data_8YEM
# 
_entry.id   8YEM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8YEM         pdb_00008yem 10.2210/pdb8yem/pdb 
WWPDB D_1300045493 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YEM 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              593672467@qq.com 
_pdbx_contact_author.name_first         Yuxi 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4056-5829 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wu, C.Y.'   1 ? 
'Wang, Y.X.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Tubulin-RB3_SLD-TTL in complex with compound 9' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, C.Y.'   1 ? 
primary 'Wang, Y.X.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Detyrosinated tubulin alpha-1B chain'                                              48966.324 2 ?        ? ? ? 
2  polymer     man 'Tubulin beta chain'                                                                48391.410 2 ?        ? ? ? 
3  polymer     man Stathmin-4                                                                          16082.335 1 ?        ? ? ? 
4  polymer     man 'Tubulin--tyrosine ligase'                                                          43825.914 1 6.3.2.25 ? ? ? 
5  non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                                                         523.180   2 ?        ? ? ? 
6  non-polymer syn 'CALCIUM ION'                                                                       40.078    2 ?        ? ? ? 
7  non-polymer syn 'MAGNESIUM ION'                                                                     24.305    3 ?        ? ? ? 
8  non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                                                          443.201   2 ?        ? ? ? 
9  non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                              195.237   2 ?        ? ? ? 
10 non-polymer syn '4-(2-chloranyl-6-fluoranyl-quinazolin-4-yl)-7-methoxy-1,3-dihydroquinoxalin-2-one' 358.754   2 ?        ? ? ? 
11 non-polymer syn 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                      505.208   1 ?        ? ? ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        'Stathmin-like protein B3,RB3' 
# 
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 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
A,C ? 
2 'polypeptide(L)' no no 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
B,D ? 
3 'polypeptide(L)' no no 
;MEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQK
AIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE
;
;MEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQK
AIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE
;
E   ? 
4 'polypeptide(L)' no no 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHH
;
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHH
;
F   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
5  "GUANOSINE-5'-TRIPHOSPHATE"                                                         GTP   
6  'CALCIUM ION'                                                                       CA    
7  'MAGNESIUM ION'                                                                     MG    
8  "GUANOSINE-5'-DIPHOSPHATE"                                                          GDP   
9  '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                              MES   
10 '4-(2-chloranyl-6-fluoranyl-quinazolin-4-yl)-7-methoxy-1,3-dihydroquinoxalin-2-one' A1D6D 
11 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                      ACP   
# 
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   CYS n 
1 5   ILE n 
1 6   SER n 
1 7   ILE n 
1 8   HIS n 
1 9   VAL n 
1 10  GLY n 
1 11  GLN n 
1 12  ALA n 
1 13  GLY n 
1 14  VAL n 
1 15  GLN n 
1 16  ILE n 
1 17  GLY n 
1 18  ASN n 
1 19  ALA n 
1 20  CYS n 
1 21  TRP n 
1 22  GLU n 
1 23  LEU n 
1 24  TYR n 
1 25  CYS n 
1 26  LEU n 
1 27  GLU n 
1 28  HIS n 
1 29  GLY n 
1 30  ILE n 
1 31  GLN n 
1 32  PRO n 
1 33  ASP n 
1 34  GLY n 
1 35  GLN n 
1 36  MET n 
1 37  PRO n 
1 38  SER n 
1 39  ASP n 
1 40  LYS n 
1 41  THR n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  GLY n 
1 46  ASP n 
1 47  ASP n 
1 48  SER n 
1 49  PHE n 
1 50  ASN n 
1 51  THR n 
1 52  PHE n 
1 53  PHE n 
1 54  SER n 
1 55  GLU n 
1 56  THR n 
1 57  GLY n 
1 58  ALA n 
1 59  GLY n 
1 60  LYS n 
1 61  HIS n 
1 62  VAL n 
1 63  PRO n 
1 64  ARG n 
1 65  ALA n 
1 66  VAL n 
1 67  PHE n 
1 68  VAL n 
1 69  ASP n 
1 70  LEU n 
1 71  GLU n 
1 72  PRO n 
1 73  THR n 
1 74  VAL n 
1 75  ILE n 
1 76  ASP n 
1 77  GLU n 
1 78  VAL n 
1 79  ARG n 
1 80  THR n 
1 81  GLY n 
1 82  THR n 
1 83  TYR n 
1 84  ARG n 
1 85  GLN n 
1 86  LEU n 
1 87  PHE n 
1 88  HIS n 
1 89  PRO n 
1 90  GLU n 
1 91  GLN n 
1 92  LEU n 
1 93  ILE n 
1 94  THR n 
1 95  GLY n 
1 96  LYS n 
1 97  GLU n 
1 98  ASP n 
1 99  ALA n 
1 100 ALA n 
1 101 ASN n 
1 102 ASN n 
1 103 TYR n 
1 104 ALA n 
1 105 ARG n 
1 106 GLY n 
1 107 HIS n 
1 108 TYR n 
1 109 THR n 
1 110 ILE n 
1 111 GLY n 
1 112 LYS n 
1 113 GLU n 
1 114 ILE n 
1 115 ILE n 
1 116 ASP n 
1 117 LEU n 
1 118 VAL n 
1 119 LEU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 ARG n 
1 124 LYS n 
1 125 LEU n 
1 126 ALA n 
1 127 ASP n 
1 128 GLN n 
1 129 CYS n 
1 130 THR n 
1 131 GLY n 
1 132 LEU n 
1 133 GLN n 
1 134 GLY n 
1 135 PHE n 
1 136 LEU n 
1 137 VAL n 
1 138 PHE n 
1 139 HIS n 
1 140 SER n 
1 141 PHE n 
1 142 GLY n 
1 143 GLY n 
1 144 GLY n 
1 145 THR n 
1 146 GLY n 
1 147 SER n 
1 148 GLY n 
1 149 PHE n 
1 150 THR n 
1 151 SER n 
1 152 LEU n 
1 153 LEU n 
1 154 MET n 
1 155 GLU n 
1 156 ARG n 
1 157 LEU n 
1 158 SER n 
1 159 VAL n 
1 160 ASP n 
1 161 TYR n 
1 162 GLY n 
1 163 LYS n 
1 164 LYS n 
1 165 SER n 
1 166 LYS n 
1 167 LEU n 
1 168 GLU n 
1 169 PHE n 
1 170 SER n 
1 171 ILE n 
1 172 TYR n 
1 173 PRO n 
1 174 ALA n 
1 175 PRO n 
1 176 GLN n 
1 177 VAL n 
1 178 SER n 
1 179 THR n 
1 180 ALA n 
1 181 VAL n 
1 182 VAL n 
1 183 GLU n 
1 184 PRO n 
1 185 TYR n 
1 186 ASN n 
1 187 SER n 
1 188 ILE n 
1 189 LEU n 
1 190 THR n 
1 191 THR n 
1 192 HIS n 
1 193 THR n 
1 194 THR n 
1 195 LEU n 
1 196 GLU n 
1 197 HIS n 
1 198 SER n 
1 199 ASP n 
1 200 CYS n 
1 201 ALA n 
1 202 PHE n 
1 203 MET n 
1 204 VAL n 
1 205 ASP n 
1 206 ASN n 
1 207 GLU n 
1 208 ALA n 
1 209 ILE n 
1 210 TYR n 
1 211 ASP n 
1 212 ILE n 
1 213 CYS n 
1 214 ARG n 
1 215 ARG n 
1 216 ASN n 
1 217 LEU n 
1 218 ASP n 
1 219 ILE n 
1 220 GLU n 
1 221 ARG n 
1 222 PRO n 
1 223 THR n 
1 224 TYR n 
1 225 THR n 
1 226 ASN n 
1 227 LEU n 
1 228 ASN n 
1 229 ARG n 
1 230 LEU n 
1 231 ILE n 
1 232 SER n 
1 233 GLN n 
1 234 ILE n 
1 235 VAL n 
1 236 SER n 
1 237 SER n 
1 238 ILE n 
1 239 THR n 
1 240 ALA n 
1 241 SER n 
1 242 LEU n 
1 243 ARG n 
1 244 PHE n 
1 245 ASP n 
1 246 GLY n 
1 247 ALA n 
1 248 LEU n 
1 249 ASN n 
1 250 VAL n 
1 251 ASP n 
1 252 LEU n 
1 253 THR n 
1 254 GLU n 
1 255 PHE n 
1 256 GLN n 
1 257 THR n 
1 258 ASN n 
1 259 LEU n 
1 260 VAL n 
1 261 PRO n 
1 262 TYR n 
1 263 PRO n 
1 264 ARG n 
1 265 ILE n 
1 266 HIS n 
1 267 PHE n 
1 268 PRO n 
1 269 LEU n 
1 270 ALA n 
1 271 THR n 
1 272 TYR n 
1 273 ALA n 
1 274 PRO n 
1 275 VAL n 
1 276 ILE n 
1 277 SER n 
1 278 ALA n 
1 279 GLU n 
1 280 LYS n 
1 281 ALA n 
1 282 TYR n 
1 283 HIS n 
1 284 GLU n 
1 285 GLN n 
1 286 LEU n 
1 287 SER n 
1 288 VAL n 
1 289 ALA n 
1 290 GLU n 
1 291 ILE n 
1 292 THR n 
1 293 ASN n 
1 294 ALA n 
1 295 CYS n 
1 296 PHE n 
1 297 GLU n 
1 298 PRO n 
1 299 ALA n 
1 300 ASN n 
1 301 GLN n 
1 302 MET n 
1 303 VAL n 
1 304 LYS n 
1 305 CYS n 
1 306 ASP n 
1 307 PRO n 
1 308 ARG n 
1 309 HIS n 
1 310 GLY n 
1 311 LYS n 
1 312 TYR n 
1 313 MET n 
1 314 ALA n 
1 315 CYS n 
1 316 CYS n 
1 317 LEU n 
1 318 LEU n 
1 319 TYR n 
1 320 ARG n 
1 321 GLY n 
1 322 ASP n 
1 323 VAL n 
1 324 VAL n 
1 325 PRO n 
1 326 LYS n 
1 327 ASP n 
1 328 VAL n 
1 329 ASN n 
1 330 ALA n 
1 331 ALA n 
1 332 ILE n 
1 333 ALA n 
1 334 THR n 
1 335 ILE n 
1 336 LYS n 
1 337 THR n 
1 338 LYS n 
1 339 ARG n 
1 340 SER n 
1 341 ILE n 
1 342 GLN n 
1 343 PHE n 
1 344 VAL n 
1 345 ASP n 
1 346 TRP n 
1 347 CYS n 
1 348 PRO n 
1 349 THR n 
1 350 GLY n 
1 351 PHE n 
1 352 LYS n 
1 353 VAL n 
1 354 GLY n 
1 355 ILE n 
1 356 ASN n 
1 357 TYR n 
1 358 GLN n 
1 359 PRO n 
1 360 PRO n 
1 361 THR n 
1 362 VAL n 
1 363 VAL n 
1 364 PRO n 
1 365 GLY n 
1 366 GLY n 
1 367 ASP n 
1 368 LEU n 
1 369 ALA n 
1 370 LYS n 
1 371 VAL n 
1 372 GLN n 
1 373 ARG n 
1 374 ALA n 
1 375 VAL n 
1 376 CYS n 
1 377 MET n 
1 378 LEU n 
1 379 SER n 
1 380 ASN n 
1 381 THR n 
1 382 THR n 
1 383 ALA n 
1 384 ILE n 
1 385 ALA n 
1 386 GLU n 
1 387 ALA n 
1 388 TRP n 
1 389 ALA n 
1 390 ARG n 
1 391 LEU n 
1 392 ASP n 
1 393 HIS n 
1 394 LYS n 
1 395 PHE n 
1 396 ASP n 
1 397 LEU n 
1 398 MET n 
1 399 TYR n 
1 400 ALA n 
1 401 LYS n 
1 402 ARG n 
1 403 ALA n 
1 404 PHE n 
1 405 VAL n 
1 406 HIS n 
1 407 TRP n 
1 408 TYR n 
1 409 VAL n 
1 410 GLY n 
1 411 GLU n 
1 412 GLY n 
1 413 MET n 
1 414 GLU n 
1 415 GLU n 
1 416 GLY n 
1 417 GLU n 
1 418 PHE n 
1 419 SER n 
1 420 GLU n 
1 421 ALA n 
1 422 ARG n 
1 423 GLU n 
1 424 ASP n 
1 425 MET n 
1 426 ALA n 
1 427 ALA n 
1 428 LEU n 
1 429 GLU n 
1 430 LYS n 
1 431 ASP n 
1 432 TYR n 
1 433 GLU n 
1 434 GLU n 
1 435 VAL n 
1 436 GLY n 
1 437 VAL n 
1 438 ASP n 
1 439 SER n 
1 440 VAL n 
2 1   MET n 
2 2   ARG n 
2 3   GLU n 
2 4   ILE n 
2 5   VAL n 
2 6   HIS n 
2 7   ILE n 
2 8   GLN n 
2 9   ALA n 
2 10  GLY n 
2 11  GLN n 
2 12  CYS n 
2 13  GLY n 
2 14  ASN n 
2 15  GLN n 
2 16  ILE n 
2 17  GLY n 
2 18  ALA n 
2 19  LYS n 
2 20  PHE n 
2 21  TRP n 
2 22  GLU n 
2 23  VAL n 
2 24  ILE n 
2 25  SER n 
2 26  ASP n 
2 27  GLU n 
2 28  HIS n 
2 29  GLY n 
2 30  ILE n 
2 31  ASP n 
2 32  PRO n 
2 33  THR n 
2 34  GLY n 
2 35  SER n 
2 36  TYR n 
2 37  HIS n 
2 38  GLY n 
2 39  ASP n 
2 40  SER n 
2 41  ASP n 
2 42  LEU n 
2 43  GLN n 
2 44  LEU n 
2 45  GLU n 
2 46  ARG n 
2 47  ILE n 
2 48  ASN n 
2 49  VAL n 
2 50  TYR n 
2 51  TYR n 
2 52  ASN n 
2 53  GLU n 
2 54  ALA n 
2 55  THR n 
2 56  GLY n 
2 57  ASN n 
2 58  LYS n 
2 59  TYR n 
2 60  VAL n 
2 61  PRO n 
2 62  ARG n 
2 63  ALA n 
2 64  ILE n 
2 65  LEU n 
2 66  VAL n 
2 67  ASP n 
2 68  LEU n 
2 69  GLU n 
2 70  PRO n 
2 71  GLY n 
2 72  THR n 
2 73  MET n 
2 74  ASP n 
2 75  SER n 
2 76  VAL n 
2 77  ARG n 
2 78  SER n 
2 79  GLY n 
2 80  PRO n 
2 81  PHE n 
2 82  GLY n 
2 83  GLN n 
2 84  ILE n 
2 85  PHE n 
2 86  ARG n 
2 87  PRO n 
2 88  ASP n 
2 89  ASN n 
2 90  PHE n 
2 91  VAL n 
2 92  PHE n 
2 93  GLY n 
2 94  GLN n 
2 95  SER n 
2 96  GLY n 
2 97  ALA n 
2 98  GLY n 
2 99  ASN n 
2 100 ASN n 
2 101 TRP n 
2 102 ALA n 
2 103 LYS n 
2 104 GLY n 
2 105 HIS n 
2 106 TYR n 
2 107 THR n 
2 108 GLU n 
2 109 GLY n 
2 110 ALA n 
2 111 GLU n 
2 112 LEU n 
2 113 VAL n 
2 114 ASP n 
2 115 SER n 
2 116 VAL n 
2 117 LEU n 
2 118 ASP n 
2 119 VAL n 
2 120 VAL n 
2 121 ARG n 
2 122 LYS n 
2 123 GLU n 
2 124 SER n 
2 125 GLU n 
2 126 SER n 
2 127 CYS n 
2 128 ASP n 
2 129 CYS n 
2 130 LEU n 
2 131 GLN n 
2 132 GLY n 
2 133 PHE n 
2 134 GLN n 
2 135 LEU n 
2 136 THR n 
2 137 HIS n 
2 138 SER n 
2 139 LEU n 
2 140 GLY n 
2 141 GLY n 
2 142 GLY n 
2 143 THR n 
2 144 GLY n 
2 145 SER n 
2 146 GLY n 
2 147 MET n 
2 148 GLY n 
2 149 THR n 
2 150 LEU n 
2 151 LEU n 
2 152 ILE n 
2 153 SER n 
2 154 LYS n 
2 155 ILE n 
2 156 ARG n 
2 157 GLU n 
2 158 GLU n 
2 159 TYR n 
2 160 PRO n 
2 161 ASP n 
2 162 ARG n 
2 163 ILE n 
2 164 MET n 
2 165 ASN n 
2 166 THR n 
2 167 PHE n 
2 168 SER n 
2 169 VAL n 
2 170 MET n 
2 171 PRO n 
2 172 SER n 
2 173 PRO n 
2 174 LYS n 
2 175 VAL n 
2 176 SER n 
2 177 ASP n 
2 178 THR n 
2 179 VAL n 
2 180 VAL n 
2 181 GLU n 
2 182 PRO n 
2 183 TYR n 
2 184 ASN n 
2 185 ALA n 
2 186 THR n 
2 187 LEU n 
2 188 SER n 
2 189 VAL n 
2 190 HIS n 
2 191 GLN n 
2 192 LEU n 
2 193 VAL n 
2 194 GLU n 
2 195 ASN n 
2 196 THR n 
2 197 ASP n 
2 198 GLU n 
2 199 THR n 
2 200 TYR n 
2 201 CYS n 
2 202 ILE n 
2 203 ASP n 
2 204 ASN n 
2 205 GLU n 
2 206 ALA n 
2 207 LEU n 
2 208 TYR n 
2 209 ASP n 
2 210 ILE n 
2 211 CYS n 
2 212 PHE n 
2 213 ARG n 
2 214 THR n 
2 215 LEU n 
2 216 LYS n 
2 217 LEU n 
2 218 THR n 
2 219 THR n 
2 220 PRO n 
2 221 THR n 
2 222 TYR n 
2 223 GLY n 
2 224 ASP n 
2 225 LEU n 
2 226 ASN n 
2 227 HIS n 
2 228 LEU n 
2 229 VAL n 
2 230 SER n 
2 231 ALA n 
2 232 THR n 
2 233 MET n 
2 234 SER n 
2 235 GLY n 
2 236 VAL n 
2 237 THR n 
2 238 THR n 
2 239 CYS n 
2 240 LEU n 
2 241 ARG n 
2 242 PHE n 
2 243 PRO n 
2 244 GLY n 
2 245 GLN n 
2 246 LEU n 
2 247 ASN n 
2 248 ALA n 
2 249 ASP n 
2 250 LEU n 
2 251 ARG n 
2 252 LYS n 
2 253 LEU n 
2 254 ALA n 
2 255 VAL n 
2 256 ASN n 
2 257 MET n 
2 258 VAL n 
2 259 PRO n 
2 260 PHE n 
2 261 PRO n 
2 262 ARG n 
2 263 LEU n 
2 264 HIS n 
2 265 PHE n 
2 266 PHE n 
2 267 MET n 
2 268 PRO n 
2 269 GLY n 
2 270 PHE n 
2 271 ALA n 
2 272 PRO n 
2 273 LEU n 
2 274 THR n 
2 275 SER n 
2 276 ARG n 
2 277 GLY n 
2 278 SER n 
2 279 GLN n 
2 280 GLN n 
2 281 TYR n 
2 282 ARG n 
2 283 ALA n 
2 284 LEU n 
2 285 THR n 
2 286 VAL n 
2 287 PRO n 
2 288 GLU n 
2 289 LEU n 
2 290 THR n 
2 291 GLN n 
2 292 GLN n 
2 293 MET n 
2 294 PHE n 
2 295 ASP n 
2 296 SER n 
2 297 LYS n 
2 298 ASN n 
2 299 MET n 
2 300 MET n 
2 301 ALA n 
2 302 ALA n 
2 303 CYS n 
2 304 ASP n 
2 305 PRO n 
2 306 ARG n 
2 307 HIS n 
2 308 GLY n 
2 309 ARG n 
2 310 TYR n 
2 311 LEU n 
2 312 THR n 
2 313 VAL n 
2 314 ALA n 
2 315 ALA n 
2 316 ILE n 
2 317 PHE n 
2 318 ARG n 
2 319 GLY n 
2 320 ARG n 
2 321 MET n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLU n 
2 326 VAL n 
2 327 ASP n 
2 328 GLU n 
2 329 GLN n 
2 330 MET n 
2 331 LEU n 
2 332 ASN n 
2 333 VAL n 
2 334 GLN n 
2 335 ASN n 
2 336 LYS n 
2 337 ASN n 
2 338 SER n 
2 339 SER n 
2 340 TYR n 
2 341 PHE n 
2 342 VAL n 
2 343 GLU n 
2 344 TRP n 
2 345 ILE n 
2 346 PRO n 
2 347 ASN n 
2 348 ASN n 
2 349 VAL n 
2 350 LYS n 
2 351 THR n 
2 352 ALA n 
2 353 VAL n 
2 354 CYS n 
2 355 ASP n 
2 356 ILE n 
2 357 PRO n 
2 358 PRO n 
2 359 ARG n 
2 360 GLY n 
2 361 LEU n 
2 362 LYS n 
2 363 MET n 
2 364 SER n 
2 365 ALA n 
2 366 THR n 
2 367 PHE n 
2 368 ILE n 
2 369 GLY n 
2 370 ASN n 
2 371 SER n 
2 372 THR n 
2 373 ALA n 
2 374 ILE n 
2 375 GLN n 
2 376 GLU n 
2 377 LEU n 
2 378 PHE n 
2 379 LYS n 
2 380 ARG n 
2 381 ILE n 
2 382 SER n 
2 383 GLU n 
2 384 GLN n 
2 385 PHE n 
2 386 THR n 
2 387 ALA n 
2 388 MET n 
2 389 PHE n 
2 390 ARG n 
2 391 ARG n 
2 392 LYS n 
2 393 ALA n 
2 394 PHE n 
2 395 LEU n 
2 396 HIS n 
2 397 TRP n 
2 398 TYR n 
2 399 THR n 
2 400 GLY n 
2 401 GLU n 
2 402 GLY n 
2 403 MET n 
2 404 ASP n 
2 405 GLU n 
2 406 MET n 
2 407 GLU n 
2 408 PHE n 
2 409 THR n 
2 410 GLU n 
2 411 ALA n 
2 412 GLU n 
2 413 SER n 
2 414 ASN n 
2 415 MET n 
2 416 ASN n 
2 417 ASP n 
2 418 LEU n 
2 419 VAL n 
2 420 SER n 
2 421 GLU n 
2 422 TYR n 
2 423 GLN n 
2 424 GLN n 
2 425 TYR n 
2 426 GLN n 
2 427 ASP n 
2 428 ALA n 
2 429 THR n 
2 430 ALA n 
2 431 ASP n 
3 1   MET n 
3 2   GLU n 
3 3   VAL n 
3 4   ILE n 
3 5   GLU n 
3 6   LEU n 
3 7   ASN n 
3 8   LYS n 
3 9   CYS n 
3 10  THR n 
3 11  SER n 
3 12  GLY n 
3 13  GLN n 
3 14  SER n 
3 15  PHE n 
3 16  GLU n 
3 17  VAL n 
3 18  ILE n 
3 19  LEU n 
3 20  LYS n 
3 21  PRO n 
3 22  PRO n 
3 23  SER n 
3 24  PHE n 
3 25  ASP n 
3 26  GLY n 
3 27  VAL n 
3 28  PRO n 
3 29  GLU n 
3 30  PHE n 
3 31  ASN n 
3 32  ALA n 
3 33  SER n 
3 34  LEU n 
3 35  PRO n 
3 36  ARG n 
3 37  ARG n 
3 38  ARG n 
3 39  ASP n 
3 40  PRO n 
3 41  SER n 
3 42  LEU n 
3 43  GLU n 
3 44  GLU n 
3 45  ILE n 
3 46  GLN n 
3 47  LYS n 
3 48  LYS n 
3 49  LEU n 
3 50  GLU n 
3 51  ALA n 
3 52  ALA n 
3 53  GLU n 
3 54  GLU n 
3 55  ARG n 
3 56  ARG n 
3 57  LYS n 
3 58  TYR n 
3 59  GLN n 
3 60  GLU n 
3 61  ALA n 
3 62  GLU n 
3 63  LEU n 
3 64  LEU n 
3 65  LYS n 
3 66  HIS n 
3 67  LEU n 
3 68  ALA n 
3 69  GLU n 
3 70  LYS n 
3 71  ARG n 
3 72  GLU n 
3 73  HIS n 
3 74  GLU n 
3 75  ARG n 
3 76  GLU n 
3 77  VAL n 
3 78  ILE n 
3 79  GLN n 
3 80  LYS n 
3 81  ALA n 
3 82  ILE n 
3 83  GLU n 
3 84  GLU n 
3 85  ASN n 
3 86  ASN n 
3 87  ASN n 
3 88  PHE n 
3 89  ILE n 
3 90  LYS n 
3 91  MET n 
3 92  ALA n 
3 93  LYS n 
3 94  GLU n 
3 95  LYS n 
3 96  LEU n 
3 97  ALA n 
3 98  GLN n 
3 99  LYS n 
3 100 MET n 
3 101 GLU n 
3 102 SER n 
3 103 ASN n 
3 104 LYS n 
3 105 GLU n 
3 106 ASN n 
3 107 ARG n 
3 108 GLU n 
3 109 ALA n 
3 110 HIS n 
3 111 LEU n 
3 112 ALA n 
3 113 ALA n 
3 114 MET n 
3 115 LEU n 
3 116 GLU n 
3 117 ARG n 
3 118 LEU n 
3 119 GLN n 
3 120 GLU n 
3 121 LYS n 
3 122 ASP n 
3 123 LYS n 
3 124 HIS n 
3 125 ALA n 
3 126 GLU n 
3 127 GLU n 
3 128 VAL n 
3 129 ARG n 
3 130 LYS n 
3 131 ASN n 
3 132 LYS n 
3 133 GLU n 
3 134 LEU n 
3 135 LYS n 
3 136 GLU n 
4 1   MET n 
4 2   TYR n 
4 3   THR n 
4 4   PHE n 
4 5   VAL n 
4 6   VAL n 
4 7   ARG n 
4 8   ASP n 
4 9   GLU n 
4 10  ASN n 
4 11  SER n 
4 12  SER n 
4 13  VAL n 
4 14  TYR n 
4 15  ALA n 
4 16  GLU n 
4 17  VAL n 
4 18  SER n 
4 19  ARG n 
4 20  LEU n 
4 21  LEU n 
4 22  LEU n 
4 23  ALA n 
4 24  THR n 
4 25  GLY n 
4 26  GLN n 
4 27  TRP n 
4 28  LYS n 
4 29  ARG n 
4 30  LEU n 
4 31  ARG n 
4 32  LYS n 
4 33  ASP n 
4 34  ASN n 
4 35  PRO n 
4 36  ARG n 
4 37  PHE n 
4 38  ASN n 
4 39  LEU n 
4 40  MET n 
4 41  LEU n 
4 42  GLY n 
4 43  GLU n 
4 44  ARG n 
4 45  ASN n 
4 46  ARG n 
4 47  LEU n 
4 48  PRO n 
4 49  PHE n 
4 50  GLY n 
4 51  ARG n 
4 52  LEU n 
4 53  GLY n 
4 54  HIS n 
4 55  GLU n 
4 56  PRO n 
4 57  GLY n 
4 58  LEU n 
4 59  VAL n 
4 60  GLN n 
4 61  LEU n 
4 62  VAL n 
4 63  ASN n 
4 64  TYR n 
4 65  TYR n 
4 66  ARG n 
4 67  GLY n 
4 68  ALA n 
4 69  ASP n 
4 70  LYS n 
4 71  LEU n 
4 72  CYS n 
4 73  ARG n 
4 74  LYS n 
4 75  ALA n 
4 76  SER n 
4 77  LEU n 
4 78  VAL n 
4 79  LYS n 
4 80  LEU n 
4 81  ILE n 
4 82  LYS n 
4 83  THR n 
4 84  SER n 
4 85  PRO n 
4 86  GLU n 
4 87  LEU n 
4 88  SER n 
4 89  GLU n 
4 90  SER n 
4 91  CYS n 
4 92  THR n 
4 93  TRP n 
4 94  PHE n 
4 95  PRO n 
4 96  GLU n 
4 97  SER n 
4 98  TYR n 
4 99  VAL n 
4 100 ILE n 
4 101 TYR n 
4 102 PRO n 
4 103 THR n 
4 104 ASN n 
4 105 LEU n 
4 106 LYS n 
4 107 THR n 
4 108 PRO n 
4 109 VAL n 
4 110 ALA n 
4 111 PRO n 
4 112 ALA n 
4 113 GLN n 
4 114 ASN n 
4 115 GLY n 
4 116 ILE n 
4 117 ARG n 
4 118 HIS n 
4 119 LEU n 
4 120 ILE n 
4 121 ASN n 
4 122 ASN n 
4 123 THR n 
4 124 ARG n 
4 125 THR n 
4 126 ASP n 
4 127 GLU n 
4 128 ARG n 
4 129 GLU n 
4 130 VAL n 
4 131 PHE n 
4 132 LEU n 
4 133 ALA n 
4 134 ALA n 
4 135 TYR n 
4 136 ASN n 
4 137 ARG n 
4 138 ARG n 
4 139 ARG n 
4 140 GLU n 
4 141 GLY n 
4 142 ARG n 
4 143 GLU n 
4 144 GLY n 
4 145 ASN n 
4 146 VAL n 
4 147 TRP n 
4 148 ILE n 
4 149 ALA n 
4 150 LYS n 
4 151 SER n 
4 152 SER n 
4 153 ALA n 
4 154 GLY n 
4 155 ALA n 
4 156 LYS n 
4 157 GLY n 
4 158 GLU n 
4 159 GLY n 
4 160 ILE n 
4 161 LEU n 
4 162 ILE n 
4 163 SER n 
4 164 SER n 
4 165 GLU n 
4 166 ALA n 
4 167 SER n 
4 168 GLU n 
4 169 LEU n 
4 170 LEU n 
4 171 ASP n 
4 172 PHE n 
4 173 ILE n 
4 174 ASP n 
4 175 GLU n 
4 176 GLN n 
4 177 GLY n 
4 178 GLN n 
4 179 VAL n 
4 180 HIS n 
4 181 VAL n 
4 182 ILE n 
4 183 GLN n 
4 184 LYS n 
4 185 TYR n 
4 186 LEU n 
4 187 GLU n 
4 188 LYS n 
4 189 PRO n 
4 190 LEU n 
4 191 LEU n 
4 192 LEU n 
4 193 GLU n 
4 194 PRO n 
4 195 GLY n 
4 196 HIS n 
4 197 ARG n 
4 198 LYS n 
4 199 PHE n 
4 200 ASP n 
4 201 ILE n 
4 202 ARG n 
4 203 SER n 
4 204 TRP n 
4 205 VAL n 
4 206 LEU n 
4 207 VAL n 
4 208 ASP n 
4 209 HIS n 
4 210 LEU n 
4 211 TYR n 
4 212 ASN n 
4 213 ILE n 
4 214 TYR n 
4 215 LEU n 
4 216 TYR n 
4 217 ARG n 
4 218 GLU n 
4 219 GLY n 
4 220 VAL n 
4 221 LEU n 
4 222 ARG n 
4 223 THR n 
4 224 SER n 
4 225 SER n 
4 226 GLU n 
4 227 PRO n 
4 228 TYR n 
4 229 ASN n 
4 230 SER n 
4 231 ALA n 
4 232 ASN n 
4 233 PHE n 
4 234 GLN n 
4 235 ASP n 
4 236 LYS n 
4 237 THR n 
4 238 CYS n 
4 239 HIS n 
4 240 LEU n 
4 241 THR n 
4 242 ASN n 
4 243 HIS n 
4 244 CYS n 
4 245 ILE n 
4 246 GLN n 
4 247 LYS n 
4 248 GLU n 
4 249 TYR n 
4 250 SER n 
4 251 LYS n 
4 252 ASN n 
4 253 TYR n 
4 254 GLY n 
4 255 ARG n 
4 256 TYR n 
4 257 GLU n 
4 258 GLU n 
4 259 GLY n 
4 260 ASN n 
4 261 GLU n 
4 262 MET n 
4 263 PHE n 
4 264 PHE n 
4 265 GLU n 
4 266 GLU n 
4 267 PHE n 
4 268 ASN n 
4 269 GLN n 
4 270 TYR n 
4 271 LEU n 
4 272 MET n 
4 273 ASP n 
4 274 ALA n 
4 275 LEU n 
4 276 ASN n 
4 277 THR n 
4 278 THR n 
4 279 LEU n 
4 280 GLU n 
4 281 ASN n 
4 282 SER n 
4 283 ILE n 
4 284 LEU n 
4 285 LEU n 
4 286 GLN n 
4 287 ILE n 
4 288 LYS n 
4 289 HIS n 
4 290 ILE n 
4 291 ILE n 
4 292 ARG n 
4 293 SER n 
4 294 CYS n 
4 295 LEU n 
4 296 MET n 
4 297 CYS n 
4 298 ILE n 
4 299 GLU n 
4 300 PRO n 
4 301 ALA n 
4 302 ILE n 
4 303 SER n 
4 304 THR n 
4 305 LYS n 
4 306 HIS n 
4 307 LEU n 
4 308 HIS n 
4 309 TYR n 
4 310 GLN n 
4 311 SER n 
4 312 PHE n 
4 313 GLN n 
4 314 LEU n 
4 315 PHE n 
4 316 GLY n 
4 317 PHE n 
4 318 ASP n 
4 319 PHE n 
4 320 MET n 
4 321 VAL n 
4 322 ASP n 
4 323 GLU n 
4 324 GLU n 
4 325 LEU n 
4 326 LYS n 
4 327 VAL n 
4 328 TRP n 
4 329 LEU n 
4 330 ILE n 
4 331 GLU n 
4 332 VAL n 
4 333 ASN n 
4 334 GLY n 
4 335 ALA n 
4 336 PRO n 
4 337 ALA n 
4 338 CYS n 
4 339 ALA n 
4 340 GLN n 
4 341 LYS n 
4 342 LEU n 
4 343 TYR n 
4 344 ALA n 
4 345 GLU n 
4 346 LEU n 
4 347 CYS n 
4 348 GLN n 
4 349 GLY n 
4 350 ILE n 
4 351 VAL n 
4 352 ASP n 
4 353 VAL n 
4 354 ALA n 
4 355 ILE n 
4 356 SER n 
4 357 SER n 
4 358 VAL n 
4 359 PHE n 
4 360 PRO n 
4 361 LEU n 
4 362 ALA n 
4 363 ASP n 
4 364 THR n 
4 365 GLY n 
4 366 GLN n 
4 367 LYS n 
4 368 THR n 
4 369 SER n 
4 370 GLN n 
4 371 PRO n 
4 372 THR n 
4 373 SER n 
4 374 ILE n 
4 375 PHE n 
4 376 ILE n 
4 377 LYS n 
4 378 LEU n 
4 379 HIS n 
4 380 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 440 pig          ? TUBA1B ? ? ? ? ? ? 'Sus scrofa'        9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 431 pig          ? TUBB2B ? ? ? ? ? ? 'Sus scrofa'        9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 136 'Norway rat' ? Stmn4  ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 380 ?            ? ?      ? ? ? ? ? ? 'Gallus gallus'     9031  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1D6D non-polymer         . '4-(2-chloranyl-6-fluoranyl-quinazolin-4-yl)-7-methoxy-1,3-dihydroquinoxalin-2-one' ? 
'C17 H12 Cl F N4 O2' 358.754 
ACP   non-polymer         . 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER'                                      
;ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
;
'C11 H18 N5 O12 P3'  505.208 
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 
CA    non-polymer         . 'CALCIUM ION'                                                                       ? 'Ca 2' 40.078  
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 
MES   non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                              ? 'C6 H13 N O4 S' 
195.237 
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 
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 A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   CYS 4   4   4   CYS CYS A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  TRP 21  21  21  TRP TRP A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  HIS 28  28  28  HIS HIS A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  GLN 31  31  31  GLN GLN A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  HIS 61  61  61  HIS HIS A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  THR 82  82  82  THR THR A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  GLN 85  85  85  GLN GLN A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  THR 94  94  94  THR THR A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLU 168 168 168 GLU GLU A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 HIS 192 192 192 HIS HIS A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 CYS 200 200 200 CYS CYS A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 TYR 210 210 210 TYR TYR A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 CYS 213 213 213 CYS CYS A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 ILE 238 238 238 ILE ILE A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 ASP 251 251 251 ASP ASP A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 PHE 255 255 255 PHE PHE A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 TYR 262 262 262 TYR TYR A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 ARG 264 264 264 ARG ARG A . n 
A 1 265 ILE 265 265 265 ILE ILE A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 PRO 268 268 268 PRO PRO A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 TYR 272 272 272 TYR TYR A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 ILE 276 276 276 ILE ILE A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 TYR 282 282 282 TYR TYR A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 GLN 285 285 285 GLN GLN A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 CYS 295 295 295 CYS CYS A . n 
A 1 296 PHE 296 296 296 PHE PHE A . n 
A 1 297 GLU 297 297 297 GLU GLU A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 GLN 301 301 301 GLN GLN A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 CYS 305 305 305 CYS CYS A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 GLY 310 310 310 GLY GLY A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 MET 313 313 313 MET MET A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 CYS 315 315 315 CYS CYS A . n 
A 1 316 CYS 316 316 316 CYS CYS A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 TYR 319 319 319 TYR TYR A . n 
A 1 320 ARG 320 320 320 ARG ARG A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 ARG 339 339 339 ARG ARG A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 GLN 342 342 342 GLN GLN A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 TRP 346 346 346 TRP TRP A . n 
A 1 347 CYS 347 347 347 CYS CYS A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 THR 349 349 349 THR THR A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 GLY 354 354 354 GLY GLY A . n 
A 1 355 ILE 355 355 355 ILE ILE A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 TYR 357 357 357 TYR TYR A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 PRO 359 359 359 PRO PRO A . n 
A 1 360 PRO 360 360 360 PRO PRO A . n 
A 1 361 THR 361 361 361 THR THR A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 ARG 373 373 373 ARG ARG A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 CYS 376 376 376 CYS CYS A . n 
A 1 377 MET 377 377 377 MET MET A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 SER 379 379 379 SER SER A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 THR 381 381 381 THR THR A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 ILE 384 384 384 ILE ILE A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 TRP 388 388 388 TRP TRP A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 ARG 390 390 390 ARG ARG A . n 
A 1 391 LEU 391 391 391 LEU LEU A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 LYS 394 394 394 LYS LYS A . n 
A 1 395 PHE 395 395 395 PHE PHE A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 LYS 401 401 401 LYS LYS A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 ALA 403 403 403 ALA ALA A . n 
A 1 404 PHE 404 404 404 PHE PHE A . n 
A 1 405 VAL 405 405 405 VAL VAL A . n 
A 1 406 HIS 406 406 406 HIS HIS A . n 
A 1 407 TRP 407 407 407 TRP TRP A . n 
A 1 408 TYR 408 408 408 TYR TYR A . n 
A 1 409 VAL 409 409 409 VAL VAL A . n 
A 1 410 GLY 410 410 410 GLY GLY A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 GLY 412 412 412 GLY GLY A . n 
A 1 413 MET 413 413 413 MET MET A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 GLU 417 417 417 GLU GLU A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 SER 419 419 419 SER SER A . n 
A 1 420 GLU 420 420 420 GLU GLU A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 ARG 422 422 422 ARG ARG A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 ASP 424 424 424 ASP ASP A . n 
A 1 425 MET 425 425 425 MET MET A . n 
A 1 426 ALA 426 426 426 ALA ALA A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 LEU 428 428 428 LEU LEU A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 ASP 431 431 431 ASP ASP A . n 
A 1 432 TYR 432 432 432 TYR TYR A . n 
A 1 433 GLU 433 433 433 GLU GLU A . n 
A 1 434 GLU 434 434 434 GLU GLU A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLY 436 436 436 GLY GLY A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 ASP 438 438 ?   ?   ?   A . n 
A 1 439 SER 439 439 ?   ?   ?   A . n 
A 1 440 VAL 440 440 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ARG 2   2   2   ARG ARG B . n 
B 2 3   GLU 3   3   3   GLU GLU B . n 
B 2 4   ILE 4   4   4   ILE ILE B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   HIS 6   6   6   HIS HIS B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   GLN 8   8   8   GLN GLN B . n 
B 2 9   ALA 9   9   9   ALA ALA B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLN 11  11  11  GLN GLN B . n 
B 2 12  CYS 12  12  12  CYS CYS B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  ASN 14  14  14  ASN ASN B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  GLY 17  17  17  GLY GLY B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  PHE 20  20  20  PHE PHE B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  ILE 24  24  24  ILE ILE B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  ASP 26  26  26  ASP ASP B . n 
B 2 27  GLU 27  27  27  GLU GLU B . n 
B 2 28  HIS 28  28  28  HIS HIS B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ILE 30  30  30  ILE ILE B . n 
B 2 31  ASP 31  31  31  ASP ASP B . n 
B 2 32  PRO 32  32  32  PRO PRO B . n 
B 2 33  THR 33  33  33  THR THR B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  SER 35  35  35  SER SER B . n 
B 2 36  TYR 36  36  36  TYR TYR B . n 
B 2 37  HIS 37  37  37  HIS HIS B . n 
B 2 38  GLY 38  38  38  GLY GLY B . n 
B 2 39  ASP 39  39  39  ASP ASP B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  LEU 42  42  42  LEU LEU B . n 
B 2 43  GLN 43  43  43  GLN GLN B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  GLU 45  45  45  GLU GLU B . n 
B 2 46  ARG 46  46  46  ARG ARG B . n 
B 2 47  ILE 47  47  47  ILE ILE B . n 
B 2 48  ASN 48  48  48  ASN ASN B . n 
B 2 49  VAL 49  49  49  VAL VAL B . n 
B 2 50  TYR 50  50  50  TYR TYR B . n 
B 2 51  TYR 51  51  51  TYR TYR B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  GLU 53  53  53  GLU GLU B . n 
B 2 54  ALA 54  54  54  ALA ALA B . n 
B 2 55  THR 55  55  55  THR THR B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  ARG 62  62  62  ARG ARG B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  LEU 65  65  65  LEU LEU B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PRO 70  70  70  PRO PRO B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  THR 72  72  72  THR THR B . n 
B 2 73  MET 73  73  73  MET MET B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  SER 75  75  75  SER SER B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  ARG 77  77  77  ARG ARG B . n 
B 2 78  SER 78  78  78  SER SER B . n 
B 2 79  GLY 79  79  79  GLY GLY B . n 
B 2 80  PRO 80  80  80  PRO PRO B . n 
B 2 81  PHE 81  81  81  PHE PHE B . n 
B 2 82  GLY 82  82  82  GLY GLY B . n 
B 2 83  GLN 83  83  83  GLN GLN B . n 
B 2 84  ILE 84  84  84  ILE ILE B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  ASP 88  88  88  ASP ASP B . n 
B 2 89  ASN 89  89  89  ASN ASN B . n 
B 2 90  PHE 90  90  90  PHE PHE B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  PHE 92  92  92  PHE PHE B . n 
B 2 93  GLY 93  93  93  GLY GLY B . n 
B 2 94  GLN 94  94  94  GLN GLN B . n 
B 2 95  SER 95  95  95  SER SER B . n 
B 2 96  GLY 96  96  96  GLY GLY B . n 
B 2 97  ALA 97  97  97  ALA ALA B . n 
B 2 98  GLY 98  98  98  GLY GLY B . n 
B 2 99  ASN 99  99  99  ASN ASN B . n 
B 2 100 ASN 100 100 100 ASN ASN B . n 
B 2 101 TRP 101 101 101 TRP TRP B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 LYS 103 103 103 LYS LYS B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 HIS 105 105 105 HIS HIS B . n 
B 2 106 TYR 106 106 106 TYR TYR B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 GLU 108 108 108 GLU GLU B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 ALA 110 110 110 ALA ALA B . n 
B 2 111 GLU 111 111 111 GLU GLU B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 ASP 114 114 114 ASP ASP B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 LEU 117 117 117 LEU LEU B . n 
B 2 118 ASP 118 118 118 ASP ASP B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 VAL 120 120 120 VAL VAL B . n 
B 2 121 ARG 121 121 121 ARG ARG B . n 
B 2 122 LYS 122 122 122 LYS LYS B . n 
B 2 123 GLU 123 123 123 GLU GLU B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 GLU 125 125 125 GLU GLU B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 CYS 127 127 127 CYS CYS B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 CYS 129 129 129 CYS CYS B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 GLY 132 132 132 GLY GLY B . n 
B 2 133 PHE 133 133 133 PHE PHE B . n 
B 2 134 GLN 134 134 134 GLN GLN B . n 
B 2 135 LEU 135 135 135 LEU LEU B . n 
B 2 136 THR 136 136 136 THR THR B . n 
B 2 137 HIS 137 137 137 HIS HIS B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 LEU 139 139 139 LEU LEU B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 GLY 141 141 141 GLY GLY B . n 
B 2 142 GLY 142 142 142 GLY GLY B . n 
B 2 143 THR 143 143 143 THR THR B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 SER 145 145 145 SER SER B . n 
B 2 146 GLY 146 146 146 GLY GLY B . n 
B 2 147 MET 147 147 147 MET MET B . n 
B 2 148 GLY 148 148 148 GLY GLY B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 LEU 151 151 151 LEU LEU B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 SER 153 153 153 SER SER B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 ILE 155 155 155 ILE ILE B . n 
B 2 156 ARG 156 156 156 ARG ARG B . n 
B 2 157 GLU 157 157 157 GLU GLU B . n 
B 2 158 GLU 158 158 158 GLU GLU B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 ASP 161 161 161 ASP ASP B . n 
B 2 162 ARG 162 162 162 ARG ARG B . n 
B 2 163 ILE 163 163 163 ILE ILE B . n 
B 2 164 MET 164 164 164 MET MET B . n 
B 2 165 ASN 165 165 165 ASN ASN B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 PHE 167 167 167 PHE PHE B . n 
B 2 168 SER 168 168 168 SER SER B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 MET 170 170 170 MET MET B . n 
B 2 171 PRO 171 171 171 PRO PRO B . n 
B 2 172 SER 172 172 172 SER SER B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 LYS 174 174 174 LYS LYS B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 SER 176 176 176 SER SER B . n 
B 2 177 ASP 177 177 177 ASP ASP B . n 
B 2 178 THR 178 178 178 THR THR B . n 
B 2 179 VAL 179 179 179 VAL VAL B . n 
B 2 180 VAL 180 180 180 VAL VAL B . n 
B 2 181 GLU 181 181 181 GLU GLU B . n 
B 2 182 PRO 182 182 182 PRO PRO B . n 
B 2 183 TYR 183 183 183 TYR TYR B . n 
B 2 184 ASN 184 184 184 ASN ASN B . n 
B 2 185 ALA 185 185 185 ALA ALA B . n 
B 2 186 THR 186 186 186 THR THR B . n 
B 2 187 LEU 187 187 187 LEU LEU B . n 
B 2 188 SER 188 188 188 SER SER B . n 
B 2 189 VAL 189 189 189 VAL VAL B . n 
B 2 190 HIS 190 190 190 HIS HIS B . n 
B 2 191 GLN 191 191 191 GLN GLN B . n 
B 2 192 LEU 192 192 192 LEU LEU B . n 
B 2 193 VAL 193 193 193 VAL VAL B . n 
B 2 194 GLU 194 194 194 GLU GLU B . n 
B 2 195 ASN 195 195 195 ASN ASN B . n 
B 2 196 THR 196 196 196 THR THR B . n 
B 2 197 ASP 197 197 197 ASP ASP B . n 
B 2 198 GLU 198 198 198 GLU GLU B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 CYS 201 201 201 CYS CYS B . n 
B 2 202 ILE 202 202 202 ILE ILE B . n 
B 2 203 ASP 203 203 203 ASP ASP B . n 
B 2 204 ASN 204 204 204 ASN ASN B . n 
B 2 205 GLU 205 205 205 GLU GLU B . n 
B 2 206 ALA 206 206 206 ALA ALA B . n 
B 2 207 LEU 207 207 207 LEU LEU B . n 
B 2 208 TYR 208 208 208 TYR TYR B . n 
B 2 209 ASP 209 209 209 ASP ASP B . n 
B 2 210 ILE 210 210 210 ILE ILE B . n 
B 2 211 CYS 211 211 211 CYS CYS B . n 
B 2 212 PHE 212 212 212 PHE PHE B . n 
B 2 213 ARG 213 213 213 ARG ARG B . n 
B 2 214 THR 214 214 214 THR THR B . n 
B 2 215 LEU 215 215 215 LEU LEU B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 LEU 217 217 217 LEU LEU B . n 
B 2 218 THR 218 218 218 THR THR B . n 
B 2 219 THR 219 219 219 THR THR B . n 
B 2 220 PRO 220 220 220 PRO PRO B . n 
B 2 221 THR 221 221 221 THR THR B . n 
B 2 222 TYR 222 222 222 TYR TYR B . n 
B 2 223 GLY 223 223 223 GLY GLY B . n 
B 2 224 ASP 224 224 224 ASP ASP B . n 
B 2 225 LEU 225 225 225 LEU LEU B . n 
B 2 226 ASN 226 226 226 ASN ASN B . n 
B 2 227 HIS 227 227 227 HIS HIS B . n 
B 2 228 LEU 228 228 228 LEU LEU B . n 
B 2 229 VAL 229 229 229 VAL VAL B . n 
B 2 230 SER 230 230 230 SER SER B . n 
B 2 231 ALA 231 231 231 ALA ALA B . n 
B 2 232 THR 232 232 232 THR THR B . n 
B 2 233 MET 233 233 233 MET MET B . n 
B 2 234 SER 234 234 234 SER SER B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 VAL 236 236 236 VAL VAL B . n 
B 2 237 THR 237 237 237 THR THR B . n 
B 2 238 THR 238 238 238 THR THR B . n 
B 2 239 CYS 239 239 239 CYS CYS B . n 
B 2 240 LEU 240 240 240 LEU LEU B . n 
B 2 241 ARG 241 241 241 ARG ARG B . n 
B 2 242 PHE 242 242 242 PHE PHE B . n 
B 2 243 PRO 243 243 243 PRO PRO B . n 
B 2 244 GLY 244 244 244 GLY GLY B . n 
B 2 245 GLN 245 245 245 GLN GLN B . n 
B 2 246 LEU 246 246 246 LEU LEU B . n 
B 2 247 ASN 247 247 247 ASN ASN B . n 
B 2 248 ALA 248 248 248 ALA ALA B . n 
B 2 249 ASP 249 249 249 ASP ASP B . n 
B 2 250 LEU 250 250 250 LEU LEU B . n 
B 2 251 ARG 251 251 251 ARG ARG B . n 
B 2 252 LYS 252 252 252 LYS LYS B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 ALA 254 254 254 ALA ALA B . n 
B 2 255 VAL 255 255 255 VAL VAL B . n 
B 2 256 ASN 256 256 256 ASN ASN B . n 
B 2 257 MET 257 257 257 MET MET B . n 
B 2 258 VAL 258 258 258 VAL VAL B . n 
B 2 259 PRO 259 259 259 PRO PRO B . n 
B 2 260 PHE 260 260 260 PHE PHE B . n 
B 2 261 PRO 261 261 261 PRO PRO B . n 
B 2 262 ARG 262 262 262 ARG ARG B . n 
B 2 263 LEU 263 263 263 LEU LEU B . n 
B 2 264 HIS 264 264 264 HIS HIS B . n 
B 2 265 PHE 265 265 265 PHE PHE B . n 
B 2 266 PHE 266 266 266 PHE PHE B . n 
B 2 267 MET 267 267 267 MET MET B . n 
B 2 268 PRO 268 268 268 PRO PRO B . n 
B 2 269 GLY 269 269 269 GLY GLY B . n 
B 2 270 PHE 270 270 270 PHE PHE B . n 
B 2 271 ALA 271 271 271 ALA ALA B . n 
B 2 272 PRO 272 272 272 PRO PRO B . n 
B 2 273 LEU 273 273 273 LEU LEU B . n 
B 2 274 THR 274 274 274 THR THR B . n 
B 2 275 SER 275 275 275 SER SER B . n 
B 2 276 ARG 276 276 276 ARG ARG B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 SER 278 278 278 SER SER B . n 
B 2 279 GLN 279 279 279 GLN GLN B . n 
B 2 280 GLN 280 280 280 GLN GLN B . n 
B 2 281 TYR 281 281 281 TYR TYR B . n 
B 2 282 ARG 282 282 282 ARG ARG B . n 
B 2 283 ALA 283 283 283 ALA ALA B . n 
B 2 284 LEU 284 284 284 LEU LEU B . n 
B 2 285 THR 285 285 285 THR THR B . n 
B 2 286 VAL 286 286 286 VAL VAL B . n 
B 2 287 PRO 287 287 287 PRO PRO B . n 
B 2 288 GLU 288 288 288 GLU GLU B . n 
B 2 289 LEU 289 289 289 LEU LEU B . n 
B 2 290 THR 290 290 290 THR THR B . n 
B 2 291 GLN 291 291 291 GLN GLN B . n 
B 2 292 GLN 292 292 292 GLN GLN B . n 
B 2 293 MET 293 293 293 MET MET B . n 
B 2 294 PHE 294 294 294 PHE PHE B . n 
B 2 295 ASP 295 295 295 ASP ASP B . n 
B 2 296 SER 296 296 296 SER SER B . n 
B 2 297 LYS 297 297 297 LYS LYS B . n 
B 2 298 ASN 298 298 298 ASN ASN B . n 
B 2 299 MET 299 299 299 MET MET B . n 
B 2 300 MET 300 300 300 MET MET B . n 
B 2 301 ALA 301 301 301 ALA ALA B . n 
B 2 302 ALA 302 302 302 ALA ALA B . n 
B 2 303 CYS 303 303 303 CYS CYS B . n 
B 2 304 ASP 304 304 304 ASP ASP B . n 
B 2 305 PRO 305 305 305 PRO PRO B . n 
B 2 306 ARG 306 306 306 ARG ARG B . n 
B 2 307 HIS 307 307 307 HIS HIS B . n 
B 2 308 GLY 308 308 308 GLY GLY B . n 
B 2 309 ARG 309 309 309 ARG ARG B . n 
B 2 310 TYR 310 310 310 TYR TYR B . n 
B 2 311 LEU 311 311 311 LEU LEU B . n 
B 2 312 THR 312 312 312 THR THR B . n 
B 2 313 VAL 313 313 313 VAL VAL B . n 
B 2 314 ALA 314 314 314 ALA ALA B . n 
B 2 315 ALA 315 315 315 ALA ALA B . n 
B 2 316 ILE 316 316 316 ILE ILE B . n 
B 2 317 PHE 317 317 317 PHE PHE B . n 
B 2 318 ARG 318 318 318 ARG ARG B . n 
B 2 319 GLY 319 319 319 GLY GLY B . n 
B 2 320 ARG 320 320 320 ARG ARG B . n 
B 2 321 MET 321 321 321 MET MET B . n 
B 2 322 SER 322 322 322 SER SER B . n 
B 2 323 MET 323 323 323 MET MET B . n 
B 2 324 LYS 324 324 324 LYS LYS B . n 
B 2 325 GLU 325 325 325 GLU GLU B . n 
B 2 326 VAL 326 326 326 VAL VAL B . n 
B 2 327 ASP 327 327 327 ASP ASP B . n 
B 2 328 GLU 328 328 328 GLU GLU B . n 
B 2 329 GLN 329 329 329 GLN GLN B . n 
B 2 330 MET 330 330 330 MET MET B . n 
B 2 331 LEU 331 331 331 LEU LEU B . n 
B 2 332 ASN 332 332 332 ASN ASN B . n 
B 2 333 VAL 333 333 333 VAL VAL B . n 
B 2 334 GLN 334 334 334 GLN GLN B . n 
B 2 335 ASN 335 335 335 ASN ASN B . n 
B 2 336 LYS 336 336 336 LYS LYS B . n 
B 2 337 ASN 337 337 337 ASN ASN B . n 
B 2 338 SER 338 338 338 SER SER B . n 
B 2 339 SER 339 339 339 SER SER B . n 
B 2 340 TYR 340 340 340 TYR TYR B . n 
B 2 341 PHE 341 341 341 PHE PHE B . n 
B 2 342 VAL 342 342 342 VAL VAL B . n 
B 2 343 GLU 343 343 343 GLU GLU B . n 
B 2 344 TRP 344 344 344 TRP TRP B . n 
B 2 345 ILE 345 345 345 ILE ILE B . n 
B 2 346 PRO 346 346 346 PRO PRO B . n 
B 2 347 ASN 347 347 347 ASN ASN B . n 
B 2 348 ASN 348 348 348 ASN ASN B . n 
B 2 349 VAL 349 349 349 VAL VAL B . n 
B 2 350 LYS 350 350 350 LYS LYS B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 ALA 352 352 352 ALA ALA B . n 
B 2 353 VAL 353 353 353 VAL VAL B . n 
B 2 354 CYS 354 354 354 CYS CYS B . n 
B 2 355 ASP 355 355 355 ASP ASP B . n 
B 2 356 ILE 356 356 356 ILE ILE B . n 
B 2 357 PRO 357 357 357 PRO PRO B . n 
B 2 358 PRO 358 358 358 PRO PRO B . n 
B 2 359 ARG 359 359 359 ARG ARG B . n 
B 2 360 GLY 360 360 360 GLY GLY B . n 
B 2 361 LEU 361 361 361 LEU LEU B . n 
B 2 362 LYS 362 362 362 LYS LYS B . n 
B 2 363 MET 363 363 363 MET MET B . n 
B 2 364 SER 364 364 364 SER SER B . n 
B 2 365 ALA 365 365 365 ALA ALA B . n 
B 2 366 THR 366 366 366 THR THR B . n 
B 2 367 PHE 367 367 367 PHE PHE B . n 
B 2 368 ILE 368 368 368 ILE ILE B . n 
B 2 369 GLY 369 369 369 GLY GLY B . n 
B 2 370 ASN 370 370 370 ASN ASN B . n 
B 2 371 SER 371 371 371 SER SER B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 ALA 373 373 373 ALA ALA B . n 
B 2 374 ILE 374 374 374 ILE ILE B . n 
B 2 375 GLN 375 375 375 GLN GLN B . n 
B 2 376 GLU 376 376 376 GLU GLU B . n 
B 2 377 LEU 377 377 377 LEU LEU B . n 
B 2 378 PHE 378 378 378 PHE PHE B . n 
B 2 379 LYS 379 379 379 LYS LYS B . n 
B 2 380 ARG 380 380 380 ARG ARG B . n 
B 2 381 ILE 381 381 381 ILE ILE B . n 
B 2 382 SER 382 382 382 SER SER B . n 
B 2 383 GLU 383 383 383 GLU GLU B . n 
B 2 384 GLN 384 384 384 GLN GLN B . n 
B 2 385 PHE 385 385 385 PHE PHE B . n 
B 2 386 THR 386 386 386 THR THR B . n 
B 2 387 ALA 387 387 387 ALA ALA B . n 
B 2 388 MET 388 388 388 MET MET B . n 
B 2 389 PHE 389 389 389 PHE PHE B . n 
B 2 390 ARG 390 390 390 ARG ARG B . n 
B 2 391 ARG 391 391 391 ARG ARG B . n 
B 2 392 LYS 392 392 392 LYS LYS B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 PHE 394 394 394 PHE PHE B . n 
B 2 395 LEU 395 395 395 LEU LEU B . n 
B 2 396 HIS 396 396 396 HIS HIS B . n 
B 2 397 TRP 397 397 397 TRP TRP B . n 
B 2 398 TYR 398 398 398 TYR TYR B . n 
B 2 399 THR 399 399 399 THR THR B . n 
B 2 400 GLY 400 400 400 GLY GLY B . n 
B 2 401 GLU 401 401 401 GLU GLU B . n 
B 2 402 GLY 402 402 402 GLY GLY B . n 
B 2 403 MET 403 403 403 MET MET B . n 
B 2 404 ASP 404 404 404 ASP ASP B . n 
B 2 405 GLU 405 405 405 GLU GLU B . n 
B 2 406 MET 406 406 406 MET MET B . n 
B 2 407 GLU 407 407 407 GLU GLU B . n 
B 2 408 PHE 408 408 408 PHE PHE B . n 
B 2 409 THR 409 409 409 THR THR B . n 
B 2 410 GLU 410 410 410 GLU GLU B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 GLU 412 412 412 GLU GLU B . n 
B 2 413 SER 413 413 413 SER SER B . n 
B 2 414 ASN 414 414 414 ASN ASN B . n 
B 2 415 MET 415 415 415 MET MET B . n 
B 2 416 ASN 416 416 416 ASN ASN B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 LEU 418 418 418 LEU LEU B . n 
B 2 419 VAL 419 419 419 VAL VAL B . n 
B 2 420 SER 420 420 420 SER SER B . n 
B 2 421 GLU 421 421 421 GLU GLU B . n 
B 2 422 TYR 422 422 422 TYR TYR B . n 
B 2 423 GLN 423 423 423 GLN GLN B . n 
B 2 424 GLN 424 424 424 GLN GLN B . n 
B 2 425 TYR 425 425 425 TYR TYR B . n 
B 2 426 GLN 426 426 426 GLN GLN B . n 
B 2 427 ASP 427 427 427 ASP ASP B . n 
B 2 428 ALA 428 428 428 ALA ALA B . n 
B 2 429 THR 429 429 ?   ?   ?   B . n 
B 2 430 ALA 430 430 ?   ?   ?   B . n 
B 2 431 ASP 431 431 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   ARG 2   2   2   ARG ARG C . n 
C 1 3   GLU 3   3   3   GLU GLU C . n 
C 1 4   CYS 4   4   4   CYS CYS C . n 
C 1 5   ILE 5   5   5   ILE ILE C . n 
C 1 6   SER 6   6   6   SER SER C . n 
C 1 7   ILE 7   7   7   ILE ILE C . n 
C 1 8   HIS 8   8   8   HIS HIS C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  GLN 11  11  11  GLN GLN C . n 
C 1 12  ALA 12  12  12  ALA ALA C . n 
C 1 13  GLY 13  13  13  GLY GLY C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  ILE 16  16  16  ILE ILE C . n 
C 1 17  GLY 17  17  17  GLY GLY C . n 
C 1 18  ASN 18  18  18  ASN ASN C . n 
C 1 19  ALA 19  19  19  ALA ALA C . n 
C 1 20  CYS 20  20  20  CYS CYS C . n 
C 1 21  TRP 21  21  21  TRP TRP C . n 
C 1 22  GLU 22  22  22  GLU GLU C . n 
C 1 23  LEU 23  23  23  LEU LEU C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  CYS 25  25  25  CYS CYS C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  HIS 28  28  28  HIS HIS C . n 
C 1 29  GLY 29  29  29  GLY GLY C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  GLN 31  31  31  GLN GLN C . n 
C 1 32  PRO 32  32  32  PRO PRO C . n 
C 1 33  ASP 33  33  33  ASP ASP C . n 
C 1 34  GLY 34  34  34  GLY GLY C . n 
C 1 35  GLN 35  35  35  GLN GLN C . n 
C 1 36  MET 36  36  36  MET MET C . n 
C 1 37  PRO 37  37  37  PRO PRO C . n 
C 1 38  SER 38  38  38  SER SER C . n 
C 1 39  ASP 39  39  39  ASP ASP C . n 
C 1 40  LYS 40  40  40  LYS LYS C . n 
C 1 41  THR 41  41  41  THR THR C . n 
C 1 42  ILE 42  42  42  ILE ILE C . n 
C 1 43  GLY 43  43  43  GLY GLY C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  ASP 46  46  46  ASP ASP C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  PHE 49  49  49  PHE PHE C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  THR 51  51  51  THR THR C . n 
C 1 52  PHE 52  52  52  PHE PHE C . n 
C 1 53  PHE 53  53  53  PHE PHE C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  GLU 55  55  55  GLU GLU C . n 
C 1 56  THR 56  56  56  THR THR C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  ALA 58  58  58  ALA ALA C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  HIS 61  61  61  HIS HIS C . n 
C 1 62  VAL 62  62  62  VAL VAL C . n 
C 1 63  PRO 63  63  63  PRO PRO C . n 
C 1 64  ARG 64  64  64  ARG ARG C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  VAL 66  66  66  VAL VAL C . n 
C 1 67  PHE 67  67  67  PHE PHE C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  GLU 71  71  71  GLU GLU C . n 
C 1 72  PRO 72  72  72  PRO PRO C . n 
C 1 73  THR 73  73  73  THR THR C . n 
C 1 74  VAL 74  74  74  VAL VAL C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  THR 80  80  80  THR THR C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  THR 82  82  82  THR THR C . n 
C 1 83  TYR 83  83  83  TYR TYR C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  GLN 85  85  85  GLN GLN C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  PHE 87  87  87  PHE PHE C . n 
C 1 88  HIS 88  88  88  HIS HIS C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  GLU 90  90  90  GLU GLU C . n 
C 1 91  GLN 91  91  91  GLN GLN C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  ILE 93  93  93  ILE ILE C . n 
C 1 94  THR 94  94  94  THR THR C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  LYS 96  96  96  LYS LYS C . n 
C 1 97  GLU 97  97  97  GLU GLU C . n 
C 1 98  ASP 98  98  98  ASP ASP C . n 
C 1 99  ALA 99  99  99  ALA ALA C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 ASN 101 101 101 ASN ASN C . n 
C 1 102 ASN 102 102 102 ASN ASN C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 ALA 104 104 104 ALA ALA C . n 
C 1 105 ARG 105 105 105 ARG ARG C . n 
C 1 106 GLY 106 106 106 GLY GLY C . n 
C 1 107 HIS 107 107 107 HIS HIS C . n 
C 1 108 TYR 108 108 108 TYR TYR C . n 
C 1 109 THR 109 109 109 THR THR C . n 
C 1 110 ILE 110 110 110 ILE ILE C . n 
C 1 111 GLY 111 111 111 GLY GLY C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 ILE 114 114 114 ILE ILE C . n 
C 1 115 ILE 115 115 115 ILE ILE C . n 
C 1 116 ASP 116 116 116 ASP ASP C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 ASP 120 120 120 ASP ASP C . n 
C 1 121 ARG 121 121 121 ARG ARG C . n 
C 1 122 ILE 122 122 122 ILE ILE C . n 
C 1 123 ARG 123 123 123 ARG ARG C . n 
C 1 124 LYS 124 124 124 LYS LYS C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 ALA 126 126 126 ALA ALA C . n 
C 1 127 ASP 127 127 127 ASP ASP C . n 
C 1 128 GLN 128 128 128 GLN GLN C . n 
C 1 129 CYS 129 129 129 CYS CYS C . n 
C 1 130 THR 130 130 130 THR THR C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 LEU 132 132 132 LEU LEU C . n 
C 1 133 GLN 133 133 133 GLN GLN C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 PHE 135 135 135 PHE PHE C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 VAL 137 137 137 VAL VAL C . n 
C 1 138 PHE 138 138 138 PHE PHE C . n 
C 1 139 HIS 139 139 139 HIS HIS C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 PHE 141 141 141 PHE PHE C . n 
C 1 142 GLY 142 142 142 GLY GLY C . n 
C 1 143 GLY 143 143 143 GLY GLY C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 THR 145 145 145 THR THR C . n 
C 1 146 GLY 146 146 146 GLY GLY C . n 
C 1 147 SER 147 147 147 SER SER C . n 
C 1 148 GLY 148 148 148 GLY GLY C . n 
C 1 149 PHE 149 149 149 PHE PHE C . n 
C 1 150 THR 150 150 150 THR THR C . n 
C 1 151 SER 151 151 151 SER SER C . n 
C 1 152 LEU 152 152 152 LEU LEU C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 MET 154 154 154 MET MET C . n 
C 1 155 GLU 155 155 155 GLU GLU C . n 
C 1 156 ARG 156 156 156 ARG ARG C . n 
C 1 157 LEU 157 157 157 LEU LEU C . n 
C 1 158 SER 158 158 158 SER SER C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 ASP 160 160 160 ASP ASP C . n 
C 1 161 TYR 161 161 161 TYR TYR C . n 
C 1 162 GLY 162 162 162 GLY GLY C . n 
C 1 163 LYS 163 163 163 LYS LYS C . n 
C 1 164 LYS 164 164 164 LYS LYS C . n 
C 1 165 SER 165 165 165 SER SER C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 LEU 167 167 167 LEU LEU C . n 
C 1 168 GLU 168 168 168 GLU GLU C . n 
C 1 169 PHE 169 169 169 PHE PHE C . n 
C 1 170 SER 170 170 170 SER SER C . n 
C 1 171 ILE 171 171 171 ILE ILE C . n 
C 1 172 TYR 172 172 172 TYR TYR C . n 
C 1 173 PRO 173 173 173 PRO PRO C . n 
C 1 174 ALA 174 174 174 ALA ALA C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLN 176 176 176 GLN GLN C . n 
C 1 177 VAL 177 177 177 VAL VAL C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 THR 179 179 179 THR THR C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 VAL 181 181 181 VAL VAL C . n 
C 1 182 VAL 182 182 182 VAL VAL C . n 
C 1 183 GLU 183 183 183 GLU GLU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 TYR 185 185 185 TYR TYR C . n 
C 1 186 ASN 186 186 186 ASN ASN C . n 
C 1 187 SER 187 187 187 SER SER C . n 
C 1 188 ILE 188 188 188 ILE ILE C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 THR 191 191 191 THR THR C . n 
C 1 192 HIS 192 192 192 HIS HIS C . n 
C 1 193 THR 193 193 193 THR THR C . n 
C 1 194 THR 194 194 194 THR THR C . n 
C 1 195 LEU 195 195 195 LEU LEU C . n 
C 1 196 GLU 196 196 196 GLU GLU C . n 
C 1 197 HIS 197 197 197 HIS HIS C . n 
C 1 198 SER 198 198 198 SER SER C . n 
C 1 199 ASP 199 199 199 ASP ASP C . n 
C 1 200 CYS 200 200 200 CYS CYS C . n 
C 1 201 ALA 201 201 201 ALA ALA C . n 
C 1 202 PHE 202 202 202 PHE PHE C . n 
C 1 203 MET 203 203 203 MET MET C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
C 1 205 ASP 205 205 205 ASP ASP C . n 
C 1 206 ASN 206 206 206 ASN ASN C . n 
C 1 207 GLU 207 207 207 GLU GLU C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 ILE 209 209 209 ILE ILE C . n 
C 1 210 TYR 210 210 210 TYR TYR C . n 
C 1 211 ASP 211 211 211 ASP ASP C . n 
C 1 212 ILE 212 212 212 ILE ILE C . n 
C 1 213 CYS 213 213 213 CYS CYS C . n 
C 1 214 ARG 214 214 214 ARG ARG C . n 
C 1 215 ARG 215 215 215 ARG ARG C . n 
C 1 216 ASN 216 216 216 ASN ASN C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 ASP 218 218 218 ASP ASP C . n 
C 1 219 ILE 219 219 219 ILE ILE C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 ARG 221 221 221 ARG ARG C . n 
C 1 222 PRO 222 222 222 PRO PRO C . n 
C 1 223 THR 223 223 223 THR THR C . n 
C 1 224 TYR 224 224 224 TYR TYR C . n 
C 1 225 THR 225 225 225 THR THR C . n 
C 1 226 ASN 226 226 226 ASN ASN C . n 
C 1 227 LEU 227 227 227 LEU LEU C . n 
C 1 228 ASN 228 228 228 ASN ASN C . n 
C 1 229 ARG 229 229 229 ARG ARG C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 SER 232 232 232 SER SER C . n 
C 1 233 GLN 233 233 233 GLN GLN C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 VAL 235 235 235 VAL VAL C . n 
C 1 236 SER 236 236 236 SER SER C . n 
C 1 237 SER 237 237 237 SER SER C . n 
C 1 238 ILE 238 238 238 ILE ILE C . n 
C 1 239 THR 239 239 239 THR THR C . n 
C 1 240 ALA 240 240 240 ALA ALA C . n 
C 1 241 SER 241 241 241 SER SER C . n 
C 1 242 LEU 242 242 242 LEU LEU C . n 
C 1 243 ARG 243 243 243 ARG ARG C . n 
C 1 244 PHE 244 244 244 PHE PHE C . n 
C 1 245 ASP 245 245 245 ASP ASP C . n 
C 1 246 GLY 246 246 246 GLY GLY C . n 
C 1 247 ALA 247 247 247 ALA ALA C . n 
C 1 248 LEU 248 248 248 LEU LEU C . n 
C 1 249 ASN 249 249 249 ASN ASN C . n 
C 1 250 VAL 250 250 250 VAL VAL C . n 
C 1 251 ASP 251 251 251 ASP ASP C . n 
C 1 252 LEU 252 252 252 LEU LEU C . n 
C 1 253 THR 253 253 253 THR THR C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 PHE 255 255 255 PHE PHE C . n 
C 1 256 GLN 256 256 256 GLN GLN C . n 
C 1 257 THR 257 257 257 THR THR C . n 
C 1 258 ASN 258 258 258 ASN ASN C . n 
C 1 259 LEU 259 259 259 LEU LEU C . n 
C 1 260 VAL 260 260 260 VAL VAL C . n 
C 1 261 PRO 261 261 261 PRO PRO C . n 
C 1 262 TYR 262 262 262 TYR TYR C . n 
C 1 263 PRO 263 263 263 PRO PRO C . n 
C 1 264 ARG 264 264 264 ARG ARG C . n 
C 1 265 ILE 265 265 265 ILE ILE C . n 
C 1 266 HIS 266 266 266 HIS HIS C . n 
C 1 267 PHE 267 267 267 PHE PHE C . n 
C 1 268 PRO 268 268 268 PRO PRO C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 ALA 270 270 270 ALA ALA C . n 
C 1 271 THR 271 271 271 THR THR C . n 
C 1 272 TYR 272 272 272 TYR TYR C . n 
C 1 273 ALA 273 273 273 ALA ALA C . n 
C 1 274 PRO 274 274 274 PRO PRO C . n 
C 1 275 VAL 275 275 275 VAL VAL C . n 
C 1 276 ILE 276 276 276 ILE ILE C . n 
C 1 277 SER 277 277 277 SER SER C . n 
C 1 278 ALA 278 278 278 ALA ALA C . n 
C 1 279 GLU 279 279 279 GLU GLU C . n 
C 1 280 LYS 280 280 280 LYS LYS C . n 
C 1 281 ALA 281 281 281 ALA ALA C . n 
C 1 282 TYR 282 282 282 TYR TYR C . n 
C 1 283 HIS 283 283 283 HIS HIS C . n 
C 1 284 GLU 284 284 284 GLU GLU C . n 
C 1 285 GLN 285 285 285 GLN GLN C . n 
C 1 286 LEU 286 286 286 LEU LEU C . n 
C 1 287 SER 287 287 287 SER SER C . n 
C 1 288 VAL 288 288 288 VAL VAL C . n 
C 1 289 ALA 289 289 289 ALA ALA C . n 
C 1 290 GLU 290 290 290 GLU GLU C . n 
C 1 291 ILE 291 291 291 ILE ILE C . n 
C 1 292 THR 292 292 292 THR THR C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 ALA 294 294 294 ALA ALA C . n 
C 1 295 CYS 295 295 295 CYS CYS C . n 
C 1 296 PHE 296 296 296 PHE PHE C . n 
C 1 297 GLU 297 297 297 GLU GLU C . n 
C 1 298 PRO 298 298 298 PRO PRO C . n 
C 1 299 ALA 299 299 299 ALA ALA C . n 
C 1 300 ASN 300 300 300 ASN ASN C . n 
C 1 301 GLN 301 301 301 GLN GLN C . n 
C 1 302 MET 302 302 302 MET MET C . n 
C 1 303 VAL 303 303 303 VAL VAL C . n 
C 1 304 LYS 304 304 304 LYS LYS C . n 
C 1 305 CYS 305 305 305 CYS CYS C . n 
C 1 306 ASP 306 306 306 ASP ASP C . n 
C 1 307 PRO 307 307 307 PRO PRO C . n 
C 1 308 ARG 308 308 308 ARG ARG C . n 
C 1 309 HIS 309 309 309 HIS HIS C . n 
C 1 310 GLY 310 310 310 GLY GLY C . n 
C 1 311 LYS 311 311 311 LYS LYS C . n 
C 1 312 TYR 312 312 312 TYR TYR C . n 
C 1 313 MET 313 313 313 MET MET C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 CYS 315 315 315 CYS CYS C . n 
C 1 316 CYS 316 316 316 CYS CYS C . n 
C 1 317 LEU 317 317 317 LEU LEU C . n 
C 1 318 LEU 318 318 318 LEU LEU C . n 
C 1 319 TYR 319 319 319 TYR TYR C . n 
C 1 320 ARG 320 320 320 ARG ARG C . n 
C 1 321 GLY 321 321 321 GLY GLY C . n 
C 1 322 ASP 322 322 322 ASP ASP C . n 
C 1 323 VAL 323 323 323 VAL VAL C . n 
C 1 324 VAL 324 324 324 VAL VAL C . n 
C 1 325 PRO 325 325 325 PRO PRO C . n 
C 1 326 LYS 326 326 326 LYS LYS C . n 
C 1 327 ASP 327 327 327 ASP ASP C . n 
C 1 328 VAL 328 328 328 VAL VAL C . n 
C 1 329 ASN 329 329 329 ASN ASN C . n 
C 1 330 ALA 330 330 330 ALA ALA C . n 
C 1 331 ALA 331 331 331 ALA ALA C . n 
C 1 332 ILE 332 332 332 ILE ILE C . n 
C 1 333 ALA 333 333 333 ALA ALA C . n 
C 1 334 THR 334 334 334 THR THR C . n 
C 1 335 ILE 335 335 335 ILE ILE C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 THR 337 337 337 THR THR C . n 
C 1 338 LYS 338 338 338 LYS LYS C . n 
C 1 339 ARG 339 339 339 ARG ARG C . n 
C 1 340 SER 340 340 340 SER SER C . n 
C 1 341 ILE 341 341 341 ILE ILE C . n 
C 1 342 GLN 342 342 342 GLN GLN C . n 
C 1 343 PHE 343 343 343 PHE PHE C . n 
C 1 344 VAL 344 344 344 VAL VAL C . n 
C 1 345 ASP 345 345 345 ASP ASP C . n 
C 1 346 TRP 346 346 346 TRP TRP C . n 
C 1 347 CYS 347 347 347 CYS CYS C . n 
C 1 348 PRO 348 348 348 PRO PRO C . n 
C 1 349 THR 349 349 349 THR THR C . n 
C 1 350 GLY 350 350 350 GLY GLY C . n 
C 1 351 PHE 351 351 351 PHE PHE C . n 
C 1 352 LYS 352 352 352 LYS LYS C . n 
C 1 353 VAL 353 353 353 VAL VAL C . n 
C 1 354 GLY 354 354 354 GLY GLY C . n 
C 1 355 ILE 355 355 355 ILE ILE C . n 
C 1 356 ASN 356 356 356 ASN ASN C . n 
C 1 357 TYR 357 357 357 TYR TYR C . n 
C 1 358 GLN 358 358 358 GLN GLN C . n 
C 1 359 PRO 359 359 359 PRO PRO C . n 
C 1 360 PRO 360 360 360 PRO PRO C . n 
C 1 361 THR 361 361 361 THR THR C . n 
C 1 362 VAL 362 362 362 VAL VAL C . n 
C 1 363 VAL 363 363 363 VAL VAL C . n 
C 1 364 PRO 364 364 364 PRO PRO C . n 
C 1 365 GLY 365 365 365 GLY GLY C . n 
C 1 366 GLY 366 366 366 GLY GLY C . n 
C 1 367 ASP 367 367 367 ASP ASP C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 ALA 369 369 369 ALA ALA C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 VAL 371 371 371 VAL VAL C . n 
C 1 372 GLN 372 372 372 GLN GLN C . n 
C 1 373 ARG 373 373 373 ARG ARG C . n 
C 1 374 ALA 374 374 374 ALA ALA C . n 
C 1 375 VAL 375 375 375 VAL VAL C . n 
C 1 376 CYS 376 376 376 CYS CYS C . n 
C 1 377 MET 377 377 377 MET MET C . n 
C 1 378 LEU 378 378 378 LEU LEU C . n 
C 1 379 SER 379 379 379 SER SER C . n 
C 1 380 ASN 380 380 380 ASN ASN C . n 
C 1 381 THR 381 381 381 THR THR C . n 
C 1 382 THR 382 382 382 THR THR C . n 
C 1 383 ALA 383 383 383 ALA ALA C . n 
C 1 384 ILE 384 384 384 ILE ILE C . n 
C 1 385 ALA 385 385 385 ALA ALA C . n 
C 1 386 GLU 386 386 386 GLU GLU C . n 
C 1 387 ALA 387 387 387 ALA ALA C . n 
C 1 388 TRP 388 388 388 TRP TRP C . n 
C 1 389 ALA 389 389 389 ALA ALA C . n 
C 1 390 ARG 390 390 390 ARG ARG C . n 
C 1 391 LEU 391 391 391 LEU LEU C . n 
C 1 392 ASP 392 392 392 ASP ASP C . n 
C 1 393 HIS 393 393 393 HIS HIS C . n 
C 1 394 LYS 394 394 394 LYS LYS C . n 
C 1 395 PHE 395 395 395 PHE PHE C . n 
C 1 396 ASP 396 396 396 ASP ASP C . n 
C 1 397 LEU 397 397 397 LEU LEU C . n 
C 1 398 MET 398 398 398 MET MET C . n 
C 1 399 TYR 399 399 399 TYR TYR C . n 
C 1 400 ALA 400 400 400 ALA ALA C . n 
C 1 401 LYS 401 401 401 LYS LYS C . n 
C 1 402 ARG 402 402 402 ARG ARG C . n 
C 1 403 ALA 403 403 403 ALA ALA C . n 
C 1 404 PHE 404 404 404 PHE PHE C . n 
C 1 405 VAL 405 405 405 VAL VAL C . n 
C 1 406 HIS 406 406 406 HIS HIS C . n 
C 1 407 TRP 407 407 407 TRP TRP C . n 
C 1 408 TYR 408 408 408 TYR TYR C . n 
C 1 409 VAL 409 409 409 VAL VAL C . n 
C 1 410 GLY 410 410 410 GLY GLY C . n 
C 1 411 GLU 411 411 411 GLU GLU C . n 
C 1 412 GLY 412 412 412 GLY GLY C . n 
C 1 413 MET 413 413 413 MET MET C . n 
C 1 414 GLU 414 414 414 GLU GLU C . n 
C 1 415 GLU 415 415 415 GLU GLU C . n 
C 1 416 GLY 416 416 416 GLY GLY C . n 
C 1 417 GLU 417 417 417 GLU GLU C . n 
C 1 418 PHE 418 418 418 PHE PHE C . n 
C 1 419 SER 419 419 419 SER SER C . n 
C 1 420 GLU 420 420 420 GLU GLU C . n 
C 1 421 ALA 421 421 421 ALA ALA C . n 
C 1 422 ARG 422 422 422 ARG ARG C . n 
C 1 423 GLU 423 423 423 GLU GLU C . n 
C 1 424 ASP 424 424 424 ASP ASP C . n 
C 1 425 MET 425 425 425 MET MET C . n 
C 1 426 ALA 426 426 426 ALA ALA C . n 
C 1 427 ALA 427 427 427 ALA ALA C . n 
C 1 428 LEU 428 428 428 LEU LEU C . n 
C 1 429 GLU 429 429 429 GLU GLU C . n 
C 1 430 LYS 430 430 430 LYS LYS C . n 
C 1 431 ASP 431 431 431 ASP ASP C . n 
C 1 432 TYR 432 432 432 TYR TYR C . n 
C 1 433 GLU 433 433 433 GLU GLU C . n 
C 1 434 GLU 434 434 434 GLU GLU C . n 
C 1 435 VAL 435 435 435 VAL VAL C . n 
C 1 436 GLY 436 436 436 GLY GLY C . n 
C 1 437 VAL 437 437 437 VAL VAL C . n 
C 1 438 ASP 438 438 438 ASP ASP C . n 
C 1 439 SER 439 439 439 SER SER C . n 
C 1 440 VAL 440 440 440 VAL VAL C . n 
D 2 1   MET 1   1   1   MET MET D . n 
D 2 2   ARG 2   2   2   ARG ARG D . n 
D 2 3   GLU 3   3   3   GLU GLU D . n 
D 2 4   ILE 4   4   4   ILE ILE D . n 
D 2 5   VAL 5   5   5   VAL VAL D . n 
D 2 6   HIS 6   6   6   HIS HIS D . n 
D 2 7   ILE 7   7   7   ILE ILE D . n 
D 2 8   GLN 8   8   8   GLN GLN D . n 
D 2 9   ALA 9   9   9   ALA ALA D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  GLN 11  11  11  GLN GLN D . n 
D 2 12  CYS 12  12  12  CYS CYS D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  ASN 14  14  14  ASN ASN D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  ILE 16  16  16  ILE ILE D . n 
D 2 17  GLY 17  17  17  GLY GLY D . n 
D 2 18  ALA 18  18  18  ALA ALA D . n 
D 2 19  LYS 19  19  19  LYS LYS D . n 
D 2 20  PHE 20  20  20  PHE PHE D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  GLU 22  22  22  GLU GLU D . n 
D 2 23  VAL 23  23  23  VAL VAL D . n 
D 2 24  ILE 24  24  24  ILE ILE D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  ASP 26  26  26  ASP ASP D . n 
D 2 27  GLU 27  27  27  GLU GLU D . n 
D 2 28  HIS 28  28  28  HIS HIS D . n 
D 2 29  GLY 29  29  29  GLY GLY D . n 
D 2 30  ILE 30  30  30  ILE ILE D . n 
D 2 31  ASP 31  31  31  ASP ASP D . n 
D 2 32  PRO 32  32  32  PRO PRO D . n 
D 2 33  THR 33  33  33  THR THR D . n 
D 2 34  GLY 34  34  34  GLY GLY D . n 
D 2 35  SER 35  35  35  SER SER D . n 
D 2 36  TYR 36  36  36  TYR TYR D . n 
D 2 37  HIS 37  37  37  HIS HIS D . n 
D 2 38  GLY 38  38  38  GLY GLY D . n 
D 2 39  ASP 39  39  39  ASP ASP D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  ASP 41  41  41  ASP ASP D . n 
D 2 42  LEU 42  42  42  LEU LEU D . n 
D 2 43  GLN 43  43  43  GLN GLN D . n 
D 2 44  LEU 44  44  44  LEU LEU D . n 
D 2 45  GLU 45  45  45  GLU GLU D . n 
D 2 46  ARG 46  46  46  ARG ARG D . n 
D 2 47  ILE 47  47  47  ILE ILE D . n 
D 2 48  ASN 48  48  48  ASN ASN D . n 
D 2 49  VAL 49  49  49  VAL VAL D . n 
D 2 50  TYR 50  50  50  TYR TYR D . n 
D 2 51  TYR 51  51  51  TYR TYR D . n 
D 2 52  ASN 52  52  52  ASN ASN D . n 
D 2 53  GLU 53  53  53  GLU GLU D . n 
D 2 54  ALA 54  54  54  ALA ALA D . n 
D 2 55  THR 55  55  55  THR THR D . n 
D 2 56  GLY 56  56  56  GLY GLY D . n 
D 2 57  ASN 57  57  57  ASN ASN D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  TYR 59  59  59  TYR TYR D . n 
D 2 60  VAL 60  60  60  VAL VAL D . n 
D 2 61  PRO 61  61  61  PRO PRO D . n 
D 2 62  ARG 62  62  62  ARG ARG D . n 
D 2 63  ALA 63  63  63  ALA ALA D . n 
D 2 64  ILE 64  64  64  ILE ILE D . n 
D 2 65  LEU 65  65  65  LEU LEU D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  ASP 67  67  67  ASP ASP D . n 
D 2 68  LEU 68  68  68  LEU LEU D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PRO 70  70  70  PRO PRO D . n 
D 2 71  GLY 71  71  71  GLY GLY D . n 
D 2 72  THR 72  72  72  THR THR D . n 
D 2 73  MET 73  73  73  MET MET D . n 
D 2 74  ASP 74  74  74  ASP ASP D . n 
D 2 75  SER 75  75  75  SER SER D . n 
D 2 76  VAL 76  76  76  VAL VAL D . n 
D 2 77  ARG 77  77  77  ARG ARG D . n 
D 2 78  SER 78  78  78  SER SER D . n 
D 2 79  GLY 79  79  79  GLY GLY D . n 
D 2 80  PRO 80  80  80  PRO PRO D . n 
D 2 81  PHE 81  81  81  PHE PHE D . n 
D 2 82  GLY 82  82  82  GLY GLY D . n 
D 2 83  GLN 83  83  83  GLN GLN D . n 
D 2 84  ILE 84  84  84  ILE ILE D . n 
D 2 85  PHE 85  85  85  PHE PHE D . n 
D 2 86  ARG 86  86  86  ARG ARG D . n 
D 2 87  PRO 87  87  87  PRO PRO D . n 
D 2 88  ASP 88  88  88  ASP ASP D . n 
D 2 89  ASN 89  89  89  ASN ASN D . n 
D 2 90  PHE 90  90  90  PHE PHE D . n 
D 2 91  VAL 91  91  91  VAL VAL D . n 
D 2 92  PHE 92  92  92  PHE PHE D . n 
D 2 93  GLY 93  93  93  GLY GLY D . n 
D 2 94  GLN 94  94  94  GLN GLN D . n 
D 2 95  SER 95  95  95  SER SER D . n 
D 2 96  GLY 96  96  96  GLY GLY D . n 
D 2 97  ALA 97  97  97  ALA ALA D . n 
D 2 98  GLY 98  98  98  GLY GLY D . n 
D 2 99  ASN 99  99  99  ASN ASN D . n 
D 2 100 ASN 100 100 100 ASN ASN D . n 
D 2 101 TRP 101 101 101 TRP TRP D . n 
D 2 102 ALA 102 102 102 ALA ALA D . n 
D 2 103 LYS 103 103 103 LYS LYS D . n 
D 2 104 GLY 104 104 104 GLY GLY D . n 
D 2 105 HIS 105 105 105 HIS HIS D . n 
D 2 106 TYR 106 106 106 TYR TYR D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 GLU 108 108 108 GLU GLU D . n 
D 2 109 GLY 109 109 109 GLY GLY D . n 
D 2 110 ALA 110 110 110 ALA ALA D . n 
D 2 111 GLU 111 111 111 GLU GLU D . n 
D 2 112 LEU 112 112 112 LEU LEU D . n 
D 2 113 VAL 113 113 113 VAL VAL D . n 
D 2 114 ASP 114 114 114 ASP ASP D . n 
D 2 115 SER 115 115 115 SER SER D . n 
D 2 116 VAL 116 116 116 VAL VAL D . n 
D 2 117 LEU 117 117 117 LEU LEU D . n 
D 2 118 ASP 118 118 118 ASP ASP D . n 
D 2 119 VAL 119 119 119 VAL VAL D . n 
D 2 120 VAL 120 120 120 VAL VAL D . n 
D 2 121 ARG 121 121 121 ARG ARG D . n 
D 2 122 LYS 122 122 122 LYS LYS D . n 
D 2 123 GLU 123 123 123 GLU GLU D . n 
D 2 124 SER 124 124 124 SER SER D . n 
D 2 125 GLU 125 125 125 GLU GLU D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 CYS 127 127 127 CYS CYS D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 CYS 129 129 129 CYS CYS D . n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 GLN 131 131 131 GLN GLN D . n 
D 2 132 GLY 132 132 132 GLY GLY D . n 
D 2 133 PHE 133 133 133 PHE PHE D . n 
D 2 134 GLN 134 134 134 GLN GLN D . n 
D 2 135 LEU 135 135 135 LEU LEU D . n 
D 2 136 THR 136 136 136 THR THR D . n 
D 2 137 HIS 137 137 137 HIS HIS D . n 
D 2 138 SER 138 138 138 SER SER D . n 
D 2 139 LEU 139 139 139 LEU LEU D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 GLY 141 141 141 GLY GLY D . n 
D 2 142 GLY 142 142 142 GLY GLY D . n 
D 2 143 THR 143 143 143 THR THR D . n 
D 2 144 GLY 144 144 144 GLY GLY D . n 
D 2 145 SER 145 145 145 SER SER D . n 
D 2 146 GLY 146 146 146 GLY GLY D . n 
D 2 147 MET 147 147 147 MET MET D . n 
D 2 148 GLY 148 148 148 GLY GLY D . n 
D 2 149 THR 149 149 149 THR THR D . n 
D 2 150 LEU 150 150 150 LEU LEU D . n 
D 2 151 LEU 151 151 151 LEU LEU D . n 
D 2 152 ILE 152 152 152 ILE ILE D . n 
D 2 153 SER 153 153 153 SER SER D . n 
D 2 154 LYS 154 154 154 LYS LYS D . n 
D 2 155 ILE 155 155 155 ILE ILE D . n 
D 2 156 ARG 156 156 156 ARG ARG D . n 
D 2 157 GLU 157 157 157 GLU GLU D . n 
D 2 158 GLU 158 158 158 GLU GLU D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 ASP 161 161 161 ASP ASP D . n 
D 2 162 ARG 162 162 162 ARG ARG D . n 
D 2 163 ILE 163 163 163 ILE ILE D . n 
D 2 164 MET 164 164 164 MET MET D . n 
D 2 165 ASN 165 165 165 ASN ASN D . n 
D 2 166 THR 166 166 166 THR THR D . n 
D 2 167 PHE 167 167 167 PHE PHE D . n 
D 2 168 SER 168 168 168 SER SER D . n 
D 2 169 VAL 169 169 169 VAL VAL D . n 
D 2 170 MET 170 170 170 MET MET D . n 
D 2 171 PRO 171 171 171 PRO PRO D . n 
D 2 172 SER 172 172 172 SER SER D . n 
D 2 173 PRO 173 173 173 PRO PRO D . n 
D 2 174 LYS 174 174 174 LYS LYS D . n 
D 2 175 VAL 175 175 175 VAL VAL D . n 
D 2 176 SER 176 176 176 SER SER D . n 
D 2 177 ASP 177 177 177 ASP ASP D . n 
D 2 178 THR 178 178 178 THR THR D . n 
D 2 179 VAL 179 179 179 VAL VAL D . n 
D 2 180 VAL 180 180 180 VAL VAL D . n 
D 2 181 GLU 181 181 181 GLU GLU D . n 
D 2 182 PRO 182 182 182 PRO PRO D . n 
D 2 183 TYR 183 183 183 TYR TYR D . n 
D 2 184 ASN 184 184 184 ASN ASN D . n 
D 2 185 ALA 185 185 185 ALA ALA D . n 
D 2 186 THR 186 186 186 THR THR D . n 
D 2 187 LEU 187 187 187 LEU LEU D . n 
D 2 188 SER 188 188 188 SER SER D . n 
D 2 189 VAL 189 189 189 VAL VAL D . n 
D 2 190 HIS 190 190 190 HIS HIS D . n 
D 2 191 GLN 191 191 191 GLN GLN D . n 
D 2 192 LEU 192 192 192 LEU LEU D . n 
D 2 193 VAL 193 193 193 VAL VAL D . n 
D 2 194 GLU 194 194 194 GLU GLU D . n 
D 2 195 ASN 195 195 195 ASN ASN D . n 
D 2 196 THR 196 196 196 THR THR D . n 
D 2 197 ASP 197 197 197 ASP ASP D . n 
D 2 198 GLU 198 198 198 GLU GLU D . n 
D 2 199 THR 199 199 199 THR THR D . n 
D 2 200 TYR 200 200 200 TYR TYR D . n 
D 2 201 CYS 201 201 201 CYS CYS D . n 
D 2 202 ILE 202 202 202 ILE ILE D . n 
D 2 203 ASP 203 203 203 ASP ASP D . n 
D 2 204 ASN 204 204 204 ASN ASN D . n 
D 2 205 GLU 205 205 205 GLU GLU D . n 
D 2 206 ALA 206 206 206 ALA ALA D . n 
D 2 207 LEU 207 207 207 LEU LEU D . n 
D 2 208 TYR 208 208 208 TYR TYR D . n 
D 2 209 ASP 209 209 209 ASP ASP D . n 
D 2 210 ILE 210 210 210 ILE ILE D . n 
D 2 211 CYS 211 211 211 CYS CYS D . n 
D 2 212 PHE 212 212 212 PHE PHE D . n 
D 2 213 ARG 213 213 213 ARG ARG D . n 
D 2 214 THR 214 214 214 THR THR D . n 
D 2 215 LEU 215 215 215 LEU LEU D . n 
D 2 216 LYS 216 216 216 LYS LYS D . n 
D 2 217 LEU 217 217 217 LEU LEU D . n 
D 2 218 THR 218 218 218 THR THR D . n 
D 2 219 THR 219 219 219 THR THR D . n 
D 2 220 PRO 220 220 220 PRO PRO D . n 
D 2 221 THR 221 221 221 THR THR D . n 
D 2 222 TYR 222 222 222 TYR TYR D . n 
D 2 223 GLY 223 223 223 GLY GLY D . n 
D 2 224 ASP 224 224 224 ASP ASP D . n 
D 2 225 LEU 225 225 225 LEU LEU D . n 
D 2 226 ASN 226 226 226 ASN ASN D . n 
D 2 227 HIS 227 227 227 HIS HIS D . n 
D 2 228 LEU 228 228 228 LEU LEU D . n 
D 2 229 VAL 229 229 229 VAL VAL D . n 
D 2 230 SER 230 230 230 SER SER D . n 
D 2 231 ALA 231 231 231 ALA ALA D . n 
D 2 232 THR 232 232 232 THR THR D . n 
D 2 233 MET 233 233 233 MET MET D . n 
D 2 234 SER 234 234 234 SER SER D . n 
D 2 235 GLY 235 235 235 GLY GLY D . n 
D 2 236 VAL 236 236 236 VAL VAL D . n 
D 2 237 THR 237 237 237 THR THR D . n 
D 2 238 THR 238 238 238 THR THR D . n 
D 2 239 CYS 239 239 239 CYS CYS D . n 
D 2 240 LEU 240 240 240 LEU LEU D . n 
D 2 241 ARG 241 241 241 ARG ARG D . n 
D 2 242 PHE 242 242 242 PHE PHE D . n 
D 2 243 PRO 243 243 243 PRO PRO D . n 
D 2 244 GLY 244 244 244 GLY GLY D . n 
D 2 245 GLN 245 245 245 GLN GLN D . n 
D 2 246 LEU 246 246 246 LEU LEU D . n 
D 2 247 ASN 247 247 247 ASN ASN D . n 
D 2 248 ALA 248 248 248 ALA ALA D . n 
D 2 249 ASP 249 249 249 ASP ASP D . n 
D 2 250 LEU 250 250 250 LEU LEU D . n 
D 2 251 ARG 251 251 251 ARG ARG D . n 
D 2 252 LYS 252 252 252 LYS LYS D . n 
D 2 253 LEU 253 253 253 LEU LEU D . n 
D 2 254 ALA 254 254 254 ALA ALA D . n 
D 2 255 VAL 255 255 255 VAL VAL D . n 
D 2 256 ASN 256 256 256 ASN ASN D . n 
D 2 257 MET 257 257 257 MET MET D . n 
D 2 258 VAL 258 258 258 VAL VAL D . n 
D 2 259 PRO 259 259 259 PRO PRO D . n 
D 2 260 PHE 260 260 260 PHE PHE D . n 
D 2 261 PRO 261 261 261 PRO PRO D . n 
D 2 262 ARG 262 262 262 ARG ARG D . n 
D 2 263 LEU 263 263 263 LEU LEU D . n 
D 2 264 HIS 264 264 264 HIS HIS D . n 
D 2 265 PHE 265 265 265 PHE PHE D . n 
D 2 266 PHE 266 266 266 PHE PHE D . n 
D 2 267 MET 267 267 267 MET MET D . n 
D 2 268 PRO 268 268 268 PRO PRO D . n 
D 2 269 GLY 269 269 269 GLY GLY D . n 
D 2 270 PHE 270 270 270 PHE PHE D . n 
D 2 271 ALA 271 271 271 ALA ALA D . n 
D 2 272 PRO 272 272 272 PRO PRO D . n 
D 2 273 LEU 273 273 273 LEU LEU D . n 
D 2 274 THR 274 274 ?   ?   ?   D . n 
D 2 275 SER 275 275 ?   ?   ?   D . n 
D 2 276 ARG 276 276 ?   ?   ?   D . n 
D 2 277 GLY 277 277 ?   ?   ?   D . n 
D 2 278 SER 278 278 ?   ?   ?   D . n 
D 2 279 GLN 279 279 ?   ?   ?   D . n 
D 2 280 GLN 280 280 ?   ?   ?   D . n 
D 2 281 TYR 281 281 ?   ?   ?   D . n 
D 2 282 ARG 282 282 ?   ?   ?   D . n 
D 2 283 ALA 283 283 ?   ?   ?   D . n 
D 2 284 LEU 284 284 284 LEU LEU D . n 
D 2 285 THR 285 285 285 THR THR D . n 
D 2 286 VAL 286 286 286 VAL VAL D . n 
D 2 287 PRO 287 287 287 PRO PRO D . n 
D 2 288 GLU 288 288 288 GLU GLU D . n 
D 2 289 LEU 289 289 289 LEU LEU D . n 
D 2 290 THR 290 290 290 THR THR D . n 
D 2 291 GLN 291 291 291 GLN GLN D . n 
D 2 292 GLN 292 292 292 GLN GLN D . n 
D 2 293 MET 293 293 293 MET MET D . n 
D 2 294 PHE 294 294 294 PHE PHE D . n 
D 2 295 ASP 295 295 295 ASP ASP D . n 
D 2 296 SER 296 296 296 SER SER D . n 
D 2 297 LYS 297 297 297 LYS LYS D . n 
D 2 298 ASN 298 298 298 ASN ASN D . n 
D 2 299 MET 299 299 299 MET MET D . n 
D 2 300 MET 300 300 300 MET MET D . n 
D 2 301 ALA 301 301 301 ALA ALA D . n 
D 2 302 ALA 302 302 302 ALA ALA D . n 
D 2 303 CYS 303 303 303 CYS CYS D . n 
D 2 304 ASP 304 304 304 ASP ASP D . n 
D 2 305 PRO 305 305 305 PRO PRO D . n 
D 2 306 ARG 306 306 306 ARG ARG D . n 
D 2 307 HIS 307 307 307 HIS HIS D . n 
D 2 308 GLY 308 308 308 GLY GLY D . n 
D 2 309 ARG 309 309 309 ARG ARG D . n 
D 2 310 TYR 310 310 310 TYR TYR D . n 
D 2 311 LEU 311 311 311 LEU LEU D . n 
D 2 312 THR 312 312 312 THR THR D . n 
D 2 313 VAL 313 313 313 VAL VAL D . n 
D 2 314 ALA 314 314 314 ALA ALA D . n 
D 2 315 ALA 315 315 315 ALA ALA D . n 
D 2 316 ILE 316 316 316 ILE ILE D . n 
D 2 317 PHE 317 317 317 PHE PHE D . n 
D 2 318 ARG 318 318 318 ARG ARG D . n 
D 2 319 GLY 319 319 319 GLY GLY D . n 
D 2 320 ARG 320 320 320 ARG ARG D . n 
D 2 321 MET 321 321 321 MET MET D . n 
D 2 322 SER 322 322 322 SER SER D . n 
D 2 323 MET 323 323 323 MET MET D . n 
D 2 324 LYS 324 324 324 LYS LYS D . n 
D 2 325 GLU 325 325 325 GLU GLU D . n 
D 2 326 VAL 326 326 326 VAL VAL D . n 
D 2 327 ASP 327 327 327 ASP ASP D . n 
D 2 328 GLU 328 328 328 GLU GLU D . n 
D 2 329 GLN 329 329 329 GLN GLN D . n 
D 2 330 MET 330 330 330 MET MET D . n 
D 2 331 LEU 331 331 331 LEU LEU D . n 
D 2 332 ASN 332 332 332 ASN ASN D . n 
D 2 333 VAL 333 333 333 VAL VAL D . n 
D 2 334 GLN 334 334 334 GLN GLN D . n 
D 2 335 ASN 335 335 335 ASN ASN D . n 
D 2 336 LYS 336 336 336 LYS LYS D . n 
D 2 337 ASN 337 337 337 ASN ASN D . n 
D 2 338 SER 338 338 338 SER SER D . n 
D 2 339 SER 339 339 339 SER SER D . n 
D 2 340 TYR 340 340 340 TYR TYR D . n 
D 2 341 PHE 341 341 341 PHE PHE D . n 
D 2 342 VAL 342 342 342 VAL VAL D . n 
D 2 343 GLU 343 343 343 GLU GLU D . n 
D 2 344 TRP 344 344 344 TRP TRP D . n 
D 2 345 ILE 345 345 345 ILE ILE D . n 
D 2 346 PRO 346 346 346 PRO PRO D . n 
D 2 347 ASN 347 347 347 ASN ASN D . n 
D 2 348 ASN 348 348 348 ASN ASN D . n 
D 2 349 VAL 349 349 349 VAL VAL D . n 
D 2 350 LYS 350 350 350 LYS LYS D . n 
D 2 351 THR 351 351 351 THR THR D . n 
D 2 352 ALA 352 352 352 ALA ALA D . n 
D 2 353 VAL 353 353 353 VAL VAL D . n 
D 2 354 CYS 354 354 354 CYS CYS D . n 
D 2 355 ASP 355 355 355 ASP ASP D . n 
D 2 356 ILE 356 356 356 ILE ILE D . n 
D 2 357 PRO 357 357 357 PRO PRO D . n 
D 2 358 PRO 358 358 358 PRO PRO D . n 
D 2 359 ARG 359 359 359 ARG ARG D . n 
D 2 360 GLY 360 360 360 GLY GLY D . n 
D 2 361 LEU 361 361 361 LEU LEU D . n 
D 2 362 LYS 362 362 362 LYS LYS D . n 
D 2 363 MET 363 363 363 MET MET D . n 
D 2 364 SER 364 364 364 SER SER D . n 
D 2 365 ALA 365 365 365 ALA ALA D . n 
D 2 366 THR 366 366 366 THR THR D . n 
D 2 367 PHE 367 367 367 PHE PHE D . n 
D 2 368 ILE 368 368 368 ILE ILE D . n 
D 2 369 GLY 369 369 369 GLY GLY D . n 
D 2 370 ASN 370 370 370 ASN ASN D . n 
D 2 371 SER 371 371 371 SER SER D . n 
D 2 372 THR 372 372 372 THR THR D . n 
D 2 373 ALA 373 373 373 ALA ALA D . n 
D 2 374 ILE 374 374 374 ILE ILE D . n 
D 2 375 GLN 375 375 375 GLN GLN D . n 
D 2 376 GLU 376 376 376 GLU GLU D . n 
D 2 377 LEU 377 377 377 LEU LEU D . n 
D 2 378 PHE 378 378 378 PHE PHE D . n 
D 2 379 LYS 379 379 379 LYS LYS D . n 
D 2 380 ARG 380 380 380 ARG ARG D . n 
D 2 381 ILE 381 381 381 ILE ILE D . n 
D 2 382 SER 382 382 382 SER SER D . n 
D 2 383 GLU 383 383 383 GLU GLU D . n 
D 2 384 GLN 384 384 384 GLN GLN D . n 
D 2 385 PHE 385 385 385 PHE PHE D . n 
D 2 386 THR 386 386 386 THR THR D . n 
D 2 387 ALA 387 387 387 ALA ALA D . n 
D 2 388 MET 388 388 388 MET MET D . n 
D 2 389 PHE 389 389 389 PHE PHE D . n 
D 2 390 ARG 390 390 390 ARG ARG D . n 
D 2 391 ARG 391 391 391 ARG ARG D . n 
D 2 392 LYS 392 392 392 LYS LYS D . n 
D 2 393 ALA 393 393 393 ALA ALA D . n 
D 2 394 PHE 394 394 394 PHE PHE D . n 
D 2 395 LEU 395 395 395 LEU LEU D . n 
D 2 396 HIS 396 396 396 HIS HIS D . n 
D 2 397 TRP 397 397 397 TRP TRP D . n 
D 2 398 TYR 398 398 398 TYR TYR D . n 
D 2 399 THR 399 399 399 THR THR D . n 
D 2 400 GLY 400 400 400 GLY GLY D . n 
D 2 401 GLU 401 401 401 GLU GLU D . n 
D 2 402 GLY 402 402 402 GLY GLY D . n 
D 2 403 MET 403 403 403 MET MET D . n 
D 2 404 ASP 404 404 404 ASP ASP D . n 
D 2 405 GLU 405 405 405 GLU GLU D . n 
D 2 406 MET 406 406 406 MET MET D . n 
D 2 407 GLU 407 407 407 GLU GLU D . n 
D 2 408 PHE 408 408 408 PHE PHE D . n 
D 2 409 THR 409 409 409 THR THR D . n 
D 2 410 GLU 410 410 410 GLU GLU D . n 
D 2 411 ALA 411 411 411 ALA ALA D . n 
D 2 412 GLU 412 412 412 GLU GLU D . n 
D 2 413 SER 413 413 413 SER SER D . n 
D 2 414 ASN 414 414 414 ASN ASN D . n 
D 2 415 MET 415 415 415 MET MET D . n 
D 2 416 ASN 416 416 416 ASN ASN D . n 
D 2 417 ASP 417 417 417 ASP ASP D . n 
D 2 418 LEU 418 418 418 LEU LEU D . n 
D 2 419 VAL 419 419 419 VAL VAL D . n 
D 2 420 SER 420 420 420 SER SER D . n 
D 2 421 GLU 421 421 421 GLU GLU D . n 
D 2 422 TYR 422 422 422 TYR TYR D . n 
D 2 423 GLN 423 423 423 GLN GLN D . n 
D 2 424 GLN 424 424 424 GLN GLN D . n 
D 2 425 TYR 425 425 425 TYR TYR D . n 
D 2 426 GLN 426 426 426 GLN GLN D . n 
D 2 427 ASP 427 427 427 ASP ASP D . n 
D 2 428 ALA 428 428 428 ALA ALA D . n 
D 2 429 THR 429 429 429 THR THR D . n 
D 2 430 ALA 430 430 430 ALA ALA D . n 
D 2 431 ASP 431 431 431 ASP ASP D . n 
E 3 1   MET 1   6   6   MET MET E . n 
E 3 2   GLU 2   7   7   GLU GLU E . n 
E 3 3   VAL 3   8   8   VAL VAL E . n 
E 3 4   ILE 4   9   9   ILE ILE E . n 
E 3 5   GLU 5   10  10  GLU GLU E . n 
E 3 6   LEU 6   11  11  LEU LEU E . n 
E 3 7   ASN 7   12  12  ASN ASN E . n 
E 3 8   LYS 8   13  13  LYS LYS E . n 
E 3 9   CYS 9   14  14  CYS CYS E . n 
E 3 10  THR 10  15  15  THR THR E . n 
E 3 11  SER 11  16  16  SER SER E . n 
E 3 12  GLY 12  17  17  GLY GLY E . n 
E 3 13  GLN 13  18  18  GLN GLN E . n 
E 3 14  SER 14  19  19  SER SER E . n 
E 3 15  PHE 15  20  20  PHE PHE E . n 
E 3 16  GLU 16  21  21  GLU GLU E . n 
E 3 17  VAL 17  22  22  VAL VAL E . n 
E 3 18  ILE 18  23  23  ILE ILE E . n 
E 3 19  LEU 19  24  24  LEU LEU E . n 
E 3 20  LYS 20  25  25  LYS LYS E . n 
E 3 21  PRO 21  26  26  PRO PRO E . n 
E 3 22  PRO 22  27  27  PRO PRO E . n 
E 3 23  SER 23  28  28  SER SER E . n 
E 3 24  PHE 24  29  ?   ?   ?   E . n 
E 3 25  ASP 25  30  ?   ?   ?   E . n 
E 3 26  GLY 26  31  ?   ?   ?   E . n 
E 3 27  VAL 27  32  ?   ?   ?   E . n 
E 3 28  PRO 28  33  ?   ?   ?   E . n 
E 3 29  GLU 29  34  ?   ?   ?   E . n 
E 3 30  PHE 30  35  ?   ?   ?   E . n 
E 3 31  ASN 31  36  ?   ?   ?   E . n 
E 3 32  ALA 32  37  ?   ?   ?   E . n 
E 3 33  SER 33  38  ?   ?   ?   E . n 
E 3 34  LEU 34  39  ?   ?   ?   E . n 
E 3 35  PRO 35  40  ?   ?   ?   E . n 
E 3 36  ARG 36  41  ?   ?   ?   E . n 
E 3 37  ARG 37  42  ?   ?   ?   E . n 
E 3 38  ARG 38  43  ?   ?   ?   E . n 
E 3 39  ASP 39  44  44  ASP ASP E . n 
E 3 40  PRO 40  45  45  PRO PRO E . n 
E 3 41  SER 41  46  46  SER SER E . n 
E 3 42  LEU 42  47  47  LEU LEU E . n 
E 3 43  GLU 43  48  48  GLU GLU E . n 
E 3 44  GLU 44  49  49  GLU GLU E . n 
E 3 45  ILE 45  50  50  ILE ILE E . n 
E 3 46  GLN 46  51  51  GLN GLN E . n 
E 3 47  LYS 47  52  52  LYS LYS E . n 
E 3 48  LYS 48  53  53  LYS LYS E . n 
E 3 49  LEU 49  54  54  LEU LEU E . n 
E 3 50  GLU 50  55  55  GLU GLU E . n 
E 3 51  ALA 51  56  56  ALA ALA E . n 
E 3 52  ALA 52  57  57  ALA ALA E . n 
E 3 53  GLU 53  58  58  GLU GLU E . n 
E 3 54  GLU 54  59  59  GLU GLU E . n 
E 3 55  ARG 55  60  60  ARG ARG E . n 
E 3 56  ARG 56  61  61  ARG ARG E . n 
E 3 57  LYS 57  62  62  LYS LYS E . n 
E 3 58  TYR 58  63  63  TYR TYR E . n 
E 3 59  GLN 59  64  64  GLN GLN E . n 
E 3 60  GLU 60  65  65  GLU GLU E . n 
E 3 61  ALA 61  66  66  ALA ALA E . n 
E 3 62  GLU 62  67  67  GLU GLU E . n 
E 3 63  LEU 63  68  68  LEU LEU E . n 
E 3 64  LEU 64  69  69  LEU LEU E . n 
E 3 65  LYS 65  70  70  LYS LYS E . n 
E 3 66  HIS 66  71  71  HIS HIS E . n 
E 3 67  LEU 67  72  72  LEU LEU E . n 
E 3 68  ALA 68  73  73  ALA ALA E . n 
E 3 69  GLU 69  74  74  GLU GLU E . n 
E 3 70  LYS 70  75  75  LYS LYS E . n 
E 3 71  ARG 71  76  76  ARG ARG E . n 
E 3 72  GLU 72  77  77  GLU GLU E . n 
E 3 73  HIS 73  78  78  HIS HIS E . n 
E 3 74  GLU 74  79  79  GLU GLU E . n 
E 3 75  ARG 75  80  80  ARG ARG E . n 
E 3 76  GLU 76  81  81  GLU GLU E . n 
E 3 77  VAL 77  82  82  VAL VAL E . n 
E 3 78  ILE 78  83  83  ILE ILE E . n 
E 3 79  GLN 79  84  84  GLN GLN E . n 
E 3 80  LYS 80  85  85  LYS LYS E . n 
E 3 81  ALA 81  86  86  ALA ALA E . n 
E 3 82  ILE 82  87  87  ILE ILE E . n 
E 3 83  GLU 83  88  88  GLU GLU E . n 
E 3 84  GLU 84  89  89  GLU GLU E . n 
E 3 85  ASN 85  90  90  ASN ASN E . n 
E 3 86  ASN 86  91  91  ASN ASN E . n 
E 3 87  ASN 87  92  92  ASN ASN E . n 
E 3 88  PHE 88  93  93  PHE PHE E . n 
E 3 89  ILE 89  94  94  ILE ILE E . n 
E 3 90  LYS 90  95  95  LYS LYS E . n 
E 3 91  MET 91  96  96  MET MET E . n 
E 3 92  ALA 92  97  97  ALA ALA E . n 
E 3 93  LYS 93  98  98  LYS LYS E . n 
E 3 94  GLU 94  99  99  GLU GLU E . n 
E 3 95  LYS 95  100 100 LYS LYS E . n 
E 3 96  LEU 96  101 101 LEU LEU E . n 
E 3 97  ALA 97  102 102 ALA ALA E . n 
E 3 98  GLN 98  103 103 GLN GLN E . n 
E 3 99  LYS 99  104 104 LYS LYS E . n 
E 3 100 MET 100 105 105 MET MET E . n 
E 3 101 GLU 101 106 106 GLU GLU E . n 
E 3 102 SER 102 107 107 SER SER E . n 
E 3 103 ASN 103 108 108 ASN ASN E . n 
E 3 104 LYS 104 109 109 LYS LYS E . n 
E 3 105 GLU 105 110 110 GLU GLU E . n 
E 3 106 ASN 106 111 111 ASN ASN E . n 
E 3 107 ARG 107 112 112 ARG ARG E . n 
E 3 108 GLU 108 113 113 GLU GLU E . n 
E 3 109 ALA 109 114 114 ALA ALA E . n 
E 3 110 HIS 110 115 115 HIS HIS E . n 
E 3 111 LEU 111 116 116 LEU LEU E . n 
E 3 112 ALA 112 117 117 ALA ALA E . n 
E 3 113 ALA 113 118 118 ALA ALA E . n 
E 3 114 MET 114 119 119 MET MET E . n 
E 3 115 LEU 115 120 120 LEU LEU E . n 
E 3 116 GLU 116 121 121 GLU GLU E . n 
E 3 117 ARG 117 122 122 ARG ARG E . n 
E 3 118 LEU 118 123 123 LEU LEU E . n 
E 3 119 GLN 119 124 124 GLN GLN E . n 
E 3 120 GLU 120 125 125 GLU GLU E . n 
E 3 121 LYS 121 126 126 LYS LYS E . n 
E 3 122 ASP 122 127 127 ASP ASP E . n 
E 3 123 LYS 123 128 128 LYS LYS E . n 
E 3 124 HIS 124 129 129 HIS HIS E . n 
E 3 125 ALA 125 130 130 ALA ALA E . n 
E 3 126 GLU 126 131 131 GLU GLU E . n 
E 3 127 GLU 127 132 132 GLU GLU E . n 
E 3 128 VAL 128 133 133 VAL VAL E . n 
E 3 129 ARG 129 134 134 ARG ARG E . n 
E 3 130 LYS 130 135 135 LYS LYS E . n 
E 3 131 ASN 131 136 136 ASN ASN E . n 
E 3 132 LYS 132 137 137 LYS LYS E . n 
E 3 133 GLU 133 138 138 GLU GLU E . n 
E 3 134 LEU 134 139 139 LEU LEU E . n 
E 3 135 LYS 135 140 140 LYS LYS E . n 
E 3 136 GLU 136 141 141 GLU GLU E . n 
F 4 1   MET 1   1   1   MET MET F . n 
F 4 2   TYR 2   2   2   TYR TYR F . n 
F 4 3   THR 3   3   3   THR THR F . n 
F 4 4   PHE 4   4   4   PHE PHE F . n 
F 4 5   VAL 5   5   5   VAL VAL F . n 
F 4 6   VAL 6   6   6   VAL VAL F . n 
F 4 7   ARG 7   7   7   ARG ARG F . n 
F 4 8   ASP 8   8   8   ASP ASP F . n 
F 4 9   GLU 9   9   9   GLU GLU F . n 
F 4 10  ASN 10  10  10  ASN ASN F . n 
F 4 11  SER 11  11  11  SER SER F . n 
F 4 12  SER 12  12  12  SER SER F . n 
F 4 13  VAL 13  13  13  VAL VAL F . n 
F 4 14  TYR 14  14  14  TYR TYR F . n 
F 4 15  ALA 15  15  15  ALA ALA F . n 
F 4 16  GLU 16  16  16  GLU GLU F . n 
F 4 17  VAL 17  17  17  VAL VAL F . n 
F 4 18  SER 18  18  18  SER SER F . n 
F 4 19  ARG 19  19  19  ARG ARG F . n 
F 4 20  LEU 20  20  20  LEU LEU F . n 
F 4 21  LEU 21  21  21  LEU LEU F . n 
F 4 22  LEU 22  22  22  LEU LEU F . n 
F 4 23  ALA 23  23  23  ALA ALA F . n 
F 4 24  THR 24  24  24  THR THR F . n 
F 4 25  GLY 25  25  25  GLY GLY F . n 
F 4 26  GLN 26  26  26  GLN GLN F . n 
F 4 27  TRP 27  27  27  TRP TRP F . n 
F 4 28  LYS 28  28  28  LYS LYS F . n 
F 4 29  ARG 29  29  29  ARG ARG F . n 
F 4 30  LEU 30  30  30  LEU LEU F . n 
F 4 31  ARG 31  31  31  ARG ARG F . n 
F 4 32  LYS 32  32  32  LYS LYS F . n 
F 4 33  ASP 33  33  33  ASP ASP F . n 
F 4 34  ASN 34  34  34  ASN ASN F . n 
F 4 35  PRO 35  35  35  PRO PRO F . n 
F 4 36  ARG 36  36  36  ARG ARG F . n 
F 4 37  PHE 37  37  37  PHE PHE F . n 
F 4 38  ASN 38  38  38  ASN ASN F . n 
F 4 39  LEU 39  39  39  LEU LEU F . n 
F 4 40  MET 40  40  40  MET MET F . n 
F 4 41  LEU 41  41  41  LEU LEU F . n 
F 4 42  GLY 42  42  42  GLY GLY F . n 
F 4 43  GLU 43  43  43  GLU GLU F . n 
F 4 44  ARG 44  44  44  ARG ARG F . n 
F 4 45  ASN 45  45  45  ASN ASN F . n 
F 4 46  ARG 46  46  46  ARG ARG F . n 
F 4 47  LEU 47  47  47  LEU LEU F . n 
F 4 48  PRO 48  48  48  PRO PRO F . n 
F 4 49  PHE 49  49  49  PHE PHE F . n 
F 4 50  GLY 50  50  50  GLY GLY F . n 
F 4 51  ARG 51  51  51  ARG ARG F . n 
F 4 52  LEU 52  52  52  LEU LEU F . n 
F 4 53  GLY 53  53  53  GLY GLY F . n 
F 4 54  HIS 54  54  54  HIS HIS F . n 
F 4 55  GLU 55  55  55  GLU GLU F . n 
F 4 56  PRO 56  56  56  PRO PRO F . n 
F 4 57  GLY 57  57  57  GLY GLY F . n 
F 4 58  LEU 58  58  58  LEU LEU F . n 
F 4 59  VAL 59  59  59  VAL VAL F . n 
F 4 60  GLN 60  60  60  GLN GLN F . n 
F 4 61  LEU 61  61  61  LEU LEU F . n 
F 4 62  VAL 62  62  62  VAL VAL F . n 
F 4 63  ASN 63  63  63  ASN ASN F . n 
F 4 64  TYR 64  64  64  TYR TYR F . n 
F 4 65  TYR 65  65  65  TYR TYR F . n 
F 4 66  ARG 66  66  66  ARG ARG F . n 
F 4 67  GLY 67  67  67  GLY GLY F . n 
F 4 68  ALA 68  68  68  ALA ALA F . n 
F 4 69  ASP 69  69  69  ASP ASP F . n 
F 4 70  LYS 70  70  70  LYS LYS F . n 
F 4 71  LEU 71  71  71  LEU LEU F . n 
F 4 72  CYS 72  72  72  CYS CYS F . n 
F 4 73  ARG 73  73  73  ARG ARG F . n 
F 4 74  LYS 74  74  74  LYS LYS F . n 
F 4 75  ALA 75  75  75  ALA ALA F . n 
F 4 76  SER 76  76  76  SER SER F . n 
F 4 77  LEU 77  77  77  LEU LEU F . n 
F 4 78  VAL 78  78  78  VAL VAL F . n 
F 4 79  LYS 79  79  79  LYS LYS F . n 
F 4 80  LEU 80  80  80  LEU LEU F . n 
F 4 81  ILE 81  81  81  ILE ILE F . n 
F 4 82  LYS 82  82  82  LYS LYS F . n 
F 4 83  THR 83  83  83  THR THR F . n 
F 4 84  SER 84  84  84  SER SER F . n 
F 4 85  PRO 85  85  85  PRO PRO F . n 
F 4 86  GLU 86  86  86  GLU GLU F . n 
F 4 87  LEU 87  87  87  LEU LEU F . n 
F 4 88  SER 88  88  88  SER SER F . n 
F 4 89  GLU 89  89  89  GLU GLU F . n 
F 4 90  SER 90  90  90  SER SER F . n 
F 4 91  CYS 91  91  91  CYS CYS F . n 
F 4 92  THR 92  92  92  THR THR F . n 
F 4 93  TRP 93  93  93  TRP TRP F . n 
F 4 94  PHE 94  94  94  PHE PHE F . n 
F 4 95  PRO 95  95  95  PRO PRO F . n 
F 4 96  GLU 96  96  96  GLU GLU F . n 
F 4 97  SER 97  97  97  SER SER F . n 
F 4 98  TYR 98  98  98  TYR TYR F . n 
F 4 99  VAL 99  99  99  VAL VAL F . n 
F 4 100 ILE 100 100 100 ILE ILE F . n 
F 4 101 TYR 101 101 101 TYR TYR F . n 
F 4 102 PRO 102 102 102 PRO PRO F . n 
F 4 103 THR 103 103 103 THR THR F . n 
F 4 104 ASN 104 104 ?   ?   ?   F . n 
F 4 105 LEU 105 105 ?   ?   ?   F . n 
F 4 106 LYS 106 106 ?   ?   ?   F . n 
F 4 107 THR 107 107 ?   ?   ?   F . n 
F 4 108 PRO 108 108 ?   ?   ?   F . n 
F 4 109 VAL 109 109 ?   ?   ?   F . n 
F 4 110 ALA 110 110 ?   ?   ?   F . n 
F 4 111 PRO 111 111 ?   ?   ?   F . n 
F 4 112 ALA 112 112 ?   ?   ?   F . n 
F 4 113 GLN 113 113 ?   ?   ?   F . n 
F 4 114 ASN 114 114 ?   ?   ?   F . n 
F 4 115 GLY 115 115 ?   ?   ?   F . n 
F 4 116 ILE 116 116 ?   ?   ?   F . n 
F 4 117 ARG 117 117 ?   ?   ?   F . n 
F 4 118 HIS 118 118 ?   ?   ?   F . n 
F 4 119 LEU 119 119 ?   ?   ?   F . n 
F 4 120 ILE 120 120 ?   ?   ?   F . n 
F 4 121 ASN 121 121 ?   ?   ?   F . n 
F 4 122 ASN 122 122 ?   ?   ?   F . n 
F 4 123 THR 123 123 ?   ?   ?   F . n 
F 4 124 ARG 124 124 ?   ?   ?   F . n 
F 4 125 THR 125 125 ?   ?   ?   F . n 
F 4 126 ASP 126 126 ?   ?   ?   F . n 
F 4 127 GLU 127 127 ?   ?   ?   F . n 
F 4 128 ARG 128 128 ?   ?   ?   F . n 
F 4 129 GLU 129 129 ?   ?   ?   F . n 
F 4 130 VAL 130 130 130 VAL VAL F . n 
F 4 131 PHE 131 131 131 PHE PHE F . n 
F 4 132 LEU 132 132 132 LEU LEU F . n 
F 4 133 ALA 133 133 133 ALA ALA F . n 
F 4 134 ALA 134 134 134 ALA ALA F . n 
F 4 135 TYR 135 135 135 TYR TYR F . n 
F 4 136 ASN 136 136 136 ASN ASN F . n 
F 4 137 ARG 137 137 137 ARG ARG F . n 
F 4 138 ARG 138 138 138 ARG ARG F . n 
F 4 139 ARG 139 139 139 ARG ARG F . n 
F 4 140 GLU 140 140 140 GLU GLU F . n 
F 4 141 GLY 141 141 141 GLY GLY F . n 
F 4 142 ARG 142 142 142 ARG ARG F . n 
F 4 143 GLU 143 143 143 GLU GLU F . n 
F 4 144 GLY 144 144 144 GLY GLY F . n 
F 4 145 ASN 145 145 145 ASN ASN F . n 
F 4 146 VAL 146 146 146 VAL VAL F . n 
F 4 147 TRP 147 147 147 TRP TRP F . n 
F 4 148 ILE 148 148 148 ILE ILE F . n 
F 4 149 ALA 149 149 149 ALA ALA F . n 
F 4 150 LYS 150 150 ?   ?   ?   F . n 
F 4 151 SER 151 151 ?   ?   ?   F . n 
F 4 152 SER 152 152 ?   ?   ?   F . n 
F 4 153 ALA 153 153 ?   ?   ?   F . n 
F 4 154 GLY 154 154 ?   ?   ?   F . n 
F 4 155 ALA 155 155 ?   ?   ?   F . n 
F 4 156 LYS 156 156 ?   ?   ?   F . n 
F 4 157 GLY 157 157 ?   ?   ?   F . n 
F 4 158 GLU 158 158 ?   ?   ?   F . n 
F 4 159 GLY 159 159 ?   ?   ?   F . n 
F 4 160 ILE 160 160 ?   ?   ?   F . n 
F 4 161 LEU 161 161 161 LEU LEU F . n 
F 4 162 ILE 162 162 162 ILE ILE F . n 
F 4 163 SER 163 163 163 SER SER F . n 
F 4 164 SER 164 164 164 SER SER F . n 
F 4 165 GLU 165 165 165 GLU GLU F . n 
F 4 166 ALA 166 166 166 ALA ALA F . n 
F 4 167 SER 167 167 167 SER SER F . n 
F 4 168 GLU 168 168 168 GLU GLU F . n 
F 4 169 LEU 169 169 169 LEU LEU F . n 
F 4 170 LEU 170 170 170 LEU LEU F . n 
F 4 171 ASP 171 171 171 ASP ASP F . n 
F 4 172 PHE 172 172 172 PHE PHE F . n 
F 4 173 ILE 173 173 173 ILE ILE F . n 
F 4 174 ASP 174 174 174 ASP ASP F . n 
F 4 175 GLU 175 175 175 GLU GLU F . n 
F 4 176 GLN 176 176 176 GLN GLN F . n 
F 4 177 GLY 177 177 177 GLY GLY F . n 
F 4 178 GLN 178 178 178 GLN GLN F . n 
F 4 179 VAL 179 179 179 VAL VAL F . n 
F 4 180 HIS 180 180 180 HIS HIS F . n 
F 4 181 VAL 181 181 181 VAL VAL F . n 
F 4 182 ILE 182 182 182 ILE ILE F . n 
F 4 183 GLN 183 183 183 GLN GLN F . n 
F 4 184 LYS 184 184 184 LYS LYS F . n 
F 4 185 TYR 185 185 185 TYR TYR F . n 
F 4 186 LEU 186 186 186 LEU LEU F . n 
F 4 187 GLU 187 187 187 GLU GLU F . n 
F 4 188 LYS 188 188 188 LYS LYS F . n 
F 4 189 PRO 189 189 189 PRO PRO F . n 
F 4 190 LEU 190 190 190 LEU LEU F . n 
F 4 191 LEU 191 191 191 LEU LEU F . n 
F 4 192 LEU 192 192 192 LEU LEU F . n 
F 4 193 GLU 193 193 193 GLU GLU F . n 
F 4 194 PRO 194 194 194 PRO PRO F . n 
F 4 195 GLY 195 195 195 GLY GLY F . n 
F 4 196 HIS 196 196 196 HIS HIS F . n 
F 4 197 ARG 197 197 197 ARG ARG F . n 
F 4 198 LYS 198 198 198 LYS LYS F . n 
F 4 199 PHE 199 199 199 PHE PHE F . n 
F 4 200 ASP 200 200 200 ASP ASP F . n 
F 4 201 ILE 201 201 201 ILE ILE F . n 
F 4 202 ARG 202 202 202 ARG ARG F . n 
F 4 203 SER 203 203 203 SER SER F . n 
F 4 204 TRP 204 204 204 TRP TRP F . n 
F 4 205 VAL 205 205 205 VAL VAL F . n 
F 4 206 LEU 206 206 206 LEU LEU F . n 
F 4 207 VAL 207 207 207 VAL VAL F . n 
F 4 208 ASP 208 208 208 ASP ASP F . n 
F 4 209 HIS 209 209 209 HIS HIS F . n 
F 4 210 LEU 210 210 210 LEU LEU F . n 
F 4 211 TYR 211 211 211 TYR TYR F . n 
F 4 212 ASN 212 212 212 ASN ASN F . n 
F 4 213 ILE 213 213 213 ILE ILE F . n 
F 4 214 TYR 214 214 214 TYR TYR F . n 
F 4 215 LEU 215 215 215 LEU LEU F . n 
F 4 216 TYR 216 216 216 TYR TYR F . n 
F 4 217 ARG 217 217 217 ARG ARG F . n 
F 4 218 GLU 218 218 218 GLU GLU F . n 
F 4 219 GLY 219 219 219 GLY GLY F . n 
F 4 220 VAL 220 220 220 VAL VAL F . n 
F 4 221 LEU 221 221 221 LEU LEU F . n 
F 4 222 ARG 222 222 222 ARG ARG F . n 
F 4 223 THR 223 223 223 THR THR F . n 
F 4 224 SER 224 224 224 SER SER F . n 
F 4 225 SER 225 225 225 SER SER F . n 
F 4 226 GLU 226 226 226 GLU GLU F . n 
F 4 227 PRO 227 227 227 PRO PRO F . n 
F 4 228 TYR 228 228 228 TYR TYR F . n 
F 4 229 ASN 229 229 229 ASN ASN F . n 
F 4 230 SER 230 230 230 SER SER F . n 
F 4 231 ALA 231 231 231 ALA ALA F . n 
F 4 232 ASN 232 232 232 ASN ASN F . n 
F 4 233 PHE 233 233 233 PHE PHE F . n 
F 4 234 GLN 234 234 234 GLN GLN F . n 
F 4 235 ASP 235 235 235 ASP ASP F . n 
F 4 236 LYS 236 236 236 LYS LYS F . n 
F 4 237 THR 237 237 237 THR THR F . n 
F 4 238 CYS 238 238 238 CYS CYS F . n 
F 4 239 HIS 239 239 239 HIS HIS F . n 
F 4 240 LEU 240 240 240 LEU LEU F . n 
F 4 241 THR 241 241 241 THR THR F . n 
F 4 242 ASN 242 242 242 ASN ASN F . n 
F 4 243 HIS 243 243 243 HIS HIS F . n 
F 4 244 CYS 244 244 244 CYS CYS F . n 
F 4 245 ILE 245 245 245 ILE ILE F . n 
F 4 246 GLN 246 246 246 GLN GLN F . n 
F 4 247 LYS 247 247 247 LYS LYS F . n 
F 4 248 GLU 248 248 ?   ?   ?   F . n 
F 4 249 TYR 249 249 ?   ?   ?   F . n 
F 4 250 SER 250 250 ?   ?   ?   F . n 
F 4 251 LYS 251 251 ?   ?   ?   F . n 
F 4 252 ASN 252 252 ?   ?   ?   F . n 
F 4 253 TYR 253 253 253 TYR TYR F . n 
F 4 254 GLY 254 254 254 GLY GLY F . n 
F 4 255 ARG 255 255 255 ARG ARG F . n 
F 4 256 TYR 256 256 256 TYR TYR F . n 
F 4 257 GLU 257 257 257 GLU GLU F . n 
F 4 258 GLU 258 258 258 GLU GLU F . n 
F 4 259 GLY 259 259 259 GLY GLY F . n 
F 4 260 ASN 260 260 260 ASN ASN F . n 
F 4 261 GLU 261 261 261 GLU GLU F . n 
F 4 262 MET 262 262 262 MET MET F . n 
F 4 263 PHE 263 263 263 PHE PHE F . n 
F 4 264 PHE 264 264 264 PHE PHE F . n 
F 4 265 GLU 265 265 265 GLU GLU F . n 
F 4 266 GLU 266 266 266 GLU GLU F . n 
F 4 267 PHE 267 267 267 PHE PHE F . n 
F 4 268 ASN 268 268 268 ASN ASN F . n 
F 4 269 GLN 269 269 269 GLN GLN F . n 
F 4 270 TYR 270 270 270 TYR TYR F . n 
F 4 271 LEU 271 271 271 LEU LEU F . n 
F 4 272 MET 272 272 272 MET MET F . n 
F 4 273 ASP 273 273 273 ASP ASP F . n 
F 4 274 ALA 274 274 274 ALA ALA F . n 
F 4 275 LEU 275 275 275 LEU LEU F . n 
F 4 276 ASN 276 276 276 ASN ASN F . n 
F 4 277 THR 277 277 277 THR THR F . n 
F 4 278 THR 278 278 278 THR THR F . n 
F 4 279 LEU 279 279 279 LEU LEU F . n 
F 4 280 GLU 280 280 280 GLU GLU F . n 
F 4 281 ASN 281 281 281 ASN ASN F . n 
F 4 282 SER 282 282 282 SER SER F . n 
F 4 283 ILE 283 283 283 ILE ILE F . n 
F 4 284 LEU 284 284 284 LEU LEU F . n 
F 4 285 LEU 285 285 285 LEU LEU F . n 
F 4 286 GLN 286 286 286 GLN GLN F . n 
F 4 287 ILE 287 287 287 ILE ILE F . n 
F 4 288 LYS 288 288 288 LYS LYS F . n 
F 4 289 HIS 289 289 289 HIS HIS F . n 
F 4 290 ILE 290 290 290 ILE ILE F . n 
F 4 291 ILE 291 291 291 ILE ILE F . n 
F 4 292 ARG 292 292 292 ARG ARG F . n 
F 4 293 SER 293 293 293 SER SER F . n 
F 4 294 CYS 294 294 294 CYS CYS F . n 
F 4 295 LEU 295 295 295 LEU LEU F . n 
F 4 296 MET 296 296 296 MET MET F . n 
F 4 297 CYS 297 297 297 CYS CYS F . n 
F 4 298 ILE 298 298 298 ILE ILE F . n 
F 4 299 GLU 299 299 299 GLU GLU F . n 
F 4 300 PRO 300 300 300 PRO PRO F . n 
F 4 301 ALA 301 301 301 ALA ALA F . n 
F 4 302 ILE 302 302 302 ILE ILE F . n 
F 4 303 SER 303 303 303 SER SER F . n 
F 4 304 THR 304 304 304 THR THR F . n 
F 4 305 LYS 305 305 305 LYS LYS F . n 
F 4 306 HIS 306 306 306 HIS HIS F . n 
F 4 307 LEU 307 307 307 LEU LEU F . n 
F 4 308 HIS 308 308 308 HIS HIS F . n 
F 4 309 TYR 309 309 309 TYR TYR F . n 
F 4 310 GLN 310 310 310 GLN GLN F . n 
F 4 311 SER 311 311 311 SER SER F . n 
F 4 312 PHE 312 312 312 PHE PHE F . n 
F 4 313 GLN 313 313 313 GLN GLN F . n 
F 4 314 LEU 314 314 314 LEU LEU F . n 
F 4 315 PHE 315 315 315 PHE PHE F . n 
F 4 316 GLY 316 316 316 GLY GLY F . n 
F 4 317 PHE 317 317 317 PHE PHE F . n 
F 4 318 ASP 318 318 318 ASP ASP F . n 
F 4 319 PHE 319 319 319 PHE PHE F . n 
F 4 320 MET 320 320 320 MET MET F . n 
F 4 321 VAL 321 321 321 VAL VAL F . n 
F 4 322 ASP 322 322 322 ASP ASP F . n 
F 4 323 GLU 323 323 323 GLU GLU F . n 
F 4 324 GLU 324 324 324 GLU GLU F . n 
F 4 325 LEU 325 325 325 LEU LEU F . n 
F 4 326 LYS 326 326 326 LYS LYS F . n 
F 4 327 VAL 327 327 327 VAL VAL F . n 
F 4 328 TRP 328 328 328 TRP TRP F . n 
F 4 329 LEU 329 329 329 LEU LEU F . n 
F 4 330 ILE 330 330 330 ILE ILE F . n 
F 4 331 GLU 331 331 331 GLU GLU F . n 
F 4 332 VAL 332 332 332 VAL VAL F . n 
F 4 333 ASN 333 333 333 ASN ASN F . n 
F 4 334 GLY 334 334 334 GLY GLY F . n 
F 4 335 ALA 335 335 335 ALA ALA F . n 
F 4 336 PRO 336 336 336 PRO PRO F . n 
F 4 337 ALA 337 337 337 ALA ALA F . n 
F 4 338 CYS 338 338 338 CYS CYS F . n 
F 4 339 ALA 339 339 339 ALA ALA F . n 
F 4 340 GLN 340 340 340 GLN GLN F . n 
F 4 341 LYS 341 341 341 LYS LYS F . n 
F 4 342 LEU 342 342 342 LEU LEU F . n 
F 4 343 TYR 343 343 343 TYR TYR F . n 
F 4 344 ALA 344 344 344 ALA ALA F . n 
F 4 345 GLU 345 345 345 GLU GLU F . n 
F 4 346 LEU 346 346 346 LEU LEU F . n 
F 4 347 CYS 347 347 347 CYS CYS F . n 
F 4 348 GLN 348 348 348 GLN GLN F . n 
F 4 349 GLY 349 349 349 GLY GLY F . n 
F 4 350 ILE 350 350 350 ILE ILE F . n 
F 4 351 VAL 351 351 351 VAL VAL F . n 
F 4 352 ASP 352 352 352 ASP ASP F . n 
F 4 353 VAL 353 353 353 VAL VAL F . n 
F 4 354 ALA 354 354 354 ALA ALA F . n 
F 4 355 ILE 355 355 355 ILE ILE F . n 
F 4 356 SER 356 356 356 SER SER F . n 
F 4 357 SER 357 357 357 SER SER F . n 
F 4 358 VAL 358 358 358 VAL VAL F . n 
F 4 359 PHE 359 359 359 PHE PHE F . n 
F 4 360 PRO 360 360 360 PRO PRO F . n 
F 4 361 LEU 361 361 361 LEU LEU F . n 
F 4 362 ALA 362 362 ?   ?   ?   F . n 
F 4 363 ASP 363 363 ?   ?   ?   F . n 
F 4 364 THR 364 364 ?   ?   ?   F . n 
F 4 365 GLY 365 365 ?   ?   ?   F . n 
F 4 366 GLN 366 366 ?   ?   ?   F . n 
F 4 367 LYS 367 367 ?   ?   ?   F . n 
F 4 368 THR 368 368 ?   ?   ?   F . n 
F 4 369 SER 369 369 ?   ?   ?   F . n 
F 4 370 GLN 370 370 ?   ?   ?   F . n 
F 4 371 PRO 371 371 ?   ?   ?   F . n 
F 4 372 THR 372 372 372 THR THR F . n 
F 4 373 SER 373 373 373 SER SER F . n 
F 4 374 ILE 374 374 374 ILE ILE F . n 
F 4 375 PHE 375 375 375 PHE PHE F . n 
F 4 376 ILE 376 376 376 ILE ILE F . n 
F 4 377 LYS 377 377 377 LYS LYS F . n 
F 4 378 LEU 378 378 378 LEU LEU F . n 
F 4 379 HIS 379 379 379 HIS HIS F . n 
F 4 380 HIS 380 380 380 HIS HIS F . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D6D 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D6D 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 5  GTP   1 501 501 GTP   GTP A . 
H 6  CA    1 502 502 CA    CA  A . 
I 7  MG    1 503 503 MG    MG  A . 
J 8  GDP   1 501 501 GDP   GDP B . 
K 9  MES   1 502 502 MES   MES B . 
L 9  MES   1 503 503 MES   MES B . 
M 7  MG    1 504 504 MG    MG  B . 
N 10 A1D6D 1 505 505 A1D6D LIG B . 
O 5  GTP   1 501 501 GTP   GTP C . 
P 6  CA    1 502 502 CA    CA  C . 
Q 7  MG    1 503 503 MG    MG  C . 
R 8  GDP   1 501 501 GDP   GDP D . 
S 10 A1D6D 1 502 502 A1D6D LIG D . 
T 11 ACP   1 401 401 ACP   ACP F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 163 ? CG  ? A LYS 163 CG  
2  1 Y 1 A LYS 163 ? CD  ? A LYS 163 CD  
3  1 Y 1 A LYS 163 ? CE  ? A LYS 163 CE  
4  1 Y 1 A LYS 163 ? NZ  ? A LYS 163 NZ  
5  1 Y 1 A TYR 262 ? CG  ? A TYR 262 CG  
6  1 Y 1 A TYR 262 ? CD1 ? A TYR 262 CD1 
7  1 Y 1 A TYR 262 ? CD2 ? A TYR 262 CD2 
8  1 Y 1 A TYR 262 ? CE1 ? A TYR 262 CE1 
9  1 Y 1 A TYR 262 ? CE2 ? A TYR 262 CE2 
10 1 Y 1 A TYR 262 ? CZ  ? A TYR 262 CZ  
11 1 Y 1 A TYR 262 ? OH  ? A TYR 262 OH  
12 1 Y 1 B LYS 122 ? CG  ? B LYS 122 CG  
13 1 Y 1 B LYS 122 ? CD  ? B LYS 122 CD  
14 1 Y 1 B LYS 122 ? CE  ? B LYS 122 CE  
15 1 Y 1 B LYS 122 ? NZ  ? B LYS 122 NZ  
16 1 Y 1 B ARG 282 ? CG  ? B ARG 282 CG  
17 1 Y 1 B ARG 282 ? CD  ? B ARG 282 CD  
18 1 Y 1 B ARG 282 ? NE  ? B ARG 282 NE  
19 1 Y 1 B ARG 282 ? CZ  ? B ARG 282 CZ  
20 1 Y 1 B ARG 282 ? NH1 ? B ARG 282 NH1 
21 1 Y 1 B ARG 282 ? NH2 ? B ARG 282 NH2 
22 1 Y 1 C LYS 280 ? CG  ? C LYS 280 CG  
23 1 Y 1 C LYS 280 ? CD  ? C LYS 280 CD  
24 1 Y 1 C LYS 280 ? CE  ? C LYS 280 CE  
25 1 Y 1 C LYS 280 ? NZ  ? C LYS 280 NZ  
26 1 Y 1 D ARG 359 ? CG  ? D ARG 359 CG  
27 1 Y 1 D ARG 359 ? CD  ? D ARG 359 CD  
28 1 Y 1 D ARG 359 ? NE  ? D ARG 359 NE  
29 1 Y 1 D ARG 359 ? CZ  ? D ARG 359 CZ  
30 1 Y 1 D ARG 359 ? NH1 ? D ARG 359 NH1 
31 1 Y 1 D ARG 359 ? NH2 ? D ARG 359 NH2 
32 1 Y 1 D ASP 431 ? CG  ? D ASP 431 CG  
33 1 Y 1 D ASP 431 ? OD1 ? D ASP 431 OD1 
34 1 Y 1 D ASP 431 ? OD2 ? D ASP 431 OD2 
35 1 Y 1 F LEU 169 ? CG  ? F LEU 169 CG  
36 1 Y 1 F LEU 169 ? CD1 ? F LEU 169 CD1 
37 1 Y 1 F LEU 169 ? CD2 ? F LEU 169 CD2 
38 1 Y 1 F LYS 184 ? CG  ? F LYS 184 CG  
39 1 Y 1 F LYS 184 ? CD  ? F LYS 184 CD  
40 1 Y 1 F LYS 184 ? CE  ? F LYS 184 CE  
41 1 Y 1 F LYS 184 ? NZ  ? F LYS 184 NZ  
42 1 Y 1 F LYS 236 ? CG  ? F LYS 236 CG  
43 1 Y 1 F LYS 236 ? CD  ? F LYS 236 CD  
44 1 Y 1 F LYS 236 ? CE  ? F LYS 236 CE  
45 1 Y 1 F LYS 236 ? NZ  ? F LYS 236 NZ  
46 1 Y 1 F LEU 240 ? CG  ? F LEU 240 CG  
47 1 Y 1 F LEU 240 ? CD1 ? F LEU 240 CD1 
48 1 Y 1 F LEU 240 ? CD2 ? F LEU 240 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20_4459: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                  4 
# 
_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                     8YEM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     104.940 
_cell.length_a_esd                 ? 
_cell.length_b                     156.810 
_cell.length_b_esd                 ? 
_cell.length_c                     182.100 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8YEM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YEM 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.48 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '6% PEG 4000, 5% Glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YEM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.74 
_reflns.d_resolution_low                               43.72 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     79620 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          0.177 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.74 
_reflns_shell.d_res_low                                     2.81 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5817 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.594 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YEM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.74 
_refine.ls_d_res_low                             43.72 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     79528 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 2.51 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2183 
_refine.ls_R_factor_R_free                       0.2842 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2166 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.64 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.45 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        17169 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         230 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               17399 
_refine_hist.d_res_high                       2.74 
_refine_hist.d_res_low                        43.72 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.014  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.470 ? 2437 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 2622 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 3122 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.74 2.81 . . 141 5476 100.00 . . . . 0.3444 . . . . . . . . . . . 0.4289 
'X-RAY DIFFRACTION' 2.81 2.88 . . 140 5455 100.00 . . . . 0.3004 . . . . . . . . . . . 0.3530 
'X-RAY DIFFRACTION' 2.88 2.97 . . 142 5475 100.00 . . . . 0.2706 . . . . . . . . . . . 0.3292 
'X-RAY DIFFRACTION' 2.97 3.07 . . 141 5480 100.00 . . . . 0.2561 . . . . . . . . . . . 0.3295 
'X-RAY DIFFRACTION' 3.07 3.17 . . 142 5489 100.00 . . . . 0.2574 . . . . . . . . . . . 0.3311 
'X-RAY DIFFRACTION' 3.17 3.30 . . 142 5506 100.00 . . . . 0.2630 . . . . . . . . . . . 0.3688 
'X-RAY DIFFRACTION' 3.30 3.45 . . 142 5492 100.00 . . . . 0.2493 . . . . . . . . . . . 0.3045 
'X-RAY DIFFRACTION' 3.45 3.63 . . 142 5524 100.00 . . . . 0.2195 . . . . . . . . . . . 0.3002 
'X-RAY DIFFRACTION' 3.63 3.86 . . 142 5493 100.00 . . . . 0.2074 . . . . . . . . . . . 0.2964 
'X-RAY DIFFRACTION' 3.86 4.16 . . 143 5551 100.00 . . . . 0.1958 . . . . . . . . . . . 0.2774 
'X-RAY DIFFRACTION' 4.16 4.58 . . 143 5551 100.00 . . . . 0.1743 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 4.58 5.24 . . 145 5603 100.00 . . . . 0.1764 . . . . . . . . . . . 0.2326 
'X-RAY DIFFRACTION' 5.24 6.60 . . 145 5620 100.00 . . . . 0.2215 . . . . . . . . . . . 0.2875 
# 
_struct.entry_id                     8YEM 
_struct.title                        'Tubulin-RB3_SLD-TTL in complex with compound 9' 
_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        8YEM 
_struct_keywords.text            'Inhibitor, complex, tubulin, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL 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 1  ? 
D N N 2  ? 
E N N 3  ? 
F N N 4  ? 
G N N 5  ? 
H N N 6  ? 
I N N 7  ? 
J N N 8  ? 
K N N 9  ? 
L N N 9  ? 
M N N 7  ? 
N N N 10 ? 
O N N 5  ? 
P N N 6  ? 
Q N N 7  ? 
R N N 8  ? 
S N N 10 ? 
T N N 11 ? 
# 
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 TBA1B_PIG        Q2XVP4     ? 1 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV
;
1  
2 UNP A0A8D0VN39_PIG   A0A8D0VN39 ? 2 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATAD
;
1  
3 UNP STMN4_RAT        P63043     ? 3 
;MEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQK
AIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE
;
50 
4 UNP A0A8C9FGJ1_PAVCR A0A8C9FGJ1 ? 4 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKL
;
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 8YEM A 1 ? 440 ? Q2XVP4     1  ? 440 ? 1 440 
2 2 8YEM B 1 ? 431 ? A0A8D0VN39 1  ? 431 ? 1 431 
3 1 8YEM C 1 ? 440 ? Q2XVP4     1  ? 440 ? 1 440 
4 2 8YEM D 1 ? 431 ? A0A8D0VN39 1  ? 431 ? 1 431 
5 3 8YEM E 1 ? 136 ? P63043     50 ? 185 ? 6 141 
6 4 8YEM F 1 ? 378 ? A0A8C9FGJ1 1  ? 378 ? 1 378 
# 
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 
6 8YEM HIS F 379 ? UNP A0A8C9FGJ1 ? ? 'expression tag' 379 1 
6 8YEM HIS F 380 ? UNP A0A8C9FGJ1 ? ? 'expression tag' 380 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 10  ? GLY A 29  ? GLY A 10  GLY A 29  1 ? 20 
HELX_P HELX_P2  AA2 SER A 48  ? THR A 51  ? SER A 48  THR A 51  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 71  ? THR A 80  ? GLU A 71  THR A 80  1 ? 10 
HELX_P HELX_P4  AA4 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P5  AA5 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P6  AA6 ILE A 114 ? ASP A 127 ? ILE A 114 ASP A 127 1 ? 14 
HELX_P HELX_P7  AA7 GLY A 143 ? TYR A 161 ? GLY A 143 TYR A 161 1 ? 19 
HELX_P HELX_P8  AA8 VAL A 182 ? LEU A 195 ? VAL A 182 LEU A 195 1 ? 14 
HELX_P HELX_P9  AA9 GLU A 196 ? SER A 198 ? GLU A 196 SER A 198 5 ? 3  
HELX_P HELX_P10 AB1 ASN A 206 ? ASN A 216 ? ASN A 206 ASN A 216 1 ? 11 
HELX_P HELX_P11 AB2 THR A 223 ? PHE A 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P12 AB3 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P13 AB4 SER A 287 ? CYS A 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 296 ? GLN A 301 ? PHE A 296 GLN A 301 5 ? 6  
HELX_P HELX_P15 AB6 ASP A 306 ? GLY A 310 ? ASP A 306 GLY A 310 5 ? 5  
HELX_P HELX_P16 AB7 VAL A 324 ? ARG A 339 ? VAL A 324 ARG A 339 1 ? 16 
HELX_P HELX_P17 AB8 ILE A 384 ? LYS A 401 ? ILE A 384 LYS A 401 1 ? 18 
HELX_P HELX_P18 AB9 PHE A 404 ? GLY A 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P19 AC1 GLU A 414 ? GLY A 436 ? GLU A 414 GLY A 436 1 ? 23 
HELX_P HELX_P20 AC2 GLY B 10  ? HIS B 28  ? GLY B 10  HIS B 28  1 ? 19 
HELX_P HELX_P21 AC3 SER B 40  ? LEU B 44  ? SER B 40  LEU B 44  5 ? 5  
HELX_P HELX_P22 AC4 ARG B 46  ? VAL B 49  ? ARG B 46  VAL B 49  5 ? 4  
HELX_P HELX_P23 AC5 PRO B 70  ? GLY B 79  ? PRO B 70  GLY B 79  1 ? 10 
HELX_P HELX_P24 AC6 PHE B 81  ? PHE B 85  ? PHE B 81  PHE B 85  5 ? 5  
HELX_P HELX_P25 AC7 ARG B 86  ? ASP B 88  ? ARG B 86  ASP B 88  5 ? 3  
HELX_P HELX_P26 AC8 ASN B 100 ? TYR B 106 ? ASN B 100 TYR B 106 1 ? 7  
HELX_P HELX_P27 AC9 THR B 107 ? CYS B 127 ? THR B 107 CYS B 127 1 ? 21 
HELX_P HELX_P28 AD1 GLY B 142 ? TYR B 159 ? GLY B 142 TYR B 159 1 ? 18 
HELX_P HELX_P29 AD2 SER B 172 ? SER B 176 ? SER B 172 SER B 176 5 ? 5  
HELX_P HELX_P30 AD3 VAL B 180 ? THR B 196 ? VAL B 180 THR B 196 1 ? 17 
HELX_P HELX_P31 AD4 ASN B 204 ? ARG B 213 ? ASN B 204 ARG B 213 1 ? 10 
HELX_P HELX_P32 AD5 THR B 221 ? THR B 237 ? THR B 221 THR B 237 1 ? 17 
HELX_P HELX_P33 AD6 THR B 237 ? PHE B 242 ? THR B 237 PHE B 242 1 ? 6  
HELX_P HELX_P34 AD7 ASP B 249 ? VAL B 258 ? ASP B 249 VAL B 258 1 ? 10 
HELX_P HELX_P35 AD8 THR B 285 ? PHE B 294 ? THR B 285 PHE B 294 1 ? 10 
HELX_P HELX_P36 AD9 ASP B 295 ? MET B 299 ? ASP B 295 MET B 299 5 ? 5  
HELX_P HELX_P37 AE1 ASP B 304 ? GLY B 308 ? ASP B 304 GLY B 308 5 ? 5  
HELX_P HELX_P38 AE2 SER B 322 ? ASN B 337 ? SER B 322 ASN B 337 1 ? 16 
HELX_P HELX_P39 AE3 SER B 338 ? PHE B 341 ? SER B 338 PHE B 341 5 ? 4  
HELX_P HELX_P40 AE4 ILE B 374 ? ARG B 390 ? ILE B 374 ARG B 390 1 ? 17 
HELX_P HELX_P41 AE5 LEU B 395 ? GLY B 400 ? LEU B 395 GLY B 400 1 ? 6  
HELX_P HELX_P42 AE6 ASP B 404 ? GLN B 426 ? ASP B 404 GLN B 426 1 ? 23 
HELX_P HELX_P43 AE7 GLY C 10  ? GLY C 29  ? GLY C 10  GLY C 29  1 ? 20 
HELX_P HELX_P44 AE8 ASP C 47  ? THR C 51  ? ASP C 47  THR C 51  5 ? 5  
HELX_P HELX_P45 AE9 PRO C 72  ? GLY C 81  ? PRO C 72  GLY C 81  1 ? 10 
HELX_P HELX_P46 AF1 TYR C 83  ? PHE C 87  ? TYR C 83  PHE C 87  5 ? 5  
HELX_P HELX_P47 AF2 HIS C 88  ? GLU C 90  ? HIS C 88  GLU C 90  5 ? 3  
HELX_P HELX_P48 AF3 ASN C 102 ? TYR C 108 ? ASN C 102 TYR C 108 1 ? 7  
HELX_P HELX_P49 AF4 ILE C 110 ? GLU C 113 ? ILE C 110 GLU C 113 5 ? 4  
HELX_P HELX_P50 AF5 ILE C 114 ? ASP C 127 ? ILE C 114 ASP C 127 1 ? 14 
HELX_P HELX_P51 AF6 GLY C 143 ? GLY C 162 ? GLY C 143 GLY C 162 1 ? 20 
HELX_P HELX_P52 AF7 VAL C 182 ? LEU C 195 ? VAL C 182 LEU C 195 1 ? 14 
HELX_P HELX_P53 AF8 GLU C 196 ? SER C 198 ? GLU C 196 SER C 198 5 ? 3  
HELX_P HELX_P54 AF9 ASN C 206 ? LEU C 217 ? ASN C 206 LEU C 217 1 ? 12 
HELX_P HELX_P55 AG1 THR C 223 ? PHE C 244 ? THR C 223 PHE C 244 1 ? 22 
HELX_P HELX_P56 AG2 ASP C 251 ? VAL C 260 ? ASP C 251 VAL C 260 1 ? 10 
HELX_P HELX_P57 AG3 SER C 277 ? TYR C 282 ? SER C 277 TYR C 282 1 ? 6  
HELX_P HELX_P58 AG4 SER C 287 ? CYS C 295 ? SER C 287 CYS C 295 1 ? 9  
HELX_P HELX_P59 AG5 PHE C 296 ? GLN C 301 ? PHE C 296 GLN C 301 5 ? 6  
HELX_P HELX_P60 AG6 ASP C 306 ? GLY C 310 ? ASP C 306 GLY C 310 5 ? 5  
HELX_P HELX_P61 AG7 VAL C 324 ? ARG C 339 ? VAL C 324 ARG C 339 1 ? 16 
HELX_P HELX_P62 AG8 ILE C 384 ? ALA C 400 ? ILE C 384 ALA C 400 1 ? 17 
HELX_P HELX_P63 AG9 PHE C 404 ? GLY C 410 ? PHE C 404 GLY C 410 1 ? 7  
HELX_P HELX_P64 AH1 GLU C 414 ? VAL C 437 ? GLU C 414 VAL C 437 1 ? 24 
HELX_P HELX_P65 AH2 GLY D 10  ? GLY D 29  ? GLY D 10  GLY D 29  1 ? 20 
HELX_P HELX_P66 AH3 SER D 40  ? LEU D 44  ? SER D 40  LEU D 44  5 ? 5  
HELX_P HELX_P67 AH4 ARG D 46  ? VAL D 49  ? ARG D 46  VAL D 49  5 ? 4  
HELX_P HELX_P68 AH5 GLU D 69  ? GLY D 79  ? GLU D 69  GLY D 79  1 ? 11 
HELX_P HELX_P69 AH6 ARG D 86  ? ASP D 88  ? ARG D 86  ASP D 88  5 ? 3  
HELX_P HELX_P70 AH7 ASN D 100 ? TYR D 106 ? ASN D 100 TYR D 106 1 ? 7  
HELX_P HELX_P71 AH8 THR D 107 ? GLU D 125 ? THR D 107 GLU D 125 1 ? 19 
HELX_P HELX_P72 AH9 GLY D 142 ? TYR D 159 ? GLY D 142 TYR D 159 1 ? 18 
HELX_P HELX_P73 AI1 VAL D 180 ? THR D 196 ? VAL D 180 THR D 196 1 ? 17 
HELX_P HELX_P74 AI2 ASN D 204 ? THR D 214 ? ASN D 204 THR D 214 1 ? 11 
HELX_P HELX_P75 AI3 THR D 221 ? VAL D 236 ? THR D 221 VAL D 236 1 ? 16 
HELX_P HELX_P76 AI4 THR D 237 ? PHE D 242 ? THR D 237 PHE D 242 1 ? 6  
HELX_P HELX_P77 AI5 ASP D 249 ? VAL D 258 ? ASP D 249 VAL D 258 1 ? 10 
HELX_P HELX_P78 AI6 THR D 285 ? PHE D 294 ? THR D 285 PHE D 294 1 ? 10 
HELX_P HELX_P79 AI7 ASP D 295 ? MET D 299 ? ASP D 295 MET D 299 5 ? 5  
HELX_P HELX_P80 AI8 ASP D 304 ? GLY D 308 ? ASP D 304 GLY D 308 5 ? 5  
HELX_P HELX_P81 AI9 SER D 322 ? ASN D 337 ? SER D 322 ASN D 337 1 ? 16 
HELX_P HELX_P82 AJ1 SER D 338 ? PHE D 341 ? SER D 338 PHE D 341 5 ? 4  
HELX_P HELX_P83 AJ2 ILE D 374 ? ARG D 390 ? ILE D 374 ARG D 390 1 ? 17 
HELX_P HELX_P84 AJ3 LEU D 395 ? GLY D 400 ? LEU D 395 GLY D 400 1 ? 6  
HELX_P HELX_P85 AJ4 ASP D 404 ? ASP D 427 ? ASP D 404 ASP D 427 1 ? 24 
HELX_P HELX_P86 AJ5 SER E 41  ? GLU E 133 ? SER E 46  GLU E 138 1 ? 93 
HELX_P HELX_P87 AJ6 SER F 11  ? ALA F 23  ? SER F 11  ALA F 23  1 ? 13 
HELX_P HELX_P88 AJ7 PRO F 48  ? LEU F 52  ? PRO F 48  LEU F 52  5 ? 5  
HELX_P HELX_P89 AJ8 GLY F 67  ? CYS F 72  ? GLY F 67  CYS F 72  5 ? 6  
HELX_P HELX_P90 AJ9 ARG F 73  ? SER F 84  ? ARG F 73  SER F 84  1 ? 12 
HELX_P HELX_P91 AK1 PHE F 131 ? GLY F 141 ? PHE F 131 GLY F 141 1 ? 11 
HELX_P HELX_P92 AK2 GLU F 165 ? GLU F 175 ? GLU F 165 GLU F 175 1 ? 11 
HELX_P HELX_P93 AK3 GLU F 257 ? GLY F 259 ? GLU F 257 GLY F 259 5 ? 3  
HELX_P HELX_P94 AK4 PHE F 263 ? ASN F 276 ? PHE F 263 ASN F 276 1 ? 14 
HELX_P HELX_P95 AK5 THR F 278 ? ILE F 283 ? THR F 278 ILE F 283 1 ? 6  
HELX_P HELX_P96 AK6 ILE F 283 ? ILE F 298 ? ILE F 283 ILE F 298 1 ? 16 
HELX_P HELX_P97 AK7 ILE F 298 ? SER F 303 ? ILE F 298 SER F 303 1 ? 6  
HELX_P HELX_P98 AK8 ALA F 339 ? ILE F 355 ? ALA F 339 ILE F 355 1 ? 17 
# 
_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 ? ? A ASP 39  OD1 ? ? ? 1_555 H CA . CA ? ? A ASP 39  A CA 502 1_555 ? ? ? ? ? ? ? 2.889 ? ? 
metalc2  metalc ? ? A ASP 39  OD2 ? ? ? 1_555 H CA . CA ? ? A ASP 39  A CA 502 1_555 ? ? ? ? ? ? ? 2.841 ? ? 
metalc3  metalc ? ? A THR 41  O   ? ? ? 1_555 H CA . CA ? ? A THR 41  A CA 502 1_555 ? ? ? ? ? ? ? 2.829 ? ? 
metalc4  metalc ? ? A THR 41  OG1 ? ? ? 1_555 H CA . CA ? ? A THR 41  A CA 502 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc5  metalc ? ? A GLY 44  O   ? ? ? 1_555 H CA . CA ? ? A GLY 44  A CA 502 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc6  metalc ? ? A GLU 55  OE2 ? ? ? 1_555 H CA . CA ? ? A GLU 55  A CA 502 1_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc7  metalc ? ? A GLU 71  OE1 ? ? ? 1_555 I MG . MG ? ? A GLU 71  A MG 503 1_555 ? ? ? ? ? ? ? 2.601 ? ? 
metalc8  metalc ? ? G GTP .   O2G ? ? ? 1_555 I MG . MG ? ? A GTP 501 A MG 503 1_555 ? ? ? ? ? ? ? 2.774 ? ? 
metalc9  metalc ? ? G GTP .   O2B ? ? ? 1_555 I MG . MG ? ? A GTP 501 A MG 503 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc10 metalc ? ? B GLN 11  OE1 ? ? ? 1_555 M MG . MG ? ? B GLN 11  B MG 504 1_555 ? ? ? ? ? ? ? 1.812 ? ? 
metalc11 metalc ? ? B ASP 177 OD2 ? ? ? 1_555 M MG . MG ? ? B ASP 177 B MG 504 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc12 metalc ? ? J GDP .   O2A ? ? ? 1_555 M MG . MG ? ? B GDP 501 B MG 504 1_555 ? ? ? ? ? ? ? 2.807 ? ? 
metalc13 metalc ? ? C ASP 39  OD1 ? ? ? 1_555 P CA . CA ? ? C ASP 39  C CA 502 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
metalc14 metalc ? ? C ASP 39  OD2 ? ? ? 1_555 P CA . CA ? ? C ASP 39  C CA 502 1_555 ? ? ? ? ? ? ? 2.135 ? ? 
metalc15 metalc ? ? C THR 41  O   ? ? ? 1_555 P CA . CA ? ? C THR 41  C CA 502 1_555 ? ? ? ? ? ? ? 3.028 ? ? 
metalc16 metalc ? ? C THR 41  OG1 ? ? ? 1_555 P CA . CA ? ? C THR 41  C CA 502 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc17 metalc ? ? C GLY 44  O   ? ? ? 1_555 P CA . CA ? ? C GLY 44  C CA 502 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc18 metalc ? ? C GLU 55  OE2 ? ? ? 1_555 P CA . CA ? ? C GLU 55  C CA 502 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc19 metalc ? ? O GTP .   O3G ? ? ? 1_555 Q MG . MG ? ? C GTP 501 C MG 503 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc20 metalc ? ? O GTP .   O2B ? ? ? 1_555 Q MG . MG ? ? C GTP 501 C MG 503 1_555 ? ? ? ? ? ? ? 2.603 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OD2 ? A ASP 39  ? A ASP 39  ? 1_555 44.1  ? 
2  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A THR 41  ? A THR 41  ? 1_555 58.8  ? 
3  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A THR 41  ? A THR 41  ? 1_555 65.0  ? 
4  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 73.4  ? 
5  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 117.5 ? 
6  O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OG1 ? A THR 41  ? A THR 41  ? 1_555 85.3  ? 
7  OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 112.9 ? 
8  OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 98.7  ? 
9  O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 54.5  ? 
10 OG1 ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 O   ? A GLY 44  ? A GLY 44  ? 1_555 106.5 ? 
11 OD1 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 95.7  ? 
12 OD2 ? A ASP 39  ? A ASP 39  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 53.7  ? 
13 O   ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 74.6  ? 
14 OG1 ? A THR 41  ? A THR 41  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 160.0 ? 
15 O   ? A GLY 44  ? A GLY 44  ? 1_555 CA ? H CA . ? A CA 502 ? 1_555 OE2 ? A GLU 55  ? A GLU 55  ? 1_555 61.7  ? 
16 OE1 ? A GLU 71  ? A GLU 71  ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2G ? G GTP .   ? A GTP 501 ? 1_555 113.1 ? 
17 OE1 ? A GLU 71  ? A GLU 71  ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2B ? G GTP .   ? A GTP 501 ? 1_555 163.5 ? 
18 O2G ? G GTP .   ? A GTP 501 ? 1_555 MG ? I MG . ? A MG 503 ? 1_555 O2B ? G GTP .   ? A GTP 501 ? 1_555 61.7  ? 
19 OE1 ? B GLN 11  ? B GLN 11  ? 1_555 MG ? M MG . ? B MG 504 ? 1_555 OD2 ? B ASP 177 ? B ASP 177 ? 1_555 120.5 ? 
20 OE1 ? B GLN 11  ? B GLN 11  ? 1_555 MG ? M MG . ? B MG 504 ? 1_555 O2A ? J GDP .   ? B GDP 501 ? 1_555 59.5  ? 
21 OD2 ? B ASP 177 ? B ASP 177 ? 1_555 MG ? M MG . ? B MG 504 ? 1_555 O2A ? J GDP .   ? B GDP 501 ? 1_555 92.8  ? 
22 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 59.8  ? 
23 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C THR 41  ? C THR 41  ? 1_555 79.2  ? 
24 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C THR 41  ? C THR 41  ? 1_555 70.7  ? 
25 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 74.8  ? 
26 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 115.2 ? 
27 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OG1 ? C THR 41  ? C THR 41  ? 1_555 56.5  ? 
28 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 133.0 ? 
29 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 112.1 ? 
30 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 56.6  ? 
31 OG1 ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 O   ? C GLY 44  ? C GLY 44  ? 1_555 68.3  ? 
32 OD1 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 126.2 ? 
33 OD2 ? C ASP 39  ? C ASP 39  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 67.3  ? 
34 O   ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 74.8  ? 
35 OG1 ? C THR 41  ? C THR 41  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 122.8 ? 
36 O   ? C GLY 44  ? C GLY 44  ? 1_555 CA ? P CA . ? C CA 502 ? 1_555 OE2 ? C GLU 55  ? C GLU 55  ? 1_555 60.3  ? 
37 O3G ? O GTP .   ? C GTP 501 ? 1_555 MG ? Q MG . ? C MG 503 ? 1_555 O2B ? O GTP .   ? C GTP 501 ? 1_555 70.9  ? 
# 
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 273 A . ? ALA 273 A PRO 274 A ? PRO 274 A 1 3.87  
2 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 0.83  
3 ALA 273 C . ? ALA 273 C PRO 274 C ? PRO 274 C 1 -1.86 
4 ALA 271 D . ? ALA 271 D PRO 272 D ? PRO 272 D 1 -0.97 
5 GLU 193 F . ? GLU 193 F PRO 194 F ? PRO 194 F 1 3.90  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 6  ? 
AA4 ? 6  ? 
AA5 ? 10 ? 
AA6 ? 2  ? 
AA7 ? 6  ? 
AA8 ? 2  ? 
AA9 ? 4  ? 
AB1 ? 10 ? 
AB2 ? 2  ? 
AB3 ? 5  ? 
AB4 ? 3  ? 
AB5 ? 5  ? 
AB6 ? 5  ? 
# 
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      
AA2 1 2  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? parallel      
AA3 4 5  ? anti-parallel 
AA3 5 6  ? anti-parallel 
AA4 1 2  ? anti-parallel 
AA4 2 3  ? anti-parallel 
AA4 3 4  ? parallel      
AA4 4 5  ? anti-parallel 
AA4 5 6  ? anti-parallel 
AA5 1 2  ? parallel      
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? parallel      
AA6 1 2  ? anti-parallel 
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA8 1 2  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? parallel      
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB1 5 6  ? parallel      
AB1 6 7  ? parallel      
AB1 7 8  ? anti-parallel 
AB1 8 9  ? anti-parallel 
AB1 9 10 ? parallel      
AB2 1 2  ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
AB4 1 2  ? anti-parallel 
AB4 2 3  ? anti-parallel 
AB5 1 2  ? anti-parallel 
AB5 2 3  ? anti-parallel 
AB5 3 4  ? anti-parallel 
AB5 4 5  ? anti-parallel 
AB6 1 2  ? anti-parallel 
AB6 2 3  ? anti-parallel 
AB6 3 4  ? anti-parallel 
AB6 4 5  ? 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  LEU A 92  ? THR A 94  ? LEU A 92  THR A 94  
AA1 2  ALA A 65  ? ASP A 69  ? ALA A 65  ASP A 69  
AA1 3  CYS A 4   ? VAL A 9   ? CYS A 4   VAL A 9   
AA1 4  GLY A 134 ? SER A 140 ? GLY A 134 SER A 140 
AA1 5  SER A 165 ? TYR A 172 ? SER A 165 TYR A 172 
AA1 6  CYS A 200 ? ASP A 205 ? CYS A 200 ASP A 205 
AA2 1  PHE A 53  ? GLU A 55  ? PHE A 53  GLU A 55  
AA2 2  HIS A 61  ? PRO A 63  ? HIS A 61  PRO A 63  
AA3 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA3 2  ARG A 373 ? THR A 381 ? ARG A 373 THR A 381 
AA3 3  TYR A 312 ? GLY A 321 ? TYR A 312 GLY A 321 
AA3 4  THR A 349 ? ASN A 356 ? THR A 349 ASN A 356 
AA3 5  GLY E 12  ? LYS E 20  ? GLY E 17  LYS E 25  
AA3 6  GLU E 2   ? VAL E 3   ? GLU E 7   VAL E 8   
AA4 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA4 2  ARG A 373 ? THR A 381 ? ARG A 373 THR A 381 
AA4 3  TYR A 312 ? GLY A 321 ? TYR A 312 GLY A 321 
AA4 4  THR A 349 ? ASN A 356 ? THR A 349 ASN A 356 
AA4 5  GLY E 12  ? LYS E 20  ? GLY E 17  LYS E 25  
AA4 6  ASN E 7   ? LYS E 8   ? ASN E 12  LYS E 13  
AA5 1  PHE B 90  ? PHE B 92  ? PHE B 90  PHE B 92  
AA5 2  ALA B 63  ? ASP B 67  ? ALA B 63  ASP B 67  
AA5 3  GLU B 3   ? ALA B 9   ? GLU B 3   ALA B 9   
AA5 4  LEU B 130 ? SER B 138 ? LEU B 130 SER B 138 
AA5 5  ILE B 163 ? MET B 170 ? ILE B 163 MET B 170 
AA5 6  GLU B 198 ? ASP B 203 ? GLU B 198 ASP B 203 
AA5 7  PHE B 265 ? ALA B 271 ? PHE B 265 ALA B 271 
AA5 8  SER B 364 ? SER B 371 ? SER B 364 SER B 371 
AA5 9  TYR B 310 ? ARG B 318 ? TYR B 310 ARG B 318 
AA5 10 VAL B 349 ? CYS B 354 ? VAL B 349 CYS B 354 
AA6 1  TYR B 51  ? ALA B 54  ? TYR B 51  ALA B 54  
AA6 2  LYS B 58  ? PRO B 61  ? LYS B 58  PRO B 61  
AA7 1  LEU C 92  ? THR C 94  ? LEU C 92  THR C 94  
AA7 2  ALA C 65  ? ASP C 69  ? ALA C 65  ASP C 69  
AA7 3  CYS C 4   ? VAL C 9   ? CYS C 4   VAL C 9   
AA7 4  GLY C 134 ? SER C 140 ? GLY C 134 SER C 140 
AA7 5  SER C 165 ? TYR C 172 ? SER C 165 TYR C 172 
AA7 6  CYS C 200 ? ASP C 205 ? CYS C 200 ASP C 205 
AA8 1  PHE C 53  ? GLU C 55  ? PHE C 53  GLU C 55  
AA8 2  HIS C 61  ? PRO C 63  ? HIS C 61  PRO C 63  
AA9 1  LEU C 269 ? ALA C 273 ? LEU C 269 ALA C 273 
AA9 2  ARG C 373 ? THR C 381 ? ARG C 373 THR C 381 
AA9 3  TYR C 312 ? GLY C 321 ? TYR C 312 GLY C 321 
AA9 4  LYS C 352 ? ASN C 356 ? LYS C 352 ASN C 356 
AB1 1  PHE D 90  ? PHE D 92  ? PHE D 90  PHE D 92  
AB1 2  ALA D 63  ? ASP D 67  ? ALA D 63  ASP D 67  
AB1 3  GLU D 3   ? ALA D 9   ? GLU D 3   ALA D 9   
AB1 4  LEU D 130 ? SER D 138 ? LEU D 130 SER D 138 
AB1 5  ILE D 163 ? MET D 170 ? ILE D 163 MET D 170 
AB1 6  GLU D 198 ? ASP D 203 ? GLU D 198 ASP D 203 
AB1 7  PHE D 265 ? ALA D 271 ? PHE D 265 ALA D 271 
AB1 8  MET D 363 ? SER D 371 ? MET D 363 SER D 371 
AB1 9  TYR D 310 ? GLY D 319 ? TYR D 310 GLY D 319 
AB1 10 VAL D 349 ? CYS D 354 ? VAL D 349 CYS D 354 
AB2 1  TYR D 51  ? ALA D 54  ? TYR D 51  ALA D 54  
AB2 2  LYS D 58  ? PRO D 61  ? LYS D 58  PRO D 61  
AB3 1  TRP F 27  ? ARG F 29  ? TRP F 27  ARG F 29  
AB3 2  TYR F 2   ? VAL F 6   ? TYR F 2   VAL F 6   
AB3 3  LEU F 39  ? LEU F 41  ? LEU F 39  LEU F 41  
AB3 4  LEU F 61  ? VAL F 62  ? LEU F 61  VAL F 62  
AB3 5  GLN F 310 ? SER F 311 ? GLN F 310 SER F 311 
AB4 1  SER F 97  ? ILE F 100 ? SER F 97  ILE F 100 
AB4 2  HIS F 180 ? LYS F 184 ? HIS F 180 LYS F 184 
AB4 3  TRP F 147 ? ILE F 148 ? TRP F 147 ILE F 148 
AB5 1  GLU F 261 ? MET F 262 ? GLU F 261 MET F 262 
AB5 2  VAL F 220 ? THR F 223 ? VAL F 220 THR F 223 
AB5 3  PHE F 199 ? VAL F 207 ? PHE F 199 VAL F 207 
AB5 4  GLN F 313 ? VAL F 321 ? GLN F 313 VAL F 321 
AB5 5  VAL F 327 ? ASN F 333 ? VAL F 327 ASN F 333 
AB6 1  GLU F 261 ? MET F 262 ? GLU F 261 MET F 262 
AB6 2  VAL F 220 ? THR F 223 ? VAL F 220 THR F 223 
AB6 3  PHE F 199 ? VAL F 207 ? PHE F 199 VAL F 207 
AB6 4  ILE F 213 ? TYR F 216 ? ILE F 213 TYR F 216 
AB6 5  PHE F 375 ? LYS F 377 ? PHE F 375 LYS F 377 
# 
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 ILE A 93  ? O ILE A 93  N PHE A 67  ? N PHE A 67  
AA1 2 3  O VAL A 66  ? O VAL A 66  N HIS A 8   ? N HIS A 8   
AA1 3 4  N VAL A 9   ? N VAL A 9   O PHE A 138 ? O PHE A 138 
AA1 4 5  N PHE A 135 ? N PHE A 135 O LEU A 167 ? O LEU A 167 
AA1 5 6  N GLU A 168 ? N GLU A 168 O CYS A 200 ? O CYS A 200 
AA2 1 2  N SER A 54  ? N SER A 54  O VAL A 62  ? O VAL A 62  
AA3 1 2  N LEU A 269 ? N LEU A 269 O SER A 379 ? O SER A 379 
AA3 2 3  O LEU A 378 ? O LEU A 378 N CYS A 316 ? N CYS A 316 
AA3 3 4  N TYR A 319 ? N TYR A 319 O GLY A 354 ? O GLY A 354 
AA3 4 5  N VAL A 353 ? N VAL A 353 O PHE E 15  ? O PHE E 20  
AA3 5 6  O ILE E 18  ? O ILE E 23  N GLU E 2   ? N GLU E 7   
AA4 1 2  N LEU A 269 ? N LEU A 269 O SER A 379 ? O SER A 379 
AA4 2 3  O LEU A 378 ? O LEU A 378 N CYS A 316 ? N CYS A 316 
AA4 3 4  N TYR A 319 ? N TYR A 319 O GLY A 354 ? O GLY A 354 
AA4 4 5  N VAL A 353 ? N VAL A 353 O PHE E 15  ? O PHE E 20  
AA4 5 6  O SER E 14  ? O SER E 19  N ASN E 7   ? N ASN E 12  
AA5 1 2  O VAL B 91  ? O VAL B 91  N LEU B 65  ? N LEU B 65  
AA5 2 3  O ILE B 64  ? O ILE B 64  N HIS B 6   ? N HIS B 6   
AA5 3 4  N GLU B 3   ? N GLU B 3   O GLN B 131 ? O GLN B 131 
AA5 4 5  N LEU B 135 ? N LEU B 135 O PHE B 167 ? O PHE B 167 
AA5 5 6  N THR B 166 ? N THR B 166 O GLU B 198 ? O GLU B 198 
AA5 6 7  N CYS B 201 ? N CYS B 201 O PHE B 266 ? O PHE B 266 
AA5 7 8  N MET B 267 ? N MET B 267 O GLY B 369 ? O GLY B 369 
AA5 8 9  O SER B 364 ? O SER B 364 N ARG B 318 ? N ARG B 318 
AA5 9 10 N VAL B 313 ? N VAL B 313 O LYS B 350 ? O LYS B 350 
AA6 1 2  N ALA B 54  ? N ALA B 54  O LYS B 58  ? O LYS B 58  
AA7 1 2  O ILE C 93  ? O ILE C 93  N PHE C 67  ? N PHE C 67  
AA7 2 3  O VAL C 68  ? O VAL C 68  N HIS C 8   ? N HIS C 8   
AA7 3 4  N ILE C 7   ? N ILE C 7   O PHE C 138 ? O PHE C 138 
AA7 4 5  N VAL C 137 ? N VAL C 137 O LEU C 167 ? O LEU C 167 
AA7 5 6  N GLU C 168 ? N GLU C 168 O PHE C 202 ? O PHE C 202 
AA8 1 2  N SER C 54  ? N SER C 54  O VAL C 62  ? O VAL C 62  
AA9 1 2  N LEU C 269 ? N LEU C 269 O SER C 379 ? O SER C 379 
AA9 2 3  O ASN C 380 ? O ASN C 380 N MET C 313 ? N MET C 313 
AA9 3 4  N TYR C 319 ? N TYR C 319 O GLY C 354 ? O GLY C 354 
AB1 1 2  O VAL D 91  ? O VAL D 91  N LEU D 65  ? N LEU D 65  
AB1 2 3  O ILE D 64  ? O ILE D 64  N GLN D 8   ? N GLN D 8   
AB1 3 4  N VAL D 5   ? N VAL D 5   O GLY D 132 ? O GLY D 132 
AB1 4 5  N LEU D 135 ? N LEU D 135 O PHE D 167 ? O PHE D 167 
AB1 5 6  N SER D 168 ? N SER D 168 O ILE D 202 ? O ILE D 202 
AB1 6 7  N CYS D 201 ? N CYS D 201 O PHE D 266 ? O PHE D 266 
AB1 7 8  N MET D 267 ? N MET D 267 O GLY D 369 ? O GLY D 369 
AB1 8 9  O THR D 366 ? O THR D 366 N ILE D 316 ? N ILE D 316 
AB1 9 10 N PHE D 317 ? N PHE D 317 O ALA D 352 ? O ALA D 352 
AB2 1 2  N ALA D 54  ? N ALA D 54  O LYS D 58  ? O LYS D 58  
AB3 1 2  O LYS F 28  ? O LYS F 28  N PHE F 4   ? N PHE F 4   
AB3 2 3  N VAL F 5   ? N VAL F 5   O LEU F 39  ? O LEU F 39  
AB3 3 4  N MET F 40  ? N MET F 40  O LEU F 61  ? O LEU F 61  
AB3 4 5  N VAL F 62  ? N VAL F 62  O GLN F 310 ? O GLN F 310 
AB4 1 2  N TYR F 98  ? N TYR F 98  O ILE F 182 ? O ILE F 182 
AB4 2 3  O GLN F 183 ? O GLN F 183 N ILE F 148 ? N ILE F 148 
AB5 1 2  O MET F 262 ? O MET F 262 N LEU F 221 ? N LEU F 221 
AB5 2 3  O VAL F 220 ? O VAL F 220 N ARG F 202 ? N ARG F 202 
AB5 3 4  N VAL F 205 ? N VAL F 205 O PHE F 315 ? O PHE F 315 
AB5 4 5  N GLY F 316 ? N GLY F 316 O ASN F 333 ? O ASN F 333 
AB6 1 2  O MET F 262 ? O MET F 262 N LEU F 221 ? N LEU F 221 
AB6 2 3  O VAL F 220 ? O VAL F 220 N ARG F 202 ? N ARG F 202 
AB6 3 4  N LEU F 206 ? N LEU F 206 O TYR F 214 ? O TYR F 214 
AB6 4 5  N LEU F 215 ? N LEU F 215 O ILE F 376 ? O ILE F 376 
# 
_pdbx_entry_details.entry_id                   8YEM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 N   D GLN 11  ? ? O2B   D GDP 501 ? ? 1.30 
2  1 OE2 D GLU 181 ? ? "O3'" D GDP 501 ? ? 1.87 
3  1 O   D TRP 21  ? ? OG    D SER 25  ? ? 1.95 
4  1 OD2 D ASP 67  ? ? OG1   D THR 72  ? ? 2.05 
5  1 OG  A SER 178 ? ? OE2   A GLU 183 ? ? 2.14 
6  1 OG1 A THR 145 ? ? O3G   A GTP 501 ? ? 2.16 
7  1 NH1 F ARG 197 ? ? OE2   F GLU 257 ? ? 2.16 
8  1 OD1 C ASN 249 ? ? ND2   C ASN 356 ? ? 2.16 
9  1 O   A THR 56  ? ? N     A GLY 59  ? ? 2.17 
10 1 OD2 F ASP 200 ? ? OG1   F THR 241 ? ? 2.18 
11 1 OE2 F GLU 193 ? ? ND1   F HIS 196 ? ? 2.19 
# 
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 LEU A 70  ? ? -61.68  0.06    
2  1 TYR A 161 ? ? -141.02 44.32   
3  1 LYS A 280 ? ? -52.60  108.97  
4  1 ALA A 299 ? ? -64.30  1.65    
5  1 CYS A 305 ? ? -172.64 -179.94 
6  1 HIS A 309 ? ? -106.93 50.02   
7  1 PHE A 404 ? ? 70.44   -15.41  
8  1 THR B 107 ? ? -105.73 -81.67  
9  1 THR B 143 ? ? -61.46  -73.79  
10 1 LEU B 246 ? ? -65.00  -70.59  
11 1 ALA B 302 ? ? -68.85  73.44   
12 1 TYR C 108 ? ? -106.91 -73.44  
13 1 SER C 147 ? ? -90.78  -61.26  
14 1 LYS C 164 ? ? -37.32  138.65  
15 1 ALA C 314 ? ? 179.54  146.32  
16 1 PRO C 364 ? ? -30.21  129.74  
17 1 PHE C 404 ? ? 70.51   -10.63  
18 1 ASN D 57  ? ? 31.61   53.84   
19 1 PRO D 61  ? ? -46.78  150.64  
20 1 PHE D 81  ? ? 69.54   -0.48   
21 1 GLN D 94  ? ? -137.89 -54.12  
22 1 ASN D 99  ? ? 45.65   29.24   
23 1 THR D 107 ? ? -108.57 -95.89  
24 1 VAL D 175 ? ? -140.32 -23.84  
25 1 ARG D 213 ? ? -98.87  -60.77  
26 1 LYS D 216 ? ? 40.57   75.47   
27 1 TYR D 222 ? ? -52.80  -5.83   
28 1 ALA D 302 ? ? -66.99  67.31   
29 1 PHE D 385 ? ? -44.07  -72.05  
30 1 PHE D 394 ? ? 55.48   13.31   
31 1 ILE E 9   ? ? -131.70 -38.27  
32 1 GLU E 10  ? ? -142.55 58.39   
33 1 LEU E 11  ? ? -56.40  107.21  
34 1 CYS E 14  ? ? -169.63 -168.07 
35 1 PHE E 20  ? ? 175.82  156.43  
36 1 LYS E 25  ? ? -171.24 141.33  
37 1 ARG F 36  ? ? -90.74  52.08   
38 1 SER F 88  ? ? 74.45   138.93  
39 1 GLU F 89  ? ? -56.15  -6.43   
40 1 ARG F 142 ? ? 47.89   28.74   
41 1 LYS F 188 ? ? -109.27 74.28   
42 1 ASP F 235 ? ? -100.01 76.06   
43 1 THR F 237 ? ? 82.78   -29.19  
44 1 THR F 241 ? ? -89.05  42.56   
45 1 ARG F 255 ? ? -57.61  -70.88  
46 1 THR F 277 ? ? -128.21 -165.28 
47 1 ILE F 330 ? ? -97.85  -73.57  
# 
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 B 2   ? ? 0.077 'SIDE CHAIN' 
2 1 ARG B 251 ? ? 0.092 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 438 ? A ASP 438 
2  1 Y 1 A SER 439 ? A SER 439 
3  1 Y 1 A VAL 440 ? A VAL 440 
4  1 Y 1 B MET 1   ? B MET 1   
5  1 Y 1 B THR 429 ? B THR 429 
6  1 Y 1 B ALA 430 ? B ALA 430 
7  1 Y 1 B ASP 431 ? B ASP 431 
8  1 Y 1 D THR 274 ? D THR 274 
9  1 Y 1 D SER 275 ? D SER 275 
10 1 Y 1 D ARG 276 ? D ARG 276 
11 1 Y 1 D GLY 277 ? D GLY 277 
12 1 Y 1 D SER 278 ? D SER 278 
13 1 Y 1 D GLN 279 ? D GLN 279 
14 1 Y 1 D GLN 280 ? D GLN 280 
15 1 Y 1 D TYR 281 ? D TYR 281 
16 1 Y 1 D ARG 282 ? D ARG 282 
17 1 Y 1 D ALA 283 ? D ALA 283 
18 1 Y 1 E PHE 29  ? E PHE 24  
19 1 Y 1 E ASP 30  ? E ASP 25  
20 1 Y 1 E GLY 31  ? E GLY 26  
21 1 Y 1 E VAL 32  ? E VAL 27  
22 1 Y 1 E PRO 33  ? E PRO 28  
23 1 Y 1 E GLU 34  ? E GLU 29  
24 1 Y 1 E PHE 35  ? E PHE 30  
25 1 Y 1 E ASN 36  ? E ASN 31  
26 1 Y 1 E ALA 37  ? E ALA 32  
27 1 Y 1 E SER 38  ? E SER 33  
28 1 Y 1 E LEU 39  ? E LEU 34  
29 1 Y 1 E PRO 40  ? E PRO 35  
30 1 Y 1 E ARG 41  ? E ARG 36  
31 1 Y 1 E ARG 42  ? E ARG 37  
32 1 Y 1 E ARG 43  ? E ARG 38  
33 1 Y 1 F ASN 104 ? F ASN 104 
34 1 Y 1 F LEU 105 ? F LEU 105 
35 1 Y 1 F LYS 106 ? F LYS 106 
36 1 Y 1 F THR 107 ? F THR 107 
37 1 Y 1 F PRO 108 ? F PRO 108 
38 1 Y 1 F VAL 109 ? F VAL 109 
39 1 Y 1 F ALA 110 ? F ALA 110 
40 1 Y 1 F PRO 111 ? F PRO 111 
41 1 Y 1 F ALA 112 ? F ALA 112 
42 1 Y 1 F GLN 113 ? F GLN 113 
43 1 Y 1 F ASN 114 ? F ASN 114 
44 1 Y 1 F GLY 115 ? F GLY 115 
45 1 Y 1 F ILE 116 ? F ILE 116 
46 1 Y 1 F ARG 117 ? F ARG 117 
47 1 Y 1 F HIS 118 ? F HIS 118 
48 1 Y 1 F LEU 119 ? F LEU 119 
49 1 Y 1 F ILE 120 ? F ILE 120 
50 1 Y 1 F ASN 121 ? F ASN 121 
51 1 Y 1 F ASN 122 ? F ASN 122 
52 1 Y 1 F THR 123 ? F THR 123 
53 1 Y 1 F ARG 124 ? F ARG 124 
54 1 Y 1 F THR 125 ? F THR 125 
55 1 Y 1 F ASP 126 ? F ASP 126 
56 1 Y 1 F GLU 127 ? F GLU 127 
57 1 Y 1 F ARG 128 ? F ARG 128 
58 1 Y 1 F GLU 129 ? F GLU 129 
59 1 Y 1 F LYS 150 ? F LYS 150 
60 1 Y 1 F SER 151 ? F SER 151 
61 1 Y 1 F SER 152 ? F SER 152 
62 1 Y 1 F ALA 153 ? F ALA 153 
63 1 Y 1 F GLY 154 ? F GLY 154 
64 1 Y 1 F ALA 155 ? F ALA 155 
65 1 Y 1 F LYS 156 ? F LYS 156 
66 1 Y 1 F GLY 157 ? F GLY 157 
67 1 Y 1 F GLU 158 ? F GLU 158 
68 1 Y 1 F GLY 159 ? F GLY 159 
69 1 Y 1 F ILE 160 ? F ILE 160 
70 1 Y 1 F GLU 248 ? F GLU 248 
71 1 Y 1 F TYR 249 ? F TYR 249 
72 1 Y 1 F SER 250 ? F SER 250 
73 1 Y 1 F LYS 251 ? F LYS 251 
74 1 Y 1 F ASN 252 ? F ASN 252 
75 1 Y 1 F ALA 362 ? F ALA 362 
76 1 Y 1 F ASP 363 ? F ASP 363 
77 1 Y 1 F THR 364 ? F THR 364 
78 1 Y 1 F GLY 365 ? F GLY 365 
79 1 Y 1 F GLN 366 ? F GLN 366 
80 1 Y 1 F LYS 367 ? F LYS 367 
81 1 Y 1 F THR 368 ? F THR 368 
82 1 Y 1 F SER 369 ? F SER 369 
83 1 Y 1 F GLN 370 ? F GLN 370 
84 1 Y 1 F PRO 371 ? F PRO 371 
85 1 N 0 A GTP 501 ? G GTP ?   
86 1 N 0 A CA  502 ? H CA  ?   
87 1 N 0 A MG  503 ? I MG  ?   
88 1 N 0 B GDP 501 ? J GDP ?   
89 1 N 0 B MES 502 ? K MES ?   
90 1 N 0 B MES 503 ? L MES ?   
91 1 N 0 B MG  504 ? M MG  ?   
92 1 N 0 C GTP 501 ? O GTP ?   
93 1 N 0 C CA  502 ? P CA  ?   
94 1 N 0 C MG  503 ? Q MG  ?   
95 1 N 0 D GDP 501 ? R GDP ?   
96 1 N 0 F ACP 401 ? T ACP ?   
