29  ? 106 GLY B CA    1 
ATOM   805  C  C     . GLY A 1 104 ? 122.019 149.270 158.798 1.00 48.36  ? 106 GLY B C     1 
ATOM   806  O  O     . GLY A 1 104 ? 121.166 149.646 157.989 1.00 57.09  ? 106 GLY B O     1 
ATOM   807  N  N     . HIS A 1 105 ? 122.641 148.099 158.689 1.00 46.41  ? 107 HIS B N     1 
ATOM   808  C  CA    . HIS A 1 105 ? 122.313 147.187 157.605 1.00 37.40  ? 107 HIS B CA    1 
ATOM   809  C  C     . HIS A 1 105 ? 121.208 146.203 157.956 1.00 42.39  ? 107 HIS B C     1 
ATOM   810  O  O     . HIS A 1 105 ? 120.539 145.706 157.046 1.00 53.17  ? 107 HIS B O     1 
ATOM   811  C  CB    . HIS A 1 105 ? 123.555 146.404 157.174 1.00 42.77  ? 107 HIS B CB    1 
ATOM   812  C  CG    . HIS A 1 105 ? 123.418 145.738 155.841 1.00 46.99  ? 107 HIS B CG    1 
ATOM   813  N  ND1   . HIS A 1 105 ? 122.773 144.533 155.675 1.00 47.09  ? 107 HIS B ND1   1 
ATOM   814  C  CD2   . HIS A 1 105 ? 123.852 146.103 154.613 1.00 46.89  ? 107 HIS B CD2   1 
ATOM   815  C  CE1   . HIS A 1 105 ? 122.811 144.187 154.402 1.00 47.64  ? 107 HIS B CE1   1 
ATOM   816  N  NE2   . HIS A 1 105 ? 123.462 145.122 153.736 1.00 40.47  ? 107 HIS B NE2   1 
ATOM   817  N  N     . TYR A 1 106 ? 120.994 145.902 159.234 1.00 46.54  ? 108 TYR B N     1 
ATOM   818  C  CA    . TYR A 1 106 ? 120.055 144.854 159.608 1.00 45.41  ? 108 TYR B CA    1 
ATOM   819  C  C     . TYR A 1 106 ? 118.930 145.309 160.522 1.00 52.12  ? 108 TYR B C     1 
ATOM   820  O  O     . TYR A 1 106 ? 117.788 144.892 160.323 1.00 58.02  ? 108 TYR B O     1 
ATOM   821  C  CB    . TYR A 1 106 ? 120.800 143.699 160.285 1.00 41.09  ? 108 TYR B CB    1 
ATOM   822  C  CG    . TYR A 1 106 ? 121.545 142.806 159.328 1.00 42.79  ? 108 TYR B CG    1 
ATOM   823  C  CD1   . TYR A 1 106 ? 120.873 141.897 158.533 1.00 46.86  ? 108 TYR B CD1   1 
ATOM   824  C  CD2   . TYR A 1 106 ? 122.921 142.862 159.230 1.00 50.62  ? 108 TYR B CD2   1 
ATOM   825  C  CE1   . TYR A 1 106 ? 121.552 141.080 157.661 1.00 47.66  ? 108 TYR B CE1   1 
ATOM   826  C  CE2   . TYR A 1 106 ? 123.606 142.047 158.360 1.00 48.83  ? 108 TYR B CE2   1 
ATOM   827  C  CZ    . TYR A 1 106 ? 122.918 141.160 157.580 1.00 48.93  ? 108 TYR B CZ    1 
ATOM   828  O  OH    . TYR A 1 106 ? 123.603 140.348 156.714 1.00 55.15  ? 108 TYR B OH    1 
ATOM   829  N  N     . THR A 1 107 ? 119.205 146.133 161.534 1.00 53.50  ? 109 THR B N     1 
ATOM   830  C  CA    . THR A 1 107 ? 118.208 146.406 162.565 1.00 50.98  ? 109 THR B CA    1 
ATOM   831  C  C     . THR A 1 107 ? 117.507 147.746 162.372 1.00 50.68  ? 109 THR B C     1 
ATOM   832  O  O     . THR A 1 107 ? 116.283 147.791 162.236 1.00 55.90  ? 109 THR B O     1 
ATOM   833  C  CB    . THR A 1 107 ? 118.856 146.339 163.952 1.00 51.98  ? 109 THR B CB    1 
ATOM   834  O  OG1   . THR A 1 107 ? 120.001 147.197 163.990 1.00 60.04  ? 109 THR B OG1   1 
ATOM   835  C  CG2   . THR A 1 107 ? 119.284 144.922 164.264 1.00 51.60  ? 109 THR B CG2   1 
ATOM   836  N  N     . GLU A 1 108 ? 118.257 148.843 162.357 1.00 55.77  ? 110 GLU B N     1 
ATOM   837  C  CA    . GLU A 1 108 ? 117.645 150.158 162.220 1.00 55.38  ? 110 GLU B CA    1 
ATOM   838  C  C     . GLU A 1 108 ? 117.383 150.537 160.772 1.00 57.33  ? 110 GLU B C     1 
ATOM   839  O  O     . GLU A 1 108 ? 116.376 151.192 160.485 1.00 62.82  ? 110 GLU B O     1 
ATOM   840  C  CB    . GLU A 1 108 ? 118.523 151.226 162.872 1.00 57.13  ? 110 GLU B CB    1 
ATOM   841  C  CG    . GLU A 1 108 ? 118.776 150.998 164.345 1.00 59.89  ? 110 GLU B CG    1 
ATOM   842  C  CD    . GLU A 1 108 ? 117.545 151.232 165.193 1.00 65.52  ? 110 GLU B CD    1 
ATOM   843  O  OE1   . GLU A 1 108 ? 116.629 151.946 164.733 1.00 64.70  ? 110 GLU B OE1   1 
ATOM   844  O  OE2   . GLU A 1 108 ? 117.490 150.699 166.321 1.00 67.20  ? 110 GLU B OE2   1 
ATOM   845  N  N     . GLY A 1 109 ? 118.267 150.148 159.853 1.00 52.62  ? 111 GLY B N     1 
ATOM   846  C  CA    . GLY A 1 109 ? 118.047 150.437 158.451 1.00 50.78  ? 111 GLY B CA    1 
ATOM   847  C  C     . GLY A 1 109 ? 116.964 149.606 157.806 1.00 55.46  ? 111 GLY B C     1 
ATOM   848  O  O     . GLY A 1 109 ? 116.387 150.035 156.802 1.00 64.03  ? 111 GLY B O     1 
ATOM   849  N  N     . ALA A 1 110 ? 116.679 148.425 158.352 1.00 53.10  ? 112 ALA B N     1 
ATOM   850  C  CA    . ALA A 1 110 ? 115.602 147.607 157.810 1.00 53.58  ? 112 ALA B CA    1 
ATOM   851  C  C     . ALA A 1 110 ? 114.237 148.235 158.057 1.00 57.72  ? 112 ALA B C     1 
ATOM   852  O  O     . ALA A 1 110 ? 113.338 148.104 157.220 1.00 61.61  ? 112 ALA B O     1 
ATOM   853  C  CB    . ALA A 1 110 ? 115.654 146.203 158.406 1.00 55.76  ? 112 ALA B CB    1 
ATOM   854  N  N     . GLU A 1 111 ? 114.059 148.913 159.186 1.00 56.57  ? 113 GLU B N     1 
ATOM   855  C  CA    . GLU A 1 111 ? 112.790 149.554 159.498 1.00 53.63  ? 113 GLU B CA    1 
ATOM   856  C  C     . GLU A 1 111 ? 112.636 150.916 158.838 1.00 55.98  ? 113 GLU B C     1 
ATOM   857  O  O     . GLU A 1 111 ? 111.586 151.545 158.993 1.00 62.46  ? 113 GLU B O     1 
ATOM   858  C  CB    . GLU A 1 111 ? 112.632 149.694 161.011 1.00 60.76  ? 113 GLU B CB    1 
ATOM   859  C  CG    . GLU A 1 111 ? 112.710 148.381 161.767 1.00 65.54  ? 113 GLU B CG    1 
ATOM   860  C  CD    . GLU A 1 111 ? 111.513 147.487 161.509 1.00 70.44  ? 113 GLU B CD    1 
ATOM   861  O  OE1   . GLU A 1 111 ? 110.409 148.022 161.274 1.00 69.53  ? 113 GLU B OE1   1 
ATOM   862  O  OE2   . GLU A 1 111 ? 111.675 146.249 161.542 1.00 66.69  ? 113 GLU B OE2   1 
ATOM   863  N  N     . LEU A 1 112 ? 113.652 151.388 158.119 1.00 53.37  ? 114 LEU B N     1 
ATOM   864  C  CA    . LEU A 1 112 ? 113.598 152.668 157.436 1.00 51.87  ? 114 LEU B CA    1 
ATOM   865  C  C     . LEU A 1 112 ? 113.715 152.557 155.926 1.00 58.29  ? 114 LEU B C     1 
ATOM   866  O  O     . LEU A 1 112 ? 113.505 153.560 155.235 1.00 69.72  ? 114 LEU B O     1 
ATOM   867  C  CB    . LEU A 1 112 ? 114.710 153.594 157.951 1.00 54.25  ? 114 LEU B CB    1 
ATOM   868  C  CG    . LEU A 1 112 ? 114.410 155.088 157.959 1.00 58.04  ? 114 LEU B CG    1 
ATOM   869  C  CD1   . LEU A 1 112 ? 113.421 155.432 159.058 1.00 58.84  ? 114 LEU B CD1   1 
ATOM   870  C  CD2   . LEU A 1 112 ? 115.689 155.880 158.118 1.00 58.44  ? 114 LEU B CD2   1 
ATOM   871  N  N     . VAL A 1 113 ? 114.033 151.379 155.390 1.00 51.98  ? 115 VAL B N     1 
ATOM   872  C  CA    . VAL A 1 113 ? 114.307 151.266 153.964 1.00 53.37  ? 115 VAL B CA    1 
ATOM   873  C  C     . VAL A 1 113 ? 113.035 151.189 153.130 1.00 55.78  ? 115 VAL B C     1 
ATOM   874  O  O     . VAL A 1 113 ? 113.068 151.518 151.938 1.00 60.62  ? 115 VAL B O     1 
ATOM   875  C  CB    . VAL A 1 113 ? 115.212 150.053 153.690 1.00 58.23  ? 115 VAL B CB    1 
ATOM   876  C  CG1   . VAL A 1 113 ? 114.406 148.762 153.683 1.00 60.11  ? 115 VAL B CG1   1 
ATOM   877  C  CG2   . VAL A 1 113 ? 115.968 150.235 152.390 1.00 58.62  ? 115 VAL B CG2   1 
ATOM   878  N  N     . ASP A 1 114 ? 111.911 150.780 153.721 1.00 59.14  ? 116 ASP B N     1 
ATOM   879  C  CA    . ASP A 1 114 ? 110.655 150.776 152.981 1.00 58.26  ? 116 ASP B CA    1 
ATOM   880  C  C     . ASP A 1 114 ? 110.250 152.187 152.571 1.00 60.24  ? 116 ASP B C     1 
ATOM   881  O  O     . ASP A 1 114 ? 109.817 152.410 151.435 1.00 68.22  ? 116 ASP B O     1 
ATOM   882  C  CB    . ASP A 1 114 ? 109.558 150.124 153.816 1.00 61.14  ? 116 ASP B CB    1 
ATOM   883  C  CG    . ASP A 1 114 ? 109.748 148.630 153.955 1.00 68.15  ? 116 ASP B CG    1 
ATOM   884  O  OD1   . ASP A 1 114 ? 110.732 148.102 153.397 1.00 69.92  ? 116 ASP B OD1   1 
ATOM   885  O  OD2   . ASP A 1 114 ? 108.914 147.981 154.622 1.00 65.60  ? 116 ASP B OD2   1 
ATOM   886  N  N     . SER A 1 115 ? 110.393 153.154 153.479 1.00 42.25  ? 117 SER B N     1 
ATOM   887  C  CA    . SER A 1 115 ? 110.042 154.531 153.152 1.00 43.67  ? 117 SER B CA    1 
ATOM   888  C  C     . SER A 1 115 ? 110.949 155.090 152.062 1.00 51.01  ? 117 SER B C     1 
ATOM   889  O  O     . SER A 1 115 ? 110.485 155.784 151.143 1.00 61.40  ? 117 SER B O     1 
ATOM   890  C  CB    . SER A 1 115 ? 110.112 155.391 154.411 1.00 50.42  ? 117 SER B CB    1 
ATOM   891  O  OG    . SER A 1 115 ? 109.818 156.747 154.120 1.00 60.77  ? 117 SER B OG    1 
ATOM   892  N  N     . VAL A 1 116 ? 112.247 154.799 152.148 1.00 44.56  ? 118 VAL B N     1 
ATOM   893  C  CA    . VAL A 1 116 ? 113.186 155.272 151.138 1.00 44.01  ? 118 VAL B CA    1 
ATOM   894  C  C     . VAL A 1 116 ? 112.856 154.668 149.783 1.00 48.52  ? 118 VAL B C     1 
ATOM   895  O  O     . VAL A 1 116 ? 112.892 155.353 148.754 1.00 55.88  ? 118 VAL B O     1 
ATOM   896  C  CB    . VAL A 1 116 ? 114.631 154.959 151.561 1.00 46.89  ? 118 VAL B CB    1 
ATOM   897  C  CG1   . VAL A 1 116 ? 115.605 155.642 150.626 1.00 51.13  ? 118 VAL B CG1   1 
ATOM   898  C  CG2   . VAL A 1 116 ? 114.867 155.406 152.985 1.00 47.40  ? 118 VAL B CG2   1 
ATOM   899  N  N     . LEU A 1 117 ? 112.538 153.375 149.755 1.00 47.11  ? 119 LEU B N     1 
ATOM   900  C  CA    . LEU A 1 117 ? 112.166 152.749 148.494 1.00 45.46  ? 119 LEU B CA    1 
ATOM   901  C  C     . LEU A 1 117 ? 110.877 153.342 147.948 1.00 46.43  ? 119 LEU B C     1 
ATOM   902  O  O     . LEU A 1 117 ? 110.725 153.496 146.734 1.00 56.12  ? 119 LEU B O     1 
ATOM   903  C  CB    . LEU A 1 117 ? 112.040 151.240 148.672 1.00 50.65  ? 119 LEU B CB    1 
ATOM   904  C  CG    . LEU A 1 117 ? 113.353 150.473 148.545 1.00 49.22  ? 119 LEU B CG    1 
ATOM   905  C  CD1   . LEU A 1 117 ? 113.124 148.996 148.789 1.00 51.71  ? 119 LEU B CD1   1 
ATOM   906  C  CD2   . LEU A 1 117 ? 113.964 150.700 147.183 1.00 51.85  ? 119 LEU B CD2   1 
ATOM   907  N  N     . ASP A 1 118 ? 109.936 153.685 148.827 1.00 46.08  ? 120 ASP B N     1 
ATOM   908  C  CA    . ASP A 1 118 ? 108.687 154.283 148.371 1.00 45.03  ? 120 ASP B CA    1 
ATOM   909  C  C     . ASP A 1 118 ? 108.936 155.625 147.700 1.00 46.34  ? 120 ASP B C     1 
ATOM   910  O  O     . ASP A 1 118 ? 108.399 155.906 146.620 1.00 58.34  ? 120 ASP B O     1 
ATOM   911  C  CB    . ASP A 1 118 ? 107.723 154.438 149.545 1.00 51.57  ? 120 ASP B CB    1 
ATOM   912  C  CG    . ASP A 1 118 ? 106.271 154.349 149.121 1.00 62.22  ? 120 ASP B CG    1 
ATOM   913  O  OD1   . ASP A 1 118 ? 105.964 154.718 147.968 1.00 64.31  ? 120 ASP B OD1   1 
ATOM   914  O  OD2   . ASP A 1 118 ? 105.436 153.911 149.939 1.00 60.71  ? 120 ASP B OD2   1 
ATOM   915  N  N     . VAL A 1 119 ? 109.767 156.464 148.317 1.00 44.56  ? 121 VAL B N     1 
ATOM   916  C  CA    . VAL A 1 119 ? 110.027 157.775 147.728 1.00 45.51  ? 121 VAL B CA    1 
ATOM   917  C  C     . VAL A 1 119 ? 110.860 157.646 146.451 1.00 42.54  ? 121 VAL B C     1 
ATOM   918  O  O     . VAL A 1 119 ? 110.655 158.396 145.489 1.00 44.15  ? 121 VAL B O     1 
ATOM   919  C  CB    . VAL A 1 119 ? 110.664 158.720 148.765 1.00 44.38  ? 121 VAL B CB    1 
ATOM   920  C  CG1   . VAL A 1 119 ? 112.053 158.272 149.150 1.00 48.55  ? 121 VAL B CG1   1 
ATOM   921  C  CG2   . VAL A 1 119 ? 110.685 160.135 148.240 1.00 46.31  ? 121 VAL B CG2   1 
ATOM   922  N  N     . VAL A 1 120 ? 111.784 156.679 146.401 1.00 45.04  ? 122 VAL B N     1 
ATOM   923  C  CA    . VAL A 1 120 ? 112.549 156.436 145.176 1.00 38.48  ? 122 VAL B CA    1 
ATOM   924  C  C     . VAL A 1 120 ? 111.622 156.005 144.046 1.00 46.19  ? 122 VAL B C     1 
ATOM   925  O  O     . VAL A 1 120 ? 111.712 156.501 142.918 1.00 57.07  ? 122 VAL B O     1 
ATOM   926  C  CB    . VAL A 1 120 ? 113.644 155.381 145.420 1.00 42.74  ? 122 VAL B CB    1 
ATOM   927  C  CG1   . VAL A 1 120 ? 114.132 154.812 144.107 1.00 48.23  ? 122 VAL B CG1   1 
ATOM   928  C  CG2   . VAL A 1 120 ? 114.797 155.954 146.204 1.00 45.42  ? 122 VAL B CG2   1 
ATOM   929  N  N     . ARG A 1 121 ? 110.717 155.070 144.338 1.00 48.68  ? 123 ARG B N     1 
ATOM   930  C  CA    . ARG A 1 121 ? 109.812 154.553 143.321 1.00 46.28  ? 123 ARG B CA    1 
ATOM   931  C  C     . ARG A 1 121 ? 108.870 155.633 142.815 1.00 46.78  ? 123 ARG B C     1 
ATOM   932  O  O     . ARG A 1 121 ? 108.571 155.693 141.618 1.00 50.43  ? 123 ARG B O     1 
ATOM   933  C  CB    . ARG A 1 121 ? 109.030 153.372 143.888 1.00 46.40  ? 123 ARG B CB    1 
ATOM   934  C  CG    . ARG A 1 121 ? 108.387 152.494 142.845 1.00 51.92  ? 123 ARG B CG    1 
ATOM   935  C  CD    . ARG A 1 121 ? 107.823 151.238 143.473 1.00 52.98  ? 123 ARG B CD    1 
ATOM   936  N  NE    . ARG A 1 121 ? 108.802 150.538 144.294 1.00 55.42  ? 123 ARG B NE    1 
ATOM   937  C  CZ    . ARG A 1 121 ? 108.612 150.208 145.563 1.00 53.24  ? 123 ARG B CZ    1 
ATOM   938  N  NH1   . ARG A 1 121 ? 107.503 150.537 146.203 1.00 52.56  ? 123 ARG B NH1   1 
ATOM   939  N  NH2   . ARG A 1 121 ? 109.554 149.524 146.205 1.00 49.28  ? 123 ARG B NH2   1 
ATOM   940  N  N     . LYS A 1 122 ? 108.379 156.492 143.710 1.00 52.93  ? 124 LYS B N     1 
ATOM   941  C  CA    . LYS A 1 122 ? 107.568 157.618 143.258 1.00 48.63  ? 124 LYS B CA    1 
ATOM   942  C  C     . LYS A 1 122 ? 108.379 158.566 142.388 1.00 51.52  ? 124 LYS B C     1 
ATOM   943  O  O     . LYS A 1 122 ? 107.885 159.059 141.368 1.00 53.72  ? 124 LYS B O     1 
ATOM   944  C  CB    . LYS A 1 122 ? 106.983 158.365 144.452 1.00 49.76  ? 124 LYS B CB    1 
ATOM   945  C  CG    . LYS A 1 122 ? 105.807 159.253 144.100 1.00 50.54  ? 124 LYS B CG    1 
ATOM   946  C  CD    . LYS A 1 122 ? 104.635 158.432 143.578 1.00 57.89  ? 124 LYS B CD    1 
ATOM   947  C  CE    . LYS A 1 122 ? 103.448 159.315 143.218 1.00 61.29  ? 124 LYS B CE    1 
ATOM   948  N  NZ    . LYS A 1 122 ? 102.290 158.527 142.704 1.00 52.78  ? 124 LYS B NZ    1 
ATOM   949  N  N     . GLU A 1 123 ? 109.627 158.839 142.774 1.00 56.42  ? 125 GLU B N     1 
ATOM   950  C  CA    . GLU A 1 123 ? 110.442 159.778 142.012 1.00 48.67  ? 125 GLU B CA    1 
ATOM   951  C  C     . GLU A 1 123 ? 110.843 159.201 140.663 1.00 54.09  ? 125 GLU B C     1 
ATOM   952  O  O     . GLU A 1 123 ? 110.902 159.927 139.665 1.00 61.81  ? 125 GLU B O     1 
ATOM   953  C  CB    . GLU A 1 123 ? 111.680 160.165 142.817 1.00 55.67  ? 125 GLU B CB    1 
ATOM   954  C  CG    . GLU A 1 123 ? 112.093 161.613 142.663 1.00 59.73  ? 125 GLU B CG    1 
ATOM   955  C  CD    . GLU A 1 123 ? 111.468 162.509 143.711 1.00 63.43  ? 125 GLU B CD    1 
ATOM   956  O  OE1   . GLU A 1 123 ? 110.783 161.982 144.612 1.00 62.47  ? 125 GLU B OE1   1 
ATOM   957  O  OE2   . GLU A 1 123 ? 111.660 163.740 143.635 1.00 61.40  ? 125 GLU B OE2   1 
ATOM   958  N  N     . SER A 1 124 ? 111.124 157.900 140.611 1.00 49.74  ? 126 SER B N     1 
ATOM   959  C  CA    . SER A 1 124 ? 111.595 157.278 139.383 1.00 47.69  ? 126 SER B CA    1 
ATOM   960  C  C     . SER A 1 124 ? 110.487 157.035 138.370 1.00 48.19  ? 126 SER B C     1 
ATOM   961  O  O     . SER A 1 124 ? 110.783 156.844 137.188 1.00 53.60  ? 126 SER B O     1 
ATOM   962  C  CB    . SER A 1 124 ? 112.293 155.957 139.694 1.00 51.23  ? 126 SER B CB    1 
ATOM   963  O  OG    . SER A 1 124 ? 112.352 155.142 138.540 1.00 56.31  ? 126 SER B OG    1 
ATOM   964  N  N     . GLU A 1 125 ? 109.227 157.027 138.795 1.00 54.05  ? 127 GLU B N     1 
ATOM   965  C  CA    . GLU A 1 125 ? 108.126 156.853 137.859 1.00 55.31  ? 127 GLU B CA    1 
ATOM   966  C  C     . GLU A 1 125 ? 107.694 158.157 137.210 1.00 54.54  ? 127 GLU B C     1 
ATOM   967  O  O     . GLU A 1 125 ? 106.854 158.130 136.307 1.00 59.47  ? 127 GLU B O     1 
ATOM   968  C  CB    . GLU A 1 125 ? 106.928 156.212 138.564 1.00 63.42  ? 127 GLU B CB    1 
ATOM   969  C  CG    . GLU A 1 125 ? 107.122 154.745 138.914 1.00 66.73  ? 127 GLU B CG    1 
ATOM   970  C  CD    . GLU A 1 125 ? 107.227 153.861 137.688 1.00 67.58  ? 127 GLU B CD    1 
ATOM   971  O  OE1   . GLU A 1 125 ? 106.544 154.151 136.683 1.00 64.14  ? 127 GLU B OE1   1 
ATOM   972  O  OE2   . GLU A 1 125 ? 107.992 152.875 137.729 1.00 64.99  ? 127 GLU B OE2   1 
ATOM   973  N  N     . SER A 1 126 ? 108.241 159.287 137.645 1.00 59.87  ? 128 SER B N     1 
ATOM   974  C  CA    . SER A 1 126 ? 107.962 160.581 137.043 1.00 60.65  ? 128 SER B CA    1 
ATOM   975  C  C     . SER A 1 126 ? 109.011 160.981 136.017 1.00 59.54  ? 128 SER B C     1 
ATOM   976  O  O     . SER A 1 126 ? 109.033 162.137 135.586 1.00 59.52  ? 128 SER B O     1 
ATOM   977  C  CB    . SER A 1 126 ? 107.859 161.656 138.126 1.00 61.39  ? 128 SER B CB    1 
ATOM   978  O  OG    . SER A 1 126 ? 107.706 162.942 137.552 1.00 62.85  ? 128 SER B OG    1 
ATOM   979  N  N     . CYS A 1 127 ? 109.881 160.057 135.630 1.00 64.57  ? 129 CYS B N     1 
ATOM   980  C  CA    . CYS A 1 127 ? 110.931 160.316 134.660 1.00 62.48  ? 129 CYS B CA    1 
ATOM   981  C  C     . CYS A 1 127 ? 110.496 159.837 133.283 1.00 63.32  ? 129 CYS B C     1 
ATOM   982  O  O     . CYS A 1 127 ? 109.904 158.764 133.146 1.00 64.35  ? 129 CYS B O     1 
ATOM   983  C  CB    . CYS A 1 127 ? 112.231 159.624 135.070 1.00 63.29  ? 129 CYS B CB    1 
ATOM   984  S  SG    . CYS A 1 127 ? 112.958 160.249 136.595 1.00 77.34  ? 129 CYS B SG    1 
ATOM   985  N  N     . ASP A 1 128 ? 110.784 160.648 132.265 1.00 68.68  ? 130 ASP B N     1 
ATOM   986  C  CA    . ASP A 1 128 ? 110.464 160.256 130.898 1.00 68.24  ? 130 ASP B CA    1 
ATOM   987  C  C     . ASP A 1 128 ? 111.372 159.130 130.418 1.00 68.48  ? 130 ASP B C     1 
ATOM   988  O  O     . ASP A 1 128 ? 110.917 158.215 129.723 1.00 70.03  ? 130 ASP B O     1 
ATOM   989  C  CB    . ASP A 1 128 ? 110.563 161.464 129.969 1.00 71.08  ? 130 ASP B CB    1 
ATOM   990  C  CG    . ASP A 1 128 ? 109.933 161.209 128.615 1.00 76.36  ? 130 ASP B CG    1 
ATOM   991  O  OD1   . ASP A 1 128 ? 109.158 160.237 128.491 1.00 75.71  ? 130 ASP B OD1   1 
ATOM   992  O  OD2   . ASP A 1 128 ? 110.213 161.981 127.674 1.00 75.15  ? 130 ASP B OD2   1 
ATOM   993  N  N     . CYS A 1 129 ? 112.655 159.175 130.776 1.00 63.02  ? 131 CYS B N     1 
ATOM   994  C  CA    . CYS A 1 129 ? 113.589 158.118 130.394 1.00 62.52  ? 131 CYS B CA    1 
ATOM   995  C  C     . CYS A 1 129 ? 114.707 158.081 131.432 1.00 67.57  ? 131 CYS B C     1 
ATOM   996  O  O     . CYS A 1 129 ? 115.587 158.944 131.429 1.00 71.54  ? 131 CYS B O     1 
ATOM   997  C  CB    . CYS A 1 129 ? 114.138 158.347 128.994 1.00 67.75  ? 131 CYS B CB    1 
ATOM   998  S  SG    . CYS A 1 129 ? 115.431 157.188 128.514 1.00 81.93  ? 131 CYS B SG    1 
ATOM   999  N  N     . LEU A 1 130 ? 114.709 157.121 132.306 1.00 60.20  ? 132 LEU B N     1 
ATOM   1000 C  CA    . LEU A 1 130 ? 115.696 157.056 133.415 1.00 56.35  ? 132 LEU B CA    1 
ATOM   1001 C  C     . LEU A 1 130 ? 117.023 156.552 132.880 1.00 57.60  ? 132 LEU B C     1 
ATOM   1002 O  O     . LEU A 1 130 ? 117.019 155.662 132.017 1.00 59.61  ? 132 LEU B O     1 
ATOM   1003 C  CB    . LEU A 1 130 ? 115.193 156.184 134.568 1.00 55.67  ? 132 LEU B CB    1 
ATOM   1004 C  CG    . LEU A 1 130 ? 116.019 156.191 135.855 1.00 55.55  ? 132 LEU B CG    1 
ATOM   1005 C  CD1   . LEU A 1 130 ? 115.963 157.552 136.509 1.00 57.18  ? 132 LEU B CD1   1 
ATOM   1006 C  CD2   . LEU A 1 130 ? 115.480 155.134 136.789 1.00 57.70  ? 132 LEU B CD2   1 
ATOM   1007 N  N     . GLN A 1 131 ? 118.086 157.058 133.360 1.00 47.54  ? 133 GLN B N     1 
ATOM   1008 C  CA    . GLN A 1 131 ? 119.449 156.738 132.968 1.00 45.51  ? 133 GLN B CA    1 
ATOM   1009 C  C     . GLN A 1 131 ? 120.213 155.995 134.047 1.00 52.80  ? 133 GLN B C     1 
ATOM   1010 O  O     . GLN A 1 131 ? 120.957 155.063 133.737 1.00 61.64  ? 133 GLN B O     1 
ATOM   1011 C  CB    . GLN A 1 131 ? 120.201 158.020 132.592 1.00 51.03  ? 133 GLN B CB    1 
ATOM   1012 C  CG    . GLN A 1 131 ? 121.707 157.886 132.557 1.00 54.28  ? 133 GLN B CG    1 
ATOM   1013 C  CD    . GLN A 1 131 ? 122.191 157.028 131.415 1.00 57.94  ? 133 GLN B CD    1 
ATOM   1014 O  OE1   . GLN A 1 131 ? 122.378 157.509 130.301 1.00 58.36  ? 133 GLN B OE1   1 
ATOM   1015 N  NE2   . GLN A 1 131 ? 122.401 155.745 131.685 1.00 61.56  ? 133 GLN B NE2   1 
ATOM   1016 N  N     . GLY A 1 132 ? 120.044 156.373 135.306 1.00 48.75  ? 134 GLY B N     1 
ATOM   1017 C  CA    . GLY A 1 132 ? 120.755 155.701 136.370 1.00 47.59  ? 134 GLY B CA    1 
ATOM   1018 C  C     . GLY A 1 132 ? 120.523 156.383 137.697 1.00 46.16  ? 134 GLY B C     1 
ATOM   1019 O  O     . GLY A 1 132 ? 119.681 157.271 137.823 1.00 50.18  ? 134 GLY B O     1 
ATOM   1020 N  N     . PHE A 1 133 ? 121.296 155.952 138.690 1.00 43.84  ? 135 PHE B N     1 
ATOM   1021 C  CA    . PHE A 1 133 ? 121.187 156.447 140.050 1.00 38.08  ? 135 PHE B CA    1 
ATOM   1022 C  C     . PHE A 1 133 ? 122.542 156.926 140.541 1.00 40.98  ? 135 PHE B C     1 
ATOM   1023 O  O     . PHE A 1 133 ? 123.585 156.431 140.114 1.00 51.04  ? 135 PHE B O     1 
ATOM   1024 C  CB    . PHE A 1 133 ? 120.665 155.372 141.000 1.00 37.63  ? 135 PHE B CB    1 
ATOM   1025 C  CG    . PHE A 1 133 ? 119.338 154.818 140.615 1.00 38.44  ? 135 PHE B CG    1 
ATOM   1026 C  CD1   . PHE A 1 133 ? 119.247 153.786 139.707 1.00 44.68  ? 135 PHE B CD1   1 
ATOM   1027 C  CD2   . PHE A 1 133 ? 118.181 155.320 141.159 1.00 43.95  ? 135 PHE B CD2   1 
ATOM   1028 C  CE1   . PHE A 1 133 ? 118.030 153.274 139.352 1.00 45.97  ? 135 PHE B CE1   1 
ATOM   1029 C  CE2   . PHE A 1 133 ? 116.964 154.811 140.802 1.00 44.19  ? 135 PHE B CE2   1 
ATOM   1030 C  CZ    . PHE A 1 133 ? 116.889 153.786 139.899 1.00 42.53  ? 135 PHE B CZ    1 
ATOM   1031 N  N     . GLN A 1 134 ? 122.515 157.891 141.451 1.00 43.86  ? 136 GLN B N     1 
ATOM   1032 C  CA    . GLN A 1 134 ? 123.706 158.386 142.121 1.00 33.42  ? 136 GLN B CA    1 
ATOM   1033 C  C     . GLN A 1 134 ? 123.551 158.209 143.622 1.00 45.87  ? 136 GLN B C     1 
ATOM   1034 O  O     . GLN A 1 134 ? 122.474 158.451 144.176 1.00 55.85  ? 136 GLN B O     1 
ATOM   1035 C  CB    . GLN A 1 134 ? 123.945 159.855 141.811 1.00 36.53  ? 136 GLN B CB    1 
ATOM   1036 C  CG    . GLN A 1 134 ? 124.722 160.110 140.553 1.00 43.85  ? 136 GLN B CG    1 
ATOM   1037 C  CD    . GLN A 1 134 ? 125.052 161.572 140.376 1.00 57.31  ? 136 GLN B CD    1 
ATOM   1038 O  OE1   . GLN A 1 134 ? 124.545 162.424 141.101 1.00 57.57  ? 136 GLN B OE1   1 
ATOM   1039 N  NE2   . GLN A 1 134 ? 125.908 161.873 139.407 1.00 56.00  ? 136 GLN B NE2   1 
ATOM   1040 N  N     . LEU A 1 135 ? 124.626 157.792 144.281 1.00 37.00  ? 137 LEU B N     1 
ATOM   1041 C  CA    . LEU A 1 135 ? 124.645 157.665 145.730 1.00 34.54  ? 137 LEU B CA    1 
ATOM   1042 C  C     . LEU A 1 135 ? 125.923 158.283 146.265 1.00 36.93  ? 137 LEU B C     1 
ATOM   1043 O  O     . LEU A 1 135 ? 127.011 158.003 145.756 1.00 49.16  ? 137 LEU B O     1 
ATOM   1044 C  CB    . LEU A 1 135 ? 124.545 156.204 146.164 1.00 40.33  ? 137 LEU B CB    1 
ATOM   1045 C  CG    . LEU A 1 135 ? 124.548 155.952 147.671 1.00 44.48  ? 137 LEU B CG    1 
ATOM   1046 C  CD1   . LEU A 1 135 ? 123.249 156.407 148.302 1.00 45.10  ? 137 LEU B CD1   1 
ATOM   1047 C  CD2   . LEU A 1 135 ? 124.798 154.488 147.968 1.00 45.45  ? 137 LEU B CD2   1 
ATOM   1048 N  N     . THR A 1 136 ? 125.791 159.122 147.288 1.00 36.61  ? 138 THR B N     1 
ATOM   1049 C  CA    . THR A 1 136 ? 126.928 159.715 147.981 1.00 35.37  ? 138 THR B CA    1 
ATOM   1050 C  C     . THR A 1 136 ? 126.911 159.240 149.425 1.00 37.56  ? 138 THR B C     1 
ATOM   1051 O  O     . THR A 1 136 ? 125.910 159.418 150.125 1.00 45.90  ? 138 THR B O     1 
ATOM   1052 C  CB    . THR A 1 136 ? 126.879 161.240 147.922 1.00 43.01  ? 138 THR B CB    1 
ATOM   1053 O  OG1   . THR A 1 136 ? 126.711 161.661 146.566 1.00 48.47  ? 138 THR B OG1   1 
ATOM   1054 C  CG2   . THR A 1 136 ? 128.168 161.824 148.458 1.00 48.12  ? 138 THR B CG2   1 
ATOM   1055 N  N     . HIS A 1 137 ? 128.014 158.650 149.874 1.00 34.78  ? 139 HIS B N     1 
ATOM   1056 C  CA    . HIS A 1 137 ? 128.069 158.081 151.213 1.00 36.15  ? 139 HIS B CA    1 
ATOM   1057 C  C     . HIS A 1 137 ? 129.525 157.886 151.612 1.00 40.37  ? 139 HIS B C     1 
ATOM   1058 O  O     . HIS A 1 137 ? 130.446 158.240 150.873 1.00 48.17  ? 139 HIS B O     1 
ATOM   1059 C  CB    . HIS A 1 137 ? 127.288 156.767 151.274 1.00 37.73  ? 139 HIS B CB    1 
ATOM   1060 C  CG    . HIS A 1 137 ? 127.935 155.645 150.529 1.00 35.17  ? 139 HIS B CG    1 
ATOM   1061 N  ND1   . HIS A 1 137 ? 128.192 155.701 149.178 1.00 42.26  ? 139 HIS B ND1   1 
ATOM   1062 C  CD2   . HIS A 1 137 ? 128.363 154.429 150.942 1.00 41.03  ? 139 HIS B CD2   1 
ATOM   1063 C  CE1   . HIS A 1 137 ? 128.766 154.576 148.793 1.00 42.43  ? 139 HIS B CE1   1 
ATOM   1064 N  NE2   . HIS A 1 137 ? 128.877 153.786 149.844 1.00 40.09  ? 139 HIS B NE2   1 
ATOM   1065 N  N     . SER A 1 138 ? 129.724 157.318 152.798 1.00 45.79  ? 140 SER B N     1 
ATOM   1066 C  CA    . SER A 1 138 ? 131.043 156.998 153.319 1.00 41.05  ? 140 SER B CA    1 
ATOM   1067 C  C     . SER A 1 138 ? 131.063 155.551 153.786 1.00 49.07  ? 140 SER B C     1 
ATOM   1068 O  O     . SER A 1 138 ? 130.124 155.088 154.438 1.00 61.95  ? 140 SER B O     1 
ATOM   1069 C  CB    . SER A 1 138 ? 131.426 157.923 154.469 1.00 44.52  ? 140 SER B CB    1 
ATOM   1070 O  OG    . SER A 1 138 ? 130.506 157.809 155.537 1.00 53.25  ? 140 SER B OG    1 
ATOM   1071 N  N     . LEU A 1 139 ? 132.140 154.841 153.451 1.00 37.37  ? 141 LEU B N     1 
ATOM   1072 C  CA    . LEU A 1 139 ? 132.247 153.429 153.801 1.00 40.05  ? 141 LEU B CA    1 
ATOM   1073 C  C     . LEU A 1 139 ? 132.575 153.209 155.271 1.00 42.55  ? 141 LEU B C     1 
ATOM   1074 O  O     . LEU A 1 139 ? 132.224 152.164 155.826 1.00 51.77  ? 141 LEU B O     1 
ATOM   1075 C  CB    . LEU A 1 139 ? 133.313 152.747 152.943 1.00 41.90  ? 141 LEU B CB    1 
ATOM   1076 C  CG    . LEU A 1 139 ? 133.129 152.710 151.431 1.00 41.28  ? 141 LEU B CG    1 
ATOM   1077 C  CD1   . LEU A 1 139 ? 134.006 151.644 150.817 1.00 46.00  ? 141 LEU B CD1   1 
ATOM   1078 C  CD2   . LEU A 1 139 ? 131.681 152.471 151.079 1.00 48.33  ? 141 LEU B CD2   1 
ATOM   1079 N  N     . GLY A 1 140 ? 133.242 154.161 155.914 1.00 43.20  ? 142 GLY B N     1 
ATOM   1080 C  CA    . GLY A 1 140 ? 133.764 153.947 157.249 1.00 43.95  ? 142 GLY B CA    1 
ATOM   1081 C  C     . GLY A 1 140 ? 132.789 154.138 158.386 1.00 41.49  ? 142 GLY B C     1 
ATOM   1082 O  O     . GLY A 1 140 ? 133.106 153.756 159.514 1.00 52.33  ? 142 GLY B O     1 
ATOM   1083 N  N     . GLY A 1 141 ? 131.622 154.721 158.132 1.00 40.64  ? 143 GLY B N     1 
ATOM   1084 C  CA    . GLY A 1 141 ? 130.620 154.913 159.158 1.00 46.11  ? 143 GLY B CA    1 
ATOM   1085 C  C     . GLY A 1 141 ? 129.605 153.786 159.201 1.00 49.58  ? 143 GLY B C     1 
ATOM   1086 O  O     . GLY A 1 141 ? 129.738 152.755 158.540 1.00 55.63  ? 143 GLY B O     1 
ATOM   1087 N  N     . GLY A 1 142 ? 128.563 154.002 159.997 1.00 49.48  ? 144 GLY B N     1 
ATOM   1088 C  CA    . GLY A 1 142 ? 127.518 153.011 160.152 1.00 45.43  ? 144 GLY B CA    1 
ATOM   1089 C  C     . GLY A 1 142 ? 126.329 153.172 159.226 1.00 51.21  ? 144 GLY B C     1 
ATOM   1090 O  O     . GLY A 1 142 ? 125.969 152.232 158.514 1.00 56.23  ? 144 GLY B O     1 
ATOM   1091 N  N     . THR A 1 143 ? 125.703 154.351 159.227 1.00 52.51  ? 145 THR B N     1 
ATOM   1092 C  CA    . THR A 1 143 ? 124.501 154.537 158.421 1.00 45.23  ? 145 THR B CA    1 
ATOM   1093 C  C     . THR A 1 143 ? 124.831 154.593 156.940 1.00 41.02  ? 145 THR B C     1 
ATOM   1094 O  O     . THR A 1 143 ? 124.174 153.930 156.129 1.00 53.22  ? 145 THR B O     1 
ATOM   1095 C  CB    . THR A 1 143 ? 123.752 155.798 158.849 1.00 49.06  ? 145 THR B CB    1 
ATOM   1096 O  OG1   . THR A 1 143 ? 122.482 155.840 158.192 1.00 46.15  ? 145 THR B OG1   1 
ATOM   1097 C  CG2   . THR A 1 143 ? 124.534 157.037 158.496 1.00 50.86  ? 145 THR B CG2   1 
ATOM   1098 N  N     . GLY A 1 144 ? 125.860 155.349 156.574 1.00 41.70  ? 146 GLY B N     1 
ATOM   1099 C  CA    . GLY A 1 144 ? 126.290 155.432 155.197 1.00 41.57  ? 146 GLY B CA    1 
ATOM   1100 C  C     . GLY A 1 144 ? 126.560 154.070 154.609 1.00 50.78  ? 146 GLY B C     1 
ATOM   1101 O  O     . GLY A 1 144 ? 125.844 153.632 153.711 1.00 59.96  ? 146 GLY B O     1 
ATOM   1102 N  N     . SER A 1 145 ? 127.543 153.362 155.155 1.00 48.18  ? 147 SER B N     1 
ATOM   1103 C  CA    . SER A 1 145 ? 127.941 152.065 154.629 1.00 45.15  ? 147 SER B CA    1 
ATOM   1104 C  C     . SER A 1 145 ? 126.781 151.080 154.554 1.00 46.37  ? 147 SER B C     1 
ATOM   1105 O  O     . SER A 1 145 ? 126.363 150.694 153.455 1.00 54.62  ? 147 SER B O     1 
ATOM   1106 C  CB    . SER A 1 145 ? 129.059 151.484 155.489 1.00 47.12  ? 147 SER B CB    1 
ATOM   1107 O  OG    . SER A 1 145 ? 129.419 150.195 155.039 1.00 54.61  ? 147 SER B OG    1 
ATOM   1108 N  N     . GLY A 1 146 ? 126.235 150.697 155.708 1.00 36.75  ? 148 GLY B N     1 
ATOM   1109 C  CA    . GLY A 1 146 ? 125.227 149.649 155.724 1.00 39.86  ? 148 GLY B CA    1 
ATOM   1110 C  C     . GLY A 1 146 ? 123.959 150.034 154.989 1.00 48.33  ? 148 GLY B C     1 
ATOM   1111 O  O     . GLY A 1 146 ? 123.440 149.266 154.171 1.00 57.04  ? 148 GLY B O     1 
ATOM   1112 N  N     . MET A 1 147 ? 123.443 151.234 155.262 1.00 45.23  ? 149 MET B N     1 
ATOM   1113 C  CA    . MET A 1 147 ? 122.172 151.620 154.668 1.00 42.20  ? 149 MET B CA    1 
ATOM   1114 C  C     . MET A 1 147 ? 122.304 151.848 153.167 1.00 50.62  ? 149 MET B C     1 
ATOM   1115 O  O     . MET A 1 147 ? 121.423 151.444 152.401 1.00 56.90  ? 149 MET B O     1 
ATOM   1116 C  CB    . MET A 1 147 ? 121.623 152.861 155.361 1.00 42.69  ? 149 MET B CB    1 
ATOM   1117 C  CG    . MET A 1 147 ? 120.348 153.386 154.744 1.00 54.27  ? 149 MET B CG    1 
ATOM   1118 S  SD    . MET A 1 147 ? 119.044 153.635 155.952 1.00 72.13  ? 149 MET B SD    1 
ATOM   1119 C  CE    . MET A 1 147 ? 119.646 155.099 156.783 1.00 61.13  ? 149 MET B CE    1 
ATOM   1120 N  N     . GLY A 1 148 ? 123.387 152.490 152.718 1.00 46.14  ? 150 GLY B N     1 
ATOM   1121 C  CA    . GLY A 1 148 ? 123.583 152.659 151.294 1.00 46.68  ? 150 GLY B CA    1 
ATOM   1122 C  C     . GLY A 1 148 ? 123.780 151.341 150.576 1.00 51.52  ? 150 GLY B C     1 
ATOM   1123 O  O     . GLY A 1 148 ? 123.306 151.162 149.455 1.00 56.94  ? 150 GLY B O     1 
ATOM   1124 N  N     . THR A 1 149 ? 124.474 150.394 151.212 1.00 45.01  ? 151 THR B N     1 
ATOM   1125 C  CA    . THR A 1 149 ? 124.626 149.072 150.618 1.00 45.77  ? 151 THR B CA    1 
ATOM   1126 C  C     . THR A 1 149 ? 123.277 148.375 150.467 1.00 53.63  ? 151 THR B C     1 
ATOM   1127 O  O     . THR A 1 149 ? 122.974 147.794 149.415 1.00 61.57  ? 151 THR B O     1 
ATOM   1128 C  CB    . THR A 1 149 ? 125.583 148.240 151.471 1.00 51.36  ? 151 THR B CB    1 
ATOM   1129 O  OG1   . THR A 1 149 ? 126.929 148.477 151.046 1.00 53.36  ? 151 THR B OG1   1 
ATOM   1130 C  CG2   . THR A 1 149 ? 125.266 146.760 151.357 1.00 56.92  ? 151 THR B CG2   1 
ATOM   1131 N  N     . LEU A 1 150 ? 122.442 148.438 151.508 1.00 45.35  ? 152 LEU B N     1 
ATOM   1132 C  CA    . LEU A 1 150 ? 121.118 147.829 151.427 1.00 42.71  ? 152 LEU B CA    1 
ATOM   1133 C  C     . LEU A 1 150 ? 120.266 148.490 150.347 1.00 50.04  ? 152 LEU B C     1 
ATOM   1134 O  O     . LEU A 1 150 ? 119.565 147.807 149.586 1.00 58.33  ? 152 LEU B O     1 
ATOM   1135 C  CB    . LEU A 1 150 ? 120.428 147.910 152.785 1.00 46.14  ? 152 LEU B CB    1 
ATOM   1136 C  CG    . LEU A 1 150 ? 119.169 147.075 152.978 1.00 49.43  ? 152 LEU B CG    1 
ATOM   1137 C  CD1   . LEU A 1 150 ? 119.502 145.603 152.927 1.00 50.12  ? 152 LEU B CD1   1 
ATOM   1138 C  CD2   . LEU A 1 150 ? 118.522 147.426 154.291 1.00 50.70  ? 152 LEU B CD2   1 
ATOM   1139 N  N     . LEU A 1 151 ? 120.320 149.820 150.262 1.00 50.53  ? 153 LEU B N     1 
ATOM   1140 C  CA    . LEU A 1 151 ? 119.581 150.537 149.229 1.00 46.43  ? 153 LEU B CA    1 
ATOM   1141 C  C     . LEU A 1 151 ? 120.064 150.161 147.837 1.00 53.89  ? 153 LEU B C     1 
ATOM   1142 O  O     . LEU A 1 151 ? 119.256 150.000 146.916 1.00 61.61  ? 153 LEU B O     1 
ATOM   1143 C  CB    . LEU A 1 151 ? 119.714 152.041 149.443 1.00 48.70  ? 153 LEU B CB    1 
ATOM   1144 C  CG    . LEU A 1 151 ? 118.693 152.710 150.350 1.00 56.65  ? 153 LEU B CG    1 
ATOM   1145 C  CD1   . LEU A 1 151 ? 119.059 154.161 150.537 1.00 57.76  ? 153 LEU B CD1   1 
ATOM   1146 C  CD2   . LEU A 1 151 ? 117.323 152.584 149.734 1.00 56.06  ? 153 LEU B CD2   1 
ATOM   1147 N  N     . ILE A 1 152 ? 121.380 150.034 147.659 1.00 55.95  ? 154 ILE B N     1 
ATOM   1148 C  CA    . ILE A 1 152 ? 121.925 149.653 146.362 1.00 50.12  ? 154 ILE B CA    1 
ATOM   1149 C  C     . ILE A 1 152 ? 121.429 148.272 145.973 1.00 54.35  ? 154 ILE B C     1 
ATOM   1150 O  O     . ILE A 1 152 ? 121.042 148.037 144.823 1.00 64.41  ? 154 ILE B O     1 
ATOM   1151 C  CB    . ILE A 1 152 ? 123.461 149.718 146.389 1.00 48.90  ? 154 ILE B CB    1 
ATOM   1152 C  CG1   . ILE A 1 152 ? 123.935 151.159 146.266 1.00 55.08  ? 154 ILE B CG1   1 
ATOM   1153 C  CG2   . ILE A 1 152 ? 124.051 148.896 145.270 1.00 55.32  ? 154 ILE B CG2   1 
ATOM   1154 C  CD1   . ILE A 1 152 ? 125.427 151.297 146.258 1.00 57.62  ? 154 ILE B CD1   1 
ATOM   1155 N  N     . SER A 1 153 ? 121.422 147.341 146.926 1.00 43.01  ? 155 SER B N     1 
ATOM   1156 C  CA    . SER A 1 153 ? 120.929 146.000 146.636 1.00 42.41  ? 155 SER B CA    1 
ATOM   1157 C  C     . SER A 1 153 ? 119.464 146.029 146.215 1.00 48.40  ? 155 SER B C     1 
ATOM   1158 O  O     . SER A 1 153 ? 119.082 145.418 145.207 1.00 55.16  ? 155 SER B O     1 
ATOM   1159 C  CB    . SER A 1 153 ? 121.128 145.103 147.855 1.00 47.70  ? 155 SER B CB    1 
ATOM   1160 O  OG    . SER A 1 153 ? 120.597 143.810 147.629 1.00 53.82  ? 155 SER B OG    1 
ATOM   1161 N  N     . LYS A 1 154 ? 118.627 146.746 146.969 1.00 43.16  ? 156 LYS B N     1 
ATOM   1162 C  CA    . LYS A 1 154 ? 117.203 146.794 146.642 1.00 43.34  ? 156 LYS B CA    1 
ATOM   1163 C  C     . LYS A 1 154 ? 116.966 147.431 145.277 1.00 47.10  ? 156 LYS B C     1 
ATOM   1164 O  O     . LYS A 1 154 ? 116.178 146.921 144.468 1.00 57.45  ? 156 LYS B O     1 
ATOM   1165 C  CB    . LYS A 1 154 ? 116.441 147.558 147.723 1.00 46.70  ? 156 LYS B CB    1 
ATOM   1166 C  CG    . LYS A 1 154 ? 116.455 146.906 149.092 1.00 46.52  ? 156 LYS B CG    1 
ATOM   1167 C  CD    . LYS A 1 154 ? 115.881 145.509 149.054 1.00 44.53  ? 156 LYS B CD    1 
ATOM   1168 C  CE    . LYS A 1 154 ? 115.763 144.933 150.447 1.00 45.77  ? 156 LYS B CE    1 
ATOM   1169 N  NZ    . LYS A 1 154 ? 114.771 145.685 151.253 1.00 52.69  ? 156 LYS B NZ    1 
ATOM   1170 N  N     . ILE A 1 155 ? 117.656 148.537 144.996 1.00 44.14  ? 157 ILE B N     1 
ATOM   1171 C  CA    . ILE A 1 155 ? 117.471 149.240 143.733 1.00 43.06  ? 157 ILE B CA    1 
ATOM   1172 C  C     . ILE A 1 155 ? 117.959 148.391 142.566 1.00 49.86  ? 157 ILE B C     1 
ATOM   1173 O  O     . ILE A 1 155 ? 117.326 148.356 141.505 1.00 53.16  ? 157 ILE B O     1 
ATOM   1174 C  CB    . ILE A 1 155 ? 118.177 150.604 143.784 1.00 43.92  ? 157 ILE B CB    1 
ATOM   1175 C  CG1   . ILE A 1 155 ? 117.426 151.553 144.714 1.00 50.39  ? 157 ILE B CG1   1 
ATOM   1176 C  CG2   . ILE A 1 155 ? 118.280 151.205 142.401 1.00 51.72  ? 157 ILE B CG2   1 
ATOM   1177 C  CD1   . ILE A 1 155 ? 118.169 152.826 145.012 1.00 51.07  ? 157 ILE B CD1   1 
ATOM   1178 N  N     . ARG A 1 156 ? 119.084 147.694 142.734 1.00 54.03  ? 158 ARG B N     1 
ATOM   1179 C  CA    . ARG A 1 156 ? 119.569 146.833 141.663 1.00 46.74  ? 158 ARG B CA    1 
ATOM   1180 C  C     . ARG A 1 156 ? 118.611 145.681 141.408 1.00 51.24  ? 158 ARG B C     1 
ATOM   1181 O  O     . ARG A 1 156 ? 118.431 145.261 140.260 1.00 59.51  ? 158 ARG B O     1 
ATOM   1182 C  CB    . ARG A 1 156 ? 120.961 146.306 141.989 1.00 51.23  ? 158 ARG B CB    1 
ATOM   1183 C  CG    . ARG A 1 156 ? 121.643 145.641 140.816 1.00 54.49  ? 158 ARG B CG    1 
ATOM   1184 C  CD    . ARG A 1 156 ? 122.122 146.662 139.814 1.00 53.14  ? 158 ARG B CD    1 
ATOM   1185 N  NE    . ARG A 1 156 ? 123.328 146.227 139.125 1.00 52.90  ? 158 ARG B NE    1 
ATOM   1186 C  CZ    . ARG A 1 156 ? 123.910 146.903 138.146 1.00 57.81  ? 158 ARG B CZ    1 
ATOM   1187 N  NH1   . ARG A 1 156 ? 123.420 148.053 137.716 1.00 57.19  ? 158 ARG B NH1   1 
ATOM   1188 N  NH2   . ARG A 1 156 ? 125.010 146.413 137.583 1.00 58.21  ? 158 ARG B NH2   1 
ATOM   1189 N  N     . GLU A 1 157 ? 117.996 145.147 142.462 1.00 54.05  ? 159 GLU B N     1 
ATOM   1190 C  CA    . GLU A 1 157 ? 116.981 144.122 142.260 1.00 53.75  ? 159 GLU B CA    1 
ATOM   1191 C  C     . GLU A 1 157 ? 115.789 144.672 141.486 1.00 58.02  ? 159 GLU B C     1 
ATOM   1192 O  O     . GLU A 1 157 ? 115.265 144.005 140.586 1.00 62.37  ? 159 GLU B O     1 
ATOM   1193 C  CB    . GLU A 1 157 ? 116.538 143.551 143.605 1.00 58.04  ? 159 GLU B CB    1 
ATOM   1194 C  CG    . GLU A 1 157 ? 115.317 142.656 143.527 1.00 64.38  ? 159 GLU B CG    1 
ATOM   1195 C  CD    . GLU A 1 157 ? 115.612 141.319 142.875 1.00 69.75  ? 159 GLU B CD    1 
ATOM   1196 O  OE1   . GLU A 1 157 ? 116.770 140.856 142.957 1.00 66.92  ? 159 GLU B OE1   1 
ATOM   1197 O  OE2   . GLU A 1 157 ? 114.686 140.730 142.279 1.00 65.50  ? 159 GLU B OE2   1 
ATOM   1198 N  N     . GLU A 1 158 ? 115.345 145.889 141.814 1.00 61.04  ? 160 GLU B N     1 
ATOM   1199 C  CA    . GLU A 1 158 ? 114.176 146.448 141.135 1.00 55.70  ? 160 GLU B CA    1 
ATOM   1200 C  C     . GLU A 1 158 ? 114.487 146.839 139.693 1.00 57.35  ? 160 GLU B C     1 
ATOM   1201 O  O     . GLU A 1 158 ? 113.748 146.476 138.772 1.00 62.71  ? 160 GLU B O     1 
ATOM   1202 C  CB    . GLU A 1 158 ? 113.641 147.648 141.908 1.00 52.90  ? 160 GLU B CB    1 
ATOM   1203 C  CG    . GLU A 1 158 ? 112.626 147.288 142.968 1.00 58.84  ? 160 GLU B CG    1 
ATOM   1204 C  CD    . GLU A 1 158 ? 111.952 148.506 143.564 1.00 67.52  ? 160 GLU B CD    1 
ATOM   1205 O  OE1   . GLU A 1 158 ? 112.433 149.633 143.320 1.00 70.12  ? 160 GLU B OE1   1 
ATOM   1206 O  OE2   . GLU A 1 158 ? 110.941 148.338 144.278 1.00 66.14  ? 160 GLU B OE2   1 
ATOM   1207 N  N     . TYR A 1 159 ? 115.568 147.582 139.474 1.00 57.21  ? 161 TYR B N     1 
ATOM   1208 C  CA    . TYR A 1 159 ? 115.950 148.038 138.136 1.00 56.95  ? 161 TYR B CA    1 
ATOM   1209 C  C     . TYR A 1 159 ? 117.303 147.448 137.773 1.00 60.78  ? 161 TYR B C     1 
ATOM   1210 O  O     . TYR A 1 159 ? 118.346 147.985 138.186 1.00 65.69  ? 161 TYR B O     1 
ATOM   1211 C  CB    . TYR A 1 159 ? 116.012 149.563 138.064 1.00 56.64  ? 161 TYR B CB    1 
ATOM   1212 C  CG    . TYR A 1 159 ? 114.823 150.288 138.643 1.00 56.85  ? 161 TYR B CG    1 
ATOM   1213 C  CD1   . TYR A 1 159 ? 114.809 150.680 139.968 1.00 60.54  ? 161 TYR B CD1   1 
ATOM   1214 C  CD2   . TYR A 1 159 ? 113.726 150.593 137.863 1.00 57.70  ? 161 TYR B CD2   1 
ATOM   1215 C  CE1   . TYR A 1 159 ? 113.733 151.348 140.500 1.00 59.09  ? 161 TYR B CE1   1 
ATOM   1216 C  CE2   . TYR A 1 159 ? 112.646 151.261 138.387 1.00 59.36  ? 161 TYR B CE2   1 
ATOM   1217 C  CZ    . TYR A 1 159 ? 112.655 151.633 139.707 1.00 59.80  ? 161 TYR B CZ    1 
ATOM   1218 O  OH    . TYR A 1 159 ? 111.578 152.301 140.237 1.00 63.01  ? 161 TYR B OH    1 
ATOM   1219 N  N     . PRO A 1 160 ? 117.352 146.362 137.004 1.00 59.44  ? 162 PRO B N     1 
ATOM   1220 C  CA    . PRO A 1 160 ? 118.634 145.723 136.689 1.00 59.81  ? 162 PRO B CA    1 
ATOM   1221 C  C     . PRO A 1 160 ? 119.318 146.205 135.419 1.00 59.94  ? 162 PRO B C     1 
ATOM   1222 O  O     . PRO A 1 160 ? 120.413 145.720 135.119 1.00 65.04  ? 162 PRO B O     1 
ATOM   1223 C  CB    . PRO A 1 160 ? 118.238 144.247 136.556 1.00 59.81  ? 162 PRO B CB    1 
ATOM   1224 C  CG    . PRO A 1 160 ? 116.783 144.249 136.213 1.00 57.84  ? 162 PRO B CG    1 
ATOM   1225 C  CD    . PRO A 1 160 ? 116.213 145.611 136.458 1.00 58.85  ? 162 PRO B CD    1 
ATOM   1226 N  N     . ASP A 1 161 ? 118.732 147.135 134.675 1.00 57.19  ? 163 ASP B N     1 
ATOM   1227 C  CA    . ASP A 1 161 ? 119.284 147.587 133.405 1.00 57.11  ? 163 ASP B CA    1 
ATOM   1228 C  C     . ASP A 1 161 ? 119.604 149.074 133.445 1.00 67.00  ? 163 ASP B C     1 
ATOM   1229 O  O     . ASP A 1 161 ? 119.485 149.782 132.444 1.00 69.47  ? 163 ASP B O     1 
ATOM   1230 C  CB    . ASP A 1 161 ? 118.327 147.279 132.258 1.00 62.61  ? 163 ASP B CB    1 
ATOM   1231 C  CG    . ASP A 1 161 ? 116.970 147.917 132.450 1.00 69.30  ? 163 ASP B CG    1 
ATOM   1232 O  OD1   . ASP A 1 161 ? 116.551 148.081 133.615 1.00 69.65  ? 163 ASP B OD1   1 
ATOM   1233 O  OD2   . ASP A 1 161 ? 116.322 148.255 131.438 1.00 64.69  ? 163 ASP B OD2   1 
ATOM   1234 N  N     . ARG A 1 162 ? 120.022 149.563 134.607 1.00 61.31  ? 164 ARG B N     1 
ATOM   1235 C  CA    . ARG A 1 162 ? 120.296 150.974 134.813 1.00 51.62  ? 164 ARG B CA    1 
ATOM   1236 C  C     . ARG A 1 162 ? 121.680 151.138 135.419 1.00 55.84  ? 164 ARG B C     1 
ATOM   1237 O  O     . ARG A 1 162 ? 122.224 150.220 136.035 1.00 63.50  ? 164 ARG B O     1 
ATOM   1238 C  CB    . ARG A 1 162 ? 119.255 151.620 135.728 1.00 55.23  ? 164 ARG B CB    1 
ATOM   1239 C  CG    . ARG A 1 162 ? 117.848 151.578 135.191 1.00 55.66  ? 164 ARG B CG    1 
ATOM   1240 C  CD    . ARG A 1 162 ? 117.786 152.163 133.809 1.00 54.73  ? 164 ARG B CD    1 
ATOM   1241 N  NE    . ARG A 1 162 ? 116.428 152.172 133.285 1.00 61.03  ? 164 ARG B NE    1 
ATOM   1242 C  CZ    . ARG A 1 162 ? 116.121 152.439 132.024 1.00 66.63  ? 164 ARG B CZ    1 
ATOM   1243 N  NH1   . ARG A 1 162 ? 117.056 152.707 131.128 1.00 65.79  ? 164 ARG B NH1   1 
ATOM   1244 N  NH2   . ARG A 1 162 ? 114.844 152.436 131.653 1.00 67.22  ? 164 ARG B NH2   1 
ATOM   1245 N  N     . ILE A 1 163 ? 122.241 152.321 135.239 1.00 48.47  ? 165 ILE B N     1 
ATOM   1246 C  CA    . ILE A 1 163 ? 123.564 152.631 135.763 1.00 47.55  ? 165 ILE B CA    1 
ATOM   1247 C  C     . ILE A 1 163 ? 123.462 152.914 137.254 1.00 55.78  ? 165 ILE B C     1 
ATOM   1248 O  O     . ILE A 1 163 ? 122.518 153.560 137.719 1.00 61.78  ? 165 ILE B O     1 
ATOM   1249 C  CB    . ILE A 1 163 ? 124.174 153.820 135.001 1.00 53.34  ? 165 ILE B CB    1 
ATOM   1250 C  CG1   . ILE A 1 163 ? 124.545 153.407 133.580 1.00 51.48  ? 165 ILE B CG1   1 
ATOM   1251 C  CG2   . ILE A 1 163 ? 125.396 154.360 135.719 1.00 59.05  ? 165 ILE B CG2   1 
ATOM   1252 C  CD1   . ILE A 1 163 ? 125.573 152.315 133.516 1.00 55.13  ? 165 ILE B CD1   1 
ATOM   1253 N  N     . MET A 1 164 ? 124.432 152.416 138.017 1.00 59.38  ? 166 MET B N     1 
ATOM   1254 C  CA    . MET A 1 164 ? 124.550 152.703 139.444 1.00 53.05  ? 166 MET B CA    1 
ATOM   1255 C  C     . MET A 1 164 ? 125.978 153.168 139.696 1.00 55.50  ? 166 MET B C     1 
ATOM   1256 O  O     . MET A 1 164 ? 126.893 152.345 139.767 1.00 64.25  ? 166 MET B O     1 
ATOM   1257 C  CB    . MET A 1 164 ? 124.223 151.480 140.287 1.00 51.59  ? 166 MET B CB    1 
ATOM   1258 C  CG    . MET A 1 164 ? 122.776 151.054 140.250 1.00 57.89  ? 166 MET B CG    1 
ATOM   1259 S  SD    . MET A 1 164 ? 121.785 151.940 141.460 1.00 75.87  ? 166 MET B SD    1 
ATOM   1260 C  CE    . MET A 1 164 ? 122.859 151.855 142.882 1.00 60.36  ? 166 MET B CE    1 
ATOM   1261 N  N     . ASN A 1 165 ? 126.181 154.474 139.819 1.00 47.11  ? 167 ASN B N     1 
ATOM   1262 C  CA    . ASN A 1 165 ? 127.497 155.011 140.125 1.00 49.75  ? 167 ASN B CA    1 
ATOM   1263 C  C     . ASN A 1 165 ? 127.490 155.676 141.494 1.00 48.71  ? 167 ASN B C     1 
ATOM   1264 O  O     . ASN A 1 165 ? 126.561 156.413 141.834 1.00 58.63  ? 167 ASN B O     1 
ATOM   1265 C  CB    . ASN A 1 165 ? 127.975 155.992 139.049 1.00 47.43  ? 167 ASN B CB    1 
ATOM   1266 C  CG    . ASN A 1 165 ? 126.887 156.908 138.559 1.00 53.91  ? 167 ASN B CG    1 
ATOM   1267 O  OD1   . ASN A 1 165 ? 126.015 157.322 139.317 1.00 63.04  ? 167 ASN B OD1   1 
ATOM   1268 N  ND2   . ASN A 1 165 ? 126.935 157.239 137.276 1.00 58.38  ? 167 ASN B ND2   1 
ATOM   1269 N  N     . THR A 1 166 ? 128.524 155.393 142.280 1.00 36.88  ? 168 THR B N     1 
ATOM   1270 C  CA    . THR A 1 166 ? 128.627 155.850 143.656 1.00 36.46  ? 168 THR B CA    1 
ATOM   1271 C  C     . THR A 1 166 ? 129.918 156.626 143.854 1.00 41.69  ? 168 THR B C     1 
ATOM   1272 O  O     . THR A 1 166 ? 130.944 156.305 143.251 1.00 52.70  ? 168 THR B O     1 
ATOM   1273 C  CB    . THR A 1 166 ? 128.583 154.675 144.637 1.00 42.75  ? 168 THR B CB    1 
ATOM   1274 O  OG1   . THR A 1 166 ? 129.787 153.911 144.528 1.00 50.00  ? 168 THR B OG1   1 
ATOM   1275 C  CG2   . THR A 1 166 ? 127.403 153.778 144.344 1.00 48.93  ? 168 THR B CG2   1 
ATOM   1276 N  N     . PHE A 1 167 ? 129.853 157.650 144.691 1.00 42.18  ? 169 PHE B N     1 
ATOM   1277 C  CA    . PHE A 1 167 ? 131.011 158.433 145.101 1.00 40.18  ? 169 PHE B CA    1 
ATOM   1278 C  C     . PHE A 1 167 ? 131.231 158.118 146.575 1.00 44.67  ? 169 PHE B C     1 
ATOM   1279 O  O     . PHE A 1 167 ? 130.635 158.740 147.454 1.00 49.27  ? 169 PHE B O     1 
ATOM   1280 C  CB    . PHE A 1 167 ? 130.789 159.918 144.863 1.00 43.73  ? 169 PHE B CB    1 
ATOM   1281 C  CG    . PHE A 1 167 ? 130.633 160.284 143.418 1.00 49.86  ? 169 PHE B CG    1 
ATOM   1282 C  CD1   . PHE A 1 167 ? 129.437 160.069 142.760 1.00 50.07  ? 169 PHE B CD1   1 
ATOM   1283 C  CD2   . PHE A 1 167 ? 131.676 160.860 142.721 1.00 47.03  ? 169 PHE B CD2   1 
ATOM   1284 C  CE1   . PHE A 1 167 ? 129.290 160.405 141.435 1.00 45.05  ? 169 PHE B CE1   1 
ATOM   1285 C  CE2   . PHE A 1 167 ? 131.532 161.201 141.397 1.00 48.17  ? 169 PHE B CE2   1 
ATOM   1286 C  CZ    . PHE A 1 167 ? 130.336 160.973 140.755 1.00 42.92  ? 169 PHE B CZ    1 
ATOM   1287 N  N     . SER A 1 168 ? 132.091 157.145 146.841 1.00 45.53  ? 170 SER B N     1 
ATOM   1288 C  CA    . SER A 1 168 ? 132.279 156.618 148.182 1.00 48.59  ? 170 SER B CA    1 
ATOM   1289 C  C     . SER A 1 168 ? 133.584 157.133 148.766 1.00 47.65  ? 170 SER B C     1 
ATOM   1290 O  O     . SER A 1 168 ? 134.641 157.008 148.143 1.00 49.48  ? 170 SER B O     1 
ATOM   1291 C  CB    . SER A 1 168 ? 132.270 155.091 148.164 1.00 50.39  ? 170 SER B CB    1 
ATOM   1292 O  OG    . SER A 1 168 ? 133.100 154.598 147.132 1.00 53.78  ? 170 SER B OG    1 
ATOM   1293 N  N     . VAL A 1 169 ? 133.503 157.714 149.957 1.00 41.24  ? 171 VAL B N     1 
ATOM   1294 C  CA    . VAL A 1 169 ? 134.687 158.184 150.665 1.00 38.32  ? 171 VAL B CA    1 
ATOM   1295 C  C     . VAL A 1 169 ? 135.291 157.008 151.421 1.00 44.33  ? 171 VAL B C     1 
ATOM   1296 O  O     . VAL A 1 169 ? 134.650 156.427 152.301 1.00 54.18  ? 171 VAL B O     1 
ATOM   1297 C  CB    . VAL A 1 169 ? 134.344 159.338 151.614 1.00 39.13  ? 171 VAL B CB    1 
ATOM   1298 C  CG1   . VAL A 1 169 ? 135.538 159.688 152.471 1.00 37.13  ? 171 VAL B CG1   1 
ATOM   1299 C  CG2   . VAL A 1 169 ? 133.891 160.541 150.823 1.00 40.82  ? 171 VAL B CG2   1 
ATOM   1300 N  N     . VAL A 1 170 ? 136.525 156.659 151.080 1.00 46.73  ? 172 VAL B N     1 
ATOM   1301 C  CA    . VAL A 1 170 ? 137.164 155.434 151.550 1.00 39.91  ? 172 VAL B CA    1 
ATOM   1302 C  C     . VAL A 1 170 ? 138.061 155.749 152.741 1.00 43.66  ? 172 VAL B C     1 
ATOM   1303 O  O     . VAL A 1 170 ? 138.690 156.816 152.773 1.00 49.76  ? 172 VAL B O     1 
ATOM   1304 C  CB    . VAL A 1 170 ? 137.948 154.769 150.406 1.00 49.28  ? 172 VAL B CB    1 
ATOM   1305 C  CG1   . VAL A 1 170 ? 139.118 153.964 150.932 1.00 54.29  ? 172 VAL B CG1   1 
ATOM   1306 C  CG2   . VAL A 1 170 ? 137.036 153.887 149.572 1.00 45.75  ? 172 VAL B CG2   1 
ATOM   1307 N  N     . PRO A 1 171 ? 138.142 154.869 153.740 1.00 51.11  ? 173 PRO B N     1 
ATOM   1308 C  CA    . PRO A 1 171 ? 139.041 155.114 154.873 1.00 48.86  ? 173 PRO B CA    1 
ATOM   1309 C  C     . PRO A 1 171 ? 140.485 155.284 154.430 1.00 51.92  ? 173 PRO B C     1 
ATOM   1310 O  O     . PRO A 1 171 ? 140.958 154.615 153.510 1.00 58.07  ? 173 PRO B O     1 
ATOM   1311 C  CB    . PRO A 1 171 ? 138.863 153.863 155.737 1.00 48.61  ? 173 PRO B CB    1 
ATOM   1312 C  CG    . PRO A 1 171 ? 137.522 153.357 155.387 1.00 53.42  ? 173 PRO B CG    1 
ATOM   1313 C  CD    . PRO A 1 171 ? 137.310 153.674 153.945 1.00 54.64  ? 173 PRO B CD    1 
ATOM   1314 N  N     . SER A 1 172 ? 141.177 156.176 155.094 1.00 61.82  ? 174 SER B N     1 
ATOM   1315 C  CA    . SER A 1 172 ? 142.546 156.569 154.814 1.00 64.14  ? 174 SER B CA    1 
ATOM   1316 C  C     . SER A 1 172 ? 143.506 155.952 155.822 1.00 63.64  ? 174 SER B C     1 
ATOM   1317 O  O     . SER A 1 172 ? 143.136 155.705 156.972 1.00 65.90  ? 174 SER B O     1 
ATOM   1318 C  CB    . SER A 1 172 ? 142.684 158.093 154.850 1.00 66.35  ? 174 SER B CB    1 
ATOM   1319 O  OG    . SER A 1 172 ? 141.836 158.706 153.896 1.00 69.59  ? 174 SER B OG    1 
ATOM   1320 N  N     . PRO A 1 173 ? 144.746 155.684 155.411 1.00 64.93  ? 175 PRO B N     1 
ATOM   1321 C  CA    . PRO A 1 173 ? 145.710 155.049 156.322 1.00 66.85  ? 175 PRO B CA    1 
ATOM   1322 C  C     . PRO A 1 173 ? 146.165 155.949 157.460 1.00 69.17  ? 175 PRO B C     1 
ATOM   1323 O  O     . PRO A 1 173 ? 146.119 155.555 158.629 1.00 67.51  ? 175 PRO B O     1 
ATOM   1324 C  CB    . PRO A 1 173 ? 146.880 154.696 155.396 1.00 68.19  ? 175 PRO B CB    1 
ATOM   1325 C  CG    . PRO A 1 173 ? 146.779 155.679 154.275 1.00 69.92  ? 175 PRO B CG    1 
ATOM   1326 C  CD    . PRO A 1 173 ? 145.316 155.922 154.073 1.00 63.95  ? 175 PRO B CD    1 
ATOM   1327 N  N     . LYS A 1 174 ? 146.609 157.159 157.129 1.00 74.06  ? 176 LYS B N     1 
ATOM   1328 C  CA    . LYS A 1 174 ? 147.211 158.060 158.100 1.00 72.20  ? 176 LYS B CA    1 
ATOM   1329 C  C     . LYS A 1 174 ? 146.207 158.977 158.784 1.00 71.48  ? 176 LYS B C     1 
ATOM   1330 O  O     . LYS A 1 174 ? 146.569 159.645 159.757 1.00 72.59  ? 176 LYS B O     1 
ATOM   1331 C  CB    . LYS A 1 174 ? 148.291 158.907 157.423 1.00 72.33  ? 176 LYS B CB    1 
ATOM   1332 C  CG    . LYS A 1 174 ? 149.516 158.118 157.004 1.00 74.77  ? 176 LYS B CG    1 
ATOM   1333 C  CD    . LYS A 1 174 ? 150.633 159.036 156.536 1.00 72.92  ? 176 LYS B CD    1 
ATOM   1334 C  CE    . LYS A 1 174 ? 151.898 158.250 156.235 1.00 73.49  ? 176 LYS B CE    1 
ATOM   1335 N  NZ    . LYS A 1 174 ? 153.019 159.137 155.819 1.00 70.69  ? 176 LYS B NZ    1 
ATOM   1336 N  N     . VAL A 1 175 ? 144.968 159.030 158.308 1.00 66.79  ? 177 VAL B N     1 
ATOM   1337 C  CA    . VAL A 1 175 ? 143.931 159.868 158.895 1.00 64.91  ? 177 VAL B CA    1 
ATOM   1338 C  C     . VAL A 1 175 ? 142.756 158.971 159.247 1.00 68.36  ? 177 VAL B C     1 
ATOM   1339 O  O     . VAL A 1 175 ? 142.200 158.300 158.368 1.00 70.28  ? 177 VAL B O     1 
ATOM   1340 C  CB    . VAL A 1 175 ? 143.489 160.991 157.943 1.00 65.89  ? 177 VAL B CB    1 
ATOM   1341 C  CG1   . VAL A 1 175 ? 142.205 161.623 158.431 1.00 69.05  ? 177 VAL B CG1   1 
ATOM   1342 C  CG2   . VAL A 1 175 ? 144.581 162.034 157.818 1.00 66.93  ? 177 VAL B CG2   1 
ATOM   1343 N  N     . SER A 1 176 ? 142.377 158.956 160.521 1.00 61.63  ? 178 SER B N     1 
ATOM   1344 C  CA    . SER A 1 176 ? 141.301 158.091 160.973 1.00 61.41  ? 178 SER B CA    1 
ATOM   1345 C  C     . SER A 1 176 ? 140.579 158.746 162.139 1.00 64.68  ? 178 SER B C     1 
ATOM   1346 O  O     . SER A 1 176 ? 141.185 159.457 162.944 1.00 67.51  ? 178 SER B O     1 
ATOM   1347 C  CB    . SER A 1 176 ? 141.827 156.713 161.383 1.00 63.74  ? 178 SER B CB    1 
ATOM   1348 O  OG    . SER A 1 176 ? 142.647 156.805 162.533 1.00 68.80  ? 178 SER B OG    1 
ATOM   1349 N  N     . ASP A 1 177 ? 139.275 158.494 162.218 1.00 59.73  ? 179 ASP B N     1 
ATOM   1350 C  CA    . ASP A 1 177 ? 138.444 159.027 163.284 1.00 58.38  ? 179 ASP B CA    1 
ATOM   1351 C  C     . ASP A 1 177 ? 137.604 157.972 163.985 1.00 60.67  ? 179 ASP B C     1 
ATOM   1352 O  O     . ASP A 1 177 ? 136.979 158.289 165.002 1.00 65.93  ? 179 ASP B O     1 
ATOM   1353 C  CB    . ASP A 1 177 ? 137.512 160.119 162.740 1.00 61.83  ? 179 ASP B CB    1 
ATOM   1354 C  CG    . ASP A 1 177 ? 138.260 161.216 162.018 1.00 68.24  ? 179 ASP B CG    1 
ATOM   1355 O  OD1   . ASP A 1 177 ? 139.359 161.590 162.476 1.00 64.00  ? 179 ASP B OD1   1 
ATOM   1356 O  OD2   . ASP A 1 177 ? 137.750 161.705 160.988 1.00 70.56  ? 179 ASP B OD2   1 
ATOM   1357 N  N     . THR A 1 178 ? 137.605 156.738 163.410 1.00 46.91  ? 180 THR B N     1 
ATOM   1358 C  CA    . THR A 1 178 ? 136.802 155.660 163.997 1.00 47.28  ? 180 THR B CA    1 
ATOM   1359 C  C     . THR A 1 178 ? 137.715 154.497 164.320 1.00 50.15  ? 180 THR B C     1 
ATOM   1360 O  O     . THR A 1 178 ? 138.748 154.384 163.643 1.00 53.29  ? 180 THR B O     1 
ATOM   1361 C  CB    . THR A 1 178 ? 135.671 155.295 163.040 1.00 51.66  ? 180 THR B CB    1 
ATOM   1362 O  OG1   . THR A 1 178 ? 135.168 156.504 162.485 1.00 53.21  ? 180 THR B OG1   1 
ATOM   1363 C  CG2   . THR A 1 178 ? 134.537 154.558 163.730 1.00 52.96  ? 180 THR B CG2   1 
ATOM   1364 N  N     . VAL A 1 179 ? 137.387 153.690 165.365 1.00 45.60  ? 181 VAL B N     1 
ATOM   1365 C  CA    . VAL A 1 179 ? 138.173 152.508 165.691 1.00 42.05  ? 181 VAL B CA    1 
ATOM   1366 C  C     . VAL A 1 179 ? 137.722 151.273 164.921 1.00 42.97  ? 181 VAL B C     1 
ATOM   1367 O  O     . VAL A 1 179 ? 138.532 150.363 164.700 1.00 46.21  ? 181 VAL B O     1 
ATOM   1368 C  CB    . VAL A 1 179 ? 138.124 152.221 167.203 1.00 41.07  ? 181 VAL B CB    1 
ATOM   1369 C  CG1   . VAL A 1 179 ? 139.309 151.389 167.626 1.00 42.01  ? 181 VAL B CG1   1 
ATOM   1370 C  CG2   . VAL A 1 179 ? 138.093 153.515 167.983 1.00 46.31  ? 181 VAL B CG2   1 
ATOM   1371 N  N     . VAL A 1 180 ? 136.465 151.219 164.492 1.00 43.60  ? 182 VAL B N     1 
ATOM   1372 C  CA    . VAL A 1 180 ? 135.918 150.030 163.852 1.00 43.01  ? 182 VAL B CA    1 
ATOM   1373 C  C     . VAL A 1 180 ? 135.739 150.282 162.361 1.00 42.71  ? 182 VAL B C     1 
ATOM   1374 O  O     . VAL A 1 180 ? 134.883 149.674 161.712 1.00 48.52  ? 182 VAL B O     1 
ATOM   1375 C  CB    . VAL A 1 180 ? 134.592 149.615 164.512 1.00 42.34  ? 182 VAL B CB    1 
ATOM   1376 C  CG1   . VAL A 1 180 ? 134.851 149.043 165.883 1.00 41.77  ? 182 VAL B CG1   1 
ATOM   1377 C  CG2   . VAL A 1 180 ? 133.667 150.803 164.614 1.00 41.31  ? 182 VAL B CG2   1 
ATOM   1378 N  N     . GLU A 1 181 ? 136.550 151.183 161.816 1.00 50.01  ? 183 GLU B N     1 
ATOM   1379 C  CA    . GLU A 1 181 ? 136.495 151.491 160.387 1.00 48.21  ? 183 GLU B CA    1 
ATOM   1380 C  C     . GLU A 1 181 ? 136.793 150.294 159.489 1.00 53.52  ? 183 GLU B C     1 
ATOM   1381 O  O     . GLU A 1 181 ? 136.076 150.114 158.488 1.00 57.64  ? 183 GLU B O     1 
ATOM   1382 C  CB    . GLU A 1 181 ? 137.451 152.651 160.093 1.00 48.31  ? 183 GLU B CB    1 
ATOM   1383 C  CG    . GLU A 1 181 ? 136.929 153.657 159.094 1.00 54.78  ? 183 GLU B CG    1 
ATOM   1384 C  CD    . GLU A 1 181 ? 137.785 154.904 159.036 1.00 62.44  ? 183 GLU B CD    1 
ATOM   1385 O  OE1   . GLU A 1 181 ? 138.827 154.940 159.723 1.00 60.36  ? 183 GLU B OE1   1 
ATOM   1386 O  OE2   . GLU A 1 181 ? 137.416 155.848 158.307 1.00 61.66  ? 183 GLU B OE2   1 
ATOM   1387 N  N     . PRO A 1 182 ? 137.826 149.474 159.742 1.00 43.13  ? 184 PRO B N     1 
ATOM   1388 C  CA    . PRO A 1 182 ? 138.117 148.376 158.806 1.00 37.31  ? 184 PRO B CA    1 
ATOM   1389 C  C     . PRO A 1 182 ? 136.967 147.412 158.609 1.00 40.51  ? 184 PRO B C     1 
ATOM   1390 O  O     . PRO A 1 182 ? 136.726 146.964 157.479 1.00 49.32  ? 184 PRO B O     1 
ATOM   1391 C  CB    . PRO A 1 182 ? 139.321 147.683 159.454 1.00 39.39  ? 184 PRO B CB    1 
ATOM   1392 C  CG    . PRO A 1 182 ? 139.940 148.708 160.284 1.00 36.55  ? 184 PRO B CG    1 
ATOM   1393 C  CD    . PRO A 1 182 ? 138.833 149.533 160.815 1.00 42.44  ? 184 PRO B CD    1 
ATOM   1394 N  N     . TYR A 1 183 ? 136.241 147.087 159.677 1.00 35.21  ? 185 TYR B N     1 
ATOM   1395 C  CA    . TYR A 1 183 ? 135.109 146.178 159.559 1.00 39.16  ? 185 TYR B CA    1 
ATOM   1396 C  C     . TYR A 1 183 ? 134.083 146.718 158.577 1.00 44.05  ? 185 TYR B C     1 
ATOM   1397 O  O     . TYR A 1 183 ? 133.648 146.014 157.654 1.00 55.78  ? 185 TYR B O     1 
ATOM   1398 C  CB    . TYR A 1 183 ? 134.467 145.972 160.927 1.00 42.33  ? 185 TYR B CB    1 
ATOM   1399 C  CG    . TYR A 1 183 ? 135.259 145.122 161.885 1.00 40.25  ? 185 TYR B CG    1 
ATOM   1400 C  CD1   . TYR A 1 183 ? 136.298 144.326 161.448 1.00 41.11  ? 185 TYR B CD1   1 
ATOM   1401 C  CD2   . TYR A 1 183 ? 134.961 145.122 163.232 1.00 45.52  ? 185 TYR B CD2   1 
ATOM   1402 C  CE1   . TYR A 1 183 ? 137.011 143.553 162.329 1.00 41.50  ? 185 TYR B CE1   1 
ATOM   1403 C  CE2   . TYR A 1 183 ? 135.668 144.354 164.114 1.00 41.80  ? 185 TYR B CE2   1 
ATOM   1404 C  CZ    . TYR A 1 183 ? 136.689 143.574 163.660 1.00 39.00  ? 185 TYR B CZ    1 
ATOM   1405 O  OH    . TYR A 1 183 ? 137.396 142.808 164.551 1.00 43.30  ? 185 TYR B OH    1 
ATOM   1406 N  N     . ASN A 1 184 ? 133.689 147.976 158.763 1.00 37.28  ? 186 ASN B N     1 
ATOM   1407 C  CA    . ASN A 1 184 ? 132.684 148.582 157.905 1.00 33.38  ? 186 ASN B CA    1 
ATOM   1408 C  C     . ASN A 1 184 ? 133.168 148.679 156.467 1.00 38.03  ? 186 ASN B C     1 
ATOM   1409 O  O     . ASN A 1 184 ? 132.418 148.373 155.533 1.00 46.71  ? 186 ASN B O     1 
ATOM   1410 C  CB    . ASN A 1 184 ? 132.315 149.959 158.444 1.00 30.52  ? 186 ASN B CB    1 
ATOM   1411 C  CG    . ASN A 1 184 ? 132.126 149.961 159.938 1.00 37.33  ? 186 ASN B CG    1 
ATOM   1412 O  OD1   . ASN A 1 184 ? 132.126 148.913 160.573 1.00 42.65  ? 186 ASN B OD1   1 
ATOM   1413 N  ND2   . ASN A 1 184 ? 131.973 151.140 160.512 1.00 41.61  ? 186 ASN B ND2   1 
ATOM   1414 N  N     . ALA A 1 185 ? 134.417 149.100 156.266 1.00 38.16  ? 187 ALA B N     1 
ATOM   1415 C  CA    . ALA A 1 185 ? 134.930 149.232 154.907 1.00 37.41  ? 187 ALA B CA    1 
ATOM   1416 C  C     . ALA A 1 185 ? 134.939 147.890 154.186 1.00 37.15  ? 187 ALA B C     1 
ATOM   1417 O  O     . ALA A 1 185 ? 134.543 147.803 153.015 1.00 46.62  ? 187 ALA B O     1 
ATOM   1418 C  CB    . ALA A 1 185 ? 136.328 149.841 154.929 1.00 43.09  ? 187 ALA B CB    1 
ATOM   1419 N  N     . THR A 1 186 ? 135.375 146.829 154.869 1.00 34.86  ? 188 THR B N     1 
ATOM   1420 C  CA    . THR A 1 186 ? 135.400 145.513 154.241 1.00 30.11  ? 188 THR B CA    1 
ATOM   1421 C  C     . THR A 1 186 ? 133.993 145.036 153.911 1.00 38.18  ? 188 THR B C     1 
ATOM   1422 O  O     . THR A 1 186 ? 133.719 144.595 152.783 1.00 49.81  ? 188 THR B O     1 
ATOM   1423 C  CB    . THR A 1 186 ? 136.106 144.514 155.148 1.00 32.65  ? 188 THR B CB    1 
ATOM   1424 O  OG1   . THR A 1 186 ? 137.390 145.028 155.513 1.00 45.16  ? 188 THR B OG1   1 
ATOM   1425 C  CG2   . THR A 1 186 ? 136.290 143.197 154.438 1.00 38.40  ? 188 THR B CG2   1 
ATOM   1426 N  N     . LEU A 1 187 ? 133.082 145.122 154.883 1.00 36.29  ? 189 LEU B N     1 
ATOM   1427 C  CA    . LEU A 1 187 ? 131.723 144.659 154.658 1.00 35.52  ? 189 LEU B CA    1 
ATOM   1428 C  C     . LEU A 1 187 ? 130.998 145.487 153.609 1.00 38.59  ? 189 LEU B C     1 
ATOM   1429 O  O     . LEU A 1 187 ? 130.022 145.006 153.027 1.00 45.67  ? 189 LEU B O     1 
ATOM   1430 C  CB    . LEU A 1 187 ? 130.945 144.671 155.971 1.00 32.85  ? 189 LEU B CB    1 
ATOM   1431 C  CG    . LEU A 1 187 ? 131.437 143.694 157.036 1.00 31.65  ? 189 LEU B CG    1 
ATOM   1432 C  CD1   . LEU A 1 187 ? 130.900 144.075 158.391 1.00 41.53  ? 189 LEU B CD1   1 
ATOM   1433 C  CD2   . LEU A 1 187 ? 131.041 142.282 156.698 1.00 37.53  ? 189 LEU B CD2   1 
ATOM   1434 N  N     . SER A 1 188 ? 131.451 146.711 153.349 1.00 38.40  ? 190 SER B N     1 
ATOM   1435 C  CA    . SER A 1 188 ? 130.842 147.546 152.323 1.00 38.99  ? 190 SER B CA    1 
ATOM   1436 C  C     . SER A 1 188 ? 131.394 147.260 150.933 1.00 43.83  ? 190 SER B C     1 
ATOM   1437 O  O     . SER A 1 188 ? 130.633 147.240 149.956 1.00 55.28  ? 190 SER B O     1 
ATOM   1438 C  CB    . SER A 1 188 ? 131.043 149.020 152.668 1.00 42.39  ? 190 SER B CB    1 
ATOM   1439 O  OG    . SER A 1 188 ? 130.010 149.815 152.117 1.00 50.26  ? 190 SER B OG    1 
ATOM   1440 N  N     . VAL A 1 189 ? 132.705 147.045 150.820 1.00 39.32  ? 191 VAL B N     1 
ATOM   1441 C  CA    . VAL A 1 189 ? 133.280 146.688 149.526 1.00 39.39  ? 191 VAL B CA    1 
ATOM   1442 C  C     . VAL A 1 189 ? 132.746 145.340 149.067 1.00 42.68  ? 191 VAL B C     1 
ATOM   1443 O  O     . VAL A 1 189 ? 132.508 145.122 147.870 1.00 54.75  ? 191 VAL B O     1 
ATOM   1444 C  CB    . VAL A 1 189 ? 134.816 146.696 149.596 1.00 41.88  ? 191 VAL B CB    1 
ATOM   1445 C  CG1   . VAL A 1 189 ? 135.412 146.109 148.336 1.00 46.13  ? 191 VAL B CG1   1 
ATOM   1446 C  CG2   . VAL A 1 189 ? 135.327 148.103 149.813 1.00 44.15  ? 191 VAL B CG2   1 
ATOM   1447 N  N     . HIS A 1 190 ? 132.522 144.422 150.013 1.00 38.09  ? 192 HIS B N     1 
ATOM   1448 C  CA    . HIS A 1 190 ? 132.032 143.096 149.648 1.00 39.23  ? 192 HIS B CA    1 
ATOM   1449 C  C     . HIS A 1 190 ? 130.713 143.162 148.886 1.00 39.39  ? 192 HIS B C     1 
ATOM   1450 O  O     . HIS A 1 190 ? 130.409 142.261 148.098 1.00 46.50  ? 192 HIS B O     1 
ATOM   1451 C  CB    . HIS A 1 190 ? 131.891 142.238 150.905 1.00 44.15  ? 192 HIS B CB    1 
ATOM   1452 C  CG    . HIS A 1 190 ? 131.136 140.963 150.695 1.00 42.97  ? 192 HIS B CG    1 
ATOM   1453 N  ND1   . HIS A 1 190 ? 131.532 140.004 149.792 1.00 46.08  ? 192 HIS B ND1   1 
ATOM   1454 C  CD2   . HIS A 1 190 ? 130.028 140.475 151.299 1.00 46.20  ? 192 HIS B CD2   1 
ATOM   1455 C  CE1   . HIS A 1 190 ? 130.690 138.989 149.833 1.00 45.86  ? 192 HIS B CE1   1 
ATOM   1456 N  NE2   . HIS A 1 190 ? 129.768 139.250 150.739 1.00 47.43  ? 192 HIS B NE2   1 
ATOM   1457 N  N     . GLN A 1 191 ? 129.929 144.217 149.087 1.00 42.11  ? 193 GLN B N     1 
ATOM   1458 C  CA    . GLN A 1 191 ? 128.673 144.397 148.371 1.00 46.60  ? 193 GLN B CA    1 
ATOM   1459 C  C     . GLN A 1 191 ? 128.781 145.356 147.197 1.00 48.34  ? 193 GLN B C     1 
ATOM   1460 O  O     . GLN A 1 191 ? 128.086 145.171 146.185 1.00 56.79  ? 193 GLN B O     1 
ATOM   1461 C  CB    . GLN A 1 191 ? 127.593 144.904 149.326 1.00 46.93  ? 193 GLN B CB    1 
ATOM   1462 C  CG    . GLN A 1 191 ? 127.485 144.093 150.594 1.00 47.60  ? 193 GLN B CG    1 
ATOM   1463 C  CD    . GLN A 1 191 ? 126.165 143.380 150.712 1.00 56.14  ? 193 GLN B CD    1 
ATOM   1464 O  OE1   . GLN A 1 191 ? 125.269 143.570 149.894 1.00 53.39  ? 193 GLN B OE1   1 
ATOM   1465 N  NE2   . GLN A 1 191 ? 126.033 142.551 151.736 1.00 52.58  ? 193 GLN B NE2   1 
ATOM   1466 N  N     . LEU A 1 192 ? 129.630 146.377 147.314 1.00 45.67  ? 194 LEU B N     1 
ATOM   1467 C  CA    . LEU A 1 192 ? 129.840 147.290 146.198 1.00 40.57  ? 194 LEU B CA    1 
ATOM   1468 C  C     . LEU A 1 192 ? 130.389 146.555 144.987 1.00 47.31  ? 194 LEU B C     1 
ATOM   1469 O  O     . LEU A 1 192 ? 130.009 146.851 143.849 1.00 56.04  ? 194 LEU B O     1 
ATOM   1470 C  CB    . LEU A 1 192 ? 130.784 148.415 146.605 1.00 38.88  ? 194 LEU B CB    1 
ATOM   1471 C  CG    . LEU A 1 192 ? 130.168 149.571 147.380 1.00 40.59  ? 194 LEU B CG    1 
ATOM   1472 C  CD1   . LEU A 1 192 ? 131.193 150.664 147.563 1.00 47.09  ? 194 LEU B CD1   1 
ATOM   1473 C  CD2   . LEU A 1 192 ? 128.945 150.098 146.668 1.00 50.46  ? 194 LEU B CD2   1 
ATOM   1474 N  N     . VAL A 1 193 ? 131.285 145.591 145.205 1.00 39.40  ? 195 VAL B N     1 
ATOM   1475 C  CA    . VAL A 1 193 ? 131.894 144.884 144.085 1.00 39.73  ? 195 VAL B CA    1 
ATOM   1476 C  C     . VAL A 1 193 ? 130.900 144.039 143.310 1.00 45.89  ? 195 VAL B C     1 
ATOM   1477 O  O     . VAL A 1 193 ? 131.213 143.598 142.201 1.00 53.68  ? 195 VAL B O     1 
ATOM   1478 C  CB    . VAL A 1 193 ? 133.065 144.010 144.576 1.00 42.10  ? 195 VAL B CB    1 
ATOM   1479 C  CG1   . VAL A 1 193 ? 132.565 142.666 145.055 1.00 44.80  ? 195 VAL B CG1   1 
ATOM   1480 C  CG2   . VAL A 1 193 ? 134.092 143.838 143.481 1.00 45.75  ? 195 VAL B CG2   1 
ATOM   1481 N  N     . GLU A 1 194 ? 129.707 143.809 143.852 1.00 54.54  ? 196 GLU B N     1 
ATOM   1482 C  CA    . GLU A 1 194 ? 128.708 142.980 143.195 1.00 52.80  ? 196 GLU B CA    1 
ATOM   1483 C  C     . GLU A 1 194 ? 127.497 143.746 142.693 1.00 55.04  ? 196 GLU B C     1 
ATOM   1484 O  O     . GLU A 1 194 ? 126.917 143.350 141.683 1.00 61.14  ? 196 GLU B O     1 
ATOM   1485 C  CB    . GLU A 1 194 ? 128.221 141.876 144.140 1.00 53.60  ? 196 GLU B CB    1 
ATOM   1486 C  CG    . GLU A 1 194 ? 129.289 140.882 144.535 1.00 59.66  ? 196 GLU B CG    1 
ATOM   1487 C  CD    . GLU A 1 194 ? 128.765 139.809 145.466 1.00 66.16  ? 196 GLU B CD    1 
ATOM   1488 O  OE1   . GLU A 1 194 ? 127.574 139.873 145.836 1.00 66.25  ? 196 GLU B OE1   1 
ATOM   1489 O  OE2   . GLU A 1 194 ? 129.543 138.901 145.827 1.00 66.17  ? 196 GLU B OE2   1 
ATOM   1490 N  N     . ASN A 1 195 ? 127.089 144.825 143.363 1.00 51.95  ? 197 ASN B N     1 
ATOM   1491 C  CA    . ASN A 1 195 ? 125.833 145.481 143.019 1.00 52.32  ? 197 ASN B CA    1 
ATOM   1492 C  C     . ASN A 1 195 ? 126.018 146.875 142.428 1.00 54.16  ? 197 ASN B C     1 
ATOM   1493 O  O     . ASN A 1 195 ? 125.085 147.681 142.462 1.00 64.60  ? 197 ASN B O     1 
ATOM   1494 C  CB    . ASN A 1 195 ? 124.928 145.546 144.247 1.00 54.49  ? 197 ASN B CB    1 
ATOM   1495 C  CG    . ASN A 1 195 ? 124.550 144.177 144.761 1.00 61.29  ? 197 ASN B CG    1 
ATOM   1496 O  OD1   . ASN A 1 195 ? 124.331 143.250 143.984 1.00 61.90  ? 197 ASN B OD1   1 
ATOM   1497 N  ND2   . ASN A 1 195 ? 124.478 144.039 146.077 1.00 59.80  ? 197 ASN B ND2   1 
ATOM   1498 N  N     . THR A 1 196 ? 127.188 147.178 141.873 1.00 49.15  ? 198 THR B N     1 
ATOM   1499 C  CA    . THR A 1 196 ? 127.479 148.510 141.364 1.00 44.80  ? 198 THR B CA    1 
ATOM   1500 C  C     . THR A 1 196 ? 128.011 148.416 139.943 1.00 53.45  ? 198 THR B C     1 
ATOM   1501 O  O     . THR A 1 196 ? 128.588 147.403 139.543 1.00 62.91  ? 198 THR B O     1 
ATOM   1502 C  CB    . THR A 1 196 ? 128.493 149.242 142.250 1.00 50.24  ? 198 THR B CB    1 
ATOM   1503 O  OG1   . THR A 1 196 ? 128.277 148.880 143.618 1.00 59.35  ? 198 THR B OG1   1 
ATOM   1504 C  CG2   . THR A 1 196 ? 128.338 150.736 142.120 1.00 49.45  ? 198 THR B CG2   1 
ATOM   1505 N  N     . ASP A 1 197 ? 127.810 149.490 139.180 1.00 58.07  ? 199 ASP B N     1 
ATOM   1506 C  CA    . ASP A 1 197 ? 128.275 149.569 137.801 1.00 50.48  ? 199 ASP B CA    1 
ATOM   1507 C  C     . ASP A 1 197 ? 129.577 150.340 137.649 1.00 48.55  ? 199 ASP B C     1 
ATOM   1508 O  O     . ASP A 1 197 ? 130.391 149.991 136.790 1.00 57.58  ? 199 ASP B O     1 
ATOM   1509 C  CB    . ASP A 1 197 ? 127.202 150.216 136.922 1.00 52.61  ? 199 ASP B CB    1 
ATOM   1510 C  CG    . ASP A 1 197 ? 127.065 149.537 135.580 1.00 60.60  ? 199 ASP B CG    1 
ATOM   1511 O  OD1   . ASP A 1 197 ? 128.093 149.365 134.892 1.00 58.58  ? 199 ASP B OD1   1 
ATOM   1512 O  OD2   . ASP A 1 197 ? 125.930 149.170 135.213 1.00 60.11  ? 199 ASP B OD2   1 
ATOM   1513 N  N     . GLU A 1 198 ? 129.791 151.380 138.452 1.00 46.46  ? 200 GLU B N     1 
ATOM   1514 C  CA    . GLU A 1 198 ? 131.071 152.082 138.489 1.00 46.36  ? 200 GLU B CA    1 
ATOM   1515 C  C     . GLU A 1 198 ? 131.124 152.900 139.767 1.00 48.40  ? 200 GLU B C     1 
ATOM   1516 O  O     . GLU A 1 198 ? 130.253 153.738 139.996 1.00 56.00  ? 200 GLU B O     1 
ATOM   1517 C  CB    . GLU A 1 198 ? 131.252 152.977 137.264 1.00 54.04  ? 200 GLU B CB    1 
ATOM   1518 C  CG    . GLU A 1 198 ? 130.003 153.699 136.807 1.00 56.13  ? 200 GLU B CG    1 
ATOM   1519 C  CD    . GLU A 1 198 ? 130.211 154.434 135.503 1.00 58.09  ? 200 GLU B CD    1 
ATOM   1520 O  OE1   . GLU A 1 198 ? 131.163 154.089 134.775 1.00 60.63  ? 200 GLU B OE1   1 
ATOM   1521 O  OE2   . GLU A 1 198 ? 129.427 155.356 135.206 1.00 57.77  ? 200 GLU B OE2   1 
ATOM   1522 N  N     . THR A 1 199 ? 132.142 152.672 140.591 1.00 43.42  ? 201 THR B N     1 
ATOM   1523 C  CA    . THR A 1 199 ? 132.281 153.347 141.873 1.00 40.13  ? 201 THR B CA    1 
ATOM   1524 C  C     . THR A 1 199 ? 133.539 154.202 141.873 1.00 42.16  ? 201 THR B C     1 
ATOM   1525 O  O     . THR A 1 199 ? 134.611 153.735 141.481 1.00 48.02  ? 201 THR B O     1 
ATOM   1526 C  CB    . THR A 1 199 ? 132.323 152.340 143.024 1.00 42.06  ? 201 THR B CB    1 
ATOM   1527 O  OG1   . THR A 1 199 ? 131.103 151.593 143.054 1.00 48.54  ? 201 THR B OG1   1 
ATOM   1528 C  CG2   . THR A 1 199 ? 132.508 153.047 144.343 1.00 45.72  ? 201 THR B CG2   1 
ATOM   1529 N  N     . TYR A 1 200 ? 133.403 155.449 142.313 1.00 44.38  ? 202 TYR B N     1 
ATOM   1530 C  CA    . TYR A 1 200 ? 134.507 156.399 142.356 1.00 42.74  ? 202 TYR B CA    1 
ATOM   1531 C  C     . TYR A 1 200 ? 135.066 156.450 143.770 1.00 48.47  ? 202 TYR B C     1 
ATOM   1532 O  O     . TYR A 1 200 ? 134.337 156.751 144.718 1.00 52.93  ? 202 TYR B O     1 
ATOM   1533 C  CB    . TYR A 1 200 ? 134.056 157.790 141.920 1.00 42.42  ? 202 TYR B CB    1 
ATOM   1534 C  CG    . TYR A 1 200 ? 133.519 157.861 140.517 1.00 43.93  ? 202 TYR B CG    1 
ATOM   1535 C  CD1   . TYR A 1 200 ? 132.235 157.437 140.223 1.00 46.66  ? 202 TYR B CD1   1 
ATOM   1536 C  CD2   . TYR A 1 200 ? 134.291 158.354 139.488 1.00 45.25  ? 202 TYR B CD2   1 
ATOM   1537 C  CE1   . TYR A 1 200 ? 131.741 157.500 138.945 1.00 45.92  ? 202 TYR B CE1   1 
ATOM   1538 C  CE2   . TYR A 1 200 ? 133.803 158.421 138.208 1.00 48.43  ? 202 TYR B CE2   1 
ATOM   1539 C  CZ    . TYR A 1 200 ? 132.528 157.996 137.943 1.00 46.96  ? 202 TYR B CZ    1 
ATOM   1540 O  OH    . TYR A 1 200 ? 132.037 158.060 136.666 1.00 48.68  ? 202 TYR B OH    1 
ATOM   1541 N  N     . CYS A 1 201 ? 136.356 156.174 143.904 1.00 49.98  ? 203 CYS B N     1 
ATOM   1542 C  CA    . CYS A 1 201 ? 137.007 156.079 145.201 1.00 42.90  ? 203 CYS B CA    1 
ATOM   1543 C  C     . CYS A 1 201 ? 137.645 157.412 145.564 1.00 51.96  ? 203 CYS B C     1 
ATOM   1544 O  O     . CYS A 1 201 ? 138.449 157.951 144.799 1.00 60.97  ? 203 CYS B O     1 
ATOM   1545 C  CB    . CYS A 1 201 ? 138.060 154.975 145.192 1.00 52.46  ? 203 CYS B CB    1 
ATOM   1546 S  SG    . CYS A 1 201 ? 137.382 153.312 145.122 1.00 74.48  ? 203 CYS B SG    1 
ATOM   1547 N  N     . ILE A 1 202 ? 137.287 157.933 146.733 1.00 49.57  ? 204 ILE B N     1 
ATOM   1548 C  CA    . ILE A 1 202 ? 137.804 159.193 147.249 1.00 41.26  ? 204 ILE B CA    1 
ATOM   1549 C  C     . ILE A 1 202 ? 138.258 158.965 148.682 1.00 45.61  ? 204 ILE B C     1 
ATOM   1550 O  O     . ILE A 1 202 ? 137.631 158.201 149.423 1.00 56.51  ? 204 ILE B O     1 
ATOM   1551 C  CB    . ILE A 1 202 ? 136.741 160.308 147.189 1.00 40.52  ? 204 ILE B CB    1 
ATOM   1552 C  CG1   . ILE A 1 202 ? 136.204 160.457 145.773 1.00 43.05  ? 204 ILE B CG1   1 
ATOM   1553 C  CG2   . ILE A 1 202 ? 137.311 161.627 147.658 1.00 52.19  ? 204 ILE B CG2   1 
ATOM   1554 C  CD1   . ILE A 1 202 ? 135.111 161.475 145.655 1.00 51.64  ? 204 ILE B CD1   1 
ATOM   1555 N  N     . ASP A 1 203 ? 139.352 159.607 149.071 1.00 47.98  ? 205 ASP B N     1 
ATOM   1556 C  CA    . ASP A 1 203 ? 139.799 159.582 150.453 1.00 45.48  ? 205 ASP B CA    1 
ATOM   1557 C  C     . ASP A 1 203 ? 140.196 160.981 150.888 1.00 46.94  ? 205 ASP B C     1 
ATOM   1558 O  O     . ASP A 1 203 ? 140.664 161.792 150.085 1.00 55.13  ? 205 ASP B O     1 
ATOM   1559 C  CB    . ASP A 1 203 ? 140.963 158.619 150.655 1.00 51.35  ? 205 ASP B CB    1 
ATOM   1560 C  CG    . ASP A 1 203 ? 141.932 158.632 149.504 1.00 63.68  ? 205 ASP B CG    1 
ATOM   1561 O  OD1   . ASP A 1 203 ? 142.224 159.727 148.984 1.00 63.04  ? 205 ASP B OD1   1 
ATOM   1562 O  OD2   . ASP A 1 203 ? 142.396 157.543 149.108 1.00 66.64  ? 205 ASP B OD2   1 
ATOM   1563 N  N     . ASN A 1 204 ? 140.002 161.254 152.176 1.00 41.71  ? 206 ASN B N     1 
ATOM   1564 C  CA    . ASN A 1 204 ? 140.246 162.587 152.703 1.00 39.91  ? 206 ASN B CA    1 
ATOM   1565 C  C     . ASN A 1 204 ? 141.720 162.956 152.702 1.00 48.00  ? 206 ASN B C     1 
ATOM   1566 O  O     . ASN A 1 204 ? 142.045 164.147 152.666 1.00 55.58  ? 206 ASN B O     1 
ATOM   1567 C  CB    . ASN A 1 204 ? 139.685 162.696 154.115 1.00 42.68  ? 206 ASN B CB    1 
ATOM   1568 C  CG    . ASN A 1 204 ? 138.194 162.893 154.131 1.00 44.28  ? 206 ASN B CG    1 
ATOM   1569 O  OD1   . ASN A 1 204 ? 137.631 163.511 153.235 1.00 48.01  ? 206 ASN B OD1   1 
ATOM   1570 N  ND2   . ASN A 1 204 ? 137.542 162.372 155.155 1.00 46.40  ? 206 ASN B ND2   1 
ATOM   1571 N  N     . GLU A 1 205 ? 142.617 161.972 152.738 1.00 53.45  ? 207 GLU B N     1 
ATOM   1572 C  CA    . GLU A 1 205 ? 144.042 162.278 152.769 1.00 52.51  ? 207 GLU B CA    1 
ATOM   1573 C  C     . GLU A 1 205 ? 144.497 162.955 151.484 1.00 60.51  ? 207 GLU B C     1 
ATOM   1574 O  O     . GLU A 1 205 ? 145.240 163.943 151.526 1.00 68.96  ? 207 GLU B O     1 
ATOM   1575 C  CB    . GLU A 1 205 ? 144.844 161.005 153.016 1.00 56.99  ? 207 GLU B CB    1 
ATOM   1576 C  CG    . GLU A 1 205 ? 146.330 161.163 152.790 1.00 65.24  ? 207 GLU B CG    1 
ATOM   1577 C  CD    . GLU A 1 205 ? 147.078 159.856 152.926 1.00 71.17  ? 207 GLU B CD    1 
ATOM   1578 O  OE1   . GLU A 1 205 ? 146.439 158.838 153.262 1.00 69.98  ? 207 GLU B OE1   1 
ATOM   1579 O  OE2   . GLU A 1 205 ? 148.305 159.845 152.697 1.00 67.60  ? 207 GLU B OE2   1 
ATOM   1580 N  N     . ALA A 1 206 ? 144.057 162.447 150.332 1.00 50.23  ? 208 ALA B N     1 
ATOM   1581 C  CA    . ALA A 1 206 ? 144.442 163.062 149.070 1.00 46.19  ? 208 ALA B CA    1 
ATOM   1582 C  C     . ALA A 1 206 ? 143.857 164.459 148.937 1.00 48.79  ? 208 ALA B C     1 
ATOM   1583 O  O     . ALA A 1 206 ? 144.506 165.362 148.398 1.00 58.82  ? 208 ALA B O     1 
ATOM   1584 C  CB    . ALA A 1 206 ? 144.009 162.183 147.901 1.00 49.19  ? 208 ALA B CB    1 
ATOM   1585 N  N     . LEU A 1 207 ? 142.628 164.655 149.410 1.00 37.22  ? 209 LEU B N     1 
ATOM   1586 C  CA    . LEU A 1 207 ? 142.024 165.979 149.356 1.00 40.46  ? 209 LEU B CA    1 
ATOM   1587 C  C     . LEU A 1 207 ? 142.780 166.964 150.237 1.00 45.46  ? 209 LEU B C     1 
ATOM   1588 O  O     . LEU A 1 207 ? 143.018 168.112 149.836 1.00 54.16  ? 209 LEU B O     1 
ATOM   1589 C  CB    . LEU A 1 207 ? 140.554 165.892 149.757 1.00 43.74  ? 209 LEU B CB    1 
ATOM   1590 C  CG    . LEU A 1 207 ? 139.679 165.072 148.811 1.00 45.44  ? 209 LEU B CG    1 
ATOM   1591 C  CD1   . LEU A 1 207 ? 138.417 164.616 149.504 1.00 45.80  ? 209 LEU B CD1   1 
ATOM   1592 C  CD2   . LEU A 1 207 ? 139.338 165.885 147.588 1.00 48.95  ? 209 LEU B CD2   1 
ATOM   1593 N  N     . TYR A 1 208 ? 143.181 166.529 151.431 1.00 43.58  ? 210 TYR B N     1 
ATOM   1594 C  CA    . TYR A 1 208 ? 144.005 167.373 152.287 1.00 38.95  ? 210 TYR B CA    1 
ATOM   1595 C  C     . TYR A 1 208 ? 145.332 167.700 151.620 1.00 42.95  ? 210 TYR B C     1 
ATOM   1596 O  O     . TYR A 1 208 ? 145.821 168.829 151.716 1.00 53.00  ? 210 TYR B O     1 
ATOM   1597 C  CB    . TYR A 1 208 ? 144.241 166.683 153.625 1.00 44.64  ? 210 TYR B CB    1 
ATOM   1598 C  CG    . TYR A 1 208 ? 143.159 166.915 154.643 1.00 41.83  ? 210 TYR B CG    1 
ATOM   1599 C  CD1   . TYR A 1 208 ? 142.804 168.192 155.021 1.00 42.64  ? 210 TYR B CD1   1 
ATOM   1600 C  CD2   . TYR A 1 208 ? 142.502 165.854 155.231 1.00 43.86  ? 210 TYR B CD2   1 
ATOM   1601 C  CE1   . TYR A 1 208 ? 141.822 168.403 155.952 1.00 44.40  ? 210 TYR B CE1   1 
ATOM   1602 C  CE2   . TYR A 1 208 ? 141.520 166.055 156.156 1.00 42.81  ? 210 TYR B CE2   1 
ATOM   1603 C  CZ    . TYR A 1 208 ? 141.182 167.330 156.514 1.00 45.07  ? 210 TYR B CZ    1 
ATOM   1604 O  OH    . TYR A 1 208 ? 140.195 167.532 157.445 1.00 47.39  ? 210 TYR B OH    1 
ATOM   1605 N  N     . ASP A 1 209 ? 145.941 166.715 150.957 1.00 48.45  ? 211 ASP B N     1 
ATOM   1606 C  CA    . ASP A 1 209 ? 147.209 166.954 150.278 1.00 46.83  ? 211 ASP B CA    1 
ATOM   1607 C  C     . ASP A 1 209 ? 147.053 167.979 149.163 1.00 47.00  ? 211 ASP B C     1 
ATOM   1608 O  O     . ASP A 1 209 ? 147.889 168.879 149.015 1.00 51.10  ? 211 ASP B O     1 
ATOM   1609 C  CB    . ASP A 1 209 ? 147.760 165.641 149.729 1.00 49.64  ? 211 ASP B CB    1 
ATOM   1610 C  CG    . ASP A 1 209 ? 149.196 165.758 149.279 1.00 59.86  ? 211 ASP B CG    1 
ATOM   1611 O  OD1   . ASP A 1 209 ? 150.073 165.977 150.140 1.00 61.16  ? 211 ASP B OD1   1 
ATOM   1612 O  OD2   . ASP A 1 209 ? 149.451 165.633 148.063 1.00 61.49  ? 211 ASP B OD2   1 
ATOM   1613 N  N     . ILE A 1 210 ? 145.979 167.867 148.379 1.00 47.33  ? 212 ILE B N     1 
ATOM   1614 C  CA    . ILE A 1 210 ? 145.717 168.836 147.317 1.00 48.66  ? 212 ILE B CA    1 
ATOM   1615 C  C     . ILE A 1 210 ? 145.544 170.229 147.902 1.00 50.19  ? 212 ILE B C     1 
ATOM   1616 O  O     . ILE A 1 210 ? 146.136 171.202 147.420 1.00 56.02  ? 212 ILE B O     1 
ATOM   1617 C  CB    . ILE A 1 210 ? 144.482 168.420 146.500 1.00 47.09  ? 212 ILE B CB    1 
ATOM   1618 C  CG1   . ILE A 1 210 ? 144.778 167.173 145.676 1.00 49.56  ? 212 ILE B CG1   1 
ATOM   1619 C  CG2   . ILE A 1 210 ? 144.039 169.548 145.600 1.00 49.36  ? 212 ILE B CG2   1 
ATOM   1620 C  CD1   . ILE A 1 210 ? 143.591 166.677 144.906 1.00 48.14  ? 212 ILE B CD1   1 
ATOM   1621 N  N     . CYS A 1 211 ? 144.749 170.342 148.966 1.00 53.20  ? 213 CYS B N     1 
ATOM   1622 C  CA    . CYS A 1 211 ? 144.500 171.648 149.566 1.00 46.94  ? 213 CYS B CA    1 
ATOM   1623 C  C     . CYS A 1 211 ? 145.775 172.256 150.134 1.00 47.27  ? 213 CYS B C     1 
ATOM   1624 O  O     . CYS A 1 211 ? 146.012 173.461 149.994 1.00 55.38  ? 213 CYS B O     1 
ATOM   1625 C  CB    . CYS A 1 211 ? 143.433 171.528 150.651 1.00 51.88  ? 213 CYS B CB    1 
ATOM   1626 S  SG    . CYS A 1 211 ? 141.796 171.114 150.033 1.00 72.62  ? 213 CYS B SG    1 
ATOM   1627 N  N     . PHE A 1 212 ? 146.610 171.444 150.778 1.00 46.87  ? 214 PHE B N     1 
ATOM   1628 C  CA    . PHE A 1 212 ? 147.808 171.978 151.415 1.00 47.42  ? 214 PHE B CA    1 
ATOM   1629 C  C     . PHE A 1 212 ? 148.868 172.358 150.392 1.00 53.12  ? 214 PHE B C     1 
ATOM   1630 O  O     . PHE A 1 212 ? 149.548 173.378 150.551 1.00 58.50  ? 214 PHE B O     1 
ATOM   1631 C  CB    . PHE A 1 212 ? 148.366 170.963 152.409 1.00 51.47  ? 214 PHE B CB    1 
ATOM   1632 C  CG    . PHE A 1 212 ? 147.691 170.993 153.746 1.00 56.55  ? 214 PHE B CG    1 
ATOM   1633 C  CD1   . PHE A 1 212 ? 147.343 172.191 154.330 1.00 55.14  ? 214 PHE B CD1   1 
ATOM   1634 C  CD2   . PHE A 1 212 ? 147.394 169.820 154.414 1.00 57.07  ? 214 PHE B CD2   1 
ATOM   1635 C  CE1   . PHE A 1 212 ? 146.724 172.220 155.556 1.00 57.74  ? 214 PHE B CE1   1 
ATOM   1636 C  CE2   . PHE A 1 212 ? 146.771 169.844 155.639 1.00 51.19  ? 214 PHE B CE2   1 
ATOM   1637 C  CZ    . PHE A 1 212 ? 146.435 171.044 156.210 1.00 50.93  ? 214 PHE B CZ    1 
ATOM   1638 N  N     . ARG A 1 213 ? 149.029 171.562 149.336 1.00 54.72  ? 215 ARG B N     1 
ATOM   1639 C  CA    . ARG A 1 213 ? 150.112 171.773 148.383 1.00 50.37  ? 215 ARG B CA    1 
ATOM   1640 C  C     . ARG A 1 213 ? 149.685 172.607 147.180 1.00 53.21  ? 215 ARG B C     1 
ATOM   1641 O  O     . ARG A 1 213 ? 150.255 173.673 146.931 1.00 63.25  ? 215 ARG B O     1 
ATOM   1642 C  CB    . ARG A 1 213 ? 150.667 170.419 147.934 1.00 51.54  ? 215 ARG B CB    1 
ATOM   1643 C  CG    . ARG A 1 213 ? 151.859 170.518 147.012 1.00 58.67  ? 215 ARG B CG    1 
ATOM   1644 C  CD    . ARG A 1 213 ? 152.980 169.607 147.469 1.00 62.37  ? 215 ARG B CD    1 
ATOM   1645 N  NE    . ARG A 1 213 ? 152.642 168.198 147.322 1.00 63.16  ? 215 ARG B NE    1 
ATOM   1646 C  CZ    . ARG A 1 213 ? 152.292 167.406 148.325 1.00 60.34  ? 215 ARG B CZ    1 
ATOM   1647 N  NH1   . ARG A 1 213 ? 152.200 167.859 149.563 1.00 56.04  ? 215 ARG B NH1   1 
ATOM   1648 N  NH2   . ARG A 1 213 ? 152.029 166.126 148.078 1.00 60.72  ? 215 ARG B NH2   1 
ATOM   1649 N  N     . THR A 1 214 ? 148.694 172.142 146.420 1.00 44.65  ? 216 THR B N     1 
ATOM   1650 C  CA    . THR A 1 214 ? 148.334 172.823 145.182 1.00 44.47  ? 216 THR B CA    1 
ATOM   1651 C  C     . THR A 1 214 ? 147.649 174.158 145.453 1.00 48.09  ? 216 THR B C     1 
ATOM   1652 O  O     . THR A 1 214 ? 148.017 175.183 144.871 1.00 50.01  ? 216 THR B O     1 
ATOM   1653 C  CB    . THR A 1 214 ? 147.438 171.922 144.335 1.00 48.95  ? 216 THR B CB    1 
ATOM   1654 O  OG1   . THR A 1 214 ? 148.113 170.688 144.074 1.00 49.30  ? 216 THR B OG1   1 
ATOM   1655 C  CG2   . THR A 1 214 ? 147.113 172.587 143.026 1.00 51.95  ? 216 THR B CG2   1 
ATOM   1656 N  N     . LEU A 1 215 ? 146.653 174.168 146.337 1.00 49.04  ? 217 LEU B N     1 
ATOM   1657 C  CA    . LEU A 1 215 ? 145.872 175.371 146.591 1.00 47.47  ? 217 LEU B CA    1 
ATOM   1658 C  C     . LEU A 1 215 ? 146.521 176.312 147.594 1.00 49.57  ? 217 LEU B C     1 
ATOM   1659 O  O     . LEU A 1 215 ? 146.086 177.463 147.699 1.00 53.32  ? 217 LEU B O     1 
ATOM   1660 C  CB    . LEU A 1 215 ? 144.478 174.997 147.091 1.00 46.81  ? 217 LEU B CB    1 
ATOM   1661 C  CG    . LEU A 1 215 ? 143.576 174.270 146.099 1.00 47.07  ? 217 LEU B CG    1 
ATOM   1662 C  CD1   . LEU A 1 215 ? 142.307 173.796 146.771 1.00 52.29  ? 217 LEU B CD1   1 
ATOM   1663 C  CD2   . LEU A 1 215 ? 143.255 175.164 144.931 1.00 50.60  ? 217 LEU B CD2   1 
ATOM   1664 N  N     . LYS A 1 216 ? 147.526 175.852 148.336 1.00 49.21  ? 218 LYS B N     1 
ATOM   1665 C  CA    . LYS A 1 216 ? 148.240 176.669 149.315 1.00 42.69  ? 218 LYS B CA    1 
ATOM   1666 C  C     . LYS A 1 216 ? 147.305 177.231 150.379 1.00 47.74  ? 218 LYS B C     1 
ATOM   1667 O  O     . LYS A 1 216 ? 147.539 178.314 150.913 1.00 52.86  ? 218 LYS B O     1 
ATOM   1668 C  CB    . LYS A 1 216 ? 149.007 177.806 148.637 1.00 48.48  ? 218 LYS B CB    1 
ATOM   1669 C  CG    . LYS A 1 216 ? 150.047 177.350 147.641 1.00 49.31  ? 218 LYS B CG    1 
ATOM   1670 C  CD    . LYS A 1 216 ? 151.123 176.529 148.301 1.00 48.97  ? 218 LYS B CD    1 
ATOM   1671 C  CE    . LYS A 1 216 ? 152.295 176.339 147.364 1.00 51.46  ? 218 LYS B CE    1 
ATOM   1672 N  NZ    . LYS A 1 216 ? 151.877 175.726 146.074 1.00 52.20  ? 218 LYS B NZ    1 
ATOM   1673 N  N     . LEU A 1 217 ? 146.240 176.506 150.696 1.00 54.04  ? 219 LEU B N     1 
ATOM   1674 C  CA    . LEU A 1 217 ? 145.327 176.940 151.740 1.00 48.95  ? 219 LEU B CA    1 
ATOM   1675 C  C     . LEU A 1 217 ? 145.968 176.768 153.110 1.00 53.68  ? 219 LEU B C     1 
ATOM   1676 O  O     . LEU A 1 217 ? 146.728 175.828 153.353 1.00 53.53  ? 219 LEU B O     1 
ATOM   1677 C  CB    . LEU A 1 217 ? 144.019 176.159 151.670 1.00 46.76  ? 219 LEU B CB    1 
ATOM   1678 C  CG    . LEU A 1 217 ? 143.069 176.529 150.537 1.00 50.44  ? 219 LEU B CG    1 
ATOM   1679 C  CD1   . LEU A 1 217 ? 141.871 175.604 150.537 1.00 52.86  ? 219 LEU B CD1   1 
ATOM   1680 C  CD2   . LEU A 1 217 ? 142.634 177.973 150.665 1.00 51.21  ? 219 LEU B CD2   1 
ATOM   1681 N  N     . THR A 1 218 ? 145.654 177.695 154.012 1.00 60.70  ? 220 THR B N     1 
ATOM   1682 C  CA    . THR A 1 218 ? 146.224 177.687 155.352 1.00 59.83  ? 220 THR B CA    1 
ATOM   1683 C  C     . THR A 1 218 ? 145.481 176.740 156.285 1.00 59.45  ? 220 THR B C     1 
ATOM   1684 O  O     . THR A 1 218 ? 146.088 175.838 156.870 1.00 64.38  ? 220 THR B O     1 
ATOM   1685 C  CB    . THR A 1 218 ? 146.213 179.099 155.937 1.00 61.79  ? 220 THR B CB    1 
ATOM   1686 O  OG1   . THR A 1 218 ? 144.861 179.557 156.048 1.00 60.28  ? 220 THR B OG1   1 
ATOM   1687 C  CG2   . THR A 1 218 ? 146.989 180.049 155.041 1.00 59.28  ? 220 THR B CG2   1 
ATOM   1688 N  N     . THR A 1 219 ? 144.174 176.930 156.436 1.00 47.93  ? 221 THR B N     1 
ATOM   1689 C  CA    . THR A 1 219 ? 143.349 176.114 157.323 1.00 50.47  ? 221 THR B CA    1 
ATOM   1690 C  C     . THR A 1 219 ? 142.163 175.556 156.541 1.00 51.58  ? 221 THR B C     1 
ATOM   1691 O  O     . THR A 1 219 ? 141.067 176.131 156.525 1.00 53.66  ? 221 THR B O     1 
ATOM   1692 C  CB    . THR A 1 219 ? 142.956 176.910 158.577 1.00 60.09  ? 221 THR B CB    1 
ATOM   1693 O  OG1   . THR A 1 219 ? 142.363 176.042 159.554 1.00 59.76  ? 221 THR B OG1   1 
ATOM   1694 C  CG2   . THR A 1 219 ? 142.080 178.139 158.286 1.00 56.93  ? 221 THR B CG2   1 
ATOM   1695 N  N     . PRO A 1 220 ? 142.360 174.436 155.855 1.00 43.11  ? 222 PRO B N     1 
ATOM   1696 C  CA    . PRO A 1 220 ? 141.256 173.826 155.113 1.00 43.33  ? 222 PRO B CA    1 
ATOM   1697 C  C     . PRO A 1 220 ? 140.234 173.195 156.039 1.00 48.50  ? 222 PRO B C     1 
ATOM   1698 O  O     . PRO A 1 220 ? 140.566 172.626 157.081 1.00 57.19  ? 222 PRO B O     1 
ATOM   1699 C  CB    . PRO A 1 220 ? 141.949 172.769 154.252 1.00 47.25  ? 222 PRO B CB    1 
ATOM   1700 C  CG    . PRO A 1 220 ? 143.186 172.456 154.973 1.00 49.34  ? 222 PRO B CG    1 
ATOM   1701 C  CD    . PRO A 1 220 ? 143.624 173.718 155.646 1.00 49.70  ? 222 PRO B CD    1 
ATOM   1702 N  N     . THR A 1 221 ? 138.976 173.298 155.640 1.00 47.00  ? 223 THR B N     1 
ATOM   1703 C  CA    . THR A 1 221 ? 137.850 172.717 156.350 1.00 46.39  ? 223 THR B CA    1 
ATOM   1704 C  C     . THR A 1 221 ? 137.145 171.731 155.429 1.00 51.66  ? 223 THR B C     1 
ATOM   1705 O  O     . THR A 1 221 ? 137.545 171.527 154.282 1.00 62.34  ? 223 THR B O     1 
ATOM   1706 C  CB    . THR A 1 221 ? 136.886 173.804 156.830 1.00 48.59  ? 223 THR B CB    1 
ATOM   1707 O  OG1   . THR A 1 221 ? 136.355 174.503 155.700 1.00 54.75  ? 223 THR B OG1   1 
ATOM   1708 C  CG2   . THR A 1 221 ? 137.608 174.792 157.722 1.00 48.72  ? 223 THR B CG2   1 
ATOM   1709 N  N     . TYR A 1 222 ? 136.080 171.114 155.938 1.00 43.95  ? 224 TYR B N     1 
ATOM   1710 C  CA    . TYR A 1 222 ? 135.336 170.159 155.126 1.00 45.86  ? 224 TYR B CA    1 
ATOM   1711 C  C     . TYR A 1 222 ? 134.655 170.819 153.936 1.00 52.21  ? 224 TYR B C     1 
ATOM   1712 O  O     . TYR A 1 222 ? 134.325 170.127 152.965 1.00 60.51  ? 224 TYR B O     1 
ATOM   1713 C  CB    . TYR A 1 222 ? 134.303 169.429 155.980 1.00 46.85  ? 224 TYR B CB    1 
ATOM   1714 C  CG    . TYR A 1 222 ? 134.876 168.280 156.770 1.00 48.10  ? 224 TYR B CG    1 
ATOM   1715 C  CD1   . TYR A 1 222 ? 136.002 167.611 156.330 1.00 54.30  ? 224 TYR B CD1   1 
ATOM   1716 C  CD2   . TYR A 1 222 ? 134.291 167.865 157.952 1.00 47.24  ? 224 TYR B CD2   1 
ATOM   1717 C  CE1   . TYR A 1 222 ? 136.530 166.561 157.042 1.00 54.20  ? 224 TYR B CE1   1 
ATOM   1718 C  CE2   . TYR A 1 222 ? 134.813 166.814 158.672 1.00 47.17  ? 224 TYR B CE2   1 
ATOM   1719 C  CZ    . TYR A 1 222 ? 135.932 166.167 158.212 1.00 52.21  ? 224 TYR B CZ    1 
ATOM   1720 O  OH    . TYR A 1 222 ? 136.458 165.119 158.926 1.00 56.31  ? 224 TYR B OH    1 
ATOM   1721 N  N     . GLY A 1 223 ? 134.446 172.134 153.986 1.00 55.33  ? 225 GLY B N     1 
ATOM   1722 C  CA    . GLY A 1 223 ? 133.843 172.818 152.856 1.00 56.46  ? 225 GLY B CA    1 
ATOM   1723 C  C     . GLY A 1 223 ? 134.665 172.685 151.591 1.00 58.65  ? 225 GLY B C     1 
ATOM   1724 O  O     . GLY A 1 223 ? 134.130 172.405 150.518 1.00 64.14  ? 225 GLY B O     1 
ATOM   1725 N  N     . ASP A 1 224 ? 135.982 172.870 151.701 1.00 52.17  ? 226 ASP B N     1 
ATOM   1726 C  CA    . ASP A 1 224 ? 136.847 172.768 150.530 1.00 55.65  ? 226 ASP B CA    1 
ATOM   1727 C  C     . ASP A 1 224 ? 136.870 171.353 149.967 1.00 60.64  ? 226 ASP B C     1 
ATOM   1728 O  O     . ASP A 1 224 ? 136.853 171.161 148.743 1.00 67.16  ? 226 ASP B O     1 
ATOM   1729 C  CB    . ASP A 1 224 ? 138.256 173.223 150.888 1.00 58.72  ? 226 ASP B CB    1 
ATOM   1730 C  CG    . ASP A 1 224 ? 138.260 174.457 151.756 1.00 66.45  ? 226 ASP B CG    1 
ATOM   1731 O  OD1   . ASP A 1 224 ? 137.242 175.177 151.764 1.00 64.72  ? 226 ASP B OD1   1 
ATOM   1732 O  OD2   . ASP A 1 224 ? 139.279 174.708 152.433 1.00 68.83  ? 226 ASP B OD2   1 
ATOM   1733 N  N     . LEU A 1 225 ? 136.924 170.351 150.843 1.00 47.92  ? 227 LEU B N     1 
ATOM   1734 C  CA    . LEU A 1 225 ? 136.924 168.966 150.392 1.00 49.53  ? 227 LEU B CA    1 
ATOM   1735 C  C     . LEU A 1 225 ? 135.630 168.636 149.657 1.00 51.84  ? 227 LEU B C     1 
ATOM   1736 O  O     . LEU A 1 225 ? 135.645 168.080 148.547 1.00 56.10  ? 227 LEU B O     1 
ATOM   1737 C  CB    . LEU A 1 225 ? 137.124 168.039 151.592 1.00 49.33  ? 227 LEU B CB    1 
ATOM   1738 C  CG    . LEU A 1 225 ? 138.525 167.844 152.183 1.00 50.79  ? 227 LEU B CG    1 
ATOM   1739 C  CD1   . LEU A 1 225 ? 139.073 169.114 152.783 1.00 52.93  ? 227 LEU B CD1   1 
ATOM   1740 C  CD2   . LEU A 1 225 ? 138.503 166.742 153.223 1.00 48.64  ? 227 LEU B CD2   1 
ATOM   1741 N  N     . ASN A 1 226 ? 134.495 168.984 150.266 1.00 42.59  ? 228 ASN B N     1 
ATOM   1742 C  CA    . ASN A 1 226 ? 133.209 168.765 149.622 1.00 40.99  ? 228 ASN B CA    1 
ATOM   1743 C  C     . ASN A 1 226 ? 133.101 169.541 148.321 1.00 50.77  ? 228 ASN B C     1 
ATOM   1744 O  O     . ASN A 1 226 ? 132.462 169.079 147.372 1.00 57.90  ? 228 ASN B O     1 
ATOM   1745 C  CB    . ASN A 1 226 ? 132.082 169.150 150.574 1.00 43.87  ? 228 ASN B CB    1 
ATOM   1746 C  CG    . ASN A 1 226 ? 132.126 168.372 151.861 1.00 45.53  ? 228 ASN B CG    1 
ATOM   1747 O  OD1   . ASN A 1 226 ? 133.034 167.580 152.083 1.00 45.53  ? 228 ASN B OD1   1 
ATOM   1748 N  ND2   . ASN A 1 226 ? 131.153 168.603 152.727 1.00 50.83  ? 228 ASN B ND2   1 
ATOM   1749 N  N     . HIS A 1 227 ? 133.733 170.708 148.253 1.00 49.67  ? 229 HIS B N     1 
ATOM   1750 C  CA    . HIS A 1 227 ? 133.716 171.517 147.044 1.00 47.74  ? 229 HIS B CA    1 
ATOM   1751 C  C     . HIS A 1 227 ? 134.482 170.842 145.909 1.00 49.77  ? 229 HIS B C     1 
ATOM   1752 O  O     . HIS A 1 227 ? 134.010 170.811 144.766 1.00 59.58  ? 229 HIS B O     1 
ATOM   1753 C  CB    . HIS A 1 227 ? 134.291 172.885 147.392 1.00 51.50  ? 229 HIS B CB    1 
ATOM   1754 C  CG    . HIS A 1 227 ? 134.182 173.908 146.308 1.00 56.04  ? 229 HIS B CG    1 
ATOM   1755 N  ND1   . HIS A 1 227 ? 134.280 175.258 146.565 1.00 54.44  ? 229 HIS B ND1   1 
ATOM   1756 C  CD2   . HIS A 1 227 ? 134.022 173.791 144.971 1.00 58.67  ? 229 HIS B CD2   1 
ATOM   1757 C  CE1   . HIS A 1 227 ? 134.172 175.929 145.435 1.00 59.03  ? 229 HIS B CE1   1 
ATOM   1758 N  NE2   . HIS A 1 227 ? 134.014 175.062 144.453 1.00 64.49  ? 229 HIS B NE2   1 
ATOM   1759 N  N     . LEU A 1 228 ? 135.654 170.279 146.208 1.00 40.79  ? 230 LEU B N     1 
ATOM   1760 C  CA    . LEU A 1 228 ? 136.395 169.520 145.201 1.00 44.37  ? 230 LEU B CA    1 
ATOM   1761 C  C     . LEU A 1 228 ? 135.583 168.328 144.705 1.00 49.12  ? 230 LEU B C     1 
ATOM   1762 O  O     . LEU A 1 228 ? 135.494 168.068 143.492 1.00 54.89  ? 230 LEU B O     1 
ATOM   1763 C  CB    . LEU A 1 228 ? 137.725 169.045 145.782 1.00 45.60  ? 230 LEU B CB    1 
ATOM   1764 C  CG    . LEU A 1 228 ? 138.849 170.064 145.919 1.00 46.79  ? 230 LEU B CG    1 
ATOM   1765 C  CD1   . LEU A 1 228 ? 139.986 169.481 146.720 1.00 51.16  ? 230 LEU B CD1   1 
ATOM   1766 C  CD2   . LEU A 1 228 ? 139.334 170.492 144.553 1.00 50.44  ? 230 LEU B CD2   1 
ATOM   1767 N  N     . VAL A 1 229 ? 134.980 167.592 145.637 1.00 47.12  ? 231 VAL B N     1 
ATOM   1768 C  CA    . VAL A 1 229 ? 134.194 166.425 145.249 1.00 47.63  ? 231 VAL B CA    1 
ATOM   1769 C  C     . VAL A 1 229 ? 133.009 166.840 144.385 1.00 49.91  ? 231 VAL B C     1 
ATOM   1770 O  O     . VAL A 1 229 ? 132.677 166.174 143.398 1.00 56.29  ? 231 VAL B O     1 
ATOM   1771 C  CB    . VAL A 1 229 ? 133.748 165.644 146.497 1.00 48.76  ? 231 VAL B CB    1 
ATOM   1772 C  CG1   . VAL A 1 229 ? 132.898 164.462 146.103 1.00 45.82  ? 231 VAL B CG1   1 
ATOM   1773 C  CG2   . VAL A 1 229 ? 134.952 165.184 147.288 1.00 47.85  ? 231 VAL B CG2   1 
ATOM   1774 N  N     . SER A 1 230 ? 132.354 167.947 144.740 1.00 43.54  ? 232 SER B N     1 
ATOM   1775 C  CA    . SER A 1 230 ? 131.223 168.431 143.957 1.00 41.78  ? 232 SER B CA    1 
ATOM   1776 C  C     . SER A 1 230 ? 131.658 168.858 142.563 1.00 47.27  ? 232 SER B C     1 
ATOM   1777 O  O     . SER A 1 230 ? 130.928 168.648 141.586 1.00 53.82  ? 232 SER B O     1 
ATOM   1778 C  CB    . SER A 1 230 ? 130.545 169.583 144.687 1.00 47.09  ? 232 SER B CB    1 
ATOM   1779 O  OG    . SER A 1 230 ? 131.440 170.661 144.877 1.00 56.53  ? 232 SER B OG    1 
ATOM   1780 N  N     . ALA A 1 231 ? 132.841 169.460 142.449 1.00 48.10  ? 233 ALA B N     1 
ATOM   1781 C  CA    . ALA A 1 231 ? 133.355 169.825 141.135 1.00 46.72  ? 233 ALA B CA    1 
ATOM   1782 C  C     . ALA A 1 231 ? 133.534 168.594 140.257 1.00 48.87  ? 233 ALA B C     1 
ATOM   1783 O  O     . ALA A 1 231 ? 133.122 168.583 139.090 1.00 54.11  ? 233 ALA B O     1 
ATOM   1784 C  CB    . ALA A 1 231 ? 134.674 170.581 141.280 1.00 46.97  ? 233 ALA B CB    1 
ATOM   1785 N  N     . THR A 1 232 ? 134.121 167.530 140.808 1.00 48.21  ? 234 THR B N     1 
ATOM   1786 C  CA    . THR A 1 232 ? 134.303 166.332 139.986 1.00 47.11  ? 234 THR B CA    1 
ATOM   1787 C  C     . THR A 1 232 ? 132.964 165.668 139.656 1.00 46.07  ? 234 THR B C     1 
ATOM   1788 O  O     . THR A 1 232 ? 132.779 165.154 138.543 1.00 47.10  ? 234 THR B O     1 
ATOM   1789 C  CB    . THR A 1 232 ? 135.270 165.350 140.658 1.00 48.57  ? 234 THR B CB    1 
ATOM   1790 O  OG1   . THR A 1 232 ? 135.892 164.544 139.654 1.00 51.98  ? 234 THR B OG1   1 
ATOM   1791 C  CG2   . THR A 1 232 ? 134.569 164.434 141.639 1.00 51.56  ? 234 THR B CG2   1 
ATOM   1792 N  N     . MET A 1 233 ? 132.006 165.699 140.591 1.00 50.65  ? 235 MET B N     1 
ATOM   1793 C  CA    . MET A 1 233 ? 130.690 165.121 140.323 1.00 50.04  ? 235 MET B CA    1 
ATOM   1794 C  C     . MET A 1 233 ? 129.988 165.861 139.196 1.00 52.26  ? 235 MET B C     1 
ATOM   1795 O  O     . MET A 1 233 ? 129.358 165.242 138.332 1.00 55.20  ? 235 MET B O     1 
ATOM   1796 C  CB    . MET A 1 233 ? 129.823 165.153 141.581 1.00 48.54  ? 235 MET B CB    1 
ATOM   1797 C  CG    . MET A 1 233 ? 130.257 164.229 142.694 1.00 51.57  ? 235 MET B CG    1 
ATOM   1798 S  SD    . MET A 1 233 ? 129.266 164.451 144.181 1.00 70.34  ? 235 MET B SD    1 
ATOM   1799 C  CE    . MET A 1 233 ? 127.768 163.590 143.732 1.00 56.32  ? 235 MET B CE    1 
ATOM   1800 N  N     . SER A 1 234 ? 130.071 167.191 139.200 1.00 49.50  ? 236 SER B N     1 
ATOM   1801 C  CA    . SER A 1 234 ? 129.488 167.971 138.117 1.00 43.98  ? 236 SER B CA    1 
ATOM   1802 C  C     . SER A 1 234 ? 130.195 167.691 136.801 1.00 44.16  ? 236 SER B C     1 
ATOM   1803 O  O     . SER A 1 234 ? 129.556 167.625 135.746 1.00 50.38  ? 236 SER B O     1 
ATOM   1804 C  CB    . SER A 1 234 ? 129.548 169.458 138.451 1.00 50.32  ? 236 SER B CB    1 
ATOM   1805 O  OG    . SER A 1 234 ? 129.201 170.241 137.326 1.00 51.72  ? 236 SER B OG    1 
ATOM   1806 N  N     . GLY A 1 235 ? 131.518 167.527 136.840 1.00 51.18  ? 237 GLY B N     1 
ATOM   1807 C  CA    . GLY A 1 235 ? 132.256 167.306 135.610 1.00 51.40  ? 237 GLY B CA    1 
ATOM   1808 C  C     . GLY A 1 235 ? 132.015 165.950 134.979 1.00 49.83  ? 237 GLY B C     1 
ATOM   1809 O  O     . GLY A 1 235 ? 132.168 165.797 133.765 1.00 50.58  ? 237 GLY B O     1 
ATOM   1810 N  N     . VAL A 1 236 ? 131.639 164.949 135.779 1.00 50.90  ? 238 VAL B N     1 
ATOM   1811 C  CA    . VAL A 1 236 ? 131.453 163.607 135.226 1.00 41.39  ? 238 VAL B CA    1 
ATOM   1812 C  C     . VAL A 1 236 ? 130.322 163.588 134.203 1.00 44.44  ? 238 VAL B C     1 
ATOM   1813 O  O     . VAL A 1 236 ? 130.438 162.965 133.142 1.00 51.59  ? 238 VAL B O     1 
ATOM   1814 C  CB    . VAL A 1 236 ? 131.216 162.587 136.355 1.00 48.37  ? 238 VAL B CB    1 
ATOM   1815 C  CG1   . VAL A 1 236 ? 130.493 161.367 135.831 1.00 47.78  ? 238 VAL B CG1   1 
ATOM   1816 C  CG2   . VAL A 1 236 ? 132.535 162.188 136.982 1.00 49.51  ? 238 VAL B CG2   1 
ATOM   1817 N  N     . THR A 1 237 ? 129.222 164.279 134.488 1.00 47.62  ? 239 THR B N     1 
ATOM   1818 C  CA    . THR A 1 237 ? 128.016 164.215 133.666 1.00 46.29  ? 239 THR B CA    1 
ATOM   1819 C  C     . THR A 1 237 ? 127.717 165.534 132.958 1.00 48.29  ? 239 THR B C     1 
ATOM   1820 O  O     . THR A 1 237 ? 126.563 165.951 132.859 1.00 51.09  ? 239 THR B O     1 
ATOM   1821 C  CB    . THR A 1 237 ? 126.816 163.797 134.509 1.00 54.51  ? 239 THR B CB    1 
ATOM   1822 O  OG1   . THR A 1 237 ? 125.612 163.983 133.756 1.00 54.40  ? 239 THR B OG1   1 
ATOM   1823 C  CG2   . THR A 1 237 ? 126.745 164.629 135.768 1.00 52.26  ? 239 THR B CG2   1 
ATOM   1824 N  N     . THR A 1 238 ? 128.748 166.200 132.443 1.00 50.92  ? 240 THR B N     1 
ATOM   1825 C  CA    . THR A 1 238 ? 128.550 167.464 131.748 1.00 44.36  ? 240 THR B CA    1 
ATOM   1826 C  C     . THR A 1 238 ? 127.956 167.292 130.360 1.00 44.72  ? 240 THR B C     1 
ATOM   1827 O  O     . THR A 1 238 ? 127.339 168.229 129.846 1.00 52.74  ? 240 THR B O     1 
ATOM   1828 C  CB    . THR A 1 238 ? 129.870 168.222 131.635 1.00 47.44  ? 240 THR B CB    1 
ATOM   1829 O  OG1   . THR A 1 238 ? 129.660 169.438 130.910 1.00 53.63  ? 240 THR B OG1   1 
ATOM   1830 C  CG2   . THR A 1 238 ? 130.901 167.388 130.910 1.00 50.21  ? 240 THR B CG2   1 
ATOM   1831 N  N     . CYS A 1 239 ? 128.128 166.127 129.741 1.00 49.56  ? 241 CYS B N     1 
ATOM   1832 C  CA    . CYS A 1 239 ? 127.636 165.906 128.391 1.00 49.76  ? 241 CYS B CA    1 
ATOM   1833 C  C     . CYS A 1 239 ? 126.174 165.495 128.354 1.00 52.74  ? 241 CYS B C     1 
ATOM   1834 O  O     . CYS A 1 239 ? 125.618 165.348 127.262 1.00 56.99  ? 241 CYS B O     1 
ATOM   1835 C  CB    . CYS A 1 239 ? 128.488 164.848 127.691 1.00 51.91  ? 241 CYS B CB    1 
ATOM   1836 S  SG    . CYS A 1 239 ? 130.148 165.401 127.267 1.00 67.73  ? 241 CYS B SG    1 
ATOM   1837 N  N     . LEU A 1 240 ? 125.545 165.299 129.508 1.00 50.03  ? 242 LEU B N     1 
ATOM   1838 C  CA    . LEU A 1 240 ? 124.125 164.989 129.562 1.00 46.17  ? 242 LEU B CA    1 
ATOM   1839 C  C     . LEU A 1 240 ? 123.247 166.229 129.531 1.00 51.78  ? 242 LEU B C     1 
ATOM   1840 O  O     . LEU A 1 240 ? 122.027 166.095 129.393 1.00 58.68  ? 242 LEU B O     1 
ATOM   1841 C  CB    . LEU A 1 240 ? 123.809 164.183 130.820 1.00 49.64  ? 242 LEU B CB    1 
ATOM   1842 C  CG    . LEU A 1 240 ? 123.828 162.666 130.695 1.00 47.62  ? 242 LEU B CG    1 
ATOM   1843 C  CD1   . LEU A 1 240 ? 123.431 162.028 132.000 1.00 49.60  ? 242 LEU B CD1   1 
ATOM   1844 C  CD2   . LEU A 1 240 ? 122.898 162.236 129.588 1.00 49.51  ? 242 LEU B CD2   1 
ATOM   1845 N  N     . ARG A 1 241 ? 123.822 167.426 129.655 1.00 46.67  ? 243 ARG B N     1 
ATOM   1846 C  CA    . ARG A 1 241 ? 123.009 168.631 129.693 1.00 46.26  ? 243 ARG B CA    1 
ATOM   1847 C  C     . ARG A 1 241 ? 123.557 169.799 128.889 1.00 47.25  ? 243 ARG B C     1 
ATOM   1848 O  O     . ARG A 1 241 ? 122.950 170.873 128.920 1.00 53.97  ? 243 ARG B O     1 
ATOM   1849 C  CB    . ARG A 1 241 ? 122.798 169.082 131.140 1.00 45.27  ? 243 ARG B CB    1 
ATOM   1850 C  CG    . ARG A 1 241 ? 123.980 168.855 132.024 1.00 45.31  ? 243 ARG B CG    1 
ATOM   1851 C  CD    . ARG A 1 241 ? 123.576 168.948 133.466 1.00 47.33  ? 243 ARG B CD    1 
ATOM   1852 N  NE    . ARG A 1 241 ? 124.640 168.488 134.344 1.00 41.56  ? 243 ARG B NE    1 
ATOM   1853 C  CZ    . ARG A 1 241 ? 125.672 169.229 134.712 1.00 44.42  ? 243 ARG B CZ    1 
ATOM   1854 N  NH1   . ARG A 1 241 ? 125.813 170.473 134.292 1.00 49.15  ? 243 ARG B NH1   1 
ATOM   1855 N  NH2   . ARG A 1 241 ? 126.586 168.709 135.523 1.00 48.04  ? 243 ARG B NH2   1 
ATOM   1856 N  N     . PHE A 1 242 ? 124.661 169.639 128.176 1.00 44.77  ? 244 PHE B N     1 
ATOM   1857 C  CA    . PHE A 1 242 ? 125.172 170.697 127.323 1.00 46.91  ? 244 PHE B CA    1 
ATOM   1858 C  C     . PHE A 1 242 ? 125.666 170.095 126.018 1.00 56.63  ? 244 PHE B C     1 
ATOM   1859 O  O     . PHE A 1 242 ? 126.052 168.921 125.980 1.00 58.42  ? 244 PHE B O     1 
ATOM   1860 C  CB    . PHE A 1 242 ? 126.308 171.472 128.005 1.00 48.75  ? 244 PHE B CB    1 
ATOM   1861 C  CG    . PHE A 1 242 ? 125.852 172.347 129.132 1.00 51.30  ? 244 PHE B CG    1 
ATOM   1862 C  CD1   . PHE A 1 242 ? 124.974 173.387 128.905 1.00 53.75  ? 244 PHE B CD1   1 
ATOM   1863 C  CD2   . PHE A 1 242 ? 126.313 172.141 130.415 1.00 46.67  ? 244 PHE B CD2   1 
ATOM   1864 C  CE1   . PHE A 1 242 ? 124.557 174.195 129.939 1.00 51.44  ? 244 PHE B CE1   1 
ATOM   1865 C  CE2   . PHE A 1 242 ? 125.898 172.946 131.446 1.00 44.63  ? 244 PHE B CE2   1 
ATOM   1866 C  CZ    . PHE A 1 242 ? 125.021 173.973 131.207 1.00 49.30  ? 244 PHE B CZ    1 
ATOM   1867 N  N     . PRO A 1 243 ? 125.663 170.870 124.933 1.00 47.63  ? 245 PRO B N     1 