# 
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 
A1D6D N12    N  N N 1   
A1D6D C13    C  N N 2   
A1D6D C17    C  Y N 3   
A1D6D C20    C  Y N 4   
A1D6D C21    C  Y N 5   
A1D6D C22    C  Y N 6   
A1D6D C24    C  N N 7   
A1D6D C01    C  Y N 8   
A1D6D C02    C  Y N 9   
A1D6D C03    C  Y N 10  
A1D6D C04    C  Y N 11  
A1D6D C05    C  Y N 12  
A1D6D C06    C  Y N 13  
A1D6D C07    C  Y N 14  
A1D6D C09    C  Y N 15  
A1D6D C14    C  N N 16  
A1D6D C18    C  Y N 17  
A1D6D C19    C  Y N 18  
A1D6D F25    F  N N 19  
A1D6D N08    N  Y N 20  
A1D6D N10    N  Y N 21  
A1D6D N16    N  N N 22  
A1D6D O15    O  N N 23  
A1D6D O23    O  N N 24  
A1D6D CL11   CL N N 25  
A1D6D H131   H  N N 26  
A1D6D H132   H  N N 27  
A1D6D H201   H  N N 28  
A1D6D H221   H  N N 29  
A1D6D H243   H  N N 30  
A1D6D H242   H  N N 31  
A1D6D H241   H  N N 32  
A1D6D H021   H  N N 33  
A1D6D H031   H  N N 34  
A1D6D H061   H  N N 35  
A1D6D H191   H  N N 36  
A1D6D H161   H  N N 37  
ACP   PG     P  N N 38  
ACP   O1G    O  N N 39  
ACP   O2G    O  N N 40  
ACP   O3G    O  N N 41  
ACP   PB     P  N S 42  
ACP   O1B    O  N N 43  
ACP   O2B    O  N N 44  
ACP   C3B    C  N N 45  
ACP   PA     P  N R 46  
ACP   O1A    O  N N 47  
ACP   O2A    O  N N 48  
ACP   O3A    O  N N 49  
ACP   "O5'"  O  N N 50  
ACP   "C5'"  C  N N 51  
ACP   "C4'"  C  N R 52  
ACP   "O4'"  O  N N 53  
ACP   "C3'"  C  N S 54  
ACP   "O3'"  O  N N 55  
ACP   "C2'"  C  N R 56  
ACP   "O2'"  O  N N 57  
ACP   "C1'"  C  N R 58  
ACP   N9     N  Y N 59  
ACP   C8     C  Y N 60  
ACP   N7     N  Y N 61  
ACP   C5     C  Y N 62  
ACP   C6     C  Y N 63  
ACP   N6     N  N N 64  
ACP   N1     N  Y N 65  
ACP   C2     C  Y N 66  
ACP   N3     N  Y N 67  
ACP   C4     C  Y N 68  
ACP   HOG2   H  N N 69  
ACP   HOG3   H  N N 70  
ACP   HOB2   H  N N 71  
ACP   H3B1   H  N N 72  
ACP   H3B2   H  N N 73  
ACP   HOA2   H  N N 74  
ACP   "H5'1" H  N N 75  
ACP   "H5'2" H  N N 76  
ACP   "H4'"  H  N N 77  
ACP   "H3'"  H  N N 78  
ACP   "HO3'" H  N N 79  
ACP   "H2'"  H  N N 80  
ACP   "HO2'" H  N N 81  
ACP   "H1'"  H  N N 82  
ACP   H8     H  N N 83  
ACP   HN61   H  N N 84  
ACP   HN62   H  N N 85  
ACP   H2     H  N N 86  
ALA   N      N  N N 87  
ALA   CA     C  N S 88  
ALA   C      C  N N 89  
ALA   O      O  N N 90  
ALA   CB     C  N N 91  
ALA   OXT    O  N N 92  
ALA   H      H  N N 93  
ALA   H2     H  N N 94  
ALA   HA     H  N N 95  
ALA   HB1    H  N N 96  
ALA   HB2    H  N N 97  
ALA   HB3    H  N N 98  
ALA   HXT    H  N N 99  
ARG   N      N  N N 100 
ARG   CA     C  N S 101 
ARG   C      C  N N 102 
ARG   O      O  N N 103 
ARG   CB     C  N N 104 
ARG   CG     C  N N 105 
ARG   CD     C  N N 106 
ARG   NE     N  N N 107 
ARG   CZ     C  N N 108 
ARG   NH1    N  N N 109 
ARG   NH2    N  N N 110 
ARG   OXT    O  N N 111 
ARG   H      H  N N 112 
ARG   H2     H  N N 113 
ARG   HA     H  N N 114 
ARG   HB2    H  N N 115 
ARG   HB3    H  N N 116 
ARG   HG2    H  N N 117 
ARG   HG3    H  N N 118 
ARG   HD2    H  N N 119 
ARG   HD3    H  N N 120 
ARG   HE     H  N N 121 
ARG   HH11   H  N N 122 
ARG   HH12   H  N N 123 
ARG   HH21   H  N N 124 
ARG   HH22   H  N N 125 
ARG   HXT    H  N N 126 
ASN   N      N  N N 127 
ASN   CA     C  N S 128 
ASN   C      C  N N 129 
ASN   O      O  N N 130 
ASN   CB     C  N N 131 
ASN   CG     C  N N 132 
ASN   OD1    O  N N 133 
ASN   ND2    N  N N 134 
ASN   OXT    O  N N 135 
ASN   H      H  N N 136 
ASN   H2     H  N N 137 
ASN   HA     H  N N 138 
ASN   HB2    H  N N 139 
ASN   HB3    H  N N 140 
ASN   HD21   H  N N 141 
ASN   HD22   H  N N 142 
ASN   HXT    H  N N 143 
ASP   N      N  N N 144 
ASP   CA     C  N S 145 
ASP   C      C  N N 146 
ASP   O      O  N N 147 
ASP   CB     C  N N 148 
ASP   CG     C  N N 149 
ASP   OD1    O  N N 150 
ASP   OD2    O  N N 151 
ASP   OXT    O  N N 152 
ASP   H      H  N N 153 
ASP   H2     H  N N 154 
ASP   HA     H  N N 155 
ASP   HB2    H  N N 156 
ASP   HB3    H  N N 157 
ASP   HD2    H  N N 158 
ASP   HXT    H  N N 159 
CA    CA     CA N N 160 
CYS   N      N  N N 161 
CYS   CA     C  N R 162 
CYS   C      C  N N 163 
CYS   O      O  N N 164 
CYS   CB     C  N N 165 
CYS   SG     S  N N 166 
CYS   OXT    O  N N 167 
CYS   H      H  N N 168 
CYS   H2     H  N N 169 
CYS   HA     H  N N 170 
CYS   HB2    H  N N 171 
CYS   HB3    H  N N 172 
CYS   HG     H  N N 173 
CYS   HXT    H  N N 174 
GDP   PB     P  N N 175 
GDP   O1B    O  N N 176 
GDP   O2B    O  N N 177 
GDP   O3B    O  N N 178 
GDP   O3A    O  N N 179 
GDP   PA     P  N N 180 
GDP   O1A    O  N N 181 
GDP   O2A    O  N N 182 
GDP   "O5'"  O  N N 183 
GDP   "C5'"  C  N N 184 
GDP   "C4'"  C  N R 185 
GDP   "O4'"  O  N N 186 
GDP   "C3'"  C  N S 187 
GDP   "O3'"  O  N N 188 
GDP   "C2'"  C  N R 189 
GDP   "O2'"  O  N N 190 
GDP   "C1'"  C  N R 191 
GDP   N9     N  Y N 192 
GDP   C8     C  Y N 193 
GDP   N7     N  Y N 194 
GDP   C5     C  Y N 195 
GDP   C6     C  N N 196 
GDP   O6     O  N N 197 
GDP   N1     N  N N 198 
GDP   C2     C  N N 199 
GDP   N2     N  N N 200 
GDP   N3     N  N N 201 
GDP   C4     C  Y N 202 
GDP   HOB2   H  N N 203 
GDP   HOB3   H  N N 204 
GDP   HOA2   H  N N 205 
GDP   "H5'"  H  N N 206 
GDP   "H5''" H  N N 207 
GDP   "H4'"  H  N N 208 
GDP   "H3'"  H  N N 209 
GDP   "HO3'" H  N N 210 
GDP   "H2'"  H  N N 211 
GDP   "HO2'" H  N N 212 
GDP   "H1'"  H  N N 213 
GDP   H8     H  N N 214 
GDP   HN1    H  N N 215 
GDP   HN21   H  N N 216 
GDP   HN22   H  N N 217 
GLN   N      N  N N 218 
GLN   CA     C  N S 219 
GLN   C      C  N N 220 
GLN   O      O  N N 221 
GLN   CB     C  N N 222 
GLN   CG     C  N N 223 
GLN   CD     C  N N 224 
GLN   OE1    O  N N 225 
GLN   NE2    N  N N 226 
GLN   OXT    O  N N 227 
GLN   H      H  N N 228 
GLN   H2     H  N N 229 
GLN   HA     H  N N 230 
GLN   HB2    H  N N 231 
GLN   HB3    H  N N 232 
GLN   HG2    H  N N 233 
GLN   HG3    H  N N 234 
GLN   HE21   H  N N 235 
GLN   HE22   H  N N 236 
GLN   HXT    H  N N 237 
GLU   N      N  N N 238 
GLU   CA     C  N S 239 
GLU   C      C  N N 240 
GLU   O      O  N N 241 
GLU   CB     C  N N 242 
GLU   CG     C  N N 243 
GLU   CD     C  N N 244 
GLU   OE1    O  N N 245 
GLU   OE2    O  N N 246 
GLU   OXT    O  N N 247 
GLU   H      H  N N 248 
GLU   H2     H  N N 249 
GLU   HA     H  N N 250 
GLU   HB2    H  N N 251 
GLU   HB3    H  N N 252 
GLU   HG2    H  N N 253 
GLU   HG3    H  N N 254 
GLU   HE2    H  N N 255 
GLU   HXT    H  N N 256 
GLY   N      N  N N 257 
GLY   CA     C  N N 258 
GLY   C      C  N N 259 
GLY   O      O  N N 260 
GLY   OXT    O  N N 261 
GLY   H      H  N N 262 
GLY   H2     H  N N 263 
GLY   HA2    H  N N 264 
GLY   HA3    H  N N 265 
GLY   HXT    H  N N 266 
GTP   PG     P  N N 267 
GTP   O1G    O  N N 268 
GTP   O2G    O  N N 269 
GTP   O3G    O  N N 270 
GTP   O3B    O  N N 271 
GTP   PB     P  N N 272 
GTP   O1B    O  N N 273 
GTP   O2B    O  N N 274 
GTP   O3A    O  N N 275 
GTP   PA     P  N N 276 
GTP   O1A    O  N N 277 
GTP   O2A    O  N N 278 
GTP   "O5'"  O  N N 279 
GTP   "C5'"  C  N N 280 
GTP   "C4'"  C  N R 281 
GTP   "O4'"  O  N N 282 
GTP   "C3'"  C  N S 283 
GTP   "O3'"  O  N N 284 
GTP   "C2'"  C  N R 285 
GTP   "O2'"  O  N N 286 
GTP   "C1'"  C  N R 287 
GTP   N9     N  Y N 288 
GTP   C8     C  Y N 289 
GTP   N7     N  Y N 290 
GTP   C5     C  Y N 291 
GTP   C6     C  N N 292 
GTP   O6     O  N N 293 
GTP   N1     N  N N 294 
GTP   C2     C  N N 295 
GTP   N2     N  N N 296 
GTP   N3     N  N N 297 
GTP   C4     C  Y N 298 
GTP   HOG2   H  N N 299 
GTP   HOG3   H  N N 300 
GTP   HOB2   H  N N 301 
GTP   HOA2   H  N N 302 
GTP   "H5'"  H  N N 303 
GTP   "H5''" H  N N 304 
GTP   "H4'"  H  N N 305 
GTP   "H3'"  H  N N 306 
GTP   "HO3'" H  N N 307 
GTP   "H2'"  H  N N 308 
GTP   "HO2'" H  N N 309 
GTP   "H1'"  H  N N 310 
GTP   H8     H  N N 311 
GTP   HN1    H  N N 312 
GTP   HN21   H  N N 313 
GTP   HN22   H  N N 314 
HIS   N      N  N N 315 
HIS   CA     C  N S 316 
HIS   C      C  N N 317 
HIS   O      O  N N 318 
HIS   CB     C  N N 319 
HIS   CG     C  Y N 320 
HIS   ND1    N  Y N 321 
HIS   CD2    C  Y N 322 
HIS   CE1    C  Y N 323 
HIS   NE2    N  Y N 324 
HIS   OXT    O  N N 325 
HIS   H      H  N N 326 
HIS   H2     H  N N 327 
HIS   HA     H  N N 328 
HIS   HB2    H  N N 329 
HIS   HB3    H  N N 330 
HIS   HD1    H  N N 331 
HIS   HD2    H  N N 332 
HIS   HE1    H  N N 333 
HIS   HE2    H  N N 334 
HIS   HXT    H  N N 335 
ILE   N      N  N N 336 
ILE   CA     C  N S 337 
ILE   C      C  N N 338 
ILE   O      O  N N 339 
ILE   CB     C  N S 340 
ILE   CG1    C  N N 341 
ILE   CG2    C  N N 342 
ILE   CD1    C  N N 343 
ILE   OXT    O  N N 344 
ILE   H      H  N N 345 
ILE   H2     H  N N 346 
ILE   HA     H  N N 347 
ILE   HB     H  N N 348 
ILE   HG12   H  N N 349 
ILE   HG13   H  N N 350 
ILE   HG21   H  N N 351 
ILE   HG22   H  N N 352 
ILE   HG23   H  N N 353 
ILE   HD11   H  N N 354 
ILE   HD12   H  N N 355 
ILE   HD13   H  N N 356 
ILE   HXT    H  N N 357 
LEU   N      N  N N 358 
LEU   CA     C  N S 359 
LEU   C      C  N N 360 
LEU   O      O  N N 361 
LEU   CB     C  N N 362 
LEU   CG     C  N N 363 
LEU   CD1    C  N N 364 
LEU   CD2    C  N N 365 
LEU   OXT    O  N N 366 
LEU   H      H  N N 367 
LEU   H2     H  N N 368 
LEU   HA     H  N N 369 
LEU   HB2    H  N N 370 
LEU   HB3    H  N N 371 
LEU   HG     H  N N 372 
LEU   HD11   H  N N 373 
LEU   HD12   H  N N 374 
LEU   HD13   H  N N 375 
LEU   HD21   H  N N 376 
LEU   HD22   H  N N 377 
LEU   HD23   H  N N 378 
LEU   HXT    H  N N 379 
LYS   N      N  N N 380 
LYS   CA     C  N S 381 
LYS   C      C  N N 382 
LYS   O      O  N N 383 
LYS   CB     C  N N 384 
LYS   CG     C  N N 385 
LYS   CD     C  N N 386 
LYS   CE     C  N N 387 
LYS   NZ     N  N N 388 
LYS   OXT    O  N N 389 
LYS   H      H  N N 390 
LYS   H2     H  N N 391 
LYS   HA     H  N N 392 
LYS   HB2    H  N N 393 
LYS   HB3    H  N N 394 
LYS   HG2    H  N N 395 
LYS   HG3    H  N N 396 
LYS   HD2    H  N N 397 
LYS   HD3    H  N N 398 
LYS   HE2    H  N N 399 
LYS   HE3    H  N N 400 
LYS   HZ1    H  N N 401 
LYS   HZ2    H  N N 402 
LYS   HZ3    H  N N 403 
LYS   HXT    H  N N 404 
MES   O1     O  N N 405 
MES   C2     C  N N 406 
MES   C3     C  N N 407 
MES   N4     N  N N 408 
MES   C5     C  N N 409 
MES   C6     C  N N 410 
MES   C7     C  N N 411 
MES   C8     C  N N 412 
MES   S      S  N N 413 
MES   O1S    O  N N 414 
MES   O2S    O  N N 415 
MES   O3S    O  N N 416 
MES   H21    H  N N 417 
MES   H22    H  N N 418 
MES   H31    H  N N 419 
MES   H32    H  N N 420 
MES   HN4    H  N N 421 
MES   H51    H  N N 422 
MES   H52    H  N N 423 
MES   H61    H  N N 424 
MES   H62    H  N N 425 
MES   H71    H  N N 426 
MES   H72    H  N N 427 
MES   H81    H  N N 428 
MES   H82    H  N N 429 
MET   N      N  N N 430 
MET   CA     C  N S 431 
MET   C      C  N N 432 
MET   O      O  N N 433 
MET   CB     C  N N 434 
MET   CG     C  N N 435 
MET   SD     S  N N 436 
MET   CE     C  N N 437 
MET   OXT    O  N N 438 
MET   H      H  N N 439 
MET   H2     H  N N 440 
MET   HA     H  N N 441 
MET   HB2    H  N N 442 
MET   HB3    H  N N 443 
MET   HG2    H  N N 444 
MET   HG3    H  N N 445 
MET   HE1    H  N N 446 
MET   HE2    H  N N 447 
MET   HE3    H  N N 448 
MET   HXT    H  N N 449 
MG    MG     MG N N 450 
PHE   N      N  N N 451 
PHE   CA     C  N S 452 
PHE   C      C  N N 453 
PHE   O      O  N N 454 
PHE   CB     C  N N 455 
PHE   CG     C  Y N 456 
PHE   CD1    C  Y N 457 
PHE   CD2    C  Y N 458 
PHE   CE1    C  Y N 459 
PHE   CE2    C  Y N 460 
PHE   CZ     C  Y N 461 
PHE   OXT    O  N N 462 
PHE   H      H  N N 463 
PHE   H2     H  N N 464 
PHE   HA     H  N N 465 
PHE   HB2    H  N N 466 
PHE   HB3    H  N N 467 
PHE   HD1    H  N N 468 
PHE   HD2    H  N N 469 
PHE   HE1    H  N N 470 
PHE   HE2    H  N N 471 
PHE   HZ     H  N N 472 
PHE   HXT    H  N N 473 
PRO   N      N  N N 474 
PRO   CA     C  N S 475 
PRO   C      C  N N 476 
PRO   O      O  N N 477 
PRO   CB     C  N N 478 
PRO   CG     C  N N 479 
PRO   CD     C  N N 480 
PRO   OXT    O  N N 481 
PRO   H      H  N N 482 
PRO   HA     H  N N 483 
PRO   HB2    H  N N 484 
PRO   HB3    H  N N 485 
PRO   HG2    H  N N 486 
PRO   HG3    H  N N 487 
PRO   HD2    H  N N 488 
PRO   HD3    H  N N 489 
PRO   HXT    H  N N 490 
SER   N      N  N N 491 
SER   CA     C  N S 492 
SER   C      C  N N 493 
SER   O      O  N N 494 
SER   CB     C  N N 495 
SER   OG     O  N N 496 
SER   OXT    O  N N 497 
SER   H      H  N N 498 
SER   H2     H  N N 499 
SER   HA     H  N N 500 
SER   HB2    H  N N 501 
SER   HB3    H  N N 502 
SER   HG     H  N N 503 
SER   HXT    H  N N 504 
THR   N      N  N N 505 
THR   CA     C  N S 506 
THR   C      C  N N 507 
THR   O      O  N N 508 
THR   CB     C  N R 509 
THR   OG1    O  N N 510 
THR   CG2    C  N N 511 
THR   OXT    O  N N 512 
THR   H      H  N N 513 
THR   H2     H  N N 514 
THR   HA     H  N N 515 
THR   HB     H  N N 516 
THR   HG1    H  N N 517 
THR   HG21   H  N N 518 
THR   HG22   H  N N 519 
THR   HG23   H  N N 520 
THR   HXT    H  N N 521 
TRP   N      N  N N 522 
TRP   CA     C  N S 523 
TRP   C      C  N N 524 
TRP   O      O  N N 525 
TRP   CB     C  N N 526 
TRP   CG     C  Y N 527 
TRP   CD1    C  Y N 528 
TRP   CD2    C  Y N 529 
TRP   NE1    N  Y N 530 
TRP   CE2    C  Y N 531 
TRP   CE3    C  Y N 532 
TRP   CZ2    C  Y N 533 
TRP   CZ3    C  Y N 534 
TRP   CH2    C  Y N 535 
TRP   OXT    O  N N 536 
TRP   H      H  N N 537 
TRP   H2     H  N N 538 
TRP   HA     H  N N 539 
TRP   HB2    H  N N 540 
TRP   HB3    H  N N 541 
TRP   HD1    H  N N 542 
TRP   HE1    H  N N 543 
TRP   HE3    H  N N 544 
TRP   HZ2    H  N N 545 
TRP   HZ3    H  N N 546 
TRP   HH2    H  N N 547 
TRP   HXT    H  N N 548 
TYR   N      N  N N 549 
TYR   CA     C  N S 550 
TYR   C      C  N N 551 
TYR   O      O  N N 552 
TYR   CB     C  N N 553 
TYR   CG     C  Y N 554 
TYR   CD1    C  Y N 555 
TYR   CD2    C  Y N 556 
TYR   CE1    C  Y N 557 
TYR   CE2    C  Y N 558 
TYR   CZ     C  Y N 559 
TYR   OH     O  N N 560 
TYR   OXT    O  N N 561 
TYR   H      H  N N 562 
TYR   H2     H  N N 563 
TYR   HA     H  N N 564 
TYR   HB2    H  N N 565 
TYR   HB3    H  N N 566 
TYR   HD1    H  N N 567 
TYR   HD2    H  N N 568 
TYR   HE1    H  N N 569 
TYR   HE2    H  N N 570 
TYR   HH     H  N N 571 
TYR   HXT    H  N N 572 
VAL   N      N  N N 573 
VAL   CA     C  N S 574 
VAL   C      C  N N 575 
VAL   O      O  N N 576 
VAL   CB     C  N N 577 
VAL   CG1    C  N N 578 
VAL   CG2    C  N N 579 
VAL   OXT    O  N N 580 
VAL   H      H  N N 581 
VAL   H2     H  N N 582 
VAL   HA     H  N N 583 
VAL   HB     H  N N 584 
VAL   HG11   H  N N 585 
VAL   HG12   H  N N 586 
VAL   HG13   H  N N 587 
VAL   HG21   H  N N 588 
VAL   HG22   H  N N 589 
VAL   HG23   H  N N 590 
VAL   HXT    H  N N 591 
# 
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 
A1D6D C24   O23    sing N N 1   
A1D6D O23   C21    sing N N 2   
A1D6D C22   C21    doub Y N 3   
A1D6D C22   C17    sing Y N 4   
A1D6D C21   C20    sing Y N 5   
A1D6D N16   C17    sing N N 6   
A1D6D N16   C14    sing N N 7   
A1D6D C17   C18    doub Y N 8   
A1D6D C20   C19    doub Y N 9   
A1D6D O15   C14    doub N N 10  
A1D6D C14   C13    sing N N 11  
A1D6D C18   C19    sing Y N 12  
A1D6D C18   N12    sing N N 13  
A1D6D F25   C01    sing N N 14  
A1D6D C13   N12    sing N N 15  
A1D6D N12   C07    sing N N 16  
A1D6D C06   C01    doub Y N 17  
A1D6D C06   C05    sing Y N 18  
A1D6D C01   C02    sing Y N 19  
A1D6D C07   C05    doub Y N 20  
A1D6D C07   N08    sing Y N 21  
A1D6D C05   C04    sing Y N 22  
A1D6D C02   C03    doub Y N 23  
A1D6D N08   C09    doub Y N 24  
A1D6D C04   C03    sing Y N 25  
A1D6D C04   N10    doub Y N 26  
A1D6D C09   N10    sing Y N 27  
A1D6D C09   CL11   sing N N 28  
A1D6D C13   H131   sing N N 29  
A1D6D C13   H132   sing N N 30  
A1D6D C20   H201   sing N N 31  
A1D6D C22   H221   sing N N 32  
A1D6D C24   H243   sing N N 33  
A1D6D C24   H242   sing N N 34  
A1D6D C24   H241   sing N N 35  
A1D6D C02   H021   sing N N 36  
A1D6D C03   H031   sing N N 37  
A1D6D C06   H061   sing N N 38  
A1D6D C19   H191   sing N N 39  
A1D6D N16   H161   sing N N 40  
ACP   PG    O1G    doub N N 41  
ACP   PG    O2G    sing N N 42  
ACP   PG    O3G    sing N N 43  
ACP   PG    C3B    sing N N 44  
ACP   O2G   HOG2   sing N N 45  
ACP   O3G   HOG3   sing N N 46  
ACP   PB    O1B    doub N N 47  
ACP   PB    O2B    sing N N 48  
ACP   PB    C3B    sing N N 49  
ACP   PB    O3A    sing N N 50  
ACP   O2B   HOB2   sing N N 51  
ACP   C3B   H3B1   sing N N 52  
ACP   C3B   H3B2   sing N N 53  
ACP   PA    O1A    doub N N 54  
ACP   PA    O2A    sing N N 55  
ACP   PA    O3A    sing N N 56  
ACP   PA    "O5'"  sing N N 57  
ACP   O2A   HOA2   sing N N 58  
ACP   "O5'" "C5'"  sing N N 59  
ACP   "C5'" "C4'"  sing N N 60  
ACP   "C5'" "H5'1" sing N N 61  
ACP   "C5'" "H5'2" sing N N 62  
ACP   "C4'" "O4'"  sing N N 63  
ACP   "C4'" "C3'"  sing N N 64  
ACP   "C4'" "H4'"  sing N N 65  
ACP   "O4'" "C1'"  sing N N 66  
ACP   "C3'" "O3'"  sing N N 67  
ACP   "C3'" "C2'"  sing N N 68  
ACP   "C3'" "H3'"  sing N N 69  
ACP   "O3'" "HO3'" sing N N 70  
ACP   "C2'" "O2'"  sing N N 71  
ACP   "C2'" "C1'"  sing N N 72  
ACP   "C2'" "H2'"  sing N N 73  
ACP   "O2'" "HO2'" sing N N 74  
ACP   "C1'" N9     sing N N 75  
ACP   "C1'" "H1'"  sing N N 76  
ACP   N9    C8     sing Y N 77  
ACP   N9    C4     sing Y N 78  
ACP   C8    N7     doub Y N 79  
ACP   C8    H8     sing N N 80  
ACP   N7    C5     sing Y N 81  
ACP   C5    C6     sing Y N 82  
ACP   C5    C4     doub Y N 83  
ACP   C6    N6     sing N N 84  
ACP   C6    N1     doub Y N 85  
ACP   N6    HN61   sing N N 86  
ACP   N6    HN62   sing N N 87  
ACP   N1    C2     sing Y N 88  
ACP   C2    N3     doub Y N 89  
ACP   C2    H2     sing N N 90  
ACP   N3    C4     sing Y N 91  
ALA   N     CA     sing N N 92  
ALA   N     H      sing N N 93  
ALA   N     H2     sing N N 94  
ALA   CA    C      sing N N 95  
ALA   CA    CB     sing N N 96  
ALA   CA    HA     sing N N 97  
ALA   C     O      doub N N 98  
ALA   C     OXT    sing N N 99  
ALA   CB    HB1    sing N N 100 
ALA   CB    HB2    sing N N 101 
ALA   CB    HB3    sing N N 102 
ALA   OXT   HXT    sing N N 103 
ARG   N     CA     sing N N 104 
ARG   N     H      sing N N 105 
ARG   N     H2     sing N N 106 
ARG   CA    C      sing N N 107 
ARG   CA    CB     sing N N 108 
ARG   CA    HA     sing N N 109 
ARG   C     O      doub N N 110 
ARG   C     OXT    sing N N 111 
ARG   CB    CG     sing N N 112 
ARG   CB    HB2    sing N N 113 
ARG   CB    HB3    sing N N 114 
ARG   CG    CD     sing N N 115 
ARG   CG    HG2    sing N N 116 
ARG   CG    HG3    sing N N 117 
ARG   CD    NE     sing N N 118 
ARG   CD    HD2    sing N N 119 
ARG   CD    HD3    sing N N 120 
ARG   NE    CZ     sing N N 121 
ARG   NE    HE     sing N N 122 
ARG   CZ    NH1    sing N N 123 
ARG   CZ    NH2    doub N N 124 
ARG   NH1   HH11   sing N N 125 
ARG   NH1   HH12   sing N N 126 
ARG   NH2   HH21   sing N N 127 
ARG   NH2   HH22   sing N N 128 
ARG   OXT   HXT    sing N N 129 
ASN   N     CA     sing N N 130 
ASN   N     H      sing N N 131 
ASN   N     H2     sing N N 132 
ASN   CA    C      sing N N 133 
ASN   CA    CB     sing N N 134 
ASN   CA    HA     sing N N 135 
ASN   C     O      doub N N 136 
ASN   C     OXT    sing N N 137 
ASN   CB    CG     sing N N 138 
ASN   CB    HB2    sing N N 139 
ASN   CB    HB3    sing N N 140 
ASN   CG    OD1    doub N N 141 
ASN   CG    ND2    sing N N 142 
ASN   ND2   HD21   sing N N 143 
ASN   ND2   HD22   sing N N 144 
ASN   OXT   HXT    sing N N 145 
ASP   N     CA     sing N N 146 
ASP   N     H      sing N N 147 
ASP   N     H2     sing N N 148 
ASP   CA    C      sing N N 149 
ASP   CA    CB     sing N N 150 
ASP   CA    HA     sing N N 151 
ASP   C     O      doub N N 152 
ASP   C     OXT    sing N N 153 
ASP   CB    CG     sing N N 154 
ASP   CB    HB2    sing N N 155 
ASP   CB    HB3    sing N N 156 
ASP   CG    OD1    doub N N 157 
ASP   CG    OD2    sing N N 158 
ASP   OD2   HD2    sing N N 159 
ASP   OXT   HXT    sing N N 160 
CYS   N     CA     sing N N 161 
CYS   N     H      sing N N 162 
CYS   N     H2     sing N N 163 
CYS   CA    C      sing N N 164 
CYS   CA    CB     sing N N 165 
CYS   CA    HA     sing N N 166 
CYS   C     O      doub N N 167 
CYS   C     OXT    sing N N 168 
CYS   CB    SG     sing N N 169 
CYS   CB    HB2    sing N N 170 
CYS   CB    HB3    sing N N 171 
CYS   SG    HG     sing N N 172 
CYS   OXT   HXT    sing N N 173 
GDP   PB    O1B    doub N N 174 
GDP   PB    O2B    sing N N 175 
GDP   PB    O3B    sing N N 176 
GDP   PB    O3A    sing N N 177 
GDP   O2B   HOB2   sing N N 178 
GDP   O3B   HOB3   sing N N 179 
GDP   O3A   PA     sing N N 180 
GDP   PA    O1A    doub N N 181 
GDP   PA    O2A    sing N N 182 
GDP   PA    "O5'"  sing N N 183 
GDP   O2A   HOA2   sing N N 184 
GDP   "O5'" "C5'"  sing N N 185 
GDP   "C5'" "C4'"  sing N N 186 
GDP   "C5'" "H5'"  sing N N 187 
GDP   "C5'" "H5''" sing N N 188 
GDP   "C4'" "O4'"  sing N N 189 
GDP   "C4'" "C3'"  sing N N 190 
GDP   "C4'" "H4'"  sing N N 191 
GDP   "O4'" "C1'"  sing N N 192 
GDP   "C3'" "O3'"  sing N N 193 
GDP   "C3'" "C2'"  sing N N 194 
GDP   "C3'" "H3'"  sing N N 195 
GDP   "O3'" "HO3'" sing N N 196 
GDP   "C2'" "O2'"  sing N N 197 
GDP   "C2'" "C1'"  sing N N 198 
GDP   "C2'" "H2'"  sing N N 199 
GDP   "O2'" "HO2'" sing N N 200 
GDP   "C1'" N9     sing N N 201 
GDP   "C1'" "H1'"  sing N N 202 
GDP   N9    C8     sing Y N 203 
GDP   N9    C4     sing Y N 204 
GDP   C8    N7     doub Y N 205 
GDP   C8    H8     sing N N 206 
GDP   N7    C5     sing Y N 207 
GDP   C5    C6     sing N N 208 
GDP   C5    C4     doub Y N 209 
GDP   C6    O6     doub N N 210 
GDP   C6    N1     sing N N 211 
GDP   N1    C2     sing N N 212 
GDP   N1    HN1    sing N N 213 
GDP   C2    N2     sing N N 214 
GDP   C2    N3     doub N N 215 
GDP   N2    HN21   sing N N 216 
GDP   N2    HN22   sing N N 217 
GDP   N3    C4     sing N N 218 
GLN   N     CA     sing N N 219 
GLN   N     H      sing N N 220 
GLN   N     H2     sing N N 221 
GLN   CA    C      sing N N 222 
GLN   CA    CB     sing N N 223 
GLN   CA    HA     sing N N 224 
GLN   C     O      doub N N 225 
GLN   C     OXT    sing N N 226 
GLN   CB    CG     sing N N 227 
GLN   CB    HB2    sing N N 228 
GLN   CB    HB3    sing N N 229 
GLN   CG    CD     sing N N 230 
GLN   CG    HG2    sing N N 231 
GLN   CG    HG3    sing N N 232 
GLN   CD    OE1    doub N N 233 
GLN   CD    NE2    sing N N 234 
GLN   NE2   HE21   sing N N 235 
GLN   NE2   HE22   sing N N 236 
GLN   OXT   HXT    sing N N 237 
GLU   N     CA     sing N N 238 
GLU   N     H      sing N N 239 
GLU   N     H2     sing N N 240 
GLU   CA    C      sing N N 241 
GLU   CA    CB     sing N N 242 
GLU   CA    HA     sing N N 243 
GLU   C     O      doub N N 244 
GLU   C     OXT    sing N N 245 
GLU   CB    CG     sing N N 246 
GLU   CB    HB2    sing N N 247 
GLU   CB    HB3    sing N N 248 
GLU   CG    CD     sing N N 249 
GLU   CG    HG2    sing N N 250 
GLU   CG    HG3    sing N N 251 
GLU   CD    OE1    doub N N 252 
GLU   CD    OE2    sing N N 253 
GLU   OE2   HE2    sing N N 254 
GLU   OXT   HXT    sing N N 255 
GLY   N     CA     sing N N 256 
GLY   N     H      sing N N 257 
GLY   N     H2     sing N N 258 
GLY   CA    C      sing N N 259 
GLY   CA    HA2    sing N N 260 
GLY   CA    HA3    sing N N 261 
GLY   C     O      doub N N 262 
GLY   C     OXT    sing N N 263 
GLY   OXT   HXT    sing N N 264 
GTP   PG    O1G    doub N N 265 
GTP   PG    O2G    sing N N 266 
GTP   PG    O3G    sing N N 267 
GTP   PG    O3B    sing N N 268 
GTP   O2G   HOG2   sing N N 269 
GTP   O3G   HOG3   sing N N 270 
GTP   O3B   PB     sing N N 271 
GTP   PB    O1B    doub N N 272 
GTP   PB    O2B    sing N N 273 
GTP   PB    O3A    sing N N 274 
GTP   O2B   HOB2   sing N N 275 
GTP   O3A   PA     sing N N 276 
GTP   PA    O1A    doub N N 277 
GTP   PA    O2A    sing N N 278 
GTP   PA    "O5'"  sing N N 279 
GTP   O2A   HOA2   sing N N 280 
GTP   "O5'" "C5'"  sing N N 281 
GTP   "C5'" "C4'"  sing N N 282 
GTP   "C5'" "H5'"  sing N N 283 
GTP   "C5'" "H5''" sing N N 284 
GTP   "C4'" "O4'"  sing N N 285 
GTP   "C4'" "C3'"  sing N N 286 
GTP   "C4'" "H4'"  sing N N 287 
GTP   "O4'" "C1'"  sing N N 288 
GTP   "C3'" "O3'"  sing N N 289 
GTP   "C3'" "C2'"  sing N N 290 
GTP   "C3'" "H3'"  sing N N 291 
GTP   "O3'" "HO3'" sing N N 292 
GTP   "C2'" "O2'"  sing N N 293 
GTP   "C2'" "C1'"  sing N N 294 
GTP   "C2'" "H2'"  sing N N 295 
GTP   "O2'" "HO2'" sing N N 296 
GTP   "C1'" N9     sing N N 297 
GTP   "C1'" "H1'"  sing N N 298 
GTP   N9    C8     sing Y N 299 
GTP   N9    C4     sing Y N 300 
GTP   C8    N7     doub Y N 301 
GTP   C8    H8     sing N N 302 
GTP   N7    C5     sing Y N 303 
GTP   C5    C6     sing N N 304 
GTP   C5    C4     doub Y N 305 
GTP   C6    O6     doub N N 306 
GTP   C6    N1     sing N N 307 
GTP   N1    C2     sing N N 308 
GTP   N1    HN1    sing N N 309 
GTP   C2    N2     sing N N 310 
GTP   C2    N3     doub N N 311 
GTP   N2    HN21   sing N N 312 
GTP   N2    HN22   sing N N 313 
GTP   N3    C4     sing N N 314 
HIS   N     CA     sing N N 315 
HIS   N     H      sing N N 316 
HIS   N     H2     sing N N 317 
HIS   CA    C      sing N N 318 
HIS   CA    CB     sing N N 319 
HIS   CA    HA     sing N N 320 
HIS   C     O      doub N N 321 
HIS   C     OXT    sing N N 322 
HIS   CB    CG     sing N N 323 
HIS   CB    HB2    sing N N 324 
HIS   CB    HB3    sing N N 325 
HIS   CG    ND1    sing Y N 326 
HIS   CG    CD2    doub Y N 327 
HIS   ND1   CE1    doub Y N 328 
HIS   ND1   HD1    sing N N 329 
HIS   CD2   NE2    sing Y N 330 
HIS   CD2   HD2    sing N N 331 
HIS   CE1   NE2    sing Y N 332 
HIS   CE1   HE1    sing N N 333 
HIS   NE2   HE2    sing N N 334 
HIS   OXT   HXT    sing N N 335 
ILE   N     CA     sing N N 336 
ILE   N     H      sing N N 337 
ILE   N     H2     sing N N 338 
ILE   CA    C      sing N N 339 
ILE   CA    CB     sing N N 340 
ILE   CA    HA     sing N N 341 
ILE   C     O      doub N N 342 
ILE   C     OXT    sing N N 343 
ILE   CB    CG1    sing N N 344 
ILE   CB    CG2    sing N N 345 
ILE   CB    HB     sing N N 346 
ILE   CG1   CD1    sing N N 347 
ILE   CG1   HG12   sing N N 348 
ILE   CG1   HG13   sing N N 349 
ILE   CG2   HG21   sing N N 350 
ILE   CG2   HG22   sing N N 351 
ILE   CG2   HG23   sing N N 352 
ILE   CD1   HD11   sing N N 353 
ILE   CD1   HD12   sing N N 354 
ILE   CD1   HD13   sing N N 355 
ILE   OXT   HXT    sing N N 356 
LEU   N     CA     sing N N 357 
LEU   N     H      sing N N 358 
LEU   N     H2     sing N N 359 
LEU   CA    C      sing N N 360 
LEU   CA    CB     sing N N 361 
LEU   CA    HA     sing N N 362 
LEU   C     O      doub N N 363 
LEU   C     OXT    sing N N 364 
LEU   CB    CG     sing N N 365 
LEU   CB    HB2    sing N N 366 
LEU   CB    HB3    sing N N 367 
LEU   CG    CD1    sing N N 368 
LEU   CG    CD2    sing N N 369 
LEU   CG    HG     sing N N 370 
LEU   CD1   HD11   sing N N 371 
LEU   CD1   HD12   sing N N 372 
LEU   CD1   HD13   sing N N 373 
LEU   CD2   HD21   sing N N 374 
LEU   CD2   HD22   sing N N 375 
LEU   CD2   HD23   sing N N 376 
LEU   OXT   HXT    sing N N 377 
LYS   N     CA     sing N N 378 
LYS   N     H      sing N N 379 
LYS   N     H2     sing N N 380 
LYS   CA    C      sing N N 381 
LYS   CA    CB     sing N N 382 
LYS   CA    HA     sing N N 383 
LYS   C     O      doub N N 384 
LYS   C     OXT    sing N N 385 
LYS   CB    CG     sing N N 386 
LYS   CB    HB2    sing N N 387 
LYS   CB    HB3    sing N N 388 
LYS   CG    CD     sing N N 389 
LYS   CG    HG2    sing N N 390 
LYS   CG    HG3    sing N N 391 
LYS   CD    CE     sing N N 392 
LYS   CD    HD2    sing N N 393 
LYS   CD    HD3    sing N N 394 
LYS   CE    NZ     sing N N 395 
LYS   CE    HE2    sing N N 396 
LYS   CE    HE3    sing N N 397 
LYS   NZ    HZ1    sing N N 398 
LYS   NZ    HZ2    sing N N 399 
LYS   NZ    HZ3    sing N N 400 
LYS   OXT   HXT    sing N N 401 
MES   O1    C2     sing N N 402 
MES   O1    C6     sing N N 403 
MES   C2    C3     sing N N 404 
MES   C2    H21    sing N N 405 
MES   C2    H22    sing N N 406 
MES   C3    N4     sing N N 407 
MES   C3    H31    sing N N 408 
MES   C3    H32    sing N N 409 
MES   N4    C5     sing N N 410 
MES   N4    C7     sing N N 411 
MES   N4    HN4    sing N N 412 
MES   C5    C6     sing N N 413 
MES   C5    H51    sing N N 414 
MES   C5    H52    sing N N 415 
MES   C6    H61    sing N N 416 
MES   C6    H62    sing N N 417 
MES   C7    C8     sing N N 418 
MES   C7    H71    sing N N 419 
MES   C7    H72    sing N N 420 
MES   C8    S      sing N N 421 
MES   C8    H81    sing N N 422 
MES   C8    H82    sing N N 423 
MES   S     O1S    doub N N 424 
MES   S     O2S    doub N N 425 
MES   S     O3S    sing N N 426 
MET   N     CA     sing N N 427 
MET   N     H      sing N N 428 
MET   N     H2     sing N N 429 
MET   CA    C      sing N N 430 
MET   CA    CB     sing N N 431 
MET   CA    HA     sing N N 432 
MET   C     O      doub N N 433 
MET   C     OXT    sing N N 434 
MET   CB    CG     sing N N 435 
MET   CB    HB2    sing N N 436 
MET   CB    HB3    sing N N 437 
MET   CG    SD     sing N N 438 
MET   CG    HG2    sing N N 439 
MET   CG    HG3    sing N N 440 
MET   SD    CE     sing N N 441 
MET   CE    HE1    sing N N 442 
MET   CE    HE2    sing N N 443 
MET   CE    HE3    sing N N 444 
MET   OXT   HXT    sing N N 445 
PHE   N     CA     sing N N 446 
PHE   N     H      sing N N 447 
PHE   N     H2     sing N N 448 
PHE   CA    C      sing N N 449 
PHE   CA    CB     sing N N 450 
PHE   CA    HA     sing N N 451 
PHE   C     O      doub N N 452 
PHE   C     OXT    sing N N 453 
PHE   CB    CG     sing N N 454 
PHE   CB    HB2    sing N N 455 
PHE   CB    HB3    sing N N 456 
PHE   CG    CD1    doub Y N 457 
PHE   CG    CD2    sing Y N 458 
PHE   CD1   CE1    sing Y N 459 
PHE   CD1   HD1    sing N N 460 
PHE   CD2   CE2    doub Y N 461 
PHE   CD2   HD2    sing N N 462 
PHE   CE1   CZ     doub Y N 463 
PHE   CE1   HE1    sing N N 464 
PHE   CE2   CZ     sing Y N 465 
PHE   CE2   HE2    sing N N 466 
PHE   CZ    HZ     sing N N 467 
PHE   OXT   HXT    sing N N 468 
PRO   N     CA     sing N N 469 
PRO   N     CD     sing N N 470 
PRO   N     H      sing N N 471 
PRO   CA    C      sing N N 472 
PRO   CA    CB     sing N N 473 
PRO   CA    HA     sing N N 474 
PRO   C     O      doub N N 475 
PRO   C     OXT    sing N N 476 
PRO   CB    CG     sing N N 477 
PRO   CB    HB2    sing N N 478 
PRO   CB    HB3    sing N N 479 
PRO   CG    CD     sing N N 480 
PRO   CG    HG2    sing N N 481 
PRO   CG    HG3    sing N N 482 
PRO   CD    HD2    sing N N 483 
PRO   CD    HD3    sing N N 484 
PRO   OXT   HXT    sing N N 485 
SER   N     CA     sing N N 486 
SER   N     H      sing N N 487 
SER   N     H2     sing N N 488 
SER   CA    C      sing N N 489 
SER   CA    CB     sing N N 490 
SER   CA    HA     sing N N 491 
SER   C     O      doub N N 492 
SER   C     OXT    sing N N 493 
SER   CB    OG     sing N N 494 
SER   CB    HB2    sing N N 495 
SER   CB    HB3    sing N N 496 
SER   OG    HG     sing N N 497 
SER   OXT   HXT    sing N N 498 
THR   N     CA     sing N N 499 
THR   N     H      sing N N 500 
THR   N     H2     sing N N 501 
THR   CA    C      sing N N 502 
THR   CA    CB     sing N N 503 
THR   CA    HA     sing N N 504 
THR   C     O      doub N N 505 
THR   C     OXT    sing N N 506 
THR   CB    OG1    sing N N 507 
THR   CB    CG2    sing N N 508 
THR   CB    HB     sing N N 509 
THR   OG1   HG1    sing N N 510 
THR   CG2   HG21   sing N N 511 
THR   CG2   HG22   sing N N 512 
THR   CG2   HG23   sing N N 513 
THR   OXT   HXT    sing N N 514 
TRP   N     CA     sing N N 515 
TRP   N     H      sing N N 516 
TRP   N     H2     sing N N 517 
TRP   CA    C      sing N N 518 
TRP   CA    CB     sing N N 519 
TRP   CA    HA     sing N N 520 
TRP   C     O      doub N N 521 
TRP   C     OXT    sing N N 522 
TRP   CB    CG     sing N N 523 
TRP   CB    HB2    sing N N 524 
TRP   CB    HB3    sing N N 525 
TRP   CG    CD1    doub Y N 526 
TRP   CG    CD2    sing Y N 527 
TRP   CD1   NE1    sing Y N 528 
TRP   CD1   HD1    sing N N 529 
TRP   CD2   CE2    doub Y N 530 
TRP   CD2   CE3    sing Y N 531 
TRP   NE1   CE2    sing Y N 532 
TRP   NE1   HE1    sing N N 533 
TRP   CE2   CZ2    sing Y N 534 
TRP   CE3   CZ3    doub Y N 535 
TRP   CE3   HE3    sing N N 536 
TRP   CZ2   CH2    doub Y N 537 
TRP   CZ2   HZ2    sing N N 538 
TRP   CZ3   CH2    sing Y N 539 
TRP   CZ3   HZ3    sing N N 540 
TRP   CH2   HH2    sing N N 541 
TRP   OXT   HXT    sing N N 542 
TYR   N     CA     sing N N 543 
TYR   N     H      sing N N 544 
TYR   N     H2     sing N N 545 
TYR   CA    C      sing N N 546 
TYR   CA    CB     sing N N 547 
TYR   CA    HA     sing N N 548 
TYR   C     O      doub N N 549 
TYR   C     OXT    sing N N 550 
TYR   CB    CG     sing N N 551 
TYR   CB    HB2    sing N N 552 
TYR   CB    HB3    sing N N 553 
TYR   CG    CD1    doub Y N 554 
TYR   CG    CD2    sing Y N 555 
TYR   CD1   CE1    sing Y N 556 
TYR   CD1   HD1    sing N N 557 
TYR   CD2   CE2    doub Y N 558 
TYR   CD2   HD2    sing N N 559 
TYR   CE1   CZ     doub Y N 560 
TYR   CE1   HE1    sing N N 561 
TYR   CE2   CZ     sing Y N 562 
TYR   CE2   HE2    sing N N 563 
TYR   CZ    OH     sing N N 564 
TYR   OH    HH     sing N N 565 
TYR   OXT   HXT    sing N N 566 
VAL   N     CA     sing N N 567 
VAL   N     H      sing N N 568 
VAL   N     H2     sing N N 569 
VAL   CA    C      sing N N 570 
VAL   CA    CB     sing N N 571 
VAL   CA    HA     sing N N 572 
VAL   C     O      doub N N 573 
VAL   C     OXT    sing N N 574 
VAL   CB    CG1    sing N N 575 
VAL   CB    CG2    sing N N 576 
VAL   CB    HB     sing N N 577 
VAL   CG1   HG11   sing N N 578 
VAL   CG1   HG12   sing N N 579 
VAL   CG1   HG13   sing N N 580 
VAL   CG2   HG21   sing N N 581 
VAL   CG2   HG22   sing N N 582 
VAL   CG2   HG23   sing N N 583 
VAL   OXT   HXT    sing N N 584 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6D88 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YEM 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009529 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006377 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005491 
_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  
CA 
CL 
F  
H  
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   ? 39.875  -102.060 -66.133  1.00 81.00  ? 1   MET   A N      1 
ATOM   2     C  CA     . MET   A 1  1   ? 38.828  -101.131 -65.693  1.00 76.34  ? 1   MET   A CA     1 
ATOM   3     C  C      . MET   A 1  1   ? 39.423  -99.921  -64.933  1.00 70.51  ? 1   MET   A C      1 
ATOM   4     O  O      . MET   A 1  1   ? 40.427  -100.049 -64.213  1.00 68.71  ? 1   MET   A O      1 
ATOM   5     C  CB     . MET   A 1  1   ? 37.809  -101.872 -64.822  1.00 67.54  ? 1   MET   A CB     1 
ATOM   6     C  CG     . MET   A 1  1   ? 36.984  -101.011 -63.860  1.00 69.48  ? 1   MET   A CG     1 
ATOM   7     S  SD     . MET   A 1  1   ? 37.843  -100.530 -62.338  1.00 72.06  ? 1   MET   A SD     1 
ATOM   8     C  CE     . MET   A 1  1   ? 37.267  -101.786 -61.186  1.00 64.57  ? 1   MET   A CE     1 
ATOM   9     N  N      . ARG   A 1  2   ? 38.782  -98.761  -65.085  1.00 66.73  ? 2   ARG   A N      1 
ATOM   10    C  CA     . ARG   A 1  2   ? 39.255  -97.496  -64.525  1.00 70.60  ? 2   ARG   A CA     1 
ATOM   11    C  C      . ARG   A 1  2   ? 38.231  -96.935  -63.537  1.00 69.35  ? 2   ARG   A C      1 
ATOM   12    O  O      . ARG   A 1  2   ? 37.063  -96.726  -63.892  1.00 62.50  ? 2   ARG   A O      1 
ATOM   13    C  CB     . ARG   A 1  2   ? 39.531  -96.480  -65.638  1.00 70.62  ? 2   ARG   A CB     1 
ATOM   14    C  CG     . ARG   A 1  2   ? 40.057  -97.074  -66.934  1.00 70.45  ? 2   ARG   A CG     1 
ATOM   15    C  CD     . ARG   A 1  2   ? 40.944  -96.046  -67.624  1.00 78.73  ? 2   ARG   A CD     1 
ATOM   16    N  NE     . ARG   A 1  2   ? 42.119  -95.739  -66.811  1.00 77.63  ? 2   ARG   A NE     1 
ATOM   17    C  CZ     . ARG   A 1  2   ? 42.746  -94.568  -66.799  1.00 78.62  ? 2   ARG   A CZ     1 
ATOM   18    N  NH1    . ARG   A 1  2   ? 42.321  -93.549  -67.535  1.00 68.16  ? 2   ARG   A NH1    1 
ATOM   19    N  NH2    . ARG   A 1  2   ? 43.825  -94.417  -66.030  1.00 71.56  ? 2   ARG   A NH2    1 
ATOM   20    N  N      . GLU   A 1  3   ? 38.684  -96.658  -62.312  1.00 68.90  ? 3   GLU   A N      1 
ATOM   21    C  CA     . GLU   A 1  3   ? 37.804  -96.222  -61.233  1.00 62.19  ? 3   GLU   A CA     1 
ATOM   22    C  C      . GLU   A 1  3   ? 37.527  -94.724  -61.315  1.00 59.45  ? 3   GLU   A C      1 
ATOM   23    O  O      . GLU   A 1  3   ? 38.310  -93.946  -61.872  1.00 56.56  ? 3   GLU   A O      1 
ATOM   24    C  CB     . GLU   A 1  3   ? 38.411  -96.560  -59.864  1.00 63.44  ? 3   GLU   A CB     1 
ATOM   25    C  CG     . GLU   A 1  3   ? 38.740  -98.044  -59.660  1.00 64.70  ? 3   GLU   A CG     1 
ATOM   26    C  CD     . GLU   A 1  3   ? 40.107  -98.431  -60.241  1.00 65.38  ? 3   GLU   A CD     1 
ATOM   27    O  OE1    . GLU   A 1  3   ? 40.727  -97.603  -60.957  1.00 66.16  ? 3   GLU   A OE1    1 
ATOM   28    O  OE2    . GLU   A 1  3   ? 40.546  -99.576  -60.010  1.00 58.85  ? 3   GLU   A OE2    1 
ATOM   29    N  N      . CYS   A 1  4   ? 36.383  -94.332  -60.747  1.00 65.48  ? 4   CYS   A N      1 
ATOM   30    C  CA     . CYS   A 1  4   ? 35.913  -92.951  -60.680  1.00 60.31  ? 4   CYS   A CA     1 
ATOM   31    C  C      . CYS   A 1  4   ? 35.583  -92.631  -59.231  1.00 55.14  ? 4   CYS   A C      1 
ATOM   32    O  O      . CYS   A 1  4   ? 34.856  -93.394  -58.585  1.00 52.79  ? 4   CYS   A O      1 
ATOM   33    C  CB     . CYS   A 1  4   ? 34.661  -92.756  -61.547  1.00 60.37  ? 4   CYS   A CB     1 
ATOM   34    S  SG     . CYS   A 1  4   ? 34.980  -92.635  -63.295  1.00 59.77  ? 4   CYS   A SG     1 
ATOM   35    N  N      . ILE   A 1  5   ? 36.099  -91.514  -58.714  1.00 53.18  ? 5   ILE   A N      1 
ATOM   36    C  CA     . ILE   A 1  5   ? 35.844  -91.125  -57.325  1.00 54.13  ? 5   ILE   A CA     1 
ATOM   37    C  C      . ILE   A 1  5   ? 34.822  -89.993  -57.292  1.00 51.36  ? 5   ILE   A C      1 
ATOM   38    O  O      . ILE   A 1  5   ? 34.970  -88.985  -58.003  1.00 50.14  ? 5   ILE   A O      1 
ATOM   39    C  CB     . ILE   A 1  5   ? 37.130  -90.715  -56.591  1.00 52.46  ? 5   ILE   A CB     1 
ATOM   40    C  CG1    . ILE   A 1  5   ? 38.132  -91.856  -56.575  1.00 45.36  ? 5   ILE   A CG1    1 
ATOM   41    C  CG2    . ILE   A 1  5   ? 36.812  -90.338  -55.157  1.00 49.71  ? 5   ILE   A CG2    1 
ATOM   42    C  CD1    . ILE   A 1  5   ? 39.449  -91.412  -56.032  1.00 49.78  ? 5   ILE   A CD1    1 
ATOM   43    N  N      . SER   A 1  6   ? 33.791  -90.163  -56.465  1.00 42.50  ? 6   SER   A N      1 
ATOM   44    C  CA     . SER   A 1  6   ? 32.729  -89.176  -56.304  1.00 49.59  ? 6   SER   A CA     1 
ATOM   45    C  C      . SER   A 1  6   ? 32.982  -88.334  -55.056  1.00 60.90  ? 6   SER   A C      1 
ATOM   46    O  O      . SER   A 1  6   ? 33.151  -88.881  -53.955  1.00 58.27  ? 6   SER   A O      1 
ATOM   47    C  CB     . SER   A 1  6   ? 31.359  -89.847  -56.188  1.00 48.18  ? 6   SER   A CB     1 
ATOM   48    O  OG     . SER   A 1  6   ? 30.901  -90.326  -57.430  1.00 42.70  ? 6   SER   A OG     1 
ATOM   49    N  N      . ILE   A 1  7   ? 32.969  -87.008  -55.221  1.00 54.63  ? 7   ILE   A N      1 
ATOM   50    C  CA     . ILE   A 1  7   ? 33.187  -86.067  -54.128  1.00 52.11  ? 7   ILE   A CA     1 
ATOM   51    C  C      . ILE   A 1  7   ? 31.931  -85.219  -53.967  1.00 49.60  ? 7   ILE   A C      1 
ATOM   52    O  O      . ILE   A 1  7   ? 31.584  -84.432  -54.857  1.00 43.06  ? 7   ILE   A O      1 
ATOM   53    C  CB     . ILE   A 1  7   ? 34.413  -85.180  -54.383  1.00 56.14  ? 7   ILE   A CB     1 
ATOM   54    C  CG1    . ILE   A 1  7   ? 35.655  -86.041  -54.644  1.00 50.92  ? 7   ILE   A CG1    1 
ATOM   55    C  CG2    . ILE   A 1  7   ? 34.601  -84.189  -53.240  1.00 43.04  ? 7   ILE   A CG2    1 
ATOM   56    C  CD1    . ILE   A 1  7   ? 36.821  -85.256  -55.295  1.00 49.03  ? 7   ILE   A CD1    1 
ATOM   57    N  N      . HIS   A 1  8   ? 31.270  -85.353  -52.826  1.00 48.25  ? 8   HIS   A N      1 
ATOM   58    C  CA     . HIS   A 1  8   ? 30.047  -84.613  -52.543  1.00 46.74  ? 8   HIS   A CA     1 
ATOM   59    C  C      . HIS   A 1  8   ? 30.321  -83.523  -51.508  1.00 50.00  ? 8   HIS   A C      1 
ATOM   60    O  O      . HIS   A 1  8   ? 30.672  -83.835  -50.366  1.00 51.58  ? 8   HIS   A O      1 
ATOM   61    C  CB     . HIS   A 1  8   ? 28.974  -85.568  -52.041  1.00 47.50  ? 8   HIS   A CB     1 
ATOM   62    C  CG     . HIS   A 1  8   ? 28.882  -86.831  -52.832  1.00 56.05  ? 8   HIS   A CG     1 
ATOM   63    N  ND1    . HIS   A 1  8   ? 28.222  -86.902  -54.041  1.00 58.28  ? 8   HIS   A ND1    1 
ATOM   64    C  CD2    . HIS   A 1  8   ? 29.357  -88.076  -52.588  1.00 57.37  ? 8   HIS   A CD2    1 
ATOM   65    C  CE1    . HIS   A 1  8   ? 28.301  -88.134  -54.511  1.00 51.87  ? 8   HIS   A CE1    1 
ATOM   66    N  NE2    . HIS   A 1  8   ? 28.980  -88.867  -53.646  1.00 51.21  ? 8   HIS   A NE2    1 
ATOM   67    N  N      . VAL   A 1  9   ? 30.106  -82.257  -51.883  1.00 46.35  ? 9   VAL   A N      1 
ATOM   68    C  CA     . VAL   A 1  9   ? 30.522  -81.111  -51.076  1.00 43.23  ? 9   VAL   A CA     1 
ATOM   69    C  C      . VAL   A 1  9   ? 29.329  -80.243  -50.736  1.00 45.79  ? 9   VAL   A C      1 
ATOM   70    O  O      . VAL   A 1  9   ? 28.565  -79.854  -51.627  1.00 50.27  ? 9   VAL   A O      1 
ATOM   71    C  CB     . VAL   A 1  9   ? 31.567  -80.250  -51.794  1.00 45.09  ? 9   VAL   A CB     1 
ATOM   72    C  CG1    . VAL   A 1  9   ? 31.929  -79.087  -50.916  1.00 43.91  ? 9   VAL   A CG1    1 
ATOM   73    C  CG2    . VAL   A 1  9   ? 32.774  -81.090  -52.156  1.00 45.82  ? 9   VAL   A CG2    1 
ATOM   74    N  N      . GLY   A 1  10  ? 29.211  -79.885  -49.457  1.00 44.46  ? 10  GLY   A N      1 
ATOM   75    C  CA     . GLY   A 1  10  ? 28.149  -79.014  -49.015  1.00 40.77  ? 10  GLY   A CA     1 
ATOM   76    C  C      . GLY   A 1  10  ? 26.890  -79.789  -48.734  1.00 39.67  ? 10  GLY   A C      1 
ATOM   77    O  O      . GLY   A 1  10  ? 26.825  -80.999  -48.882  1.00 42.49  ? 10  GLY   A O      1 
ATOM   78    N  N      . GLN   A 1  11  ? 25.855  -79.067  -48.311  1.00 44.11  ? 11  GLN   A N      1 
ATOM   79    C  CA     . GLN   A 1  11  ? 24.565  -79.712  -48.097  1.00 43.52  ? 11  GLN   A CA     1 
ATOM   80    C  C      . GLN   A 1  11  ? 23.982  -80.239  -49.407  1.00 44.17  ? 11  GLN   A C      1 
ATOM   81    O  O      . GLN   A 1  11  ? 23.648  -81.427  -49.517  1.00 41.90  ? 11  GLN   A O      1 
ATOM   82    C  CB     . GLN   A 1  11  ? 23.589  -78.757  -47.429  1.00 40.06  ? 11  GLN   A CB     1 
ATOM   83    C  CG     . GLN   A 1  11  ? 22.331  -79.456  -47.033  1.00 42.50  ? 11  GLN   A CG     1 
ATOM   84    C  CD     . GLN   A 1  11  ? 21.330  -78.547  -46.402  1.00 43.14  ? 11  GLN   A CD     1 
ATOM   85    O  OE1    . GLN   A 1  11  ? 21.529  -78.075  -45.282  1.00 47.63  ? 11  GLN   A OE1    1 
ATOM   86    N  NE2    . GLN   A 1  11  ? 20.241  -78.276  -47.119  1.00 36.33  ? 11  GLN   A NE2    1 
ATOM   87    N  N      . ALA   A 1  12  ? 23.840  -79.370  -50.415  1.00 38.81  ? 12  ALA   A N      1 
ATOM   88    C  CA     . ALA   A 1  12  ? 23.310  -79.841  -51.696  1.00 38.42  ? 12  ALA   A CA     1 
ATOM   89    C  C      . ALA   A 1  12  ? 24.115  -81.026  -52.230  1.00 41.93  ? 12  ALA   A C      1 
ATOM   90    O  O      . ALA   A 1  12  ? 23.536  -82.021  -52.677  1.00 50.98  ? 12  ALA   A O      1 
ATOM   91    C  CB     . ALA   A 1  12  ? 23.264  -78.706  -52.723  1.00 30.93  ? 12  ALA   A CB     1 
ATOM   92    N  N      . GLY   A 1  13  ? 25.448  -80.957  -52.165  1.00 43.08  ? 13  GLY   A N      1 
ATOM   93    C  CA     . GLY   A 1  13  ? 26.266  -82.076  -52.631  1.00 44.08  ? 13  GLY   A CA     1 
ATOM   94    C  C      . GLY   A 1  13  ? 25.984  -83.379  -51.901  1.00 46.54  ? 13  GLY   A C      1 
ATOM   95    O  O      . GLY   A 1  13  ? 25.774  -84.420  -52.526  1.00 49.77  ? 13  GLY   A O      1 
ATOM   96    N  N      . VAL   A 1  14  ? 25.954  -83.334  -50.564  1.00 48.80  ? 14  VAL   A N      1 
ATOM   97    C  CA     . VAL   A 1  14  ? 25.835  -84.547  -49.754  1.00 46.43  ? 14  VAL   A CA     1 
ATOM   98    C  C      . VAL   A 1  14  ? 24.448  -85.164  -49.888  1.00 43.98  ? 14  VAL   A C      1 
ATOM   99    O  O      . VAL   A 1  14  ? 24.302  -86.385  -50.024  1.00 38.29  ? 14  VAL   A O      1 
ATOM   100   C  CB     . VAL   A 1  14  ? 26.176  -84.220  -48.288  1.00 39.85  ? 14  VAL   A CB     1 
ATOM   101   C  CG1    . VAL   A 1  14  ? 25.848  -85.391  -47.376  1.00 37.67  ? 14  VAL   A CG1    1 
ATOM   102   C  CG2    . VAL   A 1  14  ? 27.634  -83.845  -48.177  1.00 43.40  ? 14  VAL   A CG2    1 
ATOM   103   N  N      . GLN   A 1  15  ? 23.406  -84.341  -49.802  1.00 47.83  ? 15  GLN   A N      1 
ATOM   104   C  CA     . GLN   A 1  15  ? 22.058  -84.879  -49.892  1.00 45.66  ? 15  GLN   A CA     1 
ATOM   105   C  C      . GLN   A 1  15  ? 21.767  -85.453  -51.277  1.00 49.12  ? 15  GLN   A C      1 
ATOM   106   O  O      . GLN   A 1  15  ? 21.065  -86.470  -51.378  1.00 42.40  ? 15  GLN   A O      1 
ATOM   107   C  CB     . GLN   A 1  15  ? 21.051  -83.804  -49.501  1.00 41.03  ? 15  GLN   A CB     1 
ATOM   108   C  CG     . GLN   A 1  15  ? 20.797  -83.813  -48.015  1.00 53.46  ? 15  GLN   A CG     1 
ATOM   109   C  CD     . GLN   A 1  15  ? 19.972  -82.650  -47.512  1.00 53.31  ? 15  GLN   A CD     1 
ATOM   110   O  OE1    . GLN   A 1  15  ? 19.482  -81.822  -48.290  1.00 51.83  ? 15  GLN   A OE1    1 
ATOM   111   N  NE2    . GLN   A 1  15  ? 19.849  -82.558  -46.187  1.00 51.07  ? 15  GLN   A NE2    1 
ATOM   112   N  N      . ILE   A 1  16  ? 22.308  -84.835  -52.341  1.00 46.12  ? 16  ILE   A N      1 
ATOM   113   C  CA     . ILE   A 1  16  ? 22.192  -85.408  -53.681  1.00 44.70  ? 16  ILE   A CA     1 
ATOM   114   C  C      . ILE   A 1  16  ? 23.043  -86.673  -53.803  1.00 45.23  ? 16  ILE   A C      1 
ATOM   115   O  O      . ILE   A 1  16  ? 22.606  -87.669  -54.393  1.00 41.09  ? 16  ILE   A O      1 
ATOM   116   C  CB     . ILE   A 1  16  ? 22.557  -84.353  -54.742  1.00 42.04  ? 16  ILE   A CB     1 
ATOM   117   C  CG1    . ILE   A 1  16  ? 21.395  -83.365  -54.902  1.00 41.55  ? 16  ILE   A CG1    1 
ATOM   118   C  CG2    . ILE   A 1  16  ? 22.879  -85.006  -56.065  1.00 34.90  ? 16  ILE   A CG2    1 
ATOM   119   C  CD1    . ILE   A 1  16  ? 21.710  -82.142  -55.733  1.00 32.10  ? 16  ILE   A CD1    1 
ATOM   120   N  N      . GLY   A 1  17  ? 24.265  -86.661  -53.233  1.00 48.23  ? 17  GLY   A N      1 
ATOM   121   C  CA     . GLY   A 1  17  ? 25.087  -87.870  -53.191  1.00 42.74  ? 17  GLY   A CA     1 
ATOM   122   C  C      . GLY   A 1  17  ? 24.363  -89.057  -52.577  1.00 48.93  ? 17  GLY   A C      1 
ATOM   123   O  O      . GLY   A 1  17  ? 24.396  -90.169  -53.115  1.00 48.80  ? 17  GLY   A O      1 
ATOM   124   N  N      . ASN   A 1  18  ? 23.704  -88.837  -51.439  1.00 44.33  ? 18  ASN   A N      1 
ATOM   125   C  CA     . ASN   A 1  18  ? 22.853  -89.855  -50.843  1.00 43.45  ? 18  ASN   A CA     1 
ATOM   126   C  C      . ASN   A 1  18  ? 21.817  -90.350  -51.837  1.00 48.42  ? 18  ASN   A C      1 
ATOM   127   O  O      . ASN   A 1  18  ? 21.643  -91.557  -52.034  1.00 53.57  ? 18  ASN   A O      1 
ATOM   128   C  CB     . ASN   A 1  18  ? 22.153  -89.273  -49.619  1.00 47.00  ? 18  ASN   A CB     1 
ATOM   129   C  CG     . ASN   A 1  18  ? 22.895  -89.549  -48.341  1.00 56.74  ? 18  ASN   A CG     1 
ATOM   130   O  OD1    . ASN   A 1  18  ? 22.975  -90.698  -47.851  1.00 56.80  ? 18  ASN   A OD1    1 
ATOM   131   N  ND2    . ASN   A 1  18  ? 23.510  -88.505  -47.820  1.00 60.92  ? 18  ASN   A ND2    1 
ATOM   132   N  N      . ALA   A 1  19  ? 21.080  -89.426  -52.441  1.00 46.15  ? 19  ALA   A N      1 
ATOM   133   C  CA     . ALA   A 1  19  ? 20.080  -89.808  -53.416  1.00 45.01  ? 19  ALA   A CA     1 
ATOM   134   C  C      . ALA   A 1  19  ? 20.683  -90.725  -54.486  1.00 52.17  ? 19  ALA   A C      1 
ATOM   135   O  O      . ALA   A 1  19  ? 20.135  -91.788  -54.791  1.00 51.13  ? 19  ALA   A O      1 
ATOM   136   C  CB     . ALA   A 1  19  ? 19.477  -88.542  -54.028  1.00 47.04  ? 19  ALA   A CB     1 
ATOM   137   N  N      . CYS   A 1  20  ? 21.824  -90.331  -55.061  1.00 48.99  ? 20  CYS   A N      1 
ATOM   138   C  CA     . CYS   A 1  20  ? 22.444  -91.137  -56.107  1.00 49.74  ? 20  CYS   A CA     1 
ATOM   139   C  C      . CYS   A 1  20  ? 22.919  -92.479  -55.569  1.00 50.73  ? 20  CYS   A C      1 
ATOM   140   O  O      . CYS   A 1  20  ? 22.580  -93.535  -56.110  1.00 52.92  ? 20  CYS   A O      1 
ATOM   141   C  CB     . CYS   A 1  20  ? 23.611  -90.386  -56.729  1.00 42.61  ? 20  CYS   A CB     1 
ATOM   142   S  SG     . CYS   A 1  20  ? 23.056  -88.963  -57.573  1.00 49.86  ? 20  CYS   A SG     1 
ATOM   143   N  N      . TRP   A 1  21  ? 23.740  -92.461  -54.524  1.00 49.55  ? 21  TRP   A N      1 
ATOM   144   C  CA     . TRP   A 1  21  ? 24.314  -93.714  -54.064  1.00 47.51  ? 21  TRP   A CA     1 
ATOM   145   C  C      . TRP   A 1  21  ? 23.225  -94.713  -53.731  1.00 45.21  ? 21  TRP   A C      1 
ATOM   146   O  O      . TRP   A 1  21  ? 23.365  -95.904  -54.007  1.00 50.09  ? 21  TRP   A O      1 
ATOM   147   C  CB     . TRP   A 1  21  ? 25.247  -93.459  -52.882  1.00 48.86  ? 21  TRP   A CB     1 
ATOM   148   C  CG     . TRP   A 1  21  ? 26.500  -92.966  -53.419  1.00 49.14  ? 21  TRP   A CG     1 
ATOM   149   C  CD1    . TRP   A 1  21  ? 26.940  -91.687  -53.415  1.00 49.93  ? 21  TRP   A CD1    1 
ATOM   150   C  CD2    . TRP   A 1  21  ? 27.450  -93.722  -54.173  1.00 53.85  ? 21  TRP   A CD2    1 
ATOM   151   N  NE1    . TRP   A 1  21  ? 28.140  -91.595  -54.080  1.00 50.10  ? 21  TRP   A NE1    1 
ATOM   152   C  CE2    . TRP   A 1  21  ? 28.477  -92.831  -54.560  1.00 50.87  ? 21  TRP   A CE2    1 
ATOM   153   C  CE3    . TRP   A 1  21  ? 27.549  -95.071  -54.533  1.00 50.98  ? 21  TRP   A CE3    1 
ATOM   154   C  CZ2    . TRP   A 1  21  ? 29.595  -93.240  -55.284  1.00 45.31  ? 21  TRP   A CZ2    1 
ATOM   155   C  CZ3    . TRP   A 1  21  ? 28.659  -95.475  -55.256  1.00 54.68  ? 21  TRP   A CZ3    1 
ATOM   156   C  CH2    . TRP   A 1  21  ? 29.667  -94.558  -55.627  1.00 49.47  ? 21  TRP   A CH2    1 
ATOM   157   N  N      . GLU   A 1  22  ? 22.116  -94.246  -53.173  1.00 46.23  ? 22  GLU   A N      1 
ATOM   158   C  CA     . GLU   A 1  22  ? 21.014  -95.154  -52.911  1.00 50.85  ? 22  GLU   A CA     1 
ATOM   159   C  C      . GLU   A 1  22  ? 20.449  -95.705  -54.213  1.00 54.78  ? 22  GLU   A C      1 
ATOM   160   O  O      . GLU   A 1  22  ? 20.113  -96.893  -54.295  1.00 55.69  ? 22  GLU   A O      1 
ATOM   161   C  CB     . GLU   A 1  22  ? 19.928  -94.445  -52.118  1.00 49.74  ? 22  GLU   A CB     1 
ATOM   162   C  CG     . GLU   A 1  22  ? 18.587  -95.100  -52.290  1.00 54.53  ? 22  GLU   A CG     1 
ATOM   163   C  CD     . GLU   A 1  22  ? 17.446  -94.164  -52.004  1.00 66.01  ? 22  GLU   A CD     1 
ATOM   164   O  OE1    . GLU   A 1  22  ? 17.477  -92.997  -52.480  1.00 63.66  ? 22  GLU   A OE1    1 
ATOM   165   O  OE2    . GLU   A 1  22  ? 16.508  -94.602  -51.302  1.00 72.79  ? 22  GLU   A OE2    1 
ATOM   166   N  N      . LEU   A 1  23  ? 20.347  -94.854  -55.243  1.00 49.67  ? 23  LEU   A N      1 
ATOM   167   C  CA     . LEU   A 1  23  ? 19.864  -95.295  -56.549  1.00 51.82  ? 23  LEU   A CA     1 
ATOM   168   C  C      . LEU   A 1  23  ? 20.819  -96.312  -57.171  1.00 52.06  ? 23  LEU   A C      1 
ATOM   169   O  O      . LEU   A 1  23  ? 20.410  -97.426  -57.515  1.00 50.57  ? 23  LEU   A O      1 
ATOM   170   C  CB     . LEU   A 1  23  ? 19.660  -94.092  -57.472  1.00 44.21  ? 23  LEU   A CB     1 
ATOM   171   C  CG     . LEU   A 1  23  ? 18.903  -94.361  -58.773  1.00 47.40  ? 23  LEU   A CG     1 
ATOM   172   C  CD1    . LEU   A 1  23  ? 17.580  -95.082  -58.522  1.00 50.20  ? 23  LEU   A CD1    1 
ATOM   173   C  CD2    . LEU   A 1  23  ? 18.652  -93.066  -59.494  1.00 47.32  ? 23  LEU   A CD2    1 
ATOM   174   N  N      . TYR   A 1  24  ? 22.098  -95.953  -57.313  1.00 51.00  ? 24  TYR   A N      1 
ATOM   175   C  CA     . TYR   A 1  24  ? 23.120  -96.925  -57.690  1.00 52.45  ? 24  TYR   A CA     1 
ATOM   176   C  C      . TYR   A 1  24  ? 22.901  -98.286  -57.022  1.00 57.07  ? 24  TYR   A C      1 
ATOM   177   O  O      . TYR   A 1  24  ? 22.762  -99.309  -57.700  1.00 55.97  ? 24  TYR   A O      1 
ATOM   178   C  CB     . TYR   A 1  24  ? 24.506  -96.383  -57.343  1.00 45.01  ? 24  TYR   A CB     1 
ATOM   179   C  CG     . TYR   A 1  24  ? 24.872  -95.126  -58.092  1.00 50.48  ? 24  TYR   A CG     1 
ATOM   180   C  CD1    . TYR   A 1  24  ? 24.046  -94.610  -59.079  1.00 50.19  ? 24  TYR   A CD1    1 
ATOM   181   C  CD2    . TYR   A 1  24  ? 26.048  -94.447  -57.810  1.00 52.17  ? 24  TYR   A CD2    1 
ATOM   182   C  CE1    . TYR   A 1  24  ? 24.393  -93.452  -59.781  1.00 50.80  ? 24  TYR   A CE1    1 
ATOM   183   C  CE2    . TYR   A 1  24  ? 26.393  -93.284  -58.498  1.00 52.32  ? 24  TYR   A CE2    1 
ATOM   184   C  CZ     . TYR   A 1  24  ? 25.568  -92.796  -59.477  1.00 48.69  ? 24  TYR   A CZ     1 
ATOM   185   O  OH     . TYR   A 1  24  ? 25.920  -91.647  -60.139  1.00 42.59  ? 24  TYR   A OH     1 
ATOM   186   N  N      . CYS   A 1  25  ? 22.853  -98.315  -55.686  1.00 58.00  ? 25  CYS   A N      1 
ATOM   187   C  CA     . CYS   A 1  25  ? 22.692  -99.584  -54.980  1.00 54.15  ? 25  CYS   A CA     1 
ATOM   188   C  C      . CYS   A 1  25  ? 21.459  -100.334 -55.466  1.00 55.02  ? 25  CYS   A C      1 
ATOM   189   O  O      . CYS   A 1  25  ? 21.503  -101.553 -55.659  1.00 60.06  ? 25  CYS   A O      1 
ATOM   190   C  CB     . CYS   A 1  25  ? 22.626  -99.352  -53.468  1.00 50.15  ? 25  CYS   A CB     1 
ATOM   191   S  SG     . CYS   A 1  25  ? 24.226  -98.865  -52.702  1.00 57.79  ? 25  CYS   A SG     1 
ATOM   192   N  N      . LEU   A 1  26  ? 20.349  -99.634  -55.679  1.00 54.23  ? 26  LEU   A N      1 
ATOM   193   C  CA     . LEU   A 1  26  ? 19.165  -100.309 -56.205  1.00 58.49  ? 26  LEU   A CA     1 
ATOM   194   C  C      . LEU   A 1  26  ? 19.436  -100.897 -57.584  1.00 56.45  ? 26  LEU   A C      1 
ATOM   195   O  O      . LEU   A 1  26  ? 19.099  -102.054 -57.855  1.00 59.87  ? 26  LEU   A O      1 
ATOM   196   C  CB     . LEU   A 1  26  ? 17.983  -99.342  -56.257  1.00 53.78  ? 26  LEU   A CB     1 
ATOM   197   C  CG     . LEU   A 1  26  ? 17.437  -99.206  -54.845  1.00 53.26  ? 26  LEU   A CG     1 
ATOM   198   C  CD1    . LEU   A 1  26  ? 16.044  -98.619  -54.832  1.00 56.58  ? 26  LEU   A CD1    1 
ATOM   199   C  CD2    . LEU   A 1  26  ? 17.459  -100.582 -54.228  1.00 40.75  ? 26  LEU   A CD2    1 
ATOM   200   N  N      . GLU   A 1  27  ? 20.081  -100.119 -58.455  1.00 53.08  ? 27  GLU   A N      1 
ATOM   201   C  CA     . GLU   A 1  27  ? 20.275  -100.535 -59.836  1.00 57.12  ? 27  GLU   A CA     1 
ATOM   202   C  C      . GLU   A 1  27  ? 21.275  -101.682 -59.940  1.00 60.23  ? 27  GLU   A C      1 
ATOM   203   O  O      . GLU   A 1  27  ? 21.106  -102.581 -60.773  1.00 63.68  ? 27  GLU   A O      1 
ATOM   204   C  CB     . GLU   A 1  27  ? 20.716  -99.334  -60.686  1.00 52.60  ? 27  GLU   A CB     1 
ATOM   205   C  CG     . GLU   A 1  27  ? 19.613  -98.300  -60.875  1.00 54.57  ? 27  GLU   A CG     1 
ATOM   206   C  CD     . GLU   A 1  27  ? 20.045  -97.051  -61.644  1.00 54.41  ? 27  GLU   A CD     1 
ATOM   207   O  OE1    . GLU   A 1  27  ? 21.224  -96.980  -62.048  1.00 47.34  ? 27  GLU   A OE1    1 
ATOM   208   O  OE2    . GLU   A 1  27  ? 19.186  -96.146  -61.843  1.00 52.90  ? 27  GLU   A OE2    1 
ATOM   209   N  N      . HIS   A 1  28  ? 22.322  -101.664 -59.113  1.00 55.18  ? 28  HIS   A N      1 
ATOM   210   C  CA     . HIS   A 1  28  ? 23.351  -102.696 -59.098  1.00 55.21  ? 28  HIS   A CA     1 
ATOM   211   C  C      . HIS   A 1  28  ? 23.037  -103.856 -58.150  1.00 59.34  ? 28  HIS   A C      1 
ATOM   212   O  O      . HIS   A 1  28  ? 23.855  -104.776 -58.031  1.00 55.34  ? 28  HIS   A O      1 
ATOM   213   C  CB     . HIS   A 1  28  ? 24.705  -102.099 -58.708  1.00 57.18  ? 28  HIS   A CB     1 
ATOM   214   C  CG     . HIS   A 1  28  ? 25.271  -101.136 -59.703  1.00 57.69  ? 28  HIS   A CG     1 
ATOM   215   N  ND1    . HIS   A 1  28  ? 25.940  -101.544 -60.836  1.00 56.11  ? 28  HIS   A ND1    1 
ATOM   216   C  CD2    . HIS   A 1  28  ? 25.317  -99.781  -59.707  1.00 57.93  ? 28  HIS   A CD2    1 
ATOM   217   C  CE1    . HIS   A 1  28  ? 26.349  -100.482 -61.510  1.00 55.42  ? 28  HIS   A CE1    1 
ATOM   218   N  NE2    . HIS   A 1  28  ? 25.988  -99.400  -60.844  1.00 56.19  ? 28  HIS   A NE2    1 
ATOM   219   N  N      . GLY   A 1  29  ? 21.890  -103.838 -57.471  1.00 56.49  ? 29  GLY   A N      1 
ATOM   220   C  CA     . GLY   A 1  29  ? 21.522  -104.934 -56.602  1.00 55.60  ? 29  GLY   A CA     1 
ATOM   221   C  C      . GLY   A 1  29  ? 22.289  -105.021 -55.304  1.00 56.43  ? 29  GLY   A C      1 
ATOM   222   O  O      . GLY   A 1  29  ? 22.061  -105.963 -54.540  1.00 60.53  ? 29  GLY   A O      1 
ATOM   223   N  N      . ILE   A 1  30  ? 23.189  -104.070 -55.036  1.00 62.93  ? 30  ILE   A N      1 
ATOM   224   C  CA     . ILE   A 1  30  ? 23.847  -103.933 -53.738  1.00 58.98  ? 30  ILE   A CA     1 
ATOM   225   C  C      . ILE   A 1  30  ? 22.841  -103.559 -52.649  1.00 64.52  ? 30  ILE   A C      1 
ATOM   226   O  O      . ILE   A 1  30  ? 21.878  -102.812 -52.882  1.00 63.42  ? 30  ILE   A O      1 
ATOM   227   C  CB     . ILE   A 1  30  ? 24.956  -102.877 -53.862  1.00 55.86  ? 30  ILE   A CB     1 
ATOM   228   C  CG1    . ILE   A 1  30  ? 25.632  -103.007 -55.232  1.00 58.11  ? 30  ILE   A CG1    1 
ATOM   229   C  CG2    . ILE   A 1  30  ? 25.938  -102.972 -52.718  1.00 64.57  ? 30  ILE   A CG2    1 
ATOM   230   C  CD1    . ILE   A 1  30  ? 26.819  -102.096 -55.401  1.00 63.60  ? 30  ILE   A CD1    1 
ATOM   231   N  N      . GLN   A 1  31  ? 23.071  -104.065 -51.441  1.00 70.41  ? 31  GLN   A N      1 
ATOM   232   C  CA     . GLN   A 1  31  ? 22.170  -103.866 -50.312  1.00 71.97  ? 31  GLN   A CA     1 
ATOM   233   C  C      . GLN   A 1  31  ? 22.695  -102.785 -49.380  1.00 68.30  ? 31  GLN   A C      1 
ATOM   234   O  O      . GLN   A 1  31  ? 23.821  -102.304 -49.528  1.00 67.59  ? 31  GLN   A O      1 
ATOM   235   C  CB     . GLN   A 1  31  ? 21.986  -105.181 -49.555  1.00 71.32  ? 31  GLN   A CB     1 
ATOM   236   C  CG     . GLN   A 1  31  ? 21.765  -106.343 -50.482  1.00 70.43  ? 31  GLN   A CG     1 
ATOM   237   C  CD     . GLN   A 1  31  ? 21.154  -107.523 -49.789  1.00 78.51  ? 31  GLN   A CD     1 
ATOM   238   O  OE1    . GLN   A 1  31  ? 21.855  -108.320 -49.152  1.00 75.43  ? 31  GLN   A OE1    1 
ATOM   239   N  NE2    . GLN   A 1  31  ? 19.833  -107.651 -49.904  1.00 83.41  ? 31  GLN   A NE2    1 
ATOM   240   N  N      . PRO   A 1  32  ? 21.881  -102.363 -48.408  1.00 67.45  ? 32  PRO   A N      1 
ATOM   241   C  CA     . PRO   A 1  32  ? 22.315  -101.318 -47.460  1.00 66.14  ? 32  PRO   A CA     1 
ATOM   242   C  C      . PRO   A 1  32  ? 23.558  -101.650 -46.640  1.00 69.57  ? 32  PRO   A C      1 
ATOM   243   O  O      . PRO   A 1  32  ? 24.100  -100.739 -45.999  1.00 70.82  ? 32  PRO   A O      1 
ATOM   244   C  CB     . PRO   A 1  32  ? 21.095  -101.148 -46.554  1.00 59.59  ? 32  PRO   A CB     1 
ATOM   245   C  CG     . PRO   A 1  32  ? 19.950  -101.469 -47.452  1.00 63.00  ? 32  PRO   A CG     1 
ATOM   246   C  CD     . PRO   A 1  32  ? 20.425  -102.573 -48.370  1.00 63.10  ? 32  PRO   A CD     1 
ATOM   247   N  N      . ASP   A 1  33  ? 24.015  -102.900 -46.613  1.00 70.74  ? 33  ASP   A N      1 
ATOM   248   C  CA     . ASP   A 1  33  ? 25.255  -103.250 -45.929  1.00 69.46  ? 33  ASP   A CA     1 
ATOM   249   C  C      . ASP   A 1  33  ? 26.407  -103.500 -46.887  1.00 68.91  ? 33  ASP   A C      1 
ATOM   250   O  O      . ASP   A 1  33  ? 27.491  -103.891 -46.444  1.00 69.08  ? 33  ASP   A O      1 
ATOM   251   C  CB     . ASP   A 1  33  ? 25.051  -104.480 -45.043  1.00 69.90  ? 33  ASP   A CB     1 
ATOM   252   C  CG     . ASP   A 1  33  ? 24.292  -105.584 -45.742  1.00 73.81  ? 33  ASP   A CG     1 
ATOM   253   O  OD1    . ASP   A 1  33  ? 24.682  -105.959 -46.865  1.00 76.01  ? 33  ASP   A OD1    1 
ATOM   254   O  OD2    . ASP   A 1  33  ? 23.280  -106.051 -45.177  1.00 76.58  ? 33  ASP   A OD2    1 
ATOM   255   N  N      . GLY   A 1  34  ? 26.198  -103.293 -48.182  1.00 70.65  ? 34  GLY   A N      1 
ATOM   256   C  CA     . GLY   A 1  34  ? 27.255  -103.453 -49.150  1.00 68.41  ? 34  GLY   A CA     1 
ATOM   257   C  C      . GLY   A 1  34  ? 27.502  -104.870 -49.595  1.00 67.01  ? 34  GLY   A C      1 
ATOM   258   O  O      . GLY   A 1  34  ? 28.542  -105.132 -50.212  1.00 67.14  ? 34  GLY   A O      1 
ATOM   259   N  N      . GLN   A 1  35  ? 26.594  -105.796 -49.289  1.00 68.87  ? 35  GLN   A N      1 
ATOM   260   C  CA     . GLN   A 1  35  ? 26.664  -107.159 -49.806  1.00 72.68  ? 35  GLN   A CA     1 
ATOM   261   C  C      . GLN   A 1  35  ? 25.935  -107.202 -51.138  1.00 70.88  ? 35  GLN   A C      1 
ATOM   262   O  O      . GLN   A 1  35  ? 24.757  -106.833 -51.209  1.00 70.94  ? 35  GLN   A O      1 
ATOM   263   C  CB     . GLN   A 1  35  ? 26.046  -108.171 -48.839  1.00 64.44  ? 35  GLN   A CB     1 
ATOM   264   C  CG     . GLN   A 1  35  ? 26.978  -108.561 -47.702  1.00 65.65  ? 35  GLN   A CG     1 
ATOM   265   C  CD     . GLN   A 1  35  ? 28.224  -109.292 -48.173  1.00 70.09  ? 35  GLN   A CD     1 
ATOM   266   O  OE1    . GLN   A 1  35  ? 29.345  -108.794 -48.026  1.00 68.44  ? 35  GLN   A OE1    1 
ATOM   267   N  NE2    . GLN   A 1  35  ? 28.038  -110.499 -48.713  1.00 70.68  ? 35  GLN   A NE2    1 
ATOM   268   N  N      . MET   A 1  36  ? 26.636  -107.644 -52.188  1.00 68.09  ? 36  MET   A N      1 
ATOM   269   C  CA     . MET   A 1  36  ? 26.068  -107.794 -53.527  1.00 68.14  ? 36  MET   A CA     1 
ATOM   270   C  C      . MET   A 1  36  ? 25.905  -109.263 -53.894  1.00 66.84  ? 36  MET   A C      1 
ATOM   271   O  O      . MET   A 1  36  ? 26.770  -109.828 -54.584  1.00 65.18  ? 36  MET   A O      1 
ATOM   272   C  CB     . MET   A 1  36  ? 26.947  -107.099 -54.564  1.00 68.86  ? 36  MET   A CB     1 
ATOM   273   C  CG     . MET   A 1  36  ? 26.221  -106.747 -55.847  1.00 63.93  ? 36  MET   A CG     1 
ATOM   274   S  SD     . MET   A 1  36  ? 27.418  -105.928 -56.886  1.00 70.48  ? 36  MET   A SD     1 
ATOM   275   C  CE     . MET   A 1  36  ? 26.521  -105.816 -58.420  1.00 67.60  ? 36  MET   A CE     1 
ATOM   276   N  N      . PRO   A 1  37  ? 24.793  -109.917 -53.499  1.00 64.74  ? 37  PRO   A N      1 
ATOM   277   C  CA     . PRO   A 1  37  ? 24.580  -111.326 -53.868  1.00 67.42  ? 37  PRO   A CA     1 
ATOM   278   C  C      . PRO   A 1  37  ? 25.067  -111.684 -55.267  1.00 72.57  ? 37  PRO   A C      1 
ATOM   279   O  O      . PRO   A 1  37  ? 25.787  -112.673 -55.444  1.00 74.86  ? 37  PRO   A O      1 
ATOM   280   C  CB     . PRO   A 1  37  ? 23.058  -111.478 -53.762  1.00 69.15  ? 37  PRO   A CB     1 
ATOM   281   C  CG     . PRO   A 1  37  ? 22.651  -110.486 -52.731  1.00 62.65  ? 37  PRO   A CG     1 
ATOM   282   C  CD     . PRO   A 1  37  ? 23.615  -109.337 -52.824  1.00 63.14  ? 37  PRO   A CD     1 
ATOM   283   N  N      . SER   A 1  38  ? 24.704  -110.871 -56.265  1.00 75.80  ? 38  SER   A N      1 
ATOM   284   C  CA     . SER   A 1  38  ? 25.021  -111.197 -57.653  1.00 73.53  ? 38  SER   A CA     1 
ATOM   285   C  C      . SER   A 1  38  ? 26.517  -111.168 -57.959  1.00 71.55  ? 38  SER   A C      1 
ATOM   286   O  O      . SER   A 1  38  ? 26.925  -111.787 -58.948  1.00 72.00  ? 38  SER   A O      1 
ATOM   287   C  CB     . SER   A 1  38  ? 24.302  -110.245 -58.620  1.00 70.19  ? 38  SER   A CB     1 
ATOM   288   O  OG     . SER   A 1  38  ? 24.330  -108.906 -58.159  1.00 65.09  ? 38  SER   A OG     1 
ATOM   289   N  N      . ASP   A 1  39  ? 27.345  -110.448 -57.180  1.00 72.29  ? 39  ASP   A N      1 
ATOM   290   C  CA     . ASP   A 1  39  ? 28.786  -110.486 -57.440  1.00 69.91  ? 39  ASP   A CA     1 
ATOM   291   C  C      . ASP   A 1  39  ? 29.326  -111.828 -56.989  1.00 74.78  ? 39  ASP   A C      1 
ATOM   292   O  O      . ASP   A 1  39  ? 29.139  -112.229 -55.832  1.00 74.77  ? 39  ASP   A O      1 
ATOM   293   C  CB     . ASP   A 1  39  ? 29.568  -109.367 -56.747  1.00 66.71  ? 39  ASP   A CB     1 
ATOM   294   C  CG     . ASP   A 1  39  ? 31.080  -109.383 -57.122  1.00 70.66  ? 39  ASP   A CG     1 
ATOM   295   O  OD1    . ASP   A 1  39  ? 31.571  -110.369 -57.705  1.00 67.39  ? 39  ASP   A OD1    1 
ATOM   296   O  OD2    . ASP   A 1  39  ? 31.800  -108.408 -56.848  1.00 68.97  ? 39  ASP   A OD2    1 
ATOM   297   N  N      . LYS   A 1  40  ? 29.983  -112.522 -57.914  1.00 72.88  ? 40  LYS   A N      1 
ATOM   298   C  CA     . LYS   A 1  40  ? 30.637  -113.781 -57.618  1.00 68.61  ? 40  LYS   A CA     1 
ATOM   299   C  C      . LYS   A 1  40  ? 32.148  -113.660 -57.546  1.00 68.09  ? 40  LYS   A C      1 
ATOM   300   O  O      . LYS   A 1  40  ? 32.778  -114.494 -56.892  1.00 68.55  ? 40  LYS   A O      1 
ATOM   301   C  CB     . LYS   A 1  40  ? 30.257  -114.828 -58.665  1.00 67.11  ? 40  LYS   A CB     1 
ATOM   302   C  CG     . LYS   A 1  40  ? 28.799  -114.776 -59.092  1.00 59.25  ? 40  LYS   A CG     1 
ATOM   303   C  CD     . LYS   A 1  40  ? 27.889  -115.178 -57.971  1.00 67.08  ? 40  LYS   A CD     1 
ATOM   304   C  CE     . LYS   A 1  40  ? 26.493  -115.421 -58.500  1.00 69.06  ? 40  LYS   A CE     1 
ATOM   305   N  NZ     . LYS   A 1  40  ? 25.585  -115.956 -57.460  1.00 65.24  ? 40  LYS   A NZ     1 
ATOM   306   N  N      . THR   A 1  41  ? 32.741  -112.647 -58.187  1.00 69.72  ? 41  THR   A N      1 
ATOM   307   C  CA     . THR   A 1  41  ? 34.133  -112.301 -57.916  1.00 73.96  ? 41  THR   A CA     1 
ATOM   308   C  C      . THR   A 1  41  ? 34.183  -111.614 -56.556  1.00 73.45  ? 41  THR   A C      1 
ATOM   309   O  O      . THR   A 1  41  ? 34.089  -110.380 -56.468  1.00 73.79  ? 41  THR   A O      1 
ATOM   310   C  CB     . THR   A 1  41  ? 34.733  -111.395 -59.003  1.00 76.11  ? 41  THR   A CB     1 
ATOM   311   O  OG1    . THR   A 1  41  ? 33.733  -111.058 -59.980  1.00 74.93  ? 41  THR   A OG1    1 
ATOM   312   C  CG2    . THR   A 1  41  ? 35.923  -112.082 -59.680  1.00 63.88  ? 41  THR   A CG2    1 
ATOM   313   N  N      . ILE   A 1  42  ? 34.313  -112.428 -55.504  1.00 66.41  ? 42  ILE   A N      1 
ATOM   314   C  CA     . ILE   A 1  42  ? 34.202  -111.983 -54.119  1.00 66.11  ? 42  ILE   A CA     1 
ATOM   315   C  C      . ILE   A 1  42  ? 35.504  -111.333 -53.678  1.00 66.64  ? 42  ILE   A C      1 
ATOM   316   O  O      . ILE   A 1  42  ? 36.590  -111.889 -53.873  1.00 66.71  ? 42  ILE   A O      1 
ATOM   317   C  CB     . ILE   A 1  42  ? 33.845  -113.164 -53.207  1.00 58.99  ? 42  ILE   A CB     1 
ATOM   318   C  CG1    . ILE   A 1  42  ? 32.399  -113.600 -53.456  1.00 58.20  ? 42  ILE   A CG1    1 
ATOM   319   C  CG2    . ILE   A 1  42  ? 34.103  -112.803 -51.776  1.00 55.87  ? 42  ILE   A CG2    1 
ATOM   320   C  CD1    . ILE   A 1  42  ? 31.822  -114.493 -52.386  1.00 48.32  ? 42  ILE   A CD1    1 
ATOM   321   N  N      . GLY   A 1  43  ? 35.398  -110.160 -53.061  1.00 69.15  ? 43  GLY   A N      1 
ATOM   322   C  CA     . GLY   A 1  43  ? 36.593  -109.419 -52.715  1.00 68.63  ? 43  GLY   A CA     1 
ATOM   323   C  C      . GLY   A 1  43  ? 37.360  -108.867 -53.895  1.00 69.88  ? 43  GLY   A C      1 
ATOM   324   O  O      . GLY   A 1  43  ? 38.541  -108.543 -53.748  1.00 64.78  ? 43  GLY   A O      1 
ATOM   325   N  N      . GLY   A 1  44  ? 36.735  -108.759 -55.067  1.00 75.99  ? 44  GLY   A N      1 
ATOM   326   C  CA     . GLY   A 1  44  ? 37.412  -108.156 -56.201  1.00 77.79  ? 44  GLY   A CA     1 
ATOM   327   C  C      . GLY   A 1  44  ? 36.657  -108.325 -57.504  1.00 71.01  ? 44  GLY   A C      1 
ATOM   328   O  O      . GLY   A 1  44  ? 35.549  -108.871 -57.561  1.00 69.01  ? 44  GLY   A O      1 
ATOM   329   N  N      . GLY   A 1  45  ? 37.298  -107.842 -58.552  1.00 66.73  ? 45  GLY   A N      1 
ATOM   330   C  CA     . GLY   A 1  45  ? 36.760  -107.874 -59.900  1.00 74.69  ? 45  GLY   A CA     1 
ATOM   331   C  C      . GLY   A 1  45  ? 37.174  -106.587 -60.595  1.00 80.44  ? 45  GLY   A C      1 
ATOM   332   O  O      . GLY   A 1  45  ? 37.432  -105.558 -59.964  1.00 77.56  ? 45  GLY   A O      1 
ATOM   333   N  N      . ASP   A 1  46  ? 37.290  -106.652 -61.927  1.00 77.90  ? 46  ASP   A N      1 
ATOM   334   C  CA     . ASP   A 1  46  ? 37.332  -105.416 -62.703  1.00 75.66  ? 46  ASP   A CA     1 
ATOM   335   C  C      . ASP   A 1  46  ? 36.104  -105.382 -63.611  1.00 74.46  ? 46  ASP   A C      1 
ATOM   336   O  O      . ASP   A 1  46  ? 36.206  -105.146 -64.823  1.00 72.88  ? 46  ASP   A O      1 
ATOM   337   C  CB     . ASP   A 1  46  ? 38.656  -105.248 -63.478  1.00 73.27  ? 46  ASP   A CB     1 
ATOM   338   C  CG     . ASP   A 1  46  ? 38.886  -106.320 -64.516  1.00 77.22  ? 46  ASP   A CG     1 
ATOM   339   O  OD1    . ASP   A 1  46  ? 39.774  -106.126 -65.381  1.00 78.50  ? 46  ASP   A OD1    1 
ATOM   340   O  OD2    . ASP   A 1  46  ? 38.185  -107.353 -64.468  1.00 85.63  ? 46  ASP   A OD2    1 
ATOM   341   N  N      . ASP   A 1  47  ? 34.938  -105.626 -63.003  1.00 70.28  ? 47  ASP   A N      1 
ATOM   342   C  CA     . ASP   A 1  47  ? 33.634  -105.421 -63.621  1.00 68.68  ? 47  ASP   A CA     1 
ATOM   343   C  C      . ASP   A 1  47  ? 33.372  -103.929 -63.849  1.00 70.24  ? 47  ASP   A C      1 
ATOM   344   O  O      . ASP   A 1  47  ? 34.188  -103.052 -63.526  1.00 70.60  ? 47  ASP   A O      1 
ATOM   345   C  CB     . ASP   A 1  47  ? 32.540  -106.045 -62.758  1.00 63.13  ? 47  ASP   A CB     1 
ATOM   346   C  CG     . ASP   A 1  47  ? 32.668  -107.545 -62.684  1.00 68.95  ? 47  ASP   A CG     1 
ATOM   347   O  OD1    . ASP   A 1  47  ? 33.327  -108.100 -63.585  1.00 73.42  ? 47  ASP   A OD1    1 
ATOM   348   O  OD2    . ASP   A 1  47  ? 32.150  -108.165 -61.734  1.00 68.49  ? 47  ASP   A OD2    1 
ATOM   349   N  N      . SER   A 1  48  ? 32.219  -103.630 -64.437  1.00 67.66  ? 48  SER   A N      1 
ATOM   350   C  CA     . SER   A 1  48  ? 31.957  -102.235 -64.758  1.00 69.34  ? 48  SER   A CA     1 
ATOM   351   C  C      . SER   A 1  48  ? 31.441  -101.471 -63.541  1.00 67.44  ? 48  SER   A C      1 
ATOM   352   O  O      . SER   A 1  48  ? 31.780  -100.296 -63.353  1.00 61.60  ? 48  SER   A O      1 
ATOM   353   C  CB     . SER   A 1  48  ? 30.990  -102.135 -65.934  1.00 61.26  ? 48  SER   A CB     1 
ATOM   354   O  OG     . SER   A 1  48  ? 31.605  -101.394 -66.964  1.00 57.16  ? 48  SER   A OG     1 
ATOM   355   N  N      . PHE   A 1  49  ? 30.652  -102.121 -62.686  1.00 63.18  ? 49  PHE   A N      1 
ATOM   356   C  CA     . PHE   A 1  49  ? 30.270  -101.455 -61.454  1.00 62.20  ? 49  PHE   A CA     1 
ATOM   357   C  C      . PHE   A 1  49  ? 31.477  -101.176 -60.565  1.00 64.55  ? 49  PHE   A C      1 
ATOM   358   O  O      . PHE   A 1  49  ? 31.442  -100.230 -59.770  1.00 63.19  ? 49  PHE   A O      1 
ATOM   359   C  CB     . PHE   A 1  49  ? 29.195  -102.269 -60.728  1.00 62.95  ? 49  PHE   A CB     1 
ATOM   360   C  CG     . PHE   A 1  49  ? 29.689  -103.529 -60.060  1.00 71.36  ? 49  PHE   A CG     1 
ATOM   361   C  CD1    . PHE   A 1  49  ? 30.279  -103.484 -58.801  1.00 72.68  ? 49  PHE   A CD1    1 
ATOM   362   C  CD2    . PHE   A 1  49  ? 29.493  -104.772 -60.655  1.00 67.65  ? 49  PHE   A CD2    1 
ATOM   363   C  CE1    . PHE   A 1  49  ? 30.700  -104.650 -58.164  1.00 74.76  ? 49  PHE   A CE1    1 
ATOM   364   C  CE2    . PHE   A 1  49  ? 29.910  -105.941 -60.019  1.00 70.63  ? 49  PHE   A CE2    1 
ATOM   365   C  CZ     . PHE   A 1  49  ? 30.517  -105.877 -58.774  1.00 73.31  ? 49  PHE   A CZ     1 
ATOM   366   N  N      . ASN   A 1  50  ? 32.565  -101.931 -60.719  1.00 67.79  ? 50  ASN   A N      1 
ATOM   367   C  CA     . ASN   A 1  50  ? 33.737  -101.730 -59.875  1.00 64.95  ? 50  ASN   A CA     1 
ATOM   368   C  C      . ASN   A 1  50  ? 34.389  -100.378 -60.127  1.00 60.77  ? 50  ASN   A C      1 
ATOM   369   O  O      . ASN   A 1  50  ? 35.346  -100.017 -59.439  1.00 63.37  ? 50  ASN   A O      1 
ATOM   370   C  CB     . ASN   A 1  50  ? 34.744  -102.861 -60.077  1.00 60.46  ? 50  ASN   A CB     1 
ATOM   371   C  CG     . ASN   A 1  50  ? 34.291  -104.133 -59.442  1.00 69.04  ? 50  ASN   A CG     1 
ATOM   372   O  OD1    . ASN   A 1  50  ? 34.461  -105.214 -59.998  1.00 74.17  ? 50  ASN   A OD1    1 
ATOM   373   N  ND2    . ASN   A 1  50  ? 33.679  -104.017 -58.267  1.00 72.16  ? 50  ASN   A ND2    1 
ATOM   374   N  N      . THR   A 1  51  ? 33.900  -99.624  -61.115  1.00 61.78  ? 51  THR   A N      1 
ATOM   375   C  CA     . THR   A 1  51  ? 34.382  -98.256  -61.290  1.00 64.15  ? 51  THR   A CA     1 
ATOM   376   C  C      . THR   A 1  51  ? 33.836  -97.321  -60.219  1.00 61.96  ? 51  THR   A C      1 
ATOM   377   O  O      . THR   A 1  51  ? 34.435  -96.270  -59.954  1.00 61.66  ? 51  THR   A O      1 
ATOM   378   C  CB     . THR   A 1  51  ? 34.006  -97.698  -62.670  1.00 62.11  ? 51  THR   A CB     1 
ATOM   379   O  OG1    . THR   A 1  51  ? 32.600  -97.821  -62.861  1.00 62.73  ? 51  THR   A OG1    1 
ATOM   380   C  CG2    . THR   A 1  51  ? 34.723  -98.440  -63.798  1.00 58.69  ? 51  THR   A CG2    1 
ATOM   381   N  N      . PHE   A 1  52  ? 32.727  -97.687  -59.586  1.00 59.54  ? 52  PHE   A N      1 
ATOM   382   C  CA     . PHE   A 1  52  ? 32.138  -96.881  -58.537  1.00 58.89  ? 52  PHE   A CA     1 
ATOM   383   C  C      . PHE   A 1  52  ? 32.190  -97.545  -57.183  1.00 59.10  ? 52  PHE   A C      1 
ATOM   384   O  O      . PHE   A 1  52  ? 31.932  -96.874  -56.174  1.00 56.02  ? 52  PHE   A O      1 
ATOM   385   C  CB     . PHE   A 1  52  ? 30.677  -96.561  -58.857  1.00 55.14  ? 52  PHE   A CB     1 
ATOM   386   C  CG     . PHE   A 1  52  ? 30.511  -95.417  -59.788  1.00 56.87  ? 52  PHE   A CG     1 
ATOM   387   C  CD1    . PHE   A 1  52  ? 31.153  -95.405  -61.005  1.00 53.02  ? 52  PHE   A CD1    1 
ATOM   388   C  CD2    . PHE   A 1  52  ? 29.715  -94.336  -59.434  1.00 58.79  ? 52  PHE   A CD2    1 
ATOM   389   C  CE1    . PHE   A 1  52  ? 30.983  -94.351  -61.864  1.00 59.93  ? 52  PHE   A CE1    1 
ATOM   390   C  CE2    . PHE   A 1  52  ? 29.542  -93.276  -60.292  1.00 52.24  ? 52  PHE   A CE2    1 
ATOM   391   C  CZ     . PHE   A 1  52  ? 30.178  -93.283  -61.510  1.00 54.90  ? 52  PHE   A CZ     1 
ATOM   392   N  N      . PHE   A 1  53  ? 32.485  -98.835  -57.141  1.00 58.62  ? 53  PHE   A N      1 
ATOM   393   C  CA     . PHE   A 1  53  ? 32.565  -99.579  -55.904  1.00 58.29  ? 53  PHE   A CA     1 
ATOM   394   C  C      . PHE   A 1  53  ? 33.879  -100.335 -55.858  1.00 63.00  ? 53  PHE   A C      1 
ATOM   395   O  O      . PHE   A 1  53  ? 34.400  -100.777 -56.888  1.00 64.89  ? 53  PHE   A O      1 
ATOM   396   C  CB     . PHE   A 1  53  ? 31.416  -100.557 -55.769  1.00 53.76  ? 53  PHE   A CB     1 
ATOM   397   C  CG     . PHE   A 1  53  ? 30.083  -99.910  -55.714  1.00 55.05  ? 53  PHE   A CG     1 
ATOM   398   C  CD1    . PHE   A 1  53  ? 29.468  -99.464  -56.866  1.00 56.84  ? 53  PHE   A CD1    1 
ATOM   399   C  CD2    . PHE   A 1  53  ? 29.428  -99.752  -54.496  1.00 60.04  ? 53  PHE   A CD2    1 
ATOM   400   C  CE1    . PHE   A 1  53  ? 28.201  -98.867  -56.813  1.00 57.93  ? 53  PHE   A CE1    1 
ATOM   401   C  CE2    . PHE   A 1  53  ? 28.171  -99.149  -54.421  1.00 58.48  ? 53  PHE   A CE2    1 
ATOM   402   C  CZ     . PHE   A 1  53  ? 27.552  -98.708  -55.581  1.00 58.10  ? 53  PHE   A CZ     1 
ATOM   403   N  N      . SER   A 1  54  ? 34.417  -100.449 -54.649  1.00 67.56  ? 54  SER   A N      1 
ATOM   404   C  CA     . SER   A 1  54  ? 35.429  -101.433 -54.299  1.00 62.63  ? 54  SER   A CA     1 
ATOM   405   C  C      . SER   A 1  54  ? 34.776  -102.566 -53.514  1.00 60.53  ? 54  SER   A C      1 
ATOM   406   O  O      . SER   A 1  54  ? 33.695  -102.417 -52.930  1.00 58.99  ? 54  SER   A O      1 
ATOM   407   C  CB     . SER   A 1  54  ? 36.554  -100.800 -53.484  1.00 56.08  ? 54  SER   A CB     1 
ATOM   408   O  OG     . SER   A 1  54  ? 36.029  -100.074 -52.387  1.00 64.21  ? 54  SER   A OG     1 
ATOM   409   N  N      . GLU   A 1  55  ? 35.429  -103.720 -53.535  1.00 65.06  ? 55  GLU   A N      1 
ATOM   410   C  CA     . GLU   A 1  55  ? 34.948  -104.876 -52.797  1.00 68.37  ? 55  GLU   A CA     1 
ATOM   411   C  C      . GLU   A 1  55  ? 35.839  -105.100 -51.582  1.00 64.99  ? 55  GLU   A C      1 
ATOM   412   O  O      . GLU   A 1  55  ? 36.988  -104.646 -51.532  1.00 64.22  ? 55  GLU   A O      1 
ATOM   413   C  CB     . GLU   A 1  55  ? 34.902  -106.123 -53.694  1.00 71.25  ? 55  GLU   A CB     1 
ATOM   414   C  CG     . GLU   A 1  55  ? 34.405  -105.871 -55.133  1.00 67.44  ? 55  GLU   A CG     1 
ATOM   415   C  CD     . GLU   A 1  55  ? 33.918  -107.142 -55.796  1.00 74.59  ? 55  GLU   A CD     1 
ATOM   416   O  OE1    . GLU   A 1  55  ? 33.533  -108.059 -55.037  1.00 75.11  ? 55  GLU   A OE1    1 
ATOM   417   O  OE2    . GLU   A 1  55  ? 33.896  -107.233 -57.052  1.00 75.35  ? 55  GLU   A OE2    1 
ATOM   418   N  N      . THR   A 1  56  ? 35.293  -105.767 -50.574  1.00 63.73  ? 56  THR   A N      1 
ATOM   419   C  CA     . THR   A 1  56  ? 36.055  -106.050 -49.368  1.00 68.40  ? 56  THR   A CA     1 
ATOM   420   C  C      . THR   A 1  56  ? 36.330  -107.542 -49.266  1.00 73.50  ? 56  THR   A C      1 
ATOM   421   O  O      . THR   A 1  56  ? 35.532  -108.367 -49.725  1.00 73.20  ? 56  THR   A O      1 
ATOM   422   C  CB     . THR   A 1  56  ? 35.327  -105.585 -48.106  1.00 67.05  ? 56  THR   A CB     1 
ATOM   423   O  OG1    . THR   A 1  56  ? 34.284  -106.512 -47.778  1.00 64.23  ? 56  THR   A OG1    1 
ATOM   424   C  CG2    . THR   A 1  56  ? 34.737  -104.212 -48.317  1.00 69.55  ? 56  THR   A CG2    1 
ATOM   425   N  N      . GLY   A 1  57  ? 37.473  -107.877 -48.662  1.00 73.78  ? 57  GLY   A N      1 
ATOM   426   C  CA     . GLY   A 1  57  ? 37.792  -109.262 -48.383  1.00 69.86  ? 57  GLY   A CA     1 
ATOM   427   C  C      . GLY   A 1  57  ? 36.581  -109.997 -47.844  1.00 72.07  ? 57  GLY   A C      1 
ATOM   428   O  O      . GLY   A 1  57  ? 36.403  -111.193 -48.098  1.00 77.39  ? 57  GLY   A O      1 
ATOM   429   N  N      . ALA   A 1  58  ? 35.737  -109.289 -47.089  1.00 71.48  ? 58  ALA   A N      1 
ATOM   430   C  CA     . ALA   A 1  58  ? 34.456  -109.824 -46.649  1.00 72.69  ? 58  ALA   A CA     1 
ATOM   431   C  C      . ALA   A 1  58  ? 33.352  -109.534 -47.650  1.00 76.85  ? 58  ALA   A C      1 
ATOM   432   O  O      . ALA   A 1  58  ? 32.169  -109.574 -47.285  1.00 77.64  ? 58  ALA   A O      1 
ATOM   433   C  CB     . ALA   A 1  58  ? 34.081  -109.277 -45.268  1.00 69.09  ? 58  ALA   A CB     1 
ATOM   434   N  N      . GLY   A 1  59  ? 33.721  -109.216 -48.893  1.00 72.83  ? 59  GLY   A N      1 
ATOM   435   C  CA     . GLY   A 1  59  ? 32.756  -109.108 -49.973  1.00 73.72  ? 59  GLY   A CA     1 
ATOM   436   C  C      . GLY   A 1  59  ? 31.769  -107.970 -49.846  1.00 71.61  ? 59  GLY   A C      1 
ATOM   437   O  O      . GLY   A 1  59  ? 30.644  -108.070 -50.353  1.00 73.77  ? 59  GLY   A O      1 
ATOM   438   N  N      . LYS   A 1  60  ? 32.154  -106.886 -49.193  1.00 70.66  ? 60  LYS   A N      1 
ATOM   439   C  CA     . LYS   A 1  60  ? 31.303  -105.711 -49.156  1.00 71.08  ? 60  LYS   A CA     1 
ATOM   440   C  C      . LYS   A 1  60  ? 31.647  -104.781 -50.310  1.00 66.97  ? 60  LYS   A C      1 
ATOM   441   O  O      . LYS   A 1  60  ? 32.803  -104.684 -50.744  1.00 60.36  ? 60  LYS   A O      1 
ATOM   442   C  CB     . LYS   A 1  60  ? 31.438  -104.964 -47.831  1.00 69.10  ? 60  LYS   A CB     1 
ATOM   443   C  CG     . LYS   A 1  60  ? 31.073  -103.506 -47.953  1.00 69.87  ? 60  LYS   A CG     1 
ATOM   444   C  CD     . LYS   A 1  60  ? 31.493  -102.721 -46.738  1.00 70.20  ? 60  LYS   A CD     1 
ATOM   445   C  CE     . LYS   A 1  60  ? 30.484  -102.859 -45.624  1.00 61.57  ? 60  LYS   A CE     1 
ATOM   446   N  NZ     . LYS   A 1  60  ? 30.793  -101.810 -44.643  1.00 66.93  ? 60  LYS   A NZ     1 
ATOM   447   N  N      . HIS   A 1  61  ? 30.622  -104.096 -50.805  1.00 65.54  ? 61  HIS   A N      1 
ATOM   448   C  CA     . HIS   A 1  61  ? 30.757  -103.192 -51.937  1.00 67.92  ? 61  HIS   A CA     1 
ATOM   449   C  C      . HIS   A 1  61  ? 30.613  -101.765 -51.429  1.00 63.24  ? 61  HIS   A C      1 
ATOM   450   O  O      . HIS   A 1  61  ? 29.575  -101.401 -50.868  1.00 67.09  ? 61  HIS   A O      1 
ATOM   451   C  CB     . HIS   A 1  61  ? 29.734  -103.531 -53.019  1.00 65.61  ? 61  HIS   A CB     1 
ATOM   452   C  CG     . HIS   A 1  61  ? 29.964  -104.874 -53.639  1.00 70.17  ? 61  HIS   A CG     1 
ATOM   453   N  ND1    . HIS   A 1  61  ? 29.591  -106.054 -53.027  1.00 70.06  ? 61  HIS   A ND1    1 
ATOM   454   C  CD2    . HIS   A 1  61  ? 30.586  -105.228 -54.787  1.00 71.03  ? 61  HIS   A CD2    1 
ATOM   455   C  CE1    . HIS   A 1  61  ? 29.946  -107.074 -53.787  1.00 71.22  ? 61  HIS   A CE1    1 
ATOM   456   N  NE2    . HIS   A 1  61  ? 30.552  -106.600 -54.861  1.00 75.37  ? 61  HIS   A NE2    1 
ATOM   457   N  N      . VAL   A 1  62  ? 31.656  -100.970 -51.619  1.00 53.50  ? 62  VAL   A N      1 
ATOM   458   C  CA     . VAL   A 1  62  ? 31.858  -99.744  -50.864  1.00 62.89  ? 62  VAL   A CA     1 
ATOM   459   C  C      . VAL   A 1  62  ? 31.973  -98.577  -51.837  1.00 59.30  ? 62  VAL   A C      1 
ATOM   460   O  O      . VAL   A 1  62  ? 32.867  -98.566  -52.688  1.00 61.69  ? 62  VAL   A O      1 
ATOM   461   C  CB     . VAL   A 1  62  ? 33.105  -99.827  -49.964  1.00 61.93  ? 62  VAL   A CB     1 
ATOM   462   C  CG1    . VAL   A 1  62  ? 33.554  -98.444  -49.554  1.00 64.19  ? 62  VAL   A CG1    1 
ATOM   463   C  CG2    . VAL   A 1  62  ? 32.807  -100.651 -48.724  1.00 60.81  ? 62  VAL   A CG2    1 
ATOM   464   N  N      . PRO   A 1  63  ? 31.121  -97.567  -51.732  1.00 49.47  ? 63  PRO   A N      1 
ATOM   465   C  CA     . PRO   A 1  63  ? 31.218  -96.412  -52.629  1.00 55.72  ? 63  PRO   A CA     1 
ATOM   466   C  C      . PRO   A 1  63  ? 32.623  -95.817  -52.686  1.00 54.96  ? 63  PRO   A C      1 
ATOM   467   O  O      . PRO   A 1  63  ? 33.268  -95.593  -51.659  1.00 60.81  ? 63  PRO   A O      1 
ATOM   468   C  CB     . PRO   A 1  63  ? 30.212  -95.436  -52.019  1.00 51.38  ? 63  PRO   A CB     1 
ATOM   469   C  CG     . PRO   A 1  63  ? 29.184  -96.343  -51.392  1.00 56.49  ? 63  PRO   A CG     1 
ATOM   470   C  CD     . PRO   A 1  63  ? 29.952  -97.485  -50.838  1.00 58.62  ? 63  PRO   A CD     1 
ATOM   471   N  N      . ARG   A 1  64  ? 33.104  -95.561  -53.907  1.00 52.04  ? 64  ARG   A N      1 
ATOM   472   C  CA     . ARG   A 1  64  ? 34.307  -94.744  -54.114  1.00 56.50  ? 64  ARG   A CA     1 
ATOM   473   C  C      . ARG   A 1  64  ? 33.932  -93.273  -53.933  1.00 57.97  ? 64  ARG   A C      1 
ATOM   474   O  O      . ARG   A 1  64  ? 34.160  -92.414  -54.787  1.00 58.05  ? 64  ARG   A O      1 
ATOM   475   C  CB     . ARG   A 1  64  ? 34.938  -94.998  -55.481  1.00 54.83  ? 64  ARG   A CB     1 
ATOM   476   C  CG     . ARG   A 1  64  ? 35.574  -96.381  -55.625  1.00 58.45  ? 64  ARG   A CG     1 
ATOM   477   C  CD     . ARG   A 1  64  ? 36.319  -96.595  -56.951  1.00 58.42  ? 64  ARG   A CD     1 
ATOM   478   N  NE     . ARG   A 1  64  ? 36.304  -98.017  -57.278  1.00 65.31  ? 64  ARG   A NE     1 
ATOM   479   C  CZ     . ARG   A 1  64  ? 37.108  -98.935  -56.753  1.00 65.78  ? 64  ARG   A CZ     1 
ATOM   480   N  NH1    . ARG   A 1  64  ? 38.153  -98.606  -56.007  1.00 66.92  ? 64  ARG   A NH1    1 
ATOM   481   N  NH2    . ARG   A 1  64  ? 36.852  -100.217 -56.973  1.00 60.70  ? 64  ARG   A NH2    1 
ATOM   482   N  N      . ALA   A 1  65  ? 33.323  -93.016  -52.778  1.00 57.11  ? 65  ALA   A N      1 
ATOM   483   C  CA     . ALA   A 1  65  ? 32.713  -91.745  -52.450  1.00 55.33  ? 65  ALA   A CA     1 
ATOM   484   C  C      . ALA   A 1  65  ? 33.438  -91.096  -51.277  1.00 64.64  ? 65  ALA   A C      1 
ATOM   485   O  O      . ALA   A 1  65  ? 33.876  -91.777  -50.338  1.00 62.20  ? 65  ALA   A O      1 
ATOM   486   C  CB     . ALA   A 1  65  ? 31.236  -91.937  -52.098  1.00 52.73  ? 65  ALA   A CB     1 
ATOM   487   N  N      . VAL   A 1  66  ? 33.544  -89.767  -51.343  1.00 61.03  ? 66  VAL   A N      1 
ATOM   488   C  CA     . VAL   A 1  66  ? 33.954  -88.918  -50.227  1.00 58.76  ? 66  VAL   A CA     1 
ATOM   489   C  C      . VAL   A 1  66  ? 32.887  -87.845  -50.039  1.00 56.41  ? 66  VAL   A C      1 
ATOM   490   O  O      . VAL   A 1  66  ? 32.599  -87.080  -50.969  1.00 57.01  ? 66  VAL   A O      1 
ATOM   491   C  CB     . VAL   A 1  66  ? 35.316  -88.246  -50.469  1.00 54.07  ? 66  VAL   A CB     1 
ATOM   492   C  CG1    . VAL   A 1  66  ? 35.418  -86.997  -49.615  1.00 50.26  ? 66  VAL   A CG1    1 
ATOM   493   C  CG2    . VAL   A 1  66  ? 36.444  -89.197  -50.175  1.00 58.41  ? 66  VAL   A CG2    1 
ATOM   494   N  N      . PHE   A 1  67  ? 32.324  -87.768  -48.845  1.00 55.73  ? 67  PHE   A N      1 
ATOM   495   C  CA     . PHE   A 1  67  ? 31.424  -86.683  -48.482  1.00 49.58  ? 67  PHE   A CA     1 
ATOM   496   C  C      . PHE   A 1  67  ? 32.182  -85.687  -47.616  1.00 55.13  ? 67  PHE   A C      1 
ATOM   497   O  O      . PHE   A 1  67  ? 32.982  -86.079  -46.763  1.00 59.12  ? 67  PHE   A O      1 
ATOM   498   C  CB     . PHE   A 1  67  ? 30.210  -87.213  -47.726  1.00 50.80  ? 67  PHE   A CB     1 
ATOM   499   C  CG     . PHE   A 1  67  ? 29.318  -88.088  -48.553  1.00 56.99  ? 67  PHE   A CG     1 
ATOM   500   C  CD1    . PHE   A 1  67  ? 29.820  -89.207  -49.192  1.00 61.45  ? 67  PHE   A CD1    1 
ATOM   501   C  CD2    . PHE   A 1  67  ? 27.976  -87.816  -48.661  1.00 53.49  ? 67  PHE   A CD2    1 
ATOM   502   C  CE1    . PHE   A 1  67  ? 29.010  -90.014  -49.939  1.00 58.71  ? 67  PHE   A CE1    1 
ATOM   503   C  CE2    . PHE   A 1  67  ? 27.162  -88.630  -49.397  1.00 56.20  ? 67  PHE   A CE2    1 
ATOM   504   C  CZ     . PHE   A 1  67  ? 27.679  -89.730  -50.038  1.00 56.64  ? 67  PHE   A CZ     1 
ATOM   505   N  N      . VAL   A 1  68  ? 31.935  -84.403  -47.825  1.00 50.47  ? 68  VAL   A N      1 
ATOM   506   C  CA     . VAL   A 1  68  ? 32.633  -83.389  -47.050  1.00 50.67  ? 68  VAL   A CA     1 
ATOM   507   C  C      . VAL   A 1  68  ? 31.749  -82.167  -46.853  1.00 48.71  ? 68  VAL   A C      1 
ATOM   508   O  O      . VAL   A 1  68  ? 31.376  -81.490  -47.816  1.00 49.86  ? 68  VAL   A O      1 
ATOM   509   C  CB     . VAL   A 1  68  ? 33.964  -83.011  -47.717  1.00 46.58  ? 68  VAL   A CB     1 
ATOM   510   C  CG1    . VAL   A 1  68  ? 33.741  -82.781  -49.159  1.00 52.40  ? 68  VAL   A CG1    1 
ATOM   511   C  CG2    . VAL   A 1  68  ? 34.480  -81.717  -47.117  1.00 45.74  ? 68  VAL   A CG2    1 
ATOM   512   N  N      . ASP   A 1  69  ? 31.414  -81.873  -45.603  1.00 53.45  ? 69  ASP   A N      1 
ATOM   513   C  CA     . ASP   A 1  69  ? 30.637  -80.693  -45.272  1.00 53.48  ? 69  ASP   A CA     1 
ATOM   514   C  C      . ASP   A 1  69  ? 31.362  -79.940  -44.171  1.00 57.33  ? 69  ASP   A C      1 
ATOM   515   O  O      . ASP   A 1  69  ? 31.838  -80.548  -43.201  1.00 55.29  ? 69  ASP   A O      1 
ATOM   516   C  CB     . ASP   A 1  69  ? 29.203  -81.066  -44.831  1.00 51.89  ? 69  ASP   A CB     1 
ATOM   517   C  CG     . ASP   A 1  69  ? 28.246  -79.891  -44.919  1.00 52.91  ? 69  ASP   A CG     1 
ATOM   518   O  OD1    . ASP   A 1  69  ? 28.686  -78.795  -45.355  1.00 50.64  ? 69  ASP   A OD1    1 
ATOM   519   O  OD2    . ASP   A 1  69  ? 27.049  -80.074  -44.585  1.00 57.87  ? 69  ASP   A OD2    1 
ATOM   520   N  N      . LEU   A 1  70  ? 31.442  -78.619  -44.319  1.00 51.81  ? 70  LEU   A N      1 
ATOM   521   C  CA     . LEU   A 1  70  ? 31.999  -77.805  -43.248  1.00 50.21  ? 70  LEU   A CA     1 
ATOM   522   C  C      . LEU   A 1  70  ? 31.192  -77.902  -41.952  1.00 55.30  ? 70  LEU   A C      1 
ATOM   523   O  O      . LEU   A 1  70  ? 31.575  -77.282  -40.954  1.00 57.37  ? 70  LEU   A O      1 
ATOM   524   C  CB     . LEU   A 1  70  ? 32.112  -76.350  -43.710  1.00 39.75  ? 70  LEU   A CB     1 
ATOM   525   C  CG     . LEU   A 1  70  ? 33.073  -76.305  -44.899  1.00 45.62  ? 70  LEU   A CG     1 
ATOM   526   C  CD1    . LEU   A 1  70  ? 33.461  -74.896  -45.305  1.00 42.17  ? 70  LEU   A CD1    1 
ATOM   527   C  CD2    . LEU   A 1  70  ? 34.307  -77.122  -44.595  1.00 46.20  ? 70  LEU   A CD2    1 
ATOM   528   N  N      . GLU   A 1  71  ? 30.112  -78.680  -41.919  1.00 51.82  ? 71  GLU   A N      1 
ATOM   529   C  CA     . GLU   A 1  71  ? 29.239  -78.676  -40.768  1.00 55.70  ? 71  GLU   A CA     1 
ATOM   530   C  C      . GLU   A 1  71  ? 28.644  -80.067  -40.587  1.00 54.81  ? 71  GLU   A C      1 
ATOM   531   O  O      . GLU   A 1  71  ? 28.290  -80.721  -41.580  1.00 63.19  ? 71  GLU   A O      1 
ATOM   532   C  CB     . GLU   A 1  71  ? 28.136  -77.620  -40.956  1.00 56.52  ? 71  GLU   A CB     1 
ATOM   533   C  CG     . GLU   A 1  71  ? 26.889  -77.914  -40.184  1.00 58.29  ? 71  GLU   A CG     1 
ATOM   534   C  CD     . GLU   A 1  71  ? 25.682  -77.780  -41.056  1.00 64.07  ? 71  GLU   A CD     1 
ATOM   535   O  OE1    . GLU   A 1  71  ? 25.781  -77.130  -42.128  1.00 72.36  ? 71  GLU   A OE1    1 
ATOM   536   O  OE2    . GLU   A 1  71  ? 24.654  -78.404  -40.718  1.00 69.04  ? 71  GLU   A OE2    1 
ATOM   537   N  N      . PRO   A 1  72  ? 28.490  -80.533  -39.343  1.00 55.38  ? 72  PRO   A N      1 
ATOM   538   C  CA     . PRO   A 1  72  ? 28.204  -81.962  -39.118  1.00 55.48  ? 72  PRO   A CA     1 
ATOM   539   C  C      . PRO   A 1  72  ? 26.763  -82.395  -39.343  1.00 58.97  ? 72  PRO   A C      1 
ATOM   540   O  O      . PRO   A 1  72  ? 26.497  -83.600  -39.328  1.00 59.66  ? 72  PRO   A O      1 
ATOM   541   C  CB     . PRO   A 1  72  ? 28.590  -82.160  -37.646  1.00 52.89  ? 72  PRO   A CB     1 
ATOM   542   C  CG     . PRO   A 1  72  ? 28.374  -80.835  -37.014  1.00 42.47  ? 72  PRO   A CG     1 
ATOM   543   C  CD     . PRO   A 1  72  ? 28.767  -79.820  -38.079  1.00 55.33  ? 72  PRO   A CD     1 
ATOM   544   N  N      . THR   A 1  73  ? 25.820  -81.481  -39.540  1.00 59.27  ? 73  THR   A N      1 
ATOM   545   C  CA     . THR   A 1  73  ? 24.424  -81.884  -39.424  1.00 61.01  ? 73  THR   A CA     1 
ATOM   546   C  C      . THR   A 1  73  ? 23.999  -82.823  -40.545  1.00 62.54  ? 73  THR   A C      1 
ATOM   547   O  O      . THR   A 1  73  ? 23.268  -83.792  -40.300  1.00 63.71  ? 73  THR   A O      1 
ATOM   548   C  CB     . THR   A 1  73  ? 23.534  -80.655  -39.398  1.00 62.45  ? 73  THR   A CB     1 
ATOM   549   O  OG1    . THR   A 1  73  ? 24.219  -79.619  -38.698  1.00 63.19  ? 73  THR   A OG1    1 
ATOM   550   C  CG2    . THR   A 1  73  ? 22.252  -80.975  -38.687  1.00 68.73  ? 73  THR   A CG2    1 
ATOM   551   N  N      . VAL   A 1  74  ? 24.427  -82.548  -41.779  1.00 60.58  ? 74  VAL   A N      1 
ATOM   552   C  CA     . VAL   A 1  74  ? 23.910  -83.287  -42.925  1.00 55.31  ? 74  VAL   A CA     1 
ATOM   553   C  C      . VAL   A 1  74  ? 24.617  -84.626  -43.069  1.00 59.19  ? 74  VAL   A C      1 
ATOM   554   O  O      . VAL   A 1  74  ? 23.976  -85.673  -43.208  1.00 59.10  ? 74  VAL   A O      1 
ATOM   555   C  CB     . VAL   A 1  74  ? 24.034  -82.435  -44.198  1.00 55.90  ? 74  VAL   A CB     1 
ATOM   556   C  CG1    . VAL   A 1  74  ? 23.229  -83.059  -45.320  1.00 52.51  ? 74  VAL   A CG1    1 
ATOM   557   C  CG2    . VAL   A 1  74  ? 23.552  -80.999  -43.920  1.00 51.81  ? 74  VAL   A CG2    1 
ATOM   558   N  N      . ILE   A 1  75  ? 25.950  -84.617  -43.028  1.00 58.27  ? 75  ILE   A N      1 
ATOM   559   C  CA     . ILE   A 1  75  ? 26.711  -85.853  -43.110  1.00 50.66  ? 75  ILE   A CA     1 
ATOM   560   C  C      . ILE   A 1  75  ? 26.457  -86.755  -41.905  1.00 58.68  ? 75  ILE   A C      1 
ATOM   561   O  O      . ILE   A 1  75  ? 26.635  -87.977  -41.994  1.00 59.57  ? 75  ILE   A O      1 
ATOM   562   C  CB     . ILE   A 1  75  ? 28.189  -85.471  -43.300  1.00 42.06  ? 75  ILE   A CB     1 
ATOM   563   C  CG1    . ILE   A 1  75  ? 28.379  -84.915  -44.718  1.00 42.20  ? 75  ILE   A CG1    1 
ATOM   564   C  CG2    . ILE   A 1  75  ? 29.104  -86.623  -42.969  1.00 45.77  ? 75  ILE   A CG2    1 
ATOM   565   C  CD1    . ILE   A 1  75  ? 29.794  -84.720  -45.119  1.00 48.34  ? 75  ILE   A CD1    1 
ATOM   566   N  N      . ASP   A 1  76  ? 26.012  -86.186  -40.782  1.00 56.65  ? 76  ASP   A N      1 
ATOM   567   C  CA     . ASP   A 1  76  ? 25.630  -87.010  -39.639  1.00 61.80  ? 76  ASP   A CA     1 
ATOM   568   C  C      . ASP   A 1  76  ? 24.438  -87.888  -39.973  1.00 65.96  ? 76  ASP   A C      1 
ATOM   569   O  O      . ASP   A 1  76  ? 24.391  -89.059  -39.578  1.00 67.88  ? 76  ASP   A O      1 
ATOM   570   C  CB     . ASP   A 1  76  ? 25.300  -86.138  -38.429  1.00 62.24  ? 76  ASP   A CB     1 
ATOM   571   C  CG     . ASP   A 1  76  ? 26.498  -85.908  -37.531  1.00 65.45  ? 76  ASP   A CG     1 
ATOM   572   O  OD1    . ASP   A 1  76  ? 27.503  -86.647  -37.681  1.00 63.79  ? 76  ASP   A OD1    1 
ATOM   573   O  OD2    . ASP   A 1  76  ? 26.440  -84.957  -36.710  1.00 56.88  ? 76  ASP   A OD2    1 
ATOM   574   N  N      . GLU   A 1  77  ? 23.456  -87.341  -40.687  1.00 66.27  ? 77  GLU   A N      1 
ATOM   575   C  CA     . GLU   A 1  77  ? 22.318  -88.159  -41.083  1.00 66.64  ? 77  GLU   A CA     1 
ATOM   576   C  C      . GLU   A 1  77  ? 22.750  -89.300  -41.992  1.00 65.81  ? 77  GLU   A C      1 
ATOM   577   O  O      . GLU   A 1  77  ? 22.139  -90.374  -41.958  1.00 73.47  ? 77  GLU   A O      1 
ATOM   578   C  CB     . GLU   A 1  77  ? 21.253  -87.287  -41.741  1.00 68.64  ? 77  GLU   A CB     1 
ATOM   579   C  CG     . GLU   A 1  77  ? 20.669  -86.239  -40.799  1.00 64.98  ? 77  GLU   A CG     1 
ATOM   580   C  CD     . GLU   A 1  77  ? 19.546  -85.442  -41.435  1.00 79.40  ? 77  GLU   A CD     1 
ATOM   581   O  OE1    . GLU   A 1  77  ? 18.503  -86.042  -41.792  1.00 87.26  ? 77  GLU   A OE1    1 
ATOM   582   O  OE2    . GLU   A 1  77  ? 19.712  -84.210  -41.592  1.00 79.07  ? 77  GLU   A OE2    1 
ATOM   583   N  N      . VAL   A 1  78  ? 23.810  -89.105  -42.786  1.00 65.04  ? 78  VAL   A N      1 
ATOM   584   C  CA     . VAL   A 1  78  ? 24.438  -90.232  -43.479  1.00 64.31  ? 78  VAL   A CA     1 
ATOM   585   C  C      . VAL   A 1  78  ? 25.017  -91.215  -42.461  1.00 70.97  ? 78  VAL   A C      1 
ATOM   586   O  O      . VAL   A 1  78  ? 24.772  -92.425  -42.532  1.00 74.17  ? 78  VAL   A O      1 
ATOM   587   C  CB     . VAL   A 1  78  ? 25.525  -89.748  -44.461  1.00 63.48  ? 78  VAL   A CB     1 
ATOM   588   C  CG1    . VAL   A 1  78  ? 25.937  -90.879  -45.394  1.00 59.27  ? 78  VAL   A CG1    1 
ATOM   589   C  CG2    . VAL   A 1  78  ? 25.079  -88.526  -45.261  1.00 57.08  ? 78  VAL   A CG2    1 
ATOM   590   N  N      . ARG   A 1  79  ? 25.781  -90.707  -41.484  1.00 67.61  ? 79  ARG   A N      1 
ATOM   591   C  CA     . ARG   A 1  79  ? 26.415  -91.585  -40.502  1.00 66.43  ? 79  ARG   A CA     1 
ATOM   592   C  C      . ARG   A 1  79  ? 25.418  -92.447  -39.735  1.00 68.87  ? 79  ARG   A C      1 
ATOM   593   O  O      . ARG   A 1  79  ? 25.831  -93.413  -39.085  1.00 70.25  ? 79  ARG   A O      1 
ATOM   594   C  CB     . ARG   A 1  79  ? 27.232  -90.769  -39.506  1.00 58.63  ? 79  ARG   A CB     1 
ATOM   595   C  CG     . ARG   A 1  79  ? 28.482  -90.202  -40.074  1.00 61.65  ? 79  ARG   A CG     1 
ATOM   596   C  CD     . ARG   A 1  79  ? 28.958  -89.053  -39.240  1.00 61.18  ? 79  ARG   A CD     1 
ATOM   597   N  NE     . ARG   A 1  79  ? 30.322  -88.695  -39.599  1.00 58.82  ? 79  ARG   A NE     1 
ATOM   598   C  CZ     . ARG   A 1  79  ? 30.788  -87.456  -39.630  1.00 54.75  ? 79  ARG   A CZ     1 
ATOM   599   N  NH1    . ARG   A 1  79  ? 30.016  -86.421  -39.341  1.00 58.16  ? 79  ARG   A NH1    1 
ATOM   600   N  NH2    . ARG   A 1  79  ? 32.056  -87.252  -39.965  1.00 51.09  ? 79  ARG   A NH2    1 
ATOM   601   N  N      . THR   A 1  80  ? 24.122  -92.122  -39.791  1.00 66.96  ? 80  THR   A N      1 
ATOM   602   C  CA     . THR   A 1  80  ? 23.113  -92.806  -38.993  1.00 63.40  ? 80  THR   A CA     1 
ATOM   603   C  C      . THR   A 1  80  ? 21.942  -93.287  -39.843  1.00 67.42  ? 80  THR   A C      1 
ATOM   604   O  O      . THR   A 1  80  ? 20.888  -93.625  -39.297  1.00 71.82  ? 80  THR   A O      1 
ATOM   605   C  CB     . THR   A 1  80  ? 22.599  -91.883  -37.883  1.00 71.16  ? 80  THR   A CB     1 
ATOM   606   O  OG1    . THR   A 1  80  ? 22.076  -90.680  -38.469  1.00 68.45  ? 80  THR   A OG1    1 
ATOM   607   C  CG2    . THR   A 1  80  ? 23.717  -91.528  -36.890  1.00 63.73  ? 80  THR   A CG2    1 
ATOM   608   N  N      . GLY   A 1  81  ? 22.103  -93.321  -41.164  1.00 65.74  ? 81  GLY   A N      1 
ATOM   609   C  CA     . GLY   A 1  81  ? 21.018  -93.624  -42.070  1.00 65.31  ? 81  GLY   A CA     1 
ATOM   610   C  C      . GLY   A 1  81  ? 20.999  -95.075  -42.516  1.00 65.50  ? 81  GLY   A C      1 
ATOM   611   O  O      . GLY   A 1  81  ? 21.862  -95.875  -42.160  1.00 68.58  ? 81  GLY   A O      1 
ATOM   612   N  N      . THR   A 1  82  ? 19.978  -95.398  -43.320  1.00 60.66  ? 82  THR   A N      1 
ATOM   613   C  CA     . THR   A 1  82  ? 19.808  -96.767  -43.802  1.00 67.89  ? 82  THR   A CA     1 
ATOM   614   C  C      . THR   A 1  82  ? 21.086  -97.309  -44.439  1.00 71.44  ? 82  THR   A C      1 
ATOM   615   O  O      . THR   A 1  82  ? 21.331  -98.527  -44.411  1.00 68.73  ? 82  THR   A O      1 
ATOM   616   C  CB     . THR   A 1  82  ? 18.656  -96.842  -44.809  1.00 64.84  ? 82  THR   A CB     1 
ATOM   617   O  OG1    . THR   A 1  82  ? 19.065  -96.217  -46.029  1.00 76.10  ? 82  THR   A OG1    1 
ATOM   618   C  CG2    . THR   A 1  82  ? 17.412  -96.134  -44.291  1.00 59.51  ? 82  THR   A CG2    1 
ATOM   619   N  N      . TYR   A 1  83  ? 21.912  -96.430  -45.014  1.00 65.15  ? 83  TYR   A N      1 
ATOM   620   C  CA     . TYR   A 1  83  ? 23.137  -96.845  -45.681  1.00 68.80  ? 83  TYR   A CA     1 
ATOM   621   C  C      . TYR   A 1  83  ? 24.364  -96.479  -44.858  1.00 71.92  ? 83  TYR   A C      1 
ATOM   622   O  O      . TYR   A 1  83  ? 25.437  -96.212  -45.406  1.00 71.40  ? 83  TYR   A O      1 
ATOM   623   C  CB     . TYR   A 1  83  ? 23.213  -96.258  -47.093  1.00 68.04  ? 83  TYR   A CB     1 
ATOM   624   C  CG     . TYR   A 1  83  ? 22.178  -96.860  -48.029  1.00 69.65  ? 83  TYR   A CG     1 
ATOM   625   C  CD1    . TYR   A 1  83  ? 22.426  -98.062  -48.692  1.00 71.27  ? 83  TYR   A CD1    1 
ATOM   626   C  CD2    . TYR   A 1  83  ? 20.947  -96.240  -48.234  1.00 62.03  ? 83  TYR   A CD2    1 
ATOM   627   C  CE1    . TYR   A 1  83  ? 21.479  -98.633  -49.534  1.00 68.56  ? 83  TYR   A CE1    1 
ATOM   628   C  CE2    . TYR   A 1  83  ? 19.993  -96.796  -49.076  1.00 62.65  ? 83  TYR   A CE2    1 
ATOM   629   C  CZ     . TYR   A 1  83  ? 20.258  -97.997  -49.727  1.00 71.27  ? 83  TYR   A CZ     1 
ATOM   630   O  OH     . TYR   A 1  83  ? 19.310  -98.566  -50.577  1.00 69.09  ? 83  TYR   A OH     1 
ATOM   631   N  N      . ARG   A 1  84  ? 24.218  -96.486  -43.533  1.00 72.64  ? 84  ARG   A N      1 
ATOM   632   C  CA     . ARG   A 1  84  ? 25.356  -96.196  -42.673  1.00 73.22  ? 84  ARG   A CA     1 
ATOM   633   C  C      . ARG   A 1  84  ? 26.480  -97.203  -42.879  1.00 75.12  ? 84  ARG   A C      1 
ATOM   634   O  O      . ARG   A 1  84  ? 27.660  -96.838  -42.840  1.00 79.96  ? 84  ARG   A O      1 
ATOM   635   C  CB     . ARG   A 1  84  ? 24.920  -96.175  -41.209  1.00 74.42  ? 84  ARG   A CB     1 
ATOM   636   C  CG     . ARG   A 1  84  ? 25.221  -97.454  -40.458  1.00 79.46  ? 84  ARG   A CG     1 
ATOM   637   C  CD     . ARG   A 1  84  ? 24.216  -97.696  -39.360  1.00 78.68  ? 84  ARG   A CD     1 
ATOM   638   N  NE     . ARG   A 1  84  ? 22.863  -97.698  -39.901  1.00 79.28  ? 84  ARG   A NE     1 
ATOM   639   C  CZ     . ARG   A 1  84  ? 21.792  -98.093  -39.230  1.00 81.43  ? 84  ARG   A CZ     1 
ATOM   640   N  NH1    . ARG   A 1  84  ? 21.891  -98.595  -38.010  1.00 84.90  ? 84  ARG   A NH1    1 
ATOM   641   N  NH2    . ARG   A 1  84  ? 20.595  -97.993  -39.801  1.00 74.17  ? 84  ARG   A NH2    1 
ATOM   642   N  N      . GLN   A 1  85  ? 26.145  -98.478  -43.086  1.00 74.58  ? 85  GLN   A N      1 
ATOM   643   C  CA     . GLN   A 1  85  ? 27.196  -99.479  -43.225  1.00 76.54  ? 85  GLN   A CA     1 
ATOM   644   C  C      . GLN   A 1  85  ? 27.899  -99.390  -44.569  1.00 75.11  ? 85  GLN   A C      1 
ATOM   645   O  O      . GLN   A 1  85  ? 29.050  -99.832  -44.685  1.00 74.24  ? 85  GLN   A O      1 
ATOM   646   C  CB     . GLN   A 1  85  ? 26.618  -100.878 -43.020  1.00 76.05  ? 85  GLN   A CB     1 
ATOM   647   C  CG     . GLN   A 1  85  ? 25.753  -100.983 -41.769  1.00 84.18  ? 85  GLN   A CG     1 
ATOM   648   C  CD     . GLN   A 1  85  ? 24.654  -102.021 -41.910  1.00 89.42  ? 85  GLN   A CD     1 
ATOM   649   O  OE1    . GLN   A 1  85  ? 23.545  -101.731 -42.385  1.00 82.39  ? 85  GLN   A OE1    1 
ATOM   650   N  NE2    . GLN   A 1  85  ? 24.961  -103.247 -41.499  1.00 85.92  ? 85  GLN   A NE2    1 
ATOM   651   N  N      . LEU   A 1  86  ? 27.242  -98.786  -45.560  1.00 68.42  ? 86  LEU   A N      1 
ATOM   652   C  CA     . LEU   A 1  86  ? 27.792  -98.704  -46.910  1.00 72.08  ? 86  LEU   A CA     1 
ATOM   653   C  C      . LEU   A 1  86  ? 29.126  -97.971  -46.934  1.00 72.69  ? 86  LEU   A C      1 
ATOM   654   O  O      . LEU   A 1  86  ? 30.099  -98.433  -47.547  1.00 67.21  ? 86  LEU   A O      1 
ATOM   655   C  CB     . LEU   A 1  86  ? 26.793  -97.991  -47.812  1.00 72.25  ? 86  LEU   A CB     1 
ATOM   656   C  CG     . LEU   A 1  86  ? 26.864  -98.367  -49.269  1.00 69.10  ? 86  LEU   A CG     1 
ATOM   657   C  CD1    . LEU   A 1  86  ? 26.279  -99.758  -49.384  1.00 73.06  ? 86  LEU   A CD1    1 
ATOM   658   C  CD2    . LEU   A 1  86  ? 26.076  -97.339  -50.050  1.00 66.37  ? 86  LEU   A CD2    1 
ATOM   659   N  N      . PHE   A 1  87  ? 29.178  -96.809  -46.297  1.00 71.95  ? 87  PHE   A N      1 
ATOM   660   C  CA     . PHE   A 1  87  ? 30.350  -95.957  -46.354  1.00 69.05  ? 87  PHE   A CA     1 
ATOM   661   C  C      . PHE   A 1  87  ? 31.310  -96.272  -45.219  1.00 72.74  ? 87  PHE   A C      1 
ATOM   662   O  O      . PHE   A 1  87  ? 30.951  -96.904  -44.220  1.00 75.91  ? 87  PHE   A O      1 
ATOM   663   C  CB     . PHE   A 1  87  ? 29.935  -94.494  -46.296  1.00 67.25  ? 87  PHE   A CB     1 
ATOM   664   C  CG     . PHE   A 1  87  ? 28.921  -94.123  -47.324  1.00 67.07  ? 87  PHE   A CG     1 
ATOM   665   C  CD1    . PHE   A 1  87  ? 29.315  -93.793  -48.613  1.00 59.78  ? 87  PHE   A CD1    1 
ATOM   666   C  CD2    . PHE   A 1  87  ? 27.573  -94.102  -47.008  1.00 63.17  ? 87  PHE   A CD2    1 
ATOM   667   C  CE1    . PHE   A 1  87  ? 28.389  -93.447  -49.551  1.00 57.61  ? 87  PHE   A CE1    1 
ATOM   668   C  CE2    . PHE   A 1  87  ? 26.642  -93.754  -47.952  1.00 56.61  ? 87  PHE   A CE2    1 
ATOM   669   C  CZ     . PHE   A 1  87  ? 27.047  -93.432  -49.223  1.00 57.50  ? 87  PHE   A CZ     1 
ATOM   670   N  N      . HIS   A 1  88  ? 32.542  -95.816  -45.386  1.00 66.02  ? 88  HIS   A N      1 
ATOM   671   C  CA     . HIS   A 1  88  ? 33.545  -96.029  -44.374  1.00 69.67  ? 88  HIS   A CA     1 
ATOM   672   C  C      . HIS   A 1  88  ? 33.809  -94.723  -43.643  1.00 75.75  ? 88  HIS   A C      1 
ATOM   673   O  O      . HIS   A 1  88  ? 34.101  -93.703  -44.286  1.00 71.84  ? 88  HIS   A O      1 
ATOM   674   C  CB     . HIS   A 1  88  ? 34.842  -96.571  -44.997  1.00 74.19  ? 88  HIS   A CB     1 
ATOM   675   C  CG     . HIS   A 1  88  ? 36.062  -96.356  -44.151  1.00 86.03  ? 88  HIS   A CG     1 
ATOM   676   N  ND1    . HIS   A 1  88  ? 36.336  -97.125  -43.035  1.00 93.80  ? 88  HIS   A ND1    1 
ATOM   677   C  CD2    . HIS   A 1  88  ? 37.111  -95.508  -44.287  1.00 86.08  ? 88  HIS   A CD2    1 
ATOM   678   C  CE1    . HIS   A 1  88  ? 37.475  -96.730  -42.494  1.00 86.36  ? 88  HIS   A CE1    1 
ATOM   679   N  NE2    . HIS   A 1  88  ? 37.974  -95.761  -43.243  1.00 87.99  ? 88  HIS   A NE2    1 
ATOM   680   N  N      . PRO   A 1  89  ? 33.701  -94.716  -42.311  1.00 75.21  ? 89  PRO   A N      1 
ATOM   681   C  CA     . PRO   A 1  89  ? 33.837  -93.470  -41.541  1.00 70.27  ? 89  PRO   A CA     1 
ATOM   682   C  C      . PRO   A 1  89  ? 34.776  -92.409  -42.113  1.00 67.50  ? 89  PRO   A C      1 
ATOM   683   O  O      . PRO   A 1  89  ? 34.386  -91.238  -42.155  1.00 65.37  ? 89  PRO   A O      1 
ATOM   684   C  CB     . PRO   A 1  89  ? 34.326  -93.982  -40.186  1.00 68.62  ? 89  PRO   A CB     1 
ATOM   685   C  CG     . PRO   A 1  89  ? 33.574  -95.287  -40.039  1.00 73.73  ? 89  PRO   A CG     1 
ATOM   686   C  CD     . PRO   A 1  89  ? 33.360  -95.854  -41.441  1.00 68.91  ? 89  PRO   A CD     1 
ATOM   687   N  N      . GLU   A 1  90  ? 35.996  -92.757  -42.548  1.00 72.57  ? 90  GLU   A N      1 
ATOM   688   C  CA     . GLU   A 1  90  ? 36.897  -91.693  -43.005  1.00 69.84  ? 90  GLU   A CA     1 
ATOM   689   C  C      . GLU   A 1  90  ? 36.508  -91.118  -44.354  1.00 70.00  ? 90  GLU   A C      1 
ATOM   690   O  O      . GLU   A 1  90  ? 37.208  -90.220  -44.837  1.00 69.12  ? 90  GLU   A O      1 
ATOM   691   C  CB     . GLU   A 1  90  ? 38.355  -92.156  -43.086  1.00 72.17  ? 90  GLU   A CB     1 
ATOM   692   C  CG     . GLU   A 1  90  ? 38.721  -93.362  -42.224  1.00 83.36  ? 90  GLU   A CG     1 
ATOM   693   C  CD     . GLU   A 1  90  ? 40.201  -93.758  -42.381  1.00 91.58  ? 90  GLU   A CD     1 
ATOM   694   O  OE1    . GLU   A 1  90  ? 40.654  -93.922  -43.544  1.00 92.34  ? 90  GLU   A OE1    1 
ATOM   695   O  OE2    . GLU   A 1  90  ? 40.904  -93.954  -41.357  1.00 93.51  ? 90  GLU   A OE2    1 
ATOM   696   N  N      . GLN   A 1  91  ? 35.451  -91.618  -44.995  1.00 72.31  ? 91  GLN   A N      1 
ATOM   697   C  CA     . GLN   A 1  91  ? 34.969  -91.008  -46.227  1.00 64.98  ? 91  GLN   A CA     1 
ATOM   698   C  C      . GLN   A 1  91  ? 33.911  -89.953  -45.961  1.00 63.48  ? 91  GLN   A C      1 
ATOM   699   O  O      . GLN   A 1  91  ? 33.576  -89.194  -46.881  1.00 65.72  ? 91  GLN   A O      1 
ATOM   700   C  CB     . GLN   A 1  91  ? 34.402  -92.073  -47.175  1.00 71.54  ? 91  GLN   A CB     1 
ATOM   701   C  CG     . GLN   A 1  91  ? 34.934  -93.477  -46.936  1.00 72.27  ? 91  GLN   A CG     1 
ATOM   702   C  CD     . GLN   A 1  91  ? 34.201  -94.540  -47.738  1.00 73.25  ? 91  GLN   A CD     1 
ATOM   703   O  OE1    . GLN   A 1  91  ? 32.973  -94.675  -47.660  1.00 72.62  ? 91  GLN   A OE1    1 
ATOM   704   N  NE2    . GLN   A 1  91  ? 34.961  -95.337  -48.473  1.00 75.34  ? 91  GLN   A NE2    1 
ATOM   705   N  N      . LEU   A 1  92  ? 33.387  -89.903  -44.729  1.00 60.24  ? 92  LEU   A N      1 
ATOM   706   C  CA     . LEU   A 1  92  ? 32.413  -88.914  -44.263  1.00 55.31  ? 92  LEU   A CA     1 
ATOM   707   C  C      . LEU   A 1  92  ? 33.141  -87.880  -43.405  1.00 57.59  ? 92  LEU   A C      1 
ATOM   708   O  O      . LEU   A 1  92  ? 33.219  -88.018  -42.188  1.00 65.91  ? 92  LEU   A O      1 
ATOM   709   C  CB     . LEU   A 1  92  ? 31.311  -89.605  -43.472  1.00 55.98  ? 92  LEU   A CB     1 
ATOM   710   C  CG     . LEU   A 1  92  ? 30.610  -90.757  -44.196  1.00 55.36  ? 92  LEU   A CG     1 
ATOM   711   C  CD1    . LEU   A 1  92  ? 29.570  -91.334  -43.299  1.00 57.00  ? 92  LEU   A CD1    1 
ATOM   712   C  CD2    . LEU   A 1  92  ? 29.970  -90.275  -45.486  1.00 55.11  ? 92  LEU   A CD2    1 
ATOM   713   N  N      . ILE   A 1  93  ? 33.667  -86.825  -44.048  1.00 57.63  ? 93  ILE   A N      1 
ATOM   714   C  CA     . ILE   A 1  93  ? 34.451  -85.766  -43.398  1.00 50.43  ? 93  ILE   A CA     1 
ATOM   715   C  C      . ILE   A 1  93  ? 33.556  -84.572  -43.064  1.00 56.10  ? 93  ILE   A C      1 
ATOM   716   O  O      . ILE   A 1  93  ? 32.929  -83.986  -43.954  1.00 57.76  ? 93  ILE   A O      1 
ATOM   717   C  CB     . ILE   A 1  93  ? 35.603  -85.308  -44.310  1.00 49.68  ? 93  ILE   A CB     1 
ATOM   718   C  CG1    . ILE   A 1  93  ? 36.423  -86.487  -44.808  1.00 58.25  ? 93  ILE   A CG1    1 
ATOM   719   C  CG2    . ILE   A 1  93  ? 36.449  -84.212  -43.665  1.00 43.60  ? 93  ILE   A CG2    1 
ATOM   720   C  CD1    . ILE   A 1  93  ? 37.180  -86.155  -46.065  1.00 59.74  ? 93  ILE   A CD1    1 
ATOM   721   N  N      . THR   A 1  94  ? 33.544  -84.153  -41.797  1.00 58.73  ? 94  THR   A N      1 
ATOM   722   C  CA     . THR   A 1  94  ? 32.722  -83.023  -41.383  1.00 50.38  ? 94  THR   A CA     1 
ATOM   723   C  C      . THR   A 1  94  ? 33.548  -82.034  -40.575  1.00 54.04  ? 94  THR   A C      1 
ATOM   724   O  O      . THR   A 1  94  ? 34.438  -82.419  -39.813  1.00 54.59  ? 94  THR   A O      1 
ATOM   725   C  CB     . THR   A 1  94  ? 31.514  -83.493  -40.563  1.00 51.77  ? 94  THR   A CB     1 
ATOM   726   O  OG1    . THR   A 1  94  ? 30.914  -82.373  -39.915  1.00 58.48  ? 94  THR   A OG1    1 
ATOM   727   C  CG2    . THR   A 1  94  ? 31.949  -84.437  -39.499  1.00 55.38  ? 94  THR   A CG2    1 
ATOM   728   N  N      . GLY   A 1  95  ? 33.249  -80.747  -40.754  1.00 58.62  ? 95  GLY   A N      1 
ATOM   729   C  CA     . GLY   A 1  95  ? 33.782  -79.696  -39.908  1.00 48.88  ? 95  GLY   A CA     1 
ATOM   730   C  C      . GLY   A 1  95  ? 32.896  -79.453  -38.699  1.00 55.02  ? 95  GLY   A C      1 
ATOM   731   O  O      . GLY   A 1  95  ? 32.134  -80.319  -38.262  1.00 52.21  ? 95  GLY   A O      1 
ATOM   732   N  N      . LYS   A 1  96  ? 33.011  -78.253  -38.145  1.00 57.04  ? 96  LYS   A N      1 
ATOM   733   C  CA     . LYS   A 1  96  ? 32.218  -77.851  -36.988  1.00 61.45  ? 96  LYS   A CA     1 
ATOM   734   C  C      . LYS   A 1  96  ? 31.414  -76.586  -37.231  1.00 58.38  ? 96  LYS   A C      1 
ATOM   735   O  O      . LYS   A 1  96  ? 30.248  -76.520  -36.847  1.00 54.45  ? 96  LYS   A O      1 
ATOM   736   C  CB     . LYS   A 1  96  ? 33.125  -77.639  -35.756  1.00 68.04  ? 96  LYS   A CB     1 
ATOM   737   C  CG     . LYS   A 1  96  ? 32.623  -78.346  -34.495  1.00 79.86  ? 96  LYS   A CG     1 
ATOM   738   C  CD     . LYS   A 1  96  ? 33.319  -77.847  -33.217  1.00 80.05  ? 96  LYS   A CD     1 
ATOM   739   C  CE     . LYS   A 1  96  ? 32.615  -78.356  -31.928  1.00 80.97  ? 96  LYS   A CE     1 
ATOM   740   N  NZ     . LYS   A 1  96  ? 32.182  -79.795  -31.965  1.00 84.75  ? 96  LYS   A NZ     1 
ATOM   741   N  N      . GLU   A 1  97  ? 32.022  -75.589  -37.869  1.00 52.72  ? 97  GLU   A N      1 
ATOM   742   C  CA     . GLU   A 1  97  ? 31.417  -74.307  -38.177  1.00 51.85  ? 97  GLU   A CA     1 
ATOM   743   C  C      . GLU   A 1  97  ? 31.327  -74.197  -39.697  1.00 58.68  ? 97  GLU   A C      1 
ATOM   744   O  O      . GLU   A 1  97  ? 32.341  -74.392  -40.380  1.00 61.54  ? 97  GLU   A O      1 
ATOM   745   C  CB     . GLU   A 1  97  ? 32.284  -73.189  -37.591  1.00 52.68  ? 97  GLU   A CB     1 
ATOM   746   C  CG     . GLU   A 1  97  ? 31.537  -72.106  -36.864  1.00 55.29  ? 97  GLU   A CG     1 
ATOM   747   C  CD     . GLU   A 1  97  ? 32.410  -70.905  -36.588  1.00 63.74  ? 97  GLU   A CD     1 
ATOM   748   O  OE1    . GLU   A 1  97  ? 32.956  -70.331  -37.558  1.00 64.00  ? 97  GLU   A OE1    1 
ATOM   749   O  OE2    . GLU   A 1  97  ? 32.526  -70.508  -35.409  1.00 69.70  ? 97  GLU   A OE2    1 
ATOM   750   N  N      . ASP   A 1  98  ? 30.130  -73.898  -40.236  1.00 51.59  ? 98  ASP   A N      1 
ATOM   751   C  CA     . ASP   A 1  98  ? 29.963  -73.895  -41.688  1.00 46.10  ? 98  ASP   A CA     1 
ATOM   752   C  C      . ASP   A 1  98  ? 30.318  -72.527  -42.278  1.00 42.39  ? 98  ASP   A C      1 
ATOM   753   O  O      . ASP   A 1  98  ? 30.754  -71.613  -41.581  1.00 45.59  ? 98  ASP   A O      1 
ATOM   754   C  CB     . ASP   A 1  98  ? 28.554  -74.351  -42.088  1.00 42.66  ? 98  ASP   A CB     1 
ATOM   755   C  CG     . ASP   A 1  98  ? 27.480  -73.284  -41.889  1.00 42.45  ? 98  ASP   A CG     1 
ATOM   756   O  OD1    . ASP   A 1  98  ? 27.743  -72.082  -42.099  1.00 45.01  ? 98  ASP   A OD1    1 
ATOM   757   O  OD2    . ASP   A 1  98  ? 26.329  -73.663  -41.601  1.00 41.54  ? 98  ASP   A OD2    1 
ATOM   758   N  N      . ALA   A 1  99  ? 30.165  -72.388  -43.591  1.00 39.91  ? 99  ALA   A N      1 
ATOM   759   C  CA     . ALA   A 1  99  ? 30.640  -71.197  -44.288  1.00 41.60  ? 99  ALA   A CA     1 
ATOM   760   C  C      . ALA   A 1  99  ? 29.647  -70.042  -44.252  1.00 42.65  ? 99  ALA   A C      1 
ATOM   761   O  O      . ALA   A 1  99  ? 29.893  -69.026  -44.909  1.00 44.96  ? 99  ALA   A O      1 
ATOM   762   C  CB     . ALA   A 1  99  ? 30.989  -71.514  -45.754  1.00 30.63  ? 99  ALA   A CB     1 
ATOM   763   N  N      . ALA   A 1  100 ? 28.525  -70.179  -43.548  1.00 34.55  ? 100 ALA   A N      1 
ATOM   764   C  CA     . ALA   A 1  100 ? 27.526  -69.114  -43.453  1.00 40.76  ? 100 ALA   A CA     1 
ATOM   765   C  C      . ALA   A 1  100 ? 27.232  -68.466  -44.812  1.00 37.36  ? 100 ALA   A C      1 
ATOM   766   O  O      . ALA   A 1  100 ? 27.226  -67.245  -44.956  1.00 41.63  ? 100 ALA   A O      1 
ATOM   767   C  CB     . ALA   A 1  100 ? 27.955  -68.056  -42.417  1.00 33.87  ? 100 ALA   A CB     1 
ATOM   768   N  N      . ASN   A 1  101 ? 26.969  -69.297  -45.821  1.00 36.08  ? 101 ASN   A N      1 
ATOM   769   C  CA     . ASN   A 1  101 ? 26.609  -68.829  -47.170  1.00 40.14  ? 101 ASN   A CA     1 
ATOM   770   C  C      . ASN   A 1  101 ? 27.608  -67.826  -47.722  1.00 42.39  ? 101 ASN   A C      1 
ATOM   771   O  O      . ASN   A 1  101 ? 27.247  -66.960  -48.514  1.00 42.88  ? 101 ASN   A O      1 
ATOM   772   C  CB     . ASN   A 1  101 ? 25.223  -68.185  -47.229  1.00 42.24  ? 101 ASN   A CB     1 
ATOM   773   C  CG     . ASN   A 1  101 ? 24.189  -68.942  -46.459  1.00 39.65  ? 101 ASN   A CG     1 
ATOM   774   O  OD1    . ASN   A 1  101 ? 23.209  -68.357  -46.012  1.00 42.19  ? 101 ASN   A OD1    1 
ATOM   775   N  ND2    . ASN   A 1  101 ? 24.390  -70.246  -46.296  1.00 43.11  ? 101 ASN   A ND2    1 
ATOM   776   N  N      . ASN   A 1  102 ? 28.863  -67.952  -47.328  1.00 44.67  ? 102 ASN   A N      1 
ATOM   777   C  CA     . ASN   A 1  102 ? 29.904  -66.975  -47.614  1.00 41.14  ? 102 ASN   A CA     1 
ATOM   778   C  C      . ASN   A 1  102 ? 30.960  -67.690  -48.438  1.00 45.26  ? 102 ASN   A C      1 
ATOM   779   O  O      . ASN   A 1  102 ? 31.734  -68.485  -47.895  1.00 49.01  ? 102 ASN   A O      1 
ATOM   780   C  CB     . ASN   A 1  102 ? 30.493  -66.436  -46.304  1.00 45.84  ? 102 ASN   A CB     1 
ATOM   781   C  CG     . ASN   A 1  102 ? 31.250  -65.138  -46.482  1.00 45.58  ? 102 ASN   A CG     1 
ATOM   782   O  OD1    . ASN   A 1  102 ? 31.646  -64.773  -47.590  1.00 41.47  ? 102 ASN   A OD1    1 
ATOM   783   N  ND2    . ASN   A 1  102 ? 31.447  -64.427  -45.381  1.00 44.68  ? 102 ASN   A ND2    1 
ATOM   784   N  N      . TYR   A 1  103 ? 30.998  -67.420  -49.742  1.00 44.59  ? 103 TYR   A N      1 
ATOM   785   C  CA     . TYR   A 1  103 ? 32.053  -68.000  -50.573  1.00 46.33  ? 103 TYR   A CA     1 
ATOM   786   C  C      . TYR   A 1  103 ? 33.433  -67.874  -49.917  1.00 45.46  ? 103 TYR   A C      1 
ATOM   787   O  O      . TYR   A 1  103 ? 34.164  -68.862  -49.790  1.00 42.81  ? 103 TYR   A O      1 
ATOM   788   C  CB     . TYR   A 1  103 ? 32.058  -67.340  -51.952  1.00 46.24  ? 103 TYR   A CB     1 
ATOM   789   C  CG     . TYR   A 1  103 ? 33.223  -67.797  -52.807  1.00 51.27  ? 103 TYR   A CG     1 
ATOM   790   C  CD1    . TYR   A 1  103 ? 33.263  -69.087  -53.335  1.00 45.76  ? 103 TYR   A CD1    1 
ATOM   791   C  CD2    . TYR   A 1  103 ? 34.281  -66.949  -53.078  1.00 50.19  ? 103 TYR   A CD2    1 
ATOM   792   C  CE1    . TYR   A 1  103 ? 34.325  -69.510  -54.116  1.00 49.22  ? 103 TYR   A CE1    1 
ATOM   793   C  CE2    . TYR   A 1  103 ? 35.344  -67.363  -53.862  1.00 53.54  ? 103 TYR   A CE2    1 
ATOM   794   C  CZ     . TYR   A 1  103 ? 35.367  -68.641  -54.379  1.00 52.17  ? 103 TYR   A CZ     1 
ATOM   795   O  OH     . TYR   A 1  103 ? 36.439  -69.030  -55.157  1.00 49.00  ? 103 TYR   A OH     1 
ATOM   796   N  N      . ALA   A 1  104 ? 33.797  -66.652  -49.490  1.00 51.97  ? 104 ALA   A N      1 
ATOM   797   C  CA     . ALA   A 1  104 ? 35.112  -66.378  -48.898  1.00 44.06  ? 104 ALA   A CA     1 
ATOM   798   C  C      . ALA   A 1  104 ? 35.340  -67.140  -47.607  1.00 42.82  ? 104 ALA   A C      1 
ATOM   799   O  O      . ALA   A 1  104 ? 36.473  -67.532  -47.326  1.00 47.13  ? 104 ALA   A O      1 
ATOM   800   C  CB     . ALA   A 1  104 ? 35.291  -64.881  -48.638  1.00 43.51  ? 104 ALA   A CB     1 
ATOM   801   N  N      . ARG   A 1  105 ? 34.297  -67.363  -46.806  1.00 46.54  ? 105 ARG   A N      1 
ATOM   802   C  CA     . ARG   A 1  105 ? 34.495  -68.114  -45.569  1.00 46.18  ? 105 ARG   A CA     1 
ATOM   803   C  C      . ARG   A 1  105 ? 34.779  -69.588  -45.851  1.00 44.17  ? 105 ARG   A C      1 
ATOM   804   O  O      . ARG   A 1  105 ? 35.629  -70.199  -45.195  1.00 45.57  ? 105 ARG   A O      1 
ATOM   805   C  CB     . ARG   A 1  105 ? 33.282  -67.944  -44.662  1.00 49.55  ? 105 ARG   A CB     1 
ATOM   806   C  CG     . ARG   A 1  105 ? 33.369  -68.647  -43.305  1.00 46.72  ? 105 ARG   A CG     1 
ATOM   807   C  CD     . ARG   A 1  105 ? 32.127  -68.300  -42.489  1.00 40.17  ? 105 ARG   A CD     1 
ATOM   808   N  NE     . ARG   A 1  105 ? 32.292  -68.588  -41.074  1.00 49.21  ? 105 ARG   A NE     1 
ATOM   809   C  CZ     . ARG   A 1  105 ? 32.882  -67.776  -40.207  1.00 50.47  ? 105 ARG   A CZ     1 
ATOM   810   N  NH1    . ARG   A 1  105 ? 33.407  -66.616  -40.585  1.00 41.72  ? 105 ARG   A NH1    1 
ATOM   811   N  NH2    . ARG   A 1  105 ? 32.937  -68.130  -38.926  1.00 52.05  ? 105 ARG   A NH2    1 
ATOM   812   N  N      . GLY   A 1  106 ? 34.104  -70.170  -46.839  1.00 47.38  ? 106 GLY   A N      1 
ATOM   813   C  CA     . GLY   A 1  106 ? 34.375  -71.556  -47.189  1.00 44.11  ? 106 GLY   A CA     1 
ATOM   814   C  C      . GLY   A 1  106 ? 35.678  -71.752  -47.937  1.00 46.71  ? 106 GLY   A C      1 
ATOM   815   O  O      . GLY   A 1  106 ? 36.319  -72.806  -47.802  1.00 43.99  ? 106 GLY   A O      1 
ATOM   816   N  N      . HIS   A 1  107 ? 36.087  -70.757  -48.733  1.00 40.93  ? 107 HIS   A N      1 
ATOM   817   C  CA     . HIS   A 1  107 ? 37.301  -70.899  -49.531  1.00 45.35  ? 107 HIS   A CA     1 
ATOM   818   C  C      . HIS   A 1  107 ? 38.546  -70.576  -48.718  1.00 52.43  ? 107 HIS   A C      1 
ATOM   819   O  O      . HIS   A 1  107 ? 39.436  -71.421  -48.554  1.00 55.66  ? 107 HIS   A O      1 
ATOM   820   C  CB     . HIS   A 1  107 ? 37.238  -70.003  -50.771  1.00 48.60  ? 107 HIS   A CB     1 
ATOM   821   C  CG     . HIS   A 1  107 ? 38.396  -70.194  -51.713  1.00 53.86  ? 107 HIS   A CG     1 
ATOM   822   N  ND1    . HIS   A 1  107 ? 38.404  -71.167  -52.693  1.00 54.01  ? 107 HIS   A ND1    1 
ATOM   823   C  CD2    . HIS   A 1  107 ? 39.563  -69.519  -51.850  1.00 51.79  ? 107 HIS   A CD2    1 
ATOM   824   C  CE1    . HIS   A 1  107 ? 39.531  -71.095  -53.378  1.00 54.08  ? 107 HIS   A CE1    1 
ATOM   825   N  NE2    . HIS   A 1  107 ? 40.248  -70.097  -52.895  1.00 54.11  ? 107 HIS   A NE2    1 
ATOM   826   N  N      . TYR   A 1  108 ? 38.612  -69.351  -48.195  1.00 53.32  ? 108 TYR   A N      1 
ATOM   827   C  CA     . TYR   A 1  108 ? 39.776  -68.835  -47.493  1.00 37.80  ? 108 TYR   A CA     1 
ATOM   828   C  C      . TYR   A 1  108 ? 39.769  -69.202  -46.016  1.00 48.14  ? 108 TYR   A C      1 
ATOM   829   O  O      . TYR   A 1  108 ? 40.615  -69.968  -45.555  1.00 56.42  ? 108 TYR   A O      1 
ATOM   830   C  CB     . TYR   A 1  108 ? 39.835  -67.331  -47.677  1.00 38.57  ? 108 TYR   A CB     1 
ATOM   831   C  CG     . TYR   A 1  108 ? 40.017  -66.892  -49.105  1.00 40.96  ? 108 TYR   A CG     1 
ATOM   832   C  CD1    . TYR   A 1  108 ? 41.271  -66.874  -49.691  1.00 43.34  ? 108 TYR   A CD1    1 
ATOM   833   C  CD2    . TYR   A 1  108 ? 38.939  -66.492  -49.868  1.00 45.30  ? 108 TYR   A CD2    1 
ATOM   834   C  CE1    . TYR   A 1  108 ? 41.450  -66.467  -50.992  1.00 44.50  ? 108 TYR   A CE1    1 
ATOM   835   C  CE2    . TYR   A 1  108 ? 39.108  -66.075  -51.200  1.00 47.67  ? 108 TYR   A CE2    1 
ATOM   836   C  CZ     . TYR   A 1  108 ? 40.371  -66.076  -51.744  1.00 44.81  ? 108 TYR   A CZ     1 
ATOM   837   O  OH     . TYR   A 1  108 ? 40.569  -65.665  -53.027  1.00 44.52  ? 108 TYR   A OH     1 
ATOM   838   N  N      . THR   A 1  109 ? 38.815  -68.691  -45.257  1.00 52.43  ? 109 THR   A N      1 
ATOM   839   C  CA     . THR   A 1  109 ? 38.948  -68.850  -43.815  1.00 52.43  ? 109 THR   A CA     1 
ATOM   840   C  C      . THR   A 1  109 ? 38.847  -70.316  -43.405  1.00 55.29  ? 109 THR   A C      1 
ATOM   841   O  O      . THR   A 1  109 ? 39.850  -70.911  -43.007  1.00 60.65  ? 109 THR   A O      1 
ATOM   842   C  CB     . THR   A 1  109 ? 37.919  -68.003  -43.084  1.00 45.79  ? 109 THR   A CB     1 
ATOM   843   O  OG1    . THR   A 1  109 ? 37.881  -66.705  -43.675  1.00 47.21  ? 109 THR   A OG1    1 
ATOM   844   C  CG2    . THR   A 1  109 ? 38.337  -67.853  -41.678  1.00 55.01  ? 109 THR   A CG2    1 
ATOM   845   N  N      . ILE   A 1  110 ? 37.662  -70.921  -43.518  1.00 52.94  ? 110 ILE   A N      1 
ATOM   846   C  CA     . ILE   A 1  110 ? 37.491  -72.319  -43.114  1.00 57.04  ? 110 ILE   A CA     1 
ATOM   847   C  C      . ILE   A 1  110 ? 38.041  -73.322  -44.140  1.00 61.79  ? 110 ILE   A C      1 
ATOM   848   O  O      . ILE   A 1  110 ? 38.313  -74.479  -43.787  1.00 60.94  ? 110 ILE   A O      1 
ATOM   849   C  CB     . ILE   A 1  110 ? 36.008  -72.568  -42.834  1.00 50.23  ? 110 ILE   A CB     1 
ATOM   850   C  CG1    . ILE   A 1  110 ? 35.527  -71.558  -41.768  1.00 55.77  ? 110 ILE   A CG1    1 
ATOM   851   C  CG2    . ILE   A 1  110 ? 35.805  -74.005  -42.462  1.00 49.25  ? 110 ILE   A CG2    1 
ATOM   852   C  CD1    . ILE   A 1  110 ? 34.201  -71.892  -41.084  1.00 51.14  ? 110 ILE   A CD1    1 
ATOM   853   N  N      . GLY   A 1  111 ? 38.226  -72.911  -45.399  1.00 57.73  ? 111 GLY   A N      1 
ATOM   854   C  CA     . GLY   A 1  111 ? 38.743  -73.829  -46.394  1.00 51.52  ? 111 GLY   A CA     1 
ATOM   855   C  C      . GLY   A 1  111 ? 40.165  -74.247  -46.099  1.00 58.97  ? 111 GLY   A C      1 
ATOM   856   O  O      . GLY   A 1  111 ? 40.519  -75.421  -46.241  1.00 60.11  ? 111 GLY   A O      1 
ATOM   857   N  N      . LYS   A 1  112 ? 40.997  -73.297  -45.667  1.00 61.13  ? 112 LYS   A N      1 
ATOM   858   C  CA     . LYS   A 1  112 ? 42.420  -73.564  -45.487  1.00 55.51  ? 112 LYS   A CA     1 
ATOM   859   C  C      . LYS   A 1  112 ? 42.700  -74.586  -44.389  1.00 57.57  ? 112 LYS   A C      1 
ATOM   860   O  O      . LYS   A 1  112 ? 43.746  -75.241  -44.421  1.00 62.05  ? 112 LYS   A O      1 
ATOM   861   C  CB     . LYS   A 1  112 ? 43.147  -72.255  -45.199  1.00 49.69  ? 112 LYS   A CB     1 
ATOM   862   C  CG     . LYS   A 1  112 ? 44.666  -72.336  -45.228  1.00 65.40  ? 112 LYS   A CG     1 
ATOM   863   C  CD     . LYS   A 1  112 ? 45.290  -71.133  -44.511  1.00 70.32  ? 112 LYS   A CD     1 
ATOM   864   C  CE     . LYS   A 1  112 ? 46.439  -70.525  -45.317  1.00 79.01  ? 112 LYS   A CE     1 
ATOM   865   N  NZ     . LYS   A 1  112 ? 46.023  -69.409  -46.238  1.00 72.77  ? 112 LYS   A NZ     1 
ATOM   866   N  N      . GLU   A 1  113 ? 41.796  -74.766  -43.434  1.00 57.54  ? 113 GLU   A N      1 
ATOM   867   C  CA     . GLU   A 1  113 ? 42.072  -75.647  -42.309  1.00 56.62  ? 113 GLU   A CA     1 
ATOM   868   C  C      . GLU   A 1  113 ? 41.575  -77.051  -42.545  1.00 53.59  ? 113 GLU   A C      1 
ATOM   869   O  O      . GLU   A 1  113 ? 41.668  -77.893  -41.645  1.00 49.77  ? 113 GLU   A O      1 
ATOM   870   C  CB     . GLU   A 1  113 ? 41.442  -75.103  -41.012  1.00 60.39  ? 113 GLU   A CB     1 
ATOM   871   C  CG     . GLU   A 1  113 ? 41.381  -73.581  -40.916  1.00 65.93  ? 113 GLU   A CG     1 
ATOM   872   C  CD     . GLU   A 1  113 ? 40.300  -73.076  -39.943  1.00 83.31  ? 113 GLU   A CD     1 
ATOM   873   O  OE1    . GLU   A 1  113 ? 40.179  -71.838  -39.788  1.00 87.95  ? 113 GLU   A OE1    1 
ATOM   874   O  OE2    . GLU   A 1  113 ? 39.572  -73.903  -39.334  1.00 82.76  ? 113 GLU   A OE2    1 
ATOM   875   N  N      . ILE   A 1  114 ? 41.013  -77.325  -43.708  1.00 54.37  ? 114 ILE   A N      1 
ATOM   876   C  CA     . ILE   A 1  114 ? 40.486  -78.665  -43.921  1.00 59.67  ? 114 ILE   A CA     1 
ATOM   877   C  C      . ILE   A 1  114 ? 40.905  -79.152  -45.306  1.00 55.26  ? 114 ILE   A C      1 
ATOM   878   O  O      . ILE   A 1  114 ? 40.838  -80.349  -45.594  1.00 55.83  ? 114 ILE   A O      1 
ATOM   879   C  CB     . ILE   A 1  114 ? 38.957  -78.699  -43.692  1.00 54.16  ? 114 ILE   A CB     1 
ATOM   880   C  CG1    . ILE   A 1  114 ? 38.491  -80.097  -43.287  1.00 51.66  ? 114 ILE   A CG1    1 
ATOM   881   C  CG2    . ILE   A 1  114 ? 38.179  -78.172  -44.896  1.00 53.45  ? 114 ILE   A CG2    1 
ATOM   882   C  CD1    . ILE   A 1  114 ? 37.094  -80.114  -42.665  1.00 46.19  ? 114 ILE   A CD1    1 
ATOM   883   N  N      . ILE   A 1  115 ? 41.413  -78.244  -46.148  1.00 49.28  ? 115 ILE   A N      1 
ATOM   884   C  CA     . ILE   A 1  115 ? 41.781  -78.644  -47.506  1.00 59.52  ? 115 ILE   A CA     1 
ATOM   885   C  C      . ILE   A 1  115 ? 42.821  -79.757  -47.480  1.00 62.81  ? 115 ILE   A C      1 
ATOM   886   O  O      . ILE   A 1  115 ? 42.831  -80.618  -48.365  1.00 65.82  ? 115 ILE   A O      1 
ATOM   887   C  CB     . ILE   A 1  115 ? 42.253  -77.433  -48.350  1.00 60.50  ? 115 ILE   A CB     1 
ATOM   888   C  CG1    . ILE   A 1  115 ? 42.604  -77.862  -49.780  1.00 58.15  ? 115 ILE   A CG1    1 
ATOM   889   C  CG2    . ILE   A 1  115 ? 43.440  -76.745  -47.723  1.00 56.81  ? 115 ILE   A CG2    1 
ATOM   890   C  CD1    . ILE   A 1  115 ? 41.419  -78.240  -50.618  1.00 51.87  ? 115 ILE   A CD1    1 
ATOM   891   N  N      . ASP   A 1  116 ? 43.685  -79.789  -46.460  1.00 63.61  ? 116 ASP   A N      1 
ATOM   892   C  CA     . ASP   A 1  116 ? 44.684  -80.854  -46.389  1.00 62.14  ? 116 ASP   A CA     1 
ATOM   893   C  C      . ASP   A 1  116 ? 44.076  -82.165  -45.903  1.00 57.49  ? 116 ASP   A C      1 
ATOM   894   O  O      . ASP   A 1  116 ? 44.308  -83.225  -46.494  1.00 61.04  ? 116 ASP   A O      1 
ATOM   895   C  CB     . ASP   A 1  116 ? 45.850  -80.433  -45.498  1.00 60.80  ? 116 ASP   A CB     1 
ATOM   896   C  CG     . ASP   A 1  116 ? 46.775  -79.442  -46.190  1.00 70.26  ? 116 ASP   A CG     1 
ATOM   897   O  OD1    . ASP   A 1  116 ? 46.700  -79.321  -47.444  1.00 62.33  ? 116 ASP   A OD1    1 
ATOM   898   O  OD2    . ASP   A 1  116 ? 47.574  -78.785  -45.482  1.00 73.19  ? 116 ASP   A OD2    1 
ATOM   899   N  N      . LEU   A 1  117 ? 43.288  -82.122  -44.837  1.00 57.63  ? 117 LEU   A N      1 
ATOM   900   C  CA     . LEU   A 1  117 ? 42.665  -83.352  -44.360  1.00 55.58  ? 117 LEU   A CA     1 
ATOM   901   C  C      . LEU   A 1  117 ? 41.836  -84.007  -45.463  1.00 63.92  ? 117 LEU   A C      1 
ATOM   902   O  O      . LEU   A 1  117 ? 41.783  -85.240  -45.565  1.00 61.47  ? 117 LEU   A O      1 
ATOM   903   C  CB     . LEU   A 1  117 ? 41.799  -83.049  -43.141  1.00 54.63  ? 117 LEU   A CB     1 
ATOM   904   C  CG     . LEU   A 1  117 ? 40.713  -84.057  -42.806  1.00 59.11  ? 117 LEU   A CG     1 
ATOM   905   C  CD1    . LEU   A 1  117 ? 41.363  -85.408  -42.653  1.00 65.66  ? 117 LEU   A CD1    1 
ATOM   906   C  CD2    . LEU   A 1  117 ? 39.990  -83.679  -41.538  1.00 54.39  ? 117 LEU   A CD2    1 
ATOM   907   N  N      . VAL   A 1  118 ? 41.194  -83.192  -46.309  1.00 67.94  ? 118 VAL   A N      1 
ATOM   908   C  CA     . VAL   A 1  118 ? 40.297  -83.719  -47.339  1.00 63.09  ? 118 VAL   A CA     1 
ATOM   909   C  C      . VAL   A 1  118 ? 41.102  -84.357  -48.468  1.00 62.43  ? 118 VAL   A C      1 
ATOM   910   O  O      . VAL   A 1  118 ? 40.884  -85.524  -48.812  1.00 60.86  ? 118 VAL   A O      1 
ATOM   911   C  CB     . VAL   A 1  118 ? 39.351  -82.612  -47.857  1.00 61.80  ? 118 VAL   A CB     1 
ATOM   912   C  CG1    . VAL   A 1  118 ? 38.799  -82.950  -49.243  1.00 59.29  ? 118 VAL   A CG1    1 
ATOM   913   C  CG2    . VAL   A 1  118 ? 38.199  -82.385  -46.868  1.00 51.72  ? 118 VAL   A CG2    1 
ATOM   914   N  N      . LEU   A 1  119 ? 42.056  -83.614  -49.049  1.00 60.47  ? 119 LEU   A N      1 
ATOM   915   C  CA     . LEU   A 1  119 ? 42.923  -84.194  -50.076  1.00 60.51  ? 119 LEU   A CA     1 
ATOM   916   C  C      . LEU   A 1  119 ? 43.656  -85.442  -49.585  1.00 63.11  ? 119 LEU   A C      1 
ATOM   917   O  O      . LEU   A 1  119 ? 44.179  -86.204  -50.407  1.00 65.79  ? 119 LEU   A O      1 
ATOM   918   C  CB     . LEU   A 1  119 ? 43.952  -83.176  -50.574  1.00 50.14  ? 119 LEU   A CB     1 
ATOM   919   C  CG     . LEU   A 1  119 ? 43.434  -81.936  -51.292  1.00 58.68  ? 119 LEU   A CG     1 
ATOM   920   C  CD1    . LEU   A 1  119 ? 44.499  -80.855  -51.262  1.00 61.53  ? 119 LEU   A CD1    1 
ATOM   921   C  CD2    . LEU   A 1  119 ? 43.037  -82.242  -52.707  1.00 56.55  ? 119 LEU   A CD2    1 
ATOM   922   N  N      . ASP   A 1  120 ? 43.708  -85.678  -48.274  1.00 59.98  ? 120 ASP   A N      1 
ATOM   923   C  CA     . ASP   A 1  120 ? 44.342  -86.897  -47.790  1.00 61.69  ? 120 ASP   A CA     1 
ATOM   924   C  C      . ASP   A 1  120 ? 43.379  -88.074  -47.795  1.00 57.92  ? 120 ASP   A C      1 
ATOM   925   O  O      . ASP   A 1  120 ? 43.742  -89.159  -48.239  1.00 69.71  ? 120 ASP   A O      1 
ATOM   926   C  CB     . ASP   A 1  120 ? 44.921  -86.685  -46.387  1.00 72.53  ? 120 ASP   A CB     1 
ATOM   927   C  CG     . ASP   A 1  120 ? 45.780  -87.858  -45.926  1.00 73.98  ? 120 ASP   A CG     1 
ATOM   928   O  OD1    . ASP   A 1  120 ? 46.950  -87.946  -46.371  1.00 80.92  ? 120 ASP   A OD1    1 
ATOM   929   O  OD2    . ASP   A 1  120 ? 45.283  -88.685  -45.124  1.00 64.88  ? 120 ASP   A OD2    1 
ATOM   930   N  N      . ARG   A 1  121 ? 42.157  -87.903  -47.297  1.00 62.52  ? 121 ARG   A N      1 
ATOM   931   C  CA     . ARG   A 1  121 ? 41.189  -88.991  -47.416  1.00 65.21  ? 121 ARG   A CA     1 
ATOM   932   C  C      . ARG   A 1  121 ? 40.853  -89.265  -48.882  1.00 64.34  ? 121 ARG   A C      1 
ATOM   933   O  O      . ARG   A 1  121 ? 40.506  -90.396  -49.251  1.00 59.16  ? 121 ARG   A O      1 
ATOM   934   C  CB     . ARG   A 1  121 ? 39.931  -88.661  -46.606  1.00 61.19  ? 121 ARG   A CB     1 
ATOM   935   C  CG     . ARG   A 1  121 ? 40.214  -88.003  -45.258  1.00 62.15  ? 121 ARG   A CG     1 
ATOM   936   C  CD     . ARG   A 1  121 ? 40.723  -88.974  -44.211  1.00 58.33  ? 121 ARG   A CD     1 
ATOM   937   N  NE     . ARG   A 1  121 ? 39.623  -89.395  -43.350  1.00 67.74  ? 121 ARG   A NE     1 
ATOM   938   C  CZ     . ARG   A 1  121 ? 39.339  -88.876  -42.160  1.00 68.57  ? 121 ARG   A CZ     1 
ATOM   939   N  NH1    . ARG   A 1  121 ? 40.107  -87.955  -41.601  1.00 64.40  ? 121 ARG   A NH1    1 
ATOM   940   N  NH2    . ARG   A 1  121 ? 38.247  -89.284  -41.518  1.00 76.91  ? 121 ARG   A NH2    1 
ATOM   941   N  N      . ILE   A 1  122 ? 40.972  -88.250  -49.735  1.00 64.72  ? 122 ILE   A N      1 
ATOM   942   C  CA     . ILE   A 1  122 ? 40.810  -88.464  -51.166  1.00 61.47  ? 122 ILE   A CA     1 
ATOM   943   C  C      . ILE   A 1  122 ? 41.933  -89.347  -51.708  1.00 66.95  ? 122 ILE   A C      1 
ATOM   944   O  O      . ILE   A 1  122 ? 41.682  -90.341  -52.400  1.00 68.67  ? 122 ILE   A O      1 
ATOM   945   C  CB     . ILE   A 1  122 ? 40.742  -87.116  -51.893  1.00 55.06  ? 122 ILE   A CB     1 
ATOM   946   C  CG1    . ILE   A 1  122 ? 39.311  -86.574  -51.850  1.00 52.29  ? 122 ILE   A CG1    1 
ATOM   947   C  CG2    . ILE   A 1  122 ? 41.290  -87.257  -53.298  1.00 58.23  ? 122 ILE   A CG2    1 
ATOM   948   C  CD1    . ILE   A 1  122 ? 39.143  -85.213  -52.525  1.00 47.32  ? 122 ILE   A CD1    1 
ATOM   949   N  N      . ARG   A 1  123 ? 43.190  -89.012  -51.393  1.00 67.27  ? 123 ARG   A N      1 
ATOM   950   C  CA     . ARG   A 1  123 ? 44.300  -89.838  -51.865  1.00 66.19  ? 123 ARG   A CA     1 
ATOM   951   C  C      . ARG   A 1  123 ? 44.270  -91.241  -51.254  1.00 64.86  ? 123 ARG   A C      1 
ATOM   952   O  O      . ARG   A 1  123 ? 44.765  -92.196  -51.868  1.00 62.10  ? 123 ARG   A O      1 
ATOM   953   C  CB     . ARG   A 1  123 ? 45.631  -89.152  -51.573  1.00 64.57  ? 123 ARG   A CB     1 
ATOM   954   C  CG     . ARG   A 1  123 ? 46.810  -90.099  -51.532  1.00 66.82  ? 123 ARG   A CG     1 
ATOM   955   C  CD     . ARG   A 1  123 ? 47.596  -90.044  -52.821  1.00 71.26  ? 123 ARG   A CD     1 
ATOM   956   N  NE     . ARG   A 1  123 ? 47.872  -88.672  -53.238  1.00 72.45  ? 123 ARG   A NE     1 
ATOM   957   C  CZ     . ARG   A 1  123 ? 47.913  -88.272  -54.504  1.00 75.08  ? 123 ARG   A CZ     1 
ATOM   958   N  NH1    . ARG   A 1  123 ? 47.709  -89.117  -55.502  1.00 69.93  ? 123 ARG   A NH1    1 
ATOM   959   N  NH2    . ARG   A 1  123 ? 48.159  -86.989  -54.777  1.00 74.68  ? 123 ARG   A NH2    1 
ATOM   960   N  N      . LYS   A 1  124 ? 43.687  -91.399  -50.066  1.00 61.51  ? 124 LYS   A N      1 
ATOM   961   C  CA     . LYS   A 1  124 ? 43.544  -92.743  -49.519  1.00 60.61  ? 124 LYS   A CA     1 
ATOM   962   C  C      . LYS   A 1  124 ? 42.687  -93.608  -50.431  1.00 69.59  ? 124 LYS   A C      1 
ATOM   963   O  O      . LYS   A 1  124 ? 42.875  -94.831  -50.493  1.00 70.21  ? 124 LYS   A O      1 
ATOM   964   C  CB     . LYS   A 1  124 ? 42.953  -92.695  -48.106  1.00 61.80  ? 124 LYS   A CB     1 
ATOM   965   C  CG     . LYS   A 1  124 ? 43.989  -92.654  -46.957  1.00 74.76  ? 124 LYS   A CG     1 
ATOM   966   C  CD     . LYS   A 1  124 ? 44.979  -91.472  -47.061  1.00 70.87  ? 124 LYS   A CD     1 
ATOM   967   C  CE     . LYS   A 1  124 ? 46.272  -91.718  -46.263  1.00 70.57  ? 124 LYS   A CE     1 
ATOM   968   N  NZ     . LYS   A 1  124 ? 46.012  -92.268  -44.892  1.00 66.96  ? 124 LYS   A NZ     1 
ATOM   969   N  N      . LEU   A 1  125 ? 41.749  -92.983  -51.158  1.00 71.97  ? 125 LEU   A N      1 
ATOM   970   C  CA     . LEU   A 1  125 ? 40.909  -93.701  -52.110  1.00 65.16  ? 125 LEU   A CA     1 
ATOM   971   C  C      . LEU   A 1  125 ? 41.615  -93.869  -53.455  1.00 60.77  ? 125 LEU   A C      1 
ATOM   972   O  O      . LEU   A 1  125 ? 41.580  -94.956  -54.041  1.00 65.98  ? 125 LEU   A O      1 
ATOM   973   C  CB     . LEU   A 1  125 ? 39.564  -92.980  -52.262  1.00 58.61  ? 125 LEU   A CB     1 
ATOM   974   C  CG     . LEU   A 1  125 ? 38.353  -93.721  -51.679  1.00 61.42  ? 125 LEU   A CG     1 
ATOM   975   C  CD1    . LEU   A 1  125 ? 38.576  -94.087  -50.227  1.00 64.99  ? 125 LEU   A CD1    1 
ATOM   976   C  CD2    . LEU   A 1  125 ? 37.096  -92.887  -51.811  1.00 58.53  ? 125 LEU   A CD2    1 
ATOM   977   N  N      . ALA   A 1  126 ? 42.291  -92.826  -53.938  1.00 54.22  ? 126 ALA   A N      1 
ATOM   978   C  CA     . ALA   A 1  126 ? 43.064  -92.944  -55.167  1.00 62.29  ? 126 ALA   A CA     1 
ATOM   979   C  C      . ALA   A 1  126 ? 44.095  -94.069  -55.105  1.00 67.44  ? 126 ALA   A C      1 
ATOM   980   O  O      . ALA   A 1  126 ? 44.503  -94.584  -56.154  1.00 65.56  ? 126 ALA   A O      1 
ATOM   981   C  CB     . ALA   A 1  126 ? 43.757  -91.616  -55.486  1.00 62.74  ? 126 ALA   A CB     1 
ATOM   982   N  N      . ASP   A 1  127 ? 44.508  -94.478  -53.905  1.00 71.89  ? 127 ASP   A N      1 
ATOM   983   C  CA     . ASP   A 1  127 ? 45.517  -95.520  -53.762  1.00 66.92  ? 127 ASP   A CA     1 
ATOM   984   C  C      . ASP   A 1  127 ? 44.949  -96.936  -53.867  1.00 62.83  ? 127 ASP   A C      1 
ATOM   985   O  O      . ASP   A 1  127 ? 45.728  -97.873  -54.059  1.00 61.66  ? 127 ASP   A O      1 
ATOM   986   C  CB     . ASP   A 1  127 ? 46.260  -95.343  -52.430  1.00 64.36  ? 127 ASP   A CB     1 
ATOM   987   C  CG     . ASP   A 1  127 ? 47.318  -94.247  -52.488  1.00 61.30  ? 127 ASP   A CG     1 
ATOM   988   O  OD1    . ASP   A 1  127 ? 47.564  -93.680  -53.575  1.00 61.03  ? 127 ASP   A OD1    1 
ATOM   989   O  OD2    . ASP   A 1  127 ? 47.904  -93.950  -51.433  1.00 67.39  ? 127 ASP   A OD2    1 
ATOM   990   N  N      . GLN   A 1  128 ? 43.631  -97.124  -53.737  1.00 59.85  ? 128 GLN   A N      1 
ATOM   991   C  CA     . GLN   A 1  128 ? 43.007  -98.409  -54.030  1.00 66.39  ? 128 GLN   A CA     1 
ATOM   992   C  C      . GLN   A 1  128 ? 42.551  -98.507  -55.482  1.00 66.33  ? 128 GLN   A C      1 
ATOM   993   O  O      . GLN   A 1  128 ? 41.743  -99.381  -55.818  1.00 63.58  ? 128 GLN   A O      1 
ATOM   994   C  CB     . GLN   A 1  128 ? 41.825  -98.673  -53.090  1.00 67.25  ? 128 GLN   A CB     1 
ATOM   995   C  CG     . GLN   A 1  128 ? 42.028  -98.189  -51.659  1.00 73.41  ? 128 GLN   A CG     1 
ATOM   996   C  CD     . GLN   A 1  128 ? 40.705  -97.971  -50.906  1.00 77.81  ? 128 GLN   A CD     1 
ATOM   997   O  OE1    . GLN   A 1  128 ? 39.620  -98.284  -51.423  1.00 78.93  ? 128 GLN   A OE1    1 
ATOM   998   N  NE2    . GLN   A 1  128 ? 40.791  -97.410  -49.691  1.00 66.03  ? 128 GLN   A NE2    1 
ATOM   999   N  N      . CYS   A 1  129 ? 43.056  -97.632  -56.344  1.00 63.60  ? 129 CYS   A N      1 
ATOM   1000  C  CA     . CYS   A 1  129 ? 42.631  -97.540  -57.731  1.00 65.70  ? 129 CYS   A CA     1 
ATOM   1001  C  C      . CYS   A 1  129 ? 43.793  -97.874  -58.649  1.00 69.50  ? 129 CYS   A C      1 
ATOM   1002  O  O      . CYS   A 1  129 ? 44.848  -97.231  -58.589  1.00 68.71  ? 129 CYS   A O      1 
ATOM   1003  C  CB     . CYS   A 1  129 ? 42.107  -96.139  -58.070  1.00 69.67  ? 129 CYS   A CB     1 
ATOM   1004  S  SG     . CYS   A 1  129 ? 40.610  -95.650  -57.206  1.00 71.76  ? 129 CYS   A SG     1 
ATOM   1005  N  N      . THR   A 1  130 ? 43.566  -98.844  -59.530  1.00 70.82  ? 130 THR   A N      1 
ATOM   1006  C  CA     . THR   A 1  130 ? 44.583  -99.294  -60.467  1.00 60.69  ? 130 THR   A CA     1 
ATOM   1007  C  C      . THR   A 1  130 ? 44.771  -98.311  -61.614  1.00 64.30  ? 130 THR   A C      1 
ATOM   1008  O  O      . THR   A 1  130 ? 45.901  -98.094  -62.062  1.00 67.21  ? 130 THR   A O      1 
ATOM   1009  C  CB     . THR   A 1  130 ? 44.188  -100.665 -60.984  1.00 65.65  ? 130 THR   A CB     1 
ATOM   1010  O  OG1    . THR   A 1  130 ? 43.027  -100.525 -61.819  1.00 73.54  ? 130 THR   A OG1    1 
ATOM   1011  C  CG2    . THR   A 1  130 ? 43.842  -101.576 -59.805  1.00 53.18  ? 130 THR   A CG2    1 
ATOM   1012  N  N      . GLY   A 1  131 ? 43.684  -97.712  -62.108  1.00 67.06  ? 131 GLY   A N      1 
ATOM   1013  C  CA     . GLY   A 1  131 ? 43.786  -96.741  -63.186  1.00 64.37  ? 131 GLY   A CA     1 
ATOM   1014  C  C      . GLY   A 1  131 ? 42.758  -95.628  -63.118  1.00 69.19  ? 131 GLY   A C      1 
ATOM   1015  O  O      . GLY   A 1  131 ? 41.895  -95.517  -63.996  1.00 70.62  ? 131 GLY   A O      1 
ATOM   1016  N  N      . LEU   A 1  132 ? 42.862  -94.792  -62.085  1.00 66.84  ? 132 LEU   A N      1 
ATOM   1017  C  CA     . LEU   A 1  132 ? 41.916  -93.712  -61.821  1.00 57.67  ? 132 LEU   A CA     1 
ATOM   1018  C  C      . LEU   A 1  132 ? 41.646  -92.832  -63.040  1.00 62.93  ? 132 LEU   A C      1 
ATOM   1019  O  O      . LEU   A 1  132 ? 42.564  -92.235  -63.616  1.00 59.07  ? 132 LEU   A O      1 
ATOM   1020  C  CB     . LEU   A 1  132 ? 42.450  -92.848  -60.686  1.00 61.83  ? 132 LEU   A CB     1 
ATOM   1021  C  CG     . LEU   A 1  132 ? 41.566  -91.685  -60.248  1.00 60.74  ? 132 LEU   A CG     1 
ATOM   1022  C  CD1    . LEU   A 1  132 ? 40.434  -92.191  -59.340  1.00 52.81  ? 132 LEU   A CD1    1 
ATOM   1023  C  CD2    . LEU   A 1  132 ? 42.409  -90.595  -59.591  1.00 56.02  ? 132 LEU   A CD2    1 
ATOM   1024  N  N      . GLN   A 1  133 ? 40.358  -92.712  -63.378  1.00 61.60  ? 133 GLN   A N      1 
ATOM   1025  C  CA     . GLN   A 1  133 ? 39.868  -91.817  -64.418  1.00 55.60  ? 133 GLN   A CA     1 
ATOM   1026  C  C      . GLN   A 1  133 ? 39.826  -90.369  -63.945  1.00 59.67  ? 133 GLN   A C      1 
ATOM   1027  O  O      . GLN   A 1  133 ? 40.210  -89.450  -64.682  1.00 58.51  ? 133 GLN   A O      1 
ATOM   1028  C  CB     . GLN   A 1  133 ? 38.456  -92.241  -64.814  1.00 60.84  ? 133 GLN   A CB     1 
ATOM   1029  C  CG     . GLN   A 1  133 ? 38.348  -93.131  -66.005  1.00 62.05  ? 133 GLN   A CG     1 
ATOM   1030  C  CD     . GLN   A 1  133 ? 36.980  -93.707  -66.095  1.00 59.97  ? 133 GLN   A CD     1 
ATOM   1031  O  OE1    . GLN   A 1  133 ? 36.042  -93.026  -66.507  1.00 63.31  ? 133 GLN   A OE1    1 
ATOM   1032  N  NE2    . GLN   A 1  133 ? 36.822  -94.935  -65.604  1.00 57.97  ? 133 GLN   A NE2    1 
ATOM   1033  N  N      . GLY   A 1  134 ? 39.295  -90.140  -62.749  1.00 57.58  ? 134 GLY   A N      1 
ATOM   1034  C  CA     . GLY   A 1  134 ? 39.061  -88.792  -62.280  1.00 55.93  ? 134 GLY   A CA     1 
ATOM   1035  C  C      . GLY   A 1  134 ? 37.845  -88.736  -61.379  1.00 53.58  ? 134 GLY   A C      1 
ATOM   1036  O  O      . GLY   A 1  134 ? 37.399  -89.751  -60.836  1.00 51.60  ? 134 GLY   A O      1 
ATOM   1037  N  N      . PHE   A 1  135 ? 37.316  -87.515  -61.253  1.00 55.86  ? 135 PHE   A N      1 
ATOM   1038  C  CA     . PHE   A 1  135 ? 36.407  -87.161  -60.167  1.00 53.20  ? 135 PHE   A CA     1 
ATOM   1039  C  C      . PHE   A 1  135 ? 35.091  -86.607  -60.683  1.00 49.19  ? 135 PHE   A C      1 
ATOM   1040  O  O      . PHE   A 1  135 ? 35.048  -85.869  -61.676  1.00 49.01  ? 135 PHE   A O      1 
ATOM   1041  C  CB     . PHE   A 1  135 ? 37.062  -86.140  -59.221  1.00 51.67  ? 135 PHE   A CB     1 
ATOM   1042  C  CG     . PHE   A 1  135 ? 38.435  -86.553  -58.756  1.00 50.57  ? 135 PHE   A CG     1 
ATOM   1043  C  CD1    . PHE   A 1  135 ? 38.593  -87.357  -57.633  1.00 51.51  ? 135 PHE   A CD1    1 
ATOM   1044  C  CD2    . PHE   A 1  135 ? 39.562  -86.191  -59.474  1.00 49.25  ? 135 PHE   A CD2    1 
ATOM   1045  C  CE1    . PHE   A 1  135 ? 39.857  -87.757  -57.227  1.00 52.01  ? 135 PHE   A CE1    1 
ATOM   1046  C  CE2    . PHE   A 1  135 ? 40.825  -86.597  -59.071  1.00 47.74  ? 135 PHE   A CE2    1 
ATOM   1047  C  CZ     . PHE   A 1  135 ? 40.970  -87.375  -57.950  1.00 47.57  ? 135 PHE   A CZ     1 
ATOM   1048  N  N      . LEU   A 1  136 ? 34.020  -86.993  -59.994  1.00 51.59  ? 136 LEU   A N      1 
ATOM   1049  C  CA     . LEU   A 1  136 ? 32.685  -86.424  -60.158  1.00 53.20  ? 136 LEU   A CA     1 
ATOM   1050  C  C      . LEU   A 1  136 ? 32.402  -85.616  -58.897  1.00 46.41  ? 136 LEU   A C      1 
ATOM   1051  O  O      . LEU   A 1  136 ? 32.308  -86.190  -57.803  1.00 46.23  ? 136 LEU   A O      1 
ATOM   1052  C  CB     . LEU   A 1  136 ? 31.633  -87.521  -60.347  1.00 52.16  ? 136 LEU   A CB     1 
ATOM   1053  C  CG     . LEU   A 1  136 ? 31.667  -88.290  -61.664  1.00 49.55  ? 136 LEU   A CG     1 
ATOM   1054  C  CD1    . LEU   A 1  136 ? 32.893  -89.201  -61.683  1.00 51.24  ? 136 LEU   A CD1    1 
ATOM   1055  C  CD2    . LEU   A 1  136 ? 30.391  -89.089  -61.818  1.00 44.84  ? 136 LEU   A CD2    1 
ATOM   1056  N  N      . VAL   A 1  137 ? 32.251  -84.301  -59.053  1.00 44.37  ? 137 VAL   A N      1 
ATOM   1057  C  CA     . VAL   A 1  137 ? 32.170  -83.352  -57.938  1.00 45.01  ? 137 VAL   A CA     1 
ATOM   1058  C  C      . VAL   A 1  137 ? 30.765  -82.749  -57.889  1.00 41.14  ? 137 VAL   A C      1 
ATOM   1059  O  O      . VAL   A 1  137 ? 30.348  -82.057  -58.827  1.00 45.21  ? 137 VAL   A O      1 
ATOM   1060  C  CB     . VAL   A 1  137 ? 33.244  -82.260  -58.078  1.00 48.22  ? 137 VAL   A CB     1 
ATOM   1061  C  CG1    . VAL   A 1  137 ? 33.390  -81.451  -56.808  1.00 45.34  ? 137 VAL   A CG1    1 
ATOM   1062  C  CG2    . VAL   A 1  137 ? 34.584  -82.894  -58.444  1.00 52.42  ? 137 VAL   A CG2    1 
ATOM   1063  N  N      . PHE   A 1  138 ? 30.052  -83.004  -56.788  1.00 40.95  ? 138 PHE   A N      1 
ATOM   1064  C  CA     . PHE   A 1  138 ? 28.648  -82.630  -56.566  1.00 45.79  ? 138 PHE   A CA     1 
ATOM   1065  C  C      . PHE   A 1  138 ? 28.560  -81.487  -55.536  1.00 44.67  ? 138 PHE   A C      1 
ATOM   1066  O  O      . PHE   A 1  138 ? 28.980  -81.648  -54.387  1.00 45.30  ? 138 PHE   A O      1 
ATOM   1067  C  CB     . PHE   A 1  138 ? 27.843  -83.841  -56.058  1.00 44.63  ? 138 PHE   A CB     1 
ATOM   1068  C  CG     . PHE   A 1  138 ? 27.791  -85.013  -57.023  1.00 52.28  ? 138 PHE   A CG     1 
ATOM   1069  C  CD1    . PHE   A 1  138 ? 28.917  -85.790  -57.265  1.00 47.05  ? 138 PHE   A CD1    1 
ATOM   1070  C  CD2    . PHE   A 1  138 ? 26.604  -85.359  -57.667  1.00 51.11  ? 138 PHE   A CD2    1 
ATOM   1071  C  CE1    . PHE   A 1  138 ? 28.869  -86.855  -58.150  1.00 50.29  ? 138 PHE   A CE1    1 
ATOM   1072  C  CE2    . PHE   A 1  138 ? 26.557  -86.425  -58.547  1.00 47.02  ? 138 PHE   A CE2    1 
ATOM   1073  C  CZ     . PHE   A 1  138 ? 27.684  -87.172  -58.790  1.00 49.72  ? 138 PHE   A CZ     1 
ATOM   1074  N  N      . HIS   A 1  139 ? 27.968  -80.361  -55.920  1.00 41.90  ? 139 HIS   A N      1 
ATOM   1075  C  CA     . HIS   A 1  139 ? 27.995  -79.178  -55.066  1.00 43.70  ? 139 HIS   A CA     1 
ATOM   1076  C  C      . HIS   A 1  139 ? 26.942  -78.179  -55.531  1.00 46.17  ? 139 HIS   A C      1 
ATOM   1077  O  O      . HIS   A 1  139 ? 26.557  -78.166  -56.705  1.00 42.76  ? 139 HIS   A O      1 
ATOM   1078  C  CB     . HIS   A 1  139 ? 29.380  -78.520  -55.085  1.00 41.38  ? 139 HIS   A CB     1 
ATOM   1079  C  CG     . HIS   A 1  139 ? 29.754  -77.910  -56.403  1.00 36.97  ? 139 HIS   A CG     1 
ATOM   1080  N  ND1    . HIS   A 1  139 ? 29.620  -76.565  -56.666  1.00 44.34  ? 139 HIS   A ND1    1 
ATOM   1081  C  CD2    . HIS   A 1  139 ? 30.274  -78.457  -57.527  1.00 41.28  ? 139 HIS   A CD2    1 
ATOM   1082  C  CE1    . HIS   A 1  139 ? 30.031  -76.309  -57.896  1.00 41.16  ? 139 HIS   A CE1    1 
ATOM   1083  N  NE2    . HIS   A 1  139 ? 30.433  -77.441  -58.440  1.00 40.83  ? 139 HIS   A NE2    1 
ATOM   1084  N  N      . SER   A 1  140 ? 26.505  -77.316  -54.605  1.00 39.88  ? 140 SER   A N      1 
ATOM   1085  C  CA     . SER   A 1  140 ? 25.681  -76.163  -54.964  1.00 43.18  ? 140 SER   A CA     1 
ATOM   1086  C  C      . SER   A 1  140 ? 26.558  -74.983  -55.372  1.00 41.98  ? 140 SER   A C      1 
ATOM   1087  O  O      . SER   A 1  140 ? 27.649  -74.801  -54.837  1.00 41.19  ? 140 SER   A O      1 
ATOM   1088  C  CB     . SER   A 1  140 ? 24.789  -75.738  -53.801  1.00 43.09  ? 140 SER   A CB     1 
ATOM   1089  O  OG     . SER   A 1  140 ? 25.573  -75.225  -52.738  1.00 39.76  ? 140 SER   A OG     1 
ATOM   1090  N  N      . PHE   A 1  141 ? 26.079  -74.193  -56.343  1.00 43.17  ? 141 PHE   A N      1 
ATOM   1091  C  CA     . PHE   A 1  141 ? 26.653  -72.870  -56.579  1.00 39.93  ? 141 PHE   A CA     1 
ATOM   1092  C  C      . PHE   A 1  141 ? 26.435  -71.937  -55.382  1.00 47.24  ? 141 PHE   A C      1 
ATOM   1093  O  O      . PHE   A 1  141 ? 27.241  -71.029  -55.150  1.00 43.23  ? 141 PHE   A O      1 
ATOM   1094  C  CB     . PHE   A 1  141 ? 26.023  -72.210  -57.803  1.00 39.71  ? 141 PHE   A CB     1 
ATOM   1095  C  CG     . PHE   A 1  141 ? 26.575  -72.655  -59.126  1.00 42.45  ? 141 PHE   A CG     1 
ATOM   1096  C  CD1    . PHE   A 1  141 ? 27.547  -73.632  -59.218  1.00 48.26  ? 141 PHE   A CD1    1 
ATOM   1097  C  CD2    . PHE   A 1  141 ? 26.095  -72.082  -60.302  1.00 39.82  ? 141 PHE   A CD2    1 
ATOM   1098  C  CE1    . PHE   A 1  141 ? 28.028  -74.035  -60.477  1.00 42.05  ? 141 PHE   A CE1    1 
ATOM   1099  C  CE2    . PHE   A 1  141 ? 26.566  -72.478  -61.540  1.00 42.62  ? 141 PHE   A CE2    1 
ATOM   1100  C  CZ     . PHE   A 1  141 ? 27.534  -73.453  -61.627  1.00 38.47  ? 141 PHE   A CZ     1 
ATOM   1101  N  N      . GLY   A 1  142 ? 25.336  -72.118  -54.635  1.00 50.88  ? 142 GLY   A N      1 
ATOM   1102  C  CA     . GLY   A 1  142 ? 24.862  -71.120  -53.690  1.00 36.63  ? 142 GLY   A CA     1 
ATOM   1103  C  C      . GLY   A 1  142 ? 25.476  -71.177  -52.312  1.00 38.89  ? 142 GLY   A C      1 
ATOM   1104  O  O      . GLY   A 1  142 ? 25.867  -70.147  -51.775  1.00 43.91  ? 142 GLY   A O      1 
ATOM   1105  N  N      . GLY   A 1  143 ? 25.556  -72.355  -51.709  1.00 41.71  ? 143 GLY   A N      1 
ATOM   1106  C  CA     . GLY   A 1  143 ? 26.101  -72.442  -50.369  1.00 37.84  ? 143 GLY   A CA     1 
ATOM   1107  C  C      . GLY   A 1  143 ? 27.519  -71.909  -50.306  1.00 40.25  ? 143 GLY   A C      1 
ATOM   1108  O  O      . GLY   A 1  143 ? 28.246  -71.905  -51.289  1.00 48.73  ? 143 GLY   A O      1 
ATOM   1109  N  N      . GLY   A 1  144 ? 27.910  -71.410  -49.138  1.00 44.67  ? 144 GLY   A N      1 
ATOM   1110  C  CA     . GLY   A 1  144 ? 29.291  -70.991  -48.965  1.00 42.78  ? 144 GLY   A CA     1 
ATOM   1111  C  C      . GLY   A 1  144 ? 30.256  -72.160  -49.056  1.00 44.79  ? 144 GLY   A C      1 
ATOM   1112  O  O      . GLY   A 1  144 ? 31.317  -72.040  -49.678  1.00 45.45  ? 144 GLY   A O      1 
ATOM   1113  N  N      . THR   A 1  145 ? 29.916  -73.293  -48.407  1.00 38.85  ? 145 THR   A N      1 
ATOM   1114  C  CA     . THR   A 1  145 ? 30.671  -74.531  -48.568  1.00 31.52  ? 145 THR   A CA     1 
ATOM   1115  C  C      . THR   A 1  145 ? 30.570  -75.052  -49.993  1.00 39.93  ? 145 THR   A C      1 
ATOM   1116  O  O      . THR   A 1  145 ? 31.582  -75.374  -50.620  1.00 47.15  ? 145 THR   A O      1 
ATOM   1117  C  CB     . THR   A 1  145 ? 30.174  -75.583  -47.589  1.00 34.02  ? 145 THR   A CB     1 
ATOM   1118  O  OG1    . THR   A 1  145 ? 30.070  -75.016  -46.286  1.00 46.01  ? 145 THR   A OG1    1 
ATOM   1119  C  CG2    . THR   A 1  145 ? 31.097  -76.762  -47.545  1.00 42.69  ? 145 THR   A CG2    1 
ATOM   1120  N  N      . GLY   A 1  146 ? 29.355  -75.146  -50.519  1.00 42.82  ? 146 GLY   A N      1 
ATOM   1121  C  CA     . GLY   A 1  146 ? 29.181  -75.587  -51.888  1.00 38.50  ? 146 GLY   A CA     1 
ATOM   1122  C  C      . GLY   A 1  146 ? 30.005  -74.806  -52.891  1.00 38.09  ? 146 GLY   A C      1 
ATOM   1123  O  O      . GLY   A 1  146 ? 30.624  -75.385  -53.784  1.00 44.44  ? 146 GLY   A O      1 
ATOM   1124  N  N      . SER   A 1  147 ? 30.023  -73.487  -52.778  1.00 35.43  ? 147 SER   A N      1 
ATOM   1125  C  CA     . SER   A 1  147 ? 30.731  -72.723  -53.802  1.00 39.55  ? 147 SER   A CA     1 
ATOM   1126  C  C      . SER   A 1  147 ? 32.213  -72.562  -53.515  1.00 45.89  ? 147 SER   A C      1 
ATOM   1127  O  O      . SER   A 1  147 ? 33.031  -72.655  -54.437  1.00 44.16  ? 147 SER   A O      1 
ATOM   1128  C  CB     . SER   A 1  147 ? 30.128  -71.328  -53.964  1.00 41.92  ? 147 SER   A CB     1 
ATOM   1129  O  OG     . SER   A 1  147 ? 30.243  -70.572  -52.778  1.00 36.23  ? 147 SER   A OG     1 
ATOM   1130  N  N      . GLY   A 1  148 ? 32.568  -72.303  -52.255  1.00 49.40  ? 148 GLY   A N      1 
ATOM   1131  C  CA     . GLY   A 1  148 ? 33.874  -71.783  -51.910  1.00 44.22  ? 148 GLY   A CA     1 
ATOM   1132  C  C      . GLY   A 1  148 ? 34.845  -72.880  -51.569  1.00 43.19  ? 148 GLY   A C      1 
ATOM   1133  O  O      . GLY   A 1  148 ? 35.999  -72.847  -51.994  1.00 47.05  ? 148 GLY   A O      1 
ATOM   1134  N  N      . PHE   A 1  149 ? 34.400  -73.876  -50.817  1.00 40.49  ? 149 PHE   A N      1 
ATOM   1135  C  CA     . PHE   A 1  149 ? 35.307  -74.985  -50.569  1.00 47.74  ? 149 PHE   A CA     1 
ATOM   1136  C  C      . PHE   A 1  149 ? 35.555  -75.783  -51.847  1.00 50.97  ? 149 PHE   A C      1 
ATOM   1137  O  O      . PHE   A 1  149 ? 36.685  -76.211  -52.118  1.00 51.63  ? 149 PHE   A O      1 
ATOM   1138  C  CB     . PHE   A 1  149 ? 34.766  -75.883  -49.476  1.00 39.79  ? 149 PHE   A CB     1 
ATOM   1139  C  CG     . PHE   A 1  149 ? 35.683  -76.984  -49.156  1.00 46.92  ? 149 PHE   A CG     1 
ATOM   1140  C  CD1    . PHE   A 1  149 ? 36.984  -76.708  -48.789  1.00 50.18  ? 149 PHE   A CD1    1 
ATOM   1141  C  CD2    . PHE   A 1  149 ? 35.278  -78.297  -49.287  1.00 52.59  ? 149 PHE   A CD2    1 
ATOM   1142  C  CE1    . PHE   A 1  149 ? 37.856  -77.715  -48.510  1.00 53.92  ? 149 PHE   A CE1    1 
ATOM   1143  C  CE2    . PHE   A 1  149 ? 36.137  -79.326  -49.017  1.00 55.10  ? 149 PHE   A CE2    1 
ATOM   1144  C  CZ     . PHE   A 1  149 ? 37.436  -79.038  -48.626  1.00 62.38  ? 149 PHE   A CZ     1 
ATOM   1145  N  N      . THR   A 1  150 ? 34.507  -75.961  -52.654  1.00 52.66  ? 150 THR   A N      1 
ATOM   1146  C  CA     . THR   A 1  150 ? 34.609  -76.696  -53.907  1.00 48.04  ? 150 THR   A CA     1 
ATOM   1147  C  C      . THR   A 1  150 ? 35.661  -76.098  -54.836  1.00 50.23  ? 150 THR   A C      1 
ATOM   1148  O  O      . THR   A 1  150 ? 36.458  -76.833  -55.429  1.00 53.56  ? 150 THR   A O      1 
ATOM   1149  C  CB     . THR   A 1  150 ? 33.237  -76.724  -54.574  1.00 47.24  ? 150 THR   A CB     1 
ATOM   1150  O  OG1    . THR   A 1  150 ? 32.351  -77.492  -53.751  1.00 45.69  ? 150 THR   A OG1    1 
ATOM   1151  C  CG2    . THR   A 1  150 ? 33.302  -77.331  -55.980  1.00 43.70  ? 150 THR   A CG2    1 
ATOM   1152  N  N      . SER   A 1  151 ? 35.694  -74.773  -54.983  1.00 41.31  ? 151 SER   A N      1 
ATOM   1153  C  CA     . SER   A 1  151 ? 36.717  -74.226  -55.866  1.00 45.37  ? 151 SER   A CA     1 
ATOM   1154  C  C      . SER   A 1  151 ? 38.125  -74.341  -55.262  1.00 54.26  ? 151 SER   A C      1 
ATOM   1155  O  O      . SER   A 1  151 ? 39.113  -74.418  -56.003  1.00 52.65  ? 151 SER   A O      1 
ATOM   1156  C  CB     . SER   A 1  151 ? 36.388  -72.781  -56.238  1.00 43.10  ? 151 SER   A CB     1 
ATOM   1157  O  OG     . SER   A 1  151 ? 36.645  -71.895  -55.172  1.00 46.64  ? 151 SER   A OG     1 
ATOM   1158  N  N      . LEU   A 1  152 ? 38.254  -74.358  -53.933  1.00 53.75  ? 152 LEU   A N      1 
ATOM   1159  C  CA     . LEU   A 1  152 ? 39.573  -74.613  -53.366  1.00 53.77  ? 152 LEU   A CA     1 
ATOM   1160  C  C      . LEU   A 1  152 ? 39.971  -76.064  -53.581  1.00 54.20  ? 152 LEU   A C      1 
ATOM   1161  O  O      . LEU   A 1  152 ? 41.132  -76.355  -53.888  1.00 54.25  ? 152 LEU   A O      1 
ATOM   1162  C  CB     . LEU   A 1  152 ? 39.617  -74.273  -51.869  1.00 57.90  ? 152 LEU   A CB     1 
ATOM   1163  C  CG     . LEU   A 1  152 ? 40.977  -74.637  -51.229  1.00 56.62  ? 152 LEU   A CG     1 
ATOM   1164  C  CD1    . LEU   A 1  152 ? 42.143  -73.897  -51.929  1.00 58.49  ? 152 LEU   A CD1    1 
ATOM   1165  C  CD2    . LEU   A 1  152 ? 41.020  -74.464  -49.713  1.00 53.79  ? 152 LEU   A CD2    1 
ATOM   1166  N  N      . LEU   A 1  153 ? 39.017  -76.986  -53.415  1.00 55.66  ? 153 LEU   A N      1 
ATOM   1167  C  CA     . LEU   A 1  153 ? 39.281  -78.393  -53.705  1.00 54.53  ? 153 LEU   A CA     1 
ATOM   1168  C  C      . LEU   A 1  153 ? 39.609  -78.600  -55.178  1.00 56.42  ? 153 LEU   A C      1 
ATOM   1169  O  O      . LEU   A 1  153 ? 40.611  -79.240  -55.511  1.00 61.35  ? 153 LEU   A O      1 
ATOM   1170  C  CB     . LEU   A 1  153 ? 38.092  -79.253  -53.300  1.00 47.37  ? 153 LEU   A CB     1 
ATOM   1171  C  CG     . LEU   A 1  153 ? 38.326  -80.717  -53.592  1.00 46.12  ? 153 LEU   A CG     1 
ATOM   1172  C  CD1    . LEU   A 1  153 ? 39.755  -81.021  -53.241  1.00 55.16  ? 153 LEU   A CD1    1 
ATOM   1173  C  CD2    . LEU   A 1  153 ? 37.390  -81.575  -52.774  1.00 38.40  ? 153 LEU   A CD2    1 
ATOM   1174  N  N      . MET   A 1  154 ? 38.777  -78.049  -56.074  1.00 53.40  ? 154 MET   A N      1 
ATOM   1175  C  CA     . MET   A 1  154 ? 39.029  -78.151  -57.508  1.00 53.76  ? 154 MET   A CA     1 
ATOM   1176  C  C      . MET   A 1  154 ? 40.443  -77.687  -57.867  1.00 56.38  ? 154 MET   A C      1 
ATOM   1177  O  O      . MET   A 1  154 ? 41.082  -78.258  -58.755  1.00 56.35  ? 154 MET   A O      1 
ATOM   1178  C  CB     . MET   A 1  154 ? 38.002  -77.323  -58.280  1.00 49.45  ? 154 MET   A CB     1 
ATOM   1179  C  CG     . MET   A 1  154 ? 36.656  -77.966  -58.619  1.00 50.12  ? 154 MET   A CG     1 
ATOM   1180  S  SD     . MET   A 1  154 ? 36.586  -79.680  -59.152  1.00 48.64  ? 154 MET   A SD     1 
ATOM   1181  C  CE     . MET   A 1  154 ? 36.135  -79.446  -60.880  1.00 44.64  ? 154 MET   A CE     1 
ATOM   1182  N  N      . GLU   A 1  155 ? 40.941  -76.633  -57.216  1.00 58.40  ? 155 GLU   A N      1 
ATOM   1183  C  CA     . GLU   A 1  155 ? 42.268  -76.118  -57.578  1.00 63.35  ? 155 GLU   A CA     1 
ATOM   1184  C  C      . GLU   A 1  155 ? 43.374  -77.104  -57.209  1.00 61.00  ? 155 GLU   A C      1 
ATOM   1185  O  O      . GLU   A 1  155 ? 44.298  -77.333  -57.998  1.00 60.33  ? 155 GLU   A O      1 
ATOM   1186  C  CB     . GLU   A 1  155 ? 42.530  -74.763  -56.909  1.00 61.08  ? 155 GLU   A CB     1 
ATOM   1187  C  CG     . GLU   A 1  155 ? 41.865  -73.590  -57.605  1.00 62.56  ? 155 GLU   A CG     1 
ATOM   1188  C  CD     . GLU   A 1  155 ? 42.489  -72.280  -57.216  1.00 61.82  ? 155 GLU   A CD     1 
ATOM   1189  O  OE1    . GLU   A 1  155 ? 42.727  -72.115  -56.001  1.00 53.64  ? 155 GLU   A OE1    1 
ATOM   1190  O  OE2    . GLU   A 1  155 ? 42.725  -71.428  -58.116  1.00 65.58  ? 155 GLU   A OE2    1 
ATOM   1191  N  N      . ARG   A 1  156 ? 43.296  -77.700  -56.018  1.00 54.54  ? 156 ARG   A N      1 
ATOM   1192  C  CA     . ARG   A 1  156 ? 44.314  -78.654  -55.615  1.00 58.84  ? 156 ARG   A CA     1 
ATOM   1193  C  C      . ARG   A 1  156 ? 44.242  -79.927  -56.449  1.00 65.53  ? 156 ARG   A C      1 
ATOM   1194  O  O      . ARG   A 1  156 ? 45.280  -80.488  -56.825  1.00 68.01  ? 156 ARG   A O      1 
ATOM   1195  C  CB     . ARG   A 1  156 ? 44.180  -78.962  -54.128  1.00 60.82  ? 156 ARG   A CB     1 
ATOM   1196  C  CG     . ARG   A 1  156 ? 44.651  -77.811  -53.250  1.00 69.09  ? 156 ARG   A CG     1 
ATOM   1197  C  CD     . ARG   A 1  156 ? 46.172  -77.686  -53.263  1.00 67.55  ? 156 ARG   A CD     1 
ATOM   1198  N  NE     . ARG   A 1  156 ? 46.760  -78.637  -52.330  1.00 67.84  ? 156 ARG   A NE     1 
ATOM   1199  C  CZ     . ARG   A 1  156 ? 46.754  -78.478  -51.014  1.00 70.56  ? 156 ARG   A CZ     1 
ATOM   1200  N  NH1    . ARG   A 1  156 ? 46.248  -77.391  -50.451  1.00 74.23  ? 156 ARG   A NH1    1 
ATOM   1201  N  NH2    . ARG   A 1  156 ? 47.244  -79.443  -50.239  1.00 69.15  ? 156 ARG   A NH2    1 
ATOM   1202  N  N      . LEU   A 1  157 ? 43.032  -80.404  -56.753  1.00 63.23  ? 157 LEU   A N      1 
ATOM   1203  C  CA     . LEU   A 1  157 ? 42.915  -81.614  -57.562  1.00 58.43  ? 157 LEU   A CA     1 
ATOM   1204  C  C      . LEU   A 1  157 ? 43.637  -81.443  -58.896  1.00 57.01  ? 157 LEU   A C      1 
ATOM   1205  O  O      . LEU   A 1  157 ? 44.432  -82.299  -59.290  1.00 59.06  ? 157 LEU   A O      1 
ATOM   1206  C  CB     . LEU   A 1  157 ? 41.440  -81.974  -57.754  1.00 56.09  ? 157 LEU   A CB     1 
ATOM   1207  C  CG     . LEU   A 1  157 ? 40.724  -82.484  -56.499  1.00 50.17  ? 157 LEU   A CG     1 
ATOM   1208  C  CD1    . LEU   A 1  157 ? 39.332  -83.017  -56.816  1.00 50.85  ? 157 LEU   A CD1    1 
ATOM   1209  C  CD2    . LEU   A 1  157 ? 41.556  -83.553  -55.863  1.00 47.96  ? 157 LEU   A CD2    1 
ATOM   1210  N  N      . SER   A 1  158 ? 43.405  -80.320  -59.587  1.00 55.24  ? 158 SER   A N      1 
ATOM   1211  C  CA     . SER   A 1  158 ? 44.181  -80.008  -60.780  1.00 57.04  ? 158 SER   A CA     1 
ATOM   1212  C  C      . SER   A 1  158 ? 45.678  -80.115  -60.535  1.00 62.73  ? 158 SER   A C      1 
ATOM   1213  O  O      . SER   A 1  158 ? 46.443  -80.349  -61.476  1.00 68.27  ? 158 SER   A O      1 
ATOM   1214  C  CB     . SER   A 1  158 ? 43.859  -78.601  -61.286  1.00 56.88  ? 158 SER   A CB     1 
ATOM   1215  O  OG     . SER   A 1  158 ? 42.667  -78.577  -62.049  1.00 60.59  ? 158 SER   A OG     1 
ATOM   1216  N  N      . VAL   A 1  159 ? 46.119  -79.939  -59.299  1.00 65.22  ? 159 VAL   A N      1 
ATOM   1217  C  CA     . VAL   A 1  159 ? 47.542  -79.966  -58.993  1.00 65.33  ? 159 VAL   A CA     1 
ATOM   1218  C  C      . VAL   A 1  159 ? 48.018  -81.381  -58.701  1.00 62.94  ? 159 VAL   A C      1 
ATOM   1219  O  O      . VAL   A 1  159 ? 48.991  -81.847  -59.293  1.00 71.81  ? 159 VAL   A O      1 
ATOM   1220  C  CB     . VAL   A 1  159 ? 47.843  -79.009  -57.821  1.00 65.74  ? 159 VAL   A CB     1 
ATOM   1221  C  CG1    . VAL   A 1  159 ? 49.028  -79.514  -57.035  1.00 66.33  ? 159 VAL   A CG1    1 
ATOM   1222  C  CG2    . VAL   A 1  159 ? 48.072  -77.588  -58.335  1.00 60.65  ? 159 VAL   A CG2    1 
ATOM   1223  N  N      . ASP   A 1  160 ? 47.337  -82.105  -57.813  1.00 62.83  ? 160 ASP   A N      1 
ATOM   1224  C  CA     . ASP   A 1  160 ? 47.772  -83.448  -57.443  1.00 63.22  ? 160 ASP   A CA     1 
ATOM   1225  C  C      . ASP   A 1  160 ? 47.414  -84.520  -58.466  1.00 67.02  ? 160 ASP   A C      1 
ATOM   1226  O  O      . ASP   A 1  160 ? 47.931  -85.639  -58.357  1.00 67.89  ? 160 ASP   A O      1 
ATOM   1227  C  CB     . ASP   A 1  160 ? 47.180  -83.860  -56.095  1.00 63.51  ? 160 ASP   A CB     1 
ATOM   1228  C  CG     . ASP   A 1  160 ? 47.483  -82.871  -55.000  1.00 69.84  ? 160 ASP   A CG     1 
ATOM   1229  O  OD1    . ASP   A 1  160 ? 48.120  -81.823  -55.299  1.00 67.97  ? 160 ASP   A OD1    1 
ATOM   1230  O  OD2    . ASP   A 1  160 ? 47.091  -83.166  -53.842  1.00 64.96  ? 160 ASP   A OD2    1 
ATOM   1231  N  N      . TYR   A 1  161 ? 46.537  -84.229  -59.431  1.00 69.25  ? 161 TYR   A N      1 
ATOM   1232  C  CA     . TYR   A 1  161 ? 46.079  -85.214  -60.414  1.00 57.74  ? 161 TYR   A CA     1 
ATOM   1233  C  C      . TYR   A 1  161 ? 45.947  -84.576  -61.775  1.00 57.11  ? 161 TYR   A C      1 
ATOM   1234  O  O      . TYR   A 1  161 ? 44.956  -84.784  -62.475  1.00 65.24  ? 161 TYR   A O      1 
ATOM   1235  C  CB     . TYR   A 1  161 ? 44.739  -85.827  -60.024  1.00 53.25  ? 161 TYR   A CB     1 
ATOM   1236  C  CG     . TYR   A 1  161 ? 44.672  -86.450  -58.651  1.00 55.62  ? 161 TYR   A CG     1 
ATOM   1237  C  CD1    . TYR   A 1  161 ? 44.557  -85.665  -57.505  1.00 55.70  ? 161 TYR   A CD1    1 
ATOM   1238  C  CD2    . TYR   A 1  161 ? 44.672  -87.820  -58.500  1.00 49.48  ? 161 TYR   A CD2    1 
ATOM   1239  C  CE1    . TYR   A 1  161 ? 44.481  -86.240  -56.247  1.00 49.80  ? 161 TYR   A CE1    1 
ATOM   1240  C  CE2    . TYR   A 1  161 ? 44.596  -88.395  -57.248  1.00 57.73  ? 161 TYR   A CE2    1 
ATOM   1241  C  CZ     . TYR   A 1  161 ? 44.506  -87.603  -56.132  1.00 52.88  ? 161 TYR   A CZ     1 
ATOM   1242  O  OH     . TYR   A 1  161 ? 44.417  -88.202  -54.905  1.00 63.38  ? 161 TYR   A OH     1 
ATOM   1243  N  N      . GLY   A 1  162 ? 46.926  -83.780  -62.170  1.00 60.30  ? 162 GLY   A N      1 
ATOM   1244  C  CA     . GLY   A 1  162 ? 46.835  -83.043  -63.416  1.00 61.56  ? 162 GLY   A CA     1 
ATOM   1245  C  C      . GLY   A 1  162 ? 46.360  -83.843  -64.614  1.00 60.24  ? 162 GLY   A C      1 
ATOM   1246  O  O      . GLY   A 1  162 ? 45.863  -83.264  -65.585  1.00 57.58  ? 162 GLY   A O      1 
ATOM   1247  N  N      . LYS   A 1  163 ? 46.500  -85.173  -64.562  1.00 64.34  ? 163 LYS   A N      1 
ATOM   1248  C  CA     . LYS   A 1  163 ? 46.181  -86.032  -65.702  1.00 71.58  ? 163 LYS   A CA     1 
ATOM   1249  C  C      . LYS   A 1  163 ? 44.780  -86.659  -65.630  1.00 72.23  ? 163 LYS   A C      1 
ATOM   1250  O  O      . LYS   A 1  163 ? 44.332  -87.273  -66.614  1.00 67.49  ? 163 LYS   A O      1 
ATOM   1251  C  CB     . LYS   A 1  163 ? 47.253  -87.132  -65.844  1.00 59.02  ? 163 LYS   A CB     1 
ATOM   1252  N  N      . LYS   A 1  164 ? 44.069  -86.499  -64.516  1.00 67.29  ? 164 LYS   A N      1 
ATOM   1253  C  CA     . LYS   A 1  164 ? 42.753  -87.087  -64.335  1.00 58.69  ? 164 LYS   A CA     1 
ATOM   1254  C  C      . LYS   A 1  164 ? 41.662  -86.057  -64.625  1.00 58.07  ? 164 LYS   A C      1 
ATOM   1255  O  O      . LYS   A 1  164 ? 41.853  -84.852  -64.445  1.00 59.31  ? 164 LYS   A O      1 
ATOM   1256  C  CB     . LYS   A 1  164 ? 42.613  -87.651  -62.917  1.00 57.48  ? 164 LYS   A CB     1 
ATOM   1257  C  CG     . LYS   A 1  164 ? 43.935  -87.956  -62.218  1.00 56.56  ? 164 LYS   A CG     1 
ATOM   1258  C  CD     . LYS   A 1  164 ? 44.822  -88.981  -62.959  1.00 60.58  ? 164 LYS   A CD     1 
ATOM   1259  C  CE     . LYS   A 1  164 ? 46.346  -88.877  -62.552  1.00 72.58  ? 164 LYS   A CE     1 
ATOM   1260  N  NZ     . LYS   A 1  164 ? 47.150  -87.621  -62.956  1.00 59.56  ? 164 LYS   A NZ     1 
ATOM   1261  N  N      . SER   A 1  165 ? 40.516  -86.550  -65.099  1.00 59.06  ? 165 SER   A N      1 
ATOM   1262  C  CA     . SER   A 1  165 ? 39.398  -85.701  -65.496  1.00 56.19  ? 165 SER   A CA     1 
ATOM   1263  C  C      . SER   A 1  165 ? 38.544  -85.315  -64.285  1.00 57.72  ? 165 SER   A C      1 
ATOM   1264  O  O      . SER   A 1  165 ? 38.433  -86.061  -63.297  1.00 48.95  ? 165 SER   A O      1 
ATOM   1265  C  CB     . SER   A 1  165 ? 38.520  -86.427  -66.520  1.00 59.30  ? 165 SER   A CB     1 
ATOM   1266  O  OG     . SER   A 1  165 ? 39.017  -86.289  -67.838  1.00 56.87  ? 165 SER   A OG     1 
ATOM   1267  N  N      . LYS   A 1  166 ? 37.919  -84.142  -64.376  1.00 53.69  ? 166 LYS   A N      1 
ATOM   1268  C  CA     . LYS   A 1  166 ? 37.026  -83.663  -63.323  1.00 55.82  ? 166 LYS   A CA     1 
ATOM   1269  C  C      . LYS   A 1  166 ? 35.695  -83.224  -63.936  1.00 52.86  ? 166 LYS   A C      1 
ATOM   1270  O  O      . LYS   A 1  166 ? 35.649  -82.283  -64.747  1.00 45.98  ? 166 LYS   A O      1 
ATOM   1271  C  CB     . LYS   A 1  166 ? 37.667  -82.515  -62.524  1.00 53.64  ? 166 LYS   A CB     1 
ATOM   1272  C  CG     . LYS   A 1  166 ? 38.974  -82.849  -61.779  1.00 56.00  ? 166 LYS   A CG     1 
ATOM   1273  C  CD     . LYS   A 1  166 ? 39.582  -81.586  -61.112  1.00 51.95  ? 166 LYS   A CD     1 
ATOM   1274  C  CE     . LYS   A 1  166 ? 40.846  -81.159  -61.832  1.00 53.12  ? 166 LYS   A CE     1 
ATOM   1275  N  NZ     . LYS   A 1  166 ? 40.649  -81.211  -63.341  1.00 59.94  ? 166 LYS   A NZ     1 
ATOM   1276  N  N      . LEU   A 1  167 ? 34.616  -83.894  -63.540  1.00 47.52  ? 167 LEU   A N      1 
ATOM   1277  C  CA     . LEU   A 1  167 ? 33.268  -83.533  -63.959  1.00 49.17  ? 167 LEU   A CA     1 
ATOM   1278  C  C      . LEU   A 1  167 ? 32.467  -82.988  -62.775  1.00 51.54  ? 167 LEU   A C      1 
ATOM   1279  O  O      . LEU   A 1  167 ? 32.648  -83.415  -61.620  1.00 45.48  ? 167 LEU   A O      1 
ATOM   1280  C  CB     . LEU   A 1  167 ? 32.540  -84.736  -64.563  1.00 42.30  ? 167 LEU   A CB     1 
ATOM   1281  C  CG     . LEU   A 1  167 ? 32.766  -85.098  -66.024  1.00 41.98  ? 167 LEU   A CG     1 
ATOM   1282  C  CD1    . LEU   A 1  167 ? 34.205  -85.488  -66.266  1.00 47.29  ? 167 LEU   A CD1    1 
ATOM   1283  C  CD2    . LEU   A 1  167 ? 31.877  -86.264  -66.335  1.00 48.50  ? 167 LEU   A CD2    1 
ATOM   1284  N  N      . GLU   A 1  168 ? 31.567  -82.044  -63.082  1.00 46.10  ? 168 GLU   A N      1 
ATOM   1285  C  CA     . GLU   A 1  168 ? 30.756  -81.352  -62.087  1.00 46.51  ? 168 GLU   A CA     1 
ATOM   1286  C  C      . GLU   A 1  168 ? 29.268  -81.664  -62.255  1.00 47.08  ? 168 GLU   A C      1 
ATOM   1287  O  O      . GLU   A 1  168 ? 28.752  -81.747  -63.376  1.00 43.09  ? 168 GLU   A O      1 
ATOM   1288  C  CB     . GLU   A 1  168 ? 30.947  -79.842  -62.200  1.00 43.50  ? 168 GLU   A CB     1 
ATOM   1289  C  CG     . GLU   A 1  168 ? 32.068  -79.251  -61.374  1.00 43.99  ? 168 GLU   A CG     1 
ATOM   1290  C  CD     . GLU   A 1  168 ? 32.112  -77.744  -61.518  1.00 42.34  ? 168 GLU   A CD     1 
ATOM   1291  O  OE1    . GLU   A 1  168 ? 32.407  -77.242  -62.619  1.00 47.47  ? 168 GLU   A OE1    1 
ATOM   1292  O  OE2    . GLU   A 1  168 ? 31.796  -77.046  -60.549  1.00 47.70  ? 168 GLU   A OE2    1 
ATOM   1293  N  N      . PHE   A 1  169 ? 28.580  -81.824  -61.132  1.00 45.50  ? 169 PHE   A N      1 
ATOM   1294  C  CA     . PHE   A 1  169 ? 27.124  -81.717  -61.063  1.00 42.85  ? 169 PHE   A CA     1 
ATOM   1295  C  C      . PHE   A 1  169 ? 26.814  -80.569  -60.115  1.00 41.45  ? 169 PHE   A C      1 
ATOM   1296  O  O      . PHE   A 1  169 ? 27.017  -80.692  -58.905  1.00 42.49  ? 169 PHE   A O      1 
ATOM   1297  C  CB     . PHE   A 1  169 ? 26.484  -83.013  -60.578  1.00 45.06  ? 169 PHE   A CB     1 
ATOM   1298  C  CG     . PHE   A 1  169 ? 26.647  -84.155  -61.534  1.00 53.07  ? 169 PHE   A CG     1 
ATOM   1299  C  CD1    . PHE   A 1  169 ? 25.797  -84.293  -62.625  1.00 46.21  ? 169 PHE   A CD1    1 
ATOM   1300  C  CD2    . PHE   A 1  169 ? 27.672  -85.085  -61.358  1.00 50.90  ? 169 PHE   A CD2    1 
ATOM   1301  C  CE1    . PHE   A 1  169 ? 25.967  -85.345  -63.518  1.00 46.34  ? 169 PHE   A CE1    1 
ATOM   1302  C  CE2    . PHE   A 1  169 ? 27.837  -86.135  -62.246  1.00 50.33  ? 169 PHE   A CE2    1 
ATOM   1303  C  CZ     . PHE   A 1  169 ? 26.985  -86.268  -63.327  1.00 44.70  ? 169 PHE   A CZ     1 
ATOM   1304  N  N      . SER   A 1  170 ? 26.335  -79.455  -60.661  1.00 41.70  ? 170 SER   A N      1 
ATOM   1305  C  CA     . SER   A 1  170 ? 26.214  -78.198  -59.932  1.00 39.10  ? 170 SER   A CA     1 
ATOM   1306  C  C      . SER   A 1  170 ? 24.752  -77.802  -59.835  1.00 36.99  ? 170 SER   A C      1 
ATOM   1307  O  O      . SER   A 1  170 ? 24.092  -77.633  -60.862  1.00 39.62  ? 170 SER   A O      1 
ATOM   1308  C  CB     . SER   A 1  170 ? 27.016  -77.096  -60.629  1.00 38.95  ? 170 SER   A CB     1 
ATOM   1309  O  OG     . SER   A 1  170 ? 28.317  -77.563  -60.981  1.00 43.41  ? 170 SER   A OG     1 
ATOM   1310  N  N      . ILE   A 1  171 ? 24.255  -77.638  -58.608  1.00 41.48  ? 171 ILE   A N      1 
ATOM   1311  C  CA     . ILE   A 1  171 ? 22.924  -77.083  -58.356  1.00 37.27  ? 171 ILE   A CA     1 
ATOM   1312  C  C      . ILE   A 1  171 ? 22.989  -75.568  -58.516  1.00 35.73  ? 171 ILE   A C      1 
ATOM   1313  O  O      . ILE   A 1  171 ? 23.607  -74.882  -57.700  1.00 43.65  ? 171 ILE   A O      1 
ATOM   1314  C  CB     . ILE   A 1  171 ? 22.408  -77.448  -56.962  1.00 34.50  ? 171 ILE   A CB     1 
ATOM   1315  C  CG1    . ILE   A 1  171 ? 22.351  -78.957  -56.771  1.00 31.86  ? 171 ILE   A CG1    1 
ATOM   1316  C  CG2    . ILE   A 1  171 ? 21.033  -76.780  -56.736  1.00 38.04  ? 171 ILE   A CG2    1 
ATOM   1317  C  CD1    . ILE   A 1  171 ? 21.578  -79.708  -57.814  1.00 38.11  ? 171 ILE   A CD1    1 
ATOM   1318  N  N      . TYR   A 1  172 ? 22.323  -75.038  -59.537  1.00 35.36  ? 172 TYR   A N      1 
ATOM   1319  C  CA     . TYR   A 1  172 ? 22.259  -73.609  -59.841  1.00 37.74  ? 172 TYR   A CA     1 
ATOM   1320  C  C      . TYR   A 1  172 ? 21.129  -72.954  -59.031  1.00 37.97  ? 172 TYR   A C      1 
ATOM   1321  O  O      . TYR   A 1  172 ? 20.076  -73.563  -58.830  1.00 32.11  ? 172 TYR   A O      1 
ATOM   1322  C  CB     . TYR   A 1  172 ? 22.067  -73.418  -61.346  1.00 34.80  ? 172 TYR   A CB     1 
ATOM   1323  C  CG     . TYR   A 1  172 ? 21.670  -72.057  -61.877  1.00 32.42  ? 172 TYR   A CG     1 
ATOM   1324  C  CD1    . TYR   A 1  172 ? 20.398  -71.540  -61.638  1.00 32.49  ? 172 TYR   A CD1    1 
ATOM   1325  C  CD2    . TYR   A 1  172 ? 22.532  -71.326  -62.706  1.00 30.49  ? 172 TYR   A CD2    1 
ATOM   1326  C  CE1    . TYR   A 1  172 ? 20.002  -70.311  -62.169  1.00 32.61  ? 172 TYR   A CE1    1 
ATOM   1327  C  CE2    . TYR   A 1  172 ? 22.137  -70.087  -63.255  1.00 31.43  ? 172 TYR   A CE2    1 
ATOM   1328  C  CZ     . TYR   A 1  172 ? 20.864  -69.598  -62.981  1.00 34.82  ? 172 TYR   A CZ     1 
ATOM   1329  O  OH     . TYR   A 1  172 ? 20.432  -68.386  -63.472  1.00 40.80  ? 172 TYR   A OH     1 
ATOM   1330  N  N      . PRO   A 1  173 ? 21.314  -71.728  -58.527  1.00 42.72  ? 173 PRO   A N      1 
ATOM   1331  C  CA     . PRO   A 1  173 ? 20.495  -71.247  -57.396  1.00 30.00  ? 173 PRO   A CA     1 
ATOM   1332  C  C      . PRO   A 1  173 ? 19.118  -70.793  -57.838  1.00 32.08  ? 173 PRO   A C      1 
ATOM   1333  O  O      . PRO   A 1  173 ? 18.988  -70.002  -58.773  1.00 39.66  ? 173 PRO   A O      1 
ATOM   1334  C  CB     . PRO   A 1  173 ? 21.305  -70.068  -56.863  1.00 34.01  ? 173 PRO   A CB     1 
ATOM   1335  C  CG     . PRO   A 1  173 ? 21.938  -69.503  -58.121  1.00 39.71  ? 173 PRO   A CG     1 
ATOM   1336  C  CD     . PRO   A 1  173 ? 22.218  -70.676  -59.041  1.00 35.60  ? 173 PRO   A CD     1 
ATOM   1337  N  N      . ALA   A 1  174 ? 18.084  -71.276  -57.149  1.00 43.60  ? 174 ALA   A N      1 
ATOM   1338  C  CA     . ALA   A 1  174 ? 16.707  -70.873  -57.433  1.00 37.01  ? 174 ALA   A CA     1 
ATOM   1339  C  C      . ALA   A 1  174 ? 16.087  -70.231  -56.198  1.00 41.41  ? 174 ALA   A C      1 
ATOM   1340  O  O      . ALA   A 1  174 ? 16.104  -70.828  -55.109  1.00 40.75  ? 174 ALA   A O      1 
ATOM   1341  C  CB     . ALA   A 1  174 ? 15.846  -72.077  -57.885  1.00 30.56  ? 174 ALA   A CB     1 
ATOM   1342  N  N      . PRO   A 1  175 ? 15.521  -69.033  -56.328  1.00 43.95  ? 175 PRO   A N      1 
ATOM   1343  C  CA     . PRO   A 1  175 ? 14.931  -68.355  -55.157  1.00 48.58  ? 175 PRO   A CA     1 
ATOM   1344  C  C      . PRO   A 1  175 ? 13.858  -69.131  -54.411  1.00 47.07  ? 175 PRO   A C      1 
ATOM   1345  O  O      . PRO   A 1  175 ? 13.779  -68.980  -53.187  1.00 45.39  ? 175 PRO   A O      1 
ATOM   1346  C  CB     . PRO   A 1  175 ? 14.366  -67.066  -55.768  1.00 47.59  ? 175 PRO   A CB     1 
ATOM   1347  C  CG     . PRO   A 1  175 ? 15.342  -66.763  -56.870  1.00 43.87  ? 175 PRO   A CG     1 
ATOM   1348  C  CD     . PRO   A 1  175 ? 15.710  -68.110  -57.457  1.00 40.33  ? 175 PRO   A CD     1 
ATOM   1349  N  N      . GLN   A 1  176 ? 13.020  -69.933  -55.083  1.00 51.74  ? 176 GLN   A N      1 
ATOM   1350  C  CA     . GLN   A 1  176 ? 11.929  -70.619  -54.376  1.00 48.96  ? 176 GLN   A CA     1 
ATOM   1351  C  C      . GLN   A 1  176 ? 12.455  -71.502  -53.251  1.00 50.18  ? 176 GLN   A C      1 
ATOM   1352  O  O      . GLN   A 1  176 ? 11.965  -71.441  -52.126  1.00 59.24  ? 176 GLN   A O      1 
ATOM   1353  C  CB     . GLN   A 1  176 ? 11.086  -71.465  -55.333  1.00 46.43  ? 176 GLN   A CB     1 
ATOM   1354  C  CG     . GLN   A 1  176 ? 10.829  -70.848  -56.683  1.00 59.32  ? 176 GLN   A CG     1 
ATOM   1355  C  CD     . GLN   A 1  176 ? 9.372   -70.945  -57.072  1.00 66.59  ? 176 GLN   A CD     1 
ATOM   1356  O  OE1    . GLN   A 1  176 ? 8.480   -70.766  -56.236  1.00 68.07  ? 176 GLN   A OE1    1 
ATOM   1357  N  NE2    . GLN   A 1  176 ? 9.118   -71.281  -58.334  1.00 60.93  ? 176 GLN   A NE2    1 
ATOM   1358  N  N      . VAL   A 1  177 ? 13.429  -72.363  -53.536  1.00 47.20  ? 177 VAL   A N      1 
ATOM   1359  C  CA     . VAL   A 1  177 ? 13.955  -73.250  -52.509  1.00 49.84  ? 177 VAL   A CA     1 
ATOM   1360  C  C      . VAL   A 1  177 ? 15.223  -72.688  -51.867  1.00 52.40  ? 177 VAL   A C      1 
ATOM   1361  O  O      . VAL   A 1  177 ? 15.850  -73.360  -51.039  1.00 54.27  ? 177 VAL   A O      1 
ATOM   1362  C  CB     . VAL   A 1  177 ? 14.185  -74.661  -53.066  1.00 47.53  ? 177 VAL   A CB     1 
ATOM   1363  C  CG1    . VAL   A 1  177 ? 12.855  -75.284  -53.419  1.00 54.38  ? 177 VAL   A CG1    1 
ATOM   1364  C  CG2    . VAL   A 1  177 ? 15.036  -74.609  -54.308  1.00 39.99  ? 177 VAL   A CG2    1 
ATOM   1365  N  N      . SER   A 1  178 ? 15.591  -71.453  -52.202  1.00 43.66  ? 178 SER   A N      1 
ATOM   1366  C  CA     . SER   A 1  178 ? 16.846  -70.870  -51.754  1.00 47.88  ? 178 SER   A CA     1 
ATOM   1367  C  C      . SER   A 1  178 ? 16.778  -70.321  -50.346  1.00 52.16  ? 178 SER   A C      1 
ATOM   1368  O  O      . SER   A 1  178 ? 15.788  -69.719  -49.941  1.00 54.13  ? 178 SER   A O      1 
ATOM   1369  C  CB     . SER   A 1  178 ? 17.276  -69.737  -52.668  1.00 54.10  ? 178 SER   A CB     1 
ATOM   1370  O  OG     . SER   A 1  178 ? 18.606  -69.397  -52.357  1.00 54.21  ? 178 SER   A OG     1 
ATOM   1371  N  N      . THR   A 1  179 ? 17.888  -70.444  -49.632  1.00 61.42  ? 179 THR   A N      1 
ATOM   1372  C  CA     . THR   A 1  179 ? 17.948  -70.003  -48.249  1.00 58.23  ? 179 THR   A CA     1 
ATOM   1373  C  C      . THR   A 1  179 ? 18.708  -68.690  -48.079  1.00 56.72  ? 179 THR   A C      1 
ATOM   1374  O  O      . THR   A 1  179 ? 18.747  -68.161  -46.966  1.00 52.06  ? 179 THR   A O      1 
ATOM   1375  C  CB     . THR   A 1  179 ? 18.655  -71.064  -47.403  1.00 64.24  ? 179 THR   A CB     1 
ATOM   1376  O  OG1    . THR   A 1  179 ? 18.792  -72.280  -48.156  1.00 63.40  ? 179 THR   A OG1    1 
ATOM   1377  C  CG2    . THR   A 1  179 ? 17.813  -71.359  -46.164  1.00 58.30  ? 179 THR   A CG2    1 
ATOM   1378  N  N      . ALA   A 1  180 ? 19.342  -68.167  -49.129  1.00 46.00  ? 180 ALA   A N      1 
ATOM   1379  C  CA     . ALA   A 1  180 ? 20.295  -67.093  -48.937  1.00 43.03  ? 180 ALA   A CA     1 
ATOM   1380  C  C      . ALA   A 1  180 ? 20.168  -66.091  -50.060  1.00 45.12  ? 180 ALA   A C      1 
ATOM   1381  O  O      . ALA   A 1  180 ? 19.864  -66.461  -51.199  1.00 52.43  ? 180 ALA   A O      1 
ATOM   1382  C  CB     . ALA   A 1  180 ? 21.727  -67.627  -48.874  1.00 46.51  ? 180 ALA   A CB     1 
ATOM   1383  N  N      . VAL   A 1  181 ? 20.408  -64.813  -49.734  1.00 34.10  ? 181 VAL   A N      1 
ATOM   1384  C  CA     . VAL   A 1  181 ? 20.322  -63.777  -50.761  1.00 39.46  ? 181 VAL   A CA     1 
ATOM   1385  C  C      . VAL   A 1  181 ? 21.647  -63.545  -51.476  1.00 39.77  ? 181 VAL   A C      1 
ATOM   1386  O  O      . VAL   A 1  181 ? 21.686  -62.795  -52.457  1.00 37.44  ? 181 VAL   A O      1 
ATOM   1387  C  CB     . VAL   A 1  181 ? 19.832  -62.435  -50.183  1.00 40.95  ? 181 VAL   A CB     1 
ATOM   1388  C  CG1    . VAL   A 1  181 ? 18.395  -62.524  -49.761  1.00 42.01  ? 181 VAL   A CG1    1 
ATOM   1389  C  CG2    . VAL   A 1  181 ? 20.687  -62.034  -49.006  1.00 46.00  ? 181 VAL   A CG2    1 
ATOM   1390  N  N      . VAL   A 1  182 ? 22.731  -64.170  -51.033  1.00 34.09  ? 182 VAL   A N      1 
ATOM   1391  C  CA     . VAL   A 1  182 ? 24.032  -63.889  -51.610  1.00 39.89  ? 182 VAL   A CA     1 
ATOM   1392  C  C      . VAL   A 1  182 ? 24.439  -64.944  -52.633  1.00 44.71  ? 182 VAL   A C      1 
ATOM   1393  O  O      . VAL   A 1  182 ? 25.574  -64.914  -53.123  1.00 44.52  ? 182 VAL   A O      1 
ATOM   1394  C  CB     . VAL   A 1  182 ? 25.105  -63.760  -50.509  1.00 39.14  ? 182 VAL   A CB     1 
ATOM   1395  C  CG1    . VAL   A 1  182 ? 24.939  -62.455  -49.778  1.00 35.89  ? 182 VAL   A CG1    1 
ATOM   1396  C  CG2    . VAL   A 1  182 ? 25.012  -64.921  -49.532  1.00 33.77  ? 182 VAL   A CG2    1 
ATOM   1397  N  N      . GLU   A 1  183 ? 23.550  -65.891  -52.943  1.00 46.27  ? 183 GLU   A N      1 
ATOM   1398  C  CA     . GLU   A 1  183 ? 23.880  -66.984  -53.859  1.00 41.85  ? 183 GLU   A CA     1 
ATOM   1399  C  C      . GLU   A 1  183 ? 24.460  -66.494  -55.184  1.00 44.53  ? 183 GLU   A C      1 
ATOM   1400  O  O      . GLU   A 1  183 ? 25.384  -67.149  -55.706  1.00 45.73  ? 183 GLU   A O      1 
ATOM   1401  C  CB     . GLU   A 1  183 ? 22.633  -67.852  -54.088  1.00 44.23  ? 183 GLU   A CB     1 
ATOM   1402  C  CG     . GLU   A 1  183 ? 22.092  -68.496  -52.813  1.00 43.33  ? 183 GLU   A CG     1 
ATOM   1403  C  CD     . GLU   A 1  183 ? 21.466  -69.852  -53.069  1.00 46.82  ? 183 GLU   A CD     1 
ATOM   1404  O  OE1    . GLU   A 1  183 ? 21.874  -70.523  -54.035  1.00 51.62  ? 183 GLU   A OE1    1 
ATOM   1405  O  OE2    . GLU   A 1  183 ? 20.560  -70.261  -52.317  1.00 55.69  ? 183 GLU   A OE2    1 
ATOM   1406  N  N      . PRO   A 1  184 ? 24.030  -65.367  -55.755  1.00 39.29  ? 184 PRO   A N      1 
ATOM   1407  C  CA     . PRO   A 1  184 ? 24.673  -64.926  -57.001  1.00 40.35  ? 184 PRO   A CA     1 
ATOM   1408  C  C      . PRO   A 1  184 ? 26.128  -64.524  -56.822  1.00 43.86  ? 184 PRO   A C      1 
ATOM   1409  O  O      . PRO   A 1  184 ? 26.931  -64.736  -57.738  1.00 43.71  ? 184 PRO   A O      1 
ATOM   1410  C  CB     . PRO   A 1  184 ? 23.799  -63.746  -57.460  1.00 34.07  ? 184 PRO   A CB     1 
ATOM   1411  C  CG     . PRO   A 1  184 ? 22.539  -63.902  -56.727  1.00 36.90  ? 184 PRO   A CG     1 
ATOM   1412  C  CD     . PRO   A 1  184 ? 22.921  -64.478  -55.392  1.00 35.70  ? 184 PRO   A CD     1 
ATOM   1413  N  N      . TYR   A 1  185 ? 26.499  -63.931  -55.683  1.00 41.23  ? 185 TYR   A N      1 
ATOM   1414  C  CA     . TYR   A 1  185 ? 27.914  -63.692  -55.426  1.00 41.95  ? 185 TYR   A CA     1 
ATOM   1415  C  C      . TYR   A 1  185 ? 28.689  -65.005  -55.451  1.00 44.42  ? 185 TYR   A C      1 
ATOM   1416  O  O      . TYR   A 1  185 ? 29.658  -65.159  -56.207  1.00 42.84  ? 185 TYR   A O      1 
ATOM   1417  C  CB     . TYR   A 1  185 ? 28.099  -62.980  -54.083  1.00 43.16  ? 185 TYR   A CB     1 
ATOM   1418  C  CG     . TYR   A 1  185 ? 27.808  -61.491  -54.126  1.00 44.76  ? 185 TYR   A CG     1 
ATOM   1419  C  CD1    . TYR   A 1  185 ? 27.517  -60.855  -55.323  1.00 44.51  ? 185 TYR   A CD1    1 
ATOM   1420  C  CD2    . TYR   A 1  185 ? 27.827  -60.723  -52.968  1.00 43.62  ? 185 TYR   A CD2    1 
ATOM   1421  C  CE1    . TYR   A 1  185 ? 27.252  -59.491  -55.367  1.00 45.47  ? 185 TYR   A CE1    1 
ATOM   1422  C  CE2    . TYR   A 1  185 ? 27.568  -59.361  -53.004  1.00 41.04  ? 185 TYR   A CE2    1 
ATOM   1423  C  CZ     . TYR   A 1  185 ? 27.282  -58.748  -54.207  1.00 42.45  ? 185 TYR   A CZ     1 
ATOM   1424  O  OH     . TYR   A 1  185 ? 27.010  -57.396  -54.249  1.00 39.33  ? 185 TYR   A OH     1 
ATOM   1425  N  N      . ASN   A 1  186 ? 28.236  -65.980  -54.657  1.00 40.59  ? 186 ASN   A N      1 
ATOM   1426  C  CA     . ASN   A 1  186 ? 28.907  -67.269  -54.555  1.00 38.60  ? 186 ASN   A CA     1 
ATOM   1427  C  C      . ASN   A 1  186 ? 28.967  -67.998  -55.892  1.00 44.87  ? 186 ASN   A C      1 
ATOM   1428  O  O      . ASN   A 1  186 ? 29.945  -68.702  -56.176  1.00 46.10  ? 186 ASN   A O      1 
ATOM   1429  C  CB     . ASN   A 1  186 ? 28.190  -68.131  -53.528  1.00 39.32  ? 186 ASN   A CB     1 
ATOM   1430  C  CG     . ASN   A 1  186 ? 28.158  -67.489  -52.167  1.00 45.73  ? 186 ASN   A CG     1 
ATOM   1431  O  OD1    . ASN   A 1  186 ? 28.858  -66.490  -51.922  1.00 44.77  ? 186 ASN   A OD1    1 
ATOM   1432  N  ND2    . ASN   A 1  186 ? 27.384  -68.073  -51.250  1.00 38.42  ? 186 ASN   A ND2    1 
ATOM   1433  N  N      . SER   A 1  187 ? 27.917  -67.881  -56.705  1.00 44.44  ? 187 SER   A N      1 
ATOM   1434  C  CA     . SER   A 1  187 ? 27.888  -68.568  -57.996  1.00 43.58  ? 187 SER   A CA     1 
ATOM   1435  C  C      . SER   A 1  187 ? 28.983  -68.048  -58.924  1.00 41.71  ? 187 SER   A C      1 
ATOM   1436  O  O      . SER   A 1  187 ? 29.831  -68.817  -59.382  1.00 48.73  ? 187 SER   A O      1 
ATOM   1437  C  CB     . SER   A 1  187 ? 26.506  -68.422  -58.658  1.00 44.21  ? 187 SER   A CB     1 
ATOM   1438  O  OG     . SER   A 1  187 ? 25.470  -69.045  -57.923  1.00 38.50  ? 187 SER   A OG     1 
ATOM   1439  N  N      . ILE   A 1  188 ? 28.966  -66.746  -59.237  1.00 42.01  ? 188 ILE   A N      1 
ATOM   1440  C  CA     . ILE   A 1  188 ? 30.004  -66.149  -60.087  1.00 41.98  ? 188 ILE   A CA     1 
ATOM   1441  C  C      . ILE   A 1  188 ? 31.401  -66.427  -59.539  1.00 42.50  ? 188 ILE   A C      1 
ATOM   1442  O  O      . ILE   A 1  188 ? 32.326  -66.756  -60.287  1.00 40.03  ? 188 ILE   A O      1 
ATOM   1443  C  CB     . ILE   A 1  188 ? 29.791  -64.635  -60.227  1.00 39.72  ? 188 ILE   A CB     1 
ATOM   1444  C  CG1    . ILE   A 1  188 ? 28.786  -64.330  -61.328  1.00 34.07  ? 188 ILE   A CG1    1 
ATOM   1445  C  CG2    . ILE   A 1  188 ? 31.139  -63.951  -60.472  1.00 37.07  ? 188 ILE   A CG2    1 
ATOM   1446  C  CD1    . ILE   A 1  188 ? 27.440  -64.799  -61.003  1.00 45.36  ? 188 ILE   A CD1    1 
ATOM   1447  N  N      . LEU   A 1  189 ? 31.591  -66.233  -58.232  1.00 45.54  ? 189 LEU   A N      1 
ATOM   1448  C  CA     . LEU   A 1  189 ? 32.920  -66.407  -57.662  1.00 46.23  ? 189 LEU   A CA     1 
ATOM   1449  C  C      . LEU   A 1  189 ? 33.428  -67.819  -57.920  1.00 47.85  ? 189 LEU   A C      1 
ATOM   1450  O  O      . LEU   A 1  189 ? 34.572  -68.011  -58.354  1.00 46.40  ? 189 LEU   A O      1 
ATOM   1451  C  CB     . LEU   A 1  189 ? 32.916  -66.095  -56.157  1.00 45.57  ? 189 LEU   A CB     1 
ATOM   1452  C  CG     . LEU   A 1  189 ? 32.676  -64.658  -55.663  1.00 46.93  ? 189 LEU   A CG     1 
ATOM   1453  C  CD1    . LEU   A 1  189 ? 32.660  -64.581  -54.132  1.00 41.83  ? 189 LEU   A CD1    1 
ATOM   1454  C  CD2    . LEU   A 1  189 ? 33.690  -63.711  -56.239  1.00 40.07  ? 189 LEU   A CD2    1 
ATOM   1455  N  N      . THR   A 1  190 ? 32.585  -68.824  -57.667  1.00 42.93  ? 190 THR   A N      1 
ATOM   1456  C  CA     . THR   A 1  190 ? 33.063  -70.192  -57.777  1.00 43.61  ? 190 THR   A CA     1 
ATOM   1457  C  C      . THR   A 1  190 ? 33.145  -70.654  -59.217  1.00 44.26  ? 190 THR   A C      1 
ATOM   1458  O  O      . THR   A 1  190 ? 33.987  -71.495  -59.544  1.00 46.50  ? 190 THR   A O      1 
ATOM   1459  C  CB     . THR   A 1  190 ? 32.179  -71.154  -57.013  1.00 45.84  ? 190 THR   A CB     1 
ATOM   1460  O  OG1    . THR   A 1  190 ? 32.925  -72.350  -56.796  1.00 44.34  ? 190 THR   A OG1    1 
ATOM   1461  C  CG2    . THR   A 1  190 ? 30.951  -71.494  -57.846  1.00 43.90  ? 190 THR   A CG2    1 
ATOM   1462  N  N      . THR   A 1  191 ? 32.307  -70.122  -60.099  1.00 45.98  ? 191 THR   A N      1 
ATOM   1463  C  CA     . THR   A 1  191 ? 32.449  -70.494  -61.498  1.00 47.58  ? 191 THR   A CA     1 
ATOM   1464  C  C      . THR   A 1  191 ? 33.778  -69.989  -62.039  1.00 46.84  ? 191 THR   A C      1 
ATOM   1465  O  O      . THR   A 1  191 ? 34.548  -70.747  -62.642  1.00 52.88  ? 191 THR   A O      1 
ATOM   1466  C  CB     . THR   A 1  191 ? 31.260  -69.976  -62.310  1.00 45.45  ? 191 THR   A CB     1 
ATOM   1467  O  OG1    . THR   A 1  191 ? 30.043  -70.513  -61.766  1.00 39.03  ? 191 THR   A OG1    1 
ATOM   1468  C  CG2    . THR   A 1  191 ? 31.389  -70.416  -63.773  1.00 43.32  ? 191 THR   A CG2    1 
ATOM   1469  N  N      . HIS   A 1  192 ? 34.096  -68.721  -61.760  1.00 49.02  ? 192 HIS   A N      1 
ATOM   1470  C  CA     . HIS   A 1  192 ? 35.343  -68.120  -62.228  1.00 50.06  ? 192 HIS   A CA     1 
ATOM   1471  C  C      . HIS   A 1  192 ? 36.575  -68.899  -61.757  1.00 51.85  ? 192 HIS   A C      1 
ATOM   1472  O  O      . HIS   A 1  192 ? 37.487  -69.174  -62.543  1.00 61.95  ? 192 HIS   A O      1 
ATOM   1473  C  CB     . HIS   A 1  192 ? 35.394  -66.671  -61.764  1.00 47.30  ? 192 HIS   A CB     1 
ATOM   1474  C  CG     . HIS   A 1  192 ? 36.760  -66.076  -61.796  1.00 55.81  ? 192 HIS   A CG     1 
ATOM   1475  N  ND1    . HIS   A 1  192 ? 37.561  -66.115  -62.918  1.00 57.16  ? 192 HIS   A ND1    1 
ATOM   1476  C  CD2    . HIS   A 1  192 ? 37.453  -65.388  -60.859  1.00 54.43  ? 192 HIS   A CD2    1 
ATOM   1477  C  CE1    . HIS   A 1  192 ? 38.697  -65.489  -62.662  1.00 60.98  ? 192 HIS   A CE1    1 
ATOM   1478  N  NE2    . HIS   A 1  192 ? 38.654  -65.034  -61.422  1.00 56.11  ? 192 HIS   A NE2    1 
ATOM   1479  N  N      . THR   A 1  193 ? 36.618  -69.279  -60.493  1.00 46.97  ? 193 THR   A N      1 
ATOM   1480  C  CA     . THR   A 1  193 ? 37.780  -69.970  -59.958  1.00 50.03  ? 193 THR   A CA     1 
ATOM   1481  C  C      . THR   A 1  193 ? 37.792  -71.460  -60.285  1.00 51.85  ? 193 THR   A C      1 
ATOM   1482  O  O      . THR   A 1  193 ? 38.839  -72.096  -60.129  1.00 52.62  ? 193 THR   A O      1 
ATOM   1483  C  CB     . THR   A 1  193 ? 37.841  -69.755  -58.434  1.00 50.05  ? 193 THR   A CB     1 
ATOM   1484  O  OG1    . THR   A 1  193 ? 37.892  -68.349  -58.153  1.00 54.43  ? 193 THR   A OG1    1 
ATOM   1485  C  CG2    . THR   A 1  193 ? 39.055  -70.454  -57.792  1.00 49.98  ? 193 THR   A CG2    1 
ATOM   1486  N  N      . THR   A 1  194 ? 36.664  -72.040  -60.709  1.00 52.18  ? 194 THR   A N      1 
ATOM   1487  C  CA     . THR   A 1  194 ? 36.612  -73.456  -61.079  1.00 53.08  ? 194 THR   A CA     1 
ATOM   1488  C  C      . THR   A 1  194 ? 36.651  -73.675  -62.588  1.00 53.34  ? 194 THR   A C      1 
ATOM   1489  O  O      . THR   A 1  194 ? 36.919  -74.799  -63.023  1.00 53.91  ? 194 THR   A O      1 
ATOM   1490  C  CB     . THR   A 1  194 ? 35.341  -74.149  -60.514  1.00 46.15  ? 194 THR   A CB     1 
ATOM   1491  O  OG1    . THR   A 1  194 ? 35.264  -73.991  -59.092  1.00 46.30  ? 194 THR   A OG1    1 
ATOM   1492  C  CG2    . THR   A 1  194 ? 35.351  -75.638  -60.804  1.00 46.72  ? 194 THR   A CG2    1 
ATOM   1493  N  N      . LEU   A 1  195 ? 36.419  -72.632  -63.392  1.00 50.79  ? 195 LEU   A N      1 
ATOM   1494  C  CA     . LEU   A 1  195 ? 36.185  -72.823  -64.823  1.00 48.32  ? 195 LEU   A CA     1 
ATOM   1495  C  C      . LEU   A 1  195 ? 37.253  -73.701  -65.462  1.00 51.58  ? 195 LEU   A C      1 
ATOM   1496  O  O      . LEU   A 1  195 ? 36.953  -74.781  -65.978  1.00 57.74  ? 195 LEU   A O      1 
ATOM   1497  C  CB     . LEU   A 1  195 ? 36.088  -71.471  -65.517  1.00 44.48  ? 195 LEU   A CB     1 
ATOM   1498  C  CG     . LEU   A 1  195 ? 35.333  -71.505  -66.840  1.00 50.68  ? 195 LEU   A CG     1 
ATOM   1499  C  CD1    . LEU   A 1  195 ? 34.055  -72.363  -66.795  1.00 46.94  ? 195 LEU   A CD1    1 
ATOM   1500  C  CD2    . LEU   A 1  195 ? 35.015  -70.071  -67.262  1.00 49.43  ? 195 LEU   A CD2    1 
ATOM   1501  N  N      . GLU   A 1  196 ? 38.513  -73.279  -65.399  1.00 56.93  ? 196 GLU   A N      1 
ATOM   1502  C  CA     . GLU   A 1  196 ? 39.600  -74.018  -66.036  1.00 58.02  ? 196 GLU   A CA     1 
ATOM   1503  C  C      . GLU   A 1  196 ? 39.987  -75.306  -65.312  1.00 51.16  ? 196 GLU   A C      1 
ATOM   1504  O  O      . GLU   A 1  196 ? 40.939  -75.966  -65.732  1.00 63.01  ? 196 GLU   A O      1 
ATOM   1505  C  CB     . GLU   A 1  196 ? 40.821  -73.105  -66.177  1.00 64.38  ? 196 GLU   A CB     1 
ATOM   1506  C  CG     . GLU   A 1  196 ? 40.757  -72.157  -67.390  1.00 66.91  ? 196 GLU   A CG     1 
ATOM   1507  C  CD     . GLU   A 1  196 ? 41.758  -70.994  -67.289  1.00 89.38  ? 196 GLU   A CD     1 
ATOM   1508  O  OE1    . GLU   A 1  196 ? 42.524  -70.958  -66.287  1.00 91.33  ? 196 GLU   A OE1    1 
ATOM   1509  O  OE2    . GLU   A 1  196 ? 41.765  -70.114  -68.197  1.00 78.21  ? 196 GLU   A OE2    1 
ATOM   1510  N  N      . HIS   A 1  197 ? 39.289  -75.707  -64.264  1.00 49.35  ? 197 HIS   A N      1 
ATOM   1511  C  CA     . HIS   A 1  197 ? 39.599  -76.937  -63.553  1.00 50.39  ? 197 HIS   A CA     1 
ATOM   1512  C  C      . HIS   A 1  197 ? 38.572  -78.016  -63.789  1.00 53.26  ? 197 HIS   A C      1 
ATOM   1513  O  O      . HIS   A 1  197 ? 38.803  -79.167  -63.396  1.00 58.24  ? 197 HIS   A O      1 
ATOM   1514  C  CB     . HIS   A 1  197 ? 39.692  -76.682  -62.042  1.00 55.55  ? 197 HIS   A CB     1 
ATOM   1515  C  CG     . HIS   A 1  197 ? 40.700  -75.642  -61.668  1.00 58.80  ? 197 HIS   A CG     1 
ATOM   1516  N  ND1    . HIS   A 1  197 ? 41.920  -75.956  -61.116  1.00 59.27  ? 197 HIS   A ND1    1 
ATOM   1517  C  CD2    . HIS   A 1  197 ? 40.683  -74.294  -61.806  1.00 54.83  ? 197 HIS   A CD2    1 
ATOM   1518  C  CE1    . HIS   A 1  197 ? 42.605  -74.845  -60.916  1.00 66.73  ? 197 HIS   A CE1    1 
ATOM   1519  N  NE2    . HIS   A 1  197 ? 41.876  -73.822  -61.326  1.00 57.95  ? 197 HIS   A NE2    1 
ATOM   1520  N  N      . SER   A 1  198 ? 37.440  -77.668  -64.386  1.00 52.33  ? 198 SER   A N      1 
ATOM   1521  C  CA     . SER   A 1  198 ? 36.351  -78.595  -64.629  1.00 51.01  ? 198 SER   A CA     1 
ATOM   1522  C  C      . SER   A 1  198 ? 36.314  -78.966  -66.101  1.00 50.31  ? 198 SER   A C      1 
ATOM   1523  O  O      . SER   A 1  198 ? 36.300  -78.087  -66.973  1.00 55.25  ? 198 SER   A O      1 
ATOM   1524  C  CB     . SER   A 1  198 ? 35.022  -77.979  -64.215  1.00 49.46  ? 198 SER   A CB     1 
ATOM   1525  O  OG     . SER   A 1  198 ? 34.040  -78.983  -64.123  1.00 52.58  ? 198 SER   A OG     1 
ATOM   1526  N  N      . ASP   A 1  199 ? 36.278  -80.260  -66.380  1.00 46.44  ? 199 ASP   A N      1 
ATOM   1527  C  CA     . ASP   A 1  199 ? 36.275  -80.663  -67.782  1.00 57.03  ? 199 ASP   A CA     1 
ATOM   1528  C  C      . ASP   A 1  199 ? 34.870  -80.627  -68.386  1.00 56.44  ? 199 ASP   A C      1 
ATOM   1529  O  O      . ASP   A 1  199 ? 34.709  -80.284  -69.568  1.00 48.87  ? 199 ASP   A O      1 
ATOM   1530  C  CB     . ASP   A 1  199 ? 36.916  -82.043  -67.908  1.00 56.14  ? 199 ASP   A CB     1 
ATOM   1531  C  CG     . ASP   A 1  199 ? 38.348  -82.059  -67.382  1.00 55.03  ? 199 ASP   A CG     1 
ATOM   1532  O  OD1    . ASP   A 1  199 ? 39.159  -81.241  -67.897  1.00 52.26  ? 199 ASP   A OD1    1 
ATOM   1533  O  OD2    . ASP   A 1  199 ? 38.641  -82.860  -66.446  1.00 54.10  ? 199 ASP   A OD2    1 
ATOM   1534  N  N      . CYS   A 1  200 ? 33.851  -80.901  -67.572  1.00 52.48  ? 200 CYS   A N      1 
ATOM   1535  C  CA     . CYS   A 1  200 ? 32.470  -80.930  -68.025  1.00 48.62  ? 200 CYS   A CA     1 
ATOM   1536  C  C      . CYS   A 1  200 ? 31.578  -80.713  -66.811  1.00 47.19  ? 200 CYS   A C      1 
ATOM   1537  O  O      . CYS   A 1  200 ? 31.782  -81.344  -65.766  1.00 49.88  ? 200 CYS   A O      1 
ATOM   1538  C  CB     . CYS   A 1  200 ? 32.174  -82.273  -68.706  1.00 43.76  ? 200 CYS   A CB     1 
ATOM   1539  S  SG     . CYS   A 1  200 ? 30.538  -82.416  -69.401  1.00 48.50  ? 200 CYS   A SG     1 
ATOM   1540  N  N      . ALA   A 1  201 ? 30.596  -79.835  -66.930  1.00 45.14  ? 201 ALA   A N      1 
ATOM   1541  C  CA     . ALA   A 1  201 ? 29.728  -79.577  -65.790  1.00 44.50  ? 201 ALA   A CA     1 
ATOM   1542  C  C      . ALA   A 1  201 ? 28.279  -79.617  -66.237  1.00 40.13  ? 201 ALA   A C      1 
ATOM   1543  O  O      . ALA   A 1  201 ? 27.912  -78.968  -67.224  1.00 43.01  ? 201 ALA   A O      1 
ATOM   1544  C  CB     . ALA   A 1  201 ? 30.064  -78.230  -65.150  1.00 40.86  ? 201 ALA   A CB     1 
ATOM   1545  N  N      . PHE   A 1  202 ? 27.460  -80.370  -65.515  1.00 34.43  ? 202 PHE   A N      1 
ATOM   1546  C  CA     . PHE   A 1  202 ? 26.020  -80.412  -65.770  1.00 39.39  ? 202 PHE   A CA     1 
ATOM   1547  C  C      . PHE   A 1  202 ? 25.312  -79.551  -64.719  1.00 43.89  ? 202 PHE   A C      1 
ATOM   1548  O  O      . PHE   A 1  202 ? 25.351  -79.865  -63.523  1.00 36.19  ? 202 PHE   A O      1 
ATOM   1549  C  CB     . PHE   A 1  202 ? 25.495  -81.849  -65.750  1.00 40.92  ? 202 PHE   A CB     1 
ATOM   1550  C  CG     . PHE   A 1  202 ? 26.232  -82.786  -66.681  1.00 40.81  ? 202 PHE   A CG     1 
ATOM   1551  C  CD1    . PHE   A 1  202 ? 25.955  -82.799  -68.029  1.00 38.22  ? 202 PHE   A CD1    1 
ATOM   1552  C  CD2    . PHE   A 1  202 ? 27.205  -83.659  -66.196  1.00 42.12  ? 202 PHE   A CD2    1 
ATOM   1553  C  CE1    . PHE   A 1  202 ? 26.649  -83.658  -68.888  1.00 41.58  ? 202 PHE   A CE1    1 
ATOM   1554  C  CE2    . PHE   A 1  202 ? 27.895  -84.509  -67.049  1.00 42.46  ? 202 PHE   A CE2    1 
ATOM   1555  C  CZ     . PHE   A 1  202 ? 27.609  -84.510  -68.398  1.00 40.49  ? 202 PHE   A CZ     1 
ATOM   1556  N  N      . MET   A 1  203 ? 24.681  -78.455  -65.165  1.00 44.15  ? 203 MET   A N      1 
ATOM   1557  C  CA     . MET   A 1  203 ? 23.947  -77.575  -64.265  1.00 34.34  ? 203 MET   A CA     1 
ATOM   1558  C  C      . MET   A 1  203 ? 22.533  -78.080  -64.084  1.00 39.66  ? 203 MET   A C      1 
ATOM   1559  O  O      . MET   A 1  203 ? 21.894  -78.522  -65.036  1.00 43.39  ? 203 MET   A O      1 
ATOM   1560  C  CB     . MET   A 1  203 ? 23.865  -76.161  -64.809  1.00 34.75  ? 203 MET   A CB     1 
ATOM   1561  C  CG     . MET   A 1  203 ? 25.182  -75.467  -64.945  1.00 49.45  ? 203 MET   A CG     1 
ATOM   1562  S  SD     . MET   A 1  203 ? 24.993  -73.696  -64.833  1.00 61.46  ? 203 MET   A SD     1 
ATOM   1563  C  CE     . MET   A 1  203 ? 24.717  -73.290  -66.554  1.00 37.26  ? 203 MET   A CE     1 
ATOM   1564  N  N      . VAL   A 1  204 ? 22.025  -77.972  -62.866  1.00 40.64  ? 204 VAL   A N      1 
ATOM   1565  C  CA     . VAL   A 1  204 ? 20.645  -78.310  -62.568  1.00 40.59  ? 204 VAL   A CA     1 
ATOM   1566  C  C      . VAL   A 1  204 ? 20.062  -77.113  -61.835  1.00 39.97  ? 204 VAL   A C      1 
ATOM   1567  O  O      . VAL   A 1  204 ? 20.279  -76.950  -60.633  1.00 47.66  ? 204 VAL   A O      1 
ATOM   1568  C  CB     . VAL   A 1  204 ? 20.526  -79.589  -61.739  1.00 41.42  ? 204 VAL   A CB     1 
ATOM   1569  C  CG1    . VAL   A 1  204 ? 19.086  -79.920  -61.492  1.00 38.62  ? 204 VAL   A CG1    1 
ATOM   1570  C  CG2    . VAL   A 1  204 ? 21.220  -80.723  -62.480  1.00 41.97  ? 204 VAL   A CG2    1 
ATOM   1571  N  N      . ASP   A 1  205 ? 19.346  -76.257  -62.555  1.00 42.54  ? 205 ASP   A N      1 
ATOM   1572  C  CA     . ASP   A 1  205 ? 18.674  -75.123  -61.933  1.00 39.80  ? 205 ASP   A CA     1 
ATOM   1573  C  C      . ASP   A 1  205 ? 17.505  -75.631  -61.090  1.00 35.73  ? 205 ASP   A C      1 
ATOM   1574  O  O      . ASP   A 1  205 ? 16.552  -76.194  -61.634  1.00 34.12  ? 205 ASP   A O      1 
ATOM   1575  C  CB     . ASP   A 1  205 ? 18.213  -74.144  -63.014  1.00 31.96  ? 205 ASP   A CB     1 
ATOM   1576  C  CG     . ASP   A 1  205 ? 17.546  -72.896  -62.442  1.00 40.37  ? 205 ASP   A CG     1 
ATOM   1577  O  OD1    . ASP   A 1  205 ? 17.213  -72.865  -61.224  1.00 34.34  ? 205 ASP   A OD1    1 
ATOM   1578  O  OD2    . ASP   A 1  205 ? 17.357  -71.927  -63.228  1.00 46.52  ? 205 ASP   A OD2    1 
ATOM   1579  N  N      . ASN   A 1  206 ? 17.585  -75.432  -59.760  1.00 31.73  ? 206 ASN   A N      1 
ATOM   1580  C  CA     . ASN   A 1  206 ? 16.524  -75.875  -58.855  1.00 32.71  ? 206 ASN   A CA     1 
ATOM   1581  C  C      . ASN   A 1  206 ? 15.148  -75.383  -59.287  1.00 39.74  ? 206 ASN   A C      1 
ATOM   1582  O  O      . ASN   A 1  206 ? 14.135  -76.028  -58.994  1.00 35.59  ? 206 ASN   A O      1 
ATOM   1583  C  CB     . ASN   A 1  206 ? 16.799  -75.410  -57.435  1.00 29.58  ? 206 ASN   A CB     1 
ATOM   1584  C  CG     . ASN   A 1  206 ? 17.446  -76.488  -56.585  1.00 35.24  ? 206 ASN   A CG     1 
ATOM   1585  O  OD1    . ASN   A 1  206 ? 17.563  -77.639  -57.003  1.00 38.26  ? 206 ASN   A OD1    1 
ATOM   1586  N  ND2    . ASN   A 1  206 ? 17.891  -76.115  -55.395  1.00 32.27  ? 206 ASN   A ND2    1 
ATOM   1587  N  N      . GLU   A 1  207 ? 15.081  -74.246  -59.977  1.00 37.24  ? 207 GLU   A N      1 
ATOM   1588  C  CA     . GLU   A 1  207 ? 13.805  -73.804  -60.506  1.00 34.92  ? 207 GLU   A CA     1 
ATOM   1589  C  C      . GLU   A 1  207 ? 13.203  -74.865  -61.424  1.00 43.50  ? 207 GLU   A C      1 
ATOM   1590  O  O      . GLU   A 1  207 ? 12.016  -75.196  -61.309  1.00 47.36  ? 207 GLU   A O      1 
ATOM   1591  C  CB     . GLU   A 1  207 ? 13.994  -72.484  -61.231  1.00 34.89  ? 207 GLU   A CB     1 
ATOM   1592  C  CG     . GLU   A 1  207 ? 12.755  -71.907  -61.785  1.00 36.05  ? 207 GLU   A CG     1 
ATOM   1593  C  CD     . GLU   A 1  207 ? 13.040  -70.866  -62.832  1.00 39.93  ? 207 GLU   A CD     1 
ATOM   1594  O  OE1    . GLU   A 1  207 ? 13.694  -71.191  -63.847  1.00 51.53  ? 207 GLU   A OE1    1 
ATOM   1595  O  OE2    . GLU   A 1  207 ? 12.652  -69.708  -62.621  1.00 40.33  ? 207 GLU   A OE2    1 
ATOM   1596  N  N      . ALA   A 1  208 ? 14.014  -75.430  -62.333  1.00 42.06  ? 208 ALA   A N      1 
ATOM   1597  C  CA     . ALA   A 1  208 ? 13.483  -76.382  -63.311  1.00 36.43  ? 208 ALA   A CA     1 
ATOM   1598  C  C      . ALA   A 1  208 ? 13.023  -77.661  -62.631  1.00 38.03  ? 208 ALA   A C      1 
ATOM   1599  O  O      . ALA   A 1  208 ? 11.919  -78.147  -62.895  1.00 42.32  ? 208 ALA   A O      1 
ATOM   1600  C  CB     . ALA   A 1  208 ? 14.521  -76.693  -64.386  1.00 28.87  ? 208 ALA   A CB     1 
ATOM   1601  N  N      . ILE   A 1  209 ? 13.858  -78.219  -61.750  1.00 34.01  ? 209 ILE   A N      1 
ATOM   1602  C  CA     . ILE   A 1  209 ? 13.499  -79.443  -61.046  1.00 34.27  ? 209 ILE   A CA     1 
ATOM   1603  C  C      . ILE   A 1  209 ? 12.235  -79.242  -60.225  1.00 42.21  ? 209 ILE   A C      1 
ATOM   1604  O  O      . ILE   A 1  209 ? 11.399  -80.150  -60.110  1.00 45.73  ? 209 ILE   A O      1 
ATOM   1605  C  CB     . ILE   A 1  209 ? 14.666  -79.902  -60.161  1.00 41.85  ? 209 ILE   A CB     1 
ATOM   1606  C  CG1    . ILE   A 1  209 ? 15.883  -80.094  -61.025  1.00 42.77  ? 209 ILE   A CG1    1 
ATOM   1607  C  CG2    . ILE   A 1  209 ? 14.332  -81.206  -59.489  1.00 42.32  ? 209 ILE   A CG2    1 
ATOM   1608  C  CD1    . ILE   A 1  209 ? 15.560  -80.888  -62.218  1.00 35.90  ? 209 ILE   A CD1    1 
ATOM   1609  N  N      . TYR   A 1  210 ? 12.087  -78.061  -59.625  1.00 36.59  ? 210 TYR   A N      1 
ATOM   1610  C  CA     . TYR   A 1  210 ? 10.943  -77.792  -58.768  1.00 41.38  ? 210 TYR   A CA     1 
ATOM   1611  C  C      . TYR   A 1  210 ? 9.655   -77.796  -59.561  1.00 45.29  ? 210 TYR   A C      1 
ATOM   1612  O  O      . TYR   A 1  210 ? 8.639   -78.332  -59.103  1.00 44.08  ? 210 TYR   A O      1 
ATOM   1613  C  CB     . TYR   A 1  210 ? 11.120  -76.442  -58.102  1.00 42.60  ? 210 TYR   A CB     1 
ATOM   1614  C  CG     . TYR   A 1  210 ? 10.155  -76.093  -57.013  1.00 40.26  ? 210 TYR   A CG     1 
ATOM   1615  C  CD1    . TYR   A 1  210 ? 10.331  -76.576  -55.730  1.00 44.07  ? 210 TYR   A CD1    1 
ATOM   1616  C  CD2    . TYR   A 1  210 ? 9.139   -75.187  -57.238  1.00 50.80  ? 210 TYR   A CD2    1 
ATOM   1617  C  CE1    . TYR   A 1  210 ? 9.482   -76.211  -54.707  1.00 45.69  ? 210 TYR   A CE1    1 
ATOM   1618  C  CE2    . TYR   A 1  210 ? 8.289   -74.800  -56.228  1.00 50.54  ? 210 TYR   A CE2    1 
ATOM   1619  C  CZ     . TYR   A 1  210 ? 8.461   -75.318  -54.963  1.00 51.07  ? 210 TYR   A CZ     1 
ATOM   1620  O  OH     . TYR   A 1  210 ? 7.599   -74.948  -53.953  1.00 58.66  ? 210 TYR   A OH     1 
ATOM   1621  N  N      . ASP   A 1  211 ? 9.669   -77.192  -60.747  1.00 42.31  ? 211 ASP   A N      1 
ATOM   1622  C  CA     . ASP   A 1  211 ? 8.434   -77.123  -61.503  1.00 43.33  ? 211 ASP   A CA     1 
ATOM   1623  C  C      . ASP   A 1  211 ? 8.123   -78.432  -62.207  1.00 48.27  ? 211 ASP   A C      1 
ATOM   1624  O  O      . ASP   A 1  211 ? 6.944   -78.757  -62.376  1.00 49.39  ? 211 ASP   A O      1 
ATOM   1625  C  CB     . ASP   A 1  211 ? 8.494   -75.973  -62.487  1.00 49.19  ? 211 ASP   A CB     1 
ATOM   1626  C  CG     . ASP   A 1  211 ? 7.994   -74.723  -61.868  1.00 67.65  ? 211 ASP   A CG     1 
ATOM   1627  O  OD1    . ASP   A 1  211 ? 6.992   -74.837  -61.122  1.00 69.60  ? 211 ASP   A OD1    1 
ATOM   1628  O  OD2    . ASP   A 1  211 ? 8.597   -73.641  -62.084  1.00 70.14  ? 211 ASP   A OD2    1 
ATOM   1629  N  N      . ILE   A 1  212 ? 9.142   -79.208  -62.605  1.00 42.85  ? 212 ILE   A N      1 
ATOM   1630  C  CA     . ILE   A 1  212 ? 8.874   -80.577  -63.040  1.00 43.34  ? 212 ILE   A CA     1 
ATOM   1631  C  C      . ILE   A 1  212 ? 8.200   -81.353  -61.921  1.00 46.82  ? 212 ILE   A C      1 
ATOM   1632  O  O      . ILE   A 1  212 ? 7.275   -82.139  -62.159  1.00 49.40  ? 212 ILE   A O      1 
ATOM   1633  C  CB     . ILE   A 1  212 ? 10.162  -81.281  -63.501  1.00 38.49  ? 212 ILE   A CB     1 
ATOM   1634  C  CG1    . ILE   A 1  212 ? 10.584  -80.774  -64.871  1.00 34.77  ? 212 ILE   A CG1    1 
ATOM   1635  C  CG2    . ILE   A 1  212 ? 9.947   -82.780  -63.509  1.00 28.52  ? 212 ILE   A CG2    1 
ATOM   1636  C  CD1    . ILE   A 1  212 ? 12.069  -80.804  -65.075  1.00 33.30  ? 212 ILE   A CD1    1 
ATOM   1637  N  N      . CYS   A 1  213 ? 8.638   -81.131  -60.677  1.00 46.18  ? 213 CYS   A N      1 
ATOM   1638  C  CA     . CYS   A 1  213 ? 8.047   -81.855  -59.559  1.00 47.13  ? 213 CYS   A CA     1 
ATOM   1639  C  C      . CYS   A 1  213 ? 6.604   -81.436  -59.304  1.00 51.24  ? 213 CYS   A C      1 
ATOM   1640  O  O      . CYS   A 1  213 ? 5.799   -82.263  -58.863  1.00 56.16  ? 213 CYS   A O      1 
ATOM   1641  C  CB     . CYS   A 1  213 ? 8.880   -81.661  -58.294  1.00 45.85  ? 213 CYS   A CB     1 
ATOM   1642  S  SG     . CYS   A 1  213 ? 10.290  -82.779  -58.176  1.00 45.32  ? 213 CYS   A SG     1 
ATOM   1643  N  N      . ARG   A 1  214 ? 6.252   -80.172  -59.561  1.00 46.39  ? 214 ARG   A N      1 
ATOM   1644  C  CA     . ARG   A 1  214 ? 4.878   -79.734  -59.332  1.00 48.53  ? 214 ARG   A CA     1 
ATOM   1645  C  C      . ARG   A 1  214 ? 3.956   -80.196  -60.458  1.00 52.45  ? 214 ARG   A C      1 
ATOM   1646  O  O      . ARG   A 1  214 ? 2.957   -80.885  -60.209  1.00 53.56  ? 214 ARG   A O      1 
ATOM   1647  C  CB     . ARG   A 1  214 ? 4.821   -78.213  -59.189  1.00 55.42  ? 214 ARG   A CB     1 
ATOM   1648  C  CG     . ARG   A 1  214 ? 5.156   -77.698  -57.803  1.00 54.86  ? 214 ARG   A CG     1 
ATOM   1649  C  CD     . ARG   A 1  214 ? 5.429   -76.216  -57.866  1.00 54.98  ? 214 ARG   A CD     1 
ATOM   1650  N  NE     . ARG   A 1  214 ? 4.455   -75.547  -58.721  1.00 71.39  ? 214 ARG   A NE     1 
ATOM   1651  C  CZ     . ARG   A 1  214 ? 4.365   -74.231  -58.884  1.00 82.47  ? 214 ARG   A CZ     1 
ATOM   1652  N  NH1    . ARG   A 1  214 ? 5.189   -73.391  -58.259  1.00 65.58  ? 214 ARG   A NH1    1 
ATOM   1653  N  NH2    . ARG   A 1  214 ? 3.429   -73.743  -59.699  1.00 77.06  ? 214 ARG   A NH2    1 
ATOM   1654  N  N      . ARG   A 1  215 ? 4.288   -79.821  -61.702  1.00 44.78  ? 215 ARG   A N      1 
ATOM   1655  C  CA     . ARG   A 1  215 ? 3.585   -80.225  -62.914  1.00 47.52  ? 215 ARG   A CA     1 
ATOM   1656  C  C      . ARG   A 1  215 ? 3.439   -81.736  -63.046  1.00 52.16  ? 215 ARG   A C      1 
ATOM   1657  O  O      . ARG   A 1  215 ? 2.334   -82.281  -62.953  1.00 58.82  ? 215 ARG   A O      1 
ATOM   1658  C  CB     . ARG   A 1  215 ? 4.324   -79.734  -64.152  1.00 50.54  ? 215 ARG   A CB     1 
ATOM   1659  C  CG     . ARG   A 1  215 ? 3.992   -78.367  -64.659  1.00 53.17  ? 215 ARG   A CG     1 
ATOM   1660  C  CD     . ARG   A 1  215 ? 4.487   -78.234  -66.123  1.00 54.04  ? 215 ARG   A CD     1 
ATOM   1661  N  NE     . ARG   A 1  215 ? 5.798   -77.596  -66.180  1.00 60.54  ? 215 ARG   A NE     1 
ATOM   1662  C  CZ     . ARG   A 1  215 ? 6.939   -78.235  -66.420  1.00 61.00  ? 215 ARG   A CZ     1 
ATOM   1663  N  NH1    . ARG   A 1  215 ? 6.960   -79.525  -66.733  1.00 58.90  ? 215 ARG   A NH1    1 
ATOM   1664  N  NH2    . ARG   A 1  215 ? 8.089   -77.563  -66.344  1.00 53.14  ? 215 ARG   A NH2    1 
ATOM   1665  N  N      . ASN   A 1  216 ? 4.553   -82.423  -63.282  1.00 52.74  ? 216 ASN   A N      1 
ATOM   1666  C  CA     . ASN   A 1  216 ? 4.494   -83.808  -63.730  1.00 49.71  ? 216 ASN   A CA     1 
ATOM   1667  C  C      . ASN   A 1  216 ? 4.393   -84.802  -62.578  1.00 52.72  ? 216 ASN   A C      1 
ATOM   1668  O  O      . ASN   A 1  216 ? 4.127   -85.985  -62.825  1.00 51.03  ? 216 ASN   A O      1 
ATOM   1669  C  CB     . ASN   A 1  216 ? 5.700   -84.094  -64.635  1.00 34.50  ? 216 ASN   A CB     1 
ATOM   1670  C  CG     . ASN   A 1  216 ? 5.739   -83.153  -65.845  1.00 39.84  ? 216 ASN   A CG     1 
ATOM   1671  O  OD1    . ASN   A 1  216 ? 4.741   -82.519  -66.153  1.00 53.86  ? 216 ASN   A OD1    1 
ATOM   1672  N  ND2    . ASN   A 1  216 ? 6.882   -83.040  -66.510  1.00 46.93  ? 216 ASN   A ND2    1 
ATOM   1673  N  N      . LEU   A 1  217 ? 4.539   -84.350  -61.326  1.00 49.34  ? 217 LEU   A N      1 
ATOM   1674  C  CA     . LEU   A 1  217 ? 4.384   -85.233  -60.181  1.00 47.34  ? 217 LEU   A CA     1 
ATOM   1675  C  C      . LEU   A 1  217 ? 3.233   -84.847  -59.278  1.00 50.50  ? 217 LEU   A C      1 
ATOM   1676  O  O      . LEU   A 1  217 ? 2.929   -85.600  -58.347  1.00 47.47  ? 217 LEU   A O      1 
ATOM   1677  C  CB     . LEU   A 1  217 ? 5.670   -85.281  -59.348  1.00 44.51  ? 217 LEU   A CB     1 
ATOM   1678  C  CG     . LEU   A 1  217 ? 6.888   -85.861  -60.063  1.00 48.69  ? 217 LEU   A CG     1 
ATOM   1679  C  CD1    . LEU   A 1  217 ? 8.083   -85.859  -59.138  1.00 44.46  ? 217 LEU   A CD1    1 
ATOM   1680  C  CD2    . LEU   A 1  217 ? 6.607   -87.267  -60.601  1.00 46.17  ? 217 LEU   A CD2    1 
ATOM   1681  N  N      . ASP   A 1  218 ? 2.584   -83.708  -59.521  1.00 55.63  ? 218 ASP   A N      1 
ATOM   1682  C  CA     . ASP   A 1  218 ? 1.489   -83.245  -58.665  1.00 60.01  ? 218 ASP   A CA     1 
ATOM   1683  C  C      . ASP   A 1  218 ? 1.939   -83.138  -57.214  1.00 56.54  ? 218 ASP   A C      1 
ATOM   1684  O  O      . ASP   A 1  218 ? 1.218   -83.527  -56.294  1.00 55.66  ? 218 ASP   A O      1 
ATOM   1685  C  CB     . ASP   A 1  218 ? 0.268   -84.163  -58.768  1.00 58.20  ? 218 ASP   A CB     1 
ATOM   1686  C  CG     . ASP   A 1  218 ? -0.174  -84.384  -60.193  1.00 69.04  ? 218 ASP   A CG     1 
ATOM   1687  O  OD1    . ASP   A 1  218 ? -0.323  -83.377  -60.927  1.00 72.62  ? 218 ASP   A OD1    1 
ATOM   1688  O  OD2    . ASP   A 1  218 ? -0.360  -85.567  -60.574  1.00 69.43  ? 218 ASP   A OD2    1 
ATOM   1689  N  N      . ILE   A 1  219 ? 3.152   -82.645  -57.010  1.00 53.58  ? 219 ILE   A N      1 
ATOM   1690  C  CA     . ILE   A 1  219 ? 3.662   -82.333  -55.684  1.00 51.41  ? 219 ILE   A CA     1 
ATOM   1691  C  C      . ILE   A 1  219 ? 3.496   -80.834  -55.474  1.00 55.84  ? 219 ILE   A C      1 
ATOM   1692  O  O      . ILE   A 1  219 ? 4.046   -80.027  -56.235  1.00 54.94  ? 219 ILE   A O      1 
ATOM   1693  C  CB     . ILE   A 1  219 ? 5.124   -82.765  -55.531  1.00 52.75  ? 219 ILE   A CB     1 
ATOM   1694  C  CG1    . ILE   A 1  219 ? 5.237   -84.271  -55.760  1.00 55.96  ? 219 ILE   A CG1    1 
ATOM   1695  C  CG2    . ILE   A 1  219 ? 5.658   -82.384  -54.166  1.00 48.68  ? 219 ILE   A CG2    1 
ATOM   1696  C  CD1    . ILE   A 1  219 ? 6.492   -84.682  -56.491  1.00 54.90  ? 219 ILE   A CD1    1 
ATOM   1697  N  N      . GLU   A 1  220 ? 2.715   -80.468  -54.455  1.00 60.98  ? 220 GLU   A N      1 
ATOM   1698  C  CA     . GLU   A 1  220 ? 2.342   -79.086  -54.181  1.00 61.19  ? 220 GLU   A CA     1 
ATOM   1699  C  C      . GLU   A 1  220 ? 3.563   -78.220  -53.900  1.00 61.15  ? 220 GLU   A C      1 
ATOM   1700  O  O      . GLU   A 1  220 ? 3.873   -77.312  -54.679  1.00 56.50  ? 220 GLU   A O      1 
ATOM   1701  C  CB     . GLU   A 1  220 ? 1.380   -79.024  -52.997  1.00 58.19  ? 220 GLU   A CB     1 
ATOM   1702  C  CG     . GLU   A 1  220 ? 0.048   -78.415  -53.325  1.00 68.25  ? 220 GLU   A CG     1 
ATOM   1703  C  CD     . GLU   A 1  220 ? -0.890  -78.437  -52.137  1.00 80.04  ? 220 GLU   A CD     1 
ATOM   1704  O  OE1    . GLU   A 1  220 ? -0.541  -77.824  -51.100  1.00 80.26  ? 220 GLU   A OE1    1 
ATOM   1705  O  OE2    . GLU   A 1  220 ? -1.964  -79.075  -52.233  1.00 76.09  ? 220 GLU   A OE2    1 
ATOM   1706  N  N      . ARG   A 1  221 ? 4.243   -78.466  -52.777  1.00 58.62  ? 221 ARG   A N      1 
ATOM   1707  C  CA     . ARG   A 1  221 ? 5.489   -77.777  -52.457  1.00 55.91  ? 221 ARG   A CA     1 
ATOM   1708  C  C      . ARG   A 1  221 ? 6.587   -78.830  -52.415  1.00 51.03  ? 221 ARG   A C      1 
ATOM   1709  O  O      . ARG   A 1  221 ? 6.812   -79.456  -51.371  1.00 53.26  ? 221 ARG   A O      1 
ATOM   1710  C  CB     . ARG   A 1  221 ? 5.386   -76.996  -51.144  1.00 57.41  ? 221 ARG   A CB     1 
ATOM   1711  C  CG     . ARG   A 1  221 ? 6.360   -75.799  -51.102  1.00 66.64  ? 221 ARG   A CG     1 
ATOM   1712  C  CD     . ARG   A 1  221 ? 6.793   -75.343  -49.696  1.00 75.15  ? 221 ARG   A CD     1 
ATOM   1713  N  NE     . ARG   A 1  221 ? 7.979   -74.482  -49.743  1.00 78.29  ? 221 ARG   A NE     1 
ATOM   1714  C  CZ     . ARG   A 1  221 ? 9.180   -74.869  -50.176  1.00 75.98  ? 221 ARG   A CZ     1 
ATOM   1715  N  NH1    . ARG   A 1  221 ? 9.403   -76.104  -50.598  1.00 67.57  ? 221 ARG   A NH1    1 
ATOM   1716  N  NH2    . ARG   A 1  221 ? 10.188  -73.998  -50.176  1.00 73.79  ? 221 ARG   A NH2    1 
ATOM   1717  N  N      . PRO   A 1  222 ? 7.273   -79.073  -53.532  1.00 54.05  ? 222 PRO   A N      1 
ATOM   1718  C  CA     . PRO   A 1  222 ? 8.410   -80.017  -53.547  1.00 53.32  ? 222 PRO   A CA     1 
ATOM   1719  C  C      . PRO   A 1  222 ? 9.429   -79.803  -52.434  1.00 51.30  ? 222 PRO   A C      1 
ATOM   1720  O  O      . PRO   A 1  222 ? 9.899   -78.685  -52.196  1.00 53.14  ? 222 PRO   A O      1 
ATOM   1721  C  CB     . PRO   A 1  222 ? 9.044   -79.764  -54.919  1.00 42.49  ? 222 PRO   A CB     1 
ATOM   1722  C  CG     . PRO   A 1  222 ? 7.865   -79.409  -55.795  1.00 48.45  ? 222 PRO   A CG     1 
ATOM   1723  C  CD     . PRO   A 1  222 ? 6.857   -78.690  -54.896  1.00 51.43  ? 222 PRO   A CD     1 
ATOM   1724  N  N      . THR   A 1  223 ? 9.807   -80.901  -51.778  1.00 51.27  ? 223 THR   A N      1 
ATOM   1725  C  CA     . THR   A 1  223 ? 10.881  -80.914  -50.790  1.00 53.34  ? 223 THR   A CA     1 
ATOM   1726  C  C      . THR   A 1  223 ? 12.230  -81.251  -51.440  1.00 51.90  ? 223 THR   A C      1 
ATOM   1727  O  O      . THR   A 1  223 ? 12.321  -81.590  -52.620  1.00 50.94  ? 223 THR   A O      1 
ATOM   1728  C  CB     . THR   A 1  223 ? 10.571  -81.914  -49.672  1.00 57.66  ? 223 THR   A CB     1 
ATOM   1729  O  OG1    . THR   A 1  223 ? 10.201  -83.183  -50.237  1.00 56.46  ? 223 THR   A OG1    1 
ATOM   1730  C  CG2    . THR   A 1  223 ? 9.447   -81.396  -48.794  1.00 49.80  ? 223 THR   A CG2    1 
ATOM   1731  N  N      . TYR   A 1  224 ? 13.303  -81.157  -50.654  1.00 51.69  ? 224 TYR   A N      1 
ATOM   1732  C  CA     . TYR   A 1  224 ? 14.596  -81.545  -51.208  1.00 50.02  ? 224 TYR   A CA     1 
ATOM   1733  C  C      . TYR   A 1  224 ? 14.610  -83.025  -51.573  1.00 51.85  ? 224 TYR   A C      1 
ATOM   1734  O  O      . TYR   A 1  224 ? 15.255  -83.413  -52.560  1.00 51.91  ? 224 TYR   A O      1 
ATOM   1735  C  CB     . TYR   A 1  224 ? 15.730  -81.223  -50.240  1.00 40.32  ? 224 TYR   A CB     1 
ATOM   1736  C  CG     . TYR   A 1  224 ? 16.134  -79.764  -50.217  1.00 45.26  ? 224 TYR   A CG     1 
ATOM   1737  C  CD1    . TYR   A 1  224 ? 16.178  -78.986  -51.382  1.00 40.14  ? 224 TYR   A CD1    1 
ATOM   1738  C  CD2    . TYR   A 1  224 ? 16.470  -79.162  -49.017  1.00 42.50  ? 224 TYR   A CD2    1 
ATOM   1739  C  CE1    . TYR   A 1  224 ? 16.546  -77.633  -51.321  1.00 37.60  ? 224 TYR   A CE1    1 
ATOM   1740  C  CE2    . TYR   A 1  224 ? 16.834  -77.850  -48.952  1.00 46.05  ? 224 TYR   A CE2    1 
ATOM   1741  C  CZ     . TYR   A 1  224 ? 16.876  -77.083  -50.083  1.00 42.26  ? 224 TYR   A CZ     1 
ATOM   1742  O  OH     . TYR   A 1  224 ? 17.245  -75.764  -49.903  1.00 49.29  ? 224 TYR   A OH     1 
ATOM   1743  N  N      . THR   A 1  225 ? 13.883  -83.865  -50.825  1.00 48.18  ? 225 THR   A N      1 
ATOM   1744  C  CA     . THR   A 1  225 ? 13.890  -85.284  -51.163  1.00 48.99  ? 225 THR   A CA     1 
ATOM   1745  C  C      . THR   A 1  225 ? 13.112  -85.549  -52.445  1.00 54.35  ? 225 THR   A C      1 
ATOM   1746  O  O      . THR   A 1  225 ? 13.468  -86.464  -53.200  1.00 51.86  ? 225 THR   A O      1 
ATOM   1747  C  CB     . THR   A 1  225 ? 13.340  -86.131  -50.013  1.00 48.23  ? 225 THR   A CB     1 
ATOM   1748  O  OG1    . THR   A 1  225 ? 11.919  -86.125  -50.069  1.00 66.61  ? 225 THR   A OG1    1 
ATOM   1749  C  CG2    . THR   A 1  225 ? 13.783  -85.591  -48.653  1.00 48.18  ? 225 THR   A CG2    1 
ATOM   1750  N  N      . ASN   A 1  226 ? 12.069  -84.755  -52.727  1.00 50.41  ? 226 ASN   A N      1 
ATOM   1751  C  CA     . ASN   A 1  226 ? 11.438  -84.827  -54.044  1.00 49.15  ? 226 ASN   A CA     1 
ATOM   1752  C  C      . ASN   A 1  226 ? 12.438  -84.456  -55.132  1.00 49.11  ? 226 ASN   A C      1 
ATOM   1753  O  O      . ASN   A 1  226 ? 12.608  -85.186  -56.109  1.00 51.51  ? 226 ASN   A O      1 
ATOM   1754  C  CB     . ASN   A 1  226 ? 10.218  -83.898  -54.129  1.00 57.36  ? 226 ASN   A CB     1 
ATOM   1755  C  CG     . ASN   A 1  226 ? 9.132   -84.237  -53.123  1.00 57.09  ? 226 ASN   A CG     1 
ATOM   1756  O  OD1    . ASN   A 1  226 ? 8.583   -83.341  -52.480  1.00 55.71  ? 226 ASN   A OD1    1 
ATOM   1757  N  ND2    . ASN   A 1  226 ? 8.815   -85.522  -52.983  1.00 57.63  ? 226 ASN   A ND2    1 
ATOM   1758  N  N      . LEU   A 1  227 ? 13.109  -83.309  -54.975  1.00 50.85  ? 227 LEU   A N      1 
ATOM   1759  C  CA     . LEU   A 1  227 ? 14.041  -82.839  -55.991  1.00 47.43  ? 227 LEU   A CA     1 
ATOM   1760  C  C      . LEU   A 1  227 ? 15.267  -83.725  -56.080  1.00 47.50  ? 227 LEU   A C      1 
ATOM   1761  O  O      . LEU   A 1  227 ? 15.897  -83.824  -57.142  1.00 46.50  ? 227 LEU   A O      1 
ATOM   1762  C  CB     . LEU   A 1  227 ? 14.491  -81.404  -55.701  1.00 47.13  ? 227 LEU   A CB     1 
ATOM   1763  C  CG     . LEU   A 1  227 ? 13.525  -80.262  -55.411  1.00 44.66  ? 227 LEU   A CG     1 
ATOM   1764  C  CD1    . LEU   A 1  227 ? 14.332  -79.019  -55.031  1.00 41.68  ? 227 LEU   A CD1    1 
ATOM   1765  C  CD2    . LEU   A 1  227 ? 12.612  -79.993  -56.618  1.00 44.86  ? 227 LEU   A CD2    1 
ATOM   1766  N  N      . ASN   A 1  228 ? 15.651  -84.347  -54.980  1.00 46.95  ? 228 ASN   A N      1 
ATOM   1767  C  CA     . ASN   A 1  228 ? 16.901  -85.074  -55.051  1.00 47.39  ? 228 ASN   A CA     1 
ATOM   1768  C  C      . ASN   A 1  228 ? 16.708  -86.448  -55.668  1.00 50.78  ? 228 ASN   A C      1 
ATOM   1769  O  O      . ASN   A 1  228 ? 17.571  -86.901  -56.427  1.00 51.75  ? 228 ASN   A O      1 
ATOM   1770  C  CB     . ASN   A 1  228 ? 17.534  -85.138  -53.668  1.00 44.90  ? 228 ASN   A CB     1 
ATOM   1771  C  CG     . ASN   A 1  228 ? 18.180  -83.832  -53.291  1.00 42.44  ? 228 ASN   A CG     1 
ATOM   1772  O  OD1    . ASN   A 1  228 ? 18.477  -83.013  -54.160  1.00 43.16  ? 228 ASN   A OD1    1 
ATOM   1773  N  ND2    . ASN   A 1  228 ? 18.398  -83.619  -51.999  1.00 44.76  ? 228 ASN   A ND2    1 
ATOM   1774  N  N      . ARG   A 1  229 ? 15.572  -87.103  -55.409  1.00 52.15  ? 229 ARG   A N      1 
ATOM   1775  C  CA     . ARG   A 1  229 ? 15.315  -88.374  -56.076  1.00 46.22  ? 229 ARG   A CA     1 
ATOM   1776  C  C      . ARG   A 1  229 ? 15.160  -88.172  -57.577  1.00 47.27  ? 229 ARG   A C      1 
ATOM   1777  O  O      . ARG   A 1  229 ? 15.736  -88.925  -58.371  1.00 46.13  ? 229 ARG   A O      1 
ATOM   1778  C  CB     . ARG   A 1  229 ? 14.094  -89.057  -55.470  1.00 41.71  ? 229 ARG   A CB     1 
ATOM   1779  C  CG     . ARG   A 1  229 ? 14.342  -89.441  -54.018  1.00 52.67  ? 229 ARG   A CG     1 
ATOM   1780  C  CD     . ARG   A 1  229 ? 13.672  -90.736  -53.606  1.00 55.66  ? 229 ARG   A CD     1 
ATOM   1781  N  NE     . ARG   A 1  229 ? 12.795  -90.542  -52.458  1.00 62.26  ? 229 ARG   A NE     1 
ATOM   1782  C  CZ     . ARG   A 1  229 ? 12.586  -91.449  -51.514  1.00 70.52  ? 229 ARG   A CZ     1 
ATOM   1783  N  NH1    . ARG   A 1  229 ? 13.263  -92.588  -51.488  1.00 66.92  ? 229 ARG   A NH1    1 
ATOM   1784  N  NH2    . ARG   A 1  229 ? 11.683  -91.203  -50.565  1.00 76.57  ? 229 ARG   A NH2    1 
ATOM   1785  N  N      . LEU   A 1  230 ? 14.428  -87.134  -57.992  1.00 43.75  ? 230 LEU   A N      1 
ATOM   1786  C  CA     . LEU   A 1  230 ? 14.381  -86.811  -59.414  1.00 41.63  ? 230 LEU   A CA     1 
ATOM   1787  C  C      . LEU   A 1  230 ? 15.763  -86.443  -59.959  1.00 48.15  ? 230 LEU   A C      1 
ATOM   1788  O  O      . LEU   A 1  230 ? 16.120  -86.853  -61.069  1.00 47.89  ? 230 LEU   A O      1 
ATOM   1789  C  CB     . LEU   A 1  230 ? 13.389  -85.684  -59.668  1.00 38.74  ? 230 LEU   A CB     1 
ATOM   1790  C  CG     . LEU   A 1  230 ? 13.455  -85.012  -61.037  1.00 38.46  ? 230 LEU   A CG     1 
ATOM   1791  C  CD1    . LEU   A 1  230 ? 13.152  -85.989  -62.179  1.00 33.66  ? 230 LEU   A CD1    1 
ATOM   1792  C  CD2    . LEU   A 1  230 ? 12.493  -83.850  -61.031  1.00 36.07  ? 230 LEU   A CD2    1 
ATOM   1793  N  N      . ILE   A 1  231 ? 16.560  -85.669  -59.204  1.00 50.43  ? 231 ILE   A N      1 
ATOM   1794  C  CA     . ILE   A 1  231 ? 17.899  -85.309  -59.696  1.00 48.78  ? 231 ILE   A CA     1 
ATOM   1795  C  C      . ILE   A 1  231 ? 18.825  -86.522  -59.751  1.00 50.27  ? 231 ILE   A C      1 
ATOM   1796  O  O      . ILE   A 1  231 ? 19.727  -86.581  -60.598  1.00 48.66  ? 231 ILE   A O      1 
ATOM   1797  C  CB     . ILE   A 1  231 ? 18.567  -84.199  -58.865  1.00 48.15  ? 231 ILE   A CB     1 
ATOM   1798  C  CG1    . ILE   A 1  231 ? 17.978  -82.825  -59.188  1.00 50.95  ? 231 ILE   A CG1    1 
ATOM   1799  C  CG2    . ILE   A 1  231 ? 20.069  -84.176  -59.170  1.00 33.51  ? 231 ILE   A CG2    1 
ATOM   1800  C  CD1    . ILE   A 1  231 ? 18.401  -81.755  -58.209  1.00 45.16  ? 231 ILE   A CD1    1 
ATOM   1801  N  N      . SER   A 1  232 ? 18.669  -87.495  -58.856  1.00 44.83  ? 232 SER   A N      1 
ATOM   1802  C  CA     . SER   A 1  232 ? 19.600  -88.607  -58.996  1.00 49.74  ? 232 SER   A CA     1 
ATOM   1803  C  C      . SER   A 1  232 ? 19.213  -89.495  -60.170  1.00 45.38  ? 232 SER   A C      1 
ATOM   1804  O  O      . SER   A 1  232 ? 20.100  -90.057  -60.819  1.00 47.14  ? 232 SER   A O      1 
ATOM   1805  C  CB     . SER   A 1  232 ? 19.751  -89.404  -57.688  1.00 53.44  ? 232 SER   A CB     1 
ATOM   1806  O  OG     . SER   A 1  232 ? 18.565  -89.470  -56.924  1.00 60.47  ? 232 SER   A OG     1 
ATOM   1807  N  N      . GLN   A 1  233 ? 17.922  -89.572  -60.514  1.00 44.16  ? 233 GLN   A N      1 
ATOM   1808  C  CA     . GLN   A 1  233 ? 17.539  -90.214  -61.772  1.00 45.03  ? 233 GLN   A CA     1 
ATOM   1809  C  C      . GLN   A 1  233 ? 18.358  -89.646  -62.923  1.00 50.05  ? 233 GLN   A C      1 
ATOM   1810  O  O      . GLN   A 1  233 ? 18.996  -90.389  -63.682  1.00 49.76  ? 233 GLN   A O      1 
ATOM   1811  C  CB     . GLN   A 1  233 ? 16.043  -90.032  -62.058  1.00 42.13  ? 233 GLN   A CB     1 
ATOM   1812  C  CG     . GLN   A 1  233 ? 15.144  -90.784  -61.118  1.00 46.79  ? 233 GLN   A CG     1 
ATOM   1813  C  CD     . GLN   A 1  233 ? 15.153  -92.261  -61.379  1.00 52.99  ? 233 GLN   A CD     1 
ATOM   1814  O  OE1    . GLN   A 1  233 ? 14.835  -92.697  -62.485  1.00 65.60  ? 233 GLN   A OE1    1 
ATOM   1815  N  NE2    . GLN   A 1  233 ? 15.565  -93.047  -60.386  1.00 42.77  ? 233 GLN   A NE2    1 
ATOM   1816  N  N      . ILE   A 1  234 ? 18.354  -88.320  -63.076  1.00 45.85  ? 234 ILE   A N      1 
ATOM   1817  C  CA     . ILE   A 1  234 ? 19.118  -87.759  -64.178  1.00 47.44  ? 234 ILE   A CA     1 
ATOM   1818  C  C      . ILE   A 1  234 ? 20.586  -88.127  -64.024  1.00 46.22  ? 234 ILE   A C      1 
ATOM   1819  O  O      . ILE   A 1  234 ? 21.228  -88.547  -64.996  1.00 46.34  ? 234 ILE   A O      1 
ATOM   1820  C  CB     . ILE   A 1  234 ? 18.902  -86.235  -64.301  1.00 47.32  ? 234 ILE   A CB     1 
ATOM   1821  C  CG1    . ILE   A 1  234 ? 17.532  -85.937  -64.869  1.00 40.47  ? 234 ILE   A CG1    1 
ATOM   1822  C  CG2    . ILE   A 1  234 ? 19.943  -85.591  -65.192  1.00 43.61  ? 234 ILE   A CG2    1 
ATOM   1823  C  CD1    . ILE   A 1  234 ? 16.448  -86.240  -63.885  1.00 47.38  ? 234 ILE   A CD1    1 
ATOM   1824  N  N      . VAL   A 1  235 ? 21.129  -88.030  -62.797  1.00 42.25  ? 235 VAL   A N      1 
ATOM   1825  C  CA     . VAL   A 1  235 ? 22.552  -88.321  -62.596  1.00 47.56  ? 235 VAL   A CA     1 
ATOM   1826  C  C      . VAL   A 1  235 ? 22.860  -89.755  -63.006  1.00 50.21  ? 235 VAL   A C      1 
ATOM   1827  O  O      . VAL   A 1  235 ? 23.819  -90.021  -63.747  1.00 48.54  ? 235 VAL   A O      1 
ATOM   1828  C  CB     . VAL   A 1  235 ? 22.984  -88.058  -61.142  1.00 45.39  ? 235 VAL   A CB     1 
ATOM   1829  C  CG1    . VAL   A 1  235 ? 24.455  -88.450  -60.954  1.00 38.94  ? 235 VAL   A CG1    1 
ATOM   1830  C  CG2    . VAL   A 1  235 ? 22.805  -86.614  -60.792  1.00 42.88  ? 235 VAL   A CG2    1 
ATOM   1831  N  N      . SER   A 1  236 ? 22.056  -90.698  -62.512  1.00 41.92  ? 236 SER   A N      1 
ATOM   1832  C  CA     . SER   A 1  236 ? 22.180  -92.084  -62.927  1.00 45.05  ? 236 SER   A CA     1 
ATOM   1833  C  C      . SER   A 1  236 ? 22.228  -92.197  -64.452  1.00 50.73  ? 236 SER   A C      1 
ATOM   1834  O  O      . SER   A 1  236 ? 23.149  -92.801  -65.015  1.00 55.72  ? 236 SER   A O      1 
ATOM   1835  C  CB     . SER   A 1  236 ? 21.019  -92.887  -62.335  1.00 46.98  ? 236 SER   A CB     1 
ATOM   1836  O  OG     . SER   A 1  236 ? 21.326  -94.263  -62.229  1.00 48.07  ? 236 SER   A OG     1 
ATOM   1837  N  N      . SER   A 1  237 ? 21.262  -91.589  -65.147  1.00 53.62  ? 237 SER   A N      1 
ATOM   1838  C  CA     . SER   A 1  237 ? 21.263  -91.635  -66.612  1.00 51.11  ? 237 SER   A CA     1 
ATOM   1839  C  C      . SER   A 1  237 ? 22.604  -91.229  -67.194  1.00 46.85  ? 237 SER   A C      1 
ATOM   1840  O  O      . SER   A 1  237 ? 23.058  -91.812  -68.181  1.00 50.75  ? 237 SER   A O      1 
ATOM   1841  C  CB     . SER   A 1  237 ? 20.178  -90.725  -67.184  1.00 49.16  ? 237 SER   A CB     1 
ATOM   1842  O  OG     . SER   A 1  237 ? 18.909  -91.142  -66.752  1.00 55.62  ? 237 SER   A OG     1 
ATOM   1843  N  N      . ILE   A 1  238 ? 23.237  -90.203  -66.620  1.00 48.95  ? 238 ILE   A N      1 
ATOM   1844  C  CA     . ILE   A 1  238 ? 24.481  -89.676  -67.175  1.00 46.17  ? 238 ILE   A CA     1 
ATOM   1845  C  C      . ILE   A 1  238 ? 25.687  -90.517  -66.798  1.00 48.11  ? 238 ILE   A C      1 
ATOM   1846  O  O      . ILE   A 1  238 ? 26.719  -90.442  -67.475  1.00 48.25  ? 238 ILE   A O      1 
ATOM   1847  C  CB     . ILE   A 1  238 ? 24.709  -88.233  -66.709  1.00 40.95  ? 238 ILE   A CB     1 
ATOM   1848  C  CG1    . ILE   A 1  238 ? 23.481  -87.391  -67.036  1.00 46.45  ? 238 ILE   A CG1    1 
ATOM   1849  C  CG2    . ILE   A 1  238 ? 25.970  -87.673  -67.337  1.00 37.08  ? 238 ILE   A CG2    1 
ATOM   1850  C  CD1    . ILE   A 1  238 ? 23.489  -86.011  -66.436  1.00 40.57  ? 238 ILE   A CD1    1 
ATOM   1851  N  N      . THR   A 1  239 ? 25.598  -91.307  -65.729  1.00 48.47  ? 239 THR   A N      1 
ATOM   1852  C  CA     . THR   A 1  239 ? 26.730  -92.114  -65.307  1.00 52.37  ? 239 THR   A CA     1 
ATOM   1853  C  C      . THR   A 1  239 ? 26.603  -93.575  -65.702  1.00 53.20  ? 239 THR   A C      1 
ATOM   1854  O  O      . THR   A 1  239 ? 27.626  -94.266  -65.729  1.00 59.45  ? 239 THR   A O      1 
ATOM   1855  C  CB     . THR   A 1  239 ? 26.928  -92.038  -63.787  1.00 48.02  ? 239 THR   A CB     1 
ATOM   1856  O  OG1    . THR   A 1  239 ? 25.661  -92.183  -63.147  1.00 47.29  ? 239 THR   A OG1    1 
ATOM   1857  C  CG2    . THR   A 1  239 ? 27.562  -90.725  -63.394  1.00 42.00  ? 239 THR   A CG2    1 
ATOM   1858  N  N      . ALA   A 1  240 ? 25.394  -94.055  -66.014  1.00 48.16  ? 240 ALA   A N      1 
ATOM   1859  C  CA     . ALA   A 1  240 ? 25.189  -95.456  -66.366  1.00 47.44  ? 240 ALA   A CA     1 
ATOM   1860  C  C      . ALA   A 1  240 ? 26.292  -95.994  -67.278  1.00 49.73  ? 240 ALA   A C      1 
ATOM   1861  O  O      . ALA   A 1  240 ? 26.796  -97.097  -67.057  1.00 49.37  ? 240 ALA   A O      1 
ATOM   1862  C  CB     . ALA   A 1  240 ? 23.822  -95.625  -67.013  1.00 51.18  ? 240 ALA   A CB     1 
ATOM   1863  N  N      . SER   A 1  241 ? 26.718  -95.205  -68.270  1.00 47.40  ? 241 SER   A N      1 
ATOM   1864  C  CA     . SER   A 1  241 ? 27.746  -95.663  -69.201  1.00 45.95  ? 241 SER   A CA     1 
ATOM   1865  C  C      . SER   A 1  241 ? 29.082  -95.923  -68.539  1.00 52.43  ? 241 SER   A C      1 
ATOM   1866  O  O      . SER   A 1  241 ? 29.921  -96.616  -69.126  1.00 58.12  ? 241 SER   A O      1 
ATOM   1867  C  CB     . SER   A 1  241 ? 27.970  -94.656  -70.320  1.00 48.71  ? 241 SER   A CB     1 
ATOM   1868  O  OG     . SER   A 1  241 ? 28.236  -93.369  -69.810  1.00 48.98  ? 241 SER   A OG     1 
ATOM   1869  N  N      . LEU   A 1  242 ? 29.323  -95.356  -67.362  1.00 55.71  ? 242 LEU   A N      1 
ATOM   1870  C  CA     . LEU   A 1  242 ? 30.534  -95.684  -66.622  1.00 52.22  ? 242 LEU   A CA     1 
ATOM   1871  C  C      . LEU   A 1  242 ? 30.363  -96.933  -65.782  1.00 51.25  ? 242 LEU   A C      1 
ATOM   1872  O  O      . LEU   A 1  242 ? 31.353  -97.612  -65.517  1.00 59.07  ? 242 LEU   A O      1 
ATOM   1873  C  CB     . LEU   A 1  242 ? 30.936  -94.520  -65.734  1.00 43.14  ? 242 LEU   A CB     1 
ATOM   1874  C  CG     . LEU   A 1  242 ? 31.197  -93.262  -66.536  1.00 46.29  ? 242 LEU   A CG     1 
ATOM   1875  C  CD1    . LEU   A 1  242 ? 31.148  -92.042  -65.640  1.00 53.48  ? 242 LEU   A CD1    1 
ATOM   1876  C  CD2    . LEU   A 1  242 ? 32.551  -93.374  -67.162  1.00 52.93  ? 242 LEU   A CD2    1 
ATOM   1877  N  N      . ARG   A 1  243 ? 29.131  -97.273  -65.414  1.00 46.00  ? 243 ARG   A N      1 
ATOM   1878  C  CA     . ARG   A 1  243 ? 28.837  -98.357  -64.491  1.00 52.70  ? 243 ARG   A CA     1 
ATOM   1879  C  C      . ARG   A 1  243 ? 28.240  -99.579  -65.177  1.00 56.08  ? 243 ARG   A C      1 
ATOM   1880  O  O      . ARG   A 1  243 ? 27.911  -100.553 -64.495  1.00 54.40  ? 243 ARG   A O      1 
ATOM   1881  C  CB     . ARG   A 1  243 ? 27.870  -97.867  -63.393  1.00 53.02  ? 243 ARG   A CB     1 
ATOM   1882  C  CG     . ARG   A 1  243 ? 27.826  -96.344  -63.240  1.00 53.56  ? 243 ARG   A CG     1 
ATOM   1883  C  CD     . ARG   A 1  243 ? 27.070  -95.826  -61.991  1.00 53.32  ? 243 ARG   A CD     1 
ATOM   1884  N  NE     . ARG   A 1  243 ? 25.776  -96.466  -61.778  1.00 54.72  ? 243 ARG   A NE     1 
ATOM   1885  C  CZ     . ARG   A 1  243 ? 24.642  -96.125  -62.379  1.00 51.32  ? 243 ARG   A CZ     1 
ATOM   1886  N  NH1    . ARG   A 1  243 ? 24.583  -95.111  -63.226  1.00 53.73  ? 243 ARG   A NH1    1 
ATOM   1887  N  NH2    . ARG   A 1  243 ? 23.542  -96.829  -62.132  1.00 48.30  ? 243 ARG   A NH2    1 
ATOM   1888  N  N      . PHE   A 1  244 ? 28.073  -99.556  -66.500  1.00 62.27  ? 244 PHE   A N      1 
ATOM   1889  C  CA     . PHE   A 1  244 ? 27.415  -100.643 -67.217  1.00 54.42  ? 244 PHE   A CA     1 
ATOM   1890  C  C      . PHE   A 1  244 ? 28.176  -100.968 -68.503  1.00 58.26  ? 244 PHE   A C      1 
ATOM   1891  O  O      . PHE   A 1  244 ? 28.924  -100.145 -69.046  1.00 53.45  ? 244 PHE   A O      1 
ATOM   1892  C  CB     . PHE   A 1  244 ? 25.951  -100.295 -67.553  1.00 48.56  ? 244 PHE   A CB     1 
ATOM   1893  C  CG     . PHE   A 1  244 ? 25.024  -100.309 -66.372  1.00 53.38  ? 244 PHE   A CG     1 
ATOM   1894  C  CD1    . PHE   A 1  244 ? 24.743  -101.488 -65.704  1.00 54.84  ? 244 PHE   A CD1    1 
ATOM   1895  C  CD2    . PHE   A 1  244 ? 24.435  -99.136  -65.922  1.00 57.51  ? 244 PHE   A CD2    1 
ATOM   1896  C  CE1    . PHE   A 1  244 ? 23.896  -101.497 -64.597  1.00 54.33  ? 244 PHE   A CE1    1 
ATOM   1897  C  CE2    . PHE   A 1  244 ? 23.581  -99.139  -64.819  1.00 55.65  ? 244 PHE   A CE2    1 
ATOM   1898  C  CZ     . PHE   A 1  244 ? 23.311  -100.320 -64.157  1.00 52.44  ? 244 PHE   A CZ     1 
ATOM   1899  N  N      . ASP   A 1  245 ? 27.964  -102.190 -68.991  1.00 59.60  ? 245 ASP   A N      1 
ATOM   1900  C  CA     . ASP   A 1  245 ? 28.473  -102.556 -70.300  1.00 57.11  ? 245 ASP   A CA     1 
ATOM   1901  C  C      . ASP   A 1  245 ? 27.948  -101.575 -71.325  1.00 58.80  ? 245 ASP   A C      1 
ATOM   1902  O  O      . ASP   A 1  245 ? 26.753  -101.272 -71.352  1.00 61.18  ? 245 ASP   A O      1 
ATOM   1903  C  CB     . ASP   A 1  245 ? 28.056  -103.985 -70.672  1.00 59.92  ? 245 ASP   A CB     1 
ATOM   1904  C  CG     . ASP   A 1  245 ? 29.060  -104.661 -71.600  1.00 59.52  ? 245 ASP   A CG     1 
ATOM   1905  O  OD1    . ASP   A 1  245 ? 30.218  -104.187 -71.629  1.00 63.14  ? 245 ASP   A OD1    1 
ATOM   1906  O  OD2    . ASP   A 1  245 ? 28.717  -105.662 -72.283  1.00 61.96  ? 245 ASP   A OD2    1 
ATOM   1907  N  N      . GLY   A 1  246 ? 28.850  -101.069 -72.153  1.00 60.01  ? 246 GLY   A N      1 
ATOM   1908  C  CA     . GLY   A 1  246 ? 28.450  -100.195 -73.233  1.00 50.10  ? 246 GLY   A CA     1 
ATOM   1909  C  C      . GLY   A 1  246 ? 29.666  -99.751  -74.003  1.00 57.56  ? 246 GLY   A C      1 
ATOM   1910  O  O      . GLY   A 1  246 ? 30.808  -100.111 -73.684  1.00 58.54  ? 246 GLY   A O      1 
ATOM   1911  N  N      . ALA   A 1  247 ? 29.395  -98.949  -75.031  1.00 58.91  ? 247 ALA   A N      1 
ATOM   1912  C  CA     . ALA   A 1  247 ? 30.411  -98.478  -75.959  1.00 63.80  ? 247 ALA   A CA     1 
ATOM   1913  C  C      . ALA   A 1  247 ? 30.347  -96.977  -76.154  1.00 64.38  ? 247 ALA   A C      1 
ATOM   1914  O  O      . ALA   A 1  247 ? 31.103  -96.439  -76.974  1.00 62.89  ? 247 ALA   A O      1 
ATOM   1915  C  CB     . ALA   A 1  247 ? 30.263  -99.167  -77.325  1.00 64.91  ? 247 ALA   A CB     1 
ATOM   1916  N  N      . LEU   A 1  248 ? 29.454  -96.295  -75.443  1.00 60.79  ? 248 LEU   A N      1 
ATOM   1917  C  CA     . LEU   A 1  248 ? 29.315  -94.851  -75.513  1.00 61.99  ? 248 LEU   A CA     1 
ATOM   1918  C  C      . LEU   A 1  248 ? 29.526  -94.255  -74.128  1.00 60.39  ? 248 LEU   A C      1 
ATOM   1919  O  O      . LEU   A 1  248 ? 28.968  -94.754  -73.138  1.00 51.92  ? 248 LEU   A O      1 
ATOM   1920  C  CB     . LEU   A 1  248 ? 27.942  -94.456  -76.052  1.00 59.19  ? 248 LEU   A CB     1 
ATOM   1921  C  CG     . LEU   A 1  248 ? 27.767  -92.945  -76.125  1.00 53.94  ? 248 LEU   A CG     1 
ATOM   1922  C  CD1    . LEU   A 1  248 ? 28.610  -92.355  -77.274  1.00 51.61  ? 248 LEU   A CD1    1 
ATOM   1923  C  CD2    . LEU   A 1  248 ? 26.298  -92.646  -76.280  1.00 48.06  ? 248 LEU   A CD2    1 
ATOM   1924  N  N      . ASN   A 1  249 ? 30.319  -93.180  -74.076  1.00 57.90  ? 249 ASN   A N      1 
ATOM   1925  C  CA     . ASN   A 1  249 ? 30.723  -92.539  -72.828  1.00 54.08  ? 249 ASN   A CA     1 
ATOM   1926  C  C      . ASN   A 1  249 ? 31.204  -93.577  -71.825  1.00 55.47  ? 249 ASN   A C      1 
ATOM   1927  O  O      . ASN   A 1  249 ? 30.745  -93.627  -70.684  1.00 54.27  ? 249 ASN   A O      1 
ATOM   1928  C  CB     . ASN   A 1  249 ? 29.587  -91.721  -72.214  1.00 52.00  ? 249 ASN   A CB     1 
ATOM   1929  C  CG     . ASN   A 1  249 ? 29.165  -90.566  -73.067  1.00 49.58  ? 249 ASN   A CG     1 
ATOM   1930  O  OD1    . ASN   A 1  249 ? 29.932  -90.072  -73.902  1.00 56.48  ? 249 ASN   A OD1    1 
ATOM   1931  N  ND2    . ASN   A 1  249 ? 27.923  -90.117  -72.867  1.00 45.87  ? 249 ASN   A ND2    1 
ATOM   1932  N  N      . VAL   A 1  250 ? 32.131  -94.429  -72.258  1.00 59.23  ? 250 VAL   A N      1 
ATOM   1933  C  CA     . VAL   A 1  250 ? 32.619  -95.457  -71.344  1.00 56.71  ? 250 VAL   A CA     1 
ATOM   1934  C  C      . VAL   A 1  250 ? 33.587  -94.907  -70.307  1.00 51.98  ? 250 VAL   A C      1 
ATOM   1935  O  O      . VAL   A 1  250 ? 33.728  -95.523  -69.249  1.00 55.61  ? 250 VAL   A O      1 
ATOM   1936  C  CB     . VAL   A 1  250 ? 33.273  -96.633  -72.094  1.00 60.19  ? 250 VAL   A CB     1 
ATOM   1937  C  CG1    . VAL   A 1  250 ? 32.254  -97.748  -72.297  1.00 60.20  ? 250 VAL   A CG1    1 
ATOM   1938  C  CG2    . VAL   A 1  250 ? 33.854  -96.172  -73.440  1.00 58.00  ? 250 VAL   A CG2    1 
ATOM   1939  N  N      . ASP   A 1  251 ? 34.274  -93.788  -70.585  1.00 52.05  ? 251 ASP   A N      1 
ATOM   1940  C  CA     . ASP   A 1  251 ? 35.143  -93.134  -69.614  1.00 54.67  ? 251 ASP   A CA     1 
ATOM   1941  C  C      . ASP   A 1  251 ? 34.880  -91.628  -69.598  1.00 55.30  ? 251 ASP   A C      1 
ATOM   1942  O  O      . ASP   A 1  251 ? 34.386  -91.054  -70.574  1.00 56.78  ? 251 ASP   A O      1 
ATOM   1943  C  CB     . ASP   A 1  251 ? 36.637  -93.440  -69.887  1.00 51.77  ? 251 ASP   A CB     1 
ATOM   1944  C  CG     . ASP   A 1  251 ? 37.226  -92.660  -71.093  1.00 64.32  ? 251 ASP   A CG     1 
ATOM   1945  O  OD1    . ASP   A 1  251 ? 36.840  -91.490  -71.355  1.00 65.95  ? 251 ASP   A OD1    1 
ATOM   1946  O  OD2    . ASP   A 1  251 ? 38.131  -93.220  -71.775  1.00 66.57  ? 251 ASP   A OD2    1 
ATOM   1947  N  N      . LEU   A 1  252 ? 35.230  -90.986  -68.474  1.00 47.59  ? 252 LEU   A N      1 
ATOM   1948  C  CA     . LEU   A 1  252 ? 35.025  -89.546  -68.297  1.00 52.89  ? 252 LEU   A CA     1 
ATOM   1949  C  C      . LEU   A 1  252 ? 35.699  -88.695  -69.375  1.00 56.18  ? 252 LEU   A C      1 
ATOM   1950  O  O      . LEU   A 1  252 ? 35.391  -87.498  -69.478  1.00 58.43  ? 252 LEU   A O      1 
ATOM   1951  C  CB     . LEU   A 1  252 ? 35.549  -89.081  -66.929  1.00 51.34  ? 252 LEU   A CB     1 
ATOM   1952  C  CG     . LEU   A 1  252 ? 35.246  -89.930  -65.706  1.00 49.22  ? 252 LEU   A CG     1 
ATOM   1953  C  CD1    . LEU   A 1  252 ? 36.129  -89.500  -64.555  1.00 48.75  ? 252 LEU   A CD1    1 
ATOM   1954  C  CD2    . LEU   A 1  252 ? 33.776  -89.800  -65.367  1.00 51.30  ? 252 LEU   A CD2    1 
ATOM   1955  N  N      . THR   A 1  253 ? 36.636  -89.248  -70.147  1.00 46.17  ? 253 THR   A N      1 
ATOM   1956  C  CA     . THR   A 1  253 ? 37.236  -88.422  -71.179  1.00 55.46  ? 253 THR   A CA     1 
ATOM   1957  C  C      . THR   A 1  253 ? 36.298  -88.296  -72.369  1.00 54.73  ? 253 THR   A C      1 
ATOM   1958  O  O      . THR   A 1  253 ? 36.303  -87.269  -73.057  1.00 52.29  ? 253 THR   A O      1 
ATOM   1959  C  CB     . THR   A 1  253 ? 38.614  -88.972  -71.602  1.00 61.29  ? 253 THR   A CB     1 
ATOM   1960  O  OG1    . THR   A 1  253 ? 39.274  -89.569  -70.476  1.00 55.00  ? 253 THR   A OG1    1 
ATOM   1961  C  CG2    . THR   A 1  253 ? 39.513  -87.839  -72.125  1.00 56.44  ? 253 THR   A CG2    1 
ATOM   1962  N  N      . GLU   A 1  254 ? 35.464  -89.309  -72.604  1.00 55.76  ? 254 GLU   A N      1 
ATOM   1963  C  CA     . GLU   A 1  254 ? 34.535  -89.242  -73.725  1.00 57.71  ? 254 GLU   A CA     1 
ATOM   1964  C  C      . GLU   A 1  254 ? 33.526  -88.118  -73.540  1.00 59.56  ? 254 GLU   A C      1 
ATOM   1965  O  O      . GLU   A 1  254 ? 33.102  -87.501  -74.529  1.00 57.54  ? 254 GLU   A O      1 
ATOM   1966  C  CB     . GLU   A 1  254 ? 33.816  -90.576  -73.882  1.00 56.85  ? 254 GLU   A CB     1 
ATOM   1967  C  CG     . GLU   A 1  254 ? 34.259  -91.390  -75.064  1.00 62.75  ? 254 GLU   A CG     1 
ATOM   1968  C  CD     . GLU   A 1  254 ? 33.548  -92.731  -75.121  1.00 70.37  ? 254 GLU   A CD     1 
ATOM   1969  O  OE1    . GLU   A 1  254 ? 32.416  -92.782  -75.671  1.00 65.17  ? 254 GLU   A OE1    1 
ATOM   1970  O  OE2    . GLU   A 1  254 ? 34.124  -93.728  -74.611  1.00 65.89  ? 254 GLU   A OE2    1 
ATOM   1971  N  N      . PHE   A 1  255 ? 33.132  -87.838  -72.285  1.00 52.21  ? 255 PHE   A N      1 
ATOM   1972  C  CA     . PHE   A 1  255 ? 32.183  -86.757  -72.021  1.00 50.23  ? 255 PHE   A CA     1 
ATOM   1973  C  C      . PHE   A 1  255 ? 32.692  -85.434  -72.575  1.00 52.99  ? 255 PHE   A C      1 
ATOM   1974  O  O      . PHE   A 1  255 ? 31.919  -84.645  -73.138  1.00 52.79  ? 255 PHE   A O      1 
ATOM   1975  C  CB     . PHE   A 1  255 ? 31.923  -86.630  -70.521  1.00 52.13  ? 255 PHE   A CB     1 
ATOM   1976  C  CG     . PHE   A 1  255 ? 31.009  -87.713  -69.940  1.00 53.87  ? 255 PHE   A CG     1 
ATOM   1977  C  CD1    . PHE   A 1  255 ? 29.632  -87.549  -69.919  1.00 44.80  ? 255 PHE   A CD1    1 
ATOM   1978  C  CD2    . PHE   A 1  255 ? 31.535  -88.872  -69.375  1.00 51.43  ? 255 PHE   A CD2    1 
ATOM   1979  C  CE1    . PHE   A 1  255 ? 28.810  -88.515  -69.367  1.00 39.83  ? 255 PHE   A CE1    1 
ATOM   1980  C  CE2    . PHE   A 1  255 ? 30.701  -89.842  -68.832  1.00 47.18  ? 255 PHE   A CE2    1 
ATOM   1981  C  CZ     . PHE   A 1  255 ? 29.338  -89.653  -68.826  1.00 36.51  ? 255 PHE   A CZ     1 
ATOM   1982  N  N      . GLN   A 1  256 ? 33.993  -85.173  -72.429  1.00 54.55  ? 256 GLN   A N      1 
ATOM   1983  C  CA     . GLN   A 1  256 ? 34.570  -83.944  -72.968  1.00 54.84  ? 256 GLN   A CA     1 
ATOM   1984  C  C      . GLN   A 1  256 ? 34.696  -84.027  -74.478  1.00 55.67  ? 256 GLN   A C      1 
ATOM   1985  O  O      . GLN   A 1  256 ? 34.520  -83.025  -75.181  1.00 56.93  ? 256 GLN   A O      1 
ATOM   1986  C  CB     . GLN   A 1  256 ? 35.941  -83.699  -72.349  1.00 52.62  ? 256 GLN   A CB     1 
ATOM   1987  C  CG     . GLN   A 1  256 ? 36.042  -84.185  -70.911  1.00 60.49  ? 256 GLN   A CG     1 
ATOM   1988  C  CD     . GLN   A 1  256 ? 37.494  -84.417  -70.480  1.00 68.95  ? 256 GLN   A CD     1 
ATOM   1989  O  OE1    . GLN   A 1  256 ? 37.782  -85.278  -69.629  1.00 58.36  ? 256 GLN   A OE1    1 
ATOM   1990  N  NE2    . GLN   A 1  256 ? 38.417  -83.643  -71.071  1.00 66.65  ? 256 GLN   A NE2    1 
ATOM   1991  N  N      . THR   A 1  257 ? 35.031  -85.220  -74.979  1.00 55.67  ? 257 THR   A N      1 
ATOM   1992  C  CA     . THR   A 1  257 ? 35.152  -85.464  -76.412  1.00 55.41  ? 257 THR   A CA     1 
ATOM   1993  C  C      . THR   A 1  257 ? 33.804  -85.368  -77.113  1.00 58.20  ? 257 THR   A C      1 
ATOM   1994  O  O      . THR   A 1  257 ? 33.689  -84.754  -78.178  1.00 53.01  ? 257 THR   A O      1 
ATOM   1995  C  CB     . THR   A 1  257 ? 35.751  -86.844  -76.648  1.00 50.78  ? 257 THR   A CB     1 
ATOM   1996  O  OG1    . THR   A 1  257 ? 37.168  -86.761  -76.553  1.00 55.13  ? 257 THR   A OG1    1 
ATOM   1997  C  CG2    . THR   A 1  257 ? 35.340  -87.375  -78.009  1.00 52.62  ? 257 THR   A CG2    1 
ATOM   1998  N  N      . ASN   A 1  258 ? 32.774  -85.984  -76.531  1.00 54.61  ? 258 ASN   A N      1 
ATOM   1999  C  CA     . ASN   A 1  258 ? 31.476  -86.064  -77.180  1.00 54.76  ? 258 ASN   A CA     1 
ATOM   2000  C  C      . ASN   A 1  258 ? 30.657  -84.790  -77.017  1.00 56.06  ? 258 ASN   A C      1 
ATOM   2001  O  O      . ASN   A 1  258 ? 29.887  -84.445  -77.917  1.00 53.79  ? 258 ASN   A O      1 
ATOM   2002  C  CB     . ASN   A 1  258 ? 30.699  -87.253  -76.620  1.00 56.37  ? 258 ASN   A CB     1 
ATOM   2003  C  CG     . ASN   A 1  258 ? 31.325  -88.570  -76.983  1.00 50.62  ? 258 ASN   A CG     1 
ATOM   2004  O  OD1    . ASN   A 1  258 ? 32.036  -88.674  -77.979  1.00 52.22  ? 258 ASN   A OD1    1 
ATOM   2005  N  ND2    . ASN   A 1  258 ? 31.098  -89.580  -76.155  1.00 47.59  ? 258 ASN   A ND2    1 
ATOM   2006  N  N      . LEU   A 1  259 ? 30.809  -84.077  -75.894  1.00 57.78  ? 259 LEU   A N      1 
ATOM   2007  C  CA     . LEU   A 1  259 ? 29.945  -82.944  -75.571  1.00 55.77  ? 259 LEU   A CA     1 
ATOM   2008  C  C      . LEU   A 1  259 ? 30.655  -81.596  -75.454  1.00 56.27  ? 259 LEU   A C      1 
ATOM   2009  O  O      . LEU   A 1  259 ? 29.967  -80.574  -75.351  1.00 52.30  ? 259 LEU   A O      1 
ATOM   2010  C  CB     . LEU   A 1  259 ? 29.198  -83.221  -74.256  1.00 57.15  ? 259 LEU   A CB     1 
ATOM   2011  C  CG     . LEU   A 1  259 ? 28.318  -84.466  -74.297  1.00 48.38  ? 259 LEU   A CG     1 
ATOM   2012  C  CD1    . LEU   A 1  259 ? 28.030  -84.960  -72.914  1.00 45.19  ? 259 LEU   A CD1    1 
ATOM   2013  C  CD2    . LEU   A 1  259 ? 27.054  -84.085  -74.967  1.00 48.49  ? 259 LEU   A CD2    1 
ATOM   2014  N  N      . VAL   A 1  260 ? 31.987  -81.545  -75.483  1.00 57.07  ? 260 VAL   A N      1 
ATOM   2015  C  CA     . VAL   A 1  260 ? 32.676  -80.283  -75.216  1.00 52.51  ? 260 VAL   A CA     1 
ATOM   2016  C  C      . VAL   A 1  260 ? 33.739  -80.000  -76.273  1.00 55.23  ? 260 VAL   A C      1 
ATOM   2017  O  O      . VAL   A 1  260 ? 34.926  -80.246  -76.024  1.00 55.04  ? 260 VAL   A O      1 
ATOM   2018  C  CB     . VAL   A 1  260 ? 33.320  -80.303  -73.824  1.00 56.48  ? 260 VAL   A CB     1 
ATOM   2019  C  CG1    . VAL   A 1  260 ? 34.170  -79.043  -73.611  1.00 60.61  ? 260 VAL   A CG1    1 
ATOM   2020  C  CG2    . VAL   A 1  260 ? 32.274  -80.485  -72.746  1.00 53.18  ? 260 VAL   A CG2    1 
ATOM   2021  N  N      . PRO   A 1  261 ? 33.386  -79.466  -77.447  1.00 60.74  ? 261 PRO   A N      1 
ATOM   2022  C  CA     . PRO   A 1  261 ? 34.424  -79.177  -78.448  1.00 59.47  ? 261 PRO   A CA     1 
ATOM   2023  C  C      . PRO   A 1  261 ? 35.310  -78.000  -78.041  1.00 56.32  ? 261 PRO   A C      1 
ATOM   2024  O  O      . PRO   A 1  261 ? 36.536  -78.096  -78.099  1.00 52.62  ? 261 PRO   A O      1 
ATOM   2025  C  CB     . PRO   A 1  261 ? 33.615  -78.884  -79.722  1.00 51.39  ? 261 PRO   A CB     1 
ATOM   2026  C  CG     . PRO   A 1  261 ? 32.277  -78.455  -79.250  1.00 53.51  ? 261 PRO   A CG     1 
ATOM   2027  C  CD     . PRO   A 1  261 ? 32.028  -79.180  -77.954  1.00 56.75  ? 261 PRO   A CD     1 
ATOM   2028  N  N      . TYR   A 1  262 ? 34.707  -76.870  -77.660  1.00 62.25  ? 262 TYR   A N      1 
ATOM   2029  C  CA     . TYR   A 1  262 ? 35.476  -75.782  -77.068  1.00 55.77  ? 262 TYR   A CA     1 
ATOM   2030  C  C      . TYR   A 1  262 ? 35.490  -75.949  -75.545  1.00 61.64  ? 262 TYR   A C      1 
ATOM   2031  O  O      . TYR   A 1  262 ? 34.450  -76.250  -74.942  1.00 60.16  ? 262 TYR   A O      1 
ATOM   2032  C  CB     . TYR   A 1  262 ? 34.884  -74.422  -77.458  1.00 44.90  ? 262 TYR   A CB     1 
ATOM   2033  N  N      . PRO   A 1  263 ? 36.651  -75.768  -74.889  1.00 62.93  ? 263 PRO   A N      1 
ATOM   2034  C  CA     . PRO   A 1  263 ? 36.779  -76.180  -73.479  1.00 57.36  ? 263 PRO   A CA     1 
ATOM   2035  C  C      . PRO   A 1  263 ? 36.073  -75.306  -72.456  1.00 51.41  ? 263 PRO   A C      1 
ATOM   2036  O  O      . PRO   A 1  263 ? 35.607  -75.839  -71.442  1.00 55.59  ? 263 PRO   A O      1 
ATOM   2037  C  CB     . PRO   A 1  263 ? 38.300  -76.158  -73.245  1.00 57.42  ? 263 PRO   A CB     1 
ATOM   2038  C  CG     . PRO   A 1  263 ? 38.907  -76.158  -74.598  1.00 59.61  ? 263 PRO   A CG     1 
ATOM   2039  C  CD     . PRO   A 1  263 ? 37.949  -75.366  -75.448  1.00 60.64  ? 263 PRO   A CD     1 
ATOM   2040  N  N      . ARG   A 1  264 ? 36.004  -73.984  -72.662  1.00 57.37  ? 264 ARG   A N      1 
ATOM   2041  C  CA     . ARG   A 1  264 ? 35.269  -73.134  -71.715  1.00 59.88  ? 264 ARG   A CA     1 
ATOM   2042  C  C      . ARG   A 1  264 ? 33.786  -73.437  -71.754  1.00 55.52  ? 264 ARG   A C      1 
ATOM   2043  O  O      . ARG   A 1  264 ? 33.130  -73.542  -70.712  1.00 53.50  ? 264 ARG   A O      1 
ATOM   2044  C  CB     . ARG   A 1  264 ? 35.473  -71.650  -72.019  1.00 51.47  ? 264 ARG   A CB     1 
ATOM   2045  C  CG     . ARG   A 1  264 ? 36.652  -71.062  -71.336  1.00 47.74  ? 264 ARG   A CG     1 
ATOM   2046  C  CD     . ARG   A 1  264 ? 37.030  -69.771  -72.014  1.00 57.06  ? 264 ARG   A CD     1 
ATOM   2047  N  NE     . ARG   A 1  264 ? 36.199  -68.656  -71.585  1.00 58.19  ? 264 ARG   A NE     1 
ATOM   2048  C  CZ     . ARG   A 1  264 ? 36.294  -68.074  -70.395  1.00 54.29  ? 264 ARG   A CZ     1 
ATOM   2049  N  NH1    . ARG   A 1  264 ? 37.120  -68.534  -69.461  1.00 47.11  ? 264 ARG   A NH1    1 
ATOM   2050  N  NH2    . ARG   A 1  264 ? 35.545  -67.007  -70.138  1.00 52.19  ? 264 ARG   A NH2    1 
ATOM   2051  N  N      . ILE   A 1  265 ? 33.239  -73.560  -72.956  1.00 51.51  ? 265 ILE   A N      1 
ATOM   2052  C  CA     . ILE   A 1  265 ? 31.815  -73.753  -73.119  1.00 49.42  ? 265 ILE   A CA     1 
ATOM   2053  C  C      . ILE   A 1  265 ? 31.482  -75.199  -72.822  1.00 47.88  ? 265 ILE   A C      1 
ATOM   2054  O  O      . ILE   A 1  265 ? 31.085  -75.938  -73.727  1.00 52.18  ? 265 ILE   A O      1 
ATOM   2055  C  CB     . ILE   A 1  265 ? 31.392  -73.353  -74.532  1.00 48.04  ? 265 ILE   A CB     1 
ATOM   2056  C  CG1    . ILE   A 1  265 ? 32.020  -72.018  -74.863  1.00 46.17  ? 265 ILE   A CG1    1 
ATOM   2057  C  CG2    . ILE   A 1  265 ? 29.914  -73.204  -74.606  1.00 49.79  ? 265 ILE   A CG2    1 
ATOM   2058  C  CD1    . ILE   A 1  265 ? 31.347  -71.341  -75.993  1.00 54.66  ? 265 ILE   A CD1    1 
ATOM   2059  N  N      . HIS   A 1  266 ? 31.638  -75.612  -71.558  1.00 46.53  ? 266 HIS   A N      1 
ATOM   2060  C  CA     . HIS   A 1  266 ? 31.502  -77.018  -71.190  1.00 42.13  ? 266 HIS   A CA     1 
ATOM   2061  C  C      . HIS   A 1  266 ? 30.344  -77.265  -70.224  1.00 45.90  ? 266 HIS   A C      1 
ATOM   2062  O  O      . HIS   A 1  266 ? 30.481  -78.022  -69.252  1.00 47.28  ? 266 HIS   A O      1 
ATOM   2063  C  CB     . HIS   A 1  266 ? 32.812  -77.544  -70.600  1.00 45.42  ? 266 HIS   A CB     1 
ATOM   2064  C  CG     . HIS   A 1  266 ? 33.273  -76.817  -69.370  1.00 57.26  ? 266 HIS   A CG     1 
ATOM   2065  N  ND1    . HIS   A 1  266 ? 34.315  -75.912  -69.385  1.00 56.20  ? 266 HIS   A ND1    1 
ATOM   2066  C  CD2    . HIS   A 1  266 ? 32.848  -76.878  -68.082  1.00 53.11  ? 266 HIS   A CD2    1 
ATOM   2067  C  CE1    . HIS   A 1  266 ? 34.500  -75.439  -68.164  1.00 54.69  ? 266 HIS   A CE1    1 
ATOM   2068  N  NE2    . HIS   A 1  266 ? 33.626  -76.011  -67.355  1.00 47.05  ? 266 HIS   A NE2    1 
ATOM   2069  N  N      . PHE   A 1  267 ? 29.180  -76.668  -70.517  1.00 48.99  ? 267 PHE   A N      1 
ATOM   2070  C  CA     . PHE   A 1  267 ? 27.978  -76.758  -69.688  1.00 39.14  ? 267 PHE   A CA     1 
ATOM   2071  C  C      . PHE   A 1  267 ? 26.840  -77.381  -70.490  1.00 40.32  ? 267 PHE   A C      1 
ATOM   2072  O  O      . PHE   A 1  267 ? 25.925  -76.676  -70.937  1.00 39.97  ? 267 PHE   A O      1 
ATOM   2073  C  CB     . PHE   A 1  267 ? 27.605  -75.377  -69.156  1.00 46.29  ? 267 PHE   A CB     1 
ATOM   2074  C  CG     . PHE   A 1  267 ? 28.655  -74.796  -68.239  1.00 45.24  ? 267 PHE   A CG     1 
ATOM   2075  C  CD1    . PHE   A 1  267 ? 28.673  -75.126  -66.883  1.00 39.95  ? 267 PHE   A CD1    1 
ATOM   2076  C  CD2    . PHE   A 1  267 ? 29.643  -73.958  -68.736  1.00 43.95  ? 267 PHE   A CD2    1 
ATOM   2077  C  CE1    . PHE   A 1  267 ? 29.639  -74.607  -66.049  1.00 41.06  ? 267 PHE   A CE1    1 
ATOM   2078  C  CE2    . PHE   A 1  267 ? 30.620  -73.439  -67.899  1.00 47.32  ? 267 PHE   A CE2    1 
ATOM   2079  C  CZ     . PHE   A 1  267 ? 30.614  -73.761  -66.557  1.00 43.66  ? 267 PHE   A CZ     1 
ATOM   2080  N  N      . PRO   A 1  268 ? 26.858  -78.706  -70.670  1.00 41.68  ? 268 PRO   A N      1 
ATOM   2081  C  CA     . PRO   A 1  268 ? 25.828  -79.376  -71.470  1.00 37.69  ? 268 PRO   A CA     1 
ATOM   2082  C  C      . PRO   A 1  268 ? 24.467  -79.349  -70.794  1.00 35.87  ? 268 PRO   A C      1 
ATOM   2083  O  O      . PRO   A 1  268 ? 24.334  -79.732  -69.635  1.00 36.22  ? 268 PRO   A O      1 
ATOM   2084  C  CB     . PRO   A 1  268 ? 26.349  -80.815  -71.562  1.00 40.55  ? 268 PRO   A CB     1 
ATOM   2085  C  CG     . PRO   A 1  268 ? 27.772  -80.755  -71.133  1.00 36.83  ? 268 PRO   A CG     1 
ATOM   2086  C  CD     . PRO   A 1  268 ? 27.814  -79.683  -70.130  1.00 41.79  ? 268 PRO   A CD     1 
ATOM   2087  N  N      . LEU   A 1  269 ? 23.449  -78.946  -71.552  1.00 38.84  ? 269 LEU   A N      1 
ATOM   2088  C  CA     . LEU   A 1  269 ? 22.062  -78.986  -71.094  1.00 34.59  ? 269 LEU   A CA     1 
ATOM   2089  C  C      . LEU   A 1  269 ? 21.538  -80.430  -71.033  1.00 35.76  ? 269 LEU   A C      1 
ATOM   2090  O  O      . LEU   A 1  269 ? 21.743  -81.221  -71.959  1.00 38.81  ? 269 LEU   A O      1 
ATOM   2091  C  CB     . LEU   A 1  269 ? 21.188  -78.132  -72.025  1.00 32.20  ? 269 LEU   A CB     1 
ATOM   2092  C  CG     . LEU   A 1  269 ? 19.696  -78.072  -71.717  1.00 37.83  ? 269 LEU   A CG     1 
ATOM   2093  C  CD1    . LEU   A 1  269 ? 19.499  -77.507  -70.309  1.00 42.38  ? 269 LEU   A CD1    1 
ATOM   2094  C  CD2    . LEU   A 1  269 ? 18.924  -77.265  -72.747  1.00 31.50  ? 269 LEU   A CD2    1 
ATOM   2095  N  N      . ALA   A 1  270 ? 20.864  -80.774  -69.940  1.00 28.98  ? 270 ALA   A N      1 
ATOM   2096  C  CA     . ALA   A 1  270 ? 20.255  -82.080  -69.760  1.00 30.16  ? 270 ALA   A CA     1 
ATOM   2097  C  C      . ALA   A 1  270 ? 18.745  -81.947  -69.893  1.00 38.05  ? 270 ALA   A C      1 
ATOM   2098  O  O      . ALA   A 1  270 ? 18.148  -81.032  -69.324  1.00 39.50  ? 270 ALA   A O      1 
ATOM   2099  C  CB     . ALA   A 1  270 ? 20.593  -82.672  -68.395  1.00 30.17  ? 270 ALA   A CB     1 
ATOM   2100  N  N      . THR   A 1  271 ? 18.132  -82.824  -70.681  1.00 38.84  ? 271 THR   A N      1 
ATOM   2101  C  CA     . THR   A 1  271 ? 16.680  -82.900  -70.737  1.00 43.49  ? 271 THR   A CA     1 
ATOM   2102  C  C      . THR   A 1  271 ? 16.314  -84.343  -70.445  1.00 44.82  ? 271 THR   A C      1 
ATOM   2103  O  O      . THR   A 1  271 ? 17.036  -85.258  -70.857  1.00 41.86  ? 271 THR   A O      1 
ATOM   2104  C  CB     . THR   A 1  271 ? 16.082  -82.448  -72.087  1.00 39.64  ? 271 THR   A CB     1 
ATOM   2105  O  OG1    . THR   A 1  271 ? 16.744  -81.262  -72.548  1.00 41.02  ? 271 THR   A OG1    1 
ATOM   2106  C  CG2    . THR   A 1  271 ? 14.597  -82.152  -71.909  1.00 37.34  ? 271 THR   A CG2    1 
ATOM   2107  N  N      . TYR   A 1  272 ? 15.217  -84.539  -69.702  1.00 38.06  ? 272 TYR   A N      1 
ATOM   2108  C  CA     . TYR   A 1  272 ? 14.826  -85.867  -69.248  1.00 40.90  ? 272 TYR   A CA     1 
ATOM   2109  C  C      . TYR   A 1  272 ? 13.324  -86.069  -69.409  1.00 44.72  ? 272 TYR   A C      1 
ATOM   2110  O  O      . TYR   A 1  272 ? 12.528  -85.267  -68.901  1.00 42.35  ? 272 TYR   A O      1 
ATOM   2111  C  CB     . TYR   A 1  272 ? 15.225  -86.083  -67.791  1.00 31.25  ? 272 TYR   A CB     1 
ATOM   2112  C  CG     . TYR   A 1  272 ? 15.020  -87.498  -67.331  1.00 35.16  ? 272 TYR   A CG     1 
ATOM   2113  C  CD1    . TYR   A 1  272 ? 13.814  -87.904  -66.771  1.00 39.58  ? 272 TYR   A CD1    1 
ATOM   2114  C  CD2    . TYR   A 1  272 ? 16.026  -88.437  -67.456  1.00 36.56  ? 272 TYR   A CD2    1 
ATOM   2115  C  CE1    . TYR   A 1  272 ? 13.619  -89.216  -66.341  1.00 34.95  ? 272 TYR   A CE1    1 
ATOM   2116  C  CE2    . TYR   A 1  272 ? 15.839  -89.747  -67.032  1.00 38.00  ? 272 TYR   A CE2    1 
ATOM   2117  C  CZ     . TYR   A 1  272 ? 14.635  -90.134  -66.485  1.00 35.60  ? 272 TYR   A CZ     1 
ATOM   2118  O  OH     . TYR   A 1  272 ? 14.460  -91.430  -66.054  1.00 38.80  ? 272 TYR   A OH     1 
ATOM   2119  N  N      . ALA   A 1  273 ? 12.945  -87.146  -70.102  1.00 37.18  ? 273 ALA   A N      1 
ATOM   2120  C  CA     . ALA   A 1  273 ? 11.564  -87.607  -70.148  1.00 43.84  ? 273 ALA   A CA     1 
ATOM   2121  C  C      . ALA   A 1  273 ? 11.542  -89.126  -70.098  1.00 43.02  ? 273 ALA   A C      1 
ATOM   2122  O  O      . ALA   A 1  273 ? 12.450  -89.785  -70.624  1.00 43.47  ? 273 ALA   A O      1 
ATOM   2123  C  CB     . ALA   A 1  273 ? 10.819  -87.125  -71.405  1.00 37.29  ? 273 ALA   A CB     1 
ATOM   2124  N  N      . PRO   A 1  274 ? 10.485  -89.709  -69.535  1.00 39.62  ? 274 PRO   A N      1 
ATOM   2125  C  CA     . PRO   A 1  274 ? 9.299   -89.048  -69.025  1.00 43.71  ? 274 PRO   A CA     1 
ATOM   2126  C  C      . PRO   A 1  274 ? 9.259   -89.055  -67.499  1.00 45.72  ? 274 PRO   A C      1 
ATOM   2127  O  O      . PRO   A 1  274 ? 9.660   -90.029  -66.860  1.00 39.76  ? 274 PRO   A O      1 
ATOM   2128  C  CB     . PRO   A 1  274 ? 8.185   -89.905  -69.621  1.00 41.33  ? 274 PRO   A CB     1 
ATOM   2129  C  CG     . PRO   A 1  274 ? 8.748   -91.298  -69.441  1.00 37.08  ? 274 PRO   A CG     1 
ATOM   2130  C  CD     . PRO   A 1  274 ? 10.241  -91.157  -69.677  1.00 43.42  ? 274 PRO   A CD     1 
ATOM   2131  N  N      . VAL   A 1  275 ? 8.745   -87.997  -66.885  1.00 46.87  ? 275 VAL   A N      1 
ATOM   2132  C  CA     . VAL   A 1  275 ? 8.593   -87.939  -65.442  1.00 42.06  ? 275 VAL   A CA     1 
ATOM   2133  C  C      . VAL   A 1  275 ? 7.111   -88.121  -65.144  1.00 44.97  ? 275 VAL   A C      1 
ATOM   2134  O  O      . VAL   A 1  275 ? 6.303   -87.217  -65.397  1.00 41.03  ? 275 VAL   A O      1 
ATOM   2135  C  CB     . VAL   A 1  275 ? 9.143   -86.632  -64.862  1.00 38.40  ? 275 VAL   A CB     1 
ATOM   2136  C  CG1    . VAL   A 1  275 ? 8.854   -86.559  -63.370  1.00 42.52  ? 275 VAL   A CG1    1 
ATOM   2137  C  CG2    . VAL   A 1  275 ? 10.635  -86.567  -65.107  1.00 29.36  ? 275 VAL   A CG2    1 
ATOM   2138  N  N      . ILE   A 1  276 ? 6.770   -89.282  -64.577  1.00 42.80  ? 276 ILE   A N      1 
ATOM   2139  C  CA     . ILE   A 1  276 ? 5.397   -89.759  -64.443  1.00 50.15  ? 276 ILE   A CA     1 
ATOM   2140  C  C      . ILE   A 1  276 ? 5.120   -90.067  -62.977  1.00 46.80  ? 276 ILE   A C      1 
ATOM   2141  O  O      . ILE   A 1  276 ? 5.880   -90.806  -62.340  1.00 47.32  ? 276 ILE   A O      1 
ATOM   2142  C  CB     . ILE   A 1  276 ? 5.159   -91.010  -65.325  1.00 56.40  ? 276 ILE   A CB     1 
ATOM   2143  C  CG1    . ILE   A 1  276 ? 5.199   -90.641  -66.812  1.00 45.85  ? 276 ILE   A CG1    1 
ATOM   2144  C  CG2    . ILE   A 1  276 ? 3.868   -91.723  -64.962  1.00 46.29  ? 276 ILE   A CG2    1 
ATOM   2145  C  CD1    . ILE   A 1  276 ? 4.257   -89.551  -67.163  1.00 45.44  ? 276 ILE   A CD1    1 
ATOM   2146  N  N      . SER   A 1  277 ? 4.010   -89.539  -62.460  1.00 52.10  ? 277 SER   A N      1 
ATOM   2147  C  CA     . SER   A 1  277 ? 3.694   -89.669  -61.040  1.00 54.17  ? 277 SER   A CA     1 
ATOM   2148  C  C      . SER   A 1  277 ? 3.323   -91.100  -60.666  1.00 54.53  ? 277 SER   A C      1 
ATOM   2149  O  O      . SER   A 1  277 ? 2.575   -91.776  -61.373  1.00 59.18  ? 277 SER   A O      1 
ATOM   2150  C  CB     . SER   A 1  277 ? 2.545   -88.737  -60.656  1.00 53.22  ? 277 SER   A CB     1 
ATOM   2151  O  OG     . SER   A 1  277 ? 2.059   -89.067  -59.363  1.00 53.13  ? 277 SER   A OG     1 
ATOM   2152  N  N      . ALA   A 1  278 ? 3.832   -91.554  -59.520  1.00 60.20  ? 278 ALA   A N      1 
ATOM   2153  C  CA     . ALA   A 1  278 ? 3.483   -92.878  -59.018  1.00 59.90  ? 278 ALA   A CA     1 
ATOM   2154  C  C      . ALA   A 1  278 ? 2.061   -92.940  -58.471  1.00 63.49  ? 278 ALA   A C      1 
ATOM   2155  O  O      . ALA   A 1  278 ? 1.550   -94.041  -58.246  1.00 60.76  ? 278 ALA   A O      1 
ATOM   2156  C  CB     . ALA   A 1  278 ? 4.482   -93.305  -57.944  1.00 51.28  ? 278 ALA   A CB     1 
ATOM   2157  N  N      . GLU   A 1  279 ? 1.410   -91.791  -58.269  1.00 65.72  ? 279 GLU   A N      1 
ATOM   2158  C  CA     . GLU   A 1  279 ? 0.030   -91.771  -57.798  1.00 64.23  ? 279 GLU   A CA     1 
ATOM   2159  C  C      . GLU   A 1  279 ? -0.962  -92.010  -58.922  1.00 67.56  ? 279 GLU   A C      1 
ATOM   2160  O  O      . GLU   A 1  279 ? -2.038  -92.564  -58.677  1.00 74.94  ? 279 GLU   A O      1 
ATOM   2161  C  CB     . GLU   A 1  279 ? -0.289  -90.435  -57.117  1.00 70.29  ? 279 GLU   A CB     1 
ATOM   2162  C  CG     . GLU   A 1  279 ? 0.389   -90.244  -55.780  1.00 69.03  ? 279 GLU   A CG     1 
ATOM   2163  C  CD     . GLU   A 1  279 ? 0.372   -91.516  -54.963  1.00 74.94  ? 279 GLU   A CD     1 
ATOM   2164  O  OE1    . GLU   A 1  279 ? -0.729  -92.101  -54.821  1.00 71.11  ? 279 GLU   A OE1    1 
ATOM   2165  O  OE2    . GLU   A 1  279 ? 1.457   -91.940  -54.489  1.00 66.06  ? 279 GLU   A OE2    1 
ATOM   2166  N  N      . LYS   A 1  280 ? -0.637  -91.578  -60.141  1.00 66.85  ? 280 LYS   A N      1 
ATOM   2167  C  CA     . LYS   A 1  280 ? -1.449  -91.881  -61.312  1.00 72.59  ? 280 LYS   A CA     1 
ATOM   2168  C  C      . LYS   A 1  280 ? -1.697  -93.380  -61.418  1.00 81.88  ? 280 LYS   A C      1 
ATOM   2169  O  O      . LYS   A 1  280 ? -0.776  -94.147  -61.729  1.00 82.77  ? 280 LYS   A O      1 
ATOM   2170  C  CB     . LYS   A 1  280 ? -0.773  -91.359  -62.586  1.00 68.97  ? 280 LYS   A CB     1 
ATOM   2171  C  CG     . LYS   A 1  280 ? -1.236  -89.966  -62.973  1.00 71.07  ? 280 LYS   A CG     1 
ATOM   2172  C  CD     . LYS   A 1  280 ? -0.712  -89.546  -64.327  1.00 67.91  ? 280 LYS   A CD     1 
ATOM   2173  C  CE     . LYS   A 1  280 ? -1.151  -90.474  -65.424  1.00 65.84  ? 280 LYS   A CE     1 
ATOM   2174  N  NZ     . LYS   A 1  280 ? -0.390  -90.162  -66.668  1.00 59.74  ? 280 LYS   A NZ     1 
ATOM   2175  N  N      . ALA   A 1  281 ? -2.938  -93.809  -61.163  1.00 87.19  ? 281 ALA   A N      1 
ATOM   2176  C  CA     . ALA   A 1  281 ? -3.238  -95.238  -61.189  1.00 93.01  ? 281 ALA   A CA     1 
ATOM   2177  C  C      . ALA   A 1  281 ? -3.189  -95.782  -62.609  1.00 98.61  ? 281 ALA   A C      1 
ATOM   2178  O  O      . ALA   A 1  281 ? -2.671  -96.881  -62.840  1.00 101.42 ? 281 ALA   A O      1 
ATOM   2179  C  CB     . ALA   A 1  281 ? -4.604  -95.505  -60.559  1.00 91.32  ? 281 ALA   A CB     1 
ATOM   2180  N  N      . TYR   A 1  282 ? -3.709  -95.014  -63.573  1.00 98.31  ? 282 TYR   A N      1 
ATOM   2181  C  CA     . TYR   A 1  282 ? -3.786  -95.400  -64.981  1.00 97.74  ? 282 TYR   A CA     1 
ATOM   2182  C  C      . TYR   A 1  282 ? -2.856  -94.496  -65.782  1.00 94.80  ? 282 TYR   A C      1 
ATOM   2183  O  O      . TYR   A 1  282 ? -3.100  -93.288  -65.894  1.00 90.33  ? 282 TYR   A O      1 
ATOM   2184  C  CB     . TYR   A 1  282 ? -5.221  -95.295  -65.495  1.00 98.74  ? 282 TYR   A CB     1 
ATOM   2185  C  CG     . TYR   A 1  282 ? -5.376  -95.558  -66.974  1.00 101.04 ? 282 TYR   A CG     1 
ATOM   2186  C  CD1    . TYR   A 1  282 ? -5.497  -96.852  -67.462  1.00 101.99 ? 282 TYR   A CD1    1 
ATOM   2187  C  CD2    . TYR   A 1  282 ? -5.394  -94.510  -67.886  1.00 101.65 ? 282 TYR   A CD2    1 
ATOM   2188  C  CE1    . TYR   A 1  282 ? -5.639  -97.092  -68.818  1.00 102.38 ? 282 TYR   A CE1    1 
ATOM   2189  C  CE2    . TYR   A 1  282 ? -5.533  -94.742  -69.247  1.00 102.70 ? 282 TYR   A CE2    1 
ATOM   2190  C  CZ     . TYR   A 1  282 ? -5.654  -96.038  -69.706  1.00 102.72 ? 282 TYR   A CZ     1 
ATOM   2191  O  OH     . TYR   A 1  282 ? -5.792  -96.279  -71.054  1.00 101.85 ? 282 TYR   A OH     1 
ATOM   2192  N  N      . HIS   A 1  283 ? -1.798  -95.081  -66.339  1.00 90.02  ? 283 HIS   A N      1 
ATOM   2193  C  CA     . HIS   A 1  283 ? -0.817  -94.343  -67.122  1.00 80.86  ? 283 HIS   A CA     1 
ATOM   2194  C  C      . HIS   A 1  283 ? -0.589  -95.039  -68.453  1.00 82.05  ? 283 HIS   A C      1 
ATOM   2195  O  O      . HIS   A 1  283 ? -0.275  -96.234  -68.484  1.00 87.01  ? 283 HIS   A O      1 
ATOM   2196  C  CB     . HIS   A 1  283 ? 0.521   -94.220  -66.387  1.00 76.49  ? 283 HIS   A CB     1 
ATOM   2197  C  CG     . HIS   A 1  283 ? 1.593   -93.595  -67.224  1.00 76.67  ? 283 HIS   A CG     1 
ATOM   2198  N  ND1    . HIS   A 1  283 ? 1.468   -92.330  -67.768  1.00 74.42  ? 283 HIS   A ND1    1 
ATOM   2199  C  CD2    . HIS   A 1  283 ? 2.775   -94.084  -67.674  1.00 71.78  ? 283 HIS   A CD2    1 
ATOM   2200  C  CE1    . HIS   A 1  283 ? 2.543   -92.054  -68.487  1.00 71.50  ? 283 HIS   A CE1    1 
ATOM   2201  N  NE2    . HIS   A 1  283 ? 3.352   -93.101  -68.445  1.00 74.20  ? 283 HIS   A NE2    1 
ATOM   2202  N  N      . GLU   A 1  284 ? -0.720  -94.288  -69.544  1.00 77.32  ? 284 GLU   A N      1 
ATOM   2203  C  CA     . GLU   A 1  284 ? -0.456  -94.808  -70.882  1.00 75.04  ? 284 GLU   A CA     1 
ATOM   2204  C  C      . GLU   A 1  284 ? 1.034   -94.666  -71.166  1.00 76.81  ? 284 GLU   A C      1 
ATOM   2205  O  O      . GLU   A 1  284 ? 1.569   -93.550  -71.141  1.00 76.48  ? 284 GLU   A O      1 
ATOM   2206  C  CB     . GLU   A 1  284 ? -1.292  -94.068  -71.929  1.00 77.02  ? 284 GLU   A CB     1 
ATOM   2207  C  CG     . GLU   A 1  284 ? -2.798  -94.011  -71.604  1.00 75.41  ? 284 GLU   A CG     1 
ATOM   2208  C  CD     . GLU   A 1  284 ? -3.618  -93.288  -72.670  1.00 76.67  ? 284 GLU   A CD     1 
ATOM   2209  O  OE1    . GLU   A 1  284 ? -3.095  -92.328  -73.278  1.00 78.92  ? 284 GLU   A OE1    1 
ATOM   2210  O  OE2    . GLU   A 1  284 ? -4.799  -93.655  -72.883  1.00 77.24  ? 284 GLU   A OE2    1 
ATOM   2211  N  N      . GLN   A 1  285 ? 1.704   -95.791  -71.429  1.00 80.41  ? 285 GLN   A N      1 
ATOM   2212  C  CA     . GLN   A 1  285 ? 3.161   -95.779  -71.537  1.00 72.76  ? 285 GLN   A CA     1 
ATOM   2213  C  C      . GLN   A 1  285 ? 3.591   -95.081  -72.818  1.00 67.09  ? 285 GLN   A C      1 
ATOM   2214  O  O      . GLN   A 1  285 ? 3.123   -95.419  -73.911  1.00 70.75  ? 285 GLN   A O      1 
ATOM   2215  C  CB     . GLN   A 1  285 ? 3.726   -97.204  -71.480  1.00 73.78  ? 285 GLN   A CB     1 
ATOM   2216  C  CG     . GLN   A 1  285 ? 3.571   -97.868  -70.102  1.00 78.07  ? 285 GLN   A CG     1 
ATOM   2217  C  CD     . GLN   A 1  285 ? 4.586   -97.374  -69.058  1.00 77.45  ? 285 GLN   A CD     1 
ATOM   2218  O  OE1    . GLN   A 1  285 ? 5.731   -97.034  -69.381  1.00 73.61  ? 285 GLN   A OE1    1 
ATOM   2219  N  NE2    . GLN   A 1  285 ? 4.144   -97.292  -67.807  1.00 73.52  ? 285 GLN   A NE2    1 
ATOM   2220  N  N      . LEU   A 1  286 ? 4.489   -94.107  -72.670  1.00 64.39  ? 286 LEU   A N      1 
ATOM   2221  C  CA     . LEU   A 1  286 ? 4.975   -93.295  -73.775  1.00 54.48  ? 286 LEU   A CA     1 
ATOM   2222  C  C      . LEU   A 1  286 ? 5.999   -94.034  -74.633  1.00 50.92  ? 286 LEU   A C      1 
ATOM   2223  O  O      . LEU   A 1  286 ? 6.804   -94.830  -74.144  1.00 55.71  ? 286 LEU   A O      1 
ATOM   2224  C  CB     . LEU   A 1  286 ? 5.595   -92.009  -73.243  1.00 54.25  ? 286 LEU   A CB     1 
ATOM   2225  C  CG     . LEU   A 1  286 ? 4.626   -90.898  -72.886  1.00 48.94  ? 286 LEU   A CG     1 
ATOM   2226  C  CD1    . LEU   A 1  286 ? 4.025   -91.204  -71.565  1.00 60.98  ? 286 LEU   A CD1    1 
ATOM   2227  C  CD2    . LEU   A 1  286 ? 5.445   -89.647  -72.804  1.00 58.11  ? 286 LEU   A CD2    1 
ATOM   2228  N  N      . SER   A 1  287 ? 5.997   -93.705  -75.918  1.00 47.70  ? 287 SER   A N      1 
ATOM   2229  C  CA     . SER   A 1  287 ? 6.771   -94.379  -76.943  1.00 44.96  ? 287 SER   A CA     1 
ATOM   2230  C  C      . SER   A 1  287 ? 8.171   -93.796  -77.067  1.00 49.80  ? 287 SER   A C      1 
ATOM   2231  O  O      . SER   A 1  287 ? 8.488   -92.748  -76.507  1.00 49.65  ? 287 SER   A O      1 
ATOM   2232  C  CB     . SER   A 1  287 ? 6.063   -94.240  -78.276  1.00 43.74  ? 287 SER   A CB     1 
ATOM   2233  O  OG     . SER   A 1  287 ? 5.998   -92.872  -78.598  1.00 42.99  ? 287 SER   A OG     1 
ATOM   2234  N  N      . VAL   A 1  288 ? 9.009   -94.481  -77.853  1.00 49.53  ? 288 VAL   A N      1 
ATOM   2235  C  CA     . VAL   A 1  288 ? 10.305  -93.913  -78.209  1.00 42.98  ? 288 VAL   A CA     1 
ATOM   2236  C  C      . VAL   A 1  288 ? 10.130  -92.531  -78.819  1.00 43.84  ? 288 VAL   A C      1 
ATOM   2237  O  O      . VAL   A 1  288 ? 10.860  -91.592  -78.488  1.00 49.91  ? 288 VAL   A O      1 
ATOM   2238  C  CB     . VAL   A 1  288 ? 11.078  -94.851  -79.156  1.00 39.04  ? 288 VAL   A CB     1 
ATOM   2239  C  CG1    . VAL   A 1  288 ? 12.277  -94.125  -79.775  1.00 34.34  ? 288 VAL   A CG1    1 
ATOM   2240  C  CG2    . VAL   A 1  288 ? 11.534  -96.065  -78.415  1.00 44.38  ? 288 VAL   A CG2    1 
ATOM   2241  N  N      . ALA   A 1  289 ? 9.177   -92.368  -79.724  1.00 45.70  ? 289 ALA   A N      1 
ATOM   2242  C  CA     . ALA   A 1  289 ? 9.130   -91.072  -80.388  1.00 52.21  ? 289 ALA   A CA     1 
ATOM   2243  C  C      . ALA   A 1  289 ? 8.579   -90.013  -79.444  1.00 54.06  ? 289 ALA   A C      1 
ATOM   2244  O  O      . ALA   A 1  289 ? 9.117   -88.903  -79.375  1.00 50.35  ? 289 ALA   A O      1 
ATOM   2245  C  CB     . ALA   A 1  289 ? 8.322   -91.143  -81.684  1.00 44.78  ? 289 ALA   A CB     1 
ATOM   2246  N  N      . GLU   A 1  290 ? 7.539   -90.353  -78.671  1.00 48.36  ? 290 GLU   A N      1 
ATOM   2247  C  CA     . GLU   A 1  290 ? 6.982   -89.386  -77.730  1.00 47.50  ? 290 GLU   A CA     1 
ATOM   2248  C  C      . GLU   A 1  290 ? 8.047   -88.878  -76.747  1.00 51.77  ? 290 GLU   A C      1 
ATOM   2249  O  O      . GLU   A 1  290 ? 8.117   -87.672  -76.469  1.00 51.26  ? 290 GLU   A O      1 
ATOM   2250  C  CB     . GLU   A 1  290 ? 5.782   -89.998  -76.987  1.00 50.99  ? 290 GLU   A CB     1 
ATOM   2251  C  CG     . GLU   A 1  290 ? 4.522   -90.282  -77.857  1.00 44.80  ? 290 GLU   A CG     1 
ATOM   2252  C  CD     . GLU   A 1  290 ? 3.419   -91.052  -77.101  1.00 51.14  ? 290 GLU   A CD     1 
ATOM   2253  O  OE1    . GLU   A 1  290 ? 3.677   -92.209  -76.689  1.00 48.93  ? 290 GLU   A OE1    1 
ATOM   2254  O  OE2    . GLU   A 1  290 ? 2.281   -90.536  -76.947  1.00 52.39  ? 290 GLU   A OE2    1 
ATOM   2255  N  N      . ILE   A 1  291 ? 8.886   -89.777  -76.213  1.00 50.78  ? 291 ILE   A N      1 
ATOM   2256  C  CA     . ILE   A 1  291 ? 9.865   -89.367  -75.208  1.00 45.50  ? 291 ILE   A CA     1 
ATOM   2257  C  C      . ILE   A 1  291 ? 11.073  -88.694  -75.854  1.00 51.83  ? 291 ILE   A C      1 
ATOM   2258  O  O      . ILE   A 1  291 ? 11.707  -87.834  -75.232  1.00 53.19  ? 291 ILE   A O      1 
ATOM   2259  C  CB     . ILE   A 1  291 ? 10.308  -90.549  -74.319  1.00 41.40  ? 291 ILE   A CB     1 
ATOM   2260  C  CG1    . ILE   A 1  291 ? 11.183  -91.524  -75.083  1.00 39.25  ? 291 ILE   A CG1    1 
ATOM   2261  C  CG2    . ILE   A 1  291 ? 9.131   -91.279  -73.699  1.00 43.63  ? 291 ILE   A CG2    1 
ATOM   2262  C  CD1    . ILE   A 1  291 ? 11.638  -92.667  -74.221  1.00 42.90  ? 291 ILE   A CD1    1 
ATOM   2263  N  N      . THR   A 1  292 ? 11.432  -89.062  -77.089  1.00 47.69  ? 292 THR   A N      1 
ATOM   2264  C  CA     . THR   A 1  292 ? 12.491  -88.315  -77.764  1.00 49.15  ? 292 THR   A CA     1 
ATOM   2265  C  C      . THR   A 1  292 ? 12.042  -86.909  -78.134  1.00 51.72  ? 292 THR   A C      1 
ATOM   2266  O  O      . THR   A 1  292 ? 12.867  -85.989  -78.211  1.00 58.14  ? 292 THR   A O      1 
ATOM   2267  C  CB     . THR   A 1  292 ? 12.961  -89.038  -79.022  1.00 49.22  ? 292 THR   A CB     1 
ATOM   2268  O  OG1    . THR   A 1  292 ? 13.258  -90.399  -78.705  1.00 49.53  ? 292 THR   A OG1    1 
ATOM   2269  C  CG2    . THR   A 1  292 ? 14.209  -88.379  -79.557  1.00 43.52  ? 292 THR   A CG2    1 
ATOM   2270  N  N      . ASN   A 1  293 ? 10.754  -86.729  -78.406  1.00 51.74  ? 293 ASN   A N      1 
ATOM   2271  C  CA     . ASN   A 1  293 ? 10.251  -85.399  -78.708  1.00 52.59  ? 293 ASN   A CA     1 
ATOM   2272  C  C      . ASN   A 1  293 ? 10.247  -84.539  -77.456  1.00 54.31  ? 293 ASN   A C      1 
ATOM   2273  O  O      . ASN   A 1  293 ? 10.541  -83.338  -77.523  1.00 52.45  ? 293 ASN   A O      1 
ATOM   2274  C  CB     . ASN   A 1  293 ? 8.846   -85.494  -79.306  1.00 54.52  ? 293 ASN   A CB     1 
ATOM   2275  C  CG     . ASN   A 1  293 ? 8.421   -84.214  -80.008  1.00 64.86  ? 293 ASN   A CG     1 
ATOM   2276  O  OD1    . ASN   A 1  293 ? 9.203   -83.605  -80.758  1.00 66.50  ? 293 ASN   A OD1    1 
ATOM   2277  N  ND2    . ASN   A 1  293 ? 7.182   -83.770  -79.733  1.00 60.15  ? 293 ASN   A ND2    1 
ATOM   2278  N  N      . ALA   A 1  294 ? 9.927   -85.151  -76.304  1.00 53.80  ? 294 ALA   A N      1 
ATOM   2279  C  CA     . ALA   A 1  294 ? 9.913   -84.451  -75.023  1.00 50.82  ? 294 ALA   A CA     1 
ATOM   2280  C  C      . ALA   A 1  294 ? 11.276  -83.869  -74.665  1.00 47.19  ? 294 ALA   A C      1 
ATOM   2281  O  O      . ALA   A 1  294 ? 11.342  -82.947  -73.852  1.00 47.40  ? 294 ALA   A O      1 
ATOM   2282  C  CB     . ALA   A 1  294 ? 9.429   -85.393  -73.922  1.00 43.53  ? 294 ALA   A CB     1 
ATOM   2283  N  N      . CYS   A 1  295 ? 12.350  -84.373  -75.269  1.00 45.64  ? 295 CYS   A N      1 
ATOM   2284  C  CA     . CYS   A 1  295 ? 13.693  -83.865  -75.054  1.00 44.52  ? 295 CYS   A CA     1 
ATOM   2285  C  C      . CYS   A 1  295 ? 13.901  -82.487  -75.661  1.00 45.02  ? 295 CYS   A C      1 
ATOM   2286  O  O      . CYS   A 1  295 ? 14.915  -81.845  -75.360  1.00 45.25  ? 295 CYS   A O      1 
ATOM   2287  C  CB     . CYS   A 1  295 ? 14.711  -84.855  -75.638  1.00 48.46  ? 295 CYS   A CB     1 
ATOM   2288  S  SG     . CYS   A 1  295 ? 14.848  -86.442  -74.743  1.00 53.66  ? 295 CYS   A SG     1 
ATOM   2289  N  N      . PHE   A 1  296 ? 12.989  -82.028  -76.518  1.00 45.27  ? 296 PHE   A N      1 
ATOM   2290  C  CA     . PHE   A 1  296 ? 13.094  -80.720  -77.156  1.00 48.20  ? 296 PHE   A CA     1 
ATOM   2291  C  C      . PHE   A 1  296 ? 12.029  -79.766  -76.663  1.00 55.59  ? 296 PHE   A C      1 
ATOM   2292  O  O      . PHE   A 1  296 ? 11.810  -78.720  -77.284  1.00 57.74  ? 296 PHE   A O      1 
ATOM   2293  C  CB     . PHE   A 1  296 ? 13.034  -80.839  -78.679  1.00 43.14  ? 296 PHE   A CB     1 
ATOM   2294  C  CG     . PHE   A 1  296 ? 14.153  -81.659  -79.243  1.00 53.74  ? 296 PHE   A CG     1 
ATOM   2295  C  CD1    . PHE   A 1  296 ? 15.349  -81.060  -79.629  1.00 41.92  ? 296 PHE   A CD1    1 
ATOM   2296  C  CD2    . PHE   A 1  296 ? 14.036  -83.048  -79.319  1.00 50.85  ? 296 PHE   A CD2    1 
ATOM   2297  C  CE1    . PHE   A 1  296 ? 16.387  -81.812  -80.111  1.00 43.61  ? 296 PHE   A CE1    1 
ATOM   2298  C  CE2    . PHE   A 1  296 ? 15.075  -83.806  -79.809  1.00 51.42  ? 296 PHE   A CE2    1 
ATOM   2299  C  CZ     . PHE   A 1  296 ? 16.263  -83.182  -80.208  1.00 49.86  ? 296 PHE   A CZ     1 
ATOM   2300  N  N      . GLU   A 1  297 ? 11.359  -80.111  -75.567  1.00 49.49  ? 297 GLU   A N      1 
ATOM   2301  C  CA     . GLU   A 1  297 ? 10.457  -79.212  -74.876  1.00 53.72  ? 297 GLU   A CA     1 
ATOM   2302  C  C      . GLU   A 1  297 ? 11.198  -78.585  -73.701  1.00 53.19  ? 297 GLU   A C      1 
ATOM   2303  O  O      . GLU   A 1  297 ? 11.811  -79.312  -72.903  1.00 51.88  ? 297 GLU   A O      1 
ATOM   2304  C  CB     . GLU   A 1  297 ? 9.220   -79.960  -74.387  1.00 52.85  ? 297 GLU   A CB     1 
ATOM   2305  C  CG     . GLU   A 1  297 ? 7.964   -79.154  -74.568  1.00 62.53  ? 297 GLU   A CG     1 
ATOM   2306  C  CD     . GLU   A 1  297 ? 7.633   -78.991  -76.033  1.00 74.13  ? 297 GLU   A CD     1 
ATOM   2307  O  OE1    . GLU   A 1  297 ? 7.102   -79.947  -76.640  1.00 75.07  ? 297 GLU   A OE1    1 
ATOM   2308  O  OE2    . GLU   A 1  297 ? 7.947   -77.920  -76.592  1.00 75.80  ? 297 GLU   A OE2    1 
ATOM   2309  N  N      . PRO   A 1  298 ? 11.208  -77.258  -73.566  1.00 50.16  ? 298 PRO   A N      1 
ATOM   2310  C  CA     . PRO   A 1  298 ? 11.929  -76.659  -72.438  1.00 39.61  ? 298 PRO   A CA     1 
ATOM   2311  C  C      . PRO   A 1  298 ? 11.420  -77.108  -71.081  1.00 39.99  ? 298 PRO   A C      1 
ATOM   2312  O  O      . PRO   A 1  298 ? 12.224  -77.268  -70.165  1.00 42.36  ? 298 PRO   A O      1 
ATOM   2313  C  CB     . PRO   A 1  298 ? 11.726  -75.162  -72.675  1.00 48.80  ? 298 PRO   A CB     1 
ATOM   2314  C  CG     . PRO   A 1  298 ? 11.637  -75.073  -74.200  1.00 49.76  ? 298 PRO   A CG     1 
ATOM   2315  C  CD     . PRO   A 1  298 ? 10.765  -76.241  -74.537  1.00 51.25  ? 298 PRO   A CD     1 
ATOM   2316  N  N      . ALA   A 1  299 ? 10.124  -77.368  -70.923  1.00 42.87  ? 299 ALA   A N      1 
ATOM   2317  C  CA     . ALA   A 1  299 ? 9.595   -77.757  -69.616  1.00 40.19  ? 299 ALA   A CA     1 
ATOM   2318  C  C      . ALA   A 1  299 ? 10.140  -79.085  -69.113  1.00 42.26  ? 299 ALA   A C      1 
ATOM   2319  O  O      . ALA   A 1  299 ? 9.721   -79.530  -68.034  1.00 39.19  ? 299 ALA   A O      1 
ATOM   2320  C  CB     . ALA   A 1  299 ? 8.074   -77.841  -69.639  1.00 35.93  ? 299 ALA   A CB     1 
ATOM   2321  N  N      . ASN   A 1  300 ? 11.035  -79.735  -69.850  1.00 38.89  ? 300 ASN   A N      1 
ATOM   2322  C  CA     . ASN   A 1  300 ? 11.662  -80.957  -69.378  1.00 41.08  ? 300 ASN   A CA     1 
ATOM   2323  C  C      . ASN   A 1  300 ? 13.156  -80.776  -69.123  1.00 41.48  ? 300 ASN   A C      1 
ATOM   2324  O  O      . ASN   A 1  300 ? 13.811  -81.690  -68.609  1.00 37.99  ? 300 ASN   A O      1 
ATOM   2325  C  CB     . ASN   A 1  300 ? 11.409  -82.096  -70.381  1.00 39.22  ? 300 ASN   A CB     1 
ATOM   2326  C  CG     . ASN   A 1  300 ? 9.922   -82.330  -70.633  1.00 42.27  ? 300 ASN   A CG     1 
ATOM   2327  O  OD1    . ASN   A 1  300 ? 9.097   -82.327  -69.703  1.00 36.71  ? 300 ASN   A OD1    1 
ATOM   2328  N  ND2    . ASN   A 1  300 ? 9.573   -82.550  -71.897  1.00 47.46  ? 300 ASN   A ND2    1 
ATOM   2329  N  N      . GLN   A 1  301 ? 13.702  -79.614  -69.451  1.00 42.73  ? 301 GLN   A N      1 
ATOM   2330  C  CA     . GLN   A 1  301 ? 15.125  -79.357  -69.328  1.00 39.70  ? 301 GLN   A CA     1 
ATOM   2331  C  C      . GLN   A 1  301 ? 15.514  -79.160  -67.863  1.00 36.34  ? 301 GLN   A C      1 
ATOM   2332  O  O      . GLN   A 1  301 ? 14.693  -78.780  -67.027  1.00 39.19  ? 301 GLN   A O      1 
ATOM   2333  C  CB     . GLN   A 1  301 ? 15.474  -78.139  -70.178  1.00 37.12  ? 301 GLN   A CB     1 
ATOM   2334  C  CG     . GLN   A 1  301 ? 15.031  -78.349  -71.610  1.00 39.30  ? 301 GLN   A CG     1 
ATOM   2335  C  CD     . GLN   A 1  301 ? 15.157  -77.120  -72.475  1.00 48.22  ? 301 GLN   A CD     1 
ATOM   2336  O  OE1    . GLN   A 1  301 ? 15.533  -76.055  -72.002  1.00 53.48  ? 301 GLN   A OE1    1 
ATOM   2337  N  NE2    . GLN   A 1  301 ? 14.863  -77.264  -73.761  1.00 46.45  ? 301 GLN   A NE2    1 
ATOM   2338  N  N      . MET   A 1  302 ? 16.772  -79.485  -67.547  1.00 37.79  ? 302 MET   A N      1 
ATOM   2339  C  CA     . MET   A 1  302 ? 17.343  -79.220  -66.234  1.00 34.90  ? 302 MET   A CA     1 
ATOM   2340  C  C      . MET   A 1  302 ? 17.550  -77.735  -65.982  1.00 41.66  ? 302 MET   A C      1 
ATOM   2341  O  O      . MET   A 1  302 ? 17.766  -77.333  -64.833  1.00 41.73  ? 302 MET   A O      1 
ATOM   2342  C  CB     . MET   A 1  302 ? 18.671  -79.942  -66.080  1.00 30.12  ? 302 MET   A CB     1 
ATOM   2343  C  CG     . MET   A 1  302 ? 18.520  -81.417  -65.801  1.00 41.76  ? 302 MET   A CG     1 
ATOM   2344  S  SD     . MET   A 1  302 ? 17.092  -81.841  -64.769  1.00 51.40  ? 302 MET   A SD     1 
ATOM   2345  C  CE     . MET   A 1  302 ? 16.237  -82.949  -65.843  1.00 41.16  ? 302 MET   A CE     1 
ATOM   2346  N  N      . VAL   A 1  303 ? 17.483  -76.920  -67.026  1.00 35.83  ? 303 VAL   A N      1 
ATOM   2347  C  CA     . VAL   A 1  303 ? 17.574  -75.475  -66.929  1.00 34.21  ? 303 VAL   A CA     1 
ATOM   2348  C  C      . VAL   A 1  303 ? 16.560  -74.931  -67.914  1.00 44.54  ? 303 VAL   A C      1 
ATOM   2349  O  O      . VAL   A 1  303 ? 16.506  -75.389  -69.061  1.00 49.48  ? 303 VAL   A O      1 
ATOM   2350  C  CB     . VAL   A 1  303 ? 18.986  -74.948  -67.274  1.00 38.88  ? 303 VAL   A CB     1 
ATOM   2351  C  CG1    . VAL   A 1  303 ? 19.085  -73.450  -67.023  1.00 40.44  ? 303 VAL   A CG1    1 
ATOM   2352  C  CG2    . VAL   A 1  303 ? 20.078  -75.716  -66.522  1.00 35.38  ? 303 VAL   A CG2    1 
ATOM   2353  N  N      . LYS   A 1  304 ? 15.751  -73.969  -67.489  1.00 45.74  ? 304 LYS   A N      1 
ATOM   2354  C  CA     . LYS   A 1  304 ? 14.775  -73.402  -68.409  1.00 42.87  ? 304 LYS   A CA     1 
ATOM   2355  C  C      . LYS   A 1  304 ? 15.492  -72.434  -69.343  1.00 46.20  ? 304 LYS   A C      1 
ATOM   2356  O  O      . LYS   A 1  304 ? 16.205  -71.534  -68.887  1.00 54.00  ? 304 LYS   A O      1 
ATOM   2357  C  CB     . LYS   A 1  304 ? 13.658  -72.706  -67.644  1.00 45.97  ? 304 LYS   A CB     1 
ATOM   2358  C  CG     . LYS   A 1  304 ? 12.763  -73.634  -66.884  1.00 40.18  ? 304 LYS   A CG     1 
ATOM   2359  C  CD     . LYS   A 1  304 ? 11.657  -72.869  -66.182  1.00 43.48  ? 304 LYS   A CD     1 
ATOM   2360  C  CE     . LYS   A 1  304 ? 10.805  -73.803  -65.345  1.00 48.71  ? 304 LYS   A CE     1 
ATOM   2361  N  NZ     . LYS   A 1  304 ? 9.585   -73.107  -64.855  1.00 64.82  ? 304 LYS   A NZ     1 
ATOM   2362  N  N      . CYS   A 1  305 ? 15.343  -72.649  -70.640  1.00 41.91  ? 305 CYS   A N      1 
ATOM   2363  C  CA     . CYS   A 1  305 ? 15.920  -71.799  -71.675  1.00 42.65  ? 305 CYS   A CA     1 
ATOM   2364  C  C      . CYS   A 1  305 ? 15.347  -72.304  -72.985  1.00 47.32  ? 305 CYS   A C      1 
ATOM   2365  O  O      . CYS   A 1  305 ? 14.571  -73.261  -73.005  1.00 44.77  ? 305 CYS   A O      1 
ATOM   2366  C  CB     . CYS   A 1  305 ? 17.453  -71.805  -71.697  1.00 41.50  ? 305 CYS   A CB     1 
ATOM   2367  S  SG     . CYS   A 1  305 ? 18.247  -73.422  -71.895  1.00 46.50  ? 305 CYS   A SG     1 
ATOM   2368  N  N      . ASP   A 1  306 ? 15.743  -71.666  -74.085  1.00 43.44  ? 306 ASP   A N      1 
ATOM   2369  C  CA     . ASP   A 1  306 ? 15.112  -71.891  -75.377  1.00 41.95  ? 306 ASP   A CA     1 
ATOM   2370  C  C      . ASP   A 1  306 ? 16.162  -72.310  -76.391  1.00 47.21  ? 306 ASP   A C      1 
ATOM   2371  O  O      . ASP   A 1  306 ? 16.743  -71.456  -77.079  1.00 50.93  ? 306 ASP   A O      1 
ATOM   2372  C  CB     . ASP   A 1  306 ? 14.394  -70.633  -75.836  1.00 49.13  ? 306 ASP   A CB     1 
ATOM   2373  C  CG     . ASP   A 1  306 ? 13.301  -70.922  -76.815  1.00 50.67  ? 306 ASP   A CG     1 
ATOM   2374  O  OD1    . ASP   A 1  306 ? 13.390  -71.972  -77.483  1.00 52.91  ? 306 ASP   A OD1    1 
ATOM   2375  O  OD2    . ASP   A 1  306 ? 12.360  -70.105  -76.918  1.00 51.23  ? 306 ASP   A OD2    1 
ATOM   2376  N  N      . PRO   A 1  307 ? 16.415  -73.611  -76.544  1.00 45.72  ? 307 PRO   A N      1 
ATOM   2377  C  CA     . PRO   A 1  307 ? 17.451  -74.049  -77.492  1.00 52.15  ? 307 PRO   A CA     1 
ATOM   2378  C  C      . PRO   A 1  307 ? 17.175  -73.659  -78.952  1.00 57.59  ? 307 PRO   A C      1 
ATOM   2379  O  O      . PRO   A 1  307 ? 18.122  -73.689  -79.759  1.00 53.93  ? 307 PRO   A O      1 
ATOM   2380  C  CB     . PRO   A 1  307 ? 17.472  -75.575  -77.315  1.00 42.56  ? 307 PRO   A CB     1 
ATOM   2381  C  CG     . PRO   A 1  307 ? 16.781  -75.837  -76.047  1.00 50.33  ? 307 PRO   A CG     1 
ATOM   2382  C  CD     . PRO   A 1  307 ? 15.775  -74.750  -75.874  1.00 49.14  ? 307 PRO   A CD     1 
ATOM   2383  N  N      . ARG   A 1  308 ? 15.922  -73.312  -79.314  1.00 48.23  ? 308 ARG   A N      1 
ATOM   2384  C  CA     . ARG   A 1  308 ? 15.647  -72.806  -80.659  1.00 48.51  ? 308 ARG   A CA     1 
ATOM   2385  C  C      . ARG   A 1  308 ? 16.458  -71.556  -80.961  1.00 51.49  ? 308 ARG   A C      1 
ATOM   2386  O  O      . ARG   A 1  308 ? 16.806  -71.300  -82.119  1.00 50.39  ? 308 ARG   A O      1 
ATOM   2387  C  CB     . ARG   A 1  308 ? 14.172  -72.469  -80.842  1.00 45.02  ? 308 ARG   A CB     1 
ATOM   2388  C  CG     . ARG   A 1  308 ? 13.220  -73.620  -80.653  1.00 49.28  ? 308 ARG   A CG     1 
ATOM   2389  C  CD     . ARG   A 1  308 ? 11.785  -73.128  -80.741  1.00 45.25  ? 308 ARG   A CD     1 
ATOM   2390  N  NE     . ARG   A 1  308 ? 11.467  -72.226  -79.646  1.00 46.20  ? 308 ARG   A NE     1 
ATOM   2391  C  CZ     . ARG   A 1  308 ? 10.272  -71.710  -79.418  1.00 41.96  ? 308 ARG   A CZ     1 
ATOM   2392  N  NH1    . ARG   A 1  308 ? 9.250   -71.969  -80.211  1.00 40.56  ? 308 ARG   A NH1    1 
ATOM   2393  N  NH2    . ARG   A 1  308 ? 10.100  -70.919  -78.365  1.00 38.11  ? 308 ARG   A NH2    1 
ATOM   2394  N  N      . HIS   A 1  309 ? 16.758  -70.762  -79.939  1.00 52.31  ? 309 HIS   A N      1 
ATOM   2395  C  CA     . HIS   A 1  309 ? 17.484  -69.520  -80.129  1.00 50.09  ? 309 HIS   A CA     1 
ATOM   2396  C  C      . HIS   A 1  309 ? 18.899  -69.682  -79.616  1.00 53.36  ? 309 HIS   A C      1 
ATOM   2397  O  O      . HIS   A 1  309 ? 19.397  -68.879  -78.824  1.00 67.43  ? 309 HIS   A O      1 
ATOM   2398  C  CB     . HIS   A 1  309 ? 16.742  -68.378  -79.459  1.00 44.45  ? 309 HIS   A CB     1 
ATOM   2399  C  CG     . HIS   A 1  309 ? 15.392  -68.146  -80.053  1.00 50.29  ? 309 HIS   A CG     1 
ATOM   2400  N  ND1    . HIS   A 1  309 ? 14.221  -68.446  -79.390  1.00 52.02  ? 309 HIS   A ND1    1 
ATOM   2401  C  CD2    . HIS   A 1  309 ? 15.027  -67.687  -81.276  1.00 52.09  ? 309 HIS   A CD2    1 
ATOM   2402  C  CE1    . HIS   A 1  309 ? 13.190  -68.150  -80.167  1.00 52.53  ? 309 HIS   A CE1    1 
ATOM   2403  N  NE2    . HIS   A 1  309 ? 13.652  -67.687  -81.316  1.00 55.43  ? 309 HIS   A NE2    1 
ATOM   2404  N  N      . GLY   A 1  310 ? 19.530  -70.752  -80.060  1.00 47.72  ? 310 GLY   A N      1 
ATOM   2405  C  CA     . GLY   A 1  310 ? 20.948  -70.967  -79.892  1.00 55.23  ? 310 GLY   A CA     1 
ATOM   2406  C  C      . GLY   A 1  310 ? 21.417  -71.947  -80.947  1.00 57.50  ? 310 GLY   A C      1 
ATOM   2407  O  O      . GLY   A 1  310 ? 20.739  -72.163  -81.956  1.00 59.65  ? 310 GLY   A O      1 
ATOM   2408  N  N      . LYS   A 1  311 ? 22.563  -72.561  -80.736  1.00 53.35  ? 311 LYS   A N      1 
ATOM   2409  C  CA     . LYS   A 1  311 ? 23.039  -73.547  -81.679  1.00 54.47  ? 311 LYS   A CA     1 
ATOM   2410  C  C      . LYS   A 1  311 ? 23.666  -74.685  -80.902  1.00 52.52  ? 311 LYS   A C      1 
ATOM   2411  O  O      . LYS   A 1  311 ? 24.223  -74.486  -79.821  1.00 53.60  ? 311 LYS   A O      1 
ATOM   2412  C  CB     . LYS   A 1  311 ? 24.025  -72.923  -82.666  1.00 61.97  ? 311 LYS   A CB     1 
ATOM   2413  C  CG     . LYS   A 1  311 ? 23.407  -71.780  -83.492  1.00 66.31  ? 311 LYS   A CG     1 
ATOM   2414  C  CD     . LYS   A 1  311 ? 23.713  -71.903  -84.981  1.00 66.48  ? 311 LYS   A CD     1 
ATOM   2415  C  CE     . LYS   A 1  311 ? 23.719  -70.543  -85.653  1.00 68.34  ? 311 LYS   A CE     1 
ATOM   2416  N  NZ     . LYS   A 1  311 ? 25.083  -69.942  -85.607  1.00 73.17  ? 311 LYS   A NZ     1 
ATOM   2417  N  N      . TYR   A 1  312 ? 23.539  -75.884  -81.444  1.00 49.28  ? 312 TYR   A N      1 
ATOM   2418  C  CA     . TYR   A 1  312 ? 24.128  -77.049  -80.819  1.00 49.92  ? 312 TYR   A CA     1 
ATOM   2419  C  C      . TYR   A 1  312 ? 25.556  -77.256  -81.310  1.00 50.28  ? 312 TYR   A C      1 
ATOM   2420  O  O      . TYR   A 1  312 ? 25.918  -76.847  -82.414  1.00 51.43  ? 312 TYR   A O      1 
ATOM   2421  C  CB     . TYR   A 1  312 ? 23.301  -78.291  -81.114  1.00 46.59  ? 312 TYR   A CB     1 
ATOM   2422  C  CG     . TYR   A 1  312 ? 21.901  -78.281  -80.558  1.00 49.63  ? 312 TYR   A CG     1 
ATOM   2423  C  CD1    . TYR   A 1  312 ? 20.846  -77.725  -81.276  1.00 44.41  ? 312 TYR   A CD1    1 
ATOM   2424  C  CD2    . TYR   A 1  312 ? 21.620  -78.870  -79.326  1.00 47.07  ? 312 TYR   A CD2    1 
ATOM   2425  C  CE1    . TYR   A 1  312 ? 19.567  -77.738  -80.771  1.00 43.41  ? 312 TYR   A CE1    1 
ATOM   2426  C  CE2    . TYR   A 1  312 ? 20.331  -78.885  -78.819  1.00 40.91  ? 312 TYR   A CE2    1 
ATOM   2427  C  CZ     . TYR   A 1  312 ? 19.320  -78.320  -79.544  1.00 42.13  ? 312 TYR   A CZ     1 
ATOM   2428  O  OH     . TYR   A 1  312 ? 18.049  -78.342  -79.032  1.00 55.65  ? 312 TYR   A OH     1 
ATOM   2429  N  N      . MET   A 1  313 ? 26.372  -77.880  -80.457  1.00 48.49  ? 313 MET   A N      1 
ATOM   2430  C  CA     . MET   A 1  313 ? 27.674  -78.404  -80.847  1.00 50.21  ? 313 MET   A CA     1 
ATOM   2431  C  C      . MET   A 1  313 ? 27.795  -79.891  -80.559  1.00 47.09  ? 313 MET   A C      1 
ATOM   2432  O  O      . MET   A 1  313 ? 28.825  -80.492  -80.869  1.00 50.58  ? 313 MET   A O      1 
ATOM   2433  C  CB     . MET   A 1  313 ? 28.807  -77.659  -80.127  1.00 46.22  ? 313 MET   A CB     1 
ATOM   2434  C  CG     . MET   A 1  313 ? 28.530  -76.207  -79.875  1.00 50.64  ? 313 MET   A CG     1 
ATOM   2435  S  SD     . MET   A 1  313 ? 29.452  -75.634  -78.439  1.00 52.20  ? 313 MET   A SD     1 
ATOM   2436  C  CE     . MET   A 1  313 ? 28.725  -74.016  -78.248  1.00 55.40  ? 313 MET   A CE     1 
ATOM   2437  N  N      . ALA   A 1  314 ? 26.790  -80.498  -79.947  1.00 45.39  ? 314 ALA   A N      1 
ATOM   2438  C  CA     . ALA   A 1  314 ? 26.873  -81.915  -79.644  1.00 50.87  ? 314 ALA   A CA     1 
ATOM   2439  C  C      . ALA   A 1  314 ? 25.534  -82.368  -79.082  1.00 55.00  ? 314 ALA   A C      1 
ATOM   2440  O  O      . ALA   A 1  314 ? 24.724  -81.558  -78.626  1.00 58.22  ? 314 ALA   A O      1 
ATOM   2441  C  CB     . ALA   A 1  314 ? 28.004  -82.219  -78.668  1.00 41.91  ? 314 ALA   A CB     1 
ATOM   2442  N  N      . CYS   A 1  315 ? 25.303  -83.673  -79.133  1.00 48.69  ? 315 CYS   A N      1 
ATOM   2443  C  CA     . CYS   A 1  315 ? 24.034  -84.189  -78.667  1.00 45.60  ? 315 CYS   A CA     1 
ATOM   2444  C  C      . CYS   A 1  315 ? 24.214  -85.672  -78.397  1.00 54.48  ? 315 CYS   A C      1 
ATOM   2445  O  O      . CYS   A 1  315 ? 24.753  -86.390  -79.243  1.00 58.99  ? 315 CYS   A O      1 
ATOM   2446  C  CB     . CYS   A 1  315 ? 22.960  -83.929  -79.711  1.00 51.84  ? 315 CYS   A CB     1 
ATOM   2447  S  SG     . CYS   A 1  315 ? 21.344  -83.534  -79.057  1.00 63.24  ? 315 CYS   A SG     1 
ATOM   2448  N  N      . CYS   A 1  316 ? 23.831  -86.111  -77.204  1.00 45.18  ? 316 CYS   A N      1 
ATOM   2449  C  CA     . CYS   A 1  316 ? 23.727  -87.527  -76.891  1.00 49.50  ? 316 CYS   A CA     1 
ATOM   2450  C  C      . CYS   A 1  316 ? 22.297  -87.831  -76.506  1.00 50.24  ? 316 CYS   A C      1 
ATOM   2451  O  O      . CYS   A 1  316 ? 21.657  -87.043  -75.804  1.00 55.10  ? 316 CYS   A O      1 
ATOM   2452  C  CB     . CYS   A 1  316 ? 24.640  -87.954  -75.740  1.00 43.62  ? 316 CYS   A CB     1 
ATOM   2453  S  SG     . CYS   A 1  316 ? 26.330  -87.791  -76.109  1.00 64.86  ? 316 CYS   A SG     1 
ATOM   2454  N  N      . LEU   A 1  317 ? 21.800  -88.973  -76.948  1.00 46.73  ? 317 LEU   A N      1 
ATOM   2455  C  CA     . LEU   A 1  317 ? 20.575  -89.534  -76.397  1.00 49.14  ? 317 LEU   A CA     1 
ATOM   2456  C  C      . LEU   A 1  317 ? 20.950  -90.772  -75.596  1.00 47.16  ? 317 LEU   A C      1 
ATOM   2457  O  O      . LEU   A 1  317 ? 21.534  -91.724  -76.134  1.00 49.43  ? 317 LEU   A O      1 
ATOM   2458  C  CB     . LEU   A 1  317 ? 19.564  -89.869  -77.489  1.00 49.00  ? 317 LEU   A CB     1 
ATOM   2459  C  CG     . LEU   A 1  317 ? 19.127  -88.676  -78.331  1.00 49.73  ? 317 LEU   A CG     1 
ATOM   2460  C  CD1    . LEU   A 1  317 ? 18.473  -89.173  -79.609  1.00 44.16  ? 317 LEU   A CD1    1 
ATOM   2461  C  CD2    . LEU   A 1  317 ? 18.190  -87.783  -77.533  1.00 47.59  ? 317 LEU   A CD2    1 
ATOM   2462  N  N      . LEU   A 1  318 ? 20.652  -90.746  -74.315  1.00 40.78  ? 318 LEU   A N      1 
ATOM   2463  C  CA     . LEU   A 1  318 ? 20.875  -91.895  -73.455  1.00 43.37  ? 318 LEU   A CA     1 
ATOM   2464  C  C      . LEU   A 1  318 ? 19.512  -92.491  -73.107  1.00 45.45  ? 318 LEU   A C      1 
ATOM   2465  O  O      . LEU   A 1  318 ? 18.750  -91.896  -72.338  1.00 44.61  ? 318 LEU   A O      1 
ATOM   2466  C  CB     . LEU   A 1  318 ? 21.664  -91.474  -72.221  1.00 43.11  ? 318 LEU   A CB     1 
ATOM   2467  C  CG     . LEU   A 1  318 ? 22.881  -90.579  -72.543  1.00 44.07  ? 318 LEU   A CG     1 
ATOM   2468  C  CD1    . LEU   A 1  318 ? 23.499  -90.023  -71.268  1.00 38.66  ? 318 LEU   A CD1    1 
ATOM   2469  C  CD2    . LEU   A 1  318 ? 23.947  -91.283  -73.404  1.00 36.31  ? 318 LEU   A CD2    1 
ATOM   2470  N  N      . TYR   A 1  319 ? 19.186  -93.640  -73.704  1.00 41.23  ? 319 TYR   A N      1 
ATOM   2471  C  CA     . TYR   A 1  319 ? 17.952  -94.343  -73.378  1.00 43.63  ? 319 TYR   A CA     1 
ATOM   2472  C  C      . TYR   A 1  319 ? 18.191  -95.445  -72.353  1.00 46.69  ? 319 TYR   A C      1 
ATOM   2473  O  O      . TYR   A 1  319 ? 19.260  -96.060  -72.293  1.00 47.02  ? 319 TYR   A O      1 
ATOM   2474  C  CB     . TYR   A 1  319 ? 17.312  -94.978  -74.609  1.00 47.08  ? 319 TYR   A CB     1 
ATOM   2475  C  CG     . TYR   A 1  319 ? 16.916  -94.003  -75.653  1.00 40.03  ? 319 TYR   A CG     1 
ATOM   2476  C  CD1    . TYR   A 1  319 ? 17.867  -93.500  -76.530  1.00 40.35  ? 319 TYR   A CD1    1 
ATOM   2477  C  CD2    . TYR   A 1  319 ? 15.601  -93.577  -75.770  1.00 37.72  ? 319 TYR   A CD2    1 
ATOM   2478  C  CE1    . TYR   A 1  319 ? 17.530  -92.588  -77.507  1.00 39.75  ? 319 TYR   A CE1    1 
ATOM   2479  C  CE2    . TYR   A 1  319 ? 15.242  -92.661  -76.746  1.00 42.71  ? 319 TYR   A CE2    1 
ATOM   2480  C  CZ     . TYR   A 1  319 ? 16.223  -92.180  -77.616  1.00 41.76  ? 319 TYR   A CZ     1 
ATOM   2481  O  OH     . TYR   A 1  319 ? 15.917  -91.283  -78.598  1.00 44.93  ? 319 TYR   A OH     1 
ATOM   2482  N  N      . ARG   A 1  320 ? 17.162  -95.698  -71.553  1.00 48.85  ? 320 ARG   A N      1 
ATOM   2483  C  CA     . ARG   A 1  320 ? 17.142  -96.810  -70.616  1.00 52.48  ? 320 ARG   A CA     1 
ATOM   2484  C  C      . ARG   A 1  320 ? 15.795  -97.492  -70.753  1.00 53.07  ? 320 ARG   A C      1 
ATOM   2485  O  O      . ARG   A 1  320 ? 14.753  -96.853  -70.556  1.00 49.81  ? 320 ARG   A O      1 
ATOM   2486  C  CB     . ARG   A 1  320 ? 17.360  -96.354  -69.169  1.00 52.23  ? 320 ARG   A CB     1 
ATOM   2487  C  CG     . ARG   A 1  320 ? 18.745  -95.857  -68.876  1.00 50.72  ? 320 ARG   A CG     1 
ATOM   2488  C  CD     . ARG   A 1  320 ? 18.808  -95.345  -67.463  1.00 50.73  ? 320 ARG   A CD     1 
ATOM   2489  N  NE     . ARG   A 1  320 ? 19.338  -96.374  -66.586  1.00 59.00  ? 320 ARG   A NE     1 
ATOM   2490  C  CZ     . ARG   A 1  320 ? 19.878  -96.134  -65.401  1.00 61.77  ? 320 ARG   A CZ     1 
ATOM   2491  N  NH1    . ARG   A 1  320 ? 19.881  -94.917  -64.876  1.00 59.66  ? 320 ARG   A NH1    1 
ATOM   2492  N  NH2    . ARG   A 1  320 ? 20.444  -97.135  -64.733  1.00 61.22  ? 320 ARG   A NH2    1 
ATOM   2493  N  N      . GLY   A 1  321 ? 15.824  -98.782  -71.091  1.00 54.71  ? 321 GLY   A N      1 
ATOM   2494  C  CA     . GLY   A 1  321 ? 14.620  -99.572  -71.249  1.00 49.93  ? 321 GLY   A CA     1 
ATOM   2495  C  C      . GLY   A 1  321 ? 14.392  -100.114 -72.642  1.00 49.85  ? 321 GLY   A C      1 
ATOM   2496  O  O      . GLY   A 1  321 ? 15.318  -100.279 -73.455  1.00 47.32  ? 321 GLY   A O      1 
ATOM   2497  N  N      . ASP   A 1  322 ? 13.122  -100.375 -72.920  1.00 51.71  ? 322 ASP   A N      1 
ATOM   2498  C  CA     . ASP   A 1  322 ? 12.701  -101.028 -74.155  1.00 52.29  ? 322 ASP   A CA     1 
ATOM   2499  C  C      . ASP   A 1  322 ? 12.826  -100.031 -75.310  1.00 44.53  ? 322 ASP   A C      1 
ATOM   2500  O  O      . ASP   A 1  322 ? 11.881  -99.338  -75.694  1.00 55.31  ? 322 ASP   A O      1 
ATOM   2501  C  CB     . ASP   A 1  322 ? 11.278  -101.553 -73.962  1.00 55.78  ? 322 ASP   A CB     1 
ATOM   2502  C  CG     . ASP   A 1  322 ? 10.708  -102.229 -75.182  1.00 56.91  ? 322 ASP   A CG     1 
ATOM   2503  O  OD1    . ASP   A 1  322 ? 11.345  -103.145 -75.728  1.00 58.14  ? 322 ASP   A OD1    1 
ATOM   2504  O  OD2    . ASP   A 1  322 ? 9.598   -101.830 -75.592  1.00 59.21  ? 322 ASP   A OD2    1 
ATOM   2505  N  N      . VAL   A 1  323 ? 14.027  -99.959  -75.871  1.00 42.85  ? 323 VAL   A N      1 
ATOM   2506  C  CA     . VAL   A 1  323 ? 14.325  -99.068  -76.985  1.00 46.72  ? 323 VAL   A CA     1 
ATOM   2507  C  C      . VAL   A 1  323 ? 15.235  -99.809  -77.957  1.00 43.94  ? 323 VAL   A C      1 
ATOM   2508  O  O      . VAL   A 1  323 ? 16.175  -100.493 -77.535  1.00 43.95  ? 323 VAL   A O      1 
ATOM   2509  C  CB     . VAL   A 1  323 ? 14.988  -97.761  -76.487  1.00 46.10  ? 323 VAL   A CB     1 
ATOM   2510  C  CG1    . VAL   A 1  323 ? 15.757  -97.054  -77.629  1.00 37.89  ? 323 VAL   A CG1    1 
ATOM   2511  C  CG2    . VAL   A 1  323 ? 13.961  -96.830  -75.855  1.00 50.05  ? 323 VAL   A CG2    1 
ATOM   2512  N  N      . VAL   A 1  324 ? 14.952  -99.671  -79.256  1.00 49.38  ? 324 VAL   A N      1 
ATOM   2513  C  CA     . VAL   A 1  324 ? 15.767  -100.257 -80.331  1.00 50.93  ? 324 VAL   A CA     1 
ATOM   2514  C  C      . VAL   A 1  324 ? 16.210  -99.145  -81.267  1.00 46.55  ? 324 VAL   A C      1 
ATOM   2515  O  O      . VAL   A 1  324 ? 15.446  -98.198  -81.493  1.00 47.26  ? 324 VAL   A O      1 
ATOM   2516  C  CB     . VAL   A 1  324 ? 15.010  -101.329 -81.139  1.00 46.94  ? 324 VAL   A CB     1 
ATOM   2517  C  CG1    . VAL   A 1  324 ? 15.066  -102.668 -80.434  1.00 47.46  ? 324 VAL   A CG1    1 
ATOM   2518  C  CG2    . VAL   A 1  324 ? 13.579  -100.894 -81.365  1.00 42.52  ? 324 VAL   A CG2    1 
ATOM   2519  N  N      . PRO   A 1  325 ? 17.404  -99.247  -81.858  1.00 45.82  ? 325 PRO   A N      1 
ATOM   2520  C  CA     . PRO   A 1  325 ? 17.870  -98.216  -82.812  1.00 44.74  ? 325 PRO   A CA     1 
ATOM   2521  C  C      . PRO   A 1  325 ? 16.845  -97.757  -83.842  1.00 53.30  ? 325 PRO   A C      1 
ATOM   2522  O  O      . PRO   A 1  325 ? 16.746  -96.546  -84.089  1.00 55.73  ? 325 PRO   A O      1 
ATOM   2523  C  CB     . PRO   A 1  325 ? 19.068  -98.897  -83.485  1.00 39.72  ? 325 PRO   A CB     1 
ATOM   2524  C  CG     . PRO   A 1  325 ? 19.635  -99.787  -82.414  1.00 47.19  ? 325 PRO   A CG     1 
ATOM   2525  C  CD     . PRO   A 1  325 ? 18.439  -100.256 -81.573  1.00 47.52  ? 325 PRO   A CD     1 
ATOM   2526  N  N      . LYS   A 1  326 ? 16.088  -98.675  -84.455  1.00 50.85  ? 326 LYS   A N      1 
ATOM   2527  C  CA     . LYS   A 1  326 ? 15.178  -98.295  -85.533  1.00 52.55  ? 326 LYS   A CA     1 
ATOM   2528  C  C      . LYS   A 1  326 ? 14.142  -97.280  -85.047  1.00 57.82  ? 326 LYS   A C      1 
ATOM   2529  O  O      . LYS   A 1  326 ? 13.912  -96.243  -85.691  1.00 53.09  ? 326 LYS   A O      1 
ATOM   2530  C  CB     . LYS   A 1  326 ? 14.497  -99.548  -86.097  1.00 56.68  ? 326 LYS   A CB     1 
ATOM   2531  C  CG     . LYS   A 1  326 ? 13.761  -99.336  -87.422  1.00 58.50  ? 326 LYS   A CG     1 
ATOM   2532  C  CD     . LYS   A 1  326 ? 12.716  -100.432 -87.689  1.00 64.75  ? 326 LYS   A CD     1 
ATOM   2533  C  CE     . LYS   A 1  326 ? 12.046  -100.921 -86.403  1.00 68.14  ? 326 LYS   A CE     1 
ATOM   2534  N  NZ     . LYS   A 1  326 ? 11.104  -102.077 -86.619  1.00 59.60  ? 326 LYS   A NZ     1 
ATOM   2535  N  N      . ASP   A 1  327 ? 13.500  -97.568  -83.907  1.00 51.62  ? 327 ASP   A N      1 
ATOM   2536  C  CA     . ASP   A 1  327 ? 12.536  -96.632  -83.337  1.00 47.92  ? 327 ASP   A CA     1 
ATOM   2537  C  C      . ASP   A 1  327 ? 13.159  -95.257  -83.088  1.00 53.92  ? 327 ASP   A C      1 
ATOM   2538  O  O      . ASP   A 1  327 ? 12.500  -94.224  -83.287  1.00 56.23  ? 327 ASP   A O      1 
ATOM   2539  C  CB     . ASP   A 1  327 ? 11.970  -97.188  -82.037  1.00 49.91  ? 327 ASP   A CB     1 
ATOM   2540  C  CG     . ASP   A 1  327 ? 11.249  -98.505  -82.219  1.00 58.23  ? 327 ASP   A CG     1 
ATOM   2541  O  OD1    . ASP   A 1  327 ? 10.783  -98.764  -83.348  1.00 66.97  ? 327 ASP   A OD1    1 
ATOM   2542  O  OD2    . ASP   A 1  327 ? 11.150  -99.278  -81.226  1.00 55.36  ? 327 ASP   A OD2    1 
ATOM   2543  N  N      . VAL   A 1  328 ? 14.424  -95.225  -82.644  1.00 51.69  ? 328 VAL   A N      1 
ATOM   2544  C  CA     . VAL   A 1  328 ? 15.111  -93.957  -82.382  1.00 51.73  ? 328 VAL   A CA     1 
ATOM   2545  C  C      . VAL   A 1  328 ? 15.262  -93.147  -83.671  1.00 52.33  ? 328 VAL   A C      1 
ATOM   2546  O  O      . VAL   A 1  328 ? 14.940  -91.954  -83.719  1.00 52.37  ? 328 VAL   A O      1 
ATOM   2547  C  CB     . VAL   A 1  328 ? 16.476  -94.209  -81.708  1.00 51.04  ? 328 VAL   A CB     1 
ATOM   2548  C  CG1    . VAL   A 1  328 ? 17.259  -92.892  -81.568  1.00 49.47  ? 328 VAL   A CG1    1 
ATOM   2549  C  CG2    . VAL   A 1  328 ? 16.315  -94.916  -80.339  1.00 39.25  ? 328 VAL   A CG2    1 
ATOM   2550  N  N      . ASN   A 1  329 ? 15.738  -93.786  -84.739  1.00 51.59  ? 329 ASN   A N      1 
ATOM   2551  C  CA     . ASN   A 1  329 ? 15.985  -93.054  -85.977  1.00 57.26  ? 329 ASN   A CA     1 
ATOM   2552  C  C      . ASN   A 1  329 ? 14.693  -92.593  -86.638  1.00 58.01  ? 329 ASN   A C      1 
ATOM   2553  O  O      . ASN   A 1  329 ? 14.665  -91.534  -87.283  1.00 52.26  ? 329 ASN   A O      1 
ATOM   2554  C  CB     . ASN   A 1  329 ? 16.784  -93.920  -86.942  1.00 62.10  ? 329 ASN   A CB     1 
ATOM   2555  C  CG     . ASN   A 1  329 ? 18.149  -94.281  -86.390  1.00 66.28  ? 329 ASN   A CG     1 
ATOM   2556  O  OD1    . ASN   A 1  329 ? 18.722  -93.554  -85.556  1.00 67.21  ? 329 ASN   A OD1    1 
ATOM   2557  N  ND2    . ASN   A 1  329 ? 18.690  -95.405  -86.862  1.00 63.52  ? 329 ASN   A ND2    1 
ATOM   2558  N  N      . ALA   A 1  330 ? 13.622  -93.373  -86.505  1.00 54.87  ? 330 ALA   A N      1 
ATOM   2559  C  CA     . ALA   A 1  330 ? 12.331  -92.899  -86.983  1.00 56.70  ? 330 ALA   A CA     1 
ATOM   2560  C  C      . ALA   A 1  330 ? 11.869  -91.693  -86.181  1.00 58.45  ? 330 ALA   A C      1 
ATOM   2561  O  O      . ALA   A 1  330 ? 11.304  -90.749  -86.744  1.00 56.36  ? 330 ALA   A O      1 
ATOM   2562  C  CB     . ALA   A 1  330 ? 11.297  -94.020  -86.923  1.00 48.84  ? 330 ALA   A CB     1 
ATOM   2563  N  N      . ALA   A 1  331 ? 12.100  -91.709  -84.860  1.00 57.38  ? 331 ALA   A N      1 
ATOM   2564  C  CA     . ALA   A 1  331 ? 11.699  -90.578  -84.031  1.00 58.71  ? 331 ALA   A CA     1 
ATOM   2565  C  C      . ALA   A 1  331 ? 12.598  -89.378  -84.280  1.00 61.52  ? 331 ALA   A C      1 
ATOM   2566  O  O      . ALA   A 1  331 ? 12.125  -88.238  -84.276  1.00 62.30  ? 331 ALA   A O      1 
ATOM   2567  C  CB     . ALA   A 1  331 ? 11.699  -90.965  -82.548  1.00 52.80  ? 331 ALA   A CB     1 
ATOM   2568  N  N      . ILE   A 1  332 ? 13.895  -89.612  -84.507  1.00 58.86  ? 332 ILE   A N      1 
ATOM   2569  C  CA     . ILE   A 1  332 ? 14.801  -88.525  -84.880  1.00 55.71  ? 332 ILE   A CA     1 
ATOM   2570  C  C      . ILE   A 1  332 ? 14.386  -87.910  -86.213  1.00 63.96  ? 332 ILE   A C      1 
ATOM   2571  O  O      . ILE   A 1  332 ? 14.345  -86.684  -86.362  1.00 63.57  ? 332 ILE   A O      1 
ATOM   2572  C  CB     . ILE   A 1  332 ? 16.248  -89.031  -84.944  1.00 55.26  ? 332 ILE   A CB     1 
ATOM   2573  C  CG1    . ILE   A 1  332 ? 16.799  -89.264  -83.546  1.00 56.97  ? 332 ILE   A CG1    1 
ATOM   2574  C  CG2    . ILE   A 1  332 ? 17.113  -88.037  -85.717  1.00 60.61  ? 332 ILE   A CG2    1 
ATOM   2575  C  CD1    . ILE   A 1  332 ? 18.261  -89.676  -83.550  1.00 56.07  ? 332 ILE   A CD1    1 
ATOM   2576  N  N      . ALA   A 1  333 ? 14.105  -88.757  -87.211  1.00 66.99  ? 333 ALA   A N      1 
ATOM   2577  C  CA     . ALA   A 1  333 ? 13.714  -88.265  -88.532  1.00 65.63  ? 333 ALA   A CA     1 
ATOM   2578  C  C      . ALA   A 1  333 ? 12.417  -87.470  -88.464  1.00 62.87  ? 333 ALA   A C      1 
ATOM   2579  O  O      . ALA   A 1  333 ? 12.318  -86.371  -89.019  1.00 68.82  ? 333 ALA   A O      1 
ATOM   2580  C  CB     . ALA   A 1  333 ? 13.567  -89.438  -89.502  1.00 64.48  ? 333 ALA   A CB     1 
ATOM   2581  N  N      . THR   A 1  334 ? 11.400  -88.032  -87.810  1.00 63.93  ? 334 THR   A N      1 
ATOM   2582  C  CA     . THR   A 1  334 ? 10.144  -87.320  -87.581  1.00 62.26  ? 334 THR   A CA     1 
ATOM   2583  C  C      . THR   A 1  334 ? 10.359  -86.000  -86.849  1.00 64.89  ? 334 THR   A C      1 
ATOM   2584  O  O      . THR   A 1  334 ? 9.704   -84.998  -87.155  1.00 68.32  ? 334 THR   A O      1 
ATOM   2585  C  CB     . THR   A 1  334 ? 9.180   -88.224  -86.800  1.00 62.41  ? 334 THR   A CB     1 
ATOM   2586  O  OG1    . THR   A 1  334 ? 7.862   -87.674  -86.815  1.00 58.12  ? 334 THR   A OG1    1 
ATOM   2587  C  CG2    . THR   A 1  334 ? 9.633   -88.435  -85.349  1.00 68.91  ? 334 THR   A CG2    1 
ATOM   2588  N  N      . ILE   A 1  335 ? 11.263  -85.978  -85.874  1.00 66.73  ? 335 ILE   A N      1 
ATOM   2589  C  CA     . ILE   A 1  335 ? 11.478  -84.764  -85.096  1.00 71.36  ? 335 ILE   A CA     1 
ATOM   2590  C  C      . ILE   A 1  335 ? 12.291  -83.744  -85.887  1.00 75.25  ? 335 ILE   A C      1 
ATOM   2591  O  O      . ILE   A 1  335 ? 12.040  -82.536  -85.789  1.00 77.70  ? 335 ILE   A O      1 
ATOM   2592  C  CB     . ILE   A 1  335 ? 12.138  -85.110  -83.744  1.00 66.02  ? 335 ILE   A CB     1 
ATOM   2593  C  CG1    . ILE   A 1  335 ? 11.084  -85.155  -82.636  1.00 60.74  ? 335 ILE   A CG1    1 
ATOM   2594  C  CG2    . ILE   A 1  335 ? 13.218  -84.118  -83.401  1.00 61.08  ? 335 ILE   A CG2    1 
ATOM   2595  C  CD1    . ILE   A 1  335 ? 11.426  -86.112  -81.530  1.00 56.97  ? 335 ILE   A CD1    1 
ATOM   2596  N  N      . LYS   A 1  336 ? 13.267  -84.199  -86.682  1.00 68.49  ? 336 LYS   A N      1 
ATOM   2597  C  CA     . LYS   A 1  336 ? 14.133  -83.252  -87.382  1.00 72.22  ? 336 LYS   A CA     1 
ATOM   2598  C  C      . LYS   A 1  336 ? 13.306  -82.266  -88.191  1.00 79.75  ? 336 LYS   A C      1 
ATOM   2599  O  O      . LYS   A 1  336 ? 13.546  -81.051  -88.158  1.00 82.81  ? 336 LYS   A O      1 
ATOM   2600  C  CB     . LYS   A 1  336 ? 15.119  -83.981  -88.291  1.00 76.13  ? 336 LYS   A CB     1 
ATOM   2601  C  CG     . LYS   A 1  336 ? 16.024  -83.041  -89.077  1.00 79.18  ? 336 LYS   A CG     1 
ATOM   2602  C  CD     . LYS   A 1  336 ? 16.805  -82.120  -88.139  1.00 77.29  ? 336 LYS   A CD     1 
ATOM   2603  C  CE     . LYS   A 1  336 ? 17.029  -80.736  -88.749  1.00 77.21  ? 336 LYS   A CE     1 
ATOM   2604  N  NZ     . LYS   A 1  336 ? 18.378  -80.629  -89.382  1.00 79.72  ? 336 LYS   A NZ     1 
ATOM   2605  N  N      . THR   A 1  337 ? 12.306  -82.773  -88.909  1.00 76.70  ? 337 THR   A N      1 
ATOM   2606  C  CA     . THR   A 1  337 ? 11.459  -81.893  -89.703  1.00 81.60  ? 337 THR   A CA     1 
ATOM   2607  C  C      . THR   A 1  337 ? 10.797  -80.825  -88.830  1.00 81.99  ? 337 THR   A C      1 
ATOM   2608  O  O      . THR   A 1  337 ? 10.961  -79.624  -89.075  1.00 90.58  ? 337 THR   A O      1 
ATOM   2609  C  CB     . THR   A 1  337 ? 10.412  -82.717  -90.454  1.00 76.57  ? 337 THR   A CB     1 
ATOM   2610  O  OG1    . THR   A 1  337 ? 9.387   -83.135  -89.543  1.00 78.85  ? 337 THR   A OG1    1 
ATOM   2611  C  CG2    . THR   A 1  337 ? 11.058  -83.944  -91.082  1.00 64.33  ? 337 THR   A CG2    1 
ATOM   2612  N  N      . LYS   A 1  338 ? 10.086  -81.243  -87.776  1.00 78.04  ? 338 LYS   A N      1 
ATOM   2613  C  CA     . LYS   A 1  338 ? 9.206   -80.344  -87.030  1.00 76.66  ? 338 LYS   A CA     1 
ATOM   2614  C  C      . LYS   A 1  338 ? 9.926   -79.393  -86.065  1.00 81.32  ? 338 LYS   A C      1 
ATOM   2615  O  O      . LYS   A 1  338 ? 9.318   -78.400  -85.653  1.00 82.47  ? 338 LYS   A O      1 
ATOM   2616  C  CB     . LYS   A 1  338 ? 8.177   -81.161  -86.242  1.00 73.33  ? 338 LYS   A CB     1 
ATOM   2617  C  CG     . LYS   A 1  338 ? 7.570   -82.330  -87.007  1.00 76.00  ? 338 LYS   A CG     1 
ATOM   2618  C  CD     . LYS   A 1  338 ? 6.119   -82.049  -87.354  1.00 81.04  ? 338 LYS   A CD     1 
ATOM   2619  C  CE     . LYS   A 1  338 ? 5.208   -83.202  -86.974  1.00 75.13  ? 338 LYS   A CE     1 
ATOM   2620  N  NZ     . LYS   A 1  338 ? 3.851   -83.002  -87.548  1.00 77.34  ? 338 LYS   A NZ     1 
ATOM   2621  N  N      . ARG   A 1  339 ? 11.176  -79.657  -85.676  1.00 82.87  ? 339 ARG   A N      1 
ATOM   2622  C  CA     . ARG   A 1  339 ? 11.851  -78.864  -84.650  1.00 78.59  ? 339 ARG   A CA     1 
ATOM   2623  C  C      . ARG   A 1  339 ? 12.968  -78.010  -85.243  1.00 80.17  ? 339 ARG   A C      1 
ATOM   2624  O  O      . ARG   A 1  339 ? 13.487  -78.272  -86.336  1.00 79.70  ? 339 ARG   A O      1 
ATOM   2625  C  CB     . ARG   A 1  339 ? 12.447  -79.741  -83.537  1.00 70.06  ? 339 ARG   A CB     1 
ATOM   2626  C  CG     . ARG   A 1  339 ? 11.456  -80.488  -82.678  1.00 61.86  ? 339 ARG   A CG     1 
ATOM   2627  C  CD     . ARG   A 1  339 ? 10.953  -79.682  -81.510  1.00 60.50  ? 339 ARG   A CD     1 
ATOM   2628  N  NE     . ARG   A 1  339 ? 10.143  -80.510  -80.618  1.00 63.30  ? 339 ARG   A NE     1 
ATOM   2629  C  CZ     . ARG   A 1  339 ? 9.304   -80.036  -79.700  1.00 68.38  ? 339 ARG   A CZ     1 
ATOM   2630  N  NH1    . ARG   A 1  339 ? 9.121   -78.732  -79.531  1.00 64.75  ? 339 ARG   A NH1    1 
ATOM   2631  N  NH2    . ARG   A 1  339 ? 8.634   -80.890  -78.930  1.00 60.76  ? 339 ARG   A NH2    1 
ATOM   2632  N  N      . SER   A 1  340 ? 13.349  -76.988  -84.472  1.00 77.71  ? 340 SER   A N      1 
ATOM   2633  C  CA     . SER   A 1  340 ? 14.299  -75.968  -84.914  1.00 76.98  ? 340 SER   A CA     1 
ATOM   2634  C  C      . SER   A 1  340 ? 15.650  -76.294  -84.291  1.00 71.53  ? 340 SER   A C      1 
ATOM   2635  O  O      . SER   A 1  340 ? 16.033  -75.758  -83.248  1.00 68.17  ? 340 SER   A O      1 
ATOM   2636  C  CB     . SER   A 1  340 ? 13.811  -74.579  -84.518  1.00 70.91  ? 340 SER   A CB     1 
ATOM   2637  O  OG     . SER   A 1  340 ? 12.404  -74.498  -84.674  1.00 62.07  ? 340 SER   A OG     1 
ATOM   2638  N  N      . ILE   A 1  341 ? 16.375  -77.193  -84.955  1.00 64.55  ? 341 ILE   A N      1 
ATOM   2639  C  CA     . ILE   A 1  341 ? 17.613  -77.764  -84.436  1.00 61.97  ? 341 ILE   A CA     1 
ATOM   2640  C  C      . ILE   A 1  341 ? 18.745  -77.330  -85.356  1.00 68.64  ? 341 ILE   A C      1 
ATOM   2641  O  O      . ILE   A 1  341 ? 18.942  -77.894  -86.440  1.00 77.49  ? 341 ILE   A O      1 
ATOM   2642  C  CB     . ILE   A 1  341 ? 17.546  -79.287  -84.321  1.00 62.64  ? 341 ILE   A CB     1 
ATOM   2643  C  CG1    . ILE   A 1  341 ? 16.587  -79.673  -83.200  1.00 61.84  ? 341 ILE   A CG1    1 
ATOM   2644  C  CG2    . ILE   A 1  341 ? 18.932  -79.849  -84.086  1.00 56.47  ? 341 ILE   A CG2    1 
ATOM   2645  C  CD1    . ILE   A 1  341 ? 15.778  -80.927  -83.473  1.00 67.89  ? 341 ILE   A CD1    1 
ATOM   2646  N  N      . GLN   A 1  342 ? 19.511  -76.345  -84.907  1.00 65.65  ? 342 GLN   A N      1 
ATOM   2647  C  CA     . GLN   A 1  342 ? 20.557  -75.715  -85.689  1.00 59.43  ? 342 GLN   A CA     1 
ATOM   2648  C  C      . GLN   A 1  342 ? 21.879  -75.967  -84.987  1.00 63.04  ? 342 GLN   A C      1 
ATOM   2649  O  O      . GLN   A 1  342 ? 22.049  -75.571  -83.829  1.00 62.70  ? 342 GLN   A O      1 
ATOM   2650  C  CB     . GLN   A 1  342 ? 20.284  -74.220  -85.806  1.00 64.79  ? 342 GLN   A CB     1 
ATOM   2651  C  CG     . GLN   A 1  342 ? 19.641  -73.811  -87.085  1.00 71.46  ? 342 GLN   A CG     1 
ATOM   2652  C  CD     . GLN   A 1  342 ? 20.670  -73.770  -88.184  1.00 84.80  ? 342 GLN   A CD     1 
ATOM   2653  O  OE1    . GLN   A 1  342 ? 21.759  -73.213  -87.996  1.00 87.65  ? 342 GLN   A OE1    1 
ATOM   2654  N  NE2    . GLN   A 1  342 ? 20.343  -74.353  -89.342  1.00 83.70  ? 342 GLN   A NE2    1 
ATOM   2655  N  N      . PHE   A 1  343 ? 22.798  -76.646  -85.665  1.00 62.40  ? 343 PHE   A N      1 
ATOM   2656  C  CA     . PHE   A 1  343 ? 24.139  -76.834  -85.135  1.00 56.29  ? 343 PHE   A CA     1 
ATOM   2657  C  C      . PHE   A 1  343 ? 25.061  -75.739  -85.634  1.00 60.38  ? 343 PHE   A C      1 
ATOM   2658  O  O      . PHE   A 1  343 ? 24.785  -75.054  -86.623  1.00 63.80  ? 343 PHE   A O      1 
ATOM   2659  C  CB     . PHE   A 1  343 ? 24.735  -78.181  -85.545  1.00 58.59  ? 343 PHE   A CB     1 
ATOM   2660  C  CG     . PHE   A 1  343 ? 24.320  -79.330  -84.681  1.00 57.42  ? 343 PHE   A CG     1 
ATOM   2661  C  CD1    . PHE   A 1  343 ? 22.982  -79.650  -84.525  1.00 54.18  ? 343 PHE   A CD1    1 
ATOM   2662  C  CD2    . PHE   A 1  343 ? 25.266  -80.125  -84.066  1.00 54.88  ? 343 PHE   A CD2    1 
ATOM   2663  C  CE1    . PHE   A 1  343 ? 22.603  -80.718  -83.745  1.00 48.39  ? 343 PHE   A CE1    1 
ATOM   2664  C  CE2    . PHE   A 1  343 ? 24.876  -81.207  -83.290  1.00 48.70  ? 343 PHE   A CE2    1 
ATOM   2665  C  CZ     . PHE   A 1  343 ? 23.550  -81.495  -83.137  1.00 46.72  ? 343 PHE   A CZ     1 
ATOM   2666  N  N      . VAL   A 1  344 ? 26.187  -75.593  -84.937  1.00 61.65  ? 344 VAL   A N      1 
ATOM   2667  C  CA     . VAL   A 1  344 ? 27.251  -74.753  -85.447  1.00 63.93  ? 344 VAL   A CA     1 
ATOM   2668  C  C      . VAL   A 1  344 ? 27.794  -75.379  -86.725  1.00 73.48  ? 344 VAL   A C      1 
ATOM   2669  O  O      . VAL   A 1  344 ? 27.769  -76.603  -86.908  1.00 73.66  ? 344 VAL   A O      1 
ATOM   2670  C  CB     . VAL   A 1  344 ? 28.358  -74.581  -84.398  1.00 65.85  ? 344 VAL   A CB     1 
ATOM   2671  C  CG1    . VAL   A 1  344 ? 27.791  -73.921  -83.145  1.00 57.71  ? 344 VAL   A CG1    1 
ATOM   2672  C  CG2    . VAL   A 1  344 ? 28.985  -75.940  -84.085  1.00 66.41  ? 344 VAL   A CG2    1 
ATOM   2673  N  N      . ASP   A 1  345 ? 28.308  -74.532  -87.615  1.00 76.23  ? 345 ASP   A N      1 
ATOM   2674  C  CA     . ASP   A 1  345 ? 28.688  -75.007  -88.939  1.00 72.84  ? 345 ASP   A CA     1 
ATOM   2675  C  C      . ASP   A 1  345 ? 29.895  -75.930  -88.892  1.00 76.22  ? 345 ASP   A C      1 
ATOM   2676  O  O      . ASP   A 1  345 ? 30.042  -76.802  -89.754  1.00 79.86  ? 345 ASP   A O      1 
ATOM   2677  C  CB     . ASP   A 1  345 ? 28.949  -73.813  -89.846  1.00 72.89  ? 345 ASP   A CB     1 
ATOM   2678  C  CG     . ASP   A 1  345 ? 27.667  -73.112  -90.245  1.00 77.74  ? 345 ASP   A CG     1 
ATOM   2679  O  OD1    . ASP   A 1  345 ? 26.639  -73.809  -90.434  1.00 82.25  ? 345 ASP   A OD1    1 
ATOM   2680  O  OD2    . ASP   A 1  345 ? 27.675  -71.865  -90.351  1.00 82.25  ? 345 ASP   A OD2    1 
ATOM   2681  N  N      . TRP   A 1  346 ? 30.764  -75.773  -87.907  1.00 69.41  ? 346 TRP   A N      1 
ATOM   2682  C  CA     . TRP   A 1  346 ? 31.900  -76.671  -87.796  1.00 70.86  ? 346 TRP   A CA     1 
ATOM   2683  C  C      . TRP   A 1  346 ? 31.565  -77.977  -87.083  1.00 76.23  ? 346 TRP   A C      1 
ATOM   2684  O  O      . TRP   A 1  346 ? 32.494  -78.745  -86.780  1.00 80.36  ? 346 TRP   A O      1 
ATOM   2685  C  CB     . TRP   A 1  346 ? 33.050  -75.945  -87.113  1.00 65.69  ? 346 TRP   A CB     1 
ATOM   2686  C  CG     . TRP   A 1  346 ? 33.112  -76.006  -85.620  1.00 80.98  ? 346 TRP   A CG     1 
ATOM   2687  C  CD1    . TRP   A 1  346 ? 33.642  -76.992  -84.821  1.00 85.18  ? 346 TRP   A CD1    1 
ATOM   2688  C  CD2    . TRP   A 1  346 ? 32.598  -75.000  -84.735  1.00 76.96  ? 346 TRP   A CD2    1 
ATOM   2689  N  NE1    . TRP   A 1  346 ? 33.495  -76.634  -83.475  1.00 77.10  ? 346 TRP   A NE1    1 
ATOM   2690  C  CE2    . TRP   A 1  346 ? 32.876  -75.414  -83.405  1.00 79.29  ? 346 TRP   A CE2    1 
ATOM   2691  C  CE3    . TRP   A 1  346 ? 31.954  -73.774  -84.944  1.00 71.62  ? 346 TRP   A CE3    1 
ATOM   2692  C  CZ2    . TRP   A 1  346 ? 32.539  -74.644  -82.284  1.00 83.42  ? 346 TRP   A CZ2    1 
ATOM   2693  C  CZ3    . TRP   A 1  346 ? 31.617  -72.995  -83.824  1.00 78.23  ? 346 TRP   A CZ3    1 
ATOM   2694  C  CH2    . TRP   A 1  346 ? 31.914  -73.446  -82.503  1.00 83.43  ? 346 TRP   A CH2    1 
ATOM   2695  N  N      . CYS   A 1  347 ? 30.280  -78.256  -86.805  1.00 73.15  ? 347 CYS   A N      1 
ATOM   2696  C  CA     . CYS   A 1  347 ? 29.931  -79.515  -86.171  1.00 70.35  ? 347 CYS   A CA     1 
ATOM   2697  C  C      . CYS   A 1  347 ? 28.912  -80.246  -87.026  1.00 69.53  ? 347 CYS   A C      1 
ATOM   2698  O  O      . CYS   A 1  347 ? 28.015  -79.614  -87.594  1.00 70.56  ? 347 CYS   A O      1 
ATOM   2699  C  CB     . CYS   A 1  347 ? 29.361  -79.308  -84.762  1.00 69.41  ? 347 CYS   A CB     1 
ATOM   2700  S  SG     . CYS   A 1  347 ? 30.594  -78.711  -83.548  1.00 81.80  ? 347 CYS   A SG     1 
ATOM   2701  N  N      . PRO   A 1  348 ? 29.029  -81.561  -87.142  1.00 68.68  ? 348 PRO   A N      1 
ATOM   2702  C  CA     . PRO   A 1  348 ? 28.001  -82.322  -87.853  1.00 68.72  ? 348 PRO   A CA     1 
ATOM   2703  C  C      . PRO   A 1  348 ? 26.686  -82.271  -87.099  1.00 64.88  ? 348 PRO   A C      1 
ATOM   2704  O  O      . PRO   A 1  348 ? 26.640  -82.499  -85.891  1.00 62.71  ? 348 PRO   A O      1 
ATOM   2705  C  CB     . PRO   A 1  348 ? 28.577  -83.742  -87.901  1.00 66.17  ? 348 PRO   A CB     1 
ATOM   2706  C  CG     . PRO   A 1  348 ? 29.630  -83.773  -86.848  1.00 66.42  ? 348 PRO   A CG     1 
ATOM   2707  C  CD     . PRO   A 1  348 ? 30.188  -82.388  -86.779  1.00 65.92  ? 348 PRO   A CD     1 
ATOM   2708  N  N      . THR   A 1  349 ? 25.618  -81.931  -87.815  1.00 63.01  ? 349 THR   A N      1 
ATOM   2709  C  CA     . THR   A 1  349 ? 24.282  -82.163  -87.288  1.00 61.37  ? 349 THR   A CA     1 
ATOM   2710  C  C      . THR   A 1  349 ? 24.087  -83.659  -87.111  1.00 67.45  ? 349 THR   A C      1 
ATOM   2711  O  O      . THR   A 1  349 ? 24.077  -84.399  -88.096  1.00 67.39  ? 349 THR   A O      1 
ATOM   2712  C  CB     . THR   A 1  349 ? 23.220  -81.612  -88.242  1.00 70.20  ? 349 THR   A CB     1 
ATOM   2713  O  OG1    . THR   A 1  349 ? 23.470  -80.222  -88.509  1.00 72.74  ? 349 THR   A OG1    1 
ATOM   2714  C  CG2    . THR   A 1  349 ? 21.818  -81.794  -87.653  1.00 63.13  ? 349 THR   A CG2    1 
ATOM   2715  N  N      . GLY   A 1  350 ? 23.956  -84.115  -85.862  1.00 68.09  ? 350 GLY   A N      1 
ATOM   2716  C  CA     . GLY   A 1  350 ? 23.724  -85.527  -85.610  1.00 63.35  ? 350 GLY   A CA     1 
ATOM   2717  C  C      . GLY   A 1  350 ? 23.869  -85.936  -84.160  1.00 64.09  ? 350 GLY   A C      1 
ATOM   2718  O  O      . GLY   A 1  350 ? 24.517  -85.240  -83.371  1.00 66.91  ? 350 GLY   A O      1 
ATOM   2719  N  N      . PHE   A 1  351 ? 23.308  -87.091  -83.811  1.00 58.99  ? 351 PHE   A N      1 
ATOM   2720  C  CA     . PHE   A 1  351 ? 23.199  -87.538  -82.434  1.00 52.56  ? 351 PHE   A CA     1 
ATOM   2721  C  C      . PHE   A 1  351 ? 24.084  -88.749  -82.172  1.00 56.79  ? 351 PHE   A C      1 
ATOM   2722  O  O      . PHE   A 1  351 ? 24.146  -89.670  -82.985  1.00 63.68  ? 351 PHE   A O      1 
ATOM   2723  C  CB     . PHE   A 1  351 ? 21.747  -87.886  -82.123  1.00 55.31  ? 351 PHE   A CB     1 
ATOM   2724  C  CG     . PHE   A 1  351 ? 20.799  -86.781  -82.432  1.00 64.72  ? 351 PHE   A CG     1 
ATOM   2725  C  CD1    . PHE   A 1  351 ? 20.497  -86.458  -83.745  1.00 62.51  ? 351 PHE   A CD1    1 
ATOM   2726  C  CD2    . PHE   A 1  351 ? 20.232  -86.031  -81.411  1.00 61.65  ? 351 PHE   A CD2    1 
ATOM   2727  C  CE1    . PHE   A 1  351 ? 19.641  -85.422  -84.032  1.00 56.79  ? 351 PHE   A CE1    1 
ATOM   2728  C  CE2    . PHE   A 1  351 ? 19.372  -84.987  -81.700  1.00 51.45  ? 351 PHE   A CE2    1 
ATOM   2729  C  CZ     . PHE   A 1  351 ? 19.085  -84.682  -83.006  1.00 52.89  ? 351 PHE   A CZ     1 
ATOM   2730  N  N      . LYS   A 1  352 ? 24.756  -88.764  -81.028  1.00 55.27  ? 352 LYS   A N      1 
ATOM   2731  C  CA     . LYS   A 1  352 ? 25.351  -89.992  -80.518  1.00 50.56  ? 352 LYS   A CA     1 
ATOM   2732  C  C      . LYS   A 1  352 ? 24.336  -90.640  -79.595  1.00 51.57  ? 352 LYS   A C      1 
ATOM   2733  O  O      . LYS   A 1  352 ? 23.952  -90.049  -78.583  1.00 54.48  ? 352 LYS   A O      1 
ATOM   2734  C  CB     . LYS   A 1  352 ? 26.658  -89.721  -79.780  1.00 46.75  ? 352 LYS   A CB     1 
ATOM   2735  C  CG     . LYS   A 1  352 ? 27.713  -89.150  -80.668  1.00 53.31  ? 352 LYS   A CG     1 
ATOM   2736  C  CD     . LYS   A 1  352 ? 29.107  -89.432  -80.188  1.00 48.21  ? 352 LYS   A CD     1 
ATOM   2737  C  CE     . LYS   A 1  352 ? 30.056  -88.575  -80.992  1.00 44.96  ? 352 LYS   A CE     1 
ATOM   2738  N  NZ     . LYS   A 1  352 ? 31.450  -89.053  -80.883  1.00 56.59  ? 352 LYS   A NZ     1 
ATOM   2739  N  N      . VAL   A 1  353 ? 23.892  -91.838  -79.945  1.00 54.87  ? 353 VAL   A N      1 
ATOM   2740  C  CA     . VAL   A 1  353 ? 22.841  -92.528  -79.202  1.00 51.20  ? 353 VAL   A CA     1 
ATOM   2741  C  C      . VAL   A 1  353 ? 23.450  -93.614  -78.329  1.00 50.84  ? 353 VAL   A C      1 
ATOM   2742  O  O      . VAL   A 1  353 ? 24.407  -94.295  -78.720  1.00 47.77  ? 353 VAL   A O      1 
ATOM   2743  C  CB     . VAL   A 1  353 ? 21.781  -93.123  -80.146  1.00 51.84  ? 353 VAL   A CB     1 
ATOM   2744  C  CG1    . VAL   A 1  353 ? 20.575  -93.634  -79.338  1.00 45.64  ? 353 VAL   A CG1    1 
ATOM   2745  C  CG2    . VAL   A 1  353 ? 21.379  -92.093  -81.199  1.00 50.56  ? 353 VAL   A CG2    1 
ATOM   2746  N  N      . GLY   A 1  354 ? 22.887  -93.774  -77.139  1.00 47.77  ? 354 GLY   A N      1 
ATOM   2747  C  CA     . GLY   A 1  354 ? 23.282  -94.848  -76.272  1.00 41.67  ? 354 GLY   A CA     1 
ATOM   2748  C  C      . GLY   A 1  354 ? 22.044  -95.451  -75.664  1.00 46.79  ? 354 GLY   A C      1 
ATOM   2749  O  O      . GLY   A 1  354 ? 21.164  -94.709  -75.201  1.00 44.88  ? 354 GLY   A O      1 
ATOM   2750  N  N      . ILE   A 1  355 ? 21.959  -96.787  -75.657  1.00 45.35  ? 355 ILE   A N      1 
ATOM   2751  C  CA     . ILE   A 1  355 ? 20.784  -97.490  -75.159  1.00 45.90  ? 355 ILE   A CA     1 
ATOM   2752  C  C      . ILE   A 1  355 ? 21.234  -98.521  -74.155  1.00 44.05  ? 355 ILE   A C      1 
ATOM   2753  O  O      . ILE   A 1  355 ? 22.114  -99.329  -74.452  1.00 51.36  ? 355 ILE   A O      1 
ATOM   2754  C  CB     . ILE   A 1  355 ? 19.992  -98.182  -76.281  1.00 45.77  ? 355 ILE   A CB     1 
ATOM   2755  C  CG1    . ILE   A 1  355 ? 19.454  -97.158  -77.273  1.00 46.04  ? 355 ILE   A CG1    1 
ATOM   2756  C  CG2    . ILE   A 1  355 ? 18.855  -99.004  -75.692  1.00 40.82  ? 355 ILE   A CG2    1 
ATOM   2757  C  CD1    . ILE   A 1  355 ? 18.654  -97.788  -78.395  1.00 46.43  ? 355 ILE   A CD1    1 
ATOM   2758  N  N      . ASN   A 1  356 ? 20.620  -98.509  -72.984  1.00 46.93  ? 356 ASN   A N      1 
ATOM   2759  C  CA     . ASN   A 1  356 ? 20.766  -99.574  -72.009  1.00 48.29  ? 356 ASN   A CA     1 
ATOM   2760  C  C      . ASN   A 1  356 ? 19.408  -100.217 -71.792  1.00 52.76  ? 356 ASN   A C      1 
ATOM   2761  O  O      . ASN   A 1  356 ? 18.429  -99.524  -71.501  1.00 50.50  ? 356 ASN   A O      1 
ATOM   2762  C  CB     . ASN   A 1  356 ? 21.322  -99.054  -70.684  1.00 51.42  ? 356 ASN   A CB     1 
ATOM   2763  C  CG     . ASN   A 1  356 ? 21.976  -100.149 -69.872  1.00 62.67  ? 356 ASN   A CG     1 
ATOM   2764  O  OD1    . ASN   A 1  356 ? 21.303  -100.926 -69.168  1.00 62.40  ? 356 ASN   A OD1    1 
ATOM   2765  N  ND2    . ASN   A 1  356 ? 23.292  -100.256 -70.004  1.00 62.59  ? 356 ASN   A ND2    1 
ATOM   2766  N  N      . TYR   A 1  357 ? 19.356  -101.541 -71.935  1.00 58.41  ? 357 TYR   A N      1 
ATOM   2767  C  CA     . TYR   A 1  357 ? 18.082  -102.250 -71.886  1.00 58.05  ? 357 TYR   A CA     1 
ATOM   2768  C  C      . TYR   A 1  357 ? 17.467  -102.301 -70.488  1.00 57.49  ? 357 TYR   A C      1 
ATOM   2769  O  O      . TYR   A 1  357 ? 16.254  -102.512 -70.390  1.00 55.67  ? 357 TYR   A O      1 
ATOM   2770  C  CB     . TYR   A 1  357 ? 18.247  -103.678 -72.415  1.00 57.44  ? 357 TYR   A CB     1 
ATOM   2771  C  CG     . TYR   A 1  357 ? 18.630  -103.788 -73.878  1.00 60.23  ? 357 TYR   A CG     1 
ATOM   2772  C  CD1    . TYR   A 1  357 ? 18.106  -102.929 -74.839  1.00 59.74  ? 357 TYR   A CD1    1 
ATOM   2773  C  CD2    . TYR   A 1  357 ? 19.542  -104.741 -74.290  1.00 60.78  ? 357 TYR   A CD2    1 
ATOM   2774  C  CE1    . TYR   A 1  357 ? 18.474  -103.041 -76.175  1.00 58.21  ? 357 TYR   A CE1    1 
ATOM   2775  C  CE2    . TYR   A 1  357 ? 19.910  -104.859 -75.610  1.00 62.89  ? 357 TYR   A CE2    1 
ATOM   2776  C  CZ     . TYR   A 1  357 ? 19.383  -104.016 -76.545  1.00 61.20  ? 357 TYR   A CZ     1 
ATOM   2777  O  OH     . TYR   A 1  357 ? 19.784  -104.178 -77.849  1.00 62.80  ? 357 TYR   A OH     1 
ATOM   2778  N  N      . GLN   A 1  358 ? 18.240  -102.125 -69.409  1.00 57.19  ? 358 GLN   A N      1 
ATOM   2779  C  CA     . GLN   A 1  358 ? 17.581  -102.161 -68.088  1.00 62.02  ? 358 GLN   A CA     1 
ATOM   2780  C  C      . GLN   A 1  358 ? 16.738  -100.906 -67.855  1.00 62.34  ? 358 GLN   A C      1 
ATOM   2781  O  O      . GLN   A 1  358 ? 17.298  -99.801  -67.762  1.00 58.70  ? 358 GLN   A O      1 
ATOM   2782  C  CB     . GLN   A 1  358 ? 18.591  -102.318 -66.956  1.00 66.99  ? 358 GLN   A CB     1 
ATOM   2783  C  CG     . GLN   A 1  358 ? 17.947  -102.668 -65.606  1.00 69.29  ? 358 GLN   A CG     1 
ATOM   2784  C  CD     . GLN   A 1  358 ? 18.858  -102.416 -64.389  1.00 73.14  ? 358 GLN   A CD     1 
ATOM   2785  O  OE1    . GLN   A 1  358 ? 19.293  -101.287 -64.130  1.00 70.94  ? 358 GLN   A OE1    1 
ATOM   2786  N  NE2    . GLN   A 1  358 ? 19.172  -103.485 -63.661  1.00 69.94  ? 358 GLN   A NE2    1 
ATOM   2787  N  N      . PRO   A 1  359 ? 15.414  -101.021 -67.754  1.00 62.59  ? 359 PRO   A N      1 
ATOM   2788  C  CA     . PRO   A 1  359 ? 14.558  -99.823  -67.615  1.00 59.86  ? 359 PRO   A CA     1 
ATOM   2789  C  C      . PRO   A 1  359 ? 14.872  -99.066  -66.339  1.00 56.93  ? 359 PRO   A C      1 
ATOM   2790  O  O      . PRO   A 1  359 ? 15.411  -99.642  -65.382  1.00 61.00  ? 359 PRO   A O      1 
ATOM   2791  C  CB     . PRO   A 1  359 ? 13.132  -100.399 -67.583  1.00 56.12  ? 359 PRO   A CB     1 
ATOM   2792  C  CG     . PRO   A 1  359 ? 13.298  -101.859 -67.285  1.00 55.28  ? 359 PRO   A CG     1 
ATOM   2793  C  CD     . PRO   A 1  359 ? 14.640  -102.276 -67.792  1.00 56.77  ? 359 PRO   A CD     1 
ATOM   2794  N  N      . PRO   A 1  360 ? 14.544  -97.778  -66.278  1.00 50.91  ? 360 PRO   A N      1 
ATOM   2795  C  CA     . PRO   A 1  360 ? 14.915  -96.987  -65.103  1.00 51.10  ? 360 PRO   A CA     1 
ATOM   2796  C  C      . PRO   A 1  360 ? 14.434  -97.641  -63.821  1.00 52.90  ? 360 PRO   A C      1 
ATOM   2797  O  O      . PRO   A 1  360 ? 13.440  -98.371  -63.793  1.00 50.87  ? 360 PRO   A O      1 
ATOM   2798  C  CB     . PRO   A 1  360 ? 14.235  -95.636  -65.343  1.00 48.68  ? 360 PRO   A CB     1 
ATOM   2799  C  CG     . PRO   A 1  360 ? 14.102  -95.574  -66.849  1.00 58.87  ? 360 PRO   A CG     1 
ATOM   2800  C  CD     . PRO   A 1  360 ? 13.809  -96.983  -67.274  1.00 56.60  ? 360 PRO   A CD     1 
ATOM   2801  N  N      . THR   A 1  361 ? 15.178  -97.390  -62.760  1.00 52.78  ? 361 THR   A N      1 
ATOM   2802  C  CA     . THR   A 1  361 ? 14.873  -97.929  -61.451  1.00 53.76  ? 361 THR   A CA     1 
ATOM   2803  C  C      . THR   A 1  361 ? 14.261  -96.833  -60.590  1.00 52.67  ? 361 THR   A C      1 
ATOM   2804  O  O      . THR   A 1  361 ? 14.655  -95.666  -60.660  1.00 54.50  ? 361 THR   A O      1 
ATOM   2805  C  CB     . THR   A 1  361 ? 16.140  -98.506  -60.821  1.00 56.96  ? 361 THR   A CB     1 
ATOM   2806  O  OG1    . THR   A 1  361 ? 16.802  -99.354  -61.785  1.00 52.10  ? 361 THR   A OG1    1 
ATOM   2807  C  CG2    . THR   A 1  361 ? 15.801  -99.293  -59.577  1.00 54.93  ? 361 THR   A CG2    1 
ATOM   2808  N  N      . VAL   A 1  362 ? 13.251  -97.191  -59.823  1.00 58.30  ? 362 VAL   A N      1 
ATOM   2809  C  CA     . VAL   A 1  362 ? 12.577  -96.227  -58.966  1.00 64.90  ? 362 VAL   A CA     1 
ATOM   2810  C  C      . VAL   A 1  362 ? 12.680  -96.726  -57.537  1.00 64.48  ? 362 VAL   A C      1 
ATOM   2811  O  O      . VAL   A 1  362 ? 12.340  -97.882  -57.252  1.00 64.19  ? 362 VAL   A O      1 
ATOM   2812  C  CB     . VAL   A 1  362 ? 11.117  -96.018  -59.388  1.00 59.85  ? 362 VAL   A CB     1 
ATOM   2813  C  CG1    . VAL   A 1  362 ? 11.055  -95.024  -60.545  1.00 54.79  ? 362 VAL   A CG1    1 
ATOM   2814  C  CG2    . VAL   A 1  362 ? 10.511  -97.347  -59.778  1.00 61.90  ? 362 VAL   A CG2    1 
ATOM   2815  N  N      . VAL   A 1  363 ? 13.190  -95.873  -56.653  1.00 58.67  ? 363 VAL   A N      1 
ATOM   2816  C  CA     . VAL   A 1  363 ? 13.303  -96.291  -55.250  1.00 67.06  ? 363 VAL   A CA     1 
ATOM   2817  C  C      . VAL   A 1  363 ? 11.912  -96.591  -54.711  1.00 60.46  ? 363 VAL   A C      1 
ATOM   2818  O  O      . VAL   A 1  363 ? 10.990  -95.773  -54.889  1.00 58.94  ? 363 VAL   A O      1 
ATOM   2819  C  CB     . VAL   A 1  363 ? 14.014  -95.213  -54.410  1.00 62.12  ? 363 VAL   A CB     1 
ATOM   2820  C  CG1    . VAL   A 1  363 ? 15.226  -94.707  -55.162  1.00 62.41  ? 363 VAL   A CG1    1 
ATOM   2821  C  CG2    . VAL   A 1  363 ? 13.076  -94.065  -54.102  1.00 66.36  ? 363 VAL   A CG2    1 
ATOM   2822  N  N      . PRO   A 1  364 ? 11.681  -97.752  -54.111  1.00 62.76  ? 364 PRO   A N      1 
ATOM   2823  C  CA     . PRO   A 1  364 ? 10.320  -98.085  -53.681  1.00 67.26  ? 364 PRO   A CA     1 
ATOM   2824  C  C      . PRO   A 1  364 ? 9.747   -96.998  -52.780  1.00 66.23  ? 364 PRO   A C      1 
ATOM   2825  O  O      . PRO   A 1  364 ? 10.422  -96.475  -51.884  1.00 54.14  ? 364 PRO   A O      1 
ATOM   2826  C  CB     . PRO   A 1  364 ? 10.502  -99.418  -52.948  1.00 65.52  ? 364 PRO   A CB     1 
ATOM   2827  C  CG     . PRO   A 1  364 ? 11.702  -100.037 -53.619  1.00 61.58  ? 364 PRO   A CG     1 
ATOM   2828  C  CD     . PRO   A 1  364 ? 12.619  -98.873  -53.907  1.00 62.05  ? 364 PRO   A CD     1 
ATOM   2829  N  N      . GLY   A 1  365 ? 8.495   -96.629  -53.055  1.00 64.48  ? 365 GLY   A N      1 
ATOM   2830  C  CA     . GLY   A 1  365 ? 7.841   -95.576  -52.307  1.00 64.44  ? 365 GLY   A CA     1 
ATOM   2831  C  C      . GLY   A 1  365 ? 8.315   -94.175  -52.613  1.00 68.21  ? 365 GLY   A C      1 
ATOM   2832  O  O      . GLY   A 1  365 ? 8.177   -93.285  -51.771  1.00 71.90  ? 365 GLY   A O      1 
ATOM   2833  N  N      . GLY   A 1  366 ? 8.900   -93.955  -53.785  1.00 64.67  ? 366 GLY   A N      1 
ATOM   2834  C  CA     . GLY   A 1  366 ? 9.195   -92.624  -54.260  1.00 60.44  ? 366 GLY   A CA     1 
ATOM   2835  C  C      . GLY   A 1  366 ? 7.995   -92.035  -54.968  1.00 56.99  ? 366 GLY   A C      1 
ATOM   2836  O  O      . GLY   A 1  366 ? 6.881   -92.554  -54.905  1.00 59.88  ? 366 GLY   A O      1 
ATOM   2837  N  N      . ASP   A 1  367 ? 8.239   -90.941  -55.676  1.00 56.54  ? 367 ASP   A N      1 
ATOM   2838  C  CA     . ASP   A 1  367 ? 7.192   -90.289  -56.440  1.00 52.68  ? 367 ASP   A CA     1 
ATOM   2839  C  C      . ASP   A 1  367 ? 7.240   -90.634  -57.925  1.00 54.29  ? 367 ASP   A C      1 
ATOM   2840  O  O      . ASP   A 1  367 ? 6.274   -90.359  -58.638  1.00 52.02  ? 367 ASP   A O      1 
ATOM   2841  C  CB     . ASP   A 1  367 ? 7.279   -88.767  -56.252  1.00 56.19  ? 367 ASP   A CB     1 
ATOM   2842  C  CG     . ASP   A 1  367 ? 7.419   -88.366  -54.778  1.00 62.90  ? 367 ASP   A CG     1 
ATOM   2843  O  OD1    . ASP   A 1  367 ? 6.422   -88.490  -54.034  1.00 53.26  ? 367 ASP   A OD1    1 
ATOM   2844  O  OD2    . ASP   A 1  367 ? 8.531   -87.939  -54.362  1.00 63.02  ? 367 ASP   A OD2    1 
ATOM   2845  N  N      . LEU   A 1  368 ? 8.321   -91.235  -58.414  1.00 52.99  ? 368 LEU   A N      1 
ATOM   2846  C  CA     . LEU   A 1  368 ? 8.392   -91.587  -59.826  1.00 55.89  ? 368 LEU   A CA     1 
ATOM   2847  C  C      . LEU   A 1  368 ? 7.784   -92.963  -60.067  1.00 57.62  ? 368 LEU   A C      1 
ATOM   2848  O  O      . LEU   A 1  368 ? 8.001   -93.902  -59.294  1.00 57.30  ? 368 LEU   A O      1 
ATOM   2849  C  CB     . LEU   A 1  368 ? 9.834   -91.559  -60.336  1.00 52.39  ? 368 LEU   A CB     1 
ATOM   2850  C  CG     . LEU   A 1  368 ? 10.548  -90.217  -60.256  1.00 48.32  ? 368 LEU   A CG     1 
ATOM   2851  C  CD1    . LEU   A 1  368 ? 11.772  -90.221  -61.163  1.00 43.31  ? 368 LEU   A CD1    1 
ATOM   2852  C  CD2    . LEU   A 1  368 ? 9.572   -89.133  -60.647  1.00 52.38  ? 368 LEU   A CD2    1 
ATOM   2853  N  N      . ALA   A 1  369 ? 7.015   -93.069  -61.143  1.00 54.28  ? 369 ALA   A N      1 
ATOM   2854  C  CA     . ALA   A 1  369 ? 6.453   -94.339  -61.562  1.00 50.56  ? 369 ALA   A CA     1 
ATOM   2855  C  C      . ALA   A 1  369 ? 7.475   -95.123  -62.379  1.00 51.94  ? 369 ALA   A C      1 
ATOM   2856  O  O      . ALA   A 1  369 ? 8.288   -94.538  -63.102  1.00 52.39  ? 369 ALA   A O      1 
ATOM   2857  C  CB     . ALA   A 1  369 ? 5.187   -94.094  -62.380  1.00 45.03  ? 369 ALA   A CB     1 
ATOM   2858  N  N      . LYS   A 1  370 ? 7.453   -96.451  -62.241  1.00 53.74  ? 370 LYS   A N      1 
ATOM   2859  C  CA     . LYS   A 1  370 ? 8.144   -97.302  -63.205  1.00 52.27  ? 370 LYS   A CA     1 
ATOM   2860  C  C      . LYS   A 1  370 ? 7.627   -97.020  -64.610  1.00 50.00  ? 370 LYS   A C      1 
ATOM   2861  O  O      . LYS   A 1  370 ? 6.440   -96.742  -64.810  1.00 49.56  ? 370 LYS   A O      1 
ATOM   2862  C  CB     . LYS   A 1  370 ? 7.954   -98.786  -62.875  1.00 54.09  ? 370 LYS   A CB     1 
ATOM   2863  C  CG     . LYS   A 1  370 ? 8.716   -99.269  -61.637  1.00 69.22  ? 370 LYS   A CG     1 
ATOM   2864  C  CD     . LYS   A 1  370 ? 8.011   -100.429 -60.926  1.00 75.77  ? 370 LYS   A CD     1 
ATOM   2865  C  CE     . LYS   A 1  370 ? 7.780   -100.068 -59.449  1.00 72.62  ? 370 LYS   A CE     1 
ATOM   2866  N  NZ     . LYS   A 1  370 ? 6.688   -99.041  -59.278  1.00 71.66  ? 370 LYS   A NZ     1 
ATOM   2867  N  N      . VAL   A 1  371 ? 8.530   -97.085  -65.586  1.00 48.21  ? 371 VAL   A N      1 
ATOM   2868  C  CA     . VAL   A 1  371 ? 8.204   -96.849  -66.984  1.00 51.64  ? 371 VAL   A CA     1 
ATOM   2869  C  C      . VAL   A 1  371 ? 9.019   -97.812  -67.827  1.00 56.19  ? 371 VAL   A C      1 
ATOM   2870  O  O      . VAL   A 1  371 ? 10.097  -98.261  -67.426  1.00 57.75  ? 371 VAL   A O      1 
ATOM   2871  C  CB     . VAL   A 1  371 ? 8.475   -95.389  -67.430  1.00 57.27  ? 371 VAL   A CB     1 
ATOM   2872  C  CG1    . VAL   A 1  371 ? 7.708   -94.385  -66.568  1.00 44.29  ? 371 VAL   A CG1    1 
ATOM   2873  C  CG2    . VAL   A 1  371 ? 9.973   -95.100  -67.441  1.00 56.19  ? 371 VAL   A CG2    1 
ATOM   2874  N  N      . GLN   A 1  372 ? 8.499   -98.125  -69.013  1.00 63.14  ? 372 GLN   A N      1 
ATOM   2875  C  CA     . GLN   A 1  372 ? 9.146   -99.125  -69.855  1.00 64.69  ? 372 GLN   A CA     1 
ATOM   2876  C  C      . GLN   A 1  372 ? 10.378  -98.570  -70.546  1.00 58.76  ? 372 GLN   A C      1 
ATOM   2877  O  O      . GLN   A 1  372 ? 11.324  -99.318  -70.817  1.00 59.33  ? 372 GLN   A O      1 
ATOM   2878  C  CB     . GLN   A 1  372 ? 8.169   -99.648  -70.909  1.00 73.40  ? 372 GLN   A CB     1 
ATOM   2879  C  CG     . GLN   A 1  372 ? 7.362   -100.853 -70.470  1.00 79.82  ? 372 GLN   A CG     1 
ATOM   2880  C  CD     . GLN   A 1  372 ? 5.880   -100.686 -70.775  1.00 83.76  ? 372 GLN   A CD     1 
ATOM   2881  O  OE1    . GLN   A 1  372 ? 5.502   -100.003 -71.740  1.00 82.03  ? 372 GLN   A OE1    1 
ATOM   2882  N  NE2    . GLN   A 1  372 ? 5.029   -101.301 -69.947  1.00 82.66  ? 372 GLN   A NE2    1 
ATOM   2883  N  N      . ARG   A 1  373 ? 10.373  -97.278  -70.850  1.00 53.39  ? 373 ARG   A N      1 
ATOM   2884  C  CA     . ARG   A 1  373 ? 11.504  -96.634  -71.492  1.00 53.87  ? 373 ARG   A CA     1 
ATOM   2885  C  C      . ARG   A 1  373 ? 11.615  -95.187  -71.011  1.00 54.48  ? 373 ARG   A C      1 
ATOM   2886  O  O      . ARG   A 1  373 ? 10.606  -94.501  -70.805  1.00 51.90  ? 373 ARG   A O      1 
ATOM   2887  C  CB     . ARG   A 1  373 ? 11.378  -96.718  -73.025  1.00 54.23  ? 373 ARG   A CB     1 
ATOM   2888  C  CG     . ARG   A 1  373 ? 10.094  -96.142  -73.644  1.00 51.90  ? 373 ARG   A CG     1 
ATOM   2889  C  CD     . ARG   A 1  373 ? 9.823   -96.757  -75.045  1.00 49.74  ? 373 ARG   A CD     1 
ATOM   2890  N  NE     . ARG   A 1  373 ? 9.136   -98.049  -74.987  1.00 57.01  ? 373 ARG   A NE     1 
ATOM   2891  C  CZ     . ARG   A 1  373 ? 8.015   -98.272  -74.307  1.00 62.92  ? 373 ARG   A CZ     1 
ATOM   2892  N  NH1    . ARG   A 1  373 ? 7.411   -97.306  -73.640  1.00 65.51  ? 373 ARG   A NH1    1 
ATOM   2893  N  NH2    . ARG   A 1  373 ? 7.490   -99.497  -74.284  1.00 57.90  ? 373 ARG   A NH2    1 
ATOM   2894  N  N      . ALA   A 1  374 ? 12.853  -94.749  -70.795  1.00 51.57  ? 374 ALA   A N      1 
ATOM   2895  C  CA     . ALA   A 1  374 ? 13.168  -93.363  -70.490  1.00 45.13  ? 374 ALA   A CA     1 
ATOM   2896  C  C      . ALA   A 1  374 ? 14.352  -92.934  -71.337  1.00 43.68  ? 374 ALA   A C      1 
ATOM   2897  O  O      . ALA   A 1  374 ? 15.045  -93.763  -71.939  1.00 40.59  ? 374 ALA   A O      1 
ATOM   2898  C  CB     . ALA   A 1  374 ? 13.501  -93.154  -69.021  1.00 41.78  ? 374 ALA   A CB     1 
ATOM   2899  N  N      . VAL   A 1  375 ? 14.567  -91.620  -71.394  1.00 37.15  ? 375 VAL   A N      1 
ATOM   2900  C  CA     . VAL   A 1  375 ? 15.679  -91.074  -72.156  1.00 38.80  ? 375 VAL   A CA     1 
ATOM   2901  C  C      . VAL   A 1  375 ? 16.184  -89.838  -71.436  1.00 44.73  ? 375 VAL   A C      1 
ATOM   2902  O  O      . VAL   A 1  375 ? 15.431  -89.156  -70.731  1.00 42.75  ? 375 VAL   A O      1 
ATOM   2903  C  CB     . VAL   A 1  375 ? 15.289  -90.740  -73.612  1.00 43.08  ? 375 VAL   A CB     1 
ATOM   2904  C  CG1    . VAL   A 1  375 ? 14.179  -89.698  -73.644  1.00 40.25  ? 375 VAL   A CG1    1 
ATOM   2905  C  CG2    . VAL   A 1  375 ? 16.524  -90.268  -74.389  1.00 41.07  ? 375 VAL   A CG2    1 
ATOM   2906  N  N      . CYS   A 1  376 ? 17.478  -89.560  -71.604  1.00 39.78  ? 376 CYS   A N      1 
ATOM   2907  C  CA     . CYS   A 1  376 ? 18.080  -88.344  -71.075  1.00 40.13  ? 376 CYS   A CA     1 
ATOM   2908  C  C      . CYS   A 1  376 ? 18.923  -87.780  -72.193  1.00 41.43  ? 376 CYS   A C      1 
ATOM   2909  O  O      . CYS   A 1  376 ? 19.940  -88.377  -72.555  1.00 46.69  ? 376 CYS   A O      1 
ATOM   2910  C  CB     . CYS   A 1  376 ? 18.938  -88.597  -69.829  1.00 48.31  ? 376 CYS   A CB     1 
ATOM   2911  S  SG     . CYS   A 1  376 ? 19.865  -87.136  -69.230  1.00 47.08  ? 376 CYS   A SG     1 
ATOM   2912  N  N      . MET   A 1  377 ? 18.494  -86.655  -72.753  1.00 40.39  ? 377 MET   A N      1 
ATOM   2913  C  CA     . MET   A 1  377 ? 19.295  -85.975  -73.757  1.00 42.52  ? 377 MET   A CA     1 
ATOM   2914  C  C      . MET   A 1  377 ? 20.348  -85.097  -73.074  1.00 45.16  ? 377 MET   A C      1 
ATOM   2915  O  O      . MET   A 1  377 ? 20.038  -84.367  -72.129  1.00 45.41  ? 377 MET   A O      1 
ATOM   2916  C  CB     . MET   A 1  377 ? 18.405  -85.133  -74.661  1.00 45.12  ? 377 MET   A CB     1 
ATOM   2917  C  CG     . MET   A 1  377 ? 19.186  -84.273  -75.641  1.00 48.97  ? 377 MET   A CG     1 
ATOM   2918  S  SD     . MET   A 1  377 ? 18.303  -84.079  -77.187  1.00 57.25  ? 377 MET   A SD     1 
ATOM   2919  C  CE     . MET   A 1  377 ? 17.491  -82.538  -76.870  1.00 48.77  ? 377 MET   A CE     1 
ATOM   2920  N  N      . LEU   A 1  378 ? 21.593  -85.180  -73.546  1.00 47.65  ? 378 LEU   A N      1 
ATOM   2921  C  CA     . LEU   A 1  378 ? 22.664  -84.260  -73.175  1.00 40.85  ? 378 LEU   A CA     1 
ATOM   2922  C  C      . LEU   A 1  378 ? 22.991  -83.449  -74.411  1.00 41.55  ? 378 LEU   A C      1 
ATOM   2923  O  O      . LEU   A 1  378 ? 23.436  -84.011  -75.412  1.00 50.37  ? 378 LEU   A O      1 
ATOM   2924  C  CB     . LEU   A 1  378 ? 23.919  -84.998  -72.703  1.00 38.21  ? 378 LEU   A CB     1 
ATOM   2925  C  CG     . LEU   A 1  378 ? 23.837  -85.999  -71.550  1.00 43.42  ? 378 LEU   A CG     1 
ATOM   2926  C  CD1    . LEU   A 1  378 ? 25.187  -86.694  -71.315  1.00 38.08  ? 378 LEU   A CD1    1 
ATOM   2927  C  CD2    . LEU   A 1  378 ? 23.337  -85.322  -70.306  1.00 35.25  ? 378 LEU   A CD2    1 
ATOM   2928  N  N      . SER   A 1  379 ? 22.765  -82.150  -74.367  1.00 38.82  ? 379 SER   A N      1 
ATOM   2929  C  CA     . SER   A 1  379 ? 23.023  -81.336  -75.551  1.00 47.73  ? 379 SER   A CA     1 
ATOM   2930  C  C      . SER   A 1  379 ? 23.830  -80.107  -75.159  1.00 48.06  ? 379 SER   A C      1 
ATOM   2931  O  O      . SER   A 1  379 ? 23.475  -79.405  -74.209  1.00 50.76  ? 379 SER   A O      1 
ATOM   2932  C  CB     . SER   A 1  379 ? 21.718  -80.923  -76.240  1.00 42.50  ? 379 SER   A CB     1 
ATOM   2933  O  OG     . SER   A 1  379 ? 20.687  -80.612  -75.308  1.00 48.43  ? 379 SER   A OG     1 
ATOM   2934  N  N      . ASN   A 1  380 ? 24.915  -79.851  -75.875  1.00 39.39  ? 380 ASN   A N      1 
ATOM   2935  C  CA     . ASN   A 1  380 ? 25.676  -78.630  -75.650  1.00 43.51  ? 380 ASN   A CA     1 
ATOM   2936  C  C      . ASN   A 1  380 ? 25.109  -77.531  -76.538  1.00 39.80  ? 380 ASN   A C      1 
ATOM   2937  O  O      . ASN   A 1  380 ? 25.574  -77.289  -77.648  1.00 45.11  ? 380 ASN   A O      1 
ATOM   2938  C  CB     . ASN   A 1  380 ? 27.153  -78.869  -75.924  1.00 48.92  ? 380 ASN   A CB     1 
ATOM   2939  C  CG     . ASN   A 1  380 ? 28.020  -77.853  -75.269  1.00 45.18  ? 380 ASN   A CG     1 
ATOM   2940  O  OD1    . ASN   A 1  380 ? 27.616  -76.705  -75.112  1.00 47.04  ? 380 ASN   A OD1    1 
ATOM   2941  N  ND2    . ASN   A 1  380 ? 29.200  -78.271  -74.827  1.00 46.74  ? 380 ASN   A ND2    1 
ATOM   2942  N  N      . THR   A 1  381 ? 24.075  -76.864  -76.042  1.00 41.31  ? 381 THR   A N      1 
ATOM   2943  C  CA     . THR   A 1  381 ? 23.432  -75.770  -76.768  1.00 45.18  ? 381 THR   A CA     1 
ATOM   2944  C  C      . THR   A 1  381 ? 23.826  -74.429  -76.164  1.00 46.97  ? 381 THR   A C      1 
ATOM   2945  O  O      . THR   A 1  381 ? 23.913  -74.288  -74.940  1.00 43.86  ? 381 THR   A O      1 
ATOM   2946  C  CB     . THR   A 1  381 ? 21.904  -75.886  -76.763  1.00 38.61  ? 381 THR   A CB     1 
ATOM   2947  O  OG1    . THR   A 1  381 ? 21.351  -74.648  -77.210  1.00 49.69  ? 381 THR   A OG1    1 
ATOM   2948  C  CG2    . THR   A 1  381 ? 21.366  -76.177  -75.392  1.00 37.01  ? 381 THR   A CG2    1 
ATOM   2949  N  N      . THR   A 1  382 ? 24.091  -73.443  -77.026  1.00 51.26  ? 382 THR   A N      1 
ATOM   2950  C  CA     . THR   A 1  382 ? 24.464  -72.143  -76.478  1.00 49.68  ? 382 THR   A CA     1 
ATOM   2951  C  C      . THR   A 1  382 ? 23.327  -71.508  -75.700  1.00 45.67  ? 382 THR   A C      1 
ATOM   2952  O  O      . THR   A 1  382 ? 23.569  -70.541  -74.983  1.00 43.84  ? 382 THR   A O      1 
ATOM   2953  C  CB     . THR   A 1  382 ? 24.928  -71.167  -77.569  1.00 47.68  ? 382 THR   A CB     1 
ATOM   2954  O  OG1    . THR   A 1  382 ? 23.893  -71.004  -78.549  1.00 52.11  ? 382 THR   A OG1    1 
ATOM   2955  C  CG2    . THR   A 1  382 ? 26.219  -71.636  -78.214  1.00 44.51  ? 382 THR   A CG2    1 
ATOM   2956  N  N      . ALA   A 1  383 ? 22.106  -72.031  -75.818  1.00 43.92  ? 383 ALA   A N      1 
ATOM   2957  C  CA     . ALA   A 1  383 ? 20.965  -71.398  -75.175  1.00 46.45  ? 383 ALA   A CA     1 
ATOM   2958  C  C      . ALA   A 1  383 ? 21.050  -71.453  -73.653  1.00 46.64  ? 383 ALA   A C      1 
ATOM   2959  O  O      . ALA   A 1  383 ? 20.316  -70.726  -72.979  1.00 50.79  ? 383 ALA   A O      1 
ATOM   2960  C  CB     . ALA   A 1  383 ? 19.668  -72.045  -75.679  1.00 46.68  ? 383 ALA   A CB     1 
ATOM   2961  N  N      . ILE   A 1  384 ? 21.917  -72.305  -73.098  1.00 45.54  ? 384 ILE   A N      1 
ATOM   2962  C  CA     . ILE   A 1  384 ? 22.127  -72.361  -71.657  1.00 39.63  ? 384 ILE   A CA     1 
ATOM   2963  C  C      . ILE   A 1  384 ? 22.820  -71.105  -71.139  1.00 43.15  ? 384 ILE   A C      1 
ATOM   2964  O  O      . ILE   A 1  384 ? 22.768  -70.821  -69.934  1.00 45.54  ? 384 ILE   A O      1 
ATOM   2965  C  CB     . ILE   A 1  384 ? 22.939  -73.617  -71.285  1.00 36.98  ? 384 ILE   A CB     1 
ATOM   2966  C  CG1    . ILE   A 1  384 ? 22.622  -74.073  -69.861  1.00 32.79  ? 384 ILE   A CG1    1 
ATOM   2967  C  CG2    . ILE   A 1  384 ? 24.405  -73.381  -71.475  1.00 31.87  ? 384 ILE   A CG2    1 
ATOM   2968  C  CD1    . ILE   A 1  384 ? 23.037  -75.482  -69.609  1.00 32.28  ? 384 ILE   A CD1    1 
ATOM   2969  N  N      . ALA   A 1  385 ? 23.486  -70.345  -72.012  1.00 43.00  ? 385 ALA   A N      1 
ATOM   2970  C  CA     . ALA   A 1  385 ? 24.045  -69.068  -71.587  1.00 43.28  ? 385 ALA   A CA     1 
ATOM   2971  C  C      . ALA   A 1  385 ? 22.980  -68.156  -71.003  1.00 43.08  ? 385 ALA   A C      1 
ATOM   2972  O  O      . ALA   A 1  385 ? 23.315  -67.274  -70.208  1.00 48.92  ? 385 ALA   A O      1 
ATOM   2973  C  CB     . ALA   A 1  385 ? 24.751  -68.366  -72.749  1.00 44.69  ? 385 ALA   A CB     1 
ATOM   2974  N  N      . GLU   A 1  386 ? 21.709  -68.358  -71.364  1.00 43.08  ? 386 GLU   A N      1 
ATOM   2975  C  CA     . GLU   A 1  386 ? 20.625  -67.605  -70.739  1.00 40.95  ? 386 GLU   A CA     1 
ATOM   2976  C  C      . GLU   A 1  386 ? 20.732  -67.645  -69.222  1.00 44.61  ? 386 GLU   A C      1 
ATOM   2977  O  O      . GLU   A 1  386 ? 20.449  -66.649  -68.544  1.00 43.90  ? 386 GLU   A O      1 
ATOM   2978  C  CB     . GLU   A 1  386 ? 19.271  -68.157  -71.176  1.00 38.05  ? 386 GLU   A CB     1 
ATOM   2979  C  CG     . GLU   A 1  386 ? 18.764  -67.638  -72.511  1.00 44.77  ? 386 GLU   A CG     1 
ATOM   2980  C  CD     . GLU   A 1  386 ? 17.492  -68.348  -72.980  1.00 51.67  ? 386 GLU   A CD     1 
ATOM   2981  O  OE1    . GLU   A 1  386 ? 16.555  -68.508  -72.146  1.00 47.49  ? 386 GLU   A OE1    1 
ATOM   2982  O  OE2    . GLU   A 1  386 ? 17.441  -68.736  -74.179  1.00 48.02  ? 386 GLU   A OE2    1 
ATOM   2983  N  N      . ALA   A 1  387 ? 21.128  -68.793  -68.670  1.00 41.25  ? 387 ALA   A N      1 
ATOM   2984  C  CA     . ALA   A 1  387 ? 21.204  -68.910  -67.222  1.00 40.09  ? 387 ALA   A CA     1 
ATOM   2985  C  C      . ALA   A 1  387 ? 22.325  -68.042  -66.680  1.00 43.76  ? 387 ALA   A C      1 
ATOM   2986  O  O      . ALA   A 1  387 ? 22.172  -67.426  -65.620  1.00 43.38  ? 387 ALA   A O      1 
ATOM   2987  C  CB     . ALA   A 1  387 ? 21.380  -70.378  -66.810  1.00 32.56  ? 387 ALA   A CB     1 
ATOM   2988  N  N      . TRP   A 1  388 ? 23.453  -67.975  -67.408  1.00 44.96  ? 388 TRP   A N      1 
ATOM   2989  C  CA     . TRP   A 1  388 ? 24.555  -67.078  -67.046  1.00 46.95  ? 388 TRP   A CA     1 
ATOM   2990  C  C      . TRP   A 1  388 ? 24.120  -65.615  -67.075  1.00 48.34  ? 388 TRP   A C      1 
ATOM   2991  O  O      . TRP   A 1  388 ? 24.483  -64.832  -66.195  1.00 41.99  ? 388 TRP   A O      1 
ATOM   2992  C  CB     . TRP   A 1  388 ? 25.736  -67.273  -67.999  1.00 42.92  ? 388 TRP   A CB     1 
ATOM   2993  C  CG     . TRP   A 1  388 ? 26.362  -68.620  -67.955  1.00 44.37  ? 388 TRP   A CG     1 
ATOM   2994  C  CD1    . TRP   A 1  388 ? 26.690  -69.397  -69.026  1.00 44.54  ? 388 TRP   A CD1    1 
ATOM   2995  C  CD2    . TRP   A 1  388 ? 26.759  -69.355  -66.788  1.00 39.34  ? 388 TRP   A CD2    1 
ATOM   2996  N  NE1    . TRP   A 1  388 ? 27.261  -70.579  -68.596  1.00 46.70  ? 388 TRP   A NE1    1 
ATOM   2997  C  CE2    . TRP   A 1  388 ? 27.309  -70.576  -67.228  1.00 41.91  ? 388 TRP   A CE2    1 
ATOM   2998  C  CE3    . TRP   A 1  388 ? 26.690  -69.106  -65.420  1.00 41.62  ? 388 TRP   A CE3    1 
ATOM   2999  C  CZ2    . TRP   A 1  388 ? 27.786  -71.544  -66.346  1.00 44.88  ? 388 TRP   A CZ2    1 
ATOM   3000  C  CZ3    . TRP   A 1  388 ? 27.178  -70.068  -64.539  1.00 41.45  ? 388 TRP   A CZ3    1 
ATOM   3001  C  CH2    . TRP   A 1  388 ? 27.718  -71.272  -65.009  1.00 43.22  ? 388 TRP   A CH2    1 
ATOM   3002  N  N      . ALA   A 1  389 ? 23.368  -65.213  -68.095  1.00 48.69  ? 389 ALA   A N      1 
ATOM   3003  C  CA     . ALA   A 1  389 ? 22.884  -63.844  -68.103  1.00 46.24  ? 389 ALA   A CA     1 
ATOM   3004  C  C      . ALA   A 1  389 ? 22.024  -63.573  -66.870  1.00 45.58  ? 389 ALA   A C      1 
ATOM   3005  O  O      . ALA   A 1  389 ? 22.281  -62.624  -66.126  1.00 48.56  ? 389 ALA   A O      1 
ATOM   3006  C  CB     . ALA   A 1  389 ? 22.131  -63.568  -69.394  1.00 39.88  ? 389 ALA   A CB     1 
ATOM   3007  N  N      . ARG   A 1  390 ? 21.026  -64.425  -66.610  1.00 44.55  ? 390 ARG   A N      1 
ATOM   3008  C  CA     . ARG   A 1  390 ? 20.205  -64.288  -65.404  1.00 43.92  ? 390 ARG   A CA     1 
ATOM   3009  C  C      . ARG   A 1  390 ? 21.077  -64.090  -64.162  1.00 44.72  ? 390 ARG   A C      1 
ATOM   3010  O  O      . ARG   A 1  390 ? 20.983  -63.077  -63.465  1.00 40.85  ? 390 ARG   A O      1 
ATOM   3011  C  CB     . ARG   A 1  390 ? 19.307  -65.525  -65.224  1.00 44.96  ? 390 ARG   A CB     1 
ATOM   3012  C  CG     . ARG   A 1  390 ? 18.309  -65.804  -66.358  1.00 45.20  ? 390 ARG   A CG     1 
ATOM   3013  C  CD     . ARG   A 1  390 ? 17.509  -67.139  -66.185  1.00 42.02  ? 390 ARG   A CD     1 
ATOM   3014  N  NE     . ARG   A 1  390 ? 17.137  -67.487  -64.816  1.00 41.66  ? 390 ARG   A NE     1 
ATOM   3015  C  CZ     . ARG   A 1  390 ? 17.224  -68.713  -64.303  1.00 47.66  ? 390 ARG   A CZ     1 
ATOM   3016  N  NH1    . ARG   A 1  390 ? 17.765  -69.716  -64.981  1.00 43.60  ? 390 ARG   A NH1    1 
ATOM   3017  N  NH2    . ARG   A 1  390 ? 16.753  -68.944  -63.081  1.00 43.12  ? 390 ARG   A NH2    1 
ATOM   3018  N  N      . LEU   A 1  391 ? 21.933  -65.071  -63.873  1.00 49.31  ? 391 LEU   A N      1 
ATOM   3019  C  CA     . LEU   A 1  391 ? 22.817  -65.000  -62.714  1.00 42.85  ? 391 LEU   A CA     1 
ATOM   3020  C  C      . LEU   A 1  391 ? 23.667  -63.739  -62.726  1.00 46.00  ? 391 LEU   A C      1 
ATOM   3021  O  O      . LEU   A 1  391 ? 23.856  -63.107  -61.681  1.00 49.42  ? 391 LEU   A O      1 
ATOM   3022  C  CB     . LEU   A 1  391 ? 23.711  -66.229  -62.680  1.00 42.17  ? 391 LEU   A CB     1 
ATOM   3023  C  CG     . LEU   A 1  391 ? 24.132  -66.724  -61.305  1.00 48.08  ? 391 LEU   A CG     1 
ATOM   3024  C  CD1    . LEU   A 1  391 ? 22.922  -67.062  -60.439  1.00 37.88  ? 391 LEU   A CD1    1 
ATOM   3025  C  CD2    . LEU   A 1  391 ? 25.003  -67.950  -61.507  1.00 46.05  ? 391 LEU   A CD2    1 
ATOM   3026  N  N      . ASP   A 1  392 ? 24.187  -63.353  -63.898  1.00 46.14  ? 392 ASP   A N      1 
ATOM   3027  C  CA     . ASP   A 1  392 ? 25.080  -62.194  -63.972  1.00 44.46  ? 392 ASP   A CA     1 
ATOM   3028  C  C      . ASP   A 1  392 ? 24.315  -60.888  -63.811  1.00 41.01  ? 392 ASP   A C      1 
ATOM   3029  O  O      . ASP   A 1  392 ? 24.858  -59.911  -63.295  1.00 39.66  ? 392 ASP   A O      1 
ATOM   3030  C  CB     . ASP   A 1  392 ? 25.861  -62.193  -65.295  1.00 45.70  ? 392 ASP   A CB     1 
ATOM   3031  C  CG     . ASP   A 1  392 ? 26.989  -63.234  -65.321  1.00 49.38  ? 392 ASP   A CG     1 
ATOM   3032  O  OD1    . ASP   A 1  392 ? 27.422  -63.694  -64.233  1.00 48.57  ? 392 ASP   A OD1    1 
ATOM   3033  O  OD2    . ASP   A 1  392 ? 27.433  -63.604  -66.432  1.00 47.14  ? 392 ASP   A OD2    1 
ATOM   3034  N  N      . HIS   A 1  393 ? 23.060  -60.836  -64.240  1.00 45.87  ? 393 HIS   A N      1 
ATOM   3035  C  CA     . HIS   A 1  393 ? 22.265  -59.654  -63.932  1.00 48.98  ? 393 HIS   A CA     1 
ATOM   3036  C  C      . HIS   A 1  393 ? 22.075  -59.506  -62.430  1.00 47.36  ? 393 HIS   A C      1 
ATOM   3037  O  O      . HIS   A 1  393 ? 22.374  -58.452  -61.854  1.00 48.44  ? 393 HIS   A O      1 
ATOM   3038  C  CB     . HIS   A 1  393 ? 20.912  -59.712  -64.615  1.00 43.42  ? 393 HIS   A CB     1 
ATOM   3039  C  CG     . HIS   A 1  393 ? 20.214  -58.395  -64.626  1.00 46.09  ? 393 HIS   A CG     1 
ATOM   3040  N  ND1    . HIS   A 1  393 ? 20.743  -57.288  -65.256  1.00 52.61  ? 393 HIS   A ND1    1 
ATOM   3041  C  CD2    . HIS   A 1  393 ? 19.033  -58.003  -64.097  1.00 45.02  ? 393 HIS   A CD2    1 
ATOM   3042  C  CE1    . HIS   A 1  393 ? 19.911  -56.271  -65.121  1.00 52.62  ? 393 HIS   A CE1    1 
ATOM   3043  N  NE2    . HIS   A 1  393 ? 18.868  -56.678  -64.418  1.00 54.53  ? 393 HIS   A NE2    1 
ATOM   3044  N  N      . LYS   A 1  394 ? 21.570  -60.554  -61.777  1.00 42.61  ? 394 LYS   A N      1 
ATOM   3045  C  CA     . LYS   A 1  394 ? 21.368  -60.486  -60.338  1.00 42.86  ? 394 LYS   A CA     1 
ATOM   3046  C  C      . LYS   A 1  394 ? 22.635  -60.012  -59.637  1.00 47.01  ? 394 LYS   A C      1 
ATOM   3047  O  O      . LYS   A 1  394 ? 22.576  -59.202  -58.703  1.00 45.93  ? 394 LYS   A O      1 
ATOM   3048  C  CB     . LYS   A 1  394 ? 20.914  -61.846  -59.826  1.00 39.88  ? 394 LYS   A CB     1 
ATOM   3049  C  CG     . LYS   A 1  394 ? 19.513  -62.200  -60.307  1.00 38.38  ? 394 LYS   A CG     1 
ATOM   3050  C  CD     . LYS   A 1  394 ? 19.002  -63.471  -59.681  1.00 36.36  ? 394 LYS   A CD     1 
ATOM   3051  C  CE     . LYS   A 1  394 ? 17.494  -63.479  -59.576  1.00 37.08  ? 394 LYS   A CE     1 
ATOM   3052  N  NZ     . LYS   A 1  394 ? 16.982  -64.889  -59.442  1.00 48.88  ? 394 LYS   A NZ     1 
ATOM   3053  N  N      . PHE   A 1  395 ? 23.798  -60.461  -60.119  1.00 45.72  ? 395 PHE   A N      1 
ATOM   3054  C  CA     . PHE   A 1  395 ? 25.062  -60.078  -59.501  1.00 42.19  ? 395 PHE   A CA     1 
ATOM   3055  C  C      . PHE   A 1  395 ? 25.362  -58.597  -59.729  1.00 46.33  ? 395 PHE   A C      1 
ATOM   3056  O  O      . PHE   A 1  395 ? 25.771  -57.886  -58.799  1.00 50.51  ? 395 PHE   A O      1 
ATOM   3057  C  CB     . PHE   A 1  395 ? 26.161  -60.996  -60.046  1.00 43.91  ? 395 PHE   A CB     1 
ATOM   3058  C  CG     . PHE   A 1  395 ? 27.579  -60.595  -59.691  1.00 37.56  ? 395 PHE   A CG     1 
ATOM   3059  C  CD1    . PHE   A 1  395 ? 28.162  -59.462  -60.234  1.00 40.53  ? 395 PHE   A CD1    1 
ATOM   3060  C  CD2    . PHE   A 1  395 ? 28.353  -61.412  -58.904  1.00 36.16  ? 395 PHE   A CD2    1 
ATOM   3061  C  CE1    . PHE   A 1  395 ? 29.469  -59.130  -59.949  1.00 40.91  ? 395 PHE   A CE1    1 
ATOM   3062  C  CE2    . PHE   A 1  395 ? 29.660  -61.082  -58.616  1.00 38.98  ? 395 PHE   A CE2    1 
ATOM   3063  C  CZ     . PHE   A 1  395 ? 30.215  -59.939  -59.136  1.00 39.56  ? 395 PHE   A CZ     1 
ATOM   3064  N  N      . ASP   A 1  396 ? 25.150  -58.101  -60.947  1.00 41.08  ? 396 ASP   A N      1 
ATOM   3065  C  CA     . ASP   A 1  396 ? 25.391  -56.684  -61.197  1.00 43.51  ? 396 ASP   A CA     1 
ATOM   3066  C  C      . ASP   A 1  396 ? 24.490  -55.803  -60.327  1.00 47.79  ? 396 ASP   A C      1 
ATOM   3067  O  O      . ASP   A 1  396 ? 24.922  -54.745  -59.842  1.00 43.52  ? 396 ASP   A O      1 
ATOM   3068  C  CB     . ASP   A 1  396 ? 25.192  -56.378  -62.679  1.00 35.62  ? 396 ASP   A CB     1 
ATOM   3069  C  CG     . ASP   A 1  396 ? 26.159  -57.146  -63.565  1.00 43.76  ? 396 ASP   A CG     1 
ATOM   3070  O  OD1    . ASP   A 1  396 ? 27.190  -57.627  -63.042  1.00 48.17  ? 396 ASP   A OD1    1 
ATOM   3071  O  OD2    . ASP   A 1  396 ? 25.885  -57.288  -64.780  1.00 41.97  ? 396 ASP   A OD2    1 
ATOM   3072  N  N      . LEU   A 1  397 ? 23.249  -56.241  -60.083  1.00 45.12  ? 397 LEU   A N      1 
ATOM   3073  C  CA     . LEU   A 1  397 ? 22.332  -55.441  -59.273  1.00 44.97  ? 397 LEU   A CA     1 
ATOM   3074  C  C      . LEU   A 1  397 ? 22.875  -55.228  -57.858  1.00 46.54  ? 397 LEU   A C      1 
ATOM   3075  O  O      . LEU   A 1  397 ? 22.977  -54.087  -57.389  1.00 44.41  ? 397 LEU   A O      1 
ATOM   3076  C  CB     . LEU   A 1  397 ? 20.940  -56.084  -59.251  1.00 43.59  ? 397 LEU   A CB     1 
ATOM   3077  C  CG     . LEU   A 1  397 ? 20.124  -55.859  -60.537  1.00 43.88  ? 397 LEU   A CG     1 
ATOM   3078  C  CD1    . LEU   A 1  397 ? 18.748  -56.446  -60.442  1.00 45.55  ? 397 LEU   A CD1    1 
ATOM   3079  C  CD2    . LEU   A 1  397 ? 20.041  -54.387  -60.871  1.00 41.01  ? 397 LEU   A CD2    1 
ATOM   3080  N  N      . MET   A 1  398 ? 23.217  -56.315  -57.152  1.00 44.92  ? 398 MET   A N      1 
ATOM   3081  C  CA     . MET   A 1  398 ? 23.765  -56.159  -55.811  1.00 42.20  ? 398 MET   A CA     1 
ATOM   3082  C  C      . MET   A 1  398 ? 25.102  -55.430  -55.839  1.00 44.26  ? 398 MET   A C      1 
ATOM   3083  O  O      . MET   A 1  398 ? 25.337  -54.527  -55.026  1.00 41.72  ? 398 MET   A O      1 
ATOM   3084  C  CB     . MET   A 1  398 ? 23.939  -57.510  -55.117  1.00 42.38  ? 398 MET   A CB     1 
ATOM   3085  C  CG     . MET   A 1  398 ? 22.858  -58.562  -55.305  1.00 46.65  ? 398 MET   A CG     1 
ATOM   3086  S  SD     . MET   A 1  398 ? 22.724  -59.512  -53.763  1.00 51.87  ? 398 MET   A SD     1 
ATOM   3087  C  CE     . MET   A 1  398 ? 24.056  -60.678  -54.076  1.00 49.21  ? 398 MET   A CE     1 
ATOM   3088  N  N      . TYR   A 1  399 ? 26.000  -55.820  -56.754  1.00 45.59  ? 399 TYR   A N      1 
ATOM   3089  C  CA     . TYR   A 1  399 ? 27.375  -55.334  -56.693  1.00 41.21  ? 399 TYR   A CA     1 
ATOM   3090  C  C      . TYR   A 1  399 ? 27.495  -53.862  -57.041  1.00 40.93  ? 399 TYR   A C      1 
ATOM   3091  O  O      . TYR   A 1  399 ? 28.460  -53.222  -56.626  1.00 46.70  ? 399 TYR   A O      1 
ATOM   3092  C  CB     . TYR   A 1  399 ? 28.267  -56.143  -57.616  1.00 40.73  ? 399 TYR   A CB     1 
ATOM   3093  C  CG     . TYR   A 1  399 ? 29.717  -55.836  -57.414  1.00 42.10  ? 399 TYR   A CG     1 
ATOM   3094  C  CD1    . TYR   A 1  399 ? 30.422  -56.406  -56.365  1.00 47.12  ? 399 TYR   A CD1    1 
ATOM   3095  C  CD2    . TYR   A 1  399 ? 30.384  -54.959  -58.255  1.00 42.47  ? 399 TYR   A CD2    1 
ATOM   3096  C  CE1    . TYR   A 1  399 ? 31.767  -56.119  -56.162  1.00 51.01  ? 399 TYR   A CE1    1 
ATOM   3097  C  CE2    . TYR   A 1  399 ? 31.718  -54.656  -58.061  1.00 44.25  ? 399 TYR   A CE2    1 
ATOM   3098  C  CZ     . TYR   A 1  399 ? 32.411  -55.237  -57.015  1.00 52.20  ? 399 TYR   A CZ     1 
ATOM   3099  O  OH     . TYR   A 1  399 ? 33.750  -54.948  -56.817  1.00 50.71  ? 399 TYR   A OH     1 
ATOM   3100  N  N      . ALA   A 1  400 ? 26.546  -53.306  -57.793  1.00 44.45  ? 400 ALA   A N      1 
ATOM   3101  C  CA     . ALA   A 1  400 ? 26.606  -51.879  -58.091  1.00 43.07  ? 400 ALA   A CA     1 
ATOM   3102  C  C      . ALA   A 1  400 ? 26.556  -51.058  -56.817  1.00 44.24  ? 400 ALA   A C      1 
ATOM   3103  O  O      . ALA   A 1  400 ? 27.189  -50.001  -56.732  1.00 49.54  ? 400 ALA   A O      1 
ATOM   3104  C  CB     . ALA   A 1  400 ? 25.473  -51.481  -59.030  1.00 36.59  ? 400 ALA   A CB     1 
ATOM   3105  N  N      . LYS   A 1  401 ? 25.824  -51.531  -55.822  1.00 41.12  ? 401 LYS   A N      1 
ATOM   3106  C  CA     . LYS   A 1  401 ? 25.789  -50.943  -54.499  1.00 40.42  ? 401 LYS   A CA     1 
ATOM   3107  C  C      . LYS   A 1  401 ? 26.816  -51.541  -53.556  1.00 35.90  ? 401 LYS   A C      1 
ATOM   3108  O  O      . LYS   A 1  401 ? 26.993  -51.031  -52.452  1.00 42.24  ? 401 LYS   A O      1 
ATOM   3109  C  CB     . LYS   A 1  401 ? 24.389  -51.119  -53.910  1.00 49.41  ? 401 LYS   A CB     1 
ATOM   3110  C  CG     . LYS   A 1  401 ? 23.297  -50.734  -54.881  1.00 49.68  ? 401 LYS   A CG     1 
ATOM   3111  C  CD     . LYS   A 1  401 ? 23.158  -49.226  -54.906  1.00 53.18  ? 401 LYS   A CD     1 
ATOM   3112  C  CE     . LYS   A 1  401 ? 22.047  -48.760  -55.849  1.00 65.35  ? 401 LYS   A CE     1 
ATOM   3113  N  NZ     . LYS   A 1  401 ? 22.347  -49.059  -57.288  1.00 65.14  ? 401 LYS   A NZ     1 
ATOM   3114  N  N      . ARG   A 1  402 ? 27.507  -52.590  -53.963  1.00 39.67  ? 402 ARG   A N      1 
ATOM   3115  C  CA     . ARG   A 1  402 ? 28.418  -53.334  -53.087  1.00 42.56  ? 402 ARG   A CA     1 
ATOM   3116  C  C      . ARG   A 1  402 ? 27.710  -53.874  -51.852  1.00 41.50  ? 402 ARG   A C      1 
ATOM   3117  O  O      . ARG   A 1  402 ? 28.335  -54.051  -50.801  1.00 41.41  ? 402 ARG   A O      1 
ATOM   3118  C  CB     . ARG   A 1  402 ? 29.649  -52.506  -52.695  1.00 45.44  ? 402 ARG   A CB     1 
ATOM   3119  C  CG     . ARG   A 1  402 ? 30.893  -52.866  -53.540  1.00 51.04  ? 402 ARG   A CG     1 
ATOM   3120  C  CD     . ARG   A 1  402 ? 31.863  -51.706  -53.723  1.00 60.23  ? 402 ARG   A CD     1 
ATOM   3121  N  NE     . ARG   A 1  402 ? 32.570  -51.800  -55.001  1.00 59.94  ? 402 ARG   A NE     1 
ATOM   3122  C  CZ     . ARG   A 1  402 ? 31.966  -51.828  -56.186  1.00 56.73  ? 402 ARG   A CZ     1 
ATOM   3123  N  NH1    . ARG   A 1  402 ? 30.646  -51.884  -56.292  1.00 48.91  ? 402 ARG   A NH1    1 
ATOM   3124  N  NH2    . ARG   A 1  402 ? 32.700  -51.805  -57.294  1.00 51.61  ? 402 ARG   A NH2    1 
ATOM   3125  N  N      . ALA   A 1  403 ? 26.423  -54.206  -51.988  1.00 34.54  ? 403 ALA   A N      1 
ATOM   3126  C  CA     . ALA   A 1  403 ? 25.707  -54.826  -50.886  1.00 34.96  ? 403 ALA   A CA     1 
ATOM   3127  C  C      . ALA   A 1  403 ? 26.368  -56.142  -50.496  1.00 35.83  ? 403 ALA   A C      1 
ATOM   3128  O  O      . ALA   A 1  403 ? 26.768  -56.925  -51.353  1.00 36.98  ? 403 ALA   A O      1 
ATOM   3129  C  CB     . ALA   A 1  403 ? 24.244  -55.056  -51.262  1.00 40.31  ? 403 ALA   A CB     1 
ATOM   3130  N  N      . PHE   A 1  404 ? 26.506  -56.370  -49.189  1.00 35.19  ? 404 PHE   A N      1 
ATOM   3131  C  CA     . PHE   A 1  404 ? 27.052  -57.612  -48.649  1.00 33.70  ? 404 PHE   A CA     1 
ATOM   3132  C  C      . PHE   A 1  404 ? 28.552  -57.820  -48.875  1.00 37.76  ? 404 PHE   A C      1 
ATOM   3133  O  O      . PHE   A 1  404 ? 29.161  -58.666  -48.204  1.00 36.71  ? 404 PHE   A O      1 
ATOM   3134  C  CB     . PHE   A 1  404 ? 26.278  -58.786  -49.222  1.00 36.43  ? 404 PHE   A CB     1 
ATOM   3135  C  CG     . PHE   A 1  404 ? 24.838  -58.755  -48.872  1.00 35.88  ? 404 PHE   A CG     1 