ATOM   1868 C  CA    . PRO A 1 243 ? 126.179 170.360 123.657 1.00 40.61  ? 245 PRO B CA    1 
ATOM   1869 C  C     . PRO A 1 243 ? 127.692 170.227 123.639 1.00 47.51  ? 245 PRO B C     1 
ATOM   1870 O  O     . PRO A 1 243 ? 128.356 170.465 124.651 1.00 55.51  ? 245 PRO B O     1 
ATOM   1871 C  CB    . PRO A 1 243 ? 125.699 171.406 122.648 1.00 43.75  ? 245 PRO B CB    1 
ATOM   1872 C  CG    . PRO A 1 243 ? 125.531 172.638 123.443 1.00 45.88  ? 245 PRO B CG    1 
ATOM   1873 C  CD    . PRO A 1 243 ? 125.056 172.201 124.785 1.00 48.15  ? 245 PRO B CD    1 
ATOM   1874 N  N     . GLY A 1 244 ? 128.246 169.840 122.499 1.00 39.85  ? 246 GLY B N     1 
ATOM   1875 C  CA    . GLY A 1 244 ? 129.681 169.681 122.383 1.00 39.90  ? 246 GLY B CA    1 
ATOM   1876 C  C     . GLY A 1 244 ? 130.032 168.923 121.126 1.00 44.76  ? 246 GLY B C     1 
ATOM   1877 O  O     . GLY A 1 244 ? 129.171 168.371 120.437 1.00 52.95  ? 246 GLY B O     1 
ATOM   1878 N  N     . GLN A 1 245 ? 131.332 168.902 120.837 1.00 41.43  ? 247 GLN B N     1 
ATOM   1879 C  CA    . GLN A 1 245 ? 131.820 168.264 119.619 1.00 38.49  ? 247 GLN B CA    1 
ATOM   1880 C  C     . GLN A 1 245 ? 131.857 166.745 119.739 1.00 50.14  ? 247 GLN B C     1 
ATOM   1881 O  O     . GLN A 1 245 ? 131.591 166.039 118.761 1.00 55.81  ? 247 GLN B O     1 
ATOM   1882 C  CB    . GLN A 1 245 ? 133.198 168.815 119.268 1.00 48.16  ? 247 GLN B CB    1 
ATOM   1883 C  CG    . GLN A 1 245 ? 133.173 170.282 118.911 1.00 49.79  ? 247 GLN B CG    1 
ATOM   1884 C  CD    . GLN A 1 245 ? 134.509 170.955 119.104 1.00 58.71  ? 247 GLN B CD    1 
ATOM   1885 O  OE1   . GLN A 1 245 ? 135.200 170.715 120.091 1.00 59.33  ? 247 GLN B OE1   1 
ATOM   1886 N  NE2   . GLN A 1 245 ? 134.884 171.804 118.157 1.00 56.30  ? 247 GLN B NE2   1 
ATOM   1887 N  N     . LEU A 1 246 ? 132.191 166.223 120.915 1.00 50.68  ? 248 LEU B N     1 
ATOM   1888 C  CA    . LEU A 1 246 ? 132.136 164.794 121.195 1.00 41.15  ? 248 LEU B CA    1 
ATOM   1889 C  C     . LEU A 1 246 ? 131.326 164.582 122.459 1.00 45.73  ? 248 LEU B C     1 
ATOM   1890 O  O     . LEU A 1 246 ? 131.572 165.241 123.473 1.00 56.15  ? 248 LEU B O     1 
ATOM   1891 C  CB    . LEU A 1 246 ? 133.534 164.202 121.361 1.00 46.19  ? 248 LEU B CB    1 
ATOM   1892 C  CG    . LEU A 1 246 ? 134.072 163.358 120.213 1.00 46.31  ? 248 LEU B CG    1 
ATOM   1893 C  CD1   . LEU A 1 246 ? 135.541 163.067 120.421 1.00 48.33  ? 248 LEU B CD1   1 
ATOM   1894 C  CD2   . LEU A 1 246 ? 133.285 162.075 120.103 1.00 46.81  ? 248 LEU B CD2   1 
ATOM   1895 N  N     . ASN A 1 247 ? 130.372 163.662 122.408 1.00 44.37  ? 249 ASN B N     1 
ATOM   1896 C  CA    . ASN A 1 247 ? 129.456 163.433 123.514 1.00 46.01  ? 249 ASN B CA    1 
ATOM   1897 C  C     . ASN A 1 247 ? 129.721 162.071 124.137 1.00 49.31  ? 249 ASN B C     1 
ATOM   1898 O  O     . ASN A 1 247 ? 129.817 161.066 123.425 1.00 55.56  ? 249 ASN B O     1 
ATOM   1899 C  CB    . ASN A 1 247 ? 128.006 163.528 123.046 1.00 47.38  ? 249 ASN B CB    1 
ATOM   1900 C  CG    . ASN A 1 247 ? 127.580 164.951 122.772 1.00 53.02  ? 249 ASN B CG    1 
ATOM   1901 O  OD1   . ASN A 1 247 ? 128.006 165.878 123.454 1.00 58.07  ? 249 ASN B OD1   1 
ATOM   1902 N  ND2   . ASN A 1 247 ? 126.729 165.131 121.771 1.00 52.74  ? 249 ASN B ND2   1 
ATOM   1903 N  N     . ALA A 1 248 ? 129.839 162.041 125.461 1.00 44.98  ? 250 ALA B N     1 
ATOM   1904 C  CA    . ALA A 1 248 ? 129.999 160.803 126.207 1.00 49.98  ? 250 ALA B CA    1 
ATOM   1905 C  C     . ALA A 1 248 ? 128.997 160.769 127.349 1.00 51.47  ? 250 ALA B C     1 
ATOM   1906 O  O     . ALA A 1 248 ? 128.905 161.721 128.128 1.00 48.60  ? 250 ALA B O     1 
ATOM   1907 C  CB    . ALA A 1 248 ? 131.421 160.657 126.749 1.00 50.88  ? 250 ALA B CB    1 
ATOM   1908 N  N     . ASP A 1 249 ? 128.258 159.674 127.446 1.00 58.94  ? 251 ASP B N     1 
ATOM   1909 C  CA    . ASP A 1 249 ? 127.268 159.468 128.487 1.00 55.55  ? 251 ASP B CA    1 
ATOM   1910 C  C     . ASP A 1 249 ? 127.846 158.560 129.570 1.00 62.62  ? 251 ASP B C     1 
ATOM   1911 O  O     . ASP A 1 249 ? 129.028 158.209 129.557 1.00 67.44  ? 251 ASP B O     1 
ATOM   1912 C  CB    . ASP A 1 249 ? 125.990 158.888 127.879 1.00 56.85  ? 251 ASP B CB    1 
ATOM   1913 C  CG    . ASP A 1 249 ? 124.761 159.191 128.705 1.00 67.00  ? 251 ASP B CG    1 
ATOM   1914 O  OD1   . ASP A 1 249 ? 124.912 159.728 129.821 1.00 68.04  ? 251 ASP B OD1   1 
ATOM   1915 O  OD2   . ASP A 1 249 ? 123.642 158.897 128.234 1.00 70.02  ? 251 ASP B OD2   1 
ATOM   1916 N  N     . LEU A 1 250 ? 127.000 158.179 130.527 1.00 52.51  ? 252 LEU B N     1 
ATOM   1917 C  CA    . LEU A 1 250 ? 127.450 157.295 131.596 1.00 46.25  ? 252 LEU B CA    1 
ATOM   1918 C  C     . LEU A 1 250 ? 127.721 155.892 131.071 1.00 48.17  ? 252 LEU B C     1 
ATOM   1919 O  O     . LEU A 1 250 ? 128.743 155.277 131.403 1.00 58.44  ? 252 LEU B O     1 
ATOM   1920 C  CB    . LEU A 1 250 ? 126.412 157.260 132.714 1.00 49.86  ? 252 LEU B CB    1 
ATOM   1921 C  CG    . LEU A 1 250 ? 126.200 158.546 133.511 1.00 52.06  ? 252 LEU B CG    1 
ATOM   1922 C  CD1   . LEU A 1 250 ? 125.193 158.315 134.615 1.00 51.57  ? 252 LEU B CD1   1 
ATOM   1923 C  CD2   . LEU A 1 250 ? 127.503 159.061 134.084 1.00 50.74  ? 252 LEU B CD2   1 
ATOM   1924 N  N     . ARG A 1 251 ? 126.811 155.365 130.250 1.00 46.90  ? 253 ARG B N     1 
ATOM   1925 C  CA    . ARG A 1 251 ? 127.005 154.028 129.708 1.00 48.96  ? 253 ARG B CA    1 
ATOM   1926 C  C     . ARG A 1 251 ? 128.212 153.970 128.785 1.00 47.62  ? 253 ARG B C     1 
ATOM   1927 O  O     . ARG A 1 251 ? 128.905 152.951 128.739 1.00 53.98  ? 253 ARG B O     1 
ATOM   1928 C  CB    . ARG A 1 251 ? 125.751 153.570 128.974 1.00 46.70  ? 253 ARG B CB    1 
ATOM   1929 C  CG    . ARG A 1 251 ? 125.626 152.076 128.877 1.00 45.96  ? 253 ARG B CG    1 
ATOM   1930 C  CD    . ARG A 1 251 ? 124.307 151.688 128.268 1.00 46.84  ? 253 ARG B CD    1 
ATOM   1931 N  NE    . ARG A 1 251 ? 123.198 152.408 128.877 1.00 47.58  ? 253 ARG B NE    1 
ATOM   1932 C  CZ    . ARG A 1 251 ? 122.433 151.921 129.842 1.00 55.72  ? 253 ARG B CZ    1 
ATOM   1933 N  NH1   . ARG A 1 251 ? 122.623 150.706 130.326 1.00 56.04  ? 253 ARG B NH1   1 
ATOM   1934 N  NH2   . ARG A 1 251 ? 121.448 152.669 130.329 1.00 58.80  ? 253 ARG B NH2   1 
ATOM   1935 N  N     . LYS A 1 252 ? 128.477 155.047 128.045 1.00 38.68  ? 254 LYS B N     1 
ATOM   1936 C  CA    . LYS A 1 252 ? 129.663 155.108 127.197 1.00 40.69  ? 254 LYS B CA    1 
ATOM   1937 C  C     . LYS A 1 252 ? 130.932 154.999 128.028 1.00 48.87  ? 254 LYS B C     1 
ATOM   1938 O  O     . LYS A 1 252 ? 131.859 154.250 127.687 1.00 57.98  ? 254 LYS B O     1 
ATOM   1939 C  CB    . LYS A 1 252 ? 129.651 156.414 126.410 1.00 43.48  ? 254 LYS B CB    1 
ATOM   1940 C  CG    . LYS A 1 252 ? 130.241 156.345 125.028 1.00 49.06  ? 254 LYS B CG    1 
ATOM   1941 C  CD    . LYS A 1 252 ? 129.712 157.483 124.188 1.00 48.93  ? 254 LYS B CD    1 
ATOM   1942 C  CE    . LYS A 1 252 ? 130.365 157.528 122.830 1.00 48.30  ? 254 LYS B CE    1 
ATOM   1943 N  NZ    . LYS A 1 252 ? 129.792 158.608 121.989 1.00 47.49  ? 254 LYS B NZ    1 
ATOM   1944 N  N     . LEU A 1 253 ? 130.995 155.780 129.098 1.00 44.70  ? 255 LEU B N     1 
ATOM   1945 C  CA    . LEU A 1 253 ? 132.169 155.711 130.001 1.00 43.18  ? 255 LEU B CA    1 
ATOM   1946 C  C     . LEU A 1 253 ? 132.281 154.318 130.644 1.00 46.74  ? 255 LEU B C     1 
ATOM   1947 O  O     . LEU A 1 253 ? 133.405 153.846 130.760 1.00 52.73  ? 255 LEU B O     1 
ATOM   1948 C  CB    . LEU A 1 253 ? 132.100 156.823 131.045 1.00 45.25  ? 255 LEU B CB    1 
ATOM   1949 C  CG    . LEU A 1 253 ? 132.215 158.254 130.520 1.00 51.48  ? 255 LEU B CG    1 
ATOM   1950 C  CD1   . LEU A 1 253 ? 132.067 159.245 131.654 1.00 51.98  ? 255 LEU B CD1   1 
ATOM   1951 C  CD2   . LEU A 1 253 ? 133.539 158.442 129.814 1.00 46.50  ? 255 LEU B CD2   1 
ATOM   1952 N  N     . ALA A 1 254 ? 131.185 153.662 131.011 1.00 49.34  ? 256 ALA B N     1 
ATOM   1953 C  CA    . ALA A 1 254 ? 131.269 152.306 131.544 1.00 42.69  ? 256 ALA B CA    1 
ATOM   1954 C  C     . ALA A 1 254 ? 131.777 151.324 130.496 1.00 43.46  ? 256 ALA B C     1 
ATOM   1955 O  O     . ALA A 1 254 ? 132.596 150.451 130.801 1.00 50.15  ? 256 ALA B O     1 
ATOM   1956 C  CB    . ALA A 1 254 ? 129.909 151.863 132.081 1.00 46.04  ? 256 ALA B CB    1 
ATOM   1957 N  N     . VAL A 1 255 ? 131.296 151.443 129.258 1.00 36.22  ? 257 VAL B N     1 
ATOM   1958 C  CA    . VAL A 1 255 ? 131.699 150.512 128.207 1.00 37.98  ? 257 VAL B CA    1 
ATOM   1959 C  C     . VAL A 1 255 ? 133.181 150.659 127.906 1.00 40.95  ? 257 VAL B C     1 
ATOM   1960 O  O     . VAL A 1 255 ? 133.901 149.668 127.757 1.00 45.82  ? 257 VAL B O     1 
ATOM   1961 C  CB    . VAL A 1 255 ? 130.841 150.721 126.945 1.00 34.94  ? 257 VAL B CB    1 
ATOM   1962 C  CG1   . VAL A 1 255 ? 131.506 150.103 125.740 1.00 31.04  ? 257 VAL B CG1   1 
ATOM   1963 C  CG2   . VAL A 1 255 ? 129.461 150.134 127.140 1.00 43.52  ? 257 VAL B CG2   1 
ATOM   1964 N  N     . ASN A 1 256 ? 133.664 151.896 127.828 1.00 40.36  ? 258 ASN B N     1 
ATOM   1965 C  CA    . ASN A 1 256 ? 135.064 152.107 127.489 1.00 36.06  ? 258 ASN B CA    1 
ATOM   1966 C  C     . ASN A 1 256 ? 136.002 151.819 128.654 1.00 41.62  ? 258 ASN B C     1 
ATOM   1967 O  O     . ASN A 1 256 ? 137.155 151.442 128.428 1.00 46.56  ? 258 ASN B O     1 
ATOM   1968 C  CB    . ASN A 1 256 ? 135.267 153.536 126.996 1.00 36.99  ? 258 ASN B CB    1 
ATOM   1969 C  CG    . ASN A 1 256 ? 134.650 153.770 125.639 1.00 40.75  ? 258 ASN B CG    1 
ATOM   1970 O  OD1   . ASN A 1 256 ? 135.286 153.558 124.612 1.00 41.42  ? 258 ASN B OD1   1 
ATOM   1971 N  ND2   . ASN A 1 256 ? 133.400 154.198 125.628 1.00 41.52  ? 258 ASN B ND2   1 
ATOM   1972 N  N     . MET A 1 257 ? 135.542 151.979 129.894 1.00 43.95  ? 259 MET B N     1 
ATOM   1973 C  CA    . MET A 1 257 ? 136.438 151.937 131.043 1.00 40.26  ? 259 MET B CA    1 
ATOM   1974 C  C     . MET A 1 257 ? 136.458 150.602 131.775 1.00 46.75  ? 259 MET B C     1 
ATOM   1975 O  O     . MET A 1 257 ? 137.407 150.347 132.521 1.00 50.51  ? 259 MET B O     1 
ATOM   1976 C  CB    . MET A 1 257 ? 136.063 153.039 132.040 1.00 42.07  ? 259 MET B CB    1 
ATOM   1977 C  CG    . MET A 1 257 ? 136.428 154.433 131.585 1.00 43.77  ? 259 MET B CG    1 
ATOM   1978 S  SD    . MET A 1 257 ? 138.083 154.911 132.081 1.00 70.57  ? 259 MET B SD    1 
ATOM   1979 C  CE    . MET A 1 257 ? 137.965 154.732 133.855 1.00 44.19  ? 259 MET B CE    1 
ATOM   1980 N  N     . VAL A 1 258 ? 135.457 149.750 131.589 1.00 40.38  ? 260 VAL B N     1 
ATOM   1981 C  CA    . VAL A 1 258 ? 135.375 148.501 132.341 1.00 35.99  ? 260 VAL B CA    1 
ATOM   1982 C  C     . VAL A 1 258 ? 135.622 147.319 131.412 1.00 36.60  ? 260 VAL B C     1 
ATOM   1983 O  O     . VAL A 1 258 ? 134.723 146.925 130.658 1.00 47.65  ? 260 VAL B O     1 
ATOM   1984 C  CB    . VAL A 1 258 ? 134.019 148.371 133.048 1.00 40.25  ? 260 VAL B CB    1 
ATOM   1985 C  CG1   . VAL A 1 258 ? 133.941 147.074 133.809 1.00 37.69  ? 260 VAL B CG1   1 
ATOM   1986 C  CG2   . VAL A 1 258 ? 133.800 149.543 133.979 1.00 43.97  ? 260 VAL B CG2   1 
ATOM   1987 N  N     . PRO A 1 259 ? 136.812 146.731 131.428 1.00 30.82  ? 261 PRO B N     1 
ATOM   1988 C  CA    . PRO A 1 259 ? 137.079 145.581 130.557 1.00 30.93  ? 261 PRO B CA    1 
ATOM   1989 C  C     . PRO A 1 259 ? 136.473 144.288 131.075 1.00 42.93  ? 261 PRO B C     1 
ATOM   1990 O  O     . PRO A 1 259 ? 136.027 143.449 130.289 1.00 43.38  ? 261 PRO B O     1 
ATOM   1991 C  CB    . PRO A 1 259 ? 138.608 145.517 130.528 1.00 28.56  ? 261 PRO B CB    1 
ATOM   1992 C  CG    . PRO A 1 259 ? 139.032 146.154 131.781 1.00 36.18  ? 261 PRO B CG    1 
ATOM   1993 C  CD    . PRO A 1 259 ? 138.020 147.192 132.126 1.00 40.00  ? 261 PRO B CD    1 
ATOM   1994 N  N     . PHE A 1 260 ? 136.458 144.115 132.391 1.00 51.88  ? 262 PHE B N     1 
ATOM   1995 C  CA    . PHE A 1 260 ? 135.878 142.949 133.033 1.00 37.45  ? 262 PHE B CA    1 
ATOM   1996 C  C     . PHE A 1 260 ? 134.988 143.396 134.181 1.00 44.32  ? 262 PHE B C     1 
ATOM   1997 O  O     . PHE A 1 260 ? 135.262 144.417 134.817 1.00 54.19  ? 262 PHE B O     1 
ATOM   1998 C  CB    . PHE A 1 260 ? 136.972 142.008 133.547 1.00 36.78  ? 262 PHE B CB    1 
ATOM   1999 C  CG    . PHE A 1 260 ? 137.934 141.577 132.489 1.00 40.51  ? 262 PHE B CG    1 
ATOM   2000 C  CD1   . PHE A 1 260 ? 137.629 140.530 131.649 1.00 42.22  ? 262 PHE B CD1   1 
ATOM   2001 C  CD2   . PHE A 1 260 ? 139.142 142.223 132.329 1.00 44.99  ? 262 PHE B CD2   1 
ATOM   2002 C  CE1   . PHE A 1 260 ? 138.511 140.137 130.675 1.00 42.57  ? 262 PHE B CE1   1 
ATOM   2003 C  CE2   . PHE A 1 260 ? 140.024 141.832 131.354 1.00 45.06  ? 262 PHE B CE2   1 
ATOM   2004 C  CZ    . PHE A 1 260 ? 139.708 140.789 130.529 1.00 41.02  ? 262 PHE B CZ    1 
ATOM   2005 N  N     . PRO A 1 261 ? 133.923 142.644 134.474 1.00 34.82  ? 263 PRO B N     1 
ATOM   2006 C  CA    . PRO A 1 261 ? 132.863 143.185 135.344 1.00 35.73  ? 263 PRO B CA    1 
ATOM   2007 C  C     . PRO A 1 261 ? 133.327 143.619 136.724 1.00 43.60  ? 263 PRO B C     1 
ATOM   2008 O  O     . PRO A 1 261 ? 132.797 144.596 137.262 1.00 47.52  ? 263 PRO B O     1 
ATOM   2009 C  CB    . PRO A 1 261 ? 131.866 142.023 135.425 1.00 39.48  ? 263 PRO B CB    1 
ATOM   2010 C  CG    . PRO A 1 261 ? 132.114 141.232 134.210 1.00 33.74  ? 263 PRO B CG    1 
ATOM   2011 C  CD    . PRO A 1 261 ? 133.575 141.314 133.955 1.00 30.94  ? 263 PRO B CD    1 
ATOM   2012 N  N     . ARG A 1 262 ? 134.292 142.920 137.320 1.00 43.35  ? 264 ARG B N     1 
ATOM   2013 C  CA    . ARG A 1 262 ? 134.714 143.263 138.673 1.00 38.63  ? 264 ARG B CA    1 
ATOM   2014 C  C     . ARG A 1 262 ? 135.492 144.572 138.702 1.00 42.83  ? 264 ARG B C     1 
ATOM   2015 O  O     . ARG A 1 262 ? 135.377 145.347 139.657 1.00 50.58  ? 264 ARG B O     1 
ATOM   2016 C  CB    . ARG A 1 262 ? 135.559 142.138 139.262 1.00 44.60  ? 264 ARG B CB    1 
ATOM   2017 C  CG    . ARG A 1 262 ? 135.082 140.748 138.915 1.00 43.97  ? 264 ARG B CG    1 
ATOM   2018 C  CD    . ARG A 1 262 ? 133.934 140.315 139.792 1.00 38.26  ? 264 ARG B CD    1 
ATOM   2019 N  NE    . ARG A 1 262 ? 134.267 140.377 141.208 1.00 40.59  ? 264 ARG B NE    1 
ATOM   2020 C  CZ    . ARG A 1 262 ? 135.097 139.549 141.826 1.00 38.49  ? 264 ARG B CZ    1 
ATOM   2021 N  NH1   . ARG A 1 262 ? 135.701 138.566 141.182 1.00 43.33  ? 264 ARG B NH1   1 
ATOM   2022 N  NH2   . ARG A 1 262 ? 135.320 139.707 143.125 1.00 37.44  ? 264 ARG B NH2   1 
ATOM   2023 N  N     . LEU A 1 263 ? 136.283 144.835 137.670 1.00 37.62  ? 265 LEU B N     1 
ATOM   2024 C  CA    . LEU A 1 263 ? 137.217 145.958 137.663 1.00 40.28  ? 265 LEU B CA    1 
ATOM   2025 C  C     . LEU A 1 263 ? 136.472 147.236 137.304 1.00 42.56  ? 265 LEU B C     1 
ATOM   2026 O  O     . LEU A 1 263 ? 136.453 147.666 136.152 1.00 47.67  ? 265 LEU B O     1 
ATOM   2027 C  CB    . LEU A 1 263 ? 138.353 145.682 136.689 1.00 42.64  ? 265 LEU B CB    1 
ATOM   2028 C  CG    . LEU A 1 263 ? 138.952 144.281 136.788 1.00 37.99  ? 265 LEU B CG    1 
ATOM   2029 C  CD1   . LEU A 1 263 ? 140.059 144.097 135.784 1.00 41.79  ? 265 LEU B CD1   1 
ATOM   2030 C  CD2   . LEU A 1 263 ? 139.461 144.039 138.189 1.00 41.37  ? 265 LEU B CD2   1 
ATOM   2031 N  N     . HIS A 1 264 ? 135.851 147.860 138.303 1.00 36.84  ? 266 HIS B N     1 
ATOM   2032 C  CA    . HIS A 1 264 ? 135.138 149.114 138.092 1.00 38.01  ? 266 HIS B CA    1 
ATOM   2033 C  C     . HIS A 1 264 ? 135.371 150.086 139.242 1.00 45.16  ? 266 HIS B C     1 
ATOM   2034 O  O     . HIS A 1 264 ? 134.442 150.748 139.711 1.00 49.12  ? 266 HIS B O     1 
ATOM   2035 C  CB    . HIS A 1 264 ? 133.646 148.867 137.886 1.00 36.64  ? 266 HIS B CB    1 
ATOM   2036 C  CG    . HIS A 1 264 ? 132.980 148.188 139.038 1.00 31.93  ? 266 HIS B CG    1 
ATOM   2037 N  ND1   . HIS A 1 264 ? 132.724 148.824 140.231 1.00 40.12  ? 266 HIS B ND1   1 
ATOM   2038 C  CD2   . HIS A 1 264 ? 132.504 146.930 139.174 1.00 30.59  ? 266 HIS B CD2   1 
ATOM   2039 C  CE1   . HIS A 1 264 ? 132.126 147.984 141.055 1.00 36.77  ? 266 HIS B CE1   1 
ATOM   2040 N  NE2   . HIS A 1 264 ? 131.983 146.828 140.438 1.00 30.70  ? 266 HIS B NE2   1 
ATOM   2041 N  N     . PHE A 1 265 ? 136.609 150.202 139.707 1.00 42.92  ? 267 PHE B N     1 
ATOM   2042 C  CA    . PHE A 1 265 ? 136.961 151.129 140.775 1.00 36.20  ? 267 PHE B CA    1 
ATOM   2043 C  C     . PHE A 1 265 ? 137.875 152.204 140.204 1.00 40.93  ? 267 PHE B C     1 
ATOM   2044 O  O     . PHE A 1 265 ? 138.933 151.892 139.651 1.00 47.36  ? 267 PHE B O     1 
ATOM   2045 C  CB    . PHE A 1 265 ? 137.626 150.392 141.934 1.00 42.84  ? 267 PHE B CB    1 
ATOM   2046 C  CG    . PHE A 1 265 ? 136.680 149.534 142.719 1.00 41.66  ? 267 PHE B CG    1 
ATOM   2047 C  CD1   . PHE A 1 265 ? 136.295 148.297 142.246 1.00 39.74  ? 267 PHE B CD1   1 
ATOM   2048 C  CD2   . PHE A 1 265 ? 136.166 149.970 143.918 1.00 43.03  ? 267 PHE B CD2   1 
ATOM   2049 C  CE1   . PHE A 1 265 ? 135.419 147.514 142.956 1.00 39.92  ? 267 PHE B CE1   1 
ATOM   2050 C  CE2   . PHE A 1 265 ? 135.293 149.188 144.630 1.00 43.88  ? 267 PHE B CE2   1 
ATOM   2051 C  CZ    . PHE A 1 265 ? 134.920 147.961 144.148 1.00 39.42  ? 267 PHE B CZ    1 
ATOM   2052 N  N     . PHE A 1 266 ? 137.470 153.465 140.344 1.00 42.25  ? 268 PHE B N     1 
ATOM   2053 C  CA    . PHE A 1 266 ? 138.118 154.577 139.666 1.00 34.73  ? 268 PHE B CA    1 
ATOM   2054 C  C     . PHE A 1 266 ? 138.649 155.600 140.659 1.00 38.76  ? 268 PHE B C     1 
ATOM   2055 O  O     . PHE A 1 266 ? 138.149 155.723 141.778 1.00 51.98  ? 268 PHE B O     1 
ATOM   2056 C  CB    . PHE A 1 266 ? 137.160 155.281 138.706 1.00 41.52  ? 268 PHE B CB    1 
ATOM   2057 C  CG    . PHE A 1 266 ? 136.497 154.368 137.727 1.00 42.14  ? 268 PHE B CG    1 
ATOM   2058 C  CD1   . PHE A 1 266 ? 137.185 153.320 137.162 1.00 42.61  ? 268 PHE B CD1   1 
ATOM   2059 C  CD2   . PHE A 1 266 ? 135.186 154.573 137.359 1.00 45.29  ? 268 PHE B CD2   1 
ATOM   2060 C  CE1   . PHE A 1 266 ? 136.576 152.488 136.262 1.00 42.83  ? 268 PHE B CE1   1 
ATOM   2061 C  CE2   . PHE A 1 266 ? 134.578 153.743 136.458 1.00 44.41  ? 268 PHE B CE2   1 
ATOM   2062 C  CZ    . PHE A 1 266 ? 135.275 152.701 135.909 1.00 43.77  ? 268 PHE B CZ    1 
ATOM   2063 N  N     . MET A 1 267 ? 139.661 156.339 140.226 1.00 35.60  ? 269 MET B N     1 
ATOM   2064 C  CA    . MET A 1 267 ? 140.226 157.444 140.997 1.00 46.39  ? 269 MET B CA    1 
ATOM   2065 C  C     . MET A 1 267 ? 140.027 158.755 140.251 1.00 47.02  ? 269 MET B C     1 
ATOM   2066 O  O     . MET A 1 267 ? 140.608 158.938 139.165 1.00 51.12  ? 269 MET B O     1 
ATOM   2067 C  CB    . MET A 1 267 ? 141.709 157.203 141.272 1.00 46.99  ? 269 MET B CB    1 
ATOM   2068 C  CG    . MET A 1 267 ? 142.436 156.476 140.166 1.00 48.27  ? 269 MET B CG    1 
ATOM   2069 S  SD    . MET A 1 267 ? 144.189 156.281 140.521 1.00 68.93  ? 269 MET B SD    1 
ATOM   2070 C  CE    . MET A 1 267 ? 144.113 155.386 142.066 1.00 54.35  ? 269 MET B CE    1 
ATOM   2071 N  N     . PRO A 1 268 ? 139.240 159.687 140.773 1.00 39.70  ? 270 PRO B N     1 
ATOM   2072 C  CA    . PRO A 1 268 ? 138.928 160.910 140.029 1.00 39.70  ? 270 PRO B CA    1 
ATOM   2073 C  C     . PRO A 1 268 ? 140.006 161.979 140.172 1.00 46.46  ? 270 PRO B C     1 
ATOM   2074 O  O     . PRO A 1 268 ? 140.919 161.887 140.991 1.00 49.95  ? 270 PRO B O     1 
ATOM   2075 C  CB    . PRO A 1 268 ? 137.610 161.366 140.655 1.00 43.25  ? 270 PRO B CB    1 
ATOM   2076 C  CG    . PRO A 1 268 ? 137.662 160.845 142.035 1.00 49.25  ? 270 PRO B CG    1 
ATOM   2077 C  CD    . PRO A 1 268 ? 138.429 159.559 141.992 1.00 47.07  ? 270 PRO B CD    1 
ATOM   2078 N  N     . GLY A 1 269 ? 139.871 163.011 139.346 1.00 47.41  ? 271 GLY B N     1 
ATOM   2079 C  CA    . GLY A 1 269 ? 140.790 164.137 139.331 1.00 41.72  ? 271 GLY B CA    1 
ATOM   2080 C  C     . GLY A 1 269 ? 140.151 165.312 138.624 1.00 45.00  ? 271 GLY B C     1 
ATOM   2081 O  O     . GLY A 1 269 ? 139.128 165.176 137.949 1.00 53.08  ? 271 GLY B O     1 
ATOM   2082 N  N     . PHE A 1 270 ? 140.767 166.481 138.793 1.00 43.10  ? 272 PHE B N     1 
ATOM   2083 C  CA    . PHE A 1 270 ? 140.225 167.713 138.235 1.00 40.67  ? 272 PHE B CA    1 
ATOM   2084 C  C     . PHE A 1 270 ? 141.358 168.664 137.879 1.00 45.29  ? 272 PHE B C     1 
ATOM   2085 O  O     . PHE A 1 270 ? 142.433 168.625 138.481 1.00 57.55  ? 272 PHE B O     1 
ATOM   2086 C  CB    . PHE A 1 270 ? 139.256 168.389 139.211 1.00 48.97  ? 272 PHE B CB    1 
ATOM   2087 C  CG    . PHE A 1 270 ? 138.624 169.643 138.678 1.00 46.89  ? 272 PHE B CG    1 
ATOM   2088 C  CD1   . PHE A 1 270 ? 137.590 169.585 137.765 1.00 51.19  ? 272 PHE B CD1   1 
ATOM   2089 C  CD2   . PHE A 1 270 ? 139.059 170.881 139.102 1.00 49.02  ? 272 PHE B CD2   1 
ATOM   2090 C  CE1   . PHE A 1 270 ? 137.011 170.739 137.283 1.00 49.39  ? 272 PHE B CE1   1 
ATOM   2091 C  CE2   . PHE A 1 270 ? 138.484 172.033 138.623 1.00 50.45  ? 272 PHE B CE2   1 
ATOM   2092 C  CZ    . PHE A 1 270 ? 137.459 171.961 137.711 1.00 47.71  ? 272 PHE B CZ    1 
ATOM   2093 N  N     . ALA A 1 271 ? 141.101 169.522 136.896 1.00 48.64  ? 273 ALA B N     1 
ATOM   2094 C  CA    . ALA A 1 271 ? 142.053 170.532 136.458 1.00 47.21  ? 273 ALA B CA    1 
ATOM   2095 C  C     . ALA A 1 271 ? 141.278 171.676 135.830 1.00 50.12  ? 273 ALA B C     1 
ATOM   2096 O  O     . ALA A 1 271 ? 140.240 171.439 135.204 1.00 56.81  ? 273 ALA B O     1 
ATOM   2097 C  CB    . ALA A 1 271 ? 143.057 169.952 135.455 1.00 46.30  ? 273 ALA B CB    1 
ATOM   2098 N  N     . PRO A 1 272 ? 141.748 172.921 135.965 1.00 44.85  ? 274 PRO B N     1 
ATOM   2099 C  CA    . PRO A 1 272 ? 142.959 173.374 136.650 1.00 46.00  ? 274 PRO B CA    1 
ATOM   2100 C  C     . PRO A 1 272 ? 142.778 173.541 138.145 1.00 55.42  ? 274 PRO B C     1 
ATOM   2101 O  O     . PRO A 1 272 ? 141.664 173.684 138.639 1.00 60.15  ? 274 PRO B O     1 
ATOM   2102 C  CB    . PRO A 1 272 ? 143.234 174.716 135.975 1.00 46.17  ? 274 PRO B CB    1 
ATOM   2103 C  CG    . PRO A 1 272 ? 141.873 175.252 135.705 1.00 43.26  ? 274 PRO B CG    1 
ATOM   2104 C  CD    . PRO A 1 272 ? 141.022 174.052 135.366 1.00 42.77  ? 274 PRO B CD    1 
ATOM   2105 N  N     . LEU A 1 273 ? 143.878 173.527 138.889 1.00 59.22  ? 275 LEU B N     1 
ATOM   2106 C  CA    . LEU A 1 273 ? 143.864 173.825 140.316 1.00 51.32  ? 275 LEU B CA    1 
ATOM   2107 C  C     . LEU A 1 273 ? 145.085 174.682 140.606 1.00 53.57  ? 275 LEU B C     1 
ATOM   2108 O  O     . LEU A 1 273 ? 146.217 174.198 140.525 1.00 59.87  ? 275 LEU B O     1 
ATOM   2109 C  CB    . LEU A 1 273 ? 143.876 172.550 141.152 1.00 52.94  ? 275 LEU B CB    1 
ATOM   2110 C  CG    . LEU A 1 273 ? 142.568 171.770 141.249 1.00 51.26  ? 275 LEU B CG    1 
ATOM   2111 C  CD1   . LEU A 1 273 ? 142.785 170.509 142.048 1.00 54.35  ? 275 LEU B CD1   1 
ATOM   2112 C  CD2   . LEU A 1 273 ? 141.480 172.607 141.873 1.00 52.26  ? 275 LEU B CD2   1 
ATOM   2113 N  N     . THR A 1 274 ? 144.861 175.953 140.911 1.00 54.95  ? 276 THR B N     1 
ATOM   2114 C  CA    . THR A 1 274 ? 145.925 176.877 141.255 1.00 53.36  ? 276 THR B CA    1 
ATOM   2115 C  C     . THR A 1 274 ? 145.534 177.622 142.519 1.00 55.79  ? 276 THR B C     1 
ATOM   2116 O  O     . THR A 1 274 ? 144.427 177.472 143.038 1.00 63.97  ? 276 THR B O     1 
ATOM   2117 C  CB    . THR A 1 274 ? 146.205 177.856 140.113 1.00 59.88  ? 276 THR B CB    1 
ATOM   2118 O  OG1   . THR A 1 274 ? 144.973 178.429 139.664 1.00 63.92  ? 276 THR B OG1   1 
ATOM   2119 C  CG2   . THR A 1 274 ? 146.865 177.136 138.964 1.00 63.56  ? 276 THR B CG2   1 
ATOM   2120 N  N     . SER A 1 275 ? 146.450 178.436 143.015 1.00 55.89  ? 277 SER B N     1 
ATOM   2121 C  CA    . SER A 1 275 ? 146.207 179.232 144.204 1.00 56.47  ? 277 SER B CA    1 
ATOM   2122 C  C     . SER A 1 275 ? 145.956 180.679 143.821 1.00 57.38  ? 277 SER B C     1 
ATOM   2123 O  O     . SER A 1 275 ? 146.510 181.187 142.843 1.00 67.01  ? 277 SER B O     1 
ATOM   2124 C  CB    . SER A 1 275 ? 147.391 179.152 145.166 1.00 61.48  ? 277 SER B CB    1 
ATOM   2125 O  OG    . SER A 1 275 ? 148.578 179.613 144.548 1.00 66.27  ? 277 SER B OG    1 
ATOM   2126 N  N     . ARG A 1 276 ? 145.093 181.334 144.589 1.00 61.67  ? 278 ARG B N     1 
ATOM   2127 C  CA    . ARG A 1 276 ? 144.926 182.770 144.445 1.00 62.46  ? 278 ARG B CA    1 
ATOM   2128 C  C     . ARG A 1 276 ? 146.268 183.454 144.650 1.00 67.40  ? 278 ARG B C     1 
ATOM   2129 O  O     . ARG A 1 276 ? 147.012 183.133 145.580 1.00 72.54  ? 278 ARG B O     1 
ATOM   2130 C  CB    . ARG A 1 276 ? 143.908 183.290 145.454 1.00 65.91  ? 278 ARG B CB    1 
ATOM   2131 C  CG    . ARG A 1 276 ? 142.496 182.802 145.224 1.00 69.62  ? 278 ARG B CG    1 
ATOM   2132 C  CD    . ARG A 1 276 ? 141.700 182.844 146.513 1.00 72.45  ? 278 ARG B CD    1 
ATOM   2133 N  NE    . ARG A 1 276 ? 140.262 182.787 146.280 1.00 76.21  ? 278 ARG B NE    1 
ATOM   2134 C  CZ    . ARG A 1 276 ? 139.452 183.835 146.344 1.00 74.28  ? 278 ARG B CZ    1 
ATOM   2135 N  NH1   . ARG A 1 276 ? 139.907 185.044 146.630 1.00 71.87  ? 278 ARG B NH1   1 
ATOM   2136 N  NH2   . ARG A 1 276 ? 138.153 183.665 146.119 1.00 72.14  ? 278 ARG B NH2   1 
ATOM   2137 N  N     . GLY A 1 277 ? 146.580 184.397 143.774 1.00 62.93  ? 279 GLY B N     1 
ATOM   2138 C  CA    . GLY A 1 277 ? 147.908 184.961 143.760 1.00 64.29  ? 279 GLY B CA    1 
ATOM   2139 C  C     . GLY A 1 277 ? 148.902 184.197 142.922 1.00 64.95  ? 279 GLY B C     1 
ATOM   2140 O  O     . GLY A 1 277 ? 150.087 184.544 142.924 1.00 69.21  ? 279 GLY B O     1 
ATOM   2141 N  N     . SER A 1 278 ? 148.460 183.162 142.209 1.00 64.71  ? 280 SER B N     1 
ATOM   2142 C  CA    . SER A 1 278 ? 149.333 182.459 141.280 1.00 64.11  ? 280 SER B CA    1 
ATOM   2143 C  C     . SER A 1 278 ? 148.648 182.163 139.951 1.00 64.48  ? 280 SER B C     1 
ATOM   2144 O  O     . SER A 1 278 ? 149.225 181.449 139.124 1.00 69.72  ? 280 SER B O     1 
ATOM   2145 C  CB    . SER A 1 278 ? 149.846 181.158 141.901 1.00 66.50  ? 280 SER B CB    1 
ATOM   2146 O  OG    . SER A 1 278 ? 150.653 180.442 140.984 1.00 69.54  ? 280 SER B OG    1 
ATOM   2147 N  N     . GLN A 1 279 ? 147.447 182.686 139.715 1.00 65.24  ? 281 GLN B N     1 
ATOM   2148 C  CA    . GLN A 1 279 ? 146.771 182.477 138.443 1.00 67.30  ? 281 GLN B CA    1 
ATOM   2149 C  C     . GLN A 1 279 ? 147.204 183.470 137.376 1.00 70.95  ? 281 GLN B C     1 
ATOM   2150 O  O     . GLN A 1 279 ? 147.077 183.176 136.182 1.00 72.84  ? 281 GLN B O     1 
ATOM   2151 C  CB    . GLN A 1 279 ? 145.254 182.558 138.624 1.00 65.61  ? 281 GLN B CB    1 
ATOM   2152 C  CG    . GLN A 1 279 ? 144.748 183.933 138.998 1.00 67.36  ? 281 GLN B CG    1 
ATOM   2153 C  CD    . GLN A 1 279 ? 143.258 184.076 138.788 1.00 72.94  ? 281 GLN B CD    1 
ATOM   2154 O  OE1   . GLN A 1 279 ? 142.552 183.090 138.579 1.00 71.39  ? 281 GLN B OE1   1 
ATOM   2155 N  NE2   . GLN A 1 279 ? 142.769 185.309 138.840 1.00 73.37  ? 281 GLN B NE2   1 
ATOM   2156 N  N     . GLN A 1 280 ? 147.708 184.638 137.773 1.00 70.54  ? 282 GLN B N     1 
ATOM   2157 C  CA    . GLN A 1 280 ? 148.167 185.619 136.800 1.00 67.95  ? 282 GLN B CA    1 
ATOM   2158 C  C     . GLN A 1 280 ? 149.453 185.193 136.112 1.00 68.66  ? 282 GLN B C     1 
ATOM   2159 O  O     . GLN A 1 280 ? 149.747 185.683 135.018 1.00 71.18  ? 282 GLN B O     1 
ATOM   2160 C  CB    . GLN A 1 280 ? 148.371 186.974 137.476 1.00 67.43  ? 282 GLN B CB    1 
ATOM   2161 C  CG    . GLN A 1 280 ? 147.094 187.619 137.977 1.00 70.59  ? 282 GLN B CG    1 
ATOM   2162 C  CD    . GLN A 1 280 ? 146.716 187.157 139.369 1.00 75.97  ? 282 GLN B CD    1 
ATOM   2163 O  OE1   . GLN A 1 280 ? 147.289 186.204 139.896 1.00 76.76  ? 282 GLN B OE1   1 
ATOM   2164 N  NE2   . GLN A 1 280 ? 145.747 187.834 139.974 1.00 72.42  ? 282 GLN B NE2   1 
ATOM   2165 N  N     . TYR A 1 281 ? 150.219 184.297 136.722 1.00 57.84  ? 283 TYR B N     1 
ATOM   2166 C  CA    . TYR A 1 281 ? 151.506 183.877 136.197 1.00 51.06  ? 283 TYR B CA    1 
ATOM   2167 C  C     . TYR A 1 281 ? 151.425 182.602 135.375 1.00 58.20  ? 283 TYR B C     1 
ATOM   2168 O  O     . TYR A 1 281 ? 152.463 182.092 134.948 1.00 63.11  ? 283 TYR B O     1 
ATOM   2169 C  CB    . TYR A 1 281 ? 152.497 183.683 137.344 1.00 54.40  ? 283 TYR B CB    1 
ATOM   2170 C  CG    . TYR A 1 281 ? 152.703 184.905 138.198 1.00 53.02  ? 283 TYR B CG    1 
ATOM   2171 C  CD1   . TYR A 1 281 ? 153.724 185.795 137.927 1.00 55.10  ? 283 TYR B CD1   1 
ATOM   2172 C  CD2   . TYR A 1 281 ? 151.883 185.165 139.279 1.00 55.87  ? 283 TYR B CD2   1 
ATOM   2173 C  CE1   . TYR A 1 281 ? 153.920 186.904 138.700 1.00 56.49  ? 283 TYR B CE1   1 
ATOM   2174 C  CE2   . TYR A 1 281 ? 152.072 186.276 140.058 1.00 57.73  ? 283 TYR B CE2   1 
ATOM   2175 C  CZ    . TYR A 1 281 ? 153.092 187.141 139.766 1.00 60.58  ? 283 TYR B CZ    1 
ATOM   2176 O  OH    . TYR A 1 281 ? 153.287 188.256 140.545 1.00 65.34  ? 283 TYR B OH    1 
ATOM   2177 N  N     . ARG A 1 282 ? 150.228 182.073 135.142 1.00 62.19  ? 284 ARG B N     1 
ATOM   2178 C  CA    . ARG A 1 282 ? 150.062 180.798 134.462 1.00 60.57  ? 284 ARG B CA    1 
ATOM   2179 C  C     . ARG A 1 282 ? 149.144 180.961 133.264 1.00 63.01  ? 284 ARG B C     1 
ATOM   2180 O  O     . ARG A 1 282 ? 148.073 181.563 133.376 1.00 67.70  ? 284 ARG B O     1 
ATOM   2181 C  CB    . ARG A 1 282 ? 149.491 179.742 135.410 1.00 66.65  ? 284 ARG B CB    1 
ATOM   2182 C  CG    . ARG A 1 282 ? 148.711 178.645 134.712 1.00 69.56  ? 284 ARG B CG    1 
ATOM   2183 C  CD    . ARG A 1 282 ? 147.977 177.780 135.708 1.00 69.54  ? 284 ARG B CD    1 
ATOM   2184 N  NE    . ARG A 1 282 ? 148.862 176.821 136.357 1.00 72.91  ? 284 ARG B NE    1 
ATOM   2185 C  CZ    . ARG A 1 282 ? 148.836 175.513 136.144 1.00 76.11  ? 284 ARG B CZ    1 
ATOM   2186 N  NH1   . ARG A 1 282 ? 147.977 174.967 135.299 1.00 72.31  ? 284 ARG B NH1   1 
ATOM   2187 N  NH2   . ARG A 1 282 ? 149.692 174.732 136.797 1.00 71.77  ? 284 ARG B NH2   1 
ATOM   2188 N  N     . ALA A 1 283 ? 149.561 180.422 132.126 1.00 62.94  ? 285 ALA B N     1 
ATOM   2189 C  CA    . ALA A 1 283 ? 148.720 180.376 130.942 1.00 61.70  ? 285 ALA B CA    1 
ATOM   2190 C  C     . ALA A 1 283 ? 147.901 179.097 130.948 1.00 67.11  ? 285 ALA B C     1 
ATOM   2191 O  O     . ALA A 1 283 ? 148.421 178.015 131.229 1.00 73.88  ? 285 ALA B O     1 
ATOM   2192 C  CB    . ALA A 1 283 ? 149.565 180.450 129.671 1.00 59.43  ? 285 ALA B CB    1 
ATOM   2193 N  N     . LEU A 1 284 ? 146.618 179.225 130.638 1.00 60.39  ? 286 LEU B N     1 
ATOM   2194 C  CA    . LEU A 1 284 ? 145.695 178.095 130.645 1.00 59.11  ? 286 LEU B CA    1 
ATOM   2195 C  C     . LEU A 1 284 ? 145.518 177.607 129.213 1.00 63.94  ? 286 LEU B C     1 
ATOM   2196 O  O     . LEU A 1 284 ? 144.796 178.216 128.421 1.00 65.68  ? 286 LEU B O     1 
ATOM   2197 C  CB    . LEU A 1 284 ? 144.365 178.492 131.270 1.00 57.69  ? 286 LEU B CB    1 
ATOM   2198 C  CG    . LEU A 1 284 ? 143.478 177.332 131.710 1.00 62.13  ? 286 LEU B CG    1 
ATOM   2199 C  CD1   . LEU A 1 284 ? 144.261 176.381 132.590 1.00 65.17  ? 286 LEU B CD1   1 
ATOM   2200 C  CD2   . LEU A 1 284 ? 142.250 177.849 132.436 1.00 62.82  ? 286 LEU B CD2   1 
ATOM   2201 N  N     . THR A 1 285 ? 146.182 176.502 128.883 1.00 59.72  ? 287 THR B N     1 
ATOM   2202 C  CA    . THR A 1 285 ? 146.058 175.857 127.587 1.00 54.46  ? 287 THR B CA    1 
ATOM   2203 C  C     . THR A 1 285 ? 145.806 174.370 127.794 1.00 58.19  ? 287 THR B C     1 
ATOM   2204 O  O     . THR A 1 285 ? 145.916 173.848 128.906 1.00 64.85  ? 287 THR B O     1 
ATOM   2205 C  CB    . THR A 1 285 ? 147.307 176.068 126.727 1.00 57.72  ? 287 THR B CB    1 
ATOM   2206 O  OG1   . THR A 1 285 ? 148.471 175.701 127.475 1.00 63.87  ? 287 THR B OG1   1 
ATOM   2207 C  CG2   . THR A 1 285 ? 147.423 177.518 126.307 1.00 58.45  ? 287 THR B CG2   1 
ATOM   2208 N  N     . VAL A 1 286 ? 145.447 173.689 126.702 1.00 51.03  ? 288 VAL B N     1 
ATOM   2209 C  CA    . VAL A 1 286 ? 145.222 172.243 126.771 1.00 52.49  ? 288 VAL B CA    1 
ATOM   2210 C  C     . VAL A 1 286 ? 146.442 171.496 127.288 1.00 59.50  ? 288 VAL B C     1 
ATOM   2211 O  O     . VAL A 1 286 ? 146.274 170.569 128.100 1.00 64.73  ? 288 VAL B O     1 
ATOM   2212 C  CB    . VAL A 1 286 ? 144.724 171.719 125.418 1.00 55.87  ? 288 VAL B CB    1 
ATOM   2213 C  CG1   . VAL A 1 286 ? 144.233 170.296 125.555 1.00 56.35  ? 288 VAL B CG1   1 
ATOM   2214 C  CG2   . VAL A 1 286 ? 143.623 172.604 124.884 1.00 54.23  ? 288 VAL B CG2   1 
ATOM   2215 N  N     . PRO A 1 287 ? 147.677 171.805 126.870 1.00 55.46  ? 289 PRO B N     1 
ATOM   2216 C  CA    . PRO A 1 287 ? 148.827 171.114 127.472 1.00 53.51  ? 289 PRO B CA    1 
ATOM   2217 C  C     . PRO A 1 287 ? 148.906 171.252 128.982 1.00 55.79  ? 289 PRO B C     1 
ATOM   2218 O  O     . PRO A 1 287 ? 149.296 170.294 129.656 1.00 63.28  ? 289 PRO B O     1 
ATOM   2219 C  CB    . PRO A 1 287 ? 150.021 171.773 126.777 1.00 54.14  ? 289 PRO B CB    1 
ATOM   2220 C  CG    . PRO A 1 287 ? 149.496 172.176 125.472 1.00 48.70  ? 289 PRO B CG    1 
ATOM   2221 C  CD    . PRO A 1 287 ? 148.091 172.608 125.706 1.00 50.72  ? 289 PRO B CD    1 
ATOM   2222 N  N     . GLU A 1 288 ? 148.547 172.411 129.538 1.00 52.83  ? 290 GLU B N     1 
ATOM   2223 C  CA    . GLU A 1 288 ? 148.599 172.577 130.988 1.00 52.52  ? 290 GLU B CA    1 
ATOM   2224 C  C     . GLU A 1 288 ? 147.581 171.687 131.688 1.00 56.21  ? 290 GLU B C     1 
ATOM   2225 O  O     . GLU A 1 288 ? 147.899 171.043 132.698 1.00 64.65  ? 290 GLU B O     1 
ATOM   2226 C  CB    . GLU A 1 288 ? 148.374 174.038 131.359 1.00 56.90  ? 290 GLU B CB    1 
ATOM   2227 C  CG    . GLU A 1 288 ? 149.476 174.963 130.895 1.00 59.58  ? 290 GLU B CG    1 
ATOM   2228 C  CD    . GLU A 1 288 ? 150.802 174.676 131.568 1.00 66.53  ? 290 GLU B CD    1 
ATOM   2229 O  OE1   . GLU A 1 288 ? 150.797 174.263 132.746 1.00 67.78  ? 290 GLU B OE1   1 
ATOM   2230 O  OE2   . GLU A 1 288 ? 151.852 174.864 130.918 1.00 66.32  ? 290 GLU B OE2   1 
ATOM   2231 N  N     . LEU A 1 289 ? 146.357 171.631 131.163 1.00 47.43  ? 291 LEU B N     1 
ATOM   2232 C  CA    . LEU A 1 289 ? 145.353 170.746 131.738 1.00 47.86  ? 291 LEU B CA    1 
ATOM   2233 C  C     . LEU A 1 289 ? 145.803 169.295 131.669 1.00 53.68  ? 291 LEU B C     1 
ATOM   2234 O  O     . LEU A 1 289 ? 145.670 168.548 132.646 1.00 58.70  ? 291 LEU B O     1 
ATOM   2235 C  CB    . LEU A 1 289 ? 144.023 170.921 131.012 1.00 47.72  ? 291 LEU B CB    1 
ATOM   2236 C  CG    . LEU A 1 289 ? 143.311 172.262 131.123 1.00 53.25  ? 291 LEU B CG    1 
ATOM   2237 C  CD1   . LEU A 1 289 ? 141.889 172.134 130.634 1.00 52.40  ? 291 LEU B CD1   1 
ATOM   2238 C  CD2   . LEU A 1 289 ? 143.340 172.758 132.552 1.00 56.36  ? 291 LEU B CD2   1 
ATOM   2239 N  N     . THR A 1 290 ? 146.342 168.879 130.522 1.00 51.75  ? 292 THR B N     1 
ATOM   2240 C  CA    . THR A 1 290 ? 146.797 167.499 130.383 1.00 47.72  ? 292 THR B CA    1 
ATOM   2241 C  C     . THR A 1 290 ? 147.941 167.195 131.339 1.00 51.72  ? 292 THR B C     1 
ATOM   2242 O  O     . THR A 1 290 ? 147.982 166.122 131.949 1.00 60.80  ? 292 THR B O     1 
ATOM   2243 C  CB    . THR A 1 290 ? 147.217 167.226 128.940 1.00 52.78  ? 292 THR B CB    1 
ATOM   2244 O  OG1   . THR A 1 290 ? 146.177 167.651 128.054 1.00 57.33  ? 292 THR B OG1   1 
ATOM   2245 C  CG2   . THR A 1 290 ? 147.462 165.753 128.735 1.00 55.74  ? 292 THR B CG2   1 
ATOM   2246 N  N     . GLN A 1 291 ? 148.879 168.129 131.485 1.00 50.48  ? 293 GLN B N     1 
ATOM   2247 C  CA    . GLN A 1 291 ? 150.004 167.920 132.385 1.00 49.44  ? 293 GLN B CA    1 
ATOM   2248 C  C     . GLN A 1 291 ? 149.540 167.785 133.825 1.00 52.68  ? 293 GLN B C     1 
ATOM   2249 O  O     . GLN A 1 291 ? 150.047 166.941 134.571 1.00 58.41  ? 293 GLN B O     1 
ATOM   2250 C  CB    . GLN A 1 291 ? 150.997 169.072 132.249 1.00 52.64  ? 293 GLN B CB    1 
ATOM   2251 C  CG    . GLN A 1 291 ? 152.422 168.718 132.615 1.00 57.82  ? 293 GLN B CG    1 
ATOM   2252 C  CD    . GLN A 1 291 ? 153.175 168.071 131.469 1.00 66.91  ? 293 GLN B CD    1 
ATOM   2253 O  OE1   . GLN A 1 291 ? 152.659 167.956 130.358 1.00 66.32  ? 293 GLN B OE1   1 
ATOM   2254 N  NE2   . GLN A 1 291 ? 154.404 167.643 131.736 1.00 61.86  ? 293 GLN B NE2   1 
ATOM   2255 N  N     . GLN A 1 292 ? 148.577 168.608 134.240 1.00 50.14  ? 294 GLN B N     1 
ATOM   2256 C  CA    . GLN A 1 292 ? 148.124 168.541 135.624 1.00 48.34  ? 294 GLN B CA    1 
ATOM   2257 C  C     . GLN A 1 292 ? 147.282 167.296 135.880 1.00 55.93  ? 294 GLN B C     1 
ATOM   2258 O  O     . GLN A 1 292 ? 147.344 166.718 136.970 1.00 58.81  ? 294 GLN B O     1 
ATOM   2259 C  CB    . GLN A 1 292 ? 147.339 169.795 135.988 1.00 48.67  ? 294 GLN B CB    1 
ATOM   2260 C  CG    . GLN A 1 292 ? 147.136 169.950 137.470 1.00 48.60  ? 294 GLN B CG    1 
ATOM   2261 C  CD    . GLN A 1 292 ? 146.508 171.264 137.833 1.00 51.87  ? 294 GLN B CD    1 
ATOM   2262 O  OE1   . GLN A 1 292 ? 146.285 171.552 139.005 1.00 56.21  ? 294 GLN B OE1   1 
ATOM   2263 N  NE2   . GLN A 1 292 ? 146.209 172.073 136.829 1.00 51.68  ? 294 GLN B NE2   1 
ATOM   2264 N  N     . MET A 1 293 ? 146.481 166.874 134.899 1.00 53.83  ? 295 MET B N     1 
ATOM   2265 C  CA    . MET A 1 293 ? 145.586 165.740 135.111 1.00 46.51  ? 295 MET B CA    1 
ATOM   2266 C  C     . MET A 1 293 ? 146.356 164.459 135.396 1.00 56.39  ? 295 MET B C     1 
ATOM   2267 O  O     . MET A 1 293 ? 146.008 163.710 136.314 1.00 59.96  ? 295 MET B O     1 
ATOM   2268 C  CB    . MET A 1 293 ? 144.692 165.540 133.893 1.00 48.02  ? 295 MET B CB    1 
ATOM   2269 C  CG    . MET A 1 293 ? 143.466 166.406 133.848 1.00 56.67  ? 295 MET B CG    1 
ATOM   2270 S  SD    . MET A 1 293 ? 142.882 166.547 132.154 1.00 72.72  ? 295 MET B SD    1 
ATOM   2271 C  CE    . MET A 1 293 ? 142.904 164.835 131.651 1.00 58.00  ? 295 MET B CE    1 
ATOM   2272 N  N     . PHE A 1 294 ? 147.403 164.186 134.621 1.00 49.62  ? 296 PHE B N     1 
ATOM   2273 C  CA    . PHE A 1 294 ? 148.152 162.945 134.740 1.00 51.68  ? 296 PHE B CA    1 
ATOM   2274 C  C     . PHE A 1 294 ? 149.272 163.035 135.764 1.00 54.76  ? 296 PHE B C     1 
ATOM   2275 O  O     . PHE A 1 294 ? 150.172 162.190 135.761 1.00 53.77  ? 296 PHE B O     1 
ATOM   2276 C  CB    . PHE A 1 294 ? 148.710 162.534 133.377 1.00 50.70  ? 296 PHE B CB    1 
ATOM   2277 C  CG    . PHE A 1 294 ? 147.667 162.026 132.429 1.00 50.02  ? 296 PHE B CG    1 
ATOM   2278 C  CD1   . PHE A 1 294 ? 146.978 162.897 131.614 1.00 51.66  ? 296 PHE B CD1   1 
ATOM   2279 C  CD2   . PHE A 1 294 ? 147.369 160.680 132.360 1.00 50.22  ? 296 PHE B CD2   1 
ATOM   2280 C  CE1   . PHE A 1 294 ? 146.017 162.436 130.748 1.00 49.05  ? 296 PHE B CE1   1 
ATOM   2281 C  CE2   . PHE A 1 294 ? 146.409 160.218 131.495 1.00 51.36  ? 296 PHE B CE2   1 
ATOM   2282 C  CZ    . PHE A 1 294 ? 145.733 161.098 130.689 1.00 48.72  ? 296 PHE B CZ    1 
ATOM   2283 N  N     . ASP A 1 295 ? 149.237 164.038 136.634 1.00 58.40  ? 297 ASP B N     1 
ATOM   2284 C  CA    . ASP A 1 295 ? 150.203 164.150 137.713 1.00 55.25  ? 297 ASP B CA    1 
ATOM   2285 C  C     . ASP A 1 295 ? 149.770 163.291 138.892 1.00 55.63  ? 297 ASP B C     1 
ATOM   2286 O  O     . ASP A 1 295 ? 148.585 163.219 139.224 1.00 56.99  ? 297 ASP B O     1 
ATOM   2287 C  CB    . ASP A 1 295 ? 150.351 165.606 138.147 1.00 54.87  ? 297 ASP B CB    1 
ATOM   2288 C  CG    . ASP A 1 295 ? 151.663 165.873 138.846 1.00 61.85  ? 297 ASP B CG    1 
ATOM   2289 O  OD1   . ASP A 1 295 ? 152.434 164.913 139.052 1.00 64.81  ? 297 ASP B OD1   1 
ATOM   2290 O  OD2   . ASP A 1 295 ? 151.927 167.044 139.190 1.00 63.55  ? 297 ASP B OD2   1 
ATOM   2291 N  N     . ALA A 1 296 ? 150.744 162.634 139.524 1.00 57.30  ? 298 ALA B N     1 
ATOM   2292 C  CA    . ALA A 1 296 ? 150.450 161.732 140.628 1.00 57.25  ? 298 ALA B CA    1 
ATOM   2293 C  C     . ALA A 1 296 ? 149.870 162.451 141.837 1.00 60.73  ? 298 ALA B C     1 
ATOM   2294 O  O     . ALA A 1 296 ? 149.123 161.839 142.606 1.00 62.23  ? 298 ALA B O     1 
ATOM   2295 C  CB    . ALA A 1 296 ? 151.713 160.977 141.033 1.00 55.57  ? 298 ALA B CB    1 
ATOM   2296 N  N     . LYS A 1 297 ? 150.187 163.731 142.020 1.00 59.14  ? 299 LYS B N     1 
ATOM   2297 C  CA    . LYS A 1 297 ? 149.765 164.484 143.191 1.00 51.97  ? 299 LYS B CA    1 
ATOM   2298 C  C     . LYS A 1 297 ? 148.480 165.266 142.956 1.00 55.23  ? 299 LYS B C     1 
ATOM   2299 O  O     . LYS A 1 297 ? 148.229 166.255 143.650 1.00 63.19  ? 299 LYS B O     1 
ATOM   2300 C  CB    . LYS A 1 297 ? 150.882 165.425 143.637 1.00 56.33  ? 299 LYS B CB    1 
ATOM   2301 C  CG    . LYS A 1 297 ? 151.331 166.397 142.567 1.00 57.38  ? 299 LYS B CG    1 
ATOM   2302 C  CD    . LYS A 1 297 ? 152.424 167.319 143.078 1.00 58.48  ? 299 LYS B CD    1 
ATOM   2303 C  CE    . LYS A 1 297 ? 153.636 166.533 143.548 1.00 62.75  ? 299 LYS B CE    1 
ATOM   2304 N  NZ    . LYS A 1 297 ? 154.716 167.428 144.049 1.00 61.40  ? 299 LYS B NZ    1 
ATOM   2305 N  N     . ASN A 1 298 ? 147.665 164.848 141.991 1.00 52.17  ? 300 ASN B N     1 
ATOM   2306 C  CA    . ASN A 1 298 ? 146.387 165.487 141.731 1.00 50.65  ? 300 ASN B CA    1 
ATOM   2307 C  C     . ASN A 1 298 ? 145.202 164.548 141.873 1.00 50.34  ? 300 ASN B C     1 
ATOM   2308 O  O     . ASN A 1 298 ? 144.062 165.020 141.873 1.00 56.27  ? 300 ASN B O     1 
ATOM   2309 C  CB    . ASN A 1 298 ? 146.370 166.101 140.323 1.00 51.29  ? 300 ASN B CB    1 
ATOM   2310 C  CG    . ASN A 1 298 ? 145.298 167.151 140.159 1.00 54.96  ? 300 ASN B CG    1 
ATOM   2311 O  OD1   . ASN A 1 298 ? 144.872 167.773 141.130 1.00 60.63  ? 300 ASN B OD1   1 
ATOM   2312 N  ND2   . ASN A 1 298 ? 144.851 167.352 138.930 1.00 50.85  ? 300 ASN B ND2   1 
ATOM   2313 N  N     . MET A 1 299 ? 145.432 163.246 141.993 1.00 43.93  ? 301 MET B N     1 
ATOM   2314 C  CA    . MET A 1 299 ? 144.340 162.304 142.170 1.00 49.26  ? 301 MET B CA    1 
ATOM   2315 C  C     . MET A 1 299 ? 143.728 162.450 143.556 1.00 51.76  ? 301 MET B C     1 
ATOM   2316 O  O     . MET A 1 299 ? 144.405 162.799 144.525 1.00 54.67  ? 301 MET B O     1 
ATOM   2317 C  CB    . MET A 1 299 ? 144.832 160.875 141.962 1.00 50.92  ? 301 MET B CB    1 
ATOM   2318 C  CG    . MET A 1 299 ? 145.793 160.710 140.806 1.00 53.49  ? 301 MET B CG    1 
ATOM   2319 S  SD    . MET A 1 299 ? 145.087 161.213 139.232 1.00 65.96  ? 301 MET B SD    1 
ATOM   2320 C  CE    . MET A 1 299 ? 146.443 160.849 138.128 1.00 55.58  ? 301 MET B CE    1 
ATOM   2321 N  N     . MET A 1 300 ? 142.431 162.177 143.644 1.00 51.08  ? 302 MET B N     1 
ATOM   2322 C  CA    . MET A 1 300 ? 141.696 162.279 144.895 1.00 49.31  ? 302 MET B CA    1 
ATOM   2323 C  C     . MET A 1 300 ? 141.681 160.977 145.679 1.00 51.12  ? 302 MET B C     1 
ATOM   2324 O  O     . MET A 1 300 ? 141.006 160.900 146.709 1.00 56.54  ? 302 MET B O     1 
ATOM   2325 C  CB    . MET A 1 300 ? 140.263 162.739 144.633 1.00 50.38  ? 302 MET B CB    1 
ATOM   2326 C  CG    . MET A 1 300 ? 140.158 164.124 144.039 1.00 49.28  ? 302 MET B CG    1 
ATOM   2327 S  SD    . MET A 1 300 ? 138.455 164.616 143.765 1.00 58.62  ? 302 MET B SD    1 
ATOM   2328 C  CE    . MET A 1 300 ? 138.689 166.189 142.956 1.00 52.71  ? 302 MET B CE    1 
ATOM   2329 N  N     . ALA A 1 301 ? 142.393 159.957 145.219 1.00 56.72  ? 303 ALA B N     1 
ATOM   2330 C  CA    . ALA A 1 301 ? 142.578 158.723 145.965 1.00 53.52  ? 303 ALA B CA    1 
ATOM   2331 C  C     . ALA A 1 301 ? 144.031 158.628 146.400 1.00 55.54  ? 303 ALA B C     1 
ATOM   2332 O  O     . ALA A 1 301 ? 144.935 159.017 145.656 1.00 59.87  ? 303 ALA B O     1 
ATOM   2333 C  CB    . ALA A 1 301 ? 142.193 157.503 145.132 1.00 54.32  ? 303 ALA B CB    1 
ATOM   2334 N  N     . ALA A 1 302 ? 144.254 158.118 147.610 1.00 59.62  ? 304 ALA B N     1 
ATOM   2335 C  CA    . ALA A 1 302 ? 145.590 158.082 148.202 1.00 60.72  ? 304 ALA B CA    1 
ATOM   2336 C  C     . ALA A 1 302 ? 146.381 156.885 147.672 1.00 61.19  ? 304 ALA B C     1 
ATOM   2337 O  O     . ALA A 1 302 ? 146.890 156.048 148.416 1.00 61.37  ? 304 ALA B O     1 
ATOM   2338 C  CB    . ALA A 1 302 ? 145.495 158.056 149.721 1.00 62.58  ? 304 ALA B CB    1 
ATOM   2339 N  N     . CYS A 1 303 ? 146.480 156.823 146.350 1.00 66.16  ? 305 CYS B N     1 
ATOM   2340 C  CA    . CYS A 1 303 ? 147.217 155.780 145.656 1.00 60.69  ? 305 CYS B CA    1 
ATOM   2341 C  C     . CYS A 1 303 ? 148.110 156.420 144.608 1.00 66.12  ? 305 CYS B C     1 
ATOM   2342 O  O     . CYS A 1 303 ? 147.737 157.421 143.990 1.00 71.61  ? 305 CYS B O     1 
ATOM   2343 C  CB    . CYS A 1 303 ? 146.274 154.775 144.995 1.00 58.16  ? 305 CYS B CB    1 
ATOM   2344 S  SG    . CYS A 1 303 ? 145.227 153.858 146.145 1.00 83.20  ? 305 CYS B SG    1 
ATOM   2345 N  N     . ASP A 1 304 ? 149.288 155.841 144.411 1.00 61.29  ? 306 ASP B N     1 
ATOM   2346 C  CA    . ASP A 1 304 ? 150.232 156.368 143.443 1.00 58.77  ? 306 ASP B CA    1 
ATOM   2347 C  C     . ASP A 1 304 ? 150.111 155.571 142.158 1.00 59.35  ? 306 ASP B C     1 
ATOM   2348 O  O     . ASP A 1 304 ? 150.418 154.370 142.157 1.00 64.18  ? 306 ASP B O     1 
ATOM   2349 C  CB    . ASP A 1 304 ? 151.655 156.298 143.987 1.00 60.60  ? 306 ASP B CB    1 
ATOM   2350 C  CG    . ASP A 1 304 ? 152.570 157.312 143.347 1.00 65.18  ? 306 ASP B CG    1 
ATOM   2351 O  OD1   . ASP A 1 304 ? 152.060 158.219 142.662 1.00 65.43  ? 306 ASP B OD1   1 
ATOM   2352 O  OD2   . ASP A 1 304 ? 153.800 157.206 143.530 1.00 66.83  ? 306 ASP B OD2   1 
ATOM   2353 N  N     . PRO A 1 305 ? 149.668 156.173 141.055 1.00 51.37  ? 307 PRO B N     1 
ATOM   2354 C  CA    . PRO A 1 305 ? 149.524 155.409 139.809 1.00 51.90  ? 307 PRO B CA    1 
ATOM   2355 C  C     . PRO A 1 305 ? 150.830 154.856 139.280 1.00 59.52  ? 307 PRO B C     1 
ATOM   2356 O  O     . PRO A 1 305 ? 150.802 153.958 138.431 1.00 65.31  ? 307 PRO B O     1 
ATOM   2357 C  CB    . PRO A 1 305 ? 148.920 156.432 138.841 1.00 56.88  ? 307 PRO B CB    1 
ATOM   2358 C  CG    . PRO A 1 305 ? 148.304 157.461 139.710 1.00 57.19  ? 307 PRO B CG    1 
ATOM   2359 C  CD    . PRO A 1 305 ? 149.182 157.551 140.911 1.00 54.78  ? 307 PRO B CD    1 
ATOM   2360 N  N     . ARG A 1 306 ? 151.974 155.369 139.736 1.00 63.35  ? 308 ARG B N     1 
ATOM   2361 C  CA    . ARG A 1 306 ? 153.255 154.828 139.305 1.00 57.69  ? 308 ARG B CA    1 
ATOM   2362 C  C     . ARG A 1 306 ? 153.494 153.417 139.826 1.00 57.64  ? 308 ARG B C     1 
ATOM   2363 O  O     . ARG A 1 306 ? 154.351 152.709 139.290 1.00 62.70  ? 308 ARG B O     1 
ATOM   2364 C  CB    . ARG A 1 306 ? 154.385 155.752 139.750 1.00 57.78  ? 308 ARG B CB    1 
ATOM   2365 C  CG    . ARG A 1 306 ? 154.569 156.970 138.868 1.00 58.93  ? 308 ARG B CG    1 
ATOM   2366 C  CD    . ARG A 1 306 ? 153.845 158.173 139.432 1.00 60.25  ? 308 ARG B CD    1 
ATOM   2367 N  NE    . ARG A 1 306 ? 154.393 158.589 140.716 1.00 65.79  ? 308 ARG B NE    1 
ATOM   2368 C  CZ    . ARG A 1 306 ? 155.395 159.445 140.861 1.00 66.33  ? 308 ARG B CZ    1 
ATOM   2369 N  NH1   . ARG A 1 306 ? 155.988 159.998 139.815 1.00 64.27  ? 308 ARG B NH1   1 
ATOM   2370 N  NH2   . ARG A 1 306 ? 155.811 159.756 142.085 1.00 63.82  ? 308 ARG B NH2   1 
ATOM   2371 N  N     . HIS A 1 307 ? 152.766 152.995 140.854 1.00 53.17  ? 309 HIS B N     1 
ATOM   2372 C  CA    . HIS A 1 307 ? 152.850 151.626 141.361 1.00 53.88  ? 309 HIS B CA    1 
ATOM   2373 C  C     . HIS A 1 307 ? 151.804 150.730 140.708 1.00 59.46  ? 309 HIS B C     1 
ATOM   2374 O  O     . HIS A 1 307 ? 151.042 150.041 141.380 1.00 66.30  ? 309 HIS B O     1 
ATOM   2375 C  CB    . HIS A 1 307 ? 152.694 151.624 142.875 1.00 58.77  ? 309 HIS B CB    1 
ATOM   2376 C  CG    . HIS A 1 307 ? 153.657 152.521 143.586 1.00 61.84  ? 309 HIS B CG    1 
ATOM   2377 N  ND1   . HIS A 1 307 ? 153.411 153.028 144.843 1.00 57.99  ? 309 HIS B ND1   1 
ATOM   2378 C  CD2   . HIS A 1 307 ? 154.867 153.002 143.217 1.00 62.00  ? 309 HIS B CD2   1 
ATOM   2379 C  CE1   . HIS A 1 307 ? 154.426 153.785 145.215 1.00 58.79  ? 309 HIS B CE1   1 
ATOM   2380 N  NE2   . HIS A 1 307 ? 155.322 153.786 144.247 1.00 59.77  ? 309 HIS B NE2   1 
ATOM   2381 N  N     . GLY A 1 308 ? 151.766 150.732 139.388 1.00 43.12  ? 310 GLY B N     1 
ATOM   2382 C  CA    . GLY A 1 308 ? 150.750 149.996 138.669 1.00 42.58  ? 310 GLY B CA    1 
ATOM   2383 C  C     . GLY A 1 308 ? 150.600 150.537 137.267 1.00 46.65  ? 310 GLY B C     1 
ATOM   2384 O  O     . GLY A 1 308 ? 151.231 151.518 136.880 1.00 54.57  ? 310 GLY B O     1 
ATOM   2385 N  N     . ARG A 1 309 ? 149.738 149.872 136.511 1.00 43.26  ? 311 ARG B N     1 
ATOM   2386 C  CA    . ARG A 1 309 ? 149.504 150.207 135.119 1.00 43.76  ? 311 ARG B CA    1 
ATOM   2387 C  C     . ARG A 1 309 ? 148.043 150.566 134.913 1.00 47.82  ? 311 ARG B C     1 
ATOM   2388 O  O     . ARG A 1 309 ? 147.149 149.903 135.443 1.00 58.26  ? 311 ARG B O     1 
ATOM   2389 C  CB    . ARG A 1 309 ? 149.894 149.050 134.196 1.00 47.55  ? 311 ARG B CB    1 
ATOM   2390 C  CG    . ARG A 1 309 ? 151.309 148.553 134.388 1.00 52.80  ? 311 ARG B CG    1 
ATOM   2391 C  CD    . ARG A 1 309 ? 151.517 147.206 133.729 1.00 52.35  ? 311 ARG B CD    1 
ATOM   2392 N  NE    . ARG A 1 309 ? 152.072 147.327 132.388 1.00 54.59  ? 311 ARG B NE    1 
ATOM   2393 C  CZ    . ARG A 1 309 ? 153.359 147.494 132.123 1.00 54.89  ? 311 ARG B CZ    1 
ATOM   2394 N  NH1   . ARG A 1 309 ? 154.260 147.565 133.089 1.00 53.53  ? 311 ARG B NH1   1 
ATOM   2395 N  NH2   . ARG A 1 309 ? 153.754 147.594 130.858 1.00 52.60  ? 311 ARG B NH2   1 
ATOM   2396 N  N     . TYR A 1 310 ? 147.810 151.627 134.148 1.00 45.68  ? 312 TYR B N     1 
ATOM   2397 C  CA    . TYR A 1 310 ? 146.455 152.004 133.787 1.00 43.27  ? 312 TYR B CA    1 
ATOM   2398 C  C     . TYR A 1 310 ? 145.846 150.971 132.853 1.00 45.22  ? 312 TYR B C     1 
ATOM   2399 O  O     . TYR A 1 310 ? 146.471 150.538 131.883 1.00 54.83  ? 312 TYR B O     1 
ATOM   2400 C  CB    . TYR A 1 310 ? 146.439 153.367 133.103 1.00 42.36  ? 312 TYR B CB    1 
ATOM   2401 C  CG    . TYR A 1 310 ? 146.668 154.543 134.013 1.00 45.11  ? 312 TYR B CG    1 
ATOM   2402 C  CD1   . TYR A 1 310 ? 145.692 154.959 134.895 1.00 44.50  ? 312 TYR B CD1   1 
ATOM   2403 C  CD2   . TYR A 1 310 ? 147.850 155.254 133.964 1.00 46.13  ? 312 TYR B CD2   1 
ATOM   2404 C  CE1   . TYR A 1 310 ? 145.897 156.036 135.715 1.00 44.11  ? 312 TYR B CE1   1 
ATOM   2405 C  CE2   . TYR A 1 310 ? 148.062 156.333 134.777 1.00 45.43  ? 312 TYR B CE2   1 
ATOM   2406 C  CZ    . TYR A 1 310 ? 147.083 156.721 135.651 1.00 46.25  ? 312 TYR B CZ    1 
ATOM   2407 O  OH    . TYR A 1 310 ? 147.292 157.803 136.469 1.00 51.05  ? 312 TYR B OH    1 
ATOM   2408 N  N     . LEU A 1 311 ? 144.611 150.583 133.145 1.00 38.31  ? 313 LEU B N     1 
ATOM   2409 C  CA    . LEU A 1 311 ? 143.833 149.775 132.222 1.00 37.17  ? 313 LEU B CA    1 
ATOM   2410 C  C     . LEU A 1 311 ? 143.065 150.642 131.235 1.00 42.61  ? 313 LEU B C     1 
ATOM   2411 O  O     . LEU A 1 311 ? 142.972 150.303 130.053 1.00 52.99  ? 313 LEU B O     1 
ATOM   2412 C  CB    . LEU A 1 311 ? 142.862 148.883 132.997 1.00 37.06  ? 313 LEU B CB    1 
ATOM   2413 C  CG    . LEU A 1 311 ? 143.259 147.441 133.283 1.00 35.16  ? 313 LEU B CG    1 
ATOM   2414 C  CD1   . LEU A 1 311 ? 144.513 147.393 134.117 1.00 41.24  ? 313 LEU B CD1   1 
ATOM   2415 C  CD2   . LEU A 1 311 ? 142.133 146.737 133.999 1.00 42.08  ? 313 LEU B CD2   1 
ATOM   2416 N  N     . THR A 1 312 ? 142.505 151.753 131.707 1.00 39.66  ? 314 THR B N     1 
ATOM   2417 C  CA    . THR A 1 312 ? 141.785 152.697 130.866 1.00 38.74  ? 314 THR B CA    1 
ATOM   2418 C  C     . THR A 1 312 ? 141.780 154.056 131.551 1.00 41.74  ? 314 THR B C     1 
ATOM   2419 O  O     . THR A 1 312 ? 141.873 154.144 132.775 1.00 51.62  ? 314 THR B O     1 
ATOM   2420 C  CB    . THR A 1 312 ? 140.351 152.234 130.592 1.00 44.12  ? 314 THR B CB    1 
ATOM   2421 O  OG1   . THR A 1 312 ? 140.339 150.832 130.308 1.00 48.28  ? 314 THR B OG1   1 
ATOM   2422 C  CG2   . THR A 1 312 ? 139.769 152.974 129.398 1.00 46.14  ? 314 THR B CG2   1 
ATOM   2423 N  N     . VAL A 1 313 ? 141.672 155.110 130.748 1.00 36.87  ? 315 VAL B N     1 
ATOM   2424 C  CA    . VAL A 1 313 ? 141.600 156.480 131.239 1.00 28.42  ? 315 VAL B CA    1 
ATOM   2425 C  C     . VAL A 1 313 ? 140.512 157.214 130.470 1.00 35.90  ? 315 VAL B C     1 
ATOM   2426 O  O     . VAL A 1 313 ? 140.392 157.061 129.252 1.00 48.07  ? 315 VAL B O     1 
ATOM   2427 C  CB    . VAL A 1 313 ? 142.959 157.194 131.104 1.00 34.66  ? 315 VAL B CB    1 
ATOM   2428 C  CG1   . VAL A 1 313 ? 142.780 158.692 131.040 1.00 43.79  ? 315 VAL B CG1   1 
ATOM   2429 C  CG2   . VAL A 1 313 ? 143.855 156.826 132.256 1.00 39.66  ? 315 VAL B CG2   1 
ATOM   2430 N  N     . ALA A 1 314 ? 139.706 158.000 131.182 1.00 34.29  ? 316 ALA B N     1 
ATOM   2431 C  CA    . ALA A 1 314 ? 138.661 158.819 130.584 1.00 31.39  ? 316 ALA B CA    1 
ATOM   2432 C  C     . ALA A 1 314 ? 138.928 160.282 130.894 1.00 44.36  ? 316 ALA B C     1 
ATOM   2433 O  O     . ALA A 1 314 ? 139.134 160.647 132.054 1.00 50.83  ? 316 ALA B O     1 
ATOM   2434 C  CB    . ALA A 1 314 ? 137.279 158.417 131.095 1.00 34.10  ? 316 ALA B CB    1 
ATOM   2435 N  N     . ALA A 1 315 ? 138.927 161.115 129.858 1.00 40.97  ? 317 ALA B N     1 
ATOM   2436 C  CA    . ALA A 1 315 ? 139.192 162.542 129.985 1.00 30.04  ? 317 ALA B CA    1 
ATOM   2437 C  C     . ALA A 1 315 ? 138.025 163.311 129.387 1.00 38.89  ? 317 ALA B C     1 
ATOM   2438 O  O     . ALA A 1 315 ? 137.713 163.149 128.204 1.00 44.13  ? 317 ALA B O     1 
ATOM   2439 C  CB    . ALA A 1 315 ? 140.499 162.918 129.292 1.00 32.90  ? 317 ALA B CB    1 
ATOM   2440 N  N     . VAL A 1 316 ? 137.384 164.145 130.199 1.00 39.15  ? 318 VAL B N     1 
ATOM   2441 C  CA    . VAL A 1 316 ? 136.217 164.913 129.784 1.00 31.91  ? 318 VAL B CA    1 
ATOM   2442 C  C     . VAL A 1 316 ? 136.594 166.385 129.811 1.00 36.94  ? 318 VAL B C     1 
ATOM   2443 O  O     . VAL A 1 316 ? 136.972 166.916 130.861 1.00 45.33  ? 318 VAL B O     1 
ATOM   2444 C  CB    . VAL A 1 316 ? 135.000 164.641 130.680 1.00 36.29  ? 318 VAL B CB    1 
ATOM   2445 C  CG1   . VAL A 1 316 ? 133.740 165.147 130.015 1.00 42.92  ? 318 VAL B CG1   1 
ATOM   2446 C  CG2   . VAL A 1 316 ? 134.881 163.163 130.985 1.00 33.73  ? 318 VAL B CG2   1 
ATOM   2447 N  N     . PHE A 1 317 ? 136.489 167.042 128.661 1.00 42.61  ? 319 PHE B N     1 
ATOM   2448 C  CA    . PHE A 1 317 ? 136.939 168.414 128.485 1.00 38.68  ? 319 PHE B CA    1 
ATOM   2449 C  C     . PHE A 1 317 ? 135.752 169.359 128.377 1.00 41.50  ? 319 PHE B C     1 
ATOM   2450 O  O     . PHE A 1 317 ? 134.709 169.014 127.819 1.00 49.93  ? 319 PHE B O     1 
ATOM   2451 C  CB    . PHE A 1 317 ? 137.805 168.547 127.232 1.00 38.10  ? 319 PHE B CB    1 
ATOM   2452 C  CG    . PHE A 1 317 ? 139.199 168.029 127.395 1.00 36.16  ? 319 PHE B CG    1 
ATOM   2453 C  CD1   . PHE A 1 317 ? 139.509 166.725 127.083 1.00 40.75  ? 319 PHE B CD1   1 
ATOM   2454 C  CD2   . PHE A 1 317 ? 140.205 168.856 127.841 1.00 39.83  ? 319 PHE B CD2   1 
ATOM   2455 C  CE1   . PHE A 1 317 ? 140.790 166.259 127.231 1.00 42.58  ? 319 PHE B CE1   1 
ATOM   2456 C  CE2   . PHE A 1 317 ? 141.484 168.391 127.988 1.00 36.91  ? 319 PHE B CE2   1 
ATOM   2457 C  CZ    . PHE A 1 317 ? 141.776 167.096 127.688 1.00 38.00  ? 319 PHE B CZ    1 
ATOM   2458 N  N     . ARG A 1 318 ? 135.925 170.564 128.914 1.00 46.73  ? 320 ARG B N     1 
ATOM   2459 C  CA    . ARG A 1 318 ? 134.905 171.601 128.862 1.00 43.37  ? 320 ARG B CA    1 
ATOM   2460 C  C     . ARG A 1 318 ? 135.521 172.886 128.337 1.00 43.56  ? 320 ARG B C     1 
ATOM   2461 O  O     . ARG A 1 318 ? 136.554 173.332 128.843 1.00 52.04  ? 320 ARG B O     1 
ATOM   2462 C  CB    . ARG A 1 318 ? 134.289 171.841 130.239 1.00 42.53  ? 320 ARG B CB    1 
ATOM   2463 C  CG    . ARG A 1 318 ? 133.714 170.606 130.881 1.00 45.11  ? 320 ARG B CG    1 
ATOM   2464 C  CD    . ARG A 1 318 ? 132.976 170.941 132.153 1.00 46.30  ? 320 ARG B CD    1 
ATOM   2465 N  NE    . ARG A 1 318 ? 131.856 171.840 131.916 1.00 50.13  ? 320 ARG B NE    1 
ATOM   2466 C  CZ    . ARG A 1 318 ? 130.968 172.182 132.837 1.00 51.31  ? 320 ARG B CZ    1 
ATOM   2467 N  NH1   . ARG A 1 318 ? 131.043 171.718 134.072 1.00 48.07  ? 320 ARG B NH1   1 
ATOM   2468 N  NH2   . ARG A 1 318 ? 129.978 173.006 132.509 1.00 50.63  ? 320 ARG B NH2   1 
ATOM   2469 N  N     . GLY A 1 319 ? 134.889 173.478 127.331 1.00 43.13  ? 321 GLY B N     1 
ATOM   2470 C  CA    . GLY A 1 319 ? 135.310 174.740 126.771 1.00 45.60  ? 321 GLY B CA    1 
ATOM   2471 C  C     . GLY A 1 319 ? 135.424 174.665 125.269 1.00 50.64  ? 321 GLY B C     1 
ATOM   2472 O  O     . GLY A 1 319 ? 134.982 173.706 124.630 1.00 53.06  ? 321 GLY B O     1 
ATOM   2473 N  N     . ARG A 1 320 ? 136.026 175.699 124.690 1.00 65.03  ? 322 ARG B N     1 
ATOM   2474 C  CA    . ARG A 1 320 ? 136.306 175.756 123.261 1.00 64.04  ? 322 ARG B CA    1 
ATOM   2475 C  C     . ARG A 1 320 ? 137.764 175.384 123.034 1.00 66.72  ? 322 ARG B C     1 
ATOM   2476 O  O     . ARG A 1 320 ? 138.666 176.044 123.558 1.00 67.96  ? 322 ARG B O     1 
ATOM   2477 C  CB    . ARG A 1 320 ? 136.018 177.145 122.696 1.00 62.22  ? 322 ARG B CB    1 
ATOM   2478 C  CG    . ARG A 1 320 ? 134.560 177.403 122.379 1.00 65.71  ? 322 ARG B CG    1 
ATOM   2479 C  CD    . ARG A 1 320 ? 134.277 178.890 122.264 1.00 67.70  ? 322 ARG B CD    1 
ATOM   2480 N  NE    . ARG A 1 320 ? 133.697 179.432 123.486 1.00 73.63  ? 322 ARG B NE    1 
ATOM   2481 C  CZ    . ARG A 1 320 ? 134.398 179.949 124.485 1.00 73.41  ? 322 ARG B CZ    1 
ATOM   2482 N  NH1   . ARG A 1 320 ? 135.719 180.017 124.440 1.00 69.93  ? 322 ARG B NH1   1 
ATOM   2483 N  NH2   . ARG A 1 320 ? 133.759 180.411 125.556 1.00 66.52  ? 322 ARG B NH2   1 
ATOM   2484 N  N     . MET A 1 321 ? 137.991 174.335 122.251 1.00 57.13  ? 323 MET B N     1 
ATOM   2485 C  CA    . MET A 1 321 ? 139.337 173.828 122.045 1.00 50.83  ? 323 MET B CA    1 
ATOM   2486 C  C     . MET A 1 321 ? 139.376 173.033 120.753 1.00 55.17  ? 323 MET B C     1 
ATOM   2487 O  O     . MET A 1 321 ? 138.345 172.594 120.239 1.00 58.11  ? 323 MET B O     1 
ATOM   2488 C  CB    . MET A 1 321 ? 139.788 172.966 123.225 1.00 53.41  ? 323 MET B CB    1 
ATOM   2489 C  CG    . MET A 1 321 ? 138.758 171.948 123.657 1.00 55.21  ? 323 MET B CG    1 
ATOM   2490 S  SD    . MET A 1 321 ? 138.978 171.458 125.371 1.00 66.47  ? 323 MET B SD    1 
ATOM   2491 C  CE    . MET A 1 321 ? 138.624 172.998 126.204 1.00 55.05  ? 323 MET B CE    1 
ATOM   2492 N  N     . SER A 1 322 ? 140.586 172.852 120.239 1.00 55.45  ? 324 SER B N     1 
ATOM   2493 C  CA    . SER A 1 322 ? 140.790 172.092 119.020 1.00 45.65  ? 324 SER B CA    1 
ATOM   2494 C  C     . SER A 1 322 ? 140.843 170.601 119.313 1.00 49.13  ? 324 SER B C     1 
ATOM   2495 O  O     . SER A 1 322 ? 141.347 170.167 120.351 1.00 59.82  ? 324 SER B O     1 
ATOM   2496 C  CB    . SER A 1 322 ? 142.080 172.524 118.334 1.00 51.03  ? 324 SER B CB    1 
ATOM   2497 O  OG    . SER A 1 322 ? 142.457 171.594 117.337 1.00 56.19  ? 324 SER B OG    1 
ATOM   2498 N  N     . MET A 1 323 ? 140.317 169.812 118.379 1.00 48.91  ? 325 MET B N     1 
ATOM   2499 C  CA    . MET A 1 323 ? 140.393 168.363 118.511 1.00 54.21  ? 325 MET B CA    1 
ATOM   2500 C  C     . MET A 1 323 ? 141.793 167.837 118.231 1.00 51.64  ? 325 MET B C     1 
ATOM   2501 O  O     . MET A 1 323 ? 142.201 166.832 118.826 1.00 52.75  ? 325 MET B O     1 
ATOM   2502 C  CB    . MET A 1 323 ? 139.384 167.697 117.579 1.00 56.65  ? 325 MET B CB    1 
ATOM   2503 C  CG    . MET A 1 323 ? 137.964 168.187 117.753 1.00 55.76  ? 325 MET B CG    1 
ATOM   2504 S  SD    . MET A 1 323 ? 137.321 167.895 119.404 1.00 62.60  ? 325 MET B SD    1 
ATOM   2505 C  CE    . MET A 1 323 ? 137.541 166.129 119.550 1.00 54.44  ? 325 MET B CE    1 
ATOM   2506 N  N     . LYS A 1 324 ? 142.539 168.497 117.344 1.00 48.21  ? 326 LYS B N     1 
ATOM   2507 C  CA    . LYS A 1 324 ? 143.893 168.048 117.044 1.00 45.57  ? 326 LYS B CA    1 
ATOM   2508 C  C     . LYS A 1 324 ? 144.781 168.124 118.276 1.00 53.54  ? 326 LYS B C     1 
ATOM   2509 O  O     . LYS A 1 324 ? 145.562 167.204 118.543 1.00 60.98  ? 326 LYS B O     1 
ATOM   2510 C  CB    . LYS A 1 324 ? 144.491 168.874 115.909 1.00 48.13  ? 326 LYS B CB    1 
ATOM   2511 C  CG    . LYS A 1 324 ? 145.843 168.364 115.468 1.00 51.34  ? 326 LYS B CG    1 
ATOM   2512 C  CD    . LYS A 1 324 ? 146.534 169.322 114.536 1.00 50.67  ? 326 LYS B CD    1 
ATOM   2513 C  CE    . LYS A 1 324 ? 147.881 168.776 114.106 1.00 53.72  ? 326 LYS B CE    1 
ATOM   2514 N  NZ    . LYS A 1 324 ? 148.748 168.465 115.273 1.00 55.92  ? 326 LYS B NZ    1 
ATOM   2515 N  N     . GLU A 1 325 ? 144.675 169.212 119.042 1.00 51.76  ? 327 GLU B N     1 
ATOM   2516 C  CA    . GLU A 1 325 ? 145.468 169.339 120.259 1.00 47.84  ? 327 GLU B CA    1 
ATOM   2517 C  C     . GLU A 1 325 ? 145.122 168.254 121.266 1.00 55.03  ? 327 GLU B C     1 
ATOM   2518 O  O     . GLU A 1 325 ? 146.015 167.668 121.887 1.00 62.88  ? 327 GLU B O     1 
ATOM   2519 C  CB    . GLU A 1 325 ? 145.268 170.715 120.883 1.00 49.77  ? 327 GLU B CB    1 
ATOM   2520 C  CG    . GLU A 1 325 ? 145.866 171.844 120.090 1.00 53.67  ? 327 GLU B CG    1 
ATOM   2521 C  CD    . GLU A 1 325 ? 146.106 173.072 120.940 1.00 60.44  ? 327 GLU B CD    1 
ATOM   2522 O  OE1   . GLU A 1 325 ? 146.037 172.958 122.180 1.00 61.19  ? 327 GLU B OE1   1 
ATOM   2523 O  OE2   . GLU A 1 325 ? 146.362 174.150 120.369 1.00 62.69  ? 327 GLU B OE2   1 
ATOM   2524 N  N     . VAL A 1 326 ? 143.833 167.971 121.443 1.00 45.30  ? 328 VAL B N     1 
ATOM   2525 C  CA    . VAL A 1 326 ? 143.429 166.954 122.407 1.00 44.89  ? 328 VAL B CA    1 
ATOM   2526 C  C     . VAL A 1 326 ? 143.962 165.589 121.994 1.00 52.37  ? 328 VAL B C     1 
ATOM   2527 O  O     . VAL A 1 326 ? 144.515 164.844 122.813 1.00 62.73  ? 328 VAL B O     1 
ATOM   2528 C  CB    . VAL A 1 326 ? 141.900 166.940 122.566 1.00 49.53  ? 328 VAL B CB    1 
ATOM   2529 C  CG1   . VAL A 1 326 ? 141.489 165.879 123.556 1.00 51.74  ? 328 VAL B CG1   1 
ATOM   2530 C  CG2   . VAL A 1 326 ? 141.417 168.290 123.032 1.00 53.37  ? 328 VAL B CG2   1 
ATOM   2531 N  N     . ASP A 1 327 ? 143.810 165.244 120.713 1.00 55.31  ? 329 ASP B N     1 
ATOM   2532 C  CA    . ASP A 1 327 ? 144.292 163.951 120.241 1.00 50.33  ? 329 ASP B CA    1 
ATOM   2533 C  C     . ASP A 1 327 ? 145.804 163.845 120.372 1.00 51.39  ? 329 ASP B C     1 
ATOM   2534 O  O     . ASP A 1 327 ? 146.327 162.813 120.807 1.00 59.80  ? 329 ASP B O     1 
ATOM   2535 C  CB    . ASP A 1 327 ? 143.861 163.727 118.795 1.00 56.16  ? 329 ASP B CB    1 
ATOM   2536 C  CG    . ASP A 1 327 ? 142.419 163.290 118.683 1.00 64.55  ? 329 ASP B CG    1 
ATOM   2537 O  OD1   . ASP A 1 327 ? 141.959 162.533 119.563 1.00 63.64  ? 329 ASP B OD1   1 
ATOM   2538 O  OD2   . ASP A 1 327 ? 141.744 163.704 117.718 1.00 65.29  ? 329 ASP B OD2   1 
ATOM   2539 N  N     . GLU A 1 328 ? 146.522 164.913 120.027 1.00 51.75  ? 330 GLU B N     1 
ATOM   2540 C  CA    . GLU A 1 328 ? 147.974 164.889 120.120 1.00 51.91  ? 330 GLU B CA    1 
ATOM   2541 C  C     . GLU A 1 328 ? 148.437 164.735 121.562 1.00 58.34  ? 330 GLU B C     1 
ATOM   2542 O  O     . GLU A 1 328 ? 149.365 163.968 121.842 1.00 62.98  ? 330 GLU B O     1 
ATOM   2543 C  CB    . GLU A 1 328 ? 148.549 166.160 119.497 1.00 53.82  ? 330 GLU B CB    1 
ATOM   2544 C  CG    . GLU A 1 328 ? 150.035 166.362 119.734 1.00 61.90  ? 330 GLU B CG    1 
ATOM   2545 C  CD    . GLU A 1 328 ? 150.877 165.234 119.169 1.00 70.21  ? 330 GLU B CD    1 
ATOM   2546 O  OE1   . GLU A 1 328 ? 150.548 164.734 118.072 1.00 66.62  ? 330 GLU B OE1   1 
ATOM   2547 O  OE2   . GLU A 1 328 ? 151.870 164.848 119.821 1.00 70.67  ? 330 GLU B OE2   1 
ATOM   2548 N  N     . GLN A 1 329 ? 147.813 165.462 122.491 1.00 51.58  ? 331 GLN B N     1 
ATOM   2549 C  CA    . GLN A 1 329 ? 148.205 165.349 123.891 1.00 43.73  ? 331 GLN B CA    1 
ATOM   2550 C  C     . GLN A 1 329 ? 147.905 163.962 124.438 1.00 47.03  ? 331 GLN B C     1 
ATOM   2551 O  O     . GLN A 1 329 ? 148.742 163.367 125.129 1.00 54.37  ? 331 GLN B O     1 
ATOM   2552 C  CB    . GLN A 1 329 ? 147.504 166.418 124.723 1.00 46.64  ? 331 GLN B CB    1 
ATOM   2553 C  CG    . GLN A 1 329 ? 147.953 167.829 124.421 1.00 46.95  ? 331 GLN B CG    1 
ATOM   2554 C  CD    . GLN A 1 329 ? 149.443 167.998 124.523 1.00 48.45  ? 331 GLN B CD    1 
ATOM   2555 O  OE1   . GLN A 1 329 ? 150.084 167.447 125.414 1.00 52.59  ? 331 GLN B OE1   1 
ATOM   2556 N  NE2   . GLN A 1 329 ? 150.010 168.767 123.606 1.00 53.68  ? 331 GLN B NE2   1 
ATOM   2557 N  N     . MET A 1 330 ? 146.724 163.424 124.133 1.00 54.06  ? 332 MET B N     1 
ATOM   2558 C  CA    . MET A 1 330 ? 146.374 162.099 124.622 1.00 53.52  ? 332 MET B CA    1 
ATOM   2559 C  C     . MET A 1 330 ? 147.193 161.004 123.960 1.00 50.45  ? 332 MET B C     1 
ATOM   2560 O  O     . MET A 1 330 ? 147.272 159.897 124.500 1.00 58.77  ? 332 MET B O     1 
ATOM   2561 C  CB    . MET A 1 330 ? 144.886 161.839 124.417 1.00 49.18  ? 332 MET B CB    1 
ATOM   2562 C  CG    . MET A 1 330 ? 144.006 162.706 125.282 1.00 45.53  ? 332 MET B CG    1 
ATOM   2563 S  SD    . MET A 1 330 ? 144.614 162.798 126.968 1.00 69.81  ? 332 MET B SD    1 
ATOM   2564 C  CE    . MET A 1 330 ? 143.614 164.128 127.609 1.00 58.71  ? 332 MET B CE    1 
ATOM   2565 N  N     . LEU A 1 331 ? 147.798 161.276 122.807 1.00 50.49  ? 333 LEU B N     1 
ATOM   2566 C  CA    . LEU A 1 331 ? 148.681 160.280 122.218 1.00 46.85  ? 333 LEU B CA    1 
ATOM   2567 C  C     . LEU A 1 331 ? 150.091 160.378 122.783 1.00 54.00  ? 333 LEU B C     1 
ATOM   2568 O  O     . LEU A 1 331 ? 150.725 159.351 123.053 1.00 64.08  ? 333 LEU B O     1 
ATOM   2569 C  CB    . LEU A 1 331 ? 148.705 160.426 120.701 1.00 49.86  ? 333 LEU B CB    1 
ATOM   2570 C  CG    . LEU A 1 331 ? 149.512 159.359 119.968 1.00 52.91  ? 333 LEU B CG    1 
ATOM   2571 C  CD1   . LEU A 1 331 ? 148.796 158.023 120.020 1.00 55.28  ? 333 LEU B CD1   1 
ATOM   2572 C  CD2   . LEU A 1 331 ? 149.756 159.784 118.538 1.00 55.10  ? 333 LEU B CD2   1 
ATOM   2573 N  N     . ASN A 1 332 ? 150.602 161.595 122.980 1.00 49.81  ? 334 ASN B N     1 
ATOM   2574 C  CA    . ASN A 1 332 ? 151.953 161.719 123.510 1.00 47.84  ? 334 ASN B CA    1 
ATOM   2575 C  C     . ASN A 1 332 ? 152.029 161.367 124.988 1.00 54.96  ? 334 ASN B C     1 
ATOM   2576 O  O     . ASN A 1 332 ? 153.100 160.965 125.455 1.00 59.39  ? 334 ASN B O     1 
ATOM   2577 C  CB    . ASN A 1 332 ? 152.521 163.121 123.270 1.00 51.42  ? 334 ASN B CB    1 
ATOM   2578 C  CG    . ASN A 1 332 ? 151.674 164.217 123.869 1.00 60.22  ? 334 ASN B CG    1 
ATOM   2579 O  OD1   . ASN A 1 332 ? 151.404 164.232 125.070 1.00 58.80  ? 334 ASN B OD1   1 
ATOM   2580 N  ND2   . ASN A 1 332 ? 151.275 165.168 123.034 1.00 63.75  ? 334 ASN B ND2   1 
ATOM   2581 N  N     . VAL A 1 333 ? 150.927 161.488 125.730 1.00 54.17  ? 335 VAL B N     1 
ATOM   2582 C  CA    . VAL A 1 333 ? 150.922 161.012 127.110 1.00 46.44  ? 335 VAL B CA    1 
ATOM   2583 C  C     . VAL A 1 333 ? 151.194 159.516 127.150 1.00 50.44  ? 335 VAL B C     1 
ATOM   2584 O  O     . VAL A 1 333 ? 151.997 159.036 127.958 1.00 52.57  ? 335 VAL B O     1 
ATOM   2585 C  CB    . VAL A 1 333 ? 149.590 161.367 127.794 1.00 46.24  ? 335 VAL B CB    1 
ATOM   2586 C  CG1   . VAL A 1 333 ? 149.318 160.429 128.950 1.00 51.81  ? 335 VAL B CG1   1 
ATOM   2587 C  CG2   . VAL A 1 333 ? 149.614 162.802 128.274 1.00 55.80  ? 335 VAL B CG2   1 
ATOM   2588 N  N     . GLN A 1 334 ? 150.537 158.755 126.274 1.00 54.28  ? 336 GLN B N     1 
ATOM   2589 C  CA    . GLN A 1 334 ? 150.761 157.315 126.228 1.00 47.81  ? 336 GLN B CA    1 
ATOM   2590 C  C     . GLN A 1 334 ? 152.129 156.979 125.653 1.00 46.37  ? 336 GLN B C     1 
ATOM   2591 O  O     . GLN A 1 334 ? 152.795 156.053 126.130 1.00 59.44  ? 336 GLN B O     1 
ATOM   2592 C  CB    . GLN A 1 334 ? 149.665 156.637 125.415 1.00 49.57  ? 336 GLN B CB    1 
ATOM   2593 C  CG    . GLN A 1 334 ? 148.265 157.052 125.791 1.00 50.97  ? 336 GLN B CG    1 
ATOM   2594 C  CD    . GLN A 1 334 ? 147.216 156.325 124.989 1.00 55.68  ? 336 GLN B CD    1 
ATOM   2595 O  OE1   . GLN A 1 334 ? 147.316 155.124 124.766 1.00 60.64  ? 336 GLN B OE1   1 
ATOM   2596 N  NE2   . GLN A 1 334 ? 146.203 157.051 124.545 1.00 54.59  ? 336 GLN B NE2   1 
ATOM   2597 N  N     . ASN A 1 335 ? 152.565 157.708 124.626 1.00 47.15  ? 337 ASN B N     1 
ATOM   2598 C  CA    . ASN A 1 335 ? 153.854 157.412 124.012 1.00 49.17  ? 337 ASN B CA    1 
ATOM   2599 C  C     . ASN A 1 335 ? 155.005 157.650 124.980 1.00 52.34  ? 337 ASN B C     1 
ATOM   2600 O  O     . ASN A 1 335 ? 155.949 156.855 125.041 1.00 54.95  ? 337 ASN B O     1 
ATOM   2601 C  CB    . ASN A 1 335 ? 154.038 158.250 122.751 1.00 51.47  ? 337 ASN B CB    1 
ATOM   2602 C  CG    . ASN A 1 335 ? 153.616 157.518 121.503 1.00 57.29  ? 337 ASN B CG    1 
ATOM   2603 O  OD1   . ASN A 1 335 ? 153.039 156.434 121.571 1.00 57.52  ? 337 ASN B OD1   1 
ATOM   2604 N  ND2   . ASN A 1 335 ? 153.897 158.107 120.349 1.00 56.78  ? 337 ASN B ND2   1 
ATOM   2605 N  N     . LYS A 1 336 ? 154.948 158.737 125.748 1.00 51.58  ? 338 LYS B N     1 
ATOM   2606 C  CA    . LYS A 1 336 ? 156.044 159.066 126.650 1.00 51.04  ? 338 LYS B CA    1 
ATOM   2607 C  C     . LYS A 1 336 ? 156.069 158.174 127.887 1.00 55.64  ? 338 LYS B C     1 
ATOM   2608 O  O     . LYS A 1 336 ? 157.140 157.954 128.463 1.00 61.35  ? 338 LYS B O     1 
ATOM   2609 C  CB    . LYS A 1 336 ? 155.952 160.537 127.054 1.00 54.94  ? 338 LYS B CB    1 
ATOM   2610 C  CG    . LYS A 1 336 ? 157.080 161.024 127.942 1.00 60.37  ? 338 LYS B CG    1 
ATOM   2611 C  CD    . LYS A 1 336 ? 158.425 160.903 127.245 1.00 65.31  ? 338 LYS B CD    1 
ATOM   2612 C  CE    . LYS A 1 336 ? 158.515 161.839 126.051 1.00 63.71  ? 338 LYS B CE    1 
ATOM   2613 N  NZ    . LYS A 1 336 ? 159.838 161.749 125.374 1.00 59.62  ? 338 LYS B NZ    1 
ATOM   2614 N  N     . ASN A 1 337 ? 154.921 157.644 128.299 1.00 55.23  ? 339 ASN B N     1 
ATOM   2615 C  CA    . ASN A 1 337 ? 154.822 156.877 129.534 1.00 53.55  ? 339 ASN B CA    1 
ATOM   2616 C  C     . ASN A 1 337 ? 154.338 155.458 129.271 1.00 57.61  ? 339 ASN B C     1 
ATOM   2617 O  O     . ASN A 1 337 ? 153.415 154.982 129.939 1.00 65.25  ? 339 ASN B O     1 
ATOM   2618 C  CB    . ASN A 1 337 ? 153.878 157.570 130.518 1.00 57.33  ? 339 ASN B CB    1 
ATOM   2619 C  CG    . ASN A 1 337 ? 154.323 158.972 130.860 1.00 60.40  ? 339 ASN B CG    1 
ATOM   2620 O  OD1   . ASN A 1 337 ? 155.506 159.296 130.785 1.00 63.90  ? 339 ASN B OD1   1 
ATOM   2621 N  ND2   . ASN A 1 337 ? 153.373 159.816 131.239 1.00 56.75  ? 339 ASN B ND2   1 
ATOM   2622 N  N     . SER A 1 338 ? 154.944 154.776 128.298 1.00 48.82  ? 340 SER B N     1 
ATOM   2623 C  CA    . SER A 1 338 ? 154.458 153.464 127.888 1.00 46.91  ? 340 SER B CA    1 
ATOM   2624 C  C     . SER A 1 338 ? 154.562 152.421 128.992 1.00 49.44  ? 340 SER B C     1 
ATOM   2625 O  O     . SER A 1 338 ? 153.918 151.372 128.894 1.00 54.91  ? 340 SER B O     1 
ATOM   2626 C  CB    . SER A 1 338 ? 155.220 152.981 126.657 1.00 49.53  ? 340 SER B CB    1 
ATOM   2627 O  OG    . SER A 1 338 ? 156.598 152.830 126.940 1.00 52.19  ? 340 SER B OG    1 
ATOM   2628 N  N     . SER A 1 339 ? 155.352 152.673 130.033 1.00 51.43  ? 341 SER B N     1 
ATOM   2629 C  CA    . SER A 1 339 ? 155.503 151.691 131.099 1.00 52.48  ? 341 SER B CA    1 
ATOM   2630 C  C     . SER A 1 339 ? 154.369 151.738 132.110 1.00 50.24  ? 341 SER B C     1 
ATOM   2631 O  O     . SER A 1 339 ? 154.339 150.905 133.020 1.00 50.30  ? 341 SER B O     1 
ATOM   2632 C  CB    . SER A 1 339 ? 156.837 151.894 131.812 1.00 56.57  ? 341 SER B CB    1 
ATOM   2633 O  OG    . SER A 1 339 ? 156.927 153.196 132.360 1.00 56.27  ? 341 SER B OG    1 
ATOM   2634 N  N     . TYR A 1 340 ? 153.449 152.691 131.983 1.00 55.09  ? 342 TYR B N     1 
ATOM   2635 C  CA    . TYR A 1 340 ? 152.330 152.833 132.901 1.00 49.93  ? 342 TYR B CA    1 
ATOM   2636 C  C     . TYR A 1 340 ? 150.997 152.480 132.257 1.00 53.02  ? 342 TYR B C     1 
ATOM   2637 O  O     . TYR A 1 340 ? 149.948 152.796 132.823 1.00 59.99  ? 342 TYR B O     1 
ATOM   2638 C  CB    . TYR A 1 340 ? 152.280 154.258 133.447 1.00 50.68  ? 342 TYR B CB    1 
ATOM   2639 C  CG    . TYR A 1 340 ? 153.510 154.668 134.217 1.00 55.01  ? 342 TYR B CG    1 
ATOM   2640 C  CD1   . TYR A 1 340 ? 154.309 153.725 134.841 1.00 59.91  ? 342 TYR B CD1   1 
ATOM   2641 C  CD2   . TYR A 1 340 ? 153.882 155.997 134.301 1.00 56.45  ? 342 TYR B CD2   1 
ATOM   2642 C  CE1   . TYR A 1 340 ? 155.436 154.097 135.538 1.00 58.57  ? 342 TYR B CE1   1 
ATOM   2643 C  CE2   . TYR A 1 340 ? 155.004 156.377 134.994 1.00 58.20  ? 342 TYR B CE2   1 
ATOM   2644 C  CZ    . TYR A 1 340 ? 155.778 155.424 135.610 1.00 58.36  ? 342 TYR B CZ    1 
ATOM   2645 O  OH    . TYR A 1 340 ? 156.902 155.800 136.306 1.00 58.32  ? 342 TYR B OH    1 
ATOM   2646 N  N     . PHE A 1 341 ? 151.008 151.838 131.094 1.00 44.53  ? 343 PHE B N     1 
ATOM   2647 C  CA    . PHE A 1 341 ? 149.788 151.484 130.389 1.00 41.48  ? 343 PHE B CA    1 
ATOM   2648 C  C     . PHE A 1 341 ? 149.843 150.025 129.963 1.00 50.74  ? 343 PHE B C     1 
ATOM   2649 O  O     . PHE A 1 341 ? 150.909 149.493 129.647 1.00 56.83  ? 343 PHE B O     1 
ATOM   2650 C  CB    . PHE A 1 341 ? 149.575 152.374 129.170 1.00 41.60  ? 343 PHE B CB    1 
ATOM   2651 C  CG    . PHE A 1 341 ? 149.205 153.783 129.505 1.00 45.67  ? 343 PHE B CG    1 
ATOM   2652 C  CD1   . PHE A 1 341 ? 147.883 154.148 129.657 1.00 47.70  ? 343 PHE B CD1   1 
ATOM   2653 C  CD2   . PHE A 1 341 ? 150.176 154.747 129.658 1.00 51.14  ? 343 PHE B CD2   1 
ATOM   2654 C  CE1   . PHE A 1 341 ? 147.542 155.441 129.960 1.00 47.24  ? 343 PHE B CE1   1 
ATOM   2655 C  CE2   . PHE A 1 341 ? 149.835 156.042 129.960 1.00 50.58  ? 343 PHE B CE2   1 
ATOM   2656 C  CZ    . PHE A 1 341 ? 148.517 156.387 130.108 1.00 49.14  ? 343 PHE B CZ    1 
ATOM   2657 N  N     . VAL A 1 342 ? 148.678 149.383 129.960 1.00 45.81  ? 344 VAL B N     1 
ATOM   2658 C  CA    . VAL A 1 342 ? 148.587 147.975 129.602 1.00 41.96  ? 344 VAL B CA    1 
ATOM   2659 C  C     . VAL A 1 342 ? 148.858 147.811 128.114 1.00 48.78  ? 344 VAL B C     1 
ATOM   2660 O  O     . VAL A 1 342 ? 148.336 148.565 127.283 1.00 53.64  ? 344 VAL B O     1 
ATOM   2661 C  CB    . VAL A 1 342 ? 147.213 147.415 129.993 1.00 44.57  ? 344 VAL B CB    1 
ATOM   2662 C  CG1   . VAL A 1 342 ? 146.842 146.240 129.121 1.00 48.08  ? 344 VAL B CG1   1 
ATOM   2663 C  CG2   . VAL A 1 342 ? 147.217 147.015 131.447 1.00 48.41  ? 344 VAL B CG2   1 
ATOM   2664 N  N     . GLU A 1 343 ? 149.679 146.820 127.771 1.00 49.56  ? 345 GLU B N     1 
ATOM   2665 C  CA    . GLU A 1 343 ? 150.172 146.685 126.408 1.00 46.64  ? 345 GLU B CA    1 
ATOM   2666 C  C     . GLU A 1 343 ? 149.135 146.116 125.448 1.00 45.88  ? 345 GLU B C     1 
ATOM   2667 O  O     . GLU A 1 343 ? 149.087 146.535 124.288 1.00 50.43  ? 345 GLU B O     1 
ATOM   2668 C  CB    . GLU A 1 343 ? 151.426 145.814 126.397 1.00 51.74  ? 345 GLU B CB    1 
ATOM   2669 C  CG    . GLU A 1 343 ? 152.261 145.950 125.138 1.00 56.27  ? 345 GLU B CG    1 
ATOM   2670 C  CD    . GLU A 1 343 ? 153.600 145.248 125.250 1.00 61.89  ? 345 GLU B CD    1 
ATOM   2671 O  OE1   . GLU A 1 343 ? 153.909 144.722 126.340 1.00 61.99  ? 345 GLU B OE1   1 
ATOM   2672 O  OE2   . GLU A 1 343 ? 154.344 145.222 124.247 1.00 57.35  ? 345 GLU B OE2   1 
ATOM   2673 N  N     . TRP A 1 344 ? 148.304 145.176 125.889 1.00 42.02  ? 346 TRP B N     1 
ATOM   2674 C  CA    . TRP A 1 344 ? 147.380 144.504 124.985 1.00 43.24  ? 346 TRP B CA    1 
ATOM   2675 C  C     . TRP A 1 344 ? 146.102 145.290 124.728 1.00 48.02  ? 346 TRP B C     1 
ATOM   2676 O  O     . TRP A 1 344 ? 145.262 144.833 123.948 1.00 50.64  ? 346 TRP B O     1 
ATOM   2677 C  CB    . TRP A 1 344 ? 147.029 143.109 125.511 1.00 42.45  ? 346 TRP B CB    1 
ATOM   2678 C  CG    . TRP A 1 344 ? 146.653 143.072 126.942 1.00 39.24  ? 346 TRP B CG    1 
ATOM   2679 C  CD1   . TRP A 1 344 ? 147.494 142.956 128.001 1.00 45.47  ? 346 TRP B CD1   1 
ATOM   2680 C  CD2   . TRP A 1 344 ? 145.335 143.149 127.482 1.00 40.95  ? 346 TRP B CD2   1 
ATOM   2681 N  NE1   . TRP A 1 344 ? 146.784 142.956 129.171 1.00 45.91  ? 346 TRP B NE1   1 
ATOM   2682 C  CE2   . TRP A 1 344 ? 145.453 143.077 128.878 1.00 43.10  ? 346 TRP B CE2   1 
ATOM   2683 C  CE3   . TRP A 1 344 ? 144.065 143.278 126.920 1.00 47.96  ? 346 TRP B CE3   1 
ATOM   2684 C  CZ2   . TRP A 1 344 ? 144.352 143.133 129.723 1.00 44.23  ? 346 TRP B CZ2   1 
ATOM   2685 C  CZ3   . TRP A 1 344 ? 142.972 143.328 127.760 1.00 51.21  ? 346 TRP B CZ3   1 
ATOM   2686 C  CH2   . TRP A 1 344 ? 143.122 143.258 129.146 1.00 43.56  ? 346 TRP B CH2   1 
ATOM   2687 N  N     . ILE A 1 345 ? 145.925 146.445 125.359 1.00 50.57  ? 347 ILE B N     1 
ATOM   2688 C  CA    . ILE A 1 345 ? 144.841 147.365 125.038 1.00 42.40  ? 347 ILE B CA    1 
ATOM   2689 C  C     . ILE A 1 345 ? 145.463 148.588 124.370 1.00 48.42  ? 347 ILE B C     1 
ATOM   2690 O  O     . ILE A 1 345 ? 146.143 149.378 125.041 1.00 52.27  ? 347 ILE B O     1 
ATOM   2691 C  CB    . ILE A 1 345 ? 144.039 147.772 126.281 1.00 44.28  ? 347 ILE B CB    1 
ATOM   2692 C  CG1   . ILE A 1 345 ? 143.149 146.635 126.756 1.00 48.35  ? 347 ILE B CG1   1 
ATOM   2693 C  CG2   . ILE A 1 345 ? 143.172 148.972 125.977 1.00 45.40  ? 347 ILE B CG2   1 
ATOM   2694 C  CD1   . ILE A 1 345 ? 142.230 147.030 127.882 1.00 47.61  ? 347 ILE B CD1   1 
ATOM   2695 N  N     . PRO A 1 346 ? 145.291 148.776 123.068 1.00 47.13  ? 348 PRO B N     1 
ATOM   2696 C  CA    . PRO A 1 346 ? 145.736 150.020 122.441 1.00 45.28  ? 348 PRO B CA    1 
ATOM   2697 C  C     . PRO A 1 346 ? 144.716 151.124 122.656 1.00 51.23  ? 348 PRO B C     1 
ATOM   2698 O  O     . PRO A 1 346 ? 143.511 150.879 122.753 1.00 54.66  ? 348 PRO B O     1 
ATOM   2699 C  CB    . PRO A 1 346 ? 145.845 149.649 120.958 1.00 41.80  ? 348 PRO B CB    1 
ATOM   2700 C  CG    . PRO A 1 346 ? 145.697 148.153 120.915 1.00 46.92  ? 348 PRO B CG    1 
ATOM   2701 C  CD    . PRO A 1 346 ? 144.845 147.804 122.067 1.00 44.73  ? 348 PRO B CD    1 
ATOM   2702 N  N     . ASN A 1 347 ? 145.220 152.354 122.738 1.00 44.59  ? 349 ASN B N     1 
ATOM   2703 C  CA    . ASN A 1 347 ? 144.389 153.536 122.962 1.00 47.14  ? 349 ASN B CA    1 
ATOM   2704 C  C     . ASN A 1 347 ? 143.601 153.414 124.271 1.00 49.07  ? 349 ASN B C     1 
ATOM   2705 O  O     . ASN A 1 347 ? 142.377 153.279 124.294 1.00 53.17  ? 349 ASN B O     1 
ATOM   2706 C  CB    . ASN A 1 347 ? 143.457 153.789 121.773 1.00 46.41  ? 349 ASN B CB    1 
ATOM   2707 C  CG    . ASN A 1 347 ? 142.768 155.129 121.857 1.00 53.50  ? 349 ASN B CG    1 
ATOM   2708 O  OD1   . ASN A 1 347 ? 143.374 156.167 121.592 1.00 53.71  ? 349 ASN B OD1   1 
ATOM   2709 N  ND2   . ASN A 1 347 ? 141.493 155.118 122.224 1.00 53.90  ? 349 ASN B ND2   1 
ATOM   2710 N  N     . ASN A 1 348 ? 144.353 153.450 125.372 1.00 39.96  ? 350 ASN B N     1 
ATOM   2711 C  CA    . ASN A 1 348 ? 143.768 153.366 126.703 1.00 44.19  ? 350 ASN B CA    1 
ATOM   2712 C  C     . ASN A 1 348 ? 142.956 154.598 127.091 1.00 49.80  ? 350 ASN B C     1 
ATOM   2713 O  O     . ASN A 1 348 ? 142.330 154.585 128.155 1.00 52.60  ? 350 ASN B O     1 
ATOM   2714 C  CB    . ASN A 1 348 ? 144.862 153.146 127.750 1.00 42.43  ? 350 ASN B CB    1 
ATOM   2715 C  CG    . ASN A 1 348 ? 145.869 152.104 127.334 1.00 45.46  ? 350 ASN B CG    1 
ATOM   2716 O  OD1   . ASN A 1 348 ? 146.723 152.354 126.489 1.00 48.72  ? 350 ASN B OD1   1 
ATOM   2717 N  ND2   . ASN A 1 348 ? 145.779 150.928 127.930 1.00 46.11  ? 350 ASN B ND2   1 
ATOM   2718 N  N     . VAL A 1 349 ? 142.950 155.651 126.280 1.00 43.61  ? 351 VAL B N     1 
ATOM   2719 C  CA    . VAL A 1 349 ? 142.339 156.927 126.640 1.00 35.29  ? 351 VAL B CA    1 
ATOM   2720 C  C     . VAL A 1 349 ? 141.092 157.156 125.796 1.00 37.81  ? 351 VAL B C     1 
ATOM   2721 O  O     . VAL A 1 349 ? 141.085 156.881 124.592 1.00 43.25  ? 351 VAL B O     1 
ATOM   2722 C  CB    . VAL A 1 349 ? 143.339 158.088 126.469 1.00 35.93  ? 351 VAL B CB    1 
ATOM   2723 C  CG1   . VAL A 1 349 ? 142.667 159.418 126.729 1.00 44.00  ? 351 VAL B CG1   1 
ATOM   2724 C  CG2   . VAL A 1 349 ? 144.517 157.909 127.396 1.00 40.95  ? 351 VAL B CG2   1 
ATOM   2725 N  N     . LYS A 1 350 ? 140.033 157.652 126.436 1.00 36.71  ? 352 LYS B N     1 
ATOM   2726 C  CA    . LYS A 1 350 ? 138.825 158.108 125.762 1.00 34.70  ? 352 LYS B CA    1 
ATOM   2727 C  C     . LYS A 1 350 ? 138.654 159.606 125.974 1.00 43.25  ? 352 LYS B C     1 
ATOM   2728 O  O     . LYS A 1 350 ? 138.914 160.119 127.066 1.00 53.97  ? 352 LYS B O     1 
ATOM   2729 C  CB    . LYS A 1 350 ? 137.587 157.374 126.269 1.00 27.32  ? 352 LYS B CB    1 
ATOM   2730 C  CG    . LYS A 1 350 ? 136.304 157.966 125.737 1.00 32.17  ? 352 LYS B CG    1 
ATOM   2731 C  CD    . LYS A 1 350 ? 135.131 157.053 125.912 1.00 39.80  ? 352 LYS B CD    1 
ATOM   2732 C  CE    . LYS A 1 350 ? 133.922 157.615 125.195 1.00 43.46  ? 352 LYS B CE    1 
ATOM   2733 N  NZ    . LYS A 1 350 ? 134.292 158.124 123.850 1.00 38.32  ? 352 LYS B NZ    1 
ATOM   2734 N  N     . THR A 1 351 ? 138.211 160.304 124.930 1.00 34.24  ? 353 THR B N     1 
ATOM   2735 C  CA    . THR A 1 351 ? 138.099 161.756 124.935 1.00 30.51  ? 353 THR B CA    1 
ATOM   2736 C  C     . THR A 1 351 ? 136.652 162.175 124.722 1.00 38.00  ? 353 THR B C     1 
ATOM   2737 O  O     . THR A 1 351 ? 135.973 161.649 123.836 1.00 47.49  ? 353 THR B O     1 
ATOM   2738 C  CB    . THR A 1 351 ? 138.993 162.369 123.855 1.00 37.61  ? 353 THR B CB    1 
ATOM   2739 O  OG1   . THR A 1 351 ? 140.340 162.429 124.332 1.00 45.15  ? 353 THR B OG1   1 
ATOM   2740 C  CG2   . THR A 1 351 ? 138.528 163.768 123.489 1.00 44.24  ? 353 THR B CG2   1 
ATOM   2741 N  N     . ALA A 1 352 ? 136.183 163.109 125.546 1.00 39.32  ? 354 ALA B N     1 
ATOM   2742 C  CA    . ALA A 1 352 ? 134.902 163.770 125.359 1.00 40.02  ? 354 ALA B CA    1 
ATOM   2743 C  C     . ALA A 1 352 ? 135.103 165.272 125.479 1.00 40.90  ? 354 ALA B C     1 
ATOM   2744 O  O     . ALA A 1 352 ? 135.862 165.734 126.335 1.00 45.05  ? 354 ALA B O     1 
ATOM   2745 C  CB    . ALA A 1 352 ? 133.872 163.298 126.378 1.00 43.56  ? 354 ALA B CB    1 
ATOM   2746 N  N     . VAL A 1 353 ? 134.433 166.035 124.618 1.00 38.27  ? 355 VAL B N     1 
ATOM   2747 C  CA    . VAL A 1 353 ? 134.581 167.485 124.584 1.00 35.32  ? 355 VAL B CA    1 
ATOM   2748 C  C     . VAL A 1 353 ? 133.204 168.128 124.656 1.00 37.48  ? 355 VAL B C     1 
ATOM   2749 O  O     . VAL A 1 353 ? 132.341 167.847 123.819 1.00 47.55  ? 355 VAL B O     1 
ATOM   2750 C  CB    . VAL A 1 353 ? 135.328 167.957 123.330 1.00 41.84  ? 355 VAL B CB    1 
ATOM   2751 C  CG1   . VAL A 1 353 ? 135.324 169.464 123.258 1.00 45.32  ? 355 VAL B CG1   1 
ATOM   2752 C  CG2   . VAL A 1 353 ? 136.747 167.443 123.343 1.00 44.83  ? 355 VAL B CG2   1 
ATOM   2753 N  N     . CYS A 1 354 ? 133.010 169.004 125.638 1.00 48.70  ? 356 CYS B N     1 
ATOM   2754 C  CA    . CYS A 1 354 ? 131.801 169.799 125.790 1.00 42.89  ? 356 CYS B CA    1 
ATOM   2755 C  C     . CYS A 1 354 ? 132.149 171.272 125.629 1.00 52.41  ? 356 CYS B C     1 
ATOM   2756 O  O     . CYS A 1 354 ? 133.244 171.707 125.996 1.00 60.41  ? 356 CYS B O     1 
ATOM   2757 C  CB    . CYS A 1 354 ? 131.146 169.558 127.151 1.00 42.16  ? 356 CYS B CB    1 
ATOM   2758 S  SG    . CYS A 1 354 ? 129.896 170.755 127.621 1.00 66.59  ? 356 CYS B SG    1 
ATOM   2759 N  N     . ASP A 1 355 ? 131.212 172.045 125.081 1.00 53.62  ? 357 ASP B N     1 
ATOM   2760 C  CA    . ASP A 1 355 ? 131.513 173.389 124.604 1.00 51.75  ? 357 ASP B CA    1 
ATOM   2761 C  C     . ASP A 1 355 ? 131.043 174.493 125.547 1.00 54.43  ? 357 ASP B C     1 
ATOM   2762 O  O     . ASP A 1 355 ? 131.013 175.661 125.150 1.00 58.30  ? 357 ASP B O     1 
ATOM   2763 C  CB    . ASP A 1 355 ? 130.920 173.598 123.211 1.00 55.00  ? 357 ASP B CB    1 
ATOM   2764 C  CG    . ASP A 1 355 ? 129.432 173.312 123.156 1.00 63.05  ? 357 ASP B CG    1 
ATOM   2765 O  OD1   . ASP A 1 355 ? 128.806 173.157 124.225 1.00 65.90  ? 357 ASP B OD1   1 
ATOM   2766 O  OD2   . ASP A 1 355 ? 128.885 173.240 122.035 1.00 58.97  ? 357 ASP B OD2   1 
ATOM   2767 N  N     . ILE A 1 356 ? 130.679 174.164 126.780 1.00 51.00  ? 358 ILE B N     1 
ATOM   2768 C  CA    . ILE A 1 356 ? 130.279 175.191 127.740 1.00 47.68  ? 358 ILE B CA    1 
ATOM   2769 C  C     . ILE A 1 356 ? 131.167 175.096 128.974 1.00 50.57  ? 358 ILE B C     1 
ATOM   2770 O  O     . ILE A 1 356 ? 131.041 174.146 129.758 1.00 56.07  ? 358 ILE B O     1 
ATOM   2771 C  CB    . ILE A 1 356 ? 128.794 175.068 128.108 1.00 48.33  ? 358 ILE B CB    1 
ATOM   2772 C  CG1   . ILE A 1 356 ? 127.923 175.318 126.878 1.00 52.75  ? 358 ILE B CG1   1 
ATOM   2773 C  CG2   . ILE A 1 356 ? 128.441 176.045 129.212 1.00 53.53  ? 358 ILE B CG2   1 
ATOM   2774 C  CD1   . ILE A 1 356 ? 127.999 176.729 126.359 1.00 53.94  ? 358 ILE B CD1   1 
ATOM   2775 N  N     . PRO A 1 357 ? 132.074 176.044 129.182 1.00 49.47  ? 359 PRO B N     1 
ATOM   2776 C  CA    . PRO A 1 357 ? 133.003 175.959 130.307 1.00 47.06  ? 359 PRO B CA    1 
ATOM   2777 C  C     . PRO A 1 357 ? 132.312 176.288 131.616 1.00 52.09  ? 359 PRO B C     1 
ATOM   2778 O  O     . PRO A 1 357 ? 131.231 176.895 131.622 1.00 59.26  ? 359 PRO B O     1 
ATOM   2779 C  CB    . PRO A 1 357 ? 134.058 177.014 129.960 1.00 46.35  ? 359 PRO B CB    1 
ATOM   2780 C  CG    . PRO A 1 357 ? 133.314 178.014 129.170 1.00 49.45  ? 359 PRO B CG    1 
ATOM   2781 C  CD    . PRO A 1 357 ? 132.291 177.257 128.379 1.00 51.10  ? 359 PRO B CD    1 
ATOM   2782 N  N     . PRO A 1 358 ? 132.901 175.903 132.746 1.00 50.35  ? 360 PRO B N     1 
ATOM   2783 C  CA    . PRO A 1 358 ? 132.338 176.304 134.038 1.00 48.22  ? 360 PRO B CA    1 
ATOM   2784 C  C     . PRO A 1 358 ? 132.408 177.811 134.217 1.00 54.96  ? 360 PRO B C     1 
ATOM   2785 O  O     . PRO A 1 358 ? 133.274 178.485 133.655 1.00 59.09  ? 360 PRO B O     1 
ATOM   2786 C  CB    . PRO A 1 358 ? 133.224 175.577 135.055 1.00 51.08  ? 360 PRO B CB    1 
ATOM   2787 C  CG    . PRO A 1 358 ? 133.880 174.488 134.292 1.00 53.00  ? 360 PRO B CG    1 
ATOM   2788 C  CD    . PRO A 1 358 ? 134.054 175.005 132.904 1.00 56.64  ? 360 PRO B CD    1 
ATOM   2789 N  N     . ARG A 1 359 ? 131.473 178.338 135.002 1.00 60.12  ? 369 ARG B N     1 
ATOM   2790 C  CA    . ARG A 1 359 ? 131.382 179.778 135.193 1.00 57.07  ? 369 ARG B CA    1 
ATOM   2791 C  C     . ARG A 1 359 ? 132.663 180.316 135.810 1.00 61.57  ? 369 ARG B C     1 
ATOM   2792 O  O     . ARG A 1 359 ? 133.157 179.787 136.808 1.00 69.44  ? 369 ARG B O     1 
ATOM   2793 C  CB    . ARG A 1 359 ? 130.182 180.110 136.075 1.00 63.79  ? 369 ARG B CB    1 
ATOM   2794 C  CG    . ARG A 1 359 ? 130.103 181.566 136.506 1.00 68.72  ? 369 ARG B CG    1 
ATOM   2795 C  CD    . ARG A 1 359 ? 128.677 181.948 136.868 1.00 66.93  ? 369 ARG B CD    1 
ATOM   2796 N  NE    . ARG A 1 359 ? 127.794 181.859 135.712 1.00 70.63  ? 369 ARG B NE    1 
ATOM   2797 C  CZ    . ARG A 1 359 ? 126.512 182.193 135.719 1.00 70.32  ? 369 ARG B CZ    1 
ATOM   2798 N  NH1   . ARG A 1 359 ? 125.921 182.641 136.815 1.00 67.73  ? 369 ARG B NH1   1 
ATOM   2799 N  NH2   . ARG A 1 359 ? 125.805 182.074 134.600 1.00 67.78  ? 369 ARG B NH2   1 
ATOM   2800 N  N     . GLY A 1 360 ? 133.202 181.372 135.212 1.00 49.75  ? 370 GLY B N     1 
ATOM   2801 C  CA    . GLY A 1 360 ? 134.423 181.983 135.686 1.00 50.52  ? 370 GLY B CA    1 
ATOM   2802 C  C     . GLY A 1 360 ? 135.702 181.397 135.136 1.00 51.19  ? 370 GLY B C     1 
ATOM   2803 O  O     . GLY A 1 360 ? 136.783 181.890 135.477 1.00 54.20  ? 370 GLY B O     1 
ATOM   2804 N  N     . LEU A 1 361 ? 135.624 180.370 134.297 1.00 52.87  ? 371 LEU B N     1 
ATOM   2805 C  CA    . LEU A 1 361 ? 136.800 179.764 133.699 1.00 50.05  ? 371 LEU B CA    1 
ATOM   2806 C  C     . LEU A 1 361 ? 136.672 179.778 132.185 1.00 56.57  ? 371 LEU B C     1 
ATOM   2807 O  O     . LEU A 1 361 ? 135.583 179.936 131.631 1.00 61.84  ? 371 LEU B O     1 
ATOM   2808 C  CB    . LEU A 1 361 ? 137.010 178.319 134.163 1.00 47.39  ? 371 LEU B CB    1 
ATOM   2809 C  CG    . LEU A 1 361 ? 137.410 178.039 135.605 1.00 49.88  ? 371 LEU B CG    1 
ATOM   2810 C  CD1   . LEU A 1 361 ? 136.278 177.329 136.314 1.00 55.74  ? 371 LEU B CD1   1 
ATOM   2811 C  CD2   . LEU A 1 361 ? 138.677 177.217 135.661 1.00 55.62  ? 371 LEU B CD2   1 
ATOM   2812 N  N     . LYS A 1 362 ? 137.810 179.605 131.520 1.00 51.45  ? 372 LYS B N     1 
ATOM   2813 C  CA    . LYS A 1 362 ? 137.847 179.396 130.081 1.00 47.44  ? 372 LYS B CA    1 
ATOM   2814 C  C     . LYS A 1 362 ? 137.908 177.923 129.703 1.00 55.23  ? 372 LYS B C     1 
ATOM   2815 O  O     . LYS A 1 362 ? 137.303 177.521 128.708 1.00 60.20  ? 372 LYS B O     1 
ATOM   2816 C  CB    . LYS A 1 362 ? 139.045 180.127 129.474 1.00 49.87  ? 372 LYS B CB    1 
ATOM   2817 C  CG    . LYS A 1 362 ? 139.061 181.617 129.756 1.00 56.18  ? 372 LYS B CG    1 
ATOM   2818 C  CD    . LYS A 1 362 ? 137.843 182.313 129.168 1.00 59.34  ? 372 LYS B CD    1 
ATOM   2819 C  CE    . LYS A 1 362 ? 137.871 182.295 127.652 1.00 57.84  ? 372 LYS B CE    1 
ATOM   2820 N  NZ    . LYS A 1 362 ? 139.067 183.002 127.116 1.00 57.63  ? 372 LYS B NZ    1 
ATOM   2821 N  N     . MET A 1 363 ? 138.624 177.110 130.476 1.00 53.26  ? 373 MET B N     1 
ATOM   2822 C  CA    . MET A 1 363 ? 138.777 175.691 130.203 1.00 49.77  ? 373 MET B CA    1 
ATOM   2823 C  C     . MET A 1 363 ? 138.741 174.921 131.514 1.00 52.24  ? 373 MET B C     1 
ATOM   2824 O  O     . MET A 1 363 ? 138.967 175.478 132.589 1.00 59.32  ? 373 MET B O     1 
ATOM   2825 C  CB    . MET A 1 363 ? 140.087 175.399 129.466 1.00 50.85  ? 373 MET B CB    1 
ATOM   2826 C  CG    . MET A 1 363 ? 140.171 175.994 128.079 1.00 57.73  ? 373 MET B CG    1 
ATOM   2827 S  SD    . MET A 1 363 ? 141.845 175.966 127.426 1.00 74.56  ? 373 MET B SD    1 
ATOM   2828 C  CE    . MET A 1 363 ? 142.310 174.285 127.807 1.00 62.26  ? 373 MET B CE    1 
ATOM   2829 N  N     . SER A 1 364 ? 138.455 173.627 131.412 1.00 44.76  ? 374 SER B N     1 
ATOM   2830 C  CA    . SER A 1 364 ? 138.447 172.738 132.566 1.00 39.31  ? 374 SER B CA    1 
ATOM   2831 C  C     . SER A 1 364 ? 138.484 171.302 132.067 1.00 42.35  ? 374 SER B C     1 
ATOM   2832 O  O     . SER A 1 364 ? 138.325 171.037 130.874 1.00 49.68  ? 374 SER B O     1 
ATOM   2833 C  CB    . SER A 1 364 ? 137.224 172.976 133.450 1.00 50.13  ? 374 SER B CB    1 
ATOM   2834 O  OG    . SER A 1 364 ? 136.124 172.199 133.014 1.00 53.15  ? 374 SER B OG    1 
ATOM   2835 N  N     . ALA A 1 365 ? 138.690 170.373 132.998 1.00 44.51  ? 375 ALA B N     1 
ATOM   2836 C  CA    . ALA A 1 365 ? 138.772 168.964 132.645 1.00 40.75  ? 375 ALA B CA    1 
ATOM   2837 C  C     . ALA A 1 365 ? 138.615 168.105 133.890 1.00 43.75  ? 375 ALA B C     1 
ATOM   2838 O  O     . ALA A 1 365 ? 138.979 168.517 134.993 1.00 52.16  ? 375 ALA B O     1 
ATOM   2839 C  CB    . ALA A 1 365 ? 140.095 168.645 131.950 1.00 37.15  ? 375 ALA B CB    1 
ATOM   2840 N  N     . THR A 1 366 ? 138.073 166.905 133.697 1.00 43.36  ? 376 THR B N     1 
ATOM   2841 C  CA    . THR A 1 366 ? 137.962 165.906 134.748 1.00 43.98  ? 376 THR B CA    1 
ATOM   2842 C  C     . THR A 1 366 ? 138.624 164.614 134.290 1.00 45.24  ? 376 THR B C     1 
ATOM   2843 O  O     . THR A 1 366 ? 138.623 164.285 133.102 1.00 48.99  ? 376 THR B O     1 
ATOM   2844 C  CB    . THR A 1 366 ? 136.503 165.634 135.132 1.00 40.53  ? 376 THR B CB    1 
ATOM   2845 O  OG1   . THR A 1 366 ? 135.762 165.255 133.968 1.00 47.26  ? 376 THR B OG1   1 
ATOM   2846 C  CG2   . THR A 1 366 ? 135.877 166.871 135.745 1.00 44.14  ? 376 THR B CG2   1 
ATOM   2847 N  N     . PHE A 1 367 ? 139.195 163.886 135.245 1.00 42.31  ? 377 PHE B N     1 
ATOM   2848 C  CA    . PHE A 1 367 ? 139.999 162.703 134.977 1.00 37.34  ? 377 PHE B CA    1 
ATOM   2849 C  C     . PHE A 1 367 ? 139.417 161.511 135.720 1.00 45.81  ? 377 PHE B C     1 
ATOM   2850 O  O     . PHE A 1 367 ? 139.236 161.566 136.939 1.00 52.53  ? 377 PHE B O     1 
ATOM   2851 C  CB    . PHE A 1 367 ? 141.447 162.951 135.399 1.00 42.80  ? 377 PHE B CB    1 
ATOM   2852 C  CG    . PHE A 1 367 ? 142.326 161.738 135.353 1.00 45.85  ? 377 PHE B CG    1 
ATOM   2853 C  CD1   . PHE A 1 367 ? 142.977 161.385 134.191 1.00 47.05  ? 377 PHE B CD1   1 
ATOM   2854 C  CD2   . PHE A 1 367 ? 142.532 160.972 136.485 1.00 46.28  ? 377 PHE B CD2   1 
ATOM   2855 C  CE1   . PHE A 1 367 ? 143.798 160.284 134.154 1.00 50.13  ? 377 PHE B CE1   1 
ATOM   2856 C  CE2   . PHE A 1 367 ? 143.346 159.870 136.447 1.00 46.76  ? 377 PHE B CE2   1 
ATOM   2857 C  CZ    . PHE A 1 367 ? 143.982 159.527 135.282 1.00 46.52  ? 377 PHE B CZ    1 
ATOM   2858 N  N     . ILE A 1 368 ? 139.126 160.441 134.988 1.00 42.08  ? 378 ILE B N     1 
ATOM   2859 C  CA    . ILE A 1 368 ? 138.679 159.177 135.559 1.00 34.48  ? 378 ILE B CA    1 
ATOM   2860 C  C     . ILE A 1 368 ? 139.658 158.099 135.119 1.00 40.39  ? 378 ILE B C     1 
ATOM   2861 O  O     . ILE A 1 368 ? 139.936 157.964 133.924 1.00 48.95  ? 378 ILE B O     1 
ATOM   2862 C  CB    . ILE A 1 368 ? 137.247 158.826 135.118 1.00 39.99  ? 378 ILE B CB    1 
ATOM   2863 C  CG1   . ILE A 1 368 ? 136.308 159.999 135.369 1.00 45.96  ? 378 ILE B CG1   1 
ATOM   2864 C  CG2   . ILE A 1 368 ? 136.748 157.609 135.855 1.00 47.86  ? 378 ILE B CG2   1 
ATOM   2865 C  CD1   . ILE A 1 368 ? 134.907 159.754 134.884 1.00 44.02  ? 378 ILE B CD1   1 
ATOM   2866 N  N     . GLY A 1 369 ? 140.176 157.337 136.074 1.00 34.02  ? 379 GLY B N     1 
ATOM   2867 C  CA    . GLY A 1 369 ? 141.204 156.359 135.785 1.00 36.26  ? 379 GLY B CA    1 
ATOM   2868 C  C     . GLY A 1 369 ? 140.943 155.028 136.458 1.00 41.74  ? 379 GLY B C     1 
ATOM   2869 O  O     . GLY A 1 369 ? 140.341 154.953 137.525 1.00 50.89  ? 379 GLY B O     1 
ATOM   2870 N  N     . ASN A 1 370 ? 141.432 153.968 135.815 1.00 43.04  ? 380 ASN B N     1 
ATOM   2871 C  CA    . ASN A 1 370 ? 141.248 152.586 136.260 1.00 35.72  ? 380 ASN B CA    1 
ATOM   2872 C  C     . ASN A 1 370 ? 142.620 151.921 136.282 1.00 42.62  ? 380 ASN B C     1 
ATOM   2873 O  O     . ASN A 1 370 ? 143.055 151.357 135.276 1.00 52.91  ? 380 ASN B O     1 
ATOM   2874 C  CB    . ASN A 1 370 ? 140.285 151.852 135.342 1.00 37.61  ? 380 ASN B CB    1 
ATOM   2875 C  CG    . ASN A 1 370 ? 139.737 150.588 135.958 1.00 46.19  ? 380 ASN B CG    1 
ATOM   2876 O  OD1   . ASN A 1 370 ? 140.207 150.138 136.999 1.00 50.59  ? 380 ASN B OD1   1 
ATOM   2877 N  ND2   . ASN A 1 370 ? 138.735 150.008 135.318 1.00 43.67  ? 380 ASN B ND2   1 
ATOM   2878 N  N     . SER A 1 371 ? 143.297 151.983 137.423 1.00 41.01  ? 381 SER B N     1 
ATOM   2879 C  CA    . SER A 1 371 ? 144.662 151.503 137.538 1.00 36.06  ? 381 SER B CA    1 
ATOM   2880 C  C     . SER A 1 371 ? 144.738 150.348 138.523 1.00 44.84  ? 381 SER B C     1 
ATOM   2881 O  O     . SER A 1 371 ? 143.919 150.224 139.436 1.00 52.83  ? 381 SER B O     1 
ATOM   2882 C  CB    . SER A 1 371 ? 145.612 152.619 137.979 1.00 42.41  ? 381 SER B CB    1 
ATOM   2883 O  OG    . SER A 1 371 ? 145.343 153.012 139.310 1.00 48.83  ? 381 SER B OG    1 
ATOM   2884 N  N     . THR A 1 372 ? 145.739 149.493 138.316 1.00 44.76  ? 382 THR B N     1 
ATOM   2885 C  CA    . THR A 1 372 ? 146.002 148.384 139.222 1.00 39.97  ? 382 THR B CA    1 
ATOM   2886 C  C     . THR A 1 372 ? 146.582 148.844 140.548 1.00 48.55  ? 382 THR B C     1 
ATOM   2887 O  O     . THR A 1 372 ? 146.698 148.030 141.469 1.00 57.17  ? 382 THR B O     1 
ATOM   2888 C  CB    . THR A 1 372 ? 146.947 147.387 138.566 1.00 42.94  ? 382 THR B CB    1 
ATOM   2889 O  OG1   . THR A 1 372 ? 148.213 148.011 138.344 1.00 54.04  ? 382 THR B OG1   1 
ATOM   2890 C  CG2   . THR A 1 372 ? 146.385 146.946 137.240 1.00 40.37  ? 382 THR B CG2   1 
ATOM   2891 N  N     . ALA A 1 373 ? 146.950 150.118 140.664 1.00 50.99  ? 383 ALA B N     1 
ATOM   2892 C  CA    . ALA A 1 373 ? 147.427 150.666 141.923 1.00 52.33  ? 383 ALA B CA    1 
ATOM   2893 C  C     . ALA A 1 373 ? 146.336 150.771 142.979 1.00 55.91  ? 383 ALA B C     1 
ATOM   2894 O  O     . ALA A 1 373 ? 146.654 151.031 144.143 1.00 63.41  ? 383 ALA B O     1 
ATOM   2895 C  CB    . ALA A 1 373 ? 148.050 152.041 141.693 1.00 54.59  ? 383 ALA B CB    1 
ATOM   2896 N  N     . ILE A 1 374 ? 145.067 150.587 142.611 1.00 47.57  ? 384 ILE B N     1 
ATOM   2897 C  CA    . ILE A 1 374 ? 143.990 150.606 143.592 1.00 46.79  ? 384 ILE B CA    1 
ATOM   2898 C  C     . ILE A 1 374 ? 144.039 149.413 144.528 1.00 55.96  ? 384 ILE B C     1 
ATOM   2899 O  O     . ILE A 1 374 ? 143.330 149.397 145.539 1.00 62.19  ? 384 ILE B O     1 
ATOM   2900 C  CB    . ILE A 1 374 ? 142.618 150.663 142.890 1.00 49.91  ? 384 ILE B CB    1 
ATOM   2901 C  CG1   . ILE A 1 374 ? 141.590 151.370 143.771 1.00 52.63  ? 384 ILE B CG1   1 
ATOM   2902 C  CG2   . ILE A 1 374 ? 142.142 149.272 142.527 1.00 55.69  ? 384 ILE B CG2   1 
ATOM   2903 C  CD1   . ILE A 1 374 ? 141.878 152.827 143.998 1.00 57.45  ? 384 ILE B CD1   1 
ATOM   2904 N  N     . GLN A 1 375 ? 144.870 148.417 144.226 1.00 53.19  ? 385 GLN B N     1 
ATOM   2905 C  CA    . GLN A 1 375 ? 144.923 147.215 145.042 1.00 49.35  ? 385 GLN B CA    1 
ATOM   2906 C  C     . GLN A 1 375 ? 145.619 147.440 146.374 1.00 54.64  ? 385 GLN B C     1 
ATOM   2907 O  O     . GLN A 1 375 ? 145.463 146.619 147.284 1.00 62.28  ? 385 GLN B O     1 
ATOM   2908 C  CB    . GLN A 1 375 ? 145.623 146.100 144.272 1.00 45.75  ? 385 GLN B CB    1 
ATOM   2909 C  CG    . GLN A 1 375 ? 147.112 146.276 144.175 1.00 50.68  ? 385 GLN B CG    1 
ATOM   2910 C  CD    . GLN A 1 375 ? 147.791 145.092 143.547 1.00 57.59  ? 385 GLN B CD    1 
ATOM   2911 O  OE1   . GLN A 1 375 ? 147.143 144.241 142.942 1.00 63.20  ? 385 GLN B OE1   1 
ATOM   2912 N  NE2   . GLN A 1 375 ? 149.107 145.023 143.687 1.00 57.03  ? 385 GLN B NE2   1 
ATOM   2913 N  N     . GLU A 1 376 ? 146.383 148.522 146.515 1.00 53.37  ? 386 GLU B N     1 
ATOM   2914 C  CA    . GLU A 1 376 ? 147.065 148.773 147.779 1.00 56.40  ? 386 GLU B CA    1 
ATOM   2915 C  C     . GLU A 1 376 ? 146.105 149.294 148.840 1.00 58.85  ? 386 GLU B C     1 
ATOM   2916 O  O     . GLU A 1 376 ? 146.290 149.022 150.034 1.00 68.21  ? 386 GLU B O     1 
ATOM   2917 C  CB    . GLU A 1 376 ? 148.223 149.741 147.564 1.00 55.87  ? 386 GLU B CB    1 
ATOM   2918 C  CG    . GLU A 1 376 ? 147.820 151.110 147.084 1.00 60.73  ? 386 GLU B CG    1 
ATOM   2919 C  CD    . GLU A 1 376 ? 149.016 151.996 146.817 1.00 70.79  ? 386 GLU B CD    1 
ATOM   2920 O  OE1   . GLU A 1 376 ? 150.084 151.456 146.462 1.00 69.35  ? 386 GLU B OE1   1 
ATOM   2921 O  OE2   . GLU A 1 376 ? 148.890 153.230 146.961 1.00 71.38  ? 386 GLU B OE2   1 
ATOM   2922 N  N     . LEU A 1 377 ? 145.073 150.027 148.424 1.00 50.29  ? 387 LEU B N     1 
ATOM   2923 C  CA    . LEU A 1 377 ? 144.027 150.458 149.345 1.00 53.15  ? 387 LEU B CA    1 
ATOM   2924 C  C     . LEU A 1 377 ? 143.357 149.259 150.007 1.00 57.88  ? 387 LEU B C     1 
ATOM   2925 O  O     . LEU A 1 377 ? 143.254 149.179 151.243 1.00 63.76  ? 387 LEU B O     1 
ATOM   2926 C  CB    . LEU A 1 377 ? 143.013 151.294 148.568 1.00 50.45  ? 387 LEU B CB    1 
ATOM   2927 C  CG    . LEU A 1 377 ? 141.878 152.048 149.243 1.00 57.29  ? 387 LEU B CG    1 
ATOM   2928 C  CD1   . LEU A 1 377 ? 141.635 153.325 148.470 1.00 60.60  ? 387 LEU B CD1   1 
ATOM   2929 C  CD2   . LEU A 1 377 ? 140.627 151.194 149.268 1.00 57.55  ? 387 LEU B CD2   1 
ATOM   2930 N  N     . PHE A 1 378 ? 142.915 148.303 149.190 1.00 53.18  ? 388 PHE B N     1 