ATOM   3136  C  CD1    . PHE   A 1  404 ? 24.418  -59.187  -47.619  1.00 28.26  ? 404 PHE   A CD1    1 
ATOM   3137  C  CD2    . PHE   A 1  404 ? 23.895  -58.282  -49.786  1.00 35.89  ? 404 PHE   A CD2    1 
ATOM   3138  C  CE1    . PHE   A 1  404 ? 23.076  -59.138  -47.281  1.00 34.44  ? 404 PHE   A CE1    1 
ATOM   3139  C  CE2    . PHE   A 1  404 ? 22.542  -58.245  -49.455  1.00 34.73  ? 404 PHE   A CE2    1 
ATOM   3140  C  CZ     . PHE   A 1  404 ? 22.137  -58.666  -48.194  1.00 31.74  ? 404 PHE   A CZ     1 
ATOM   3141  N  N      . VAL   A 1  405 ? 29.164  -57.050  -49.787  1.00 35.72  ? 405 VAL   A N      1 
ATOM   3142  C  CA     . VAL   A 1  405 ? 30.588  -57.219  -50.079  1.00 36.64  ? 405 VAL   A CA     1 
ATOM   3143  C  C      . VAL   A 1  405 ? 31.415  -57.303  -48.792  1.00 38.75  ? 405 VAL   A C      1 
ATOM   3144  O  O      . VAL   A 1  405 ? 32.329  -58.135  -48.671  1.00 42.71  ? 405 VAL   A O      1 
ATOM   3145  C  CB     . VAL   A 1  405 ? 31.076  -56.078  -50.992  1.00 40.02  ? 405 VAL   A CB     1 
ATOM   3146  C  CG1    . VAL   A 1  405 ? 32.570  -56.165  -51.196  1.00 38.26  ? 405 VAL   A CG1    1 
ATOM   3147  C  CG2    . VAL   A 1  405 ? 30.348  -56.109  -52.313  1.00 37.87  ? 405 VAL   A CG2    1 
ATOM   3148  N  N      . HIS   A 1  406 ? 31.119  -56.439  -47.817  1.00 35.23  ? 406 HIS   A N      1 
ATOM   3149  C  CA     . HIS   A 1  406 ? 31.925  -56.395  -46.604  1.00 35.72  ? 406 HIS   A CA     1 
ATOM   3150  C  C      . HIS   A 1  406 ? 32.038  -57.766  -45.939  1.00 39.44  ? 406 HIS   A C      1 
ATOM   3151  O  O      . HIS   A 1  406 ? 33.070  -58.082  -45.338  1.00 42.22  ? 406 HIS   A O      1 
ATOM   3152  C  CB     . HIS   A 1  406 ? 31.351  -55.352  -45.644  1.00 34.65  ? 406 HIS   A CB     1 
ATOM   3153  C  CG     . HIS   A 1  406 ? 30.018  -55.716  -45.078  1.00 40.86  ? 406 HIS   A CG     1 
ATOM   3154  N  ND1    . HIS   A 1  406 ? 29.868  -56.274  -43.823  1.00 38.76  ? 406 HIS   A ND1    1 
ATOM   3155  C  CD2    . HIS   A 1  406 ? 28.774  -55.612  -45.599  1.00 33.95  ? 406 HIS   A CD2    1 
ATOM   3156  C  CE1    . HIS   A 1  406 ? 28.589  -56.505  -43.596  1.00 35.84  ? 406 HIS   A CE1    1 
ATOM   3157  N  NE2    . HIS   A 1  406 ? 27.905  -56.108  -44.656  1.00 41.27  ? 406 HIS   A NE2    1 
ATOM   3158  N  N      . TRP   A 1  407 ? 31.011  -58.601  -46.044  1.00 39.69  ? 407 TRP   A N      1 
ATOM   3159  C  CA     . TRP   A 1  407 ? 31.102  -59.924  -45.443  1.00 40.69  ? 407 TRP   A CA     1 
ATOM   3160  C  C      . TRP   A 1  407 ? 32.240  -60.717  -46.046  1.00 42.10  ? 407 TRP   A C      1 
ATOM   3161  O  O      . TRP   A 1  407 ? 32.856  -61.546  -45.366  1.00 40.69  ? 407 TRP   A O      1 
ATOM   3162  C  CB     . TRP   A 1  407 ? 29.793  -60.675  -45.644  1.00 44.82  ? 407 TRP   A CB     1 
ATOM   3163  C  CG     . TRP   A 1  407 ? 28.743  -60.197  -44.761  1.00 42.82  ? 407 TRP   A CG     1 
ATOM   3164  C  CD1    . TRP   A 1  407 ? 27.625  -59.515  -45.120  1.00 39.50  ? 407 TRP   A CD1    1 
ATOM   3165  C  CD2    . TRP   A 1  407 ? 28.711  -60.323  -43.332  1.00 43.53  ? 407 TRP   A CD2    1 
ATOM   3166  N  NE1    . TRP   A 1  407 ? 26.889  -59.211  -43.994  1.00 45.63  ? 407 TRP   A NE1    1 
ATOM   3167  C  CE2    . TRP   A 1  407 ? 27.534  -59.701  -42.887  1.00 44.00  ? 407 TRP   A CE2    1 
ATOM   3168  C  CE3    . TRP   A 1  407 ? 29.561  -60.910  -42.388  1.00 42.85  ? 407 TRP   A CE3    1 
ATOM   3169  C  CZ2    . TRP   A 1  407 ? 27.179  -59.656  -41.537  1.00 39.15  ? 407 TRP   A CZ2    1 
ATOM   3170  C  CZ3    . TRP   A 1  407 ? 29.203  -60.859  -41.043  1.00 39.49  ? 407 TRP   A CZ3    1 
ATOM   3171  C  CH2    . TRP   A 1  407 ? 28.025  -60.241  -40.637  1.00 38.24  ? 407 TRP   A CH2    1 
ATOM   3172  N  N      . TYR   A 1  408 ? 32.508  -60.485  -47.329  1.00 41.65  ? 408 TYR   A N      1 
ATOM   3173  C  CA     . TYR   A 1  408 ? 33.527  -61.222  -48.063  1.00 44.16  ? 408 TYR   A CA     1 
ATOM   3174  C  C      . TYR   A 1  408 ? 34.916  -60.656  -47.778  1.00 49.56  ? 408 TYR   A C      1 
ATOM   3175  O  O      . TYR   A 1  408 ? 35.830  -61.398  -47.392  1.00 43.02  ? 408 TYR   A O      1 
ATOM   3176  C  CB     . TYR   A 1  408 ? 33.203  -61.171  -49.562  1.00 41.78  ? 408 TYR   A CB     1 
ATOM   3177  C  CG     . TYR   A 1  408 ? 31.923  -61.906  -49.917  1.00 49.54  ? 408 TYR   A CG     1 
ATOM   3178  C  CD1    . TYR   A 1  408 ? 30.656  -61.318  -49.714  1.00 40.96  ? 408 TYR   A CD1    1 
ATOM   3179  C  CD2    . TYR   A 1  408 ? 31.974  -63.202  -50.418  1.00 43.26  ? 408 TYR   A CD2    1 
ATOM   3180  C  CE1    . TYR   A 1  408 ? 29.511  -62.002  -50.014  1.00 35.23  ? 408 TYR   A CE1    1 
ATOM   3181  C  CE2    . TYR   A 1  408 ? 30.838  -63.885  -50.716  1.00 42.23  ? 408 TYR   A CE2    1 
ATOM   3182  C  CZ     . TYR   A 1  408 ? 29.609  -63.299  -50.519  1.00 44.73  ? 408 TYR   A CZ     1 
ATOM   3183  O  OH     . TYR   A 1  408 ? 28.489  -64.044  -50.844  1.00 45.73  ? 408 TYR   A OH     1 
ATOM   3184  N  N      . VAL   A 1  409 ? 35.075  -59.337  -47.965  1.00 44.40  ? 409 VAL   A N      1 
ATOM   3185  C  CA     . VAL   A 1  409 ? 36.334  -58.667  -47.672  1.00 40.99  ? 409 VAL   A CA     1 
ATOM   3186  C  C      . VAL   A 1  409 ? 36.776  -58.996  -46.255  1.00 47.46  ? 409 VAL   A C      1 
ATOM   3187  O  O      . VAL   A 1  409 ? 37.961  -59.247  -45.988  1.00 51.07  ? 409 VAL   A O      1 
ATOM   3188  C  CB     . VAL   A 1  409 ? 36.176  -57.151  -47.891  1.00 42.76  ? 409 VAL   A CB     1 
ATOM   3189  C  CG1    . VAL   A 1  409 ? 37.367  -56.419  -47.351  1.00 34.16  ? 409 VAL   A CG1    1 
ATOM   3190  C  CG2    . VAL   A 1  409 ? 35.948  -56.829  -49.384  1.00 33.17  ? 409 VAL   A CG2    1 
ATOM   3191  N  N      . GLY   A 1  410 ? 35.819  -59.051  -45.331  1.00 47.56  ? 410 GLY   A N      1 
ATOM   3192  C  CA     . GLY   A 1  410 ? 36.085  -59.350  -43.938  1.00 43.47  ? 410 GLY   A CA     1 
ATOM   3193  C  C      . GLY   A 1  410 ? 36.558  -60.754  -43.653  1.00 44.75  ? 410 GLY   A C      1 
ATOM   3194  O  O      . GLY   A 1  410 ? 36.763  -61.097  -42.487  1.00 48.05  ? 410 GLY   A O      1 
ATOM   3195  N  N      . GLU   A 1  411 ? 36.722  -61.590  -44.672  1.00 48.65  ? 411 GLU   A N      1 
ATOM   3196  C  CA     . GLU   A 1  411 ? 37.336  -62.898  -44.495  1.00 50.54  ? 411 GLU   A CA     1 
ATOM   3197  C  C      . GLU   A 1  411 ? 38.674  -63.008  -45.205  1.00 51.82  ? 411 GLU   A C      1 
ATOM   3198  O  O      . GLU   A 1  411 ? 39.314  -64.055  -45.113  1.00 52.80  ? 411 GLU   A O      1 
ATOM   3199  C  CB     . GLU   A 1  411 ? 36.419  -64.028  -44.989  1.00 44.27  ? 411 GLU   A CB     1 
ATOM   3200  C  CG     . GLU   A 1  411 ? 35.068  -64.106  -44.316  1.00 41.54  ? 411 GLU   A CG     1 
ATOM   3201  C  CD     . GLU   A 1  411 ? 35.092  -64.827  -42.980  1.00 49.91  ? 411 GLU   A CD     1 
ATOM   3202  O  OE1    . GLU   A 1  411 ? 36.193  -65.104  -42.446  1.00 57.02  ? 411 GLU   A OE1    1 
ATOM   3203  O  OE2    . GLU   A 1  411 ? 33.996  -65.121  -42.444  1.00 57.93  ? 411 GLU   A OE2    1 
ATOM   3204  N  N      . GLY   A 1  412 ? 39.110  -61.970  -45.910  1.00 39.95  ? 412 GLY   A N      1 
ATOM   3205  C  CA     . GLY   A 1  412 ? 40.320  -62.092  -46.697  1.00 48.18  ? 412 GLY   A CA     1 
ATOM   3206  C  C      . GLY   A 1  412 ? 40.199  -61.588  -48.125  1.00 55.00  ? 412 GLY   A C      1 
ATOM   3207  O  O      . GLY   A 1  412 ? 41.147  -61.023  -48.683  1.00 56.41  ? 412 GLY   A O      1 
ATOM   3208  N  N      . MET   A 1  413 ? 39.035  -61.787  -48.730  1.00 52.87  ? 413 MET   A N      1 
ATOM   3209  C  CA     . MET   A 1  413 ? 38.881  -61.541  -50.152  1.00 46.84  ? 413 MET   A CA     1 
ATOM   3210  C  C      . MET   A 1  413 ? 38.990  -60.044  -50.430  1.00 53.62  ? 413 MET   A C      1 
ATOM   3211  O  O      . MET   A 1  413 ? 38.855  -59.212  -49.528  1.00 56.72  ? 413 MET   A O      1 
ATOM   3212  C  CB     . MET   A 1  413 ? 37.540  -62.093  -50.627  1.00 49.18  ? 413 MET   A CB     1 
ATOM   3213  C  CG     . MET   A 1  413 ? 37.228  -61.897  -52.113  1.00 52.49  ? 413 MET   A CG     1 
ATOM   3214  S  SD     . MET   A 1  413 ? 35.814  -62.915  -52.618  1.00 51.97  ? 413 MET   A SD     1 
ATOM   3215  C  CE     . MET   A 1  413 ? 35.935  -64.260  -51.434  1.00 40.31  ? 413 MET   A CE     1 
ATOM   3216  N  N      . GLU   A 1  414 ? 39.279  -59.702  -51.683  1.00 45.74  ? 414 GLU   A N      1 
ATOM   3217  C  CA     . GLU   A 1  414 ? 39.455  -58.313  -52.070  1.00 47.21  ? 414 GLU   A CA     1 
ATOM   3218  C  C      . GLU   A 1  414 ? 38.379  -57.931  -53.065  1.00 48.60  ? 414 GLU   A C      1 
ATOM   3219  O  O      . GLU   A 1  414 ? 38.085  -58.694  -53.983  1.00 49.18  ? 414 GLU   A O      1 
ATOM   3220  C  CB     . GLU   A 1  414 ? 40.836  -58.072  -52.694  1.00 55.24  ? 414 GLU   A CB     1 
ATOM   3221  C  CG     . GLU   A 1  414 ? 41.963  -58.919  -52.112  1.00 63.09  ? 414 GLU   A CG     1 
ATOM   3222  C  CD     . GLU   A 1  414 ? 43.274  -58.695  -52.833  1.00 69.66  ? 414 GLU   A CD     1 
ATOM   3223  O  OE1    . GLU   A 1  414 ? 43.482  -57.574  -53.340  1.00 67.29  ? 414 GLU   A OE1    1 
ATOM   3224  O  OE2    . GLU   A 1  414 ? 44.081  -59.647  -52.924  1.00 75.80  ? 414 GLU   A OE2    1 
ATOM   3225  N  N      . GLU   A 1  415 ? 37.809  -56.739  -52.908  1.00 45.12  ? 415 GLU   A N      1 
ATOM   3226  C  CA     . GLU   A 1  415 ? 36.819  -56.298  -53.875  1.00 49.12  ? 415 GLU   A CA     1 
ATOM   3227  C  C      . GLU   A 1  415 ? 37.237  -56.684  -55.299  1.00 51.51  ? 415 GLU   A C      1 
ATOM   3228  O  O      . GLU   A 1  415 ? 36.385  -56.861  -56.174  1.00 56.80  ? 415 GLU   A O      1 
ATOM   3229  C  CB     . GLU   A 1  415 ? 36.591  -54.784  -53.760  1.00 46.37  ? 415 GLU   A CB     1 
ATOM   3230  C  CG     . GLU   A 1  415 ? 35.140  -54.419  -53.499  1.00 51.38  ? 415 GLU   A CG     1 
ATOM   3231  C  CD     . GLU   A 1  415 ? 34.884  -52.941  -53.224  1.00 61.74  ? 415 GLU   A CD     1 
ATOM   3232  O  OE1    . GLU   A 1  415 ? 35.069  -52.118  -54.155  1.00 61.79  ? 415 GLU   A OE1    1 
ATOM   3233  O  OE2    . GLU   A 1  415 ? 34.464  -52.604  -52.083  1.00 66.11  ? 415 GLU   A OE2    1 
ATOM   3234  N  N      . GLY   A 1  416 ? 38.536  -56.863  -55.536  1.00 45.82  ? 416 GLY   A N      1 
ATOM   3235  C  CA     . GLY   A 1  416 ? 39.010  -57.135  -56.884  1.00 54.62  ? 416 GLY   A CA     1 
ATOM   3236  C  C      . GLY   A 1  416 ? 38.552  -58.470  -57.433  1.00 51.03  ? 416 GLY   A C      1 
ATOM   3237  O  O      . GLY   A 1  416 ? 38.121  -58.543  -58.586  1.00 48.81  ? 416 GLY   A O      1 
ATOM   3238  N  N      . GLU   A 1  417 ? 38.631  -59.538  -56.616  1.00 42.71  ? 417 GLU   A N      1 
ATOM   3239  C  CA     . GLU   A 1  417 ? 38.143  -60.853  -57.026  1.00 47.27  ? 417 GLU   A CA     1 
ATOM   3240  C  C      . GLU   A 1  417 ? 36.678  -60.811  -57.479  1.00 54.01  ? 417 GLU   A C      1 
ATOM   3241  O  O      . GLU   A 1  417 ? 36.258  -61.643  -58.293  1.00 54.52  ? 417 GLU   A O      1 
ATOM   3242  C  CB     . GLU   A 1  417 ? 38.330  -61.851  -55.887  1.00 40.58  ? 417 GLU   A CB     1 
ATOM   3243  C  CG     . GLU   A 1  417 ? 37.979  -63.301  -56.257  1.00 39.29  ? 417 GLU   A CG     1 
ATOM   3244  C  CD     . GLU   A 1  417 ? 38.550  -64.297  -55.247  1.00 45.52  ? 417 GLU   A CD     1 
ATOM   3245  O  OE1    . GLU   A 1  417 ? 39.143  -63.826  -54.242  1.00 42.94  ? 417 GLU   A OE1    1 
ATOM   3246  O  OE2    . GLU   A 1  417 ? 38.441  -65.539  -55.469  1.00 48.85  ? 417 GLU   A OE2    1 
ATOM   3247  N  N      . PHE   A 1  418 ? 35.894  -59.852  -56.978  1.00 50.74  ? 418 PHE   A N      1 
ATOM   3248  C  CA     . PHE   A 1  418 ? 34.514  -59.695  -57.427  1.00 50.02  ? 418 PHE   A CA     1 
ATOM   3249  C  C      . PHE   A 1  418 ? 34.458  -59.269  -58.894  1.00 50.32  ? 418 PHE   A C      1 
ATOM   3250  O  O      . PHE   A 1  418 ? 33.733  -59.857  -59.697  1.00 47.44  ? 418 PHE   A O      1 
ATOM   3251  C  CB     . PHE   A 1  418 ? 33.800  -58.661  -56.545  1.00 51.20  ? 418 PHE   A CB     1 
ATOM   3252  C  CG     . PHE   A 1  418 ? 33.139  -59.231  -55.310  1.00 50.06  ? 418 PHE   A CG     1 
ATOM   3253  C  CD1    . PHE   A 1  418 ? 31.834  -59.705  -55.347  1.00 48.93  ? 418 PHE   A CD1    1 
ATOM   3254  C  CD2    . PHE   A 1  418 ? 33.832  -59.294  -54.101  1.00 55.74  ? 418 PHE   A CD2    1 
ATOM   3255  C  CE1    . PHE   A 1  418 ? 31.234  -60.232  -54.192  1.00 47.63  ? 418 PHE   A CE1    1 
ATOM   3256  C  CE2    . PHE   A 1  418 ? 33.237  -59.821  -52.941  1.00 49.90  ? 418 PHE   A CE2    1 
ATOM   3257  C  CZ     . PHE   A 1  418 ? 31.941  -60.295  -52.995  1.00 45.37  ? 418 PHE   A CZ     1 
ATOM   3258  N  N      . SER   A 1  419 ? 35.182  -58.212  -59.255  1.00 55.65  ? 419 SER   A N      1 
ATOM   3259  C  CA     . SER   A 1  419 ? 35.143  -57.744  -60.638  1.00 51.13  ? 419 SER   A CA     1 
ATOM   3260  C  C      . SER   A 1  419 ? 35.947  -58.650  -61.543  1.00 51.61  ? 419 SER   A C      1 
ATOM   3261  O  O      . SER   A 1  419 ? 35.701  -58.701  -62.751  1.00 56.71  ? 419 SER   A O      1 
ATOM   3262  C  CB     . SER   A 1  419 ? 35.695  -56.332  -60.728  1.00 44.07  ? 419 SER   A CB     1 
ATOM   3263  O  OG     . SER   A 1  419 ? 36.785  -56.236  -59.824  1.00 59.27  ? 419 SER   A OG     1 
ATOM   3264  N  N      . GLU   A 1  420 ? 36.925  -59.350  -60.990  1.00 48.14  ? 420 GLU   A N      1 
ATOM   3265  C  CA     . GLU   A 1  420 ? 37.664  -60.283  -61.813  1.00 54.17  ? 420 GLU   A CA     1 
ATOM   3266  C  C      . GLU   A 1  420 ? 36.772  -61.464  -62.181  1.00 56.36  ? 420 GLU   A C      1 
ATOM   3267  O  O      . GLU   A 1  420 ? 36.627  -61.795  -63.366  1.00 57.35  ? 420 GLU   A O      1 
ATOM   3268  C  CB     . GLU   A 1  420 ? 38.936  -60.696  -61.076  1.00 50.21  ? 420 GLU   A CB     1 
ATOM   3269  C  CG     . GLU   A 1  420 ? 39.709  -61.828  -61.651  1.00 60.43  ? 420 GLU   A CG     1 
ATOM   3270  C  CD     . GLU   A 1  420 ? 40.807  -62.248  -60.697  1.00 71.74  ? 420 GLU   A CD     1 
ATOM   3271  O  OE1    . GLU   A 1  420 ? 41.415  -61.332  -60.086  1.00 66.82  ? 420 GLU   A OE1    1 
ATOM   3272  O  OE2    . GLU   A 1  420 ? 41.007  -63.481  -60.512  1.00 65.40  ? 420 GLU   A OE2    1 
ATOM   3273  N  N      . ALA   A 1  421 ? 36.105  -62.057  -61.179  1.00 50.07  ? 421 ALA   A N      1 
ATOM   3274  C  CA     . ALA   A 1  421 ? 35.167  -63.142  -61.438  1.00 46.78  ? 421 ALA   A CA     1 
ATOM   3275  C  C      . ALA   A 1  421 ? 34.041  -62.704  -62.381  1.00 49.04  ? 421 ALA   A C      1 
ATOM   3276  O  O      . ALA   A 1  421 ? 33.614  -63.482  -63.244  1.00 48.98  ? 421 ALA   A O      1 
ATOM   3277  C  CB     . ALA   A 1  421 ? 34.617  -63.675  -60.112  1.00 42.12  ? 421 ALA   A CB     1 
ATOM   3278  N  N      . ARG   A 1  422 ? 33.562  -61.461  -62.254  1.00 40.64  ? 422 ARG   A N      1 
ATOM   3279  C  CA     . ARG   A 1  422 ? 32.507  -60.972  -63.139  1.00 43.27  ? 422 ARG   A CA     1 
ATOM   3280  C  C      . ARG   A 1  422 ? 32.995  -60.723  -64.563  1.00 49.54  ? 422 ARG   A C      1 
ATOM   3281  O  O      . ARG   A 1  422 ? 32.193  -60.738  -65.502  1.00 50.55  ? 422 ARG   A O      1 
ATOM   3282  C  CB     . ARG   A 1  422 ? 31.923  -59.684  -62.593  1.00 44.68  ? 422 ARG   A CB     1 
ATOM   3283  C  CG     . ARG   A 1  422 ? 30.774  -59.130  -63.409  1.00 37.92  ? 422 ARG   A CG     1 
ATOM   3284  C  CD     . ARG   A 1  422 ? 29.568  -60.026  -63.368  1.00 37.19  ? 422 ARG   A CD     1 
ATOM   3285  N  NE     . ARG   A 1  422 ? 28.516  -59.489  -64.217  1.00 39.53  ? 422 ARG   A NE     1 
ATOM   3286  C  CZ     . ARG   A 1  422 ? 28.431  -59.678  -65.530  1.00 45.50  ? 422 ARG   A CZ     1 
ATOM   3287  N  NH1    . ARG   A 1  422 ? 29.303  -60.440  -66.183  1.00 44.63  ? 422 ARG   A NH1    1 
ATOM   3288  N  NH2    . ARG   A 1  422 ? 27.432  -59.111  -66.202  1.00 32.34  ? 422 ARG   A NH2    1 
ATOM   3289  N  N      . GLU   A 1  423 ? 34.280  -60.435  -64.744  1.00 54.78  ? 423 GLU   A N      1 
ATOM   3290  C  CA     . GLU   A 1  423 ? 34.792  -60.219  -66.093  1.00 56.18  ? 423 GLU   A CA     1 
ATOM   3291  C  C      . GLU   A 1  423 ? 34.975  -61.542  -66.822  1.00 52.50  ? 423 GLU   A C      1 
ATOM   3292  O  O      . GLU   A 1  423 ? 34.731  -61.628  -68.034  1.00 46.91  ? 423 GLU   A O      1 
ATOM   3293  C  CB     . GLU   A 1  423 ? 36.109  -59.445  -66.046  1.00 56.12  ? 423 GLU   A CB     1 
ATOM   3294  C  CG     . GLU   A 1  423 ? 35.983  -57.986  -66.461  1.00 59.89  ? 423 GLU   A CG     1 
ATOM   3295  C  CD     . GLU   A 1  423 ? 34.934  -57.780  -67.542  1.00 66.90  ? 423 GLU   A CD     1 
ATOM   3296  O  OE1    . GLU   A 1  423 ? 35.091  -58.379  -68.631  1.00 69.80  ? 423 GLU   A OE1    1 
ATOM   3297  O  OE2    . GLU   A 1  423 ? 33.955  -57.032  -67.306  1.00 62.38  ? 423 GLU   A OE2    1 
ATOM   3298  N  N      . ASP   A 1  424 ? 35.433  -62.567  -66.100  1.00 46.68  ? 424 ASP   A N      1 
ATOM   3299  C  CA     . ASP   A 1  424 ? 35.431  -63.919  -66.637  1.00 45.24  ? 424 ASP   A CA     1 
ATOM   3300  C  C      . ASP   A 1  424 ? 34.041  -64.260  -67.159  1.00 51.94  ? 424 ASP   A C      1 
ATOM   3301  O  O      . ASP   A 1  424 ? 33.860  -64.568  -68.343  1.00 51.94  ? 424 ASP   A O      1 
ATOM   3302  C  CB     . ASP   A 1  424 ? 35.888  -64.897  -65.549  1.00 48.53  ? 424 ASP   A CB     1 
ATOM   3303  C  CG     . ASP   A 1  424 ? 36.555  -66.135  -66.114  1.00 55.28  ? 424 ASP   A CG     1 
ATOM   3304  O  OD1    . ASP   A 1  424 ? 36.569  -66.251  -67.357  1.00 55.42  ? 424 ASP   A OD1    1 
ATOM   3305  O  OD2    . ASP   A 1  424 ? 37.050  -66.991  -65.324  1.00 52.33  ? 424 ASP   A OD2    1 
ATOM   3306  N  N      . MET   A 1  425 ? 33.031  -64.147  -66.287  1.00 51.38  ? 425 MET   A N      1 
ATOM   3307  C  CA     . MET   A 1  425 ? 31.645  -64.353  -66.693  1.00 46.88  ? 425 MET   A CA     1 
ATOM   3308  C  C      . MET   A 1  425 ? 31.296  -63.523  -67.923  1.00 50.88  ? 425 MET   A C      1 
ATOM   3309  O  O      . MET   A 1  425 ? 30.586  -63.994  -68.818  1.00 54.75  ? 425 MET   A O      1 
ATOM   3310  C  CB     . MET   A 1  425 ? 30.711  -64.002  -65.538  1.00 46.66  ? 425 MET   A CB     1 
ATOM   3311  C  CG     . MET   A 1  425 ? 30.969  -64.816  -64.298  1.00 45.34  ? 425 MET   A CG     1 
ATOM   3312  S  SD     . MET   A 1  425 ? 30.960  -66.569  -64.686  1.00 54.25  ? 425 MET   A SD     1 
ATOM   3313  C  CE     . MET   A 1  425 ? 29.379  -66.675  -65.533  1.00 44.24  ? 425 MET   A CE     1 
ATOM   3314  N  N      . ALA   A 1  426 ? 31.765  -62.273  -67.976  1.00 51.21  ? 426 ALA   A N      1 
ATOM   3315  C  CA     . ALA   A 1  426 ? 31.523  -61.457  -69.162  1.00 54.12  ? 426 ALA   A CA     1 
ATOM   3316  C  C      . ALA   A 1  426 ? 32.245  -62.032  -70.374  1.00 57.80  ? 426 ALA   A C      1 
ATOM   3317  O  O      . ALA   A 1  426 ? 31.706  -62.031  -71.487  1.00 57.10  ? 426 ALA   A O      1 
ATOM   3318  C  CB     . ALA   A 1  426 ? 31.952  -60.017  -68.912  1.00 47.55  ? 426 ALA   A CB     1 
ATOM   3319  N  N      . ALA   A 1  427 ? 33.466  -62.530  -70.179  1.00 53.59  ? 427 ALA   A N      1 
ATOM   3320  C  CA     . ALA   A 1  427 ? 34.110  -63.301  -71.232  1.00 52.93  ? 427 ALA   A CA     1 
ATOM   3321  C  C      . ALA   A 1  427 ? 33.254  -64.497  -71.625  1.00 56.23  ? 427 ALA   A C      1 
ATOM   3322  O  O      . ALA   A 1  427 ? 33.055  -64.768  -72.815  1.00 55.22  ? 427 ALA   A O      1 
ATOM   3323  C  CB     . ALA   A 1  427 ? 35.495  -63.767  -70.781  1.00 47.73  ? 427 ALA   A CB     1 
ATOM   3324  N  N      . LEU   A 1  428 ? 32.724  -65.220  -70.632  1.00 53.87  ? 428 LEU   A N      1 
ATOM   3325  C  CA     . LEU   A 1  428 ? 31.973  -66.437  -70.927  1.00 52.33  ? 428 LEU   A CA     1 
ATOM   3326  C  C      . LEU   A 1  428 ? 30.737  -66.150  -71.769  1.00 50.24  ? 428 LEU   A C      1 
ATOM   3327  O  O      . LEU   A 1  428 ? 30.425  -66.910  -72.689  1.00 56.13  ? 428 LEU   A O      1 
ATOM   3328  C  CB     . LEU   A 1  428 ? 31.581  -67.157  -69.640  1.00 45.36  ? 428 LEU   A CB     1 
ATOM   3329  C  CG     . LEU   A 1  428 ? 31.130  -68.580  -69.934  1.00 43.68  ? 428 LEU   A CG     1 
ATOM   3330  C  CD1    . LEU   A 1  428 ? 32.249  -69.301  -70.601  1.00 49.34  ? 428 LEU   A CD1    1 
ATOM   3331  C  CD2    . LEU   A 1  428 ? 30.742  -69.300  -68.657  1.00 48.58  ? 428 LEU   A CD2    1 
ATOM   3332  N  N      . GLU   A 1  429 ? 30.009  -65.070  -71.470  1.00 51.42  ? 429 GLU   A N      1 
ATOM   3333  C  CA     . GLU   A 1  429 ? 28.781  -64.781  -72.214  1.00 54.37  ? 429 GLU   A CA     1 
ATOM   3334  C  C      . GLU   A 1  429 ? 29.073  -64.343  -73.636  1.00 59.45  ? 429 GLU   A C      1 
ATOM   3335  O  O      . GLU   A 1  429 ? 28.209  -64.476  -74.511  1.00 60.94  ? 429 GLU   A O      1 
ATOM   3336  C  CB     . GLU   A 1  429 ? 27.963  -63.687  -71.520  1.00 50.73  ? 429 GLU   A CB     1 
ATOM   3337  C  CG     . GLU   A 1  429 ? 27.196  -64.152  -70.299  1.00 46.78  ? 429 GLU   A CG     1 
ATOM   3338  C  CD     . GLU   A 1  429 ? 26.221  -63.099  -69.793  1.00 56.96  ? 429 GLU   A CD     1 
ATOM   3339  O  OE1    . GLU   A 1  429 ? 25.326  -62.689  -70.581  1.00 55.80  ? 429 GLU   A OE1    1 
ATOM   3340  O  OE2    . GLU   A 1  429 ? 26.342  -62.699  -68.604  1.00 51.85  ? 429 GLU   A OE2    1 
ATOM   3341  N  N      . LYS   A 1  430 ? 30.264  -63.799  -73.861  1.00 57.17  ? 430 LYS   A N      1 
ATOM   3342  C  CA     . LYS   A 1  430 ? 30.709  -63.384  -75.178  1.00 56.48  ? 430 LYS   A CA     1 
ATOM   3343  C  C      . LYS   A 1  430 ? 31.118  -64.600  -76.007  1.00 56.15  ? 430 LYS   A C      1 
ATOM   3344  O  O      . LYS   A 1  430 ? 30.696  -64.738  -77.157  1.00 59.38  ? 430 LYS   A O      1 
ATOM   3345  C  CB     . LYS   A 1  430 ? 31.865  -62.384  -75.017  1.00 63.88  ? 430 LYS   A CB     1 
ATOM   3346  C  CG     . LYS   A 1  430 ? 31.904  -61.223  -76.000  1.00 64.06  ? 430 LYS   A CG     1 
ATOM   3347  C  CD     . LYS   A 1  430 ? 33.149  -60.342  -75.764  1.00 71.31  ? 430 LYS   A CD     1 
ATOM   3348  C  CE     . LYS   A 1  430 ? 33.762  -59.845  -77.078  1.00 73.27  ? 430 LYS   A CE     1 
ATOM   3349  N  NZ     . LYS   A 1  430 ? 34.501  -60.938  -77.781  1.00 75.19  ? 430 LYS   A NZ     1 
ATOM   3350  N  N      . ASP   A 1  431 ? 31.924  -65.502  -75.428  1.00 55.28  ? 431 ASP   A N      1 
ATOM   3351  C  CA     . ASP   A 1  431 ? 32.191  -66.798  -76.055  1.00 55.78  ? 431 ASP   A CA     1 
ATOM   3352  C  C      . ASP   A 1  431 ? 30.899  -67.426  -76.564  1.00 58.18  ? 431 ASP   A C      1 
ATOM   3353  O  O      . ASP   A 1  431 ? 30.739  -67.692  -77.759  1.00 59.88  ? 431 ASP   A O      1 
ATOM   3354  C  CB     . ASP   A 1  431 ? 32.866  -67.764  -75.071  1.00 53.85  ? 431 ASP   A CB     1 
ATOM   3355  C  CG     . ASP   A 1  431 ? 34.226  -67.282  -74.578  1.00 61.78  ? 431 ASP   A CG     1 
ATOM   3356  O  OD1    . ASP   A 1  431 ? 34.798  -66.323  -75.159  1.00 62.37  ? 431 ASP   A OD1    1 
ATOM   3357  O  OD2    . ASP   A 1  431 ? 34.741  -67.904  -73.615  1.00 61.49  ? 431 ASP   A OD2    1 
ATOM   3358  N  N      . TYR   A 1  432 ? 29.962  -67.681  -75.655  1.00 55.84  ? 432 TYR   A N      1 
ATOM   3359  C  CA     . TYR   A 1  432 ? 28.692  -68.252  -76.071  1.00 55.89  ? 432 TYR   A CA     1 
ATOM   3360  C  C      . TYR   A 1  432 ? 28.104  -67.468  -77.232  1.00 55.53  ? 432 TYR   A C      1 
ATOM   3361  O  O      . TYR   A 1  432 ? 27.792  -68.036  -78.279  1.00 64.20  ? 432 TYR   A O      1 
ATOM   3362  C  CB     . TYR   A 1  432 ? 27.715  -68.286  -74.900  1.00 54.45  ? 432 TYR   A CB     1 
ATOM   3363  C  CG     . TYR   A 1  432 ? 27.810  -69.505  -74.016  1.00 47.78  ? 432 TYR   A CG     1 
ATOM   3364  C  CD1    . TYR   A 1  432 ? 27.213  -70.700  -74.377  1.00 47.55  ? 432 TYR   A CD1    1 
ATOM   3365  C  CD2    . TYR   A 1  432 ? 28.473  -69.447  -72.799  1.00 49.05  ? 432 TYR   A CD2    1 
ATOM   3366  C  CE1    . TYR   A 1  432 ? 27.279  -71.800  -73.552  1.00 47.02  ? 432 TYR   A CE1    1 
ATOM   3367  C  CE2    . TYR   A 1  432 ? 28.539  -70.540  -71.962  1.00 45.55  ? 432 TYR   A CE2    1 
ATOM   3368  C  CZ     . TYR   A 1  432 ? 27.944  -71.716  -72.341  1.00 46.18  ? 432 TYR   A CZ     1 
ATOM   3369  O  OH     . TYR   A 1  432 ? 28.023  -72.821  -71.512  1.00 49.97  ? 432 TYR   A OH     1 
ATOM   3370  N  N      . GLU   A 1  433 ? 27.964  -66.154  -77.079  1.00 61.84  ? 433 GLU   A N      1 
ATOM   3371  C  CA     . GLU   A 1  433 ? 27.253  -65.396  -78.108  1.00 63.59  ? 433 GLU   A CA     1 
ATOM   3372  C  C      . GLU   A 1  433 ? 27.974  -65.441  -79.446  1.00 61.18  ? 433 GLU   A C      1 
ATOM   3373  O  O      . GLU   A 1  433 ? 27.318  -65.414  -80.494  1.00 65.01  ? 433 GLU   A O      1 
ATOM   3374  C  CB     . GLU   A 1  433 ? 27.042  -63.945  -77.689  1.00 63.46  ? 433 GLU   A CB     1 
ATOM   3375  C  CG     . GLU   A 1  433 ? 26.188  -63.200  -78.695  1.00 69.00  ? 433 GLU   A CG     1 
ATOM   3376  C  CD     . GLU   A 1  433 ? 25.114  -62.337  -78.073  1.00 82.44  ? 433 GLU   A CD     1 
ATOM   3377  O  OE1    . GLU   A 1  433 ? 25.282  -61.901  -76.909  1.00 85.10  ? 433 GLU   A OE1    1 
ATOM   3378  O  OE2    . GLU   A 1  433 ? 24.086  -62.112  -78.754  1.00 86.54  ? 433 GLU   A OE2    1 
ATOM   3379  N  N      . GLU   A 1  434 ? 29.309  -65.500  -79.440  1.00 59.78  ? 434 GLU   A N      1 
ATOM   3380  C  CA     . GLU   A 1  434 ? 30.041  -65.706  -80.689  1.00 64.50  ? 434 GLU   A CA     1 
ATOM   3381  C  C      . GLU   A 1  434 ? 29.553  -66.976  -81.376  1.00 66.00  ? 434 GLU   A C      1 
ATOM   3382  O  O      . GLU   A 1  434 ? 28.980  -66.931  -82.472  1.00 65.33  ? 434 GLU   A O      1 
ATOM   3383  C  CB     . GLU   A 1  434 ? 31.559  -65.778  -80.431  1.00 59.77  ? 434 GLU   A CB     1 
ATOM   3384  C  CG     . GLU   A 1  434 ? 32.358  -64.535  -80.843  1.00 62.84  ? 434 GLU   A CG     1 
ATOM   3385  C  CD     . GLU   A 1  434 ? 33.550  -64.238  -79.906  1.00 85.18  ? 434 GLU   A CD     1 
ATOM   3386  O  OE1    . GLU   A 1  434 ? 34.274  -65.190  -79.514  1.00 82.57  ? 434 GLU   A OE1    1 
ATOM   3387  O  OE2    . GLU   A 1  434 ? 33.760  -63.050  -79.546  1.00 81.36  ? 434 GLU   A OE2    1 
ATOM   3388  N  N      . VAL   A 1  435 ? 29.741  -68.119  -80.704  1.00 57.61  ? 435 VAL   A N      1 
ATOM   3389  C  CA     . VAL   A 1  435 ? 29.375  -69.425  -81.239  1.00 54.17  ? 435 VAL   A CA     1 
ATOM   3390  C  C      . VAL   A 1  435 ? 27.933  -69.466  -81.744  1.00 62.25  ? 435 VAL   A C      1 
ATOM   3391  O  O      . VAL   A 1  435 ? 27.629  -70.155  -82.727  1.00 69.03  ? 435 VAL   A O      1 
ATOM   3392  C  CB     . VAL   A 1  435 ? 29.643  -70.502  -80.165  1.00 54.54  ? 435 VAL   A CB     1 
ATOM   3393  C  CG1    . VAL   A 1  435 ? 29.440  -71.894  -80.724  1.00 54.11  ? 435 VAL   A CG1    1 
ATOM   3394  C  CG2    . VAL   A 1  435 ? 31.065  -70.363  -79.611  1.00 46.32  ? 435 VAL   A CG2    1 
ATOM   3395  N  N      . GLY   A 1  436 ? 27.029  -68.730  -81.110  1.00 63.51  ? 436 GLY   A N      1 
ATOM   3396  C  CA     . GLY   A 1  436 ? 25.623  -68.874  -81.440  1.00 65.54  ? 436 GLY   A CA     1 
ATOM   3397  C  C      . GLY   A 1  436 ? 24.982  -67.745  -82.219  1.00 75.14  ? 436 GLY   A C      1 
ATOM   3398  O  O      . GLY   A 1  436 ? 23.828  -67.391  -81.953  1.00 81.97  ? 436 GLY   A O      1 
ATOM   3399  N  N      . VAL   A 1  437 ? 25.694  -67.171  -83.185  1.00 80.89  ? 437 VAL   A N      1 
ATOM   3400  C  CA     . VAL   A 1  437 ? 25.064  -66.211  -84.094  1.00 81.18  ? 437 VAL   A CA     1 
ATOM   3401  C  C      . VAL   A 1  437 ? 25.613  -66.278  -85.518  1.00 86.81  ? 437 VAL   A C      1 
ATOM   3402  O  O      . VAL   A 1  437 ? 24.860  -66.102  -86.485  1.00 89.06  ? 437 VAL   A O      1 
ATOM   3403  C  CB     . VAL   A 1  437 ? 25.188  -64.799  -83.561  1.00 75.84  ? 437 VAL   A CB     1 
ATOM   3404  C  CG1    . VAL   A 1  437 ? 25.015  -63.810  -84.709  1.00 86.57  ? 437 VAL   A CG1    1 
ATOM   3405  C  CG2    . VAL   A 1  437 ? 24.135  -64.573  -82.477  1.00 68.21  ? 437 VAL   A CG2    1 
ATOM   3406  N  N      . ARG   B 2  2   ? 25.720  -75.590  -31.401  1.00 57.15  ? 2   ARG   B N      1 
ATOM   3407  C  CA     . ARG   B 2  2   ? 25.928  -74.147  -31.543  1.00 53.76  ? 2   ARG   B CA     1 
ATOM   3408  C  C      . ARG   B 2  2   ? 25.190  -73.445  -30.388  1.00 59.71  ? 2   ARG   B C      1 
ATOM   3409  O  O      . ARG   B 2  2   ? 23.986  -73.143  -30.469  1.00 52.90  ? 2   ARG   B O      1 
ATOM   3410  C  CB     . ARG   B 2  2   ? 25.451  -73.619  -32.910  1.00 46.02  ? 2   ARG   B CB     1 
ATOM   3411  C  CG     . ARG   B 2  2   ? 26.222  -74.107  -34.144  1.00 51.41  ? 2   ARG   B CG     1 
ATOM   3412  C  CD     . ARG   B 2  2   ? 27.420  -73.246  -34.563  1.00 51.19  ? 2   ARG   B CD     1 
ATOM   3413  N  NE     . ARG   B 2  2   ? 27.014  -71.871  -34.850  1.00 55.74  ? 2   ARG   B NE     1 
ATOM   3414  C  CZ     . ARG   B 2  2   ? 27.795  -70.901  -35.320  1.00 49.14  ? 2   ARG   B CZ     1 
ATOM   3415  N  NH1    . ARG   B 2  2   ? 28.969  -71.157  -35.858  1.00 52.09  ? 2   ARG   B NH1    1 
ATOM   3416  N  NH2    . ARG   B 2  2   ? 27.389  -69.634  -35.229  1.00 47.86  ? 2   ARG   B NH2    1 
ATOM   3417  N  N      . GLU   B 2  3   ? 25.926  -73.201  -29.302  1.00 61.13  ? 3   GLU   B N      1 
ATOM   3418  C  CA     . GLU   B 2  3   ? 25.367  -72.564  -28.123  1.00 53.72  ? 3   GLU   B CA     1 
ATOM   3419  C  C      . GLU   B 2  3   ? 25.342  -71.050  -28.283  1.00 54.74  ? 3   GLU   B C      1 
ATOM   3420  O  O      . GLU   B 2  3   ? 26.183  -70.458  -28.969  1.00 47.18  ? 3   GLU   B O      1 
ATOM   3421  C  CB     . GLU   B 2  3   ? 26.167  -72.934  -26.884  1.00 55.31  ? 3   GLU   B CB     1 
ATOM   3422  C  CG     . GLU   B 2  3   ? 26.098  -74.404  -26.534  1.00 60.27  ? 3   GLU   B CG     1 
ATOM   3423  C  CD     . GLU   B 2  3   ? 27.193  -75.216  -27.193  1.00 60.70  ? 3   GLU   B CD     1 
ATOM   3424  O  OE1    . GLU   B 2  3   ? 27.880  -74.687  -28.096  1.00 57.92  ? 3   GLU   B OE1    1 
ATOM   3425  O  OE2    . GLU   B 2  3   ? 27.375  -76.382  -26.791  1.00 63.48  ? 3   GLU   B OE2    1 
ATOM   3426  N  N      . ILE   B 2  4   ? 24.326  -70.441  -27.663  1.00 57.33  ? 4   ILE   B N      1 
ATOM   3427  C  CA     . ILE   B 2  4   ? 24.164  -68.996  -27.543  1.00 49.47  ? 4   ILE   B CA     1 
ATOM   3428  C  C      . ILE   B 2  4   ? 24.288  -68.655  -26.069  1.00 45.33  ? 4   ILE   B C      1 
ATOM   3429  O  O      . ILE   B 2  4   ? 23.848  -69.432  -25.218  1.00 48.69  ? 4   ILE   B O      1 
ATOM   3430  C  CB     . ILE   B 2  4   ? 22.800  -68.524  -28.083  1.00 45.34  ? 4   ILE   B CB     1 
ATOM   3431  C  CG1    . ILE   B 2  4   ? 22.722  -68.691  -29.593  1.00 42.12  ? 4   ILE   B CG1    1 
ATOM   3432  C  CG2    . ILE   B 2  4   ? 22.541  -67.077  -27.674  1.00 42.51  ? 4   ILE   B CG2    1 
ATOM   3433  C  CD1    . ILE   B 2  4   ? 21.425  -68.210  -30.207  1.00 40.34  ? 4   ILE   B CD1    1 
ATOM   3434  N  N      . VAL   B 2  5   ? 24.890  -67.507  -25.761  1.00 48.99  ? 5   VAL   B N      1 
ATOM   3435  C  CA     . VAL   B 2  5   ? 25.037  -67.043  -24.375  1.00 48.56  ? 5   VAL   B CA     1 
ATOM   3436  C  C      . VAL   B 2  5   ? 24.183  -65.800  -24.199  1.00 45.41  ? 5   VAL   B C      1 
ATOM   3437  O  O      . VAL   B 2  5   ? 24.396  -64.776  -24.868  1.00 44.14  ? 5   VAL   B O      1 
ATOM   3438  C  CB     . VAL   B 2  5   ? 26.502  -66.764  -23.996  1.00 47.16  ? 5   VAL   B CB     1 
ATOM   3439  C  CG1    . VAL   B 2  5   ? 26.578  -66.267  -22.573  1.00 40.09  ? 5   VAL   B CG1    1 
ATOM   3440  C  CG2    . VAL   B 2  5   ? 27.374  -68.031  -24.178  1.00 43.79  ? 5   VAL   B CG2    1 
ATOM   3441  N  N      . HIS   B 2  6   ? 23.209  -65.895  -23.309  1.00 45.39  ? 6   HIS   B N      1 
ATOM   3442  C  CA     . HIS   B 2  6   ? 22.254  -64.823  -23.081  1.00 47.41  ? 6   HIS   B CA     1 
ATOM   3443  C  C      . HIS   B 2  6   ? 22.697  -63.969  -21.889  1.00 46.78  ? 6   HIS   B C      1 
ATOM   3444  O  O      . HIS   B 2  6   ? 23.177  -64.485  -20.874  1.00 45.26  ? 6   HIS   B O      1 
ATOM   3445  C  CB     . HIS   B 2  6   ? 20.856  -65.418  -22.863  1.00 46.52  ? 6   HIS   B CB     1 
ATOM   3446  C  CG     . HIS   B 2  6   ? 19.865  -64.466  -22.265  1.00 52.01  ? 6   HIS   B CG     1 
ATOM   3447  N  ND1    . HIS   B 2  6   ? 19.148  -63.555  -23.018  1.00 49.15  ? 6   HIS   B ND1    1 
ATOM   3448  C  CD2    . HIS   B 2  6   ? 19.461  -64.299  -20.981  1.00 45.68  ? 6   HIS   B CD2    1 
ATOM   3449  C  CE1    . HIS   B 2  6   ? 18.358  -62.861  -22.218  1.00 49.22  ? 6   HIS   B CE1    1 
ATOM   3450  N  NE2    . HIS   B 2  6   ? 18.527  -63.294  -20.978  1.00 45.35  ? 6   HIS   B NE2    1 
ATOM   3451  N  N      . ILE   B 2  7   ? 22.549  -62.659  -22.028  1.00 43.36  ? 7   ILE   B N      1 
ATOM   3452  C  CA     . ILE   B 2  7   ? 22.898  -61.714  -20.980  1.00 43.20  ? 7   ILE   B CA     1 
ATOM   3453  C  C      . ILE   B 2  7   ? 21.790  -60.681  -20.892  1.00 41.35  ? 7   ILE   B C      1 
ATOM   3454  O  O      . ILE   B 2  7   ? 21.406  -60.096  -21.907  1.00 45.03  ? 7   ILE   B O      1 
ATOM   3455  C  CB     . ILE   B 2  7   ? 24.243  -61.040  -21.292  1.00 47.02  ? 7   ILE   B CB     1 
ATOM   3456  C  CG1    . ILE   B 2  7   ? 25.353  -62.083  -21.321  1.00 42.98  ? 7   ILE   B CG1    1 
ATOM   3457  C  CG2    . ILE   B 2  7   ? 24.541  -59.957  -20.296  1.00 41.84  ? 7   ILE   B CG2    1 
ATOM   3458  C  CD1    . ILE   B 2  7   ? 26.644  -61.514  -21.761  1.00 40.70  ? 7   ILE   B CD1    1 
ATOM   3459  N  N      . GLN   B 2  8   ? 21.278  -60.445  -19.693  1.00 44.20  ? 8   GLN   B N      1 
ATOM   3460  C  CA     . GLN   B 2  8   ? 20.255  -59.427  -19.478  1.00 41.08  ? 8   GLN   B CA     1 
ATOM   3461  C  C      . GLN   B 2  8   ? 20.721  -58.476  -18.390  1.00 41.15  ? 8   GLN   B C      1 
ATOM   3462  O  O      . GLN   B 2  8   ? 21.150  -58.926  -17.324  1.00 41.63  ? 8   GLN   B O      1 
ATOM   3463  C  CB     . GLN   B 2  8   ? 18.940  -60.065  -19.079  1.00 42.01  ? 8   GLN   B CB     1 
ATOM   3464  C  CG     . GLN   B 2  8   ? 19.047  -60.944  -17.847  1.00 42.11  ? 8   GLN   B CG     1 
ATOM   3465  C  CD     . GLN   B 2  8   ? 17.828  -61.820  -17.715  1.00 44.93  ? 8   GLN   B CD     1 
ATOM   3466  O  OE1    . GLN   B 2  8   ? 17.495  -62.587  -18.631  1.00 38.80  ? 8   GLN   B OE1    1 
ATOM   3467  N  NE2    . GLN   B 2  8   ? 17.128  -61.686  -16.604  1.00 42.30  ? 8   GLN   B NE2    1 
ATOM   3468  N  N      . ALA   B 2  9   ? 20.625  -57.171  -18.646  1.00 38.90  ? 9   ALA   B N      1 
ATOM   3469  C  CA     . ALA   B 2  9   ? 21.338  -56.175  -17.850  1.00 42.24  ? 9   ALA   B CA     1 
ATOM   3470  C  C      . ALA   B 2  9   ? 20.433  -55.001  -17.483  1.00 36.90  ? 9   ALA   B C      1 
ATOM   3471  O  O      . ALA   B 2  9   ? 19.891  -54.323  -18.364  1.00 38.47  ? 9   ALA   B O      1 
ATOM   3472  C  CB     . ALA   B 2  9   ? 22.575  -55.687  -18.609  1.00 36.45  ? 9   ALA   B CB     1 
ATOM   3473  N  N      . GLY   B 2  10  ? 20.302  -54.743  -16.189  1.00 33.36  ? 10  GLY   B N      1 
ATOM   3474  C  CA     . GLY   B 2  10  ? 19.519  -53.634  -15.682  1.00 38.81  ? 10  GLY   B CA     1 
ATOM   3475  C  C      . GLY   B 2  10  ? 18.032  -53.936  -15.497  1.00 37.85  ? 10  GLY   B C      1 
ATOM   3476  O  O      . GLY   B 2  10  ? 17.525  -55.017  -15.807  1.00 40.73  ? 10  GLY   B O      1 
ATOM   3477  N  N      . GLN   B 2  11  ? 17.322  -52.935  -14.963  1.00 36.91  ? 11  GLN   B N      1 
ATOM   3478  C  CA     . GLN   B 2  11  ? 15.884  -53.036  -14.727  1.00 40.33  ? 11  GLN   B CA     1 
ATOM   3479  C  C      . GLN   B 2  11  ? 15.186  -53.677  -15.928  1.00 41.15  ? 11  GLN   B C      1 
ATOM   3480  O  O      . GLN   B 2  11  ? 14.614  -54.774  -15.825  1.00 42.74  ? 11  GLN   B O      1 
ATOM   3481  C  CB     . GLN   B 2  11  ? 15.322  -51.634  -14.400  1.00 43.11  ? 11  GLN   B CB     1 
ATOM   3482  C  CG     . GLN   B 2  11  ? 13.848  -51.492  -13.934  1.00 44.08  ? 11  GLN   B CG     1 
ATOM   3483  C  CD     . GLN   B 2  11  ? 13.482  -50.051  -13.399  1.00 58.12  ? 11  GLN   B CD     1 
ATOM   3484  O  OE1    . GLN   B 2  11  ? 13.840  -48.959  -13.980  1.00 40.78  ? 11  GLN   B OE1    1 
ATOM   3485  N  NE2    . GLN   B 2  11  ? 12.769  -50.061  -12.267  1.00 51.75  ? 11  GLN   B NE2    1 
ATOM   3486  N  N      . CYS   B 2  12  ? 15.284  -53.034  -17.093  1.00 35.40  ? 12  CYS   B N      1 
ATOM   3487  C  CA     . CYS   B 2  12  ? 14.487  -53.454  -18.238  1.00 30.48  ? 12  CYS   B CA     1 
ATOM   3488  C  C      . CYS   B 2  12  ? 14.992  -54.780  -18.811  1.00 38.66  ? 12  CYS   B C      1 
ATOM   3489  O  O      . CYS   B 2  12  ? 14.201  -55.694  -19.086  1.00 41.65  ? 12  CYS   B O      1 
ATOM   3490  C  CB     . CYS   B 2  12  ? 14.487  -52.362  -19.292  1.00 25.09  ? 12  CYS   B CB     1 
ATOM   3491  S  SG     . CYS   B 2  12  ? 13.754  -52.876  -20.845  1.00 28.11  ? 12  CYS   B SG     1 
ATOM   3492  N  N      . GLY   B 2  13  ? 16.306  -54.919  -18.981  1.00 36.27  ? 13  GLY   B N      1 
ATOM   3493  C  CA     . GLY   B 2  13  ? 16.828  -56.147  -19.556  1.00 36.40  ? 13  GLY   B CA     1 
ATOM   3494  C  C      . GLY   B 2  13  ? 16.530  -57.380  -18.730  1.00 36.35  ? 13  GLY   B C      1 
ATOM   3495  O  O      . GLY   B 2  13  ? 16.394  -58.474  -19.272  1.00 36.57  ? 13  GLY   B O      1 
ATOM   3496  N  N      . ASN   B 2  14  ? 16.444  -57.233  -17.411  1.00 41.28  ? 14  ASN   B N      1 
ATOM   3497  C  CA     . ASN   B 2  14  ? 16.124  -58.388  -16.576  1.00 41.46  ? 14  ASN   B CA     1 
ATOM   3498  C  C      . ASN   B 2  14  ? 14.621  -58.685  -16.586  1.00 45.13  ? 14  ASN   B C      1 
ATOM   3499  O  O      . ASN   B 2  14  ? 14.215  -59.852  -16.628  1.00 41.71  ? 14  ASN   B O      1 
ATOM   3500  C  CB     . ASN   B 2  14  ? 16.638  -58.163  -15.150  1.00 37.82  ? 14  ASN   B CB     1 
ATOM   3501  C  CG     . ASN   B 2  14  ? 18.118  -58.499  -14.999  1.00 39.25  ? 14  ASN   B CG     1 
ATOM   3502  O  OD1    . ASN   B 2  14  ? 18.490  -59.662  -14.901  1.00 44.89  ? 14  ASN   B OD1    1 
ATOM   3503  N  ND2    . ASN   B 2  14  ? 18.961  -57.487  -14.989  1.00 37.24  ? 14  ASN   B ND2    1 
ATOM   3504  N  N      . GLN   B 2  15  ? 13.776  -57.652  -16.595  1.00 43.29  ? 15  GLN   B N      1 
ATOM   3505  C  CA     . GLN   B 2  15  ? 12.343  -57.912  -16.659  1.00 47.01  ? 15  GLN   B CA     1 
ATOM   3506  C  C      . GLN   B 2  15  ? 11.952  -58.551  -17.993  1.00 43.59  ? 15  GLN   B C      1 
ATOM   3507  O  O      . GLN   B 2  15  ? 11.200  -59.537  -18.018  1.00 39.12  ? 15  GLN   B O      1 
ATOM   3508  C  CB     . GLN   B 2  15  ? 11.550  -56.628  -16.372  1.00 40.04  ? 15  GLN   B CB     1 
ATOM   3509  C  CG     . GLN   B 2  15  ? 11.001  -56.615  -14.927  1.00 49.98  ? 15  GLN   B CG     1 
ATOM   3510  C  CD     . GLN   B 2  15  ? 11.088  -55.236  -14.219  1.00 61.19  ? 15  GLN   B CD     1 
ATOM   3511  O  OE1    . GLN   B 2  15  ? 11.218  -54.192  -14.870  1.00 50.44  ? 15  GLN   B OE1    1 
ATOM   3512  N  NE2    . GLN   B 2  15  ? 11.044  -55.247  -12.872  1.00 57.05  ? 15  GLN   B NE2    1 
ATOM   3513  N  N      . ILE   B 2  16  ? 12.460  -58.044  -19.119  1.00 43.31  ? 16  ILE   B N      1 
ATOM   3514  C  CA     . ILE   B 2  16  ? 12.098  -58.737  -20.354  1.00 45.62  ? 16  ILE   B CA     1 
ATOM   3515  C  C      . ILE   B 2  16  ? 12.910  -60.015  -20.482  1.00 43.68  ? 16  ILE   B C      1 
ATOM   3516  O  O      . ILE   B 2  16  ? 12.372  -61.069  -20.835  1.00 45.85  ? 16  ILE   B O      1 
ATOM   3517  C  CB     . ILE   B 2  16  ? 12.225  -57.841  -21.603  1.00 39.58  ? 16  ILE   B CB     1 
ATOM   3518  C  CG1    . ILE   B 2  16  ? 13.652  -57.848  -22.133  1.00 45.39  ? 16  ILE   B CG1    1 
ATOM   3519  C  CG2    . ILE   B 2  16  ? 11.713  -56.426  -21.334  1.00 34.87  ? 16  ILE   B CG2    1 
ATOM   3520  C  CD1    . ILE   B 2  16  ? 13.899  -56.724  -23.137  1.00 47.28  ? 16  ILE   B CD1    1 
ATOM   3521  N  N      . GLY   B 2  17  ? 14.191  -59.962  -20.149  1.00 43.46  ? 17  GLY   B N      1 
ATOM   3522  C  CA     . GLY   B 2  17  ? 14.969  -61.175  -20.028  1.00 40.98  ? 17  GLY   B CA     1 
ATOM   3523  C  C      . GLY   B 2  17  ? 14.232  -62.276  -19.298  1.00 41.76  ? 17  GLY   B C      1 
ATOM   3524  O  O      . GLY   B 2  17  ? 14.223  -63.422  -19.751  1.00 44.39  ? 17  GLY   B O      1 
ATOM   3525  N  N      . ALA   B 2  18  ? 13.593  -61.951  -18.173  1.00 45.28  ? 18  ALA   B N      1 
ATOM   3526  C  CA     . ALA   B 2  18  ? 12.912  -62.994  -17.410  1.00 45.30  ? 18  ALA   B CA     1 
ATOM   3527  C  C      . ALA   B 2  18  ? 11.694  -63.519  -18.158  1.00 41.36  ? 18  ALA   B C      1 
ATOM   3528  O  O      . ALA   B 2  18  ? 11.441  -64.728  -18.166  1.00 46.40  ? 18  ALA   B O      1 
ATOM   3529  C  CB     . ALA   B 2  18  ? 12.515  -62.483  -16.026  1.00 40.83  ? 18  ALA   B CB     1 
ATOM   3530  N  N      . LYS   B 2  19  ? 10.937  -62.643  -18.810  1.00 35.99  ? 19  LYS   B N      1 
ATOM   3531  C  CA     . LYS   B 2  19  ? 9.764   -63.135  -19.526  1.00 46.48  ? 19  LYS   B CA     1 
ATOM   3532  C  C      . LYS   B 2  19  ? 10.169  -64.072  -20.668  1.00 48.71  ? 19  LYS   B C      1 
ATOM   3533  O  O      . LYS   B 2  19  ? 9.574   -65.141  -20.851  1.00 45.26  ? 19  LYS   B O      1 
ATOM   3534  C  CB     . LYS   B 2  19  ? 8.934   -61.955  -20.032  1.00 47.43  ? 19  LYS   B CB     1 
ATOM   3535  C  CG     . LYS   B 2  19  ? 8.065   -61.347  -18.959  1.00 42.14  ? 19  LYS   B CG     1 
ATOM   3536  C  CD     . LYS   B 2  19  ? 6.773   -62.097  -18.894  1.00 57.25  ? 19  LYS   B CD     1 
ATOM   3537  C  CE     . LYS   B 2  19  ? 6.229   -62.340  -20.315  1.00 58.66  ? 19  LYS   B CE     1 
ATOM   3538  N  NZ     . LYS   B 2  19  ? 4.738   -62.357  -20.369  1.00 57.46  ? 19  LYS   B NZ     1 
ATOM   3539  N  N      . PHE   B 2  20  ? 11.199  -63.696  -21.430  1.00 49.68  ? 20  PHE   B N      1 
ATOM   3540  C  CA     . PHE   B 2  20  ? 11.686  -64.547  -22.503  1.00 46.19  ? 20  PHE   B CA     1 
ATOM   3541  C  C      . PHE   B 2  20  ? 11.900  -65.977  -22.023  1.00 49.28  ? 20  PHE   B C      1 
ATOM   3542  O  O      . PHE   B 2  20  ? 11.444  -66.930  -22.665  1.00 47.63  ? 20  PHE   B O      1 
ATOM   3543  C  CB     . PHE   B 2  20  ? 12.976  -63.964  -23.062  1.00 47.19  ? 20  PHE   B CB     1 
ATOM   3544  C  CG     . PHE   B 2  20  ? 13.660  -64.849  -24.058  1.00 48.18  ? 20  PHE   B CG     1 
ATOM   3545  C  CD1    . PHE   B 2  20  ? 13.215  -64.914  -25.367  1.00 45.44  ? 20  PHE   B CD1    1 
ATOM   3546  C  CD2    . PHE   B 2  20  ? 14.759  -65.607  -23.686  1.00 45.54  ? 20  PHE   B CD2    1 
ATOM   3547  C  CE1    . PHE   B 2  20  ? 13.852  -65.723  -26.288  1.00 44.59  ? 20  PHE   B CE1    1 
ATOM   3548  C  CE2    . PHE   B 2  20  ? 15.394  -66.415  -24.596  1.00 47.35  ? 20  PHE   B CE2    1 
ATOM   3549  C  CZ     . PHE   B 2  20  ? 14.945  -66.468  -25.907  1.00 44.54  ? 20  PHE   B CZ     1 
ATOM   3550  N  N      . TRP   B 2  21  ? 12.592  -66.150  -20.886  1.00 47.89  ? 21  TRP   B N      1 
ATOM   3551  C  CA     . TRP   B 2  21  ? 12.911  -67.503  -20.423  1.00 46.08  ? 21  TRP   B CA     1 
ATOM   3552  C  C      . TRP   B 2  21  ? 11.671  -68.238  -19.942  1.00 50.82  ? 21  TRP   B C      1 
ATOM   3553  O  O      . TRP   B 2  21  ? 11.557  -69.454  -20.129  1.00 53.10  ? 21  TRP   B O      1 
ATOM   3554  C  CB     . TRP   B 2  21  ? 13.975  -67.464  -19.328  1.00 44.68  ? 21  TRP   B CB     1 
ATOM   3555  C  CG     . TRP   B 2  21  ? 15.300  -67.175  -19.897  1.00 44.46  ? 21  TRP   B CG     1 
ATOM   3556  C  CD1    . TRP   B 2  21  ? 15.972  -65.989  -19.834  1.00 45.14  ? 21  TRP   B CD1    1 
ATOM   3557  C  CD2    . TRP   B 2  21  ? 16.117  -68.063  -20.684  1.00 50.45  ? 21  TRP   B CD2    1 
ATOM   3558  N  NE1    . TRP   B 2  21  ? 17.166  -66.084  -20.520  1.00 50.38  ? 21  TRP   B NE1    1 
ATOM   3559  C  CE2    . TRP   B 2  21  ? 17.281  -67.344  -21.051  1.00 50.44  ? 21  TRP   B CE2    1 
ATOM   3560  C  CE3    . TRP   B 2  21  ? 15.987  -69.397  -21.099  1.00 48.24  ? 21  TRP   B CE3    1 
ATOM   3561  C  CZ2    . TRP   B 2  21  ? 18.308  -67.915  -21.808  1.00 42.55  ? 21  TRP   B CZ2    1 
ATOM   3562  C  CZ3    . TRP   B 2  21  ? 17.012  -69.962  -21.866  1.00 49.03  ? 21  TRP   B CZ3    1 
ATOM   3563  C  CH2    . TRP   B 2  21  ? 18.154  -69.219  -22.206  1.00 47.55  ? 21  TRP   B CH2    1 
ATOM   3564  N  N      . GLU   B 2  22  ? 10.738  -67.530  -19.307  1.00 49.70  ? 22  GLU   B N      1 
ATOM   3565  C  CA     . GLU   B 2  22  ? 9.434   -68.119  -19.046  1.00 52.27  ? 22  GLU   B CA     1 
ATOM   3566  C  C      . GLU   B 2  22  ? 8.817   -68.643  -20.332  1.00 53.78  ? 22  GLU   B C      1 
ATOM   3567  O  O      . GLU   B 2  22  ? 8.533   -69.837  -20.475  1.00 56.80  ? 22  GLU   B O      1 
ATOM   3568  C  CB     . GLU   B 2  22  ? 8.506   -67.081  -18.459  1.00 47.62  ? 22  GLU   B CB     1 
ATOM   3569  C  CG     . GLU   B 2  22  ? 8.690   -66.773  -17.061  1.00 54.55  ? 22  GLU   B CG     1 
ATOM   3570  C  CD     . GLU   B 2  22  ? 7.695   -65.734  -16.681  1.00 61.47  ? 22  GLU   B CD     1 
ATOM   3571  O  OE1    . GLU   B 2  22  ? 6.599   -65.760  -17.304  1.00 55.25  ? 22  GLU   B OE1    1 
ATOM   3572  O  OE2    . GLU   B 2  22  ? 8.006   -64.911  -15.787  1.00 64.57  ? 22  GLU   B OE2    1 
ATOM   3573  N  N      . VAL   B 2  23  ? 8.585   -67.723  -21.268  1.00 45.12  ? 23  VAL   B N      1 
ATOM   3574  C  CA     . VAL   B 2  23  ? 7.889   -68.019  -22.514  1.00 47.52  ? 23  VAL   B CA     1 
ATOM   3575  C  C      . VAL   B 2  23  ? 8.515   -69.211  -23.233  1.00 53.44  ? 23  VAL   B C      1 
ATOM   3576  O  O      . VAL   B 2  23  ? 7.825   -70.181  -23.573  1.00 55.17  ? 23  VAL   B O      1 
ATOM   3577  C  CB     . VAL   B 2  23  ? 7.872   -66.760  -23.396  1.00 46.64  ? 23  VAL   B CB     1 
ATOM   3578  C  CG1    . VAL   B 2  23  ? 7.318   -67.044  -24.764  1.00 42.17  ? 23  VAL   B CG1    1 
ATOM   3579  C  CG2    . VAL   B 2  23  ? 7.054   -65.694  -22.702  1.00 49.40  ? 23  VAL   B CG2    1 
ATOM   3580  N  N      . ILE   B 2  24  ? 9.827   -69.159  -23.485  1.00 48.69  ? 24  ILE   B N      1 
ATOM   3581  C  CA     . ILE   B 2  24  ? 10.443  -70.239  -24.245  1.00 50.52  ? 24  ILE   B CA     1 
ATOM   3582  C  C      . ILE   B 2  24  ? 10.660  -71.472  -23.384  1.00 51.81  ? 24  ILE   B C      1 
ATOM   3583  O  O      . ILE   B 2  24  ? 10.759  -72.581  -23.917  1.00 58.04  ? 24  ILE   B O      1 
ATOM   3584  C  CB     . ILE   B 2  24  ? 11.777  -69.844  -24.916  1.00 51.10  ? 24  ILE   B CB     1 
ATOM   3585  C  CG1    . ILE   B 2  24  ? 12.928  -69.852  -23.911  1.00 52.53  ? 24  ILE   B CG1    1 
ATOM   3586  C  CG2    . ILE   B 2  24  ? 11.681  -68.508  -25.635  1.00 45.44  ? 24  ILE   B CG2    1 
ATOM   3587  C  CD1    . ILE   B 2  24  ? 14.288  -69.920  -24.560  1.00 48.20  ? 24  ILE   B CD1    1 
ATOM   3588  N  N      . SER   B 2  25  ? 10.726  -71.328  -22.065  1.00 51.65  ? 25  SER   B N      1 
ATOM   3589  C  CA     . SER   B 2  25  ? 10.763  -72.526  -21.232  1.00 60.66  ? 25  SER   B CA     1 
ATOM   3590  C  C      . SER   B 2  25  ? 9.460   -73.302  -21.332  1.00 61.60  ? 25  SER   B C      1 
ATOM   3591  O  O      . SER   B 2  25  ? 9.451   -74.532  -21.202  1.00 62.48  ? 25  SER   B O      1 
ATOM   3592  C  CB     . SER   B 2  25  ? 11.048  -72.169  -19.775  1.00 60.34  ? 25  SER   B CB     1 
ATOM   3593  O  OG     . SER   B 2  25  ? 12.403  -71.813  -19.601  1.00 59.24  ? 25  SER   B OG     1 
ATOM   3594  N  N      . ASP   B 2  26  ? 8.354   -72.594  -21.554  1.00 60.59  ? 26  ASP   B N      1 
ATOM   3595  C  CA     . ASP   B 2  26  ? 7.058   -73.232  -21.732  1.00 59.22  ? 26  ASP   B CA     1 
ATOM   3596  C  C      . ASP   B 2  26  ? 6.959   -73.890  -23.106  1.00 63.35  ? 26  ASP   B C      1 
ATOM   3597  O  O      . ASP   B 2  26  ? 6.355   -74.960  -23.252  1.00 62.55  ? 26  ASP   B O      1 
ATOM   3598  C  CB     . ASP   B 2  26  ? 5.960   -72.185  -21.528  1.00 61.83  ? 26  ASP   B CB     1 
ATOM   3599  C  CG     . ASP   B 2  26  ? 4.566   -72.729  -21.780  1.00 73.13  ? 26  ASP   B CG     1 
ATOM   3600  O  OD1    . ASP   B 2  26  ? 4.130   -72.725  -22.958  1.00 66.94  ? 26  ASP   B OD1    1 
ATOM   3601  O  OD2    . ASP   B 2  26  ? 3.901   -73.138  -20.797  1.00 76.61  ? 26  ASP   B OD2    1 
ATOM   3602  N  N      . GLU   B 2  27  ? 7.568   -73.277  -24.122  1.00 61.54  ? 27  GLU   B N      1 
ATOM   3603  C  CA     . GLU   B 2  27  ? 7.513   -73.848  -25.459  1.00 56.15  ? 27  GLU   B CA     1 
ATOM   3604  C  C      . GLU   B 2  27  ? 8.362   -75.106  -25.570  1.00 60.44  ? 27  GLU   B C      1 
ATOM   3605  O  O      . GLU   B 2  27  ? 8.069   -75.974  -26.397  1.00 64.31  ? 27  GLU   B O      1 
ATOM   3606  C  CB     . GLU   B 2  27  ? 7.975   -72.822  -26.489  1.00 55.52  ? 27  GLU   B CB     1 
ATOM   3607  C  CG     . GLU   B 2  27  ? 7.390   -71.433  -26.329  1.00 51.65  ? 27  GLU   B CG     1 
ATOM   3608  C  CD     . GLU   B 2  27  ? 7.585   -70.597  -27.590  1.00 54.55  ? 27  GLU   B CD     1 
ATOM   3609  O  OE1    . GLU   B 2  27  ? 8.391   -71.022  -28.460  1.00 51.74  ? 27  GLU   B OE1    1 
ATOM   3610  O  OE2    . GLU   B 2  27  ? 6.930   -69.535  -27.713  1.00 47.60  ? 27  GLU   B OE2    1 
ATOM   3611  N  N      . HIS   B 2  28  ? 9.433   -75.211  -24.785  1.00 58.87  ? 28  HIS   B N      1 
ATOM   3612  C  CA     . HIS   B 2  28  ? 10.273  -76.401  -24.793  1.00 60.39  ? 28  HIS   B CA     1 
ATOM   3613  C  C      . HIS   B 2  28  ? 9.921   -77.341  -23.661  1.00 61.84  ? 28  HIS   B C      1 
ATOM   3614  O  O      . HIS   B 2  28  ? 10.723  -78.210  -23.309  1.00 64.20  ? 28  HIS   B O      1 
ATOM   3615  C  CB     . HIS   B 2  28  ? 11.752  -76.024  -24.730  1.00 56.05  ? 28  HIS   B CB     1 
ATOM   3616  C  CG     . HIS   B 2  28  ? 12.217  -75.251  -25.920  1.00 57.45  ? 28  HIS   B CG     1 
ATOM   3617  N  ND1    . HIS   B 2  28  ? 12.548  -75.852  -27.114  1.00 61.92  ? 28  HIS   B ND1    1 
ATOM   3618  C  CD2    . HIS   B 2  28  ? 12.374  -73.921  -26.115  1.00 56.77  ? 28  HIS   B CD2    1 
ATOM   3619  C  CE1    . HIS   B 2  28  ? 12.907  -74.929  -27.989  1.00 57.96  ? 28  HIS   B CE1    1 
ATOM   3620  N  NE2    . HIS   B 2  28  ? 12.806  -73.748  -27.408  1.00 58.45  ? 28  HIS   B NE2    1 
ATOM   3621  N  N      . GLY   B 2  29  ? 8.739   -77.171  -23.080  1.00 59.22  ? 29  GLY   B N      1 
ATOM   3622  C  CA     . GLY   B 2  29  ? 8.277   -78.039  -22.023  1.00 62.54  ? 29  GLY   B CA     1 
ATOM   3623  C  C      . GLY   B 2  29  ? 9.170   -78.124  -20.807  1.00 67.57  ? 29  GLY   B C      1 
ATOM   3624  O  O      . GLY   B 2  29  ? 9.048   -79.084  -20.047  1.00 70.63  ? 29  GLY   B O      1 
ATOM   3625  N  N      . ILE   B 2  30  ? 10.074  -77.159  -20.592  1.00 64.87  ? 30  ILE   B N      1 
ATOM   3626  C  CA     . ILE   B 2  30  ? 10.886  -77.128  -19.377  1.00 63.51  ? 30  ILE   B CA     1 
ATOM   3627  C  C      . ILE   B 2  30  ? 10.103  -76.371  -18.319  1.00 62.59  ? 30  ILE   B C      1 
ATOM   3628  O  O      . ILE   B 2  30  ? 9.520   -75.322  -18.605  1.00 63.24  ? 30  ILE   B O      1 
ATOM   3629  C  CB     . ILE   B 2  30  ? 12.254  -76.468  -19.620  1.00 63.76  ? 30  ILE   B CB     1 
ATOM   3630  C  CG1    . ILE   B 2  30  ? 12.988  -77.086  -20.808  1.00 62.52  ? 30  ILE   B CG1    1 
ATOM   3631  C  CG2    . ILE   B 2  30  ? 13.109  -76.591  -18.393  1.00 64.07  ? 30  ILE   B CG2    1 
ATOM   3632  C  CD1    . ILE   B 2  30  ? 12.668  -78.528  -21.045  1.00 68.35  ? 30  ILE   B CD1    1 
ATOM   3633  N  N      . ASP   B 2  31  ? 10.083  -76.896  -17.101  1.00 65.61  ? 31  ASP   B N      1 
ATOM   3634  C  CA     . ASP   B 2  31  ? 9.264   -76.283  -16.058  1.00 69.37  ? 31  ASP   B CA     1 
ATOM   3635  C  C      . ASP   B 2  31  ? 10.125  -75.449  -15.112  1.00 71.40  ? 31  ASP   B C      1 
ATOM   3636  O  O      . ASP   B 2  31  ? 11.353  -75.375  -15.289  1.00 68.89  ? 31  ASP   B O      1 
ATOM   3637  C  CB     . ASP   B 2  31  ? 8.499   -77.350  -15.275  1.00 66.30  ? 31  ASP   B CB     1 
ATOM   3638  C  CG     . ASP   B 2  31  ? 9.414   -78.317  -14.561  1.00 69.85  ? 31  ASP   B CG     1 
ATOM   3639  O  OD1    . ASP   B 2  31  ? 10.585  -77.982  -14.339  1.00 73.03  ? 31  ASP   B OD1    1 
ATOM   3640  O  OD2    . ASP   B 2  31  ? 8.975   -79.428  -14.223  1.00 77.55  ? 31  ASP   B OD2    1 
ATOM   3641  N  N      . PRO   B 2  32  ? 9.533   -74.815  -14.095  1.00 63.57  ? 32  PRO   B N      1 
ATOM   3642  C  CA     . PRO   B 2  32  ? 10.329  -73.942  -13.223  1.00 65.77  ? 32  PRO   B CA     1 
ATOM   3643  C  C      . PRO   B 2  32  ? 11.383  -74.683  -12.423  1.00 74.63  ? 32  PRO   B C      1 
ATOM   3644  O  O      . PRO   B 2  32  ? 12.224  -74.028  -11.794  1.00 76.64  ? 32  PRO   B O      1 
ATOM   3645  C  CB     . PRO   B 2  32  ? 9.280   -73.294  -12.312  1.00 68.89  ? 32  PRO   B CB     1 
ATOM   3646  C  CG     . PRO   B 2  32  ? 7.993   -73.421  -13.064  1.00 67.85  ? 32  PRO   B CG     1 
ATOM   3647  C  CD     . PRO   B 2  32  ? 8.093   -74.716  -13.802  1.00 66.43  ? 32  PRO   B CD     1 
ATOM   3648  N  N      . THR   B 2  33  ? 11.379  -76.014  -12.422  1.00 75.69  ? 33  THR   B N      1 
ATOM   3649  C  CA     . THR   B 2  33  ? 12.447  -76.761  -11.768  1.00 75.59  ? 33  THR   B CA     1 
ATOM   3650  C  C      . THR   B 2  33  ? 13.582  -77.147  -12.708  1.00 73.15  ? 33  THR   B C      1 
ATOM   3651  O  O      . THR   B 2  33  ? 14.630  -77.604  -12.234  1.00 73.09  ? 33  THR   B O      1 
ATOM   3652  C  CB     . THR   B 2  33  ? 11.901  -78.032  -11.087  1.00 81.05  ? 33  THR   B CB     1 
ATOM   3653  O  OG1    . THR   B 2  33  ? 12.935  -79.027  -11.045  1.00 91.84  ? 33  THR   B OG1    1 
ATOM   3654  C  CG2    . THR   B 2  33  ? 10.658  -78.587  -11.784  1.00 76.86  ? 33  THR   B CG2    1 
ATOM   3655  N  N      . GLY   B 2  34  ? 13.411  -76.964  -14.012  1.00 72.43  ? 34  GLY   B N      1 
ATOM   3656  C  CA     . GLY   B 2  34  ? 14.391  -77.423  -14.975  1.00 72.02  ? 34  GLY   B CA     1 
ATOM   3657  C  C      . GLY   B 2  34  ? 14.154  -78.810  -15.530  1.00 72.51  ? 34  GLY   B C      1 
ATOM   3658  O  O      . GLY   B 2  34  ? 15.015  -79.318  -16.260  1.00 76.17  ? 34  GLY   B O      1 
ATOM   3659  N  N      . SER   B 2  35  ? 13.014  -79.432  -15.214  1.00 75.75  ? 35  SER   B N      1 
ATOM   3660  C  CA     . SER   B 2  35  ? 12.677  -80.782  -15.654  1.00 75.42  ? 35  SER   B CA     1 
ATOM   3661  C  C      . SER   B 2  35  ? 11.758  -80.714  -16.868  1.00 74.03  ? 35  SER   B C      1 
ATOM   3662  O  O      . SER   B 2  35  ? 10.739  -80.018  -16.833  1.00 71.53  ? 35  SER   B O      1 
ATOM   3663  C  CB     . SER   B 2  35  ? 11.996  -81.569  -14.530  1.00 76.69  ? 35  SER   B CB     1 
ATOM   3664  O  OG     . SER   B 2  35  ? 12.836  -81.710  -13.395  1.00 71.50  ? 35  SER   B OG     1 
ATOM   3665  N  N      . TYR   B 2  36  ? 12.119  -81.444  -17.933  1.00 76.97  ? 36  TYR   B N      1 
ATOM   3666  C  CA     . TYR   B 2  36  ? 11.335  -81.473  -19.165  1.00 73.60  ? 36  TYR   B CA     1 
ATOM   3667  C  C      . TYR   B 2  36  ? 10.092  -82.337  -18.998  1.00 77.52  ? 36  TYR   B C      1 
ATOM   3668  O  O      . TYR   B 2  36  ? 10.184  -83.489  -18.566  1.00 80.50  ? 36  TYR   B O      1 
ATOM   3669  C  CB     . TYR   B 2  36  ? 12.157  -82.017  -20.333  1.00 73.91  ? 36  TYR   B CB     1 
ATOM   3670  C  CG     . TYR   B 2  36  ? 11.298  -82.276  -21.549  1.00 75.16  ? 36  TYR   B CG     1 
ATOM   3671  C  CD1    . TYR   B 2  36  ? 10.727  -81.217  -22.240  1.00 77.49  ? 36  TYR   B CD1    1 
ATOM   3672  C  CD2    . TYR   B 2  36  ? 11.015  -83.568  -21.984  1.00 73.23  ? 36  TYR   B CD2    1 
ATOM   3673  C  CE1    . TYR   B 2  36  ? 9.920   -81.428  -23.339  1.00 77.93  ? 36  TYR   B CE1    1 
ATOM   3674  C  CE2    . TYR   B 2  36  ? 10.203  -83.789  -23.097  1.00 71.12  ? 36  TYR   B CE2    1 
ATOM   3675  C  CZ     . TYR   B 2  36  ? 9.662   -82.708  -23.765  1.00 74.26  ? 36  TYR   B CZ     1 
ATOM   3676  O  OH     . TYR   B 2  36  ? 8.850   -82.863  -24.863  1.00 77.33  ? 36  TYR   B OH     1 
ATOM   3677  N  N      . HIS   B 2  37  ? 8.928   -81.785  -19.359  1.00 80.74  ? 37  HIS   B N      1 
ATOM   3678  C  CA     . HIS   B 2  37  ? 7.645   -82.495  -19.306  1.00 78.91  ? 37  HIS   B CA     1 
ATOM   3679  C  C      . HIS   B 2  37  ? 6.803   -82.158  -20.547  1.00 77.01  ? 37  HIS   B C      1 
ATOM   3680  O  O      . HIS   B 2  37  ? 5.688   -81.646  -20.460  1.00 71.06  ? 37  HIS   B O      1 
ATOM   3681  C  CB     . HIS   B 2  37  ? 6.871   -82.157  -18.031  1.00 78.20  ? 37  HIS   B CB     1 
ATOM   3682  C  CG     . HIS   B 2  37  ? 7.437   -82.765  -16.779  1.00 88.41  ? 37  HIS   B CG     1 
ATOM   3683  N  ND1    . HIS   B 2  37  ? 8.783   -83.002  -16.598  1.00 93.18  ? 37  HIS   B ND1    1 
ATOM   3684  C  CD2    . HIS   B 2  37  ? 6.827   -83.194  -15.645  1.00 93.18  ? 37  HIS   B CD2    1 
ATOM   3685  C  CE1    . HIS   B 2  37  ? 8.979   -83.547  -15.407  1.00 94.35  ? 37  HIS   B CE1    1 
ATOM   3686  N  NE2    . HIS   B 2  37  ? 7.807   -83.675  -14.809  1.00 88.17  ? 37  HIS   B NE2    1 
ATOM   3687  N  N      . GLY   B 2  38  ? 7.339   -82.460  -21.734  1.00 73.74  ? 38  GLY   B N      1 
ATOM   3688  C  CA     . GLY   B 2  38  ? 6.703   -82.112  -22.985  1.00 81.55  ? 38  GLY   B CA     1 
ATOM   3689  C  C      . GLY   B 2  38  ? 6.303   -83.326  -23.816  1.00 81.92  ? 38  GLY   B C      1 
ATOM   3690  O  O      . GLY   B 2  38  ? 6.615   -84.474  -23.490  1.00 81.11  ? 38  GLY   B O      1 
ATOM   3691  N  N      . ASP   B 2  39  ? 5.606   -83.042  -24.921  1.00 78.08  ? 39  ASP   B N      1 
ATOM   3692  C  CA     . ASP   B 2  39  ? 5.035   -84.073  -25.781  1.00 75.69  ? 39  ASP   B CA     1 
ATOM   3693  C  C      . ASP   B 2  39  ? 5.912   -84.396  -26.990  1.00 77.09  ? 39  ASP   B C      1 
ATOM   3694  O  O      . ASP   B 2  39  ? 6.150   -85.573  -27.281  1.00 79.45  ? 39  ASP   B O      1 
ATOM   3695  C  CB     . ASP   B 2  39  ? 3.615   -83.668  -26.239  1.00 73.02  ? 39  ASP   B CB     1 
ATOM   3696  C  CG     . ASP   B 2  39  ? 3.515   -82.204  -26.705  1.00 86.16  ? 39  ASP   B CG     1 
ATOM   3697  O  OD1    . ASP   B 2  39  ? 4.115   -81.299  -26.075  1.00 85.41  ? 39  ASP   B OD1    1 
ATOM   3698  O  OD2    . ASP   B 2  39  ? 2.802   -81.949  -27.705  1.00 91.19  ? 39  ASP   B OD2    1 
ATOM   3699  N  N      . SER   B 2  40  ? 6.399   -83.379  -27.702  1.00 77.51  ? 40  SER   B N      1 
ATOM   3700  C  CA     . SER   B 2  40  ? 7.113   -83.568  -28.959  1.00 72.51  ? 40  SER   B CA     1 
ATOM   3701  C  C      . SER   B 2  40  ? 8.623   -83.617  -28.756  1.00 73.65  ? 40  SER   B C      1 
ATOM   3702  O  O      . SER   B 2  40  ? 9.172   -82.981  -27.859  1.00 78.13  ? 40  SER   B O      1 
ATOM   3703  C  CB     . SER   B 2  40  ? 6.780   -82.448  -29.940  1.00 66.29  ? 40  SER   B CB     1 
ATOM   3704  O  OG     . SER   B 2  40  ? 7.628   -82.525  -31.071  1.00 76.01  ? 40  SER   B OG     1 
ATOM   3705  N  N      . ASP   B 2  41  ? 9.302   -84.382  -29.609  1.00 77.16  ? 41  ASP   B N      1 
ATOM   3706  C  CA     . ASP   B 2  41  ? 10.759  -84.339  -29.581  1.00 79.57  ? 41  ASP   B CA     1 
ATOM   3707  C  C      . ASP   B 2  41  ? 11.279  -83.042  -30.184  1.00 76.83  ? 41  ASP   B C      1 
ATOM   3708  O  O      . ASP   B 2  41  ? 12.387  -82.600  -29.848  1.00 74.88  ? 41  ASP   B O      1 
ATOM   3709  C  CB     . ASP   B 2  41  ? 11.352  -85.541  -30.315  1.00 82.94  ? 41  ASP   B CB     1 
ATOM   3710  C  CG     . ASP   B 2  41  ? 11.599  -86.719  -29.393  1.00 90.50  ? 41  ASP   B CG     1 
ATOM   3711  O  OD1    . ASP   B 2  41  ? 11.494  -86.532  -28.158  1.00 88.38  ? 41  ASP   B OD1    1 
ATOM   3712  O  OD2    . ASP   B 2  41  ? 11.905  -87.826  -29.903  1.00 89.89  ? 41  ASP   B OD2    1 
ATOM   3713  N  N      . LEU   B 2  42  ? 10.489  -82.417  -31.067  1.00 72.69  ? 42  LEU   B N      1 
ATOM   3714  C  CA     . LEU   B 2  42  ? 10.852  -81.111  -31.614  1.00 76.13  ? 42  LEU   B CA     1 
ATOM   3715  C  C      . LEU   B 2  42  ? 11.256  -80.112  -30.534  1.00 72.47  ? 42  LEU   B C      1 
ATOM   3716  O  O      . LEU   B 2  42  ? 11.961  -79.142  -30.842  1.00 68.04  ? 42  LEU   B O      1 
ATOM   3717  C  CB     . LEU   B 2  42  ? 9.681   -80.519  -32.407  1.00 74.95  ? 42  LEU   B CB     1 
ATOM   3718  C  CG     . LEU   B 2  42  ? 9.200   -81.184  -33.687  1.00 68.84  ? 42  LEU   B CG     1 
ATOM   3719  C  CD1    . LEU   B 2  42  ? 8.246   -80.249  -34.389  1.00 71.21  ? 42  LEU   B CD1    1 
ATOM   3720  C  CD2    . LEU   B 2  42  ? 10.378  -81.485  -34.568  1.00 75.10  ? 42  LEU   B CD2    1 
ATOM   3721  N  N      . GLN   B 2  43  ? 10.792  -80.311  -29.287  1.00 71.07  ? 43  GLN   B N      1 
ATOM   3722  C  CA     . GLN   B 2  43  ? 11.102  -79.421  -28.173  1.00 67.52  ? 43  GLN   B CA     1 
ATOM   3723  C  C      . GLN   B 2  43  ? 12.514  -79.604  -27.636  1.00 68.40  ? 43  GLN   B C      1 
ATOM   3724  O  O      . GLN   B 2  43  ? 13.064  -78.667  -27.050  1.00 66.66  ? 43  GLN   B O      1 
ATOM   3725  C  CB     . GLN   B 2  43  ? 10.134  -79.630  -27.007  1.00 63.95  ? 43  GLN   B CB     1 
ATOM   3726  C  CG     . GLN   B 2  43  ? 8.697   -79.786  -27.396  1.00 66.26  ? 43  GLN   B CG     1 
ATOM   3727  C  CD     . GLN   B 2  43  ? 7.758   -79.722  -26.208  1.00 69.12  ? 43  GLN   B CD     1 
ATOM   3728  O  OE1    . GLN   B 2  43  ? 7.933   -78.909  -25.307  1.00 69.37  ? 43  GLN   B OE1    1 
ATOM   3729  N  NE2    . GLN   B 2  43  ? 6.750   -80.581  -26.204  1.00 79.58  ? 43  GLN   B NE2    1 
ATOM   3730  N  N      . LEU   B 2  44  ? 13.116  -80.777  -27.798  1.00 66.19  ? 44  LEU   B N      1 
ATOM   3731  C  CA     . LEU   B 2  44  ? 14.433  -80.994  -27.228  1.00 63.92  ? 44  LEU   B CA     1 
ATOM   3732  C  C      . LEU   B 2  44  ? 15.530  -81.150  -28.261  1.00 61.02  ? 44  LEU   B C      1 
ATOM   3733  O  O      . LEU   B 2  44  ? 16.700  -81.190  -27.882  1.00 65.41  ? 44  LEU   B O      1 
ATOM   3734  C  CB     . LEU   B 2  44  ? 14.416  -82.219  -26.312  1.00 62.72  ? 44  LEU   B CB     1 
ATOM   3735  C  CG     . LEU   B 2  44  ? 13.868  -81.809  -24.955  1.00 66.13  ? 44  LEU   B CG     1 
ATOM   3736  C  CD1    . LEU   B 2  44  ? 13.141  -82.953  -24.297  1.00 67.43  ? 44  LEU   B CD1    1 
ATOM   3737  C  CD2    . LEU   B 2  44  ? 15.021  -81.317  -24.112  1.00 68.81  ? 44  LEU   B CD2    1 
ATOM   3738  N  N      . GLU   B 2  45  ? 15.196  -81.222  -29.546  1.00 58.50  ? 45  GLU   B N      1 
ATOM   3739  C  CA     . GLU   B 2  45  ? 16.226  -81.474  -30.543  1.00 57.75  ? 45  GLU   B CA     1 
ATOM   3740  C  C      . GLU   B 2  45  ? 17.269  -80.364  -30.579  1.00 63.54  ? 45  GLU   B C      1 
ATOM   3741  O  O      . GLU   B 2  45  ? 18.445  -80.625  -30.855  1.00 61.72  ? 45  GLU   B O      1 
ATOM   3742  C  CB     . GLU   B 2  45  ? 15.585  -81.643  -31.911  1.00 61.32  ? 45  GLU   B CB     1 
ATOM   3743  C  CG     . GLU   B 2  45  ? 16.427  -82.427  -32.889  1.00 63.30  ? 45  GLU   B CG     1 
ATOM   3744  C  CD     . GLU   B 2  45  ? 15.879  -82.312  -34.296  1.00 73.84  ? 45  GLU   B CD     1 
ATOM   3745  O  OE1    . GLU   B 2  45  ? 14.788  -82.894  -34.544  1.00 71.93  ? 45  GLU   B OE1    1 
ATOM   3746  O  OE2    . GLU   B 2  45  ? 16.538  -81.650  -35.144  1.00 65.36  ? 45  GLU   B OE2    1 
ATOM   3747  N  N      . ARG   B 2  46  ? 16.865  -79.118  -30.335  1.00 63.43  ? 46  ARG   B N      1 
ATOM   3748  C  CA     . ARG   B 2  46  ? 17.796  -77.997  -30.342  1.00 59.84  ? 46  ARG   B CA     1 
ATOM   3749  C  C      . ARG   B 2  46  ? 17.782  -77.242  -29.021  1.00 62.47  ? 46  ARG   B C      1 
ATOM   3750  O  O      . ARG   B 2  46  ? 18.118  -76.052  -28.981  1.00 62.36  ? 46  ARG   B O      1 
ATOM   3751  C  CB     . ARG   B 2  46  ? 17.487  -77.053  -31.500  1.00 62.73  ? 46  ARG   B CB     1 
ATOM   3752  C  CG     . ARG   B 2  46  ? 17.468  -77.743  -32.848  1.00 61.50  ? 46  ARG   B CG     1 
ATOM   3753  C  CD     . ARG   B 2  46  ? 18.375  -77.033  -33.826  1.00 57.30  ? 46  ARG   B CD     1 
ATOM   3754  N  NE     . ARG   B 2  46  ? 17.720  -75.886  -34.445  1.00 56.07  ? 46  ARG   B NE     1 
ATOM   3755  C  CZ     . ARG   B 2  46  ? 18.359  -74.878  -35.023  1.00 52.46  ? 46  ARG   B CZ     1 
ATOM   3756  N  NH1    . ARG   B 2  46  ? 19.675  -74.813  -35.041  1.00 58.45  ? 46  ARG   B NH1    1 
ATOM   3757  N  NH2    . ARG   B 2  46  ? 17.658  -73.915  -35.607  1.00 53.80  ? 46  ARG   B NH2    1 
ATOM   3758  N  N      . ILE   B 2  47  ? 17.398  -77.922  -27.940  1.00 60.13  ? 47  ILE   B N      1 
ATOM   3759  C  CA     . ILE   B 2  47  ? 17.310  -77.293  -26.629  1.00 59.29  ? 47  ILE   B CA     1 
ATOM   3760  C  C      . ILE   B 2  47  ? 18.660  -76.721  -26.204  1.00 59.26  ? 47  ILE   B C      1 
ATOM   3761  O  O      . ILE   B 2  47  ? 18.721  -75.760  -25.424  1.00 57.06  ? 47  ILE   B O      1 
ATOM   3762  C  CB     . ILE   B 2  47  ? 16.778  -78.319  -25.606  1.00 60.99  ? 47  ILE   B CB     1 
ATOM   3763  C  CG1    . ILE   B 2  47  ? 16.036  -77.632  -24.461  1.00 58.44  ? 47  ILE   B CG1    1 
ATOM   3764  C  CG2    . ILE   B 2  47  ? 17.908  -79.203  -25.087  1.00 58.63  ? 47  ILE   B CG2    1 
ATOM   3765  C  CD1    . ILE   B 2  47  ? 14.990  -76.649  -24.923  1.00 59.79  ? 47  ILE   B CD1    1 
ATOM   3766  N  N      . ASN   B 2  48  ? 19.761  -77.289  -26.702  1.00 54.25  ? 48  ASN   B N      1 
ATOM   3767  C  CA     . ASN   B 2  48  ? 21.066  -76.876  -26.207  1.00 55.12  ? 48  ASN   B CA     1 
ATOM   3768  C  C      . ASN   B 2  48  ? 21.488  -75.501  -26.706  1.00 59.47  ? 48  ASN   B C      1 
ATOM   3769  O  O      . ASN   B 2  48  ? 22.406  -74.900  -26.128  1.00 63.07  ? 48  ASN   B O      1 
ATOM   3770  C  CB     . ASN   B 2  48  ? 22.136  -77.875  -26.611  1.00 58.30  ? 48  ASN   B CB     1 
ATOM   3771  C  CG     . ASN   B 2  48  ? 22.271  -77.990  -28.111  1.00 71.75  ? 48  ASN   B CG     1 
ATOM   3772  O  OD1    . ASN   B 2  48  ? 21.309  -78.340  -28.811  1.00 72.47  ? 48  ASN   B OD1    1 
ATOM   3773  N  ND2    . ASN   B 2  48  ? 23.464  -77.666  -28.627  1.00 75.10  ? 48  ASN   B ND2    1 
ATOM   3774  N  N      . VAL   B 2  49  ? 20.868  -75.002  -27.780  1.00 56.80  ? 49  VAL   B N      1 
ATOM   3775  C  CA     . VAL   B 2  49  ? 21.188  -73.665  -28.272  1.00 52.18  ? 49  VAL   B CA     1 
ATOM   3776  C  C      . VAL   B 2  49  ? 21.036  -72.645  -27.149  1.00 54.53  ? 49  VAL   B C      1 
ATOM   3777  O  O      . VAL   B 2  49  ? 21.832  -71.702  -27.017  1.00 49.82  ? 49  VAL   B O      1 
ATOM   3778  C  CB     . VAL   B 2  49  ? 20.292  -73.322  -29.475  1.00 50.26  ? 49  VAL   B CB     1 
ATOM   3779  C  CG1    . VAL   B 2  49  ? 20.399  -71.839  -29.851  1.00 44.49  ? 49  VAL   B CG1    1 
ATOM   3780  C  CG2    . VAL   B 2  49  ? 20.625  -74.213  -30.649  1.00 51.97  ? 49  VAL   B CG2    1 
ATOM   3781  N  N      . TYR   B 2  50  ? 20.016  -72.832  -26.312  1.00 54.60  ? 50  TYR   B N      1 
ATOM   3782  C  CA     . TYR   B 2  50  ? 19.699  -71.903  -25.247  1.00 49.63  ? 50  TYR   B CA     1 
ATOM   3783  C  C      . TYR   B 2  50  ? 19.860  -72.486  -23.851  1.00 51.51  ? 50  TYR   B C      1 
ATOM   3784  O  O      . TYR   B 2  50  ? 20.092  -71.717  -22.916  1.00 53.99  ? 50  TYR   B O      1 
ATOM   3785  C  CB     . TYR   B 2  50  ? 18.263  -71.369  -25.419  1.00 49.07  ? 50  TYR   B CB     1 
ATOM   3786  C  CG     . TYR   B 2  50  ? 18.195  -70.189  -26.363  1.00 49.77  ? 50  TYR   B CG     1 
ATOM   3787  C  CD1    . TYR   B 2  50  ? 18.642  -68.931  -25.966  1.00 50.57  ? 50  TYR   B CD1    1 
ATOM   3788  C  CD2    . TYR   B 2  50  ? 17.723  -70.333  -27.655  1.00 46.82  ? 50  TYR   B CD2    1 
ATOM   3789  C  CE1    . TYR   B 2  50  ? 18.608  -67.849  -26.824  1.00 49.75  ? 50  TYR   B CE1    1 
ATOM   3790  C  CE2    . TYR   B 2  50  ? 17.684  -69.254  -28.523  1.00 48.30  ? 50  TYR   B CE2    1 
ATOM   3791  C  CZ     . TYR   B 2  50  ? 18.126  -68.016  -28.104  1.00 49.67  ? 50  TYR   B CZ     1 
ATOM   3792  O  OH     . TYR   B 2  50  ? 18.084  -66.943  -28.963  1.00 48.13  ? 50  TYR   B OH     1 
ATOM   3793  N  N      . TYR   B 2  51  ? 19.757  -73.808  -23.673  1.00 50.91  ? 51  TYR   B N      1 
ATOM   3794  C  CA     . TYR   B 2  51  ? 19.858  -74.393  -22.340  1.00 56.29  ? 51  TYR   B CA     1 
ATOM   3795  C  C      . TYR   B 2  51  ? 21.091  -75.279  -22.211  1.00 59.29  ? 51  TYR   B C      1 
ATOM   3796  O  O      . TYR   B 2  51  ? 21.517  -75.935  -23.166  1.00 56.25  ? 51  TYR   B O      1 
ATOM   3797  C  CB     . TYR   B 2  51  ? 18.630  -75.221  -21.972  1.00 53.18  ? 51  TYR   B CB     1 
ATOM   3798  C  CG     . TYR   B 2  51  ? 17.335  -74.455  -21.860  1.00 50.86  ? 51  TYR   B CG     1 
ATOM   3799  C  CD1    . TYR   B 2  51  ? 16.709  -73.943  -22.987  1.00 47.43  ? 51  TYR   B CD1    1 
ATOM   3800  C  CD2    . TYR   B 2  51  ? 16.710  -74.276  -20.626  1.00 57.96  ? 51  TYR   B CD2    1 
ATOM   3801  C  CE1    . TYR   B 2  51  ? 15.498  -73.248  -22.897  1.00 51.24  ? 51  TYR   B CE1    1 
ATOM   3802  C  CE2    . TYR   B 2  51  ? 15.487  -73.589  -20.520  1.00 55.37  ? 51  TYR   B CE2    1 
ATOM   3803  C  CZ     . TYR   B 2  51  ? 14.886  -73.079  -21.669  1.00 54.69  ? 51  TYR   B CZ     1 
ATOM   3804  O  OH     . TYR   B 2  51  ? 13.688  -72.391  -21.606  1.00 48.75  ? 51  TYR   B OH     1 
ATOM   3805  N  N      . ASN   B 2  52  ? 21.670  -75.264  -21.012  1.00 63.01  ? 52  ASN   B N      1 
ATOM   3806  C  CA     . ASN   B 2  52  ? 22.703  -76.209  -20.613  1.00 63.67  ? 52  ASN   B CA     1 
ATOM   3807  C  C      . ASN   B 2  52  ? 22.043  -77.403  -19.936  1.00 71.43  ? 52  ASN   B C      1 
ATOM   3808  O  O      . ASN   B 2  52  ? 21.101  -77.248  -19.151  1.00 70.25  ? 52  ASN   B O      1 
ATOM   3809  C  CB     . ASN   B 2  52  ? 23.698  -75.549  -19.661  1.00 55.25  ? 52  ASN   B CB     1 
ATOM   3810  C  CG     . ASN   B 2  52  ? 24.911  -75.004  -20.371  1.00 63.19  ? 52  ASN   B CG     1 
ATOM   3811  O  OD1    . ASN   B 2  52  ? 25.535  -75.695  -21.173  1.00 68.85  ? 52  ASN   B OD1    1 
ATOM   3812  N  ND2    . ASN   B 2  52  ? 25.249  -73.750  -20.093  1.00 62.56  ? 52  ASN   B ND2    1 
ATOM   3813  N  N      . GLU   B 2  53  ? 22.517  -78.601  -20.260  1.00 80.93  ? 53  GLU   B N      1 
ATOM   3814  C  CA     . GLU   B 2  53  ? 21.943  -79.814  -19.694  1.00 84.28  ? 53  GLU   B CA     1 
ATOM   3815  C  C      . GLU   B 2  53  ? 22.705  -80.175  -18.425  1.00 84.02  ? 53  GLU   B C      1 
ATOM   3816  O  O      . GLU   B 2  53  ? 23.909  -80.450  -18.472  1.00 85.54  ? 53  GLU   B O      1 
ATOM   3817  C  CB     . GLU   B 2  53  ? 21.967  -80.960  -20.704  1.00 87.13  ? 53  GLU   B CB     1 
ATOM   3818  C  CG     . GLU   B 2  53  ? 20.911  -82.022  -20.433  1.00 89.48  ? 53  GLU   B CG     1 
ATOM   3819  C  CD     . GLU   B 2  53  ? 20.810  -83.030  -21.552  1.00 94.41  ? 53  GLU   B CD     1 
ATOM   3820  O  OE1    . GLU   B 2  53  ? 21.408  -82.773  -22.624  1.00 94.07  ? 53  GLU   B OE1    1 
ATOM   3821  O  OE2    . GLU   B 2  53  ? 20.138  -84.071  -21.354  1.00 96.16  ? 53  GLU   B OE2    1 
ATOM   3822  N  N      . ALA   B 2  54  ? 22.004  -80.159  -17.299  1.00 89.84  ? 54  ALA   B N      1 
ATOM   3823  C  CA     . ALA   B 2  54  ? 22.575  -80.399  -15.982  1.00 98.32  ? 54  ALA   B CA     1 
ATOM   3824  C  C      . ALA   B 2  54  ? 22.326  -81.833  -15.519  1.00 107.91 ? 54  ALA   B C      1 
ATOM   3825  O  O      . ALA   B 2  54  ? 21.417  -82.521  -15.995  1.00 107.90 ? 54  ALA   B O      1 
ATOM   3826  C  CB     . ALA   B 2  54  ? 21.992  -79.421  -14.961  1.00 98.32  ? 54  ALA   B CB     1 
ATOM   3827  N  N      . THR   B 2  55  ? 23.148  -82.273  -14.565  1.00 110.53 ? 55  THR   B N      1 
ATOM   3828  C  CA     . THR   B 2  55  ? 23.018  -83.623  -14.031  1.00 120.33 ? 55  THR   B CA     1 
ATOM   3829  C  C      . THR   B 2  55  ? 21.616  -83.844  -13.467  1.00 118.56 ? 55  THR   B C      1 
ATOM   3830  O  O      . THR   B 2  55  ? 20.950  -82.914  -13.001  1.00 114.21 ? 55  THR   B O      1 
ATOM   3831  C  CB     . THR   B 2  55  ? 24.077  -83.877  -12.957  1.00 123.18 ? 55  THR   B CB     1 
ATOM   3832  O  OG1    . THR   B 2  55  ? 24.279  -82.678  -12.195  1.00 116.08 ? 55  THR   B OG1    1 
ATOM   3833  C  CG2    . THR   B 2  55  ? 25.399  -84.319  -13.603  1.00 123.62 ? 55  THR   B CG2    1 
ATOM   3834  N  N      . GLY   B 2  56  ? 21.169  -85.096  -13.510  1.00 118.85 ? 56  GLY   B N      1 
ATOM   3835  C  CA     . GLY   B 2  56  ? 19.764  -85.382  -13.331  1.00 111.27 ? 56  GLY   B CA     1 
ATOM   3836  C  C      . GLY   B 2  56  ? 18.937  -85.112  -14.563  1.00 108.29 ? 56  GLY   B C      1 
ATOM   3837  O  O      . GLY   B 2  56  ? 17.704  -85.154  -14.486  1.00 107.89 ? 56  GLY   B O      1 
ATOM   3838  N  N      . ASN   B 2  57  ? 19.584  -84.845  -15.697  1.00 107.01 ? 57  ASN   B N      1 
ATOM   3839  C  CA     . ASN   B 2  57  ? 18.926  -84.429  -16.935  1.00 112.47 ? 57  ASN   B CA     1 
ATOM   3840  C  C      . ASN   B 2  57  ? 17.931  -83.287  -16.676  1.00 106.66 ? 57  ASN   B C      1 
ATOM   3841  O  O      . ASN   B 2  57  ? 16.737  -83.360  -16.989  1.00 99.95  ? 57  ASN   B O      1 
ATOM   3842  C  CB     . ASN   B 2  57  ? 18.271  -85.627  -17.639  1.00 118.04 ? 57  ASN   B CB     1 
ATOM   3843  C  CG     . ASN   B 2  57  ? 19.251  -86.390  -18.548  1.00 117.21 ? 57  ASN   B CG     1 
ATOM   3844  O  OD1    . ASN   B 2  57  ? 19.568  -87.558  -18.307  1.00 116.69 ? 57  ASN   B OD1    1 
ATOM   3845  N  ND2    . ASN   B 2  57  ? 19.734  -85.721  -19.593  1.00 112.46 ? 57  ASN   B ND2    1 
ATOM   3846  N  N      . LYS   B 2  58  ? 18.464  -82.215  -16.081  1.00 104.99 ? 58  LYS   B N      1 
ATOM   3847  C  CA     . LYS   B 2  58  ? 17.796  -80.929  -15.925  1.00 93.25  ? 58  LYS   B CA     1 
ATOM   3848  C  C      . LYS   B 2  58  ? 18.388  -79.923  -16.908  1.00 87.73  ? 58  LYS   B C      1 
ATOM   3849  O  O      . LYS   B 2  58  ? 19.505  -80.095  -17.409  1.00 89.14  ? 58  LYS   B O      1 
ATOM   3850  C  CB     . LYS   B 2  58  ? 17.937  -80.398  -14.495  1.00 86.41  ? 58  LYS   B CB     1 
ATOM   3851  C  CG     . LYS   B 2  58  ? 17.544  -81.389  -13.421  1.00 92.52  ? 58  LYS   B CG     1 
ATOM   3852  C  CD     . LYS   B 2  58  ? 16.035  -81.583  -13.365  1.00 86.27  ? 58  LYS   B CD     1 
ATOM   3853  C  CE     . LYS   B 2  58  ? 15.399  -80.705  -12.283  1.00 80.34  ? 58  LYS   B CE     1 
ATOM   3854  N  NZ     . LYS   B 2  58  ? 15.341  -81.360  -10.941  1.00 80.79  ? 58  LYS   B NZ     1 
ATOM   3855  N  N      . TYR   B 2  59  ? 17.630  -78.864  -17.186  1.00 79.50  ? 59  TYR   B N      1 
ATOM   3856  C  CA     . TYR   B 2  59  ? 18.048  -77.840  -18.136  1.00 76.82  ? 59  TYR   B CA     1 
ATOM   3857  C  C      . TYR   B 2  59  ? 18.163  -76.492  -17.436  1.00 70.39  ? 59  TYR   B C      1 
ATOM   3858  O  O      . TYR   B 2  59  ? 17.228  -76.048  -16.760  1.00 70.49  ? 59  TYR   B O      1 
ATOM   3859  C  CB     . TYR   B 2  59  ? 17.081  -77.772  -19.312  1.00 67.97  ? 59  TYR   B CB     1 
ATOM   3860  C  CG     . TYR   B 2  59  ? 16.905  -79.114  -19.959  1.00 73.31  ? 59  TYR   B CG     1 
ATOM   3861  C  CD1    . TYR   B 2  59  ? 17.752  -79.528  -20.977  1.00 69.93  ? 59  TYR   B CD1    1 
ATOM   3862  C  CD2    . TYR   B 2  59  ? 15.912  -79.988  -19.527  1.00 80.78  ? 59  TYR   B CD2    1 
ATOM   3863  C  CE1    . TYR   B 2  59  ? 17.602  -80.759  -21.573  1.00 74.72  ? 59  TYR   B CE1    1 
ATOM   3864  C  CE2    . TYR   B 2  59  ? 15.753  -81.230  -20.110  1.00 83.35  ? 59  TYR   B CE2    1 
ATOM   3865  C  CZ     . TYR   B 2  59  ? 16.604  -81.611  -21.135  1.00 83.21  ? 59  TYR   B CZ     1 
ATOM   3866  O  OH     . TYR   B 2  59  ? 16.461  -82.846  -21.727  1.00 89.16  ? 59  TYR   B OH     1 
ATOM   3867  N  N      . VAL   B 2  60  ? 19.313  -75.851  -17.602  1.00 64.87  ? 60  VAL   B N      1 
ATOM   3868  C  CA     . VAL   B 2  60  ? 19.632  -74.586  -16.957  1.00 66.37  ? 60  VAL   B CA     1 
ATOM   3869  C  C      . VAL   B 2  60  ? 19.896  -73.553  -18.046  1.00 61.44  ? 60  VAL   B C      1 
ATOM   3870  O  O      . VAL   B 2  60  ? 20.842  -73.714  -18.829  1.00 54.27  ? 60  VAL   B O      1 
ATOM   3871  C  CB     . VAL   B 2  60  ? 20.855  -74.703  -16.033  1.00 67.84  ? 60  VAL   B CB     1 
ATOM   3872  C  CG1    . VAL   B 2  60  ? 21.134  -73.354  -15.368  1.00 62.10  ? 60  VAL   B CG1    1 
ATOM   3873  C  CG2    . VAL   B 2  60  ? 20.670  -75.829  -15.027  1.00 63.97  ? 60  VAL   B CG2    1 
ATOM   3874  N  N      . PRO   B 2  61  ? 19.109  -72.477  -18.128  1.00 58.90  ? 61  PRO   B N      1 
ATOM   3875  C  CA     . PRO   B 2  61  ? 19.354  -71.458  -19.158  1.00 53.94  ? 61  PRO   B CA     1 
ATOM   3876  C  C      . PRO   B 2  61  ? 20.801  -70.985  -19.140  1.00 49.98  ? 61  PRO   B C      1 
ATOM   3877  O  O      . PRO   B 2  61  ? 21.405  -70.792  -18.082  1.00 51.37  ? 61  PRO   B O      1 
ATOM   3878  C  CB     . PRO   B 2  61  ? 18.378  -70.335  -18.781  1.00 43.39  ? 61  PRO   B CB     1 
ATOM   3879  C  CG     . PRO   B 2  61  ? 17.265  -71.052  -18.094  1.00 49.07  ? 61  PRO   B CG     1 
ATOM   3880  C  CD     . PRO   B 2  61  ? 17.915  -72.166  -17.322  1.00 54.05  ? 61  PRO   B CD     1 
ATOM   3881  N  N      . ARG   B 2  62  ? 21.373  -70.831  -20.332  1.00 50.18  ? 62  ARG   B N      1 
ATOM   3882  C  CA     . ARG   B 2  62  ? 22.701  -70.239  -20.468  1.00 50.43  ? 62  ARG   B CA     1 
ATOM   3883  C  C      . ARG   B 2  62  ? 22.534  -68.721  -20.391  1.00 47.72  ? 62  ARG   B C      1 
ATOM   3884  O  O      . ARG   B 2  62  ? 22.691  -67.981  -21.366  1.00 48.59  ? 62  ARG   B O      1 
ATOM   3885  C  CB     . ARG   B 2  62  ? 23.375  -70.696  -21.759  1.00 53.23  ? 62  ARG   B CB     1 
ATOM   3886  C  CG     . ARG   B 2  62  ? 24.896  -70.818  -21.637  1.00 54.80  ? 62  ARG   B CG     1 
ATOM   3887  C  CD     . ARG   B 2  62  ? 25.555  -71.447  -22.860  1.00 59.43  ? 62  ARG   B CD     1 
ATOM   3888  N  NE     . ARG   B 2  62  ? 25.180  -72.840  -23.069  1.00 61.45  ? 62  ARG   B NE     1 
ATOM   3889  C  CZ     . ARG   B 2  62  ? 24.233  -73.226  -23.913  1.00 58.55  ? 62  ARG   B CZ     1 
ATOM   3890  N  NH1    . ARG   B 2  62  ? 23.496  -72.344  -24.564  1.00 53.80  ? 62  ARG   B NH1    1 
ATOM   3891  N  NH2    . ARG   B 2  62  ? 24.028  -74.528  -24.114  1.00 56.02  ? 62  ARG   B NH2    1 
ATOM   3892  N  N      . ALA   B 2  63  ? 22.191  -68.264  -19.183  1.00 47.04  ? 63  ALA   B N      1 
ATOM   3893  C  CA     . ALA   B 2  63  ? 21.780  -66.887  -18.936  1.00 43.65  ? 63  ALA   B CA     1 
ATOM   3894  C  C      . ALA   B 2  63  ? 22.628  -66.261  -17.840  1.00 44.97  ? 63  ALA   B C      1 
ATOM   3895  O  O      . ALA   B 2  63  ? 22.729  -66.798  -16.733  1.00 42.08  ? 63  ALA   B O      1 
ATOM   3896  C  CB     . ALA   B 2  63  ? 20.300  -66.810  -18.546  1.00 43.76  ? 63  ALA   B CB     1 
ATOM   3897  N  N      . ILE   B 2  64  ? 23.211  -65.110  -18.146  1.00 41.46  ? 64  ILE   B N      1 
ATOM   3898  C  CA     . ILE   B 2  64  ? 23.977  -64.336  -17.188  1.00 45.98  ? 64  ILE   B CA     1 
ATOM   3899  C  C      . ILE   B 2  64  ? 23.144  -63.117  -16.816  1.00 44.27  ? 64  ILE   B C      1 
ATOM   3900  O  O      . ILE   B 2  64  ? 22.721  -62.362  -17.699  1.00 46.62  ? 64  ILE   B O      1 
ATOM   3901  C  CB     . ILE   B 2  64  ? 25.337  -63.948  -17.771  1.00 40.43  ? 64  ILE   B CB     1 
ATOM   3902  C  CG1    . ILE   B 2  64  ? 26.023  -65.226  -18.238  1.00 43.93  ? 64  ILE   B CG1    1 
ATOM   3903  C  CG2    . ILE   B 2  64  ? 26.175  -63.221  -16.735  1.00 41.00  ? 64  ILE   B CG2    1 
ATOM   3904  C  CD1    . ILE   B 2  64  ? 27.185  -65.005  -19.179  1.00 50.28  ? 64  ILE   B CD1    1 
ATOM   3905  N  N      . LEU   B 2  65  ? 22.881  -62.943  -15.518  1.00 43.82  ? 65  LEU   B N      1 
ATOM   3906  C  CA     . LEU   B 2  65  ? 22.005  -61.888  -15.012  1.00 44.44  ? 65  LEU   B CA     1 
ATOM   3907  C  C      . LEU   B 2  65  ? 22.832  -60.826  -14.302  1.00 49.91  ? 65  LEU   B C      1 
ATOM   3908  O  O      . LEU   B 2  65  ? 23.536  -61.130  -13.330  1.00 52.48  ? 65  LEU   B O      1 
ATOM   3909  C  CB     . LEU   B 2  65  ? 20.945  -62.440  -14.064  1.00 45.31  ? 65  LEU   B CB     1 
ATOM   3910  C  CG     . LEU   B 2  65  ? 19.917  -63.414  -14.644  1.00 47.78  ? 65  LEU   B CG     1 
ATOM   3911  C  CD1    . LEU   B 2  65  ? 20.167  -64.840  -14.166  1.00 46.90  ? 65  LEU   B CD1    1 
ATOM   3912  C  CD2    . LEU   B 2  65  ? 18.525  -62.964  -14.287  1.00 46.22  ? 65  LEU   B CD2    1 
ATOM   3913  N  N      . VAL   B 2  66  ? 22.705  -59.580  -14.761  1.00 47.39  ? 66  VAL   B N      1 
ATOM   3914  C  CA     . VAL   B 2  66  ? 23.633  -58.497  -14.452  1.00 43.56  ? 66  VAL   B CA     1 
ATOM   3915  C  C      . VAL   B 2  66  ? 22.849  -57.248  -14.095  1.00 45.80  ? 66  VAL   B C      1 
ATOM   3916  O  O      . VAL   B 2  66  ? 22.049  -56.762  -14.903  1.00 43.74  ? 66  VAL   B O      1 
ATOM   3917  C  CB     . VAL   B 2  66  ? 24.546  -58.193  -15.641  1.00 41.83  ? 66  VAL   B CB     1 
ATOM   3918  C  CG1    . VAL   B 2  66  ? 25.409  -56.980  -15.334  1.00 39.81  ? 66  VAL   B CG1    1 
ATOM   3919  C  CG2    . VAL   B 2  66  ? 25.356  -59.423  -16.013  1.00 41.35  ? 66  VAL   B CG2    1 
ATOM   3920  N  N      . ASP   B 2  67  ? 23.101  -56.705  -12.911  1.00 47.55  ? 67  ASP   B N      1 
ATOM   3921  C  CA     . ASP   B 2  67  ? 22.544  -55.407  -12.575  1.00 46.31  ? 67  ASP   B CA     1 
ATOM   3922  C  C      . ASP   B 2  67  ? 23.497  -54.700  -11.620  1.00 45.43  ? 67  ASP   B C      1 
ATOM   3923  O  O      . ASP   B 2  67  ? 24.190  -55.340  -10.829  1.00 41.40  ? 67  ASP   B O      1 
ATOM   3924  C  CB     . ASP   B 2  67  ? 21.141  -55.549  -11.976  1.00 39.44  ? 67  ASP   B CB     1 
ATOM   3925  C  CG     . ASP   B 2  67  ? 20.269  -54.344  -12.238  1.00 42.38  ? 67  ASP   B CG     1 
ATOM   3926  O  OD1    . ASP   B 2  67  ? 20.809  -53.310  -12.742  1.00 40.38  ? 67  ASP   B OD1    1 
ATOM   3927  O  OD2    . ASP   B 2  67  ? 19.045  -54.431  -11.919  1.00 43.81  ? 67  ASP   B OD2    1 
ATOM   3928  N  N      . LEU   B 2  68  ? 23.549  -53.371  -11.720  1.00 44.05  ? 68  LEU   B N      1 
ATOM   3929  C  CA     . LEU   B 2  68  ? 24.275  -52.580  -10.736  1.00 41.69  ? 68  LEU   B CA     1 
ATOM   3930  C  C      . LEU   B 2  68  ? 23.523  -52.436  -9.416   1.00 48.76  ? 68  LEU   B C      1 
ATOM   3931  O  O      . LEU   B 2  68  ? 24.089  -51.913  -8.448   1.00 51.10  ? 68  LEU   B O      1 
ATOM   3932  C  CB     . LEU   B 2  68  ? 24.587  -51.200  -11.306  1.00 35.51  ? 68  LEU   B CB     1 
ATOM   3933  C  CG     . LEU   B 2  68  ? 25.816  -51.245  -12.213  1.00 41.21  ? 68  LEU   B CG     1 
ATOM   3934  C  CD1    . LEU   B 2  68  ? 26.038  -49.917  -12.940  1.00 38.83  ? 68  LEU   B CD1    1 
ATOM   3935  C  CD2    . LEU   B 2  68  ? 27.057  -51.658  -11.424  1.00 36.51  ? 68  LEU   B CD2    1 
ATOM   3936  N  N      . GLU   B 2  69  ? 22.277  -52.907  -9.353   1.00 51.41  ? 69  GLU   B N      1 
ATOM   3937  C  CA     . GLU   B 2  69  ? 21.346  -52.788  -8.238   1.00 52.52  ? 69  GLU   B CA     1 
ATOM   3938  C  C      . GLU   B 2  69  ? 20.769  -54.146  -7.879   1.00 51.62  ? 69  GLU   B C      1 
ATOM   3939  O  O      . GLU   B 2  69  ? 20.497  -54.956  -8.768   1.00 57.17  ? 69  GLU   B O      1 
ATOM   3940  C  CB     . GLU   B 2  69  ? 20.194  -51.863  -8.609   1.00 51.80  ? 69  GLU   B CB     1 
ATOM   3941  C  CG     . GLU   B 2  69  ? 19.878  -50.803  -7.619   1.00 58.86  ? 69  GLU   B CG     1 
ATOM   3942  C  CD     . GLU   B 2  69  ? 18.817  -49.925  -8.178   1.00 67.57  ? 69  GLU   B CD     1 
ATOM   3943  O  OE1    . GLU   B 2  69  ? 17.883  -50.518  -8.752   1.00 68.89  ? 69  GLU   B OE1    1 
ATOM   3944  O  OE2    . GLU   B 2  69  ? 18.920  -48.675  -8.085   1.00 72.66  ? 69  GLU   B OE2    1 
ATOM   3945  N  N      . PRO   B 2  70  ? 20.511  -54.408  -6.600   1.00 54.13  ? 70  PRO   B N      1 
ATOM   3946  C  CA     . PRO   B 2  70  ? 19.962  -55.721  -6.222   1.00 58.08  ? 70  PRO   B CA     1 
ATOM   3947  C  C      . PRO   B 2  70  ? 18.458  -55.824  -6.392   1.00 64.62  ? 70  PRO   B C      1 
ATOM   3948  O  O      . PRO   B 2  70  ? 17.930  -56.945  -6.371   1.00 66.48  ? 70  PRO   B O      1 
ATOM   3949  C  CB     . PRO   B 2  70  ? 20.370  -55.882  -4.756   1.00 57.88  ? 70  PRO   B CB     1 
ATOM   3950  C  CG     . PRO   B 2  70  ? 20.961  -54.566  -4.328   1.00 67.10  ? 70  PRO   B CG     1 
ATOM   3951  C  CD     . PRO   B 2  70  ? 20.913  -53.582  -5.457   1.00 58.94  ? 70  PRO   B CD     1 
ATOM   3952  N  N      . GLY   B 2  71  ? 17.764  -54.705  -6.602   1.00 57.47  ? 71  GLY   B N      1 
ATOM   3953  C  CA     . GLY   B 2  71  ? 16.320  -54.686  -6.774   1.00 62.24  ? 71  GLY   B CA     1 
ATOM   3954  C  C      . GLY   B 2  71  ? 15.664  -55.698  -7.703   1.00 65.99  ? 71  GLY   B C      1 
ATOM   3955  O  O      . GLY   B 2  71  ? 15.162  -56.727  -7.237   1.00 58.31  ? 71  GLY   B O      1 
ATOM   3956  N  N      . THR   B 2  72  ? 15.627  -55.389  -9.012   1.00 71.90  ? 72  THR   B N      1 
ATOM   3957  C  CA     . THR   B 2  72  ? 14.959  -56.250  -9.998   1.00 67.37  ? 72  THR   B CA     1 
ATOM   3958  C  C      . THR   B 2  72  ? 15.457  -57.689  -9.916   1.00 63.10  ? 72  THR   B C      1 
ATOM   3959  O  O      . THR   B 2  72  ? 14.661  -58.634  -9.971   1.00 60.32  ? 72  THR   B O      1 
ATOM   3960  C  CB     . THR   B 2  72  ? 15.163  -55.710  -11.434  1.00 65.68  ? 72  THR   B CB     1 
ATOM   3961  O  OG1    . THR   B 2  72  ? 14.570  -54.412  -11.584  1.00 62.76  ? 72  THR   B OG1    1 
ATOM   3962  C  CG2    . THR   B 2  72  ? 14.548  -56.645  -12.480  1.00 53.41  ? 72  THR   B CG2    1 
ATOM   3963  N  N      . MET   B 2  73  ? 16.771  -57.875  -9.775   1.00 62.09  ? 73  MET   B N      1 
ATOM   3964  C  CA     . MET   B 2  73  ? 17.325  -59.221  -9.832   1.00 64.97  ? 73  MET   B CA     1 
ATOM   3965  C  C      . MET   B 2  73  ? 16.779  -60.096  -8.709   1.00 63.05  ? 73  MET   B C      1 
ATOM   3966  O  O      . MET   B 2  73  ? 16.549  -61.295  -8.899   1.00 65.47  ? 73  MET   B O      1 
ATOM   3967  C  CB     . MET   B 2  73  ? 18.843  -59.143  -9.772   1.00 66.99  ? 73  MET   B CB     1 
ATOM   3968  C  CG     . MET   B 2  73  ? 19.447  -58.485  -11.003  1.00 61.41  ? 73  MET   B CG     1 
ATOM   3969  S  SD     . MET   B 2  73  ? 21.025  -59.228  -11.414  1.00 59.15  ? 73  MET   B SD     1 
ATOM   3970  C  CE     . MET   B 2  73  ? 21.575  -59.775  -9.814   1.00 57.21  ? 73  MET   B CE     1 
ATOM   3971  N  N      . ASP   B 2  74  ? 16.567  -59.518  -7.530   1.00 64.02  ? 74  ASP   B N      1 
ATOM   3972  C  CA     . ASP   B 2  74  ? 15.879  -60.251  -6.475   1.00 63.28  ? 74  ASP   B CA     1 
ATOM   3973  C  C      . ASP   B 2  74  ? 14.447  -60.602  -6.877   1.00 62.02  ? 74  ASP   B C      1 
ATOM   3974  O  O      . ASP   B 2  74  ? 13.948  -61.679  -6.537   1.00 67.96  ? 74  ASP   B O      1 
ATOM   3975  C  CB     . ASP   B 2  74  ? 15.889  -59.435  -5.185   1.00 63.54  ? 74  ASP   B CB     1 
ATOM   3976  C  CG     . ASP   B 2  74  ? 17.096  -59.720  -4.341   1.00 68.19  ? 74  ASP   B CG     1 
ATOM   3977  O  OD1    . ASP   B 2  74  ? 17.690  -60.813  -4.510   1.00 73.34  ? 74  ASP   B OD1    1 
ATOM   3978  O  OD2    . ASP   B 2  74  ? 17.454  -58.852  -3.522   1.00 69.60  ? 74  ASP   B OD2    1 
ATOM   3979  N  N      . SER   B 2  75  ? 13.767  -59.705  -7.595   1.00 65.15  ? 75  SER   B N      1 
ATOM   3980  C  CA     . SER   B 2  75  ? 12.428  -60.013  -8.087   1.00 66.22  ? 75  SER   B CA     1 
ATOM   3981  C  C      . SER   B 2  75  ? 12.446  -61.139  -9.104   1.00 69.38  ? 75  SER   B C      1 
ATOM   3982  O  O      . SER   B 2  75  ? 11.486  -61.919  -9.182   1.00 68.35  ? 75  SER   B O      1 
ATOM   3983  C  CB     . SER   B 2  75  ? 11.787  -58.782  -8.713   1.00 60.14  ? 75  SER   B CB     1 
ATOM   3984  O  OG     . SER   B 2  75  ? 11.941  -57.673  -7.863   1.00 70.84  ? 75  SER   B OG     1 
ATOM   3985  N  N      . VAL   B 2  76  ? 13.498  -61.227  -9.915   1.00 63.49  ? 76  VAL   B N      1 
ATOM   3986  C  CA     . VAL   B 2  76  ? 13.605  -62.375  -10.798  1.00 62.34  ? 76  VAL   B CA     1 
ATOM   3987  C  C      . VAL   B 2  76  ? 13.709  -63.644  -9.966   1.00 62.40  ? 76  VAL   B C      1 
ATOM   3988  O  O      . VAL   B 2  76  ? 12.943  -64.594  -10.158  1.00 65.25  ? 76  VAL   B O      1 
ATOM   3989  C  CB     . VAL   B 2  76  ? 14.785  -62.209  -11.772  1.00 62.61  ? 76  VAL   B CB     1 
ATOM   3990  C  CG1    . VAL   B 2  76  ? 15.121  -63.540  -12.431  1.00 59.91  ? 76  VAL   B CG1    1 
ATOM   3991  C  CG2    . VAL   B 2  76  ? 14.448  -61.164  -12.842  1.00 53.64  ? 76  VAL   B CG2    1 
ATOM   3992  N  N      . ARG   B 2  77  ? 14.611  -63.659  -8.985   1.00 61.21  ? 77  ARG   B N      1 
ATOM   3993  C  CA     . ARG   B 2  77  ? 14.790  -64.888  -8.224   1.00 64.42  ? 77  ARG   B CA     1 
ATOM   3994  C  C      . ARG   B 2  77  ? 13.498  -65.295  -7.544   1.00 69.52  ? 77  ARG   B C      1 
ATOM   3995  O  O      . ARG   B 2  77  ? 13.257  -66.490  -7.325   1.00 70.39  ? 77  ARG   B O      1 
ATOM   3996  C  CB     . ARG   B 2  77  ? 15.905  -64.737  -7.195   1.00 66.44  ? 77  ARG   B CB     1 
ATOM   3997  C  CG     . ARG   B 2  77  ? 16.544  -66.055  -6.772   1.00 66.98  ? 77  ARG   B CG     1 
ATOM   3998  C  CD     . ARG   B 2  77  ? 18.029  -65.877  -6.484   1.00 65.60  ? 77  ARG   B CD     1 
ATOM   3999  N  NE     . ARG   B 2  77  ? 18.334  -64.497  -6.120   1.00 71.44  ? 77  ARG   B NE     1 
ATOM   4000  C  CZ     . ARG   B 2  77  ? 19.551  -63.967  -6.140   1.00 71.75  ? 77  ARG   B CZ     1 
ATOM   4001  N  NH1    . ARG   B 2  77  ? 20.610  -64.687  -6.482   1.00 64.93  ? 77  ARG   B NH1    1 
ATOM   4002  N  NH2    . ARG   B 2  77  ? 19.709  -62.685  -5.810   1.00 64.16  ? 77  ARG   B NH2    1 
ATOM   4003  N  N      . SER   B 2  78  ? 12.650  -64.316  -7.224   1.00 72.40  ? 78  SER   B N      1 
ATOM   4004  C  CA     . SER   B 2  78  ? 11.357  -64.548  -6.593   1.00 70.50  ? 78  SER   B CA     1 
ATOM   4005  C  C      . SER   B 2  78  ? 10.270  -64.890  -7.600   1.00 68.82  ? 78  SER   B C      1 
ATOM   4006  O  O      . SER   B 2  78  ? 9.200   -65.364  -7.203   1.00 70.08  ? 78  SER   B O      1 
ATOM   4007  C  CB     . SER   B 2  78  ? 10.951  -63.303  -5.809   1.00 70.41  ? 78  SER   B CB     1 
ATOM   4008  O  OG     . SER   B 2  78  ? 11.826  -63.092  -4.711   1.00 78.22  ? 78  SER   B OG     1 
ATOM   4009  N  N      . GLY   B 2  79  ? 10.526  -64.658  -8.887   1.00 72.17  ? 79  GLY   B N      1 
ATOM   4010  C  CA     . GLY   B 2  79  ? 9.538   -64.850  -9.907   1.00 68.18  ? 79  GLY   B CA     1 
ATOM   4011  C  C      . GLY   B 2  79  ? 9.269   -66.313  -10.171  1.00 69.06  ? 79  GLY   B C      1 
ATOM   4012  O  O      . GLY   B 2  79  ? 9.858   -67.210  -9.548   1.00 68.35  ? 79  GLY   B O      1 
ATOM   4013  N  N      . PRO   B 2  80  ? 8.367   -66.565  -11.124  1.00 75.87  ? 80  PRO   B N      1 
ATOM   4014  C  CA     . PRO   B 2  80  ? 7.895   -67.953  -11.345  1.00 77.00  ? 80  PRO   B CA     1 
ATOM   4015  C  C      . PRO   B 2  80  ? 8.995   -68.914  -11.773  1.00 73.09  ? 80  PRO   B C      1 
ATOM   4016  O  O      . PRO   B 2  80  ? 9.097   -70.030  -11.239  1.00 70.31  ? 80  PRO   B O      1 
ATOM   4017  C  CB     . PRO   B 2  80  ? 6.830   -67.782  -12.440  1.00 77.28  ? 80  PRO   B CB     1 
ATOM   4018  C  CG     . PRO   B 2  80  ? 7.172   -66.447  -13.117  1.00 71.90  ? 80  PRO   B CG     1 
ATOM   4019  C  CD     . PRO   B 2  80  ? 7.721   -65.588  -12.023  1.00 68.98  ? 80  PRO   B CD     1 
ATOM   4020  N  N      . PHE   B 2  81  ? 9.809   -68.511  -12.746  1.00 66.44  ? 81  PHE   B N      1 
ATOM   4021  C  CA     . PHE   B 2  81  ? 10.924  -69.307  -13.223  1.00 64.02  ? 81  PHE   B CA     1 
ATOM   4022  C  C      . PHE   B 2  81  ? 12.238  -68.900  -12.576  1.00 60.93  ? 81  PHE   B C      1 
ATOM   4023  O  O      . PHE   B 2  81  ? 13.298  -69.348  -13.020  1.00 58.32  ? 81  PHE   B O      1 
ATOM   4024  C  CB     . PHE   B 2  81  ? 11.031  -69.199  -14.750  1.00 67.96  ? 81  PHE   B CB     1 
ATOM   4025  C  CG     . PHE   B 2  81  ? 10.216  -70.228  -15.497  1.00 66.75  ? 81  PHE   B CG     1 
ATOM   4026  C  CD1    . PHE   B 2  81  ? 8.836   -70.141  -15.547  1.00 65.61  ? 81  PHE   B CD1    1 
ATOM   4027  C  CD2    . PHE   B 2  81  ? 10.835  -71.294  -16.128  1.00 67.93  ? 81  PHE   B CD2    1 
ATOM   4028  C  CE1    . PHE   B 2  81  ? 8.089   -71.091  -16.226  1.00 66.76  ? 81  PHE   B CE1    1 
ATOM   4029  C  CE2    . PHE   B 2  81  ? 10.088  -72.252  -16.806  1.00 69.18  ? 81  PHE   B CE2    1 
ATOM   4030  C  CZ     . PHE   B 2  81  ? 8.714   -72.148  -16.853  1.00 66.65  ? 81  PHE   B CZ     1 
ATOM   4031  N  N      . GLY   B 2  82  ? 12.193  -68.057  -11.542  1.00 60.54  ? 82  GLY   B N      1 
ATOM   4032  C  CA     . GLY   B 2  82  ? 13.424  -67.571  -10.944  1.00 63.07  ? 82  GLY   B CA     1 
ATOM   4033  C  C      . GLY   B 2  82  ? 14.355  -68.682  -10.506  1.00 62.31  ? 82  GLY   B C      1 
ATOM   4034  O  O      . GLY   B 2  82  ? 15.578  -68.530  -10.540  1.00 59.20  ? 82  GLY   B O      1 
ATOM   4035  N  N      . GLN   B 2  83  ? 13.799  -69.816  -10.101  1.00 61.95  ? 83  GLN   B N      1 
ATOM   4036  C  CA     . GLN   B 2  83  ? 14.646  -70.903  -9.641   1.00 63.15  ? 83  GLN   B CA     1 
ATOM   4037  C  C      . GLN   B 2  83  ? 15.367  -71.600  -10.787  1.00 66.24  ? 83  GLN   B C      1 
ATOM   4038  O  O      . GLN   B 2  83  ? 16.316  -72.353  -10.540  1.00 65.93  ? 83  GLN   B O      1 
ATOM   4039  C  CB     . GLN   B 2  83  ? 13.812  -71.911  -8.854   1.00 70.51  ? 83  GLN   B CB     1 
ATOM   4040  C  CG     . GLN   B 2  83  ? 12.777  -71.289  -7.915   1.00 76.51  ? 83  GLN   B CG     1 
ATOM   4041  C  CD     . GLN   B 2  83  ? 13.389  -70.300  -6.924   1.00 81.69  ? 83  GLN   B CD     1 
ATOM   4042  O  OE1    . GLN   B 2  83  ? 14.608  -70.282  -6.702   1.00 75.94  ? 83  GLN   B OE1    1 
ATOM   4043  N  NE2    . GLN   B 2  83  ? 12.537  -69.481  -6.311   1.00 81.46  ? 83  GLN   B NE2    1 
ATOM   4044  N  N      . ILE   B 2  84  ? 14.945  -71.382  -12.033  1.00 65.64  ? 84  ILE   B N      1 
ATOM   4045  C  CA     . ILE   B 2  84  ? 15.590  -72.116  -13.116  1.00 65.24  ? 84  ILE   B CA     1 
ATOM   4046  C  C      . ILE   B 2  84  ? 16.999  -71.602  -13.331  1.00 58.57  ? 84  ILE   B C      1 
ATOM   4047  O  O      . ILE   B 2  84  ? 17.879  -72.360  -13.744  1.00 63.88  ? 84  ILE   B O      1 
ATOM   4048  C  CB     . ILE   B 2  84  ? 14.764  -72.063  -14.421  1.00 63.78  ? 84  ILE   B CB     1 
ATOM   4049  C  CG1    . ILE   B 2  84  ? 15.239  -73.144  -15.385  1.00 61.71  ? 84  ILE   B CG1    1 
ATOM   4050  C  CG2    . ILE   B 2  84  ? 14.855  -70.710  -15.092  1.00 60.87  ? 84  ILE   B CG2    1 
ATOM   4051  C  CD1    . ILE   B 2  84  ? 14.128  -73.753  -16.198  1.00 72.12  ? 84  ILE   B CD1    1 
ATOM   4052  N  N      . PHE   B 2  85  ? 17.251  -70.334  -13.025  1.00 61.71  ? 85  PHE   B N      1 
ATOM   4053  C  CA     . PHE   B 2  85  ? 18.523  -69.710  -13.372  1.00 60.33  ? 85  PHE   B CA     1 
ATOM   4054  C  C      . PHE   B 2  85  ? 19.635  -70.203  -12.463  1.00 60.11  ? 85  PHE   B C      1 
ATOM   4055  O  O      . PHE   B 2  85  ? 19.471  -70.261  -11.242  1.00 68.38  ? 85  PHE   B O      1 
ATOM   4056  C  CB     . PHE   B 2  85  ? 18.410  -68.191  -13.278  1.00 51.90  ? 85  PHE   B CB     1 
ATOM   4057  C  CG     . PHE   B 2  85  ? 17.505  -67.604  -14.310  1.00 54.52  ? 85  PHE   B CG     1 
ATOM   4058  C  CD1    . PHE   B 2  85  ? 17.937  -67.457  -15.615  1.00 49.61  ? 85  PHE   B CD1    1 
ATOM   4059  C  CD2    . PHE   B 2  85  ? 16.210  -67.222  -13.983  1.00 54.57  ? 85  PHE   B CD2    1 
ATOM   4060  C  CE1    . PHE   B 2  85  ? 17.103  -66.920  -16.571  1.00 47.94  ? 85  PHE   B CE1    1 
ATOM   4061  C  CE2    . PHE   B 2  85  ? 15.372  -66.695  -14.938  1.00 53.85  ? 85  PHE   B CE2    1 
ATOM   4062  C  CZ     . PHE   B 2  85  ? 15.821  -66.545  -16.239  1.00 49.36  ? 85  PHE   B CZ     1 
ATOM   4063  N  N      . ARG   B 2  86  ? 20.762  -70.553  -13.064  1.00 56.82  ? 86  ARG   B N      1 
ATOM   4064  C  CA     . ARG   B 2  86  ? 21.962  -70.968  -12.354  1.00 55.40  ? 86  ARG   B CA     1 
ATOM   4065  C  C      . ARG   B 2  86  ? 22.408  -69.866  -11.393  1.00 60.30  ? 86  ARG   B C      1 
ATOM   4066  O  O      . ARG   B 2  86  ? 22.805  -68.780  -11.839  1.00 62.22  ? 86  ARG   B O      1 
ATOM   4067  C  CB     . ARG   B 2  86  ? 23.042  -71.308  -13.378  1.00 54.58  ? 86  ARG   B CB     1 
ATOM   4068  C  CG     . ARG   B 2  86  ? 24.465  -71.300  -12.882  1.00 61.66  ? 86  ARG   B CG     1 
ATOM   4069  C  CD     . ARG   B 2  86  ? 25.407  -71.884  -13.949  1.00 66.92  ? 86  ARG   B CD     1 
ATOM   4070  N  NE     . ARG   B 2  86  ? 26.467  -72.640  -13.301  1.00 75.50  ? 86  ARG   B NE     1 
ATOM   4071  C  CZ     . ARG   B 2  86  ? 27.568  -72.089  -12.811  1.00 79.55  ? 86  ARG   B CZ     1 
ATOM   4072  N  NH1    . ARG   B 2  86  ? 27.828  -70.801  -12.984  1.00 72.83  ? 86  ARG   B NH1    1 
ATOM   4073  N  NH2    . ARG   B 2  86  ? 28.418  -72.841  -12.113  1.00 74.69  ? 86  ARG   B NH2    1 
ATOM   4074  N  N      . PRO   B 2  87  ? 22.365  -70.103  -10.075  1.00 58.53  ? 87  PRO   B N      1 
ATOM   4075  C  CA     . PRO   B 2  87  ? 22.556  -68.988  -9.127   1.00 53.23  ? 87  PRO   B CA     1 
ATOM   4076  C  C      . PRO   B 2  87  ? 23.905  -68.306  -9.233   1.00 55.65  ? 87  PRO   B C      1 
ATOM   4077  O  O      . PRO   B 2  87  ? 23.977  -67.081  -9.075   1.00 54.92  ? 87  PRO   B O      1 
ATOM   4078  C  CB     . PRO   B 2  87  ? 22.357  -69.655  -7.757   1.00 55.16  ? 87  PRO   B CB     1 
ATOM   4079  C  CG     . PRO   B 2  87  ? 22.528  -71.122  -8.004   1.00 57.48  ? 87  PRO   B CG     1 
ATOM   4080  C  CD     . PRO   B 2  87  ? 22.041  -71.368  -9.390   1.00 58.42  ? 87  PRO   B CD     1 
ATOM   4081  N  N      . ASP   B 2  88  ? 24.984  -69.050  -9.492   1.00 58.61  ? 88  ASP   B N      1 
ATOM   4082  C  CA     . ASP   B 2  88  ? 26.270  -68.398  -9.723   1.00 55.96  ? 88  ASP   B CA     1 
ATOM   4083  C  C      . ASP   B 2  88  ? 26.214  -67.314  -10.795  1.00 61.63  ? 88  ASP   B C      1 
ATOM   4084  O  O      . ASP   B 2  88  ? 27.126  -66.481  -10.869  1.00 63.69  ? 88  ASP   B O      1 
ATOM   4085  C  CB     . ASP   B 2  88  ? 27.326  -69.408  -10.141  1.00 63.07  ? 88  ASP   B CB     1 
ATOM   4086  C  CG     . ASP   B 2  88  ? 27.948  -70.092  -8.973   1.00 69.16  ? 88  ASP   B CG     1 
ATOM   4087  O  OD1    . ASP   B 2  88  ? 28.242  -69.384  -7.986   1.00 70.08  ? 88  ASP   B OD1    1 
ATOM   4088  O  OD2    . ASP   B 2  88  ? 28.190  -71.318  -9.058   1.00 72.64  ? 88  ASP   B OD2    1 
ATOM   4089  N  N      . ASN   B 2  89  ? 25.198  -67.324  -11.656  1.00 56.86  ? 89  ASN   B N      1 
ATOM   4090  C  CA     . ASN   B 2  89  ? 25.134  -66.396  -12.773  1.00 56.86  ? 89  ASN   B CA     1 
ATOM   4091  C  C      . ASN   B 2  89  ? 24.393  -65.105  -12.431  1.00 55.74  ? 89  ASN   B C      1 
ATOM   4092  O  O      . ASN   B 2  89  ? 24.055  -64.331  -13.336  1.00 52.09  ? 89  ASN   B O      1 
ATOM   4093  C  CB     . ASN   B 2  89  ? 24.491  -67.084  -13.980  1.00 57.23  ? 89  ASN   B CB     1 
ATOM   4094  C  CG     . ASN   B 2  89  ? 25.398  -68.128  -14.604  1.00 56.93  ? 89  ASN   B CG     1 
ATOM   4095  O  OD1    . ASN   B 2  89  ? 26.493  -68.385  -14.118  1.00 58.34  ? 89  ASN   B OD1    1 
ATOM   4096  N  ND2    . ASN   B 2  89  ? 24.928  -68.756  -15.676  1.00 61.58  ? 89  ASN   B ND2    1 
ATOM   4097  N  N      . PHE   B 2  90  ? 24.125  -64.863  -11.153  1.00 52.43  ? 90  PHE   B N      1 
ATOM   4098  C  CA     . PHE   B 2  90  ? 23.605  -63.585  -10.697  1.00 47.79  ? 90  PHE   B CA     1 
ATOM   4099  C  C      . PHE   B 2  90  ? 24.808  -62.734  -10.308  1.00 52.15  ? 90  PHE   B C      1 
ATOM   4100  O  O      . PHE   B 2  90  ? 25.443  -62.983  -9.282   1.00 54.17  ? 90  PHE   B O      1 
ATOM   4101  C  CB     . PHE   B 2  90  ? 22.652  -63.775  -9.523   1.00 49.60  ? 90  PHE   B CB     1 
ATOM   4102  C  CG     . PHE   B 2  90  ? 21.312  -64.369  -9.893   1.00 54.34  ? 90  PHE   B CG     1 
ATOM   4103  C  CD1    . PHE   B 2  90  ? 21.202  -65.701  -10.270  1.00 52.72  ? 90  PHE   B CD1    1 
ATOM   4104  C  CD2    . PHE   B 2  90  ? 20.146  -63.609  -9.806   1.00 56.67  ? 90  PHE   B CD2    1 
ATOM   4105  C  CE1    . PHE   B 2  90  ? 19.954  -66.261  -10.579  1.00 52.38  ? 90  PHE   B CE1    1 
ATOM   4106  C  CE2    . PHE   B 2  90  ? 18.899  -64.168  -10.114  1.00 59.11  ? 90  PHE   B CE2    1 
ATOM   4107  C  CZ     . PHE   B 2  90  ? 18.810  -65.489  -10.499  1.00 56.65  ? 90  PHE   B CZ     1 
ATOM   4108  N  N      . VAL   B 2  91  ? 25.146  -61.752  -11.137  1.00 51.52  ? 91  VAL   B N      1 
ATOM   4109  C  CA     . VAL   B 2  91  ? 26.271  -60.856  -10.884  1.00 48.30  ? 91  VAL   B CA     1 
ATOM   4110  C  C      . VAL   B 2  91  ? 25.703  -59.456  -10.685  1.00 52.50  ? 91  VAL   B C      1 
ATOM   4111  O  O      . VAL   B 2  91  ? 25.000  -58.938  -11.565  1.00 53.34  ? 91  VAL   B O      1 
ATOM   4112  C  CB     . VAL   B 2  91  ? 27.292  -60.893  -12.033  1.00 46.79  ? 91  VAL   B CB     1 
ATOM   4113  C  CG1    . VAL   B 2  91  ? 28.353  -59.841  -11.839  1.00 49.77  ? 91  VAL   B CG1    1 
ATOM   4114  C  CG2    . VAL   B 2  91  ? 27.922  -62.265  -12.115  1.00 44.88  ? 91  VAL   B CG2    1 
ATOM   4115  N  N      . PHE   B 2  92  ? 25.982  -58.850  -9.525   1.00 55.96  ? 92  PHE   B N      1 
ATOM   4116  C  CA     . PHE   B 2  92  ? 25.352  -57.566  -9.226   1.00 55.07  ? 92  PHE   B CA     1 
ATOM   4117  C  C      . PHE   B 2  92  ? 26.119  -56.770  -8.174   1.00 52.65  ? 92  PHE   B C      1 
ATOM   4118  O  O      . PHE   B 2  92  ? 26.593  -57.329  -7.185   1.00 59.60  ? 92  PHE   B O      1 
ATOM   4119  C  CB     . PHE   B 2  92  ? 23.897  -57.748  -8.765   1.00 55.78  ? 92  PHE   B CB     1 
ATOM   4120  C  CG     . PHE   B 2  92  ? 23.724  -58.604  -7.548   1.00 58.02  ? 92  PHE   B CG     1 
ATOM   4121  C  CD1    . PHE   B 2  92  ? 23.570  -59.984  -7.661   1.00 64.89  ? 92  PHE   B CD1    1 
ATOM   4122  C  CD2    . PHE   B 2  92  ? 23.678  -58.023  -6.281   1.00 66.04  ? 92  PHE   B CD2    1 
ATOM   4123  C  CE1    . PHE   B 2  92  ? 23.379  -60.779  -6.530   1.00 70.90  ? 92  PHE   B CE1    1 
ATOM   4124  C  CE2    . PHE   B 2  92  ? 23.494  -58.805  -5.145   1.00 68.30  ? 92  PHE   B CE2    1 
ATOM   4125  C  CZ     . PHE   B 2  92  ? 23.346  -60.188  -5.267   1.00 70.07  ? 92  PHE   B CZ     1 
ATOM   4126  N  N      . GLY   B 2  93  ? 26.215  -55.456  -8.399   1.00 49.92  ? 93  GLY   B N      1 
ATOM   4127  C  CA     . GLY   B 2  93  ? 26.671  -54.513  -7.399   1.00 54.25  ? 93  GLY   B CA     1 
ATOM   4128  C  C      . GLY   B 2  93  ? 25.524  -54.027  -6.537   1.00 53.92  ? 93  GLY   B C      1 
ATOM   4129  O  O      . GLY   B 2  93  ? 24.434  -54.607  -6.518   1.00 54.84  ? 93  GLY   B O      1 
ATOM   4130  N  N      . GLN   B 2  94  ? 25.772  -52.926  -5.828   1.00 55.02  ? 94  GLN   B N      1 
ATOM   4131  C  CA     . GLN   B 2  94  ? 24.798  -52.377  -4.891   1.00 52.72  ? 94  GLN   B CA     1 
ATOM   4132  C  C      . GLN   B 2  94  ? 24.506  -50.893  -5.066   1.00 54.27  ? 94  GLN   B C      1 
ATOM   4133  O  O      . GLN   B 2  94  ? 23.457  -50.436  -4.598   1.00 58.22  ? 94  GLN   B O      1 
ATOM   4134  C  CB     . GLN   B 2  94  ? 25.258  -52.612  -3.447   1.00 50.36  ? 94  GLN   B CB     1 
ATOM   4135  C  CG     . GLN   B 2  94  ? 25.130  -54.049  -2.984   1.00 58.75  ? 94  GLN   B CG     1 
ATOM   4136  C  CD     . GLN   B 2  94  ? 23.725  -54.385  -2.489   1.00 64.75  ? 94  GLN   B CD     1 
ATOM   4137  O  OE1    . GLN   B 2  94  ? 22.935  -53.493  -2.169   1.00 68.00  ? 94  GLN   B OE1    1 
ATOM   4138  N  NE2    . GLN   B 2  94  ? 23.413  -55.675  -2.423   1.00 62.06  ? 94  GLN   B NE2    1 
ATOM   4139  N  N      . SER   B 2  95  ? 25.377  -50.128  -5.713   1.00 56.35  ? 95  SER   B N      1 
ATOM   4140  C  CA     . SER   B 2  95  ? 25.215  -48.682  -5.732   1.00 56.10  ? 95  SER   B CA     1 
ATOM   4141  C  C      . SER   B 2  95  ? 24.105  -48.226  -6.661   1.00 59.03  ? 95  SER   B C      1 
ATOM   4142  O  O      . SER   B 2  95  ? 23.610  -47.104  -6.518   1.00 61.09  ? 95  SER   B O      1 
ATOM   4143  C  CB     . SER   B 2  95  ? 26.523  -48.015  -6.156   1.00 62.17  ? 95  SER   B CB     1 
ATOM   4144  O  OG     . SER   B 2  95  ? 27.517  -48.130  -5.151   1.00 70.65  ? 95  SER   B OG     1 
ATOM   4145  N  N      . GLY   B 2  96  ? 23.706  -49.054  -7.609   1.00 54.17  ? 96  GLY   B N      1 
ATOM   4146  C  CA     . GLY   B 2  96  ? 22.862  -48.571  -8.679   1.00 48.72  ? 96  GLY   B CA     1 
ATOM   4147  C  C      . GLY   B 2  96  ? 23.615  -47.692  -9.663   1.00 47.32  ? 96  GLY   B C      1 
ATOM   4148  O  O      . GLY   B 2  96  ? 24.759  -47.278  -9.420   1.00 50.29  ? 96  GLY   B O      1 
ATOM   4149  N  N      . ALA   B 2  97  ? 22.961  -47.399  -10.784  1.00 34.75  ? 97  ALA   B N      1 
ATOM   4150  C  CA     . ALA   B 2  97  ? 23.515  -46.582  -11.853  1.00 33.20  ? 97  ALA   B CA     1 
ATOM   4151  C  C      . ALA   B 2  97  ? 22.708  -45.313  -12.084  1.00 33.80  ? 97  ALA   B C      1 
ATOM   4152  O  O      . ALA   B 2  97  ? 22.993  -44.577  -13.039  1.00 29.90  ? 97  ALA   B O      1 
ATOM   4153  C  CB     . ALA   B 2  97  ? 23.599  -47.387  -13.164  1.00 28.97  ? 97  ALA   B CB     1 
ATOM   4154  N  N      . GLY   B 2  98  ? 21.681  -45.062  -11.268  1.00 35.73  ? 98  GLY   B N      1 
ATOM   4155  C  CA     . GLY   B 2  98  ? 20.874  -43.858  -11.382  1.00 33.35  ? 98  GLY   B CA     1 
ATOM   4156  C  C      . GLY   B 2  98  ? 20.472  -43.369  -12.769  1.00 35.10  ? 98  GLY   B C      1 
ATOM   4157  O  O      . GLY   B 2  98  ? 20.503  -42.159  -13.030  1.00 33.28  ? 98  GLY   B O      1 
ATOM   4158  N  N      . ASN   B 2  99  ? 20.044  -44.264  -13.662  1.00 29.67  ? 99  ASN   B N      1 
ATOM   4159  C  CA     . ASN   B 2  99  ? 19.593  -43.833  -14.979  1.00 35.61  ? 99  ASN   B CA     1 
ATOM   4160  C  C      . ASN   B 2  99  ? 20.654  -43.017  -15.707  1.00 32.65  ? 99  ASN   B C      1 
ATOM   4161  O  O      . ASN   B 2  99  ? 20.333  -42.156  -16.520  1.00 38.15  ? 99  ASN   B O      1 
ATOM   4162  C  CB     . ASN   B 2  99  ? 18.308  -43.010  -14.879  1.00 34.17  ? 99  ASN   B CB     1 
ATOM   4163  C  CG     . ASN   B 2  99  ? 17.137  -43.837  -14.485  1.00 39.44  ? 99  ASN   B CG     1 
ATOM   4164  O  OD1    . ASN   B 2  99  ? 16.804  -44.814  -15.162  1.00 48.04  ? 99  ASN   B OD1    1 
ATOM   4165  N  ND2    . ASN   B 2  99  ? 16.500  -43.476  -13.379  1.00 31.39  ? 99  ASN   B ND2    1 
ATOM   4166  N  N      . ASN   B 2  100 ? 21.920  -43.258  -15.410  1.00 36.31  ? 100 ASN   B N      1 
ATOM   4167  C  CA     . ASN   B 2  100 ? 23.028  -42.415  -15.863  1.00 33.84  ? 100 ASN   B CA     1 
ATOM   4168  C  C      . ASN   B 2  100 ? 23.964  -43.263  -16.711  1.00 37.70  ? 100 ASN   B C      1 
ATOM   4169  O  O      . ASN   B 2  100 ? 24.584  -44.197  -16.196  1.00 37.95  ? 100 ASN   B O      1 
ATOM   4170  C  CB     . ASN   B 2  100 ? 23.776  -41.810  -14.678  1.00 28.17  ? 100 ASN   B CB     1 
ATOM   4171  C  CG     . ASN   B 2  100 ? 24.777  -40.773  -15.112  1.00 39.77  ? 100 ASN   B CG     1 
ATOM   4172  O  OD1    . ASN   B 2  100 ? 25.354  -40.887  -16.190  1.00 40.98  ? 100 ASN   B OD1    1 
ATOM   4173  N  ND2    . ASN   B 2  100 ? 24.971  -39.734  -14.300  1.00 38.29  ? 100 ASN   B ND2    1 
ATOM   4174  N  N      . TRP   B 2  101 ? 24.050  -42.955  -18.013  1.00 39.99  ? 101 TRP   B N      1 
ATOM   4175  C  CA     . TRP   B 2  101 ? 24.891  -43.749  -18.905  1.00 35.13  ? 101 TRP   B CA     1 
ATOM   4176  C  C      . TRP   B 2  101 ? 26.329  -43.759  -18.429  1.00 38.62  ? 101 TRP   B C      1 
ATOM   4177  O  O      . TRP   B 2  101 ? 26.989  -44.805  -18.460  1.00 41.42  ? 101 TRP   B O      1 
ATOM   4178  C  CB     . TRP   B 2  101 ? 24.818  -43.225  -20.335  1.00 38.47  ? 101 TRP   B CB     1 
ATOM   4179  C  CG     . TRP   B 2  101 ? 25.400  -44.184  -21.367  1.00 43.02  ? 101 TRP   B CG     1 
ATOM   4180  C  CD1    . TRP   B 2  101 ? 24.759  -45.241  -21.978  1.00 41.07  ? 101 TRP   B CD1    1 
ATOM   4181  C  CD2    . TRP   B 2  101 ? 26.733  -44.156  -21.913  1.00 43.91  ? 101 TRP   B CD2    1 
ATOM   4182  N  NE1    . TRP   B 2  101 ? 25.623  -45.865  -22.856  1.00 44.25  ? 101 TRP   B NE1    1 
ATOM   4183  C  CE2    . TRP   B 2  101 ? 26.832  -45.216  -22.838  1.00 40.39  ? 101 TRP   B CE2    1 
ATOM   4184  C  CE3    . TRP   B 2  101 ? 27.854  -43.336  -21.704  1.00 43.22  ? 101 TRP   B CE3    1 
ATOM   4185  C  CZ2    . TRP   B 2  101 ? 28.000  -45.475  -23.550  1.00 36.97  ? 101 TRP   B CZ2    1 
ATOM   4186  C  CZ3    . TRP   B 2  101 ? 29.017  -43.599  -22.428  1.00 38.80  ? 101 TRP   B CZ3    1 
ATOM   4187  C  CH2    . TRP   B 2  101 ? 29.074  -44.661  -23.333  1.00 35.57  ? 101 TRP   B CH2    1 
ATOM   4188  N  N      . ALA   B 2  102 ? 26.824  -42.614  -17.947  1.00 38.15  ? 102 ALA   B N      1 
ATOM   4189  C  CA     . ALA   B 2  102 ? 28.211  -42.545  -17.504  1.00 34.63  ? 102 ALA   B CA     1 
ATOM   4190  C  C      . ALA   B 2  102 ? 28.473  -43.501  -16.346  1.00 37.69  ? 102 ALA   B C      1 
ATOM   4191  O  O      . ALA   B 2  102 ? 29.502  -44.182  -16.324  1.00 39.04  ? 102 ALA   B O      1 
ATOM   4192  C  CB     . ALA   B 2  102 ? 28.578  -41.112  -17.132  1.00 35.42  ? 102 ALA   B CB     1 
ATOM   4193  N  N      . LYS   B 2  103 ? 27.550  -43.593  -15.384  1.00 39.05  ? 103 LYS   B N      1 
ATOM   4194  C  CA     . LYS   B 2  103 ? 27.776  -44.515  -14.272  1.00 37.89  ? 103 LYS   B CA     1 
ATOM   4195  C  C      . LYS   B 2  103 ? 27.810  -45.962  -14.742  1.00 39.68  ? 103 LYS   B C      1 
ATOM   4196  O  O      . LYS   B 2  103 ? 28.463  -46.802  -14.112  1.00 40.81  ? 103 LYS   B O      1 
ATOM   4197  C  CB     . LYS   B 2  103 ? 26.707  -44.345  -13.191  1.00 34.88  ? 103 LYS   B CB     1 
ATOM   4198  C  CG     . LYS   B 2  103 ? 26.663  -42.962  -12.567  1.00 39.73  ? 103 LYS   B CG     1 
ATOM   4199  C  CD     . LYS   B 2  103 ? 25.756  -42.941  -11.357  1.00 41.52  ? 103 LYS   B CD     1 
ATOM   4200  C  CE     . LYS   B 2  103 ? 25.653  -41.543  -10.758  1.00 36.80  ? 103 LYS   B CE     1 
ATOM   4201  N  NZ     . LYS   B 2  103 ? 25.675  -41.641  -9.275   1.00 43.00  ? 103 LYS   B NZ     1 
ATOM   4202  N  N      . GLY   B 2  104 ? 27.111  -46.277  -15.835  1.00 40.68  ? 104 GLY   B N      1 
ATOM   4203  C  CA     . GLY   B 2  104 ? 27.015  -47.641  -16.318  1.00 35.02  ? 104 GLY   B CA     1 
ATOM   4204  C  C      . GLY   B 2  104 ? 28.303  -47.998  -17.014  1.00 37.86  ? 104 GLY   B C      1 
ATOM   4205  O  O      . GLY   B 2  104 ? 28.854  -49.086  -16.837  1.00 40.26  ? 104 GLY   B O      1 
ATOM   4206  N  N      . HIS   B 2  105 ? 28.820  -47.032  -17.759  1.00 35.05  ? 105 HIS   B N      1 
ATOM   4207  C  CA     . HIS   B 2  105 ? 29.880  -47.276  -18.715  1.00 38.04  ? 105 HIS   B CA     1 
ATOM   4208  C  C      . HIS   B 2  105 ? 31.280  -47.026  -18.165  1.00 41.17  ? 105 HIS   B C      1 
ATOM   4209  O  O      . HIS   B 2  105 ? 32.219  -47.725  -18.570  1.00 41.88  ? 105 HIS   B O      1 
ATOM   4210  C  CB     . HIS   B 2  105 ? 29.658  -46.399  -19.951  1.00 35.99  ? 105 HIS   B CB     1 
ATOM   4211  C  CG     . HIS   B 2  105 ? 30.291  -46.939  -21.193  1.00 40.84  ? 105 HIS   B CG     1 
ATOM   4212  N  ND1    . HIS   B 2  105 ? 29.772  -48.012  -21.885  1.00 38.81  ? 105 HIS   B ND1    1 
ATOM   4213  C  CD2    . HIS   B 2  105 ? 31.406  -46.558  -21.865  1.00 41.05  ? 105 HIS   B CD2    1 
ATOM   4214  C  CE1    . HIS   B 2  105 ? 30.532  -48.259  -22.939  1.00 43.48  ? 105 HIS   B CE1    1 
ATOM   4215  N  NE2    . HIS   B 2  105 ? 31.530  -47.391  -22.951  1.00 40.21  ? 105 HIS   B NE2    1 
ATOM   4216  N  N      . TYR   B 2  106 ? 31.447  -46.051  -17.266  1.00 39.28  ? 106 TYR   B N      1 
ATOM   4217  C  CA     . TYR   B 2  106 ? 32.757  -45.517  -16.896  1.00 36.51  ? 106 TYR   B CA     1 
ATOM   4218  C  C      . TYR   B 2  106 ? 33.103  -45.617  -15.410  1.00 42.59  ? 106 TYR   B C      1 
ATOM   4219  O  O      . TYR   B 2  106 ? 34.254  -45.892  -15.071  1.00 49.47  ? 106 TYR   B O      1 
ATOM   4220  C  CB     . TYR   B 2  106 ? 32.846  -44.061  -17.315  1.00 34.56  ? 106 TYR   B CB     1 
ATOM   4221  C  CG     . TYR   B 2  106 ? 32.924  -43.833  -18.796  1.00 36.02  ? 106 TYR   B CG     1 
ATOM   4222  C  CD1    . TYR   B 2  106 ? 33.859  -44.509  -19.577  1.00 37.02  ? 106 TYR   B CD1    1 
ATOM   4223  C  CD2    . TYR   B 2  106 ? 32.079  -42.908  -19.412  1.00 30.97  ? 106 TYR   B CD2    1 
ATOM   4224  C  CE1    . TYR   B 2  106 ? 33.952  -44.283  -20.938  1.00 35.63  ? 106 TYR   B CE1    1 
ATOM   4225  C  CE2    . TYR   B 2  106 ? 32.165  -42.660  -20.754  1.00 39.79  ? 106 TYR   B CE2    1 
ATOM   4226  C  CZ     . TYR   B 2  106 ? 33.101  -43.357  -21.522  1.00 41.82  ? 106 TYR   B CZ     1 
ATOM   4227  O  OH     . TYR   B 2  106 ? 33.168  -43.121  -22.869  1.00 37.62  ? 106 TYR   B OH     1 
ATOM   4228  N  N      . THR   B 2  107 ? 32.165  -45.383  -14.502  1.00 42.72  ? 107 THR   B N      1 
ATOM   4229  C  CA     . THR   B 2  107 ? 32.496  -45.459  -13.084  1.00 44.20  ? 107 THR   B CA     1 
ATOM   4230  C  C      . THR   B 2  107 ? 31.932  -46.725  -12.452  1.00 41.18  ? 107 THR   B C      1 
ATOM   4231  O  O      . THR   B 2  107 ? 32.639  -47.726  -12.319  1.00 49.94  ? 107 THR   B O      1 
ATOM   4232  C  CB     . THR   B 2  107 ? 31.983  -44.218  -12.378  1.00 43.48  ? 107 THR   B CB     1 
ATOM   4233  O  OG1    . THR   B 2  107 ? 30.576  -44.124  -12.609  1.00 51.73  ? 107 THR   B OG1    1 
ATOM   4234  C  CG2    . THR   B 2  107 ? 32.667  -42.970  -12.945  1.00 36.58  ? 107 THR   B CG2    1 
ATOM   4235  N  N      . GLU   B 2  108 ? 30.658  -46.709  -12.090  1.00 40.60  ? 108 GLU   B N      1 
ATOM   4236  C  CA     . GLU   B 2  108 ? 30.080  -47.837  -11.370  1.00 40.19  ? 108 GLU   B CA     1 
ATOM   4237  C  C      . GLU   B 2  108 ? 30.185  -49.145  -12.154  1.00 38.89  ? 108 GLU   B C      1 
ATOM   4238  O  O      . GLU   B 2  108 ? 30.534  -50.184  -11.593  1.00 43.26  ? 108 GLU   B O      1 
ATOM   4239  C  CB     . GLU   B 2  108 ? 28.632  -47.520  -11.040  1.00 40.21  ? 108 GLU   B CB     1 
ATOM   4240  C  CG     . GLU   B 2  108 ? 28.439  -46.171  -10.469  1.00 38.04  ? 108 GLU   B CG     1 
ATOM   4241  C  CD     . GLU   B 2  108 ? 28.823  -46.124  -9.017   1.00 48.32  ? 108 GLU   B CD     1 
ATOM   4242  O  OE1    . GLU   B 2  108 ? 28.777  -47.187  -8.367   1.00 47.42  ? 108 GLU   B OE1    1 
ATOM   4243  O  OE2    . GLU   B 2  108 ? 29.133  -45.014  -8.515   1.00 60.15  ? 108 GLU   B OE2    1 
ATOM   4244  N  N      . GLY   B 2  109 ? 29.839  -49.128  -13.445  1.00 46.92  ? 109 GLY   B N      1 
ATOM   4245  C  CA     . GLY   B 2  109 ? 29.889  -50.357  -14.233  1.00 41.91  ? 109 GLY   B CA     1 
ATOM   4246  C  C      . GLY   B 2  109 ? 31.295  -50.923  -14.349  1.00 47.97  ? 109 GLY   B C      1 
ATOM   4247  O  O      . GLY   B 2  109 ? 31.496  -52.140  -14.296  1.00 45.86  ? 109 GLY   B O      1 
ATOM   4248  N  N      . ALA   B 2  110 ? 32.291  -50.045  -14.500  1.00 49.99  ? 110 ALA   B N      1 
ATOM   4249  C  CA     . ALA   B 2  110 ? 33.676  -50.494  -14.544  1.00 45.81  ? 110 ALA   B CA     1 
ATOM   4250  C  C      . ALA   B 2  110 ? 34.004  -51.401  -13.358  1.00 50.76  ? 110 ALA   B C      1 
ATOM   4251  O  O      . ALA   B 2  110 ? 34.559  -52.495  -13.535  1.00 49.93  ? 110 ALA   B O      1 
ATOM   4252  C  CB     . ALA   B 2  110 ? 34.599  -49.282  -14.594  1.00 46.23  ? 110 ALA   B CB     1 
ATOM   4253  N  N      . GLU   B 2  111 ? 33.648  -50.982  -12.134  1.00 50.62  ? 111 GLU   B N      1 
ATOM   4254  C  CA     . GLU   B 2  111 ? 33.922  -51.840  -10.980  1.00 49.28  ? 111 GLU   B CA     1 
ATOM   4255  C  C      . GLU   B 2  111 ? 33.447  -53.272  -11.234  1.00 47.27  ? 111 GLU   B C      1 
ATOM   4256  O  O      . GLU   B 2  111 ? 34.200  -54.228  -11.036  1.00 50.29  ? 111 GLU   B O      1 
ATOM   4257  C  CB     . GLU   B 2  111 ? 33.291  -51.285  -9.690   1.00 48.60  ? 111 GLU   B CB     1 
ATOM   4258  C  CG     . GLU   B 2  111 ? 33.655  -49.847  -9.260   1.00 51.58  ? 111 GLU   B CG     1 
ATOM   4259  C  CD     . GLU   B 2  111 ? 33.402  -49.630  -7.750   1.00 72.76  ? 111 GLU   B CD     1 
ATOM   4260  O  OE1    . GLU   B 2  111 ? 33.518  -50.646  -7.026   1.00 70.96  ? 111 GLU   B OE1    1 
ATOM   4261  O  OE2    . GLU   B 2  111 ? 33.078  -48.489  -7.287   1.00 71.94  ? 111 GLU   B OE2    1 
ATOM   4262  N  N      . LEU   B 2  112 ? 32.216  -53.437  -11.731  1.00 47.81  ? 112 LEU   B N      1 
ATOM   4263  C  CA     . LEU   B 2  112 ? 31.546  -54.736  -11.758  1.00 42.14  ? 112 LEU   B CA     1 
ATOM   4264  C  C      . LEU   B 2  112 ? 31.773  -55.555  -13.035  1.00 46.63  ? 112 LEU   B C      1 
ATOM   4265  O  O      . LEU   B 2  112 ? 31.511  -56.761  -13.018  1.00 45.87  ? 112 LEU   B O      1 
ATOM   4266  C  CB     . LEU   B 2  112 ? 30.047  -54.509  -11.529  1.00 44.06  ? 112 LEU   B CB     1 
ATOM   4267  C  CG     . LEU   B 2  112 ? 29.027  -55.646  -11.482  1.00 47.96  ? 112 LEU   B CG     1 
ATOM   4268  C  CD1    . LEU   B 2  112 ? 29.280  -56.567  -10.319  1.00 43.92  ? 112 LEU   B CD1    1 
ATOM   4269  C  CD2    . LEU   B 2  112 ? 27.621  -55.053  -11.410  1.00 45.55  ? 112 LEU   B CD2    1 
ATOM   4270  N  N      . VAL   B 2  113 ? 32.280  -54.959  -14.124  1.00 44.89  ? 113 VAL   B N      1 
ATOM   4271  C  CA     . VAL   B 2  113 ? 32.238  -55.628  -15.426  1.00 43.50  ? 113 VAL   B CA     1 
ATOM   4272  C  C      . VAL   B 2  113 ? 33.082  -56.904  -15.438  1.00 51.51  ? 113 VAL   B C      1 
ATOM   4273  O  O      . VAL   B 2  113 ? 32.691  -57.903  -16.061  1.00 50.56  ? 113 VAL   B O      1 
ATOM   4274  C  CB     . VAL   B 2  113 ? 32.657  -54.668  -16.556  1.00 44.44  ? 113 VAL   B CB     1 
ATOM   4275  C  CG1    . VAL   B 2  113 ? 34.141  -54.394  -16.502  1.00 46.93  ? 113 VAL   B CG1    1 
ATOM   4276  C  CG2    . VAL   B 2  113 ? 32.328  -55.284  -17.892  1.00 40.10  ? 113 VAL   B CG2    1 
ATOM   4277  N  N      . ASP   B 2  114 ? 34.263  -56.894  -14.788  1.00 51.38  ? 114 ASP   B N      1 
ATOM   4278  C  CA     . ASP   B 2  114 ? 35.135  -58.073  -14.819  1.00 42.35  ? 114 ASP   B CA     1 
ATOM   4279  C  C      . ASP   B 2  114 ? 34.441  -59.295  -14.233  1.00 47.36  ? 114 ASP   B C      1 
ATOM   4280  O  O      . ASP   B 2  114 ? 34.585  -60.406  -14.750  1.00 48.89  ? 114 ASP   B O      1 
ATOM   4281  C  CB     . ASP   B 2  114 ? 36.431  -57.831  -14.045  1.00 48.68  ? 114 ASP   B CB     1 
ATOM   4282  C  CG     . ASP   B 2  114 ? 37.433  -56.993  -14.799  1.00 50.47  ? 114 ASP   B CG     1 
ATOM   4283  O  OD1    . ASP   B 2  114 ? 37.260  -56.763  -16.010  1.00 54.83  ? 114 ASP   B OD1    1 
ATOM   4284  O  OD2    . ASP   B 2  114 ? 38.421  -56.569  -14.165  1.00 69.42  ? 114 ASP   B OD2    1 
ATOM   4285  N  N      . SER   B 2  115 ? 33.725  -59.125  -13.122  1.00 47.37  ? 115 SER   B N      1 
ATOM   4286  C  CA     . SER   B 2  115 ? 33.012  -60.263  -12.559  1.00 42.01  ? 115 SER   B CA     1 
ATOM   4287  C  C      . SER   B 2  115 ? 31.981  -60.800  -13.532  1.00 51.23  ? 115 SER   B C      1 
ATOM   4288  O  O      . SER   B 2  115 ? 31.745  -62.014  -13.570  1.00 52.97  ? 115 SER   B O      1 
ATOM   4289  C  CB     . SER   B 2  115 ? 32.366  -59.869  -11.241  1.00 36.54  ? 115 SER   B CB     1 
ATOM   4290  O  OG     . SER   B 2  115 ? 32.730  -58.536  -10.959  1.00 55.34  ? 115 SER   B OG     1 
ATOM   4291  N  N      . VAL   B 2  116 ? 31.345  -59.924  -14.319  1.00 49.41  ? 116 VAL   B N      1 
ATOM   4292  C  CA     . VAL   B 2  116 ? 30.434  -60.407  -15.348  1.00 45.91  ? 116 VAL   B CA     1 
ATOM   4293  C  C      . VAL   B 2  116 ? 31.223  -61.172  -16.398  1.00 47.95  ? 116 VAL   B C      1 
ATOM   4294  O  O      . VAL   B 2  116 ? 30.889  -62.313  -16.744  1.00 49.44  ? 116 VAL   B O      1 
ATOM   4295  C  CB     . VAL   B 2  116 ? 29.629  -59.236  -15.955  1.00 54.22  ? 116 VAL   B CB     1 
ATOM   4296  C  CG1    . VAL   B 2  116 ? 28.701  -59.703  -17.090  1.00 42.35  ? 116 VAL   B CG1    1 
ATOM   4297  C  CG2    . VAL   B 2  116 ? 28.819  -58.493  -14.874  1.00 49.32  ? 116 VAL   B CG2    1 
ATOM   4298  N  N      . LEU   B 2  117 ? 32.337  -60.590  -16.853  1.00 45.20  ? 117 LEU   B N      1 
ATOM   4299  C  CA     . LEU   B 2  117 ? 33.162  -61.259  -17.854  1.00 46.42  ? 117 LEU   B CA     1 
ATOM   4300  C  C      . LEU   B 2  117 ? 33.649  -62.624  -17.382  1.00 49.31  ? 117 LEU   B C      1 
ATOM   4301  O  O      . LEU   B 2  117 ? 33.914  -63.503  -18.214  1.00 55.53  ? 117 LEU   B O      1 
ATOM   4302  C  CB     . LEU   B 2  117 ? 34.336  -60.371  -18.249  1.00 36.31  ? 117 LEU   B CB     1 
ATOM   4303  C  CG     . LEU   B 2  117 ? 33.757  -59.395  -19.260  1.00 45.49  ? 117 LEU   B CG     1 
ATOM   4304  C  CD1    . LEU   B 2  117 ? 34.718  -58.274  -19.579  1.00 54.66  ? 117 LEU   B CD1    1 
ATOM   4305  C  CD2    . LEU   B 2  117 ? 33.267  -60.114  -20.536  1.00 48.72  ? 117 LEU   B CD2    1 
ATOM   4306  N  N      . ASP   B 2  118 ? 33.745  -62.837  -16.064  1.00 48.97  ? 118 ASP   B N      1 
ATOM   4307  C  CA     . ASP   B 2  118 ? 34.167  -64.138  -15.564  1.00 47.91  ? 118 ASP   B CA     1 
ATOM   4308  C  C      . ASP   B 2  118 ? 33.059  -65.175  -15.709  1.00 52.68  ? 118 ASP   B C      1 
ATOM   4309  O  O      . ASP   B 2  118 ? 33.317  -66.314  -16.125  1.00 58.41  ? 118 ASP   B O      1 
ATOM   4310  C  CB     . ASP   B 2  118 ? 34.630  -64.021  -14.114  1.00 46.84  ? 118 ASP   B CB     1 
ATOM   4311  C  CG     . ASP   B 2  118 ? 35.961  -63.289  -13.989  1.00 49.79  ? 118 ASP   B CG     1 
ATOM   4312  O  OD1    . ASP   B 2  118 ? 36.673  -63.177  -15.011  1.00 44.41  ? 118 ASP   B OD1    1 
ATOM   4313  O  OD2    . ASP   B 2  118 ? 36.275  -62.808  -12.873  1.00 54.68  ? 118 ASP   B OD2    1 
ATOM   4314  N  N      . VAL   B 2  119 ? 31.818  -64.812  -15.392  1.00 46.53  ? 119 VAL   B N      1 
ATOM   4315  C  CA     . VAL   B 2  119 ? 30.739  -65.772  -15.605  1.00 54.46  ? 119 VAL   B CA     1 
ATOM   4316  C  C      . VAL   B 2  119 ? 30.538  -66.024  -17.096  1.00 59.16  ? 119 VAL   B C      1 
ATOM   4317  O  O      . VAL   B 2  119 ? 30.209  -67.142  -17.516  1.00 56.39  ? 119 VAL   B O      1 
ATOM   4318  C  CB     . VAL   B 2  119 ? 29.443  -65.295  -14.932  1.00 49.80  ? 119 VAL   B CB     1 
ATOM   4319  C  CG1    . VAL   B 2  119 ? 28.327  -66.273  -15.208  1.00 49.92  ? 119 VAL   B CG1    1 
ATOM   4320  C  CG2    . VAL   B 2  119 ? 29.664  -65.127  -13.444  1.00 47.85  ? 119 VAL   B CG2    1 
ATOM   4321  N  N      . VAL   B 2  120 ? 30.726  -64.988  -17.919  1.00 54.59  ? 120 VAL   B N      1 
ATOM   4322  C  CA     . VAL   B 2  120 ? 30.654  -65.183  -19.358  1.00 52.08  ? 120 VAL   B CA     1 
ATOM   4323  C  C      . VAL   B 2  120 ? 31.685  -66.213  -19.780  1.00 57.61  ? 120 VAL   B C      1 
ATOM   4324  O  O      . VAL   B 2  120 ? 31.395  -67.127  -20.564  1.00 55.28  ? 120 VAL   B O      1 
ATOM   4325  C  CB     . VAL   B 2  120 ? 30.856  -63.848  -20.095  1.00 52.42  ? 120 VAL   B CB     1 
ATOM   4326  C  CG1    . VAL   B 2  120 ? 31.412  -64.117  -21.475  1.00 59.19  ? 120 VAL   B CG1    1 
ATOM   4327  C  CG2    . VAL   B 2  120 ? 29.555  -63.060  -20.179  1.00 44.99  ? 120 VAL   B CG2    1 
ATOM   4328  N  N      . ARG   B 2  121 ? 32.900  -66.100  -19.236  1.00 61.88  ? 121 ARG   B N      1 
ATOM   4329  C  CA     . ARG   B 2  121 ? 33.967  -67.029  -19.594  1.00 59.67  ? 121 ARG   B CA     1 
ATOM   4330  C  C      . ARG   B 2  121 ? 33.636  -68.464  -19.185  1.00 59.06  ? 121 ARG   B C      1 
ATOM   4331  O  O      . ARG   B 2  121 ? 33.781  -69.393  -19.987  1.00 61.81  ? 121 ARG   B O      1 
ATOM   4332  C  CB     . ARG   B 2  121 ? 35.279  -66.587  -18.971  1.00 53.02  ? 121 ARG   B CB     1 
ATOM   4333  C  CG     . ARG   B 2  121 ? 36.438  -67.189  -19.698  1.00 58.18  ? 121 ARG   B CG     1 
ATOM   4334  C  CD     . ARG   B 2  121 ? 37.680  -66.436  -19.429  1.00 54.52  ? 121 ARG   B CD     1 
ATOM   4335  N  NE     . ARG   B 2  121 ? 37.518  -65.005  -19.643  1.00 52.81  ? 121 ARG   B NE     1 
ATOM   4336  C  CZ     . ARG   B 2  121 ? 37.475  -64.112  -18.661  1.00 56.02  ? 121 ARG   B CZ     1 
ATOM   4337  N  NH1    . ARG   B 2  121 ? 37.441  -64.483  -17.388  1.00 49.39  ? 121 ARG   B NH1    1 
ATOM   4338  N  NH2    . ARG   B 2  121 ? 37.483  -62.818  -18.962  1.00 49.03  ? 121 ARG   B NH2    1 
ATOM   4339  N  N      . LYS   B 2  122 ? 33.199  -68.676  -17.937  1.00 59.62  ? 122 LYS   B N      1 
ATOM   4340  C  CA     . LYS   B 2  122 ? 32.842  -70.035  -17.528  1.00 64.20  ? 122 LYS   B CA     1 
ATOM   4341  C  C      . LYS   B 2  122 ? 31.822  -70.640  -18.491  1.00 62.94  ? 122 LYS   B C      1 
ATOM   4342  O  O      . LYS   B 2  122 ? 31.977  -71.785  -18.930  1.00 65.79  ? 122 LYS   B O      1 
ATOM   4343  C  CB     . LYS   B 2  122 ? 32.313  -70.058  -16.087  1.00 52.04  ? 122 LYS   B CB     1 
ATOM   4344  N  N      . GLU   B 2  123 ? 30.798  -69.868  -18.864  1.00 58.73  ? 123 GLU   B N      1 
ATOM   4345  C  CA     . GLU   B 2  123 ? 29.790  -70.357  -19.801  1.00 60.61  ? 123 GLU   B CA     1 
ATOM   4346  C  C      . GLU   B 2  123 ? 30.380  -70.635  -21.187  1.00 64.22  ? 123 GLU   B C      1 
ATOM   4347  O  O      . GLU   B 2  123 ? 30.088  -71.673  -21.793  1.00 62.86  ? 123 GLU   B O      1 
ATOM   4348  C  CB     . GLU   B 2  123 ? 28.640  -69.355  -19.900  1.00 55.92  ? 123 GLU   B CB     1 
ATOM   4349  C  CG     . GLU   B 2  123 ? 27.720  -69.388  -18.714  1.00 51.86  ? 123 GLU   B CG     1 
ATOM   4350  C  CD     . GLU   B 2  123 ? 26.869  -70.625  -18.718  1.00 58.33  ? 123 GLU   B CD     1 
ATOM   4351  O  OE1    . GLU   B 2  123 ? 27.119  -71.483  -19.607  1.00 63.24  ? 123 GLU   B OE1    1 
ATOM   4352  O  OE2    . GLU   B 2  123 ? 25.973  -70.751  -17.838  1.00 57.81  ? 123 GLU   B OE2    1 
ATOM   4353  N  N      . SER   B 2  124 ? 31.188  -69.708  -21.723  1.00 64.00  ? 124 SER   B N      1 
ATOM   4354  C  CA     . SER   B 2  124 ? 31.771  -69.915  -23.050  1.00 57.92  ? 124 SER   B CA     1 
ATOM   4355  C  C      . SER   B 2  124 ? 32.599  -71.188  -23.109  1.00 62.60  ? 124 SER   B C      1 
ATOM   4356  O  O      . SER   B 2  124 ? 32.620  -71.875  -24.138  1.00 63.68  ? 124 SER   B O      1 
ATOM   4357  C  CB     . SER   B 2  124 ? 32.645  -68.732  -23.456  1.00 56.68  ? 124 SER   B CB     1 
ATOM   4358  O  OG     . SER   B 2  124 ? 31.899  -67.760  -24.162  1.00 61.73  ? 124 SER   B OG     1 
ATOM   4359  N  N      . GLU   B 2  125 ? 33.315  -71.506  -22.027  1.00 63.99  ? 125 GLU   B N      1 
ATOM   4360  C  CA     . GLU   B 2  125 ? 34.228  -72.645  -22.069  1.00 68.04  ? 125 GLU   B CA     1 
ATOM   4361  C  C      . GLU   B 2  125 ? 33.467  -73.960  -22.103  1.00 63.31  ? 125 GLU   B C      1 
ATOM   4362  O  O      . GLU   B 2  125 ? 33.850  -74.884  -22.828  1.00 66.67  ? 125 GLU   B O      1 
ATOM   4363  C  CB     . GLU   B 2  125 ? 35.181  -72.603  -20.882  1.00 68.40  ? 125 GLU   B CB     1 
ATOM   4364  C  CG     . GLU   B 2  125 ? 36.185  -71.479  -20.957  1.00 71.57  ? 125 GLU   B CG     1 
ATOM   4365  C  CD     . GLU   B 2  125 ? 36.705  -71.086  -19.581  1.00 79.02  ? 125 GLU   B CD     1 
ATOM   4366  O  OE1    . GLU   B 2  125 ? 36.217  -71.664  -18.564  1.00 66.09  ? 125 GLU   B OE1    1 
ATOM   4367  O  OE2    . GLU   B 2  125 ? 37.599  -70.197  -19.531  1.00 79.58  ? 125 GLU   B OE2    1 
ATOM   4368  N  N      . SER   B 2  126 ? 32.395  -74.067  -21.323  1.00 56.10  ? 126 SER   B N      1 
ATOM   4369  C  CA     . SER   B 2  126 ? 31.487  -75.184  -21.492  1.00 57.39  ? 126 SER   B CA     1 
ATOM   4370  C  C      . SER   B 2  126 ? 31.083  -75.398  -22.944  1.00 64.10  ? 126 SER   B C      1 
ATOM   4371  O  O      . SER   B 2  126 ? 30.727  -76.519  -23.318  1.00 68.51  ? 126 SER   B O      1 
ATOM   4372  C  CB     . SER   B 2  126 ? 30.248  -74.956  -20.638  1.00 67.01  ? 126 SER   B CB     1 
ATOM   4373  O  OG     . SER   B 2  126 ? 29.127  -75.646  -21.183  1.00 71.16  ? 126 SER   B OG     1 
ATOM   4374  N  N      . CYS   B 2  127 ? 31.146  -74.364  -23.776  1.00 65.19  ? 127 CYS   B N      1 
ATOM   4375  C  CA     . CYS   B 2  127 ? 30.442  -74.397  -25.051  1.00 64.49  ? 127 CYS   B CA     1 
ATOM   4376  C  C      . CYS   B 2  127 ? 31.194  -75.206  -26.086  1.00 60.35  ? 127 CYS   B C      1 
ATOM   4377  O  O      . CYS   B 2  127 ? 32.421  -75.161  -26.157  1.00 63.35  ? 127 CYS   B O      1 
ATOM   4378  C  CB     . CYS   B 2  127 ? 30.201  -72.982  -25.578  1.00 60.50  ? 127 CYS   B CB     1 
ATOM   4379  S  SG     . CYS   B 2  127 ? 28.877  -72.173  -24.688  1.00 57.31  ? 127 CYS   B SG     1 
ATOM   4380  N  N      . ASP   B 2  128 ? 30.426  -75.923  -26.910  1.00 65.66  ? 128 ASP   B N      1 
ATOM   4381  C  CA     . ASP   B 2  128 ? 30.954  -76.806  -27.945  1.00 62.33  ? 128 ASP   B CA     1 
ATOM   4382  C  C      . ASP   B 2  128 ? 31.283  -76.041  -29.230  1.00 65.75  ? 128 ASP   B C      1 
ATOM   4383  O  O      . ASP   B 2  128 ? 32.400  -76.149  -29.752  1.00 67.04  ? 128 ASP   B O      1 
ATOM   4384  C  CB     . ASP   B 2  128 ? 29.942  -77.921  -28.222  1.00 64.40  ? 128 ASP   B CB     1 
ATOM   4385  C  CG     . ASP   B 2  128 ? 30.515  -79.028  -29.068  1.00 79.10  ? 128 ASP   B CG     1 
ATOM   4386  O  OD1    . ASP   B 2  128 ? 31.273  -79.846  -28.506  1.00 87.01  ? 128 ASP   B OD1    1 
ATOM   4387  O  OD2    . ASP   B 2  128 ? 30.248  -79.053  -30.293  1.00 77.14  ? 128 ASP   B OD2    1 
ATOM   4388  N  N      . CYS   B 2  129 ? 30.313  -75.281  -29.768  1.00 61.34  ? 129 CYS   B N      1 
ATOM   4389  C  CA     . CYS   B 2  129 ? 30.546  -74.312  -30.849  1.00 58.65  ? 129 CYS   B CA     1 
ATOM   4390  C  C      . CYS   B 2  129 ? 29.691  -73.082  -30.532  1.00 58.16  ? 129 CYS   B C      1 
ATOM   4391  O  O      . CYS   B 2  129 ? 28.487  -73.046  -30.806  1.00 56.65  ? 129 CYS   B O      1 
ATOM   4392  C  CB     . CYS   B 2  129 ? 30.227  -74.893  -32.227  1.00 56.21  ? 129 CYS   B CB     1 
ATOM   4393  S  SG     . CYS   B 2  129 ? 30.590  -73.781  -33.643  1.00 67.96  ? 129 CYS   B SG     1 
ATOM   4394  N  N      . LEU   B 2  130 ? 30.315  -72.071  -29.956  1.00 52.04  ? 130 LEU   B N      1 
ATOM   4395  C  CA     . LEU   B 2  130 ? 29.583  -70.915  -29.476  1.00 48.56  ? 130 LEU   B CA     1 
ATOM   4396  C  C      . LEU   B 2  130 ? 29.293  -69.966  -30.632  1.00 50.38  ? 130 LEU   B C      1 
ATOM   4397  O  O      . LEU   B 2  130 ? 30.224  -69.452  -31.264  1.00 53.86  ? 130 LEU   B O      1 
ATOM   4398  C  CB     . LEU   B 2  130 ? 30.394  -70.232  -28.385  1.00 48.59  ? 130 LEU   B CB     1 
ATOM   4399  C  CG     . LEU   B 2  130 ? 30.030  -68.812  -27.998  1.00 44.83  ? 130 LEU   B CG     1 
ATOM   4400  C  CD1    . LEU   B 2  130 ? 28.792  -68.842  -27.126  1.00 41.78  ? 130 LEU   B CD1    1 
ATOM   4401  C  CD2    . LEU   B 2  130 ? 31.218  -68.210  -27.281  1.00 41.37  ? 130 LEU   B CD2    1 
ATOM   4402  N  N      . GLN   B 2  131 ? 28.002  -69.725  -30.907  1.00 49.59  ? 131 GLN   B N      1 
ATOM   4403  C  CA     . GLN   B 2  131 ? 27.630  -68.821  -31.997  1.00 46.24  ? 131 GLN   B CA     1 
ATOM   4404  C  C      . GLN   B 2  131 ? 27.940  -67.388  -31.634  1.00 47.05  ? 131 GLN   B C      1 
ATOM   4405  O  O      . GLN   B 2  131 ? 28.410  -66.604  -32.472  1.00 49.83  ? 131 GLN   B O      1 
ATOM   4406  C  CB     . GLN   B 2  131 ? 26.147  -68.917  -32.304  1.00 44.29  ? 131 GLN   B CB     1 
ATOM   4407  C  CG     . GLN   B 2  131 ? 25.604  -70.294  -32.408  1.00 48.12  ? 131 GLN   B CG     1 
ATOM   4408  C  CD     . GLN   B 2  131 ? 24.131  -70.268  -32.648  1.00 45.96  ? 131 GLN   B CD     1 
ATOM   4409  O  OE1    . GLN   B 2  131 ? 23.645  -69.535  -33.511  1.00 45.12  ? 131 GLN   B OE1    1 
ATOM   4410  N  NE2    . GLN   B 2  131 ? 23.394  -71.047  -31.863  1.00 49.21  ? 131 GLN   B NE2    1 
ATOM   4411  N  N      . GLY   B 2  132 ? 27.653  -67.027  -30.405  1.00 45.52  ? 132 GLY   B N      1 
ATOM   4412  C  CA     . GLY   B 2  132 ? 27.786  -65.660  -29.982  1.00 43.16  ? 132 GLY   B CA     1 
ATOM   4413  C  C      . GLY   B 2  132 ? 26.845  -65.394  -28.829  1.00 43.55  ? 132 GLY   B C      1 
ATOM   4414  O  O      . GLY   B 2  132 ? 26.514  -66.296  -28.060  1.00 40.83  ? 132 GLY   B O      1 
ATOM   4415  N  N      . PHE   B 2  133 ? 26.424  -64.142  -28.763  1.00 43.80  ? 133 PHE   B N      1 
ATOM   4416  C  CA     . PHE   B 2  133 ? 25.802  -63.596  -27.579  1.00 40.24  ? 133 PHE   B CA     1 
ATOM   4417  C  C      . PHE   B 2  133 ? 24.545  -62.839  -27.964  1.00 42.33  ? 133 PHE   B C      1 
ATOM   4418  O  O      . PHE   B 2  133 ? 24.452  -62.242  -29.047  1.00 34.83  ? 133 PHE   B O      1 
ATOM   4419  C  CB     . PHE   B 2  133 ? 26.772  -62.661  -26.857  1.00 40.59  ? 133 PHE   B CB     1 
ATOM   4420  C  CG     . PHE   B 2  133 ? 28.144  -63.241  -26.661  1.00 41.55  ? 133 PHE   B CG     1 
ATOM   4421  C  CD1    . PHE   B 2  133 ? 28.446  -63.977  -25.529  1.00 46.17  ? 133 PHE   B CD1    1 
ATOM   4422  C  CD2    . PHE   B 2  133 ? 29.125  -63.063  -27.603  1.00 42.33  ? 133 PHE   B CD2    1 
ATOM   4423  C  CE1    . PHE   B 2  133 ? 29.704  -64.519  -25.348  1.00 45.39  ? 133 PHE   B CE1    1 
ATOM   4424  C  CE2    . PHE   B 2  133 ? 30.379  -63.610  -27.418  1.00 45.89  ? 133 PHE   B CE2    1 
ATOM   4425  C  CZ     . PHE   B 2  133 ? 30.664  -64.337  -26.290  1.00 40.69  ? 133 PHE   B CZ     1 
ATOM   4426  N  N      . GLN   B 2  134 ? 23.576  -62.859  -27.059  1.00 41.74  ? 134 GLN   B N      1 
ATOM   4427  C  CA     . GLN   B 2  134 ? 22.414  -62.001  -27.204  1.00 41.39  ? 134 GLN   B CA     1 
ATOM   4428  C  C      . GLN   B 2  134 ? 22.168  -61.288  -25.883  1.00 40.94  ? 134 GLN   B C      1 
ATOM   4429  O  O      . GLN   B 2  134 ? 22.202  -61.904  -24.810  1.00 44.05  ? 134 GLN   B O      1 
ATOM   4430  C  CB     . GLN   B 2  134 ? 21.185  -62.790  -27.674  1.00 36.68  ? 134 GLN   B CB     1 
ATOM   4431  C  CG     . GLN   B 2  134 ? 20.389  -63.430  -26.598  1.00 39.81  ? 134 GLN   B CG     1 
ATOM   4432  C  CD     . GLN   B 2  134 ? 19.134  -64.098  -27.136  1.00 52.18  ? 134 GLN   B CD     1 
ATOM   4433  O  OE1    . GLN   B 2  134 ? 19.042  -64.434  -28.336  1.00 46.64  ? 134 GLN   B OE1    1 
ATOM   4434  N  NE2    . GLN   B 2  134 ? 18.154  -64.311  -26.243  1.00 47.71  ? 134 GLN   B NE2    1 
ATOM   4435  N  N      . LEU   B 2  135 ? 21.960  -59.985  -25.972  1.00 34.02  ? 135 LEU   B N      1 
ATOM   4436  C  CA     . LEU   B 2  135 ? 21.815  -59.133  -24.816  1.00 36.30  ? 135 LEU   B CA     1 
ATOM   4437  C  C      . LEU   B 2  135 ? 20.435  -58.500  -24.844  1.00 39.96  ? 135 LEU   B C      1 
ATOM   4438  O  O      . LEU   B 2  135 ? 19.973  -58.033  -25.897  1.00 37.73  ? 135 LEU   B O      1 
ATOM   4439  C  CB     . LEU   B 2  135 ? 22.896  -58.036  -24.812  1.00 36.37  ? 135 LEU   B CB     1 
ATOM   4440  C  CG     . LEU   B 2  135 ? 22.737  -56.935  -23.763  1.00 39.35  ? 135 LEU   B CG     1 
ATOM   4441  C  CD1    . LEU   B 2  135 ? 23.317  -57.424  -22.443  1.00 43.84  ? 135 LEU   B CD1    1 
ATOM   4442  C  CD2    . LEU   B 2  135 ? 23.408  -55.642  -24.203  1.00 36.68  ? 135 LEU   B CD2    1 
ATOM   4443  N  N      . THR   B 2  136 ? 19.794  -58.479  -23.685  1.00 38.01  ? 136 THR   B N      1 
ATOM   4444  C  CA     . THR   B 2  136 ? 18.558  -57.743  -23.476  1.00 40.74  ? 136 THR   B CA     1 
ATOM   4445  C  C      . THR   B 2  136 ? 18.873  -56.563  -22.567  1.00 38.90  ? 136 THR   B C      1 
ATOM   4446  O  O      . THR   B 2  136 ? 19.431  -56.735  -21.475  1.00 39.27  ? 136 THR   B O      1 
ATOM   4447  C  CB     . THR   B 2  136 ? 17.455  -58.632  -22.875  1.00 37.48  ? 136 THR   B CB     1 
ATOM   4448  O  OG1    . THR   B 2  136 ? 17.833  -59.056  -21.566  1.00 43.45  ? 136 THR   B OG1    1 
ATOM   4449  C  CG2    . THR   B 2  136 ? 17.216  -59.870  -23.737  1.00 36.27  ? 136 THR   B CG2    1 
ATOM   4450  N  N      . HIS   B 2  137 ? 18.533  -55.372  -23.025  1.00 33.46  ? 137 HIS   B N      1 
ATOM   4451  C  CA     . HIS   B 2  137 ? 18.775  -54.174  -22.241  1.00 35.42  ? 137 HIS   B CA     1 
ATOM   4452  C  C      . HIS   B 2  137 ? 17.860  -53.094  -22.781  1.00 34.06  ? 137 HIS   B C      1 
ATOM   4453  O  O      . HIS   B 2  137 ? 17.318  -53.214  -23.880  1.00 38.07  ? 137 HIS   B O      1 
ATOM   4454  C  CB     . HIS   B 2  137 ? 20.251  -53.743  -22.312  1.00 36.17  ? 137 HIS   B CB     1 
ATOM   4455  C  CG     . HIS   B 2  137 ? 20.706  -53.351  -23.685  1.00 33.82  ? 137 HIS   B CG     1 
ATOM   4456  N  ND1    . HIS   B 2  137 ? 21.633  -52.355  -23.908  1.00 34.75  ? 137 HIS   B ND1    1 
ATOM   4457  C  CD2    . HIS   B 2  137 ? 20.355  -53.815  -24.909  1.00 37.13  ? 137 HIS   B CD2    1 
ATOM   4458  C  CE1    . HIS   B 2  137 ? 21.822  -52.213  -25.210  1.00 33.18  ? 137 HIS   B CE1    1 
ATOM   4459  N  NE2    . HIS   B 2  137 ? 21.056  -53.087  -25.840  1.00 34.92  ? 137 HIS   B NE2    1 
ATOM   4460  N  N      . SER   B 2  138 ? 17.694  -52.040  -22.004  1.00 34.39  ? 138 SER   B N      1 
ATOM   4461  C  CA     . SER   B 2  138 ? 17.152  -50.799  -22.535  1.00 32.76  ? 138 SER   B CA     1 
ATOM   4462  C  C      . SER   B 2  138 ? 18.289  -49.821  -22.727  1.00 33.07  ? 138 SER   B C      1 
ATOM   4463  O  O      . SER   B 2  138 ? 19.354  -49.958  -22.124  1.00 34.60  ? 138 SER   B O      1 
ATOM   4464  C  CB     . SER   B 2  138 ? 16.111  -50.190  -21.608  1.00 35.40  ? 138 SER   B CB     1 
ATOM   4465  O  OG     . SER   B 2  138 ? 16.670  -50.009  -20.336  1.00 38.93  ? 138 SER   B OG     1 
ATOM   4466  N  N      . LEU   B 2  139 ? 18.057  -48.840  -23.587  1.00 31.94  ? 139 LEU   B N      1 
ATOM   4467  C  CA     . LEU   B 2  139 ? 19.032  -47.805  -23.877  1.00 28.46  ? 139 LEU   B CA     1 
ATOM   4468  C  C      . LEU   B 2  139 ? 18.783  -46.526  -23.085  1.00 35.09  ? 139 LEU   B C      1 
ATOM   4469  O  O      . LEU   B 2  139 ? 19.509  -45.546  -23.271  1.00 36.28  ? 139 LEU   B O      1 
ATOM   4470  C  CB     . LEU   B 2  139 ? 19.018  -47.493  -25.368  1.00 26.34  ? 139 LEU   B CB     1 
ATOM   4471  C  CG     . LEU   B 2  139 ? 19.148  -48.759  -26.207  1.00 34.48  ? 139 LEU   B CG     1 
ATOM   4472  C  CD1    . LEU   B 2  139 ? 19.153  -48.451  -27.723  1.00 37.32  ? 139 LEU   B CD1    1 
ATOM   4473  C  CD2    . LEU   B 2  139 ? 20.363  -49.567  -25.786  1.00 28.55  ? 139 LEU   B CD2    1 
ATOM   4474  N  N      . GLY   B 2  140 ? 17.775  -46.502  -22.214  1.00 33.69  ? 140 GLY   B N      1 
ATOM   4475  C  CA     . GLY   B 2  140 ? 17.341  -45.243  -21.639  1.00 31.82  ? 140 GLY   B CA     1 
ATOM   4476  C  C      . GLY   B 2  140 ? 17.713  -45.010  -20.197  1.00 29.14  ? 140 GLY   B C      1 
ATOM   4477  O  O      . GLY   B 2  140 ? 17.732  -43.861  -19.767  1.00 31.94  ? 140 GLY   B O      1 
ATOM   4478  N  N      . GLY   B 2  141 ? 17.989  -46.077  -19.444  1.00 35.19  ? 141 GLY   B N      1 
ATOM   4479  C  CA     . GLY   B 2  141 ? 18.534  -45.993  -18.097  1.00 29.16  ? 141 GLY   B CA     1 
ATOM   4480  C  C      . GLY   B 2  141 ? 20.045  -45.962  -18.124  1.00 31.75  ? 141 GLY   B C      1 
ATOM   4481  O  O      . GLY   B 2  141 ? 20.660  -45.457  -19.070  1.00 33.04  ? 141 GLY   B O      1 
ATOM   4482  N  N      . GLY   B 2  142 ? 20.657  -46.520  -17.079  1.00 28.57  ? 142 GLY   B N      1 
ATOM   4483  C  CA     . GLY   B 2  142 ? 22.098  -46.496  -16.946  1.00 28.42  ? 142 GLY   B CA     1 
ATOM   4484  C  C      . GLY   B 2  142 ? 22.801  -47.844  -16.957  1.00 32.67  ? 142 GLY   B C      1 
ATOM   4485  O  O      . GLY   B 2  142 ? 23.829  -48.015  -17.623  1.00 33.79  ? 142 GLY   B O      1 
ATOM   4486  N  N      . THR   B 2  143 ? 22.297  -48.803  -16.194  1.00 26.14  ? 143 THR   B N      1 
ATOM   4487  C  CA     . THR   B 2  143 ? 22.922  -50.109  -16.227  1.00 25.01  ? 143 THR   B CA     1 
ATOM   4488  C  C      . THR   B 2  143 ? 22.836  -50.690  -17.628  1.00 34.77  ? 143 THR   B C      1 
ATOM   4489  O  O      . THR   B 2  143 ? 23.843  -50.702  -18.341  1.00 44.00  ? 143 THR   B O      1 
ATOM   4490  C  CB     . THR   B 2  143 ? 22.297  -51.027  -15.192  1.00 28.83  ? 143 THR   B CB     1 
ATOM   4491  O  OG1    . THR   B 2  143 ? 22.471  -50.434  -13.903  1.00 31.36  ? 143 THR   B OG1    1 
ATOM   4492  C  CG2    . THR   B 2  143 ? 22.944  -52.365  -15.187  1.00 37.85  ? 143 THR   B CG2    1 
ATOM   4493  N  N      . GLY   B 2  144 ? 21.660  -51.143  -18.059  1.00 34.06  ? 144 GLY   B N      1 
ATOM   4494  C  CA     . GLY   B 2  144 ? 21.554  -51.779  -19.371  1.00 31.42  ? 144 GLY   B CA     1 
ATOM   4495  C  C      . GLY   B 2  144 ? 22.118  -50.931  -20.487  1.00 30.99  ? 144 GLY   B C      1 
ATOM   4496  O  O      . GLY   B 2  144 ? 22.728  -51.442  -21.429  1.00 33.98  ? 144 GLY   B O      1 
ATOM   4497  N  N      . SER   B 2  145 ? 21.959  -49.621  -20.381  1.00 32.77  ? 145 SER   B N      1 
ATOM   4498  C  CA     . SER   B 2  145 ? 22.437  -48.734  -21.427  1.00 29.10  ? 145 SER   B CA     1 
ATOM   4499  C  C      . SER   B 2  145 ? 23.949  -48.581  -21.378  1.00 39.56  ? 145 SER   B C      1 
ATOM   4500  O  O      . SER   B 2  145 ? 24.657  -48.976  -22.308  1.00 38.63  ? 145 SER   B O      1 
ATOM   4501  C  CB     . SER   B 2  145 ? 21.779  -47.384  -21.276  1.00 33.31  ? 145 SER   B CB     1 
ATOM   4502  O  OG     . SER   B 2  145 ? 21.632  -46.824  -22.561  1.00 46.27  ? 145 SER   B OG     1 
ATOM   4503  N  N      . GLY   B 2  146 ? 24.463  -47.983  -20.303  1.00 41.47  ? 146 GLY   B N      1 
ATOM   4504  C  CA     . GLY   B 2  146 ? 25.882  -47.713  -20.206  1.00 36.10  ? 146 GLY   B CA     1 
ATOM   4505  C  C      . GLY   B 2  146 ? 26.741  -48.928  -19.935  1.00 35.45  ? 146 GLY   B C      1 
ATOM   4506  O  O      . GLY   B 2  146 ? 27.740  -49.149  -20.621  1.00 38.09  ? 146 GLY   B O      1 
ATOM   4507  N  N      . MET   B 2  147 ? 26.400  -49.713  -18.921  1.00 35.49  ? 147 MET   B N      1 
ATOM   4508  C  CA     . MET   B 2  147 ? 27.199  -50.907  -18.656  1.00 37.41  ? 147 MET   B CA     1 
ATOM   4509  C  C      . MET   B 2  147 ? 27.008  -51.930  -19.765  1.00 39.35  ? 147 MET   B C      1 
ATOM   4510  O  O      . MET   B 2  147 ? 27.984  -52.471  -20.304  1.00 37.48  ? 147 MET   B O      1 
ATOM   4511  C  CB     . MET   B 2  147 ? 26.843  -51.527  -17.306  1.00 34.58  ? 147 MET   B CB     1 
ATOM   4512  C  CG     . MET   B 2  147 ? 27.940  -52.430  -16.791  1.00 35.90  ? 147 MET   B CG     1 
ATOM   4513  S  SD     . MET   B 2  147 ? 27.415  -53.402  -15.387  1.00 39.17  ? 147 MET   B SD     1 
ATOM   4514  C  CE     . MET   B 2  147 ? 28.457  -54.847  -15.533  1.00 42.26  ? 147 MET   B CE     1 
ATOM   4515  N  N      . GLY   B 2  148 ? 25.750  -52.203  -20.112  1.00 35.01  ? 148 GLY   B N      1 
ATOM   4516  C  CA     . GLY   B 2  148 ? 25.425  -53.022  -21.256  1.00 37.77  ? 148 GLY   B CA     1 
ATOM   4517  C  C      . GLY   B 2  148 ? 26.340  -52.823  -22.450  1.00 40.09  ? 148 GLY   B C      1 
ATOM   4518  O  O      . GLY   B 2  148 ? 26.904  -53.799  -22.946  1.00 38.84  ? 148 GLY   B O      1 
ATOM   4519  N  N      . THR   B 2  149 ? 26.499  -51.586  -22.933  1.00 34.58  ? 149 THR   B N      1 
ATOM   4520  C  CA     . THR   B 2  149 ? 27.384  -51.387  -24.071  1.00 40.29  ? 149 THR   B CA     1 
ATOM   4521  C  C      . THR   B 2  149 ? 28.851  -51.561  -23.678  1.00 40.44  ? 149 THR   B C      1 
ATOM   4522  O  O      . THR   B 2  149 ? 29.673  -51.930  -24.522  1.00 45.44  ? 149 THR   B O      1 
ATOM   4523  C  CB     . THR   B 2  149 ? 27.180  -50.010  -24.697  1.00 37.19  ? 149 THR   B CB     1 
ATOM   4524  O  OG1    . THR   B 2  149 ? 27.163  -49.029  -23.666  1.00 37.12  ? 149 THR   B OG1    1 
ATOM   4525  C  CG2    . THR   B 2  149 ? 25.869  -49.961  -25.487  1.00 33.38  ? 149 THR   B CG2    1 
ATOM   4526  N  N      . LEU   B 2  150 ? 29.206  -51.308  -22.420  1.00 36.81  ? 150 LEU   B N      1 
ATOM   4527  C  CA     . LEU   B 2  150 ? 30.573  -51.574  -21.999  1.00 37.26  ? 150 LEU   B CA     1 
ATOM   4528  C  C      . LEU   B 2  150 ? 30.873  -53.068  -22.057  1.00 39.27  ? 150 LEU   B C      1 
ATOM   4529  O  O      . LEU   B 2  150 ? 31.916  -53.486  -22.571  1.00 38.89  ? 150 LEU   B O      1 
ATOM   4530  C  CB     . LEU   B 2  150 ? 30.796  -51.016  -20.601  1.00 35.44  ? 150 LEU   B CB     1 
ATOM   4531  C  CG     . LEU   B 2  150 ? 32.151  -51.359  -20.034  1.00 34.75  ? 150 LEU   B CG     1 
ATOM   4532  C  CD1    . LEU   B 2  150 ? 33.181  -50.465  -20.698  1.00 31.73  ? 150 LEU   B CD1    1 
ATOM   4533  C  CD2    . LEU   B 2  150 ? 32.106  -51.189  -18.525  1.00 34.77  ? 150 LEU   B CD2    1 
ATOM   4534  N  N      . LEU   B 2  151 ? 29.957  -53.893  -21.569  1.00 35.63  ? 151 LEU   B N      1 
ATOM   4535  C  CA     . LEU   B 2  151 ? 30.096  -55.332  -21.749  1.00 36.56  ? 151 LEU   B CA     1 
ATOM   4536  C  C      . LEU   B 2  151 ? 30.269  -55.693  -23.217  1.00 38.09  ? 151 LEU   B C      1 
ATOM   4537  O  O      . LEU   B 2  151 ? 31.187  -56.428  -23.581  1.00 39.81  ? 151 LEU   B O      1 
ATOM   4538  C  CB     . LEU   B 2  151 ? 28.874  -56.034  -21.188  1.00 35.44  ? 151 LEU   B CB     1 
ATOM   4539  C  CG     . LEU   B 2  151 ? 28.979  -56.554  -19.784  1.00 36.70  ? 151 LEU   B CG     1 
ATOM   4540  C  CD1    . LEU   B 2  151 ? 27.563  -56.795  -19.263  1.00 47.49  ? 151 LEU   B CD1    1 
ATOM   4541  C  CD2    . LEU   B 2  151 ? 29.762  -57.822  -19.864  1.00 46.25  ? 151 LEU   B CD2    1 
ATOM   4542  N  N      . ILE   B 2  152 ? 29.368  -55.202  -24.072  1.00 39.57  ? 152 ILE   B N      1 
ATOM   4543  C  CA     . ILE   B 2  152 ? 29.428  -55.516  -25.492  1.00 37.35  ? 152 ILE   B CA     1 
ATOM   4544  C  C      . ILE   B 2  152 ? 30.802  -55.164  -26.042  1.00 42.53  ? 152 ILE   B C      1 
ATOM   4545  O  O      . ILE   B 2  152 ? 31.371  -55.910  -26.847  1.00 44.69  ? 152 ILE   B O      1 
ATOM   4546  C  CB     . ILE   B 2  152 ? 28.280  -54.800  -26.241  1.00 39.30  ? 152 ILE   B CB     1 
ATOM   4547  C  CG1    . ILE   B 2  152 ? 26.950  -55.466  -25.903  1.00 33.82  ? 152 ILE   B CG1    1 
ATOM   4548  C  CG2    . ILE   B 2  152 ? 28.457  -54.846  -27.776  1.00 36.73  ? 152 ILE   B CG2    1 
ATOM   4549  C  CD1    . ILE   B 2  152 ? 25.767  -54.637  -26.283  1.00 40.12  ? 152 ILE   B CD1    1 
ATOM   4550  N  N      . SER   B 2  153 ? 31.379  -54.042  -25.596  1.00 40.01  ? 153 SER   B N      1 
ATOM   4551  C  CA     . SER   B 2  153 ? 32.725  -53.700  -26.042  1.00 40.54  ? 153 SER   B CA     1 
ATOM   4552  C  C      . SER   B 2  153 ? 33.737  -54.734  -25.580  1.00 45.52  ? 153 SER   B C      1 
ATOM   4553  O  O      . SER   B 2  153 ? 34.633  -55.122  -26.338  1.00 45.84  ? 153 SER   B O      1 
ATOM   4554  C  CB     . SER   B 2  153 ? 33.138  -52.323  -25.538  1.00 41.42  ? 153 SER   B CB     1 
ATOM   4555  O  OG     . SER   B 2  153 ? 33.919  -51.676  -26.528  1.00 49.88  ? 153 SER   B OG     1 
ATOM   4556  N  N      . LYS   B 2  154 ? 33.606  -55.199  -24.343  1.00 45.39  ? 154 LYS   B N      1 
ATOM   4557  C  CA     . LYS   B 2  154 ? 34.606  -56.100  -23.795  1.00 42.29  ? 154 LYS   B CA     1 
ATOM   4558  C  C      . LYS   B 2  154 ? 34.452  -57.508  -24.357  1.00 46.50  ? 154 LYS   B C      1 
ATOM   4559  O  O      . LYS   B 2  154 ? 35.458  -58.147  -24.694  1.00 48.13  ? 154 LYS   B O      1 
ATOM   4560  C  CB     . LYS   B 2  154 ? 34.529  -56.067  -22.267  1.00 40.04  ? 154 LYS   B CB     1 
ATOM   4561  C  CG     . LYS   B 2  154 ? 34.947  -54.679  -21.749  1.00 43.22  ? 154 LYS   B CG     1 
ATOM   4562  C  CD     . LYS   B 2  154 ? 35.226  -54.609  -20.245  1.00 51.75  ? 154 LYS   B CD     1 
ATOM   4563  C  CE     . LYS   B 2  154 ? 36.460  -53.767  -19.985  1.00 46.84  ? 154 LYS   B CE     1 
ATOM   4564  N  NZ     . LYS   B 2  154 ? 36.584  -52.743  -21.055  1.00 50.44  ? 154 LYS   B NZ     1 
ATOM   4565  N  N      . ILE   B 2  155 ? 33.207  -57.996  -24.479  1.00 46.11  ? 155 ILE   B N      1 
ATOM   4566  C  CA     . ILE   B 2  155 ? 32.949  -59.295  -25.109  1.00 42.59  ? 155 ILE   B CA     1 
ATOM   4567  C  C      . ILE   B 2  155 ? 33.574  -59.344  -26.500  1.00 45.93  ? 155 ILE   B C      1 
ATOM   4568  O  O      . ILE   B 2  155 ? 34.255  -60.309  -26.866  1.00 46.06  ? 155 ILE   B O      1 
ATOM   4569  C  CB     . ILE   B 2  155 ? 31.440  -59.565  -25.185  1.00 39.80  ? 155 ILE   B CB     1 
ATOM   4570  C  CG1    . ILE   B 2  155 ? 30.797  -59.517  -23.800  1.00 39.91  ? 155 ILE   B CG1    1 
ATOM   4571  C  CG2    . ILE   B 2  155 ? 31.183  -60.862  -25.935  1.00 42.62  ? 155 ILE   B CG2    1 
ATOM   4572  C  CD1    . ILE   B 2  155 ? 30.708  -60.850  -23.109  1.00 50.52  ? 155 ILE   B CD1    1 
ATOM   4573  N  N      . ARG   B 2  156 ? 33.348  -58.299  -27.296  1.00 41.24  ? 156 ARG   B N      1 
ATOM   4574  C  CA     . ARG   B 2  156 ? 33.912  -58.266  -28.632  1.00 42.83  ? 156 ARG   B CA     1 
ATOM   4575  C  C      . ARG   B 2  156 ? 35.433  -58.286  -28.625  1.00 47.99  ? 156 ARG   B C      1 
ATOM   4576  O  O      . ARG   B 2  156 ? 36.038  -58.662  -29.637  1.00 53.37  ? 156 ARG   B O      1 
ATOM   4577  C  CB     . ARG   B 2  156 ? 33.438  -57.035  -29.388  1.00 38.69  ? 156 ARG   B CB     1 
ATOM   4578  C  CG     . ARG   B 2  156 ? 34.078  -56.911  -30.752  1.00 35.86  ? 156 ARG   B CG     1 
ATOM   4579  C  CD     . ARG   B 2  156 ? 33.540  -55.718  -31.496  1.00 41.04  ? 156 ARG   B CD     1 
ATOM   4580  N  NE     . ARG   B 2  156 ? 33.893  -55.752  -32.909  1.00 41.89  ? 156 ARG   B NE     1 
ATOM   4581  C  CZ     . ARG   B 2  156 ? 33.686  -54.745  -33.742  1.00 42.83  ? 156 ARG   B CZ     1 
ATOM   4582  N  NH1    . ARG   B 2  156 ? 33.178  -53.602  -33.321  1.00 48.16  ? 156 ARG   B NH1    1 
ATOM   4583  N  NH2    . ARG   B 2  156 ? 33.963  -54.900  -35.032  1.00 43.15  ? 156 ARG   B NH2    1 
ATOM   4584  N  N      . GLU   B 2  157 ? 36.075  -57.842  -27.543  1.00 49.62  ? 157 GLU   B N      1 
ATOM   4585  C  CA     . GLU   B 2  157 ? 37.533  -57.921  -27.480  1.00 47.27  ? 157 GLU   B CA     1 
ATOM   4586  C  C      . GLU   B 2  157 ? 37.985  -59.341  -27.161  1.00 47.30  ? 157 GLU   B C      1 
ATOM   4587  O  O      . GLU   B 2  157 ? 38.928  -59.857  -27.772  1.00 45.41  ? 157 GLU   B O      1 
ATOM   4588  C  CB     . GLU   B 2  157 ? 38.062  -56.947  -26.439  1.00 46.77  ? 157 GLU   B CB     1 
ATOM   4589  C  CG     . GLU   B 2  157 ? 39.531  -56.608  -26.558  1.00 55.15  ? 157 GLU   B CG     1 
ATOM   4590  C  CD     . GLU   B 2  157 ? 39.982  -55.574  -25.514  1.00 61.26  ? 157 GLU   B CD     1 
ATOM   4591  O  OE1    . GLU   B 2  157 ? 39.293  -55.445  -24.467  1.00 53.95  ? 157 GLU   B OE1    1 
ATOM   4592  O  OE2    . GLU   B 2  157 ? 41.010  -54.880  -25.755  1.00 64.36  ? 157 GLU   B OE2    1 
ATOM   4593  N  N      . GLU   B 2  158 ? 37.301  -59.991  -26.225  1.00 42.81  ? 158 GLU   B N      1 
ATOM   4594  C  CA     . GLU   B 2  158 ? 37.612  -61.371  -25.889  1.00 42.61  ? 158 GLU   B CA     1 
ATOM   4595  C  C      . GLU   B 2  158 ? 37.178  -62.346  -26.986  1.00 48.99  ? 158 GLU   B C      1 
ATOM   4596  O  O      . GLU   B 2  158 ? 37.865  -63.343  -27.231  1.00 49.72  ? 158 GLU   B O      1 
ATOM   4597  C  CB     . GLU   B 2  158 ? 36.939  -61.726  -24.569  1.00 47.58  ? 158 GLU   B CB     1 
ATOM   4598  C  CG     . GLU   B 2  158 ? 37.615  -62.822  -23.793  1.00 47.95  ? 158 GLU   B CG     1 
ATOM   4599  C  CD     . GLU   B 2  158 ? 37.119  -62.887  -22.381  1.00 67.30  ? 158 GLU   B CD     1 
ATOM   4600  O  OE1    . GLU   B 2  158 ? 37.172  -63.998  -21.787  1.00 69.48  ? 158 GLU   B OE1    1 
ATOM   4601  O  OE2    . GLU   B 2  158 ? 36.667  -61.822  -21.872  1.00 67.55  ? 158 GLU   B OE2    1 
ATOM   4602  N  N      . TYR   B 2  159 ? 36.028  -62.108  -27.625  1.00 48.10  ? 159 TYR   B N      1 
ATOM   4603  C  CA     . TYR   B 2  159 ? 35.467  -63.017  -28.628  1.00 48.54  ? 159 TYR   B CA     1 
ATOM   4604  C  C      . TYR   B 2  159 ? 35.227  -62.271  -29.934  1.00 43.38  ? 159 TYR   B C      1 
ATOM   4605  O  O      . TYR   B 2  159 ? 34.108  -62.246  -30.449  1.00 49.30  ? 159 TYR   B O      1 
ATOM   4606  C  CB     . TYR   B 2  159 ? 34.173  -63.662  -28.136  1.00 39.84  ? 159 TYR   B CB     1 
ATOM   4607  C  CG     . TYR   B 2  159 ? 34.248  -64.186  -26.721  1.00 48.68  ? 159 TYR   B CG     1 
ATOM   4608  C  CD1    . TYR   B 2  159 ? 34.112  -63.327  -25.626  1.00 52.80  ? 159 TYR   B CD1    1 
ATOM   4609  C  CD2    . TYR   B 2  159 ? 34.452  -65.536  -26.464  1.00 45.38  ? 159 TYR   B CD2    1 
ATOM   4610  C  CE1    . TYR   B 2  159 ? 34.174  -63.804  -24.318  1.00 46.23  ? 159 TYR   B CE1    1 
ATOM   4611  C  CE2    . TYR   B 2  159 ? 34.513  -66.015  -25.161  1.00 45.67  ? 159 TYR   B CE2    1 
ATOM   4612  C  CZ     . TYR   B 2  159 ? 34.376  -65.143  -24.097  1.00 49.28  ? 159 TYR   B CZ     1 
ATOM   4613  O  OH     . TYR   B 2  159 ? 34.434  -65.613  -22.803  1.00 62.98  ? 159 TYR   B OH     1 
ATOM   4614  N  N      . PRO   B 2  160 ? 36.274  -61.706  -30.525  1.00 44.90  ? 160 PRO   B N      1 
ATOM   4615  C  CA     . PRO   B 2  160 ? 36.083  -60.766  -31.648  1.00 43.85  ? 160 PRO   B CA     1 
ATOM   4616  C  C      . PRO   B 2  160 ? 35.345  -61.335  -32.835  1.00 42.37  ? 160 PRO   B C      1 
ATOM   4617  O  O      . PRO   B 2  160 ? 34.924  -60.558  -33.711  1.00 39.82  ? 160 PRO   B O      1 
ATOM   4618  C  CB     . PRO   B 2  160 ? 37.516  -60.409  -32.034  1.00 41.91  ? 160 PRO   B CB     1 
ATOM   4619  C  CG     . PRO   B 2  160 ? 38.280  -61.634  -31.648  1.00 43.57  ? 160 PRO   B CG     1 
ATOM   4620  C  CD     . PRO   B 2  160 ? 37.685  -62.063  -30.337  1.00 40.04  ? 160 PRO   B CD     1 
ATOM   4621  N  N      . ASP   B 2  161 ? 35.213  -62.656  -32.909  1.00 42.93  ? 161 ASP   B N      1 
ATOM   4622  C  CA     . ASP   B 2  161 ? 34.736  -63.344  -34.097  1.00 45.52  ? 161 ASP   B CA     1 
ATOM   4623  C  C      . ASP   B 2  161 ? 33.473  -64.159  -33.849  1.00 47.10  ? 161 ASP   B C      1 
ATOM   4624  O  O      . ASP   B 2  161 ? 33.083  -64.943  -34.714  1.00 50.35  ? 161 ASP   B O      1 
ATOM   4625  C  CB     . ASP   B 2  161 ? 35.844  -64.238  -34.653  1.00 46.61  ? 161 ASP   B CB     1 
ATOM   4626  C  CG     . ASP   B 2  161 ? 36.098  -65.440  -33.794  1.00 53.20  ? 161 ASP   B CG     1 
ATOM   4627  O  OD1    . ASP   B 2  161 ? 35.698  -65.435  -32.609  1.00 55.71  ? 161 ASP   B OD1    1 
ATOM   4628  O  OD2    . ASP   B 2  161 ? 36.712  -66.399  -34.302  1.00 69.13  ? 161 ASP   B OD2    1 
ATOM   4629  N  N      . ARG   B 2  162 ? 32.831  -63.993  -32.696  1.00 50.75  ? 162 ARG   B N      1 
ATOM   4630  C  CA     . ARG   B 2  162 ? 31.489  -64.486  -32.422  1.00 46.75  ? 162 ARG   B CA     1 
ATOM   4631  C  C      . ARG   B 2  162 ? 30.449  -63.410  -32.757  1.00 44.20  ? 162 ARG   B C      1 
ATOM   4632  O  O      . ARG   B 2  162 ? 30.758  -62.225  -32.903  1.00 41.90  ? 162 ARG   B O      1 
ATOM   4633  C  CB     . ARG   B 2  162 ? 31.366  -64.901  -30.958  1.00 44.24  ? 162 ARG   B CB     1 
ATOM   4634  C  CG     . ARG   B 2  162 ? 32.410  -65.908  -30.508  1.00 47.21  ? 162 ARG   B CG     1 
ATOM   4635  C  CD     . ARG   B 2  162 ? 32.331  -67.176  -31.303  1.00 53.44  ? 162 ARG   B CD     1 
ATOM   4636  N  NE     . ARG   B 2  162 ? 33.223  -68.216  -30.801  1.00 63.29  ? 162 ARG   B NE     1 
ATOM   4637  C  CZ     . ARG   B 2  162 ? 34.132  -68.838  -31.548  1.00 71.04  ? 162 ARG   B CZ     1 
ATOM   4638  N  NH1    . ARG   B 2  162 ? 34.282  -68.554  -32.838  1.00 66.55  ? 162 ARG   B NH1    1 
ATOM   4639  N  NH2    . ARG   B 2  162 ? 34.906  -69.767  -30.991  1.00 64.49  ? 162 ARG   B NH2    1 
ATOM   4640  N  N      . ILE   B 2  163 ? 29.212  -63.827  -32.866  1.00 42.13  ? 163 ILE   B N      1 
ATOM   4641  C  CA     . ILE   B 2  163 ? 28.151  -62.907  -33.251  1.00 44.04  ? 163 ILE   B CA     1 
ATOM   4642  C  C      . ILE   B 2  163 ? 27.630  -62.188  -32.014  1.00 41.82  ? 163 ILE   B C      1 
ATOM   4643  O  O      . ILE   B 2  163 ? 27.450  -62.802  -30.948  1.00 39.16  ? 163 ILE   B O      1 
ATOM   4644  C  CB     . ILE   B 2  163 ? 27.020  -63.654  -33.988  1.00 41.96  ? 163 ILE   B CB     1 
ATOM   4645  C  CG1    . ILE   B 2  163 ? 27.531  -64.120  -35.359  1.00 40.28  ? 163 ILE   B CG1    1 
ATOM   4646  C  CG2    . ILE   B 2  163 ? 25.767  -62.772  -34.074  1.00 31.72  ? 163 ILE   B CG2    1 
ATOM   4647  C  CD1    . ILE   B 2  163 ? 28.047  -62.980  -36.260  1.00 37.78  ? 163 ILE   B CD1    1 
ATOM   4648  N  N      . MET   B 2  164 ? 27.378  -60.884  -32.162  1.00 35.18  ? 164 MET   B N      1 
ATOM   4649  C  CA     . MET   B 2  164 ? 26.798  -60.047  -31.115  1.00 33.82  ? 164 MET   B CA     1 
ATOM   4650  C  C      . MET   B 2  164 ? 25.409  -59.582  -31.553  1.00 35.17  ? 164 MET   B C      1 
ATOM   4651  O  O      . MET   B 2  164 ? 25.269  -58.826  -32.519  1.00 30.74  ? 164 MET   B O      1 
ATOM   4652  C  CB     . MET   B 2  164 ? 27.715  -58.862  -30.792  1.00 34.74  ? 164 MET   B CB     1 
ATOM   4653  C  CG     . MET   B 2  164 ? 27.299  -57.926  -29.645  1.00 37.46  ? 164 MET   B CG     1 
ATOM   4654  S  SD     . MET   B 2  164 ? 26.714  -58.756  -28.124  1.00 45.37  ? 164 MET   B SD     1 
ATOM   4655  C  CE     . MET   B 2  164 ? 28.302  -58.960  -27.310  1.00 43.63  ? 164 MET   B CE     1 
ATOM   4656  N  N      . ASN   B 2  165 ? 24.398  -60.026  -30.807  1.00 40.81  ? 165 ASN   B N      1 
ATOM   4657  C  CA     . ASN   B 2  165 ? 22.982  -59.759  -31.024  1.00 39.14  ? 165 ASN   B CA     1 
ATOM   4658  C  C      . ASN   B 2  165 ? 22.408  -59.076  -29.778  1.00 42.31  ? 165 ASN   B C      1 
ATOM   4659  O  O      . ASN   B 2  165 ? 22.627  -59.549  -28.648  1.00 36.50  ? 165 ASN   B O      1 
ATOM   4660  C  CB     . ASN   B 2  165 ? 22.258  -61.093  -31.295  1.00 38.70  ? 165 ASN   B CB     1 
ATOM   4661  C  CG     . ASN   B 2  165 ? 20.762  -60.934  -31.504  1.00 39.90  ? 165 ASN   B CG     1 
ATOM   4662  O  OD1    . ASN   B 2  165 ? 20.318  -60.381  -32.513  1.00 42.09  ? 165 ASN   B OD1    1 
ATOM   4663  N  ND2    . ASN   B 2  165 ? 19.980  -61.419  -30.556  1.00 36.76  ? 165 ASN   B ND2    1 
ATOM   4664  N  N      . THR   B 2  166 ? 21.673  -57.972  -29.966  1.00 34.11  ? 166 THR   B N      1 
ATOM   4665  C  CA     . THR   B 2  166 ? 20.985  -57.376  -28.829  1.00 37.91  ? 166 THR   B CA     1 
ATOM   4666  C  C      . THR   B 2  166 ? 19.493  -57.252  -29.100  1.00 37.59  ? 166 THR   B C      1 
ATOM   4667  O  O      . THR   B 2  166 ? 19.046  -57.183  -30.240  1.00 36.57  ? 166 THR   B O      1 
ATOM   4668  C  CB     . THR   B 2  166 ? 21.538  -55.990  -28.458  1.00 36.85  ? 166 THR   B CB     1 
ATOM   4669  O  OG1    . THR   B 2  166 ? 21.195  -55.056  -29.479  1.00 32.28  ? 166 THR   B OG1    1 
ATOM   4670  C  CG2    . THR   B 2  166 ? 23.068  -56.027  -28.274  1.00 35.77  ? 166 THR   B CG2    1 
ATOM   4671  N  N      . PHE   B 2  167 ? 18.732  -57.245  -28.018  1.00 39.76  ? 167 PHE   B N      1 
ATOM   4672  C  CA     . PHE   B 2  167 ? 17.354  -56.769  -27.990  1.00 35.64  ? 167 PHE   B CA     1 
ATOM   4673  C  C      . PHE   B 2  167 ? 17.373  -55.437  -27.245  1.00 32.02  ? 167 PHE   B C      1 
ATOM   4674  O  O      . PHE   B 2  167 ? 17.424  -55.412  -26.011  1.00 33.16  ? 167 PHE   B O      1 
ATOM   4675  C  CB     . PHE   B 2  167 ? 16.462  -57.796  -27.308  1.00 34.84  ? 167 PHE   B CB     1 
ATOM   4676  C  CG     . PHE   B 2  167 ? 16.347  -59.061  -28.067  1.00 40.36  ? 167 PHE   B CG     1 
ATOM   4677  C  CD1    . PHE   B 2  167 ? 17.405  -59.951  -28.097  1.00 40.35  ? 167 PHE   B CD1    1 
ATOM   4678  C  CD2    . PHE   B 2  167 ? 15.187  -59.358  -28.783  1.00 41.79  ? 167 PHE   B CD2    1 
ATOM   4679  C  CE1    . PHE   B 2  167 ? 17.307  -61.121  -28.825  1.00 46.22  ? 167 PHE   B CE1    1 
ATOM   4680  C  CE2    . PHE   B 2  167 ? 15.072  -60.522  -29.511  1.00 35.76  ? 167 PHE   B CE2    1 
ATOM   4681  C  CZ     . PHE   B 2  167 ? 16.131  -61.405  -29.538  1.00 43.37  ? 167 PHE   B CZ     1 
ATOM   4682  N  N      . SER   B 2  168 ? 17.352  -54.334  -27.984  1.00 27.66  ? 168 SER   B N      1 
ATOM   4683  C  CA     . SER   B 2  168 ? 17.512  -52.998  -27.410  1.00 33.47  ? 168 SER   B CA     1 
ATOM   4684  C  C      . SER   B 2  168 ? 16.168  -52.268  -27.345  1.00 32.72  ? 168 SER   B C      1 
ATOM   4685  O  O      . SER   B 2  168 ? 15.633  -51.853  -28.377  1.00 36.65  ? 168 SER   B O      1 
ATOM   4686  C  CB     . SER   B 2  168 ? 18.526  -52.177  -28.223  1.00 35.18  ? 168 SER   B CB     1 
ATOM   4687  O  OG     . SER   B 2  168 ? 19.827  -52.770  -28.201  1.00 32.17  ? 168 SER   B OG     1 
ATOM   4688  N  N      . VAL   B 2  169 ? 15.661  -52.047  -26.135  1.00 29.21  ? 169 VAL   B N      1 
ATOM   4689  C  CA     . VAL   B 2  169 ? 14.441  -51.262  -25.926  1.00 31.93  ? 169 VAL   B CA     1 
ATOM   4690  C  C      . VAL   B 2  169 ? 14.724  -49.772  -26.082  1.00 30.38  ? 169 VAL   B C      1 
ATOM   4691  O  O      . VAL   B 2  169 ? 15.472  -49.197  -25.292  1.00 33.43  ? 169 VAL   B O      1 
ATOM   4692  C  CB     . VAL   B 2  169 ? 13.841  -51.550  -24.543  1.00 33.58  ? 169 VAL   B CB     1 
ATOM   4693  C  CG1    . VAL   B 2  169 ? 12.652  -50.621  -24.280  1.00 28.86  ? 169 VAL   B CG1    1 
ATOM   4694  C  CG2    . VAL   B 2  169 ? 13.469  -53.036  -24.455  1.00 34.11  ? 169 VAL   B CG2    1 
ATOM   4695  N  N      . MET   B 2  170 ? 14.075  -49.126  -27.086  1.00 34.69  ? 170 MET   B N      1 
ATOM   4696  C  CA     . MET   B 2  170 ? 14.139  -47.678  -27.340  1.00 38.07  ? 170 MET   B CA     1 
ATOM   4697  C  C      . MET   B 2  170 ? 13.311  -46.903  -26.310  1.00 40.09  ? 170 MET   B C      1 
ATOM   4698  O  O      . MET   B 2  170 ? 12.189  -47.300  -25.989  1.00 37.21  ? 170 MET   B O      1 
ATOM   4699  C  CB     . MET   B 2  170 ? 13.581  -47.305  -28.717  1.00 42.74  ? 170 MET   B CB     1 
ATOM   4700  C  CG     . MET   B 2  170 ? 14.313  -47.762  -29.922  1.00 45.37  ? 170 MET   B CG     1 
ATOM   4701  S  SD     . MET   B 2  170 ? 16.034  -47.995  -29.597  1.00 57.75  ? 170 MET   B SD     1 
ATOM   4702  C  CE     . MET   B 2  170 ? 16.617  -47.801  -31.280  1.00 50.39  ? 170 MET   B CE     1 
ATOM   4703  N  N      . PRO   B 2  171 ? 13.794  -45.758  -25.840  1.00 42.03  ? 171 PRO   B N      1 
ATOM   4704  C  CA     . PRO   B 2  171 ? 13.013  -44.954  -24.896  1.00 38.40  ? 171 PRO   B CA     1 
ATOM   4705  C  C      . PRO   B 2  171 ? 11.919  -44.170  -25.615  1.00 39.31  ? 171 PRO   B C      1 
ATOM   4706  O  O      . PRO   B 2  171 ? 11.947  -43.994  -26.827  1.00 38.28  ? 171 PRO   B O      1 
ATOM   4707  C  CB     . PRO   B 2  171 ? 14.067  -44.027  -24.281  1.00 34.76  ? 171 PRO   B CB     1 
ATOM   4708  C  CG     . PRO   B 2  171 ? 15.105  -43.908  -25.296  1.00 31.13  ? 171 PRO   B CG     1 
ATOM   4709  C  CD     . PRO   B 2  171 ? 15.159  -45.234  -26.014  1.00 38.12  ? 171 PRO   B CD     1 
ATOM   4710  N  N      . SER   B 2  172 ? 10.921  -43.703  -24.831  1.00 43.69  ? 172 SER   B N      1 
ATOM   4711  C  CA     . SER   B 2  172 ? 9.836   -42.868  -25.361  1.00 38.06  ? 172 SER   B CA     1 
ATOM   4712  C  C      . SER   B 2  172 ? 9.176   -41.989  -24.303  1.00 42.15  ? 172 SER   B C      1 
ATOM   4713  O  O      . SER   B 2  172 ? 8.682   -42.484  -23.275  1.00 42.37  ? 172 SER   B O      1 
ATOM   4714  C  CB     . SER   B 2  172 ? 8.742   -43.725  -26.002  1.00 41.99  ? 172 SER   B CB     1 
ATOM   4715  O  OG     . SER   B 2  172 ? 7.784   -42.889  -26.648  1.00 44.87  ? 172 SER   B OG     1 
ATOM   4716  N  N      . PRO   B 2  173 ? 9.096   -40.705  -24.548  1.00 40.55  ? 173 PRO   B N      1 
ATOM   4717  C  CA     . PRO   B 2  173 ? 8.283   -39.815  -23.692  1.00 38.26  ? 173 PRO   B CA     1 
ATOM   4718  C  C      . PRO   B 2  173 ? 6.931   -40.375  -23.266  1.00 40.57  ? 173 PRO   B C      1 
ATOM   4719  O  O      . PRO   B 2  173 ? 6.420   -39.997  -22.209  1.00 48.28  ? 173 PRO   B O      1 
ATOM   4720  C  CB     . PRO   B 2  173 ? 8.088   -38.578  -24.566  1.00 33.49  ? 173 PRO   B CB     1 
ATOM   4721  C  CG     . PRO   B 2  173 ? 9.298   -38.568  -25.463  1.00 42.93  ? 173 PRO   B CG     1 
ATOM   4722  C  CD     . PRO   B 2  173 ? 9.728   -40.007  -25.674  1.00 40.94  ? 173 PRO   B CD     1 
ATOM   4723  N  N      . LYS   B 2  174 ? 6.337   -41.276  -24.050  1.00 36.99  ? 174 LYS   B N      1 
ATOM   4724  C  CA     . LYS   B 2  174 ? 5.095   -41.894  -23.607  1.00 38.93  ? 174 LYS   B CA     1 
ATOM   4725  C  C      . LYS   B 2  174 ? 5.325   -42.921  -22.501  1.00 42.77  ? 174 LYS   B C      1 
ATOM   4726  O  O      . LYS   B 2  174 ? 4.392   -43.235  -21.752  1.00 45.93  ? 174 LYS   B O      1 
ATOM   4727  C  CB     . LYS   B 2  174 ? 4.358   -42.545  -24.788  1.00 42.87  ? 174 LYS   B CB     1 
ATOM   4728  C  CG     . LYS   B 2  174 ? 3.920   -41.585  -25.927  1.00 41.59  ? 174 LYS   B CG     1 
ATOM   4729  C  CD     . LYS   B 2  174 ? 3.881   -42.288  -27.288  1.00 46.93  ? 174 LYS   B CD     1 
ATOM   4730  C  CE     . LYS   B 2  174 ? 2.680   -41.855  -28.129  1.00 49.86  ? 174 LYS   B CE     1 
ATOM   4731  N  NZ     . LYS   B 2  174 ? 2.766   -42.355  -29.547  1.00 50.54  ? 174 LYS   B NZ     1 
ATOM   4732  N  N      . VAL   B 2  175 ? 6.532   -43.467  -22.387  1.00 42.50  ? 175 VAL   B N      1 
ATOM   4733  C  CA     . VAL   B 2  175 ? 6.850   -44.376  -21.290  1.00 39.76  ? 175 VAL   B CA     1 
ATOM   4734  C  C      . VAL   B 2  175 ? 8.246   -44.027  -20.789  1.00 44.51  ? 175 VAL   B C      1 
ATOM   4735  O  O      . VAL   B 2  175 ? 9.222   -44.698  -21.146  1.00 56.02  ? 175 VAL   B O      1 
ATOM   4736  C  CB     . VAL   B 2  175 ? 6.788   -45.851  -21.731  1.00 38.30  ? 175 VAL   B CB     1 
ATOM   4737  C  CG1    . VAL   B 2  175 ? 6.468   -46.738  -20.551  1.00 37.89  ? 175 VAL   B CG1    1 
ATOM   4738  C  CG2    . VAL   B 2  175 ? 5.822   -46.059  -22.891  1.00 34.97  ? 175 VAL   B CG2    1 
ATOM   4739  N  N      . SER   B 2  176 ? 8.388   -42.971  -19.991  1.00 41.56  ? 176 SER   B N      1 
ATOM   4740  C  CA     . SER   B 2  176 ? 9.728   -42.493  -19.709  1.00 43.66  ? 176 SER   B CA     1 
ATOM   4741  C  C      . SER   B 2  176 ? 9.928   -42.341  -18.213  1.00 42.69  ? 176 SER   B C      1 
ATOM   4742  O  O      . SER   B 2  176 ? 9.057   -41.816  -17.514  1.00 37.85  ? 176 SER   B O      1 
ATOM   4743  C  CB     . SER   B 2  176 ? 10.016  -41.179  -20.445  1.00 42.70  ? 176 SER   B CB     1 
ATOM   4744  O  OG     . SER   B 2  176 ? 9.954   -40.064  -19.609  1.00 49.05  ? 176 SER   B OG     1 
ATOM   4745  N  N      . ASP   B 2  177 ? 11.077  -42.837  -17.734  1.00 39.55  ? 177 ASP   B N      1 
ATOM   4746  C  CA     . ASP   B 2  177 ? 11.450  -42.710  -16.329  1.00 43.88  ? 177 ASP   B CA     1 
ATOM   4747  C  C      . ASP   B 2  177 ? 12.014  -41.317  -16.021  1.00 45.24  ? 177 ASP   B C      1 
ATOM   4748  O  O      . ASP   B 2  177 ? 11.675  -40.719  -14.990  1.00 41.71  ? 177 ASP   B O      1 
ATOM   4749  C  CB     . ASP   B 2  177 ? 12.479  -43.787  -15.938  1.00 45.15  ? 177 ASP   B CB     1 
ATOM   4750  C  CG     . ASP   B 2  177 ? 11.940  -45.224  -16.028  1.00 47.54  ? 177 ASP   B CG     1 
ATOM   4751  O  OD1    . ASP   B 2  177 ? 10.727  -45.407  -16.254  1.00 49.53  ? 177 ASP   B OD1    1 
ATOM   4752  O  OD2    . ASP   B 2  177 ? 12.753  -46.183  -15.866  1.00 46.73  ? 177 ASP   B OD2    1 
ATOM   4753  N  N      . THR   B 2  178 ? 12.877  -40.786  -16.894  1.00 38.91  ? 178 THR   B N      1 
ATOM   4754  C  CA     . THR   B 2  178 ? 13.613  -39.558  -16.608  1.00 38.92  ? 178 THR   B CA     1 
ATOM   4755  C  C      . THR   B 2  178 ? 13.884  -38.828  -17.912  1.00 34.96  ? 178 THR   B C      1 
ATOM   4756  O  O      . THR   B 2  178 ? 13.707  -39.381  -18.993  1.00 37.46  ? 178 THR   B O      1 
ATOM   4757  C  CB     . THR   B 2  178 ? 14.929  -39.840  -15.872  1.00 42.58  ? 178 THR   B CB     1 
ATOM   4758  O  OG1    . THR   B 2  178 ? 15.719  -40.756  -16.636  1.00 41.12  ? 178 THR   B OG1    1 
ATOM   4759  C  CG2    . THR   B 2  178 ? 14.656  -40.439  -14.473  1.00 43.48  ? 178 THR   B CG2    1 
ATOM   4760  N  N      . VAL   B 2  179 ? 14.304  -37.563  -17.808  1.00 32.31  ? 179 VAL   B N      1 
ATOM   4761  C  CA     . VAL   B 2  179 ? 14.452  -36.769  -19.024  1.00 29.26  ? 179 VAL   B CA     1 
ATOM   4762  C  C      . VAL   B 2  179 ? 15.768  -37.009  -19.738  1.00 35.19  ? 179 VAL   B C      1 
ATOM   4763  O  O      . VAL   B 2  179 ? 15.940  -36.526  -20.874  1.00 34.82  ? 179 VAL   B O      1 
ATOM   4764  C  CB     . VAL   B 2  179 ? 14.376  -35.245  -18.817  1.00 33.64  ? 179 VAL   B CB     1 
ATOM   4765  C  CG1    . VAL   B 2  179 ? 12.942  -34.834  -18.653  1.00 39.70  ? 179 VAL   B CG1    1 
ATOM   4766  C  CG2    . VAL   B 2  179 ? 15.245  -34.807  -17.651  1.00 33.48  ? 179 VAL   B CG2    1 
ATOM   4767  N  N      . VAL   B 2  180 ? 16.713  -37.724  -19.115  1.00 29.02  ? 180 VAL   B N      1 
ATOM   4768  C  CA     . VAL   B 2  180 ? 17.995  -37.949  -19.771  1.00 34.12  ? 180 VAL   B CA     1 
ATOM   4769  C  C      . VAL   B 2  180 ? 17.984  -39.161  -20.711  1.00 34.72  ? 180 VAL   B C      1 
ATOM   4770  O  O      . VAL   B 2  180 ? 19.013  -39.448  -21.336  1.00 32.90  ? 180 VAL   B O      1 
ATOM   4771  C  CB     . VAL   B 2  180 ? 19.135  -38.061  -18.732  1.00 29.64  ? 180 VAL   B CB     1 
ATOM   4772  C  CG1    . VAL   B 2  180 ? 19.408  -36.711  -18.136  1.00 22.05  ? 180 VAL   B CG1    1 
ATOM   4773  C  CG2    . VAL   B 2  180 ? 18.826  -39.099  -17.681  1.00 28.88  ? 180 VAL   B CG2    1 
ATOM   4774  N  N      . GLU   B 2  181 ? 16.854  -39.863  -20.860  1.00 38.48  ? 181 GLU   B N      1 
ATOM   4775  C  CA     . GLU   B 2  181 ? 16.819  -41.020  -21.760  1.00 35.27  ? 181 GLU   B CA     1 
ATOM   4776  C  C      . GLU   B 2  181 ? 17.335  -40.716  -23.164  1.00 35.30  ? 181 GLU   B C      1 
ATOM   4777  O  O      . GLU   B 2  181 ? 18.078  -41.547  -23.708  1.00 37.59  ? 181 GLU   B O      1 
ATOM   4778  C  CB     . GLU   B 2  181 ? 15.400  -41.612  -21.803  1.00 34.73  ? 181 GLU   B CB     1 
ATOM   4779  C  CG     . GLU   B 2  181 ? 15.029  -42.298  -20.484  1.00 38.52  ? 181 GLU   B CG     1 
ATOM   4780  C  CD     . GLU   B 2  181 ? 13.538  -42.464  -20.231  1.00 39.05  ? 181 GLU   B CD     1 
ATOM   4781  O  OE1    . GLU   B 2  181 ? 12.691  -42.007  -21.046  1.00 43.22  ? 181 GLU   B OE1    1 
ATOM   4782  O  OE2    . GLU   B 2  181 ? 13.218  -42.966  -19.133  1.00 42.57  ? 181 GLU   B OE2    1 
ATOM   4783  N  N      . PRO   B 2  182 ? 17.022  -39.591  -23.796  1.00 28.97  ? 182 PRO   B N      1 
ATOM   4784  C  CA     . PRO   B 2  182 ? 17.616  -39.347  -25.115  1.00 30.47  ? 182 PRO   B CA     1 
ATOM   4785  C  C      . PRO   B 2  182 ? 19.133  -39.266  -25.078  1.00 33.39  ? 182 PRO   B C      1 
ATOM   4786  O  O      . PRO   B 2  182 ? 19.791  -39.724  -26.025  1.00 39.63  ? 182 PRO   B O      1 
ATOM   4787  C  CB     . PRO   B 2  182 ? 16.968  -38.022  -25.552  1.00 34.83  ? 182 PRO   B CB     1 
ATOM   4788  C  CG     . PRO   B 2  182 ? 15.744  -37.922  -24.735  1.00 32.76  ? 182 PRO   B CG     1 
ATOM   4789  C  CD     . PRO   B 2  182 ? 16.092  -38.529  -23.412  1.00 27.91  ? 182 PRO   B CD     1 
ATOM   4790  N  N      . TYR   B 2  183 ? 19.711  -38.679  -24.024  1.00 33.65  ? 183 TYR   B N      1 
ATOM   4791  C  CA     . TYR   B 2  183 ? 21.166  -38.708  -23.838  1.00 34.35  ? 183 TYR   B CA     1 
ATOM   4792  C  C      . TYR   B 2  183 ? 21.688  -40.138  -23.736  1.00 33.19  ? 183 TYR   B C      1 
ATOM   4793  O  O      . TYR   B 2  183 ? 22.657  -40.505  -24.406  1.00 31.57  ? 183 TYR   B O      1 
ATOM   4794  C  CB     . TYR   B 2  183 ? 21.558  -37.943  -22.576  1.00 31.42  ? 183 TYR   B CB     1 
ATOM   4795  C  CG     . TYR   B 2  183 ? 21.547  -36.449  -22.674  1.00 30.09  ? 183 TYR   B CG     1 
ATOM   4796  C  CD1    . TYR   B 2  183 ? 21.667  -35.813  -23.874  1.00 36.43  ? 183 TYR   B CD1    1 
ATOM   4797  C  CD2    . TYR   B 2  183 ? 21.432  -35.675  -21.537  1.00 32.79  ? 183 TYR   B CD2    1 
ATOM   4798  C  CE1    . TYR   B 2  183 ? 21.674  -34.433  -23.944  1.00 42.45  ? 183 TYR   B CE1    1 
ATOM   4799  C  CE2    . TYR   B 2  183 ? 21.432  -34.309  -21.586  1.00 31.21  ? 183 TYR   B CE2    1 
ATOM   4800  C  CZ     . TYR   B 2  183 ? 21.558  -33.685  -22.789  1.00 38.97  ? 183 TYR   B CZ     1 
ATOM   4801  O  OH     . TYR   B 2  183 ? 21.569  -32.313  -22.849  1.00 38.95  ? 183 TYR   B OH     1 
ATOM   4802  N  N      . ASN   B 2  184 ? 21.087  -40.946  -22.856  1.00 31.95  ? 184 ASN   B N      1 
ATOM   4803  C  CA     . ASN   B 2  184 ? 21.565  -42.307  -22.656  1.00 35.12  ? 184 ASN   B CA     1 
ATOM   4804  C  C      . ASN   B 2  184 ? 21.469  -43.127  -23.941  1.00 41.24  ? 184 ASN   B C      1 
ATOM   4805  O  O      . ASN   B 2  184 ? 22.363  -43.930  -24.245  1.00 44.13  ? 184 ASN   B O      1 
ATOM   4806  C  CB     . ASN   B 2  184 ? 20.785  -42.983  -21.523  1.00 33.31  ? 184 ASN   B CB     1 
ATOM   4807  C  CG     . ASN   B 2  184 ? 21.045  -42.337  -20.151  1.00 41.21  ? 184 ASN   B CG     1 
ATOM   4808  O  OD1    . ASN   B 2  184 ? 22.038  -41.606  -19.978  1.00 38.71  ? 184 ASN   B OD1    1 
ATOM   4809  N  ND2    . ASN   B 2  184 ? 20.138  -42.584  -19.173  1.00 32.10  ? 184 ASN   B ND2    1 
ATOM   4810  N  N      . ALA   B 2  185 ? 20.399  -42.932  -24.720  1.00 37.01  ? 185 ALA   B N      1 
ATOM   4811  C  CA     . ALA   B 2  185 ? 20.183  -43.767  -25.895  1.00 34.57  ? 185 ALA   B CA     1 
ATOM   4812  C  C      . ALA   B 2  185 ? 21.100  -43.369  -27.051  1.00 37.59  ? 185 ALA   B C      1 
ATOM   4813  O  O      . ALA   B 2  185 ? 21.624  -44.243  -27.755  1.00 39.28  ? 185 ALA   B O      1 
ATOM   4814  C  CB     . ALA   B 2  185 ? 18.714  -43.716  -26.309  1.00 33.67  ? 185 ALA   B CB     1 
ATOM   4815  N  N      . THR   B 2  186 ? 21.303  -42.066  -27.267  1.00 34.45  ? 186 THR   B N      1 
ATOM   4816  C  CA     . THR   B 2  186 ? 22.250  -41.619  -28.294  1.00 35.38  ? 186 THR   B CA     1 
ATOM   4817  C  C      . THR   B 2  186 ? 23.652  -42.139  -28.021  1.00 34.56  ? 186 THR   B C      1 
ATOM   4818  O  O      . THR   B 2  186 ? 24.356  -42.569  -28.945  1.00 36.60  ? 186 THR   B O      1 
ATOM   4819  C  CB     . THR   B 2  186 ? 22.283  -40.092  -28.370  1.00 36.78  ? 186 THR   B CB     1 
ATOM   4820  O  OG1    . THR   B 2  186 ? 20.960  -39.568  -28.604  1.00 37.10  ? 186 THR   B OG1    1 
ATOM   4821  C  CG2    . THR   B 2  186 ? 23.270  -39.631  -29.426  1.00 32.91  ? 186 THR   B CG2    1 
ATOM   4822  N  N      . LEU   B 2  187 ? 24.083  -42.091  -26.757  1.00 37.69  ? 187 LEU   B N      1 
ATOM   4823  C  CA     . LEU   B 2  187 ? 25.383  -42.655  -26.401  1.00 41.88  ? 187 LEU   B CA     1 
ATOM   4824  C  C      . LEU   B 2  187 ? 25.430  -44.148  -26.692  1.00 39.50  ? 187 LEU   B C      1 
ATOM   4825  O  O      . LEU   B 2  187 ? 26.433  -44.649  -27.208  1.00 42.42  ? 187 LEU   B O      1 
ATOM   4826  C  CB     . LEU   B 2  187 ? 25.711  -42.392  -24.925  1.00 38.18  ? 187 LEU   B CB     1 
ATOM   4827  C  CG     . LEU   B 2  187 ? 25.931  -40.920  -24.563  1.00 39.92  ? 187 LEU   B CG     1 
ATOM   4828  C  CD1    . LEU   B 2  187 ? 25.719  -40.654  -23.065  1.00 37.01  ? 187 LEU   B CD1    1 
ATOM   4829  C  CD2    . LEU   B 2  187 ? 27.308  -40.475  -25.028  1.00 37.70  ? 187 LEU   B CD2    1 
ATOM   4830  N  N      . SER   B 2  188 ? 24.350  -44.871  -26.374  1.00 36.12  ? 188 SER   B N      1 
ATOM   4831  C  CA     . SER   B 2  188 ? 24.330  -46.308  -26.604  1.00 35.45  ? 188 SER   B CA     1 
ATOM   4832  C  C      . SER   B 2  188 ? 24.256  -46.619  -28.089  1.00 35.09  ? 188 SER   B C      1 
ATOM   4833  O  O      . SER   B 2  188 ? 24.899  -47.558  -28.559  1.00 37.30  ? 188 SER   B O      1 
ATOM   4834  C  CB     . SER   B 2  188 ? 23.144  -46.948  -25.884  1.00 39.28  ? 188 SER   B CB     1 
ATOM   4835  O  OG     . SER   B 2  188 ? 23.295  -46.904  -24.490  1.00 38.73  ? 188 SER   B OG     1 
ATOM   4836  N  N      . VAL   B 2  189 ? 23.455  -45.862  -28.843  1.00 34.51  ? 189 VAL   B N      1 
ATOM   4837  C  CA     . VAL   B 2  189 ? 23.276  -46.179  -30.256  1.00 35.01  ? 189 VAL   B CA     1 
ATOM   4838  C  C      . VAL   B 2  189 ? 24.613  -46.114  -30.975  1.00 37.39  ? 189 VAL   B C      1 
ATOM   4839  O  O      . VAL   B 2  189 ? 24.905  -46.928  -31.855  1.00 36.94  ? 189 VAL   B O      1 
ATOM   4840  C  CB     . VAL   B 2  189 ? 22.230  -45.247  -30.888  1.00 37.21  ? 189 VAL   B CB     1 
ATOM   4841  C  CG1    . VAL   B 2  189 ? 22.264  -45.360  -32.415  1.00 38.18  ? 189 VAL   B CG1    1 
ATOM   4842  C  CG2    . VAL   B 2  189 ? 20.841  -45.570  -30.337  1.00 36.96  ? 189 VAL   B CG2    1 
ATOM   4843  N  N      . HIS   B 2  190 ? 25.462  -45.173  -30.570  1.00 42.12  ? 190 HIS   B N      1 
ATOM   4844  C  CA     . HIS   B 2  190 ? 26.836  -45.101  -31.056  1.00 39.82  ? 190 HIS   B CA     1 
ATOM   4845  C  C      . HIS   B 2  190 ? 27.578  -46.409  -30.815  1.00 43.57  ? 190 HIS   B C      1 
ATOM   4846  O  O      . HIS   B 2  190 ? 28.183  -46.983  -31.734  1.00 46.94  ? 190 HIS   B O      1 
ATOM   4847  C  CB     . HIS   B 2  190 ? 27.537  -43.947  -30.353  1.00 43.79  ? 190 HIS   B CB     1 
ATOM   4848  C  CG     . HIS   B 2  190 ? 28.883  -43.632  -30.909  1.00 55.39  ? 190 HIS   B CG     1 
ATOM   4849  N  ND1    . HIS   B 2  190 ? 29.594  -44.525  -31.688  1.00 55.21  ? 190 HIS   B ND1    1 
ATOM   4850  C  CD2    . HIS   B 2  190 ? 29.654  -42.524  -30.796  1.00 51.93  ? 190 HIS   B CD2    1 
ATOM   4851  C  CE1    . HIS   B 2  190 ? 30.748  -43.979  -32.029  1.00 60.43  ? 190 HIS   B CE1    1 
ATOM   4852  N  NE2    . HIS   B 2  190 ? 30.805  -42.763  -31.510  1.00 63.52  ? 190 HIS   B NE2    1 
ATOM   4853  N  N      . GLN   B 2  191 ? 27.553  -46.889  -29.572  1.00 36.98  ? 191 GLN   B N      1 
ATOM   4854  C  CA     . GLN   B 2  191 ? 28.095  -48.207  -29.275  1.00 37.10  ? 191 GLN   B CA     1 
ATOM   4855  C  C      . GLN   B 2  191 ? 27.502  -49.295  -30.179  1.00 40.16  ? 191 GLN   B C      1 
ATOM   4856  O  O      . GLN   B 2  191 ? 28.240  -50.124  -30.725  1.00 35.84  ? 191 GLN   B O      1 
ATOM   4857  C  CB     . GLN   B 2  191 ? 27.856  -48.513  -27.809  1.00 31.12  ? 191 GLN   B CB     1 
ATOM   4858  C  CG     . GLN   B 2  191 ? 28.455  -47.458  -26.956  1.00 38.69  ? 191 GLN   B CG     1 
ATOM   4859  C  CD     . GLN   B 2  191 ? 29.965  -47.507  -27.021  1.00 37.65  ? 191 GLN   B CD     1 
ATOM   4860  O  OE1    . GLN   B 2  191 ? 30.572  -48.563  -26.822  1.00 43.09  ? 191 GLN   B OE1    1 
ATOM   4861  N  NE2    . GLN   B 2  191 ? 30.575  -46.383  -27.331  1.00 35.57  ? 191 GLN   B NE2    1 
ATOM   4862  N  N      . LEU   B 2  192 ? 26.165  -49.305  -30.357  1.00 39.20  ? 192 LEU   B N      1 
ATOM   4863  C  CA     . LEU   B 2  192 ? 25.527  -50.432  -31.038  1.00 37.40  ? 192 LEU   B CA     1 
ATOM   4864  C  C      . LEU   B 2  192 ? 25.896  -50.471  -32.514  1.00 36.00  ? 192 LEU   B C      1 
ATOM   4865  O  O      . LEU   B 2  192 ? 26.116  -51.552  -33.067  1.00 36.58  ? 192 LEU   B O      1 
ATOM   4866  C  CB     . LEU   B 2  192 ? 24.008  -50.397  -30.857  1.00 33.00  ? 192 LEU   B CB     1 
ATOM   4867  C  CG     . LEU   B 2  192 ? 23.524  -50.563  -29.412  1.00 35.03  ? 192 LEU   B CG     1 
ATOM   4868  C  CD1    . LEU   B 2  192 ? 22.012  -50.470  -29.315  1.00 28.49  ? 192 LEU   B CD1    1 
ATOM   4869  C  CD2    . LEU   B 2  192 ? 24.032  -51.857  -28.778  1.00 33.47  ? 192 LEU   B CD2    1 