ATOM   2931 C  CA    . PHE A 1 378 ? 142.296 147.097 149.719 1.00 50.43  ? 388 PHE B CA    1 
ATOM   2932 C  C     . PHE A 1 378 ? 143.285 146.281 150.535 1.00 50.65  ? 388 PHE B C     1 
ATOM   2933 O  O     . PHE A 1 378 ? 142.894 145.627 151.504 1.00 55.94  ? 388 PHE B O     1 
ATOM   2934 C  CB    . PHE A 1 378 ? 141.723 146.263 148.578 1.00 47.01  ? 388 PHE B CB    1 
ATOM   2935 C  CG    . PHE A 1 378 ? 140.701 146.985 147.759 1.00 45.05  ? 388 PHE B CG    1 
ATOM   2936 C  CD1   . PHE A 1 378 ? 139.796 147.839 148.354 1.00 55.47  ? 388 PHE B CD1   1 
ATOM   2937 C  CD2   . PHE A 1 378 ? 140.645 146.814 146.393 1.00 52.11  ? 388 PHE B CD2   1 
ATOM   2938 C  CE1   . PHE A 1 378 ? 138.853 148.506 147.600 1.00 56.16  ? 388 PHE B CE1   1 
ATOM   2939 C  CE2   . PHE A 1 378 ? 139.707 147.478 145.637 1.00 55.16  ? 388 PHE B CE2   1 
ATOM   2940 C  CZ    . PHE A 1 378 ? 138.811 148.326 146.241 1.00 49.94  ? 388 PHE B CZ    1 
ATOM   2941 N  N     . LYS A 1 379 ? 144.566 146.316 150.169 1.00 44.97  ? 389 LYS B N     1 
ATOM   2942 C  CA    . LYS A 1 379 ? 145.574 145.600 150.939 1.00 48.09  ? 389 LYS B CA    1 
ATOM   2943 C  C     . LYS A 1 379 ? 145.704 146.166 152.347 1.00 49.49  ? 389 LYS B C     1 
ATOM   2944 O  O     . LYS A 1 379 ? 145.773 145.408 153.321 1.00 58.12  ? 389 LYS B O     1 
ATOM   2945 C  CB    . LYS A 1 379 ? 146.915 145.647 150.214 1.00 50.55  ? 389 LYS B CB    1 
ATOM   2946 C  CG    . LYS A 1 379 ? 147.256 144.386 149.454 1.00 46.20  ? 389 LYS B CG    1 
ATOM   2947 C  CD    . LYS A 1 379 ? 148.516 144.574 148.634 1.00 51.28  ? 389 LYS B CD    1 
ATOM   2948 C  CE    . LYS A 1 379 ? 149.059 143.249 148.142 1.00 60.76  ? 389 LYS B CE    1 
ATOM   2949 N  NZ    . LYS A 1 379 ? 149.570 142.408 149.260 1.00 58.73  ? 389 LYS B NZ    1 
ATOM   2950 N  N     . ARG A 1 380 ? 145.737 147.494 152.482 1.00 43.54  ? 390 ARG B N     1 
ATOM   2951 C  CA    . ARG A 1 380 ? 145.811 148.083 153.817 1.00 48.28  ? 390 ARG B CA    1 
ATOM   2952 C  C     . ARG A 1 380 ? 144.555 147.785 154.627 1.00 53.57  ? 390 ARG B C     1 
ATOM   2953 O  O     . ARG A 1 380 ? 144.639 147.446 155.819 1.00 60.66  ? 390 ARG B O     1 
ATOM   2954 C  CB    . ARG A 1 380 ? 146.041 149.588 153.727 1.00 50.86  ? 390 ARG B CB    1 
ATOM   2955 C  CG    . ARG A 1 380 ? 147.322 149.974 153.026 1.00 56.24  ? 390 ARG B CG    1 
ATOM   2956 C  CD    . ARG A 1 380 ? 147.430 151.476 152.898 1.00 57.72  ? 390 ARG B CD    1 
ATOM   2957 N  NE    . ARG A 1 380 ? 146.149 152.075 152.553 1.00 61.96  ? 390 ARG B NE    1 
ATOM   2958 C  CZ    . ARG A 1 380 ? 146.013 153.181 151.836 1.00 63.97  ? 390 ARG B CZ    1 
ATOM   2959 N  NH1   . ARG A 1 380 ? 147.063 153.833 151.364 1.00 58.79  ? 390 ARG B NH1   1 
ATOM   2960 N  NH2   . ARG A 1 380 ? 144.792 153.644 151.584 1.00 60.37  ? 390 ARG B NH2   1 
ATOM   2961 N  N     . ILE A 1 381 ? 143.382 147.898 153.998 1.00 49.87  ? 391 ILE B N     1 
ATOM   2962 C  CA    . ILE A 1 381 ? 142.145 147.602 154.717 1.00 47.13  ? 391 ILE B CA    1 
ATOM   2963 C  C     . ILE A 1 381 ? 142.134 146.150 155.182 1.00 48.21  ? 391 ILE B C     1 
ATOM   2964 O  O     . ILE A 1 381 ? 141.744 145.851 156.317 1.00 57.48  ? 391 ILE B O     1 
ATOM   2965 C  CB    . ILE A 1 381 ? 140.921 147.934 153.845 1.00 47.46  ? 391 ILE B CB    1 
ATOM   2966 C  CG1   . ILE A 1 381 ? 140.820 149.438 153.625 1.00 52.22  ? 391 ILE B CG1   1 
ATOM   2967 C  CG2   . ILE A 1 381 ? 139.654 147.450 154.508 1.00 46.72  ? 391 ILE B CG2   1 
ATOM   2968 C  CD1   . ILE A 1 381 ? 139.640 149.846 152.787 1.00 53.62  ? 391 ILE B CD1   1 
ATOM   2969 N  N     . SER A 1 382 ? 142.592 145.231 154.330 1.00 40.10  ? 392 SER B N     1 
ATOM   2970 C  CA    . SER A 1 382 ? 142.627 143.819 154.693 1.00 43.23  ? 392 SER B CA    1 
ATOM   2971 C  C     . SER A 1 382 ? 143.632 143.546 155.802 1.00 47.91  ? 392 SER B C     1 
ATOM   2972 O  O     . SER A 1 382 ? 143.387 142.704 156.672 1.00 53.58  ? 392 SER B O     1 
ATOM   2973 C  CB    . SER A 1 382 ? 142.951 142.973 153.465 1.00 48.97  ? 392 SER B CB    1 
ATOM   2974 O  OG    . SER A 1 382 ? 142.957 141.595 153.786 1.00 58.07  ? 392 SER B OG    1 
ATOM   2975 N  N     . GLU A 1 383 ? 144.780 144.221 155.773 1.00 47.23  ? 393 GLU B N     1 
ATOM   2976 C  CA    . GLU A 1 383 ? 145.766 144.044 156.832 1.00 42.75  ? 393 GLU B CA    1 
ATOM   2977 C  C     . GLU A 1 383 ? 145.191 144.451 158.179 1.00 44.56  ? 393 GLU B C     1 
ATOM   2978 O  O     . GLU A 1 383 ? 145.296 143.710 159.166 1.00 53.83  ? 393 GLU B O     1 
ATOM   2979 C  CB    . GLU A 1 383 ? 147.020 144.855 156.513 1.00 49.38  ? 393 GLU B CB    1 
ATOM   2980 C  CG    . GLU A 1 383 ? 148.201 144.552 157.416 1.00 53.44  ? 393 GLU B CG    1 
ATOM   2981 C  CD    . GLU A 1 383 ? 149.529 144.902 156.774 1.00 59.51  ? 393 GLU B CD    1 
ATOM   2982 O  OE1   . GLU A 1 383 ? 149.539 145.231 155.569 1.00 60.50  ? 393 GLU B OE1   1 
ATOM   2983 O  OE2   . GLU A 1 383 ? 150.562 144.849 157.474 1.00 58.19  ? 393 GLU B OE2   1 
ATOM   2984 N  N     . GLN A 1 384 ? 144.555 145.622 158.232 1.00 39.21  ? 394 GLN B N     1 
ATOM   2985 C  CA    . GLN A 1 384 ? 143.942 146.060 159.482 1.00 38.40  ? 394 GLN B CA    1 
ATOM   2986 C  C     . GLN A 1 384 ? 142.820 145.118 159.909 1.00 44.29  ? 394 GLN B C     1 
ATOM   2987 O  O     . GLN A 1 384 ? 142.681 144.799 161.099 1.00 52.08  ? 394 GLN B O     1 
ATOM   2988 C  CB    . GLN A 1 384 ? 143.431 147.488 159.331 1.00 42.80  ? 394 GLN B CB    1 
ATOM   2989 C  CG    . GLN A 1 384 ? 144.540 148.501 159.201 1.00 43.86  ? 394 GLN B CG    1 
ATOM   2990 C  CD    . GLN A 1 384 ? 144.039 149.920 159.201 1.00 49.71  ? 394 GLN B CD    1 
ATOM   2991 O  OE1   . GLN A 1 384 ? 142.834 150.165 159.193 1.00 55.28  ? 394 GLN B OE1   1 
ATOM   2992 N  NE2   . GLN A 1 384 ? 144.961 150.870 159.213 1.00 44.30  ? 394 GLN B NE2   1 
ATOM   2993 N  N     . PHE A 1 385 ? 142.019 144.652 158.949 1.00 41.67  ? 395 PHE B N     1 
ATOM   2994 C  CA    . PHE A 1 385 ? 140.928 143.731 159.250 1.00 39.20  ? 395 PHE B CA    1 
ATOM   2995 C  C     . PHE A 1 385 ? 141.449 142.443 159.877 1.00 40.99  ? 395 PHE B C     1 
ATOM   2996 O  O     . PHE A 1 385 ? 140.920 141.977 160.890 1.00 44.78  ? 395 PHE B O     1 
ATOM   2997 C  CB    . PHE A 1 385 ? 140.149 143.440 157.967 1.00 40.06  ? 395 PHE B CB    1 
ATOM   2998 C  CG    . PHE A 1 385 ? 139.012 142.478 158.137 1.00 44.34  ? 395 PHE B CG    1 
ATOM   2999 C  CD1   . PHE A 1 385 ? 137.741 142.933 158.409 1.00 42.27  ? 395 PHE B CD1   1 
ATOM   3000 C  CD2   . PHE A 1 385 ? 139.211 141.120 158.001 1.00 48.65  ? 395 PHE B CD2   1 
ATOM   3001 C  CE1   . PHE A 1 385 ? 136.697 142.052 158.554 1.00 42.99  ? 395 PHE B CE1   1 
ATOM   3002 C  CE2   . PHE A 1 385 ? 138.171 140.240 158.147 1.00 43.87  ? 395 PHE B CE2   1 
ATOM   3003 C  CZ    . PHE A 1 385 ? 136.915 140.706 158.424 1.00 40.18  ? 395 PHE B CZ    1 
ATOM   3004 N  N     . THR A 1 386 ? 142.486 141.849 159.284 1.00 44.26  ? 396 THR B N     1 
ATOM   3005 C  CA    . THR A 1 386 ? 143.028 140.606 159.825 1.00 39.57  ? 396 THR B CA    1 
ATOM   3006 C  C     . THR A 1 386 ? 143.677 140.831 161.179 1.00 45.29  ? 396 THR B C     1 
ATOM   3007 O  O     . THR A 1 386 ? 143.593 139.971 162.062 1.00 51.87  ? 396 THR B O     1 
ATOM   3008 C  CB    . THR A 1 386 ? 144.039 139.990 158.863 1.00 41.67  ? 396 THR B CB    1 
ATOM   3009 O  OG1   . THR A 1 386 ? 144.966 140.994 158.435 1.00 48.76  ? 396 THR B OG1   1 
ATOM   3010 C  CG2   . THR A 1 386 ? 143.336 139.412 157.655 1.00 45.55  ? 396 THR B CG2   1 
ATOM   3011 N  N     . ALA A 1 387 ? 144.337 141.974 161.364 1.00 45.45  ? 397 ALA B N     1 
ATOM   3012 C  CA    . ALA A 1 387 ? 144.933 142.260 162.662 1.00 39.27  ? 397 ALA B CA    1 
ATOM   3013 C  C     . ALA A 1 387 ? 143.871 142.334 163.749 1.00 38.61  ? 397 ALA B C     1 
ATOM   3014 O  O     . ALA A 1 387 ? 144.063 141.805 164.849 1.00 44.63  ? 397 ALA B O     1 
ATOM   3015 C  CB    . ALA A 1 387 ? 145.729 143.561 162.599 1.00 39.97  ? 397 ALA B CB    1 
ATOM   3016 N  N     . MET A 1 388 ? 142.740 142.981 163.464 1.00 39.13  ? 398 MET B N     1 
ATOM   3017 C  CA    . MET A 1 388 ? 141.696 143.112 164.476 1.00 33.08  ? 398 MET B CA    1 
ATOM   3018 C  C     . MET A 1 388 ? 140.823 141.873 164.616 1.00 35.41  ? 398 MET B C     1 
ATOM   3019 O  O     . MET A 1 388 ? 140.183 141.705 165.657 1.00 45.16  ? 398 MET B O     1 
ATOM   3020 C  CB    . MET A 1 388 ? 140.798 144.311 164.168 1.00 41.43  ? 398 MET B CB    1 
ATOM   3021 C  CG    . MET A 1 388 ? 141.356 145.638 164.616 1.00 43.57  ? 398 MET B CG    1 
ATOM   3022 S  SD    . MET A 1 388 ? 140.340 147.019 164.083 1.00 55.25  ? 398 MET B SD    1 
ATOM   3023 C  CE    . MET A 1 388 ? 138.774 146.561 164.804 1.00 46.36  ? 398 MET B CE    1 
ATOM   3024 N  N     . PHE A 1 389 ? 140.773 141.008 163.608 1.00 42.57  ? 399 PHE B N     1 
ATOM   3025 C  CA    . PHE A 1 389 ? 139.825 139.901 163.604 1.00 40.85  ? 399 PHE B CA    1 
ATOM   3026 C  C     . PHE A 1 389 ? 140.377 138.626 164.226 1.00 40.26  ? 399 PHE B C     1 
ATOM   3027 O  O     . PHE A 1 389 ? 139.593 137.756 164.616 1.00 45.88  ? 399 PHE B O     1 
ATOM   3028 C  CB    . PHE A 1 389 ? 139.370 139.619 162.171 1.00 42.48  ? 399 PHE B CB    1 
ATOM   3029 C  CG    . PHE A 1 389 ? 138.292 138.587 162.066 1.00 41.18  ? 399 PHE B CG    1 
ATOM   3030 C  CD1   . PHE A 1 389 ? 137.125 138.705 162.783 1.00 41.59  ? 399 PHE B CD1   1 
ATOM   3031 C  CD2   . PHE A 1 389 ? 138.446 137.500 161.234 1.00 43.38  ? 399 PHE B CD2   1 
ATOM   3032 C  CE1   . PHE A 1 389 ? 136.138 137.754 162.677 1.00 45.77  ? 399 PHE B CE1   1 
ATOM   3033 C  CE2   . PHE A 1 389 ? 137.463 136.551 161.128 1.00 40.65  ? 399 PHE B CE2   1 
ATOM   3034 C  CZ    . PHE A 1 389 ? 136.309 136.678 161.849 1.00 43.41  ? 399 PHE B CZ    1 
ATOM   3035 N  N     . ARG A 1 390 ? 141.698 138.493 164.330 1.00 44.57  ? 400 ARG B N     1 
ATOM   3036 C  CA    . ARG A 1 390 ? 142.270 137.322 164.984 1.00 44.17  ? 400 ARG B CA    1 
ATOM   3037 C  C     . ARG A 1 390 ? 141.873 137.265 166.453 1.00 52.64  ? 400 ARG B C     1 
ATOM   3038 O  O     . ARG A 1 390 ? 141.569 136.190 166.980 1.00 54.95  ? 400 ARG B O     1 
ATOM   3039 C  CB    . ARG A 1 390 ? 143.790 137.330 164.842 1.00 44.57  ? 400 ARG B CB    1 
ATOM   3040 C  CG    . ARG A 1 390 ? 144.282 137.135 163.427 1.00 50.80  ? 400 ARG B CG    1 
ATOM   3041 C  CD    . ARG A 1 390 ? 145.669 136.524 163.415 1.00 51.98  ? 400 ARG B CD    1 
ATOM   3042 N  NE    . ARG A 1 390 ? 146.546 137.154 164.394 1.00 53.98  ? 400 ARG B NE    1 
ATOM   3043 C  CZ    . ARG A 1 390 ? 147.432 138.097 164.108 1.00 58.19  ? 400 ARG B CZ    1 
ATOM   3044 N  NH1   . ARG A 1 390 ? 147.591 138.543 162.872 1.00 54.66  ? 400 ARG B NH1   1 
ATOM   3045 N  NH2   . ARG A 1 390 ? 148.178 138.606 165.085 1.00 55.90  ? 400 ARG B NH2   1 
ATOM   3046 N  N     . ARG A 1 391 ? 141.873 138.409 167.127 1.00 49.33  ? 401 ARG B N     1 
ATOM   3047 C  CA    . ARG A 1 391 ? 141.494 138.501 168.527 1.00 41.93  ? 401 ARG B CA    1 
ATOM   3048 C  C     . ARG A 1 391 ? 139.994 138.632 168.729 1.00 40.28  ? 401 ARG B C     1 
ATOM   3049 O  O     . ARG A 1 391 ? 139.538 138.624 169.874 1.00 47.30  ? 401 ARG B O     1 
ATOM   3050 C  CB    . ARG A 1 391 ? 142.196 139.689 169.179 1.00 43.04  ? 401 ARG B CB    1 
ATOM   3051 C  CG    . ARG A 1 391 ? 143.693 139.628 169.080 1.00 42.00  ? 401 ARG B CG    1 
ATOM   3052 C  CD    . ARG A 1 391 ? 144.203 138.362 169.710 1.00 39.70  ? 401 ARG B CD    1 
ATOM   3053 N  NE    . ARG A 1 391 ? 145.292 138.624 170.637 1.00 42.28  ? 401 ARG B NE    1 
ATOM   3054 C  CZ    . ARG A 1 391 ? 145.140 138.747 171.946 1.00 45.40  ? 401 ARG B CZ    1 
ATOM   3055 N  NH1   . ARG A 1 391 ? 143.955 138.625 172.517 1.00 46.70  ? 401 ARG B NH1   1 
ATOM   3056 N  NH2   . ARG A 1 391 ? 146.205 138.993 172.701 1.00 45.68  ? 401 ARG B NH2   1 
ATOM   3057 N  N     . LYS A 1 392 ? 139.225 138.753 167.650 1.00 40.06  ? 402 LYS B N     1 
ATOM   3058 C  CA    . LYS A 1 392 ? 137.786 138.987 167.726 1.00 40.22  ? 402 LYS B CA    1 
ATOM   3059 C  C     . LYS A 1 392 ? 137.471 140.233 168.548 1.00 44.29  ? 402 LYS B C     1 
ATOM   3060 O  O     . LYS A 1 392 ? 136.576 140.232 169.393 1.00 52.28  ? 402 LYS B O     1 
ATOM   3061 C  CB    . LYS A 1 392 ? 137.058 137.764 168.279 1.00 47.31  ? 402 LYS B CB    1 
ATOM   3062 C  CG    . LYS A 1 392 ? 137.358 136.485 167.530 1.00 52.37  ? 402 LYS B CG    1 
ATOM   3063 C  CD    . LYS A 1 392 ? 136.369 135.396 167.889 1.00 52.05  ? 402 LYS B CD    1 
ATOM   3064 C  CE    . LYS A 1 392 ? 136.711 134.090 167.198 1.00 50.55  ? 402 LYS B CE    1 
ATOM   3065 N  NZ    . LYS A 1 392 ? 136.884 134.269 165.732 1.00 54.89  ? 402 LYS B NZ    1 
ATOM   3066 N  N     . ALA A 1 393 ? 138.213 141.305 168.295 1.00 41.26  ? 403 ALA B N     1 
ATOM   3067 C  CA    . ALA A 1 393 ? 138.012 142.557 169.006 1.00 42.19  ? 403 ALA B CA    1 
ATOM   3068 C  C     . ALA A 1 393 ? 136.839 143.332 168.427 1.00 42.69  ? 403 ALA B C     1 
ATOM   3069 O  O     . ALA A 1 393 ? 136.642 143.372 167.211 1.00 51.73  ? 403 ALA B O     1 
ATOM   3070 C  CB    . ALA A 1 393 ? 139.277 143.409 168.948 1.00 45.95  ? 403 ALA B CB    1 
ATOM   3071 N  N     . PHE A 1 394 ? 136.060 143.951 169.315 1.00 33.16  ? 404 PHE B N     1 
ATOM   3072 C  CA    . PHE A 1 394 ? 134.888 144.744 168.948 1.00 27.96  ? 404 PHE B CA    1 
ATOM   3073 C  C     . PHE A 1 394 ? 133.885 143.940 168.131 1.00 34.71  ? 404 PHE B C     1 
ATOM   3074 O  O     . PHE A 1 394 ? 133.101 144.504 167.368 1.00 51.58  ? 404 PHE B O     1 
ATOM   3075 C  CB    . PHE A 1 394 ? 135.277 146.013 168.189 1.00 35.22  ? 404 PHE B CB    1 
ATOM   3076 C  CG    . PHE A 1 394 ? 136.338 146.832 168.858 1.00 36.75  ? 404 PHE B CG    1 
ATOM   3077 C  CD1   . PHE A 1 394 ? 136.007 147.772 169.806 1.00 34.44  ? 404 PHE B CD1   1 
ATOM   3078 C  CD2   . PHE A 1 394 ? 137.661 146.686 168.507 1.00 39.51  ? 404 PHE B CD2   1 
ATOM   3079 C  CE1   . PHE A 1 394 ? 136.977 148.532 170.404 1.00 36.85  ? 404 PHE B CE1   1 
ATOM   3080 C  CE2   . PHE A 1 394 ? 138.632 147.442 169.104 1.00 39.36  ? 404 PHE B CE2   1 
ATOM   3081 C  CZ    . PHE A 1 394 ? 138.289 148.369 170.053 1.00 39.96  ? 404 PHE B CZ    1 
ATOM   3082 N  N     . LEU A 1 395 ? 133.887 142.619 168.287 1.00 35.75  ? 405 LEU B N     1 
ATOM   3083 C  CA    . LEU A 1 395 ? 133.043 141.761 167.472 1.00 38.56  ? 405 LEU B CA    1 
ATOM   3084 C  C     . LEU A 1 395 ? 131.691 141.469 168.100 1.00 36.04  ? 405 LEU B C     1 
ATOM   3085 O  O     . LEU A 1 395 ? 130.791 141.001 167.397 1.00 43.88  ? 405 LEU B O     1 
ATOM   3086 C  CB    . LEU A 1 395 ? 133.754 140.436 167.181 1.00 39.75  ? 405 LEU B CB    1 
ATOM   3087 C  CG    . LEU A 1 395 ? 133.448 139.777 165.838 1.00 44.69  ? 405 LEU B CG    1 
ATOM   3088 C  CD1   . LEU A 1 395 ? 133.937 140.657 164.708 1.00 47.06  ? 405 LEU B CD1   1 
ATOM   3089 C  CD2   . LEU A 1 395 ? 134.085 138.410 165.757 1.00 42.85  ? 405 LEU B CD2   1 
ATOM   3090 N  N     . HIS A 1 396 ? 131.525 141.720 169.395 1.00 36.86  ? 406 HIS B N     1 
ATOM   3091 C  CA    . HIS A 1 396 ? 130.240 141.488 170.035 1.00 34.75  ? 406 HIS B CA    1 
ATOM   3092 C  C     . HIS A 1 396 ? 129.261 142.624 169.798 1.00 39.98  ? 406 HIS B C     1 
ATOM   3093 O  O     . HIS A 1 396 ? 128.064 142.454 170.045 1.00 46.48  ? 406 HIS B O     1 
ATOM   3094 C  CB    . HIS A 1 396 ? 130.428 141.269 171.534 1.00 36.42  ? 406 HIS B CB    1 
ATOM   3095 C  CG    . HIS A 1 396 ? 130.855 142.494 172.273 1.00 35.46  ? 406 HIS B CG    1 
ATOM   3096 N  ND1   . HIS A 1 396 ? 132.129 143.006 172.190 1.00 43.19  ? 406 HIS B ND1   1 
ATOM   3097 C  CD2   . HIS A 1 396 ? 130.175 143.308 173.112 1.00 33.46  ? 406 HIS B CD2   1 
ATOM   3098 C  CE1   . HIS A 1 396 ? 132.216 144.086 172.945 1.00 46.21  ? 406 HIS B CE1   1 
ATOM   3099 N  NE2   . HIS A 1 396 ? 131.043 144.291 173.514 1.00 41.44  ? 406 HIS B NE2   1 
ATOM   3100 N  N     . TRP A 1 397 ? 129.738 143.776 169.332 1.00 41.65  ? 407 TRP B N     1 
ATOM   3101 C  CA    . TRP A 1 397 ? 128.823 144.827 168.916 1.00 34.97  ? 407 TRP B CA    1 
ATOM   3102 C  C     . TRP A 1 397 ? 128.139 144.472 167.606 1.00 44.57  ? 407 TRP B C     1 
ATOM   3103 O  O     . TRP A 1 397 ? 127.096 145.045 167.276 1.00 51.78  ? 407 TRP B O     1 
ATOM   3104 C  CB    . TRP A 1 397 ? 129.562 146.155 168.780 1.00 33.36  ? 407 TRP B CB    1 
ATOM   3105 C  CG    . TRP A 1 397 ? 130.058 146.721 170.064 1.00 39.36  ? 407 TRP B CG    1 
ATOM   3106 C  CD1   . TRP A 1 397 ? 131.354 146.859 170.444 1.00 39.55  ? 407 TRP B CD1   1 
ATOM   3107 C  CD2   . TRP A 1 397 ? 129.269 147.245 171.135 1.00 40.44  ? 407 TRP B CD2   1 
ATOM   3108 N  NE1   . TRP A 1 397 ? 131.425 147.427 171.687 1.00 38.12  ? 407 TRP B NE1   1 
ATOM   3109 C  CE2   . TRP A 1 397 ? 130.155 147.673 172.134 1.00 38.83  ? 407 TRP B CE2   1 
ATOM   3110 C  CE3   . TRP A 1 397 ? 127.896 147.383 171.349 1.00 42.83  ? 407 TRP B CE3   1 
ATOM   3111 C  CZ2   . TRP A 1 397 ? 129.719 148.236 173.324 1.00 35.80  ? 407 TRP B CZ2   1 
ATOM   3112 C  CZ3   . TRP A 1 397 ? 127.466 147.941 172.530 1.00 44.04  ? 407 TRP B CZ3   1 
ATOM   3113 C  CH2   . TRP A 1 397 ? 128.373 148.361 173.503 1.00 37.58  ? 407 TRP B CH2   1 
ATOM   3114 N  N     . TYR A 1 398 ? 128.715 143.539 166.848 1.00 42.47  ? 408 TYR B N     1 
ATOM   3115 C  CA    . TYR A 1 398 ? 128.139 143.140 165.571 1.00 35.74  ? 408 TYR B CA    1 
ATOM   3116 C  C     . TYR A 1 398 ? 127.309 141.872 165.699 1.00 44.79  ? 408 TYR B C     1 
ATOM   3117 O  O     . TYR A 1 398 ? 126.228 141.776 165.111 1.00 54.20  ? 408 TYR B O     1 
ATOM   3118 C  CB    . TYR A 1 398 ? 129.244 142.945 164.539 1.00 34.58  ? 408 TYR B CB    1 
ATOM   3119 C  CG    . TYR A 1 398 ? 129.965 144.211 164.158 1.00 41.88  ? 408 TYR B CG    1 
ATOM   3120 C  CD1   . TYR A 1 398 ? 130.911 144.771 164.996 1.00 43.02  ? 408 TYR B CD1   1 
ATOM   3121 C  CD2   . TYR A 1 398 ? 129.712 144.839 162.954 1.00 42.33  ? 408 TYR B CD2   1 
ATOM   3122 C  CE1   . TYR A 1 398 ? 131.571 145.921 164.651 1.00 38.87  ? 408 TYR B CE1   1 
ATOM   3123 C  CE2   . TYR A 1 398 ? 130.370 145.988 162.602 1.00 37.17  ? 408 TYR B CE2   1 
ATOM   3124 C  CZ    . TYR A 1 398 ? 131.296 146.523 163.455 1.00 36.70  ? 408 TYR B CZ    1 
ATOM   3125 O  OH    . TYR A 1 398 ? 131.959 147.672 163.109 1.00 43.39  ? 408 TYR B OH    1 
ATOM   3126 N  N     . THR A 1 399 ? 127.794 140.888 166.456 1.00 40.36  ? 409 THR B N     1 
ATOM   3127 C  CA    . THR A 1 399 ? 127.037 139.660 166.660 1.00 36.16  ? 409 THR B CA    1 
ATOM   3128 C  C     . THR A 1 399 ? 125.823 139.859 167.552 1.00 43.97  ? 409 THR B C     1 
ATOM   3129 O  O     . THR A 1 399 ? 124.990 138.953 167.644 1.00 52.24  ? 409 THR B O     1 
ATOM   3130 C  CB    . THR A 1 399 ? 127.929 138.576 167.253 1.00 40.95  ? 409 THR B CB    1 
ATOM   3131 O  OG1   . THR A 1 399 ? 128.437 139.015 168.518 1.00 48.64  ? 409 THR B OG1   1 
ATOM   3132 C  CG2   . THR A 1 399 ? 129.085 138.282 166.328 1.00 43.93  ? 409 THR B CG2   1 
ATOM   3133 N  N     . GLY A 1 400 ? 125.706 141.004 168.206 1.00 46.68  ? 410 GLY B N     1 
ATOM   3134 C  CA    . GLY A 1 400 ? 124.529 141.327 168.975 1.00 42.98  ? 410 GLY B CA    1 
ATOM   3135 C  C     . GLY A 1 400 ? 123.384 141.896 168.180 1.00 48.27  ? 410 GLY B C     1 
ATOM   3136 O  O     . GLY A 1 400 ? 122.328 142.183 168.748 1.00 56.41  ? 410 GLY B O     1 
ATOM   3137 N  N     . GLU A 1 401 ? 123.559 142.072 166.873 1.00 52.64  ? 411 GLU B N     1 
ATOM   3138 C  CA    . GLU A 1 401 ? 122.524 142.621 166.012 1.00 56.22  ? 411 GLU B CA    1 
ATOM   3139 C  C     . GLU A 1 401 ? 121.997 141.616 165.001 1.00 59.40  ? 411 GLU B C     1 
ATOM   3140 O  O     . GLU A 1 401 ? 121.027 141.918 164.297 1.00 64.19  ? 411 GLU B O     1 
ATOM   3141 C  CB    . GLU A 1 401 ? 123.048 143.859 165.277 1.00 55.29  ? 411 GLU B CB    1 
ATOM   3142 C  CG    . GLU A 1 401 ? 123.650 144.912 166.182 1.00 56.38  ? 411 GLU B CG    1 
ATOM   3143 C  CD    . GLU A 1 401 ? 122.618 145.586 167.059 1.00 63.32  ? 411 GLU B CD    1 
ATOM   3144 O  OE1   . GLU A 1 401 ? 121.454 145.704 166.626 1.00 63.25  ? 411 GLU B OE1   1 
ATOM   3145 O  OE2   . GLU A 1 401 ? 122.970 145.998 168.184 1.00 63.58  ? 411 GLU B OE2   1 
ATOM   3146 N  N     . GLY A 1 402 ? 122.600 140.436 164.905 1.00 48.52  ? 412 GLY B N     1 
ATOM   3147 C  CA    . GLY A 1 402 ? 122.106 139.425 163.995 1.00 51.56  ? 412 GLY B CA    1 
ATOM   3148 C  C     . GLY A 1 402 ? 123.070 139.074 162.884 1.00 56.30  ? 412 GLY B C     1 
ATOM   3149 O  O     . GLY A 1 402 ? 122.650 138.727 161.777 1.00 62.28  ? 412 GLY B O     1 
ATOM   3150 N  N     . MET A 1 403 ? 124.361 139.158 163.162 1.00 47.16  ? 413 MET B N     1 
ATOM   3151 C  CA    . MET A 1 403 ? 125.393 138.871 162.185 1.00 48.66  ? 413 MET B CA    1 
ATOM   3152 C  C     . MET A 1 403 ? 126.055 137.533 162.499 1.00 55.10  ? 413 MET B C     1 
ATOM   3153 O  O     . MET A 1 403 ? 125.639 136.805 163.405 1.00 57.63  ? 413 MET B O     1 
ATOM   3154 C  CB    . MET A 1 403 ? 126.406 140.010 162.150 1.00 52.20  ? 413 MET B CB    1 
ATOM   3155 C  CG    . MET A 1 403 ? 125.938 141.206 161.367 1.00 54.74  ? 413 MET B CG    1 
ATOM   3156 S  SD    . MET A 1 403 ? 126.718 141.311 159.755 1.00 64.89  ? 413 MET B SD    1 
ATOM   3157 C  CE    . MET A 1 403 ? 128.406 141.578 160.242 1.00 51.42  ? 413 MET B CE    1 
ATOM   3158 N  N     . ASP A 1 404 ? 127.096 137.208 161.738 1.00 63.66  ? 414 ASP B N     1 
ATOM   3159 C  CA    . ASP A 1 404 ? 127.841 135.977 161.939 1.00 62.63  ? 414 ASP B CA    1 
ATOM   3160 C  C     . ASP A 1 404 ? 129.282 136.193 161.503 1.00 65.04  ? 414 ASP B C     1 
ATOM   3161 O  O     . ASP A 1 404 ? 129.583 137.077 160.699 1.00 72.29  ? 414 ASP B O     1 
ATOM   3162 C  CB    . ASP A 1 404 ? 127.216 134.814 161.165 1.00 65.28  ? 414 ASP B CB    1 
ATOM   3163 C  CG    . ASP A 1 404 ? 126.116 134.124 161.939 1.00 71.34  ? 414 ASP B CG    1 
ATOM   3164 O  OD1   . ASP A 1 404 ? 126.264 133.962 163.169 1.00 68.64  ? 414 ASP B OD1   1 
ATOM   3165 O  OD2   . ASP A 1 404 ? 125.103 133.740 161.319 1.00 72.12  ? 414 ASP B OD2   1 
ATOM   3166 N  N     . GLU A 1 405 ? 130.176 135.366 162.049 1.00 55.42  ? 415 GLU B N     1 
ATOM   3167 C  CA    . GLU A 1 405 ? 131.583 135.444 161.672 1.00 55.56  ? 415 GLU B CA    1 
ATOM   3168 C  C     . GLU A 1 405 ? 131.804 134.991 160.235 1.00 62.75  ? 415 GLU B C     1 
ATOM   3169 O  O     . GLU A 1 405 ? 132.754 135.442 159.574 1.00 68.77  ? 415 GLU B O     1 
ATOM   3170 C  CB    . GLU A 1 405 ? 132.421 134.602 162.628 1.00 58.37  ? 415 GLU B CB    1 
ATOM   3171 C  CG    . GLU A 1 405 ? 132.178 134.909 164.088 1.00 61.39  ? 415 GLU B CG    1 
ATOM   3172 C  CD    . GLU A 1 405 ? 133.115 134.151 165.002 1.00 66.16  ? 415 GLU B CD    1 
ATOM   3173 O  OE1   . GLU A 1 405 ? 134.137 133.631 164.507 1.00 68.45  ? 415 GLU B OE1   1 
ATOM   3174 O  OE2   . GLU A 1 405 ? 132.832 134.073 166.216 1.00 64.07  ? 415 GLU B OE2   1 
ATOM   3175 N  N     . MET A 1 406 ? 130.943 134.102 159.740 1.00 60.17  ? 416 MET B N     1 
ATOM   3176 C  CA    . MET A 1 406 ? 131.060 133.652 158.361 1.00 61.97  ? 416 MET B CA    1 
ATOM   3177 C  C     . MET A 1 406 ? 130.905 134.806 157.384 1.00 61.72  ? 416 MET B C     1 
ATOM   3178 O  O     . MET A 1 406 ? 131.528 134.799 156.317 1.00 66.19  ? 416 MET B O     1 
ATOM   3179 C  CB    . MET A 1 406 ? 130.031 132.562 158.076 1.00 64.76  ? 416 MET B CB    1 
ATOM   3180 C  CG    . MET A 1 406 ? 130.384 131.223 158.690 1.00 68.78  ? 416 MET B CG    1 
ATOM   3181 S  SD    . MET A 1 406 ? 132.126 130.819 158.481 1.00 78.48  ? 416 MET B SD    1 
ATOM   3182 C  CE    . MET A 1 406 ? 132.215 130.605 156.707 1.00 64.97  ? 416 MET B CE    1 
ATOM   3183 N  N     . GLU A 1 407 ? 130.090 135.804 157.727 1.00 51.84  ? 417 GLU B N     1 
ATOM   3184 C  CA    . GLU A 1 407 ? 130.001 136.988 156.884 1.00 54.47  ? 417 GLU B CA    1 
ATOM   3185 C  C     . GLU A 1 407 ? 131.344 137.698 156.798 1.00 58.22  ? 417 GLU B C     1 
ATOM   3186 O  O     . GLU A 1 407 ? 131.765 138.123 155.713 1.00 67.01  ? 417 GLU B O     1 
ATOM   3187 C  CB    . GLU A 1 407 ? 128.930 137.934 157.415 1.00 60.12  ? 417 GLU B CB    1 
ATOM   3188 C  CG    . GLU A 1 407 ? 127.528 137.583 156.980 1.00 64.45  ? 417 GLU B CG    1 
ATOM   3189 C  CD    . GLU A 1 407 ? 126.894 138.681 156.154 1.00 67.07  ? 417 GLU B CD    1 
ATOM   3190 O  OE1   . GLU A 1 407 ? 127.602 139.653 155.821 1.00 64.75  ? 417 GLU B OE1   1 
ATOM   3191 O  OE2   . GLU A 1 407 ? 125.690 138.573 155.840 1.00 66.59  ? 417 GLU B OE2   1 
ATOM   3192 N  N     . PHE A 1 408 ? 132.034 137.831 157.931 1.00 42.08  ? 418 PHE B N     1 
ATOM   3193 C  CA    . PHE A 1 408 ? 133.346 138.460 157.922 1.00 42.63  ? 418 PHE B CA    1 
ATOM   3194 C  C     . PHE A 1 408 ? 134.321 137.678 157.052 1.00 46.65  ? 418 PHE B C     1 
ATOM   3195 O  O     . PHE A 1 408 ? 135.069 138.265 156.257 1.00 57.39  ? 418 PHE B O     1 
ATOM   3196 C  CB    . PHE A 1 408 ? 133.883 138.577 159.345 1.00 50.87  ? 418 PHE B CB    1 
ATOM   3197 C  CG    . PHE A 1 408 ? 133.224 139.644 160.163 1.00 48.37  ? 418 PHE B CG    1 
ATOM   3198 C  CD1   . PHE A 1 408 ? 131.986 139.439 160.725 1.00 45.27  ? 418 PHE B CD1   1 
ATOM   3199 C  CD2   . PHE A 1 408 ? 133.859 140.846 160.386 1.00 51.03  ? 418 PHE B CD2   1 
ATOM   3200 C  CE1   . PHE A 1 408 ? 131.393 140.416 161.482 1.00 48.57  ? 418 PHE B CE1   1 
ATOM   3201 C  CE2   . PHE A 1 408 ? 133.266 141.824 161.143 1.00 51.46  ? 418 PHE B CE2   1 
ATOM   3202 C  CZ    . PHE A 1 408 ? 132.033 141.608 161.688 1.00 49.83  ? 418 PHE B CZ    1 
ATOM   3203 N  N     . THR A 1 409 ? 134.326 136.351 157.188 1.00 49.17  ? 419 THR B N     1 
ATOM   3204 C  CA    . THR A 1 409 ? 135.260 135.545 156.405 1.00 44.88  ? 419 THR B CA    1 
ATOM   3205 C  C     . THR A 1 409 ? 134.952 135.627 154.913 1.00 51.18  ? 419 THR B C     1 
ATOM   3206 O  O     . THR A 1 409 ? 135.871 135.713 154.087 1.00 61.92  ? 419 THR B O     1 
ATOM   3207 C  CB    . THR A 1 409 ? 135.234 134.100 156.886 1.00 51.90  ? 419 THR B CB    1 
ATOM   3208 O  OG1   . THR A 1 409 ? 135.375 134.076 158.309 1.00 55.91  ? 419 THR B OG1   1 
ATOM   3209 C  CG2   . THR A 1 409 ? 136.374 133.317 156.264 1.00 54.01  ? 419 THR B CG2   1 
ATOM   3210 N  N     . GLU A 1 410 ? 133.668 135.618 154.547 1.00 46.30  ? 420 GLU B N     1 
ATOM   3211 C  CA    . GLU A 1 410 ? 133.295 135.755 153.144 1.00 46.37  ? 420 GLU B CA    1 
ATOM   3212 C  C     . GLU A 1 410 ? 133.721 137.104 152.580 1.00 50.39  ? 420 GLU B C     1 
ATOM   3213 O  O     . GLU A 1 410 ? 134.228 137.181 151.453 1.00 57.08  ? 420 GLU B O     1 
ATOM   3214 C  CB    . GLU A 1 410 ? 131.791 135.562 152.976 1.00 50.40  ? 420 GLU B CB    1 
ATOM   3215 C  CG    . GLU A 1 410 ? 131.334 134.131 153.110 1.00 57.94  ? 420 GLU B CG    1 
ATOM   3216 C  CD    . GLU A 1 410 ? 129.829 134.005 153.112 1.00 63.99  ? 420 GLU B CD    1 
ATOM   3217 O  OE1   . GLU A 1 410 ? 129.146 135.040 152.975 1.00 61.86  ? 420 GLU B OE1   1 
ATOM   3218 O  OE2   . GLU A 1 410 ? 129.327 132.870 153.253 1.00 65.26  ? 420 GLU B OE2   1 
ATOM   3219 N  N     . ALA A 1 411 ? 133.517 138.182 153.340 1.00 43.24  ? 421 ALA B N     1 
ATOM   3220 C  CA    . ALA A 1 411 ? 133.933 139.498 152.866 1.00 37.39  ? 421 ALA B CA    1 
ATOM   3221 C  C     . ALA A 1 411 ? 135.441 139.565 152.682 1.00 40.82  ? 421 ALA B C     1 
ATOM   3222 O  O     . ALA A 1 411 ? 135.934 140.132 151.696 1.00 48.37  ? 421 ALA B O     1 
ATOM   3223 C  CB    . ALA A 1 411 ? 133.460 140.577 153.837 1.00 41.32  ? 421 ALA B CB    1 
ATOM   3224 N  N     . GLU A 1 412 ? 136.193 138.983 153.616 1.00 42.25  ? 422 GLU B N     1 
ATOM   3225 C  CA    . GLU A 1 412 ? 137.644 138.975 153.482 1.00 42.88  ? 422 GLU B CA    1 
ATOM   3226 C  C     . GLU A 1 412 ? 138.079 138.203 152.242 1.00 50.80  ? 422 GLU B C     1 
ATOM   3227 O  O     . GLU A 1 412 ? 138.968 138.648 151.502 1.00 62.00  ? 422 GLU B O     1 
ATOM   3228 C  CB    . GLU A 1 412 ? 138.278 138.387 154.739 1.00 45.93  ? 422 GLU B CB    1 
ATOM   3229 C  CG    . GLU A 1 412 ? 139.788 138.422 154.752 1.00 51.96  ? 422 GLU B CG    1 
ATOM   3230 C  CD    . GLU A 1 412 ? 140.373 137.541 155.834 1.00 61.39  ? 422 GLU B CD    1 
ATOM   3231 O  OE1   . GLU A 1 412 ? 139.595 137.012 156.654 1.00 56.43  ? 422 GLU B OE1   1 
ATOM   3232 O  OE2   . GLU A 1 412 ? 141.609 137.369 155.859 1.00 65.27  ? 422 GLU B OE2   1 
ATOM   3233 N  N     . SER A 1 413 ? 137.460 137.047 151.992 1.00 45.58  ? 423 SER B N     1 
ATOM   3234 C  CA    . SER A 1 413 ? 137.821 136.259 150.817 1.00 42.04  ? 423 SER B CA    1 
ATOM   3235 C  C     . SER A 1 413 ? 137.484 136.999 149.529 1.00 44.95  ? 423 SER B C     1 
ATOM   3236 O  O     . SER A 1 413 ? 138.244 136.941 148.555 1.00 47.79  ? 423 SER B O     1 
ATOM   3237 C  CB    . SER A 1 413 ? 137.123 134.904 150.854 1.00 42.85  ? 423 SER B CB    1 
ATOM   3238 O  OG    . SER A 1 413 ? 135.752 135.034 150.537 1.00 46.10  ? 423 SER B OG    1 
ATOM   3239 N  N     . ASN A 1 414 ? 136.347 137.695 149.501 1.00 40.98  ? 424 ASN B N     1 
ATOM   3240 C  CA    . ASN A 1 414 ? 135.986 138.470 148.318 1.00 36.77  ? 424 ASN B CA    1 
ATOM   3241 C  C     . ASN A 1 414 ? 136.991 139.583 148.051 1.00 46.45  ? 424 ASN B C     1 
ATOM   3242 O  O     . ASN A 1 414 ? 137.406 139.796 146.903 1.00 50.23  ? 424 ASN B O     1 
ATOM   3243 C  CB    . ASN A 1 414 ? 134.585 139.047 148.477 1.00 38.40  ? 424 ASN B CB    1 
ATOM   3244 C  CG    . ASN A 1 414 ? 133.799 139.003 147.198 1.00 40.16  ? 424 ASN B CG    1 
ATOM   3245 O  OD1   . ASN A 1 414 ? 134.109 138.232 146.296 1.00 49.62  ? 424 ASN B OD1   1 
ATOM   3246 N  ND2   . ASN A 1 414 ? 132.778 139.836 147.102 1.00 38.53  ? 424 ASN B ND2   1 
ATOM   3247 N  N     . MET A 1 415 ? 137.397 140.305 149.098 1.00 51.32  ? 425 MET B N     1 
ATOM   3248 C  CA    . MET A 1 415 ? 138.409 141.340 148.915 1.00 43.46  ? 425 MET B CA    1 
ATOM   3249 C  C     . MET A 1 415 ? 139.718 140.750 148.407 1.00 44.05  ? 425 MET B C     1 
ATOM   3250 O  O     . MET A 1 415 ? 140.372 141.329 147.529 1.00 52.74  ? 425 MET B O     1 
ATOM   3251 C  CB    . MET A 1 415 ? 138.642 142.092 150.222 1.00 43.75  ? 425 MET B CB    1 
ATOM   3252 C  CG    . MET A 1 415 ? 138.787 143.586 150.064 1.00 42.63  ? 425 MET B CG    1 
ATOM   3253 S  SD    . MET A 1 415 ? 138.883 144.428 151.647 1.00 67.43  ? 425 MET B SD    1 
ATOM   3254 C  CE    . MET A 1 415 ? 137.626 145.672 151.444 1.00 52.76  ? 425 MET B CE    1 
ATOM   3255 N  N     . ASN A 1 416 ? 140.127 139.606 148.960 1.00 39.66  ? 426 ASN B N     1 
ATOM   3256 C  CA    . ASN A 1 416 ? 141.369 138.979 148.519 1.00 37.96  ? 426 ASN B CA    1 
ATOM   3257 C  C     . ASN A 1 416 ? 141.289 138.567 147.055 1.00 42.76  ? 426 ASN B C     1 
ATOM   3258 O  O     . ASN A 1 416 ? 142.263 138.713 146.306 1.00 47.59  ? 426 ASN B O     1 
ATOM   3259 C  CB    . ASN A 1 416 ? 141.689 137.771 149.395 1.00 40.51  ? 426 ASN B CB    1 
ATOM   3260 C  CG    . ASN A 1 416 ? 142.071 138.160 150.803 1.00 48.29  ? 426 ASN B CG    1 
ATOM   3261 O  OD1   . ASN A 1 416 ? 142.816 139.114 151.015 1.00 48.04  ? 426 ASN B OD1   1 
ATOM   3262 N  ND2   . ASN A 1 416 ? 141.565 137.418 151.779 1.00 50.09  ? 426 ASN B ND2   1 
ATOM   3263 N  N     . ASP A 1 417 ? 140.140 138.039 146.632 1.00 47.41  ? 427 ASP B N     1 
ATOM   3264 C  CA    . ASP A 1 417 ? 139.968 137.668 145.231 1.00 47.08  ? 427 ASP B CA    1 
ATOM   3265 C  C     . ASP A 1 417 ? 140.022 138.892 144.326 1.00 49.38  ? 427 ASP B C     1 
ATOM   3266 O  O     . ASP A 1 417 ? 140.573 138.830 143.222 1.00 53.82  ? 427 ASP B O     1 
ATOM   3267 C  CB    . ASP A 1 417 ? 138.657 136.910 145.046 1.00 52.64  ? 427 ASP B CB    1 
ATOM   3268 C  CG    . ASP A 1 417 ? 138.838 135.411 145.158 1.00 59.31  ? 427 ASP B CG    1 
ATOM   3269 O  OD1   . ASP A 1 417 ? 139.991 134.966 145.333 1.00 60.52  ? 427 ASP B OD1   1 
ATOM   3270 O  OD2   . ASP A 1 417 ? 137.833 134.676 145.075 1.00 61.77  ? 427 ASP B OD2   1 
ATOM   3271 N  N     . LEU A 1 418 ? 139.469 140.016 144.780 1.00 45.05  ? 428 LEU B N     1 
ATOM   3272 C  CA    . LEU A 1 418 ? 139.576 141.250 144.004 1.00 37.62  ? 428 LEU B CA    1 
ATOM   3273 C  C     . LEU A 1 418 ? 141.029 141.693 143.860 1.00 39.62  ? 428 LEU B C     1 
ATOM   3274 O  O     . LEU A 1 418 ? 141.468 142.083 142.767 1.00 46.40  ? 428 LEU B O     1 
ATOM   3275 C  CB    . LEU A 1 418 ? 138.740 142.344 144.659 1.00 44.92  ? 428 LEU B CB    1 
ATOM   3276 C  CG    . LEU A 1 418 ? 138.393 143.564 143.819 1.00 42.46  ? 428 LEU B CG    1 
ATOM   3277 C  CD1   . LEU A 1 418 ? 137.666 143.138 142.566 1.00 45.38  ? 428 LEU B CD1   1 
ATOM   3278 C  CD2   . LEU A 1 418 ? 137.542 144.505 144.629 1.00 41.24  ? 428 LEU B CD2   1 
ATOM   3279 N  N     . VAL A 1 419 ? 141.795 141.624 144.951 1.00 39.90  ? 429 VAL B N     1 
ATOM   3280 C  CA    . VAL A 1 419 ? 143.206 142.000 144.898 1.00 30.78  ? 429 VAL B CA    1 
ATOM   3281 C  C     . VAL A 1 419 ? 143.968 141.093 143.941 1.00 42.73  ? 429 VAL B C     1 
ATOM   3282 O  O     . VAL A 1 419 ? 144.801 141.557 143.154 1.00 50.08  ? 429 VAL B O     1 
ATOM   3283 C  CB    . VAL A 1 419 ? 143.820 141.978 146.306 1.00 37.66  ? 429 VAL B CB    1 
ATOM   3284 C  CG1   . VAL A 1 419 ? 145.325 142.090 146.228 1.00 45.44  ? 429 VAL B CG1   1 
ATOM   3285 C  CG2   . VAL A 1 419 ? 143.250 143.103 147.137 1.00 46.36  ? 429 VAL B CG2   1 
ATOM   3286 N  N     . SER A 1 420 ? 143.695 139.790 143.990 1.00 43.35  ? 430 SER B N     1 
ATOM   3287 C  CA    . SER A 1 420 ? 144.354 138.865 143.072 1.00 38.91  ? 430 SER B CA    1 
ATOM   3288 C  C     . SER A 1 420 ? 143.951 139.132 141.627 1.00 41.54  ? 430 SER B C     1 
ATOM   3289 O  O     . SER A 1 420 ? 144.753 138.939 140.707 1.00 48.15  ? 430 SER B O     1 
ATOM   3290 C  CB    . SER A 1 420 ? 144.034 137.424 143.461 1.00 47.01  ? 430 SER B CB    1 
ATOM   3291 O  OG    . SER A 1 420 ? 142.661 137.139 143.266 1.00 54.45  ? 430 SER B OG    1 
ATOM   3292 N  N     . GLU A 1 421 ? 142.706 139.555 141.404 1.00 46.72  ? 431 GLU B N     1 
ATOM   3293 C  CA    . GLU A 1 421 ? 142.275 139.931 140.061 1.00 43.33  ? 431 GLU B CA    1 
ATOM   3294 C  C     . GLU A 1 421 ? 143.089 141.101 139.536 1.00 43.27  ? 431 GLU B C     1 
ATOM   3295 O  O     . GLU A 1 421 ? 143.585 141.072 138.406 1.00 45.00  ? 431 GLU B O     1 
ATOM   3296 C  CB    . GLU A 1 421 ? 140.791 140.290 140.067 1.00 49.10  ? 431 GLU B CB    1 
ATOM   3297 C  CG    . GLU A 1 421 ? 139.989 139.713 138.920 1.00 51.10  ? 431 GLU B CG    1 
ATOM   3298 C  CD    . GLU A 1 421 ? 140.444 140.207 137.566 1.00 59.65  ? 431 GLU B CD    1 
ATOM   3299 O  OE1   . GLU A 1 421 ? 140.919 141.357 137.472 1.00 62.39  ? 431 GLU B OE1   1 
ATOM   3300 O  OE2   . GLU A 1 421 ? 140.328 139.441 136.586 1.00 62.89  ? 431 GLU B OE2   1 
ATOM   3301 N  N     . TYR A 1 422 ? 143.232 142.150 140.346 1.00 44.37  ? 432 TYR B N     1 
ATOM   3302 C  CA    . TYR A 1 422 ? 143.948 143.333 139.880 1.00 39.19  ? 432 TYR B CA    1 
ATOM   3303 C  C     . TYR A 1 422 ? 145.434 143.064 139.701 1.00 41.02  ? 432 TYR B C     1 
ATOM   3304 O  O     . TYR A 1 422 ? 146.063 143.649 138.815 1.00 50.07  ? 432 TYR B O     1 
ATOM   3305 C  CB    . TYR A 1 422 ? 143.736 144.489 140.852 1.00 46.27  ? 432 TYR B CB    1 
ATOM   3306 C  CG    . TYR A 1 422 ? 142.665 145.455 140.425 1.00 43.50  ? 432 TYR B CG    1 
ATOM   3307 C  CD1   . TYR A 1 422 ? 142.801 146.205 139.273 1.00 46.43  ? 432 TYR B CD1   1 
ATOM   3308 C  CD2   . TYR A 1 422 ? 141.513 145.613 141.172 1.00 44.96  ? 432 TYR B CD2   1 
ATOM   3309 C  CE1   . TYR A 1 422 ? 141.821 147.088 138.880 1.00 46.88  ? 432 TYR B CE1   1 
ATOM   3310 C  CE2   . TYR A 1 422 ? 140.530 146.488 140.789 1.00 42.58  ? 432 TYR B CE2   1 
ATOM   3311 C  CZ    . TYR A 1 422 ? 140.689 147.226 139.643 1.00 45.84  ? 432 TYR B CZ    1 
ATOM   3312 O  OH    . TYR A 1 422 ? 139.708 148.104 139.255 1.00 48.92  ? 432 TYR B OH    1 
ATOM   3313 N  N     . GLN A 1 423 ? 146.013 142.193 140.526 1.00 46.07  ? 433 GLN B N     1 
ATOM   3314 C  CA    . GLN A 1 423 ? 147.449 141.952 140.481 1.00 42.08  ? 433 GLN B CA    1 
ATOM   3315 C  C     . GLN A 1 423 ? 147.872 141.234 139.206 1.00 46.49  ? 433 GLN B C     1 
ATOM   3316 O  O     . GLN A 1 423 ? 149.040 141.318 138.817 1.00 48.72  ? 433 GLN B O     1 
ATOM   3317 C  CB    . GLN A 1 423 ? 147.866 141.164 141.727 1.00 48.78  ? 433 GLN B CB    1 
ATOM   3318 C  CG    . GLN A 1 423 ? 149.240 140.531 141.687 1.00 57.27  ? 433 GLN B CG    1 
ATOM   3319 C  CD    . GLN A 1 423 ? 150.353 141.554 141.795 1.00 64.61  ? 433 GLN B CD    1 
ATOM   3320 O  OE1   . GLN A 1 423 ? 150.142 142.669 142.272 1.00 63.62  ? 433 GLN B OE1   1 
ATOM   3321 N  NE2   . GLN A 1 423 ? 151.547 141.178 141.352 1.00 57.51  ? 433 GLN B NE2   1 
ATOM   3322 N  N     . GLN A 1 424 ? 146.939 140.569 138.526 1.00 52.53  ? 434 GLN B N     1 
ATOM   3323 C  CA    . GLN A 1 424 ? 147.288 139.805 137.334 1.00 47.67  ? 434 GLN B CA    1 
ATOM   3324 C  C     . GLN A 1 424 ? 147.796 140.709 136.220 1.00 54.46  ? 434 GLN B C     1 
ATOM   3325 O  O     . GLN A 1 424 ? 148.728 140.345 135.494 1.00 57.39  ? 434 GLN B O     1 
ATOM   3326 C  CB    . GLN A 1 424 ? 146.079 138.998 136.867 1.00 47.32  ? 434 GLN B CB    1 
ATOM   3327 C  CG    . GLN A 1 424 ? 146.282 138.258 135.568 1.00 54.21  ? 434 GLN B CG    1 
ATOM   3328 C  CD    . GLN A 1 424 ? 145.021 137.564 135.101 1.00 60.22  ? 434 GLN B CD    1 
ATOM   3329 O  OE1   . GLN A 1 424 ? 143.960 137.708 135.706 1.00 57.48  ? 434 GLN B OE1   1 
ATOM   3330 N  NE2   . GLN A 1 424 ? 145.129 136.803 134.019 1.00 58.69  ? 434 GLN B NE2   1 
ATOM   3331 N  N     . TYR A 1 425 ? 147.206 141.895 136.071 1.00 54.55  ? 435 TYR B N     1 
ATOM   3332 C  CA    . TYR A 1 425 ? 147.526 142.797 134.972 1.00 44.31  ? 435 TYR B CA    1 
ATOM   3333 C  C     . TYR A 1 425 ? 148.567 143.841 135.353 1.00 41.97  ? 435 TYR B C     1 
ATOM   3334 O  O     . TYR A 1 425 ? 148.538 144.960 134.836 1.00 54.91  ? 435 TYR B O     1 
ATOM   3335 C  CB    . TYR A 1 425 ? 146.260 143.481 134.459 1.00 45.75  ? 435 TYR B CB    1 
ATOM   3336 C  CG    . TYR A 1 425 ? 145.140 142.531 134.130 1.00 44.48  ? 435 TYR B CG    1 
ATOM   3337 C  CD1   . TYR A 1 425 ? 145.232 141.675 133.051 1.00 44.28  ? 435 TYR B CD1   1 
ATOM   3338 C  CD2   . TYR A 1 425 ? 143.987 142.500 134.889 1.00 50.16  ? 435 TYR B CD2   1 
ATOM   3339 C  CE1   . TYR A 1 425 ? 144.213 140.806 132.743 1.00 50.11  ? 435 TYR B CE1   1 
ATOM   3340 C  CE2   . TYR A 1 425 ? 142.961 141.635 134.587 1.00 48.71  ? 435 TYR B CE2   1 
ATOM   3341 C  CZ    . TYR A 1 425 ? 143.080 140.790 133.513 1.00 52.89  ? 435 TYR B CZ    1 
ATOM   3342 O  OH    . TYR A 1 425 ? 142.060 139.923 133.207 1.00 57.35  ? 435 TYR B OH    1 
ATOM   3343 N  N     . GLN A 1 426 ? 149.492 143.499 136.238 1.00 44.68  ? 436 GLN B N     1 
ATOM   3344 C  CA    . GLN A 1 426 ? 150.529 144.430 136.650 1.00 49.02  ? 436 GLN B CA    1 
ATOM   3345 C  C     . GLN A 1 426 ? 151.906 143.940 136.222 1.00 60.69  ? 436 GLN B C     1 
ATOM   3346 O  O     . GLN A 1 426 ? 152.078 142.785 135.836 1.00 63.22  ? 436 GLN B O     1 
ATOM   3347 C  CB    . GLN A 1 426 ? 150.492 144.628 138.161 1.00 52.81  ? 436 GLN B CB    1 
ATOM   3348 C  CG    . GLN A 1 426 ? 151.038 145.950 138.637 1.00 55.09  ? 436 GLN B CG    1 
ATOM   3349 C  CD    . GLN A 1 426 ? 151.002 146.071 140.144 1.00 59.72  ? 436 GLN B CD    1 
ATOM   3350 O  OE1   . GLN A 1 426 ? 150.428 147.010 140.691 1.00 61.35  ? 436 GLN B OE1   1 
ATOM   3351 N  NE2   . GLN A 1 426 ? 151.620 145.116 140.825 1.00 57.78  ? 436 GLN B NE2   1 
ATOM   3352 N  N     . MET B 2 1   ? 114.370 162.785 85.556  1.00 68.14  ? 1   MET A N     1 
ATOM   3353 C  CA    . MET B 2 1   ? 115.192 163.715 86.320  1.00 65.02  ? 1   MET A CA    1 
ATOM   3354 C  C     . MET B 2 1   ? 116.285 162.977 87.082  1.00 66.59  ? 1   MET A C     1 
ATOM   3355 O  O     . MET B 2 1   ? 116.300 161.749 87.120  1.00 74.74  ? 1   MET A O     1 
ATOM   3356 C  CB    . MET B 2 1   ? 114.327 164.524 87.282  1.00 66.19  ? 1   MET A CB    1 
ATOM   3357 C  CG    . MET B 2 1   ? 114.735 165.975 87.390  1.00 72.58  ? 1   MET A CG    1 
ATOM   3358 S  SD    . MET B 2 1   ? 116.129 166.171 88.507  1.00 87.34  ? 1   MET A SD    1 
ATOM   3359 C  CE    . MET B 2 1   ? 115.398 165.575 90.028  1.00 68.71  ? 1   MET A CE    1 
ATOM   3360 N  N     . ARG B 2 2   ? 117.203 163.727 87.685  1.00 53.99  ? 2   ARG A N     1 
ATOM   3361 C  CA    . ARG B 2 2   ? 118.356 163.163 88.380  1.00 60.94  ? 2   ARG A CA    1 
ATOM   3362 C  C     . ARG B 2 2   ? 118.353 163.673 89.811  1.00 64.27  ? 2   ARG A C     1 
ATOM   3363 O  O     . ARG B 2 2   ? 118.591 164.861 90.050  1.00 68.03  ? 2   ARG A O     1 
ATOM   3364 C  CB    . ARG B 2 2   ? 119.657 163.533 87.675  1.00 64.62  ? 2   ARG A CB    1 
ATOM   3365 C  CG    . ARG B 2 2   ? 119.590 163.458 86.165  1.00 65.90  ? 2   ARG A CG    1 
ATOM   3366 C  CD    . ARG B 2 2   ? 120.480 164.505 85.524  1.00 64.22  ? 2   ARG A CD    1 
ATOM   3367 N  NE    . ARG B 2 2   ? 120.097 165.855 85.914  1.00 64.07  ? 2   ARG A NE    1 
ATOM   3368 C  CZ    . ARG B 2 2   ? 119.167 166.572 85.302  1.00 65.73  ? 2   ARG A CZ    1 
ATOM   3369 N  NH1   . ARG B 2 2   ? 118.506 166.100 84.259  1.00 67.06  ? 2   ARG A NH1   1 
ATOM   3370 N  NH2   . ARG B 2 2   ? 118.893 167.795 85.747  1.00 63.37  ? 2   ARG A NH2   1 
ATOM   3371 N  N     . GLU B 2 3   ? 118.097 162.779 90.763  1.00 52.99  ? 3   GLU A N     1 
ATOM   3372 C  CA    . GLU B 2 3   ? 117.953 163.177 92.152  1.00 51.21  ? 3   GLU A CA    1 
ATOM   3373 C  C     . GLU B 2 3   ? 118.686 162.200 93.057  1.00 53.77  ? 3   GLU A C     1 
ATOM   3374 O  O     . GLU B 2 3   ? 118.843 161.023 92.731  1.00 56.56  ? 3   GLU A O     1 
ATOM   3375 C  CB    . GLU B 2 3   ? 116.478 163.261 92.549  1.00 54.72  ? 3   GLU A CB    1 
ATOM   3376 C  CG    . GLU B 2 3   ? 115.700 161.994 92.277  1.00 61.84  ? 3   GLU A CG    1 
ATOM   3377 C  CD    . GLU B 2 3   ? 115.015 161.999 90.924  1.00 67.89  ? 3   GLU A CD    1 
ATOM   3378 O  OE1   . GLU B 2 3   ? 115.621 162.481 89.951  1.00 70.03  ? 3   GLU A OE1   1 
ATOM   3379 O  OE2   . GLU B 2 3   ? 113.872 161.508 90.825  1.00 69.08  ? 3   GLU A OE2   1 
ATOM   3380 N  N     . CYS B 2 4   ? 119.130 162.706 94.202  1.00 50.70  ? 4   CYS A N     1 
ATOM   3381 C  CA    . CYS B 2 4   ? 119.847 161.920 95.191  1.00 46.88  ? 4   CYS A CA    1 
ATOM   3382 C  C     . CYS B 2 4   ? 119.176 162.065 96.546  1.00 51.72  ? 4   CYS A C     1 
ATOM   3383 O  O     . CYS B 2 4   ? 118.590 163.104 96.859  1.00 56.06  ? 4   CYS A O     1 
ATOM   3384 C  CB    . CYS B 2 4   ? 121.312 162.347 95.300  1.00 47.84  ? 4   CYS A CB    1 
ATOM   3385 S  SG    . CYS B 2 4   ? 122.342 161.893 93.898  1.00 59.92  ? 4   CYS A SG    1 
ATOM   3386 N  N     . ILE B 2 5   ? 119.270 161.010 97.348  1.00 42.14  ? 5   ILE A N     1 
ATOM   3387 C  CA    . ILE B 2 5   ? 118.794 161.006 98.724  1.00 35.33  ? 5   ILE A CA    1 
ATOM   3388 C  C     . ILE B 2 5   ? 119.995 160.822 99.637  1.00 41.62  ? 5   ILE A C     1 
ATOM   3389 O  O     . ILE B 2 5   ? 120.763 159.869 99.472  1.00 50.94  ? 5   ILE A O     1 
ATOM   3390 C  CB    . ILE B 2 5   ? 117.754 159.900 98.963  1.00 37.13  ? 5   ILE A CB    1 
ATOM   3391 C  CG1   . ILE B 2 5   ? 116.443 160.237 98.263  1.00 43.73  ? 5   ILE A CG1   1 
ATOM   3392 C  CG2   . ILE B 2 5   ? 117.516 159.707 100.440 1.00 46.91  ? 5   ILE A CG2   1 
ATOM   3393 C  CD1   . ILE B 2 5   ? 115.377 159.201 98.477  1.00 48.29  ? 5   ILE A CD1   1 
ATOM   3394 N  N     . SER B 2 6   ? 120.151 161.726 100.597 1.00 40.05  ? 6   SER A N     1 
ATOM   3395 C  CA    . SER B 2 6   ? 121.271 161.712 101.526 1.00 33.47  ? 6   SER A CA    1 
ATOM   3396 C  C     . SER B 2 6   ? 120.793 161.261 102.896 1.00 41.13  ? 6   SER A C     1 
ATOM   3397 O  O     . SER B 2 6   ? 119.750 161.716 103.374 1.00 50.74  ? 6   SER A O     1 
ATOM   3398 C  CB    . SER B 2 6   ? 121.912 163.094 101.626 1.00 33.44  ? 6   SER A CB    1 
ATOM   3399 O  OG    . SER B 2 6   ? 122.317 163.557 100.355 1.00 44.50  ? 6   SER A OG    1 
ATOM   3400 N  N     . ILE B 2 7   ? 121.550 160.364 103.520 1.00 39.33  ? 7   ILE A N     1 
ATOM   3401 C  CA    . ILE B 2 7   ? 121.303 159.921 104.886 1.00 31.60  ? 7   ILE A CA    1 
ATOM   3402 C  C     . ILE B 2 7   ? 122.518 160.273 105.728 1.00 35.77  ? 7   ILE A C     1 
ATOM   3403 O  O     . ILE B 2 7   ? 123.649 159.937 105.362 1.00 46.88  ? 7   ILE A O     1 
ATOM   3404 C  CB    . ILE B 2 7   ? 121.020 158.413 104.959 1.00 32.23  ? 7   ILE A CB    1 
ATOM   3405 C  CG1   . ILE B 2 7   ? 119.943 158.029 103.956 1.00 36.81  ? 7   ILE A CG1   1 
ATOM   3406 C  CG2   . ILE B 2 7   ? 120.601 158.021 106.362 1.00 42.34  ? 7   ILE A CG2   1 
ATOM   3407 C  CD1   . ILE B 2 7   ? 119.671 156.562 103.914 1.00 39.64  ? 7   ILE A CD1   1 
ATOM   3408 N  N     . HIS B 2 8   ? 122.286 160.944 106.849 1.00 31.34  ? 8   HIS A N     1 
ATOM   3409 C  CA    . HIS B 2 8   ? 123.344 161.306 107.785 1.00 25.79  ? 8   HIS A CA    1 
ATOM   3410 C  C     . HIS B 2 8   ? 123.030 160.659 109.125 1.00 39.69  ? 8   HIS A C     1 
ATOM   3411 O  O     . HIS B 2 8   ? 122.166 161.140 109.864 1.00 52.32  ? 8   HIS A O     1 
ATOM   3412 C  CB    . HIS B 2 8   ? 123.462 162.819 107.905 1.00 35.79  ? 8   HIS A CB    1 
ATOM   3413 C  CG    . HIS B 2 8   ? 123.571 163.518 106.589 1.00 37.84  ? 8   HIS A CG    1 
ATOM   3414 N  ND1   . HIS B 2 8   ? 124.763 163.640 105.911 1.00 44.93  ? 8   HIS A ND1   1 
ATOM   3415 C  CD2   . HIS B 2 8   ? 122.641 164.136 105.826 1.00 40.34  ? 8   HIS A CD2   1 
ATOM   3416 C  CE1   . HIS B 2 8   ? 124.563 164.302 104.788 1.00 46.03  ? 8   HIS A CE1   1 
ATOM   3417 N  NE2   . HIS B 2 8   ? 123.284 164.616 104.713 1.00 42.86  ? 8   HIS A NE2   1 
ATOM   3418 N  N     . VAL B 2 9   ? 123.728 159.572 109.436 1.00 38.15  ? 9   VAL A N     1 
ATOM   3419 C  CA    . VAL B 2 9   ? 123.462 158.761 110.617 1.00 33.57  ? 9   VAL A CA    1 
ATOM   3420 C  C     . VAL B 2 9   ? 124.634 158.896 111.576 1.00 40.28  ? 9   VAL A C     1 
ATOM   3421 O  O     . VAL B 2 9   ? 125.792 158.731 111.178 1.00 49.54  ? 9   VAL A O     1 
ATOM   3422 C  CB    . VAL B 2 9   ? 123.216 157.287 110.249 1.00 37.87  ? 9   VAL A CB    1 
ATOM   3423 C  CG1   . VAL B 2 9   ? 123.065 156.450 111.495 1.00 43.27  ? 9   VAL A CG1   1 
ATOM   3424 C  CG2   . VAL B 2 9   ? 122.000 157.153 109.364 1.00 43.98  ? 9   VAL A CG2   1 
ATOM   3425 N  N     . GLY B 2 10  ? 124.333 159.201 112.831 1.00 43.38  ? 10  GLY A N     1 
ATOM   3426 C  CA    . GLY B 2 10  ? 125.348 159.408 113.837 1.00 44.00  ? 10  GLY A CA    1 
ATOM   3427 C  C     . GLY B 2 10  ? 125.782 160.856 113.930 1.00 47.82  ? 10  GLY A C     1 
ATOM   3428 O  O     . GLY B 2 10  ? 125.439 161.703 113.105 1.00 57.08  ? 10  GLY A O     1 
ATOM   3429 N  N     . GLN B 2 11  ? 126.572 161.137 114.965 1.00 43.60  ? 11  GLN A N     1 
ATOM   3430 C  CA    . GLN B 2 11  ? 127.046 162.497 115.187 1.00 48.61  ? 11  GLN A CA    1 
ATOM   3431 C  C     . GLN B 2 11  ? 127.934 162.967 114.044 1.00 52.85  ? 11  GLN A C     1 
ATOM   3432 O  O     . GLN B 2 11  ? 127.774 164.083 113.533 1.00 60.18  ? 11  GLN A O     1 
ATOM   3433 C  CB    . GLN B 2 11  ? 127.794 162.574 116.512 1.00 46.47  ? 11  GLN A CB    1 
ATOM   3434 C  CG    . GLN B 2 11  ? 128.295 163.955 116.844 1.00 50.40  ? 11  GLN A CG    1 
ATOM   3435 C  CD    . GLN B 2 11  ? 128.877 164.038 118.230 1.00 49.38  ? 11  GLN A CD    1 
ATOM   3436 O  OE1   . GLN B 2 11  ? 129.358 163.047 118.770 1.00 53.03  ? 11  GLN A OE1   1 
ATOM   3437 N  NE2   . GLN B 2 11  ? 128.840 165.220 118.816 1.00 49.99  ? 11  GLN A NE2   1 
ATOM   3438 N  N     . ALA B 2 12  ? 128.877 162.122 113.629 1.00 44.88  ? 12  ALA A N     1 
ATOM   3439 C  CA    . ALA B 2 12  ? 129.769 162.481 112.535 1.00 46.55  ? 12  ALA A CA    1 
ATOM   3440 C  C     . ALA B 2 12  ? 128.981 162.749 111.262 1.00 48.42  ? 12  ALA A C     1 
ATOM   3441 O  O     . ALA B 2 12  ? 129.218 163.745 110.566 1.00 60.53  ? 12  ALA A O     1 
ATOM   3442 C  CB    . ALA B 2 12  ? 130.792 161.371 112.314 1.00 50.28  ? 12  ALA A CB    1 
ATOM   3443 N  N     . GLY B 2 13  ? 128.023 161.877 110.954 1.00 40.31  ? 13  GLY A N     1 
ATOM   3444 C  CA    . GLY B 2 13  ? 127.214 162.072 109.768 1.00 34.47  ? 13  GLY A CA    1 
ATOM   3445 C  C     . GLY B 2 13  ? 126.399 163.346 109.818 1.00 44.64  ? 13  GLY A C     1 
ATOM   3446 O  O     . GLY B 2 13  ? 126.302 164.067 108.826 1.00 53.36  ? 13  GLY A O     1 
ATOM   3447 N  N     . VAL B 2 14  ? 125.807 163.646 110.974 1.00 34.88  ? 14  VAL A N     1 
ATOM   3448 C  CA    . VAL B 2 14  ? 124.983 164.844 111.092 1.00 33.10  ? 14  VAL A CA    1 
ATOM   3449 C  C     . VAL B 2 14  ? 125.829 166.098 110.907 1.00 44.72  ? 14  VAL A C     1 
ATOM   3450 O  O     . VAL B 2 14  ? 125.418 167.045 110.224 1.00 56.42  ? 14  VAL A O     1 
ATOM   3451 C  CB    . VAL B 2 14  ? 124.236 164.853 112.436 1.00 40.88  ? 14  VAL A CB    1 
ATOM   3452 C  CG1   . VAL B 2 14  ? 123.568 166.188 112.653 1.00 47.19  ? 14  VAL A CG1   1 
ATOM   3453 C  CG2   . VAL B 2 14  ? 123.206 163.758 112.465 1.00 44.09  ? 14  VAL A CG2   1 
ATOM   3454 N  N     . GLN B 2 15  ? 127.023 166.131 111.501 1.00 40.62  ? 15  GLN A N     1 
ATOM   3455 C  CA    . GLN B 2 15  ? 127.871 167.312 111.341 1.00 43.87  ? 15  GLN A CA    1 
ATOM   3456 C  C     . GLN B 2 15  ? 128.361 167.469 109.900 1.00 47.72  ? 15  GLN A C     1 
ATOM   3457 O  O     . GLN B 2 15  ? 128.345 168.583 109.340 1.00 54.49  ? 15  GLN A O     1 
ATOM   3458 C  CB    . GLN B 2 15  ? 129.043 167.241 112.315 1.00 46.98  ? 15  GLN A CB    1 
ATOM   3459 C  CG    . GLN B 2 15  ? 128.622 166.992 113.751 1.00 47.01  ? 15  GLN A CG    1 
ATOM   3460 C  CD    . GLN B 2 15  ? 129.657 167.435 114.752 1.00 50.26  ? 15  GLN A CD    1 
ATOM   3461 O  OE1   . GLN B 2 15  ? 130.444 168.340 114.487 1.00 57.75  ? 15  GLN A OE1   1 
ATOM   3462 N  NE2   . GLN B 2 15  ? 129.683 166.782 115.899 1.00 44.69  ? 15  GLN A NE2   1 
ATOM   3463 N  N     . ILE B 2 16  ? 128.789 166.367 109.277 1.00 35.65  ? 16  ILE A N     1 
ATOM   3464 C  CA    . ILE B 2 16  ? 129.181 166.421 107.874 1.00 31.64  ? 16  ILE A CA    1 
ATOM   3465 C  C     . ILE B 2 16  ? 128.018 166.910 107.025 1.00 47.22  ? 16  ILE A C     1 
ATOM   3466 O  O     . ILE B 2 16  ? 128.204 167.675 106.072 1.00 59.26  ? 16  ILE A O     1 
ATOM   3467 C  CB    . ILE B 2 16  ? 129.684 165.046 107.401 1.00 36.47  ? 16  ILE A CB    1 
ATOM   3468 C  CG1   . ILE B 2 16  ? 130.941 164.634 108.161 1.00 41.12  ? 16  ILE A CG1   1 
ATOM   3469 C  CG2   . ILE B 2 16  ? 129.960 165.067 105.912 1.00 42.94  ? 16  ILE A CG2   1 
ATOM   3470 C  CD1   . ILE B 2 16  ? 132.199 165.239 107.616 1.00 48.95  ? 16  ILE A CD1   1 
ATOM   3471 N  N     . GLY B 2 17  ? 126.801 166.481 107.356 1.00 51.50  ? 17  GLY A N     1 
ATOM   3472 C  CA    . GLY B 2 17  ? 125.637 166.936 106.620 1.00 50.57  ? 17  GLY A CA    1 
ATOM   3473 C  C     . GLY B 2 17  ? 125.363 168.413 106.808 1.00 48.27  ? 17  GLY A C     1 
ATOM   3474 O  O     . GLY B 2 17  ? 124.903 169.087 105.885 1.00 57.89  ? 17  GLY A O     1 
ATOM   3475 N  N     . ASN B 2 18  ? 125.614 168.931 108.009 1.00 39.62  ? 18  ASN A N     1 
ATOM   3476 C  CA    . ASN B 2 18  ? 125.493 170.368 108.218 1.00 43.90  ? 18  ASN A CA    1 
ATOM   3477 C  C     . ASN B 2 18  ? 126.396 171.120 107.251 1.00 50.43  ? 18  ASN A C     1 
ATOM   3478 O  O     . ASN B 2 18  ? 125.954 172.044 106.546 1.00 59.17  ? 18  ASN A O     1 
ATOM   3479 C  CB    . ASN B 2 18  ? 125.838 170.723 109.662 1.00 47.29  ? 18  ASN A CB    1 
ATOM   3480 C  CG    . ASN B 2 18  ? 124.845 170.162 110.652 1.00 57.64  ? 18  ASN A CG    1 
ATOM   3481 O  OD1   . ASN B 2 18  ? 123.858 169.535 110.272 1.00 65.16  ? 18  ASN A OD1   1 
ATOM   3482 N  ND2   . ASN B 2 18  ? 125.103 170.381 111.934 1.00 52.89  ? 18  ASN A ND2   1 
ATOM   3483 N  N     . ALA B 2 19  ? 127.660 170.699 107.174 1.00 49.85  ? 19  ALA A N     1 
ATOM   3484 C  CA    . ALA B 2 19  ? 128.585 171.324 106.228 1.00 49.74  ? 19  ALA A CA    1 
ATOM   3485 C  C     . ALA B 2 19  ? 128.091 171.181 104.789 1.00 49.57  ? 19  ALA A C     1 
ATOM   3486 O  O     . ALA B 2 19  ? 128.076 172.153 104.019 1.00 54.46  ? 19  ALA A O     1 
ATOM   3487 C  CB    . ALA B 2 19  ? 129.978 170.721 106.382 1.00 47.81  ? 19  ALA A CB    1 
ATOM   3488 N  N     . CYS B 2 20  ? 127.657 169.975 104.420 1.00 44.68  ? 20  CYS A N     1 
ATOM   3489 C  CA    . CYS B 2 20  ? 127.243 169.713 103.047 1.00 44.26  ? 20  CYS A CA    1 
ATOM   3490 C  C     . CYS B 2 20  ? 126.070 170.590 102.641 1.00 48.53  ? 20  CYS A C     1 
ATOM   3491 O  O     . CYS B 2 20  ? 126.054 171.149 101.537 1.00 59.00  ? 20  CYS A O     1 
ATOM   3492 C  CB    . CYS B 2 20  ? 126.879 168.238 102.885 1.00 49.21  ? 20  CYS A CB    1 
ATOM   3493 S  SG    . CYS B 2 20  ? 128.272 167.097 102.885 1.00 67.72  ? 20  CYS A SG    1 
ATOM   3494 N  N     . TRP B 2 21  ? 125.075 170.719 103.511 1.00 47.07  ? 21  TRP A N     1 
ATOM   3495 C  CA    . TRP B 2 21  ? 123.868 171.438 103.133 1.00 49.87  ? 21  TRP A CA    1 
ATOM   3496 C  C     . TRP B 2 21  ? 124.071 172.942 103.156 1.00 48.53  ? 21  TRP A C     1 
ATOM   3497 O  O     . TRP B 2 21  ? 123.495 173.646 102.317 1.00 59.62  ? 21  TRP A O     1 
ATOM   3498 C  CB    . TRP B 2 21  ? 122.710 171.006 104.026 1.00 49.22  ? 21  TRP A CB    1 
ATOM   3499 C  CG    . TRP B 2 21  ? 122.245 169.655 103.624 1.00 45.70  ? 21  TRP A CG    1 
ATOM   3500 C  CD1   . TRP B 2 21  ? 122.490 168.486 104.262 1.00 49.69  ? 21  TRP A CD1   1 
ATOM   3501 C  CD2   . TRP B 2 21  ? 121.481 169.327 102.464 1.00 40.15  ? 21  TRP A CD2   1 
ATOM   3502 N  NE1   . TRP B 2 21  ? 121.923 167.446 103.579 1.00 51.58  ? 21  TRP A NE1   1 
ATOM   3503 C  CE2   . TRP B 2 21  ? 121.296 167.938 102.468 1.00 44.48  ? 21  TRP A CE2   1 
ATOM   3504 C  CE3   . TRP B 2 21  ? 120.934 170.074 101.424 1.00 49.22  ? 21  TRP A CE3   1 
ATOM   3505 C  CZ2   . TRP B 2 21  ? 120.583 167.281 101.478 1.00 50.74  ? 21  TRP A CZ2   1 
ATOM   3506 C  CZ3   . TRP B 2 21  ? 120.228 169.419 100.442 1.00 47.88  ? 21  TRP A CZ3   1 
ATOM   3507 C  CH2   . TRP B 2 21  ? 120.059 168.039 100.475 1.00 46.40  ? 21  TRP A CH2   1 
ATOM   3508 N  N     . GLU B 2 22  ? 124.914 173.451 104.055 1.00 47.70  ? 22  GLU A N     1 
ATOM   3509 C  CA    . GLU B 2 22  ? 125.314 174.848 103.932 1.00 49.43  ? 22  GLU A CA    1 
ATOM   3510 C  C     . GLU B 2 22  ? 125.982 175.104 102.585 1.00 53.23  ? 22  GLU A C     1 
ATOM   3511 O  O     . GLU B 2 22  ? 125.682 176.099 101.906 1.00 58.34  ? 22  GLU A O     1 
ATOM   3512 C  CB    . GLU B 2 22  ? 126.242 175.224 105.083 1.00 53.24  ? 22  GLU A CB    1 
ATOM   3513 C  CG    . GLU B 2 22  ? 126.742 176.647 105.045 1.00 61.36  ? 22  GLU A CG    1 
ATOM   3514 C  CD    . GLU B 2 22  ? 127.800 176.911 106.092 1.00 64.65  ? 22  GLU A CD    1 
ATOM   3515 O  OE1   . GLU B 2 22  ? 128.321 175.935 106.668 1.00 61.89  ? 22  GLU A OE1   1 
ATOM   3516 O  OE2   . GLU B 2 22  ? 128.109 178.095 106.341 1.00 64.03  ? 22  GLU A OE2   1 
ATOM   3517 N  N     . LEU B 2 23  ? 126.868 174.195 102.164 1.00 48.17  ? 23  LEU A N     1 
ATOM   3518 C  CA    . LEU B 2 23  ? 127.547 174.362 100.882 1.00 43.32  ? 23  LEU A CA    1 
ATOM   3519 C  C     . LEU B 2 23  ? 126.569 174.334 99.713  1.00 49.10  ? 23  LEU A C     1 
ATOM   3520 O  O     . LEU B 2 23  ? 126.663 175.162 98.799  1.00 53.66  ? 23  LEU A O     1 
ATOM   3521 C  CB    . LEU B 2 23  ? 128.607 173.277 100.715 1.00 48.06  ? 23  LEU A CB    1 
ATOM   3522 C  CG    . LEU B 2 23  ? 129.431 173.322 99.436  1.00 51.26  ? 23  LEU A CG    1 
ATOM   3523 C  CD1   . LEU B 2 23  ? 130.202 174.617 99.364  1.00 53.31  ? 23  LEU A CD1   1 
ATOM   3524 C  CD2   . LEU B 2 23  ? 130.365 172.137 99.366  1.00 51.22  ? 23  LEU A CD2   1 
ATOM   3525 N  N     . TYR B 2 24  ? 125.632 173.381 99.712  1.00 51.12  ? 24  TYR A N     1 
ATOM   3526 C  CA    . TYR B 2 24  ? 124.669 173.295 98.615  1.00 45.23  ? 24  TYR A CA    1 
ATOM   3527 C  C     . TYR B 2 24  ? 123.795 174.541 98.555  1.00 46.41  ? 24  TYR A C     1 
ATOM   3528 O  O     . TYR B 2 24  ? 123.507 175.059 97.466  1.00 53.27  ? 24  TYR A O     1 
ATOM   3529 C  CB    . TYR B 2 24  ? 123.789 172.055 98.762  1.00 45.26  ? 24  TYR A CB    1 
ATOM   3530 C  CG    . TYR B 2 24  ? 124.528 170.746 98.878  1.00 48.26  ? 24  TYR A CG    1 
ATOM   3531 C  CD1   . TYR B 2 24  ? 125.719 170.529 98.214  1.00 46.53  ? 24  TYR A CD1   1 
ATOM   3532 C  CD2   . TYR B 2 24  ? 124.023 169.723 99.660  1.00 51.00  ? 24  TYR A CD2   1 
ATOM   3533 C  CE1   . TYR B 2 24  ? 126.385 169.331 98.327  1.00 48.97  ? 24  TYR A CE1   1 
ATOM   3534 C  CE2   . TYR B 2 24  ? 124.681 168.525 99.778  1.00 51.67  ? 24  TYR A CE2   1 
ATOM   3535 C  CZ    . TYR B 2 24  ? 125.861 168.334 99.109  1.00 52.26  ? 24  TYR A CZ    1 
ATOM   3536 O  OH    . TYR B 2 24  ? 126.521 167.136 99.227  1.00 53.87  ? 24  TYR A OH    1 
ATOM   3537 N  N     . CYS B 2 25  ? 123.361 175.036 99.719  1.00 49.16  ? 25  CYS A N     1 
ATOM   3538 C  CA    . CYS B 2 25  ? 122.551 176.247 99.747  1.00 46.50  ? 25  CYS A CA    1 
ATOM   3539 C  C     . CYS B 2 25  ? 123.311 177.431 99.173  1.00 47.91  ? 25  CYS A C     1 
ATOM   3540 O  O     . CYS B 2 25  ? 122.749 178.226 98.412  1.00 57.08  ? 25  CYS A O     1 
ATOM   3541 C  CB    . CYS B 2 25  ? 122.098 176.544 101.173 1.00 46.88  ? 25  CYS A CB    1 
ATOM   3542 S  SG    . CYS B 2 25  ? 120.851 175.421 101.802 1.00 57.34  ? 25  CYS A SG    1 
ATOM   3543 N  N     . LEU B 2 26  ? 124.590 177.574 99.524  1.00 45.36  ? 26  LEU A N     1 
ATOM   3544 C  CA    . LEU B 2 26  ? 125.369 178.665 98.948  1.00 45.67  ? 26  LEU A CA    1 
ATOM   3545 C  C     . LEU B 2 26  ? 125.574 178.473 97.449  1.00 52.98  ? 26  LEU A C     1 
ATOM   3546 O  O     . LEU B 2 26  ? 125.628 179.448 96.694  1.00 58.62  ? 26  LEU A O     1 
ATOM   3547 C  CB    . LEU B 2 26  ? 126.710 178.795 99.664  1.00 50.67  ? 26  LEU A CB    1 
ATOM   3548 C  CG    . LEU B 2 26  ? 126.711 179.761 100.846 1.00 55.90  ? 26  LEU A CG    1 
ATOM   3549 C  CD1   . LEU B 2 26  ? 128.052 179.738 101.547 1.00 57.62  ? 26  LEU A CD1   1 
ATOM   3550 C  CD2   . LEU B 2 26  ? 126.372 181.163 100.386 1.00 54.52  ? 26  LEU A CD2   1 
ATOM   3551 N  N     . GLU B 2 27  ? 125.693 177.223 96.999  1.00 55.27  ? 27  GLU A N     1 
ATOM   3552 C  CA    . GLU B 2 27  ? 125.903 176.970 95.576  1.00 50.57  ? 27  GLU A CA    1 
ATOM   3553 C  C     . GLU B 2 27  ? 124.682 177.347 94.752  1.00 49.56  ? 27  GLU A C     1 
ATOM   3554 O  O     . GLU B 2 27  ? 124.814 177.942 93.678  1.00 58.33  ? 27  GLU A O     1 
ATOM   3555 C  CB    . GLU B 2 27  ? 126.258 175.504 95.347  1.00 52.61  ? 27  GLU A CB    1 
ATOM   3556 C  CG    . GLU B 2 27  ? 127.689 175.150 95.678  1.00 58.15  ? 27  GLU A CG    1 
ATOM   3557 C  CD    . GLU B 2 27  ? 128.036 173.725 95.309  1.00 61.62  ? 27  GLU A CD    1 
ATOM   3558 O  OE1   . GLU B 2 27  ? 127.138 172.998 94.837  1.00 63.58  ? 27  GLU A OE1   1 
ATOM   3559 O  OE2   . GLU B 2 27  ? 129.207 173.330 95.491  1.00 58.90  ? 27  GLU A OE2   1 
ATOM   3560 N  N     . HIS B 2 28  ? 123.491 177.007 95.225  1.00 43.45  ? 28  HIS A N     1 
ATOM   3561 C  CA    . HIS B 2 28  ? 122.285 177.212 94.434  1.00 39.45  ? 28  HIS A CA    1 
ATOM   3562 C  C     . HIS B 2 28  ? 121.581 178.531 94.727  1.00 47.39  ? 28  HIS A C     1 
ATOM   3563 O  O     . HIS B 2 28  ? 120.499 178.769 94.186  1.00 53.39  ? 28  HIS A O     1 
ATOM   3564 C  CB    . HIS B 2 28  ? 121.320 176.051 94.658  1.00 44.11  ? 28  HIS A CB    1 
ATOM   3565 C  CG    . HIS B 2 28  ? 121.796 174.763 94.076  1.00 45.63  ? 28  HIS A CG    1 
ATOM   3566 N  ND1   . HIS B 2 28  ? 121.605 173.549 94.696  1.00 58.60  ? 28  HIS A ND1   1 
ATOM   3567 C  CD2   . HIS B 2 28  ? 122.454 174.498 92.926  1.00 43.21  ? 28  HIS A CD2   1 
ATOM   3568 C  CE1   . HIS B 2 28  ? 122.133 172.592 93.955  1.00 52.57  ? 28  HIS A CE1   1 
ATOM   3569 N  NE2   . HIS B 2 28  ? 122.652 173.142 92.874  1.00 40.79  ? 28  HIS A NE2   1 
ATOM   3570 N  N     . GLY B 2 29  ? 122.163 179.389 95.554  1.00 48.71  ? 29  GLY A N     1 
ATOM   3571 C  CA    . GLY B 2 29  ? 121.533 180.653 95.891  1.00 48.61  ? 29  GLY A CA    1 
ATOM   3572 C  C     . GLY B 2 29  ? 120.262 180.526 96.700  1.00 53.84  ? 29  GLY A C     1 
ATOM   3573 O  O     . GLY B 2 29  ? 119.287 181.235 96.428  1.00 57.43  ? 29  GLY A O     1 
ATOM   3574 N  N     . ILE B 2 30  ? 120.249 179.643 97.693  1.00 52.89  ? 30  ILE A N     1 
ATOM   3575 C  CA    . ILE B 2 30  ? 119.085 179.402 98.535  1.00 47.33  ? 30  ILE A CA    1 
ATOM   3576 C  C     . ILE B 2 30  ? 119.387 179.920 99.930  1.00 48.44  ? 30  ILE A C     1 
ATOM   3577 O  O     . ILE B 2 30  ? 120.398 179.543 100.533 1.00 55.78  ? 30  ILE A O     1 
ATOM   3578 C  CB    . ILE B 2 30  ? 118.712 177.912 98.575  1.00 48.71  ? 30  ILE A CB    1 
ATOM   3579 C  CG1   . ILE B 2 30  ? 118.237 177.437 97.209  1.00 50.53  ? 30  ILE A CG1   1 
ATOM   3580 C  CG2   . ILE B 2 30  ? 117.634 177.668 99.600  1.00 51.41  ? 30  ILE A CG2   1 
ATOM   3581 C  CD1   . ILE B 2 30  ? 117.939 175.970 97.163  1.00 51.44  ? 30  ILE A CD1   1 
ATOM   3582 N  N     . GLN B 2 31  ? 118.519 180.787 100.436 1.00 58.42  ? 31  GLN A N     1 
ATOM   3583 C  CA    . GLN B 2 31  ? 118.685 181.329 101.768 1.00 57.76  ? 31  GLN A CA    1 
ATOM   3584 C  C     . GLN B 2 31  ? 118.364 180.265 102.814 1.00 61.83  ? 31  GLN A C     1 
ATOM   3585 O  O     . GLN B 2 31  ? 117.696 179.273 102.516 1.00 68.86  ? 31  GLN A O     1 
ATOM   3586 C  CB    . GLN B 2 31  ? 117.788 182.547 101.952 1.00 59.62  ? 31  GLN A CB    1 
ATOM   3587 C  CG    . GLN B 2 31  ? 118.155 183.723 101.077 1.00 63.57  ? 31  GLN A CG    1 
ATOM   3588 C  CD    . GLN B 2 31  ? 117.316 184.942 101.378 1.00 69.42  ? 31  GLN A CD    1 
ATOM   3589 O  OE1   . GLN B 2 31  ? 116.475 184.923 102.276 1.00 71.39  ? 31  GLN A OE1   1 
ATOM   3590 N  NE2   . GLN B 2 31  ? 117.540 186.015 100.631 1.00 67.10  ? 31  GLN A NE2   1 
ATOM   3591 N  N     . PRO B 2 32  ? 118.839 180.443 104.049 1.00 56.20  ? 32  PRO A N     1 
ATOM   3592 C  CA    . PRO B 2 32  ? 118.596 179.422 105.080 1.00 53.88  ? 32  PRO A CA    1 
ATOM   3593 C  C     . PRO B 2 32  ? 117.129 179.177 105.385 1.00 61.79  ? 32  PRO A C     1 
ATOM   3594 O  O     . PRO B 2 32  ? 116.814 178.187 106.053 1.00 63.48  ? 32  PRO A O     1 
ATOM   3595 C  CB    . PRO B 2 32  ? 119.333 179.980 106.302 1.00 55.35  ? 32  PRO A CB    1 
ATOM   3596 C  CG    . PRO B 2 32  ? 120.381 180.846 105.735 1.00 60.70  ? 32  PRO A CG    1 
ATOM   3597 C  CD    . PRO B 2 32  ? 119.780 181.471 104.518 1.00 60.85  ? 32  PRO A CD    1 
ATOM   3598 N  N     . ASP B 2 33  ? 116.226 180.044 104.942 1.00 64.48  ? 33  ASP A N     1 
ATOM   3599 C  CA    . ASP B 2 33  ? 114.799 179.842 105.141 1.00 60.11  ? 33  ASP A CA    1 
ATOM   3600 C  C     . ASP B 2 33  ? 114.125 179.145 103.968 1.00 62.58  ? 33  ASP A C     1 
ATOM   3601 O  O     . ASP B 2 33  ? 112.901 178.993 103.981 1.00 67.92  ? 33  ASP A O     1 
ATOM   3602 C  CB    . ASP B 2 33  ? 114.110 181.181 105.416 1.00 64.37  ? 33  ASP A CB    1 
ATOM   3603 C  CG    . ASP B 2 33  ? 114.099 182.092 104.209 1.00 68.68  ? 33  ASP A CG    1 
ATOM   3604 O  OD1   . ASP B 2 33  ? 115.020 181.987 103.374 1.00 72.32  ? 33  ASP A OD1   1 
ATOM   3605 O  OD2   . ASP B 2 33  ? 113.171 182.919 104.096 1.00 67.25  ? 33  ASP A OD2   1 
ATOM   3606 N  N     . GLY B 2 34  ? 114.880 178.723 102.962 1.00 59.11  ? 34  GLY A N     1 
ATOM   3607 C  CA    . GLY B 2 34  ? 114.315 178.022 101.831 1.00 57.63  ? 34  GLY A CA    1 
ATOM   3608 C  C     . GLY B 2 34  ? 113.769 178.889 100.720 1.00 64.01  ? 34  GLY A C     1 
ATOM   3609 O  O     . GLY B 2 34  ? 113.071 178.369 99.843  1.00 67.76  ? 34  GLY A O     1 
ATOM   3610 N  N     . GLN B 2 35  ? 114.063 180.184 100.719 1.00 67.41  ? 35  GLN A N     1 
ATOM   3611 C  CA    . GLN B 2 35  ? 113.604 181.098 99.682  1.00 65.82  ? 35  GLN A CA    1 
ATOM   3612 C  C     . GLN B 2 35  ? 114.797 181.604 98.884  1.00 67.93  ? 35  GLN A C     1 
ATOM   3613 O  O     . GLN B 2 35  ? 115.796 182.036 99.466  1.00 72.65  ? 35  GLN A O     1 
ATOM   3614 C  CB    . GLN B 2 35  ? 112.850 182.280 100.292 1.00 66.18  ? 35  GLN A CB    1 
ATOM   3615 C  CG    . GLN B 2 35  ? 111.786 181.901 101.296 1.00 64.64  ? 35  GLN A CG    1 
ATOM   3616 C  CD    . GLN B 2 35  ? 110.512 181.432 100.643 1.00 69.73  ? 35  GLN A CD    1 
ATOM   3617 O  OE1   . GLN B 2 35  ? 110.259 181.718 99.474  1.00 70.46  ? 35  GLN A OE1   1 
ATOM   3618 N  NE2   . GLN B 2 35  ? 109.696 180.705 101.394 1.00 70.56  ? 35  GLN A NE2   1 
ATOM   3619 N  N     . MET B 2 36  ? 114.691 181.555 97.559  1.00 77.24  ? 36  MET A N     1 
ATOM   3620 C  CA    . MET B 2 36  ? 115.730 182.082 96.687  1.00 79.65  ? 36  MET A CA    1 
ATOM   3621 C  C     . MET B 2 36  ? 115.245 183.364 96.034  1.00 80.80  ? 36  MET A C     1 
ATOM   3622 O  O     . MET B 2 36  ? 114.242 183.340 95.306  1.00 83.76  ? 36  MET A O     1 
ATOM   3623 C  CB    . MET B 2 36  ? 116.131 181.060 95.626  1.00 79.46  ? 36  MET A CB    1 
ATOM   3624 C  CG    . MET B 2 36  ? 114.980 180.324 94.981  1.00 82.28  ? 36  MET A CG    1 
ATOM   3625 S  SD    . MET B 2 36  ? 115.551 179.020 93.877  1.00 96.54  ? 36  MET A SD    1 
ATOM   3626 C  CE    . MET B 2 36  ? 117.010 179.778 93.176  1.00 78.61  ? 36  MET A CE    1 
ATOM   3627 N  N     . PRO B 2 37  ? 115.909 184.504 96.261  1.00 86.91  ? 37  PRO A N     1 
ATOM   3628 C  CA    . PRO B 2 37  ? 115.496 185.777 95.672  1.00 88.46  ? 37  PRO A CA    1 
ATOM   3629 C  C     . PRO B 2 37  ? 116.053 185.978 94.266  1.00 88.91  ? 37  PRO A C     1 
ATOM   3630 O  O     . PRO B 2 37  ? 115.990 185.049 93.461  1.00 90.68  ? 37  PRO A O     1 
ATOM   3631 C  CB    . PRO B 2 37  ? 116.075 186.810 96.639  1.00 87.49  ? 37  PRO A CB    1 
ATOM   3632 C  CG    . PRO B 2 37  ? 117.216 186.111 97.334  1.00 87.12  ? 37  PRO A CG    1 
ATOM   3633 C  CD    . PRO B 2 37  ? 117.152 184.638 97.035  1.00 85.83  ? 37  PRO A CD    1 
ATOM   3634 N  N     . ASP B 2 47  ? 116.203 172.083 87.549  1.00 62.28  ? 47  ASP A N     1 
ATOM   3635 C  CA    . ASP B 2 47  ? 116.950 173.290 87.223  1.00 58.88  ? 47  ASP A CA    1 
ATOM   3636 C  C     . ASP B 2 47  ? 118.117 173.496 88.176  1.00 60.94  ? 47  ASP A C     1 
ATOM   3637 O  O     . ASP B 2 47  ? 118.154 174.471 88.924  1.00 67.02  ? 47  ASP A O     1 
ATOM   3638 C  CB    . ASP B 2 47  ? 116.032 174.512 87.251  1.00 59.76  ? 47  ASP A CB    1 
ATOM   3639 C  CG    . ASP B 2 47  ? 116.673 175.735 86.630  1.00 64.87  ? 47  ASP A CG    1 
ATOM   3640 O  OD1   . ASP B 2 47  ? 116.717 175.821 85.385  1.00 69.45  ? 47  ASP A OD1   1 
ATOM   3641 O  OD2   . ASP B 2 47  ? 117.130 176.614 87.387  1.00 62.51  ? 47  ASP A OD2   1 
ATOM   3642 N  N     . SER B 2 48  ? 119.058 172.556 88.159  1.00 50.34  ? 48  SER A N     1 
ATOM   3643 C  CA    . SER B 2 48  ? 120.329 172.604 88.873  1.00 53.14  ? 48  SER A CA    1 
ATOM   3644 C  C     . SER B 2 48  ? 120.179 172.488 90.380  1.00 58.01  ? 48  SER A C     1 
ATOM   3645 O  O     . SER B 2 48  ? 121.194 172.425 91.080  1.00 63.01  ? 48  SER A O     1 
ATOM   3646 C  CB    . SER B 2 48  ? 121.131 173.874 88.560  1.00 54.38  ? 48  SER A CB    1 
ATOM   3647 O  OG    . SER B 2 48  ? 120.591 174.992 89.238  1.00 62.06  ? 48  SER A OG    1 
ATOM   3648 N  N     . PHE B 2 49  ? 118.961 172.455 90.908  1.00 50.82  ? 49  PHE A N     1 
ATOM   3649 C  CA    . PHE B 2 49  ? 118.744 172.197 92.321  1.00 53.54  ? 49  PHE A CA    1 
ATOM   3650 C  C     . PHE B 2 49  ? 117.844 171.005 92.577  1.00 51.60  ? 49  PHE A C     1 
ATOM   3651 O  O     . PHE B 2 49  ? 117.691 170.606 93.736  1.00 59.65  ? 49  PHE A O     1 
ATOM   3652 C  CB    . PHE B 2 49  ? 118.153 173.431 93.023  1.00 52.84  ? 49  PHE A CB    1 
ATOM   3653 C  CG    . PHE B 2 49  ? 116.802 173.838 92.517  1.00 50.94  ? 49  PHE A CG    1 
ATOM   3654 C  CD1   . PHE B 2 49  ? 115.652 173.231 92.990  1.00 53.05  ? 49  PHE A CD1   1 
ATOM   3655 C  CD2   . PHE B 2 49  ? 116.679 174.847 91.588  1.00 54.53  ? 49  PHE A CD2   1 
ATOM   3656 C  CE1   . PHE B 2 49  ? 114.415 173.608 92.524  1.00 55.04  ? 49  PHE A CE1   1 
ATOM   3657 C  CE2   . PHE B 2 49  ? 115.445 175.231 91.122  1.00 57.47  ? 49  PHE A CE2   1 
ATOM   3658 C  CZ    . PHE B 2 49  ? 114.312 174.611 91.592  1.00 57.54  ? 49  PHE A CZ    1 
ATOM   3659 N  N     . ASN B 2 50  ? 117.248 170.428 91.538  1.00 41.87  ? 50  ASN A N     1 
ATOM   3660 C  CA    . ASN B 2 50  ? 116.326 169.322 91.716  1.00 40.19  ? 50  ASN A CA    1 
ATOM   3661 C  C     . ASN B 2 50  ? 117.015 168.064 92.219  1.00 50.68  ? 50  ASN A C     1 
ATOM   3662 O  O     . ASN B 2 50  ? 116.342 167.182 92.763  1.00 60.56  ? 50  ASN A O     1 
ATOM   3663 C  CB    . ASN B 2 50  ? 115.614 169.047 90.398  1.00 47.61  ? 50  ASN A CB    1 
ATOM   3664 C  CG    . ASN B 2 50  ? 114.150 168.737 90.582  1.00 57.76  ? 50  ASN A CG    1 
ATOM   3665 O  OD1   . ASN B 2 50  ? 113.713 168.369 91.672  1.00 59.99  ? 50  ASN A OD1   1 
ATOM   3666 N  ND2   . ASN B 2 50  ? 113.378 168.883 89.515  1.00 57.04  ? 50  ASN A ND2   1 
ATOM   3667 N  N     . THR B 2 51  ? 118.333 167.957 92.055  1.00 44.73  ? 51  THR A N     1 
ATOM   3668 C  CA    . THR B 2 51  ? 119.055 166.803 92.575  1.00 40.32  ? 51  THR A CA    1 
ATOM   3669 C  C     . THR B 2 51  ? 119.090 166.808 94.094  1.00 47.35  ? 51  THR A C     1 
ATOM   3670 O  O     . THR B 2 51  ? 119.130 165.744 94.717  1.00 57.77  ? 51  THR A O     1 
ATOM   3671 C  CB    . THR B 2 51  ? 120.472 166.782 92.014  1.00 48.04  ? 51  THR A CB    1 
ATOM   3672 O  OG1   . THR B 2 51  ? 120.413 166.896 90.589  1.00 51.87  ? 51  THR A OG1   1 
ATOM   3673 C  CG2   . THR B 2 51  ? 121.179 165.490 92.377  1.00 52.79  ? 51  THR A CG2   1 
ATOM   3674 N  N     . PHE B 2 52  ? 119.054 167.988 94.705  1.00 48.83  ? 52  PHE A N     1 
ATOM   3675 C  CA    . PHE B 2 52  ? 119.163 168.115 96.144  1.00 47.74  ? 52  PHE A CA    1 
ATOM   3676 C  C     . PHE B 2 52  ? 118.027 168.893 96.794  1.00 50.13  ? 52  PHE A C     1 
ATOM   3677 O  O     . PHE B 2 52  ? 117.975 168.948 98.026  1.00 57.79  ? 52  PHE A O     1 
ATOM   3678 C  CB    . PHE B 2 52  ? 120.496 168.782 96.509  1.00 48.80  ? 52  PHE A CB    1 
ATOM   3679 C  CG    . PHE B 2 52  ? 121.675 167.865 96.415  1.00 48.67  ? 52  PHE A CG    1 
ATOM   3680 C  CD1   . PHE B 2 52  ? 121.548 166.522 96.699  1.00 53.08  ? 52  PHE A CD1   1 
ATOM   3681 C  CD2   . PHE B 2 52  ? 122.910 168.347 96.042  1.00 48.90  ? 52  PHE A CD2   1 
ATOM   3682 C  CE1   . PHE B 2 52  ? 122.632 165.682 96.614  1.00 55.37  ? 52  PHE A CE1   1 
ATOM   3683 C  CE2   . PHE B 2 52  ? 123.994 167.510 95.955  1.00 47.51  ? 52  PHE A CE2   1 
ATOM   3684 C  CZ    . PHE B 2 52  ? 123.855 166.180 96.242  1.00 53.92  ? 52  PHE A CZ    1 
ATOM   3685 N  N     . PHE B 2 53  ? 117.123 169.491 96.023  1.00 42.55  ? 53  PHE A N     1 
ATOM   3686 C  CA    . PHE B 2 53  ? 116.026 170.265 96.583  1.00 37.42  ? 53  PHE A CA    1 
ATOM   3687 C  C     . PHE B 2 53  ? 114.747 169.986 95.809  1.00 50.20  ? 53  PHE A C     1 
ATOM   3688 O  O     . PHE B 2 53  ? 114.777 169.614 94.635  1.00 55.68  ? 53  PHE A O     1 
ATOM   3689 C  CB    . PHE B 2 53  ? 116.316 171.766 96.554  1.00 44.10  ? 53  PHE A CB    1 
ATOM   3690 C  CG    . PHE B 2 53  ? 117.419 172.196 97.470  1.00 46.42  ? 53  PHE A CG    1 
ATOM   3691 C  CD1   . PHE B 2 53  ? 118.729 172.197 97.045  1.00 45.54  ? 53  PHE A CD1   1 
ATOM   3692 C  CD2   . PHE B 2 53  ? 117.143 172.621 98.749  1.00 48.43  ? 53  PHE A CD2   1 
ATOM   3693 C  CE1   . PHE B 2 53  ? 119.734 172.599 97.879  1.00 44.14  ? 53  PHE A CE1   1 
ATOM   3694 C  CE2   . PHE B 2 53  ? 118.147 173.027 99.582  1.00 45.55  ? 53  PHE A CE2   1 
ATOM   3695 C  CZ    . PHE B 2 53  ? 119.442 173.016 99.147  1.00 44.94  ? 53  PHE A CZ    1 
ATOM   3696 N  N     . SER B 2 54  ? 113.613 170.179 96.481  1.00 57.97  ? 54  SER A N     1 
ATOM   3697 C  CA    . SER B 2 54  ? 112.299 170.049 95.865  1.00 56.40  ? 54  SER A CA    1 
ATOM   3698 C  C     . SER B 2 54  ? 111.454 171.272 96.194  1.00 56.09  ? 54  SER A C     1 
ATOM   3699 O  O     . SER B 2 54  ? 111.454 171.747 97.331  1.00 61.87  ? 54  SER A O     1 
ATOM   3700 C  CB    . SER B 2 54  ? 111.579 168.779 96.333  1.00 51.70  ? 54  SER A CB    1 
ATOM   3701 O  OG    . SER B 2 54  ? 111.582 168.675 97.743  1.00 56.53  ? 54  SER A OG    1 
ATOM   3702 N  N     . GLU B 2 55  ? 110.741 171.779 95.191  1.00 57.97  ? 55  GLU A N     1 
ATOM   3703 C  CA    . GLU B 2 55  ? 109.868 172.928 95.371  1.00 53.68  ? 55  GLU A CA    1 
ATOM   3704 C  C     . GLU B 2 55  ? 108.567 172.513 96.045  1.00 62.51  ? 55  GLU A C     1 
ATOM   3705 O  O     . GLU B 2 55  ? 108.107 171.375 95.924  1.00 68.84  ? 55  GLU A O     1 
ATOM   3706 C  CB    . GLU B 2 55  ? 109.562 173.591 94.032  1.00 59.91  ? 55  GLU A CB    1 
ATOM   3707 C  CG    . GLU B 2 55  ? 110.669 174.484 93.515  1.00 66.06  ? 55  GLU A CG    1 
ATOM   3708 C  CD    . GLU B 2 55  ? 110.486 175.933 93.918  1.00 70.27  ? 55  GLU A CD    1 
ATOM   3709 O  OE1   . GLU B 2 55  ? 109.579 176.219 94.728  1.00 70.12  ? 55  GLU A OE1   1 
ATOM   3710 O  OE2   . GLU B 2 55  ? 111.251 176.788 93.423  1.00 69.02  ? 55  GLU A OE2   1 
ATOM   3711 N  N     . THR B 2 56  ? 107.966 173.462 96.760  1.00 65.56  ? 56  THR A N     1 
ATOM   3712 C  CA    . THR B 2 56  ? 106.724 173.212 97.473  1.00 65.72  ? 56  THR A CA    1 
ATOM   3713 C  C     . THR B 2 56  ? 105.546 173.999 96.924  1.00 70.31  ? 56  THR A C     1 
ATOM   3714 O  O     . THR B 2 56  ? 104.420 173.815 97.401  1.00 74.39  ? 56  THR A O     1 
ATOM   3715 C  CB    . THR B 2 56  ? 106.890 173.522 98.964  1.00 67.51  ? 56  THR A CB    1 
ATOM   3716 O  OG1   . THR B 2 56  ? 105.925 172.779 99.716  1.00 71.47  ? 56  THR A OG1   1 
ATOM   3717 C  CG2   . THR B 2 56  ? 106.688 175.002 99.222  1.00 67.33  ? 56  THR A CG2   1 
ATOM   3718 N  N     . GLY B 2 57  ? 105.760 174.855 95.931  1.00 67.54  ? 57  GLY A N     1 
ATOM   3719 C  CA    . GLY B 2 57  ? 104.698 175.592 95.294  1.00 66.52  ? 57  GLY A CA    1 
ATOM   3720 C  C     . GLY B 2 57  ? 104.536 177.012 95.784  1.00 69.41  ? 57  GLY A C     1 
ATOM   3721 O  O     . GLY B 2 57  ? 103.929 177.829 95.083  1.00 72.72  ? 57  GLY A O     1 
ATOM   3722 N  N     . ALA B 2 58  ? 105.061 177.329 96.964  1.00 67.10  ? 58  ALA A N     1 
ATOM   3723 C  CA    . ALA B 2 58  ? 105.081 178.692 97.472  1.00 67.15  ? 58  ALA A CA    1 
ATOM   3724 C  C     . ALA B 2 58  ? 106.470 179.307 97.408  1.00 67.20  ? 58  ALA A C     1 
ATOM   3725 O  O     . ALA B 2 58  ? 106.705 180.352 98.021  1.00 67.57  ? 58  ALA A O     1 
ATOM   3726 C  CB    . ALA B 2 58  ? 104.552 178.730 98.907  1.00 67.01  ? 58  ALA A CB    1 
ATOM   3727 N  N     . GLY B 2 59  ? 107.394 178.687 96.674  1.00 62.50  ? 59  GLY A N     1 
ATOM   3728 C  CA    . GLY B 2 59  ? 108.755 179.158 96.580  1.00 60.65  ? 59  GLY A CA    1 
ATOM   3729 C  C     . GLY B 2 59  ? 109.721 178.541 97.565  1.00 62.70  ? 59  GLY A C     1 
ATOM   3730 O  O     . GLY B 2 59  ? 110.925 178.805 97.470  1.00 66.59  ? 59  GLY A O     1 
ATOM   3731 N  N     . LYS B 2 60  ? 109.243 177.731 98.503  1.00 57.87  ? 60  LYS A N     1 
ATOM   3732 C  CA    . LYS B 2 60  ? 110.114 177.100 99.480  1.00 53.68  ? 60  LYS A CA    1 
ATOM   3733 C  C     . LYS B 2 60  ? 110.740 175.838 98.906  1.00 60.29  ? 60  LYS A C     1 
ATOM   3734 O  O     . LYS B 2 60  ? 110.137 175.132 98.095  1.00 64.89  ? 60  LYS A O     1 
ATOM   3735 C  CB    . LYS B 2 60  ? 109.339 176.762 100.751 1.00 53.48  ? 60  LYS A CB    1 
ATOM   3736 C  CG    . LYS B 2 60  ? 110.209 176.529 101.957 1.00 53.46  ? 60  LYS A CG    1 
ATOM   3737 C  CD    . LYS B 2 60  ? 109.383 176.409 103.208 1.00 54.64  ? 60  LYS A CD    1 
ATOM   3738 C  CE    . LYS B 2 60  ? 110.247 176.582 104.435 1.00 60.59  ? 60  LYS A CE    1 
ATOM   3739 N  NZ    . LYS B 2 60  ? 110.829 177.946 104.498 1.00 62.89  ? 60  LYS A NZ    1 
ATOM   3740 N  N     . HIS B 2 61  ? 111.966 175.556 99.340  1.00 57.79  ? 61  HIS A N     1 
ATOM   3741 C  CA    . HIS B 2 61  ? 112.710 174.388 98.892  1.00 52.94  ? 61  HIS A CA    1 
ATOM   3742 C  C     . HIS B 2 61  ? 113.052 173.514 100.088 1.00 54.04  ? 61  HIS A C     1 
ATOM   3743 O  O     . HIS B 2 61  ? 113.607 174.000 101.078 1.00 61.70  ? 61  HIS A O     1 
ATOM   3744 C  CB    . HIS B 2 61  ? 113.977 174.806 98.158  1.00 48.01  ? 61  HIS A CB    1 
ATOM   3745 C  CG    . HIS B 2 61  ? 113.718 175.637 96.944  1.00 53.20  ? 61  HIS A CG    1 
ATOM   3746 N  ND1   . HIS B 2 61  ? 113.373 176.967 97.015  1.00 54.06  ? 61  HIS A ND1   1 
ATOM   3747 C  CD2   . HIS B 2 61  ? 113.744 175.326 95.628  1.00 53.04  ? 61  HIS A CD2   1 
ATOM   3748 C  CE1   . HIS B 2 61  ? 113.203 177.441 95.795  1.00 51.35  ? 61  HIS A CE1   1 
ATOM   3749 N  NE2   . HIS B 2 61  ? 113.424 176.466 94.935  1.00 48.52  ? 61  HIS A NE2   1 
ATOM   3750 N  N     . VAL B 2 62  ? 112.732 172.234 99.992  1.00 42.93  ? 62  VAL A N     1 
ATOM   3751 C  CA    . VAL B 2 62  ? 112.946 171.270 101.068 1.00 40.85  ? 62  VAL A CA    1 
ATOM   3752 C  C     . VAL B 2 62  ? 114.018 170.286 100.624 1.00 41.28  ? 62  VAL A C     1 
ATOM   3753 O  O     . VAL B 2 62  ? 113.898 169.709 99.538  1.00 52.09  ? 62  VAL A O     1 
ATOM   3754 C  CB    . VAL B 2 62  ? 111.648 170.529 101.437 1.00 44.72  ? 62  VAL A CB    1 
ATOM   3755 C  CG1   . VAL B 2 62  ? 111.907 169.533 102.544 1.00 49.12  ? 62  VAL A CG1   1 
ATOM   3756 C  CG2   . VAL B 2 62  ? 110.586 171.519 101.850 1.00 47.12  ? 62  VAL A CG2   1 
ATOM   3757 N  N     . PRO B 2 63  ? 115.070 170.077 101.407 1.00 37.36  ? 63  PRO A N     1 
ATOM   3758 C  CA    . PRO B 2 63  ? 116.101 169.112 101.023 1.00 41.04  ? 63  PRO A CA    1 
ATOM   3759 C  C     . PRO B 2 63  ? 115.594 167.679 101.027 1.00 42.51  ? 63  PRO A C     1 
ATOM   3760 O  O     . PRO B 2 63  ? 114.692 167.311 101.781 1.00 44.30  ? 63  PRO A O     1 
ATOM   3761 C  CB    . PRO B 2 63  ? 117.182 169.309 102.089 1.00 47.11  ? 63  PRO A CB    1 
ATOM   3762 C  CG    . PRO B 2 63  ? 116.911 170.629 102.684 1.00 43.76  ? 63  PRO A CG    1 
ATOM   3763 C  CD    . PRO B 2 63  ? 115.442 170.824 102.617 1.00 45.03  ? 63  PRO A CD    1 
ATOM   3764 N  N     . ARG B 2 64  ? 116.200 166.865 100.165 1.00 42.18  ? 64  ARG A N     1 
ATOM   3765 C  CA    . ARG B 2 64  ? 115.951 165.425 100.135 1.00 40.04  ? 64  ARG A CA    1 
ATOM   3766 C  C     . ARG B 2 64  ? 116.950 164.722 101.053 1.00 44.12  ? 64  ARG A C     1 
ATOM   3767 O  O     . ARG B 2 64  ? 117.813 163.956 100.628 1.00 48.27  ? 64  ARG A O     1 
ATOM   3768 C  CB    . ARG B 2 64  ? 116.048 164.893 98.713  1.00 40.13  ? 64  ARG A CB    1 
ATOM   3769 C  CG    . ARG B 2 64  ? 115.182 165.593 97.707  1.00 44.55  ? 64  ARG A CG    1 
ATOM   3770 C  CD    . ARG B 2 64  ? 115.209 164.841 96.401  1.00 40.45  ? 64  ARG A CD    1 
ATOM   3771 N  NE    . ARG B 2 64  ? 114.884 165.699 95.273  1.00 37.87  ? 64  ARG A NE    1 
ATOM   3772 C  CZ    . ARG B 2 64  ? 113.715 165.699 94.653  1.00 42.86  ? 64  ARG A CZ    1 
ATOM   3773 N  NH1   . ARG B 2 64  ? 112.734 164.901 95.032  1.00 48.33  ? 64  ARG A NH1   1 
ATOM   3774 N  NH2   . ARG B 2 64  ? 113.526 166.523 93.629  1.00 42.57  ? 64  ARG A NH2   1 
ATOM   3775 N  N     . ALA B 2 65  ? 116.808 164.997 102.343 1.00 42.02  ? 65  ALA A N     1 
ATOM   3776 C  CA    . ALA B 2 65  ? 117.731 164.503 103.349 1.00 37.93  ? 65  ALA A CA    1 
ATOM   3777 C  C     . ALA B 2 65  ? 116.964 163.874 104.499 1.00 37.08  ? 65  ALA A C     1 
ATOM   3778 O  O     . ALA B 2 65  ? 115.826 164.249 104.790 1.00 51.88  ? 65  ALA A O     1 
ATOM   3779 C  CB    . ALA B 2 65  ? 118.625 165.619 103.885 1.00 43.26  ? 65  ALA A CB    1 
ATOM   3780 N  N     . VAL B 2 66  ? 117.605 162.909 105.147 1.00 32.34  ? 66  VAL A N     1 
ATOM   3781 C  CA    . VAL B 2 66  ? 117.107 162.305 106.374 1.00 39.41  ? 66  VAL A CA    1 
ATOM   3782 C  C     . VAL B 2 66  ? 118.239 162.305 107.392 1.00 48.43  ? 66  VAL A C     1 
ATOM   3783 O  O     . VAL B 2 66  ? 119.321 161.775 107.120 1.00 56.52  ? 66  VAL A O     1 
ATOM   3784 C  CB    . VAL B 2 66  ? 116.589 160.876 106.135 1.00 39.11  ? 66  VAL A CB    1 
ATOM   3785 C  CG1   . VAL B 2 66  ? 116.230 160.222 107.443 1.00 39.30  ? 66  VAL A CG1   1 
ATOM   3786 C  CG2   . VAL B 2 66  ? 115.388 160.903 105.221 1.00 45.33  ? 66  VAL A CG2   1 
ATOM   3787 N  N     . PHE B 2 67  ? 117.993 162.896 108.558 1.00 45.23  ? 67  PHE A N     1 
ATOM   3788 C  CA    . PHE B 2 67  ? 118.962 162.952 109.647 1.00 39.38  ? 67  PHE A CA    1 
ATOM   3789 C  C     . PHE B 2 67  ? 118.525 161.996 110.747 1.00 45.74  ? 67  PHE A C     1 
ATOM   3790 O  O     . PHE B 2 67  ? 117.370 162.036 111.180 1.00 51.73  ? 67  PHE A O     1 
ATOM   3791 C  CB    . PHE B 2 67  ? 119.079 164.365 110.211 1.00 40.83  ? 67  PHE A CB    1 
ATOM   3792 C  CG    . PHE B 2 67  ? 119.873 165.302 109.360 1.00 41.89  ? 67  PHE A CG    1 
ATOM   3793 C  CD1   . PHE B 2 67  ? 119.641 165.400 108.006 1.00 42.97  ? 67  PHE A CD1   1 
ATOM   3794 C  CD2   . PHE B 2 67  ? 120.837 166.107 109.921 1.00 49.28  ? 67  PHE A CD2   1 
ATOM   3795 C  CE1   . PHE B 2 67  ? 120.365 166.266 107.232 1.00 47.07  ? 67  PHE A CE1   1 
ATOM   3796 C  CE2   . PHE B 2 67  ? 121.561 166.973 109.147 1.00 43.54  ? 67  PHE A CE2   1 
ATOM   3797 C  CZ    . PHE B 2 67  ? 121.325 167.050 107.804 1.00 39.52  ? 67  PHE A CZ    1 
ATOM   3798 N  N     . VAL B 2 68  ? 119.440 161.144 111.201 1.00 45.83  ? 68  VAL A N     1 
ATOM   3799 C  CA    . VAL B 2 68  ? 119.130 160.096 112.166 1.00 41.41  ? 68  VAL A CA    1 
ATOM   3800 C  C     . VAL B 2 68  ? 120.176 160.096 113.271 1.00 47.32  ? 68  VAL A C     1 
ATOM   3801 O  O     . VAL B 2 68  ? 121.372 160.265 113.009 1.00 49.11  ? 68  VAL A O     1 
ATOM   3802 C  CB    . VAL B 2 68  ? 119.063 158.708 111.498 1.00 41.93  ? 68  VAL A CB    1 
ATOM   3803 C  CG1   . VAL B 2 68  ? 118.581 157.671 112.483 1.00 45.51  ? 68  VAL A CG1   1 
ATOM   3804 C  CG2   . VAL B 2 68  ? 118.157 158.737 110.288 1.00 47.28  ? 68  VAL A CG2   1 
ATOM   3805 N  N     . ASP B 2 69  ? 119.722 159.910 114.508 1.00 54.40  ? 69  ASP A N     1 
ATOM   3806 C  CA    . ASP B 2 69  ? 120.605 159.673 115.640 1.00 52.35  ? 69  ASP A CA    1 
ATOM   3807 C  C     . ASP B 2 69  ? 119.795 159.070 116.777 1.00 51.55  ? 69  ASP A C     1 
ATOM   3808 O  O     . ASP B 2 69  ? 118.613 159.376 116.939 1.00 62.85  ? 69  ASP A O     1 
ATOM   3809 C  CB    . ASP B 2 69  ? 121.290 160.957 116.101 1.00 57.12  ? 69  ASP A CB    1 
ATOM   3810 C  CG    . ASP B 2 69  ? 122.473 160.688 116.992 1.00 60.60  ? 69  ASP A CG    1 
ATOM   3811 O  OD1   . ASP B 2 69  ? 122.846 159.509 117.136 1.00 59.71  ? 69  ASP A OD1   1 
ATOM   3812 O  OD2   . ASP B 2 69  ? 123.034 161.652 117.549 1.00 63.66  ? 69  ASP A OD2   1 
ATOM   3813 N  N     . LEU B 2 70  ? 120.439 158.209 117.558 1.00 43.26  ? 70  LEU A N     1 
ATOM   3814 C  CA    . LEU B 2 70  ? 119.792 157.606 118.716 1.00 47.93  ? 70  LEU A CA    1 
ATOM   3815 C  C     . LEU B 2 70  ? 119.873 158.478 119.962 1.00 56.80  ? 70  LEU A C     1 
ATOM   3816 O  O     . LEU B 2 70  ? 119.337 158.091 121.004 1.00 64.00  ? 70  LEU A O     1 
ATOM   3817 C  CB    . LEU B 2 70  ? 120.397 156.232 119.008 1.00 58.77  ? 70  LEU A CB    1 
ATOM   3818 C  CG    . LEU B 2 70  ? 120.109 155.137 117.978 1.00 58.74  ? 70  LEU A CG    1 
ATOM   3819 C  CD1   . LEU B 2 70  ? 121.014 153.935 118.154 1.00 58.01  ? 70  LEU A CD1   1 
ATOM   3820 C  CD2   . LEU B 2 70  ? 118.660 154.721 118.056 1.00 59.74  ? 70  LEU A CD2   1 
ATOM   3821 N  N     . GLU B 2 71  ? 120.516 159.640 119.877 1.00 61.77  ? 71  GLU A N     1 
ATOM   3822 C  CA    . GLU B 2 71  ? 120.674 160.597 120.954 1.00 58.96  ? 71  GLU A CA    1 
ATOM   3823 C  C     . GLU B 2 71  ? 120.066 161.936 120.553 1.00 63.24  ? 71  GLU A C     1 
ATOM   3824 O  O     . GLU B 2 71  ? 120.254 162.384 119.418 1.00 68.38  ? 71  GLU A O     1 
ATOM   3825 C  CB    . GLU B 2 71  ? 122.159 160.783 121.291 1.00 59.66  ? 71  GLU A CB    1 
ATOM   3826 C  CG    . GLU B 2 71  ? 122.471 161.899 122.262 1.00 64.10  ? 71  GLU A CG    1 
ATOM   3827 C  CD    . GLU B 2 71  ? 123.958 162.155 122.382 1.00 68.15  ? 71  GLU A CD    1 
ATOM   3828 O  OE1   . GLU B 2 71  ? 124.741 161.410 121.757 1.00 69.32  ? 71  GLU A OE1   1 
ATOM   3829 O  OE2   . GLU B 2 71  ? 124.348 163.094 123.104 1.00 67.28  ? 71  GLU A OE2   1 
ATOM   3830 N  N     . PRO B 2 72  ? 119.339 162.594 121.450 1.00 49.37  ? 72  PRO A N     1 
ATOM   3831 C  CA    . PRO B 2 72  ? 118.626 163.817 121.070 1.00 47.12  ? 72  PRO A CA    1 
ATOM   3832 C  C     . PRO B 2 72  ? 119.454 165.090 121.124 1.00 51.53  ? 72  PRO A C     1 
ATOM   3833 O  O     . PRO B 2 72  ? 118.881 166.179 121.194 1.00 58.53  ? 72  PRO A O     1 
ATOM   3834 C  CB    . PRO B 2 72  ? 117.486 163.869 122.088 1.00 47.27  ? 72  PRO A CB    1 
ATOM   3835 C  CG    . PRO B 2 72  ? 118.047 163.230 123.281 1.00 45.00  ? 72  PRO A CG    1 
ATOM   3836 C  CD    . PRO B 2 72  ? 118.984 162.156 122.808 1.00 51.24  ? 72  PRO A CD    1 
ATOM   3837 N  N     . THR B 2 73  ? 120.781 164.993 121.107 1.00 49.27  ? 73  THR A N     1 
ATOM   3838 C  CA    . THR B 2 73  ? 121.607 166.171 121.357 1.00 51.33  ? 73  THR A CA    1 
ATOM   3839 C  C     . THR B 2 73  ? 121.949 166.954 120.087 1.00 57.57  ? 73  THR A C     1 
ATOM   3840 O  O     . THR B 2 73  ? 121.604 168.133 119.974 1.00 64.09  ? 73  THR A O     1 
ATOM   3841 C  CB    . THR B 2 73  ? 122.885 165.761 122.092 1.00 55.13  ? 73  THR A CB    1 
ATOM   3842 O  OG1   . THR B 2 73  ? 122.538 165.148 123.337 1.00 58.85  ? 73  THR A OG1   1 
ATOM   3843 C  CG2   . THR B 2 73  ? 123.745 166.977 122.368 1.00 56.87  ? 73  THR A CG2   1 
ATOM   3844 N  N     . VAL B 2 74  ? 122.633 166.321 119.130 1.00 49.52  ? 74  VAL A N     1 
ATOM   3845 C  CA    . VAL B 2 74  ? 123.130 167.058 117.968 1.00 44.33  ? 74  VAL A CA    1 
ATOM   3846 C  C     . VAL B 2 74  ? 121.981 167.478 117.053 1.00 52.01  ? 74  VAL A C     1 
ATOM   3847 O  O     . VAL B 2 74  ? 121.958 168.604 116.528 1.00 60.06  ? 74  VAL A O     1 
ATOM   3848 C  CB    . VAL B 2 74  ? 124.193 166.225 117.225 1.00 47.57  ? 74  VAL A CB    1 
ATOM   3849 C  CG1   . VAL B 2 74  ? 123.658 164.860 116.862 1.00 51.86  ? 74  VAL A CG1   1 
ATOM   3850 C  CG2   . VAL B 2 74  ? 124.681 166.961 115.995 1.00 56.41  ? 74  VAL A CG2   1 
ATOM   3851 N  N     . ILE B 2 75  ? 120.999 166.595 116.863 1.00 53.32  ? 75  ILE A N     1 
ATOM   3852 C  CA    . ILE B 2 75  ? 119.834 166.942 116.059 1.00 46.04  ? 75  ILE A CA    1 
ATOM   3853 C  C     . ILE B 2 75  ? 119.091 168.111 116.684 1.00 49.44  ? 75  ILE A C     1 
ATOM   3854 O  O     . ILE B 2 75  ? 118.486 168.922 115.975 1.00 56.10  ? 75  ILE A O     1 
ATOM   3855 C  CB    . ILE B 2 75  ? 118.923 165.713 115.881 1.00 47.94  ? 75  ILE A CB    1 
ATOM   3856 C  CG1   . ILE B 2 75  ? 119.666 164.596 115.156 1.00 53.21  ? 75  ILE A CG1   1 
ATOM   3857 C  CG2   . ILE B 2 75  ? 117.686 166.071 115.095 1.00 52.59  ? 75  ILE A CG2   1 
ATOM   3858 C  CD1   . ILE B 2 75  ? 120.017 164.929 113.741 1.00 56.55  ? 75  ILE A CD1   1 
ATOM   3859 N  N     . ASP B 2 76  ? 119.130 168.232 118.010 1.00 50.25  ? 76  ASP A N     1 
ATOM   3860 C  CA    . ASP B 2 76  ? 118.487 169.368 118.657 1.00 47.93  ? 76  ASP A CA    1 
ATOM   3861 C  C     . ASP B 2 76  ? 119.223 170.665 118.356 1.00 48.48  ? 76  ASP A C     1 
ATOM   3862 O  O     . ASP B 2 76  ? 118.597 171.721 118.218 1.00 59.26  ? 76  ASP A O     1 
ATOM   3863 C  CB    . ASP B 2 76  ? 118.392 169.135 120.161 1.00 50.78  ? 76  ASP A CB    1 
ATOM   3864 C  CG    . ASP B 2 76  ? 117.088 168.485 120.564 1.00 59.92  ? 76  ASP A CG    1 
ATOM   3865 O  OD1   . ASP B 2 76  ? 116.270 168.190 119.670 1.00 64.51  ? 76  ASP A OD1   1 
ATOM   3866 O  OD2   . ASP B 2 76  ? 116.879 168.269 121.776 1.00 58.70  ? 76  ASP A OD2   1 
ATOM   3867 N  N     . GLU B 2 77  ? 120.552 170.610 118.258 1.00 47.24  ? 77  GLU A N     1 
ATOM   3868 C  CA    . GLU B 2 77  ? 121.304 171.785 117.832 1.00 55.19  ? 77  GLU A CA    1 
ATOM   3869 C  C     . GLU B 2 77  ? 120.933 172.174 116.410 1.00 55.07  ? 77  GLU A C     1 
ATOM   3870 O  O     . GLU B 2 77  ? 120.873 173.363 116.077 1.00 54.61  ? 77  GLU A O     1 
ATOM   3871 C  CB    . GLU B 2 77  ? 122.804 171.523 117.936 1.00 55.19  ? 77  GLU A CB    1 
ATOM   3872 C  CG    . GLU B 2 77  ? 123.274 171.087 119.304 1.00 58.13  ? 77  GLU A CG    1 
ATOM   3873 C  CD    . GLU B 2 77  ? 124.770 170.867 119.353 1.00 65.62  ? 77  GLU A CD    1 
ATOM   3874 O  OE1   . GLU B 2 77  ? 125.515 171.749 118.877 1.00 64.02  ? 77  GLU A OE1   1 
ATOM   3875 O  OE2   . GLU B 2 77  ? 125.202 169.810 119.860 1.00 64.10  ? 77  GLU A OE2   1 
ATOM   3876 N  N     . VAL B 2 78  ? 120.690 171.182 115.553 1.00 51.60  ? 78  VAL A N     1 
ATOM   3877 C  CA    . VAL B 2 78  ? 120.202 171.482 114.209 1.00 48.96  ? 78  VAL A CA    1 
ATOM   3878 C  C     . VAL B 2 78  ? 118.814 172.115 114.267 1.00 53.45  ? 78  VAL A C     1 
ATOM   3879 O  O     . VAL B 2 78  ? 118.504 173.038 113.506 1.00 54.25  ? 78  VAL A O     1 
ATOM   3880 C  CB    . VAL B 2 78  ? 120.213 170.211 113.342 1.00 53.34  ? 78  VAL A CB    1 
ATOM   3881 C  CG1   . VAL B 2 78  ? 119.639 170.498 111.975 1.00 53.14  ? 78  VAL A CG1   1 
ATOM   3882 C  CG2   . VAL B 2 78  ? 121.621 169.670 113.221 1.00 54.47  ? 78  VAL A CG2   1 
ATOM   3883 N  N     . ARG B 2 79  ? 117.959 171.633 115.173 1.00 54.19  ? 79  ARG A N     1 
ATOM   3884 C  CA    . ARG B 2 79  ? 116.565 172.067 115.228 1.00 51.02  ? 79  ARG A CA    1 
ATOM   3885 C  C     . ARG B 2 79  ? 116.398 173.505 115.699 1.00 50.90  ? 79  ARG A C     1 
ATOM   3886 O  O     . ARG B 2 79  ? 115.377 174.124 115.390 1.00 54.20  ? 79  ARG A O     1 
ATOM   3887 C  CB    . ARG B 2 79  ? 115.761 171.156 116.154 1.00 46.60  ? 79  ARG A CB    1 
ATOM   3888 C  CG    . ARG B 2 79  ? 115.403 169.799 115.590 1.00 50.25  ? 79  ARG A CG    1 
ATOM   3889 C  CD    . ARG B 2 79  ? 114.290 169.166 116.400 1.00 52.69  ? 79  ARG A CD    1 
ATOM   3890 N  NE    . ARG B 2 79  ? 114.098 167.752 116.105 1.00 51.14  ? 79  ARG A NE    1 
ATOM   3891 C  CZ    . ARG B 2 79  ? 114.335 166.770 116.964 1.00 49.65  ? 79  ARG A CZ    1 
ATOM   3892 N  NH1   . ARG B 2 79  ? 114.798 167.010 118.178 1.00 53.23  ? 79  ARG A NH1   1 
ATOM   3893 N  NH2   . ARG B 2 79  ? 114.096 165.516 116.598 1.00 43.13  ? 79  ARG A NH2   1 
ATOM   3894 N  N     . THR B 2 80  ? 117.349 174.043 116.459 1.00 48.37  ? 80  THR A N     1 
ATOM   3895 C  CA    . THR B 2 80  ? 117.257 175.407 116.964 1.00 46.04  ? 80  THR A CA    1 
ATOM   3896 C  C     . THR B 2 80  ? 118.355 176.306 116.417 1.00 48.96  ? 80  THR A C     1 
ATOM   3897 O  O     . THR B 2 80  ? 118.578 177.392 116.959 1.00 50.34  ? 80  THR A O     1 
ATOM   3898 C  CB    . THR B 2 80  ? 117.301 175.418 118.493 1.00 53.60  ? 80  THR A CB    1 
ATOM   3899 O  OG1   . THR B 2 80  ? 118.602 175.015 118.935 1.00 59.19  ? 80  THR A OG1   1 
ATOM   3900 C  CG2   . THR B 2 80  ? 116.268 174.463 119.062 1.00 52.97  ? 80  THR A CG2   1 
ATOM   3901 N  N     . GLY B 2 81  ? 119.046 175.885 115.366 1.00 54.00  ? 81  GLY A N     1 
ATOM   3902 C  CA    . GLY B 2 81  ? 120.139 176.642 114.796 1.00 49.90  ? 81  GLY A CA    1 
ATOM   3903 C  C     . GLY B 2 81  ? 119.677 177.612 113.732 1.00 53.04  ? 81  GLY A C     1 
ATOM   3904 O  O     . GLY B 2 81  ? 118.519 178.032 113.693 1.00 61.00  ? 81  GLY A O     1 
ATOM   3905 N  N     . THR B 2 82  ? 120.606 177.971 112.853 1.00 55.80  ? 82  THR A N     1 
ATOM   3906 C  CA    . THR B 2 82  ? 120.328 178.927 111.792 1.00 54.15  ? 82  THR A CA    1 
ATOM   3907 C  C     . THR B 2 82  ? 119.660 178.301 110.579 1.00 56.61  ? 82  THR A C     1 
ATOM   3908 O  O     . THR B 2 82  ? 119.220 179.033 109.689 1.00 62.36  ? 82  THR A O     1 
ATOM   3909 C  CB    . THR B 2 82  ? 121.620 179.617 111.351 1.00 59.97  ? 82  THR A CB    1 
ATOM   3910 O  OG1   . THR B 2 82  ? 122.182 180.326 112.460 1.00 65.98  ? 82  THR A OG1   1 
ATOM   3911 C  CG2   . THR B 2 82  ? 121.339 180.593 110.223 1.00 58.61  ? 82  THR A CG2   1 
ATOM   3912 N  N     . TYR B 2 83  ? 119.572 176.975 110.523 1.00 55.62  ? 83  TYR A N     1 
ATOM   3913 C  CA    . TYR B 2 83  ? 118.917 176.267 109.432 1.00 51.92  ? 83  TYR A CA    1 
ATOM   3914 C  C     . TYR B 2 83  ? 117.671 175.546 109.925 1.00 52.75  ? 83  TYR A C     1 
ATOM   3915 O  O     . TYR B 2 83  ? 117.294 174.502 109.393 1.00 61.58  ? 83  TYR A O     1 
ATOM   3916 C  CB    . TYR B 2 83  ? 119.883 175.289 108.768 1.00 53.91  ? 83  TYR A CB    1 
ATOM   3917 C  CG    . TYR B 2 83  ? 120.973 175.976 107.993 1.00 52.12  ? 83  TYR A CG    1 
ATOM   3918 C  CD1   . TYR B 2 83  ? 120.716 176.540 106.757 1.00 53.63  ? 83  TYR A CD1   1 
ATOM   3919 C  CD2   . TYR B 2 83  ? 122.252 176.086 108.507 1.00 55.52  ? 83  TYR A CD2   1 
ATOM   3920 C  CE1   . TYR B 2 83  ? 121.701 177.180 106.049 1.00 58.64  ? 83  TYR A CE1   1 
ATOM   3921 C  CE2   . TYR B 2 83  ? 123.243 176.725 107.807 1.00 57.77  ? 83  TYR A CE2   1 
ATOM   3922 C  CZ    . TYR B 2 83  ? 122.962 177.271 106.577 1.00 60.83  ? 83  TYR A CZ    1 
ATOM   3923 O  OH    . TYR B 2 83  ? 123.949 177.911 105.868 1.00 64.12  ? 83  TYR A OH    1 
ATOM   3924 N  N     . ARG B 2 84  ? 117.020 176.103 110.945 1.00 47.50  ? 84  ARG A N     1 
ATOM   3925 C  CA    . ARG B 2 84  ? 115.869 175.446 111.543 1.00 50.00  ? 84  ARG A CA    1 
ATOM   3926 C  C     . ARG B 2 84  ? 114.640 175.498 110.649 1.00 59.78  ? 84  ARG A C     1 
ATOM   3927 O  O     . ARG B 2 84  ? 113.754 174.650 110.791 1.00 60.93  ? 84  ARG A O     1 
ATOM   3928 C  CB    . ARG B 2 84  ? 115.557 176.072 112.901 1.00 51.57  ? 84  ARG A CB    1 
ATOM   3929 C  CG    . ARG B 2 84  ? 114.584 177.226 112.857 1.00 54.46  ? 84  ARG A CG    1 
ATOM   3930 C  CD    . ARG B 2 84  ? 114.377 177.826 114.233 1.00 55.24  ? 84  ARG A CD    1 
ATOM   3931 N  NE    . ARG B 2 84  ? 115.455 178.733 114.606 1.00 60.58  ? 84  ARG A NE    1 
ATOM   3932 C  CZ    . ARG B 2 84  ? 115.524 180.004 114.239 1.00 62.56  ? 84  ARG A CZ    1 
ATOM   3933 N  NH1   . ARG B 2 84  ? 114.589 180.558 113.485 1.00 58.64  ? 84  ARG A NH1   1 
ATOM   3934 N  NH2   . ARG B 2 84  ? 116.558 180.739 114.638 1.00 58.73  ? 84  ARG A NH2   1 
ATOM   3935 N  N     . GLN B 2 85  ? 114.565 176.463 109.734 1.00 62.05  ? 85  GLN A N     1 
ATOM   3936 C  CA    . GLN B 2 85  ? 113.436 176.585 108.824 1.00 55.63  ? 85  GLN A CA    1 
ATOM   3937 C  C     . GLN B 2 85  ? 113.715 175.988 107.457 1.00 54.92  ? 85  GLN A C     1 
ATOM   3938 O  O     . GLN B 2 85  ? 112.911 176.165 106.539 1.00 61.00  ? 85  GLN A O     1 
ATOM   3939 C  CB    . GLN B 2 85  ? 113.024 178.046 108.673 1.00 53.73  ? 85  GLN A CB    1 
ATOM   3940 C  CG    . GLN B 2 85  ? 112.627 178.707 109.966 1.00 55.18  ? 85  GLN A CG    1 
ATOM   3941 C  CD    . GLN B 2 85  ? 111.987 180.056 109.743 1.00 59.91  ? 85  GLN A CD    1 
ATOM   3942 O  OE1   . GLN B 2 85  ? 110.868 180.146 109.242 1.00 61.15  ? 85  GLN A OE1   1 
ATOM   3943 N  NE2   . GLN B 2 85  ? 112.693 181.116 110.114 1.00 62.70  ? 85  GLN A NE2   1 
ATOM   3944 N  N     . LEU B 2 86  ? 114.831 175.289 107.299 1.00 45.93  ? 86  LEU A N     1 
ATOM   3945 C  CA    . LEU B 2 86  ? 115.153 174.657 106.031 1.00 43.80  ? 86  LEU A CA    1 
ATOM   3946 C  C     . LEU B 2 86  ? 114.667 173.219 105.969 1.00 47.74  ? 86  LEU A C     1 
ATOM   3947 O  O     . LEU B 2 86  ? 114.161 172.781 104.932 1.00 51.15  ? 86  LEU A O     1 
ATOM   3948 C  CB    . LEU B 2 86  ? 116.661 174.708 105.791 1.00 42.89  ? 86  LEU A CB    1 
ATOM   3949 C  CG    . LEU B 2 86  ? 117.165 174.217 104.439 1.00 46.36  ? 86  LEU A CG    1 
ATOM   3950 C  CD1   . LEU B 2 86  ? 116.806 175.195 103.344 1.00 46.86  ? 86  LEU A CD1   1 
ATOM   3951 C  CD2   . LEU B 2 86  ? 118.657 174.002 104.494 1.00 50.39  ? 86  LEU A CD2   1 
ATOM   3952 N  N     . PHE B 2 87  ? 114.798 172.477 107.060 1.00 46.59  ? 87  PHE A N     1 
ATOM   3953 C  CA    . PHE B 2 87  ? 114.493 171.057 107.060 1.00 43.97  ? 87  PHE A CA    1 
ATOM   3954 C  C     . PHE B 2 87  ? 113.049 170.798 107.453 1.00 46.55  ? 87  PHE A C     1 
ATOM   3955 O  O     . PHE B 2 87  ? 112.494 171.470 108.326 1.00 51.02  ? 87  PHE A O     1 
ATOM   3956 C  CB    . PHE B 2 87  ? 115.424 170.303 108.006 1.00 41.10  ? 87  PHE A CB    1 
ATOM   3957 C  CG    . PHE B 2 87  ? 116.853 170.316 107.580 1.00 38.33  ? 87  PHE A CG    1 
ATOM   3958 C  CD1   . PHE B 2 87  ? 117.281 169.522 106.539 1.00 41.59  ? 87  PHE A CD1   1 
ATOM   3959 C  CD2   . PHE B 2 87  ? 117.771 171.114 108.224 1.00 41.82  ? 87  PHE A CD2   1 
ATOM   3960 C  CE1   . PHE B 2 87  ? 118.588 169.531 106.144 1.00 39.25  ? 87  PHE A CE1   1 
ATOM   3961 C  CE2   . PHE B 2 87  ? 119.084 171.122 107.829 1.00 45.95  ? 87  PHE A CE2   1 
ATOM   3962 C  CZ    . PHE B 2 87  ? 119.491 170.329 106.791 1.00 42.69  ? 87  PHE A CZ    1 
ATOM   3963 N  N     . HIS B 2 88  ? 112.452 169.814 106.800 1.00 48.20  ? 88  HIS A N     1 
ATOM   3964 C  CA    . HIS B 2 88  ? 111.159 169.306 107.218 1.00 43.08  ? 88  HIS A CA    1 
ATOM   3965 C  C     . HIS B 2 88  ? 111.286 168.732 108.623 1.00 48.49  ? 88  HIS A C     1 
ATOM   3966 O  O     . HIS B 2 88  ? 112.218 167.961 108.889 1.00 58.43  ? 88  HIS A O     1 
ATOM   3967 C  CB    . HIS B 2 88  ? 110.691 168.238 106.233 1.00 42.81  ? 88  HIS A CB    1 
ATOM   3968 C  CG    . HIS B 2 88  ? 109.262 167.829 106.395 1.00 46.66  ? 88  HIS A CG    1 
ATOM   3969 N  ND1   . HIS B 2 88  ? 108.769 167.284 107.559 1.00 52.75  ? 88  HIS A ND1   1 
ATOM   3970 C  CD2   . HIS B 2 88  ? 108.228 167.851 105.524 1.00 49.84  ? 88  HIS A CD2   1 
ATOM   3971 C  CE1   . HIS B 2 88  ? 107.488 167.001 107.404 1.00 50.69  ? 88  HIS A CE1   1 
ATOM   3972 N  NE2   . HIS B 2 88  ? 107.135 167.335 106.177 1.00 49.87  ? 88  HIS A NE2   1 
ATOM   3973 N  N     . PRO B 2 89  ? 110.397 169.090 109.550 1.00 37.90  ? 89  PRO A N     1 
ATOM   3974 C  CA    . PRO B 2 89  ? 110.542 168.608 110.931 1.00 42.80  ? 89  PRO A CA    1 
ATOM   3975 C  C     . PRO B 2 89  ? 110.477 167.099 111.076 1.00 46.84  ? 89  PRO A C     1 
ATOM   3976 O  O     . PRO B 2 89  ? 110.985 166.572 112.071 1.00 52.72  ? 89  PRO A O     1 
ATOM   3977 C  CB    . PRO B 2 89  ? 109.383 169.294 111.668 1.00 44.48  ? 89  PRO A CB    1 
ATOM   3978 C  CG    . PRO B 2 89  ? 108.490 169.821 110.606 1.00 43.22  ? 89  PRO A CG    1 
ATOM   3979 C  CD    . PRO B 2 89  ? 109.346 170.107 109.434 1.00 46.19  ? 89  PRO A CD    1 
ATOM   3980 N  N     . GLU B 2 90  ? 109.873 166.385 110.131 1.00 53.47  ? 90  GLU A N     1 
ATOM   3981 C  CA    . GLU B 2 90  ? 109.823 164.932 110.207 1.00 53.47  ? 90  GLU A CA    1 
ATOM   3982 C  C     . GLU B 2 90  ? 111.050 164.259 109.609 1.00 53.59  ? 90  GLU A C     1 
ATOM   3983 O  O     . GLU B 2 90  ? 111.206 163.046 109.769 1.00 58.58  ? 90  GLU A O     1 
ATOM   3984 C  CB    . GLU B 2 90  ? 108.566 164.412 109.507 1.00 57.27  ? 90  GLU A CB    1 
ATOM   3985 C  CG    . GLU B 2 90  ? 107.279 164.669 110.274 1.00 60.84  ? 90  GLU A CG    1 
ATOM   3986 C  CD    . GLU B 2 90  ? 107.033 163.644 111.364 1.00 64.74  ? 90  GLU A CD    1 
ATOM   3987 O  OE1   . GLU B 2 90  ? 107.716 162.598 111.366 1.00 64.49  ? 90  GLU A OE1   1 
ATOM   3988 O  OE2   . GLU B 2 90  ? 106.155 163.885 112.219 1.00 65.23  ? 90  GLU A OE2   1 
ATOM   3989 N  N     . GLN B 2 91  ? 111.916 165.004 108.921 1.00 50.48  ? 91  GLN A N     1 
ATOM   3990 C  CA    . GLN B 2 91  ? 113.137 164.416 108.387 1.00 47.70  ? 91  GLN A CA    1 
ATOM   3991 C  C     . GLN B 2 91  ? 114.190 164.207 109.463 1.00 53.59  ? 91  GLN A C     1 
ATOM   3992 O  O     . GLN B 2 91  ? 115.003 163.284 109.355 1.00 58.69  ? 91  GLN A O     1 
ATOM   3993 C  CB    . GLN B 2 91  ? 113.705 165.289 107.272 1.00 45.46  ? 91  GLN A CB    1 