ATOM   4870  N  N      . VAL   B 2  193 ? 26.010  -49.304  -33.154  1.00 38.00  ? 193 VAL   B N      1 
ATOM   4871  C  CA     . VAL   B 2  193 ? 26.396  -49.239  -34.563  1.00 41.12  ? 193 VAL   B CA     1 
ATOM   4872  C  C      . VAL   B 2  193 ? 27.746  -49.898  -34.775  1.00 42.90  ? 193 VAL   B C      1 
ATOM   4873  O  O      . VAL   B 2  193 ? 28.000  -50.513  -35.817  1.00 42.19  ? 193 VAL   B O      1 
ATOM   4874  C  CB     . VAL   B 2  193 ? 26.430  -47.778  -35.057  1.00 41.08  ? 193 VAL   B CB     1 
ATOM   4875  C  CG1    . VAL   B 2  193 ? 27.089  -47.716  -36.411  1.00 43.05  ? 193 VAL   B CG1    1 
ATOM   4876  C  CG2    . VAL   B 2  193 ? 25.049  -47.220  -35.169  1.00 42.96  ? 193 VAL   B CG2    1 
ATOM   4877  N  N      . GLU   B 2  194 ? 28.638  -49.762  -33.802  1.00 43.36  ? 194 GLU   B N      1 
ATOM   4878  C  CA     . GLU   B 2  194 ? 29.991  -50.266  -33.946  1.00 41.38  ? 194 GLU   B CA     1 
ATOM   4879  C  C      . GLU   B 2  194 ? 30.122  -51.730  -33.553  1.00 45.03  ? 194 GLU   B C      1 
ATOM   4880  O  O      . GLU   B 2  194 ? 30.827  -52.492  -34.229  1.00 49.97  ? 194 GLU   B O      1 
ATOM   4881  C  CB     . GLU   B 2  194 ? 30.937  -49.413  -33.109  1.00 49.35  ? 194 GLU   B CB     1 
ATOM   4882  C  CG     . GLU   B 2  194 ? 30.887  -47.963  -33.494  1.00 54.70  ? 194 GLU   B CG     1 
ATOM   4883  C  CD     . GLU   B 2  194 ? 31.994  -47.619  -34.441  1.00 63.58  ? 194 GLU   B CD     1 
ATOM   4884  O  OE1    . GLU   B 2  194 ? 33.164  -47.817  -34.030  1.00 68.21  ? 194 GLU   B OE1    1 
ATOM   4885  O  OE2    . GLU   B 2  194 ? 31.694  -47.190  -35.588  1.00 59.59  ? 194 GLU   B OE2    1 
ATOM   4886  N  N      . ASN   B 2  195 ? 29.446  -52.162  -32.490  1.00 42.98  ? 195 ASN   B N      1 
ATOM   4887  C  CA     . ASN   B 2  195 ? 29.808  -53.418  -31.844  1.00 44.12  ? 195 ASN   B CA     1 
ATOM   4888  C  C      . ASN   B 2  195 ? 28.740  -54.500  -31.860  1.00 37.85  ? 195 ASN   B C      1 
ATOM   4889  O  O      . ASN   B 2  195 ? 28.904  -55.507  -31.170  1.00 38.87  ? 195 ASN   B O      1 
ATOM   4890  C  CB     . ASN   B 2  195 ? 30.227  -53.147  -30.403  1.00 43.46  ? 195 ASN   B CB     1 
ATOM   4891  C  CG     . ASN   B 2  195 ? 31.550  -52.469  -30.336  1.00 44.39  ? 195 ASN   B CG     1 
ATOM   4892  O  OD1    . ASN   B 2  195 ? 32.398  -52.701  -31.195  1.00 46.17  ? 195 ASN   B OD1    1 
ATOM   4893  N  ND2    . ASN   B 2  195 ? 31.746  -51.616  -29.333  1.00 48.58  ? 195 ASN   B ND2    1 
ATOM   4894  N  N      . THR   B 2  196 ? 27.658  -54.347  -32.603  1.00 35.56  ? 196 THR   B N      1 
ATOM   4895  C  CA     . THR   B 2  196 ? 26.759  -55.478  -32.752  1.00 38.73  ? 196 THR   B CA     1 
ATOM   4896  C  C      . THR   B 2  196 ? 26.634  -55.861  -34.223  1.00 36.74  ? 196 THR   B C      1 
ATOM   4897  O  O      . THR   B 2  196 ? 26.755  -55.018  -35.119  1.00 36.60  ? 196 THR   B O      1 
ATOM   4898  C  CB     . THR   B 2  196 ? 25.357  -55.206  -32.154  1.00 38.27  ? 196 THR   B CB     1 
ATOM   4899  O  OG1    . THR   B 2  196 ? 24.678  -54.203  -32.925  1.00 37.93  ? 196 THR   B OG1    1 
ATOM   4900  C  CG2    . THR   B 2  196 ? 25.464  -54.776  -30.726  1.00 29.41  ? 196 THR   B CG2    1 
ATOM   4901  N  N      . ASP   B 2  197 ? 26.411  -57.160  -34.445  1.00 35.65  ? 197 ASP   B N      1 
ATOM   4902  C  CA     . ASP   B 2  197 ? 25.952  -57.670  -35.736  1.00 36.24  ? 197 ASP   B CA     1 
ATOM   4903  C  C      . ASP   B 2  197 ? 24.449  -57.477  -35.939  1.00 39.86  ? 197 ASP   B C      1 
ATOM   4904  O  O      . ASP   B 2  197 ? 24.012  -57.127  -37.044  1.00 41.51  ? 197 ASP   B O      1 
ATOM   4905  C  CB     . ASP   B 2  197 ? 26.302  -59.150  -35.844  1.00 43.58  ? 197 ASP   B CB     1 
ATOM   4906  C  CG     . ASP   B 2  197 ? 27.780  -59.415  -35.599  1.00 39.35  ? 197 ASP   B CG     1 
ATOM   4907  O  OD1    . ASP   B 2  197 ? 28.564  -58.873  -36.386  1.00 37.71  ? 197 ASP   B OD1    1 
ATOM   4908  O  OD2    . ASP   B 2  197 ? 28.134  -60.141  -34.633  1.00 35.85  ? 197 ASP   B OD2    1 
ATOM   4909  N  N      . GLU   B 2  198 ? 23.640  -57.679  -34.893  1.00 39.76  ? 198 GLU   B N      1 
ATOM   4910  C  CA     . GLU   B 2  198 ? 22.180  -57.649  -35.012  1.00 38.02  ? 198 GLU   B CA     1 
ATOM   4911  C  C      . GLU   B 2  198 ? 21.560  -56.996  -33.790  1.00 36.35  ? 198 GLU   B C      1 
ATOM   4912  O  O      . GLU   B 2  198 ? 21.742  -57.497  -32.677  1.00 41.67  ? 198 GLU   B O      1 
ATOM   4913  C  CB     . GLU   B 2  198 ? 21.607  -59.070  -35.161  1.00 35.66  ? 198 GLU   B CB     1 
ATOM   4914  C  CG     . GLU   B 2  198 ? 22.038  -59.795  -36.409  1.00 32.56  ? 198 GLU   B CG     1 
ATOM   4915  C  CD     . GLU   B 2  198 ? 22.408  -61.225  -36.135  1.00 34.42  ? 198 GLU   B CD     1 
ATOM   4916  O  OE1    . GLU   B 2  198 ? 22.421  -61.647  -34.962  1.00 37.54  ? 198 GLU   B OE1    1 
ATOM   4917  O  OE2    . GLU   B 2  198 ? 22.694  -61.946  -37.098  1.00 40.37  ? 198 GLU   B OE2    1 
ATOM   4918  N  N      . THR   B 2  199 ? 20.786  -55.925  -33.982  1.00 32.73  ? 199 THR   B N      1 
ATOM   4919  C  CA     . THR   B 2  199 ? 19.991  -55.387  -32.880  1.00 34.62  ? 199 THR   B CA     1 
ATOM   4920  C  C      . THR   B 2  199 ? 18.539  -55.255  -33.314  1.00 33.78  ? 199 THR   B C      1 
ATOM   4921  O  O      . THR   B 2  199 ? 18.233  -54.681  -34.372  1.00 33.03  ? 199 THR   B O      1 
ATOM   4922  C  CB     . THR   B 2  199 ? 20.538  -54.036  -32.345  1.00 34.22  ? 199 THR   B CB     1 
ATOM   4923  O  OG1    . THR   B 2  199 ? 20.519  -53.052  -33.388  1.00 49.38  ? 199 THR   B OG1    1 
ATOM   4924  C  CG2    . THR   B 2  199 ? 21.967  -54.161  -31.860  1.00 34.50  ? 199 THR   B CG2    1 
ATOM   4925  N  N      . TYR   B 2  200 ? 17.656  -55.800  -32.488  1.00 31.74  ? 200 TYR   B N      1 
ATOM   4926  C  CA     . TYR   B 2  200 ? 16.219  -55.645  -32.647  1.00 32.89  ? 200 TYR   B CA     1 
ATOM   4927  C  C      . TYR   B 2  200 ? 15.765  -54.372  -31.932  1.00 33.63  ? 200 TYR   B C      1 
ATOM   4928  O  O      . TYR   B 2  200 ? 15.937  -54.239  -30.722  1.00 30.33  ? 200 TYR   B O      1 
ATOM   4929  C  CB     . TYR   B 2  200 ? 15.492  -56.864  -32.094  1.00 33.56  ? 200 TYR   B CB     1 
ATOM   4930  C  CG     . TYR   B 2  200 ? 15.776  -58.153  -32.841  1.00 40.02  ? 200 TYR   B CG     1 
ATOM   4931  C  CD1    . TYR   B 2  200 ? 15.134  -58.444  -34.044  1.00 40.57  ? 200 TYR   B CD1    1 
ATOM   4932  C  CD2    . TYR   B 2  200 ? 16.652  -59.098  -32.334  1.00 37.47  ? 200 TYR   B CD2    1 
ATOM   4933  C  CE1    . TYR   B 2  200 ? 15.374  -59.631  -34.720  1.00 35.91  ? 200 TYR   B CE1    1 
ATOM   4934  C  CE2    . TYR   B 2  200 ? 16.896  -60.274  -33.012  1.00 36.93  ? 200 TYR   B CE2    1 
ATOM   4935  C  CZ     . TYR   B 2  200 ? 16.261  -60.537  -34.202  1.00 35.13  ? 200 TYR   B CZ     1 
ATOM   4936  O  OH     . TYR   B 2  200 ? 16.507  -61.732  -34.853  1.00 39.77  ? 200 TYR   B OH     1 
ATOM   4937  N  N      . CYS   B 2  201 ? 15.203  -53.432  -32.682  1.00 34.82  ? 201 CYS   B N      1 
ATOM   4938  C  CA     . CYS   B 2  201 ? 14.799  -52.154  -32.116  1.00 30.74  ? 201 CYS   B CA     1 
ATOM   4939  C  C      . CYS   B 2  201 ? 13.398  -52.290  -31.549  1.00 35.71  ? 201 CYS   B C      1 
ATOM   4940  O  O      . CYS   B 2  201 ? 12.410  -52.065  -32.238  1.00 40.66  ? 201 CYS   B O      1 
ATOM   4941  C  CB     . CYS   B 2  201 ? 14.854  -51.060  -33.168  1.00 37.40  ? 201 CYS   B CB     1 
ATOM   4942  S  SG     . CYS   B 2  201 ? 16.473  -50.792  -33.862  1.00 46.98  ? 201 CYS   B SG     1 
ATOM   4943  N  N      . ILE   B 2  202 ? 13.309  -52.651  -30.272  1.00 31.68  ? 202 ILE   B N      1 
ATOM   4944  C  CA     . ILE   B 2  202 ? 12.046  -52.689  -29.536  1.00 35.30  ? 202 ILE   B CA     1 
ATOM   4945  C  C      . ILE   B 2  202 ? 11.744  -51.282  -29.015  1.00 35.08  ? 202 ILE   B C      1 
ATOM   4946  O  O      . ILE   B 2  202 ? 12.206  -50.882  -27.948  1.00 38.11  ? 202 ILE   B O      1 
ATOM   4947  C  CB     . ILE   B 2  202 ? 12.111  -53.717  -28.409  1.00 36.61  ? 202 ILE   B CB     1 
ATOM   4948  C  CG1    . ILE   B 2  202 ? 12.113  -55.114  -29.025  1.00 32.93  ? 202 ILE   B CG1    1 
ATOM   4949  C  CG2    . ILE   B 2  202 ? 11.012  -53.503  -27.394  1.00 32.43  ? 202 ILE   B CG2    1 
ATOM   4950  C  CD1    . ILE   B 2  202 ? 13.447  -55.718  -29.026  1.00 34.90  ? 202 ILE   B CD1    1 
ATOM   4951  N  N      . ASP   B 2  203 ? 10.959  -50.528  -29.768  1.00 30.50  ? 203 ASP   B N      1 
ATOM   4952  C  CA     . ASP   B 2  203 ? 10.602  -49.169  -29.406  1.00 33.24  ? 203 ASP   B CA     1 
ATOM   4953  C  C      . ASP   B 2  203 ? 9.519   -49.162  -28.335  1.00 39.49  ? 203 ASP   B C      1 
ATOM   4954  O  O      . ASP   B 2  203 ? 8.480   -49.806  -28.498  1.00 43.89  ? 203 ASP   B O      1 
ATOM   4955  C  CB     . ASP   B 2  203 ? 10.101  -48.433  -30.646  1.00 36.73  ? 203 ASP   B CB     1 
ATOM   4956  C  CG     . ASP   B 2  203 ? 10.038  -46.921  -30.456  1.00 37.80  ? 203 ASP   B CG     1 
ATOM   4957  O  OD1    . ASP   B 2  203 ? 10.173  -46.439  -29.314  1.00 40.44  ? 203 ASP   B OD1    1 
ATOM   4958  O  OD2    . ASP   B 2  203 ? 9.854   -46.207  -31.460  1.00 39.79  ? 203 ASP   B OD2    1 
ATOM   4959  N  N      . ASN   B 2  204 ? 9.742   -48.428  -27.242  1.00 32.65  ? 204 ASN   B N      1 
ATOM   4960  C  CA     . ASN   B 2  204 ? 8.672   -48.320  -26.265  1.00 32.08  ? 204 ASN   B CA     1 
ATOM   4961  C  C      . ASN   B 2  204 ? 7.556   -47.428  -26.771  1.00 39.53  ? 204 ASN   B C      1 
ATOM   4962  O  O      . ASN   B 2  204 ? 6.438   -47.496  -26.252  1.00 39.60  ? 204 ASN   B O      1 
ATOM   4963  C  CB     . ASN   B 2  204 ? 9.187   -47.786  -24.943  1.00 30.93  ? 204 ASN   B CB     1 
ATOM   4964  C  CG     . ASN   B 2  204 ? 9.476   -48.859  -23.974  1.00 30.61  ? 204 ASN   B CG     1 
ATOM   4965  O  OD1    . ASN   B 2  204 ? 9.353   -50.029  -24.288  1.00 33.52  ? 204 ASN   B OD1    1 
ATOM   4966  N  ND2    . ASN   B 2  204 ? 9.907   -48.478  -22.785  1.00 33.87  ? 204 ASN   B ND2    1 
ATOM   4967  N  N      . GLU   B 2  205 ? 7.835   -46.572  -27.752  1.00 37.06  ? 205 GLU   B N      1 
ATOM   4968  C  CA     . GLU   B 2  205 ? 6.756   -45.818  -28.368  1.00 44.74  ? 205 GLU   B CA     1 
ATOM   4969  C  C      . GLU   B 2  205 ? 5.788   -46.762  -29.073  1.00 47.94  ? 205 GLU   B C      1 
ATOM   4970  O  O      . GLU   B 2  205 ? 4.574   -46.721  -28.830  1.00 45.09  ? 205 GLU   B O      1 
ATOM   4971  C  CB     . GLU   B 2  205 ? 7.321   -44.779  -29.332  1.00 39.31  ? 205 GLU   B CB     1 
ATOM   4972  C  CG     . GLU   B 2  205 ? 6.264   -44.059  -30.151  1.00 47.87  ? 205 GLU   B CG     1 
ATOM   4973  C  CD     . GLU   B 2  205 ? 6.379   -42.547  -30.021  1.00 56.58  ? 205 GLU   B CD     1 
ATOM   4974  O  OE1    . GLU   B 2  205 ? 6.931   -42.107  -28.987  1.00 52.07  ? 205 GLU   B OE1    1 
ATOM   4975  O  OE2    . GLU   B 2  205 ? 5.958   -41.807  -30.948  1.00 53.58  ? 205 GLU   B OE2    1 
ATOM   4976  N  N      . ALA   B 2  206 ? 6.322   -47.660  -29.911  1.00 45.01  ? 206 ALA   B N      1 
ATOM   4977  C  CA     . ALA   B 2  206 ? 5.465   -48.590  -30.640  1.00 44.56  ? 206 ALA   B CA     1 
ATOM   4978  C  C      . ALA   B 2  206 ? 4.782   -49.583  -29.701  1.00 47.38  ? 206 ALA   B C      1 
ATOM   4979  O  O      . ALA   B 2  206 ? 3.609   -49.921  -29.905  1.00 50.04  ? 206 ALA   B O      1 
ATOM   4980  C  CB     . ALA   B 2  206 ? 6.264   -49.320  -31.719  1.00 36.82  ? 206 ALA   B CB     1 
ATOM   4981  N  N      . LEU   B 2  207 ? 5.477   -50.071  -28.669  1.00 39.18  ? 207 LEU   B N      1 
ATOM   4982  C  CA     . LEU   B 2  207 ? 4.781   -50.935  -27.725  1.00 39.51  ? 207 LEU   B CA     1 
ATOM   4983  C  C      . LEU   B 2  207 ? 3.631   -50.198  -27.071  1.00 42.95  ? 207 LEU   B C      1 
ATOM   4984  O  O      . LEU   B 2  207 ? 2.597   -50.804  -26.773  1.00 45.91  ? 207 LEU   B O      1 
ATOM   4985  C  CB     . LEU   B 2  207 ? 5.730   -51.475  -26.650  1.00 40.96  ? 207 LEU   B CB     1 
ATOM   4986  C  CG     . LEU   B 2  207 ? 6.999   -52.163  -27.141  1.00 41.47  ? 207 LEU   B CG     1 
ATOM   4987  C  CD1    . LEU   B 2  207 ? 7.757   -52.770  -25.980  1.00 36.36  ? 207 LEU   B CD1    1 
ATOM   4988  C  CD2    . LEU   B 2  207 ? 6.592   -53.212  -28.139  1.00 39.30  ? 207 LEU   B CD2    1 
ATOM   4989  N  N      . TYR   B 2  208 ? 3.787   -48.890  -26.832  1.00 50.09  ? 208 TYR   B N      1 
ATOM   4990  C  CA     . TYR   B 2  208 ? 2.750   -48.149  -26.116  1.00 44.36  ? 208 TYR   B CA     1 
ATOM   4991  C  C      . TYR   B 2  208 ? 1.509   -47.991  -26.979  1.00 45.74  ? 208 TYR   B C      1 
ATOM   4992  O  O      . TYR   B 2  208 ? 0.402   -48.359  -26.565  1.00 45.08  ? 208 TYR   B O      1 
ATOM   4993  C  CB     . TYR   B 2  208 ? 3.261   -46.780  -25.661  1.00 43.57  ? 208 TYR   B CB     1 
ATOM   4994  C  CG     . TYR   B 2  208 ? 2.212   -46.049  -24.851  1.00 48.39  ? 208 TYR   B CG     1 
ATOM   4995  C  CD1    . TYR   B 2  208 ? 2.093   -46.263  -23.483  1.00 46.48  ? 208 TYR   B CD1    1 
ATOM   4996  C  CD2    . TYR   B 2  208 ? 1.286   -45.196  -25.469  1.00 49.41  ? 208 TYR   B CD2    1 
ATOM   4997  C  CE1    . TYR   B 2  208 ? 1.098   -45.623  -22.737  1.00 54.75  ? 208 TYR   B CE1    1 
ATOM   4998  C  CE2    . TYR   B 2  208 ? 0.290   -44.552  -24.734  1.00 46.98  ? 208 TYR   B CE2    1 
ATOM   4999  C  CZ     . TYR   B 2  208 ? 0.198   -44.765  -23.366  1.00 53.22  ? 208 TYR   B CZ     1 
ATOM   5000  O  OH     . TYR   B 2  208 ? -0.780  -44.139  -22.611  1.00 53.46  ? 208 TYR   B OH     1 
ATOM   5001  N  N      . ASP   B 2  209 ? 1.682   -47.456  -28.188  1.00 39.94  ? 209 ASP   B N      1 
ATOM   5002  C  CA     . ASP   B 2  209 ? 0.565   -47.314  -29.104  1.00 45.71  ? 209 ASP   B CA     1 
ATOM   5003  C  C      . ASP   B 2  209 ? -0.145  -48.643  -29.342  1.00 48.25  ? 209 ASP   B C      1 
ATOM   5004  O  O      . ASP   B 2  209 ? -1.375  -48.716  -29.307  1.00 48.85  ? 209 ASP   B O      1 
ATOM   5005  C  CB     . ASP   B 2  209 ? 1.074   -46.716  -30.403  1.00 44.77  ? 209 ASP   B CB     1 
ATOM   5006  C  CG     . ASP   B 2  209 ? 1.649   -45.333  -30.201  1.00 50.48  ? 209 ASP   B CG     1 
ATOM   5007  O  OD1    . ASP   B 2  209 ? 1.213   -44.655  -29.240  1.00 48.70  ? 209 ASP   B OD1    1 
ATOM   5008  O  OD2    . ASP   B 2  209 ? 2.565   -44.940  -30.969  1.00 57.16  ? 209 ASP   B OD2    1 
ATOM   5009  N  N      . ILE   B 2  210 ? 0.609   -49.712  -29.585  1.00 45.62  ? 210 ILE   B N      1 
ATOM   5010  C  CA     . ILE   B 2  210 ? -0.038  -51.001  -29.797  1.00 44.51  ? 210 ILE   B CA     1 
ATOM   5011  C  C      . ILE   B 2  210 ? -0.868  -51.372  -28.577  1.00 48.42  ? 210 ILE   B C      1 
ATOM   5012  O  O      . ILE   B 2  210 ? -1.960  -51.940  -28.699  1.00 55.76  ? 210 ILE   B O      1 
ATOM   5013  C  CB     . ILE   B 2  210 ? 1.005   -52.082  -30.148  1.00 44.75  ? 210 ILE   B CB     1 
ATOM   5014  C  CG1    . ILE   B 2  210 ? 1.630   -51.801  -31.514  1.00 41.37  ? 210 ILE   B CG1    1 
ATOM   5015  C  CG2    . ILE   B 2  210 ? 0.393   -53.454  -30.140  1.00 43.58  ? 210 ILE   B CG2    1 
ATOM   5016  C  CD1    . ILE   B 2  210 ? 2.853   -52.606  -31.757  1.00 39.40  ? 210 ILE   B CD1    1 
ATOM   5017  N  N      . CYS   B 2  211 ? -0.383  -51.038  -27.382  1.00 46.00  ? 211 CYS   B N      1 
ATOM   5018  C  CA     . CYS   B 2  211 ? -1.164  -51.316  -26.181  1.00 49.22  ? 211 CYS   B CA     1 
ATOM   5019  C  C      . CYS   B 2  211 ? -2.404  -50.427  -26.099  1.00 52.24  ? 211 CYS   B C      1 
ATOM   5020  O  O      . CYS   B 2  211 ? -3.470  -50.871  -25.670  1.00 53.60  ? 211 CYS   B O      1 
ATOM   5021  C  CB     . CYS   B 2  211 ? -0.294  -51.139  -24.945  1.00 43.01  ? 211 CYS   B CB     1 
ATOM   5022  S  SG     . CYS   B 2  211 ? 0.521   -52.625  -24.467  1.00 45.44  ? 211 CYS   B SG     1 
ATOM   5023  N  N      . PHE   B 2  212 ? -2.286  -49.177  -26.523  1.00 50.62  ? 212 PHE   B N      1 
ATOM   5024  C  CA     . PHE   B 2  212 ? -3.359  -48.204  -26.380  1.00 53.57  ? 212 PHE   B CA     1 
ATOM   5025  C  C      . PHE   B 2  212 ? -4.357  -48.298  -27.541  1.00 60.98  ? 212 PHE   B C      1 
ATOM   5026  O  O      . PHE   B 2  212 ? -5.540  -48.588  -27.330  1.00 67.58  ? 212 PHE   B O      1 
ATOM   5027  C  CB     . PHE   B 2  212 ? -2.711  -46.822  -26.270  1.00 53.18  ? 212 PHE   B CB     1 
ATOM   5028  C  CG     . PHE   B 2  212 ? -3.661  -45.675  -26.279  1.00 61.15  ? 212 PHE   B CG     1 
ATOM   5029  C  CD1    . PHE   B 2  212 ? -4.218  -45.202  -25.096  1.00 62.80  ? 212 PHE   B CD1    1 
ATOM   5030  C  CD2    . PHE   B 2  212 ? -3.958  -45.023  -27.468  1.00 65.58  ? 212 PHE   B CD2    1 
ATOM   5031  C  CE1    . PHE   B 2  212 ? -5.079  -44.115  -25.100  1.00 67.02  ? 212 PHE   B CE1    1 
ATOM   5032  C  CE2    . PHE   B 2  212 ? -4.815  -43.923  -27.486  1.00 64.58  ? 212 PHE   B CE2    1 
ATOM   5033  C  CZ     . PHE   B 2  212 ? -5.377  -43.468  -26.300  1.00 67.30  ? 212 PHE   B CZ     1 
ATOM   5034  N  N      . ARG   B 2  213 ? -3.885  -48.108  -28.781  1.00 57.15  ? 213 ARG   B N      1 
ATOM   5035  C  CA     . ARG   B 2  213 ? -4.779  -48.082  -29.941  1.00 58.57  ? 213 ARG   B CA     1 
ATOM   5036  C  C      . ARG   B 2  213 ? -5.323  -49.461  -30.275  1.00 56.75  ? 213 ARG   B C      1 
ATOM   5037  O  O      . ARG   B 2  213 ? -6.526  -49.630  -30.473  1.00 68.83  ? 213 ARG   B O      1 
ATOM   5038  C  CB     . ARG   B 2  213 ? -4.064  -47.507  -31.160  1.00 56.67  ? 213 ARG   B CB     1 
ATOM   5039  C  CG     . ARG   B 2  213 ? -3.571  -46.093  -30.956  1.00 61.11  ? 213 ARG   B CG     1 
ATOM   5040  C  CD     . ARG   B 2  213 ? -2.491  -45.758  -31.954  1.00 60.28  ? 213 ARG   B CD     1 
ATOM   5041  N  NE     . ARG   B 2  213 ? -1.808  -44.515  -31.612  1.00 67.69  ? 213 ARG   B NE     1 
ATOM   5042  C  CZ     . ARG   B 2  213 ? -0.950  -43.885  -32.410  1.00 63.99  ? 213 ARG   B CZ     1 
ATOM   5043  N  NH1    . ARG   B 2  213 ? -0.632  -44.367  -33.600  1.00 65.70  ? 213 ARG   B NH1    1 
ATOM   5044  N  NH2    . ARG   B 2  213 ? -0.403  -42.738  -32.005  1.00 50.89  ? 213 ARG   B NH2    1 
ATOM   5045  N  N      . THR   B 2  214 ? -4.468  -50.460  -30.365  1.00 59.84  ? 214 THR   B N      1 
ATOM   5046  C  CA     . THR   B 2  214 ? -4.973  -51.709  -30.923  1.00 63.80  ? 214 THR   B CA     1 
ATOM   5047  C  C      . THR   B 2  214 ? -5.469  -52.687  -29.857  1.00 64.20  ? 214 THR   B C      1 
ATOM   5048  O  O      . THR   B 2  214 ? -6.466  -53.379  -30.081  1.00 75.38  ? 214 THR   B O      1 
ATOM   5049  C  CB     . THR   B 2  214 ? -3.905  -52.362  -31.817  1.00 58.58  ? 214 THR   B CB     1 
ATOM   5050  O  OG1    . THR   B 2  214 ? -3.587  -51.467  -32.893  1.00 57.11  ? 214 THR   B OG1    1 
ATOM   5051  C  CG2    . THR   B 2  214 ? -4.408  -53.663  -32.390  1.00 50.25  ? 214 THR   B CG2    1 
ATOM   5052  N  N      . LEU   B 2  215 ? -4.822  -52.778  -28.703  1.00 58.30  ? 215 LEU   B N      1 
ATOM   5053  C  CA     . LEU   B 2  215 ? -5.327  -53.657  -27.654  1.00 60.42  ? 215 LEU   B CA     1 
ATOM   5054  C  C      . LEU   B 2  215 ? -6.335  -52.968  -26.762  1.00 65.24  ? 215 LEU   B C      1 
ATOM   5055  O  O      . LEU   B 2  215 ? -6.877  -53.607  -25.847  1.00 59.76  ? 215 LEU   B O      1 
ATOM   5056  C  CB     . LEU   B 2  215 ? -4.180  -54.176  -26.803  1.00 64.11  ? 215 LEU   B CB     1 
ATOM   5057  C  CG     . LEU   B 2  215 ? -3.157  -54.794  -27.726  1.00 60.57  ? 215 LEU   B CG     1 
ATOM   5058  C  CD1    . LEU   B 2  215 ? -2.179  -55.642  -26.935  1.00 56.55  ? 215 LEU   B CD1    1 
ATOM   5059  C  CD2    . LEU   B 2  215 ? -3.935  -55.593  -28.782  1.00 58.34  ? 215 LEU   B CD2    1 
ATOM   5060  N  N      . LYS   B 2  216 ? -6.562  -51.671  -27.001  1.00 69.91  ? 216 LYS   B N      1 
ATOM   5061  C  CA     . LYS   B 2  216 ? -7.512  -50.830  -26.268  1.00 72.07  ? 216 LYS   B CA     1 
ATOM   5062  C  C      . LYS   B 2  216 ? -7.206  -50.753  -24.762  1.00 67.38  ? 216 LYS   B C      1 
ATOM   5063  O  O      . LYS   B 2  216 ? -8.077  -50.403  -23.966  1.00 74.18  ? 216 LYS   B O      1 
ATOM   5064  C  CB     . LYS   B 2  216 ? -8.964  -51.287  -26.519  1.00 65.66  ? 216 LYS   B CB     1 
ATOM   5065  C  CG     . LYS   B 2  216 ? -9.423  -51.234  -28.013  1.00 55.26  ? 216 LYS   B CG     1 
ATOM   5066  C  CD     . LYS   B 2  216 ? -9.110  -49.877  -28.645  1.00 59.85  ? 216 LYS   B CD     1 
ATOM   5067  C  CE     . LYS   B 2  216 ? -9.555  -49.778  -30.106  1.00 57.42  ? 216 LYS   B CE     1 
ATOM   5068  N  NZ     . LYS   B 2  216 ? -9.007  -48.555  -30.815  1.00 52.28  ? 216 LYS   B NZ     1 
ATOM   5069  N  N      . LEU   B 2  217 ? -5.978  -51.051  -24.348  1.00 64.90  ? 217 LEU   B N      1 
ATOM   5070  C  CA     . LEU   B 2  217 ? -5.560  -50.871  -22.956  1.00 63.48  ? 217 LEU   B CA     1 
ATOM   5071  C  C      . LEU   B 2  217 ? -5.452  -49.377  -22.643  1.00 62.64  ? 217 LEU   B C      1 
ATOM   5072  O  O      . LEU   B 2  217 ? -4.587  -48.670  -23.167  1.00 60.94  ? 217 LEU   B O      1 
ATOM   5073  C  CB     . LEU   B 2  217 ? -4.239  -51.594  -22.715  1.00 58.09  ? 217 LEU   B CB     1 
ATOM   5074  C  CG     . LEU   B 2  217 ? -4.404  -53.095  -22.989  1.00 63.63  ? 217 LEU   B CG     1 
ATOM   5075  C  CD1    . LEU   B 2  217 ? -3.081  -53.843  -22.969  1.00 51.26  ? 217 LEU   B CD1    1 
ATOM   5076  C  CD2    . LEU   B 2  217 ? -5.369  -53.694  -21.987  1.00 57.78  ? 217 LEU   B CD2    1 
ATOM   5077  N  N      . THR   B 2  218 ? -6.346  -48.888  -21.795  1.00 69.72  ? 218 THR   B N      1 
ATOM   5078  C  CA     . THR   B 2  218 ? -6.382  -47.460  -21.502  1.00 71.42  ? 218 THR   B CA     1 
ATOM   5079  C  C      . THR   B 2  218 ? -5.081  -46.990  -20.853  1.00 61.81  ? 218 THR   B C      1 
ATOM   5080  O  O      . THR   B 2  218 ? -4.542  -45.936  -21.215  1.00 55.79  ? 218 THR   B O      1 
ATOM   5081  C  CB     . THR   B 2  218 ? -7.598  -47.144  -20.609  1.00 78.52  ? 218 THR   B CB     1 
ATOM   5082  O  OG1    . THR   B 2  218 ? -7.557  -45.769  -20.192  1.00 71.94  ? 218 THR   B OG1    1 
ATOM   5083  C  CG2    . THR   B 2  218 ? -7.655  -48.073  -19.360  1.00 72.53  ? 218 THR   B CG2    1 
ATOM   5084  N  N      . THR   B 2  219 ? -4.567  -47.752  -19.880  1.00 60.21  ? 219 THR   B N      1 
ATOM   5085  C  CA     . THR   B 2  219 ? -3.396  -47.354  -19.094  1.00 63.47  ? 219 THR   B CA     1 
ATOM   5086  C  C      . THR   B 2  219 ? -2.410  -48.513  -19.001  1.00 59.22  ? 219 THR   B C      1 
ATOM   5087  O  O      . THR   B 2  219 ? -2.418  -49.288  -18.024  1.00 59.06  ? 219 THR   B O      1 
ATOM   5088  C  CB     . THR   B 2  219 ? -3.806  -46.865  -17.706  1.00 62.76  ? 219 THR   B CB     1 
ATOM   5089  O  OG1    . THR   B 2  219 ? -4.447  -45.585  -17.830  1.00 64.18  ? 219 THR   B OG1    1 
ATOM   5090  C  CG2    . THR   B 2  219 ? -2.581  -46.712  -16.831  1.00 58.00  ? 219 THR   B CG2    1 
ATOM   5091  N  N      . PRO   B 2  220 ? -1.520  -48.637  -19.991  1.00 50.69  ? 220 PRO   B N      1 
ATOM   5092  C  CA     . PRO   B 2  220 ? -0.663  -49.832  -20.119  1.00 53.46  ? 220 PRO   B CA     1 
ATOM   5093  C  C      . PRO   B 2  220 ? 0.515   -49.811  -19.153  1.00 54.11  ? 220 PRO   B C      1 
ATOM   5094  O  O      . PRO   B 2  220 ? 1.251   -48.825  -19.085  1.00 50.34  ? 220 PRO   B O      1 
ATOM   5095  C  CB     . PRO   B 2  220 ? -0.173  -49.763  -21.571  1.00 54.65  ? 220 PRO   B CB     1 
ATOM   5096  C  CG     . PRO   B 2  220 ? -0.957  -48.603  -22.231  1.00 53.80  ? 220 PRO   B CG     1 
ATOM   5097  C  CD     . PRO   B 2  220 ? -1.358  -47.703  -21.115  1.00 56.59  ? 220 PRO   B CD     1 
ATOM   5098  N  N      . THR   B 2  221 ? 0.695   -50.914  -18.419  1.00 45.90  ? 221 THR   B N      1 
ATOM   5099  C  CA     . THR   B 2  221 ? 1.853   -51.107  -17.565  1.00 42.59  ? 221 THR   B CA     1 
ATOM   5100  C  C      . THR   B 2  221 ? 3.073   -51.610  -18.363  1.00 47.72  ? 221 THR   B C      1 
ATOM   5101  O  O      . THR   B 2  221 ? 3.015   -51.879  -19.568  1.00 50.72  ? 221 THR   B O      1 
ATOM   5102  C  CB     . THR   B 2  221 ? 1.506   -52.084  -16.458  1.00 50.39  ? 221 THR   B CB     1 
ATOM   5103  O  OG1    . THR   B 2  221 ? 1.307   -53.402  -17.000  1.00 44.26  ? 221 THR   B OG1    1 
ATOM   5104  C  CG2    . THR   B 2  221 ? 0.255   -51.619  -15.769  1.00 52.87  ? 221 THR   B CG2    1 
ATOM   5105  N  N      . TYR   B 2  222 ? 4.214   -51.705  -17.683  1.00 44.28  ? 222 TYR   B N      1 
ATOM   5106  C  CA     . TYR   B 2  222 ? 5.343   -52.395  -18.296  1.00 46.04  ? 222 TYR   B CA     1 
ATOM   5107  C  C      . TYR   B 2  222 ? 5.004   -53.859  -18.556  1.00 48.01  ? 222 TYR   B C      1 
ATOM   5108  O  O      . TYR   B 2  222 ? 5.440   -54.426  -19.567  1.00 50.67  ? 222 TYR   B O      1 
ATOM   5109  C  CB     . TYR   B 2  222 ? 6.602   -52.265  -17.430  1.00 34.05  ? 222 TYR   B CB     1 
ATOM   5110  C  CG     . TYR   B 2  222 ? 7.285   -50.923  -17.554  1.00 38.81  ? 222 TYR   B CG     1 
ATOM   5111  C  CD1    . TYR   B 2  222 ? 7.378   -50.270  -18.788  1.00 43.51  ? 222 TYR   B CD1    1 
ATOM   5112  C  CD2    . TYR   B 2  222 ? 7.835   -50.299  -16.453  1.00 34.79  ? 222 TYR   B CD2    1 
ATOM   5113  C  CE1    . TYR   B 2  222 ? 8.008   -49.029  -18.900  1.00 34.93  ? 222 TYR   B CE1    1 
ATOM   5114  C  CE2    . TYR   B 2  222 ? 8.456   -49.076  -16.553  1.00 31.00  ? 222 TYR   B CE2    1 
ATOM   5115  C  CZ     . TYR   B 2  222 ? 8.536   -48.440  -17.766  1.00 36.07  ? 222 TYR   B CZ     1 
ATOM   5116  O  OH     . TYR   B 2  222 ? 9.152   -47.206  -17.836  1.00 40.67  ? 222 TYR   B OH     1 
ATOM   5117  N  N      . GLY   B 2  223 ? 4.197   -54.476  -17.686  1.00 44.82  ? 223 GLY   B N      1 
ATOM   5118  C  CA     . GLY   B 2  223 ? 3.780   -55.849  -17.925  1.00 44.90  ? 223 GLY   B CA     1 
ATOM   5119  C  C      . GLY   B 2  223 ? 3.022   -56.019  -19.228  1.00 51.01  ? 223 GLY   B C      1 
ATOM   5120  O  O      . GLY   B 2  223 ? 3.108   -57.071  -19.872  1.00 52.14  ? 223 GLY   B O      1 
ATOM   5121  N  N      . ASP   B 2  224 ? 2.273   -54.994  -19.637  1.00 49.16  ? 224 ASP   B N      1 
ATOM   5122  C  CA     . ASP   B 2  224 ? 1.592   -55.050  -20.927  1.00 51.69  ? 224 ASP   B CA     1 
ATOM   5123  C  C      . ASP   B 2  224 ? 2.583   -54.908  -22.063  1.00 50.74  ? 224 ASP   B C      1 
ATOM   5124  O  O      . ASP   B 2  224 ? 2.565   -55.690  -23.024  1.00 51.10  ? 224 ASP   B O      1 
ATOM   5125  C  CB     . ASP   B 2  224 ? 0.528   -53.953  -21.023  1.00 53.78  ? 224 ASP   B CB     1 
ATOM   5126  C  CG     . ASP   B 2  224 ? -0.587  -54.139  -20.016  1.00 55.47  ? 224 ASP   B CG     1 
ATOM   5127  O  OD1    . ASP   B 2  224 ? -1.085  -55.281  -19.902  1.00 51.86  ? 224 ASP   B OD1    1 
ATOM   5128  O  OD2    . ASP   B 2  224 ? -0.936  -53.151  -19.328  1.00 55.36  ? 224 ASP   B OD2    1 
ATOM   5129  N  N      . LEU   B 2  225 ? 3.443   -53.891  -21.978  1.00 52.39  ? 225 LEU   B N      1 
ATOM   5130  C  CA     . LEU   B 2  225 ? 4.519   -53.741  -22.952  1.00 50.18  ? 225 LEU   B CA     1 
ATOM   5131  C  C      . LEU   B 2  225 ? 5.351   -55.016  -23.067  1.00 50.19  ? 225 LEU   B C      1 
ATOM   5132  O  O      . LEU   B 2  225 ? 5.743   -55.417  -24.174  1.00 47.43  ? 225 LEU   B O      1 
ATOM   5133  C  CB     . LEU   B 2  225 ? 5.419   -52.568  -22.562  1.00 44.69  ? 225 LEU   B CB     1 
ATOM   5134  C  CG     . LEU   B 2  225 ? 4.781   -51.203  -22.358  1.00 48.39  ? 225 LEU   B CG     1 
ATOM   5135  C  CD1    . LEU   B 2  225 ? 5.874   -50.119  -22.358  1.00 39.31  ? 225 LEU   B CD1    1 
ATOM   5136  C  CD2    . LEU   B 2  225 ? 3.730   -50.960  -23.438  1.00 45.12  ? 225 LEU   B CD2    1 
ATOM   5137  N  N      . ASN   B 2  226 ? 5.640   -55.665  -21.930  1.00 45.03  ? 226 ASN   B N      1 
ATOM   5138  C  CA     . ASN   B 2  226 ? 6.578   -56.781  -21.932  1.00 46.58  ? 226 ASN   B CA     1 
ATOM   5139  C  C      . ASN   B 2  226 ? 5.957   -58.074  -22.430  1.00 46.35  ? 226 ASN   B C      1 
ATOM   5140  O  O      . ASN   B 2  226 ? 6.675   -58.951  -22.918  1.00 44.49  ? 226 ASN   B O      1 
ATOM   5141  C  CB     . ASN   B 2  226 ? 7.154   -56.955  -20.539  1.00 41.51  ? 226 ASN   B CB     1 
ATOM   5142  C  CG     . ASN   B 2  226 ? 8.107   -55.833  -20.179  1.00 47.11  ? 226 ASN   B CG     1 
ATOM   5143  O  OD1    . ASN   B 2  226 ? 8.499   -55.042  -21.051  1.00 42.53  ? 226 ASN   B OD1    1 
ATOM   5144  N  ND2    . ASN   B 2  226 ? 8.474   -55.740  -18.897  1.00 43.46  ? 226 ASN   B ND2    1 
ATOM   5145  N  N      . HIS   B 2  227 ? 4.638   -58.195  -22.332  1.00 55.42  ? 227 HIS   B N      1 
ATOM   5146  C  CA     . HIS   B 2  227 ? 3.923   -59.245  -23.043  1.00 50.60  ? 227 HIS   B CA     1 
ATOM   5147  C  C      . HIS   B 2  227 ? 4.169   -59.134  -24.541  1.00 47.76  ? 227 HIS   B C      1 
ATOM   5148  O  O      . HIS   B 2  227 ? 4.446   -60.129  -25.211  1.00 51.98  ? 227 HIS   B O      1 
ATOM   5149  C  CB     . HIS   B 2  227 ? 2.431   -59.148  -22.715  1.00 57.53  ? 227 HIS   B CB     1 
ATOM   5150  C  CG     . HIS   B 2  227 ? 1.572   -60.076  -23.507  1.00 61.67  ? 227 HIS   B CG     1 
ATOM   5151  N  ND1    . HIS   B 2  227 ? 1.636   -61.447  -23.368  1.00 62.96  ? 227 HIS   B ND1    1 
ATOM   5152  C  CD2    . HIS   B 2  227 ? 0.632   -59.832  -24.453  1.00 59.64  ? 227 HIS   B CD2    1 
ATOM   5153  C  CE1    . HIS   B 2  227 ? 0.773   -62.008  -24.199  1.00 66.33  ? 227 HIS   B CE1    1 
ATOM   5154  N  NE2    . HIS   B 2  227 ? 0.151   -61.050  -24.867  1.00 66.98  ? 227 HIS   B NE2    1 
ATOM   5155  N  N      . LEU   B 2  228 ? 4.094   -57.920  -25.088  1.00 49.21  ? 228 LEU   B N      1 
ATOM   5156  C  CA     . LEU   B 2  228 ? 4.434   -57.739  -26.497  1.00 45.86  ? 228 LEU   B CA     1 
ATOM   5157  C  C      . LEU   B 2  228 ? 5.893   -58.090  -26.764  1.00 48.56  ? 228 LEU   B C      1 
ATOM   5158  O  O      . LEU   B 2  228 ? 6.231   -58.627  -27.829  1.00 44.42  ? 228 LEU   B O      1 
ATOM   5159  C  CB     . LEU   B 2  228 ? 4.157   -56.298  -26.924  1.00 45.32  ? 228 LEU   B CB     1 
ATOM   5160  C  CG     . LEU   B 2  228 ? 2.700   -55.843  -26.990  1.00 46.04  ? 228 LEU   B CG     1 
ATOM   5161  C  CD1    . LEU   B 2  228 ? 2.613   -54.451  -27.599  1.00 44.89  ? 228 LEU   B CD1    1 
ATOM   5162  C  CD2    . LEU   B 2  228 ? 1.907   -56.827  -27.813  1.00 38.88  ? 228 LEU   B CD2    1 
ATOM   5163  N  N      . VAL   B 2  229 ? 6.773   -57.793  -25.809  1.00 47.16  ? 229 VAL   B N      1 
ATOM   5164  C  CA     . VAL   B 2  229 ? 8.196   -57.978  -26.041  1.00 43.75  ? 229 VAL   B CA     1 
ATOM   5165  C  C      . VAL   B 2  229 ? 8.553   -59.453  -25.993  1.00 45.93  ? 229 VAL   B C      1 
ATOM   5166  O  O      . VAL   B 2  229 ? 9.387   -59.926  -26.777  1.00 46.69  ? 229 VAL   B O      1 
ATOM   5167  C  CB     . VAL   B 2  229 ? 8.988   -57.134  -25.027  1.00 46.78  ? 229 VAL   B CB     1 
ATOM   5168  C  CG1    . VAL   B 2  229 ? 10.453  -57.539  -24.986  1.00 36.96  ? 229 VAL   B CG1    1 
ATOM   5169  C  CG2    . VAL   B 2  229 ? 8.817   -55.631  -25.352  1.00 44.66  ? 229 VAL   B CG2    1 
ATOM   5170  N  N      . SER   B 2  230 ? 7.890   -60.215  -25.122  1.00 42.01  ? 230 SER   B N      1 
ATOM   5171  C  CA     . SER   B 2  230 ? 8.166   -61.646  -25.061  1.00 49.10  ? 230 SER   B CA     1 
ATOM   5172  C  C      . SER   B 2  230 ? 7.596   -62.385  -26.276  1.00 50.75  ? 230 SER   B C      1 
ATOM   5173  O  O      . SER   B 2  230 ? 8.191   -63.367  -26.743  1.00 47.95  ? 230 SER   B O      1 
ATOM   5174  C  CB     . SER   B 2  230 ? 7.620   -62.221  -23.755  1.00 48.12  ? 230 SER   B CB     1 
ATOM   5175  O  OG     . SER   B 2  230 ? 6.232   -62.427  -23.858  1.00 50.48  ? 230 SER   B OG     1 
ATOM   5176  N  N      . ALA   B 2  231 ? 6.470   -61.911  -26.819  1.00 45.31  ? 231 ALA   B N      1 
ATOM   5177  C  CA     . ALA   B 2  231 ? 5.930   -62.484  -28.048  1.00 40.33  ? 231 ALA   B CA     1 
ATOM   5178  C  C      . ALA   B 2  231 ? 6.896   -62.297  -29.216  1.00 48.68  ? 231 ALA   B C      1 
ATOM   5179  O  O      . ALA   B 2  231 ? 7.179   -63.244  -29.959  1.00 47.05  ? 231 ALA   B O      1 
ATOM   5180  C  CB     . ALA   B 2  231 ? 4.578   -61.845  -28.368  1.00 41.12  ? 231 ALA   B CB     1 
ATOM   5181  N  N      . THR   B 2  232 ? 7.383   -61.065  -29.418  1.00 49.19  ? 232 THR   B N      1 
ATOM   5182  C  CA     . THR   B 2  232 ? 8.358   -60.818  -30.474  1.00 44.40  ? 232 THR   B CA     1 
ATOM   5183  C  C      . THR   B 2  232 ? 9.642   -61.608  -30.228  1.00 48.93  ? 232 THR   B C      1 
ATOM   5184  O  O      . THR   B 2  232 ? 10.230  -62.168  -31.167  1.00 46.70  ? 232 THR   B O      1 
ATOM   5185  C  CB     . THR   B 2  232 ? 8.662   -59.316  -30.589  1.00 45.53  ? 232 THR   B CB     1 
ATOM   5186  O  OG1    . THR   B 2  232 ? 7.456   -58.581  -30.844  1.00 48.43  ? 232 THR   B OG1    1 
ATOM   5187  C  CG2    . THR   B 2  232 ? 9.655   -59.032  -31.735  1.00 41.25  ? 232 THR   B CG2    1 
ATOM   5188  N  N      . MET   B 2  233 ? 10.088  -61.684  -28.973  1.00 42.77  ? 233 MET   B N      1 
ATOM   5189  C  CA     . MET   B 2  233 ? 11.363  -62.345  -28.718  1.00 47.02  ? 233 MET   B CA     1 
ATOM   5190  C  C      . MET   B 2  233 ? 11.272  -63.843  -28.990  1.00 47.83  ? 233 MET   B C      1 
ATOM   5191  O  O      . MET   B 2  233 ? 12.177  -64.427  -29.602  1.00 42.40  ? 233 MET   B O      1 
ATOM   5192  C  CB     . MET   B 2  233 ? 11.811  -62.069  -27.290  1.00 44.31  ? 233 MET   B CB     1 
ATOM   5193  C  CG     . MET   B 2  233 ? 12.464  -60.718  -27.170  1.00 39.64  ? 233 MET   B CG     1 
ATOM   5194  S  SD     . MET   B 2  233 ? 13.413  -60.653  -25.667  1.00 41.20  ? 233 MET   B SD     1 
ATOM   5195  C  CE     . MET   B 2  233 ? 12.072  -60.803  -24.489  1.00 51.89  ? 233 MET   B CE     1 
ATOM   5196  N  N      . SER   B 2  234 ? 10.174  -64.477  -28.569  1.00 48.82  ? 234 SER   B N      1 
ATOM   5197  C  CA     . SER   B 2  234 ? 9.962   -65.873  -28.936  1.00 50.06  ? 234 SER   B CA     1 
ATOM   5198  C  C      . SER   B 2  234 ? 9.927   -66.040  -30.452  1.00 49.57  ? 234 SER   B C      1 
ATOM   5199  O  O      . SER   B 2  234 ? 10.634  -66.886  -31.010  1.00 52.75  ? 234 SER   B O      1 
ATOM   5200  C  CB     . SER   B 2  234 ? 8.680   -66.400  -28.318  1.00 48.94  ? 234 SER   B CB     1 
ATOM   5201  O  OG     . SER   B 2  234 ? 8.201   -67.474  -29.092  1.00 46.82  ? 234 SER   B OG     1 
ATOM   5202  N  N      . GLY   B 2  235 ? 9.124   -65.226  -31.138  1.00 43.80  ? 235 GLY   B N      1 
ATOM   5203  C  CA     . GLY   B 2  235 ? 9.118   -65.179  -32.594  1.00 44.86  ? 235 GLY   B CA     1 
ATOM   5204  C  C      . GLY   B 2  235 ? 10.475  -65.144  -33.287  1.00 47.52  ? 235 GLY   B C      1 
ATOM   5205  O  O      . GLY   B 2  235 ? 10.826  -66.092  -33.992  1.00 42.15  ? 235 GLY   B O      1 
ATOM   5206  N  N      . VAL   B 2  236 ? 11.246  -64.061  -33.110  1.00 46.92  ? 236 VAL   B N      1 
ATOM   5207  C  CA     . VAL   B 2  236 ? 12.511  -63.912  -33.839  1.00 47.37  ? 236 VAL   B CA     1 
ATOM   5208  C  C      . VAL   B 2  236 ? 13.493  -65.040  -33.512  1.00 44.10  ? 236 VAL   B C      1 
ATOM   5209  O  O      . VAL   B 2  236 ? 14.352  -65.369  -34.334  1.00 50.40  ? 236 VAL   B O      1 
ATOM   5210  C  CB     . VAL   B 2  236 ? 13.161  -62.517  -33.587  1.00 45.33  ? 236 VAL   B CB     1 
ATOM   5211  C  CG1    . VAL   B 2  236 ? 12.276  -61.380  -34.085  1.00 37.00  ? 236 VAL   B CG1    1 
ATOM   5212  C  CG2    . VAL   B 2  236 ? 13.547  -62.309  -32.121  1.00 39.43  ? 236 VAL   B CG2    1 
ATOM   5213  N  N      . THR   B 2  237 ? 13.392  -65.658  -32.339  1.00 44.23  ? 237 THR   B N      1 
ATOM   5214  C  CA     . THR   B 2  237 ? 14.305  -66.746  -32.019  1.00 46.36  ? 237 THR   B CA     1 
ATOM   5215  C  C      . THR   B 2  237 ? 13.755  -68.120  -32.409  1.00 53.39  ? 237 THR   B C      1 
ATOM   5216  O  O      . THR   B 2  237 ? 14.424  -69.131  -32.151  1.00 52.32  ? 237 THR   B O      1 
ATOM   5217  C  CB     . THR   B 2  237 ? 14.687  -66.737  -30.510  1.00 51.50  ? 237 THR   B CB     1 
ATOM   5218  O  OG1    . THR   B 2  237 ? 13.533  -66.911  -29.658  1.00 42.83  ? 237 THR   B OG1    1 
ATOM   5219  C  CG2    . THR   B 2  237 ? 15.407  -65.457  -30.139  1.00 43.22  ? 237 THR   B CG2    1 
ATOM   5220  N  N      . THR   B 2  238 ? 12.566  -68.192  -33.020  1.00 48.96  ? 238 THR   B N      1 
ATOM   5221  C  CA     . THR   B 2  238 ? 12.021  -69.489  -33.416  1.00 52.47  ? 238 THR   B CA     1 
ATOM   5222  C  C      . THR   B 2  238 ? 13.039  -70.307  -34.207  1.00 55.36  ? 238 THR   B C      1 
ATOM   5223  O  O      . THR   B 2  238 ? 13.386  -71.430  -33.815  1.00 52.57  ? 238 THR   B O      1 
ATOM   5224  C  CB     . THR   B 2  238 ? 10.734  -69.323  -34.231  1.00 50.29  ? 238 THR   B CB     1 
ATOM   5225  O  OG1    . THR   B 2  238 ? 9.713   -68.744  -33.412  1.00 58.57  ? 238 THR   B OG1    1 
ATOM   5226  C  CG2    . THR   B 2  238 ? 10.238  -70.665  -34.695  1.00 46.72  ? 238 THR   B CG2    1 
ATOM   5227  N  N      . CYS   B 2  239 ? 13.555  -69.743  -35.327  1.00 49.07  ? 239 CYS   B N      1 
ATOM   5228  C  CA     . CYS   B 2  239 ? 14.324  -70.541  -36.269  1.00 50.24  ? 239 CYS   B CA     1 
ATOM   5229  C  C      . CYS   B 2  239 ? 15.686  -70.868  -35.789  1.00 58.70  ? 239 CYS   B C      1 
ATOM   5230  O  O      . CYS   B 2  239 ? 16.420  -71.408  -36.631  1.00 64.09  ? 239 CYS   B O      1 
ATOM   5231  C  CB     . CYS   B 2  239 ? 14.437  -69.835  -37.612  1.00 54.16  ? 239 CYS   B CB     1 
ATOM   5232  S  SG     . CYS   B 2  239 ? 12.887  -69.839  -38.512  1.00 56.80  ? 239 CYS   B SG     1 
ATOM   5233  N  N      . LEU   B 2  240 ? 15.991  -70.534  -34.534  1.00 55.75  ? 240 LEU   B N      1 
ATOM   5234  C  CA     . LEU   B 2  240 ? 17.209  -70.925  -33.845  1.00 47.95  ? 240 LEU   B CA     1 
ATOM   5235  C  C      . LEU   B 2  240 ? 16.983  -72.036  -32.832  1.00 49.91  ? 240 LEU   B C      1 
ATOM   5236  O  O      . LEU   B 2  240 ? 17.917  -72.792  -32.556  1.00 48.19  ? 240 LEU   B O      1 
ATOM   5237  C  CB     . LEU   B 2  240 ? 17.815  -69.723  -33.110  1.00 49.69  ? 240 LEU   B CB     1 
ATOM   5238  C  CG     . LEU   B 2  240 ? 18.178  -68.429  -33.819  1.00 45.40  ? 240 LEU   B CG     1 
ATOM   5239  C  CD1    . LEU   B 2  240 ? 18.278  -67.285  -32.817  1.00 42.98  ? 240 LEU   B CD1    1 
ATOM   5240  C  CD2    . LEU   B 2  240 ? 19.464  -68.608  -34.555  1.00 42.55  ? 240 LEU   B CD2    1 
ATOM   5241  N  N      . ARG   B 2  241 ? 15.778  -72.132  -32.249  1.00 53.34  ? 241 ARG   B N      1 
ATOM   5242  C  CA     . ARG   B 2  241 ? 15.476  -73.077  -31.173  1.00 55.43  ? 241 ARG   B CA     1 
ATOM   5243  C  C      . ARG   B 2  241 ? 14.759  -74.330  -31.632  1.00 55.51  ? 241 ARG   B C      1 
ATOM   5244  O  O      . ARG   B 2  241 ? 14.686  -75.298  -30.865  1.00 60.36  ? 241 ARG   B O      1 
ATOM   5245  C  CB     . ARG   B 2  241 ? 14.582  -72.442  -30.098  1.00 55.42  ? 241 ARG   B CB     1 
ATOM   5246  C  CG     . ARG   B 2  241 ? 15.012  -71.099  -29.616  1.00 54.48  ? 241 ARG   B CG     1 
ATOM   5247  C  CD     . ARG   B 2  241 ? 14.091  -70.609  -28.535  1.00 49.71  ? 241 ARG   B CD     1 
ATOM   5248  N  NE     . ARG   B 2  241 ? 12.994  -69.825  -29.078  1.00 47.78  ? 241 ARG   B NE     1 
ATOM   5249  C  CZ     . ARG   B 2  241 ? 11.720  -70.179  -28.988  1.00 50.48  ? 241 ARG   B CZ     1 
ATOM   5250  N  NH1    . ARG   B 2  241 ? 11.360  -71.308  -28.399  1.00 51.08  ? 241 ARG   B NH1    1 
ATOM   5251  N  NH2    . ARG   B 2  241 ? 10.785  -69.371  -29.483  1.00 45.63  ? 241 ARG   B NH2    1 
ATOM   5252  N  N      . PHE   B 2  242 ? 14.175  -74.320  -32.817  1.00 62.21  ? 242 PHE   B N      1 
ATOM   5253  C  CA     . PHE   B 2  242 ? 13.361  -75.432  -33.272  1.00 64.69  ? 242 PHE   B CA     1 
ATOM   5254  C  C      . PHE   B 2  242 ? 13.899  -75.998  -34.569  1.00 63.65  ? 242 PHE   B C      1 
ATOM   5255  O  O      . PHE   B 2  242 ? 14.583  -75.302  -35.331  1.00 59.42  ? 242 PHE   B O      1 
ATOM   5256  C  CB     . PHE   B 2  242 ? 11.900  -75.013  -33.468  1.00 56.12  ? 242 PHE   B CB     1 
ATOM   5257  C  CG     . PHE   B 2  242 ? 11.180  -74.832  -32.192  1.00 56.91  ? 242 PHE   B CG     1 
ATOM   5258  C  CD1    . PHE   B 2  242 ? 10.961  -75.913  -31.366  1.00 58.42  ? 242 PHE   B CD1    1 
ATOM   5259  C  CD2    . PHE   B 2  242 ? 10.739  -73.588  -31.804  1.00 55.06  ? 242 PHE   B CD2    1 
ATOM   5260  C  CE1    . PHE   B 2  242 ? 10.305  -75.763  -30.184  1.00 59.44  ? 242 PHE   B CE1    1 
ATOM   5261  C  CE2    . PHE   B 2  242 ? 10.078  -73.426  -30.616  1.00 53.80  ? 242 PHE   B CE2    1 
ATOM   5262  C  CZ     . PHE   B 2  242 ? 9.859   -74.516  -29.802  1.00 58.83  ? 242 PHE   B CZ     1 
ATOM   5263  N  N      . PRO   B 2  243 ? 13.612  -77.269  -34.844  1.00 68.56  ? 243 PRO   B N      1 
ATOM   5264  C  CA     . PRO   B 2  243 ? 14.016  -77.873  -36.116  1.00 65.65  ? 243 PRO   B CA     1 
ATOM   5265  C  C      . PRO   B 2  243 ? 13.041  -77.507  -37.223  1.00 68.22  ? 243 PRO   B C      1 
ATOM   5266  O  O      . PRO   B 2  243 ? 11.821  -77.504  -37.027  1.00 64.23  ? 243 PRO   B O      1 
ATOM   5267  C  CB     . PRO   B 2  243 ? 13.971  -79.373  -35.814  1.00 62.19  ? 243 PRO   B CB     1 
ATOM   5268  C  CG     . PRO   B 2  243 ? 12.881  -79.479  -34.799  1.00 67.06  ? 243 PRO   B CG     1 
ATOM   5269  C  CD     . PRO   B 2  243 ? 12.978  -78.243  -33.941  1.00 65.94  ? 243 PRO   B CD     1 
ATOM   5270  N  N      . GLY   B 2  244 ? 13.602  -77.159  -38.379  1.00 67.55  ? 244 GLY   B N      1 
ATOM   5271  C  CA     . GLY   B 2  244 ? 12.836  -76.883  -39.578  1.00 67.40  ? 244 GLY   B CA     1 
ATOM   5272  C  C      . GLY   B 2  244 ? 13.703  -77.016  -40.816  1.00 75.72  ? 244 GLY   B C      1 
ATOM   5273  O  O      . GLY   B 2  244 ? 14.844  -77.492  -40.754  1.00 73.45  ? 244 GLY   B O      1 
ATOM   5274  N  N      . GLN   B 2  245 ? 13.146  -76.589  -41.958  1.00 74.45  ? 245 GLN   B N      1 
ATOM   5275  C  CA     . GLN   B 2  245 ? 13.939  -76.593  -43.183  1.00 80.75  ? 245 GLN   B CA     1 
ATOM   5276  C  C      . GLN   B 2  245 ? 15.112  -75.636  -43.046  1.00 83.83  ? 245 GLN   B C      1 
ATOM   5277  O  O      . GLN   B 2  245 ? 16.239  -75.959  -43.444  1.00 82.93  ? 245 GLN   B O      1 
ATOM   5278  C  CB     . GLN   B 2  245 ? 13.069  -76.237  -44.391  1.00 85.20  ? 245 GLN   B CB     1 
ATOM   5279  C  CG     . GLN   B 2  245 ? 13.629  -76.722  -45.748  1.00 88.39  ? 245 GLN   B CG     1 
ATOM   5280  C  CD     . GLN   B 2  245 ? 14.271  -75.611  -46.596  1.00 87.96  ? 245 GLN   B CD     1 
ATOM   5281  O  OE1    . GLN   B 2  245 ? 14.797  -74.623  -46.059  1.00 87.79  ? 245 GLN   B OE1    1 
ATOM   5282  N  NE2    . GLN   B 2  245 ? 14.231  -75.777  -47.932  1.00 71.83  ? 245 GLN   B NE2    1 
ATOM   5283  N  N      . LEU   B 2  246 ? 14.874  -74.474  -42.427  1.00 85.38  ? 246 LEU   B N      1 
ATOM   5284  C  CA     . LEU   B 2  246 ? 15.909  -73.479  -42.177  1.00 80.65  ? 246 LEU   B CA     1 
ATOM   5285  C  C      . LEU   B 2  246 ? 16.983  -73.969  -41.217  1.00 79.12  ? 246 LEU   B C      1 
ATOM   5286  O  O      . LEU   B 2  246 ? 18.128  -74.199  -41.628  1.00 84.46  ? 246 LEU   B O      1 
ATOM   5287  C  CB     . LEU   B 2  246 ? 15.289  -72.201  -41.630  1.00 72.47  ? 246 LEU   B CB     1 
ATOM   5288  C  CG     . LEU   B 2  246 ? 15.570  -71.016  -42.544  1.00 64.46  ? 246 LEU   B CG     1 
ATOM   5289  C  CD1    . LEU   B 2  246 ? 15.214  -69.707  -41.852  1.00 56.57  ? 246 LEU   B CD1    1 
ATOM   5290  C  CD2    . LEU   B 2  246 ? 17.026  -71.045  -42.961  1.00 64.94  ? 246 LEU   B CD2    1 
ATOM   5291  N  N      . ASN   B 2  247 ? 16.637  -74.114  -39.938  1.00 67.93  ? 247 ASN   B N      1 
ATOM   5292  C  CA     . ASN   B 2  247 ? 17.621  -74.424  -38.897  1.00 73.28  ? 247 ASN   B CA     1 
ATOM   5293  C  C      . ASN   B 2  247 ? 18.757  -73.395  -38.915  1.00 72.07  ? 247 ASN   B C      1 
ATOM   5294  O  O      . ASN   B 2  247 ? 19.899  -73.684  -39.295  1.00 71.47  ? 247 ASN   B O      1 
ATOM   5295  C  CB     . ASN   B 2  247 ? 18.174  -75.847  -39.062  1.00 74.73  ? 247 ASN   B CB     1 
ATOM   5296  C  CG     . ASN   B 2  247 ? 17.305  -76.908  -38.376  1.00 76.78  ? 247 ASN   B CG     1 
ATOM   5297  O  OD1    . ASN   B 2  247 ? 16.077  -76.898  -38.492  1.00 79.08  ? 247 ASN   B OD1    1 
ATOM   5298  N  ND2    . ASN   B 2  247 ? 17.946  -77.827  -37.659  1.00 72.55  ? 247 ASN   B ND2    1 
ATOM   5299  N  N      . ALA   B 2  248 ? 18.405  -72.175  -38.499  1.00 62.12  ? 248 ALA   B N      1 
ATOM   5300  C  CA     . ALA   B 2  248 ? 19.297  -71.039  -38.677  1.00 58.83  ? 248 ALA   B CA     1 
ATOM   5301  C  C      . ALA   B 2  248 ? 20.176  -70.824  -37.447  1.00 51.94  ? 248 ALA   B C      1 
ATOM   5302  O  O      . ALA   B 2  248 ? 19.987  -71.431  -36.389  1.00 42.92  ? 248 ALA   B O      1 
ATOM   5303  C  CB     . ALA   B 2  248 ? 18.507  -69.768  -38.995  1.00 50.57  ? 248 ALA   B CB     1 
ATOM   5304  N  N      . ASP   B 2  249 ? 21.164  -69.947  -37.619  1.00 49.20  ? 249 ASP   B N      1 
ATOM   5305  C  CA     . ASP   B 2  249 ? 22.055  -69.515  -36.555  1.00 46.52  ? 249 ASP   B CA     1 
ATOM   5306  C  C      . ASP   B 2  249 ? 22.303  -68.020  -36.710  1.00 43.11  ? 249 ASP   B C      1 
ATOM   5307  O  O      . ASP   B 2  249 ? 21.993  -67.417  -37.741  1.00 41.87  ? 249 ASP   B O      1 
ATOM   5308  C  CB     . ASP   B 2  249 ? 23.389  -70.273  -36.581  1.00 46.47  ? 249 ASP   B CB     1 
ATOM   5309  C  CG     . ASP   B 2  249 ? 24.122  -70.095  -37.896  1.00 48.10  ? 249 ASP   B CG     1 
ATOM   5310  O  OD1    . ASP   B 2  249 ? 24.694  -68.994  -38.113  1.00 44.28  ? 249 ASP   B OD1    1 
ATOM   5311  O  OD2    . ASP   B 2  249 ? 24.143  -71.063  -38.694  1.00 51.26  ? 249 ASP   B OD2    1 
ATOM   5312  N  N      . LEU   B 2  250 ? 22.913  -67.426  -35.683  1.00 40.34  ? 250 LEU   B N      1 
ATOM   5313  C  CA     . LEU   B 2  250 ? 23.064  -65.976  -35.670  1.00 39.84  ? 250 LEU   B CA     1 
ATOM   5314  C  C      . LEU   B 2  250 ? 23.878  -65.484  -36.865  1.00 39.12  ? 250 LEU   B C      1 
ATOM   5315  O  O      . LEU   B 2  250 ? 23.569  -64.432  -37.434  1.00 39.30  ? 250 LEU   B O      1 
ATOM   5316  C  CB     . LEU   B 2  250 ? 23.678  -65.529  -34.344  1.00 34.73  ? 250 LEU   B CB     1 
ATOM   5317  C  CG     . LEU   B 2  250 ? 22.799  -65.863  -33.132  1.00 37.91  ? 250 LEU   B CG     1 
ATOM   5318  C  CD1    . LEU   B 2  250 ? 23.518  -65.605  -31.804  1.00 40.40  ? 250 LEU   B CD1    1 
ATOM   5319  C  CD2    . LEU   B 2  250 ? 21.494  -65.075  -33.202  1.00 36.71  ? 250 LEU   B CD2    1 
ATOM   5320  N  N      . ARG   B 2  251 ? 24.898  -66.243  -37.285  1.00 41.72  ? 251 ARG   B N      1 
ATOM   5321  C  CA     . ARG   B 2  251 ? 25.791  -65.763  -38.344  1.00 44.11  ? 251 ARG   B CA     1 
ATOM   5322  C  C      . ARG   B 2  251 ? 25.086  -65.746  -39.696  1.00 40.04  ? 251 ARG   B C      1 
ATOM   5323  O  O      . ARG   B 2  251 ? 25.087  -64.723  -40.393  1.00 39.24  ? 251 ARG   B O      1 
ATOM   5324  C  CB     . ARG   B 2  251 ? 27.074  -66.613  -38.398  1.00 42.75  ? 251 ARG   B CB     1 
ATOM   5325  C  CG     . ARG   B 2  251 ? 28.168  -66.035  -39.292  1.00 36.57  ? 251 ARG   B CG     1 
ATOM   5326  C  CD     . ARG   B 2  251 ? 29.516  -66.774  -39.163  1.00 42.16  ? 251 ARG   B CD     1 
ATOM   5327  N  NE     . ARG   B 2  251 ? 30.451  -65.939  -38.421  1.00 40.88  ? 251 ARG   B NE     1 
ATOM   5328  C  CZ     . ARG   B 2  251 ? 30.642  -66.017  -37.112  1.00 46.75  ? 251 ARG   B CZ     1 
ATOM   5329  N  NH1    . ARG   B 2  251 ? 30.263  -67.085  -36.423  1.00 47.43  ? 251 ARG   B NH1    1 
ATOM   5330  N  NH2    . ARG   B 2  251 ? 31.210  -64.992  -36.473  1.00 43.99  ? 251 ARG   B NH2    1 
ATOM   5331  N  N      . LYS   B 2  252 ? 24.478  -66.869  -40.093  1.00 39.81  ? 252 LYS   B N      1 
ATOM   5332  C  CA     . LYS   B 2  252 ? 23.734  -66.863  -41.350  1.00 39.14  ? 252 LYS   B CA     1 
ATOM   5333  C  C      . LYS   B 2  252 ? 22.689  -65.773  -41.324  1.00 36.33  ? 252 LYS   B C      1 
ATOM   5334  O  O      . LYS   B 2  252 ? 22.510  -65.055  -42.315  1.00 42.62  ? 252 LYS   B O      1 
ATOM   5335  C  CB     . LYS   B 2  252 ? 23.092  -68.225  -41.629  1.00 39.92  ? 252 LYS   B CB     1 
ATOM   5336  C  CG     . LYS   B 2  252 ? 23.903  -69.079  -42.574  1.00 37.00  ? 252 LYS   B CG     1 
ATOM   5337  C  CD     . LYS   B 2  252 ? 23.917  -70.527  -42.128  1.00 43.73  ? 252 LYS   B CD     1 
ATOM   5338  C  CE     . LYS   B 2  252 ? 24.257  -71.491  -43.279  1.00 43.11  ? 252 LYS   B CE     1 
ATOM   5339  N  NZ     . LYS   B 2  252 ? 23.971  -72.894  -42.839  1.00 52.67  ? 252 LYS   B NZ     1 
ATOM   5340  N  N      . LEU   B 2  253 ? 22.022  -65.601  -40.177  1.00 36.62  ? 253 LEU   B N      1 
ATOM   5341  C  CA     . LEU   B 2  253 ? 21.067  -64.512  -40.032  1.00 34.52  ? 253 LEU   B CA     1 
ATOM   5342  C  C      . LEU   B 2  253 ? 21.717  -63.169  -40.350  1.00 34.22  ? 253 LEU   B C      1 
ATOM   5343  O  O      . LEU   B 2  253 ? 21.176  -62.379  -41.134  1.00 34.02  ? 253 LEU   B O      1 
ATOM   5344  C  CB     . LEU   B 2  253 ? 20.472  -64.529  -38.629  1.00 36.37  ? 253 LEU   B CB     1 
ATOM   5345  C  CG     . LEU   B 2  253 ? 19.676  -63.267  -38.260  1.00 37.14  ? 253 LEU   B CG     1 
ATOM   5346  C  CD1    . LEU   B 2  253 ? 18.379  -63.167  -39.021  1.00 28.57  ? 253 LEU   B CD1    1 
ATOM   5347  C  CD2    . LEU   B 2  253 ? 19.460  -63.172  -36.753  1.00 28.10  ? 253 LEU   B CD2    1 
ATOM   5348  N  N      . ALA   B 2  254 ? 22.905  -62.909  -39.787  1.00 35.49  ? 254 ALA   B N      1 
ATOM   5349  C  CA     . ALA   B 2  254 ? 23.584  -61.631  -40.027  1.00 37.11  ? 254 ALA   B CA     1 
ATOM   5350  C  C      . ALA   B 2  254 ? 24.038  -61.492  -41.476  1.00 38.08  ? 254 ALA   B C      1 
ATOM   5351  O  O      . ALA   B 2  254 ? 23.913  -60.409  -42.063  1.00 39.35  ? 254 ALA   B O      1 
ATOM   5352  C  CB     . ALA   B 2  254 ? 24.787  -61.466  -39.089  1.00 36.00  ? 254 ALA   B CB     1 
ATOM   5353  N  N      . VAL   B 2  255 ? 24.578  -62.564  -42.068  1.00 36.48  ? 255 VAL   B N      1 
ATOM   5354  C  CA     . VAL   B 2  255 ? 25.026  -62.494  -43.462  1.00 38.00  ? 255 VAL   B CA     1 
ATOM   5355  C  C      . VAL   B 2  255 ? 23.883  -62.056  -44.371  1.00 35.05  ? 255 VAL   B C      1 
ATOM   5356  O  O      . VAL   B 2  255 ? 24.029  -61.149  -45.196  1.00 32.25  ? 255 VAL   B O      1 
ATOM   5357  C  CB     . VAL   B 2  255 ? 25.606  -63.845  -43.922  1.00 38.56  ? 255 VAL   B CB     1 
ATOM   5358  C  CG1    . VAL   B 2  255 ? 25.868  -63.792  -45.411  1.00 34.53  ? 255 VAL   B CG1    1 
ATOM   5359  C  CG2    . VAL   B 2  255 ? 26.892  -64.180  -43.181  1.00 33.05  ? 255 VAL   B CG2    1 
ATOM   5360  N  N      . ASN   B 2  256 ? 22.717  -62.679  -44.223  1.00 36.79  ? 256 ASN   B N      1 
ATOM   5361  C  CA     . ASN   B 2  256 ? 21.653  -62.441  -45.188  1.00 36.92  ? 256 ASN   B CA     1 
ATOM   5362  C  C      . ASN   B 2  256 ? 20.842  -61.188  -44.905  1.00 39.19  ? 256 ASN   B C      1 
ATOM   5363  O  O      . ASN   B 2  256 ? 20.248  -60.631  -45.837  1.00 38.42  ? 256 ASN   B O      1 
ATOM   5364  C  CB     . ASN   B 2  256 ? 20.743  -63.655  -45.245  1.00 37.83  ? 256 ASN   B CB     1 
ATOM   5365  C  CG     . ASN   B 2  256 ? 21.439  -64.857  -45.852  1.00 40.06  ? 256 ASN   B CG     1 
ATOM   5366  O  OD1    . ASN   B 2  256 ? 21.498  -64.988  -47.072  1.00 41.22  ? 256 ASN   B OD1    1 
ATOM   5367  N  ND2    . ASN   B 2  256 ? 22.005  -65.714  -45.008  1.00 35.85  ? 256 ASN   B ND2    1 
ATOM   5368  N  N      . MET   B 2  257 ? 20.818  -60.713  -43.656  1.00 39.23  ? 257 MET   B N      1 
ATOM   5369  C  CA     . MET   B 2  257 ? 20.020  -59.542  -43.322  1.00 31.54  ? 257 MET   B CA     1 
ATOM   5370  C  C      . MET   B 2  257 ? 20.777  -58.224  -43.476  1.00 36.77  ? 257 MET   B C      1 
ATOM   5371  O  O      . MET   B 2  257 ? 20.149  -57.204  -43.791  1.00 38.95  ? 257 MET   B O      1 
ATOM   5372  C  CB     . MET   B 2  257 ? 19.483  -59.680  -41.904  1.00 29.46  ? 257 MET   B CB     1 
ATOM   5373  C  CG     . MET   B 2  257 ? 18.344  -60.704  -41.777  1.00 35.07  ? 257 MET   B CG     1 
ATOM   5374  S  SD     . MET   B 2  257 ? 16.824  -60.227  -42.669  1.00 40.88  ? 257 MET   B SD     1 
ATOM   5375  C  CE     . MET   B 2  257 ? 16.297  -58.777  -41.752  1.00 35.20  ? 257 MET   B CE     1 
ATOM   5376  N  N      . VAL   B 2  258 ? 22.106  -58.223  -43.332  1.00 39.24  ? 258 VAL   B N      1 
ATOM   5377  C  CA     . VAL   B 2  258 ? 22.895  -56.994  -43.221  1.00 33.51  ? 258 VAL   B CA     1 
ATOM   5378  C  C      . VAL   B 2  258 ? 23.760  -56.716  -44.454  1.00 39.90  ? 258 VAL   B C      1 
ATOM   5379  O  O      . VAL   B 2  258 ? 24.922  -57.147  -44.501  1.00 37.36  ? 258 VAL   B O      1 
ATOM   5380  C  CB     . VAL   B 2  258 ? 23.749  -57.062  -41.954  1.00 31.39  ? 258 VAL   B CB     1 
ATOM   5381  C  CG1    . VAL   B 2  258 ? 24.426  -55.713  -41.681  1.00 34.80  ? 258 VAL   B CG1    1 
ATOM   5382  C  CG2    . VAL   B 2  258 ? 22.882  -57.474  -40.813  1.00 29.47  ? 258 VAL   B CG2    1 
ATOM   5383  N  N      . PRO   B 2  259 ? 23.256  -55.996  -45.467  1.00 37.20  ? 259 PRO   B N      1 
ATOM   5384  C  CA     . PRO   B 2  259 ? 24.088  -55.706  -46.651  1.00 34.09  ? 259 PRO   B CA     1 
ATOM   5385  C  C      . PRO   B 2  259 ? 25.228  -54.739  -46.384  1.00 37.88  ? 259 PRO   B C      1 
ATOM   5386  O  O      . PRO   B 2  259 ? 26.209  -54.720  -47.143  1.00 38.00  ? 259 PRO   B O      1 
ATOM   5387  C  CB     . PRO   B 2  259 ? 23.089  -55.099  -47.647  1.00 33.10  ? 259 PRO   B CB     1 
ATOM   5388  C  CG     . PRO   B 2  259 ? 21.987  -54.593  -46.808  1.00 36.17  ? 259 PRO   B CG     1 
ATOM   5389  C  CD     . PRO   B 2  259 ? 21.866  -55.551  -45.646  1.00 35.08  ? 259 PRO   B CD     1 
ATOM   5390  N  N      . PHE   B 2  260 ? 25.113  -53.905  -45.359  1.00 40.15  ? 260 PHE   B N      1 
ATOM   5391  C  CA     . PHE   B 2  260 ? 26.108  -52.896  -45.037  1.00 38.48  ? 260 PHE   B CA     1 
ATOM   5392  C  C      . PHE   B 2  260 ? 26.277  -52.917  -43.524  1.00 40.44  ? 260 PHE   B C      1 
ATOM   5393  O  O      . PHE   B 2  260 ? 25.283  -52.953  -42.777  1.00 41.36  ? 260 PHE   B O      1 
ATOM   5394  C  CB     . PHE   B 2  260 ? 25.687  -51.507  -45.538  1.00 34.07  ? 260 PHE   B CB     1 
ATOM   5395  C  CG     . PHE   B 2  260 ? 25.406  -51.480  -47.001  1.00 41.48  ? 260 PHE   B CG     1 
ATOM   5396  C  CD1    . PHE   B 2  260 ? 26.438  -51.616  -47.912  1.00 40.38  ? 260 PHE   B CD1    1 
ATOM   5397  C  CD2    . PHE   B 2  260 ? 24.102  -51.388  -47.478  1.00 47.87  ? 260 PHE   B CD2    1 
ATOM   5398  C  CE1    . PHE   B 2  260 ? 26.194  -51.614  -49.272  1.00 38.61  ? 260 PHE   B CE1    1 
ATOM   5399  C  CE2    . PHE   B 2  260 ? 23.833  -51.390  -48.849  1.00 43.82  ? 260 PHE   B CE2    1 
ATOM   5400  C  CZ     . PHE   B 2  260 ? 24.885  -51.501  -49.745  1.00 45.65  ? 260 PHE   B CZ     1 
ATOM   5401  N  N      . PRO   B 2  261 ? 27.510  -52.909  -43.040  1.00 36.03  ? 261 PRO   B N      1 
ATOM   5402  C  CA     . PRO   B 2  261 ? 27.720  -53.341  -41.653  1.00 36.01  ? 261 PRO   B CA     1 
ATOM   5403  C  C      . PRO   B 2  261 ? 26.987  -52.487  -40.634  1.00 33.63  ? 261 PRO   B C      1 
ATOM   5404  O  O      . PRO   B 2  261 ? 26.470  -53.032  -39.654  1.00 35.75  ? 261 PRO   B O      1 
ATOM   5405  C  CB     . PRO   B 2  261 ? 29.245  -53.278  -41.501  1.00 32.30  ? 261 PRO   B CB     1 
ATOM   5406  C  CG     . PRO   B 2  261 ? 29.768  -52.733  -42.825  1.00 30.02  ? 261 PRO   B CG     1 
ATOM   5407  C  CD     . PRO   B 2  261 ? 28.664  -52.187  -43.587  1.00 33.57  ? 261 PRO   B CD     1 
ATOM   5408  N  N      . ARG   B 2  262 ? 26.910  -51.172  -40.827  1.00 34.36  ? 262 ARG   B N      1 
ATOM   5409  C  CA     . ARG   B 2  262 ? 26.266  -50.332  -39.819  1.00 37.07  ? 262 ARG   B CA     1 
ATOM   5410  C  C      . ARG   B 2  262 ? 24.750  -50.417  -39.852  1.00 36.47  ? 262 ARG   B C      1 
ATOM   5411  O  O      . ARG   B 2  262 ? 24.107  -50.063  -38.862  1.00 38.18  ? 262 ARG   B O      1 
ATOM   5412  C  CB     . ARG   B 2  262 ? 26.644  -48.848  -39.985  1.00 43.57  ? 262 ARG   B CB     1 
ATOM   5413  C  CG     . ARG   B 2  262 ? 28.122  -48.521  -39.946  1.00 34.42  ? 262 ARG   B CG     1 
ATOM   5414  C  CD     . ARG   B 2  262 ? 28.372  -47.130  -40.456  1.00 30.55  ? 262 ARG   B CD     1 
ATOM   5415  N  NE     . ARG   B 2  262 ? 28.389  -46.183  -39.349  1.00 51.04  ? 262 ARG   B NE     1 
ATOM   5416  C  CZ     . ARG   B 2  262 ? 27.861  -44.964  -39.382  1.00 51.30  ? 262 ARG   B CZ     1 
ATOM   5417  N  NH1    . ARG   B 2  262 ? 27.237  -44.504  -40.462  1.00 49.33  ? 262 ARG   B NH1    1 
ATOM   5418  N  NH2    . ARG   B 2  262 ? 27.976  -44.182  -38.314  1.00 50.33  ? 262 ARG   B NH2    1 
ATOM   5419  N  N      . LEU   B 2  263 ? 24.158  -50.841  -40.968  1.00 39.81  ? 263 LEU   B N      1 
ATOM   5420  C  CA     . LEU   B 2  263 ? 22.701  -50.904  -41.086  1.00 35.39  ? 263 LEU   B CA     1 
ATOM   5421  C  C      . LEU   B 2  263 ? 22.193  -52.276  -40.635  1.00 34.50  ? 263 LEU   B C      1 
ATOM   5422  O  O      . LEU   B 2  263 ? 21.696  -53.078  -41.417  1.00 33.82  ? 263 LEU   B O      1 
ATOM   5423  C  CB     . LEU   B 2  263 ? 22.283  -50.601  -42.513  1.00 35.44  ? 263 LEU   B CB     1 
ATOM   5424  C  CG     . LEU   B 2  263 ? 22.902  -49.374  -43.156  1.00 42.60  ? 263 LEU   B CG     1 
ATOM   5425  C  CD1    . LEU   B 2  263 ? 22.260  -49.140  -44.495  1.00 43.57  ? 263 LEU   B CD1    1 
ATOM   5426  C  CD2    . LEU   B 2  263 ? 22.679  -48.188  -42.272  1.00 45.27  ? 263 LEU   B CD2    1 
ATOM   5427  N  N      . HIS   B 2  264 ? 22.306  -52.535  -39.332  1.00 33.81  ? 264 HIS   B N      1 
ATOM   5428  C  CA     . HIS   B 2  264 ? 21.915  -53.819  -38.769  1.00 31.07  ? 264 HIS   B CA     1 
ATOM   5429  C  C      . HIS   B 2  264 ? 20.853  -53.641  -37.678  1.00 36.61  ? 264 HIS   B C      1 
ATOM   5430  O  O      . HIS   B 2  264 ? 20.786  -54.400  -36.694  1.00 35.74  ? 264 HIS   B O      1 
ATOM   5431  C  CB     . HIS   B 2  264 ? 23.148  -54.554  -38.253  1.00 32.06  ? 264 HIS   B CB     1 
ATOM   5432  C  CG     . HIS   B 2  264 ? 23.942  -53.755  -37.258  1.00 42.28  ? 264 HIS   B CG     1 
ATOM   5433  N  ND1    . HIS   B 2  264 ? 24.887  -52.821  -37.630  1.00 39.70  ? 264 HIS   B ND1    1 
ATOM   5434  C  CD2    . HIS   B 2  264 ? 23.907  -53.733  -35.901  1.00 35.78  ? 264 HIS   B CD2    1 
ATOM   5435  C  CE1    . HIS   B 2  264 ? 25.406  -52.270  -36.546  1.00 37.40  ? 264 HIS   B CE1    1 
ATOM   5436  N  NE2    . HIS   B 2  264 ? 24.826  -52.804  -35.487  1.00 34.15  ? 264 HIS   B NE2    1 
ATOM   5437  N  N      . PHE   B 2  265 ? 19.985  -52.647  -37.853  1.00 40.89  ? 265 PHE   B N      1 
ATOM   5438  C  CA     . PHE   B 2  265 ? 18.932  -52.351  -36.886  1.00 39.12  ? 265 PHE   B CA     1 
ATOM   5439  C  C      . PHE   B 2  265 ? 17.605  -52.787  -37.478  1.00 34.22  ? 265 PHE   B C      1 
ATOM   5440  O  O      . PHE   B 2  265 ? 17.089  -52.145  -38.399  1.00 44.00  ? 265 PHE   B O      1 
ATOM   5441  C  CB     . PHE   B 2  265 ? 18.941  -50.872  -36.520  1.00 35.76  ? 265 PHE   B CB     1 
ATOM   5442  C  CG     . PHE   B 2  265 ? 20.169  -50.475  -35.769  1.00 36.93  ? 265 PHE   B CG     1 
ATOM   5443  C  CD1    . PHE   B 2  265 ? 20.216  -50.581  -34.393  1.00 34.71  ? 265 PHE   B CD1    1 
ATOM   5444  C  CD2    . PHE   B 2  265 ? 21.300  -50.041  -36.442  1.00 38.15  ? 265 PHE   B CD2    1 
ATOM   5445  C  CE1    . PHE   B 2  265 ? 21.349  -50.238  -33.688  1.00 29.21  ? 265 PHE   B CE1    1 
ATOM   5446  C  CE2    . PHE   B 2  265 ? 22.441  -49.712  -35.741  1.00 39.02  ? 265 PHE   B CE2    1 
ATOM   5447  C  CZ     . PHE   B 2  265 ? 22.458  -49.810  -34.362  1.00 34.61  ? 265 PHE   B CZ     1 
ATOM   5448  N  N      . PHE   B 2  266 ? 17.056  -53.866  -36.938  1.00 28.95  ? 266 PHE   B N      1 
ATOM   5449  C  CA     . PHE   B 2  266 ? 15.858  -54.502  -37.465  1.00 34.24  ? 266 PHE   B CA     1 
ATOM   5450  C  C      . PHE   B 2  266 ? 14.594  -54.018  -36.758  1.00 38.44  ? 266 PHE   B C      1 
ATOM   5451  O  O      . PHE   B 2  266 ? 14.587  -53.853  -35.532  1.00 37.43  ? 266 PHE   B O      1 
ATOM   5452  C  CB     . PHE   B 2  266 ? 15.962  -56.015  -37.311  1.00 34.76  ? 266 PHE   B CB     1 
ATOM   5453  C  CG     . PHE   B 2  266 ? 17.191  -56.604  -37.946  1.00 38.15  ? 266 PHE   B CG     1 
ATOM   5454  C  CD1    . PHE   B 2  266 ? 17.795  -55.985  -39.041  1.00 36.40  ? 266 PHE   B CD1    1 
ATOM   5455  C  CD2    . PHE   B 2  266 ? 17.739  -57.780  -37.463  1.00 32.86  ? 266 PHE   B CD2    1 
ATOM   5456  C  CE1    . PHE   B 2  266 ? 18.916  -56.539  -39.638  1.00 33.33  ? 266 PHE   B CE1    1 
ATOM   5457  C  CE2    . PHE   B 2  266 ? 18.862  -58.317  -38.045  1.00 27.57  ? 266 PHE   B CE2    1 
ATOM   5458  C  CZ     . PHE   B 2  266 ? 19.440  -57.711  -39.127  1.00 28.49  ? 266 PHE   B CZ     1 
ATOM   5459  N  N      . MET   B 2  267 ? 13.509  -53.803  -37.555  1.00 36.88  ? 267 MET   B N      1 
ATOM   5460  C  CA     . MET   B 2  267 ? 12.135  -53.600  -37.093  1.00 34.46  ? 267 MET   B CA     1 
ATOM   5461  C  C      . MET   B 2  267 ? 11.459  -54.941  -36.879  1.00 35.75  ? 267 MET   B C      1 
ATOM   5462  O  O      . MET   B 2  267 ? 11.150  -55.618  -37.858  1.00 38.98  ? 267 MET   B O      1 
ATOM   5463  C  CB     . MET   B 2  267 ? 11.256  -52.846  -38.092  1.00 35.62  ? 267 MET   B CB     1 
ATOM   5464  C  CG     . MET   B 2  267 ? 11.719  -51.491  -38.564  1.00 48.26  ? 267 MET   B CG     1 
ATOM   5465  S  SD     . MET   B 2  267 ? 10.275  -50.652  -39.265  1.00 58.84  ? 267 MET   B SD     1 
ATOM   5466  C  CE     . MET   B 2  267 ? 9.118   -52.001  -39.239  1.00 42.32  ? 267 MET   B CE     1 
ATOM   5467  N  N      . PRO   B 2  268 ? 11.173  -55.351  -35.656  1.00 34.12  ? 268 PRO   B N      1 
ATOM   5468  C  CA     . PRO   B 2  268 ? 10.360  -56.553  -35.460  1.00 36.62  ? 268 PRO   B CA     1 
ATOM   5469  C  C      . PRO   B 2  268 ? 8.876   -56.241  -35.606  1.00 41.74  ? 268 PRO   B C      1 
ATOM   5470  O  O      . PRO   B 2  268 ? 8.426   -55.103  -35.459  1.00 41.03  ? 268 PRO   B O      1 
ATOM   5471  C  CB     . PRO   B 2  268 ? 10.689  -56.981  -34.024  1.00 37.27  ? 268 PRO   B CB     1 
ATOM   5472  C  CG     . PRO   B 2  268 ? 11.627  -55.888  -33.482  1.00 37.71  ? 268 PRO   B CG     1 
ATOM   5473  C  CD     . PRO   B 2  268 ? 11.529  -54.721  -34.379  1.00 33.42  ? 268 PRO   B CD     1 
ATOM   5474  N  N      . GLY   B 2  269 ? 8.115   -57.285  -35.880  1.00 45.34  ? 269 GLY   B N      1 
ATOM   5475  C  CA     . GLY   B 2  269 ? 6.671   -57.164  -36.011  1.00 47.86  ? 269 GLY   B CA     1 
ATOM   5476  C  C      . GLY   B 2  269 ? 6.019   -58.482  -35.665  1.00 46.01  ? 269 GLY   B C      1 
ATOM   5477  O  O      . GLY   B 2  269 ? 6.614   -59.553  -35.826  1.00 46.09  ? 269 GLY   B O      1 
ATOM   5478  N  N      . PHE   B 2  270 ? 4.795   -58.410  -35.177  1.00 43.97  ? 270 PHE   B N      1 
ATOM   5479  C  CA     . PHE   B 2  270 ? 4.154   -59.626  -34.709  1.00 50.94  ? 270 PHE   B CA     1 
ATOM   5480  C  C      . PHE   B 2  270 ? 2.689   -59.613  -35.112  1.00 54.21  ? 270 PHE   B C      1 
ATOM   5481  O  O      . PHE   B 2  270 ? 2.086   -58.544  -35.267  1.00 54.94  ? 270 PHE   B O      1 
ATOM   5482  C  CB     . PHE   B 2  270 ? 4.310   -59.764  -33.203  1.00 43.37  ? 270 PHE   B CB     1 
ATOM   5483  C  CG     . PHE   B 2  270 ? 3.853   -61.071  -32.675  1.00 52.05  ? 270 PHE   B CG     1 
ATOM   5484  C  CD1    . PHE   B 2  270 ? 4.673   -62.195  -32.759  1.00 52.30  ? 270 PHE   B CD1    1 
ATOM   5485  C  CD2    . PHE   B 2  270 ? 2.602   -61.197  -32.082  1.00 49.03  ? 270 PHE   B CD2    1 
ATOM   5486  C  CE1    . PHE   B 2  270 ? 4.244   -63.438  -32.250  1.00 53.09  ? 270 PHE   B CE1    1 
ATOM   5487  C  CE2    . PHE   B 2  270 ? 2.166   -62.434  -31.576  1.00 49.96  ? 270 PHE   B CE2    1 
ATOM   5488  C  CZ     . PHE   B 2  270 ? 2.986   -63.553  -31.658  1.00 47.99  ? 270 PHE   B CZ     1 
ATOM   5489  N  N      . ALA   B 2  271 ? 2.130   -60.812  -35.318  1.00 48.54  ? 271 ALA   B N      1 
ATOM   5490  C  CA     . ALA   B 2  271 ? 0.705   -60.966  -35.649  1.00 52.26  ? 271 ALA   B CA     1 
ATOM   5491  C  C      . ALA   B 2  271 ? 0.246   -62.348  -35.214  1.00 51.71  ? 271 ALA   B C      1 
ATOM   5492  O  O      . ALA   B 2  271 ? 0.970   -63.326  -35.435  1.00 49.37  ? 271 ALA   B O      1 
ATOM   5493  C  CB     . ALA   B 2  271 ? 0.425   -60.777  -37.144  1.00 52.35  ? 271 ALA   B CB     1 
ATOM   5494  N  N      . PRO   B 2  272 ? -0.924  -62.468  -34.580  1.00 57.20  ? 272 PRO   B N      1 
ATOM   5495  C  CA     . PRO   B 2  272 ? -1.892  -61.423  -34.234  1.00 52.27  ? 272 PRO   B CA     1 
ATOM   5496  C  C      . PRO   B 2  272 ? -1.496  -60.670  -32.982  1.00 53.73  ? 272 PRO   B C      1 
ATOM   5497  O  O      . PRO   B 2  272 ? -1.019  -61.314  -32.052  1.00 55.69  ? 272 PRO   B O      1 
ATOM   5498  C  CB     . PRO   B 2  272 ? -3.161  -62.232  -33.998  1.00 49.35  ? 272 PRO   B CB     1 
ATOM   5499  C  CG     . PRO   B 2  272 ? -2.641  -63.484  -33.349  1.00 46.35  ? 272 PRO   B CG     1 
ATOM   5500  C  CD     . PRO   B 2  272 ? -1.336  -63.777  -34.040  1.00 52.16  ? 272 PRO   B CD     1 
ATOM   5501  N  N      . LEU   B 2  273 ? -1.681  -59.351  -32.896  1.00 57.56  ? 273 LEU   B N      1 
ATOM   5502  C  CA     . LEU   B 2  273 ? -1.475  -58.654  -31.627  1.00 55.63  ? 273 LEU   B CA     1 
ATOM   5503  C  C      . LEU   B 2  273 ? -2.533  -59.092  -30.623  1.00 66.87  ? 273 LEU   B C      1 
ATOM   5504  O  O      . LEU   B 2  273 ? -3.737  -59.014  -30.899  1.00 70.27  ? 273 LEU   B O      1 
ATOM   5505  C  CB     . LEU   B 2  273 ? -1.537  -57.144  -31.808  1.00 46.21  ? 273 LEU   B CB     1 
ATOM   5506  C  CG     . LEU   B 2  273 ? -0.515  -56.600  -32.797  1.00 54.37  ? 273 LEU   B CG     1 
ATOM   5507  C  CD1    . LEU   B 2  273 ? -0.855  -55.161  -33.249  1.00 49.41  ? 273 LEU   B CD1    1 
ATOM   5508  C  CD2    . LEU   B 2  273 ? 0.895   -56.715  -32.202  1.00 49.38  ? 273 LEU   B CD2    1 
ATOM   5509  N  N      . THR   B 2  274 ? -2.075  -59.554  -29.458  1.00 68.44  ? 274 THR   B N      1 
ATOM   5510  C  CA     . THR   B 2  274 ? -2.935  -60.042  -28.390  1.00 66.06  ? 274 THR   B CA     1 
ATOM   5511  C  C      . THR   B 2  274 ? -2.600  -59.308  -27.101  1.00 69.78  ? 274 THR   B C      1 
ATOM   5512  O  O      . THR   B 2  274 ? -1.495  -58.784  -26.937  1.00 63.70  ? 274 THR   B O      1 
ATOM   5513  C  CB     . THR   B 2  274 ? -2.767  -61.553  -28.183  1.00 70.02  ? 274 THR   B CB     1 
ATOM   5514  O  OG1    . THR   B 2  274 ? -1.623  -61.806  -27.353  1.00 62.42  ? 274 THR   B OG1    1 
ATOM   5515  C  CG2    . THR   B 2  274 ? -2.578  -62.256  -29.545  1.00 65.40  ? 274 THR   B CG2    1 
ATOM   5516  N  N      . SER   B 2  275 ? -3.570  -59.268  -26.187  1.00 78.00  ? 275 SER   B N      1 
ATOM   5517  C  CA     . SER   B 2  275 ? -3.391  -58.680  -24.866  1.00 71.67  ? 275 SER   B CA     1 
ATOM   5518  C  C      . SER   B 2  275 ? -3.501  -59.776  -23.818  1.00 73.43  ? 275 SER   B C      1 
ATOM   5519  O  O      . SER   B 2  275 ? -4.343  -60.673  -23.941  1.00 79.41  ? 275 SER   B O      1 
ATOM   5520  C  CB     . SER   B 2  275 ? -4.418  -57.577  -24.607  1.00 65.77  ? 275 SER   B CB     1 
ATOM   5521  O  OG     . SER   B 2  275 ? -5.727  -58.061  -24.811  1.00 77.87  ? 275 SER   B OG     1 
ATOM   5522  N  N      . ARG   B 2  276 ? -2.643  -59.695  -22.792  1.00 73.42  ? 276 ARG   B N      1 
ATOM   5523  C  CA     . ARG   B 2  276 ? -2.483  -60.769  -21.813  1.00 74.13  ? 276 ARG   B CA     1 
ATOM   5524  C  C      . ARG   B 2  276 ? -3.827  -61.271  -21.307  1.00 81.16  ? 276 ARG   B C      1 
ATOM   5525  O  O      . ARG   B 2  276 ? -4.797  -60.515  -21.196  1.00 86.04  ? 276 ARG   B O      1 
ATOM   5526  C  CB     . ARG   B 2  276 ? -1.663  -60.301  -20.610  1.00 69.04  ? 276 ARG   B CB     1 
ATOM   5527  C  CG     . ARG   B 2  276 ? -0.822  -59.091  -20.859  1.00 68.64  ? 276 ARG   B CG     1 
ATOM   5528  C  CD     . ARG   B 2  276 ? 0.406   -59.120  -19.970  1.00 66.95  ? 276 ARG   B CD     1 
ATOM   5529  N  NE     . ARG   B 2  276 ? 0.122   -59.108  -18.540  1.00 65.99  ? 276 ARG   B NE     1 
ATOM   5530  C  CZ     . ARG   B 2  276 ? -0.006  -58.000  -17.816  1.00 67.89  ? 276 ARG   B CZ     1 
ATOM   5531  N  NH1    . ARG   B 2  276 ? -0.059  -56.801  -18.385  1.00 54.17  ? 276 ARG   B NH1    1 
ATOM   5532  N  NH2    . ARG   B 2  276 ? -0.073  -58.095  -16.488  1.00 71.15  ? 276 ARG   B NH2    1 
ATOM   5533  N  N      . GLY   B 2  277 ? -3.868  -62.558  -20.974  1.00 75.32  ? 277 GLY   B N      1 
ATOM   5534  C  CA     . GLY   B 2  277 ? -5.049  -63.142  -20.372  1.00 88.44  ? 277 GLY   B CA     1 
ATOM   5535  C  C      . GLY   B 2  277 ? -6.174  -63.432  -21.346  1.00 97.33  ? 277 GLY   B C      1 
ATOM   5536  O  O      . GLY   B 2  277 ? -6.501  -64.599  -21.592  1.00 98.50  ? 277 GLY   B O      1 
ATOM   5537  N  N      . SER   B 2  278 ? -6.788  -62.388  -21.901  1.00 98.65  ? 278 SER   B N      1 
ATOM   5538  C  CA     . SER   B 2  278 ? -7.873  -62.594  -22.853  1.00 102.69 ? 278 SER   B CA     1 
ATOM   5539  C  C      . SER   B 2  278 ? -7.357  -63.335  -24.080  1.00 103.92 ? 278 SER   B C      1 
ATOM   5540  O  O      . SER   B 2  278 ? -6.468  -62.846  -24.791  1.00 98.02  ? 278 SER   B O      1 
ATOM   5541  C  CB     . SER   B 2  278 ? -8.502  -61.256  -23.246  1.00 101.84 ? 278 SER   B CB     1 
ATOM   5542  O  OG     . SER   B 2  278 ? -7.521  -60.246  -23.373  1.00 94.71  ? 278 SER   B OG     1 
ATOM   5543  N  N      . GLN   B 2  279 ? -7.896  -64.533  -24.301  1.00 107.25 ? 279 GLN   B N      1 
ATOM   5544  C  CA     . GLN   B 2  279 ? -7.629  -65.323  -25.497  1.00 106.06 ? 279 GLN   B CA     1 
ATOM   5545  C  C      . GLN   B 2  279 ? -8.828  -65.214  -26.429  1.00 99.93  ? 279 GLN   B C      1 
ATOM   5546  O  O      . GLN   B 2  279 ? -9.964  -65.460  -26.011  1.00 99.59  ? 279 GLN   B O      1 
ATOM   5547  C  CB     . GLN   B 2  279 ? -7.367  -66.792  -25.144  1.00 100.20 ? 279 GLN   B CB     1 
ATOM   5548  C  CG     . GLN   B 2  279 ? -7.329  -67.742  -26.353  1.00 98.31  ? 279 GLN   B CG     1 
ATOM   5549  C  CD     . GLN   B 2  279 ? -7.331  -69.223  -25.964  1.00 97.44  ? 279 GLN   B CD     1 
ATOM   5550  O  OE1    . GLN   B 2  279 ? -8.095  -70.019  -26.517  1.00 89.42  ? 279 GLN   B OE1    1 
ATOM   5551  N  NE2    . GLN   B 2  279 ? -6.472  -69.594  -25.011  1.00 93.59  ? 279 GLN   B NE2    1 
ATOM   5552  N  N      . GLN   B 2  280 ? -8.583  -64.816  -27.673  1.00 97.60  ? 280 GLN   B N      1 
ATOM   5553  C  CA     . GLN   B 2  280 ? -9.608  -64.917  -28.698  1.00 95.18  ? 280 GLN   B CA     1 
ATOM   5554  C  C      . GLN   B 2  280 ? -9.441  -66.242  -29.435  1.00 93.14  ? 280 GLN   B C      1 
ATOM   5555  O  O      . GLN   B 2  280 ? -8.345  -66.807  -29.504  1.00 86.98  ? 280 GLN   B O      1 
ATOM   5556  C  CB     . GLN   B 2  280 ? -9.561  -63.731  -29.661  1.00 99.70  ? 280 GLN   B CB     1 
ATOM   5557  C  CG     . GLN   B 2  280 ? -10.259 -62.461  -29.140  1.00 104.41 ? 280 GLN   B CG     1 
ATOM   5558  C  CD     . GLN   B 2  280 ? -9.604  -61.896  -27.883  1.00 109.88 ? 280 GLN   B CD     1 
ATOM   5559  O  OE1    . GLN   B 2  280 ? -8.413  -62.104  -27.641  1.00 110.13 ? 280 GLN   B OE1    1 
ATOM   5560  N  NE2    . GLN   B 2  280 ? -10.372 -61.142  -27.099  1.00 109.17 ? 280 GLN   B NE2    1 
ATOM   5561  N  N      . TYR   B 2  281 ? -10.558 -66.746  -29.966  1.00 92.56  ? 281 TYR   B N      1 
ATOM   5562  C  CA     . TYR   B 2  281 ? -10.720 -68.166  -30.251  1.00 82.98  ? 281 TYR   B CA     1 
ATOM   5563  C  C      . TYR   B 2  281 ? -10.754 -68.515  -31.734  1.00 79.08  ? 281 TYR   B C      1 
ATOM   5564  O  O      . TYR   B 2  281 ? -10.709 -69.706  -32.064  1.00 74.12  ? 281 TYR   B O      1 
ATOM   5565  C  CB     . TYR   B 2  281 ? -12.006 -68.687  -29.579  1.00 78.04  ? 281 TYR   B CB     1 
ATOM   5566  C  CG     . TYR   B 2  281 ? -12.202 -68.182  -28.159  1.00 76.79  ? 281 TYR   B CG     1 
ATOM   5567  C  CD1    . TYR   B 2  281 ? -11.510 -68.758  -27.092  1.00 77.88  ? 281 TYR   B CD1    1 
ATOM   5568  C  CD2    . TYR   B 2  281 ? -13.071 -67.134  -27.888  1.00 71.66  ? 281 TYR   B CD2    1 
ATOM   5569  C  CE1    . TYR   B 2  281 ? -11.675 -68.305  -25.797  1.00 77.85  ? 281 TYR   B CE1    1 
ATOM   5570  C  CE2    . TYR   B 2  281 ? -13.252 -66.670  -26.594  1.00 75.84  ? 281 TYR   B CE2    1 
ATOM   5571  C  CZ     . TYR   B 2  281 ? -12.548 -67.256  -25.546  1.00 85.42  ? 281 TYR   B CZ     1 
ATOM   5572  O  OH     . TYR   B 2  281 ? -12.715 -66.800  -24.244  1.00 79.83  ? 281 TYR   B OH     1 
ATOM   5573  N  N      . ARG   B 2  282 ? -10.854 -67.530  -32.631  1.00 75.35  ? 282 ARG   B N      1 
ATOM   5574  C  CA     . ARG   B 2  282 ? -10.736 -67.790  -34.062  1.00 67.08  ? 282 ARG   B CA     1 
ATOM   5575  C  C      . ARG   B 2  282 ? -9.271  -67.734  -34.449  1.00 69.24  ? 282 ARG   B C      1 
ATOM   5576  O  O      . ARG   B 2  282 ? -8.590  -66.741  -34.168  1.00 68.84  ? 282 ARG   B O      1 
ATOM   5577  C  CB     . ARG   B 2  282 ? -11.522 -66.763  -34.876  1.00 64.97  ? 282 ARG   B CB     1 
ATOM   5578  N  N      . ALA   B 2  283 ? -8.772  -68.795  -35.075  1.00 68.69  ? 283 ALA   B N      1 
ATOM   5579  C  CA     . ALA   B 2  283 ? -7.426  -68.680  -35.616  1.00 57.90  ? 283 ALA   B CA     1 
ATOM   5580  C  C      . ALA   B 2  283 ? -7.438  -67.768  -36.834  1.00 59.17  ? 283 ALA   B C      1 
ATOM   5581  O  O      . ALA   B 2  283 ? -8.479  -67.508  -37.458  1.00 55.43  ? 283 ALA   B O      1 
ATOM   5582  C  CB     . ALA   B 2  283 ? -6.843  -70.041  -35.981  1.00 52.57  ? 283 ALA   B CB     1 
ATOM   5583  N  N      . LEU   B 2  284 ? -6.264  -67.245  -37.153  1.00 64.10  ? 284 LEU   B N      1 
ATOM   5584  C  CA     . LEU   B 2  284 ? -6.194  -66.398  -38.324  1.00 61.68  ? 284 LEU   B CA     1 
ATOM   5585  C  C      . LEU   B 2  284 ? -6.067  -67.251  -39.578  1.00 61.45  ? 284 LEU   B C      1 
ATOM   5586  O  O      . LEU   B 2  284 ? -5.772  -68.451  -39.532  1.00 59.57  ? 284 LEU   B O      1 
ATOM   5587  C  CB     . LEU   B 2  284 ? -5.038  -65.414  -38.214  1.00 56.59  ? 284 LEU   B CB     1 
ATOM   5588  C  CG     . LEU   B 2  284 ? -5.461  -64.195  -37.404  1.00 56.83  ? 284 LEU   B CG     1 
ATOM   5589  C  CD1    . LEU   B 2  284 ? -5.713  -64.641  -35.966  1.00 56.12  ? 284 LEU   B CD1    1 
ATOM   5590  C  CD2    . LEU   B 2  284 ? -4.413  -63.074  -37.476  1.00 58.56  ? 284 LEU   B CD2    1 
ATOM   5591  N  N      . THR   B 2  285 ? -6.354  -66.624  -40.704  1.00 59.33  ? 285 THR   B N      1 
ATOM   5592  C  CA     . THR   B 2  285 ? -6.098  -67.221  -41.997  1.00 63.11  ? 285 THR   B CA     1 
ATOM   5593  C  C      . THR   B 2  285 ? -4.771  -66.686  -42.522  1.00 60.63  ? 285 THR   B C      1 
ATOM   5594  O  O      . THR   B 2  285 ? -4.451  -65.508  -42.337  1.00 59.60  ? 285 THR   B O      1 
ATOM   5595  C  CB     . THR   B 2  285 ? -7.252  -66.925  -42.961  1.00 65.67  ? 285 THR   B CB     1 
ATOM   5596  O  OG1    . THR   B 2  285 ? -7.348  -65.512  -43.223  1.00 58.08  ? 285 THR   B OG1    1 
ATOM   5597  C  CG2    . THR   B 2  285 ? -8.550  -67.416  -42.356  1.00 56.02  ? 285 THR   B CG2    1 
ATOM   5598  N  N      . VAL   B 2  286 ? -3.996  -67.565  -43.149  1.00 56.52  ? 286 VAL   B N      1 
ATOM   5599  C  CA     . VAL   B 2  286 ? -2.670  -67.230  -43.663  1.00 57.69  ? 286 VAL   B CA     1 
ATOM   5600  C  C      . VAL   B 2  286 ? -2.688  -65.863  -44.344  1.00 60.50  ? 286 VAL   B C      1 
ATOM   5601  O  O      . VAL   B 2  286 ? -1.740  -65.083  -44.169  1.00 64.91  ? 286 VAL   B O      1 
ATOM   5602  C  CB     . VAL   B 2  286 ? -2.148  -68.322  -44.612  1.00 63.33  ? 286 VAL   B CB     1 
ATOM   5603  C  CG1    . VAL   B 2  286 ? -0.978  -67.807  -45.430  1.00 61.71  ? 286 VAL   B CG1    1 
ATOM   5604  C  CG2    . VAL   B 2  286 ? -1.733  -69.562  -43.821  1.00 58.14  ? 286 VAL   B CG2    1 
ATOM   5605  N  N      . PRO   B 2  287 ? -3.716  -65.514  -45.116  1.00 55.89  ? 287 PRO   B N      1 
ATOM   5606  C  CA     . PRO   B 2  287 ? -3.780  -64.136  -45.632  1.00 58.37  ? 287 PRO   B CA     1 
ATOM   5607  C  C      . PRO   B 2  287 ? -3.816  -63.085  -44.542  1.00 57.94  ? 287 PRO   B C      1 
ATOM   5608  O  O      . PRO   B 2  287 ? -3.304  -61.977  -44.751  1.00 57.75  ? 287 PRO   B O      1 
ATOM   5609  C  CB     . PRO   B 2  287 ? -5.068  -64.134  -46.465  1.00 55.03  ? 287 PRO   B CB     1 
ATOM   5610  C  CG     . PRO   B 2  287 ? -5.174  -65.542  -46.939  1.00 54.58  ? 287 PRO   B CG     1 
ATOM   5611  C  CD     . PRO   B 2  287 ? -4.673  -66.397  -45.798  1.00 61.23  ? 287 PRO   B CD     1 
ATOM   5612  N  N      . GLU   B 2  288 ? -4.412  -63.395  -43.386  1.00 59.14  ? 288 GLU   B N      1 
ATOM   5613  C  CA     . GLU   B 2  288 ? -4.519  -62.414  -42.308  1.00 57.94  ? 288 GLU   B CA     1 
ATOM   5614  C  C      . GLU   B 2  288 ? -3.168  -62.180  -41.654  1.00 61.77  ? 288 GLU   B C      1 
ATOM   5615  O  O      . GLU   B 2  288 ? -2.730  -61.034  -41.492  1.00 60.32  ? 288 GLU   B O      1 
ATOM   5616  C  CB     . GLU   B 2  288 ? -5.536  -62.889  -41.268  1.00 63.93  ? 288 GLU   B CB     1 
ATOM   5617  C  CG     . GLU   B 2  288 ? -6.988  -62.576  -41.619  1.00 67.28  ? 288 GLU   B CG     1 
ATOM   5618  C  CD     . GLU   B 2  288 ? -7.994  -63.481  -40.915  1.00 67.38  ? 288 GLU   B CD     1 
ATOM   5619  O  OE1    . GLU   B 2  288 ? -7.610  -64.552  -40.375  1.00 64.69  ? 288 GLU   B OE1    1 
ATOM   5620  O  OE2    . GLU   B 2  288 ? -9.184  -63.110  -40.919  1.00 71.14  ? 288 GLU   B OE2    1 
ATOM   5621  N  N      . LEU   B 2  289 ? -2.497  -63.267  -41.262  1.00 60.75  ? 289 LEU   B N      1 
ATOM   5622  C  CA     . LEU   B 2  289 ? -1.142  -63.166  -40.749  1.00 51.31  ? 289 LEU   B CA     1 
ATOM   5623  C  C      . LEU   B 2  289 ? -0.294  -62.295  -41.656  1.00 52.83  ? 289 LEU   B C      1 
ATOM   5624  O  O      . LEU   B 2  289 ? 0.407   -61.391  -41.198  1.00 59.90  ? 289 LEU   B O      1 
ATOM   5625  C  CB     . LEU   B 2  289 ? -0.540  -64.559  -40.633  1.00 48.56  ? 289 LEU   B CB     1 
ATOM   5626  C  CG     . LEU   B 2  289 ? -1.113  -65.470  -39.563  1.00 51.21  ? 289 LEU   B CG     1 
ATOM   5627  C  CD1    . LEU   B 2  289 ? -0.401  -66.802  -39.634  1.00 50.00  ? 289 LEU   B CD1    1 
ATOM   5628  C  CD2    . LEU   B 2  289 ? -1.019  -64.855  -38.178  1.00 47.86  ? 289 LEU   B CD2    1 
ATOM   5629  N  N      . THR   B 2  290 ? -0.370  -62.538  -42.958  1.00 53.16  ? 290 THR   B N      1 
ATOM   5630  C  CA     . THR   B 2  290 ? 0.533   -61.876  -43.893  1.00 53.97  ? 290 THR   B CA     1 
ATOM   5631  C  C      . THR   B 2  290 ? 0.229   -60.384  -44.004  1.00 54.36  ? 290 THR   B C      1 
ATOM   5632  O  O      . THR   B 2  290 ? 1.146   -59.562  -44.025  1.00 54.48  ? 290 THR   B O      1 
ATOM   5633  C  CB     . THR   B 2  290 ? 0.452   -62.572  -45.259  1.00 55.36  ? 290 THR   B CB     1 
ATOM   5634  O  OG1    . THR   B 2  290 ? 0.715   -63.973  -45.094  1.00 52.53  ? 290 THR   B OG1    1 
ATOM   5635  C  CG2    . THR   B 2  290 ? 1.470   -62.008  -46.216  1.00 54.23  ? 290 THR   B CG2    1 
ATOM   5636  N  N      . GLN   B 2  291 ? -1.049  -60.005  -44.074  1.00 60.74  ? 291 GLN   B N      1 
ATOM   5637  C  CA     . GLN   B 2  291 ? -1.366  -58.581  -44.123  1.00 62.18  ? 291 GLN   B CA     1 
ATOM   5638  C  C      . GLN   B 2  291 ? -1.029  -57.901  -42.797  1.00 62.66  ? 291 GLN   B C      1 
ATOM   5639  O  O      . GLN   B 2  291 ? -0.432  -56.815  -42.781  1.00 60.94  ? 291 GLN   B O      1 
ATOM   5640  C  CB     . GLN   B 2  291 ? -2.843  -58.361  -44.469  1.00 58.95  ? 291 GLN   B CB     1 
ATOM   5641  C  CG     . GLN   B 2  291 ? -3.243  -56.877  -44.488  1.00 69.30  ? 291 GLN   B CG     1 
ATOM   5642  C  CD     . GLN   B 2  291 ? -3.878  -56.403  -43.172  1.00 77.99  ? 291 GLN   B CD     1 
ATOM   5643  O  OE1    . GLN   B 2  291 ? -3.330  -55.531  -42.482  1.00 83.35  ? 291 GLN   B OE1    1 
ATOM   5644  N  NE2    . GLN   B 2  291 ? -5.035  -56.971  -42.824  1.00 83.35  ? 291 GLN   B NE2    1 
ATOM   5645  N  N      . GLN   B 2  292 ? -1.403  -58.529  -41.674  1.00 56.44  ? 292 GLN   B N      1 
ATOM   5646  C  CA     . GLN   B 2  292 ? -1.153  -57.937  -40.362  1.00 59.60  ? 292 GLN   B CA     1 
ATOM   5647  C  C      . GLN   B 2  292 ? 0.338   -57.758  -40.108  1.00 59.34  ? 292 GLN   B C      1 
ATOM   5648  O  O      . GLN   B 2  292 ? 0.782   -56.659  -39.755  1.00 59.76  ? 292 GLN   B O      1 
ATOM   5649  C  CB     . GLN   B 2  292 ? -1.785  -58.790  -39.258  1.00 56.09  ? 292 GLN   B CB     1 
ATOM   5650  C  CG     . GLN   B 2  292 ? -3.302  -58.828  -39.335  1.00 57.30  ? 292 GLN   B CG     1 
ATOM   5651  C  CD     . GLN   B 2  292 ? -3.962  -59.449  -38.122  1.00 61.01  ? 292 GLN   B CD     1 
ATOM   5652  O  OE1    . GLN   B 2  292 ? -3.427  -59.422  -37.012  1.00 69.82  ? 292 GLN   B OE1    1 
ATOM   5653  N  NE2    . GLN   B 2  292 ? -5.128  -60.034  -38.335  1.00 62.76  ? 292 GLN   B NE2    1 
ATOM   5654  N  N      . MET   B 2  293 ? 1.129   -58.823  -40.316  1.00 56.79  ? 293 MET   B N      1 
ATOM   5655  C  CA     . MET   B 2  293 ? 2.559   -58.796  -40.002  1.00 54.40  ? 293 MET   B CA     1 
ATOM   5656  C  C      . MET   B 2  293 ? 3.305   -57.710  -40.761  1.00 54.90  ? 293 MET   B C      1 
ATOM   5657  O  O      . MET   B 2  293 ? 4.303   -57.185  -40.256  1.00 62.88  ? 293 MET   B O      1 
ATOM   5658  C  CB     . MET   B 2  293 ? 3.199   -60.152  -40.299  1.00 57.08  ? 293 MET   B CB     1 
ATOM   5659  C  CG     . MET   B 2  293 ? 3.842   -60.246  -41.673  1.00 56.82  ? 293 MET   B CG     1 
ATOM   5660  S  SD     . MET   B 2  293 ? 4.534   -61.899  -41.931  1.00 63.35  ? 293 MET   B SD     1 
ATOM   5661  C  CE     . MET   B 2  293 ? 4.974   -62.293  -40.246  1.00 42.64  ? 293 MET   B CE     1 
ATOM   5662  N  N      . PHE   B 2  294 ? 2.870   -57.370  -41.965  1.00 50.45  ? 294 PHE   B N      1 
ATOM   5663  C  CA     . PHE   B 2  294 ? 3.456   -56.242  -42.670  1.00 48.66  ? 294 PHE   B CA     1 
ATOM   5664  C  C      . PHE   B 2  294 ? 2.793   -54.931  -42.303  1.00 50.93  ? 294 PHE   B C      1 
ATOM   5665  O  O      . PHE   B 2  294 ? 3.211   -53.885  -42.807  1.00 55.93  ? 294 PHE   B O      1 
ATOM   5666  C  CB     . PHE   B 2  294 ? 3.352   -56.435  -44.182  1.00 48.71  ? 294 PHE   B CB     1 
ATOM   5667  C  CG     . PHE   B 2  294 ? 4.421   -57.309  -44.774  1.00 54.97  ? 294 PHE   B CG     1 
ATOM   5668  C  CD1    . PHE   B 2  294 ? 4.308   -58.696  -44.735  1.00 51.17  ? 294 PHE   B CD1    1 
ATOM   5669  C  CD2    . PHE   B 2  294 ? 5.525   -56.743  -45.417  1.00 51.87  ? 294 PHE   B CD2    1 
ATOM   5670  C  CE1    . PHE   B 2  294 ? 5.286   -59.491  -45.308  1.00 54.35  ? 294 PHE   B CE1    1 
ATOM   5671  C  CE2    . PHE   B 2  294 ? 6.517   -57.543  -45.989  1.00 42.07  ? 294 PHE   B CE2    1 
ATOM   5672  C  CZ     . PHE   B 2  294 ? 6.400   -58.901  -45.939  1.00 45.70  ? 294 PHE   B CZ     1 
ATOM   5673  N  N      . ASP   B 2  295 ? 1.755   -54.967  -41.472  1.00 53.64  ? 295 ASP   B N      1 
ATOM   5674  C  CA     . ASP   B 2  295 ? 1.036   -53.755  -41.103  1.00 56.78  ? 295 ASP   B CA     1 
ATOM   5675  C  C      . ASP   B 2  295 ? 1.903   -52.908  -40.181  1.00 56.92  ? 295 ASP   B C      1 
ATOM   5676  O  O      . ASP   B 2  295 ? 2.512   -53.430  -39.233  1.00 48.39  ? 295 ASP   B O      1 
ATOM   5677  C  CB     . ASP   B 2  295 ? -0.281  -54.126  -40.418  1.00 54.98  ? 295 ASP   B CB     1 
ATOM   5678  C  CG     . ASP   B 2  295 ? -1.345  -53.036  -40.533  1.00 60.36  ? 295 ASP   B CG     1 
ATOM   5679  O  OD1    . ASP   B 2  295 ? -1.009  -51.895  -40.925  1.00 56.78  ? 295 ASP   B OD1    1 
ATOM   5680  O  OD2    . ASP   B 2  295 ? -2.537  -53.359  -40.293  1.00 63.69  ? 295 ASP   B OD2    1 
ATOM   5681  N  N      . SER   B 2  296 ? 1.970   -51.599  -40.457  1.00 50.57  ? 296 SER   B N      1 
ATOM   5682  C  CA     . SER   B 2  296 ? 2.729   -50.741  -39.560  1.00 46.67  ? 296 SER   B CA     1 
ATOM   5683  C  C      . SER   B 2  296 ? 2.188   -50.828  -38.136  1.00 49.12  ? 296 SER   B C      1 
ATOM   5684  O  O      . SER   B 2  296 ? 2.959   -50.736  -37.176  1.00 48.61  ? 296 SER   B O      1 
ATOM   5685  C  CB     . SER   B 2  296 ? 2.738   -49.308  -40.079  1.00 44.57  ? 296 SER   B CB     1 
ATOM   5686  O  OG     . SER   B 2  296 ? 1.827   -48.499  -39.371  1.00 58.69  ? 296 SER   B OG     1 
ATOM   5687  N  N      . LYS   B 2  297 ? 0.881   -51.071  -37.982  1.00 52.30  ? 297 LYS   B N      1 
ATOM   5688  C  CA     . LYS   B 2  297 ? 0.261   -51.200  -36.670  1.00 47.00  ? 297 LYS   B CA     1 
ATOM   5689  C  C      . LYS   B 2  297 ? 0.788   -52.390  -35.879  1.00 45.91  ? 297 LYS   B C      1 
ATOM   5690  O  O      . LYS   B 2  297 ? 0.466   -52.516  -34.696  1.00 50.54  ? 297 LYS   B O      1 
ATOM   5691  C  CB     . LYS   B 2  297 ? -1.261  -51.347  -36.817  1.00 53.82  ? 297 LYS   B CB     1 
ATOM   5692  C  CG     . LYS   B 2  297 ? -2.040  -50.101  -37.229  1.00 53.19  ? 297 LYS   B CG     1 
ATOM   5693  C  CD     . LYS   B 2  297 ? -3.396  -50.499  -37.839  1.00 58.33  ? 297 LYS   B CD     1 
ATOM   5694  C  CE     . LYS   B 2  297 ? -4.402  -49.349  -37.801  1.00 65.60  ? 297 LYS   B CE     1 
ATOM   5695  N  NZ     . LYS   B 2  297 ? -3.927  -48.116  -38.516  1.00 63.81  ? 297 LYS   B NZ     1 
ATOM   5696  N  N      . ASN   B 2  298 ? 1.532   -53.290  -36.513  1.00 50.88  ? 298 ASN   B N      1 
ATOM   5697  C  CA     . ASN   B 2  298 ? 2.100   -54.471  -35.878  1.00 44.12  ? 298 ASN   B CA     1 
ATOM   5698  C  C      . ASN   B 2  298 ? 3.615   -54.384  -35.726  1.00 48.14  ? 298 ASN   B C      1 
ATOM   5699  O  O      . ASN   B 2  298 ? 4.226   -55.308  -35.179  1.00 49.64  ? 298 ASN   B O      1 
ATOM   5700  C  CB     . ASN   B 2  298 ? 1.741   -55.726  -36.686  1.00 45.95  ? 298 ASN   B CB     1 
ATOM   5701  C  CG     . ASN   B 2  298 ? 0.272   -56.075  -36.589  1.00 52.39  ? 298 ASN   B CG     1 
ATOM   5702  O  OD1    . ASN   B 2  298 ? -0.586  -55.221  -36.798  1.00 52.64  ? 298 ASN   B OD1    1 
ATOM   5703  N  ND2    . ASN   B 2  298 ? -0.029  -57.331  -36.268  1.00 50.96  ? 298 ASN   B ND2    1 
ATOM   5704  N  N      . MET   B 2  299 ? 4.236   -53.315  -36.227  1.00 46.71  ? 299 MET   B N      1 
ATOM   5705  C  CA     . MET   B 2  299 ? 5.658   -53.081  -36.051  1.00 40.55  ? 299 MET   B CA     1 
ATOM   5706  C  C      . MET   B 2  299 ? 5.963   -52.653  -34.605  1.00 43.97  ? 299 MET   B C      1 
ATOM   5707  O  O      . MET   B 2  299 ? 5.234   -51.858  -34.013  1.00 45.62  ? 299 MET   B O      1 
ATOM   5708  C  CB     . MET   B 2  299 ? 6.106   -52.004  -37.038  1.00 45.26  ? 299 MET   B CB     1 
ATOM   5709  C  CG     . MET   B 2  299 ? 5.920   -52.363  -38.519  1.00 41.00  ? 299 MET   B CG     1 
ATOM   5710  S  SD     . MET   B 2  299 ? 6.603   -53.977  -38.903  1.00 49.39  ? 299 MET   B SD     1 
ATOM   5711  C  CE     . MET   B 2  299 ? 5.938   -54.325  -40.552  1.00 48.41  ? 299 MET   B CE     1 
ATOM   5712  N  N      . MET   B 2  300 ? 7.048   -53.188  -34.032  1.00 41.53  ? 300 MET   B N      1 
ATOM   5713  C  CA     . MET   B 2  300 ? 7.501   -52.839  -32.692  1.00 38.95  ? 300 MET   B CA     1 
ATOM   5714  C  C      . MET   B 2  300 ? 8.575   -51.748  -32.681  1.00 39.35  ? 300 MET   B C      1 
ATOM   5715  O  O      . MET   B 2  300 ? 9.307   -51.631  -31.698  1.00 38.36  ? 300 MET   B O      1 
ATOM   5716  C  CB     . MET   B 2  300 ? 8.037   -54.068  -31.982  1.00 41.94  ? 300 MET   B CB     1 
ATOM   5717  C  CG     . MET   B 2  300 ? 7.173   -55.252  -32.183  1.00 47.61  ? 300 MET   B CG     1 
ATOM   5718  S  SD     . MET   B 2  300 ? 5.877   -55.269  -30.958  1.00 44.83  ? 300 MET   B SD     1 
ATOM   5719  C  CE     . MET   B 2  300 ? 5.115   -56.840  -31.365  1.00 51.07  ? 300 MET   B CE     1 
ATOM   5720  N  N      . ALA   B 2  301 ? 8.671   -50.958  -33.747  1.00 36.83  ? 301 ALA   B N      1 
ATOM   5721  C  CA     . ALA   B 2  301 ? 9.526   -49.785  -33.839  1.00 34.85  ? 301 ALA   B CA     1 
ATOM   5722  C  C      . ALA   B 2  301 ? 8.687   -48.725  -34.527  1.00 43.87  ? 301 ALA   B C      1 
ATOM   5723  O  O      . ALA   B 2  301 ? 8.235   -48.930  -35.665  1.00 43.37  ? 301 ALA   B O      1 
ATOM   5724  C  CB     . ALA   B 2  301 ? 10.817  -50.069  -34.636  1.00 37.48  ? 301 ALA   B CB     1 
ATOM   5725  N  N      . ALA   B 2  302 ? 8.453   -47.609  -33.839  1.00 40.83  ? 302 ALA   B N      1 
ATOM   5726  C  CA     . ALA   B 2  302 ? 7.470   -46.667  -34.343  1.00 32.71  ? 302 ALA   B CA     1 
ATOM   5727  C  C      . ALA   B 2  302 ? 8.001   -46.024  -35.617  1.00 43.86  ? 302 ALA   B C      1 
ATOM   5728  O  O      . ALA   B 2  302 ? 8.432   -44.863  -35.612  1.00 46.88  ? 302 ALA   B O      1 
ATOM   5729  C  CB     . ALA   B 2  302 ? 7.117   -45.641  -33.277  1.00 32.31  ? 302 ALA   B CB     1 
ATOM   5730  N  N      . CYS   B 2  303 ? 8.009   -46.799  -36.704  1.00 40.11  ? 303 CYS   B N      1 
ATOM   5731  C  CA     . CYS   B 2  303 ? 8.354   -46.316  -38.030  1.00 44.53  ? 303 CYS   B CA     1 
ATOM   5732  C  C      . CYS   B 2  303 ? 7.264   -46.723  -39.000  1.00 46.97  ? 303 CYS   B C      1 
ATOM   5733  O  O      . CYS   B 2  303 ? 6.610   -47.753  -38.833  1.00 52.02  ? 303 CYS   B O      1 
ATOM   5734  C  CB     . CYS   B 2  303 ? 9.692   -46.866  -38.512  1.00 44.97  ? 303 CYS   B CB     1 
ATOM   5735  S  SG     . CYS   B 2  303 ? 10.966  -46.607  -37.254  1.00 59.56  ? 303 CYS   B SG     1 
ATOM   5736  N  N      . ASP   B 2  304 ? 7.063   -45.873  -39.994  1.00 49.30  ? 304 ASP   B N      1 
ATOM   5737  C  CA     . ASP   B 2  304 ? 6.137   -46.129  -41.079  1.00 50.60  ? 304 ASP   B CA     1 
ATOM   5738  C  C      . ASP   B 2  304 ? 6.899   -46.855  -42.177  1.00 53.55  ? 304 ASP   B C      1 
ATOM   5739  O  O      . ASP   B 2  304 ? 7.768   -46.238  -42.822  1.00 53.42  ? 304 ASP   B O      1 
ATOM   5740  C  CB     . ASP   B 2  304 ? 5.584   -44.809  -41.596  1.00 58.67  ? 304 ASP   B CB     1 
ATOM   5741  C  CG     . ASP   B 2  304 ? 4.493   -44.984  -42.631  1.00 60.37  ? 304 ASP   B CG     1 
ATOM   5742  O  OD1    . ASP   B 2  304 ? 4.315   -46.115  -43.149  1.00 58.36  ? 304 ASP   B OD1    1 
ATOM   5743  O  OD2    . ASP   B 2  304 ? 3.834   -43.965  -42.931  1.00 61.42  ? 304 ASP   B OD2    1 
ATOM   5744  N  N      . PRO   B 2  305 ? 6.631   -48.139  -42.429  1.00 50.28  ? 305 PRO   B N      1 
ATOM   5745  C  CA     . PRO   B 2  305 ? 7.418   -48.852  -43.449  1.00 46.13  ? 305 PRO   B CA     1 
ATOM   5746  C  C      . PRO   B 2  305 ? 7.258   -48.235  -44.821  1.00 51.97  ? 305 PRO   B C      1 
ATOM   5747  O  O      . PRO   B 2  305 ? 8.161   -48.347  -45.661  1.00 47.20  ? 305 PRO   B O      1 
ATOM   5748  C  CB     . PRO   B 2  305 ? 6.856   -50.276  -43.400  1.00 40.31  ? 305 PRO   B CB     1 
ATOM   5749  C  CG     . PRO   B 2  305 ? 6.010   -50.336  -42.134  1.00 52.50  ? 305 PRO   B CG     1 
ATOM   5750  C  CD     . PRO   B 2  305 ? 5.506   -48.942  -41.939  1.00 50.14  ? 305 PRO   B CD     1 
ATOM   5751  N  N      . ARG   B 2  306 ? 6.128   -47.561  -45.066  1.00 53.16  ? 306 ARG   B N      1 
ATOM   5752  C  CA     . ARG   B 2  306 ? 5.892   -46.864  -46.326  1.00 51.66  ? 306 ARG   B CA     1 
ATOM   5753  C  C      . ARG   B 2  306 ? 6.751   -45.612  -46.498  1.00 55.89  ? 306 ARG   B C      1 
ATOM   5754  O  O      . ARG   B 2  306 ? 6.741   -45.034  -47.590  1.00 57.48  ? 306 ARG   B O      1 
ATOM   5755  C  CB     . ARG   B 2  306 ? 4.417   -46.499  -46.437  1.00 54.44  ? 306 ARG   B CB     1 
ATOM   5756  C  CG     . ARG   B 2  306 ? 3.520   -47.707  -46.564  1.00 55.80  ? 306 ARG   B CG     1 
ATOM   5757  C  CD     . ARG   B 2  306 ? 2.056   -47.327  -46.652  1.00 52.75  ? 306 ARG   B CD     1 
ATOM   5758  N  NE     . ARG   B 2  306 ? 1.328   -48.424  -47.264  1.00 53.58  ? 306 ARG   B NE     1 
ATOM   5759  C  CZ     . ARG   B 2  306 ? 1.149   -48.538  -48.571  1.00 60.48  ? 306 ARG   B CZ     1 
ATOM   5760  N  NH1    . ARG   B 2  306 ? 1.546   -47.590  -49.405  1.00 63.13  ? 306 ARG   B NH1    1 
ATOM   5761  N  NH2    . ARG   B 2  306 ? 0.588   -49.641  -49.058  1.00 57.70  ? 306 ARG   B NH2    1 
ATOM   5762  N  N      . HIS   B 2  307 ? 7.485   -45.172  -45.467  1.00 54.16  ? 307 HIS   B N      1 
ATOM   5763  C  CA     . HIS   B 2  307 ? 8.433   -44.068  -45.608  1.00 51.02  ? 307 HIS   B CA     1 
ATOM   5764  C  C      . HIS   B 2  307 ? 9.853   -44.540  -45.892  1.00 54.99  ? 307 HIS   B C      1 
ATOM   5765  O  O      . HIS   B 2  307 ? 10.742  -43.702  -46.051  1.00 64.13  ? 307 HIS   B O      1 
ATOM   5766  C  CB     . HIS   B 2  307 ? 8.457   -43.188  -44.351  1.00 55.20  ? 307 HIS   B CB     1 
ATOM   5767  C  CG     . HIS   B 2  307 ? 7.122   -42.621  -43.969  1.00 62.58  ? 307 HIS   B CG     1 
ATOM   5768  N  ND1    . HIS   B 2  307 ? 6.869   -42.108  -42.714  1.00 60.14  ? 307 HIS   B ND1    1 
ATOM   5769  C  CD2    . HIS   B 2  307 ? 5.969   -42.492  -44.667  1.00 58.40  ? 307 HIS   B CD2    1 
ATOM   5770  C  CE1    . HIS   B 2  307 ? 5.617   -41.694  -42.654  1.00 62.68  ? 307 HIS   B CE1    1 
ATOM   5771  N  NE2    . HIS   B 2  307 ? 5.049   -41.917  -43.825  1.00 60.39  ? 307 HIS   B NE2    1 
ATOM   5772  N  N      . GLY   B 2  308 ? 10.100  -45.846  -45.929  1.00 50.32  ? 308 GLY   B N      1 
ATOM   5773  C  CA     . GLY   B 2  308 ? 11.391  -46.362  -46.345  1.00 52.20  ? 308 GLY   B CA     1 
ATOM   5774  C  C      . GLY   B 2  308 ? 11.291  -47.488  -47.363  1.00 55.64  ? 308 GLY   B C      1 
ATOM   5775  O  O      . GLY   B 2  308 ? 10.213  -47.757  -47.907  1.00 53.75  ? 308 GLY   B O      1 
ATOM   5776  N  N      . ARG   B 2  309 ? 12.408  -48.152  -47.646  1.00 49.25  ? 309 ARG   B N      1 
ATOM   5777  C  CA     . ARG   B 2  309 ? 12.398  -49.365  -48.449  1.00 47.43  ? 309 ARG   B CA     1 
ATOM   5778  C  C      . ARG   B 2  309 ? 12.949  -50.504  -47.607  1.00 45.47  ? 309 ARG   B C      1 
ATOM   5779  O  O      . ARG   B 2  309 ? 13.837  -50.303  -46.775  1.00 42.00  ? 309 ARG   B O      1 
ATOM   5780  C  CB     . ARG   B 2  309 ? 13.208  -49.219  -49.743  1.00 46.96  ? 309 ARG   B CB     1 
ATOM   5781  C  CG     . ARG   B 2  309 ? 13.023  -47.884  -50.433  1.00 55.83  ? 309 ARG   B CG     1 
ATOM   5782  C  CD     . ARG   B 2  309 ? 12.618  -48.039  -51.887  1.00 54.94  ? 309 ARG   B CD     1 
ATOM   5783  N  NE     . ARG   B 2  309 ? 13.763  -48.342  -52.733  1.00 62.13  ? 309 ARG   B NE     1 
ATOM   5784  C  CZ     . ARG   B 2  309 ? 13.703  -49.069  -53.839  1.00 65.54  ? 309 ARG   B CZ     1 
ATOM   5785  N  NH1    . ARG   B 2  309 ? 12.557  -49.572  -54.273  1.00 63.93  ? 309 ARG   B NH1    1 
ATOM   5786  N  NH2    . ARG   B 2  309 ? 14.824  -49.308  -54.521  1.00 70.82  ? 309 ARG   B NH2    1 
ATOM   5787  N  N      . TYR   B 2  310 ? 12.388  -51.690  -47.798  1.00 45.48  ? 310 TYR   B N      1 
ATOM   5788  C  CA     . TYR   B 2  310 ? 12.906  -52.894  -47.164  1.00 43.05  ? 310 TYR   B CA     1 
ATOM   5789  C  C      . TYR   B 2  310 ? 14.207  -53.307  -47.845  1.00 43.18  ? 310 TYR   B C      1 
ATOM   5790  O  O      . TYR   B 2  310 ? 14.220  -53.679  -49.021  1.00 40.36  ? 310 TYR   B O      1 
ATOM   5791  C  CB     . TYR   B 2  310 ? 11.862  -54.001  -47.234  1.00 41.01  ? 310 TYR   B CB     1 
ATOM   5792  C  CG     . TYR   B 2  310 ? 10.798  -53.812  -46.188  1.00 43.39  ? 310 TYR   B CG     1 
ATOM   5793  C  CD1    . TYR   B 2  310 ? 11.100  -53.967  -44.847  1.00 42.96  ? 310 TYR   B CD1    1 
ATOM   5794  C  CD2    . TYR   B 2  310 ? 9.509   -53.443  -46.530  1.00 45.88  ? 310 TYR   B CD2    1 
ATOM   5795  C  CE1    . TYR   B 2  310 ? 10.154  -53.790  -43.879  1.00 44.00  ? 310 TYR   B CE1    1 
ATOM   5796  C  CE2    . TYR   B 2  310 ? 8.548   -53.252  -45.560  1.00 48.38  ? 310 TYR   B CE2    1 
ATOM   5797  C  CZ     . TYR   B 2  310 ? 8.881   -53.430  -44.232  1.00 48.21  ? 310 TYR   B CZ     1 
ATOM   5798  O  OH     . TYR   B 2  310 ? 7.941   -53.261  -43.242  1.00 49.71  ? 310 TYR   B OH     1 
ATOM   5799  N  N      . LEU   B 2  311 ? 15.313  -53.204  -47.117  1.00 39.24  ? 311 LEU   B N      1 
ATOM   5800  C  CA     . LEU   B 2  311 ? 16.551  -53.803  -47.584  1.00 42.45  ? 311 LEU   B CA     1 
ATOM   5801  C  C      . LEU   B 2  311 ? 16.409  -55.320  -47.647  1.00 43.25  ? 311 LEU   B C      1 
ATOM   5802  O  O      . LEU   B 2  311 ? 16.549  -55.929  -48.714  1.00 41.17  ? 311 LEU   B O      1 
ATOM   5803  C  CB     . LEU   B 2  311 ? 17.712  -53.379  -46.672  1.00 35.60  ? 311 LEU   B CB     1 
ATOM   5804  C  CG     . LEU   B 2  311 ? 18.009  -51.888  -46.818  1.00 38.74  ? 311 LEU   B CG     1 
ATOM   5805  C  CD1    . LEU   B 2  311 ? 19.263  -51.486  -46.127  1.00 40.73  ? 311 LEU   B CD1    1 
ATOM   5806  C  CD2    . LEU   B 2  311 ? 18.107  -51.547  -48.281  1.00 44.81  ? 311 LEU   B CD2    1 
ATOM   5807  N  N      . THR   B 2  312 ? 16.113  -55.945  -46.510  1.00 36.18  ? 312 THR   B N      1 
ATOM   5808  C  CA     . THR   B 2  312 ? 15.889  -57.377  -46.455  1.00 35.56  ? 312 THR   B CA     1 
ATOM   5809  C  C      . THR   B 2  312 ? 14.744  -57.655  -45.488  1.00 40.36  ? 312 THR   B C      1 
ATOM   5810  O  O      . THR   B 2  312 ? 14.322  -56.781  -44.716  1.00 38.98  ? 312 THR   B O      1 
ATOM   5811  C  CB     . THR   B 2  312 ? 17.149  -58.124  -46.029  1.00 39.95  ? 312 THR   B CB     1 
ATOM   5812  O  OG1    . THR   B 2  312 ? 17.505  -57.698  -44.711  1.00 42.77  ? 312 THR   B OG1    1 
ATOM   5813  C  CG2    . THR   B 2  312 ? 18.313  -57.861  -46.997  1.00 33.59  ? 312 THR   B CG2    1 
ATOM   5814  N  N      . VAL   B 2  313 ? 14.214  -58.876  -45.556  1.00 35.65  ? 313 VAL   B N      1 
ATOM   5815  C  CA     . VAL   B 2  313 ? 13.065  -59.257  -44.745  1.00 38.31  ? 313 VAL   B CA     1 
ATOM   5816  C  C      . VAL   B 2  313 ? 13.154  -60.741  -44.429  1.00 37.90  ? 313 VAL   B C      1 
ATOM   5817  O  O      . VAL   B 2  313 ? 13.345  -61.557  -45.331  1.00 37.94  ? 313 VAL   B O      1 
ATOM   5818  C  CB     . VAL   B 2  313 ? 11.718  -58.973  -45.447  1.00 39.16  ? 313 VAL   B CB     1 
ATOM   5819  C  CG1    . VAL   B 2  313 ? 10.574  -59.133  -44.428  1.00 38.18  ? 313 VAL   B CG1    1 
ATOM   5820  C  CG2    . VAL   B 2  313 ? 11.689  -57.616  -46.090  1.00 35.55  ? 313 VAL   B CG2    1 
ATOM   5821  N  N      . ALA   B 2  314 ? 12.976  -61.097  -43.163  1.00 33.76  ? 314 ALA   B N      1 
ATOM   5822  C  CA     . ALA   B 2  314 ? 12.748  -62.478  -42.769  1.00 37.67  ? 314 ALA   B CA     1 
ATOM   5823  C  C      . ALA   B 2  314 ? 11.373  -62.575  -42.119  1.00 43.74  ? 314 ALA   B C      1 
ATOM   5824  O  O      . ALA   B 2  314 ? 10.984  -61.689  -41.352  1.00 44.78  ? 314 ALA   B O      1 
ATOM   5825  C  CB     . ALA   B 2  314 ? 13.819  -62.965  -41.800  1.00 40.39  ? 314 ALA   B CB     1 
ATOM   5826  N  N      . ALA   B 2  315 ? 10.638  -63.647  -42.417  1.00 41.45  ? 315 ALA   B N      1 
ATOM   5827  C  CA     . ALA   B 2  315 ? 9.279   -63.828  -41.904  1.00 41.39  ? 315 ALA   B CA     1 
ATOM   5828  C  C      . ALA   B 2  315 ? 9.114   -65.269  -41.453  1.00 46.12  ? 315 ALA   B C      1 
ATOM   5829  O  O      . ALA   B 2  315 ? 9.490   -66.201  -42.178  1.00 44.73  ? 315 ALA   B O      1 
ATOM   5830  C  CB     . ALA   B 2  315 ? 8.220   -63.473  -42.955  1.00 33.87  ? 315 ALA   B CB     1 
ATOM   5831  N  N      . ILE   B 2  316 ? 8.560   -65.449  -40.255  1.00 40.36  ? 316 ILE   B N      1 
ATOM   5832  C  CA     . ILE   B 2  316 ? 8.475   -66.759  -39.625  1.00 42.37  ? 316 ILE   B CA     1 
ATOM   5833  C  C      . ILE   B 2  316 ? 7.019   -67.044  -39.272  1.00 43.26  ? 316 ILE   B C      1 
ATOM   5834  O  O      . ILE   B 2  316 ? 6.367   -66.231  -38.617  1.00 49.22  ? 316 ILE   B O      1 
ATOM   5835  C  CB     . ILE   B 2  316 ? 9.389   -66.842  -38.390  1.00 40.10  ? 316 ILE   B CB     1 
ATOM   5836  C  CG1    . ILE   B 2  316 ? 9.023   -68.044  -37.544  1.00 52.09  ? 316 ILE   B CG1    1 
ATOM   5837  C  CG2    . ILE   B 2  316 ? 9.276   -65.603  -37.565  1.00 49.57  ? 316 ILE   B CG2    1 
ATOM   5838  C  CD1    . ILE   B 2  316 ? 9.257   -69.325  -38.255  1.00 61.77  ? 316 ILE   B CD1    1 
ATOM   5839  N  N      . PHE   B 2  317 ? 6.506   -68.185  -39.731  1.00 46.90  ? 317 PHE   B N      1 
ATOM   5840  C  CA     . PHE   B 2  317 ? 5.109   -68.580  -39.559  1.00 47.59  ? 317 PHE   B CA     1 
ATOM   5841  C  C      . PHE   B 2  317 ? 5.034   -69.761  -38.599  1.00 46.49  ? 317 PHE   B C      1 
ATOM   5842  O  O      . PHE   B 2  317 ? 5.751   -70.750  -38.769  1.00 49.36  ? 317 PHE   B O      1 
ATOM   5843  C  CB     . PHE   B 2  317 ? 4.475   -68.957  -40.904  1.00 44.07  ? 317 PHE   B CB     1 
ATOM   5844  C  CG     . PHE   B 2  317 ? 4.189   -67.777  -41.803  1.00 48.08  ? 317 PHE   B CG     1 
ATOM   5845  C  CD1    . PHE   B 2  317 ? 5.184   -67.252  -42.627  1.00 42.93  ? 317 PHE   B CD1    1 
ATOM   5846  C  CD2    . PHE   B 2  317 ? 2.924   -67.198  -41.829  1.00 43.93  ? 317 PHE   B CD2    1 
ATOM   5847  C  CE1    . PHE   B 2  317 ? 4.924   -66.169  -43.452  1.00 40.54  ? 317 PHE   B CE1    1 
ATOM   5848  C  CE2    . PHE   B 2  317 ? 2.662   -66.114  -42.645  1.00 45.65  ? 317 PHE   B CE2    1 
ATOM   5849  C  CZ     . PHE   B 2  317 ? 3.660   -65.596  -43.454  1.00 46.07  ? 317 PHE   B CZ     1 
ATOM   5850  N  N      . ARG   B 2  318 ? 4.167   -69.675  -37.598  1.00 44.82  ? 318 ARG   B N      1 
ATOM   5851  C  CA     . ARG   B 2  318 ? 4.105   -70.711  -36.576  1.00 48.21  ? 318 ARG   B CA     1 
ATOM   5852  C  C      . ARG   B 2  318 ? 2.707   -71.307  -36.487  1.00 53.19  ? 318 ARG   B C      1 
ATOM   5853  O  O      . ARG   B 2  318 ? 1.729   -70.579  -36.273  1.00 53.72  ? 318 ARG   B O      1 
ATOM   5854  C  CB     . ARG   B 2  318 ? 4.563   -70.142  -35.235  1.00 53.33  ? 318 ARG   B CB     1 
ATOM   5855  C  CG     . ARG   B 2  318 ? 6.057   -69.918  -35.233  1.00 52.31  ? 318 ARG   B CG     1 
ATOM   5856  C  CD     . ARG   B 2  318 ? 6.573   -69.583  -33.885  1.00 50.80  ? 318 ARG   B CD     1 
ATOM   5857  N  NE     . ARG   B 2  318 ? 6.516   -70.727  -32.998  1.00 54.32  ? 318 ARG   B NE     1 
ATOM   5858  C  CZ     . ARG   B 2  318 ? 7.036   -70.725  -31.783  1.00 56.63  ? 318 ARG   B CZ     1 
ATOM   5859  N  NH1    . ARG   B 2  318 ? 7.698   -69.677  -31.325  1.00 51.77  ? 318 ARG   B NH1    1 
ATOM   5860  N  NH2    . ARG   B 2  318 ? 6.874   -71.791  -31.005  1.00 57.40  ? 318 ARG   B NH2    1 
ATOM   5861  N  N      . GLY   B 2  319 ? 2.628   -72.625  -36.642  1.00 54.86  ? 319 GLY   B N      1 
ATOM   5862  C  CA     . GLY   B 2  319 ? 1.391   -73.378  -36.556  1.00 60.30  ? 319 GLY   B CA     1 
ATOM   5863  C  C      . GLY   B 2  319 ? 1.210   -74.309  -37.741  1.00 62.12  ? 319 GLY   B C      1 
ATOM   5864  O  O      . GLY   B 2  319 ? 1.982   -74.309  -38.696  1.00 63.72  ? 319 GLY   B O      1 
ATOM   5865  N  N      . ARG   B 2  320 ? 0.144   -75.112  -37.656  1.00 71.03  ? 320 ARG   B N      1 
ATOM   5866  C  CA     . ARG   B 2  320 ? -0.269  -75.990  -38.752  1.00 66.98  ? 320 ARG   B CA     1 
ATOM   5867  C  C      . ARG   B 2  320 ? -0.952  -75.164  -39.836  1.00 64.75  ? 320 ARG   B C      1 
ATOM   5868  O  O      . ARG   B 2  320 ? -2.013  -74.571  -39.597  1.00 65.63  ? 320 ARG   B O      1 
ATOM   5869  C  CB     . ARG   B 2  320 ? -1.213  -77.082  -38.246  1.00 73.38  ? 320 ARG   B CB     1 
ATOM   5870  C  CG     . ARG   B 2  320 ? -0.522  -78.371  -37.775  1.00 82.03  ? 320 ARG   B CG     1 
ATOM   5871  C  CD     . ARG   B 2  320 ? -1.485  -79.585  -37.807  1.00 89.47  ? 320 ARG   B CD     1 
ATOM   5872  N  NE     . ARG   B 2  320 ? -1.910  -80.028  -36.481  1.00 99.44  ? 320 ARG   B NE     1 
ATOM   5873  C  CZ     . ARG   B 2  320 ? -3.084  -79.749  -35.922  1.00 98.21  ? 320 ARG   B CZ     1 
ATOM   5874  N  NH1    . ARG   B 2  320 ? -4.010  -79.045  -36.561  1.00 88.18  ? 320 ARG   B NH1    1 
ATOM   5875  N  NH2    . ARG   B 2  320 ? -3.333  -80.182  -34.687  1.00 94.01  ? 320 ARG   B NH2    1 
ATOM   5876  N  N      . MET   B 2  321 ? -0.346  -75.116  -41.019  1.00 62.32  ? 321 MET   B N      1 
ATOM   5877  C  CA     . MET   B 2  321 ? -0.889  -74.339  -42.126  1.00 60.19  ? 321 MET   B CA     1 
ATOM   5878  C  C      . MET   B 2  321 ? -0.194  -74.784  -43.409  1.00 65.06  ? 321 MET   B C      1 
ATOM   5879  O  O      . MET   B 2  321 ? 0.843   -75.456  -43.381  1.00 59.98  ? 321 MET   B O      1 
ATOM   5880  C  CB     . MET   B 2  321 ? -0.713  -72.836  -41.895  1.00 55.20  ? 321 MET   B CB     1 
ATOM   5881  C  CG     . MET   B 2  321 ? 0.687   -72.329  -42.230  1.00 65.57  ? 321 MET   B CG     1 
ATOM   5882  S  SD     . MET   B 2  321 ? 1.369   -71.153  -41.044  1.00 66.52  ? 321 MET   B SD     1 
ATOM   5883  C  CE     . MET   B 2  321 ? 0.154   -69.848  -41.152  1.00 63.45  ? 321 MET   B CE     1 
ATOM   5884  N  N      . SER   B 2  322 ? -0.781  -74.394  -44.543  1.00 69.84  ? 322 SER   B N      1 
ATOM   5885  C  CA     . SER   B 2  322 ? -0.250  -74.767  -45.855  1.00 69.83  ? 322 SER   B CA     1 
ATOM   5886  C  C      . SER   B 2  322 ? 0.954   -73.896  -46.187  1.00 64.67  ? 322 SER   B C      1 
ATOM   5887  O  O      . SER   B 2  322 ? 0.827   -72.675  -46.326  1.00 61.89  ? 322 SER   B O      1 
ATOM   5888  C  CB     . SER   B 2  322 ? -1.323  -74.638  -46.935  1.00 71.87  ? 322 SER   B CB     1 
ATOM   5889  O  OG     . SER   B 2  322 ? -1.888  -73.329  -46.941  1.00 77.99  ? 322 SER   B OG     1 
ATOM   5890  N  N      . MET   B 2  323 ? 2.129   -74.519  -46.316  1.00 64.63  ? 323 MET   B N      1 
ATOM   5891  C  CA     . MET   B 2  323 ? 3.243   -73.786  -46.901  1.00 63.60  ? 323 MET   B CA     1 
ATOM   5892  C  C      . MET   B 2  323 ? 2.986   -73.407  -48.351  1.00 72.22  ? 323 MET   B C      1 
ATOM   5893  O  O      . MET   B 2  323 ? 3.709   -72.563  -48.888  1.00 74.46  ? 323 MET   B O      1 
ATOM   5894  C  CB     . MET   B 2  323 ? 4.542   -74.579  -46.819  1.00 71.57  ? 323 MET   B CB     1 
ATOM   5895  C  CG     . MET   B 2  323 ? 4.878   -75.105  -45.451  1.00 73.03  ? 323 MET   B CG     1 
ATOM   5896  S  SD     . MET   B 2  323 ? 6.127   -76.388  -45.634  1.00 95.18  ? 323 MET   B SD     1 
ATOM   5897  C  CE     . MET   B 2  323 ? 7.604   -75.400  -45.920  1.00 69.39  ? 323 MET   B CE     1 
ATOM   5898  N  N      . LYS   B 2  324 ? 1.985   -73.997  -49.007  1.00 74.86  ? 324 LYS   B N      1 
ATOM   5899  C  CA     . LYS   B 2  324 ? 1.579   -73.459  -50.298  1.00 69.79  ? 324 LYS   B CA     1 
ATOM   5900  C  C      . LYS   B 2  324 ? 0.937   -72.085  -50.121  1.00 66.62  ? 324 LYS   B C      1 
ATOM   5901  O  O      . LYS   B 2  324 ? 1.345   -71.114  -50.764  1.00 66.58  ? 324 LYS   B O      1 
ATOM   5902  C  CB     . LYS   B 2  324 ? 0.646   -74.437  -51.020  1.00 70.42  ? 324 LYS   B CB     1 
ATOM   5903  C  CG     . LYS   B 2  324 ? 0.341   -74.057  -52.477  1.00 65.38  ? 324 LYS   B CG     1 
ATOM   5904  C  CD     . LYS   B 2  324 ? -1.083  -74.465  -52.876  1.00 72.91  ? 324 LYS   B CD     1 
ATOM   5905  C  CE     . LYS   B 2  324 ? -1.325  -74.309  -54.386  1.00 80.38  ? 324 LYS   B CE     1 
ATOM   5906  N  NZ     . LYS   B 2  324 ? -1.247  -75.583  -55.171  1.00 72.85  ? 324 LYS   B NZ     1 
ATOM   5907  N  N      . GLU   B 2  325 ? -0.045  -71.969  -49.227  1.00 64.78  ? 325 GLU   B N      1 
ATOM   5908  C  CA     . GLU   B 2  325 ? -0.692  -70.673  -49.043  1.00 69.59  ? 325 GLU   B CA     1 
ATOM   5909  C  C      . GLU   B 2  325 ? 0.266   -69.631  -48.461  1.00 69.69  ? 325 GLU   B C      1 
ATOM   5910  O  O      . GLU   B 2  325 ? 0.159   -68.437  -48.785  1.00 60.48  ? 325 GLU   B O      1 
ATOM   5911  C  CB     . GLU   B 2  325 ? -1.919  -70.825  -48.156  1.00 65.81  ? 325 GLU   B CB     1 
ATOM   5912  C  CG     . GLU   B 2  325 ? -3.066  -69.932  -48.559  1.00 67.42  ? 325 GLU   B CG     1 
ATOM   5913  C  CD     . GLU   B 2  325 ? -4.251  -70.079  -47.625  1.00 78.48  ? 325 GLU   B CD     1 
ATOM   5914  O  OE1    . GLU   B 2  325 ? -4.205  -70.961  -46.730  1.00 78.95  ? 325 GLU   B OE1    1 
ATOM   5915  O  OE2    . GLU   B 2  325 ? -5.228  -69.312  -47.786  1.00 82.59  ? 325 GLU   B OE2    1 
ATOM   5916  N  N      . VAL   B 2  326 ? 1.208   -70.052  -47.610  1.00 65.35  ? 326 VAL   B N      1 
ATOM   5917  C  CA     . VAL   B 2  326 ? 2.230   -69.122  -47.144  1.00 60.73  ? 326 VAL   B CA     1 
ATOM   5918  C  C      . VAL   B 2  326 ? 3.049   -68.611  -48.324  1.00 65.77  ? 326 VAL   B C      1 
ATOM   5919  O  O      . VAL   B 2  326 ? 3.159   -67.398  -48.542  1.00 67.23  ? 326 VAL   B O      1 
ATOM   5920  C  CB     . VAL   B 2  326 ? 3.117   -69.773  -46.071  1.00 61.52  ? 326 VAL   B CB     1 
ATOM   5921  C  CG1    . VAL   B 2  326 ? 3.987   -68.722  -45.435  1.00 56.18  ? 326 VAL   B CG1    1 
ATOM   5922  C  CG2    . VAL   B 2  326 ? 2.270   -70.446  -45.004  1.00 57.46  ? 326 VAL   B CG2    1 
ATOM   5923  N  N      . ASP   B 2  327 ? 3.612   -69.532  -49.119  1.00 70.47  ? 327 ASP   B N      1 
ATOM   5924  C  CA     . ASP   B 2  327 ? 4.310   -69.152  -50.350  1.00 65.17  ? 327 ASP   B CA     1 
ATOM   5925  C  C      . ASP   B 2  327 ? 3.482   -68.165  -51.166  1.00 63.87  ? 327 ASP   B C      1 
ATOM   5926  O  O      . ASP   B 2  327 ? 3.996   -67.151  -51.644  1.00 67.73  ? 327 ASP   B O      1 
ATOM   5927  C  CB     . ASP   B 2  327 ? 4.622   -70.393  -51.201  1.00 64.33  ? 327 ASP   B CB     1 
ATOM   5928  C  CG     . ASP   B 2  327 ? 5.772   -71.235  -50.644  1.00 73.95  ? 327 ASP   B CG     1 
ATOM   5929  O  OD1    . ASP   B 2  327 ? 6.100   -72.287  -51.249  1.00 74.76  ? 327 ASP   B OD1    1 
ATOM   5930  O  OD2    . ASP   B 2  327 ? 6.346   -70.860  -49.598  1.00 79.78  ? 327 ASP   B OD2    1 
ATOM   5931  N  N      . GLU   B 2  328 ? 2.188   -68.449  -51.332  1.00 67.58  ? 328 GLU   B N      1 
ATOM   5932  C  CA     . GLU   B 2  328 ? 1.352   -67.625  -52.200  1.00 70.65  ? 328 GLU   B CA     1 
ATOM   5933  C  C      . GLU   B 2  328 ? 1.071   -66.271  -51.572  1.00 66.74  ? 328 GLU   B C      1 
ATOM   5934  O  O      . GLU   B 2  328 ? 1.168   -65.236  -52.242  1.00 65.42  ? 328 GLU   B O      1 
ATOM   5935  C  CB     . GLU   B 2  328 ? 0.039   -68.344  -52.517  1.00 70.73  ? 328 GLU   B CB     1 
ATOM   5936  C  CG     . GLU   B 2  328 ? 0.226   -69.730  -53.093  1.00 74.96  ? 328 GLU   B CG     1 
ATOM   5937  C  CD     . GLU   B 2  328 ? -1.084  -70.373  -53.484  1.00 83.19  ? 328 GLU   B CD     1 
ATOM   5938  O  OE1    . GLU   B 2  328 ? -2.127  -69.682  -53.407  1.00 84.94  ? 328 GLU   B OE1    1 
ATOM   5939  O  OE2    . GLU   B 2  328 ? -1.066  -71.566  -53.865  1.00 82.50  ? 328 GLU   B OE2    1 
ATOM   5940  N  N      . GLN   B 2  329 ? 0.711   -66.261  -50.282  1.00 66.50  ? 329 GLN   B N      1 
ATOM   5941  C  CA     . GLN   B 2  329 ? 0.413   -65.004  -49.605  1.00 64.22  ? 329 GLN   B CA     1 
ATOM   5942  C  C      . GLN   B 2  329 ? 1.648   -64.124  -49.479  1.00 58.39  ? 329 GLN   B C      1 
ATOM   5943  O  O      . GLN   B 2  329 ? 1.542   -62.896  -49.558  1.00 56.17  ? 329 GLN   B O      1 
ATOM   5944  C  CB     . GLN   B 2  329 ? -0.193  -65.280  -48.232  1.00 63.84  ? 329 GLN   B CB     1 
ATOM   5945  C  CG     . GLN   B 2  329 ? -1.700  -65.503  -48.274  1.00 58.69  ? 329 GLN   B CG     1 
ATOM   5946  C  CD     . GLN   B 2  329 ? -2.394  -64.459  -49.098  1.00 62.25  ? 329 GLN   B CD     1 
ATOM   5947  O  OE1    . GLN   B 2  329 ? -1.992  -63.298  -49.110  1.00 67.14  ? 329 GLN   B OE1    1 
ATOM   5948  N  NE2    . GLN   B 2  329 ? -3.416  -64.866  -49.827  1.00 67.43  ? 329 GLN   B NE2    1 
ATOM   5949  N  N      . MET   B 2  330 ? 2.827   -64.729  -49.320  1.00 60.77  ? 330 MET   B N      1 
ATOM   5950  C  CA     . MET   B 2  330 ? 4.058   -63.943  -49.234  1.00 62.17  ? 330 MET   B CA     1 
ATOM   5951  C  C      . MET   B 2  330 ? 4.501   -63.426  -50.595  1.00 64.48  ? 330 MET   B C      1 
ATOM   5952  O  O      . MET   B 2  330 ? 4.941   -62.276  -50.707  1.00 66.08  ? 330 MET   B O      1 
ATOM   5953  C  CB     . MET   B 2  330 ? 5.178   -64.763  -48.604  1.00 52.72  ? 330 MET   B CB     1 
ATOM   5954  C  CG     . MET   B 2  330 ? 5.037   -64.944  -47.103  1.00 53.02  ? 330 MET   B CG     1 
ATOM   5955  S  SD     . MET   B 2  330 ? 5.229   -63.420  -46.163  1.00 50.10  ? 330 MET   B SD     1 
ATOM   5956  C  CE     . MET   B 2  330 ? 6.753   -62.772  -46.817  1.00 53.05  ? 330 MET   B CE     1 
ATOM   5957  N  N      . LEU   B 2  331 ? 4.398   -64.251  -51.641  1.00 62.60  ? 331 LEU   B N      1 
ATOM   5958  C  CA     . LEU   B 2  331 ? 4.697   -63.750  -52.976  1.00 63.12  ? 331 LEU   B CA     1 
ATOM   5959  C  C      . LEU   B 2  331 ? 3.731   -62.643  -53.377  1.00 61.78  ? 331 LEU   B C      1 
ATOM   5960  O  O      . LEU   B 2  331 ? 4.076   -61.769  -54.181  1.00 59.45  ? 331 LEU   B O      1 
ATOM   5961  C  CB     . LEU   B 2  331 ? 4.666   -64.893  -53.995  1.00 60.28  ? 331 LEU   B CB     1 
ATOM   5962  C  CG     . LEU   B 2  331 ? 5.970   -65.669  -54.169  1.00 58.93  ? 331 LEU   B CG     1 
ATOM   5963  C  CD1    . LEU   B 2  331 ? 5.809   -66.681  -55.279  1.00 59.53  ? 331 LEU   B CD1    1 
ATOM   5964  C  CD2    . LEU   B 2  331 ? 7.173   -64.741  -54.412  1.00 52.28  ? 331 LEU   B CD2    1 
ATOM   5965  N  N      . ASN   B 2  332 ? 2.534   -62.640  -52.804  1.00 57.03  ? 332 ASN   B N      1 
ATOM   5966  C  CA     . ASN   B 2  332 ? 1.551   -61.663  -53.234  1.00 62.22  ? 332 ASN   B CA     1 
ATOM   5967  C  C      . ASN   B 2  332 ? 1.782   -60.279  -52.620  1.00 68.41  ? 332 ASN   B C      1 
ATOM   5968  O  O      . ASN   B 2  332 ? 1.516   -59.269  -53.282  1.00 67.62  ? 332 ASN   B O      1 
ATOM   5969  C  CB     . ASN   B 2  332 ? 0.149   -62.157  -52.910  1.00 62.10  ? 332 ASN   B CB     1 
ATOM   5970  C  CG     . ASN   B 2  332 ? -0.813  -61.023  -52.733  1.00 74.15  ? 332 ASN   B CG     1 
ATOM   5971  O  OD1    . ASN   B 2  332 ? -0.850  -60.383  -51.673  1.00 76.11  ? 332 ASN   B OD1    1 
ATOM   5972  N  ND2    . ASN   B 2  332 ? -1.586  -60.735  -53.779  1.00 77.32  ? 332 ASN   B ND2    1 
ATOM   5973  N  N      . VAL   B 2  333 ? 2.264   -60.189  -51.368  1.00 66.73  ? 333 VAL   B N      1 
ATOM   5974  C  CA     . VAL   B 2  333 ? 2.450   -58.860  -50.771  1.00 68.35  ? 333 VAL   B CA     1 
ATOM   5975  C  C      . VAL   B 2  333 ? 3.655   -58.155  -51.386  1.00 65.22  ? 333 VAL   B C      1 
ATOM   5976  O  O      . VAL   B 2  333 ? 3.652   -56.922  -51.536  1.00 59.24  ? 333 VAL   B O      1 
ATOM   5977  C  CB     . VAL   B 2  333 ? 2.574   -58.924  -49.232  1.00 69.75  ? 333 VAL   B CB     1 
ATOM   5978  C  CG1    . VAL   B 2  333 ? 3.972   -59.319  -48.815  1.00 65.55  ? 333 VAL   B CG1    1 
ATOM   5979  C  CG2    . VAL   B 2  333 ? 2.190   -57.588  -48.606  1.00 59.92  ? 333 VAL   B CG2    1 
ATOM   5980  N  N      . GLN   B 2  334 ? 4.693   -58.914  -51.755  1.00 61.84  ? 334 GLN   B N      1 
ATOM   5981  C  CA     . GLN   B 2  334 ? 5.802   -58.347  -52.522  1.00 68.27  ? 334 GLN   B CA     1 
ATOM   5982  C  C      . GLN   B 2  334 ? 5.310   -57.770  -53.847  1.00 70.86  ? 334 GLN   B C      1 
ATOM   5983  O  O      . GLN   B 2  334 ? 5.385   -56.555  -54.080  1.00 69.16  ? 334 GLN   B O      1 
ATOM   5984  C  CB     . GLN   B 2  334 ? 6.888   -59.403  -52.775  1.00 63.25  ? 334 GLN   B CB     1 
ATOM   5985  C  CG     . GLN   B 2  334 ? 7.359   -60.145  -51.528  1.00 68.27  ? 334 GLN   B CG     1 
ATOM   5986  C  CD     . GLN   B 2  334 ? 8.360   -61.256  -51.844  1.00 68.01  ? 334 GLN   B CD     1 
ATOM   5987  O  OE1    . GLN   B 2  334 ? 9.319   -61.046  -52.594  1.00 66.81  ? 334 GLN   B OE1    1 
ATOM   5988  N  NE2    . GLN   B 2  334 ? 8.138   -62.447  -51.272  1.00 61.24  ? 334 GLN   B NE2    1 
ATOM   5989  N  N      . ASN   B 2  335 ? 4.805   -58.636  -54.737  1.00 72.88  ? 335 ASN   B N      1 
ATOM   5990  C  CA     . ASN   B 2  335 ? 4.376   -58.191  -56.062  1.00 72.74  ? 335 ASN   B CA     1 
ATOM   5991  C  C      . ASN   B 2  335 ? 3.224   -57.187  -56.015  1.00 70.77  ? 335 ASN   B C      1 
ATOM   5992  O  O      . ASN   B 2  335 ? 2.954   -56.541  -57.035  1.00 71.62  ? 335 ASN   B O      1 
ATOM   5993  C  CB     . ASN   B 2  335 ? 4.006   -59.400  -56.932  1.00 66.12  ? 335 ASN   B CB     1 
ATOM   5994  C  CG     . ASN   B 2  335 ? 5.131   -60.440  -56.995  1.00 74.42  ? 335 ASN   B CG     1 
ATOM   5995  O  OD1    . ASN   B 2  335 ? 6.296   -60.105  -57.247  1.00 72.02  ? 335 ASN   B OD1    1 
ATOM   5996  N  ND2    . ASN   B 2  335 ? 4.777   -61.711  -56.808  1.00 74.42  ? 335 ASN   B ND2    1 
ATOM   5997  N  N      . LYS   B 2  336 ? 2.550   -57.028  -54.871  1.00 63.46  ? 336 LYS   B N      1 
ATOM   5998  C  CA     . LYS   B 2  336 ? 1.596   -55.930  -54.734  1.00 71.17  ? 336 LYS   B CA     1 
ATOM   5999  C  C      . LYS   B 2  336 ? 2.282   -54.629  -54.335  1.00 70.88  ? 336 LYS   B C      1 
ATOM   6000  O  O      . LYS   B 2  336 ? 1.876   -53.547  -54.769  1.00 73.10  ? 336 LYS   B O      1 
ATOM   6001  C  CB     . LYS   B 2  336 ? 0.505   -56.265  -53.707  1.00 72.30  ? 336 LYS   B CB     1 
ATOM   6002  C  CG     . LYS   B 2  336 ? -0.357  -57.522  -53.981  1.00 75.59  ? 336 LYS   B CG     1 
ATOM   6003  C  CD     . LYS   B 2  336 ? -0.623  -57.832  -55.474  1.00 75.92  ? 336 LYS   B CD     1 
ATOM   6004  C  CE     . LYS   B 2  336 ? -0.820  -56.584  -56.360  1.00 79.05  ? 336 LYS   B CE     1 
ATOM   6005  N  NZ     . LYS   B 2  336 ? -0.606  -56.869  -57.827  1.00 79.80  ? 336 LYS   B NZ     1 
ATOM   6006  N  N      . ASN   B 2  337 ? 3.305   -54.707  -53.499  1.00 71.95  ? 337 ASN   B N      1 
ATOM   6007  C  CA     . ASN   B 2  337 ? 3.973   -53.530  -52.976  1.00 60.21  ? 337 ASN   B CA     1 
ATOM   6008  C  C      . ASN   B 2  337 ? 5.455   -53.599  -53.263  1.00 59.81  ? 337 ASN   B C      1 
ATOM   6009  O  O      . ASN   B 2  337 ? 6.289   -53.248  -52.425  1.00 62.17  ? 337 ASN   B O      1 
ATOM   6010  C  CB     . ASN   B 2  337 ? 3.686   -53.392  -51.493  1.00 62.87  ? 337 ASN   B CB     1 
ATOM   6011  C  CG     . ASN   B 2  337 ? 2.261   -53.712  -51.188  1.00 61.50  ? 337 ASN   B CG     1 
ATOM   6012  O  OD1    . ASN   B 2  337 ? 1.968   -54.638  -50.444  1.00 63.57  ? 337 ASN   B OD1    1 
ATOM   6013  N  ND2    . ASN   B 2  337 ? 1.355   -52.995  -51.829  1.00 61.64  ? 337 ASN   B ND2    1 
ATOM   6014  N  N      . SER   B 2  338 ? 5.776   -54.045  -54.483  1.00 57.37  ? 338 SER   B N      1 
ATOM   6015  C  CA     . SER   B 2  338 ? 7.150   -54.213  -54.930  1.00 56.51  ? 338 SER   B CA     1 
ATOM   6016  C  C      . SER   B 2  338 ? 7.931   -52.904  -54.939  1.00 55.95  ? 338 SER   B C      1 
ATOM   6017  O  O      . SER   B 2  338 ? 9.165   -52.935  -54.986  1.00 55.08  ? 338 SER   B O      1 
ATOM   6018  C  CB     . SER   B 2  338 ? 7.158   -54.834  -56.332  1.00 68.73  ? 338 SER   B CB     1 
ATOM   6019  O  OG     . SER   B 2  338 ? 7.054   -53.844  -57.358  1.00 62.37  ? 338 SER   B OG     1 
ATOM   6020  N  N      . SER   B 2  339 ? 7.249   -51.760  -54.923  1.00 52.94  ? 339 SER   B N      1 
ATOM   6021  C  CA     . SER   B 2  339 ? 7.950   -50.485  -54.817  1.00 55.85  ? 339 SER   B CA     1 
ATOM   6022  C  C      . SER   B 2  339 ? 8.787   -50.412  -53.540  1.00 60.01  ? 339 SER   B C      1 
ATOM   6023  O  O      . SER   B 2  339 ? 9.923   -49.922  -53.563  1.00 62.04  ? 339 SER   B O      1 
ATOM   6024  C  CB     . SER   B 2  339 ? 6.939   -49.334  -54.885  1.00 56.84  ? 339 SER   B CB     1 
ATOM   6025  O  OG     . SER   B 2  339 ? 7.117   -48.365  -53.858  1.00 58.05  ? 339 SER   B OG     1 
ATOM   6026  N  N      . TYR   B 2  340 ? 8.257   -50.923  -52.427  1.00 54.44  ? 340 TYR   B N      1 
ATOM   6027  C  CA     . TYR   B 2  340 ? 8.865   -50.793  -51.110  1.00 53.48  ? 340 TYR   B CA     1 
ATOM   6028  C  C      . TYR   B 2  340 ? 9.943   -51.846  -50.813  1.00 55.02  ? 340 TYR   B C      1 
ATOM   6029  O  O      . TYR   B 2  340 ? 10.371  -51.953  -49.659  1.00 55.52  ? 340 TYR   B O      1 
ATOM   6030  C  CB     . TYR   B 2  340 ? 7.778   -50.865  -50.034  1.00 54.98  ? 340 TYR   B CB     1 
ATOM   6031  C  CG     . TYR   B 2  340 ? 6.776   -49.741  -50.110  1.00 60.85  ? 340 TYR   B CG     1 
ATOM   6032  C  CD1    . TYR   B 2  340 ? 7.172   -48.425  -49.911  1.00 58.40  ? 340 TYR   B CD1    1 
ATOM   6033  C  CD2    . TYR   B 2  340 ? 5.428   -49.991  -50.393  1.00 59.60  ? 340 TYR   B CD2    1 
ATOM   6034  C  CE1    . TYR   B 2  340 ? 6.263   -47.388  -49.990  1.00 59.80  ? 340 TYR   B CE1    1 
ATOM   6035  C  CE2    . TYR   B 2  340 ? 4.508   -48.950  -50.465  1.00 53.00  ? 340 TYR   B CE2    1 
ATOM   6036  C  CZ     . TYR   B 2  340 ? 4.937   -47.656  -50.263  1.00 56.86  ? 340 TYR   B CZ     1 
ATOM   6037  O  OH     . TYR   B 2  340 ? 4.057   -46.609  -50.343  1.00 60.66  ? 340 TYR   B OH     1 
ATOM   6038  N  N      . PHE   B 2  341 ? 10.386  -52.632  -51.789  1.00 50.31  ? 341 PHE   B N      1 
ATOM   6039  C  CA     . PHE   B 2  341 ? 11.526  -53.524  -51.617  1.00 53.57  ? 341 PHE   B CA     1 
ATOM   6040  C  C      . PHE   B 2  341 ? 12.599  -53.072  -52.589  1.00 53.89  ? 341 PHE   B C      1 
ATOM   6041  O  O      . PHE   B 2  341 ? 12.289  -52.658  -53.708  1.00 58.35  ? 341 PHE   B O      1 
ATOM   6042  C  CB     . PHE   B 2  341 ? 11.157  -55.009  -51.855  1.00 42.91  ? 341 PHE   B CB     1 
ATOM   6043  C  CG     . PHE   B 2  341 ? 10.106  -55.524  -50.914  1.00 40.02  ? 341 PHE   B CG     1 
ATOM   6044  C  CD1    . PHE   B 2  341 ? 8.771   -55.208  -51.105  1.00 47.69  ? 341 PHE   B CD1    1 
ATOM   6045  C  CD2    . PHE   B 2  341 ? 10.438  -56.318  -49.841  1.00 40.19  ? 341 PHE   B CD2    1 
ATOM   6046  C  CE1    . PHE   B 2  341 ? 7.787   -55.675  -50.241  1.00 48.57  ? 341 PHE   B CE1    1 
ATOM   6047  C  CE2    . PHE   B 2  341 ? 9.453   -56.783  -48.961  1.00 39.95  ? 341 PHE   B CE2    1 
ATOM   6048  C  CZ     . PHE   B 2  341 ? 8.133   -56.454  -49.159  1.00 41.94  ? 341 PHE   B CZ     1 
ATOM   6049  N  N      . VAL   B 2  342 ? 13.859  -53.097  -52.167  1.00 48.20  ? 342 VAL   B N      1 
ATOM   6050  C  CA     . VAL   B 2  342 ? 14.872  -52.575  -53.069  1.00 57.40  ? 342 VAL   B CA     1 
ATOM   6051  C  C      . VAL   B 2  342 ? 14.978  -53.502  -54.273  1.00 58.01  ? 342 VAL   B C      1 
ATOM   6052  O  O      . VAL   B 2  342 ? 14.828  -54.729  -54.160  1.00 55.24  ? 342 VAL   B O      1 
ATOM   6053  C  CB     . VAL   B 2  342 ? 16.229  -52.355  -52.367  1.00 53.50  ? 342 VAL   B CB     1 
ATOM   6054  C  CG1    . VAL   B 2  342 ? 16.215  -51.040  -51.614  1.00 47.16  ? 342 VAL   B CG1    1 
ATOM   6055  C  CG2    . VAL   B 2  342 ? 16.606  -53.527  -51.445  1.00 46.76  ? 342 VAL   B CG2    1 
ATOM   6056  N  N      . GLU   B 2  343 ? 15.151  -52.906  -55.454  1.00 61.30  ? 343 GLU   B N      1 
ATOM   6057  C  CA     . GLU   B 2  343 ? 15.410  -53.719  -56.630  1.00 57.40  ? 343 GLU   B CA     1 
ATOM   6058  C  C      . GLU   B 2  343 ? 16.798  -54.329  -56.599  1.00 55.79  ? 343 GLU   B C      1 
ATOM   6059  O  O      . GLU   B 2  343 ? 17.010  -55.381  -57.211  1.00 60.47  ? 343 GLU   B O      1 
ATOM   6060  C  CB     . GLU   B 2  343 ? 15.239  -52.905  -57.922  1.00 63.38  ? 343 GLU   B CB     1 
ATOM   6061  C  CG     . GLU   B 2  343 ? 15.675  -51.438  -57.893  1.00 67.10  ? 343 GLU   B CG     1 
ATOM   6062  C  CD     . GLU   B 2  343 ? 15.061  -50.632  -59.052  1.00 90.97  ? 343 GLU   B CD     1 
ATOM   6063  O  OE1    . GLU   B 2  343 ? 13.893  -50.914  -59.448  1.00 84.15  ? 343 GLU   B OE1    1 
ATOM   6064  O  OE2    . GLU   B 2  343 ? 15.755  -49.726  -59.582  1.00 95.65  ? 343 GLU   B OE2    1 
ATOM   6065  N  N      . TRP   B 2  344 ? 17.748  -53.716  -55.900  1.00 53.56  ? 344 TRP   B N      1 
ATOM   6066  C  CA     . TRP   B 2  344 ? 19.143  -54.087  -56.075  1.00 47.85  ? 344 TRP   B CA     1 
ATOM   6067  C  C      . TRP   B 2  344 ? 19.616  -55.151  -55.094  1.00 52.54  ? 344 TRP   B C      1 
ATOM   6068  O  O      . TRP   B 2  344 ? 20.819  -55.452  -55.050  1.00 52.22  ? 344 TRP   B O      1 
ATOM   6069  C  CB     . TRP   B 2  344 ? 20.025  -52.855  -55.990  1.00 48.97  ? 344 TRP   B CB     1 
ATOM   6070  C  CG     . TRP   B 2  344 ? 19.652  -51.849  -54.973  1.00 51.83  ? 344 TRP   B CG     1 
ATOM   6071  C  CD1    . TRP   B 2  344 ? 18.839  -50.772  -55.150  1.00 55.12  ? 344 TRP   B CD1    1 
ATOM   6072  C  CD2    . TRP   B 2  344 ? 20.134  -51.773  -53.622  1.00 54.22  ? 344 TRP   B CD2    1 
ATOM   6073  N  NE1    . TRP   B 2  344 ? 18.765  -50.041  -53.986  1.00 53.90  ? 344 TRP   B NE1    1 
ATOM   6074  C  CE2    . TRP   B 2  344 ? 19.553  -50.635  -53.036  1.00 52.40  ? 344 TRP   B CE2    1 
ATOM   6075  C  CE3    . TRP   B 2  344 ? 20.992  -52.567  -52.849  1.00 52.69  ? 344 TRP   B CE3    1 
ATOM   6076  C  CZ2    . TRP   B 2  344 ? 19.807  -50.267  -51.719  1.00 48.15  ? 344 TRP   B CZ2    1 
ATOM   6077  C  CZ3    . TRP   B 2  344 ? 21.238  -52.202  -51.544  1.00 48.76  ? 344 TRP   B CZ3    1 
ATOM   6078  C  CH2    . TRP   B 2  344 ? 20.653  -51.059  -50.995  1.00 49.80  ? 344 TRP   B CH2    1 
ATOM   6079  N  N      . ILE   B 2  345 ? 18.708  -55.724  -54.311  1.00 50.71  ? 345 ILE   B N      1 
ATOM   6080  C  CA     . ILE   B 2  345 ? 18.953  -56.999  -53.649  1.00 42.04  ? 345 ILE   B CA     1 
ATOM   6081  C  C      . ILE   B 2  345 ? 17.866  -57.958  -54.118  1.00 45.67  ? 345 ILE   B C      1 
ATOM   6082  O  O      . ILE   B 2  345 ? 16.793  -58.026  -53.497  1.00 49.78  ? 345 ILE   B O      1 
ATOM   6083  C  CB     . ILE   B 2  345 ? 18.939  -56.869  -52.124  1.00 42.14  ? 345 ILE   B CB     1 
ATOM   6084  C  CG1    . ILE   B 2  345 ? 19.925  -55.817  -51.651  1.00 41.94  ? 345 ILE   B CG1    1 
ATOM   6085  C  CG2    . ILE   B 2  345 ? 19.237  -58.220  -51.467  1.00 42.80  ? 345 ILE   B CG2    1 
ATOM   6086  C  CD1    . ILE   B 2  345 ? 19.859  -55.643  -50.153  1.00 41.54  ? 345 ILE   B CD1    1 
ATOM   6087  N  N      . PRO   B 2  346 ? 18.086  -58.700  -55.198  1.00 44.40  ? 346 PRO   B N      1 
ATOM   6088  C  CA     . PRO   B 2  346 ? 17.065  -59.637  -55.675  1.00 38.68  ? 346 PRO   B CA     1 
ATOM   6089  C  C      . PRO   B 2  346 ? 16.596  -60.561  -54.566  1.00 40.96  ? 346 PRO   B C      1 
ATOM   6090  O  O      . PRO   B 2  346 ? 17.381  -60.986  -53.719  1.00 40.35  ? 346 PRO   B O      1 
ATOM   6091  C  CB     . PRO   B 2  346 ? 17.791  -60.415  -56.779  1.00 35.74  ? 346 PRO   B CB     1 
ATOM   6092  C  CG     . PRO   B 2  346 ? 18.821  -59.461  -57.296  1.00 43.25  ? 346 PRO   B CG     1 
ATOM   6093  C  CD     . PRO   B 2  346 ? 19.283  -58.694  -56.062  1.00 48.87  ? 346 PRO   B CD     1 
ATOM   6094  N  N      . ASN   B 2  347 ? 15.294  -60.852  -54.569  1.00 42.25  ? 347 ASN   B N      1 
ATOM   6095  C  CA     . ASN   B 2  347 ? 14.705  -61.910  -53.750  1.00 39.58  ? 347 ASN   B CA     1 
ATOM   6096  C  C      . ASN   B 2  347 ? 15.074  -61.765  -52.274  1.00 41.67  ? 347 ASN   B C      1 
ATOM   6097  O  O      . ASN   B 2  347 ? 15.506  -62.717  -51.619  1.00 42.45  ? 347 ASN   B O      1 
ATOM   6098  C  CB     . ASN   B 2  347 ? 15.111  -63.272  -54.310  1.00 40.25  ? 347 ASN   B CB     1 
ATOM   6099  C  CG     . ASN   B 2  347 ? 15.061  -63.297  -55.843  1.00 45.66  ? 347 ASN   B CG     1 
ATOM   6100  O  OD1    . ASN   B 2  347 ? 16.078  -63.534  -56.521  1.00 49.24  ? 347 ASN   B OD1    1 
ATOM   6101  N  ND2    . ASN   B 2  347 ? 13.883  -63.026  -56.395  1.00 42.53  ? 347 ASN   B ND2    1 
ATOM   6102  N  N      . ASN   B 2  348 ? 14.847  -60.559  -51.742  1.00 42.37  ? 348 ASN   B N      1 
ATOM   6103  C  CA     . ASN   B 2  348 ? 15.293  -60.151  -50.413  1.00 42.02  ? 348 ASN   B CA     1 
ATOM   6104  C  C      . ASN   B 2  348 ? 14.324  -60.519  -49.294  1.00 42.19  ? 348 ASN   B C      1 
ATOM   6105  O  O      . ASN   B 2  348 ? 14.603  -60.194  -48.135  1.00 42.44  ? 348 ASN   B O      1 
ATOM   6106  C  CB     . ASN   B 2  348 ? 15.564  -58.633  -50.387  1.00 41.46  ? 348 ASN   B CB     1 
ATOM   6107  C  CG     . ASN   B 2  348 ? 14.330  -57.796  -50.741  1.00 48.72  ? 348 ASN   B CG     1 
ATOM   6108  O  OD1    . ASN   B 2  348 ? 13.263  -58.338  -51.001  1.00 44.20  ? 348 ASN   B OD1    1 
ATOM   6109  N  ND2    . ASN   B 2  348 ? 14.492  -56.466  -50.793  1.00 49.47  ? 348 ASN   B ND2    1 
ATOM   6110  N  N      . VAL   B 2  349 ? 13.209  -61.183  -49.605  1.00 38.95  ? 349 VAL   B N      1 
ATOM   6111  C  CA     . VAL   B 2  349 ? 12.250  -61.658  -48.614  1.00 38.62  ? 349 VAL   B CA     1 
ATOM   6112  C  C      . VAL   B 2  349 ? 12.346  -63.174  -48.530  1.00 39.53  ? 349 VAL   B C      1 
ATOM   6113  O  O      . VAL   B 2  349 ? 12.110  -63.871  -49.520  1.00 40.29  ? 349 VAL   B O      1 
ATOM   6114  C  CB     . VAL   B 2  349 ? 10.818  -61.245  -48.961  1.00 42.00  ? 349 VAL   B CB     1 
ATOM   6115  C  CG1    . VAL   B 2  349 ? 9.857   -61.737  -47.867  1.00 41.90  ? 349 VAL   B CG1    1 
ATOM   6116  C  CG2    . VAL   B 2  349 ? 10.737  -59.745  -49.157  1.00 39.84  ? 349 VAL   B CG2    1 
ATOM   6117  N  N      . LYS   B 2  350 ? 12.667  -63.681  -47.351  1.00 35.36  ? 350 LYS   B N      1 
ATOM   6118  C  CA     . LYS   B 2  350 ? 12.789  -65.106  -47.098  1.00 41.33  ? 350 LYS   B CA     1 
ATOM   6119  C  C      . LYS   B 2  350 ? 11.808  -65.486  -45.998  1.00 42.08  ? 350 LYS   B C      1 
ATOM   6120  O  O      . LYS   B 2  350 ? 11.489  -64.670  -45.135  1.00 46.48  ? 350 LYS   B O      1 
ATOM   6121  C  CB     . LYS   B 2  350 ? 14.223  -65.479  -46.680  1.00 39.95  ? 350 LYS   B CB     1 
ATOM   6122  C  CG     . LYS   B 2  350 ? 15.094  -66.154  -47.739  1.00 46.46  ? 350 LYS   B CG     1 
ATOM   6123  C  CD     . LYS   B 2  350 ? 14.780  -65.746  -49.169  1.00 49.76  ? 350 LYS   B CD     1 
ATOM   6124  C  CE     . LYS   B 2  350 ? 15.879  -66.224  -50.118  1.00 51.14  ? 350 LYS   B CE     1 
ATOM   6125  N  NZ     . LYS   B 2  350 ? 15.355  -66.643  -51.441  1.00 56.97  ? 350 LYS   B NZ     1 
ATOM   6126  N  N      . THR   B 2  351 ? 11.317  -66.721  -46.036  1.00 42.51  ? 351 THR   B N      1 
ATOM   6127  C  CA     . THR   B 2  351 ? 10.242  -67.154  -45.151  1.00 40.92  ? 351 THR   B CA     1 
ATOM   6128  C  C      . THR   B 2  351 ? 10.555  -68.549  -44.625  1.00 43.52  ? 351 THR   B C      1 
ATOM   6129  O  O      . THR   B 2  351 ? 11.199  -69.353  -45.303  1.00 48.76  ? 351 THR   B O      1 
ATOM   6130  C  CB     . THR   B 2  351 ? 8.902   -67.157  -45.892  1.00 42.75  ? 351 THR   B CB     1 
ATOM   6131  O  OG1    . THR   B 2  351 ? 8.730   -65.926  -46.604  1.00 42.02  ? 351 THR   B OG1    1 
ATOM   6132  C  CG2    . THR   B 2  351 ? 7.751   -67.334  -44.931  1.00 49.02  ? 351 THR   B CG2    1 
ATOM   6133  N  N      . ALA   B 2  352 ? 10.107  -68.832  -43.409  1.00 40.27  ? 352 ALA   B N      1 
ATOM   6134  C  CA     . ALA   B 2  352 ? 10.331  -70.125  -42.780  1.00 42.05  ? 352 ALA   B CA     1 
ATOM   6135  C  C      . ALA   B 2  352 ? 9.065   -70.508  -42.031  1.00 50.19  ? 352 ALA   B C      1 
ATOM   6136  O  O      . ALA   B 2  352 ? 8.225   -69.657  -41.739  1.00 49.67  ? 352 ALA   B O      1 
ATOM   6137  C  CB     . ALA   B 2  352 ? 11.528  -70.094  -41.821  1.00 43.89  ? 352 ALA   B CB     1 
ATOM   6138  N  N      . VAL   B 2  353 ? 8.918   -71.793  -41.717  1.00 50.16  ? 353 VAL   B N      1 
ATOM   6139  C  CA     . VAL   B 2  353 ? 7.739   -72.258  -40.995  1.00 45.41  ? 353 VAL   B CA     1 
ATOM   6140  C  C      . VAL   B 2  353 ? 8.153   -73.276  -39.942  1.00 45.26  ? 353 VAL   B C      1 
ATOM   6141  O  O      . VAL   B 2  353 ? 9.057   -74.084  -40.158  1.00 55.72  ? 353 VAL   B O      1 
ATOM   6142  C  CB     . VAL   B 2  353 ? 6.669   -72.847  -41.937  1.00 46.61  ? 353 VAL   B CB     1 
ATOM   6143  C  CG1    . VAL   B 2  353 ? 5.391   -73.140  -41.157  1.00 53.66  ? 353 VAL   B CG1    1 
ATOM   6144  C  CG2    . VAL   B 2  353 ? 6.355   -71.879  -43.048  1.00 52.61  ? 353 VAL   B CG2    1 
ATOM   6145  N  N      . CYS   B 2  354 ? 7.491   -73.223  -38.798  1.00 43.94  ? 354 CYS   B N      1 
ATOM   6146  C  CA     . CYS   B 2  354 ? 7.723   -74.128  -37.688  1.00 51.51  ? 354 CYS   B CA     1 
ATOM   6147  C  C      . CYS   B 2  354 ? 6.369   -74.635  -37.200  1.00 56.37  ? 354 CYS   B C      1 
ATOM   6148  O  O      . CYS   B 2  354 ? 5.418   -73.857  -37.071  1.00 55.24  ? 354 CYS   B O      1 
ATOM   6149  C  CB     . CYS   B 2  354 ? 8.498   -73.407  -36.573  1.00 47.53  ? 354 CYS   B CB     1 
ATOM   6150  S  SG     . CYS   B 2  354 ? 8.559   -74.262  -34.996  1.00 58.18  ? 354 CYS   B SG     1 
ATOM   6151  N  N      . ASP   B 2  355 ? 6.279   -75.937  -36.940  1.00 60.33  ? 355 ASP   B N      1 
ATOM   6152  C  CA     . ASP   B 2  355 ? 4.985   -76.527  -36.608  1.00 56.83  ? 355 ASP   B CA     1 
ATOM   6153  C  C      . ASP   B 2  355 ? 4.469   -76.043  -35.262  1.00 57.17  ? 355 ASP   B C      1 
ATOM   6154  O  O      . ASP   B 2  355 ? 3.286   -75.705  -35.138  1.00 60.19  ? 355 ASP   B O      1 
ATOM   6155  C  CB     . ASP   B 2  355 ? 5.089   -78.047  -36.639  1.00 56.46  ? 355 ASP   B CB     1 
ATOM   6156  C  CG     . ASP   B 2  355 ? 5.476   -78.556  -38.011  1.00 66.72  ? 355 ASP   B CG     1 
ATOM   6157  O  OD1    . ASP   B 2  355 ? 4.893   -78.063  -39.005  1.00 60.22  ? 355 ASP   B OD1    1 
ATOM   6158  O  OD2    . ASP   B 2  355 ? 6.383   -79.416  -38.099  1.00 74.09  ? 355 ASP   B OD2    1 
ATOM   6159  N  N      . ILE   B 2  356 ? 5.329   -75.975  -34.249  1.00 55.54  ? 356 ILE   B N      1 
ATOM   6160  C  CA     . ILE   B 2  356 ? 4.869   -75.606  -32.908  1.00 54.04  ? 356 ILE   B CA     1 
ATOM   6161  C  C      . ILE   B 2  356 ? 4.463   -74.135  -32.856  1.00 54.12  ? 356 ILE   B C      1 
ATOM   6162  O  O      . ILE   B 2  356 ? 5.318   -73.257  -33.033  1.00 52.88  ? 356 ILE   B O      1 
ATOM   6163  C  CB     . ILE   B 2  356 ? 5.938   -75.895  -31.843  1.00 54.70  ? 356 ILE   B CB     1 
ATOM   6164  C  CG1    . ILE   B 2  356 ? 6.196   -77.402  -31.691  1.00 56.18  ? 356 ILE   B CG1    1 
ATOM   6165  C  CG2    . ILE   B 2  356 ? 5.534   -75.275  -30.517  1.00 57.61  ? 356 ILE   B CG2    1 
ATOM   6166  C  CD1    . ILE   B 2  356 ? 7.495   -77.879  -32.294  1.00 56.86  ? 356 ILE   B CD1    1 
ATOM   6167  N  N      . PRO   B 2  357 ? 3.199   -73.808  -32.586  1.00 58.86  ? 357 PRO   B N      1 
ATOM   6168  C  CA     . PRO   B 2  357 ? 2.838   -72.410  -32.354  1.00 55.72  ? 357 PRO   B CA     1 
ATOM   6169  C  C      . PRO   B 2  357 ? 3.230   -72.003  -30.948  1.00 56.79  ? 357 PRO   B C      1 
ATOM   6170  O  O      . PRO   B 2  357 ? 3.512   -72.864  -30.101  1.00 61.20  ? 357 PRO   B O      1 
ATOM   6171  C  CB     . PRO   B 2  357 ? 1.309   -72.397  -32.528  1.00 53.46  ? 357 PRO   B CB     1 
ATOM   6172  C  CG     . PRO   B 2  357 ? 0.868   -73.828  -32.295  1.00 56.06  ? 357 PRO   B CG     1 
ATOM   6173  C  CD     . PRO   B 2  357 ? 2.108   -74.704  -32.163  1.00 58.32  ? 357 PRO   B CD     1 
ATOM   6174  N  N      . PRO   B 2  358 ? 3.287   -70.709  -30.662  1.00 55.71  ? 358 PRO   B N      1 
ATOM   6175  C  CA     . PRO   B 2  358 ? 3.498   -70.277  -29.283  1.00 54.84  ? 358 PRO   B CA     1 
ATOM   6176  C  C      . PRO   B 2  358 ? 2.258   -70.536  -28.435  1.00 57.98  ? 358 PRO   B C      1 
ATOM   6177  O  O      . PRO   B 2  358 ? 1.151   -70.725  -28.940  1.00 57.39  ? 358 PRO   B O      1 
ATOM   6178  C  CB     . PRO   B 2  358 ? 3.777   -68.782  -29.432  1.00 50.83  ? 358 PRO   B CB     1 
ATOM   6179  C  CG     . PRO   B 2  358 ? 3.038   -68.403  -30.687  1.00 45.48  ? 358 PRO   B CG     1 
ATOM   6180  C  CD     . PRO   B 2  358 ? 3.181   -69.569  -31.590  1.00 54.52  ? 358 PRO   B CD     1 
ATOM   6181  N  N      . ARG   B 2  359 ? 2.460   -70.539  -27.119  1.00 64.39  ? 359 ARG   B N      1 
ATOM   6182  C  CA     . ARG   B 2  359 ? 1.354   -70.749  -26.192  1.00 67.64  ? 359 ARG   B CA     1 
ATOM   6183  C  C      . ARG   B 2  359 ? 0.234   -69.740  -26.427  1.00 66.60  ? 359 ARG   B C      1 
ATOM   6184  O  O      . ARG   B 2  359 ? 0.473   -68.550  -26.640  1.00 59.89  ? 359 ARG   B O      1 
ATOM   6185  C  CB     . ARG   B 2  359 ? 1.837   -70.641  -24.746  1.00 69.54  ? 359 ARG   B CB     1 
ATOM   6186  C  CG     . ARG   B 2  359 ? 0.880   -69.875  -23.846  1.00 67.08  ? 359 ARG   B CG     1 
ATOM   6187  C  CD     . ARG   B 2  359 ? 0.997   -70.341  -22.406  1.00 74.84  ? 359 ARG   B CD     1 
ATOM   6188  N  NE     . ARG   B 2  359 ? 0.692   -71.762  -22.284  1.00 82.20  ? 359 ARG   B NE     1 
ATOM   6189  C  CZ     . ARG   B 2  359 ? 0.670   -72.436  -21.141  1.00 85.51  ? 359 ARG   B CZ     1 
ATOM   6190  N  NH1    . ARG   B 2  359 ? 0.913   -71.842  -19.983  1.00 82.34  ? 359 ARG   B NH1    1 
ATOM   6191  N  NH2    . ARG   B 2  359 ? 0.399   -73.738  -21.161  1.00 88.36  ? 359 ARG   B NH2    1 
ATOM   6192  N  N      . GLY   B 2  360 ? -0.999  -70.221  -26.370  1.00 66.76  ? 360 GLY   B N      1 
ATOM   6193  C  CA     . GLY   B 2  360 ? -2.137  -69.358  -26.443  1.00 64.54  ? 360 GLY   B CA     1 
ATOM   6194  C  C      . GLY   B 2  360 ? -2.699  -69.152  -27.828  1.00 71.55  ? 360 GLY   B C      1 
ATOM   6195  O  O      . GLY   B 2  360 ? -3.902  -68.896  -27.954  1.00 80.78  ? 360 GLY   B O      1 
ATOM   6196  N  N      . LEU   B 2  361 ? -1.878  -69.255  -28.869  1.00 69.43  ? 361 LEU   B N      1 
ATOM   6197  C  CA     . LEU   B 2  361 ? -2.315  -68.992  -30.233  1.00 63.81  ? 361 LEU   B CA     1 
ATOM   6198  C  C      . LEU   B 2  361 ? -2.194  -70.260  -31.062  1.00 63.07  ? 361 LEU   B C      1 
ATOM   6199  O  O      . LEU   B 2  361 ? -1.339  -71.110  -30.802  1.00 64.99  ? 361 LEU   B O      1 
ATOM   6200  C  CB     . LEU   B 2  361 ? -1.495  -67.876  -30.862  1.00 61.29  ? 361 LEU   B CB     1 
ATOM   6201  C  CG     . LEU   B 2  361 ? -1.769  -66.500  -30.266  1.00 60.91  ? 361 LEU   B CG     1 
ATOM   6202  C  CD1    . LEU   B 2  361 ? -0.526  -65.646  -30.335  1.00 61.42  ? 361 LEU   B CD1    1 
ATOM   6203  C  CD2    . LEU   B 2  361 ? -2.903  -65.820  -31.011  1.00 67.92  ? 361 LEU   B CD2    1 
ATOM   6204  N  N      . LYS   B 2  362 ? -3.072  -70.393  -32.050  1.00 63.85  ? 362 LYS   B N      1 
ATOM   6205  C  CA     . LYS   B 2  362 ? -3.008  -71.540  -32.946  1.00 67.20  ? 362 LYS   B CA     1 
ATOM   6206  C  C      . LYS   B 2  362 ? -2.132  -71.282  -34.158  1.00 61.16  ? 362 LYS   B C      1 
ATOM   6207  O  O      . LYS   B 2  362 ? -1.654  -72.235  -34.785  1.00 59.68  ? 362 LYS   B O      1 
ATOM   6208  C  CB     . LYS   B 2  362 ? -4.414  -71.932  -33.421  1.00 66.77  ? 362 LYS   B CB     1 
ATOM   6209  C  CG     . LYS   B 2  362 ? -4.985  -73.162  -32.733  1.00 64.06  ? 362 LYS   B CG     1 
ATOM   6210  C  CD     . LYS   B 2  362 ? -6.179  -73.718  -33.495  1.00 75.47  ? 362 LYS   B CD     1 
ATOM   6211  C  CE     . LYS   B 2  362 ? -7.266  -74.159  -32.533  1.00 76.43  ? 362 LYS   B CE     1 
ATOM   6212  N  NZ     . LYS   B 2  362 ? -6.652  -74.785  -31.330  1.00 71.98  ? 362 LYS   B NZ     1 
ATOM   6213  N  N      . MET   B 2  363 ? -1.925  -70.016  -34.498  1.00 60.48  ? 363 MET   B N      1 
ATOM   6214  C  CA     . MET   B 2  363 ? -1.155  -69.648  -35.671  1.00 62.11  ? 363 MET   B CA     1 
ATOM   6215  C  C      . MET   B 2  363 ? -0.641  -68.224  -35.531  1.00 56.69  ? 363 MET   B C      1 
ATOM   6216  O  O      . MET   B 2  363 ? -1.378  -67.332  -35.104  1.00 62.74  ? 363 MET   B O      1 
ATOM   6217  C  CB     . MET   B 2  363 ? -1.985  -69.810  -36.940  1.00 63.50  ? 363 MET   B CB     1 
ATOM   6218  C  CG     . MET   B 2  363 ? -1.887  -71.212  -37.507  1.00 62.74  ? 363 MET   B CG     1 
ATOM   6219  S  SD     . MET   B 2  363 ? -2.448  -71.139  -39.204  1.00 76.67  ? 363 MET   B SD     1 
ATOM   6220  C  CE     . MET   B 2  363 ? -3.312  -69.573  -39.156  1.00 61.00  ? 363 MET   B CE     1 
ATOM   6221  N  N      . SER   B 2  364 ? 0.624   -68.020  -35.894  1.00 49.68  ? 364 SER   B N      1 
ATOM   6222  C  CA     . SER   B 2  364 ? 1.259   -66.735  -35.655  1.00 50.93  ? 364 SER   B CA     1 
ATOM   6223  C  C      . SER   B 2  364 ? 2.346   -66.453  -36.685  1.00 50.32  ? 364 SER   B C      1 
ATOM   6224  O  O      . SER   B 2  364 ? 2.976   -67.363  -37.231  1.00 53.12  ? 364 SER   B O      1 
ATOM   6225  C  CB     . SER   B 2  364 ? 1.841   -66.669  -34.237  1.00 59.89  ? 364 SER   B CB     1 
ATOM   6226  O  OG     . SER   B 2  364 ? 2.726   -67.744  -33.979  1.00 61.23  ? 364 SER   B OG     1 
ATOM   6227  N  N      . ALA   B 2  365 ? 2.555   -65.166  -36.934  1.00 47.78  ? 365 ALA   B N      1 
ATOM   6228  C  CA     . ALA   B 2  365 ? 3.541   -64.673  -37.882  1.00 44.37  ? 365 ALA   B CA     1 
ATOM   6229  C  C      . ALA   B 2  365 ? 4.437   -63.655  -37.183  1.00 50.88  ? 365 ALA   B C      1 
ATOM   6230  O  O      . ALA   B 2  365 ? 3.936   -62.650  -36.658  1.00 53.55  ? 365 ALA   B O      1 
ATOM   6231  C  CB     . ALA   B 2  365 ? 2.844   -64.035  -39.079  1.00 46.64  ? 365 ALA   B CB     1 
ATOM   6232  N  N      . THR   B 2  366 ? 5.753   -63.902  -37.172  1.00 42.39  ? 366 THR   B N      1 
ATOM   6233  C  CA     . THR   B 2  366 ? 6.725   -62.921  -36.694  1.00 45.15  ? 366 THR   B CA     1 
ATOM   6234  C  C      . THR   B 2  366 ? 7.510   -62.327  -37.860  1.00 45.66  ? 366 THR   B C      1 
ATOM   6235  O  O      . THR   B 2  366 ? 7.977   -63.056  -38.738  1.00 46.88  ? 366 THR   B O      1 
ATOM   6236  C  CB     . THR   B 2  366 ? 7.702   -63.513  -35.669  1.00 40.33  ? 366 THR   B CB     1 
ATOM   6237  O  OG1    . THR   B 2  366 ? 6.980   -64.114  -34.589  1.00 44.47  ? 366 THR   B OG1    1 
ATOM   6238  C  CG2    . THR   B 2  366 ? 8.547   -62.409  -35.086  1.00 45.18  ? 366 THR   B CG2    1 
ATOM   6239  N  N      . PHE   B 2  367 ? 7.664   -61.001  -37.854  1.00 41.29  ? 367 PHE   B N      1 
ATOM   6240  C  CA     . PHE   B 2  367 ? 8.266   -60.248  -38.947  1.00 39.46  ? 367 PHE   B CA     1 
ATOM   6241  C  C      . PHE   B 2  367 ? 9.578   -59.616  -38.494  1.00 43.02  ? 367 PHE   B C      1 
ATOM   6242  O  O      . PHE   B 2  367 ? 9.623   -58.999  -37.431  1.00 47.18  ? 367 PHE   B O      1 
ATOM   6243  C  CB     . PHE   B 2  367 ? 7.294   -59.173  -39.410  1.00 44.65  ? 367 PHE   B CB     1 
ATOM   6244  C  CG     . PHE   B 2  367 ? 7.893   -58.149  -40.306  1.00 41.32  ? 367 PHE   B CG     1 
ATOM   6245  C  CD1    . PHE   B 2  367 ? 7.977   -58.367  -41.655  1.00 42.19  ? 367 PHE   B CD1    1 
ATOM   6246  C  CD2    . PHE   B 2  367 ? 8.325   -56.948  -39.807  1.00 45.20  ? 367 PHE   B CD2    1 
ATOM   6247  C  CE1    . PHE   B 2  367 ? 8.503   -57.417  -42.495  1.00 43.76  ? 367 PHE   B CE1    1 
ATOM   6248  C  CE2    . PHE   B 2  367 ? 8.865   -55.989  -40.655  1.00 45.91  ? 367 PHE   B CE2    1 
ATOM   6249  C  CZ     . PHE   B 2  367 ? 8.950   -56.228  -41.996  1.00 41.39  ? 367 PHE   B CZ     1 
ATOM   6250  N  N      . ILE   B 2  368 ? 10.640  -59.757  -39.297  1.00 37.11  ? 368 ILE   B N      1 
ATOM   6251  C  CA     . ILE   B 2  368 ? 11.932  -59.120  -39.037  1.00 33.86  ? 368 ILE   B CA     1 
ATOM   6252  C  C      . ILE   B 2  368 ? 12.314  -58.308  -40.267  1.00 37.33  ? 368 ILE   B C      1 
ATOM   6253  O  O      . ILE   B 2  368 ? 12.742  -58.878  -41.280  1.00 40.92  ? 368 ILE   B O      1 
ATOM   6254  C  CB     . ILE   B 2  368 ? 13.046  -60.129  -38.713  1.00 36.75  ? 368 ILE   B CB     1 
ATOM   6255  C  CG1    . ILE   B 2  368 ? 12.572  -61.218  -37.766  1.00 36.92  ? 368 ILE   B CG1    1 
ATOM   6256  C  CG2    . ILE   B 2  368 ? 14.247  -59.406  -38.094  1.00 34.11  ? 368 ILE   B CG2    1 
ATOM   6257  C  CD1    . ILE   B 2  368 ? 13.705  -62.084  -37.256  1.00 32.67  ? 368 ILE   B CD1    1 
ATOM   6258  N  N      . GLY   B 2  369 ? 12.206  -56.987  -40.174  1.00 33.90  ? 369 GLY   B N      1 
ATOM   6259  C  CA     . GLY   B 2  369 ? 12.520  -56.124  -41.298  1.00 37.29  ? 369 GLY   B CA     1 
ATOM   6260  C  C      . GLY   B 2  369 ? 13.736  -55.222  -41.117  1.00 38.64  ? 369 GLY   B C      1 
ATOM   6261  O  O      . GLY   B 2  369 ? 13.837  -54.483  -40.131  1.00 36.27  ? 369 GLY   B O      1 
ATOM   6262  N  N      . ASN   B 2  370 ? 14.673  -55.279  -42.074  1.00 36.41  ? 370 ASN   B N      1 
ATOM   6263  C  CA     . ASN   B 2  370 ? 15.731  -54.276  -42.183  1.00 31.71  ? 370 ASN   B CA     1 
ATOM   6264  C  C      . ASN   B 2  370 ? 15.288  -53.192  -43.152  1.00 31.26  ? 370 ASN   B C      1 
ATOM   6265  O  O      . ASN   B 2  370 ? 15.708  -53.132  -44.298  1.00 41.12  ? 370 ASN   B O      1 
ATOM   6266  C  CB     . ASN   B 2  370 ? 17.032  -54.901  -42.641  1.00 33.87  ? 370 ASN   B CB     1 
ATOM   6267  C  CG     . ASN   B 2  370 ? 18.200  -54.010  -42.374  1.00 36.54  ? 370 ASN   B CG     1 
ATOM   6268  O  OD1    . ASN   B 2  370 ? 18.030  -52.835  -42.035  1.00 38.13  ? 370 ASN   B OD1    1 
ATOM   6269  N  ND2    . ASN   B 2  370 ? 19.409  -54.551  -42.516  1.00 39.10  ? 370 ASN   B ND2    1 
ATOM   6270  N  N      . SER   B 2  371 ? 14.423  -52.322  -42.669  1.00 35.01  ? 371 SER   B N      1 
ATOM   6271  C  CA     . SER   B 2  371 ? 13.892  -51.215  -43.440  1.00 34.47  ? 371 SER   B CA     1 
ATOM   6272  C  C      . SER   B 2  371 ? 14.710  -49.955  -43.220  1.00 38.52  ? 371 SER   B C      1 
ATOM   6273  O  O      . SER   B 2  371 ? 15.098  -49.647  -42.089  1.00 43.48  ? 371 SER   B O      1 
ATOM   6274  C  CB     . SER   B 2  371 ? 12.454  -50.929  -43.031  1.00 35.86  ? 371 SER   B CB     1 
ATOM   6275  O  OG     . SER   B 2  371 ? 12.109  -49.641  -43.471  1.00 38.03  ? 371 SER   B OG     1 
ATOM   6276  N  N      . THR   B 2  372 ? 14.931  -49.203  -44.295  1.00 38.82  ? 372 THR   B N      1 
ATOM   6277  C  CA     . THR   B 2  372 ? 15.479  -47.867  -44.128  1.00 39.16  ? 372 THR   B CA     1 
ATOM   6278  C  C      . THR   B 2  372 ? 14.500  -46.924  -43.437  1.00 41.77  ? 372 THR   B C      1 
ATOM   6279  O  O      . THR   B 2  372 ? 14.849  -45.772  -43.186  1.00 49.27  ? 372 THR   B O      1 
ATOM   6280  C  CB     . THR   B 2  372 ? 15.889  -47.255  -45.477  1.00 44.69  ? 372 THR   B CB     1 
ATOM   6281  O  OG1    . THR   B 2  372 ? 14.716  -46.888  -46.208  1.00 47.17  ? 372 THR   B OG1    1 
ATOM   6282  C  CG2    . THR   B 2  372 ? 16.730  -48.220  -46.307  1.00 44.06  ? 372 THR   B CG2    1 
ATOM   6283  N  N      . ALA   B 2  373 ? 13.294  -47.355  -43.117  1.00 37.54  ? 373 ALA   B N      1 
ATOM   6284  C  CA     . ALA   B 2  373 ? 12.418  -46.447  -42.406  1.00 38.94  ? 373 ALA   B CA     1 
ATOM   6285  C  C      . ALA   B 2  373 ? 12.751  -46.369  -40.918  1.00 42.11  ? 373 ALA   B C      1 
ATOM   6286  O  O      . ALA   B 2  373 ? 12.215  -45.491  -40.222  1.00 38.90  ? 373 ALA   B O      1 
ATOM   6287  C  CB     . ALA   B 2  373 ? 10.953  -46.859  -42.618  1.00 41.29  ? 373 ALA   B CB     1 
ATOM   6288  N  N      . ILE   B 2  374 ? 13.613  -47.262  -40.416  1.00 36.29  ? 374 ILE   B N      1 
ATOM   6289  C  CA     . ILE   B 2  374 ? 14.074  -47.172  -39.032  1.00 34.07  ? 374 ILE   B CA     1 
ATOM   6290  C  C      . ILE   B 2  374 ? 14.780  -45.848  -38.770  1.00 38.47  ? 374 ILE   B C      1 
ATOM   6291  O  O      . ILE   B 2  374 ? 14.847  -45.392  -37.628  1.00 40.59  ? 374 ILE   B O      1 
ATOM   6292  C  CB     . ILE   B 2  374 ? 15.002  -48.352  -38.692  1.00 37.28  ? 374 ILE   B CB     1 
ATOM   6293  C  CG1    . ILE   B 2  374 ? 15.199  -48.472  -37.197  1.00 32.92  ? 374 ILE   B CG1    1 
ATOM   6294  C  CG2    . ILE   B 2  374 ? 16.350  -48.199  -39.389  1.00 39.04  ? 374 ILE   B CG2    1 
ATOM   6295  C  CD1    . ILE   B 2  374 ? 14.299  -49.454  -36.562  1.00 39.44  ? 374 ILE   B CD1    1 
ATOM   6296  N  N      . GLN   B 2  375 ? 15.306  -45.199  -39.804  1.00 37.09  ? 375 GLN   B N      1 
ATOM   6297  C  CA     . GLN   B 2  375 ? 15.873  -43.882  -39.574  1.00 40.66  ? 375 GLN   B CA     1 
ATOM   6298  C  C      . GLN   B 2  375 ? 14.906  -42.978  -38.825  1.00 41.63  ? 375 GLN   B C      1 
ATOM   6299  O  O      . GLN   B 2  375 ? 15.342  -42.118  -38.066  1.00 43.06  ? 375 GLN   B O      1 
ATOM   6300  C  CB     . GLN   B 2  375 ? 16.283  -43.229  -40.890  1.00 43.52  ? 375 GLN   B CB     1 
ATOM   6301  C  CG     . GLN   B 2  375 ? 15.125  -42.786  -41.769  1.00 45.55  ? 375 GLN   B CG     1 
ATOM   6302  C  CD     . GLN   B 2  375 ? 15.571  -41.849  -42.883  1.00 56.54  ? 375 GLN   B CD     1 
ATOM   6303  O  OE1    . GLN   B 2  375 ? 15.938  -40.703  -42.628  1.00 62.50  ? 375 GLN   B OE1    1 
ATOM   6304  N  NE2    . GLN   B 2  375 ? 15.589  -42.349  -44.119  1.00 57.22  ? 375 GLN   B NE2    1 
ATOM   6305  N  N      . GLU   B 2  376 ? 13.595  -43.140  -39.035  1.00 44.68  ? 376 GLU   B N      1 
ATOM   6306  C  CA     . GLU   B 2  376 ? 12.624  -42.301  -38.336  1.00 40.69  ? 376 GLU   B CA     1 
ATOM   6307  C  C      . GLU   B 2  376 ? 12.799  -42.401  -36.828  1.00 43.01  ? 376 GLU   B C      1 
ATOM   6308  O  O      . GLU   B 2  376 ? 12.623  -41.410  -36.099  1.00 39.38  ? 376 GLU   B O      1 
ATOM   6309  C  CB     . GLU   B 2  376 ? 11.210  -42.706  -38.720  1.00 38.46  ? 376 GLU   B CB     1 
ATOM   6310  C  CG     . GLU   B 2  376 ? 10.802  -42.290  -40.110  1.00 44.17  ? 376 GLU   B CG     1 
ATOM   6311  C  CD     . GLU   B 2  376 ? 9.341   -42.629  -40.395  1.00 51.88  ? 376 GLU   B CD     1 
ATOM   6312  O  OE1    . GLU   B 2  376 ? 8.704   -43.289  -39.526  1.00 50.99  ? 376 GLU   B OE1    1 
ATOM   6313  O  OE2    . GLU   B 2  376 ? 8.842   -42.244  -41.478  1.00 47.70  ? 376 GLU   B OE2    1 
ATOM   6314  N  N      . LEU   B 2  377 ? 13.133  -43.598  -36.344  1.00 36.72  ? 377 LEU   B N      1 
ATOM   6315  C  CA     . LEU   B 2  377 ? 13.418  -43.775  -34.928  1.00 39.37  ? 377 LEU   B CA     1 
ATOM   6316  C  C      . LEU   B 2  377 ? 14.652  -42.977  -34.526  1.00 44.85  ? 377 LEU   B C      1 
ATOM   6317  O  O      . LEU   B 2  377 ? 14.626  -42.188  -33.572  1.00 46.04  ? 377 LEU   B O      1 
ATOM   6318  C  CB     . LEU   B 2  377 ? 13.610  -45.262  -34.628  1.00 38.14  ? 377 LEU   B CB     1 
ATOM   6319  C  CG     . LEU   B 2  377 ? 13.470  -45.725  -33.187  1.00 38.58  ? 377 LEU   B CG     1 
ATOM   6320  C  CD1    . LEU   B 2  377 ? 13.321  -47.216  -33.151  1.00 46.11  ? 377 LEU   B CD1    1 
ATOM   6321  C  CD2    . LEU   B 2  377 ? 14.696  -45.336  -32.433  1.00 45.26  ? 377 LEU   B CD2    1 
ATOM   6322  N  N      . PHE   B 2  378 ? 15.743  -43.156  -35.265  1.00 44.42  ? 378 PHE   B N      1 
ATOM   6323  C  CA     . PHE   B 2  378 ? 16.976  -42.474  -34.912  1.00 42.16  ? 378 PHE   B CA     1 
ATOM   6324  C  C      . PHE   B 2  378 ? 16.859  -40.968  -35.079  1.00 42.34  ? 378 PHE   B C      1 
ATOM   6325  O  O      . PHE   B 2  378 ? 17.607  -40.228  -34.440  1.00 49.62  ? 378 PHE   B O      1 
ATOM   6326  C  CB     . PHE   B 2  378 ? 18.122  -43.051  -35.732  1.00 37.29  ? 378 PHE   B CB     1 
ATOM   6327  C  CG     . PHE   B 2  378 ? 18.376  -44.490  -35.424  1.00 38.97  ? 378 PHE   B CG     1 
ATOM   6328  C  CD1    . PHE   B 2  378 ? 18.551  -44.894  -34.106  1.00 36.65  ? 378 PHE   B CD1    1 
ATOM   6329  C  CD2    . PHE   B 2  378 ? 18.415  -45.443  -36.423  1.00 36.64  ? 378 PHE   B CD2    1 
ATOM   6330  C  CE1    . PHE   B 2  378 ? 18.773  -46.237  -33.796  1.00 41.62  ? 378 PHE   B CE1    1 
ATOM   6331  C  CE2    . PHE   B 2  378 ? 18.628  -46.779  -36.126  1.00 34.31  ? 378 PHE   B CE2    1 
ATOM   6332  C  CZ     . PHE   B 2  378 ? 18.806  -47.189  -34.815  1.00 36.02  ? 378 PHE   B CZ     1 
ATOM   6333  N  N      . LYS   B 2  379 ? 15.946  -40.489  -35.922  1.00 40.30  ? 379 LYS   B N      1 
ATOM   6334  C  CA     . LYS   B 2  379 ? 15.711  -39.053  -35.985  1.00 38.34  ? 379 LYS   B CA     1 
ATOM   6335  C  C      . LYS   B 2  379 ? 14.943  -38.596  -34.766  1.00 42.86  ? 379 LYS   B C      1 
ATOM   6336  O  O      . LYS   B 2  379 ? 15.231  -37.543  -34.203  1.00 42.61  ? 379 LYS   B O      1 
ATOM   6337  C  CB     . LYS   B 2  379 ? 14.928  -38.667  -37.236  1.00 46.08  ? 379 LYS   B CB     1 
ATOM   6338  C  CG     . LYS   B 2  379 ? 15.718  -38.509  -38.535  1.00 51.69  ? 379 LYS   B CG     1 
ATOM   6339  C  CD     . LYS   B 2  379 ? 14.742  -38.543  -39.725  1.00 61.44  ? 379 LYS   B CD     1 
ATOM   6340  C  CE     . LYS   B 2  379 ? 15.456  -38.539  -41.072  1.00 73.20  ? 379 LYS   B CE     1 
ATOM   6341  N  NZ     . LYS   B 2  379 ? 14.765  -37.688  -42.092  1.00 83.19  ? 379 LYS   B NZ     1 
ATOM   6342  N  N      . ARG   B 2  380 ? 13.939  -39.367  -34.362  1.00 43.07  ? 380 ARG   B N      1 
ATOM   6343  C  CA     . ARG   B 2  380 ? 13.134  -38.966  -33.221  1.00 39.68  ? 380 ARG   B CA     1 
ATOM   6344  C  C      . ARG   B 2  380 ? 14.025  -38.709  -32.023  1.00 41.44  ? 380 ARG   B C      1 
ATOM   6345  O  O      . ARG   B 2  380 ? 13.907  -37.679  -31.344  1.00 40.52  ? 380 ARG   B O      1 
ATOM   6346  C  CB     . ARG   B 2  380 ? 12.096  -40.045  -32.907  1.00 38.25  ? 380 ARG   B CB     1 
ATOM   6347  C  CG     . ARG   B 2  380 ? 11.277  -39.751  -31.679  1.00 37.30  ? 380 ARG   B CG     1 
ATOM   6348  C  CD     . ARG   B 2  380 ? 10.307  -40.866  -31.365  1.00 42.33  ? 380 ARG   B CD     1 
ATOM   6349  N  NE     . ARG   B 2  380 ? 10.889  -41.887  -30.492  1.00 46.52  ? 380 ARG   B NE     1 
ATOM   6350  C  CZ     . ARG   B 2  380 ? 10.732  -43.197  -30.672  1.00 47.25  ? 380 ARG   B CZ     1 
ATOM   6351  N  NH1    . ARG   B 2  380 ? 9.986   -43.685  -31.659  1.00 35.97  ? 380 ARG   B NH1    1 
ATOM   6352  N  NH2    . ARG   B 2  380 ? 11.332  -44.041  -29.841  1.00 42.69  ? 380 ARG   B NH2    1 
ATOM   6353  N  N      . ILE   B 2  381 ? 14.944  -39.638  -31.764  1.00 46.03  ? 381 ILE   B N      1 
ATOM   6354  C  CA     . ILE   B 2  381 ? 15.826  -39.541  -30.611  1.00 40.23  ? 381 ILE   B CA     1 
ATOM   6355  C  C      . ILE   B 2  381 ? 16.857  -38.449  -30.829  1.00 40.23  ? 381 ILE   B C      1 
ATOM   6356  O  O      . ILE   B 2  381 ? 17.185  -37.699  -29.905  1.00 40.25  ? 381 ILE   B O      1 
ATOM   6357  C  CB     . ILE   B 2  381 ? 16.432  -40.925  -30.358  1.00 36.39  ? 381 ILE   B CB     1 
ATOM   6358  C  CG1    . ILE   B 2  381 ? 15.304  -41.830  -29.879  1.00 35.58  ? 381 ILE   B CG1    1 
ATOM   6359  C  CG2    . ILE   B 2  381 ? 17.586  -40.867  -29.364  1.00 36.95  ? 381 ILE   B CG2    1 
ATOM   6360  C  CD1    . ILE   B 2  381 ? 15.672  -43.236  -29.721  1.00 39.96  ? 381 ILE   B CD1    1 
ATOM   6361  N  N      . SER   B 2  382 ? 17.328  -38.273  -32.054  1.00 41.83  ? 382 SER   B N      1 
ATOM   6362  C  CA     . SER   B 2  382 ? 18.276  -37.193  -32.275  1.00 39.33  ? 382 SER   B CA     1 
ATOM   6363  C  C      . SER   B 2  382 ? 17.638  -35.837  -32.002  1.00 38.81  ? 382 SER   B C      1 
ATOM   6364  O  O      . SER   B 2  382 ? 18.304  -34.919  -31.520  1.00 43.22  ? 382 SER   B O      1 
ATOM   6365  C  CB     . SER   B 2  382 ? 18.814  -37.277  -33.689  1.00 36.91  ? 382 SER   B CB     1 
ATOM   6366  O  OG     . SER   B 2  382 ? 20.195  -37.045  -33.678  1.00 45.89  ? 382 SER   B OG     1 
ATOM   6367  N  N      . GLU   B 2  383 ? 16.351  -35.695  -32.277  1.00 40.09  ? 383 GLU   B N      1 
ATOM   6368  C  CA     . GLU   B 2  383 ? 15.678  -34.436  -31.995  1.00 43.33  ? 383 GLU   B CA     1 
ATOM   6369  C  C      . GLU   B 2  383 ? 15.584  -34.182  -30.499  1.00 42.98  ? 383 GLU   B C      1 
ATOM   6370  O  O      . GLU   B 2  383 ? 15.880  -33.077  -30.030  1.00 40.89  ? 383 GLU   B O      1 
ATOM   6371  C  CB     . GLU   B 2  383 ? 14.287  -34.428  -32.622  1.00 42.06  ? 383 GLU   B CB     1 
ATOM   6372  C  CG     . GLU   B 2  383 ? 14.322  -33.953  -34.045  1.00 52.33  ? 383 GLU   B CG     1 
ATOM   6373  C  CD     . GLU   B 2  383 ? 13.141  -34.448  -34.836  1.00 73.10  ? 383 GLU   B CD     1 
ATOM   6374  O  OE1    . GLU   B 2  383 ? 13.293  -34.611  -36.079  1.00 76.94  ? 383 GLU   B OE1    1 
ATOM   6375  O  OE2    . GLU   B 2  383 ? 12.070  -34.667  -34.206  1.00 73.79  ? 383 GLU   B OE2    1 
ATOM   6376  N  N      . GLN   B 2  384 ? 15.136  -35.181  -29.734  1.00 37.21  ? 384 GLN   B N      1 
ATOM   6377  C  CA     . GLN   B 2  384 ? 15.080  -35.004  -28.293  1.00 35.79  ? 384 GLN   B CA     1 
ATOM   6378  C  C      . GLN   B 2  384 ? 16.475  -34.761  -27.719  1.00 39.16  ? 384 GLN   B C      1 
ATOM   6379  O  O      . GLN   B 2  384 ? 16.648  -33.933  -26.819  1.00 42.13  ? 384 GLN   B O      1 
ATOM   6380  C  CB     . GLN   B 2  384 ? 14.397  -36.213  -27.656  1.00 41.27  ? 384 GLN   B CB     1 
ATOM   6381  C  CG     . GLN   B 2  384 ? 13.083  -36.624  -28.346  1.00 42.28  ? 384 GLN   B CG     1 
ATOM   6382  C  CD     . GLN   B 2  384 ? 12.585  -38.000  -27.912  1.00 46.54  ? 384 GLN   B CD     1 
ATOM   6383  O  OE1    . GLN   B 2  384 ? 13.288  -38.726  -27.224  1.00 52.98  ? 384 GLN   B OE1    1 
ATOM   6384  N  NE2    . GLN   B 2  384 ? 11.383  -38.369  -28.334  1.00 49.17  ? 384 GLN   B NE2    1 
ATOM   6385  N  N      . PHE   B 2  385 ? 17.488  -35.443  -28.249  1.00 34.97  ? 385 PHE   B N      1 
ATOM   6386  C  CA     . PHE   B 2  385 ? 18.857  -35.203  -27.812  1.00 37.00  ? 385 PHE   B CA     1 
ATOM   6387  C  C      . PHE   B 2  385 ? 19.261  -33.740  -27.982  1.00 40.41  ? 385 PHE   B C      1 
ATOM   6388  O  O      . PHE   B 2  385 ? 19.711  -33.096  -27.029  1.00 39.66  ? 385 PHE   B O      1 
ATOM   6389  C  CB     . PHE   B 2  385 ? 19.815  -36.122  -28.572  1.00 37.08  ? 385 PHE   B CB     1 
ATOM   6390  C  CG     . PHE   B 2  385 ? 21.280  -35.936  -28.204  1.00 39.78  ? 385 PHE   B CG     1 
ATOM   6391  C  CD1    . PHE   B 2  385 ? 22.039  -34.901  -28.756  1.00 38.72  ? 385 PHE   B CD1    1 
ATOM   6392  C  CD2    . PHE   B 2  385 ? 21.905  -36.816  -27.338  1.00 34.55  ? 385 PHE   B CD2    1 
ATOM   6393  C  CE1    . PHE   B 2  385 ? 23.380  -34.745  -28.437  1.00 39.41  ? 385 PHE   B CE1    1 
ATOM   6394  C  CE2    . PHE   B 2  385 ? 23.249  -36.659  -27.017  1.00 36.96  ? 385 PHE   B CE2    1 
ATOM   6395  C  CZ     . PHE   B 2  385 ? 23.985  -35.619  -27.570  1.00 38.35  ? 385 PHE   B CZ     1 
ATOM   6396  N  N      . THR   B 2  386 ? 19.167  -33.196  -29.195  1.00 38.17  ? 386 THR   B N      1 
ATOM   6397  C  CA     . THR   B 2  386 ? 19.683  -31.839  -29.308  1.00 39.34  ? 386 THR   B CA     1 
ATOM   6398  C  C      . THR   B 2  386 ? 18.734  -30.814  -28.711  1.00 35.88  ? 386 THR   B C      1 
ATOM   6399  O  O      . THR   B 2  386 ? 19.151  -29.690  -28.436  1.00 41.20  ? 386 THR   B O      1 
ATOM   6400  C  CB     . THR   B 2  386 ? 20.011  -31.455  -30.762  1.00 38.11  ? 386 THR   B CB     1 
ATOM   6401  O  OG1    . THR   B 2  386 ? 18.813  -31.215  -31.476  1.00 39.31  ? 386 THR   B OG1    1 
ATOM   6402  C  CG2    . THR   B 2  386 ? 20.783  -32.570  -31.465  1.00 47.44  ? 386 THR   B CG2    1 
ATOM   6403  N  N      . ALA   B 2  387 ? 17.476  -31.170  -28.473  1.00 41.45  ? 387 ALA   B N      1 
ATOM   6404  C  CA     . ALA   B 2  387 ? 16.570  -30.208  -27.855  1.00 40.37  ? 387 ALA   B CA     1 
ATOM   6405  C  C      . ALA   B 2  387 ? 17.120  -29.740  -26.515  1.00 41.19  ? 387 ALA   B C      1 
ATOM   6406  O  O      . ALA   B 2  387 ? 17.062  -28.549  -26.200  1.00 44.67  ? 387 ALA   B O      1 
ATOM   6407  C  CB     . ALA   B 2  387 ? 15.179  -30.808  -27.701  1.00 29.31  ? 387 ALA   B CB     1 
ATOM   6408  N  N      . MET   B 2  388 ? 17.703  -30.656  -25.736  1.00 34.15  ? 388 MET   B N      1 
ATOM   6409  C  CA     . MET   B 2  388 ? 18.367  -30.333  -24.486  1.00 33.80  ? 388 MET   B CA     1 
ATOM   6410  C  C      . MET   B 2  388 ? 19.832  -29.958  -24.661  1.00 39.31  ? 388 MET   B C      1 
ATOM   6411  O  O      . MET   B 2  388 ? 20.309  -29.021  -24.008  1.00 43.63  ? 388 MET   B O      1 
ATOM   6412  C  CB     . MET   B 2  388 ? 18.296  -31.508  -23.519  1.00 32.01  ? 388 MET   B CB     1 
ATOM   6413  C  CG     . MET   B 2  388 ? 16.983  -32.223  -23.502  1.00 35.13  ? 388 MET   B CG     1 
ATOM   6414  S  SD     . MET   B 2  388 ? 17.021  -33.536  -22.279  1.00 37.99  ? 388 MET   B SD     1 
ATOM   6415  C  CE     . MET   B 2  388 ? 17.701  -34.869  -23.238  1.00 32.93  ? 388 MET   B CE     1 
ATOM   6416  N  N      . PHE   B 2  389 ? 20.576  -30.696  -25.486  1.00 39.34  ? 389 PHE   B N      1 
ATOM   6417  C  CA     . PHE   B 2  389 ? 22.030  -30.510  -25.548  1.00 43.39  ? 389 PHE   B CA     1 
ATOM   6418  C  C      . PHE   B 2  389 ? 22.416  -29.143  -26.098  1.00 38.82  ? 389 PHE   B C      1 
ATOM   6419  O  O      . PHE   B 2  389 ? 23.496  -28.646  -25.766  1.00 40.71  ? 389 PHE   B O      1 
ATOM   6420  C  CB     . PHE   B 2  389 ? 22.673  -31.624  -26.387  1.00 44.60  ? 389 PHE   B CB     1 
ATOM   6421  C  CG     . PHE   B 2  389 ? 24.197  -31.641  -26.385  1.00 37.32  ? 389 PHE   B CG     1 
ATOM   6422  C  CD1    . PHE   B 2  389 ? 24.907  -32.122  -25.306  1.00 39.63  ? 389 PHE   B CD1    1 
ATOM   6423  C  CD2    . PHE   B 2  389 ? 24.910  -31.241  -27.512  1.00 39.38  ? 389 PHE   B CD2    1 
ATOM   6424  C  CE1    . PHE   B 2  389 ? 26.299  -32.184  -25.347  1.00 39.18  ? 389 PHE   B CE1    1 
ATOM   6425  C  CE2    . PHE   B 2  389 ? 26.295  -31.283  -27.549  1.00 33.04  ? 389 PHE   B CE2    1 
ATOM   6426  C  CZ     . PHE   B 2  389 ? 26.988  -31.754  -26.468  1.00 37.64  ? 389 PHE   B CZ     1 
ATOM   6427  N  N      . ARG   B 2  390 ? 21.569  -28.518  -26.931  1.00 34.79  ? 390 ARG   B N      1 
ATOM   6428  C  CA     . ARG   B 2  390 ? 21.907  -27.183  -27.435  1.00 39.89  ? 390 ARG   B CA     1 
ATOM   6429  C  C      . ARG   B 2  390 ? 21.973  -26.161  -26.299  1.00 39.10  ? 390 ARG   B C      1 
ATOM   6430  O  O      . ARG   B 2  390 ? 22.531  -25.076  -26.481  1.00 46.58  ? 390 ARG   B O      1 
ATOM   6431  C  CB     . ARG   B 2  390 ? 20.910  -26.732  -28.530  1.00 34.88  ? 390 ARG   B CB     1 
ATOM   6432  C  CG     . ARG   B 2  390 ? 19.527  -26.410  -27.981  1.00 47.22  ? 390 ARG   B CG     1 
ATOM   6433  C  CD     . ARG   B 2  390 ? 18.462  -25.976  -29.000  1.00 57.63  ? 390 ARG   B CD     1 
ATOM   6434  N  NE     . ARG   B 2  390 ? 17.140  -26.183  -28.393  1.00 60.23  ? 390 ARG   B NE     1 
ATOM   6435  C  CZ     . ARG   B 2  390 ? 15.963  -25.942  -28.969  1.00 64.46  ? 390 ARG   B CZ     1 
ATOM   6436  N  NH1    . ARG   B 2  390 ? 15.870  -25.357  -30.161  1.00 67.21  ? 390 ARG   B NH1    1 
ATOM   6437  N  NH2    . ARG   B 2  390 ? 14.848  -26.308  -28.336  1.00 54.02  ? 390 ARG   B NH2    1 
ATOM   6438  N  N      . ARG   B 2  391 ? 21.417  -26.497  -25.134  1.00 40.12  ? 391 ARG   B N      1 
ATOM   6439  C  CA     . ARG   B 2  391 ? 21.511  -25.722  -23.906  1.00 32.83  ? 391 ARG   B CA     1 
ATOM   6440  C  C      . ARG   B 2  391 ? 22.330  -26.448  -22.852  1.00 35.44  ? 391 ARG   B C      1 
ATOM   6441  O  O      . ARG   B 2  391 ? 22.387  -26.012  -21.702  1.00 33.50  ? 391 ARG   B O      1 
ATOM   6442  C  CB     . ARG   B 2  391 ? 20.107  -25.417  -23.379  1.00 38.38  ? 391 ARG   B CB     1 
ATOM   6443  C  CG     . ARG   B 2  391 ? 19.196  -24.669  -24.383  1.00 36.33  ? 391 ARG   B CG     1 
ATOM   6444  C  CD     . ARG   B 2  391 ? 19.734  -23.318  -24.665  1.00 29.28  ? 391 ARG   B CD     1 
ATOM   6445  N  NE     . ARG   B 2  391 ? 19.351  -22.402  -23.603  1.00 29.66  ? 391 ARG   B NE     1 
ATOM   6446  C  CZ     . ARG   B 2  391 ? 18.170  -21.802  -23.508  1.00 38.63  ? 391 ARG   B CZ     1 
ATOM   6447  N  NH1    . ARG   B 2  391 ? 17.233  -21.969  -24.429  1.00 38.47  ? 391 ARG   B NH1    1 
ATOM   6448  N  NH2    . ARG   B 2  391 ? 17.932  -20.997  -22.475  1.00 33.37  ? 391 ARG   B NH2    1 
ATOM   6449  N  N      . LYS   B 2  392 ? 22.977  -27.548  -23.216  1.00 38.67  ? 392 LYS   B N      1 
ATOM   6450  C  CA     . LYS   B 2  392 ? 23.835  -28.268  -22.283  1.00 42.49  ? 392 LYS   B CA     1 
ATOM   6451  C  C      . LYS   B 2  392 ? 23.073  -28.625  -21.003  1.00 39.29  ? 392 LYS   B C      1 
ATOM   6452  O  O      . LYS   B 2  392 ? 23.647  -28.714  -19.915  1.00 37.93  ? 392 LYS   B O      1 
ATOM   6453  C  CB     . LYS   B 2  392 ? 25.104  -27.462  -21.986  1.00 39.00  ? 392 LYS   B CB     1 
ATOM   6454  C  CG     . LYS   B 2  392 ? 26.260  -27.774  -22.952  1.00 53.76  ? 392 LYS   B CG     1 
ATOM   6455  C  CD     . LYS   B 2  392 ? 26.945  -26.508  -23.545  1.00 66.39  ? 392 LYS   B CD     1 
ATOM   6456  C  CE     . LYS   B 2  392 ? 28.033  -25.903  -22.615  1.00 66.08  ? 392 LYS   B CE     1 
ATOM   6457  N  NZ     . LYS   B 2  392 ? 28.781  -24.765  -23.234  1.00 66.16  ? 392 LYS   B NZ     1 
ATOM   6458  N  N      . ALA   B 2  393 ? 21.772  -28.867  -21.153  1.00 38.73  ? 393 ALA   B N      1 
ATOM   6459  C  CA     . ALA   B 2  393 ? 20.905  -29.181  -20.027  1.00 36.57  ? 393 ALA   B CA     1 
ATOM   6460  C  C      . ALA   B 2  393 ? 21.154  -30.592  -19.519  1.00 34.84  ? 393 ALA   B C      1 
ATOM   6461  O  O      . ALA   B 2  393 ? 21.329  -31.531  -20.303  1.00 34.88  ? 393 ALA   B O      1 
ATOM   6462  C  CB     . ALA   B 2  393 ? 19.431  -29.027  -20.424  1.00 31.10  ? 393 ALA   B CB     1 
ATOM   6463  N  N      . PHE   B 2  394 ? 21.121  -30.734  -18.195  1.00 31.79  ? 394 PHE   B N      1 
ATOM   6464  C  CA     . PHE   B 2  394 ? 21.316  -31.993  -17.477  1.00 31.07  ? 394 PHE   B CA     1 
ATOM   6465  C  C      . PHE   B 2  394 ? 22.706  -32.574  -17.695  1.00 30.18  ? 394 PHE   B C      1 
ATOM   6466  O  O      . PHE   B 2  394 ? 23.027  -33.616  -17.128  1.00 34.48  ? 394 PHE   B O      1 
ATOM   6467  C  CB     . PHE   B 2  394 ? 20.213  -32.990  -17.862  1.00 33.81  ? 394 PHE   B CB     1 
ATOM   6468  C  CG     . PHE   B 2  394 ? 18.857  -32.477  -17.541  1.00 31.60  ? 394 PHE   B CG     1 
ATOM   6469  C  CD1    . PHE   B 2  394 ? 18.407  -32.456  -16.232  1.00 32.46  ? 394 PHE   B CD1    1 
ATOM   6470  C  CD2    . PHE   B 2  394 ? 18.066  -31.916  -18.519  1.00 33.69  ? 394 PHE   B CD2    1 
ATOM   6471  C  CE1    . PHE   B 2  394 ? 17.174  -31.917  -15.911  1.00 30.32  ? 394 PHE   B CE1    1 
ATOM   6472  C  CE2    . PHE   B 2  394 ? 16.824  -31.371  -18.196  1.00 29.90  ? 394 PHE   B CE2    1 
ATOM   6473  C  CZ     . PHE   B 2  394 ? 16.391  -31.371  -16.893  1.00 28.28  ? 394 PHE   B CZ     1 
ATOM   6474  N  N      . LEU   B 2  395 ? 23.554  -31.895  -18.474  1.00 29.30  ? 395 LEU   B N      1 
ATOM   6475  C  CA     . LEU   B 2  395 ? 24.877  -32.439  -18.775  1.00 29.84  ? 395 LEU   B CA     1 
ATOM   6476  C  C      . LEU   B 2  395 ? 25.723  -32.691  -17.516  1.00 34.41  ? 395 LEU   B C      1 
ATOM   6477  O  O      . LEU   B 2  395 ? 26.587  -33.583  -17.513  1.00 32.96  ? 395 LEU   B O      1 
ATOM   6478  C  CB     . LEU   B 2  395 ? 25.596  -31.496  -19.729  1.00 30.35  ? 395 LEU   B CB     1 
ATOM   6479  C  CG     . LEU   B 2  395 ? 26.383  -32.198  -20.835  1.00 42.92  ? 395 LEU   B CG     1 
ATOM   6480  C  CD1    . LEU   B 2  395 ? 25.505  -33.213  -21.582  1.00 37.73  ? 395 LEU   B CD1    1 
ATOM   6481  C  CD2    . LEU   B 2  395 ? 26.904  -31.158  -21.784  1.00 45.42  ? 395 LEU   B CD2    1 
ATOM   6482  N  N      . HIS   B 2  396 ? 25.507  -31.909  -16.448  1.00 32.35  ? 396 HIS   B N      1 
ATOM   6483  C  CA     . HIS   B 2  396 ? 26.370  -32.008  -15.279  1.00 28.09  ? 396 HIS   B CA     1 
ATOM   6484  C  C      . HIS   B 2  396 ? 26.308  -33.395  -14.671  1.00 33.14  ? 396 HIS   B C      1 
ATOM   6485  O  O      . HIS   B 2  396 ? 27.296  -33.859  -14.102  1.00 34.22  ? 396 HIS   B O      1 
ATOM   6486  C  CB     . HIS   B 2  396 ? 25.985  -30.965  -14.229  1.00 27.67  ? 396 HIS   B CB     1 
ATOM   6487  C  CG     . HIS   B 2  396 ? 24.657  -31.227  -13.583  1.00 31.07  ? 396 HIS   B CG     1 
ATOM   6488  N  ND1    . HIS   B 2  396 ? 24.533  -31.880  -12.377  1.00 34.31  ? 396 HIS   B ND1    1 
ATOM   6489  C  CD2    . HIS   B 2  396 ? 23.397  -30.956  -13.991  1.00 31.67  ? 396 HIS   B CD2    1 
ATOM   6490  C  CE1    . HIS   B 2  396 ? 23.257  -32.002  -12.070  1.00 30.59  ? 396 HIS   B CE1    1 
ATOM   6491  N  NE2    . HIS   B 2  396 ? 22.548  -31.441  -13.029  1.00 32.29  ? 396 HIS   B NE2    1 
ATOM   6492  N  N      . TRP   B 2  397 ? 25.158  -34.070  -14.764  1.00 30.58  ? 397 TRP   B N      1 
ATOM   6493  C  CA     . TRP   B 2  397 ? 25.069  -35.432  -14.252  1.00 27.88  ? 397 TRP   B CA     1 
ATOM   6494  C  C      . TRP   B 2  397 ? 26.165  -36.304  -14.832  1.00 33.61  ? 397 TRP   B C      1 
ATOM   6495  O  O      . TRP   B 2  397 ? 26.553  -37.299  -14.215  1.00 36.95  ? 397 TRP   B O      1 
ATOM   6496  C  CB     . TRP   B 2  397 ? 23.708  -36.044  -14.580  1.00 33.48  ? 397 TRP   B CB     1 
ATOM   6497  C  CG     . TRP   B 2  397 ? 22.558  -35.421  -13.836  1.00 34.11  ? 397 TRP   B CG     1 
ATOM   6498  C  CD1    . TRP   B 2  397 ? 21.391  -34.895  -14.368  1.00 32.02  ? 397 TRP   B CD1    1 
ATOM   6499  C  CD2    . TRP   B 2  397 ? 22.458  -35.263  -12.428  1.00 36.11  ? 397 TRP   B CD2    1 
ATOM   6500  N  NE1    . TRP   B 2  397 ? 20.588  -34.425  -13.365  1.00 31.43  ? 397 TRP   B NE1    1 
ATOM   6501  C  CE2    . TRP   B 2  397 ? 21.217  -34.639  -12.162  1.00 36.04  ? 397 TRP   B CE2    1 
ATOM   6502  C  CE3    . TRP   B 2  397 ? 23.286  -35.610  -11.353  1.00 30.96  ? 397 TRP   B CE3    1 
ATOM   6503  C  CZ2    . TRP   B 2  397 ? 20.797  -34.346  -10.863  1.00 36.19  ? 397 TRP   B CZ2    1 
ATOM   6504  C  CZ3    . TRP   B 2  397 ? 22.862  -35.297  -10.062  1.00 31.18  ? 397 TRP   B CZ3    1 
ATOM   6505  C  CH2    . TRP   B 2  397 ? 21.635  -34.674  -9.837   1.00 32.93  ? 397 TRP   B CH2    1 
ATOM   6506  N  N      . TYR   B 2  398 ? 26.671  -35.946  -16.011  1.00 32.47  ? 398 TYR   B N      1 
ATOM   6507  C  CA     . TYR   B 2  398 ? 27.661  -36.726  -16.733  1.00 32.01  ? 398 TYR   B CA     1 
ATOM   6508  C  C      . TYR   B 2  398 ? 29.054  -36.134  -16.671  1.00 37.14  ? 398 TYR   B C      1 
ATOM   6509  O  O      . TYR   B 2  398 ? 30.036  -36.882  -16.579  1.00 39.16  ? 398 TYR   B O      1 
ATOM   6510  C  CB     . TYR   B 2  398 ? 27.282  -36.851  -18.208  1.00 35.63  ? 398 TYR   B CB     1 
ATOM   6511  C  CG     . TYR   B 2  398 ? 25.913  -37.385  -18.486  1.00 37.75  ? 398 TYR   B CG     1 
ATOM   6512  C  CD1    . TYR   B 2  398 ? 24.811  -36.536  -18.523  1.00 37.62  ? 398 TYR   B CD1    1 
ATOM   6513  C  CD2    . TYR   B 2  398 ? 25.715  -38.734  -18.735  1.00 38.42  ? 398 TYR   B CD2    1 
ATOM   6514  C  CE1    . TYR   B 2  398 ? 23.542  -37.025  -18.788  1.00 35.95  ? 398 TYR   B CE1    1 
ATOM   6515  C  CE2    . TYR   B 2  398 ? 24.460  -39.229  -19.003  1.00 39.42  ? 398 TYR   B CE2    1 
ATOM   6516  C  CZ     . TYR   B 2  398 ? 23.374  -38.373  -19.033  1.00 35.92  ? 398 TYR   B CZ     1 
ATOM   6517  O  OH     . TYR   B 2  398 ? 22.132  -38.882  -19.319  1.00 35.21  ? 398 TYR   B OH     1 
ATOM   6518  N  N      . THR   B 2  399 ? 29.180  -34.812  -16.792  1.00 35.87  ? 399 THR   B N      1 
ATOM   6519  C  CA     . THR   B 2  399 ? 30.498  -34.218  -16.610  1.00 33.45  ? 399 THR   B CA     1 
ATOM   6520  C  C      . THR   B 2  399 ? 31.009  -34.505  -15.212  1.00 32.68  ? 399 THR   B C      1 
ATOM   6521  O  O      . THR   B 2  399 ? 32.214  -34.609  -14.995  1.00 40.66  ? 399 THR   B O      1 
ATOM   6522  C  CB     . THR   B 2  399 ? 30.441  -32.722  -16.891  1.00 36.84  ? 399 THR   B CB     1 
ATOM   6523  O  OG1    . THR   B 2  399 ? 29.443  -32.112  -16.064  1.00 35.38  ? 399 THR   B OG1    1 
ATOM   6524  C  CG2    . THR   B 2  399 ? 30.109  -32.487  -18.358  1.00 25.70  ? 399 THR   B CG2    1 
ATOM   6525  N  N      . GLY   B 2  400 ? 30.102  -34.722  -14.268  1.00 36.28  ? 400 GLY   B N      1 
ATOM   6526  C  CA     . GLY   B 2  400 ? 30.474  -35.115  -12.925  1.00 32.25  ? 400 GLY   B CA     1 
ATOM   6527  C  C      . GLY   B 2  400 ? 31.087  -36.487  -12.811  1.00 34.43  ? 400 GLY   B C      1 
ATOM   6528  O  O      . GLY   B 2  400 ? 31.689  -36.783  -11.775  1.00 37.83  ? 400 GLY   B O      1 
ATOM   6529  N  N      . GLU   B 2  401 ? 30.935  -37.342  -13.814  1.00 35.58  ? 401 GLU   B N      1 
ATOM   6530  C  CA     . GLU   B 2  401 ? 31.505  -38.683  -13.754  1.00 38.15  ? 401 GLU   B CA     1 
ATOM   6531  C  C      . GLU   B 2  401 ? 32.633  -38.854  -14.749  1.00 38.82  ? 401 GLU   B C      1 
ATOM   6532  O  O      . GLU   B 2  401 ? 33.016  -39.984  -15.037  1.00 37.24  ? 401 GLU   B O      1 
ATOM   6533  C  CB     . GLU   B 2  401 ? 30.447  -39.765  -13.996  1.00 37.67  ? 401 GLU   B CB     1 
ATOM   6534  C  CG     . GLU   B 2  401 ? 29.227  -39.611  -13.141  1.00 40.62  ? 401 GLU   B CG     1 
ATOM   6535  C  CD     . GLU   B 2  401 ? 29.336  -40.321  -11.806  1.00 41.79  ? 401 GLU   B CD     1 
ATOM   6536  O  OE1    . GLU   B 2  401 ? 29.925  -41.426  -11.716  1.00 42.41  ? 401 GLU   B OE1    1 
ATOM   6537  O  OE2    . GLU   B 2  401 ? 28.845  -39.738  -10.827  1.00 44.34  ? 401 GLU   B OE2    1 
ATOM   6538  N  N      . GLY   B 2  402 ? 33.163  -37.762  -15.287  1.00 37.21  ? 402 GLY   B N      1 
ATOM   6539  C  CA     . GLY   B 2  402 ? 34.338  -37.791  -16.130  1.00 33.45  ? 402 GLY   B CA     1 
ATOM   6540  C  C      . GLY   B 2  402 ? 34.090  -37.392  -17.563  1.00 42.61  ? 402 GLY   B C      1 
ATOM   6541  O  O      . GLY   B 2  402 ? 35.059  -37.096  -18.284  1.00 49.01  ? 402 GLY   B O      1 
ATOM   6542  N  N      . MET   B 2  403 ? 32.837  -37.375  -18.015  1.00 40.17  ? 403 MET   B N      1 
ATOM   6543  C  CA     . MET   B 2  403 ? 32.622  -37.266  -19.443  1.00 35.93  ? 403 MET   B CA     1 
ATOM   6544  C  C      . MET   B 2  403 ? 32.814  -35.836  -19.896  1.00 37.85  ? 403 MET   B C      1 
ATOM   6545  O  O      . MET   B 2  403 ? 32.632  -34.881  -19.146  1.00 43.62  ? 403 MET   B O      1 
ATOM   6546  C  CB     . MET   B 2  403 ? 31.229  -37.743  -19.866  1.00 36.19  ? 403 MET   B CB     1 
ATOM   6547  C  CG     . MET   B 2  403 ? 30.818  -39.132  -19.405  1.00 40.00  ? 403 MET   B CG     1 
ATOM   6548  S  SD     . MET   B 2  403 ? 29.512  -39.864  -20.421  1.00 42.39  ? 403 MET   B SD     1 
ATOM   6549  C  CE     . MET   B 2  403 ? 29.847  -39.197  -22.052  1.00 34.97  ? 403 MET   B CE     1 
ATOM   6550  N  N      . ASP   B 2  404 ? 33.148  -35.707  -21.163  1.00 42.50  ? 404 ASP   B N      1 
ATOM   6551  C  CA     . ASP   B 2  404 ? 33.353  -34.434  -21.814  1.00 42.44  ? 404 ASP   B CA     1 
ATOM   6552  C  C      . ASP   B 2  404 ? 32.176  -34.123  -22.724  1.00 43.37  ? 404 ASP   B C      1 
ATOM   6553  O  O      . ASP   B 2  404 ? 31.524  -35.028  -23.245  1.00 44.08  ? 404 ASP   B O      1 
ATOM   6554  C  CB     . ASP   B 2  404 ? 34.620  -34.465  -22.658  1.00 46.34  ? 404 ASP   B CB     1 
ATOM   6555  C  CG     . ASP   B 2  404 ? 35.225  -33.121  -22.805  1.00 59.26  ? 404 ASP   B CG     1 
ATOM   6556  O  OD1    . ASP   B 2  404 ? 35.616  -32.566  -21.755  1.00 68.50  ? 404 ASP   B OD1    1 
ATOM   6557  O  OD2    . ASP   B 2  404 ? 35.244  -32.590  -23.945  1.00 62.54  ? 404 ASP   B OD2    1 
ATOM   6558  N  N      . GLU   B 2  405 ? 31.916  -32.828  -22.914  1.00 43.80  ? 405 GLU   B N      1 
ATOM   6559  C  CA     . GLU   B 2  405 ? 30.954  -32.409  -23.922  1.00 38.84  ? 405 GLU   B CA     1 
ATOM   6560  C  C      . GLU   B 2  405 ? 31.276  -33.035  -25.261  1.00 44.19  ? 405 GLU   B C      1 
ATOM   6561  O  O      . GLU   B 2  405 ? 30.374  -33.401  -26.021  1.00 47.70  ? 405 GLU   B O      1 
ATOM   6562  C  CB     . GLU   B 2  405 ? 30.954  -30.889  -24.047  1.00 42.03  ? 405 GLU   B CB     1 
ATOM   6563  C  CG     . GLU   B 2  405 ? 30.106  -30.199  -23.013  1.00 53.97  ? 405 GLU   B CG     1 
ATOM   6564  C  CD     . GLU   B 2  405 ? 30.018  -28.695  -23.222  1.00 63.81  ? 405 GLU   B CD     1 
ATOM   6565  O  OE1    . GLU   B 2  405 ? 30.169  -28.220  -24.382  1.00 60.21  ? 405 GLU   B OE1    1 
ATOM   6566  O  OE2    . GLU   B 2  405 ? 29.773  -27.995  -22.212  1.00 63.33  ? 405 GLU   B OE2    1 
ATOM   6567  N  N      . MET   B 2  406 ? 32.568  -33.135  -25.580  1.00 51.67  ? 406 MET   B N      1 
ATOM   6568  C  CA     . MET   B 2  406 ? 32.984  -33.661  -26.872  1.00 46.42  ? 406 MET   B CA     1 
ATOM   6569  C  C      . MET   B 2  406 ? 32.378  -35.024  -27.120  1.00 49.89  ? 406 MET   B C      1 
ATOM   6570  O  O      . MET   B 2  406 ? 31.876  -35.304  -28.215  1.00 51.79  ? 406 MET   B O      1 
ATOM   6571  C  CB     . MET   B 2  406 ? 34.505  -33.741  -26.946  1.00 46.61  ? 406 MET   B CB     1 
ATOM   6572  C  CG     . MET   B 2  406 ? 35.040  -33.470  -28.346  1.00 62.62  ? 406 MET   B CG     1 
ATOM   6573  S  SD     . MET   B 2  406 ? 36.844  -33.367  -28.436  1.00 103.23 ? 406 MET   B SD     1 
ATOM   6574  C  CE     . MET   B 2  406 ? 37.360  -34.566  -27.192  1.00 74.47  ? 406 MET   B CE     1 
ATOM   6575  N  N      . GLU   B 2  407 ? 32.393  -35.882  -26.101  1.00 49.27  ? 407 GLU   B N      1 
ATOM   6576  C  CA     . GLU   B 2  407 ? 31.879  -37.231  -26.265  1.00 43.35  ? 407 GLU   B CA     1 
ATOM   6577  C  C      . GLU   B 2  407 ? 30.428  -37.228  -26.720  1.00 44.31  ? 407 GLU   B C      1 
ATOM   6578  O  O      . GLU   B 2  407 ? 29.988  -38.154  -27.413  1.00 44.91  ? 407 GLU   B O      1 
ATOM   6579  C  CB     . GLU   B 2  407 ? 32.023  -37.990  -24.965  1.00 35.56  ? 407 GLU   B CB     1 
ATOM   6580  C  CG     . GLU   B 2  407 ? 31.635  -39.407  -25.130  1.00 40.10  ? 407 GLU   B CG     1 
ATOM   6581  C  CD     . GLU   B 2  407 ? 32.397  -40.299  -24.241  1.00 41.41  ? 407 GLU   B CD     1 
ATOM   6582  O  OE1    . GLU   B 2  407 ? 33.283  -39.815  -23.507  1.00 45.31  ? 407 GLU   B OE1    1 
ATOM   6583  O  OE2    . GLU   B 2  407 ? 32.093  -41.498  -24.271  1.00 48.75  ? 407 GLU   B OE2    1 
ATOM   6584  N  N      . PHE   B 2  408 ? 29.679  -36.197  -26.342  1.00 44.97  ? 408 PHE   B N      1 
ATOM   6585  C  CA     . PHE   B 2  408 ? 28.284  -36.087  -26.736  1.00 46.65  ? 408 PHE   B CA     1 
ATOM   6586  C  C      . PHE   B 2  408 ? 28.189  -35.648  -28.175  1.00 45.65  ? 408 PHE   B C      1 
ATOM   6587  O  O      . PHE   B 2  408 ? 27.378  -36.188  -28.935  1.00 50.61  ? 408 PHE   B O      1 
ATOM   6588  C  CB     . PHE   B 2  408 ? 27.537  -35.097  -25.826  1.00 45.15  ? 408 PHE   B CB     1 
ATOM   6589  C  CG     . PHE   B 2  408 ? 27.168  -35.668  -24.470  1.00 42.99  ? 408 PHE   B CG     1 
ATOM   6590  C  CD1    . PHE   B 2  408 ? 28.150  -36.012  -23.552  1.00 36.27  ? 408 PHE   B CD1    1 
ATOM   6591  C  CD2    . PHE   B 2  408 ? 25.829  -35.870  -24.123  1.00 47.12  ? 408 PHE   B CD2    1 
ATOM   6592  C  CE1    . PHE   B 2  408 ? 27.814  -36.528  -22.325  1.00 39.74  ? 408 PHE   B CE1    1 
ATOM   6593  C  CE2    . PHE   B 2  408 ? 25.480  -36.391  -22.879  1.00 40.93  ? 408 PHE   B CE2    1 
ATOM   6594  C  CZ     . PHE   B 2  408 ? 26.475  -36.721  -21.983  1.00 42.16  ? 408 PHE   B CZ     1 
ATOM   6595  N  N      . THR   B 2  409 ? 29.023  -34.677  -28.559  1.00 48.30  ? 409 THR   B N      1 
ATOM   6596  C  CA     . THR   B 2  409 ? 29.060  -34.224  -29.949  1.00 47.64  ? 409 THR   B CA     1 
ATOM   6597  C  C      . THR   B 2  409 ? 29.402  -35.372  -30.893  1.00 39.32  ? 409 THR   B C      1 
ATOM   6598  O  O      . THR   B 2  409 ? 28.816  -35.485  -31.970  1.00 42.61  ? 409 THR   B O      1 
ATOM   6599  C  CB     . THR   B 2  409 ? 30.054  -33.063  -30.091  1.00 42.48  ? 409 THR   B CB     1 
ATOM   6600  O  OG1    . THR   B 2  409 ? 29.609  -31.966  -29.290  1.00 45.19  ? 409 THR   B OG1    1 
ATOM   6601  C  CG2    . THR   B 2  409 ? 30.154  -32.591  -31.516  1.00 40.37  ? 409 THR   B CG2    1 
ATOM   6602  N  N      . GLU   B 2  410 ? 30.333  -36.249  -30.499  1.00 41.08  ? 410 GLU   B N      1 