ATOM   3994 C  CG    . GLN B 2 91  ? 112.873 165.292 106.013 1.00 49.32  ? 91  GLN A CG    1 
ATOM   3995 C  CD    . GLN B 2 91  ? 113.416 166.241 104.972 1.00 57.80  ? 91  GLN A CD    1 
ATOM   3996 O  OE1   . GLN B 2 91  ? 114.284 167.061 105.259 1.00 58.72  ? 91  GLN A OE1   1 
ATOM   3997 N  NE2   . GLN B 2 91  ? 112.906 166.136 103.750 1.00 57.23  ? 91  GLN A NE2   1 
ATOM   3998 N  N     . LEU B 2 92  ? 114.199 165.045 110.495 1.00 45.73  ? 92  LEU A N     1 
ATOM   3999 C  CA    . LEU B 2 92  ? 115.145 164.902 111.594 1.00 40.10  ? 92  LEU A CA    1 
ATOM   4000 C  C     . LEU B 2 92  ? 114.554 163.956 112.632 1.00 46.31  ? 92  LEU A C     1 
ATOM   4001 O  O     . LEU B 2 92  ? 113.588 164.300 113.318 1.00 53.28  ? 92  LEU A O     1 
ATOM   4002 C  CB    . LEU B 2 92  ? 115.463 166.265 112.199 1.00 42.49  ? 92  LEU A CB    1 
ATOM   4003 C  CG    . LEU B 2 92  ? 115.645 167.429 111.228 1.00 44.63  ? 92  LEU A CG    1 
ATOM   4004 C  CD1   . LEU B 2 92  ? 115.876 168.712 111.979 1.00 49.71  ? 92  LEU A CD1   1 
ATOM   4005 C  CD2   . LEU B 2 92  ? 116.785 167.167 110.274 1.00 47.35  ? 92  LEU A CD2   1 
ATOM   4006 N  N     . ILE B 2 93  ? 115.133 162.765 112.751 1.00 47.02  ? 93  ILE A N     1 
ATOM   4007 C  CA    . ILE B 2 93  ? 114.607 161.696 113.591 1.00 39.11  ? 93  ILE A CA    1 
ATOM   4008 C  C     . ILE B 2 93  ? 115.597 161.422 114.711 1.00 48.59  ? 93  ILE A C     1 
ATOM   4009 O  O     . ILE B 2 93  ? 116.794 161.254 114.457 1.00 56.40  ? 93  ILE A O     1 
ATOM   4010 C  CB    . ILE B 2 93  ? 114.340 160.421 112.775 1.00 39.68  ? 93  ILE A CB    1 
ATOM   4011 C  CG1   . ILE B 2 93  ? 113.446 160.742 111.581 1.00 47.15  ? 93  ILE A CG1   1 
ATOM   4012 C  CG2   . ILE B 2 93  ? 113.715 159.352 113.644 1.00 45.93  ? 93  ILE A CG2   1 
ATOM   4013 C  CD1   . ILE B 2 93  ? 113.160 159.564 110.699 1.00 52.05  ? 93  ILE A CD1   1 
ATOM   4014 N  N     . THR B 2 94  ? 115.100 161.373 115.944 1.00 54.09  ? 94  THR A N     1 
ATOM   4015 C  CA    . THR B 2 94  ? 115.953 161.198 117.107 1.00 50.72  ? 94  THR A CA    1 
ATOM   4016 C  C     . THR B 2 94  ? 115.344 160.169 118.047 1.00 49.69  ? 94  THR A C     1 
ATOM   4017 O  O     . THR B 2 94  ? 114.141 159.906 118.012 1.00 50.64  ? 94  THR A O     1 
ATOM   4018 C  CB    . THR B 2 94  ? 116.177 162.521 117.839 1.00 54.05  ? 94  THR A CB    1 
ATOM   4019 O  OG1   . THR B 2 94  ? 117.426 162.468 118.530 1.00 60.68  ? 94  THR A OG1   1 
ATOM   4020 C  CG2   . THR B 2 94  ? 115.061 162.790 118.831 1.00 58.71  ? 94  THR A CG2   1 
ATOM   4021 N  N     . GLY B 2 95  ? 116.198 159.570 118.878 1.00 56.74  ? 95  GLY A N     1 
ATOM   4022 C  CA    . GLY B 2 95  ? 115.798 158.557 119.817 1.00 56.99  ? 95  GLY A CA    1 
ATOM   4023 C  C     . GLY B 2 95  ? 115.834 159.038 121.253 1.00 61.20  ? 95  GLY A C     1 
ATOM   4024 O  O     . GLY B 2 95  ? 115.738 160.236 121.545 1.00 64.83  ? 95  GLY A O     1 
ATOM   4025 N  N     . LYS B 2 96  ? 115.974 158.082 122.169 1.00 61.35  ? 96  LYS A N     1 
ATOM   4026 C  CA    . LYS B 2 96  ? 116.005 158.355 123.600 1.00 61.80  ? 96  LYS A CA    1 
ATOM   4027 C  C     . LYS B 2 96  ? 117.381 158.148 124.215 1.00 62.62  ? 96  LYS A C     1 
ATOM   4028 O  O     . LYS B 2 96  ? 117.902 159.047 124.876 1.00 63.68  ? 96  LYS A O     1 
ATOM   4029 C  CB    . LYS B 2 96  ? 114.981 157.470 124.322 1.00 66.39  ? 96  LYS A CB    1 
ATOM   4030 C  CG    . LYS B 2 96  ? 113.532 157.804 124.019 1.00 66.27  ? 96  LYS A CG    1 
ATOM   4031 C  CD    . LYS B 2 96  ? 113.155 159.173 124.545 1.00 66.22  ? 96  LYS A CD    1 
ATOM   4032 C  CE    . LYS B 2 96  ? 111.654 159.384 124.491 1.00 65.76  ? 96  LYS A CE    1 
ATOM   4033 N  NZ    . LYS B 2 96  ? 110.926 158.337 125.257 1.00 67.46  ? 96  LYS A NZ    1 
ATOM   4034 N  N     . GLU B 2 97  ? 117.984 156.979 124.018 1.00 70.85  ? 97  GLU A N     1 
ATOM   4035 C  CA    . GLU B 2 97  ? 119.309 156.672 124.536 1.00 66.51  ? 97  GLU A CA    1 
ATOM   4036 C  C     . GLU B 2 97  ? 120.190 156.165 123.405 1.00 68.58  ? 97  GLU A C     1 
ATOM   4037 O  O     . GLU B 2 97  ? 119.712 155.481 122.496 1.00 71.72  ? 97  GLU A O     1 
ATOM   4038 C  CB    . GLU B 2 97  ? 119.245 155.633 125.655 1.00 67.11  ? 97  GLU A CB    1 
ATOM   4039 C  CG    . GLU B 2 97  ? 118.708 156.172 126.967 1.00 70.39  ? 97  GLU A CG    1 
ATOM   4040 C  CD    . GLU B 2 97  ? 118.941 155.222 128.123 1.00 76.51  ? 97  GLU A CD    1 
ATOM   4041 O  OE1   . GLU B 2 97  ? 119.418 154.094 127.880 1.00 74.49  ? 97  GLU A OE1   1 
ATOM   4042 O  OE2   . GLU B 2 97  ? 118.649 155.604 129.275 1.00 77.11  ? 97  GLU A OE2   1 
ATOM   4043 N  N     . ASP B 2 98  ? 121.475 156.499 123.465 1.00 59.96  ? 98  ASP A N     1 
ATOM   4044 C  CA    . ASP B 2 98  ? 122.394 156.199 122.379 1.00 60.04  ? 98  ASP A CA    1 
ATOM   4045 C  C     . ASP B 2 98  ? 122.909 154.766 122.479 1.00 64.57  ? 98  ASP A C     1 
ATOM   4046 O  O     . ASP B 2 98  ? 122.577 154.016 123.399 1.00 66.54  ? 98  ASP A O     1 
ATOM   4047 C  CB    . ASP B 2 98  ? 123.550 157.192 122.379 1.00 60.31  ? 98  ASP A CB    1 
ATOM   4048 C  CG    . ASP B 2 98  ? 124.192 157.335 123.740 1.00 68.06  ? 98  ASP A CG    1 
ATOM   4049 O  OD1   . ASP B 2 98  ? 124.963 156.435 124.134 1.00 69.18  ? 98  ASP A OD1   1 
ATOM   4050 O  OD2   . ASP B 2 98  ? 123.928 158.350 124.418 1.00 69.54  ? 98  ASP A OD2   1 
ATOM   4051 N  N     . ALA B 2 99  ? 123.737 154.381 121.508 1.00 59.01  ? 99  ALA A N     1 
ATOM   4052 C  CA    . ALA B 2 99  ? 124.291 153.037 121.454 1.00 52.60  ? 99  ALA A CA    1 
ATOM   4053 C  C     . ALA B 2 99  ? 125.467 152.839 122.397 1.00 54.76  ? 99  ALA A C     1 
ATOM   4054 O  O     . ALA B 2 99  ? 125.867 151.694 122.621 1.00 64.70  ? 99  ALA A O     1 
ATOM   4055 C  CB    . ALA B 2 99  ? 124.716 152.703 120.026 1.00 52.53  ? 99  ALA A CB    1 
ATOM   4056 N  N     . ALA B 2 100 ? 126.025 153.916 122.949 1.00 47.25  ? 100 ALA A N     1 
ATOM   4057 C  CA    . ALA B 2 100 ? 127.094 153.841 123.944 1.00 43.24  ? 100 ALA A CA    1 
ATOM   4058 C  C     . ALA B 2 100 ? 128.294 153.045 123.433 1.00 44.42  ? 100 ALA A C     1 
ATOM   4059 O  O     . ALA B 2 100 ? 128.810 152.156 124.110 1.00 54.91  ? 100 ALA A O     1 
ATOM   4060 C  CB    . ALA B 2 100 ? 126.574 153.261 125.259 1.00 47.14  ? 100 ALA A CB    1 
ATOM   4061 N  N     . ASN B 2 101 ? 128.734 153.376 122.220 1.00 36.63  ? 101 ASN A N     1 
ATOM   4062 C  CA    . ASN B 2 101 ? 129.914 152.773 121.604 1.00 37.03  ? 101 ASN A CA    1 
ATOM   4063 C  C     . ASN B 2 101 ? 129.776 151.263 121.467 1.00 48.23  ? 101 ASN A C     1 
ATOM   4064 O  O     . ASN B 2 101 ? 130.770 150.535 121.477 1.00 56.59  ? 101 ASN A O     1 
ATOM   4065 C  CB    . ASN B 2 101 ? 131.182 153.128 122.379 1.00 43.85  ? 101 ASN A CB    1 
ATOM   4066 C  CG    . ASN B 2 101 ? 131.849 154.379 121.859 1.00 46.80  ? 101 ASN A CG    1 
ATOM   4067 O  OD1   . ASN B 2 101 ? 131.446 154.929 120.840 1.00 43.52  ? 101 ASN A OD1   1 
ATOM   4068 N  ND2   . ASN B 2 101 ? 132.867 154.842 122.565 1.00 49.15  ? 101 ASN A ND2   1 
ATOM   4069 N  N     . ASN B 2 102 ? 128.547 150.779 121.331 1.00 50.41  ? 102 ASN A N     1 
ATOM   4070 C  CA    . ASN B 2 102 ? 128.260 149.353 121.256 1.00 43.83  ? 102 ASN A CA    1 
ATOM   4071 C  C     . ASN B 2 102 ? 127.573 149.052 119.936 1.00 48.16  ? 102 ASN A C     1 
ATOM   4072 O  O     . ASN B 2 102 ? 126.542 149.652 119.615 1.00 53.49  ? 102 ASN A O     1 
ATOM   4073 C  CB    . ASN B 2 102 ? 127.390 148.905 122.428 1.00 40.57  ? 102 ASN A CB    1 
ATOM   4074 C  CG    . ASN B 2 102 ? 127.794 147.561 122.968 1.00 47.98  ? 102 ASN A CG    1 
ATOM   4075 O  OD1   . ASN B 2 102 ? 128.870 147.055 122.666 1.00 54.94  ? 102 ASN A OD1   1 
ATOM   4076 N  ND2   . ASN B 2 102 ? 126.929 146.969 123.774 1.00 47.44  ? 102 ASN A ND2   1 
ATOM   4077 N  N     . TYR B 2 103 ? 128.146 148.120 119.177 1.00 40.34  ? 103 TYR A N     1 
ATOM   4078 C  CA    . TYR B 2 103 ? 127.561 147.726 117.903 1.00 36.83  ? 103 TYR A CA    1 
ATOM   4079 C  C     . TYR B 2 103 ? 126.206 147.060 118.101 1.00 45.23  ? 103 TYR A C     1 
ATOM   4080 O  O     . TYR B 2 103 ? 125.267 147.312 117.339 1.00 57.28  ? 103 TYR A O     1 
ATOM   4081 C  CB    . TYR B 2 103 ? 128.526 146.797 117.170 1.00 39.30  ? 103 TYR A CB    1 
ATOM   4082 C  CG    . TYR B 2 103 ? 128.005 146.201 115.888 1.00 37.84  ? 103 TYR A CG    1 
ATOM   4083 C  CD1   . TYR B 2 103 ? 127.303 145.011 115.892 1.00 42.31  ? 103 TYR A CD1   1 
ATOM   4084 C  CD2   . TYR B 2 103 ? 128.253 146.803 114.673 1.00 42.87  ? 103 TYR A CD2   1 
ATOM   4085 C  CE1   . TYR B 2 103 ? 126.834 144.461 114.731 1.00 45.91  ? 103 TYR A CE1   1 
ATOM   4086 C  CE2   . TYR B 2 103 ? 127.794 146.256 113.506 1.00 47.33  ? 103 TYR A CE2   1 
ATOM   4087 C  CZ    . TYR B 2 103 ? 127.082 145.085 113.541 1.00 49.98  ? 103 TYR A CZ    1 
ATOM   4088 O  OH    . TYR B 2 103 ? 126.618 144.527 112.376 1.00 53.22  ? 103 TYR A OH    1 
ATOM   4089 N  N     . ALA B 2 104 ? 126.087 146.205 119.118 1.00 43.68  ? 104 ALA A N     1 
ATOM   4090 C  CA    . ALA B 2 104 ? 124.869 145.424 119.302 1.00 39.10  ? 104 ALA A CA    1 
ATOM   4091 C  C     . ALA B 2 104 ? 123.688 146.306 119.675 1.00 44.34  ? 104 ALA A C     1 
ATOM   4092 O  O     . ALA B 2 104 ? 122.557 146.063 119.232 1.00 52.10  ? 104 ALA A O     1 
ATOM   4093 C  CB    . ALA B 2 104 ? 125.094 144.356 120.365 1.00 45.21  ? 104 ALA A CB    1 
ATOM   4094 N  N     . ARG B 2 105 ? 123.925 147.326 120.500 1.00 47.19  ? 105 ARG A N     1 
ATOM   4095 C  CA    . ARG B 2 105 ? 122.849 148.226 120.889 1.00 45.26  ? 105 ARG A CA    1 
ATOM   4096 C  C     . ARG B 2 105 ? 122.285 148.958 119.683 1.00 49.98  ? 105 ARG A C     1 
ATOM   4097 O  O     . ARG B 2 105 ? 121.064 149.055 119.521 1.00 56.95  ? 105 ARG A O     1 
ATOM   4098 C  CB    . ARG B 2 105 ? 123.352 149.219 121.935 1.00 46.66  ? 105 ARG A CB    1 
ATOM   4099 C  CG    . ARG B 2 105 ? 123.462 148.635 123.322 1.00 45.77  ? 105 ARG A CG    1 
ATOM   4100 C  CD    . ARG B 2 105 ? 123.979 149.649 124.308 1.00 47.18  ? 105 ARG A CD    1 
ATOM   4101 N  NE    . ARG B 2 105 ? 123.017 150.715 124.545 1.00 46.15  ? 105 ARG A NE    1 
ATOM   4102 C  CZ    . ARG B 2 105 ? 122.089 150.685 125.489 1.00 50.98  ? 105 ARG A CZ    1 
ATOM   4103 N  NH1   . ARG B 2 105 ? 121.961 149.648 126.298 1.00 52.24  ? 105 ARG A NH1   1 
ATOM   4104 N  NH2   . ARG B 2 105 ? 121.269 151.721 125.625 1.00 51.82  ? 105 ARG A NH2   1 
ATOM   4105 N  N     . GLY B 2 106 ? 123.156 149.469 118.816 1.00 48.45  ? 106 GLY A N     1 
ATOM   4106 C  CA    . GLY B 2 106 ? 122.682 150.128 117.617 1.00 46.01  ? 106 GLY A CA    1 
ATOM   4107 C  C     . GLY B 2 106 ? 122.137 149.177 116.581 1.00 49.76  ? 106 GLY A C     1 
ATOM   4108 O  O     . GLY B 2 106 ? 121.355 149.594 115.723 1.00 56.32  ? 106 GLY A O     1 
ATOM   4109 N  N     . HIS B 2 107 ? 122.522 147.906 116.647 1.00 43.84  ? 107 HIS A N     1 
ATOM   4110 C  CA    . HIS B 2 107 ? 122.065 146.940 115.658 1.00 40.65  ? 107 HIS A CA    1 
ATOM   4111 C  C     . HIS B 2 107 ? 120.665 146.435 115.978 1.00 47.89  ? 107 HIS A C     1 
ATOM   4112 O  O     . HIS B 2 107 ? 119.750 146.563 115.160 1.00 56.19  ? 107 HIS A O     1 
ATOM   4113 C  CB    . HIS B 2 107 ? 123.048 145.776 115.565 1.00 41.85  ? 107 HIS A CB    1 
ATOM   4114 C  CG    . HIS B 2 107 ? 122.880 144.945 114.334 1.00 49.48  ? 107 HIS A CG    1 
ATOM   4115 N  ND1   . HIS B 2 107 ? 123.669 143.849 114.062 1.00 49.65  ? 107 HIS A ND1   1 
ATOM   4116 C  CD2   . HIS B 2 107 ? 122.012 145.047 113.302 1.00 51.95  ? 107 HIS A CD2   1 
ATOM   4117 C  CE1   . HIS B 2 107 ? 123.295 143.313 112.915 1.00 48.53  ? 107 HIS A CE1   1 
ATOM   4118 N  NE2   . HIS B 2 107 ? 122.292 144.021 112.433 1.00 50.69  ? 107 HIS A NE2   1 
ATOM   4119 N  N     . TYR B 2 108 ? 120.473 145.854 117.161 1.00 48.11  ? 108 TYR A N     1 
ATOM   4120 C  CA    . TYR B 2 108 ? 119.159 145.318 117.500 1.00 46.06  ? 108 TYR A CA    1 
ATOM   4121 C  C     . TYR B 2 108 ? 118.500 146.020 118.679 1.00 52.12  ? 108 TYR A C     1 
ATOM   4122 O  O     . TYR B 2 108 ? 117.417 146.582 118.509 1.00 62.23  ? 108 TYR A O     1 
ATOM   4123 C  CB    . TYR B 2 108 ? 119.249 143.815 117.770 1.00 48.77  ? 108 TYR A CB    1 
ATOM   4124 C  CG    . TYR B 2 108 ? 117.901 143.144 117.756 1.00 51.92  ? 108 TYR A CG    1 
ATOM   4125 C  CD1   . TYR B 2 108 ? 117.251 142.885 116.566 1.00 48.62  ? 108 TYR A CD1   1 
ATOM   4126 C  CD2   . TYR B 2 108 ? 117.270 142.786 118.933 1.00 53.62  ? 108 TYR A CD2   1 
ATOM   4127 C  CE1   . TYR B 2 108 ? 116.019 142.278 116.547 1.00 52.10  ? 108 TYR A CE1   1 
ATOM   4128 C  CE2   . TYR B 2 108 ? 116.035 142.180 118.922 1.00 52.72  ? 108 TYR A CE2   1 
ATOM   4129 C  CZ    . TYR B 2 108 ? 115.418 141.926 117.726 1.00 52.73  ? 108 TYR A CZ    1 
ATOM   4130 O  OH    . TYR B 2 108 ? 114.186 141.324 117.710 1.00 54.55  ? 108 TYR A OH    1 
ATOM   4131 N  N     . THR B 2 109 ? 119.123 146.037 119.857 1.00 48.83  ? 109 THR A N     1 
ATOM   4132 C  CA    . THR B 2 109 ? 118.381 146.362 121.074 1.00 45.84  ? 109 THR A CA    1 
ATOM   4133 C  C     . THR B 2 109 ? 117.806 147.773 121.030 1.00 52.44  ? 109 THR A C     1 
ATOM   4134 O  O     . THR B 2 109 ? 116.635 147.982 121.362 1.00 53.50  ? 109 THR A O     1 
ATOM   4135 C  CB    . THR B 2 109 ? 119.276 146.181 122.295 1.00 49.92  ? 109 THR A CB    1 
ATOM   4136 O  OG1   . THR B 2 109 ? 119.680 144.812 122.380 1.00 47.70  ? 109 THR A OG1   1 
ATOM   4137 C  CG2   . THR B 2 109 ? 118.531 146.558 123.562 1.00 53.50  ? 109 THR A CG2   1 
ATOM   4138 N  N     . ILE B 2 110 ? 118.604 148.751 120.608 1.00 55.72  ? 110 ILE A N     1 
ATOM   4139 C  CA    . ILE B 2 110 ? 118.108 150.110 120.431 1.00 51.57  ? 110 ILE A CA    1 
ATOM   4140 C  C     . ILE B 2 110 ? 117.810 150.417 118.968 1.00 53.76  ? 110 ILE A C     1 
ATOM   4141 O  O     . ILE B 2 110 ? 117.107 151.398 118.683 1.00 56.90  ? 110 ILE A O     1 
ATOM   4142 C  CB    . ILE B 2 110 ? 119.104 151.137 121.008 1.00 53.89  ? 110 ILE A CB    1 
ATOM   4143 C  CG1   . ILE B 2 110 ? 119.747 150.588 122.275 1.00 54.11  ? 110 ILE A CG1   1 
ATOM   4144 C  CG2   . ILE B 2 110 ? 118.409 152.441 121.325 1.00 57.33  ? 110 ILE A CG2   1 
ATOM   4145 C  CD1   . ILE B 2 110 ? 118.790 150.460 123.432 1.00 58.15  ? 110 ILE A CD1   1 
ATOM   4146 N  N     . GLY B 2 111 ? 118.308 149.604 118.038 1.00 49.34  ? 111 GLY A N     1 
ATOM   4147 C  CA    . GLY B 2 111 ? 118.006 149.823 116.636 1.00 51.75  ? 111 GLY A CA    1 
ATOM   4148 C  C     . GLY B 2 111 ? 116.562 149.535 116.274 1.00 57.31  ? 111 GLY A C     1 
ATOM   4149 O  O     . GLY B 2 111 ? 115.965 150.254 115.470 1.00 62.36  ? 111 GLY A O     1 
ATOM   4150 N  N     . LYS B 2 112 ? 115.977 148.486 116.851 1.00 53.80  ? 112 LYS A N     1 
ATOM   4151 C  CA    . LYS B 2 112 ? 114.644 148.083 116.420 1.00 51.20  ? 112 LYS A CA    1 
ATOM   4152 C  C     . LYS B 2 112 ? 113.570 148.928 117.089 1.00 56.57  ? 112 LYS A C     1 
ATOM   4153 O  O     . LYS B 2 112 ? 112.559 148.407 117.570 1.00 61.58  ? 112 LYS A O     1 
ATOM   4154 C  CB    . LYS B 2 112 ? 114.406 146.601 116.721 1.00 54.90  ? 112 LYS A CB    1 
ATOM   4155 C  CG    . LYS B 2 112 ? 114.491 146.235 118.194 1.00 56.30  ? 112 LYS A CG    1 
ATOM   4156 C  CD    . LYS B 2 112 ? 113.674 145.013 118.536 1.00 55.97  ? 112 LYS A CD    1 
ATOM   4157 C  CE    . LYS B 2 112 ? 113.694 144.760 120.031 1.00 53.10  ? 112 LYS A CE    1 
ATOM   4158 N  NZ    . LYS B 2 112 ? 113.245 145.948 120.798 1.00 53.90  ? 112 LYS A NZ    1 
ATOM   4159 N  N     . GLU B 2 113 ? 113.753 150.242 117.081 1.00 62.06  ? 113 GLU A N     1 
ATOM   4160 C  CA    . GLU B 2 113 ? 112.759 151.147 117.643 1.00 59.21  ? 113 GLU A CA    1 
ATOM   4161 C  C     . GLU B 2 113 ? 112.503 152.377 116.797 1.00 60.26  ? 113 GLU A C     1 
ATOM   4162 O  O     . GLU B 2 113 ? 111.432 152.977 116.935 1.00 66.55  ? 113 GLU A O     1 
ATOM   4163 C  CB    . GLU B 2 113 ? 113.170 151.590 119.050 1.00 64.55  ? 113 GLU A CB    1 
ATOM   4164 C  CG    . GLU B 2 113 ? 112.566 150.750 120.159 1.00 68.47  ? 113 GLU A CG    1 
ATOM   4165 C  CD    . GLU B 2 113 ? 113.315 149.452 120.380 1.00 72.49  ? 113 GLU A CD    1 
ATOM   4166 O  OE1   . GLU B 2 113 ? 114.514 149.392 120.036 1.00 70.23  ? 113 GLU A OE1   1 
ATOM   4167 O  OE2   . GLU B 2 113 ? 112.706 148.492 120.895 1.00 71.25  ? 113 GLU A OE2   1 
ATOM   4168 N  N     . ILE B 2 114 ? 113.429 152.785 115.933 1.00 54.56  ? 114 ILE A N     1 
ATOM   4169 C  CA    . ILE B 2 114 ? 113.207 153.929 115.063 1.00 58.91  ? 114 ILE A CA    1 
ATOM   4170 C  C     . ILE B 2 114 ? 113.491 153.530 113.623 1.00 65.19  ? 114 ILE A C     1 
ATOM   4171 O  O     . ILE B 2 114 ? 113.503 154.379 112.725 1.00 72.46  ? 114 ILE A O     1 
ATOM   4172 C  CB    . ILE B 2 114 ? 114.067 155.134 115.481 1.00 61.40  ? 114 ILE A CB    1 
ATOM   4173 C  CG1   . ILE B 2 114 ? 115.544 154.764 115.485 1.00 58.38  ? 114 ILE A CG1   1 
ATOM   4174 C  CG2   . ILE B 2 114 ? 113.638 155.650 116.845 1.00 65.43  ? 114 ILE A CG2   1 
ATOM   4175 C  CD1   . ILE B 2 114 ? 116.451 155.956 115.488 1.00 62.15  ? 114 ILE A CD1   1 
ATOM   4176 N  N     . ILE B 2 115 ? 113.715 152.237 113.389 1.00 56.28  ? 115 ILE A N     1 
ATOM   4177 C  CA    . ILE B 2 115 ? 114.059 151.779 112.048 1.00 48.47  ? 115 ILE A CA    1 
ATOM   4178 C  C     . ILE B 2 115 ? 112.864 151.907 111.110 1.00 54.20  ? 115 ILE A C     1 
ATOM   4179 O  O     . ILE B 2 115 ? 113.001 152.350 109.960 1.00 64.52  ? 115 ILE A O     1 
ATOM   4180 C  CB    . ILE B 2 115 ? 114.602 150.341 112.105 1.00 48.48  ? 115 ILE A CB    1 
ATOM   4181 C  CG1   . ILE B 2 115 ? 114.861 149.808 110.701 1.00 51.11  ? 115 ILE A CG1   1 
ATOM   4182 C  CG2   . ILE B 2 115 ? 113.662 149.434 112.876 1.00 57.32  ? 115 ILE A CG2   1 
ATOM   4183 C  CD1   . ILE B 2 115 ? 115.949 150.540 109.984 1.00 56.25  ? 115 ILE A CD1   1 
ATOM   4184 N  N     . ASP B 2 116 ? 111.672 151.546 111.587 1.00 56.76  ? 116 ASP A N     1 
ATOM   4185 C  CA    . ASP B 2 116 ? 110.480 151.645 110.754 1.00 57.14  ? 116 ASP A CA    1 
ATOM   4186 C  C     . ASP B 2 116 ? 110.190 153.090 110.383 1.00 59.75  ? 116 ASP A C     1 
ATOM   4187 O  O     . ASP B 2 116 ? 109.739 153.375 109.267 1.00 67.99  ? 116 ASP A O     1 
ATOM   4188 C  CB    . ASP B 2 116 ? 109.287 151.025 111.475 1.00 62.24  ? 116 ASP A CB    1 
ATOM   4189 C  CG    . ASP B 2 116 ? 109.459 149.543 111.713 1.00 68.47  ? 116 ASP A CG    1 
ATOM   4190 O  OD1   . ASP B 2 116 ? 110.522 149.002 111.342 1.00 66.81  ? 116 ASP A OD1   1 
ATOM   4191 O  OD2   . ASP B 2 116 ? 108.535 148.916 112.271 1.00 68.03  ? 116 ASP A OD2   1 
ATOM   4192 N  N     . LEU B 2 117 ? 110.445 154.017 111.303 1.00 49.69  ? 117 LEU A N     1 
ATOM   4193 C  CA    . LEU B 2 117 ? 110.173 155.423 111.035 1.00 46.96  ? 117 LEU A CA    1 
ATOM   4194 C  C     . LEU B 2 117 ? 111.065 155.958 109.919 1.00 54.68  ? 117 LEU A C     1 
ATOM   4195 O  O     . LEU B 2 117 ? 110.583 156.629 108.994 1.00 61.48  ? 117 LEU A O     1 
ATOM   4196 C  CB    . LEU B 2 117 ? 110.356 156.222 112.319 1.00 49.75  ? 117 LEU A CB    1 
ATOM   4197 C  CG    . LEU B 2 117 ? 109.383 157.365 112.575 1.00 57.44  ? 117 LEU A CG    1 
ATOM   4198 C  CD1   . LEU B 2 117 ? 107.954 156.881 112.430 1.00 58.03  ? 117 LEU A CD1   1 
ATOM   4199 C  CD2   . LEU B 2 117 ? 109.612 157.927 113.961 1.00 55.99  ? 117 LEU A CD2   1 
ATOM   4200 N  N     . VAL B 2 118 ? 112.365 155.663 109.977 1.00 47.17  ? 118 VAL A N     1 
ATOM   4201 C  CA    . VAL B 2 118 ? 113.269 156.128 108.931 1.00 43.79  ? 118 VAL A CA    1 
ATOM   4202 C  C     . VAL B 2 118 ? 112.957 155.437 107.608 1.00 46.37  ? 118 VAL A C     1 
ATOM   4203 O  O     . VAL B 2 118 ? 113.067 156.048 106.536 1.00 55.77  ? 118 VAL A O     1 
ATOM   4204 C  CB    . VAL B 2 118 ? 114.740 155.947 109.357 1.00 44.65  ? 118 VAL A CB    1 
ATOM   4205 C  CG1   . VAL B 2 118 ? 114.931 156.384 110.786 1.00 50.34  ? 118 VAL A CG1   1 
ATOM   4206 C  CG2   . VAL B 2 118 ? 115.201 154.520 109.187 1.00 48.47  ? 118 VAL A CG2   1 
ATOM   4207 N  N     . LEU B 2 119 ? 112.549 154.167 107.654 1.00 43.30  ? 119 LEU A N     1 
ATOM   4208 C  CA    . LEU B 2 119 ? 112.158 153.488 106.423 1.00 44.40  ? 119 LEU A CA    1 
ATOM   4209 C  C     . LEU B 2 119 ? 110.945 154.153 105.792 1.00 47.91  ? 119 LEU A C     1 
ATOM   4210 O  O     . LEU B 2 119 ? 110.894 154.344 104.571 1.00 60.01  ? 119 LEU A O     1 
ATOM   4211 C  CB    . LEU B 2 119 ? 111.876 152.015 106.702 1.00 48.32  ? 119 LEU A CB    1 
ATOM   4212 C  CG    . LEU B 2 119 ? 113.091 151.101 106.825 1.00 45.82  ? 119 LEU A CG    1 
ATOM   4213 C  CD1   . LEU B 2 119 ? 112.647 149.678 107.070 1.00 51.15  ? 119 LEU A CD1   1 
ATOM   4214 C  CD2   . LEU B 2 119 ? 113.939 151.188 105.582 1.00 44.21  ? 119 LEU A CD2   1 
ATOM   4215 N  N     . ASP B 2 120 ? 109.960 154.519 106.611 1.00 47.58  ? 120 ASP A N     1 
ATOM   4216 C  CA    . ASP B 2 120 ? 108.779 155.198 106.094 1.00 49.91  ? 120 ASP A CA    1 
ATOM   4217 C  C     . ASP B 2 120 ? 109.141 156.548 105.491 1.00 51.64  ? 120 ASP A C     1 
ATOM   4218 O  O     . ASP B 2 120 ? 108.629 156.919 104.428 1.00 53.83  ? 120 ASP A O     1 
ATOM   4219 C  CB    . ASP B 2 120 ? 107.744 155.362 107.203 1.00 52.63  ? 120 ASP A CB    1 
ATOM   4220 C  CG    . ASP B 2 120 ? 106.632 156.319 106.826 1.00 66.42  ? 120 ASP A CG    1 
ATOM   4221 O  OD1   . ASP B 2 120 ? 105.815 155.966 105.950 1.00 67.23  ? 120 ASP A OD1   1 
ATOM   4222 O  OD2   . ASP B 2 120 ? 106.575 157.424 107.404 1.00 65.81  ? 120 ASP A OD2   1 
ATOM   4223 N  N     . ARG B 2 121 ? 110.027 157.295 106.151 1.00 51.33  ? 121 ARG A N     1 
ATOM   4224 C  CA    . ARG B 2 121 ? 110.432 158.587 105.606 1.00 48.13  ? 121 ARG A CA    1 
ATOM   4225 C  C     . ARG B 2 121 ? 111.151 158.431 104.272 1.00 52.25  ? 121 ARG A C     1 
ATOM   4226 O  O     . ARG B 2 121 ? 110.905 159.199 103.335 1.00 61.34  ? 121 ARG A O     1 
ATOM   4227 C  CB    . ARG B 2 121 ? 111.313 159.331 106.604 1.00 49.57  ? 121 ARG A CB    1 
ATOM   4228 C  CG    . ARG B 2 121 ? 110.570 159.830 107.823 1.00 57.77  ? 121 ARG A CG    1 
ATOM   4229 C  CD    . ARG B 2 121 ? 109.279 160.536 107.459 1.00 58.31  ? 121 ARG A CD    1 
ATOM   4230 N  NE    . ARG B 2 121 ? 109.479 161.580 106.463 1.00 59.90  ? 121 ARG A NE    1 
ATOM   4231 C  CZ    . ARG B 2 121 ? 108.549 162.450 106.096 1.00 60.54  ? 121 ARG A CZ    1 
ATOM   4232 N  NH1   . ARG B 2 121 ? 107.343 162.441 106.635 1.00 55.64  ? 121 ARG A NH1   1 
ATOM   4233 N  NH2   . ARG B 2 121 ? 108.839 163.354 105.166 1.00 61.93  ? 121 ARG A NH2   1 
ATOM   4234 N  N     . ILE B 2 122 ? 112.045 157.447 104.165 1.00 51.58  ? 122 ILE A N     1 
ATOM   4235 C  CA    . ILE B 2 122 ? 112.759 157.236 102.908 1.00 44.03  ? 122 ILE A CA    1 
ATOM   4236 C  C     . ILE B 2 122 ? 111.792 156.826 101.807 1.00 47.36  ? 122 ILE A C     1 
ATOM   4237 O  O     . ILE B 2 122 ? 111.902 157.285 100.664 1.00 60.26  ? 122 ILE A O     1 
ATOM   4238 C  CB    . ILE B 2 122 ? 113.884 156.205 103.098 1.00 44.57  ? 122 ILE A CB    1 
ATOM   4239 C  CG1   . ILE B 2 122 ? 114.984 156.798 103.968 1.00 50.76  ? 122 ILE A CG1   1 
ATOM   4240 C  CG2   . ILE B 2 122 ? 114.460 155.790 101.768 1.00 50.50  ? 122 ILE A CG2   1 
ATOM   4241 C  CD1   . ILE B 2 122 ? 116.100 155.846 104.251 1.00 54.67  ? 122 ILE A CD1   1 
ATOM   4242 N  N     . ARG B 2 123 ? 110.828 155.964 102.129 1.00 49.63  ? 123 ARG A N     1 
ATOM   4243 C  CA    . ARG B 2 123 ? 109.838 155.567 101.135 1.00 49.25  ? 123 ARG A CA    1 
ATOM   4244 C  C     . ARG B 2 123 ? 109.021 156.763 100.670 1.00 53.09  ? 123 ARG A C     1 
ATOM   4245 O  O     . ARG B 2 123 ? 108.694 156.879 99.484  1.00 60.45  ? 123 ARG A O     1 
ATOM   4246 C  CB    . ARG B 2 123 ? 108.932 154.482 101.707 1.00 51.51  ? 123 ARG A CB    1 
ATOM   4247 C  CG    . ARG B 2 123 ? 107.814 154.065 100.782 1.00 53.15  ? 123 ARG A CG    1 
ATOM   4248 C  CD    . ARG B 2 123 ? 107.081 152.856 101.326 1.00 59.43  ? 123 ARG A CD    1 
ATOM   4249 N  NE    . ARG B 2 123 ? 106.682 153.043 102.715 1.00 68.13  ? 123 ARG A NE    1 
ATOM   4250 C  CZ    . ARG B 2 123 ? 105.545 153.607 103.099 1.00 69.30  ? 123 ARG A CZ    1 
ATOM   4251 N  NH1   . ARG B 2 123 ? 104.664 154.053 102.218 1.00 64.89  ? 123 ARG A NH1   1 
ATOM   4252 N  NH2   . ARG B 2 123 ? 105.286 153.727 104.397 1.00 63.06  ? 123 ARG A NH2   1 
ATOM   4253 N  N     . LYS B 2 124 ? 108.680 157.663 101.592 1.00 52.60  ? 124 LYS A N     1 
ATOM   4254 C  CA    . LYS B 2 124 ? 107.986 158.886 101.206 1.00 47.42  ? 124 LYS A CA    1 
ATOM   4255 C  C     . LYS B 2 124 ? 108.847 159.745 100.289 1.00 52.27  ? 124 LYS A C     1 
ATOM   4256 O  O     . LYS B 2 124 ? 108.354 160.294 99.298  1.00 60.19  ? 124 LYS A O     1 
ATOM   4257 C  CB    . LYS B 2 124 ? 107.587 159.669 102.453 1.00 51.61  ? 124 LYS A CB    1 
ATOM   4258 C  CG    . LYS B 2 124 ? 106.365 160.537 102.283 1.00 54.44  ? 124 LYS A CG    1 
ATOM   4259 C  CD    . LYS B 2 124 ? 105.880 161.063 103.621 1.00 57.90  ? 124 LYS A CD    1 
ATOM   4260 C  CE    . LYS B 2 124 ? 105.661 159.937 104.613 1.00 59.65  ? 124 LYS A CE    1 
ATOM   4261 N  NZ    . LYS B 2 124 ? 104.709 158.919 104.094 1.00 59.00  ? 124 LYS A NZ    1 
ATOM   4262 N  N     . LEU B 2 125 ? 110.137 159.876 100.604 1.00 50.41  ? 125 LEU A N     1 
ATOM   4263 C  CA    . LEU B 2 125 ? 111.023 160.689 99.776  1.00 47.12  ? 125 LEU A CA    1 
ATOM   4264 C  C     . LEU B 2 125 ? 111.221 160.076 98.397  1.00 50.31  ? 125 LEU A C     1 
ATOM   4265 O  O     . LEU B 2 125 ? 111.285 160.796 97.395  1.00 55.34  ? 125 LEU A O     1 
ATOM   4266 C  CB    . LEU B 2 125 ? 112.368 160.879 100.474 1.00 49.14  ? 125 LEU A CB    1 
ATOM   4267 C  CG    . LEU B 2 125 ? 112.546 162.160 101.284 1.00 52.12  ? 125 LEU A CG    1 
ATOM   4268 C  CD1   . LEU B 2 125 ? 113.878 162.159 101.996 1.00 53.46  ? 125 LEU A CD1   1 
ATOM   4269 C  CD2   . LEU B 2 125 ? 112.430 163.368 100.380 1.00 54.41  ? 125 LEU A CD2   1 
ATOM   4270 N  N     . ALA B 2 126 ? 111.328 158.749 98.324  1.00 50.84  ? 126 ALA A N     1 
ATOM   4271 C  CA    . ALA B 2 126 ? 111.550 158.094 97.041  1.00 50.23  ? 126 ALA A CA    1 
ATOM   4272 C  C     . ALA B 2 126 ? 110.325 158.170 96.143  1.00 46.93  ? 126 ALA A C     1 
ATOM   4273 O  O     . ALA B 2 126 ? 110.459 158.162 94.916  1.00 49.74  ? 126 ALA A O     1 
ATOM   4274 C  CB    . ALA B 2 126 ? 111.952 156.638 97.260  1.00 52.66  ? 126 ALA A CB    1 
ATOM   4275 N  N     . ASP B 2 127 ? 109.130 158.234 96.725  1.00 52.52  ? 127 ASP A N     1 
ATOM   4276 C  CA    . ASP B 2 127 ? 107.917 158.317 95.924  1.00 52.93  ? 127 ASP A CA    1 
ATOM   4277 C  C     . ASP B 2 127 ? 107.724 159.692 95.304  1.00 53.22  ? 127 ASP A C     1 
ATOM   4278 O  O     . ASP B 2 127 ? 106.983 159.817 94.325  1.00 57.66  ? 127 ASP A O     1 
ATOM   4279 C  CB    . ASP B 2 127 ? 106.701 157.960 96.779  1.00 59.13  ? 127 ASP A CB    1 
ATOM   4280 C  CG    . ASP B 2 127 ? 106.494 156.464 96.904  1.00 63.14  ? 127 ASP A CG    1 
ATOM   4281 O  OD1   . ASP B 2 127 ? 107.489 155.741 97.120  1.00 63.98  ? 127 ASP A OD1   1 
ATOM   4282 O  OD2   . ASP B 2 127 ? 105.336 156.010 96.794  1.00 63.42  ? 127 ASP A OD2   1 
ATOM   4283 N  N     . GLN B 2 128 ? 108.367 160.721 95.848  1.00 57.28  ? 128 GLN A N     1 
ATOM   4284 C  CA    . GLN B 2 128 ? 108.232 162.087 95.366  1.00 57.49  ? 128 GLN A CA    1 
ATOM   4285 C  C     . GLN B 2 128 ? 109.287 162.449 94.334  1.00 54.25  ? 128 GLN A C     1 
ATOM   4286 O  O     . GLN B 2 128 ? 109.383 163.615 93.944  1.00 56.17  ? 128 GLN A O     1 
ATOM   4287 C  CB    . GLN B 2 128 ? 108.299 163.065 96.540  1.00 56.70  ? 128 GLN A CB    1 
ATOM   4288 C  CG    . GLN B 2 128 ? 107.181 164.093 96.554  1.00 61.73  ? 128 GLN A CG    1 
ATOM   4289 C  CD    . GLN B 2 128 ? 107.561 165.381 95.852  1.00 66.54  ? 128 GLN A CD    1 
ATOM   4290 O  OE1   . GLN B 2 128 ? 108.732 165.757 95.812  1.00 66.93  ? 128 GLN A OE1   1 
ATOM   4291 N  NE2   . GLN B 2 128 ? 106.569 166.065 95.292  1.00 60.95  ? 128 GLN A NE2   1 
ATOM   4292 N  N     . CYS B 2 129 ? 110.079 161.483 93.893  1.00 51.79  ? 129 CYS A N     1 
ATOM   4293 C  CA    . CYS B 2 129 ? 111.127 161.708 92.916  1.00 52.74  ? 129 CYS A CA    1 
ATOM   4294 C  C     . CYS B 2 129 ? 110.975 160.710 91.779  1.00 54.48  ? 129 CYS A C     1 
ATOM   4295 O  O     . CYS B 2 129 ? 110.696 159.531 92.010  1.00 58.77  ? 129 CYS A O     1 
ATOM   4296 C  CB    . CYS B 2 129 ? 112.507 161.592 93.567  1.00 55.44  ? 129 CYS A CB    1 
ATOM   4297 S  SG    . CYS B 2 129 ? 113.000 159.940 94.078  1.00 68.81  ? 129 CYS A SG    1 
ATOM   4298 N  N     . THR B 2 130 ? 111.145 161.191 90.548  1.00 55.48  ? 130 THR A N     1 
ATOM   4299 C  CA    . THR B 2 130 ? 110.921 160.340 89.380  1.00 55.25  ? 130 THR A CA    1 
ATOM   4300 C  C     . THR B 2 130 ? 112.144 159.483 89.063  1.00 56.12  ? 130 THR A C     1 
ATOM   4301 O  O     . THR B 2 130 ? 112.080 158.251 89.101  1.00 62.64  ? 130 THR A O     1 
ATOM   4302 C  CB    . THR B 2 130 ? 110.533 161.205 88.179  1.00 56.24  ? 130 THR A CB    1 
ATOM   4303 O  OG1   . THR B 2 130 ? 111.575 162.152 87.921  1.00 55.40  ? 130 THR A OG1   1 
ATOM   4304 C  CG2   . THR B 2 130 ? 109.243 161.949 88.462  1.00 56.58  ? 130 THR A CG2   1 
ATOM   4305 N  N     . GLY B 2 131 ? 113.265 160.122 88.741  1.00 52.31  ? 131 GLY A N     1 
ATOM   4306 C  CA    . GLY B 2 131 ? 114.470 159.405 88.369  1.00 54.29  ? 131 GLY A CA    1 
ATOM   4307 C  C     . GLY B 2 131 ? 115.509 159.228 89.456  1.00 54.67  ? 131 GLY A C     1 
ATOM   4308 O  O     . GLY B 2 131 ? 116.562 159.869 89.401  1.00 57.23  ? 131 GLY A O     1 
ATOM   4309 N  N     . LEU B 2 132 ? 115.244 158.381 90.446  1.00 52.15  ? 132 LEU A N     1 
ATOM   4310 C  CA    . LEU B 2 132 ? 116.201 158.183 91.526  1.00 52.65  ? 132 LEU A CA    1 
ATOM   4311 C  C     . LEU B 2 132 ? 117.506 157.611 90.986  1.00 54.08  ? 132 LEU A C     1 
ATOM   4312 O  O     . LEU B 2 132 ? 117.505 156.656 90.205  1.00 57.45  ? 132 LEU A O     1 
ATOM   4313 C  CB    . LEU B 2 132 ? 115.611 157.261 92.593  1.00 57.25  ? 132 LEU A CB    1 
ATOM   4314 C  CG    . LEU B 2 132 ? 116.364 157.154 93.919  1.00 55.36  ? 132 LEU A CG    1 
ATOM   4315 C  CD1   . LEU B 2 132 ? 116.754 158.528 94.412  1.00 56.42  ? 132 LEU A CD1   1 
ATOM   4316 C  CD2   . LEU B 2 132 ? 115.522 156.445 94.951  1.00 54.27  ? 132 LEU A CD2   1 
ATOM   4317 N  N     . GLN B 2 133 ? 118.622 158.196 91.413  1.00 50.96  ? 133 GLN A N     1 
ATOM   4318 C  CA    . GLN B 2 133 ? 119.939 157.818 90.921  1.00 49.11  ? 133 GLN A CA    1 
ATOM   4319 C  C     . GLN B 2 133 ? 120.764 157.035 91.929  1.00 54.06  ? 133 GLN A C     1 
ATOM   4320 O  O     . GLN B 2 133 ? 121.649 156.277 91.525  1.00 58.09  ? 133 GLN A O     1 
ATOM   4321 C  CB    . GLN B 2 133 ? 120.725 159.062 90.504  1.00 51.97  ? 133 GLN A CB    1 
ATOM   4322 C  CG    . GLN B 2 133 ? 120.194 159.737 89.262  1.00 57.75  ? 133 GLN A CG    1 
ATOM   4323 C  CD    . GLN B 2 133 ? 120.820 159.201 87.998  1.00 60.49  ? 133 GLN A CD    1 
ATOM   4324 O  OE1   . GLN B 2 133 ? 122.035 159.031 87.917  1.00 60.53  ? 133 GLN A OE1   1 
ATOM   4325 N  NE2   . GLN B 2 133 ? 119.991 158.931 86.998  1.00 60.48  ? 133 GLN A NE2   1 
ATOM   4326 N  N     . GLY B 2 134 ? 120.517 157.207 93.217  1.00 48.52  ? 134 GLY A N     1 
ATOM   4327 C  CA    . GLY B 2 134 ? 121.296 156.505 94.213  1.00 51.06  ? 134 GLY A CA    1 
ATOM   4328 C  C     . GLY B 2 134 ? 121.126 157.138 95.574  1.00 52.14  ? 134 GLY A C     1 
ATOM   4329 O  O     . GLY B 2 134 ? 120.385 158.107 95.752  1.00 57.11  ? 134 GLY A O     1 
ATOM   4330 N  N     . PHE B 2 135 ? 121.836 156.562 96.536  1.00 40.03  ? 135 PHE A N     1 
ATOM   4331 C  CA    . PHE B 2 135 ? 121.835 157.022 97.913  1.00 38.47  ? 135 PHE A CA    1 
ATOM   4332 C  C     . PHE B 2 135 ? 123.232 157.482 98.299  1.00 42.08  ? 135 PHE A C     1 
ATOM   4333 O  O     . PHE B 2 135 ? 124.233 156.970 97.793  1.00 54.26  ? 135 PHE A O     1 
ATOM   4334 C  CB    . PHE B 2 135 ? 121.386 155.920 98.869  1.00 40.99  ? 135 PHE A CB    1 
ATOM   4335 C  CG    . PHE B 2 135 ? 119.939 155.562 98.752  1.00 39.78  ? 135 PHE A CG    1 
ATOM   4336 C  CD1   . PHE B 2 135 ? 119.512 154.656 97.807  1.00 42.88  ? 135 PHE A CD1   1 
ATOM   4337 C  CD2   . PHE B 2 135 ? 119.008 156.114 99.605  1.00 43.35  ? 135 PHE A CD2   1 
ATOM   4338 C  CE1   . PHE B 2 135 ? 118.184 154.319 97.705  1.00 42.02  ? 135 PHE A CE1   1 
ATOM   4339 C  CE2   . PHE B 2 135 ? 117.681 155.782 99.504  1.00 45.42  ? 135 PHE A CE2   1 
ATOM   4340 C  CZ    . PHE B 2 135 ? 117.271 154.881 98.553  1.00 43.88  ? 135 PHE A CZ    1 
ATOM   4341 N  N     . LEU B 2 136 ? 123.289 158.452 99.202  1.00 30.46  ? 136 LEU A N     1 
ATOM   4342 C  CA    . LEU B 2 136 ? 124.545 158.979 99.726  1.00 30.39  ? 136 LEU A CA    1 
ATOM   4343 C  C     . LEU B 2 136 ? 124.470 158.867 101.245 1.00 42.80  ? 136 LEU A C     1 
ATOM   4344 O  O     . LEU B 2 136 ? 123.760 159.640 101.893 1.00 47.39  ? 136 LEU A O     1 
ATOM   4345 C  CB    . LEU B 2 136 ? 124.760 160.416 99.274  1.00 35.30  ? 136 LEU A CB    1 
ATOM   4346 C  CG    . LEU B 2 136 ? 124.663 160.657 97.770  1.00 39.71  ? 136 LEU A CG    1 
ATOM   4347 C  CD1   . LEU B 2 136 ? 124.769 162.130 97.470  1.00 41.13  ? 136 LEU A CD1   1 
ATOM   4348 C  CD2   . LEU B 2 136 ? 125.745 159.896 97.041  1.00 39.07  ? 136 LEU A CD2   1 
ATOM   4349 N  N     . VAL B 2 137 ? 125.192 157.906 101.813 1.00 43.44  ? 137 VAL A N     1 
ATOM   4350 C  CA    . VAL B 2 137 ? 125.110 157.585 103.233 1.00 32.03  ? 137 VAL A CA    1 
ATOM   4351 C  C     . VAL B 2 137 ? 126.381 158.066 103.920 1.00 36.47  ? 137 VAL A C     1 
ATOM   4352 O  O     . VAL B 2 137 ? 127.488 157.672 103.539 1.00 46.72  ? 137 VAL A O     1 
ATOM   4353 C  CB    . VAL B 2 137 ? 124.895 156.082 103.457 1.00 30.46  ? 137 VAL A CB    1 
ATOM   4354 C  CG1   . VAL B 2 137 ? 124.545 155.815 104.895 1.00 39.51  ? 137 VAL A CG1   1 
ATOM   4355 C  CG2   . VAL B 2 137 ? 123.800 155.580 102.558 1.00 35.93  ? 137 VAL A CG2   1 
ATOM   4356 N  N     . PHE B 2 138 ? 126.220 158.911 104.932 1.00 29.20  ? 138 PHE A N     1 
ATOM   4357 C  CA    . PHE B 2 138 ? 127.325 159.435 105.719 1.00 32.30  ? 138 PHE A CA    1 
ATOM   4358 C  C     . PHE B 2 138 ? 127.237 158.874 107.129 1.00 40.45  ? 138 PHE A C     1 
ATOM   4359 O  O     . PHE B 2 138 ? 126.212 159.035 107.798 1.00 46.01  ? 138 PHE A O     1 
ATOM   4360 C  CB    . PHE B 2 138 ? 127.291 160.963 105.769 1.00 39.82  ? 138 PHE A CB    1 
ATOM   4361 C  CG    . PHE B 2 138 ? 127.474 161.626 104.437 1.00 40.38  ? 138 PHE A CG    1 
ATOM   4362 C  CD1   . PHE B 2 138 ? 126.432 161.701 103.535 1.00 40.55  ? 138 PHE A CD1   1 
ATOM   4363 C  CD2   . PHE B 2 138 ? 128.681 162.198 104.098 1.00 39.50  ? 138 PHE A CD2   1 
ATOM   4364 C  CE1   . PHE B 2 138 ? 126.599 162.317 102.319 1.00 35.08  ? 138 PHE A CE1   1 
ATOM   4365 C  CE2   . PHE B 2 138 ? 128.849 162.810 102.885 1.00 42.81  ? 138 PHE A CE2   1 
ATOM   4366 C  CZ    . PHE B 2 138 ? 127.806 162.869 101.995 1.00 41.12  ? 138 PHE A CZ    1 
ATOM   4367 N  N     . HIS B 2 139 ? 128.304 158.229 107.581 1.00 35.92  ? 139 HIS A N     1 
ATOM   4368 C  CA    . HIS B 2 139 ? 128.328 157.647 108.915 1.00 34.24  ? 139 HIS A CA    1 
ATOM   4369 C  C     . HIS B 2 139 ? 129.774 157.562 109.383 1.00 42.93  ? 139 HIS A C     1 
ATOM   4370 O  O     . HIS B 2 139 ? 130.681 158.119 108.758 1.00 51.39  ? 139 HIS A O     1 
ATOM   4371 C  CB    . HIS B 2 139 ? 127.645 156.279 108.928 1.00 40.42  ? 139 HIS A CB    1 
ATOM   4372 C  CG    . HIS B 2 139 ? 128.359 155.241 108.128 1.00 43.00  ? 139 HIS A CG    1 
ATOM   4373 N  ND1   . HIS B 2 139 ? 128.119 155.044 106.787 1.00 49.33  ? 139 HIS A ND1   1 
ATOM   4374 C  CD2   . HIS B 2 139 ? 129.293 154.329 108.480 1.00 38.96  ? 139 HIS A CD2   1 
ATOM   4375 C  CE1   . HIS B 2 139 ? 128.881 154.061 106.346 1.00 49.17  ? 139 HIS A CE1   1 
ATOM   4376 N  NE2   . HIS B 2 139 ? 129.604 153.613 107.353 1.00 46.30  ? 139 HIS A NE2   1 
ATOM   4377 N  N     . SER B 2 140 ? 129.986 156.865 110.492 1.00 45.41  ? 140 SER A N     1 
ATOM   4378 C  CA    . SER B 2 140 ? 131.298 156.743 111.106 1.00 38.27  ? 140 SER A CA    1 
ATOM   4379 C  C     . SER B 2 140 ? 131.529 155.310 111.549 1.00 41.67  ? 140 SER A C     1 
ATOM   4380 O  O     . SER B 2 140 ? 130.759 154.774 112.351 1.00 53.01  ? 140 SER A O     1 
ATOM   4381 C  CB    . SER B 2 140 ? 131.428 157.678 112.306 1.00 46.68  ? 140 SER A CB    1 
ATOM   4382 O  OG    . SER B 2 140 ? 132.607 157.398 113.035 1.00 52.41  ? 140 SER A OG    1 
ATOM   4383 N  N     . PHE B 2 141 ? 132.584 154.693 111.028 1.00 46.73  ? 141 PHE A N     1 
ATOM   4384 C  CA    . PHE B 2 141 ? 133.051 153.430 111.577 1.00 48.23  ? 141 PHE A CA    1 
ATOM   4385 C  C     . PHE B 2 141 ? 133.606 153.668 112.972 1.00 56.87  ? 141 PHE A C     1 
ATOM   4386 O  O     . PHE B 2 141 ? 134.229 154.698 113.238 1.00 63.15  ? 141 PHE A O     1 
ATOM   4387 C  CB    . PHE B 2 141 ? 134.144 152.822 110.700 1.00 45.97  ? 141 PHE A CB    1 
ATOM   4388 C  CG    . PHE B 2 141 ? 133.643 152.164 109.455 1.00 49.85  ? 141 PHE A CG    1 
ATOM   4389 C  CD1   . PHE B 2 141 ? 132.329 152.287 109.058 1.00 56.71  ? 141 PHE A CD1   1 
ATOM   4390 C  CD2   . PHE B 2 141 ? 134.496 151.408 108.683 1.00 51.35  ? 141 PHE A CD2   1 
ATOM   4391 C  CE1   . PHE B 2 141 ? 131.886 151.668 107.910 1.00 52.43  ? 141 PHE A CE1   1 
ATOM   4392 C  CE2   . PHE B 2 141 ? 134.061 150.793 107.541 1.00 53.54  ? 141 PHE A CE2   1 
ATOM   4393 C  CZ    . PHE B 2 141 ? 132.756 150.923 107.151 1.00 51.36  ? 141 PHE A CZ    1 
ATOM   4394 N  N     . GLY B 2 142 ? 133.388 152.711 113.871 1.00 52.62  ? 142 GLY A N     1 
ATOM   4395 C  CA    . GLY B 2 142 ? 133.956 152.750 115.199 1.00 53.14  ? 142 GLY A CA    1 
ATOM   4396 C  C     . GLY B 2 142 ? 133.029 153.320 116.253 1.00 55.66  ? 142 GLY A C     1 
ATOM   4397 O  O     . GLY B 2 142 ? 133.333 153.225 117.448 1.00 65.51  ? 142 GLY A O     1 
ATOM   4398 N  N     . GLY B 2 143 ? 131.925 153.920 115.843 1.00 47.79  ? 143 GLY A N     1 
ATOM   4399 C  CA    . GLY B 2 143 ? 130.906 154.313 116.788 1.00 49.55  ? 143 GLY A CA    1 
ATOM   4400 C  C     . GLY B 2 143 ? 129.855 153.240 116.965 1.00 50.25  ? 143 GLY A C     1 
ATOM   4401 O  O     . GLY B 2 143 ? 129.890 152.179 116.350 1.00 59.57  ? 143 GLY A O     1 
ATOM   4402 N  N     . GLY B 2 144 ? 128.897 153.524 117.836 1.00 47.95  ? 144 GLY A N     1 
ATOM   4403 C  CA    . GLY B 2 144 ? 127.805 152.601 118.047 1.00 47.25  ? 144 GLY A CA    1 
ATOM   4404 C  C     . GLY B 2 144 ? 126.737 152.703 116.981 1.00 52.55  ? 144 GLY A C     1 
ATOM   4405 O  O     . GLY B 2 144 ? 126.467 151.735 116.266 1.00 52.55  ? 144 GLY A O     1 
ATOM   4406 N  N     . THR B 2 145 ? 126.124 153.882 116.867 1.00 56.39  ? 145 THR A N     1 
ATOM   4407 C  CA    . THR B 2 145 ? 125.069 154.085 115.881 1.00 47.77  ? 145 THR A CA    1 
ATOM   4408 C  C     . THR B 2 145 ? 125.616 154.011 114.463 1.00 49.46  ? 145 THR A C     1 
ATOM   4409 O  O     . THR B 2 145 ? 125.064 153.307 113.613 1.00 58.89  ? 145 THR A O     1 
ATOM   4410 C  CB    . THR B 2 145 ? 124.384 155.427 116.119 1.00 45.87  ? 145 THR A CB    1 
ATOM   4411 O  OG1   . THR B 2 145 ? 123.986 155.523 117.488 1.00 49.05  ? 145 THR A OG1   1 
ATOM   4412 C  CG2   . THR B 2 145 ? 123.158 155.560 115.249 1.00 51.97  ? 145 THR A CG2   1 
ATOM   4413 N  N     . GLY B 2 146 ? 126.718 154.712 114.196 1.00 47.61  ? 146 GLY A N     1 
ATOM   4414 C  CA    . GLY B 2 146 ? 127.265 154.765 112.854 1.00 49.57  ? 146 GLY A CA    1 
ATOM   4415 C  C     . GLY B 2 146 ? 127.728 153.430 112.312 1.00 55.45  ? 146 GLY A C     1 
ATOM   4416 O  O     . GLY B 2 146 ? 127.851 153.278 111.094 1.00 60.70  ? 146 GLY A O     1 
ATOM   4417 N  N     . SER B 2 147 ? 127.983 152.457 113.181 1.00 48.36  ? 147 SER A N     1 
ATOM   4418 C  CA    . SER B 2 147 ? 128.392 151.127 112.753 1.00 46.78  ? 147 SER A CA    1 
ATOM   4419 C  C     . SER B 2 147 ? 127.260 150.117 112.800 1.00 45.34  ? 147 SER A C     1 
ATOM   4420 O  O     . SER B 2 147 ? 127.180 149.245 111.933 1.00 56.70  ? 147 SER A O     1 
ATOM   4421 C  CB    . SER B 2 147 ? 129.544 150.619 113.621 1.00 48.73  ? 147 SER A CB    1 
ATOM   4422 O  OG    . SER B 2 147 ? 129.138 150.475 114.968 1.00 60.15  ? 147 SER A OG    1 
ATOM   4423 N  N     . GLY B 2 148 ? 126.385 150.208 113.793 1.00 42.85  ? 148 GLY A N     1 
ATOM   4424 C  CA    . GLY B 2 148 ? 125.329 149.234 113.940 1.00 48.10  ? 148 GLY A CA    1 
ATOM   4425 C  C     . GLY B 2 148 ? 124.056 149.609 113.220 1.00 54.53  ? 148 GLY A C     1 
ATOM   4426 O  O     . GLY B 2 148 ? 123.500 148.801 112.472 1.00 59.61  ? 148 GLY A O     1 
ATOM   4427 N  N     . PHE B 2 149 ? 123.575 150.832 113.443 1.00 51.02  ? 149 PHE A N     1 
ATOM   4428 C  CA    . PHE B 2 149 ? 122.351 151.262 112.783 1.00 45.35  ? 149 PHE A CA    1 
ATOM   4429 C  C     . PHE B 2 149 ? 122.540 151.377 111.279 1.00 52.49  ? 149 PHE A C     1 
ATOM   4430 O  O     . PHE B 2 149 ? 121.574 151.243 110.522 1.00 63.21  ? 149 PHE A O     1 
ATOM   4431 C  CB    . PHE B 2 149 ? 121.878 152.590 113.366 1.00 41.09  ? 149 PHE A CB    1 
ATOM   4432 C  CG    . PHE B 2 149 ? 120.476 152.934 112.999 1.00 44.13  ? 149 PHE A CG    1 
ATOM   4433 C  CD1   . PHE B 2 149 ? 119.417 152.395 113.694 1.00 53.02  ? 149 PHE A CD1   1 
ATOM   4434 C  CD2   . PHE B 2 149 ? 120.215 153.786 111.947 1.00 46.92  ? 149 PHE A CD2   1 
ATOM   4435 C  CE1   . PHE B 2 149 ? 118.126 152.703 113.349 1.00 53.96  ? 149 PHE A CE1   1 
ATOM   4436 C  CE2   . PHE B 2 149 ? 118.931 154.097 111.600 1.00 48.02  ? 149 PHE A CE2   1 
ATOM   4437 C  CZ    . PHE B 2 149 ? 117.882 153.558 112.302 1.00 52.14  ? 149 PHE A CZ    1 
ATOM   4438 N  N     . THR B 2 150 ? 123.769 151.620 110.830 1.00 48.13  ? 150 THR A N     1 
ATOM   4439 C  CA    . THR B 2 150 ? 124.031 151.658 109.398 1.00 42.60  ? 150 THR A CA    1 
ATOM   4440 C  C     . THR B 2 150 ? 123.954 150.266 108.787 1.00 48.13  ? 150 THR A C     1 
ATOM   4441 O  O     . THR B 2 150 ? 123.494 150.111 107.654 1.00 54.88  ? 150 THR A O     1 
ATOM   4442 C  CB    . THR B 2 150 ? 125.390 152.293 109.133 1.00 46.13  ? 150 THR A CB    1 
ATOM   4443 O  OG1   . THR B 2 150 ? 125.517 153.485 109.914 1.00 53.82  ? 150 THR A OG1   1 
ATOM   4444 C  CG2   . THR B 2 150 ? 125.527 152.652 107.673 1.00 46.51  ? 150 THR A CG2   1 
ATOM   4445 N  N     . SER B 2 151 ? 124.392 149.240 109.520 1.00 47.27  ? 151 SER A N     1 
ATOM   4446 C  CA    . SER B 2 151 ? 124.302 147.874 109.013 1.00 44.18  ? 151 SER A CA    1 
ATOM   4447 C  C     . SER B 2 151 ? 122.851 147.455 108.811 1.00 48.84  ? 151 SER A C     1 
ATOM   4448 O  O     . SER B 2 151 ? 122.480 146.930 107.753 1.00 62.32  ? 151 SER A O     1 
ATOM   4449 C  CB    . SER B 2 151 ? 125.006 146.917 109.968 1.00 50.26  ? 151 SER A CB    1 
ATOM   4450 O  OG    . SER B 2 151 ? 126.327 147.342 110.229 1.00 59.32  ? 151 SER A OG    1 
ATOM   4451 N  N     . LEU B 2 152 ? 122.014 147.690 109.821 1.00 42.29  ? 152 LEU A N     1 
ATOM   4452 C  CA    . LEU B 2 152 ? 120.600 147.352 109.723 1.00 47.39  ? 152 LEU A CA    1 
ATOM   4453 C  C     . LEU B 2 152 ? 119.922 148.134 108.605 1.00 52.00  ? 152 LEU A C     1 
ATOM   4454 O  O     . LEU B 2 152 ? 119.149 147.571 107.815 1.00 61.61  ? 152 LEU A O     1 
ATOM   4455 C  CB    . LEU B 2 152 ? 119.929 147.627 111.066 1.00 43.18  ? 152 LEU A CB    1 
ATOM   4456 C  CG    . LEU B 2 152 ? 118.461 147.288 111.268 1.00 51.93  ? 152 LEU A CG    1 
ATOM   4457 C  CD1   . LEU B 2 152 ? 118.231 145.797 111.120 1.00 55.34  ? 152 LEU A CD1   1 
ATOM   4458 C  CD2   . LEU B 2 152 ? 118.023 147.763 112.633 1.00 49.90  ? 152 LEU A CD2   1 
ATOM   4459 N  N     . LEU B 2 153 ? 120.212 149.431 108.516 1.00 45.23  ? 153 LEU A N     1 
ATOM   4460 C  CA    . LEU B 2 153 ? 119.602 150.261 107.486 1.00 46.57  ? 153 LEU A CA    1 
ATOM   4461 C  C     . LEU B 2 153 ? 120.022 149.807 106.098 1.00 48.74  ? 153 LEU A C     1 
ATOM   4462 O  O     . LEU B 2 153 ? 119.201 149.767 105.176 1.00 54.42  ? 153 LEU A O     1 
ATOM   4463 C  CB    . LEU B 2 153 ? 119.979 151.721 107.713 1.00 46.19  ? 153 LEU A CB    1 
ATOM   4464 C  CG    . LEU B 2 153 ? 119.227 152.769 106.905 1.00 48.10  ? 153 LEU A CG    1 
ATOM   4465 C  CD1   . LEU B 2 153 ? 117.753 152.703 107.217 1.00 49.71  ? 153 LEU A CD1   1 
ATOM   4466 C  CD2   . LEU B 2 153 ? 119.778 154.139 107.217 1.00 48.98  ? 153 LEU A CD2   1 
ATOM   4467 N  N     . MET B 2 154 ? 121.298 149.467 105.928 1.00 46.40  ? 154 MET A N     1 
ATOM   4468 C  CA    . MET B 2 154 ? 121.780 149.024 104.628 1.00 49.19  ? 154 MET A CA    1 
ATOM   4469 C  C     . MET B 2 154 ? 121.168 147.686 104.242 1.00 51.56  ? 154 MET A C     1 
ATOM   4470 O  O     . MET B 2 154 ? 120.821 147.472 103.077 1.00 59.51  ? 154 MET A O     1 
ATOM   4471 C  CB    . MET B 2 154 ? 123.304 148.947 104.635 1.00 51.14  ? 154 MET A CB    1 
ATOM   4472 C  CG    . MET B 2 154 ? 123.989 150.300 104.593 1.00 52.64  ? 154 MET A CG    1 
ATOM   4473 S  SD    . MET B 2 154 ? 123.989 151.063 102.971 1.00 57.23  ? 154 MET A SD    1 
ATOM   4474 C  CE    . MET B 2 154 ? 124.842 149.811 102.021 1.00 56.02  ? 154 MET A CE    1 
ATOM   4475 N  N     . GLU B 2 155 ? 121.034 146.781 105.206 1.00 49.80  ? 155 GLU A N     1 
ATOM   4476 C  CA    . GLU B 2 155 ? 120.405 145.460 104.969 1.00 49.60  ? 155 GLU A CA    1 
ATOM   4477 C  C     . GLU B 2 155 ? 118.979 145.636 104.469 1.00 55.79  ? 155 GLU A C     1 
ATOM   4478 O  O     . GLU B 2 155 ? 118.620 145.009 103.464 1.00 62.10  ? 155 GLU A O     1 
ATOM   4479 C  CB    . GLU B 2 155 ? 120.251 144.636 106.239 1.00 52.44  ? 155 GLU A CB    1 
ATOM   4480 C  CG    . GLU B 2 155 ? 121.544 143.984 106.714 1.00 60.54  ? 155 GLU A CG    1 
ATOM   4481 C  CD    . GLU B 2 155 ? 121.672 143.949 108.226 1.00 68.23  ? 155 GLU A CD    1 
ATOM   4482 O  OE1   . GLU B 2 155 ? 120.629 144.011 108.911 1.00 67.34  ? 155 GLU A OE1   1 
ATOM   4483 O  OE2   . GLU B 2 155 ? 122.815 143.868 108.722 1.00 66.80  ? 155 GLU A OE2   1 
ATOM   4484 N  N     . ARG B 2 156 ? 118.164 146.338 105.055 1.00 52.24  ? 156 ARG A N     1 
ATOM   4485 C  CA    . ARG B 2 156 ? 116.752 146.532 104.659 1.00 52.65  ? 156 ARG A CA    1 
ATOM   4486 C  C     . ARG B 2 156 ? 116.650 147.265 103.323 1.00 53.84  ? 156 ARG A C     1 
ATOM   4487 O  O     . ARG B 2 156 ? 115.823 146.844 102.501 1.00 59.97  ? 156 ARG A O     1 
ATOM   4488 C  CB    . ARG B 2 156 ? 116.072 147.294 105.801 1.00 52.43  ? 156 ARG A CB    1 
ATOM   4489 C  CG    . ARG B 2 156 ? 116.111 146.581 107.141 1.00 47.83  ? 156 ARG A CG    1 
ATOM   4490 C  CD    . ARG B 2 156 ? 114.791 145.907 107.390 1.00 47.96  ? 156 ARG A CD    1 
ATOM   4491 N  NE    . ARG B 2 156 ? 114.585 145.723 108.827 1.00 55.03  ? 156 ARG A NE    1 
ATOM   4492 C  CZ    . ARG B 2 156 ? 113.522 146.180 109.460 1.00 60.03  ? 156 ARG A CZ    1 
ATOM   4493 N  NH1   . ARG B 2 156 ? 112.444 146.502 108.771 1.00 55.45  ? 156 ARG A NH1   1 
ATOM   4494 N  NH2   . ARG B 2 156 ? 113.539 146.315 110.773 1.00 56.35  ? 156 ARG A NH2   1 
ATOM   4495 N  N     . LEU B 2 157 ? 117.434 148.427 103.174 1.00 51.18  ? 157 LEU A N     1 
ATOM   4496 C  CA    . LEU B 2 157 ? 117.433 149.115 101.859 1.00 53.00  ? 157 LEU A CA    1 
ATOM   4497 C  C     . LEU B 2 157 ? 117.866 148.164 100.732 1.00 54.93  ? 157 LEU A C     1 
ATOM   4498 O  O     . LEU B 2 157 ? 117.224 148.215 99.672  1.00 60.43  ? 157 LEU A O     1 
ATOM   4499 C  CB    . LEU B 2 157 ? 118.292 150.374 101.893 1.00 54.67  ? 157 LEU A CB    1 
ATOM   4500 C  CG    . LEU B 2 157 ? 117.795 151.527 102.767 1.00 57.39  ? 157 LEU A CG    1 
ATOM   4501 C  CD1   . LEU B 2 157 ? 118.755 152.693 102.657 1.00 56.24  ? 157 LEU A CD1   1 
ATOM   4502 C  CD2   . LEU B 2 157 ? 116.399 151.942 102.352 1.00 58.56  ? 157 LEU A CD2   1 
ATOM   4503 N  N     . SER B 2 158 ? 118.888 147.339 100.921 1.00 55.64  ? 158 SER A N     1 
ATOM   4504 C  CA    . SER B 2 158 ? 119.236 146.379 99.882  1.00 57.67  ? 158 SER A CA    1 
ATOM   4505 C  C     . SER B 2 158 ? 118.080 145.431 99.608  1.00 58.73  ? 158 SER A C     1 
ATOM   4506 O  O     . SER B 2 158 ? 117.834 145.060 98.455  1.00 62.01  ? 158 SER A O     1 
ATOM   4507 C  CB    . SER B 2 158 ? 120.487 145.601 100.282 1.00 60.80  ? 158 SER A CB    1 
ATOM   4508 O  OG    . SER B 2 158 ? 120.876 144.708 99.255  1.00 64.18  ? 158 SER A OG    1 
ATOM   4509 N  N     . VAL B 2 159 ? 117.361 145.021 100.653 1.00 60.17  ? 159 VAL A N     1 
ATOM   4510 C  CA    . VAL B 2 159 ? 116.202 144.161 100.436 1.00 59.79  ? 159 VAL A CA    1 
ATOM   4511 C  C     . VAL B 2 159 ? 115.104 144.912 99.689  1.00 57.54  ? 159 VAL A C     1 
ATOM   4512 O  O     . VAL B 2 159 ? 114.468 144.365 98.782  1.00 65.14  ? 159 VAL A O     1 
ATOM   4513 C  CB    . VAL B 2 159 ? 115.698 143.596 101.775 1.00 60.32  ? 159 VAL A CB    1 
ATOM   4514 C  CG1   . VAL B 2 159 ? 114.337 142.956 101.604 1.00 54.80  ? 159 VAL A CG1   1 
ATOM   4515 C  CG2   . VAL B 2 159 ? 116.692 142.593 102.329 1.00 59.81  ? 159 VAL A CG2   1 
ATOM   4516 N  N     . ASP B 2 160 ? 114.872 146.176 100.043 1.00 57.96  ? 160 ASP A N     1 
ATOM   4517 C  CA    . ASP B 2 160 ? 113.712 146.898 99.527  1.00 58.96  ? 160 ASP A CA    1 
ATOM   4518 C  C     . ASP B 2 160 ? 113.937 147.406 98.106  1.00 60.98  ? 160 ASP A C     1 
ATOM   4519 O  O     . ASP B 2 160 ? 113.223 147.015 97.177  1.00 65.77  ? 160 ASP A O     1 
ATOM   4520 C  CB    . ASP B 2 160 ? 113.365 148.060 100.460 1.00 62.12  ? 160 ASP A CB    1 
ATOM   4521 C  CG    . ASP B 2 160 ? 111.901 148.442 100.397 1.00 67.04  ? 160 ASP A CG    1 
ATOM   4522 O  OD1   . ASP B 2 160 ? 111.282 148.271 99.326  1.00 65.22  ? 160 ASP A OD1   1 
ATOM   4523 O  OD2   . ASP B 2 160 ? 111.365 148.914 101.422 1.00 69.73  ? 160 ASP A OD2   1 
ATOM   4524 N  N     . TYR B 2 161 ? 114.920 148.283 97.917  1.00 58.65  ? 161 TYR A N     1 
ATOM   4525 C  CA    . TYR B 2 161 ? 115.143 148.903 96.616  1.00 61.23  ? 161 TYR A CA    1 
ATOM   4526 C  C     . TYR B 2 161 ? 116.015 148.043 95.709  1.00 64.65  ? 161 TYR A C     1 
ATOM   4527 O  O     . TYR B 2 161 ? 115.655 147.794 94.555  1.00 66.80  ? 161 TYR A O     1 
ATOM   4528 C  CB    . TYR B 2 161 ? 115.753 150.293 96.802  1.00 57.24  ? 161 TYR A CB    1 
ATOM   4529 C  CG    . TYR B 2 161 ? 114.798 151.248 97.470  1.00 57.09  ? 161 TYR A CG    1 
ATOM   4530 C  CD1   . TYR B 2 161 ? 114.763 151.373 98.845  1.00 58.11  ? 161 TYR A CD1   1 
ATOM   4531 C  CD2   . TYR B 2 161 ? 113.905 151.995 96.725  1.00 57.95  ? 161 TYR A CD2   1 
ATOM   4532 C  CE1   . TYR B 2 161 ? 113.879 152.230 99.458  1.00 56.99  ? 161 TYR A CE1   1 
ATOM   4533 C  CE2   . TYR B 2 161 ? 113.020 152.853 97.329  1.00 57.99  ? 161 TYR A CE2   1 
ATOM   4534 C  CZ    . TYR B 2 161 ? 113.011 152.966 98.695  1.00 59.38  ? 161 TYR A CZ    1 
ATOM   4535 O  OH    . TYR B 2 161 ? 112.130 153.826 99.302  1.00 62.72  ? 161 TYR A OH    1 
ATOM   4536 N  N     . GLY B 2 162 ? 117.157 147.586 96.207  1.00 64.25  ? 162 GLY A N     1 
ATOM   4537 C  CA    . GLY B 2 162 ? 117.943 146.602 95.493  1.00 60.15  ? 162 GLY A CA    1 
ATOM   4538 C  C     . GLY B 2 162 ? 118.784 147.144 94.359  1.00 62.10  ? 162 GLY A C     1 
ATOM   4539 O  O     . GLY B 2 162 ? 120.008 147.234 94.479  1.00 68.07  ? 162 GLY A O     1 
ATOM   4540 N  N     . LYS B 2 163 ? 118.143 147.510 93.252  1.00 61.25  ? 163 LYS A N     1 
ATOM   4541 C  CA    . LYS B 2 163 ? 118.882 147.881 92.053  1.00 63.07  ? 163 LYS A CA    1 
ATOM   4542 C  C     . LYS B 2 163 ? 119.521 149.260 92.138  1.00 64.85  ? 163 LYS A C     1 
ATOM   4543 O  O     . LYS B 2 163 ? 120.460 149.535 91.386  1.00 68.50  ? 163 LYS A O     1 
ATOM   4544 C  CB    . LYS B 2 163 ? 117.962 147.812 90.834  1.00 65.58  ? 163 LYS A CB    1 
ATOM   4545 C  CG    . LYS B 2 163 ? 116.651 148.556 91.004  1.00 69.74  ? 163 LYS A CG    1 
ATOM   4546 C  CD    . LYS B 2 163 ? 115.789 148.447 89.756  1.00 68.70  ? 163 LYS A CD    1 
ATOM   4547 C  CE    . LYS B 2 163 ? 115.550 146.995 89.373  1.00 68.48  ? 163 LYS A CE    1 
ATOM   4548 N  NZ    . LYS B 2 163 ? 114.910 146.225 90.476  1.00 67.21  ? 163 LYS A NZ    1 
ATOM   4549 N  N     . LYS B 2 164 ? 119.047 150.128 93.025  1.00 61.55  ? 164 LYS A N     1 
ATOM   4550 C  CA    . LYS B 2 164 ? 119.618 151.461 93.138  1.00 59.62  ? 164 LYS A CA    1 
ATOM   4551 C  C     . LYS B 2 164 ? 121.009 151.400 93.756  1.00 61.36  ? 164 LYS A C     1 
ATOM   4552 O  O     . LYS B 2 164 ? 121.307 150.546 94.592  1.00 60.34  ? 164 LYS A O     1 
ATOM   4553 C  CB    . LYS B 2 164 ? 118.710 152.362 93.972  1.00 60.58  ? 164 LYS A CB    1 
ATOM   4554 C  CG    . LYS B 2 164 ? 117.370 152.663 93.325  1.00 61.07  ? 164 LYS A CG    1 
ATOM   4555 C  CD    . LYS B 2 164 ? 117.543 153.394 92.010  1.00 61.71  ? 164 LYS A CD    1 
ATOM   4556 C  CE    . LYS B 2 164 ? 116.206 153.786 91.422  1.00 62.15  ? 164 LYS A CE    1 
ATOM   4557 N  NZ    . LYS B 2 164 ? 115.342 152.597 91.205  1.00 63.72  ? 164 LYS A NZ    1 
ATOM   4558 N  N     . SER B 2 165 ? 121.867 152.320 93.329  1.00 50.64  ? 165 SER A N     1 
ATOM   4559 C  CA    . SER B 2 165 ? 123.234 152.365 93.822  1.00 45.17  ? 165 SER A CA    1 
ATOM   4560 C  C     . SER B 2 165 ? 123.288 152.932 95.235  1.00 53.65  ? 165 SER A C     1 
ATOM   4561 O  O     . SER B 2 165 ? 122.451 153.742 95.637  1.00 57.22  ? 165 SER A O     1 
ATOM   4562 C  CB    . SER B 2 165 ? 124.100 153.206 92.892  1.00 50.81  ? 165 SER A CB    1 
ATOM   4563 O  OG    . SER B 2 165 ? 125.412 153.340 93.404  1.00 62.84  ? 165 SER A OG    1 
ATOM   4564 N  N     . LYS B 2 166 ? 124.292 152.496 95.992  1.00 54.93  ? 166 LYS A N     1 
ATOM   4565 C  CA    . LYS B 2 166 ? 124.534 152.986 97.344  1.00 44.96  ? 166 LYS A CA    1 
ATOM   4566 C  C     . LYS B 2 166 ? 126.001 153.358 97.470  1.00 48.44  ? 166 LYS A C     1 
ATOM   4567 O  O     . LYS B 2 166 ? 126.876 152.501 97.310  1.00 57.10  ? 166 LYS A O     1 
ATOM   4568 C  CB    . LYS B 2 166 ? 124.156 151.939 98.391  1.00 46.09  ? 166 LYS A CB    1 
ATOM   4569 C  CG    . LYS B 2 166 ? 122.705 151.532 98.350  1.00 55.69  ? 166 LYS A CG    1 
ATOM   4570 C  CD    . LYS B 2 166 ? 122.449 150.310 99.202  1.00 57.26  ? 166 LYS A CD    1 
ATOM   4571 C  CE    . LYS B 2 166 ? 121.159 149.631 98.798  1.00 56.26  ? 166 LYS A CE    1 
ATOM   4572 N  NZ    . LYS B 2 166 ? 121.177 149.239 97.366  1.00 54.42  ? 166 LYS A NZ    1 
ATOM   4573 N  N     . LEU B 2 167 ? 126.270 154.627 97.756  1.00 36.74  ? 167 LEU A N     1 
ATOM   4574 C  CA    . LEU B 2 167 ? 127.623 155.123 97.954  1.00 36.36  ? 167 LEU A CA    1 
ATOM   4575 C  C     . LEU B 2 167 ? 127.794 155.530 99.409  1.00 46.61  ? 167 LEU A C     1 
ATOM   4576 O  O     . LEU B 2 167 ? 126.964 156.266 99.951  1.00 48.94  ? 167 LEU A O     1 
ATOM   4577 C  CB    . LEU B 2 167 ? 127.912 156.311 97.038  1.00 41.14  ? 167 LEU A CB    1 
ATOM   4578 C  CG    . LEU B 2 167 ? 127.502 156.195 95.574  1.00 50.15  ? 167 LEU A CG    1 
ATOM   4579 C  CD1   . LEU B 2 167 ? 127.962 157.418 94.815  1.00 48.90  ? 167 LEU A CD1   1 
ATOM   4580 C  CD2   . LEU B 2 167 ? 128.065 154.941 94.950  1.00 49.78  ? 167 LEU A CD2   1 
ATOM   4581 N  N     . GLU B 2 168 ? 128.866 155.059 100.036 1.00 53.36  ? 168 GLU A N     1 
ATOM   4582 C  CA    . GLU B 2 168 ? 129.093 155.259 101.459 1.00 43.13  ? 168 GLU A CA    1 
ATOM   4583 C  C     . GLU B 2 168 ? 130.315 156.138 101.675 1.00 49.11  ? 168 GLU A C     1 
ATOM   4584 O  O     . GLU B 2 168 ? 131.375 155.887 101.095 1.00 56.68  ? 168 GLU A O     1 
ATOM   4585 C  CB    . GLU B 2 168 ? 129.269 153.918 102.170 1.00 44.30  ? 168 GLU A CB    1 
ATOM   4586 C  CG    . GLU B 2 168 ? 127.966 153.217 102.478 1.00 55.35  ? 168 GLU A CG    1 
ATOM   4587 C  CD    . GLU B 2 168 ? 127.221 152.799 101.225 1.00 63.95  ? 168 GLU A CD    1 
ATOM   4588 O  OE1   . GLU B 2 168 ? 127.880 152.544 100.195 1.00 64.10  ? 168 GLU A OE1   1 
ATOM   4589 O  OE2   . GLU B 2 168 ? 125.976 152.745 101.261 1.00 62.76  ? 168 GLU A OE2   1 
ATOM   4590 N  N     . PHE B 2 169 ? 130.162 157.168 102.503 1.00 46.66  ? 169 PHE A N     1 
ATOM   4591 C  CA    . PHE B 2 169 ? 131.259 158.037 102.917 1.00 42.07  ? 169 PHE A CA    1 
ATOM   4592 C  C     . PHE B 2 169 ? 131.479 157.820 104.407 1.00 44.81  ? 169 PHE A C     1 
ATOM   4593 O  O     . PHE B 2 169 ? 130.597 158.118 105.216 1.00 53.76  ? 169 PHE A O     1 
ATOM   4594 C  CB    . PHE B 2 169 ? 130.953 159.500 102.615 1.00 44.43  ? 169 PHE A CB    1 
ATOM   4595 C  CG    . PHE B 2 169 ? 130.677 159.777 101.170 1.00 48.74  ? 169 PHE A CG    1 
ATOM   4596 C  CD1   . PHE B 2 169 ? 129.424 159.545 100.635 1.00 52.96  ? 169 PHE A CD1   1 
ATOM   4597 C  CD2   . PHE B 2 169 ? 131.661 160.284 100.348 1.00 50.89  ? 169 PHE A CD2   1 
ATOM   4598 C  CE1   . PHE B 2 169 ? 129.165 159.802 99.307  1.00 53.68  ? 169 PHE A CE1   1 
ATOM   4599 C  CE2   . PHE B 2 169 ? 131.403 160.541 99.022  1.00 52.37  ? 169 PHE A CE2   1 
ATOM   4600 C  CZ    . PHE B 2 169 ? 130.154 160.299 98.502  1.00 51.01  ? 169 PHE A CZ    1 
ATOM   4601 N  N     . SER B 2 170 ? 132.651 157.310 104.771 1.00 44.88  ? 170 SER A N     1 
ATOM   4602 C  CA    . SER B 2 170 ? 132.899 156.826 106.119 1.00 47.23  ? 170 SER A CA    1 
ATOM   4603 C  C     . SER B 2 170 ? 134.144 157.469 106.710 1.00 49.38  ? 170 SER A C     1 
ATOM   4604 O  O     . SER B 2 170 ? 135.024 157.951 105.995 1.00 59.03  ? 170 SER A O     1 
ATOM   4605 C  CB    . SER B 2 170 ? 133.057 155.303 106.134 1.00 53.36  ? 170 SER A CB    1 
ATOM   4606 O  OG    . SER B 2 170 ? 131.931 154.672 105.553 1.00 60.37  ? 170 SER A OG    1 
ATOM   4607 N  N     . ILE B 2 171 ? 134.194 157.473 108.036 1.00 41.80  ? 171 ILE A N     1 
ATOM   4608 C  CA    . ILE B 2 171 ? 135.363 157.890 108.797 1.00 39.69  ? 171 ILE A CA    1 
ATOM   4609 C  C     . ILE B 2 171 ? 135.982 156.631 109.383 1.00 45.79  ? 171 ILE A C     1 
ATOM   4610 O  O     . ILE B 2 171 ? 135.375 155.967 110.230 1.00 49.88  ? 171 ILE A O     1 
ATOM   4611 C  CB    . ILE B 2 171 ? 135.004 158.894 109.898 1.00 46.80  ? 171 ILE A CB    1 
ATOM   4612 C  CG1   . ILE B 2 171 ? 134.292 160.107 109.308 1.00 48.58  ? 171 ILE A CG1   1 
ATOM   4613 C  CG2   . ILE B 2 171 ? 136.244 159.324 110.644 1.00 52.31  ? 171 ILE A CG2   1 
ATOM   4614 C  CD1   . ILE B 2 171 ? 135.178 160.968 108.453 1.00 46.36  ? 171 ILE A CD1   1 
ATOM   4615 N  N     . TYR B 2 172 ? 137.127 156.316 108.959 1.00 47.40  ? 172 TYR A N     1 
ATOM   4616 C  CA    . TYR B 2 172 ? 137.844 155.127 109.378 1.00 48.48  ? 172 TYR A CA    1 
ATOM   4617 C  C     . TYR B 2 172 ? 138.796 155.450 110.524 1.00 55.51  ? 172 TYR A C     1 
ATOM   4618 O  O     . TYR B 2 172 ? 139.330 156.560 110.599 1.00 60.10  ? 172 TYR A O     1 
ATOM   4619 C  CB    . TYR B 2 172 ? 138.632 154.549 108.208 1.00 46.34  ? 172 TYR A CB    1 
ATOM   4620 C  CG    . TYR B 2 172 ? 138.807 153.054 108.257 1.00 47.34  ? 172 TYR A CG    1 
ATOM   4621 C  CD1   . TYR B 2 172 ? 137.715 152.211 108.255 1.00 53.03  ? 172 TYR A CD1   1 
ATOM   4622 C  CD2   . TYR B 2 172 ? 140.067 152.487 108.300 1.00 47.21  ? 172 TYR A CD2   1 
ATOM   4623 C  CE1   . TYR B 2 172 ? 137.871 150.848 108.300 1.00 54.27  ? 172 TYR A CE1   1 
ATOM   4624 C  CE2   . TYR B 2 172 ? 140.231 151.127 108.343 1.00 51.22  ? 172 TYR A CE2   1 
ATOM   4625 C  CZ    . TYR B 2 172 ? 139.129 150.312 108.342 1.00 54.78  ? 172 TYR A CZ    1 
ATOM   4626 O  OH    . TYR B 2 172 ? 139.281 148.949 108.388 1.00 58.36  ? 172 TYR A OH    1 
ATOM   4627 N  N     . PRO B 2 173 ? 139.018 154.502 111.431 1.00 46.88  ? 173 PRO A N     1 
ATOM   4628 C  CA    . PRO B 2 173 ? 139.963 154.738 112.526 1.00 35.92  ? 173 PRO A CA    1 
ATOM   4629 C  C     . PRO B 2 173 ? 141.363 155.026 112.008 1.00 47.17  ? 173 PRO A C     1 
ATOM   4630 O  O     . PRO B 2 173 ? 141.822 154.429 111.034 1.00 59.62  ? 173 PRO A O     1 
ATOM   4631 C  CB    . PRO B 2 173 ? 139.918 153.430 113.316 1.00 42.52  ? 173 PRO A CB    1 
ATOM   4632 C  CG    . PRO B 2 173 ? 138.614 152.831 112.982 1.00 46.74  ? 173 PRO A CG    1 
ATOM   4633 C  CD    . PRO B 2 173 ? 138.313 153.220 111.582 1.00 49.02  ? 173 PRO A CD    1 
ATOM   4634 N  N     . ALA B 2 174 ? 142.039 155.952 112.674 1.00 43.73  ? 174 ALA A N     1 
ATOM   4635 C  CA    . ALA B 2 174 ? 143.393 156.325 112.315 1.00 48.28  ? 174 ALA A CA    1 
ATOM   4636 C  C     . ALA B 2 174 ? 144.394 155.345 112.915 1.00 48.13  ? 174 ALA A C     1 
ATOM   4637 O  O     . ALA B 2 174 ? 144.102 154.676 113.908 1.00 52.50  ? 174 ALA A O     1 
ATOM   4638 C  CB    . ALA B 2 174 ? 143.687 157.742 112.792 1.00 49.55  ? 174 ALA A CB    1 
ATOM   4639 N  N     . PRO B 2 175 ? 145.582 155.226 112.315 1.00 47.44  ? 175 PRO A N     1 
ATOM   4640 C  CA    . PRO B 2 175 ? 146.579 154.294 112.864 1.00 52.34  ? 175 PRO A CA    1 
ATOM   4641 C  C     . PRO B 2 175 ? 146.981 154.593 114.297 1.00 58.65  ? 175 PRO A C     1 
ATOM   4642 O  O     . PRO B 2 175 ? 147.150 153.662 115.093 1.00 62.31  ? 175 PRO A O     1 
ATOM   4643 C  CB    . PRO B 2 175 ? 147.764 154.455 111.904 1.00 53.24  ? 175 PRO A CB    1 
ATOM   4644 C  CG    . PRO B 2 175 ? 147.175 154.974 110.656 1.00 54.97  ? 175 PRO A CG    1 
ATOM   4645 C  CD    . PRO B 2 175 ? 146.050 155.858 111.072 1.00 54.39  ? 175 PRO A CD    1 
ATOM   4646 N  N     . GLN B 2 176 ? 147.137 155.866 114.654 1.00 57.65  ? 176 GLN A N     1 
ATOM   4647 C  CA    . GLN B 2 176 ? 147.593 156.237 115.987 1.00 54.15  ? 176 GLN A CA    1 
ATOM   4648 C  C     . GLN B 2 176 ? 146.538 157.013 116.763 1.00 56.18  ? 176 GLN A C     1 
ATOM   4649 O  O     . GLN B 2 176 ? 146.179 156.611 117.872 1.00 58.21  ? 176 GLN A O     1 
ATOM   4650 C  CB    . GLN B 2 176 ? 148.890 157.046 115.880 1.00 56.78  ? 176 GLN A CB    1 
ATOM   4651 C  CG    . GLN B 2 176 ? 150.021 156.303 115.200 1.00 55.97  ? 176 GLN A CG    1 
ATOM   4652 C  CD    . GLN B 2 176 ? 151.319 157.077 115.223 1.00 62.91  ? 176 GLN A CD    1 
ATOM   4653 O  OE1   . GLN B 2 176 ? 151.654 157.720 116.217 1.00 64.11  ? 176 GLN A OE1   1 
ATOM   4654 N  NE2   . GLN B 2 176 ? 152.060 157.022 114.124 1.00 61.60  ? 176 GLN A NE2   1 
ATOM   4655 N  N     . VAL B 2 177 ? 146.028 158.110 116.210 1.00 56.02  ? 177 VAL A N     1 
ATOM   4656 C  CA    . VAL B 2 177 ? 145.027 158.909 116.901 1.00 55.30  ? 177 VAL A CA    1 
ATOM   4657 C  C     . VAL B 2 177 ? 143.717 158.138 116.964 1.00 59.90  ? 177 VAL A C     1 
ATOM   4658 O  O     . VAL B 2 177 ? 143.226 157.628 115.949 1.00 61.79  ? 177 VAL A O     1 
ATOM   4659 C  CB    . VAL B 2 177 ? 144.851 160.261 116.196 1.00 51.79  ? 177 VAL A CB    1 
ATOM   4660 C  CG1   . VAL B 2 177 ? 143.478 160.834 116.473 1.00 55.95  ? 177 VAL A CG1   1 
ATOM   4661 C  CG2   . VAL B 2 177 ? 145.930 161.226 116.642 1.00 54.59  ? 177 VAL A CG2   1 
ATOM   4662 N  N     . SER B 2 178 ? 143.146 158.042 118.160 1.00 57.73  ? 178 SER A N     1 
ATOM   4663 C  CA    . SER B 2 178 ? 141.868 157.377 118.341 1.00 56.43  ? 178 SER A CA    1 
ATOM   4664 C  C     . SER B 2 178 ? 141.135 158.039 119.495 1.00 59.45  ? 178 SER A C     1 
ATOM   4665 O  O     . SER B 2 178 ? 141.742 158.670 120.362 1.00 64.90  ? 178 SER A O     1 
ATOM   4666 C  CB    . SER B 2 178 ? 142.038 155.877 118.599 1.00 59.47  ? 178 SER A CB    1 
ATOM   4667 O  OG    . SER B 2 178 ? 140.781 155.240 118.738 1.00 66.48  ? 178 SER A OG    1 
ATOM   4668 N  N     . THR B 2 179 ? 139.815 157.890 119.494 1.00 52.50  ? 179 THR A N     1 
ATOM   4669 C  CA    . THR B 2 179 ? 138.962 158.481 120.514 1.00 53.27  ? 179 THR A CA    1 
ATOM   4670 C  C     . THR B 2 179 ? 138.428 157.456 121.501 1.00 56.20  ? 179 THR A C     1 
ATOM   4671 O  O     . THR B 2 179 ? 138.510 157.668 122.712 1.00 57.53  ? 179 THR A O     1 
ATOM   4672 C  CB    . THR B 2 179 ? 137.794 159.227 119.855 1.00 57.32  ? 179 THR A CB    1 
ATOM   4673 O  OG1   . THR B 2 179 ? 138.285 160.402 119.201 1.00 56.99  ? 179 THR A OG1   1 
ATOM   4674 C  CG2   . THR B 2 179 ? 136.761 159.629 120.892 1.00 55.61  ? 179 THR A CG2   1 
ATOM   4675 N  N     . ALA B 2 180 ? 137.890 156.344 121.020 1.00 54.04  ? 180 ALA A N     1 
ATOM   4676 C  CA    . ALA B 2 180 ? 137.297 155.334 121.880 1.00 50.31  ? 180 ALA A CA    1 
ATOM   4677 C  C     . ALA B 2 180 ? 138.265 154.182 122.116 1.00 51.09  ? 180 ALA A C     1 
ATOM   4678 O  O     . ALA B 2 180 ? 139.294 154.049 121.454 1.00 52.35  ? 180 ALA A O     1 
ATOM   4679 C  CB    . ALA B 2 180 ? 135.992 154.818 121.274 1.00 49.44  ? 180 ALA A CB    1 
ATOM   4680 N  N     . VAL B 2 181 ? 137.912 153.338 123.080 1.00 46.11  ? 181 VAL A N     1 
ATOM   4681 C  CA    . VAL B 2 181 ? 138.730 152.176 123.397 1.00 41.81  ? 181 VAL A CA    1 
ATOM   4682 C  C     . VAL B 2 181 ? 138.268 150.936 122.640 1.00 47.12  ? 181 VAL A C     1 
ATOM   4683 O  O     . VAL B 2 181 ? 139.073 150.038 122.379 1.00 50.72  ? 181 VAL A O     1 
ATOM   4684 C  CB    . VAL B 2 181 ? 138.724 151.927 124.913 1.00 43.38  ? 181 VAL A CB    1 
ATOM   4685 C  CG1   . VAL B 2 181 ? 139.908 151.082 125.318 1.00 45.68  ? 181 VAL A CG1   1 
ATOM   4686 C  CG2   . VAL B 2 181 ? 138.740 153.240 125.659 1.00 49.41  ? 181 VAL A CG2   1 
ATOM   4687 N  N     . VAL B 2 182 ? 136.993 150.870 122.277 1.00 53.59  ? 182 VAL A N     1 
ATOM   4688 C  CA    . VAL B 2 182 ? 136.418 149.694 121.647 1.00 49.22  ? 182 VAL A CA    1 
ATOM   4689 C  C     . VAL B 2 182 ? 136.221 149.901 120.144 1.00 54.06  ? 182 VAL A C     1 
ATOM   4690 O  O     . VAL B 2 182 ? 135.407 149.217 119.528 1.00 57.91  ? 182 VAL A O     1 
ATOM   4691 C  CB    . VAL B 2 182 ? 135.104 149.291 122.326 1.00 46.52  ? 182 VAL A CB    1 
ATOM   4692 C  CG1   . VAL B 2 182 ? 135.374 148.772 123.717 1.00 52.35  ? 182 VAL A CG1   1 
ATOM   4693 C  CG2   . VAL B 2 182 ? 134.164 150.472 122.379 1.00 45.54  ? 182 VAL A CG2   1 
ATOM   4694 N  N     . GLU B 2 183 ? 136.950 150.842 119.551 1.00 55.11  ? 183 GLU A N     1 
ATOM   4695 C  CA    . GLU B 2 183 ? 136.813 151.103 118.120 1.00 51.43  ? 183 GLU A CA    1 
ATOM   4696 C  C     . GLU B 2 183 ? 137.101 149.893 117.237 1.00 55.64  ? 183 GLU A C     1 
ATOM   4697 O  O     . GLU B 2 183 ? 136.351 149.689 116.266 1.00 60.93  ? 183 GLU A O     1 
ATOM   4698 C  CB    . GLU B 2 183 ? 137.717 152.279 117.732 1.00 51.54  ? 183 GLU A CB    1 
ATOM   4699 C  CG    . GLU B 2 183 ? 137.019 153.375 116.964 1.00 58.19  ? 183 GLU A CG    1 
ATOM   4700 C  CD    . GLU B 2 183 ? 137.896 154.591 116.770 1.00 64.47  ? 183 GLU A CD    1 
ATOM   4701 O  OE1   . GLU B 2 183 ? 139.115 154.490 117.014 1.00 67.13  ? 183 GLU A OE1   1 
ATOM   4702 O  OE2   . GLU B 2 183 ? 137.366 155.650 116.374 1.00 62.75  ? 183 GLU A OE2   1 
ATOM   4703 N  N     . PRO B 2 184 ? 138.146 149.086 117.475 1.00 41.51  ? 184 PRO A N     1 
ATOM   4704 C  CA    . PRO B 2 184 ? 138.405 147.958 116.567 1.00 41.87  ? 184 PRO A CA    1 
ATOM   4705 C  C     . PRO B 2 184 ? 137.244 146.993 116.414 1.00 44.19  ? 184 PRO A C     1 
ATOM   4706 O  O     . PRO B 2 184 ? 136.997 146.517 115.299 1.00 53.36  ? 184 PRO A O     1 
ATOM   4707 C  CB    . PRO B 2 184 ? 139.619 147.282 117.208 1.00 44.98  ? 184 PRO A CB    1 
ATOM   4708 C  CG    . PRO B 2 184 ? 140.310 148.371 117.898 1.00 44.94  ? 184 PRO A CG    1 
ATOM   4709 C  CD    . PRO B 2 184 ? 139.251 149.257 118.435 1.00 43.58  ? 184 PRO A CD    1 
ATOM   4710 N  N     . TYR B 2 185 ? 136.518 146.692 117.491 1.00 36.55  ? 185 TYR A N     1 
ATOM   4711 C  CA    . TYR B 2 185 ? 135.408 145.748 117.395 1.00 42.65  ? 185 TYR A CA    1 
ATOM   4712 C  C     . TYR B 2 185 ? 134.330 146.266 116.453 1.00 46.38  ? 185 TYR A C     1 
ATOM   4713 O  O     . TYR B 2 185 ? 133.903 145.569 115.519 1.00 56.86  ? 185 TYR A O     1 
ATOM   4714 C  CB    . TYR B 2 185 ? 134.816 145.491 118.781 1.00 45.27  ? 185 TYR A CB    1 
ATOM   4715 C  CG    . TYR B 2 185 ? 135.683 144.693 119.724 1.00 45.31  ? 185 TYR A CG    1 
ATOM   4716 C  CD1   . TYR B 2 185 ? 136.895 144.171 119.320 1.00 45.21  ? 185 TYR A CD1   1 
ATOM   4717 C  CD2   . TYR B 2 185 ? 135.276 144.454 121.022 1.00 45.26  ? 185 TYR A CD2   1 
ATOM   4718 C  CE1   . TYR B 2 185 ? 137.678 143.443 120.184 1.00 41.11  ? 185 TYR A CE1   1 
ATOM   4719 C  CE2   . TYR B 2 185 ? 136.051 143.730 121.888 1.00 41.41  ? 185 TYR A CE2   1 
ATOM   4720 C  CZ    . TYR B 2 185 ? 137.248 143.223 121.464 1.00 44.08  ? 185 TYR A CZ    1 
ATOM   4721 O  OH    . TYR B 2 185 ? 138.019 142.501 122.336 1.00 53.64  ? 185 TYR A OH    1 
ATOM   4722 N  N     . ASN B 2 186 ? 133.889 147.504 116.682 1.00 41.99  ? 186 ASN A N     1 
ATOM   4723 C  CA    . ASN B 2 186 ? 132.862 148.098 115.840 1.00 41.36  ? 186 ASN A CA    1 
ATOM   4724 C  C     . ASN B 2 186 ? 133.330 148.201 114.399 1.00 49.39  ? 186 ASN A C     1 
ATOM   4725 O  O     . ASN B 2 186 ? 132.563 147.920 113.470 1.00 57.34  ? 186 ASN A O     1 
ATOM   4726 C  CB    . ASN B 2 186 ? 132.475 149.475 116.376 1.00 40.45  ? 186 ASN A CB    1 
ATOM   4727 C  CG    . ASN B 2 186 ? 132.126 149.454 117.842 1.00 46.06  ? 186 ASN A CG    1 
ATOM   4728 O  OD1   . ASN B 2 186 ? 131.731 148.427 118.382 1.00 53.19  ? 186 ASN A OD1   1 
ATOM   4729 N  ND2   . ASN B 2 186 ? 132.251 150.598 118.493 1.00 46.41  ? 186 ASN A ND2   1 
ATOM   4730 N  N     . SER B 2 187 ? 134.589 148.590 114.190 1.00 48.26  ? 187 SER A N     1 
ATOM   4731 C  CA    . SER B 2 187 ? 135.097 148.738 112.832 1.00 44.49  ? 187 SER A CA    1 
ATOM   4732 C  C     . SER B 2 187 ? 135.125 147.405 112.099 1.00 44.66  ? 187 SER A C     1 
ATOM   4733 O  O     . SER B 2 187 ? 134.749 147.330 110.926 1.00 51.60  ? 187 SER A O     1 
ATOM   4734 C  CB    . SER B 2 187 ? 136.486 149.367 112.854 1.00 47.16  ? 187 SER A CB    1 
ATOM   4735 O  OG    . SER B 2 187 ? 137.393 148.560 113.581 1.00 58.02  ? 187 SER A OG    1 
ATOM   4736 N  N     . ILE B 2 188 ? 135.555 146.337 112.771 1.00 47.28  ? 188 ILE A N     1 
ATOM   4737 C  CA    . ILE B 2 188 ? 135.615 145.032 112.117 1.00 46.31  ? 188 ILE A CA    1 
ATOM   4738 C  C     . ILE B 2 188 ? 134.216 144.554 111.755 1.00 47.95  ? 188 ILE A C     1 
ATOM   4739 O  O     . ILE B 2 188 ? 133.968 144.086 110.634 1.00 59.61  ? 188 ILE A O     1 
ATOM   4740 C  CB    . ILE B 2 188 ? 136.350 144.016 113.008 1.00 46.84  ? 188 ILE A CB    1 
ATOM   4741 C  CG1   . ILE B 2 188 ? 137.859 144.183 112.870 1.00 51.56  ? 188 ILE A CG1   1 
ATOM   4742 C  CG2   . ILE B 2 188 ? 135.974 142.614 112.632 1.00 47.54  ? 188 ILE A CG2   1 
ATOM   4743 C  CD1   . ILE B 2 188 ? 138.362 143.978 111.472 1.00 52.70  ? 188 ILE A CD1   1 
ATOM   4744 N  N     . LEU B 2 189 ? 133.272 144.680 112.688 1.00 38.82  ? 189 LEU A N     1 
ATOM   4745 C  CA    . LEU B 2 189 ? 131.916 144.224 112.396 1.00 40.45  ? 189 LEU A CA    1 
ATOM   4746 C  C     . LEU B 2 189 ? 131.287 145.031 111.259 1.00 47.04  ? 189 LEU A C     1 
ATOM   4747 O  O     . LEU B 2 189 ? 130.682 144.465 110.336 1.00 45.84  ? 189 LEU A O     1 
ATOM   4748 C  CB    . LEU B 2 189 ? 131.067 144.292 113.661 1.00 43.99  ? 189 LEU A CB    1 
ATOM   4749 C  CG    . LEU B 2 189 ? 131.585 143.432 114.815 1.00 43.25  ? 189 LEU A CG    1 
ATOM   4750 C  CD1   . LEU B 2 189 ? 131.042 143.921 116.135 1.00 45.40  ? 189 LEU A CD1   1 
ATOM   4751 C  CD2   . LEU B 2 189 ? 131.215 141.987 114.606 1.00 48.54  ? 189 LEU A CD2   1 
ATOM   4752 N  N     . THR B 2 190 ? 131.460 146.354 111.272 1.00 52.06  ? 190 THR A N     1 
ATOM   4753 C  CA    . THR B 2 190 ? 130.838 147.157 110.228 1.00 45.43  ? 190 THR A CA    1 
ATOM   4754 C  C     . THR B 2 190 ? 131.516 146.964 108.879 1.00 49.95  ? 190 THR A C     1 
ATOM   4755 O  O     . THR B 2 190 ? 130.851 147.058 107.844 1.00 57.14  ? 190 THR A O     1 
ATOM   4756 C  CB    . THR B 2 190 ? 130.827 148.635 110.615 1.00 52.14  ? 190 THR A CB    1 
ATOM   4757 O  OG1   . THR B 2 190 ? 130.039 149.365 109.668 1.00 56.06  ? 190 THR A OG1   1 
ATOM   4758 C  CG2   . THR B 2 190 ? 132.226 149.211 110.639 1.00 55.60  ? 190 THR A CG2   1 
ATOM   4759 N  N     . THR B 2 191 ? 132.827 146.714 108.852 1.00 60.86  ? 191 THR A N     1 
ATOM   4760 C  CA    . THR B 2 191 ? 133.483 146.465 107.578 1.00 66.26  ? 191 THR A CA    1 
ATOM   4761 C  C     . THR B 2 191 ? 133.169 145.077 107.047 1.00 59.34  ? 191 THR A C     1 
ATOM   4762 O  O     . THR B 2 191 ? 133.311 144.839 105.843 1.00 63.51  ? 191 THR A O     1 
ATOM   4763 C  CB    . THR B 2 191 ? 134.999 146.663 107.699 1.00 66.07  ? 191 THR A CB    1 
ATOM   4764 O  OG1   . THR B 2 191 ? 135.567 146.818 106.392 1.00 66.90  ? 191 THR A OG1   1 
ATOM   4765 C  CG2   . THR B 2 191 ? 135.650 145.478 108.385 1.00 58.86  ? 191 THR A CG2   1 
ATOM   4766 N  N     . HIS B 2 192 ? 132.751 144.159 107.915 1.00 56.29  ? 192 HIS A N     1 
ATOM   4767 C  CA    . HIS B 2 192 ? 132.120 142.944 107.419 1.00 62.38  ? 192 HIS A CA    1 
ATOM   4768 C  C     . HIS B 2 192 ? 130.751 143.242 106.820 1.00 58.75  ? 192 HIS A C     1 
ATOM   4769 O  O     . HIS B 2 192 ? 130.354 142.611 105.837 1.00 50.77  ? 192 HIS A O     1 
ATOM   4770 C  CB    . HIS B 2 192 ? 132.004 141.916 108.545 1.00 67.40  ? 192 HIS A CB    1 
ATOM   4771 C  CG    . HIS B 2 192 ? 130.852 140.973 108.388 1.00 75.60  ? 192 HIS A CG    1 
ATOM   4772 N  ND1   . HIS B 2 192 ? 130.727 140.122 107.312 1.00 77.32  ? 192 HIS A ND1   1 
ATOM   4773 C  CD2   . HIS B 2 192 ? 129.770 140.750 109.172 1.00 70.41  ? 192 HIS A CD2   1 
ATOM   4774 C  CE1   . HIS B 2 192 ? 129.619 139.414 107.439 1.00 71.08  ? 192 HIS A CE1   1 
ATOM   4775 N  NE2   . HIS B 2 192 ? 129.020 139.776 108.559 1.00 71.85  ? 192 HIS A NE2   1 
ATOM   4776 N  N     . THR B 2 193 ? 130.012 144.188 107.402 1.00 69.17  ? 193 THR A N     1 
ATOM   4777 C  CA    . THR B 2 193 ? 128.679 144.487 106.873 1.00 71.11  ? 193 THR A CA    1 
ATOM   4778 C  C     . THR B 2 193 ? 128.709 145.286 105.569 1.00 60.29  ? 193 THR A C     1 
ATOM   4779 O  O     . THR B 2 193 ? 127.794 145.151 104.752 1.00 52.93  ? 193 THR A O     1 
ATOM   4780 C  CB    . THR B 2 193 ? 127.849 145.248 107.909 1.00 67.24  ? 193 THR A CB    1 
ATOM   4781 O  OG1   . THR B 2 193 ? 128.481 146.498 108.208 1.00 68.73  ? 193 THR A OG1   1 
ATOM   4782 C  CG2   . THR B 2 193 ? 127.700 144.432 109.185 1.00 62.52  ? 193 THR A CG2   1 
ATOM   4783 N  N     . THR B 2 194 ? 129.723 146.129 105.365 1.00 64.23  ? 194 THR A N     1 
ATOM   4784 C  CA    . THR B 2 194 ? 129.757 147.041 104.221 1.00 58.63  ? 194 THR A CA    1 
ATOM   4785 C  C     . THR B 2 194 ? 130.239 146.391 102.931 1.00 60.60  ? 194 THR A C     1 
ATOM   4786 O  O     . THR B 2 194 ? 130.170 147.029 101.877 1.00 59.04  ? 194 THR A O     1 
ATOM   4787 C  CB    . THR B 2 194 ? 130.653 148.245 104.518 1.00 58.92  ? 194 THR A CB    1 
ATOM   4788 O  OG1   . THR B 2 194 ? 130.294 149.329 103.656 1.00 61.48  ? 194 THR A OG1   1 
ATOM   4789 C  CG2   . THR B 2 194 ? 132.107 147.899 104.281 1.00 55.66  ? 194 THR A CG2   1 
ATOM   4790 N  N     . LEU B 2 195 ? 130.741 145.158 102.984 1.00 62.83  ? 195 LEU A N     1 
ATOM   4791 C  CA    . LEU B 2 195 ? 131.172 144.487 101.763 1.00 51.10  ? 195 LEU A CA    1 
ATOM   4792 C  C     . LEU B 2 195 ? 129.983 144.044 100.920 1.00 53.71  ? 195 LEU A C     1 
ATOM   4793 O  O     . LEU B 2 195 ? 129.972 144.236 99.701  1.00 55.62  ? 195 LEU A O     1 
ATOM   4794 C  CB    . LEU B 2 195 ? 132.044 143.286 102.115 1.00 48.51  ? 195 LEU A CB    1 
ATOM   4795 C  CG    . LEU B 2 195 ? 133.195 142.900 101.197 1.00 53.32  ? 195 LEU A CG    1 
ATOM   4796 C  CD1   . LEU B 2 195 ? 134.087 141.920 101.919 1.00 54.38  ? 195 LEU A CD1   1 
ATOM   4797 C  CD2   . LEU B 2 195 ? 132.687 142.300 99.905  1.00 57.85  ? 195 LEU A CD2   1 
ATOM   4798 N  N     . GLU B 2 196 ? 128.973 143.452 101.554 1.00 54.44  ? 196 GLU A N     1 
ATOM   4799 C  CA    . GLU B 2 196 ? 127.882 142.827 100.819 1.00 50.85  ? 196 GLU A CA    1 
ATOM   4800 C  C     . GLU B 2 196 ? 126.890 143.835 100.256 1.00 53.74  ? 196 GLU A C     1 
ATOM   4801 O  O     . GLU B 2 196 ? 126.390 143.644 99.144  1.00 59.49  ? 196 GLU A O     1 
ATOM   4802 C  CB    . GLU B 2 196 ? 127.149 141.836 101.726 1.00 56.08  ? 196 GLU A CB    1 
ATOM   4803 C  CG    . GLU B 2 196 ? 128.038 140.752 102.327 1.00 63.51  ? 196 GLU A CG    1 
ATOM   4804 C  CD    . GLU B 2 196 ? 127.659 140.400 103.761 1.00 66.57  ? 196 GLU A CD    1 
ATOM   4805 O  OE1   . GLU B 2 196 ? 127.810 141.260 104.656 1.00 60.24  ? 196 GLU A OE1   1 
ATOM   4806 O  OE2   . GLU B 2 196 ? 127.210 139.259 103.996 1.00 63.21  ? 196 GLU A OE2   1 
ATOM   4807 N  N     . HIS B 2 197 ? 126.588 144.905 100.992 1.00 52.61  ? 197 HIS A N     1 
ATOM   4808 C  CA    . HIS B 2 197 ? 125.464 145.765 100.655 1.00 52.27  ? 197 HIS A CA    1 
ATOM   4809 C  C     . HIS B 2 197 ? 125.844 147.069 99.973  1.00 53.18  ? 197 HIS A C     1 
ATOM   4810 O  O     . HIS B 2 197 ? 125.013 147.629 99.255  1.00 59.00  ? 197 HIS A O     1 
ATOM   4811 C  CB    . HIS B 2 197 ? 124.646 146.090 101.911 1.00 49.19  ? 197 HIS A CB    1 
ATOM   4812 C  CG    . HIS B 2 197 ? 124.129 144.879 102.621 1.00 52.93  ? 197 HIS A CG    1 
ATOM   4813 N  ND1   . HIS B 2 197 ? 123.251 143.995 102.035 1.00 53.24  ? 197 HIS A ND1   1 
ATOM   4814 C  CD2   . HIS B 2 197 ? 124.362 144.407 103.867 1.00 56.41  ? 197 HIS A CD2   1 
ATOM   4815 C  CE1   . HIS B 2 197 ? 122.968 143.029 102.888 1.00 56.05  ? 197 HIS A CE1   1 
ATOM   4816 N  NE2   . HIS B 2 197 ? 123.627 143.257 104.009 1.00 56.59  ? 197 HIS A NE2   1 
ATOM   4817 N  N     . SER B 2 198 ? 127.055 147.566 100.175 1.00 50.63  ? 198 SER A N     1 
ATOM   4818 C  CA    . SER B 2 198 ? 127.453 148.803 99.530  1.00 47.91  ? 198 SER A CA    1 
ATOM   4819 C  C     . SER B 2 198 ? 127.852 148.547 98.082  1.00 51.25  ? 198 SER A C     1 
ATOM   4820 O  O     . SER B 2 198 ? 128.193 147.430 97.690  1.00 57.85  ? 198 SER A O     1 
ATOM   4821 C  CB    . SER B 2 198 ? 128.608 149.454 100.284 1.00 56.00  ? 198 SER A CB    1 
ATOM   4822 O  OG    . SER B 2 198 ? 129.115 150.564 99.570  1.00 59.16  ? 198 SER A OG    1 
ATOM   4823 N  N     . ASP B 2 199 ? 127.806 149.610 97.282  1.00 50.43  ? 199 ASP A N     1 
ATOM   4824 C  CA    . ASP B 2 199 ? 128.258 149.557 95.901  1.00 51.40  ? 199 ASP A CA    1 
ATOM   4825 C  C     . ASP B 2 199 ? 129.556 150.309 95.658  1.00 53.02  ? 199 ASP A C     1 
ATOM   4826 O  O     . ASP B 2 199 ? 130.251 150.007 94.686  1.00 54.77  ? 199 ASP A O     1 
ATOM   4827 C  CB    . ASP B 2 199 ? 127.181 150.119 94.964  1.00 54.95  ? 199 ASP A CB    1 
ATOM   4828 C  CG    . ASP B 2 199 ? 126.064 149.131 94.706  1.00 62.03  ? 199 ASP A CG    1 
ATOM   4829 O  OD1   . ASP B 2 199 ? 126.131 148.005 95.242  1.00 61.79  ? 199 ASP A OD1   1 
ATOM   4830 O  OD2   . ASP B 2 199 ? 125.118 149.480 93.970  1.00 62.87  ? 199 ASP A OD2   1 
ATOM   4831 N  N     . CYS B 2 200 ? 129.895 151.272 96.508  1.00 51.24  ? 200 CYS A N     1 
ATOM   4832 C  CA    . CYS B 2 200 ? 131.150 152.007 96.392  1.00 43.87  ? 200 CYS A CA    1 
ATOM   4833 C  C     . CYS B 2 200 ? 131.401 152.703 97.717  1.00 49.75  ? 200 CYS A C     1 
ATOM   4834 O  O     . CYS B 2 200 ? 130.551 153.468 98.181  1.00 58.75  ? 200 CYS A O     1 
ATOM   4835 C  CB    . CYS B 2 200 ? 131.092 153.013 95.252  1.00 49.07  ? 200 CYS A CB    1 
ATOM   4836 S  SG    . CYS B 2 200 ? 132.673 153.755 94.829  1.00 66.59  ? 200 CYS A SG    1 
ATOM   4837 N  N     . ALA B 2 201 ? 132.551 152.439 98.326  1.00 44.86  ? 201 ALA A N     1 
ATOM   4838 C  CA    . ALA B 2 201 ? 132.860 152.910 99.667  1.00 42.35  ? 201 ALA A CA    1 
ATOM   4839 C  C     . ALA B 2 201 ? 134.057 153.844 99.636  1.00 40.74  ? 201 ALA A C     1 
ATOM   4840 O  O     . ALA B 2 201 ? 135.111 153.491 99.103  1.00 50.03  ? 201 ALA A O     1 
ATOM   4841 C  CB    . ALA B 2 201 ? 133.138 151.736 100.606 1.00 48.64  ? 201 ALA A CB    1 
ATOM   4842 N  N     . PHE B 2 202 ? 133.895 155.024 100.222 1.00 47.59  ? 202 PHE A N     1 
ATOM   4843 C  CA    . PHE B 2 202 ? 134.964 156.003 100.359 1.00 48.99  ? 202 PHE A CA    1 
ATOM   4844 C  C     . PHE B 2 202 ? 135.300 156.135 101.836 1.00 54.91  ? 202 PHE A C     1 
ATOM   4845 O  O     . PHE B 2 202 ? 134.414 156.408 102.652 1.00 63.10  ? 202 PHE A O     1 
ATOM   4846 C  CB    . PHE B 2 202 ? 134.547 157.354 99.784  1.00 46.60  ? 202 PHE A CB    1 
ATOM   4847 C  CG    . PHE B 2 202 ? 134.253 157.326 98.319  1.00 45.49  ? 202 PHE A CG    1 
ATOM   4848 C  CD1   . PHE B 2 202 ? 135.246 157.569 97.396  1.00 53.82  ? 202 PHE A CD1   1 
ATOM   4849 C  CD2   . PHE B 2 202 ? 132.978 157.060 97.863  1.00 46.71  ? 202 PHE A CD2   1 
ATOM   4850 C  CE1   . PHE B 2 202 ? 134.973 157.544 96.049  1.00 54.08  ? 202 PHE A CE1   1 
ATOM   4851 C  CE2   . PHE B 2 202 ? 132.703 157.035 96.518  1.00 50.04  ? 202 PHE A CE2   1 
ATOM   4852 C  CZ    . PHE B 2 202 ? 133.699 157.275 95.612  1.00 50.53  ? 202 PHE A CZ    1 
ATOM   4853 N  N     . MET B 2 203 ? 136.568 155.952 102.176 1.00 51.53  ? 203 MET A N     1 
ATOM   4854 C  CA    . MET B 2 203 ? 137.023 156.002 103.557 1.00 51.60  ? 203 MET A CA    1 
ATOM   4855 C  C     . MET B 2 203 ? 137.992 157.159 103.726 1.00 53.60  ? 203 MET A C     1 
ATOM   4856 O  O     . MET B 2 203 ? 138.932 157.303 102.940 1.00 62.77  ? 203 MET A O     1 
ATOM   4857 C  CB    . MET B 2 203 ? 137.689 154.685 103.956 1.00 56.35  ? 203 MET A CB    1 
ATOM   4858 C  CG    . MET B 2 203 ? 136.727 153.522 104.079 1.00 57.26  ? 203 MET A CG    1 
ATOM   4859 S  SD    . MET B 2 203 ? 137.541 151.926 103.968 1.00 66.53  ? 203 MET A SD    1 
ATOM   4860 C  CE    . MET B 2 203 ? 139.074 152.271 104.824 1.00 61.26  ? 203 MET A CE    1 
ATOM   4861 N  N     . VAL B 2 204 ? 137.761 157.986 104.742 1.00 45.06  ? 204 VAL A N     1 
ATOM   4862 C  CA    . VAL B 2 204 ? 138.664 159.077 105.078 1.00 45.92  ? 204 VAL A CA    1 
ATOM   4863 C  C     . VAL B 2 204 ? 138.930 159.049 106.574 1.00 48.13  ? 204 VAL A C     1 
ATOM   4864 O  O     . VAL B 2 204 ? 138.013 158.883 107.383 1.00 59.08  ? 204 VAL A O     1 
ATOM   4865 C  CB    . VAL B 2 204 ? 138.105 160.451 104.647 1.00 48.04  ? 204 VAL A CB    1 
ATOM   4866 C  CG1   . VAL B 2 204 ? 138.180 160.600 103.145 1.00 48.65  ? 204 VAL A CG1   1 
ATOM   4867 C  CG2   . VAL B 2 204 ? 136.682 160.621 105.115 1.00 50.23  ? 204 VAL A CG2   1 
ATOM   4868 N  N     . ASP B 2 205 ? 140.197 159.201 106.945 1.00 52.00  ? 205 ASP A N     1 
ATOM   4869 C  CA    . ASP B 2 205 ? 140.593 159.237 108.342 1.00 54.56  ? 205 ASP A CA    1 
ATOM   4870 C  C     . ASP B 2 205 ? 140.955 160.662 108.730 1.00 54.49  ? 205 ASP A C     1 
ATOM   4871 O  O     . ASP B 2 205 ? 141.370 161.465 107.890 1.00 61.62  ? 205 ASP A O     1 
ATOM   4872 C  CB    . ASP B 2 205 ? 141.766 158.291 108.630 1.00 58.95  ? 205 ASP A CB    1 
ATOM   4873 C  CG    . ASP B 2 205 ? 142.836 158.340 107.568 1.00 65.92  ? 205 ASP A CG    1 
ATOM   4874 O  OD1   . ASP B 2 205 ? 142.944 159.371 106.878 1.00 71.13  ? 205 ASP A OD1   1 
ATOM   4875 O  OD2   . ASP B 2 205 ? 143.576 157.345 107.423 1.00 65.65  ? 205 ASP A OD2   1 
ATOM   4876 N  N     . ASN B 2 206 ? 140.789 160.973 110.014 1.00 50.67  ? 206 ASN A N     1 
ATOM   4877 C  CA    . ASN B 2 206 ? 140.953 162.349 110.466 1.00 52.82  ? 206 ASN A CA    1 
ATOM   4878 C  C     . ASN B 2 206 ? 142.413 162.773 110.510 1.00 60.71  ? 206 ASN A C     1 
ATOM   4879 O  O     . ASN B 2 206 ? 142.711 163.964 110.364 1.00 69.18  ? 206 ASN A O     1 
ATOM   4880 C  CB    . ASN B 2 206 ? 140.316 162.529 111.840 1.00 52.32  ? 206 ASN A CB    1 
ATOM   4881 C  CG    . ASN B 2 206 ? 138.812 162.450 111.798 1.00 56.70  ? 206 ASN A CG    1 
ATOM   4882 O  OD1   . ASN B 2 206 ? 138.204 162.542 110.738 1.00 60.23  ? 206 ASN A OD1   1 
ATOM   4883 N  ND2   . ASN B 2 206 ? 138.200 162.289 112.958 1.00 56.28  ? 206 ASN A ND2   1 
ATOM   4884 N  N     . GLU B 2 207 ? 143.332 161.831 110.727 1.00 59.64  ? 207 GLU A N     1 
ATOM   4885 C  CA    . GLU B 2 207 ? 144.739 162.192 110.855 1.00 58.01  ? 207 GLU A CA    1 
ATOM   4886 C  C     . GLU B 2 207 ? 145.286 162.768 109.554 1.00 68.35  ? 207 GLU A C     1 
ATOM   4887 O  O     . GLU B 2 207 ? 146.039 163.753 109.564 1.00 72.22  ? 207 GLU A O     1 
ATOM   4888 C  CB    . GLU B 2 207 ? 145.544 160.972 111.293 1.00 61.24  ? 207 GLU A CB    1 
ATOM   4889 C  CG    . GLU B 2 207 ? 146.942 161.294 111.772 1.00 68.30  ? 207 GLU A CG    1 
ATOM   4890 C  CD    . GLU B 2 207 ? 147.587 160.131 112.494 1.00 71.94  ? 207 GLU A CD    1 
ATOM   4891 O  OE1   . GLU B 2 207 ? 146.928 159.080 112.633 1.00 70.13  ? 207 GLU A OE1   1 
ATOM   4892 O  OE2   . GLU B 2 207 ? 148.751 160.268 112.924 1.00 69.61  ? 207 GLU A OE2   1 
ATOM   4893 N  N     . ALA B 2 208 ? 144.906 162.175 108.423 1.00 57.87  ? 208 ALA A N     1 
ATOM   4894 C  CA    . ALA B 2 208 ? 145.348 162.693 107.136 1.00 54.16  ? 208 ALA A CA    1 
ATOM   4895 C  C     . ALA B 2 208 ? 144.824 164.100 106.894 1.00 57.58  ? 208 ALA A C     1 
ATOM   4896 O  O     . ALA B 2 208 ? 145.544 164.956 106.367 1.00 66.75  ? 208 ALA A O     1 
ATOM   4897 C  CB    . ALA B 2 208 ? 144.910 161.757 106.013 1.00 52.64  ? 208 ALA A CB    1 
ATOM   4898 N  N     . ILE B 2 209 ? 143.567 164.359 107.255 1.00 48.88  ? 209 ILE A N     1 
ATOM   4899 C  CA    . ILE B 2 209 ? 143.021 165.696 107.064 1.00 46.83  ? 209 ILE A CA    1 
ATOM   4900 C  C     . ILE B 2 209 ? 143.681 166.695 108.003 1.00 47.13  ? 209 ILE A C     1 
ATOM   4901 O  O     . ILE B 2 209 ? 143.873 167.857 107.634 1.00 58.21  ? 209 ILE A O     1 
ATOM   4902 C  CB    . ILE B 2 209 ? 141.492 165.689 107.217 1.00 47.95  ? 209 ILE A CB    1 
ATOM   4903 C  CG1   . ILE B 2 209 ? 140.891 164.541 106.412 1.00 49.99  ? 209 ILE A CG1   1 
ATOM   4904 C  CG2   . ILE B 2 209 ? 140.912 166.996 106.727 1.00 53.87  ? 209 ILE A CG2   1 
ATOM   4905 C  CD1   . ILE B 2 209 ? 139.393 164.567 106.345 1.00 54.69  ? 209 ILE A CD1   1 
ATOM   4906 N  N     . TYR B 2 210 ? 144.039 166.279 109.218 1.00 44.54  ? 210 TYR A N     1 
ATOM   4907 C  CA    . TYR B 2 210 ? 144.822 167.154 110.084 1.00 47.11  ? 210 TYR A CA    1 
ATOM   4908 C  C     . TYR B 2 210 ? 146.144 167.520 109.429 1.00 51.96  ? 210 TYR A C     1 
ATOM   4909 O  O     . TYR B 2 210 ? 146.561 168.684 109.454 1.00 56.76  ? 210 TYR A O     1 
ATOM   4910 C  CB    . TYR B 2 210 ? 145.088 166.483 111.427 1.00 48.73  ? 210 TYR A CB    1 
ATOM   4911 C  CG    . TYR B 2 210 ? 143.889 166.309 112.320 1.00 48.40  ? 210 TYR A CG    1 
ATOM   4912 C  CD1   . TYR B 2 210 ? 142.815 167.174 112.259 1.00 48.33  ? 210 TYR A CD1   1 
ATOM   4913 C  CD2   . TYR B 2 210 ? 143.838 165.269 113.232 1.00 54.24  ? 210 TYR A CD2   1 
ATOM   4914 C  CE1   . TYR B 2 210 ? 141.725 167.006 113.080 1.00 51.05  ? 210 TYR A CE1   1 
ATOM   4915 C  CE2   . TYR B 2 210 ? 142.755 165.095 114.052 1.00 53.03  ? 210 TYR A CE2   1 
ATOM   4916 C  CZ    . TYR B 2 210 ? 141.702 165.963 113.972 1.00 50.88  ? 210 TYR A CZ    1 
ATOM   4917 O  OH    . TYR B 2 210 ? 140.621 165.784 114.798 1.00 55.44  ? 210 TYR A OH    1 
ATOM   4918 N  N     . ASP B 2 211 ? 146.824 166.531 108.846 1.00 58.73  ? 211 ASP A N     1 
ATOM   4919 C  CA    . ASP B 2 211 ? 148.095 166.801 108.181 1.00 57.59  ? 211 ASP A CA    1 
ATOM   4920 C  C     . ASP B 2 211 ? 147.912 167.745 106.999 1.00 57.55  ? 211 ASP A C     1 
ATOM   4921 O  O     . ASP B 2 211 ? 148.728 168.650 106.784 1.00 66.70  ? 211 ASP A O     1 
ATOM   4922 C  CB    . ASP B 2 211 ? 148.735 165.492 107.729 1.00 63.24  ? 211 ASP A CB    1 
ATOM   4923 C  CG    . ASP B 2 211 ? 150.245 165.515 107.840 1.00 70.22  ? 211 ASP A CG    1 
ATOM   4924 O  OD1   . ASP B 2 211 ? 150.830 166.616 107.772 1.00 68.59  ? 211 ASP A OD1   1 
ATOM   4925 O  OD2   . ASP B 2 211 ? 150.849 164.432 107.993 1.00 68.82  ? 211 ASP A OD2   1 
ATOM   4926 N  N     . ILE B 2 212 ? 146.847 167.546 106.220 1.00 51.38  ? 212 ILE A N     1 
ATOM   4927 C  CA    . ILE B 2 212 ? 146.563 168.418 105.082 1.00 49.47  ? 212 ILE A CA    1 
ATOM   4928 C  C     . ILE B 2 212 ? 146.293 169.839 105.552 1.00 54.09  ? 212 ILE A C     1 
ATOM   4929 O  O     . ILE B 2 212 ? 146.777 170.808 104.958 1.00 61.39  ? 212 ILE A O     1 
ATOM   4930 C  CB    . ILE B 2 212 ? 145.382 167.863 104.267 1.00 55.18  ? 212 ILE A CB    1 
ATOM   4931 C  CG1   . ILE B 2 212 ? 145.808 166.625 103.485 1.00 55.38  ? 212 ILE A CG1   1 
ATOM   4932 C  CG2   . ILE B 2 212 ? 144.839 168.916 103.333 1.00 55.53  ? 212 ILE A CG2   1 
ATOM   4933 C  CD1   . ILE B 2 212 ? 144.672 165.950 102.770 1.00 56.26  ? 212 ILE A CD1   1 
ATOM   4934 N  N     . CYS B 2 213 ? 145.517 169.984 106.624 1.00 58.48  ? 213 CYS A N     1 
ATOM   4935 C  CA    . CYS B 2 213 ? 145.229 171.307 107.163 1.00 59.15  ? 213 CYS A CA    1 
ATOM   4936 C  C     . CYS B 2 213 ? 146.496 171.995 107.642 1.00 56.65  ? 213 CYS A C     1 
ATOM   4937 O  O     . CYS B 2 213 ? 146.692 173.190 107.398 1.00 61.36  ? 213 CYS A O     1 
ATOM   4938 C  CB    . CYS B 2 213 ? 144.217 171.199 108.300 1.00 62.20  ? 213 CYS A CB    1 
ATOM   4939 S  SG    . CYS B 2 213 ? 142.534 170.855 107.770 1.00 76.57  ? 213 CYS A SG    1 
ATOM   4940 N  N     . ARG B 2 214 ? 147.372 171.260 108.324 1.00 56.81  ? 214 ARG A N     1 
ATOM   4941 C  CA    . ARG B 2 214 ? 148.581 171.871 108.861 1.00 55.07  ? 214 ARG A CA    1 
ATOM   4942 C  C     . ARG B 2 214 ? 149.542 172.275 107.751 1.00 62.22  ? 214 ARG A C     1 
ATOM   4943 O  O     . ARG B 2 214 ? 150.044 173.404 107.735 1.00 66.19  ? 214 ARG A O     1 
ATOM   4944 C  CB    . ARG B 2 214 ? 149.261 170.916 109.837 1.00 58.24  ? 214 ARG A CB    1 
ATOM   4945 C  CG    . ARG B 2 214 ? 150.486 171.494 110.513 1.00 62.06  ? 214 ARG A CG    1 
ATOM   4946 C  CD    . ARG B 2 214 ? 151.516 170.415 110.797 1.00 65.29  ? 214 ARG A CD    1 
ATOM   4947 N  NE    . ARG B 2 214 ? 150.946 169.298 111.540 1.00 70.89  ? 214 ARG A NE    1 
ATOM   4948 C  CZ    . ARG B 2 214 ? 151.602 168.185 111.839 1.00 70.08  ? 214 ARG A CZ    1 
ATOM   4949 N  NH1   . ARG B 2 214 ? 152.860 168.004 111.470 1.00 68.85  ? 214 ARG A NH1   1 
ATOM   4950 N  NH2   . ARG B 2 214 ? 150.981 167.230 112.525 1.00 65.01  ? 214 ARG A NH2   1 
ATOM   4951 N  N     . ARG B 2 215 ? 149.815 171.368 106.812 1.00 65.69  ? 215 ARG A N     1 
ATOM   4952 C  CA    . ARG B 2 215 ? 150.824 171.653 105.796 1.00 62.21  ? 215 ARG A CA    1 
ATOM   4953 C  C     . ARG B 2 215 ? 150.343 172.683 104.783 1.00 59.31  ? 215 ARG A C     1 
ATOM   4954 O  O     . ARG B 2 215 ? 151.074 173.619 104.445 1.00 65.13  ? 215 ARG A O     1 
ATOM   4955 C  CB    . ARG B 2 215 ? 151.233 170.370 105.076 1.00 60.54  ? 215 ARG A CB    1 
ATOM   4956 C  CG    . ARG B 2 215 ? 151.997 169.388 105.927 1.00 63.05  ? 215 ARG A CG    1 
ATOM   4957 C  CD    . ARG B 2 215 ? 152.675 168.359 105.051 1.00 63.05  ? 215 ARG A CD    1 
ATOM   4958 N  NE    . ARG B 2 215 ? 151.904 168.115 103.839 1.00 65.10  ? 215 ARG A NE    1 
ATOM   4959 C  CZ    . ARG B 2 215 ? 150.929 167.223 103.739 1.00 67.79  ? 215 ARG A CZ    1 
ATOM   4960 N  NH1   . ARG B 2 215 ? 150.598 166.445 104.756 1.00 66.51  ? 215 ARG A NH1   1 
ATOM   4961 N  NH2   . ARG B 2 215 ? 150.267 167.112 102.591 1.00 68.43  ? 215 ARG A NH2   1 
ATOM   4962 N  N     . ASN B 2 216 ? 149.117 172.529 104.287 1.00 54.08  ? 216 ASN A N     1 
ATOM   4963 C  CA    . ASN B 2 216 ? 148.662 173.350 103.172 1.00 53.29  ? 216 ASN A CA    1 
ATOM   4964 C  C     . ASN B 2 216 ? 148.015 174.646 103.646 1.00 56.87  ? 216 ASN A C     1 
ATOM   4965 O  O     . ASN B 2 216 ? 148.455 175.741 103.281 1.00 63.81  ? 216 ASN A O     1 
ATOM   4966 C  CB    . ASN B 2 216 ? 147.694 172.552 102.302 1.00 57.00  ? 216 ASN A CB    1 
ATOM   4967 C  CG    . ASN B 2 216 ? 148.371 171.420 101.570 1.00 60.73  ? 216 ASN A CG    1 
ATOM   4968 O  OD1   . ASN B 2 216 ? 147.839 170.318 101.484 1.00 64.21  ? 216 ASN A OD1   1 
ATOM   4969 N  ND2   . ASN B 2 216 ? 149.555 171.686 101.037 1.00 60.55  ? 216 ASN A ND2   1 
ATOM   4970 N  N     . LEU B 2 217 ? 146.965 174.545 104.456 1.00 58.75  ? 217 LEU A N     1 
ATOM   4971 C  CA    . LEU B 2 217 ? 146.189 175.718 104.835 1.00 61.77  ? 217 LEU A CA    1 
ATOM   4972 C  C     . LEU B 2 217 ? 146.841 176.553 105.927 1.00 61.93  ? 217 LEU A C     1 
ATOM   4973 O  O     . LEU B 2 217 ? 146.382 177.670 106.179 1.00 61.00  ? 217 LEU A O     1 
ATOM   4974 C  CB    . LEU B 2 217 ? 144.794 175.297 105.286 1.00 60.31  ? 217 LEU A CB    1 
ATOM   4975 C  CG    . LEU B 2 217 ? 143.908 174.687 104.207 1.00 59.62  ? 217 LEU A CG    1 
ATOM   4976 C  CD1   . LEU B 2 217 ? 142.664 174.101 104.836 1.00 61.95  ? 217 LEU A CD1   1 
ATOM   4977 C  CD2   . LEU B 2 217 ? 143.544 175.737 103.183 1.00 61.53  ? 217 LEU A CD2   1 
ATOM   4978 N  N     . ASP B 2 218 ? 147.887 176.045 106.575 1.00 65.43  ? 218 ASP A N     1 
ATOM   4979 C  CA    . ASP B 2 218 ? 148.610 176.776 107.615 1.00 61.71  ? 218 ASP A CA    1 
ATOM   4980 C  C     . ASP B 2 218 ? 147.693 177.168 108.772 1.00 67.65  ? 218 ASP A C     1 
ATOM   4981 O  O     . ASP B 2 218 ? 147.656 178.320 109.205 1.00 70.00  ? 218 ASP A O     1 
ATOM   4982 C  CB    . ASP B 2 218 ? 149.317 178.002 107.037 1.00 65.55  ? 218 ASP A CB    1 
ATOM   4983 C  CG    . ASP B 2 218 ? 150.527 177.634 106.205 1.00 71.45  ? 218 ASP A CG    1 
ATOM   4984 O  OD1   . ASP B 2 218 ? 150.879 176.437 106.168 1.00 70.34  ? 218 ASP A OD1   1 
ATOM   4985 O  OD2   . ASP B 2 218 ? 151.126 178.540 105.588 1.00 70.72  ? 218 ASP A OD2   1 
ATOM   4986 N  N     . ILE B 2 219 ? 146.942 176.192 109.272 1.00 69.25  ? 219 ILE A N     1 
ATOM   4987 C  CA    . ILE B 2 219 ? 146.207 176.317 110.524 1.00 64.99  ? 219 ILE A CA    1 
ATOM   4988 C  C     . ILE B 2 219 ? 146.792 175.295 111.489 1.00 66.69  ? 219 ILE A C     1 
ATOM   4989 O  O     . ILE B 2 219 ? 146.885 174.105 111.163 1.00 70.82  ? 219 ILE A O     1 
ATOM   4990 C  CB    . ILE B 2 219 ? 144.692 176.126 110.333 1.00 64.92  ? 219 ILE A CB    1 
ATOM   4991 C  CG1   . ILE B 2 219 ? 144.374 174.777 109.692 1.00 66.00  ? 219 ILE A CG1   1 
ATOM   4992 C  CG2   . ILE B 2 219 ? 144.120 177.246 109.487 1.00 65.76  ? 219 ILE A CG2   1 
ATOM   4993 C  CD1   . ILE B 2 219 ? 143.010 174.714 109.044 1.00 66.73  ? 219 ILE A CD1   1 
ATOM   4994 N  N     . GLU B 2 220 ? 147.223 175.762 112.658 1.00 79.80  ? 220 GLU A N     1 
ATOM   4995 C  CA    . GLU B 2 220 ? 147.936 174.898 113.589 1.00 81.87  ? 220 GLU A CA    1 
ATOM   4996 C  C     . GLU B 2 220 ? 147.018 174.116 114.515 1.00 82.68  ? 220 GLU A C     1 
ATOM   4997 O  O     . GLU B 2 220 ? 147.405 173.040 114.979 1.00 84.61  ? 220 GLU A O     1 
ATOM   4998 C  CB    . GLU B 2 220 ? 148.917 175.721 114.427 1.00 81.31  ? 220 GLU A CB    1 
ATOM   4999 C  CG    . GLU B 2 220 ? 150.359 175.606 113.970 1.00 81.90  ? 220 GLU A CG    1 
ATOM   5000 C  CD    . GLU B 2 220 ? 150.949 174.239 114.243 1.00 85.85  ? 220 GLU A CD    1 
ATOM   5001 O  OE1   . GLU B 2 220 ? 150.473 173.559 115.176 1.00 86.13  ? 220 GLU A OE1   1 
ATOM   5002 O  OE2   . GLU B 2 220 ? 151.890 173.841 113.524 1.00 84.80  ? 220 GLU A OE2   1 
ATOM   5003 N  N     . ARG B 2 221 ? 145.780 174.785 114.733 1.00 69.52  ? 221 ARG A N     1 
ATOM   5004 C  CA    . ARG B 2 221 ? 144.842 174.178 115.695 1.00 68.62  ? 221 ARG A CA    1 
ATOM   5005 C  C     . ARG B 2 221 ? 143.497 173.981 114.993 1.00 66.67  ? 221 ARG A C     1 
ATOM   5006 O  O     . ARG B 2 221 ? 142.557 174.706 115.324 1.00 70.36  ? 221 ARG A O     1 
ATOM   5007 C  CB    . ARG B 2 221 ? 144.777 175.053 116.948 1.00 71.39  ? 221 ARG A CB    1 
ATOM   5008 C  CG    . ARG B 2 221 ? 146.101 175.564 117.490 1.00 73.13  ? 221 ARG A CG    1 
ATOM   5009 C  CD    . ARG B 2 221 ? 145.855 176.773 118.365 1.00 73.39  ? 221 ARG A CD    1 
ATOM   5010 N  NE    . ARG B 2 221 ? 146.751 176.760 119.523 1.00 70.50  ? 221 ARG A NE    1 
ATOM   5011 C  CZ    . ARG B 2 221 ? 148.071 176.734 119.432 1.00 72.66  ? 221 ARG A CZ    1 
ATOM   5012 N  NH1   . ARG B 2 221 ? 148.710 177.728 118.843 1.00 74.04  ? 221 ARG A NH1   1 
ATOM   5013 N  NH2   . ARG B 2 221 ? 148.746 175.714 119.930 1.00 72.86  ? 221 ARG A NH2   1 
ATOM   5014 N  N     . PRO B 2 222 ? 143.376 172.921 114.042 1.00 55.52  ? 222 PRO A N     1 
ATOM   5015 C  CA    . PRO B 2 222 ? 142.091 172.739 113.368 1.00 56.09  ? 222 PRO A CA    1 
ATOM   5016 C  C     . PRO B 2 222 ? 141.074 172.061 114.269 1.00 61.08  ? 222 PRO A C     1 
ATOM   5017 O  O     . PRO B 2 222 ? 141.398 171.493 115.313 1.00 66.84  ? 222 PRO A O     1 
ATOM   5018 C  CB    . PRO B 2 222 ? 142.440 171.847 112.172 1.00 60.78  ? 222 PRO A CB    1 
ATOM   5019 C  CG    . PRO B 2 222 ? 143.926 171.842 112.095 1.00 62.92  ? 222 PRO A CG    1 
ATOM   5020 C  CD    . PRO B 2 222 ? 144.404 172.037 113.483 1.00 59.94  ? 222 PRO A CD    1 
ATOM   5021 N  N     . THR B 2 223 ? 139.818 172.126 113.839 1.00 57.92  ? 223 THR A N     1 
ATOM   5022 C  CA    . THR B 2 223 ? 138.741 171.420 114.519 1.00 54.19  ? 223 THR A CA    1 
ATOM   5023 C  C     . THR B 2 223 ? 137.916 170.642 113.502 1.00 56.86  ? 223 THR A C     1 
ATOM   5024 O  O     . THR B 2 223 ? 138.309 170.530 112.337 1.00 62.18  ? 223 THR A O     1 
ATOM   5025 C  CB    . THR B 2 223 ? 137.863 172.395 115.305 1.00 56.20  ? 223 THR A CB    1 
ATOM   5026 O  OG1   . THR B 2 223 ? 136.760 171.688 115.882 1.00 62.46  ? 223 THR A OG1   1 
ATOM   5027 C  CG2   . THR B 2 223 ? 137.337 173.489 114.399 1.00 55.35  ? 223 THR A CG2   1 
ATOM   5028 N  N     . TYR B 2 224 ? 136.777 170.099 113.929 1.00 49.15  ? 224 TYR A N     1 
ATOM   5029 C  CA    . TYR B 2 224 ? 135.994 169.233 113.055 1.00 48.22  ? 224 TYR A CA    1 
ATOM   5030 C  C     . TYR B 2 224 ? 135.375 169.993 111.889 1.00 55.15  ? 224 TYR A C     1 
ATOM   5031 O  O     . TYR B 2 224 ? 135.090 169.395 110.842 1.00 63.64  ? 224 TYR A O     1 
ATOM   5032 C  CB    . TYR B 2 224 ? 134.911 168.530 113.864 1.00 47.27  ? 224 TYR A CB    1 
ATOM   5033 C  CG    . TYR B 2 224 ? 135.405 167.311 114.594 1.00 45.83  ? 224 TYR A CG    1 
ATOM   5034 C  CD1   . TYR B 2 224 ? 136.575 166.687 114.210 1.00 49.96  ? 224 TYR A CD1   1 
ATOM   5035 C  CD2   . TYR B 2 224 ? 134.704 166.782 115.661 1.00 53.78  ? 224 TYR A CD2   1 
ATOM   5036 C  CE1   . TYR B 2 224 ? 137.034 165.574 114.863 1.00 51.38  ? 224 TYR A CE1   1 
ATOM   5037 C  CE2   . TYR B 2 224 ? 135.157 165.668 116.322 1.00 55.56  ? 224 TYR A CE2   1 
ATOM   5038 C  CZ    . TYR B 2 224 ? 136.323 165.067 115.919 1.00 53.41  ? 224 TYR A CZ    1 
ATOM   5039 O  OH    . TYR B 2 224 ? 136.777 163.954 116.580 1.00 46.35  ? 224 TYR A OH    1 
ATOM   5040 N  N     . THR B 2 225 ? 135.164 171.300 112.044 1.00 54.51  ? 225 THR A N     1 
ATOM   5041 C  CA    . THR B 2 225 ? 134.501 172.073 110.999 1.00 53.26  ? 225 THR A CA    1 
ATOM   5042 C  C     . THR B 2 225 ? 135.318 172.097 109.712 1.00 56.17  ? 225 THR A C     1 
ATOM   5043 O  O     . THR B 2 225 ? 134.759 171.982 108.615 1.00 62.00  ? 225 THR A O     1 
ATOM   5044 C  CB    . THR B 2 225 ? 134.233 173.490 111.493 1.00 57.85  ? 225 THR A CB    1 
ATOM   5045 O  OG1   . THR B 2 225 ? 135.478 174.147 111.755 1.00 63.36  ? 225 THR A OG1   1 
ATOM   5046 C  CG2   . THR B 2 225 ? 133.407 173.453 112.761 1.00 54.96  ? 225 THR A CG2   1 
ATOM   5047 N  N     . ASN B 2 226 ? 136.638 172.245 109.822 1.00 56.08  ? 226 ASN A N     1 
ATOM   5048 C  CA    . ASN B 2 226 ? 137.480 172.275 108.630 1.00 58.81  ? 226 ASN A CA    1 
ATOM   5049 C  C     . ASN B 2 226 ? 137.444 170.939 107.896 1.00 63.87  ? 226 ASN A C     1 
ATOM   5050 O  O     . ASN B 2 226 ? 137.346 170.892 106.658 1.00 68.55  ? 226 ASN A O     1 
ATOM   5051 C  CB    . ASN B 2 226 ? 138.907 172.641 109.024 1.00 57.79  ? 226 ASN A CB    1 
ATOM   5052 C  CG    . ASN B 2 226 ? 138.958 173.649 110.152 1.00 59.43  ? 226 ASN A CG    1 
ATOM   5053 O  OD1   . ASN B 2 226 ? 139.621 173.430 111.162 1.00 66.10  ? 226 ASN A OD1   1 
ATOM   5054 N  ND2   . ASN B 2 226 ? 138.268 174.765 109.981 1.00 59.55  ? 226 ASN A ND2   1 
ATOM   5055 N  N     . LEU B 2 227 ? 137.514 169.842 108.650 1.00 49.33  ? 227 LEU A N     1 
ATOM   5056 C  CA    . LEU B 2 227 ? 137.401 168.516 108.062 1.00 48.81  ? 227 LEU A CA    1 
ATOM   5057 C  C     . LEU B 2 227 ? 136.079 168.360 107.325 1.00 53.33  ? 227 LEU A C     1 
ATOM   5058 O  O     . LEU B 2 227 ? 136.033 167.835 106.202 1.00 59.96  ? 227 LEU A O     1 
ATOM   5059 C  CB    . LEU B 2 227 ? 137.522 167.456 109.155 1.00 50.64  ? 227 LEU A CB    1 
ATOM   5060 C  CG    . LEU B 2 227 ? 138.872 167.069 109.758 1.00 52.89  ? 227 LEU A CG    1 
ATOM   5061 C  CD1   . LEU B 2 227 ? 139.599 168.243 110.372 1.00 52.66  ? 227 LEU A CD1   1 
ATOM   5062 C  CD2   . LEU B 2 227 ? 138.665 165.991 110.797 1.00 51.54  ? 227 LEU A CD2   1 
ATOM   5063 N  N     . ASN B 2 228 ? 134.990 168.814 107.946 1.00 42.36  ? 228 ASN A N     1 
ATOM   5064 C  CA    . ASN B 2 228 ? 133.684 168.672 107.320 1.00 43.13  ? 228 ASN A CA    1 
ATOM   5065 C  C     . ASN B 2 228 ? 133.580 169.522 106.064 1.00 51.37  ? 228 ASN A C     1 
ATOM   5066 O  O     . ASN B 2 228 ? 132.942 169.117 105.086 1.00 59.40  ? 228 ASN A O     1 
ATOM   5067 C  CB    . ASN B 2 228 ? 132.587 169.023 108.318 1.00 42.51  ? 228 ASN A CB    1 
ATOM   5068 C  CG    . ASN B 2 228 ? 132.629 168.150 109.550 1.00 48.77  ? 228 ASN A CG    1 
ATOM   5069 O  OD1   . ASN B 2 228 ? 133.443 167.243 109.649 1.00 50.91  ? 228 ASN A OD1   1 
ATOM   5070 N  ND2   . ASN B 2 228 ? 131.745 168.419 110.495 1.00 52.39  ? 228 ASN A ND2   1 
ATOM   5071 N  N     . ARG B 2 229 ? 134.213 170.696 106.062 1.00 45.17  ? 229 ARG A N     1 
ATOM   5072 C  CA    . ARG B 2 229 ? 134.217 171.523 104.860 1.00 44.76  ? 229 ARG A CA    1 
ATOM   5073 C  C     . ARG B 2 229 ? 134.940 170.827 103.711 1.00 49.59  ? 229 ARG A C     1 
ATOM   5074 O  O     . ARG B 2 229 ? 134.462 170.836 102.567 1.00 53.48  ? 229 ARG A O     1 
ATOM   5075 C  CB    . ARG B 2 229 ? 134.853 172.876 105.159 1.00 47.86  ? 229 ARG A CB    1 
ATOM   5076 C  CG    . ARG B 2 229 ? 134.049 173.737 106.112 1.00 45.25  ? 229 ARG A CG    1 
ATOM   5077 C  CD    . ARG B 2 229 ? 134.562 175.157 106.117 1.00 51.30  ? 229 ARG A CD    1 
ATOM   5078 N  NE    . ARG B 2 229 ? 134.182 175.880 107.323 1.00 52.80  ? 229 ARG A NE    1 
ATOM   5079 C  CZ    . ARG B 2 229 ? 133.015 176.482 107.500 1.00 54.66  ? 229 ARG A CZ    1 
ATOM   5080 N  NH1   . ARG B 2 229 ? 132.078 176.460 106.568 1.00 53.09  ? 229 ARG A NH1   1 
ATOM   5081 N  NH2   . ARG B 2 229 ? 132.783 177.124 108.640 1.00 52.89  ? 229 ARG A NH2   1 
ATOM   5082 N  N     . LEU B 2 230 ? 136.084 170.201 103.997 1.00 44.24  ? 230 LEU A N     1 
ATOM   5083 C  CA    . LEU B 2 230 ? 136.794 169.468 102.949 1.00 43.77  ? 230 LEU A CA    1 
ATOM   5084 C  C     . LEU B 2 230 ? 135.962 168.304 102.411 1.00 46.85  ? 230 LEU A C     1 
ATOM   5085 O  O     . LEU B 2 230 ? 135.890 168.083 101.189 1.00 56.59  ? 230 LEU A O     1 
ATOM   5086 C  CB    . LEU B 2 230 ? 138.132 168.970 103.484 1.00 48.89  ? 230 LEU A CB    1 
ATOM   5087 C  CG    . LEU B 2 230 ? 139.370 169.732 103.015 1.00 50.86  ? 230 LEU A CG    1 
ATOM   5088 C  CD1   . LEU B 2 230 ? 140.572 169.348 103.849 1.00 53.82  ? 230 LEU A CD1   1 
ATOM   5089 C  CD2   . LEU B 2 230 ? 139.632 169.456 101.548 1.00 51.93  ? 230 LEU A CD2   1 
ATOM   5090 N  N     . ILE B 2 231 ? 135.318 167.554 103.304 1.00 40.49  ? 231 ILE A N     1 
ATOM   5091 C  CA    . ILE B 2 231 ? 134.519 166.415 102.858 1.00 43.64  ? 231 ILE A CA    1 
ATOM   5092 C  C     . ILE B 2 231 ? 133.338 166.885 102.014 1.00 43.93  ? 231 ILE A C     1 
ATOM   5093 O  O     . ILE B 2 231 ? 132.980 166.258 101.003 1.00 55.69  ? 231 ILE A O     1 
ATOM   5094 C  CB    . ILE B 2 231 ? 134.070 165.575 104.067 1.00 47.65  ? 231 ILE A CB    1 
ATOM   5095 C  CG1   . ILE B 2 231 ? 135.293 165.017 104.794 1.00 47.80  ? 231 ILE A CG1   1 
ATOM   5096 C  CG2   . ILE B 2 231 ? 133.161 164.451 103.629 1.00 47.98  ? 231 ILE A CG2   1 
ATOM   5097 C  CD1   . ILE B 2 231 ? 134.977 163.975 105.821 1.00 48.11  ? 231 ILE A CD1   1 
ATOM   5098 N  N     . SER B 2 232 ? 132.725 168.004 102.405 1.00 41.01  ? 232 SER A N     1 
ATOM   5099 C  CA    . SER B 2 232 ? 131.639 168.565 101.613 1.00 49.24  ? 232 SER A CA    1 
ATOM   5100 C  C     . SER B 2 232 ? 132.122 168.972 100.229 1.00 48.69  ? 232 SER A C     1 
ATOM   5101 O  O     . SER B 2 232 ? 131.406 168.791 99.238  1.00 56.25  ? 232 SER A O     1 
ATOM   5102 C  CB    . SER B 2 232 ? 131.023 169.759 102.338 1.00 54.34  ? 232 SER A CB    1 
ATOM   5103 O  OG    . SER B 2 232 ? 131.926 170.849 102.385 1.00 57.04  ? 232 SER A OG    1 
ATOM   5104 N  N     . GLN B 2 233 ? 133.328 169.539 100.142 1.00 45.69  ? 233 GLN A N     1 
ATOM   5105 C  CA    . GLN B 2 233 ? 133.868 169.891 98.832  1.00 48.72  ? 233 GLN A CA    1 
ATOM   5106 C  C     . GLN B 2 233 ? 134.015 168.657 97.953  1.00 46.65  ? 233 GLN A C     1 
ATOM   5107 O  O     . GLN B 2 233 ? 133.690 168.692 96.759  1.00 50.38  ? 233 GLN A O     1 
ATOM   5108 C  CB    . GLN B 2 233 ? 135.210 170.604 98.979  1.00 45.40  ? 233 GLN A CB    1 
ATOM   5109 C  CG    . GLN B 2 233 ? 135.110 172.014 99.522  1.00 45.42  ? 233 GLN A CG    1 
ATOM   5110 C  CD    . GLN B 2 233 ? 134.461 172.977 98.553  1.00 49.69  ? 233 GLN A CD    1 
ATOM   5111 O  OE1   . GLN B 2 233 ? 134.306 172.682 97.371  1.00 51.10  ? 233 GLN A OE1   1 
ATOM   5112 N  NE2   . GLN B 2 233 ? 134.079 174.142 99.053  1.00 49.91  ? 233 GLN A NE2   1 
ATOM   5113 N  N     . ILE B 2 234 ? 134.487 167.550 98.527  1.00 43.76  ? 234 ILE A N     1 
ATOM   5114 C  CA    . ILE B 2 234 ? 134.645 166.327 97.735  1.00 38.14  ? 234 ILE A CA    1 
ATOM   5115 C  C     . ILE B 2 234 ? 133.292 165.837 97.219  1.00 42.51  ? 234 ILE A C     1 
ATOM   5116 O  O     . ILE B 2 234 ? 133.144 165.485 96.039  1.00 44.95  ? 234 ILE A O     1 
ATOM   5117 C  CB    . ILE B 2 234 ? 135.365 165.241 98.553  1.00 36.58  ? 234 ILE A CB    1 
ATOM   5118 C  CG1   . ILE B 2 234 ? 136.864 165.506 98.572  1.00 44.55  ? 234 ILE A CG1   1 
ATOM   5119 C  CG2   . ILE B 2 234 ? 135.101 163.879 97.968  1.00 41.77  ? 234 ILE A CG2   1 
ATOM   5120 C  CD1   . ILE B 2 234 ? 137.663 164.406 99.218  1.00 48.92  ? 234 ILE A CD1   1 
ATOM   5121 N  N     . VAL B 2 235 ? 132.279 165.821 98.089  1.00 47.63  ? 235 VAL A N     1 
ATOM   5122 C  CA    . VAL B 2 235 ? 130.966 165.326 97.664  1.00 44.39  ? 235 VAL A CA    1 
ATOM   5123 C  C     . VAL B 2 235 ? 130.367 166.231 96.590  1.00 41.80  ? 235 VAL A C     1 
ATOM   5124 O  O     . VAL B 2 235 ? 129.746 165.758 95.625  1.00 45.74  ? 235 VAL A O     1 
ATOM   5125 C  CB    . VAL B 2 235 ? 130.025 165.180 98.873  1.00 43.98  ? 235 VAL A CB    1 
ATOM   5126 C  CG1   . VAL B 2 235 ? 128.693 164.616 98.438  1.00 48.59  ? 235 VAL A CG1   1 
ATOM   5127 C  CG2   . VAL B 2 235 ? 130.652 164.289 99.922  1.00 46.30  ? 235 VAL A CG2   1 
ATOM   5128 N  N     . SER B 2 236 ? 130.534 167.545 96.742  1.00 42.87  ? 236 SER A N     1 
ATOM   5129 C  CA    . SER B 2 236 ? 130.028 168.470 95.735  1.00 41.27  ? 236 SER A CA    1 
ATOM   5130 C  C     . SER B 2 236 ? 130.723 168.260 94.398  1.00 47.01  ? 236 SER A C     1 
ATOM   5131 O  O     . SER B 2 236 ? 130.088 168.344 93.340  1.00 56.37  ? 236 SER A O     1 
ATOM   5132 C  CB    . SER B 2 236 ? 130.203 169.909 96.210  1.00 46.66  ? 236 SER A CB    1 
ATOM   5133 O  OG    . SER B 2 236 ? 129.794 170.822 95.210  1.00 51.09  ? 236 SER A OG    1 
ATOM   5134 N  N     . SER B 2 237 ? 132.029 167.999 94.422  1.00 43.43  ? 237 SER A N     1 
ATOM   5135 C  CA    . SER B 2 237 ? 132.730 167.706 93.179  1.00 34.96  ? 237 SER A CA    1 
ATOM   5136 C  C     . SER B 2 237 ? 132.200 166.430 92.541  1.00 43.78  ? 237 SER A C     1 
ATOM   5137 O  O     . SER B 2 237 ? 132.143 166.320 91.312  1.00 44.95  ? 237 SER A O     1 
ATOM   5138 C  CB    . SER B 2 237 ? 134.230 167.601 93.436  1.00 38.90  ? 237 SER A CB    1 
ATOM   5139 O  OG    . SER B 2 237 ? 134.938 167.388 92.231  1.00 54.53  ? 237 SER A OG    1 
ATOM   5140 N  N     . ILE B 2 238 ? 131.813 165.449 93.358  1.00 48.01  ? 238 ILE A N     1 
ATOM   5141 C  CA    . ILE B 2 238 ? 131.239 164.224 92.803  1.00 36.49  ? 238 ILE A CA    1 
ATOM   5142 C  C     . ILE B 2 238 ? 129.904 164.505 92.116  1.00 39.03  ? 238 ILE A C     1 
ATOM   5143 O  O     . ILE B 2 238 ? 129.633 163.986 91.028  1.00 46.45  ? 238 ILE A O     1 
ATOM   5144 C  CB    . ILE B 2 238 ? 131.099 163.146 93.891  1.00 38.03  ? 238 ILE A CB    1 
ATOM   5145 C  CG1   . ILE B 2 238 ? 132.463 162.553 94.225  1.00 46.10  ? 238 ILE A CG1   1 
ATOM   5146 C  CG2   . ILE B 2 238 ? 130.167 162.048 93.436  1.00 36.32  ? 238 ILE A CG2   1 
ATOM   5147 C  CD1   . ILE B 2 238 ? 132.394 161.362 95.144  1.00 47.98  ? 238 ILE A CD1   1 
ATOM   5148 N  N     . THR B 2 239 ? 129.049 165.316 92.734  1.00 39.98  ? 239 THR A N     1 
ATOM   5149 C  CA    . THR B 2 239 ? 127.694 165.507 92.213  1.00 36.94  ? 239 THR A CA    1 
ATOM   5150 C  C     . THR B 2 239 ? 127.556 166.682 91.240  1.00 40.00  ? 239 THR A C     1 
ATOM   5151 O  O     . THR B 2 239 ? 126.452 166.917 90.718  1.00 48.24  ? 239 THR A O     1 
ATOM   5152 C  CB    . THR B 2 239 ? 126.711 165.682 93.370  1.00 43.74  ? 239 THR A CB    1 
ATOM   5153 O  OG1   . THR B 2 239 ? 127.101 166.813 94.155  1.00 49.85  ? 239 THR A OG1   1 
ATOM   5154 C  CG2   . THR B 2 239 ? 126.719 164.453 94.264  1.00 49.84  ? 239 THR A CG2   1 
ATOM   5155 N  N     . ALA B 2 240 ? 128.638 167.418 90.981  1.00 38.87  ? 240 ALA A N     1 
ATOM   5156 C  CA    . ALA B 2 240 ? 128.558 168.550 90.065  1.00 41.26  ? 240 ALA A CA    1 
ATOM   5157 C  C     . ALA B 2 240 ? 128.046 168.133 88.696  1.00 38.22  ? 240 ALA A C     1 
ATOM   5158 O  O     . ALA B 2 240 ? 127.262 168.857 88.074  1.00 43.37  ? 240 ALA A O     1 
ATOM   5159 C  CB    . ALA B 2 240 ? 129.924 169.218 89.939  1.00 48.55  ? 240 ALA A CB    1 
ATOM   5160 N  N     . SER B 2 241 ? 128.477 166.972 88.208  1.00 41.56  ? 241 SER A N     1 
ATOM   5161 C  CA    . SER B 2 241 ? 128.076 166.536 86.877  1.00 40.43  ? 241 SER A CA    1 
ATOM   5162 C  C     . SER B 2 241 ? 126.566 166.391 86.774  1.00 41.05  ? 241 SER A C     1 
ATOM   5163 O  O     . SER B 2 241 ? 125.965 166.774 85.766  1.00 42.27  ? 241 SER A O     1 
ATOM   5164 C  CB    . SER B 2 241 ? 128.766 165.221 86.535  1.00 43.65  ? 241 SER A CB    1 
ATOM   5165 O  OG    . SER B 2 241 ? 128.325 164.727 85.286  1.00 49.86  ? 241 SER A OG    1 
ATOM   5166 N  N     . LEU B 2 242 ? 125.936 165.836 87.808  1.00 47.99  ? 242 LEU A N     1 
ATOM   5167 C  CA    . LEU B 2 242 ? 124.482 165.752 87.818  1.00 44.35  ? 242 LEU A CA    1 
ATOM   5168 C  C     . LEU B 2 242 ? 123.848 167.130 87.919  1.00 43.63  ? 242 LEU A C     1 
ATOM   5169 O  O     . LEU B 2 242 ? 122.842 167.404 87.256  1.00 49.90  ? 242 LEU A O     1 
ATOM   5170 C  CB    . LEU B 2 242 ? 124.007 164.875 88.971  1.00 41.56  ? 242 LEU A CB    1 
ATOM   5171 C  CG    . LEU B 2 242 ? 124.273 163.381 88.885  1.00 43.41  ? 242 LEU A CG    1 
ATOM   5172 C  CD1   . LEU B 2 242 ? 123.583 162.699 90.036  1.00 39.57  ? 242 LEU A CD1   1 
ATOM   5173 C  CD2   . LEU B 2 242 ? 123.787 162.823 87.563  1.00 50.07  ? 242 LEU A CD2   1 
ATOM   5174 N  N     . ARG B 2 243 ? 124.406 168.009 88.752  1.00 43.46  ? 243 ARG A N     1 
ATOM   5175 C  CA    . ARG B 2 243 ? 123.745 169.291 88.985  1.00 42.61  ? 243 ARG A CA    1 
ATOM   5176 C  C     . ARG B 2 243 ? 123.867 170.215 87.776  1.00 42.55  ? 243 ARG A C     1 
ATOM   5177 O  O     . ARG B 2 243 ? 122.861 170.619 87.185  1.00 46.34  ? 243 ARG A O     1 
ATOM   5178 C  CB    . ARG B 2 243 ? 124.313 169.952 90.240  1.00 46.94  ? 243 ARG A CB    1 
ATOM   5179 C  CG    . ARG B 2 243 ? 123.713 169.416 91.521  1.00 39.75  ? 243 ARG A CG    1 
ATOM   5180 C  CD    . ARG B 2 243 ? 124.308 170.086 92.733  1.00 41.21  ? 243 ARG A CD    1 
ATOM   5181 N  NE    . ARG B 2 243 ? 125.595 169.514 93.090  1.00 38.40  ? 243 ARG A NE    1 
ATOM   5182 C  CZ    . ARG B 2 243 ? 126.704 170.216 93.258  1.00 45.20  ? 243 ARG A CZ    1 
ATOM   5183 N  NH1   . ARG B 2 243 ? 126.712 171.530 93.138  1.00 50.13  ? 243 ARG A NH1   1 
ATOM   5184 N  NH2   . ARG B 2 243 ? 127.832 169.583 93.559  1.00 49.40  ? 243 ARG A NH2   1 
ATOM   5185 N  N     . PHE B 2 244 ? 125.088 170.561 87.393  1.00 40.42  ? 244 PHE A N     1 
ATOM   5186 C  CA    . PHE B 2 244 ? 125.341 171.539 86.349  1.00 40.00  ? 244 PHE A CA    1 
ATOM   5187 C  C     . PHE B 2 244 ? 125.711 170.849 85.038  1.00 46.74  ? 244 PHE A C     1 
ATOM   5188 O  O     . PHE B 2 244 ? 125.634 169.624 84.909  1.00 50.58  ? 244 PHE A O     1 
ATOM   5189 C  CB    . PHE B 2 244 ? 126.429 172.503 86.806  1.00 39.82  ? 244 PHE A CB    1 
ATOM   5190 C  CG    . PHE B 2 244 ? 126.154 173.123 88.131  1.00 35.50  ? 244 PHE A CG    1 
ATOM   5191 C  CD1   . PHE B 2 244 ? 125.198 174.105 88.260  1.00 42.08  ? 244 PHE A CD1   1 
ATOM   5192 C  CD2   . PHE B 2 244 ? 126.839 172.715 89.251  1.00 43.69  ? 244 PHE A CD2   1 
ATOM   5193 C  CE1   . PHE B 2 244 ? 124.937 174.676 89.479  1.00 46.69  ? 244 PHE A CE1   1 
ATOM   5194 C  CE2   . PHE B 2 244 ? 126.583 173.280 90.470  1.00 49.46  ? 244 PHE A CE2   1 
ATOM   5195 C  CZ    . PHE B 2 244 ? 125.629 174.262 90.585  1.00 49.23  ? 244 PHE A CZ    1 
ATOM   5196 N  N     . ASP B 2 245 ? 126.125 171.640 84.049  1.00 47.11  ? 245 ASP A N     1 
ATOM   5197 C  CA    . ASP B 2 245 ? 126.429 171.135 82.719  1.00 47.32  ? 245 ASP A CA    1 
ATOM   5198 C  C     . ASP B 2 245 ? 127.839 171.530 82.308  1.00 46.59  ? 245 ASP A C     1 
ATOM   5199 O  O     . ASP B 2 245 ? 128.383 172.533 82.771  1.00 48.62  ? 245 ASP A O     1 
ATOM   5200 C  CB    . ASP B 2 245 ? 125.438 171.656 81.675  1.00 52.50  ? 245 ASP A CB    1 
ATOM   5201 C  CG    . ASP B 2 245 ? 125.500 173.157 81.515  1.00 57.54  ? 245 ASP A CG    1 
ATOM   5202 O  OD1   . ASP B 2 245 ? 125.799 173.850 82.509  1.00 55.35  ? 245 ASP A OD1   1 
ATOM   5203 O  OD2   . ASP B 2 245 ? 125.250 173.647 80.394  1.00 55.97  ? 245 ASP A OD2   1 
ATOM   5204 N  N     . GLY B 2 246 ? 128.415 170.728 81.423  1.00 51.17  ? 246 GLY A N     1 
ATOM   5205 C  CA    . GLY B 2 246 ? 129.770 170.950 80.956  1.00 50.40  ? 246 GLY A CA    1 
ATOM   5206 C  C     . GLY B 2 246 ? 130.144 169.884 79.953  1.00 51.41  ? 246 GLY A C     1 
ATOM   5207 O  O     . GLY B 2 246 ? 129.313 169.071 79.536  1.00 55.67  ? 246 GLY A O     1 
ATOM   5208 N  N     . ALA B 2 247 ? 131.413 169.902 79.559  1.00 50.74  ? 247 ALA A N     1 
ATOM   5209 C  CA    . ALA B 2 247 ? 131.936 168.914 78.625  1.00 45.37  ? 247 ALA A CA    1 
ATOM   5210 C  C     . ALA B 2 247 ? 132.334 167.642 79.360  1.00 55.28  ? 247 ALA A C     1 
ATOM   5211 O  O     . ALA B 2 247 ? 133.014 167.700 80.387  1.00 65.30  ? 247 ALA A O     1 
ATOM   5212 C  CB    . ALA B 2 247 ? 133.138 169.478 77.874  1.00 43.99  ? 247 ALA A CB    1 
ATOM   5213 N  N     . LEU B 2 248 ? 131.927 166.491 78.825  1.00 50.13  ? 248 LEU A N     1 
ATOM   5214 C  CA    . LEU B 2 248 ? 132.261 165.182 79.387  1.00 49.49  ? 248 LEU A CA    1 
ATOM   5215 C  C     . LEU B 2 248 ? 131.768 165.055 80.832  1.00 53.58  ? 248 LEU A C     1 
ATOM   5216 O  O     . LEU B 2 248 ? 132.539 164.941 81.782  1.00 58.13  ? 248 LEU A O     1 
ATOM   5217 C  CB    . LEU B 2 248 ? 133.766 164.909 79.298  1.00 45.03  ? 248 LEU A CB    1 
ATOM   5218 C  CG    . LEU B 2 248 ? 134.371 164.831 77.904  1.00 51.21  ? 248 LEU A CG    1 
ATOM   5219 C  CD1   . LEU B 2 248 ? 135.862 164.616 78.000  1.00 52.51  ? 248 LEU A CD1   1 
ATOM   5220 C  CD2   . LEU B 2 248 ? 133.717 163.716 77.111  1.00 53.06  ? 248 LEU A CD2   1 
ATOM   5221 N  N     . ASN B 2 249 ? 130.449 165.080 80.970  1.00 54.93  ? 249 ASN A N     1 
ATOM   5222 C  CA    . ASN B 2 249 ? 129.809 164.924 82.267  1.00 57.84  ? 249 ASN A CA    1 
ATOM   5223 C  C     . ASN B 2 249 ? 129.578 163.446 82.554  1.00 57.37  ? 249 ASN A C     1 
ATOM   5224 O  O     . ASN B 2 249 ? 129.038 162.720 81.716  1.00 58.99  ? 249 ASN A O     1 
ATOM   5225 C  CB    . ASN B 2 249 ? 128.493 165.698 82.308  1.00 60.12  ? 249 ASN A CB    1 
ATOM   5226 C  CG    . ASN B 2 249 ? 127.785 165.714 80.973  1.00 64.28  ? 249 ASN A CG    1 
ATOM   5227 O  OD1   . ASN B 2 249 ? 127.750 164.711 80.261  1.00 62.42  ? 249 ASN A OD1   1 
ATOM   5228 N  ND2   . ASN B 2 249 ? 127.214 166.860 80.623  1.00 63.33  ? 249 ASN A ND2   1 
ATOM   5229 N  N     . VAL B 2 250 ? 129.987 163.008 83.744  1.00 48.33  ? 250 VAL A N     1 
ATOM   5230 C  CA    . VAL B 2 250 ? 129.980 161.603 84.131  1.00 48.04  ? 250 VAL A CA    1 
ATOM   5231 C  C     . VAL B 2 250 ? 129.113 161.438 85.370  1.00 52.50  ? 250 VAL A C     1 
ATOM   5232 O  O     . VAL B 2 250 ? 129.313 162.135 86.370  1.00 57.73  ? 250 VAL A O     1 
ATOM   5233 C  CB    . VAL B 2 250 ? 131.408 161.088 84.388  1.00 48.66  ? 250 VAL A CB    1 
ATOM   5234 C  CG1   . VAL B 2 250 ? 131.369 159.673 84.903  1.00 50.52  ? 250 VAL A CG1   1 
ATOM   5235 C  CG2   . VAL B 2 250 ? 132.238 161.165 83.125  1.00 52.03  ? 250 VAL A CG2   1 
ATOM   5236 N  N     . ASP B 2 251 ? 128.209 160.515 85.334  1.00 56.89  ? 251 ASP A N     1 
ATOM   5237 C  CA    . ASP B 2 251 ? 127.248 160.308 86.433  1.00 54.92  ? 251 ASP A CA    1 
ATOM   5238 C  C     . ASP B 2 251 ? 127.666 159.107 87.257  1.00 58.06  ? 251 ASP A C     1 
ATOM   5239 O  O     . ASP B 2 251 ? 128.727 158.535 86.970  1.00 59.76  ? 251 ASP A O     1 
ATOM   5240 C  CB    . ASP B 2 251 ? 125.862 160.113 85.861  1.00 56.24  ? 251 ASP A CB    1 
ATOM   5241 C  CG    . ASP B 2 251 ? 125.544 158.715 85.362  1.00 64.20  ? 251 ASP A CG    1 
ATOM   5242 O  OD1   . ASP B 2 251 ? 126.065 158.347 84.290  1.00 64.41  ? 251 ASP A OD1   1 
ATOM   5243 O  OD2   . ASP B 2 251 ? 124.779 158.012 86.053  1.00 67.25  ? 251 ASP A OD2   1 
ATOM   5244 N  N     . LEU B 2 252 ? 126.807 158.646 88.141  1.00 57.43  ? 252 LEU A N     1 
ATOM   5245 C  CA    . LEU B 2 252 ? 127.211 157.644 89.126  1.00 57.99  ? 252 LEU A CA    1 
ATOM   5246 C  C     . LEU B 2 252 ? 127.535 156.305 88.472  1.00 61.74  ? 252 LEU A C     1 
ATOM   5247 O  O     . LEU B 2 252 ? 128.549 155.667 88.794  1.00 71.50  ? 252 LEU A O     1 
ATOM   5248 C  CB    . LEU B 2 252 ? 126.113 157.480 90.175  1.00 57.84  ? 252 LEU A CB    1 
ATOM   5249 C  CG    . LEU B 2 252 ? 125.656 158.738 90.915  1.00 56.00  ? 252 LEU A CG    1 
ATOM   5250 C  CD1   . LEU B 2 252 ? 124.842 158.365 92.133  1.00 59.95  ? 252 LEU A CD1   1 
ATOM   5251 C  CD2   . LEU B 2 252 ? 126.840 159.588 91.312  1.00 55.21  ? 252 LEU A CD2   1 
ATOM   5252 N  N     . THR B 2 253 ? 126.688 155.865 87.541  1.00 50.99  ? 253 THR A N     1 
ATOM   5253 C  CA    . THR B 2 253 ? 126.895 154.559 86.930  1.00 54.50  ? 253 THR A CA    1 
ATOM   5254 C  C     . THR B 2 253 ? 128.163 154.524 86.084  1.00 61.59  ? 253 THR A C     1 
ATOM   5255 O  O     . THR B 2 253 ? 128.825 153.482 86.015  1.00 64.95  ? 253 THR A O     1 
ATOM   5256 C  CB    . THR B 2 253 ? 125.671 154.157 86.105  1.00 56.35  ? 253 THR A CB    1 
ATOM   5257 O  OG1   . THR B 2 253 ? 125.840 152.822 85.617  1.00 61.15  ? 253 THR A OG1   1 
ATOM   5258 C  CG2   . THR B 2 253 ? 125.465 155.097 84.927  1.00 60.32  ? 253 THR A CG2   1 
ATOM   5259 N  N     . GLU B 2 254 ? 128.535 155.641 85.455  1.00 60.11  ? 254 GLU A N     1 
ATOM   5260 C  CA    . GLU B 2 254 ? 129.782 155.673 84.699  1.00 55.82  ? 254 GLU A CA    1 
ATOM   5261 C  C     . GLU B 2 254 ? 130.991 155.571 85.623  1.00 61.91  ? 254 GLU A C     1 
ATOM   5262 O  O     . GLU B 2 254 ? 131.950 154.846 85.322  1.00 68.98  ? 254 GLU A O     1 
ATOM   5263 C  CB    . GLU B 2 254 ? 129.848 156.936 83.845  1.00 58.31  ? 254 GLU A CB    1 
ATOM   5264 C  CG    . GLU B 2 254 ? 128.752 157.022 82.797  1.00 64.66  ? 254 GLU A CG    1 
ATOM   5265 C  CD    . GLU B 2 254 ? 128.774 155.856 81.821  1.00 72.45  ? 254 GLU A CD    1 
ATOM   5266 O  OE1   . GLU B 2 254 ? 129.848 155.585 81.243  1.00 70.28  ? 254 GLU A OE1   1 
ATOM   5267 O  OE2   . GLU B 2 254 ? 127.720 155.208 81.632  1.00 65.64  ? 254 GLU A OE2   1 
ATOM   5268 N  N     . PHE B 2 255 ? 130.957 156.272 86.758  1.00 60.04  ? 255 PHE A N     1 
ATOM   5269 C  CA    . PHE B 2 255 ? 132.005 156.114 87.761  1.00 61.18  ? 255 PHE A CA    1 
ATOM   5270 C  C     . PHE B 2 255 ? 132.148 154.657 88.157  1.00 62.49  ? 255 PHE A C     1 
ATOM   5271 O  O     . PHE B 2 255 ? 133.257 154.112 88.196  1.00 66.73  ? 255 PHE A O     1 
ATOM   5272 C  CB    . PHE B 2 255 ? 131.689 156.945 89.006  1.00 58.77  ? 255 PHE A CB    1 
ATOM   5273 C  CG    . PHE B 2 255 ? 131.862 158.412 88.821  1.00 67.05  ? 255 PHE A CG    1 
ATOM   5274 C  CD1   . PHE B 2 255 ? 133.068 158.933 88.395  1.00 71.41  ? 255 PHE A CD1   1 
ATOM   5275 C  CD2   . PHE B 2 255 ? 130.814 159.278 89.083  1.00 70.31  ? 255 PHE A CD2   1 
ATOM   5276 C  CE1   . PHE B 2 255 ? 133.224 160.289 88.229  1.00 72.85  ? 255 PHE A CE1   1 
ATOM   5277 C  CE2   . PHE B 2 255 ? 130.963 160.636 88.916  1.00 68.66  ? 255 PHE A CE2   1 
ATOM   5278 C  CZ    . PHE B 2 255 ? 132.168 161.142 88.488  1.00 71.12  ? 255 PHE A CZ    1 
ATOM   5279 N  N     . GLN B 2 256 ? 131.024 154.011 88.468  1.00 57.41  ? 256 GLN A N     1 
ATOM   5280 C  CA    . GLN B 2 256 ? 131.089 152.634 88.936  1.00 54.06  ? 256 GLN A CA    1 
ATOM   5281 C  C     . GLN B 2 256 ? 131.616 151.698 87.856  1.00 57.31  ? 256 GLN A C     1 
ATOM   5282 O  O     . GLN B 2 256 ? 132.440 150.822 88.139  1.00 61.08  ? 256 GLN A O     1 
ATOM   5283 C  CB    . GLN B 2 256 ? 129.717 152.187 89.428  1.00 56.49  ? 256 GLN A CB    1 
ATOM   5284 C  CG    . GLN B 2 256 ? 129.261 152.919 90.670  1.00 55.44  ? 256 GLN A CG    1 
ATOM   5285 C  CD    . GLN B 2 256 ? 127.935 152.423 91.179  1.00 59.63  ? 256 GLN A CD    1 
ATOM   5286 O  OE1   . GLN B 2 256 ? 127.227 153.132 91.889  1.00 62.60  ? 256 GLN A OE1   1 
ATOM   5287 N  NE2   . GLN B 2 256 ? 127.589 151.194 90.826  1.00 61.27  ? 256 GLN A NE2   1 
ATOM   5288 N  N     . THR B 2 257 ? 131.168 151.867 86.611  1.00 47.64  ? 257 THR A N     1 
ATOM   5289 C  CA    . THR B 2 257 ? 131.620 150.975 85.553  1.00 47.97  ? 257 THR A CA    1 
ATOM   5290 C  C     . THR B 2 257 ? 133.057 151.245 85.136  1.00 49.21  ? 257 THR A C     1 
ATOM   5291 O  O     . THR B 2 257 ? 133.666 150.390 84.487  1.00 53.99  ? 257 THR A O     1 
ATOM   5292 C  CB    . THR B 2 257 ? 130.703 151.074 84.334  1.00 47.39  ? 257 THR A CB    1 
ATOM   5293 O  OG1   . THR B 2 257 ? 131.011 150.017 83.420  1.00 47.36  ? 257 THR A OG1   1 
ATOM   5294 C  CG2   . THR B 2 257 ? 130.895 152.389 83.624  1.00 52.49  ? 257 THR A CG2   1 
ATOM   5295 N  N     . ASN B 2 258 ? 133.613 152.404 85.479  1.00 47.28  ? 258 ASN A N     1 
ATOM   5296 C  CA    . ASN B 2 258 ? 134.995 152.703 85.138  1.00 40.97  ? 258 ASN A CA    1 
ATOM   5297 C  C     . ASN B 2 258 ? 135.943 152.603 86.322  1.00 51.37  ? 258 ASN A C     1 
ATOM   5298 O  O     . ASN B 2 258 ? 137.146 152.802 86.147  1.00 62.29  ? 258 ASN A O     1 
ATOM   5299 C  CB    . ASN B 2 258 ? 135.094 154.100 84.526  1.00 48.12  ? 258 ASN A CB    1 
ATOM   5300 C  CG    . ASN B 2 258 ? 134.292 154.236 83.255  1.00 55.05  ? 258 ASN A CG    1 
ATOM   5301 O  OD1   . ASN B 2 258 ? 134.688 153.744 82.204  1.00 56.01  ? 258 ASN A OD1   1 
ATOM   5302 N  ND2   . ASN B 2 258 ? 133.159 154.915 83.343  1.00 56.15  ? 258 ASN A ND2   1 
ATOM   5303 N  N     . LEU B 2 259 ? 135.441 152.302 87.518  1.00 46.89  ? 259 LEU A N     1 
ATOM   5304 C  CA    . LEU B 2 259 ? 136.282 152.251 88.705  1.00 44.01  ? 259 LEU A CA    1 
ATOM   5305 C  C     . LEU B 2 259 ? 136.297 150.906 89.409  1.00 49.34  ? 259 LEU A C     1 
ATOM   5306 O  O     . LEU B 2 259 ? 137.220 150.654 90.188  1.00 56.54  ? 259 LEU A O     1 
ATOM   5307 C  CB    . LEU B 2 259 ? 135.839 153.318 89.714  1.00 44.29  ? 259 LEU A CB    1 
ATOM   5308 C  CG    . LEU B 2 259 ? 136.899 153.847 90.666  1.00 48.85  ? 259 LEU A CG    1 
ATOM   5309 C  CD1   . LEU B 2 259 ? 138.121 154.277 89.889  1.00 47.87  ? 259 LEU A CD1   1 
ATOM   5310 C  CD2   . LEU B 2 259 ? 136.341 155.003 91.453  1.00 50.52  ? 259 LEU A CD2   1 
ATOM   5311 N  N     . VAL B 2 260 ? 135.318 150.044 89.167  1.00 40.67  ? 260 VAL A N     1 
ATOM   5312 C  CA    . VAL B 2 260 ? 135.213 148.780 89.889  1.00 37.15  ? 260 VAL A CA    1 
ATOM   5313 C  C     . VAL B 2 260 ? 135.477 147.631 88.925  1.00 41.09  ? 260 VAL A C     1 
ATOM   5314 O  O     . VAL B 2 260 ? 134.586 147.253 88.153  1.00 48.60  ? 260 VAL A O     1 
ATOM   5315 C  CB    . VAL B 2 260 ? 133.838 148.647 90.559  1.00 37.45  ? 260 VAL A CB    1 
ATOM   5316 C  CG1   . VAL B 2 260 ? 133.768 147.390 91.382  1.00 40.15  ? 260 VAL A CG1   1 
ATOM   5317 C  CG2   . VAL B 2 260 ? 133.561 149.858 91.419  1.00 40.68  ? 260 VAL A CG2   1 
ATOM   5318 N  N     . PRO B 2 261 ? 136.673 147.053 88.933  1.00 34.63  ? 261 PRO A N     1 
ATOM   5319 C  CA    . PRO B 2 261 ? 136.979 145.962 88.001  1.00 34.95  ? 261 PRO A CA    1 
ATOM   5320 C  C     . PRO B 2 261 ? 136.230 144.678 88.313  1.00 44.86  ? 261 PRO A C     1 
ATOM   5321 O  O     . PRO B 2 261 ? 135.611 144.082 87.427  1.00 53.04  ? 261 PRO A O     1 
ATOM   5322 C  CB    . PRO B 2 261 ? 138.490 145.785 88.164  1.00 32.42  ? 261 PRO A CB    1 
ATOM   5323 C  CG    . PRO B 2 261 ? 138.781 146.273 89.514  1.00 43.44  ? 261 PRO A CG    1 
ATOM   5324 C  CD    . PRO B 2 261 ? 137.807 147.363 89.815  1.00 43.89  ? 261 PRO A CD    1 
ATOM   5325 N  N     . TYR B 2 262 ? 136.280 144.247 89.564  1.00 40.67  ? 262 TYR A N     1 
ATOM   5326 C  CA    . TYR B 2 262 ? 135.621 143.048 90.049  1.00 29.03  ? 262 TYR A CA    1 
ATOM   5327 C  C     . TYR B 2 262 ? 134.633 143.429 91.140  1.00 42.42  ? 262 TYR A C     1 
ATOM   5328 O  O     . TYR B 2 262 ? 134.794 144.466 91.792  1.00 53.07  ? 262 TYR A O     1 
ATOM   5329 C  CB    . TYR B 2 262 ? 136.648 142.050 90.594  1.00 31.27  ? 262 TYR A CB    1 
ATOM   5330 C  CG    . TYR B 2 262 ? 137.686 141.661 89.584  1.00 35.79  ? 262 TYR A CG    1 
ATOM   5331 C  CD1   . TYR B 2 262 ? 137.408 140.730 88.605  1.00 43.04  ? 262 TYR A CD1   1 
ATOM   5332 C  CD2   . TYR B 2 262 ? 138.943 142.225 89.607  1.00 41.17  ? 262 TYR A CD2   1 
ATOM   5333 C  CE1   . TYR B 2 262 ? 138.354 140.371 87.678  1.00 41.68  ? 262 TYR A CE1   1 
ATOM   5334 C  CE2   . TYR B 2 262 ? 139.893 141.873 88.684  1.00 42.20  ? 262 TYR A CE2   1 
ATOM   5335 C  CZ    . TYR B 2 262 ? 139.596 140.944 87.723  1.00 42.30  ? 262 TYR A CZ    1 
ATOM   5336 O  OH    . TYR B 2 262 ? 140.547 140.591 86.800  1.00 47.94  ? 262 TYR A OH    1 
ATOM   5337 N  N     . PRO B 2 263 ? 133.599 142.616 91.370  1.00 44.50  ? 263 PRO A N     1 
ATOM   5338 C  CA    . PRO B 2 263 ? 132.504 143.068 92.245  1.00 39.23  ? 263 PRO A CA    1 
ATOM   5339 C  C     . PRO B 2 263 ? 132.930 143.444 93.654  1.00 45.96  ? 263 PRO A C     1 
ATOM   5340 O  O     . PRO B 2 263 ? 132.350 144.368 94.234  1.00 50.24  ? 263 PRO A O     1 
ATOM   5341 C  CB    . PRO B 2 263 ? 131.550 141.870 92.243  1.00 34.18  ? 263 PRO A CB    1 
ATOM   5342 C  CG    . PRO B 2 263 ? 131.819 141.187 90.971  1.00 34.21  ? 263 PRO A CG    1 
ATOM   5343 C  CD    . PRO B 2 263 ? 133.286 141.327 90.735  1.00 43.23  ? 263 PRO A CD    1 
ATOM   5344 N  N     . ARG B 2 264 ? 133.919 142.765 94.227  1.00 48.14  ? 264 ARG A N     1 
ATOM   5345 C  CA    . ARG B 2 264 ? 134.329 143.052 95.594  1.00 40.06  ? 264 ARG A CA    1 
ATOM   5346 C  C     . ARG B 2 264 ? 135.405 144.123 95.697  1.00 42.48  ? 264 ARG A C     1 
ATOM   5347 O  O     . ARG B 2 264 ? 135.641 144.631 96.796  1.00 52.18  ? 264 ARG A O     1 
ATOM   5348 C  CB    . ARG B 2 264 ? 134.825 141.778 96.276  1.00 36.75  ? 264 ARG A CB    1 
ATOM   5349 C  CG    . ARG B 2 264 ? 133.842 140.637 96.221  1.00 45.23  ? 264 ARG A CG    1 
ATOM   5350 C  CD    . ARG B 2 264 ? 134.452 139.379 96.781  1.00 48.88  ? 264 ARG A CD    1 
ATOM   5351 N  NE    . ARG B 2 264 ? 134.291 139.293 98.225  1.00 48.10  ? 264 ARG A NE    1 
ATOM   5352 C  CZ    . ARG B 2 264 ? 135.124 138.650 99.029  1.00 48.04  ? 264 ARG A CZ    1 
ATOM   5353 N  NH1   . ARG B 2 264 ? 136.199 138.040 98.563  1.00 46.68  ? 264 ARG A NH1   1 
ATOM   5354 N  NH2   . ARG B 2 264 ? 134.874 138.624 100.333 1.00 46.69  ? 264 ARG A NH2   1 
ATOM   5355 N  N     . ILE B 2 265 ? 136.063 144.477 94.598  1.00 39.44  ? 265 ILE A N     1 
ATOM   5356 C  CA    . ILE B 2 265 ? 137.132 145.491 94.630  1.00 43.32  ? 265 ILE A CA    1 
ATOM   5357 C  C     . ILE B 2 265 ? 136.458 146.829 94.351  1.00 48.03  ? 265 ILE A C     1 
ATOM   5358 O  O     . ILE B 2 265 ? 136.459 147.352 93.236  1.00 50.40  ? 265 ILE A O     1 
ATOM   5359 C  CB    . ILE B 2 265 ? 138.250 145.172 93.635  1.00 42.13  ? 265 ILE A CB    1 
ATOM   5360 C  CG1   . ILE B 2 265 ? 138.624 143.693 93.710  1.00 40.12  ? 265 ILE A CG1   1 
ATOM   5361 C  CG2   . ILE B 2 265 ? 139.461 146.045 93.887  1.00 48.66  ? 265 ILE A CG2   1 
ATOM   5362 C  CD1   . ILE B 2 265 ? 139.185 143.268 95.034  1.00 45.56  ? 265 ILE A CD1   1 
ATOM   5363 N  N     . HIS B 2 266 ? 135.869 147.407 95.396  1.00 43.80  ? 266 HIS A N     1 
ATOM   5364 C  CA    . HIS B 2 266 ? 135.112 148.650 95.260  1.00 45.78  ? 266 HIS A CA    1 
ATOM   5365 C  C     . HIS B 2 266 ? 135.377 149.600 96.426  1.00 48.90  ? 266 HIS A C     1 
ATOM   5366 O  O     . HIS B 2 266 ? 134.456 150.157 97.021  1.00 50.11  ? 266 HIS A O     1 
ATOM   5367 C  CB    . HIS B 2 266 ? 133.619 148.371 95.110  1.00 43.09  ? 266 HIS A CB    1 
ATOM   5368 C  CG    . HIS B 2 266 ? 133.001 147.682 96.284  1.00 38.25  ? 266 HIS A CG    1 
ATOM   5369 N  ND1   . HIS B 2 266 ? 132.678 148.339 97.450  1.00 43.77  ? 266 HIS A ND1   1 
ATOM   5370 C  CD2   . HIS B 2 266 ? 132.622 146.396 96.462  1.00 39.72  ? 266 HIS A CD2   1 
ATOM   5371 C  CE1   . HIS B 2 266 ? 132.135 147.485 98.298  1.00 43.28  ? 266 HIS A CE1   1 
ATOM   5372 N  NE2   . HIS B 2 266 ? 132.093 146.299 97.724  1.00 44.48  ? 266 HIS A NE2   1 
ATOM   5373 N  N     . PHE B 2 267 ? 136.647 149.806 96.769  1.00 49.51  ? 267 PHE A N     1 
ATOM   5374 C  CA    . PHE B 2 267 ? 137.033 150.658 97.896  1.00 41.30  ? 267 PHE A CA    1 
ATOM   5375 C  C     . PHE B 2 267 ? 138.020 151.726 97.448  1.00 38.70  ? 267 PHE A C     1 
ATOM   5376 O  O     . PHE B 2 267 ? 139.220 151.632 97.730  1.00 44.09  ? 267 PHE A O     1 
ATOM   5377 C  CB    . PHE B 2 267 ? 137.637 149.829 99.028  1.00 44.79  ? 267 PHE A CB    1 
ATOM   5378 C  CG    . PHE B 2 267 ? 136.674 148.882 99.662  1.00 43.12  ? 267 PHE A CG    1 
ATOM   5379 C  CD1   . PHE B 2 267 ? 136.444 147.639 99.114  1.00 49.01  ? 267 PHE A CD1   1 
ATOM   5380 C  CD2   . PHE B 2 267 ? 136.002 149.233 100.809 1.00 41.97  ? 267 PHE A CD2   1 
ATOM   5381 C  CE1   . PHE B 2 267 ? 135.557 146.772 99.695  1.00 51.14  ? 267 PHE A CE1   1 
ATOM   5382 C  CE2   . PHE B 2 267 ? 135.118 148.370 101.392 1.00 41.41  ? 267 PHE A CE2   1 
ATOM   5383 C  CZ    . PHE B 2 267 ? 134.895 147.139 100.835 1.00 44.41  ? 267 PHE A CZ    1 
ATOM   5384 N  N     . PRO B 2 268 ? 137.554 152.759 96.757  1.00 38.39  ? 268 PRO A N     1 
ATOM   5385 C  CA    . PRO B 2 268 ? 138.453 153.834 96.335  1.00 41.36  ? 268 PRO A CA    1 
ATOM   5386 C  C     . PRO B 2 268 ? 138.785 154.792 97.470  1.00 47.38  ? 268 PRO A C     1 
ATOM   5387 O  O     . PRO B 2 268 ? 138.117 154.841 98.503  1.00 57.48  ? 268 PRO A O     1 
ATOM   5388 C  CB    . PRO B 2 268 ? 137.660 154.554 95.236  1.00 44.54  ? 268 PRO A CB    1 
ATOM   5389 C  CG    . PRO B 2 268 ? 136.451 153.727 94.991  1.00 44.93  ? 268 PRO A CG    1 
ATOM   5390 C  CD    . PRO B 2 268 ? 136.199 152.953 96.228  1.00 45.85  ? 268 PRO A CD    1 
ATOM   5391 N  N     . LEU B 2 269 ? 140.032 155.552 96.990  1.00 38.53  ? 269 LEU A N     1 
ATOM   5392 C  CA    . LEU B 2 269 ? 140.656 156.586 97.841  1.00 41.19  ? 269 LEU A CA    1 
ATOM   5393 C  C     . LEU B 2 269 ? 140.415 157.939 97.181  1.00 45.25  ? 269 LEU A C     1 
ATOM   5394 O  O     . LEU B 2 269 ? 140.597 158.010 95.962  1.00 48.73  ? 269 LEU A O     1 
ATOM   5395 C  CB    . LEU B 2 269 ? 142.143 156.278 97.942  1.00 43.87  ? 269 LEU A CB    1 
ATOM   5396 C  CG    . LEU B 2 269 ? 142.569 155.069 98.771  1.00 43.03  ? 269 LEU A CG    1 
ATOM   5397 C  CD1   . LEU B 2 269 ? 142.607 153.809 97.920  1.00 42.22  ? 269 LEU A CD1   1 
ATOM   5398 C  CD2   . LEU B 2 269 ? 143.969 155.443 99.184  1.00 47.74  ? 269 LEU A CD2   1 
ATOM   5399 N  N     . ALA B 2 270 ? 139.895 158.999 98.072  1.00 52.88  ? 270 ALA A N     1 
ATOM   5400 C  CA    . ALA B 2 270 ? 139.670 160.281 97.422  1.00 45.50  ? 270 ALA A CA    1 
ATOM   5401 C  C     . ALA B 2 270 ? 140.784 161.278 97.720  1.00 51.54  ? 270 ALA A C     1 
ATOM   5402 O  O     . ALA B 2 270 ? 141.524 161.154 98.697  1.00 57.08  ? 270 ALA A O     1 
ATOM   5403 C  CB    . ALA B 2 270 ? 138.325 160.866 97.851  1.00 48.91  ? 270 ALA A CB    1 
ATOM   5404 N  N     . THR B 2 271 ? 140.882 162.283 96.852  1.00 57.24  ? 271 THR A N     1 
ATOM   5405 C  CA    . THR B 2 271 ? 141.850 163.362 96.977  1.00 54.57  ? 271 THR A CA    1 
ATOM   5406 C  C     . THR B 2 271 ? 141.237 164.624 96.387  1.00 52.45  ? 271 THR A C     1 
ATOM   5407 O  O     . THR B 2 271 ? 140.393 164.554 95.492  1.00 54.83  ? 271 THR A O     1 
ATOM   5408 C  CB    . THR B 2 271 ? 143.163 163.029 96.261  1.00 52.46  ? 271 THR A CB    1 
ATOM   5409 O  OG1   . THR B 2 271 ? 143.557 161.690 96.577  1.00 56.93  ? 271 THR A OG1   1 
ATOM   5410 C  CG2   . THR B 2 271 ? 144.265 163.974 96.683  1.00 53.92  ? 271 THR A CG2   1 
ATOM   5411 N  N     . TYR B 2 272 ? 141.662 165.777 96.895  1.00 50.05  ? 272 TYR A N     1 
ATOM   5412 C  CA    . TYR B 2 272 ? 141.220 167.062 96.375  1.00 45.50  ? 272 TYR A CA    1 
ATOM   5413 C  C     . TYR B 2 272 ? 142.424 167.962 96.146  1.00 48.11  ? 272 TYR A C     1 
ATOM   5414 O  O     . TYR B 2 272 ? 143.434 167.865 96.846  1.00 57.04  ? 272 TYR A O     1 
ATOM   5415 C  CB    . TYR B 2 272 ? 140.231 167.746 97.323  1.00 48.40  ? 272 TYR A CB    1 
ATOM   5416 C  CG    . TYR B 2 272 ? 139.398 168.827 96.676  1.00 48.99  ? 272 TYR A CG    1 
ATOM   5417 C  CD1   . TYR B 2 272 ? 138.390 168.509 95.786  1.00 53.15  ? 272 TYR A CD1   1 
ATOM   5418 C  CD2   . TYR B 2 272 ? 139.609 170.163 96.971  1.00 47.68  ? 272 TYR A CD2   1 
ATOM   5419 C  CE1   . TYR B 2 272 ? 137.623 169.489 95.198  1.00 50.09  ? 272 TYR A CE1   1 
ATOM   5420 C  CE2   . TYR B 2 272 ? 138.846 171.148 96.387  1.00 48.63  ? 272 TYR A CE2   1 
ATOM   5421 C  CZ    . TYR B 2 272 ? 137.856 170.805 95.501  1.00 50.93  ? 272 TYR A CZ    1 
ATOM   5422 O  OH    . TYR B 2 272 ? 137.092 171.783 94.917  1.00 52.95  ? 272 TYR A OH    1 
ATOM   5423 N  N     . ALA B 2 273 ? 142.308 168.840 95.149  1.00 42.78  ? 273 ALA A N     1 
ATOM   5424 C  CA    . ALA B 2 273 ? 143.351 169.803 94.838  1.00 41.86  ? 273 ALA A CA    1 
ATOM   5425 C  C     . ALA B 2 273 ? 142.723 170.963 94.092  1.00 44.87  ? 273 ALA A C     1 
ATOM   5426 O  O     . ALA B 2 273 ? 141.847 170.730 93.249  1.00 55.20  ? 273 ALA A O     1 
ATOM   5427 C  CB    . ALA B 2 273 ? 144.462 169.172 93.996  1.00 45.59  ? 273 ALA A CB    1 
ATOM   5428 N  N     . PRO B 2 274 ? 143.127 172.208 94.359  1.00 41.45  ? 274 PRO A N     1 
ATOM   5429 C  CA    . PRO B 2 274 ? 144.147 172.646 95.307  1.00 43.75  ? 274 PRO A CA    1 
ATOM   5430 C  C     . PRO B 2 274 ? 143.589 173.089 96.652  1.00 53.55  ? 274 PRO A C     1 
ATOM   5431 O  O     . PRO B 2 274 ? 142.640 173.864 96.719  1.00 60.36  ? 274 PRO A O     1 
ATOM   5432 C  CB    . PRO B 2 274 ? 144.794 173.816 94.567  1.00 44.15  ? 274 PRO A CB    1 
ATOM   5433 C  CG    . PRO B 2 274 ? 143.691 174.395 93.717  1.00 43.27  ? 274 PRO A CG    1 
ATOM   5434 C  CD    . PRO B 2 274 ? 142.609 173.344 93.587  1.00 42.59  ? 274 PRO A CD    1 
ATOM   5435 N  N     . VAL B 2 275 ? 144.163 172.603 97.750  1.00 51.04  ? 275 VAL A N     1 
ATOM   5436 C  CA    . VAL B 2 275 ? 143.806 173.072 99.088  1.00 51.66  ? 275 VAL A CA    1 
ATOM   5437 C  C     . VAL B 2 275 ? 144.861 174.107 99.465  1.00 55.69  ? 275 VAL A C     1 
ATOM   5438 O  O     . VAL B 2 275 ? 145.917 173.785 100.002 1.00 65.53  ? 275 VAL A O     1 
ATOM   5439 C  CB    . VAL B 2 275 ? 143.724 171.928 100.093 1.00 56.94  ? 275 VAL A CB    1 
ATOM   5440 C  CG1   . VAL B 2 275 ? 143.062 172.400 101.372 1.00 60.64  ? 275 VAL A CG1   1 
ATOM   5441 C  CG2   . VAL B 2 275 ? 142.956 170.768 99.502  1.00 54.14  ? 275 VAL A CG2   1 
ATOM   5442 N  N     . ILE B 2 276 ? 144.566 175.370 99.174  1.00 48.83  ? 276 ILE A N     1 
ATOM   5443 C  CA    . ILE B 2 276 ? 145.523 176.450 99.345  1.00 53.12  ? 276 ILE A CA    1 
ATOM   5444 C  C     . ILE B 2 276 ? 144.880 177.556 100.167 1.00 55.71  ? 276 ILE A C     1 
ATOM   5445 O  O     . ILE B 2 276 ? 143.656 177.690 100.226 1.00 58.30  ? 276 ILE A O     1 
ATOM   5446 C  CB    . ILE B 2 276 ? 146.026 176.992 97.987  1.00 53.75  ? 276 ILE A CB    1 
ATOM   5447 C  CG1   . ILE B 2 276 ? 147.474 177.467 98.095  1.00 56.49  ? 276 ILE A CG1   1 
ATOM   5448 C  CG2   . ILE B 2 276 ? 145.125 178.099 97.470  1.00 58.50  ? 276 ILE A CG2   1 
ATOM   5449 C  CD1   . ILE B 2 276 ? 148.467 176.348 98.291  1.00 58.94  ? 276 ILE A CD1   1 
ATOM   5450 N  N     . SER B 2 277 ? 145.725 178.341 100.819 1.00 58.88  ? 277 SER A N     1 
ATOM   5451 C  CA    . SER B 2 277 ? 145.273 179.448 101.642 1.00 61.05  ? 277 SER A CA    1 
ATOM   5452 C  C     . SER B 2 277 ? 145.196 180.726 100.814 1.00 65.29  ? 277 SER A C     1 
ATOM   5453 O  O     . SER B 2 277 ? 145.693 180.802 99.690  1.00 69.64  ? 277 SER A O     1 
ATOM   5454 C  CB    . SER B 2 277 ? 146.205 179.642 102.834 1.00 62.98  ? 277 SER A CB    1 
ATOM   5455 O  OG    . SER B 2 277 ? 145.852 180.795 103.576 1.00 67.06  ? 277 SER A OG    1 
ATOM   5456 N  N     . ALA B 2 278 ? 144.563 181.746 101.393 1.00 62.16  ? 278 ALA A N     1 
ATOM   5457 C  CA    . ALA B 2 278 ? 144.413 183.013 100.690 1.00 56.93  ? 278 ALA A CA    1 
ATOM   5458 C  C     . ALA B 2 278 ? 145.762 183.671 100.435 1.00 62.76  ? 278 ALA A C     1 
ATOM   5459 O  O     . ALA B 2 278 ? 145.994 184.227 99.356  1.00 65.58  ? 278 ALA A O     1 
ATOM   5460 C  CB    . ALA B 2 278 ? 143.500 183.946 101.482 1.00 58.69  ? 278 ALA A CB    1 
ATOM   5461 N  N     . GLU B 2 279 ? 146.662 183.625 101.418 1.00 64.19  ? 279 GLU A N     1 
ATOM   5462 C  CA    . GLU B 2 279 ? 147.971 184.248 101.250 1.00 62.10  ? 279 GLU A CA    1 
ATOM   5463 C  C     . GLU B 2 279 ? 148.777 183.562 100.157 1.00 65.15  ? 279 GLU A C     1 
ATOM   5464 O  O     . GLU B 2 279 ? 149.429 184.228 99.345  1.00 67.00  ? 279 GLU A O     1 
ATOM   5465 C  CB    . GLU B 2 279 ? 148.732 184.228 102.573 1.00 68.63  ? 279 GLU A CB    1 
ATOM   5466 C  CG    . GLU B 2 279 ? 150.084 184.921 102.524 1.00 70.72  ? 279 GLU A CG    1 
ATOM   5467 C  CD    . GLU B 2 279 ? 151.240 183.942 102.446 1.00 72.65  ? 279 GLU A CD    1 
ATOM   5468 O  OE1   . GLU B 2 279 ? 151.074 182.788 102.894 1.00 72.33  ? 279 GLU A OE1   1 
ATOM   5469 O  OE2   . GLU B 2 279 ? 152.313 184.326 101.937 1.00 70.37  ? 279 GLU A OE2   1 
ATOM   5470 N  N     . LYS B 2 280 ? 148.750 182.236 100.120 1.00 62.09  ? 280 LYS A N     1 
ATOM   5471 C  CA    . LYS B 2 280 ? 149.450 181.469 99.102  1.00 59.49  ? 280 LYS A CA    1 
ATOM   5472 C  C     . LYS B 2 280 ? 148.621 181.267 97.843  1.00 63.32  ? 280 LYS A C     1 
ATOM   5473 O  O     . LYS B 2 280 ? 149.103 180.634 96.900  1.00 68.59  ? 280 LYS A O     1 
ATOM   5474 C  CB    . LYS B 2 280 ? 149.868 180.106 99.661  1.00 61.27  ? 280 LYS A CB    1 
ATOM   5475 C  CG    . LYS B 2 280 ? 150.683 180.178 100.934 1.00 62.01  ? 280 LYS A CG    1 
ATOM   5476 C  CD    . LYS B 2 280 ? 150.537 178.913 101.759 1.00 62.56  ? 280 LYS A CD    1 
ATOM   5477 C  CE    . LYS B 2 280 ? 151.098 177.710 101.034 1.00 64.70  ? 280 LYS A CE    1 
ATOM   5478 N  NZ    . LYS B 2 280 ? 150.905 176.462 101.816 1.00 63.76  ? 280 LYS A NZ    1 
ATOM   5479 N  N     . ALA B 2 281 ? 147.378 181.749 97.817  1.00 59.06  ? 281 ALA A N     1 
ATOM   5480 C  CA    . ALA B 2 281 ? 146.585 181.660 96.597  1.00 58.37  ? 281 ALA A CA    1 
ATOM   5481 C  C     . ALA B 2 281 ? 147.233 182.465 95.486  1.00 61.60  ? 281 ALA A C     1 
ATOM   5482 O  O     . ALA B 2 281 ? 147.407 181.974 94.366  1.00 63.41  ? 281 ALA A O     1 
ATOM   5483 C  CB    . ALA B 2 281 ? 145.159 182.146 96.856  1.00 66.11  ? 281 ALA A CB    1 
ATOM   5484 N  N     . TYR B 2 282 ? 147.607 183.706 95.781  1.00 65.97  ? 282 TYR A N     1 
ATOM   5485 C  CA    . TYR B 2 282 ? 148.497 184.433 94.899  1.00 62.96  ? 282 TYR A CA    1 
ATOM   5486 C  C     . TYR B 2 282 ? 149.868 183.770 94.933  1.00 66.90  ? 282 TYR A C     1 
ATOM   5487 O  O     . TYR B 2 282 ? 150.105 182.809 95.669  1.00 73.64  ? 282 TYR A O     1 
ATOM   5488 C  CB    . TYR B 2 282 ? 148.590 185.897 95.310  1.00 64.19  ? 282 TYR A CB    1 
ATOM   5489 C  CG    . TYR B 2 282 ? 147.296 186.488 95.814  1.00 70.26  ? 282 TYR A CG    1 
ATOM   5490 C  CD1   . TYR B 2 282 ? 146.239 186.734 94.951  1.00 72.55  ? 282 TYR A CD1   1 
ATOM   5491 C  CD2   . TYR B 2 282 ? 147.138 186.814 97.152  1.00 70.68  ? 282 TYR A CD2   1 
ATOM   5492 C  CE1   . TYR B 2 282 ? 145.056 187.279 95.412  1.00 70.83  ? 282 TYR A CE1   1 
ATOM   5493 C  CE2   . TYR B 2 282 ? 145.963 187.359 97.621  1.00 71.15  ? 282 TYR A CE2   1 
ATOM   5494 C  CZ    . TYR B 2 282 ? 144.924 187.589 96.749  1.00 72.89  ? 282 TYR A CZ    1 
ATOM   5495 O  OH    . TYR B 2 282 ? 143.749 188.133 97.214  1.00 71.91  ? 282 TYR A OH    1 
ATOM   5496 N  N     . HIS B 2 283 ? 150.784 184.281 94.122  1.00 59.31  ? 283 HIS A N     1 
ATOM   5497 C  CA    . HIS B 2 283 ? 152.140 183.762 94.008  1.00 63.31  ? 283 HIS A CA    1 
ATOM   5498 C  C     . HIS B 2 283 ? 152.188 182.361 93.414  1.00 61.97  ? 283 HIS A C     1 
ATOM   5499 O  O     . HIS B 2 283 ? 153.258 181.746 93.393  1.00 65.86  ? 283 HIS A O     1 
ATOM   5500 C  CB    . HIS B 2 283 ? 152.860 183.763 95.362  1.00 63.13  ? 283 HIS A CB    1 
ATOM   5501 C  CG    . HIS B 2 283 ? 152.763 185.060 96.101  1.00 62.70  ? 283 HIS A CG    1 
ATOM   5502 N  ND1   . HIS B 2 283 ? 152.980 185.158 97.457  1.00 64.27  ? 283 HIS A ND1   1 
ATOM   5503 C  CD2   . HIS B 2 283 ? 152.501 186.315 95.671  1.00 68.82  ? 283 HIS A CD2   1 
ATOM   5504 C  CE1   . HIS B 2 283 ? 152.838 186.415 97.834  1.00 67.27  ? 283 HIS A CE1   1 
ATOM   5505 N  NE2   . HIS B 2 283 ? 152.550 187.139 96.769  1.00 69.73  ? 283 HIS A NE2   1 
ATOM   5506 N  N     . GLU B 2 284 ? 151.067 181.836 92.926  1.00 57.84  ? 284 GLU A N     1 
ATOM   5507 C  CA    . GLU B 2 284 ? 151.029 180.505 92.339  1.00 58.52  ? 284 GLU A CA    1 
ATOM   5508 C  C     . GLU B 2 284 ? 150.218 180.521 91.053  1.00 60.65  ? 284 GLU A C     1 
ATOM   5509 O  O     . GLU B 2 284 ? 149.180 181.181 90.972  1.00 62.48  ? 284 GLU A O     1 
ATOM   5510 C  CB    . GLU B 2 284 ? 150.441 179.483 93.316  1.00 65.41  ? 284 GLU A CB    1 
ATOM   5511 C  CG    . GLU B 2 284 ? 151.335 179.185 94.508  1.00 71.25  ? 284 GLU A CG    1 
ATOM   5512 C  CD    . GLU B 2 284 ? 150.830 178.028 95.346  1.00 73.17  ? 284 GLU A CD    1 
ATOM   5513 O  OE1   . GLU B 2 284 ? 149.844 177.381 94.937  1.00 72.50  ? 284 GLU A OE1   1 
ATOM   5514 O  OE2   . GLU B 2 284 ? 151.419 177.766 96.416  1.00 69.91  ? 284 GLU A OE2   1 
ATOM   5515 N  N     . GLN B 2 285 ? 150.698 179.783 90.050  1.00 61.19  ? 285 GLN A N     1 
ATOM   5516 C  CA    . GLN B 2 285 ? 150.005 179.721 88.767  1.00 59.13  ? 285 GLN A CA    1 
ATOM   5517 C  C     . GLN B 2 285 ? 148.704 178.939 88.878  1.00 61.15  ? 285 GLN A C     1 
ATOM   5518 O  O     . GLN B 2 285 ? 147.658 179.383 88.395  1.00 62.63  ? 285 GLN A O     1 
ATOM   5519 C  CB    . GLN B 2 285 ? 150.915 179.088 87.715  1.00 58.41  ? 285 GLN A CB    1 
ATOM   5520 C  CG    . GLN B 2 285 ? 151.994 180.003 87.189  1.00 62.66  ? 285 GLN A CG    1 
ATOM   5521 C  CD    . GLN B 2 285 ? 151.560 180.751 85.951  1.00 67.58  ? 285 GLN A CD    1 
ATOM   5522 O  OE1   . GLN B 2 285 ? 150.462 180.537 85.438  1.00 66.28  ? 285 GLN A OE1   1 
ATOM   5523 N  NE2   . GLN B 2 285 ? 152.419 181.636 85.461  1.00 66.01  ? 285 GLN A NE2   1 
ATOM   5524 N  N     . LEU B 2 286 ? 148.757 177.767 89.511  1.00 57.59  ? 286 LEU A N     1 
ATOM   5525 C  CA    . LEU B 2 286 ? 147.592 176.918 89.742  1.00 50.10  ? 286 LEU A CA    1 
ATOM   5526 C  C     . LEU B 2 286 ? 146.937 176.511 88.422  1.00 54.55  ? 286 LEU A C     1 
ATOM   5527 O  O     . LEU B 2 286 ? 145.752 176.741 88.181  1.00 60.38  ? 286 LEU A O     1 
ATOM   5528 C  CB    . LEU B 2 286 ? 146.597 177.612 90.674  1.00 50.93  ? 286 LEU A CB    1 
ATOM   5529 C  CG    . LEU B 2 286 ? 147.089 177.861 92.096  1.00 50.46  ? 286 LEU A CG    1 
ATOM   5530 C  CD1   . LEU B 2 286 ? 146.079 178.676 92.866  1.00 53.68  ? 286 LEU A CD1   1 
ATOM   5531 C  CD2   . LEU B 2 286 ? 147.345 176.550 92.799  1.00 56.65  ? 286 LEU A CD2   1 
ATOM   5532 N  N     . SER B 2 287 ? 147.739 175.884 87.568  1.00 53.48  ? 287 SER A N     1 
ATOM   5533 C  CA    . SER B 2 287 ? 147.288 175.442 86.262  1.00 49.90  ? 287 SER A CA    1 
ATOM   5534 C  C     . SER B 2 287 ? 146.740 174.019 86.340  1.00 51.90  ? 287 SER A C     1 
ATOM   5535 O  O     . SER B 2 287 ? 146.716 173.389 87.399  1.00 59.57  ? 287 SER A O     1 
ATOM   5536 C  CB    . SER B 2 287 ? 148.425 175.529 85.251  1.00 51.15  ? 287 SER A CB    1 
ATOM   5537 O  OG    . SER B 2 287 ? 149.496 174.682 85.619  1.00 58.46  ? 287 SER A OG    1 
ATOM   5538 N  N     . VAL B 2 288 ? 146.291 173.506 85.194  1.00 46.23  ? 288 VAL A N     1 
ATOM   5539 C  CA    . VAL B 2 288 ? 145.707 172.169 85.148  1.00 42.85  ? 288 VAL A CA    1 
ATOM   5540 C  C     . VAL B 2 288 ? 146.752 171.114 85.487  1.00 52.03  ? 288 VAL A C     1 
ATOM   5541 O  O     . VAL B 2 288 ? 146.506 170.208 86.292  1.00 61.21  ? 288 VAL A O     1 
ATOM   5542 C  CB    . VAL B 2 288 ? 145.073 171.912 83.771  1.00 46.06  ? 288 VAL A CB    1 
ATOM   5543 C  CG1   . VAL B 2 288 ? 144.643 170.476 83.650  1.00 46.68  ? 288 VAL A CG1   1 
ATOM   5544 C  CG2   . VAL B 2 288 ? 143.889 172.824 83.560  1.00 54.28  ? 288 VAL A CG2   1 
ATOM   5545 N  N     . ALA B 2 289 ? 147.932 171.211 84.874  1.00 49.53  ? 289 ALA A N     1 
ATOM   5546 C  CA    . ALA B 2 289 ? 148.983 170.230 85.127  1.00 47.95  ? 289 ALA A CA    1 
ATOM   5547 C  C     . ALA B 2 289 ? 149.452 170.283 86.573  1.00 47.38  ? 289 ALA A C     1 
ATOM   5548 O  O     . ALA B 2 289 ? 149.706 169.242 87.191  1.00 52.88  ? 289 ALA A O     1 
ATOM   5549 C  CB    . ALA B 2 289 ? 150.154 170.460 84.176  1.00 49.60  ? 289 ALA A CB    1 
ATOM   5550 N  N     . GLU B 2 290 ? 149.572 171.486 87.129  1.00 47.82  ? 290 GLU A N     1 
ATOM   5551 C  CA    . GLU B 2 290 ? 150.030 171.626 88.506  1.00 47.89  ? 290 GLU A CA    1 
ATOM   5552 C  C     . GLU B 2 290 ? 149.017 171.051 89.488  1.00 52.58  ? 290 GLU A C     1 
ATOM   5553 O  O     . GLU B 2 290 ? 149.398 170.456 90.501  1.00 61.52  ? 290 GLU A O     1 
ATOM   5554 C  CB    . GLU B 2 290 ? 150.317 173.095 88.806  1.00 51.20  ? 290 GLU A CB    1 
ATOM   5555 C  CG    . GLU B 2 290 ? 150.766 173.368 90.223  1.00 57.32  ? 290 GLU A CG    1 
ATOM   5556 C  CD    . GLU B 2 290 ? 151.203 174.804 90.421  1.00 64.18  ? 290 GLU A CD    1 
ATOM   5557 O  OE1   . GLU B 2 290 ? 151.266 175.546 89.419  1.00 64.29  ? 290 GLU A OE1   1 
ATOM   5558 O  OE2   . GLU B 2 290 ? 151.481 175.190 91.575  1.00 64.91  ? 290 GLU A OE2   1 
ATOM   5559 N  N     . ILE B 2 291 ? 147.726 171.214 89.205  1.00 42.38  ? 291 ILE A N     1 
ATOM   5560 C  CA    . ILE B 2 291 ? 146.701 170.619 90.054  1.00 43.17  ? 291 ILE A CA    1 
ATOM   5561 C  C     . ILE B 2 291 ? 146.697 169.101 89.910  1.00 49.35  ? 291 ILE A C     1 
ATOM   5562 O  O     . ILE B 2 291 ? 146.555 168.374 90.898  1.00 56.11  ? 291 ILE A O     1 
ATOM   5563 C  CB    . ILE B 2 291 ? 145.326 171.226 89.731  1.00 51.36  ? 291 ILE A CB    1 
ATOM   5564 C  CG1   . ILE B 2 291 ? 145.278 172.688 90.163  1.00 58.92  ? 291 ILE A CG1   1 
ATOM   5565 C  CG2   . ILE B 2 291 ? 144.226 170.462 90.421  1.00 54.98  ? 291 ILE A CG2   1 
ATOM   5566 C  CD1   . ILE B 2 291 ? 143.922 173.331 89.984  1.00 54.91  ? 291 ILE A CD1   1 
ATOM   5567 N  N     . THR B 2 292 ? 146.852 168.598 88.684  1.00 46.70  ? 292 THR A N     1 
ATOM   5568 C  CA    . THR B 2 292 ? 146.825 167.155 88.467  1.00 40.57  ? 292 THR A CA    1 
ATOM   5569 C  C     . THR B 2 292 ? 148.006 166.465 89.137  1.00 43.69  ? 292 THR A C     1 
ATOM   5570 O  O     . THR B 2 292 ? 147.852 165.388 89.722  1.00 48.91  ? 292 THR A O     1 
ATOM   5571 C  CB    . THR B 2 292 ? 146.803 166.853 86.971  1.00 47.68  ? 292 THR A CB    1 
ATOM   5572 O  OG1   . THR B 2 292 ? 145.617 167.408 86.393  1.00 54.30  ? 292 THR A OG1   1 
ATOM   5573 C  CG2   . THR B 2 292 ? 146.822 165.361 86.723  1.00 49.45  ? 292 THR A CG2   1 
ATOM   5574 N  N     . ASN B 2 293 ? 149.191 167.067 89.067  1.00 50.30  ? 293 ASN A N     1 
ATOM   5575 C  CA    . ASN B 2 293 ? 150.365 166.446 89.671  1.00 47.12  ? 293 ASN A CA    1 
ATOM   5576 C  C     . ASN B 2 293 ? 150.235 166.367 91.186  1.00 52.74  ? 293 ASN A C     1 
ATOM   5577 O  O     . ASN B 2 293 ? 150.750 165.435 91.811  1.00 52.26  ? 293 ASN A O     1 
ATOM   5578 C  CB    . ASN B 2 293 ? 151.620 167.215 89.275  1.00 46.52  ? 293 ASN A CB    1 
ATOM   5579 C  CG    . ASN B 2 293 ? 152.166 166.782 87.940  1.00 50.67  ? 293 ASN A CG    1 
ATOM   5580 O  OD1   . ASN B 2 293 ? 151.482 166.125 87.161  1.00 55.05  ? 293 ASN A OD1   1 
ATOM   5581 N  ND2   . ASN B 2 293 ? 153.405 167.153 87.662  1.00 49.97  ? 293 ASN A ND2   1 
ATOM   5582 N  N     . ALA B 2 294 ? 149.548 167.334 91.793  1.00 59.39  ? 294 ALA A N     1 
ATOM   5583 C  CA    . ALA B 2 294 ? 149.385 167.350 93.240  1.00 52.42  ? 294 ALA A CA    1 
ATOM   5584 C  C     . ALA B 2 294 ? 148.411 166.296 93.738  1.00 50.58  ? 294 ALA A C     1 
ATOM   5585 O  O     . ALA B 2 294 ? 148.366 166.045 94.945  1.00 59.29  ? 294 ALA A O     1 
ATOM   5586 C  CB    . ALA B 2 294 ? 148.920 168.730 93.704  1.00 50.07  ? 294 ALA A CB    1 
ATOM   5587 N  N     . CYS B 2 295 ? 147.638 165.677 92.856  1.00 52.64  ? 295 CYS A N     1 
ATOM   5588 C  CA    . CYS B 2 295 ? 146.679 164.666 93.269  1.00 54.92  ? 295 CYS A CA    1 
ATOM   5589 C  C     . CYS B 2 295 ? 147.301 163.283 93.404  1.00 60.86  ? 295 CYS A C     1 
ATOM   5590 O  O     . CYS B 2 295 ? 146.643 162.373 93.917  1.00 58.90  ? 295 CYS A O     1 
ATOM   5591 C  CB    . CYS B 2 295 ? 145.512 164.619 92.283  1.00 53.80  ? 295 CYS A CB    1 
ATOM   5592 S  SG    . CYS B 2 295 ? 144.532 166.123 92.256  1.00 79.55  ? 295 CYS A SG    1 
ATOM   5593 N  N     . PHE B 2 296 ? 148.549 163.105 92.972  1.00 62.77  ? 296 PHE A N     1 
ATOM   5594 C  CA    . PHE B 2 296 ? 149.251 161.835 93.084  1.00 53.94  ? 296 PHE A CA    1 
ATOM   5595 C  C     . PHE B 2 296 ? 150.342 161.850 94.142  1.00 56.60  ? 296 PHE A C     1 
ATOM   5596 O  O     . PHE B 2 296 ? 151.027 160.840 94.317  1.00 61.22  ? 296 PHE A O     1 
ATOM   5597 C  CB    . PHE B 2 296 ? 149.860 161.446 91.736  1.00 50.79  ? 296 PHE A CB    1 
ATOM   5598 C  CG    . PHE B 2 296 ? 148.872 160.873 90.770  1.00 50.61  ? 296 PHE A CG    1 
ATOM   5599 C  CD1   . PHE B 2 296 ? 148.618 159.523 90.740  1.00 54.93  ? 296 PHE A CD1   1 
ATOM   5600 C  CD2   . PHE B 2 296 ? 148.197 161.691 89.889  1.00 53.55  ? 296 PHE A CD2   1 
ATOM   5601 C  CE1   . PHE B 2 296 ? 147.712 159.001 89.855  1.00 57.74  ? 296 PHE A CE1   1 
ATOM   5602 C  CE2   . PHE B 2 296 ? 147.288 161.170 89.000  1.00 53.89  ? 296 PHE A CE2   1 
ATOM   5603 C  CZ    . PHE B 2 296 ? 147.049 159.826 88.982  1.00 54.98  ? 296 PHE A CZ    1 
ATOM   5604 N  N     . GLU B 2 297 ? 150.530 162.965 94.838  1.00 65.59  ? 297 GLU A N     1 
ATOM   5605 C  CA    . GLU B 2 297 ? 151.497 163.004 95.921  1.00 64.38  ? 297 GLU A CA    1 
ATOM   5606 C  C     . GLU B 2 297 ? 151.007 162.147 97.085  1.00 68.22  ? 297 GLU A C     1 
ATOM   5607 O  O     . GLU B 2 297 ? 149.803 162.085 97.347  1.00 68.56  ? 297 GLU A O     1 
ATOM   5608 C  CB    . GLU B 2 297 ? 151.722 164.439 96.387  1.00 63.73  ? 297 GLU A CB    1 
ATOM   5609 C  CG    . GLU B 2 297 ? 152.428 165.312 95.372  1.00 69.26  ? 297 GLU A CG    1 
ATOM   5610 C  CD    . GLU B 2 297 ? 152.720 166.698 95.905  1.00 74.31  ? 297 GLU A CD    1 
ATOM   5611 O  OE1   . GLU B 2 297 ? 152.367 166.975 97.070  1.00 73.52  ? 297 GLU A OE1   1 
ATOM   5612 O  OE2   . GLU B 2 297 ? 153.303 167.513 95.159  1.00 71.79  ? 297 GLU A OE2   1 
ATOM   5613 N  N     . PRO B 2 298 ? 151.911 161.476 97.803  1.00 59.38  ? 298 PRO A N     1 
ATOM   5614 C  CA    . PRO B 2 298 ? 151.478 160.614 98.908  1.00 59.78  ? 298 PRO A CA    1 
ATOM   5615 C  C     . PRO B 2 298 ? 151.079 161.367 100.164 1.00 59.05  ? 298 PRO A C     1 
ATOM   5616 O  O     . PRO B 2 298 ? 150.515 160.749 101.076 1.00 65.00  ? 298 PRO A O     1 
ATOM   5617 C  CB    . PRO B 2 298 ? 152.703 159.730 99.164  1.00 60.94  ? 298 PRO A CB    1 
ATOM   5618 C  CG    . PRO B 2 298 ? 153.861 160.440 98.553  1.00 62.41  ? 298 PRO A CG    1 
ATOM   5619 C  CD    . PRO B 2 298 ? 153.375 161.572 97.706  1.00 59.35  ? 298 PRO A CD    1 
ATOM   5620 N  N     . ALA B 2 299 ? 151.346 162.668 100.247 1.00 60.83  ? 299 ALA A N     1 
ATOM   5621 C  CA    . ALA B 2 299 ? 150.979 163.458 101.411 1.00 61.80  ? 299 ALA A CA    1 
ATOM   5622 C  C     . ALA B 2 299 ? 149.629 164.148 101.273 1.00 64.17  ? 299 ALA A C     1 
ATOM   5623 O  O     . ALA B 2 299 ? 149.134 164.700 102.261 1.00 70.55  ? 299 ALA A O     1 
ATOM   5624 C  CB    . ALA B 2 299 ? 152.058 164.507 101.696 1.00 63.55  ? 299 ALA A CB    1 
ATOM   5625 N  N     . ASN B 2 300 ? 149.025 164.136 100.088 1.00 55.41  ? 300 ASN A N     1 
ATOM   5626 C  CA    . ASN B 2 300 ? 147.713 164.729 99.875  1.00 52.63  ? 300 ASN A CA    1 
ATOM   5627 C  C     . ASN B 2 300 ? 146.589 163.710 99.943  1.00 55.75  ? 300 ASN A C     1 
ATOM   5628 O  O     . ASN B 2 300 ? 145.437 164.061 99.680  1.00 61.18  ? 300 ASN A O     1 
ATOM   5629 C  CB    . ASN B 2 300 ? 147.663 165.452 98.527  1.00 57.40  ? 300 ASN A CB    1 
ATOM   5630 C  CG    . ASN B 2 300 ? 148.371 166.782 98.557  1.00 56.87  ? 300 ASN A CG    1 
ATOM   5631 O  OD1   . ASN B 2 300 ? 149.081 167.095 99.507  1.00 57.46  ? 300 ASN A OD1   1 
ATOM   5632 N  ND2   . ASN B 2 300 ? 148.183 167.574 97.513  1.00 57.37  ? 300 ASN A ND2   1 
ATOM   5633 N  N     . GLN B 2 301 ? 146.893 162.462 100.278 1.00 56.49  ? 301 GLN A N     1 
ATOM   5634 C  CA    . GLN B 2 301 ? 145.868 161.440 100.391 1.00 54.43  ? 301 GLN A CA    1 
ATOM   5635 C  C     . GLN B 2 301 ? 145.120 161.585 101.704 1.00 56.76  ? 301 GLN A C     1 
ATOM   5636 O  O     . GLN B 2 301 ? 145.710 161.889 102.743 1.00 61.96  ? 301 GLN A O     1 
ATOM   5637 C  CB    . GLN B 2 301 ? 146.484 160.049 100.284 1.00 57.19  ? 301 GLN A CB    1 
ATOM   5638 C  CG    . GLN B 2 301 ? 147.436 159.897 99.118  1.00 61.00  ? 301 GLN A CG    1 
ATOM   5639 C  CD    . GLN B 2 301 ? 146.728 159.942 97.780  1.00 64.77  ? 301 GLN A CD    1 
ATOM   5640 O  OE1   . GLN B 2 301 ? 145.543 159.633 97.682  1.00 66.28  ? 301 GLN A OE1   1 
ATOM   5641 N  NE2   . GLN B 2 301 ? 147.455 160.325 96.740  1.00 64.14  ? 301 GLN A NE2   1 
ATOM   5642 N  N     . MET B 2 302 ? 143.813 161.369 101.651 1.00 50.94  ? 302 MET A N     1 
ATOM   5643 C  CA    . MET B 2 302 ? 142.956 161.502 102.816 1.00 54.67  ? 302 MET A CA    1 
ATOM   5644 C  C     . MET B 2 302 ? 142.841 160.207 103.600 1.00 55.30  ? 302 MET A C     1 
ATOM   5645 O  O     . MET B 2 302 ? 141.964 160.093 104.460 1.00 62.80  ? 302 MET A O     1 
ATOM   5646 C  CB    . MET B 2 302 ? 141.575 161.998 102.393 1.00 56.06  ? 302 MET A CB    1 
ATOM   5647 C  CG    . MET B 2 302 ? 141.603 163.391 101.802 1.00 58.69  ? 302 MET A CG    1 
ATOM   5648 S  SD    . MET B 2 302 ? 140.049 164.281 101.936 1.00 71.49  ? 302 MET A SD    1 
ATOM   5649 C  CE    . MET B 2 302 ? 140.531 165.879 101.297 1.00 60.95  ? 302 MET A CE    1 
ATOM   5650 N  N     . VAL B 2 303 ? 143.684 159.226 103.301 1.00 53.46  ? 303 VAL A N     1 
ATOM   5651 C  CA    . VAL B 2 303 ? 143.855 158.038 104.121 1.00 50.21  ? 303 VAL A CA    1 
ATOM   5652 C  C     . VAL B 2 303 ? 145.345 157.881 104.376 1.00 56.32  ? 303 VAL A C     1 
ATOM   5653 O  O     . VAL B 2 303 ? 146.177 158.350 103.594 1.00 64.97  ? 303 VAL A O     1 
ATOM   5654 C  CB    . VAL B 2 303 ? 143.278 156.770 103.459 1.00 52.46  ? 303 VAL A CB    1 
ATOM   5655 C  CG1   . VAL B 2 303 ? 142.946 155.731 104.504 1.00 54.10  ? 303 VAL A CG1   1 
ATOM   5656 C  CG2   . VAL B 2 303 ? 142.062 157.102 102.620 1.00 55.97  ? 303 VAL A CG2   1 
ATOM   5657 N  N     . LYS B 2 304 ? 145.685 157.219 105.480 1.00 54.51  ? 304 LYS A N     1 
ATOM   5658 C  CA    . LYS B 2 304 ? 147.083 157.035 105.865 1.00 53.16  ? 304 LYS A CA    1 
ATOM   5659 C  C     . LYS B 2 304 ? 147.628 155.796 105.161 1.00 59.64  ? 304 LYS A C     1 
ATOM   5660 O  O     . LYS B 2 304 ? 147.774 154.718 105.741 1.00 65.02  ? 304 LYS A O     1 
ATOM   5661 C  CB    . LYS B 2 304 ? 147.211 156.924 107.376 1.00 60.22  ? 304 LYS A CB    1 
ATOM   5662 C  CG    . LYS B 2 304 ? 147.325 158.255 108.083 1.00 60.82  ? 304 LYS A CG    1 
ATOM   5663 C  CD    . LYS B 2 304 ? 148.594 158.978 107.690 1.00 59.66  ? 304 LYS A CD    1 
ATOM   5664 C  CE    . LYS B 2 304 ? 148.734 160.283 108.446 1.00 58.91  ? 304 LYS A CE    1 
ATOM   5665 N  NZ    . LYS B 2 304 ? 149.968 161.016 108.068 1.00 61.20  ? 304 LYS A NZ    1 
ATOM   5666 N  N     . CYS B 2 305 ? 147.939 155.962 103.879 1.00 61.11  ? 305 CYS A N     1 
ATOM   5667 C  CA    . CYS B 2 305 ? 148.461 154.863 103.071 1.00 58.84  ? 305 CYS A CA    1 
ATOM   5668 C  C     . CYS B 2 305 ? 149.169 155.456 101.867 1.00 67.16  ? 305 CYS A C     1 
ATOM   5669 O  O     . CYS B 2 305 ? 148.562 156.222 101.112 1.00 72.22  ? 305 CYS A O     1 
ATOM   5670 C  CB    . CYS B 2 305 ? 147.341 153.922 102.632 1.00 58.98  ? 305 CYS A CB    1 
ATOM   5671 S  SG    . CYS B 2 305 ? 145.945 154.727 101.828 1.00 74.47  ? 305 CYS A SG    1 
ATOM   5672 N  N     . ASP B 2 306 ? 150.441 155.121 101.687 1.00 68.81  ? 306 ASP A N     1 
ATOM   5673 C  CA    . ASP B 2 306 ? 151.179 155.632 100.541 1.00 64.88  ? 306 ASP A CA    1 
ATOM   5674 C  C     . ASP B 2 306 ? 150.929 154.740 99.334  1.00 61.98  ? 306 ASP A C     1 
ATOM   5675 O  O     . ASP B 2 306 ? 151.164 153.529 99.413  1.00 65.21  ? 306 ASP A O     1 
ATOM   5676 C  CB    . ASP B 2 306 ? 152.667 155.720 100.842 1.00 65.76  ? 306 ASP A CB    1 
ATOM   5677 C  CG    . ASP B 2 306 ? 153.240 154.413 101.335 1.00 74.55  ? 306 ASP A CG    1 
ATOM   5678 O  OD1   . ASP B 2 306 ? 152.522 153.675 102.041 1.00 76.58  ? 306 ASP A OD1   1 
ATOM   5679 O  OD2   . ASP B 2 306 ? 154.409 154.123 101.011 1.00 74.37  ? 306 ASP A OD2   1 
ATOM   5680 N  N     . PRO B 2 307 ? 150.438 155.280 98.218  1.00 58.71  ? 307 PRO A N     1 
ATOM   5681 C  CA    . PRO B 2 307 ? 150.165 154.437 97.046  1.00 59.49  ? 307 PRO A CA    1 
ATOM   5682 C  C     . PRO B 2 307 ? 151.408 153.865 96.397  1.00 64.64  ? 307 PRO A C     1 
ATOM   5683 O  O     . PRO B 2 307 ? 151.280 152.996 95.527  1.00 71.62  ? 307 PRO A O     1 
ATOM   5684 C  CB    . PRO B 2 307 ? 149.435 155.390 96.093  1.00 62.40  ? 307 PRO A CB    1 
ATOM   5685 C  CG    . PRO B 2 307 ? 148.927 156.489 96.966  1.00 65.32  ? 307 PRO A CG    1 
ATOM   5686 C  CD    . PRO B 2 307 ? 149.946 156.652 98.034  1.00 64.74  ? 307 PRO A CD    1 
ATOM   5687 N  N     . ARG B 2 308 ? 152.599 154.325 96.778  1.00 63.00  ? 308 ARG A N     1 
ATOM   5688 C  CA    . ARG B 2 308 ? 153.815 153.790 96.183  1.00 61.55  ? 308 ARG A CA    1 
ATOM   5689 C  C     . ARG B 2 308 ? 154.070 152.352 96.614  1.00 63.76  ? 308 ARG A C     1 
ATOM   5690 O  O     . ARG B 2 308 ? 154.756 151.608 95.906  1.00 67.06  ? 308 ARG A O     1 
ATOM   5691 C  CB    . ARG B 2 308 ? 155.001 154.683 96.532  1.00 59.71  ? 308 ARG A CB    1 
ATOM   5692 C  CG    . ARG B 2 308 ? 154.907 156.057 95.910  1.00 61.05  ? 308 ARG A CG    1 
ATOM   5693 C  CD    . ARG B 2 308 ? 156.012 156.972 96.386  1.00 62.67  ? 308 ARG A CD    1 
ATOM   5694 N  NE    . ARG B 2 308 ? 156.094 157.035 97.838  1.00 63.97  ? 308 ARG A NE    1 
ATOM   5695 C  CZ    . ARG B 2 308 ? 156.911 157.837 98.504  1.00 68.35  ? 308 ARG A CZ    1 
ATOM   5696 N  NH1   . ARG B 2 308 ? 157.718 158.676 97.878  1.00 66.55  ? 308 ARG A NH1   1 
ATOM   5697 N  NH2   . ARG B 2 308 ? 156.915 157.800 99.834  1.00 67.68  ? 308 ARG A NH2   1 
ATOM   5698 N  N     . HIS B 2 309 ? 153.535 151.944 97.759  1.00 60.30  ? 309 HIS A N     1 
ATOM   5699 C  CA    . HIS B 2 309 ? 153.552 150.540 98.165  1.00 57.44  ? 309 HIS A CA    1 
ATOM   5700 C  C     . HIS B 2 309 ? 152.347 149.798 97.598  1.00 60.77  ? 309 HIS A C     1 
ATOM   5701 O  O     . HIS B 2 309 ? 151.613 149.124 98.316  1.00 66.89  ? 309 HIS A O     1 
ATOM   5702 C  CB    . HIS B 2 309 ? 153.582 150.437 99.685  1.00 61.35  ? 309 HIS A CB    1 
ATOM   5703 C  CG    . HIS B 2 309 ? 154.838 150.958 100.307 1.00 65.09  ? 309 HIS A CG    1 
ATOM   5704 N  ND1   . HIS B 2 309 ? 154.872 151.491 101.577 1.00 65.70  ? 309 HIS A ND1   1 
ATOM   5705 C  CD2   . HIS B 2 309 ? 156.105 151.026 99.836  1.00 67.27  ? 309 HIS A CD2   1 
ATOM   5706 C  CE1   . HIS B 2 309 ? 156.106 151.863 101.862 1.00 66.30  ? 309 HIS A CE1   1 
ATOM   5707 N  NE2   . HIS B 2 309 ? 156.874 151.595 100.822 1.00 70.38  ? 309 HIS A NE2   1 
ATOM   5708 N  N     . GLY B 2 310 ? 152.135 149.916 96.296  1.00 50.40  ? 310 GLY A N     1 
ATOM   5709 C  CA    . GLY B 2 310 ? 150.967 149.314 95.684  1.00 49.29  ? 310 GLY A CA    1 
ATOM   5710 C  C     . GLY B 2 310 ? 150.893 149.679 94.221  1.00 52.70  ? 310 GLY A C     1 
ATOM   5711 O  O     . GLY B 2 310 ? 151.754 150.383 93.685  1.00 60.49  ? 310 GLY A O     1 
ATOM   5712 N  N     . LYS B 2 311 ? 149.841 149.188 93.578  1.00 48.57  ? 311 LYS A N     1 
ATOM   5713 C  CA    . LYS B 2 311 ? 149.616 149.409 92.159  1.00 49.17  ? 311 LYS A CA    1 
ATOM   5714 C  C     . LYS B 2 311 ? 148.216 149.958 91.946  1.00 53.18  ? 311 LYS A C     1 
ATOM   5715 O  O     . LYS B 2 311 ? 147.256 149.489 92.562  1.00 61.11  ? 311 LYS A O     1 
ATOM   5716 C  CB    . LYS B 2 311 ? 149.794 148.116 91.360  1.00 52.78  ? 311 LYS A CB    1 
ATOM   5717 C  CG    . LYS B 2 311 ? 150.986 147.287 91.781  1.00 55.34  ? 311 LYS A CG    1 
ATOM   5718 C  CD    . LYS B 2 311 ? 151.085 146.003 90.982  1.00 53.50  ? 311 LYS A CD    1 
ATOM   5719 C  CE    . LYS B 2 311 ? 151.796 146.218 89.670  1.00 56.32  ? 311 LYS A CE    1 
ATOM   5720 N  NZ    . LYS B 2 311 ? 153.197 146.659 89.885  1.00 58.79  ? 311 LYS A NZ    1 
ATOM   5721 N  N     . TYR B 2 312 ? 148.104 150.951 91.071  1.00 53.22  ? 312 TYR A N     1 
ATOM   5722 C  CA    . TYR B 2 312 ? 146.806 151.492 90.709  1.00 49.62  ? 312 TYR A CA    1 
ATOM   5723 C  C     . TYR B 2 312 ? 146.069 150.537 89.782  1.00 55.01  ? 312 TYR A C     1 
ATOM   5724 O  O     . TYR B 2 312 ? 146.677 149.821 88.983  1.00 62.91  ? 312 TYR A O     1 
ATOM   5725 C  CB    . TYR B 2 312 ? 146.950 152.846 90.020  1.00 51.60  ? 312 TYR A CB    1 
ATOM   5726 C  CG    . TYR B 2 312 ? 147.360 153.974 90.927  1.00 51.57  ? 312 TYR A CG    1 
ATOM   5727 C  CD1   . TYR B 2 312 ? 148.688 154.191 91.234  1.00 50.61  ? 312 TYR A CD1   1 
ATOM   5728 C  CD2   . TYR B 2 312 ? 146.419 154.828 91.469  1.00 51.59  ? 312 TYR A CD2   1 
ATOM   5729 C  CE1   . TYR B 2 312 ? 149.065 155.221 92.055  1.00 50.34  ? 312 TYR A CE1   1 
ATOM   5730 C  CE2   . TYR B 2 312 ? 146.788 155.858 92.290  1.00 52.10  ? 312 TYR A CE2   1 
ATOM   5731 C  CZ    . TYR B 2 312 ? 148.111 156.049 92.580  1.00 51.91  ? 312 TYR A CZ    1 
ATOM   5732 O  OH    . TYR B 2 312 ? 148.481 157.081 93.403  1.00 54.36  ? 312 TYR A OH    1 
ATOM   5733 N  N     . MET B 2 313 ? 144.745 150.537 89.889  1.00 52.71  ? 313 MET A N     1 
ATOM   5734 C  CA    . MET B 2 313 ? 143.889 149.761 89.004  1.00 49.72  ? 313 MET A CA    1 
ATOM   5735 C  C     . MET B 2 313 ? 143.100 150.639 88.047  1.00 52.18  ? 313 MET A C     1 
ATOM   5736 O  O     . MET B 2 313 ? 143.035 150.350 86.853  1.00 60.56  ? 313 MET A O     1 
ATOM   5737 C  CB    . MET B 2 313 ? 142.925 148.893 89.820  1.00 50.83  ? 313 MET A CB    1 
ATOM   5738 C  CG    . MET B 2 313 ? 143.585 148.027 90.866  1.00 52.40  ? 313 MET A CG    1 
ATOM   5739 S  SD    . MET B 2 313 ? 142.390 146.940 91.647  1.00 64.93  ? 313 MET A SD    1 
ATOM   5740 C  CE    . MET B 2 313 ? 143.153 146.675 93.240  1.00 60.18  ? 313 MET A CE    1 
ATOM   5741 N  N     . ALA B 2 314 ? 142.493 151.707 88.550  1.00 52.39  ? 314 ALA A N     1 
ATOM   5742 C  CA    . ALA B 2 314 ? 141.797 152.678 87.723  1.00 53.16  ? 314 ALA A CA    1 
ATOM   5743 C  C     . ALA B 2 314 ? 141.645 153.956 88.529  1.00 51.41  ? 314 ALA A C     1 
ATOM   5744 O  O     . ALA B 2 314 ? 141.582 153.919 89.758  1.00 57.25  ? 314 ALA A O     1 
ATOM   5745 C  CB    . ALA B 2 314 ? 140.428 152.163 87.274  1.00 52.53  ? 314 ALA A CB    1 
ATOM   5746 N  N     . CYS B 2 315 ? 141.592 155.085 87.833  1.00 47.07  ? 315 CYS A N     1 
ATOM   5747 C  CA    . CYS B 2 315 ? 141.362 156.362 88.490  1.00 48.68  ? 315 CYS A CA    1 
ATOM   5748 C  C     . CYS B 2 315 ? 140.478 157.236 87.615  1.00 49.95  ? 315 CYS A C     1 
ATOM   5749 O  O     . CYS B 2 315 ? 140.648 157.274 86.395  1.00 53.44  ? 315 CYS A O     1 
ATOM   5750 C  CB    . CYS B 2 315 ? 142.684 157.072 88.806  1.00 48.28  ? 315 CYS A CB    1 
ATOM   5751 S  SG    . CYS B 2 315 ? 143.943 156.926 87.542  1.00 65.70  ? 315 CYS A SG    1 
ATOM   5752 N  N     . CYS B 2 316 ? 139.530 157.931 88.241  1.00 46.41  ? 316 CYS A N     1 
ATOM   5753 C  CA    . CYS B 2 316 ? 138.635 158.855 87.553  1.00 45.63  ? 316 CYS A CA    1 
ATOM   5754 C  C     . CYS B 2 316 ? 138.943 160.271 88.010  1.00 45.70  ? 316 CYS A C     1 
ATOM   5755 O  O     . CYS B 2 316 ? 138.881 160.568 89.206  1.00 52.67  ? 316 CYS A O     1 
ATOM   5756 C  CB    . CYS B 2 316 ? 137.167 158.517 87.812  1.00 45.72  ? 316 CYS A CB    1 
ATOM   5757 S  SG    . CYS B 2 316 ? 136.742 158.265 89.546  1.00 73.07  ? 316 CYS A SG    1 
ATOM   5758 N  N     . LEU B 2 317 ? 139.265 161.137 87.059  1.00 43.06  ? 317 LEU A N     1 
ATOM   5759 C  CA    . LEU B 2 317 ? 139.635 162.515 87.334  1.00 40.67  ? 317 LEU A CA    1 
ATOM   5760 C  C     . LEU B 2 317 ? 138.479 163.435 86.972  1.00 48.44  ? 317 LEU A C     1 
ATOM   5761 O  O     . LEU B 2 317 ? 137.909 163.322 85.884  1.00 55.46  ? 317 LEU A O     1 
ATOM   5762 C  CB    . LEU B 2 317 ? 140.886 162.898 86.550  1.00 34.69  ? 317 LEU A CB    1 
ATOM   5763 C  CG    . LEU B 2 317 ? 142.196 162.458 87.182  1.00 42.24  ? 317 LEU A CG    1 
ATOM   5764 C  CD1   . LEU B 2 317 ? 143.282 162.450 86.157  1.00 44.68  ? 317 LEU A CD1   1 
ATOM   5765 C  CD2   . LEU B 2 317 ? 142.551 163.407 88.297  1.00 47.37  ? 317 LEU A CD2   1 
ATOM   5766 N  N     . LEU B 2 318 ? 138.134 164.336 87.885  1.00 42.87  ? 318 LEU A N     1 
ATOM   5767 C  CA    . LEU B 2 318 ? 136.987 165.224 87.735  1.00 37.73  ? 318 LEU A CA    1 
ATOM   5768 C  C     . LEU B 2 318 ? 137.463 166.665 87.823  1.00 40.87  ? 318 LEU A C     1 
ATOM   5769 O  O     . LEU B 2 318 ? 137.994 167.083 88.856  1.00 50.72  ? 318 LEU A O     1 
ATOM   5770 C  CB    . LEU B 2 318 ? 135.945 164.939 88.807  1.00 42.14  ? 318 LEU A CB    1 
ATOM   5771 C  CG    . LEU B 2 318 ? 135.364 163.533 88.806  1.00 38.31  ? 318 LEU A CG    1 
ATOM   5772 C  CD1   . LEU B 2 318 ? 134.292 163.426 89.857  1.00 40.53  ? 318 LEU A CD1   1 
ATOM   5773 C  CD2   . LEU B 2 318 ? 134.811 163.228 87.438  1.00 42.14  ? 318 LEU A CD2   1 
ATOM   5774 N  N     . TYR B 2 319 ? 137.255 167.428 86.757  1.00 36.64  ? 319 TYR A N     1 
ATOM   5775 C  CA    . TYR B 2 319 ? 137.672 168.819 86.696  1.00 33.57  ? 319 TYR A CA    1 
ATOM   5776 C  C     . TYR B 2 319 ? 136.458 169.735 86.674  1.00 39.38  ? 319 TYR A C     1 
ATOM   5777 O  O     . TYR B 2 319 ? 135.502 169.497 85.933  1.00 50.26  ? 319 TYR A O     1 
ATOM   5778 C  CB    . TYR B 2 319 ? 138.533 169.073 85.462  1.00 36.99  ? 319 TYR A CB    1 
ATOM   5779 C  CG    . TYR B 2 319 ? 139.871 168.387 85.481  1.00 30.94  ? 319 TYR A CG    1 
ATOM   5780 C  CD1   . TYR B 2 319 ? 140.031 167.120 84.955  1.00 38.87  ? 319 TYR A CD1   1 
ATOM   5781 C  CD2   . TYR B 2 319 ? 140.979 169.017 86.006  1.00 36.16  ? 319 TYR A CD2   1 
ATOM   5782 C  CE1   . TYR B 2 319 ? 141.253 166.500 84.965  1.00 38.36  ? 319 TYR A CE1   1 
ATOM   5783 C  CE2   . TYR B 2 319 ? 142.200 168.404 86.019  1.00 37.62  ? 319 TYR A CE2   1 
ATOM   5784 C  CZ    . TYR B 2 319 ? 142.332 167.147 85.503  1.00 35.21  ? 319 TYR A CZ    1 
ATOM   5785 O  OH    . TYR B 2 319 ? 143.559 166.540 85.520  1.00 45.28  ? 319 TYR A OH    1 
ATOM   5786 N  N     . ARG B 2 320 ? 136.495 170.779 87.496  1.00 32.41  ? 320 ARG A N     1 
ATOM   5787 C  CA    . ARG B 2 320 ? 135.456 171.796 87.479  1.00 36.67  ? 320 ARG A CA    1 
ATOM   5788 C  C     . ARG B 2 320 ? 136.111 173.166 87.429  1.00 41.48  ? 320 ARG A C     1 
ATOM   5789 O  O     . ARG B 2 320 ? 137.083 173.418 88.144  1.00 49.55  ? 320 ARG A O     1 
ATOM   5790 C  CB    . ARG B 2 320 ? 134.529 171.673 88.692  1.00 40.17  ? 320 ARG A CB    1 
ATOM   5791 C  CG    . ARG B 2 320 ? 135.229 171.547 90.018  1.00 46.12  ? 320 ARG A CG    1 
ATOM   5792 C  CD    . ARG B 2 320 ? 134.241 171.235 91.122  1.00 47.17  ? 320 ARG A CD    1 
ATOM   5793 N  NE    . ARG B 2 320 ? 133.148 172.197 91.176  1.00 45.60  ? 320 ARG A NE    1 
ATOM   5794 C  CZ    . ARG B 2 320 ? 132.149 172.147 92.047  1.00 47.73  ? 320 ARG A CZ    1 
ATOM   5795 N  NH1   . ARG B 2 320 ? 132.078 171.194 92.960  1.00 52.11  ? 320 ARG A NH1   1 
ATOM   5796 N  NH2   . ARG B 2 320 ? 131.199 173.074 91.999  1.00 44.74  ? 320 ARG A NH2   1 
ATOM   5797 N  N     . GLY B 2 321 ? 135.584 174.041 86.570  1.00 45.40  ? 321 GLY A N     1 
ATOM   5798 C  CA    . GLY B 2 321 ? 136.108 175.381 86.397  1.00 46.12  ? 321 GLY A CA    1 
ATOM   5799 C  C     . GLY B 2 321 ? 136.464 175.651 84.942  1.00 50.98  ? 321 GLY A C     1 
ATOM   5800 O  O     . GLY B 2 321 ? 135.753 175.228 84.024  1.00 54.70  ? 321 GLY A O     1 
ATOM   5801 N  N     . ASP B 2 322 ? 137.571 176.361 84.744  1.00 52.84  ? 322 ASP A N     1 
ATOM   5802 C  CA    . ASP B 2 322 ? 138.077 176.696 83.415  1.00 49.19  ? 322 ASP A CA    1 
ATOM   5803 C  C     . ASP B 2 322 ? 139.147 175.674 83.049  1.00 50.96  ? 322 ASP A C     1 
ATOM   5804 O  O     . ASP B 2 322 ? 140.331 175.865 83.318  1.00 54.61  ? 322 ASP A O     1 
ATOM   5805 C  CB    . ASP B 2 322 ? 138.624 178.117 83.391  1.00 57.03  ? 322 ASP A CB    1 
ATOM   5806 C  CG    . ASP B 2 322 ? 138.764 178.668 81.985  1.00 62.90  ? 322 ASP A CG    1 
ATOM   5807 O  OD1   . ASP B 2 322 ? 139.280 177.947 81.105  1.00 64.11  ? 322 ASP A OD1   1 
ATOM   5808 O  OD2   . ASP B 2 322 ? 138.356 179.826 81.757  1.00 61.42  ? 322 ASP A OD2   1 
ATOM   5809 N  N     . VAL B 2 323 ? 138.720 174.577 82.430  1.00 47.19  ? 323 VAL A N     1 
ATOM   5810 C  CA    . VAL B 2 323 ? 139.610 173.503 82.009  1.00 41.57  ? 323 VAL A CA    1 
ATOM   5811 C  C     . VAL B 2 323 ? 139.335 173.204 80.545  1.00 47.55  ? 323 VAL A C     1 
ATOM   5812 O  O     . VAL B 2 323 ? 138.185 173.264 80.096  1.00 54.39  ? 323 VAL A O     1 
ATOM   5813 C  CB    . VAL B 2 323 ? 139.424 172.232 82.865  1.00 46.96  ? 323 VAL A CB    1 
ATOM   5814 C  CG1   . VAL B 2 323 ? 140.564 171.260 82.627  1.00 52.31  ? 323 VAL A CG1   1 
ATOM   5815 C  CG2   . VAL B 2 323 ? 139.323 172.582 84.330  1.00 46.54  ? 323 VAL A CG2   1 
ATOM   5816 N  N     . VAL B 2 324 ? 140.388 172.890 79.799  1.00 56.31  ? 324 VAL A N     1 
ATOM   5817 C  CA    . VAL B 2 324 ? 140.277 172.539 78.385  1.00 52.45  ? 324 VAL A CA    1 
ATOM   5818 C  C     . VAL B 2 324 ? 140.800 171.117 78.210  1.00 57.15  ? 324 VAL A C     1 
ATOM   5819 O  O     . VAL B 2 324 ? 141.791 170.744 78.854  1.00 64.32  ? 324 VAL A O     1 
ATOM   5820 C  CB    . VAL B 2 324 ? 141.048 173.538 77.509  1.00 52.61  ? 324 VAL A CB    1 
ATOM   5821 C  CG1   . VAL B 2 324 ? 140.675 173.378 76.052  1.00 55.86  ? 324 VAL A CG1   1 
ATOM   5822 C  CG2   . VAL B 2 324 ? 140.790 174.956 77.973  1.00 52.45  ? 324 VAL A CG2   1 
ATOM   5823 N  N     . PRO B 2 325 ? 140.168 170.290 77.374  1.00 47.97  ? 325 PRO A N     1 
ATOM   5824 C  CA    . PRO B 2 325 ? 140.606 168.889 77.255  1.00 47.33  ? 325 PRO A CA    1 
ATOM   5825 C  C     . PRO B 2 325 ? 142.050 168.697 76.819  1.00 50.02  ? 325 PRO A C     1 
ATOM   5826 O  O     . PRO B 2 325 ? 142.664 167.688 77.196  1.00 58.21  ? 325 PRO A O     1 
ATOM   5827 C  CB    . PRO B 2 325 ? 139.625 168.319 76.228  1.00 51.40  ? 325 PRO A CB    1 
ATOM   5828 C  CG    . PRO B 2 325 ? 138.391 169.104 76.447  1.00 53.64  ? 325 PRO A CG    1 
ATOM   5829 C  CD    . PRO B 2 325 ? 138.829 170.494 76.802  1.00 48.44  ? 325 PRO A CD    1 
ATOM   5830 N  N     . LYS B 2 326 ? 142.612 169.615 76.032  1.00 43.80  ? 326 LYS A N     1 
ATOM   5831 C  CA    . LYS B 2 326 ? 144.006 169.480 75.621  1.00 45.32  ? 326 LYS A CA    1 
ATOM   5832 C  C     . LYS B 2 326 ? 144.933 169.438 76.831  1.00 54.23  ? 326 LYS A C     1 
ATOM   5833 O  O     . LYS B 2 326 ? 145.865 168.622 76.890  1.00 60.38  ? 326 LYS A O     1 
ATOM   5834 C  CB    . LYS B 2 326 ? 144.385 170.634 74.689  1.00 49.48  ? 326 LYS A CB    1 
ATOM   5835 C  CG    . LYS B 2 326 ? 143.370 170.903 73.578  1.00 55.41  ? 326 LYS A CG    1 
ATOM   5836 C  CD    . LYS B 2 326 ? 143.687 172.172 72.779  1.00 60.41  ? 326 LYS A CD    1 
ATOM   5837 C  CE    . LYS B 2 326 ? 142.647 172.411 71.673  1.00 57.16  ? 326 LYS A CE    1 
ATOM   5838 N  NZ    . LYS B 2 326 ? 142.876 173.649 70.856  1.00 32.12  ? 326 LYS A NZ    1 
ATOM   5839 N  N     . ASP B 2 327 ? 144.683 170.307 77.812  1.00 48.26  ? 327 ASP A N     1 
ATOM   5840 C  CA    . ASP B 2 327 ? 145.503 170.334 79.015  1.00 45.87  ? 327 ASP A CA    1 
ATOM   5841 C  C     . ASP B 2 327 ? 145.366 169.043 79.806  1.00 48.95  ? 327 ASP A C     1 
ATOM   5842 O  O     . ASP B 2 327 ? 146.346 168.546 80.373  1.00 55.39  ? 327 ASP A O     1 
ATOM   5843 C  CB    . ASP B 2 327 ? 145.122 171.535 79.873  1.00 53.62  ? 327 ASP A CB    1 
ATOM   5844 C  CG    . ASP B 2 327 ? 145.470 172.851 79.215  1.00 59.77  ? 327 ASP A CG    1 
ATOM   5845 O  OD1   . ASP B 2 327 ? 146.476 172.899 78.479  1.00 60.19  ? 327 ASP A OD1   1 
ATOM   5846 O  OD2   . ASP B 2 327 ? 144.736 173.838 79.432  1.00 58.23  ? 327 ASP A OD2   1 
ATOM   5847 N  N     . VAL B 2 328 ? 144.157 168.487 79.863  1.00 47.04  ? 328 VAL A N     1 
ATOM   5848 C  CA    . VAL B 2 328 ? 143.957 167.221 80.555  1.00 40.62  ? 328 VAL A CA    1 
ATOM   5849 C  C     . VAL B 2 328 ? 144.747 166.116 79.874  1.00 48.71  ? 328 VAL A C     1 
ATOM   5850 O  O     . VAL B 2 328 ? 145.351 165.269 80.539  1.00 55.10  ? 328 VAL A O     1 
ATOM   5851 C  CB    . VAL B 2 328 ? 142.461 166.882 80.630  1.00 42.45  ? 328 VAL A CB    1 
ATOM   5852 C  CG1   . VAL B 2 328 ? 142.262 165.504 81.225  1.00 48.25  ? 328 VAL A CG1   1 
ATOM   5853 C  CG2   . VAL B 2 328 ? 141.740 167.922 81.442  1.00 48.09  ? 328 VAL A CG2   1 
ATOM   5854 N  N     . ASN B 2 329 ? 144.748 166.096 78.541  1.00 44.34  ? 329 ASN A N     1 
ATOM   5855 C  CA    . ASN B 2 329 ? 145.513 165.078 77.830  1.00 34.18  ? 329 ASN A CA    1 
ATOM   5856 C  C     . ASN B 2 329 ? 147.003 165.216 78.103  1.00 37.13  ? 329 ASN A C     1 
ATOM   5857 O  O     . ASN B 2 329 ? 147.695 164.216 78.328  1.00 48.75  ? 329 ASN A O     1 
ATOM   5858 C  CB    . ASN B 2 329 ? 145.235 165.159 76.334  1.00 42.33  ? 329 ASN A CB    1 
ATOM   5859 C  CG    . ASN B 2 329 ? 143.879 164.616 75.969  1.00 48.25  ? 329 ASN A CG    1 
ATOM   5860 O  OD1   . ASN B 2 329 ? 143.382 163.686 76.600  1.00 51.58  ? 329 ASN A OD1   1 
ATOM   5861 N  ND2   . ASN B 2 329 ? 143.265 165.196 74.949  1.00 45.83  ? 329 ASN A ND2   1 
ATOM   5862 N  N     . ALA B 2 330 ? 147.514 166.448 78.094  1.00 32.34  ? 330 ALA A N     1 
ATOM   5863 C  CA    . ALA B 2 330 ? 148.925 166.654 78.408  1.00 31.04  ? 330 ALA A CA    1 
ATOM   5864 C  C     . ALA B 2 330 ? 149.254 166.195 79.826  1.00 43.16  ? 330 ALA A C     1 
ATOM   5865 O  O     . ALA B 2 330 ? 150.282 165.542 80.056  1.00 50.22  ? 330 ALA A O     1 
ATOM   5866 C  CB    . ALA B 2 330 ? 149.297 168.121 78.216  1.00 38.04  ? 330 ALA A CB    1 
ATOM   5867 N  N     . ALA B 2 331 ? 148.388 166.517 80.791  1.00 43.04  ? 331 ALA A N     1 
ATOM   5868 C  CA    . ALA B 2 331 ? 148.623 166.105 82.171  1.00 35.87  ? 331 ALA A CA    1 
ATOM   5869 C  C     . ALA B 2 331 ? 148.589 164.589 82.315  1.00 40.70  ? 331 ALA A C     1 
ATOM   5870 O  O     . ALA B 2 331 ? 149.410 164.007 83.036  1.00 46.67  ? 331 ALA A O     1 
ATOM   5871 C  CB    . ALA B 2 331 ? 147.594 166.754 83.092  1.00 42.73  ? 331 ALA A CB    1 
ATOM   5872 N  N     . ILE B 2 332 ? 147.645 163.933 81.641  1.00 37.70  ? 332 ILE A N     1 
ATOM   5873 C  CA    . ILE B 2 332 ? 147.565 162.477 81.684  1.00 36.29  ? 332 ILE A CA    1 
ATOM   5874 C  C     . ILE B 2 332 ? 148.825 161.860 81.099  1.00 38.60  ? 332 ILE A C     1 
ATOM   5875 O  O     . ILE B 2 332 ? 149.363 160.887 81.638  1.00 46.56  ? 332 ILE A O     1 
ATOM   5876 C  CB    . ILE B 2 332 ? 146.304 161.991 80.949  1.00 41.80  ? 332 ILE A CB    1 
ATOM   5877 C  CG1   . ILE B 2 332 ? 145.051 162.392 81.718  1.00 34.49  ? 332 ILE A CG1   1 
ATOM   5878 C  CG2   . ILE B 2 332 ? 146.340 160.489 80.771  1.00 46.56  ? 332 ILE A CG2   1 
ATOM   5879 C  CD1   . ILE B 2 332 ? 145.083 161.982 83.145  1.00 43.01  ? 332 ILE A CD1   1 
ATOM   5880 N  N     . ALA B 2 333 ? 149.314 162.410 79.986  1.00 35.81  ? 333 ALA A N     1 
ATOM   5881 C  CA    . ALA B 2 333 ? 150.538 161.888 79.387  1.00 34.96  ? 333 ALA A CA    1 
ATOM   5882 C  C     . ALA B 2 333 ? 151.724 162.037 80.333  1.00 37.95  ? 333 ALA A C     1 
ATOM   5883 O  O     . ALA B 2 333 ? 152.523 161.103 80.494  1.00 42.49  ? 333 ALA A O     1 
ATOM   5884 C  CB    . ALA B 2 333 ? 150.817 162.596 78.066  1.00 37.77  ? 333 ALA A CB    1 
ATOM   5885 N  N     . THR B 2 334 ? 151.850 163.199 80.979  1.00 44.24  ? 334 THR A N     1 
ATOM   5886 C  CA    . THR B 2 334 ? 152.956 163.395 81.912  1.00 42.76  ? 334 THR A CA    1 
ATOM   5887 C  C     . THR B 2 334 ? 152.867 162.433 83.090  1.00 46.27  ? 334 THR A C     1 
ATOM   5888 O  O     . THR B 2 334 ? 153.886 161.890 83.531  1.00 48.65  ? 334 THR A O     1 
ATOM   5889 C  CB    . THR B 2 334 ? 152.996 164.839 82.410  1.00 49.18  ? 334 THR A CB    1 
ATOM   5890 O  OG1   . THR B 2 334 ? 151.698 165.223 82.880  1.00 52.92  ? 334 THR A OG1   1 
ATOM   5891 C  CG2   . THR B 2 334 ? 153.431 165.775 81.299  1.00 46.12  ? 334 THR A CG2   1 
ATOM   5892 N  N     . ILE B 2 335 ? 151.662 162.214 83.619  1.00 48.74  ? 335 ILE A N     1 
ATOM   5893 C  CA    . ILE B 2 335 ? 151.502 161.266 84.719  1.00 43.65  ? 335 ILE A CA    1 
ATOM   5894 C  C     . ILE B 2 335 ? 151.875 159.863 84.267  1.00 40.62  ? 335 ILE A C     1 
ATOM   5895 O  O     . ILE B 2 335 ? 152.544 159.116 84.990  1.00 49.82  ? 335 ILE A O     1 
ATOM   5896 C  CB    . ILE B 2 335 ? 150.067 161.317 85.273  1.00 46.12  ? 335 ILE A CB    1 
ATOM   5897 C  CG1   . ILE B 2 335 ? 149.878 162.545 86.160  1.00 50.86  ? 335 ILE A CG1   1 
ATOM   5898 C  CG2   . ILE B 2 335 ? 149.751 160.061 86.046  1.00 42.84  ? 335 ILE A CG2   1 
ATOM   5899 C  CD1   . ILE B 2 335 ? 150.731 162.529 87.398  1.00 50.78  ? 335 ILE A CD1   1 
ATOM   5900 N  N     . LYS B 2 336 ? 151.459 159.487 83.060  1.00 44.29  ? 336 LYS A N     1 
ATOM   5901 C  CA    . LYS B 2 336 ? 151.743 158.151 82.552  1.00 44.04  ? 336 LYS A CA    1 
ATOM   5902 C  C     . LYS B 2 336 ? 153.231 157.943 82.308  1.00 44.20  ? 336 LYS A C     1 
ATOM   5903 O  O     . LYS B 2 336 ? 153.710 156.806 82.355  1.00 46.98  ? 336 LYS A O     1 
ATOM   5904 C  CB    . LYS B 2 336 ? 150.954 157.914 81.267  1.00 43.70  ? 336 LYS A CB    1 
ATOM   5905 C  CG    . LYS B 2 336 ? 150.674 156.466 80.982  1.00 51.03  ? 336 LYS A CG    1 
ATOM   5906 C  CD    . LYS B 2 336 ? 149.208 156.149 81.183  1.00 50.89  ? 336 LYS A CD    1 
ATOM   5907 C  CE    . LYS B 2 336 ? 148.366 156.791 80.101  1.00 47.02  ? 336 LYS A CE    1 
ATOM   5908 N  NZ    . LYS B 2 336 ? 146.973 156.275 80.116  1.00 51.41  ? 336 LYS A NZ    1 
ATOM   5909 N  N     . THR B 2 337 ? 153.971 159.016 82.030  1.00 53.29  ? 337 THR A N     1 
ATOM   5910 C  CA    . THR B 2 337 ? 155.408 158.906 81.805  1.00 52.76  ? 337 THR A CA    1 
ATOM   5911 C  C     . THR B 2 337 ? 156.183 158.483 83.048  1.00 54.61  ? 337 THR A C     1 
ATOM   5912 O  O     . THR B 2 337 ? 157.145 157.718 82.925  1.00 56.16  ? 337 THR A O     1 
ATOM   5913 C  CB    . THR B 2 337 ? 155.949 160.241 81.278  1.00 57.38  ? 337 THR A CB    1 
ATOM   5914 O  OG1   . THR B 2 337 ? 155.739 160.317 79.863  1.00 58.66  ? 337 THR A OG1   1 
ATOM   5915 C  CG2   . THR B 2 337 ? 157.429 160.398 81.572  1.00 55.62  ? 337 THR A CG2   1 
ATOM   5916 N  N     . LYS B 2 338 ? 155.772 158.923 84.234  1.00 66.00  ? 338 LYS A N     1 
ATOM   5917 C  CA    . LYS B 2 338 ? 156.548 158.730 85.450  1.00 61.82  ? 338 LYS A CA    1 
ATOM   5918 C  C     . LYS B 2 338 ? 156.692 157.248 85.787  1.00 61.66  ? 338 LYS A C     1 
ATOM   5919 O  O     . LYS B 2 338 ? 155.949 156.391 85.304  1.00 65.82  ? 338 LYS A O     1 
ATOM   5920 C  CB    . LYS B 2 338 ? 155.903 159.468 86.618  1.00 60.52  ? 338 LYS A CB    1 
ATOM   5921 C  CG    . LYS B 2 338 ? 156.243 160.939 86.671  1.00 63.59  ? 338 LYS A CG    1 
ATOM   5922 C  CD    . LYS B 2 338 ? 155.637 161.595 87.891  1.00 64.60  ? 338 LYS A CD    1 
ATOM   5923 C  CE    . LYS B 2 338 ? 156.099 163.033 88.026  1.00 67.20  ? 338 LYS A CE    1 
ATOM   5924 N  NZ    . LYS B 2 338 ? 155.780 163.833 86.811  1.00 67.29  ? 338 LYS A NZ    1 
ATOM   5925 N  N     . ARG B 2 339 ? 157.671 156.956 86.640  1.00 68.56  ? 339 ARG A N     1 
ATOM   5926 C  CA    . ARG B 2 339 ? 157.988 155.595 87.046  1.00 67.70  ? 339 ARG A CA    1 
ATOM   5927 C  C     . ARG B 2 339 ? 157.479 155.235 88.431  1.00 70.32  ? 339 ARG A C     1 
ATOM   5928 O  O     . ARG B 2 339 ? 157.123 154.080 88.660  1.00 71.64  ? 339 ARG A O     1 
ATOM   5929 C  CB    . ARG B 2 339 ? 159.504 155.369 87.008  1.00 71.99  ? 339 ARG A CB    1 
ATOM   5930 C  CG    . ARG B 2 339 ? 160.189 155.918 85.767  1.00 71.76  ? 339 ARG A CG    1 
ATOM   5931 C  CD    . ARG B 2 339 ? 159.600 155.325 84.498  1.00 73.20  ? 339 ARG A CD    1 
ATOM   5932 N  NE    . ARG B 2 339 ? 159.735 153.874 84.460  1.00 78.26  ? 339 ARG A NE    1 
ATOM   5933 C  CZ    . ARG B 2 339 ? 159.308 153.108 83.465  1.00 78.39  ? 339 ARG A CZ    1 
ATOM   5934 N  NH1   . ARG B 2 339 ? 158.710 153.624 82.404  1.00 75.74  ? 339 ARG A NH1   1 
ATOM   5935 N  NH2   . ARG B 2 339 ? 159.486 151.792 83.536  1.00 74.42  ? 339 ARG A NH2   1 
ATOM   5936 N  N     . SER B 2 340 ? 157.436 156.193 89.359  1.00 64.93  ? 340 SER A N     1 
ATOM   5937 C  CA    . SER B 2 340 ? 156.946 155.932 90.706  1.00 60.45  ? 340 SER A CA    1 
ATOM   5938 C  C     . SER B 2 340 ? 155.461 155.605 90.744  1.00 65.51  ? 340 SER A C     1 
ATOM   5939 O  O     . SER B 2 340 ? 154.983 155.090 91.759  1.00 67.37  ? 340 SER A O     1 
ATOM   5940 C  CB    . SER B 2 340 ? 157.229 157.132 91.607  1.00 62.21  ? 340 SER A CB    1 
ATOM   5941 O  OG    . SER B 2 340 ? 156.527 158.278 91.162  1.00 65.95  ? 340 SER A OG    1 
ATOM   5942 N  N     . ILE B 2 341 ? 154.727 155.881 89.673  1.00 56.88  ? 341 ILE A N     1 
ATOM   5943 C  CA    . ILE B 2 341 ? 153.309 155.570 89.578  1.00 52.15  ? 341 ILE A CA    1 
ATOM   5944 C  C     . ILE B 2 341 ? 153.161 154.284 88.775  1.00 57.23  ? 341 ILE A C     1 
ATOM   5945 O  O     . ILE B 2 341 ? 153.555 154.226 87.605  1.00 61.84  ? 341 ILE A O     1 
ATOM   5946 C  CB    . ILE B 2 341 ? 152.533 156.725 88.931  1.00 59.50  ? 341 ILE A CB    1 
ATOM   5947 C  CG1   . ILE B 2 341 ? 152.703 157.995 89.762  1.00 61.58  ? 341 ILE A CG1   1 
ATOM   5948 C  CG2   . ILE B 2 341 ? 151.067 156.382 88.806  1.00 61.09  ? 341 ILE A CG2   1 
ATOM   5949 C  CD1   . ILE B 2 341 ? 152.259 159.246 89.054  1.00 59.08  ? 341 ILE A CD1   1 
ATOM   5950 N  N     . GLN B 2 342 ? 152.593 153.256 89.398  1.00 58.06  ? 342 GLN A N     1 
ATOM   5951 C  CA    . GLN B 2 342 ? 152.470 151.931 88.806  1.00 56.60  ? 342 GLN A CA    1 
ATOM   5952 C  C     . GLN B 2 342 ? 151.015 151.620 88.491  1.00 57.05  ? 342 GLN A C     1 
ATOM   5953 O  O     . GLN B 2 342 ? 150.118 151.934 89.279  1.00 65.72  ? 342 GLN A O     1 
ATOM   5954 C  CB    . GLN B 2 342 ? 153.024 150.856 89.744  1.00 59.72  ? 342 GLN A CB    1 
ATOM   5955 C  CG    . GLN B 2 342 ? 154.534 150.815 89.846  1.00 61.60  ? 342 GLN A CG    1 
ATOM   5956 C  CD    . GLN B 2 342 ? 155.185 150.346 88.565  1.00 68.96  ? 342 GLN A CD    1 
ATOM   5957 O  OE1   . GLN B 2 342 ? 154.601 149.571 87.809  1.00 70.31  ? 342 GLN A OE1   1 
ATOM   5958 N  NE2   . GLN B 2 342 ? 156.400 150.818 88.310  1.00 68.02  ? 342 GLN A NE2   1 
ATOM   5959 N  N     . PHE B 2 343 ? 150.789 150.997 87.341  1.00 46.03  ? 343 PHE A N     1 
ATOM   5960 C  CA    . PHE B 2 343 ? 149.474 150.536 86.930  1.00 43.83  ? 343 PHE A CA    1 
ATOM   5961 C  C     . PHE B 2 343 ? 149.528 149.045 86.640  1.00 53.80  ? 343 PHE A C     1 
ATOM   5962 O  O     . PHE B 2 343 ? 150.553 148.521 86.197  1.00 60.65  ? 343 PHE A O     1 
ATOM   5963 C  CB    . PHE B 2 343 ? 148.978 151.287 85.694  1.00 51.87  ? 343 PHE A CB    1 
ATOM   5964 C  CG    . PHE B 2 343 ? 148.286 152.573 86.009  1.00 55.77  ? 343 PHE A CG    1 
ATOM   5965 C  CD1   . PHE B 2 343 ? 149.004 153.679 86.419  1.00 57.08  ? 343 PHE A CD1   1 
ATOM   5966 C  CD2   . PHE B 2 343 ? 146.914 152.675 85.906  1.00 55.74  ? 343 PHE A CD2   1 
ATOM   5967 C  CE1   . PHE B 2 343 ? 148.367 154.860 86.713  1.00 56.60  ? 343 PHE A CE1   1 
ATOM   5968 C  CE2   . PHE B 2 343 ? 146.275 153.851 86.202  1.00 53.86  ? 343 PHE A CE2   1 
ATOM   5969 C  CZ    . PHE B 2 343 ? 147.002 154.945 86.607  1.00 53.86  ? 343 PHE A CZ    1 
ATOM   5970 N  N     . VAL B 2 344 ? 148.415 148.361 86.895  1.00 52.45  ? 344 VAL A N     1 
ATOM   5971 C  CA    . VAL B 2 344 ? 148.371 146.924 86.685  1.00 46.55  ? 344 VAL A CA    1 
ATOM   5972 C  C     . VAL B 2 344 ? 148.448 146.620 85.195  1.00 57.75  ? 344 VAL A C     1 
ATOM   5973 O  O     . VAL B 2 344 ? 148.000 147.405 84.349  1.00 63.23  ? 344 VAL A O     1 
ATOM   5974 C  CB    . VAL B 2 344 ? 147.105 146.318 87.313  1.00 47.13  ? 344 VAL A CB    1 
ATOM   5975 C  CG1   . VAL B 2 344 ? 147.279 146.190 88.803  1.00 52.74  ? 344 VAL A CG1   1 
ATOM   5976 C  CG2   . VAL B 2 344 ? 145.900 147.177 86.997  1.00 49.49  ? 344 VAL A CG2   1 
ATOM   5977 N  N     . ASP B 2 345 ? 149.028 145.465 84.869  1.00 62.90  ? 345 ASP A N     1 
ATOM   5978 C  CA    . ASP B 2 345 ? 149.276 145.122 83.476  1.00 56.32  ? 345 ASP A CA    1 
ATOM   5979 C  C     . ASP B 2 345 ? 147.999 144.843 82.699  1.00 51.73  ? 345 ASP A C     1 
ATOM   5980 O  O     . ASP B 2 345 ? 148.037 144.829 81.465  1.00 58.10  ? 345 ASP A O     1 
ATOM   5981 C  CB    . ASP B 2 345 ? 150.205 143.913 83.391  1.00 55.96  ? 345 ASP A CB    1 
ATOM   5982 C  CG    . ASP B 2 345 ? 149.745 142.765 84.262  1.00 62.73  ? 345 ASP A CG    1 
ATOM   5983 O  OD1   . ASP B 2 345 ? 148.771 142.947 85.022  1.00 64.27  ? 345 ASP A OD1   1 
ATOM   5984 O  OD2   . ASP B 2 345 ? 150.355 141.678 84.187  1.00 63.44  ? 345 ASP A OD2   1 
ATOM   5985 N  N     . TRP B 2 346 ? 146.875 144.626 83.374  1.00 42.16  ? 346 TRP A N     1 
ATOM   5986 C  CA    . TRP B 2 346 ? 145.639 144.289 82.689  1.00 48.24  ? 346 TRP A CA    1 
ATOM   5987 C  C     . TRP B 2 346 ? 144.713 145.482 82.510  1.00 53.15  ? 346 TRP A C     1 
ATOM   5988 O  O     . TRP B 2 346 ? 143.548 145.299 82.145  1.00 56.41  ? 346 TRP A O     1 
ATOM   5989 C  CB    . TRP B 2 346 ? 144.912 143.162 83.421  1.00 46.79  ? 346 TRP A CB    1 
ATOM   5990 C  CG    . TRP B 2 346 ? 144.794 143.338 84.891  1.00 45.78  ? 346 TRP A CG    1 
ATOM   5991 C  CD1   . TRP B 2 346 ? 145.639 142.861 85.836  1.00 51.84  ? 346 TRP A CD1   1 
ATOM   5992 C  CD2   . TRP B 2 346 ? 143.752 144.022 85.592  1.00 48.95  ? 346 TRP A CD2   1 
ATOM   5993 N  NE1   . TRP B 2 346 ? 145.198 143.209 87.085  1.00 50.30  ? 346 TRP A NE1   1 
ATOM   5994 C  CE2   . TRP B 2 346 ? 144.039 143.925 86.961  1.00 45.45  ? 346 TRP A CE2   1 
ATOM   5995 C  CE3   . TRP B 2 346 ? 142.606 144.711 85.192  1.00 52.78  ? 346 TRP A CE3   1 
ATOM   5996 C  CZ2   . TRP B 2 346 ? 143.226 144.487 87.932  1.00 47.42  ? 346 TRP A CZ2   1 
ATOM   5997 C  CZ3   . TRP B 2 346 ? 141.802 145.269 86.159  1.00 49.87  ? 346 TRP A CZ3   1 
ATOM   5998 C  CH2   . TRP B 2 346 ? 142.115 145.155 87.511  1.00 49.19  ? 346 TRP A CH2   1 
ATOM   5999 N  N     . CYS B 2 347 ? 145.195 146.696 82.756  1.00 52.53  ? 347 CYS A N     1 
ATOM   6000 C  CA    . CYS B 2 347 ? 144.416 147.917 82.556  1.00 49.33  ? 347 CYS A CA    1 
ATOM   6001 C  C     . CYS B 2 347 ? 145.259 148.900 81.759  1.00 51.13  ? 347 CYS A C     1 
ATOM   6002 O  O     . CYS B 2 347 ? 145.784 149.875 82.312  1.00 54.66  ? 347 CYS A O     1 
ATOM   6003 C  CB    . CYS B 2 347 ? 143.978 148.520 83.889  1.00 48.70  ? 347 CYS A CB    1 
ATOM   6004 S  SG    . CYS B 2 347 ? 142.773 149.843 83.730  1.00 66.25  ? 347 CYS A SG    1 
ATOM   6005 N  N     . PRO B 2 348 ? 145.419 148.670 80.455  1.00 46.87  ? 348 PRO A N     1 
ATOM   6006 C  CA    . PRO B 2 348 ? 146.270 149.562 79.656  1.00 44.56  ? 348 PRO A CA    1 
ATOM   6007 C  C     . PRO B 2 348 ? 145.788 150.997 79.627  1.00 49.78  ? 348 PRO A C     1 
ATOM   6008 O  O     . PRO B 2 348 ? 146.610 151.918 79.556  1.00 57.19  ? 348 PRO A O     1 
ATOM   6009 C  CB    . PRO B 2 348 ? 146.229 148.921 78.266  1.00 43.60  ? 348 PRO A CB    1 
ATOM   6010 C  CG    . PRO B 2 348 ? 144.968 148.162 78.245  1.00 43.17  ? 348 PRO A CG    1 
ATOM   6011 C  CD    . PRO B 2 348 ? 144.778 147.639 79.627  1.00 51.61  ? 348 PRO A CD    1 
ATOM   6012 N  N     . THR B 2 349 ? 144.481 151.217 79.676  1.00 49.27  ? 349 THR A N     1 
ATOM   6013 C  CA    . THR B 2 349 ? 143.891 152.548 79.746  1.00 49.13  ? 349 THR A CA    1 
ATOM   6014 C  C     . THR B 2 349 ? 143.268 152.703 81.125  1.00 52.86  ? 349 THR A C     1 
ATOM   6015 O  O     . THR B 2 349 ? 142.259 152.058 81.428  1.00 59.90  ? 349 THR A O     1 
ATOM   6016 C  CB    . THR B 2 349 ? 142.846 152.732 78.654  1.00 50.62  ? 349 THR A CB    1 
ATOM   6017 O  OG1   . THR B 2 349 ? 141.872 151.688 78.759  1.00 49.02  ? 349 THR A OG1   1 
ATOM   6018 C  CG2   . THR B 2 349 ? 143.495 152.674 77.281  1.00 50.44  ? 349 THR A CG2   1 
ATOM   6019 N  N     . GLY B 2 350 ? 143.856 153.556 81.956  1.00 43.14  ? 350 GLY A N     1 
ATOM   6020 C  CA    . GLY B 2 350 ? 143.417 153.623 83.334  1.00 42.89  ? 350 GLY A CA    1 
ATOM   6021 C  C     . GLY B 2 350 ? 142.947 154.979 83.806  1.00 48.49  ? 350 GLY A C     1 
ATOM   6022 O  O     . GLY B 2 350 ? 143.241 155.371 84.937  1.00 51.73  ? 350 GLY A O     1 
ATOM   6023 N  N     . PHE B 2 351 ? 142.216 155.708 82.968  1.00 44.56  ? 351 PHE A N     1 
ATOM   6024 C  CA    . PHE B 2 351 ? 141.761 157.041 83.330  1.00 38.91  ? 351 PHE A CA    1 
ATOM   6025 C  C     . PHE B 2 351 ? 140.360 157.287 82.803  1.00 38.77  ? 351 PHE A C     1 
ATOM   6026 O  O     . PHE B 2 351 ? 140.022 156.875 81.692  1.00 50.37  ? 351 PHE A O     1 
ATOM   6027 C  CB    . PHE B 2 351 ? 142.699 158.118 82.785  1.00 44.25  ? 351 PHE A CB    1 
ATOM   6028 C  CG    . PHE B 2 351 ? 144.049 158.118 83.419  1.00 37.63  ? 351 PHE A CG    1 
ATOM   6029 C  CD1   . PHE B 2 351 ? 144.278 158.815 84.582  1.00 34.21  ? 351 PHE A CD1   1 
ATOM   6030 C  CD2   . PHE B 2 351 ? 145.092 157.420 82.849  1.00 45.94  ? 351 PHE A CD2   1 
ATOM   6031 C  CE1   . PHE B 2 351 ? 145.516 158.816 85.163  1.00 40.13  ? 351 PHE A CE1   1 
ATOM   6032 C  CE2   . PHE B 2 351 ? 146.335 157.419 83.430  1.00 48.39  ? 351 PHE A CE2   1 
ATOM   6033 C  CZ    . PHE B 2 351 ? 146.545 158.118 84.588  1.00 41.05  ? 351 PHE A CZ    1 
ATOM   6034 N  N     . LYS B 2 352 ? 139.554 157.973 83.608  1.00 39.75  ? 352 LYS A N     1 
ATOM   6035 C  CA    . LYS B 2 352 ? 138.237 158.450 83.212  1.00 40.38  ? 352 LYS A CA    1 
ATOM   6036 C  C     . LYS B 2 352 ? 138.187 159.942 83.496  1.00 44.31  ? 352 LYS A C     1 
ATOM   6037 O  O     . LYS B 2 352 ? 138.426 160.365 84.630  1.00 52.06  ? 352 LYS A O     1 
ATOM   6038 C  CB    . LYS B 2 352 ? 137.131 157.712 83.966  1.00 40.25  ? 352 LYS A CB    1 
ATOM   6039 C  CG    . LYS B 2 352 ? 135.747 158.273 83.754  1.00 44.72  ? 352 LYS A CG    1 
ATOM   6040 C  CD    . LYS B 2 352 ? 135.202 157.924 82.390  1.00 48.60  ? 352 LYS A CD    1 
ATOM   6041 C  CE    . LYS B 2 352 ? 133.727 158.250 82.302  1.00 48.39  ? 352 LYS A CE    1 
ATOM   6042 N  NZ    . LYS B 2 352 ? 133.209 158.134 80.917  1.00 47.36  ? 352 LYS A NZ    1 
ATOM   6043 N  N     . VAL B 2 353 ? 137.877 160.734 82.475  1.00 39.87  ? 353 VAL A N     1 
ATOM   6044 C  CA    . VAL B 2 353 ? 138.013 162.184 82.527  1.00 33.57  ? 353 VAL A CA    1 
ATOM   6045 C  C     . VAL B 2 353 ? 136.632 162.814 82.481  1.00 42.64  ? 353 VAL A C     1 
ATOM   6046 O  O     . VAL B 2 353 ? 135.802 162.450 81.641  1.00 52.15  ? 353 VAL A O     1 
ATOM   6047 C  CB    . VAL B 2 353 ? 138.893 162.701 81.379  1.00 44.42  ? 353 VAL A CB    1 
ATOM   6048 C  CG1   . VAL B 2 353 ? 138.800 164.206 81.275  1.00 47.65  ? 353 VAL A CG1   1 
ATOM   6049 C  CG2   . VAL B 2 353 ? 140.324 162.276 81.594  1.00 47.52  ? 353 VAL A CG2   1 
ATOM   6050 N  N     . GLY B 2 354 ? 136.386 163.751 83.391  1.00 41.63  ? 354 GLY A N     1 
ATOM   6051 C  CA    . GLY B 2 354 ? 135.161 164.524 83.391  1.00 43.77  ? 354 GLY A CA    1 
ATOM   6052 C  C     . GLY B 2 354 ? 135.407 165.992 83.666  1.00 45.81  ? 354 GLY A C     1 
ATOM   6053 O  O     . GLY B 2 354 ? 136.232 166.330 84.517  1.00 53.63  ? 354 GLY A O     1 
ATOM   6054 N  N     . ILE B 2 355 ? 134.705 166.876 82.960  1.00 40.84  ? 355 ILE A N     1 
ATOM   6055 C  CA    . ILE B 2 355 ? 134.904 168.315 83.076  1.00 33.06  ? 355 ILE A CA    1 
ATOM   6056 C  C     . ILE B 2 355 ? 133.566 168.984 83.357  1.00 38.64  ? 355 ILE A C     1 
ATOM   6057 O  O     . ILE B 2 355 ? 132.525 168.550 82.854  1.00 47.03  ? 355 ILE A O     1 
ATOM   6058 C  CB    . ILE B 2 355 ? 135.553 168.905 81.808  1.00 35.82  ? 355 ILE A CB    1 
ATOM   6059 C  CG1   . ILE B 2 355 ? 136.782 168.088 81.413  1.00 45.67  ? 355 ILE A CG1   1 
ATOM   6060 C  CG2   . ILE B 2 355 ? 135.940 170.351 82.028  1.00 42.94  ? 355 ILE A CG2   1 
ATOM   6061 C  CD1   . ILE B 2 355 ? 137.541 168.650 80.248  1.00 47.64  ? 355 ILE A CD1   1 
ATOM   6062 N  N     . ASN B 2 356 ? 133.515 170.007 84.204  1.00 44.50  ? 356 ASN A N     1 
ATOM   6063 C  CA    . ASN B 2 356 ? 132.269 170.769 84.481  1.00 36.26  ? 356 ASN A CA    1 
ATOM   6064 C  C     . ASN B 2 356 ? 132.669 172.235 84.483  1.00 45.92  ? 356 ASN A C     1 
ATOM   6065 O  O     . ASN B 2 356 ? 133.793 172.529 84.868  1.00 54.08  ? 356 ASN A O     1 
ATOM   6066 C  CB    . ASN B 2 356 ? 131.526 170.259 85.711  1.00 32.87  ? 356 ASN A CB    1 
ATOM   6067 C  CG    . ASN B 2 356 ? 130.058 170.583 85.723  1.00 42.79  ? 356 ASN A CG    1 
ATOM   6068 O  OD1   . ASN B 2 356 ? 129.287 170.013 84.947  1.00 47.74  ? 356 ASN A OD1   1 
ATOM   6069 N  ND2   . ASN B 2 356 ? 129.653 171.466 86.621  1.00 46.67  ? 356 ASN A ND2   1 
ATOM   6070 N  N     . TYR B 2 357 ? 131.803 173.112 84.052  1.00 45.54  ? 357 TYR A N     1 
ATOM   6071 C  CA    . TYR B 2 357 ? 132.032 174.538 83.880  1.00 44.70  ? 357 TYR A CA    1 
ATOM   6072 C  C     . TYR B 2 357 ? 131.809 175.343 85.151  1.00 48.55  ? 357 TYR A C     1 
ATOM   6073 O  O     . TYR B 2 357 ? 132.101 176.543 85.160  1.00 51.47  ? 357 TYR A O     1 
ATOM   6074 C  CB    . TYR B 2 357 ? 131.123 175.087 82.776  1.00 48.09  ? 357 TYR A CB    1 
ATOM   6075 C  CG    . TYR B 2 357 ? 131.474 174.601 81.391  1.00 49.87  ? 357 TYR A CG    1 
ATOM   6076 C  CD1   . TYR B 2 357 ? 132.790 174.363 81.032  1.00 51.17  ? 357 TYR A CD1   1 
ATOM   6077 C  CD2   . TYR B 2 357 ? 130.491 174.391 80.440  1.00 49.44  ? 357 TYR A CD2   1 
ATOM   6078 C  CE1   . TYR B 2 357 ? 133.115 173.923 79.771  1.00 52.74  ? 357 TYR A CE1   1 
ATOM   6079 C  CE2   . TYR B 2 357 ? 130.806 173.952 79.175  1.00 50.27  ? 357 TYR A CE2   1 
ATOM   6080 C  CZ    . TYR B 2 357 ? 132.119 173.718 78.847  1.00 52.17  ? 357 TYR A CZ    1 
ATOM   6081 O  OH    . TYR B 2 357 ? 132.436 173.280 77.584  1.00 55.50  ? 357 TYR A OH    1 
ATOM   6082 N  N     . GLN B 2 358 ? 131.309 174.724 86.218  1.00 50.71  ? 358 GLN A N     1 
ATOM   6083 C  CA    . GLN B 2 358 ? 130.960 175.454 87.429  1.00 45.28  ? 358 GLN A CA    1 
ATOM   6084 C  C     . GLN B 2 358 ? 132.137 175.447 88.393  1.00 51.34  ? 358 GLN A C     1 
ATOM   6085 O  O     . GLN B 2 358 ? 132.498 174.377 88.903  1.00 54.53  ? 358 GLN A O     1 
ATOM   6086 C  CB    . GLN B 2 358 ? 129.737 174.841 88.084  1.00 51.60  ? 358 GLN A CB    1 
ATOM   6087 C  CG    . GLN B 2 358 ? 129.236 175.607 89.284  1.00 53.75  ? 358 GLN A CG    1 
ATOM   6088 C  CD    . GLN B 2 358 ? 128.669 176.954 88.913  1.00 54.97  ? 358 GLN A CD    1 
ATOM   6089 O  OE1   . GLN B 2 358 ? 128.262 177.176 87.775  1.00 57.42  ? 358 GLN A OE1   1 
ATOM   6090 N  NE2   . GLN B 2 358 ? 128.634 177.864 89.876  1.00 52.00  ? 358 GLN A NE2   1 
ATOM   6091 N  N     . PRO B 2 359 ? 132.752 176.589 88.675  1.00 51.25  ? 359 PRO A N     1 
ATOM   6092 C  CA    . PRO B 2 359 ? 133.906 176.615 89.569  1.00 44.60  ? 359 PRO A CA    1 
ATOM   6093 C  C     . PRO B 2 359 ? 133.487 176.381 91.007  1.00 46.70  ? 359 PRO A C     1 
ATOM   6094 O  O     . PRO B 2 359 ? 132.304 176.525 91.348  1.00 54.08  ? 359 PRO A O     1 
ATOM   6095 C  CB    . PRO B 2 359 ? 134.466 178.030 89.371  1.00 50.48  ? 359 PRO A CB    1 
ATOM   6096 C  CG    . PRO B 2 359 ? 133.307 178.827 88.912  1.00 49.97  ? 359 PRO A CG    1 
ATOM   6097 C  CD    . PRO B 2 359 ? 132.467 177.911 88.097  1.00 49.98  ? 359 PRO A CD    1 
ATOM   6098 N  N     . PRO B 2 360 ? 134.422 176.007 91.878  1.00 48.49  ? 360 PRO A N     1 
ATOM   6099 C  CA    . PRO B 2 360 ? 134.068 175.768 93.280  1.00 46.71  ? 360 PRO A CA    1 
ATOM   6100 C  C     . PRO B 2 360 ? 133.566 177.033 93.954  1.00 52.09  ? 360 PRO A C     1 
ATOM   6101 O  O     . PRO B 2 360 ? 133.950 178.149 93.599  1.00 58.82  ? 360 PRO A O     1 
ATOM   6102 C  CB    . PRO B 2 360 ? 135.383 175.292 93.903  1.00 48.28  ? 360 PRO A CB    1 
ATOM   6103 C  CG    . PRO B 2 360 ? 136.220 174.864 92.762  1.00 52.77  ? 360 PRO A CG    1 
ATOM   6104 C  CD    . PRO B 2 360 ? 135.842 175.735 91.620  1.00 51.71  ? 360 PRO A CD    1 
ATOM   6105 N  N     . THR B 2 361 ? 132.694 176.849 94.938  1.00 52.86  ? 361 THR A N     1 
ATOM   6106 C  CA    . THR B 2 361 ? 132.126 177.959 95.687  1.00 48.82  ? 361 THR A CA    1 
ATOM   6107 C  C     . THR B 2 361 ? 132.828 178.104 97.027  1.00 53.25  ? 361 THR A C     1 
ATOM   6108 O  O     . THR B 2 361 ? 133.124 177.112 97.697  1.00 55.86  ? 361 THR A O     1 
ATOM   6109 C  CB    . THR B 2 361 ? 130.629 177.765 95.913  1.00 50.27  ? 361 THR A CB    1 
ATOM   6110 O  OG1   . THR B 2 361 ? 130.410 176.562 96.656  1.00 51.43  ? 361 THR A OG1   1 
ATOM   6111 C  CG2   . THR B 2 361 ? 129.905 177.681 94.582  1.00 53.49  ? 361 THR A CG2   1 
ATOM   6112 N  N     . VAL B 2 362 ? 133.096 179.342 97.407  1.00 54.18  ? 362 VAL A N     1 
ATOM   6113 C  CA    . VAL B 2 362 ? 133.729 179.654 98.679  1.00 59.14  ? 362 VAL A CA    1 
ATOM   6114 C  C     . VAL B 2 362 ? 132.644 179.908 99.711  1.00 57.69  ? 362 VAL A C     1 
ATOM   6115 O  O     . VAL B 2 362 ? 131.565 180.421 99.388  1.00 58.80  ? 362 VAL A O     1 
ATOM   6116 C  CB    . VAL B 2 362 ? 134.677 180.861 98.553  1.00 58.94  ? 362 VAL A CB    1 
ATOM   6117 C  CG1   . VAL B 2 362 ? 135.636 180.654 97.398  1.00 54.91  ? 362 VAL A CG1   1 
ATOM   6118 C  CG2   . VAL B 2 362 ? 133.896 182.145 98.365  1.00 58.08  ? 362 VAL A CG2   1 
ATOM   6119 N  N     . VAL B 2 363 ? 132.914 179.520 100.950 1.00 57.93  ? 363 VAL A N     1 
ATOM   6120 C  CA    . VAL B 2 363 ? 131.988 179.777 102.045 1.00 59.89  ? 363 VAL A CA    1 