ATOM   6603  C  CA     . GLU   B 2  410 ? 30.648  -37.411  -31.333  1.00 48.12  ? 410 GLU   B CA     1 
ATOM   6604  C  C      . GLU   B 2  410 ? 29.457  -38.364  -31.442  1.00 48.26  ? 410 GLU   B C      1 
ATOM   6605  O  O      . GLU   B 2  410 ? 29.072  -38.760  -32.546  1.00 44.26  ? 410 GLU   B O      1 
ATOM   6606  C  CB     . GLU   B 2  410 ? 31.871  -38.152  -30.794  1.00 44.80  ? 410 GLU   B CB     1 
ATOM   6607  C  CG     . GLU   B 2  410 ? 33.152  -37.365  -30.909  1.00 56.31  ? 410 GLU   B CG     1 
ATOM   6608  C  CD     . GLU   B 2  410 ? 34.221  -37.838  -29.932  1.00 64.79  ? 410 GLU   B CD     1 
ATOM   6609  O  OE1    . GLU   B 2  410 ? 34.061  -38.944  -29.350  1.00 63.26  ? 410 GLU   B OE1    1 
ATOM   6610  O  OE2    . GLU   B 2  410 ? 35.203  -37.086  -29.724  1.00 60.03  ? 410 GLU   B OE2    1 
ATOM   6611  N  N      . ALA   B 2  411 ? 28.868  -38.755  -30.302  1.00 47.80  ? 411 ALA   B N      1 
ATOM   6612  C  CA     . ALA   B 2  411 ? 27.710  -39.643  -30.341  1.00 44.14  ? 411 ALA   B CA     1 
ATOM   6613  C  C      . ALA   B 2  411 ? 26.574  -39.022  -31.151  1.00 43.01  ? 411 ALA   B C      1 
ATOM   6614  O  O      . ALA   B 2  411 ? 26.004  -39.668  -32.038  1.00 40.90  ? 411 ALA   B O      1 
ATOM   6615  C  CB     . ALA   B 2  411 ? 27.253  -39.987  -28.921  1.00 38.60  ? 411 ALA   B CB     1 
ATOM   6616  N  N      . GLU   B 2  412 ? 26.234  -37.761  -30.864  1.00 37.06  ? 412 GLU   B N      1 
ATOM   6617  C  CA     . GLU   B 2  412 ? 25.226  -37.077  -31.666  1.00 39.67  ? 412 GLU   B CA     1 
ATOM   6618  C  C      . GLU   B 2  412 ? 25.561  -37.172  -33.142  1.00 44.18  ? 412 GLU   B C      1 
ATOM   6619  O  O      . GLU   B 2  412 ? 24.700  -37.464  -33.979  1.00 46.96  ? 412 GLU   B O      1 
ATOM   6620  C  CB     . GLU   B 2  412 ? 25.126  -35.619  -31.240  1.00 39.27  ? 412 GLU   B CB     1 
ATOM   6621  C  CG     . GLU   B 2  412 ? 24.194  -34.730  -32.068  1.00 45.02  ? 412 GLU   B CG     1 
ATOM   6622  C  CD     . GLU   B 2  412 ? 24.521  -33.239  -31.868  1.00 56.74  ? 412 GLU   B CD     1 
ATOM   6623  O  OE1    . GLU   B 2  412 ? 25.716  -32.885  -32.023  1.00 61.66  ? 412 GLU   B OE1    1 
ATOM   6624  O  OE2    . GLU   B 2  412 ? 23.615  -32.422  -31.546  1.00 51.50  ? 412 GLU   B OE2    1 
ATOM   6625  N  N      . SER   B 2  413 ? 26.830  -36.974  -33.462  1.00 45.05  ? 413 SER   B N      1 
ATOM   6626  C  CA     . SER   B 2  413 ? 27.277  -36.891  -34.838  1.00 38.61  ? 413 SER   B CA     1 
ATOM   6627  C  C      . SER   B 2  413 ? 27.220  -38.261  -35.511  1.00 44.21  ? 413 SER   B C      1 
ATOM   6628  O  O      . SER   B 2  413 ? 26.787  -38.382  -36.663  1.00 39.05  ? 413 SER   B O      1 
ATOM   6629  C  CB     . SER   B 2  413 ? 28.688  -36.326  -34.823  1.00 35.71  ? 413 SER   B CB     1 
ATOM   6630  O  OG     . SER   B 2  413 ? 28.905  -35.497  -35.915  1.00 42.58  ? 413 SER   B OG     1 
ATOM   6631  N  N      . ASN   B 2  414 ? 27.629  -39.313  -34.793  1.00 40.62  ? 414 ASN   B N      1 
ATOM   6632  C  CA     . ASN   B 2  414 ? 27.587  -40.648  -35.360  1.00 39.74  ? 414 ASN   B CA     1 
ATOM   6633  C  C      . ASN   B 2  414 ? 26.159  -41.045  -35.701  1.00 50.17  ? 414 ASN   B C      1 
ATOM   6634  O  O      . ASN   B 2  414 ? 25.915  -41.685  -36.740  1.00 46.15  ? 414 ASN   B O      1 
ATOM   6635  C  CB     . ASN   B 2  414 ? 28.204  -41.666  -34.402  1.00 49.53  ? 414 ASN   B CB     1 
ATOM   6636  C  CG     . ASN   B 2  414 ? 28.613  -42.971  -35.113  1.00 56.68  ? 414 ASN   B CG     1 
ATOM   6637  O  OD1    . ASN   B 2  414 ? 28.716  -43.016  -36.349  1.00 52.84  ? 414 ASN   B OD1    1 
ATOM   6638  N  ND2    . ASN   B 2  414 ? 28.835  -44.033  -34.332  1.00 53.80  ? 414 ASN   B ND2    1 
ATOM   6639  N  N      . MET   B 2  415 ? 25.195  -40.659  -34.844  1.00 45.01  ? 415 MET   B N      1 
ATOM   6640  C  CA     . MET   B 2  415 ? 23.803  -41.008  -35.101  1.00 38.98  ? 415 MET   B CA     1 
ATOM   6641  C  C      . MET   B 2  415 ? 23.251  -40.262  -36.300  1.00 46.86  ? 415 MET   B C      1 
ATOM   6642  O  O      . MET   B 2  415 ? 22.529  -40.846  -37.115  1.00 48.29  ? 415 MET   B O      1 
ATOM   6643  C  CB     . MET   B 2  415 ? 22.915  -40.720  -33.906  1.00 39.88  ? 415 MET   B CB     1 
ATOM   6644  C  CG     . MET   B 2  415 ? 21.718  -41.614  -33.979  1.00 38.64  ? 415 MET   B CG     1 
ATOM   6645  S  SD     . MET   B 2  415 ? 20.890  -41.777  -32.417  1.00 49.23  ? 415 MET   B SD     1 
ATOM   6646  C  CE     . MET   B 2  415 ? 20.785  -40.049  -31.964  1.00 47.27  ? 415 MET   B CE     1 
ATOM   6647  N  N      . ASN   B 2  416 ? 23.531  -38.962  -36.406  1.00 45.30  ? 416 ASN   B N      1 
ATOM   6648  C  CA     . ASN   B 2  416 ? 23.099  -38.244  -37.597  1.00 42.39  ? 416 ASN   B CA     1 
ATOM   6649  C  C      . ASN   B 2  416 ? 23.730  -38.849  -38.851  1.00 47.52  ? 416 ASN   B C      1 
ATOM   6650  O  O      . ASN   B 2  416 ? 23.064  -38.988  -39.884  1.00 45.84  ? 416 ASN   B O      1 
ATOM   6651  C  CB     . ASN   B 2  416 ? 23.408  -36.763  -37.447  1.00 37.19  ? 416 ASN   B CB     1 
ATOM   6652  C  CG     . ASN   B 2  416 ? 22.566  -36.112  -36.347  1.00 50.63  ? 416 ASN   B CG     1 
ATOM   6653  O  OD1    . ASN   B 2  416 ? 21.439  -36.560  -36.070  1.00 46.23  ? 416 ASN   B OD1    1 
ATOM   6654  N  ND2    . ASN   B 2  416 ? 23.104  -35.054  -35.710  1.00 51.78  ? 416 ASN   B ND2    1 
ATOM   6655  N  N      . ASP   B 2  417 ? 24.993  -39.276  -38.765  1.00 43.68  ? 417 ASP   B N      1 
ATOM   6656  C  CA     . ASP   B 2  417 ? 25.573  -40.059  -39.847  1.00 42.06  ? 417 ASP   B CA     1 
ATOM   6657  C  C      . ASP   B 2  417 ? 24.737  -41.301  -40.141  1.00 49.19  ? 417 ASP   B C      1 
ATOM   6658  O  O      . ASP   B 2  417 ? 24.388  -41.566  -41.299  1.00 46.58  ? 417 ASP   B O      1 
ATOM   6659  C  CB     . ASP   B 2  417 ? 26.995  -40.463  -39.500  1.00 44.37  ? 417 ASP   B CB     1 
ATOM   6660  C  CG     . ASP   B 2  417 ? 27.946  -39.301  -39.523  1.00 46.44  ? 417 ASP   B CG     1 
ATOM   6661  O  OD1    . ASP   B 2  417 ? 27.533  -38.212  -39.986  1.00 46.59  ? 417 ASP   B OD1    1 
ATOM   6662  O  OD2    . ASP   B 2  417 ? 29.106  -39.485  -39.070  1.00 45.30  ? 417 ASP   B OD2    1 
ATOM   6663  N  N      . LEU   B 2  418 ? 24.424  -42.093  -39.103  1.00 47.77  ? 418 LEU   B N      1 
ATOM   6664  C  CA     . LEU   B 2  418 ? 23.630  -43.301  -39.316  1.00 42.41  ? 418 LEU   B CA     1 
ATOM   6665  C  C      . LEU   B 2  418 ? 22.351  -42.975  -40.061  1.00 45.25  ? 418 LEU   B C      1 
ATOM   6666  O  O      . LEU   B 2  418 ? 21.959  -43.700  -40.984  1.00 48.45  ? 418 LEU   B O      1 
ATOM   6667  C  CB     . LEU   B 2  418 ? 23.304  -43.991  -37.986  1.00 42.51  ? 418 LEU   B CB     1 
ATOM   6668  C  CG     . LEU   B 2  418 ? 22.455  -45.273  -38.077  1.00 43.64  ? 418 LEU   B CG     1 
ATOM   6669  C  CD1    . LEU   B 2  418 ? 23.182  -46.353  -38.840  1.00 45.03  ? 418 LEU   B CD1    1 
ATOM   6670  C  CD2    . LEU   B 2  418 ? 22.000  -45.828  -36.728  1.00 39.44  ? 418 LEU   B CD2    1 
ATOM   6671  N  N      . VAL   B 2  419 ? 21.695  -41.873  -39.694  1.00 43.63  ? 419 VAL   B N      1 
ATOM   6672  C  CA     . VAL   B 2  419 ? 20.442  -41.527  -40.352  1.00 43.27  ? 419 VAL   B CA     1 
ATOM   6673  C  C      . VAL   B 2  419 ? 20.695  -41.134  -41.801  1.00 46.59  ? 419 VAL   B C      1 
ATOM   6674  O  O      . VAL   B 2  419 ? 19.876  -41.424  -42.680  1.00 50.44  ? 419 VAL   B O      1 
ATOM   6675  C  CB     . VAL   B 2  419 ? 19.710  -40.416  -39.578  1.00 44.47  ? 419 VAL   B CB     1 
ATOM   6676  C  CG1    . VAL   B 2  419 ? 18.630  -39.792  -40.439  1.00 49.88  ? 419 VAL   B CG1    1 
ATOM   6677  C  CG2    . VAL   B 2  419 ? 19.083  -40.968  -38.314  1.00 44.21  ? 419 VAL   B CG2    1 
ATOM   6678  N  N      . SER   B 2  420 ? 21.821  -40.474  -42.079  1.00 44.37  ? 420 SER   B N      1 
ATOM   6679  C  CA     . SER   B 2  420 ? 22.166  -40.151  -43.459  1.00 44.04  ? 420 SER   B CA     1 
ATOM   6680  C  C      . SER   B 2  420 ? 22.389  -41.418  -44.266  1.00 48.75  ? 420 SER   B C      1 
ATOM   6681  O  O      . SER   B 2  420 ? 21.970  -41.515  -45.424  1.00 45.16  ? 420 SER   B O      1 
ATOM   6682  C  CB     . SER   B 2  420 ? 23.414  -39.274  -43.491  1.00 44.92  ? 420 SER   B CB     1 
ATOM   6683  O  OG     . SER   B 2  420 ? 23.227  -38.132  -42.680  1.00 55.98  ? 420 SER   B OG     1 
ATOM   6684  N  N      . GLU   B 2  421 ? 23.038  -42.406  -43.657  1.00 49.89  ? 421 GLU   B N      1 
ATOM   6685  C  CA     . GLU   B 2  421 ? 23.282  -43.660  -44.346  1.00 50.55  ? 421 GLU   B CA     1 
ATOM   6686  C  C      . GLU   B 2  421 ? 21.971  -44.376  -44.668  1.00 55.06  ? 421 GLU   B C      1 
ATOM   6687  O  O      . GLU   B 2  421 ? 21.773  -44.856  -45.793  1.00 56.26  ? 421 GLU   B O      1 
ATOM   6688  C  CB     . GLU   B 2  421 ? 24.206  -44.534  -43.504  1.00 48.53  ? 421 GLU   B CB     1 
ATOM   6689  C  CG     . GLU   B 2  421 ? 25.001  -45.525  -44.312  1.00 53.11  ? 421 GLU   B CG     1 
ATOM   6690  C  CD     . GLU   B 2  421 ? 25.803  -46.452  -43.433  1.00 59.57  ? 421 GLU   B CD     1 
ATOM   6691  O  OE1    . GLU   B 2  421 ? 26.227  -45.965  -42.339  1.00 54.16  ? 421 GLU   B OE1    1 
ATOM   6692  O  OE2    . GLU   B 2  421 ? 26.003  -47.641  -43.839  1.00 50.66  ? 421 GLU   B OE2    1 
ATOM   6693  N  N      . TYR   B 2  422 ? 21.056  -44.467  -43.699  1.00 47.35  ? 422 TYR   B N      1 
ATOM   6694  C  CA     . TYR   B 2  422 ? 19.764  -45.056  -44.034  1.00 45.67  ? 422 TYR   B CA     1 
ATOM   6695  C  C      . TYR   B 2  422 ? 19.084  -44.249  -45.137  1.00 54.52  ? 422 TYR   B C      1 
ATOM   6696  O  O      . TYR   B 2  422 ? 18.363  -44.807  -45.969  1.00 54.80  ? 422 TYR   B O      1 
ATOM   6697  C  CB     . TYR   B 2  422 ? 18.877  -45.157  -42.789  1.00 42.83  ? 422 TYR   B CB     1 
ATOM   6698  C  CG     . TYR   B 2  422 ? 19.068  -46.441  -41.989  1.00 44.33  ? 422 TYR   B CG     1 
ATOM   6699  C  CD1    . TYR   B 2  422 ? 18.789  -47.671  -42.549  1.00 41.69  ? 422 TYR   B CD1    1 
ATOM   6700  C  CD2    . TYR   B 2  422 ? 19.531  -46.419  -40.674  1.00 39.45  ? 422 TYR   B CD2    1 
ATOM   6701  C  CE1    . TYR   B 2  422 ? 18.955  -48.838  -41.837  1.00 40.10  ? 422 TYR   B CE1    1 
ATOM   6702  C  CE2    . TYR   B 2  422 ? 19.702  -47.595  -39.947  1.00 34.54  ? 422 TYR   B CE2    1 
ATOM   6703  C  CZ     . TYR   B 2  422 ? 19.413  -48.807  -40.538  1.00 43.52  ? 422 TYR   B CZ     1 
ATOM   6704  O  OH     . TYR   B 2  422 ? 19.559  -50.022  -39.860  1.00 47.75  ? 422 TYR   B OH     1 
ATOM   6705  N  N      . GLN   B 2  423 ? 19.345  -42.944  -45.197  1.00 54.15  ? 423 GLN   B N      1 
ATOM   6706  C  CA     . GLN   B 2  423 ? 18.688  -42.113  -46.196  1.00 57.37  ? 423 GLN   B CA     1 
ATOM   6707  C  C      . GLN   B 2  423 ? 19.260  -42.344  -47.585  1.00 64.95  ? 423 GLN   B C      1 
ATOM   6708  O  O      . GLN   B 2  423 ? 18.540  -42.201  -48.587  1.00 67.46  ? 423 GLN   B O      1 
ATOM   6709  C  CB     . GLN   B 2  423 ? 18.820  -40.639  -45.813  1.00 60.84  ? 423 GLN   B CB     1 
ATOM   6710  C  CG     . GLN   B 2  423 ? 17.516  -40.001  -45.373  1.00 69.98  ? 423 GLN   B CG     1 
ATOM   6711  C  CD     . GLN   B 2  423 ? 16.533  -39.879  -46.523  1.00 75.60  ? 423 GLN   B CD     1 
ATOM   6712  O  OE1    . GLN   B 2  423 ? 16.916  -39.973  -47.701  1.00 77.39  ? 423 GLN   B OE1    1 
ATOM   6713  N  NE2    . GLN   B 2  423 ? 15.258  -39.673  -46.193  1.00 72.37  ? 423 GLN   B NE2    1 
ATOM   6714  N  N      . GLN   B 2  424 ? 20.552  -42.683  -47.661  1.00 60.58  ? 424 GLN   B N      1 
ATOM   6715  C  CA     . GLN   B 2  424 ? 21.199  -42.947  -48.941  1.00 53.76  ? 424 GLN   B CA     1 
ATOM   6716  C  C      . GLN   B 2  424 ? 20.486  -44.051  -49.717  1.00 63.07  ? 424 GLN   B C      1 
ATOM   6717  O  O      . GLN   B 2  424 ? 20.241  -43.920  -50.922  1.00 69.07  ? 424 GLN   B O      1 
ATOM   6718  C  CB     . GLN   B 2  424 ? 22.651  -43.325  -48.691  1.00 56.88  ? 424 GLN   B CB     1 
ATOM   6719  C  CG     . GLN   B 2  424 ? 23.328  -44.038  -49.828  1.00 61.29  ? 424 GLN   B CG     1 
ATOM   6720  C  CD     . GLN   B 2  424 ? 24.772  -44.348  -49.498  1.00 67.51  ? 424 GLN   B CD     1 
ATOM   6721  O  OE1    . GLN   B 2  424 ? 25.122  -44.544  -48.321  1.00 63.23  ? 424 GLN   B OE1    1 
ATOM   6722  N  NE2    . GLN   B 2  424 ? 25.636  -44.354  -50.528  1.00 64.65  ? 424 GLN   B NE2    1 
ATOM   6723  N  N      . TYR   B 2  425 ? 20.145  -45.151  -49.041  1.00 59.63  ? 425 TYR   B N      1 
ATOM   6724  C  CA     . TYR   B 2  425 ? 19.594  -46.324  -49.702  1.00 56.84  ? 425 TYR   B CA     1 
ATOM   6725  C  C      . TYR   B 2  425 ? 18.094  -46.244  -49.920  1.00 63.56  ? 425 TYR   B C      1 
ATOM   6726  O  O      . TYR   B 2  425 ? 17.549  -47.066  -50.667  1.00 68.68  ? 425 TYR   B O      1 
ATOM   6727  C  CB     . TYR   B 2  425 ? 19.960  -47.563  -48.897  1.00 50.47  ? 425 TYR   B CB     1 
ATOM   6728  C  CG     . TYR   B 2  425 ? 21.449  -47.693  -48.791  1.00 54.52  ? 425 TYR   B CG     1 
ATOM   6729  C  CD1    . TYR   B 2  425 ? 22.210  -48.023  -49.903  1.00 48.89  ? 425 TYR   B CD1    1 
ATOM   6730  C  CD2    . TYR   B 2  425 ? 22.105  -47.459  -47.593  1.00 57.28  ? 425 TYR   B CD2    1 
ATOM   6731  C  CE1    . TYR   B 2  425 ? 23.580  -48.133  -49.821  1.00 49.27  ? 425 TYR   B CE1    1 
ATOM   6732  C  CE2    . TYR   B 2  425 ? 23.483  -47.567  -47.499  1.00 53.27  ? 425 TYR   B CE2    1 
ATOM   6733  C  CZ     . TYR   B 2  425 ? 24.216  -47.904  -48.618  1.00 54.33  ? 425 TYR   B CZ     1 
ATOM   6734  O  OH     . TYR   B 2  425 ? 25.590  -48.013  -48.523  1.00 58.72  ? 425 TYR   B OH     1 
ATOM   6735  N  N      . GLN   B 2  426 ? 17.419  -45.275  -49.304  1.00 66.45  ? 426 GLN   B N      1 
ATOM   6736  C  CA     . GLN   B 2  426 ? 16.009  -45.041  -49.574  1.00 62.62  ? 426 GLN   B CA     1 
ATOM   6737  C  C      . GLN   B 2  426 ? 15.790  -44.424  -50.938  1.00 70.16  ? 426 GLN   B C      1 
ATOM   6738  O  O      . GLN   B 2  426 ? 14.655  -44.397  -51.422  1.00 72.09  ? 426 GLN   B O      1 
ATOM   6739  C  CB     . GLN   B 2  426 ? 15.415  -44.135  -48.501  1.00 67.32  ? 426 GLN   B CB     1 
ATOM   6740  C  CG     . GLN   B 2  426 ? 14.154  -44.677  -47.903  1.00 68.12  ? 426 GLN   B CG     1 
ATOM   6741  C  CD     . GLN   B 2  426 ? 13.702  -43.884  -46.707  1.00 69.39  ? 426 GLN   B CD     1 
ATOM   6742  O  OE1    . GLN   B 2  426 ? 14.041  -44.205  -45.563  1.00 66.51  ? 426 GLN   B OE1    1 
ATOM   6743  N  NE2    . GLN   B 2  426 ? 12.950  -42.818  -46.966  1.00 74.84  ? 426 GLN   B NE2    1 
ATOM   6744  N  N      . ASP   B 2  427 ? 16.847  -43.925  -51.567  1.00 76.75  ? 427 ASP   B N      1 
ATOM   6745  C  CA     . ASP   B 2  427 ? 16.761  -43.381  -52.914  1.00 82.37  ? 427 ASP   B CA     1 
ATOM   6746  C  C      . ASP   B 2  427 ? 17.440  -44.252  -53.966  1.00 84.37  ? 427 ASP   B C      1 
ATOM   6747  O  O      . ASP   B 2  427 ? 16.982  -44.282  -55.113  1.00 84.48  ? 427 ASP   B O      1 
ATOM   6748  C  CB     . ASP   B 2  427 ? 17.355  -41.968  -52.925  1.00 79.34  ? 427 ASP   B CB     1 
ATOM   6749  C  CG     . ASP   B 2  427 ? 16.643  -41.035  -51.934  1.00 88.28  ? 427 ASP   B CG     1 
ATOM   6750  O  OD1    . ASP   B 2  427 ? 15.469  -41.316  -51.573  1.00 85.58  ? 427 ASP   B OD1    1 
ATOM   6751  O  OD2    . ASP   B 2  427 ? 17.269  -40.046  -51.487  1.00 86.48  ? 427 ASP   B OD2    1 
ATOM   6752  N  N      . ALA   B 2  428 ? 18.476  -45.002  -53.587  1.00 84.36  ? 428 ALA   B N      1 
ATOM   6753  C  CA     . ALA   B 2  428 ? 19.209  -45.890  -54.496  1.00 80.97  ? 428 ALA   B CA     1 
ATOM   6754  C  C      . ALA   B 2  428 ? 18.288  -46.715  -55.401  1.00 80.30  ? 428 ALA   B C      1 
ATOM   6755  O  O      . ALA   B 2  428 ? 18.698  -47.158  -56.482  1.00 84.77  ? 428 ALA   B O      1 
ATOM   6756  C  CB     . ALA   B 2  428 ? 20.128  -46.818  -53.685  1.00 68.01  ? 428 ALA   B CB     1 
ATOM   6757  N  N      . MET   C 1  1   ? 19.835  -50.720  1.384    1.00 81.12  ? 1   MET   C N      1 
ATOM   6758  C  CA     . MET   C 1  1   ? 20.595  -49.859  2.284    1.00 66.28  ? 1   MET   C CA     1 
ATOM   6759  C  C      . MET   C 1  1   ? 20.083  -48.488  1.992    1.00 62.33  ? 1   MET   C C      1 
ATOM   6760  O  O      . MET   C 1  1   ? 18.959  -48.149  2.357    1.00 71.09  ? 1   MET   C O      1 
ATOM   6761  C  CB     . MET   C 1  1   ? 22.104  -49.935  2.034    1.00 59.91  ? 1   MET   C CB     1 
ATOM   6762  C  CG     . MET   C 1  1   ? 22.618  -51.351  1.727    1.00 68.01  ? 1   MET   C CG     1 
ATOM   6763  S  SD     . MET   C 1  1   ? 24.079  -51.374  0.648    1.00 78.49  ? 1   MET   C SD     1 
ATOM   6764  C  CE     . MET   C 1  1   ? 23.504  -50.329  -0.701   1.00 63.34  ? 1   MET   C CE     1 
ATOM   6765  N  N      . ARG   C 1  2   ? 20.903  -47.716  1.286    1.00 58.68  ? 2   ARG   C N      1 
ATOM   6766  C  CA     . ARG   C 1  2   ? 20.538  -46.375  0.863    1.00 55.06  ? 2   ARG   C CA     1 
ATOM   6767  C  C      . ARG   C 1  2   ? 20.009  -45.571  2.052    1.00 48.70  ? 2   ARG   C C      1 
ATOM   6768  O  O      . ARG   C 1  2   ? 18.931  -44.982  2.006    1.00 55.03  ? 2   ARG   C O      1 
ATOM   6769  C  CB     . ARG   C 1  2   ? 19.520  -46.446  -0.278   1.00 57.92  ? 2   ARG   C CB     1 
ATOM   6770  C  CG     . ARG   C 1  2   ? 19.947  -47.341  -1.451   1.00 66.44  ? 2   ARG   C CG     1 
ATOM   6771  C  CD     . ARG   C 1  2   ? 20.749  -46.591  -2.515   1.00 64.75  ? 2   ARG   C CD     1 
ATOM   6772  N  NE     . ARG   C 1  2   ? 22.158  -46.578  -2.136   1.00 70.92  ? 2   ARG   C NE     1 
ATOM   6773  C  CZ     . ARG   C 1  2   ? 23.014  -45.613  -2.455   1.00 69.57  ? 2   ARG   C CZ     1 
ATOM   6774  N  NH1    . ARG   C 1  2   ? 22.686  -44.636  -3.297   1.00 68.98  ? 2   ARG   C NH1    1 
ATOM   6775  N  NH2    . ARG   C 1  2   ? 24.221  -45.614  -1.901   1.00 58.17  ? 2   ARG   C NH2    1 
ATOM   6776  N  N      . GLU   C 1  3   ? 20.779  -45.565  3.136    1.00 40.95  ? 3   GLU   C N      1 
ATOM   6777  C  CA     . GLU   C 1  3   ? 20.409  -44.865  4.364    1.00 42.23  ? 3   GLU   C CA     1 
ATOM   6778  C  C      . GLU   C 1  3   ? 20.638  -43.364  4.222    1.00 38.69  ? 3   GLU   C C      1 
ATOM   6779  O  O      . GLU   C 1  3   ? 21.596  -42.925  3.589    1.00 38.08  ? 3   GLU   C O      1 
ATOM   6780  C  CB     . GLU   C 1  3   ? 21.230  -45.380  5.560    1.00 44.15  ? 3   GLU   C CB     1 
ATOM   6781  C  CG     . GLU   C 1  3   ? 21.188  -46.892  5.782    1.00 39.63  ? 3   GLU   C CG     1 
ATOM   6782  C  CD     . GLU   C 1  3   ? 22.511  -47.569  5.417    1.00 46.59  ? 3   GLU   C CD     1 
ATOM   6783  O  OE1    . GLU   C 1  3   ? 23.156  -47.145  4.427    1.00 44.63  ? 3   GLU   C OE1    1 
ATOM   6784  O  OE2    . GLU   C 1  3   ? 22.887  -48.558  6.083    1.00 49.12  ? 3   GLU   C OE2    1 
ATOM   6785  N  N      . CYS   C 1  4   ? 19.756  -42.571  4.831    1.00 40.39  ? 4   CYS   C N      1 
ATOM   6786  C  CA     . CYS   C 1  4   ? 19.890  -41.115  4.858    1.00 37.07  ? 4   CYS   C CA     1 
ATOM   6787  C  C      . CYS   C 1  4   ? 20.078  -40.670  6.301    1.00 38.30  ? 4   CYS   C C      1 
ATOM   6788  O  O      . CYS   C 1  4   ? 19.319  -41.083  7.184    1.00 41.13  ? 4   CYS   C O      1 
ATOM   6789  C  CB     . CYS   C 1  4   ? 18.657  -40.407  4.284    1.00 34.61  ? 4   CYS   C CB     1 
ATOM   6790  S  SG     . CYS   C 1  4   ? 18.091  -41.021  2.669    1.00 53.63  ? 4   CYS   C SG     1 
ATOM   6791  N  N      . ILE   C 1  5   ? 21.063  -39.816  6.543    1.00 36.26  ? 5   ILE   C N      1 
ATOM   6792  C  CA     . ILE   C 1  5   ? 21.213  -39.147  7.828    1.00 38.49  ? 5   ILE   C CA     1 
ATOM   6793  C  C      . ILE   C 1  5   ? 20.578  -37.762  7.742    1.00 36.20  ? 5   ILE   C C      1 
ATOM   6794  O  O      . ILE   C 1  5   ? 20.841  -37.000  6.802    1.00 35.45  ? 5   ILE   C O      1 
ATOM   6795  C  CB     . ILE   C 1  5   ? 22.689  -39.049  8.241    1.00 37.41  ? 5   ILE   C CB     1 
ATOM   6796  C  CG1    . ILE   C 1  5   ? 23.236  -40.442  8.527    1.00 36.77  ? 5   ILE   C CG1    1 
ATOM   6797  C  CG2    . ILE   C 1  5   ? 22.838  -38.118  9.439    1.00 32.41  ? 5   ILE   C CG2    1 
ATOM   6798  C  CD1    . ILE   C 1  5   ? 24.713  -40.600  8.225    1.00 31.00  ? 5   ILE   C CD1    1 
ATOM   6799  N  N      . SER   C 1  6   ? 19.732  -37.443  8.714    1.00 35.62  ? 6   SER   C N      1 
ATOM   6800  C  CA     . SER   C 1  6   ? 19.118  -36.130  8.823    1.00 34.17  ? 6   SER   C CA     1 
ATOM   6801  C  C      . SER   C 1  6   ? 19.871  -35.320  9.862    1.00 36.01  ? 6   SER   C C      1 
ATOM   6802  O  O      . SER   C 1  6   ? 20.190  -35.832  10.937   1.00 40.31  ? 6   SER   C O      1 
ATOM   6803  C  CB     . SER   C 1  6   ? 17.653  -36.269  9.222    1.00 35.39  ? 6   SER   C CB     1 
ATOM   6804  O  OG     . SER   C 1  6   ? 17.009  -37.168  8.343    1.00 39.60  ? 6   SER   C OG     1 
ATOM   6805  N  N      . ILE   C 1  7   ? 20.175  -34.069  9.536    1.00 35.05  ? 7   ILE   C N      1 
ATOM   6806  C  CA     . ILE   C 1  7   ? 20.779  -33.132  10.480   1.00 35.86  ? 7   ILE   C CA     1 
ATOM   6807  C  C      . ILE   C 1  7   ? 19.882  -31.913  10.662   1.00 39.92  ? 7   ILE   C C      1 
ATOM   6808  O  O      . ILE   C 1  7   ? 19.552  -31.218  9.687    1.00 36.80  ? 7   ILE   C O      1 
ATOM   6809  C  CB     . ILE   C 1  7   ? 22.194  -32.709  10.060   1.00 31.30  ? 7   ILE   C CB     1 
ATOM   6810  C  CG1    . ILE   C 1  7   ? 23.000  -33.926  9.658    1.00 35.29  ? 7   ILE   C CG1    1 
ATOM   6811  C  CG2    . ILE   C 1  7   ? 22.854  -31.881  11.127   1.00 33.58  ? 7   ILE   C CG2    1 
ATOM   6812  C  CD1    . ILE   C 1  7   ? 24.317  -33.545  9.086    1.00 37.89  ? 7   ILE   C CD1    1 
ATOM   6813  N  N      . HIS   C 1  8   ? 19.537  -31.639  11.931   1.00 36.78  ? 8   HIS   C N      1 
ATOM   6814  C  CA     . HIS   C 1  8   ? 18.599  -30.600  12.340   1.00 29.18  ? 8   HIS   C CA     1 
ATOM   6815  C  C      . HIS   C 1  8   ? 19.361  -29.542  13.111   1.00 30.86  ? 8   HIS   C C      1 
ATOM   6816  O  O      . HIS   C 1  8   ? 19.889  -29.819  14.190   1.00 36.86  ? 8   HIS   C O      1 
ATOM   6817  C  CB     . HIS   C 1  8   ? 17.481  -31.210  13.178   1.00 34.82  ? 8   HIS   C CB     1 
ATOM   6818  C  CG     . HIS   C 1  8   ? 16.800  -32.356  12.494   1.00 37.32  ? 8   HIS   C CG     1 
ATOM   6819  N  ND1    . HIS   C 1  8   ? 15.622  -32.216  11.795   1.00 34.26  ? 8   HIS   C ND1    1 
ATOM   6820  C  CD2    . HIS   C 1  8   ? 17.161  -33.656  12.365   1.00 38.31  ? 8   HIS   C CD2    1 
ATOM   6821  C  CE1    . HIS   C 1  8   ? 15.267  -33.386  11.295   1.00 37.96  ? 8   HIS   C CE1    1 
ATOM   6822  N  NE2    . HIS   C 1  8   ? 16.187  -34.276  11.624   1.00 36.60  ? 8   HIS   C NE2    1 
ATOM   6823  N  N      . VAL   C 1  9   ? 19.405  -28.334  12.566   1.00 30.04  ? 9   VAL   C N      1 
ATOM   6824  C  CA     . VAL   C 1  9   ? 20.339  -27.302  12.988   1.00 30.52  ? 9   VAL   C CA     1 
ATOM   6825  C  C      . VAL   C 1  9   ? 19.539  -26.080  13.408   1.00 32.71  ? 9   VAL   C C      1 
ATOM   6826  O  O      . VAL   C 1  9   ? 18.862  -25.469  12.573   1.00 33.71  ? 9   VAL   C O      1 
ATOM   6827  C  CB     . VAL   C 1  9   ? 21.324  -26.949  11.856   1.00 33.30  ? 9   VAL   C CB     1 
ATOM   6828  C  CG1    . VAL   C 1  9   ? 22.051  -25.633  12.123   1.00 34.57  ? 9   VAL   C CG1    1 
ATOM   6829  C  CG2    . VAL   C 1  9   ? 22.305  -28.093  11.602   1.00 31.22  ? 9   VAL   C CG2    1 
ATOM   6830  N  N      . GLY   C 1  10  ? 19.641  -25.709  14.698   1.00 34.41  ? 10  GLY   C N      1 
ATOM   6831  C  CA     . GLY   C 1  10  ? 19.018  -24.511  15.242   1.00 31.93  ? 10  GLY   C CA     1 
ATOM   6832  C  C      . GLY   C 1  10  ? 17.560  -24.735  15.620   1.00 31.74  ? 10  GLY   C C      1 
ATOM   6833  O  O      . GLY   C 1  10  ? 16.995  -25.819  15.461   1.00 34.40  ? 10  GLY   C O      1 
ATOM   6834  N  N      . GLN   C 1  11  ? 16.925  -23.678  16.114   1.00 25.76  ? 11  GLN   C N      1 
ATOM   6835  C  CA     . GLN   C 1  11  ? 15.563  -23.836  16.609   1.00 29.50  ? 11  GLN   C CA     1 
ATOM   6836  C  C      . GLN   C 1  11  ? 14.611  -24.358  15.529   1.00 33.44  ? 11  GLN   C C      1 
ATOM   6837  O  O      . GLN   C 1  11  ? 13.956  -25.390  15.715   1.00 36.18  ? 11  GLN   C O      1 
ATOM   6838  C  CB     . GLN   C 1  11  ? 15.047  -22.534  17.194   1.00 27.00  ? 11  GLN   C CB     1 
ATOM   6839  C  CG     . GLN   C 1  11  ? 13.769  -22.756  17.917   1.00 28.68  ? 11  GLN   C CG     1 
ATOM   6840  C  CD     . GLN   C 1  11  ? 13.135  -21.464  18.322   1.00 36.33  ? 11  GLN   C CD     1 
ATOM   6841  O  OE1    . GLN   C 1  11  ? 13.640  -20.757  19.200   1.00 41.32  ? 11  GLN   C OE1    1 
ATOM   6842  N  NE2    . GLN   C 1  11  ? 12.035  -21.113  17.655   1.00 34.15  ? 11  GLN   C NE2    1 
ATOM   6843  N  N      . ALA   C 1  12  ? 14.485  -23.645  14.408   1.00 28.23  ? 12  ALA   C N      1 
ATOM   6844  C  CA     . ALA   C 1  12  ? 13.600  -24.118  13.350   1.00 26.98  ? 12  ALA   C CA     1 
ATOM   6845  C  C      . ALA   C 1  12  ? 13.930  -25.559  12.974   1.00 35.79  ? 12  ALA   C C      1 
ATOM   6846  O  O      . ALA   C 1  12  ? 13.067  -26.447  13.058   1.00 36.17  ? 12  ALA   C O      1 
ATOM   6847  C  CB     . ALA   C 1  12  ? 13.672  -23.207  12.122   1.00 24.93  ? 12  ALA   C CB     1 
ATOM   6848  N  N      . GLY   C 1  13  ? 15.192  -25.809  12.583   1.00 28.38  ? 13  GLY   C N      1 
ATOM   6849  C  CA     . GLY   C 1  13  ? 15.600  -27.155  12.207   1.00 32.02  ? 13  GLY   C CA     1 
ATOM   6850  C  C      . GLY   C 1  13  ? 15.281  -28.211  13.253   1.00 32.68  ? 13  GLY   C C      1 
ATOM   6851  O  O      . GLY   C 1  13  ? 14.761  -29.276  12.934   1.00 32.78  ? 13  GLY   C O      1 
ATOM   6852  N  N      . VAL   C 1  14  ? 15.587  -27.934  14.520   1.00 34.14  ? 14  VAL   C N      1 
ATOM   6853  C  CA     . VAL   C 1  14  ? 15.314  -28.922  15.564   1.00 36.13  ? 14  VAL   C CA     1 
ATOM   6854  C  C      . VAL   C 1  14  ? 13.813  -29.142  15.708   1.00 35.61  ? 14  VAL   C C      1 
ATOM   6855  O  O      . VAL   C 1  14  ? 13.318  -30.269  15.617   1.00 39.82  ? 14  VAL   C O      1 
ATOM   6856  C  CB     . VAL   C 1  14  ? 15.950  -28.500  16.903   1.00 34.49  ? 14  VAL   C CB     1 
ATOM   6857  C  CG1    . VAL   C 1  14  ? 15.328  -29.315  18.058   1.00 33.97  ? 14  VAL   C CG1    1 
ATOM   6858  C  CG2    . VAL   C 1  14  ? 17.442  -28.689  16.859   1.00 28.33  ? 14  VAL   C CG2    1 
ATOM   6859  N  N      . GLN   C 1  15  ? 13.064  -28.072  15.947   1.00 36.07  ? 15  GLN   C N      1 
ATOM   6860  C  CA     . GLN   C 1  15  ? 11.618  -28.211  16.119   1.00 38.86  ? 15  GLN   C CA     1 
ATOM   6861  C  C      . GLN   C 1  15  ? 10.961  -28.854  14.896   1.00 39.82  ? 15  GLN   C C      1 
ATOM   6862  O  O      . GLN   C 1  15  ? 9.998   -29.616  15.034   1.00 37.07  ? 15  GLN   C O      1 
ATOM   6863  C  CB     . GLN   C 1  15  ? 11.002  -26.844  16.429   1.00 32.40  ? 15  GLN   C CB     1 
ATOM   6864  C  CG     . GLN   C 1  15  ? 11.300  -26.402  17.845   1.00 31.73  ? 15  GLN   C CG     1 
ATOM   6865  C  CD     . GLN   C 1  15  ? 10.774  -25.021  18.212   1.00 39.56  ? 15  GLN   C CD     1 
ATOM   6866  O  OE1    . GLN   C 1  15  ? 10.223  -24.303  17.380   1.00 41.32  ? 15  GLN   C OE1    1 
ATOM   6867  N  NE2    . GLN   C 1  15  ? 10.945  -24.645  19.483   1.00 42.92  ? 15  GLN   C NE2    1 
ATOM   6868  N  N      . ILE   C 1  16  ? 11.478  -28.600  13.691   1.00 39.35  ? 16  ILE   C N      1 
ATOM   6869  C  CA     . ILE   C 1  16  ? 10.871  -29.267  12.549   1.00 37.38  ? 16  ILE   C CA     1 
ATOM   6870  C  C      . ILE   C 1  16  ? 11.235  -30.747  12.553   1.00 37.92  ? 16  ILE   C C      1 
ATOM   6871  O  O      . ILE   C 1  16  ? 10.411  -31.592  12.181   1.00 37.94  ? 16  ILE   C O      1 
ATOM   6872  C  CB     . ILE   C 1  16  ? 11.253  -28.528  11.249   1.00 40.71  ? 16  ILE   C CB     1 
ATOM   6873  C  CG1    . ILE   C 1  16  ? 10.424  -27.243  11.150   1.00 33.36  ? 16  ILE   C CG1    1 
ATOM   6874  C  CG2    . ILE   C 1  16  ? 11.006  -29.380  10.007   1.00 34.27  ? 16  ILE   C CG2    1 
ATOM   6875  C  CD1    . ILE   C 1  16  ? 11.068  -26.169  10.360   1.00 33.15  ? 16  ILE   C CD1    1 
ATOM   6876  N  N      . GLY   C 1  17  ? 12.441  -31.095  13.028   1.00 38.77  ? 17  GLY   C N      1 
ATOM   6877  C  CA     . GLY   C 1  17  ? 12.784  -32.500  13.227   1.00 32.80  ? 17  GLY   C CA     1 
ATOM   6878  C  C      . GLY   C 1  17  ? 11.871  -33.214  14.213   1.00 37.08  ? 17  GLY   C C      1 
ATOM   6879  O  O      . GLY   C 1  17  ? 11.517  -34.380  14.012   1.00 39.11  ? 17  GLY   C O      1 
ATOM   6880  N  N      . ASN   C 1  18  ? 11.456  -32.530  15.280   1.00 38.82  ? 18  ASN   C N      1 
ATOM   6881  C  CA     . ASN   C 1  18  ? 10.474  -33.119  16.189   1.00 35.59  ? 18  ASN   C CA     1 
ATOM   6882  C  C      . ASN   C 1  18  ? 9.181   -33.449  15.468   1.00 35.72  ? 18  ASN   C C      1 
ATOM   6883  O  O      . ASN   C 1  18  ? 8.648   -34.555  15.596   1.00 40.28  ? 18  ASN   C O      1 
ATOM   6884  C  CB     . ASN   C 1  18  ? 10.201  -32.179  17.355   1.00 38.44  ? 18  ASN   C CB     1 
ATOM   6885  C  CG     . ASN   C 1  18  ? 11.274  -32.268  18.435   1.00 51.21  ? 18  ASN   C CG     1 
ATOM   6886  O  OD1    . ASN   C 1  18  ? 11.799  -31.238  18.874   1.00 50.49  ? 18  ASN   C OD1    1 
ATOM   6887  N  ND2    . ASN   C 1  18  ? 11.606  -33.508  18.871   1.00 48.15  ? 18  ASN   C ND2    1 
ATOM   6888  N  N      . ALA   C 1  19  ? 8.655   -32.508  14.694   1.00 37.03  ? 19  ALA   C N      1 
ATOM   6889  C  CA     . ALA   C 1  19  ? 7.449   -32.816  13.934   1.00 36.19  ? 19  ALA   C CA     1 
ATOM   6890  C  C      . ALA   C 1  19  ? 7.686   -33.986  12.978   1.00 38.05  ? 19  ALA   C C      1 
ATOM   6891  O  O      . ALA   C 1  19  ? 6.921   -34.959  12.987   1.00 41.70  ? 19  ALA   C O      1 
ATOM   6892  C  CB     . ALA   C 1  19  ? 6.950   -31.574  13.192   1.00 38.21  ? 19  ALA   C CB     1 
ATOM   6893  N  N      . CYS   C 1  20  ? 8.765   -33.932  12.171   1.00 36.70  ? 20  CYS   C N      1 
ATOM   6894  C  CA     . CYS   C 1  20  ? 9.015   -34.995  11.187   1.00 36.47  ? 20  CYS   C CA     1 
ATOM   6895  C  C      . CYS   C 1  20  ? 9.220   -36.355  11.852   1.00 40.78  ? 20  CYS   C C      1 
ATOM   6896  O  O      . CYS   C 1  20  ? 8.699   -37.375  11.372   1.00 38.06  ? 20  CYS   C O      1 
ATOM   6897  C  CB     . CYS   C 1  20  ? 10.225  -34.674  10.321   1.00 29.79  ? 20  CYS   C CB     1 
ATOM   6898  S  SG     . CYS   C 1  20  ? 10.003  -33.369  9.148    1.00 46.80  ? 20  CYS   C SG     1 
ATOM   6899  N  N      . TRP   C 1  21  ? 10.002  -36.405  12.942   1.00 36.33  ? 21  TRP   C N      1 
ATOM   6900  C  CA     . TRP   C 1  21  ? 10.286  -37.713  13.513   1.00 39.82  ? 21  TRP   C CA     1 
ATOM   6901  C  C      . TRP   C 1  21  ? 9.098   -38.258  14.305   1.00 42.05  ? 21  TRP   C C      1 
ATOM   6902  O  O      . TRP   C 1  21  ? 8.912   -39.478  14.365   1.00 39.17  ? 21  TRP   C O      1 
ATOM   6903  C  CB     . TRP   C 1  21  ? 11.561  -37.661  14.352   1.00 39.89  ? 21  TRP   C CB     1 
ATOM   6904  C  CG     . TRP   C 1  21  ? 12.787  -37.578  13.470   1.00 38.13  ? 21  TRP   C CG     1 
ATOM   6905  C  CD1    . TRP   C 1  21  ? 13.528  -36.458  13.196   1.00 37.10  ? 21  TRP   C CD1    1 
ATOM   6906  C  CD2    . TRP   C 1  21  ? 13.382  -38.642  12.720   1.00 39.72  ? 21  TRP   C CD2    1 
ATOM   6907  N  NE1    . TRP   C 1  21  ? 14.547  -36.758  12.338   1.00 38.26  ? 21  TRP   C NE1    1 
ATOM   6908  C  CE2    . TRP   C 1  21  ? 14.484  -38.093  12.021   1.00 43.44  ? 21  TRP   C CE2    1 
ATOM   6909  C  CE3    . TRP   C 1  21  ? 13.090  -40.000  12.557   1.00 38.10  ? 21  TRP   C CE3    1 
ATOM   6910  C  CZ2    . TRP   C 1  21  ? 15.302  -38.865  11.176   1.00 36.86  ? 21  TRP   C CZ2    1 
ATOM   6911  C  CZ3    . TRP   C 1  21  ? 13.901  -40.759  11.714   1.00 36.90  ? 21  TRP   C CZ3    1 
ATOM   6912  C  CH2    . TRP   C 1  21  ? 14.994  -40.184  11.038   1.00 35.92  ? 21  TRP   C CH2    1 
ATOM   6913  N  N      . GLU   C 1  22  ? 8.255   -37.394  14.876   1.00 39.25  ? 22  GLU   C N      1 
ATOM   6914  C  CA     . GLU   C 1  22  ? 7.023   -37.914  15.456   1.00 43.04  ? 22  GLU   C CA     1 
ATOM   6915  C  C      . GLU   C 1  22  ? 6.092   -38.423  14.355   1.00 48.01  ? 22  GLU   C C      1 
ATOM   6916  O  O      . GLU   C 1  22  ? 5.418   -39.451  14.522   1.00 48.22  ? 22  GLU   C O      1 
ATOM   6917  C  CB     . GLU   C 1  22  ? 6.332   -36.852  16.311   1.00 45.38  ? 22  GLU   C CB     1 
ATOM   6918  C  CG     . GLU   C 1  22  ? 4.879   -37.202  16.617   1.00 51.36  ? 22  GLU   C CG     1 
ATOM   6919  C  CD     . GLU   C 1  22  ? 4.190   -36.223  17.541   1.00 52.62  ? 22  GLU   C CD     1 
ATOM   6920  O  OE1    . GLU   C 1  22  ? 4.405   -35.011  17.377   1.00 49.90  ? 22  GLU   C OE1    1 
ATOM   6921  O  OE2    . GLU   C 1  22  ? 3.434   -36.671  18.435   1.00 62.56  ? 22  GLU   C OE2    1 
ATOM   6922  N  N      . LEU   C 1  23  ? 6.065   -37.735  13.211   1.00 39.10  ? 23  LEU   C N      1 
ATOM   6923  C  CA     . LEU   C 1  23  ? 5.235   -38.182  12.101   1.00 40.34  ? 23  LEU   C CA     1 
ATOM   6924  C  C      . LEU   C 1  23  ? 5.721   -39.515  11.532   1.00 46.71  ? 23  LEU   C C      1 
ATOM   6925  O  O      . LEU   C 1  23  ? 4.915   -40.433  11.335   1.00 45.21  ? 23  LEU   C O      1 
ATOM   6926  C  CB     . LEU   C 1  23  ? 5.193   -37.109  11.021   1.00 38.95  ? 23  LEU   C CB     1 
ATOM   6927  C  CG     . LEU   C 1  23  ? 4.226   -37.385  9.890    1.00 37.48  ? 23  LEU   C CG     1 
ATOM   6928  C  CD1    . LEU   C 1  23  ? 2.865   -37.651  10.471   1.00 36.46  ? 23  LEU   C CD1    1 
ATOM   6929  C  CD2    . LEU   C 1  23  ? 4.194   -36.190  8.985    1.00 39.82  ? 23  LEU   C CD2    1 
ATOM   6930  N  N      . TYR   C 1  24  ? 7.034   -39.644  11.247   1.00 46.41  ? 24  TYR   C N      1 
ATOM   6931  C  CA     . TYR   C 1  24  ? 7.572   -40.918  10.751   1.00 42.75  ? 24  TYR   C CA     1 
ATOM   6932  C  C      . TYR   C 1  24  ? 7.159   -42.072  11.659   1.00 45.35  ? 24  TYR   C C      1 
ATOM   6933  O  O      . TYR   C 1  24  ? 6.679   -43.112  11.183   1.00 44.90  ? 24  TYR   C O      1 
ATOM   6934  C  CB     . TYR   C 1  24  ? 9.109   -40.880  10.640   1.00 41.46  ? 24  TYR   C CB     1 
ATOM   6935  C  CG     . TYR   C 1  24  ? 9.678   -39.885  9.655    1.00 38.96  ? 24  TYR   C CG     1 
ATOM   6936  C  CD1    . TYR   C 1  24  ? 8.928   -39.416  8.595    1.00 40.66  ? 24  TYR   C CD1    1 
ATOM   6937  C  CD2    . TYR   C 1  24  ? 10.960  -39.383  9.815    1.00 39.17  ? 24  TYR   C CD2    1 
ATOM   6938  C  CE1    . TYR   C 1  24  ? 9.438   -38.496  7.703    1.00 35.54  ? 24  TYR   C CE1    1 
ATOM   6939  C  CE2    . TYR   C 1  24  ? 11.475  -38.455  8.941    1.00 39.02  ? 24  TYR   C CE2    1 
ATOM   6940  C  CZ     . TYR   C 1  24  ? 10.704  -38.010  7.886    1.00 38.67  ? 24  TYR   C CZ     1 
ATOM   6941  O  OH     . TYR   C 1  24  ? 11.212  -37.080  7.006    1.00 41.58  ? 24  TYR   C OH     1 
ATOM   6942  N  N      . CYS   C 1  25  ? 7.342   -41.902  12.976   1.00 38.78  ? 25  CYS   C N      1 
ATOM   6943  C  CA     . CYS   C 1  25  ? 6.983   -42.951  13.928   1.00 44.19  ? 25  CYS   C CA     1 
ATOM   6944  C  C      . CYS   C 1  25  ? 5.535   -43.397  13.765   1.00 48.35  ? 25  CYS   C C      1 
ATOM   6945  O  O      . CYS   C 1  25  ? 5.242   -44.600  13.769   1.00 45.63  ? 25  CYS   C O      1 
ATOM   6946  C  CB     . CYS   C 1  25  ? 7.196   -42.474  15.361   1.00 41.63  ? 25  CYS   C CB     1 
ATOM   6947  S  SG     . CYS   C 1  25  ? 8.882   -42.335  15.820   1.00 46.51  ? 25  CYS   C SG     1 
ATOM   6948  N  N      . LEU   C 1  26  ? 4.603   -42.444  13.682   1.00 44.04  ? 26  LEU   C N      1 
ATOM   6949  C  CA     . LEU   C 1  26  ? 3.216   -42.831  13.466   1.00 44.40  ? 26  LEU   C CA     1 
ATOM   6950  C  C      . LEU   C 1  26  ? 3.051   -43.533  12.126   1.00 47.50  ? 26  LEU   C C      1 
ATOM   6951  O  O      . LEU   C 1  26  ? 2.282   -44.493  12.017   1.00 48.75  ? 26  LEU   C O      1 
ATOM   6952  C  CB     . LEU   C 1  26  ? 2.310   -41.608  13.555   1.00 46.43  ? 26  LEU   C CB     1 
ATOM   6953  C  CG     . LEU   C 1  26  ? 2.392   -41.016  14.954   1.00 45.67  ? 26  LEU   C CG     1 
ATOM   6954  C  CD1    . LEU   C 1  26  ? 1.918   -39.571  14.972   1.00 43.16  ? 26  LEU   C CD1    1 
ATOM   6955  C  CD2    . LEU   C 1  26  ? 1.600   -41.885  15.887   1.00 41.35  ? 26  LEU   C CD2    1 
ATOM   6956  N  N      . GLU   C 1  27  ? 3.771   -43.078  11.094   1.00 45.26  ? 27  GLU   C N      1 
ATOM   6957  C  CA     . GLU   C 1  27  ? 3.677   -43.730  9.791    1.00 46.17  ? 27  GLU   C CA     1 
ATOM   6958  C  C      . GLU   C 1  27  ? 4.151   -45.176  9.864    1.00 46.50  ? 27  GLU   C C      1 
ATOM   6959  O  O      . GLU   C 1  27  ? 3.498   -46.075  9.321    1.00 45.26  ? 27  GLU   C O      1 
ATOM   6960  C  CB     . GLU   C 1  27  ? 4.489   -42.962  8.745    1.00 45.12  ? 27  GLU   C CB     1 
ATOM   6961  C  CG     . GLU   C 1  27  ? 4.091   -41.509  8.598    1.00 44.24  ? 27  GLU   C CG     1 
ATOM   6962  C  CD     . GLU   C 1  27  ? 4.506   -40.882  7.277    1.00 40.15  ? 27  GLU   C CD     1 
ATOM   6963  O  OE1    . GLU   C 1  27  ? 4.994   -41.586  6.370    1.00 37.84  ? 27  GLU   C OE1    1 
ATOM   6964  O  OE2    . GLU   C 1  27  ? 4.329   -39.659  7.157    1.00 40.18  ? 27  GLU   C OE2    1 
ATOM   6965  N  N      . HIS   C 1  28  ? 5.275   -45.424  10.534   1.00 38.57  ? 28  HIS   C N      1 
ATOM   6966  C  CA     . HIS   C 1  28  ? 5.865   -46.757  10.523   1.00 42.18  ? 28  HIS   C CA     1 
ATOM   6967  C  C      . HIS   C 1  28  ? 5.436   -47.634  11.701   1.00 48.14  ? 28  HIS   C C      1 
ATOM   6968  O  O      . HIS   C 1  28  ? 5.937   -48.759  11.828   1.00 52.24  ? 28  HIS   C O      1 
ATOM   6969  C  CB     . HIS   C 1  28  ? 7.394   -46.653  10.482   1.00 41.56  ? 28  HIS   C CB     1 
ATOM   6970  C  CG     . HIS   C 1  28  ? 7.911   -45.972  9.260    1.00 39.48  ? 28  HIS   C CG     1 
ATOM   6971  N  ND1    . HIS   C 1  28  ? 7.787   -46.517  7.999    1.00 38.36  ? 28  HIS   C ND1    1 
ATOM   6972  C  CD2    . HIS   C 1  28  ? 8.528   -44.777  9.096    1.00 37.97  ? 28  HIS   C CD2    1 
ATOM   6973  C  CE1    . HIS   C 1  28  ? 8.307   -45.688  7.109    1.00 38.70  ? 28  HIS   C CE1    1 
ATOM   6974  N  NE2    . HIS   C 1  28  ? 8.751   -44.620  7.746    1.00 40.27  ? 28  HIS   C NE2    1 
ATOM   6975  N  N      . GLY   C 1  29  ? 4.531   -47.162  12.557   1.00 43.13  ? 29  GLY   C N      1 
ATOM   6976  C  CA     . GLY   C 1  29  ? 4.142   -47.914  13.731   1.00 38.71  ? 29  GLY   C CA     1 
ATOM   6977  C  C      . GLY   C 1  29  ? 5.175   -48.004  14.831   1.00 44.61  ? 29  GLY   C C      1 
ATOM   6978  O  O      . GLY   C 1  29  ? 5.131   -48.948  15.624   1.00 54.98  ? 29  GLY   C O      1 
ATOM   6979  N  N      . ILE   C 1  30  ? 6.108   -47.065  14.913   1.00 45.22  ? 30  ILE   C N      1 
ATOM   6980  C  CA     . ILE   C 1  30  ? 7.150   -47.096  15.938   1.00 48.29  ? 30  ILE   C CA     1 
ATOM   6981  C  C      . ILE   C 1  30  ? 6.651   -46.316  17.146   1.00 46.01  ? 30  ILE   C C      1 
ATOM   6982  O  O      . ILE   C 1  30  ? 6.084   -45.233  17.005   1.00 45.86  ? 30  ILE   C O      1 
ATOM   6983  C  CB     . ILE   C 1  30  ? 8.482   -46.533  15.388   1.00 46.72  ? 30  ILE   C CB     1 
ATOM   6984  C  CG1    . ILE   C 1  30  ? 8.878   -47.269  14.106   1.00 48.40  ? 30  ILE   C CG1    1 
ATOM   6985  C  CG2    . ILE   C 1  30  ? 9.612   -46.642  16.400   1.00 38.60  ? 30  ILE   C CG2    1 
ATOM   6986  C  CD1    . ILE   C 1  30  ? 10.227  -46.833  13.527   1.00 43.87  ? 30  ILE   C CD1    1 
ATOM   6987  N  N      . GLN   C 1  31  ? 6.838   -46.883  18.349   1.00 59.75  ? 31  GLN   C N      1 
ATOM   6988  C  CA     . GLN   C 1  31  ? 6.366   -46.235  19.567   1.00 58.63  ? 31  GLN   C CA     1 
ATOM   6989  C  C      . GLN   C 1  31  ? 7.443   -45.344  20.156   1.00 56.21  ? 31  GLN   C C      1 
ATOM   6990  O  O      . GLN   C 1  31  ? 8.631   -45.510  19.868   1.00 57.61  ? 31  GLN   C O      1 
ATOM   6991  C  CB     . GLN   C 1  31  ? 5.952   -47.273  20.601   1.00 57.29  ? 31  GLN   C CB     1 
ATOM   6992  C  CG     . GLN   C 1  31  ? 5.210   -48.467  20.029   1.00 61.96  ? 31  GLN   C CG     1 
ATOM   6993  C  CD     . GLN   C 1  31  ? 5.122   -49.628  21.019   1.00 72.80  ? 31  GLN   C CD     1 
ATOM   6994  O  OE1    . GLN   C 1  31  ? 5.844   -49.667  22.030   1.00 72.35  ? 31  GLN   C OE1    1 
ATOM   6995  N  NE2    . GLN   C 1  31  ? 4.256   -50.594  20.718   1.00 78.19  ? 31  GLN   C NE2    1 
ATOM   6996  N  N      . PRO   C 1  32  ? 7.047   -44.397  21.008   1.00 54.86  ? 32  PRO   C N      1 
ATOM   6997  C  CA     . PRO   C 1  32  ? 8.019   -43.437  21.556   1.00 55.00  ? 32  PRO   C CA     1 
ATOM   6998  C  C      . PRO   C 1  32  ? 9.214   -44.074  22.254   1.00 54.13  ? 32  PRO   C C      1 
ATOM   6999  O  O      . PRO   C 1  32  ? 10.248  -43.413  22.395   1.00 57.89  ? 32  PRO   C O      1 
ATOM   7000  C  CB     . PRO   C 1  32  ? 7.170   -42.610  22.532   1.00 49.84  ? 32  PRO   C CB     1 
ATOM   7001  C  CG     . PRO   C 1  32  ? 5.795   -42.718  22.000   1.00 45.45  ? 32  PRO   C CG     1 
ATOM   7002  C  CD     . PRO   C 1  32  ? 5.673   -44.099  21.441   1.00 50.16  ? 32  PRO   C CD     1 
ATOM   7003  N  N      . ASP   C 1  33  ? 9.120   -45.321  22.702   1.00 58.59  ? 33  ASP   C N      1 
ATOM   7004  C  CA     . ASP   C 1  33  ? 10.285  -45.996  23.253   1.00 59.94  ? 33  ASP   C CA     1 
ATOM   7005  C  C      . ASP   C 1  33  ? 11.140  -46.661  22.173   1.00 59.26  ? 33  ASP   C C      1 
ATOM   7006  O  O      . ASP   C 1  33  ? 12.198  -47.215  22.487   1.00 63.19  ? 33  ASP   C O      1 
ATOM   7007  C  CB     . ASP   C 1  33  ? 9.858   -47.017  24.327   1.00 52.26  ? 33  ASP   C CB     1 
ATOM   7008  C  CG     . ASP   C 1  33  ? 9.181   -48.255  23.751   1.00 64.35  ? 33  ASP   C CG     1 
ATOM   7009  O  OD1    . ASP   C 1  33  ? 8.895   -48.308  22.527   1.00 62.95  ? 33  ASP   C OD1    1 
ATOM   7010  O  OD2    . ASP   C 1  33  ? 8.927   -49.188  24.550   1.00 69.59  ? 33  ASP   C OD2    1 
ATOM   7011  N  N      . GLY   C 1  34  ? 10.720  -46.612  20.913   1.00 56.05  ? 34  GLY   C N      1 
ATOM   7012  C  CA     . GLY   C 1  34  ? 11.504  -47.156  19.829   1.00 54.02  ? 34  GLY   C CA     1 
ATOM   7013  C  C      . GLY   C 1  34  ? 11.127  -48.555  19.392   1.00 52.62  ? 34  GLY   C C      1 
ATOM   7014  O  O      . GLY   C 1  34  ? 11.623  -49.014  18.358   1.00 48.98  ? 34  GLY   C O      1 
ATOM   7015  N  N      . GLN   C 1  35  ? 10.265  -49.245  20.126   1.00 57.77  ? 35  GLN   C N      1 
ATOM   7016  C  CA     . GLN   C 1  35  ? 9.882   -50.580  19.696   1.00 57.61  ? 35  GLN   C CA     1 
ATOM   7017  C  C      . GLN   C 1  35  ? 8.894   -50.516  18.527   1.00 55.99  ? 35  GLN   C C      1 
ATOM   7018  O  O      . GLN   C 1  35  ? 8.114   -49.562  18.382   1.00 51.10  ? 35  GLN   C O      1 
ATOM   7019  C  CB     . GLN   C 1  35  ? 9.303   -51.372  20.870   1.00 53.65  ? 35  GLN   C CB     1 
ATOM   7020  C  CG     . GLN   C 1  35  ? 10.157  -51.296  22.120   1.00 57.20  ? 35  GLN   C CG     1 
ATOM   7021  C  CD     . GLN   C 1  35  ? 11.418  -52.154  22.036   1.00 63.37  ? 35  GLN   C CD     1 
ATOM   7022  O  OE1    . GLN   C 1  35  ? 11.426  -53.226  21.417   1.00 55.35  ? 35  GLN   C OE1    1 
ATOM   7023  N  NE2    . GLN   C 1  35  ? 12.495  -51.681  22.664   1.00 65.42  ? 35  GLN   C NE2    1 
ATOM   7024  N  N      . MET   C 1  36  ? 8.965   -51.542  17.677   1.00 54.87  ? 36  MET   C N      1 
ATOM   7025  C  CA     . MET   C 1  36  ? 8.107   -51.700  16.499   1.00 54.89  ? 36  MET   C CA     1 
ATOM   7026  C  C      . MET   C 1  36  ? 7.622   -53.140  16.526   1.00 59.24  ? 36  MET   C C      1 
ATOM   7027  O  O      . MET   C 1  36  ? 8.372   -54.054  16.145   1.00 64.42  ? 36  MET   C O      1 
ATOM   7028  C  CB     . MET   C 1  36  ? 8.869   -51.447  15.197   1.00 54.36  ? 36  MET   C CB     1 
ATOM   7029  C  CG     . MET   C 1  36  ? 8.086   -51.038  13.937   1.00 50.35  ? 36  MET   C CG     1 
ATOM   7030  S  SD     . MET   C 1  36  ? 9.289   -50.517  12.660   1.00 57.71  ? 36  MET   C SD     1 
ATOM   7031  C  CE     . MET   C 1  36  ? 8.596   -51.115  11.135   1.00 53.07  ? 36  MET   C CE     1 
ATOM   7032  N  N      . PRO   C 1  37  ? 6.393   -53.392  16.962   1.00 58.54  ? 37  PRO   C N      1 
ATOM   7033  C  CA     . PRO   C 1  37  ? 5.901   -54.781  16.949   1.00 61.01  ? 37  PRO   C CA     1 
ATOM   7034  C  C      . PRO   C 1  37  ? 5.942   -55.465  15.583   1.00 60.49  ? 37  PRO   C C      1 
ATOM   7035  O  O      . PRO   C 1  37  ? 6.145   -56.687  15.527   1.00 58.75  ? 37  PRO   C O      1 
ATOM   7036  C  CB     . PRO   C 1  37  ? 4.474   -54.628  17.475   1.00 61.35  ? 37  PRO   C CB     1 
ATOM   7037  C  CG     . PRO   C 1  37  ? 4.595   -53.473  18.444   1.00 59.18  ? 37  PRO   C CG     1 
ATOM   7038  C  CD     . PRO   C 1  37  ? 5.575   -52.518  17.818   1.00 60.79  ? 37  PRO   C CD     1 
ATOM   7039  N  N      . SER   C 1  38  ? 5.771   -54.728  14.480   1.00 60.74  ? 38  SER   C N      1 
ATOM   7040  C  CA     . SER   C 1  38  ? 5.742   -55.366  13.164   1.00 59.37  ? 38  SER   C CA     1 
ATOM   7041  C  C      . SER   C 1  38  ? 7.129   -55.743  12.652   1.00 63.09  ? 38  SER   C C      1 
ATOM   7042  O  O      . SER   C 1  38  ? 7.244   -56.658  11.830   1.00 68.38  ? 38  SER   C O      1 
ATOM   7043  C  CB     . SER   C 1  38  ? 5.060   -54.469  12.132   1.00 54.55  ? 38  SER   C CB     1 
ATOM   7044  O  OG     . SER   C 1  38  ? 5.543   -53.143  12.194   1.00 58.18  ? 38  SER   C OG     1 
ATOM   7045  N  N      . ASP   C 1  39  ? 8.194   -55.069  13.088   1.00 63.79  ? 39  ASP   C N      1 
ATOM   7046  C  CA     . ASP   C 1  39  ? 9.527   -55.530  12.699   1.00 60.95  ? 39  ASP   C CA     1 
ATOM   7047  C  C      . ASP   C 1  39  ? 9.800   -56.840  13.423   1.00 60.05  ? 39  ASP   C C      1 
ATOM   7048  O  O      . ASP   C 1  39  ? 10.006  -56.861  14.641   1.00 61.44  ? 39  ASP   C O      1 
ATOM   7049  C  CB     . ASP   C 1  39  ? 10.614  -54.496  13.008   1.00 57.83  ? 39  ASP   C CB     1 
ATOM   7050  C  CG     . ASP   C 1  39  ? 11.918  -54.758  12.232   1.00 59.40  ? 39  ASP   C CG     1 
ATOM   7051  O  OD1    . ASP   C 1  39  ? 11.965  -55.621  11.345   1.00 64.61  ? 39  ASP   C OD1    1 
ATOM   7052  O  OD2    . ASP   C 1  39  ? 12.928  -54.112  12.510   1.00 58.19  ? 39  ASP   C OD2    1 
ATOM   7053  N  N      . LYS   C 1  40  ? 9.768   -57.941  12.685   1.00 61.83  ? 40  LYS   C N      1 
ATOM   7054  C  CA     . LYS   C 1  40  ? 10.232  -59.207  13.238   1.00 62.30  ? 40  LYS   C CA     1 
ATOM   7055  C  C      . LYS   C 1  40  ? 11.749  -59.385  13.140   1.00 61.78  ? 40  LYS   C C      1 
ATOM   7056  O  O      . LYS   C 1  40  ? 12.295  -60.258  13.822   1.00 63.28  ? 40  LYS   C O      1 
ATOM   7057  C  CB     . LYS   C 1  40  ? 9.507   -60.349  12.539   1.00 51.17  ? 40  LYS   C CB     1 
ATOM   7058  C  CG     . LYS   C 1  40  ? 8.023   -60.113  12.526   1.00 58.09  ? 40  LYS   C CG     1 
ATOM   7059  C  CD     . LYS   C 1  40  ? 7.463   -60.106  13.949   1.00 55.31  ? 40  LYS   C CD     1 
ATOM   7060  C  CE     . LYS   C 1  40  ? 6.225   -59.213  14.050   1.00 55.78  ? 40  LYS   C CE     1 
ATOM   7061  N  NZ     . LYS   C 1  40  ? 5.082   -59.875  14.749   1.00 67.31  ? 40  LYS   C NZ     1 
ATOM   7062  N  N      . THR   C 1  41  ? 12.436  -58.580  12.317   1.00 58.63  ? 41  THR   C N      1 
ATOM   7063  C  CA     . THR   C 1  41  ? 13.889  -58.644  12.162   1.00 61.06  ? 41  THR   C CA     1 
ATOM   7064  C  C      . THR   C 1  41  ? 14.510  -57.774  13.243   1.00 64.75  ? 41  THR   C C      1 
ATOM   7065  O  O      . THR   C 1  41  ? 14.699  -56.564  13.069   1.00 66.60  ? 41  THR   C O      1 
ATOM   7066  C  CB     . THR   C 1  41  ? 14.329  -58.182  10.777   1.00 65.30  ? 41  THR   C CB     1 
ATOM   7067  O  OG1    . THR   C 1  41  ? 14.059  -56.770  10.619   1.00 66.62  ? 41  THR   C OG1    1 
ATOM   7068  C  CG2    . THR   C 1  41  ? 13.629  -58.995  9.698    1.00 60.11  ? 41  THR   C CG2    1 
ATOM   7069  N  N      . ILE   C 1  42  ? 14.850  -58.405  14.363   1.00 63.81  ? 42  ILE   C N      1 
ATOM   7070  C  CA     . ILE   C 1  42  ? 15.370  -57.690  15.519   1.00 61.41  ? 42  ILE   C CA     1 
ATOM   7071  C  C      . ILE   C 1  42  ? 16.848  -57.396  15.329   1.00 61.61  ? 42  ILE   C C      1 
ATOM   7072  O  O      . ILE   C 1  42  ? 17.605  -58.227  14.815   1.00 67.54  ? 42  ILE   C O      1 
ATOM   7073  C  CB     . ILE   C 1  42  ? 15.132  -58.500  16.797   1.00 58.24  ? 42  ILE   C CB     1 
ATOM   7074  C  CG1    . ILE   C 1  42  ? 13.643  -58.793  16.959   1.00 53.64  ? 42  ILE   C CG1    1 
ATOM   7075  C  CG2    . ILE   C 1  42  ? 15.666  -57.733  17.969   1.00 62.73  ? 42  ILE   C CG2    1 
ATOM   7076  C  CD1    . ILE   C 1  42  ? 13.337  -60.249  16.934   1.00 60.86  ? 42  ILE   C CD1    1 
ATOM   7077  N  N      . GLY   C 1  43  ? 17.264  -56.205  15.757   1.00 65.73  ? 43  GLY   C N      1 
ATOM   7078  C  CA     . GLY   C 1  43  ? 18.644  -55.773  15.650   1.00 67.67  ? 43  GLY   C CA     1 
ATOM   7079  C  C      . GLY   C 1  43  ? 19.076  -55.259  14.287   1.00 68.15  ? 43  GLY   C C      1 
ATOM   7080  O  O      . GLY   C 1  43  ? 20.180  -54.685  14.185   1.00 62.69  ? 43  GLY   C O      1 
ATOM   7081  N  N      . GLY   C 1  44  ? 18.263  -55.445  13.247   1.00 61.64  ? 44  GLY   C N      1 
ATOM   7082  C  CA     . GLY   C 1  44  ? 18.628  -54.962  11.928   1.00 59.70  ? 44  GLY   C CA     1 
ATOM   7083  C  C      . GLY   C 1  44  ? 17.576  -55.270  10.877   1.00 62.71  ? 44  GLY   C C      1 
ATOM   7084  O  O      . GLY   C 1  44  ? 16.424  -55.611  11.173   1.00 65.18  ? 44  GLY   C O      1 
ATOM   7085  N  N      . GLY   C 1  45  ? 18.007  -55.132  9.637    1.00 58.49  ? 45  GLY   C N      1 
ATOM   7086  C  CA     . GLY   C 1  45  ? 17.177  -55.375  8.474    1.00 58.28  ? 45  GLY   C CA     1 
ATOM   7087  C  C      . GLY   C 1  45  ? 17.523  -54.385  7.384    1.00 59.56  ? 45  GLY   C C      1 
ATOM   7088  O  O      . GLY   C 1  45  ? 18.216  -53.391  7.606    1.00 61.13  ? 45  GLY   C O      1 
ATOM   7089  N  N      . ASP   C 1  46  ? 17.045  -54.687  6.172    1.00 62.30  ? 46  ASP   C N      1 
ATOM   7090  C  CA     . ASP   C 1  46  ? 17.106  -53.752  5.044    1.00 63.29  ? 46  ASP   C CA     1 
ATOM   7091  C  C      . ASP   C 1  46  ? 15.700  -53.411  4.544    1.00 57.93  ? 46  ASP   C C      1 
ATOM   7092  O  O      . ASP   C 1  46  ? 15.475  -53.215  3.349    1.00 57.04  ? 46  ASP   C O      1 
ATOM   7093  C  CB     . ASP   C 1  46  ? 17.976  -54.279  3.895    1.00 58.08  ? 46  ASP   C CB     1 
ATOM   7094  C  CG     . ASP   C 1  46  ? 17.678  -55.738  3.532    1.00 73.24  ? 46  ASP   C CG     1 
ATOM   7095  O  OD1    . ASP   C 1  46  ? 16.723  -56.343  4.095    1.00 74.74  ? 46  ASP   C OD1    1 
ATOM   7096  O  OD2    . ASP   C 1  46  ? 18.390  -56.272  2.647    1.00 81.60  ? 46  ASP   C OD2    1 
ATOM   7097  N  N      . ASP   C 1  47  ? 14.738  -53.350  5.454    1.00 52.51  ? 47  ASP   C N      1 
ATOM   7098  C  CA     . ASP   C 1  47  ? 13.421  -52.873  5.089    1.00 53.37  ? 47  ASP   C CA     1 
ATOM   7099  C  C      . ASP   C 1  47  ? 13.470  -51.380  4.782    1.00 53.12  ? 47  ASP   C C      1 
ATOM   7100  O  O      . ASP   C 1  47  ? 14.416  -50.668  5.140    1.00 50.08  ? 47  ASP   C O      1 
ATOM   7101  C  CB     . ASP   C 1  47  ? 12.426  -53.174  6.201    1.00 52.60  ? 47  ASP   C CB     1 
ATOM   7102  C  CG     . ASP   C 1  47  ? 12.332  -54.645  6.484    1.00 52.27  ? 47  ASP   C CG     1 
ATOM   7103  O  OD1    . ASP   C 1  47  ? 11.853  -55.350  5.581    1.00 47.78  ? 47  ASP   C OD1    1 
ATOM   7104  O  OD2    . ASP   C 1  47  ? 12.759  -55.097  7.577    1.00 62.01  ? 47  ASP   C OD2    1 
ATOM   7105  N  N      . SER   C 1  48  ? 12.442  -50.912  4.080    1.00 51.57  ? 48  SER   C N      1 
ATOM   7106  C  CA     . SER   C 1  48  ? 12.480  -49.550  3.577    1.00 47.89  ? 48  SER   C CA     1 
ATOM   7107  C  C      . SER   C 1  48  ? 12.649  -48.556  4.718    1.00 49.47  ? 48  SER   C C      1 
ATOM   7108  O  O      . SER   C 1  48  ? 13.463  -47.634  4.626    1.00 49.91  ? 48  SER   C O      1 
ATOM   7109  C  CB     . SER   C 1  48  ? 11.223  -49.266  2.770    1.00 51.09  ? 48  SER   C CB     1 
ATOM   7110  O  OG     . SER   C 1  48  ? 11.431  -49.657  1.425    1.00 58.53  ? 48  SER   C OG     1 
ATOM   7111  N  N      . PHE   C 1  49  ? 11.911  -48.747  5.821    1.00 44.18  ? 49  PHE   C N      1 
ATOM   7112  C  CA     . PHE   C 1  49  ? 12.022  -47.820  6.938    1.00 44.55  ? 49  PHE   C CA     1 
ATOM   7113  C  C      . PHE   C 1  49  ? 13.434  -47.784  7.504    1.00 43.64  ? 49  PHE   C C      1 
ATOM   7114  O  O      . PHE   C 1  49  ? 13.804  -46.796  8.144    1.00 43.73  ? 49  PHE   C O      1 
ATOM   7115  C  CB     . PHE   C 1  49  ? 11.003  -48.148  8.043    1.00 42.92  ? 49  PHE   C CB     1 
ATOM   7116  C  CG     . PHE   C 1  49  ? 11.175  -49.527  8.666    1.00 53.88  ? 49  PHE   C CG     1 
ATOM   7117  C  CD1    . PHE   C 1  49  ? 12.129  -49.751  9.665    1.00 48.91  ? 49  PHE   C CD1    1 
ATOM   7118  C  CD2    . PHE   C 1  49  ? 10.362  -50.600  8.268    1.00 44.70  ? 49  PHE   C CD2    1 
ATOM   7119  C  CE1    . PHE   C 1  49  ? 12.276  -51.010  10.228   1.00 45.95  ? 49  PHE   C CE1    1 
ATOM   7120  C  CE2    . PHE   C 1  49  ? 10.518  -51.849  8.824    1.00 41.41  ? 49  PHE   C CE2    1 
ATOM   7121  C  CZ     . PHE   C 1  49  ? 11.472  -52.054  9.807    1.00 47.46  ? 49  PHE   C CZ     1 
ATOM   7122  N  N      . ASN   C 1  50  ? 14.248  -48.807  7.256    1.00 43.08  ? 50  ASN   C N      1 
ATOM   7123  C  CA     . ASN   C 1  50  ? 15.605  -48.770  7.799    1.00 46.51  ? 50  ASN   C CA     1 
ATOM   7124  C  C      . ASN   C 1  50  ? 16.494  -47.739  7.092    1.00 45.68  ? 50  ASN   C C      1 
ATOM   7125  O  O      . ASN   C 1  50  ? 17.592  -47.436  7.582    1.00 36.60  ? 50  ASN   C O      1 
ATOM   7126  C  CB     . ASN   C 1  50  ? 16.217  -50.174  7.750    1.00 39.14  ? 50  ASN   C CB     1 
ATOM   7127  C  CG     . ASN   C 1  50  ? 15.638  -51.095  8.829    1.00 53.12  ? 50  ASN   C CG     1 
ATOM   7128  O  OD1    . ASN   C 1  50  ? 15.062  -52.159  8.532    1.00 56.15  ? 50  ASN   C OD1    1 
ATOM   7129  N  ND2    . ASN   C 1  50  ? 15.770  -50.682  10.091   1.00 48.84  ? 50  ASN   C ND2    1 
ATOM   7130  N  N      . THR   C 1  51  ? 16.036  -47.158  5.978    1.00 47.76  ? 51  THR   C N      1 
ATOM   7131  C  CA     . THR   C 1  51  ? 16.781  -46.050  5.397    1.00 42.22  ? 51  THR   C CA     1 
ATOM   7132  C  C      . THR   C 1  51  ? 16.820  -44.867  6.354    1.00 41.48  ? 51  THR   C C      1 
ATOM   7133  O  O      . THR   C 1  51  ? 17.790  -44.101  6.346    1.00 43.45  ? 51  THR   C O      1 
ATOM   7134  C  CB     . THR   C 1  51  ? 16.196  -45.623  4.034    1.00 41.75  ? 51  THR   C CB     1 
ATOM   7135  O  OG1    . THR   C 1  51  ? 14.830  -45.222  4.180    1.00 43.65  ? 51  THR   C OG1    1 
ATOM   7136  C  CG2    . THR   C 1  51  ? 16.284  -46.728  3.014    1.00 37.01  ? 51  THR   C CG2    1 
ATOM   7137  N  N      . PHE   C 1  52  ? 15.790  -44.705  7.197    1.00 41.02  ? 52  PHE   C N      1 
ATOM   7138  C  CA     . PHE   C 1  52  ? 15.772  -43.629  8.190    1.00 41.69  ? 52  PHE   C CA     1 
ATOM   7139  C  C      . PHE   C 1  52  ? 15.955  -44.091  9.637    1.00 37.24  ? 52  PHE   C C      1 
ATOM   7140  O  O      . PHE   C 1  52  ? 16.138  -43.248  10.516   1.00 42.17  ? 52  PHE   C O      1 
ATOM   7141  C  CB     . PHE   C 1  52  ? 14.462  -42.828  8.092    1.00 39.80  ? 52  PHE   C CB     1 
ATOM   7142  C  CG     . PHE   C 1  52  ? 14.475  -41.780  7.026    1.00 39.19  ? 52  PHE   C CG     1 
ATOM   7143  C  CD1    . PHE   C 1  52  ? 14.817  -42.106  5.726    1.00 35.08  ? 52  PHE   C CD1    1 
ATOM   7144  C  CD2    . PHE   C 1  52  ? 14.114  -40.465  7.314    1.00 43.24  ? 52  PHE   C CD2    1 
ATOM   7145  C  CE1    . PHE   C 1  52  ? 14.849  -41.129  4.722    1.00 35.31  ? 52  PHE   C CE1    1 
ATOM   7146  C  CE2    . PHE   C 1  52  ? 14.122  -39.488  6.318    1.00 40.47  ? 52  PHE   C CE2    1 
ATOM   7147  C  CZ     . PHE   C 1  52  ? 14.508  -39.832  5.014    1.00 38.45  ? 52  PHE   C CZ     1 
ATOM   7148  N  N      . PHE   C 1  53  ? 15.899  -45.382  9.925    1.00 39.24  ? 53  PHE   C N      1 
ATOM   7149  C  CA     . PHE   C 1  53  ? 15.925  -45.867  11.301   1.00 42.24  ? 53  PHE   C CA     1 
ATOM   7150  C  C      . PHE   C 1  53  ? 16.901  -47.033  11.411   1.00 45.48  ? 53  PHE   C C      1 
ATOM   7151  O  O      . PHE   C 1  53  ? 16.720  -48.059  10.736   1.00 39.62  ? 53  PHE   C O      1 
ATOM   7152  C  CB     . PHE   C 1  53  ? 14.537  -46.341  11.751   1.00 37.05  ? 53  PHE   C CB     1 
ATOM   7153  C  CG     . PHE   C 1  53  ? 13.551  -45.251  12.040   1.00 38.17  ? 53  PHE   C CG     1 
ATOM   7154  C  CD1    . PHE   C 1  53  ? 12.652  -44.830  11.072   1.00 39.25  ? 53  PHE   C CD1    1 
ATOM   7155  C  CD2    . PHE   C 1  53  ? 13.451  -44.708  13.316   1.00 42.58  ? 53  PHE   C CD2    1 
ATOM   7156  C  CE1    . PHE   C 1  53  ? 11.693  -43.856  11.362   1.00 44.21  ? 53  PHE   C CE1    1 
ATOM   7157  C  CE2    . PHE   C 1  53  ? 12.489  -43.734  13.620   1.00 43.80  ? 53  PHE   C CE2    1 
ATOM   7158  C  CZ     . PHE   C 1  53  ? 11.613  -43.303  12.637   1.00 43.22  ? 53  PHE   C CZ     1 
ATOM   7159  N  N      . SER   C 1  54  ? 17.901  -46.902  12.285   1.00 41.98  ? 54  SER   C N      1 
ATOM   7160  C  CA     . SER   C 1  54  ? 18.647  -48.088  12.696   1.00 47.07  ? 54  SER   C CA     1 
ATOM   7161  C  C      . SER   C 1  54  ? 17.885  -48.829  13.797   1.00 50.77  ? 54  SER   C C      1 
ATOM   7162  O  O      . SER   C 1  54  ? 16.920  -48.312  14.374   1.00 51.05  ? 54  SER   C O      1 
ATOM   7163  C  CB     . SER   C 1  54  ? 20.055  -47.727  13.168   1.00 43.16  ? 54  SER   C CB     1 
ATOM   7164  O  OG     . SER   C 1  54  ? 20.010  -46.704  14.142   1.00 45.30  ? 54  SER   C OG     1 
ATOM   7165  N  N      . GLU   C 1  55  ? 18.300  -50.077  14.045   1.00 56.17  ? 55  GLU   C N      1 
ATOM   7166  C  CA     . GLU   C 1  55  ? 17.723  -50.947  15.068   1.00 51.38  ? 55  GLU   C CA     1 
ATOM   7167  C  C      . GLU   C 1  55  ? 18.814  -51.379  16.043   1.00 54.41  ? 55  GLU   C C      1 
ATOM   7168  O  O      . GLU   C 1  55  ? 19.875  -51.855  15.621   1.00 56.92  ? 55  GLU   C O      1 
ATOM   7169  C  CB     . GLU   C 1  55  ? 17.083  -52.211  14.468   1.00 52.50  ? 55  GLU   C CB     1 
ATOM   7170  C  CG     . GLU   C 1  55  ? 16.146  -52.075  13.262   1.00 56.42  ? 55  GLU   C CG     1 
ATOM   7171  C  CD     . GLU   C 1  55  ? 15.403  -53.398  12.977   1.00 59.40  ? 55  GLU   C CD     1 
ATOM   7172  O  OE1    . GLU   C 1  55  ? 15.180  -54.159  13.941   1.00 62.61  ? 55  GLU   C OE1    1 
ATOM   7173  O  OE2    . GLU   C 1  55  ? 15.054  -53.704  11.809   1.00 57.44  ? 55  GLU   C OE2    1 
ATOM   7174  N  N      . THR   C 1  56  ? 18.549  -51.232  17.338   1.00 57.51  ? 56  THR   C N      1 
ATOM   7175  C  CA     . THR   C 1  56  ? 19.370  -51.861  18.367   1.00 50.94  ? 56  THR   C CA     1 
ATOM   7176  C  C      . THR   C 1  56  ? 18.946  -53.303  18.580   1.00 58.60  ? 56  THR   C C      1 
ATOM   7177  O  O      . THR   C 1  56  ? 17.794  -53.681  18.331   1.00 54.80  ? 56  THR   C O      1 
ATOM   7178  C  CB     . THR   C 1  56  ? 19.259  -51.136  19.707   1.00 52.66  ? 56  THR   C CB     1 
ATOM   7179  O  OG1    . THR   C 1  56  ? 18.072  -51.578  20.393   1.00 52.76  ? 56  THR   C OG1    1 
ATOM   7180  C  CG2    . THR   C 1  56  ? 19.221  -49.645  19.518   1.00 50.89  ? 56  THR   C CG2    1 
ATOM   7181  N  N      . GLY   C 1  57  ? 19.892  -54.104  19.087   1.00 64.26  ? 57  GLY   C N      1 
ATOM   7182  C  CA     . GLY   C 1  57  ? 19.605  -55.499  19.386   1.00 64.13  ? 57  GLY   C CA     1 
ATOM   7183  C  C      . GLY   C 1  57  ? 18.424  -55.688  20.319   1.00 57.65  ? 57  GLY   C C      1 
ATOM   7184  O  O      . GLY   C 1  57  ? 17.711  -56.692  20.226   1.00 52.67  ? 57  GLY   C O      1 
ATOM   7185  N  N      . ALA   C 1  58  ? 18.195  -54.731  21.222   1.00 54.50  ? 58  ALA   C N      1 
ATOM   7186  C  CA     . ALA   C 1  58  ? 17.061  -54.774  22.139   1.00 54.41  ? 58  ALA   C CA     1 
ATOM   7187  C  C      . ALA   C 1  58  ? 15.738  -54.406  21.470   1.00 65.72  ? 58  ALA   C C      1 
ATOM   7188  O  O      . ALA   C 1  58  ? 14.712  -54.313  22.163   1.00 66.44  ? 58  ALA   C O      1 
ATOM   7189  C  CB     . ALA   C 1  58  ? 17.318  -53.847  23.329   1.00 52.23  ? 58  ALA   C CB     1 
ATOM   7190  N  N      . GLY   C 1  59  ? 15.734  -54.177  20.154   1.00 61.59  ? 59  GLY   C N      1 
ATOM   7191  C  CA     . GLY   C 1  59  ? 14.514  -53.917  19.424   1.00 59.76  ? 59  GLY   C CA     1 
ATOM   7192  C  C      . GLY   C 1  59  ? 14.179  -52.461  19.209   1.00 54.49  ? 59  GLY   C C      1 
ATOM   7193  O  O      . GLY   C 1  59  ? 13.120  -52.164  18.653   1.00 51.39  ? 59  GLY   C O      1 
ATOM   7194  N  N      . LYS   C 1  60  ? 15.039  -51.547  19.628   1.00 58.51  ? 60  LYS   C N      1 
ATOM   7195  C  CA     . LYS   C 1  60  ? 14.740  -50.130  19.482   1.00 56.63  ? 60  LYS   C CA     1 
ATOM   7196  C  C      . LYS   C 1  60  ? 15.116  -49.662  18.080   1.00 53.67  ? 60  LYS   C C      1 
ATOM   7197  O  O      . LYS   C 1  60  ? 16.186  -49.999  17.560   1.00 50.33  ? 60  LYS   C O      1 
ATOM   7198  C  CB     . LYS   C 1  60  ? 15.474  -49.299  20.534   1.00 47.01  ? 60  LYS   C CB     1 
ATOM   7199  C  CG     . LYS   C 1  60  ? 15.166  -47.832  20.426   1.00 53.46  ? 60  LYS   C CG     1 
ATOM   7200  C  CD     . LYS   C 1  60  ? 16.110  -46.981  21.250   1.00 56.14  ? 60  LYS   C CD     1 
ATOM   7201  C  CE     . LYS   C 1  60  ? 15.757  -47.008  22.719   1.00 51.34  ? 60  LYS   C CE     1 
ATOM   7202  N  NZ     . LYS   C 1  60  ? 16.581  -46.009  23.451   1.00 57.76  ? 60  LYS   C NZ     1 
ATOM   7203  N  N      . HIS   C 1  61  ? 14.215  -48.914  17.460   1.00 51.90  ? 61  HIS   C N      1 
ATOM   7204  C  CA     . HIS   C 1  61  ? 14.487  -48.243  16.204   1.00 47.83  ? 61  HIS   C CA     1 
ATOM   7205  C  C      . HIS   C 1  61  ? 14.869  -46.806  16.514   1.00 47.47  ? 61  HIS   C C      1 
ATOM   7206  O  O      . HIS   C 1  61  ? 14.150  -46.107  17.242   1.00 50.08  ? 61  HIS   C O      1 
ATOM   7207  C  CB     . HIS   C 1  61  ? 13.278  -48.316  15.278   1.00 50.15  ? 61  HIS   C CB     1 
ATOM   7208  C  CG     . HIS   C 1  61  ? 12.829  -49.718  15.004   1.00 50.73  ? 61  HIS   C CG     1 
ATOM   7209  N  ND1    . HIS   C 1  61  ? 12.405  -50.567  16.001   1.00 45.19  ? 61  HIS   C ND1    1 
ATOM   7210  C  CD2    . HIS   C 1  61  ? 12.743  -50.421  13.851   1.00 50.93  ? 61  HIS   C CD2    1 
ATOM   7211  C  CE1    . HIS   C 1  61  ? 12.076  -51.732  15.474   1.00 52.32  ? 61  HIS   C CE1    1 
ATOM   7212  N  NE2    . HIS   C 1  61  ? 12.275  -51.672  14.171   1.00 51.34  ? 61  HIS   C NE2    1 
ATOM   7213  N  N      . VAL   C 1  62  ? 16.002  -46.382  15.981   1.00 45.04  ? 62  VAL   C N      1 
ATOM   7214  C  CA     . VAL   C 1  62  ? 16.682  -45.156  16.399   1.00 43.71  ? 62  VAL   C CA     1 
ATOM   7215  C  C      . VAL   C 1  62  ? 16.867  -44.269  15.202   1.00 41.05  ? 62  VAL   C C      1 
ATOM   7216  O  O      . VAL   C 1  62  ? 17.400  -44.704  14.169   1.00 41.26  ? 62  VAL   C O      1 
ATOM   7217  C  CB     . VAL   C 1  62  ? 18.034  -45.483  17.076   1.00 41.06  ? 62  VAL   C CB     1 
ATOM   7218  C  CG1    . VAL   C 1  62  ? 18.748  -44.233  17.528   1.00 33.96  ? 62  VAL   C CG1    1 
ATOM   7219  C  CG2    . VAL   C 1  62  ? 17.767  -46.419  18.236   1.00 42.65  ? 62  VAL   C CG2    1 
ATOM   7220  N  N      . PRO   C 1  63  ? 16.406  -43.017  15.226   1.00 37.81  ? 63  PRO   C N      1 
ATOM   7221  C  CA     . PRO   C 1  63  ? 16.560  -42.146  14.062   1.00 42.04  ? 63  PRO   C CA     1 
ATOM   7222  C  C      . PRO   C 1  63  ? 18.022  -41.987  13.666   1.00 42.93  ? 63  PRO   C C      1 
ATOM   7223  O  O      . PRO   C 1  63  ? 18.886  -41.707  14.502   1.00 40.59  ? 63  PRO   C O      1 
ATOM   7224  C  CB     . PRO   C 1  63  ? 15.960  -40.814  14.532   1.00 35.81  ? 63  PRO   C CB     1 
ATOM   7225  C  CG     . PRO   C 1  63  ? 15.038  -41.164  15.575   1.00 38.62  ? 63  PRO   C CG     1 
ATOM   7226  C  CD     . PRO   C 1  63  ? 15.614  -42.372  16.283   1.00 46.89  ? 63  PRO   C CD     1 
ATOM   7227  N  N      . ARG   C 1  64  ? 18.290  -42.148  12.372   1.00 38.32  ? 64  ARG   C N      1 
ATOM   7228  C  CA     . ARG   C 1  64  ? 19.557  -41.706  11.822   1.00 33.79  ? 64  ARG   C CA     1 
ATOM   7229  C  C      . ARG   C 1  64  ? 19.512  -40.188  11.734   1.00 38.12  ? 64  ARG   C C      1 
ATOM   7230  O  O      . ARG   C 1  64  ? 19.456  -39.622  10.640   1.00 42.59  ? 64  ARG   C O      1 
ATOM   7231  C  CB     . ARG   C 1  64  ? 19.809  -42.342  10.455   1.00 38.33  ? 64  ARG   C CB     1 
ATOM   7232  C  CG     . ARG   C 1  64  ? 19.772  -43.887  10.463   1.00 38.77  ? 64  ARG   C CG     1 
ATOM   7233  C  CD     . ARG   C 1  64  ? 20.197  -44.485  9.140    1.00 37.63  ? 64  ARG   C CD     1 
ATOM   7234  N  NE     . ARG   C 1  64  ? 19.754  -45.865  8.993    1.00 43.43  ? 64  ARG   C NE     1 
ATOM   7235  C  CZ     . ARG   C 1  64  ? 20.376  -46.926  9.498    1.00 42.38  ? 64  ARG   C CZ     1 
ATOM   7236  N  NH1    . ARG   C 1  64  ? 21.502  -46.813  10.185   1.00 37.10  ? 64  ARG   C NH1    1 
ATOM   7237  N  NH2    . ARG   C 1  64  ? 19.851  -48.131  9.313    1.00 37.56  ? 64  ARG   C NH2    1 
ATOM   7238  N  N      . ALA   C 1  65  ? 19.536  -39.516  12.882   1.00 36.23  ? 65  ALA   C N      1 
ATOM   7239  C  CA     . ALA   C 1  65  ? 19.431  -38.068  12.935   1.00 34.73  ? 65  ALA   C CA     1 
ATOM   7240  C  C      . ALA   C 1  65  ? 20.386  -37.516  13.975   1.00 35.77  ? 65  ALA   C C      1 
ATOM   7241  O  O      . ALA   C 1  65  ? 20.813  -38.211  14.896   1.00 34.26  ? 65  ALA   C O      1 
ATOM   7242  C  CB     . ALA   C 1  65  ? 18.006  -37.618  13.272   1.00 37.97  ? 65  ALA   C CB     1 
ATOM   7243  N  N      . VAL   C 1  66  ? 20.702  -36.238  13.814   1.00 39.35  ? 66  VAL   C N      1 
ATOM   7244  C  CA     . VAL   C 1  66  ? 21.501  -35.470  14.757   1.00 38.88  ? 66  VAL   C CA     1 
ATOM   7245  C  C      . VAL   C 1  66  ? 20.803  -34.130  14.928   1.00 37.57  ? 66  VAL   C C      1 
ATOM   7246  O  O      . VAL   C 1  66  ? 20.388  -33.513  13.942   1.00 37.94  ? 66  VAL   C O      1 
ATOM   7247  C  CB     . VAL   C 1  66  ? 22.956  -35.274  14.264   1.00 42.81  ? 66  VAL   C CB     1 
ATOM   7248  C  CG1    . VAL   C 1  66  ? 23.668  -34.176  15.066   1.00 38.20  ? 66  VAL   C CG1    1 
ATOM   7249  C  CG2    . VAL   C 1  66  ? 23.749  -36.557  14.391   1.00 41.76  ? 66  VAL   C CG2    1 
ATOM   7250  N  N      . PHE   C 1  67  ? 20.645  -33.695  16.171   1.00 37.14  ? 67  PHE   C N      1 
ATOM   7251  C  CA     . PHE   C 1  67  ? 20.116  -32.372  16.462   1.00 37.12  ? 67  PHE   C CA     1 
ATOM   7252  C  C      . PHE   C 1  67  ? 21.257  -31.535  17.012   1.00 35.73  ? 67  PHE   C C      1 
ATOM   7253  O  O      . PHE   C 1  67  ? 21.888  -31.921  17.998   1.00 39.11  ? 67  PHE   C O      1 
ATOM   7254  C  CB     . PHE   C 1  67  ? 18.956  -32.428  17.461   1.00 41.09  ? 67  PHE   C CB     1 
ATOM   7255  C  CG     . PHE   C 1  67  ? 17.729  -33.141  16.953   1.00 36.57  ? 67  PHE   C CG     1 
ATOM   7256  C  CD1    . PHE   C 1  67  ? 17.815  -34.395  16.395   1.00 34.38  ? 67  PHE   C CD1    1 
ATOM   7257  C  CD2    . PHE   C 1  67  ? 16.480  -32.563  17.082   1.00 35.93  ? 67  PHE   C CD2    1 
ATOM   7258  C  CE1    . PHE   C 1  67  ? 16.669  -35.058  15.946   1.00 43.31  ? 67  PHE   C CE1    1 
ATOM   7259  C  CE2    . PHE   C 1  67  ? 15.338  -33.226  16.638   1.00 42.67  ? 67  PHE   C CE2    1 
ATOM   7260  C  CZ     . PHE   C 1  67  ? 15.428  -34.478  16.060   1.00 35.52  ? 67  PHE   C CZ     1 
ATOM   7261  N  N      . VAL   C 1  68  ? 21.532  -30.411  16.367   1.00 30.97  ? 68  VAL   C N      1 
ATOM   7262  C  CA     . VAL   C 1  68  ? 22.590  -29.513  16.790   1.00 33.25  ? 68  VAL   C CA     1 
ATOM   7263  C  C      . VAL   C 1  68  ? 21.975  -28.141  16.976   1.00 35.71  ? 68  VAL   C C      1 
ATOM   7264  O  O      . VAL   C 1  68  ? 21.223  -27.676  16.119   1.00 37.97  ? 68  VAL   C O      1 
ATOM   7265  C  CB     . VAL   C 1  68  ? 23.738  -29.445  15.771   1.00 32.27  ? 68  VAL   C CB     1 
ATOM   7266  C  CG1    . VAL   C 1  68  ? 24.956  -28.843  16.427   1.00 33.45  ? 68  VAL   C CG1    1 
ATOM   7267  C  CG2    . VAL   C 1  68  ? 24.032  -30.821  15.201   1.00 37.11  ? 68  VAL   C CG2    1 
ATOM   7268  N  N      . ASP   C 1  69  ? 22.256  -27.516  18.104   1.00 34.33  ? 69  ASP   C N      1 
ATOM   7269  C  CA     . ASP   C 1  69  ? 21.864  -26.143  18.325   1.00 37.47  ? 69  ASP   C CA     1 
ATOM   7270  C  C      . ASP   C 1  69  ? 22.907  -25.555  19.253   1.00 43.12  ? 69  ASP   C C      1 
ATOM   7271  O  O      . ASP   C 1  69  ? 23.452  -26.268  20.106   1.00 40.80  ? 69  ASP   C O      1 
ATOM   7272  C  CB     . ASP   C 1  69  ? 20.450  -26.012  18.919   1.00 40.22  ? 69  ASP   C CB     1 
ATOM   7273  C  CG     . ASP   C 1  69  ? 19.934  -24.574  18.895   1.00 37.35  ? 69  ASP   C CG     1 
ATOM   7274  O  OD1    . ASP   C 1  69  ? 20.646  -23.696  18.336   1.00 35.98  ? 69  ASP   C OD1    1 
ATOM   7275  O  OD2    . ASP   C 1  69  ? 18.825  -24.328  19.439   1.00 38.48  ? 69  ASP   C OD2    1 
ATOM   7276  N  N      . LEU   C 1  70  ? 23.216  -24.274  19.041   1.00 34.36  ? 70  LEU   C N      1 
ATOM   7277  C  CA     . LEU   C 1  70  ? 24.237  -23.596  19.812   1.00 37.48  ? 70  LEU   C CA     1 
ATOM   7278  C  C      . LEU   C 1  70  ? 23.782  -23.228  21.226   1.00 44.86  ? 70  LEU   C C      1 
ATOM   7279  O  O      . LEU   C 1  70  ? 24.585  -22.704  22.011   1.00 48.57  ? 70  LEU   C O      1 
ATOM   7280  C  CB     . LEU   C 1  70  ? 24.681  -22.364  19.042   1.00 37.32  ? 70  LEU   C CB     1 
ATOM   7281  C  CG     . LEU   C 1  70  ? 25.506  -22.693  17.816   1.00 36.76  ? 70  LEU   C CG     1 
ATOM   7282  C  CD1    . LEU   C 1  70  ? 26.146  -21.439  17.233   1.00 40.78  ? 70  LEU   C CD1    1 
ATOM   7283  C  CD2    . LEU   C 1  70  ? 26.557  -23.720  18.164   1.00 37.25  ? 70  LEU   C CD2    1 
ATOM   7284  N  N      . GLU   C 1  71  ? 22.523  -23.473  21.570   1.00 46.38  ? 71  GLU   C N      1 
ATOM   7285  C  CA     . GLU   C 1  71  ? 22.079  -23.361  22.952   1.00 46.78  ? 71  GLU   C CA     1 
ATOM   7286  C  C      . GLU   C 1  71  ? 21.158  -24.532  23.277   1.00 49.37  ? 71  GLU   C C      1 
ATOM   7287  O  O      . GLU   C 1  71  ? 20.755  -25.292  22.379   1.00 46.34  ? 71  GLU   C O      1 
ATOM   7288  C  CB     . GLU   C 1  71  ? 21.385  -22.018  23.225   1.00 46.24  ? 71  GLU   C CB     1 
ATOM   7289  C  CG     . GLU   C 1  71  ? 20.349  -21.592  22.192   1.00 45.19  ? 71  GLU   C CG     1 
ATOM   7290  C  CD     . GLU   C 1  71  ? 18.909  -21.671  22.704   1.00 51.33  ? 71  GLU   C CD     1 
ATOM   7291  O  OE1    . GLU   C 1  71  ? 18.728  -22.037  23.888   1.00 48.71  ? 71  GLU   C OE1    1 
ATOM   7292  O  OE2    . GLU   C 1  71  ? 17.959  -21.401  21.911   1.00 56.75  ? 71  GLU   C OE2    1 
ATOM   7293  N  N      . PRO   C 1  72  ? 20.808  -24.704  24.556   1.00 49.72  ? 72  PRO   C N      1 
ATOM   7294  C  CA     . PRO   C 1  72  ? 20.175  -25.950  24.995   1.00 41.16  ? 72  PRO   C CA     1 
ATOM   7295  C  C      . PRO   C 1  72  ? 18.681  -25.848  25.226   1.00 42.77  ? 72  PRO   C C      1 
ATOM   7296  O  O      . PRO   C 1  72  ? 18.021  -26.884  25.361   1.00 45.45  ? 72  PRO   C O      1 
ATOM   7297  C  CB     . PRO   C 1  72  ? 20.904  -26.232  26.301   1.00 42.23  ? 72  PRO   C CB     1 
ATOM   7298  C  CG     . PRO   C 1  72  ? 21.059  -24.848  26.874   1.00 40.78  ? 72  PRO   C CG     1 
ATOM   7299  C  CD     . PRO   C 1  72  ? 21.304  -23.919  25.698   1.00 41.56  ? 72  PRO   C CD     1 
ATOM   7300  N  N      . THR   C 1  73  ? 18.133  -24.629  25.298   1.00 45.56  ? 73  THR   C N      1 
ATOM   7301  C  CA     . THR   C 1  73  ? 16.687  -24.451  25.444   1.00 44.91  ? 73  THR   C CA     1 
ATOM   7302  C  C      . THR   C 1  73  ? 15.910  -25.431  24.569   1.00 46.35  ? 73  THR   C C      1 
ATOM   7303  O  O      . THR   C 1  73  ? 15.180  -26.290  25.072   1.00 51.83  ? 73  THR   C O      1 
ATOM   7304  C  CB     . THR   C 1  73  ? 16.288  -23.016  25.083   1.00 47.96  ? 73  THR   C CB     1 
ATOM   7305  O  OG1    . THR   C 1  73  ? 17.063  -22.100  25.841   1.00 59.49  ? 73  THR   C OG1    1 
ATOM   7306  C  CG2    . THR   C 1  73  ? 14.806  -22.755  25.335   1.00 50.92  ? 73  THR   C CG2    1 
ATOM   7307  N  N      . VAL   C 1  74  ? 16.086  -25.325  23.250   1.00 42.97  ? 74  VAL   C N      1 
ATOM   7308  C  CA     . VAL   C 1  74  ? 15.247  -26.062  22.319   1.00 43.87  ? 74  VAL   C CA     1 
ATOM   7309  C  C      . VAL   C 1  74  ? 15.549  -27.561  22.372   1.00 44.29  ? 74  VAL   C C      1 
ATOM   7310  O  O      . VAL   C 1  74  ? 14.635  -28.391  22.306   1.00 44.54  ? 74  VAL   C O      1 
ATOM   7311  C  CB     . VAL   C 1  74  ? 15.411  -25.491  20.896   1.00 41.66  ? 74  VAL   C CB     1 
ATOM   7312  C  CG1    . VAL   C 1  74  ? 14.339  -26.039  19.997   1.00 36.06  ? 74  VAL   C CG1    1 
ATOM   7313  C  CG2    . VAL   C 1  74  ? 15.363  -23.964  20.897   1.00 36.62  ? 74  VAL   C CG2    1 
ATOM   7314  N  N      . ILE   C 1  75  ? 16.820  -27.949  22.465   1.00 45.22  ? 75  ILE   C N      1 
ATOM   7315  C  CA     . ILE   C 1  75  ? 17.065  -29.390  22.439   1.00 46.93  ? 75  ILE   C CA     1 
ATOM   7316  C  C      . ILE   C 1  75  ? 16.799  -30.018  23.820   1.00 49.63  ? 75  ILE   C C      1 
ATOM   7317  O  O      . ILE   C 1  75  ? 16.410  -31.194  23.906   1.00 45.92  ? 75  ILE   C O      1 
ATOM   7318  C  CB     . ILE   C 1  75  ? 18.477  -29.688  21.879   1.00 41.67  ? 75  ILE   C CB     1 
ATOM   7319  C  CG1    . ILE   C 1  75  ? 18.457  -29.587  20.332   1.00 38.78  ? 75  ILE   C CG1    1 
ATOM   7320  C  CG2    . ILE   C 1  75  ? 18.952  -31.079  22.264   1.00 37.54  ? 75  ILE   C CG2    1 
ATOM   7321  C  CD1    . ILE   C 1  75  ? 19.803  -29.270  19.686   1.00 32.25  ? 75  ILE   C CD1    1 
ATOM   7322  N  N      . ASP   C 1  76  ? 16.935  -29.250  24.910   1.00 46.13  ? 76  ASP   C N      1 
ATOM   7323  C  CA     . ASP   C 1  76  ? 16.479  -29.750  26.210   1.00 47.42  ? 76  ASP   C CA     1 
ATOM   7324  C  C      . ASP   C 1  76  ? 15.041  -30.259  26.162   1.00 44.56  ? 76  ASP   C C      1 
ATOM   7325  O  O      . ASP   C 1  76  ? 14.697  -31.203  26.878   1.00 47.29  ? 76  ASP   C O      1 
ATOM   7326  C  CB     . ASP   C 1  76  ? 16.596  -28.664  27.278   1.00 40.94  ? 76  ASP   C CB     1 
ATOM   7327  C  CG     . ASP   C 1  76  ? 18.019  -28.442  27.716   1.00 50.11  ? 76  ASP   C CG     1 
ATOM   7328  O  OD1    . ASP   C 1  76  ? 18.852  -29.345  27.450   1.00 54.66  ? 76  ASP   C OD1    1 
ATOM   7329  O  OD2    . ASP   C 1  76  ? 18.317  -27.349  28.271   1.00 49.26  ? 76  ASP   C OD2    1 
ATOM   7330  N  N      . GLU   C 1  77  ? 14.183  -29.658  25.335   1.00 38.91  ? 77  GLU   C N      1 
ATOM   7331  C  CA     . GLU   C 1  77  ? 12.809  -30.140  25.279   1.00 43.29  ? 77  GLU   C CA     1 
ATOM   7332  C  C      . GLU   C 1  77  ? 12.705  -31.490  24.572   1.00 46.44  ? 77  GLU   C C      1 
ATOM   7333  O  O      . GLU   C 1  77  ? 11.831  -32.290  24.913   1.00 48.33  ? 77  GLU   C O      1 
ATOM   7334  C  CB     . GLU   C 1  77  ? 11.902  -29.097  24.628   1.00 48.38  ? 77  GLU   C CB     1 
ATOM   7335  C  CG     . GLU   C 1  77  ? 11.319  -28.087  25.647   1.00 55.77  ? 77  GLU   C CG     1 
ATOM   7336  C  CD     . GLU   C 1  77  ? 10.572  -26.923  25.003   1.00 73.14  ? 77  GLU   C CD     1 
ATOM   7337  O  OE1    . GLU   C 1  77  ? 9.451   -27.135  24.484   1.00 83.06  ? 77  GLU   C OE1    1 
ATOM   7338  O  OE2    . GLU   C 1  77  ? 11.103  -25.789  25.012   1.00 73.55  ? 77  GLU   C OE2    1 
ATOM   7339  N  N      . VAL   C 1  78  ? 13.581  -31.773  23.602   1.00 47.04  ? 78  VAL   C N      1 
ATOM   7340  C  CA     . VAL   C 1  78  ? 13.660  -33.123  23.044   1.00 47.81  ? 78  VAL   C CA     1 
ATOM   7341  C  C      . VAL   C 1  78  ? 14.139  -34.109  24.110   1.00 48.92  ? 78  VAL   C C      1 
ATOM   7342  O  O      . VAL   C 1  78  ? 13.601  -35.213  24.249   1.00 51.45  ? 78  VAL   C O      1 
ATOM   7343  C  CB     . VAL   C 1  78  ? 14.582  -33.153  21.805   1.00 44.85  ? 78  VAL   C CB     1 
ATOM   7344  C  CG1    . VAL   C 1  78  ? 14.713  -34.568  21.262   1.00 34.46  ? 78  VAL   C CG1    1 
ATOM   7345  C  CG2    . VAL   C 1  78  ? 14.095  -32.206  20.729   1.00 40.22  ? 78  VAL   C CG2    1 
ATOM   7346  N  N      . ARG   C 1  79  ? 15.175  -33.731  24.863   1.00 48.08  ? 79  ARG   C N      1 
ATOM   7347  C  CA     . ARG   C 1  79  ? 15.747  -34.628  25.860   1.00 48.96  ? 79  ARG   C CA     1 
ATOM   7348  C  C      . ARG   C 1  79  ? 14.745  -35.006  26.944   1.00 54.53  ? 79  ARG   C C      1 
ATOM   7349  O  O      . ARG   C 1  79  ? 14.938  -36.027  27.616   1.00 50.33  ? 79  ARG   C O      1 
ATOM   7350  C  CB     . ARG   C 1  79  ? 16.993  -33.995  26.497   1.00 40.60  ? 79  ARG   C CB     1 
ATOM   7351  C  CG     . ARG   C 1  79  ? 18.266  -34.061  25.638   1.00 45.31  ? 79  ARG   C CG     1 
ATOM   7352  C  CD     . ARG   C 1  79  ? 19.351  -33.064  26.120   1.00 45.74  ? 79  ARG   C CD     1 
ATOM   7353  N  NE     . ARG   C 1  79  ? 20.530  -33.042  25.255   1.00 45.34  ? 79  ARG   C NE     1 
ATOM   7354  C  CZ     . ARG   C 1  79  ? 21.295  -31.975  25.034   1.00 44.50  ? 79  ARG   C CZ     1 
ATOM   7355  N  NH1    . ARG   C 1  79  ? 21.068  -30.813  25.635   1.00 39.12  ? 79  ARG   C NH1    1 
ATOM   7356  N  NH2    . ARG   C 1  79  ? 22.311  -32.074  24.181   1.00 39.42  ? 79  ARG   C NH2    1 
ATOM   7357  N  N      . THR   C 1  80  ? 13.672  -34.226  27.127   1.00 53.45  ? 80  THR   C N      1 
ATOM   7358  C  CA     . THR   C 1  80  ? 12.717  -34.491  28.200   1.00 51.88  ? 80  THR   C CA     1 
ATOM   7359  C  C      . THR   C 1  80  ? 11.291  -34.724  27.709   1.00 54.30  ? 80  THR   C C      1 
ATOM   7360  O  O      . THR   C 1  80  ? 10.382  -34.845  28.532   1.00 58.46  ? 80  THR   C O      1 
ATOM   7361  C  CB     . THR   C 1  80  ? 12.726  -33.340  29.210   1.00 49.69  ? 80  THR   C CB     1 
ATOM   7362  O  OG1    . THR   C 1  80  ? 12.334  -32.129  28.558   1.00 53.02  ? 80  THR   C OG1    1 
ATOM   7363  C  CG2    . THR   C 1  80  ? 14.116  -33.160  29.810   1.00 48.92  ? 80  THR   C CG2    1 
ATOM   7364  N  N      . GLY   C 1  81  ? 11.064  -34.803  26.400   1.00 55.53  ? 81  GLY   C N      1 
ATOM   7365  C  CA     . GLY   C 1  81  ? 9.728   -34.817  25.849   1.00 57.78  ? 81  GLY   C CA     1 
ATOM   7366  C  C      . GLY   C 1  81  ? 9.224   -36.210  25.507   1.00 58.38  ? 81  GLY   C C      1 
ATOM   7367  O  O      . GLY   C 1  81  ? 9.880   -37.228  25.740   1.00 59.65  ? 81  GLY   C O      1 
ATOM   7368  N  N      . THR   C 1  82  ? 8.028   -36.234  24.911   1.00 56.90  ? 82  THR   C N      1 
ATOM   7369  C  CA     . THR   C 1  82  ? 7.356   -37.494  24.611   1.00 59.05  ? 82  THR   C CA     1 
ATOM   7370  C  C      . THR   C 1  82  ? 8.288   -38.526  23.987   1.00 60.40  ? 82  THR   C C      1 
ATOM   7371  O  O      . THR   C 1  82  ? 8.116   -39.733  24.212   1.00 64.82  ? 82  THR   C O      1 
ATOM   7372  C  CB     . THR   C 1  82  ? 6.185   -37.259  23.657   1.00 59.27  ? 82  THR   C CB     1 
ATOM   7373  O  OG1    . THR   C 1  82  ? 5.400   -36.149  24.106   1.00 63.92  ? 82  THR   C OG1    1 
ATOM   7374  C  CG2    . THR   C 1  82  ? 5.327   -38.500  23.577   1.00 57.25  ? 82  THR   C CG2    1 
ATOM   7375  N  N      . TYR   C 1  83  ? 9.250   -38.086  23.170   1.00 60.02  ? 83  TYR   C N      1 
ATOM   7376  C  CA     . TYR   C 1  83  ? 10.064  -38.998  22.371   1.00 59.30  ? 83  TYR   C CA     1 
ATOM   7377  C  C      . TYR   C 1  83  ? 11.520  -39.030  22.839   1.00 60.23  ? 83  TYR   C C      1 
ATOM   7378  O  O      . TYR   C 1  83  ? 12.408  -39.452  22.092   1.00 57.23  ? 83  TYR   C O      1 
ATOM   7379  C  CB     . TYR   C 1  83  ? 9.954   -38.634  20.890   1.00 47.14  ? 83  TYR   C CB     1 
ATOM   7380  C  CG     . TYR   C 1  83  ? 8.662   -39.113  20.251   1.00 52.82  ? 83  TYR   C CG     1 
ATOM   7381  C  CD1    . TYR   C 1  83  ? 8.543   -40.417  19.784   1.00 52.31  ? 83  TYR   C CD1    1 
ATOM   7382  C  CD2    . TYR   C 1  83  ? 7.557   -38.268  20.119   1.00 50.77  ? 83  TYR   C CD2    1 
ATOM   7383  C  CE1    . TYR   C 1  83  ? 7.366   -40.880  19.202   1.00 49.51  ? 83  TYR   C CE1    1 
ATOM   7384  C  CE2    . TYR   C 1  83  ? 6.364   -38.724  19.536   1.00 51.90  ? 83  TYR   C CE2    1 
ATOM   7385  C  CZ     . TYR   C 1  83  ? 6.276   -40.044  19.074   1.00 55.64  ? 83  TYR   C CZ     1 
ATOM   7386  O  OH     . TYR   C 1  83  ? 5.109   -40.544  18.478   1.00 55.80  ? 83  TYR   C OH     1 
ATOM   7387  N  N      . ARG   C 1  84  ? 11.764  -38.633  24.088   1.00 55.21  ? 84  ARG   C N      1 
ATOM   7388  C  CA     . ARG   C 1  84  ? 13.113  -38.625  24.629   1.00 53.52  ? 84  ARG   C CA     1 
ATOM   7389  C  C      . ARG   C 1  84  ? 13.784  -39.994  24.534   1.00 54.36  ? 84  ARG   C C      1 
ATOM   7390  O  O      . ARG   C 1  84  ? 15.005  -40.080  24.356   1.00 58.28  ? 84  ARG   C O      1 
ATOM   7391  C  CB     . ARG   C 1  84  ? 13.069  -38.142  26.079   1.00 57.47  ? 84  ARG   C CB     1 
ATOM   7392  C  CG     . ARG   C 1  84  ? 12.428  -39.140  27.036   1.00 62.86  ? 84  ARG   C CG     1 
ATOM   7393  C  CD     . ARG   C 1  84  ? 12.486  -38.668  28.500   1.00 65.37  ? 84  ARG   C CD     1 
ATOM   7394  N  NE     . ARG   C 1  84  ? 11.440  -39.279  29.313   1.00 67.51  ? 84  ARG   C NE     1 
ATOM   7395  C  CZ     . ARG   C 1  84  ? 10.141  -39.145  29.081   1.00 67.12  ? 84  ARG   C CZ     1 
ATOM   7396  N  NH1    . ARG   C 1  84  ? 9.689   -38.346  28.131   1.00 57.74  ? 84  ARG   C NH1    1 
ATOM   7397  N  NH2    . ARG   C 1  84  ? 9.275   -39.834  29.818   1.00 78.01  ? 84  ARG   C NH2    1 
ATOM   7398  N  N      . GLN   C 1  85  ? 13.025  -41.079  24.669   1.00 57.52  ? 85  GLN   C N      1 
ATOM   7399  C  CA     . GLN   C 1  85  ? 13.663  -42.398  24.636   1.00 58.76  ? 85  GLN   C CA     1 
ATOM   7400  C  C      . GLN   C 1  85  ? 14.122  -42.801  23.247   1.00 54.81  ? 85  GLN   C C      1 
ATOM   7401  O  O      . GLN   C 1  85  ? 14.854  -43.786  23.112   1.00 57.92  ? 85  GLN   C O      1 
ATOM   7402  C  CB     . GLN   C 1  85  ? 12.716  -43.474  25.154   1.00 62.06  ? 85  GLN   C CB     1 
ATOM   7403  C  CG     . GLN   C 1  85  ? 12.757  -43.660  26.650   1.00 64.36  ? 85  GLN   C CG     1 
ATOM   7404  C  CD     . GLN   C 1  85  ? 11.387  -43.966  27.200   1.00 67.66  ? 85  GLN   C CD     1 
ATOM   7405  O  OE1    . GLN   C 1  85  ? 10.509  -44.430  26.467   1.00 71.07  ? 85  GLN   C OE1    1 
ATOM   7406  N  NE2    . GLN   C 1  85  ? 11.185  -43.700  28.490   1.00 73.34  ? 85  GLN   C NE2    1 
ATOM   7407  N  N      . LEU   C 1  86  ? 13.685  -42.083  22.220   1.00 53.83  ? 86  LEU   C N      1 
ATOM   7408  C  CA     . LEU   C 1  86  ? 13.968  -42.483  20.852   1.00 50.87  ? 86  LEU   C CA     1 
ATOM   7409  C  C      . LEU   C 1  86  ? 15.417  -42.208  20.490   1.00 53.89  ? 86  LEU   C C      1 
ATOM   7410  O  O      . LEU   C 1  86  ? 16.017  -42.953  19.705   1.00 53.27  ? 86  LEU   C O      1 
ATOM   7411  C  CB     . LEU   C 1  86  ? 13.028  -41.731  19.913   1.00 52.44  ? 86  LEU   C CB     1 
ATOM   7412  C  CG     . LEU   C 1  86  ? 12.668  -42.203  18.515   1.00 47.75  ? 86  LEU   C CG     1 
ATOM   7413  C  CD1    . LEU   C 1  86  ? 12.042  -43.594  18.544   1.00 49.64  ? 86  LEU   C CD1    1 
ATOM   7414  C  CD2    . LEU   C 1  86  ? 11.724  -41.178  17.932   1.00 38.81  ? 86  LEU   C CD2    1 
ATOM   7415  N  N      . PHE   C 1  87  ? 15.990  -41.149  21.050   1.00 48.83  ? 87  PHE   C N      1 
ATOM   7416  C  CA     . PHE   C 1  87  ? 17.295  -40.662  20.638   1.00 51.27  ? 87  PHE   C CA     1 
ATOM   7417  C  C      . PHE   C 1  87  ? 18.333  -41.008  21.687   1.00 51.83  ? 87  PHE   C C      1 
ATOM   7418  O  O      . PHE   C 1  87  ? 18.091  -40.857  22.888   1.00 61.34  ? 87  PHE   C O      1 
ATOM   7419  C  CB     . PHE   C 1  87  ? 17.291  -39.139  20.423   1.00 52.86  ? 87  PHE   C CB     1 
ATOM   7420  C  CG     . PHE   C 1  87  ? 16.265  -38.661  19.447   1.00 46.48  ? 87  PHE   C CG     1 
ATOM   7421  C  CD1    . PHE   C 1  87  ? 16.427  -38.890  18.085   1.00 41.31  ? 87  PHE   C CD1    1 
ATOM   7422  C  CD2    . PHE   C 1  87  ? 15.140  -37.969  19.886   1.00 50.84  ? 87  PHE   C CD2    1 
ATOM   7423  C  CE1    . PHE   C 1  87  ? 15.466  -38.461  17.180   1.00 45.21  ? 87  PHE   C CE1    1 
ATOM   7424  C  CE2    . PHE   C 1  87  ? 14.175  -37.521  18.978   1.00 46.51  ? 87  PHE   C CE2    1 
ATOM   7425  C  CZ     . PHE   C 1  87  ? 14.342  -37.774  17.622   1.00 43.52  ? 87  PHE   C CZ     1 
ATOM   7426  N  N      . HIS   C 1  88  ? 19.484  -41.427  21.231   1.00 50.74  ? 88  HIS   C N      1 
ATOM   7427  C  CA     . HIS   C 1  88  ? 20.609  -41.620  22.123   1.00 46.94  ? 88  HIS   C CA     1 
ATOM   7428  C  C      . HIS   C 1  88  ? 21.177  -40.257  22.496   1.00 48.95  ? 88  HIS   C C      1 
ATOM   7429  O  O      . HIS   C 1  88  ? 21.393  -39.421  21.617   1.00 50.74  ? 88  HIS   C O      1 
ATOM   7430  C  CB     . HIS   C 1  88  ? 21.668  -42.489  21.442   1.00 53.65  ? 88  HIS   C CB     1 
ATOM   7431  C  CG     . HIS   C 1  88  ? 22.907  -42.712  22.257   1.00 59.04  ? 88  HIS   C CG     1 
ATOM   7432  N  ND1    . HIS   C 1  88  ? 23.599  -41.687  22.875   1.00 60.68  ? 88  HIS   C ND1    1 
ATOM   7433  C  CD2    . HIS   C 1  88  ? 23.593  -43.846  22.533   1.00 54.37  ? 88  HIS   C CD2    1 
ATOM   7434  C  CE1    . HIS   C 1  88  ? 24.644  -42.183  23.512   1.00 63.72  ? 88  HIS   C CE1    1 
ATOM   7435  N  NE2    . HIS   C 1  88  ? 24.663  -43.490  23.320   1.00 67.20  ? 88  HIS   C NE2    1 
ATOM   7436  N  N      . PRO   C 1  89  ? 21.417  -40.003  23.753   1.00 50.89  ? 89  PRO   C N      1 
ATOM   7437  C  CA     . PRO   C 1  89  ? 21.960  -38.703  24.169   1.00 51.74  ? 89  PRO   C CA     1 
ATOM   7438  C  C      . PRO   C 1  89  ? 22.929  -38.083  23.179   1.00 48.54  ? 89  PRO   C C      1 
ATOM   7439  O  O      . PRO   C 1  89  ? 22.837  -36.896  22.858   1.00 53.77  ? 89  PRO   C O      1 
ATOM   7440  C  CB     . PRO   C 1  89  ? 22.675  -39.046  25.476   1.00 51.74  ? 89  PRO   C CB     1 
ATOM   7441  C  CG     . PRO   C 1  89  ? 21.862  -40.163  26.023   1.00 52.48  ? 89  PRO   C CG     1 
ATOM   7442  C  CD     . PRO   C 1  89  ? 21.307  -40.946  24.871   1.00 48.46  ? 89  PRO   C CD     1 
ATOM   7443  N  N      . GLU   C 1  90  ? 23.871  -38.887  22.694   1.00 53.60  ? 90  GLU   C N      1 
ATOM   7444  C  CA     . GLU   C 1  90  ? 24.944  -38.397  21.833   1.00 58.40  ? 90  GLU   C CA     1 
ATOM   7445  C  C      . GLU   C 1  90  ? 24.446  -37.881  20.482   1.00 55.14  ? 90  GLU   C C      1 
ATOM   7446  O  O      . GLU   C 1  90  ? 25.210  -37.213  19.766   1.00 45.77  ? 90  GLU   C O      1 
ATOM   7447  C  CB     . GLU   C 1  90  ? 25.974  -39.507  21.618   1.00 57.47  ? 90  GLU   C CB     1 
ATOM   7448  C  CG     . GLU   C 1  90  ? 26.728  -39.946  22.863   1.00 56.71  ? 90  GLU   C CG     1 
ATOM   7449  C  CD     . GLU   C 1  90  ? 28.059  -40.546  22.479   1.00 68.94  ? 90  GLU   C CD     1 
ATOM   7450  O  OE1    . GLU   C 1  90  ? 28.054  -41.387  21.553   1.00 74.43  ? 90  GLU   C OE1    1 
ATOM   7451  O  OE2    . GLU   C 1  90  ? 29.104  -40.154  23.052   1.00 68.33  ? 90  GLU   C OE2    1 
ATOM   7452  N  N      . GLN   C 1  91  ? 23.202  -38.197  20.110   1.00 50.25  ? 91  GLN   C N      1 
ATOM   7453  C  CA     . GLN   C 1  91  ? 22.580  -37.608  18.934   1.00 44.56  ? 91  GLN   C CA     1 
ATOM   7454  C  C      . GLN   C 1  91  ? 22.139  -36.169  19.167   1.00 49.34  ? 91  GLN   C C      1 
ATOM   7455  O  O      . GLN   C 1  91  ? 21.921  -35.445  18.187   1.00 51.77  ? 91  GLN   C O      1 
ATOM   7456  C  CB     . GLN   C 1  91  ? 21.366  -38.433  18.515   1.00 40.22  ? 91  GLN   C CB     1 
ATOM   7457  C  CG     . GLN   C 1  91  ? 21.698  -39.714  17.829   1.00 39.60  ? 91  GLN   C CG     1 
ATOM   7458  C  CD     . GLN   C 1  91  ? 20.486  -40.589  17.666   1.00 45.73  ? 91  GLN   C CD     1 
ATOM   7459  O  OE1    . GLN   C 1  91  ? 20.276  -41.514  18.447   1.00 47.01  ? 91  GLN   C OE1    1 
ATOM   7460  N  NE2    . GLN   C 1  91  ? 19.662  -40.294  16.653   1.00 40.61  ? 91  GLN   C NE2    1 
ATOM   7461  N  N      . LEU   C 1  92  ? 21.986  -35.743  20.432   1.00 42.80  ? 92  LEU   C N      1 
ATOM   7462  C  CA     . LEU   C 1  92  ? 21.436  -34.437  20.783   1.00 40.04  ? 92  LEU   C CA     1 
ATOM   7463  C  C      . LEU   C 1  92  ? 22.553  -33.555  21.339   1.00 46.43  ? 92  LEU   C C      1 
ATOM   7464  O  O      . LEU   C 1  92  ? 22.973  -33.737  22.490   1.00 48.57  ? 92  LEU   C O      1 
ATOM   7465  C  CB     . LEU   C 1  92  ? 20.302  -34.593  21.788   1.00 40.89  ? 92  LEU   C CB     1 
ATOM   7466  C  CG     . LEU   C 1  92  ? 19.162  -35.578  21.518   1.00 38.42  ? 92  LEU   C CG     1 
ATOM   7467  C  CD1    . LEU   C 1  92  ? 18.077  -35.248  22.481   1.00 42.32  ? 92  LEU   C CD1    1 
ATOM   7468  C  CD2    . LEU   C 1  92  ? 18.645  -35.410  20.133   1.00 42.49  ? 92  LEU   C CD2    1 
ATOM   7469  N  N      . ILE   C 1  93  ? 23.002  -32.583  20.534   1.00 36.93  ? 93  ILE   C N      1 
ATOM   7470  C  CA     . ILE   C 1  93  ? 24.227  -31.823  20.769   1.00 34.99  ? 93  ILE   C CA     1 
ATOM   7471  C  C      . ILE   C 1  93  ? 23.880  -30.351  20.963   1.00 40.77  ? 93  ILE   C C      1 
ATOM   7472  O  O      . ILE   C 1  93  ? 23.284  -29.728  20.076   1.00 43.72  ? 93  ILE   C O      1 
ATOM   7473  C  CB     . ILE   C 1  93  ? 25.216  -31.983  19.602   1.00 38.70  ? 93  ILE   C CB     1 
ATOM   7474  C  CG1    . ILE   C 1  93  ? 25.536  -33.456  19.359   1.00 40.57  ? 93  ILE   C CG1    1 
ATOM   7475  C  CG2    . ILE   C 1  93  ? 26.489  -31.160  19.827   1.00 35.78  ? 93  ILE   C CG2    1 
ATOM   7476  C  CD1    . ILE   C 1  93  ? 26.481  -33.663  18.178   1.00 47.94  ? 93  ILE   C CD1    1 
ATOM   7477  N  N      . THR   C 1  94  ? 24.313  -29.773  22.083   1.00 37.85  ? 94  THR   C N      1 
ATOM   7478  C  CA     . THR   C 1  94  ? 24.005  -28.385  22.368   1.00 36.12  ? 94  THR   C CA     1 
ATOM   7479  C  C      . THR   C 1  94  ? 25.242  -27.664  22.881   1.00 39.89  ? 94  THR   C C      1 
ATOM   7480  O  O      . THR   C 1  94  ? 26.126  -28.267  23.482   1.00 44.89  ? 94  THR   C O      1 
ATOM   7481  C  CB     . THR   C 1  94  ? 22.861  -28.269  23.385   1.00 42.28  ? 94  THR   C CB     1 
ATOM   7482  O  OG1    . THR   C 1  94  ? 23.363  -28.521  24.702   1.00 52.23  ? 94  THR   C OG1    1 
ATOM   7483  C  CG2    . THR   C 1  94  ? 21.787  -29.298  23.085   1.00 39.62  ? 94  THR   C CG2    1 
ATOM   7484  N  N      . GLY   C 1  95  ? 25.302  -26.362  22.625   1.00 46.43  ? 95  GLY   C N      1 
ATOM   7485  C  CA     . GLY   C 1  95  ? 26.287  -25.482  23.227   1.00 39.15  ? 95  GLY   C CA     1 
ATOM   7486  C  C      . GLY   C 1  95  ? 25.743  -24.798  24.461   1.00 44.90  ? 95  GLY   C C      1 
ATOM   7487  O  O      . GLY   C 1  95  ? 24.854  -25.313  25.150   1.00 48.98  ? 95  GLY   C O      1 
ATOM   7488  N  N      . LYS   C 1  96  ? 26.279  -23.618  24.746   1.00 43.04  ? 96  LYS   C N      1 
ATOM   7489  C  CA     . LYS   C 1  96  ? 25.881  -22.849  25.921   1.00 46.66  ? 96  LYS   C CA     1 
ATOM   7490  C  C      . LYS   C 1  96  ? 25.404  -21.457  25.575   1.00 50.07  ? 96  LYS   C C      1 
ATOM   7491  O  O      . LYS   C 1  96  ? 24.681  -20.851  26.375   1.00 56.54  ? 96  LYS   C O      1 
ATOM   7492  C  CB     . LYS   C 1  96  ? 27.052  -22.713  26.917   1.00 53.24  ? 96  LYS   C CB     1 
ATOM   7493  C  CG     . LYS   C 1  96  ? 27.524  -24.011  27.591   1.00 61.12  ? 96  LYS   C CG     1 
ATOM   7494  C  CD     . LYS   C 1  96  ? 26.972  -24.150  28.999   1.00 67.24  ? 96  LYS   C CD     1 
ATOM   7495  C  CE     . LYS   C 1  96  ? 27.641  -25.291  29.737   1.00 75.79  ? 96  LYS   C CE     1 
ATOM   7496  N  NZ     . LYS   C 1  96  ? 26.656  -26.121  30.494   1.00 79.62  ? 96  LYS   C NZ     1 
ATOM   7497  N  N      . GLU   C 1  97  ? 25.789  -20.936  24.419   1.00 47.46  ? 97  GLU   C N      1 
ATOM   7498  C  CA     . GLU   C 1  97  ? 25.544  -19.572  23.979   1.00 49.85  ? 97  GLU   C CA     1 
ATOM   7499  C  C      . GLU   C 1  97  ? 25.130  -19.694  22.525   1.00 51.62  ? 97  GLU   C C      1 
ATOM   7500  O  O      . GLU   C 1  97  ? 25.858  -20.300  21.732   1.00 54.06  ? 97  GLU   C O      1 
ATOM   7501  C  CB     . GLU   C 1  97  ? 26.818  -18.727  24.102   1.00 45.99  ? 97  GLU   C CB     1 
ATOM   7502  C  CG     . GLU   C 1  97  ? 26.629  -17.259  24.187   1.00 48.54  ? 97  GLU   C CG     1 
ATOM   7503  C  CD     . GLU   C 1  97  ? 27.892  -16.560  24.638   1.00 63.51  ? 97  GLU   C CD     1 
ATOM   7504  O  OE1    . GLU   C 1  97  ? 28.899  -17.267  24.866   1.00 67.50  ? 97  GLU   C OE1    1 
ATOM   7505  O  OE2    . GLU   C 1  97  ? 27.885  -15.311  24.783   1.00 71.78  ? 97  GLU   C OE2    1 
ATOM   7506  N  N      . ASP   C 1  98  ? 23.979  -19.159  22.156   1.00 44.54  ? 98  ASP   C N      1 
ATOM   7507  C  CA     . ASP   C 1  98  ? 23.572  -19.376  20.779   1.00 42.18  ? 98  ASP   C CA     1 
ATOM   7508  C  C      . ASP   C 1  98  ? 24.278  -18.341  19.889   1.00 44.83  ? 98  ASP   C C      1 
ATOM   7509  O  O      . ASP   C 1  98  ? 25.270  -17.713  20.288   1.00 43.70  ? 98  ASP   C O      1 
ATOM   7510  C  CB     . ASP   C 1  98  ? 22.053  -19.413  20.684   1.00 35.04  ? 98  ASP   C CB     1 
ATOM   7511  C  CG     . ASP   C 1  98  ? 21.404  -18.074  20.920   1.00 35.86  ? 98  ASP   C CG     1 
ATOM   7512  O  OD1    . ASP   C 1  98  ? 22.087  -17.021  20.899   1.00 39.87  ? 98  ASP   C OD1    1 
ATOM   7513  O  OD2    . ASP   C 1  98  ? 20.159  -18.096  21.083   1.00 40.71  ? 98  ASP   C OD2    1 
ATOM   7514  N  N      . ALA   C 1  99  ? 23.833  -18.206  18.641   1.00 33.62  ? 99  ALA   C N      1 
ATOM   7515  C  CA     . ALA   C 1  99  ? 24.551  -17.347  17.715   1.00 39.75  ? 99  ALA   C CA     1 
ATOM   7516  C  C      . ALA   C 1  99  ? 24.084  -15.901  17.779   1.00 43.07  ? 99  ALA   C C      1 
ATOM   7517  O  O      . ALA   C 1  99  ? 24.612  -15.066  17.030   1.00 37.14  ? 99  ALA   C O      1 
ATOM   7518  C  CB     . ALA   C 1  99  ? 24.417  -17.877  16.295   1.00 34.98  ? 99  ALA   C CB     1 
ATOM   7519  N  N      . ALA   C 1  100 ? 23.112  -15.605  18.657   1.00 37.32  ? 100 ALA   C N      1 
ATOM   7520  C  CA     . ALA   C 1  100 ? 22.487  -14.286  18.780   1.00 42.50  ? 100 ALA   C CA     1 
ATOM   7521  C  C      . ALA   C 1  100 ? 22.097  -13.701  17.412   1.00 44.56  ? 100 ALA   C C      1 
ATOM   7522  O  O      . ALA   C 1  100 ? 22.355  -12.533  17.103   1.00 36.91  ? 100 ALA   C O      1 
ATOM   7523  C  CB     . ALA   C 1  100 ? 23.390  -13.321  19.551   1.00 41.48  ? 100 ALA   C CB     1 
ATOM   7524  N  N      . ASN   C 1  101 ? 21.435  -14.516  16.592   1.00 34.16  ? 101 ASN   C N      1 
ATOM   7525  C  CA     . ASN   C 1  101 ? 20.949  -14.064  15.294   1.00 37.87  ? 101 ASN   C CA     1 
ATOM   7526  C  C      . ASN   C 1  101 ? 22.060  -13.622  14.350   1.00 38.58  ? 101 ASN   C C      1 
ATOM   7527  O  O      . ASN   C 1  101 ? 21.784  -12.875  13.413   1.00 36.66  ? 101 ASN   C O      1 
ATOM   7528  C  CB     . ASN   C 1  101 ? 19.971  -12.895  15.414   1.00 36.49  ? 101 ASN   C CB     1 
ATOM   7529  C  CG     . ASN   C 1  101 ? 18.796  -13.186  16.299   1.00 37.64  ? 101 ASN   C CG     1 
ATOM   7530  O  OD1    . ASN   C 1  101 ? 18.125  -12.255  16.748   1.00 44.05  ? 101 ASN   C OD1    1 
ATOM   7531  N  ND2    . ASN   C 1  101 ? 18.543  -14.458  16.577   1.00 35.23  ? 101 ASN   C ND2    1 
ATOM   7532  N  N      . ASN   C 1  102 ? 23.312  -14.028  14.573   1.00 38.79  ? 102 ASN   C N      1 
ATOM   7533  C  CA     . ASN   C 1  102 ? 24.450  -13.487  13.835   1.00 38.83  ? 102 ASN   C CA     1 
ATOM   7534  C  C      . ASN   C 1  102 ? 25.129  -14.580  13.013   1.00 38.42  ? 102 ASN   C C      1 
ATOM   7535  O  O      . ASN   C 1  102 ? 25.606  -15.577  13.566   1.00 36.20  ? 102 ASN   C O      1 
ATOM   7536  C  CB     . ASN   C 1  102 ? 25.447  -12.832  14.790   1.00 36.97  ? 102 ASN   C CB     1 
ATOM   7537  C  CG     . ASN   C 1  102 ? 26.512  -12.015  14.059   1.00 43.15  ? 102 ASN   C CG     1 
ATOM   7538  O  OD1    . ASN   C 1  102 ? 26.702  -12.141  12.842   1.00 41.69  ? 102 ASN   C OD1    1 
ATOM   7539  N  ND2    . ASN   C 1  102 ? 27.210  -11.167  14.806   1.00 44.48  ? 102 ASN   C ND2    1 
ATOM   7540  N  N      . TYR   C 1  103 ? 25.188  -14.387  11.691   1.00 39.44  ? 103 TYR   C N      1 
ATOM   7541  C  CA     . TYR   C 1  103 ? 25.763  -15.428  10.845   1.00 39.03  ? 103 TYR   C CA     1 
ATOM   7542  C  C      . TYR   C 1  103 ? 27.207  -15.672  11.224   1.00 42.13  ? 103 TYR   C C      1 
ATOM   7543  O  O      . TYR   C 1  103 ? 27.657  -16.824  11.267   1.00 41.13  ? 103 TYR   C O      1 
ATOM   7544  C  CB     . TYR   C 1  103 ? 25.646  -15.056  9.373    1.00 37.77  ? 103 TYR   C CB     1 
ATOM   7545  C  CG     . TYR   C 1  103 ? 26.446  -15.946  8.420    1.00 44.93  ? 103 TYR   C CG     1 
ATOM   7546  C  CD1    . TYR   C 1  103 ? 27.789  -15.668  8.123    1.00 35.74  ? 103 TYR   C CD1    1 
ATOM   7547  C  CD2    . TYR   C 1  103 ? 25.846  -17.056  7.797    1.00 41.72  ? 103 TYR   C CD2    1 
ATOM   7548  C  CE1    . TYR   C 1  103 ? 28.494  -16.459  7.270    1.00 35.69  ? 103 TYR   C CE1    1 
ATOM   7549  C  CE2    . TYR   C 1  103 ? 26.559  -17.864  6.921    1.00 36.87  ? 103 TYR   C CE2    1 
ATOM   7550  C  CZ     . TYR   C 1  103 ? 27.880  -17.564  6.651    1.00 39.69  ? 103 TYR   C CZ     1 
ATOM   7551  O  OH     . TYR   C 1  103 ? 28.599  -18.369  5.773    1.00 34.66  ? 103 TYR   C OH     1 
ATOM   7552  N  N      . ALA   C 1  104 ? 27.936  -14.598  11.551   1.00 41.54  ? 104 ALA   C N      1 
ATOM   7553  C  CA     . ALA   C 1  104 ? 29.345  -14.731  11.891   1.00 36.54  ? 104 ALA   C CA     1 
ATOM   7554  C  C      . ALA   C 1  104 ? 29.531  -15.598  13.124   1.00 37.85  ? 104 ALA   C C      1 
ATOM   7555  O  O      . ALA   C 1  104 ? 30.415  -16.455  13.164   1.00 43.02  ? 104 ALA   C O      1 
ATOM   7556  C  CB     . ALA   C 1  104 ? 29.962  -13.355  12.106   1.00 38.45  ? 104 ALA   C CB     1 
ATOM   7557  N  N      . ARG   C 1  105 ? 28.715  -15.385  14.150   1.00 38.37  ? 105 ARG   C N      1 
ATOM   7558  C  CA     . ARG   C 1  105 ? 28.868  -16.179  15.362   1.00 38.19  ? 105 ARG   C CA     1 
ATOM   7559  C  C      . ARG   C 1  105 ? 28.532  -17.635  15.095   1.00 40.88  ? 105 ARG   C C      1 
ATOM   7560  O  O      . ARG   C 1  105 ? 29.196  -18.532  15.623   1.00 43.14  ? 105 ARG   C O      1 
ATOM   7561  C  CB     . ARG   C 1  105 ? 27.996  -15.608  16.489   1.00 40.75  ? 105 ARG   C CB     1 
ATOM   7562  C  CG     . ARG   C 1  105 ? 28.382  -14.186  16.916   1.00 41.01  ? 105 ARG   C CG     1 
ATOM   7563  C  CD     . ARG   C 1  105 ? 27.461  -13.628  18.003   1.00 50.14  ? 105 ARG   C CD     1 
ATOM   7564  N  NE     . ARG   C 1  105 ? 27.615  -14.316  19.285   1.00 53.92  ? 105 ARG   C NE     1 
ATOM   7565  C  CZ     . ARG   C 1  105 ? 28.573  -14.050  20.165   1.00 49.69  ? 105 ARG   C CZ     1 
ATOM   7566  N  NH1    . ARG   C 1  105 ? 29.462  -13.092  19.949   1.00 43.46  ? 105 ARG   C NH1    1 
ATOM   7567  N  NH2    . ARG   C 1  105 ? 28.647  -14.768  21.283   1.00 47.00  ? 105 ARG   C NH2    1 
ATOM   7568  N  N      . GLY   C 1  106 ? 27.509  -17.885  14.264   1.00 42.12  ? 106 GLY   C N      1 
ATOM   7569  C  CA     . GLY   C 1  106 ? 27.157  -19.252  13.922   1.00 36.43  ? 106 GLY   C CA     1 
ATOM   7570  C  C      . GLY   C 1  106 ? 28.231  -19.933  13.098   1.00 39.78  ? 106 GLY   C C      1 
ATOM   7571  O  O      . GLY   C 1  106 ? 28.559  -21.101  13.331   1.00 43.64  ? 106 GLY   C O      1 
ATOM   7572  N  N      . HIS   C 1  107 ? 28.815  -19.210  12.147   1.00 33.95  ? 107 HIS   C N      1 
ATOM   7573  C  CA     . HIS   C 1  107 ? 29.832  -19.812  11.292   1.00 40.09  ? 107 HIS   C CA     1 
ATOM   7574  C  C      . HIS   C 1  107 ? 31.202  -19.870  11.973   1.00 46.31  ? 107 HIS   C C      1 
ATOM   7575  O  O      . HIS   C 1  107 ? 31.873  -20.907  11.950   1.00 45.54  ? 107 HIS   C O      1 
ATOM   7576  C  CB     . HIS   C 1  107 ? 29.917  -19.047  9.976    1.00 38.79  ? 107 HIS   C CB     1 
ATOM   7577  C  CG     . HIS   C 1  107 ? 30.750  -19.730  8.942    1.00 44.69  ? 107 HIS   C CG     1 
ATOM   7578  N  ND1    . HIS   C 1  107 ? 32.126  -19.718  8.972    1.00 43.42  ? 107 HIS   C ND1    1 
ATOM   7579  C  CD2    . HIS   C 1  107 ? 30.402  -20.467  7.861    1.00 42.82  ? 107 HIS   C CD2    1 
ATOM   7580  C  CE1    . HIS   C 1  107 ? 32.591  -20.403  7.941    1.00 49.79  ? 107 HIS   C CE1    1 
ATOM   7581  N  NE2    . HIS   C 1  107 ? 31.564  -20.861  7.247    1.00 50.44  ? 107 HIS   C NE2    1 
ATOM   7582  N  N      . TYR   C 1  108 ? 31.635  -18.773  12.589   1.00 48.90  ? 108 TYR   C N      1 
ATOM   7583  C  CA     . TYR   C 1  108 ? 32.991  -18.680  13.120   1.00 44.68  ? 108 TYR   C CA     1 
ATOM   7584  C  C      . TYR   C 1  108 ? 33.046  -18.754  14.644   1.00 45.49  ? 108 TYR   C C      1 
ATOM   7585  O  O      . TYR   C 1  108 ? 33.463  -19.779  15.182   1.00 46.69  ? 108 TYR   C O      1 
ATOM   7586  C  CB     . TYR   C 1  108 ? 33.646  -17.387  12.643   1.00 44.87  ? 108 TYR   C CB     1 
ATOM   7587  C  CG     . TYR   C 1  108 ? 33.675  -17.198  11.128   1.00 54.64  ? 108 TYR   C CG     1 
ATOM   7588  C  CD1    . TYR   C 1  108 ? 32.595  -16.628  10.451   1.00 46.92  ? 108 TYR   C CD1    1 
ATOM   7589  C  CD2    . TYR   C 1  108 ? 34.815  -17.558  10.377   1.00 52.28  ? 108 TYR   C CD2    1 
ATOM   7590  C  CE1    . TYR   C 1  108 ? 32.644  -16.438  9.067    1.00 49.26  ? 108 TYR   C CE1    1 
ATOM   7591  C  CE2    . TYR   C 1  108 ? 34.874  -17.372  9.015    1.00 47.04  ? 108 TYR   C CE2    1 
ATOM   7592  C  CZ     . TYR   C 1  108 ? 33.787  -16.815  8.357    1.00 53.78  ? 108 TYR   C CZ     1 
ATOM   7593  O  OH     . TYR   C 1  108 ? 33.860  -16.625  6.990    1.00 53.48  ? 108 TYR   C OH     1 
ATOM   7594  N  N      . THR   C 1  109 ? 32.632  -17.685  15.343   1.00 44.58  ? 109 THR   C N      1 
ATOM   7595  C  CA     . THR   C 1  109 ? 32.913  -17.489  16.763   1.00 36.86  ? 109 THR   C CA     1 
ATOM   7596  C  C      . THR   C 1  109 ? 32.357  -18.593  17.637   1.00 40.54  ? 109 THR   C C      1 
ATOM   7597  O  O      . THR   C 1  109 ? 33.114  -19.326  18.272   1.00 51.77  ? 109 THR   C O      1 
ATOM   7598  C  CB     . THR   C 1  109 ? 32.354  -16.159  17.240   1.00 42.98  ? 109 THR   C CB     1 
ATOM   7599  O  OG1    . THR   C 1  109 ? 32.940  -15.117  16.467   1.00 50.37  ? 109 THR   C OG1    1 
ATOM   7600  C  CG2    . THR   C 1  109 ? 32.690  -15.930  18.702   1.00 39.85  ? 109 THR   C CG2    1 
ATOM   7601  N  N      . ILE   C 1  110 ? 31.041  -18.728  17.696   1.00 39.26  ? 110 ILE   C N      1 
ATOM   7602  C  CA     . ILE   C 1  110 ? 30.487  -19.783  18.539   1.00 47.04  ? 110 ILE   C CA     1 
ATOM   7603  C  C      . ILE   C 1  110 ? 30.537  -21.152  17.851   1.00 50.36  ? 110 ILE   C C      1 
ATOM   7604  O  O      . ILE   C 1  110 ? 30.723  -22.182  18.518   1.00 50.53  ? 110 ILE   C O      1 
ATOM   7605  C  CB     . ILE   C 1  110 ? 29.057  -19.419  18.967   1.00 41.24  ? 110 ILE   C CB     1 
ATOM   7606  C  CG1    . ILE   C 1  110 ? 29.054  -18.027  19.610   1.00 46.56  ? 110 ILE   C CG1    1 
ATOM   7607  C  CG2    . ILE   C 1  110 ? 28.473  -20.494  19.826   1.00 41.35  ? 110 ILE   C CG2    1 
ATOM   7608  C  CD1    . ILE   C 1  110 ? 29.649  -17.976  21.001   1.00 46.77  ? 110 ILE   C CD1    1 
ATOM   7609  N  N      . GLY   C 1  111 ? 30.390  -21.194  16.527   1.00 45.07  ? 111 GLY   C N      1 
ATOM   7610  C  CA     . GLY   C 1  111 ? 30.290  -22.478  15.853   1.00 49.59  ? 111 GLY   C CA     1 
ATOM   7611  C  C      . GLY   C 1  111 ? 31.603  -23.240  15.799   1.00 49.96  ? 111 GLY   C C      1 
ATOM   7612  O  O      . GLY   C 1  111 ? 31.617  -24.472  15.910   1.00 43.05  ? 111 GLY   C O      1 
ATOM   7613  N  N      . LYS   C 1  112 ? 32.724  -22.524  15.616   1.00 48.37  ? 112 LYS   C N      1 
ATOM   7614  C  CA     . LYS   C 1  112 ? 34.014  -23.204  15.531   1.00 46.24  ? 112 LYS   C CA     1 
ATOM   7615  C  C      . LYS   C 1  112 ? 34.315  -24.018  16.781   1.00 43.72  ? 112 LYS   C C      1 
ATOM   7616  O  O      . LYS   C 1  112 ? 35.187  -24.887  16.740   1.00 45.08  ? 112 LYS   C O      1 
ATOM   7617  C  CB     . LYS   C 1  112 ? 35.150  -22.204  15.279   1.00 50.07  ? 112 LYS   C CB     1 
ATOM   7618  C  CG     . LYS   C 1  112 ? 35.494  -21.306  16.451   1.00 50.63  ? 112 LYS   C CG     1 
ATOM   7619  C  CD     . LYS   C 1  112 ? 36.605  -20.316  16.098   1.00 50.07  ? 112 LYS   C CD     1 
ATOM   7620  C  CE     . LYS   C 1  112 ? 36.721  -19.225  17.173   1.00 55.75  ? 112 LYS   C CE     1 
ATOM   7621  N  NZ     . LYS   C 1  112 ? 36.702  -19.754  18.579   1.00 49.63  ? 112 LYS   C NZ     1 
ATOM   7622  N  N      . GLU   C 1  113 ? 33.606  -23.773  17.881   1.00 46.84  ? 113 GLU   C N      1 
ATOM   7623  C  CA     . GLU   C 1  113 ? 33.855  -24.490  19.121   1.00 41.74  ? 113 GLU   C CA     1 
ATOM   7624  C  C      . GLU   C 1  113 ? 33.132  -25.828  19.206   1.00 43.81  ? 113 GLU   C C      1 
ATOM   7625  O  O      . GLU   C 1  113 ? 33.427  -26.602  20.118   1.00 45.87  ? 113 GLU   C O      1 
ATOM   7626  C  CB     . GLU   C 1  113 ? 33.462  -23.620  20.332   1.00 47.13  ? 113 GLU   C CB     1 
ATOM   7627  C  CG     . GLU   C 1  113 ? 34.309  -22.359  20.555   1.00 50.74  ? 113 GLU   C CG     1 
ATOM   7628  C  CD     . GLU   C 1  113 ? 35.825  -22.638  20.678   1.00 60.03  ? 113 GLU   C CD     1 
ATOM   7629  O  OE1    . GLU   C 1  113 ? 36.215  -23.525  21.482   1.00 60.07  ? 113 GLU   C OE1    1 
ATOM   7630  O  OE2    . GLU   C 1  113 ? 36.624  -21.972  19.963   1.00 54.69  ? 113 GLU   C OE2    1 
ATOM   7631  N  N      . ILE   C 1  114 ? 32.196  -26.132  18.301   1.00 43.16  ? 114 ILE   C N      1 
ATOM   7632  C  CA     . ILE   C 1  114 ? 31.408  -27.359  18.421   1.00 34.07  ? 114 ILE   C CA     1 
ATOM   7633  C  C      . ILE   C 1  114 ? 31.433  -28.184  17.124   1.00 33.57  ? 114 ILE   C C      1 
ATOM   7634  O  O      . ILE   C 1  114 ? 30.989  -29.334  17.103   1.00 34.03  ? 114 ILE   C O      1 
ATOM   7635  C  CB     . ILE   C 1  114 ? 29.968  -27.008  18.845   1.00 36.37  ? 114 ILE   C CB     1 
ATOM   7636  C  CG1    . ILE   C 1  114 ? 29.242  -28.215  19.431   1.00 38.64  ? 114 ILE   C CG1    1 
ATOM   7637  C  CG2    . ILE   C 1  114 ? 29.184  -26.442  17.672   1.00 34.44  ? 114 ILE   C CG2    1 
ATOM   7638  C  CD1    . ILE   C 1  114 ? 27.891  -27.877  20.047   1.00 39.99  ? 114 ILE   C CD1    1 
ATOM   7639  N  N      . ILE   C 1  115 ? 32.009  -27.635  16.050   1.00 33.95  ? 115 ILE   C N      1 
ATOM   7640  C  CA     . ILE   C 1  115 ? 31.950  -28.288  14.738   1.00 35.37  ? 115 ILE   C CA     1 
ATOM   7641  C  C      . ILE   C 1  115 ? 32.643  -29.644  14.744   1.00 35.04  ? 115 ILE   C C      1 
ATOM   7642  O  O      . ILE   C 1  115 ? 32.161  -30.595  14.121   1.00 40.98  ? 115 ILE   C O      1 
ATOM   7643  C  CB     . ILE   C 1  115 ? 32.545  -27.394  13.639   1.00 36.73  ? 115 ILE   C CB     1 
ATOM   7644  C  CG1    . ILE   C 1  115 ? 32.326  -28.041  12.276   1.00 33.90  ? 115 ILE   C CG1    1 
ATOM   7645  C  CG2    . ILE   C 1  115 ? 34.025  -27.233  13.847   1.00 37.54  ? 115 ILE   C CG2    1 
ATOM   7646  C  CD1    . ILE   C 1  115 ? 30.929  -27.870  11.738   1.00 33.83  ? 115 ILE   C CD1    1 
ATOM   7647  N  N      . ASP   C 1  116 ? 33.810  -29.754  15.376   1.00 40.69  ? 116 ASP   C N      1 
ATOM   7648  C  CA     . ASP   C 1  116 ? 34.462  -31.062  15.382   1.00 40.29  ? 116 ASP   C CA     1 
ATOM   7649  C  C      . ASP   C 1  116 ? 33.585  -32.069  16.104   1.00 37.62  ? 116 ASP   C C      1 
ATOM   7650  O  O      . ASP   C 1  116 ? 33.392  -33.192  15.634   1.00 38.25  ? 116 ASP   C O      1 
ATOM   7651  C  CB     . ASP   C 1  116 ? 35.847  -31.002  16.021   1.00 29.15  ? 116 ASP   C CB     1 
ATOM   7652  C  CG     . ASP   C 1  116 ? 36.825  -30.119  15.259   1.00 37.68  ? 116 ASP   C CG     1 
ATOM   7653  O  OD1    . ASP   C 1  116 ? 36.656  -29.882  14.045   1.00 34.05  ? 116 ASP   C OD1    1 
ATOM   7654  O  OD2    . ASP   C 1  116 ? 37.784  -29.621  15.906   1.00 54.61  ? 116 ASP   C OD2    1 
ATOM   7655  N  N      . LEU   C 1  117 ? 33.005  -31.665  17.225   1.00 35.07  ? 117 LEU   C N      1 
ATOM   7656  C  CA     . LEU   C 1  117 ? 32.171  -32.593  17.963   1.00 39.29  ? 117 LEU   C CA     1 
ATOM   7657  C  C      . LEU   C 1  117 ? 30.947  -32.998  17.148   1.00 48.39  ? 117 LEU   C C      1 
ATOM   7658  O  O      . LEU   C 1  117 ? 30.524  -34.165  17.186   1.00 50.29  ? 117 LEU   C O      1 
ATOM   7659  C  CB     . LEU   C 1  117 ? 31.756  -31.978  19.291   1.00 40.94  ? 117 LEU   C CB     1 
ATOM   7660  C  CG     . LEU   C 1  117 ? 30.770  -32.920  19.956   1.00 46.04  ? 117 LEU   C CG     1 
ATOM   7661  C  CD1    . LEU   C 1  117 ? 31.491  -34.196  20.376   1.00 48.23  ? 117 LEU   C CD1    1 
ATOM   7662  C  CD2    . LEU   C 1  117 ? 30.069  -32.247  21.102   1.00 42.27  ? 117 LEU   C CD2    1 
ATOM   7663  N  N      . VAL   C 1  118 ? 30.353  -32.051  16.408   1.00 44.86  ? 118 VAL   C N      1 
ATOM   7664  C  CA     . VAL   C 1  118 ? 29.202  -32.401  15.580   1.00 45.57  ? 118 VAL   C CA     1 
ATOM   7665  C  C      . VAL   C 1  118 ? 29.630  -33.341  14.459   1.00 40.65  ? 118 VAL   C C      1 
ATOM   7666  O  O      . VAL   C 1  118 ? 28.990  -34.372  14.227   1.00 39.84  ? 118 VAL   C O      1 
ATOM   7667  C  CB     . VAL   C 1  118 ? 28.488  -31.146  15.036   1.00 46.95  ? 118 VAL   C CB     1 
ATOM   7668  C  CG1    . VAL   C 1  118 ? 27.511  -31.538  13.922   1.00 43.53  ? 118 VAL   C CG1    1 
ATOM   7669  C  CG2    . VAL   C 1  118 ? 27.738  -30.424  16.139   1.00 41.01  ? 118 VAL   C CG2    1 
ATOM   7670  N  N      . LEU   C 1  119 ? 30.728  -33.024  13.765   1.00 38.23  ? 119 LEU   C N      1 
ATOM   7671  C  CA     . LEU   C 1  119 ? 31.185  -33.927  12.701   1.00 39.85  ? 119 LEU   C CA     1 
ATOM   7672  C  C      . LEU   C 1  119 ? 31.468  -35.324  13.241   1.00 38.13  ? 119 LEU   C C      1 
ATOM   7673  O  O      . LEU   C 1  119 ? 31.098  -36.320  12.618   1.00 41.13  ? 119 LEU   C O      1 
ATOM   7674  C  CB     . LEU   C 1  119 ? 32.417  -33.372  11.993   1.00 28.38  ? 119 LEU   C CB     1 
ATOM   7675  C  CG     . LEU   C 1  119 ? 32.126  -32.256  11.002   1.00 34.65  ? 119 LEU   C CG     1 
ATOM   7676  C  CD1    . LEU   C 1  119 ? 33.425  -31.739  10.419   1.00 43.89  ? 119 LEU   C CD1    1 
ATOM   7677  C  CD2    . LEU   C 1  119 ? 31.209  -32.736  9.909    1.00 31.52  ? 119 LEU   C CD2    1 
ATOM   7678  N  N      . ASP   C 1  120 ? 32.102  -35.415  14.411   1.00 46.26  ? 120 ASP   C N      1 
ATOM   7679  C  CA     . ASP   C 1  120 ? 32.392  -36.708  15.021   1.00 39.76  ? 120 ASP   C CA     1 
ATOM   7680  C  C      . ASP   C 1  120 ? 31.116  -37.502  15.221   1.00 45.99  ? 120 ASP   C C      1 
ATOM   7681  O  O      . ASP   C 1  120 ? 31.018  -38.668  14.814   1.00 42.77  ? 120 ASP   C O      1 
ATOM   7682  C  CB     . ASP   C 1  120 ? 33.092  -36.502  16.365   1.00 41.50  ? 120 ASP   C CB     1 
ATOM   7683  C  CG     . ASP   C 1  120 ? 34.543  -36.039  16.209   1.00 61.13  ? 120 ASP   C CG     1 
ATOM   7684  O  OD1    . ASP   C 1  120 ? 34.992  -35.832  15.040   1.00 58.36  ? 120 ASP   C OD1    1 
ATOM   7685  O  OD2    . ASP   C 1  120 ? 35.225  -35.858  17.262   1.00 64.09  ? 120 ASP   C OD2    1 
ATOM   7686  N  N      . ARG   C 1  121 ? 30.129  -36.888  15.875   1.00 43.15  ? 121 ARG   C N      1 
ATOM   7687  C  CA     . ARG   C 1  121 ? 28.866  -37.574  16.092   1.00 40.20  ? 121 ARG   C CA     1 
ATOM   7688  C  C      . ARG   C 1  121 ? 28.260  -38.033  14.779   1.00 44.02  ? 121 ARG   C C      1 
ATOM   7689  O  O      . ARG   C 1  121 ? 27.708  -39.140  14.706   1.00 48.49  ? 121 ARG   C O      1 
ATOM   7690  C  CB     . ARG   C 1  121 ? 27.906  -36.658  16.835   1.00 49.79  ? 121 ARG   C CB     1 
ATOM   7691  C  CG     . ARG   C 1  121 ? 28.508  -36.157  18.098   1.00 51.41  ? 121 ARG   C CG     1 
ATOM   7692  C  CD     . ARG   C 1  121 ? 28.664  -37.326  19.057   1.00 55.42  ? 121 ARG   C CD     1 
ATOM   7693  N  NE     . ARG   C 1  121 ? 29.121  -36.850  20.350   1.00 57.55  ? 121 ARG   C NE     1 
ATOM   7694  C  CZ     . ARG   C 1  121 ? 28.313  -36.372  21.278   1.00 56.66  ? 121 ARG   C CZ     1 
ATOM   7695  N  NH1    . ARG   C 1  121 ? 27.000  -36.366  21.110   1.00 53.21  ? 121 ARG   C NH1    1 
ATOM   7696  N  NH2    . ARG   C 1  121 ? 28.833  -35.886  22.400   1.00 68.07  ? 121 ARG   C NH2    1 
ATOM   7697  N  N      . ILE   C 1  122 ? 28.350  -37.202  13.726   1.00 39.19  ? 122 ILE   C N      1 
ATOM   7698  C  CA     . ILE   C 1  122 ? 27.840  -37.622  12.420   1.00 39.84  ? 122 ILE   C CA     1 
ATOM   7699  C  C      . ILE   C 1  122 ? 28.600  -38.841  11.925   1.00 36.96  ? 122 ILE   C C      1 
ATOM   7700  O  O      . ILE   C 1  122 ? 28.000  -39.794  11.419   1.00 37.25  ? 122 ILE   C O      1 
ATOM   7701  C  CB     . ILE   C 1  122 ? 27.890  -36.475  11.393   1.00 36.36  ? 122 ILE   C CB     1 
ATOM   7702  C  CG1    . ILE   C 1  122 ? 26.870  -35.379  11.744   1.00 31.70  ? 122 ILE   C CG1    1 
ATOM   7703  C  CG2    . ILE   C 1  122 ? 27.611  -37.029  10.010   1.00 27.58  ? 122 ILE   C CG2    1 
ATOM   7704  C  CD1    . ILE   C 1  122 ? 27.026  -34.132  10.927   1.00 27.38  ? 122 ILE   C CD1    1 
ATOM   7705  N  N      . ARG   C 1  123 ? 29.926  -38.843  12.077   1.00 36.87  ? 123 ARG   C N      1 
ATOM   7706  C  CA     . ARG   C 1  123 ? 30.700  -39.998  11.637   1.00 38.95  ? 123 ARG   C CA     1 
ATOM   7707  C  C      . ARG   C 1  123 ? 30.235  -41.286  12.321   1.00 44.84  ? 123 ARG   C C      1 
ATOM   7708  O  O      . ARG   C 1  123 ? 30.184  -42.343  11.683   1.00 42.17  ? 123 ARG   C O      1 
ATOM   7709  C  CB     . ARG   C 1  123 ? 32.185  -39.763  11.872   1.00 38.12  ? 123 ARG   C CB     1 
ATOM   7710  C  CG     . ARG   C 1  123 ? 33.052  -40.900  11.373   1.00 42.28  ? 123 ARG   C CG     1 
ATOM   7711  C  CD     . ARG   C 1  123 ? 33.029  -40.983  9.853    1.00 47.50  ? 123 ARG   C CD     1 
ATOM   7712  N  NE     . ARG   C 1  123 ? 33.667  -39.813  9.264    1.00 46.24  ? 123 ARG   C NE     1 
ATOM   7713  C  CZ     . ARG   C 1  123 ? 33.905  -39.639  7.971    1.00 45.03  ? 123 ARG   C CZ     1 
ATOM   7714  N  NH1    . ARG   C 1  123 ? 33.613  -40.574  7.079    1.00 38.17  ? 123 ARG   C NH1    1 
ATOM   7715  N  NH2    . ARG   C 1  123 ? 34.448  -38.492  7.565    1.00 52.60  ? 123 ARG   C NH2    1 
ATOM   7716  N  N      . LYS   C 1  124 ? 29.876  -41.225  13.614   1.00 44.22  ? 124 LYS   C N      1 
ATOM   7717  C  CA     . LYS   C 1  124 ? 29.378  -42.430  14.270   1.00 36.78  ? 124 LYS   C CA     1 
ATOM   7718  C  C      . LYS   C 1  124 ? 28.073  -42.889  13.646   1.00 44.71  ? 124 LYS   C C      1 
ATOM   7719  O  O      . LYS   C 1  124 ? 27.765  -44.084  13.668   1.00 50.85  ? 124 LYS   C O      1 
ATOM   7720  C  CB     . LYS   C 1  124 ? 29.192  -42.214  15.776   1.00 50.25  ? 124 LYS   C CB     1 
ATOM   7721  C  CG     . LYS   C 1  124 ? 30.499  -42.104  16.624   1.00 56.75  ? 124 LYS   C CG     1 
ATOM   7722  C  CD     . LYS   C 1  124 ? 31.572  -43.130  16.195   1.00 64.08  ? 124 LYS   C CD     1 
ATOM   7723  C  CE     . LYS   C 1  124 ? 33.000  -42.640  16.535   1.00 71.83  ? 124 LYS   C CE     1 
ATOM   7724  N  NZ     . LYS   C 1  124 ? 33.760  -42.217  15.272   1.00 54.22  ? 124 LYS   C NZ     1 
ATOM   7725  N  N      . LEU   C 1  125 ? 27.293  -41.968  13.069   1.00 48.00  ? 125 LEU   C N      1 
ATOM   7726  C  CA     . LEU   C 1  125 ? 26.076  -42.389  12.372   1.00 42.22  ? 125 LEU   C CA     1 
ATOM   7727  C  C      . LEU   C 1  125 ? 26.387  -42.965  10.991   1.00 45.12  ? 125 LEU   C C      1 
ATOM   7728  O  O      . LEU   C 1  125 ? 25.715  -43.901  10.534   1.00 47.33  ? 125 LEU   C O      1 
ATOM   7729  C  CB     . LEU   C 1  125 ? 25.098  -41.223  12.227   1.00 34.60  ? 125 LEU   C CB     1 
ATOM   7730  C  CG     . LEU   C 1  125 ? 24.351  -40.749  13.470   1.00 39.70  ? 125 LEU   C CG     1 
ATOM   7731  C  CD1    . LEU   C 1  125 ? 23.543  -39.473  13.213   1.00 39.55  ? 125 LEU   C CD1    1 
ATOM   7732  C  CD2    . LEU   C 1  125 ? 23.476  -41.840  14.000   1.00 40.72  ? 125 LEU   C CD2    1 
ATOM   7733  N  N      . ALA   C 1  126 ? 27.372  -42.402  10.291   1.00 43.23  ? 126 ALA   C N      1 
ATOM   7734  C  CA     . ALA   C 1  126 ? 27.674  -42.922  8.966    1.00 45.41  ? 126 ALA   C CA     1 
ATOM   7735  C  C      . ALA   C 1  126 ? 28.357  -44.278  9.055    1.00 47.61  ? 126 ALA   C C      1 
ATOM   7736  O  O      . ALA   C 1  126 ? 28.083  -45.157  8.236    1.00 55.64  ? 126 ALA   C O      1 
ATOM   7737  C  CB     . ALA   C 1  126 ? 28.534  -41.926  8.183    1.00 40.74  ? 126 ALA   C CB     1 
ATOM   7738  N  N      . ASP   C 1  127 ? 29.209  -44.480  10.059   1.00 47.60  ? 127 ASP   C N      1 
ATOM   7739  C  CA     . ASP   C 1  127 ? 29.891  -45.760  10.235   1.00 50.21  ? 127 ASP   C CA     1 
ATOM   7740  C  C      . ASP   C 1  127 ? 28.923  -46.912  10.474   1.00 53.17  ? 127 ASP   C C      1 
ATOM   7741  O  O      . ASP   C 1  127 ? 29.332  -48.070  10.351   1.00 57.92  ? 127 ASP   C O      1 
ATOM   7742  C  CB     . ASP   C 1  127 ? 30.892  -45.682  11.398   1.00 45.67  ? 127 ASP   C CB     1 
ATOM   7743  C  CG     . ASP   C 1  127 ? 32.136  -44.854  11.059   1.00 54.53  ? 127 ASP   C CG     1 
ATOM   7744  O  OD1    . ASP   C 1  127 ? 32.347  -44.534  9.859    1.00 50.29  ? 127 ASP   C OD1    1 
ATOM   7745  O  OD2    . ASP   C 1  127 ? 32.899  -44.519  12.002   1.00 52.22  ? 127 ASP   C OD2    1 
ATOM   7746  N  N      . GLN   C 1  128 ? 27.664  -46.636  10.825   1.00 49.77  ? 128 GLN   C N      1 
ATOM   7747  C  CA     . GLN   C 1  128 ? 26.664  -47.689  10.969   1.00 54.41  ? 128 GLN   C CA     1 
ATOM   7748  C  C      . GLN   C 1  128 ? 25.916  -47.963  9.678    1.00 52.49  ? 128 GLN   C C      1 
ATOM   7749  O  O      . GLN   C 1  128 ? 24.874  -48.629  9.710    1.00 53.16  ? 128 GLN   C O      1 
ATOM   7750  C  CB     . GLN   C 1  128 ? 25.636  -47.337  12.043   1.00 53.62  ? 128 GLN   C CB     1 
ATOM   7751  C  CG     . GLN   C 1  128 ? 26.197  -47.022  13.401   1.00 62.45  ? 128 GLN   C CG     1 
ATOM   7752  C  CD     . GLN   C 1  128 ? 25.088  -46.851  14.435   1.00 69.70  ? 128 GLN   C CD     1 
ATOM   7753  O  OE1    . GLN   C 1  128 ? 24.089  -46.154  14.187   1.00 61.26  ? 128 GLN   C OE1    1 
ATOM   7754  N  NE2    . GLN   C 1  128 ? 25.253  -47.504  15.600   1.00 65.64  ? 128 GLN   C NE2    1 
ATOM   7755  N  N      . CYS   C 1  129 ? 26.407  -47.445  8.557    1.00 51.55  ? 129 CYS   C N      1 
ATOM   7756  C  CA     . CYS   C 1  129 ? 25.691  -47.457  7.288    1.00 51.80  ? 129 CYS   C CA     1 
ATOM   7757  C  C      . CYS   C 1  129 ? 26.370  -48.409  6.311    1.00 50.34  ? 129 CYS   C C      1 
ATOM   7758  O  O      . CYS   C 1  129 ? 27.582  -48.314  6.084    1.00 49.85  ? 129 CYS   C O      1 
ATOM   7759  C  CB     . CYS   C 1  129 ? 25.633  -46.047  6.693    1.00 49.96  ? 129 CYS   C CB     1 
ATOM   7760  S  SG     . CYS   C 1  129 ? 24.396  -44.962  7.449    1.00 50.29  ? 129 CYS   C SG     1 
ATOM   7761  N  N      . THR   C 1  130 ? 25.588  -49.322  5.736    1.00 47.07  ? 130 THR   C N      1 
ATOM   7762  C  CA     . THR   C 1  130 ? 26.134  -50.216  4.726    1.00 47.63  ? 130 THR   C CA     1 
ATOM   7763  C  C      . THR   C 1  130 ? 26.187  -49.569  3.349    1.00 48.34  ? 130 THR   C C      1 
ATOM   7764  O  O      . THR   C 1  130 ? 27.028  -49.960  2.537    1.00 57.91  ? 130 THR   C O      1 
ATOM   7765  C  CB     . THR   C 1  130 ? 25.340  -51.531  4.674    1.00 48.35  ? 130 THR   C CB     1 
ATOM   7766  O  OG1    . THR   C 1  130 ? 23.972  -51.282  4.355    1.00 55.03  ? 130 THR   C OG1    1 
ATOM   7767  C  CG2    . THR   C 1  130 ? 25.378  -52.216  6.010    1.00 48.79  ? 130 THR   C CG2    1 
ATOM   7768  N  N      . GLY   C 1  131 ? 25.347  -48.568  3.078    1.00 48.95  ? 131 GLY   C N      1 
ATOM   7769  C  CA     . GLY   C 1  131 ? 25.401  -47.852  1.814    1.00 42.98  ? 131 GLY   C CA     1 
ATOM   7770  C  C      . GLY   C 1  131 ? 24.878  -46.431  1.884    1.00 44.30  ? 131 GLY   C C      1 
ATOM   7771  O  O      . GLY   C 1  131 ? 23.910  -46.085  1.202    1.00 48.49  ? 131 GLY   C O      1 
ATOM   7772  N  N      . LEU   C 1  132 ? 25.520  -45.593  2.693    1.00 41.67  ? 132 LEU   C N      1 
ATOM   7773  C  CA     . LEU   C 1  132 ? 25.038  -44.239  2.931    1.00 37.81  ? 132 LEU   C CA     1 
ATOM   7774  C  C      . LEU   C 1  132 ? 24.756  -43.489  1.633    1.00 39.51  ? 132 LEU   C C      1 
ATOM   7775  O  O      . LEU   C 1  132 ? 25.622  -43.355  0.767    1.00 36.54  ? 132 LEU   C O      1 
ATOM   7776  C  CB     . LEU   C 1  132 ? 26.044  -43.470  3.780    1.00 32.56  ? 132 LEU   C CB     1 
ATOM   7777  C  CG     . LEU   C 1  132 ? 25.647  -42.018  4.009    1.00 36.58  ? 132 LEU   C CG     1 
ATOM   7778  C  CD1    . LEU   C 1  132 ? 24.261  -41.949  4.617    1.00 35.22  ? 132 LEU   C CD1    1 
ATOM   7779  C  CD2    . LEU   C 1  132 ? 26.652  -41.308  4.876    1.00 28.02  ? 132 LEU   C CD2    1 
ATOM   7780  N  N      . GLN   C 1  133 ? 23.526  -42.999  1.515    1.00 44.92  ? 133 GLN   C N      1 
ATOM   7781  C  CA     . GLN   C 1  133 ? 23.077  -42.254  0.344    1.00 44.69  ? 133 GLN   C CA     1 
ATOM   7782  C  C      . GLN   C 1  133 ? 23.410  -40.773  0.466    1.00 41.29  ? 133 GLN   C C      1 
ATOM   7783  O  O      . GLN   C 1  133 ? 23.984  -40.189  -0.453   1.00 42.07  ? 133 GLN   C O      1 
ATOM   7784  C  CB     . GLN   C 1  133 ? 21.565  -42.443  0.144    1.00 44.18  ? 133 GLN   C CB     1 
ATOM   7785  C  CG     . GLN   C 1  133 ? 21.113  -42.391  -1.315   1.00 52.81  ? 133 GLN   C CG     1 
ATOM   7786  C  CD     . GLN   C 1  133 ? 19.666  -42.809  -1.459   1.00 62.91  ? 133 GLN   C CD     1 
ATOM   7787  O  OE1    . GLN   C 1  133 ? 18.936  -42.881  -0.460   1.00 59.41  ? 133 GLN   C OE1    1 
ATOM   7788  N  NE2    . GLN   C 1  133 ? 19.238  -43.102  -2.694   1.00 67.32  ? 133 GLN   C NE2    1 
ATOM   7789  N  N      . GLY   C 1  134 ? 23.061  -40.144  1.582    1.00 36.31  ? 134 GLY   C N      1 
ATOM   7790  C  CA     . GLY   C 1  134 ? 23.277  -38.720  1.676    1.00 39.69  ? 134 GLY   C CA     1 
ATOM   7791  C  C      . GLY   C 1  134 ? 22.751  -38.179  2.982    1.00 39.15  ? 134 GLY   C C      1 
ATOM   7792  O  O      . GLY   C 1  134 ? 22.362  -38.930  3.869    1.00 39.94  ? 134 GLY   C O      1 
ATOM   7793  N  N      . PHE   C 1  135 ? 22.737  -36.853  3.075    1.00 37.13  ? 135 PHE   C N      1 
ATOM   7794  C  CA     . PHE   C 1  135 ? 22.276  -36.135  4.248    1.00 36.20  ? 135 PHE   C CA     1 
ATOM   7795  C  C      . PHE   C 1  135 ? 21.057  -35.299  3.899    1.00 34.98  ? 135 PHE   C C      1 
ATOM   7796  O  O      . PHE   C 1  135 ? 20.886  -34.872  2.754    1.00 34.12  ? 135 PHE   C O      1 
ATOM   7797  C  CB     . PHE   C 1  135 ? 23.382  -35.236  4.794    1.00 35.95  ? 135 PHE   C CB     1 
ATOM   7798  C  CG     . PHE   C 1  135 ? 24.677  -35.952  5.001    1.00 38.43  ? 135 PHE   C CG     1 
ATOM   7799  C  CD1    . PHE   C 1  135 ? 24.947  -36.602  6.192    1.00 41.58  ? 135 PHE   C CD1    1 
ATOM   7800  C  CD2    . PHE   C 1  135 ? 25.618  -36.012  3.987    1.00 39.20  ? 135 PHE   C CD2    1 
ATOM   7801  C  CE1    . PHE   C 1  135 ? 26.161  -37.285  6.367    1.00 39.17  ? 135 PHE   C CE1    1 
ATOM   7802  C  CE2    . PHE   C 1  135 ? 26.831  -36.688  4.161    1.00 37.73  ? 135 PHE   C CE2    1 
ATOM   7803  C  CZ     . PHE   C 1  135 ? 27.100  -37.316  5.341    1.00 34.55  ? 135 PHE   C CZ     1 
ATOM   7804  N  N      . LEU   C 1  136 ? 20.207  -35.079  4.902    1.00 33.05  ? 136 LEU   C N      1 
ATOM   7805  C  CA     . LEU   C 1  136 ? 19.044  -34.200  4.810    1.00 30.94  ? 136 LEU   C CA     1 
ATOM   7806  C  C      . LEU   C 1  136 ? 19.201  -33.163  5.914    1.00 32.50  ? 136 LEU   C C      1 
ATOM   7807  O  O      . LEU   C 1  136 ? 19.101  -33.503  7.100    1.00 33.22  ? 136 LEU   C O      1 
ATOM   7808  C  CB     . LEU   C 1  136 ? 17.737  -34.988  4.965    1.00 30.13  ? 136 LEU   C CB     1 
ATOM   7809  C  CG     . LEU   C 1  136 ? 17.390  -36.008  3.859    1.00 34.91  ? 136 LEU   C CG     1 
ATOM   7810  C  CD1    . LEU   C 1  136 ? 18.031  -37.385  4.102    1.00 35.96  ? 136 LEU   C CD1    1 
ATOM   7811  C  CD2    . LEU   C 1  136 ? 15.891  -36.185  3.706    1.00 38.58  ? 136 LEU   C CD2    1 
ATOM   7812  N  N      . VAL   C 1  137 ? 19.438  -31.907  5.532    1.00 27.12  ? 137 VAL   C N      1 
ATOM   7813  C  CA     . VAL   C 1  137 ? 19.829  -30.846  6.464    1.00 29.97  ? 137 VAL   C CA     1 
ATOM   7814  C  C      . VAL   C 1  137 ? 18.678  -29.850  6.626    1.00 31.12  ? 137 VAL   C C      1 
ATOM   7815  O  O      . VAL   C 1  137 ? 18.288  -29.176  5.664    1.00 31.73  ? 137 VAL   C O      1 
ATOM   7816  C  CB     . VAL   C 1  137 ? 21.111  -30.145  5.983    1.00 31.28  ? 137 VAL   C CB     1 
ATOM   7817  C  CG1    . VAL   C 1  137 ? 21.644  -29.191  7.034    1.00 30.17  ? 137 VAL   C CG1    1 
ATOM   7818  C  CG2    . VAL   C 1  137 ? 22.179  -31.192  5.589    1.00 32.67  ? 137 VAL   C CG2    1 
ATOM   7819  N  N      . PHE   C 1  138 ? 18.151  -29.740  7.843    1.00 31.12  ? 138 PHE   C N      1 
ATOM   7820  C  CA     . PHE   C 1  138 ? 17.014  -28.874  8.163    1.00 30.06  ? 138 PHE   C CA     1 
ATOM   7821  C  C      . PHE   C 1  138 ? 17.496  -27.659  8.950    1.00 30.42  ? 138 PHE   C C      1 
ATOM   7822  O  O      . PHE   C 1  138 ? 18.141  -27.811  9.986    1.00 36.08  ? 138 PHE   C O      1 
ATOM   7823  C  CB     . PHE   C 1  138 ? 15.969  -29.620  9.005    1.00 30.09  ? 138 PHE   C CB     1 
ATOM   7824  C  CG     . PHE   C 1  138 ? 15.350  -30.792  8.317    1.00 30.65  ? 138 PHE   C CG     1 
ATOM   7825  C  CD1    . PHE   C 1  138 ? 16.105  -31.923  8.009    1.00 31.65  ? 138 PHE   C CD1    1 
ATOM   7826  C  CD2    . PHE   C 1  138 ? 14.005  -30.781  7.991    1.00 33.07  ? 138 PHE   C CD2    1 
ATOM   7827  C  CE1    . PHE   C 1  138 ? 15.532  -33.025  7.372    1.00 31.42  ? 138 PHE   C CE1    1 
ATOM   7828  C  CE2    . PHE   C 1  138 ? 13.420  -31.869  7.345    1.00 38.18  ? 138 PHE   C CE2    1 
ATOM   7829  C  CZ     . PHE   C 1  138 ? 14.191  -33.004  7.041    1.00 35.51  ? 138 PHE   C CZ     1 
ATOM   7830  N  N      . HIS   C 1  139 ? 17.151  -26.462  8.502    1.00 25.53  ? 139 HIS   C N      1 
ATOM   7831  C  CA     . HIS   C 1  139 ? 17.694  -25.263  9.131    1.00 25.88  ? 139 HIS   C CA     1 
ATOM   7832  C  C      . HIS   C 1  139 ? 16.912  -24.066  8.637    1.00 28.64  ? 139 HIS   C C      1 
ATOM   7833  O  O      . HIS   C 1  139 ? 16.392  -24.071  7.517    1.00 30.80  ? 139 HIS   C O      1 
ATOM   7834  C  CB     . HIS   C 1  139 ? 19.189  -25.065  8.804    1.00 31.12  ? 139 HIS   C CB     1 
ATOM   7835  C  CG     . HIS   C 1  139 ? 19.460  -24.841  7.340    1.00 30.21  ? 139 HIS   C CG     1 
ATOM   7836  N  ND1    . HIS   C 1  139 ? 19.553  -23.584  6.780    1.00 25.60  ? 139 HIS   C ND1    1 
ATOM   7837  C  CD2    . HIS   C 1  139 ? 19.614  -25.718  6.319    1.00 26.45  ? 139 HIS   C CD2    1 
ATOM   7838  C  CE1    . HIS   C 1  139 ? 19.743  -23.696  5.481    1.00 25.95  ? 139 HIS   C CE1    1 
ATOM   7839  N  NE2    . HIS   C 1  139 ? 19.780  -24.980  5.175    1.00 26.63  ? 139 HIS   C NE2    1 
ATOM   7840  N  N      . SER   C 1  140 ? 16.840  -23.041  9.472    1.00 29.30  ? 140 SER   C N      1 
ATOM   7841  C  CA     . SER   C 1  140 ? 16.299  -21.772  9.018    1.00 29.86  ? 140 SER   C CA     1 
ATOM   7842  C  C      . SER   C 1  140 ? 17.347  -21.006  8.191    1.00 29.89  ? 140 SER   C C      1 
ATOM   7843  O  O      . SER   C 1  140 ? 18.558  -21.199  8.343    1.00 28.83  ? 140 SER   C O      1 
ATOM   7844  C  CB     . SER   C 1  140 ? 15.836  -20.932  10.212   1.00 26.82  ? 140 SER   C CB     1 
ATOM   7845  O  OG     . SER   C 1  140 ? 16.941  -20.307  10.868   1.00 28.44  ? 140 SER   C OG     1 
ATOM   7846  N  N      . PHE   C 1  141 ? 16.856  -20.148  7.287    1.00 27.94  ? 141 PHE   C N      1 
ATOM   7847  C  CA     . PHE   C 1  141 ? 17.685  -19.109  6.697    1.00 26.55  ? 141 PHE   C CA     1 
ATOM   7848  C  C      . PHE   C 1  141 ? 18.005  -18.019  7.701    1.00 34.24  ? 141 PHE   C C      1 
ATOM   7849  O  O      . PHE   C 1  141 ? 19.047  -17.364  7.586    1.00 32.49  ? 141 PHE   C O      1 
ATOM   7850  C  CB     . PHE   C 1  141 ? 16.968  -18.455  5.527    1.00 28.60  ? 141 PHE   C CB     1 
ATOM   7851  C  CG     . PHE   C 1  141 ? 17.118  -19.188  4.244    1.00 36.73  ? 141 PHE   C CG     1 
ATOM   7852  C  CD1    . PHE   C 1  141 ? 17.910  -20.337  4.180    1.00 29.50  ? 141 PHE   C CD1    1 
ATOM   7853  C  CD2    . PHE   C 1  141 ? 16.457  -18.748  3.094    1.00 33.07  ? 141 PHE   C CD2    1 
ATOM   7854  C  CE1    . PHE   C 1  141 ? 18.024  -21.038  3.015    1.00 29.88  ? 141 PHE   C CE1    1 
ATOM   7855  C  CE2    . PHE   C 1  141 ? 16.582  -19.448  1.904    1.00 38.30  ? 141 PHE   C CE2    1 
ATOM   7856  C  CZ     . PHE   C 1  141 ? 17.373  -20.592  1.859    1.00 35.95  ? 141 PHE   C CZ     1 
ATOM   7857  N  N      . GLY   C 1  142 ? 17.098  -17.777  8.654    1.00 32.73  ? 142 GLY   C N      1 
ATOM   7858  C  CA     . GLY   C 1  142 ? 17.098  -16.555  9.438    1.00 31.22  ? 142 GLY   C CA     1 
ATOM   7859  C  C      . GLY   C 1  142 ? 17.971  -16.543  10.672   1.00 32.12  ? 142 GLY   C C      1 
ATOM   7860  O  O      . GLY   C 1  142 ? 18.589  -15.521  10.974   1.00 35.50  ? 142 GLY   C O      1 
ATOM   7861  N  N      . GLY   C 1  143 ? 18.013  -17.643  11.412   1.00 29.81  ? 143 GLY   C N      1 
ATOM   7862  C  CA     . GLY   C 1  143 ? 18.767  -17.661  12.637   1.00 26.79  ? 143 GLY   C CA     1 
ATOM   7863  C  C      . GLY   C 1  143 ? 20.255  -17.702  12.379   1.00 31.72  ? 143 GLY   C C      1 
ATOM   7864  O  O      . GLY   C 1  143 ? 20.724  -18.096  11.315   1.00 36.21  ? 143 GLY   C O      1 
ATOM   7865  N  N      . GLY   C 1  144 ? 21.012  -17.237  13.370   1.00 35.62  ? 144 GLY   C N      1 
ATOM   7866  C  CA     . GLY   C 1  144 ? 22.456  -17.225  13.247   1.00 33.49  ? 144 GLY   C CA     1 
ATOM   7867  C  C      . GLY   C 1  144 ? 23.067  -18.608  13.250   1.00 34.79  ? 144 GLY   C C      1 
ATOM   7868  O  O      . GLY   C 1  144 ? 24.091  -18.835  12.597   1.00 39.53  ? 144 GLY   C O      1 
ATOM   7869  N  N      . THR   C 1  145 ? 22.467  -19.550  13.979   1.00 29.01  ? 145 THR   C N      1 
ATOM   7870  C  CA     . THR   C 1  145 ? 22.868  -20.941  13.834   1.00 27.65  ? 145 THR   C CA     1 
ATOM   7871  C  C      . THR   C 1  145 ? 22.339  -21.523  12.521   1.00 32.96  ? 145 THR   C C      1 
ATOM   7872  O  O      . THR   C 1  145 ? 23.109  -22.015  11.692   1.00 36.63  ? 145 THR   C O      1 
ATOM   7873  C  CB     . THR   C 1  145 ? 22.367  -21.741  15.026   1.00 29.39  ? 145 THR   C CB     1 
ATOM   7874  O  OG1    . THR   C 1  145 ? 22.656  -21.032  16.236   1.00 33.56  ? 145 THR   C OG1    1 
ATOM   7875  C  CG2    . THR   C 1  145 ? 23.028  -23.082  15.062   1.00 38.90  ? 145 THR   C CG2    1 
ATOM   7876  N  N      . GLY   C 1  146 ? 21.030  -21.442  12.302   1.00 32.56  ? 146 GLY   C N      1 
ATOM   7877  C  CA     . GLY   C 1  146 ? 20.420  -21.843  11.052   1.00 29.17  ? 146 GLY   C CA     1 
ATOM   7878  C  C      . GLY   C 1  146 ? 21.227  -21.473  9.827    1.00 32.80  ? 146 GLY   C C      1 
ATOM   7879  O  O      . GLY   C 1  146 ? 21.371  -22.298  8.917    1.00 34.99  ? 146 GLY   C O      1 
ATOM   7880  N  N      . SER   C 1  147 ? 21.775  -20.255  9.785    1.00 30.91  ? 147 SER   C N      1 
ATOM   7881  C  CA     . SER   C 1  147 ? 22.523  -19.803  8.614    1.00 36.16  ? 147 SER   C CA     1 
ATOM   7882  C  C      . SER   C 1  147 ? 24.017  -20.117  8.706    1.00 39.37  ? 147 SER   C C      1 
ATOM   7883  O  O      . SER   C 1  147 ? 24.551  -20.862  7.875    1.00 37.06  ? 147 SER   C O      1 
ATOM   7884  C  CB     . SER   C 1  147 ? 22.304  -18.301  8.379    1.00 37.74  ? 147 SER   C CB     1 
ATOM   7885  O  OG     . SER   C 1  147 ? 22.727  -17.515  9.468    1.00 37.09  ? 147 SER   C OG     1 
ATOM   7886  N  N      . GLY   C 1  148 ? 24.700  -19.565  9.714    1.00 36.60  ? 148 GLY   C N      1 
ATOM   7887  C  CA     . GLY   C 1  148 ? 26.143  -19.691  9.772    1.00 36.21  ? 148 GLY   C CA     1 
ATOM   7888  C  C      . GLY   C 1  148 ? 26.671  -21.041  10.228   1.00 35.88  ? 148 GLY   C C      1 
ATOM   7889  O  O      . GLY   C 1  148 ? 27.766  -21.428  9.827    1.00 44.85  ? 148 GLY   C O      1 
ATOM   7890  N  N      . PHE   C 1  149 ? 25.946  -21.764  11.088   1.00 32.45  ? 149 PHE   C N      1 
ATOM   7891  C  CA     . PHE   C 1  149 ? 26.449  -23.091  11.444   1.00 34.70  ? 149 PHE   C CA     1 
ATOM   7892  C  C      . PHE   C 1  149 ? 26.144  -24.109  10.358   1.00 37.25  ? 149 PHE   C C      1 
ATOM   7893  O  O      . PHE   C 1  149 ? 26.979  -24.965  10.055   1.00 35.93  ? 149 PHE   C O      1 
ATOM   7894  C  CB     . PHE   C 1  149 ? 25.876  -23.588  12.775   1.00 40.12  ? 149 PHE   C CB     1 
ATOM   7895  C  CG     . PHE   C 1  149 ? 26.596  -24.812  13.318   1.00 41.37  ? 149 PHE   C CG     1 
ATOM   7896  C  CD1    . PHE   C 1  149 ? 27.892  -24.715  13.794   1.00 35.73  ? 149 PHE   C CD1    1 
ATOM   7897  C  CD2    . PHE   C 1  149 ? 25.983  -26.057  13.338   1.00 40.40  ? 149 PHE   C CD2    1 
ATOM   7898  C  CE1    . PHE   C 1  149 ? 28.547  -25.837  14.274   1.00 36.68  ? 149 PHE   C CE1    1 
ATOM   7899  C  CE2    . PHE   C 1  149 ? 26.644  -27.175  13.825   1.00 35.68  ? 149 PHE   C CE2    1 
ATOM   7900  C  CZ     . PHE   C 1  149 ? 27.925  -27.066  14.286   1.00 32.23  ? 149 PHE   C CZ     1 
ATOM   7901  N  N      . THR   C 1  150 ? 24.938  -24.050  9.787    1.00 41.44  ? 150 THR   C N      1 
ATOM   7902  C  CA     . THR   C 1  150 ? 24.605  -24.904  8.653    1.00 34.07  ? 150 THR   C CA     1 
ATOM   7903  C  C      . THR   C 1  150 ? 25.685  -24.824  7.589    1.00 36.45  ? 150 THR   C C      1 
ATOM   7904  O  O      . THR   C 1  150 ? 26.165  -25.846  7.091    1.00 37.59  ? 150 THR   C O      1 
ATOM   7905  C  CB     . THR   C 1  150 ? 23.257  -24.481  8.071    1.00 34.14  ? 150 THR   C CB     1 
ATOM   7906  O  OG1    . THR   C 1  150 ? 22.233  -24.683  9.041    1.00 32.60  ? 150 THR   C OG1    1 
ATOM   7907  C  CG2    . THR   C 1  150 ? 22.937  -25.240  6.783    1.00 28.39  ? 150 THR   C CG2    1 
ATOM   7908  N  N      . SER   C 1  151 ? 26.087  -23.608  7.229    1.00 35.11  ? 151 SER   C N      1 
ATOM   7909  C  CA     . SER   C 1  151 ? 26.989  -23.474  6.100    1.00 36.01  ? 151 SER   C CA     1 
ATOM   7910  C  C      . SER   C 1  151 ? 28.398  -23.924  6.447    1.00 41.11  ? 151 SER   C C      1 
ATOM   7911  O  O      . SER   C 1  151 ? 29.093  -24.454  5.574    1.00 39.41  ? 151 SER   C O      1 
ATOM   7912  C  CB     . SER   C 1  151 ? 26.991  -22.036  5.597    1.00 37.16  ? 151 SER   C CB     1 
ATOM   7913  O  OG     . SER   C 1  151 ? 27.396  -21.174  6.626    1.00 41.77  ? 151 SER   C OG     1 
ATOM   7914  N  N      . LEU   C 1  152 ? 28.829  -23.725  7.703    1.00 42.63  ? 152 LEU   C N      1 
ATOM   7915  C  CA     . LEU   C 1  152 ? 30.090  -24.302  8.174    1.00 42.33  ? 152 LEU   C CA     1 
ATOM   7916  C  C      . LEU   C 1  152 ? 30.055  -25.823  8.096    1.00 41.11  ? 152 LEU   C C      1 
ATOM   7917  O  O      . LEU   C 1  152 ? 31.008  -26.461  7.633    1.00 43.21  ? 152 LEU   C O      1 
ATOM   7918  C  CB     . LEU   C 1  152 ? 30.371  -23.866  9.615    1.00 43.11  ? 152 LEU   C CB     1 
ATOM   7919  C  CG     . LEU   C 1  152 ? 31.591  -24.546  10.260   1.00 41.62  ? 152 LEU   C CG     1 
ATOM   7920  C  CD1    . LEU   C 1  152 ? 32.871  -23.989  9.641    1.00 41.51  ? 152 LEU   C CD1    1 
ATOM   7921  C  CD2    . LEU   C 1  152 ? 31.610  -24.393  11.765   1.00 38.05  ? 152 LEU   C CD2    1 
ATOM   7922  N  N      . LEU   C 1  153 ? 28.958  -26.416  8.557    1.00 36.02  ? 153 LEU   C N      1 
ATOM   7923  C  CA     . LEU   C 1  153 ? 28.793  -27.859  8.512    1.00 34.63  ? 153 LEU   C CA     1 
ATOM   7924  C  C      . LEU   C 1  153 ? 28.721  -28.376  7.084    1.00 38.50  ? 153 LEU   C C      1 
ATOM   7925  O  O      . LEU   C 1  153 ? 29.107  -29.524  6.820    1.00 37.73  ? 153 LEU   C O      1 
ATOM   7926  C  CB     . LEU   C 1  153 ? 27.542  -28.237  9.303    1.00 32.33  ? 153 LEU   C CB     1 
ATOM   7927  C  CG     . LEU   C 1  153 ? 27.026  -29.664  9.245    1.00 38.81  ? 153 LEU   C CG     1 
ATOM   7928  C  CD1    . LEU   C 1  153 ? 27.990  -30.597  9.932    1.00 35.19  ? 153 LEU   C CD1    1 
ATOM   7929  C  CD2    . LEU   C 1  153 ? 25.636  -29.776  9.888    1.00 37.79  ? 153 LEU   C CD2    1 
ATOM   7930  N  N      . MET   C 1  154 ? 28.204  -27.554  6.164    1.00 41.48  ? 154 MET   C N      1 
ATOM   7931  C  CA     . MET   C 1  154 ? 28.049  -27.949  4.767    1.00 34.25  ? 154 MET   C CA     1 
ATOM   7932  C  C      . MET   C 1  154 ? 29.410  -28.021  4.095    1.00 37.97  ? 154 MET   C C      1 
ATOM   7933  O  O      . MET   C 1  154 ? 29.739  -29.015  3.444    1.00 37.55  ? 154 MET   C O      1 
ATOM   7934  C  CB     . MET   C 1  154 ? 27.171  -26.933  4.046    1.00 38.37  ? 154 MET   C CB     1 
ATOM   7935  C  CG     . MET   C 1  154 ? 25.657  -27.075  4.075    1.00 39.29  ? 154 MET   C CG     1 
ATOM   7936  S  SD     . MET   C 1  154 ? 24.835  -28.654  3.984    1.00 40.94  ? 154 MET   C SD     1 
ATOM   7937  C  CE     . MET   C 1  154 ? 24.214  -28.522  2.314    1.00 34.12  ? 154 MET   C CE     1 
ATOM   7938  N  N      . GLU   C 1  155 ? 30.199  -26.942  4.211    1.00 40.17  ? 155 GLU   C N      1 
ATOM   7939  C  CA     . GLU   C 1  155 ? 31.591  -26.976  3.773    1.00 38.82  ? 155 GLU   C CA     1 
ATOM   7940  C  C      . GLU   C 1  155 ? 32.294  -28.204  4.347    1.00 40.69  ? 155 GLU   C C      1 
ATOM   7941  O  O      . GLU   C 1  155 ? 32.954  -28.957  3.619    1.00 38.56  ? 155 GLU   C O      1 
ATOM   7942  C  CB     . GLU   C 1  155 ? 32.313  -25.682  4.186    1.00 34.02  ? 155 GLU   C CB     1 
ATOM   7943  C  CG     . GLU   C 1  155 ? 31.648  -24.415  3.662    1.00 38.73  ? 155 GLU   C CG     1 
ATOM   7944  C  CD     . GLU   C 1  155 ? 32.181  -23.127  4.318    1.00 45.72  ? 155 GLU   C CD     1 
ATOM   7945  O  OE1    . GLU   C 1  155 ? 32.224  -23.035  5.550    1.00 52.75  ? 155 GLU   C OE1    1 
ATOM   7946  O  OE2    . GLU   C 1  155 ? 32.503  -22.160  3.615    1.00 48.64  ? 155 GLU   C OE2    1 
ATOM   7947  N  N      . ARG   C 1  156 ? 32.128  -28.447  5.646    1.00 34.16  ? 156 ARG   C N      1 
ATOM   7948  C  CA     . ARG   C 1  156 ? 32.817  -29.565  6.260    1.00 34.32  ? 156 ARG   C CA     1 
ATOM   7949  C  C      . ARG   C 1  156 ? 32.336  -30.885  5.682    1.00 41.26  ? 156 ARG   C C      1 
ATOM   7950  O  O      . ARG   C 1  156 ? 33.151  -31.713  5.256    1.00 42.74  ? 156 ARG   C O      1 
ATOM   7951  C  CB     . ARG   C 1  156 ? 32.646  -29.523  7.773    1.00 36.99  ? 156 ARG   C CB     1 
ATOM   7952  C  CG     . ARG   C 1  156 ? 33.498  -28.440  8.407    1.00 38.83  ? 156 ARG   C CG     1 
ATOM   7953  C  CD     . ARG   C 1  156 ? 35.003  -28.728  8.246    1.00 43.18  ? 156 ARG   C CD     1 
ATOM   7954  N  NE     . ARG   C 1  156 ? 35.426  -29.750  9.196    1.00 45.40  ? 156 ARG   C NE     1 
ATOM   7955  C  CZ     . ARG   C 1  156 ? 35.755  -29.505  10.458   1.00 37.20  ? 156 ARG   C CZ     1 
ATOM   7956  N  NH1    . ARG   C 1  156 ? 35.853  -28.265  10.920   1.00 34.50  ? 156 ARG   C NH1    1 
ATOM   7957  N  NH2    . ARG   C 1  156 ? 35.963  -30.530  11.281   1.00 36.45  ? 156 ARG   C NH2    1 
ATOM   7958  N  N      . LEU   C 1  157 ? 31.011  -31.093  5.631    1.00 41.32  ? 157 LEU   C N      1 
ATOM   7959  C  CA     . LEU   C 1  157 ? 30.485  -32.330  5.056    1.00 35.04  ? 157 LEU   C CA     1 
ATOM   7960  C  C      . LEU   C 1  157 ? 31.027  -32.576  3.650    1.00 36.72  ? 157 LEU   C C      1 
ATOM   7961  O  O      . LEU   C 1  157 ? 31.326  -33.717  3.289    1.00 39.58  ? 157 LEU   C O      1 
ATOM   7962  C  CB     . LEU   C 1  157 ? 28.972  -32.293  5.038    1.00 33.66  ? 157 LEU   C CB     1 
ATOM   7963  C  CG     . LEU   C 1  157 ? 28.305  -32.355  6.411    1.00 42.97  ? 157 LEU   C CG     1 
ATOM   7964  C  CD1    . LEU   C 1  157 ? 26.786  -32.560  6.250    1.00 35.50  ? 157 LEU   C CD1    1 
ATOM   7965  C  CD2    . LEU   C 1  157 ? 28.922  -33.458  7.272    1.00 37.98  ? 157 LEU   C CD2    1 
ATOM   7966  N  N      . SER   C 1  158 ? 31.180  -31.518  2.849    1.00 32.37  ? 158 SER   C N      1 
ATOM   7967  C  CA     . SER   C 1  158 ? 31.768  -31.659  1.521    1.00 34.88  ? 158 SER   C CA     1 
ATOM   7968  C  C      . SER   C 1  158 ? 33.194  -32.178  1.585    1.00 44.59  ? 158 SER   C C      1 
ATOM   7969  O  O      . SER   C 1  158 ? 33.648  -32.869  0.662    1.00 43.26  ? 158 SER   C O      1 
ATOM   7970  C  CB     . SER   C 1  158 ? 31.772  -30.322  0.786    1.00 36.25  ? 158 SER   C CB     1 
ATOM   7971  O  OG     . SER   C 1  158 ? 30.512  -30.043  0.213    1.00 45.35  ? 158 SER   C OG     1 
ATOM   7972  N  N      . VAL   C 1  159 ? 33.929  -31.816  2.640    1.00 46.35  ? 159 VAL   C N      1 
ATOM   7973  C  CA     . VAL   C 1  159 ? 35.315  -32.249  2.772    1.00 44.24  ? 159 VAL   C CA     1 
ATOM   7974  C  C      . VAL   C 1  159 ? 35.373  -33.698  3.244    1.00 40.11  ? 159 VAL   C C      1 
ATOM   7975  O  O      . VAL   C 1  159 ? 36.113  -34.516  2.686    1.00 43.48  ? 159 VAL   C O      1 
ATOM   7976  C  CB     . VAL   C 1  159 ? 36.071  -31.281  3.710    1.00 41.96  ? 159 VAL   C CB     1 
ATOM   7977  C  CG1    . VAL   C 1  159 ? 37.346  -31.891  4.226    1.00 40.44  ? 159 VAL   C CG1    1 
ATOM   7978  C  CG2    . VAL   C 1  159 ? 36.386  -29.979  2.971    1.00 41.27  ? 159 VAL   C CG2    1 
ATOM   7979  N  N      . ASP   C 1  160 ? 34.560  -34.047  4.233    1.00 35.11  ? 160 ASP   C N      1 
ATOM   7980  C  CA     . ASP   C 1  160 ? 34.600  -35.385  4.803    1.00 42.31  ? 160 ASP   C CA     1 
ATOM   7981  C  C      . ASP   C 1  160 ? 33.808  -36.395  3.991    1.00 41.20  ? 160 ASP   C C      1 
ATOM   7982  O  O      . ASP   C 1  160 ? 34.005  -37.599  4.178    1.00 43.97  ? 160 ASP   C O      1 
ATOM   7983  C  CB     . ASP   C 1  160 ? 34.061  -35.402  6.250    1.00 39.90  ? 160 ASP   C CB     1 
ATOM   7984  C  CG     . ASP   C 1  160 ? 34.899  -34.576  7.219    1.00 45.88  ? 160 ASP   C CG     1 
ATOM   7985  O  OD1    . ASP   C 1  160 ? 35.629  -33.638  6.800    1.00 46.60  ? 160 ASP   C OD1    1 
ATOM   7986  O  OD2    . ASP   C 1  160 ? 34.810  -34.869  8.430    1.00 50.67  ? 160 ASP   C OD2    1 
ATOM   7987  N  N      . TYR   C 1  161 ? 32.879  -35.958  3.141    1.00 39.66  ? 161 TYR   C N      1 
ATOM   7988  C  CA     . TYR   C 1  161 ? 32.065  -36.922  2.409    1.00 40.08  ? 161 TYR   C CA     1 
ATOM   7989  C  C      . TYR   C 1  161 ? 32.019  -36.609  0.918    1.00 44.77  ? 161 TYR   C C      1 
ATOM   7990  O  O      . TYR   C 1  161 ? 31.225  -37.219  0.190    1.00 44.66  ? 161 TYR   C O      1 
ATOM   7991  C  CB     . TYR   C 1  161 ? 30.655  -37.010  2.999    1.00 35.82  ? 161 TYR   C CB     1 
ATOM   7992  C  CG     . TYR   C 1  161 ? 30.610  -37.473  4.451    1.00 40.78  ? 161 TYR   C CG     1 
ATOM   7993  C  CD1    . TYR   C 1  161 ? 30.544  -38.832  4.776    1.00 32.04  ? 161 TYR   C CD1    1 
ATOM   7994  C  CD2    . TYR   C 1  161 ? 30.624  -36.545  5.504    1.00 38.08  ? 161 TYR   C CD2    1 
ATOM   7995  C  CE1    . TYR   C 1  161 ? 30.498  -39.249  6.099    1.00 36.41  ? 161 TYR   C CE1    1 
ATOM   7996  C  CE2    . TYR   C 1  161 ? 30.584  -36.953  6.828    1.00 33.22  ? 161 TYR   C CE2    1 
ATOM   7997  C  CZ     . TYR   C 1  161 ? 30.520  -38.298  7.128    1.00 36.69  ? 161 TYR   C CZ     1 
ATOM   7998  O  OH     . TYR   C 1  161 ? 30.468  -38.688  8.454    1.00 36.46  ? 161 TYR   C OH     1 
ATOM   7999  N  N      . GLY   C 1  162 ? 32.861  -35.691  0.448    1.00 43.23  ? 162 GLY   C N      1 
ATOM   8000  C  CA     . GLY   C 1  162 ? 33.006  -35.495  -0.978   1.00 41.86  ? 162 GLY   C CA     1 
ATOM   8001  C  C      . GLY   C 1  162 ? 31.671  -35.163  -1.597   1.00 54.04  ? 162 GLY   C C      1 
ATOM   8002  O  O      . GLY   C 1  162 ? 30.937  -34.297  -1.103   1.00 57.91  ? 162 GLY   C O      1 
ATOM   8003  N  N      . LYS   C 1  163 ? 31.329  -35.858  -2.684   1.00 52.04  ? 163 LYS   C N      1 
ATOM   8004  C  CA     . LYS   C 1  163 ? 30.151  -35.490  -3.463   1.00 51.59  ? 163 LYS   C CA     1 
ATOM   8005  C  C      . LYS   C 1  163 ? 28.878  -36.212  -3.019   1.00 55.34  ? 163 LYS   C C      1 
ATOM   8006  O  O      . LYS   C 1  163 ? 27.811  -35.942  -3.592   1.00 56.72  ? 163 LYS   C O      1 
ATOM   8007  C  CB     . LYS   C 1  163 ? 30.399  -35.726  -4.961   1.00 47.60  ? 163 LYS   C CB     1 
ATOM   8008  C  CG     . LYS   C 1  163 ? 31.465  -34.810  -5.569   1.00 55.67  ? 163 LYS   C CG     1 
ATOM   8009  C  CD     . LYS   C 1  163 ? 30.853  -33.555  -6.203   1.00 55.46  ? 163 LYS   C CD     1 
ATOM   8010  C  CE     . LYS   C 1  163 ? 30.179  -32.686  -5.130   1.00 60.96  ? 163 LYS   C CE     1 
ATOM   8011  N  NZ     . LYS   C 1  163 ? 29.867  -31.292  -5.568   1.00 60.06  ? 163 LYS   C NZ     1 
ATOM   8012  N  N      . LYS   C 1  164 ? 28.967  -37.109  -2.023   1.00 45.72  ? 164 LYS   C N      1 
ATOM   8013  C  CA     . LYS   C 1  164 ? 27.797  -37.683  -1.359   1.00 40.29  ? 164 LYS   C CA     1 
ATOM   8014  C  C      . LYS   C 1  164 ? 26.704  -36.628  -1.210   1.00 39.59  ? 164 LYS   C C      1 
ATOM   8015  O  O      . LYS   C 1  164 ? 26.999  -35.474  -0.897   1.00 47.09  ? 164 LYS   C O      1 
ATOM   8016  C  CB     . LYS   C 1  164 ? 28.218  -38.216  0.015    1.00 39.65  ? 164 LYS   C CB     1 
ATOM   8017  C  CG     . LYS   C 1  164 ? 27.195  -39.059  0.702    1.00 41.54  ? 164 LYS   C CG     1 
ATOM   8018  C  CD     . LYS   C 1  164 ? 27.772  -40.386  1.113    1.00 37.52  ? 164 LYS   C CD     1 
ATOM   8019  C  CE     . LYS   C 1  164 ? 27.626  -41.392  0.014    1.00 40.17  ? 164 LYS   C CE     1 
ATOM   8020  N  NZ     . LYS   C 1  164 ? 28.043  -42.756  0.467    1.00 45.19  ? 164 LYS   C NZ     1 
ATOM   8021  N  N      . SER   C 1  165 ? 25.442  -37.016  -1.450   1.00 38.18  ? 165 SER   C N      1 
ATOM   8022  C  CA     . SER   C 1  165 ? 24.333  -36.048  -1.522   1.00 36.58  ? 165 SER   C CA     1 
ATOM   8023  C  C      . SER   C 1  165 ? 24.080  -35.278  -0.237   1.00 36.61  ? 165 SER   C C      1 
ATOM   8024  O  O      . SER   C 1  165 ? 24.020  -35.858  0.856    1.00 37.19  ? 165 SER   C O      1 
ATOM   8025  C  CB     . SER   C 1  165 ? 23.018  -36.724  -1.876   1.00 28.98  ? 165 SER   C CB     1 
ATOM   8026  O  OG     . SER   C 1  165 ? 22.737  -36.482  -3.220   1.00 49.59  ? 165 SER   C OG     1 
ATOM   8027  N  N      . LYS   C 1  166 ? 23.824  -33.977  -0.397   1.00 27.41  ? 166 LYS   C N      1 
ATOM   8028  C  CA     . LYS   C 1  166 ? 23.355  -33.109  0.683    1.00 29.88  ? 166 LYS   C CA     1 
ATOM   8029  C  C      . LYS   C 1  166 ? 22.109  -32.366  0.195    1.00 33.51  ? 166 LYS   C C      1 
ATOM   8030  O  O      . LYS   C 1  166 ? 22.199  -31.480  -0.664   1.00 32.50  ? 166 LYS   C O      1 
ATOM   8031  C  CB     . LYS   C 1  166 ? 24.453  -32.140  1.120    1.00 26.11  ? 166 LYS   C CB     1 
ATOM   8032  C  CG     . LYS   C 1  166 ? 25.739  -32.838  1.515    1.00 27.01  ? 166 LYS   C CG     1 
ATOM   8033  C  CD     . LYS   C 1  166 ? 26.588  -31.966  2.466    1.00 35.75  ? 166 LYS   C CD     1 
ATOM   8034  C  CE     . LYS   C 1  166 ? 27.688  -31.131  1.774    1.00 34.89  ? 166 LYS   C CE     1 
ATOM   8035  N  NZ     . LYS   C 1  166 ? 28.404  -31.874  0.693    1.00 40.88  ? 166 LYS   C NZ     1 
ATOM   8036  N  N      . LEU   C 1  167 ? 20.945  -32.750  0.719    1.00 32.12  ? 167 LEU   C N      1 
ATOM   8037  C  CA     . LEU   C 1  167 ? 19.689  -32.060  0.485    1.00 29.13  ? 167 LEU   C CA     1 
ATOM   8038  C  C      . LEU   C 1  167 ? 19.418  -31.120  1.651    1.00 33.42  ? 167 LEU   C C      1 
ATOM   8039  O  O      . LEU   C 1  167 ? 19.805  -31.383  2.795    1.00 31.64  ? 167 LEU   C O      1 
ATOM   8040  C  CB     . LEU   C 1  167 ? 18.547  -33.069  0.341    1.00 35.21  ? 167 LEU   C CB     1 
ATOM   8041  C  CG     . LEU   C 1  167 ? 18.125  -33.577  -1.046   1.00 41.72  ? 167 LEU   C CG     1 
ATOM   8042  C  CD1    . LEU   C 1  167 ? 19.226  -34.391  -1.745   1.00 36.47  ? 167 LEU   C CD1    1 
ATOM   8043  C  CD2    . LEU   C 1  167 ? 16.912  -34.441  -0.886   1.00 39.21  ? 167 LEU   C CD2    1 
ATOM   8044  N  N      . GLU   C 1  168 ? 18.740  -30.023  1.356    1.00 35.84  ? 168 GLU   C N      1 
ATOM   8045  C  CA     . GLU   C 1  168 ? 18.397  -29.009  2.345    1.00 34.30  ? 168 GLU   C CA     1 
ATOM   8046  C  C      . GLU   C 1  168 ? 16.888  -28.867  2.420    1.00 36.23  ? 168 GLU   C C      1 
ATOM   8047  O  O      . GLU   C 1  168 ? 16.210  -28.871  1.381    1.00 33.57  ? 168 GLU   C O      1 
ATOM   8048  C  CB     . GLU   C 1  168 ? 18.958  -27.648  1.959    1.00 36.56  ? 168 GLU   C CB     1 
ATOM   8049  C  CG     . GLU   C 1  168 ? 20.303  -27.305  2.448    1.00 34.54  ? 168 GLU   C CG     1 
ATOM   8050  C  CD     . GLU   C 1  168 ? 20.784  -26.037  1.824    1.00 38.93  ? 168 GLU   C CD     1 
ATOM   8051  O  OE1    . GLU   C 1  168 ? 20.916  -26.044  0.578    1.00 45.15  ? 168 GLU   C OE1    1 
ATOM   8052  O  OE2    . GLU   C 1  168 ? 20.980  -25.028  2.550    1.00 34.23  ? 168 GLU   C OE2    1 
ATOM   8053  N  N      . PHE   C 1  169 ? 16.370  -28.723  3.647    1.00 35.80  ? 169 PHE   C N      1 
ATOM   8054  C  CA     . PHE   C 1  169 ? 15.034  -28.166  3.901    1.00 29.40  ? 169 PHE   C CA     1 
ATOM   8055  C  C      . PHE   C 1  169 ? 15.253  -26.838  4.631    1.00 32.49  ? 169 PHE   C C      1 
ATOM   8056  O  O      . PHE   C 1  169 ? 15.698  -26.823  5.784    1.00 31.80  ? 169 PHE   C O      1 
ATOM   8057  C  CB     . PHE   C 1  169 ? 14.166  -29.134  4.701    1.00 29.44  ? 169 PHE   C CB     1 
ATOM   8058  C  CG     . PHE   C 1  169 ? 13.577  -30.268  3.866    1.00 44.09  ? 169 PHE   C CG     1 
ATOM   8059  C  CD1    . PHE   C 1  169 ? 12.491  -30.049  3.022    1.00 40.70  ? 169 PHE   C CD1    1 
ATOM   8060  C  CD2    . PHE   C 1  169 ? 14.127  -31.555  3.907    1.00 42.13  ? 169 PHE   C CD2    1 
ATOM   8061  C  CE1    . PHE   C 1  169 ? 11.977  -31.094  2.254    1.00 38.96  ? 169 PHE   C CE1    1 
ATOM   8062  C  CE2    . PHE   C 1  169 ? 13.608  -32.602  3.133    1.00 32.24  ? 169 PHE   C CE2    1 
ATOM   8063  C  CZ     . PHE   C 1  169 ? 12.545  -32.371  2.314    1.00 34.96  ? 169 PHE   C CZ     1 
ATOM   8064  N  N      . SER   C 1  170 ? 14.997  -25.723  3.944    1.00 28.82  ? 170 SER   C N      1 
ATOM   8065  C  CA     . SER   C 1  170 ? 15.438  -24.404  4.378    1.00 26.88  ? 170 SER   C CA     1 
ATOM   8066  C  C      . SER   C 1  170 ? 14.224  -23.547  4.682    1.00 30.18  ? 170 SER   C C      1 
ATOM   8067  O  O      . SER   C 1  170 ? 13.420  -23.303  3.781    1.00 30.71  ? 170 SER   C O      1 
ATOM   8068  C  CB     . SER   C 1  170 ? 16.282  -23.709  3.300    1.00 31.61  ? 170 SER   C CB     1 
ATOM   8069  O  OG     . SER   C 1  170 ? 17.393  -24.486  2.882    1.00 39.65  ? 170 SER   C OG     1 
ATOM   8070  N  N      . ILE   C 1  171 ? 14.115  -23.060  5.926    1.00 32.04  ? 171 ILE   C N      1 
ATOM   8071  C  CA     . ILE   C 1  171 ? 13.040  -22.150  6.334    1.00 29.58  ? 171 ILE   C CA     1 
ATOM   8072  C  C      . ILE   C 1  171 ? 13.409  -20.744  5.890    1.00 30.34  ? 171 ILE   C C      1 
ATOM   8073  O  O      . ILE   C 1  171 ? 14.327  -20.135  6.440    1.00 31.43  ? 171 ILE   C O      1 
ATOM   8074  C  CB     . ILE   C 1  171 ? 12.791  -22.180  7.846    1.00 31.06  ? 171 ILE   C CB     1 
ATOM   8075  C  CG1    . ILE   C 1  171 ? 12.623  -23.613  8.354    1.00 34.12  ? 171 ILE   C CG1    1 
ATOM   8076  C  CG2    . ILE   C 1  171 ? 11.600  -21.322  8.197    1.00 24.90  ? 171 ILE   C CG2    1 
ATOM   8077  C  CD1    . ILE   C 1  171 ? 11.912  -24.525  7.406    1.00 35.77  ? 171 ILE   C CD1    1 
ATOM   8078  N  N      . TYR   C 1  172 ? 12.678  -20.223  4.931    1.00 32.75  ? 172 TYR   C N      1 
ATOM   8079  C  CA     . TYR   C 1  172 ? 12.804  -18.896  4.329    1.00 33.25  ? 172 TYR   C CA     1 
ATOM   8080  C  C      . TYR   C 1  172 ? 12.022  -17.890  5.163    1.00 34.76  ? 172 TYR   C C      1 
ATOM   8081  O  O      . TYR   C 1  172 ? 10.878  -18.162  5.537    1.00 31.46  ? 172 TYR   C O      1 
ATOM   8082  C  CB     . TYR   C 1  172 ? 12.281  -18.924  2.903    1.00 33.78  ? 172 TYR   C CB     1 
ATOM   8083  C  CG     . TYR   C 1  172 ? 12.241  -17.623  2.139    1.00 36.36  ? 172 TYR   C CG     1 
ATOM   8084  C  CD1    . TYR   C 1  172 ? 11.203  -16.708  2.333    1.00 37.62  ? 172 TYR   C CD1    1 
ATOM   8085  C  CD2    . TYR   C 1  172 ? 13.185  -17.346  1.145    1.00 35.73  ? 172 TYR   C CD2    1 
ATOM   8086  C  CE1    . TYR   C 1  172 ? 11.133  -15.531  1.602    1.00 31.54  ? 172 TYR   C CE1    1 
ATOM   8087  C  CE2    . TYR   C 1  172 ? 13.106  -16.168  0.395    1.00 37.31  ? 172 TYR   C CE2    1 
ATOM   8088  C  CZ     . TYR   C 1  172 ? 12.079  -15.261  0.640    1.00 33.77  ? 172 TYR   C CZ     1 
ATOM   8089  O  OH     . TYR   C 1  172 ? 11.990  -14.086  -0.086   1.00 37.08  ? 172 TYR   C OH     1 
ATOM   8090  N  N      . PRO   C 1  173 ? 12.602  -16.744  5.490    1.00 35.36  ? 173 PRO   C N      1 
ATOM   8091  C  CA     . PRO   C 1  173 ? 12.032  -15.903  6.535    1.00 27.87  ? 173 PRO   C CA     1 
ATOM   8092  C  C      . PRO   C 1  173 ? 10.809  -15.150  6.063    1.00 35.27  ? 173 PRO   C C      1 
ATOM   8093  O  O      . PRO   C 1  173 ? 10.665  -14.801  4.891    1.00 40.32  ? 173 PRO   C O      1 
ATOM   8094  C  CB     . PRO   C 1  173 ? 13.177  -14.947  6.863    1.00 27.81  ? 173 PRO   C CB     1 
ATOM   8095  C  CG     . PRO   C 1  173 ? 13.993  -14.911  5.653    1.00 28.70  ? 173 PRO   C CG     1 
ATOM   8096  C  CD     . PRO   C 1  173 ? 13.896  -16.236  5.011    1.00 34.31  ? 173 PRO   C CD     1 
ATOM   8097  N  N      . ALA   C 1  174 ? 9.923   -14.888  7.017    1.00 41.53  ? 174 ALA   C N      1 
ATOM   8098  C  CA     . ALA   C 1  174 ? 8.648   -14.256  6.778    1.00 32.57  ? 174 ALA   C CA     1 
ATOM   8099  C  C      . ALA   C 1  174 ? 8.412   -13.268  7.908    1.00 41.33  ? 174 ALA   C C      1 
ATOM   8100  O  O      . ALA   C 1  174 ? 8.702   -13.579  9.077    1.00 50.00  ? 174 ALA   C O      1 
ATOM   8101  C  CB     . ALA   C 1  174 ? 7.519   -15.294  6.738    1.00 37.11  ? 174 ALA   C CB     1 
ATOM   8102  N  N      . PRO   C 1  175 ? 7.866   -12.086  7.606    1.00 53.61  ? 175 PRO   C N      1 
ATOM   8103  C  CA     . PRO   C 1  175 ? 7.743   -11.040  8.647    1.00 47.94  ? 175 PRO   C CA     1 
ATOM   8104  C  C      . PRO   C 1  175 ? 6.809   -11.394  9.795    1.00 46.83  ? 175 PRO   C C      1 
ATOM   8105  O  O      . PRO   C 1  175 ? 6.992   -10.844  10.886   1.00 49.13  ? 175 PRO   C O      1 
ATOM   8106  C  CB     . PRO   C 1  175 ? 7.217   -9.839   7.864    1.00 40.28  ? 175 PRO   C CB     1 
ATOM   8107  C  CG     . PRO   C 1  175 ? 6.446   -10.465  6.736    1.00 43.75  ? 175 PRO   C CG     1 
ATOM   8108  C  CD     . PRO   C 1  175 ? 7.225   -11.684  6.338    1.00 47.61  ? 175 PRO   C CD     1 
ATOM   8109  N  N      . GLN   C 1  176 ? 5.835   -12.299  9.588    1.00 47.06  ? 176 GLN   C N      1 
ATOM   8110  C  CA     . GLN   C 1  176 ? 4.832   -12.618  10.613   1.00 49.23  ? 176 GLN   C CA     1 
ATOM   8111  C  C      . GLN   C 1  176 ? 5.407   -13.440  11.764   1.00 48.16  ? 176 GLN   C C      1 
ATOM   8112  O  O      . GLN   C 1  176 ? 4.906   -13.346  12.892   1.00 44.46  ? 176 GLN   C O      1 
ATOM   8113  C  CB     . GLN   C 1  176 ? 3.648   -13.397  10.015   1.00 45.69  ? 176 GLN   C CB     1 
ATOM   8114  C  CG     . GLN   C 1  176 ? 2.726   -12.618  9.127    1.00 42.97  ? 176 GLN   C CG     1 
ATOM   8115  C  CD     . GLN   C 1  176 ? 3.091   -12.796  7.679    1.00 49.83  ? 176 GLN   C CD     1 
ATOM   8116  O  OE1    . GLN   C 1  176 ? 4.264   -13.000  7.350    1.00 50.88  ? 176 GLN   C OE1    1 
ATOM   8117  N  NE2    . GLN   C 1  176 ? 2.098   -12.718  6.793    1.00 51.04  ? 176 GLN   C NE2    1 
ATOM   8118  N  N      . VAL   C 1  177 ? 6.411   -14.282  11.507   1.00 46.00  ? 177 VAL   C N      1 
ATOM   8119  C  CA     . VAL   C 1  177 ? 6.993   -15.103  12.560   1.00 42.40  ? 177 VAL   C CA     1 
ATOM   8120  C  C      . VAL   C 1  177 ? 8.477   -14.842  12.727   1.00 45.30  ? 177 VAL   C C      1 
ATOM   8121  O  O      . VAL   C 1  177 ? 9.149   -15.570  13.450   1.00 50.83  ? 177 VAL   C O      1 
ATOM   8122  C  CB     . VAL   C 1  177 ? 6.725   -16.602  12.322   1.00 40.64  ? 177 VAL   C CB     1 
ATOM   8123  C  CG1    . VAL   C 1  177 ? 5.429   -17.041  12.991   1.00 41.38  ? 177 VAL   C CG1    1 
ATOM   8124  C  CG2    . VAL   C 1  177 ? 6.651   -16.885  10.846   1.00 44.12  ? 177 VAL   C CG2    1 
ATOM   8125  N  N      . SER   C 1  178 ? 9.004   -13.807  12.086   1.00 46.68  ? 178 SER   C N      1 
ATOM   8126  C  CA     . SER   C 1  178 ? 10.439  -13.576  12.148   1.00 45.55  ? 178 SER   C CA     1 
ATOM   8127  C  C      . SER   C 1  178 ? 10.882  -13.203  13.565   1.00 50.43  ? 178 SER   C C      1 
ATOM   8128  O  O      . SER   C 1  178 ? 10.117  -12.641  14.358   1.00 55.21  ? 178 SER   C O      1 
ATOM   8129  C  CB     . SER   C 1  178 ? 10.839  -12.488  11.155   1.00 43.56  ? 178 SER   C CB     1 
ATOM   8130  O  OG     . SER   C 1  178 ? 10.533  -11.216  11.699   1.00 55.94  ? 178 SER   C OG     1 
ATOM   8131  N  N      . THR   C 1  179 ? 12.147  -13.526  13.865   1.00 51.91  ? 179 THR   C N      1 
ATOM   8132  C  CA     . THR   C 1  179 ? 12.859  -13.261  15.116   1.00 45.99  ? 179 THR   C CA     1 
ATOM   8133  C  C      . THR   C 1  179 ? 13.705  -11.994  15.060   1.00 48.48  ? 179 THR   C C      1 
ATOM   8134  O  O      . THR   C 1  179 ? 13.784  -11.258  16.042   1.00 46.01  ? 179 THR   C O      1 
ATOM   8135  C  CB     . THR   C 1  179 ? 13.820  -14.426  15.446   1.00 49.40  ? 179 THR   C CB     1 
ATOM   8136  O  OG1    . THR   C 1  179 ? 13.107  -15.663  15.615   1.00 50.13  ? 179 THR   C OG1    1 
ATOM   8137  C  CG2    . THR   C 1  179 ? 14.697  -14.102  16.703   1.00 45.05  ? 179 THR   C CG2    1 
ATOM   8138  N  N      . ALA   C 1  180 ? 14.392  -11.756  13.943   1.00 44.32  ? 180 ALA   C N      1 
ATOM   8139  C  CA     . ALA   C 1  180 ? 15.515  -10.842  13.902   1.00 32.77  ? 180 ALA   C CA     1 
ATOM   8140  C  C      . ALA   C 1  180 ? 15.377  -9.935   12.703   1.00 37.09  ? 180 ALA   C C      1 
ATOM   8141  O  O      . ALA   C 1  180 ? 14.942  -10.371  11.634   1.00 47.01  ? 180 ALA   C O      1 
ATOM   8142  C  CB     . ALA   C 1  180 ? 16.827  -11.603  13.821   1.00 36.76  ? 180 ALA   C CB     1 
ATOM   8143  N  N      . VAL   C 1  181 ? 15.746  -8.669   12.878   1.00 32.52  ? 181 VAL   C N      1 
ATOM   8144  C  CA     . VAL   C 1  181 ? 15.740  -7.752   11.750   1.00 34.61  ? 181 VAL   C CA     1 
ATOM   8145  C  C      . VAL   C 1  181 ? 16.860  -8.042   10.757   1.00 32.35  ? 181 VAL   C C      1 
ATOM   8146  O  O      . VAL   C 1  181 ? 16.869  -7.465   9.656    1.00 31.41  ? 181 VAL   C O      1 
ATOM   8147  C  CB     . VAL   C 1  181 ? 15.831  -6.297   12.263   1.00 36.85  ? 181 VAL   C CB     1 
ATOM   8148  C  CG1    . VAL   C 1  181 ? 17.228  -6.000   12.822   1.00 31.55  ? 181 VAL   C CG1    1 
ATOM   8149  C  CG2    . VAL   C 1  181 ? 15.488  -5.332   11.150   1.00 34.49  ? 181 VAL   C CG2    1 
ATOM   8150  N  N      . VAL   C 1  182 ? 17.824  -8.892   11.123   1.00 28.77  ? 182 VAL   C N      1 
ATOM   8151  C  CA     . VAL   C 1  182 ? 18.967  -9.174   10.265   1.00 29.44  ? 182 VAL   C CA     1 
ATOM   8152  C  C      . VAL   C 1  182 ? 18.782  -10.472  9.489    1.00 35.24  ? 182 VAL   C C      1 
ATOM   8153  O  O      . VAL   C 1  182 ? 19.725  -10.941  8.850    1.00 34.42  ? 182 VAL   C O      1 
ATOM   8154  C  CB     . VAL   C 1  182 ? 20.302  -9.184   11.038   1.00 29.16  ? 182 VAL   C CB     1 
ATOM   8155  C  CG1    . VAL   C 1  182 ? 20.608  -7.809   11.564   1.00 34.27  ? 182 VAL   C CG1    1 
ATOM   8156  C  CG2    . VAL   C 1  182 ? 20.331  -10.218  12.142   1.00 29.83  ? 182 VAL   C CG2    1 
ATOM   8157  N  N      . GLU   C 1  183 ? 17.576  -11.042  9.497    1.00 33.66  ? 183 GLU   C N      1 
ATOM   8158  C  CA     . GLU   C 1  183 ? 17.356  -12.274  8.759    1.00 30.73  ? 183 GLU   C CA     1 
ATOM   8159  C  C      . GLU   C 1  183 ? 17.735  -12.148  7.283    1.00 32.72  ? 183 GLU   C C      1 
ATOM   8160  O  O      . GLU   C 1  183 ? 18.267  -13.130  6.745    1.00 38.41  ? 183 GLU   C O      1 
ATOM   8161  C  CB     . GLU   C 1  183 ? 15.905  -12.759  8.984    1.00 31.77  ? 183 GLU   C CB     1 
ATOM   8162  C  CG     . GLU   C 1  183 ? 15.780  -13.358  10.390   1.00 35.70  ? 183 GLU   C CG     1 
ATOM   8163  C  CD     . GLU   C 1  183 ? 14.486  -14.089  10.709   1.00 40.65  ? 183 GLU   C CD     1 
ATOM   8164  O  OE1    . GLU   C 1  183 ? 14.119  -15.016  9.961    1.00 41.07  ? 183 GLU   C OE1    1 
ATOM   8165  O  OE2    . GLU   C 1  183 ? 13.863  -13.785  11.764   1.00 37.45  ? 183 GLU   C OE2    1 
ATOM   8166  N  N      . PRO   C 1  184 ? 17.565  -11.013  6.593    1.00 33.01  ? 184 PRO   C N      1 
ATOM   8167  C  CA     . PRO   C 1  184 ? 18.045  -10.965  5.193    1.00 31.19  ? 184 PRO   C CA     1 
ATOM   8168  C  C      . PRO   C 1  184 ? 19.556  -11.174  5.053    1.00 38.25  ? 184 PRO   C C      1 
ATOM   8169  O  O      . PRO   C 1  184 ? 20.003  -11.878  4.136    1.00 35.96  ? 184 PRO   C O      1 
ATOM   8170  C  CB     . PRO   C 1  184 ? 17.598  -9.574   4.719    1.00 24.67  ? 184 PRO   C CB     1 
ATOM   8171  C  CG     . PRO   C 1  184 ? 16.439  -9.269   5.525    1.00 25.73  ? 184 PRO   C CG     1 
ATOM   8172  C  CD     . PRO   C 1  184 ? 16.736  -9.838   6.910    1.00 29.18  ? 184 PRO   C CD     1 
ATOM   8173  N  N      . TYR   C 1  185 ? 20.362  -10.590  5.945    1.00 39.44  ? 185 TYR   C N      1 
ATOM   8174  C  CA     . TYR   C 1  185 ? 21.804  -10.800  5.879    1.00 32.78  ? 185 TYR   C CA     1 
ATOM   8175  C  C      . TYR   C 1  185 ? 22.147  -12.266  6.081    1.00 34.53  ? 185 TYR   C C      1 
ATOM   8176  O  O      . TYR   C 1  185 ? 22.848  -12.874  5.265    1.00 36.15  ? 185 TYR   C O      1 
ATOM   8177  C  CB     . TYR   C 1  185 ? 22.520  -9.956   6.929    1.00 33.08  ? 185 TYR   C CB     1 
ATOM   8178  C  CG     . TYR   C 1  185 ? 22.589  -8.483   6.616    1.00 38.01  ? 185 TYR   C CG     1 
ATOM   8179  C  CD1    . TYR   C 1  185 ? 22.190  -7.982   5.381    1.00 32.97  ? 185 TYR   C CD1    1 
ATOM   8180  C  CD2    . TYR   C 1  185 ? 23.037  -7.584   7.578    1.00 38.08  ? 185 TYR   C CD2    1 
ATOM   8181  C  CE1    . TYR   C 1  185 ? 22.263  -6.636   5.118    1.00 34.64  ? 185 TYR   C CE1    1 
ATOM   8182  C  CE2    . TYR   C 1  185 ? 23.105  -6.238   7.324    1.00 35.87  ? 185 TYR   C CE2    1 
ATOM   8183  C  CZ     . TYR   C 1  185 ? 22.727  -5.765   6.097    1.00 39.48  ? 185 TYR   C CZ     1 
ATOM   8184  O  OH     . TYR   C 1  185 ? 22.810  -4.406   5.875    1.00 42.31  ? 185 TYR   C OH     1 
ATOM   8185  N  N      . ASN   C 1  186 ? 21.692  -12.850  7.181    1.00 33.34  ? 186 ASN   C N      1 
ATOM   8186  C  CA     . ASN   C 1  186 ? 22.005  -14.253  7.380    1.00 34.70  ? 186 ASN   C CA     1 
ATOM   8187  C  C      . ASN   C 1  186 ? 21.530  -15.064  6.193    1.00 39.45  ? 186 ASN   C C      1 
ATOM   8188  O  O      . ASN   C 1  186 ? 22.187  -16.047  5.816    1.00 38.10  ? 186 ASN   C O      1 
ATOM   8189  C  CB     . ASN   C 1  186 ? 21.376  -14.787  8.667    1.00 32.65  ? 186 ASN   C CB     1 
ATOM   8190  C  CG     . ASN   C 1  186 ? 21.730  -13.963  9.879    1.00 34.54  ? 186 ASN   C CG     1 
ATOM   8191  O  OD1    . ASN   C 1  186 ? 22.775  -13.301  9.926    1.00 35.49  ? 186 ASN   C OD1    1 
ATOM   8192  N  ND2    . ASN   C 1  186 ? 20.875  -14.019  10.886   1.00 35.08  ? 186 ASN   C ND2    1 
ATOM   8193  N  N      . SER   C 1  187 ? 20.413  -14.641  5.570    1.00 39.43  ? 187 SER   C N      1 
ATOM   8194  C  CA     . SER   C 1  187 ? 19.822  -15.400  4.467    1.00 32.07  ? 187 SER   C CA     1 
ATOM   8195  C  C      . SER   C 1  187 ? 20.759  -15.453  3.274    1.00 33.54  ? 187 SER   C C      1 
ATOM   8196  O  O      . SER   C 1  187 ? 21.105  -16.536  2.803    1.00 33.81  ? 187 SER   C O      1 
ATOM   8197  C  CB     . SER   C 1  187 ? 18.479  -14.805  4.068    1.00 33.05  ? 187 SER   C CB     1 
ATOM   8198  O  OG     . SER   C 1  187 ? 17.444  -15.346  4.885    1.00 38.66  ? 187 SER   C OG     1 
ATOM   8199  N  N      . ILE   C 1  188 ? 21.209  -14.290  2.796    1.00 35.23  ? 188 ILE   C N      1 
ATOM   8200  C  CA     . ILE   C 1  188 ? 22.111  -14.238  1.651    1.00 28.94  ? 188 ILE   C CA     1 
ATOM   8201  C  C      . ILE   C 1  188 ? 23.452  -14.879  1.981    1.00 32.59  ? 188 ILE   C C      1 
ATOM   8202  O  O      . ILE   C 1  188 ? 24.028  -15.606  1.165    1.00 35.75  ? 188 ILE   C O      1 
ATOM   8203  C  CB     . ILE   C 1  188 ? 22.300  -12.786  1.184    1.00 32.69  ? 188 ILE   C CB     1 
ATOM   8204  C  CG1    . ILE   C 1  188 ? 21.251  -12.379  0.122    1.00 35.29  ? 188 ILE   C CG1    1 
ATOM   8205  C  CG2    . ILE   C 1  188 ? 23.696  -12.628  0.648    1.00 27.53  ? 188 ILE   C CG2    1 
ATOM   8206  C  CD1    . ILE   C 1  188 ? 19.816  -12.338  0.585    1.00 25.81  ? 188 ILE   C CD1    1 
ATOM   8207  N  N      . LEU   C 1  189 ? 23.996  -14.606  3.162    1.00 35.57  ? 189 LEU   C N      1 
ATOM   8208  C  CA     . LEU   C 1  189 ? 25.302  -15.168  3.478    1.00 32.12  ? 189 LEU   C CA     1 
ATOM   8209  C  C      . LEU   C 1  189 ? 25.263  -16.689  3.379    1.00 38.73  ? 189 LEU   C C      1 
ATOM   8210  O  O      . LEU   C 1  189 ? 26.088  -17.306  2.689    1.00 40.26  ? 189 LEU   C O      1 
ATOM   8211  C  CB     . LEU   C 1  189 ? 25.760  -14.701  4.860    1.00 33.01  ? 189 LEU   C CB     1 
ATOM   8212  C  CG     . LEU   C 1  189 ? 26.014  -13.189  5.018    1.00 31.22  ? 189 LEU   C CG     1 
ATOM   8213  C  CD1    . LEU   C 1  189 ? 26.275  -12.912  6.447    1.00 30.60  ? 189 LEU   C CD1    1 
ATOM   8214  C  CD2    . LEU   C 1  189 ? 27.179  -12.678  4.168    1.00 33.69  ? 189 LEU   C CD2    1 
ATOM   8215  N  N      . THR   C 1  190 ? 24.265  -17.313  4.003    1.00 37.09  ? 190 THR   C N      1 
ATOM   8216  C  CA     . THR   C 1  190 ? 24.224  -18.767  3.986    1.00 37.97  ? 190 THR   C CA     1 
ATOM   8217  C  C      . THR   C 1  190 ? 23.843  -19.305  2.599    1.00 38.97  ? 190 THR   C C      1 
ATOM   8218  O  O      . THR   C 1  190 ? 24.338  -20.368  2.188    1.00 37.98  ? 190 THR   C O      1 
ATOM   8219  C  CB     . THR   C 1  190 ? 23.281  -19.267  5.091    1.00 35.32  ? 190 THR   C CB     1 
ATOM   8220  O  OG1    . THR   C 1  190 ? 23.422  -20.684  5.244    1.00 37.39  ? 190 THR   C OG1    1 
ATOM   8221  C  CG2    . THR   C 1  190 ? 21.850  -18.947  4.751    1.00 36.32  ? 190 THR   C CG2    1 
ATOM   8222  N  N      . THR   C 1  191 ? 23.000  -18.592  1.847    1.00 31.78  ? 191 THR   C N      1 
ATOM   8223  C  CA     . THR   C 1  191 ? 22.660  -19.094  0.517    1.00 37.63  ? 191 THR   C CA     1 
ATOM   8224  C  C      . THR   C 1  191 ? 23.893  -19.118  -0.370   1.00 37.04  ? 191 THR   C C      1 
ATOM   8225  O  O      . THR   C 1  191 ? 24.093  -20.059  -1.147   1.00 42.48  ? 191 THR   C O      1 
ATOM   8226  C  CB     . THR   C 1  191 ? 21.539  -18.267  -0.130   1.00 33.87  ? 191 THR   C CB     1 
ATOM   8227  O  OG1    . THR   C 1  191 ? 20.292  -18.573  0.509    1.00 34.07  ? 191 THR   C OG1    1 
ATOM   8228  C  CG2    . THR   C 1  191 ? 21.398  -18.633  -1.591   1.00 30.22  ? 191 THR   C CG2    1 
ATOM   8229  N  N      . HIS   C 1  192 ? 24.748  -18.111  -0.236   1.00 36.20  ? 192 HIS   C N      1 
ATOM   8230  C  CA     . HIS   C 1  192 ? 25.970  -18.055  -1.023   1.00 36.12  ? 192 HIS   C CA     1 
ATOM   8231  C  C      . HIS   C 1  192 ? 26.972  -19.116  -0.580   1.00 36.05  ? 192 HIS   C C      1 
ATOM   8232  O  O      . HIS   C 1  192 ? 27.560  -19.820  -1.403   1.00 38.37  ? 192 HIS   C O      1 
ATOM   8233  C  CB     . HIS   C 1  192 ? 26.571  -16.667  -0.889   1.00 39.99  ? 192 HIS   C CB     1 
ATOM   8234  C  CG     . HIS   C 1  192 ? 27.995  -16.589  -1.312   1.00 40.29  ? 192 HIS   C CG     1 
ATOM   8235  N  ND1    . HIS   C 1  192 ? 28.430  -17.063  -2.530   1.00 39.94  ? 192 HIS   C ND1    1 
ATOM   8236  C  CD2    . HIS   C 1  192 ? 29.076  -16.056  -0.704   1.00 40.98  ? 192 HIS   C CD2    1 
ATOM   8237  C  CE1    . HIS   C 1  192 ? 29.727  -16.844  -2.643   1.00 41.55  ? 192 HIS   C CE1    1 
ATOM   8238  N  NE2    . HIS   C 1  192 ? 30.144  -16.232  -1.551   1.00 41.94  ? 192 HIS   C NE2    1 
ATOM   8239  N  N      . THR   C 1  193 ? 27.190  -19.233  0.724    1.00 37.38  ? 193 THR   C N      1 
ATOM   8240  C  CA     . THR   C 1  193 ? 28.186  -20.166  1.242    1.00 36.53  ? 193 THR   C CA     1 
ATOM   8241  C  C      . THR   C 1  193 ? 27.800  -21.627  1.004    1.00 37.42  ? 193 THR   C C      1 
ATOM   8242  O  O      . THR   C 1  193 ? 28.666  -22.507  0.950    1.00 37.96  ? 193 THR   C O      1 
ATOM   8243  C  CB     . THR   C 1  193 ? 28.385  -19.902  2.736    1.00 35.47  ? 193 THR   C CB     1 
ATOM   8244  O  OG1    . THR   C 1  193 ? 28.894  -18.576  2.926    1.00 40.11  ? 193 THR   C OG1    1 
ATOM   8245  C  CG2    . THR   C 1  193 ? 29.366  -20.888  3.299    1.00 44.11  ? 193 THR   C CG2    1 
ATOM   8246  N  N      . THR   C 1  194 ? 26.515  -21.907  0.885    1.00 36.00  ? 194 THR   C N      1 
ATOM   8247  C  CA     . THR   C 1  194 ? 26.044  -23.266  0.772    1.00 32.60  ? 194 THR   C CA     1 
ATOM   8248  C  C      . THR   C 1  194 ? 25.853  -23.707  -0.666   1.00 34.06  ? 194 THR   C C      1 
ATOM   8249  O  O      . THR   C 1  194 ? 25.814  -24.910  -0.923   1.00 34.36  ? 194 THR   C O      1 
ATOM   8250  C  CB     . THR   C 1  194 ? 24.735  -23.388  1.541    1.00 35.74  ? 194 THR   C CB     1 
ATOM   8251  O  OG1    . THR   C 1  194 ? 25.025  -23.217  2.936    1.00 36.11  ? 194 THR   C OG1    1 
ATOM   8252  C  CG2    . THR   C 1  194 ? 24.072  -24.734  1.295    1.00 35.24  ? 194 THR   C CG2    1 
ATOM   8253  N  N      . LEU   C 1  195 ? 25.775  -22.760  -1.601   1.00 31.36  ? 195 LEU   C N      1 
ATOM   8254  C  CA     . LEU   C 1  195 ? 25.230  -23.040  -2.920   1.00 27.24  ? 195 LEU   C CA     1 
ATOM   8255  C  C      . LEU   C 1  195 ? 26.009  -24.143  -3.625   1.00 35.02  ? 195 LEU   C C      1 
ATOM   8256  O  O      . LEU   C 1  195 ? 25.409  -25.022  -4.254   1.00 39.47  ? 195 LEU   C O      1 
ATOM   8257  C  CB     . LEU   C 1  195 ? 25.212  -21.742  -3.722   1.00 25.68  ? 195 LEU   C CB     1 
ATOM   8258  C  CG     . LEU   C 1  195 ? 24.344  -21.609  -4.970   1.00 33.02  ? 195 LEU   C CG     1 
ATOM   8259  C  CD1    . LEU   C 1  195 ? 22.946  -22.197  -4.773   1.00 31.64  ? 195 LEU   C CD1    1 
ATOM   8260  C  CD2    . LEU   C 1  195 ? 24.254  -20.157  -5.374   1.00 32.17  ? 195 LEU   C CD2    1 
ATOM   8261  N  N      . GLU   C 1  196 ? 27.351  -24.110  -3.521   1.00 38.87  ? 196 GLU   C N      1 
ATOM   8262  C  CA     . GLU   C 1  196 ? 28.267  -25.120  -4.059   1.00 30.40  ? 196 GLU   C CA     1 
ATOM   8263  C  C      . GLU   C 1  196 ? 28.152  -26.464  -3.374   1.00 30.00  ? 196 GLU   C C      1 
ATOM   8264  O  O      . GLU   C 1  196 ? 28.645  -27.461  -3.905   1.00 31.48  ? 196 GLU   C O      1 
ATOM   8265  C  CB     . GLU   C 1  196 ? 29.710  -24.688  -3.848   1.00 38.03  ? 196 GLU   C CB     1 
ATOM   8266  C  CG     . GLU   C 1  196 ? 30.476  -24.207  -5.025   1.00 49.06  ? 196 GLU   C CG     1 
ATOM   8267  C  CD     . GLU   C 1  196 ? 31.757  -23.564  -4.564   1.00 70.52  ? 196 GLU   C CD     1 
ATOM   8268  O  OE1    . GLU   C 1  196 ? 32.511  -23.071  -5.429   1.00 80.49  ? 196 GLU   C OE1    1 
ATOM   8269  O  OE2    . GLU   C 1  196 ? 31.992  -23.536  -3.313   1.00 71.88  ? 196 GLU   C OE2    1 
ATOM   8270  N  N      . HIS   C 1  197 ? 27.618  -26.501  -2.170   1.00 30.01  ? 197 HIS   C N      1 
ATOM   8271  C  CA     . HIS   C 1  197 ? 27.706  -27.685  -1.336   1.00 32.31  ? 197 HIS   C CA     1 
ATOM   8272  C  C      . HIS   C 1  197 ? 26.396  -28.415  -1.200   1.00 36.36  ? 197 HIS   C C      1 
ATOM   8273  O  O      . HIS   C 1  197 ? 26.319  -29.375  -0.432   1.00 37.63  ? 197 HIS   C O      1 
ATOM   8274  C  CB     . HIS   C 1  197 ? 28.229  -27.300  0.039    1.00 31.98  ? 197 HIS   C CB     1 
ATOM   8275  C  CG     . HIS   C 1  197 ? 29.614  -26.772  -0.017   1.00 36.88  ? 197 HIS   C CG     1 
ATOM   8276  N  ND1    . HIS   C 1  197 ? 30.715  -27.597  -0.036   1.00 35.89  ? 197 HIS   C ND1    1 
ATOM   8277  C  CD2    . HIS   C 1  197 ? 30.079  -25.512  -0.147   1.00 36.55  ? 197 HIS   C CD2    1 
ATOM   8278  C  CE1    . HIS   C 1  197 ? 31.802  -26.864  -0.149   1.00 37.03  ? 197 HIS   C CE1    1 
ATOM   8279  N  NE2    . HIS   C 1  197 ? 31.444  -25.595  -0.208   1.00 40.27  ? 197 HIS   C NE2    1 
ATOM   8280  N  N      . SER   C 1  198 ? 25.363  -27.977  -1.903   1.00 31.85  ? 198 SER   C N      1 
ATOM   8281  C  CA     . SER   C 1  198 ? 24.064  -28.581  -1.789   1.00 32.62  ? 198 SER   C CA     1 
ATOM   8282  C  C      . SER   C 1  198 ? 23.608  -28.983  -3.179   1.00 37.86  ? 198 SER   C C      1 
ATOM   8283  O  O      . SER   C 1  198 ? 23.812  -28.237  -4.140   1.00 39.72  ? 198 SER   C O      1 
ATOM   8284  C  CB     . SER   C 1  198 ? 23.089  -27.622  -1.132   1.00 32.58  ? 198 SER   C CB     1 
ATOM   8285  O  OG     . SER   C 1  198 ? 21.845  -28.264  -0.960   1.00 36.95  ? 198 SER   C OG     1 
ATOM   8286  N  N      . ASP   C 1  199 ? 23.037  -30.190  -3.270   1.00 32.69  ? 199 ASP   C N      1 
ATOM   8287  C  CA     . ASP   C 1  199 ? 22.544  -30.794  -4.494   1.00 28.24  ? 199 ASP   C CA     1 
ATOM   8288  C  C      . ASP   C 1  199 ? 21.071  -30.514  -4.760   1.00 33.79  ? 199 ASP   C C      1 
ATOM   8289  O  O      . ASP   C 1  199 ? 20.624  -30.599  -5.914   1.00 37.20  ? 199 ASP   C O      1 
ATOM   8290  C  CB     . ASP   C 1  199 ? 22.729  -32.309  -4.426   1.00 31.52  ? 199 ASP   C CB     1 
ATOM   8291  C  CG     . ASP   C 1  199 ? 24.111  -32.695  -4.086   1.00 33.81  ? 199 ASP   C CG     1 
ATOM   8292  O  OD1    . ASP   C 1  199 ? 24.973  -32.471  -4.932   1.00 41.50  ? 199 ASP   C OD1    1 
ATOM   8293  O  OD2    . ASP   C 1  199 ? 24.353  -33.224  -2.978   1.00 43.55  ? 199 ASP   C OD2    1 
ATOM   8294  N  N      . CYS   C 1  200 ? 20.308  -30.229  -3.721   1.00 35.07  ? 200 CYS   C N      1 
ATOM   8295  C  CA     . CYS   C 1  200 ? 18.880  -30.014  -3.844   1.00 31.89  ? 200 CYS   C CA     1 
ATOM   8296  C  C      . CYS   C 1  200 ? 18.425  -29.316  -2.573   1.00 33.72  ? 200 CYS   C C      1 
ATOM   8297  O  O      . CYS   C 1  200 ? 18.787  -29.740  -1.469   1.00 41.38  ? 200 CYS   C O      1 
ATOM   8298  C  CB     . CYS   C 1  200 ? 18.161  -31.341  -4.058   1.00 35.59  ? 200 CYS   C CB     1 
ATOM   8299  S  SG     . CYS   C 1  200 ? 16.512  -31.119  -4.695   1.00 43.30  ? 200 CYS   C SG     1 
ATOM   8300  N  N      . ALA   C 1  201 ? 17.665  -28.240  -2.700   1.00 30.60  ? 201 ALA   C N      1 
ATOM   8301  C  CA     . ALA   C 1  201 ? 17.198  -27.505  -1.530   1.00 36.72  ? 201 ALA   C CA     1 
ATOM   8302  C  C      . ALA   C 1  201 ? 15.717  -27.178  -1.697   1.00 30.12  ? 201 ALA   C C      1 
ATOM   8303  O  O      . ALA   C 1  201 ? 15.332  -26.479  -2.638   1.00 30.31  ? 201 ALA   C O      1 
ATOM   8304  C  CB     . ALA   C 1  201 ? 18.029  -26.231  -1.330   1.00 35.28  ? 201 ALA   C CB     1 
ATOM   8305  N  N      . PHE   C 1  202 ? 14.885  -27.688  -0.803   1.00 27.71  ? 202 PHE   C N      1 
ATOM   8306  C  CA     . PHE   C 1  202 ? 13.472  -27.340  -0.805   1.00 26.81  ? 202 PHE   C CA     1 
ATOM   8307  C  C      . PHE   C 1  202 ? 13.266  -26.166  0.154    1.00 31.40  ? 202 PHE   C C      1 
ATOM   8308  O  O      . PHE   C 1  202 ? 13.441  -26.314  1.371    1.00 30.68  ? 202 PHE   C O      1 
ATOM   8309  C  CB     . PHE   C 1  202 ? 12.630  -28.550  -0.411   1.00 29.01  ? 202 PHE   C CB     1 
ATOM   8310  C  CG     . PHE   C 1  202 ? 12.895  -29.784  -1.242   1.00 32.10  ? 202 PHE   C CG     1 
ATOM   8311  C  CD1    . PHE   C 1  202 ? 12.261  -29.982  -2.451   1.00 31.26  ? 202 PHE   C CD1    1 
ATOM   8312  C  CD2    . PHE   C 1  202 ? 13.772  -30.760  -0.802   1.00 34.30  ? 202 PHE   C CD2    1 
ATOM   8313  C  CE1    . PHE   C 1  202 ? 12.492  -31.121  -3.188   1.00 28.28  ? 202 PHE   C CE1    1 
ATOM   8314  C  CE2    . PHE   C 1  202 ? 14.013  -31.890  -1.559   1.00 32.36  ? 202 PHE   C CE2    1 
ATOM   8315  C  CZ     . PHE   C 1  202 ? 13.371  -32.058  -2.755   1.00 27.80  ? 202 PHE   C CZ     1 
ATOM   8316  N  N      . MET   C 1  203 ? 12.924  -24.986  -0.382   1.00 28.80  ? 203 MET   C N      1 
ATOM   8317  C  CA     . MET   C 1  203 ? 12.604  -23.846  0.473    1.00 26.76  ? 203 MET   C CA     1 
ATOM   8318  C  C      . MET   C 1  203 ? 11.156  -23.875  0.958    1.00 32.98  ? 203 MET   C C      1 
ATOM   8319  O  O      . MET   C 1  203 ? 10.222  -24.148  0.195    1.00 33.23  ? 203 MET   C O      1 
ATOM   8320  C  CB     . MET   C 1  203 ? 12.863  -22.534  -0.250   1.00 29.59  ? 203 MET   C CB     1 
ATOM   8321  C  CG     . MET   C 1  203 ? 14.321  -22.289  -0.519   1.00 39.31  ? 203 MET   C CG     1 
ATOM   8322  S  SD     . MET   C 1  203 ? 14.609  -20.628  -1.176   1.00 45.61  ? 203 MET   C SD     1 
ATOM   8323  C  CE     . MET   C 1  203 ? 14.551  -20.980  -2.912   1.00 31.18  ? 203 MET   C CE     1 
ATOM   8324  N  N      . VAL   C 1  204 ? 10.973  -23.567  2.234    1.00 33.58  ? 204 VAL   C N      1 
ATOM   8325  C  CA     . VAL   C 1  204 ? 9.654   -23.398  2.835    1.00 34.21  ? 204 VAL   C CA     1 
ATOM   8326  C  C      . VAL   C 1  204 ? 9.525   -21.940  3.226    1.00 36.02  ? 204 VAL   C C      1 
ATOM   8327  O  O      . VAL   C 1  204 ? 10.284  -21.444  4.068    1.00 37.92  ? 204 VAL   C O      1 
ATOM   8328  C  CB     . VAL   C 1  204 ? 9.451   -24.292  4.066    1.00 35.60  ? 204 VAL   C CB     1 
ATOM   8329  C  CG1    . VAL   C 1  204 ? 8.049   -24.095  4.613    1.00 34.60  ? 204 VAL   C CG1    1 
ATOM   8330  C  CG2    . VAL   C 1  204 ? 9.713   -25.752  3.729    1.00 33.97  ? 204 VAL   C CG2    1 
ATOM   8331  N  N      . ASP   C 1  205 ? 8.581   -21.254  2.613    1.00 36.32  ? 205 ASP   C N      1 
ATOM   8332  C  CA     . ASP   C 1  205 ? 8.338   -19.851  2.900    1.00 35.35  ? 205 ASP   C CA     1 
ATOM   8333  C  C      . ASP   C 1  205 ? 7.406   -19.766  4.105    1.00 40.07  ? 205 ASP   C C      1 
ATOM   8334  O  O      . ASP   C 1  205 ? 6.236   -20.176  4.030    1.00 35.72  ? 205 ASP   C O      1 
ATOM   8335  C  CB     . ASP   C 1  205 ? 7.745   -19.173  1.669    1.00 29.29  ? 205 ASP   C CB     1 
ATOM   8336  C  CG     . ASP   C 1  205 ? 7.471   -17.713  1.876    1.00 35.76  ? 205 ASP   C CG     1 