ATOM   6121 C  C     . VAL B 2 363 ? 132.569 180.890 102.907 1.00 61.85  ? 363 VAL A C     1 
ATOM   6122 O  O     . VAL B 2 363 ? 133.772 180.879 103.202 1.00 66.48  ? 363 VAL A O     1 
ATOM   6123 C  CB    . VAL B 2 363 ? 131.715 178.505 102.861 1.00 62.48  ? 363 VAL A CB    1 
ATOM   6124 C  CG1   . VAL B 2 363 ? 130.942 177.510 102.025 1.00 61.67  ? 363 VAL A CG1   1 
ATOM   6125 C  CG2   . VAL B 2 363 ? 133.009 177.881 103.338 1.00 61.60  ? 363 VAL A CG2   1 
ATOM   6126 N  N     . PRO B 2 364 ? 131.776 181.884 103.298 1.00 59.12  ? 364 PRO A N     1 
ATOM   6127 C  CA    . PRO B 2 364 ? 132.280 182.902 104.222 1.00 63.81  ? 364 PRO A CA    1 
ATOM   6128 C  C     . PRO B 2 364 ? 132.696 182.281 105.545 1.00 63.99  ? 364 PRO A C     1 
ATOM   6129 O  O     . PRO B 2 364 ? 132.093 181.320 106.026 1.00 62.07  ? 364 PRO A O     1 
ATOM   6130 C  CB    . PRO B 2 364 ? 131.088 183.851 104.393 1.00 61.46  ? 364 PRO A CB    1 
ATOM   6131 C  CG    . PRO B 2 364 ? 129.902 183.084 103.906 1.00 60.11  ? 364 PRO A CG    1 
ATOM   6132 C  CD    . PRO B 2 364 ? 130.413 182.184 102.840 1.00 57.78  ? 364 PRO A CD    1 
ATOM   6133 N  N     . GLY B 2 365 ? 133.741 182.849 106.136 1.00 62.69  ? 365 GLY A N     1 
ATOM   6134 C  CA    . GLY B 2 365 ? 134.311 182.280 107.344 1.00 63.46  ? 365 GLY A CA    1 
ATOM   6135 C  C     . GLY B 2 365 ? 134.988 180.947 107.119 1.00 63.48  ? 365 GLY A C     1 
ATOM   6136 O  O     . GLY B 2 365 ? 134.865 180.044 107.955 1.00 64.79  ? 365 GLY A O     1 
ATOM   6137 N  N     . GLY B 2 366 ? 135.703 180.801 106.002 1.00 67.15  ? 366 GLY A N     1 
ATOM   6138 C  CA    . GLY B 2 366 ? 136.353 179.556 105.671 1.00 68.18  ? 366 GLY A CA    1 
ATOM   6139 C  C     . GLY B 2 366 ? 137.815 179.778 105.328 1.00 71.68  ? 366 GLY A C     1 
ATOM   6140 O  O     . GLY B 2 366 ? 138.283 180.911 105.203 1.00 74.19  ? 366 GLY A O     1 
ATOM   6141 N  N     . ASP B 2 367 ? 138.528 178.666 105.176 1.00 71.63  ? 367 ASP A N     1 
ATOM   6142 C  CA    . ASP B 2 367 ? 139.965 178.699 104.960 1.00 70.70  ? 367 ASP A CA    1 
ATOM   6143 C  C     . ASP B 2 367 ? 140.363 178.565 103.498 1.00 73.43  ? 367 ASP A C     1 
ATOM   6144 O  O     . ASP B 2 367 ? 141.436 179.046 103.120 1.00 75.50  ? 367 ASP A O     1 
ATOM   6145 C  CB    . ASP B 2 367 ? 140.641 177.592 105.772 1.00 71.91  ? 367 ASP A CB    1 
ATOM   6146 C  CG    . ASP B 2 367 ? 140.237 177.612 107.232 1.00 76.32  ? 367 ASP A CG    1 
ATOM   6147 O  OD1   . ASP B 2 367 ? 139.964 178.710 107.759 1.00 76.29  ? 367 ASP A OD1   1 
ATOM   6148 O  OD2   . ASP B 2 367 ? 140.191 176.529 107.852 1.00 77.90  ? 367 ASP A OD2   1 
ATOM   6149 N  N     . LEU B 2 368 ? 139.541 177.931 102.672 1.00 66.59  ? 368 LEU A N     1 
ATOM   6150 C  CA    . LEU B 2 368 ? 139.867 177.734 101.271 1.00 63.35  ? 368 LEU A CA    1 
ATOM   6151 C  C     . LEU B 2 368 ? 139.742 179.043 100.504 1.00 63.93  ? 368 LEU A C     1 
ATOM   6152 O  O     . LEU B 2 368 ? 138.889 179.882 100.801 1.00 68.65  ? 368 LEU A O     1 
ATOM   6153 C  CB    . LEU B 2 368 ? 138.959 176.674 100.650 1.00 65.14  ? 368 LEU A CB    1 
ATOM   6154 C  CG    . LEU B 2 368 ? 139.469 175.236 100.719 1.00 68.20  ? 368 LEU A CG    1 
ATOM   6155 C  CD1   . LEU B 2 368 ? 139.307 174.674 102.119 1.00 67.31  ? 368 LEU A CD1   1 
ATOM   6156 C  CD2   . LEU B 2 368 ? 138.740 174.368 99.709  1.00 68.23  ? 368 LEU A CD2   1 
ATOM   6157 N  N     . ALA B 2 369 ? 140.608 179.212 99.514  1.00 57.37  ? 369 ALA A N     1 
ATOM   6158 C  CA    . ALA B 2 369 ? 140.663 180.422 98.712  1.00 61.59  ? 369 ALA A CA    1 
ATOM   6159 C  C     . ALA B 2 369 ? 139.827 180.273 97.448  1.00 62.76  ? 369 ALA A C     1 
ATOM   6160 O  O     . ALA B 2 369 ? 139.484 179.167 97.026  1.00 62.47  ? 369 ALA A O     1 
ATOM   6161 C  CB    . ALA B 2 369 ? 142.107 180.762 98.344  1.00 60.64  ? 369 ALA A CB    1 
ATOM   6162 N  N     . LYS B 2 370 ? 139.501 181.413 96.844  1.00 61.11  ? 370 LYS A N     1 
ATOM   6163 C  CA    . LYS B 2 370 ? 138.727 181.430 95.607  1.00 55.15  ? 370 LYS A CA    1 
ATOM   6164 C  C     . LYS B 2 370 ? 139.623 181.032 94.445  1.00 58.84  ? 370 LYS A C     1 
ATOM   6165 O  O     . LYS B 2 370 ? 140.453 181.824 93.990  1.00 62.58  ? 370 LYS A O     1 
ATOM   6166 C  CB    . LYS B 2 370 ? 138.122 182.808 95.373  1.00 56.58  ? 370 LYS A CB    1 
ATOM   6167 C  CG    . LYS B 2 370 ? 137.381 182.915 94.059  1.00 57.71  ? 370 LYS A CG    1 
ATOM   6168 C  CD    . LYS B 2 370 ? 136.590 184.198 93.956  1.00 60.01  ? 370 LYS A CD    1 
ATOM   6169 C  CE    . LYS B 2 370 ? 135.813 184.243 92.657  1.00 58.40  ? 370 LYS A CE    1 
ATOM   6170 N  NZ    . LYS B 2 370 ? 134.986 185.475 92.550  1.00 59.82  ? 370 LYS A NZ    1 
ATOM   6171 N  N     . VAL B 2 371 ? 139.456 179.808 93.961  1.00 57.22  ? 371 VAL A N     1 
ATOM   6172 C  CA    . VAL B 2 371 ? 140.252 179.290 92.864  1.00 51.33  ? 371 VAL A CA    1 
ATOM   6173 C  C     . VAL B 2 371 ? 139.404 179.290 91.602  1.00 51.52  ? 371 VAL A C     1 
ATOM   6174 O  O     . VAL B 2 371 ? 138.175 179.387 91.645  1.00 57.90  ? 371 VAL A O     1 
ATOM   6175 C  CB    . VAL B 2 371 ? 140.790 177.881 93.162  1.00 56.93  ? 371 VAL A CB    1 
ATOM   6176 C  CG1   . VAL B 2 371 ? 141.720 177.923 94.354  1.00 58.12  ? 371 VAL A CG1   1 
ATOM   6177 C  CG2   . VAL B 2 371 ? 139.643 176.927 93.414  1.00 54.33  ? 371 VAL A CG2   1 
ATOM   6178 N  N     . GLN B 2 372 ? 140.078 179.191 90.462  1.00 48.86  ? 372 GLN A N     1 
ATOM   6179 C  CA    . GLN B 2 372 ? 139.397 179.169 89.178  1.00 48.25  ? 372 GLN A CA    1 
ATOM   6180 C  C     . GLN B 2 372 ? 139.238 177.768 88.604  1.00 51.58  ? 372 GLN A C     1 
ATOM   6181 O  O     . GLN B 2 372 ? 138.538 177.608 87.601  1.00 54.34  ? 372 GLN A O     1 
ATOM   6182 C  CB    . GLN B 2 372 ? 140.140 180.054 88.182  1.00 45.70  ? 372 GLN A CB    1 
ATOM   6183 C  CG    . GLN B 2 372 ? 140.015 181.527 88.490  1.00 50.09  ? 372 GLN A CG    1 
ATOM   6184 C  CD    . GLN B 2 372 ? 140.849 182.384 87.570  1.00 57.50  ? 372 GLN A CD    1 
ATOM   6185 O  OE1   . GLN B 2 372 ? 141.687 181.880 86.825  1.00 59.62  ? 372 GLN A OE1   1 
ATOM   6186 N  NE2   . GLN B 2 372 ? 140.627 183.690 87.617  1.00 55.23  ? 372 GLN A NE2   1 
ATOM   6187 N  N     . ARG B 2 373 ? 139.861 176.761 89.206  1.00 42.96  ? 373 ARG A N     1 
ATOM   6188 C  CA    . ARG B 2 373 ? 139.707 175.384 88.765  1.00 40.47  ? 373 ARG A CA    1 
ATOM   6189 C  C     . ARG B 2 373 ? 140.131 174.454 89.891  1.00 41.90  ? 373 ARG A C     1 
ATOM   6190 O  O     . ARG B 2 373 ? 140.956 174.818 90.731  1.00 50.14  ? 373 ARG A O     1 
ATOM   6191 C  CB    . ARG B 2 373 ? 140.527 175.108 87.503  1.00 41.37  ? 373 ARG A CB    1 
ATOM   6192 C  CG    . ARG B 2 373 ? 141.990 175.430 87.645  1.00 43.04  ? 373 ARG A CG    1 
ATOM   6193 C  CD    . ARG B 2 373 ? 142.686 175.438 86.306  1.00 46.73  ? 373 ARG A CD    1 
ATOM   6194 N  NE    . ARG B 2 373 ? 142.328 176.601 85.507  1.00 48.08  ? 373 ARG A NE    1 
ATOM   6195 C  CZ    . ARG B 2 373 ? 142.959 177.764 85.557  1.00 47.12  ? 373 ARG A CZ    1 
ATOM   6196 N  NH1   . ARG B 2 373 ? 143.983 177.960 86.369  1.00 48.14  ? 373 ARG A NH1   1 
ATOM   6197 N  NH2   . ARG B 2 373 ? 142.549 178.758 84.777  1.00 43.40  ? 373 ARG A NH2   1 
ATOM   6198 N  N     . ALA B 2 374 ? 139.564 173.251 89.897  1.00 36.78  ? 374 ALA A N     1 
ATOM   6199 C  CA    . ALA B 2 374 ? 139.863 172.269 90.927  1.00 36.37  ? 374 ALA A CA    1 
ATOM   6200 C  C     . ALA B 2 374 ? 139.707 170.872 90.348  1.00 36.62  ? 374 ALA A C     1 
ATOM   6201 O  O     . ALA B 2 374 ? 139.039 170.673 89.333  1.00 41.00  ? 374 ALA A O     1 
ATOM   6202 C  CB    . ALA B 2 374 ? 138.961 172.447 92.152  1.00 42.82  ? 374 ALA A CB    1 
ATOM   6203 N  N     . VAL B 2 375 ? 140.337 169.899 91.007  1.00 35.68  ? 375 VAL A N     1 
ATOM   6204 C  CA    . VAL B 2 375 ? 140.234 168.497 90.630  1.00 33.44  ? 375 VAL A CA    1 
ATOM   6205 C  C     . VAL B 2 375 ? 139.842 167.684 91.855  1.00 43.73  ? 375 VAL A C     1 
ATOM   6206 O  O     . VAL B 2 375 ? 140.024 168.105 92.998  1.00 52.34  ? 375 VAL A O     1 
ATOM   6207 C  CB    . VAL B 2 375 ? 141.540 167.945 90.016  1.00 36.55  ? 375 VAL A CB    1 
ATOM   6208 C  CG1   . VAL B 2 375 ? 142.471 167.447 91.102  1.00 44.56  ? 375 VAL A CG1   1 
ATOM   6209 C  CG2   . VAL B 2 375 ? 141.238 166.831 89.038  1.00 42.50  ? 375 VAL A CG2   1 
ATOM   6210 N  N     . CYS B 2 376 ? 139.283 166.507 91.595  1.00 43.85  ? 376 CYS A N     1 
ATOM   6211 C  CA    . CYS B 2 376 ? 138.971 165.540 92.641  1.00 36.15  ? 376 CYS A CA    1 
ATOM   6212 C  C     . CYS B 2 376 ? 139.195 164.156 92.055  1.00 46.47  ? 376 CYS A C     1 
ATOM   6213 O  O     . CYS B 2 376 ? 138.381 163.687 91.257  1.00 54.13  ? 376 CYS A O     1 
ATOM   6214 C  CB    . CYS B 2 376 ? 137.541 165.700 93.138  1.00 42.20  ? 376 CYS A CB    1 
ATOM   6215 S  SG    . CYS B 2 376 ? 136.983 164.395 94.236  1.00 66.90  ? 376 CYS A SG    1 
ATOM   6216 N  N     . MET B 2 377 ? 140.288 163.508 92.440  1.00 46.56  ? 377 MET A N     1 
ATOM   6217 C  CA    . MET B 2 377 ? 140.631 162.193 91.921  1.00 45.95  ? 377 MET A CA    1 
ATOM   6218 C  C     . MET B 2 377 ? 140.196 161.107 92.892  1.00 51.68  ? 377 MET A C     1 
ATOM   6219 O  O     . MET B 2 377 ? 140.517 161.163 94.081  1.00 57.96  ? 377 MET A O     1 
ATOM   6220 C  CB    . MET B 2 377 ? 142.128 162.071 91.657  1.00 47.59  ? 377 MET A CB    1 
ATOM   6221 C  CG    . MET B 2 377 ? 142.505 160.790 90.953  1.00 51.43  ? 377 MET A CG    1 
ATOM   6222 S  SD    . MET B 2 377 ? 144.265 160.453 90.973  1.00 73.76  ? 377 MET A SD    1 
ATOM   6223 C  CE    . MET B 2 377 ? 144.513 160.102 92.707  1.00 55.70  ? 377 MET A CE    1 
ATOM   6224 N  N     . LEU B 2 378 ? 139.475 160.120 92.375  1.00 46.58  ? 378 LEU A N     1 
ATOM   6225 C  CA    . LEU B 2 378 ? 139.113 158.919 93.112  1.00 42.33  ? 378 LEU A CA    1 
ATOM   6226 C  C     . LEU B 2 378 ? 139.795 157.737 92.441  1.00 47.96  ? 378 LEU A C     1 
ATOM   6227 O  O     . LEU B 2 378 ? 139.553 157.468 91.261  1.00 50.34  ? 378 LEU A O     1 
ATOM   6228 C  CB    . LEU B 2 378 ? 137.600 158.724 93.129  1.00 43.83  ? 378 LEU A CB    1 
ATOM   6229 C  CG    . LEU B 2 378 ? 136.734 159.977 93.138  1.00 50.02  ? 378 LEU A CG    1 
ATOM   6230 C  CD1   . LEU B 2 378 ? 135.278 159.596 92.983  1.00 48.08  ? 378 LEU A CD1   1 
ATOM   6231 C  CD2   . LEU B 2 378 ? 136.945 160.761 94.419  1.00 53.14  ? 378 LEU A CD2   1 
ATOM   6232 N  N     . SER B 2 379 ? 140.642 157.033 93.186  1.00 45.27  ? 379 SER A N     1 
ATOM   6233 C  CA    . SER B 2 379 ? 141.406 155.911 92.661  1.00 39.93  ? 379 SER A CA    1 
ATOM   6234 C  C     . SER B 2 379 ? 141.353 154.742 93.630  1.00 44.01  ? 379 SER A C     1 
ATOM   6235 O  O     . SER B 2 379 ? 141.410 154.937 94.847  1.00 54.17  ? 379 SER A O     1 
ATOM   6236 C  CB    . SER B 2 379 ? 142.851 156.310 92.418  1.00 47.30  ? 379 SER A CB    1 
ATOM   6237 O  OG    . SER B 2 379 ? 143.351 157.035 93.522  1.00 50.61  ? 379 SER A OG    1 
ATOM   6238 N  N     . ASN B 2 380 ? 141.249 153.528 93.095  1.00 45.55  ? 380 ASN A N     1 
ATOM   6239 C  CA    . ASN B 2 380 ? 141.296 152.313 93.902  1.00 52.96  ? 380 ASN A CA    1 
ATOM   6240 C  C     . ASN B 2 380 ? 142.630 151.620 93.658  1.00 52.74  ? 380 ASN A C     1 
ATOM   6241 O  O     . ASN B 2 380 ? 142.893 151.127 92.558  1.00 52.40  ? 380 ASN A O     1 
ATOM   6242 C  CB    . ASN B 2 380 ? 140.124 151.384 93.596  1.00 46.37  ? 380 ASN A CB    1 
ATOM   6243 C  CG    . ASN B 2 380 ? 139.955 151.124 92.133  1.00 53.84  ? 380 ASN A CG    1 
ATOM   6244 O  OD1   . ASN B 2 380 ? 140.500 151.842 91.300  1.00 60.29  ? 380 ASN A OD1   1 
ATOM   6245 N  ND2   . ASN B 2 380 ? 139.190 150.094 91.802  1.00 54.94  ? 380 ASN A ND2   1 
ATOM   6246 N  N     . THR B 2 381 ? 143.465 151.587 94.688  1.00 52.31  ? 381 THR A N     1 
ATOM   6247 C  CA    . THR B 2 381 ? 144.787 150.989 94.643  1.00 48.45  ? 381 THR A CA    1 
ATOM   6248 C  C     . THR B 2 381 ? 144.832 149.756 95.533  1.00 53.66  ? 381 THR A C     1 
ATOM   6249 O  O     . THR B 2 381 ? 143.903 149.470 96.290  1.00 57.14  ? 381 THR A O     1 
ATOM   6250 C  CB    . THR B 2 381 ? 145.851 151.994 95.091  1.00 53.98  ? 381 THR A CB    1 
ATOM   6251 O  OG1   . THR B 2 381 ? 145.905 152.025 96.521  1.00 61.46  ? 381 THR A OG1   1 
ATOM   6252 C  CG2   . THR B 2 381 ? 145.513 153.377 94.588  1.00 53.40  ? 381 THR A CG2   1 
ATOM   6253 N  N     . THR B 2 382 ? 145.936 149.023 95.435  1.00 47.85  ? 382 THR A N     1 
ATOM   6254 C  CA    . THR B 2 382 ? 146.205 147.929 96.356  1.00 44.02  ? 382 THR A CA    1 
ATOM   6255 C  C     . THR B 2 382 ? 146.829 148.406 97.657  1.00 46.16  ? 382 THR A C     1 
ATOM   6256 O  O     . THR B 2 382 ? 147.097 147.583 98.536  1.00 56.75  ? 382 THR A O     1 
ATOM   6257 C  CB    . THR B 2 382 ? 147.121 146.891 95.704  1.00 45.71  ? 382 THR A CB    1 
ATOM   6258 O  OG1   . THR B 2 382 ? 148.416 147.459 95.489  1.00 52.02  ? 382 THR A OG1   1 
ATOM   6259 C  CG2   . THR B 2 382 ? 146.554 146.437 94.384  1.00 43.61  ? 382 THR A CG2   1 
ATOM   6260 N  N     . ALA B 2 383 ? 147.068 149.706 97.798  1.00 46.39  ? 383 ALA A N     1 
ATOM   6261 C  CA    . ALA B 2 383 ? 147.632 150.274 99.013  1.00 50.25  ? 383 ALA A CA    1 
ATOM   6262 C  C     . ALA B 2 383 ? 146.587 150.537 100.085 1.00 52.26  ? 383 ALA A C     1 
ATOM   6263 O  O     . ALA B 2 383 ? 146.940 151.009 101.169 1.00 55.43  ? 383 ALA A O     1 
ATOM   6264 C  CB    . ALA B 2 383 ? 148.374 151.570 98.688  1.00 54.32  ? 383 ALA A CB    1 
ATOM   6265 N  N     . ILE B 2 384 ? 145.312 150.250 99.810  1.00 52.08  ? 384 ILE A N     1 
ATOM   6266 C  CA    . ILE B 2 384 ? 144.259 150.398 100.811 1.00 45.10  ? 384 ILE A CA    1 
ATOM   6267 C  C     . ILE B 2 384 ? 144.230 149.249 101.804 1.00 50.22  ? 384 ILE A C     1 
ATOM   6268 O  O     . ILE B 2 384 ? 143.407 149.260 102.727 1.00 57.97  ? 384 ILE A O     1 
ATOM   6269 C  CB    . ILE B 2 384 ? 142.893 150.537 100.109 1.00 47.53  ? 384 ILE A CB    1 
ATOM   6270 C  CG1   . ILE B 2 384 ? 141.876 151.235 101.015 1.00 48.87  ? 384 ILE A CG1   1 
ATOM   6271 C  CG2   . ILE B 2 384 ? 142.383 149.183 99.661  1.00 54.04  ? 384 ILE A CG2   1 
ATOM   6272 C  CD1   . ILE B 2 384 ? 142.352 152.549 101.566 1.00 54.95  ? 384 ILE A CD1   1 
ATOM   6273 N  N     . ALA B 2 385 ? 145.113 148.266 101.661 1.00 50.32  ? 385 ALA A N     1 
ATOM   6274 C  CA    . ALA B 2 385 ? 145.122 147.113 102.547 1.00 51.26  ? 385 ALA A CA    1 
ATOM   6275 C  C     . ALA B 2 385 ? 146.029 147.285 103.758 1.00 48.45  ? 385 ALA A C     1 
ATOM   6276 O  O     . ALA B 2 385 ? 146.061 146.397 104.615 1.00 54.98  ? 385 ALA A O     1 
ATOM   6277 C  CB    . ALA B 2 385 ? 145.540 145.861 101.775 1.00 53.12  ? 385 ALA A CB    1 
ATOM   6278 N  N     . GLU B 2 386 ? 146.768 148.389 103.851 1.00 47.92  ? 386 GLU A N     1 
ATOM   6279 C  CA    . GLU B 2 386 ? 147.602 148.623 105.023 1.00 54.45  ? 386 GLU A CA    1 
ATOM   6280 C  C     . GLU B 2 386 ? 146.759 148.988 106.240 1.00 58.68  ? 386 GLU A C     1 
ATOM   6281 O  O     . GLU B 2 386 ? 146.968 148.456 107.341 1.00 63.20  ? 386 GLU A O     1 
ATOM   6282 C  CB    . GLU B 2 386 ? 148.615 149.724 104.720 1.00 59.19  ? 386 GLU A CB    1 
ATOM   6283 C  CG    . GLU B 2 386 ? 149.917 149.227 104.123 1.00 57.95  ? 386 GLU A CG    1 
ATOM   6284 C  CD    . GLU B 2 386 ? 149.756 148.722 102.705 1.00 66.24  ? 386 GLU A CD    1 
ATOM   6285 O  OE1   . GLU B 2 386 ? 148.736 149.050 102.066 1.00 65.12  ? 386 GLU A OE1   1 
ATOM   6286 O  OE2   . GLU B 2 386 ? 150.653 147.995 102.228 1.00 69.06  ? 386 GLU A OE2   1 
ATOM   6287 N  N     . ALA B 2 387 ? 145.797 149.896 106.060 1.00 49.45  ? 387 ALA A N     1 
ATOM   6288 C  CA    . ALA B 2 387 ? 144.956 150.320 107.173 1.00 55.67  ? 387 ALA A CA    1 
ATOM   6289 C  C     . ALA B 2 387 ? 144.142 149.156 107.713 1.00 58.64  ? 387 ALA A C     1 
ATOM   6290 O  O     . ALA B 2 387 ? 143.975 149.007 108.933 1.00 63.36  ? 387 ALA A O     1 
ATOM   6291 C  CB    . ALA B 2 387 ? 144.039 151.456 106.728 1.00 55.82  ? 387 ALA A CB    1 
ATOM   6292 N  N     . TRP B 2 388 ? 143.633 148.318 106.814 1.00 51.62  ? 388 TRP A N     1 
ATOM   6293 C  CA    . TRP B 2 388 ? 142.897 147.137 107.233 1.00 50.14  ? 388 TRP A CA    1 
ATOM   6294 C  C     . TRP B 2 388 ? 143.780 146.205 108.050 1.00 55.74  ? 388 TRP A C     1 
ATOM   6295 O  O     . TRP B 2 388 ? 143.333 145.635 109.052 1.00 59.41  ? 388 TRP A O     1 
ATOM   6296 C  CB    . TRP B 2 388 ? 142.339 146.424 106.008 1.00 50.52  ? 388 TRP A CB    1 
ATOM   6297 C  CG    . TRP B 2 388 ? 141.274 147.193 105.297 1.00 54.67  ? 388 TRP A CG    1 
ATOM   6298 C  CD1   . TRP B 2 388 ? 140.536 148.215 105.796 1.00 55.11  ? 388 TRP A CD1   1 
ATOM   6299 C  CD2   . TRP B 2 388 ? 140.834 146.998 103.952 1.00 54.20  ? 388 TRP A CD2   1 
ATOM   6300 N  NE1   . TRP B 2 388 ? 139.657 148.671 104.848 1.00 52.04  ? 388 TRP A NE1   1 
ATOM   6301 C  CE2   . TRP B 2 388 ? 139.822 147.938 103.705 1.00 52.60  ? 388 TRP A CE2   1 
ATOM   6302 C  CE3   . TRP B 2 388 ? 141.198 146.118 102.932 1.00 53.92  ? 388 TRP A CE3   1 
ATOM   6303 C  CZ2   . TRP B 2 388 ? 139.172 148.025 102.484 1.00 56.70  ? 388 TRP A CZ2   1 
ATOM   6304 C  CZ3   . TRP B 2 388 ? 140.555 146.205 101.725 1.00 53.22  ? 388 TRP A CZ3   1 
ATOM   6305 C  CH2   . TRP B 2 388 ? 139.553 147.150 101.508 1.00 56.24  ? 388 TRP A CH2   1 
ATOM   6306 N  N     . ALA B 2 389 ? 145.037 146.040 107.638 1.00 49.56  ? 389 ALA A N     1 
ATOM   6307 C  CA    . ALA B 2 389 ? 145.956 145.193 108.388 1.00 46.63  ? 389 ALA A CA    1 
ATOM   6308 C  C     . ALA B 2 389 ? 146.205 145.746 109.785 1.00 54.18  ? 389 ALA A C     1 
ATOM   6309 O  O     . ALA B 2 389 ? 146.222 144.990 110.767 1.00 59.25  ? 389 ALA A O     1 
ATOM   6310 C  CB    . ALA B 2 389 ? 147.269 145.046 107.625 1.00 50.15  ? 389 ALA A CB    1 
ATOM   6311 N  N     . ARG B 2 390 ? 146.397 147.062 109.899 1.00 50.96  ? 390 ARG A N     1 
ATOM   6312 C  CA    . ARG B 2 390 ? 146.604 147.658 111.217 1.00 48.19  ? 390 ARG A CA    1 
ATOM   6313 C  C     . ARG B 2 390 ? 145.396 147.439 112.117 1.00 53.02  ? 390 ARG A C     1 
ATOM   6314 O  O     . ARG B 2 390 ? 145.536 147.069 113.295 1.00 60.14  ? 390 ARG A O     1 
ATOM   6315 C  CB    . ARG B 2 390 ? 146.901 149.148 111.078 1.00 45.69  ? 390 ARG A CB    1 
ATOM   6316 C  CG    . ARG B 2 390 ? 148.242 149.448 110.456 1.00 53.44  ? 390 ARG A CG    1 
ATOM   6317 C  CD    . ARG B 2 390 ? 148.565 150.922 110.528 1.00 59.19  ? 390 ARG A CD    1 
ATOM   6318 N  NE    . ARG B 2 390 ? 147.976 151.669 109.424 1.00 61.50  ? 390 ARG A NE    1 
ATOM   6319 C  CZ    . ARG B 2 390 ? 148.674 152.305 108.494 1.00 56.24  ? 390 ARG A CZ    1 
ATOM   6320 N  NH1   . ARG B 2 390 ? 149.996 152.303 108.502 1.00 55.21  ? 390 ARG A NH1   1 
ATOM   6321 N  NH2   . ARG B 2 390 ? 148.030 152.959 107.533 1.00 53.50  ? 390 ARG A NH2   1 
ATOM   6322 N  N     . LEU B 2 391 ? 144.197 147.655 111.578 1.00 45.48  ? 391 LEU A N     1 
ATOM   6323 C  CA    . LEU B 2 391 ? 143.000 147.480 112.389 1.00 48.35  ? 391 LEU A CA    1 
ATOM   6324 C  C     . LEU B 2 391 ? 142.820 146.026 112.803 1.00 54.11  ? 391 LEU A C     1 
ATOM   6325 O  O     . LEU B 2 391 ? 142.402 145.745 113.932 1.00 59.56  ? 391 LEU A O     1 
ATOM   6326 C  CB    . LEU B 2 391 ? 141.777 147.987 111.633 1.00 48.18  ? 391 LEU A CB    1 
ATOM   6327 C  CG    . LEU B 2 391 ? 140.682 148.613 112.491 1.00 48.93  ? 391 LEU A CG    1 
ATOM   6328 C  CD1   . LEU B 2 391 ? 141.275 149.437 113.610 1.00 50.36  ? 391 LEU A CD1   1 
ATOM   6329 C  CD2   . LEU B 2 391 ? 139.810 149.479 111.617 1.00 53.72  ? 391 LEU A CD2   1 
ATOM   6330 N  N     . ASP B 2 392 ? 143.128 145.089 111.906 1.00 53.86  ? 392 ASP A N     1 
ATOM   6331 C  CA    . ASP B 2 392 ? 143.036 143.678 112.260 1.00 47.73  ? 392 ASP A CA    1 
ATOM   6332 C  C     . ASP B 2 392 ? 144.019 143.321 113.365 1.00 52.58  ? 392 ASP A C     1 
ATOM   6333 O  O     . ASP B 2 392 ? 143.694 142.534 114.262 1.00 59.05  ? 392 ASP A O     1 
ATOM   6334 C  CB    . ASP B 2 392 ? 143.276 142.813 111.026 1.00 55.66  ? 392 ASP A CB    1 
ATOM   6335 C  CG    . ASP B 2 392 ? 142.163 142.931 110.010 1.00 67.09  ? 392 ASP A CG    1 
ATOM   6336 O  OD1   . ASP B 2 392 ? 141.331 143.852 110.146 1.00 66.42  ? 392 ASP A OD1   1 
ATOM   6337 O  OD2   . ASP B 2 392 ? 142.113 142.100 109.079 1.00 67.82  ? 392 ASP A OD2   1 
ATOM   6338 N  N     . HIS B 2 393 ? 145.228 143.883 113.315 1.00 49.46  ? 393 HIS A N     1 
ATOM   6339 C  CA    . HIS B 2 393 ? 146.202 143.624 114.371 1.00 46.43  ? 393 HIS A CA    1 
ATOM   6340 C  C     . HIS B 2 393 ? 145.685 144.115 115.714 1.00 45.94  ? 393 HIS A C     1 
ATOM   6341 O  O     . HIS B 2 393 ? 145.761 143.405 116.727 1.00 53.27  ? 393 HIS A O     1 
ATOM   6342 C  CB    . HIS B 2 393 ? 147.530 144.290 114.027 1.00 48.03  ? 393 HIS A CB    1 
ATOM   6343 C  CG    . HIS B 2 393 ? 148.538 144.234 115.130 1.00 55.33  ? 393 HIS A CG    1 
ATOM   6344 N  ND1   . HIS B 2 393 ? 149.103 143.055 115.562 1.00 55.30  ? 393 HIS A ND1   1 
ATOM   6345 C  CD2   . HIS B 2 393 ? 149.092 145.214 115.881 1.00 55.30  ? 393 HIS A CD2   1 
ATOM   6346 C  CE1   . HIS B 2 393 ? 149.957 143.310 116.537 1.00 55.54  ? 393 HIS A CE1   1 
ATOM   6347 N  NE2   . HIS B 2 393 ? 149.969 144.613 116.749 1.00 55.90  ? 393 HIS A NE2   1 
ATOM   6348 N  N     . LYS B 2 394 ? 145.129 145.325 115.731 1.00 45.46  ? 394 LYS A N     1 
ATOM   6349 C  CA    . LYS B 2 394 ? 144.567 145.867 116.964 1.00 38.46  ? 394 LYS A CA    1 
ATOM   6350 C  C     . LYS B 2 394 ? 143.441 144.979 117.485 1.00 40.38  ? 394 LYS A C     1 
ATOM   6351 O  O     . LYS B 2 394 ? 143.378 144.659 118.683 1.00 44.66  ? 394 LYS A O     1 
ATOM   6352 C  CB    . LYS B 2 394 ? 144.063 147.285 116.708 1.00 41.76  ? 394 LYS A CB    1 
ATOM   6353 C  CG    . LYS B 2 394 ? 144.592 148.313 117.662 1.00 44.67  ? 394 LYS A CG    1 
ATOM   6354 C  CD    . LYS B 2 394 ? 144.529 149.708 117.083 1.00 43.65  ? 394 LYS A CD    1 
ATOM   6355 C  CE    . LYS B 2 394 ? 145.393 149.847 115.858 1.00 45.03  ? 394 LYS A CE    1 
ATOM   6356 N  NZ    . LYS B 2 394 ? 145.466 151.264 115.426 1.00 47.54  ? 394 LYS A NZ    1 
ATOM   6357 N  N     . PHE B 2 395 ? 142.555 144.552 116.585 1.00 44.32  ? 395 PHE A N     1 
ATOM   6358 C  CA    . PHE B 2 395 ? 141.420 143.726 116.976 1.00 41.88  ? 395 PHE A CA    1 
ATOM   6359 C  C     . PHE B 2 395 ? 141.876 142.413 117.587 1.00 47.20  ? 395 PHE A C     1 
ATOM   6360 O  O     . PHE B 2 395 ? 141.359 141.990 118.625 1.00 55.78  ? 395 PHE A O     1 
ATOM   6361 C  CB    . PHE B 2 395 ? 140.523 143.461 115.769 1.00 44.32  ? 395 PHE A CB    1 
ATOM   6362 C  CG    . PHE B 2 395 ? 139.483 142.407 116.008 1.00 43.10  ? 395 PHE A CG    1 
ATOM   6363 C  CD1   . PHE B 2 395 ? 138.275 142.735 116.581 1.00 49.92  ? 395 PHE A CD1   1 
ATOM   6364 C  CD2   . PHE B 2 395 ? 139.708 141.095 115.660 1.00 44.48  ? 395 PHE A CD2   1 
ATOM   6365 C  CE1   . PHE B 2 395 ? 137.317 141.777 116.801 1.00 49.49  ? 395 PHE A CE1   1 
ATOM   6366 C  CE2   . PHE B 2 395 ? 138.751 140.137 115.881 1.00 45.18  ? 395 PHE A CE2   1 
ATOM   6367 C  CZ    . PHE B 2 395 ? 137.556 140.480 116.450 1.00 44.81  ? 395 PHE A CZ    1 
ATOM   6368 N  N     . ASP B 2 396 ? 142.829 141.736 116.946 1.00 45.72  ? 396 ASP A N     1 
ATOM   6369 C  CA    . ASP B 2 396 ? 143.235 140.432 117.456 1.00 43.09  ? 396 ASP A CA    1 
ATOM   6370 C  C     . ASP B 2 396 ? 143.983 140.569 118.773 1.00 46.87  ? 396 ASP A C     1 
ATOM   6371 O  O     . ASP B 2 396 ? 143.816 139.737 119.676 1.00 51.28  ? 396 ASP A O     1 
ATOM   6372 C  CB    . ASP B 2 396 ? 144.058 139.670 116.413 1.00 44.83  ? 396 ASP A CB    1 
ATOM   6373 C  CG    . ASP B 2 396 ? 145.353 140.363 116.042 1.00 53.90  ? 396 ASP A CG    1 
ATOM   6374 O  OD1   . ASP B 2 396 ? 146.170 140.664 116.938 1.00 59.10  ? 396 ASP A OD1   1 
ATOM   6375 O  OD2   . ASP B 2 396 ? 145.573 140.576 114.832 1.00 54.53  ? 396 ASP A OD2   1 
ATOM   6376 N  N     . LEU B 2 397 ? 144.780 141.629 118.921 1.00 47.97  ? 397 LEU A N     1 
ATOM   6377 C  CA    . LEU B 2 397 ? 145.437 141.873 120.199 1.00 40.93  ? 397 LEU A CA    1 
ATOM   6378 C  C     . LEU B 2 397 ? 144.415 142.020 121.317 1.00 39.16  ? 397 LEU A C     1 
ATOM   6379 O  O     . LEU B 2 397 ? 144.570 141.438 122.394 1.00 40.50  ? 397 LEU A O     1 
ATOM   6380 C  CB    . LEU B 2 397 ? 146.308 143.122 120.103 1.00 40.77  ? 397 LEU A CB    1 
ATOM   6381 C  CG    . LEU B 2 397 ? 147.536 143.187 121.002 1.00 49.68  ? 397 LEU A CG    1 
ATOM   6382 C  CD1   . LEU B 2 397 ? 148.502 142.072 120.658 1.00 49.48  ? 397 LEU A CD1   1 
ATOM   6383 C  CD2   . LEU B 2 397 ? 148.206 144.538 120.863 1.00 47.69  ? 397 LEU A CD2   1 
ATOM   6384 N  N     . MET B 2 398 ? 143.355 142.795 121.080 1.00 45.93  ? 398 MET A N     1 
ATOM   6385 C  CA    . MET B 2 398 ? 142.367 142.992 122.139 1.00 43.24  ? 398 MET A CA    1 
ATOM   6386 C  C     . MET B 2 398 ? 141.539 141.736 122.379 1.00 41.36  ? 398 MET A C     1 
ATOM   6387 O  O     . MET B 2 398 ? 141.177 141.435 123.521 1.00 41.15  ? 398 MET A O     1 
ATOM   6388 C  CB    . MET B 2 398 ? 141.461 144.172 121.804 1.00 45.57  ? 398 MET A CB    1 
ATOM   6389 C  CG    . MET B 2 398 ? 141.735 145.401 122.633 1.00 44.75  ? 398 MET A CG    1 
ATOM   6390 S  SD    . MET B 2 398 ? 140.516 146.692 122.379 1.00 60.40  ? 398 MET A SD    1 
ATOM   6391 C  CE    . MET B 2 398 ? 139.017 145.830 122.822 1.00 51.03  ? 398 MET A CE    1 
ATOM   6392 N  N     . TYR B 2 399 ? 141.224 140.992 121.318 1.00 45.70  ? 399 TYR A N     1 
ATOM   6393 C  CA    . TYR B 2 399 ? 140.316 139.856 121.410 1.00 42.10  ? 399 TYR A CA    1 
ATOM   6394 C  C     . TYR B 2 399 ? 140.985 138.604 121.949 1.00 43.67  ? 399 TYR A C     1 
ATOM   6395 O  O     . TYR B 2 399 ? 140.284 137.682 122.374 1.00 48.04  ? 399 TYR A O     1 
ATOM   6396 C  CB    . TYR B 2 399 ? 139.712 139.574 120.032 1.00 41.47  ? 399 TYR A CB    1 
ATOM   6397 C  CG    . TYR B 2 399 ? 138.624 138.527 119.996 1.00 47.13  ? 399 TYR A CG    1 
ATOM   6398 C  CD1   . TYR B 2 399 ? 137.466 138.674 120.735 1.00 47.11  ? 399 TYR A CD1   1 
ATOM   6399 C  CD2   . TYR B 2 399 ? 138.739 137.409 119.182 1.00 47.43  ? 399 TYR A CD2   1 
ATOM   6400 C  CE1   . TYR B 2 399 ? 136.467 137.725 120.689 1.00 44.21  ? 399 TYR A CE1   1 
ATOM   6401 C  CE2   . TYR B 2 399 ? 137.744 136.458 119.130 1.00 40.72  ? 399 TYR A CE2   1 
ATOM   6402 C  CZ    . TYR B 2 399 ? 136.612 136.622 119.888 1.00 41.40  ? 399 TYR A CZ    1 
ATOM   6403 O  OH    . TYR B 2 399 ? 135.617 135.678 119.841 1.00 50.42  ? 399 TYR A OH    1 
ATOM   6404 N  N     . ALA B 2 400 ? 142.318 138.544 121.946 1.00 46.74  ? 400 ALA A N     1 
ATOM   6405 C  CA    . ALA B 2 400 ? 142.991 137.392 122.534 1.00 39.37  ? 400 ALA A CA    1 
ATOM   6406 C  C     . ALA B 2 400 ? 142.655 137.252 124.013 1.00 43.88  ? 400 ALA A C     1 
ATOM   6407 O  O     . ALA B 2 400 ? 142.398 136.145 124.496 1.00 46.64  ? 400 ALA A O     1 
ATOM   6408 C  CB    . ALA B 2 400 ? 144.500 137.507 122.335 1.00 44.83  ? 400 ALA A CB    1 
ATOM   6409 N  N     . LYS B 2 401 ? 142.650 138.364 124.748 1.00 52.26  ? 401 LYS A N     1 
ATOM   6410 C  CA    . LYS B 2 401 ? 142.252 138.371 126.149 1.00 43.71  ? 401 LYS A CA    1 
ATOM   6411 C  C     . LYS B 2 401 ? 140.743 138.394 126.334 1.00 44.07  ? 401 LYS A C     1 
ATOM   6412 O  O     . LYS B 2 401 ? 140.271 138.197 127.456 1.00 47.19  ? 401 LYS A O     1 
ATOM   6413 C  CB    . LYS B 2 401 ? 142.862 139.579 126.857 1.00 42.11  ? 401 LYS A CB    1 
ATOM   6414 C  CG    . LYS B 2 401 ? 144.367 139.620 126.824 1.00 44.70  ? 401 LYS A CG    1 
ATOM   6415 C  CD    . LYS B 2 401 ? 144.956 138.623 127.794 1.00 42.63  ? 401 LYS A CD    1 
ATOM   6416 C  CE    . LYS B 2 401 ? 146.467 138.708 127.818 1.00 48.19  ? 401 LYS A CE    1 
ATOM   6417 N  NZ    . LYS B 2 401 ? 147.059 138.357 126.500 1.00 50.52  ? 401 LYS A NZ    1 
ATOM   6418 N  N     . ARG B 2 402 ? 139.988 138.624 125.264 1.00 49.35  ? 402 ARG A N     1 
ATOM   6419 C  CA    . ARG B 2 402 ? 138.536 138.773 125.307 1.00 44.77  ? 402 ARG A CA    1 
ATOM   6420 C  C     . ARG B 2 402 ? 138.126 139.875 126.282 1.00 43.62  ? 402 ARG A C     1 
ATOM   6421 O  O     . ARG B 2 402 ? 137.342 139.674 127.208 1.00 46.88  ? 402 ARG A O     1 
ATOM   6422 C  CB    . ARG B 2 402 ? 137.850 137.448 125.637 1.00 42.17  ? 402 ARG A CB    1 
ATOM   6423 C  CG    . ARG B 2 402 ? 137.287 136.774 124.408 1.00 45.92  ? 402 ARG A CG    1 
ATOM   6424 C  CD    . ARG B 2 402 ? 137.104 135.298 124.611 1.00 50.75  ? 402 ARG A CD    1 
ATOM   6425 N  NE    . ARG B 2 402 ? 136.592 134.651 123.411 1.00 55.91  ? 402 ARG A NE    1 
ATOM   6426 C  CZ    . ARG B 2 402 ? 137.342 134.284 122.382 1.00 53.32  ? 402 ARG A CZ    1 
ATOM   6427 N  NH1   . ARG B 2 402 ? 138.650 134.471 122.379 1.00 45.33  ? 402 ARG A NH1   1 
ATOM   6428 N  NH2   . ARG B 2 402 ? 136.765 133.704 121.334 1.00 50.37  ? 402 ARG A NH2   1 
ATOM   6429 N  N     . ALA B 2 403 ? 138.672 141.059 126.040 1.00 41.66  ? 403 ALA A N     1 
ATOM   6430 C  CA    . ALA B 2 403 ? 138.325 142.243 126.801 1.00 35.07  ? 403 ALA A CA    1 
ATOM   6431 C  C     . ALA B 2 403 ? 137.122 142.923 126.170 1.00 41.92  ? 403 ALA A C     1 
ATOM   6432 O  O     . ALA B 2 403 ? 136.991 142.962 124.945 1.00 52.40  ? 403 ALA A O     1 
ATOM   6433 C  CB    . ALA B 2 403 ? 139.503 143.212 126.859 1.00 37.90  ? 403 ALA A CB    1 
ATOM   6434 N  N     . PHE B 2 404 ? 136.236 143.436 127.015 1.00 36.68  ? 404 PHE A N     1 
ATOM   6435 C  CA    . PHE B 2 404 ? 135.033 144.156 126.615 1.00 29.23  ? 404 PHE A CA    1 
ATOM   6436 C  C     . PHE B 2 404 ? 134.047 143.295 125.836 1.00 34.26  ? 404 PHE A C     1 
ATOM   6437 O  O     . PHE B 2 404 ? 133.052 143.817 125.326 1.00 46.01  ? 404 PHE A O     1 
ATOM   6438 C  CB    . PHE B 2 404 ? 135.369 145.407 125.793 1.00 37.07  ? 404 PHE A CB    1 
ATOM   6439 C  CG    . PHE B 2 404 ? 136.324 146.348 126.464 1.00 35.83  ? 404 PHE A CG    1 
ATOM   6440 C  CD1   . PHE B 2 404 ? 135.882 147.219 127.435 1.00 35.06  ? 404 PHE A CD1   1 
ATOM   6441 C  CD2   . PHE B 2 404 ? 137.652 146.387 126.101 1.00 37.03  ? 404 PHE A CD2   1 
ATOM   6442 C  CE1   . PHE B 2 404 ? 136.748 148.094 128.044 1.00 38.28  ? 404 PHE A CE1   1 
ATOM   6443 C  CE2   . PHE B 2 404 ? 138.521 147.263 126.710 1.00 38.48  ? 404 PHE A CE2   1 
ATOM   6444 C  CZ    . PHE B 2 404 ? 138.068 148.115 127.682 1.00 40.66  ? 404 PHE A CZ    1 
ATOM   6445 N  N     . VAL B 2 405 ? 134.284 141.988 125.730 1.00 35.82  ? 405 VAL A N     1 
ATOM   6446 C  CA    . VAL B 2 405 ? 133.361 141.139 124.985 1.00 37.03  ? 405 VAL A CA    1 
ATOM   6447 C  C     . VAL B 2 405 ? 132.071 140.925 125.765 1.00 39.18  ? 405 VAL A C     1 
ATOM   6448 O  O     . VAL B 2 405 ? 131.015 140.685 125.170 1.00 47.39  ? 405 VAL A O     1 
ATOM   6449 C  CB    . VAL B 2 405 ? 134.037 139.807 124.616 1.00 37.48  ? 405 VAL A CB    1 
ATOM   6450 C  CG1   . VAL B 2 405 ? 133.108 138.938 123.800 1.00 43.89  ? 405 VAL A CG1   1 
ATOM   6451 C  CG2   . VAL B 2 405 ? 135.305 140.064 123.843 1.00 41.94  ? 405 VAL A CG2   1 
ATOM   6452 N  N     . HIS B 2 406 ? 132.115 141.038 127.092 1.00 36.13  ? 406 HIS A N     1 
ATOM   6453 C  CA    . HIS B 2 406 ? 130.907 140.839 127.885 1.00 36.88  ? 406 HIS A CA    1 
ATOM   6454 C  C     . HIS B 2 406 ? 129.877 141.932 127.637 1.00 39.84  ? 406 HIS A C     1 
ATOM   6455 O  O     . HIS B 2 406 ? 128.677 141.697 127.812 1.00 46.17  ? 406 HIS A O     1 
ATOM   6456 C  CB    . HIS B 2 406 ? 131.252 140.761 129.368 1.00 32.48  ? 406 HIS A CB    1 
ATOM   6457 C  CG    . HIS B 2 406 ? 131.674 142.064 129.966 1.00 35.19  ? 406 HIS A CG    1 
ATOM   6458 N  ND1   . HIS B 2 406 ? 132.922 142.608 129.763 1.00 42.84  ? 406 HIS A ND1   1 
ATOM   6459 C  CD2   . HIS B 2 406 ? 131.020 142.922 130.784 1.00 37.16  ? 406 HIS A CD2   1 
ATOM   6460 C  CE1   . HIS B 2 406 ? 133.014 143.751 130.416 1.00 42.36  ? 406 HIS A CE1   1 
ATOM   6461 N  NE2   . HIS B 2 406 ? 131.874 143.965 131.043 1.00 38.11  ? 406 HIS A NE2   1 
ATOM   6462 N  N     . TRP B 2 407 ? 130.314 143.127 127.240 1.00 43.18  ? 407 TRP A N     1 
ATOM   6463 C  CA    . TRP B 2 407 ? 129.364 144.175 126.882 1.00 39.41  ? 407 TRP A CA    1 
ATOM   6464 C  C     . TRP B 2 407 ? 128.569 143.795 125.644 1.00 39.56  ? 407 TRP A C     1 
ATOM   6465 O  O     . TRP B 2 407 ? 127.368 144.069 125.560 1.00 45.73  ? 407 TRP A O     1 
ATOM   6466 C  CB    . TRP B 2 407 ? 130.092 145.496 126.650 1.00 36.68  ? 407 TRP A CB    1 
ATOM   6467 C  CG    . TRP B 2 407 ? 130.552 146.184 127.891 1.00 36.50  ? 407 TRP A CG    1 
ATOM   6468 C  CD1   . TRP B 2 407 ? 131.835 146.409 128.268 1.00 35.99  ? 407 TRP A CD1   1 
ATOM   6469 C  CD2   . TRP B 2 407 ? 129.729 146.745 128.916 1.00 36.82  ? 407 TRP A CD2   1 
ATOM   6470 N  NE1   . TRP B 2 407 ? 131.868 147.076 129.463 1.00 42.57  ? 407 TRP A NE1   1 
ATOM   6471 C  CE2   . TRP B 2 407 ? 130.584 147.288 129.884 1.00 38.45  ? 407 TRP A CE2   1 
ATOM   6472 C  CE3   . TRP B 2 407 ? 128.351 146.835 129.110 1.00 40.89  ? 407 TRP A CE3   1 
ATOM   6473 C  CZ2   . TRP B 2 407 ? 130.109 147.917 131.025 1.00 38.02  ? 407 TRP A CZ2   1 
ATOM   6474 C  CZ3   . TRP B 2 407 ? 127.885 147.457 130.241 1.00 39.64  ? 407 TRP A CZ3   1 
ATOM   6475 C  CH2   . TRP B 2 407 ? 128.759 147.991 131.184 1.00 37.08  ? 407 TRP A CH2   1 
ATOM   6476 N  N     . TYR B 2 408 ? 129.224 143.162 124.672 1.00 41.98  ? 408 TYR A N     1 
ATOM   6477 C  CA    . TYR B 2 408 ? 128.580 142.841 123.406 1.00 40.19  ? 408 TYR A CA    1 
ATOM   6478 C  C     . TYR B 2 408 ? 127.655 141.636 123.522 1.00 45.68  ? 408 TYR A C     1 
ATOM   6479 O  O     . TYR B 2 408 ? 126.605 141.598 122.873 1.00 54.93  ? 408 TYR A O     1 
ATOM   6480 C  CB    . TYR B 2 408 ? 129.641 142.605 122.337 1.00 37.77  ? 408 TYR A CB    1 
ATOM   6481 C  CG    . TYR B 2 408 ? 130.357 143.861 121.923 1.00 46.11  ? 408 TYR A CG    1 
ATOM   6482 C  CD1   . TYR B 2 408 ? 131.365 144.391 122.703 1.00 44.19  ? 408 TYR A CD1   1 
ATOM   6483 C  CD2   . TYR B 2 408 ? 130.020 144.519 120.757 1.00 43.88  ? 408 TYR A CD2   1 
ATOM   6484 C  CE1   . TYR B 2 408 ? 132.019 145.539 122.336 1.00 44.20  ? 408 TYR A CE1   1 
ATOM   6485 C  CE2   . TYR B 2 408 ? 130.670 145.664 120.380 1.00 42.94  ? 408 TYR A CE2   1 
ATOM   6486 C  CZ    . TYR B 2 408 ? 131.667 146.172 121.174 1.00 46.62  ? 408 TYR A CZ    1 
ATOM   6487 O  OH    . TYR B 2 408 ? 132.316 147.319 120.795 1.00 51.66  ? 408 TYR A OH    1 
ATOM   6488 N  N     . VAL B 2 409 ? 128.019 140.644 124.339 1.00 42.42  ? 409 VAL A N     1 
ATOM   6489 C  CA    . VAL B 2 409 ? 127.175 139.461 124.500 1.00 37.77  ? 409 VAL A CA    1 
ATOM   6490 C  C     . VAL B 2 409 ? 126.009 139.683 125.446 1.00 42.27  ? 409 VAL A C     1 
ATOM   6491 O  O     . VAL B 2 409 ? 125.072 138.878 125.453 1.00 46.77  ? 409 VAL A O     1 
ATOM   6492 C  CB    . VAL B 2 409 ? 127.981 138.250 125.000 1.00 36.14  ? 409 VAL A CB    1 
ATOM   6493 C  CG1   . VAL B 2 409 ? 129.127 137.958 124.064 1.00 37.51  ? 409 VAL A CG1   1 
ATOM   6494 C  CG2   . VAL B 2 409 ? 128.491 138.502 126.397 1.00 41.41  ? 409 VAL A CG2   1 
ATOM   6495 N  N     . GLY B 2 410 ? 126.032 140.742 126.240 1.00 47.93  ? 410 GLY A N     1 
ATOM   6496 C  CA    . GLY B 2 410 ? 124.892 141.055 127.065 1.00 47.27  ? 410 GLY A CA    1 
ATOM   6497 C  C     . GLY B 2 410 ? 123.768 141.742 126.340 1.00 48.66  ? 410 GLY A C     1 
ATOM   6498 O  O     . GLY B 2 410 ? 122.736 142.039 126.945 1.00 56.70  ? 410 GLY A O     1 
ATOM   6499 N  N     . GLU B 2 411 ? 123.944 142.008 125.047 1.00 46.40  ? 411 GLU A N     1 
ATOM   6500 C  CA    . GLU B 2 411 ? 122.919 142.620 124.215 1.00 54.59  ? 411 GLU A CA    1 
ATOM   6501 C  C     . GLU B 2 411 ? 122.387 141.660 123.158 1.00 60.47  ? 411 GLU A C     1 
ATOM   6502 O  O     . GLU B 2 411 ? 121.708 142.089 122.221 1.00 63.25  ? 411 GLU A O     1 
ATOM   6503 C  CB    . GLU B 2 411 ? 123.461 143.888 123.558 1.00 54.75  ? 411 GLU A CB    1 
ATOM   6504 C  CG    . GLU B 2 411 ? 123.926 144.945 124.540 1.00 54.74  ? 411 GLU A CG    1 
ATOM   6505 C  CD    . GLU B 2 411 ? 122.774 145.633 125.239 1.00 61.56  ? 411 GLU A CD    1 
ATOM   6506 O  OE1   . GLU B 2 411 ? 121.675 145.698 124.650 1.00 63.57  ? 411 GLU A OE1   1 
ATOM   6507 O  OE2   . GLU B 2 411 ? 122.965 146.110 126.376 1.00 61.43  ? 411 GLU A OE2   1 
ATOM   6508 N  N     . GLY B 2 412 ? 122.681 140.371 123.288 1.00 57.95  ? 412 GLY A N     1 
ATOM   6509 C  CA    . GLY B 2 412 ? 122.150 139.380 122.379 1.00 55.57  ? 412 GLY A CA    1 
ATOM   6510 C  C     . GLY B 2 412 ? 123.044 138.993 121.226 1.00 54.87  ? 412 GLY A C     1 
ATOM   6511 O  O     . GLY B 2 412 ? 122.550 138.429 120.245 1.00 64.09  ? 412 GLY A O     1 
ATOM   6512 N  N     . MET B 2 413 ? 124.337 139.270 121.305 1.00 49.57  ? 413 MET A N     1 
ATOM   6513 C  CA    . MET B 2 413 ? 125.277 138.958 120.241 1.00 50.00  ? 413 MET A CA    1 
ATOM   6514 C  C     . MET B 2 413 ? 126.099 137.745 120.643 1.00 55.59  ? 413 MET A C     1 
ATOM   6515 O  O     . MET B 2 413 ? 126.688 137.723 121.728 1.00 64.20  ? 413 MET A O     1 
ATOM   6516 C  CB    . MET B 2 413 ? 126.192 140.151 119.962 1.00 54.40  ? 413 MET A CB    1 
ATOM   6517 C  CG    . MET B 2 413 ? 126.942 140.073 118.653 1.00 57.71  ? 413 MET A CG    1 
ATOM   6518 S  SD    . MET B 2 413 ? 127.711 141.631 118.196 1.00 68.42  ? 413 MET A SD    1 
ATOM   6519 C  CE    . MET B 2 413 ? 128.184 141.286 116.508 1.00 59.56  ? 413 MET A CE    1 
ATOM   6520 N  N     . GLU B 2 414 ? 126.135 136.738 119.777 1.00 63.85  ? 414 GLU A N     1 
ATOM   6521 C  CA    . GLU B 2 414 ? 126.947 135.566 120.049 1.00 64.00  ? 414 GLU A CA    1 
ATOM   6522 C  C     . GLU B 2 414 ? 128.426 135.897 119.880 1.00 65.06  ? 414 GLU A C     1 
ATOM   6523 O  O     . GLU B 2 414 ? 128.807 136.974 119.417 1.00 68.38  ? 414 GLU A O     1 
ATOM   6524 C  CB    . GLU B 2 414 ? 126.561 134.411 119.130 1.00 63.80  ? 414 GLU A CB    1 
ATOM   6525 C  CG    . GLU B 2 414 ? 125.169 133.865 119.361 1.00 71.52  ? 414 GLU A CG    1 
ATOM   6526 C  CD    . GLU B 2 414 ? 124.958 132.522 118.692 1.00 73.40  ? 414 GLU A CD    1 
ATOM   6527 O  OE1   . GLU B 2 414 ? 125.951 131.930 118.219 1.00 73.50  ? 414 GLU A OE1   1 
ATOM   6528 O  OE2   . GLU B 2 414 ? 123.800 132.057 118.640 1.00 71.70  ? 414 GLU A OE2   1 
ATOM   6529 N  N     . GLU B 2 415 ? 129.265 134.943 120.258 1.00 60.94  ? 415 GLU A N     1 
ATOM   6530 C  CA    . GLU B 2 415 ? 130.708 135.109 120.214 1.00 60.64  ? 415 GLU A CA    1 
ATOM   6531 C  C     . GLU B 2 415 ? 131.319 134.663 118.895 1.00 65.99  ? 415 GLU A C     1 
ATOM   6532 O  O     . GLU B 2 415 ? 132.530 134.814 118.709 1.00 70.75  ? 415 GLU A O     1 
ATOM   6533 C  CB    . GLU B 2 415 ? 131.349 134.334 121.365 1.00 63.13  ? 415 GLU A CB    1 
ATOM   6534 C  CG    . GLU B 2 415 ? 132.525 135.034 122.007 1.00 66.04  ? 415 GLU A CG    1 
ATOM   6535 C  CD    . GLU B 2 415 ? 133.041 134.292 123.220 1.00 70.58  ? 415 GLU A CD    1 
ATOM   6536 O  OE1   . GLU B 2 415 ? 132.286 133.474 123.783 1.00 71.28  ? 415 GLU A OE1   1 
ATOM   6537 O  OE2   . GLU B 2 415 ? 134.202 134.526 123.611 1.00 68.22  ? 415 GLU A OE2   1 
ATOM   6538 N  N     . GLY B 2 416 ? 130.524 134.120 117.981 1.00 61.65  ? 416 GLY A N     1 
ATOM   6539 C  CA    . GLY B 2 416 ? 131.043 133.662 116.709 1.00 58.96  ? 416 GLY A CA    1 
ATOM   6540 C  C     . GLY B 2 416 ? 131.049 134.740 115.649 1.00 64.26  ? 416 GLY A C     1 
ATOM   6541 O  O     . GLY B 2 416 ? 131.739 134.616 114.629 1.00 69.20  ? 416 GLY A O     1 
ATOM   6542 N  N     . GLU B 2 417 ? 130.284 135.808 115.881 1.00 65.01  ? 417 GLU A N     1 
ATOM   6543 C  CA    . GLU B 2 417 ? 130.283 136.929 114.949 1.00 66.05  ? 417 GLU A CA    1 
ATOM   6544 C  C     . GLU B 2 417 ? 131.670 137.542 114.828 1.00 69.83  ? 417 GLU A C     1 
ATOM   6545 O  O     . GLU B 2 417 ? 132.075 137.968 113.741 1.00 73.21  ? 417 GLU A O     1 
ATOM   6546 C  CB    . GLU B 2 417 ? 129.279 137.988 115.395 1.00 65.80  ? 417 GLU A CB    1 
ATOM   6547 C  CG    . GLU B 2 417 ? 127.856 137.744 114.946 1.00 68.41  ? 417 GLU A CG    1 
ATOM   6548 C  CD    . GLU B 2 417 ? 127.070 136.926 115.941 1.00 75.11  ? 417 GLU A CD    1 
ATOM   6549 O  OE1   . GLU B 2 417 ? 127.695 136.316 116.832 1.00 76.29  ? 417 GLU A OE1   1 
ATOM   6550 O  OE2   . GLU B 2 417 ? 125.827 136.902 115.841 1.00 74.89  ? 417 GLU A OE2   1 
ATOM   6551 N  N     . PHE B 2 418 ? 132.410 137.602 115.935 1.00 52.65  ? 418 PHE A N     1 
ATOM   6552 C  CA    . PHE B 2 418 ? 133.745 138.185 115.900 1.00 50.23  ? 418 PHE A CA    1 
ATOM   6553 C  C     . PHE B 2 418 ? 134.660 137.392 114.980 1.00 53.96  ? 418 PHE A C     1 
ATOM   6554 O  O     . PHE B 2 418 ? 135.344 137.960 114.117 1.00 65.94  ? 418 PHE A O     1 
ATOM   6555 C  CB    . PHE B 2 418 ? 134.329 138.244 117.310 1.00 57.52  ? 418 PHE A CB    1 
ATOM   6556 C  CG    . PHE B 2 418 ? 133.616 139.187 118.233 1.00 54.93  ? 418 PHE A CG    1 
ATOM   6557 C  CD1   . PHE B 2 418 ? 132.430 138.828 118.836 1.00 57.04  ? 418 PHE A CD1   1 
ATOM   6558 C  CD2   . PHE B 2 418 ? 134.154 140.421 118.524 1.00 52.98  ? 418 PHE A CD2   1 
ATOM   6559 C  CE1   . PHE B 2 418 ? 131.786 139.691 119.693 1.00 55.66  ? 418 PHE A CE1   1 
ATOM   6560 C  CE2   . PHE B 2 418 ? 133.512 141.282 119.376 1.00 52.81  ? 418 PHE A CE2   1 
ATOM   6561 C  CZ    . PHE B 2 418 ? 132.329 140.914 119.963 1.00 54.15  ? 418 PHE A CZ    1 
ATOM   6562 N  N     . SER B 2 419 ? 134.677 136.071 115.147 1.00 54.10  ? 419 SER A N     1 
ATOM   6563 C  CA    . SER B 2 419 ? 135.510 135.227 114.301 1.00 53.76  ? 419 SER A CA    1 
ATOM   6564 C  C     . SER B 2 419 ? 135.071 135.300 112.846 1.00 55.94  ? 419 SER A C     1 
ATOM   6565 O  O     . SER B 2 419 ? 135.911 135.346 111.939 1.00 63.50  ? 419 SER A O     1 
ATOM   6566 C  CB    . SER B 2 419 ? 135.474 133.786 114.804 1.00 54.37  ? 419 SER A CB    1 
ATOM   6567 O  OG    . SER B 2 419 ? 134.142 133.321 114.918 1.00 60.35  ? 419 SER A OG    1 
ATOM   6568 N  N     . GLU B 2 420 ? 133.759 135.313 112.601 1.00 51.64  ? 420 GLU A N     1 
ATOM   6569 C  CA    . GLU B 2 420 ? 133.275 135.389 111.228 1.00 53.87  ? 420 GLU A CA    1 
ATOM   6570 C  C     . GLU B 2 420 ? 133.705 136.688 110.559 1.00 57.78  ? 420 GLU A C     1 
ATOM   6571 O  O     . GLU B 2 420 ? 134.151 136.686 109.404 1.00 60.82  ? 420 GLU A O     1 
ATOM   6572 C  CB    . GLU B 2 420 ? 131.757 135.249 111.201 1.00 58.40  ? 420 GLU A CB    1 
ATOM   6573 C  CG    . GLU B 2 420 ? 131.266 133.847 111.499 1.00 61.98  ? 420 GLU A CG    1 
ATOM   6574 C  CD    . GLU B 2 420 ? 129.758 133.726 111.415 1.00 67.54  ? 420 GLU A CD    1 
ATOM   6575 O  OE1   . GLU B 2 420 ? 129.105 134.698 110.981 1.00 65.01  ? 420 GLU A OE1   1 
ATOM   6576 O  OE2   . GLU B 2 420 ? 129.225 132.658 111.784 1.00 65.88  ? 420 GLU A OE2   1 
ATOM   6577 N  N     . ALA B 2 421 ? 133.591 137.809 111.271 1.00 53.89  ? 421 ALA A N     1 
ATOM   6578 C  CA    . ALA B 2 421 ? 133.982 139.090 110.699 1.00 51.53  ? 421 ALA A CA    1 
ATOM   6579 C  C     . ALA B 2 421 ? 135.483 139.157 110.464 1.00 50.38  ? 421 ALA A C     1 
ATOM   6580 O  O     . ALA B 2 421 ? 135.936 139.706 109.450 1.00 61.12  ? 421 ALA A O     1 
ATOM   6581 C  CB    . ALA B 2 421 ? 133.524 140.225 111.609 1.00 55.02  ? 421 ALA A CB    1 
ATOM   6582 N  N     . ARG B 2 422 ? 136.273 138.608 111.386 1.00 42.47  ? 422 ARG A N     1 
ATOM   6583 C  CA    . ARG B 2 422 ? 137.714 138.577 111.176 1.00 45.42  ? 422 ARG A CA    1 
ATOM   6584 C  C     . ARG B 2 422 ? 138.075 137.735 109.954 1.00 53.85  ? 422 ARG A C     1 
ATOM   6585 O  O     . ARG B 2 422 ? 138.960 138.107 109.172 1.00 62.57  ? 422 ARG A O     1 
ATOM   6586 C  CB    . ARG B 2 422 ? 138.408 138.058 112.433 1.00 46.42  ? 422 ARG A CB    1 
ATOM   6587 C  CG    . ARG B 2 422 ? 139.913 138.150 112.388 1.00 47.87  ? 422 ARG A CG    1 
ATOM   6588 C  CD    . ARG B 2 422 ? 140.365 139.572 112.179 1.00 48.96  ? 422 ARG A CD    1 
ATOM   6589 N  NE    . ARG B 2 422 ? 141.811 139.693 112.292 1.00 49.40  ? 422 ARG A NE    1 
ATOM   6590 C  CZ    . ARG B 2 422 ? 142.665 139.354 111.338 1.00 51.24  ? 422 ARG A CZ    1 
ATOM   6591 N  NH1   . ARG B 2 422 ? 142.253 138.859 110.185 1.00 47.52  ? 422 ARG A NH1   1 
ATOM   6592 N  NH2   . ARG B 2 422 ? 143.968 139.513 111.549 1.00 55.71  ? 422 ARG A NH2   1 
ATOM   6593 N  N     . GLU B 2 423 ? 137.386 136.607 109.761 1.00 54.79  ? 423 GLU A N     1 
ATOM   6594 C  CA    . GLU B 2 423 ? 137.618 135.789 108.573 1.00 51.94  ? 423 GLU A CA    1 
ATOM   6595 C  C     . GLU B 2 423 ? 137.249 136.538 107.297 1.00 59.08  ? 423 GLU A C     1 
ATOM   6596 O  O     . GLU B 2 423 ? 137.957 136.444 106.287 1.00 65.46  ? 423 GLU A O     1 
ATOM   6597 C  CB    . GLU B 2 423 ? 136.832 134.485 108.670 1.00 54.56  ? 423 GLU A CB    1 
ATOM   6598 C  CG    . GLU B 2 423 ? 137.386 133.504 109.683 1.00 61.47  ? 423 GLU A CG    1 
ATOM   6599 C  CD    . GLU B 2 423 ? 138.812 133.094 109.380 1.00 69.00  ? 423 GLU A CD    1 
ATOM   6600 O  OE1   . GLU B 2 423 ? 139.129 132.873 108.192 1.00 67.74  ? 423 GLU A OE1   1 
ATOM   6601 O  OE2   . GLU B 2 423 ? 139.618 132.991 110.329 1.00 67.75  ? 423 GLU A OE2   1 
ATOM   6602 N  N     . ASP B 2 424 ? 136.136 137.275 107.320 1.00 57.09  ? 424 ASP A N     1 
ATOM   6603 C  CA    . ASP B 2 424 ? 135.748 138.059 106.149 1.00 56.09  ? 424 ASP A CA    1 
ATOM   6604 C  C     . ASP B 2 424 ? 136.796 139.113 105.817 1.00 56.13  ? 424 ASP A C     1 
ATOM   6605 O  O     . ASP B 2 424 ? 137.144 139.310 104.643 1.00 60.45  ? 424 ASP A O     1 
ATOM   6606 C  CB    . ASP B 2 424 ? 134.392 138.713 106.384 1.00 55.90  ? 424 ASP A CB    1 
ATOM   6607 C  CG    . ASP B 2 424 ? 133.271 137.706 106.483 1.00 62.90  ? 424 ASP A CG    1 
ATOM   6608 O  OD1   . ASP B 2 424 ? 133.319 136.691 105.757 1.00 62.78  ? 424 ASP A OD1   1 
ATOM   6609 O  OD2   . ASP B 2 424 ? 132.343 137.926 107.288 1.00 66.58  ? 424 ASP A OD2   1 
ATOM   6610 N  N     . MET B 2 425 ? 137.316 139.798 106.835 1.00 48.66  ? 425 MET A N     1 
ATOM   6611 C  CA    . MET B 2 425 ? 138.368 140.781 106.594 1.00 48.11  ? 425 MET A CA    1 
ATOM   6612 C  C     . MET B 2 425 ? 139.616 140.127 106.019 1.00 51.27  ? 425 MET A C     1 
ATOM   6613 O  O     . MET B 2 425 ? 140.254 140.677 105.111 1.00 59.80  ? 425 MET A O     1 
ATOM   6614 C  CB    . MET B 2 425 ? 138.707 141.524 107.882 1.00 52.80  ? 425 MET A CB    1 
ATOM   6615 C  CG    . MET B 2 425 ? 138.140 142.921 107.971 1.00 57.31  ? 425 MET A CG    1 
ATOM   6616 S  SD    . MET B 2 425 ? 138.278 143.843 106.434 1.00 69.80  ? 425 MET A SD    1 
ATOM   6617 C  CE    . MET B 2 425 ? 140.050 143.889 106.255 1.00 56.42  ? 425 MET A CE    1 
ATOM   6618 N  N     . ALA B 2 426 ? 139.989 138.958 106.542 1.00 49.09  ? 426 ALA A N     1 
ATOM   6619 C  CA    . ALA B 2 426 ? 141.163 138.268 106.021 1.00 46.18  ? 426 ALA A CA    1 
ATOM   6620 C  C     . ALA B 2 426 ? 140.972 137.891 104.559 1.00 49.08  ? 426 ALA A C     1 
ATOM   6621 O  O     . ALA B 2 426 ? 141.890 138.043 103.740 1.00 54.54  ? 426 ALA A O     1 
ATOM   6622 C  CB    . ALA B 2 426 ? 141.459 137.029 106.862 1.00 47.56  ? 426 ALA A CB    1 
ATOM   6623 N  N     . ALA B 2 427 ? 139.781 137.406 104.211 1.00 44.72  ? 427 ALA A N     1 
ATOM   6624 C  CA    . ALA B 2 427 ? 139.502 137.056 102.826 1.00 47.36  ? 427 ALA A CA    1 
ATOM   6625 C  C     . ALA B 2 427 ? 139.582 138.276 101.921 1.00 51.61  ? 427 ALA A C     1 
ATOM   6626 O  O     . ALA B 2 427 ? 140.133 138.203 100.817 1.00 55.99  ? 427 ALA A O     1 
ATOM   6627 C  CB    . ALA B 2 427 ? 138.129 136.398 102.720 1.00 51.96  ? 427 ALA A CB    1 
ATOM   6628 N  N     . LEU B 2 428 ? 139.036 139.407 102.369 1.00 50.77  ? 428 LEU A N     1 
ATOM   6629 C  CA    . LEU B 2 428 ? 139.098 140.621 101.560 1.00 45.77  ? 428 LEU A CA    1 
ATOM   6630 C  C     . LEU B 2 428 ? 140.537 141.070 101.341 1.00 48.10  ? 428 LEU A C     1 
ATOM   6631 O  O     . LEU B 2 428 ? 140.915 141.460 100.226 1.00 60.22  ? 428 LEU A O     1 
ATOM   6632 C  CB    . LEU B 2 428 ? 138.282 141.730 102.220 1.00 53.22  ? 428 LEU A CB    1 
ATOM   6633 C  CG    . LEU B 2 428 ? 138.006 142.988 101.403 1.00 54.27  ? 428 LEU A CG    1 
ATOM   6634 C  CD1   . LEU B 2 428 ? 137.294 142.643 100.117 1.00 52.53  ? 428 LEU A CD1   1 
ATOM   6635 C  CD2   . LEU B 2 428 ? 137.187 143.969 102.210 1.00 50.24  ? 428 LEU A CD2   1 
ATOM   6636 N  N     . GLU B 2 429 ? 141.356 141.021 102.392 1.00 47.39  ? 429 GLU A N     1 
ATOM   6637 C  CA    . GLU B 2 429 ? 142.752 141.422 102.250 1.00 48.98  ? 429 GLU A CA    1 
ATOM   6638 C  C     . GLU B 2 429 ? 143.492 140.512 101.280 1.00 53.64  ? 429 GLU A C     1 
ATOM   6639 O  O     . GLU B 2 429 ? 144.268 140.984 100.437 1.00 62.91  ? 429 GLU A O     1 
ATOM   6640 C  CB    . GLU B 2 429 ? 143.438 141.421 103.612 1.00 52.23  ? 429 GLU A CB    1 
ATOM   6641 C  CG    . GLU B 2 429 ? 142.975 142.521 104.535 1.00 61.48  ? 429 GLU A CG    1 
ATOM   6642 C  CD    . GLU B 2 429 ? 143.831 142.629 105.776 1.00 63.80  ? 429 GLU A CD    1 
ATOM   6643 O  OE1   . GLU B 2 429 ? 144.978 142.136 105.752 1.00 66.22  ? 429 GLU A OE1   1 
ATOM   6644 O  OE2   . GLU B 2 429 ? 143.361 143.210 106.776 1.00 63.38  ? 429 GLU A OE2   1 
ATOM   6645 N  N     . LYS B 2 430 ? 143.260 139.203 101.378 1.00 53.08  ? 430 LYS A N     1 
ATOM   6646 C  CA    . LYS B 2 430 ? 143.920 138.280 100.464 1.00 54.00  ? 430 LYS A CA    1 
ATOM   6647 C  C     . LYS B 2 430 ? 143.455 138.501 99.030  1.00 53.41  ? 430 LYS A C     1 
ATOM   6648 O  O     . LYS B 2 430 ? 144.251 138.392 98.091  1.00 58.70  ? 430 LYS A O     1 
ATOM   6649 C  CB    . LYS B 2 430 ? 143.671 136.838 100.902 1.00 57.35  ? 430 LYS A CB    1 
ATOM   6650 C  CG    . LYS B 2 430 ? 144.270 135.793 99.983  1.00 59.83  ? 430 LYS A CG    1 
ATOM   6651 C  CD    . LYS B 2 430 ? 143.941 134.391 100.459 1.00 59.13  ? 430 LYS A CD    1 
ATOM   6652 C  CE    . LYS B 2 430 ? 144.521 133.343 99.526  1.00 58.31  ? 430 LYS A CE    1 
ATOM   6653 N  NZ    . LYS B 2 430 ? 144.193 131.960 99.972  1.00 57.95  ? 430 LYS A NZ    1 
ATOM   6654 N  N     . ASP B 2 431 ? 142.241 138.986 98.837  1.00 53.45  ? 431 ASP A N     1 
ATOM   6655 C  CA    . ASP B 2 431 ? 141.798 139.349 97.465  1.00 54.32  ? 431 ASP A CA    1 
ATOM   6656 C  C     . ASP B 2 431 ? 142.579 140.557 96.954  1.00 53.68  ? 431 ASP A C     1 
ATOM   6657 O  O     . ASP B 2 431 ? 143.092 140.496 95.835  1.00 57.44  ? 431 ASP A O     1 
ATOM   6658 C  CB    . ASP B 2 431 ? 140.317 139.641 97.412  1.00 53.67  ? 431 ASP A CB    1 
ATOM   6659 C  CG    . ASP B 2 431 ? 139.418 138.416 97.447  1.00 64.94  ? 431 ASP A CG    1 
ATOM   6660 O  OD1   . ASP B 2 431 ? 139.872 137.371 97.956  1.00 64.11  ? 431 ASP A OD1   1 
ATOM   6661 O  OD2   . ASP B 2 431 ? 138.274 138.519 96.961  1.00 67.19  ? 431 ASP A OD2   1 
ATOM   6662 N  N     . TYR B 2 432 ? 142.660 141.620 97.732  1.00 44.95  ? 432 TYR A N     1 
ATOM   6663 C  CA    . TYR B 2 432 ? 143.318 142.844 97.236  1.00 45.52  ? 432 TYR A CA    1 
ATOM   6664 C  C     . TYR B 2 432 ? 144.771 142.508 97.012  1.00 50.17  ? 432 TYR A C     1 
ATOM   6665 O  O     . TYR B 2 432 ? 145.384 143.166 96.159  1.00 56.70  ? 432 TYR A O     1 
ATOM   6666 C  CB    . TYR B 2 432 ? 143.073 144.024 98.176  1.00 47.69  ? 432 TYR A CB    1 
ATOM   6667 C  CG    . TYR B 2 432 ? 142.018 145.038 97.761  1.00 49.58  ? 432 TYR A CG    1 
ATOM   6668 C  CD1   . TYR B 2 432 ? 142.372 146.207 97.108  1.00 50.43  ? 432 TYR A CD1   1 
ATOM   6669 C  CD2   . TYR B 2 432 ? 140.678 144.848 98.061  1.00 48.52  ? 432 TYR A CD2   1 
ATOM   6670 C  CE1   . TYR B 2 432 ? 141.425 147.143 96.737  1.00 48.51  ? 432 TYR A CE1   1 
ATOM   6671 C  CE2   . TYR B 2 432 ? 139.719 145.777 97.700  1.00 52.20  ? 432 TYR A CE2   1 
ATOM   6672 C  CZ    . TYR B 2 432 ? 140.097 146.930 97.041  1.00 46.47  ? 432 TYR A CZ    1 
ATOM   6673 O  OH    . TYR B 2 432 ? 139.171 147.857 96.671  1.00 42.62  ? 432 TYR A OH    1 
ATOM   6674 N  N     . GLU B 2 433 ? 145.317 141.510 97.700  1.00 56.22  ? 433 GLU A N     1 
ATOM   6675 C  CA    . GLU B 2 433 ? 146.703 141.148 97.421  1.00 54.78  ? 433 GLU A CA    1 
ATOM   6676 C  C     . GLU B 2 433 ? 146.817 140.330 96.140  1.00 54.80  ? 433 GLU A C     1 
ATOM   6677 O  O     . GLU B 2 433 ? 147.715 140.564 95.325  1.00 55.15  ? 433 GLU A O     1 
ATOM   6678 C  CB    . GLU B 2 433 ? 147.288 140.378 98.603  1.00 57.25  ? 433 GLU A CB    1 
ATOM   6679 C  CG    . GLU B 2 433 ? 148.581 139.644 98.295  1.00 60.68  ? 433 GLU A CG    1 
ATOM   6680 C  CD    . GLU B 2 433 ? 149.692 140.575 97.848  1.00 66.87  ? 433 GLU A CD    1 
ATOM   6681 O  OE1   . GLU B 2 433 ? 149.816 141.677 98.425  1.00 66.76  ? 433 GLU A OE1   1 
ATOM   6682 O  OE2   . GLU B 2 433 ? 150.443 140.206 96.921  1.00 66.06  ? 433 GLU A OE2   1 
ATOM   6683 N  N     . GLU B 2 434 ? 145.911 139.373 95.939  1.00 56.36  ? 434 GLU A N     1 
ATOM   6684 C  CA    . GLU B 2 434 ? 146.016 138.494 94.782  1.00 52.87  ? 434 GLU A CA    1 
ATOM   6685 C  C     . GLU B 2 434 ? 145.613 139.194 93.492  1.00 50.95  ? 434 GLU A C     1 
ATOM   6686 O  O     . GLU B 2 434 ? 146.146 138.868 92.426  1.00 54.69  ? 434 GLU A O     1 
ATOM   6687 C  CB    . GLU B 2 434 ? 145.175 137.233 94.998  1.00 56.80  ? 434 GLU A CB    1 
ATOM   6688 C  CG    . GLU B 2 434 ? 143.677 137.413 94.812  1.00 59.18  ? 434 GLU A CG    1 
ATOM   6689 C  CD    . GLU B 2 434 ? 143.198 136.960 93.446  1.00 63.04  ? 434 GLU A CD    1 
ATOM   6690 O  OE1   . GLU B 2 434 ? 144.012 136.392 92.687  1.00 61.52  ? 434 GLU A OE1   1 
ATOM   6691 O  OE2   . GLU B 2 434 ? 142.008 137.172 93.131  1.00 60.25  ? 434 GLU A OE2   1 
ATOM   6692 N  N     . VAL B 2 435 ? 144.683 140.149 93.552  1.00 52.33  ? 435 VAL A N     1 
ATOM   6693 C  CA    . VAL B 2 435 ? 144.359 140.908 92.350  1.00 47.57  ? 435 VAL A CA    1 
ATOM   6694 C  C     . VAL B 2 435 ? 145.457 141.901 92.012  1.00 43.89  ? 435 VAL A C     1 
ATOM   6695 O  O     . VAL B 2 435 ? 145.585 142.296 90.850  1.00 41.11  ? 435 VAL A O     1 
ATOM   6696 C  CB    . VAL B 2 435 ? 143.010 141.636 92.482  1.00 44.12  ? 435 VAL A CB    1 
ATOM   6697 C  CG1   . VAL B 2 435 ? 143.170 142.957 93.207  1.00 48.00  ? 435 VAL A CG1   1 
ATOM   6698 C  CG2   . VAL B 2 435 ? 142.403 141.862 91.123  1.00 44.72  ? 435 VAL A CG2   1 
ATOM   6699 N  N     . GLY B 2 436 ? 146.260 142.310 92.995  1.00 57.11  ? 436 GLY A N     1 
ATOM   6700 C  CA    . GLY B 2 436 ? 147.343 143.234 92.701  1.00 56.48  ? 436 GLY A CA    1 
ATOM   6701 C  C     . GLY B 2 436 ? 148.382 142.656 91.758  1.00 56.09  ? 436 GLY A C     1 
ATOM   6702 O  O     . GLY B 2 436 ? 148.844 143.335 90.840  1.00 61.10  ? 436 GLY A O     1 
ATOM   6703 N  N     . VAL B 2 437 ? 148.761 141.401 91.969  1.00 55.14  ? 437 VAL A N     1 
ATOM   6704 C  CA    . VAL B 2 437 ? 149.838 140.781 91.203  1.00 51.99  ? 437 VAL A CA    1 
ATOM   6705 C  C     . VAL B 2 437 ? 149.413 140.497 89.772  1.00 55.43  ? 437 VAL A C     1 
ATOM   6706 O  O     . VAL B 2 437 ? 148.241 140.629 89.423  1.00 60.29  ? 437 VAL A O     1 
ATOM   6707 C  CB    . VAL B 2 437 ? 150.321 139.489 91.883  1.00 52.76  ? 437 VAL A CB    1 
ATOM   6708 C  CG1   . VAL B 2 437 ? 149.454 138.313 91.469  1.00 49.30  ? 437 VAL A CG1   1 
ATOM   6709 C  CG2   . VAL B 2 437 ? 151.784 139.228 91.558  1.00 55.79  ? 437 VAL A CG2   1 
ATOM   6710 N  N     . ASN C 3 8   ? 141.873 116.957 134.245 1.00 63.08  ? 8   ASN K N     1 
ATOM   6711 C  CA    . ASN C 3 8   ? 142.097 117.494 132.910 1.00 67.57  ? 8   ASN K CA    1 
ATOM   6712 C  C     . ASN C 3 8   ? 140.790 117.526 132.127 1.00 65.26  ? 8   ASN K C     1 
ATOM   6713 O  O     . ASN C 3 8   ? 139.867 116.769 132.418 1.00 69.58  ? 8   ASN K O     1 
ATOM   6714 C  CB    . ASN C 3 8   ? 143.146 116.667 132.164 1.00 70.51  ? 8   ASN K CB    1 
ATOM   6715 C  CG    . ASN C 3 8   ? 143.934 117.490 131.162 1.00 72.94  ? 8   ASN K CG    1 
ATOM   6716 O  OD1   . ASN C 3 8   ? 144.039 118.708 131.290 1.00 72.04  ? 8   ASN K OD1   1 
ATOM   6717 N  ND2   . ASN C 3 8   ? 144.493 116.825 130.159 1.00 67.26  ? 8   ASN K ND2   1 
ATOM   6718 N  N     . ILE C 3 9   ? 140.719 118.399 131.130 1.00 48.46  ? 9   ILE K N     1 
ATOM   6719 C  CA    . ILE C 3 9   ? 139.491 118.620 130.379 1.00 46.18  ? 9   ILE K CA    1 
ATOM   6720 C  C     . ILE C 3 9   ? 139.537 117.812 129.093 1.00 51.01  ? 9   ILE K C     1 
ATOM   6721 O  O     . ILE C 3 9   ? 140.471 117.945 128.295 1.00 54.16  ? 9   ILE K O     1 
ATOM   6722 C  CB    . ILE C 3 9   ? 139.291 120.113 130.076 1.00 51.38  ? 9   ILE K CB    1 
ATOM   6723 C  CG1   . ILE C 3 9   ? 139.850 120.979 131.204 1.00 57.23  ? 9   ILE K CG1   1 
ATOM   6724 C  CG2   . ILE C 3 9   ? 137.823 120.416 129.879 1.00 52.56  ? 9   ILE K CG2   1 
ATOM   6725 C  CD1   . ILE C 3 9   ? 139.015 120.972 132.458 1.00 57.58  ? 9   ILE K CD1   1 
ATOM   6726 N  N     . LYS C 3 10  ? 138.524 116.977 128.889 1.00 52.16  ? 10  LYS K N     1 
ATOM   6727 C  CA    . LYS C 3 10  ? 138.335 116.233 127.655 1.00 49.86  ? 10  LYS K CA    1 
ATOM   6728 C  C     . LYS C 3 10  ? 137.091 116.753 126.953 1.00 53.19  ? 10  LYS K C     1 
ATOM   6729 O  O     . LYS C 3 10  ? 136.054 116.964 127.588 1.00 62.42  ? 10  LYS K O     1 
ATOM   6730 C  CB    . LYS C 3 10  ? 138.191 114.733 127.919 1.00 52.91  ? 10  LYS K CB    1 
ATOM   6731 C  CG    . LYS C 3 10  ? 139.409 114.086 128.540 1.00 53.24  ? 10  LYS K CG    1 
ATOM   6732 C  CD    . LYS C 3 10  ? 140.644 114.315 127.687 1.00 60.67  ? 10  LYS K CD    1 
ATOM   6733 C  CE    . LYS C 3 10  ? 141.893 113.778 128.368 1.00 62.91  ? 10  LYS K CE    1 
ATOM   6734 N  NZ    . LYS C 3 10  ? 143.123 114.060 127.577 1.00 61.70  ? 10  LYS K NZ    1 
ATOM   6735 N  N     . VAL C 3 11  ? 137.191 116.964 125.645 1.00 51.28  ? 11  VAL K N     1 
ATOM   6736 C  CA    . VAL C 3 11  ? 136.079 117.453 124.841 1.00 47.69  ? 11  VAL K CA    1 
ATOM   6737 C  C     . VAL C 3 11  ? 135.753 116.404 123.789 1.00 51.79  ? 11  VAL K C     1 
ATOM   6738 O  O     . VAL C 3 11  ? 136.608 116.055 122.967 1.00 62.01  ? 11  VAL K O     1 
ATOM   6739 C  CB    . VAL C 3 11  ? 136.399 118.803 124.186 1.00 49.31  ? 11  VAL K CB    1 
ATOM   6740 C  CG1   . VAL C 3 11  ? 135.225 119.268 123.351 1.00 53.60  ? 11  VAL K CG1   1 
ATOM   6741 C  CG2   . VAL C 3 11  ? 136.740 119.833 125.239 1.00 51.66  ? 11  VAL K CG2   1 
ATOM   6742 N  N     . MET C 3 12  ? 134.521 115.906 123.814 1.00 56.11  ? 12  MET K N     1 
ATOM   6743 C  CA    . MET C 3 12  ? 134.033 114.945 122.841 1.00 57.76  ? 12  MET K CA    1 
ATOM   6744 C  C     . MET C 3 12  ? 132.917 115.579 122.025 1.00 60.48  ? 12  MET K C     1 
ATOM   6745 O  O     . MET C 3 12  ? 132.188 116.446 122.514 1.00 66.12  ? 12  MET K O     1 
ATOM   6746 C  CB    . MET C 3 12  ? 133.505 113.673 123.510 1.00 54.93  ? 12  MET K CB    1 
ATOM   6747 C  CG    . MET C 3 12  ? 134.292 113.201 124.709 1.00 54.97  ? 12  MET K CG    1 
ATOM   6748 S  SD    . MET C 3 12  ? 135.945 112.632 124.300 1.00 78.09  ? 12  MET K SD    1 
ATOM   6749 C  CE    . MET C 3 12  ? 136.463 111.968 125.878 1.00 65.91  ? 12  MET K CE    1 
ATOM   6750 N  N     . CYS C 3 13  ? 132.787 115.144 120.776 1.00 54.95  ? 13  CYS K N     1 
ATOM   6751 C  CA    . CYS C 3 13  ? 131.733 115.613 119.890 1.00 49.90  ? 13  CYS K CA    1 
ATOM   6752 C  C     . CYS C 3 13  ? 130.996 114.418 119.311 1.00 54.93  ? 13  CYS K C     1 
ATOM   6753 O  O     . CYS C 3 13  ? 131.615 113.544 118.697 1.00 66.52  ? 13  CYS K O     1 
ATOM   6754 C  CB    . CYS C 3 13  ? 132.298 116.475 118.766 1.00 55.90  ? 13  CYS K CB    1 
ATOM   6755 S  SG    . CYS C 3 13  ? 131.043 117.224 117.726 1.00 66.30  ? 13  CYS K SG    1 
ATOM   6756 N  N     . ARG C 3 14  ? 129.682 114.381 119.501 1.00 48.09  ? 14  ARG K N     1 
ATOM   6757 C  CA    . ARG C 3 14  ? 128.855 113.297 118.995 1.00 51.62  ? 14  ARG K CA    1 
ATOM   6758 C  C     . ARG C 3 14  ? 127.854 113.839 117.986 1.00 55.11  ? 14  ARG K C     1 
ATOM   6759 O  O     . ARG C 3 14  ? 127.152 114.816 118.264 1.00 54.85  ? 14  ARG K O     1 
ATOM   6760 C  CB    . ARG C 3 14  ? 128.114 112.574 120.119 1.00 47.90  ? 14  ARG K CB    1 
ATOM   6761 C  CG    . ARG C 3 14  ? 127.213 111.480 119.594 1.00 50.27  ? 14  ARG K CG    1 
ATOM   6762 C  CD    . ARG C 3 14  ? 126.399 110.817 120.670 1.00 49.11  ? 14  ARG K CD    1 
ATOM   6763 N  NE    . ARG C 3 14  ? 125.884 109.534 120.213 1.00 46.81  ? 14  ARG K NE    1 
ATOM   6764 C  CZ    . ARG C 3 14  ? 125.010 108.798 120.882 1.00 51.01  ? 14  ARG K CZ    1 
ATOM   6765 N  NH1   . ARG C 3 14  ? 124.516 109.197 122.039 1.00 55.20  ? 14  ARG K NH1   1 
ATOM   6766 N  NH2   . ARG C 3 14  ? 124.621 107.634 120.374 1.00 52.30  ? 14  ARG K NH2   1 
ATOM   6767 N  N     . PHE C 3 15  ? 127.797 113.206 116.821 1.00 60.52  ? 15  PHE K N     1 
ATOM   6768 C  CA    . PHE C 3 15  ? 126.843 113.528 115.776 1.00 54.71  ? 15  PHE K CA    1 
ATOM   6769 C  C     . PHE C 3 15  ? 125.711 112.510 115.798 1.00 59.16  ? 15  PHE K C     1 
ATOM   6770 O  O     . PHE C 3 15  ? 125.759 111.513 116.523 1.00 68.19  ? 15  PHE K O     1 
ATOM   6771 C  CB    . PHE C 3 15  ? 127.521 113.536 114.405 1.00 54.56  ? 15  PHE K CB    1 
ATOM   6772 C  CG    . PHE C 3 15  ? 128.391 114.731 114.165 1.00 56.90  ? 15  PHE K CG    1 
ATOM   6773 C  CD1   . PHE C 3 15  ? 129.619 114.837 114.779 1.00 58.00  ? 15  PHE K CD1   1 
ATOM   6774 C  CD2   . PHE C 3 15  ? 127.991 115.738 113.312 1.00 58.52  ? 15  PHE K CD2   1 
ATOM   6775 C  CE1   . PHE C 3 15  ? 130.420 115.928 114.559 1.00 58.58  ? 15  PHE K CE1   1 
ATOM   6776 C  CE2   . PHE C 3 15  ? 128.794 116.831 113.090 1.00 56.15  ? 15  PHE K CE2   1 
ATOM   6777 C  CZ    . PHE C 3 15  ? 130.006 116.925 113.715 1.00 55.55  ? 15  PHE K CZ    1 
ATOM   6778 N  N     . ARG C 3 16  ? 124.689 112.766 114.997 1.00 61.19  ? 16  ARG K N     1 
ATOM   6779 C  CA    . ARG C 3 16  ? 123.530 111.897 114.916 1.00 60.13  ? 16  ARG K CA    1 
ATOM   6780 C  C     . ARG C 3 16  ? 123.148 111.659 113.462 1.00 67.44  ? 16  ARG K C     1 
ATOM   6781 O  O     . ARG C 3 16  ? 123.433 112.491 112.593 1.00 74.96  ? 16  ARG K O     1 
ATOM   6782 C  CB    . ARG C 3 16  ? 122.346 112.505 115.680 1.00 60.24  ? 16  ARG K CB    1 
ATOM   6783 C  CG    . ARG C 3 16  ? 121.754 113.731 115.040 1.00 61.21  ? 16  ARG K CG    1 
ATOM   6784 C  CD    . ARG C 3 16  ? 120.364 113.991 115.567 1.00 61.33  ? 16  ARG K CD    1 
ATOM   6785 N  NE    . ARG C 3 16  ? 119.796 115.209 115.008 1.00 66.48  ? 16  ARG K NE    1 
ATOM   6786 C  CZ    . ARG C 3 16  ? 119.130 115.268 113.864 1.00 67.01  ? 16  ARG K CZ    1 
ATOM   6787 N  NH1   . ARG C 3 16  ? 118.922 114.189 113.129 1.00 68.68  ? 16  ARG K NH1   1 
ATOM   6788 N  NH2   . ARG C 3 16  ? 118.662 116.439 113.447 1.00 66.33  ? 16  ARG K NH2   1 
ATOM   6789 N  N     . PRO C 3 17  ? 122.516 110.531 113.153 1.00 65.53  ? 17  PRO K N     1 
ATOM   6790 C  CA    . PRO C 3 17  ? 122.071 110.290 111.780 1.00 67.24  ? 17  PRO K CA    1 
ATOM   6791 C  C     . PRO C 3 17  ? 120.900 111.184 111.402 1.00 68.47  ? 17  PRO K C     1 
ATOM   6792 O  O     . PRO C 3 17  ? 120.126 111.637 112.246 1.00 70.36  ? 17  PRO K O     1 
ATOM   6793 C  CB    . PRO C 3 17  ? 121.657 108.815 111.785 1.00 66.21  ? 17  PRO K CB    1 
ATOM   6794 C  CG    . PRO C 3 17  ? 121.410 108.473 113.198 1.00 65.40  ? 17  PRO K CG    1 
ATOM   6795 C  CD    . PRO C 3 17  ? 122.082 109.472 114.079 1.00 65.79  ? 17  PRO K CD    1 
ATOM   6796 N  N     . LEU C 3 18  ? 120.784 111.436 110.101 1.00 63.93  ? 18  LEU K N     1 
ATOM   6797 C  CA    . LEU C 3 18  ? 119.695 112.259 109.598 1.00 63.26  ? 18  LEU K CA    1 
ATOM   6798 C  C     . LEU C 3 18  ? 118.373 111.523 109.755 1.00 71.55  ? 18  LEU K C     1 
ATOM   6799 O  O     . LEU C 3 18  ? 118.256 110.352 109.383 1.00 73.23  ? 18  LEU K O     1 
ATOM   6800 C  CB    . LEU C 3 18  ? 119.933 112.620 108.135 1.00 64.48  ? 18  LEU K CB    1 
ATOM   6801 C  CG    . LEU C 3 18  ? 121.038 113.636 107.857 1.00 68.91  ? 18  LEU K CG    1 
ATOM   6802 C  CD1   . LEU C 3 18  ? 121.321 113.715 106.372 1.00 68.33  ? 18  LEU K CD1   1 
ATOM   6803 C  CD2   . LEU C 3 18  ? 120.658 115.000 108.401 1.00 72.44  ? 18  LEU K CD2   1 
ATOM   6804 N  N     . ASN C 3 19  ? 117.378 112.208 110.310 1.00 75.66  ? 19  ASN K N     1 
ATOM   6805 C  CA    . ASN C 3 19  ? 116.111 111.559 110.598 1.00 72.43  ? 19  ASN K CA    1 
ATOM   6806 C  C     . ASN C 3 19  ? 115.246 111.478 109.346 1.00 75.88  ? 19  ASN K C     1 
ATOM   6807 O  O     . ASN C 3 19  ? 115.465 112.183 108.358 1.00 79.32  ? 19  ASN K O     1 
ATOM   6808 C  CB    . ASN C 3 19  ? 115.363 112.295 111.707 1.00 72.96  ? 19  ASN K CB    1 
ATOM   6809 C  CG    . ASN C 3 19  ? 115.194 113.764 111.417 1.00 76.75  ? 19  ASN K CG    1 
ATOM   6810 O  OD1   . ASN C 3 19  ? 114.238 114.172 110.760 1.00 80.25  ? 19  ASN K OD1   1 
ATOM   6811 N  ND2   . ASN C 3 19  ? 116.122 114.574 111.908 1.00 76.51  ? 19  ASN K ND2   1 
ATOM   6812 N  N     . GLU C 3 20  ? 114.247 110.595 109.403 1.00 84.81  ? 20  GLU K N     1 
ATOM   6813 C  CA    . GLU C 3 20  ? 113.356 110.404 108.265 1.00 85.35  ? 20  GLU K CA    1 
ATOM   6814 C  C     . GLU C 3 20  ? 112.535 111.651 107.976 1.00 83.45  ? 20  GLU K C     1 
ATOM   6815 O  O     . GLU C 3 20  ? 112.207 111.919 106.815 1.00 84.39  ? 20  GLU K O     1 
ATOM   6816 C  CB    . GLU C 3 20  ? 112.437 109.208 108.515 1.00 87.32  ? 20  GLU K CB    1 
ATOM   6817 C  CG    . GLU C 3 20  ? 111.666 108.742 107.290 1.00 87.80  ? 20  GLU K CG    1 
ATOM   6818 C  CD    . GLU C 3 20  ? 110.268 109.327 107.224 1.00 88.62  ? 20  GLU K CD    1 
ATOM   6819 O  OE1   . GLU C 3 20  ? 109.769 109.798 108.267 1.00 87.36  ? 20  GLU K OE1   1 
ATOM   6820 O  OE2   . GLU C 3 20  ? 109.668 109.313 106.128 1.00 86.37  ? 20  GLU K OE2   1 
ATOM   6821 N  N     . SER C 3 21  ? 112.199 112.427 109.006 1.00 85.31  ? 21  SER K N     1 
ATOM   6822 C  CA    . SER C 3 21  ? 111.424 113.644 108.805 1.00 87.02  ? 21  SER K CA    1 
ATOM   6823 C  C     . SER C 3 21  ? 112.187 114.706 108.027 1.00 84.58  ? 21  SER K C     1 
ATOM   6824 O  O     . SER C 3 21  ? 111.572 115.674 107.571 1.00 87.38  ? 21  SER K O     1 
ATOM   6825 C  CB    . SER C 3 21  ? 110.981 114.215 110.152 1.00 87.66  ? 21  SER K CB    1 
ATOM   6826 O  OG    . SER C 3 21  ? 110.261 115.423 109.980 1.00 88.77  ? 21  SER K OG    1 
ATOM   6827 N  N     . GLU C 3 22  ? 113.500 114.554 107.869 1.00 78.15  ? 22  GLU K N     1 
ATOM   6828 C  CA    . GLU C 3 22  ? 114.295 115.471 107.070 1.00 79.50  ? 22  GLU K CA    1 
ATOM   6829 C  C     . GLU C 3 22  ? 115.056 114.776 105.954 1.00 81.40  ? 22  GLU K C     1 
ATOM   6830 O  O     . GLU C 3 22  ? 115.900 115.412 105.314 1.00 83.97  ? 22  GLU K O     1 
ATOM   6831 C  CB    . GLU C 3 22  ? 115.278 116.246 107.957 1.00 83.53  ? 22  GLU K CB    1 
ATOM   6832 C  CG    . GLU C 3 22  ? 116.383 115.399 108.557 1.00 86.38  ? 22  GLU K CG    1 
ATOM   6833 C  CD    . GLU C 3 22  ? 117.317 116.206 109.435 1.00 85.72  ? 22  GLU K CD    1 
ATOM   6834 O  OE1   . GLU C 3 22  ? 117.329 117.448 109.308 1.00 83.90  ? 22  GLU K OE1   1 
ATOM   6835 O  OE2   . GLU C 3 22  ? 118.034 115.599 110.258 1.00 85.90  ? 22  GLU K OE2   1 
ATOM   6836 N  N     . VAL C 3 23  ? 114.799 113.490 105.707 1.00 80.36  ? 23  VAL K N     1 
ATOM   6837 C  CA    . VAL C 3 23  ? 115.406 112.837 104.554 1.00 82.38  ? 23  VAL K CA    1 
ATOM   6838 C  C     . VAL C 3 23  ? 114.593 113.120 103.301 1.00 85.03  ? 23  VAL K C     1 
ATOM   6839 O  O     . VAL C 3 23  ? 115.093 112.974 102.179 1.00 86.07  ? 23  VAL K O     1 
ATOM   6840 C  CB    . VAL C 3 23  ? 115.554 111.325 104.799 1.00 81.10  ? 23  VAL K CB    1 
ATOM   6841 C  CG1   . VAL C 3 23  ? 114.217 110.627 104.654 1.00 81.81  ? 23  VAL K CG1   1 
ATOM   6842 C  CG2   . VAL C 3 23  ? 116.577 110.729 103.848 1.00 80.64  ? 23  VAL K CG2   1 
ATOM   6843 N  N     . ASN C 3 24  ? 113.338 113.534 103.465 1.00 87.89  ? 24  ASN K N     1 
ATOM   6844 C  CA    . ASN C 3 24  ? 112.480 113.848 102.333 1.00 85.20  ? 24  ASN K CA    1 
ATOM   6845 C  C     . ASN C 3 24  ? 112.719 115.243 101.778 1.00 85.89  ? 24  ASN K C     1 
ATOM   6846 O  O     . ASN C 3 24  ? 112.240 115.544 100.679 1.00 91.00  ? 24  ASN K O     1 
ATOM   6847 C  CB    . ASN C 3 24  ? 111.013 113.704 102.737 1.00 85.11  ? 24  ASN K CB    1 
ATOM   6848 C  CG    . ASN C 3 24  ? 110.658 114.544 103.945 1.00 88.98  ? 24  ASN K CG    1 
ATOM   6849 O  OD1   . ASN C 3 24  ? 111.488 115.288 104.464 1.00 89.75  ? 24  ASN K OD1   1 
ATOM   6850 N  ND2   . ASN C 3 24  ? 109.418 114.425 104.403 1.00 89.63  ? 24  ASN K ND2   1 
ATOM   6851 N  N     . ARG C 3 25  ? 113.438 116.096 102.500 1.00 81.18  ? 25  ARG K N     1 
ATOM   6852 C  CA    . ARG C 3 25  ? 113.704 117.453 102.049 1.00 84.66  ? 25  ARG K CA    1 
ATOM   6853 C  C     . ARG C 3 25  ? 114.964 117.560 101.207 1.00 84.75  ? 25  ARG K C     1 
ATOM   6854 O  O     . ARG C 3 25  ? 115.306 118.662 100.768 1.00 83.35  ? 25  ARG K O     1 
ATOM   6855 C  CB    . ARG C 3 25  ? 113.817 118.397 103.245 1.00 83.06  ? 25  ARG K CB    1 
ATOM   6856 C  CG    . ARG C 3 25  ? 112.515 118.651 103.967 1.00 82.97  ? 25  ARG K CG    1 
ATOM   6857 C  CD    . ARG C 3 25  ? 112.646 119.856 104.870 1.00 84.60  ? 25  ARG K CD    1 
ATOM   6858 N  NE    . ARG C 3 25  ? 113.731 119.683 105.828 1.00 86.58  ? 25  ARG K NE    1 
ATOM   6859 C  CZ    . ARG C 3 25  ? 114.046 120.561 106.769 1.00 86.95  ? 25  ARG K CZ    1 
ATOM   6860 N  NH1   . ARG C 3 25  ? 113.374 121.691 106.914 1.00 86.64  ? 25  ARG K NH1   1 
ATOM   6861 N  NH2   . ARG C 3 25  ? 115.060 120.297 107.587 1.00 84.65  ? 25  ARG K NH2   1 
ATOM   6862 N  N     . GLY C 3 26  ? 115.661 116.453 100.973 1.00 90.37  ? 26  GLY K N     1 
ATOM   6863 C  CA    . GLY C 3 26  ? 116.890 116.513 100.213 1.00 92.45  ? 26  GLY K CA    1 
ATOM   6864 C  C     . GLY C 3 26  ? 118.048 117.145 100.946 1.00 93.51  ? 26  GLY K C     1 
ATOM   6865 O  O     . GLY C 3 26  ? 118.995 117.609 100.306 1.00 91.71  ? 26  GLY K O     1 
ATOM   6866 N  N     . ASP C 3 27  ? 117.997 117.187 102.275 1.00 88.93  ? 27  ASP K N     1 
ATOM   6867 C  CA    . ASP C 3 27  ? 119.089 117.752 103.049 1.00 87.65  ? 27  ASP K CA    1 
ATOM   6868 C  C     . ASP C 3 27  ? 120.345 116.908 102.885 1.00 85.82  ? 27  ASP K C     1 
ATOM   6869 O  O     . ASP C 3 27  ? 120.285 115.687 102.722 1.00 87.32  ? 27  ASP K O     1 
ATOM   6870 C  CB    . ASP C 3 27  ? 118.703 117.845 104.523 1.00 88.57  ? 27  ASP K CB    1 
ATOM   6871 C  CG    . ASP C 3 27  ? 117.545 118.784 104.759 1.00 90.14  ? 27  ASP K CG    1 
ATOM   6872 O  OD1   . ASP C 3 27  ? 117.392 119.744 103.976 1.00 90.72  ? 27  ASP K OD1   1 
ATOM   6873 O  OD2   . ASP C 3 27  ? 116.785 118.566 105.725 1.00 92.28  ? 27  ASP K OD2   1 
ATOM   6874 N  N     . LYS C 3 28  ? 121.494 117.572 102.929 1.00 71.82  ? 28  LYS K N     1 
ATOM   6875 C  CA    . LYS C 3 28  ? 122.763 116.937 102.622 1.00 77.36  ? 28  LYS K CA    1 
ATOM   6876 C  C     . LYS C 3 28  ? 123.659 116.880 103.851 1.00 78.61  ? 28  LYS K C     1 
ATOM   6877 O  O     . LYS C 3 28  ? 123.659 117.790 104.686 1.00 79.58  ? 28  LYS K O     1 
ATOM   6878 C  CB    . LYS C 3 28  ? 123.486 117.678 101.492 1.00 78.15  ? 28  LYS K CB    1 
ATOM   6879 C  CG    . LYS C 3 28  ? 122.730 117.673 100.172 1.00 78.64  ? 28  LYS K CG    1 
ATOM   6880 C  CD    . LYS C 3 28  ? 123.679 117.654 98.984  1.00 80.38  ? 28  LYS K CD    1 
ATOM   6881 C  CE    . LYS C 3 28  ? 124.695 118.780 99.065  1.00 78.18  ? 28  LYS K CE    1 
ATOM   6882 N  NZ    . LYS C 3 28  ? 125.683 118.710 97.954  1.00 78.90  ? 28  LYS K NZ    1 
ATOM   6883 N  N     . TYR C 3 29  ? 124.405 115.782 103.962 1.00 64.02  ? 29  TYR K N     1 
ATOM   6884 C  CA    . TYR C 3 29  ? 125.380 115.641 105.065 1.00 61.38  ? 29  TYR K CA    1 
ATOM   6885 C  C     . TYR C 3 29  ? 126.549 116.527 104.742 1.00 65.55  ? 29  TYR K C     1 
ATOM   6886 O  O     . TYR C 3 29  ? 126.926 116.637 103.565 1.00 69.80  ? 29  TYR K O     1 
ATOM   6887 C  CB    . TYR C 3 29  ? 125.738 114.163 105.041 1.00 63.94  ? 29  TYR K CB    1 
ATOM   6888 C  CG    . TYR C 3 29  ? 126.092 113.479 106.350 1.00 64.86  ? 29  TYR K CG    1 
ATOM   6889 C  CD1   . TYR C 3 29  ? 125.221 112.570 106.932 1.00 66.15  ? 29  TYR K CD1   1 
ATOM   6890 C  CD2   . TYR C 3 29  ? 127.310 113.703 106.974 1.00 63.15  ? 29  TYR K CD2   1 
ATOM   6891 C  CE1   . TYR C 3 29  ? 125.536 111.922 108.111 1.00 66.36  ? 29  TYR K CE1   1 
ATOM   6892 C  CE2   . TYR C 3 29  ? 127.638 113.061 108.155 1.00 63.59  ? 29  TYR K CE2   1 
ATOM   6893 C  CZ    . TYR C 3 29  ? 126.748 112.169 108.724 1.00 66.74  ? 29  TYR K CZ    1 
ATOM   6894 O  OH    . TYR C 3 29  ? 127.054 111.530 109.889 1.00 68.86  ? 29  TYR K OH    1 
ATOM   6895 N  N     . ILE C 3 30  ? 127.109 117.156 105.759 1.00 61.83  ? 30  ILE K N     1 
ATOM   6896 C  CA    . ILE C 3 30  ? 128.043 118.299 105.617 1.00 62.71  ? 30  ILE K CA    1 
ATOM   6897 C  C     . ILE C 3 30  ? 129.337 117.865 106.282 1.00 62.88  ? 30  ILE K C     1 
ATOM   6898 O  O     . ILE C 3 30  ? 130.405 118.348 105.884 1.00 67.95  ? 30  ILE K O     1 
ATOM   6899 C  CB    . ILE C 3 30  ? 127.439 119.516 106.327 1.00 68.47  ? 30  ILE K CB    1 
ATOM   6900 C  CG1   . ILE C 3 30  ? 126.089 119.891 105.732 1.00 67.84  ? 30  ILE K CG1   1 
ATOM   6901 C  CG2   . ILE C 3 30  ? 128.396 120.708 106.314 1.00 69.77  ? 30  ILE K CG2   1 
ATOM   6902 C  CD1   . ILE C 3 30  ? 126.147 120.241 104.256 1.00 66.13  ? 30  ILE K CD1   1 
ATOM   6903 N  N     . ALA C 3 31  ? 129.243 116.940 107.217 1.00 56.35  ? 31  ALA K N     1 
ATOM   6904 C  CA    . ALA C 3 31  ? 130.381 116.501 108.007 1.00 56.81  ? 31  ALA K CA    1 
ATOM   6905 C  C     . ALA C 3 31  ? 131.262 115.545 107.217 1.00 59.97  ? 31  ALA K C     1 
ATOM   6906 O  O     . ALA C 3 31  ? 130.766 114.622 106.564 1.00 65.44  ? 31  ALA K O     1 
ATOM   6907 C  CB    . ALA C 3 31  ? 129.903 115.829 109.291 1.00 61.06  ? 31  ALA K CB    1 
ATOM   6908 N  N     . LYS C 3 32  ? 132.570 115.769 107.282 1.00 61.06  ? 32  LYS K N     1 
ATOM   6909 C  CA    . LYS C 3 32  ? 133.563 114.833 106.779 1.00 60.84  ? 32  LYS K CA    1 
ATOM   6910 C  C     . LYS C 3 32  ? 134.511 114.502 107.918 1.00 63.05  ? 32  LYS K C     1 
ATOM   6911 O  O     . LYS C 3 32  ? 135.047 115.408 108.563 1.00 73.08  ? 32  LYS K O     1 
ATOM   6912 C  CB    . LYS C 3 32  ? 134.335 115.418 105.594 1.00 64.08  ? 32  LYS K CB    1 
ATOM   6913 C  CG    . LYS C 3 32  ? 133.593 115.351 104.274 1.00 65.59  ? 32  LYS K CG    1 
ATOM   6914 C  CD    . LYS C 3 32  ? 134.449 115.881 103.140 1.00 67.26  ? 32  LYS K CD    1 
ATOM   6915 C  CE    . LYS C 3 32  ? 135.815 115.212 103.117 1.00 68.96  ? 32  LYS K CE    1 
ATOM   6916 N  NZ    . LYS C 3 32  ? 135.708 113.731 103.006 1.00 68.52  ? 32  LYS K NZ    1 
ATOM   6917 N  N     . PHE C 3 33  ? 134.719 113.215 108.164 1.00 56.47  ? 33  PHE K N     1 
ATOM   6918 C  CA    . PHE C 3 33  ? 135.499 112.756 109.303 1.00 55.01  ? 33  PHE K CA    1 
ATOM   6919 C  C     . PHE C 3 33  ? 136.909 112.395 108.863 1.00 60.29  ? 33  PHE K C     1 
ATOM   6920 O  O     . PHE C 3 33  ? 137.092 111.661 107.887 1.00 65.79  ? 33  PHE K O     1 
ATOM   6921 C  CB    . PHE C 3 33  ? 134.828 111.553 109.964 1.00 55.27  ? 33  PHE K CB    1 
ATOM   6922 C  CG    . PHE C 3 33  ? 133.450 111.838 110.466 1.00 53.87  ? 33  PHE K CG    1 
ATOM   6923 C  CD1   . PHE C 3 33  ? 133.238 112.821 111.408 1.00 59.60  ? 33  PHE K CD1   1 
ATOM   6924 C  CD2   . PHE C 3 33  ? 132.367 111.132 109.992 1.00 56.60  ? 33  PHE K CD2   1 
ATOM   6925 C  CE1   . PHE C 3 33  ? 131.976 113.091 111.869 1.00 61.85  ? 33  PHE K CE1   1 
ATOM   6926 C  CE2   . PHE C 3 33  ? 131.100 111.400 110.452 1.00 62.16  ? 33  PHE K CE2   1 
ATOM   6927 C  CZ    . PHE C 3 33  ? 130.906 112.382 111.391 1.00 64.20  ? 33  PHE K CZ    1 
ATOM   6928 N  N     . GLN C 3 34  ? 137.899 112.917 109.581 1.00 66.81  ? 34  GLN K N     1 
ATOM   6929 C  CA    . GLN C 3 34  ? 139.296 112.549 109.394 1.00 70.07  ? 34  GLN K CA    1 
ATOM   6930 C  C     . GLN C 3 34  ? 139.770 111.819 110.639 1.00 67.47  ? 34  GLN K C     1 
ATOM   6931 O  O     . GLN C 3 34  ? 139.727 112.377 111.740 1.00 72.59  ? 34  GLN K O     1 
ATOM   6932 C  CB    . GLN C 3 34  ? 140.172 113.774 109.138 1.00 67.09  ? 34  GLN K CB    1 
ATOM   6933 C  CG    . GLN C 3 34  ? 139.864 114.506 107.852 1.00 71.04  ? 34  GLN K CG    1 
ATOM   6934 C  CD    . GLN C 3 34  ? 140.820 115.651 107.603 1.00 74.05  ? 34  GLN K CD    1 
ATOM   6935 O  OE1   . GLN C 3 34  ? 141.736 115.890 108.389 1.00 74.58  ? 34  GLN K OE1   1 
ATOM   6936 N  NE2   . GLN C 3 34  ? 140.615 116.367 106.504 1.00 72.37  ? 34  GLN K NE2   1 
ATOM   6937 N  N     . GLY C 3 35  ? 140.230 110.587 110.464 1.00 68.70  ? 35  GLY K N     1 
ATOM   6938 C  CA    . GLY C 3 35  ? 140.758 109.841 111.592 1.00 70.11  ? 35  GLY K CA    1 
ATOM   6939 C  C     . GLY C 3 35  ? 139.707 109.642 112.662 1.00 69.87  ? 35  GLY K C     1 
ATOM   6940 O  O     . GLY C 3 35  ? 138.579 109.216 112.391 1.00 71.87  ? 35  GLY K O     1 
ATOM   6941 N  N     . GLU C 3 36  ? 140.075 109.959 113.905 1.00 69.02  ? 36  GLU K N     1 
ATOM   6942 C  CA    . GLU C 3 36  ? 139.153 109.802 115.020 1.00 73.26  ? 36  GLU K CA    1 
ATOM   6943 C  C     . GLU C 3 36  ? 139.140 111.019 115.939 1.00 75.08  ? 36  GLU K C     1 
ATOM   6944 O  O     . GLU C 3 36  ? 138.624 110.931 117.058 1.00 80.67  ? 36  GLU K O     1 
ATOM   6945 C  CB    . GLU C 3 36  ? 139.497 108.549 115.829 1.00 76.09  ? 36  GLU K CB    1 
ATOM   6946 C  CG    . GLU C 3 36  ? 140.983 108.270 115.930 1.00 79.13  ? 36  GLU K CG    1 
ATOM   6947 C  CD    . GLU C 3 36  ? 141.657 109.084 117.017 1.00 82.68  ? 36  GLU K CD    1 
ATOM   6948 O  OE1   . GLU C 3 36  ? 140.984 109.421 118.013 1.00 81.78  ? 36  GLU K OE1   1 
ATOM   6949 O  OE2   . GLU C 3 36  ? 142.861 109.386 116.875 1.00 81.98  ? 36  GLU K OE2   1 
ATOM   6950 N  N     . ASP C 3 37  ? 139.691 112.152 115.502 1.00 65.01  ? 37  ASP K N     1 
ATOM   6951 C  CA    . ASP C 3 37  ? 139.730 113.331 116.356 1.00 65.95  ? 37  ASP K CA    1 
ATOM   6952 C  C     . ASP C 3 37  ? 139.435 114.633 115.622 1.00 69.99  ? 37  ASP K C     1 
ATOM   6953 O  O     . ASP C 3 37  ? 139.657 115.705 116.198 1.00 77.00  ? 37  ASP K O     1 
ATOM   6954 C  CB    . ASP C 3 37  ? 141.090 113.438 117.048 1.00 70.42  ? 37  ASP K CB    1 
ATOM   6955 C  CG    . ASP C 3 37  ? 142.249 113.323 116.077 1.00 77.49  ? 37  ASP K CG    1 
ATOM   6956 O  OD1   . ASP C 3 37  ? 142.465 114.269 115.290 1.00 77.21  ? 37  ASP K OD1   1 
ATOM   6957 O  OD2   . ASP C 3 37  ? 142.946 112.287 116.102 1.00 77.23  ? 37  ASP K OD2   1 
ATOM   6958 N  N     . THR C 3 38  ? 138.948 114.591 114.385 1.00 57.98  ? 38  THR K N     1 
ATOM   6959 C  CA    . THR C 3 38  ? 138.691 115.808 113.632 1.00 59.91  ? 38  THR K CA    1 
ATOM   6960 C  C     . THR C 3 38  ? 137.416 115.661 112.819 1.00 63.41  ? 38  THR K C     1 
ATOM   6961 O  O     . THR C 3 38  ? 137.028 114.555 112.436 1.00 69.17  ? 38  THR K O     1 
ATOM   6962 C  CB    . THR C 3 38  ? 139.850 116.156 112.693 1.00 66.99  ? 38  THR K CB    1 
ATOM   6963 O  OG1   . THR C 3 38  ? 140.418 114.951 112.166 1.00 74.12  ? 38  THR K OG1   1 
ATOM   6964 C  CG2   . THR C 3 38  ? 140.924 116.938 113.432 1.00 66.86  ? 38  THR K CG2   1 
ATOM   6965 N  N     . VAL C 3 39  ? 136.767 116.793 112.567 1.00 50.59  ? 39  VAL K N     1 
ATOM   6966 C  CA    . VAL C 3 39  ? 135.617 116.876 111.679 1.00 48.68  ? 39  VAL K CA    1 
ATOM   6967 C  C     . VAL C 3 39  ? 135.812 118.094 110.790 1.00 58.19  ? 39  VAL K C     1 
ATOM   6968 O  O     . VAL C 3 39  ? 136.240 119.151 111.265 1.00 63.26  ? 39  VAL K O     1 
ATOM   6969 C  CB    . VAL C 3 39  ? 134.292 116.964 112.462 1.00 52.03  ? 39  VAL K CB    1 
ATOM   6970 C  CG1   . VAL C 3 39  ? 134.360 118.047 113.520 1.00 58.41  ? 39  VAL K CG1   1 
ATOM   6971 C  CG2   . VAL C 3 39  ? 133.125 117.197 111.521 1.00 56.03  ? 39  VAL K CG2   1 
ATOM   6972 N  N     . VAL C 3 40  ? 135.529 117.942 109.500 1.00 67.47  ? 40  VAL K N     1 
ATOM   6973 C  CA    . VAL C 3 40  ? 135.734 118.999 108.517 1.00 59.88  ? 40  VAL K CA    1 
ATOM   6974 C  C     . VAL C 3 40  ? 134.373 119.464 108.025 1.00 60.40  ? 40  VAL K C     1 
ATOM   6975 O  O     . VAL C 3 40  ? 133.664 118.719 107.339 1.00 63.92  ? 40  VAL K O     1 
ATOM   6976 C  CB    . VAL C 3 40  ? 136.605 118.521 107.348 1.00 63.26  ? 40  VAL K CB    1 
ATOM   6977 C  CG1   . VAL C 3 40  ? 136.766 119.628 106.324 1.00 66.66  ? 40  VAL K CG1   1 
ATOM   6978 C  CG2   . VAL C 3 40  ? 137.955 118.055 107.855 1.00 63.94  ? 40  VAL K CG2   1 
ATOM   6979 N  N     . ILE C 3 41  ? 134.018 120.699 108.362 1.00 67.57  ? 41  ILE K N     1 
ATOM   6980 C  CA    . ILE C 3 41  ? 132.769 121.315 107.934 1.00 68.89  ? 41  ILE K CA    1 
ATOM   6981 C  C     . ILE C 3 41  ? 133.119 122.586 107.176 1.00 73.48  ? 41  ILE K C     1 
ATOM   6982 O  O     . ILE C 3 41  ? 133.822 123.454 107.709 1.00 76.60  ? 41  ILE K O     1 
ATOM   6983 C  CB    . ILE C 3 41  ? 131.843 121.630 109.119 1.00 69.26  ? 41  ILE K CB    1 
ATOM   6984 C  CG1   . ILE C 3 41  ? 131.192 120.351 109.639 1.00 69.83  ? 41  ILE K CG1   1 
ATOM   6985 C  CG2   . ILE C 3 41  ? 130.784 122.634 108.715 1.00 71.87  ? 41  ILE K CG2   1 
ATOM   6986 C  CD1   . ILE C 3 41  ? 130.226 120.581 110.767 1.00 71.54  ? 41  ILE K CD1   1 
ATOM   6987 N  N     . ALA C 3 42  ? 132.628 122.697 105.941 1.00 75.93  ? 42  ALA K N     1 
ATOM   6988 C  CA    . ALA C 3 42  ? 132.902 123.846 105.079 1.00 76.57  ? 42  ALA K CA    1 
ATOM   6989 C  C     . ALA C 3 42  ? 134.401 124.071 104.911 1.00 73.88  ? 42  ALA K C     1 
ATOM   6990 O  O     . ALA C 3 42  ? 134.887 125.201 104.973 1.00 76.27  ? 42  ALA K O     1 
ATOM   6991 C  CB    . ALA C 3 42  ? 132.218 125.109 105.605 1.00 76.77  ? 42  ALA K CB    1 
ATOM   6992 N  N     . SER C 3 43  ? 135.137 122.981 104.697 1.00 74.03  ? 43  SER K N     1 
ATOM   6993 C  CA    . SER C 3 43  ? 136.583 123.023 104.471 1.00 76.83  ? 43  SER K CA    1 
ATOM   6994 C  C     . SER C 3 43  ? 137.312 123.728 105.611 1.00 77.13  ? 43  SER K C     1 
ATOM   6995 O  O     . SER C 3 43  ? 138.242 124.506 105.392 1.00 80.97  ? 43  SER K O     1 
ATOM   6996 C  CB    . SER C 3 43  ? 136.915 123.680 103.130 1.00 77.24  ? 43  SER K CB    1 
ATOM   6997 O  OG    . SER C 3 43  ? 136.751 125.086 103.195 1.00 78.95  ? 43  SER K OG    1 
ATOM   6998 N  N     . LYS C 3 44  ? 136.885 123.459 106.839 1.00 68.50  ? 44  LYS K N     1 
ATOM   6999 C  CA    . LYS C 3 44  ? 137.541 124.010 108.015 1.00 66.71  ? 44  LYS K CA    1 
ATOM   7000 C  C     . LYS C 3 44  ? 137.659 122.933 109.085 1.00 66.60  ? 44  LYS K C     1 
ATOM   7001 O  O     . LYS C 3 44  ? 136.641 122.424 109.569 1.00 74.88  ? 44  LYS K O     1 
ATOM   7002 C  CB    . LYS C 3 44  ? 136.771 125.218 108.547 1.00 69.77  ? 44  LYS K CB    1 
ATOM   7003 C  CG    . LYS C 3 44  ? 137.588 126.122 109.455 1.00 73.89  ? 44  LYS K CG    1 
ATOM   7004 C  CD    . LYS C 3 44  ? 136.749 127.260 110.010 1.00 75.12  ? 44  LYS K CD    1 
ATOM   7005 C  CE    . LYS C 3 44  ? 136.029 128.010 108.901 1.00 75.69  ? 44  LYS K CE    1 
ATOM   7006 N  NZ    . LYS C 3 44  ? 136.979 128.561 107.897 1.00 73.44  ? 44  LYS K NZ    1 
ATOM   7007 N  N     . PRO C 3 45  ? 138.871 122.553 109.474 1.00 59.10  ? 45  PRO K N     1 
ATOM   7008 C  CA    . PRO C 3 45  ? 139.024 121.488 110.469 1.00 62.18  ? 45  PRO K CA    1 
ATOM   7009 C  C     . PRO C 3 45  ? 138.566 121.927 111.849 1.00 65.08  ? 45  PRO K C     1 
ATOM   7010 O  O     . PRO C 3 45  ? 138.623 123.105 112.208 1.00 66.72  ? 45  PRO K O     1 
ATOM   7011 C  CB    . PRO C 3 45  ? 140.527 121.205 110.453 1.00 62.00  ? 45  PRO K CB    1 
ATOM   7012 C  CG    . PRO C 3 45  ? 141.133 122.491 110.032 1.00 65.95  ? 45  PRO K CG    1 
ATOM   7013 C  CD    . PRO C 3 45  ? 140.167 123.114 109.062 1.00 65.09  ? 45  PRO K CD    1 
ATOM   7014 N  N     . TYR C 3 46  ? 138.109 120.950 112.628 1.00 64.96  ? 46  TYR K N     1 
ATOM   7015 C  CA    . TYR C 3 46  ? 137.705 121.164 114.017 1.00 61.22  ? 46  TYR K CA    1 
ATOM   7016 C  C     . TYR C 3 46  ? 138.232 119.972 114.808 1.00 64.15  ? 46  TYR K C     1 
ATOM   7017 O  O     . TYR C 3 46  ? 137.743 118.851 114.644 1.00 69.22  ? 46  TYR K O     1 
ATOM   7018 C  CB    . TYR C 3 46  ? 136.195 121.288 114.146 1.00 62.12  ? 46  TYR K CB    1 
ATOM   7019 C  CG    . TYR C 3 46  ? 135.623 122.576 113.615 1.00 59.82  ? 46  TYR K CG    1 
ATOM   7020 C  CD1   . TYR C 3 46  ? 135.801 123.767 114.290 1.00 58.44  ? 46  TYR K CD1   1 
ATOM   7021 C  CD2   . TYR C 3 46  ? 134.891 122.595 112.440 1.00 64.04  ? 46  TYR K CD2   1 
ATOM   7022 C  CE1   . TYR C 3 46  ? 135.275 124.941 113.808 1.00 63.18  ? 46  TYR K CE1   1 
ATOM   7023 C  CE2   . TYR C 3 46  ? 134.359 123.765 111.951 1.00 64.88  ? 46  TYR K CE2   1 
ATOM   7024 C  CZ    . TYR C 3 46  ? 134.554 124.934 112.637 1.00 65.35  ? 46  TYR K CZ    1 
ATOM   7025 O  OH    . TYR C 3 46  ? 134.026 126.105 112.151 1.00 69.63  ? 46  TYR K OH    1 
ATOM   7026 N  N     . ALA C 3 47  ? 139.221 120.209 115.662 1.00 59.99  ? 47  ALA K N     1 
ATOM   7027 C  CA    . ALA C 3 47  ? 139.902 119.130 116.363 1.00 60.51  ? 47  ALA K CA    1 
ATOM   7028 C  C     . ALA C 3 47  ? 139.379 118.991 117.786 1.00 64.90  ? 47  ALA K C     1 
ATOM   7029 O  O     . ALA C 3 47  ? 139.251 119.984 118.508 1.00 65.57  ? 47  ALA K O     1 
ATOM   7030 C  CB    . ALA C 3 47  ? 141.411 119.371 116.380 1.00 58.26  ? 47  ALA K CB    1 
ATOM   7031 N  N     . PHE C 3 48  ? 139.084 117.757 118.183 1.00 63.48  ? 48  PHE K N     1 
ATOM   7032 C  CA    . PHE C 3 48  ? 138.637 117.433 119.529 1.00 56.65  ? 48  PHE K CA    1 
ATOM   7033 C  C     . PHE C 3 48  ? 139.433 116.243 120.048 1.00 60.61  ? 48  PHE K C     1 
ATOM   7034 O  O     . PHE C 3 48  ? 140.304 115.701 119.363 1.00 68.20  ? 48  PHE K O     1 
ATOM   7035 C  CB    . PHE C 3 48  ? 137.139 117.125 119.562 1.00 54.91  ? 48  PHE K CB    1 
ATOM   7036 C  CG    . PHE C 3 48  ? 136.283 118.264 119.130 1.00 58.63  ? 48  PHE K CG    1 
ATOM   7037 C  CD1   . PHE C 3 48  ? 136.165 119.387 119.916 1.00 59.23  ? 48  PHE K CD1   1 
ATOM   7038 C  CD2   . PHE C 3 48  ? 135.580 118.206 117.949 1.00 59.68  ? 48  PHE K CD2   1 
ATOM   7039 C  CE1   . PHE C 3 48  ? 135.375 120.435 119.525 1.00 57.73  ? 48  PHE K CE1   1 
ATOM   7040 C  CE2   . PHE C 3 48  ? 134.790 119.249 117.555 1.00 59.94  ? 48  PHE K CE2   1 
ATOM   7041 C  CZ    . PHE C 3 48  ? 134.686 120.367 118.344 1.00 59.79  ? 48  PHE K CZ    1 
ATOM   7042 N  N     . ASP C 3 49  ? 139.132 115.836 121.279 1.00 58.70  ? 49  ASP K N     1 
ATOM   7043 C  CA    . ASP C 3 49  ? 139.806 114.682 121.855 1.00 60.89  ? 49  ASP K CA    1 
ATOM   7044 C  C     . ASP C 3 49  ? 139.271 113.372 121.298 1.00 65.79  ? 49  ASP K C     1 
ATOM   7045 O  O     . ASP C 3 49  ? 140.030 112.408 121.163 1.00 73.52  ? 49  ASP K O     1 
ATOM   7046 C  CB    . ASP C 3 49  ? 139.681 114.705 123.376 1.00 64.66  ? 49  ASP K CB    1 
ATOM   7047 C  CG    . ASP C 3 49  ? 140.491 115.820 124.005 1.00 71.55  ? 49  ASP K CG    1 
ATOM   7048 O  OD1   . ASP C 3 49  ? 141.645 116.031 123.578 1.00 70.93  ? 49  ASP K OD1   1 
ATOM   7049 O  OD2   . ASP C 3 49  ? 139.974 116.491 124.922 1.00 73.48  ? 49  ASP K OD2   1 
ATOM   7050 N  N     . ARG C 3 50  ? 137.982 113.315 120.975 1.00 65.95  ? 50  ARG K N     1 
ATOM   7051 C  CA    . ARG C 3 50  ? 137.410 112.150 120.314 1.00 65.65  ? 50  ARG K CA    1 
ATOM   7052 C  C     . ARG C 3 50  ? 136.091 112.551 119.676 1.00 69.94  ? 50  ARG K C     1 
ATOM   7053 O  O     . ARG C 3 50  ? 135.250 113.170 120.334 1.00 73.55  ? 50  ARG K O     1 
ATOM   7054 C  CB    . ARG C 3 50  ? 137.204 110.999 121.296 1.00 60.46  ? 50  ARG K CB    1 
ATOM   7055 C  CG    . ARG C 3 50  ? 136.198 109.979 120.823 1.00 65.80  ? 50  ARG K CG    1 
ATOM   7056 C  CD    . ARG C 3 50  ? 136.476 108.618 121.419 1.00 67.91  ? 50  ARG K CD    1 
ATOM   7057 N  NE    . ARG C 3 50  ? 137.363 107.832 120.573 1.00 70.27  ? 50  ARG K NE    1 
ATOM   7058 C  CZ    . ARG C 3 50  ? 136.975 107.184 119.483 1.00 72.45  ? 50  ARG K CZ    1 
ATOM   7059 N  NH1   . ARG C 3 50  ? 135.717 107.207 119.077 1.00 68.73  ? 50  ARG K NH1   1 
ATOM   7060 N  NH2   . ARG C 3 50  ? 137.873 106.496 118.784 1.00 71.16  ? 50  ARG K NH2   1 
ATOM   7061 N  N     . VAL C 3 51  ? 135.912 112.199 118.406 1.00 59.53  ? 51  VAL K N     1 
ATOM   7062 C  CA    . VAL C 3 51  ? 134.726 112.565 117.641 1.00 53.03  ? 51  VAL K CA    1 
ATOM   7063 C  C     . VAL C 3 51  ? 133.999 111.289 117.254 1.00 51.36  ? 51  VAL K C     1 
ATOM   7064 O  O     . VAL C 3 51  ? 134.550 110.450 116.532 1.00 57.44  ? 51  VAL K O     1 
ATOM   7065 C  CB    . VAL C 3 51  ? 135.086 113.385 116.394 1.00 53.08  ? 51  VAL K CB    1 
ATOM   7066 C  CG1   . VAL C 3 51  ? 133.840 113.715 115.609 1.00 57.06  ? 51  VAL K CG1   1 
ATOM   7067 C  CG2   . VAL C 3 51  ? 135.822 114.646 116.789 1.00 60.47  ? 51  VAL K CG2   1 
ATOM   7068 N  N     . PHE C 3 52  ? 132.769 111.141 117.727 1.00 50.23  ? 52  PHE K N     1 
ATOM   7069 C  CA    . PHE C 3 52  ? 131.958 109.985 117.388 1.00 53.28  ? 52  PHE K CA    1 
ATOM   7070 C  C     . PHE C 3 52  ? 131.234 110.215 116.068 1.00 63.87  ? 52  PHE K C     1 
ATOM   7071 O  O     . PHE C 3 52  ? 131.143 111.337 115.565 1.00 69.58  ? 52  PHE K O     1 
ATOM   7072 C  CB    . PHE C 3 52  ? 130.935 109.685 118.484 1.00 51.16  ? 52  PHE K CB    1 
ATOM   7073 C  CG    . PHE C 3 52  ? 131.539 109.385 119.824 1.00 53.74  ? 52  PHE K CG    1 
ATOM   7074 C  CD1   . PHE C 3 52  ? 132.027 108.130 120.113 1.00 61.05  ? 52  PHE K CD1   1 
ATOM   7075 C  CD2   . PHE C 3 52  ? 131.582 110.350 120.809 1.00 53.51  ? 52  PHE K CD2   1 
ATOM   7076 C  CE1   . PHE C 3 52  ? 132.570 107.854 121.346 1.00 61.95  ? 52  PHE K CE1   1 
ATOM   7077 C  CE2   . PHE C 3 52  ? 132.125 110.075 122.045 1.00 52.05  ? 52  PHE K CE2   1 
ATOM   7078 C  CZ    . PHE C 3 52  ? 132.616 108.828 122.312 1.00 52.80  ? 52  PHE K CZ    1 
ATOM   7079 N  N     . GLN C 3 53  ? 130.716 109.131 115.508 1.00 65.90  ? 53  GLN K N     1 
ATOM   7080 C  CA    . GLN C 3 53  ? 129.931 109.164 114.284 1.00 59.83  ? 53  GLN K CA    1 
ATOM   7081 C  C     . GLN C 3 53  ? 128.551 108.575 114.556 1.00 62.58  ? 53  GLN K C     1 
ATOM   7082 O  O     . GLN C 3 53  ? 128.216 108.212 115.684 1.00 68.97  ? 53  GLN K O     1 
ATOM   7083 C  CB    . GLN C 3 53  ? 130.643 108.412 113.159 1.00 60.63  ? 53  GLN K CB    1 
ATOM   7084 C  CG    . GLN C 3 53  ? 132.055 108.895 112.907 1.00 63.40  ? 53  GLN K CG    1 
ATOM   7085 C  CD    . GLN C 3 53  ? 132.695 108.226 111.717 1.00 64.04  ? 53  GLN K CD    1 
ATOM   7086 O  OE1   . GLN C 3 53  ? 132.010 107.777 110.800 1.00 66.87  ? 53  GLN K OE1   1 
ATOM   7087 N  NE2   . GLN C 3 53  ? 134.018 108.154 111.721 1.00 62.81  ? 53  GLN K NE2   1 
ATOM   7088 N  N     . SER C 3 54  ? 127.744 108.480 113.500 1.00 61.66  ? 54  SER K N     1 
ATOM   7089 C  CA    . SER C 3 54  ? 126.360 108.051 113.666 1.00 66.08  ? 54  SER K CA    1 
ATOM   7090 C  C     . SER C 3 54  ? 126.257 106.584 114.064 1.00 61.11  ? 54  SER K C     1 
ATOM   7091 O  O     . SER C 3 54  ? 125.310 106.199 114.758 1.00 62.14  ? 54  SER K O     1 
ATOM   7092 C  CB    . SER C 3 54  ? 125.576 108.306 112.380 1.00 70.54  ? 54  SER K CB    1 
ATOM   7093 O  OG    . SER C 3 54  ? 125.627 109.675 112.020 1.00 69.24  ? 54  SER K OG    1 
ATOM   7094 N  N     . SER C 3 55  ? 127.207 105.754 113.641 1.00 60.95  ? 55  SER K N     1 
ATOM   7095 C  CA    . SER C 3 55  ? 127.162 104.339 113.979 1.00 65.41  ? 55  SER K CA    1 
ATOM   7096 C  C     . SER C 3 55  ? 127.515 104.060 115.434 1.00 73.40  ? 55  SER K C     1 
ATOM   7097 O  O     . SER C 3 55  ? 127.347 102.921 115.882 1.00 73.82  ? 55  SER K O     1 
ATOM   7098 C  CB    . SER C 3 55  ? 128.105 103.555 113.067 1.00 69.22  ? 55  SER K CB    1 
ATOM   7099 O  OG    . SER C 3 55  ? 128.047 102.168 113.348 1.00 73.70  ? 55  SER K OG    1 
ATOM   7100 N  N     . THR C 3 56  ? 127.997 105.056 116.173 1.00 72.22  ? 56  THR K N     1 
ATOM   7101 C  CA    . THR C 3 56  ? 128.427 104.837 117.548 1.00 63.21  ? 56  THR K CA    1 
ATOM   7102 C  C     . THR C 3 56  ? 127.248 104.469 118.435 1.00 61.70  ? 56  THR K C     1 
ATOM   7103 O  O     . THR C 3 56  ? 126.132 104.960 118.249 1.00 64.84  ? 56  THR K O     1 
ATOM   7104 C  CB    . THR C 3 56  ? 129.118 106.082 118.093 1.00 66.48  ? 56  THR K CB    1 
ATOM   7105 O  OG1   . THR C 3 56  ? 128.322 107.237 117.804 1.00 70.08  ? 56  THR K OG1   1 
ATOM   7106 C  CG2   . THR C 3 56  ? 130.488 106.243 117.456 1.00 64.88  ? 56  THR K CG2   1 
ATOM   7107 N  N     . SER C 3 57  ? 127.503 103.601 119.406 1.00 58.17  ? 57  SER K N     1 
ATOM   7108 C  CA    . SER C 3 57  ? 126.481 103.129 120.326 1.00 60.42  ? 57  SER K CA    1 
ATOM   7109 C  C     . SER C 3 57  ? 126.552 103.885 121.647 1.00 63.33  ? 57  SER K C     1 
ATOM   7110 O  O     . SER C 3 57  ? 127.515 104.596 121.941 1.00 73.68  ? 57  SER K O     1 
ATOM   7111 C  CB    . SER C 3 57  ? 126.630 101.627 120.565 1.00 64.27  ? 57  SER K CB    1 
ATOM   7112 O  OG    . SER C 3 57  ? 125.632 101.162 121.456 1.00 64.60  ? 57  SER K OG    1 
ATOM   7113 N  N     . GLN C 3 58  ? 125.500 103.720 122.450 1.00 54.18  ? 58  GLN K N     1 
ATOM   7114 C  CA    . GLN C 3 58  ? 125.435 104.386 123.747 1.00 56.84  ? 58  GLN K CA    1 
ATOM   7115 C  C     . GLN C 3 58  ? 126.516 103.877 124.694 1.00 63.08  ? 58  GLN K C     1 
ATOM   7116 O  O     . GLN C 3 58  ? 127.135 104.663 125.428 1.00 66.64  ? 58  GLN K O     1 
ATOM   7117 C  CB    . GLN C 3 58  ? 124.054 104.184 124.358 1.00 53.79  ? 58  GLN K CB    1 
ATOM   7118 C  CG    . GLN C 3 58  ? 122.917 104.617 123.462 1.00 57.27  ? 58  GLN K CG    1 
ATOM   7119 C  CD    . GLN C 3 58  ? 122.598 106.080 123.600 1.00 59.77  ? 58  GLN K CD    1 
ATOM   7120 O  OE1   . GLN C 3 58  ? 122.593 106.823 122.622 1.00 66.13  ? 58  GLN K OE1   1 
ATOM   7121 N  NE2   . GLN C 3 58  ? 122.326 106.508 124.820 1.00 59.36  ? 58  GLN K NE2   1 
ATOM   7122 N  N     . GLU C 3 59  ? 126.753 102.565 124.692 1.00 66.06  ? 59  GLU K N     1 
ATOM   7123 C  CA    . GLU C 3 59  ? 127.724 101.981 125.608 1.00 65.73  ? 59  GLU K CA    1 
ATOM   7124 C  C     . GLU C 3 59  ? 129.124 102.516 125.344 1.00 63.92  ? 59  GLU K C     1 
ATOM   7125 O  O     . GLU C 3 59  ? 129.889 102.758 126.284 1.00 72.42  ? 59  GLU K O     1 
ATOM   7126 C  CB    . GLU C 3 59  ? 127.698 100.458 125.493 1.00 67.12  ? 59  GLU K CB    1 
ATOM   7127 C  CG    . GLU C 3 59  ? 128.217 99.731  126.720 1.00 71.97  ? 59  GLU K CG    1 
ATOM   7128 C  CD    . GLU C 3 59  ? 127.876 98.254  126.707 1.00 74.81  ? 59  GLU K CD    1 
ATOM   7129 O  OE1   . GLU C 3 59  ? 127.261 97.793  125.723 1.00 75.03  ? 59  GLU K OE1   1 
ATOM   7130 O  OE2   . GLU C 3 59  ? 128.223 97.553  127.681 1.00 74.39  ? 59  GLU K OE2   1 
ATOM   7131 N  N     . GLN C 3 60  ? 129.485 102.696 124.073 1.00 55.26  ? 60  GLN K N     1 
ATOM   7132 C  CA    . GLN C 3 60  ? 130.799 103.248 123.758 1.00 60.52  ? 60  GLN K CA    1 
ATOM   7133 C  C     . GLN C 3 60  ? 130.932 104.670 124.279 1.00 63.73  ? 60  GLN K C     1 
ATOM   7134 O  O     . GLN C 3 60  ? 131.989 105.055 124.794 1.00 73.84  ? 60  GLN K O     1 
ATOM   7135 C  CB    . GLN C 3 60  ? 131.049 103.204 122.253 1.00 63.09  ? 60  GLN K CB    1 
ATOM   7136 C  CG    . GLN C 3 60  ? 131.065 101.807 121.669 1.00 67.54  ? 60  GLN K CG    1 
ATOM   7137 C  CD    . GLN C 3 60  ? 131.517 101.788 120.224 1.00 72.99  ? 60  GLN K CD    1 
ATOM   7138 O  OE1   . GLN C 3 60  ? 131.789 102.833 119.633 1.00 73.78  ? 60  GLN K OE1   1 
ATOM   7139 N  NE2   . GLN C 3 60  ? 131.600 100.595 119.645 1.00 68.53  ? 60  GLN K NE2   1 
ATOM   7140 N  N     . VAL C 3 61  ? 129.872 105.466 124.151 1.00 50.26  ? 61  VAL K N     1 
ATOM   7141 C  CA    . VAL C 3 61  ? 129.901 106.830 124.666 1.00 50.12  ? 61  VAL K CA    1 
ATOM   7142 C  C     . VAL C 3 61  ? 130.111 106.821 126.170 1.00 56.31  ? 61  VAL K C     1 
ATOM   7143 O  O     . VAL C 3 61  ? 130.905 107.604 126.707 1.00 63.74  ? 61  VAL K O     1 
ATOM   7144 C  CB    . VAL C 3 61  ? 128.610 107.573 124.285 1.00 52.73  ? 61  VAL K CB    1 
ATOM   7145 C  CG1   . VAL C 3 61  ? 128.619 108.969 124.862 1.00 55.72  ? 61  VAL K CG1   1 
ATOM   7146 C  CG2   . VAL C 3 61  ? 128.457 107.621 122.780 1.00 60.27  ? 61  VAL K CG2   1 
ATOM   7147 N  N     . TYR C 3 62  ? 129.411 105.934 126.874 1.00 54.73  ? 62  TYR K N     1 
ATOM   7148 C  CA    . TYR C 3 62  ? 129.589 105.849 128.319 1.00 50.19  ? 62  TYR K CA    1 
ATOM   7149 C  C     . TYR C 3 62  ? 131.005 105.419 128.680 1.00 53.34  ? 62  TYR K C     1 
ATOM   7150 O  O     . TYR C 3 62  ? 131.611 105.972 129.605 1.00 62.43  ? 62  TYR K O     1 
ATOM   7151 C  CB    . TYR C 3 62  ? 128.568 104.886 128.911 1.00 54.36  ? 62  TYR K CB    1 
ATOM   7152 C  CG    . TYR C 3 62  ? 128.713 104.662 130.391 1.00 55.10  ? 62  TYR K CG    1 
ATOM   7153 C  CD1   . TYR C 3 62  ? 128.662 105.716 131.279 1.00 55.51  ? 62  TYR K CD1   1 
ATOM   7154 C  CD2   . TYR C 3 62  ? 128.877 103.388 130.901 1.00 54.65  ? 62  TYR K CD2   1 
ATOM   7155 C  CE1   . TYR C 3 62  ? 128.786 105.511 132.630 1.00 57.12  ? 62  TYR K CE1   1 
ATOM   7156 C  CE2   . TYR C 3 62  ? 128.999 103.174 132.246 1.00 55.05  ? 62  TYR K CE2   1 
ATOM   7157 C  CZ    . TYR C 3 62  ? 128.953 104.237 133.109 1.00 59.18  ? 62  TYR K CZ    1 
ATOM   7158 O  OH    . TYR C 3 62  ? 129.077 104.026 134.461 1.00 67.71  ? 62  TYR K OH    1 
ATOM   7159 N  N     . ASN C 3 63  ? 131.555 104.443 127.956 1.00 57.38  ? 63  ASN K N     1 
ATOM   7160 C  CA    . ASN C 3 63  ? 132.881 103.932 128.292 1.00 55.22  ? 63  ASN K CA    1 
ATOM   7161 C  C     . ASN C 3 63  ? 133.976 104.938 127.976 1.00 57.87  ? 63  ASN K C     1 
ATOM   7162 O  O     . ASN C 3 63  ? 135.024 104.932 128.630 1.00 63.78  ? 63  ASN K O     1 
ATOM   7163 C  CB    . ASN C 3 63  ? 133.150 102.624 127.555 1.00 53.74  ? 63  ASN K CB    1 
ATOM   7164 C  CG    . ASN C 3 63  ? 132.380 101.467 128.136 1.00 60.71  ? 63  ASN K CG    1 
ATOM   7165 O  OD1   . ASN C 3 63  ? 132.721 100.954 129.199 1.00 63.47  ? 63  ASN K OD1   1 
ATOM   7166 N  ND2   . ASN C 3 63  ? 131.334 101.044 127.442 1.00 62.47  ? 63  ASN K ND2   1 
ATOM   7167 N  N     . ASP C 3 64  ? 133.769 105.795 126.985 1.00 61.06  ? 64  ASP K N     1 
ATOM   7168 C  CA    . ASP C 3 64  ? 134.778 106.771 126.614 1.00 60.29  ? 64  ASP K CA    1 
ATOM   7169 C  C     . ASP C 3 64  ? 134.522 108.157 127.187 1.00 64.46  ? 64  ASP K C     1 
ATOM   7170 O  O     . ASP C 3 64  ? 135.323 109.062 126.944 1.00 65.14  ? 64  ASP K O     1 
ATOM   7171 C  CB    . ASP C 3 64  ? 134.888 106.856 125.092 1.00 67.44  ? 64  ASP K CB    1 
ATOM   7172 C  CG    . ASP C 3 64  ? 135.527 105.625 124.487 1.00 75.63  ? 64  ASP K CG    1 
ATOM   7173 O  OD1   . ASP C 3 64  ? 136.136 104.840 125.242 1.00 77.67  ? 64  ASP K OD1   1 
ATOM   7174 O  OD2   . ASP C 3 64  ? 135.409 105.434 123.258 1.00 75.21  ? 64  ASP K OD2   1 
ATOM   7175 N  N     . CYS C 3 65  ? 133.442 108.353 127.935 1.00 56.02  ? 65  CYS K N     1 
ATOM   7176 C  CA    . CYS C 3 65  ? 133.157 109.678 128.471 1.00 47.41  ? 65  CYS K CA    1 
ATOM   7177 C  C     . CYS C 3 65  ? 132.984 109.722 129.981 1.00 52.90  ? 65  CYS K C     1 
ATOM   7178 O  O     . CYS C 3 65  ? 133.475 110.656 130.615 1.00 60.58  ? 65  CYS K O     1 
ATOM   7179 C  CB    . CYS C 3 65  ? 131.902 110.256 127.805 1.00 48.68  ? 65  CYS K CB    1 
ATOM   7180 N  N     . ALA C 3 66  ? 132.303 108.746 130.586 1.00 55.24  ? 66  ALA K N     1 
ATOM   7181 C  CA    . ALA C 3 66  ? 131.881 108.883 131.973 1.00 52.76  ? 66  ALA K CA    1 
ATOM   7182 C  C     . ALA C 3 66  ? 132.242 107.725 132.893 1.00 55.33  ? 66  ALA K C     1 
ATOM   7183 O  O     . ALA C 3 66  ? 131.909 107.787 134.080 1.00 62.33  ? 66  ALA K O     1 