ATOM   8337  O  OD1    . ASP   C 1  205 ? 7.653   -17.202  3.004    1.00 35.48  ? 205 ASP   C OD1    1 
ATOM   8338  O  OD2    . ASP   C 1  205 ? 7.087   -17.061  0.874    1.00 43.71  ? 205 ASP   C OD2    1 
ATOM   8339  N  N      . ASN   C 1  206 ? 7.920   -19.231  5.215    1.00 34.32  ? 206 ASN   C N      1 
ATOM   8340  C  CA     . ASN   C 1  206 ? 7.102   -19.143  6.415    1.00 35.45  ? 206 ASN   C CA     1 
ATOM   8341  C  C      . ASN   C 1  206 ? 5.786   -18.420  6.169    1.00 39.19  ? 206 ASN   C C      1 
ATOM   8342  O  O      . ASN   C 1  206 ? 4.774   -18.754  6.795    1.00 35.54  ? 206 ASN   C O      1 
ATOM   8343  C  CB     . ASN   C 1  206 ? 7.881   -18.478  7.535    1.00 30.85  ? 206 ASN   C CB     1 
ATOM   8344  C  CG     . ASN   C 1  206 ? 8.399   -19.490  8.513    1.00 27.78  ? 206 ASN   C CG     1 
ATOM   8345  O  OD1    . ASN   C 1  206 ? 8.050   -20.670  8.426    1.00 29.46  ? 206 ASN   C OD1    1 
ATOM   8346  N  ND2    . ASN   C 1  206 ? 9.255   -19.064  9.416    1.00 28.81  ? 206 ASN   C ND2    1 
ATOM   8347  N  N      . GLU   C 1  207 ? 5.760   -17.448  5.257    1.00 39.63  ? 207 GLU   C N      1 
ATOM   8348  C  CA     . GLU   C 1  207 ? 4.500   -16.770  4.988    1.00 40.62  ? 207 GLU   C CA     1 
ATOM   8349  C  C      . GLU   C 1  207 ? 3.562   -17.658  4.178    1.00 42.21  ? 207 GLU   C C      1 
ATOM   8350  O  O      . GLU   C 1  207 ? 2.348   -17.663  4.416    1.00 37.43  ? 207 GLU   C O      1 
ATOM   8351  C  CB     . GLU   C 1  207 ? 4.766   -15.453  4.282    1.00 39.70  ? 207 GLU   C CB     1 
ATOM   8352  C  CG     . GLU   C 1  207 ? 3.635   -14.485  4.324    1.00 40.85  ? 207 GLU   C CG     1 
ATOM   8353  C  CD     . GLU   C 1  207 ? 3.967   -13.287  3.510    1.00 46.61  ? 207 GLU   C CD     1 
ATOM   8354  O  OE1    . GLU   C 1  207 ? 5.035   -12.709  3.773    1.00 51.49  ? 207 GLU   C OE1    1 
ATOM   8355  O  OE2    . GLU   C 1  207 ? 3.209   -12.942  2.585    1.00 51.10  ? 207 GLU   C OE2    1 
ATOM   8356  N  N      . ALA   C 1  208 ? 4.102   -18.429  3.230    1.00 37.27  ? 208 ALA   C N      1 
ATOM   8357  C  CA     . ALA   C 1  208 ? 3.279   -19.413  2.535    1.00 33.23  ? 208 ALA   C CA     1 
ATOM   8358  C  C      . ALA   C 1  208 ? 2.616   -20.354  3.529    1.00 36.69  ? 208 ALA   C C      1 
ATOM   8359  O  O      . ALA   C 1  208 ? 1.393   -20.538  3.520    1.00 38.48  ? 208 ALA   C O      1 
ATOM   8360  C  CB     . ALA   C 1  208 ? 4.126   -20.201  1.533    1.00 32.76  ? 208 ALA   C CB     1 
ATOM   8361  N  N      . ILE   C 1  209 ? 3.424   -20.970  4.394    1.00 38.40  ? 209 ILE   C N      1 
ATOM   8362  C  CA     . ILE   C 1  209 ? 2.905   -21.892  5.394    1.00 34.49  ? 209 ILE   C CA     1 
ATOM   8363  C  C      . ILE   C 1  209 ? 1.920   -21.178  6.318    1.00 38.43  ? 209 ILE   C C      1 
ATOM   8364  O  O      . ILE   C 1  209 ? 0.863   -21.724  6.665    1.00 38.04  ? 209 ILE   C O      1 
ATOM   8365  C  CB     . ILE   C 1  209 ? 4.080   -22.533  6.167    1.00 32.78  ? 209 ILE   C CB     1 
ATOM   8366  C  CG1    . ILE   C 1  209 ? 4.896   -23.399  5.230    1.00 30.86  ? 209 ILE   C CG1    1 
ATOM   8367  C  CG2    . ILE   C 1  209 ? 3.600   -23.446  7.249    1.00 37.01  ? 209 ILE   C CG2    1 
ATOM   8368  C  CD1    . ILE   C 1  209 ? 4.093   -23.962  4.141    1.00 34.75  ? 209 ILE   C CD1    1 
ATOM   8369  N  N      . TYR   C 1  210 ? 2.240   -19.940  6.714    1.00 36.09  ? 210 TYR   C N      1 
ATOM   8370  C  CA     . TYR   C 1  210 ? 1.383   -19.200  7.636    1.00 36.10  ? 210 TYR   C CA     1 
ATOM   8371  C  C      . TYR   C 1  210 ? 0.019   -18.924  7.026    1.00 42.66  ? 210 TYR   C C      1 
ATOM   8372  O  O      . TYR   C 1  210 ? -1.005  -19.060  7.704    1.00 44.31  ? 210 TYR   C O      1 
ATOM   8373  C  CB     . TYR   C 1  210 ? 2.051   -17.894  8.018    1.00 36.64  ? 210 TYR   C CB     1 
ATOM   8374  C  CG     . TYR   C 1  210 ? 1.443   -17.135  9.155    1.00 35.35  ? 210 TYR   C CG     1 
ATOM   8375  C  CD1    . TYR   C 1  210 ? 1.820   -17.388  10.471   1.00 42.68  ? 210 TYR   C CD1    1 
ATOM   8376  C  CD2    . TYR   C 1  210 ? 0.549   -16.109  8.914    1.00 39.91  ? 210 TYR   C CD2    1 
ATOM   8377  C  CE1    . TYR   C 1  210 ? 1.264   -16.666  11.525   1.00 49.76  ? 210 TYR   C CE1    1 
ATOM   8378  C  CE2    . TYR   C 1  210 ? -0.008  -15.381  9.947    1.00 43.38  ? 210 TYR   C CE2    1 
ATOM   8379  C  CZ     . TYR   C 1  210 ? 0.343   -15.657  11.245   1.00 48.79  ? 210 TYR   C CZ     1 
ATOM   8380  O  OH     . TYR   C 1  210 ? -0.212  -14.913  12.255   1.00 48.18  ? 210 TYR   C OH     1 
ATOM   8381  N  N      . ASP   C 1  211 ? -0.012  -18.526  5.748    1.00 39.89  ? 211 ASP   C N      1 
ATOM   8382  C  CA     . ASP   C 1  211 ? -1.273  -18.242  5.072    1.00 36.52  ? 211 ASP   C CA     1 
ATOM   8383  C  C      . ASP   C 1  211 ? -2.108  -19.508  4.904    1.00 41.29  ? 211 ASP   C C      1 
ATOM   8384  O  O      . ASP   C 1  211 ? -3.311  -19.509  5.192    1.00 45.24  ? 211 ASP   C O      1 
ATOM   8385  C  CB     . ASP   C 1  211 ? -1.003  -17.585  3.715    1.00 41.71  ? 211 ASP   C CB     1 
ATOM   8386  C  CG     . ASP   C 1  211 ? -0.524  -16.136  3.841    1.00 44.65  ? 211 ASP   C CG     1 
ATOM   8387  O  OD1    . ASP   C 1  211 ? -0.595  -15.583  4.969    1.00 44.80  ? 211 ASP   C OD1    1 
ATOM   8388  O  OD2    . ASP   C 1  211 ? -0.073  -15.552  2.819    1.00 43.81  ? 211 ASP   C OD2    1 
ATOM   8389  N  N      . ILE   C 1  212 ? -1.494  -20.601  4.442    1.00 39.60  ? 212 ILE   C N      1 
ATOM   8390  C  CA     . ILE   C 1  212 ? -2.229  -21.865  4.318    1.00 43.83  ? 212 ILE   C CA     1 
ATOM   8391  C  C      . ILE   C 1  212 ? -2.881  -22.229  5.652    1.00 38.28  ? 212 ILE   C C      1 
ATOM   8392  O  O      . ILE   C 1  212 ? -4.051  -22.623  5.710    1.00 40.81  ? 212 ILE   C O      1 
ATOM   8393  C  CB     . ILE   C 1  212 ? -1.292  -22.986  3.814    1.00 38.89  ? 212 ILE   C CB     1 
ATOM   8394  C  CG1    . ILE   C 1  212 ? -0.784  -22.692  2.403    1.00 35.80  ? 212 ILE   C CG1    1 
ATOM   8395  C  CG2    . ILE   C 1  212 ? -1.975  -24.328  3.881    1.00 28.66  ? 212 ILE   C CG2    1 
ATOM   8396  C  CD1    . ILE   C 1  212 ? 0.420   -23.552  2.001    1.00 32.35  ? 212 ILE   C CD1    1 
ATOM   8397  N  N      . CYS   C 1  213 ? -2.135  -22.092  6.742    1.00 37.93  ? 213 CYS   C N      1 
ATOM   8398  C  CA     . CYS   C 1  213 ? -2.680  -22.374  8.064    1.00 43.54  ? 213 CYS   C CA     1 
ATOM   8399  C  C      . CYS   C 1  213 ? -3.878  -21.487  8.376    1.00 45.15  ? 213 CYS   C C      1 
ATOM   8400  O  O      . CYS   C 1  213 ? -4.912  -21.968  8.852    1.00 48.45  ? 213 CYS   C O      1 
ATOM   8401  C  CB     . CYS   C 1  213 ? -1.603  -22.178  9.122    1.00 38.05  ? 213 CYS   C CB     1 
ATOM   8402  S  SG     . CYS   C 1  213 ? -0.642  -23.627  9.391    1.00 47.68  ? 213 CYS   C SG     1 
ATOM   8403  N  N      . ARG   C 1  214 ? -3.737  -20.176  8.162    1.00 38.75  ? 214 ARG   C N      1 
ATOM   8404  C  CA     . ARG   C 1  214 ? -4.824  -19.264  8.472    1.00 43.86  ? 214 ARG   C CA     1 
ATOM   8405  C  C      . ARG   C 1  214 ? -6.044  -19.573  7.622    1.00 47.81  ? 214 ARG   C C      1 
ATOM   8406  O  O      . ARG   C 1  214 ? -7.182  -19.513  8.101    1.00 51.01  ? 214 ARG   C O      1 
ATOM   8407  C  CB     . ARG   C 1  214 ? -4.378  -17.821  8.255    1.00 43.20  ? 214 ARG   C CB     1 
ATOM   8408  C  CG     . ARG   C 1  214 ? -3.837  -17.141  9.482    1.00 46.97  ? 214 ARG   C CG     1 
ATOM   8409  C  CD     . ARG   C 1  214 ? -3.806  -15.621  9.312    1.00 50.27  ? 214 ARG   C CD     1 
ATOM   8410  N  NE     . ARG   C 1  214 ? -3.200  -15.230  8.043    1.00 53.99  ? 214 ARG   C NE     1 
ATOM   8411  C  CZ     . ARG   C 1  214 ? -2.471  -14.134  7.864    1.00 60.25  ? 214 ARG   C CZ     1 
ATOM   8412  N  NH1    . ARG   C 1  214 ? -2.208  -13.307  8.870    1.00 56.97  ? 214 ARG   C NH1    1 
ATOM   8413  N  NH2    . ARG   C 1  214 ? -1.990  -13.860  6.649    1.00 45.12  ? 214 ARG   C NH2    1 
ATOM   8414  N  N      . ARG   C 1  215 ? -5.822  -19.940  6.368    1.00 44.19  ? 215 ARG   C N      1 
ATOM   8415  C  CA     . ARG   C 1  215 ? -6.871  -19.977  5.366    1.00 46.14  ? 215 ARG   C CA     1 
ATOM   8416  C  C      . ARG   C 1  215 ? -7.492  -21.366  5.195    1.00 51.19  ? 215 ARG   C C      1 
ATOM   8417  O  O      . ARG   C 1  215 ? -8.706  -21.469  4.975    1.00 52.13  ? 215 ARG   C O      1 
ATOM   8418  C  CB     . ARG   C 1  215 ? -6.306  -19.436  4.037    1.00 36.72  ? 215 ARG   C CB     1 
ATOM   8419  C  CG     . ARG   C 1  215 ? -7.213  -19.552  2.844    1.00 44.87  ? 215 ARG   C CG     1 
ATOM   8420  C  CD     . ARG   C 1  215 ? -6.456  -19.873  1.520    1.00 63.07  ? 215 ARG   C CD     1 
ATOM   8421  N  NE     . ARG   C 1  215 ? -5.344  -18.960  1.238    1.00 71.79  ? 215 ARG   C NE     1 
ATOM   8422  C  CZ     . ARG   C 1  215 ? -4.077  -19.328  1.047    1.00 62.17  ? 215 ARG   C CZ     1 
ATOM   8423  N  NH1    . ARG   C 1  215 ? -3.718  -20.609  1.012    1.00 50.32  ? 215 ARG   C NH1    1 
ATOM   8424  N  NH2    . ARG   C 1  215 ? -3.144  -18.386  0.894    1.00 52.22  ? 215 ARG   C NH2    1 
ATOM   8425  N  N      . ASN   C 1  216 ? -6.722  -22.453  5.302    1.00 42.94  ? 216 ASN   C N      1 
ATOM   8426  C  CA     . ASN   C 1  216 ? -7.328  -23.752  5.059    1.00 39.71  ? 216 ASN   C CA     1 
ATOM   8427  C  C      . ASN   C 1  216 ? -7.551  -24.536  6.340    1.00 44.24  ? 216 ASN   C C      1 
ATOM   8428  O  O      . ASN   C 1  216 ? -8.233  -25.570  6.312    1.00 46.01  ? 216 ASN   C O      1 
ATOM   8429  C  CB     . ASN   C 1  216 ? -6.476  -24.604  4.089    1.00 39.99  ? 216 ASN   C CB     1 
ATOM   8430  C  CG     . ASN   C 1  216 ? -6.189  -23.909  2.767    1.00 37.58  ? 216 ASN   C CG     1 
ATOM   8431  O  OD1    . ASN   C 1  216 ? -5.152  -24.116  2.190    1.00 50.51  ? 216 ASN   C OD1    1 
ATOM   8432  N  ND2    . ASN   C 1  216 ? -7.084  -23.067  2.310    1.00 42.93  ? 216 ASN   C ND2    1 
ATOM   8433  N  N      . LEU   C 1  217 ? -6.970  -24.102  7.448    1.00 42.18  ? 217 LEU   C N      1 
ATOM   8434  C  CA     . LEU   C 1  217 ? -7.144  -24.807  8.700    1.00 44.24  ? 217 LEU   C CA     1 
ATOM   8435  C  C      . LEU   C 1  217 ? -7.850  -23.942  9.727    1.00 45.95  ? 217 LEU   C C      1 
ATOM   8436  O  O      . LEU   C 1  217 ? -8.120  -24.415  10.840   1.00 45.25  ? 217 LEU   C O      1 
ATOM   8437  C  CB     . LEU   C 1  217 ? -5.785  -25.298  9.225    1.00 46.82  ? 217 LEU   C CB     1 
ATOM   8438  C  CG     . LEU   C 1  217 ? -5.118  -26.410  8.418    1.00 41.79  ? 217 LEU   C CG     1 
ATOM   8439  C  CD1    . LEU   C 1  217 ? -3.714  -26.695  8.896    1.00 40.03  ? 217 LEU   C CD1    1 
ATOM   8440  C  CD2    . LEU   C 1  217 ? -5.952  -27.641  8.539    1.00 45.81  ? 217 LEU   C CD2    1 
ATOM   8441  N  N      . ASP   C 1  218 ? -8.168  -22.697  9.360    1.00 47.15  ? 218 ASP   C N      1 
ATOM   8442  C  CA     . ASP   C 1  218 ? -8.857  -21.717  10.201   1.00 48.93  ? 218 ASP   C CA     1 
ATOM   8443  C  C      . ASP   C 1  218 ? -8.184  -21.517  11.557   1.00 52.03  ? 218 ASP   C C      1 
ATOM   8444  O  O      . ASP   C 1  218 ? -8.847  -21.406  12.583   1.00 53.40  ? 218 ASP   C O      1 
ATOM   8445  C  CB     . ASP   C 1  218 ? -10.327 -22.079  10.380   1.00 52.05  ? 218 ASP   C CB     1 
ATOM   8446  C  CG     . ASP   C 1  218 ? -11.217 -20.848  10.450   1.00 74.88  ? 218 ASP   C CG     1 
ATOM   8447  O  OD1    . ASP   C 1  218 ? -11.930 -20.674  11.485   1.00 74.60  ? 218 ASP   C OD1    1 
ATOM   8448  O  OD2    . ASP   C 1  218 ? -11.185 -20.048  9.479    1.00 76.81  ? 218 ASP   C OD2    1 
ATOM   8449  N  N      . ILE   C 1  219 ? -6.852  -21.428  11.555   1.00 52.24  ? 219 ILE   C N      1 
ATOM   8450  C  CA     . ILE   C 1  219 ? -6.085  -21.067  12.747   1.00 48.12  ? 219 ILE   C CA     1 
ATOM   8451  C  C      . ILE   C 1  219 ? -5.843  -19.566  12.728   1.00 48.53  ? 219 ILE   C C      1 
ATOM   8452  O  O      . ILE   C 1  219 ? -5.252  -19.044  11.775   1.00 48.12  ? 219 ILE   C O      1 
ATOM   8453  C  CB     . ILE   C 1  219 ? -4.757  -21.832  12.815   1.00 53.81  ? 219 ILE   C CB     1 
ATOM   8454  C  CG1    . ILE   C 1  219 ? -5.024  -23.347  12.813   1.00 58.19  ? 219 ILE   C CG1    1 
ATOM   8455  C  CG2    . ILE   C 1  219 ? -3.933  -21.379  14.028   1.00 46.63  ? 219 ILE   C CG2    1 
ATOM   8456  C  CD1    . ILE   C 1  219 ? -3.896  -24.192  12.181   1.00 55.92  ? 219 ILE   C CD1    1 
ATOM   8457  N  N      . GLU   C 1  220 ? -6.287  -18.870  13.783   1.00 50.81  ? 220 GLU   C N      1 
ATOM   8458  C  CA     . GLU   C 1  220 ? -6.255  -17.404  13.784   1.00 58.65  ? 220 GLU   C CA     1 
ATOM   8459  C  C      . GLU   C 1  220 ? -4.829  -16.864  13.756   1.00 54.76  ? 220 GLU   C C      1 
ATOM   8460  O  O      . GLU   C 1  220 ? -4.477  -16.056  12.886   1.00 51.27  ? 220 GLU   C O      1 
ATOM   8461  C  CB     . GLU   C 1  220 ? -6.993  -16.847  15.000   1.00 59.15  ? 220 GLU   C CB     1 
ATOM   8462  C  CG     . GLU   C 1  220 ? -8.414  -17.315  15.142   1.00 72.83  ? 220 GLU   C CG     1 
ATOM   8463  C  CD     . GLU   C 1  220 ? -9.341  -16.191  15.587   1.00 88.42  ? 220 GLU   C CD     1 
ATOM   8464  O  OE1    . GLU   C 1  220 ? -8.828  -15.169  16.108   1.00 90.45  ? 220 GLU   C OE1    1 
ATOM   8465  O  OE2    . GLU   C 1  220 ? -10.580 -16.337  15.404   1.00 92.12  ? 220 GLU   C OE2    1 
ATOM   8466  N  N      . ARG   C 1  221 ? -4.007  -17.257  14.733   1.00 49.51  ? 221 ARG   C N      1 
ATOM   8467  C  CA     . ARG   C 1  221 ? -2.612  -16.821  14.823   1.00 56.91  ? 221 ARG   C CA     1 
ATOM   8468  C  C      . ARG   C 1  221 ? -1.728  -18.054  14.935   1.00 53.21  ? 221 ARG   C C      1 
ATOM   8469  O  O      . ARG   C 1  221 ? -1.238  -18.390  16.022   1.00 50.14  ? 221 ARG   C O      1 
ATOM   8470  C  CB     . ARG   C 1  221 ? -2.382  -15.859  15.987   1.00 52.83  ? 221 ARG   C CB     1 
ATOM   8471  C  CG     . ARG   C 1  221 ? -1.457  -14.712  15.644   1.00 59.41  ? 221 ARG   C CG     1 
ATOM   8472  C  CD     . ARG   C 1  221 ? -0.035  -14.996  16.073   1.00 66.76  ? 221 ARG   C CD     1 
ATOM   8473  N  NE     . ARG   C 1  221 ? 0.056   -15.193  17.521   1.00 82.87  ? 221 ARG   C NE     1 
ATOM   8474  C  CZ     . ARG   C 1  221 ? 0.437   -14.271  18.401   1.00 82.17  ? 221 ARG   C CZ     1 
ATOM   8475  N  NH1    . ARG   C 1  221 ? 0.720   -13.031  18.031   1.00 75.48  ? 221 ARG   C NH1    1 
ATOM   8476  N  NH2    . ARG   C 1  221 ? 0.544   -14.605  19.688   1.00 78.34  ? 221 ARG   C NH2    1 
ATOM   8477  N  N      . PRO   C 1  222 ? -1.447  -18.708  13.807   1.00 52.33  ? 222 PRO   C N      1 
ATOM   8478  C  CA     . PRO   C 1  222 ? -0.774  -20.016  13.847   1.00 47.54  ? 222 PRO   C CA     1 
ATOM   8479  C  C      . PRO   C 1  222 ? 0.577   -19.933  14.528   1.00 41.10  ? 222 PRO   C C      1 
ATOM   8480  O  O      . PRO   C 1  222 ? 1.288   -18.936  14.433   1.00 43.95  ? 222 PRO   C O      1 
ATOM   8481  C  CB     . PRO   C 1  222 ? -0.623  -20.389  12.363   1.00 50.29  ? 222 PRO   C CB     1 
ATOM   8482  C  CG     . PRO   C 1  222 ? -1.472  -19.361  11.596   1.00 49.60  ? 222 PRO   C CG     1 
ATOM   8483  C  CD     . PRO   C 1  222 ? -1.507  -18.139  12.448   1.00 42.57  ? 222 PRO   C CD     1 
ATOM   8484  N  N      . THR   C 1  223 ? 0.929   -21.002  15.213   1.00 45.15  ? 223 THR   C N      1 
ATOM   8485  C  CA     . THR   C 1  223 ? 2.168   -21.088  15.967   1.00 47.91  ? 223 THR   C CA     1 
ATOM   8486  C  C      . THR   C 1  223 ? 3.239   -21.836  15.171   1.00 43.18  ? 223 THR   C C      1 
ATOM   8487  O  O      . THR   C 1  223 ? 3.009   -22.325  14.064   1.00 41.03  ? 223 THR   C O      1 
ATOM   8488  C  CB     . THR   C 1  223 ? 1.915   -21.806  17.287   1.00 50.58  ? 223 THR   C CB     1 
ATOM   8489  O  OG1    . THR   C 1  223 ? 1.213   -23.028  16.999   1.00 47.38  ? 223 THR   C OG1    1 
ATOM   8490  C  CG2    . THR   C 1  223 ? 1.109   -20.931  18.228   1.00 40.75  ? 223 THR   C CG2    1 
ATOM   8491  N  N      . TYR   C 1  224 ? 4.434   -21.946  15.761   1.00 44.55  ? 224 TYR   C N      1 
ATOM   8492  C  CA     . TYR   C 1  224 ? 5.430   -22.840  15.188   1.00 37.47  ? 224 TYR   C CA     1 
ATOM   8493  C  C      . TYR   C 1  224 ? 4.940   -24.281  15.221   1.00 42.82  ? 224 TYR   C C      1 
ATOM   8494  O  O      . TYR   C 1  224 ? 5.253   -25.066  14.323   1.00 42.24  ? 224 TYR   C O      1 
ATOM   8495  C  CB     . TYR   C 1  224 ? 6.741   -22.726  15.940   1.00 36.47  ? 224 TYR   C CB     1 
ATOM   8496  C  CG     . TYR   C 1  224 ? 7.507   -21.450  15.739   1.00 36.31  ? 224 TYR   C CG     1 
ATOM   8497  C  CD1    . TYR   C 1  224 ? 7.566   -20.819  14.499   1.00 32.58  ? 224 TYR   C CD1    1 
ATOM   8498  C  CD2    . TYR   C 1  224 ? 8.220   -20.903  16.788   1.00 35.86  ? 224 TYR   C CD2    1 
ATOM   8499  C  CE1    . TYR   C 1  224 ? 8.317   -19.658  14.337   1.00 28.73  ? 224 TYR   C CE1    1 
ATOM   8500  C  CE2    . TYR   C 1  224 ? 8.945   -19.756  16.637   1.00 35.59  ? 224 TYR   C CE2    1 
ATOM   8501  C  CZ     . TYR   C 1  224 ? 8.991   -19.140  15.419   1.00 31.20  ? 224 TYR   C CZ     1 
ATOM   8502  O  OH     . TYR   C 1  224 ? 9.713   -17.989  15.331   1.00 36.43  ? 224 TYR   C OH     1 
ATOM   8503  N  N      . THR   C 1  225 ? 4.153   -24.651  16.233   1.00 44.97  ? 225 THR   C N      1 
ATOM   8504  C  CA     . THR   C 1  225 ? 3.592   -25.996  16.222   1.00 44.05  ? 225 THR   C CA     1 
ATOM   8505  C  C      . THR   C 1  225 ? 2.605   -26.183  15.080   1.00 49.02  ? 225 THR   C C      1 
ATOM   8506  O  O      . THR   C 1  225 ? 2.579   -27.251  14.457   1.00 47.72  ? 225 THR   C O      1 
ATOM   8507  C  CB     . THR   C 1  225 ? 2.919   -26.304  17.543   1.00 47.19  ? 225 THR   C CB     1 
ATOM   8508  O  OG1    . THR   C 1  225 ? 3.877   -26.122  18.593   1.00 58.33  ? 225 THR   C OG1    1 
ATOM   8509  C  CG2    . THR   C 1  225 ? 2.421   -27.747  17.529   1.00 48.00  ? 225 THR   C CG2    1 
ATOM   8510  N  N      . ASN   C 1  226 ? 1.780   -25.163  14.796   1.00 45.04  ? 226 ASN   C N      1 
ATOM   8511  C  CA     . ASN   C 1  226 ? 0.876   -25.236  13.651   1.00 38.50  ? 226 ASN   C CA     1 
ATOM   8512  C  C      . ASN   C 1  226 ? 1.650   -25.403  12.351   1.00 38.82  ? 226 ASN   C C      1 
ATOM   8513  O  O      . ASN   C 1  226 ? 1.346   -26.293  11.548   1.00 34.08  ? 226 ASN   C O      1 
ATOM   8514  C  CB     . ASN   C 1  226 ? -0.004  -23.988  13.575   1.00 45.73  ? 226 ASN   C CB     1 
ATOM   8515  C  CG     . ASN   C 1  226 ? -0.977  -23.880  14.734   1.00 46.81  ? 226 ASN   C CG     1 
ATOM   8516  O  OD1    . ASN   C 1  226 ? -1.123  -22.818  15.345   1.00 46.58  ? 226 ASN   C OD1    1 
ATOM   8517  N  ND2    . ASN   C 1  226 ? -1.636  -24.977  15.045   1.00 37.47  ? 226 ASN   C ND2    1 
ATOM   8518  N  N      . LEU   C 1  227 ? 2.666   -24.552  12.131   1.00 40.87  ? 227 LEU   C N      1 
ATOM   8519  C  CA     . LEU   C 1  227 ? 3.420   -24.593  10.875   1.00 37.00  ? 227 LEU   C CA     1 
ATOM   8520  C  C      . LEU   C 1  227 ? 4.229   -25.872  10.745   1.00 37.97  ? 227 LEU   C C      1 
ATOM   8521  O  O      . LEU   C 1  227 ? 4.309   -26.451  9.652    1.00 36.31  ? 227 LEU   C O      1 
ATOM   8522  C  CB     . LEU   C 1  227 ? 4.346   -23.388  10.747   1.00 28.43  ? 227 LEU   C CB     1 
ATOM   8523  C  CG     . LEU   C 1  227 ? 3.739   -21.995  10.926   1.00 33.52  ? 227 LEU   C CG     1 
ATOM   8524  C  CD1    . LEU   C 1  227 ? 4.828   -20.960  10.905   1.00 33.59  ? 227 LEU   C CD1    1 
ATOM   8525  C  CD2    . LEU   C 1  227 ? 2.704   -21.676  9.858    1.00 33.93  ? 227 LEU   C CD2    1 
ATOM   8526  N  N      . ASN   C 1  228 ? 4.839   -26.328  11.843   1.00 36.28  ? 228 ASN   C N      1 
ATOM   8527  C  CA     . ASN   C 1  228 ? 5.702   -27.497  11.755   1.00 35.22  ? 228 ASN   C CA     1 
ATOM   8528  C  C      . ASN   C 1  228 ? 4.905   -28.732  11.372   1.00 37.46  ? 228 ASN   C C      1 
ATOM   8529  O  O      . ASN   C 1  228 ? 5.333   -29.520  10.522   1.00 40.03  ? 228 ASN   C O      1 
ATOM   8530  C  CB     . ASN   C 1  228 ? 6.449   -27.707  13.070   1.00 38.75  ? 228 ASN   C CB     1 
ATOM   8531  C  CG     . ASN   C 1  228 ? 7.503   -26.630  13.328   1.00 39.68  ? 228 ASN   C CG     1 
ATOM   8532  O  OD1    . ASN   C 1  228 ? 7.823   -25.828  12.441   1.00 36.30  ? 228 ASN   C OD1    1 
ATOM   8533  N  ND2    . ASN   C 1  228 ? 8.032   -26.598  14.555   1.00 35.66  ? 228 ASN   C ND2    1 
ATOM   8534  N  N      . ARG   C 1  229 ? 3.729   -28.906  11.960   1.00 40.90  ? 229 ARG   C N      1 
ATOM   8535  C  CA     . ARG   C 1  229 ? 2.916   -30.065  11.621   1.00 39.77  ? 229 ARG   C CA     1 
ATOM   8536  C  C      . ARG   C 1  229 ? 2.481   -30.053  10.161   1.00 37.27  ? 229 ARG   C C      1 
ATOM   8537  O  O      . ARG   C 1  229 ? 2.208   -31.116  9.598    1.00 40.89  ? 229 ARG   C O      1 
ATOM   8538  C  CB     . ARG   C 1  229 ? 1.706   -30.137  12.546   1.00 43.06  ? 229 ARG   C CB     1 
ATOM   8539  C  CG     . ARG   C 1  229 ? 2.042   -30.331  14.019   1.00 46.71  ? 229 ARG   C CG     1 
ATOM   8540  C  CD     . ARG   C 1  229 ? 0.912   -31.090  14.678   1.00 55.51  ? 229 ARG   C CD     1 
ATOM   8541  N  NE     . ARG   C 1  229 ? 0.976   -31.123  16.133   1.00 62.59  ? 229 ARG   C NE     1 
ATOM   8542  C  CZ     . ARG   C 1  229 ? 0.065   -30.553  16.911   1.00 70.66  ? 229 ARG   C CZ     1 
ATOM   8543  N  NH1    . ARG   C 1  229 ? -0.900  -29.787  16.402   1.00 55.04  ? 229 ARG   C NH1    1 
ATOM   8544  N  NH2    . ARG   C 1  229 ? 0.123   -30.751  18.228   1.00 74.04  ? 229 ARG   C NH2    1 
ATOM   8545  N  N      . LEU   C 1  230 ? 2.434   -28.889  9.520    1.00 38.05  ? 230 LEU   C N      1 
ATOM   8546  C  CA     . LEU   C 1  230 ? 2.165   -28.881  8.084    1.00 36.75  ? 230 LEU   C CA     1 
ATOM   8547  C  C      . LEU   C 1  230 ? 3.441   -29.152  7.277    1.00 38.06  ? 230 LEU   C C      1 
ATOM   8548  O  O      . LEU   C 1  230 ? 3.410   -29.899  6.297    1.00 35.70  ? 230 LEU   C O      1 
ATOM   8549  C  CB     . LEU   C 1  230 ? 1.508   -27.551  7.692    1.00 33.19  ? 230 LEU   C CB     1 
ATOM   8550  C  CG     . LEU   C 1  230 ? 1.201   -27.217  6.218    1.00 41.04  ? 230 LEU   C CG     1 
ATOM   8551  C  CD1    . LEU   C 1  230 ? 0.568   -28.387  5.437    1.00 32.42  ? 230 LEU   C CD1    1 
ATOM   8552  C  CD2    . LEU   C 1  230 ? 0.315   -25.975  6.144    1.00 40.71  ? 230 LEU   C CD2    1 
ATOM   8553  N  N      . ILE   C 1  231 ? 4.577   -28.572  7.685    1.00 40.91  ? 231 ILE   C N      1 
ATOM   8554  C  CA     . ILE   C 1  231 ? 5.835   -28.817  6.981    1.00 38.84  ? 231 ILE   C CA     1 
ATOM   8555  C  C      . ILE   C 1  231 ? 6.186   -30.300  6.995    1.00 40.08  ? 231 ILE   C C      1 
ATOM   8556  O  O      . ILE   C 1  231 ? 6.631   -30.861  5.987    1.00 41.84  ? 231 ILE   C O      1 
ATOM   8557  C  CB     . ILE   C 1  231 ? 6.955   -27.961  7.595    1.00 35.00  ? 231 ILE   C CB     1 
ATOM   8558  C  CG1    . ILE   C 1  231 ? 6.500   -26.515  7.599    1.00 34.51  ? 231 ILE   C CG1    1 
ATOM   8559  C  CG2    . ILE   C 1  231 ? 8.269   -28.102  6.827    1.00 30.14  ? 231 ILE   C CG2    1 
ATOM   8560  C  CD1    . ILE   C 1  231 ? 7.554   -25.593  7.996    1.00 31.40  ? 231 ILE   C CD1    1 
ATOM   8561  N  N      . SER   C 1  232 ? 5.986   -30.966  8.123    1.00 37.39  ? 232 SER   C N      1 
ATOM   8562  C  CA     . SER   C 1  232 ? 6.403   -32.357  8.188    1.00 40.58  ? 232 SER   C CA     1 
ATOM   8563  C  C      . SER   C 1  232 ? 5.577   -33.237  7.255    1.00 42.50  ? 232 SER   C C      1 
ATOM   8564  O  O      . SER   C 1  232 ? 6.055   -34.289  6.805    1.00 40.97  ? 232 SER   C O      1 
ATOM   8565  C  CB     . SER   C 1  232 ? 6.307   -32.824  9.627    1.00 42.77  ? 232 SER   C CB     1 
ATOM   8566  O  OG     . SER   C 1  232 ? 5.280   -32.071  10.240   1.00 49.15  ? 232 SER   C OG     1 
ATOM   8567  N  N      . GLN   C 1  233 ? 4.338   -32.836  6.967    1.00 38.23  ? 233 GLN   C N      1 
ATOM   8568  C  CA     . GLN   C 1  233 ? 3.558   -33.544  5.970    1.00 34.04  ? 233 GLN   C CA     1 
ATOM   8569  C  C      . GLN   C 1  233 ? 4.229   -33.448  4.610    1.00 39.90  ? 233 GLN   C C      1 
ATOM   8570  O  O      . GLN   C 1  233 ? 4.374   -34.449  3.900    1.00 40.13  ? 233 GLN   C O      1 
ATOM   8571  C  CB     . GLN   C 1  233 ? 2.134   -32.981  5.936    1.00 42.00  ? 233 GLN   C CB     1 
ATOM   8572  C  CG     . GLN   C 1  233 ? 1.273   -33.436  7.094    1.00 39.46  ? 233 GLN   C CG     1 
ATOM   8573  C  CD     . GLN   C 1  233 ? 1.193   -34.933  7.112    1.00 40.16  ? 233 GLN   C CD     1 
ATOM   8574  O  OE1    . GLN   C 1  233 ? 1.221   -35.567  6.061    1.00 51.83  ? 233 GLN   C OE1    1 
ATOM   8575  N  NE2    . GLN   C 1  233 ? 1.112   -35.508  8.278    1.00 34.63  ? 233 GLN   C NE2    1 
ATOM   8576  N  N      . ILE   C 1  234 ? 4.672   -32.247  4.238    1.00 38.54  ? 234 ILE   C N      1 
ATOM   8577  C  CA     . ILE   C 1  234 ? 5.370   -32.086  2.969    1.00 38.89  ? 234 ILE   C CA     1 
ATOM   8578  C  C      . ILE   C 1  234 ? 6.718   -32.805  2.995    1.00 41.99  ? 234 ILE   C C      1 
ATOM   8579  O  O      . ILE   C 1  234 ? 7.119   -33.433  2.004    1.00 43.57  ? 234 ILE   C O      1 
ATOM   8580  C  CB     . ILE   C 1  234 ? 5.505   -30.588  2.642    1.00 37.54  ? 234 ILE   C CB     1 
ATOM   8581  C  CG1    . ILE   C 1  234 ? 4.110   -30.003  2.426    1.00 41.23  ? 234 ILE   C CG1    1 
ATOM   8582  C  CG2    . ILE   C 1  234 ? 6.372   -30.382  1.427    1.00 33.16  ? 234 ILE   C CG2    1 
ATOM   8583  C  CD1    . ILE   C 1  234 ? 3.750   -28.901  3.367    1.00 41.57  ? 234 ILE   C CD1    1 
ATOM   8584  N  N      . VAL   C 1  235 ? 7.447   -32.718  4.115    1.00 36.94  ? 235 VAL   C N      1 
ATOM   8585  C  CA     . VAL   C 1  235 ? 8.687   -33.480  4.228    1.00 38.82  ? 235 VAL   C CA     1 
ATOM   8586  C  C      . VAL   C 1  235 ? 8.395   -34.971  4.147    1.00 40.43  ? 235 VAL   C C      1 
ATOM   8587  O  O      . VAL   C 1  235 ? 9.072   -35.725  3.440    1.00 39.58  ? 235 VAL   C O      1 
ATOM   8588  C  CB     . VAL   C 1  235 ? 9.413   -33.137  5.535    1.00 39.69  ? 235 VAL   C CB     1 
ATOM   8589  C  CG1    . VAL   C 1  235 ? 10.546  -34.133  5.771    1.00 34.89  ? 235 VAL   C CG1    1 
ATOM   8590  C  CG2    . VAL   C 1  235 ? 9.893   -31.698  5.524    1.00 35.22  ? 235 VAL   C CG2    1 
ATOM   8591  N  N      . SER   C 1  236 ? 7.386   -35.425  4.876    1.00 41.87  ? 236 SER   C N      1 
ATOM   8592  C  CA     . SER   C 1  236 ? 7.023   -36.836  4.807    1.00 42.56  ? 236 SER   C CA     1 
ATOM   8593  C  C      . SER   C 1  236 ? 6.817   -37.286  3.359    1.00 38.27  ? 236 SER   C C      1 
ATOM   8594  O  O      . SER   C 1  236 ? 7.348   -38.317  2.942    1.00 41.10  ? 236 SER   C O      1 
ATOM   8595  C  CB     . SER   C 1  236 ? 5.777   -37.087  5.661    1.00 38.35  ? 236 SER   C CB     1 
ATOM   8596  O  OG     . SER   C 1  236 ? 5.411   -38.446  5.600    1.00 42.74  ? 236 SER   C OG     1 
ATOM   8597  N  N      . SER   C 1  237 ? 6.062   -36.511  2.572    1.00 37.86  ? 237 SER   C N      1 
ATOM   8598  C  CA     . SER   C 1  237 ? 5.772   -36.899  1.190    1.00 36.89  ? 237 SER   C CA     1 
ATOM   8599  C  C      . SER   C 1  237 ? 7.038   -36.948  0.346    1.00 38.42  ? 237 SER   C C      1 
ATOM   8600  O  O      . SER   C 1  237 ? 7.207   -37.844  -0.483   1.00 39.21  ? 237 SER   C O      1 
ATOM   8601  C  CB     . SER   C 1  237 ? 4.764   -35.929  0.562    1.00 39.64  ? 237 SER   C CB     1 
ATOM   8602  O  OG     . SER   C 1  237 ? 3.582   -35.845  1.353    1.00 47.07  ? 237 SER   C OG     1 
ATOM   8603  N  N      . ILE   C 1  238 ? 7.934   -35.981  0.527    1.00 37.31  ? 238 ILE   C N      1 
ATOM   8604  C  CA     . ILE   C 1  238 ? 9.165   -35.994  -0.243   1.00 37.61  ? 238 ILE   C CA     1 
ATOM   8605  C  C      . ILE   C 1  238 ? 10.052  -37.186  0.125    1.00 36.88  ? 238 ILE   C C      1 
ATOM   8606  O  O      . ILE   C 1  238 ? 10.737  -37.738  -0.745   1.00 38.00  ? 238 ILE   C O      1 
ATOM   8607  C  CB     . ILE   C 1  238 ? 9.879   -34.643  -0.075   1.00 37.00  ? 238 ILE   C CB     1 
ATOM   8608  C  CG1    . ILE   C 1  238 ? 9.104   -33.556  -0.843   1.00 40.80  ? 238 ILE   C CG1    1 
ATOM   8609  C  CG2    . ILE   C 1  238 ? 11.290  -34.731  -0.562   1.00 33.20  ? 238 ILE   C CG2    1 
ATOM   8610  C  CD1    . ILE   C 1  238 ? 9.390   -32.103  -0.360   1.00 41.87  ? 238 ILE   C CD1    1 
ATOM   8611  N  N      . THR   C 1  239 ? 10.041  -37.632  1.386    1.00 34.08  ? 239 THR   C N      1 
ATOM   8612  C  CA     . THR   C 1  239 ? 10.880  -38.760  1.780    1.00 39.55  ? 239 THR   C CA     1 
ATOM   8613  C  C      . THR   C 1  239 ? 10.140  -40.088  1.795    1.00 39.26  ? 239 THR   C C      1 
ATOM   8614  O  O      . THR   C 1  239 ? 10.768  -41.116  2.037    1.00 42.46  ? 239 THR   C O      1 
ATOM   8615  C  CB     . THR   C 1  239 ? 11.525  -38.547  3.164    1.00 37.83  ? 239 THR   C CB     1 
ATOM   8616  O  OG1    . THR   C 1  239 ? 10.513  -38.421  4.165    1.00 42.32  ? 239 THR   C OG1    1 
ATOM   8617  C  CG2    . THR   C 1  239 ? 12.418  -37.320  3.201    1.00 34.27  ? 239 THR   C CG2    1 
ATOM   8618  N  N      . ALA   C 1  240 ? 8.835   -40.100  1.548    1.00 37.87  ? 240 ALA   C N      1 
ATOM   8619  C  CA     . ALA   C 1  240 ? 8.100   -41.356  1.630    1.00 42.16  ? 240 ALA   C CA     1 
ATOM   8620  C  C      . ALA   C 1  240 ? 8.601   -42.364  0.617    1.00 41.59  ? 240 ALA   C C      1 
ATOM   8621  O  O      . ALA   C 1  240 ? 8.564   -43.569  0.882    1.00 45.34  ? 240 ALA   C O      1 
ATOM   8622  C  CB     . ALA   C 1  240 ? 6.599   -41.126  1.432    1.00 46.21  ? 240 ALA   C CB     1 
ATOM   8623  N  N      . SER   C 1  241 ? 9.045   -41.897  -0.552   1.00 42.81  ? 241 SER   C N      1 
ATOM   8624  C  CA     . SER   C 1  241 ? 9.698   -42.773  -1.526   1.00 46.22  ? 241 SER   C CA     1 
ATOM   8625  C  C      . SER   C 1  241 ? 10.919  -43.489  -0.941   1.00 46.53  ? 241 SER   C C      1 
ATOM   8626  O  O      . SER   C 1  241 ? 11.171  -44.652  -1.271   1.00 49.54  ? 241 SER   C O      1 
ATOM   8627  C  CB     . SER   C 1  241 ? 10.076  -41.952  -2.758   1.00 55.05  ? 241 SER   C CB     1 
ATOM   8628  O  OG     . SER   C 1  241 ? 10.272  -40.578  -2.415   1.00 57.76  ? 241 SER   C OG     1 
ATOM   8629  N  N      . LEU   C 1  242 ? 11.674  -42.825  -0.064   1.00 45.32  ? 242 LEU   C N      1 
ATOM   8630  C  CA     . LEU   C 1  242 ? 12.805  -43.463  0.606    1.00 41.33  ? 242 LEU   C CA     1 
ATOM   8631  C  C      . LEU   C 1  242 ? 12.370  -44.459  1.678    1.00 44.01  ? 242 LEU   C C      1 
ATOM   8632  O  O      . LEU   C 1  242 ? 12.965  -45.533  1.816    1.00 45.90  ? 242 LEU   C O      1 
ATOM   8633  C  CB     . LEU   C 1  242 ? 13.678  -42.393  1.246    1.00 44.26  ? 242 LEU   C CB     1 
ATOM   8634  C  CG     . LEU   C 1  242 ? 14.228  -41.407  0.231    1.00 48.42  ? 242 LEU   C CG     1 
ATOM   8635  C  CD1    . LEU   C 1  242 ? 15.119  -40.370  0.906    1.00 33.22  ? 242 LEU   C CD1    1 
ATOM   8636  C  CD2    . LEU   C 1  242 ? 14.967  -42.207  -0.844   1.00 51.81  ? 242 LEU   C CD2    1 
ATOM   8637  N  N      . ARG   C 1  243 ? 11.367  -44.114  2.470    1.00 43.18  ? 243 ARG   C N      1 
ATOM   8638  C  CA     . ARG   C 1  243 ? 11.013  -44.907  3.635    1.00 43.93  ? 243 ARG   C CA     1 
ATOM   8639  C  C      . ARG   C 1  243 ? 10.071  -46.065  3.333    1.00 45.31  ? 243 ARG   C C      1 
ATOM   8640  O  O      . ARG   C 1  243 ? 9.871   -46.914  4.204    1.00 47.77  ? 243 ARG   C O      1 
ATOM   8641  C  CB     . ARG   C 1  243 ? 10.379  -43.999  4.689    1.00 41.99  ? 243 ARG   C CB     1 
ATOM   8642  C  CG     . ARG   C 1  243 ? 11.282  -42.857  5.117    1.00 38.01  ? 243 ARG   C CG     1 
ATOM   8643  C  CD     . ARG   C 1  243 ? 10.623  -42.014  6.174    1.00 39.95  ? 243 ARG   C CD     1 
ATOM   8644  N  NE     . ARG   C 1  243 ? 9.673   -41.068  5.592    1.00 44.78  ? 243 ARG   C NE     1 
ATOM   8645  C  CZ     . ARG   C 1  243 ? 8.355   -41.148  5.727    1.00 39.22  ? 243 ARG   C CZ     1 
ATOM   8646  N  NH1    . ARG   C 1  243 ? 7.792   -42.124  6.412    1.00 39.73  ? 243 ARG   C NH1    1 
ATOM   8647  N  NH2    . ARG   C 1  243 ? 7.587   -40.224  5.163    1.00 40.80  ? 243 ARG   C NH2    1 
ATOM   8648  N  N      . PHE   C 1  244 ? 9.479   -46.116  2.142    1.00 48.89  ? 244 PHE   C N      1 
ATOM   8649  C  CA     . PHE   C 1  244 ? 8.454   -47.098  1.817    1.00 48.44  ? 244 PHE   C CA     1 
ATOM   8650  C  C      . PHE   C 1  244 ? 8.802   -47.816  0.527    1.00 51.51  ? 244 PHE   C C      1 
ATOM   8651  O  O      . PHE   C 1  244 ? 9.430   -47.253  -0.373   1.00 53.29  ? 244 PHE   C O      1 
ATOM   8652  C  CB     . PHE   C 1  244 ? 7.074   -46.458  1.650    1.00 45.42  ? 244 PHE   C CB     1 
ATOM   8653  C  CG     . PHE   C 1  244 ? 6.490   -45.962  2.914    1.00 44.49  ? 244 PHE   C CG     1 
ATOM   8654  C  CD1    . PHE   C 1  244 ? 5.954   -46.840  3.839    1.00 48.71  ? 244 PHE   C CD1    1 
ATOM   8655  C  CD2    . PHE   C 1  244 ? 6.498   -44.612  3.203    1.00 40.54  ? 244 PHE   C CD2    1 
ATOM   8656  C  CE1    . PHE   C 1  244 ? 5.407   -46.375  5.030    1.00 43.26  ? 244 PHE   C CE1    1 
ATOM   8657  C  CE2    . PHE   C 1  244 ? 5.953   -44.143  4.386    1.00 40.62  ? 244 PHE   C CE2    1 
ATOM   8658  C  CZ     . PHE   C 1  244 ? 5.411   -45.025  5.302    1.00 41.45  ? 244 PHE   C CZ     1 
ATOM   8659  N  N      . ASP   C 1  245 ? 8.384   -49.069  0.459    1.00 51.61  ? 245 ASP   C N      1 
ATOM   8660  C  CA     . ASP   C 1  245 ? 8.414   -49.840  -0.766   1.00 61.87  ? 245 ASP   C CA     1 
ATOM   8661  C  C      . ASP   C 1  245 ? 7.180   -49.512  -1.610   1.00 67.87  ? 245 ASP   C C      1 
ATOM   8662  O  O      . ASP   C 1  245 ? 6.273   -48.786  -1.184   1.00 70.28  ? 245 ASP   C O      1 
ATOM   8663  C  CB     . ASP   C 1  245 ? 8.485   -51.327  -0.424   1.00 68.48  ? 245 ASP   C CB     1 
ATOM   8664  C  CG     . ASP   C 1  245 ? 9.891   -51.762  -0.007   1.00 86.43  ? 245 ASP   C CG     1 
ATOM   8665  O  OD1    . ASP   C 1  245 ? 10.872  -51.084  -0.403   1.00 87.38  ? 245 ASP   C OD1    1 
ATOM   8666  O  OD2    . ASP   C 1  245 ? 10.011  -52.744  0.773    1.00 91.35  ? 245 ASP   C OD2    1 
ATOM   8667  N  N      . GLY   C 1  246 ? 7.147   -50.052  -2.822   1.00 65.85  ? 246 GLY   C N      1 
ATOM   8668  C  CA     . GLY   C 1  246 ? 6.005   -49.823  -3.679   1.00 60.68  ? 246 GLY   C CA     1 
ATOM   8669  C  C      . GLY   C 1  246 ? 6.253   -50.047  -5.156   1.00 62.17  ? 246 GLY   C C      1 
ATOM   8670  O  O      . GLY   C 1  246 ? 7.192   -49.490  -5.735   1.00 56.22  ? 246 GLY   C O      1 
ATOM   8671  N  N      . ALA   C 1  247 ? 5.395   -50.866  -5.772   1.00 61.31  ? 247 ALA   C N      1 
ATOM   8672  C  CA     . ALA   C 1  247 ? 5.444   -51.080  -7.212   1.00 57.58  ? 247 ALA   C CA     1 
ATOM   8673  C  C      . ALA   C 1  247 ? 5.608   -49.754  -7.958   1.00 65.49  ? 247 ALA   C C      1 
ATOM   8674  O  O      . ALA   C 1  247 ? 6.628   -49.510  -8.622   1.00 61.52  ? 247 ALA   C O      1 
ATOM   8675  C  CB     . ALA   C 1  247 ? 4.175   -51.813  -7.657   1.00 53.10  ? 247 ALA   C CB     1 
ATOM   8676  N  N      . LEU   C 1  248 ? 4.605   -48.870  -7.832   1.00 63.20  ? 248 LEU   C N      1 
ATOM   8677  C  CA     . LEU   C 1  248 ? 4.559   -47.577  -8.505   1.00 58.64  ? 248 LEU   C CA     1 
ATOM   8678  C  C      . LEU   C 1  248 ? 5.320   -46.507  -7.789   1.00 54.52  ? 248 LEU   C C      1 
ATOM   8679  O  O      . LEU   C 1  248 ? 5.077   -45.318  -8.040   1.00 53.93  ? 248 LEU   C O      1 
ATOM   8680  C  CB     . LEU   C 1  248 ? 3.113   -47.115  -8.676   1.00 58.63  ? 248 LEU   C CB     1 
ATOM   8681  C  CG     . LEU   C 1  248 ? 2.198   -48.066  -9.429   1.00 59.92  ? 248 LEU   C CG     1 
ATOM   8682  C  CD1    . LEU   C 1  248 ? 0.903   -48.062  -8.728   1.00 50.95  ? 248 LEU   C CD1    1 
ATOM   8683  C  CD2    . LEU   C 1  248 ? 2.038   -47.591  -10.871  1.00 60.07  ? 248 LEU   C CD2    1 
ATOM   8684  N  N      . ASN   C 1  249 ? 6.216   -46.885  -6.896   1.00 55.47  ? 249 ASN   C N      1 
ATOM   8685  C  CA     . ASN   C 1  249 ? 6.947   -45.920  -6.102   1.00 55.44  ? 249 ASN   C CA     1 
ATOM   8686  C  C      . ASN   C 1  249 ? 8.261   -45.582  -6.798   1.00 59.26  ? 249 ASN   C C      1 
ATOM   8687  O  O      . ASN   C 1  249 ? 8.911   -46.448  -7.390   1.00 65.73  ? 249 ASN   C O      1 
ATOM   8688  C  CB     . ASN   C 1  249 ? 7.167   -46.476  -4.694   1.00 57.20  ? 249 ASN   C CB     1 
ATOM   8689  C  CG     . ASN   C 1  249 ? 7.984   -45.564  -3.838   1.00 61.32  ? 249 ASN   C CG     1 
ATOM   8690  O  OD1    . ASN   C 1  249 ? 7.550   -44.461  -3.500   1.00 60.13  ? 249 ASN   C OD1    1 
ATOM   8691  N  ND2    . ASN   C 1  249 ? 9.172   -46.026  -3.447   1.00 61.73  ? 249 ASN   C ND2    1 
ATOM   8692  N  N      . VAL   C 1  250 ? 8.642   -44.315  -6.728   1.00 57.18  ? 250 VAL   C N      1 
ATOM   8693  C  CA     . VAL   C 1  250 ? 9.738   -43.759  -7.509   1.00 53.50  ? 250 VAL   C CA     1 
ATOM   8694  C  C      . VAL   C 1  250 ? 10.741  -43.107  -6.562   1.00 53.36  ? 250 VAL   C C      1 
ATOM   8695  O  O      . VAL   C 1  250 ? 10.369  -42.262  -5.737   1.00 52.63  ? 250 VAL   C O      1 
ATOM   8696  C  CB     . VAL   C 1  250 ? 9.188   -42.762  -8.542   1.00 46.70  ? 250 VAL   C CB     1 
ATOM   8697  C  CG1    . VAL   C 1  250 ? 10.280  -41.921  -9.156   1.00 43.92  ? 250 VAL   C CG1    1 
ATOM   8698  C  CG2    . VAL   C 1  250 ? 8.430   -43.527  -9.572   1.00 45.51  ? 250 VAL   C CG2    1 
ATOM   8699  N  N      . ASP   C 1  251 ? 12.007  -43.506  -6.676   1.00 54.95  ? 251 ASP   C N      1 
ATOM   8700  C  CA     . ASP   C 1  251 ? 13.023  -43.005  -5.758   1.00 56.10  ? 251 ASP   C CA     1 
ATOM   8701  C  C      . ASP   C 1  251 ? 13.127  -41.490  -5.853   1.00 56.08  ? 251 ASP   C C      1 
ATOM   8702  O  O      . ASP   C 1  251 ? 13.062  -40.913  -6.942   1.00 53.44  ? 251 ASP   C O      1 
ATOM   8703  C  CB     . ASP   C 1  251 ? 14.394  -43.630  -6.045   1.00 51.15  ? 251 ASP   C CB     1 
ATOM   8704  C  CG     . ASP   C 1  251 ? 15.160  -43.945  -4.768   1.00 68.16  ? 251 ASP   C CG     1 
ATOM   8705  O  OD1    . ASP   C 1  251 ? 14.524  -44.480  -3.820   1.00 67.67  ? 251 ASP   C OD1    1 
ATOM   8706  O  OD2    . ASP   C 1  251 ? 16.375  -43.619  -4.688   1.00 71.65  ? 251 ASP   C OD2    1 
ATOM   8707  N  N      . LEU   C 1  252 ? 13.285  -40.841  -4.699   1.00 52.94  ? 252 LEU   C N      1 
ATOM   8708  C  CA     . LEU   C 1  252 ? 13.567  -39.413  -4.714   1.00 51.62  ? 252 LEU   C CA     1 
ATOM   8709  C  C      . LEU   C 1  252 ? 14.689  -39.081  -5.690   1.00 52.22  ? 252 LEU   C C      1 
ATOM   8710  O  O      . LEU   C 1  252 ? 14.568  -38.159  -6.501   1.00 52.81  ? 252 LEU   C O      1 
ATOM   8711  C  CB     . LEU   C 1  252 ? 13.914  -38.941  -3.305   1.00 49.67  ? 252 LEU   C CB     1 
ATOM   8712  C  CG     . LEU   C 1  252 ? 14.249  -37.465  -3.137   1.00 46.92  ? 252 LEU   C CG     1 
ATOM   8713  C  CD1    . LEU   C 1  252 ? 13.507  -36.545  -4.096   1.00 33.89  ? 252 LEU   C CD1    1 
ATOM   8714  C  CD2    . LEU   C 1  252 ? 13.970  -37.093  -1.690   1.00 51.82  ? 252 LEU   C CD2    1 
ATOM   8715  N  N      . THR   C 1  253 ? 15.790  -39.828  -5.632   1.00 56.80  ? 253 THR   C N      1 
ATOM   8716  C  CA     . THR   C 1  253 ? 16.940  -39.536  -6.484   1.00 53.73  ? 253 THR   C CA     1 
ATOM   8717  C  C      . THR   C 1  253 ? 16.558  -39.519  -7.964   1.00 50.52  ? 253 THR   C C      1 
ATOM   8718  O  O      . THR   C 1  253 ? 17.149  -38.783  -8.766   1.00 50.52  ? 253 THR   C O      1 
ATOM   8719  C  CB     . THR   C 1  253 ? 18.023  -40.575  -6.207   1.00 53.65  ? 253 THR   C CB     1 
ATOM   8720  O  OG1    . THR   C 1  253 ? 17.477  -41.881  -6.425   1.00 60.78  ? 253 THR   C OG1    1 
ATOM   8721  C  CG2    . THR   C 1  253 ? 18.459  -40.498  -4.763   1.00 46.41  ? 253 THR   C CG2    1 
ATOM   8722  N  N      . GLU   C 1  254 ? 15.571  -40.315  -8.347   1.00 46.50  ? 254 GLU   C N      1 
ATOM   8723  C  CA     . GLU   C 1  254 ? 15.126  -40.291  -9.734   1.00 48.46  ? 254 GLU   C CA     1 
ATOM   8724  C  C      . GLU   C 1  254 ? 14.398  -38.988  -10.067  1.00 45.89  ? 254 GLU   C C      1 
ATOM   8725  O  O      . GLU   C 1  254 ? 14.554  -38.439  -11.165  1.00 46.15  ? 254 GLU   C O      1 
ATOM   8726  C  CB     . GLU   C 1  254 ? 14.237  -41.496  -9.993   1.00 41.12  ? 254 GLU   C CB     1 
ATOM   8727  C  CG     . GLU   C 1  254 ? 14.073  -41.848  -11.417  1.00 37.53  ? 254 GLU   C CG     1 
ATOM   8728  C  CD     . GLU   C 1  254 ? 13.555  -43.235  -11.539  1.00 50.37  ? 254 GLU   C CD     1 
ATOM   8729  O  OE1    . GLU   C 1  254 ? 14.216  -44.138  -10.969  1.00 52.58  ? 254 GLU   C OE1    1 
ATOM   8730  O  OE2    . GLU   C 1  254 ? 12.478  -43.419  -12.160  1.00 50.37  ? 254 GLU   C OE2    1 
ATOM   8731  N  N      . PHE   C 1  255 ? 13.574  -38.493  -9.146   1.00 44.86  ? 255 PHE   C N      1 
ATOM   8732  C  CA     . PHE   C 1  255 ? 13.039  -37.151  -9.312   1.00 42.91  ? 255 PHE   C CA     1 
ATOM   8733  C  C      . PHE   C 1  255 ? 14.150  -36.100  -9.375   1.00 45.35  ? 255 PHE   C C      1 
ATOM   8734  O  O      . PHE   C 1  255 ? 14.003  -35.106  -10.099  1.00 45.45  ? 255 PHE   C O      1 
ATOM   8735  C  CB     . PHE   C 1  255 ? 12.070  -36.821  -8.176   1.00 47.87  ? 255 PHE   C CB     1 
ATOM   8736  C  CG     . PHE   C 1  255 ? 10.800  -37.609  -8.214   1.00 47.43  ? 255 PHE   C CG     1 
ATOM   8737  C  CD1    . PHE   C 1  255 ? 9.875   -37.415  -9.232   1.00 41.46  ? 255 PHE   C CD1    1 
ATOM   8738  C  CD2    . PHE   C 1  255 ? 10.519  -38.534  -7.221   1.00 47.61  ? 255 PHE   C CD2    1 
ATOM   8739  C  CE1    . PHE   C 1  255 ? 8.696   -38.134  -9.249   1.00 42.31  ? 255 PHE   C CE1    1 
ATOM   8740  C  CE2    . PHE   C 1  255 ? 9.341   -39.273  -7.242   1.00 45.59  ? 255 PHE   C CE2    1 
ATOM   8741  C  CZ     . PHE   C 1  255 ? 8.432   -39.070  -8.250   1.00 43.55  ? 255 PHE   C CZ     1 
ATOM   8742  N  N      . GLN   C 1  256 ? 15.265  -36.276  -8.631   1.00 38.82  ? 256 GLN   C N      1 
ATOM   8743  C  CA     . GLN   C 1  256 ? 16.323  -35.265  -8.728   1.00 43.08  ? 256 GLN   C CA     1 
ATOM   8744  C  C      . GLN   C 1  256 ? 16.944  -35.204  -10.111  1.00 42.68  ? 256 GLN   C C      1 
ATOM   8745  O  O      . GLN   C 1  256 ? 17.405  -34.130  -10.514  1.00 40.68  ? 256 GLN   C O      1 
ATOM   8746  C  CB     . GLN   C 1  256 ? 17.457  -35.467  -7.733   1.00 42.95  ? 256 GLN   C CB     1 
ATOM   8747  C  CG     . GLN   C 1  256 ? 17.123  -35.139  -6.307   1.00 50.08  ? 256 GLN   C CG     1 
ATOM   8748  C  CD     . GLN   C 1  256 ? 18.144  -35.764  -5.378   1.00 60.46  ? 256 GLN   C CD     1 
ATOM   8749  O  OE1    . GLN   C 1  256 ? 17.796  -36.623  -4.582   1.00 64.84  ? 256 GLN   C OE1    1 
ATOM   8750  N  NE2    . GLN   C 1  256 ? 19.418  -35.352  -5.487   1.00 59.03  ? 256 GLN   C NE2    1 
ATOM   8751  N  N      . THR   C 1  257 ? 17.038  -36.337  -10.823  1.00 41.60  ? 257 THR   C N      1 
ATOM   8752  C  CA     . THR   C 1  257 ? 17.542  -36.267  -12.191  1.00 38.44  ? 257 THR   C CA     1 
ATOM   8753  C  C      . THR   C 1  257 ? 16.810  -35.183  -12.950  1.00 37.63  ? 257 THR   C C      1 
ATOM   8754  O  O      . THR   C 1  257 ? 17.423  -34.377  -13.662  1.00 37.46  ? 257 THR   C O      1 
ATOM   8755  C  CB     . THR   C 1  257 ? 17.372  -37.598  -12.925  1.00 42.54  ? 257 THR   C CB     1 
ATOM   8756  O  OG1    . THR   C 1  257 ? 17.854  -38.686  -12.118  1.00 45.68  ? 257 THR   C OG1    1 
ATOM   8757  C  CG2    . THR   C 1  257 ? 18.121  -37.552  -14.268  1.00 26.96  ? 257 THR   C CG2    1 
ATOM   8758  N  N      . ASN   C 1  258 ? 15.479  -35.149  -12.783  1.00 41.43  ? 258 ASN   C N      1 
ATOM   8759  C  CA     . ASN   C 1  258 ? 14.608  -34.225  -13.505  1.00 38.32  ? 258 ASN   C CA     1 
ATOM   8760  C  C      . ASN   C 1  258 ? 14.629  -32.822  -12.921  1.00 39.71  ? 258 ASN   C C      1 
ATOM   8761  O  O      . ASN   C 1  258 ? 14.452  -31.846  -13.671  1.00 39.67  ? 258 ASN   C O      1 
ATOM   8762  C  CB     . ASN   C 1  258 ? 13.170  -34.737  -13.494  1.00 37.40  ? 258 ASN   C CB     1 
ATOM   8763  C  CG     . ASN   C 1  258 ? 12.909  -35.871  -14.512  1.00 46.58  ? 258 ASN   C CG     1 
ATOM   8764  O  OD1    . ASN   C 1  258 ? 13.816  -36.390  -15.174  1.00 43.22  ? 258 ASN   C OD1    1 
ATOM   8765  N  ND2    . ASN   C 1  258 ? 11.637  -36.231  -14.649  1.00 52.90  ? 258 ASN   C ND2    1 
ATOM   8766  N  N      . LEU   C 1  259 ? 14.866  -32.697  -11.605  1.00 33.05  ? 259 LEU   C N      1 
ATOM   8767  C  CA     . LEU   C 1  259 ? 14.644  -31.425  -10.935  1.00 32.92  ? 259 LEU   C CA     1 
ATOM   8768  C  C      . LEU   C 1  259 ? 15.798  -30.457  -11.078  1.00 31.55  ? 259 LEU   C C      1 
ATOM   8769  O  O      . LEU   C 1  259 ? 15.584  -29.249  -10.980  1.00 36.93  ? 259 LEU   C O      1 
ATOM   8770  C  CB     . LEU   C 1  259 ? 14.383  -31.659  -9.461   1.00 37.35  ? 259 LEU   C CB     1 
ATOM   8771  C  CG     . LEU   C 1  259 ? 12.994  -32.228  -9.180   1.00 37.47  ? 259 LEU   C CG     1 
ATOM   8772  C  CD1    . LEU   C 1  259 ? 13.049  -32.769  -7.769   1.00 31.15  ? 259 LEU   C CD1    1 
ATOM   8773  C  CD2    . LEU   C 1  259 ? 11.889  -31.170  -9.399   1.00 26.34  ? 259 LEU   C CD2    1 
ATOM   8774  N  N      . VAL   C 1  260 ? 17.001  -30.950  -11.325  1.00 31.14  ? 260 VAL   C N      1 
ATOM   8775  C  CA     . VAL   C 1  260 ? 18.190  -30.109  -11.378  1.00 30.09  ? 260 VAL   C CA     1 
ATOM   8776  C  C      . VAL   C 1  260 ? 18.751  -30.099  -12.797  1.00 31.78  ? 260 VAL   C C      1 
ATOM   8777  O  O      . VAL   C 1  260 ? 19.529  -30.987  -13.159  1.00 31.26  ? 260 VAL   C O      1 
ATOM   8778  C  CB     . VAL   C 1  260 ? 19.236  -30.602  -10.368  1.00 30.40  ? 260 VAL   C CB     1 
ATOM   8779  C  CG1    . VAL   C 1  260 ? 20.362  -29.604  -10.241  1.00 27.02  ? 260 VAL   C CG1    1 
ATOM   8780  C  CG2    . VAL   C 1  260 ? 18.571  -30.848  -9.026   1.00 29.66  ? 260 VAL   C CG2    1 
ATOM   8781  N  N      . PRO   C 1  261 ? 18.416  -29.132  -13.619  1.00 28.78  ? 261 PRO   C N      1 
ATOM   8782  C  CA     . PRO   C 1  261 ? 18.964  -29.112  -14.974  1.00 26.63  ? 261 PRO   C CA     1 
ATOM   8783  C  C      . PRO   C 1  261 ? 20.379  -28.566  -15.018  1.00 29.45  ? 261 PRO   C C      1 
ATOM   8784  O  O      . PRO   C 1  261 ? 21.121  -28.845  -15.957  1.00 32.23  ? 261 PRO   C O      1 
ATOM   8785  C  CB     . PRO   C 1  261 ? 18.010  -28.174  -15.718  1.00 29.66  ? 261 PRO   C CB     1 
ATOM   8786  C  CG     . PRO   C 1  261 ? 17.610  -27.170  -14.683  1.00 29.16  ? 261 PRO   C CG     1 
ATOM   8787  C  CD     . PRO   C 1  261 ? 17.561  -27.962  -13.354  1.00 33.75  ? 261 PRO   C CD     1 
ATOM   8788  N  N      . TYR   C 1  262 ? 20.738  -27.708  -14.076  1.00 29.63  ? 262 TYR   C N      1 
ATOM   8789  C  CA     . TYR   C 1  262 ? 22.117  -27.278  -13.918  1.00 26.32  ? 262 TYR   C CA     1 
ATOM   8790  C  C      . TYR   C 1  262 ? 22.442  -27.265  -12.436  1.00 29.91  ? 262 TYR   C C      1 
ATOM   8791  O  O      . TYR   C 1  262 ? 21.541  -27.170  -11.593  1.00 32.11  ? 262 TYR   C O      1 
ATOM   8792  C  CB     . TYR   C 1  262 ? 22.371  -25.900  -14.535  1.00 23.23  ? 262 TYR   C CB     1 
ATOM   8793  C  CG     . TYR   C 1  262 ? 21.893  -25.765  -15.953  1.00 30.36  ? 262 TYR   C CG     1 
ATOM   8794  C  CD1    . TYR   C 1  262 ? 20.555  -25.450  -16.240  1.00 38.19  ? 262 TYR   C CD1    1 
ATOM   8795  C  CD2    . TYR   C 1  262 ? 22.758  -25.940  -17.015  1.00 22.89  ? 262 TYR   C CD2    1 
ATOM   8796  C  CE1    . TYR   C 1  262 ? 20.107  -25.321  -17.549  1.00 28.40  ? 262 TYR   C CE1    1 
ATOM   8797  C  CE2    . TYR   C 1  262 ? 22.320  -25.816  -18.309  1.00 23.91  ? 262 TYR   C CE2    1 
ATOM   8798  C  CZ     . TYR   C 1  262 ? 21.012  -25.502  -18.565  1.00 30.71  ? 262 TYR   C CZ     1 
ATOM   8799  O  OH     . TYR   C 1  262 ? 20.607  -25.376  -19.851  1.00 36.60  ? 262 TYR   C OH     1 
ATOM   8800  N  N      . PRO   C 1  263 ? 23.715  -27.363  -12.080  1.00 34.98  ? 263 PRO   C N      1 
ATOM   8801  C  CA     . PRO   C 1  263 ? 24.035  -27.444  -10.631  1.00 28.49  ? 263 PRO   C CA     1 
ATOM   8802  C  C      . PRO   C 1  263 ? 23.376  -26.351  -9.812   1.00 26.65  ? 263 PRO   C C      1 
ATOM   8803  O  O      . PRO   C 1  263 ? 22.727  -26.675  -8.813   1.00 31.17  ? 263 PRO   C O      1 
ATOM   8804  C  CB     . PRO   C 1  263 ? 25.555  -27.409  -10.612  1.00 18.72  ? 263 PRO   C CB     1 
ATOM   8805  C  CG     . PRO   C 1  263 ? 25.913  -28.108  -11.969  1.00 23.37  ? 263 PRO   C CG     1 
ATOM   8806  C  CD     . PRO   C 1  263 ? 24.876  -27.622  -12.949  1.00 24.18  ? 263 PRO   C CD     1 
ATOM   8807  N  N      . ARG   C 1  264 ? 23.458  -25.077  -10.224  1.00 29.08  ? 264 ARG   C N      1 
ATOM   8808  C  CA     . ARG   C 1  264 ? 22.885  -24.006  -9.399   1.00 30.45  ? 264 ARG   C CA     1 
ATOM   8809  C  C      . ARG   C 1  264 ? 21.353  -23.945  -9.450   1.00 35.62  ? 264 ARG   C C      1 
ATOM   8810  O  O      . ARG   C 1  264 ? 20.740  -23.441  -8.504   1.00 31.59  ? 264 ARG   C O      1 
ATOM   8811  C  CB     . ARG   C 1  264 ? 23.460  -22.647  -9.800   1.00 29.16  ? 264 ARG   C CB     1 
ATOM   8812  C  CG     . ARG   C 1  264 ? 24.912  -22.434  -9.400   1.00 25.35  ? 264 ARG   C CG     1 
ATOM   8813  C  CD     . ARG   C 1  264 ? 25.541  -21.414  -10.269  1.00 16.14  ? 264 ARG   C CD     1 
ATOM   8814  N  NE     . ARG   C 1  264 ? 24.989  -20.079  -10.054  1.00 29.67  ? 264 ARG   C NE     1 
ATOM   8815  C  CZ     . ARG   C 1  264 ? 25.395  -19.242  -9.099   1.00 33.50  ? 264 ARG   C CZ     1 
ATOM   8816  N  NH1    . ARG   C 1  264 ? 26.283  -19.615  -8.189   1.00 29.00  ? 264 ARG   C NH1    1 
ATOM   8817  N  NH2    . ARG   C 1  264 ? 24.906  -17.995  -9.063   1.00 29.49  ? 264 ARG   C NH2    1 
ATOM   8818  N  N      . ILE   C 1  265 ? 20.718  -24.408  -10.532  1.00 27.72  ? 265 ILE   C N      1 
ATOM   8819  C  CA     . ILE   C 1  265 ? 19.266  -24.426  -10.596  1.00 26.87  ? 265 ILE   C CA     1 
ATOM   8820  C  C      . ILE   C 1  265 ? 18.764  -25.641  -9.814   1.00 33.66  ? 265 ILE   C C      1 
ATOM   8821  O  O      . ILE   C 1  265 ? 18.285  -26.623  -10.406  1.00 29.23  ? 265 ILE   C O      1 
ATOM   8822  C  CB     . ILE   C 1  265 ? 18.766  -24.476  -12.054  1.00 31.74  ? 265 ILE   C CB     1 
ATOM   8823  C  CG1    . ILE   C 1  265 ? 19.327  -23.336  -12.920  1.00 30.92  ? 265 ILE   C CG1    1 
ATOM   8824  C  CG2    . ILE   C 1  265 ? 17.200  -24.591  -12.123  1.00 26.52  ? 265 ILE   C CG2    1 
ATOM   8825  C  CD1    . ILE   C 1  265 ? 19.693  -22.081  -12.176  1.00 31.43  ? 265 ILE   C CD1    1 
ATOM   8826  N  N      . HIS   C 1  266 ? 18.825  -25.584  -8.484   1.00 28.43  ? 266 HIS   C N      1 
ATOM   8827  C  CA     . HIS   C 1  266 ? 18.447  -26.755  -7.711   1.00 27.23  ? 266 HIS   C CA     1 
ATOM   8828  C  C      . HIS   C 1  266 ? 17.444  -26.440  -6.601   1.00 33.08  ? 266 HIS   C C      1 
ATOM   8829  O  O      . HIS   C 1  266 ? 17.447  -27.098  -5.560   1.00 34.58  ? 266 HIS   C O      1 
ATOM   8830  C  CB     . HIS   C 1  266 ? 19.686  -27.460  -7.144   1.00 30.74  ? 266 HIS   C CB     1 
ATOM   8831  C  CG     . HIS   C 1  266 ? 20.429  -26.695  -6.075   1.00 33.95  ? 266 HIS   C CG     1 
ATOM   8832  N  ND1    . HIS   C 1  266 ? 21.737  -26.273  -6.229   1.00 33.94  ? 266 HIS   C ND1    1 
ATOM   8833  C  CD2    . HIS   C 1  266 ? 20.079  -26.346  -4.814   1.00 33.96  ? 266 HIS   C CD2    1 
ATOM   8834  C  CE1    . HIS   C 1  266 ? 22.142  -25.668  -5.127   1.00 29.44  ? 266 HIS   C CE1    1 
ATOM   8835  N  NE2    . HIS   C 1  266 ? 21.162  -25.713  -4.248   1.00 33.88  ? 266 HIS   C NE2    1 
ATOM   8836  N  N      . PHE   C 1  267 ? 16.524  -25.493  -6.819   1.00 38.45  ? 267 PHE   C N      1 
ATOM   8837  C  CA     . PHE   C 1  267 ? 15.549  -25.108  -5.795   1.00 33.29  ? 267 PHE   C CA     1 
ATOM   8838  C  C      . PHE   C 1  267 ? 14.125  -25.441  -6.224   1.00 34.93  ? 267 PHE   C C      1 
ATOM   8839  O  O      . PHE   C 1  267 ? 13.443  -24.601  -6.828   1.00 43.32  ? 267 PHE   C O      1 
ATOM   8840  C  CB     . PHE   C 1  267 ? 15.684  -23.616  -5.489   1.00 30.62  ? 267 PHE   C CB     1 
ATOM   8841  C  CG     . PHE   C 1  267 ? 17.007  -23.254  -4.907   1.00 33.91  ? 267 PHE   C CG     1 
ATOM   8842  C  CD1    . PHE   C 1  267 ? 18.090  -22.966  -5.737   1.00 30.03  ? 267 PHE   C CD1    1 
ATOM   8843  C  CD2    . PHE   C 1  267 ? 17.190  -23.248  -3.527   1.00 31.81  ? 267 PHE   C CD2    1 
ATOM   8844  C  CE1    . PHE   C 1  267 ? 19.326  -22.652  -5.200   1.00 27.33  ? 267 PHE   C CE1    1 
ATOM   8845  C  CE2    . PHE   C 1  267 ? 18.431  -22.930  -2.986   1.00 30.71  ? 267 PHE   C CE2    1 
ATOM   8846  C  CZ     . PHE   C 1  267 ? 19.492  -22.628  -3.823   1.00 29.37  ? 267 PHE   C CZ     1 
ATOM   8847  N  N      . PRO   C 1  268 ? 13.615  -26.629  -5.917   1.00 27.26  ? 268 PRO   C N      1 
ATOM   8848  C  CA     . PRO   C 1  268 ? 12.304  -27.016  -6.430   1.00 31.86  ? 268 PRO   C CA     1 
ATOM   8849  C  C      . PRO   C 1  268 ? 11.175  -26.438  -5.599   1.00 34.09  ? 268 PRO   C C      1 
ATOM   8850  O  O      . PRO   C 1  268 ? 11.265  -26.301  -4.375   1.00 35.54  ? 268 PRO   C O      1 
ATOM   8851  C  CB     . PRO   C 1  268 ? 12.311  -28.554  -6.329   1.00 35.23  ? 268 PRO   C CB     1 
ATOM   8852  C  CG     . PRO   C 1  268 ? 13.693  -28.951  -5.978   1.00 29.01  ? 268 PRO   C CG     1 
ATOM   8853  C  CD     . PRO   C 1  268 ? 14.245  -27.753  -5.216   1.00 35.78  ? 268 PRO   C CD     1 
ATOM   8854  N  N      . LEU   C 1  269 ? 10.085  -26.129  -6.289   1.00 30.86  ? 269 LEU   C N      1 
ATOM   8855  C  CA     . LEU   C 1  269 ? 8.909   -25.566  -5.658   1.00 26.55  ? 269 LEU   C CA     1 
ATOM   8856  C  C      . LEU   C 1  269 ? 8.040   -26.718  -5.184   1.00 30.49  ? 269 LEU   C C      1 
ATOM   8857  O  O      . LEU   C 1  269 ? 7.744   -27.631  -5.953   1.00 34.15  ? 269 LEU   C O      1 
ATOM   8858  C  CB     . LEU   C 1  269 ? 8.165   -24.655  -6.628   1.00 26.03  ? 269 LEU   C CB     1 
ATOM   8859  C  CG     . LEU   C 1  269 ? 6.975   -23.911  -6.007   1.00 34.85  ? 269 LEU   C CG     1 
ATOM   8860  C  CD1    . LEU   C 1  269 ? 7.330   -23.093  -4.713   1.00 26.68  ? 269 LEU   C CD1    1 
ATOM   8861  C  CD2    . LEU   C 1  269 ? 6.278   -23.054  -7.072   1.00 27.66  ? 269 LEU   C CD2    1 
ATOM   8862  N  N      . ALA   C 1  270 ? 7.695   -26.719  -3.909   1.00 31.43  ? 270 ALA   C N      1 
ATOM   8863  C  CA     . ALA   C 1  270 ? 6.826   -27.745  -3.358   1.00 34.25  ? 270 ALA   C CA     1 
ATOM   8864  C  C      . ALA   C 1  270 ? 5.404   -27.201  -3.283   1.00 33.65  ? 270 ALA   C C      1 
ATOM   8865  O  O      . ALA   C 1  270 ? 5.182   -26.007  -3.062   1.00 30.94  ? 270 ALA   C O      1 
ATOM   8866  C  CB     . ALA   C 1  270 ? 7.291   -28.218  -1.967   1.00 28.09  ? 270 ALA   C CB     1 
ATOM   8867  N  N      . THR   C 1  271 ? 4.445   -28.085  -3.527   1.00 32.01  ? 271 THR   C N      1 
ATOM   8868  C  CA     . THR   C 1  271 ? 3.040   -27.748  -3.381   1.00 33.55  ? 271 THR   C CA     1 
ATOM   8869  C  C      . THR   C 1  271 ? 2.355   -28.993  -2.869   1.00 33.28  ? 271 THR   C C      1 
ATOM   8870  O  O      . THR   C 1  271 ? 2.712   -30.106  -3.261   1.00 36.42  ? 271 THR   C O      1 
ATOM   8871  C  CB     . THR   C 1  271 ? 2.400   -27.278  -4.689   1.00 38.60  ? 271 THR   C CB     1 
ATOM   8872  O  OG1    . THR   C 1  271 ? 3.252   -26.320  -5.328   1.00 41.96  ? 271 THR   C OG1    1 
ATOM   8873  C  CG2    . THR   C 1  271 ? 1.065   -26.623  -4.410   1.00 39.46  ? 271 THR   C CG2    1 
ATOM   8874  N  N      . TYR   C 1  272 ? 1.385   -28.804  -1.985   1.00 35.66  ? 272 TYR   C N      1 
ATOM   8875  C  CA     . TYR   C 1  272 ? 0.807   -29.919  -1.248   1.00 38.56  ? 272 TYR   C CA     1 
ATOM   8876  C  C      . TYR   C 1  272 ? -0.705  -29.766  -1.140   1.00 36.33  ? 272 TYR   C C      1 
ATOM   8877  O  O      . TYR   C 1  272 ? -1.204  -28.676  -0.843   1.00 42.47  ? 272 TYR   C O      1 
ATOM   8878  C  CB     . TYR   C 1  272 ? 1.440   -30.006  0.130    1.00 29.05  ? 272 TYR   C CB     1 
ATOM   8879  C  CG     . TYR   C 1  272 ? 0.936   -31.151  0.921    1.00 38.83  ? 272 TYR   C CG     1 
ATOM   8880  C  CD1    . TYR   C 1  272 ? 1.490   -32.411  0.777    1.00 38.84  ? 272 TYR   C CD1    1 
ATOM   8881  C  CD2    . TYR   C 1  272 ? -0.107  -30.983  1.832    1.00 40.07  ? 272 TYR   C CD2    1 
ATOM   8882  C  CE1    . TYR   C 1  272 ? 1.014   -33.482  1.512    1.00 37.55  ? 272 TYR   C CE1    1 
ATOM   8883  C  CE2    . TYR   C 1  272 ? -0.577  -32.038  2.565    1.00 37.12  ? 272 TYR   C CE2    1 
ATOM   8884  C  CZ     . TYR   C 1  272 ? -0.020  -33.286  2.398    1.00 34.37  ? 272 TYR   C CZ     1 
ATOM   8885  O  OH     . TYR   C 1  272 ? -0.496  -34.340  3.136    1.00 47.63  ? 272 TYR   C OH     1 
ATOM   8886  N  N      . ALA   C 1  273 ? -1.430  -30.856  -1.375   1.00 32.02  ? 273 ALA   C N      1 
ATOM   8887  C  CA     . ALA   C 1  273 ? -2.880  -30.872  -1.204   1.00 37.14  ? 273 ALA   C CA     1 
ATOM   8888  C  C      . ALA   C 1  273 ? -3.298  -32.263  -0.757   1.00 38.05  ? 273 ALA   C C      1 
ATOM   8889  O  O      . ALA   C 1  273 ? -2.617  -33.240  -1.087   1.00 41.50  ? 273 ALA   C O      1 
ATOM   8890  C  CB     . ALA   C 1  273 ? -3.617  -30.491  -2.499   1.00 27.78  ? 273 ALA   C CB     1 
ATOM   8891  N  N      . PRO   C 1  274 ? -4.406  -32.395  -0.025   1.00 35.55  ? 274 PRO   C N      1 
ATOM   8892  C  CA     . PRO   C 1  274 ? -5.288  -31.344  0.455    1.00 38.97  ? 274 PRO   C CA     1 
ATOM   8893  C  C      . PRO   C 1  274 ? -4.885  -30.916  1.835    1.00 35.53  ? 274 PRO   C C      1 
ATOM   8894  O  O      . PRO   C 1  274 ? -4.661  -31.773  2.692    1.00 37.93  ? 274 PRO   C O      1 
ATOM   8895  C  CB     . PRO   C 1  274 ? -6.650  -32.041  0.475    1.00 34.83  ? 274 PRO   C CB     1 
ATOM   8896  C  CG     . PRO   C 1  274 ? -6.282  -33.433  0.998    1.00 30.85  ? 274 PRO   C CG     1 
ATOM   8897  C  CD     . PRO   C 1  274 ? -4.918  -33.727  0.366    1.00 35.01  ? 274 PRO   C CD     1 
ATOM   8898  N  N      . VAL   C 1  275 ? -4.813  -29.620  2.102    1.00 36.39  ? 275 VAL   C N      1 
ATOM   8899  C  CA     . VAL   C 1  275 ? -4.704  -29.107  3.466    1.00 38.56  ? 275 VAL   C CA     1 
ATOM   8900  C  C      . VAL   C 1  275 ? -6.084  -28.620  3.879    1.00 37.87  ? 275 VAL   C C      1 
ATOM   8901  O  O      . VAL   C 1  275 ? -6.579  -27.618  3.357    1.00 43.74  ? 275 VAL   C O      1 
ATOM   8902  C  CB     . VAL   C 1  275 ? -3.650  -28.002  3.577    1.00 31.06  ? 275 VAL   C CB     1 
ATOM   8903  C  CG1    . VAL   C 1  275 ? -3.378  -27.709  5.021    1.00 39.96  ? 275 VAL   C CG1    1 
ATOM   8904  C  CG2    . VAL   C 1  275 ? -2.368  -28.461  2.920    1.00 31.89  ? 275 VAL   C CG2    1 
ATOM   8905  N  N      . ILE   C 1  276 ? -6.709  -29.319  4.818    1.00 35.47  ? 276 ILE   C N      1 
ATOM   8906  C  CA     . ILE   C 1  276 ? -8.154  -29.219  5.000    1.00 36.92  ? 276 ILE   C CA     1 
ATOM   8907  C  C      . ILE   C 1  276 ? -8.469  -29.630  6.427    1.00 35.26  ? 276 ILE   C C      1 
ATOM   8908  O  O      . ILE   C 1  276 ? -7.971  -30.650  6.903    1.00 41.22  ? 276 ILE   C O      1 
ATOM   8909  C  CB     . ILE   C 1  276 ? -8.889  -30.115  3.977    1.00 36.94  ? 276 ILE   C CB     1 
ATOM   8910  C  CG1    . ILE   C 1  276 ? -10.386 -29.967  4.057    1.00 46.34  ? 276 ILE   C CG1    1 
ATOM   8911  C  CG2    . ILE   C 1  276 ? -8.658  -31.585  4.251    1.00 36.30  ? 276 ILE   C CG2    1 
ATOM   8912  C  CD1    . ILE   C 1  276 ? -11.062 -30.755  2.931    1.00 49.21  ? 276 ILE   C CD1    1 
ATOM   8913  N  N      . SER   C 1  277 ? -9.285  -28.845  7.119    1.00 41.75  ? 277 SER   C N      1 
ATOM   8914  C  CA     . SER   C 1  277 ? -9.693  -29.191  8.480    1.00 40.47  ? 277 SER   C CA     1 
ATOM   8915  C  C      . SER   C 1  277 ? -10.673 -30.374  8.499    1.00 42.28  ? 277 SER   C C      1 
ATOM   8916  O  O      . SER   C 1  277 ? -11.362 -30.659  7.515    1.00 46.98  ? 277 SER   C O      1 
ATOM   8917  C  CB     . SER   C 1  277 ? -10.358 -27.996  9.145    1.00 43.71  ? 277 SER   C CB     1 
ATOM   8918  O  OG     . SER   C 1  277 ? -11.667 -27.840  8.615    1.00 51.31  ? 277 SER   C OG     1 
ATOM   8919  N  N      . ALA   C 1  278 ? -10.758 -31.044  9.656    1.00 40.61  ? 278 ALA   C N      1 
ATOM   8920  C  CA     . ALA   C 1  278 ? -11.694 -32.162  9.817    1.00 38.94  ? 278 ALA   C CA     1 
ATOM   8921  C  C      . ALA   C 1  278 ? -13.134 -31.774  9.459    1.00 50.20  ? 278 ALA   C C      1 
ATOM   8922  O  O      . ALA   C 1  278 ? -13.831 -32.505  8.742    1.00 50.64  ? 278 ALA   C O      1 
ATOM   8923  C  CB     . ALA   C 1  278 ? -11.637 -32.692  11.242   1.00 30.55  ? 278 ALA   C CB     1 
ATOM   8924  N  N      . GLU   C 1  279 ? -13.609 -30.634  9.962    1.00 48.29  ? 279 GLU   C N      1 
ATOM   8925  C  CA     . GLU   C 1  279 ? -15.006 -30.271  9.740    1.00 47.94  ? 279 GLU   C CA     1 
ATOM   8926  C  C      . GLU   C 1  279 ? -15.309 -30.112  8.262    1.00 49.09  ? 279 GLU   C C      1 
ATOM   8927  O  O      . GLU   C 1  279 ? -16.362 -30.553  7.786    1.00 53.65  ? 279 GLU   C O      1 
ATOM   8928  C  CB     . GLU   C 1  279 ? -15.339 -28.980  10.478   1.00 51.79  ? 279 GLU   C CB     1 
ATOM   8929  C  CG     . GLU   C 1  279 ? -15.080 -29.041  11.965   1.00 53.33  ? 279 GLU   C CG     1 
ATOM   8930  C  CD     . GLU   C 1  279 ? -13.866 -28.250  12.347   1.00 61.90  ? 279 GLU   C CD     1 
ATOM   8931  O  OE1    . GLU   C 1  279 ? -12.728 -28.753  12.115   1.00 53.91  ? 279 GLU   C OE1    1 
ATOM   8932  O  OE2    . GLU   C 1  279 ? -14.061 -27.122  12.867   1.00 69.04  ? 279 GLU   C OE2    1 
ATOM   8933  N  N      . LYS   C 1  280 ? -14.404 -29.457  7.525    1.00 52.57  ? 280 LYS   C N      1 
ATOM   8934  C  CA     . LYS   C 1  280 ? -14.557 -29.233  6.090    1.00 51.06  ? 280 LYS   C CA     1 
ATOM   8935  C  C      . LYS   C 1  280 ? -14.246 -30.480  5.262    1.00 51.13  ? 280 LYS   C C      1 
ATOM   8936  O  O      . LYS   C 1  280 ? -14.660 -30.565  4.101    1.00 59.78  ? 280 LYS   C O      1 
ATOM   8937  C  CB     . LYS   C 1  280 ? -13.659 -28.070  5.655    1.00 44.10  ? 280 LYS   C CB     1 
ATOM   8938  N  N      . ALA   C 1  281 ? -13.527 -31.443  5.828    1.00 49.33  ? 281 ALA   C N      1 
ATOM   8939  C  CA     . ALA   C 1  281 ? -13.221 -32.688  5.145    1.00 48.34  ? 281 ALA   C CA     1 
ATOM   8940  C  C      . ALA   C 1  281 ? -14.266 -33.756  5.405    1.00 52.05  ? 281 ALA   C C      1 
ATOM   8941  O  O      . ALA   C 1  281 ? -14.320 -34.745  4.664    1.00 50.15  ? 281 ALA   C O      1 
ATOM   8942  C  CB     . ALA   C 1  281 ? -11.839 -33.191  5.583    1.00 43.17  ? 281 ALA   C CB     1 
ATOM   8943  N  N      . TYR   C 1  282 ? -15.073 -33.580  6.453    1.00 52.38  ? 282 TYR   C N      1 
ATOM   8944  C  CA     . TYR   C 1  282 ? -16.214 -34.447  6.730    1.00 47.86  ? 282 TYR   C CA     1 
ATOM   8945  C  C      . TYR   C 1  282 ? -17.230 -34.433  5.593    1.00 52.24  ? 282 TYR   C C      1 
ATOM   8946  O  O      . TYR   C 1  282 ? -17.639 -33.367  5.118    1.00 57.41  ? 282 TYR   C O      1 
ATOM   8947  C  CB     . TYR   C 1  282 ? -16.894 -33.975  8.007    1.00 55.84  ? 282 TYR   C CB     1 
ATOM   8948  C  CG     . TYR   C 1  282 ? -17.846 -34.978  8.587    1.00 55.50  ? 282 TYR   C CG     1 
ATOM   8949  C  CD1    . TYR   C 1  282 ? -17.409 -36.241  8.941    1.00 53.24  ? 282 TYR   C CD1    1 
ATOM   8950  C  CD2    . TYR   C 1  282 ? -19.203 -34.687  8.698    1.00 52.31  ? 282 TYR   C CD2    1 
ATOM   8951  C  CE1    . TYR   C 1  282 ? -18.285 -37.176  9.461    1.00 59.32  ? 282 TYR   C CE1    1 
ATOM   8952  C  CE2    . TYR   C 1  282 ? -20.096 -35.612  9.200    1.00 55.02  ? 282 TYR   C CE2    1 
ATOM   8953  C  CZ     . TYR   C 1  282 ? -19.631 -36.861  9.591    1.00 61.22  ? 282 TYR   C CZ     1 
ATOM   8954  O  OH     . TYR   C 1  282 ? -20.502 -37.813  10.096   1.00 57.08  ? 282 TYR   C OH     1 
ATOM   8955  N  N      . HIS   C 1  283 ? -17.648 -35.622  5.163    1.00 51.08  ? 283 HIS   C N      1 
ATOM   8956  C  CA     . HIS   C 1  283 ? -18.632 -35.822  4.098    1.00 65.41  ? 283 HIS   C CA     1 
ATOM   8957  C  C      . HIS   C 1  283 ? -18.162 -35.304  2.743    1.00 66.82  ? 283 HIS   C C      1 
ATOM   8958  O  O      . HIS   C 1  283 ? -18.928 -35.370  1.769    1.00 60.26  ? 283 HIS   C O      1 
ATOM   8959  C  CB     . HIS   C 1  283 ? -19.973 -35.148  4.417    1.00 63.99  ? 283 HIS   C CB     1 
ATOM   8960  C  CG     . HIS   C 1  283 ? -20.886 -35.982  5.268    1.00 66.67  ? 283 HIS   C CG     1 
ATOM   8961  N  ND1    . HIS   C 1  283 ? -22.231 -35.702  5.417    1.00 65.56  ? 283 HIS   C ND1    1 
ATOM   8962  C  CD2    . HIS   C 1  283 ? -20.652 -37.101  6.001    1.00 61.47  ? 283 HIS   C CD2    1 
ATOM   8963  C  CE1    . HIS   C 1  283 ? -22.779 -36.597  6.224    1.00 71.52  ? 283 HIS   C CE1    1 
ATOM   8964  N  NE2    . HIS   C 1  283 ? -21.842 -37.458  6.592    1.00 64.99  ? 283 HIS   C NE2    1 
ATOM   8965  N  N      . GLU   C 1  284 ? -16.932 -34.807  2.637    1.00 60.87  ? 284 GLU   C N      1 
ATOM   8966  C  CA     . GLU   C 1  284 ? -16.424 -34.230  1.393    1.00 66.49  ? 284 GLU   C CA     1 
ATOM   8967  C  C      . GLU   C 1  284 ? -15.117 -34.926  1.003    1.00 60.36  ? 284 GLU   C C      1 
ATOM   8968  O  O      . GLU   C 1  284 ? -14.033 -34.399  1.242    1.00 68.47  ? 284 GLU   C O      1 
ATOM   8969  C  CB     . GLU   C 1  284 ? -16.250 -32.680  1.547    1.00 63.84  ? 284 GLU   C CB     1 
ATOM   8970  C  CG     . GLU   C 1  284 ? -15.292 -32.054  0.530    1.00 74.86  ? 284 GLU   C CG     1 
ATOM   8971  C  CD     . GLU   C 1  284 ? -15.656 -30.624  0.151    1.00 88.42  ? 284 GLU   C CD     1 
ATOM   8972  O  OE1    . GLU   C 1  284 ? -16.768 -30.180  0.513    1.00 88.31  ? 284 GLU   C OE1    1 
ATOM   8973  O  OE2    . GLU   C 1  284 ? -14.841 -29.948  -0.525   1.00 80.67  ? 284 GLU   C OE2    1 
ATOM   8974  N  N      . GLN   C 1  285 ? -15.228 -36.096  0.369    1.00 58.16  ? 285 GLN   C N      1 
ATOM   8975  C  CA     . GLN   C 1  285 ? -14.063 -36.816  -0.145   1.00 62.97  ? 285 GLN   C CA     1 
ATOM   8976  C  C      . GLN   C 1  285 ? -13.446 -36.093  -1.337   1.00 61.53  ? 285 GLN   C C      1 
ATOM   8977  O  O      . GLN   C 1  285 ? -14.149 -35.731  -2.289   1.00 58.86  ? 285 GLN   C O      1 
ATOM   8978  C  CB     . GLN   C 1  285 ? -14.450 -38.231  -0.565   1.00 64.07  ? 285 GLN   C CB     1 
ATOM   8979  C  CG     . GLN   C 1  285 ? -14.680 -39.159  0.598    1.00 65.68  ? 285 GLN   C CG     1 
ATOM   8980  C  CD     . GLN   C 1  285 ? -13.588 -39.045  1.641    1.00 67.42  ? 285 GLN   C CD     1 
ATOM   8981  O  OE1    . GLN   C 1  285 ? -12.456 -38.648  1.337    1.00 74.51  ? 285 GLN   C OE1    1 
ATOM   8982  N  NE2    . GLN   C 1  285 ? -13.926 -39.365  2.886    1.00 63.46  ? 285 GLN   C NE2    1 
ATOM   8983  N  N      . LEU   C 1  286 ? -12.132 -35.886  -1.295   1.00 52.37  ? 286 LEU   C N      1 
ATOM   8984  C  CA     . LEU   C 1  286 ? -11.443 -35.174  -2.361   1.00 50.10  ? 286 LEU   C CA     1 
ATOM   8985  C  C      . LEU   C 1  286 ? -10.705 -36.177  -3.243   1.00 53.19  ? 286 LEU   C C      1 
ATOM   8986  O  O      . LEU   C 1  286 ? -9.833  -36.919  -2.772   1.00 56.30  ? 286 LEU   C O      1 
ATOM   8987  C  CB     . LEU   C 1  286 ? -10.482 -34.122  -1.814   1.00 59.29  ? 286 LEU   C CB     1 
ATOM   8988  C  CG     . LEU   C 1  286 ? -11.045 -32.712  -1.570   1.00 62.40  ? 286 LEU   C CG     1 
ATOM   8989  C  CD1    . LEU   C 1  286 ? -10.259 -32.033  -0.445   1.00 52.05  ? 286 LEU   C CD1    1 
ATOM   8990  C  CD2    . LEU   C 1  286 ? -11.104 -31.830  -2.841   1.00 58.17  ? 286 LEU   C CD2    1 
ATOM   8991  N  N      . SER   C 1  287 ? -11.050 -36.177  -4.523   1.00 48.61  ? 287 SER   C N      1 
ATOM   8992  C  CA     . SER   C 1  287 ? -10.659 -37.182  -5.481   1.00 40.44  ? 287 SER   C CA     1 
ATOM   8993  C  C      . SER   C 1  287 ? -9.240  -36.935  -5.977   1.00 47.05  ? 287 SER   C C      1 
ATOM   8994  O  O      . SER   C 1  287 ? -8.636  -35.885  -5.732   1.00 44.09  ? 287 SER   C O      1 
ATOM   8995  C  CB     . SER   C 1  287 ? -11.602 -37.140  -6.663   1.00 44.45  ? 287 SER   C CB     1 
ATOM   8996  O  OG     . SER   C 1  287 ? -11.329 -35.965  -7.405   1.00 42.66  ? 287 SER   C OG     1 
ATOM   8997  N  N      . VAL   C 1  288 ? -8.721  -37.905  -6.736   1.00 44.19  ? 288 VAL   C N      1 
ATOM   8998  C  CA     . VAL   C 1  288 ? -7.418  -37.698  -7.351   1.00 38.48  ? 288 VAL   C CA     1 
ATOM   8999  C  C      . VAL   C 1  288 ? -7.418  -36.417  -8.180   1.00 38.12  ? 288 VAL   C C      1 
ATOM   9000  O  O      . VAL   C 1  288 ? -6.467  -35.630  -8.120   1.00 42.26  ? 288 VAL   C O      1 
ATOM   9001  C  CB     . VAL   C 1  288 ? -6.999  -38.925  -8.174   1.00 29.08  ? 288 VAL   C CB     1 
ATOM   9002  C  CG1    . VAL   C 1  288 ? -5.934  -38.546  -9.165   1.00 34.49  ? 288 VAL   C CG1    1 
ATOM   9003  C  CG2    . VAL   C 1  288 ? -6.468  -39.978  -7.254   1.00 44.54  ? 288 VAL   C CG2    1 
ATOM   9004  N  N      . ALA   C 1  289 ? -8.492  -36.156  -8.929   1.00 43.75  ? 289 ALA   C N      1 
ATOM   9005  C  CA     . ALA   C 1  289 ? -8.487  -34.991  -9.820   1.00 47.02  ? 289 ALA   C CA     1 
ATOM   9006  C  C      . ALA   C 1  289 ? -8.600  -33.673  -9.065   1.00 47.80  ? 289 ALA   C C      1 
ATOM   9007  O  O      . ALA   C 1  289 ? -8.243  -32.619  -9.609   1.00 46.72  ? 289 ALA   C O      1 
ATOM   9008  C  CB     . ALA   C 1  289 ? -9.618  -35.073  -10.840  1.00 39.52  ? 289 ALA   C CB     1 
ATOM   9009  N  N      . GLU   C 1  290 ? -9.088  -33.706  -7.829   1.00 47.29  ? 290 GLU   C N      1 
ATOM   9010  C  CA     . GLU   C 1  290 ? -9.258  -32.470  -7.082   1.00 43.71  ? 290 GLU   C CA     1 
ATOM   9011  C  C      . GLU   C 1  290 ? -7.934  -32.039  -6.466   1.00 40.92  ? 290 GLU   C C      1 
ATOM   9012  O  O      . GLU   C 1  290 ? -7.489  -30.902  -6.671   1.00 39.18  ? 290 GLU   C O      1 
ATOM   9013  C  CB     . GLU   C 1  290 ? -10.375 -32.664  -6.042   1.00 46.13  ? 290 GLU   C CB     1 
ATOM   9014  C  CG     . GLU   C 1  290 ? -11.665 -33.188  -6.721   1.00 51.09  ? 290 GLU   C CG     1 
ATOM   9015  C  CD     . GLU   C 1  290 ? -12.930 -33.128  -5.879   1.00 55.22  ? 290 GLU   C CD     1 
ATOM   9016  O  OE1    . GLU   C 1  290 ? -13.156 -34.035  -5.047   1.00 50.74  ? 290 GLU   C OE1    1 
ATOM   9017  O  OE2    . GLU   C 1  290 ? -13.711 -32.167  -6.065   1.00 57.99  ? 290 GLU   C OE2    1 
ATOM   9018  N  N      . ILE   C 1  291 ? -7.263  -32.968  -5.766   1.00 42.70  ? 291 ILE   C N      1 
ATOM   9019  C  CA     . ILE   C 1  291 ? -5.963  -32.689  -5.160   1.00 36.18  ? 291 ILE   C CA     1 
ATOM   9020  C  C      . ILE   C 1  291 ? -4.912  -32.355  -6.222   1.00 42.54  ? 291 ILE   C C      1 
ATOM   9021  O  O      . ILE   C 1  291 ? -4.153  -31.391  -6.065   1.00 36.92  ? 291 ILE   C O      1 
ATOM   9022  C  CB     . ILE   C 1  291 ? -5.522  -33.863  -4.262   1.00 39.59  ? 291 ILE   C CB     1 
ATOM   9023  C  CG1    . ILE   C 1  291 ? -5.198  -35.133  -5.051   1.00 36.63  ? 291 ILE   C CG1    1 
ATOM   9024  C  CG2    . ILE   C 1  291 ? -6.581  -34.173  -3.213   1.00 43.97  ? 291 ILE   C CG2    1 
ATOM   9025  C  CD1    . ILE   C 1  291 ? -4.712  -36.259  -4.131   1.00 35.55  ? 291 ILE   C CD1    1 
ATOM   9026  N  N      . THR   C 1  292 ? -4.852  -33.122  -7.324   1.00 44.61  ? 292 THR   C N      1 
ATOM   9027  C  CA     . THR   C 1  292 ? -3.922  -32.774  -8.398   1.00 43.93  ? 292 THR   C CA     1 
ATOM   9028  C  C      . THR   C 1  292 ? -4.137  -31.335  -8.837   1.00 43.55  ? 292 THR   C C      1 
ATOM   9029  O  O      . THR   C 1  292 ? -3.183  -30.563  -9.014   1.00 39.13  ? 292 THR   C O      1 
ATOM   9030  C  CB     . THR   C 1  292 ? -4.079  -33.705  -9.605   1.00 36.58  ? 292 THR   C CB     1 
ATOM   9031  O  OG1    . THR   C 1  292 ? -3.963  -35.063  -9.183   1.00 32.98  ? 292 THR   C OG1    1 
ATOM   9032  C  CG2    . THR   C 1  292 ? -2.963  -33.432  -10.614  1.00 30.75  ? 292 THR   C CG2    1 
ATOM   9033  N  N      . ASN   C 1  293 ? -5.398  -30.961  -9.015   1.00 42.25  ? 293 ASN   C N      1 
ATOM   9034  C  CA     . ASN   C 1  293 ? -5.699  -29.610  -9.448   1.00 44.89  ? 293 ASN   C CA     1 
ATOM   9035  C  C      . ASN   C 1  293 ? -5.173  -28.580  -8.448   1.00 48.25  ? 293 ASN   C C      1 
ATOM   9036  O  O      . ASN   C 1  293 ? -4.608  -27.549  -8.840   1.00 40.50  ? 293 ASN   C O      1 
ATOM   9037  C  CB     . ASN   C 1  293 ? -7.198  -29.493  -9.654   1.00 49.70  ? 293 ASN   C CB     1 
ATOM   9038  C  CG     . ASN   C 1  293 ? -7.532  -28.820  -10.949  1.00 63.56  ? 293 ASN   C CG     1 
ATOM   9039  O  OD1    . ASN   C 1  293 ? -7.334  -27.615  -11.092  1.00 62.75  ? 293 ASN   C OD1    1 
ATOM   9040  N  ND2    . ASN   C 1  293 ? -7.948  -29.610  -11.944  1.00 65.09  ? 293 ASN   C ND2    1 
ATOM   9041  N  N      . ALA   C 1  294 ? -5.329  -28.860  -7.148   1.00 43.95  ? 294 ALA   C N      1 
ATOM   9042  C  CA     . ALA   C 1  294 ? -4.881  -27.935  -6.119   1.00 37.44  ? 294 ALA   C CA     1 
ATOM   9043  C  C      . ALA   C 1  294 ? -3.399  -27.617  -6.251   1.00 42.30  ? 294 ALA   C C      1 
ATOM   9044  O  O      . ALA   C 1  294 ? -2.959  -26.539  -5.835   1.00 43.06  ? 294 ALA   C O      1 
ATOM   9045  C  CB     . ALA   C 1  294 ? -5.194  -28.520  -4.739   1.00 37.49  ? 294 ALA   C CB     1 
ATOM   9046  N  N      . CYS   C 1  295 ? -2.611  -28.533  -6.826   1.00 39.66  ? 295 CYS   C N      1 
ATOM   9047  C  CA     . CYS   C 1  295 ? -1.179  -28.293  -6.910   1.00 38.30  ? 295 CYS   C CA     1 
ATOM   9048  C  C      . CYS   C 1  295 ? -0.862  -27.090  -7.771   1.00 39.63  ? 295 CYS   C C      1 
ATOM   9049  O  O      . CYS   C 1  295 ? 0.203   -26.491  -7.617   1.00 51.46  ? 295 CYS   C O      1 
ATOM   9050  C  CB     . CYS   C 1  295 ? -0.456  -29.510  -7.461   1.00 43.00  ? 295 CYS   C CB     1 
ATOM   9051  S  SG     . CYS   C 1  295 ? -0.598  -30.953  -6.480   1.00 43.50  ? 295 CYS   C SG     1 
ATOM   9052  N  N      . PHE   C 1  296 ? -1.746  -26.731  -8.688   1.00 37.88  ? 296 PHE   C N      1 
ATOM   9053  C  CA     . PHE   C 1  296 ? -1.496  -25.624  -9.591   1.00 40.36  ? 296 PHE   C CA     1 
ATOM   9054  C  C      . PHE   C 1  296 ? -2.190  -24.353  -9.156   1.00 42.57  ? 296 PHE   C C      1 
ATOM   9055  O  O      . PHE   C 1  296 ? -2.211  -23.379  -9.916   1.00 50.48  ? 296 PHE   C O      1 
ATOM   9056  C  CB     . PHE   C 1  296 ? -1.900  -26.010  -11.020  1.00 48.20  ? 296 PHE   C CB     1 
ATOM   9057  C  CG     . PHE   C 1  296 ? -1.046  -27.106  -11.599  1.00 44.73  ? 296 PHE   C CG     1 
ATOM   9058  C  CD1    . PHE   C 1  296 ? -1.352  -28.440  -11.362  1.00 40.53  ? 296 PHE   C CD1    1 
ATOM   9059  C  CD2    . PHE   C 1  296 ? 0.092   -26.797  -12.320  1.00 37.22  ? 296 PHE   C CD2    1 
ATOM   9060  C  CE1    . PHE   C 1  296 ? -0.565  -29.443  -11.850  1.00 35.69  ? 296 PHE   C CE1    1 
ATOM   9061  C  CE2    . PHE   C 1  296 ? 0.887   -27.799  -12.817  1.00 44.00  ? 296 PHE   C CE2    1 
ATOM   9062  C  CZ     . PHE   C 1  296 ? 0.554   -29.134  -12.578  1.00 45.44  ? 296 PHE   C CZ     1 
ATOM   9063  N  N      . GLU   C 1  297 ? -2.747  -24.337  -7.954   1.00 40.67  ? 297 GLU   C N      1 
ATOM   9064  C  CA     . GLU   C 1  297 ? -3.199  -23.104  -7.347   1.00 45.74  ? 297 GLU   C CA     1 
ATOM   9065  C  C      . GLU   C 1  297 ? -2.066  -22.506  -6.516   1.00 45.53  ? 297 GLU   C C      1 
ATOM   9066  O  O      . GLU   C 1  297 ? -1.665  -23.113  -5.511   1.00 37.26  ? 297 GLU   C O      1 
ATOM   9067  C  CB     . GLU   C 1  297 ? -4.417  -23.344  -6.479   1.00 50.05  ? 297 GLU   C CB     1 
ATOM   9068  C  CG     . GLU   C 1  297 ? -5.303  -22.105  -6.427   1.00 60.84  ? 297 GLU   C CG     1 
ATOM   9069  C  CD     . GLU   C 1  297 ? -5.959  -21.831  -7.793   1.00 74.62  ? 297 GLU   C CD     1 
ATOM   9070  O  OE1    . GLU   C 1  297 ? -5.864  -20.667  -8.290   1.00 73.89  ? 297 GLU   C OE1    1 
ATOM   9071  O  OE2    . GLU   C 1  297 ? -6.564  -22.791  -8.356   1.00 69.51  ? 297 GLU   C OE2    1 
ATOM   9072  N  N      . PRO   C 1  298 ? -1.529  -21.338  -6.894   1.00 44.56  ? 298 PRO   C N      1 
ATOM   9073  C  CA     . PRO   C 1  298 ? -0.384  -20.779  -6.159   1.00 40.15  ? 298 PRO   C CA     1 
ATOM   9074  C  C      . PRO   C 1  298 ? -0.628  -20.636  -4.678   1.00 37.57  ? 298 PRO   C C      1 
ATOM   9075  O  O      . PRO   C 1  298 ? 0.341   -20.595  -3.923   1.00 45.89  ? 298 PRO   C O      1 
ATOM   9076  C  CB     . PRO   C 1  298 ? -0.168  -19.414  -6.828   1.00 39.80  ? 298 PRO   C CB     1 
ATOM   9077  C  CG     . PRO   C 1  298 ? -0.629  -19.632  -8.222   1.00 44.85  ? 298 PRO   C CG     1 
ATOM   9078  C  CD     . PRO   C 1  298 ? -1.861  -20.525  -8.074   1.00 45.12  ? 298 PRO   C CD     1 
ATOM   9079  N  N      . ALA   C 1  299 ? -1.870  -20.590  -4.220   1.00 36.63  ? 299 ALA   C N      1 
ATOM   9080  C  CA     . ALA   C 1  299 ? -2.065  -20.465  -2.783   1.00 39.32  ? 299 ALA   C CA     1 
ATOM   9081  C  C      . ALA   C 1  299 ? -1.776  -21.746  -2.023   1.00 40.02  ? 299 ALA   C C      1 
ATOM   9082  O  O      . ALA   C 1  299 ? -1.857  -21.726  -0.793   1.00 42.69  ? 299 ALA   C O      1 
ATOM   9083  C  CB     . ALA   C 1  299 ? -3.489  -20.016  -2.463   1.00 42.61  ? 299 ALA   C CB     1 
ATOM   9084  N  N      . ASN   C 1  300 ? -1.470  -22.857  -2.691   1.00 38.68  ? 300 ASN   C N      1 
ATOM   9085  C  CA     . ASN   C 1  300 ? -1.086  -24.068  -1.984   1.00 37.95  ? 300 ASN   C CA     1 
ATOM   9086  C  C      . ASN   C 1  300 ? 0.424   -24.331  -1.993   1.00 40.81  ? 300 ASN   C C      1 
ATOM   9087  O  O      . ASN   C 1  300 ? 0.844   -25.383  -1.498   1.00 42.15  ? 300 ASN   C O      1 
ATOM   9088  C  CB     . ASN   C 1  300 ? -1.817  -25.275  -2.560   1.00 39.54  ? 300 ASN   C CB     1 
ATOM   9089  C  CG     . ASN   C 1  300 ? -3.315  -25.225  -2.337   1.00 43.47  ? 300 ASN   C CG     1 
ATOM   9090  O  OD1    . ASN   C 1  300 ? -3.799  -24.892  -1.245   1.00 45.71  ? 300 ASN   C OD1    1 
ATOM   9091  N  ND2    . ASN   C 1  300 ? -4.063  -25.616  -3.361   1.00 44.64  ? 300 ASN   C ND2    1 
ATOM   9092  N  N      . GLN   C 1  301 ? 1.239   -23.410  -2.532   1.00 32.20  ? 301 GLN   C N      1 
ATOM   9093  C  CA     . GLN   C 1  301 ? 2.689   -23.572  -2.642   1.00 36.51  ? 301 GLN   C CA     1 
ATOM   9094  C  C      . GLN   C 1  301 ? 3.440   -23.340  -1.326   1.00 35.91  ? 301 GLN   C C      1 
ATOM   9095  O  O      . GLN   C 1  301 ? 3.019   -22.560  -0.466   1.00 37.48  ? 301 GLN   C O      1 
ATOM   9096  C  CB     . GLN   C 1  301 ? 3.234   -22.609  -3.685   1.00 37.00  ? 301 GLN   C CB     1 
ATOM   9097  C  CG     . GLN   C 1  301 ? 2.416   -22.632  -4.943   1.00 39.69  ? 301 GLN   C CG     1 
ATOM   9098  C  CD     . GLN   C 1  301 ? 2.902   -21.629  -5.930   1.00 37.72  ? 301 GLN   C CD     1 
ATOM   9099  O  OE1    . GLN   C 1  301 ? 2.567   -21.676  -7.112   1.00 40.06  ? 301 GLN   C OE1    1 
ATOM   9100  N  NE2    . GLN   C 1  301 ? 3.720   -20.704  -5.454   1.00 41.29  ? 301 GLN   C NE2    1 
ATOM   9101  N  N      . MET   C 1  302 ? 4.584   -24.022  -1.182   1.00 37.92  ? 302 MET   C N      1 
ATOM   9102  C  CA     . MET   C 1  302 ? 5.450   -23.794  -0.020   1.00 38.13  ? 302 MET   C CA     1 
ATOM   9103  C  C      . MET   C 1  302 ? 6.135   -22.443  -0.072   1.00 35.56  ? 302 MET   C C      1 
ATOM   9104  O  O      . MET   C 1  302 ? 6.623   -21.979  0.954    1.00 42.72  ? 302 MET   C O      1 
ATOM   9105  C  CB     . MET   C 1  302 ? 6.570   -24.845  0.106    1.00 36.66  ? 302 MET   C CB     1 
ATOM   9106  C  CG     . MET   C 1  302 ? 6.195   -26.184  0.675    1.00 40.76  ? 302 MET   C CG     1 
ATOM   9107  S  SD     . MET   C 1  302 ? 4.761   -26.099  1.775    1.00 69.00  ? 302 MET   C SD     1 
ATOM   9108  C  CE     . MET   C 1  302 ? 3.492   -26.710  0.646    1.00 44.75  ? 302 MET   C CE     1 
ATOM   9109  N  N      . VAL   C 1  303 ? 6.233   -21.833  -1.242   1.00 31.45  ? 303 VAL   C N      1 
ATOM   9110  C  CA     . VAL   C 1  303 ? 6.936   -20.571  -1.415   1.00 34.33  ? 303 VAL   C CA     1 
ATOM   9111  C  C      . VAL   C 1  303 ? 6.057   -19.641  -2.244   1.00 38.53  ? 303 VAL   C C      1 
ATOM   9112  O  O      . VAL   C 1  303 ? 5.514   -20.045  -3.282   1.00 40.36  ? 303 VAL   C O      1 
ATOM   9113  C  CB     . VAL   C 1  303 ? 8.303   -20.778  -2.096   1.00 29.66  ? 303 VAL   C CB     1 
ATOM   9114  C  CG1    . VAL   C 1  303 ? 8.970   -19.428  -2.414   1.00 19.94  ? 303 VAL   C CG1    1 
ATOM   9115  C  CG2    . VAL   C 1  303 ? 9.173   -21.656  -1.215   1.00 27.43  ? 303 VAL   C CG2    1 
ATOM   9116  N  N      . LYS   C 1  304 ? 5.939   -18.393  -1.813   1.00 37.18  ? 304 LYS   C N      1 
ATOM   9117  C  CA     . LYS   C 1  304 ? 5.106   -17.443  -2.537   1.00 35.48  ? 304 LYS   C CA     1 
ATOM   9118  C  C      . LYS   C 1  304 ? 5.800   -16.995  -3.829   1.00 40.74  ? 304 LYS   C C      1 
ATOM   9119  O  O      . LYS   C 1  304 ? 6.903   -16.437  -3.798   1.00 41.60  ? 304 LYS   C O      1 
ATOM   9120  C  CB     . LYS   C 1  304 ? 4.761   -16.284  -1.604   1.00 32.60  ? 304 LYS   C CB     1 
ATOM   9121  C  CG     . LYS   C 1  304 ? 3.875   -16.799  -0.445   1.00 34.88  ? 304 LYS   C CG     1 
ATOM   9122  C  CD     . LYS   C 1  304 ? 3.293   -15.742  0.469    1.00 41.39  ? 304 LYS   C CD     1 
ATOM   9123  C  CE     . LYS   C 1  304 ? 2.070   -15.080  -0.121   1.00 44.86  ? 304 LYS   C CE     1 
ATOM   9124  N  NZ     . LYS   C 1  304 ? 1.228   -14.466  0.948    1.00 50.33  ? 304 LYS   C NZ     1 
ATOM   9125  N  N      . CYS   C 1  305 ? 5.156   -17.253  -4.968   1.00 38.14  ? 305 CYS   C N      1 
ATOM   9126  C  CA     . CYS   C 1  305 ? 5.640   -16.859  -6.289   1.00 39.84  ? 305 CYS   C CA     1 
ATOM   9127  C  C      . CYS   C 1  305 ? 4.577   -17.249  -7.296   1.00 39.16  ? 305 CYS   C C      1 
ATOM   9128  O  O      . CYS   C 1  305 ? 3.711   -18.075  -7.012   1.00 37.06  ? 305 CYS   C O      1 
ATOM   9129  C  CB     . CYS   C 1  305 ? 6.977   -17.536  -6.664   1.00 45.77  ? 305 CYS   C CB     1 
ATOM   9130  S  SG     . CYS   C 1  305 ? 6.987   -19.402  -6.675   1.00 37.92  ? 305 CYS   C SG     1 
ATOM   9131  N  N      . ASP   C 1  306 ? 4.683   -16.693  -8.492   1.00 41.83  ? 306 ASP   C N      1 
ATOM   9132  C  CA     . ASP   C 1  306 ? 3.729   -16.999  -9.553   1.00 43.97  ? 306 ASP   C CA     1 
ATOM   9133  C  C      . ASP   C 1  306 ? 4.306   -17.926  -10.623  1.00 39.29  ? 306 ASP   C C      1 
ATOM   9134  O  O      . ASP   C 1  306 ? 4.989   -17.448  -11.553  1.00 37.04  ? 306 ASP   C O      1 
ATOM   9135  C  CB     . ASP   C 1  306 ? 3.233   -15.703  -10.189  1.00 46.65  ? 306 ASP   C CB     1 
ATOM   9136  C  CG     . ASP   C 1  306 ? 1.761   -15.737  -10.471  1.00 59.30  ? 306 ASP   C CG     1 
ATOM   9137  O  OD1    . ASP   C 1  306 ? 1.138   -16.825  -10.330  1.00 54.33  ? 306 ASP   C OD1    1 
ATOM   9138  O  OD2    . ASP   C 1  306 ? 1.225   -14.661  -10.818  1.00 76.07  ? 306 ASP   C OD2    1 
ATOM   9139  N  N      . PRO   C 1  307 ? 4.051   -19.239  -10.561  1.00 40.67  ? 307 PRO   C N      1 
ATOM   9140  C  CA     . PRO   C 1  307 ? 4.544   -20.104  -11.634  1.00 41.04  ? 307 PRO   C CA     1 
ATOM   9141  C  C      . PRO   C 1  307 ? 3.914   -19.752  -12.955  1.00 47.16  ? 307 PRO   C C      1 
ATOM   9142  O  O      . PRO   C 1  307 ? 4.571   -19.893  -13.993  1.00 50.59  ? 307 PRO   C O      1 
ATOM   9143  C  CB     . PRO   C 1  307 ? 4.171   -21.516  -11.156  1.00 35.83  ? 307 PRO   C CB     1 
ATOM   9144  C  CG     . PRO   C 1  307 ? 3.997   -21.386  -9.692   1.00 34.94  ? 307 PRO   C CG     1 
ATOM   9145  C  CD     . PRO   C 1  307 ? 3.382   -20.027  -9.512   1.00 42.78  ? 307 PRO   C CD     1 
ATOM   9146  N  N      . ARG   C 1  308 ? 2.677   -19.245  -12.935  1.00 45.35  ? 308 ARG   C N      1 
ATOM   9147  C  CA     . ARG   C 1  308 ? 2.019   -18.785  -14.154  1.00 51.39  ? 308 ARG   C CA     1 
ATOM   9148  C  C      . ARG   C 1  308 ? 2.876   -17.798  -14.944  1.00 50.85  ? 308 ARG   C C      1 
ATOM   9149  O  O      . ARG   C 1  308 ? 2.924   -17.865  -16.175  1.00 63.94  ? 308 ARG   C O      1 
ATOM   9150  C  CB     . ARG   C 1  308 ? 0.662   -18.165  -13.808  1.00 56.19  ? 308 ARG   C CB     1 
ATOM   9151  C  CG     . ARG   C 1  308 ? -0.160  -19.050  -12.881  1.00 58.30  ? 308 ARG   C CG     1 
ATOM   9152  C  CD     . ARG   C 1  308 ? -1.593  -18.603  -12.736  1.00 67.57  ? 308 ARG   C CD     1 
ATOM   9153  N  NE     . ARG   C 1  308 ? -1.808  -17.873  -11.492  1.00 71.73  ? 308 ARG   C NE     1 
ATOM   9154  C  CZ     . ARG   C 1  308 ? -2.833  -18.067  -10.671  1.00 66.10  ? 308 ARG   C CZ     1 
ATOM   9155  N  NH1    . ARG   C 1  308 ? -3.766  -18.975  -10.928  1.00 56.46  ? 308 ARG   C NH1    1 
ATOM   9156  N  NH2    . ARG   C 1  308 ? -2.922  -17.332  -9.562   1.00 55.12  ? 308 ARG   C NH2    1 
ATOM   9157  N  N      . HIS   C 1  309 ? 3.560   -16.877  -14.273  1.00 51.12  ? 309 HIS   C N      1 
ATOM   9158  C  CA     . HIS   C 1  309 ? 4.351   -15.879  -14.986  1.00 58.41  ? 309 HIS   C CA     1 
ATOM   9159  C  C      . HIS   C 1  309 ? 5.821   -16.284  -15.101  1.00 58.51  ? 309 HIS   C C      1 
ATOM   9160  O  O      . HIS   C 1  309 ? 6.679   -15.427  -15.355  1.00 60.22  ? 309 HIS   C O      1 
ATOM   9161  C  CB     . HIS   C 1  309 ? 4.199   -14.489  -14.340  1.00 58.04  ? 309 HIS   C CB     1 
ATOM   9162  C  CG     . HIS   C 1  309 ? 2.780   -13.990  -14.302  1.00 64.30  ? 309 HIS   C CG     1 
ATOM   9163  N  ND1    . HIS   C 1  309 ? 2.157   -13.590  -13.136  1.00 64.30  ? 309 HIS   C ND1    1 
ATOM   9164  C  CD2    . HIS   C 1  309 ? 1.851   -13.860  -15.283  1.00 65.31  ? 309 HIS   C CD2    1 
ATOM   9165  C  CE1    . HIS   C 1  309 ? 0.911   -13.234  -13.402  1.00 63.95  ? 309 HIS   C CE1    1 
ATOM   9166  N  NE2    . HIS   C 1  309 ? 0.700   -13.387  -14.697  1.00 64.75  ? 309 HIS   C NE2    1 
ATOM   9167  N  N      . GLY   C 1  310 ? 6.119   -17.573  -14.920  1.00 46.11  ? 310 GLY   C N      1 
ATOM   9168  C  CA     . GLY   C 1  310 ? 7.425   -18.135  -15.204  1.00 43.72  ? 310 GLY   C CA     1 
ATOM   9169  C  C      . GLY   C 1  310 ? 7.345   -19.370  -16.087  1.00 43.06  ? 310 GLY   C C      1 
ATOM   9170  O  O      . GLY   C 1  310 ? 6.320   -19.608  -16.726  1.00 47.25  ? 310 GLY   C O      1 
ATOM   9171  N  N      . LYS   C 1  311 ? 8.403   -20.171  -16.127  1.00 36.79  ? 311 LYS   C N      1 
ATOM   9172  C  CA     . LYS   C 1  311 ? 8.477   -21.322  -17.011  1.00 38.31  ? 311 LYS   C CA     1 
ATOM   9173  C  C      . LYS   C 1  311 ? 8.874   -22.570  -16.236  1.00 41.92  ? 311 LYS   C C      1 
ATOM   9174  O  O      . LYS   C 1  311 ? 9.688   -22.520  -15.306  1.00 41.78  ? 311 LYS   C O      1 
ATOM   9175  C  CB     . LYS   C 1  311 ? 9.465   -21.081  -18.158  1.00 41.03  ? 311 LYS   C CB     1 
ATOM   9176  C  CG     . LYS   C 1  311 ? 8.950   -20.070  -19.165  1.00 47.30  ? 311 LYS   C CG     1 
ATOM   9177  C  CD     . LYS   C 1  311 ? 9.750   -20.078  -20.428  1.00 51.23  ? 311 LYS   C CD     1 
ATOM   9178  C  CE     . LYS   C 1  311 ? 9.242   -19.051  -21.419  1.00 52.53  ? 311 LYS   C CE     1 
ATOM   9179  N  NZ     . LYS   C 1  311 ? 10.166  -19.008  -22.592  1.00 58.46  ? 311 LYS   C NZ     1 
ATOM   9180  N  N      . TYR   C 1  312 ? 8.302   -23.699  -16.625  1.00 41.47  ? 312 TYR   C N      1 
ATOM   9181  C  CA     . TYR   C 1  312 ? 8.626   -24.951  -15.970  1.00 38.31  ? 312 TYR   C CA     1 
ATOM   9182  C  C      . TYR   C 1  312 ? 9.824   -25.604  -16.628  1.00 38.92  ? 312 TYR   C C      1 
ATOM   9183  O  O      . TYR   C 1  312 ? 9.959   -25.612  -17.856  1.00 36.17  ? 312 TYR   C O      1 
ATOM   9184  C  CB     . TYR   C 1  312 ? 7.460   -25.917  -16.010  1.00 34.35  ? 312 TYR   C CB     1 
ATOM   9185  C  CG     . TYR   C 1  312 ? 6.339   -25.573  -15.088  1.00 37.96  ? 312 TYR   C CG     1 
ATOM   9186  C  CD1    . TYR   C 1  312 ? 5.330   -24.716  -15.492  1.00 41.35  ? 312 TYR   C CD1    1 
ATOM   9187  C  CD2    . TYR   C 1  312 ? 6.263   -26.128  -13.824  1.00 38.16  ? 312 TYR   C CD2    1 
ATOM   9188  C  CE1    . TYR   C 1  312 ? 4.287   -24.419  -14.672  1.00 37.49  ? 312 TYR   C CE1    1 
ATOM   9189  C  CE2    . TYR   C 1  312 ? 5.211   -25.842  -13.004  1.00 39.97  ? 312 TYR   C CE2    1 
ATOM   9190  C  CZ     . TYR   C 1  312 ? 4.233   -24.986  -13.440  1.00 34.63  ? 312 TYR   C CZ     1 
ATOM   9191  O  OH     . TYR   C 1  312 ? 3.196   -24.691  -12.629  1.00 42.35  ? 312 TYR   C OH     1 
ATOM   9192  N  N      . MET   C 1  313 ? 10.689  -26.152  -15.794  1.00 36.02  ? 313 MET   C N      1 
ATOM   9193  C  CA     . MET   C 1  313 ? 11.789  -26.957  -16.265  1.00 38.54  ? 313 MET   C CA     1 
ATOM   9194  C  C      . MET   C 1  313 ? 11.603  -28.413  -15.893  1.00 38.36  ? 313 MET   C C      1 
ATOM   9195  O  O      . MET   C 1  313 ? 12.369  -29.267  -16.340  1.00 42.59  ? 313 MET   C O      1 
ATOM   9196  C  CB     . MET   C 1  313 ? 13.107  -26.426  -15.690  1.00 40.36  ? 313 MET   C CB     1 
ATOM   9197  C  CG     . MET   C 1  313 ? 13.601  -25.193  -16.421  1.00 38.57  ? 313 MET   C CG     1 
ATOM   9198  S  SD     . MET   C 1  313 ? 14.819  -24.229  -15.514  1.00 44.87  ? 313 MET   C SD     1 
ATOM   9199  C  CE     . MET   C 1  313 ? 13.904  -23.640  -14.092  1.00 34.77  ? 313 MET   C CE     1 
ATOM   9200  N  N      . ALA   C 1  314 ? 10.597  -28.709  -15.097  1.00 38.26  ? 314 ALA   C N      1 
ATOM   9201  C  CA     . ALA   C 1  314 ? 10.344  -30.044  -14.590  1.00 35.89  ? 314 ALA   C CA     1 
ATOM   9202  C  C      . ALA   C 1  314 ? 9.116   -29.919  -13.722  1.00 38.34  ? 314 ALA   C C      1 
ATOM   9203  O  O      . ALA   C 1  314 ? 8.912   -28.877  -13.088  1.00 39.90  ? 314 ALA   C O      1 
ATOM   9204  C  CB     . ALA   C 1  314 ? 11.516  -30.603  -13.783  1.00 30.03  ? 314 ALA   C CB     1 
ATOM   9205  N  N      . CYS   C 1  315 ? 8.294   -30.961  -13.700  1.00 39.30  ? 315 CYS   C N      1 
ATOM   9206  C  CA     . CYS   C 1  315 ? 7.127   -30.999  -12.830  1.00 35.80  ? 315 CYS   C CA     1 
ATOM   9207  C  C      . CYS   C 1  315 ? 6.887   -32.454  -12.423  1.00 33.21  ? 315 CYS   C C      1 
ATOM   9208  O  O      . CYS   C 1  315 ? 6.706   -33.330  -13.277  1.00 32.83  ? 315 CYS   C O      1 
ATOM   9209  C  CB     . CYS   C 1  315 ? 5.930   -30.349  -13.561  1.00 36.83  ? 315 CYS   C CB     1 
ATOM   9210  S  SG     . CYS   C 1  315 ? 4.309   -30.696  -12.912  1.00 59.79  ? 315 CYS   C SG     1 
ATOM   9211  N  N      . CYS   C 1  316 ? 6.930   -32.721  -11.118  1.00 35.96  ? 316 CYS   C N      1 
ATOM   9212  C  CA     . CYS   C 1  316 ? 6.827   -34.068  -10.556  1.00 34.32  ? 316 CYS   C CA     1 
ATOM   9213  C  C      . CYS   C 1  316 ? 5.602   -34.156  -9.663   1.00 33.23  ? 316 CYS   C C      1 
ATOM   9214  O  O      . CYS   C 1  316 ? 5.292   -33.207  -8.945   1.00 35.89  ? 316 CYS   C O      1 
ATOM   9215  C  CB     . CYS   C 1  316 ? 8.086   -34.407  -9.732   1.00 37.22  ? 316 CYS   C CB     1 
ATOM   9216  S  SG     . CYS   C 1  316 ? 9.621   -34.255  -10.731  1.00 46.14  ? 316 CYS   C SG     1 
ATOM   9217  N  N      . LEU   C 1  317 ? 4.910   -35.289  -9.677   1.00 31.30  ? 317 LEU   C N      1 
ATOM   9218  C  CA     . LEU   C 1  317 ? 3.810   -35.505  -8.742   1.00 28.37  ? 317 LEU   C CA     1 
ATOM   9219  C  C      . LEU   C 1  317 ? 4.103   -36.694  -7.827   1.00 28.61  ? 317 LEU   C C      1 
ATOM   9220  O  O      . LEU   C 1  317 ? 4.255   -37.829  -8.290   1.00 34.40  ? 317 LEU   C O      1 
ATOM   9221  C  CB     . LEU   C 1  317 ? 2.497   -35.684  -9.502   1.00 34.82  ? 317 LEU   C CB     1 
ATOM   9222  C  CG     . LEU   C 1  317 ? 2.059   -34.318  -10.060  1.00 32.50  ? 317 LEU   C CG     1 
ATOM   9223  C  CD1    . LEU   C 1  317 ? 1.083   -34.409  -11.237  1.00 27.16  ? 317 LEU   C CD1    1 
ATOM   9224  C  CD2    . LEU   C 1  317 ? 1.481   -33.492  -8.937   1.00 37.18  ? 317 LEU   C CD2    1 
ATOM   9225  N  N      . LEU   C 1  318 ? 4.179   -36.444  -6.542   1.00 26.06  ? 318 LEU   C N      1 
ATOM   9226  C  CA     . LEU   C 1  318 ? 4.374   -37.507  -5.556   1.00 35.98  ? 318 LEU   C CA     1 
ATOM   9227  C  C      . LEU   C 1  318 ? 3.049   -37.771  -4.818   1.00 34.75  ? 318 LEU   C C      1 
ATOM   9228  O  O      . LEU   C 1  318 ? 2.688   -37.034  -3.901   1.00 35.58  ? 318 LEU   C O      1 
ATOM   9229  C  CB     . LEU   C 1  318 ? 5.497   -37.129  -4.586   1.00 33.99  ? 318 LEU   C CB     1 
ATOM   9230  C  CG     . LEU   C 1  318 ? 6.951   -37.125  -5.061   1.00 29.79  ? 318 LEU   C CG     1 
ATOM   9231  C  CD1    . LEU   C 1  318 ? 7.146   -36.266  -6.300   1.00 28.62  ? 318 LEU   C CD1    1 
ATOM   9232  C  CD2    . LEU   C 1  318 ? 7.767   -36.581  -3.927   1.00 34.48  ? 318 LEU   C CD2    1 
ATOM   9233  N  N      . TYR   C 1  319 ? 2.338   -38.832  -5.203   1.00 32.20  ? 319 TYR   C N      1 
ATOM   9234  C  CA     . TYR   C 1  319 ? 1.069   -39.199  -4.584   1.00 34.54  ? 319 TYR   C CA     1 
ATOM   9235  C  C      . TYR   C 1  319 ? 1.293   -40.188  -3.459   1.00 36.35  ? 319 TYR   C C      1 
ATOM   9236  O  O      . TYR   C 1  319 ? 2.186   -41.027  -3.527   1.00 39.19  ? 319 TYR   C O      1 
ATOM   9237  C  CB     . TYR   C 1  319 ? 0.103   -39.857  -5.569   1.00 31.47  ? 319 TYR   C CB     1 
ATOM   9238  C  CG     . TYR   C 1  319 ? -0.369  -38.954  -6.662   1.00 34.10  ? 319 TYR   C CG     1 
ATOM   9239  C  CD1    . TYR   C 1  319 ? 0.375   -38.800  -7.813   1.00 34.88  ? 319 TYR   C CD1    1 
ATOM   9240  C  CD2    . TYR   C 1  319 ? -1.542  -38.250  -6.553   1.00 33.50  ? 319 TYR   C CD2    1 
ATOM   9241  C  CE1    . TYR   C 1  319 ? -0.025  -37.971  -8.814   1.00 35.13  ? 319 TYR   C CE1    1 
ATOM   9242  C  CE2    . TYR   C 1  319 ? -1.954  -37.406  -7.573   1.00 31.60  ? 319 TYR   C CE2    1 
ATOM   9243  C  CZ     . TYR   C 1  319 ? -1.190  -37.283  -8.693   1.00 32.61  ? 319 TYR   C CZ     1 
ATOM   9244  O  OH     . TYR   C 1  319 ? -1.573  -36.459  -9.718   1.00 37.33  ? 319 TYR   C OH     1 
ATOM   9245  N  N      . ARG   C 1  320 ? 0.442   -40.122  -2.444   1.00 32.17  ? 320 ARG   C N      1 
ATOM   9246  C  CA     . ARG   C 1  320 ? 0.371   -41.216  -1.495   1.00 42.97  ? 320 ARG   C CA     1 
ATOM   9247  C  C      . ARG   C 1  320 ? -1.088  -41.520  -1.173   1.00 41.81  ? 320 ARG   C C      1 
ATOM   9248  O  O      . ARG   C 1  320 ? -1.965  -40.664  -1.308   1.00 43.47  ? 320 ARG   C O      1 
ATOM   9249  C  CB     . ARG   C 1  320 ? 1.200   -40.931  -0.224   1.00 41.23  ? 320 ARG   C CB     1 
ATOM   9250  C  CG     . ARG   C 1  320 ? 0.641   -39.915  0.718    1.00 40.56  ? 320 ARG   C CG     1 
ATOM   9251  C  CD     . ARG   C 1  320 ? 1.763   -39.440  1.600    1.00 47.53  ? 320 ARG   C CD     1 
ATOM   9252  N  NE     . ARG   C 1  320 ? 2.382   -40.551  2.308    1.00 48.59  ? 320 ARG   C NE     1 
ATOM   9253  C  CZ     . ARG   C 1  320 ? 3.204   -40.402  3.337    1.00 50.14  ? 320 ARG   C CZ     1 
ATOM   9254  N  NH1    . ARG   C 1  320 ? 3.569   -39.203  3.759    1.00 42.64  ? 320 ARG   C NH1    1 
ATOM   9255  N  NH2    . ARG   C 1  320 ? 3.661   -41.483  3.967    1.00 50.92  ? 320 ARG   C NH2    1 
ATOM   9256  N  N      . GLY   C 1  321 ? -1.337  -42.768  -0.786   1.00 36.43  ? 321 GLY   C N      1 
ATOM   9257  C  CA     . GLY   C 1  321 ? -2.667  -43.231  -0.465   1.00 46.71  ? 321 GLY   C CA     1 
ATOM   9258  C  C      . GLY   C 1  321 ? -3.441  -43.839  -1.623   1.00 46.99  ? 321 GLY   C C      1 
ATOM   9259  O  O      . GLY   C 1  321 ? -2.862  -44.412  -2.547   1.00 44.24  ? 321 GLY   C O      1 
ATOM   9260  N  N      . ASP   C 1  322 ? -4.771  -43.717  -1.576   1.00 47.95  ? 322 ASP   C N      1 
ATOM   9261  C  CA     . ASP   C 1  322 ? -5.643  -44.332  -2.569   1.00 50.91  ? 322 ASP   C CA     1 
ATOM   9262  C  C      . ASP   C 1  322 ? -5.557  -43.618  -3.917   1.00 49.67  ? 322 ASP   C C      1 
ATOM   9263  O  O      . ASP   C 1  322 ? -6.383  -42.745  -4.218   1.00 42.81  ? 322 ASP   C O      1 
ATOM   9264  C  CB     . ASP   C 1  322 ? -7.088  -44.336  -2.085   1.00 47.93  ? 322 ASP   C CB     1 
ATOM   9265  C  CG     . ASP   C 1  322 ? -8.001  -45.035  -3.056   1.00 53.04  ? 322 ASP   C CG     1 
ATOM   9266  O  OD1    . ASP   C 1  322 ? -7.584  -46.091  -3.588   1.00 53.54  ? 322 ASP   C OD1    1 
ATOM   9267  O  OD2    . ASP   C 1  322 ? -9.107  -44.516  -3.322   1.00 56.48  ? 322 ASP   C OD2    1 
ATOM   9268  N  N      . VAL   C 1  323 ? -4.583  -44.006  -4.745   1.00 42.45  ? 323 VAL   C N      1 
ATOM   9269  C  CA     . VAL   C 1  323 ? -4.338  -43.387  -6.046   1.00 42.10  ? 323 VAL   C CA     1 
ATOM   9270  C  C      . VAL   C 1  323 ? -3.849  -44.463  -7.010   1.00 46.14  ? 323 VAL   C C      1 
ATOM   9271  O  O      . VAL   C 1  323 ? -3.020  -45.306  -6.647   1.00 44.53  ? 323 VAL   C O      1 
ATOM   9272  C  CB     . VAL   C 1  323 ? -3.314  -42.230  -5.957   1.00 40.64  ? 323 VAL   C CB     1 
ATOM   9273  C  CG1    . VAL   C 1  323 ? -3.096  -41.568  -7.321   1.00 36.58  ? 323 VAL   C CG1    1 
ATOM   9274  C  CG2    . VAL   C 1  323 ? -3.751  -41.202  -4.913   1.00 34.11  ? 323 VAL   C CG2    1 
ATOM   9275  N  N      . VAL   C 1  324 ? -4.375  -44.441  -8.237   1.00 46.22  ? 324 VAL   C N      1 
ATOM   9276  C  CA     . VAL   C 1  324 ? -4.013  -45.405  -9.278   1.00 41.19  ? 324 VAL   C CA     1 
ATOM   9277  C  C      . VAL   C 1  324 ? -3.678  -44.636  -10.541  1.00 39.52  ? 324 VAL   C C      1 
ATOM   9278  O  O      . VAL   C 1  324 ? -4.233  -43.552  -10.758  1.00 45.77  ? 324 VAL   C O      1 
ATOM   9279  C  CB     . VAL   C 1  324 ? -5.143  -46.397  -9.578   1.00 40.38  ? 324 VAL   C CB     1 
ATOM   9280  C  CG1    . VAL   C 1  324 ? -5.671  -47.040  -8.329   1.00 32.65  ? 324 VAL   C CG1    1 
ATOM   9281  C  CG2    . VAL   C 1  324 ? -6.247  -45.685  -10.379  1.00 39.99  ? 324 VAL   C CG2    1 
ATOM   9282  N  N      . PRO   C 1  325 ? -2.824  -45.171  -11.415  1.00 42.10  ? 325 PRO   C N      1 
ATOM   9283  C  CA     . PRO   C 1  325 ? -2.332  -44.349  -12.539  1.00 35.83  ? 325 PRO   C CA     1 
ATOM   9284  C  C      . PRO   C 1  325 ? -3.428  -43.841  -13.466  1.00 41.80  ? 325 PRO   C C      1 
ATOM   9285  O  O      . PRO   C 1  325 ? -3.363  -42.683  -13.902  1.00 41.09  ? 325 PRO   C O      1 
ATOM   9286  C  CB     . PRO   C 1  325 ? -1.338  -45.292  -13.229  1.00 31.57  ? 325 PRO   C CB     1 
ATOM   9287  C  CG     . PRO   C 1  325 ? -0.759  -46.085  -12.055  1.00 37.01  ? 325 PRO   C CG     1 
ATOM   9288  C  CD     . PRO   C 1  325 ? -1.975  -46.358  -11.177  1.00 41.48  ? 325 PRO   C CD     1 
ATOM   9289  N  N      . LYS   C 1  326 ? -4.448  -44.657  -13.759  1.00 46.98  ? 326 LYS   C N      1 
ATOM   9290  C  CA     . LYS   C 1  326 ? -5.565  -44.219  -14.602  1.00 45.07  ? 326 LYS   C CA     1 
ATOM   9291  C  C      . LYS   C 1  326 ? -6.108  -42.851  -14.181  1.00 45.57  ? 326 LYS   C C      1 
ATOM   9292  O  O      . LYS   C 1  326 ? -6.279  -41.951  -15.018  1.00 39.82  ? 326 LYS   C O      1 
ATOM   9293  C  CB     . LYS   C 1  326 ? -6.679  -45.270  -14.561  1.00 48.40  ? 326 LYS   C CB     1 
ATOM   9294  C  CG     . LYS   C 1  326 ? -7.643  -45.229  -15.739  1.00 56.98  ? 326 LYS   C CG     1 
ATOM   9295  C  CD     . LYS   C 1  326 ? -9.012  -44.645  -15.386  1.00 61.74  ? 326 LYS   C CD     1 
ATOM   9296  C  CE     . LYS   C 1  326 ? -9.755  -44.176  -16.666  1.00 73.35  ? 326 LYS   C CE     1 
ATOM   9297  N  NZ     . LYS   C 1  326 ? -9.012  -43.174  -17.519  1.00 58.64  ? 326 LYS   C NZ     1 
ATOM   9298  N  N      . ASP   C 1  327 ? -6.398  -42.683  -12.881  1.00 44.87  ? 327 ASP   C N      1 
ATOM   9299  C  CA     . ASP   C 1  327 ? -6.900  -41.405  -12.377  1.00 44.86  ? 327 ASP   C CA     1 
ATOM   9300  C  C      . ASP   C 1  327 ? -5.889  -40.296  -12.591  1.00 44.02  ? 327 ASP   C C      1 
ATOM   9301  O  O      . ASP   C 1  327 ? -6.186  -39.285  -13.242  1.00 42.70  ? 327 ASP   C O      1 
ATOM   9302  C  CB     . ASP   C 1  327 ? -7.251  -41.510  -10.896  1.00 45.03  ? 327 ASP   C CB     1 
ATOM   9303  C  CG     . ASP   C 1  327 ? -8.290  -42.559  -10.634  1.00 53.25  ? 327 ASP   C CG     1 
ATOM   9304  O  OD1    . ASP   C 1  327 ? -9.175  -42.691  -11.514  1.00 49.86  ? 327 ASP   C OD1    1 
ATOM   9305  O  OD2    . ASP   C 1  327 ? -8.196  -43.253  -9.583   1.00 51.09  ? 327 ASP   C OD2    1 
ATOM   9306  N  N      . VAL   C 1  328 ? -4.690  -40.467  -12.034  1.00 37.81  ? 328 VAL   C N      1 
ATOM   9307  C  CA     . VAL   C 1  328 ? -3.587  -39.549  -12.275  1.00 39.60  ? 328 VAL   C CA     1 
ATOM   9308  C  C      . VAL   C 1  328 ? -3.551  -39.113  -13.737  1.00 39.28  ? 328 VAL   C C      1 
ATOM   9309  O  O      . VAL   C 1  328 ? -3.603  -37.916  -14.036  1.00 39.59  ? 328 VAL   C O      1 
ATOM   9310  C  CB     . VAL   C 1  328 ? -2.244  -40.168  -11.853  1.00 37.32  ? 328 VAL   C CB     1 
ATOM   9311  C  CG1    . VAL   C 1  328 ? -1.112  -39.238  -12.274  1.00 32.20  ? 328 VAL   C CG1    1 
ATOM   9312  C  CG2    . VAL   C 1  328 ? -2.232  -40.386  -10.344  1.00 30.39  ? 328 VAL   C CG2    1 
ATOM   9313  N  N      . ASN   C 1  329 ? -3.478  -40.063  -14.670  1.00 43.35  ? 329 ASN   C N      1 
ATOM   9314  C  CA     . ASN   C 1  329 ? -3.398  -39.651  -16.071  1.00 42.93  ? 329 ASN   C CA     1 
ATOM   9315  C  C      . ASN   C 1  329 ? -4.607  -38.826  -16.480  1.00 44.25  ? 329 ASN   C C      1 
ATOM   9316  O  O      . ASN   C 1  329 ? -4.463  -37.814  -17.175  1.00 48.98  ? 329 ASN   C O      1 
ATOM   9317  C  CB     . ASN   C 1  329 ? -3.247  -40.858  -16.975  1.00 44.76  ? 329 ASN   C CB     1 
ATOM   9318  C  CG     . ASN   C 1  329 ? -1.972  -41.584  -16.730  1.00 51.93  ? 329 ASN   C CG     1 
ATOM   9319  O  OD1    . ASN   C 1  329 ? -0.921  -40.953  -16.545  1.00 61.55  ? 329 ASN   C OD1    1 
ATOM   9320  N  ND2    . ASN   C 1  329 ? -2.036  -42.919  -16.706  1.00 45.87  ? 329 ASN   C ND2    1 
ATOM   9321  N  N      . ALA   C 1  330 ? -5.810  -39.224  -16.056  1.00 44.26  ? 330 ALA   C N      1 
ATOM   9322  C  CA     . ALA   C 1  330 ? -6.980  -38.419  -16.394  1.00 44.77  ? 330 ALA   C CA     1 
ATOM   9323  C  C      . ALA   C 1  330 ? -6.804  -36.979  -15.911  1.00 48.11  ? 330 ALA   C C      1 
ATOM   9324  O  O      . ALA   C 1  330 ? -6.936  -36.028  -16.695  1.00 44.51  ? 330 ALA   C O      1 
ATOM   9325  C  CB     . ALA   C 1  330 ? -8.231  -39.058  -15.807  1.00 40.16  ? 330 ALA   C CB     1 
ATOM   9326  N  N      . ALA   C 1  331 ? -6.433  -36.814  -14.629  1.00 45.24  ? 331 ALA   C N      1 
ATOM   9327  C  CA     . ALA   C 1  331 ? -6.339  -35.492  -14.010  1.00 44.03  ? 331 ALA   C CA     1 
ATOM   9328  C  C      . ALA   C 1  331 ? -5.305  -34.609  -14.697  1.00 45.98  ? 331 ALA   C C      1 
ATOM   9329  O  O      . ALA   C 1  331 ? -5.564  -33.429  -14.942  1.00 44.08  ? 331 ALA   C O      1 
ATOM   9330  C  CB     . ALA   C 1  331 ? -6.017  -35.635  -12.525  1.00 39.52  ? 331 ALA   C CB     1 
ATOM   9331  N  N      . ILE   C 1  332 ? -4.125  -35.158  -15.010  1.00 48.74  ? 332 ILE   C N      1 
ATOM   9332  C  CA     . ILE   C 1  332 ? -3.088  -34.376  -15.687  1.00 48.95  ? 332 ILE   C CA     1 
ATOM   9333  C  C      . ILE   C 1  332 ? -3.587  -33.874  -17.037  1.00 49.86  ? 332 ILE   C C      1 
ATOM   9334  O  O      . ILE   C 1  332 ? -3.315  -32.730  -17.434  1.00 45.84  ? 332 ILE   C O      1 
ATOM   9335  C  CB     . ILE   C 1  332 ? -1.795  -35.206  -15.828  1.00 44.41  ? 332 ILE   C CB     1 
ATOM   9336  C  CG1    . ILE   C 1  332 ? -1.204  -35.470  -14.448  1.00 36.67  ? 332 ILE   C CG1    1 
ATOM   9337  C  CG2    . ILE   C 1  332 ? -0.760  -34.476  -16.705  1.00 40.07  ? 332 ILE   C CG2    1 
ATOM   9338  C  CD1    . ILE   C 1  332 ? -0.017  -36.367  -14.459  1.00 39.68  ? 332 ILE   C CD1    1 
ATOM   9339  N  N      . ALA   C 1  333 ? -4.343  -34.714  -17.754  1.00 49.47  ? 333 ALA   C N      1 
ATOM   9340  C  CA     . ALA   C 1  333 ? -4.805  -34.341  -19.087  1.00 43.53  ? 333 ALA   C CA     1 
ATOM   9341  C  C      . ALA   C 1  333 ? -5.775  -33.172  -19.027  1.00 52.60  ? 333 ALA   C C      1 
ATOM   9342  O  O      . ALA   C 1  333 ? -5.690  -32.244  -19.844  1.00 57.91  ? 333 ALA   C O      1 
ATOM   9343  C  CB     . ALA   C 1  333 ? -5.443  -35.541  -19.766  1.00 40.49  ? 333 ALA   C CB     1 
ATOM   9344  N  N      . THR   C 1  334 ? -6.702  -33.187  -18.063  1.00 46.23  ? 334 THR   C N      1 
ATOM   9345  C  CA     . THR   C 1  334 ? -7.578  -32.034  -17.898  1.00 55.70  ? 334 THR   C CA     1 
ATOM   9346  C  C      . THR   C 1  334 ? -6.771  -30.790  -17.542  1.00 59.21  ? 334 THR   C C      1 
ATOM   9347  O  O      . THR   C 1  334 ? -6.938  -29.727  -18.155  1.00 62.74  ? 334 THR   C O      1 
ATOM   9348  C  CB     . THR   C 1  334 ? -8.645  -32.318  -16.842  1.00 57.35  ? 334 THR   C CB     1 
ATOM   9349  O  OG1    . THR   C 1  334 ? -8.026  -32.427  -15.555  1.00 66.38  ? 334 THR   C OG1    1 
ATOM   9350  C  CG2    . THR   C 1  334 ? -9.375  -33.617  -17.154  1.00 54.27  ? 334 THR   C CG2    1 
ATOM   9351  N  N      . ILE   C 1  335 ? -5.852  -30.917  -16.584  1.00 53.57  ? 335 ILE   C N      1 
ATOM   9352  C  CA     . ILE   C 1  335 ? -5.096  -29.750  -16.139  1.00 55.99  ? 335 ILE   C CA     1 
ATOM   9353  C  C      . ILE   C 1  335 ? -4.329  -29.131  -17.298  1.00 59.98  ? 335 ILE   C C      1 
ATOM   9354  O  O      . ILE   C 1  335 ? -4.264  -27.903  -17.430  1.00 60.17  ? 335 ILE   C O      1 
ATOM   9355  C  CB     . ILE   C 1  335 ? -4.158  -30.122  -14.980  1.00 50.69  ? 335 ILE   C CB     1 
ATOM   9356  C  CG1    . ILE   C 1  335 ? -4.913  -30.044  -13.651  1.00 48.48  ? 335 ILE   C CG1    1 
ATOM   9357  C  CG2    . ILE   C 1  335 ? -2.941  -29.209  -14.984  1.00 48.32  ? 335 ILE   C CG2    1 
ATOM   9358  C  CD1    . ILE   C 1  335 ? -4.436  -31.067  -12.609  1.00 48.98  ? 335 ILE   C CD1    1 
ATOM   9359  N  N      . LYS   C 1  336 ? -3.731  -29.966  -18.153  1.00 60.60  ? 336 LYS   C N      1 
ATOM   9360  C  CA     . LYS   C 1  336 ? -2.914  -29.431  -19.237  1.00 62.20  ? 336 LYS   C CA     1 
ATOM   9361  C  C      . LYS   C 1  336 ? -3.713  -28.506  -20.145  1.00 71.25  ? 336 LYS   C C      1 
ATOM   9362  O  O      . LYS   C 1  336 ? -3.165  -27.515  -20.650  1.00 75.99  ? 336 LYS   C O      1 
ATOM   9363  C  CB     . LYS   C 1  336 ? -2.291  -30.568  -20.039  1.00 57.76  ? 336 LYS   C CB     1 
ATOM   9364  C  CG     . LYS   C 1  336 ? -0.866  -30.818  -19.634  1.00 57.99  ? 336 LYS   C CG     1 
ATOM   9365  C  CD     . LYS   C 1  336 ? -0.408  -32.221  -19.937  1.00 53.58  ? 336 LYS   C CD     1 
ATOM   9366  C  CE     . LYS   C 1  336 ? 0.790   -32.542  -19.050  1.00 58.47  ? 336 LYS   C CE     1 
ATOM   9367  N  NZ     . LYS   C 1  336 ? 2.072   -32.084  -19.664  1.00 49.72  ? 336 LYS   C NZ     1 
ATOM   9368  N  N      . THR   C 1  337 ? -5.005  -28.792  -20.347  1.00 65.00  ? 337 THR   C N      1 
ATOM   9369  C  CA     . THR   C 1  337 ? -5.822  -27.950  -21.212  1.00 66.91  ? 337 THR   C CA     1 
ATOM   9370  C  C      . THR   C 1  337 ? -6.391  -26.740  -20.481  1.00 72.00  ? 337 THR   C C      1 
ATOM   9371  O  O      . THR   C 1  337 ? -6.584  -25.681  -21.091  1.00 78.09  ? 337 THR   C O      1 
ATOM   9372  C  CB     . THR   C 1  337 ? -6.986  -28.747  -21.823  1.00 71.10  ? 337 THR   C CB     1 
ATOM   9373  O  OG1    . THR   C 1  337 ? -8.127  -28.661  -20.960  1.00 66.23  ? 337 THR   C OG1    1 
ATOM   9374  C  CG2    . THR   C 1  337 ? -6.621  -30.220  -22.027  1.00 67.95  ? 337 THR   C CG2    1 
ATOM   9375  N  N      . LYS   C 1  338 ? -6.644  -26.859  -19.186  1.00 72.23  ? 338 LYS   C N      1 
ATOM   9376  C  CA     . LYS   C 1  338 ? -7.327  -25.815  -18.438  1.00 71.14  ? 338 LYS   C CA     1 
ATOM   9377  C  C      . LYS   C 1  338 ? -6.390  -24.949  -17.598  1.00 73.10  ? 338 LYS   C C      1 
ATOM   9378  O  O      . LYS   C 1  338 ? -6.868  -24.048  -16.898  1.00 75.30  ? 338 LYS   C O      1 
ATOM   9379  C  CB     . LYS   C 1  338 ? -8.404  -26.448  -17.548  1.00 59.60  ? 338 LYS   C CB     1 
ATOM   9380  C  CG     . LYS   C 1  338 ? -9.537  -27.042  -18.358  1.00 64.36  ? 338 LYS   C CG     1 
ATOM   9381  C  CD     . LYS   C 1  338 ? -10.492 -27.820  -17.499  1.00 67.32  ? 338 LYS   C CD     1 
ATOM   9382  C  CE     . LYS   C 1  338 ? -11.869 -27.818  -18.122  1.00 67.57  ? 338 LYS   C CE     1 
ATOM   9383  N  NZ     . LYS   C 1  338 ? -12.636 -26.571  -17.742  1.00 79.08  ? 338 LYS   C NZ     1 
ATOM   9384  N  N      . ARG   C 1  339 ? -5.076  -25.179  -17.647  1.00 71.23  ? 339 ARG   C N      1 
ATOM   9385  C  CA     . ARG   C 1  339 ? -4.159  -24.409  -16.823  1.00 66.82  ? 339 ARG   C CA     1 
ATOM   9386  C  C      . ARG   C 1  339 ? -2.974  -23.884  -17.621  1.00 72.53  ? 339 ARG   C C      1 
ATOM   9387  O  O      . ARG   C 1  339 ? -2.673  -24.327  -18.738  1.00 72.04  ? 339 ARG   C O      1 
ATOM   9388  C  CB     . ARG   C 1  339 ? -3.652  -25.198  -15.615  1.00 60.90  ? 339 ARG   C CB     1 
ATOM   9389  C  CG     . ARG   C 1  339 ? -4.572  -24.984  -14.450  1.00 64.57  ? 339 ARG   C CG     1 
ATOM   9390  C  CD     . ARG   C 1  339 ? -3.805  -24.716  -13.171  1.00 65.84  ? 339 ARG   C CD     1 
ATOM   9391  N  NE     . ARG   C 1  339 ? -4.659  -24.536  -11.996  1.00 59.70  ? 339 ARG   C NE     1 
ATOM   9392  C  CZ     . ARG   C 1  339 ? -5.494  -25.454  -11.524  1.00 63.55  ? 339 ARG   C CZ     1 
ATOM   9393  N  NH1    . ARG   C 1  339 ? -5.717  -26.591  -12.172  1.00 68.01  ? 339 ARG   C NH1    1 
ATOM   9394  N  NH2    . ARG   C 1  339 ? -6.115  -25.234  -10.370  1.00 55.74  ? 339 ARG   C NH2    1 
ATOM   9395  N  N      . SER   C 1  340 ? -2.308  -22.915  -16.995  1.00 71.12  ? 340 SER   C N      1 
ATOM   9396  C  CA     . SER   C 1  340 ? -1.221  -22.148  -17.596  1.00 74.81  ? 340 SER   C CA     1 
ATOM   9397  C  C      . SER   C 1  340 ? 0.093   -22.823  -17.203  1.00 69.08  ? 340 SER   C C      1 
ATOM   9398  O  O      . SER   C 1  340 ? 0.638   -22.562  -16.122  1.00 71.03  ? 340 SER   C O      1 
ATOM   9399  C  CB     . SER   C 1  340 ? -1.298  -20.695  -17.123  1.00 75.51  ? 340 SER   C CB     1 
ATOM   9400  O  OG     . SER   C 1  340 ? -0.334  -19.858  -17.750  1.00 83.24  ? 340 SER   C OG     1 
ATOM   9401  N  N      . ILE   C 1  341 ? 0.610   -23.705  -18.065  1.00 58.26  ? 341 ILE   C N      1 
ATOM   9402  C  CA     . ILE   C 1  341 ? 1.799   -24.498  -17.743  1.00 56.47  ? 341 ILE   C CA     1 
ATOM   9403  C  C      . ILE   C 1  341 ? 2.761   -24.432  -18.927  1.00 54.66  ? 341 ILE   C C      1 
ATOM   9404  O  O      . ILE   C 1  341 ? 2.799   -25.337  -19.763  1.00 55.55  ? 341 ILE   C O      1 
ATOM   9405  C  CB     . ILE   C 1  341 ? 1.464   -25.948  -17.385  1.00 58.48  ? 341 ILE   C CB     1 
ATOM   9406  C  CG1    . ILE   C 1  341 ? 0.637   -26.022  -16.115  1.00 54.62  ? 341 ILE   C CG1    1 
ATOM   9407  C  CG2    . ILE   C 1  341 ? 2.731   -26.753  -17.137  1.00 55.69  ? 341 ILE   C CG2    1 
ATOM   9408  C  CD1    . ILE   C 1  341 ? -0.376  -27.145  -16.142  1.00 57.49  ? 341 ILE   C CD1    1 
ATOM   9409  N  N      . GLN   C 1  342 ? 3.580   -23.385  -18.981  1.00 50.18  ? 342 GLN   C N      1 
ATOM   9410  C  CA     . GLN   C 1  342 ? 4.545   -23.236  -20.054  1.00 45.66  ? 342 GLN   C CA     1 
ATOM   9411  C  C      . GLN   C 1  342 ? 5.887   -23.823  -19.624  1.00 45.13  ? 342 GLN   C C      1 
ATOM   9412  O  O      . GLN   C 1  342 ? 6.439   -23.426  -18.591  1.00 42.23  ? 342 GLN   C O      1 
ATOM   9413  C  CB     . GLN   C 1  342 ? 4.699   -21.769  -20.444  1.00 50.06  ? 342 GLN   C CB     1 
ATOM   9414  C  CG     . GLN   C 1  342 ? 5.195   -21.603  -21.873  1.00 70.81  ? 342 GLN   C CG     1 
ATOM   9415  C  CD     . GLN   C 1  342 ? 4.084   -21.719  -22.930  1.00 85.80  ? 342 GLN   C CD     1 
ATOM   9416  O  OE1    . GLN   C 1  342 ? 2.921   -21.366  -22.677  1.00 76.62  ? 342 GLN   C OE1    1 
ATOM   9417  N  NE2    . GLN   C 1  342 ? 4.446   -22.224  -24.122  1.00 80.59  ? 342 GLN   C NE2    1 
ATOM   9418  N  N      . PHE   C 1  343 ? 6.409   -24.761  -20.416  1.00 39.70  ? 343 PHE   C N      1 
ATOM   9419  C  CA     . PHE   C 1  343 ? 7.733   -25.328  -20.226  1.00 32.51  ? 343 PHE   C CA     1 
ATOM   9420  C  C      . PHE   C 1  343 ? 8.748   -24.517  -21.015  1.00 42.15  ? 343 PHE   C C      1 
ATOM   9421  O  O      . PHE   C 1  343 ? 8.426   -23.937  -22.056  1.00 37.38  ? 343 PHE   C O      1 
ATOM   9422  C  CB     . PHE   C 1  343 ? 7.789   -26.773  -20.696  1.00 33.87  ? 343 PHE   C CB     1 
ATOM   9423  C  CG     . PHE   C 1  343 ? 7.348   -27.778  -19.674  1.00 41.00  ? 343 PHE   C CG     1 
ATOM   9424  C  CD1    . PHE   C 1  343 ? 6.000   -28.047  -19.477  1.00 43.36  ? 343 PHE   C CD1    1 
ATOM   9425  C  CD2    . PHE   C 1  343 ? 8.284   -28.481  -18.918  1.00 39.19  ? 343 PHE   C CD2    1 
ATOM   9426  C  CE1    . PHE   C 1  343 ? 5.578   -28.989  -18.528  1.00 41.78  ? 343 PHE   C CE1    1 
ATOM   9427  C  CE2    . PHE   C 1  343 ? 7.868   -29.412  -17.969  1.00 41.21  ? 343 PHE   C CE2    1 
ATOM   9428  C  CZ     . PHE   C 1  343 ? 6.511   -29.672  -17.781  1.00 40.27  ? 343 PHE   C CZ     1 
ATOM   9429  N  N      . VAL   C 1  344 ? 9.987   -24.462  -20.506  1.00 43.31  ? 344 VAL   C N      1 
ATOM   9430  C  CA     . VAL   C 1  344 ? 11.053  -23.919  -21.332  1.00 40.91  ? 344 VAL   C CA     1 
ATOM   9431  C  C      . VAL   C 1  344 ? 11.212  -24.798  -22.575  1.00 35.89  ? 344 VAL   C C      1 
ATOM   9432  O  O      . VAL   C 1  344 ? 10.770  -25.951  -22.620  1.00 38.68  ? 344 VAL   C O      1 
ATOM   9433  C  CB     . VAL   C 1  344 ? 12.369  -23.788  -20.551  1.00 40.30  ? 344 VAL   C CB     1 
ATOM   9434  C  CG1    . VAL   C 1  344 ? 12.107  -23.012  -19.298  1.00 43.76  ? 344 VAL   C CG1    1 
ATOM   9435  C  CG2    . VAL   C 1  344 ? 12.964  -25.136  -20.220  1.00 39.57  ? 344 VAL   C CG2    1 
ATOM   9436  N  N      . ASP   C 1  345 ? 11.791  -24.227  -23.619  1.00 36.62  ? 345 ASP   C N      1 
ATOM   9437  C  CA     . ASP   C 1  345 ? 11.733  -24.970  -24.871  1.00 38.85  ? 345 ASP   C CA     1 
ATOM   9438  C  C      . ASP   C 1  345 ? 12.724  -26.115  -24.936  1.00 43.99  ? 345 ASP   C C      1 
ATOM   9439  O  O      . ASP   C 1  345 ? 12.665  -26.897  -25.886  1.00 44.47  ? 345 ASP   C O      1 
ATOM   9440  C  CB     . ASP   C 1  345 ? 11.950  -24.057  -26.078  1.00 37.34  ? 345 ASP   C CB     1 
ATOM   9441  C  CG     . ASP   C 1  345 ? 13.361  -23.504  -26.170  1.00 44.55  ? 345 ASP   C CG     1 
ATOM   9442  O  OD1    . ASP   C 1  345 ? 14.294  -24.117  -25.596  1.00 41.23  ? 345 ASP   C OD1    1 
ATOM   9443  O  OD2    . ASP   C 1  345 ? 13.524  -22.450  -26.840  1.00 46.31  ? 345 ASP   C OD2    1 
ATOM   9444  N  N      . TRP   C 1  346 ? 13.634  -26.227  -23.970  1.00 42.95  ? 346 TRP   C N      1 
ATOM   9445  C  CA     . TRP   C 1  346 ? 14.704  -27.197  -24.051  1.00 35.46  ? 346 TRP   C CA     1 
ATOM   9446  C  C      . TRP   C 1  346 ? 14.455  -28.415  -23.183  1.00 39.82  ? 346 TRP   C C      1 
ATOM   9447  O  O      . TRP   C 1  346 ? 15.362  -29.235  -22.997  1.00 43.57  ? 346 TRP   C O      1 
ATOM   9448  C  CB     . TRP   C 1  346 ? 16.033  -26.546  -23.677  1.00 36.42  ? 346 TRP   C CB     1 
ATOM   9449  C  CG     . TRP   C 1  346 ? 16.022  -25.716  -22.417  1.00 39.47  ? 346 TRP   C CG     1 
ATOM   9450  C  CD1    . TRP   C 1  346 ? 15.933  -24.362  -22.337  1.00 38.68  ? 346 TRP   C CD1    1 
ATOM   9451  C  CD2    . TRP   C 1  346 ? 16.153  -26.193  -21.057  1.00 35.96  ? 346 TRP   C CD2    1 
ATOM   9452  N  NE1    . TRP   C 1  346 ? 15.982  -23.960  -21.021  1.00 38.89  ? 346 TRP   C NE1    1 
ATOM   9453  C  CE2    . TRP   C 1  346 ? 16.117  -25.062  -20.216  1.00 36.06  ? 346 TRP   C CE2    1 
ATOM   9454  C  CE3    . TRP   C 1  346 ? 16.301  -27.465  -20.478  1.00 35.18  ? 346 TRP   C CE3    1 
ATOM   9455  C  CZ2    . TRP   C 1  346 ? 16.225  -25.157  -18.822  1.00 35.86  ? 346 TRP   C CZ2    1 
ATOM   9456  C  CZ3    . TRP   C 1  346 ? 16.396  -27.565  -19.092  1.00 36.73  ? 346 TRP   C CZ3    1 
ATOM   9457  C  CH2    . TRP   C 1  346 ? 16.359  -26.413  -18.279  1.00 36.93  ? 346 TRP   C CH2    1 
ATOM   9458  N  N      . CYS   C 1  347 ? 13.260  -28.571  -22.645  1.00 34.91  ? 347 CYS   C N      1 
ATOM   9459  C  CA     . CYS   C 1  347 ? 13.095  -29.737  -21.804  1.00 42.55  ? 347 CYS   C CA     1 
ATOM   9460  C  C      . CYS   C 1  347 ? 11.713  -30.324  -22.016  1.00 37.35  ? 347 CYS   C C      1 
ATOM   9461  O  O      . CYS   C 1  347 ? 10.758  -29.590  -22.284  1.00 40.43  ? 347 CYS   C O      1 
ATOM   9462  C  CB     . CYS   C 1  347 ? 13.330  -29.387  -20.322  1.00 48.44  ? 347 CYS   C CB     1 
ATOM   9463  S  SG     . CYS   C 1  347 ? 11.892  -29.277  -19.315  1.00 57.65  ? 347 CYS   C SG     1 
ATOM   9464  N  N      . PRO   C 1  348 ? 11.585  -31.645  -21.921  1.00 42.13  ? 348 PRO   C N      1 
ATOM   9465  C  CA     . PRO   C 1  348 ? 10.302  -32.303  -22.216  1.00 37.01  ? 348 PRO   C CA     1 
ATOM   9466  C  C      . PRO   C 1  348 ? 9.236   -31.846  -21.241  1.00 44.37  ? 348 PRO   C C      1 
ATOM   9467  O  O      . PRO   C 1  348 ? 9.528   -31.400  -20.129  1.00 52.27  ? 348 PRO   C O      1 
ATOM   9468  C  CB     . PRO   C 1  348 ? 10.598  -33.793  -22.021  1.00 32.06  ? 348 PRO   C CB     1 
ATOM   9469  C  CG     . PRO   C 1  348 ? 12.041  -33.882  -21.543  1.00 42.34  ? 348 PRO   C CG     1 
ATOM   9470  C  CD     . PRO   C 1  348 ? 12.514  -32.513  -21.185  1.00 40.22  ? 348 PRO   C CD     1 
ATOM   9471  N  N      . THR   C 1  349 ? 7.985   -32.005  -21.648  1.00 38.98  ? 349 THR   C N      1 
ATOM   9472  C  CA     . THR   C 1  349 ? 6.863   -31.477  -20.897  1.00 45.92  ? 349 THR   C CA     1 
ATOM   9473  C  C      . THR   C 1  349 ? 6.058   -32.570  -20.196  1.00 45.50  ? 349 THR   C C      1 
ATOM   9474  O  O      . THR   C 1  349 ? 4.983   -32.295  -19.659  1.00 54.08  ? 349 THR   C O      1 
ATOM   9475  C  CB     . THR   C 1  349 ? 5.971   -30.642  -21.826  1.00 41.19  ? 349 THR   C CB     1 
ATOM   9476  O  OG1    . THR   C 1  349 ? 5.203   -31.524  -22.624  1.00 42.66  ? 349 THR   C OG1    1 
ATOM   9477  C  CG2    . THR   C 1  349 ? 6.817   -29.816  -22.749  1.00 38.80  ? 349 THR   C CG2    1 
ATOM   9478  N  N      . GLY   C 1  350 ? 6.547   -33.794  -20.156  1.00 39.17  ? 350 GLY   C N      1 
ATOM   9479  C  CA     . GLY   C 1  350 ? 5.839   -34.819  -19.415  1.00 47.44  ? 350 GLY   C CA     1 
ATOM   9480  C  C      . GLY   C 1  350 ? 5.895   -34.577  -17.919  1.00 47.93  ? 350 GLY   C C      1 
ATOM   9481  O  O      . GLY   C 1  350 ? 6.812   -33.945  -17.398  1.00 62.71  ? 350 GLY   C O      1 
ATOM   9482  N  N      . PHE   C 1  351 ? 4.890   -35.070  -17.217  1.00 42.98  ? 351 PHE   C N      1 
ATOM   9483  C  CA     . PHE   C 1  351 ? 4.899   -35.067  -15.762  1.00 41.59  ? 351 PHE   C CA     1 
ATOM   9484  C  C      . PHE   C 1  351 ? 5.411   -36.407  -15.267  1.00 34.45  ? 351 PHE   C C      1 
ATOM   9485  O  O      . PHE   C 1  351 ? 5.036   -37.451  -15.791  1.00 44.25  ? 351 PHE   C O      1 
ATOM   9486  C  CB     . PHE   C 1  351 ? 3.499   -34.830  -15.199  1.00 44.99  ? 351 PHE   C CB     1 
ATOM   9487  C  CG     . PHE   C 1  351 ? 2.983   -33.443  -15.398  1.00 53.52  ? 351 PHE   C CG     1 
ATOM   9488  C  CD1    . PHE   C 1  351 ? 3.600   -32.571  -16.279  1.00 54.91  ? 351 PHE   C CD1    1 
ATOM   9489  C  CD2    . PHE   C 1  351 ? 1.886   -32.998  -14.680  1.00 53.63  ? 351 PHE   C CD2    1 
ATOM   9490  C  CE1    . PHE   C 1  351 ? 3.118   -31.285  -16.451  1.00 51.35  ? 351 PHE   C CE1    1 
ATOM   9491  C  CE2    . PHE   C 1  351 ? 1.408   -31.711  -14.844  1.00 47.80  ? 351 PHE   C CE2    1 
ATOM   9492  C  CZ     . PHE   C 1  351 ? 2.027   -30.856  -15.740  1.00 47.63  ? 351 PHE   C CZ     1 
ATOM   9493  N  N      . LYS   C 1  352 ? 6.272   -36.378  -14.271  1.00 35.06  ? 352 LYS   C N      1 
ATOM   9494  C  CA     . LYS   C 1  352 ? 6.811   -37.591  -13.666  1.00 35.56  ? 352 LYS   C CA     1 
ATOM   9495  C  C      . LYS   C 1  352 ? 6.063   -37.869  -12.373  1.00 35.17  ? 352 LYS   C C      1 
ATOM   9496  O  O      . LYS   C 1  352 ? 6.027   -37.020  -11.473  1.00 39.18  ? 352 LYS   C O      1 
ATOM   9497  C  CB     . LYS   C 1  352 ? 8.311   -37.461  -13.409  1.00 37.89  ? 352 LYS   C CB     1 
ATOM   9498  C  CG     . LYS   C 1  352 ? 9.040   -38.777  -13.273  1.00 37.20  ? 352 LYS   C CG     1 
ATOM   9499  C  CD     . LYS   C 1  352 ? 10.326  -38.591  -12.480  1.00 42.53  ? 352 LYS   C CD     1 
ATOM   9500  C  CE     . LYS   C 1  352 ? 11.156  -39.882  -12.344  1.00 44.51  ? 352 LYS   C CE     1 
ATOM   9501  N  NZ     . LYS   C 1  352 ? 10.384  -41.147  -12.506  1.00 45.72  ? 352 LYS   C NZ     1 
ATOM   9502  N  N      . VAL   C 1  353 ? 5.489   -39.062  -12.280  1.00 39.90  ? 353 VAL   C N      1 
ATOM   9503  C  CA     . VAL   C 1  353 ? 4.538   -39.430  -11.237  1.00 38.78  ? 353 VAL   C CA     1 
ATOM   9504  C  C      . VAL   C 1  353 ? 5.081   -40.574  -10.384  1.00 34.73  ? 353 VAL   C C      1 
ATOM   9505  O  O      . VAL   C 1  353 ? 5.594   -41.578  -10.890  1.00 40.37  ? 353 VAL   C O      1 
ATOM   9506  C  CB     . VAL   C 1  353 ? 3.186   -39.829  -11.868  1.00 37.49  ? 353 VAL   C CB     1 
ATOM   9507  C  CG1    . VAL   C 1  353 ? 2.277   -40.520  -10.831  1.00 35.21  ? 353 VAL   C CG1    1 
ATOM   9508  C  CG2    . VAL   C 1  353 ? 2.531   -38.626  -12.522  1.00 35.80  ? 353 VAL   C CG2    1 
ATOM   9509  N  N      . GLY   C 1  354 ? 4.922   -40.453  -9.088   1.00 34.71  ? 354 GLY   C N      1 
ATOM   9510  C  CA     . GLY   C 1  354 ? 5.163   -41.568  -8.202   1.00 38.71  ? 354 GLY   C CA     1 
ATOM   9511  C  C      . GLY   C 1  354 ? 3.991   -41.699  -7.256   1.00 37.87  ? 354 GLY   C C      1 
ATOM   9512  O  O      . GLY   C 1  354 ? 3.363   -40.712  -6.869   1.00 33.44  ? 354 GLY   C O      1 
ATOM   9513  N  N      . ILE   C 1  355 ? 3.702   -42.940  -6.887   1.00 36.08  ? 355 ILE   C N      1 
ATOM   9514  C  CA     . ILE   C 1  355 ? 2.551   -43.255  -6.062   1.00 36.09  ? 355 ILE   C CA     1 
ATOM   9515  C  C      . ILE   C 1  355 ? 3.042   -44.125  -4.923   1.00 38.23  ? 355 ILE   C C      1 
ATOM   9516  O  O      . ILE   C 1  355 ? 3.648   -45.174  -5.161   1.00 41.46  ? 355 ILE   C O      1 
ATOM   9517  C  CB     . ILE   C 1  355 ? 1.449   -43.968  -6.875   1.00 37.56  ? 355 ILE   C CB     1 
ATOM   9518  C  CG1    . ILE   C 1  355 ? 0.961   -43.075  -8.025   1.00 30.22  ? 355 ILE   C CG1    1 
ATOM   9519  C  CG2    . ILE   C 1  355 ? 0.301   -44.366  -5.977   1.00 42.06  ? 355 ILE   C CG2    1 
ATOM   9520  C  CD1    . ILE   C 1  355 ? -0.170  -43.625  -8.801   1.00 32.73  ? 355 ILE   C CD1    1 
ATOM   9521  N  N      . ASN   C 1  356 ? 2.804   -43.686  -3.691   1.00 40.11  ? 356 ASN   C N      1 
ATOM   9522  C  CA     . ASN   C 1  356 ? 2.993   -44.526  -2.518   1.00 44.32  ? 356 ASN   C CA     1 
ATOM   9523  C  C      . ASN   C 1  356 ? 1.638   -44.892  -1.955   1.00 47.37  ? 356 ASN   C C      1 
ATOM   9524  O  O      . ASN   C 1  356 ? 0.780   -44.030  -1.805   1.00 48.02  ? 356 ASN   C O      1 
ATOM   9525  C  CB     . ASN   C 1  356 ? 3.824   -43.857  -1.434   1.00 40.47  ? 356 ASN   C CB     1 
ATOM   9526  C  CG     . ASN   C 1  356 ? 5.205   -44.439  -1.362   1.00 58.17  ? 356 ASN   C CG     1 
ATOM   9527  O  OD1    . ASN   C 1  356 ? 5.416   -45.485  -0.740   1.00 69.79  ? 356 ASN   C OD1    1 
ATOM   9528  N  ND2    . ASN   C 1  356 ? 6.169   -43.767  -1.985   1.00 57.27  ? 356 ASN   C ND2    1 
ATOM   9529  N  N      . TYR   C 1  357 ? 1.445   -46.162  -1.622   1.00 52.24  ? 357 TYR   C N      1 
ATOM   9530  C  CA     . TYR   C 1  357 ? 0.093   -46.586  -1.295   1.00 51.25  ? 357 TYR   C CA     1 
ATOM   9531  C  C      . TYR   C 1  357 ? -0.282  -46.312  0.144    1.00 51.48  ? 357 TYR   C C      1 
ATOM   9532  O  O      . TYR   C 1  357 ? -1.458  -46.038  0.416    1.00 52.52  ? 357 TYR   C O      1 
ATOM   9533  C  CB     . TYR   C 1  357 ? -0.088  -48.060  -1.661   1.00 60.90  ? 357 TYR   C CB     1 
ATOM   9534  C  CG     . TYR   C 1  357 ? -0.330  -48.206  -3.162   1.00 64.34  ? 357 TYR   C CG     1 
ATOM   9535  C  CD1    . TYR   C 1  357 ? -1.258  -47.388  -3.800   1.00 64.60  ? 357 TYR   C CD1    1 
ATOM   9536  C  CD2    . TYR   C 1  357 ? 0.389   -49.116  -3.940   1.00 63.76  ? 357 TYR   C CD2    1 
ATOM   9537  C  CE1    . TYR   C 1  357 ? -1.492  -47.477  -5.150   1.00 65.65  ? 357 TYR   C CE1    1 
ATOM   9538  C  CE2    . TYR   C 1  357 ? 0.169   -49.210  -5.315   1.00 64.96  ? 357 TYR   C CE2    1 
ATOM   9539  C  CZ     . TYR   C 1  357 ? -0.777  -48.379  -5.909   1.00 72.54  ? 357 TYR   C CZ     1 
ATOM   9540  O  OH     . TYR   C 1  357 ? -1.056  -48.437  -7.261   1.00 70.16  ? 357 TYR   C OH     1 
ATOM   9541  N  N      . GLN   C 1  358 ? 0.688   -46.331  1.049    1.00 51.44  ? 358 GLN   C N      1 
ATOM   9542  C  CA     . GLN   C 1  358 ? 0.438   -46.028  2.454    1.00 53.73  ? 358 GLN   C CA     1 
ATOM   9543  C  C      . GLN   C 1  358 ? -0.212  -44.658  2.589    1.00 60.40  ? 358 GLN   C C      1 
ATOM   9544  O  O      . GLN   C 1  358 ? 0.390   -43.658  2.174    1.00 60.83  ? 358 GLN   C O      1 
ATOM   9545  C  CB     . GLN   C 1  358 ? 1.735   -46.076  3.256    1.00 57.74  ? 358 GLN   C CB     1 
ATOM   9546  C  CG     . GLN   C 1  358 ? 2.348   -47.472  3.403    1.00 70.16  ? 358 GLN   C CG     1 
ATOM   9547  C  CD     . GLN   C 1  358 ? 3.033   -47.991  2.130    1.00 71.58  ? 358 GLN   C CD     1 
ATOM   9548  O  OE1    . GLN   C 1  358 ? 3.315   -47.231  1.182    1.00 69.34  ? 358 GLN   C OE1    1 
ATOM   9549  N  NE2    . GLN   C 1  358 ? 3.302   -49.302  2.109    1.00 66.32  ? 358 GLN   C NE2    1 
ATOM   9550  N  N      . PRO   C 1  359 ? -1.401  -44.549  3.175    1.00 66.92  ? 359 PRO   C N      1 
ATOM   9551  C  CA     . PRO   C 1  359 ? -2.121  -43.268  3.154    1.00 59.15  ? 359 PRO   C CA     1 
ATOM   9552  C  C      . PRO   C 1  359 ? -1.466  -42.301  4.120    1.00 50.94  ? 359 PRO   C C      1 
ATOM   9553  O  O      . PRO   C 1  359 ? -0.687  -42.714  4.998    1.00 55.83  ? 359 PRO   C O      1 
ATOM   9554  C  CB     . PRO   C 1  359 ? -3.545  -43.639  3.598    1.00 58.14  ? 359 PRO   C CB     1 
ATOM   9555  C  CG     . PRO   C 1  359 ? -3.497  -45.115  4.039    1.00 61.01  ? 359 PRO   C CG     1 
ATOM   9556  C  CD     . PRO   C 1  359 ? -2.039  -45.511  4.081    1.00 66.51  ? 359 PRO   C CD     1 
ATOM   9557  N  N      . PRO   C 1  360 ? -1.755  -41.015  4.001    1.00 47.69  ? 360 PRO   C N      1 
ATOM   9558  C  CA     . PRO   C 1  360 ? -1.088  -40.042  4.869    1.00 50.14  ? 360 PRO   C CA     1 
ATOM   9559  C  C      . PRO   C 1  360 ? -1.554  -40.209  6.294    1.00 51.29  ? 360 PRO   C C      1 
ATOM   9560  O  O      . PRO   C 1  360 ? -2.633  -40.739  6.568    1.00 51.61  ? 360 PRO   C O      1 
ATOM   9561  C  CB     . PRO   C 1  360 ? -1.493  -38.672  4.303    1.00 49.52  ? 360 PRO   C CB     1 
ATOM   9562  C  CG     . PRO   C 1  360 ? -2.556  -38.939  3.268    1.00 56.39  ? 360 PRO   C CG     1 
ATOM   9563  C  CD     . PRO   C 1  360 ? -2.774  -40.424  3.125    1.00 51.85  ? 360 PRO   C CD     1 
ATOM   9564  N  N      . THR   C 1  361 ? -0.706  -39.775  7.208    1.00 49.57  ? 361 THR   C N      1 
ATOM   9565  C  CA     . THR   C 1  361 ? -1.016  -39.871  8.616    1.00 48.39  ? 361 THR   C CA     1 
ATOM   9566  C  C      . THR   C 1  361 ? -1.138  -38.473  9.198    1.00 52.24  ? 361 THR   C C      1 
ATOM   9567  O  O      . THR   C 1  361 ? -0.629  -37.487  8.655    1.00 50.20  ? 361 THR   C O      1 
ATOM   9568  C  CB     . THR   C 1  361 ? 0.048   -40.675  9.366    1.00 47.08  ? 361 THR   C CB     1 
ATOM   9569  O  OG1    . THR   C 1  361 ? 0.478   -41.745  8.532    1.00 50.30  ? 361 THR   C OG1    1 
ATOM   9570  C  CG2    . THR   C 1  361 ? -0.528  -41.254  10.634   1.00 51.92  ? 361 THR   C CG2    1 
ATOM   9571  N  N      . VAL   C 1  362 ? -1.847  -38.402  10.312   1.00 58.70  ? 362 VAL   C N      1 
ATOM   9572  C  CA     . VAL   C 1  362 ? -2.005  -37.157  11.034   1.00 55.17  ? 362 VAL   C CA     1 
ATOM   9573  C  C      . VAL   C 1  362 ? -1.574  -37.443  12.448   1.00 52.21  ? 362 VAL   C C      1 
ATOM   9574  O  O      . VAL   C 1  362 ? -1.550  -38.592  12.891   1.00 44.75  ? 362 VAL   C O      1 
ATOM   9575  C  CB     . VAL   C 1  362 ? -3.444  -36.622  11.011   1.00 51.04  ? 362 VAL   C CB     1 
ATOM   9576  C  CG1    . VAL   C 1  362 ? -3.706  -35.929  9.678    1.00 45.46  ? 362 VAL   C CG1    1 
ATOM   9577  C  CG2    . VAL   C 1  362 ? -4.439  -37.779  11.285   1.00 41.95  ? 362 VAL   C CG2    1 
ATOM   9578  N  N      . VAL   C 1  363 ? -1.252  -36.368  13.143   1.00 50.83  ? 363 VAL   C N      1 
ATOM   9579  C  CA     . VAL   C 1  363 ? -0.688  -36.417  14.478   1.00 48.46  ? 363 VAL   C CA     1 
ATOM   9580  C  C      . VAL   C 1  363 ? -1.812  -36.134  15.462   1.00 54.67  ? 363 VAL   C C      1 
ATOM   9581  O  O      . VAL   C 1  363 ? -2.561  -35.168  15.255   1.00 56.85  ? 363 VAL   C O      1 
ATOM   9582  C  CB     . VAL   C 1  363 ? 0.441   -35.387  14.619   1.00 51.18  ? 363 VAL   C CB     1 
ATOM   9583  C  CG1    . VAL   C 1  363 ? 0.557   -34.916  16.053   1.00 56.75  ? 363 VAL   C CG1    1 
ATOM   9584  C  CG2    . VAL   C 1  363 ? 1.718   -35.998  14.113   1.00 47.53  ? 363 VAL   C CG2    1 
ATOM   9585  N  N      . PRO   C 1  364 ? -1.989  -36.968  16.518   1.00 60.20  ? 364 PRO   C N      1 
ATOM   9586  C  CA     . PRO   C 1  364 ? -2.981  -36.669  17.563   1.00 56.94  ? 364 PRO   C CA     1 
ATOM   9587  C  C      . PRO   C 1  364 ? -3.223  -35.189  17.791   1.00 57.13  ? 364 PRO   C C      1 
ATOM   9588  O  O      . PRO   C 1  364 ? -2.278  -34.413  17.954   1.00 55.88  ? 364 PRO   C O      1 
ATOM   9589  C  CB     . PRO   C 1  364 ? -2.373  -37.325  18.818   1.00 57.16  ? 364 PRO   C CB     1 
ATOM   9590  C  CG     . PRO   C 1  364 ? -1.122  -38.121  18.331   1.00 62.87  ? 364 PRO   C CG     1 
ATOM   9591  C  CD     . PRO   C 1  364 ? -1.265  -38.212  16.825   1.00 57.54  ? 364 PRO   C CD     1 
ATOM   9592  N  N      . GLY   C 1  365 ? -4.492  -34.790  17.793   1.00 59.95  ? 365 GLY   C N      1 
ATOM   9593  C  CA     . GLY   C 1  365 ? -4.825  -33.422  18.131   1.00 60.61  ? 365 GLY   C CA     1 
ATOM   9594  C  C      . GLY   C 1  365 ? -4.356  -32.406  17.127   1.00 65.84  ? 365 GLY   C C      1 
ATOM   9595  O  O      . GLY   C 1  365 ? -4.177  -31.233  17.474   1.00 68.05  ? 365 GLY   C O      1 
ATOM   9596  N  N      . GLY   C 1  366 ? -4.139  -32.824  15.889   1.00 62.53  ? 366 GLY   C N      1 
ATOM   9597  C  CA     . GLY   C 1  366 ? -3.730  -31.898  14.868   1.00 52.39  ? 366 GLY   C CA     1 
ATOM   9598  C  C      . GLY   C 1  366 ? -4.909  -31.195  14.252   1.00 51.91  ? 366 GLY   C C      1 
ATOM   9599  O  O      . GLY   C 1  366 ? -6.082  -31.477  14.498   1.00 56.18  ? 366 GLY   C O      1 
ATOM   9600  N  N      . ASP   C 1  367 ? -4.593  -30.235  13.416   1.00 46.79  ? 367 ASP   C N      1 
ATOM   9601  C  CA     . ASP   C 1  367 ? -5.645  -29.542  12.723   1.00 50.47  ? 367 ASP   C CA     1 
ATOM   9602  C  C      . ASP   C 1  367 ? -5.897  -30.102  11.333   1.00 52.14  ? 367 ASP   C C      1 
ATOM   9603  O  O      . ASP   C 1  367 ? -6.951  -29.820  10.757   1.00 50.92  ? 367 ASP   C O      1 
ATOM   9604  C  CB     . ASP   C 1  367 ? -5.305  -28.050  12.674   1.00 63.36  ? 367 ASP   C CB     1 
ATOM   9605  C  CG     . ASP   C 1  367 ? -4.962  -27.503  14.060   1.00 67.12  ? 367 ASP   C CG     1 
ATOM   9606  O  OD1    . ASP   C 1  367 ? -5.892  -27.078  14.792   1.00 65.29  ? 367 ASP   C OD1    1 
ATOM   9607  O  OD2    . ASP   C 1  367 ? -3.760  -27.528  14.424   1.00 66.53  ? 367 ASP   C OD2    1 
ATOM   9608  N  N      . LEU   C 1  368 ? -5.000  -30.940  10.812   1.00 52.99  ? 368 LEU   C N      1 
ATOM   9609  C  CA     . LEU   C 1  368 ? -5.158  -31.485  9.470    1.00 44.52  ? 368 LEU   C CA     1 
ATOM   9610  C  C      . LEU   C 1  368 ? -6.150  -32.640  9.471    1.00 40.38  ? 368 LEU   C C      1 
ATOM   9611  O  O      . LEU   C 1  368 ? -6.093  -33.519  10.332   1.00 37.84  ? 368 LEU   C O      1 
ATOM   9612  C  CB     . LEU   C 1  368 ? -3.819  -31.970  8.928    1.00 42.11  ? 368 LEU   C CB     1 
ATOM   9613  C  CG     . LEU   C 1  368 ? -3.301  -31.117  7.789    1.00 54.41  ? 368 LEU   C CG     1 
ATOM   9614  C  CD1    . LEU   C 1  368 ? -1.871  -31.527  7.430    1.00 49.68  ? 368 LEU   C CD1    1 
ATOM   9615  C  CD2    . LEU   C 1  368 ? -4.266  -31.199  6.583    1.00 52.42  ? 368 LEU   C CD2    1 
ATOM   9616  N  N      . ALA   C 1  369 ? -7.057  -32.637  8.505    1.00 42.13  ? 369 ALA   C N      1 
ATOM   9617  C  CA     . ALA   C 1  369 ? -7.934  -33.782  8.301    1.00 39.26  ? 369 ALA   C CA     1 
ATOM   9618  C  C      . ALA   C 1  369 ? -7.126  -34.981  7.842    1.00 39.41  ? 369 ALA   C C      1 
ATOM   9619  O  O      . ALA   C 1  369 ? -6.210  -34.852  7.026    1.00 41.91  ? 369 ALA   C O      1 
ATOM   9620  C  CB     . ALA   C 1  369 ? -9.003  -33.467  7.257    1.00 35.90  ? 369 ALA   C CB     1 
ATOM   9621  N  N      . LYS   C 1  370 ? -7.475  -36.157  8.360    1.00 41.70  ? 370 LYS   C N      1 
ATOM   9622  C  CA     . LYS   C 1  370 ? -6.938  -37.409  7.833    1.00 44.01  ? 370 LYS   C CA     1 
ATOM   9623  C  C      . LYS   C 1  370 ? -7.674  -37.706  6.534    1.00 42.81  ? 370 LYS   C C      1 
ATOM   9624  O  O      . LYS   C 1  370 ? -8.863  -38.017  6.559    1.00 48.47  ? 370 LYS   C O      1 
ATOM   9625  C  CB     . LYS   C 1  370 ? -7.096  -38.561  8.824    1.00 40.85  ? 370 LYS   C CB     1 
ATOM   9626  C  CG     . LYS   C 1  370 ? -5.904  -39.531  8.847    1.00 49.60  ? 370 LYS   C CG     1 
ATOM   9627  C  CD     . LYS   C 1  370 ? -6.245  -40.925  9.404    1.00 50.86  ? 370 LYS   C CD     1 
ATOM   9628  C  CE     . LYS   C 1  370 ? -5.527  -42.033  8.616    1.00 56.00  ? 370 LYS   C CE     1 
ATOM   9629  N  NZ     . LYS   C 1  370 ? -5.940  -43.429  9.019    1.00 62.07  ? 370 LYS   C NZ     1 
ATOM   9630  N  N      . VAL   C 1  371 ? -6.983  -37.596  5.401    1.00 42.57  ? 371 VAL   C N      1 
ATOM   9631  C  CA     . VAL   C 1  371 ? -7.597  -37.796  4.109    1.00 41.50  ? 371 VAL   C CA     1 
ATOM   9632  C  C      . VAL   C 1  371 ? -7.222  -39.169  3.567    1.00 46.27  ? 371 VAL   C C      1 
ATOM   9633  O  O      . VAL   C 1  371 ? -6.249  -39.800  3.988    1.00 47.49  ? 371 VAL   C O      1 
ATOM   9634  C  CB     . VAL   C 1  371 ? -7.197  -36.687  3.117    1.00 41.00  ? 371 VAL   C CB     1 
ATOM   9635  C  CG1    . VAL   C 1  371 ? -7.718  -35.358  3.602    1.00 36.36  ? 371 VAL   C CG1    1 
ATOM   9636  C  CG2    . VAL   C 1  371 ? -5.690  -36.658  2.927    1.00 45.10  ? 371 VAL   C CG2    1 
ATOM   9637  N  N      . GLN   C 1  372 ? -7.996  -39.630  2.586    1.00 52.39  ? 372 GLN   C N      1 
ATOM   9638  C  CA     . GLN   C 1  372 ? -7.702  -40.917  1.960    1.00 55.49  ? 372 GLN   C CA     1 
ATOM   9639  C  C      . GLN   C 1  372 ? -6.496  -40.853  1.016    1.00 55.91  ? 372 GLN   C C      1 
ATOM   9640  O  O      . GLN   C 1  372 ? -5.804  -41.870  0.832    1.00 51.27  ? 372 GLN   C O      1 
ATOM   9641  C  CB     . GLN   C 1  372 ? -8.934  -41.420  1.213    1.00 54.01  ? 372 GLN   C CB     1 
ATOM   9642  C  CG     . GLN   C 1  372 ? -9.832  -42.329  2.035    1.00 54.15  ? 372 GLN   C CG     1 
ATOM   9643  C  CD     . GLN   C 1  372 ? -11.105 -42.706  1.273    1.00 62.99  ? 372 GLN   C CD     1 
ATOM   9644  O  OE1    . GLN   C 1  372 ? -11.790 -41.838  0.701    1.00 60.34  ? 372 GLN   C OE1    1 
ATOM   9645  N  NE2    . GLN   C 1  372 ? -11.426 -44.006  1.258    1.00 60.27  ? 372 GLN   C NE2    1 
ATOM   9646  N  N      . ARG   C 1  373 ? -6.222  -39.685  0.423    1.00 49.97  ? 373 ARG   C N      1 
ATOM   9647  C  CA     . ARG   C 1  373 ? -5.161  -39.574  -0.565   1.00 44.20  ? 373 ARG   C CA     1 
ATOM   9648  C  C      . ARG   C 1  373 ? -4.585  -38.159  -0.579   1.00 44.87  ? 373 ARG   C C      1 
ATOM   9649  O  O      . ARG   C 1  373 ? -5.291  -37.191  -0.302   1.00 46.84  ? 373 ARG   C O      1 
ATOM   9650  C  CB     . ARG   C 1  373 ? -5.697  -39.965  -1.930   1.00 43.82  ? 373 ARG   C CB     1 
ATOM   9651  C  CG     . ARG   C 1  373 ? -6.605  -38.949  -2.531   1.00 42.09  ? 373 ARG   C CG     1 
ATOM   9652  C  CD     . ARG   C 1  373 ? -7.353  -39.599  -3.631   1.00 43.45  ? 373 ARG   C CD     1 
ATOM   9653  N  NE     . ARG   C 1  373 ? -8.026  -40.790  -3.134   1.00 50.11  ? 373 ARG   C NE     1 
ATOM   9654  C  CZ     . ARG   C 1  373 ? -9.211  -40.777  -2.538   1.00 54.16  ? 373 ARG   C CZ     1 
ATOM   9655  N  NH1    . ARG   C 1  373 ? -9.885  -39.648  -2.367   1.00 48.37  ? 373 ARG   C NH1    1 
ATOM   9656  N  NH2    . ARG   C 1  373 ? -9.733  -41.925  -2.101   1.00 50.10  ? 373 ARG   C NH2    1 
ATOM   9657  N  N      . ALA   C 1  374 ? -3.291  -38.045  -0.903   1.00 40.27  ? 374 ALA   C N      1 
ATOM   9658  C  CA     . ALA   C 1  374 ? -2.579  -36.770  -0.862   1.00 36.70  ? 374 ALA   C CA     1 
ATOM   9659  C  C      . ALA   C 1  374 ? -1.584  -36.680  -2.017   1.00 35.04  ? 374 ALA   C C      1 
ATOM   9660  O  O      . ALA   C 1  374 ? -1.349  -37.654  -2.738   1.00 39.24  ? 374 ALA   C O      1 
ATOM   9661  C  CB     . ALA   C 1  374 ? -1.868  -36.578  0.480    1.00 39.74  ? 374 ALA   C CB     1 
ATOM   9662  N  N      . VAL   C 1  375 ? -1.001  -35.498  -2.207   1.00 27.99  ? 375 VAL   C N      1 
ATOM   9663  C  CA     . VAL   C 1  375 ? -0.041  -35.282  -3.293   1.00 31.67  ? 375 VAL   C CA     1 
ATOM   9664  C  C      . VAL   C 1  375 ? 0.896   -34.128  -2.946   1.00 32.83  ? 375 VAL   C C      1 
ATOM   9665  O  O      . VAL   C 1  375 ? 0.470   -33.090  -2.430   1.00 35.86  ? 375 VAL   C O      1 
ATOM   9666  C  CB     . VAL   C 1  375 ? -0.734  -34.986  -4.641   1.00 32.39  ? 375 VAL   C CB     1 
ATOM   9667  C  CG1    . VAL   C 1  375 ? -1.422  -33.622  -4.609   1.00 32.79  ? 375 VAL   C CG1    1 
ATOM   9668  C  CG2    . VAL   C 1  375 ? 0.306   -35.032  -5.786   1.00 32.72  ? 375 VAL   C CG2    1 
ATOM   9669  N  N      . CYS   C 1  376 ? 2.172   -34.289  -3.273   1.00 30.82  ? 376 CYS   C N      1 
ATOM   9670  C  CA     . CYS   C 1  376 ? 3.101   -33.167  -3.277   1.00 33.67  ? 376 CYS   C CA     1 
ATOM   9671  C  C      . CYS   C 1  376 ? 3.670   -33.053  -4.681   1.00 31.18  ? 376 CYS   C C      1 
ATOM   9672  O  O      . CYS   C 1  376 ? 4.224   -34.021  -5.210   1.00 34.38  ? 376 CYS   C O      1 
ATOM   9673  C  CB     . CYS   C 1  376 ? 4.198   -33.343  -2.225   1.00 32.21  ? 376 CYS   C CB     1 
ATOM   9674  S  SG     . CYS   C 1  376 ? 5.365   -32.069  -2.194   1.00 54.43  ? 376 CYS   C SG     1 
ATOM   9675  N  N      . MET   C 1  377 ? 3.467   -31.902  -5.303   1.00 29.62  ? 377 MET   C N      1 
ATOM   9676  C  CA     . MET   C 1  377 ? 4.093   -31.591  -6.572   1.00 28.35  ? 377 MET   C CA     1 
ATOM   9677  C  C      . MET   C 1  377 ? 5.424   -30.916  -6.283   1.00 32.62  ? 377 MET   C C      1 
ATOM   9678  O  O      . MET   C 1  377 ? 5.519   -30.059  -5.397   1.00 34.02  ? 377 MET   C O      1 
ATOM   9679  C  CB     . MET   C 1  377 ? 3.195   -30.687  -7.418   1.00 30.67  ? 377 MET   C CB     1 
ATOM   9680  C  CG     . MET   C 1  377 ? 3.554   -30.646  -8.878   1.00 34.70  ? 377 MET   C CG     1 
ATOM   9681  S  SD     . MET   C 1  377 ? 2.545   -29.557  -9.934   1.00 46.86  ? 377 MET   C SD     1 
ATOM   9682  C  CE     . MET   C 1  377 ? 3.267   -27.949  -9.675   1.00 41.62  ? 377 MET   C CE     1 
ATOM   9683  N  N      . LEU   C 1  378 ? 6.464   -31.369  -6.978   1.00 33.24  ? 378 LEU   C N      1 
ATOM   9684  C  CA     . LEU   C 1  378 ? 7.787   -30.756  -6.976   1.00 28.25  ? 378 LEU   C CA     1 
ATOM   9685  C  C      . LEU   C 1  378 ? 8.026   -30.237  -8.383   1.00 30.67  ? 378 LEU   C C      1 
ATOM   9686  O  O      . LEU   C 1  378 ? 8.209   -31.027  -9.319   1.00 38.18  ? 378 LEU   C O      1 
ATOM   9687  C  CB     . LEU   C 1  378 ? 8.877   -31.760  -6.593   1.00 31.16  ? 378 LEU   C CB     1 
ATOM   9688  C  CG     . LEU   C 1  378 ? 8.877   -32.435  -5.222   1.00 31.73  ? 378 LEU   C CG     1 
ATOM   9689  C  CD1    . LEU   C 1  378 ? 10.009  -33.463  -5.122   1.00 22.84  ? 378 LEU   C CD1    1 
ATOM   9690  C  CD2    . LEU   C 1  378 ? 8.991   -31.392  -4.124   1.00 35.16  ? 378 LEU   C CD2    1 
ATOM   9691  N  N      . SER   C 1  379 ? 8.010   -28.928  -8.551   1.00 29.19  ? 379 SER   C N      1 
ATOM   9692  C  CA     . SER   C 1  379 ? 8.286   -28.330  -9.850   1.00 32.26  ? 379 SER   C CA     1 
ATOM   9693  C  C      . SER   C 1  379 ? 9.566   -27.527  -9.747   1.00 39.52  ? 379 SER   C C      1 
ATOM   9694  O  O      . SER   C 1  379 ? 9.908   -27.005  -8.677   1.00 42.89  ? 379 SER   C O      1 
ATOM   9695  C  CB     . SER   C 1  379 ? 7.126   -27.422  -10.369  1.00 30.89  ? 379 SER   C CB     1 
ATOM   9696  O  OG     . SER   C 1  379 ? 6.195   -27.093  -9.340   1.00 41.37  ? 379 SER   C OG     1 
ATOM   9697  N  N      . ASN   C 1  380 ? 10.298  -27.474  -10.851  1.00 34.10  ? 380 ASN   C N      1 
ATOM   9698  C  CA     . ASN   C 1  380 ? 11.390  -26.535  -10.985  1.00 32.12  ? 380 ASN   C CA     1 
ATOM   9699  C  C      . ASN   C 1  380 ? 10.883  -25.467  -11.950  1.00 36.76  ? 380 ASN   C C      1 
ATOM   9700  O  O      . ASN   C 1  380 ? 10.774  -25.689  -13.160  1.00 37.42  ? 380 ASN   C O      1 
ATOM   9701  C  CB     . ASN   C 1  380 ? 12.668  -27.218  -11.452  1.00 33.40  ? 380 ASN   C CB     1 
ATOM   9702  C  CG     . ASN   C 1  380 ? 13.735  -26.220  -11.854  1.00 39.36  ? 380 ASN   C CG     1 
ATOM   9703  O  OD1    . ASN   C 1  380 ? 14.451  -26.421  -12.833  1.00 44.25  ? 380 ASN   C OD1    1 
ATOM   9704  N  ND2    . ASN   C 1  380 ? 13.816  -25.113  -11.123  1.00 36.53  ? 380 ASN   C ND2    1 
ATOM   9705  N  N      . THR   C 1  381 ? 10.499  -24.336  -11.394  1.00 31.75  ? 381 THR   C N      1 
ATOM   9706  C  CA     . THR   C 1  381 ? 9.986   -23.219  -12.154  1.00 33.96  ? 381 THR   C CA     1 
ATOM   9707  C  C      . THR   C 1  381 ? 10.878  -22.017  -11.914  1.00 36.03  ? 381 THR   C C      1 
ATOM   9708  O  O      . THR   C 1  381 ? 11.415  -21.840  -10.813  1.00 37.90  ? 381 THR   C O      1 
ATOM   9709  C  CB     . THR   C 1  381 ? 8.546   -22.871  -11.755  1.00 34.38  ? 381 THR   C CB     1 
ATOM   9710  O  OG1    . THR   C 1  381 ? 8.242   -21.548  -12.216  1.00 45.17  ? 381 THR   C OG1    1 
ATOM   9711  C  CG2    . THR   C 1  381 ? 8.400   -22.890  -10.293  1.00 29.72  ? 381 THR   C CG2    1 
ATOM   9712  N  N      . THR   C 1  382 ? 11.036  -21.200  -12.952  1.00 32.54  ? 382 THR   C N      1 
ATOM   9713  C  CA     . THR   C 1  382 ? 11.806  -19.978  -12.800  1.00 34.06  ? 382 THR   C CA     1 
ATOM   9714  C  C      . THR   C 1  382 ? 11.154  -19.048  -11.792  1.00 35.07  ? 382 THR   C C      1 
ATOM   9715  O  O      . THR   C 1  382 ? 11.831  -18.226  -11.179  1.00 33.20  ? 382 THR   C O      1 
ATOM   9716  C  CB     . THR   C 1  382 ? 11.944  -19.299  -14.153  1.00 38.04  ? 382 THR   C CB     1 
ATOM   9717  O  OG1    . THR   C 1  382 ? 10.630  -19.012  -14.675  1.00 37.86  ? 382 THR   C OG1    1 
ATOM   9718  C  CG2    . THR   C 1  382 ? 12.700  -20.217  -15.103  1.00 30.19  ? 382 THR   C CG2    1 
ATOM   9719  N  N      . ALA   C 1  383 ? 9.843   -19.180  -11.592  1.00 39.96  ? 383 ALA   C N      1 
ATOM   9720  C  CA     . ALA   C 1  383 ? 9.138   -18.308  -10.662  1.00 36.21  ? 383 ALA   C CA     1 
ATOM   9721  C  C      . ALA   C 1  383 ? 9.760   -18.297  -9.269   1.00 40.50  ? 383 ALA   C C      1 
ATOM   9722  O  O      . ALA   C 1  383 ? 9.555   -17.332  -8.521   1.00 39.94  ? 383 ALA   C O      1 
ATOM   9723  C  CB     . ALA   C 1  383 ? 7.673   -18.733  -10.566  1.00 38.76  ? 383 ALA   C CB     1 
ATOM   9724  N  N      . ILE   C 1  384 ? 10.478  -19.356  -8.872   1.00 36.22  ? 384 ILE   C N      1 
ATOM   9725  C  CA     . ILE   C 1  384 ? 11.041  -19.364  -7.524   1.00 33.92  ? 384 ILE   C CA     1 
ATOM   9726  C  C      . ILE   C 1  384 ? 12.002  -18.188  -7.354   1.00 37.28  ? 384 ILE   C C      1 
ATOM   9727  O  O      . ILE   C 1  384 ? 12.169  -17.653  -6.246   1.00 34.47  ? 384 ILE   C O      1 
ATOM   9728  C  CB     . ILE   C 1  384 ? 11.742  -20.705  -7.246   1.00 35.98  ? 384 ILE   C CB     1 
ATOM   9729  C  CG1    . ILE   C 1  384 ? 11.933  -20.956  -5.742   1.00 33.45  ? 384 ILE   C CG1    1 
ATOM   9730  C  CG2    . ILE   C 1  384 ? 13.070  -20.747  -7.980   1.00 34.37  ? 384 ILE   C CG2    1 
ATOM   9731  C  CD1    . ILE   C 1  384 ? 11.005  -22.009  -5.185   1.00 25.71  ? 384 ILE   C CD1    1 
ATOM   9732  N  N      . ALA   C 1  385 ? 12.632  -17.755  -8.445   1.00 30.74  ? 385 ALA   C N      1 
ATOM   9733  C  CA     . ALA   C 1  385 ? 13.576  -16.655  -8.355   1.00 31.18  ? 385 ALA   C CA     1 
ATOM   9734  C  C      . ALA   C 1  385 ? 12.938  -15.420  -7.739   1.00 32.12  ? 385 ALA   C C      1 
ATOM   9735  O  O      . ALA   C 1  385 ? 13.637  -14.602  -7.141   1.00 39.79  ? 385 ALA   C O      1 
ATOM   9736  C  CB     . ALA   C 1  385 ? 14.159  -16.354  -9.740   1.00 29.82  ? 385 ALA   C CB     1 
ATOM   9737  N  N      . GLU   C 1  386 ? 11.619  -15.268  -7.845   1.00 33.51  ? 386 GLU   C N      1 
ATOM   9738  C  CA     . GLU   C 1  386 ? 10.938  -14.179  -7.138   1.00 32.92  ? 386 GLU   C CA     1 
ATOM   9739  C  C      . GLU   C 1  386 ? 11.290  -14.164  -5.648   1.00 32.66  ? 386 GLU   C C      1 
ATOM   9740  O  O      . GLU   C 1  386 ? 11.630  -13.121  -5.085   1.00 33.86  ? 386 GLU   C O      1 
ATOM   9741  C  CB     . GLU   C 1  386 ? 9.425   -14.304  -7.318   1.00 32.25  ? 386 GLU   C CB     1 
ATOM   9742  C  CG     . GLU   C 1  386 ? 8.890   -13.949  -8.702   1.00 27.87  ? 386 GLU   C CG     1 
ATOM   9743  C  CD     . GLU   C 1  386 ? 7.464   -14.431  -8.885   1.00 46.73  ? 386 GLU   C CD     1 
ATOM   9744  O  OE1    . GLU   C 1  386 ? 6.706   -14.426  -7.876   1.00 47.07  ? 386 GLU   C OE1    1 
ATOM   9745  O  OE2    . GLU   C 1  386 ? 7.098   -14.809  -10.030  1.00 47.20  ? 386 GLU   C OE2    1 
ATOM   9746  N  N      . ALA   C 1  387 ? 11.195  -15.319  -4.985   1.00 34.40  ? 387 ALA   C N      1 
ATOM   9747  C  CA     . ALA   C 1  387 ? 11.622  -15.396  -3.597   1.00 34.71  ? 387 ALA   C CA     1 
ATOM   9748  C  C      . ALA   C 1  387 ? 13.048  -14.875  -3.424   1.00 36.85  ? 387 ALA   C C      1 
ATOM   9749  O  O      . ALA   C 1  387 ? 13.341  -14.167  -2.456   1.00 36.38  ? 387 ALA   C O      1 
ATOM   9750  C  CB     . ALA   C 1  387 ? 11.497  -16.826  -3.088   1.00 33.32  ? 387 ALA   C CB     1 
ATOM   9751  N  N      . TRP   C 1  388 ? 13.948  -15.200  -4.356   1.00 33.44  ? 388 TRP   C N      1 
ATOM   9752  C  CA     . TRP   C 1  388 ? 15.299  -14.653  -4.278   1.00 33.13  ? 388 TRP   C CA     1 
ATOM   9753  C  C      . TRP   C 1  388 ? 15.265  -13.144  -4.448   1.00 37.56  ? 388 TRP   C C      1 
ATOM   9754  O  O      . TRP   C 1  388 ? 15.916  -12.409  -3.697   1.00 37.05  ? 388 TRP   C O      1 
ATOM   9755  C  CB     . TRP   C 1  388 ? 16.221  -15.263  -5.348   1.00 38.38  ? 388 TRP   C CB     1 
ATOM   9756  C  CG     . TRP   C 1  388 ? 16.482  -16.759  -5.273   1.00 35.54  ? 388 TRP   C CG     1 
ATOM   9757  C  CD1    . TRP   C 1  388 ? 16.443  -17.656  -6.312   1.00 33.03  ? 388 TRP   C CD1    1 
ATOM   9758  C  CD2    . TRP   C 1  388 ? 16.829  -17.514  -4.108   1.00 29.12  ? 388 TRP   C CD2    1 
ATOM   9759  N  NE1    . TRP   C 1  388 ? 16.748  -18.918  -5.856   1.00 34.76  ? 388 TRP   C NE1    1 
ATOM   9760  C  CE2    . TRP   C 1  388 ? 16.978  -18.855  -4.505   1.00 33.51  ? 388 TRP   C CE2    1 
ATOM   9761  C  CE3    . TRP   C 1  388 ? 17.044  -17.182  -2.771   1.00 36.87  ? 388 TRP   C CE3    1 
ATOM   9762  C  CZ2    . TRP   C 1  388 ? 17.320  -19.869  -3.600   1.00 41.72  ? 388 TRP   C CZ2    1 
ATOM   9763  C  CZ3    . TRP   C 1  388 ? 17.389  -18.193  -1.859   1.00 34.24  ? 388 TRP   C CZ3    1 
ATOM   9764  C  CH2    . TRP   C 1  388 ? 17.516  -19.517  -2.277   1.00 38.04  ? 388 TRP   C CH2    1 
ATOM   9765  N  N      . ALA   C 1  389 ? 14.516  -12.663  -5.452   1.00 36.45  ? 389 ALA   C N      1 
ATOM   9766  C  CA     . ALA   C 1  389 ? 14.382  -11.225  -5.679   1.00 37.06  ? 389 ALA   C CA     1 
ATOM   9767  C  C      . ALA   C 1  389 ? 13.928  -10.489  -4.416   1.00 39.42  ? 389 ALA   C C      1 
ATOM   9768  O  O      . ALA   C 1  389 ? 14.586  -9.541   -3.975   1.00 41.62  ? 389 ALA   C O      1 
ATOM   9769  C  CB     . ALA   C 1  389 ? 13.411  -10.958  -6.825   1.00 30.97  ? 389 ALA   C CB     1 
ATOM   9770  N  N      . ARG   C 1  390 ? 12.796  -10.895  -3.826   1.00 32.60  ? 390 ARG   C N      1 
ATOM   9771  C  CA     . ARG   C 1  390 ? 12.312  -10.194  -2.643   1.00 30.88  ? 390 ARG   C CA     1 
ATOM   9772  C  C      . ARG   C 1  390 ? 13.407  -10.109  -1.604   1.00 33.09  ? 390 ARG   C C      1 
ATOM   9773  O  O      . ARG   C 1  390 ? 13.830  -9.021   -1.219   1.00 37.76  ? 390 ARG   C O      1 
ATOM   9774  C  CB     . ARG   C 1  390 ? 11.096  -10.903  -2.050   1.00 29.85  ? 390 ARG   C CB     1 
ATOM   9775  C  CG     . ARG   C 1  390 ? 9.915   -10.947  -2.957   1.00 29.80  ? 390 ARG   C CG     1 
ATOM   9776  C  CD     . ARG   C 1  390 ? 8.660   -11.301  -2.200   1.00 28.39  ? 390 ARG   C CD     1 
ATOM   9777  N  NE     . ARG   C 1  390 ? 8.646   -12.669  -1.702   1.00 33.82  ? 390 ARG   C NE     1 
ATOM   9778  C  CZ     . ARG   C 1  390 ? 8.349   -13.728  -2.446   1.00 35.44  ? 390 ARG   C CZ     1 
ATOM   9779  N  NH1    . ARG   C 1  390 ? 8.145   -13.621  -3.745   1.00 29.44  ? 390 ARG   C NH1    1 
ATOM   9780  N  NH2    . ARG   C 1  390 ? 8.264   -14.927  -1.870   1.00 37.51  ? 390 ARG   C NH2    1 
ATOM   9781  N  N      . LEU   C 1  391 ? 13.868  -11.275  -1.141   1.00 35.63  ? 391 LEU   C N      1 
ATOM   9782  C  CA     . LEU   C 1  391 ? 14.890  -11.369  -0.105   1.00 32.32  ? 391 LEU   C CA     1 
ATOM   9783  C  C      . LEU   C 1  391 ? 16.142  -10.572  -0.463   1.00 39.20  ? 391 LEU   C C      1 
ATOM   9784  O  O      . LEU   C 1  391 ? 16.755  -9.932   0.402    1.00 40.12  ? 391 LEU   C O      1 
ATOM   9785  C  CB     . LEU   C 1  391 ? 15.246  -12.835  0.108    1.00 29.20  ? 391 LEU   C CB     1 
ATOM   9786  C  CG     . LEU   C 1  391 ? 15.874  -13.219  1.446    1.00 38.89  ? 391 LEU   C CG     1 
ATOM   9787  C  CD1    . LEU   C 1  391 ? 15.216  -12.495  2.656    1.00 34.01  ? 391 LEU   C CD1    1 
ATOM   9788  C  CD2    . LEU   C 1  391 ? 15.928  -14.742  1.633    1.00 34.85  ? 391 LEU   C CD2    1 
ATOM   9789  N  N      . ASP   C 1  392 ? 16.552  -10.620  -1.730   1.00 37.16  ? 392 ASP   C N      1 
ATOM   9790  C  CA     . ASP   C 1  392 ? 17.696  -9.834   -2.161   1.00 35.63  ? 392 ASP   C CA     1 
ATOM   9791  C  C      . ASP   C 1  392 ? 17.422  -8.343   -2.022   1.00 39.17  ? 392 ASP   C C      1 
ATOM   9792  O  O      . ASP   C 1  392 ? 18.337  -7.569   -1.718   1.00 41.93  ? 392 ASP   C O      1 
ATOM   9793  C  CB     . ASP   C 1  392 ? 18.070  -10.213  -3.603   1.00 37.67  ? 392 ASP   C CB     1 
ATOM   9794  C  CG     . ASP   C 1  392 ? 18.983  -11.452  -3.662   1.00 38.39  ? 392 ASP   C CG     1 
ATOM   9795  O  OD1    . ASP   C 1  392 ? 19.565  -11.797  -2.609   1.00 40.73  ? 392 ASP   C OD1    1 
ATOM   9796  O  OD2    . ASP   C 1  392 ? 19.116  -12.096  -4.736   1.00 38.90  ? 392 ASP   C OD2    1 
ATOM   9797  N  N      . HIS   C 1  393 ? 16.170  -7.918   -2.209   1.00 41.87  ? 393 HIS   C N      1 
ATOM   9798  C  CA     . HIS   C 1  393 ? 15.851  -6.502   -2.065   1.00 38.77  ? 393 HIS   C CA     1 
ATOM   9799  C  C      . HIS   C 1  393 ? 15.954  -6.055   -0.609   1.00 41.72  ? 393 HIS   C C      1 
ATOM   9800  O  O      . HIS   C 1  393 ? 16.507  -4.986   -0.327   1.00 46.79  ? 393 HIS   C O      1 
ATOM   9801  C  CB     . HIS   C 1  393 ? 14.463  -6.201   -2.611   1.00 33.28  ? 393 HIS   C CB     1 
ATOM   9802  C  CG     . HIS   C 1  393 ? 14.098  -4.748   -2.543   1.00 42.31  ? 393 HIS   C CG     1 
ATOM   9803  N  ND1    . HIS   C 1  393 ? 14.757  -3.779   -3.272   1.00 45.77  ? 393 HIS   C ND1    1 
ATOM   9804  C  CD2    . HIS   C 1  393 ? 13.166  -4.094   -1.810   1.00 38.93  ? 393 HIS   C CD2    1 
ATOM   9805  C  CE1    . HIS   C 1  393 ? 14.235  -2.595   -3.006   1.00 36.50  ? 393 HIS   C CE1    1 
ATOM   9806  N  NE2    . HIS   C 1  393 ? 13.269  -2.758   -2.121   1.00 40.28  ? 393 HIS   C NE2    1 
ATOM   9807  N  N      . LYS   C 1  394 ? 15.413  -6.839   0.335    1.00 31.15  ? 394 LYS   C N      1 
ATOM   9808  C  CA     . LYS   C 1  394 ? 15.550  -6.461   1.738    1.00 34.15  ? 394 LYS   C CA     1 
ATOM   9809  C  C      . LYS   C 1  394 ? 17.019  -6.359   2.129    1.00 40.17  ? 394 LYS   C C      1 
ATOM   9810  O  O      . LYS   C 1  394 ? 17.435  -5.385   2.766    1.00 39.81  ? 394 LYS   C O      1 
ATOM   9811  C  CB     . LYS   C 1  394 ? 14.828  -7.450   2.640    1.00 35.45  ? 394 LYS   C CB     1 
ATOM   9812  C  CG     . LYS   C 1  394 ? 13.340  -7.513   2.449    1.00 31.30  ? 394 LYS   C CG     1 
ATOM   9813  C  CD     . LYS   C 1  394 ? 12.821  -8.668   3.239    1.00 33.42  ? 394 LYS   C CD     1 
ATOM   9814  C  CE     . LYS   C 1  394 ? 11.435  -8.401   3.811    1.00 41.71  ? 394 LYS   C CE     1 
ATOM   9815  N  NZ     . LYS   C 1  394 ? 10.590  -7.703   2.850    1.00 41.31  ? 394 LYS   C NZ     1 
ATOM   9816  N  N      . PHE   C 1  395 ? 17.828  -7.349   1.738    1.00 37.62  ? 395 PHE   C N      1 
ATOM   9817  C  CA     . PHE   C 1  395 ? 19.272  -7.246   1.935    1.00 37.49  ? 395 PHE   C CA     1 
ATOM   9818  C  C      . PHE   C 1  395 ? 19.818  -5.897   1.462    1.00 45.07  ? 395 PHE   C C      1 
ATOM   9819  O  O      . PHE   C 1  395 ? 20.597  -5.249   2.174    1.00 41.94  ? 395 PHE   C O      1 
ATOM   9820  C  CB     . PHE   C 1  395 ? 19.986  -8.374   1.206    1.00 34.20  ? 395 PHE   C CB     1 
ATOM   9821  C  CG     . PHE   C 1  395 ? 21.484  -8.313   1.309    1.00 36.20  ? 395 PHE   C CG     1 
ATOM   9822  C  CD1    . PHE   C 1  395 ? 22.219  -7.431   0.514    1.00 36.17  ? 395 PHE   C CD1    1 
ATOM   9823  C  CD2    . PHE   C 1  395 ? 22.171  -9.161   2.191    1.00 35.43  ? 395 PHE   C CD2    1 
ATOM   9824  C  CE1    . PHE   C 1  395 ? 23.622  -7.394   0.590    1.00 29.98  ? 395 PHE   C CE1    1 
ATOM   9825  C  CE2    . PHE   C 1  395 ? 23.573  -9.127   2.284    1.00 30.67  ? 395 PHE   C CE2    1 
ATOM   9826  C  CZ     . PHE   C 1  395 ? 24.291  -8.239   1.475    1.00 32.78  ? 395 PHE   C CZ     1 
ATOM   9827  N  N      . ASP   C 1  396 ? 19.445  -5.466   0.246    1.00 44.28  ? 396 ASP   C N      1 
ATOM   9828  C  CA     . ASP   C 1  396 ? 20.027  -4.235   -0.307   1.00 41.28  ? 396 ASP   C CA     1 
ATOM   9829  C  C      . ASP   C 1  396 ? 19.625  -3.002   0.496    1.00 39.62  ? 396 ASP   C C      1 
ATOM   9830  O  O      . ASP   C 1  396 ? 20.455  -2.119   0.741    1.00 37.73  ? 396 ASP   C O      1 
ATOM   9831  C  CB     . ASP   C 1  396 ? 19.630  -4.053   -1.767   1.00 34.37  ? 396 ASP   C CB     1 
ATOM   9832  C  CG     . ASP   C 1  396 ? 20.137  -5.168   -2.650   1.00 46.46  ? 396 ASP   C CG     1 
ATOM   9833  O  OD1    . ASP   C 1  396 ? 21.277  -5.656   -2.417   1.00 40.71  ? 396 ASP   C OD1    1 
ATOM   9834  O  OD2    . ASP   C 1  396 ? 19.368  -5.579   -3.562   1.00 49.55  ? 396 ASP   C OD2    1 
ATOM   9835  N  N      . LEU   C 1  397 ? 18.358  -2.908   0.900    1.00 40.29  ? 397 LEU   C N      1 
ATOM   9836  C  CA     . LEU   C 1  397 ? 17.912  -1.696   1.573    1.00 39.11  ? 397 LEU   C CA     1 
ATOM   9837  C  C      . LEU   C 1  397 ? 18.838  -1.359   2.721    1.00 45.82  ? 397 LEU   C C      1 
ATOM   9838  O  O      . LEU   C 1  397 ? 19.190  -0.192   2.938    1.00 49.59  ? 397 LEU   C O      1 
ATOM   9839  C  CB     . LEU   C 1  397 ? 16.486  -1.867   2.076    1.00 37.38  ? 397 LEU   C CB     1 
ATOM   9840  C  CG     . LEU   C 1  397 ? 15.433  -1.773   0.977    1.00 44.67  ? 397 LEU   C CG     1 
ATOM   9841  C  CD1    . LEU   C 1  397 ? 14.080  -2.307   1.480    1.00 38.24  ? 397 LEU   C CD1    1 
ATOM   9842  C  CD2    . LEU   C 1  397 ? 15.350  -0.333   0.451    1.00 31.15  ? 397 LEU   C CD2    1 
ATOM   9843  N  N      . MET   C 1  398 ? 19.270  -2.387   3.445    1.00 46.60  ? 398 MET   C N      1 
ATOM   9844  C  CA     . MET   C 1  398 ? 20.085  -2.264   4.633    1.00 38.85  ? 398 MET   C CA     1 
ATOM   9845  C  C      . MET   C 1  398 ? 21.565  -2.131   4.307    1.00 43.51  ? 398 MET   C C      1 
ATOM   9846  O  O      . MET   C 1  398 ? 22.262  -1.298   4.909    1.00 47.11  ? 398 MET   C O      1 
ATOM   9847  C  CB     . MET   C 1  398 ? 19.838  -3.472   5.534    1.00 36.16  ? 398 MET   C CB     1 
ATOM   9848  C  CG     . MET   C 1  398 ? 18.475  -3.463   6.193    1.00 36.22  ? 398 MET   C CG     1 
ATOM   9849  S  SD     . MET   C 1  398 ? 18.252  -4.745   7.458    1.00 41.41  ? 398 MET   C SD     1 
ATOM   9850  C  CE     . MET   C 1  398 ? 18.927  -6.213   6.708    1.00 35.84  ? 398 MET   C CE     1 
ATOM   9851  N  N      . TYR   C 1  399 ? 22.066  -2.926   3.362    1.00 37.85  ? 399 TYR   C N      1 
ATOM   9852  C  CA     . TYR   C 1  399 ? 23.503  -2.927   3.128    1.00 38.76  ? 399 TYR   C CA     1 
ATOM   9853  C  C      . TYR   C 1  399 ? 23.982  -1.617   2.515    1.00 40.15  ? 399 TYR   C C      1 
ATOM   9854  O  O      . TYR   C 1  399 ? 25.173  -1.296   2.631    1.00 40.96  ? 399 TYR   C O      1 
ATOM   9855  C  CB     . TYR   C 1  399 ? 23.905  -4.128   2.253    1.00 41.83  ? 399 TYR   C CB     1 
ATOM   9856  C  CG     . TYR   C 1  399 ? 25.400  -4.351   2.217    1.00 34.41  ? 399 TYR   C CG     1 
ATOM   9857  C  CD1    . TYR   C 1  399 ? 26.075  -4.859   3.314    1.00 36.17  ? 399 TYR   C CD1    1 
ATOM   9858  C  CD2    . TYR   C 1  399 ? 26.133  -4.002   1.107    1.00 33.48  ? 399 TYR   C CD2    1 
ATOM   9859  C  CE1    . TYR   C 1  399 ? 27.451  -5.020   3.292    1.00 39.86  ? 399 TYR   C CE1    1 
ATOM   9860  C  CE2    . TYR   C 1  399 ? 27.486  -4.162   1.061    1.00 36.77  ? 399 TYR   C CE2    1 
ATOM   9861  C  CZ     . TYR   C 1  399 ? 28.154  -4.664   2.148    1.00 44.76  ? 399 TYR   C CZ     1 
ATOM   9862  O  OH     . TYR   C 1  399 ? 29.523  -4.810   2.068    1.00 43.33  ? 399 TYR   C OH     1 
ATOM   9863  N  N      . ALA   C 1  400 ? 23.079  -0.840   1.896    1.00 40.20  ? 400 ALA   C N      1 
ATOM   9864  C  CA     . ALA   C 1  400 ? 23.472  0.441    1.311    1.00 36.36  ? 400 ALA   C CA     1 
ATOM   9865  C  C      . ALA   C 1  400 ? 23.796  1.470    2.384    1.00 48.78  ? 400 ALA   C C      1 
ATOM   9866  O  O      . ALA   C 1  400 ? 24.610  2.373    2.144    1.00 53.77  ? 400 ALA   C O      1 
ATOM   9867  C  CB     . ALA   C 1  400 ? 22.386  0.972    0.384    1.00 32.52  ? 400 ALA   C CB     1 
ATOM   9868  N  N      . LYS   C 1  401 ? 23.182  1.355    3.564    1.00 46.60  ? 401 LYS   C N      1 
ATOM   9869  C  CA     . LYS   C 1  401 ? 23.580  2.140    4.725    1.00 47.83  ? 401 LYS   C CA     1 
ATOM   9870  C  C      . LYS   C 1  401 ? 24.474  1.357    5.674    1.00 46.37  ? 401 LYS   C C      1 
ATOM   9871  O  O      . LYS   C 1  401 ? 24.797  1.858    6.755    1.00 46.34  ? 401 LYS   C O      1 
ATOM   9872  C  CB     . LYS   C 1  401 ? 22.350  2.651    5.480    1.00 43.69  ? 401 LYS   C CB     1 
ATOM   9873  C  CG     . LYS   C 1  401 ? 21.204  3.081    4.586    1.00 47.07  ? 401 LYS   C CG     1 
ATOM   9874  C  CD     . LYS   C 1  401 ? 21.434  4.452    3.970    1.00 46.06  ? 401 LYS   C CD     1 
ATOM   9875  C  CE     . LYS   C 1  401 ? 20.237  4.908    3.128    1.00 50.06  ? 401 LYS   C CE     1 
ATOM   9876  N  NZ     . LYS   C 1  401 ? 19.860  3.941    2.058    1.00 52.19  ? 401 LYS   C NZ     1 
ATOM   9877  N  N      . ARG   C 1  402 ? 24.872  0.140    5.299    1.00 44.35  ? 402 ARG   C N      1 
ATOM   9878  C  CA     . ARG   C 1  402 ? 25.653  -0.749   6.172    1.00 46.10  ? 402 ARG   C CA     1 
ATOM   9879  C  C      . ARG   C 1  402 ? 25.022  -0.947   7.553    1.00 43.92  ? 402 ARG   C C      1 
ATOM   9880  O  O      . ARG   C 1  402 ? 25.720  -1.307   8.503    1.00 40.13  ? 402 ARG   C O      1 
ATOM   9881  C  CB     . ARG   C 1  402 ? 27.082  -0.250   6.331    1.00 37.13  ? 402 ARG   C CB     1 
ATOM   9882  C  CG     . ARG   C 1  402 ? 27.785  -0.114   5.014    1.00 46.88  ? 402 ARG   C CG     1 
ATOM   9883  C  CD     . ARG   C 1  402 ? 27.881  -1.457   4.303    1.00 49.87  ? 402 ARG   C CD     1 
ATOM   9884  N  NE     . ARG   C 1  402 ? 28.973  -1.480   3.334    1.00 50.28  ? 402 ARG   C NE     1 
ATOM   9885  C  CZ     . ARG   C 1  402 ? 28.851  -1.090   2.072    1.00 50.02  ? 402 ARG   C CZ     1 
ATOM   9886  N  NH1    . ARG   C 1  402 ? 27.685  -0.694   1.584    1.00 38.44  ? 402 ARG   C NH1    1 
ATOM   9887  N  NH2    . ARG   C 1  402 ? 29.926  -1.099   1.281    1.00 52.31  ? 402 ARG   C NH2    1 
ATOM   9888  N  N      . ALA   C 1  403 ? 23.707  -0.756   7.673    1.00 41.80  ? 403 ALA   C N      1 
ATOM   9889  C  CA     . ALA   C 1  403 ? 23.016  -1.039   8.922    1.00 40.44  ? 403 ALA   C CA     1 
ATOM   9890  C  C      . ALA   C 1  403 ? 23.371  -2.424   9.430    1.00 38.56  ? 403 ALA   C C      1 
ATOM   9891  O  O      . ALA   C 1  403 ? 23.351  -3.398   8.672    1.00 40.81  ? 403 ALA   C O      1 
ATOM   9892  C  CB     . ALA   C 1  403 ? 21.500  -0.937   8.731    1.00 38.65  ? 403 ALA   C CB     1 
ATOM   9893  N  N      . PHE   C 1  404 ? 23.689  -2.504   10.724   1.00 40.25  ? 404 PHE   C N      1 
ATOM   9894  C  CA     . PHE   C 1  404 ? 23.929  -3.757   11.441   1.00 36.57  ? 404 PHE   C CA     1 
ATOM   9895  C  C      . PHE   C 1  404 ? 25.230  -4.417   11.011   1.00 36.85  ? 404 PHE   C C      1 
ATOM   9896  O  O      . PHE   C 1  404 ? 25.697  -5.346   11.673   1.00 33.54  ? 404 PHE   C O      1 
ATOM   9897  C  CB     . PHE   C 1  404 ? 22.761  -4.723   11.252   1.00 34.60  ? 404 PHE   C CB     1 
ATOM   9898  C  CG     . PHE   C 1  404 ? 21.448  -4.153   11.674   1.00 37.72  ? 404 PHE   C CG     1 
ATOM   9899  C  CD1    . PHE   C 1  404 ? 21.084  -4.149   12.994   1.00 39.06  ? 404 PHE   C CD1    1 
ATOM   9900  C  CD2    . PHE   C 1  404 ? 20.594  -3.588   10.756   1.00 40.33  ? 404 PHE   C CD2    1 
ATOM   9901  C  CE1    . PHE   C 1  404 ? 19.889  -3.611   13.380   1.00 41.88  ? 404 PHE   C CE1    1 
ATOM   9902  C  CE2    . PHE   C 1  404 ? 19.401  -3.056   11.146   1.00 41.29  ? 404 PHE   C CE2    1 
ATOM   9903  C  CZ     . PHE   C 1  404 ? 19.052  -3.061   12.457   1.00 38.71  ? 404 PHE   C CZ     1 
ATOM   9904  N  N      . VAL   C 1  405 ? 25.842  -3.918   9.931    1.00 37.77  ? 405 VAL   C N      1 
ATOM   9905  C  CA     . VAL   C 1  405 ? 26.991  -4.598   9.355    1.00 40.23  ? 405 VAL   C CA     1 
ATOM   9906  C  C      . VAL   C 1  405 ? 28.154  -4.650   10.327   1.00 39.15  ? 405 VAL   C C      1 
ATOM   9907  O  O      . VAL   C 1  405 ? 29.000  -5.558   10.233   1.00 35.87  ? 405 VAL   C O      1 
ATOM   9908  C  CB     . VAL   C 1  405 ? 27.378  -3.939   8.019    1.00 44.20  ? 405 VAL   C CB     1 
ATOM   9909  C  CG1    . VAL   C 1  405 ? 28.829  -4.326   7.612    1.00 39.32  ? 405 VAL   C CG1    1 
ATOM   9910  C  CG2    . VAL   C 1  405 ? 26.362  -4.354   6.951    1.00 34.19  ? 405 VAL   C CG2    1 
ATOM   9911  N  N      . HIS   C 1  406 ? 28.188  -3.716   11.292   1.00 42.35  ? 406 HIS   C N      1 
ATOM   9912  C  CA     . HIS   C 1  406 ? 29.202  -3.734   12.348   1.00 39.58  ? 406 HIS   C CA     1 
ATOM   9913  C  C      . HIS   C 1  406 ? 29.065  -4.951   13.264   1.00 40.05  ? 406 HIS   C C      1 
ATOM   9914  O  O      . HIS   C 1  406 ? 30.083  -5.466   13.735   1.00 38.96  ? 406 HIS   C O      1 
ATOM   9915  C  CB     . HIS   C 1  406 ? 29.153  -2.430   13.158   1.00 37.81  ? 406 HIS   C CB     1 
ATOM   9916  C  CG     . HIS   C 1  406 ? 28.081  -2.394   14.197   1.00 39.89  ? 406 HIS   C CG     1 
ATOM   9917  N  ND1    . HIS   C 1  406 ? 26.795  -1.978   13.920   1.00 42.16  ? 406 HIS   C ND1    1 
ATOM   9918  C  CD2    . HIS   C 1  406 ? 28.091  -2.747   15.503   1.00 42.52  ? 406 HIS   C CD2    1 
ATOM   9919  C  CE1    . HIS   C 1  406 ? 26.057  -2.081   15.011   1.00 41.33  ? 406 HIS   C CE1    1 
ATOM   9920  N  NE2    . HIS   C 1  406 ? 26.819  -2.538   15.988   1.00 42.72  ? 406 HIS   C NE2    1 
ATOM   9921  N  N      . TRP   C 1  407 ? 27.845  -5.458   13.499   1.00 35.38  ? 407 TRP   C N      1 
ATOM   9922  C  CA     . TRP   C 1  407 ? 27.724  -6.656   14.334   1.00 41.57  ? 407 TRP   C CA     1 
ATOM   9923  C  C      . TRP   C 1  407 ? 28.388  -7.865   13.684   1.00 43.22  ? 407 TRP   C C      1 
ATOM   9924  O  O      . TRP   C 1  407 ? 28.761  -8.813   14.381   1.00 40.93  ? 407 TRP   C O      1 
ATOM   9925  C  CB     . TRP   C 1  407 ? 26.250  -6.979   14.652   1.00 43.60  ? 407 TRP   C CB     1 
ATOM   9926  C  CG     . TRP   C 1  407 ? 25.575  -5.998   15.585   1.00 43.12  ? 407 TRP   C CG     1 
ATOM   9927  C  CD1    . TRP   C 1  407 ? 24.490  -5.237   15.309   1.00 45.62  ? 407 TRP   C CD1    1 
ATOM   9928  C  CD2    . TRP   C 1  407 ? 25.976  -5.653   16.917   1.00 45.75  ? 407 TRP   C CD2    1 
ATOM   9929  N  NE1    . TRP   C 1  407 ? 24.175  -4.443   16.383   1.00 48.35  ? 407 TRP   C NE1    1 
ATOM   9930  C  CE2    . TRP   C 1  407 ? 25.073  -4.678   17.386   1.00 46.36  ? 407 TRP   C CE2    1 
ATOM   9931  C  CE3    . TRP   C 1  407 ? 27.004  -6.073   17.755   1.00 38.70  ? 407 TRP   C CE3    1 
ATOM   9932  C  CZ2    . TRP   C 1  407 ? 25.162  -4.122   18.654   1.00 41.72  ? 407 TRP   C CZ2    1 
ATOM   9933  C  CZ3    . TRP   C 1  407 ? 27.092  -5.514   19.008   1.00 50.96  ? 407 TRP   C CZ3    1 
ATOM   9934  C  CH2    . TRP   C 1  407 ? 26.173  -4.548   19.448   1.00 48.61  ? 407 TRP   C CH2    1 
ATOM   9935  N  N      . TYR   C 1  408 ? 28.529  -7.866   12.354   1.00 44.11  ? 408 TYR   C N      1 
ATOM   9936  C  CA     . TYR   C 1  408 ? 29.204  -8.966   11.683   1.00 37.64  ? 408 TYR   C CA     1 
ATOM   9937  C  C      . TYR   C 1  408 ? 30.697  -8.720   11.580   1.00 43.18  ? 408 TYR   C C      1 
ATOM   9938  O  O      . TYR   C 1  408 ? 31.486  -9.657   11.745   1.00 46.93  ? 408 TYR   C O      1 
ATOM   9939  C  CB     . TYR   C 1  408 ? 28.619  -9.187   10.289   1.00 37.11  ? 408 TYR   C CB     1 
ATOM   9940  C  CG     . TYR   C 1  408 ? 27.163  -9.569   10.301   1.00 38.73  ? 408 TYR   C CG     1 
ATOM   9941  C  CD1    . TYR   C 1  408 ? 26.196  -8.659   10.703   1.00 35.43  ? 408 TYR   C CD1    1 
ATOM   9942  C  CD2    . TYR   C 1  408 ? 26.749  -10.832  9.901    1.00 41.61  ? 408 TYR   C CD2    1 
ATOM   9943  C  CE1    . TYR   C 1  408 ? 24.871  -8.992   10.719   1.00 37.70  ? 408 TYR   C CE1    1 
ATOM   9944  C  CE2    . TYR   C 1  408 ? 25.403  -11.187  9.921    1.00 39.25  ? 408 TYR   C CE2    1 
ATOM   9945  C  CZ     . TYR   C 1  408 ? 24.472  -10.259  10.329   1.00 40.71  ? 408 TYR   C CZ     1 
ATOM   9946  O  OH     . TYR   C 1  408 ? 23.133  -10.566  10.355   1.00 39.78  ? 408 TYR   C OH     1 
ATOM   9947  N  N      . VAL   C 1  409 ? 31.106  -7.471   11.327   1.00 42.04  ? 409 VAL   C N      1 
ATOM   9948  C  CA     . VAL   C 1  409 ? 32.528  -7.169   11.171   1.00 39.73  ? 409 VAL   C CA     1 
ATOM   9949  C  C      . VAL   C 1  409 ? 33.286  -7.379   12.483   1.00 44.21  ? 409 VAL   C C      1 
ATOM   9950  O  O      . VAL   C 1  409 ? 34.431  -7.836   12.482   1.00 51.40  ? 409 VAL   C O      1 
ATOM   9951  C  CB     . VAL   C 1  409 ? 32.720  -5.740   10.637   1.00 42.62  ? 409 VAL   C CB     1 
ATOM   9952  C  CG1    . VAL   C 1  409 ? 34.165  -5.311   10.842   1.00 43.40  ? 409 VAL   C CG1    1 
ATOM   9953  C  CG2    . VAL   C 1  409 ? 32.327  -5.649   9.162    1.00 41.05  ? 409 VAL   C CG2    1 
ATOM   9954  N  N      . GLY   C 1  410 ? 32.666  -7.051   13.618   1.00 43.42  ? 410 GLY   C N      1 
ATOM   9955  C  CA     . GLY   C 1  410 ? 33.285  -7.268   14.911   1.00 35.39  ? 410 GLY   C CA     1 
ATOM   9956  C  C      . GLY   C 1  410 ? 33.432  -8.720   15.301   1.00 40.74  ? 410 GLY   C C      1 
ATOM   9957  O  O      . GLY   C 1  410 ? 34.199  -9.030   16.217   1.00 38.85  ? 410 GLY   C O      1 
ATOM   9958  N  N      . GLU   C 1  411 ? 32.701  -9.618   14.651   1.00 45.88  ? 411 GLU   C N      1 
ATOM   9959  C  CA     . GLU   C 1  411 ? 32.897  -11.039  14.873   1.00 45.55  ? 411 GLU   C CA     1 
ATOM   9960  C  C      . GLU   C 1  411 ? 33.904  -11.645  13.901   1.00 47.13  ? 411 GLU   C C      1 
ATOM   9961  O  O      . GLU   C 1  411 ? 34.109  -12.860  13.924   1.00 47.14  ? 411 GLU   C O      1 
ATOM   9962  C  CB     . GLU   C 1  411 ? 31.562  -11.766  14.797   1.00 41.51  ? 411 GLU   C CB     1 
ATOM   9963  C  CG     . GLU   C 1  411 ? 30.637  -11.370  15.920   1.00 37.39  ? 411 GLU   C CG     1 
ATOM   9964  C  CD     . GLU   C 1  411 ? 31.015  -12.005  17.238   1.00 48.28  ? 411 GLU   C CD     1 
ATOM   9965  O  OE1    . GLU   C 1  411 ? 31.875  -12.913  17.238   1.00 50.19  ? 411 GLU   C OE1    1 
ATOM   9966  O  OE2    . GLU   C 1  411 ? 30.446  -11.609  18.285   1.00 45.72  ? 411 GLU   C OE2    1 
ATOM   9967  N  N      . GLY   C 1  412 ? 34.546  -10.824  13.065   1.00 44.15  ? 412 GLY   C N      1 
ATOM   9968  C  CA     . GLY   C 1  412 ? 35.625  -11.259  12.202   1.00 48.64  ? 412 GLY   C CA     1 
ATOM   9969  C  C      . GLY   C 1  412 ? 35.353  -11.169  10.712   1.00 46.38  ? 412 GLY   C C      1 
ATOM   9970  O  O      . GLY   C 1  412 ? 36.293  -11.310  9.926    1.00 43.64  ? 412 GLY   C O      1 
ATOM   9971  N  N      . MET   C 1  413 ? 34.113  -10.946  10.289   1.00 45.76  ? 413 MET   C N      1 
ATOM   9972  C  CA     . MET   C 1  413 ? 33.797  -10.912  8.870    1.00 47.04  ? 413 MET   C CA     1 
ATOM   9973  C  C      . MET   C 1  413 ? 34.121  -9.564   8.238    1.00 45.96  ? 413 MET   C C      1 
ATOM   9974  O  O      . MET   C 1  413 ? 34.080  -8.518   8.890    1.00 50.74  ? 413 MET   C O      1 
ATOM   9975  C  CB     . MET   C 1  413 ? 32.322  -11.229  8.633    1.00 46.62  ? 413 MET   C CB     1 
ATOM   9976  C  CG     . MET   C 1  413 ? 31.906  -12.648  8.979    1.00 43.87  ? 413 MET   C CG     1 
ATOM   9977  S  SD     . MET   C 1  413 ? 30.205  -12.841  8.475    1.00 43.87  ? 413 MET   C SD     1 
ATOM   9978  C  CE     . MET   C 1  413 ? 30.295  -12.373  6.736    1.00 36.27  ? 413 MET   C CE     1 
ATOM   9979  N  N      . GLU   C 1  414 ? 34.407  -9.597   6.941    1.00 45.57  ? 414 GLU   C N      1 
ATOM   9980  C  CA     . GLU   C 1  414 ? 34.718  -8.400   6.176    1.00 45.49  ? 414 GLU   C CA     1 
ATOM   9981  C  C      . GLU   C 1  414 ? 33.546  -8.022   5.284    1.00 47.07  ? 414 GLU   C C      1 
ATOM   9982  O  O      . GLU   C 1  414 ? 32.765  -8.876   4.850    1.00 50.24  ? 414 GLU   C O      1 
ATOM   9983  C  CB     . GLU   C 1  414 ? 35.961  -8.599   5.319    1.00 39.93  ? 414 GLU   C CB     1 
ATOM   9984  C  CG     . GLU   C 1  414 ? 37.196  -8.869   6.134    1.00 47.09  ? 414 GLU   C CG     1 
ATOM   9985  C  CD     . GLU   C 1  414 ? 38.366  -9.183   5.247    1.00 50.04  ? 414 GLU   C CD     1 
ATOM   9986  O  OE1    . GLU   C 1  414 ? 38.413  -8.547   4.174    1.00 57.19  ? 414 GLU   C OE1    1 
ATOM   9987  O  OE2    . GLU   C 1  414 ? 39.219  -10.041  5.610    1.00 45.49  ? 414 GLU   C OE2    1 
ATOM   9988  N  N      . GLU   C 1  415 ? 33.425  -6.725   5.014    1.00 44.98  ? 415 GLU   C N      1 
ATOM   9989  C  CA     . GLU   C 1  415 ? 32.401  -6.273   4.083    1.00 43.39  ? 415 GLU   C CA     1 
ATOM   9990  C  C      . GLU   C 1  415 ? 32.466  -7.048   2.767    1.00 45.07  ? 415 GLU   C C      1 
ATOM   9991  O  O      . GLU   C 1  415 ? 31.437  -7.248   2.107    1.00 46.45  ? 415 GLU   C O      1 
ATOM   9992  C  CB     . GLU   C 1  415 ? 32.555  -4.768   3.840    1.00 44.86  ? 415 GLU   C CB     1 
ATOM   9993  C  CG     . GLU   C 1  415 ? 31.889  -3.874   4.912    1.00 57.74  ? 415 GLU   C CG     1 
ATOM   9994  C  CD     . GLU   C 1  415 ? 31.787  -2.393   4.513    1.00 60.09  ? 415 GLU   C CD     1 
ATOM   9995  O  OE1    . GLU   C 1  415 ? 32.187  -2.029   3.378    1.00 58.26  ? 415 GLU   C OE1    1 
ATOM   9996  O  OE2    . GLU   C 1  415 ? 31.305  -1.590   5.351    1.00 62.56  ? 415 GLU   C OE2    1 
ATOM   9997  N  N      . GLY   C 1  416 ? 33.661  -7.501   2.374    1.00 41.25  ? 416 GLY   C N      1 
ATOM   9998  C  CA     . GLY   C 1  416 ? 33.805  -8.142   1.080    1.00 38.76  ? 416 GLY   C CA     1 
ATOM   9999  C  C      . GLY   C 1  416 ? 33.029  -9.434   0.964    1.00 41.23  ? 416 GLY   C C      1 
ATOM   10000 O  O      . GLY   C 1  416 ? 32.505  -9.755   -0.105   1.00 43.92  ? 416 GLY   C O      1 
ATOM   10001 N  N      . GLU   C 1  417 ? 32.951  -10.196  2.053    1.00 41.98  ? 417 GLU   C N      1 
ATOM   10002 C  CA     . GLU   C 1  417 ? 32.070  -11.356  2.091    1.00 43.20  ? 417 GLU   C CA     1 
ATOM   10003 C  C      . GLU   C 1  417 ? 30.625  -10.983  1.772    1.00 42.68  ? 417 GLU   C C      1 
ATOM   10004 O  O      . GLU   C 1  417 ? 29.900  -11.767  1.151    1.00 48.04  ? 417 GLU   C O      1 
ATOM   10005 C  CB     . GLU   C 1  417 ? 32.153  -12.006  3.458    1.00 40.69  ? 417 GLU   C CB     1 
ATOM   10006 C  CG     . GLU   C 1  417 ? 33.513  -12.512  3.757    1.00 37.97  ? 417 GLU   C CG     1 
ATOM   10007 C  CD     . GLU   C 1  417 ? 33.637  -12.931  5.198    1.00 50.26  ? 417 GLU   C CD     1 
ATOM   10008 O  OE1    . GLU   C 1  417 ? 33.160  -14.058  5.515    1.00 51.52  ? 417 GLU   C OE1    1 
ATOM   10009 O  OE2    . GLU   C 1  417 ? 34.205  -12.137  6.000    1.00 45.94  ? 417 GLU   C OE2    1 
ATOM   10010 N  N      . PHE   C 1  418 ? 30.193  -9.793   2.190    1.00 40.39  ? 418 PHE   C N      1 
ATOM   10011 C  CA     . PHE   C 1  418 ? 28.832  -9.346   1.913    1.00 39.34  ? 418 PHE   C CA     1 
ATOM   10012 C  C      . PHE   C 1  418 ? 28.634  -9.108   0.432    1.00 41.57  ? 418 PHE   C C      1 
ATOM   10013 O  O      . PHE   C 1  418 ? 27.656  -9.582   -0.157   1.00 43.11  ? 418 PHE   C O      1 
ATOM   10014 C  CB     . PHE   C 1  418 ? 28.503  -8.062   2.690    1.00 41.29  ? 418 PHE   C CB     1 
ATOM   10015 C  CG     . PHE   C 1  418 ? 28.098  -8.299   4.116    1.00 41.16  ? 418 PHE   C CG     1 
ATOM   10016 C  CD1    . PHE   C 1  418 ? 29.040  -8.626   5.079    1.00 40.69  ? 418 PHE   C CD1    1 
ATOM   10017 C  CD2    . PHE   C 1  418 ? 26.776  -8.198   4.494    1.00 39.95  ? 418 PHE   C CD2    1 
ATOM   10018 C  CE1    . PHE   C 1  418 ? 28.662  -8.852   6.386    1.00 40.28  ? 418 PHE   C CE1    1 
ATOM   10019 C  CE2    . PHE   C 1  418 ? 26.390  -8.431   5.814    1.00 37.70  ? 418 PHE   C CE2    1 
ATOM   10020 C  CZ     . PHE   C 1  418 ? 27.333  -8.760   6.750    1.00 39.77  ? 418 PHE   C CZ     1 
ATOM   10021 N  N      . SER   C 1  419 ? 29.532  -8.349   -0.192   1.00 43.83  ? 419 SER   C N      1 
ATOM   10022 C  CA     . SER   C 1  419 ? 29.320  -8.071   -1.610   1.00 42.91  ? 419 SER   C CA     1 
ATOM   10023 C  C      . SER   C 1  419 ? 29.538  -9.322   -2.431   1.00 42.64  ? 419 SER   C C      1 
ATOM   10024 O  O      . SER   C 1  419 ? 28.865  -9.523   -3.445   1.00 47.31  ? 419 SER   C O      1 
ATOM   10025 C  CB     . SER   C 1  419 ? 30.221  -6.943   -2.093   1.00 34.38  ? 419 SER   C CB     1 
ATOM   10026 O  OG     . SER   C 1  419 ? 31.447  -6.973   -1.396   1.00 51.42  ? 419 SER   C OG     1 
ATOM   10027 N  N      . GLU   C 1  420 ? 30.451  -10.186  -1.998   1.00 41.69  ? 420 GLU   C N      1 
ATOM   10028 C  CA     . GLU   C 1  420 ? 30.645  -11.440  -2.699   1.00 39.86  ? 420 GLU   C CA     1 
ATOM   10029 C  C      . GLU   C 1  420 ? 29.370  -12.274  -2.649   1.00 42.08  ? 420 GLU   C C      1 
ATOM   10030 O  O      . GLU   C 1  420 ? 28.909  -12.785  -3.675   1.00 41.49  ? 420 GLU   C O      1 
ATOM   10031 C  CB     . GLU   C 1  420 ? 31.836  -12.170  -2.096   1.00 41.80  ? 420 GLU   C CB     1 
ATOM   10032 C  CG     . GLU   C 1  420 ? 31.925  -13.630  -2.452   1.00 52.51  ? 420 GLU   C CG     1 
ATOM   10033 C  CD     . GLU   C 1  420 ? 33.035  -14.330  -1.699   1.00 60.67  ? 420 GLU   C CD     1 
ATOM   10034 O  OE1    . GLU   C 1  420 ? 34.165  -13.768  -1.659   1.00 65.42  ? 420 GLU   C OE1    1 
ATOM   10035 O  OE2    . GLU   C 1  420 ? 32.765  -15.430  -1.149   1.00 50.66  ? 420 GLU   C OE2    1 
ATOM   10036 N  N      . ALA   C 1  421 ? 28.761  -12.391  -1.464   1.00 39.18  ? 421 ALA   C N      1 
ATOM   10037 C  CA     . ALA   C 1  421 ? 27.503  -13.118  -1.347   1.00 34.35  ? 421 ALA   C CA     1 
ATOM   10038 C  C      . ALA   C 1  421 ? 26.406  -12.490  -2.214   1.00 38.65  ? 421 ALA   C C      1 
ATOM   10039 O  O      . ALA   C 1  421 ? 25.749  -13.182  -3.005   1.00 39.06  ? 421 ALA   C O      1 
ATOM   10040 C  CB     . ALA   C 1  421 ? 27.067  -13.172  0.110    1.00 36.21  ? 421 ALA   C CB     1 
ATOM   10041 N  N      . ARG   C 1  422 ? 26.192  -11.178  -2.089   1.00 31.04  ? 422 ARG   C N      1 
ATOM   10042 C  CA     . ARG   C 1  422 ? 25.126  -10.566  -2.872   1.00 32.70  ? 422 ARG   C CA     1 
ATOM   10043 C  C      . ARG   C 1  422 ? 25.382  -10.683  -4.368   1.00 34.50  ? 422 ARG   C C      1 
ATOM   10044 O  O      . ARG   C 1  422 ? 24.430  -10.747  -5.151   1.00 39.61  ? 422 ARG   C O      1 
ATOM   10045 C  CB     . ARG   C 1  422 ? 24.926  -9.100   -2.490   1.00 35.10  ? 422 ARG   C CB     1 
ATOM   10046 C  CG     . ARG   C 1  422 ? 23.836  -8.413   -3.305   1.00 28.24  ? 422 ARG   C CG     1 
ATOM   10047 C  CD     . ARG   C 1  422 ? 22.478  -8.955   -2.938   1.00 38.09  ? 422 ARG   C CD     1 
ATOM   10048 N  NE     . ARG   C 1  422 ? 21.408  -8.250   -3.628   1.00 37.11  ? 422 ARG   C NE     1 
ATOM   10049 C  CZ     . ARG   C 1  422 ? 21.097  -8.448   -4.901   1.00 42.44  ? 422 ARG   C CZ     1 
ATOM   10050 N  NH1    . ARG   C 1  422 ? 21.751  -9.331   -5.644   1.00 38.29  ? 422 ARG   C NH1    1 
ATOM   10051 N  NH2    . ARG   C 1  422 ? 20.104  -7.745   -5.443   1.00 41.71  ? 422 ARG   C NH2    1 
ATOM   10052 N  N      . GLU   C 1  423 ? 26.638  -10.695  -4.800   1.00 36.46  ? 423 GLU   C N      1 
ATOM   10053 C  CA     . GLU   C 1  423 ? 26.886  -10.859  -6.225   1.00 37.57  ? 423 GLU   C CA     1 
ATOM   10054 C  C      . GLU   C 1  423 ? 26.514  -12.266  -6.662   1.00 37.44  ? 423 GLU   C C      1 
ATOM   10055 O  O      . GLU   C 1  423 ? 25.845  -12.455  -7.682   1.00 37.89  ? 423 GLU   C O      1 
ATOM   10056 C  CB     . GLU   C 1  423 ? 28.343  -10.555  -6.560   1.00 38.58  ? 423 GLU   C CB     1 
ATOM   10057 C  CG     . GLU   C 1  423 ? 28.779  -9.148   -6.221   1.00 50.38  ? 423 GLU   C CG     1 
ATOM   10058 C  CD     . GLU   C 1  423 ? 30.214  -8.840   -6.658   1.00 65.11  ? 423 GLU   C CD     1 
ATOM   10059 O  OE1    . GLU   C 1  423 ? 30.922  -8.146   -5.891   1.00 59.21  ? 423 GLU   C OE1    1 
ATOM   10060 O  OE2    . GLU   C 1  423 ? 30.625  -9.257   -7.773   1.00 75.37  ? 423 GLU   C OE2    1 
ATOM   10061 N  N      . ASP   C 1  424 ? 26.919  -13.270  -5.887   1.00 33.32  ? 424 ASP   C N      1 
ATOM   10062 C  CA     . ASP   C 1  424 ? 26.497  -14.625  -6.191   1.00 28.65  ? 424 ASP   C CA     1 
ATOM   10063 C  C      . ASP   C 1  424 ? 24.982  -14.666  -6.378   1.00 37.47  ? 424 ASP   C C      1 
ATOM   10064 O  O      . ASP   C 1  424 ? 24.480  -15.161  -7.395   1.00 38.40  ? 424 ASP   C O      1 
ATOM   10065 C  CB     . ASP   C 1  424 ? 26.960  -15.559  -5.077   1.00 30.35  ? 424 ASP   C CB     1 
ATOM   10066 C  CG     . ASP   C 1  424 ? 26.935  -17.010  -5.483   1.00 31.35  ? 424 ASP   C CG     1 
ATOM   10067 O  OD1    . ASP   C 1  424 ? 26.690  -17.261  -6.664   1.00 34.94  ? 424 ASP   C OD1    1 
ATOM   10068 O  OD2    . ASP   C 1  424 ? 27.138  -17.904  -4.626   1.00 33.36  ? 424 ASP   C OD2    1 
ATOM   10069 N  N      . MET   C 1  425 ? 24.243  -14.112  -5.409   1.00 34.89  ? 425 MET   C N      1 