ATOM   7184 C  CB    . ALA C 3 66  ? 130.364 109.100 132.042 1.00 59.44  ? 66  ALA K CB    1 
ATOM   7185 N  N     . LYS C 3 67  ? 132.898 106.675 132.400 1.00 56.71  ? 67  LYS K N     1 
ATOM   7186 C  CA    . LYS C 3 67  ? 133.232 105.553 133.273 1.00 50.28  ? 67  LYS K CA    1 
ATOM   7187 C  C     . LYS C 3 67  ? 134.297 105.940 134.292 1.00 53.29  ? 67  LYS K C     1 
ATOM   7188 O  O     . LYS C 3 67  ? 134.169 105.644 135.488 1.00 59.15  ? 67  LYS K O     1 
ATOM   7189 C  CB    . LYS C 3 67  ? 133.698 104.361 132.443 1.00 54.66  ? 67  LYS K CB    1 
ATOM   7190 C  CG    . LYS C 3 67  ? 133.691 103.047 133.193 1.00 59.88  ? 67  LYS K CG    1 
ATOM   7191 C  CD    . LYS C 3 67  ? 134.235 101.924 132.329 1.00 57.39  ? 67  LYS K CD    1 
ATOM   7192 C  CE    . LYS C 3 67  ? 133.358 100.692 132.415 1.00 59.29  ? 67  LYS K CE    1 
ATOM   7193 N  NZ    . LYS C 3 67  ? 132.635 100.624 133.710 1.00 60.83  ? 67  LYS K NZ    1 
ATOM   7194 N  N     . LYS C 3 68  ? 135.360 106.600 133.833 1.00 56.87  ? 68  LYS K N     1 
ATOM   7195 C  CA    . LYS C 3 68  ? 136.455 106.958 134.725 1.00 56.47  ? 68  LYS K CA    1 
ATOM   7196 C  C     . LYS C 3 68  ? 135.990 107.914 135.812 1.00 64.80  ? 68  LYS K C     1 
ATOM   7197 O  O     . LYS C 3 68  ? 136.425 107.814 136.964 1.00 70.90  ? 68  LYS K O     1 
ATOM   7198 C  CB    . LYS C 3 68  ? 137.602 107.568 133.925 1.00 60.47  ? 68  LYS K CB    1 
ATOM   7199 C  CG    . LYS C 3 68  ? 138.829 107.899 134.753 1.00 67.14  ? 68  LYS K CG    1 
ATOM   7200 C  CD    . LYS C 3 68  ? 139.552 106.640 135.201 1.00 68.53  ? 68  LYS K CD    1 
ATOM   7201 C  CE    . LYS C 3 68  ? 140.041 105.831 134.011 1.00 66.27  ? 68  LYS K CE    1 
ATOM   7202 N  NZ    . LYS C 3 68  ? 140.920 106.635 133.118 1.00 65.37  ? 68  LYS K NZ    1 
ATOM   7203 N  N     . ILE C 3 69  ? 135.110 108.852 135.465 1.00 59.04  ? 69  ILE K N     1 
ATOM   7204 C  CA    . ILE C 3 69  ? 134.597 109.787 136.458 1.00 49.59  ? 69  ILE K CA    1 
ATOM   7205 C  C     . ILE C 3 69  ? 133.779 109.055 137.513 1.00 55.26  ? 69  ILE K C     1 
ATOM   7206 O  O     . ILE C 3 69  ? 133.895 109.335 138.711 1.00 64.78  ? 69  ILE K O     1 
ATOM   7207 C  CB    . ILE C 3 69  ? 133.785 110.897 135.772 1.00 55.01  ? 69  ILE K CB    1 
ATOM   7208 C  CG1   . ILE C 3 69  ? 134.649 111.627 134.749 1.00 58.52  ? 69  ILE K CG1   1 
ATOM   7209 C  CG2   . ILE C 3 69  ? 133.259 111.878 136.793 1.00 56.12  ? 69  ILE K CG2   1 
ATOM   7210 C  CD1   . ILE C 3 69  ? 133.932 112.746 134.035 1.00 62.75  ? 69  ILE K CD1   1 
ATOM   7211 N  N     . VAL C 3 70  ? 132.941 108.108 137.090 1.00 52.11  ? 70  VAL K N     1 
ATOM   7212 C  CA    . VAL C 3 70  ? 132.126 107.355 138.040 1.00 53.95  ? 70  VAL K CA    1 
ATOM   7213 C  C     . VAL C 3 70  ? 133.007 106.540 138.972 1.00 57.01  ? 70  VAL K C     1 
ATOM   7214 O  O     . VAL C 3 70  ? 132.770 106.487 140.185 1.00 64.10  ? 70  VAL K O     1 
ATOM   7215 C  CB    . VAL C 3 70  ? 131.120 106.463 137.294 1.00 61.29  ? 70  VAL K CB    1 
ATOM   7216 C  CG1   . VAL C 3 70  ? 130.528 105.434 138.233 1.00 57.02  ? 70  VAL K CG1   1 
ATOM   7217 C  CG2   . VAL C 3 70  ? 130.027 107.312 136.679 1.00 60.29  ? 70  VAL K CG2   1 
ATOM   7218 N  N     . LYS C 3 71  ? 134.036 105.893 138.428 1.00 54.59  ? 71  LYS K N     1 
ATOM   7219 C  CA    . LYS C 3 71  ? 134.944 105.131 139.278 1.00 53.60  ? 71  LYS K CA    1 
ATOM   7220 C  C     . LYS C 3 71  ? 135.702 106.044 140.237 1.00 58.15  ? 71  LYS K C     1 
ATOM   7221 O  O     . LYS C 3 71  ? 135.924 105.688 141.400 1.00 66.63  ? 71  LYS K O     1 
ATOM   7222 C  CB    . LYS C 3 71  ? 135.908 104.318 138.418 1.00 56.08  ? 71  LYS K CB    1 
ATOM   7223 C  CG    . LYS C 3 71  ? 137.120 103.791 139.160 1.00 65.15  ? 71  LYS K CG    1 
ATOM   7224 C  CD    . LYS C 3 71  ? 138.014 102.974 138.244 1.00 64.52  ? 71  LYS K CD    1 
ATOM   7225 C  CE    . LYS C 3 71  ? 139.391 102.769 138.857 1.00 62.63  ? 71  LYS K CE    1 
ATOM   7226 N  NZ    . LYS C 3 71  ? 140.096 104.060 139.091 1.00 64.22  ? 71  LYS K NZ    1 
ATOM   7227 N  N     . ASP C 3 72  ? 136.102 107.229 139.771 1.00 53.55  ? 72  ASP K N     1 
ATOM   7228 C  CA    . ASP C 3 72  ? 136.859 108.148 140.617 1.00 57.99  ? 72  ASP K CA    1 
ATOM   7229 C  C     . ASP C 3 72  ? 136.019 108.688 141.768 1.00 59.90  ? 72  ASP K C     1 
ATOM   7230 O  O     . ASP C 3 72  ? 136.519 108.828 142.890 1.00 67.48  ? 72  ASP K O     1 
ATOM   7231 C  CB    . ASP C 3 72  ? 137.412 109.299 139.779 1.00 66.01  ? 72  ASP K CB    1 
ATOM   7232 C  CG    . ASP C 3 72  ? 138.809 109.025 139.264 1.00 72.95  ? 72  ASP K CG    1 
ATOM   7233 O  OD1   . ASP C 3 72  ? 139.609 108.419 140.007 1.00 73.78  ? 72  ASP K OD1   1 
ATOM   7234 O  OD2   . ASP C 3 72  ? 139.110 109.419 138.118 1.00 70.51  ? 72  ASP K OD2   1 
ATOM   7235 N  N     . VAL C 3 73  ? 134.753 109.016 141.511 1.00 54.92  ? 73  VAL K N     1 
ATOM   7236 C  CA    . VAL C 3 73  ? 133.899 109.569 142.558 1.00 54.21  ? 73  VAL K CA    1 
ATOM   7237 C  C     . VAL C 3 73  ? 133.744 108.573 143.698 1.00 52.48  ? 73  VAL K C     1 
ATOM   7238 O  O     . VAL C 3 73  ? 133.701 108.950 144.874 1.00 56.69  ? 73  VAL K O     1 
ATOM   7239 C  CB    . VAL C 3 73  ? 132.537 109.985 141.973 1.00 58.09  ? 73  VAL K CB    1 
ATOM   7240 C  CG1   . VAL C 3 73  ? 131.545 110.279 143.076 1.00 55.88  ? 73  VAL K CG1   1 
ATOM   7241 C  CG2   . VAL C 3 73  ? 132.700 111.200 141.081 1.00 58.98  ? 73  VAL K CG2   1 
ATOM   7242 N  N     . LEU C 3 74  ? 133.676 107.286 143.369 1.00 48.29  ? 74  LEU K N     1 
ATOM   7243 C  CA    . LEU C 3 74  ? 133.585 106.240 144.376 1.00 46.14  ? 74  LEU K CA    1 
ATOM   7244 C  C     . LEU C 3 74  ? 134.835 106.134 145.236 1.00 56.93  ? 74  LEU K C     1 
ATOM   7245 O  O     . LEU C 3 74  ? 134.786 105.492 146.290 1.00 63.56  ? 74  LEU K O     1 
ATOM   7246 C  CB    . LEU C 3 74  ? 133.311 104.906 143.696 1.00 44.22  ? 74  LEU K CB    1 
ATOM   7247 C  CG    . LEU C 3 74  ? 131.865 104.430 143.646 1.00 53.52  ? 74  LEU K CG    1 
ATOM   7248 C  CD1   . LEU C 3 74  ? 130.913 105.587 143.482 1.00 57.29  ? 74  LEU K CD1   1 
ATOM   7249 C  CD2   . LEU C 3 74  ? 131.710 103.472 142.491 1.00 57.55  ? 74  LEU K CD2   1 
ATOM   7250 N  N     . GLU C 3 75  ? 135.946 106.736 144.820 1.00 64.81  ? 75  GLU K N     1 
ATOM   7251 C  CA    . GLU C 3 75  ? 137.177 106.746 145.596 1.00 56.40  ? 75  GLU K CA    1 
ATOM   7252 C  C     . GLU C 3 75  ? 137.361 108.034 146.384 1.00 59.26  ? 75  GLU K C     1 
ATOM   7253 O  O     . GLU C 3 75  ? 138.450 108.275 146.909 1.00 61.81  ? 75  GLU K O     1 
ATOM   7254 C  CB    . GLU C 3 75  ? 138.379 106.521 144.682 1.00 61.19  ? 75  GLU K CB    1 
ATOM   7255 C  CG    . GLU C 3 75  ? 138.397 105.164 144.005 1.00 66.25  ? 75  GLU K CG    1 
ATOM   7256 C  CD    . GLU C 3 75  ? 139.643 104.947 143.171 1.00 70.96  ? 75  GLU K CD    1 
ATOM   7257 O  OE1   . GLU C 3 75  ? 140.469 105.879 143.082 1.00 69.86  ? 75  GLU K OE1   1 
ATOM   7258 O  OE2   . GLU C 3 75  ? 139.797 103.844 142.605 1.00 67.12  ? 75  GLU K OE2   1 
ATOM   7259 N  N     . GLY C 3 76  ? 136.329 108.865 146.475 1.00 64.06  ? 76  GLY K N     1 
ATOM   7260 C  CA    . GLY C 3 76  ? 136.389 110.078 147.260 1.00 65.89  ? 76  GLY K CA    1 
ATOM   7261 C  C     . GLY C 3 76  ? 136.747 111.337 146.506 1.00 66.56  ? 76  GLY K C     1 
ATOM   7262 O  O     . GLY C 3 76  ? 137.047 112.351 147.144 1.00 69.67  ? 76  GLY K O     1 
ATOM   7263 N  N     . TYR C 3 77  ? 136.726 111.310 145.182 1.00 59.48  ? 77  TYR K N     1 
ATOM   7264 C  CA    . TYR C 3 77  ? 137.100 112.449 144.366 1.00 59.76  ? 77  TYR K CA    1 
ATOM   7265 C  C     . TYR C 3 77  ? 135.846 113.147 143.847 1.00 60.90  ? 77  TYR K C     1 
ATOM   7266 O  O     . TYR C 3 77  ? 134.722 112.826 144.240 1.00 64.54  ? 77  TYR K O     1 
ATOM   7267 C  CB    . TYR C 3 77  ? 138.014 111.987 143.233 1.00 63.08  ? 77  TYR K CB    1 
ATOM   7268 C  CG    . TYR C 3 77  ? 139.407 111.634 143.692 1.00 63.74  ? 77  TYR K CG    1 
ATOM   7269 C  CD1   . TYR C 3 77  ? 140.417 112.581 143.696 1.00 65.09  ? 77  TYR K CD1   1 
ATOM   7270 C  CD2   . TYR C 3 77  ? 139.708 110.355 144.129 1.00 63.65  ? 77  TYR K CD2   1 
ATOM   7271 C  CE1   . TYR C 3 77  ? 141.689 112.263 144.116 1.00 65.75  ? 77  TYR K CE1   1 
ATOM   7272 C  CE2   . TYR C 3 77  ? 140.975 110.028 144.553 1.00 65.76  ? 77  TYR K CE2   1 
ATOM   7273 C  CZ    . TYR C 3 77  ? 141.963 110.985 144.545 1.00 67.03  ? 77  TYR K CZ    1 
ATOM   7274 O  OH    . TYR C 3 77  ? 143.232 110.662 144.966 1.00 69.56  ? 77  TYR K OH    1 
ATOM   7275 N  N     . ASN C 3 78  ? 136.033 114.113 142.956 1.00 55.53  ? 78  ASN K N     1 
ATOM   7276 C  CA    . ASN C 3 78  ? 134.931 114.861 142.374 1.00 50.25  ? 78  ASN K CA    1 
ATOM   7277 C  C     . ASN C 3 78  ? 135.041 114.859 140.858 1.00 59.10  ? 78  ASN K C     1 
ATOM   7278 O  O     . ASN C 3 78  ? 136.124 114.686 140.297 1.00 66.43  ? 78  ASN K O     1 
ATOM   7279 C  CB    . ASN C 3 78  ? 134.898 116.299 142.883 1.00 47.20  ? 78  ASN K CB    1 
ATOM   7280 C  CG    . ASN C 3 78  ? 134.373 116.402 144.292 1.00 54.95  ? 78  ASN K CG    1 
ATOM   7281 O  OD1   . ASN C 3 78  ? 133.577 115.576 144.729 1.00 66.14  ? 78  ASN K OD1   1 
ATOM   7282 N  ND2   . ASN C 3 78  ? 134.815 117.420 145.015 1.00 57.88  ? 78  ASN K ND2   1 
ATOM   7283 N  N     . GLY C 3 79  ? 133.903 115.054 140.200 1.00 46.82  ? 79  GLY K N     1 
ATOM   7284 C  CA    . GLY C 3 79  ? 133.867 115.100 138.752 1.00 45.07  ? 79  GLY K CA    1 
ATOM   7285 C  C     . GLY C 3 79  ? 132.670 115.881 138.260 1.00 44.88  ? 79  GLY K C     1 
ATOM   7286 O  O     . GLY C 3 79  ? 131.695 116.089 138.986 1.00 52.09  ? 79  GLY K O     1 
ATOM   7287 N  N     . THR C 3 80  ? 132.754 116.307 137.004 1.00 46.74  ? 80  THR K N     1 
ATOM   7288 C  CA    . THR C 3 80  ? 131.725 117.128 136.385 1.00 45.25  ? 80  THR K CA    1 
ATOM   7289 C  C     . THR C 3 80  ? 131.548 116.711 134.934 1.00 48.24  ? 80  THR K C     1 
ATOM   7290 O  O     . THR C 3 80  ? 132.524 116.405 134.247 1.00 55.64  ? 80  THR K O     1 
ATOM   7291 C  CB    . THR C 3 80  ? 132.085 118.616 136.458 1.00 53.20  ? 80  THR K CB    1 
ATOM   7292 O  OG1   . THR C 3 80  ? 132.413 118.963 137.808 1.00 59.35  ? 80  THR K OG1   1 
ATOM   7293 C  CG2   . THR C 3 80  ? 130.918 119.471 136.004 1.00 52.98  ? 80  THR K CG2   1 
ATOM   7294 N  N     . ILE C 3 81  ? 130.301 116.691 134.472 1.00 46.73  ? 81  ILE K N     1 
ATOM   7295 C  CA    . ILE C 3 81  ? 129.974 116.367 133.089 1.00 41.49  ? 81  ILE K CA    1 
ATOM   7296 C  C     . ILE C 3 81  ? 129.009 117.420 132.564 1.00 43.48  ? 81  ILE K C     1 
ATOM   7297 O  O     . ILE C 3 81  ? 127.942 117.633 133.149 1.00 52.70  ? 81  ILE K O     1 
ATOM   7298 C  CB    . ILE C 3 81  ? 129.366 114.963 132.953 1.00 42.09  ? 81  ILE K CB    1 
ATOM   7299 C  CG1   . ILE C 3 81  ? 130.394 113.899 133.321 1.00 46.74  ? 81  ILE K CG1   1 
ATOM   7300 C  CG2   . ILE C 3 81  ? 128.877 114.735 131.549 1.00 41.25  ? 81  ILE K CG2   1 
ATOM   7301 C  CD1   . ILE C 3 81  ? 129.865 112.503 133.238 1.00 46.26  ? 81  ILE K CD1   1 
ATOM   7302 N  N     . PHE C 3 82  ? 129.383 118.076 131.472 1.00 42.97  ? 82  PHE K N     1 
ATOM   7303 C  CA    . PHE C 3 82  ? 128.539 119.061 130.814 1.00 41.48  ? 82  PHE K CA    1 
ATOM   7304 C  C     . PHE C 3 82  ? 127.837 118.426 129.619 1.00 44.64  ? 82  PHE K C     1 
ATOM   7305 O  O     . PHE C 3 82  ? 128.181 117.332 129.175 1.00 53.79  ? 82  PHE K O     1 
ATOM   7306 C  CB    . PHE C 3 82  ? 129.363 120.270 130.364 1.00 47.13  ? 82  PHE K CB    1 
ATOM   7307 C  CG    . PHE C 3 82  ? 129.960 121.061 131.492 1.00 43.71  ? 82  PHE K CG    1 
ATOM   7308 C  CD1   . PHE C 3 82  ? 131.185 120.715 132.023 1.00 48.96  ? 82  PHE K CD1   1 
ATOM   7309 C  CD2   . PHE C 3 82  ? 129.305 122.156 132.011 1.00 42.64  ? 82  PHE K CD2   1 
ATOM   7310 C  CE1   . PHE C 3 82  ? 131.735 121.440 133.051 1.00 45.86  ? 82  PHE K CE1   1 
ATOM   7311 C  CE2   . PHE C 3 82  ? 129.854 122.881 133.039 1.00 45.81  ? 82  PHE K CE2   1 
ATOM   7312 C  CZ    . PHE C 3 82  ? 131.069 122.521 133.557 1.00 45.28  ? 82  PHE K CZ    1 
ATOM   7313 N  N     . ALA C 3 83  ? 126.841 119.131 129.094 1.00 46.02  ? 83  ALA K N     1 
ATOM   7314 C  CA    . ALA C 3 83  ? 126.108 118.660 127.923 1.00 43.46  ? 83  ALA K CA    1 
ATOM   7315 C  C     . ALA C 3 83  ? 125.571 119.876 127.188 1.00 49.91  ? 83  ALA K C     1 
ATOM   7316 O  O     . ALA C 3 83  ? 124.666 120.550 127.685 1.00 57.51  ? 83  ALA K O     1 
ATOM   7317 C  CB    . ALA C 3 83  ? 124.980 117.717 128.320 1.00 47.07  ? 83  ALA K CB    1 
ATOM   7318 N  N     . TYR C 3 84  ? 126.121 120.151 126.013 1.00 47.77  ? 84  TYR K N     1 
ATOM   7319 C  CA    . TYR C 3 84  ? 125.757 121.319 125.229 1.00 44.19  ? 84  TYR K CA    1 
ATOM   7320 C  C     . TYR C 3 84  ? 125.188 120.885 123.891 1.00 50.82  ? 84  TYR K C     1 
ATOM   7321 O  O     . TYR C 3 84  ? 125.692 119.949 123.264 1.00 58.24  ? 84  TYR K O     1 
ATOM   7322 C  CB    . TYR C 3 84  ? 126.959 122.227 124.998 1.00 44.95  ? 84  TYR K CB    1 
ATOM   7323 C  CG    . TYR C 3 84  ? 126.613 123.500 124.278 1.00 51.62  ? 84  TYR K CG    1 
ATOM   7324 C  CD1   . TYR C 3 84  ? 125.825 124.465 124.879 1.00 52.94  ? 84  TYR K CD1   1 
ATOM   7325 C  CD2   . TYR C 3 84  ? 127.052 123.729 122.988 1.00 54.61  ? 84  TYR K CD2   1 
ATOM   7326 C  CE1   . TYR C 3 84  ? 125.499 125.628 124.221 1.00 50.54  ? 84  TYR K CE1   1 
ATOM   7327 C  CE2   . TYR C 3 84  ? 126.730 124.891 122.322 1.00 55.25  ? 84  TYR K CE2   1 
ATOM   7328 C  CZ    . TYR C 3 84  ? 125.951 125.835 122.944 1.00 51.83  ? 84  TYR K CZ    1 
ATOM   7329 O  OH    . TYR C 3 84  ? 125.628 126.995 122.286 1.00 58.52  ? 84  TYR K OH    1 
ATOM   7330 N  N     . GLY C 3 85  ? 124.138 121.564 123.462 1.00 57.21  ? 85  GLY K N     1 
ATOM   7331 C  CA    . GLY C 3 85  ? 123.564 121.296 122.164 1.00 57.12  ? 85  GLY K CA    1 
ATOM   7332 C  C     . GLY C 3 85  ? 122.392 122.214 121.910 1.00 61.60  ? 85  GLY K C     1 
ATOM   7333 O  O     . GLY C 3 85  ? 121.762 122.730 122.839 1.00 63.51  ? 85  GLY K O     1 
ATOM   7334 N  N     . GLN C 3 86  ? 122.113 122.410 120.628 1.00 59.09  ? 86  GLN K N     1 
ATOM   7335 C  CA    . GLN C 3 86  ? 120.929 123.137 120.213 1.00 56.12  ? 86  GLN K CA    1 
ATOM   7336 C  C     . GLN C 3 86  ? 119.726 122.202 120.260 1.00 61.32  ? 86  GLN K C     1 
ATOM   7337 O  O     . GLN C 3 86  ? 119.846 121.008 120.547 1.00 68.26  ? 86  GLN K O     1 
ATOM   7338 C  CB    . GLN C 3 86  ? 121.127 123.717 118.818 1.00 59.32  ? 86  GLN K CB    1 
ATOM   7339 C  CG    . GLN C 3 86  ? 122.367 124.571 118.667 1.00 61.95  ? 86  GLN K CG    1 
ATOM   7340 C  CD    . GLN C 3 86  ? 122.179 125.971 119.195 1.00 65.19  ? 86  GLN K CD    1 
ATOM   7341 O  OE1   . GLN C 3 86  ? 121.055 126.449 119.330 1.00 64.41  ? 86  GLN K OE1   1 
ATOM   7342 N  NE2   . GLN C 3 86  ? 123.282 126.644 119.491 1.00 64.11  ? 86  GLN K NE2   1 
ATOM   7343 N  N     . THR C 3 87  ? 118.545 122.740 119.985 1.00 62.41  ? 87  THR K N     1 
ATOM   7344 C  CA    . THR C 3 87  ? 117.353 121.908 119.957 1.00 63.07  ? 87  THR K CA    1 
ATOM   7345 C  C     . THR C 3 87  ? 117.428 120.921 118.798 1.00 65.83  ? 87  THR K C     1 
ATOM   7346 O  O     . THR C 3 87  ? 117.934 121.243 117.720 1.00 69.13  ? 87  THR K O     1 
ATOM   7347 C  CB    . THR C 3 87  ? 116.098 122.770 119.838 1.00 68.89  ? 87  THR K CB    1 
ATOM   7348 O  OG1   . THR C 3 87  ? 114.978 121.938 119.515 1.00 70.22  ? 87  THR K OG1   1 
ATOM   7349 C  CG2   . THR C 3 87  ? 116.272 123.822 118.753 1.00 69.86  ? 87  THR K CG2   1 
ATOM   7350 N  N     . SER C 3 88  ? 116.931 119.708 119.037 1.00 63.87  ? 88  SER K N     1 
ATOM   7351 C  CA    . SER C 3 88  ? 116.943 118.629 118.047 1.00 65.97  ? 88  SER K CA    1 
ATOM   7352 C  C     . SER C 3 88  ? 118.365 118.307 117.593 1.00 60.01  ? 88  SER K C     1 
ATOM   7353 O  O     . SER C 3 88  ? 118.673 118.288 116.401 1.00 64.90  ? 88  SER K O     1 
ATOM   7354 C  CB    . SER C 3 88  ? 116.048 118.966 116.852 1.00 69.48  ? 88  SER K CB    1 
ATOM   7355 O  OG    . SER C 3 88  ? 114.685 119.022 117.236 1.00 70.07  ? 88  SER K OG    1 
ATOM   7356 N  N     . SER C 3 89  ? 119.240 118.047 118.561 1.00 53.89  ? 89  SER K N     1 
ATOM   7357 C  CA    . SER C 3 89  ? 120.634 117.754 118.275 1.00 57.29  ? 89  SER K CA    1 
ATOM   7358 C  C     . SER C 3 89  ? 121.153 116.497 118.956 1.00 60.74  ? 89  SER K C     1 
ATOM   7359 O  O     . SER C 3 89  ? 122.320 116.149 118.758 1.00 62.78  ? 89  SER K O     1 
ATOM   7360 C  CB    . SER C 3 89  ? 121.524 118.939 118.675 1.00 63.99  ? 89  SER K CB    1 
ATOM   7361 O  OG    . SER C 3 89  ? 121.208 120.091 117.914 1.00 68.62  ? 89  SER K OG    1 
ATOM   7362 N  N     . GLY C 3 90  ? 120.336 115.809 119.741 1.00 62.16  ? 90  GLY K N     1 
ATOM   7363 C  CA    . GLY C 3 90  ? 120.756 114.589 120.393 1.00 59.60  ? 90  GLY K CA    1 
ATOM   7364 C  C     . GLY C 3 90  ? 121.158 114.716 121.843 1.00 58.79  ? 90  GLY K C     1 
ATOM   7365 O  O     . GLY C 3 90  ? 121.657 113.739 122.413 1.00 66.77  ? 90  GLY K O     1 
ATOM   7366 N  N     . LYS C 3 91  ? 120.947 115.878 122.462 1.00 56.21  ? 91  LYS K N     1 
ATOM   7367 C  CA    . LYS C 3 91  ? 121.320 116.051 123.861 1.00 54.36  ? 91  LYS K CA    1 
ATOM   7368 C  C     . LYS C 3 91  ? 120.552 115.092 124.763 1.00 60.30  ? 91  LYS K C     1 
ATOM   7369 O  O     . LYS C 3 91  ? 121.146 114.379 125.582 1.00 71.15  ? 91  LYS K O     1 
ATOM   7370 C  CB    . LYS C 3 91  ? 121.079 117.497 124.286 1.00 54.35  ? 91  LYS K CB    1 
ATOM   7371 C  CG    . LYS C 3 91  ? 121.858 117.928 125.502 1.00 59.18  ? 91  LYS K CG    1 
ATOM   7372 C  CD    . LYS C 3 91  ? 122.010 119.431 125.543 1.00 60.97  ? 91  LYS K CD    1 
ATOM   7373 C  CE    . LYS C 3 91  ? 120.660 120.119 125.533 1.00 58.98  ? 91  LYS K CE    1 
ATOM   7374 N  NZ    . LYS C 3 91  ? 119.838 119.746 126.710 1.00 63.56  ? 91  LYS K NZ    1 
ATOM   7375 N  N     . THR C 3 92  ? 119.227 115.052 124.622 1.00 59.39  ? 92  THR K N     1 
ATOM   7376 C  CA    . THR C 3 92  ? 118.422 114.240 125.528 1.00 61.16  ? 92  THR K CA    1 
ATOM   7377 C  C     . THR C 3 92  ? 118.624 112.754 125.267 1.00 60.58  ? 92  THR K C     1 
ATOM   7378 O  O     . THR C 3 92  ? 118.590 111.945 126.201 1.00 69.91  ? 92  THR K O     1 
ATOM   7379 C  CB    . THR C 3 92  ? 116.948 114.615 125.406 1.00 63.78  ? 92  THR K CB    1 
ATOM   7380 O  OG1   . THR C 3 92  ? 116.822 116.041 125.356 1.00 64.38  ? 92  THR K OG1   1 
ATOM   7381 C  CG2   . THR C 3 92  ? 116.167 114.092 126.597 1.00 63.21  ? 92  THR K CG2   1 
ATOM   7382 N  N     . HIS C 3 93  ? 118.829 112.371 124.007 1.00 47.95  ? 93  HIS K N     1 
ATOM   7383 C  CA    . HIS C 3 93  ? 119.130 110.977 123.709 1.00 52.82  ? 93  HIS K CA    1 
ATOM   7384 C  C     . HIS C 3 93  ? 120.467 110.562 124.302 1.00 63.12  ? 93  HIS K C     1 
ATOM   7385 O  O     . HIS C 3 93  ? 120.583 109.479 124.886 1.00 66.69  ? 93  HIS K O     1 
ATOM   7386 C  CB    . HIS C 3 93  ? 119.127 110.746 122.204 1.00 55.84  ? 93  HIS K CB    1 
ATOM   7387 C  CG    . HIS C 3 93  ? 119.417 109.334 121.810 1.00 58.90  ? 93  HIS K CG    1 
ATOM   7388 N  ND1   . HIS C 3 93  ? 118.510 108.313 121.980 1.00 62.37  ? 93  HIS K ND1   1 
ATOM   7389 C  CD2   . HIS C 3 93  ? 120.513 108.774 121.249 1.00 57.07  ? 93  HIS K CD2   1 
ATOM   7390 C  CE1   . HIS C 3 93  ? 119.033 107.184 121.539 1.00 60.95  ? 93  HIS K CE1   1 
ATOM   7391 N  NE2   . HIS C 3 93  ? 120.249 107.436 121.092 1.00 59.86  ? 93  HIS K NE2   1 
ATOM   7392 N  N     . THR C 3 94  ? 121.427 111.483 124.346 1.00 62.37  ? 94  THR K N     1 
ATOM   7393 C  CA    . THR C 3 94  ? 122.753 111.075 124.838 1.00 57.99  ? 94  THR K CA    1 
ATOM   7394 C  C     . THR C 3 94  ? 122.779 111.110 126.340 1.00 59.85  ? 94  THR K C     1 
ATOM   7395 O  O     . THR C 3 94  ? 123.634 110.403 126.910 1.00 65.18  ? 94  THR K O     1 
ATOM   7396 C  CB    . THR C 3 94  ? 123.857 111.937 124.244 1.00 58.18  ? 94  THR K CB    1 
ATOM   7397 O  OG1   . THR C 3 94  ? 125.013 111.110 124.276 1.00 65.98  ? 94  THR K OG1   1 
ATOM   7398 C  CG2   . THR C 3 94  ? 124.136 113.198 125.038 1.00 59.02  ? 94  THR K CG2   1 
ATOM   7399 N  N     . MET C 3 95  ? 121.894 111.855 126.988 1.00 59.47  ? 95  MET K N     1 
ATOM   7400 C  CA    . MET C 3 95  ? 122.020 111.996 128.458 1.00 57.41  ? 95  MET K CA    1 
ATOM   7401 C  C     . MET C 3 95  ? 120.709 111.611 129.137 1.00 62.69  ? 95  MET K C     1 
ATOM   7402 O  O     . MET C 3 95  ? 120.432 112.181 130.206 1.00 66.68  ? 95  MET K O     1 
ATOM   7403 C  CB    . MET C 3 95  ? 122.454 113.411 128.839 1.00 58.10  ? 95  MET K CB    1 
ATOM   7404 C  CG    . MET C 3 95  ? 123.948 113.618 128.834 1.00 59.20  ? 95  MET K CG    1 
ATOM   7405 S  SD    . MET C 3 95  ? 124.482 114.750 130.131 1.00 78.98  ? 95  MET K SD    1 
ATOM   7406 C  CE    . MET C 3 95  ? 124.911 113.613 131.455 1.00 65.29  ? 95  MET K CE    1 
ATOM   7407 N  N     . GLU C 3 96  ? 119.966 110.663 128.580 1.00 70.24  ? 96  GLU K N     1 
ATOM   7408 C  CA    . GLU C 3 96  ? 118.724 110.158 129.210 1.00 67.96  ? 96  GLU K CA    1 
ATOM   7409 C  C     . GLU C 3 96  ? 118.234 108.978 128.380 1.00 70.94  ? 96  GLU K C     1 
ATOM   7410 O  O     . GLU C 3 96  ? 118.080 107.892 128.948 1.00 75.08  ? 96  GLU K O     1 
ATOM   7411 C  CB    . GLU C 3 96  ? 117.631 111.210 129.352 1.00 70.69  ? 96  GLU K CB    1 
ATOM   7412 C  CG    . GLU C 3 96  ? 117.986 112.318 130.337 1.00 76.01  ? 96  GLU K CG    1 
ATOM   7413 C  CD    . GLU C 3 96  ? 116.927 113.401 130.422 1.00 79.73  ? 96  GLU K CD    1 
ATOM   7414 O  OE1   . GLU C 3 96  ? 116.008 113.389 129.577 1.00 79.04  ? 96  GLU K OE1   1 
ATOM   7415 O  OE2   . GLU C 3 96  ? 117.021 114.255 131.328 1.00 77.26  ? 96  GLU K OE2   1 
ATOM   7416 N  N     . GLY C 3 97  ? 118.032 109.173 127.089 1.00 72.74  ? 97  GLY K N     1 
ATOM   7417 C  CA    . GLY C 3 97  ? 117.675 108.050 126.250 1.00 71.67  ? 97  GLY K CA    1 
ATOM   7418 C  C     . GLY C 3 97  ? 116.413 107.356 126.733 1.00 75.15  ? 97  GLY K C     1 
ATOM   7419 O  O     . GLY C 3 97  ? 115.595 107.915 127.466 1.00 78.93  ? 97  GLY K O     1 
ATOM   7420 N  N     . LYS C 3 98  ? 116.261 106.107 126.302 1.00 79.11  ? 98  LYS K N     1 
ATOM   7421 C  CA    . LYS C 3 98  ? 115.171 105.281 126.797 1.00 80.71  ? 98  LYS K CA    1 
ATOM   7422 C  C     . LYS C 3 98  ? 115.468 104.853 128.228 1.00 84.59  ? 98  LYS K C     1 
ATOM   7423 O  O     . LYS C 3 98  ? 116.497 104.226 128.499 1.00 87.26  ? 98  LYS K O     1 
ATOM   7424 C  CB    . LYS C 3 98  ? 114.978 104.064 125.898 1.00 82.17  ? 98  LYS K CB    1 
ATOM   7425 C  CG    . LYS C 3 98  ? 113.690 104.087 125.093 1.00 83.10  ? 98  LYS K CG    1 
ATOM   7426 C  CD    . LYS C 3 98  ? 113.532 105.399 124.343 1.00 85.40  ? 98  LYS K CD    1 
ATOM   7427 C  CE    . LYS C 3 98  ? 112.189 105.473 123.634 1.00 83.94  ? 98  LYS K CE    1 
ATOM   7428 N  NZ    . LYS C 3 98  ? 111.985 106.787 122.964 1.00 83.06  ? 98  LYS K NZ    1 
ATOM   7429 N  N     . LEU C 3 99  ? 114.562 105.189 129.146 1.00 86.86  ? 99  LEU K N     1 
ATOM   7430 C  CA    . LEU C 3 99  ? 114.837 105.044 130.571 1.00 87.41  ? 99  LEU K CA    1 
ATOM   7431 C  C     . LEU C 3 99  ? 114.886 103.597 131.039 1.00 87.50  ? 99  LEU K C     1 
ATOM   7432 O  O     . LEU C 3 99  ? 115.341 103.349 132.160 1.00 88.34  ? 99  LEU K O     1 
ATOM   7433 C  CB    . LEU C 3 99  ? 113.791 105.805 131.386 1.00 86.45  ? 99  LEU K CB    1 
ATOM   7434 C  CG    . LEU C 3 99  ? 113.758 107.322 131.205 1.00 86.46  ? 99  LEU K CG    1 
ATOM   7435 C  CD1   . LEU C 3 99  ? 112.733 107.951 132.135 1.00 85.36  ? 99  LEU K CD1   1 
ATOM   7436 C  CD2   . LEU C 3 99  ? 115.136 107.915 131.446 1.00 84.35  ? 99  LEU K CD2   1 
ATOM   7437 N  N     . HIS C 3 100 ? 114.438 102.641 130.228 1.00 85.71  ? 100 HIS K N     1 
ATOM   7438 C  CA    . HIS C 3 100 ? 114.406 101.250 130.654 1.00 84.71  ? 100 HIS K CA    1 
ATOM   7439 C  C     . HIS C 3 100 ? 115.009 100.275 129.657 1.00 84.37  ? 100 HIS K C     1 
ATOM   7440 O  O     . HIS C 3 100 ? 115.198 99.107  130.012 1.00 83.55  ? 100 HIS K O     1 
ATOM   7441 C  CB    . HIS C 3 100 ? 112.965 100.812 130.957 1.00 88.33  ? 100 HIS K CB    1 
ATOM   7442 C  CG    . HIS C 3 100 ? 112.288 101.637 132.007 1.00 90.94  ? 100 HIS K CG    1 
ATOM   7443 N  ND1   . HIS C 3 100 ? 111.798 102.901 131.760 1.00 89.29  ? 100 HIS K ND1   1 
ATOM   7444 C  CD2   . HIS C 3 100 ? 112.020 101.378 133.308 1.00 89.66  ? 100 HIS K CD2   1 
ATOM   7445 C  CE1   . HIS C 3 100 ? 111.256 103.385 132.863 1.00 87.65  ? 100 HIS K CE1   1 
ATOM   7446 N  NE2   . HIS C 3 100 ? 111.378 102.480 133.817 1.00 89.83  ? 100 HIS K NE2   1 
ATOM   7447 N  N     . ASP C 3 101 ? 115.311 100.699 128.441 1.00 93.14  ? 101 ASP K N     1 
ATOM   7448 C  CA    . ASP C 3 101 ? 115.882 99.788  127.458 1.00 93.75  ? 101 ASP K CA    1 
ATOM   7449 C  C     . ASP C 3 101 ? 117.361 99.568  127.753 1.00 91.49  ? 101 ASP K C     1 
ATOM   7450 O  O     . ASP C 3 101 ? 118.124 100.538 127.824 1.00 92.79  ? 101 ASP K O     1 
ATOM   7451 C  CB    . ASP C 3 101 ? 115.700 100.342 126.048 1.00 94.80  ? 101 ASP K CB    1 
ATOM   7452 C  CG    . ASP C 3 101 ? 116.155 99.371  124.977 1.00 96.22  ? 101 ASP K CG    1 
ATOM   7453 O  OD1   . ASP C 3 101 ? 115.516 98.308  124.826 1.00 94.92  ? 101 ASP K OD1   1 
ATOM   7454 O  OD2   . ASP C 3 101 ? 117.151 99.669  124.286 1.00 97.03  ? 101 ASP K OD2   1 
ATOM   7455 N  N     . PRO C 3 102 ? 117.805 98.321  127.931 1.00 84.75  ? 102 PRO K N     1 
ATOM   7456 C  CA    . PRO C 3 102 ? 119.225 98.079  128.226 1.00 84.24  ? 102 PRO K CA    1 
ATOM   7457 C  C     . PRO C 3 102 ? 120.162 98.472  127.100 1.00 85.53  ? 102 PRO K C     1 
ATOM   7458 O  O     . PRO C 3 102 ? 121.351 98.696  127.362 1.00 85.82  ? 102 PRO K O     1 
ATOM   7459 C  CB    . PRO C 3 102 ? 119.274 96.570  128.488 1.00 84.54  ? 102 PRO K CB    1 
ATOM   7460 C  CG    . PRO C 3 102 ? 118.117 96.022  127.734 1.00 86.63  ? 102 PRO K CG    1 
ATOM   7461 C  CD    . PRO C 3 102 ? 117.044 97.069  127.794 1.00 87.69  ? 102 PRO K CD    1 
ATOM   7462 N  N     . GLU C 3 103 ? 119.677 98.560  125.863 1.00 92.01  ? 103 GLU K N     1 
ATOM   7463 C  CA    . GLU C 3 103 ? 120.490 99.013  124.747 1.00 92.42  ? 103 GLU K CA    1 
ATOM   7464 C  C     . GLU C 3 103 ? 120.222 100.455 124.348 1.00 92.62  ? 103 GLU K C     1 
ATOM   7465 O  O     . GLU C 3 103 ? 120.876 100.953 123.428 1.00 93.78  ? 103 GLU K O     1 
ATOM   7466 C  CB    . GLU C 3 103 ? 120.268 98.114  123.522 1.00 93.53  ? 103 GLU K CB    1 
ATOM   7467 C  CG    . GLU C 3 103 ? 121.333 97.047  123.332 1.00 95.81  ? 103 GLU K CG    1 
ATOM   7468 C  CD    . GLU C 3 103 ? 121.230 95.932  124.355 1.00 97.88  ? 103 GLU K CD    1 
ATOM   7469 O  OE1   . GLU C 3 103 ? 120.109 95.667  124.837 1.00 98.53  ? 103 GLU K OE1   1 
ATOM   7470 O  OE2   . GLU C 3 103 ? 122.270 95.319  124.676 1.00 97.34  ? 103 GLU K OE2   1 
ATOM   7471 N  N     . GLY C 3 104 ? 119.281 101.128 125.001 1.00 84.45  ? 104 GLY K N     1 
ATOM   7472 C  CA    . GLY C 3 104 ? 118.945 102.487 124.639 1.00 82.58  ? 104 GLY K CA    1 
ATOM   7473 C  C     . GLY C 3 104 ? 119.139 103.498 125.747 1.00 83.64  ? 104 GLY K C     1 
ATOM   7474 O  O     . GLY C 3 104 ? 118.880 104.688 125.551 1.00 87.04  ? 104 GLY K O     1 
ATOM   7475 N  N     . MET C 3 105 ? 119.587 103.049 126.913 1.00 75.26  ? 105 MET K N     1 
ATOM   7476 C  CA    . MET C 3 105 ? 119.807 103.967 128.020 1.00 72.52  ? 105 MET K CA    1 
ATOM   7477 C  C     . MET C 3 105 ? 121.023 104.845 127.758 1.00 75.21  ? 105 MET K C     1 
ATOM   7478 O  O     . MET C 3 105 ? 121.958 104.458 127.055 1.00 81.27  ? 105 MET K O     1 
ATOM   7479 C  CB    . MET C 3 105 ? 119.972 103.200 129.330 1.00 75.06  ? 105 MET K CB    1 
ATOM   7480 C  CG    . MET C 3 105 ? 120.919 102.027 129.263 1.00 78.86  ? 105 MET K CG    1 
ATOM   7481 S  SD    . MET C 3 105 ? 121.299 101.365 130.896 1.00 88.31  ? 105 MET K SD    1 
ATOM   7482 C  CE    . MET C 3 105 ? 119.656 101.093 131.545 1.00 79.73  ? 105 MET K CE    1 
ATOM   7483 N  N     . GLY C 3 106 ? 120.997 106.044 128.327 1.00 66.43  ? 106 GLY K N     1 
ATOM   7484 C  CA    . GLY C 3 106 ? 122.014 107.036 128.049 1.00 64.47  ? 106 GLY K CA    1 
ATOM   7485 C  C     . GLY C 3 106 ? 123.159 107.045 129.034 1.00 60.71  ? 106 GLY K C     1 
ATOM   7486 O  O     . GLY C 3 106 ? 123.778 106.009 129.288 1.00 66.30  ? 106 GLY K O     1 
ATOM   7487 N  N     . ILE C 3 107 ? 123.452 108.213 129.592 1.00 50.63  ? 107 ILE K N     1 
ATOM   7488 C  CA    . ILE C 3 107 ? 124.571 108.356 130.513 1.00 51.87  ? 107 ILE K CA    1 
ATOM   7489 C  C     . ILE C 3 107 ? 124.106 108.341 131.961 1.00 55.83  ? 107 ILE K C     1 
ATOM   7490 O  O     . ILE C 3 107 ? 124.684 107.643 132.797 1.00 65.73  ? 107 ILE K O     1 
ATOM   7491 C  CB    . ILE C 3 107 ? 125.360 109.640 130.183 1.00 47.66  ? 107 ILE K CB    1 
ATOM   7492 C  CG1   . ILE C 3 107 ? 126.342 109.383 129.046 1.00 51.91  ? 107 ILE K CG1   1 
ATOM   7493 C  CG2   . ILE C 3 107 ? 126.093 110.151 131.403 1.00 54.22  ? 107 ILE K CG2   1 
ATOM   7494 C  CD1   . ILE C 3 107 ? 127.215 110.560 128.738 1.00 56.58  ? 107 ILE K CD1   1 
ATOM   7495 N  N     . ILE C 3 108 ? 123.067 109.111 132.289 1.00 53.35  ? 108 ILE K N     1 
ATOM   7496 C  CA    . ILE C 3 108 ? 122.622 109.201 133.682 1.00 54.05  ? 108 ILE K CA    1 
ATOM   7497 C  C     . ILE C 3 108 ? 122.129 107.862 134.223 1.00 57.64  ? 108 ILE K C     1 
ATOM   7498 O  O     . ILE C 3 108 ? 122.548 107.476 135.330 1.00 66.68  ? 108 ILE K O     1 
ATOM   7499 C  CB    . ILE C 3 108 ? 121.579 110.323 133.831 1.00 58.08  ? 108 ILE K CB    1 
ATOM   7500 C  CG1   . ILE C 3 108 ? 122.135 111.638 133.292 1.00 59.12  ? 108 ILE K CG1   1 
ATOM   7501 C  CG2   . ILE C 3 108 ? 121.167 110.476 135.277 1.00 63.04  ? 108 ILE K CG2   1 
ATOM   7502 C  CD1   . ILE C 3 108 ? 121.214 112.814 133.499 1.00 59.14  ? 108 ILE K CD1   1 
ATOM   7503 N  N     . PRO C 3 109 ? 121.238 107.129 133.542 1.00 48.84  ? 109 PRO K N     1 
ATOM   7504 C  CA    . PRO C 3 109 ? 120.843 105.820 134.080 1.00 53.95  ? 109 PRO K CA    1 
ATOM   7505 C  C     . PRO C 3 109 ? 122.001 104.853 134.200 1.00 57.51  ? 109 PRO K C     1 
ATOM   7506 O  O     . PRO C 3 109 ? 122.054 104.069 135.153 1.00 65.90  ? 109 PRO K O     1 
ATOM   7507 C  CB    . PRO C 3 109 ? 119.794 105.335 133.073 1.00 57.30  ? 109 PRO K CB    1 
ATOM   7508 C  CG    . PRO C 3 109 ? 119.288 106.553 132.440 1.00 56.49  ? 109 PRO K CG    1 
ATOM   7509 C  CD    . PRO C 3 109 ? 120.466 107.455 132.333 1.00 55.46  ? 109 PRO K CD    1 
ATOM   7510 N  N     . ARG C 3 110 ? 122.942 104.886 133.260 1.00 52.56  ? 110 ARG K N     1 
ATOM   7511 C  CA    . ARG C 3 110 ? 124.095 104.002 133.362 1.00 52.47  ? 110 ARG K CA    1 
ATOM   7512 C  C     . ARG C 3 110 ? 124.958 104.369 134.563 1.00 56.71  ? 110 ARG K C     1 
ATOM   7513 O  O     . ARG C 3 110 ? 125.495 103.486 135.245 1.00 64.74  ? 110 ARG K O     1 
ATOM   7514 C  CB    . ARG C 3 110 ? 124.899 104.048 132.066 1.00 57.04  ? 110 ARG K CB    1 
ATOM   7515 C  CG    . ARG C 3 110 ? 124.328 103.170 130.972 1.00 58.40  ? 110 ARG K CG    1 
ATOM   7516 C  CD    . ARG C 3 110 ? 125.297 102.993 129.826 1.00 58.52  ? 110 ARG K CD    1 
ATOM   7517 N  NE    . ARG C 3 110 ? 124.982 101.812 129.034 1.00 56.05  ? 110 ARG K NE    1 
ATOM   7518 C  CZ    . ARG C 3 110 ? 124.157 101.802 127.999 1.00 61.32  ? 110 ARG K CZ    1 
ATOM   7519 N  NH1   . ARG C 3 110 ? 123.547 102.902 127.593 1.00 64.53  ? 110 ARG K NH1   1 
ATOM   7520 N  NH2   . ARG C 3 110 ? 123.940 100.661 127.354 1.00 65.81  ? 110 ARG K NH2   1 
ATOM   7521 N  N     . ILE C 3 111 ? 125.087 105.666 134.847 1.00 56.09  ? 111 ILE K N     1 
ATOM   7522 C  CA    . ILE C 3 111 ? 125.857 106.107 136.005 1.00 53.20  ? 111 ILE K CA    1 
ATOM   7523 C  C     . ILE C 3 111 ? 125.212 105.616 137.290 1.00 54.55  ? 111 ILE K C     1 
ATOM   7524 O  O     . ILE C 3 111 ? 125.894 105.092 138.180 1.00 59.90  ? 111 ILE K O     1 
ATOM   7525 C  CB    . ILE C 3 111 ? 126.009 107.639 136.003 1.00 52.30  ? 111 ILE K CB    1 
ATOM   7526 C  CG1   . ILE C 3 111 ? 126.996 108.079 134.929 1.00 55.62  ? 111 ILE K CG1   1 
ATOM   7527 C  CG2   . ILE C 3 111 ? 126.491 108.125 137.349 1.00 54.24  ? 111 ILE K CG2   1 
ATOM   7528 C  CD1   . ILE C 3 111 ? 127.355 109.540 135.002 1.00 59.31  ? 111 ILE K CD1   1 
ATOM   7529 N  N     . VAL C 3 112 ? 123.892 105.770 137.414 1.00 52.62  ? 112 VAL K N     1 
ATOM   7530 C  CA    . VAL C 3 112 ? 123.242 105.311 138.641 1.00 53.73  ? 112 VAL K CA    1 
ATOM   7531 C  C     . VAL C 3 112 ? 123.316 103.790 138.749 1.00 56.17  ? 112 VAL K C     1 
ATOM   7532 O  O     . VAL C 3 112 ? 123.490 103.238 139.846 1.00 63.84  ? 112 VAL K O     1 
ATOM   7533 C  CB    . VAL C 3 112 ? 121.795 105.836 138.743 1.00 53.73  ? 112 VAL K CB    1 
ATOM   7534 C  CG1   . VAL C 3 112 ? 121.768 107.344 138.581 1.00 57.71  ? 112 VAL K CG1   1 
ATOM   7535 C  CG2   . VAL C 3 112 ? 120.874 105.166 137.749 1.00 57.04  ? 112 VAL K CG2   1 
ATOM   7536 N  N     . GLN C 3 113 ? 123.227 103.090 137.615 1.00 57.43  ? 113 GLN K N     1 
ATOM   7537 C  CA    . GLN C 3 113 ? 123.333 101.638 137.624 1.00 55.10  ? 113 GLN K CA    1 
ATOM   7538 C  C     . GLN C 3 113 ? 124.692 101.193 138.145 1.00 61.41  ? 113 GLN K C     1 
ATOM   7539 O  O     . GLN C 3 113 ? 124.781 100.314 139.009 1.00 68.04  ? 113 GLN K O     1 
ATOM   7540 C  CB    . GLN C 3 113 ? 123.088 101.094 136.218 1.00 54.54  ? 113 GLN K CB    1 
ATOM   7541 C  CG    . GLN C 3 113 ? 122.612 99.660  136.172 1.00 61.62  ? 113 GLN K CG    1 
ATOM   7542 C  CD    . GLN C 3 113 ? 121.130 99.531  136.451 1.00 71.49  ? 113 GLN K CD    1 
ATOM   7543 O  OE1   . GLN C 3 113 ? 120.400 100.522 136.466 1.00 72.40  ? 113 GLN K OE1   1 
ATOM   7544 N  NE2   . GLN C 3 113 ? 120.674 98.303  136.674 1.00 68.59  ? 113 GLN K NE2   1 
ATOM   7545 N  N     . ASP C 3 114 ? 125.765 101.802 137.639 1.00 65.40  ? 114 ASP K N     1 
ATOM   7546 C  CA    . ASP C 3 114 ? 127.101 101.447 138.110 1.00 64.24  ? 114 ASP K CA    1 
ATOM   7547 C  C     . ASP C 3 114 ? 127.285 101.812 139.577 1.00 63.25  ? 114 ASP K C     1 
ATOM   7548 O  O     . ASP C 3 114 ? 127.875 101.043 140.352 1.00 65.12  ? 114 ASP K O     1 
ATOM   7549 C  CB    . ASP C 3 114 ? 128.157 102.133 137.248 1.00 66.28  ? 114 ASP K CB    1 
ATOM   7550 C  CG    . ASP C 3 114 ? 129.544 101.567 137.467 1.00 74.68  ? 114 ASP K CG    1 
ATOM   7551 O  OD1   . ASP C 3 114 ? 129.655 100.468 138.049 1.00 74.75  ? 114 ASP K OD1   1 
ATOM   7552 O  OD2   . ASP C 3 114 ? 130.526 102.221 137.056 1.00 75.77  ? 114 ASP K OD2   1 
ATOM   7553 N  N     . ILE C 3 115 ? 126.775 102.978 139.982 1.00 55.99  ? 115 ILE K N     1 
ATOM   7554 C  CA    . ILE C 3 115 ? 126.979 103.437 141.348 1.00 56.46  ? 115 ILE K CA    1 
ATOM   7555 C  C     . ILE C 3 115 ? 126.293 102.503 142.328 1.00 57.78  ? 115 ILE K C     1 
ATOM   7556 O  O     . ILE C 3 115 ? 126.812 102.258 143.422 1.00 63.75  ? 115 ILE K O     1 
ATOM   7557 C  CB    . ILE C 3 115 ? 126.501 104.895 141.497 1.00 56.45  ? 115 ILE K CB    1 
ATOM   7558 C  CG1   . ILE C 3 115 ? 127.373 105.829 140.669 1.00 58.03  ? 115 ILE K CG1   1 
ATOM   7559 C  CG2   . ILE C 3 115 ? 126.539 105.353 142.942 1.00 57.39  ? 115 ILE K CG2   1 
ATOM   7560 C  CD1   . ILE C 3 115 ? 126.816 107.224 140.552 1.00 61.37  ? 115 ILE K CD1   1 
ATOM   7561 N  N     . PHE C 3 116 ? 125.138 101.949 141.963 1.00 57.81  ? 116 PHE K N     1 
ATOM   7562 C  CA    . PHE C 3 116 ? 124.468 101.028 142.870 1.00 51.58  ? 116 PHE K CA    1 
ATOM   7563 C  C     . PHE C 3 116 ? 124.987 99.605  142.755 1.00 57.02  ? 116 PHE K C     1 
ATOM   7564 O  O     . PHE C 3 116 ? 124.895 98.844  143.724 1.00 64.99  ? 116 PHE K O     1 
ATOM   7565 C  CB    . PHE C 3 116 ? 122.961 101.042 142.630 1.00 55.19  ? 116 PHE K CB    1 
ATOM   7566 C  CG    . PHE C 3 116 ? 122.219 101.951 143.551 1.00 56.60  ? 116 PHE K CG    1 
ATOM   7567 C  CD1   . PHE C 3 116 ? 121.976 103.261 143.198 1.00 55.58  ? 116 PHE K CD1   1 
ATOM   7568 C  CD2   . PHE C 3 116 ? 121.772 101.500 144.775 1.00 63.69  ? 116 PHE K CD2   1 
ATOM   7569 C  CE1   . PHE C 3 116 ? 121.296 104.102 144.039 1.00 57.43  ? 116 PHE K CE1   1 
ATOM   7570 C  CE2   . PHE C 3 116 ? 121.090 102.341 145.625 1.00 65.83  ? 116 PHE K CE2   1 
ATOM   7571 C  CZ    . PHE C 3 116 ? 120.854 103.645 145.254 1.00 61.75  ? 116 PHE K CZ    1 
ATOM   7572 N  N     . ASN C 3 117 ? 125.523 99.219  141.596 1.00 56.68  ? 117 ASN K N     1 
ATOM   7573 C  CA    . ASN C 3 117 ? 126.164 97.916  141.496 1.00 55.84  ? 117 ASN K CA    1 
ATOM   7574 C  C     . ASN C 3 117 ? 127.413 97.856  142.356 1.00 62.62  ? 117 ASN K C     1 
ATOM   7575 O  O     . ASN C 3 117 ? 127.768 96.786  142.861 1.00 68.11  ? 117 ASN K O     1 
ATOM   7576 C  CB    . ASN C 3 117 ? 126.511 97.604  140.044 1.00 55.35  ? 117 ASN K CB    1 
ATOM   7577 C  CG    . ASN C 3 117 ? 125.295 97.280  139.217 1.00 63.07  ? 117 ASN K CG    1 
ATOM   7578 O  OD1   . ASN C 3 117 ? 124.164 97.468  139.658 1.00 67.63  ? 117 ASN K OD1   1 
ATOM   7579 N  ND2   . ASN C 3 117 ? 125.518 96.790  138.005 1.00 61.63  ? 117 ASN K ND2   1 
ATOM   7580 N  N     . TYR C 3 118 ? 128.094 98.988  142.524 1.00 62.92  ? 118 TYR K N     1 
ATOM   7581 C  CA    . TYR C 3 118 ? 129.219 99.028  143.453 1.00 60.00  ? 118 TYR K CA    1 
ATOM   7582 C  C     . TYR C 3 118 ? 128.773 98.750  144.884 1.00 62.66  ? 118 TYR K C     1 
ATOM   7583 O  O     . TYR C 3 118 ? 129.431 97.993  145.607 1.00 68.16  ? 118 TYR K O     1 
ATOM   7584 C  CB    . TYR C 3 118 ? 129.909 100.384 143.369 1.00 60.78  ? 118 TYR K CB    1 
ATOM   7585 C  CG    . TYR C 3 118 ? 131.275 100.438 144.002 1.00 55.23  ? 118 TYR K CG    1 
ATOM   7586 C  CD1   . TYR C 3 118 ? 132.380 99.917  143.356 1.00 58.36  ? 118 TYR K CD1   1 
ATOM   7587 C  CD2   . TYR C 3 118 ? 131.461 101.033 145.235 1.00 60.55  ? 118 TYR K CD2   1 
ATOM   7588 C  CE1   . TYR C 3 118 ? 133.629 99.978  143.925 1.00 62.57  ? 118 TYR K CE1   1 
ATOM   7589 C  CE2   . TYR C 3 118 ? 132.705 101.098 145.811 1.00 63.25  ? 118 TYR K CE2   1 
ATOM   7590 C  CZ    . TYR C 3 118 ? 133.786 100.571 145.152 1.00 62.99  ? 118 TYR K CZ    1 
ATOM   7591 O  OH    . TYR C 3 118 ? 135.031 100.633 145.729 1.00 64.80  ? 118 TYR K OH    1 
ATOM   7592 N  N     . ILE C 3 119 ? 127.661 99.355  145.313 1.00 64.05  ? 119 ILE K N     1 
ATOM   7593 C  CA    . ILE C 3 119 ? 127.201 99.194  146.692 1.00 60.56  ? 119 ILE K CA    1 
ATOM   7594 C  C     . ILE C 3 119 ? 126.814 97.751  146.965 1.00 66.46  ? 119 ILE K C     1 
ATOM   7595 O  O     . ILE C 3 119 ? 127.163 97.184  148.007 1.00 70.34  ? 119 ILE K O     1 
ATOM   7596 C  CB    . ILE C 3 119 ? 126.027 100.144 146.989 1.00 64.03  ? 119 ILE K CB    1 
ATOM   7597 C  CG1   . ILE C 3 119 ? 126.260 101.516 146.364 1.00 64.17  ? 119 ILE K CG1   1 
ATOM   7598 C  CG2   . ILE C 3 119 ? 125.796 100.255 148.484 1.00 63.94  ? 119 ILE K CG2   1 
ATOM   7599 C  CD1   . ILE C 3 119 ? 127.446 102.236 146.910 1.00 65.78  ? 119 ILE K CD1   1 
ATOM   7600 N  N     . TYR C 3 120 ? 126.088 97.131  146.037 1.00 72.49  ? 120 TYR K N     1 
ATOM   7601 C  CA    . TYR C 3 120 ? 125.610 95.768  146.226 1.00 67.14  ? 120 TYR K CA    1 
ATOM   7602 C  C     . TYR C 3 120 ? 126.726 94.739  146.205 1.00 66.51  ? 120 TYR K C     1 
ATOM   7603 O  O     . TYR C 3 120 ? 126.431 93.543  146.263 1.00 68.85  ? 120 TYR K O     1 
ATOM   7604 C  CB    . TYR C 3 120 ? 124.582 95.418  145.149 1.00 68.78  ? 120 TYR K CB    1 
ATOM   7605 C  CG    . TYR C 3 120 ? 123.295 96.205  145.237 1.00 72.73  ? 120 TYR K CG    1 
ATOM   7606 C  CD1   . TYR C 3 120 ? 122.936 96.859  146.406 1.00 74.13  ? 120 TYR K CD1   1 
ATOM   7607 C  CD2   . TYR C 3 120 ? 122.438 96.292  144.150 1.00 68.66  ? 120 TYR K CD2   1 
ATOM   7608 C  CE1   . TYR C 3 120 ? 121.762 97.578  146.489 1.00 75.61  ? 120 TYR K CE1   1 
ATOM   7609 C  CE2   . TYR C 3 120 ? 121.264 97.008  144.224 1.00 69.93  ? 120 TYR K CE2   1 
ATOM   7610 C  CZ    . TYR C 3 120 ? 120.930 97.649  145.395 1.00 74.15  ? 120 TYR K CZ    1 
ATOM   7611 O  OH    . TYR C 3 120 ? 119.759 98.365  145.476 1.00 71.01  ? 120 TYR K OH    1 
ATOM   7612 N  N     . SER C 3 121 ? 127.990 95.156  146.116 1.00 63.96  ? 121 SER K N     1 
ATOM   7613 C  CA    . SER C 3 121 ? 129.090 94.212  145.979 1.00 65.83  ? 121 SER K CA    1 
ATOM   7614 C  C     . SER C 3 121 ? 130.298 94.593  146.825 1.00 70.39  ? 121 SER K C     1 
ATOM   7615 O  O     . SER C 3 121 ? 131.409 94.134  146.542 1.00 76.59  ? 121 SER K O     1 
ATOM   7616 C  CB    . SER C 3 121 ? 129.502 94.083  144.513 1.00 71.28  ? 121 SER K CB    1 
ATOM   7617 O  OG    . SER C 3 121 ? 130.704 93.344  144.386 1.00 77.29  ? 121 SER K OG    1 
ATOM   7618 N  N     . MET C 3 122 ? 130.118 95.412  147.856 1.00 77.60  ? 122 MET K N     1 
ATOM   7619 C  CA    . MET C 3 122 ? 131.233 95.871  148.684 1.00 80.76  ? 122 MET K CA    1 
ATOM   7620 C  C     . MET C 3 122 ? 131.005 95.429  150.124 1.00 82.59  ? 122 MET K C     1 
ATOM   7621 O  O     . MET C 3 122 ? 130.516 96.203  150.949 1.00 85.98  ? 122 MET K O     1 
ATOM   7622 C  CB    . MET C 3 122 ? 131.395 97.389  148.583 1.00 80.89  ? 122 MET K CB    1 
ATOM   7623 C  CG    . MET C 3 122 ? 132.248 97.852  147.416 1.00 80.70  ? 122 MET K CG    1 
ATOM   7624 S  SD    . MET C 3 122 ? 133.906 97.154  147.455 1.00 84.69  ? 122 MET K SD    1 
ATOM   7625 C  CE    . MET C 3 122 ? 133.931 96.249  145.910 1.00 80.03  ? 122 MET K CE    1 
ATOM   7626 N  N     . ASP C 3 123 ? 131.384 94.192  150.416 1.00 100.66 ? 123 ASP K N     1 
ATOM   7627 C  CA    . ASP C 3 123 ? 131.490 93.625  151.765 1.00 103.54 ? 123 ASP K CA    1 
ATOM   7628 C  C     . ASP C 3 123 ? 130.251 93.969  152.595 1.00 102.41 ? 123 ASP K C     1 
ATOM   7629 O  O     . ASP C 3 123 ? 129.146 94.116  152.063 1.00 101.71 ? 123 ASP K O     1 
ATOM   7630 C  CB    . ASP C 3 123 ? 132.803 94.080  152.377 1.00 103.61 ? 123 ASP K CB    1 
ATOM   7631 C  CG    . ASP C 3 123 ? 133.276 93.166  153.488 1.00 103.94 ? 123 ASP K CG    1 
ATOM   7632 O  OD1   . ASP C 3 123 ? 133.898 92.127  153.183 1.00 104.86 ? 123 ASP K OD1   1 
ATOM   7633 O  OD2   . ASP C 3 123 ? 133.018 93.487  154.668 1.00 101.19 ? 123 ASP K OD2   1 
ATOM   7634 N  N     . GLU C 3 124 ? 130.427 94.082  153.911 1.00 102.99 ? 124 GLU K N     1 
ATOM   7635 C  CA    . GLU C 3 124 ? 129.359 94.503  154.803 1.00 104.46 ? 124 GLU K CA    1 
ATOM   7636 C  C     . GLU C 3 124 ? 129.832 95.483  155.864 1.00 103.10 ? 124 GLU K C     1 
ATOM   7637 O  O     . GLU C 3 124 ? 129.024 95.892  156.703 1.00 101.65 ? 124 GLU K O     1 
ATOM   7638 C  CB    . GLU C 3 124 ? 128.713 93.286  155.486 1.00 106.47 ? 124 GLU K CB    1 
ATOM   7639 C  CG    . GLU C 3 124 ? 127.221 93.435  155.741 1.00 106.80 ? 124 GLU K CG    1 
ATOM   7640 C  CD    . GLU C 3 124 ? 126.615 92.206  156.391 1.00 106.45 ? 124 GLU K CD    1 
ATOM   7641 O  OE1   . GLU C 3 124 ? 127.335 91.198  156.546 1.00 106.82 ? 124 GLU K OE1   1 
ATOM   7642 O  OE2   . GLU C 3 124 ? 125.418 92.249  156.747 1.00 104.42 ? 124 GLU K OE2   1 
ATOM   7643 N  N     . ASN C 3 125 ? 131.105 95.868  155.860 1.00 105.51 ? 125 ASN K N     1 
ATOM   7644 C  CA    . ASN C 3 125 ? 131.648 96.805  156.833 1.00 108.08 ? 125 ASN K CA    1 
ATOM   7645 C  C     . ASN C 3 125 ? 131.621 98.247  156.348 1.00 109.52 ? 125 ASN K C     1 
ATOM   7646 O  O     . ASN C 3 125 ? 132.105 99.133  157.061 1.00 110.48 ? 125 ASN K O     1 
ATOM   7647 C  CB    . ASN C 3 125 ? 133.083 96.413  157.191 1.00 109.01 ? 125 ASN K CB    1 
ATOM   7648 C  CG    . ASN C 3 125 ? 133.188 94.989  157.699 1.00 110.13 ? 125 ASN K CG    1 
ATOM   7649 O  OD1   . ASN C 3 125 ? 132.213 94.237  157.678 1.00 110.54 ? 125 ASN K OD1   1 
ATOM   7650 N  ND2   . ASN C 3 125 ? 134.375 94.610  158.155 1.00 108.02 ? 125 ASN K ND2   1 
ATOM   7651 N  N     . LEU C 3 126 ? 131.076 98.506  155.164 1.00 96.34  ? 126 LEU K N     1 
ATOM   7652 C  CA    . LEU C 3 126 ? 131.023 99.844  154.591 1.00 92.27  ? 126 LEU K CA    1 
ATOM   7653 C  C     . LEU C 3 126 ? 129.578 100.312 154.514 1.00 90.54  ? 126 LEU K C     1 
ATOM   7654 O  O     . LEU C 3 126 ? 128.722 99.605  153.974 1.00 91.24  ? 126 LEU K O     1 
ATOM   7655 C  CB    . LEU C 3 126 ? 131.658 99.868  153.201 1.00 92.51  ? 126 LEU K CB    1 
ATOM   7656 C  CG    . LEU C 3 126 ? 133.160 99.599  153.119 1.00 94.47  ? 126 LEU K CG    1 
ATOM   7657 C  CD1   . LEU C 3 126 ? 133.440 98.119  152.898 1.00 93.07  ? 126 LEU K CD1   1 
ATOM   7658 C  CD2   . LEU C 3 126 ? 133.794 100.438 152.021 1.00 92.94  ? 126 LEU K CD2   1 
ATOM   7659 N  N     . GLU C 3 127 ? 129.314 101.501 155.045 1.00 83.97  ? 127 GLU K N     1 
ATOM   7660 C  CA    . GLU C 3 127 ? 127.989 102.100 155.030 1.00 85.56  ? 127 GLU K CA    1 
ATOM   7661 C  C     . GLU C 3 127 ? 127.941 103.209 153.988 1.00 91.09  ? 127 GLU K C     1 
ATOM   7662 O  O     . GLU C 3 127 ? 128.869 104.018 153.889 1.00 92.83  ? 127 GLU K O     1 
ATOM   7663 C  CB    . GLU C 3 127 ? 127.623 102.661 156.405 1.00 86.14  ? 127 GLU K CB    1 
ATOM   7664 C  CG    . GLU C 3 127 ? 126.805 101.714 157.262 1.00 89.96  ? 127 GLU K CG    1 
ATOM   7665 C  CD    . GLU C 3 127 ? 125.366 101.601 156.797 1.00 92.43  ? 127 GLU K CD    1 
ATOM   7666 O  OE1   . GLU C 3 127 ? 124.877 102.541 156.136 1.00 92.06  ? 127 GLU K OE1   1 
ATOM   7667 O  OE2   . GLU C 3 127 ? 124.723 100.572 157.093 1.00 91.08  ? 127 GLU K OE2   1 
ATOM   7668 N  N     . PHE C 3 128 ? 126.860 103.244 153.214 1.00 74.72  ? 128 PHE K N     1 
ATOM   7669 C  CA    . PHE C 3 128 ? 126.724 104.180 152.108 1.00 67.04  ? 128 PHE K CA    1 
ATOM   7670 C  C     . PHE C 3 128 ? 125.488 105.049 152.284 1.00 71.90  ? 128 PHE K C     1 
ATOM   7671 O  O     . PHE C 3 128 ? 124.463 104.594 152.796 1.00 74.36  ? 128 PHE K O     1 
ATOM   7672 C  CB    . PHE C 3 128 ? 126.642 103.441 150.783 1.00 66.45  ? 128 PHE K CB    1 
ATOM   7673 C  CG    . PHE C 3 128 ? 127.944 102.861 150.333 1.00 70.14  ? 128 PHE K CG    1 
ATOM   7674 C  CD1   . PHE C 3 128 ? 128.866 103.635 149.657 1.00 73.33  ? 128 PHE K CD1   1 
ATOM   7675 C  CD2   . PHE C 3 128 ? 128.246 101.536 150.580 1.00 71.81  ? 128 PHE K CD2   1 
ATOM   7676 C  CE1   . PHE C 3 128 ? 130.060 103.097 149.234 1.00 72.73  ? 128 PHE K CE1   1 
ATOM   7677 C  CE2   . PHE C 3 128 ? 129.440 100.996 150.161 1.00 75.03  ? 128 PHE K CE2   1 
ATOM   7678 C  CZ    . PHE C 3 128 ? 130.348 101.778 149.487 1.00 72.67  ? 128 PHE K CZ    1 
ATOM   7679 N  N     . HIS C 3 129 ? 125.596 106.305 151.856 1.00 70.90  ? 129 HIS K N     1 
ATOM   7680 C  CA    . HIS C 3 129 ? 124.468 107.224 151.805 1.00 68.28  ? 129 HIS K CA    1 
ATOM   7681 C  C     . HIS C 3 129 ? 124.569 108.052 150.535 1.00 68.48  ? 129 HIS K C     1 
ATOM   7682 O  O     . HIS C 3 129 ? 125.639 108.582 150.225 1.00 74.49  ? 129 HIS K O     1 
ATOM   7683 C  CB    . HIS C 3 129 ? 124.436 108.139 153.032 1.00 66.28  ? 129 HIS K CB    1 
ATOM   7684 C  CG    . HIS C 3 129 ? 124.272 107.409 154.326 1.00 69.78  ? 129 HIS K CG    1 
ATOM   7685 N  ND1   . HIS C 3 129 ? 125.342 106.994 155.087 1.00 72.10  ? 129 HIS K ND1   1 
ATOM   7686 C  CD2   . HIS C 3 129 ? 123.162 107.026 154.997 1.00 68.70  ? 129 HIS K CD2   1 
ATOM   7687 C  CE1   . HIS C 3 129 ? 124.898 106.382 156.170 1.00 71.82  ? 129 HIS K CE1   1 
ATOM   7688 N  NE2   . HIS C 3 129 ? 123.578 106.388 156.140 1.00 69.64  ? 129 HIS K NE2   1 
ATOM   7689 N  N     . ILE C 3 130 ? 123.462 108.167 149.807 1.00 53.29  ? 130 ILE K N     1 
ATOM   7690 C  CA    . ILE C 3 130 ? 123.424 108.877 148.536 1.00 49.94  ? 130 ILE K CA    1 
ATOM   7691 C  C     . ILE C 3 130 ? 122.525 110.091 148.699 1.00 58.36  ? 130 ILE K C     1 
ATOM   7692 O  O     . ILE C 3 130 ? 121.353 109.959 149.069 1.00 65.48  ? 130 ILE K O     1 
ATOM   7693 C  CB    . ILE C 3 130 ? 122.926 107.983 147.392 1.00 51.87  ? 130 ILE K CB    1 
ATOM   7694 C  CG1   . ILE C 3 130 ? 123.515 106.583 147.516 1.00 55.78  ? 130 ILE K CG1   1 
ATOM   7695 C  CG2   . ILE C 3 130 ? 123.292 108.585 146.053 1.00 56.27  ? 130 ILE K CG2   1 
ATOM   7696 C  CD1   . ILE C 3 130 ? 125.005 106.535 147.311 1.00 59.25  ? 130 ILE K CD1   1 
ATOM   7697 N  N     . LYS C 3 131 ? 123.073 111.268 148.426 1.00 61.21  ? 131 LYS K N     1 
ATOM   7698 C  CA    . LYS C 3 131 ? 122.349 112.525 148.507 1.00 59.34  ? 131 LYS K CA    1 
ATOM   7699 C  C     . LYS C 3 131 ? 122.148 113.076 147.104 1.00 63.85  ? 131 LYS K C     1 
ATOM   7700 O  O     . LYS C 3 131 ? 123.066 113.046 146.280 1.00 71.04  ? 131 LYS K O     1 
ATOM   7701 C  CB    . LYS C 3 131 ? 123.105 113.542 149.361 1.00 63.02  ? 131 LYS K CB    1 
ATOM   7702 C  CG    . LYS C 3 131 ? 123.022 113.302 150.852 1.00 64.71  ? 131 LYS K CG    1 
ATOM   7703 C  CD    . LYS C 3 131 ? 121.718 113.818 151.414 1.00 68.43  ? 131 LYS K CD    1 
ATOM   7704 C  CE    . LYS C 3 131 ? 121.962 114.786 152.558 1.00 68.87  ? 131 LYS K CE    1 
ATOM   7705 N  NZ    . LYS C 3 131 ? 120.700 115.426 153.022 1.00 67.09  ? 131 LYS K NZ    1 
ATOM   7706 N  N     . VAL C 3 132 ? 120.948 113.578 146.835 1.00 55.69  ? 132 VAL K N     1 
ATOM   7707 C  CA    . VAL C 3 132 ? 120.578 114.059 145.513 1.00 50.88  ? 132 VAL K CA    1 
ATOM   7708 C  C     . VAL C 3 132 ? 120.054 115.481 145.638 1.00 53.92  ? 132 VAL K C     1 
ATOM   7709 O  O     . VAL C 3 132 ? 119.200 115.760 146.485 1.00 64.62  ? 132 VAL K O     1 
ATOM   7710 C  CB    . VAL C 3 132 ? 119.531 113.146 144.851 1.00 56.82  ? 132 VAL K CB    1 
ATOM   7711 C  CG1   . VAL C 3 132 ? 118.701 113.918 143.841 1.00 61.70  ? 132 VAL K CG1   1 
ATOM   7712 C  CG2   . VAL C 3 132 ? 120.213 111.979 144.182 1.00 58.15  ? 132 VAL K CG2   1 
ATOM   7713 N  N     . SER C 3 133 ? 120.573 116.374 144.803 1.00 51.08  ? 133 SER K N     1 
ATOM   7714 C  CA    . SER C 3 133 ? 120.102 117.744 144.707 1.00 48.48  ? 133 SER K CA    1 
ATOM   7715 C  C     . SER C 3 133 ? 119.772 118.047 143.255 1.00 53.29  ? 133 SER K C     1 
ATOM   7716 O  O     . SER C 3 133 ? 120.249 117.377 142.337 1.00 65.86  ? 133 SER K O     1 
ATOM   7717 C  CB    . SER C 3 133 ? 121.140 118.741 145.230 1.00 57.57  ? 133 SER K CB    1 
ATOM   7718 O  OG    . SER C 3 133 ? 121.497 118.449 146.568 1.00 66.67  ? 133 SER K OG    1 
ATOM   7719 N  N     . TYR C 3 134 ? 118.983 119.034 142.993 1.00 47.67  ? 134 TYR K N     1 
ATOM   7720 C  CA    . TYR C 3 134 ? 118.595 119.403 141.608 1.00 48.54  ? 134 TYR K CA    1 
ATOM   7721 C  C     . TYR C 3 134 ? 118.067 120.814 141.591 1.00 54.86  ? 134 TYR K C     1 
ATOM   7722 O  O     . TYR C 3 134 ? 117.013 121.049 142.194 1.00 60.40  ? 134 TYR K O     1 
ATOM   7723 C  CB    . TYR C 3 134 ? 117.456 118.539 141.090 1.00 51.46  ? 134 TYR K CB    1 
ATOM   7724 C  CG    . TYR C 3 134 ? 117.345 118.319 139.592 1.00 52.09  ? 134 TYR K CG    1 
ATOM   7725 C  CD1   . TYR C 3 134 ? 118.303 118.805 138.721 1.00 51.99  ? 134 TYR K CD1   1 
ATOM   7726 C  CD2   . TYR C 3 134 ? 116.280 117.615 139.060 1.00 53.15  ? 134 TYR K CD2   1 
ATOM   7727 C  CE1   . TYR C 3 134 ? 118.207 118.588 137.360 1.00 50.64  ? 134 TYR K CE1   1 
ATOM   7728 C  CE2   . TYR C 3 134 ? 116.164 117.400 137.700 1.00 53.92  ? 134 TYR K CE2   1 
ATOM   7729 C  CZ    . TYR C 3 134 ? 117.129 117.894 136.848 1.00 53.91  ? 134 TYR K CZ    1 
ATOM   7730 O  OH    . TYR C 3 134 ? 117.023 117.682 135.508 1.00 60.40  ? 134 TYR K OH    1 
ATOM   7731 N  N     . PHE C 3 135 ? 118.706 121.716 140.929 1.00 54.01  ? 135 PHE K N     1 
ATOM   7732 C  CA    . PHE C 3 135 ? 118.319 123.116 140.876 1.00 56.48  ? 135 PHE K CA    1 
ATOM   7733 C  C     . PHE C 3 135 ? 118.666 123.701 139.517 1.00 56.72  ? 135 PHE K C     1 
ATOM   7734 O  O     . PHE C 3 135 ? 119.464 123.143 138.761 1.00 57.38  ? 135 PHE K O     1 
ATOM   7735 C  CB    . PHE C 3 135 ? 118.972 123.927 142.003 1.00 54.64  ? 135 PHE K CB    1 
ATOM   7736 C  CG    . PHE C 3 135 ? 120.447 123.729 142.129 1.00 45.22  ? 135 PHE K CG    1 
ATOM   7737 C  CD1   . PHE C 3 135 ? 120.961 122.736 142.936 1.00 50.80  ? 135 PHE K CD1   1 
ATOM   7738 C  CD2   . PHE C 3 135 ? 121.321 124.563 141.470 1.00 53.71  ? 135 PHE K CD2   1 
ATOM   7739 C  CE1   . PHE C 3 135 ? 122.317 122.563 143.060 1.00 57.44  ? 135 PHE K CE1   1 
ATOM   7740 C  CE2   . PHE C 3 135 ? 122.676 124.396 141.592 1.00 61.73  ? 135 PHE K CE2   1 
ATOM   7741 C  CZ    . PHE C 3 135 ? 123.175 123.395 142.388 1.00 59.38  ? 135 PHE K CZ    1 
ATOM   7742 N  N     . GLU C 3 136 ? 118.047 124.841 139.214 1.00 61.45  ? 136 GLU K N     1 
ATOM   7743 C  CA    . GLU C 3 136 ? 118.218 125.519 137.941 1.00 55.04  ? 136 GLU K CA    1 
ATOM   7744 C  C     . GLU C 3 136 ? 118.651 126.959 138.166 1.00 53.62  ? 136 GLU K C     1 
ATOM   7745 O  O     . GLU C 3 136 ? 118.496 127.515 139.255 1.00 66.77  ? 136 GLU K O     1 
ATOM   7746 C  CB    . GLU C 3 136 ? 116.931 125.493 137.114 1.00 55.65  ? 136 GLU K CB    1 
ATOM   7747 C  CG    . GLU C 3 136 ? 116.012 126.667 137.363 1.00 61.68  ? 136 GLU K CG    1 
ATOM   7748 C  CD    . GLU C 3 136 ? 114.809 126.654 136.452 1.00 68.94  ? 136 GLU K CD    1 
ATOM   7749 O  OE1   . GLU C 3 136 ? 114.608 125.640 135.754 1.00 65.94  ? 136 GLU K OE1   1 
ATOM   7750 O  OE2   . GLU C 3 136 ? 114.062 127.654 136.433 1.00 72.62  ? 136 GLU K OE2   1 
ATOM   7751 N  N     . ILE C 3 137 ? 119.207 127.557 137.116 1.00 49.92  ? 137 ILE K N     1 
ATOM   7752 C  CA    . ILE C 3 137 ? 119.591 128.964 137.102 1.00 55.79  ? 137 ILE K CA    1 
ATOM   7753 C  C     . ILE C 3 137 ? 118.807 129.655 135.998 1.00 58.94  ? 137 ILE K C     1 
ATOM   7754 O  O     . ILE C 3 137 ? 119.062 129.422 134.811 1.00 62.38  ? 137 ILE K O     1 
ATOM   7755 C  CB    . ILE C 3 137 ? 121.099 129.147 136.889 1.00 56.69  ? 137 ILE K CB    1 
ATOM   7756 C  CG1   . ILE C 3 137 ? 121.884 128.550 138.050 1.00 59.15  ? 137 ILE K CG1   1 
ATOM   7757 C  CG2   . ILE C 3 137 ? 121.437 130.610 136.721 1.00 58.10  ? 137 ILE K CG2   1 
ATOM   7758 C  CD1   . ILE C 3 137 ? 123.371 128.632 137.867 1.00 59.57  ? 137 ILE K CD1   1 
ATOM   7759 N  N     . TYR C 3 138 ? 117.867 130.513 136.383 1.00 54.19  ? 138 TYR K N     1 
ATOM   7760 C  CA    . TYR C 3 138 ? 116.997 131.205 135.441 1.00 54.18  ? 138 TYR K CA    1 
ATOM   7761 C  C     . TYR C 3 138 ? 117.085 132.698 135.704 1.00 58.48  ? 138 TYR K C     1 
ATOM   7762 O  O     . TYR C 3 138 ? 116.786 133.149 136.813 1.00 63.55  ? 138 TYR K O     1 
ATOM   7763 C  CB    . TYR C 3 138 ? 115.552 130.721 135.573 1.00 60.30  ? 138 TYR K CB    1 
ATOM   7764 C  CG    . TYR C 3 138 ? 114.593 131.342 134.589 1.00 59.03  ? 138 TYR K CG    1 
ATOM   7765 C  CD1   . TYR C 3 138 ? 114.593 130.966 133.259 1.00 59.13  ? 138 TYR K CD1   1 
ATOM   7766 C  CD2   . TYR C 3 138 ? 113.683 132.299 134.995 1.00 60.60  ? 138 TYR K CD2   1 
ATOM   7767 C  CE1   . TYR C 3 138 ? 113.716 131.529 132.362 1.00 58.94  ? 138 TYR K CE1   1 
ATOM   7768 C  CE2   . TYR C 3 138 ? 112.804 132.867 134.105 1.00 60.51  ? 138 TYR K CE2   1 
ATOM   7769 C  CZ    . TYR C 3 138 ? 112.825 132.478 132.790 1.00 60.38  ? 138 TYR K CZ    1 
ATOM   7770 O  OH    . TYR C 3 138 ? 111.948 133.044 131.897 1.00 63.44  ? 138 TYR K OH    1 
ATOM   7771 N  N     . LEU C 3 139 ? 117.493 133.456 134.687 1.00 64.13  ? 139 LEU K N     1 
ATOM   7772 C  CA    . LEU C 3 139 ? 117.650 134.907 134.789 1.00 61.22  ? 139 LEU K CA    1 
ATOM   7773 C  C     . LEU C 3 139 ? 118.570 135.286 135.947 1.00 64.25  ? 139 LEU K C     1 
ATOM   7774 O  O     . LEU C 3 139 ? 118.272 136.189 136.730 1.00 69.33  ? 139 LEU K O     1 
ATOM   7775 C  CB    . LEU C 3 139 ? 116.294 135.601 134.916 1.00 62.26  ? 139 LEU K CB    1 
ATOM   7776 C  CG    . LEU C 3 139 ? 115.701 136.152 133.621 1.00 64.38  ? 139 LEU K CG    1 
ATOM   7777 C  CD1   . LEU C 3 139 ? 115.354 135.024 132.676 1.00 64.18  ? 139 LEU K CD1   1 
ATOM   7778 C  CD2   . LEU C 3 139 ? 114.476 136.994 133.915 1.00 61.48  ? 139 LEU K CD2   1 
ATOM   7779 N  N     . ASP C 3 140 ? 119.695 134.580 136.053 1.00 63.43  ? 140 ASP K N     1 
ATOM   7780 C  CA    . ASP C 3 140 ? 120.699 134.821 137.090 1.00 63.67  ? 140 ASP K CA    1 
ATOM   7781 C  C     . ASP C 3 140 ? 120.111 134.665 138.490 1.00 68.85  ? 140 ASP K C     1 
ATOM   7782 O  O     . ASP C 3 140 ? 120.456 135.402 139.414 1.00 73.74  ? 140 ASP K O     1 
ATOM   7783 C  CB    . ASP C 3 140 ? 121.348 136.196 136.924 1.00 68.36  ? 140 ASP K CB    1 
ATOM   7784 C  CG    . ASP C 3 140 ? 122.845 136.161 137.144 1.00 75.00  ? 140 ASP K CG    1 
ATOM   7785 O  OD1   . ASP C 3 140 ? 123.421 135.053 137.143 1.00 76.78  ? 140 ASP K OD1   1 
ATOM   7786 O  OD2   . ASP C 3 140 ? 123.448 137.241 137.319 1.00 77.41  ? 140 ASP K OD2   1 
ATOM   7787 N  N     . LYS C 3 141 ? 119.212 133.699 138.648 1.00 65.04  ? 141 LYS K N     1 
ATOM   7788 C  CA    . LYS C 3 141 ? 118.617 133.402 139.942 1.00 64.37  ? 141 LYS K CA    1 
ATOM   7789 C  C     . LYS C 3 141 ? 118.551 131.896 140.132 1.00 64.35  ? 141 LYS K C     1 
ATOM   7790 O  O     . LYS C 3 141 ? 118.049 131.180 139.262 1.00 72.60  ? 141 LYS K O     1 
ATOM   7791 C  CB    . LYS C 3 141 ? 117.219 134.017 140.068 1.00 65.05  ? 141 LYS K CB    1 
ATOM   7792 C  CG    . LYS C 3 141 ? 117.230 135.484 140.450 1.00 69.69  ? 141 LYS K CG    1 
ATOM   7793 C  CD    . LYS C 3 141 ? 115.837 135.978 140.779 1.00 70.22  ? 141 LYS K CD    1 
ATOM   7794 C  CE    . LYS C 3 141 ? 114.972 136.046 139.534 1.00 70.81  ? 141 LYS K CE    1 
ATOM   7795 N  NZ    . LYS C 3 141 ? 113.624 136.607 139.824 1.00 71.93  ? 141 LYS K NZ    1 
ATOM   7796 N  N     . ILE C 3 142 ? 119.051 131.427 141.268 1.00 54.12  ? 142 ILE K N     1 
ATOM   7797 C  CA    . ILE C 3 142 ? 119.064 130.004 141.577 1.00 50.44  ? 142 ILE K CA    1 
ATOM   7798 C  C     . ILE C 3 142 ? 117.696 129.592 142.098 1.00 54.27  ? 142 ILE K C     1 
ATOM   7799 O  O     . ILE C 3 142 ? 117.150 130.218 143.013 1.00 63.28  ? 142 ILE K O     1 
ATOM   7800 C  CB    . ILE C 3 142 ? 120.168 129.686 142.594 1.00 53.64  ? 142 ILE K CB    1 
ATOM   7801 C  CG1   . ILE C 3 142 ? 121.512 130.172 142.064 1.00 56.99  ? 142 ILE K CG1   1 
ATOM   7802 C  CG2   . ILE C 3 142 ? 120.213 128.206 142.883 1.00 56.29  ? 142 ILE K CG2   1 
ATOM   7803 C  CD1   . ILE C 3 142 ? 122.644 129.960 143.009 1.00 58.94  ? 142 ILE K CD1   1 
ATOM   7804 N  N     . ARG C 3 143 ? 117.137 128.537 141.514 1.00 59.93  ? 143 ARG K N     1 
ATOM   7805 C  CA    . ARG C 3 143 ? 115.825 128.034 141.884 1.00 59.73  ? 143 ARG K CA    1 
ATOM   7806 C  C     . ARG C 3 143 ? 115.881 126.528 142.085 1.00 58.45  ? 143 ARG K C     1 
ATOM   7807 O  O     . ARG C 3 143 ? 116.609 125.820 141.390 1.00 62.78  ? 143 ARG K O     1 
ATOM   7808 C  CB    . ARG C 3 143 ? 114.779 128.370 140.824 1.00 60.09  ? 143 ARG K CB    1 
ATOM   7809 C  CG    . ARG C 3 143 ? 114.559 129.849 140.616 1.00 58.60  ? 143 ARG K CG    1 
ATOM   7810 C  CD    . ARG C 3 143 ? 113.766 130.092 139.356 1.00 59.79  ? 143 ARG K CD    1 
ATOM   7811 N  NE    . ARG C 3 143 ? 112.565 129.271 139.314 1.00 66.08  ? 143 ARG K NE    1 
ATOM   7812 C  CZ    . ARG C 3 143 ? 111.350 129.704 139.615 1.00 67.08  ? 143 ARG K CZ    1 
ATOM   7813 N  NH1   . ARG C 3 143 ? 111.133 130.958 139.976 1.00 64.73  ? 143 ARG K NH1   1 
ATOM   7814 N  NH2   . ARG C 3 143 ? 110.326 128.858 139.551 1.00 62.81  ? 143 ARG K NH2   1 
ATOM   7815 N  N     . ASP C 3 144 ? 115.081 126.045 143.029 1.00 61.76  ? 144 ASP K N     1 
ATOM   7816 C  CA    . ASP C 3 144 ? 115.032 124.635 143.390 1.00 60.25  ? 144 ASP K CA    1 
ATOM   7817 C  C     . ASP C 3 144 ? 113.923 123.941 142.617 1.00 66.61  ? 144 ASP K C     1 
ATOM   7818 O  O     . ASP C 3 144 ? 112.781 124.411 142.607 1.00 73.73  ? 144 ASP K O     1 
ATOM   7819 C  CB    . ASP C 3 144 ? 114.798 124.474 144.888 1.00 65.07  ? 144 ASP K CB    1 
ATOM   7820 C  CG    . ASP C 3 144 ? 115.374 123.192 145.431 1.00 73.22  ? 144 ASP K CG    1 
ATOM   7821 O  OD1   . ASP C 3 144 ? 116.070 122.485 144.676 1.00 74.37  ? 144 ASP K OD1   1 
ATOM   7822 O  OD2   . ASP C 3 144 ? 115.132 122.888 146.616 1.00 76.22  ? 144 ASP K OD2   1 
ATOM   7823 N  N     . LEU C 3 145 ? 114.257 122.828 141.971 1.00 59.82  ? 145 LEU K N     1 
ATOM   7824 C  CA    . LEU C 3 145 ? 113.281 122.088 141.188 1.00 62.92  ? 145 LEU K CA    1 
ATOM   7825 C  C     . LEU C 3 145 ? 112.543 121.029 141.992 1.00 64.19  ? 145 LEU K C     1 
ATOM   7826 O  O     . LEU C 3 145 ? 111.542 120.494 141.506 1.00 68.98  ? 145 LEU K O     1 
ATOM   7827 C  CB    . LEU C 3 145 ? 113.954 121.430 139.983 1.00 61.96  ? 145 LEU K CB    1 
ATOM   7828 C  CG    . LEU C 3 145 ? 114.599 122.379 138.975 1.00 63.07  ? 145 LEU K CG    1 
ATOM   7829 C  CD1   . LEU C 3 145 ? 115.264 121.598 137.862 1.00 58.89  ? 145 LEU K CD1   1 
ATOM   7830 C  CD2   . LEU C 3 145 ? 113.565 123.333 138.417 1.00 65.60  ? 145 LEU K CD2   1 
ATOM   7831 N  N     . LEU C 3 146 ? 113.004 120.709 143.196 1.00 57.38  ? 146 LEU K N     1 
ATOM   7832 C  CA    . LEU C 3 146 ? 112.306 119.763 144.053 1.00 58.40  ? 146 LEU K CA    1 
ATOM   7833 C  C     . LEU C 3 146 ? 111.350 120.436 145.028 1.00 64.60  ? 146 LEU K C     1 
ATOM   7834 O  O     . LEU C 3 146 ? 110.591 119.738 145.707 1.00 67.97  ? 146 LEU K O     1 
ATOM   7835 C  CB    . LEU C 3 146 ? 113.310 118.916 144.834 1.00 62.45  ? 146 LEU K CB    1 
ATOM   7836 C  CG    . LEU C 3 146 ? 114.260 118.047 144.015 1.00 61.42  ? 146 LEU K CG    1 
ATOM   7837 C  CD1   . LEU C 3 146 ? 115.058 117.138 144.925 1.00 62.59  ? 146 LEU K CD1   1 
ATOM   7838 C  CD2   . LEU C 3 146 ? 113.498 117.240 142.985 1.00 63.37  ? 146 LEU K CD2   1 
ATOM   7839 N  N     . ASP C 3 147 ? 111.365 121.764 145.110 1.00 75.35  ? 147 ASP K N     1 
ATOM   7840 C  CA    . ASP C 3 147 ? 110.466 122.501 145.995 1.00 72.19  ? 147 ASP K CA    1 
ATOM   7841 C  C     . ASP C 3 147 ? 110.325 123.905 145.426 1.00 72.95  ? 147 ASP K C     1 
ATOM   7842 O  O     . ASP C 3 147 ? 111.275 124.691 145.483 1.00 77.25  ? 147 ASP K O     1 
ATOM   7843 C  CB    . ASP C 3 147 ? 111.006 122.532 147.418 1.00 74.89  ? 147 ASP K CB    1 
ATOM   7844 C  CG    . ASP C 3 147 ? 109.984 123.034 148.418 1.00 82.09  ? 147 ASP K CG    1 
ATOM   7845 O  OD1   . ASP C 3 147 ? 108.826 123.278 148.019 1.00 83.68  ? 147 ASP K OD1   1 
ATOM   7846 O  OD2   . ASP C 3 147 ? 110.339 123.186 149.606 1.00 82.97  ? 147 ASP K OD2   1 
ATOM   7847 N  N     . VAL C 3 148 ? 109.147 124.219 144.884 1.00 66.51  ? 148 VAL K N     1 
ATOM   7848 C  CA    . VAL C 3 148 ? 108.954 125.479 144.177 1.00 69.31  ? 148 VAL K CA    1 
ATOM   7849 C  C     . VAL C 3 148 ? 108.846 126.680 145.102 1.00 69.34  ? 148 VAL K C     1 
ATOM   7850 O  O     . VAL C 3 148 ? 108.814 127.816 144.618 1.00 74.13  ? 148 VAL K O     1 
ATOM   7851 C  CB    . VAL C 3 148 ? 107.698 125.409 143.286 1.00 74.28  ? 148 VAL K CB    1 
ATOM   7852 C  CG1   . VAL C 3 148 ? 107.802 124.241 142.322 1.00 71.18  ? 148 VAL K CG1   1 
ATOM   7853 C  CG2   . VAL C 3 148 ? 106.447 125.292 144.142 1.00 74.58  ? 148 VAL K CG2   1 
ATOM   7854 N  N     . SER C 3 149 ? 108.772 126.465 146.415 1.00 67.12  ? 149 SER K N     1 
ATOM   7855 C  CA    . SER C 3 149 ? 108.698 127.589 147.341 1.00 69.21  ? 149 SER K CA    1 
ATOM   7856 C  C     . SER C 3 149 ? 109.969 128.427 147.299 1.00 69.56  ? 149 SER K C     1 
ATOM   7857 O  O     . SER C 3 149 ? 109.910 129.661 147.304 1.00 70.39  ? 149 SER K O     1 
ATOM   7858 C  CB    . SER C 3 149 ? 108.435 127.082 148.756 1.00 71.52  ? 149 SER K CB    1 
ATOM   7859 O  OG    . SER C 3 149 ? 107.332 126.195 148.781 1.00 72.34  ? 149 SER K OG    1 
ATOM   7860 N  N     . LYS C 3 150 ? 111.127 127.776 147.257 1.00 70.73  ? 150 LYS K N     1 
ATOM   7861 C  CA    . LYS C 3 150 ? 112.401 128.480 147.250 1.00 67.47  ? 150 LYS K CA    1 
ATOM   7862 C  C     . LYS C 3 150 ? 112.736 128.935 145.837 1.00 68.84  ? 150 LYS K C     1 
ATOM   7863 O  O     . LYS C 3 150 ? 112.740 128.129 144.903 1.00 75.11  ? 150 LYS K O     1 
ATOM   7864 C  CB    . LYS C 3 150 ? 113.500 127.570 147.793 1.00 69.23  ? 150 LYS K CB    1 
ATOM   7865 C  CG    . LYS C 3 150 ? 113.059 126.733 148.979 1.00 68.80  ? 150 LYS K CG    1 
ATOM   7866 C  CD    . LYS C 3 150 ? 114.097 125.695 149.347 1.00 70.39  ? 150 LYS K CD    1 
ATOM   7867 C  CE    . LYS C 3 150 ? 113.649 124.872 150.539 1.00 70.81  ? 150 LYS K CE    1 
ATOM   7868 N  NZ    . LYS C 3 150 ? 114.684 123.887 150.956 1.00 70.31  ? 150 LYS K NZ    1 
ATOM   7869 N  N     . THR C 3 151 ? 113.018 130.228 145.678 1.00 67.67  ? 151 THR K N     1 
ATOM   7870 C  CA    . THR C 3 151 ? 113.244 130.774 144.345 1.00 69.99  ? 151 THR K CA    1 
ATOM   7871 C  C     . THR C 3 151 ? 114.436 131.712 144.217 1.00 69.73  ? 151 THR K C     1 
ATOM   7872 O  O     . THR C 3 151 ? 114.798 132.040 143.085 1.00 72.14  ? 151 THR K O     1 
ATOM   7873 C  CB    . THR C 3 151 ? 111.991 131.515 143.857 1.00 71.65  ? 151 THR K CB    1 
ATOM   7874 O  OG1   . THR C 3 151 ? 112.245 132.089 142.570 1.00 73.31  ? 151 THR K OG1   1 
ATOM   7875 C  CG2   . THR C 3 151 ? 111.612 132.619 144.832 1.00 71.83  ? 151 THR K CG2   1 
ATOM   7876 N  N     . ASN C 3 152 ? 115.050 132.164 145.304 1.00 62.50  ? 152 ASN K N     1 
ATOM   7877 C  CA    . ASN C 3 152 ? 116.166 133.102 145.220 1.00 62.67  ? 152 ASN K CA    1 
ATOM   7878 C  C     . ASN C 3 152 ? 117.283 132.694 146.176 1.00 64.70  ? 152 ASN K C     1 
ATOM   7879 O  O     . ASN C 3 152 ? 117.788 133.501 146.957 1.00 68.95  ? 152 ASN K O     1 
ATOM   7880 C  CB    . ASN C 3 152 ? 115.706 134.528 145.498 1.00 63.10  ? 152 ASN K CB    1 
ATOM   7881 C  CG    . ASN C 3 152 ? 116.641 135.562 144.915 1.00 63.93  ? 152 ASN K CG    1 
ATOM   7882 O  OD1   . ASN C 3 152 ? 117.536 135.238 144.137 1.00 62.06  ? 152 ASN K OD1   1 
ATOM   7883 N  ND2   . ASN C 3 152 ? 116.442 136.819 145.291 1.00 65.28  ? 152 ASN K ND2   1 
ATOM   7884 N  N     . LEU C 3 153 ? 117.676 131.425 146.128 1.00 61.37  ? 153 LEU K N     1 
ATOM   7885 C  CA    . LEU C 3 153 ? 118.748 130.942 146.984 1.00 59.93  ? 153 LEU K CA    1 
ATOM   7886 C  C     . LEU C 3 153 ? 120.056 131.659 146.662 1.00 61.43  ? 153 LEU K C     1 
ATOM   7887 O  O     . LEU C 3 153 ? 120.216 132.278 145.609 1.00 62.19  ? 153 LEU K O     1 
ATOM   7888 C  CB    . LEU C 3 153 ? 118.923 129.436 146.822 1.00 61.24  ? 153 LEU K CB    1 
ATOM   7889 C  CG    . LEU C 3 153 ? 117.646 128.605 146.906 1.00 61.72  ? 153 LEU K CG    1 
ATOM   7890 C  CD1   . LEU C 3 153 ? 117.969 127.133 146.770 1.00 62.50  ? 153 LEU K CD1   1 
ATOM   7891 C  CD2   . LEU C 3 153 ? 116.919 128.877 148.204 1.00 63.24  ? 153 LEU K CD2   1 
ATOM   7892 N  N     . SER C 3 154 ? 121.000 131.569 147.591 1.00 63.10  ? 154 SER K N     1 
ATOM   7893 C  CA    . SER C 3 154 ? 122.267 132.276 147.495 1.00 64.05  ? 154 SER K CA    1 
ATOM   7894 C  C     . SER C 3 154 ? 123.427 131.301 147.641 1.00 63.59  ? 154 SER K C     1 
ATOM   7895 O  O     . SER C 3 154 ? 123.261 130.161 148.077 1.00 71.76  ? 154 SER K O     1 
ATOM   7896 C  CB    . SER C 3 154 ? 122.360 133.374 148.559 1.00 66.32  ? 154 SER K CB    1 
ATOM   7897 O  OG    . SER C 3 154 ? 121.259 134.261 148.469 1.00 69.99  ? 154 SER K OG    1 
ATOM   7898 N  N     . VAL C 3 155 ? 124.617 131.771 147.281 1.00 54.15  ? 155 VAL K N     1 
ATOM   7899 C  CA    . VAL C 3 155 ? 125.835 130.973 147.335 1.00 51.76  ? 155 VAL K CA    1 
ATOM   7900 C  C     . VAL C 3 155 ? 126.712 131.515 148.450 1.00 58.42  ? 155 VAL K C     1 
ATOM   7901 O  O     . VAL C 3 155 ? 126.968 132.722 148.513 1.00 62.70  ? 155 VAL K O     1 
ATOM   7902 C  CB    . VAL C 3 155 ? 126.591 130.988 145.997 1.00 56.01  ? 155 VAL K CB    1 
ATOM   7903 C  CG1   . VAL C 3 155 ? 127.832 130.125 146.090 1.00 56.08  ? 155 VAL K CG1   1 
ATOM   7904 C  CG2   . VAL C 3 155 ? 125.694 130.508 144.882 1.00 58.76  ? 155 VAL K CG2   1 
ATOM   7905 N  N     . HIS C 3 156 ? 127.170 130.626 149.326 1.00 59.08  ? 156 HIS K N     1 
ATOM   7906 C  CA    . HIS C 3 156 ? 127.991 130.988 150.469 1.00 54.79  ? 156 HIS K CA    1 
ATOM   7907 C  C     . HIS C 3 156 ? 129.207 130.071 150.519 1.00 56.91  ? 156 HIS K C     1 
ATOM   7908 O  O     . HIS C 3 156 ? 129.444 129.269 149.613 1.00 64.60  ? 156 HIS K O     1 
ATOM   7909 C  CB    . HIS C 3 156 ? 127.181 130.913 151.767 1.00 51.13  ? 156 HIS K CB    1 
ATOM   7910 C  CG    . HIS C 3 156 ? 126.045 131.883 151.826 1.00 57.21  ? 156 HIS K CG    1 
ATOM   7911 N  ND1   . HIS C 3 156 ? 126.000 133.025 151.059 1.00 62.46  ? 156 HIS K ND1   1 
ATOM   7912 C  CD2   . HIS C 3 156 ? 124.913 131.884 152.566 1.00 60.20  ? 156 HIS K CD2   1 
ATOM   7913 C  CE1   . HIS C 3 156 ? 124.888 133.687 151.321 1.00 60.63  ? 156 HIS K CE1   1 
ATOM   7914 N  NE2   . HIS C 3 156 ? 124.210 133.015 152.233 1.00 57.86  ? 156 HIS K NE2   1 
ATOM   7915 N  N     . GLU C 3 157 ? 129.990 130.196 151.586 1.00 61.83  ? 157 GLU K N     1 
ATOM   7916 C  CA    . GLU C 3 157 ? 131.220 129.439 151.745 1.00 61.41  ? 157 GLU K CA    1 
ATOM   7917 C  C     . GLU C 3 157 ? 131.271 128.798 153.123 1.00 66.92  ? 157 GLU K C     1 
ATOM   7918 O  O     . GLU C 3 157 ? 130.609 129.248 154.060 1.00 72.99  ? 157 GLU K O     1 
ATOM   7919 C  CB    . GLU C 3 157 ? 132.455 130.319 151.565 1.00 63.07  ? 157 GLU K CB    1 
ATOM   7920 C  CG    . GLU C 3 157 ? 132.575 130.955 150.202 1.00 70.03  ? 157 GLU K CG    1 
ATOM   7921 C  CD    . GLU C 3 157 ? 133.824 131.799 150.066 1.00 70.48  ? 157 GLU K CD    1 
ATOM   7922 O  OE1   . GLU C 3 157 ? 134.526 131.990 151.081 1.00 71.40  ? 157 GLU K OE1   1 
ATOM   7923 O  OE2   . GLU C 3 157 ? 134.106 132.272 148.946 1.00 68.30  ? 157 GLU K OE2   1 
ATOM   7924 N  N     . ASP C 3 158 ? 132.063 127.735 153.234 1.00 76.27  ? 158 ASP K N     1 
ATOM   7925 C  CA    . ASP C 3 158 ? 132.379 127.143 154.523 1.00 76.31  ? 158 ASP K CA    1 
ATOM   7926 C  C     . ASP C 3 158 ? 133.768 127.606 154.962 1.00 75.93  ? 158 ASP K C     1 
ATOM   7927 O  O     . ASP C 3 158 ? 134.389 128.464 154.331 1.00 79.37  ? 158 ASP K O     1 
ATOM   7928 C  CB    . ASP C 3 158 ? 132.272 125.621 154.464 1.00 77.64  ? 158 ASP K CB    1 
ATOM   7929 C  CG    . ASP C 3 158 ? 133.084 125.017 153.340 1.00 80.78  ? 158 ASP K CG    1 
ATOM   7930 O  OD1   . ASP C 3 158 ? 134.318 125.200 153.323 1.00 78.47  ? 158 ASP K OD1   1 
ATOM   7931 O  OD2   . ASP C 3 158 ? 132.486 124.334 152.484 1.00 85.12  ? 158 ASP K OD2   1 
ATOM   7932 N  N     . LYS C 3 159 ? 134.269 127.037 156.059 1.00 80.76  ? 159 LYS K N     1 
ATOM   7933 C  CA    . LYS C 3 159 ? 135.548 127.476 156.605 1.00 83.87  ? 159 LYS K CA    1 
ATOM   7934 C  C     . LYS C 3 159 ? 136.693 127.196 155.641 1.00 85.99  ? 159 LYS K C     1 
ATOM   7935 O  O     . LYS C 3 159 ? 137.646 127.979 155.556 1.00 86.59  ? 159 LYS K O     1 
ATOM   7936 C  CB    . LYS C 3 159 ? 135.803 126.794 157.948 1.00 86.09  ? 159 LYS K CB    1 
ATOM   7937 C  CG    . LYS C 3 159 ? 134.673 126.949 158.953 1.00 87.47  ? 159 LYS K CG    1 
ATOM   7938 C  CD    . LYS C 3 159 ? 134.802 125.945 160.088 1.00 85.55  ? 159 LYS K CD    1 
ATOM   7939 C  CE    . LYS C 3 159 ? 134.655 124.519 159.583 1.00 85.69  ? 159 LYS K CE    1 
ATOM   7940 N  NZ    . LYS C 3 159 ? 133.340 124.301 158.919 1.00 86.52  ? 159 LYS K NZ    1 
ATOM   7941 N  N     . ASN C 3 160 ? 136.619 126.087 154.907 1.00 81.72  ? 160 ASN K N     1 
ATOM   7942 C  CA    . ASN C 3 160 ? 137.661 125.686 153.972 1.00 76.17  ? 160 ASN K CA    1 
ATOM   7943 C  C     . ASN C 3 160 ? 137.490 126.305 152.596 1.00 76.62  ? 160 ASN K C     1 
ATOM   7944 O  O     . ASN C 3 160 ? 138.030 125.763 151.626 1.00 79.20  ? 160 ASN K O     1 
ATOM   7945 C  CB    . ASN C 3 160 ? 137.696 124.163 153.852 1.00 77.05  ? 160 ASN K CB    1 
ATOM   7946 C  CG    . ASN C 3 160 ? 137.489 123.472 155.181 1.00 79.67  ? 160 ASN K CG    1 
ATOM   7947 O  OD1   . ASN C 3 160 ? 136.558 122.686 155.345 1.00 83.24  ? 160 ASN K OD1   1 
ATOM   7948 N  ND2   . ASN C 3 160 ? 138.356 123.765 156.141 1.00 79.28  ? 160 ASN K ND2   1 
ATOM   7949 N  N     . ARG C 3 161 ? 136.768 127.419 152.511 1.00 80.20  ? 161 ARG K N     1 
ATOM   7950 C  CA    . ARG C 3 161 ? 136.411 128.100 151.263 1.00 79.36  ? 161 ARG K CA    1 
ATOM   7951 C  C     . ARG C 3 161 ? 136.070 127.107 150.152 1.00 79.59  ? 161 ARG K C     1 
ATOM   7952 O  O     . ARG C 3 161 ? 136.690 127.067 149.090 1.00 81.56  ? 161 ARG K O     1 
ATOM   7953 C  CB    . ARG C 3 161 ? 137.496 129.089 150.823 1.00 81.18  ? 161 ARG K CB    1 
ATOM   7954 C  CG    . ARG C 3 161 ? 138.930 128.592 150.817 1.00 81.95  ? 161 ARG K CG    1 
ATOM   7955 C  CD    . ARG C 3 161 ? 139.893 129.751 150.635 1.00 80.87  ? 161 ARG K CD    1 
ATOM   7956 N  NE    . ARG C 3 161 ? 139.547 130.880 151.489 1.00 82.61  ? 161 ARG K NE    1 
ATOM   7957 C  CZ    . ARG C 3 161 ? 139.929 131.010 152.752 1.00 85.71  ? 161 ARG K CZ    1 
ATOM   7958 N  NH1   . ARG C 3 161 ? 140.679 130.095 153.345 1.00 86.65  ? 161 ARG K NH1   1 
ATOM   7959 N  NH2   . ARG C 3 161 ? 139.550 132.085 153.437 1.00 84.55  ? 161 ARG K NH2   1 
ATOM   7960 N  N     . VAL C 3 162 ? 135.056 126.294 150.427 1.00 65.94  ? 162 VAL K N     1 
ATOM   7961 C  CA    . VAL C 3 162 ? 134.439 125.409 149.447 1.00 64.15  ? 162 VAL K CA    1 
ATOM   7962 C  C     . VAL C 3 162 ? 132.999 125.877 149.251 1.00 65.12  ? 162 VAL K C     1 
ATOM   7963 O  O     . VAL C 3 162 ? 132.164 125.692 150.147 1.00 65.34  ? 162 VAL K O     1 
ATOM   7964 C  CB    . VAL C 3 162 ? 134.493 123.943 149.890 1.00 64.40  ? 162 VAL K CB    1 
ATOM   7965 C  CG1   . VAL C 3 162 ? 133.695 123.073 148.938 1.00 63.39  ? 162 VAL K CG1   1 
ATOM   7966 C  CG2   . VAL C 3 162 ? 135.933 123.470 149.968 1.00 68.05  ? 162 VAL K CG2   1 
ATOM   7967 N  N     . PRO C 3 163 ? 132.661 126.486 148.118 1.00 60.94  ? 163 PRO K N     1 
ATOM   7968 C  CA    . PRO C 3 163 ? 131.331 127.084 147.971 1.00 54.21  ? 163 PRO K CA    1 
ATOM   7969 C  C     . PRO C 3 163 ? 130.223 126.046 147.981 1.00 56.09  ? 163 PRO K C     1 
ATOM   7970 O  O     . PRO C 3 163 ? 130.416 124.887 147.611 1.00 60.57  ? 163 PRO K O     1 
ATOM   7971 C  CB    . PRO C 3 163 ? 131.408 127.794 146.615 1.00 53.71  ? 163 PRO K CB    1 
ATOM   7972 C  CG    . PRO C 3 163 ? 132.856 127.913 146.317 1.00 59.98  ? 163 PRO K CG    1 
ATOM   7973 C  CD    . PRO C 3 163 ? 133.502 126.724 146.938 1.00 63.28  ? 163 PRO K CD    1 
ATOM   7974 N  N     . TYR C 3 164 ? 129.045 126.487 148.412 1.00 55.40  ? 164 TYR K N     1 
ATOM   7975 C  CA    . TYR C 3 164 ? 127.863 125.642 148.456 1.00 53.79  ? 164 TYR K CA    1 
ATOM   7976 C  C     . TYR C 3 164 ? 126.630 126.527 148.372 1.00 56.54  ? 164 TYR K C     1 
ATOM   7977 O  O     . TYR C 3 164 ? 126.690 127.731 148.626 1.00 61.16  ? 164 TYR K O     1 
ATOM   7978 C  CB    . TYR C 3 164 ? 127.829 124.786 149.724 1.00 54.71  ? 164 TYR K CB    1 
ATOM   7979 C  CG    . TYR C 3 164 ? 127.525 125.563 150.981 1.00 57.19  ? 164 TYR K CG    1 
ATOM   7980 C  CD1   . TYR C 3 164 ? 128.510 126.292 151.620 1.00 56.93  ? 164 TYR K CD1   1 
ATOM   7981 C  CD2   . TYR C 3 164 ? 126.255 125.564 151.530 1.00 57.34  ? 164 TYR K CD2   1 
ATOM   7982 C  CE1   . TYR C 3 164 ? 128.239 127.001 152.764 1.00 56.92  ? 164 TYR K CE1   1 
ATOM   7983 C  CE2   . TYR C 3 164 ? 125.975 126.272 152.675 1.00 59.56  ? 164 TYR K CE2   1 
ATOM   7984 C  CZ    . TYR C 3 164 ? 126.971 126.988 153.286 1.00 58.54  ? 164 TYR K CZ    1 
ATOM   7985 O  OH    . TYR C 3 164 ? 126.699 127.697 154.431 1.00 60.40  ? 164 TYR K OH    1 
ATOM   7986 N  N     . VAL C 3 165 ? 125.507 125.916 148.015 1.00 57.76  ? 165 VAL K N     1 
ATOM   7987 C  CA    . VAL C 3 165 ? 124.232 126.612 147.894 1.00 56.30  ? 165 VAL K CA    1 
ATOM   7988 C  C     . VAL C 3 165 ? 123.457 126.413 149.185 1.00 63.29  ? 165 VAL K C     1 
ATOM   7989 O  O     . VAL C 3 165 ? 123.251 125.275 149.625 1.00 69.04  ? 165 VAL K O     1 
ATOM   7990 C  CB    . VAL C 3 165 ? 123.431 126.102 146.686 1.00 56.98  ? 165 VAL K CB    1 
ATOM   7991 C  CG1   . VAL C 3 165 ? 122.121 126.843 146.572 1.00 57.52  ? 165 VAL K CG1   1 
ATOM   7992 C  CG2   . VAL C 3 165 ? 124.239 126.258 145.413 1.00 59.71  ? 165 VAL K CG2   1 
ATOM   7993 N  N     . LYS C 3 166 ? 123.026 127.511 149.793 1.00 65.06  ? 166 LYS K N     1 
ATOM   7994 C  CA    . LYS C 3 166 ? 122.381 127.466 151.096 1.00 59.00  ? 166 LYS K CA    1 
ATOM   7995 C  C     . LYS C 3 166 ? 120.875 127.329 150.930 1.00 59.23  ? 166 LYS K C     1 
ATOM   7996 O  O     . LYS C 3 166 ? 120.253 128.095 150.189 1.00 63.28  ? 166 LYS K O     1 
ATOM   7997 C  CB    . LYS C 3 166 ? 122.719 128.718 151.904 1.00 60.07  ? 166 LYS K CB    1 
ATOM   7998 C  CG    . LYS C 3 166 ? 121.682 129.096 152.939 1.00 62.80  ? 166 LYS K CG    1 
ATOM   7999 C  CD    . LYS C 3 166 ? 122.184 130.213 153.834 1.00 62.29  ? 166 LYS K CD    1 
ATOM   8000 C  CE    . LYS C 3 166 ? 123.361 129.759 154.679 1.00 62.53  ? 166 LYS K CE    1 
ATOM   8001 N  NZ    . LYS C 3 166 ? 123.001 128.611 155.552 1.00 64.64  ? 166 LYS K NZ    1 
ATOM   8002 N  N     . GLY C 3 167 ? 120.297 126.350 151.620 1.00 63.21  ? 167 GLY K N     1 
ATOM   8003 C  CA    . GLY C 3 167 ? 118.869 126.132 151.609 1.00 63.57  ? 167 GLY K CA    1 
ATOM   8004 C  C     . GLY C 3 167 ? 118.355 125.167 150.564 1.00 68.66  ? 167 GLY K C     1 
ATOM   8005 O  O     . GLY C 3 167 ? 117.145 124.918 150.523 1.00 72.03  ? 167 GLY K O     1 
ATOM   8006 N  N     . CYS C 3 168 ? 119.223 124.614 149.724 1.00 74.59  ? 168 CYS K N     1 
ATOM   8007 C  CA    . CYS C 3 168 ? 118.773 123.695 148.689 1.00 71.61  ? 168 CYS K CA    1 
ATOM   8008 C  C     . CYS C 3 168 ? 118.275 122.394 149.303 1.00 71.67  ? 168 CYS K C     1 
ATOM   8009 O  O     . CYS C 3 168 ? 118.798 121.925 150.317 1.00 75.22  ? 168 CYS K O     1 
ATOM   8010 C  CB    . CYS C 3 168 ? 119.904 123.411 147.705 1.00 75.20  ? 168 CYS K CB    1 
ATOM   8011 S  SG    . CYS C 3 168 ? 119.433 122.363 146.312 1.00 91.50  ? 168 CYS K SG    1 
ATOM   8012 N  N     . THR C 3 169 ? 117.253 121.811 148.683 1.00 69.43  ? 169 THR K N     1 
ATOM   8013 C  CA    . THR C 3 169 ? 116.725 120.538 149.149 1.00 71.53  ? 169 THR K CA    1 
ATOM   8014 C  C     . THR C 3 169 ? 117.669 119.406 148.765 1.00 71.28  ? 169 THR K C     1 
ATOM   8015 O  O     . THR C 3 169 ? 118.086 119.294 147.609 1.00 71.66  ? 169 THR K O     1 
ATOM   8016 C  CB    . THR C 3 169 ? 115.339 120.288 148.561 1.00 70.93  ? 169 THR K CB    1 
ATOM   8017 O  OG1   . THR C 3 169 ? 114.469 121.369 148.915 1.00 73.76  ? 169 THR K OG1   1 
ATOM   8018 C  CG2   . THR C 3 169 ? 114.763 118.990 149.095 1.00 69.36  ? 169 THR K CG2   1 
ATOM   8019 N  N     . GLU C 3 170 ? 118.004 118.566 149.738 1.00 68.65  ? 170 GLU K N     1 
ATOM   8020 C  CA    . GLU C 3 170 ? 118.876 117.417 149.528 1.00 66.99  ? 170 GLU K CA    1 
ATOM   8021 C  C     . GLU C 3 170 ? 118.194 116.205 150.144 1.00 66.67  ? 170 GLU K C     1 
ATOM   8022 O  O     . GLU C 3 170 ? 118.077 116.115 151.369 1.00 68.96  ? 170 GLU K O     1 
ATOM   8023 C  CB    . GLU C 3 170 ? 120.252 117.652 150.148 1.00 70.54  ? 170 GLU K CB    1 
ATOM   8024 C  CG    . GLU C 3 170 ? 121.378 116.893 149.469 1.00 75.15  ? 170 GLU K CG    1 
ATOM   8025 C  CD    . GLU C 3 170 ? 122.730 117.175 150.095 1.00 77.92  ? 170 GLU K CD    1 
ATOM   8026 O  OE1   . GLU C 3 170 ? 122.764 117.684 151.235 1.00 76.82  ? 170 GLU K OE1   1 
ATOM   8027 O  OE2   . GLU C 3 170 ? 123.758 116.888 149.446 1.00 75.05  ? 170 GLU K OE2   1 
ATOM   8028 N  N     . ARG C 3 171 ? 117.744 115.278 149.304 1.00 58.62  ? 171 ARG K N     1 
ATOM   8029 C  CA    . ARG C 3 171 ? 116.964 114.140 149.759 1.00 56.66  ? 171 ARG K CA    1 
ATOM   8030 C  C     . ARG C 3 171 ? 117.728 112.843 149.535 1.00 57.96  ? 171 ARG K C     1 
ATOM   8031 O  O     . ARG C 3 171 ? 118.514 112.716 148.593 1.00 63.08  ? 171 ARG K O     1 
ATOM   8032 C  CB    . ARG C 3 171 ? 115.606 114.079 149.055 1.00 51.60  ? 171 ARG K CB    1 
ATOM   8033 C  CG    . ARG C 3 171 ? 115.669 113.715 147.597 1.00 56.82  ? 171 ARG K CG    1 
ATOM   8034 C  CD    . ARG C 3 171 ? 114.285 113.410 147.060 1.00 59.80  ? 171 ARG K CD    1 
ATOM   8035 N  NE    . ARG C 3 171 ? 113.366 114.520 147.274 1.00 62.73  ? 171 ARG K NE    1 
ATOM   8036 C  CZ    . ARG C 3 171 ? 112.181 114.631 146.691 1.00 61.27  ? 171 ARG K CZ    1 
ATOM   8037 N  NH1   . ARG C 3 171 ? 111.741 113.719 145.841 1.00 59.65  ? 171 ARG K NH1   1 
ATOM   8038 N  NH2   . ARG C 3 171 ? 111.419 115.685 146.966 1.00 60.44  ? 171 ARG K NH2   1 
ATOM   8039 N  N     . PHE C 3 172 ? 117.493 111.884 150.424 1.00 53.33  ? 172 PHE K N     1 
ATOM   8040 C  CA    . PHE C 3 172 ? 118.176 110.603 150.374 1.00 51.53  ? 172 PHE K CA    1 
ATOM   8041 C  C     . PHE C 3 172 ? 117.472 109.640 149.430 1.00 52.80  ? 172 PHE K C     1 
ATOM   8042 O  O     . PHE C 3 172 ? 116.245 109.623 149.322 1.00 55.07  ? 172 PHE K O     1 
ATOM   8043 C  CB    . PHE C 3 172 ? 118.256 109.984 151.766 1.00 51.97  ? 172 PHE K CB    1 
ATOM   8044 C  CG    . PHE C 3 172 ? 119.127 110.741 152.716 1.00 56.96  ? 172 PHE K CG    1 
ATOM   8045 C  CD1   . PHE C 3 172 ? 118.624 111.802 153.439 1.00 56.96  ? 172 PHE K CD1   1 
ATOM   8046 C  CD2   . PHE C 3 172 ? 120.446 110.382 152.899 1.00 59.18  ? 172 PHE K CD2   1 
ATOM   8047 C  CE1   . PHE C 3 172 ? 119.423 112.496 154.316 1.00 54.96  ? 172 PHE K CE1   1 
ATOM   8048 C  CE2   . PHE C 3 172 ? 121.248 111.073 153.777 1.00 57.44  ? 172 PHE K CE2   1 
ATOM   8049 C  CZ    . PHE C 3 172 ? 120.736 112.130 154.485 1.00 54.96  ? 172 PHE K CZ    1 
ATOM   8050 N  N     . VAL C 3 173 ? 118.270 108.824 148.745 1.00 55.57  ? 173 VAL K N     1 
ATOM   8051 C  CA    . VAL C 3 173 ? 117.768 107.815 147.828 1.00 55.18  ? 173 VAL K CA    1 
ATOM   8052 C  C     . VAL C 3 173 ? 118.400 106.477 148.183 1.00 59.99  ? 173 VAL K C     1 
ATOM   8053 O  O     . VAL C 3 173 ? 119.480 106.408 148.771 1.00 62.52  ? 173 VAL K O     1 
ATOM   8054 C  CB    . VAL C 3 173 ? 118.047 108.171 146.354 1.00 63.33  ? 173 VAL K CB    1 
ATOM   8055 C  CG1   . VAL C 3 173 ? 117.386 109.489 145.993 1.00 64.33  ? 173 VAL K CG1   1 
ATOM   8056 C  CG2   . VAL C 3 173 ? 119.540 108.232 146.095 1.00 65.09  ? 173 VAL K CG2   1 
ATOM   8057 N  N     . CYS C 3 174 ? 117.705 105.403 147.817 1.00 62.26  ? 174 CYS K N     1 
ATOM   8058 C  CA    . CYS C 3 174 ? 118.137 104.058 148.159 1.00 59.04  ? 174 CYS K CA    1 
ATOM   8059 C  C     . CYS C 3 174 ? 118.047 103.070 147.006 1.00 64.14  ? 174 CYS K C     1 
ATOM   8060 O  O     . CYS C 3 174 ? 118.332 101.887 147.211 1.00 68.00  ? 174 CYS K O     1 
ATOM   8061 C  CB    . CYS C 3 174 ? 117.318 103.522 149.341 1.00 61.84  ? 174 CYS K CB    1 
ATOM   8062 S  SG    . CYS C 3 174 ? 117.530 104.448 150.878 1.00 78.64  ? 174 CYS K SG    1 
ATOM   8063 N  N     . SER C 3 175 ? 117.663 103.509 145.813 1.00 73.60  ? 175 SER K N     1 
ATOM   8064 C  CA    . SER C 3 175 ? 117.526 102.622 144.667 1.00 73.22  ? 175 SER K CA    1 
ATOM   8065 C  C     . SER C 3 175 ? 117.527 103.467 143.403 1.00 76.83  ? 175 SER K C     1 
ATOM   8066 O  O     . SER C 3 175 ? 117.223 104.665 143.455 1.00 83.01  ? 175 SER K O     1 
ATOM   8067 C  CB    . SER C 3 175 ? 116.239 101.786 144.760 1.00 77.20  ? 175 SER K CB    1 
ATOM   8068 O  OG    . SER C 3 175 ? 115.096 102.617 144.868 1.00 80.82  ? 175 SER K OG    1 
ATOM   8069 N  N     . PRO C 3 176 ? 117.875 102.880 142.255 1.00 66.33  ? 176 PRO K N     1 
ATOM   8070 C  CA    . PRO C 3 176 ? 117.843 103.649 141.000 1.00 69.96  ? 176 PRO K CA    1 
ATOM   8071 C  C     . PRO C 3 176 ? 116.466 104.178 140.645 1.00 70.04  ? 176 PRO K C     1 
ATOM   8072 O  O     . PRO C 3 176 ? 116.361 105.239 140.011 1.00 74.60  ? 176 PRO K O     1 
ATOM   8073 C  CB    . PRO C 3 176 ? 118.344 102.637 139.964 1.00 70.01  ? 176 PRO K CB    1 
ATOM   8074 C  CG    . PRO C 3 176 ? 119.140 101.663 140.748 1.00 68.45  ? 176 PRO K CG    1 
ATOM   8075 C  CD    . PRO C 3 176 ? 118.449 101.540 142.063 1.00 62.84  ? 176 PRO K CD    1 
ATOM   8076 N  N     . ASP C 3 177 ? 115.406 103.465 141.027 1.00 71.26  ? 177 ASP K N     1 
ATOM   8077 C  CA    . ASP C 3 177 ? 114.056 103.926 140.729 1.00 73.14  ? 177 ASP K CA    1 
ATOM   8078 C  C     . ASP C 3 177 ? 113.778 105.271 141.384 1.00 78.46  ? 177 ASP K C     1 
ATOM   8079 O  O     . ASP C 3 177 ? 113.157 106.150 140.775 1.00 85.57  ? 177 ASP K O     1 
ATOM   8080 C  CB    . ASP C 3 177 ? 113.036 102.884 141.184 1.00 78.39  ? 177 ASP K CB    1 
ATOM   8081 C  CG    . ASP C 3 177 ? 111.635 103.181 140.682 1.00 84.60  ? 177 ASP K CG    1 
ATOM   8082 O  OD1   . ASP C 3 177 ? 111.499 103.973 139.726 1.00 83.34  ? 177 ASP K OD1   1 
ATOM   8083 O  OD2   . ASP C 3 177 ? 110.670 102.623 141.245 1.00 82.87  ? 177 ASP K OD2   1 
ATOM   8084 N  N     . GLU C 3 178 ? 114.237 105.454 142.622 1.00 68.22  ? 178 GLU K N     1 
ATOM   8085 C  CA    . GLU C 3 178 ? 114.050 106.733 143.296 1.00 67.25  ? 178 GLU K CA    1 
ATOM   8086 C  C     . GLU C 3 178 ? 114.802 107.853 142.587 1.00 72.06  ? 178 GLU K C     1 
ATOM   8087 O  O     . GLU C 3 178 ? 114.298 108.978 142.486 1.00 78.79  ? 178 GLU K O     1 
ATOM   8088 C  CB    . GLU C 3 178 ? 114.489 106.624 144.752 1.00 70.62  ? 178 GLU K CB    1 
ATOM   8089 C  CG    . GLU C 3 178 ? 113.715 105.592 145.548 1.00 75.35  ? 178 GLU K CG    1 
ATOM   8090 C  CD    . GLU C 3 178 ? 114.035 105.638 147.029 1.00 78.87  ? 178 GLU K CD    1 
ATOM   8091 O  OE1   . GLU C 3 178 ? 114.614 106.648 147.482 1.00 79.26  ? 178 GLU K OE1   1 
ATOM   8092 O  OE2   . GLU C 3 178 ? 113.709 104.665 147.740 1.00 77.47  ? 178 GLU K OE2   1 
ATOM   8093 N  N     . VAL C 3 179 ? 116.009 107.571 142.090 1.00 60.45  ? 179 VAL K N     1 
ATOM   8094 C  CA    . VAL C 3 179 ? 116.770 108.591 141.376 1.00 59.71  ? 179 VAL K CA    1 
ATOM   8095 C  C     . VAL C 3 179 ? 116.064 108.982 140.084 1.00 67.30  ? 179 VAL K C     1 
ATOM   8096 O  O     . VAL C 3 179 ? 115.968 110.169 139.745 1.00 72.00  ? 179 VAL K O     1 
ATOM   8097 C  CB    . VAL C 3 179 ? 118.205 108.108 141.111 1.00 58.58  ? 179 VAL K CB    1 
ATOM   8098 C  CG1   . VAL C 3 179 ? 119.023 109.213 140.482 1.00 62.13  ? 179 VAL K CG1   1 
ATOM   8099 C  CG2   . VAL C 3 179 ? 118.848 107.640 142.397 1.00 63.22  ? 179 VAL K CG2   1 
ATOM   8100 N  N     . MET C 3 180 ? 115.558 107.999 139.339 1.00 68.54  ? 180 MET K N     1 
ATOM   8101 C  CA    . MET C 3 180 ? 114.818 108.328 138.125 1.00 64.91  ? 180 MET K CA    1 
ATOM   8102 C  C     . MET C 3 180 ? 113.555 109.121 138.445 1.00 66.36  ? 180 MET K C     1 
ATOM   8103 O  O     . MET C 3 180 ? 113.202 110.066 137.725 1.00 73.06  ? 180 MET K O     1 
ATOM   8104 C  CB    . MET C 3 180 ? 114.481 107.055 137.354 1.00 67.72  ? 180 MET K CB    1 
ATOM   8105 C  CG    . MET C 3 180 ? 115.698 106.233 136.967 1.00 68.03  ? 180 MET K CG    1 
ATOM   8106 S  SD    . MET C 3 180 ? 117.108 107.232 136.459 1.00 75.24  ? 180 MET K SD    1 
ATOM   8107 C  CE    . MET C 3 180 ? 116.516 107.920 134.918 1.00 70.80  ? 180 MET K CE    1 
ATOM   8108 N  N     . ASP C 3 181 ? 112.863 108.757 139.527 1.00 67.80  ? 181 ASP K N     1 
ATOM   8109 C  CA    . ASP C 3 181 ? 111.655 109.477 139.910 1.00 69.95  ? 181 ASP K CA    1 
ATOM   8110 C  C     . ASP C 3 181 ? 111.962 110.925 140.269 1.00 73.01  ? 181 ASP K C     1 
ATOM   8111 O  O     . ASP C 3 181 ? 111.226 111.839 139.873 1.00 77.86  ? 181 ASP K O     1 
ATOM   8112 C  CB    . ASP C 3 181 ? 110.973 108.769 141.078 1.00 74.83  ? 181 ASP K CB    1 
ATOM   8113 C  CG    . ASP C 3 181 ? 109.515 109.158 141.224 1.00 79.17  ? 181 ASP K CG    1 
ATOM   8114 O  OD1   . ASP C 3 181 ? 109.015 109.925 140.375 1.00 78.12  ? 181 ASP K OD1   1 
ATOM   8115 O  OD2   . ASP C 3 181 ? 108.869 108.698 142.189 1.00 78.13  ? 181 ASP K OD2   1 
ATOM   8116 N  N     . THR C 3 182 ? 113.041 111.158 141.020 1.00 62.31  ? 182 THR K N     1 
ATOM   8117 C  CA    . THR C 3 182 ? 113.375 112.534 141.369 1.00 66.16  ? 182 THR K CA    1 
ATOM   8118 C  C     . THR C 3 182 ? 113.833 113.316 140.147 1.00 70.11  ? 182 THR K C     1 
ATOM   8119 O  O     . THR C 3 182 ? 113.567 114.519 140.054 1.00 74.00  ? 182 THR K O     1 
ATOM   8120 C  CB    . THR C 3 182 ? 114.426 112.582 142.484 1.00 65.44  ? 182 THR K CB    1 
ATOM   8121 O  OG1   . THR C 3 182 ? 114.506 113.914 143.005 1.00 73.44  ? 182 THR K OG1   1 
ATOM   8122 C  CG2   . THR C 3 182 ? 115.788 112.185 141.986 1.00 65.26  ? 182 THR K CG2   1 
ATOM   8123 N  N     . ILE C 3 183 ? 114.482 112.656 139.186 1.00 65.31  ? 183 ILE K N     1 
ATOM   8124 C  CA    . ILE C 3 183 ? 114.853 113.345 137.954 1.00 63.34  ? 183 ILE K CA    1 
ATOM   8125 C  C     . ILE C 3 183 ? 113.606 113.781 137.196 1.00 66.72  ? 183 ILE K C     1 
ATOM   8126 O  O     . ILE C 3 183 ? 113.534 114.906 136.684 1.00 75.82  ? 183 ILE K O     1 
ATOM   8127 C  CB    . ILE C 3 183 ? 115.763 112.449 137.094 1.00 67.82  ? 183 ILE K CB    1 
ATOM   8128 C  CG1   . ILE C 3 183 ? 117.223 112.632 137.503 1.00 67.68  ? 183 ILE K CG1   1 
ATOM   8129 C  CG2   . ILE C 3 183 ? 115.584 112.749 135.619 1.00 71.16  ? 183 ILE K CG2   1 
ATOM   8130 C  CD1   . ILE C 3 183 ? 117.882 113.850 136.895 1.00 67.78  ? 183 ILE K CD1   1 
ATOM   8131 N  N     . ASP C 3 184 ? 112.604 112.902 137.113 1.00 67.41  ? 184 ASP K N     1 
ATOM   8132 C  CA    . ASP C 3 184 ? 111.361 113.267 136.435 1.00 68.23  ? 184 ASP K CA    1 
ATOM   8133 C  C     . ASP C 3 184 ? 110.649 114.409 137.151 1.00 69.35  ? 184 ASP K C     1 
ATOM   8134 O  O     . ASP C 3 184 ? 110.166 115.354 136.510 1.00 72.16  ? 184 ASP K O     1 
ATOM   8135 C  CB    . ASP C 3 184 ? 110.445 112.052 136.330 1.00 69.81  ? 184 ASP K CB    1 
ATOM   8136 C  CG    . ASP C 3 184 ? 110.923 111.054 135.299 1.00 77.59  ? 184 ASP K CG    1 
ATOM   8137 O  OD1   . ASP C 3 184 ? 111.941 111.332 134.632 1.00 77.89  ? 184 ASP K OD1   1 
ATOM   8138 O  OD2   . ASP C 3 184 ? 110.282 109.991 135.154 1.00 76.65  ? 184 ASP K OD2   1 
ATOM   8139 N  N     . GLU C 3 185 ? 110.582 114.346 138.480 1.00 68.49  ? 185 GLU K N     1 
ATOM   8140 C  CA    . GLU C 3 185 ? 109.939 115.416 139.233 1.00 65.29  ? 185 GLU K CA    1 
ATOM   8141 C  C     . GLU C 3 185 ? 110.656 116.740 139.022 1.00 66.64  ? 185 GLU K C     1 
ATOM   8142 O  O     . GLU C 3 185 ? 110.012 117.787 138.887 1.00 71.65  ? 185 GLU K O     1 
ATOM   8143 C  CB    . GLU C 3 185 ? 109.892 115.061 140.716 1.00 68.55  ? 185 GLU K CB    1 
ATOM   8144 C  CG    . GLU C 3 185 ? 109.131 116.058 141.558 1.00 70.49  ? 185 GLU K CG    1 
ATOM   8145 C  CD    . GLU C 3 185 ? 108.892 115.565 142.968 1.00 78.23  ? 185 GLU K CD    1 
ATOM   8146 O  OE1   . GLU C 3 185 ? 109.061 114.351 143.210 1.00 79.32  ? 185 GLU K OE1   1 
ATOM   8147 O  OE2   . GLU C 3 185 ? 108.535 116.390 143.834 1.00 76.83  ? 185 GLU K OE2   1 
ATOM   8148 N  N     . GLY C 3 186 ? 111.987 116.718 138.993 1.00 67.34  ? 186 GLY K N     1 
ATOM   8149 C  CA    . GLY C 3 186 ? 112.729 117.942 138.749 1.00 71.57  ? 186 GLY K CA    1 
ATOM   8150 C  C     . GLY C 3 186 ? 112.513 118.492 137.352 1.00 71.57  ? 186 GLY K C     1 
ATOM   8151 O  O     . GLY C 3 186 ? 112.345 119.701 137.172 1.00 73.28  ? 186 GLY K O     1 
ATOM   8152 N  N     . LYS C 3 187 ? 112.515 117.617 136.344 1.00 64.89  ? 187 LYS K N     1 
ATOM   8153 C  CA    . LYS C 3 187 ? 112.286 118.068 134.978 1.00 62.62  ? 187 LYS K CA    1 
ATOM   8154 C  C     . LYS C 3 187 ? 110.874 118.591 134.773 1.00 59.13  ? 187 LYS K C     1 
ATOM   8155 O  O     . LYS C 3 187 ? 110.642 119.361 133.838 1.00 59.55  ? 187 LYS K O     1 
ATOM   8156 C  CB    . LYS C 3 187 ? 112.564 116.940 133.989 1.00 62.00  ? 187 LYS K CB    1 
ATOM   8157 C  CG    . LYS C 3 187 ? 114.018 116.816 133.591 1.00 63.98  ? 187 LYS K CG    1 
ATOM   8158 C  CD    . LYS C 3 187 ? 114.230 115.641 132.655 1.00 66.53  ? 187 LYS K CD    1 
ATOM   8159 C  CE    . LYS C 3 187 ? 113.277 115.697 131.474 1.00 66.64  ? 187 LYS K CE    1 
ATOM   8160 N  NZ    . LYS C 3 187 ? 113.245 114.409 130.728 1.00 67.31  ? 187 LYS K NZ    1 
ATOM   8161 N  N     . SER C 3 188 ? 109.927 118.185 135.616 1.00 61.86  ? 188 SER K N     1 
ATOM   8162 C  CA    . SER C 3 188 ? 108.571 118.704 135.490 1.00 60.80  ? 188 SER K CA    1 
ATOM   8163 C  C     . SER C 3 188 ? 108.491 120.210 135.710 1.00 60.97  ? 188 SER K C     1 
ATOM   8164 O  O     . SER C 3 188 ? 107.557 120.843 135.211 1.00 65.56  ? 188 SER K O     1 
ATOM   8165 C  CB    . SER C 3 188 ? 107.646 117.993 136.475 1.00 62.05  ? 188 SER K CB    1 
ATOM   8166 O  OG    . SER C 3 188 ? 106.336 118.525 136.416 1.00 63.17  ? 188 SER K OG    1 
ATOM   8167 N  N     . ASN C 3 189 ? 109.441 120.802 136.439 1.00 59.12  ? 189 ASN K N     1 
ATOM   8168 C  CA    . ASN C 3 189 ? 109.365 122.210 136.814 1.00 57.01  ? 189 ASN K CA    1 
ATOM   8169 C  C     . ASN C 3 189 ? 110.466 123.054 136.183 1.00 60.60  ? 189 ASN K C     1 
ATOM   8170 O  O     . ASN C 3 189 ? 110.718 124.171 136.640 1.00 63.11  ? 189 ASN K O     1 
ATOM   8171 C  CB    . ASN C 3 189 ? 109.409 122.362 138.333 1.00 55.48  ? 189 ASN K CB    1 
ATOM   8172 C  CG    . ASN C 3 189 ? 108.244 121.698 139.014 1.00 60.39  ? 189 ASN K CG    1 
ATOM   8173 O  OD1   . ASN C 3 189 ? 107.168 121.562 138.436 1.00 65.97  ? 189 ASN K OD1   1 
ATOM   8174 N  ND2   . ASN C 3 189 ? 108.448 121.277 140.253 1.00 60.79  ? 189 ASN K ND2   1 
ATOM   8175 N  N     . ARG C 3 190 ? 111.130 122.553 135.151 1.00 64.20  ? 190 ARG K N     1 
ATOM   8176 C  CA    . ARG C 3 190 ? 112.143 123.338 134.465 1.00 59.74  ? 190 ARG K CA    1 
ATOM   8177 C  C     . ARG C 3 190 ? 111.498 124.234 133.414 1.00 66.14  ? 190 ARG K C     1 
ATOM   8178 O  O     . ARG C 3 190 ? 110.582 123.826 132.697 1.00 71.64  ? 190 ARG K O     1 
ATOM   8179 C  CB    . ARG C 3 190 ? 113.178 122.425 133.813 1.00 57.29  ? 190 ARG K CB    1 
ATOM   8180 C  CG    . ARG C 3 190 ? 114.405 123.150 133.320 1.00 61.48  ? 190 ARG K CG    1 
ATOM   8181 C  CD    . ARG C 3 190 ? 115.364 122.210 132.626 1.00 62.33  ? 190 ARG K CD    1 
ATOM   8182 N  NE    . ARG C 3 190 ? 116.520 122.926 132.102 1.00 67.44  ? 190 ARG K NE    1 
ATOM   8183 C  CZ    . ARG C 3 190 ? 117.474 122.374 131.367 1.00 68.07  ? 190 ARG K CZ    1 
ATOM   8184 N  NH1   . ARG C 3 190 ? 117.445 121.091 131.047 1.00 67.30  ? 190 ARG K NH1   1 
ATOM   8185 N  NH2   . ARG C 3 190 ? 118.481 123.129 130.940 1.00 66.43  ? 190 ARG K NH2   1 
ATOM   8186 N  N     . HIS C 3 191 ? 111.985 125.469 133.332 1.00 62.99  ? 191 HIS K N     1 
ATOM   8187 C  CA    . HIS C 3 191 ? 111.455 126.447 132.387 1.00 61.60  ? 191 HIS K CA    1 
ATOM   8188 C  C     . HIS C 3 191 ? 111.782 125.989 130.973 1.00 64.03  ? 191 HIS K C     1 
ATOM   8189 O  O     . HIS C 3 191 ? 112.955 125.855 130.613 1.00 67.03  ? 191 HIS K O     1 
ATOM   8190 C  CB    . HIS C 3 191 ? 112.038 127.828 132.664 1.00 61.00  ? 191 HIS K CB    1 
ATOM   8191 C  CG    . HIS C 3 191 ? 111.310 128.591 133.725 1.00 62.97  ? 191 HIS K CG    1 
ATOM   8192 N  ND1   . HIS C 3 191 ? 111.421 128.293 135.065 1.00 63.34  ? 191 HIS K ND1   1 
ATOM   8193 C  CD2   . HIS C 3 191 ? 110.466 129.646 133.644 1.00 62.23  ? 191 HIS K CD2   1 
ATOM   8194 C  CE1   . HIS C 3 191 ? 110.673 129.128 135.763 1.00 65.29  ? 191 HIS K CE1   1 
ATOM   8195 N  NE2   . HIS C 3 191 ? 110.084 129.960 134.924 1.00 64.19  ? 191 HIS K NE2   1 
ATOM   8196 N  N     . VAL C 3 192 ? 110.750 125.746 130.171 1.00 60.51  ? 192 VAL K N     1 
ATOM   8197 C  CA    . VAL C 3 192 ? 110.903 125.234 128.816 1.00 57.24  ? 192 VAL K CA    1 
ATOM   8198 C  C     . VAL C 3 192 ? 110.085 126.102 127.873 1.00 62.01  ? 192 VAL K C     1 
ATOM   8199 O  O     . VAL C 3 192 ? 108.919 126.397 128.150 1.00 66.51  ? 192 VAL K O     1 
ATOM   8200 C  CB    . VAL C 3 192 ? 110.454 123.766 128.695 1.00 30.00  ? 192 VAL K CB    1 
ATOM   8201 C  CG1   . VAL C 3 192 ? 110.513 123.308 127.246 1.00 30.00  ? 192 VAL K CG1   1 
ATOM   8202 C  CG2   . VAL C 3 192 ? 111.310 122.872 129.579 1.00 30.00  ? 192 VAL K CG2   1 
ATOM   8203 N  N     . ALA C 3 193 ? 110.694 126.507 126.763 1.00 74.29  ? 193 ALA K N     1 
ATOM   8204 C  CA    . ALA C 3 193 ? 109.991 127.298 125.769 1.00 72.55  ? 193 ALA K CA    1 
ATOM   8205 C  C     . ALA C 3 193 ? 109.037 126.417 124.966 1.00 75.32  ? 193 ALA K C     1 
ATOM   8206 O  O     . ALA C 3 193 ? 109.112 125.186 124.987 1.00 75.47  ? 193 ALA K O     1 
ATOM   8207 C  CB    . ALA C 3 193 ? 110.981 127.996 124.839 1.00 73.28  ? 193 ALA K CB    1 
ATOM   8208 N  N     . VAL C 3 194 ? 108.127 127.068 124.252 1.00 84.08  ? 194 VAL K N     1 
ATOM   8209 C  CA    . VAL C 3 194 ? 107.123 126.366 123.462 1.00 85.39  ? 194 VAL K CA    1 
ATOM   8210 C  C     . VAL C 3 194 ? 107.771 125.597 122.318 1.00 83.48  ? 194 VAL K C     1 
ATOM   8211 O  O     . VAL C 3 194 ? 107.217 124.614 121.829 1.00 84.42  ? 194 VAL K O     1 
ATOM   8212 C  CB    . VAL C 3 194 ? 106.064 127.343 122.923 1.00 88.08  ? 194 VAL K CB    1 
ATOM   8213 C  CG1   . VAL C 3 194 ? 105.532 128.221 124.045 1.00 83.45  ? 194 VAL K CG1   1 
ATOM   8214 C  CG2   . VAL C 3 194 ? 106.647 128.193 121.805 1.00 85.58  ? 194 VAL K CG2   1 
ATOM   8215 N  N     . GLU C 3 199 ? 110.729 123.056 119.509 1.00 108.56 ? 199 GLU K N     1 
ATOM   8216 C  CA    . GLU C 3 199 ? 109.989 122.075 120.294 1.00 110.38 ? 199 GLU K CA    1 
ATOM   8217 C  C     . GLU C 3 199 ? 110.794 121.631 121.511 1.00 110.21 ? 199 GLU K C     1 
ATOM   8218 O  O     . GLU C 3 199 ? 111.826 120.974 121.376 1.00 110.41 ? 199 GLU K O     1 
ATOM   8219 C  CB    . GLU C 3 199 ? 109.623 120.866 119.432 1.00 109.20 ? 199 GLU K CB    1 
ATOM   8220 C  CG    . GLU C 3 199 ? 108.824 119.802 120.162 1.00 109.14 ? 199 GLU K CG    1 
ATOM   8221 C  CD    . GLU C 3 199 ? 108.354 118.694 119.240 1.00 111.54 ? 199 GLU K CD    1 
ATOM   8222 O  OE1   . GLU C 3 199 ? 108.545 118.820 118.012 1.00 112.01 ? 199 GLU K OE1   1 
ATOM   8223 O  OE2   . GLU C 3 199 ? 107.793 117.697 119.742 1.00 111.34 ? 199 GLU K OE2   1 
ATOM   8224 N  N     . HIS C 3 200 ? 110.309 122.000 122.697 1.00 105.30 ? 200 HIS K N     1 
ATOM   8225 C  CA    . HIS C 3 200 ? 110.947 121.670 123.971 1.00 105.67 ? 200 HIS K CA    1 
ATOM   8226 C  C     . HIS C 3 200 ? 112.378 122.218 124.023 1.00 104.58 ? 200 HIS K C     1 
ATOM   8227 O  O     . HIS C 3 200 ? 113.365 121.484 124.093 1.00 105.40 ? 200 HIS K O     1 
ATOM   8228 C  CB    . HIS C 3 200 ? 110.916 120.158 124.221 1.00 106.31 ? 200 HIS K CB    1 
ATOM   8229 C  CG    . HIS C 3 200 ? 109.534 119.593 124.324 1.00 109.46 ? 200 HIS K CG    1 
ATOM   8230 N  ND1   . HIS C 3 200 ? 108.431 120.371 124.604 1.00 111.60 ? 200 HIS K ND1   1 
ATOM   8231 C  CD2   . HIS C 3 200 ? 109.075 118.326 124.188 1.00 108.17 ? 200 HIS K CD2   1 
ATOM   8232 C  CE1   . HIS C 3 200 ? 107.353 119.609 124.633 1.00 108.79 ? 200 HIS K CE1   1 
ATOM   8233 N  NE2   . HIS C 3 200 ? 107.716 118.364 124.384 1.00 108.99 ? 200 HIS K NE2   1 
ATOM   8234 N  N     . SER C 3 201 ? 112.455 123.544 123.985 1.00 79.44  ? 201 SER K N     1 
ATOM   8235 C  CA    . SER C 3 201 ? 113.715 124.267 124.087 1.00 78.76  ? 201 SER K CA    1 
ATOM   8236 C  C     . SER C 3 201 ? 113.905 124.758 125.515 1.00 81.66  ? 201 SER K C     1 
ATOM   8237 O  O     . SER C 3 201 ? 113.002 125.376 126.088 1.00 85.14  ? 201 SER K O     1 
ATOM   8238 C  CB    . SER C 3 201 ? 113.747 125.446 123.116 1.00 80.33  ? 201 SER K CB    1 
ATOM   8239 O  OG    . SER C 3 201 ? 114.938 126.196 123.268 1.00 82.79  ? 201 SER K OG    1 
ATOM   8240 N  N     . SER C 3 202 ? 115.074 124.481 126.082 1.00 66.18  ? 202 SER K N     1 
ATOM   8241 C  CA    . SER C 3 202 ? 115.365 124.871 127.454 1.00 58.03  ? 202 SER K CA    1 
ATOM   8242 C  C     . SER C 3 202 ? 115.880 126.301 127.507 1.00 61.79  ? 202 SER K C     1 
ATOM   8243 O  O     . SER C 3 202 ? 116.644 126.735 126.641 1.00 64.97  ? 202 SER K O     1 
ATOM   8244 C  CB    . SER C 3 202 ? 116.390 123.922 128.068 1.00 61.72  ? 202 SER K CB    1 
ATOM   8245 O  OG    . SER C 3 202 ? 117.562 123.859 127.274 1.00 68.83  ? 202 SER K OG    1 
ATOM   8246 N  N     . ARG C 3 203 ? 115.451 127.038 128.533 1.00 62.92  ? 203 ARG K N     1 
ATOM   8247 C  CA    . ARG C 3 203 ? 115.825 128.437 128.702 1.00 59.28  ? 203 ARG K CA    1 
ATOM   8248 C  C     . ARG C 3 203 ? 116.504 128.690 130.040 1.00 59.15  ? 203 ARG K C     1 
ATOM   8249 O  O     . ARG C 3 203 ? 116.606 129.839 130.473 1.00 64.60  ? 203 ARG K O     1 
ATOM   8250 C  CB    . ARG C 3 203 ? 114.601 129.339 128.555 1.00 60.56  ? 203 ARG K CB    1 
ATOM   8251 C  CG    . ARG C 3 203 ? 113.756 129.039 127.336 1.00 64.41  ? 203 ARG K CG    1 
ATOM   8252 C  CD    . ARG C 3 203 ? 114.491 129.381 126.055 1.00 64.82  ? 203 ARG K CD    1 
ATOM   8253 N  NE    . ARG C 3 203 ? 114.591 130.817 125.837 1.00 66.12  ? 203 ARG K NE    1 
ATOM   8254 C  CZ    . ARG C 3 203 ? 115.393 131.381 124.947 1.00 69.52  ? 203 ARG K CZ    1 
ATOM   8255 N  NH1   . ARG C 3 203 ? 116.189 130.658 124.179 1.00 69.59  ? 203 ARG K NH1   1 
ATOM   8256 N  NH2   . ARG C 3 203 ? 115.397 132.705 124.824 1.00 68.59  ? 203 ARG K NH2   1 
ATOM   8257 N  N     . SER C 3 204 ? 116.964 127.636 130.706 1.00 58.23  ? 204 SER K N     1 
ATOM   8258 C  CA    . SER C 3 204 ? 117.664 127.762 131.972 1.00 51.38  ? 204 SER K CA    1 
ATOM   8259 C  C     . SER C 3 204 ? 118.603 126.579 132.126 1.00 52.95  ? 204 SER K C     1 
ATOM   8260 O  O     . SER C 3 204 ? 118.326 125.481 131.638 1.00 61.30  ? 204 SER K O     1 
ATOM   8261 C  CB    . SER C 3 204 ? 116.694 127.819 133.152 1.00 54.89  ? 204 SER K CB    1 
ATOM   8262 O  OG    . SER C 3 204 ? 115.907 126.644 133.212 1.00 61.86  ? 204 SER K OG    1 
ATOM   8263 N  N     . HIS C 3 205 ? 119.716 126.811 132.807 1.00 47.81  ? 205 HIS K N     1 
ATOM   8264 C  CA    . HIS C 3 205 ? 120.677 125.752 133.061 1.00 45.62  ? 205 HIS K CA    1 
ATOM   8265 C  C     . HIS C 3 205 ? 120.216 124.884 134.223 1.00 50.72  ? 205 HIS K C     1 
ATOM   8266 O  O     . HIS C 3 205 ? 119.561 125.354 135.153 1.00 59.11  ? 205 HIS K O     1 
ATOM   8267 C  CB    . HIS C 3 205 ? 122.052 126.346 133.351 1.00 48.05  ? 205 HIS K CB    1 
ATOM   8268 C  CG    . HIS C 3 205 ? 122.552 127.259 132.278 1.00 47.73  ? 205 HIS K CG    1 
ATOM   8269 N  ND1   . HIS C 3 205 ? 122.095 127.204 130.981 1.00 61.48  ? 205 HIS K ND1   1 
ATOM   8270 C  CD2   . HIS C 3 205 ? 123.468 128.254 132.310 1.00 48.53  ? 205 HIS K CD2   1 
ATOM   8271 C  CE1   . HIS C 3 205 ? 122.710 128.123 130.259 1.00 56.66  ? 205 HIS K CE1   1 
ATOM   8272 N  NE2   . HIS C 3 205 ? 123.547 128.775 131.043 1.00 48.54  ? 205 HIS K NE2   1 
ATOM   8273 N  N     . SER C 3 206 ? 120.563 123.603 134.159 1.00 51.39  ? 206 SER K N     1 
ATOM   8274 C  CA    . SER C 3 206 ? 120.118 122.617 135.132 1.00 47.55  ? 206 SER K CA    1 
ATOM   8275 C  C     . SER C 3 206 ? 121.317 121.849 135.658 1.00 50.34  ? 206 SER K C     1 
ATOM   8276 O  O     . SER C 3 206 ? 122.163 121.406 134.876 1.00 60.45  ? 206 SER K O     1 
ATOM   8277 C  CB    . SER C 3 206 ? 119.108 121.658 134.505 1.00 56.51  ? 206 SER K CB    1 
ATOM   8278 O  OG    . SER C 3 206 ? 118.442 120.904 135.496 1.00 64.78  ? 206 SER K OG    1 
ATOM   8279 N  N     . ILE C 3 207 ? 121.386 121.683 136.976 1.00 46.73  ? 207 ILE K N     1 
ATOM   8280 C  CA    . ILE C 3 207 ? 122.514 121.040 137.639 1.00 47.27  ? 207 ILE K CA    1 
ATOM   8281 C  C     . ILE C 3 207 ? 121.990 119.921 138.530 1.00 45.08  ? 207 ILE K C     1 
ATOM   8282 O  O     . ILE C 3 207 ? 121.010 120.109 139.257 1.00 50.89  ? 207 ILE K O     1 
ATOM   8283 C  CB    . ILE C 3 207 ? 123.341 122.047 138.459 1.00 43.35  ? 207 ILE K CB    1 
ATOM   8284 C  CG1   . ILE C 3 207 ? 123.682 123.265 137.604 1.00 44.98  ? 207 ILE K CG1   1 
ATOM   8285 C  CG2   . ILE C 3 207 ? 124.604 121.404 138.973 1.00 46.29  ? 207 ILE K CG2   1 
ATOM   8286 C  CD1   . ILE C 3 207 ? 124.574 124.253 138.293 1.00 46.11  ? 207 ILE K CD1   1 
ATOM   8287 N  N     . PHE C 3 208 ? 122.640 118.761 138.467 1.00 46.89  ? 208 PHE K N     1 
ATOM   8288 C  CA    . PHE C 3 208 ? 122.262 117.582 139.235 1.00 44.90  ? 208 PHE K CA    1 
ATOM   8289 C  C     . PHE C 3 208 ? 123.450 117.113 140.059 1.00 48.68  ? 208 PHE K C     1 
ATOM   8290 O  O     . PHE C 3 208 ? 124.534 116.885 139.514 1.00 56.46  ? 208 PHE K O     1 
ATOM   8291 C  CB    . PHE C 3 208 ? 121.790 116.468 138.302 1.00 47.77  ? 208 PHE K CB    1 
ATOM   8292 C  CG    . PHE C 3 208 ? 121.052 115.367 138.992 1.00 46.16  ? 208 PHE K CG    1 
ATOM   8293 C  CD1   . PHE C 3 208 ? 119.856 115.615 139.634 1.00 51.72  ? 208 PHE K CD1   1 
ATOM   8294 C  CD2   . PHE C 3 208 ? 121.537 114.078 138.977 1.00 46.07  ? 208 PHE K CD2   1 
ATOM   8295 C  CE1   . PHE C 3 208 ? 119.172 114.603 140.259 1.00 53.53  ? 208 PHE K CE1   1 
ATOM   8296 C  CE2   . PHE C 3 208 ? 120.855 113.066 139.602 1.00 51.98  ? 208 PHE K CE2   1 
ATOM   8297 C  CZ    . PHE C 3 208 ? 119.673 113.328 140.242 1.00 51.92  ? 208 PHE K CZ    1 
ATOM   8298 N  N     . LEU C 3 209 ? 123.247 116.964 141.364 1.00 44.40  ? 209 LEU K N     1 
ATOM   8299 C  CA    . LEU C 3 209 ? 124.298 116.570 142.292 1.00 40.52  ? 209 LEU K CA    1 
ATOM   8300 C  C     . LEU C 3 209 ? 123.977 115.198 142.867 1.00 48.63  ? 209 LEU K C     1 
ATOM   8301 O  O     . LEU C 3 209 ? 122.870 114.975 143.364 1.00 56.60  ? 209 LEU K O     1 
ATOM   8302 C  CB    . LEU C 3 209 ? 124.442 117.594 143.418 1.00 42.81  ? 209 LEU K CB    1 
ATOM   8303 C  CG    . LEU C 3 209 ? 125.552 117.388 144.444 1.00 51.91  ? 209 LEU K CG    1 
ATOM   8304 C  CD1   . LEU C 3 209 ? 126.146 118.719 144.818 1.00 50.65  ? 209 LEU K CD1   1 
ATOM   8305 C  CD2   . LEU C 3 209 ? 125.030 116.682 145.687 1.00 60.53  ? 209 LEU K CD2   1 
ATOM   8306 N  N     . ILE C 3 210 ? 124.940 114.286 142.793 1.00 47.68  ? 210 ILE K N     1 
ATOM   8307 C  CA    . ILE C 3 210 ? 124.827 112.954 143.376 1.00 44.97  ? 210 ILE K CA    1 
ATOM   8308 C  C     . ILE C 3 210 ? 125.990 112.809 144.346 1.00 48.09  ? 210 ILE K C     1 
ATOM   8309 O  O     . ILE C 3 210 ? 127.146 112.677 143.928 1.00 59.20  ? 210 ILE K O     1 
ATOM   8310 C  CB    . ILE C 3 210 ? 124.844 111.846 142.320 1.00 46.67  ? 210 ILE K CB    1 
ATOM   8311 C  CG1   . ILE C 3 210 ? 123.822 112.128 141.227 1.00 51.04  ? 210 ILE K CG1   1 
ATOM   8312 C  CG2   . ILE C 3 210 ? 124.549 110.507 142.957 1.00 52.47  ? 210 ILE K CG2   1 
ATOM   8313 C  CD1   . ILE C 3 210 ? 123.740 111.039 140.190 1.00 54.65  ? 210 ILE K CD1   1 
ATOM   8314 N  N     . ASN C 3 211 ? 125.694 112.828 145.640 1.00 51.35  ? 211 ASN K N     1 
ATOM   8315 C  CA    . ASN C 3 211 ? 126.711 112.799 146.682 1.00 51.72  ? 211 ASN K CA    1 
ATOM   8316 C  C     . ASN C 3 211 ? 126.804 111.393 147.259 1.00 61.35  ? 211 ASN K C     1 
ATOM   8317 O  O     . ASN C 3 211 ? 125.859 110.915 147.894 1.00 69.41  ? 211 ASN K O     1 
ATOM   8318 C  CB    . ASN C 3 211 ? 126.377 113.806 147.778 1.00 49.12  ? 211 ASN K CB    1 
ATOM   8319 C  CG    . ASN C 3 211 ? 127.568 114.151 148.630 1.00 61.78  ? 211 ASN K CG    1 
ATOM   8320 O  OD1   . ASN C 3 211 ? 128.503 113.365 148.758 1.00 63.77  ? 211 ASN K OD1   1 
ATOM   8321 N  ND2   . ASN C 3 211 ? 127.539 115.332 149.231 1.00 61.80  ? 211 ASN K ND2   1 
ATOM   8322 N  N     . VAL C 3 212 ? 127.941 110.740 147.050 1.00 52.19  ? 212 VAL K N     1 
ATOM   8323 C  CA    . VAL C 3 212 ? 128.174 109.382 147.521 1.00 46.09  ? 212 VAL K CA    1 
ATOM   8324 C  C     . VAL C 3 212 ? 129.211 109.451 148.629 1.00 56.36  ? 212 VAL K C     1 
ATOM   8325 O  O     . VAL C 3 212 ? 130.392 109.710 148.371 1.00 64.31  ? 212 VAL K O     1 
ATOM   8326 C  CB    . VAL C 3 212 ? 128.635 108.455 146.392 1.00 50.09  ? 212 VAL K CB    1 
ATOM   8327 C  CG1   . VAL C 3 212 ? 128.943 107.081 146.938 1.00 55.50  ? 212 VAL K CG1   1 
ATOM   8328 C  CG2   . VAL C 3 212 ? 127.572 108.371 145.322 1.00 58.43  ? 212 VAL K CG2   1 
ATOM   8329 N  N     . LYS C 3 213 ? 128.777 109.210 149.862 1.00 65.69  ? 213 LYS K N     1 
ATOM   8330 C  CA    . LYS C 3 213 ? 129.654 109.219 151.023 1.00 63.35  ? 213 LYS K CA    1 
ATOM   8331 C  C     . LYS C 3 213 ? 129.684 107.830 151.638 1.00 66.01  ? 213 LYS K C     1 
ATOM   8332 O  O     . LYS C 3 213 ? 128.632 107.239 151.895 1.00 70.18  ? 213 LYS K O     1 
ATOM   8333 C  CB    . LYS C 3 213 ? 129.195 110.249 152.054 1.00 63.40  ? 213 LYS K CB    1 
ATOM   8334 C  CG    . LYS C 3 213 ? 127.698 110.391 152.170 1.00 67.77  ? 213 LYS K CG    1 
ATOM   8335 C  CD    . LYS C 3 213 ? 127.336 111.540 153.090 1.00 70.88  ? 213 LYS K CD    1 
ATOM   8336 C  CE    . LYS C 3 213 ? 127.802 112.867 152.527 1.00 69.07  ? 213 LYS K CE    1 
ATOM   8337 N  NZ    . LYS C 3 213 ? 127.445 114.004 153.419 1.00 69.72  ? 213 LYS K NZ    1 
ATOM   8338 N  N     . GLN C 3 214 ? 130.888 107.315 151.872 1.00 70.13  ? 214 GLN K N     1 
ATOM   8339 C  CA    . GLN C 3 214 ? 131.087 106.001 152.463 1.00 67.84  ? 214 GLN K CA    1 
ATOM   8340 C  C     . GLN C 3 214 ? 131.913 106.125 153.733 1.00 71.08  ? 214 GLN K C     1 
ATOM   8341 O  O     . GLN C 3 214 ? 132.877 106.893 153.786 1.00 76.54  ? 214 GLN K O     1 
ATOM   8342 C  CB    . GLN C 3 214 ? 131.776 105.051 151.483 1.00 71.86  ? 214 GLN K CB    1 
ATOM   8343 C  CG    . GLN C 3 214 ? 132.982 105.639 150.785 1.00 72.47  ? 214 GLN K CG    1 
ATOM   8344 C  CD    . GLN C 3 214 ? 133.664 104.644 149.873 1.00 74.37  ? 214 GLN K CD    1 
ATOM   8345 O  OE1   . GLN C 3 214 ? 134.737 104.131 150.186 1.00 77.29  ? 214 GLN K OE1   1 
ATOM   8346 N  NE2   . GLN C 3 214 ? 133.041 104.361 148.740 1.00 73.78  ? 214 GLN K NE2   1 
ATOM   8347 N  N     . GLU C 3 215 ? 131.527 105.364 154.754 1.00 90.98  ? 215 GLU K N     1 
ATOM   8348 C  CA    . GLU C 3 215 ? 132.183 105.394 156.057 1.00 91.86  ? 215 GLU K CA    1 
ATOM   8349 C  C     . GLU C 3 215 ? 132.478 103.965 156.485 1.00 93.37  ? 215 GLU K C     1 
ATOM   8350 O  O     . GLU C 3 215 ? 131.553 103.164 156.659 1.00 96.85  ? 215 GLU K O     1 
ATOM   8351 C  CB    . GLU C 3 215 ? 131.311 106.101 157.094 1.00 93.47  ? 215 GLU K CB    1 
ATOM   8352 C  CG    . GLU C 3 215 ? 132.011 106.376 158.415 1.00 96.02  ? 215 GLU K CG    1 
ATOM   8353 C  CD    . GLU C 3 215 ? 131.728 105.314 159.458 1.00 100.30 ? 215 GLU K CD    1 
ATOM   8354 O  OE1   . GLU C 3 215 ? 130.766 104.538 159.273 1.00 99.08  ? 215 GLU K OE1   1 
ATOM   8355 O  OE2   . GLU C 3 215 ? 132.467 105.253 160.464 1.00 99.49  ? 215 GLU K OE2   1 
ATOM   8356 N  N     . ASN C 3 216 ? 133.756 103.644 156.657 1.00 98.05  ? 216 ASN K N     1 
ATOM   8357 C  CA    . ASN C 3 216 ? 134.144 102.326 157.137 1.00 98.95  ? 216 ASN K CA    1 
ATOM   8358 C  C     . ASN C 3 216 ? 134.030 102.276 158.654 1.00 101.24 ? 216 ASN K C     1 
ATOM   8359 O  O     . ASN C 3 216 ? 134.629 103.095 159.358 1.00 103.52 ? 216 ASN K O     1 
ATOM   8360 C  CB    . ASN C 3 216 ? 135.568 101.991 156.706 1.00 101.36 ? 216 ASN K CB    1 
ATOM   8361 C  CG    . ASN C 3 216 ? 135.815 100.504 156.642 1.00 102.61 ? 216 ASN K CG    1 
ATOM   8362 O  OD1   . ASN C 3 216 ? 135.173 99.729  157.348 1.00 102.39 ? 216 ASN K OD1   1 
ATOM   8363 N  ND2   . ASN C 3 216 ? 136.750 100.094 155.794 1.00 102.37 ? 216 ASN K ND2   1 
ATOM   8364 N  N     . THR C 3 217 ? 133.257 101.312 159.155 1.00 104.52 ? 217 THR K N     1 
ATOM   8365 C  CA    . THR C 3 217 ? 133.038 101.220 160.594 1.00 107.18 ? 217 THR K CA    1 
ATOM   8366 C  C     . THR C 3 217 ? 134.317 100.836 161.328 1.00 109.16 ? 217 THR K C     1 
ATOM   8367 O  O     . THR C 3 217 ? 134.576 101.326 162.433 1.00 107.92 ? 217 THR K O     1 
ATOM   8368 C  CB    . THR C 3 217 ? 131.930 100.214 160.893 1.00 105.32 ? 217 THR K CB    1 
ATOM   8369 O  OG1   . THR C 3 217 ? 132.207 98.984  160.215 1.00 104.77 ? 217 THR K OG1   1 
ATOM   8370 C  CG2   . THR C 3 217 ? 130.591 100.750 160.424 1.00 104.42 ? 217 THR K CG2   1 
ATOM   8371 N  N     . GLN C 3 218 ? 135.129 99.965  160.730 1.00 110.10 ? 218 GLN K N     1 
ATOM   8372 C  CA    . GLN C 3 218 ? 136.325 99.480  161.407 1.00 106.57 ? 218 GLN K CA    1 
ATOM   8373 C  C     . GLN C 3 218 ? 137.435 100.525 161.394 1.00 106.39 ? 218 GLN K C     1 
ATOM   8374 O  O     . GLN C 3 218 ? 137.884 100.983 162.449 1.00 106.94 ? 218 GLN K O     1 
ATOM   8375 C  CB    . GLN C 3 218 ? 136.800 98.180  160.755 1.00 107.70 ? 218 GLN K CB    1 
ATOM   8376 C  CG    . GLN C 3 218 ? 135.847 97.015  160.941 1.00 109.17 ? 218 GLN K CG    1 
ATOM   8377 C  CD    . GLN C 3 218 ? 136.493 95.682  160.624 1.00 110.86 ? 218 GLN K CD    1 
ATOM   8378 O  OE1   . GLN C 3 218 ? 137.653 95.622  160.217 1.00 110.52 ? 218 GLN K OE1   1 
ATOM   8379 N  NE2   . GLN C 3 218 ? 135.746 94.601  160.817 1.00 109.03 ? 218 GLN K NE2   1 
ATOM   8380 N  N     . THR C 3 219 ? 137.885 100.919 160.203 1.00 110.10 ? 219 THR K N     1 
ATOM   8381 C  CA    . THR C 3 219 ? 139.005 101.847 160.100 1.00 111.41 ? 219 THR K CA    1 
ATOM   8382 C  C     . THR C 3 219 ? 138.622 103.269 160.489 1.00 111.54 ? 219 THR K C     1 
ATOM   8383 O  O     . THR C 3 219 ? 139.513 104.106 160.670 1.00 110.73 ? 219 THR K O     1 
ATOM   8384 C  CB    . THR C 3 219 ? 139.568 101.831 158.678 1.00 112.17 ? 219 THR K CB    1 
ATOM   8385 O  OG1   . THR C 3 219 ? 138.538 102.200 157.753 1.00 113.01 ? 219 THR K OG1   1 
ATOM   8386 C  CG2   . THR C 3 219 ? 140.081 100.443 158.320 1.00 110.70 ? 219 THR K CG2   1 
ATOM   8387 N  N     . GLU C 3 220 ? 137.327 103.555 160.628 1.00 113.89 ? 220 GLU K N     1 
ATOM   8388 C  CA    . GLU C 3 220 ? 136.841 104.894 160.968 1.00 113.74 ? 220 GLU K CA    1 
ATOM   8389 C  C     . GLU C 3 220 ? 137.331 105.935 159.963 1.00 114.71 ? 220 GLU K C     1 
ATOM   8390 O  O     . GLU C 3 220 ? 137.740 107.037 160.331 1.00 114.95 ? 220 GLU K O     1 
ATOM   8391 C  CB    . GLU C 3 220 ? 137.237 105.282 162.393 1.00 114.44 ? 220 GLU K CB    1 
ATOM   8392 C  CG    . GLU C 3 220 ? 136.761 104.304 163.454 1.00 115.21 ? 220 GLU K CG    1 
ATOM   8393 C  CD    . GLU C 3 220 ? 137.876 103.859 164.380 1.00 117.06 ? 220 GLU K CD    1 
ATOM   8394 O  OE1   . GLU C 3 220 ? 139.044 104.218 164.123 1.00 117.03 ? 220 GLU K OE1   1 
ATOM   8395 O  OE2   . GLU C 3 220 ? 137.584 103.149 165.365 1.00 115.82 ? 220 GLU K OE2   1 
ATOM   8396 N  N     . GLN C 3 221 ? 137.284 105.581 158.683 1.00 105.29 ? 221 GLN K N     1 
ATOM   8397 C  CA    . GLN C 3 221 ? 137.683 106.467 157.601 1.00 102.15 ? 221 GLN K CA    1 
ATOM   8398 C  C     . GLN C 3 221 ? 136.458 106.882 156.799 1.00 100.84 ? 221 GLN K C     1 
ATOM   8399 O  O     . GLN C 3 221 ? 135.607 106.050 156.474 1.00 102.31 ? 221 GLN K O     1 
ATOM   8400 C  CB    . GLN C 3 221 ? 138.706 105.791 156.687 1.00 100.84 ? 221 GLN K CB    1 
ATOM   8401 C  CG    . GLN C 3 221 ? 140.052 105.549 157.350 1.00 104.04 ? 221 GLN K CG    1 
ATOM   8402 C  CD    . GLN C 3 221 ? 141.091 105.008 156.388 1.00 105.61 ? 221 GLN K CD    1 
ATOM   8403 O  OE1   . GLN C 3 221 ? 140.793 104.729 155.226 1.00 106.16 ? 221 GLN K OE1   1 
ATOM   8404 N  NE2   . GLN C 3 221 ? 142.320 104.860 156.867 1.00 103.66 ? 221 GLN K NE2   1 
ATOM   8405 N  N     . LYS C 3 222 ? 136.373 108.170 156.482 1.00 83.82  ? 222 LYS K N     1 
ATOM   8406 C  CA    . LYS C 3 222 ? 135.242 108.728 155.758 1.00 82.77  ? 222 LYS K CA    1 
ATOM   8407 C  C     . LYS C 3 222 ? 135.695 109.287 154.417 1.00 81.14  ? 222 LYS K C     1 
ATOM   8408 O  O     . LYS C 3 222 ? 136.737 109.942 154.326 1.00 83.48  ? 222 LYS K O     1 
ATOM   8409 C  CB    . LYS C 3 222 ? 134.555 109.828 156.570 1.00 83.79  ? 222 LYS K CB    1 
ATOM   8410 C  CG    . LYS C 3 222 ? 134.039 109.377 157.923 1.00 86.43  ? 222 LYS K CG    1 
ATOM   8411 C  CD    . LYS C 3 222 ? 134.972 109.802 159.044 1.00 87.03  ? 222 LYS K CD    1 
ATOM   8412 C  CE    . LYS C 3 222 ? 135.086 111.316 159.121 1.00 88.26  ? 222 LYS K CE    1 
ATOM   8413 N  NZ    . LYS C 3 222 ? 135.999 111.751 160.214 1.00 86.76  ? 222 LYS K NZ    1 
ATOM   8414 N  N     . LEU C 3 223 ? 134.907 109.020 153.380 1.00 67.44  ? 223 LEU K N     1 
ATOM   8415 C  CA    . LEU C 3 223 ? 135.164 109.508 152.034 1.00 66.80  ? 223 LEU K CA    1 
ATOM   8416 C  C     . LEU C 3 223 ? 133.902 110.160 151.494 1.00 69.40  ? 223 LEU K C     1 
ATOM   8417 O  O     . LEU C 3 223 ? 132.797 109.658 151.710 1.00 75.68  ? 223 LEU K O     1 
ATOM   8418 C  CB    . LEU C 3 223 ? 135.602 108.377 151.109 1.00 67.69  ? 223 LEU K CB    1 
ATOM   8419 C  CG    . LEU C 3 223 ? 136.937 107.731 151.455 1.00 69.58  ? 223 LEU K CG    1 
ATOM   8420 C  CD1   . LEU C 3 223 ? 137.250 106.615 150.478 1.00 70.55  ? 223 LEU K CD1   1 
ATOM   8421 C  CD2   . LEU C 3 223 ? 138.043 108.768 151.461 1.00 70.65  ? 223 LEU K CD2   1 
ATOM   8422 N  N     . SER C 3 224 ? 134.067 111.278 150.792 1.00 60.38  ? 224 SER K N     1 
ATOM   8423 C  CA    . SER C 3 224 ? 132.940 112.025 150.251 1.00 58.39  ? 224 SER K CA    1 
ATOM   8424 C  C     . SER C 3 224 ? 133.213 112.390 148.803 1.00 63.84  ? 224 SER K C     1 
ATOM   8425 O  O     . SER C 3 224 ? 134.295 112.889 148.479 1.00 67.30  ? 224 SER K O     1 
ATOM   8426 C  CB    . SER C 3 224 ? 132.674 113.290 151.068 1.00 64.77  ? 224 SER K CB    1 
ATOM   8427 O  OG    . SER C 3 224 ? 131.716 114.113 150.427 1.00 68.69  ? 224 SER K OG    1 
ATOM   8428 N  N     . GLY C 3 225 ? 132.233 112.146 147.938 1.00 63.40  ? 225 GLY K N     1 
ATOM   8429 C  CA    . GLY C 3 225 ? 132.364 112.476 146.535 1.00 57.41  ? 225 GLY K CA    1 
ATOM   8430 C  C     . GLY C 3 225 ? 131.110 113.090 145.955 1.00 57.78  ? 225 GLY K C     1 
ATOM   8431 O  O     . GLY C 3 225 ? 130.000 112.645 146.254 1.00 68.36  ? 225 GLY K O     1 
ATOM   8432 N  N     . LYS C 3 226 ? 131.275 114.111 145.122 1.00 41.09  ? 226 LYS K N     1 
ATOM   8433 C  CA    . LYS C 3 226 ? 130.167 114.822 144.506 1.00 42.66  ? 226 LYS K CA    1 
ATOM   8434 C  C     . LYS C 3 226 ? 130.320 114.763 142.996 1.00 47.45  ? 226 LYS K C     1 
ATOM   8435 O  O     . LYS C 3 226 ? 131.404 115.027 142.468 1.00 59.44  ? 226 LYS K O     1 
ATOM   8436 C  CB    . LYS C 3 226 ? 130.119 116.274 144.983 1.00 53.52  ? 226 LYS K CB    1 
ATOM   8437 C  CG    . LYS C 3 226 ? 130.343 116.440 146.474 1.00 55.16  ? 226 LYS K CG    1 
ATOM   8438 C  CD    . LYS C 3 226 ? 130.558 117.893 146.857 1.00 49.69  ? 226 LYS K CD    1 
ATOM   8439 C  CE    . LYS C 3 226 ? 129.338 118.734 146.542 1.00 54.96  ? 226 LYS K CE    1 
ATOM   8440 N  NZ    . LYS C 3 226 ? 129.502 120.142 146.999 1.00 53.83  ? 226 LYS K NZ    1 
ATOM   8441 N  N     . LEU C 3 227 ? 129.242 114.408 142.307 1.00 37.82  ? 227 LEU K N     1 
ATOM   8442 C  CA    . LEU C 3 227 ? 129.221 114.313 140.855 1.00 36.83  ? 227 LEU K CA    1 
ATOM   8443 C  C     . LEU C 3 227 ? 128.203 115.303 140.316 1.00 45.68  ? 227 LEU K C     1 
ATOM   8444 O  O     . LEU C 3 227 ? 127.060 115.336 140.780 1.00 58.00  ? 227 LEU K O     1 
ATOM   8445 C  CB    . LEU C 3 227 ? 128.885 112.893 140.403 1.00 41.75  ? 227 LEU K CB    1 
ATOM   8446 C  CG    . LEU C 3 227 ? 128.877 112.632 138.904 1.00 43.67  ? 227 LEU K CG    1 
ATOM   8447 C  CD1   . LEU C 3 227 ? 130.181 113.082 138.298 1.00 50.07  ? 227 LEU K CD1   1 
ATOM   8448 C  CD2   . LEU C 3 227 ? 128.668 111.162 138.646 1.00 40.37  ? 227 LEU K CD2   1 
ATOM   8449 N  N     . TYR C 3 228 ? 128.619 116.105 139.345 1.00 39.47  ? 228 TYR K N     1 
ATOM   8450 C  CA    . TYR C 3 228 ? 127.794 117.165 138.787 1.00 31.89  ? 228 TYR K CA    1 
ATOM   8451 C  C     . TYR C 3 228 ? 127.470 116.862 137.333 1.00 44.19  ? 228 TYR K C     1 
ATOM   8452 O  O     . TYR C 3 228 ? 128.366 116.545 136.547 1.00 56.90  ? 228 TYR K O     1 
ATOM   8453 C  CB    . TYR C 3 228 ? 128.504 118.512 138.885 1.00 37.43  ? 228 TYR K CB    1 
ATOM   8454 C  CG    . TYR C 3 228 ? 128.476 119.136 140.253 1.00 43.96  ? 228 TYR K CG    1 
ATOM   8455 C  CD1   . TYR C 3 228 ? 127.369 119.837 140.690 1.00 47.70  ? 228 TYR K CD1   1 
ATOM   8456 C  CD2   . TYR C 3 228 ? 129.564 119.046 141.098 1.00 46.34  ? 228 TYR K CD2   1 
ATOM   8457 C  CE1   . TYR C 3 228 ? 127.343 120.417 141.930 1.00 47.46  ? 228 TYR K CE1   1 
ATOM   8458 C  CE2   . TYR C 3 228 ? 129.545 119.623 142.342 1.00 45.70  ? 228 TYR K CE2   1 
ATOM   8459 C  CZ    . TYR C 3 228 ? 128.433 120.307 142.752 1.00 45.77  ? 228 TYR K CZ    1 
ATOM   8460 O  OH    . TYR C 3 228 ? 128.409 120.887 143.995 1.00 48.77  ? 228 TYR K OH    1 
ATOM   8461 N  N     . LEU C 3 229 ? 126.192 116.964 136.982 1.00 41.67  ? 229 LEU K N     1 
ATOM   8462 C  CA    . LEU C 3 229 ? 125.720 116.779 135.614 1.00 40.15  ? 229 LEU K CA    1 
ATOM   8463 C  C     . LEU C 3 229 ? 124.975 118.041 135.201 1.00 44.11  ? 229 LEU K C     1 
ATOM   8464 O  O     . LEU C 3 229 ? 123.881 118.311 135.703 1.00 46.08  ? 229 LEU K O     1 
ATOM   8465 C  CB    . LEU C 3 229 ? 124.825 115.547 135.513 1.00 45.40  ? 229 LEU K CB    1 
ATOM   8466 C  CG    . LEU C 3 229 ? 125.391 114.270 136.126 1.00 41.12  ? 229 LEU K CG    1 
ATOM   8467 C  CD1   . LEU C 3 229 ? 124.295 113.250 136.302 1.00 43.18  ? 229 LEU K CD1   1 
ATOM   8468 C  CD2   . LEU C 3 229 ? 126.483 113.715 135.248 1.00 47.48  ? 229 LEU K CD2   1 
ATOM   8469 N  N     . VAL C 3 230 ? 125.561 118.806 134.284 1.00 44.66  ? 230 VAL K N     1 
ATOM   8470 C  CA    . VAL C 3 230 ? 125.046 120.111 133.888 1.00 40.91  ? 230 VAL K CA    1 
ATOM   8471 C  C     . VAL C 3 230 ? 124.467 120.009 132.486 1.00 47.86  ? 230 VAL K C     1 
ATOM   8472 O  O     . VAL C 3 230 ? 125.139 119.540 131.561 1.00 54.59  ? 230 VAL K O     1 
ATOM   8473 C  CB    . VAL C 3 230 ? 126.142 121.188 133.950 1.00 47.61  ? 230 VAL K CB    1 
ATOM   8474 C  CG1   . VAL C 3 230 ? 125.587 122.530 133.516 1.00 52.77  ? 230 VAL K CG1   1 
ATOM   8475 C  CG2   . VAL C 3 230 ? 126.711 121.280 135.345 1.00 48.47  ? 230 VAL K CG2   1 
ATOM   8476 N  N     . ASP C 3 231 ? 123.221 120.445 132.332 1.00 57.79  ? 231 ASP K N     1 
ATOM   8477 C  CA    . ASP C 3 231 ? 122.537 120.507 131.043 1.00 55.24  ? 231 ASP K CA    1 
ATOM   8478 C  C     . ASP C 3 231 ? 122.415 121.979 130.668 1.00 55.48  ? 231 ASP K C     1 
ATOM   8479 O  O     . ASP C 3 231 ? 121.536 122.685 131.169 1.00 60.21  ? 231 ASP K O     1 
ATOM   8480 C  CB    . ASP C 3 231 ? 121.173 119.832 131.120 1.00 60.80  ? 231 ASP K CB    1 
ATOM   8481 C  CG    . ASP C 3 231 ? 120.466 119.784 129.780 1.00 68.51  ? 231 ASP K CG    1 
ATOM   8482 O  OD1   . ASP C 3 231 ? 121.074 120.179 128.763 1.00 67.61  ? 231 ASP K OD1   1 
ATOM   8483 O  OD2   . ASP C 3 231 ? 119.295 119.350 129.743 1.00 66.64  ? 231 ASP K OD2   1 
ATOM   8484 N  N     . LEU C 3 232 ? 123.295 122.437 129.787 1.00 46.72  ? 232 LEU K N     1 
ATOM   8485 C  CA    . LEU C 3 232 ? 123.358 123.840 129.411 1.00 47.82  ? 232 LEU K CA    1 
ATOM   8486 C  C     . LEU C 3 232 ? 122.357 124.164 128.313 1.00 54.53  ? 232 LEU K C     1 
ATOM   8487 O  O     . LEU C 3 232 ? 122.012 123.318 127.486 1.00 54.93  ? 232 LEU K O     1 
ATOM   8488 C  CB    . LEU C 3 232 ? 124.760 124.210 128.937 1.00 42.77  ? 232 LEU K CB    1 
ATOM   8489 C  CG    . LEU C 3 232 ? 125.881 124.115 129.960 1.00 45.91  ? 232 LEU K CG    1 
ATOM   8490 C  CD1   . LEU C 3 232 ? 127.204 124.047 129.243 1.00 47.68  ? 232 LEU K CD1   1 
ATOM   8491 C  CD2   . LEU C 3 232 ? 125.837 125.300 130.892 1.00 49.48  ? 232 LEU K CD2   1 
ATOM   8492 N  N     . ALA C 3 233 ? 121.892 125.409 128.315 1.00 55.48  ? 233 ALA K N     1 
ATOM   8493 C  CA    . ALA C 3 233 ? 121.040 125.912 127.253 1.00 51.66  ? 233 ALA K CA    1 
ATOM   8494 C  C     . ALA C 3 233 ? 121.886 126.512 126.135 1.00 58.00  ? 233 ALA K C     1 
ATOM   8495 O  O     . ALA C 3 233 ? 123.036 126.910 126.335 1.00 63.95  ? 233 ALA K O     1 
ATOM   8496 C  CB    . ALA C 3 233 ? 120.063 126.952 127.794 1.00 51.32  ? 233 ALA K CB    1 
ATOM   8497 N  N     . GLY C 3 234 ? 121.301 126.576 124.944 1.00 61.14  ? 234 GLY K N     1 
ATOM   8498 C  CA    . GLY C 3 234 ? 122.044 126.958 123.761 1.00 61.20  ? 234 GLY K CA    1 
ATOM   8499 C  C     . GLY C 3 234 ? 121.985 128.445 123.462 1.00 59.80  ? 234 GLY K C     1 
ATOM   8500 O  O     . GLY C 3 234 ? 120.987 129.111 123.714 1.00 65.86  ? 234 GLY K O     1 
ATOM   8501 N  N     . SER C 3 235 ? 123.080 128.954 122.910 1.00 51.75  ? 235 SER K N     1 
ATOM   8502 C  CA    . SER C 3 235 ? 123.162 130.362 122.560 1.00 52.73  ? 235 SER K CA    1 
ATOM   8503 C  C     . SER C 3 235 ? 122.242 130.680 121.390 1.00 62.19  ? 235 SER K C     1 
ATOM   8504 O  O     . SER C 3 235 ? 122.012 129.852 120.506 1.00 68.28  ? 235 SER K O     1 
ATOM   8505 C  CB    . SER C 3 235 ? 124.597 130.745 122.214 1.00 55.97  ? 235 SER K CB    1 
ATOM   8506 O  OG    . SER C 3 235 ? 125.061 130.001 121.104 1.00 62.73  ? 235 SER K OG    1 
ATOM   8507 N  N     . GLU C 3 236 ? 121.712 131.898 121.395 1.00 67.94  ? 236 GLU K N     1 
ATOM   8508 C  CA    . GLU C 3 236 ? 120.761 132.353 120.393 1.00 63.78  ? 236 GLU K CA    1 
ATOM   8509 C  C     . GLU C 3 236 ? 121.296 133.600 119.711 1.00 64.11  ? 236 GLU K C     1 
ATOM   8510 O  O     . GLU C 3 236 ? 121.779 134.519 120.379 1.00 65.79  ? 236 GLU K O     1 
ATOM   8511 C  CB    . GLU C 3 236 ? 119.401 132.643 121.029 1.00 63.64  ? 236 GLU K CB    1 
ATOM   8512 C  CG    . GLU C 3 236 ? 118.317 133.019 120.037 1.00 70.80  ? 236 GLU K CG    1 
ATOM   8513 C  CD    . GLU C 3 236 ? 116.942 133.061 120.669 1.00 76.41  ? 236 GLU K CD    1 
ATOM   8514 O  OE1   . GLU C 3 236 ? 116.779 132.510 121.778 1.00 74.47  ? 236 GLU K OE1   1 
ATOM   8515 O  OE2   . GLU C 3 236 ? 116.022 133.644 120.057 1.00 75.38  ? 236 GLU K OE2   1 
ATOM   8516 N  N     . LYS C 3 237 ? 121.215 133.627 118.385 1.00 65.60  ? 237 LYS K N     1 
ATOM   8517 C  CA    . LYS C 3 237 ? 121.511 134.825 117.611 1.00 64.94  ? 237 LYS K CA    1 
ATOM   8518 C  C     . LYS C 3 237 ? 120.218 135.620 117.472 1.00 65.38  ? 237 LYS K C     1 
ATOM   8519 O  O     . LYS C 3 237 ? 119.340 135.260 116.683 1.00 68.56  ? 237 LYS K O     1 
ATOM   8520 C  CB    . LYS C 3 237 ? 122.093 134.462 116.249 1.00 71.29  ? 237 LYS K CB    1 
ATOM   8521 C  CG    . LYS C 3 237 ? 122.847 135.595 115.584 1.00 71.91  ? 237 LYS K CG    1 
ATOM   8522 C  CD    . LYS C 3 237 ? 123.527 135.132 114.310 1.00 71.74  ? 237 LYS K CD    1 
ATOM   8523 C  CE    . LYS C 3 237 ? 124.397 133.913 114.563 1.00 70.12  ? 237 LYS K CE    1 
ATOM   8524 N  NZ    . LYS C 3 237 ? 125.408 134.162 115.625 1.00 67.46  ? 237 LYS K NZ    1 
ATOM   8525 N  N     . VAL C 3 238 ? 120.108 136.702 118.240 1.00 56.81  ? 238 VAL K N     1 
ATOM   8526 C  CA    . VAL C 3 238 ? 118.841 137.410 118.374 1.00 54.97  ? 238 VAL K CA    1 
ATOM   8527 C  C     . VAL C 3 238 ? 118.448 138.088 117.068 1.00 62.01  ? 238 VAL K C     1 
ATOM   8528 O  O     . VAL C 3 238 ? 117.265 138.144 116.715 1.00 65.07  ? 238 VAL K O     1 
ATOM   8529 C  CB    . VAL C 3 238 ? 118.927 138.414 119.535 1.00 55.01  ? 238 VAL K CB    1 
ATOM   8530 C  CG1   . VAL C 3 238 ? 117.668 139.239 119.605 1.00 60.66  ? 238 VAL K CG1   1 
ATOM   8531 C  CG2   . VAL C 3 238 ? 119.139 137.681 120.836 1.00 58.71  ? 238 VAL K CG2   1 
ATOM   8532 N  N     . SER C 3 239 ? 119.429 138.609 116.329 1.00 68.77  ? 239 SER K N     1 
ATOM   8533 C  CA    . SER C 3 239 ? 119.130 139.362 115.115 1.00 62.37  ? 239 SER K CA    1 
ATOM   8534 C  C     . SER C 3 239 ? 118.398 138.518 114.080 1.00 65.47  ? 239 SER K C     1 
ATOM   8535 O  O     . SER C 3 239 ? 117.625 139.055 113.280 1.00 68.45  ? 239 SER K O     1 
ATOM   8536 C  CB    . SER C 3 239 ? 120.421 139.920 114.523 1.00 63.07  ? 239 SER K CB    1 
ATOM   8537 O  OG    . SER C 3 239 ? 121.125 140.690 115.479 1.00 69.77  ? 239 SER K OG    1 
ATOM   8538 N  N     . LYS C 3 240 ? 118.622 137.207 114.077 1.00 70.26  ? 240 LYS K N     1 
ATOM   8539 C  CA    . LYS C 3 240 ? 118.001 136.314 113.111 1.00 66.76  ? 240 LYS K CA    1 
ATOM   8540 C  C     . LYS C 3 240 ? 116.718 135.672 113.619 1.00 68.61  ? 240 LYS K C     1 
ATOM   8541 O  O     . LYS C 3 240 ? 116.112 134.882 112.890 1.00 73.38  ? 240 LYS K O     1 
ATOM   8542 C  CB    . LYS C 3 240 ? 118.987 135.217 112.700 1.00 69.37  ? 240 LYS K CB    1 
ATOM   8543 C  CG    . LYS C 3 240 ? 120.186 135.714 111.919 1.00 73.43  ? 240 LYS K CG    1 
ATOM   8544 C  CD    . LYS C 3 240 ? 121.092 134.562 111.523 1.00 73.03  ? 240 LYS K CD    1 
ATOM   8545 C  CE    . LYS C 3 240 ? 120.343 133.533 110.692 1.00 73.44  ? 240 LYS K CE    1 
ATOM   8546 N  NZ    . LYS C 3 240 ? 121.209 132.379 110.324 1.00 72.99  ? 240 LYS K NZ    1 
ATOM   8547 N  N     . THR C 3 241 ? 116.287 135.981 114.838 1.00 64.50  ? 241 THR K N     1 
ATOM   8548 C  CA    . THR C 3 241 ? 115.095 135.376 115.415 1.00 66.33  ? 241 THR K CA    1 
ATOM   8549 C  C     . THR C 3 241 ? 113.968 136.373 115.630 1.00 65.71  ? 241 THR K C     1 
ATOM   8550 O  O     . THR C 3 241 ? 112.818 136.087 115.285 1.00 71.28  ? 241 THR K O     1 
ATOM   8551 C  CB    . THR C 3 241 ? 115.437 134.689 116.743 1.00 71.66  ? 241 THR K CB    1 
ATOM   8552 O  OG1   . THR C 3 241 ? 115.938 135.659 117.672 1.00 76.56  ? 241 THR K OG1   1 
ATOM   8553 C  CG2   . THR C 3 241 ? 116.481 133.611 116.528 1.00 65.21  ? 241 THR K CG2   1 
ATOM   8554 N  N     . GLY C 3 242 ? 114.262 137.539 116.191 1.00 60.97  ? 242 GLY K N     1 
ATOM   8555 C  CA    . GLY C 3 242 ? 113.233 138.528 116.431 1.00 61.47  ? 242 GLY K CA    1 
ATOM   8556 C  C     . GLY C 3 242 ? 112.733 138.501 117.857 1.00 64.62  ? 242 GLY K C     1 
ATOM   8557 O  O     . GLY C 3 242 ? 111.528 138.597 118.105 1.00 70.17  ? 242 GLY K O     1 
ATOM   8558 N  N     . ALA C 3 243 ? 113.656 138.370 118.805 1.00 62.84  ? 243 ALA K N     1 
ATOM   8559 C  CA    . ALA C 3 243 ? 113.281 138.260 120.206 1.00 65.69  ? 243 ALA K CA    1 
ATOM   8560 C  C     . ALA C 3 243 ? 112.769 139.594 120.732 1.00 63.40  ? 243 ALA K C     1 
ATOM   8561 O  O     . ALA C 3 243 ? 113.409 140.633 120.553 1.00 67.12  ? 243 ALA K O     1 
ATOM   8562 C  CB    . ALA C 3 243 ? 114.471 137.784 121.033 1.00 68.74  ? 243 ALA K CB    1 
ATOM   8563 N  N     . GLU C 3 244 ? 111.610 139.559 121.381 1.00 67.68  ? 244 GLU K N     1 
ATOM   8564 C  CA    . GLU C 3 244 ? 111.044 140.716 122.051 1.00 70.34  ? 244 GLU K CA    1 
ATOM   8565 C  C     . GLU C 3 244 ? 110.478 140.274 123.391 1.00 70.70  ? 244 GLU K C     1 
ATOM   8566 O  O     . GLU C 3 244 ? 109.916 139.184 123.512 1.00 75.05  ? 244 GLU K O     1 
ATOM   8567 C  CB    . GLU C 3 244 ? 109.944 141.378 121.214 1.00 71.42  ? 244 GLU K CB    1 
ATOM   8568 C  CG    . GLU C 3 244 ? 110.392 141.849 119.844 1.00 72.55  ? 244 GLU K CG    1 
ATOM   8569 C  CD    . GLU C 3 244 ? 110.133 143.325 119.624 1.00 78.39  ? 244 GLU K CD    1 
ATOM   8570 O  OE1   . GLU C 3 244 ? 109.974 144.057 120.623 1.00 77.49  ? 244 GLU K OE1   1 
ATOM   8571 O  OE2   . GLU C 3 244 ? 110.086 143.753 118.452 1.00 79.24  ? 244 GLU K OE2   1 
ATOM   8572 N  N     . GLY C 3 245 ? 110.631 141.127 124.396 1.00 61.47  ? 245 GLY K N     1 
ATOM   8573 C  CA    . GLY C 3 245 ? 110.093 140.830 125.707 1.00 64.60  ? 245 GLY K CA    1 
ATOM   8574 C  C     . GLY C 3 245 ? 110.966 139.918 126.542 1.00 63.74  ? 245 GLY K C     1 
ATOM   8575 O  O     . GLY C 3 245 ? 112.186 140.092 126.591 1.00 69.46  ? 245 GLY K O     1 
ATOM   8576 N  N     . ALA C 3 246 ? 110.347 138.943 127.211 1.00 59.23  ? 246 ALA K N     1 
ATOM   8577 C  CA    . ALA C 3 246 ? 111.092 138.071 128.111 1.00 64.70  ? 246 ALA K CA    1 
ATOM   8578 C  C     . ALA C 3 246 ? 112.069 137.178 127.360 1.00 65.82  ? 246 ALA K C     1 
ATOM   8579 O  O     . ALA C 3 246 ? 113.113 136.804 127.912 1.00 71.83  ? 246 ALA K O     1 
ATOM   8580 C  CB    . ALA C 3 246 ? 110.128 137.222 128.936 1.00 66.14  ? 246 ALA K CB    1 
ATOM   8581 N  N     . VAL C 3 247 ? 111.753 136.825 126.114 1.00 60.76  ? 247 VAL K N     1 
ATOM   8582 C  CA    . VAL C 3 247 ? 112.631 135.948 125.346 1.00 66.76  ? 247 VAL K CA    1 
ATOM   8583 C  C     . VAL C 3 247 ? 113.985 136.608 125.130 1.00 68.85  ? 247 VAL K C     1 
ATOM   8584 O  O     . VAL C 3 247 ? 115.034 135.958 125.223 1.00 71.21  ? 247 VAL K O     1 
ATOM   8585 C  CB    . VAL C 3 247 ? 111.967 135.563 124.013 1.00 63.86  ? 247 VAL K CB    1 
ATOM   8586 C  CG1   . VAL C 3 247 ? 112.719 134.421 123.358 1.00 65.19  ? 247 VAL K CG1   1 
ATOM   8587 C  CG2   . VAL C 3 247 ? 110.517 135.189 124.241 1.00 60.14  ? 247 VAL K CG2   1 
ATOM   8588 N  N     . LEU C 3 248 ? 113.986 137.910 124.844 1.00 61.93  ? 248 LEU K N     1 
ATOM   8589 C  CA    . LEU C 3 248 ? 115.241 138.625 124.648 1.00 59.15  ? 248 LEU K CA    1 
ATOM   8590 C  C     . LEU C 3 248 ? 116.068 138.659 125.928 1.00 65.69  ? 248 LEU K C     1 
ATOM   8591 O  O     . LEU C 3 248 ? 117.296 138.505 125.887 1.00 72.09  ? 248 LEU K O     1 
ATOM   8592 C  CB    . LEU C 3 248 ? 114.956 140.037 124.146 1.00 59.69  ? 248 LEU K CB    1 
ATOM   8593 C  CG    . LEU C 3 248 ? 116.158 140.914 123.818 1.00 62.07  ? 248 LEU K CG    1 
ATOM   8594 C  CD1   . LEU C 3 248 ? 117.177 140.143 123.012 1.00 64.45  ? 248 LEU K CD1   1 
ATOM   8595 C  CD2   . LEU C 3 248 ? 115.715 142.148 123.067 1.00 60.42  ? 248 LEU K CD2   1 
ATOM   8596 N  N     . ASP C 3 249 ? 115.418 138.871 127.075 1.00 63.63  ? 249 ASP K N     1 
ATOM   8597 C  CA    . ASP C 3 249 ? 116.139 138.871 128.344 1.00 62.86  ? 249 ASP K CA    1 
ATOM   8598 C  C     . ASP C 3 249 ? 116.753 137.507 128.625 1.00 64.67  ? 249 ASP K C     1 
ATOM   8599 O  O     . ASP C 3 249 ? 117.911 137.411 129.060 1.00 72.81  ? 249 ASP K O     1 
ATOM   8600 C  CB    . ASP C 3 249 ? 115.202 139.281 129.477 1.00 64.30  ? 249 ASP K CB    1 
ATOM   8601 C  CG    . ASP C 3 249 ? 114.551 140.625 129.234 1.00 70.92  ? 249 ASP K CG    1 
ATOM   8602 O  OD1   . ASP C 3 249 ? 114.812 141.229 128.173 1.00 71.96  ? 249 ASP K OD1   1 
ATOM   8603 O  OD2   . ASP C 3 249 ? 113.779 141.079 130.104 1.00 71.28  ? 249 ASP K OD2   1 
ATOM   8604 N  N     . GLU C 3 250 ? 115.995 136.440 128.369 1.00 54.11  ? 250 GLU K N     1 
ATOM   8605 C  CA    . GLU C 3 250 ? 116.541 135.100 128.531 1.00 58.13  ? 250 GLU K CA    1 
ATOM   8606 C  C     . GLU C 3 250 ? 117.733 134.880 127.611 1.00 61.72  ? 250 GLU K C     1 
ATOM   8607 O  O     . GLU C 3 250 ? 118.737 134.283 128.018 1.00 71.20  ? 250 GLU K O     1 
ATOM   8608 C  CB    . GLU C 3 250 ? 115.458 134.059 128.263 1.00 62.74  ? 250 GLU K CB    1 
ATOM   8609 C  CG    . GLU C 3 250 ? 114.313 134.085 129.253 1.00 66.83  ? 250 GLU K CG    1 
ATOM   8610 C  CD    . GLU C 3 250 ? 113.122 133.271 128.786 1.00 70.51  ? 250 GLU K CD    1 
ATOM   8611 O  OE1   . GLU C 3 250 ? 113.233 132.598 127.741 1.00 66.19  ? 250 GLU K OE1   1 
ATOM   8612 O  OE2   . GLU C 3 250 ? 112.075 133.304 129.463 1.00 72.15  ? 250 GLU K OE2   1 
ATOM   8613 N  N     . ALA C 3 251 ? 117.642 135.352 126.366 1.00 51.16  ? 251 ALA K N     1 
ATOM   8614 C  CA    . ALA C 3 251 ? 118.740 135.169 125.423 1.00 54.79  ? 251 ALA K CA    1 
ATOM   8615 C  C     . ALA C 3 251 ? 119.993 135.898 125.884 1.00 57.55  ? 251 ALA K C     1 
ATOM   8616 O  O     . ALA C 3 251 ? 121.102 135.352 125.813 1.00 65.73  ? 251 ALA K O     1 
ATOM   8617 C  CB    . ALA C 3 251 ? 118.321 135.647 124.035 1.00 59.90  ? 251 ALA K CB    1 
ATOM   8618 N  N     . LYS C 3 252 ? 119.833 137.129 126.367 1.00 52.72  ? 252 LYS K N     1 
ATOM   8619 C  CA    . LYS C 3 252 ? 120.970 137.883 126.879 1.00 51.95  ? 252 LYS K CA    1 
ATOM   8620 C  C     . LYS C 3 252 ? 121.628 137.154 128.041 1.00 56.60  ? 252 LYS K C     1 
ATOM   8621 O  O     . LYS C 3 252 ? 122.859 137.000 128.084 1.00 61.39  ? 252 LYS K O     1 
ATOM   8622 C  CB    . LYS C 3 252 ? 120.514 139.270 127.321 1.00 53.41  ? 252 LYS K CB    1 
ATOM   8623 C  CG    . LYS C 3 252 ? 120.027 140.170 126.210 1.00 56.35  ? 252 LYS K CG    1 
ATOM   8624 C  CD    . LYS C 3 252 ? 119.303 141.367 126.795 1.00 56.80  ? 252 LYS K CD    1 
ATOM   8625 C  CE    . LYS C 3 252 ? 118.911 142.364 125.732 1.00 62.67  ? 252 LYS K CE    1 
ATOM   8626 N  NZ    . LYS C 3 252 ? 118.038 143.424 126.299 1.00 57.68  ? 252 LYS K NZ    1 
ATOM   8627 N  N     . ASN C 3 253 ? 120.816 136.688 128.994 1.00 57.59  ? 253 ASN K N     1 
ATOM   8628 C  CA    . ASN C 3 253 ? 121.369 136.008 130.159 1.00 56.90  ? 253 ASN K CA    1 
ATOM   8629 C  C     . ASN C 3 253 ? 122.102 134.735 129.760 1.00 59.68  ? 253 ASN K C     1 
ATOM   8630 O  O     . ASN C 3 253 ? 123.198 134.452 130.263 1.00 63.92  ? 253 ASN K O     1 
ATOM   8631 C  CB    . ASN C 3 253 ? 120.258 135.700 131.158 1.00 57.91  ? 253 ASN K CB    1 
ATOM   8632 C  CG    . ASN C 3 253 ? 120.793 135.251 132.496 1.00 67.11  ? 253 ASN K CG    1 
ATOM   8633 O  OD1   . ASN C 3 253 ? 120.684 134.081 132.861 1.00 70.25  ? 253 ASN K OD1   1 
ATOM   8634 N  ND2   . ASN C 3 253 ? 121.382 136.181 133.237 1.00 63.89  ? 253 ASN K ND2   1 
ATOM   8635 N  N     . ILE C 3 254 ? 121.517 133.962 128.844 1.00 51.60  ? 254 ILE K N     1 
ATOM   8636 C  CA    . ILE C 3 254 ? 122.132 132.711 128.415 1.00 42.96  ? 254 ILE K CA    1 
ATOM   8637 C  C     . ILE C 3 254 ? 123.465 132.977 127.732 1.00 47.89  ? 254 ILE K C     1 
ATOM   8638 O  O     . ILE C 3 254 ? 124.464 132.294 127.996 1.00 58.77  ? 254 ILE K O     1 
ATOM   8639 C  CB    . ILE C 3 254 ? 121.171 131.935 127.500 1.00 47.44  ? 254 ILE K CB    1 
ATOM   8640 C  CG1   . ILE C 3 254 ? 120.021 131.352 128.313 1.00 49.25  ? 254 ILE K CG1   1 
ATOM   8641 C  CG2   . ILE C 3 254 ? 121.907 130.834 126.763 1.00 54.30  ? 254 ILE K CG2   1 
ATOM   8642 C  CD1   . ILE C 3 254 ? 118.949 130.722 127.474 1.00 53.23  ? 254 ILE K CD1   1 
ATOM   8643 N  N     . ASN C 3 255 ? 123.503 133.967 126.836 1.00 44.48  ? 255 ASN K N     1 
ATOM   8644 C  CA    . ASN C 3 255 ? 124.748 134.270 126.138 1.00 40.20  ? 255 ASN K CA    1 
ATOM   8645 C  C     . ASN C 3 255 ? 125.837 134.691 127.112 1.00 48.83  ? 255 ASN K C     1 
ATOM   8646 O  O     . ASN C 3 255 ? 126.981 134.218 127.025 1.00 50.60  ? 255 ASN K O     1 
ATOM   8647 C  CB    . ASN C 3 255 ? 124.514 135.359 125.095 1.00 40.34  ? 255 ASN K CB    1 
ATOM   8648 C  CG    . ASN C 3 255 ? 123.717 134.866 123.914 1.00 49.29  ? 255 ASN K CG    1 
ATOM   8649 O  OD1   . ASN C 3 255 ? 123.020 133.861 124.000 1.00 53.04  ? 255 ASN K OD1   1 
ATOM   8650 N  ND2   . ASN C 3 255 ? 123.812 135.575 122.801 1.00 49.66  ? 255 ASN K ND2   1 
ATOM   8651 N  N     . LYS C 3 256 ? 125.497 135.564 128.063 1.00 41.95  ? 256 LYS K N     1 
ATOM   8652 C  CA    . LYS C 3 256 ? 126.490 136.019 129.028 1.00 38.25  ? 256 LYS K CA    1 
ATOM   8653 C  C     . LYS C 3 256 ? 127.019 134.861 129.868 1.00 42.50  ? 256 LYS K C     1 
ATOM   8654 O  O     . LYS C 3 256 ? 128.233 134.741 130.083 1.00 47.90  ? 256 LYS K O     1 
ATOM   8655 C  CB    . LYS C 3 256 ? 125.882 137.099 129.919 1.00 47.97  ? 256 LYS K CB    1 
ATOM   8656 C  CG    . LYS C 3 256 ? 126.855 138.166 130.363 1.00 48.76  ? 256 LYS K CG    1 
ATOM   8657 C  CD    . LYS C 3 256 ? 126.132 139.307 131.043 1.00 42.81  ? 256 LYS K CD    1 
ATOM   8658 C  CE    . LYS C 3 256 ? 127.104 140.377 131.480 1.00 45.06  ? 256 LYS K CE    1 
ATOM   8659 N  NZ    . LYS C 3 256 ? 126.411 141.511 132.144 1.00 50.41  ? 256 LYS K NZ    1 
ATOM   8660 N  N     . SER C 3 257 ? 126.125 133.986 130.333 1.00 41.14  ? 257 SER K N     1 
ATOM   8661 C  CA    . SER C 3 257 ? 126.555 132.862 131.159 1.00 33.63  ? 257 SER K CA    1 
ATOM   8662 C  C     . SER C 3 257 ? 127.448 131.905 130.383 1.00 39.00  ? 257 SER K C     1 
ATOM   8663 O  O     . SER C 3 257 ? 128.453 131.411 130.914 1.00 46.18  ? 257 SER K O     1 
ATOM   8664 C  CB    . SER C 3 257 ? 125.339 132.126 131.709 1.00 44.67  ? 257 SER K CB    1 
ATOM   8665 O  OG    . SER C 3 257 ? 124.493 133.010 132.421 1.00 51.67  ? 257 SER K OG    1 
ATOM   8666 N  N     . LEU C 3 258 ? 127.090 131.612 129.131 1.00 37.39  ? 258 LEU K N     1 
ATOM   8667 C  CA    . LEU C 3 258 ? 127.902 130.704 128.331 1.00 29.64  ? 258 LEU K CA    1 
ATOM   8668 C  C     . LEU C 3 258 ? 129.288 131.280 128.081 1.00 38.27  ? 258 LEU K C     1 
ATOM   8669 O  O     . LEU C 3 258 ? 130.291 130.557 128.137 1.00 50.45  ? 258 LEU K O     1 
ATOM   8670 C  CB    . LEU C 3 258 ? 127.199 130.395 127.012 1.00 39.18  ? 258 LEU K CB    1 
ATOM   8671 C  CG    . LEU C 3 258 ? 125.971 129.495 127.108 1.00 42.87  ? 258 LEU K CG    1 
ATOM   8672 C  CD1   . LEU C 3 258 ? 125.443 129.177 125.730 1.00 43.71  ? 258 LEU K CD1   1 
ATOM   8673 C  CD2   . LEU C 3 258 ? 126.305 128.227 127.856 1.00 45.05  ? 258 LEU K CD2   1 
ATOM   8674 N  N     . SER C 3 259 ? 129.368 132.585 127.812 1.00 40.89  ? 259 SER K N     1 
ATOM   8675 C  CA    . SER C 3 259 ? 130.674 133.209 127.634 1.00 34.26  ? 259 SER K CA    1 
ATOM   8676 C  C     . SER C 3 259 ? 131.499 133.146 128.915 1.00 38.29  ? 259 SER K C     1 
ATOM   8677 O  O     . SER C 3 259 ? 132.715 132.920 128.866 1.00 44.92  ? 259 SER K O     1 
ATOM   8678 C  CB    . SER C 3 259 ? 130.505 134.651 127.165 1.00 41.62  ? 259 SER K CB    1 
ATOM   8679 O  OG    . SER C 3 259 ? 131.762 135.247 126.905 1.00 49.58  ? 259 SER K OG    1 
ATOM   8680 N  N     . ALA C 3 260 ? 130.861 133.338 130.072 1.00 36.97  ? 260 ALA K N     1 
ATOM   8681 C  CA    . ALA C 3 260 ? 131.594 133.241 131.334 1.00 35.08  ? 260 ALA K CA    1 
ATOM   8682 C  C     . ALA C 3 260 ? 132.137 131.834 131.562 1.00 39.57  ? 260 ALA K C     1 
ATOM   8683 O  O     . ALA C 3 260 ? 133.279 131.660 132.015 1.00 41.04  ? 260 ALA K O     1 
ATOM   8684 C  CB    . ALA C 3 260 ? 130.696 133.662 132.494 1.00 38.17  ? 260 ALA K CB    1 
ATOM   8685 N  N     . LEU C 3 261 ? 131.331 130.816 131.257 1.00 45.54  ? 261 LEU K N     1 
ATOM   8686 C  CA    . LEU C 3 261 ? 131.800 129.441 131.393 1.00 30.82  ? 261 LEU K CA    1 
ATOM   8687 C  C     . LEU C 3 261 ? 132.968 129.166 130.460 1.00 31.26  ? 261 LEU K C     1 
ATOM   8688 O  O     . LEU C 3 261 ? 133.937 128.495 130.841 1.00 47.13  ? 261 LEU K O     1 
ATOM   8689 C  CB    . LEU C 3 261 ? 130.660 128.468 131.118 1.00 33.49  ? 261 LEU K CB    1 
ATOM   8690 C  CG    . LEU C 3 261 ? 131.004 126.991 131.238 1.00 36.13  ? 261 LEU K CG    1 
ATOM   8691 C  CD1   . LEU C 3 261 ? 131.622 126.711 132.585 1.00 38.59  ? 261 LEU K CD1   1 
ATOM   8692 C  CD2   . LEU C 3 261 ? 129.759 126.163 131.041 1.00 41.02  ? 261 LEU K CD2   1 
ATOM   8693 N  N     . GLY C 3 262 ? 132.889 129.670 129.230 1.00 28.06  ? 262 GLY K N     1 
ATOM   8694 C  CA    . GLY C 3 262 ? 134.005 129.520 128.316 1.00 36.84  ? 262 GLY K CA    1 
ATOM   8695 C  C     . GLY C 3 262 ? 135.267 130.172 128.839 1.00 35.54  ? 262 GLY K C     1 
ATOM   8696 O  O     . GLY C 3 262 ? 136.362 129.623 128.706 1.00 41.28  ? 262 GLY K O     1 
ATOM   8697 N  N     . ASN C 3 263 ? 135.132 131.356 129.434 1.00 38.79  ? 263 ASN K N     1 
ATOM   8698 C  CA    . ASN C 3 263 ? 136.292 132.034 129.999 1.00 40.10  ? 263 ASN K CA    1 
ATOM   8699 C  C     . ASN C 3 263 ? 136.922 131.207 131.110 1.00 40.46  ? 263 ASN K C     1 
ATOM   8700 O  O     . ASN C 3 263 ? 138.149 131.070 131.171 1.00 42.62  ? 263 ASN K O     1 
ATOM   8701 C  CB    . ASN C 3 263 ? 135.887 133.409 130.525 1.00 43.75  ? 263 ASN K CB    1 
ATOM   8702 C  CG    . ASN C 3 263 ? 135.753 134.433 129.426 1.00 46.52  ? 263 ASN K CG    1 
ATOM   8703 O  OD1   . ASN C 3 263 ? 136.411 134.340 128.394 1.00 51.17  ? 263 ASN K OD1   1 
ATOM   8704 N  ND2   . ASN C 3 263 ? 134.899 135.421 129.642 1.00 40.73  ? 263 ASN K ND2   1 
ATOM   8705 N  N     . VAL C 3 264 ? 136.097 130.640 131.993 1.00 51.54  ? 264 VAL K N     1 
ATOM   8706 C  CA    . VAL C 3 264 ? 136.634 129.835 133.091 1.00 35.69  ? 264 VAL K CA    1 
ATOM   8707 C  C     . VAL C 3 264 ? 137.360 128.607 132.552 1.00 39.34  ? 264 VAL K C     1 
ATOM   8708 O  O     . VAL C 3 264 ? 138.463 128.267 133.000 1.00 45.12  ? 264 VAL K O     1 
ATOM   8709 C  CB    . VAL C 3 264 ? 135.516 129.441 134.070 1.00 39.05  ? 264 VAL K CB    1 
ATOM   8710 C  CG1   . VAL C 3 264 ? 136.061 128.525 135.137 1.00 36.93  ? 264 VAL K CG1   1 
ATOM   8711 C  CG2   . VAL C 3 264 ? 134.911 130.674 134.697 1.00 46.54  ? 264 VAL K CG2   1 
ATOM   8712 N  N     . ILE C 3 265 ? 136.753 127.922 131.579 1.00 39.30  ? 265 ILE K N     1 
ATOM   8713 C  CA    . ILE C 3 265 ? 137.364 126.710 131.041 1.00 26.05  ? 265 ILE K CA    1 
ATOM   8714 C  C     . ILE C 3 265 ? 138.667 127.031 130.318 1.00 36.34  ? 265 ILE K C     1 
ATOM   8715 O  O     . ILE C 3 265 ? 139.656 126.299 130.443 1.00 49.62  ? 265 ILE K O     1 
ATOM   8716 C  CB    . ILE C 3 265 ? 136.375 125.969 130.127 1.00 23.19  ? 265 ILE K CB    1 
ATOM   8717 C  CG1   . ILE C 3 265 ? 135.187 125.468 130.939 1.00 35.65  ? 265 ILE K CG1   1 
ATOM   8718 C  CG2   . ILE C 3 265 ? 137.046 124.805 129.463 1.00 34.30  ? 265 ILE K CG2   1 
ATOM   8719 C  CD1   . ILE C 3 265 ? 134.149 124.757 130.116 1.00 40.99  ? 265 ILE K CD1   1 
ATOM   8720 N  N     . SER C 3 266 ? 138.695 128.123 129.554 1.00 42.37  ? 266 SER K N     1 
ATOM   8721 C  CA    . SER C 3 266 ? 139.926 128.517 128.877 1.00 35.56  ? 266 SER K CA    1 
ATOM   8722 C  C     . SER C 3 266 ? 141.016 128.877 129.876 1.00 35.99  ? 266 SER K C     1 
ATOM   8723 O  O     . SER C 3 266 ? 142.184 128.522 129.685 1.00 44.24  ? 266 SER K O     1 
ATOM   8724 C  CB    . SER C 3 266 ? 139.656 129.687 127.935 1.00 45.81  ? 266 SER K CB    1 
ATOM   8725 O  OG    . SER C 3 266 ? 140.865 130.206 127.414 1.00 53.44  ? 266 SER K OG    1 
ATOM   8726 N  N     . ALA C 3 267 ? 140.656 129.583 130.948 1.00 40.07  ? 267 ALA K N     1 
ATOM   8727 C  CA    . ALA C 3 267 ? 141.642 129.921 131.966 1.00 40.93  ? 267 ALA K CA    1 
ATOM   8728 C  C     . ALA C 3 267 ? 142.209 128.669 132.612 1.00 44.82  ? 267 ALA K C     1 
ATOM   8729 O  O     . ALA C 3 267 ? 143.413 128.588 132.879 1.00 49.06  ? 267 ALA K O     1 
ATOM   8730 C  CB    . ALA C 3 267 ? 141.017 130.833 133.019 1.00 46.83  ? 267 ALA K CB    1 
ATOM   8731 N  N     . LEU C 3 268 ? 141.354 127.683 132.883 1.00 47.15  ? 268 LEU K N     1 
ATOM   8732 C  CA    . LEU C 3 268 ? 141.837 126.437 133.466 1.00 41.07  ? 268 LEU K CA    1 
ATOM   8733 C  C     . LEU C 3 268 ? 142.759 125.694 132.508 1.00 42.36  ? 268 LEU K C     1 
ATOM   8734 O  O     . LEU C 3 268 ? 143.803 125.178 132.919 1.00 46.39  ? 268 LEU K O     1 
ATOM   8735 C  CB    . LEU C 3 268 ? 140.655 125.557 133.862 1.00 37.18  ? 268 LEU K CB    1 
ATOM   8736 C  CG    . LEU C 3 268 ? 140.210 125.629 135.317 1.00 40.58  ? 268 LEU K CG    1 
ATOM   8737 C  CD1   . LEU C 3 268 ? 139.091 124.644 135.568 1.00 45.91  ? 268 LEU K CD1   1 
ATOM   8738 C  CD2   . LEU C 3 268 ? 141.378 125.367 136.239 1.00 45.71  ? 268 LEU K CD2   1 
ATOM   8739 N  N     . ALA C 3 269 ? 142.395 125.636 131.227 1.00 44.12  ? 269 ALA K N     1 
ATOM   8740 C  CA    . ALA C 3 269 ? 143.185 124.867 130.271 1.00 39.05  ? 269 ALA K CA    1 
ATOM   8741 C  C     . ALA C 3 269 ? 144.521 125.529 129.960 1.00 40.80  ? 269 ALA K C     1 
ATOM   8742 O  O     . ALA C 3 269 ? 145.509 124.831 129.714 1.00 45.49  ? 269 ALA K O     1 
ATOM   8743 C  CB    . ALA C 3 269 ? 142.391 124.655 128.984 1.00 42.89  ? 269 ALA K CB    1 
ATOM   8744 N  N     . GLU C 3 270 ? 144.580 126.857 129.960 1.00 46.75  ? 270 GLU K N     1 
ATOM   8745 C  CA    . GLU C 3 270 ? 145.813 127.551 129.614 1.00 44.12  ? 270 GLU K CA    1 
ATOM   8746 C  C     . GLU C 3 270 ? 146.770 127.693 130.786 1.00 48.73  ? 270 GLU K C     1 
ATOM   8747 O  O     . GLU C 3 270 ? 147.843 128.278 130.617 1.00 52.71  ? 270 GLU K O     1 
ATOM   8748 C  CB    . GLU C 3 270 ? 145.496 128.936 129.046 1.00 51.47  ? 270 GLU K CB    1 
ATOM   8749 C  CG    . GLU C 3 270 ? 144.790 128.912 127.704 1.00 57.04  ? 270 GLU K CG    1 
ATOM   8750 C  CD    . GLU C 3 270 ? 144.581 130.300 127.134 1.00 60.01  ? 270 GLU K CD    1 
ATOM   8751 O  OE1   . GLU C 3 270 ? 145.134 131.266 127.702 1.00 59.07  ? 270 GLU K OE1   1 
ATOM   8752 O  OE2   . GLU C 3 270 ? 143.863 130.426 126.120 1.00 59.25  ? 270 GLU K OE2   1 
ATOM   8753 N  N     . GLY C 3 271 ? 146.419 127.179 131.958 1.00 49.58  ? 271 GLY K N     1 
ATOM   8754 C  CA    . GLY C 3 271 ? 147.281 127.305 133.119 1.00 47.35  ? 271 GLY K CA    1 
ATOM   8755 C  C     . GLY C 3 271 ? 147.429 128.722 133.624 1.00 50.47  ? 271 GLY K C     1 
ATOM   8756 O  O     . GLY C 3 271 ? 148.534 129.128 134.003 1.00 53.22  ? 271 GLY K O     1 
ATOM   8757 N  N     . SER C 3 272 ? 146.343 129.486 133.640 1.00 59.30  ? 272 SER K N     1 
ATOM   8758 C  CA    . SER C 3 272 ? 146.390 130.865 134.096 1.00 54.69  ? 272 SER K CA    1 
ATOM   8759 C  C     . SER C 3 272 ? 146.490 130.927 135.614 1.00 50.98  ? 272 SER K C     1 
ATOM   8760 O  O     . SER C 3 272 ? 145.949 130.081 136.330 1.00 52.23  ? 272 SER K O     1 
ATOM   8761 C  CB    . SER C 3 272 ? 145.154 131.626 133.617 1.00 55.45  ? 272 SER K CB    1 
ATOM   8762 O  OG    . SER C 3 272 ? 145.177 132.968 134.066 1.00 62.33  ? 272 SER K OG    1 
ATOM   8763 N  N     . THR C 3 273 ? 147.204 131.943 136.101 1.00 51.66  ? 273 THR K N     1 
ATOM   8764 C  CA    . THR C 3 273 ? 147.350 132.126 137.541 1.00 52.84  ? 273 THR K CA    1 
ATOM   8765 C  C     . THR C 3 273 ? 146.007 132.405 138.205 1.00 55.84  ? 273 THR K C     1 
ATOM   8766 O  O     . THR C 3 273 ? 145.726 131.891 139.293 1.00 59.32  ? 273 THR K O     1 
ATOM   8767 C  CB    . THR C 3 273 ? 148.332 133.261 137.825 1.00 55.76  ? 273 THR K CB    1 
ATOM   8768 O  OG1   . THR C 3 273 ? 149.610 132.941 137.261 1.00 55.99  ? 273 THR K OG1   1 
ATOM   8769 C  CG2   . THR C 3 273 ? 148.488 133.471 139.321 1.00 55.14  ? 273 THR K CG2   1 
ATOM   8770 N  N     . TYR C 3 274 ? 145.163 133.209 137.566 1.00 53.22  ? 274 TYR K N     1 
ATOM   8771 C  CA    . TYR C 3 274 ? 143.861 133.576 138.103 1.00 47.21  ? 274 TYR K CA    1 
ATOM   8772 C  C     . TYR C 3 274 ? 142.758 133.018 137.218 1.00 47.72  ? 274 TYR K C     1 
ATOM   8773 O  O     . TYR C 3 274 ? 142.782 133.203 135.999 1.00 52.82  ? 274 TYR K O     1 
ATOM   8774 C  CB    . TYR C 3 274 ? 143.724 135.094 138.213 1.00 49.21  ? 274 TYR K CB    1 
ATOM   8775 C  CG    . TYR C 3 274 ? 142.348 135.550 138.631 1.00 52.60  ? 274 TYR K CG    1 
ATOM   8776 C  CD1   . TYR C 3 274 ? 141.955 135.500 139.958 1.00 53.85  ? 274 TYR K CD1   1 
ATOM   8777 C  CD2   . TYR C 3 274 ? 141.445 136.038 137.702 1.00 48.04  ? 274 TYR K CD2   1 
ATOM   8778 C  CE1   . TYR C 3 274 ? 140.700 135.918 140.345 1.00 51.46  ? 274 TYR K CE1   1 
ATOM   8779 C  CE2   . TYR C 3 274 ? 140.190 136.454 138.079 1.00 47.70  ? 274 TYR K CE2   1 
ATOM   8780 C  CZ    . TYR C 3 274 ? 139.824 136.395 139.402 1.00 51.72  ? 274 TYR K CZ    1 
ATOM   8781 O  OH    . TYR C 3 274 ? 138.571 136.812 139.780 1.00 57.45  ? 274 TYR K OH    1 
ATOM   8782 N  N     . VAL C 3 275 ? 141.795 132.346 137.834 1.00 45.00  ? 275 VAL K N     1 
ATOM   8783 C  CA    . VAL C 3 275 ? 140.639 131.770 137.153 1.00 44.62  ? 275 VAL K CA    1 
ATOM   8784 C  C     . VAL C 3 275 ? 139.398 132.529 137.609 1.00 46.18  ? 275 VAL K C     1 
ATOM   8785 O  O     . VAL C 3 275 ? 139.089 132.530 138.807 1.00 51.78  ? 275 VAL K O     1 
ATOM   8786 C  CB    . VAL C 3 275 ? 140.502 130.269 137.442 1.00 44.23  ? 275 VAL K CB    1 
ATOM   8787 C  CG1   . VAL C 3 275 ? 139.554 129.634 136.450 1.00 45.72  ? 275 VAL K CG1   1 
ATOM   8788 C  CG2   . VAL C 3 275 ? 141.854 129.599 137.385 1.00 48.51  ? 275 VAL K CG2   1 
ATOM   8789 N  N     . PRO C 3 276 ? 138.663 133.181 136.709 1.00 43.53  ? 276 PRO K N     1 
ATOM   8790 C  CA    . PRO C 3 276 ? 137.528 134.033 137.116 1.00 42.35  ? 276 PRO K CA    1 
ATOM   8791 C  C     . PRO C 3 276 ? 136.280 133.236 137.473 1.00 45.97  ? 276 PRO K C     1 
ATOM   8792 O  O     . PRO C 3 276 ? 135.288 133.193 136.747 1.00 51.42  ? 276 PRO K O     1 
ATOM   8793 C  CB    . PRO C 3 276 ? 137.327 134.914 135.882 1.00 39.63  ? 276 PRO K CB    1 
ATOM   8794 C  CG    . PRO C 3 276 ? 137.748 134.070 134.762 1.00 39.31  ? 276 PRO K CG    1 
ATOM   8795 C  CD    . PRO C 3 276 ? 138.872 133.209 135.254 1.00 42.51  ? 276 PRO K CD    1 
ATOM   8796 N  N     . TYR C 3 277 ? 136.311 132.597 138.640 1.00 42.99  ? 277 TYR K N     1 
ATOM   8797 C  CA    . TYR C 3 277 ? 135.176 131.792 139.068 1.00 40.27  ? 277 TYR K CA    1 
ATOM   8798 C  C     . TYR C 3 277 ? 134.001 132.637 139.535 1.00 41.51  ? 277 TYR K C     1 
ATOM   8799 O  O     . TYR C 3 277 ? 132.885 132.120 139.629 1.00 53.37  ? 277 TYR K O     1 
ATOM   8800 C  CB    . TYR C 3 277 ? 135.591 130.851 140.195 1.00 43.50  ? 277 TYR K CB    1 
ATOM   8801 C  CG    . TYR C 3 277 ? 136.395 129.652 139.761 1.00 40.09  ? 277 TYR K CG    1 
ATOM   8802 C  CD1   . TYR C 3 277 ? 135.860 128.704 138.915 1.00 46.32  ? 277 TYR K CD1   1 
ATOM   8803 C  CD2   . TYR C 3 277 ? 137.684 129.462 140.221 1.00 38.98  ? 277 TYR K CD2   1 
ATOM   8804 C  CE1   . TYR C 3 277 ? 136.589 127.609 138.530 1.00 47.29  ? 277 TYR K CE1   1 
ATOM   8805 C  CE2   . TYR C 3 277 ? 138.420 128.372 139.839 1.00 39.81  ? 277 TYR K CE2   1 
ATOM   8806 C  CZ    . TYR C 3 277 ? 137.870 127.448 138.995 1.00 44.77  ? 277 TYR K CZ    1 
ATOM   8807 O  OH    . TYR C 3 277 ? 138.609 126.355 138.613 1.00 51.34  ? 277 TYR K OH    1 
ATOM   8808 N  N     . ARG C 3 278 ? 134.219 133.916 139.830 1.00 43.86  ? 278 ARG K N     1 
ATOM   8809 C  CA    . ARG C 3 278 ? 133.209 134.750 140.464 1.00 44.62  ? 278 ARG K CA    1 
ATOM   8810 C  C     . ARG C 3 278 ? 132.484 135.660 139.483 1.00 51.78  ? 278 ARG K C     1 
ATOM   8811 O  O     . ARG C 3 278 ? 131.768 136.570 139.910 1.00 56.54  ? 278 ARG K O     1 
ATOM   8812 C  CB    . ARG C 3 278 ? 133.837 135.582 141.579 1.00 38.62  ? 278 ARG K CB    1 
ATOM   8813 C  CG    . ARG C 3 278 ? 134.531 134.765 142.639 1.00 50.53  ? 278 ARG K CG    1 
ATOM   8814 C  CD    . ARG C 3 278 ? 135.163 135.659 143.681 1.00 50.81  ? 278 ARG K CD    1 
ATOM   8815 N  NE    . ARG C 3 278 ? 134.340 135.762 144.878 1.00 50.52  ? 278 ARG K NE    1 
ATOM   8816 C  CZ    . ARG C 3 278 ? 134.642 135.210 146.043 1.00 47.90  ? 278 ARG K CZ    1 
ATOM   8817 N  NH1   . ARG C 3 278 ? 135.743 134.498 146.205 1.00 44.11  ? 278 ARG K NH1   1 
ATOM   8818 N  NH2   . ARG C 3 278 ? 133.817 135.375 147.072 1.00 50.51  ? 278 ARG K NH2   1 
ATOM   8819 N  N     . ASP C 3 279 ? 132.652 135.444 138.185 1.00 52.82  ? 279 ASP K N     1 
ATOM   8820 C  CA    . ASP C 3 279 ? 131.977 136.262 137.190 1.00 49.78  ? 279 ASP K CA    1 
ATOM   8821 C  C     . ASP C 3 279 ? 130.608 135.722 136.813 1.00 51.75  ? 279 ASP K C     1 
ATOM   8822 O  O     . ASP C 3 279 ? 129.946 136.307 135.951 1.00 61.19  ? 279 ASP K O     1 
ATOM   8823 C  CB    . ASP C 3 279 ? 132.841 136.392 135.936 1.00 55.59  ? 279 ASP K CB    1 
ATOM   8824 C  CG    . ASP C 3 279 ? 133.920 137.440 136.084 1.00 63.14  ? 279 ASP K CG    1 
ATOM   8825 O  OD1   . ASP C 3 279 ? 133.989 138.074 137.156 1.00 66.47  ? 279 ASP K OD1   1 
ATOM   8826 O  OD2   . ASP C 3 279 ? 134.702 137.630 135.129 1.00 61.31  ? 279 ASP K OD2   1 
ATOM   8827 N  N     . SER C 3 280 ? 130.169 134.630 137.429 1.00 45.86  ? 280 SER K N     1 
ATOM   8828 C  CA    . SER C 3 280 ? 128.839 134.101 137.176 1.00 47.36  ? 280 SER K CA    1 
ATOM   8829 C  C     . SER C 3 280 ? 128.434 133.209 138.338 1.00 54.60  ? 280 SER K C     1 
ATOM   8830 O  O     . SER C 3 280 ? 129.278 132.723 139.095 1.00 57.37  ? 280 SER K O     1 
ATOM   8831 C  CB    . SER C 3 280 ? 128.782 133.332 135.856 1.00 54.87  ? 280 SER K CB    1 
ATOM   8832 O  OG    . SER C 3 280 ? 129.818 132.375 135.785 1.00 66.62  ? 280 SER K OG    1 
ATOM   8833 N  N     . LYS C 3 281 ? 127.123 133.004 138.469 1.00 58.31  ? 281 LYS K N     1 
ATOM   8834 C  CA    . LYS C 3 281 ? 126.607 132.138 139.524 1.00 54.80  ? 281 LYS K CA    1 
ATOM   8835 C  C     . LYS C 3 281 ? 127.038 130.694 139.318 1.00 56.23  ? 281 LYS K C     1 
ATOM   8836 O  O     . LYS C 3 281 ? 127.443 130.018 140.270 1.00 63.85  ? 281 LYS K O     1 
ATOM   8837 C  CB    . LYS C 3 281 ? 125.085 132.228 139.576 1.00 55.05  ? 281 LYS K CB    1 
ATOM   8838 C  CG    . LYS C 3 281 ? 124.545 133.560 140.043 1.00 55.36  ? 281 LYS K CG    1 
ATOM   8839 C  CD    . LYS C 3 281 ? 124.529 133.648 141.549 1.00 54.89  ? 281 LYS K CD    1 
ATOM   8840 C  CE    . LYS C 3 281 ? 123.837 134.914 142.010 1.00 59.34  ? 281 LYS K CE    1 
ATOM   8841 N  NZ    . LYS C 3 281 ? 122.501 135.071 141.381 1.00 58.07  ? 281 LYS K NZ    1 
ATOM   8842 N  N     . MET C 3 282 ? 126.962 130.203 138.081 1.00 50.96  ? 282 MET K N     1 
ATOM   8843 C  CA    . MET C 3 282 ? 127.208 128.789 137.822 1.00 53.24  ? 282 MET K CA    1 
ATOM   8844 C  C     . MET C 3 282 ? 128.660 128.413 138.085 1.00 56.26  ? 282 MET K C     1 
ATOM   8845 O  O     . MET C 3 282 ? 128.938 127.414 138.758 1.00 63.84  ? 282 MET K O     1 
ATOM   8846 C  CB    . MET C 3 282 ? 126.811 128.448 136.388 1.00 56.40  ? 282 MET K CB    1 
ATOM   8847 C  CG    . MET C 3 282 ? 127.501 127.230 135.824 1.00 57.21  ? 282 MET K CG    1 
ATOM   8848 S  SD    . MET C 3 282 ? 126.711 126.685 134.310 1.00 76.03  ? 282 MET K SD    1 
ATOM   8849 C  CE    . MET C 3 282 ? 125.220 125.960 134.977 1.00 63.32  ? 282 MET K CE    1 
ATOM   8850 N  N     . THR C 3 283 ? 129.603 129.199 137.563 1.00 43.27  ? 283 THR K N     1 
ATOM   8851 C  CA    . THR C 3 283 ? 131.014 128.877 137.749 1.00 41.03  ? 283 THR K CA    1 
ATOM   8852 C  C     . THR C 3 283 ? 131.429 128.969 139.210 1.00 50.09  ? 283 THR K C     1 
ATOM   8853 O  O     . THR C 3 283 ? 132.355 128.271 139.634 1.00 53.62  ? 283 THR K O     1 
ATOM   8854 C  CB    . THR C 3 283 ? 131.881 129.794 136.891 1.00 43.21  ? 283 THR K CB    1 
ATOM   8855 O  OG1   . THR C 3 283 ? 131.758 131.144 137.353 1.00 50.23  ? 283 THR K OG1   1 
ATOM   8856 C  CG2   . THR C 3 283 ? 131.454 129.717 135.445 1.00 48.14  ? 283 THR K CG2   1 
ATOM   8857 N  N     . ARG C 3 284 ? 130.772 129.831 139.986 1.00 51.66  ? 284 ARG K N     1 
ATOM   8858 C  CA    . ARG C 3 284 ? 131.039 129.898 141.418 1.00 45.81  ? 284 ARG K CA    1 
ATOM   8859 C  C     . ARG C 3 284 ? 130.641 128.605 142.119 1.00 48.67  ? 284 ARG K C     1 
ATOM   8860 O  O     . ARG C 3 284 ? 131.355 128.128 143.008 1.00 57.25  ? 284 ARG K O     1 
ATOM   8861 C  CB    . ARG C 3 284 ? 130.293 131.082 142.023 1.00 46.59  ? 284 ARG K CB    1 
ATOM   8862 C  CG    . ARG C 3 284 ? 130.460 131.224 143.511 1.00 51.41  ? 284 ARG K CG    1 
ATOM   8863 C  CD    . ARG C 3 284 ? 131.593 132.149 143.849 1.00 49.80  ? 284 ARG K CD    1 
ATOM   8864 N  NE    . ARG C 3 284 ? 131.520 132.589 145.234 1.00 51.33  ? 284 ARG K NE    1 
ATOM   8865 C  CZ    . ARG C 3 284 ? 132.327 132.165 146.195 1.00 55.81  ? 284 ARG K CZ    1 
ATOM   8866 N  NH1   . ARG C 3 284 ? 133.289 131.292 145.954 1.00 51.08  ? 284 ARG K NH1   1 
ATOM   8867 N  NH2   . ARG C 3 284 ? 132.168 132.635 147.428 1.00 57.53  ? 284 ARG K NH2   1 
ATOM   8868 N  N     . ILE C 3 285 ? 129.499 128.030 141.739 1.00 38.25  ? 285 ILE K N     1 
ATOM   8869 C  CA    . ILE C 3 285 ? 129.026 126.804 142.376 1.00 38.60  ? 285 ILE K CA    1 
ATOM   8870 C  C     . ILE C 3 285 ? 130.002 125.662 142.136 1.00 45.82  ? 285 ILE K C     1 
ATOM   8871 O  O     . ILE C 3 285 ? 130.305 124.882 143.047 1.00 53.72  ? 285 ILE K O     1 
ATOM   8872 C  CB    . ILE C 3 285 ? 127.616 126.448 141.873 1.00 38.23  ? 285 ILE K CB    1 
ATOM   8873 C  CG1   . ILE C 3 285 ? 126.644 127.589 142.146 1.00 43.71  ? 285 ILE K CG1   1 
ATOM   8874 C  CG2   . ILE C 3 285 ? 127.125 125.174 142.521 1.00 40.65  ? 285 ILE K CG2   1 
ATOM   8875 C  CD1   . ILE C 3 285 ? 125.277 127.353 141.582 1.00 44.14  ? 285 ILE K CD1   1 
ATOM   8876 N  N     . LEU C 3 286 ? 130.513 125.545 140.912 1.00 46.67  ? 286 LEU K N     1 
ATOM   8877 C  CA    . LEU C 3 286 ? 131.364 124.429 140.523 1.00 40.23  ? 286 LEU K CA    1 
ATOM   8878 C  C     . LEU C 3 286 ? 132.842 124.706 140.742 1.00 47.25  ? 286 LEU K C     1 
ATOM   8879 O  O     . LEU C 3 286 ? 133.682 124.134 140.037 1.00 60.06  ? 286 LEU K O     1 
ATOM   8880 C  CB    . LEU C 3 286 ? 131.113 124.063 139.062 1.00 44.45  ? 286 LEU K CB    1 
ATOM   8881 C  CG    . LEU C 3 286 ? 129.674 123.819 138.624 1.00 45.42  ? 286 LEU K CG    1 
ATOM   8882 C  CD1   . LEU C 3 286 ? 129.631 123.475 137.156 1.00 48.52  ? 286 LEU K CD1   1 
ATOM   8883 C  CD2   . LEU C 3 286 ? 129.057 122.711 139.445 1.00 49.04  ? 286 LEU K CD2   1 
ATOM   8884 N  N     . GLN C 3 287 ? 133.188 125.574 141.692 1.00 50.96  ? 287 GLN K N     1 
ATOM   8885 C  CA    . GLN C 3 287 ? 134.593 125.891 141.917 1.00 52.53  ? 287 GLN K CA    1 
ATOM   8886 C  C     . GLN C 3 287 ? 135.375 124.667 142.372 1.00 58.06  ? 287 GLN K C     1 
ATOM   8887 O  O     . GLN C 3 287 ? 136.516 124.456 141.946 1.00 62.35  ? 287 GLN K O     1 
ATOM   8888 C  CB    . GLN C 3 287 ? 134.716 127.014 142.942 1.00 50.16  ? 287 GLN K CB    1 
ATOM   8889 C  CG    . GLN C 3 287 ? 136.099 127.612 143.028 1.00 56.42  ? 287 GLN K CG    1 
ATOM   8890 C  CD    . GLN C 3 287 ? 136.131 128.869 143.864 1.00 62.02  ? 287 GLN K CD    1 
ATOM   8891 O  OE1   . GLN C 3 287 ? 135.089 129.407 144.230 1.00 61.20  ? 287 GLN K OE1   1 
ATOM   8892 N  NE2   . GLN C 3 287 ? 137.329 129.348 144.166 1.00 60.47  ? 287 GLN K NE2   1 
ATOM   8893 N  N     . ASP C 3 288 ? 134.781 123.850 143.240 1.00 61.43  ? 288 ASP K N     1 
ATOM   8894 C  CA    . ASP C 3 288 ? 135.481 122.693 143.781 1.00 60.04  ? 288 ASP K CA    1 
ATOM   8895 C  C     . ASP C 3 288 ? 135.574 121.546 142.783 1.00 60.15  ? 288 ASP K C     1 
ATOM   8896 O  O     . ASP C 3 288 ? 136.529 120.764 142.837 1.00 64.87  ? 288 ASP K O     1 
ATOM   8897 C  CB    . ASP C 3 288 ? 134.790 122.219 145.058 1.00 64.13  ? 288 ASP K CB    1 
ATOM   8898 C  CG    . ASP C 3 288 ? 135.525 121.075 145.730 1.00 69.92  ? 288 ASP K CG    1 
ATOM   8899 O  OD1   . ASP C 3 288 ? 136.637 121.304 146.249 1.00 66.84  ? 288 ASP K OD1   1 
ATOM   8900 O  OD2   . ASP C 3 288 ? 134.989 119.947 145.740 1.00 73.26  ? 288 ASP K OD2   1 
ATOM   8901 N  N     . SER C 3 289 ? 134.612 121.426 141.871 1.00 56.63  ? 289 SER K N     1 
ATOM   8902 C  CA    . SER C 3 289 ? 134.524 120.280 140.977 1.00 54.56  ? 289 SER K CA    1 
ATOM   8903 C  C     . SER C 3 289 ? 135.034 120.570 139.572 1.00 59.27  ? 289 SER K C     1 
ATOM   8904 O  O     . SER C 3 289 ? 134.874 119.727 138.684 1.00 65.68  ? 289 SER K O     1 
ATOM   8905 C  CB    . SER C 3 289 ? 133.081 119.783 140.911 1.00 60.65  ? 289 SER K CB    1 
ATOM   8906 O  OG    . SER C 3 289 ? 132.624 119.398 142.195 1.00 63.50  ? 289 SER K OG    1 
ATOM   8907 N  N     . LEU C 3 290 ? 135.644 121.729 139.344 1.00 56.82  ? 290 LEU K N     1 
ATOM   8908 C  CA    . LEU C 3 290 ? 136.155 122.080 138.024 1.00 56.27  ? 290 LEU K CA    1 
ATOM   8909 C  C     . LEU C 3 290 ? 137.672 122.127 137.981 1.00 61.73  ? 290 LEU K C     1 
ATOM   8910 O  O     . LEU C 3 290 ? 138.284 121.467 137.133 1.00 62.93  ? 290 LEU K O     1 
ATOM   8911 C  CB    . LEU C 3 290 ? 135.575 123.428 137.580 1.00 50.37  ? 290 LEU K CB    1 
ATOM   8912 C  CG    . LEU C 3 290 ? 134.967 123.462 136.185 1.00 52.87  ? 290 LEU K CG    1 
ATOM   8913 C  CD1   . LEU C 3 290 ? 133.776 122.535 136.124 1.00 59.23  ? 290 LEU K CD1   1 
ATOM   8914 C  CD2   . LEU C 3 290 ? 134.548 124.871 135.839 1.00 54.69  ? 290 LEU K CD2   1 
ATOM   8915 N  N     . GLY C 3 291 ? 138.302 122.887 138.873 1.00 79.46  ? 291 GLY K N     1 
ATOM   8916 C  CA    . GLY C 3 291 ? 139.745 122.951 138.929 1.00 81.81  ? 291 GLY K CA    1 
ATOM   8917 C  C     . GLY C 3 291 ? 140.339 121.872 139.817 1.00 87.12  ? 291 GLY K C     1 
ATOM   8918 O  O     . GLY C 3 291 ? 139.646 121.015 140.363 1.00 86.34  ? 291 GLY K O     1 
ATOM   8919 N  N     . GLY C 3 292 ? 141.662 121.930 139.959 1.00 101.15 ? 292 GLY K N     1 
ATOM   8920 C  CA    . GLY C 3 292 ? 142.352 120.972 140.798 1.00 98.50  ? 292 GLY K CA    1 
ATOM   8921 C  C     . GLY C 3 292 ? 142.353 119.575 140.199 1.00 98.30  ? 292 GLY K C     1 
ATOM   8922 O  O     . GLY C 3 292 ? 142.239 119.383 138.985 1.00 96.22  ? 292 GLY K O     1 
ATOM   8923 N  N     . ASN C 3 293 ? 142.481 118.581 141.076 1.00 107.98 ? 293 ASN K N     1 
ATOM   8924 C  CA    . ASN C 3 293 ? 142.530 117.180 140.660 1.00 109.42 ? 293 ASN K CA    1 
ATOM   8925 C  C     . ASN C 3 293 ? 141.116 116.624 140.482 1.00 108.66 ? 293 ASN K C     1 
ATOM   8926 O  O     . ASN C 3 293 ? 140.650 115.758 141.222 1.00 108.40 ? 293 ASN K O     1 
ATOM   8927 C  CB    . ASN C 3 293 ? 143.328 116.359 141.666 1.00 109.14 ? 293 ASN K CB    1 
ATOM   8928 C  CG    . ASN C 3 293 ? 144.752 116.856 141.826 1.00 110.14 ? 293 ASN K CG    1 
ATOM   8929 O  OD1   . ASN C 3 293 ? 145.065 117.998 141.490 1.00 111.62 ? 293 ASN K OD1   1 
ATOM   8930 N  ND2   . ASN C 3 293 ? 145.624 115.997 142.341 1.00 108.21 ? 293 ASN K ND2   1 
ATOM   8931 N  N     . CYS C 3 294 ? 140.432 117.150 139.470 1.00 87.13  ? 294 CYS K N     1 
ATOM   8932 C  CA    . CYS C 3 294 ? 139.082 116.730 139.130 1.00 85.81  ? 294 CYS K CA    1 
ATOM   8933 C  C     . CYS C 3 294 ? 139.004 116.450 137.637 1.00 84.70  ? 294 CYS K C     1 
ATOM   8934 O  O     . CYS C 3 294 ? 139.634 117.144 136.834 1.00 86.67  ? 294 CYS K O     1 
ATOM   8935 C  CB    . CYS C 3 294 ? 138.053 117.796 139.520 1.00 84.79  ? 294 CYS K CB    1 
ATOM   8936 S  SG    . CYS C 3 294 ? 138.010 118.180 141.286 1.00 87.56  ? 294 CYS K SG    1 
ATOM   8937 N  N     . ARG C 3 295 ? 138.232 115.432 137.271 1.00 63.55  ? 295 ARG K N     1 
ATOM   8938 C  CA    . ARG C 3 295 ? 138.055 115.042 135.880 1.00 57.35  ? 295 ARG K CA    1 
ATOM   8939 C  C     . ARG C 3 295 ? 136.729 115.587 135.374 1.00 62.32  ? 295 ARG K C     1 
ATOM   8940 O  O     . ARG C 3 295 ? 135.669 115.242 135.906 1.00 68.16  ? 295 ARG K O     1 
ATOM   8941 C  CB    . ARG C 3 295 ? 138.103 113.524 135.731 1.00 60.71  ? 295 ARG K CB    1 
ATOM   8942 C  CG    . ARG C 3 295 ? 139.327 112.886 136.355 1.00 68.96  ? 295 ARG K CG    1 
ATOM   8943 C  CD    . ARG C 3 295 ? 139.641 111.546 135.711 1.00 70.18  ? 295 ARG K CD    1 
ATOM   8944 N  NE    . ARG C 3 295 ? 140.258 111.703 134.399 1.00 72.57  ? 295 ARG K NE    1 
ATOM   8945 C  CZ    . ARG C 3 295 ? 141.563 111.831 134.196 1.00 71.96  ? 295 ARG K CZ    1 
ATOM   8946 N  NH1   . ARG C 3 295 ? 142.423 111.824 135.201 1.00 68.61  ? 295 ARG K NH1   1 
ATOM   8947 N  NH2   . ARG C 3 295 ? 142.015 111.971 132.953 1.00 69.54  ? 295 ARG K NH2   1 
ATOM   8948 N  N     . THR C 3 296 ? 136.788 116.436 134.353 1.00 55.19  ? 296 THR K N     1 
ATOM   8949 C  CA    . THR C 3 296 ? 135.600 117.009 133.739 1.00 50.17  ? 296 THR K CA    1 
ATOM   8950 C  C     . THR C 3 296 ? 135.640 116.772 132.240 1.00 53.13  ? 296 THR K C     1 
ATOM   8951 O  O     . THR C 3 296 ? 136.677 116.970 131.602 1.00 61.88  ? 296 THR K O     1 
ATOM   8952 C  CB    . THR C 3 296 ? 135.483 118.512 134.020 1.00 53.41  ? 296 THR K CB    1 
ATOM   8953 O  OG1   . THR C 3 296 ? 136.458 119.219 133.249 1.00 55.18  ? 296 THR K OG1   1 
ATOM   8954 C  CG2   . THR C 3 296 ? 135.703 118.807 135.494 1.00 57.71  ? 296 THR K CG2   1 
ATOM   8955 N  N     . THR C 3 297 ? 134.513 116.341 131.683 1.00 41.97  ? 297 THR K N     1 
ATOM   8956 C  CA    . THR C 3 297 ? 134.372 116.135 130.252 1.00 41.89  ? 297 THR K CA    1 
ATOM   8957 C  C     . THR C 3 297 ? 133.209 116.964 129.731 1.00 49.06  ? 297 THR K C     1 
ATOM   8958 O  O     . THR C 3 297 ? 132.222 117.188 130.435 1.00 58.53  ? 297 THR K O     1 
ATOM   8959 C  CB    . THR C 3 297 ? 134.139 114.663 129.907 1.00 45.12  ? 297 THR K CB    1 
ATOM   8960 O  OG1   . THR C 3 297 ? 132.827 114.276 130.322 1.00 51.72  ? 297 THR K OG1   1 
ATOM   8961 C  CG2   . THR C 3 297 ? 135.155 113.782 130.601 1.00 48.29  ? 297 THR K CG2   1 
ATOM   8962 N  N     . ILE C 3 298 ? 133.338 117.425 128.491 1.00 47.06  ? 298 ILE K N     1 
ATOM   8963 C  CA    . ILE C 3 298 ? 132.289 118.160 127.797 1.00 41.34  ? 298 ILE K CA    1 
ATOM   8964 C  C     . ILE C 3 298 ? 131.904 117.364 126.564 1.00 48.74  ? 298 ILE K C     1 
ATOM   8965 O  O     . ILE C 3 298 ? 132.763 117.049 125.732 1.00 60.30  ? 298 ILE K O     1 
ATOM   8966 C  CB    . ILE C 3 298 ? 132.743 119.573 127.404 1.00 47.41  ? 298 ILE K CB    1 
ATOM   8967 C  CG1   . ILE C 3 298 ? 133.326 120.308 128.606 1.00 51.74  ? 298 ILE K CG1   1 
ATOM   8968 C  CG2   . ILE C 3 298 ? 131.594 120.354 126.805 1.00 50.02  ? 298 ILE K CG2   1 
ATOM   8969 C  CD1   . ILE C 3 298 ? 133.885 121.657 128.263 1.00 49.93  ? 298 ILE K CD1   1 
ATOM   8970 N  N     . VAL C 3 299 ? 130.535 117.075 126.525 1.00 45.09  ? 299 VAL K N     1 
ATOM   8971 C  CA    . VAL C 3 299 ? 129.911 116.352 125.379 1.00 40.38  ? 299 VAL K CA    1 
ATOM   8972 C  C     . VAL C 3 299 ? 129.082 117.365 124.586 1.00 52.28  ? 299 VAL K C     1 
ATOM   8973 O  O     . VAL C 3 299 ? 128.089 117.854 125.145 1.00 61.44  ? 299 VAL K O     1 
ATOM   8974 C  CB    . VAL C 3 299 ? 128.990 115.187 125.779 1.00 39.14  ? 299 VAL K CB    1 
ATOM   8975 C  CG1   . VAL C 3 299 ? 128.293 114.572 124.576 1.00 41.51  ? 299 VAL K CG1   1 
ATOM   8976 C  CG2   . VAL C 3 299 ? 129.719 114.127 126.587 1.00 44.36  ? 299 VAL K CG2   1 
ATOM   8977 N  N     . ILE C 3 300 ? 129.527 117.686 123.310 1.00 52.84  ? 300 ILE K N     1 
ATOM   8978 C  CA    . ILE C 3 300 ? 128.765 118.622 122.493 1.00 43.77  ? 300 ILE K CA    1 
ATOM   8979 C  C     . ILE C 3 300 ? 128.093 117.838 121.378 1.00 51.09  ? 300 ILE K C     1 
ATOM   8980 O  O     . ILE C 3 300 ? 128.742 117.042 120.690 1.00 59.22  ? 300 ILE K O     1 
ATOM   8981 C  CB    . ILE C 3 300 ? 129.654 119.743 121.930 1.00 43.60  ? 300 ILE K CB    1 
ATOM   8982 C  CG1   . ILE C 3 300 ? 130.916 119.174 121.296 1.00 49.26  ? 300 ILE K CG1   1 
ATOM   8983 C  CG2   . ILE C 3 300 ? 130.036 120.709 123.024 1.00 50.60  ? 300 ILE K CG2   1 
ATOM   8984 C  CD1   . ILE C 3 300 ? 131.835 120.228 120.744 1.00 52.30  ? 300 ILE K CD1   1 
ATOM   8985 N  N     . CYS C 3 301 ? 126.793 118.047 121.213 1.00 53.31  ? 301 CYS K N     1 
ATOM   8986 C  CA    . CYS C 3 301 ? 125.992 117.308 120.250 1.00 53.60  ? 301 CYS K CA    1 
ATOM   8987 C  C     . CYS C 3 301 ? 125.584 118.224 119.106 1.00 56.37  ? 301 CYS K C     1 
ATOM   8988 O  O     . CYS C 3 301 ? 125.084 119.329 119.338 1.00 57.33  ? 301 CYS K O     1 
ATOM   8989 C  CB    . CYS C 3 301 ? 124.761 116.713 120.925 1.00 55.92  ? 301 CYS K CB    1 
ATOM   8990 S  SG    . CYS C 3 301 ? 125.144 115.789 122.418 1.00 64.07  ? 301 CYS K SG    1 
ATOM   8991 N  N     . CYS C 3 302 ? 125.793 117.762 117.877 1.00 63.81  ? 302 CYS K N     1 
ATOM   8992 C  CA    . CYS C 3 302 ? 125.508 118.535 116.679 1.00 62.76  ? 302 CYS K CA    1 
ATOM   8993 C  C     . CYS C 3 302 ? 124.699 117.687 115.708 1.00 61.98  ? 302 CYS K C     1 
ATOM   8994 O  O     . CYS C 3 302 ? 124.519 116.484 115.899 1.00 66.95  ? 302 CYS K O     1 
ATOM   8995 C  CB    . CYS C 3 302 ? 126.798 119.017 116.007 1.00 65.67  ? 302 CYS K CB    1 
ATOM   8996 S  SG    . CYS C 3 302 ? 127.920 119.912 117.091 1.00 88.22  ? 302 CYS K SG    1 
ATOM   8997 N  N     . SER C 3 303 ? 124.213 118.331 114.650 1.00 63.40  ? 303 SER K N     1 
ATOM   8998 C  CA    . SER C 3 303 ? 123.477 117.659 113.597 1.00 60.08  ? 303 SER K CA    1 
ATOM   8999 C  C     . SER C 3 303 ? 124.178 117.857 112.261 1.00 61.39  ? 303 SER K C     1 
ATOM   9000 O  O     . SER C 3 303 ? 124.752 118.922 112.017 1.00 71.06  ? 303 SER K O     1 
ATOM   9001 C  CB    . SER C 3 303 ? 122.043 118.186 113.499 1.00 60.81  ? 303 SER K CB    1 
ATOM   9002 O  OG    . SER C 3 303 ? 122.031 119.572 113.213 1.00 62.78  ? 303 SER K OG    1 
ATOM   9003 N  N     . PRO C 3 304 ? 124.154 116.859 111.380 1.00 53.63  ? 304 PRO K N     1 
ATOM   9004 C  CA    . PRO C 3 304 ? 124.839 116.975 110.087 1.00 52.37  ? 304 PRO K CA    1 
ATOM   9005 C  C     . PRO C 3 304 ? 123.981 117.515 108.954 1.00 57.70  ? 304 PRO K C     1 
ATOM   9006 O  O     . PRO C 3 304 ? 124.417 117.463 107.801 1.00 60.44  ? 304 PRO K O     1 
ATOM   9007 C  CB    . PRO C 3 304 ? 125.238 115.523 109.804 1.00 54.77  ? 304 PRO K CB    1 
ATOM   9008 C  CG    . PRO C 3 304 ? 124.223 114.699 110.519 1.00 57.14  ? 304 PRO K CG    1 
ATOM   9009 C  CD    . PRO C 3 304 ? 123.496 115.555 111.522 1.00 57.94  ? 304 PRO K CD    1 
ATOM   9010 N  N     . SER C 3 305 ? 122.788 118.018 109.244 1.00 58.77  ? 305 SER K N     1 
ATOM   9011 C  CA    . SER C 3 305 ? 121.929 118.545 108.199 1.00 55.76  ? 305 SER K CA    1 
ATOM   9012 C  C     . SER C 3 305 ? 122.503 119.833 107.631 1.00 61.56  ? 305 SER K C     1 
ATOM   9013 O  O     . SER C 3 305 ? 123.121 120.626 108.346 1.00 65.19  ? 305 SER K O     1 
ATOM   9014 C  CB    . SER C 3 305 ? 120.527 118.796 108.744 1.00 66.22  ? 305 SER K CB    1 
ATOM   9015 O  OG    . SER C 3 305 ? 119.687 119.348 107.748 1.00 72.77  ? 305 SER K OG    1 
ATOM   9016 N  N     . SER C 3 306 ? 122.305 120.035 106.330 1.00 68.20  ? 306 SER K N     1 
ATOM   9017 C  CA    . SER C 3 306 ? 122.665 121.302 105.712 1.00 62.77  ? 306 SER K CA    1 
ATOM   9018 C  C     . SER C 3 306 ? 121.798 122.444 106.211 1.00 62.30  ? 306 SER K C     1 
ATOM   9019 O  O     . SER C 3 306 ? 122.225 123.601 106.159 1.00 68.13  ? 306 SER K O     1 
ATOM   9020 C  CB    . SER C 3 306 ? 122.557 121.199 104.193 1.00 67.57  ? 306 SER K CB    1 
ATOM   9021 O  OG    . SER C 3 306 ? 122.835 122.445 103.579 1.00 70.59  ? 306 SER K OG    1 
ATOM   9022 N  N     . TYR C 3 307 ? 120.651 122.117 106.803 1.00 58.50  ? 307 TYR K N     1 
ATOM   9023 C  CA    . TYR C 3 307 ? 119.731 123.189 107.229 1.00 57.77  ? 307 TYR K CA    1 
ATOM   9024 C  C     . TYR C 3 307 ? 120.234 123.756 108.519 1.00 66.09  ? 307 TYR K C     1 
ATOM   9025 O  O     . TYR C 3 307 ? 119.829 124.877 108.866 1.00 72.00  ? 307 TYR K O     1 
ATOM   9026 C  CB    . TYR C 3 307 ? 118.394 122.463 107.339 1.00 64.41  ? 307 TYR K CB    1 
ATOM   9027 C  CG    . TYR C 3 307 ? 117.193 123.303 107.736 1.00 68.21  ? 307 TYR K CG    1 
ATOM   9028 C  CD1   . TYR C 3 307 ? 116.477 124.019 106.790 1.00 69.83  ? 307 TYR K CD1   1 
ATOM   9029 C  CD2   . TYR C 3 307 ? 116.763 123.357 109.054 1.00 66.90  ? 307 TYR K CD2   1 
ATOM   9030 C  CE1   . TYR C 3 307 ? 115.379 124.780 107.144 1.00 68.60  ? 307 TYR K CE1   1 
ATOM   9031 C  CE2   . TYR C 3 307 ? 115.666 124.114 109.422 1.00 66.88  ? 307 TYR K CE2   1 
ATOM   9032 C  CZ    . TYR C 3 307 ? 114.971 124.827 108.463 1.00 70.92  ? 307 TYR K CZ    1 
ATOM   9033 O  OH    . TYR C 3 307 ? 113.887 125.576 108.818 1.00 73.44  ? 307 TYR K OH    1 
ATOM   9034 N  N     . ASN C 3 308 ? 121.121 123.051 109.210 1.00 71.16  ? 308 ASN K N     1 
ATOM   9035 C  CA    . ASN C 3 308 ? 121.592 123.471 110.521 1.00 67.28  ? 308 ASN K CA    1 
ATOM   9036 C  C     . ASN C 3 308 ? 123.094 123.704 110.522 1.00 65.66  ? 308 ASN K C     1 
ATOM   9037 O  O     . ASN C 3 308 ? 123.791 123.257 111.437 1.00 73.57  ? 308 ASN K O     1 
ATOM   9038 C  CB    . ASN C 3 308 ? 121.234 122.427 111.578 1.00 66.73  ? 308 ASN K CB    1 
ATOM   9039 C  CG    . ASN C 3 308 ? 119.775 122.046 111.549 1.00 70.33  ? 308 ASN K CG    1 
ATOM   9040 O  OD1   . ASN C 3 308 ? 119.427 120.902 111.267 1.00 69.90  ? 308 ASN K OD1   1 
ATOM   9041 N  ND2   . ASN C 3 308 ? 118.908 123.004 111.849 1.00 69.45  ? 308 ASN K ND2   1 
ATOM   9042 N  N     . GLU C 3 309 ? 123.610 124.391 109.505 1.00 61.21  ? 309 GLU K N     1 
ATOM   9043 C  CA    . GLU C 3 309 ? 125.049 124.610 109.443 1.00 62.11  ? 309 GLU K CA    1 
ATOM   9044 C  C     . GLU C 3 309 ? 125.503 125.628 110.482 1.00 68.11  ? 309 GLU K C     1 
ATOM   9045 O  O     . GLU C 3 309 ? 126.518 125.421 111.158 1.00 70.05  ? 309 GLU K O     1 
ATOM   9046 C  CB    . GLU C 3 309 ? 125.451 125.053 108.039 1.00 64.79  ? 309 GLU K CB    1 
ATOM   9047 C  CG    . GLU C 3 309 ? 126.865 124.669 107.654 1.00 70.00  ? 309 GLU K CG    1 
ATOM   9048 C  CD    . GLU C 3 309 ? 127.850 125.804 107.851 1.00 76.86  ? 309 GLU K CD    1 
ATOM   9049 O  OE1   . GLU C 3 309 ? 127.419 126.900 108.267 1.00 76.95  ? 309 GLU K OE1   1 
ATOM   9050 O  OE2   . GLU C 3 309 ? 129.055 125.601 107.590 1.00 77.82  ? 309 GLU K OE2   1 
ATOM   9051 N  N     . SER C 3 310 ? 124.761 126.726 110.635 1.00 72.99  ? 310 SER K N     1 
ATOM   9052 C  CA    . SER C 3 310 ? 125.194 127.800 111.526 1.00 72.01  ? 310 SER K CA    1 
ATOM   9053 C  C     . SER C 3 310 ? 125.183 127.364 112.988 1.00 73.25  ? 310 SER K C     1 
ATOM   9054 O  O     . SER C 3 310 ? 126.123 127.663 113.738 1.00 75.79  ? 310 SER K O     1 
ATOM   9055 C  CB    . SER C 3 310 ? 124.309 129.027 111.326 1.00 70.41  ? 310 SER K CB    1 
ATOM   9056 O  OG    . SER C 3 310 ? 122.944 128.702 111.518 1.00 69.77  ? 310 SER K OG    1 
ATOM   9057 N  N     . GLU C 3 311 ? 124.129 126.668 113.416 1.00 70.11  ? 311 GLU K N     1 
ATOM   9058 C  CA    . GLU C 3 311 ? 124.069 126.204 114.798 1.00 69.88  ? 311 GLU K CA    1 
ATOM   9059 C  C     . GLU C 3 311 ? 125.160 125.181 115.088 1.00 72.43  ? 311 GLU K C     1 
ATOM   9060 O  O     . GLU C 3 311 ? 125.759 125.191 116.172 1.00 78.19  ? 311 GLU K O     1 
ATOM   9061 C  CB    . GLU C 3 311 ? 122.689 125.628 115.098 1.00 68.72  ? 311 GLU K CB    1 
ATOM   9062 C  CG    . GLU C 3 311 ? 121.940 125.141 113.878 1.00 71.54  ? 311 GLU K CG    1 
ATOM   9063 C  CD    . GLU C 3 311 ? 120.513 124.741 114.195 1.00 80.20  ? 311 GLU K CD    1 
ATOM   9064 O  OE1   . GLU C 3 311 ? 120.267 124.249 115.316 1.00 79.94  ? 311 GLU K OE1   1 
ATOM   9065 O  OE2   . GLU C 3 311 ? 119.636 124.920 113.324 1.00 80.08  ? 311 GLU K OE2   1 
ATOM   9066 N  N     . THR C 3 312 ? 125.430 124.289 114.133 1.00 60.68  ? 312 THR K N     1 
ATOM   9067 C  CA    . THR C 3 312 ? 126.519 123.336 114.305 1.00 60.87  ? 312 THR K CA    1 
ATOM   9068 C  C     . THR C 3 312 ? 127.856 124.054 114.422 1.00 61.47  ? 312 THR K C     1 
ATOM   9069 O  O     . THR C 3 312 ? 128.698 123.685 115.250 1.00 69.17  ? 312 THR K O     1 
ATOM   9070 C  CB    . THR C 3 312 ? 126.538 122.348 113.141 1.00 63.37  ? 312 THR K CB    1 
ATOM   9071 O  OG1   . THR C 3 312 ? 125.285 121.657 113.085 1.00 62.42  ? 312 THR K OG1   1 
ATOM   9072 C  CG2   . THR C 3 312 ? 127.650 121.335 113.317 1.00 66.69  ? 312 THR K CG2   1 
ATOM   9073 N  N     . LYS C 3 313 ? 128.063 125.088 113.608 1.00 58.65  ? 313 LYS K N     1 
ATOM   9074 C  CA    . LYS C 3 313 ? 129.292 125.866 113.698 1.00 61.50  ? 313 LYS K CA    1 
ATOM   9075 C  C     . LYS C 3 313 ? 129.426 126.527 115.062 1.00 66.66  ? 313 LYS K C     1 
ATOM   9076 O  O     . LYS C 3 313 ? 130.513 126.535 115.651 1.00 69.95  ? 313 LYS K O     1 
ATOM   9077 C  CB    . LYS C 3 313 ? 129.328 126.917 112.589 1.00 63.17  ? 313 LYS K CB    1 
ATOM   9078 C  CG    . LYS C 3 313 ? 129.543 126.354 111.197 1.00 67.14  ? 313 LYS K CG    1 
ATOM   9079 C  CD    . LYS C 3 313 ? 130.057 127.414 110.241 1.00 67.63  ? 313 LYS K CD    1 
ATOM   9080 C  CE    . LYS C 3 313 ? 131.491 127.797 110.561 1.00 70.19  ? 313 LYS K CE    1 
ATOM   9081 N  NZ    . LYS C 3 313 ? 132.407 126.625 110.493 1.00 70.87  ? 313 LYS K NZ    1 
ATOM   9082 N  N     . SER C 3 314 ? 128.332 127.087 115.580 1.00 61.04  ? 314 SER K N     1 
ATOM   9083 C  CA    . SER C 3 314 ? 128.376 127.721 116.894 1.00 55.28  ? 314 SER K CA    1 
ATOM   9084 C  C     . SER C 3 314 ? 128.711 126.713 117.988 1.00 61.89  ? 314 SER K C     1 
ATOM   9085 O  O     . SER C 3 314 ? 129.535 126.991 118.870 1.00 71.64  ? 314 SER K O     1 
ATOM   9086 C  CB    . SER C 3 314 ? 127.044 128.404 117.189 1.00 59.56  ? 314 SER K CB    1 
ATOM   9087 O  OG    . SER C 3 314 ? 126.828 129.496 116.313 1.00 67.82  ? 314 SER K OG    1 
ATOM   9088 N  N     . THR C 3 315 ? 128.081 125.536 117.950 1.00 52.79  ? 315 THR K N     1 
ATOM   9089 C  CA    . THR C 3 315 ? 128.370 124.515 118.951 1.00 45.70  ? 315 THR K CA    1 
ATOM   9090 C  C     . THR C 3 315 ? 129.824 124.067 118.882 1.00 49.20  ? 315 THR K C     1 
ATOM   9091 O  O     . THR C 3 315 ? 130.488 123.917 119.916 1.00 60.53  ? 315 THR K O     1 
ATOM   9092 C  CB    . THR C 3 315 ? 127.442 123.319 118.768 1.00 45.98  ? 315 THR K CB    1 
ATOM   9093 O  OG1   . THR C 3 315 ? 126.083 123.741 118.915 1.00 57.91  ? 315 THR K OG1   1 
ATOM   9094 C  CG2   . THR C 3 315 ? 127.745 122.254 119.798 1.00 51.17  ? 315 THR K CG2   1 
ATOM   9095 N  N     . LEU C 3 316 ? 130.339 123.852 117.670 1.00 51.22  ? 316 LEU K N     1 
ATOM   9096 C  CA    . LEU C 3 316 ? 131.725 123.423 117.533 1.00 56.14  ? 316 LEU K CA    1 
ATOM   9097 C  C     . LEU C 3 316 ? 132.683 124.503 118.011 1.00 58.29  ? 316 LEU K C     1 
ATOM   9098 O  O     . LEU C 3 316 ? 133.720 124.200 118.608 1.00 64.62  ? 316 LEU K O     1 
ATOM   9099 C  CB    . LEU C 3 316 ? 132.019 123.038 116.085 1.00 55.31  ? 316 LEU K CB    1 
ATOM   9100 C  CG    . LEU C 3 316 ? 131.323 121.774 115.584 1.00 52.78  ? 316 LEU K CG    1 
ATOM   9101 C  CD1   . LEU C 3 316 ? 131.599 121.559 114.116 1.00 56.71  ? 316 LEU K CD1   1 
ATOM   9102 C  CD2   . LEU C 3 316 ? 131.770 120.578 116.380 1.00 56.66  ? 316 LEU K CD2   1 
ATOM   9103 N  N     . LEU C 3 317 ? 132.360 125.769 117.751 1.00 54.34  ? 317 LEU K N     1 
ATOM   9104 C  CA    . LEU C 3 317 ? 133.209 126.855 118.223 1.00 52.40  ? 317 LEU K CA    1 
ATOM   9105 C  C     . LEU C 3 317 ? 133.220 126.919 119.744 1.00 52.74  ? 317 LEU K C     1 
ATOM   9106 O  O     . LEU C 3 317 ? 134.274 127.137 120.357 1.00 58.12  ? 317 LEU K O     1 
ATOM   9107 C  CB    . LEU C 3 317 ? 132.734 128.176 117.626 1.00 52.27  ? 317 LEU K CB    1 
ATOM   9108 C  CG    . LEU C 3 317 ? 133.767 129.287 117.479 1.00 56.89  ? 317 LEU K CG    1 
ATOM   9109 C  CD1   . LEU C 3 317 ? 134.947 128.802 116.661 1.00 58.28  ? 317 LEU K CD1   1 
ATOM   9110 C  CD2   . LEU C 3 317 ? 133.134 130.500 116.835 1.00 55.52  ? 317 LEU K CD2   1 
ATOM   9111 N  N     . PHE C 3 318 ? 132.060 126.726 120.374 1.00 50.02  ? 318 PHE K N     1 
ATOM   9112 C  CA    . PHE C 3 318 ? 132.021 126.693 121.832 1.00 49.24  ? 318 PHE K CA    1 
ATOM   9113 C  C     . PHE C 3 318 ? 132.844 125.537 122.379 1.00 51.15  ? 318 PHE K C     1 
ATOM   9114 O  O     . PHE C 3 318 ? 133.555 125.690 123.378 1.00 57.21  ? 318 PHE K O     1 
ATOM   9115 C  CB    . PHE C 3 318 ? 130.583 126.595 122.324 1.00 49.14  ? 318 PHE K CB    1 
ATOM   9116 C  CG    . PHE C 3 318 ? 130.466 126.253 123.778 1.00 49.87  ? 318 PHE K CG    1 
ATOM   9117 C  CD1   . PHE C 3 318 ? 130.733 127.199 124.748 1.00 53.03  ? 318 PHE K CD1   1 
ATOM   9118 C  CD2   . PHE C 3 318 ? 130.076 124.992 124.176 1.00 51.77  ? 318 PHE K CD2   1 
ATOM   9119 C  CE1   . PHE C 3 318 ? 130.620 126.888 126.081 1.00 50.97  ? 318 PHE K CE1   1 
ATOM   9120 C  CE2   . PHE C 3 318 ? 129.960 124.680 125.509 1.00 53.13  ? 318 PHE K CE2   1 
ATOM   9121 C  CZ    . PHE C 3 318 ? 130.233 125.628 126.460 1.00 50.52  ? 318 PHE K CZ    1 
ATOM   9122 N  N     . GLY C 3 319 ? 132.752 124.369 121.745 1.00 52.42  ? 319 GLY K N     1 
ATOM   9123 C  CA    . GLY C 3 319 ? 133.571 123.248 122.175 1.00 48.62  ? 319 GLY K CA    1 
ATOM   9124 C  C     . GLY C 3 319 ? 135.053 123.516 122.007 1.00 42.23  ? 319 GLY K C     1 
ATOM   9125 O  O     . GLY C 3 319 ? 135.866 123.129 122.848 1.00 48.61  ? 319 GLY K O     1 
ATOM   9126 N  N     . GLN C 3 320 ? 135.422 124.187 120.916 1.00 47.24  ? 320 GLN K N     1 
ATOM   9127 C  CA    . GLN C 3 320 ? 136.820 124.508 120.660 1.00 51.83  ? 320 GLN K CA    1 
ATOM   9128 C  C     . GLN C 3 320 ? 137.350 125.531 121.651 1.00 51.33  ? 320 GLN K C     1 
ATOM   9129 O  O     . GLN C 3 320 ? 138.549 125.545 121.943 1.00 53.94  ? 320 GLN K O     1 
ATOM   9130 C  CB    . GLN C 3 320 ? 136.976 125.027 119.232 1.00 54.15  ? 320 GLN K CB    1 
ATOM   9131 C  CG    . GLN C 3 320 ? 138.321 124.750 118.607 1.00 55.08  ? 320 GLN K CG    1 
ATOM   9132 C  CD    . GLN C 3 320 ? 138.418 123.345 118.061 1.00 60.48  ? 320 GLN K CD    1 
ATOM   9133 O  OE1   . GLN C 3 320 ? 137.407 122.668 117.883 1.00 60.48  ? 320 GLN K OE1   1 
ATOM   9134 N  NE2   . GLN C 3 320 ? 139.637 122.896 117.791 1.00 58.58  ? 320 GLN K NE2   1 
ATOM   9135 N  N     . ARG C 3 321 ? 136.476 126.399 122.161 1.00 54.92  ? 321 ARG K N     1 
ATOM   9136 C  CA    . ARG C 3 321 ? 136.897 127.380 123.156 1.00 52.16  ? 321 ARG K CA    1 
ATOM   9137 C  C     . ARG C 3 321 ? 137.533 126.711 124.368 1.00 50.62  ? 321 ARG K C     1 
ATOM   9138 O  O     . ARG C 3 321 ? 138.432 127.283 124.992 1.00 49.99  ? 321 ARG K O     1 
ATOM   9139 C  CB    . ARG C 3 321 ? 135.697 128.233 123.573 1.00 46.29  ? 321 ARG K CB    1 
ATOM   9140 C  CG    . ARG C 3 321 ? 135.931 129.155 124.752 1.00 50.37  ? 321 ARG K CG    1 
ATOM   9141 C  CD    . ARG C 3 321 ? 136.760 130.361 124.361 1.00 49.40  ? 321 ARG K CD    1 
ATOM   9142 N  NE    . ARG C 3 321 ? 136.883 131.310 125.458 1.00 50.85  ? 321 ARG K NE    1 
ATOM   9143 C  CZ    . ARG C 3 321 ? 137.915 132.123 125.630 1.00 52.19  ? 321 ARG K CZ    1 
ATOM   9144 N  NH1   . ARG C 3 321 ? 138.934 132.132 124.790 1.00 53.94  ? 321 ARG K NH1   1 
ATOM   9145 N  NH2   . ARG C 3 321 ? 137.929 132.940 126.679 1.00 50.89  ? 321 ARG K NH2   1 
ATOM   9146 N  N     . ALA C 3 322 ? 137.090 125.501 124.707 1.00 59.24  ? 322 ALA K N     1 
ATOM   9147 C  CA    . ALA C 3 322 ? 137.652 124.785 125.846 1.00 58.16  ? 322 ALA K CA    1 
ATOM   9148 C  C     . ALA C 3 322 ? 139.126 124.469 125.628 1.00 55.41  ? 322 ALA K C     1 
ATOM   9149 O  O     . ALA C 3 322 ? 139.993 124.942 126.370 1.00 58.37  ? 322 ALA K O     1 
ATOM   9150 C  CB    . ALA C 3 322 ? 136.857 123.503 126.098 1.00 60.12  ? 322 ALA K CB    1 
ATOM   9151 N  N     . LYS C 3 323 ? 139.424 123.667 124.610 1.00 62.33  ? 323 LYS K N     1 
ATOM   9152 C  CA    . LYS C 3 323 ? 140.789 123.251 124.292 1.00 63.76  ? 323 LYS K CA    1 
ATOM   9153 C  C     . LYS C 3 323 ? 141.489 122.634 125.498 1.00 67.60  ? 323 LYS K C     1 
ATOM   9154 O  O     . LYS C 3 323 ? 142.506 121.955 125.358 1.00 69.78  ? 323 LYS K O     1 
ATOM   9155 C  CB    . LYS C 3 323 ? 141.603 124.431 123.758 1.00 64.25  ? 323 LYS K CB    1 
ATOM   9156 C  CG    . LYS C 3 323 ? 142.719 124.034 122.809 1.00 68.29  ? 323 LYS K CG    1 
ATOM   9157 C  CD    . LYS C 3 323 ? 143.712 125.170 122.618 1.00 68.51  ? 323 LYS K CD    1 
ATOM   9158 C  CE    . LYS C 3 323 ? 144.589 125.356 123.843 1.00 67.45  ? 323 LYS K CE    1 
ATOM   9159 N  NZ    . LYS C 3 323 ? 145.281 124.097 124.226 1.00 66.69  ? 323 LYS K NZ    1 
HETATM 9160 P  PB    . GDP D 4 .   ? 127.976 158.196 159.837 1.00 20.43  ? 501 GDP B PB    1 
HETATM 9161 O  O1B   . GDP D 4 .   ? 127.493 157.109 160.761 1.00 20.43  ? 501 GDP B O1B   1 
HETATM 9162 O  O2B   . GDP D 4 .   ? 127.301 159.496 160.200 1.00 20.43  ? 501 GDP B O2B   1 
HETATM 9163 O  O3B   . GDP D 4 .   ? 127.684 157.824 158.415 1.00 20.43  ? 501 GDP B O3B   1 
HETATM 9164 O  O3A   . GDP D 4 .   ? 129.561 158.334 160.020 1.00 20.43  ? 501 GDP B O3A   1 
HETATM 9165 P  PA    . GDP D 4 .   ? 130.400 159.392 159.159 1.00 20.43  ? 501 GDP B PA    1 
HETATM 9166 O  O1A   . GDP D 4 .   ? 130.684 160.619 159.986 1.00 20.43  ? 501 GDP B O1A   1 
HETATM 9167 O  O2A   . GDP D 4 .   ? 129.655 159.751 157.905 1.00 20.43  ? 501 GDP B O2A   1 
HETATM 9168 O  "O5'" . GDP D 4 .   ? 131.757 158.615 158.789 1.00 20.43  ? 501 GDP B "O5'" 1 
HETATM 9169 C  "C5'" . GDP D 4 .   ? 133.025 159.137 159.174 1.00 20.43  ? 501 GDP B "C5'" 1 
HETATM 9170 C  "C4'" . GDP D 4 .   ? 133.935 159.305 157.970 1.00 20.43  ? 501 GDP B "C4'" 1 
HETATM 9171 O  "O4'" . GDP D 4 .   ? 133.393 160.330 157.139 1.00 20.43  ? 501 GDP B "O4'" 1 
HETATM 9172 C  "C3'" . GDP D 4 .   ? 135.297 159.796 158.405 1.00 20.43  ? 501 GDP B "C3'" 1 
HETATM 9173 O  "O3'" . GDP D 4 .   ? 136.293 159.269 157.523 1.00 20.43  ? 501 GDP B "O3'" 1 
HETATM 9174 C  "C2'" . GDP D 4 .   ? 135.207 161.299 158.249 1.00 20.43  ? 501 GDP B "C2'" 1 
HETATM 9175 O  "O2'" . GDP D 4 .   ? 136.491 161.867 157.977 1.00 20.43  ? 501 GDP B "O2'" 1 
HETATM 9176 C  "C1'" . GDP D 4 .   ? 134.265 161.462 157.073 1.00 20.43  ? 501 GDP B "C1'" 1 
HETATM 9177 N  N9    . GDP D 4 .   ? 133.443 162.694 157.151 1.00 20.43  ? 501 GDP B N9    1 
HETATM 9178 C  C8    . GDP D 4 .   ? 132.579 162.984 158.134 1.00 20.43  ? 501 GDP B C8    1 
HETATM 9179 N  N7    . GDP D 4 .   ? 131.967 164.171 157.913 1.00 20.43  ? 501 GDP B N7    1 
HETATM 9180 C  C5    . GDP D 4 .   ? 132.434 164.657 156.754 1.00 20.43  ? 501 GDP B C5    1 
HETATM 9181 C  C6    . GDP D 4 .   ? 132.204 165.869 155.938 1.00 20.43  ? 501 GDP B C6    1 
HETATM 9182 O  O6    . GDP D 4 .   ? 131.399 166.751 156.296 1.00 20.43  ? 501 GDP B O6    1 
HETATM 9183 N  N1    . GDP D 4 .   ? 132.889 165.996 154.803 1.00 20.43  ? 501 GDP B N1    1 
HETATM 9184 C  C2    . GDP D 4 .   ? 133.766 165.069 154.387 1.00 20.43  ? 501 GDP B C2    1 
HETATM 9185 N  N2    . GDP D 4 .   ? 134.421 165.277 153.224 1.00 20.43  ? 501 GDP B N2    1 
HETATM 9186 N  N3    . GDP D 4 .   ? 134.028 163.939 155.081 1.00 20.43  ? 501 GDP B N3    1 
HETATM 9187 C  C4    . GDP D 4 .   ? 133.403 163.678 156.252 1.00 20.43  ? 501 GDP B C4    1 
HETATM 9188 O  O01   . TA1 E 5 .   ? 137.107 179.906 144.388 1.00 74.55  ? 502 TA1 B O01   1 
HETATM 9189 C  C01   . TA1 E 5 .   ? 137.453 179.711 143.034 1.00 76.21  ? 502 TA1 B C01   1 
HETATM 9190 C  C02   . TA1 E 5 .   ? 138.810 178.881 143.087 1.00 74.77  ? 502 TA1 B C02   1 
HETATM 9191 O  O02   . TA1 E 5 .   ? 138.425 177.736 143.851 1.00 81.22  ? 502 TA1 B O02   1 
HETATM 9192 C  C03   . TA1 E 5 .   ? 138.869 177.529 145.089 1.00 77.66  ? 502 TA1 B C03   1 
HETATM 9193 O  O03   . TA1 E 5 .   ? 139.639 178.252 145.664 1.00 76.74  ? 502 TA1 B O03   1 
HETATM 9194 C  C04   . TA1 E 5 .   ? 138.305 176.295 145.680 1.00 73.86  ? 502 TA1 B C04   1 
HETATM 9195 C  C05   . TA1 E 5 .   ? 137.778 176.368 146.966 1.00 74.85  ? 502 TA1 B C05   1 
HETATM 9196 C  C06   . TA1 E 5 .   ? 137.243 175.241 147.557 1.00 74.17  ? 502 TA1 B C06   1 
HETATM 9197 C  C07   . TA1 E 5 .   ? 137.253 174.039 146.866 1.00 76.16  ? 502 TA1 B C07   1 
HETATM 9198 C  C08   . TA1 E 5 .   ? 137.763 173.956 145.583 1.00 72.44  ? 502 TA1 B C08   1 
HETATM 9199 C  C09   . TA1 E 5 .   ? 138.298 175.084 144.991 1.00 69.62  ? 502 TA1 B C09   1 
HETATM 9200 C  C10   . TA1 E 5 .   ? 139.500 178.378 141.755 1.00 69.68  ? 502 TA1 B C10   1 
HETATM 9201 C  C11   . TA1 E 5 .   ? 139.900 176.869 141.770 1.00 75.82  ? 502 TA1 B C11   1 
HETATM 9202 O  O04   . TA1 E 5 .   ? 138.700 176.099 141.836 1.00 76.30  ? 502 TA1 B O04   1 
HETATM 9203 C  C12   . TA1 E 5 .   ? 137.780 175.925 140.889 1.00 74.37  ? 502 TA1 B C12   1 
HETATM 9204 O  O05   . TA1 E 5 .   ? 137.780 176.475 139.824 1.00 72.54  ? 502 TA1 B O05   1 
HETATM 9205 C  C13   . TA1 E 5 .   ? 136.744 174.948 141.352 1.00 71.02  ? 502 TA1 B C13   1 
HETATM 9206 C  C14   . TA1 E 5 .   ? 140.970 176.409 142.767 1.00 76.73  ? 502 TA1 B C14   1 
HETATM 9207 O  O06   . TA1 E 5 .   ? 141.792 175.901 141.708 1.00 81.77  ? 502 TA1 B O06   1 
HETATM 9208 C  C15   . TA1 E 5 .   ? 140.886 176.377 140.683 1.00 77.48  ? 502 TA1 B C15   1 
HETATM 9209 C  C16   . TA1 E 5 .   ? 141.557 177.345 139.732 1.00 72.93  ? 502 TA1 B C16   1 
HETATM 9210 C  C17   . TA1 E 5 .   ? 140.944 178.729 139.678 1.00 73.57  ? 502 TA1 B C17   1 
HETATM 9211 O  O07   . TA1 E 5 .   ? 141.669 179.607 138.851 1.00 75.96  ? 502 TA1 B O07   1 
HETATM 9212 C  C18   . TA1 E 5 .   ? 140.679 179.291 141.124 1.00 71.00  ? 502 TA1 B C18   1 
HETATM 9213 C  C19   . TA1 E 5 .   ? 142.020 179.282 141.868 1.00 71.22  ? 502 TA1 B C19   1 
HETATM 9214 C  C20   . TA1 E 5 .   ? 140.302 180.777 140.893 1.00 75.91  ? 502 TA1 B C20   1 
HETATM 9215 O  O08   . TA1 E 5 .   ? 141.093 181.597 141.293 1.00 78.27  ? 502 TA1 B O08   1 
HETATM 9216 C  C21   . TA1 E 5 .   ? 139.067 181.425 140.214 1.00 78.17  ? 502 TA1 B C21   1 
HETATM 9217 O  O09   . TA1 E 5 .   ? 139.117 182.837 140.215 1.00 80.09  ? 502 TA1 B O09   1 
HETATM 9218 C  C22   . TA1 E 5 .   ? 139.355 183.531 139.097 1.00 77.78  ? 502 TA1 B C22   1 
HETATM 9219 O  O10   . TA1 E 5 .   ? 139.470 183.023 138.012 1.00 75.62  ? 502 TA1 B O10   1 
HETATM 9220 C  C23   . TA1 E 5 .   ? 139.449 184.994 139.397 1.00 74.44  ? 502 TA1 B C23   1 
HETATM 9221 C  C24   . TA1 E 5 .   ? 137.810 180.961 140.923 1.00 73.95  ? 502 TA1 B C24   1 
HETATM 9222 C  C25   . TA1 E 5 .   ? 137.019 180.100 140.229 1.00 72.89  ? 502 TA1 B C25   1 
HETATM 9223 C  C26   . TA1 E 5 .   ? 135.888 179.390 140.945 1.00 73.49  ? 502 TA1 B C26   1 
HETATM 9224 O  O11   . TA1 E 5 .   ? 135.314 178.263 140.251 1.00 81.81  ? 502 TA1 B O11   1 
HETATM 9225 C  C27   . TA1 E 5 .   ? 134.182 178.460 139.580 1.00 75.95  ? 502 TA1 B C27   1 
HETATM 9226 O  O12   . TA1 E 5 .   ? 133.633 179.521 139.482 1.00 71.74  ? 502 TA1 B O12   1 
HETATM 9227 C  C28   . TA1 E 5 .   ? 133.668 177.181 138.919 1.00 73.30  ? 502 TA1 B C28   1 
HETATM 9228 O  O13   . TA1 E 5 .   ? 132.494 177.419 138.219 1.00 73.77  ? 502 TA1 B O13   1 
HETATM 9229 C  C29   . TA1 E 5 .   ? 133.347 176.163 140.021 1.00 72.59  ? 502 TA1 B C29   1 
HETATM 9230 N  N01   . TA1 E 5 .   ? 132.460 176.817 140.948 1.00 67.34  ? 502 TA1 B N01   1 
HETATM 9231 C  C30   . TA1 E 5 .   ? 132.344 176.409 142.222 1.00 74.51  ? 502 TA1 B C30   1 
HETATM 9232 O  O14   . TA1 E 5 .   ? 132.976 175.461 142.660 1.00 82.44  ? 502 TA1 B O14   1 
HETATM 9233 C  C31   . TA1 E 5 .   ? 131.409 177.183 143.078 1.00 69.96  ? 502 TA1 B C31   1 
HETATM 9234 C  C32   . TA1 E 5 .   ? 130.058 177.187 142.769 1.00 68.48  ? 502 TA1 B C32   1 
HETATM 9235 C  C33   . TA1 E 5 .   ? 129.173 177.901 143.551 1.00 68.95  ? 502 TA1 B C33   1 
HETATM 9236 C  C34   . TA1 E 5 .   ? 129.631 178.621 144.642 1.00 73.02  ? 502 TA1 B C34   1 
HETATM 9237 C  C35   . TA1 E 5 .   ? 130.978 178.625 144.954 1.00 74.01  ? 502 TA1 B C35   1 
HETATM 9238 C  C36   . TA1 E 5 .   ? 131.864 177.908 144.173 1.00 72.17  ? 502 TA1 B C36   1 
HETATM 9239 C  C37   . TA1 E 5 .   ? 132.852 174.850 139.465 1.00 72.52  ? 502 TA1 B C37   1 
HETATM 9240 C  C38   . TA1 E 5 .   ? 133.771 173.857 139.149 1.00 72.03  ? 502 TA1 B C38   1 
HETATM 9241 C  C39   . TA1 E 5 .   ? 133.355 172.638 138.641 1.00 72.53  ? 502 TA1 B C39   1 
HETATM 9242 C  C40   . TA1 E 5 .   ? 132.006 172.392 138.444 1.00 72.76  ? 502 TA1 B C40   1 
HETATM 9243 C  C41   . TA1 E 5 .   ? 131.086 173.378 138.756 1.00 75.39  ? 502 TA1 B C41   1 
HETATM 9244 C  C42   . TA1 E 5 .   ? 131.503 174.598 139.267 1.00 75.69  ? 502 TA1 B C42   1 
HETATM 9245 C  C43   . TA1 E 5 .   ? 136.345 178.898 142.324 1.00 73.60  ? 502 TA1 B C43   1 
HETATM 9246 C  C44   . TA1 E 5 .   ? 137.234 179.673 138.810 1.00 72.79  ? 502 TA1 B C44   1 
HETATM 9247 C  C45   . TA1 E 5 .   ? 137.595 181.149 142.440 1.00 73.70  ? 502 TA1 B C45   1 
HETATM 9248 C  C46   . TA1 E 5 .   ? 136.380 182.087 142.700 1.00 71.54  ? 502 TA1 B C46   1 
HETATM 9249 C  C47   . TA1 E 5 .   ? 138.596 181.955 143.289 1.00 73.74  ? 502 TA1 B C47   1 
HETATM 9250 P  PG    . GTP F 6 .   ? 127.211 156.695 119.557 1.00 55.15  ? 501 GTP A PG    1 
HETATM 9251 O  O1G   . GTP F 6 .   ? 128.045 155.721 120.337 1.00 55.72  ? 501 GTP A O1G   1 
HETATM 9252 O  O2G   . GTP F 6 .   ? 125.759 156.352 119.746 1.00 57.33  ? 501 GTP A O2G   1 
HETATM 9253 O  O3G   . GTP F 6 .   ? 127.481 158.098 120.032 1.00 60.27  ? 501 GTP A O3G   1 
HETATM 9254 O  O3B   . GTP F 6 .   ? 127.572 156.513 118.007 1.00 47.85  ? 501 GTP A O3B   1 
HETATM 9255 P  PB    . GTP F 6 .   ? 128.078 157.724 117.093 1.00 47.00  ? 501 GTP A PB    1 
HETATM 9256 O  O1B   . GTP F 6 .   ? 127.278 158.959 117.394 1.00 56.05  ? 501 GTP A O1B   1 
HETATM 9257 O  O2B   . GTP F 6 .   ? 127.972 157.314 115.652 1.00 51.06  ? 501 GTP A O2B   1 
HETATM 9258 O  O3A   . GTP F 6 .   ? 129.602 157.936 117.535 1.00 52.38  ? 501 GTP A O3A   1 
HETATM 9259 P  PA    . GTP F 6 .   ? 130.586 158.884 116.707 1.00 51.75  ? 501 GTP A PA    1 
HETATM 9260 O  O1A   . GTP F 6 .   ? 130.853 160.124 117.514 1.00 54.30  ? 501 GTP A O1A   1 
HETATM 9261 O  O2A   . GTP F 6 .   ? 129.992 159.201 115.362 1.00 51.49  ? 501 GTP A O2A   1 
HETATM 9262 O  "O5'" . GTP F 6 .   ? 131.907 157.978 116.567 1.00 55.65  ? 501 GTP A "O5'" 1 
HETATM 9263 C  "C5'" . GTP F 6 .   ? 133.189 158.370 117.000 1.00 48.21  ? 501 GTP A "C5'" 1 
HETATM 9264 C  "C4'" . GTP F 6 .   ? 134.110 158.463 115.793 1.00 45.11  ? 501 GTP A "C4'" 1 
HETATM 9265 O  "O4'" . GTP F 6 .   ? 133.592 159.456 114.940 1.00 52.22  ? 501 GTP A "O4'" 1 
HETATM 9266 C  "C3'" . GTP F 6 .   ? 135.513 158.892 116.157 1.00 51.04  ? 501 GTP A "C3'" 1 
HETATM 9267 O  "O3'" . GTP F 6 .   ? 136.412 158.250 115.285 1.00 56.49  ? 501 GTP A "O3'" 1 
HETATM 9268 C  "C2'" . GTP F 6 .   ? 135.511 160.373 115.875 1.00 54.53  ? 501 GTP A "C2'" 1 
HETATM 9269 O  "O2'" . GTP F 6 .   ? 136.786 160.830 115.492 1.00 60.19  ? 501 GTP A "O2'" 1 
HETATM 9270 C  "C1'" . GTP F 6 .   ? 134.514 160.506 114.743 1.00 53.51  ? 501 GTP A "C1'" 1 
HETATM 9271 N  N9    . GTP F 6 .   ? 133.787 161.778 114.831 1.00 46.85  ? 501 GTP A N9    1 
HETATM 9272 C  C8    . GTP F 6 .   ? 132.963 162.146 115.854 1.00 49.60  ? 501 GTP A C8    1 
HETATM 9273 N  N7    . GTP F 6 .   ? 132.466 163.370 115.590 1.00 50.32  ? 501 GTP A N7    1 
HETATM 9274 C  C5    . GTP F 6 .   ? 132.955 163.786 114.408 1.00 51.61  ? 501 GTP A C5    1 
HETATM 9275 C  C6    . GTP F 6 .   ? 132.766 164.951 113.680 1.00 53.49  ? 501 GTP A C6    1 
HETATM 9276 O  O6    . GTP F 6 .   ? 132.038 165.841 114.101 1.00 58.70  ? 501 GTP A O6    1 
HETATM 9277 N  N1    . GTP F 6 .   ? 133.402 165.117 112.479 1.00 45.58  ? 501 GTP A N1    1 
HETATM 9278 C  C2    . GTP F 6 .   ? 134.226 164.124 112.007 1.00 48.49  ? 501 GTP A C2    1 
HETATM 9279 N  N2    . GTP F 6 .   ? 134.840 164.283 110.845 1.00 48.89  ? 501 GTP A N2    1 
HETATM 9280 N  N3    . GTP F 6 .   ? 134.408 162.968 112.731 1.00 50.62  ? 501 GTP A N3    1 
HETATM 9281 C  C4    . GTP F 6 .   ? 133.783 162.796 113.916 1.00 46.44  ? 501 GTP A C4    1 
HETATM 9282 MG MG    . MG  G 7 .   ? 126.711 160.030 119.892 1.00 42.46  ? 502 MG  A MG    1 
HETATM 9283 P  PB    . ADP H 8 .   ? 116.735 117.275 121.661 1.00 81.31  ? 501 ADP K PB    1 
HETATM 9284 O  O1B   . ADP H 8 .   ? 116.487 116.900 123.097 1.00 73.10  ? 501 ADP K O1B   1 
HETATM 9285 O  O2B   . ADP H 8 .   ? 115.535 117.862 120.962 1.00 74.79  ? 501 ADP K O2B   1 
HETATM 9286 O  O3B   . ADP H 8 .   ? 118.019 118.030 121.432 1.00 74.52  ? 501 ADP K O3B   1 
HETATM 9287 P  PA    . ADP H 8 .   ? 115.991 114.631 121.260 1.00 78.29  ? 501 ADP K PA    1 
HETATM 9288 O  O1A   . ADP H 8 .   ? 116.629 113.796 122.339 1.00 78.48  ? 501 ADP K O1A   1 
HETATM 9289 O  O2A   . ADP H 8 .   ? 114.599 115.184 121.437 1.00 73.40  ? 501 ADP K O2A   1 
HETATM 9290 O  O3A   . ADP H 8 .   ? 116.964 115.862 120.928 1.00 69.00  ? 501 ADP K O3A   1 
HETATM 9291 O  "O5'" . ADP H 8 .   ? 116.004 113.764 119.910 1.00 69.38  ? 501 ADP K "O5'" 1 
HETATM 9292 C  "C5'" . ADP H 8 .   ? 114.787 113.166 119.478 1.00 71.01  ? 501 ADP K "C5'" 1 
HETATM 9293 C  "C4'" . ADP H 8 .   ? 115.042 111.901 118.672 1.00 69.97  ? 501 ADP K "C4'" 1 
HETATM 9294 O  "O4'" . ADP H 8 .   ? 116.316 111.925 118.035 1.00 62.16  ? 501 ADP K "O4'" 1 
HETATM 9295 C  "C3'" . ADP H 8 .   ? 115.033 110.663 119.549 1.00 73.80  ? 501 ADP K "C3'" 1 
HETATM 9296 O  "O3'" . ADP H 8 .   ? 113.779 109.987 119.436 1.00 73.96  ? 501 ADP K "O3'" 1 
HETATM 9297 C  "C2'" . ADP H 8 .   ? 116.139 109.786 119.007 1.00 74.19  ? 501 ADP K "C2'" 1 
HETATM 9298 O  "O2'" . ADP H 8 .   ? 115.588 108.579 118.475 1.00 79.39  ? 501 ADP K "O2'" 1 
HETATM 9299 C  "C1'" . ADP H 8 .   ? 116.791 110.589 117.897 1.00 66.45  ? 501 ADP K "C1'" 1 
HETATM 9300 N  N9    . ADP H 8 .   ? 118.256 110.552 118.062 1.00 67.12  ? 501 ADP K N9    1 
HETATM 9301 C  C8    . ADP H 8 .   ? 118.992 111.507 118.650 1.00 72.16  ? 501 ADP K C8    1 
HETATM 9302 N  N7    . ADP H 8 .   ? 120.306 111.178 118.648 1.00 72.32  ? 501 ADP K N7    1 
HETATM 9303 C  C5    . ADP H 8 .   ? 120.418 109.984 118.047 1.00 67.02  ? 501 ADP K C5    1 
HETATM 9304 C  C6    . ADP H 8 .   ? 121.524 109.067 117.714 1.00 71.62  ? 501 ADP K C6    1 
HETATM 9305 N  N6    . ADP H 8 .   ? 122.803 109.373 118.034 1.00 72.42  ? 501 ADP K N6    1 
HETATM 9306 N  N1    . ADP H 8 .   ? 121.214 107.918 117.081 1.00 73.26  ? 501 ADP K N1    1 
HETATM 9307 C  C2    . ADP H 8 .   ? 119.948 107.607 116.761 1.00 70.75  ? 501 ADP K C2    1 
HETATM 9308 N  N3    . ADP H 8 .   ? 118.896 108.394 117.031 1.00 69.15  ? 501 ADP K N3    1 
HETATM 9309 C  C4    . ADP H 8 .   ? 119.065 109.575 117.664 1.00 65.53  ? 501 ADP K C4    1 
# 