ATOM   10070 C  CA     . MET   C 1  425 ? 22.792  -13.997  -5.508   1.00 32.87  ? 425 MET   C CA     1 
ATOM   10071 C  C      . MET   C 1  425 ? 22.371  -13.227  -6.755   1.00 35.42  ? 425 MET   C C      1 
ATOM   10072 O  O      . MET   C 1  425 ? 21.354  -13.541  -7.380   1.00 36.89  ? 425 MET   C O      1 
ATOM   10073 C  CB     . MET   C 1  425 ? 22.234  -13.280  -4.271   1.00 32.07  ? 425 MET   C CB     1 
ATOM   10074 C  CG     . MET   C 1  425 ? 22.295  -14.020  -2.970   1.00 33.65  ? 425 MET   C CG     1 
ATOM   10075 S  SD     . MET   C 1  425 ? 21.897  -15.762  -3.163   1.00 38.69  ? 425 MET   C SD     1 
ATOM   10076 C  CE     . MET   C 1  425 ? 20.113  -15.697  -3.273   1.00 32.17  ? 425 MET   C CE     1 
ATOM   10077 N  N      . ALA   C 1  426 ? 23.083  -12.153  -7.084   1.00 35.92  ? 426 ALA   C N      1 
ATOM   10078 C  CA     . ALA   C 1  426 ? 22.743  -11.416  -8.297   1.00 36.36  ? 426 ALA   C CA     1 
ATOM   10079 C  C      . ALA   C 1  426 ? 22.860  -12.324  -9.512   1.00 40.31  ? 426 ALA   C C      1 
ATOM   10080 O  O      . ALA   C 1  426 ? 21.996  -12.325  -10.395  1.00 40.36  ? 426 ALA   C O      1 
ATOM   10081 C  CB     . ALA   C 1  426 ? 23.653  -10.205  -8.446   1.00 23.59  ? 426 ALA   C CB     1 
ATOM   10082 N  N      . ALA   C 1  427 ? 23.934  -13.113  -9.556   1.00 41.57  ? 427 ALA   C N      1 
ATOM   10083 C  CA     . ALA   C 1  427 ? 24.145  -14.072  -10.625  1.00 35.44  ? 427 ALA   C CA     1 
ATOM   10084 C  C      . ALA   C 1  427 ? 23.056  -15.150  -10.622  1.00 37.81  ? 427 ALA   C C      1 
ATOM   10085 O  O      . ALA   C 1  427 ? 22.483  -15.466  -11.671  1.00 38.35  ? 427 ALA   C O      1 
ATOM   10086 C  CB     . ALA   C 1  427 ? 25.551  -14.662  -10.472  1.00 22.33  ? 427 ALA   C CB     1 
ATOM   10087 N  N      . LEU   C 1  428 ? 22.753  -15.725  -9.451   1.00 32.34  ? 428 LEU   C N      1 
ATOM   10088 C  CA     . LEU   C 1  428 ? 21.699  -16.729  -9.369   1.00 29.83  ? 428 LEU   C CA     1 
ATOM   10089 C  C      . LEU   C 1  428 ? 20.412  -16.210  -9.993   1.00 36.66  ? 428 LEU   C C      1 
ATOM   10090 O  O      . LEU   C 1  428 ? 19.761  -16.902  -10.783  1.00 37.32  ? 428 LEU   C O      1 
ATOM   10091 C  CB     . LEU   C 1  428 ? 21.456  -17.133  -7.910   1.00 29.24  ? 428 LEU   C CB     1 
ATOM   10092 C  CG     . LEU   C 1  428 ? 20.514  -18.312  -7.622   1.00 30.97  ? 428 LEU   C CG     1 
ATOM   10093 C  CD1    . LEU   C 1  428 ? 20.990  -19.538  -8.346   1.00 29.77  ? 428 LEU   C CD1    1 
ATOM   10094 C  CD2    . LEU   C 1  428 ? 20.378  -18.632  -6.146   1.00 31.53  ? 428 LEU   C CD2    1 
ATOM   10095 N  N      . GLU   C 1  429 ? 20.006  -14.996  -9.624   1.00 39.98  ? 429 GLU   C N      1 
ATOM   10096 C  CA     . GLU   C 1  429 ? 18.805  -14.426  -10.219  1.00 38.67  ? 429 GLU   C CA     1 
ATOM   10097 C  C      . GLU   C 1  429 ? 18.956  -14.266  -11.731  1.00 36.78  ? 429 GLU   C C      1 
ATOM   10098 O  O      . GLU   C 1  429 ? 17.969  -14.392  -12.463  1.00 37.95  ? 429 GLU   C O      1 
ATOM   10099 C  CB     . GLU   C 1  429 ? 18.477  -13.084  -9.559   1.00 38.86  ? 429 GLU   C CB     1 
ATOM   10100 C  CG     . GLU   C 1  429 ? 17.702  -13.167  -8.236   1.00 39.65  ? 429 GLU   C CG     1 
ATOM   10101 C  CD     . GLU   C 1  429 ? 17.372  -11.772  -7.720   1.00 41.95  ? 429 GLU   C CD     1 
ATOM   10102 O  OE1    . GLU   C 1  429 ? 16.589  -11.072  -8.383   1.00 44.96  ? 429 GLU   C OE1    1 
ATOM   10103 O  OE2    . GLU   C 1  429 ? 17.923  -11.352  -6.686   1.00 42.84  ? 429 GLU   C OE2    1 
ATOM   10104 N  N      . LYS   C 1  430 ? 20.178  -14.001  -12.210  1.00 33.55  ? 430 LYS   C N      1 
ATOM   10105 C  CA     . LYS   C 1  430 ? 20.443  -13.901  -13.645  1.00 38.60  ? 430 LYS   C CA     1 
ATOM   10106 C  C      . LYS   C 1  430 ? 20.442  -15.268  -14.323  1.00 39.16  ? 430 LYS   C C      1 
ATOM   10107 O  O      . LYS   C 1  430 ? 19.994  -15.392  -15.467  1.00 40.03  ? 430 LYS   C O      1 
ATOM   10108 C  CB     . LYS   C 1  430 ? 21.780  -13.203  -13.897  1.00 34.57  ? 430 LYS   C CB     1 
ATOM   10109 C  CG     . LYS   C 1  430 ? 21.868  -12.459  -15.219  1.00 46.45  ? 430 LYS   C CG     1 
ATOM   10110 C  CD     . LYS   C 1  430 ? 20.832  -11.317  -15.246  1.00 64.74  ? 430 LYS   C CD     1 
ATOM   10111 C  CE     . LYS   C 1  430 ? 20.409  -10.895  -16.654  1.00 67.62  ? 430 LYS   C CE     1 
ATOM   10112 N  NZ     . LYS   C 1  430 ? 20.341  -9.395   -16.726  1.00 73.04  ? 430 LYS   C NZ     1 
ATOM   10113 N  N      . ASP   C 1  431 ? 20.951  -16.298  -13.641  1.00 34.81  ? 431 ASP   C N      1 
ATOM   10114 C  CA     . ASP   C 1  431 ? 20.810  -17.658  -14.143  1.00 34.48  ? 431 ASP   C CA     1 
ATOM   10115 C  C      . ASP   C 1  431 ? 19.347  -18.038  -14.310  1.00 34.73  ? 431 ASP   C C      1 
ATOM   10116 O  O      . ASP   C 1  431 ? 18.973  -18.728  -15.270  1.00 34.19  ? 431 ASP   C O      1 
ATOM   10117 C  CB     . ASP   C 1  431 ? 21.501  -18.625  -13.200  1.00 27.71  ? 431 ASP   C CB     1 
ATOM   10118 C  CG     . ASP   C 1  431 ? 22.988  -18.483  -13.248  1.00 37.89  ? 431 ASP   C CG     1 
ATOM   10119 O  OD1    . ASP   C 1  431 ? 23.493  -18.181  -14.359  1.00 42.87  ? 431 ASP   C OD1    1 
ATOM   10120 O  OD2    . ASP   C 1  431 ? 23.648  -18.638  -12.184  1.00 38.76  ? 431 ASP   C OD2    1 
ATOM   10121 N  N      . TYR   C 1  432 ? 18.501  -17.612  -13.385  1.00 32.46  ? 432 TYR   C N      1 
ATOM   10122 C  CA     . TYR   C 1  432 ? 17.120  -18.030  -13.490  1.00 33.62  ? 432 TYR   C CA     1 
ATOM   10123 C  C      . TYR   C 1  432 ? 16.447  -17.309  -14.635  1.00 37.45  ? 432 TYR   C C      1 
ATOM   10124 O  O      . TYR   C 1  432 ? 15.553  -17.877  -15.275  1.00 40.79  ? 432 TYR   C O      1 
ATOM   10125 C  CB     . TYR   C 1  432 ? 16.399  -17.822  -12.164  1.00 39.07  ? 432 TYR   C CB     1 
ATOM   10126 C  CG     . TYR   C 1  432 ? 16.421  -19.055  -11.299  1.00 33.23  ? 432 TYR   C CG     1 
ATOM   10127 C  CD1    . TYR   C 1  432 ? 15.604  -20.129  -11.601  1.00 33.50  ? 432 TYR   C CD1    1 
ATOM   10128 C  CD2    . TYR   C 1  432 ? 17.272  -19.164  -10.199  1.00 31.12  ? 432 TYR   C CD2    1 
ATOM   10129 C  CE1    . TYR   C 1  432 ? 15.602  -21.287  -10.822  1.00 31.73  ? 432 TYR   C CE1    1 
ATOM   10130 C  CE2    . TYR   C 1  432 ? 17.271  -20.337  -9.398   1.00 36.04  ? 432 TYR   C CE2    1 
ATOM   10131 C  CZ     . TYR   C 1  432 ? 16.430  -21.394  -9.730   1.00 34.54  ? 432 TYR   C CZ     1 
ATOM   10132 O  OH     . TYR   C 1  432 ? 16.389  -22.571  -9.000   1.00 39.13  ? 432 TYR   C OH     1 
ATOM   10133 N  N      . GLU   C 1  433 ? 16.915  -16.099  -14.963  1.00 36.82  ? 433 GLU   C N      1 
ATOM   10134 C  CA     . GLU   C 1  433 ? 16.456  -15.449  -16.188  1.00 35.06  ? 433 GLU   C CA     1 
ATOM   10135 C  C      . GLU   C 1  433 ? 16.920  -16.217  -17.418  1.00 39.42  ? 433 GLU   C C      1 
ATOM   10136 O  O      . GLU   C 1  433 ? 16.145  -16.431  -18.362  1.00 37.89  ? 433 GLU   C O      1 
ATOM   10137 C  CB     . GLU   C 1  433 ? 16.962  -14.012  -16.255  1.00 38.03  ? 433 GLU   C CB     1 
ATOM   10138 C  CG     . GLU   C 1  433 ? 16.139  -12.962  -15.491  1.00 61.56  ? 433 GLU   C CG     1 
ATOM   10139 C  CD     . GLU   C 1  433 ? 16.828  -11.593  -15.460  1.00 71.99  ? 433 GLU   C CD     1 
ATOM   10140 O  OE1    . GLU   C 1  433 ? 17.027  -11.055  -14.332  1.00 68.92  ? 433 GLU   C OE1    1 
ATOM   10141 O  OE2    . GLU   C 1  433 ? 17.182  -11.084  -16.561  1.00 61.68  ? 433 GLU   C OE2    1 
ATOM   10142 N  N      . GLU   C 1  434 ? 18.187  -16.636  -17.426  1.00 35.52  ? 434 GLU   C N      1 
ATOM   10143 C  CA     . GLU   C 1  434 ? 18.774  -17.189  -18.636  1.00 38.06  ? 434 GLU   C CA     1 
ATOM   10144 C  C      . GLU   C 1  434 ? 18.116  -18.520  -19.013  1.00 40.92  ? 434 GLU   C C      1 
ATOM   10145 O  O      . GLU   C 1  434 ? 17.788  -18.745  -20.183  1.00 41.03  ? 434 GLU   C O      1 
ATOM   10146 C  CB     . GLU   C 1  434 ? 20.286  -17.342  -18.456  1.00 34.92  ? 434 GLU   C CB     1 
ATOM   10147 C  CG     . GLU   C 1  434 ? 21.091  -16.043  -18.583  1.00 37.66  ? 434 GLU   C CG     1 
ATOM   10148 C  CD     . GLU   C 1  434 ? 22.576  -16.176  -18.136  1.00 54.30  ? 434 GLU   C CD     1 
ATOM   10149 O  OE1    . GLU   C 1  434 ? 23.099  -17.318  -18.006  1.00 53.90  ? 434 GLU   C OE1    1 
ATOM   10150 O  OE2    . GLU   C 1  434 ? 23.226  -15.127  -17.898  1.00 52.55  ? 434 GLU   C OE2    1 
ATOM   10151 N  N      . VAL   C 1  435 ? 17.894  -19.409  -18.037  1.00 33.77  ? 435 VAL   C N      1 
ATOM   10152 C  CA     . VAL   C 1  435 ? 17.282  -20.691  -18.363  1.00 33.23  ? 435 VAL   C CA     1 
ATOM   10153 C  C      . VAL   C 1  435 ? 15.918  -20.507  -19.037  1.00 35.27  ? 435 VAL   C C      1 
ATOM   10154 O  O      . VAL   C 1  435 ? 15.459  -21.380  -19.784  1.00 42.86  ? 435 VAL   C O      1 
ATOM   10155 C  CB     . VAL   C 1  435 ? 17.163  -21.571  -17.097  1.00 39.65  ? 435 VAL   C CB     1 
ATOM   10156 C  CG1    . VAL   C 1  435 ? 18.536  -22.015  -16.585  1.00 30.02  ? 435 VAL   C CG1    1 
ATOM   10157 C  CG2    . VAL   C 1  435 ? 16.341  -20.879  -16.016  1.00 33.74  ? 435 VAL   C CG2    1 
ATOM   10158 N  N      . GLY   C 1  436 ? 15.251  -19.392  -18.798  1.00 35.52  ? 436 GLY   C N      1 
ATOM   10159 C  CA     . GLY   C 1  436 ? 13.892  -19.251  -19.276  1.00 35.25  ? 436 GLY   C CA     1 
ATOM   10160 C  C      . GLY   C 1  436 ? 13.807  -18.732  -20.695  1.00 40.91  ? 436 GLY   C C      1 
ATOM   10161 O  O      . GLY   C 1  436 ? 12.841  -19.004  -21.418  1.00 44.35  ? 436 GLY   C O      1 
ATOM   10162 N  N      . VAL   C 1  437 ? 14.820  -17.964  -21.097  1.00 38.98  ? 437 VAL   C N      1 
ATOM   10163 C  CA     . VAL   C 1  437 ? 14.881  -17.454  -22.455  1.00 34.51  ? 437 VAL   C CA     1 
ATOM   10164 C  C      . VAL   C 1  437 ? 14.874  -18.613  -23.437  1.00 38.46  ? 437 VAL   C C      1 
ATOM   10165 O  O      . VAL   C 1  437 ? 15.429  -19.685  -23.172  1.00 38.11  ? 437 VAL   C O      1 
ATOM   10166 C  CB     . VAL   C 1  437 ? 16.144  -16.606  -22.658  1.00 36.49  ? 437 VAL   C CB     1 
ATOM   10167 C  CG1    . VAL   C 1  437 ? 16.291  -16.248  -24.113  1.00 39.04  ? 437 VAL   C CG1    1 
ATOM   10168 C  CG2    . VAL   C 1  437 ? 16.128  -15.393  -21.750  1.00 30.62  ? 437 VAL   C CG2    1 
ATOM   10169 N  N      . ASP   C 1  438 ? 14.271  -18.384  -24.600  1.00 45.25  ? 438 ASP   C N      1 
ATOM   10170 C  CA     . ASP   C 1  438 ? 14.179  -19.411  -25.627  1.00 46.54  ? 438 ASP   C CA     1 
ATOM   10171 C  C      . ASP   C 1  438 ? 15.550  -19.655  -26.264  1.00 47.28  ? 438 ASP   C C      1 
ATOM   10172 O  O      . ASP   C 1  438 ? 16.523  -18.925  -26.029  1.00 46.70  ? 438 ASP   C O      1 
ATOM   10173 C  CB     . ASP   C 1  438 ? 13.156  -19.004  -26.688  1.00 47.75  ? 438 ASP   C CB     1 
ATOM   10174 C  CG     . ASP   C 1  438 ? 11.717  -19.180  -26.226  1.00 53.44  ? 438 ASP   C CG     1 
ATOM   10175 O  OD1    . ASP   C 1  438 ? 11.426  -20.068  -25.386  1.00 51.89  ? 438 ASP   C OD1    1 
ATOM   10176 O  OD2    . ASP   C 1  438 ? 10.872  -18.399  -26.705  1.00 59.17  ? 438 ASP   C OD2    1 
ATOM   10177 N  N      . SER   C 1  439 ? 15.622  -20.718  -27.064  1.00 49.48  ? 439 SER   C N      1 
ATOM   10178 C  CA     . SER   C 1  439 ? 16.829  -21.087  -27.785  1.00 47.07  ? 439 SER   C CA     1 
ATOM   10179 C  C      . SER   C 1  439 ? 16.868  -20.406  -29.153  1.00 53.27  ? 439 SER   C C      1 
ATOM   10180 O  O      . SER   C 1  439 ? 15.886  -19.816  -29.615  1.00 55.82  ? 439 SER   C O      1 
ATOM   10181 C  CB     . SER   C 1  439 ? 16.907  -22.601  -27.932  1.00 42.66  ? 439 SER   C CB     1 
ATOM   10182 O  OG     . SER   C 1  439 ? 16.765  -23.240  -26.688  1.00 38.27  ? 439 SER   C OG     1 
ATOM   10183 N  N      . VAL   C 1  440 ? 18.024  -20.507  -29.807  1.00 58.63  ? 440 VAL   C N      1 
ATOM   10184 C  CA     . VAL   C 1  440 ? 18.285  -19.816  -31.074  1.00 64.93  ? 440 VAL   C CA     1 
ATOM   10185 C  C      . VAL   C 1  440 ? 18.560  -20.805  -32.218  1.00 71.92  ? 440 VAL   C C      1 
ATOM   10186 O  O      . VAL   C 1  440 ? 18.498  -20.461  -33.410  1.00 81.88  ? 440 VAL   C O      1 
ATOM   10187 C  CB     . VAL   C 1  440 ? 19.466  -18.855  -30.907  1.00 68.27  ? 440 VAL   C CB     1 
ATOM   10188 C  CG1    . VAL   C 1  440 ? 19.402  -18.185  -29.522  1.00 55.88  ? 440 VAL   C CG1    1 
ATOM   10189 C  CG2    . VAL   C 1  440 ? 20.801  -19.595  -31.140  1.00 63.58  ? 440 VAL   C CG2    1 
ATOM   10190 N  N      . MET   D 2  1   ? 21.219  -21.387  31.635   1.00 82.81  ? 1   MET   D N      1 
ATOM   10191 C  CA     . MET   D 2  1   ? 21.256  -20.137  32.401   1.00 86.53  ? 1   MET   D CA     1 
ATOM   10192 C  C      . MET   D 2  1   ? 22.119  -19.044  31.714   1.00 83.35  ? 1   MET   D C      1 
ATOM   10193 O  O      . MET   D 2  1   ? 23.223  -19.330  31.251   1.00 86.32  ? 1   MET   D O      1 
ATOM   10194 C  CB     . MET   D 2  1   ? 21.749  -20.445  33.827   1.00 84.98  ? 1   MET   D CB     1 
ATOM   10195 C  CG     . MET   D 2  1   ? 23.188  -20.968  33.887   1.00 90.40  ? 1   MET   D CG     1 
ATOM   10196 S  SD     . MET   D 2  1   ? 23.695  -21.636  35.504   1.00 113.61 ? 1   MET   D SD     1 
ATOM   10197 C  CE     . MET   D 2  1   ? 22.553  -23.005  35.729   1.00 92.00  ? 1   MET   D CE     1 
ATOM   10198 N  N      . ARG   D 2  2   ? 21.606  -17.810  31.620   1.00 73.95  ? 2   ARG   D N      1 
ATOM   10199 C  CA     . ARG   D 2  2   ? 22.337  -16.677  31.037   1.00 63.81  ? 2   ARG   D CA     1 
ATOM   10200 C  C      . ARG   D 2  2   ? 22.299  -15.560  32.069   1.00 67.69  ? 2   ARG   D C      1 
ATOM   10201 O  O      . ARG   D 2  2   ? 21.262  -14.920  32.250   1.00 70.39  ? 2   ARG   D O      1 
ATOM   10202 C  CB     . ARG   D 2  2   ? 21.725  -16.214  29.715   1.00 63.04  ? 2   ARG   D CB     1 
ATOM   10203 C  CG     . ARG   D 2  2   ? 21.925  -17.143  28.540   1.00 64.98  ? 2   ARG   D CG     1 
ATOM   10204 C  CD     . ARG   D 2  2   ? 23.262  -16.882  27.850   1.00 61.76  ? 2   ARG   D CD     1 
ATOM   10205 N  NE     . ARG   D 2  2   ? 23.309  -15.565  27.214   1.00 61.63  ? 2   ARG   D NE     1 
ATOM   10206 C  CZ     . ARG   D 2  2   ? 24.412  -15.024  26.703   1.00 65.18  ? 2   ARG   D CZ     1 
ATOM   10207 N  NH1    . ARG   D 2  2   ? 25.566  -15.673  26.725   1.00 65.96  ? 2   ARG   D NH1    1 
ATOM   10208 N  NH2    . ARG   D 2  2   ? 24.361  -13.801  26.166   1.00 49.32  ? 2   ARG   D NH2    1 
ATOM   10209 N  N      . GLU   D 2  3   ? 23.415  -15.313  32.746   1.00 68.58  ? 3   GLU   D N      1 
ATOM   10210 C  CA     . GLU   D 2  3   ? 23.410  -14.442  33.918   1.00 61.88  ? 3   GLU   D CA     1 
ATOM   10211 C  C      . GLU   D 2  3   ? 23.699  -13.006  33.514   1.00 56.11  ? 3   GLU   D C      1 
ATOM   10212 O  O      . GLU   D 2  3   ? 24.776  -12.706  32.999   1.00 58.29  ? 3   GLU   D O      1 
ATOM   10213 C  CB     . GLU   D 2  3   ? 24.436  -14.908  34.949   1.00 61.43  ? 3   GLU   D CB     1 
ATOM   10214 C  CG     . GLU   D 2  3   ? 24.133  -16.266  35.529   1.00 63.66  ? 3   GLU   D CG     1 
ATOM   10215 C  CD     . GLU   D 2  3   ? 24.773  -17.375  34.726   1.00 69.61  ? 3   GLU   D CD     1 
ATOM   10216 O  OE1    . GLU   D 2  3   ? 25.438  -17.054  33.718   1.00 69.64  ? 3   GLU   D OE1    1 
ATOM   10217 O  OE2    . GLU   D 2  3   ? 24.616  -18.560  35.095   1.00 71.94  ? 3   GLU   D OE2    1 
ATOM   10218 N  N      . ILE   D 2  4   ? 22.759  -12.132  33.745   1.00 58.06  ? 4   ILE   D N      1 
ATOM   10219 C  CA     . ILE   D 2  4   ? 23.082  -10.716  33.798   1.00 55.61  ? 4   ILE   D CA     1 
ATOM   10220 C  C      . ILE   D 2  4   ? 23.633  -10.426  35.181   1.00 57.88  ? 4   ILE   D C      1 
ATOM   10221 O  O      . ILE   D 2  4   ? 23.269  -11.071  36.173   1.00 56.67  ? 4   ILE   D O      1 
ATOM   10222 C  CB     . ILE   D 2  4   ? 21.860  -9.831   33.487   1.00 58.72  ? 4   ILE   D CB     1 
ATOM   10223 C  CG1    . ILE   D 2  4   ? 21.528  -9.903   32.003   1.00 56.37  ? 4   ILE   D CG1    1 
ATOM   10224 C  CG2    . ILE   D 2  4   ? 22.125  -8.391   33.884   1.00 56.60  ? 4   ILE   D CG2    1 
ATOM   10225 C  CD1    . ILE   D 2  4   ? 20.068  -10.146  31.744   1.00 57.34  ? 4   ILE   D CD1    1 
ATOM   10226 N  N      . VAL   D 2  5   ? 24.526  -9.447   35.236   1.00 63.34  ? 5   VAL   D N      1 
ATOM   10227 C  CA     . VAL   D 2  5   ? 25.090  -8.924   36.471   1.00 56.69  ? 5   VAL   D CA     1 
ATOM   10228 C  C      . VAL   D 2  5   ? 24.640  -7.470   36.624   1.00 60.07  ? 5   VAL   D C      1 
ATOM   10229 O  O      . VAL   D 2  5   ? 24.907  -6.629   35.753   1.00 55.36  ? 5   VAL   D O      1 
ATOM   10230 C  CB     . VAL   D 2  5   ? 26.619  -9.047   36.469   1.00 59.91  ? 5   VAL   D CB     1 
ATOM   10231 C  CG1    . VAL   D 2  5   ? 27.249  -7.965   37.328   1.00 62.70  ? 5   VAL   D CG1    1 
ATOM   10232 C  CG2    . VAL   D 2  5   ? 27.029  -10.439  36.949   1.00 63.02  ? 5   VAL   D CG2    1 
ATOM   10233 N  N      . HIS   D 2  6   ? 23.944  -7.183   37.721   1.00 62.31  ? 6   HIS   D N      1 
ATOM   10234 C  CA     . HIS   D 2  6   ? 23.389  -5.861   37.986   1.00 61.29  ? 6   HIS   D CA     1 
ATOM   10235 C  C      . HIS   D 2  6   ? 24.364  -5.019   38.808   1.00 63.36  ? 6   HIS   D C      1 
ATOM   10236 O  O      . HIS   D 2  6   ? 25.063  -5.530   39.686   1.00 62.34  ? 6   HIS   D O      1 
ATOM   10237 C  CB     . HIS   D 2  6   ? 22.059  -6.020   38.715   1.00 60.43  ? 6   HIS   D CB     1 
ATOM   10238 C  CG     . HIS   D 2  6   ? 21.338  -4.738   38.981   1.00 67.36  ? 6   HIS   D CG     1 
ATOM   10239 N  ND1    . HIS   D 2  6   ? 20.130  -4.703   39.641   1.00 73.02  ? 6   HIS   D ND1    1 
ATOM   10240 C  CD2    . HIS   D 2  6   ? 21.643  -3.451   38.693   1.00 69.73  ? 6   HIS   D CD2    1 
ATOM   10241 C  CE1    . HIS   D 2  6   ? 19.720  -3.450   39.747   1.00 70.37  ? 6   HIS   D CE1    1 
ATOM   10242 N  NE2    . HIS   D 2  6   ? 20.622  -2.668   39.182   1.00 67.82  ? 6   HIS   D NE2    1 
ATOM   10243 N  N      . ILE   D 2  7   ? 24.408  -3.717   38.511   1.00 61.22  ? 7   ILE   D N      1 
ATOM   10244 C  CA     . ILE   D 2  7   ? 25.295  -2.771   39.187   1.00 61.72  ? 7   ILE   D CA     1 
ATOM   10245 C  C      . ILE   D 2  7   ? 24.573  -1.448   39.413   1.00 62.12  ? 7   ILE   D C      1 
ATOM   10246 O  O      . ILE   D 2  7   ? 24.338  -0.706   38.455   1.00 65.25  ? 7   ILE   D O      1 
ATOM   10247 C  CB     . ILE   D 2  7   ? 26.574  -2.532   38.363   1.00 57.88  ? 7   ILE   D CB     1 
ATOM   10248 C  CG1    . ILE   D 2  7   ? 27.504  -3.729   38.395   1.00 54.67  ? 7   ILE   D CG1    1 
ATOM   10249 C  CG2    . ILE   D 2  7   ? 27.323  -1.310   38.848   1.00 53.75  ? 7   ILE   D CG2    1 
ATOM   10250 C  CD1    . ILE   D 2  7   ? 28.814  -3.422   37.727   1.00 52.98  ? 7   ILE   D CD1    1 
ATOM   10251 N  N      . GLN   D 2  8   ? 24.237  -1.125   40.666   1.00 67.49  ? 8   GLN   D N      1 
ATOM   10252 C  CA     . GLN   D 2  8   ? 23.690  0.182    41.031   1.00 64.20  ? 8   GLN   D CA     1 
ATOM   10253 C  C      . GLN   D 2  8   ? 24.790  1.063    41.590   1.00 62.57  ? 8   GLN   D C      1 
ATOM   10254 O  O      . GLN   D 2  8   ? 25.560  0.621    42.449   1.00 66.41  ? 8   GLN   D O      1 
ATOM   10255 C  CB     . GLN   D 2  8   ? 22.592  0.049    42.077   1.00 65.38  ? 8   GLN   D CB     1 
ATOM   10256 C  CG     . GLN   D 2  8   ? 21.985  -1.313   42.124   1.00 66.48  ? 8   GLN   D CG     1 
ATOM   10257 C  CD     . GLN   D 2  8   ? 21.071  -1.484   43.302   1.00 68.37  ? 8   GLN   D CD     1 
ATOM   10258 O  OE1    . GLN   D 2  8   ? 21.162  -0.751   44.299   1.00 71.75  ? 8   GLN   D OE1    1 
ATOM   10259 N  NE2    . GLN   D 2  8   ? 20.152  -2.441   43.191   1.00 64.02  ? 8   GLN   D NE2    1 
ATOM   10260 N  N      . ALA   D 2  9   ? 24.845  2.313    41.133   1.00 61.03  ? 9   ALA   D N      1 
ATOM   10261 C  CA     . ALA   D 2  9   ? 25.894  3.228    41.557   1.00 63.74  ? 9   ALA   D CA     1 
ATOM   10262 C  C      . ALA   D 2  9   ? 25.332  4.622    41.805   1.00 71.87  ? 9   ALA   D C      1 
ATOM   10263 O  O      . ALA   D 2  9   ? 24.587  5.164    40.978   1.00 67.71  ? 9   ALA   D O      1 
ATOM   10264 C  CB     . ALA   D 2  9   ? 27.015  3.300    40.526   1.00 56.94  ? 9   ALA   D CB     1 
ATOM   10265 N  N      . GLY   D 2  10  ? 25.705  5.197    42.956   1.00 71.89  ? 10  GLY   D N      1 
ATOM   10266 C  CA     . GLY   D 2  10  ? 25.395  6.577    43.266   1.00 75.87  ? 10  GLY   D CA     1 
ATOM   10267 C  C      . GLY   D 2  10  ? 24.059  6.739    43.958   1.00 78.49  ? 10  GLY   D C      1 
ATOM   10268 O  O      . GLY   D 2  10  ? 23.340  5.777    44.260   1.00 69.75  ? 10  GLY   D O      1 
ATOM   10269 N  N      . GLN   D 2  11  ? 23.702  7.996    44.212   1.00 77.08  ? 11  GLN   D N      1 
ATOM   10270 C  CA     . GLN   D 2  11  ? 22.411  8.225    44.848   1.00 84.81  ? 11  GLN   D CA     1 
ATOM   10271 C  C      . GLN   D 2  11  ? 21.274  7.756    43.941   1.00 78.41  ? 11  GLN   D C      1 
ATOM   10272 O  O      . GLN   D 2  11  ? 20.537  6.824    44.284   1.00 69.56  ? 11  GLN   D O      1 
ATOM   10273 C  CB     . GLN   D 2  11  ? 22.246  9.702    45.236   1.00 90.40  ? 11  GLN   D CB     1 
ATOM   10274 C  CG     . GLN   D 2  11  ? 21.058  9.924    46.170   1.00 83.79  ? 11  GLN   D CG     1 
ATOM   10275 C  CD     . GLN   D 2  11  ? 20.677  11.387   46.355   1.00 86.67  ? 11  GLN   D CD     1 
ATOM   10276 O  OE1    . GLN   D 2  11  ? 21.359  12.320   45.891   1.00 81.16  ? 11  GLN   D OE1    1 
ATOM   10277 N  NE2    . GLN   D 2  11  ? 19.540  11.589   47.003   1.00 79.37  ? 11  GLN   D NE2    1 
ATOM   10278 N  N      . CYS   D 2  12  ? 21.141  8.366    42.756   1.00 76.71  ? 12  CYS   D N      1 
ATOM   10279 C  CA     . CYS   D 2  12  ? 20.058  7.962    41.861   1.00 74.50  ? 12  CYS   D CA     1 
ATOM   10280 C  C      . CYS   D 2  12  ? 20.138  6.478    41.538   1.00 71.84  ? 12  CYS   D C      1 
ATOM   10281 O  O      . CYS   D 2  12  ? 19.123  5.770    41.557   1.00 65.29  ? 12  CYS   D O      1 
ATOM   10282 C  CB     . CYS   D 2  12  ? 20.072  8.763    40.562   1.00 75.78  ? 12  CYS   D CB     1 
ATOM   10283 S  SG     . CYS   D 2  12  ? 18.724  8.197    39.466   1.00 63.52  ? 12  CYS   D SG     1 
ATOM   10284 N  N      . GLY   D 2  13  ? 21.344  5.998    41.218   1.00 71.49  ? 13  GLY   D N      1 
ATOM   10285 C  CA     . GLY   D 2  13  ? 21.503  4.608    40.823   1.00 67.99  ? 13  GLY   D CA     1 
ATOM   10286 C  C      . GLY   D 2  13  ? 20.911  3.617    41.810   1.00 68.63  ? 13  GLY   D C      1 
ATOM   10287 O  O      . GLY   D 2  13  ? 20.151  2.720    41.433   1.00 64.36  ? 13  GLY   D O      1 
ATOM   10288 N  N      . ASN   D 2  14  ? 21.265  3.747    43.091   1.00 72.59  ? 14  ASN   D N      1 
ATOM   10289 C  CA     . ASN   D 2  14  ? 20.854  2.724    44.049   1.00 68.54  ? 14  ASN   D CA     1 
ATOM   10290 C  C      . ASN   D 2  14  ? 19.354  2.747    44.302   1.00 69.53  ? 14  ASN   D C      1 
ATOM   10291 O  O      . ASN   D 2  14  ? 18.745  1.693    44.539   1.00 64.83  ? 14  ASN   D O      1 
ATOM   10292 C  CB     . ASN   D 2  14  ? 21.620  2.895    45.354   1.00 67.37  ? 14  ASN   D CB     1 
ATOM   10293 C  CG     . ASN   D 2  14  ? 23.058  2.503    45.216   1.00 72.39  ? 14  ASN   D CG     1 
ATOM   10294 O  OD1    . ASN   D 2  14  ? 23.412  1.332    45.399   1.00 72.65  ? 14  ASN   D OD1    1 
ATOM   10295 N  ND2    . ASN   D 2  14  ? 23.908  3.474    44.860   1.00 73.12  ? 14  ASN   D ND2    1 
ATOM   10296 N  N      . GLN   D 2  15  ? 18.734  3.925    44.246   1.00 71.52  ? 15  GLN   D N      1 
ATOM   10297 C  CA     . GLN   D 2  15  ? 17.306  3.995    44.524   1.00 73.30  ? 15  GLN   D CA     1 
ATOM   10298 C  C      . GLN   D 2  15  ? 16.481  3.363    43.395   1.00 71.68  ? 15  GLN   D C      1 
ATOM   10299 O  O      . GLN   D 2  15  ? 15.674  2.453    43.644   1.00 65.53  ? 15  GLN   D O      1 
ATOM   10300 C  CB     . GLN   D 2  15  ? 16.913  5.447    44.805   1.00 73.03  ? 15  GLN   D CB     1 
ATOM   10301 C  CG     . GLN   D 2  15  ? 17.010  5.755    46.308   1.00 79.66  ? 15  GLN   D CG     1 
ATOM   10302 C  CD     . GLN   D 2  15  ? 16.457  7.107    46.694   1.00 82.79  ? 15  GLN   D CD     1 
ATOM   10303 O  OE1    . GLN   D 2  15  ? 17.149  8.132    46.590   1.00 81.86  ? 15  GLN   D OE1    1 
ATOM   10304 N  NE2    . GLN   D 2  15  ? 15.201  7.125    47.143   1.00 77.11  ? 15  GLN   D NE2    1 
ATOM   10305 N  N      . ILE   D 2  16  ? 16.698  3.788    42.140   1.00 63.66  ? 16  ILE   D N      1 
ATOM   10306 C  CA     . ILE   D 2  16  ? 15.957  3.158    41.044   1.00 65.92  ? 16  ILE   D CA     1 
ATOM   10307 C  C      . ILE   D 2  16  ? 16.319  1.680    40.942   1.00 63.16  ? 16  ILE   D C      1 
ATOM   10308 O  O      . ILE   D 2  16  ? 15.464  0.836    40.640   1.00 59.17  ? 16  ILE   D O      1 
ATOM   10309 C  CB     . ILE   D 2  16  ? 16.181  3.908    39.707   1.00 67.05  ? 16  ILE   D CB     1 
ATOM   10310 C  CG1    . ILE   D 2  16  ? 17.420  3.410    38.971   1.00 62.05  ? 16  ILE   D CG1    1 
ATOM   10311 C  CG2    . ILE   D 2  16  ? 16.296  5.425    39.917   1.00 64.20  ? 16  ILE   D CG2    1 
ATOM   10312 C  CD1    . ILE   D 2  16  ? 17.685  4.222    37.718   1.00 60.28  ? 16  ILE   D CD1    1 
ATOM   10313 N  N      . GLY   D 2  17  ? 17.571  1.333    41.240   1.00 64.60  ? 17  GLY   D N      1 
ATOM   10314 C  CA     . GLY   D 2  17  ? 17.930  -0.070   41.343   1.00 65.69  ? 17  GLY   D CA     1 
ATOM   10315 C  C      . GLY   D 2  17  ? 17.158  -0.820   42.416   1.00 67.30  ? 17  GLY   D C      1 
ATOM   10316 O  O      . GLY   D 2  17  ? 16.853  -2.007   42.255   1.00 71.21  ? 17  GLY   D O      1 
ATOM   10317 N  N      . ALA   D 2  18  ? 16.826  -0.151   43.521   1.00 67.23  ? 18  ALA   D N      1 
ATOM   10318 C  CA     . ALA   D 2  18  ? 16.161  -0.853   44.617   1.00 69.87  ? 18  ALA   D CA     1 
ATOM   10319 C  C      . ALA   D 2  18  ? 14.722  -1.220   44.258   1.00 73.63  ? 18  ALA   D C      1 
ATOM   10320 O  O      . ALA   D 2  18  ? 14.306  -2.379   44.414   1.00 64.47  ? 18  ALA   D O      1 
ATOM   10321 C  CB     . ALA   D 2  18  ? 16.207  -0.003   45.883   1.00 71.70  ? 18  ALA   D CB     1 
ATOM   10322 N  N      . LYS   D 2  19  ? 13.934  -0.245   43.785   1.00 72.79  ? 19  LYS   D N      1 
ATOM   10323 C  CA     . LYS   D 2  19  ? 12.544  -0.562   43.475   1.00 70.40  ? 19  LYS   D CA     1 
ATOM   10324 C  C      . LYS   D 2  19  ? 12.461  -1.533   42.311   1.00 73.21  ? 19  LYS   D C      1 
ATOM   10325 O  O      . LYS   D 2  19  ? 11.541  -2.361   42.261   1.00 70.71  ? 19  LYS   D O      1 
ATOM   10326 C  CB     . LYS   D 2  19  ? 11.741  0.709    43.195   1.00 71.40  ? 19  LYS   D CB     1 
ATOM   10327 C  CG     . LYS   D 2  19  ? 10.365  0.746    43.910   1.00 82.11  ? 19  LYS   D CG     1 
ATOM   10328 C  CD     . LYS   D 2  19  ? 10.515  0.924    45.435   1.00 81.05  ? 19  LYS   D CD     1 
ATOM   10329 C  CE     . LYS   D 2  19  ? 10.504  2.405    45.833   1.00 81.88  ? 19  LYS   D CE     1 
ATOM   10330 N  NZ     . LYS   D 2  19  ? 11.017  2.655    47.210   1.00 83.41  ? 19  LYS   D NZ     1 
ATOM   10331 N  N      . PHE   D 2  20  ? 13.425  -1.468   41.386   1.00 71.02  ? 20  PHE   D N      1 
ATOM   10332 C  CA     . PHE   D 2  20  ? 13.572  -2.519   40.389   1.00 67.79  ? 20  PHE   D CA     1 
ATOM   10333 C  C      . PHE   D 2  20  ? 13.431  -3.894   41.040   1.00 70.50  ? 20  PHE   D C      1 
ATOM   10334 O  O      . PHE   D 2  20  ? 12.471  -4.627   40.764   1.00 68.44  ? 20  PHE   D O      1 
ATOM   10335 C  CB     . PHE   D 2  20  ? 14.920  -2.373   39.666   1.00 68.49  ? 20  PHE   D CB     1 
ATOM   10336 C  CG     . PHE   D 2  20  ? 15.235  -3.506   38.709   1.00 69.68  ? 20  PHE   D CG     1 
ATOM   10337 C  CD1    . PHE   D 2  20  ? 14.422  -3.754   37.616   1.00 65.88  ? 20  PHE   D CD1    1 
ATOM   10338 C  CD2    . PHE   D 2  20  ? 16.349  -4.314   38.899   1.00 65.64  ? 20  PHE   D CD2    1 
ATOM   10339 C  CE1    . PHE   D 2  20  ? 14.704  -4.792   36.739   1.00 63.44  ? 20  PHE   D CE1    1 
ATOM   10340 C  CE2    . PHE   D 2  20  ? 16.634  -5.348   38.023   1.00 63.32  ? 20  PHE   D CE2    1 
ATOM   10341 C  CZ     . PHE   D 2  20  ? 15.811  -5.581   36.938   1.00 60.98  ? 20  PHE   D CZ     1 
ATOM   10342 N  N      . TRP   D 2  21  ? 14.362  -4.237   41.948   1.00 69.56  ? 21  TRP   D N      1 
ATOM   10343 C  CA     . TRP   D 2  21  ? 14.360  -5.576   42.548   1.00 71.93  ? 21  TRP   D CA     1 
ATOM   10344 C  C      . TRP   D 2  21  ? 13.083  -5.838   43.339   1.00 68.16  ? 21  TRP   D C      1 
ATOM   10345 O  O      . TRP   D 2  21  ? 12.574  -6.965   43.358   1.00 64.12  ? 21  TRP   D O      1 
ATOM   10346 C  CB     . TRP   D 2  21  ? 15.587  -5.770   43.442   1.00 64.63  ? 21  TRP   D CB     1 
ATOM   10347 C  CG     . TRP   D 2  21  ? 16.861  -5.876   42.691   1.00 63.94  ? 21  TRP   D CG     1 
ATOM   10348 C  CD1    . TRP   D 2  21  ? 17.798  -4.904   42.554   1.00 64.00  ? 21  TRP   D CD1    1 
ATOM   10349 C  CD2    . TRP   D 2  21  ? 17.351  -7.015   41.964   1.00 65.00  ? 21  TRP   D CD2    1 
ATOM   10350 N  NE1    . TRP   D 2  21  ? 18.842  -5.358   41.800   1.00 64.27  ? 21  TRP   D NE1    1 
ATOM   10351 C  CE2    . TRP   D 2  21  ? 18.595  -6.648   41.413   1.00 62.02  ? 21  TRP   D CE2    1 
ATOM   10352 C  CE3    . TRP   D 2  21  ? 16.858  -8.305   41.724   1.00 64.32  ? 21  TRP   D CE3    1 
ATOM   10353 C  CZ2    . TRP   D 2  21  ? 19.360  -7.516   40.632   1.00 58.07  ? 21  TRP   D CZ2    1 
ATOM   10354 C  CZ3    . TRP   D 2  21  ? 17.624  -9.175   40.946   1.00 66.54  ? 21  TRP   D CZ3    1 
ATOM   10355 C  CH2    . TRP   D 2  21  ? 18.863  -8.772   40.412   1.00 61.76  ? 21  TRP   D CH2    1 
ATOM   10356 N  N      . GLU   D 2  22  ? 12.558  -4.815   44.015   1.00 70.75  ? 22  GLU   D N      1 
ATOM   10357 C  CA     . GLU   D 2  22  ? 11.279  -4.986   44.692   1.00 76.10  ? 22  GLU   D CA     1 
ATOM   10358 C  C      . GLU   D 2  22  ? 10.205  -5.449   43.712   1.00 73.91  ? 22  GLU   D C      1 
ATOM   10359 O  O      . GLU   D 2  22  ? 9.433   -6.365   44.017   1.00 69.06  ? 22  GLU   D O      1 
ATOM   10360 C  CB     . GLU   D 2  22  ? 10.869  -3.682   45.386   1.00 77.37  ? 22  GLU   D CB     1 
ATOM   10361 C  CG     . GLU   D 2  22  ? 11.549  -3.461   46.746   1.00 84.97  ? 22  GLU   D CG     1 
ATOM   10362 C  CD     . GLU   D 2  22  ? 11.217  -2.111   47.373   1.00 94.91  ? 22  GLU   D CD     1 
ATOM   10363 O  OE1    . GLU   D 2  22  ? 10.030  -1.711   47.321   1.00 99.69  ? 22  GLU   D OE1    1 
ATOM   10364 O  OE2    . GLU   D 2  22  ? 12.139  -1.454   47.919   1.00 88.79  ? 22  GLU   D OE2    1 
ATOM   10365 N  N      . VAL   D 2  23  ? 10.168  -4.850   42.512   1.00 71.44  ? 23  VAL   D N      1 
ATOM   10366 C  CA     . VAL   D 2  23  ? 9.123   -5.166   41.541   1.00 67.94  ? 23  VAL   D CA     1 
ATOM   10367 C  C      . VAL   D 2  23  ? 9.345   -6.544   40.934   1.00 70.41  ? 23  VAL   D C      1 
ATOM   10368 O  O      . VAL   D 2  23  ? 8.425   -7.369   40.877   1.00 70.50  ? 23  VAL   D O      1 
ATOM   10369 C  CB     . VAL   D 2  23  ? 9.054   -4.093   40.440   1.00 68.69  ? 23  VAL   D CB     1 
ATOM   10370 C  CG1    . VAL   D 2  23  ? 7.875   -4.363   39.533   1.00 66.50  ? 23  VAL   D CG1    1 
ATOM   10371 C  CG2    . VAL   D 2  23  ? 8.955   -2.708   41.031   1.00 67.17  ? 23  VAL   D CG2    1 
ATOM   10372 N  N      . ILE   D 2  24  ? 10.553  -6.805   40.431   1.00 68.17  ? 24  ILE   D N      1 
ATOM   10373 C  CA     . ILE   D 2  24  ? 10.732  -8.060   39.714   1.00 71.32  ? 24  ILE   D CA     1 
ATOM   10374 C  C      . ILE   D 2  24  ? 10.719  -9.222   40.694   1.00 74.20  ? 24  ILE   D C      1 
ATOM   10375 O  O      . ILE   D 2  24  ? 10.378  -10.355  40.323   1.00 73.39  ? 24  ILE   D O      1 
ATOM   10376 C  CB     . ILE   D 2  24  ? 12.027  -8.056   38.879   1.00 71.59  ? 24  ILE   D CB     1 
ATOM   10377 C  CG1    . ILE   D 2  24  ? 13.164  -7.413   39.654   1.00 72.76  ? 24  ILE   D CG1    1 
ATOM   10378 C  CG2    . ILE   D 2  24  ? 11.851  -7.280   37.584   1.00 65.29  ? 24  ILE   D CG2    1 
ATOM   10379 C  CD1    . ILE   D 2  24  ? 14.440  -7.405   38.882   1.00 68.30  ? 24  ILE   D CD1    1 
ATOM   10380 N  N      . SER   D 2  25  ? 11.088  -8.968   41.954   1.00 74.09  ? 25  SER   D N      1 
ATOM   10381 C  CA     . SER   D 2  25  ? 10.980  -10.003  42.978   1.00 74.61  ? 25  SER   D CA     1 
ATOM   10382 C  C      . SER   D 2  25  ? 9.523   -10.376  43.212   1.00 72.93  ? 25  SER   D C      1 
ATOM   10383 O  O      . SER   D 2  25  ? 9.188   -11.559  43.349   1.00 72.03  ? 25  SER   D O      1 
ATOM   10384 C  CB     . SER   D 2  25  ? 11.626  -9.524   44.277   1.00 74.99  ? 25  SER   D CB     1 
ATOM   10385 O  OG     . SER   D 2  25  ? 12.809  -8.793   44.003   1.00 75.16  ? 25  SER   D OG     1 
ATOM   10386 N  N      . ASP   D 2  26  ? 8.642   -9.370   43.241   1.00 71.79  ? 26  ASP   D N      1 
ATOM   10387 C  CA     . ASP   D 2  26  ? 7.210   -9.607   43.392   1.00 74.56  ? 26  ASP   D CA     1 
ATOM   10388 C  C      . ASP   D 2  26  ? 6.634   -10.347  42.184   1.00 79.34  ? 26  ASP   D C      1 
ATOM   10389 O  O      . ASP   D 2  26  ? 5.866   -11.304  42.350   1.00 75.08  ? 26  ASP   D O      1 
ATOM   10390 C  CB     . ASP   D 2  26  ? 6.494   -8.272   43.613   1.00 72.28  ? 26  ASP   D CB     1 
ATOM   10391 C  CG     . ASP   D 2  26  ? 5.035   -8.298   43.177   1.00 77.65  ? 26  ASP   D CG     1 
ATOM   10392 O  OD1    . ASP   D 2  26  ? 4.308   -9.249   43.534   1.00 75.47  ? 26  ASP   D OD1    1 
ATOM   10393 O  OD2    . ASP   D 2  26  ? 4.627   -7.373   42.442   1.00 79.00  ? 26  ASP   D OD2    1 
ATOM   10394 N  N      . GLU   D 2  27  ? 6.992   -9.927   40.959   1.00 77.35  ? 27  GLU   D N      1 
ATOM   10395 C  CA     . GLU   D 2  27  ? 6.524   -10.633  39.765   1.00 72.99  ? 27  GLU   D CA     1 
ATOM   10396 C  C      . GLU   D 2  27  ? 6.961   -12.096  39.778   1.00 77.39  ? 27  GLU   D C      1 
ATOM   10397 O  O      . GLU   D 2  27  ? 6.195   -12.993  39.398   1.00 74.10  ? 27  GLU   D O      1 
ATOM   10398 C  CB     . GLU   D 2  27  ? 7.039   -9.939   38.502   1.00 72.29  ? 27  GLU   D CB     1 
ATOM   10399 C  CG     . GLU   D 2  27  ? 6.632   -8.475   38.348   1.00 77.42  ? 27  GLU   D CG     1 
ATOM   10400 C  CD     . GLU   D 2  27  ? 7.091   -7.862   37.023   1.00 75.53  ? 27  GLU   D CD     1 
ATOM   10401 O  OE1    . GLU   D 2  27  ? 7.218   -8.605   36.028   1.00 73.42  ? 27  GLU   D OE1    1 
ATOM   10402 O  OE2    . GLU   D 2  27  ? 7.320   -6.633   36.970   1.00 78.90  ? 27  GLU   D OE2    1 
ATOM   10403 N  N      . HIS   D 2  28  ? 8.189   -12.356  40.226   1.00 80.00  ? 28  HIS   D N      1 
ATOM   10404 C  CA     . HIS   D 2  28  ? 8.770   -13.692  40.194   1.00 83.41  ? 28  HIS   D CA     1 
ATOM   10405 C  C      . HIS   D 2  28  ? 8.421   -14.550  41.409   1.00 84.75  ? 28  HIS   D C      1 
ATOM   10406 O  O      . HIS   D 2  28  ? 8.698   -15.756  41.390   1.00 84.84  ? 28  HIS   D O      1 
ATOM   10407 C  CB     . HIS   D 2  28  ? 10.296  -13.589  40.048   1.00 81.41  ? 28  HIS   D CB     1 
ATOM   10408 C  CG     . HIS   D 2  28  ? 10.741  -13.231  38.663   1.00 75.54  ? 28  HIS   D CG     1 
ATOM   10409 N  ND1    . HIS   D 2  28  ? 10.808  -14.158  37.645   1.00 66.75  ? 28  HIS   D ND1    1 
ATOM   10410 C  CD2    . HIS   D 2  28  ? 11.146  -12.055  38.130   1.00 69.60  ? 28  HIS   D CD2    1 
ATOM   10411 C  CE1    . HIS   D 2  28  ? 11.223  -13.564  36.541   1.00 70.29  ? 28  HIS   D CE1    1 
ATOM   10412 N  NE2    . HIS   D 2  28  ? 11.434  -12.288  36.808   1.00 68.70  ? 28  HIS   D NE2    1 
ATOM   10413 N  N      . GLY   D 2  29  ? 7.825   -13.970  42.454   1.00 86.68  ? 29  GLY   D N      1 
ATOM   10414 C  CA     . GLY   D 2  29  ? 7.458   -14.722  43.644   1.00 91.37  ? 29  GLY   D CA     1 
ATOM   10415 C  C      . GLY   D 2  29  ? 8.587   -14.903  44.645   1.00 91.54  ? 29  GLY   D C      1 
ATOM   10416 O  O      . GLY   D 2  29  ? 8.902   -16.031  45.041   1.00 93.15  ? 29  GLY   D O      1 
ATOM   10417 N  N      . ILE   D 2  30  ? 9.197   -13.798  45.069   1.00 83.05  ? 30  ILE   D N      1 
ATOM   10418 C  CA     . ILE   D 2  30  ? 10.317  -13.815  46.001   1.00 81.11  ? 30  ILE   D CA     1 
ATOM   10419 C  C      . ILE   D 2  30  ? 10.057  -12.769  47.074   1.00 85.28  ? 30  ILE   D C      1 
ATOM   10420 O  O      . ILE   D 2  30  ? 9.865   -11.588  46.760   1.00 85.08  ? 30  ILE   D O      1 
ATOM   10421 C  CB     . ILE   D 2  30  ? 11.651  -13.539  45.292   1.00 81.87  ? 30  ILE   D CB     1 
ATOM   10422 C  CG1    . ILE   D 2  30  ? 12.115  -14.782  44.531   1.00 82.39  ? 30  ILE   D CG1    1 
ATOM   10423 C  CG2    . ILE   D 2  30  ? 12.693  -13.084  46.285   1.00 82.06  ? 30  ILE   D CG2    1 
ATOM   10424 C  CD1    . ILE   D 2  30  ? 13.432  -14.611  43.837   1.00 74.28  ? 30  ILE   D CD1    1 
ATOM   10425 N  N      . ASP   D 2  31  ? 10.051  -13.196  48.332   1.00 89.53  ? 31  ASP   D N      1 
ATOM   10426 C  CA     . ASP   D 2  31  ? 9.920   -12.282  49.462   1.00 89.71  ? 31  ASP   D CA     1 
ATOM   10427 C  C      . ASP   D 2  31  ? 11.287  -11.770  49.878   1.00 87.57  ? 31  ASP   D C      1 
ATOM   10428 O  O      . ASP   D 2  31  ? 12.321  -12.200  49.362   1.00 91.48  ? 31  ASP   D O      1 
ATOM   10429 C  CB     . ASP   D 2  31  ? 9.222   -12.983  50.622   1.00 84.06  ? 31  ASP   D CB     1 
ATOM   10430 C  CG     . ASP   D 2  31  ? 9.856   -14.309  50.959   1.00 89.95  ? 31  ASP   D CG     1 
ATOM   10431 O  OD1    . ASP   D 2  31  ? 11.019  -14.529  50.554   1.00 94.16  ? 31  ASP   D OD1    1 
ATOM   10432 O  OD2    . ASP   D 2  31  ? 9.196   -15.131  51.628   1.00 90.01  ? 31  ASP   D OD2    1 
ATOM   10433 N  N      . PRO   D 2  32  ? 11.336  -10.842  50.818   1.00 83.04  ? 32  PRO   D N      1 
ATOM   10434 C  CA     . PRO   D 2  32  ? 12.624  -10.223  51.161   1.00 88.64  ? 32  PRO   D CA     1 
ATOM   10435 C  C      . PRO   D 2  32  ? 13.617  -11.178  51.814   1.00 84.77  ? 32  PRO   D C      1 
ATOM   10436 O  O      . PRO   D 2  32  ? 14.760  -10.791  52.068   1.00 88.32  ? 32  PRO   D O      1 
ATOM   10437 C  CB     . PRO   D 2  32  ? 12.223  -9.079   52.103   1.00 93.65  ? 32  PRO   D CB     1 
ATOM   10438 C  CG     . PRO   D 2  32  ? 10.787  -8.788   51.749   1.00 93.72  ? 32  PRO   D CG     1 
ATOM   10439 C  CD     . PRO   D 2  32  ? 10.200  -10.131  51.424   1.00 85.80  ? 32  PRO   D CD     1 
ATOM   10440 N  N      . THR   D 2  33  ? 13.220  -12.418  52.081   1.00 82.10  ? 33  THR   D N      1 
ATOM   10441 C  CA     . THR   D 2  33  ? 14.174  -13.399  52.580   1.00 88.25  ? 33  THR   D CA     1 
ATOM   10442 C  C      . THR   D 2  33  ? 14.880  -14.157  51.468   1.00 95.24  ? 33  THR   D C      1 
ATOM   10443 O  O      . THR   D 2  33  ? 15.956  -14.721  51.707   1.00 97.16  ? 33  THR   D O      1 
ATOM   10444 C  CB     . THR   D 2  33  ? 13.492  -14.413  53.511   1.00 94.15  ? 33  THR   D CB     1 
ATOM   10445 O  OG1    . THR   D 2  33  ? 14.369  -15.530  53.742   1.00 94.43  ? 33  THR   D OG1    1 
ATOM   10446 C  CG2    . THR   D 2  33  ? 12.195  -14.911  52.912   1.00 87.24  ? 33  THR   D CG2    1 
ATOM   10447 N  N      . GLY   D 2  34  ? 14.310  -14.184  50.270   1.00 90.43  ? 34  GLY   D N      1 
ATOM   10448 C  CA     . GLY   D 2  34  ? 14.878  -14.934  49.178   1.00 88.22  ? 34  GLY   D CA     1 
ATOM   10449 C  C      . GLY   D 2  34  ? 14.263  -16.293  48.956   1.00 92.34  ? 34  GLY   D C      1 
ATOM   10450 O  O      . GLY   D 2  34  ? 14.903  -17.147  48.332   1.00 94.58  ? 34  GLY   D O      1 
ATOM   10451 N  N      . SER   D 2  35  ? 13.057  -16.527  49.452   1.00 93.56  ? 35  SER   D N      1 
ATOM   10452 C  CA     . SER   D 2  35  ? 12.354  -17.776  49.210   1.00 96.27  ? 35  SER   D CA     1 
ATOM   10453 C  C      . SER   D 2  35  ? 11.242  -17.558  48.194   1.00 91.49  ? 35  SER   D C      1 
ATOM   10454 O  O      . SER   D 2  35  ? 10.755  -16.442  47.995   1.00 89.07  ? 35  SER   D O      1 
ATOM   10455 C  CB     . SER   D 2  35  ? 11.791  -18.341  50.516   1.00 93.76  ? 35  SER   D CB     1 
ATOM   10456 O  OG     . SER   D 2  35  ? 11.632  -17.315  51.475   1.00 91.01  ? 35  SER   D OG     1 
ATOM   10457 N  N      . TYR   D 2  36  ? 10.853  -18.639  47.537   1.00 90.13  ? 36  TYR   D N      1 
ATOM   10458 C  CA     . TYR   D 2  36  ? 9.872   -18.571  46.463   1.00 95.62  ? 36  TYR   D CA     1 
ATOM   10459 C  C      . TYR   D 2  36  ? 8.515   -19.005  46.997   1.00 96.98  ? 36  TYR   D C      1 
ATOM   10460 O  O      . TYR   D 2  36  ? 8.307   -20.179  47.319   1.00 92.92  ? 36  TYR   D O      1 
ATOM   10461 C  CB     . TYR   D 2  36  ? 10.287  -19.432  45.276   1.00 94.50  ? 36  TYR   D CB     1 
ATOM   10462 C  CG     . TYR   D 2  36  ? 9.209   -19.560  44.225   1.00 95.97  ? 36  TYR   D CG     1 
ATOM   10463 C  CD1    . TYR   D 2  36  ? 8.867   -18.481  43.411   1.00 96.02  ? 36  TYR   D CD1    1 
ATOM   10464 C  CD2    . TYR   D 2  36  ? 8.534   -20.758  44.043   1.00 92.91  ? 36  TYR   D CD2    1 
ATOM   10465 C  CE1    . TYR   D 2  36  ? 7.882   -18.597  42.446   1.00 91.92  ? 36  TYR   D CE1    1 
ATOM   10466 C  CE2    . TYR   D 2  36  ? 7.551   -20.887  43.080   1.00 94.42  ? 36  TYR   D CE2    1 
ATOM   10467 C  CZ     . TYR   D 2  36  ? 7.226   -19.807  42.283   1.00 95.08  ? 36  TYR   D CZ     1 
ATOM   10468 O  OH     . TYR   D 2  36  ? 6.241   -19.951  41.327   1.00 92.81  ? 36  TYR   D OH     1 
ATOM   10469 N  N      . HIS   D 2  37  ? 7.599   -18.050  47.092   1.00 99.38  ? 37  HIS   D N      1 
ATOM   10470 C  CA     . HIS   D 2  37  ? 6.203   -18.301  47.431   1.00 104.15 ? 37  HIS   D CA     1 
ATOM   10471 C  C      . HIS   D 2  37  ? 5.399   -17.815  46.236   1.00 103.26 ? 37  HIS   D C      1 
ATOM   10472 O  O      . HIS   D 2  37  ? 4.907   -16.686  46.215   1.00 108.06 ? 37  HIS   D O      1 
ATOM   10473 C  CB     . HIS   D 2  37  ? 5.780   -17.588  48.753   1.00 108.51 ? 37  HIS   D CB     1 
ATOM   10474 C  CG     . HIS   D 2  37  ? 6.255   -18.280  49.996   1.00 109.25 ? 37  HIS   D CG     1 
ATOM   10475 N  ND1    . HIS   D 2  37  ? 7.476   -18.013  50.581   1.00 103.80 ? 37  HIS   D ND1    1 
ATOM   10476 C  CD2    . HIS   D 2  37  ? 5.674   -19.238  50.759   1.00 103.52 ? 37  HIS   D CD2    1 
ATOM   10477 C  CE1    . HIS   D 2  37  ? 7.624   -18.775  51.651   1.00 107.76 ? 37  HIS   D CE1    1 
ATOM   10478 N  NE2    . HIS   D 2  37  ? 6.545   -19.527  51.781   1.00 108.26 ? 37  HIS   D NE2    1 
ATOM   10479 N  N      . GLY   D 2  38  ? 5.291   -18.672  45.222   1.00 99.93  ? 38  GLY   D N      1 
ATOM   10480 C  CA     . GLY   D 2  38  ? 4.657   -18.294  43.983   1.00 102.81 ? 38  GLY   D CA     1 
ATOM   10481 C  C      . GLY   D 2  38  ? 3.690   -19.355  43.496   1.00 104.44 ? 38  GLY   D C      1 
ATOM   10482 O  O      . GLY   D 2  38  ? 3.754   -20.526  43.877   1.00 100.86 ? 38  GLY   D O      1 
ATOM   10483 N  N      . ASP   D 2  39  ? 2.788   -18.913  42.621   1.00 111.95 ? 39  ASP   D N      1 
ATOM   10484 C  CA     . ASP   D 2  39  ? 1.750   -19.771  42.061   1.00 109.70 ? 39  ASP   D CA     1 
ATOM   10485 C  C      . ASP   D 2  39  ? 2.260   -20.563  40.856   1.00 106.97 ? 39  ASP   D C      1 
ATOM   10486 O  O      . ASP   D 2  39  ? 2.225   -21.797  40.855   1.00 110.13 ? 39  ASP   D O      1 
ATOM   10487 C  CB     . ASP   D 2  39  ? 0.524   -18.925  41.684   1.00 111.75 ? 39  ASP   D CB     1 
ATOM   10488 C  CG     . ASP   D 2  39  ? 0.898   -17.574  41.080   1.00 118.77 ? 39  ASP   D CG     1 
ATOM   10489 O  OD1    . ASP   D 2  39  ? 1.523   -16.746  41.781   1.00 122.08 ? 39  ASP   D OD1    1 
ATOM   10490 O  OD2    . ASP   D 2  39  ? 0.548   -17.332  39.905   1.00 121.16 ? 39  ASP   D OD2    1 
ATOM   10491 N  N      . SER   D 2  40  ? 2.748   -19.865  39.833   1.00 102.05 ? 40  SER   D N      1 
ATOM   10492 C  CA     . SER   D 2  40  ? 3.124   -20.467  38.562   1.00 101.47 ? 40  SER   D CA     1 
ATOM   10493 C  C      . SER   D 2  40  ? 4.633   -20.686  38.495   1.00 92.80  ? 40  SER   D C      1 
ATOM   10494 O  O      . SER   D 2  40  ? 5.415   -19.922  39.060   1.00 93.67  ? 40  SER   D O      1 
ATOM   10495 C  CB     . SER   D 2  40  ? 2.664   -19.578  37.397   1.00 101.56 ? 40  SER   D CB     1 
ATOM   10496 O  OG     . SER   D 2  40  ? 2.914   -20.169  36.133   1.00 96.82  ? 40  SER   D OG     1 
ATOM   10497 N  N      . ASP   D 2  41  ? 5.039   -21.749  37.806   1.00 90.25  ? 41  ASP   D N      1 
ATOM   10498 C  CA     . ASP   D 2  41  ? 6.463   -21.991  37.607   1.00 95.25  ? 41  ASP   D CA     1 
ATOM   10499 C  C      . ASP   D 2  41  ? 7.021   -21.230  36.418   1.00 93.00  ? 41  ASP   D C      1 
ATOM   10500 O  O      . ASP   D 2  41  ? 8.216   -21.341  36.127   1.00 92.08  ? 41  ASP   D O      1 
ATOM   10501 C  CB     . ASP   D 2  41  ? 6.746   -23.484  37.430   1.00 99.70  ? 41  ASP   D CB     1 
ATOM   10502 C  CG     . ASP   D 2  41  ? 5.782   -24.149  36.469   1.00 105.54 ? 41  ASP   D CG     1 
ATOM   10503 O  OD1    . ASP   D 2  41  ? 5.745   -25.401  36.442   1.00 102.72 ? 41  ASP   D OD1    1 
ATOM   10504 O  OD2    . ASP   D 2  41  ? 5.055   -23.419  35.756   1.00 100.50 ? 41  ASP   D OD2    1 
ATOM   10505 N  N      . LEU   D 2  42  ? 6.185   -20.479  35.709   1.00 92.91  ? 42  LEU   D N      1 
ATOM   10506 C  CA     . LEU   D 2  42  ? 6.712   -19.559  34.718   1.00 82.87  ? 42  LEU   D CA     1 
ATOM   10507 C  C      . LEU   D 2  42  ? 7.523   -18.444  35.361   1.00 81.20  ? 42  LEU   D C      1 
ATOM   10508 O  O      . LEU   D 2  42  ? 8.251   -17.741  34.654   1.00 83.86  ? 42  LEU   D O      1 
ATOM   10509 C  CB     . LEU   D 2  42  ? 5.569   -18.970  33.897   1.00 80.63  ? 42  LEU   D CB     1 
ATOM   10510 C  CG     . LEU   D 2  42  ? 5.377   -19.514  32.482   1.00 76.23  ? 42  LEU   D CG     1 
ATOM   10511 C  CD1    . LEU   D 2  42  ? 5.429   -21.017  32.436   1.00 75.17  ? 42  LEU   D CD1    1 
ATOM   10512 C  CD2    . LEU   D 2  42  ? 4.059   -19.026  31.941   1.00 77.12  ? 42  LEU   D CD2    1 
ATOM   10513 N  N      . GLN   D 2  43  ? 7.409   -18.254  36.681   1.00 78.34  ? 43  GLN   D N      1 
ATOM   10514 C  CA     . GLN   D 2  43  ? 8.191   -17.218  37.346   1.00 81.33  ? 43  GLN   D CA     1 
ATOM   10515 C  C      . GLN   D 2  43  ? 9.586   -17.686  37.728   1.00 79.74  ? 43  GLN   D C      1 
ATOM   10516 O  O      . GLN   D 2  43  ? 10.412  -16.858  38.128   1.00 73.58  ? 43  GLN   D O      1 
ATOM   10517 C  CB     . GLN   D 2  43  ? 7.479   -16.703  38.601   1.00 83.87  ? 43  GLN   D CB     1 
ATOM   10518 C  CG     . GLN   D 2  43  ? 5.974   -16.684  38.522   1.00 90.10  ? 43  GLN   D CG     1 
ATOM   10519 C  CD     . GLN   D 2  43  ? 5.318   -16.903  39.871   1.00 93.32  ? 43  GLN   D CD     1 
ATOM   10520 O  OE1    . GLN   D 2  43  ? 5.423   -17.976  40.463   1.00 96.48  ? 43  GLN   D OE1    1 
ATOM   10521 N  NE2    . GLN   D 2  43  ? 4.639   -15.882  40.364   1.00 92.25  ? 43  GLN   D NE2    1 
ATOM   10522 N  N      . LEU   D 2  44  ? 9.869   -18.982  37.604   1.00 81.60  ? 44  LEU   D N      1 
ATOM   10523 C  CA     . LEU   D 2  44  ? 11.173  -19.531  37.934   1.00 75.88  ? 44  LEU   D CA     1 
ATOM   10524 C  C      . LEU   D 2  44  ? 11.987  -19.936  36.718   1.00 77.29  ? 44  LEU   D C      1 
ATOM   10525 O  O      . LEU   D 2  44  ? 13.216  -19.949  36.806   1.00 83.61  ? 44  LEU   D O      1 
ATOM   10526 C  CB     . LEU   D 2  44  ? 11.023  -20.762  38.844   1.00 79.68  ? 44  LEU   D CB     1 
ATOM   10527 C  CG     . LEU   D 2  44  ? 10.452  -20.587  40.255   1.00 85.89  ? 44  LEU   D CG     1 
ATOM   10528 C  CD1    . LEU   D 2  44  ? 10.507  -21.909  41.012   1.00 82.30  ? 44  LEU   D CD1    1 
ATOM   10529 C  CD2    . LEU   D 2  44  ? 11.178  -19.483  41.026   1.00 83.51  ? 44  LEU   D CD2    1 
ATOM   10530 N  N      . GLU   D 2  45  ? 11.338  -20.236  35.589   1.00 80.93  ? 45  GLU   D N      1 
ATOM   10531 C  CA     . GLU   D 2  45  ? 12.015  -20.891  34.468   1.00 78.44  ? 45  GLU   D CA     1 
ATOM   10532 C  C      . GLU   D 2  45  ? 13.331  -20.214  34.097   1.00 70.97  ? 45  GLU   D C      1 
ATOM   10533 O  O      . GLU   D 2  45  ? 14.318  -20.888  33.793   1.00 73.30  ? 45  GLU   D O      1 
ATOM   10534 C  CB     . GLU   D 2  45  ? 11.089  -20.930  33.258   1.00 73.24  ? 45  GLU   D CB     1 
ATOM   10535 C  CG     . GLU   D 2  45  ? 11.076  -22.265  32.586   1.00 77.01  ? 45  GLU   D CG     1 
ATOM   10536 C  CD     . GLU   D 2  45  ? 10.398  -22.219  31.242   1.00 83.19  ? 45  GLU   D CD     1 
ATOM   10537 O  OE1    . GLU   D 2  45  ? 10.799  -21.376  30.407   1.00 79.88  ? 45  GLU   D OE1    1 
ATOM   10538 O  OE2    . GLU   D 2  45  ? 9.458   -23.018  31.030   1.00 78.45  ? 45  GLU   D OE2    1 
ATOM   10539 N  N      . ARG   D 2  46  ? 13.359  -18.886  34.100   1.00 71.79  ? 46  ARG   D N      1 
ATOM   10540 C  CA     . ARG   D 2  46  ? 14.550  -18.119  33.768   1.00 68.89  ? 46  ARG   D CA     1 
ATOM   10541 C  C      . ARG   D 2  46  ? 14.974  -17.234  34.935   1.00 70.42  ? 46  ARG   D C      1 
ATOM   10542 O  O      . ARG   D 2  46  ? 15.521  -16.147  34.731   1.00 68.29  ? 46  ARG   D O      1 
ATOM   10543 C  CB     . ARG   D 2  46  ? 14.315  -17.262  32.523   1.00 71.32  ? 46  ARG   D CB     1 
ATOM   10544 C  CG     . ARG   D 2  46  ? 13.650  -17.966  31.354   1.00 70.37  ? 46  ARG   D CG     1 
ATOM   10545 C  CD     . ARG   D 2  46  ? 14.680  -18.443  30.330   1.00 77.97  ? 46  ARG   D CD     1 
ATOM   10546 N  NE     . ARG   D 2  46  ? 15.350  -17.337  29.648   1.00 79.89  ? 46  ARG   D NE     1 
ATOM   10547 C  CZ     . ARG   D 2  46  ? 14.728  -16.306  29.084   1.00 73.78  ? 46  ARG   D CZ     1 
ATOM   10548 N  NH1    . ARG   D 2  46  ? 13.409  -16.213  29.072   1.00 72.13  ? 46  ARG   D NH1    1 
ATOM   10549 N  NH2    . ARG   D 2  46  ? 15.450  -15.348  28.510   1.00 71.01  ? 46  ARG   D NH2    1 
ATOM   10550 N  N      . ILE   D 2  47  ? 14.709  -17.676  36.167   1.00 72.58  ? 47  ILE   D N      1 
ATOM   10551 C  CA     . ILE   D 2  47  ? 14.994  -16.835  37.325   1.00 73.85  ? 47  ILE   D CA     1 
ATOM   10552 C  C      . ILE   D 2  47  ? 16.494  -16.620  37.482   1.00 71.10  ? 47  ILE   D C      1 
ATOM   10553 O  O      . ILE   D 2  47  ? 16.937  -15.554  37.938   1.00 66.41  ? 47  ILE   D O      1 
ATOM   10554 C  CB     . ILE   D 2  47  ? 14.364  -17.448  38.591   1.00 74.14  ? 47  ILE   D CB     1 
ATOM   10555 C  CG1    . ILE   D 2  47  ? 14.367  -16.425  39.737   1.00 74.14  ? 47  ILE   D CG1    1 
ATOM   10556 C  CG2    . ILE   D 2  47  ? 15.085  -18.726  38.977   1.00 68.99  ? 47  ILE   D CG2    1 
ATOM   10557 C  CD1    . ILE   D 2  47  ? 13.393  -15.281  39.541   1.00 65.94  ? 47  ILE   D CD1    1 
ATOM   10558 N  N      . ASN   D 2  48  ? 17.298  -17.613  37.094   1.00 69.52  ? 48  ASN   D N      1 
ATOM   10559 C  CA     . ASN   D 2  48  ? 18.754  -17.534  37.194   1.00 69.75  ? 48  ASN   D CA     1 
ATOM   10560 C  C      . ASN   D 2  48  ? 19.350  -16.340  36.461   1.00 64.64  ? 48  ASN   D C      1 
ATOM   10561 O  O      . ASN   D 2  48  ? 20.516  -16.009  36.707   1.00 63.55  ? 48  ASN   D O      1 
ATOM   10562 C  CB     . ASN   D 2  48  ? 19.349  -18.823  36.655   1.00 68.91  ? 48  ASN   D CB     1 
ATOM   10563 C  CG     . ASN   D 2  48  ? 18.528  -19.381  35.521   1.00 81.43  ? 48  ASN   D CG     1 
ATOM   10564 O  OD1    . ASN   D 2  48  ? 17.389  -19.812  35.738   1.00 80.57  ? 48  ASN   D OD1    1 
ATOM   10565 N  ND2    . ASN   D 2  48  ? 19.078  -19.357  34.297   1.00 79.31  ? 48  ASN   D ND2    1 
ATOM   10566 N  N      . VAL   D 2  49  ? 18.585  -15.691  35.578   1.00 66.04  ? 49  VAL   D N      1 
ATOM   10567 C  CA     . VAL   D 2  49  ? 19.085  -14.543  34.823   1.00 61.64  ? 49  VAL   D CA     1 
ATOM   10568 C  C      . VAL   D 2  49  ? 19.404  -13.375  35.748   1.00 63.68  ? 49  VAL   D C      1 
ATOM   10569 O  O      . VAL   D 2  49  ? 20.374  -12.638  35.529   1.00 62.70  ? 49  VAL   D O      1 
ATOM   10570 C  CB     . VAL   D 2  49  ? 18.063  -14.144  33.745   1.00 59.11  ? 49  VAL   D CB     1 
ATOM   10571 C  CG1    . VAL   D 2  49  ? 18.575  -12.962  32.947   1.00 60.70  ? 49  VAL   D CG1    1 
ATOM   10572 C  CG2    . VAL   D 2  49  ? 17.774  -15.325  32.827   1.00 60.83  ? 49  VAL   D CG2    1 
ATOM   10573 N  N      . TYR   D 2  50  ? 18.593  -13.176  36.785   1.00 60.74  ? 50  TYR   D N      1 
ATOM   10574 C  CA     . TYR   D 2  50  ? 18.833  -12.108  37.734   1.00 63.04  ? 50  TYR   D CA     1 
ATOM   10575 C  C      . TYR   D 2  50  ? 19.121  -12.605  39.141   1.00 64.90  ? 50  TYR   D C      1 
ATOM   10576 O  O      . TYR   D 2  50  ? 19.358  -11.783  40.031   1.00 64.74  ? 50  TYR   D O      1 
ATOM   10577 C  CB     . TYR   D 2  50  ? 17.635  -11.153  37.757   1.00 61.80  ? 50  TYR   D CB     1 
ATOM   10578 C  CG     . TYR   D 2  50  ? 17.658  -10.139  36.637   1.00 60.73  ? 50  TYR   D CG     1 
ATOM   10579 C  CD1    . TYR   D 2  50  ? 18.560  -9.088   36.662   1.00 62.66  ? 50  TYR   D CD1    1 
ATOM   10580 C  CD2    . TYR   D 2  50  ? 16.795  -10.242  35.547   1.00 51.83  ? 50  TYR   D CD2    1 
ATOM   10581 C  CE1    . TYR   D 2  50  ? 18.599  -8.157   35.643   1.00 66.56  ? 50  TYR   D CE1    1 
ATOM   10582 C  CE2    . TYR   D 2  50  ? 16.827  -9.323   34.525   1.00 52.43  ? 50  TYR   D CE2    1 
ATOM   10583 C  CZ     . TYR   D 2  50  ? 17.733  -8.274   34.572   1.00 60.29  ? 50  TYR   D CZ     1 
ATOM   10584 O  OH     . TYR   D 2  50  ? 17.789  -7.323   33.567   1.00 51.73  ? 50  TYR   D OH     1 
ATOM   10585 N  N      . TYR   D 2  51  ? 19.135  -13.914  39.372   1.00 61.31  ? 51  TYR   D N      1 
ATOM   10586 C  CA     . TYR   D 2  51  ? 19.145  -14.420  40.735   1.00 67.28  ? 51  TYR   D CA     1 
ATOM   10587 C  C      . TYR   D 2  51  ? 20.150  -15.546  40.921   1.00 67.60  ? 51  TYR   D C      1 
ATOM   10588 O  O      . TYR   D 2  51  ? 20.195  -16.483  40.118   1.00 64.37  ? 51  TYR   D O      1 
ATOM   10589 C  CB     . TYR   D 2  51  ? 17.754  -14.915  41.126   1.00 69.70  ? 51  TYR   D CB     1 
ATOM   10590 C  CG     . TYR   D 2  51  ? 16.776  -13.799  41.372   1.00 71.99  ? 51  TYR   D CG     1 
ATOM   10591 C  CD1    . TYR   D 2  51  ? 16.877  -13.004  42.501   1.00 72.25  ? 51  TYR   D CD1    1 
ATOM   10592 C  CD2    . TYR   D 2  51  ? 15.747  -13.537  40.473   1.00 72.60  ? 51  TYR   D CD2    1 
ATOM   10593 C  CE1    . TYR   D 2  51  ? 15.977  -11.982  42.730   1.00 75.49  ? 51  TYR   D CE1    1 
ATOM   10594 C  CE2    . TYR   D 2  51  ? 14.845  -12.517  40.694   1.00 69.00  ? 51  TYR   D CE2    1 
ATOM   10595 C  CZ     . TYR   D 2  51  ? 14.965  -11.744  41.824   1.00 72.92  ? 51  TYR   D CZ     1 
ATOM   10596 O  OH     . TYR   D 2  51  ? 14.079  -10.724  42.061   1.00 72.00  ? 51  TYR   D OH     1 
ATOM   10597 N  N      . ASN   D 2  52  ? 20.929  -15.460  42.002   1.00 67.77  ? 52  ASN   D N      1 
ATOM   10598 C  CA     . ASN   D 2  52  ? 21.764  -16.568  42.456   1.00 70.11  ? 52  ASN   D CA     1 
ATOM   10599 C  C      . ASN   D 2  52  ? 20.934  -17.536  43.290   1.00 74.38  ? 52  ASN   D C      1 
ATOM   10600 O  O      . ASN   D 2  52  ? 20.201  -17.121  44.193   1.00 79.31  ? 52  ASN   D O      1 
ATOM   10601 C  CB     . ASN   D 2  52  ? 22.934  -16.051  43.290   1.00 67.94  ? 52  ASN   D CB     1 
ATOM   10602 C  CG     . ASN   D 2  52  ? 24.042  -15.489  42.446   1.00 67.61  ? 52  ASN   D CG     1 
ATOM   10603 O  OD1    . ASN   D 2  52  ? 24.392  -16.069  41.420   1.00 66.86  ? 52  ASN   D OD1    1 
ATOM   10604 N  ND2    . ASN   D 2  52  ? 24.597  -14.344  42.860   1.00 63.35  ? 52  ASN   D ND2    1 
ATOM   10605 N  N      . GLU   D 2  53  ? 21.045  -18.825  42.992   1.00 78.29  ? 53  GLU   D N      1 
ATOM   10606 C  CA     . GLU   D 2  53  ? 20.338  -19.846  43.753   1.00 83.86  ? 53  GLU   D CA     1 
ATOM   10607 C  C      . GLU   D 2  53  ? 21.217  -20.255  44.925   1.00 90.91  ? 53  GLU   D C      1 
ATOM   10608 O  O      . GLU   D 2  53  ? 22.306  -20.801  44.731   1.00 95.64  ? 53  GLU   D O      1 
ATOM   10609 C  CB     . GLU   D 2  53  ? 19.993  -21.047  42.877   1.00 87.33  ? 53  GLU   D CB     1 
ATOM   10610 C  CG     . GLU   D 2  53  ? 18.553  -21.522  43.026   1.00 90.28  ? 53  GLU   D CG     1 
ATOM   10611 C  CD     . GLU   D 2  53  ? 18.383  -23.004  42.718   1.00 98.88  ? 53  GLU   D CD     1 
ATOM   10612 O  OE1    . GLU   D 2  53  ? 19.129  -23.528  41.854   1.00 96.49  ? 53  GLU   D OE1    1 
ATOM   10613 O  OE2    . GLU   D 2  53  ? 17.486  -23.637  43.324   1.00 96.76  ? 53  GLU   D OE2    1 
ATOM   10614 N  N      . ALA   D 2  54  ? 20.757  -19.975  46.139   1.00 95.93  ? 54  ALA   D N      1 
ATOM   10615 C  CA     . ALA   D 2  54  ? 21.401  -20.467  47.347   1.00 96.27  ? 54  ALA   D CA     1 
ATOM   10616 C  C      . ALA   D 2  54  ? 20.621  -21.662  47.876   1.00 102.83 ? 54  ALA   D C      1 
ATOM   10617 O  O      . ALA   D 2  54  ? 19.383  -21.660  47.876   1.00 102.37 ? 54  ALA   D O      1 
ATOM   10618 C  CB     . ALA   D 2  54  ? 21.476  -19.372  48.412   1.00 92.44  ? 54  ALA   D CB     1 
ATOM   10619 N  N      . THR   D 2  55  ? 21.344  -22.692  48.306   1.00 107.16 ? 55  THR   D N      1 
ATOM   10620 C  CA     . THR   D 2  55  ? 20.682  -23.775  49.013   1.00 111.26 ? 55  THR   D CA     1 
ATOM   10621 C  C      . THR   D 2  55  ? 19.980  -23.218  50.258   1.00 106.75 ? 55  THR   D C      1 
ATOM   10622 O  O      . THR   D 2  55  ? 20.214  -22.081  50.692   1.00 99.12  ? 55  THR   D O      1 
ATOM   10623 C  CB     . THR   D 2  55  ? 21.674  -24.883  49.365   1.00 110.39 ? 55  THR   D CB     1 
ATOM   10624 O  OG1    . THR   D 2  55  ? 22.862  -24.311  49.926   1.00 116.58 ? 55  THR   D OG1    1 
ATOM   10625 C  CG2    . THR   D 2  55  ? 22.031  -25.680  48.121   1.00 104.23 ? 55  THR   D CG2    1 
ATOM   10626 N  N      . GLY   D 2  56  ? 19.118  -24.042  50.845   1.00 104.56 ? 56  GLY   D N      1 
ATOM   10627 C  CA     . GLY   D 2  56  ? 18.001  -23.457  51.548   1.00 101.60 ? 56  GLY   D CA     1 
ATOM   10628 C  C      . GLY   D 2  56  ? 17.062  -22.768  50.598   1.00 106.68 ? 56  GLY   D C      1 
ATOM   10629 O  O      . GLY   D 2  56  ? 16.337  -21.857  51.006   1.00 110.74 ? 56  GLY   D O      1 
ATOM   10630 N  N      . ASN   D 2  57  ? 17.092  -23.174  49.324   1.00 102.25 ? 57  ASN   D N      1 
ATOM   10631 C  CA     . ASN   D 2  57  ? 16.347  -22.577  48.219   1.00 101.72 ? 57  ASN   D CA     1 
ATOM   10632 C  C      . ASN   D 2  57  ? 16.133  -21.079  48.389   1.00 100.88 ? 57  ASN   D C      1 
ATOM   10633 O  O      . ASN   D 2  57  ? 15.002  -20.587  48.316   1.00 101.37 ? 57  ASN   D O      1 
ATOM   10634 C  CB     . ASN   D 2  57  ? 15.005  -23.282  48.027   1.00 101.51 ? 57  ASN   D CB     1 
ATOM   10635 C  CG     . ASN   D 2  57  ? 15.043  -24.310  46.905   1.00 105.82 ? 57  ASN   D CG     1 
ATOM   10636 O  OD1    . ASN   D 2  57  ? 14.827  -25.501  47.129   1.00 105.22 ? 57  ASN   D OD1    1 
ATOM   10637 N  ND2    . ASN   D 2  57  ? 15.335  -23.849  45.689   1.00 97.80  ? 57  ASN   D ND2    1 
ATOM   10638 N  N      . LYS   D 2  58  ? 17.217  -20.346  48.601   1.00 95.47  ? 58  LYS   D N      1 
ATOM   10639 C  CA     . LYS   D 2  58  ? 17.173  -18.898  48.711   1.00 95.64  ? 58  LYS   D CA     1 
ATOM   10640 C  C      . LYS   D 2  58  ? 17.718  -18.295  47.423   1.00 92.02  ? 58  LYS   D C      1 
ATOM   10641 O  O      . LYS   D 2  58  ? 18.814  -18.655  46.982   1.00 93.75  ? 58  LYS   D O      1 
ATOM   10642 C  CB     . LYS   D 2  58  ? 17.975  -18.415  49.928   1.00 98.40  ? 58  LYS   D CB     1 
ATOM   10643 C  CG     . LYS   D 2  58  ? 17.901  -16.905  50.179   1.00 96.64  ? 58  LYS   D CG     1 
ATOM   10644 C  CD     . LYS   D 2  58  ? 18.075  -16.546  51.662   1.00 99.83  ? 58  LYS   D CD     1 
ATOM   10645 C  CE     . LYS   D 2  58  ? 19.280  -15.631  51.902   1.00 93.17  ? 58  LYS   D CE     1 
ATOM   10646 N  NZ     . LYS   D 2  58  ? 20.001  -15.971  53.162   1.00 83.99  ? 58  LYS   D NZ     1 
ATOM   10647 N  N      . TYR   D 2  59  ? 16.952  -17.390  46.820   1.00 86.98  ? 59  TYR   D N      1 
ATOM   10648 C  CA     . TYR   D 2  59  ? 17.368  -16.677  45.619   1.00 79.35  ? 59  TYR   D CA     1 
ATOM   10649 C  C      . TYR   D 2  59  ? 17.938  -15.327  46.017   1.00 77.83  ? 59  TYR   D C      1 
ATOM   10650 O  O      . TYR   D 2  59  ? 17.259  -14.533  46.675   1.00 81.98  ? 59  TYR   D O      1 
ATOM   10651 C  CB     . TYR   D 2  59  ? 16.199  -16.494  44.660   1.00 79.44  ? 59  TYR   D CB     1 
ATOM   10652 C  CG     . TYR   D 2  59  ? 15.651  -17.803  44.178   1.00 85.89  ? 59  TYR   D CG     1 
ATOM   10653 C  CD1    . TYR   D 2  59  ? 16.276  -18.500  43.154   1.00 85.03  ? 59  TYR   D CD1    1 
ATOM   10654 C  CD2    . TYR   D 2  59  ? 14.537  -18.369  44.780   1.00 85.94  ? 59  TYR   D CD2    1 
ATOM   10655 C  CE1    . TYR   D 2  59  ? 15.785  -19.706  42.721   1.00 86.67  ? 59  TYR   D CE1    1 
ATOM   10656 C  CE2    . TYR   D 2  59  ? 14.039  -19.574  44.357   1.00 84.11  ? 59  TYR   D CE2    1 
ATOM   10657 C  CZ     . TYR   D 2  59  ? 14.665  -20.238  43.326   1.00 86.67  ? 59  TYR   D CZ     1 
ATOM   10658 O  OH     . TYR   D 2  59  ? 14.175  -21.445  42.898   1.00 90.87  ? 59  TYR   D OH     1 
ATOM   10659 N  N      . VAL   D 2  60  ? 19.174  -15.073  45.619   1.00 71.74  ? 60  VAL   D N      1 
ATOM   10660 C  CA     . VAL   D 2  60  ? 19.897  -13.855  45.966   1.00 69.84  ? 60  VAL   D CA     1 
ATOM   10661 C  C      . VAL   D 2  60  ? 20.071  -13.044  44.690   1.00 69.27  ? 60  VAL   D C      1 
ATOM   10662 O  O      . VAL   D 2  60  ? 20.677  -13.539  43.731   1.00 70.76  ? 60  VAL   D O      1 
ATOM   10663 C  CB     . VAL   D 2  60  ? 21.259  -14.165  46.610   1.00 66.41  ? 60  VAL   D CB     1 
ATOM   10664 C  CG1    . VAL   D 2  60  ? 21.817  -12.932  47.310   1.00 66.00  ? 60  VAL   D CG1    1 
ATOM   10665 C  CG2    . VAL   D 2  60  ? 21.132  -15.339  47.559   1.00 67.62  ? 60  VAL   D CG2    1 
ATOM   10666 N  N      . PRO   D 2  61  ? 19.566  -11.815  44.626   1.00 70.62  ? 61  PRO   D N      1 
ATOM   10667 C  CA     . PRO   D 2  61  ? 19.848  -10.975  43.464   1.00 68.46  ? 61  PRO   D CA     1 
ATOM   10668 C  C      . PRO   D 2  61  ? 21.333  -11.030  43.145   1.00 67.89  ? 61  PRO   D C      1 
ATOM   10669 O  O      . PRO   D 2  61  ? 22.166  -11.264  44.021   1.00 68.22  ? 61  PRO   D O      1 
ATOM   10670 C  CB     . PRO   D 2  61  ? 19.428  -9.576   43.923   1.00 68.25  ? 61  PRO   D CB     1 
ATOM   10671 C  CG     . PRO   D 2  61  ? 18.450  -9.813   44.989   1.00 71.41  ? 61  PRO   D CG     1 
ATOM   10672 C  CD     . PRO   D 2  61  ? 18.866  -11.073  45.687   1.00 74.41  ? 61  PRO   D CD     1 
ATOM   10673 N  N      . ARG   D 2  62  ? 21.653  -10.860  41.870   1.00 69.10  ? 62  ARG   D N      1 
ATOM   10674 C  CA     . ARG   D 2  62  ? 23.037  -10.753  41.437   1.00 64.99  ? 62  ARG   D CA     1 
ATOM   10675 C  C      . ARG   D 2  62  ? 23.373  -9.271   41.286   1.00 65.64  ? 62  ARG   D C      1 
ATOM   10676 O  O      . ARG   D 2  62  ? 23.654  -8.751   40.203   1.00 62.23  ? 62  ARG   D O      1 
ATOM   10677 C  CB     . ARG   D 2  62  ? 23.250  -11.545  40.153   1.00 63.13  ? 62  ARG   D CB     1 
ATOM   10678 C  CG     . ARG   D 2  62  ? 24.718  -11.860  39.900   1.00 69.05  ? 62  ARG   D CG     1 
ATOM   10679 C  CD     . ARG   D 2  62  ? 24.965  -12.547  38.563   1.00 63.32  ? 62  ARG   D CD     1 
ATOM   10680 N  NE     . ARG   D 2  62  ? 23.777  -13.201  38.031   1.00 63.79  ? 62  ARG   D NE     1 
ATOM   10681 C  CZ     . ARG   D 2  62  ? 23.350  -14.386  38.432   1.00 62.60  ? 62  ARG   D CZ     1 
ATOM   10682 N  NH1    . ARG   D 2  62  ? 23.974  -15.047  39.386   1.00 65.83  ? 62  ARG   D NH1    1 
ATOM   10683 N  NH2    . ARG   D 2  62  ? 22.268  -14.916  37.863   1.00 57.84  ? 62  ARG   D NH2    1 
ATOM   10684 N  N      . ALA   D 2  63  ? 23.302  -8.583   42.424   1.00 67.47  ? 63  ALA   D N      1 
ATOM   10685 C  CA     . ALA   D 2  63  ? 23.381  -7.133   42.463   1.00 68.81  ? 63  ALA   D CA     1 
ATOM   10686 C  C      . ALA   D 2  63  ? 24.634  -6.687   43.203   1.00 63.60  ? 63  ALA   D C      1 
ATOM   10687 O  O      . ALA   D 2  63  ? 25.003  -7.271   44.220   1.00 69.31  ? 63  ALA   D O      1 
ATOM   10688 C  CB     . ALA   D 2  63  ? 22.127  -6.540   43.123   1.00 64.35  ? 63  ALA   D CB     1 
ATOM   10689 N  N      . ILE   D 2  64  ? 25.285  -5.654   42.676   1.00 62.33  ? 64  ILE   D N      1 
ATOM   10690 C  CA     . ILE   D 2  64  ? 26.445  -5.020   43.290   1.00 64.26  ? 64  ILE   D CA     1 
ATOM   10691 C  C      . ILE   D 2  64  ? 26.022  -3.601   43.616   1.00 72.21  ? 64  ILE   D C      1 
ATOM   10692 O  O      . ILE   D 2  64  ? 25.956  -2.755   42.714   1.00 71.49  ? 64  ILE   D O      1 
ATOM   10693 C  CB     . ILE   D 2  64  ? 27.665  -5.001   42.359   1.00 65.76  ? 64  ILE   D CB     1 
ATOM   10694 C  CG1    . ILE   D 2  64  ? 27.969  -6.388   41.813   1.00 61.87  ? 64  ILE   D CG1    1 
ATOM   10695 C  CG2    . ILE   D 2  64  ? 28.858  -4.379   43.057   1.00 63.37  ? 64  ILE   D CG2    1 
ATOM   10696 C  CD1    . ILE   D 2  64  ? 27.567  -7.486   42.747   1.00 68.30  ? 64  ILE   D CD1    1 
ATOM   10697 N  N      . LEU   D 2  65  ? 25.742  -3.325   44.891   1.00 72.56  ? 65  LEU   D N      1 
ATOM   10698 C  CA     . LEU   D 2  65  ? 25.371  -1.982   45.329   1.00 68.82  ? 65  LEU   D CA     1 
ATOM   10699 C  C      . LEU   D 2  65  ? 26.642  -1.180   45.589   1.00 68.29  ? 65  LEU   D C      1 
ATOM   10700 O  O      . LEU   D 2  65  ? 27.571  -1.683   46.223   1.00 72.20  ? 65  LEU   D O      1 
ATOM   10701 C  CB     . LEU   D 2  65  ? 24.500  -2.067   46.579   1.00 70.60  ? 65  LEU   D CB     1 
ATOM   10702 C  CG     . LEU   D 2  65  ? 23.577  -3.290   46.503   1.00 72.62  ? 65  LEU   D CG     1 
ATOM   10703 C  CD1    . LEU   D 2  65  ? 22.543  -3.340   47.601   1.00 77.89  ? 65  LEU   D CD1    1 
ATOM   10704 C  CD2    . LEU   D 2  65  ? 22.892  -3.305   45.175   1.00 73.11  ? 65  LEU   D CD2    1 
ATOM   10705 N  N      . VAL   D 2  66  ? 26.697  0.049    45.081   1.00 65.76  ? 66  VAL   D N      1 
ATOM   10706 C  CA     . VAL   D 2  66  ? 27.920  0.852    45.124   1.00 68.92  ? 66  VAL   D CA     1 
ATOM   10707 C  C      . VAL   D 2  66  ? 27.550  2.311    45.350   1.00 73.31  ? 66  VAL   D C      1 
ATOM   10708 O  O      . VAL   D 2  66  ? 26.546  2.788    44.811   1.00 74.71  ? 66  VAL   D O      1 
ATOM   10709 C  CB     . VAL   D 2  66  ? 28.737  0.700    43.820   1.00 70.30  ? 66  VAL   D CB     1 
ATOM   10710 C  CG1    . VAL   D 2  66  ? 29.689  1.884    43.612   1.00 64.11  ? 66  VAL   D CG1    1 
ATOM   10711 C  CG2    . VAL   D 2  66  ? 29.485  -0.625   43.809   1.00 74.62  ? 66  VAL   D CG2    1 
ATOM   10712 N  N      . ASP   D 2  67  ? 28.354  3.020    46.152   1.00 76.19  ? 67  ASP   D N      1 
ATOM   10713 C  CA     . ASP   D 2  67  ? 28.211  4.467    46.315   1.00 77.68  ? 67  ASP   D CA     1 
ATOM   10714 C  C      . ASP   D 2  67  ? 29.493  5.028    46.914   1.00 79.00  ? 67  ASP   D C      1 
ATOM   10715 O  O      . ASP   D 2  67  ? 30.353  4.283    47.391   1.00 84.32  ? 67  ASP   D O      1 
ATOM   10716 C  CB     . ASP   D 2  67  ? 27.004  4.823    47.188   1.00 78.65  ? 67  ASP   D CB     1 
ATOM   10717 C  CG     . ASP   D 2  67  ? 26.536  6.258    46.986   1.00 81.12  ? 67  ASP   D CG     1 
ATOM   10718 O  OD1    . ASP   D 2  67  ? 27.263  7.057    46.347   1.00 77.18  ? 67  ASP   D OD1    1 
ATOM   10719 O  OD2    . ASP   D 2  67  ? 25.426  6.579    47.459   1.00 87.61  ? 67  ASP   D OD2    1 
ATOM   10720 N  N      . LEU   D 2  68  ? 29.613  6.358    46.890   1.00 77.60  ? 68  LEU   D N      1 
ATOM   10721 C  CA     . LEU   D 2  68  ? 30.720  7.035    47.558   1.00 86.19  ? 68  LEU   D CA     1 
ATOM   10722 C  C      . LEU   D 2  68  ? 30.350  7.623    48.929   1.00 91.37  ? 68  LEU   D C      1 
ATOM   10723 O  O      . LEU   D 2  68  ? 31.211  8.229    49.579   1.00 90.17  ? 68  LEU   D O      1 
ATOM   10724 C  CB     . LEU   D 2  68  ? 31.297  8.125    46.646   1.00 82.76  ? 68  LEU   D CB     1 
ATOM   10725 C  CG     . LEU   D 2  68  ? 32.175  7.577    45.516   1.00 79.91  ? 68  LEU   D CG     1 
ATOM   10726 C  CD1    . LEU   D 2  68  ? 33.106  8.635    44.946   1.00 80.29  ? 68  LEU   D CD1    1 
ATOM   10727 C  CD2    . LEU   D 2  68  ? 32.973  6.381    46.009   1.00 76.76  ? 68  LEU   D CD2    1 
ATOM   10728 N  N      . GLU   D 2  69  ? 29.103  7.437    49.396   1.00 89.14  ? 69  GLU   D N      1 
ATOM   10729 C  CA     . GLU   D 2  69  ? 28.640  7.909    50.698   1.00 88.91  ? 69  GLU   D CA     1 
ATOM   10730 C  C      . GLU   D 2  69  ? 27.798  6.836    51.374   1.00 91.91  ? 69  GLU   D C      1 
ATOM   10731 O  O      . GLU   D 2  69  ? 26.768  6.431    50.825   1.00 97.86  ? 69  GLU   D O      1 
ATOM   10732 C  CB     . GLU   D 2  69  ? 27.821  9.193    50.556   1.00 90.06  ? 69  GLU   D CB     1 
ATOM   10733 C  CG     . GLU   D 2  69  ? 28.550  10.329   49.847   1.00 96.18  ? 69  GLU   D CG     1 
ATOM   10734 C  CD     . GLU   D 2  69  ? 27.698  11.591   49.689   1.00 99.65  ? 69  GLU   D CD     1 
ATOM   10735 O  OE1    . GLU   D 2  69  ? 26.454  11.501   49.833   1.00 93.70  ? 69  GLU   D OE1    1 
ATOM   10736 O  OE2    . GLU   D 2  69  ? 28.279  12.673   49.420   1.00 95.14  ? 69  GLU   D OE2    1 
ATOM   10737 N  N      . PRO   D 2  70  ? 28.163  6.384    52.579   1.00 94.56  ? 70  PRO   D N      1 
ATOM   10738 C  CA     . PRO   D 2  70  ? 27.459  5.244    53.191   1.00 98.41  ? 70  PRO   D CA     1 
ATOM   10739 C  C      . PRO   D 2  70  ? 26.001  5.507    53.516   1.00 100.05 ? 70  PRO   D C      1 
ATOM   10740 O  O      . PRO   D 2  70  ? 25.331  4.605    54.033   1.00 100.97 ? 70  PRO   D O      1 
ATOM   10741 C  CB     . PRO   D 2  70  ? 28.254  4.981    54.474   1.00 99.56  ? 70  PRO   D CB     1 
ATOM   10742 C  CG     . PRO   D 2  70  ? 28.909  6.278    54.796   1.00 104.00 ? 70  PRO   D CG     1 
ATOM   10743 C  CD     . PRO   D 2  70  ? 29.057  7.075    53.524   1.00 96.89  ? 70  PRO   D CD     1 
ATOM   10744 N  N      . GLY   D 2  71  ? 25.486  6.700    53.236   1.00 100.83 ? 71  GLY   D N      1 
ATOM   10745 C  CA     . GLY   D 2  71  ? 24.109  7.018    53.556   1.00 104.87 ? 71  GLY   D CA     1 
ATOM   10746 C  C      . GLY   D 2  71  ? 23.126  6.261    52.691   1.00 103.98 ? 71  GLY   D C      1 
ATOM   10747 O  O      . GLY   D 2  71  ? 22.338  5.448    53.183   1.00 103.58 ? 71  GLY   D O      1 
ATOM   10748 N  N      . THR   D 2  72  ? 23.163  6.548    51.390   1.00 107.15 ? 72  THR   D N      1 
ATOM   10749 C  CA     . THR   D 2  72  ? 22.403  5.790    50.404   1.00 107.76 ? 72  THR   D CA     1 
ATOM   10750 C  C      . THR   D 2  72  ? 22.468  4.294    50.697   1.00 105.25 ? 72  THR   D C      1 
ATOM   10751 O  O      . THR   D 2  72  ? 21.454  3.593    50.648   1.00 101.58 ? 72  THR   D O      1 
ATOM   10752 C  CB     . THR   D 2  72  ? 22.949  6.093    49.004   1.00 103.70 ? 72  THR   D CB     1 
ATOM   10753 O  OG1    . THR   D 2  72  ? 24.323  5.679    48.937   1.00 94.04  ? 72  THR   D OG1    1 
ATOM   10754 C  CG2    . THR   D 2  72  ? 22.863  7.587    48.714   1.00 93.66  ? 72  THR   D CG2    1 
ATOM   10755 N  N      . MET   D 2  73  ? 23.663  3.797    51.020   1.00 106.68 ? 73  MET   D N      1 
ATOM   10756 C  CA     . MET   D 2  73  ? 23.832  2.392    51.379   1.00 108.32 ? 73  MET   D CA     1 
ATOM   10757 C  C      . MET   D 2  73  ? 22.883  1.962    52.498   1.00 109.53 ? 73  MET   D C      1 
ATOM   10758 O  O      . MET   D 2  73  ? 22.065  1.050    52.319   1.00 104.22 ? 73  MET   D O      1 
ATOM   10759 C  CB     . MET   D 2  73  ? 25.293  2.139    51.764   1.00 108.76 ? 73  MET   D CB     1 
ATOM   10760 C  CG     . MET   D 2  73  ? 25.536  0.948    52.698   1.00 110.72 ? 73  MET   D CG     1 
ATOM   10761 S  SD     . MET   D 2  73  ? 27.260  0.423    52.681   1.00 131.46 ? 73  MET   D SD     1 
ATOM   10762 C  CE     . MET   D 2  73  ? 27.693  0.566    54.418   1.00 111.30 ? 73  MET   D CE     1 
ATOM   10763 N  N      . ASP   D 2  74  ? 22.992  2.597    53.672   1.00 110.64 ? 74  ASP   D N      1 
ATOM   10764 C  CA     . ASP   D 2  74  ? 22.206  2.153    54.820   1.00 108.13 ? 74  ASP   D CA     1 
ATOM   10765 C  C      . ASP   D 2  74  ? 20.721  2.090    54.483   1.00 105.91 ? 74  ASP   D C      1 
ATOM   10766 O  O      . ASP   D 2  74  ? 20.030  1.136    54.865   1.00 101.74 ? 74  ASP   D O      1 
ATOM   10767 C  CB     . ASP   D 2  74  ? 22.454  3.076    56.013   1.00 111.64 ? 74  ASP   D CB     1 
ATOM   10768 C  CG     . ASP   D 2  74  ? 22.237  2.377    57.344   1.00 112.57 ? 74  ASP   D CG     1 
ATOM   10769 O  OD1    . ASP   D 2  74  ? 21.073  2.041    57.652   1.00 109.53 ? 74  ASP   D OD1    1 
ATOM   10770 O  OD2    . ASP   D 2  74  ? 23.226  2.163    58.078   1.00 110.87 ? 74  ASP   D OD2    1 
ATOM   10771 N  N      . SER   D 2  75  ? 20.218  3.093    53.757   1.00 103.44 ? 75  SER   D N      1 
ATOM   10772 C  CA     . SER   D 2  75  ? 18.812  3.103    53.369   1.00 101.63 ? 75  SER   D CA     1 
ATOM   10773 C  C      . SER   D 2  75  ? 18.398  1.775    52.755   1.00 105.38 ? 75  SER   D C      1 
ATOM   10774 O  O      . SER   D 2  75  ? 17.306  1.268    53.029   1.00 106.02 ? 75  SER   D O      1 
ATOM   10775 C  CB     . SER   D 2  75  ? 18.553  4.235    52.381   1.00 101.42 ? 75  SER   D CB     1 
ATOM   10776 O  OG     . SER   D 2  75  ? 19.761  4.906    52.077   1.00 102.85 ? 75  SER   D OG     1 
ATOM   10777 N  N      . VAL   D 2  76  ? 19.266  1.187    51.930   1.00 103.96 ? 76  VAL   D N      1 
ATOM   10778 C  CA     . VAL   D 2  76  ? 18.885  -0.003   51.171   1.00 98.45  ? 76  VAL   D CA     1 
ATOM   10779 C  C      . VAL   D 2  76  ? 18.529  -1.151   52.106   1.00 97.85  ? 76  VAL   D C      1 
ATOM   10780 O  O      . VAL   D 2  76  ? 17.412  -1.677   52.063   1.00 101.57 ? 76  VAL   D O      1 
ATOM   10781 C  CB     . VAL   D 2  76  ? 19.999  -0.404   50.192   1.00 97.31  ? 76  VAL   D CB     1 
ATOM   10782 C  CG1    . VAL   D 2  76  ? 19.575  -1.627   49.398   1.00 92.34  ? 76  VAL   D CG1    1 
ATOM   10783 C  CG2    . VAL   D 2  76  ? 20.300  0.745    49.261   1.00 93.98  ? 76  VAL   D CG2    1 
ATOM   10784 N  N      . ARG   D 2  77  ? 19.476  -1.582   52.946   1.00 98.69  ? 77  ARG   D N      1 
ATOM   10785 C  CA     . ARG   D 2  77  ? 19.169  -2.690   53.848   1.00 98.65  ? 77  ARG   D CA     1 
ATOM   10786 C  C      . ARG   D 2  77  ? 17.946  -2.378   54.688   1.00 102.22 ? 77  ARG   D C      1 
ATOM   10787 O  O      . ARG   D 2  77  ? 17.110  -3.255   54.937   1.00 99.77  ? 77  ARG   D O      1 
ATOM   10788 C  CB     . ARG   D 2  77  ? 20.341  -3.007   54.774   1.00 93.89  ? 77  ARG   D CB     1 
ATOM   10789 C  CG     . ARG   D 2  77  ? 21.705  -2.664   54.264   1.00 99.73  ? 77  ARG   D CG     1 
ATOM   10790 C  CD     . ARG   D 2  77  ? 22.730  -3.158   55.280   1.00 98.73  ? 77  ARG   D CD     1 
ATOM   10791 N  NE     . ARG   D 2  77  ? 24.099  -2.837   54.899   1.00 89.51  ? 77  ARG   D NE     1 
ATOM   10792 C  CZ     . ARG   D 2  77  ? 24.557  -1.604   54.726   1.00 97.63  ? 77  ARG   D CZ     1 
ATOM   10793 N  NH1    . ARG   D 2  77  ? 23.772  -0.548   54.881   1.00 103.97 ? 77  ARG   D NH1    1 
ATOM   10794 N  NH2    . ARG   D 2  77  ? 25.831  -1.426   54.383   1.00 94.55  ? 77  ARG   D NH2    1 
ATOM   10795 N  N      . SER   D 2  78  ? 17.832  -1.129   55.146   1.00 103.90 ? 78  SER   D N      1 
ATOM   10796 C  CA     . SER   D 2  78  ? 16.701  -0.742   55.981   1.00 104.08 ? 78  SER   D CA     1 
ATOM   10797 C  C      . SER   D 2  78  ? 15.383  -0.947   55.241   1.00 101.63 ? 78  SER   D C      1 
ATOM   10798 O  O      . SER   D 2  78  ? 14.434  -1.521   55.787   1.00 98.09  ? 78  SER   D O      1 
ATOM   10799 C  CB     . SER   D 2  78  ? 16.854  0.716    56.420   1.00 108.99 ? 78  SER   D CB     1 
ATOM   10800 O  OG     . SER   D 2  78  ? 16.330  1.602    55.442   1.00 111.66 ? 78  SER   D OG     1 
ATOM   10801 N  N      . GLY   D 2  79  ? 15.316  -0.494   53.989   1.00 101.88 ? 79  GLY   D N      1 
ATOM   10802 C  CA     . GLY   D 2  79  ? 14.122  -0.607   53.189   1.00 102.77 ? 79  GLY   D CA     1 
ATOM   10803 C  C      . GLY   D 2  79  ? 13.668  -2.038   52.971   1.00 98.13  ? 79  GLY   D C      1 
ATOM   10804 O  O      . GLY   D 2  79  ? 14.279  -3.003   53.447   1.00 93.98  ? 79  GLY   D O      1 
ATOM   10805 N  N      . PRO   D 2  80  ? 12.566  -2.195   52.239   1.00 99.45  ? 80  PRO   D N      1 
ATOM   10806 C  CA     . PRO   D 2  80  ? 12.064  -3.541   51.935   1.00 99.68  ? 80  PRO   D CA     1 
ATOM   10807 C  C      . PRO   D 2  80  ? 13.089  -4.293   51.108   1.00 102.82 ? 80  PRO   D C      1 
ATOM   10808 O  O      . PRO   D 2  80  ? 13.748  -3.712   50.243   1.00 106.48 ? 80  PRO   D O      1 
ATOM   10809 C  CB     . PRO   D 2  80  ? 10.783  -3.274   51.126   1.00 100.75 ? 80  PRO   D CB     1 
ATOM   10810 C  CG     . PRO   D 2  80  ? 10.450  -1.823   51.353   1.00 104.64 ? 80  PRO   D CG     1 
ATOM   10811 C  CD     . PRO   D 2  80  ? 11.771  -1.139   51.588   1.00 102.83 ? 80  PRO   D CD     1 
ATOM   10812 N  N      . PHE   D 2  81  ? 13.229  -5.590   51.378   1.00 103.79 ? 81  PHE   D N      1 
ATOM   10813 C  CA     . PHE   D 2  81  ? 14.133  -6.470   50.640   1.00 99.08  ? 81  PHE   D CA     1 
ATOM   10814 C  C      . PHE   D 2  81  ? 15.604  -6.164   50.911   1.00 95.14  ? 81  PHE   D C      1 
ATOM   10815 O  O      . PHE   D 2  81  ? 16.470  -6.841   50.352   1.00 96.52  ? 81  PHE   D O      1 
ATOM   10816 C  CB     . PHE   D 2  81  ? 13.886  -6.407   49.121   1.00 90.61  ? 81  PHE   D CB     1 
ATOM   10817 C  CG     . PHE   D 2  81  ? 12.562  -6.979   48.686   1.00 88.48  ? 81  PHE   D CG     1 
ATOM   10818 C  CD1    . PHE   D 2  81  ? 11.510  -6.139   48.364   1.00 89.54  ? 81  PHE   D CD1    1 
ATOM   10819 C  CD2    . PHE   D 2  81  ? 12.371  -8.350   48.577   1.00 91.86  ? 81  PHE   D CD2    1 
ATOM   10820 C  CE1    . PHE   D 2  81  ? 10.284  -6.643   47.951   1.00 87.29  ? 81  PHE   D CE1    1 
ATOM   10821 C  CE2    . PHE   D 2  81  ? 11.144  -8.871   48.163   1.00 91.86  ? 81  PHE   D CE2    1 
ATOM   10822 C  CZ     . PHE   D 2  81  ? 10.098  -8.010   47.850   1.00 89.74  ? 81  PHE   D CZ     1 
ATOM   10823 N  N      . GLY   D 2  82  ? 15.921  -5.166   51.746   1.00 94.18  ? 82  GLY   D N      1 
ATOM   10824 C  CA     . GLY   D 2  82  ? 17.317  -4.864   52.009   1.00 94.50  ? 82  GLY   D CA     1 
ATOM   10825 C  C      . GLY   D 2  82  ? 18.104  -6.087   52.425   1.00 96.89  ? 82  GLY   D C      1 
ATOM   10826 O  O      . GLY   D 2  82  ? 19.314  -6.164   52.189   1.00 96.58  ? 82  GLY   D O      1 
ATOM   10827 N  N      . GLN   D 2  83  ? 17.431  -7.062   53.036   1.00 99.75  ? 83  GLN   D N      1 
ATOM   10828 C  CA     . GLN   D 2  83  ? 18.062  -8.283   53.516   1.00 98.99  ? 83  GLN   D CA     1 
ATOM   10829 C  C      . GLN   D 2  83  ? 17.947  -9.437   52.533   1.00 95.20  ? 83  GLN   D C      1 
ATOM   10830 O  O      . GLN   D 2  83  ? 18.329  -10.565  52.874   1.00 94.82  ? 83  GLN   D O      1 
ATOM   10831 C  CB     . GLN   D 2  83  ? 17.458  -8.692   54.865   1.00 107.91 ? 83  GLN   D CB     1 
ATOM   10832 C  CG     . GLN   D 2  83  ? 17.441  -7.575   55.908   1.00 108.49 ? 83  GLN   D CG     1 
ATOM   10833 C  CD     . GLN   D 2  83  ? 18.790  -6.877   56.049   1.00 107.14 ? 83  GLN   D CD     1 
ATOM   10834 O  OE1    . GLN   D 2  83  ? 18.896  -5.657   55.880   1.00 106.15 ? 83  GLN   D OE1    1 
ATOM   10835 N  NE2    . GLN   D 2  83  ? 19.827  -7.649   56.367   1.00 106.34 ? 83  GLN   D NE2    1 
ATOM   10836 N  N      . ILE   D 2  84  ? 17.400  -9.196   51.339   1.00 94.06  ? 84  ILE   D N      1 
ATOM   10837 C  CA     . ILE   D 2  84  ? 17.509  -10.191  50.278   1.00 94.24  ? 84  ILE   D CA     1 
ATOM   10838 C  C      . ILE   D 2  84  ? 18.866  -10.096  49.596   1.00 83.96  ? 84  ILE   D C      1 
ATOM   10839 O  O      . ILE   D 2  84  ? 19.349  -11.091  49.043   1.00 77.82  ? 84  ILE   D O      1 
ATOM   10840 C  CB     . ILE   D 2  84  ? 16.383  -10.054  49.236   1.00 87.73  ? 84  ILE   D CB     1 
ATOM   10841 C  CG1    . ILE   D 2  84  ? 16.375  -11.267  48.308   1.00 86.58  ? 84  ILE   D CG1    1 
ATOM   10842 C  CG2    . ILE   D 2  84  ? 16.561  -8.796   48.391   1.00 82.64  ? 84  ILE   D CG2    1 
ATOM   10843 C  CD1    . ILE   D 2  84  ? 14.996  -11.805  48.052   1.00 85.72  ? 84  ILE   D CD1    1 
ATOM   10844 N  N      . PHE   D 2  85  ? 19.506  -8.933   49.656   1.00 75.96  ? 85  PHE   D N      1 
ATOM   10845 C  CA     . PHE   D 2  85  ? 20.760  -8.741   48.961   1.00 79.83  ? 85  PHE   D CA     1 
ATOM   10846 C  C      . PHE   D 2  85  ? 21.876  -9.527   49.637   1.00 84.42  ? 85  PHE   D C      1 
ATOM   10847 O  O      . PHE   D 2  85  ? 21.697  -10.138  50.694   1.00 89.10  ? 85  PHE   D O      1 
ATOM   10848 C  CB     . PHE   D 2  85  ? 21.106  -7.255   48.883   1.00 80.68  ? 85  PHE   D CB     1 
ATOM   10849 C  CG     . PHE   D 2  85  ? 20.191  -6.480   47.978   1.00 82.44  ? 85  PHE   D CG     1 
ATOM   10850 C  CD1    . PHE   D 2  85  ? 19.829  -5.180   48.269   1.00 84.39  ? 85  PHE   D CD1    1 
ATOM   10851 C  CD2    . PHE   D 2  85  ? 19.670  -7.076   46.838   1.00 80.47  ? 85  PHE   D CD2    1 
ATOM   10852 C  CE1    . PHE   D 2  85  ? 18.975  -4.490   47.431   1.00 83.85  ? 85  PHE   D CE1    1 
ATOM   10853 C  CE2    . PHE   D 2  85  ? 18.826  -6.393   46.004   1.00 73.30  ? 85  PHE   D CE2    1 
ATOM   10854 C  CZ     . PHE   D 2  85  ? 18.477  -5.100   46.296   1.00 77.47  ? 85  PHE   D CZ     1 
ATOM   10855 N  N      . ARG   D 2  86  ? 23.036  -9.528   48.981   1.00 84.49  ? 86  ARG   D N      1 
ATOM   10856 C  CA     . ARG   D 2  86  ? 24.229  -10.155  49.522   1.00 78.31  ? 86  ARG   D CA     1 
ATOM   10857 C  C      . ARG   D 2  86  ? 24.991  -9.124   50.341   1.00 78.56  ? 86  ARG   D C      1 
ATOM   10858 O  O      . ARG   D 2  86  ? 25.327  -8.055   49.810   1.00 71.92  ? 86  ARG   D O      1 
ATOM   10859 C  CB     . ARG   D 2  86  ? 25.104  -10.707  48.407   1.00 75.84  ? 86  ARG   D CB     1 
ATOM   10860 C  CG     . ARG   D 2  86  ? 25.676  -12.077  48.732   1.00 81.59  ? 86  ARG   D CG     1 
ATOM   10861 C  CD     . ARG   D 2  86  ? 26.784  -12.505  47.777   1.00 79.25  ? 86  ARG   D CD     1 
ATOM   10862 N  NE     . ARG   D 2  86  ? 27.590  -13.595  48.328   1.00 91.49  ? 86  ARG   D NE     1 
ATOM   10863 C  CZ     . ARG   D 2  86  ? 28.843  -13.467  48.758   1.00 93.09  ? 86  ARG   D CZ     1 
ATOM   10864 N  NH1    . ARG   D 2  86  ? 29.486  -12.314  48.680   1.00 90.80  ? 86  ARG   D NH1    1 
ATOM   10865 N  NH2    . ARG   D 2  86  ? 29.458  -14.517  49.299   1.00 88.25  ? 86  ARG   D NH2    1 
ATOM   10866 N  N      . PRO   D 2  87  ? 25.255  -9.383   51.629   1.00 86.57  ? 87  PRO   D N      1 
ATOM   10867 C  CA     . PRO   D 2  87  ? 25.913  -8.361   52.465   1.00 76.86  ? 87  PRO   D CA     1 
ATOM   10868 C  C      . PRO   D 2  87  ? 27.274  -7.959   51.947   1.00 74.55  ? 87  PRO   D C      1 
ATOM   10869 O  O      . PRO   D 2  87  ? 27.664  -6.792   52.079   1.00 70.77  ? 87  PRO   D O      1 
ATOM   10870 C  CB     . PRO   D 2  87  ? 26.010  -9.043   53.837   1.00 75.52  ? 87  PRO   D CB     1 
ATOM   10871 C  CG     . PRO   D 2  87  ? 24.973  -10.130  53.812   1.00 78.55  ? 87  PRO   D CG     1 
ATOM   10872 C  CD     . PRO   D 2  87  ? 24.947  -10.609  52.389   1.00 79.72  ? 87  PRO   D CD     1 
ATOM   10873 N  N      . ASP   D 2  88  ? 28.000  -8.900   51.342   1.00 77.45  ? 88  ASP   D N      1 
ATOM   10874 C  CA     . ASP   D 2  88  ? 29.312  -8.606   50.782   1.00 77.46  ? 88  ASP   D CA     1 
ATOM   10875 C  C      . ASP   D 2  88  ? 29.220  -7.718   49.550   1.00 79.63  ? 88  ASP   D C      1 
ATOM   10876 O  O      . ASP   D 2  88  ? 30.163  -6.976   49.252   1.00 80.64  ? 88  ASP   D O      1 
ATOM   10877 C  CB     . ASP   D 2  88  ? 30.018  -9.912   50.430   1.00 83.48  ? 88  ASP   D CB     1 
ATOM   10878 C  CG     . ASP   D 2  88  ? 30.671  -10.561  51.633   1.00 89.09  ? 88  ASP   D CG     1 
ATOM   10879 O  OD1    . ASP   D 2  88  ? 30.539  -10.006  52.747   1.00 83.08  ? 88  ASP   D OD1    1 
ATOM   10880 O  OD2    . ASP   D 2  88  ? 31.310  -11.628  51.469   1.00 92.87  ? 88  ASP   D OD2    1 
ATOM   10881 N  N      . ASN   D 2  89  ? 28.107  -7.776   48.820   1.00 79.46  ? 89  ASN   D N      1 
ATOM   10882 C  CA     . ASN   D 2  89  ? 28.009  -7.044   47.565   1.00 74.18  ? 89  ASN   D CA     1 
ATOM   10883 C  C      . ASN   D 2  89  ? 27.794  -5.553   47.760   1.00 73.78  ? 89  ASN   D C      1 
ATOM   10884 O  O      . ASN   D 2  89  ? 27.743  -4.818   46.767   1.00 73.59  ? 89  ASN   D O      1 
ATOM   10885 C  CB     . ASN   D 2  89  ? 26.892  -7.619   46.695   1.00 71.69  ? 89  ASN   D CB     1 
ATOM   10886 C  CG     . ASN   D 2  89  ? 27.172  -9.047   46.255   1.00 73.13  ? 89  ASN   D CG     1 
ATOM   10887 O  OD1    . ASN   D 2  89  ? 27.897  -9.782   46.927   1.00 80.12  ? 89  ASN   D OD1    1 
ATOM   10888 N  ND2    . ASN   D 2  89  ? 26.606  -9.444   45.118   1.00 66.14  ? 89  ASN   D ND2    1 
ATOM   10889 N  N      . PHE   D 2  90  ? 27.664  -5.084   48.997   1.00 76.11  ? 90  PHE   D N      1 
ATOM   10890 C  CA     . PHE   D 2  90  ? 27.698  -3.653   49.260   1.00 77.43  ? 90  PHE   D CA     1 
ATOM   10891 C  C      . PHE   D 2  90  ? 29.143  -3.174   49.188   1.00 74.25  ? 90  PHE   D C      1 
ATOM   10892 O  O      . PHE   D 2  90  ? 30.035  -3.804   49.761   1.00 81.88  ? 90  PHE   D O      1 
ATOM   10893 C  CB     . PHE   D 2  90  ? 27.102  -3.341   50.633   1.00 79.58  ? 90  PHE   D CB     1 
ATOM   10894 C  CG     . PHE   D 2  90  ? 25.620  -3.603   50.740   1.00 77.40  ? 90  PHE   D CG     1 
ATOM   10895 C  CD1    . PHE   D 2  90  ? 25.144  -4.872   51.035   1.00 76.91  ? 90  PHE   D CD1    1 
ATOM   10896 C  CD2    . PHE   D 2  90  ? 24.706  -2.574   50.578   1.00 76.71  ? 90  PHE   D CD2    1 
ATOM   10897 C  CE1    . PHE   D 2  90  ? 23.780  -5.111   51.154   1.00 78.31  ? 90  PHE   D CE1    1 
ATOM   10898 C  CE2    . PHE   D 2  90  ? 23.347  -2.810   50.699   1.00 79.54  ? 90  PHE   D CE2    1 
ATOM   10899 C  CZ     . PHE   D 2  90  ? 22.882  -4.078   50.984   1.00 77.21  ? 90  PHE   D CZ     1 
ATOM   10900 N  N      . VAL   D 2  91  ? 29.379  -2.079   48.464   1.00 75.15  ? 91  VAL   D N      1 
ATOM   10901 C  CA     . VAL   D 2  91  ? 30.698  -1.444   48.390   1.00 81.04  ? 91  VAL   D CA     1 
ATOM   10902 C  C      . VAL   D 2  91  ? 30.523  0.067    48.479   1.00 85.40  ? 91  VAL   D C      1 
ATOM   10903 O  O      . VAL   D 2  91  ? 29.891  0.682    47.610   1.00 79.95  ? 91  VAL   D O      1 
ATOM   10904 C  CB     . VAL   D 2  91  ? 31.480  -1.805   47.117   1.00 73.57  ? 91  VAL   D CB     1 
ATOM   10905 C  CG1    . VAL   D 2  91  ? 32.815  -1.095   47.142   1.00 68.77  ? 91  VAL   D CG1    1 
ATOM   10906 C  CG2    . VAL   D 2  91  ? 31.662  -3.308   47.010   1.00 70.89  ? 91  VAL   D CG2    1 
ATOM   10907 N  N      . PHE   D 2  92  ? 31.154  0.664    49.483   1.00 94.20  ? 92  PHE   D N      1 
ATOM   10908 C  CA     . PHE   D 2  92  ? 30.799  1.965    50.029   1.00 92.02  ? 92  PHE   D CA     1 
ATOM   10909 C  C      . PHE   D 2  92  ? 32.042  2.833    50.104   1.00 89.38  ? 92  PHE   D C      1 
ATOM   10910 O  O      . PHE   D 2  92  ? 33.082  2.394    50.599   1.00 88.99  ? 92  PHE   D O      1 
ATOM   10911 C  CB     . PHE   D 2  92  ? 30.194  1.768    51.419   1.00 97.68  ? 92  PHE   D CB     1 
ATOM   10912 C  CG     . PHE   D 2  92  ? 30.859  0.647    52.197   1.00 105.83 ? 92  PHE   D CG     1 
ATOM   10913 C  CD1    . PHE   D 2  92  ? 30.119  -0.431   52.655   1.00 105.34 ? 92  PHE   D CD1    1 
ATOM   10914 C  CD2    . PHE   D 2  92  ? 32.231  0.662    52.453   1.00 106.73 ? 92  PHE   D CD2    1 
ATOM   10915 C  CE1    . PHE   D 2  92  ? 30.718  -1.467   53.357   1.00 110.28 ? 92  PHE   D CE1    1 
ATOM   10916 C  CE2    . PHE   D 2  92  ? 32.848  -0.375   53.154   1.00 104.87 ? 92  PHE   D CE2    1 
ATOM   10917 C  CZ     . PHE   D 2  92  ? 32.089  -1.440   53.610   1.00 110.68 ? 92  PHE   D CZ     1 
ATOM   10918 N  N      . GLY   D 2  93  ? 31.945  4.051    49.596   1.00 89.44  ? 93  GLY   D N      1 
ATOM   10919 C  CA     . GLY   D 2  93  ? 32.936  5.052    49.901   1.00 93.39  ? 93  GLY   D CA     1 
ATOM   10920 C  C      . GLY   D 2  93  ? 32.710  5.591    51.300   1.00 98.47  ? 93  GLY   D C      1 
ATOM   10921 O  O      . GLY   D 2  93  ? 31.990  5.019    52.122   1.00 94.62  ? 93  GLY   D O      1 
ATOM   10922 N  N      . GLN   D 2  94  ? 33.352  6.721    51.570   1.00 100.12 ? 94  GLN   D N      1 
ATOM   10923 C  CA     . GLN   D 2  94  ? 33.069  7.473    52.780   1.00 100.00 ? 94  GLN   D CA     1 
ATOM   10924 C  C      . GLN   D 2  94  ? 33.028  8.942    52.406   1.00 94.16  ? 94  GLN   D C      1 
ATOM   10925 O  O      . GLN   D 2  94  ? 32.025  9.621    52.639   1.00 91.80  ? 94  GLN   D O      1 
ATOM   10926 C  CB     . GLN   D 2  94  ? 34.125  7.206    53.857   1.00 97.77  ? 94  GLN   D CB     1 
ATOM   10927 C  CG     . GLN   D 2  94  ? 33.930  5.912    54.637   1.00 98.68  ? 94  GLN   D CG     1 
ATOM   10928 C  CD     . GLN   D 2  94  ? 32.737  5.972    55.576   1.00 99.54  ? 94  GLN   D CD     1 
ATOM   10929 O  OE1    . GLN   D 2  94  ? 32.435  7.023    56.135   1.00 101.99 ? 94  GLN   D OE1    1 
ATOM   10930 N  NE2    . GLN   D 2  94  ? 32.078  4.833    55.783   1.00 96.42  ? 94  GLN   D NE2    1 
ATOM   10931 N  N      . SER   D 2  95  ? 34.106  9.411    51.770   1.00 95.59  ? 95  SER   D N      1 
ATOM   10932 C  CA     . SER   D 2  95  ? 34.280  10.831   51.484   1.00 102.95 ? 95  SER   D CA     1 
ATOM   10933 C  C      . SER   D 2  95  ? 33.193  11.388   50.568   1.00 105.88 ? 95  SER   D C      1 
ATOM   10934 O  O      . SER   D 2  95  ? 32.988  12.608   50.546   1.00 102.74 ? 95  SER   D O      1 
ATOM   10935 C  CB     . SER   D 2  95  ? 35.667  11.078   50.868   1.00 100.41 ? 95  SER   D CB     1 
ATOM   10936 O  OG     . SER   D 2  95  ? 36.716  10.868   51.805   1.00 93.90  ? 95  SER   D OG     1 
ATOM   10937 N  N      . GLY   D 2  96  ? 32.496  10.535   49.812   1.00 101.83 ? 96  GLY   D N      1 
ATOM   10938 C  CA     . GLY   D 2  96  ? 31.451  10.997   48.921   1.00 95.11  ? 96  GLY   D CA     1 
ATOM   10939 C  C      . GLY   D 2  96  ? 32.000  11.585   47.632   1.00 98.36  ? 96  GLY   D C      1 
ATOM   10940 O  O      . GLY   D 2  96  ? 33.212  11.668   47.405   1.00 97.54  ? 96  GLY   D O      1 
ATOM   10941 N  N      . ALA   D 2  97  ? 31.070  12.016   46.769   1.00 94.69  ? 97  ALA   D N      1 
ATOM   10942 C  CA     . ALA   D 2  97  ? 31.400  12.547   45.449   1.00 87.50  ? 97  ALA   D CA     1 
ATOM   10943 C  C      . ALA   D 2  97  ? 31.091  14.024   45.285   1.00 83.36  ? 97  ALA   D C      1 
ATOM   10944 O  O      . ALA   D 2  97  ? 31.727  14.685   44.459   1.00 83.78  ? 97  ALA   D O      1 
ATOM   10945 C  CB     . ALA   D 2  97  ? 30.657  11.769   44.355   1.00 80.80  ? 97  ALA   D CB     1 
ATOM   10946 N  N      . GLY   D 2  98  ? 30.132  14.552   46.041   1.00 85.45  ? 98  GLY   D N      1 
ATOM   10947 C  CA     . GLY   D 2  98  ? 29.818  15.965   45.991   1.00 83.32  ? 98  GLY   D CA     1 
ATOM   10948 C  C      . GLY   D 2  98  ? 29.489  16.461   44.600   1.00 84.05  ? 98  GLY   D C      1 
ATOM   10949 O  O      . GLY   D 2  98  ? 30.063  17.450   44.134   1.00 81.31  ? 98  GLY   D O      1 
ATOM   10950 N  N      . ASN   D 2  99  ? 28.577  15.758   43.923   1.00 86.09  ? 99  ASN   D N      1 
ATOM   10951 C  CA     . ASN   D 2  99  ? 28.072  16.147   42.601   1.00 82.35  ? 99  ASN   D CA     1 
ATOM   10952 C  C      . ASN   D 2  99  ? 29.187  16.567   41.639   1.00 80.86  ? 99  ASN   D C      1 
ATOM   10953 O  O      . ASN   D 2  99  ? 28.969  17.376   40.736   1.00 78.06  ? 99  ASN   D O      1 
ATOM   10954 C  CB     . ASN   D 2  99  ? 27.031  17.262   42.714   1.00 75.95  ? 99  ASN   D CB     1 
ATOM   10955 C  CG     . ASN   D 2  99  ? 25.655  16.743   43.072   1.00 79.26  ? 99  ASN   D CG     1 
ATOM   10956 O  OD1    . ASN   D 2  99  ? 25.500  15.805   43.867   1.00 72.11  ? 99  ASN   D OD1    1 
ATOM   10957 N  ND2    . ASN   D 2  99  ? 24.640  17.331   42.453   1.00 83.30  ? 99  ASN   D ND2    1 
ATOM   10958 N  N      . ASN   D 2  100 ? 30.386  16.016   41.803   1.00 81.63  ? 100 ASN   D N      1 
ATOM   10959 C  CA     . ASN   D 2  100 ? 31.505  16.300   40.916   1.00 80.81  ? 100 ASN   D CA     1 
ATOM   10960 C  C      . ASN   D 2  100 ? 31.812  15.056   40.089   1.00 86.13  ? 100 ASN   D C      1 
ATOM   10961 O  O      . ASN   D 2  100 ? 31.893  13.946   40.633   1.00 83.60  ? 100 ASN   D O      1 
ATOM   10962 C  CB     . ASN   D 2  100 ? 32.736  16.744   41.714   1.00 84.87  ? 100 ASN   D CB     1 
ATOM   10963 C  CG     . ASN   D 2  100 ? 33.812  17.371   40.839   1.00 86.03  ? 100 ASN   D CG     1 
ATOM   10964 O  OD1    . ASN   D 2  100 ? 34.118  16.873   39.755   1.00 85.52  ? 100 ASN   D OD1    1 
ATOM   10965 N  ND2    . ASN   D 2  100 ? 34.390  18.469   41.311   1.00 87.70  ? 100 ASN   D ND2    1 
ATOM   10966 N  N      . TRP   D 2  101 ? 31.969  15.243   38.774   1.00 85.33  ? 101 TRP   D N      1 
ATOM   10967 C  CA     . TRP   D 2  101 ? 32.267  14.116   37.894   1.00 83.74  ? 101 TRP   D CA     1 
ATOM   10968 C  C      . TRP   D 2  101 ? 33.707  13.642   38.074   1.00 81.64  ? 101 TRP   D C      1 
ATOM   10969 O  O      . TRP   D 2  101 ? 33.963  12.432   38.139   1.00 77.44  ? 101 TRP   D O      1 
ATOM   10970 C  CB     . TRP   D 2  101 ? 31.991  14.496   36.430   1.00 83.39  ? 101 TRP   D CB     1 
ATOM   10971 C  CG     . TRP   D 2  101 ? 31.998  13.313   35.466   1.00 80.00  ? 101 TRP   D CG     1 
ATOM   10972 C  CD1    . TRP   D 2  101 ? 30.999  12.394   35.279   1.00 73.24  ? 101 TRP   D CD1    1 
ATOM   10973 C  CD2    . TRP   D 2  101 ? 33.057  12.938   34.566   1.00 80.42  ? 101 TRP   D CD2    1 
ATOM   10974 N  NE1    . TRP   D 2  101 ? 31.377  11.468   34.334   1.00 70.02  ? 101 TRP   D NE1    1 
ATOM   10975 C  CE2    . TRP   D 2  101 ? 32.630  11.780   33.878   1.00 73.56  ? 101 TRP   D CE2    1 
ATOM   10976 C  CE3    . TRP   D 2  101 ? 34.326  13.463   34.285   1.00 79.60  ? 101 TRP   D CE3    1 
ATOM   10977 C  CZ2    . TRP   D 2  101 ? 33.423  11.144   32.923   1.00 75.16  ? 101 TRP   D CZ2    1 
ATOM   10978 C  CZ3    . TRP   D 2  101 ? 35.115  12.829   33.340   1.00 79.20  ? 101 TRP   D CZ3    1 
ATOM   10979 C  CH2    . TRP   D 2  101 ? 34.658  11.681   32.667   1.00 80.12  ? 101 TRP   D CH2    1 
ATOM   10980 N  N      . ALA   D 2  102 ? 34.659  14.581   38.155   1.00 81.48  ? 102 ALA   D N      1 
ATOM   10981 C  CA     . ALA   D 2  102 ? 36.063  14.205   38.314   1.00 80.54  ? 102 ALA   D CA     1 
ATOM   10982 C  C      . ALA   D 2  102 ? 36.273  13.373   39.571   1.00 81.98  ? 102 ALA   D C      1 
ATOM   10983 O  O      . ALA   D 2  102 ? 37.093  12.448   39.584   1.00 82.15  ? 102 ALA   D O      1 
ATOM   10984 C  CB     . ALA   D 2  102 ? 36.944  15.449   38.360   1.00 83.57  ? 102 ALA   D CB     1 
ATOM   10985 N  N      . LYS   D 2  103 ? 35.541  13.690   40.641   1.00 82.10  ? 103 LYS   D N      1 
ATOM   10986 C  CA     . LYS   D 2  103 ? 35.669  12.931   41.878   1.00 82.72  ? 103 LYS   D CA     1 
ATOM   10987 C  C      . LYS   D 2  103 ? 35.189  11.491   41.709   1.00 82.42  ? 103 LYS   D C      1 
ATOM   10988 O  O      . LYS   D 2  103 ? 35.696  10.587   42.387   1.00 81.77  ? 103 LYS   D O      1 
ATOM   10989 C  CB     . LYS   D 2  103 ? 34.899  13.627   43.004   1.00 88.01  ? 103 LYS   D CB     1 
ATOM   10990 C  CG     . LYS   D 2  103 ? 35.523  14.940   43.463   1.00 84.58  ? 103 LYS   D CG     1 
ATOM   10991 C  CD     . LYS   D 2  103 ? 34.820  15.476   44.694   1.00 84.23  ? 103 LYS   D CD     1 
ATOM   10992 C  CE     . LYS   D 2  103 ? 35.721  16.425   45.468   1.00 87.80  ? 103 LYS   D CE     1 
ATOM   10993 N  NZ     . LYS   D 2  103 ? 34.969  17.579   46.041   1.00 88.09  ? 103 LYS   D NZ     1 
ATOM   10994 N  N      . GLY   D 2  104 ? 34.220  11.255   40.818   1.00 84.29  ? 104 GLY   D N      1 
ATOM   10995 C  CA     . GLY   D 2  104 ? 33.766  9.896    40.568   1.00 78.13  ? 104 GLY   D CA     1 
ATOM   10996 C  C      . GLY   D 2  104 ? 34.622  9.129    39.579   1.00 77.14  ? 104 GLY   D C      1 
ATOM   10997 O  O      . GLY   D 2  104 ? 34.773  7.908    39.708   1.00 68.92  ? 104 GLY   D O      1 
ATOM   10998 N  N      . HIS   D 2  105 ? 35.206  9.826    38.598   1.00 75.61  ? 105 HIS   D N      1 
ATOM   10999 C  CA     . HIS   D 2  105 ? 35.913  9.179    37.497   1.00 76.01  ? 105 HIS   D CA     1 
ATOM   11000 C  C      . HIS   D 2  105 ? 37.405  9.056    37.779   1.00 78.61  ? 105 HIS   D C      1 
ATOM   11001 O  O      . HIS   D 2  105 ? 37.955  7.947    37.791   1.00 81.75  ? 105 HIS   D O      1 
ATOM   11002 C  CB     . HIS   D 2  105 ? 35.671  9.947    36.187   1.00 78.78  ? 105 HIS   D CB     1 
ATOM   11003 C  CG     . HIS   D 2  105 ? 35.812  9.108    34.942   1.00 77.95  ? 105 HIS   D CG     1 
ATOM   11004 N  ND1    . HIS   D 2  105 ? 34.882  8.158    34.578   1.00 75.70  ? 105 HIS   D ND1    1 
ATOM   11005 C  CD2    . HIS   D 2  105 ? 36.730  9.132    33.942   1.00 79.16  ? 105 HIS   D CD2    1 
ATOM   11006 C  CE1    . HIS   D 2  105 ? 35.244  7.601    33.436   1.00 71.90  ? 105 HIS   D CE1    1 
ATOM   11007 N  NE2    . HIS   D 2  105 ? 36.361  8.177    33.026   1.00 74.34  ? 105 HIS   D NE2    1 
ATOM   11008 N  N      . TYR   D 2  106 ? 38.068  10.180   38.033   1.00 82.07  ? 106 TYR   D N      1 
ATOM   11009 C  CA     . TYR   D 2  106 ? 39.525  10.161   38.081   1.00 83.56  ? 106 TYR   D CA     1 
ATOM   11010 C  C      . TYR   D 2  106 ? 40.104  9.947    39.481   1.00 82.40  ? 106 TYR   D C      1 
ATOM   11011 O  O      . TYR   D 2  106 ? 41.080  9.201    39.627   1.00 87.63  ? 106 TYR   D O      1 
ATOM   11012 C  CB     . TYR   D 2  106 ? 40.066  11.447   37.465   1.00 77.17  ? 106 TYR   D CB     1 
ATOM   11013 C  CG     . TYR   D 2  106 ? 39.812  11.487   35.988   1.00 77.53  ? 106 TYR   D CG     1 
ATOM   11014 C  CD1    . TYR   D 2  106 ? 39.096  12.522   35.413   1.00 77.92  ? 106 TYR   D CD1    1 
ATOM   11015 C  CD2    . TYR   D 2  106 ? 40.272  10.463   35.167   1.00 79.58  ? 106 TYR   D CD2    1 
ATOM   11016 C  CE1    . TYR   D 2  106 ? 38.860  12.551   34.052   1.00 82.07  ? 106 TYR   D CE1    1 
ATOM   11017 C  CE2    . TYR   D 2  106 ? 40.048  10.476   33.807   1.00 75.02  ? 106 TYR   D CE2    1 
ATOM   11018 C  CZ     . TYR   D 2  106 ? 39.340  11.522   33.249   1.00 82.33  ? 106 TYR   D CZ     1 
ATOM   11019 O  OH     . TYR   D 2  106 ? 39.106  11.541   31.887   1.00 85.72  ? 106 TYR   D OH     1 
ATOM   11020 N  N      . THR   D 2  107 ? 39.524  10.557   40.523   1.00 81.04  ? 107 THR   D N      1 
ATOM   11021 C  CA     . THR   D 2  107 ? 40.159  10.574   41.830   1.00 78.71  ? 107 THR   D CA     1 
ATOM   11022 C  C      . THR   D 2  107 ? 39.380  9.657    42.762   1.00 78.45  ? 107 THR   D C      1 
ATOM   11023 O  O      . THR   D 2  107 ? 39.630  8.438    42.769   1.00 76.85  ? 107 THR   D O      1 
ATOM   11024 C  CB     . THR   D 2  107 ? 40.263  12.006   42.366   1.00 77.34  ? 107 THR   D CB     1 
ATOM   11025 O  OG1    . THR   D 2  107 ? 39.066  12.328   43.079   1.00 79.99  ? 107 THR   D OG1    1 
ATOM   11026 C  CG2    . THR   D 2  107 ? 40.449  13.003   41.221   1.00 81.61  ? 107 THR   D CG2    1 
ATOM   11027 N  N      . GLU   D 2  108 ? 38.449  10.176   43.567   1.00 77.93  ? 108 GLU   D N      1 
ATOM   11028 C  CA     . GLU   D 2  108 ? 37.894  9.402    44.675   1.00 79.48  ? 108 GLU   D CA     1 
ATOM   11029 C  C      . GLU   D 2  108 ? 37.236  8.116    44.195   1.00 84.90  ? 108 GLU   D C      1 
ATOM   11030 O  O      . GLU   D 2  108 ? 37.299  7.090    44.882   1.00 83.15  ? 108 GLU   D O      1 
ATOM   11031 C  CB     . GLU   D 2  108 ? 36.889  10.245   45.455   1.00 86.06  ? 108 GLU   D CB     1 
ATOM   11032 C  CG     . GLU   D 2  108 ? 37.330  11.666   45.726   1.00 88.47  ? 108 GLU   D CG     1 
ATOM   11033 C  CD     . GLU   D 2  108 ? 36.839  12.156   47.066   1.00 96.75  ? 108 GLU   D CD     1 
ATOM   11034 O  OE1    . GLU   D 2  108 ? 36.646  13.383   47.219   1.00 100.64 ? 108 GLU   D OE1    1 
ATOM   11035 O  OE2    . GLU   D 2  108 ? 36.639  11.305   47.963   1.00 98.73  ? 108 GLU   D OE2    1 
ATOM   11036 N  N      . GLY   D 2  109 ? 36.573  8.158    43.033   1.00 86.30  ? 109 GLY   D N      1 
ATOM   11037 C  CA     . GLY   D 2  109 ? 36.016  6.939    42.466   1.00 79.54  ? 109 GLY   D CA     1 
ATOM   11038 C  C      . GLY   D 2  109 ? 37.088  5.925    42.116   1.00 79.02  ? 109 GLY   D C      1 
ATOM   11039 O  O      . GLY   D 2  109 ? 36.929  4.728    42.376   1.00 73.87  ? 109 GLY   D O      1 
ATOM   11040 N  N      . ALA   D 2  110 ? 38.202  6.395    41.530   1.00 81.53  ? 110 ALA   D N      1 
ATOM   11041 C  CA     . ALA   D 2  110 ? 39.348  5.529    41.262   1.00 76.82  ? 110 ALA   D CA     1 
ATOM   11042 C  C      . ALA   D 2  110 ? 39.742  4.730    42.497   1.00 78.51  ? 110 ALA   D C      1 
ATOM   11043 O  O      . ALA   D 2  110 ? 40.029  3.530    42.409   1.00 77.54  ? 110 ALA   D O      1 
ATOM   11044 C  CB     . ALA   D 2  110 ? 40.526  6.365    40.766   1.00 68.46  ? 110 ALA   D CB     1 
ATOM   11045 N  N      . GLU   D 2  111 ? 39.746  5.377    43.664   1.00 79.30  ? 111 GLU   D N      1 
ATOM   11046 C  CA     . GLU   D 2  111 ? 40.154  4.701    44.886   1.00 79.71  ? 111 GLU   D CA     1 
ATOM   11047 C  C      . GLU   D 2  111 ? 39.184  3.597    45.298   1.00 82.97  ? 111 GLU   D C      1 
ATOM   11048 O  O      . GLU   D 2  111 ? 39.597  2.632    45.955   1.00 90.26  ? 111 GLU   D O      1 
ATOM   11049 C  CB     . GLU   D 2  111 ? 40.320  5.727    46.001   1.00 76.17  ? 111 GLU   D CB     1 
ATOM   11050 C  CG     . GLU   D 2  111 ? 41.250  6.860    45.607   1.00 80.88  ? 111 GLU   D CG     1 
ATOM   11051 C  CD     . GLU   D 2  111 ? 41.079  8.085    46.483   1.00 87.56  ? 111 GLU   D CD     1 
ATOM   11052 O  OE1    . GLU   D 2  111 ? 40.234  8.041    47.404   1.00 89.88  ? 111 GLU   D OE1    1 
ATOM   11053 O  OE2    . GLU   D 2  111 ? 41.785  9.093    46.248   1.00 83.93  ? 111 GLU   D OE2    1 
ATOM   11054 N  N      . LEU   D 2  112 ? 37.914  3.692    44.925   1.00 78.01  ? 112 LEU   D N      1 
ATOM   11055 C  CA     . LEU   D 2  112 ? 36.982  2.638    45.283   1.00 75.50  ? 112 LEU   D CA     1 
ATOM   11056 C  C      . LEU   D 2  112 ? 36.733  1.652    44.148   1.00 75.25  ? 112 LEU   D C      1 
ATOM   11057 O  O      . LEU   D 2  112 ? 36.180  0.579    44.405   1.00 77.84  ? 112 LEU   D O      1 
ATOM   11058 C  CB     . LEU   D 2  112 ? 35.656  3.250    45.767   1.00 72.77  ? 112 LEU   D CB     1 
ATOM   11059 C  CG     . LEU   D 2  112 ? 34.694  2.348    46.553   1.00 78.08  ? 112 LEU   D CG     1 
ATOM   11060 C  CD1    . LEU   D 2  112 ? 35.195  2.100    47.954   1.00 82.79  ? 112 LEU   D CD1    1 
ATOM   11061 C  CD2    . LEU   D 2  112 ? 33.309  2.967    46.610   1.00 77.61  ? 112 LEU   D CD2    1 
ATOM   11062 N  N      . VAL   D 2  113 ? 37.165  1.962    42.918   1.00 73.93  ? 113 VAL   D N      1 
ATOM   11063 C  CA     . VAL   D 2  113 ? 36.803  1.135    41.765   1.00 72.32  ? 113 VAL   D CA     1 
ATOM   11064 C  C      . VAL   D 2  113 ? 37.289  -0.297   41.954   1.00 74.14  ? 113 VAL   D C      1 
ATOM   11065 O  O      . VAL   D 2  113 ? 36.502  -1.250   41.869   1.00 72.76  ? 113 VAL   D O      1 
ATOM   11066 C  CB     . VAL   D 2  113 ? 37.333  1.754    40.456   1.00 70.75  ? 113 VAL   D CB     1 
ATOM   11067 C  CG1    . VAL   D 2  113 ? 38.781  1.366    40.180   1.00 70.29  ? 113 VAL   D CG1    1 
ATOM   11068 C  CG2    . VAL   D 2  113 ? 36.441  1.347    39.292   1.00 65.91  ? 113 VAL   D CG2    1 
ATOM   11069 N  N      . ASP   D 2  114 ? 38.589  -0.475   42.228   1.00 73.53  ? 114 ASP   D N      1 
ATOM   11070 C  CA     . ASP   D 2  114 ? 39.140  -1.821   42.300   1.00 72.70  ? 114 ASP   D CA     1 
ATOM   11071 C  C      . ASP   D 2  114 ? 38.449  -2.640   43.382   1.00 76.28  ? 114 ASP   D C      1 
ATOM   11072 O  O      . ASP   D 2  114 ? 38.422  -3.872   43.294   1.00 76.27  ? 114 ASP   D O      1 
ATOM   11073 C  CB     . ASP   D 2  114 ? 40.654  -1.762   42.514   1.00 63.75  ? 114 ASP   D CB     1 
ATOM   11074 C  CG     . ASP   D 2  114 ? 41.374  -0.991   41.403   1.00 78.28  ? 114 ASP   D CG     1 
ATOM   11075 O  OD1    . ASP   D 2  114 ? 40.807  -0.837   40.299   1.00 77.87  ? 114 ASP   D OD1    1 
ATOM   11076 O  OD2    . ASP   D 2  114 ? 42.516  -0.532   41.623   1.00 83.10  ? 114 ASP   D OD2    1 
ATOM   11077 N  N      . SER   D 2  115 ? 37.835  -1.978   44.366   1.00 76.32  ? 115 SER   D N      1 
ATOM   11078 C  CA     . SER   D 2  115 ? 37.077  -2.690   45.392   1.00 79.26  ? 115 SER   D CA     1 
ATOM   11079 C  C      . SER   D 2  115 ? 35.721  -3.151   44.867   1.00 74.36  ? 115 SER   D C      1 
ATOM   11080 O  O      . SER   D 2  115 ? 35.172  -4.147   45.359   1.00 66.76  ? 115 SER   D O      1 
ATOM   11081 C  CB     . SER   D 2  115 ? 36.918  -1.793   46.623   1.00 77.67  ? 115 SER   D CB     1 
ATOM   11082 O  OG     . SER   D 2  115 ? 37.861  -0.725   46.561   1.00 83.02  ? 115 SER   D OG     1 
ATOM   11083 N  N      . VAL   D 2  116 ? 35.172  -2.437   43.876   1.00 76.46  ? 116 VAL   D N      1 
ATOM   11084 C  CA     . VAL   D 2  116 ? 33.999  -2.917   43.146   1.00 76.35  ? 116 VAL   D CA     1 
ATOM   11085 C  C      . VAL   D 2  116 ? 34.397  -4.006   42.156   1.00 70.65  ? 116 VAL   D C      1 
ATOM   11086 O  O      . VAL   D 2  116 ? 33.843  -5.111   42.164   1.00 61.00  ? 116 VAL   D O      1 
ATOM   11087 C  CB     . VAL   D 2  116 ? 33.293  -1.753   42.427   1.00 76.58  ? 116 VAL   D CB     1 
ATOM   11088 C  CG1    . VAL   D 2  116 ? 31.851  -2.132   42.122   1.00 70.73  ? 116 VAL   D CG1    1 
ATOM   11089 C  CG2    . VAL   D 2  116 ? 33.371  -0.463   43.257   1.00 75.31  ? 116 VAL   D CG2    1 
ATOM   11090 N  N      . LEU   D 2  117 ? 35.384  -3.713   41.306   1.00 65.79  ? 117 LEU   D N      1 
ATOM   11091 C  CA     . LEU   D 2  117 ? 35.845  -4.693   40.333   1.00 70.69  ? 117 LEU   D CA     1 
ATOM   11092 C  C      . LEU   D 2  117 ? 36.007  -6.067   40.960   1.00 66.75  ? 117 LEU   D C      1 
ATOM   11093 O  O      . LEU   D 2  117 ? 35.741  -7.084   40.311   1.00 69.50  ? 117 LEU   D O      1 
ATOM   11094 C  CB     . LEU   D 2  117 ? 37.149  -4.215   39.698   1.00 68.16  ? 117 LEU   D CB     1 
ATOM   11095 C  CG     . LEU   D 2  117 ? 36.910  -3.033   38.762   1.00 66.14  ? 117 LEU   D CG     1 
ATOM   11096 C  CD1    . LEU   D 2  117 ? 38.165  -2.634   38.021   1.00 66.96  ? 117 LEU   D CD1    1 
ATOM   11097 C  CD2    . LEU   D 2  117 ? 35.774  -3.372   37.791   1.00 67.73  ? 117 LEU   D CD2    1 
ATOM   11098 N  N      . ASP   D 2  118 ? 36.386  -6.122   42.231   1.00 66.65  ? 118 ASP   D N      1 
ATOM   11099 C  CA     . ASP   D 2  118 ? 36.588  -7.417   42.870   1.00 71.33  ? 118 ASP   D CA     1 
ATOM   11100 C  C      . ASP   D 2  118 ? 35.269  -8.153   43.070   1.00 69.69  ? 118 ASP   D C      1 
ATOM   11101 O  O      . ASP   D 2  118 ? 35.195  -9.373   42.856   1.00 68.11  ? 118 ASP   D O      1 
ATOM   11102 C  CB     . ASP   D 2  118 ? 37.314  -7.238   44.200   1.00 75.91  ? 118 ASP   D CB     1 
ATOM   11103 C  CG     . ASP   D 2  118 ? 38.830  -7.194   44.040   1.00 81.63  ? 118 ASP   D CG     1 
ATOM   11104 O  OD1    . ASP   D 2  118 ? 39.334  -6.414   43.190   1.00 80.77  ? 118 ASP   D OD1    1 
ATOM   11105 O  OD2    . ASP   D 2  118 ? 39.513  -7.952   44.760   1.00 85.72  ? 118 ASP   D OD2    1 
ATOM   11106 N  N      . VAL   D 2  119 ? 34.218  -7.431   43.475   1.00 66.57  ? 119 VAL   D N      1 
ATOM   11107 C  CA     . VAL   D 2  119 ? 32.901  -8.045   43.625   1.00 65.68  ? 119 VAL   D CA     1 
ATOM   11108 C  C      . VAL   D 2  119 ? 32.337  -8.435   42.267   1.00 67.58  ? 119 VAL   D C      1 
ATOM   11109 O  O      . VAL   D 2  119 ? 31.709  -9.493   42.124   1.00 66.54  ? 119 VAL   D O      1 
ATOM   11110 C  CB     . VAL   D 2  119 ? 31.940  -7.102   44.374   1.00 72.08  ? 119 VAL   D CB     1 
ATOM   11111 C  CG1    . VAL   D 2  119 ? 30.770  -7.904   45.008   1.00 63.95  ? 119 VAL   D CG1    1 
ATOM   11112 C  CG2    . VAL   D 2  119 ? 32.702  -6.250   45.401   1.00 68.24  ? 119 VAL   D CG2    1 
ATOM   11113 N  N      . VAL   D 2  120 ? 32.519  -7.576   41.256   1.00 62.62  ? 120 VAL   D N      1 
ATOM   11114 C  CA     . VAL   D 2  120 ? 32.185  -7.962   39.887   1.00 61.16  ? 120 VAL   D CA     1 
ATOM   11115 C  C      . VAL   D 2  120 ? 32.741  -9.354   39.590   1.00 66.20  ? 120 VAL   D C      1 
ATOM   11116 O  O      . VAL   D 2  120 ? 31.989  -10.307  39.348   1.00 63.33  ? 120 VAL   D O      1 
ATOM   11117 C  CB     . VAL   D 2  120 ? 32.701  -6.916   38.883   1.00 65.53  ? 120 VAL   D CB     1 
ATOM   11118 C  CG1    . VAL   D 2  120 ? 32.502  -7.418   37.473   1.00 66.24  ? 120 VAL   D CG1    1 
ATOM   11119 C  CG2    . VAL   D 2  120 ? 31.976  -5.570   39.052   1.00 57.61  ? 120 VAL   D CG2    1 
ATOM   11120 N  N      . ARG   D 2  121 ? 34.072  -9.506   39.662   1.00 66.65  ? 121 ARG   D N      1 
ATOM   11121 C  CA     . ARG   D 2  121 ? 34.694  -10.781  39.297   1.00 66.46  ? 121 ARG   D CA     1 
ATOM   11122 C  C      . ARG   D 2  121 ? 34.110  -11.940  40.094   1.00 66.18  ? 121 ARG   D C      1 
ATOM   11123 O  O      . ARG   D 2  121 ? 33.756  -12.979  39.528   1.00 69.93  ? 121 ARG   D O      1 
ATOM   11124 C  CB     . ARG   D 2  121 ? 36.206  -10.724  39.490   1.00 63.66  ? 121 ARG   D CB     1 
ATOM   11125 C  CG     . ARG   D 2  121 ? 36.896  -9.762   38.559   1.00 71.40  ? 121 ARG   D CG     1 
ATOM   11126 C  CD     . ARG   D 2  121 ? 38.390  -9.835   38.713   1.00 66.23  ? 121 ARG   D CD     1 
ATOM   11127 N  NE     . ARG   D 2  121 ? 39.005  -8.542   38.432   1.00 75.60  ? 121 ARG   D NE     1 
ATOM   11128 C  CZ     . ARG   D 2  121 ? 39.334  -7.655   39.365   1.00 78.23  ? 121 ARG   D CZ     1 
ATOM   11129 N  NH1    . ARG   D 2  121 ? 39.077  -7.875   40.646   1.00 75.44  ? 121 ARG   D NH1    1 
ATOM   11130 N  NH2    . ARG   D 2  121 ? 39.937  -6.521   39.006   1.00 68.67  ? 121 ARG   D NH2    1 
ATOM   11131 N  N      . LYS   D 2  122 ? 34.025  -11.797  41.417   1.00 61.56  ? 122 LYS   D N      1 
ATOM   11132 C  CA     . LYS   D 2  122 ? 33.455  -12.876  42.215   1.00 65.01  ? 122 LYS   D CA     1 
ATOM   11133 C  C      . LYS   D 2  122 ? 32.098  -13.285  41.659   1.00 67.89  ? 122 LYS   D C      1 
ATOM   11134 O  O      . LYS   D 2  122 ? 31.787  -14.480  41.555   1.00 69.88  ? 122 LYS   D O      1 
ATOM   11135 C  CB     . LYS   D 2  122 ? 33.343  -12.447  43.683   1.00 64.45  ? 122 LYS   D CB     1 
ATOM   11136 C  CG     . LYS   D 2  122 ? 32.564  -13.398  44.582   1.00 63.50  ? 122 LYS   D CG     1 
ATOM   11137 C  CD     . LYS   D 2  122 ? 33.472  -14.340  45.368   1.00 74.27  ? 122 LYS   D CD     1 
ATOM   11138 C  CE     . LYS   D 2  122 ? 32.794  -14.792  46.663   1.00 74.95  ? 122 LYS   D CE     1 
ATOM   11139 N  NZ     . LYS   D 2  122 ? 32.696  -16.279  46.778   1.00 74.08  ? 122 LYS   D NZ     1 
ATOM   11140 N  N      . GLU   D 2  123 ? 31.285  -12.301  41.266   1.00 65.04  ? 123 GLU   D N      1 
ATOM   11141 C  CA     . GLU   D 2  123 ? 29.963  -12.616  40.744   1.00 67.24  ? 123 GLU   D CA     1 
ATOM   11142 C  C      . GLU   D 2  123 ? 30.061  -13.135  39.317   1.00 66.74  ? 123 GLU   D C      1 
ATOM   11143 O  O      . GLU   D 2  123 ? 29.362  -14.087  38.945   1.00 62.79  ? 123 GLU   D O      1 
ATOM   11144 C  CB     . GLU   D 2  123 ? 29.047  -11.387  40.820   1.00 65.95  ? 123 GLU   D CB     1 
ATOM   11145 C  CG     . GLU   D 2  123 ? 28.614  -10.978  42.232   1.00 62.29  ? 123 GLU   D CG     1 
ATOM   11146 C  CD     . GLU   D 2  123 ? 27.367  -11.718  42.718   1.00 69.61  ? 123 GLU   D CD     1 
ATOM   11147 O  OE1    . GLU   D 2  123 ? 26.802  -12.517  41.936   1.00 69.72  ? 123 GLU   D OE1    1 
ATOM   11148 O  OE2    . GLU   D 2  123 ? 26.963  -11.522  43.891   1.00 67.24  ? 123 GLU   D OE2    1 
ATOM   11149 N  N      . SER   D 2  124 ? 30.947  -12.535  38.518   1.00 64.22  ? 124 SER   D N      1 
ATOM   11150 C  CA     . SER   D 2  124 ? 31.090  -12.931  37.121   1.00 65.05  ? 124 SER   D CA     1 
ATOM   11151 C  C      . SER   D 2  124 ? 31.593  -14.365  36.999   1.00 63.84  ? 124 SER   D C      1 
ATOM   11152 O  O      . SER   D 2  124 ? 31.062  -15.153  36.213   1.00 64.57  ? 124 SER   D O      1 
ATOM   11153 C  CB     . SER   D 2  124 ? 32.033  -11.967  36.395   1.00 64.60  ? 124 SER   D CB     1 
ATOM   11154 O  OG     . SER   D 2  124 ? 31.345  -10.841  35.866   1.00 55.22  ? 124 SER   D OG     1 
ATOM   11155 N  N      . GLU   D 2  125 ? 32.629  -14.723  37.757   1.00 67.01  ? 125 GLU   D N      1 
ATOM   11156 C  CA     . GLU   D 2  125 ? 33.194  -16.060  37.622   1.00 70.82  ? 125 GLU   D CA     1 
ATOM   11157 C  C      . GLU   D 2  125 ? 32.253  -17.157  38.123   1.00 73.58  ? 125 GLU   D C      1 
ATOM   11158 O  O      . GLU   D 2  125 ? 32.495  -18.338  37.851   1.00 72.26  ? 125 GLU   D O      1 
ATOM   11159 C  CB     . GLU   D 2  125 ? 34.535  -16.127  38.350   1.00 69.12  ? 125 GLU   D CB     1 
ATOM   11160 C  CG     . GLU   D 2  125 ? 34.423  -16.758  39.717   1.00 79.35  ? 125 GLU   D CG     1 
ATOM   11161 C  CD     . GLU   D 2  125 ? 35.752  -16.859  40.429   1.00 84.43  ? 125 GLU   D CD     1 
ATOM   11162 O  OE1    . GLU   D 2  125 ? 36.768  -17.177  39.763   1.00 85.80  ? 125 GLU   D OE1    1 
ATOM   11163 O  OE2    . GLU   D 2  125 ? 35.774  -16.619  41.658   1.00 82.31  ? 125 GLU   D OE2    1 
ATOM   11164 N  N      . SER   D 2  126 ? 31.190  -16.804  38.837   1.00 74.00  ? 126 SER   D N      1 
ATOM   11165 C  CA     . SER   D 2  126 ? 30.172  -17.763  39.251   1.00 74.49  ? 126 SER   D CA     1 
ATOM   11166 C  C      . SER   D 2  126 ? 29.168  -18.085  38.146   1.00 77.14  ? 126 SER   D C      1 
ATOM   11167 O  O      . SER   D 2  126 ? 28.235  -18.868  38.383   1.00 81.66  ? 126 SER   D O      1 
ATOM   11168 C  CB     . SER   D 2  126 ? 29.433  -17.223  40.487   1.00 79.73  ? 126 SER   D CB     1 
ATOM   11169 O  OG     . SER   D 2  126 ? 28.127  -17.785  40.615   1.00 85.05  ? 126 SER   D OG     1 
ATOM   11170 N  N      . CYS   D 2  127 ? 29.323  -17.503  36.960   1.00 72.15  ? 127 CYS   D N      1 
ATOM   11171 C  CA     . CYS   D 2  127 ? 28.303  -17.563  35.923   1.00 71.08  ? 127 CYS   D CA     1 
ATOM   11172 C  C      . CYS   D 2  127 ? 28.612  -18.683  34.941   1.00 72.51  ? 127 CYS   D C      1 
ATOM   11173 O  O      . CYS   D 2  127 ? 29.701  -18.722  34.359   1.00 71.03  ? 127 CYS   D O      1 
ATOM   11174 C  CB     . CYS   D 2  127 ? 28.213  -16.233  35.171   1.00 67.51  ? 127 CYS   D CB     1 
ATOM   11175 S  SG     . CYS   D 2  127 ? 27.509  -14.867  36.112   1.00 59.84  ? 127 CYS   D SG     1 
ATOM   11176 N  N      . ASP   D 2  128 ? 27.645  -19.577  34.738   1.00 69.83  ? 128 ASP   D N      1 
ATOM   11177 C  CA     . ASP   D 2  128 ? 27.770  -20.518  33.637   1.00 65.91  ? 128 ASP   D CA     1 
ATOM   11178 C  C      . ASP   D 2  128 ? 27.950  -19.790  32.308   1.00 67.44  ? 128 ASP   D C      1 
ATOM   11179 O  O      . ASP   D 2  128 ? 28.807  -20.171  31.506   1.00 72.23  ? 128 ASP   D O      1 
ATOM   11180 C  CB     . ASP   D 2  128 ? 26.559  -21.440  33.578   1.00 73.02  ? 128 ASP   D CB     1 
ATOM   11181 C  CG     . ASP   D 2  128 ? 26.674  -22.467  32.463   1.00 85.12  ? 128 ASP   D CG     1 
ATOM   11182 O  OD1    . ASP   D 2  128 ? 25.628  -22.840  31.876   1.00 87.52  ? 128 ASP   D OD1    1 
ATOM   11183 O  OD2    . ASP   D 2  128 ? 27.817  -22.904  32.176   1.00 78.35  ? 128 ASP   D OD2    1 
ATOM   11184 N  N      . CYS   D 2  129 ? 27.164  -18.733  32.055   1.00 66.36  ? 129 CYS   D N      1 
ATOM   11185 C  CA     . CYS   D 2  129 ? 27.239  -18.053  30.755   1.00 63.06  ? 129 CYS   D CA     1 
ATOM   11186 C  C      . CYS   D 2  129 ? 26.845  -16.583  30.909   1.00 62.60  ? 129 CYS   D C      1 
ATOM   11187 O  O      . CYS   D 2  129 ? 25.672  -16.223  30.798   1.00 68.23  ? 129 CYS   D O      1 
ATOM   11188 C  CB     . CYS   D 2  129 ? 26.363  -18.745  29.728   1.00 68.00  ? 129 CYS   D CB     1 
ATOM   11189 S  SG     . CYS   D 2  129 ? 26.825  -18.292  28.067   1.00 64.00  ? 129 CYS   D SG     1 
ATOM   11190 N  N      . LEU   D 2  130 ? 27.844  -15.734  31.097   1.00 60.29  ? 130 LEU   D N      1 
ATOM   11191 C  CA     . LEU   D 2  130 ? 27.598  -14.356  31.503   1.00 61.25  ? 130 LEU   D CA     1 
ATOM   11192 C  C      . LEU   D 2  130 ? 27.127  -13.521  30.306   1.00 56.95  ? 130 LEU   D C      1 
ATOM   11193 O  O      . LEU   D 2  130 ? 27.898  -13.255  29.382   1.00 56.99  ? 130 LEU   D O      1 
ATOM   11194 C  CB     . LEU   D 2  130 ? 28.865  -13.794  32.145   1.00 53.25  ? 130 LEU   D CB     1 
ATOM   11195 C  CG     . LEU   D 2  130 ? 28.918  -12.309  32.480   1.00 55.09  ? 130 LEU   D CG     1 
ATOM   11196 C  CD1    . LEU   D 2  130 ? 28.075  -12.013  33.688   1.00 51.70  ? 130 LEU   D CD1    1 
ATOM   11197 C  CD2    . LEU   D 2  130 ? 30.357  -11.843  32.678   1.00 50.68  ? 130 LEU   D CD2    1 
ATOM   11198 N  N      . GLN   D 2  131 ? 25.855  -13.103  30.323   1.00 56.24  ? 131 GLN   D N      1 
ATOM   11199 C  CA     . GLN   D 2  131 ? 25.372  -12.103  29.366   1.00 57.09  ? 131 GLN   D CA     1 
ATOM   11200 C  C      . GLN   D 2  131 ? 26.205  -10.824  29.432   1.00 54.75  ? 131 GLN   D C      1 
ATOM   11201 O  O      . GLN   D 2  131 ? 26.687  -10.307  28.417   1.00 50.54  ? 131 GLN   D O      1 
ATOM   11202 C  CB     . GLN   D 2  131 ? 23.913  -11.748  29.659   1.00 52.91  ? 131 GLN   D CB     1 
ATOM   11203 C  CG     . GLN   D 2  131 ? 22.891  -12.855  29.545   1.00 55.26  ? 131 GLN   D CG     1 
ATOM   11204 C  CD     . GLN   D 2  131 ? 21.483  -12.312  29.361   1.00 52.41  ? 131 GLN   D CD     1 
ATOM   11205 O  OE1    . GLN   D 2  131 ? 21.264  -11.362  28.614   1.00 46.13  ? 131 GLN   D OE1    1 
ATOM   11206 N  NE2    . GLN   D 2  131 ? 20.532  -12.889  30.070   1.00 56.01  ? 131 GLN   D NE2    1 
ATOM   11207 N  N      . GLY   D 2  132 ? 26.359  -10.290  30.609   1.00 53.60  ? 132 GLY   D N      1 
ATOM   11208 C  CA     . GLY   D 2  132 ? 26.908  -8.975   30.723   1.00 53.78  ? 132 GLY   D CA     1 
ATOM   11209 C  C      . GLY   D 2  132 ? 26.305  -8.296   31.933   1.00 55.16  ? 132 GLY   D C      1 
ATOM   11210 O  O      . GLY   D 2  132 ? 25.908  -8.956   32.889   1.00 57.78  ? 132 GLY   D O      1 
ATOM   11211 N  N      . PHE   D 2  133 ? 26.198  -6.981   31.836   1.00 59.01  ? 133 PHE   D N      1 
ATOM   11212 C  CA     . PHE   D 2  133 ? 25.876  -6.145   32.979   1.00 65.56  ? 133 PHE   D CA     1 
ATOM   11213 C  C      . PHE   D 2  133 ? 24.832  -5.103   32.598   1.00 57.90  ? 133 PHE   D C      1 
ATOM   11214 O  O      . PHE   D 2  133 ? 24.743  -4.679   31.441   1.00 61.10  ? 133 PHE   D O      1 
ATOM   11215 C  CB     . PHE   D 2  133 ? 27.150  -5.451   33.494   1.00 63.60  ? 133 PHE   D CB     1 
ATOM   11216 C  CG     . PHE   D 2  133 ? 28.362  -6.327   33.452   1.00 62.50  ? 133 PHE   D CG     1 
ATOM   11217 C  CD1    . PHE   D 2  133 ? 28.562  -7.298   34.424   1.00 63.04  ? 133 PHE   D CD1    1 
ATOM   11218 C  CD2    . PHE   D 2  133 ? 29.283  -6.206   32.437   1.00 61.25  ? 133 PHE   D CD2    1 
ATOM   11219 C  CE1    . PHE   D 2  133 ? 29.666  -8.126   34.393   1.00 57.30  ? 133 PHE   D CE1    1 
ATOM   11220 C  CE2    . PHE   D 2  133 ? 30.403  -7.036   32.405   1.00 63.45  ? 133 PHE   D CE2    1 
ATOM   11221 C  CZ     . PHE   D 2  133 ? 30.589  -7.996   33.383   1.00 56.21  ? 133 PHE   D CZ     1 
ATOM   11222 N  N      . GLN   D 2  134 ? 24.042  -4.691   33.580   1.00 52.80  ? 134 GLN   D N      1 
ATOM   11223 C  CA     . GLN   D 2  134 ? 23.234  -3.487   33.460   1.00 53.78  ? 134 GLN   D CA     1 
ATOM   11224 C  C      . GLN   D 2  134 ? 23.546  -2.587   34.641   1.00 60.07  ? 134 GLN   D C      1 
ATOM   11225 O  O      . GLN   D 2  134 ? 23.503  -3.032   35.792   1.00 64.22  ? 134 GLN   D O      1 
ATOM   11226 C  CB     . GLN   D 2  134 ? 21.735  -3.786   33.402   1.00 54.39  ? 134 GLN   D CB     1 
ATOM   11227 C  CG     . GLN   D 2  134 ? 21.211  -4.571   34.563   1.00 56.13  ? 134 GLN   D CG     1 
ATOM   11228 C  CD     . GLN   D 2  134 ? 19.742  -4.890   34.425   1.00 61.75  ? 134 GLN   D CD     1 
ATOM   11229 O  OE1    . GLN   D 2  134 ? 19.199  -4.875   33.321   1.00 64.94  ? 134 GLN   D OE1    1 
ATOM   11230 N  NE2    . GLN   D 2  134 ? 19.090  -5.212   35.545   1.00 60.71  ? 134 GLN   D NE2    1 
ATOM   11231 N  N      . LEU   D 2  135 ? 23.878  -1.335   34.355   1.00 56.32  ? 135 LEU   D N      1 
ATOM   11232 C  CA     . LEU   D 2  135 ? 24.200  -0.359   35.383   1.00 57.84  ? 135 LEU   D CA     1 
ATOM   11233 C  C      . LEU   D 2  135 ? 23.031  0.601    35.524   1.00 64.52  ? 135 LEU   D C      1 
ATOM   11234 O  O      . LEU   D 2  135 ? 22.619  1.223    34.537   1.00 66.81  ? 135 LEU   D O      1 
ATOM   11235 C  CB     . LEU   D 2  135 ? 25.472  0.405    35.025   1.00 58.57  ? 135 LEU   D CB     1 
ATOM   11236 C  CG     . LEU   D 2  135 ? 25.686  1.655    35.873   1.00 60.77  ? 135 LEU   D CG     1 
ATOM   11237 C  CD1    . LEU   D 2  135 ? 26.212  1.260    37.244   1.00 59.26  ? 135 LEU   D CD1    1 
ATOM   11238 C  CD2    . LEU   D 2  135 ? 26.620  2.621    35.163   1.00 58.69  ? 135 LEU   D CD2    1 
ATOM   11239 N  N      . THR   D 2  136 ? 22.497  0.721    36.740   1.00 64.98  ? 136 THR   D N      1 
ATOM   11240 C  CA     . THR   D 2  136 ? 21.513  1.749    37.079   1.00 59.88  ? 136 THR   D CA     1 
ATOM   11241 C  C      . THR   D 2  136 ? 22.239  2.897    37.752   1.00 57.25  ? 136 THR   D C      1 
ATOM   11242 O  O      . THR   D 2  136 ? 22.872  2.700    38.788   1.00 62.54  ? 136 THR   D O      1 
ATOM   11243 C  CB     . THR   D 2  136 ? 20.446  1.206    38.017   1.00 58.82  ? 136 THR   D CB     1 
ATOM   11244 O  OG1    . THR   D 2  136 ? 21.028  0.185    38.831   1.00 65.70  ? 136 THR   D OG1    1 
ATOM   11245 C  CG2    . THR   D 2  136 ? 19.295  0.638    37.241   1.00 59.13  ? 136 THR   D CG2    1 
ATOM   11246 N  N      . HIS   D 2  137 ? 22.150  4.083    37.174   1.00 57.24  ? 137 HIS   D N      1 
ATOM   11247 C  CA     . HIS   D 2  137 ? 22.860  5.232    37.710   1.00 57.44  ? 137 HIS   D CA     1 
ATOM   11248 C  C      . HIS   D 2  137 ? 22.161  6.497    37.221   1.00 66.40  ? 137 HIS   D C      1 
ATOM   11249 O  O      . HIS   D 2  137 ? 21.094  6.442    36.603   1.00 67.66  ? 137 HIS   D O      1 
ATOM   11250 C  CB     . HIS   D 2  137 ? 24.329  5.178    37.304   1.00 56.19  ? 137 HIS   D CB     1 
ATOM   11251 C  CG     . HIS   D 2  137 ? 24.569  5.460    35.853   1.00 60.67  ? 137 HIS   D CG     1 
ATOM   11252 N  ND1    . HIS   D 2  137 ? 25.667  6.158    35.404   1.00 61.42  ? 137 HIS   D ND1    1 
ATOM   11253 C  CD2    . HIS   D 2  137 ? 23.854  5.139    34.750   1.00 63.23  ? 137 HIS   D CD2    1 
ATOM   11254 C  CE1    . HIS   D 2  137 ? 25.621  6.255    34.088   1.00 61.88  ? 137 HIS   D CE1    1 
ATOM   11255 N  NE2    . HIS   D 2  137 ? 24.529  5.647    33.665   1.00 63.85  ? 137 HIS   D NE2    1 
ATOM   11256 N  N      . SER   D 2  138 ? 22.762  7.643    37.519   1.00 63.31  ? 138 SER   D N      1 
ATOM   11257 C  CA     . SER   D 2  138 ? 22.321  8.926    37.007   1.00 59.39  ? 138 SER   D CA     1 
ATOM   11258 C  C      . SER   D 2  138 ? 23.490  9.561    36.267   1.00 63.74  ? 138 SER   D C      1 
ATOM   11259 O  O      . SER   D 2  138 ? 24.651  9.232    36.517   1.00 67.67  ? 138 SER   D O      1 
ATOM   11260 C  CB     . SER   D 2  138 ? 21.830  9.840    38.140   1.00 66.51  ? 138 SER   D CB     1 
ATOM   11261 O  OG     . SER   D 2  138 ? 22.893  10.169   39.028   1.00 76.36  ? 138 SER   D OG     1 
ATOM   11262 N  N      . LEU   D 2  139 ? 23.200  10.461   35.338   1.00 56.54  ? 139 LEU   D N      1 
ATOM   11263 C  CA     . LEU   D 2  139 ? 24.276  11.207   34.716   1.00 64.88  ? 139 LEU   D CA     1 
ATOM   11264 C  C      . LEU   D 2  139 ? 24.389  12.616   35.280   1.00 74.29  ? 139 LEU   D C      1 
ATOM   11265 O  O      . LEU   D 2  139 ? 25.244  13.393   34.829   1.00 73.16  ? 139 LEU   D O      1 
ATOM   11266 C  CB     . LEU   D 2  139 ? 24.102  11.241   33.193   1.00 69.46  ? 139 LEU   D CB     1 
ATOM   11267 C  CG     . LEU   D 2  139 ? 23.655  9.959    32.475   1.00 68.85  ? 139 LEU   D CG     1 
ATOM   11268 C  CD1    . LEU   D 2  139 ? 23.164  10.246   31.037   1.00 59.79  ? 139 LEU   D CD1    1 
ATOM   11269 C  CD2    . LEU   D 2  139 ? 24.754  8.895    32.500   1.00 65.08  ? 139 LEU   D CD2    1 
ATOM   11270 N  N      . GLY   D 2  140 ? 23.566  12.947   36.276   1.00 72.55  ? 140 GLY   D N      1 
ATOM   11271 C  CA     . GLY   D 2  140 ? 23.505  14.278   36.858   1.00 78.45  ? 140 GLY   D CA     1 
ATOM   11272 C  C      . GLY   D 2  140 ? 24.528  14.594   37.941   1.00 78.58  ? 140 GLY   D C      1 
ATOM   11273 O  O      . GLY   D 2  140 ? 25.065  15.706   37.972   1.00 75.56  ? 140 GLY   D O      1 
ATOM   11274 N  N      . GLY   D 2  141 ? 24.824  13.652   38.836   1.00 78.54  ? 141 GLY   D N      1 
ATOM   11275 C  CA     . GLY   D 2  141 ? 25.803  13.993   39.837   1.00 76.45  ? 141 GLY   D CA     1 
ATOM   11276 C  C      . GLY   D 2  141 ? 26.596  12.929   40.552   1.00 83.15  ? 141 GLY   D C      1 
ATOM   11277 O  O      . GLY   D 2  141 ? 26.070  12.067   41.278   1.00 86.72  ? 141 GLY   D O      1 
ATOM   11278 N  N      . GLY   D 2  142 ? 27.885  13.026   40.368   1.00 74.57  ? 142 GLY   D N      1 
ATOM   11279 C  CA     . GLY   D 2  142 ? 28.792  12.475   41.370   1.00 77.28  ? 142 GLY   D CA     1 
ATOM   11280 C  C      . GLY   D 2  142 ? 29.184  11.018   41.103   1.00 71.01  ? 142 GLY   D C      1 
ATOM   11281 O  O      . GLY   D 2  142 ? 29.948  10.737   40.191   1.00 71.04  ? 142 GLY   D O      1 
ATOM   11282 N  N      . THR   D 2  143 ? 28.682  10.125   41.947   1.00 69.57  ? 143 THR   D N      1 
ATOM   11283 C  CA     . THR   D 2  143 ? 29.159  8.749    41.918   1.00 71.37  ? 143 THR   D CA     1 
ATOM   11284 C  C      . THR   D 2  143 ? 28.638  8.019    40.697   1.00 75.06  ? 143 THR   D C      1 
ATOM   11285 O  O      . THR   D 2  143 ? 29.421  7.521    39.884   1.00 74.14  ? 143 THR   D O      1 
ATOM   11286 C  CB     . THR   D 2  143 ? 28.726  8.021    43.190   1.00 73.74  ? 143 THR   D CB     1 
ATOM   11287 O  OG1    . THR   D 2  143 ? 29.044  8.842    44.321   1.00 81.31  ? 143 THR   D OG1    1 
ATOM   11288 C  CG2    . THR   D 2  143 ? 29.441  6.706    43.299   1.00 74.58  ? 143 THR   D CG2    1 
ATOM   11289 N  N      . GLY   D 2  144 ? 27.307  7.930    40.564   1.00 73.68  ? 144 GLY   D N      1 
ATOM   11290 C  CA     . GLY   D 2  144 ? 26.728  7.232    39.430   1.00 66.60  ? 144 GLY   D CA     1 
ATOM   11291 C  C      . GLY   D 2  144 ? 27.221  7.752    38.093   1.00 66.05  ? 144 GLY   D C      1 
ATOM   11292 O  O      . GLY   D 2  144 ? 27.487  6.977    37.173   1.00 64.76  ? 144 GLY   D O      1 
ATOM   11293 N  N      . SER   D 2  145 ? 27.360  9.069    37.966   1.00 67.08  ? 145 SER   D N      1 
ATOM   11294 C  CA     . SER   D 2  145 ? 27.708  9.631    36.667   1.00 67.61  ? 145 SER   D CA     1 
ATOM   11295 C  C      . SER   D 2  145 ? 29.159  9.335    36.309   1.00 69.70  ? 145 SER   D C      1 
ATOM   11296 O  O      . SER   D 2  145 ? 29.455  8.913    35.187   1.00 69.44  ? 145 SER   D O      1 
ATOM   11297 C  CB     . SER   D 2  145 ? 27.451  11.134   36.658   1.00 72.93  ? 145 SER   D CB     1 
ATOM   11298 O  OG     . SER   D 2  145 ? 28.658  11.834   36.889   1.00 76.72  ? 145 SER   D OG     1 
ATOM   11299 N  N      . GLY   D 2  146 ? 30.078  9.550    37.251   1.00 74.02  ? 146 GLY   D N      1 
ATOM   11300 C  CA     . GLY   D 2  146 ? 31.498  9.464    36.962   1.00 70.13  ? 146 GLY   D CA     1 
ATOM   11301 C  C      . GLY   D 2  146 ? 32.128  8.134    37.308   1.00 68.23  ? 146 GLY   D C      1 
ATOM   11302 O  O      . GLY   D 2  146 ? 32.834  7.547    36.486   1.00 69.24  ? 146 GLY   D O      1 
ATOM   11303 N  N      . MET   D 2  147 ? 31.925  7.654    38.537   1.00 73.79  ? 147 MET   D N      1 
ATOM   11304 C  CA     . MET   D 2  147 ? 32.468  6.342    38.874   1.00 75.33  ? 147 MET   D CA     1 
ATOM   11305 C  C      . MET   D 2  147 ? 31.757  5.267    38.068   1.00 69.32  ? 147 MET   D C      1 
ATOM   11306 O  O      . MET   D 2  147 ? 32.385  4.286    37.643   1.00 64.21  ? 147 MET   D O      1 
ATOM   11307 C  CB     . MET   D 2  147 ? 32.334  6.069    40.375   1.00 67.93  ? 147 MET   D CB     1 
ATOM   11308 C  CG     . MET   D 2  147 ? 32.892  4.722    40.820   1.00 71.41  ? 147 MET   D CG     1 
ATOM   11309 S  SD     . MET   D 2  147 ? 32.733  4.482    42.600   1.00 69.92  ? 147 MET   D SD     1 
ATOM   11310 C  CE     . MET   D 2  147 ? 32.821  2.695    42.783   1.00 69.31  ? 147 MET   D CE     1 
ATOM   11311 N  N      . GLY   D 2  148 ? 30.453  5.472    37.831   1.00 68.05  ? 148 GLY   D N      1 
ATOM   11312 C  CA     . GLY   D 2  148 ? 29.682  4.571    36.994   1.00 63.57  ? 148 GLY   D CA     1 
ATOM   11313 C  C      . GLY   D 2  148 ? 30.239  4.435    35.588   1.00 63.21  ? 148 GLY   D C      1 
ATOM   11314 O  O      . GLY   D 2  148 ? 30.270  3.331    35.040   1.00 62.84  ? 148 GLY   D O      1 
ATOM   11315 N  N      . THR   D 2  149 ? 30.676  5.555    34.975   1.00 60.35  ? 149 THR   D N      1 
ATOM   11316 C  CA     . THR   D 2  149 ? 31.309  5.472    33.657   1.00 62.82  ? 149 THR   D CA     1 
ATOM   11317 C  C      . THR   D 2  149 ? 32.766  5.029    33.735   1.00 66.28  ? 149 THR   D C      1 
ATOM   11318 O  O      . THR   D 2  149 ? 33.295  4.511    32.740   1.00 70.96  ? 149 THR   D O      1 
ATOM   11319 C  CB     . THR   D 2  149 ? 31.256  6.803    32.875   1.00 61.38  ? 149 THR   D CB     1 
ATOM   11320 O  OG1    . THR   D 2  149 ? 31.678  7.885    33.696   1.00 61.93  ? 149 THR   D OG1    1 
ATOM   11321 C  CG2    . THR   D 2  149 ? 29.851  7.099    32.390   1.00 66.02  ? 149 THR   D CG2    1 
ATOM   11322 N  N      . LEU   D 2  150 ? 33.432  5.227    34.881   1.00 66.95  ? 150 LEU   D N      1 
ATOM   11323 C  CA     . LEU   D 2  150 ? 34.770  4.666    35.060   1.00 68.67  ? 150 LEU   D CA     1 
ATOM   11324 C  C      . LEU   D 2  150 ? 34.696  3.170    35.322   1.00 62.77  ? 150 LEU   D C      1 
ATOM   11325 O  O      . LEU   D 2  150 ? 35.528  2.398    34.824   1.00 58.05  ? 150 LEU   D O      1 
ATOM   11326 C  CB     . LEU   D 2  150 ? 35.509  5.358    36.207   1.00 70.30  ? 150 LEU   D CB     1 
ATOM   11327 C  CG     . LEU   D 2  150 ? 36.639  4.500    36.789   1.00 66.25  ? 150 LEU   D CG     1 
ATOM   11328 C  CD1    . LEU   D 2  150 ? 37.855  4.476    35.864   1.00 60.66  ? 150 LEU   D CD1    1 
ATOM   11329 C  CD2    . LEU   D 2  150 ? 37.018  4.963    38.180   1.00 66.37  ? 150 LEU   D CD2    1 
ATOM   11330 N  N      . LEU   D 2  151 ? 33.708  2.744    36.105   1.00 56.53  ? 151 LEU   D N      1 
ATOM   11331 C  CA     . LEU   D 2  151 ? 33.464  1.320    36.253   1.00 61.78  ? 151 LEU   D CA     1 
ATOM   11332 C  C      . LEU   D 2  151 ? 33.124  0.676    34.903   1.00 67.66  ? 151 LEU   D C      1 
ATOM   11333 O  O      . LEU   D 2  151 ? 33.610  -0.418   34.589   1.00 61.99  ? 151 LEU   D O      1 
ATOM   11334 C  CB     . LEU   D 2  151 ? 32.356  1.102    37.275   1.00 60.48  ? 151 LEU   D CB     1 
ATOM   11335 C  CG     . LEU   D 2  151 ? 32.429  -0.237   38.012   1.00 69.64  ? 151 LEU   D CG     1 
ATOM   11336 C  CD1    . LEU   D 2  151 ? 33.373  -0.169   39.191   1.00 71.55  ? 151 LEU   D CD1    1 
ATOM   11337 C  CD2    . LEU   D 2  151 ? 31.055  -0.688   38.467   1.00 68.93  ? 151 LEU   D CD2    1 
ATOM   11338 N  N      . ILE   D 2  152 ? 32.305  1.345    34.080   1.00 63.72  ? 152 ILE   D N      1 
ATOM   11339 C  CA     . ILE   D 2  152 ? 32.044  0.839    32.731   1.00 62.61  ? 152 ILE   D CA     1 
ATOM   11340 C  C      . ILE   D 2  152 ? 33.363  0.596    32.003   1.00 61.85  ? 152 ILE   D C      1 
ATOM   11341 O  O      . ILE   D 2  152 ? 33.660  -0.523   31.571   1.00 61.78  ? 152 ILE   D O      1 
ATOM   11342 C  CB     . ILE   D 2  152 ? 31.128  1.801    31.947   1.00 63.51  ? 152 ILE   D CB     1 
ATOM   11343 C  CG1    . ILE   D 2  152 ? 29.679  1.670    32.432   1.00 56.17  ? 152 ILE   D CG1    1 
ATOM   11344 C  CG2    . ILE   D 2  152 ? 31.220  1.542    30.411   1.00 55.15  ? 152 ILE   D CG2    1 
ATOM   11345 C  CD1    . ILE   D 2  152 ? 28.785  2.848    32.057   1.00 52.38  ? 152 ILE   D CD1    1 
ATOM   11346 N  N      . SER   D 2  153 ? 34.177  1.645    31.861   1.00 58.17  ? 153 SER   D N      1 
ATOM   11347 C  CA     . SER   D 2  153 ? 35.481  1.481    31.234   1.00 57.43  ? 153 SER   D CA     1 
ATOM   11348 C  C      . SER   D 2  153 ? 36.196  0.236    31.742   1.00 59.71  ? 153 SER   D C      1 
ATOM   11349 O  O      . SER   D 2  153 ? 36.600  -0.617   30.950   1.00 59.21  ? 153 SER   D O      1 
ATOM   11350 C  CB     . SER   D 2  153 ? 36.343  2.718    31.474   1.00 60.04  ? 153 SER   D CB     1 
ATOM   11351 O  OG     . SER   D 2  153 ? 36.529  3.437    30.272   1.00 72.62  ? 153 SER   D OG     1 
ATOM   11352 N  N      . LYS   D 2  154 ? 36.342  0.104    33.069   1.00 59.59  ? 154 LYS   D N      1 
ATOM   11353 C  CA     . LYS   D 2  154 ? 37.158  -0.977   33.628   1.00 61.66  ? 154 LYS   D CA     1 
ATOM   11354 C  C      . LYS   D 2  154 ? 36.550  -2.342   33.345   1.00 54.20  ? 154 LYS   D C      1 
ATOM   11355 O  O      . LYS   D 2  154 ? 37.271  -3.307   33.087   1.00 54.33  ? 154 LYS   D O      1 
ATOM   11356 C  CB     . LYS   D 2  154 ? 37.340  -0.805   35.143   1.00 63.86  ? 154 LYS   D CB     1 
ATOM   11357 C  CG     . LYS   D 2  154 ? 38.084  0.442    35.568   1.00 63.29  ? 154 LYS   D CG     1 
ATOM   11358 C  CD     . LYS   D 2  154 ? 39.337  0.627    34.753   1.00 62.99  ? 154 LYS   D CD     1 
ATOM   11359 C  CE     . LYS   D 2  154 ? 40.577  0.381    35.595   1.00 75.60  ? 154 LYS   D CE     1 
ATOM   11360 N  NZ     . LYS   D 2  154 ? 41.813  0.378    34.762   1.00 77.60  ? 154 LYS   D NZ     1 
ATOM   11361 N  N      . ILE   D 2  155 ? 35.230  -2.447   33.419   1.00 60.29  ? 155 ILE   D N      1 
ATOM   11362 C  CA     . ILE   D 2  155 ? 34.573  -3.727   33.193   1.00 60.25  ? 155 ILE   D CA     1 
ATOM   11363 C  C      . ILE   D 2  155 ? 34.732  -4.156   31.736   1.00 64.18  ? 155 ILE   D C      1 
ATOM   11364 O  O      . ILE   D 2  155 ? 35.100  -5.301   31.446   1.00 61.11  ? 155 ILE   D O      1 
ATOM   11365 C  CB     . ILE   D 2  155 ? 33.099  -3.633   33.614   1.00 53.49  ? 155 ILE   D CB     1 
ATOM   11366 C  CG1    . ILE   D 2  155 ? 33.020  -2.938   34.975   1.00 55.90  ? 155 ILE   D CG1    1 
ATOM   11367 C  CG2    . ILE   D 2  155 ? 32.470  -5.016   33.641   1.00 59.64  ? 155 ILE   D CG2    1 
ATOM   11368 C  CD1    . ILE   D 2  155 ? 31.751  -3.177   35.772   1.00 64.03  ? 155 ILE   D CD1    1 
ATOM   11369 N  N      . ARG   D 2  156 ? 34.477  -3.236   30.799   1.00 55.76  ? 156 ARG   D N      1 
ATOM   11370 C  CA     . ARG   D 2  156 ? 34.641  -3.562   29.391   1.00 58.49  ? 156 ARG   D CA     1 
ATOM   11371 C  C      . ARG   D 2  156 ? 36.065  -4.030   29.099   1.00 63.51  ? 156 ARG   D C      1 
ATOM   11372 O  O      . ARG   D 2  156 ? 36.278  -4.869   28.212   1.00 63.56  ? 156 ARG   D O      1 
ATOM   11373 C  CB     . ARG   D 2  156 ? 34.255  -2.345   28.536   1.00 64.13  ? 156 ARG   D CB     1 
ATOM   11374 C  CG     . ARG   D 2  156 ? 33.769  -2.651   27.106   1.00 63.99  ? 156 ARG   D CG     1 
ATOM   11375 C  CD     . ARG   D 2  156 ? 33.259  -1.386   26.412   1.00 65.93  ? 156 ARG   D CD     1 
ATOM   11376 N  NE     . ARG   D 2  156 ? 32.721  -1.608   25.068   1.00 68.09  ? 156 ARG   D NE     1 
ATOM   11377 C  CZ     . ARG   D 2  156 ? 31.675  -2.378   24.776   1.00 62.91  ? 156 ARG   D CZ     1 
ATOM   11378 N  NH1    . ARG   D 2  156 ? 31.098  -3.149   25.688   1.00 52.38  ? 156 ARG   D NH1    1 
ATOM   11379 N  NH2    . ARG   D 2  156 ? 31.189  -2.370   23.537   1.00 56.37  ? 156 ARG   D NH2    1 
ATOM   11380 N  N      . GLU   D 2  157 ? 37.045  -3.524   29.852   1.00 66.29  ? 157 GLU   D N      1 
ATOM   11381 C  CA     . GLU   D 2  157 ? 38.436  -3.940   29.675   1.00 63.00  ? 157 GLU   D CA     1 
ATOM   11382 C  C      . GLU   D 2  157 ? 38.639  -5.394   30.105   1.00 58.17  ? 157 GLU   D C      1 
ATOM   11383 O  O      . GLU   D 2  157 ? 39.393  -6.137   29.475   1.00 58.29  ? 157 GLU   D O      1 
ATOM   11384 C  CB     . GLU   D 2  157 ? 39.343  -2.990   30.462   1.00 59.80  ? 157 GLU   D CB     1 
ATOM   11385 C  CG     . GLU   D 2  157 ? 40.775  -2.939   30.015   1.00 65.18  ? 157 GLU   D CG     1 
ATOM   11386 C  CD     . GLU   D 2  157 ? 41.589  -1.923   30.798   1.00 75.16  ? 157 GLU   D CD     1 
ATOM   11387 O  OE1    . GLU   D 2  157 ? 41.086  -1.422   31.829   1.00 72.53  ? 157 GLU   D OE1    1 
ATOM   11388 O  OE2    . GLU   D 2  157 ? 42.739  -1.634   30.388   1.00 75.58  ? 157 GLU   D OE2    1 
ATOM   11389 N  N      . GLU   D 2  158 ? 37.965  -5.825   31.162   1.00 57.34  ? 158 GLU   D N      1 
ATOM   11390 C  CA     . GLU   D 2  158 ? 38.063  -7.211   31.597   1.00 61.62  ? 158 GLU   D CA     1 
ATOM   11391 C  C      . GLU   D 2  158 ? 37.088  -8.135   30.881   1.00 61.02  ? 158 GLU   D C      1 
ATOM   11392 O  O      . GLU   D 2  158 ? 37.318  -9.349   30.841   1.00 58.44  ? 158 GLU   D O      1 
ATOM   11393 C  CB     . GLU   D 2  158 ? 37.815  -7.311   33.106   1.00 64.15  ? 158 GLU   D CB     1 
ATOM   11394 C  CG     . GLU   D 2  158 ? 39.057  -7.080   33.957   1.00 69.34  ? 158 GLU   D CG     1 
ATOM   11395 C  CD     . GLU   D 2  158 ? 38.844  -7.449   35.418   1.00 73.01  ? 158 GLU   D CD     1 
ATOM   11396 O  OE1    . GLU   D 2  158 ? 38.427  -8.601   35.693   1.00 68.58  ? 158 GLU   D OE1    1 
ATOM   11397 O  OE2    . GLU   D 2  158 ? 39.087  -6.576   36.284   1.00 70.16  ? 158 GLU   D OE2    1 
ATOM   11398 N  N      . TYR   D 2  159 ? 36.001  -7.595   30.342   1.00 59.22  ? 159 TYR   D N      1 
ATOM   11399 C  CA     . TYR   D 2  159 ? 34.989  -8.376   29.639   1.00 54.98  ? 159 TYR   D CA     1 
ATOM   11400 C  C      . TYR   D 2  159 ? 34.687  -7.722   28.302   1.00 57.65  ? 159 TYR   D C      1 
ATOM   11401 O  O      . TYR   D 2  159 ? 33.534  -7.403   28.006   1.00 62.12  ? 159 TYR   D O      1 
ATOM   11402 C  CB     . TYR   D 2  159 ? 33.713  -8.499   30.468   1.00 53.35  ? 159 TYR   D CB     1 
ATOM   11403 C  CG     . TYR   D 2  159 ? 33.927  -9.053   31.843   1.00 57.35  ? 159 TYR   D CG     1 
ATOM   11404 C  CD1    . TYR   D 2  159 ? 33.887  -10.421  32.077   1.00 54.05  ? 159 TYR   D CD1    1 
ATOM   11405 C  CD2    . TYR   D 2  159 ? 34.160  -8.209   32.917   1.00 61.97  ? 159 TYR   D CD2    1 
ATOM   11406 C  CE1    . TYR   D 2  159 ? 34.089  -10.937  33.340   1.00 53.01  ? 159 TYR   D CE1    1 
ATOM   11407 C  CE2    . TYR   D 2  159 ? 34.360  -8.715   34.182   1.00 63.52  ? 159 TYR   D CE2    1 
ATOM   11408 C  CZ     . TYR   D 2  159 ? 34.325  -10.077  34.392   1.00 59.46  ? 159 TYR   D CZ     1 
ATOM   11409 O  OH     . TYR   D 2  159 ? 34.531  -10.566  35.663   1.00 63.79  ? 159 TYR   D OH     1 
ATOM   11410 N  N      . PRO   D 2  160 ? 35.697  -7.531   27.450   1.00 55.98  ? 160 PRO   D N      1 
ATOM   11411 C  CA     . PRO   D 2  160 ? 35.455  -6.815   26.185   1.00 62.01  ? 160 PRO   D CA     1 
ATOM   11412 C  C      . PRO   D 2  160 ? 34.416  -7.485   25.302   1.00 57.73  ? 160 PRO   D C      1 
ATOM   11413 O  O      . PRO   D 2  160 ? 33.910  -6.839   24.378   1.00 56.85  ? 160 PRO   D O      1 
ATOM   11414 C  CB     . PRO   D 2  160 ? 36.835  -6.799   25.516   1.00 57.91  ? 160 PRO   D CB     1 
ATOM   11415 C  CG     . PRO   D 2  160 ? 37.517  -7.984   26.077   1.00 57.93  ? 160 PRO   D CG     1 
ATOM   11416 C  CD     . PRO   D 2  160 ? 37.013  -8.179   27.474   1.00 57.10  ? 160 PRO   D CD     1 
ATOM   11417 N  N      . ASP   D 2  161 ? 34.072  -8.742   25.581   1.00 56.75  ? 161 ASP   D N      1 
ATOM   11418 C  CA     . ASP   D 2  161 ? 33.171  -9.548   24.769   1.00 53.89  ? 161 ASP   D CA     1 
ATOM   11419 C  C      . ASP   D 2  161 ? 31.833  -9.804   25.459   1.00 50.67  ? 161 ASP   D C      1 
ATOM   11420 O  O      . ASP   D 2  161 ? 31.140  -10.768  25.131   1.00 48.06  ? 161 ASP   D O      1 
ATOM   11421 C  CB     . ASP   D 2  161 ? 33.863  -10.864  24.412   1.00 52.07  ? 161 ASP   D CB     1 
ATOM   11422 C  CG     . ASP   D 2  161 ? 34.373  -11.622  25.645   1.00 58.53  ? 161 ASP   D CG     1 
ATOM   11423 O  OD1    . ASP   D 2  161 ? 34.479  -11.027  26.743   1.00 57.91  ? 161 ASP   D OD1    1 
ATOM   11424 O  OD2    . ASP   D 2  161 ? 34.703  -12.821  25.509   1.00 59.57  ? 161 ASP   D OD2    1 
ATOM   11425 N  N      . ARG   D 2  162 ? 31.463  -8.970   26.419   1.00 53.73  ? 162 ARG   D N      1 
ATOM   11426 C  CA     . ARG   D 2  162 ? 30.193  -9.077   27.113   1.00 52.31  ? 162 ARG   D CA     1 
ATOM   11427 C  C      . ARG   D 2  162 ? 29.398  -7.802   26.863   1.00 49.76  ? 162 ARG   D C      1 
ATOM   11428 O  O      . ARG   D 2  162 ? 29.945  -6.775   26.447   1.00 51.43  ? 162 ARG   D O      1 
ATOM   11429 C  CB     . ARG   D 2  162 ? 30.396  -9.311   28.617   1.00 50.86  ? 162 ARG   D CB     1 
ATOM   11430 C  CG     . ARG   D 2  162 ? 31.226  -10.539  28.953   1.00 49.46  ? 162 ARG   D CG     1 
ATOM   11431 C  CD     . ARG   D 2  162 ? 30.438  -11.826  28.793   1.00 53.28  ? 162 ARG   D CD     1 
ATOM   11432 N  NE     . ARG   D 2  162 ? 31.285  -13.010  28.956   1.00 62.61  ? 162 ARG   D NE     1 
ATOM   11433 C  CZ     . ARG   D 2  162 ? 30.968  -14.239  28.555   1.00 61.28  ? 162 ARG   D CZ     1 
ATOM   11434 N  NH1    . ARG   D 2  162 ? 29.815  -14.503  27.952   1.00 64.69  ? 162 ARG   D NH1    1 
ATOM   11435 N  NH2    . ARG   D 2  162 ? 31.828  -15.229  28.756   1.00 56.56  ? 162 ARG   D NH2    1 
ATOM   11436 N  N      . ILE   D 2  163 ? 28.103  -7.867   27.090   1.00 49.32  ? 163 ILE   D N      1 
ATOM   11437 C  CA     . ILE   D 2  163 ? 27.245  -6.739   26.745   1.00 51.86  ? 163 ILE   D CA     1 
ATOM   11438 C  C      . ILE   D 2  163 ? 27.242  -5.757   27.908   1.00 47.02  ? 163 ILE   D C      1 
ATOM   11439 O  O      . ILE   D 2  163 ? 27.279  -6.158   29.075   1.00 54.67  ? 163 ILE   D O      1 
ATOM   11440 C  CB     . ILE   D 2  163 ? 25.822  -7.216   26.383   1.00 46.59  ? 163 ILE   D CB     1 
ATOM   11441 C  CG1    . ILE   D 2  163 ? 25.869  -8.105   25.135   1.00 46.84  ? 163 ILE   D CG1    1 
ATOM   11442 C  CG2    . ILE   D 2  163 ? 24.907  -6.020   26.131   1.00 49.04  ? 163 ILE   D CG2    1 
ATOM   11443 C  CD1    . ILE   D 2  163 ? 26.214  -7.350   23.864   1.00 36.27  ? 163 ILE   D CD1    1 
ATOM   11444 N  N      . MET   D 2  164 ? 27.210  -4.470   27.598   1.00 44.96  ? 164 MET   D N      1 
ATOM   11445 C  CA     . MET   D 2  164 ? 27.149  -3.417   28.610   1.00 48.42  ? 164 MET   D CA     1 
ATOM   11446 C  C      . MET   D 2  164 ? 25.861  -2.622   28.405   1.00 48.10  ? 164 MET   D C      1 
ATOM   11447 O  O      . MET   D 2  164 ? 25.788  -1.765   27.518   1.00 46.79  ? 164 MET   D O      1 
ATOM   11448 C  CB     . MET   D 2  164 ? 28.378  -2.510   28.530   1.00 54.00  ? 164 MET   D CB     1 
ATOM   11449 C  CG     . MET   D 2  164 ? 28.387  -1.423   29.571   1.00 54.22  ? 164 MET   D CG     1 
ATOM   11450 S  SD     . MET   D 2  164 ? 28.640  -2.164   31.187   1.00 65.81  ? 164 MET   D SD     1 
ATOM   11451 C  CE     . MET   D 2  164 ? 30.324  -2.739   31.030   1.00 58.66  ? 164 MET   D CE     1 
ATOM   11452 N  N      . ASN   D 2  165 ? 24.865  -2.893   29.244   1.00 48.62  ? 165 ASN   D N      1 
ATOM   11453 C  CA     . ASN   D 2  165 ? 23.559  -2.241   29.195   1.00 56.04  ? 165 ASN   D CA     1 
ATOM   11454 C  C      . ASN   D 2  165 ? 23.394  -1.317   30.405   1.00 56.56  ? 165 ASN   D C      1 
ATOM   11455 O  O      . ASN   D 2  165 ? 23.430  -1.780   31.548   1.00 52.35  ? 165 ASN   D O      1 
ATOM   11456 C  CB     . ASN   D 2  165 ? 22.452  -3.298   29.175   1.00 50.79  ? 165 ASN   D CB     1 
ATOM   11457 C  CG     . ASN   D 2  165 ? 21.061  -2.695   29.256   1.00 51.69  ? 165 ASN   D CG     1 
ATOM   11458 O  OD1    . ASN   D 2  165 ? 20.648  -1.958   28.372   1.00 53.27  ? 165 ASN   D OD1    1 
ATOM   11459 N  ND2    . ASN   D 2  165 ? 20.333  -3.011   30.320   1.00 54.48  ? 165 ASN   D ND2    1 
ATOM   11460 N  N      . THR   D 2  166 ? 23.192  -0.021   30.166   1.00 52.04  ? 166 THR   D N      1 
ATOM   11461 C  CA     . THR   D 2  166 ? 22.981  0.910    31.270   1.00 54.24  ? 166 THR   D CA     1 
ATOM   11462 C  C      . THR   D 2  166 ? 21.594  1.533    31.202   1.00 56.31  ? 166 THR   D C      1 
ATOM   11463 O  O      . THR   D 2  166 ? 21.042  1.735    30.118   1.00 59.49  ? 166 THR   D O      1 
ATOM   11464 C  CB     . THR   D 2  166 ? 24.017  2.042    31.306   1.00 54.05  ? 166 THR   D CB     1 
ATOM   11465 O  OG1    . THR   D 2  166 ? 23.651  3.065    30.373   1.00 53.79  ? 166 THR   D OG1    1 
ATOM   11466 C  CG2    . THR   D 2  166 ? 25.404  1.525    30.981   1.00 59.12  ? 166 THR   D CG2    1 
ATOM   11467 N  N      . PHE   D 2  167 ? 21.037  1.818    32.392   1.00 61.18  ? 167 PHE   D N      1 
ATOM   11468 C  CA     . PHE   D 2  167 ? 19.860  2.670    32.588   1.00 54.15  ? 167 PHE   D CA     1 
ATOM   11469 C  C      . PHE   D 2  167 ? 20.328  4.023    33.117   1.00 58.01  ? 167 PHE   D C      1 
ATOM   11470 O  O      . PHE   D 2  167 ? 20.521  4.194    34.321   1.00 64.65  ? 167 PHE   D O      1 
ATOM   11471 C  CB     . PHE   D 2  167 ? 18.893  2.037    33.571   1.00 48.79  ? 167 PHE   D CB     1 
ATOM   11472 C  CG     . PHE   D 2  167 ? 18.266  0.784    33.077   1.00 56.88  ? 167 PHE   D CG     1 
ATOM   11473 C  CD1    . PHE   D 2  167 ? 18.886  -0.436   33.271   1.00 56.56  ? 167 PHE   D CD1    1 
ATOM   11474 C  CD2    . PHE   D 2  167 ? 17.046  0.818    32.423   1.00 56.90  ? 167 PHE   D CD2    1 
ATOM   11475 C  CE1    . PHE   D 2  167 ? 18.303  -1.609   32.833   1.00 53.99  ? 167 PHE   D CE1    1 
ATOM   11476 C  CE2    . PHE   D 2  167 ? 16.449  -0.356   31.977   1.00 58.66  ? 167 PHE   D CE2    1 
ATOM   11477 C  CZ     . PHE   D 2  167 ? 17.078  -1.571   32.183   1.00 55.70  ? 167 PHE   D CZ     1 
ATOM   11478 N  N      . SER   D 2  168 ? 20.507  4.986    32.232   1.00 51.32  ? 168 SER   D N      1 
ATOM   11479 C  CA     . SER   D 2  168 ? 21.032  6.284    32.618   1.00 59.89  ? 168 SER   D CA     1 
ATOM   11480 C  C      . SER   D 2  168 ? 19.900  7.287    32.816   1.00 67.67  ? 168 SER   D C      1 
ATOM   11481 O  O      . SER   D 2  168 ? 19.000  7.399    31.979   1.00 69.56  ? 168 SER   D O      1 
ATOM   11482 C  CB     . SER   D 2  168 ? 22.029  6.780    31.571   1.00 61.07  ? 168 SER   D CB     1 
ATOM   11483 O  OG     . SER   D 2  168 ? 22.971  5.753    31.297   1.00 54.95  ? 168 SER   D OG     1 
ATOM   11484 N  N      . VAL   D 2  169 ? 19.950  8.014    33.934   1.00 68.94  ? 169 VAL   D N      1 
ATOM   11485 C  CA     . VAL   D 2  169 ? 18.915  8.969    34.325   1.00 64.82  ? 169 VAL   D CA     1 
ATOM   11486 C  C      . VAL   D 2  169 ? 19.423  10.379   34.039   1.00 64.82  ? 169 VAL   D C      1 
ATOM   11487 O  O      . VAL   D 2  169 ? 20.317  10.882   34.731   1.00 69.13  ? 169 VAL   D O      1 
ATOM   11488 C  CB     . VAL   D 2  169 ? 18.524  8.801    35.796   1.00 63.72  ? 169 VAL   D CB     1 
ATOM   11489 C  CG1    . VAL   D 2  169 ? 17.487  9.830    36.183   1.00 63.39  ? 169 VAL   D CG1    1 
ATOM   11490 C  CG2    . VAL   D 2  169 ? 17.996  7.385    36.027   1.00 62.35  ? 169 VAL   D CG2    1 
ATOM   11491 N  N      . MET   D 2  170 ? 18.828  11.030   33.011   1.00 62.70  ? 170 MET   D N      1 
ATOM   11492 C  CA     . MET   D 2  170 ? 19.272  12.313   32.479   1.00 69.88  ? 170 MET   D CA     1 
ATOM   11493 C  C      . MET   D 2  170 ? 18.736  13.466   33.317   1.00 75.72  ? 170 MET   D C      1 
ATOM   11494 O  O      . MET   D 2  170 ? 17.572  13.444   33.740   1.00 70.56  ? 170 MET   D O      1 
ATOM   11495 C  CB     . MET   D 2  170 ? 18.811  12.500   31.041   1.00 71.86  ? 170 MET   D CB     1 
ATOM   11496 C  CG     . MET   D 2  170 ? 18.515  11.206   30.342   1.00 71.65  ? 170 MET   D CG     1 
ATOM   11497 S  SD     . MET   D 2  170 ? 20.054  10.389   29.887   1.00 83.83  ? 170 MET   D SD     1 
ATOM   11498 C  CE     . MET   D 2  170 ? 20.925  11.724   29.045   1.00 66.56  ? 170 MET   D CE     1 
ATOM   11499 N  N      . PRO   D 2  171 ? 19.553  14.500   33.514   1.00 78.35  ? 171 PRO   D N      1 
ATOM   11500 C  CA     . PRO   D 2  171 ? 19.167  15.601   34.404   1.00 78.84  ? 171 PRO   D CA     1 
ATOM   11501 C  C      . PRO   D 2  171 ? 18.126  16.518   33.778   1.00 81.69  ? 171 PRO   D C      1 
ATOM   11502 O  O      . PRO   D 2  171 ? 18.167  16.817   32.581   1.00 88.29  ? 171 PRO   D O      1 
ATOM   11503 C  CB     . PRO   D 2  171 ? 20.489  16.342   34.626   1.00 79.50  ? 171 PRO   D CB     1 
ATOM   11504 C  CG     . PRO   D 2  171 ? 21.278  16.063   33.385   1.00 76.10  ? 171 PRO   D CG     1 
ATOM   11505 C  CD     . PRO   D 2  171 ? 20.925  14.653   32.997   1.00 74.89  ? 171 PRO   D CD     1 
ATOM   11506 N  N      . SER   D 2  172 ? 17.194  16.985   34.609   1.00 82.05  ? 172 SER   D N      1 
ATOM   11507 C  CA     . SER   D 2  172 ? 16.206  17.974   34.182   1.00 83.67  ? 172 SER   D CA     1 
ATOM   11508 C  C      . SER   D 2  172 ? 16.161  19.125   35.183   1.00 84.87  ? 172 SER   D C      1 
ATOM   11509 O  O      . SER   D 2  172 ? 15.886  18.893   36.386   1.00 79.04  ? 172 SER   D O      1 
ATOM   11510 C  CB     . SER   D 2  172 ? 14.827  17.335   34.016   1.00 75.39  ? 172 SER   D CB     1 
ATOM   11511 O  OG     . SER   D 2  172 ? 13.889  18.325   33.650   1.00 73.13  ? 172 SER   D OG     1 
ATOM   11512 N  N      . PRO   D 2  173 ? 16.422  20.366   34.751   1.00 79.25  ? 173 PRO   D N      1 
ATOM   11513 C  CA     . PRO   D 2  173 ? 16.322  21.513   35.667   1.00 73.11  ? 173 PRO   D CA     1 
ATOM   11514 C  C      . PRO   D 2  173 ? 14.961  21.645   36.331   1.00 77.44  ? 173 PRO   D C      1 
ATOM   11515 O  O      . PRO   D 2  173 ? 14.828  22.423   37.286   1.00 78.11  ? 173 PRO   D O      1 
ATOM   11516 C  CB     . PRO   D 2  173 ? 16.614  22.708   34.755   1.00 72.56  ? 173 PRO   D CB     1 
ATOM   11517 C  CG     . PRO   D 2  173 ? 17.473  22.137   33.679   1.00 77.29  ? 173 PRO   D CG     1 
ATOM   11518 C  CD     . PRO   D 2  173 ? 16.877  20.781   33.414   1.00 82.29  ? 173 PRO   D CD     1 
ATOM   11519 N  N      . LYS   D 2  174 ? 13.953  20.919   35.864   1.00 71.66  ? 174 LYS   D N      1 
ATOM   11520 C  CA     . LYS   D 2  174 ? 12.681  20.819   36.560   1.00 76.04  ? 174 LYS   D CA     1 
ATOM   11521 C  C      . LYS   D 2  174 ? 12.699  19.795   37.689   1.00 78.87  ? 174 LYS   D C      1 
ATOM   11522 O  O      . LYS   D 2  174 ? 11.628  19.517   38.241   1.00 83.26  ? 174 LYS   D O      1 
ATOM   11523 C  CB     . LYS   D 2  174 ? 11.548  20.450   35.588   1.00 80.12  ? 174 LYS   D CB     1 
ATOM   11524 C  CG     . LYS   D 2  174 ? 11.714  20.924   34.143   1.00 81.59  ? 174 LYS   D CG     1 
ATOM   11525 C  CD     . LYS   D 2  174 ? 10.364  20.872   33.405   1.00 84.15  ? 174 LYS   D CD     1 
ATOM   11526 C  CE     . LYS   D 2  174 ? 10.437  21.517   32.017   1.00 79.23  ? 174 LYS   D CE     1 
ATOM   11527 N  NZ     . LYS   D 2  174 ? 9.604   20.797   31.004   1.00 77.03  ? 174 LYS   D NZ     1 
ATOM   11528 N  N      . VAL   D 2  175 ? 13.848  19.205   38.035   1.00 77.55  ? 175 VAL   D N      1 
ATOM   11529 C  CA     . VAL   D 2  175 ? 13.855  18.189   39.091   1.00 83.51  ? 175 VAL   D CA     1 
ATOM   11530 C  C      . VAL   D 2  175 ? 15.077  18.309   40.002   1.00 86.61  ? 175 VAL   D C      1 
ATOM   11531 O  O      . VAL   D 2  175 ? 15.040  17.855   41.155   1.00 82.36  ? 175 VAL   D O      1 
ATOM   11532 C  CB     . VAL   D 2  175 ? 13.751  16.761   38.511   1.00 82.39  ? 175 VAL   D CB     1 
ATOM   11533 C  CG1    . VAL   D 2  175 ? 14.415  15.743   39.439   1.00 77.57  ? 175 VAL   D CG1    1 
ATOM   11534 C  CG2    . VAL   D 2  175 ? 12.292  16.376   38.291   1.00 78.63  ? 175 VAL   D CG2    1 
ATOM   11535 N  N      . SER   D 2  176 ? 16.167  18.906   39.512   1.00 82.00  ? 176 SER   D N      1 
ATOM   11536 C  CA     . SER   D 2  176 ? 17.312  19.165   40.375   1.00 82.35  ? 176 SER   D CA     1 
ATOM   11537 C  C      . SER   D 2  176 ? 17.946  20.497   40.021   1.00 87.35  ? 176 SER   D C      1 
ATOM   11538 O  O      . SER   D 2  176 ? 17.996  20.897   38.856   1.00 85.00  ? 176 SER   D O      1 
ATOM   11539 C  CB     . SER   D 2  176 ? 18.381  18.076   40.305   1.00 80.63  ? 176 SER   D CB     1 
ATOM   11540 O  OG     . SER   D 2  176 ? 19.303  18.241   41.373   1.00 87.46  ? 176 SER   D OG     1 
ATOM   11541 N  N      . ASP   D 2  177 ? 18.452  21.170   41.048   1.00 90.50  ? 177 ASP   D N      1 
ATOM   11542 C  CA     . ASP   D 2  177 ? 18.957  22.518   40.886   1.00 91.29  ? 177 ASP   D CA     1 
ATOM   11543 C  C      . ASP   D 2  177 ? 20.463  22.585   40.732   1.00 93.37  ? 177 ASP   D C      1 
ATOM   11544 O  O      . ASP   D 2  177 ? 20.961  23.552   40.142   1.00 94.93  ? 177 ASP   D O      1 
ATOM   11545 C  CB     . ASP   D 2  177 ? 18.546  23.384   42.077   1.00 90.23  ? 177 ASP   D CB     1 
ATOM   11546 C  CG     . ASP   D 2  177 ? 17.190  23.984   41.890   1.00 95.60  ? 177 ASP   D CG     1 
ATOM   11547 O  OD1    . ASP   D 2  177 ? 16.987  24.643   40.844   1.00 89.13  ? 177 ASP   D OD1    1 
ATOM   11548 O  OD2    . ASP   D 2  177 ? 16.333  23.795   42.780   1.00 101.02 ? 177 ASP   D OD2    1 
ATOM   11549 N  N      . THR   D 2  178 ? 21.195  21.604   41.251   1.00 83.56  ? 178 THR   D N      1 
ATOM   11550 C  CA     . THR   D 2  178 ? 22.646  21.699   41.233   1.00 82.45  ? 178 THR   D CA     1 
ATOM   11551 C  C      . THR   D 2  178 ? 23.150  21.966   39.824   1.00 86.06  ? 178 THR   D C      1 
ATOM   11552 O  O      . THR   D 2  178 ? 22.896  21.190   38.902   1.00 91.58  ? 178 THR   D O      1 
ATOM   11553 C  CB     . THR   D 2  178 ? 23.255  20.431   41.823   1.00 82.60  ? 178 THR   D CB     1 
ATOM   11554 O  OG1    . THR   D 2  178 ? 24.650  20.377   41.498   1.00 88.09  ? 178 THR   D OG1    1 
ATOM   11555 C  CG2    . THR   D 2  178 ? 22.490  19.167   41.375   1.00 85.44  ? 178 THR   D CG2    1 
ATOM   11556 N  N      . VAL   D 2  179 ? 23.843  23.094   39.652   1.00 87.69  ? 179 VAL   D N      1 
ATOM   11557 C  CA     . VAL   D 2  179 ? 24.027  23.645   38.314   1.00 87.22  ? 179 VAL   D CA     1 
ATOM   11558 C  C      . VAL   D 2  179 ? 25.062  22.884   37.500   1.00 89.44  ? 179 VAL   D C      1 
ATOM   11559 O  O      . VAL   D 2  179 ? 25.126  23.060   36.280   1.00 90.86  ? 179 VAL   D O      1 
ATOM   11560 C  CB     . VAL   D 2  179 ? 24.414  25.133   38.392   1.00 88.20  ? 179 VAL   D CB     1 
ATOM   11561 C  CG1    . VAL   D 2  179 ? 23.178  25.989   38.665   1.00 88.90  ? 179 VAL   D CG1    1 
ATOM   11562 C  CG2    . VAL   D 2  179 ? 25.502  25.351   39.438   1.00 88.84  ? 179 VAL   D CG2    1 
ATOM   11563 N  N      . VAL   D 2  180 ? 25.892  22.047   38.133   1.00 88.96  ? 180 VAL   D N      1 
ATOM   11564 C  CA     . VAL   D 2  180 ? 26.927  21.332   37.385   1.00 90.02  ? 180 VAL   D CA     1 
ATOM   11565 C  C      . VAL   D 2  180 ? 26.383  20.123   36.630   1.00 83.84  ? 180 VAL   D C      1 
ATOM   11566 O  O      . VAL   D 2  180 ? 27.158  19.411   35.975   1.00 81.51  ? 180 VAL   D O      1 
ATOM   11567 C  CB     . VAL   D 2  180 ? 28.074  20.918   38.334   1.00 82.37  ? 180 VAL   D CB     1 
ATOM   11568 C  CG1    . VAL   D 2  180 ? 29.105  22.034   38.447   1.00 80.16  ? 180 VAL   D CG1    1 
ATOM   11569 C  CG2    . VAL   D 2  180 ? 27.521  20.558   39.699   1.00 83.69  ? 180 VAL   D CG2    1 
ATOM   11570 N  N      . GLU   D 2  181 ? 25.072  19.877   36.675   1.00 76.14  ? 181 GLU   D N      1 
ATOM   11571 C  CA     . GLU   D 2  181 ? 24.524  18.699   36.006   1.00 81.45  ? 181 GLU   D CA     1 
ATOM   11572 C  C      . GLU   D 2  181 ? 24.715  18.726   34.495   1.00 83.70  ? 181 GLU   D C      1 
ATOM   11573 O  O      . GLU   D 2  181 ? 25.104  17.689   33.926   1.00 82.26  ? 181 GLU   D O      1 
ATOM   11574 C  CB     . GLU   D 2  181 ? 23.052  18.534   36.389   1.00 73.86  ? 181 GLU   D CB     1 
ATOM   11575 C  CG     . GLU   D 2  181 ? 22.860  17.673   37.606   1.00 76.56  ? 181 GLU   D CG     1 
ATOM   11576 C  CD     . GLU   D 2  181 ? 21.499  17.826   38.233   1.00 80.92  ? 181 GLU   D CD     1 
ATOM   11577 O  OE1    . GLU   D 2  181 ? 20.710  18.660   37.747   1.00 83.78  ? 181 GLU   D OE1    1 
ATOM   11578 O  OE2    . GLU   D 2  181 ? 21.202  17.071   39.185   1.00 82.36  ? 181 GLU   D OE2    1 
ATOM   11579 N  N      . PRO   D 2  182 ? 24.467  19.829   33.787   1.00 79.34  ? 182 PRO   D N      1 
ATOM   11580 C  CA     . PRO   D 2  182 ? 24.774  19.849   32.348   1.00 78.10  ? 182 PRO   D CA     1 
ATOM   11581 C  C      . PRO   D 2  182 ? 26.213  19.485   32.047   1.00 75.35  ? 182 PRO   D C      1 
ATOM   11582 O  O      . PRO   D 2  182 ? 26.521  19.034   30.939   1.00 75.80  ? 182 PRO   D O      1 
ATOM   11583 C  CB     . PRO   D 2  182 ? 24.462  21.298   31.953   1.00 78.82  ? 182 PRO   D CB     1 
ATOM   11584 C  CG     . PRO   D 2  182 ? 23.378  21.690   32.894   1.00 79.91  ? 182 PRO   D CG     1 
ATOM   11585 C  CD     . PRO   D 2  182 ? 23.737  21.035   34.210   1.00 79.01  ? 182 PRO   D CD     1 
ATOM   11586 N  N      . TYR   D 2  183 ? 27.113  19.694   33.005   1.00 78.97  ? 183 TYR   D N      1 
ATOM   11587 C  CA     . TYR   D 2  183 ? 28.493  19.250   32.849   1.00 80.22  ? 183 TYR   D CA     1 
ATOM   11588 C  C      . TYR   D 2  183 ? 28.604  17.745   33.057   1.00 75.20  ? 183 TYR   D C      1 
ATOM   11589 O  O      . TYR   D 2  183 ? 29.198  17.032   32.238   1.00 72.46  ? 183 TYR   D O      1 
ATOM   11590 C  CB     . TYR   D 2  183 ? 29.392  19.989   33.844   1.00 80.45  ? 183 TYR   D CB     1 
ATOM   11591 C  CG     . TYR   D 2  183 ? 29.850  21.353   33.392   1.00 80.84  ? 183 TYR   D CG     1 
ATOM   11592 C  CD1    . TYR   D 2  183 ? 29.939  21.666   32.047   1.00 79.99  ? 183 TYR   D CD1    1 
ATOM   11593 C  CD2    . TYR   D 2  183 ? 30.189  22.334   34.317   1.00 84.83  ? 183 TYR   D CD2    1 
ATOM   11594 C  CE1    . TYR   D 2  183 ? 30.361  22.917   31.628   1.00 83.96  ? 183 TYR   D CE1    1 
ATOM   11595 C  CE2    . TYR   D 2  183 ? 30.606  23.589   33.910   1.00 84.18  ? 183 TYR   D CE2    1 
ATOM   11596 C  CZ     . TYR   D 2  183 ? 30.689  23.874   32.562   1.00 86.75  ? 183 TYR   D CZ     1 
ATOM   11597 O  OH     . TYR   D 2  183 ? 31.103  25.113   32.132   1.00 85.16  ? 183 TYR   D OH     1 
ATOM   11598 N  N      . ASN   D 2  184 ? 28.034  17.246   34.157   1.00 75.08  ? 184 ASN   D N      1 
ATOM   11599 C  CA     . ASN   D 2  184 ? 28.178  15.835   34.507   1.00 78.86  ? 184 ASN   D CA     1 
ATOM   11600 C  C      . ASN   D 2  184 ? 27.619  14.936   33.409   1.00 77.25  ? 184 ASN   D C      1 
ATOM   11601 O  O      . ASN   D 2  184 ? 28.302  14.019   32.933   1.00 71.96  ? 184 ASN   D O      1 
ATOM   11602 C  CB     . ASN   D 2  184 ? 27.482  15.542   35.843   1.00 81.94  ? 184 ASN   D CB     1 
ATOM   11603 C  CG     . ASN   D 2  184 ? 28.262  16.066   37.066   1.00 83.03  ? 184 ASN   D CG     1 
ATOM   11604 O  OD1    . ASN   D 2  184 ? 29.197  16.865   36.943   1.00 78.13  ? 184 ASN   D OD1    1 
ATOM   11605 N  ND2    . ASN   D 2  184 ? 27.879  15.586   38.253   1.00 78.66  ? 184 ASN   D ND2    1 
ATOM   11606 N  N      . ALA   D 2  185 ? 26.374  15.192   32.992   1.00 76.04  ? 185 ALA   D N      1 
ATOM   11607 C  CA     . ALA   D 2  185 ? 25.756  14.437   31.905   1.00 68.96  ? 185 ALA   D CA     1 
ATOM   11608 C  C      . ALA   D 2  185 ? 26.642  14.405   30.657   1.00 68.81  ? 185 ALA   D C      1 
ATOM   11609 O  O      . ALA   D 2  185 ? 26.988  13.330   30.158   1.00 73.77  ? 185 ALA   D O      1 
ATOM   11610 C  CB     . ALA   D 2  185 ? 24.383  15.026   31.582   1.00 69.80  ? 185 ALA   D CB     1 
ATOM   11611 N  N      . THR   D 2  186 ? 27.020  15.576   30.130   1.00 61.14  ? 186 THR   D N      1 
ATOM   11612 C  CA     . THR   D 2  186 ? 27.799  15.606   28.891   1.00 61.93  ? 186 THR   D CA     1 
ATOM   11613 C  C      . THR   D 2  186 ? 29.105  14.821   29.005   1.00 68.25  ? 186 THR   D C      1 
ATOM   11614 O  O      . THR   D 2  186 ? 29.546  14.193   28.039   1.00 72.06  ? 186 THR   D O      1 
ATOM   11615 C  CB     . THR   D 2  186 ? 28.093  17.047   28.473   1.00 63.59  ? 186 THR   D CB     1 
ATOM   11616 O  OG1    . THR   D 2  186 ? 26.862  17.757   28.327   1.00 65.37  ? 186 THR   D OG1    1 
ATOM   11617 C  CG2    . THR   D 2  186 ? 28.888  17.085   27.164   1.00 53.85  ? 186 THR   D CG2    1 
ATOM   11618 N  N      . LEU   D 2  187 ? 29.766  14.871   30.154   1.00 72.64  ? 187 LEU   D N      1 
ATOM   11619 C  CA     . LEU   D 2  187 ? 30.998  14.102   30.277   1.00 72.40  ? 187 LEU   D CA     1 
ATOM   11620 C  C      . LEU   D 2  187 ? 30.694  12.605   30.374   1.00 67.32  ? 187 LEU   D C      1 
ATOM   11621 O  O      . LEU   D 2  187 ? 31.512  11.777   29.957   1.00 64.18  ? 187 LEU   D O      1 
ATOM   11622 C  CB     . LEU   D 2  187 ? 31.805  14.615   31.483   1.00 74.94  ? 187 LEU   D CB     1 
ATOM   11623 C  CG     . LEU   D 2  187 ? 32.303  16.074   31.477   1.00 66.17  ? 187 LEU   D CG     1 
ATOM   11624 C  CD1    . LEU   D 2  187 ? 32.632  16.482   32.869   1.00 70.21  ? 187 LEU   D CD1    1 
ATOM   11625 C  CD2    . LEU   D 2  187 ? 33.524  16.298   30.590   1.00 62.12  ? 187 LEU   D CD2    1 
ATOM   11626 N  N      . SER   D 2  188 ? 29.519  12.242   30.900   1.00 64.11  ? 188 SER   D N      1 
ATOM   11627 C  CA     . SER   D 2  188 ? 29.128  10.836   30.954   1.00 67.05  ? 188 SER   D CA     1 
ATOM   11628 C  C      . SER   D 2  188 ? 28.803  10.313   29.559   1.00 69.17  ? 188 SER   D C      1 
ATOM   11629 O  O      . SER   D 2  188 ? 29.342  9.284    29.127   1.00 65.64  ? 188 SER   D O      1 
ATOM   11630 C  CB     . SER   D 2  188 ? 27.919  10.657   31.875   1.00 67.58  ? 188 SER   D CB     1 
ATOM   11631 O  OG     . SER   D 2  188 ? 28.148  11.224   33.145   1.00 68.71  ? 188 SER   D OG     1 
ATOM   11632 N  N      . VAL   D 2  189 ? 27.913  11.020   28.845   1.00 66.70  ? 189 VAL   D N      1 
ATOM   11633 C  CA     . VAL   D 2  189 ? 27.496  10.617   27.504   1.00 64.04  ? 189 VAL   D CA     1 
ATOM   11634 C  C      . VAL   D 2  189 ? 28.700  10.441   26.594   1.00 64.84  ? 189 VAL   D C      1 
ATOM   11635 O  O      . VAL   D 2  189 ? 28.713  9.561    25.725   1.00 64.39  ? 189 VAL   D O      1 
ATOM   11636 C  CB     . VAL   D 2  189 ? 26.512  11.640   26.916   1.00 59.33  ? 189 VAL   D CB     1 
ATOM   11637 C  CG1    . VAL   D 2  189 ? 26.424  11.450   25.412   1.00 61.90  ? 189 VAL   D CG1    1 
ATOM   11638 C  CG2    . VAL   D 2  189 ? 25.156  11.497   27.572   1.00 59.54  ? 189 VAL   D CG2    1 
ATOM   11639 N  N      . HIS   D 2  190 ? 29.709  11.299   26.747   1.00 62.02  ? 190 HIS   D N      1 
ATOM   11640 C  CA     . HIS   D 2  190 ? 30.958  11.117   26.016   1.00 63.63  ? 190 HIS   D CA     1 
ATOM   11641 C  C      . HIS   D 2  190 ? 31.524  9.722    26.233   1.00 64.45  ? 190 HIS   D C      1 
ATOM   11642 O  O      . HIS   D 2  190 ? 32.162  9.159    25.335   1.00 66.44  ? 190 HIS   D O      1 
ATOM   11643 C  CB     . HIS   D 2  190 ? 31.955  12.182   26.458   1.00 65.57  ? 190 HIS   D CB     1 
ATOM   11644 C  CG     . HIS   D 2  190 ? 33.291  12.085   25.795   1.00 70.71  ? 190 HIS   D CG     1 
ATOM   11645 N  ND1    . HIS   D 2  190 ? 33.477  12.326   24.451   1.00 70.70  ? 190 HIS   D ND1    1 
ATOM   11646 C  CD2    . HIS   D 2  190 ? 34.516  11.811   26.302   1.00 68.65  ? 190 HIS   D CD2    1 
ATOM   11647 C  CE1    . HIS   D 2  190 ? 34.758  12.195   24.155   1.00 67.22  ? 190 HIS   D CE1    1 
ATOM   11648 N  NE2    . HIS   D 2  190 ? 35.410  11.880   25.260   1.00 72.31  ? 190 HIS   D NE2    1 
ATOM   11649 N  N      . GLN   D 2  191 ? 31.295  9.151    27.416   1.00 60.95  ? 191 GLN   D N      1 
ATOM   11650 C  CA     . GLN   D 2  191 ? 31.731  7.799    27.740   1.00 63.42  ? 191 GLN   D CA     1 
ATOM   11651 C  C      . GLN   D 2  191 ? 30.714  6.751    27.318   1.00 62.57  ? 191 GLN   D C      1 
ATOM   11652 O  O      . GLN   D 2  191 ? 31.099  5.660    26.887   1.00 57.02  ? 191 GLN   D O      1 
ATOM   11653 C  CB     . GLN   D 2  191 ? 31.978  7.674    29.242   1.00 65.80  ? 191 GLN   D CB     1 
ATOM   11654 C  CG     . GLN   D 2  191 ? 32.839  8.770    29.815   1.00 67.72  ? 191 GLN   D CG     1 
ATOM   11655 C  CD     . GLN   D 2  191 ? 34.287  8.499    29.584   1.00 66.12  ? 191 GLN   D CD     1 
ATOM   11656 O  OE1    . GLN   D 2  191 ? 34.759  7.386    29.833   1.00 68.40  ? 191 GLN   D OE1    1 
ATOM   11657 N  NE2    . GLN   D 2  191 ? 35.016  9.510    29.106   1.00 63.16  ? 191 GLN   D NE2    1 
ATOM   11658 N  N      . LEU   D 2  192 ? 29.421  7.074    27.445   1.00 62.27  ? 192 LEU   D N      1 
ATOM   11659 C  CA     . LEU   D 2  192 ? 28.361  6.129    27.122   1.00 58.28  ? 192 LEU   D CA     1 
ATOM   11660 C  C      . LEU   D 2  192 ? 28.292  5.842    25.627   1.00 58.41  ? 192 LEU   D C      1 
ATOM   11661 O  O      . LEU   D 2  192 ? 27.988  4.711    25.225   1.00 55.90  ? 192 LEU   D O      1 
ATOM   11662 C  CB     . LEU   D 2  192 ? 27.023  6.666    27.616   1.00 58.94  ? 192 LEU   D CB     1 
ATOM   11663 C  CG     . LEU   D 2  192 ? 26.720  6.468    29.096   1.00 60.78  ? 192 LEU   D CG     1 
ATOM   11664 C  CD1    . LEU   D 2  192 ? 25.444  7.207    29.459   1.00 54.82  ? 192 LEU   D CD1    1 
ATOM   11665 C  CD2    . LEU   D 2  192 ? 26.615  4.989    29.430   1.00 59.57  ? 192 LEU   D CD2    1 
ATOM   11666 N  N      . VAL   D 2  193 ? 28.569  6.848    24.797   1.00 56.59  ? 193 VAL   D N      1 
ATOM   11667 C  CA     . VAL   D 2  193 ? 28.576  6.665    23.351   1.00 53.80  ? 193 VAL   D CA     1 
ATOM   11668 C  C      . VAL   D 2  193 ? 29.669  5.688    22.948   1.00 56.15  ? 193 VAL   D C      1 
ATOM   11669 O  O      . VAL   D 2  193 ? 29.529  4.967    21.950   1.00 60.73  ? 193 VAL   D O      1 
ATOM   11670 C  CB     . VAL   D 2  193 ? 28.739  8.033    22.644   1.00 55.26  ? 193 VAL   D CB     1 
ATOM   11671 C  CG1    . VAL   D 2  193 ? 29.464  7.903    21.305   1.00 50.49  ? 193 VAL   D CG1    1 
ATOM   11672 C  CG2    . VAL   D 2  193 ? 27.394  8.689    22.464   1.00 44.42  ? 193 VAL   D CG2    1 
ATOM   11673 N  N      . GLU   D 2  194 ? 30.750  5.612    23.731   1.00 57.35  ? 194 GLU   D N      1 
ATOM   11674 C  CA     . GLU   D 2  194 ? 31.930  4.841    23.364   1.00 51.55  ? 194 GLU   D CA     1 
ATOM   11675 C  C      . GLU   D 2  194 ? 32.051  3.492    24.052   1.00 46.62  ? 194 GLU   D C      1 
ATOM   11676 O  O      . GLU   D 2  194 ? 32.870  2.689    23.617   1.00 55.58  ? 194 GLU   D O      1 
ATOM   11677 C  CB     . GLU   D 2  194 ? 33.198  5.633    23.665   1.00 52.77  ? 194 GLU   D CB     1 
ATOM   11678 C  CG     . GLU   D 2  194 ? 33.249  6.962    22.986   1.00 55.23  ? 194 GLU   D CG     1 
ATOM   11679 C  CD     . GLU   D 2  194 ? 33.854  6.837    21.629   1.00 60.40  ? 194 GLU   D CD     1 
ATOM   11680 O  OE1    . GLU   D 2  194 ? 34.803  6.034    21.516   1.00 64.14  ? 194 GLU   D OE1    1 
ATOM   11681 O  OE2    . GLU   D 2  194 ? 33.383  7.508    20.681   1.00 65.94  ? 194 GLU   D OE2    1 
ATOM   11682 N  N      . ASN   D 2  195 ? 31.295  3.208    25.109   1.00 47.53  ? 195 ASN   D N      1 
ATOM   11683 C  CA     . ASN   D 2  195 ? 31.590  1.988    25.855   1.00 54.23  ? 195 ASN   D CA     1 
ATOM   11684 C  C      . ASN   D 2  195 ? 30.371  1.194    26.303   1.00 54.47  ? 195 ASN   D C      1 
ATOM   11685 O  O      . ASN   D 2  195 ? 30.540  0.198    27.022   1.00 55.33  ? 195 ASN   D O      1 
ATOM   11686 C  CB     . ASN   D 2  195 ? 32.468  2.300    27.081   1.00 55.36  ? 195 ASN   D CB     1 
ATOM   11687 C  CG     . ASN   D 2  195 ? 33.893  2.625    26.693   1.00 59.35  ? 195 ASN   D CG     1 
ATOM   11688 O  OD1    . ASN   D 2  195 ? 34.441  2.010    25.778   1.00 65.27  ? 195 ASN   D OD1    1 
ATOM   11689 N  ND2    . ASN   D 2  195 ? 34.496  3.605    27.365   1.00 55.12  ? 195 ASN   D ND2    1 
ATOM   11690 N  N      . THR   D 2  196 ? 29.161  1.587    25.919   1.00 53.10  ? 196 THR   D N      1 
ATOM   11691 C  CA     . THR   D 2  196 ? 27.989  0.753    26.130   1.00 54.46  ? 196 THR   D CA     1 
ATOM   11692 C  C      . THR   D 2  196 ? 27.444  0.244    24.802   1.00 54.50  ? 196 THR   D C      1 
ATOM   11693 O  O      . THR   D 2  196 ? 27.616  0.864    23.747   1.00 48.26  ? 196 THR   D O      1 
ATOM   11694 C  CB     . THR   D 2  196 ? 26.874  1.506    26.848   1.00 56.93  ? 196 THR   D CB     1 
ATOM   11695 O  OG1    . THR   D 2  196 ? 26.663  2.754    26.176   1.00 57.07  ? 196 THR   D OG1    1 
ATOM   11696 C  CG2    . THR   D 2  196 ? 27.235  1.739    28.295   1.00 53.55  ? 196 THR   D CG2    1 
ATOM   11697 N  N      . ASP   D 2  197 ? 26.764  -0.891   24.882   1.00 52.64  ? 197 ASP   D N      1 
ATOM   11698 C  CA     . ASP   D 2  197 ? 26.052  -1.430   23.743   1.00 48.29  ? 197 ASP   D CA     1 
ATOM   11699 C  C      . ASP   D 2  197 ? 24.591  -1.017   23.724   1.00 50.64  ? 197 ASP   D C      1 
ATOM   11700 O  O      . ASP   D 2  197 ? 23.991  -0.943   22.649   1.00 55.43  ? 197 ASP   D O      1 
ATOM   11701 C  CB     . ASP   D 2  197 ? 26.202  -2.946   23.754   1.00 51.86  ? 197 ASP   D CB     1 
ATOM   11702 C  CG     . ASP   D 2  197 ? 27.649  -3.348   23.738   1.00 55.47  ? 197 ASP   D CG     1 
ATOM   11703 O  OD1    . ASP   D 2  197 ? 28.288  -2.992   22.720   1.00 54.63  ? 197 ASP   D OD1    1 
ATOM   11704 O  OD2    . ASP   D 2  197 ? 28.148  -3.945   24.735   1.00 48.52  ? 197 ASP   D OD2    1 
ATOM   11705 N  N      . GLU   D 2  198 ? 24.013  -0.717   24.880   1.00 49.45  ? 198 GLU   D N      1 
ATOM   11706 C  CA     . GLU   D 2  198 ? 22.604  -0.361   24.969   1.00 49.76  ? 198 GLU   D CA     1 
ATOM   11707 C  C      . GLU   D 2  198 ? 22.378  0.549    26.168   1.00 56.28  ? 198 GLU   D C      1 
ATOM   11708 O  O      . GLU   D 2  198 ? 22.603  0.132    27.313   1.00 56.98  ? 198 GLU   D O      1 
ATOM   11709 C  CB     . GLU   D 2  198 ? 21.745  -1.606   25.116   1.00 47.29  ? 198 GLU   D CB     1 
ATOM   11710 C  CG     . GLU   D 2  198 ? 21.944  -2.662   24.109   1.00 50.29  ? 198 GLU   D CG     1 
ATOM   11711 C  CD     . GLU   D 2  198 ? 21.523  -4.008   24.642   1.00 55.31  ? 198 GLU   D CD     1 
ATOM   11712 O  OE1    . GLU   D 2  198 ? 21.757  -4.263   25.838   1.00 55.00  ? 198 GLU   D OE1    1 
ATOM   11713 O  OE2    . GLU   D 2  198 ? 20.917  -4.793   23.882   1.00 55.57  ? 198 GLU   D OE2    1 
ATOM   11714 N  N      . THR   D 2  199 ? 21.883  1.762    25.931   1.00 53.39  ? 199 THR   D N      1 
ATOM   11715 C  CA     . THR   D 2  199 ? 21.520  2.652    27.030   1.00 54.86  ? 199 THR   D CA     1 
ATOM   11716 C  C      . THR   D 2  199 ? 20.078  3.099    26.875   1.00 50.52  ? 199 THR   D C      1 
ATOM   11717 O  O      . THR   D 2  199 ? 19.747  3.819    25.927   1.00 45.24  ? 199 THR   D O      1 
ATOM   11718 C  CB     . THR   D 2  199 ? 22.429  3.869    27.097   1.00 56.65  ? 199 THR   D CB     1 
ATOM   11719 O  OG1    . THR   D 2  199 ? 23.648  3.502    27.751   1.00 63.03  ? 199 THR   D OG1    1 
ATOM   11720 C  CG2    . THR   D 2  199 ? 21.735  4.953    27.902   1.00 56.28  ? 199 THR   D CG2    1 
ATOM   11721 N  N      . TYR   D 2  200 ? 19.236  2.682    27.811   1.00 48.69  ? 200 TYR   D N      1 
ATOM   11722 C  CA     . TYR   D 2  200 ? 17.905  3.253    27.952   1.00 54.43  ? 200 TYR   D CA     1 
ATOM   11723 C  C      . TYR   D 2  200 ? 17.983  4.643    28.583   1.00 60.30  ? 200 TYR   D C      1 
ATOM   11724 O  O      . TYR   D 2  200 ? 18.382  4.778    29.745   1.00 58.62  ? 200 TYR   D O      1 
ATOM   11725 C  CB     . TYR   D 2  200 ? 17.049  2.365    28.837   1.00 54.25  ? 200 TYR   D CB     1 
ATOM   11726 C  CG     . TYR   D 2  200 ? 16.813  0.982    28.347   1.00 55.29  ? 200 TYR   D CG     1 
ATOM   11727 C  CD1    . TYR   D 2  200 ? 15.716  0.681    27.563   1.00 51.02  ? 200 TYR   D CD1    1 
ATOM   11728 C  CD2    . TYR   D 2  200 ? 17.664  -0.040   28.707   1.00 56.82  ? 200 TYR   D CD2    1 
ATOM   11729 C  CE1    . TYR   D 2  200 ? 15.488  -0.600   27.137   1.00 48.04  ? 200 TYR   D CE1    1 
ATOM   11730 C  CE2    . TYR   D 2  200 ? 17.446  -1.324   28.285   1.00 54.16  ? 200 TYR   D CE2    1 
ATOM   11731 C  CZ     . TYR   D 2  200 ? 16.359  -1.600   27.500   1.00 51.50  ? 200 TYR   D CZ     1 
ATOM   11732 O  OH     . TYR   D 2  200 ? 16.149  -2.898   27.088   1.00 55.93  ? 200 TYR   D OH     1 
ATOM   11733 N  N      . CYS   D 2  201 ? 17.565  5.667    27.847   1.00 56.58  ? 201 CYS   D N      1 
ATOM   11734 C  CA     . CYS   D 2  201 ? 17.445  7.007    28.412   1.00 60.55  ? 201 CYS   D CA     1 
ATOM   11735 C  C      . CYS   D 2  201 ? 16.213  7.093    29.310   1.00 61.49  ? 201 CYS   D C      1 
ATOM   11736 O  O      . CYS   D 2  201 ? 15.081  7.015    28.830   1.00 64.73  ? 201 CYS   D O      1 
ATOM   11737 C  CB     . CYS   D 2  201 ? 17.364  8.033    27.290   1.00 61.17  ? 201 CYS   D CB     1 
ATOM   11738 S  SG     . CYS   D 2  201 ? 18.841  8.013    26.282   1.00 63.60  ? 201 CYS   D SG     1 
ATOM   11739 N  N      . ILE   D 2  202 ? 16.424  7.236    30.613   1.00 65.86  ? 202 ILE   D N      1 
ATOM   11740 C  CA     . ILE   D 2  202 ? 15.382  7.631    31.559   1.00 64.65  ? 202 ILE   D CA     1 
ATOM   11741 C  C      . ILE   D 2  202 ? 15.537  9.137    31.751   1.00 61.64  ? 202 ILE   D C      1 
ATOM   11742 O  O      . ILE   D 2  202 ? 16.540  9.587    32.309   1.00 68.38  ? 202 ILE   D O      1 
ATOM   11743 C  CB     . ILE   D 2  202 ? 15.522  6.882    32.895   1.00 68.85  ? 202 ILE   D CB     1 
ATOM   11744 C  CG1    . ILE   D 2  202 ? 15.722  5.361    32.700   1.00 61.44  ? 202 ILE   D CG1    1 
ATOM   11745 C  CG2    . ILE   D 2  202 ? 14.333  7.170    33.805   1.00 65.82  ? 202 ILE   D CG2    1 
ATOM   11746 C  CD1    . ILE   D 2  202 ? 14.530  4.627    32.123   1.00 58.83  ? 202 ILE   D CD1    1 
ATOM   11747 N  N      . ASP   D 2  203 ? 14.594  9.937    31.259   1.00 62.48  ? 203 ASP   D N      1 
ATOM   11748 C  CA     . ASP   D 2  203 ? 14.724  11.395   31.284   1.00 67.69  ? 203 ASP   D CA     1 
ATOM   11749 C  C      . ASP   D 2  203 ? 13.916  11.990   32.440   1.00 73.27  ? 203 ASP   D C      1 
ATOM   11750 O  O      . ASP   D 2  203 ? 12.677  11.932   32.442   1.00 73.34  ? 203 ASP   D O      1 
ATOM   11751 C  CB     . ASP   D 2  203 ? 14.284  12.015   29.958   1.00 66.39  ? 203 ASP   D CB     1 
ATOM   11752 C  CG     . ASP   D 2  203 ? 14.764  13.452   29.798   1.00 70.90  ? 203 ASP   D CG     1 
ATOM   11753 O  OD1    . ASP   D 2  203 ? 15.281  14.029   30.781   1.00 75.39  ? 203 ASP   D OD1    1 
ATOM   11754 O  OD2    . ASP   D 2  203 ? 14.627  14.013   28.689   1.00 68.96  ? 203 ASP   D OD2    1 
ATOM   11755 N  N      . ASN   D 2  204 ? 14.615  12.586   33.411   1.00 72.53  ? 204 ASN   D N      1 
ATOM   11756 C  CA     . ASN   D 2  204 ? 13.910  13.197   34.535   1.00 78.36  ? 204 ASN   D CA     1 
ATOM   11757 C  C      . ASN   D 2  204 ? 12.996  14.331   34.069   1.00 76.42  ? 204 ASN   D C      1 
ATOM   11758 O  O      . ASN   D 2  204 ? 12.003  14.643   34.739   1.00 74.52  ? 204 ASN   D O      1 
ATOM   11759 C  CB     . ASN   D 2  204 ? 14.915  13.681   35.593   1.00 74.72  ? 204 ASN   D CB     1 
ATOM   11760 C  CG     . ASN   D 2  204 ? 15.182  12.631   36.698   1.00 72.13  ? 204 ASN   D CG     1 
ATOM   11761 O  OD1    . ASN   D 2  204 ? 14.601  11.534   36.706   1.00 67.15  ? 204 ASN   D OD1    1 
ATOM   11762 N  ND2    . ASN   D 2  204 ? 16.062  12.978   37.637   1.00 70.92  ? 204 ASN   D ND2    1 
ATOM   11763 N  N      . GLU   D 2  205 ? 13.294  14.937   32.912   1.00 72.39  ? 205 GLU   D N      1 
ATOM   11764 C  CA     . GLU   D 2  205 ? 12.402  15.952   32.361   1.00 71.06  ? 205 GLU   D CA     1 
ATOM   11765 C  C      . GLU   D 2  205 ? 11.094  15.338   31.886   1.00 73.21  ? 205 GLU   D C      1 
ATOM   11766 O  O      . GLU   D 2  205 ? 10.024  15.933   32.050   1.00 73.76  ? 205 GLU   D O      1 
ATOM   11767 C  CB     . GLU   D 2  205 ? 13.081  16.692   31.215   1.00 71.98  ? 205 GLU   D CB     1 
ATOM   11768 C  CG     . GLU   D 2  205 ? 12.113  17.559   30.434   1.00 76.14  ? 205 GLU   D CG     1 
ATOM   11769 C  CD     . GLU   D 2  205 ? 12.547  19.024   30.329   1.00 81.27  ? 205 GLU   D CD     1 
ATOM   11770 O  OE1    . GLU   D 2  205 ? 13.630  19.394   30.859   1.00 77.89  ? 205 GLU   D OE1    1 
ATOM   11771 O  OE2    . GLU   D 2  205 ? 11.780  19.810   29.722   1.00 81.28  ? 205 GLU   D OE2    1 
ATOM   11772 N  N      . ALA   D 2  206 ? 11.160  14.151   31.290   1.00 74.27  ? 206 ALA   D N      1 
ATOM   11773 C  CA     . ALA   D 2  206 ? 9.952   13.476   30.837   1.00 69.82  ? 206 ALA   D CA     1 
ATOM   11774 C  C      . ALA   D 2  206 ? 9.245   12.764   31.972   1.00 67.94  ? 206 ALA   D C      1 
ATOM   11775 O  O      . ALA   D 2  206 ? 8.028   12.578   31.911   1.00 69.09  ? 206 ALA   D O      1 
ATOM   11776 C  CB     . ALA   D 2  206 ? 10.283  12.475   29.729   1.00 65.97  ? 206 ALA   D CB     1 
ATOM   11777 N  N      . LEU   D 2  207 ? 9.986   12.338   32.996   1.00 70.64  ? 207 LEU   D N      1 
ATOM   11778 C  CA     . LEU   D 2  207 ? 9.344   11.726   34.158   1.00 77.08  ? 207 LEU   D CA     1 
ATOM   11779 C  C      . LEU   D 2  207 ? 8.555   12.754   34.955   1.00 76.43  ? 207 LEU   D C      1 
ATOM   11780 O  O      . LEU   D 2  207 ? 7.439   12.477   35.412   1.00 71.38  ? 207 LEU   D O      1 
ATOM   11781 C  CB     . LEU   D 2  207 ? 10.387  11.062   35.048   1.00 76.05  ? 207 LEU   D CB     1 
ATOM   11782 C  CG     . LEU   D 2  207 ? 11.063  9.832    34.465   1.00 71.25  ? 207 LEU   D CG     1 
ATOM   11783 C  CD1    . LEU   D 2  207 ? 12.311  9.546    35.255   1.00 62.83  ? 207 LEU   D CD1    1 
ATOM   11784 C  CD2    . LEU   D 2  207 ? 10.087  8.666    34.527   1.00 69.96  ? 207 LEU   D CD2    1 
ATOM   11785 N  N      . TYR   D 2  208 ? 9.133   13.938   35.143   1.00 79.51  ? 208 TYR   D N      1 
ATOM   11786 C  CA     . TYR   D 2  208 ? 8.434   15.041   35.773   1.00 80.06  ? 208 TYR   D CA     1 
ATOM   11787 C  C      . TYR   D 2  208 ? 7.185   15.384   34.971   1.00 82.57  ? 208 TYR   D C      1 
ATOM   11788 O  O      . TYR   D 2  208 ? 6.064   15.184   35.458   1.00 81.80  ? 208 TYR   D O      1 
ATOM   11789 C  CB     . TYR   D 2  208 ? 9.369   16.239   35.897   1.00 81.61  ? 208 TYR   D CB     1 
ATOM   11790 C  CG     . TYR   D 2  208 ? 8.710   17.425   36.524   1.00 87.23  ? 208 TYR   D CG     1 
ATOM   11791 C  CD1    . TYR   D 2  208 ? 8.255   17.371   37.838   1.00 86.20  ? 208 TYR   D CD1    1 
ATOM   11792 C  CD2    . TYR   D 2  208 ? 8.550   18.611   35.811   1.00 86.98  ? 208 TYR   D CD2    1 
ATOM   11793 C  CE1    . TYR   D 2  208 ? 7.642   18.458   38.427   1.00 91.21  ? 208 TYR   D CE1    1 
ATOM   11794 C  CE2    . TYR   D 2  208 ? 7.944   19.711   36.393   1.00 95.36  ? 208 TYR   D CE2    1 
ATOM   11795 C  CZ     . TYR   D 2  208 ? 7.488   19.629   37.702   1.00 95.17  ? 208 TYR   D CZ     1 
ATOM   11796 O  OH     . TYR   D 2  208 ? 6.882   20.720   38.275   1.00 87.18  ? 208 TYR   D OH     1 
ATOM   11797 N  N      . ASP   D 2  209 ? 7.374   15.874   33.734   1.00 78.56  ? 209 ASP   D N      1 
ATOM   11798 C  CA     . ASP   D 2  209 ? 6.245   16.263   32.887   1.00 74.97  ? 209 ASP   D CA     1 
ATOM   11799 C  C      . ASP   D 2  209 ? 5.129   15.234   32.908   1.00 74.05  ? 209 ASP   D C      1 
ATOM   11800 O  O      . ASP   D 2  209 ? 3.954   15.591   32.981   1.00 76.78  ? 209 ASP   D O      1 
ATOM   11801 C  CB     . ASP   D 2  209 ? 6.700   16.488   31.452   1.00 66.35  ? 209 ASP   D CB     1 
ATOM   11802 C  CG     . ASP   D 2  209 ? 7.571   17.694   31.313   1.00 73.73  ? 209 ASP   D CG     1 
ATOM   11803 O  OD1    . ASP   D 2  209 ? 7.982   18.241   32.358   1.00 78.67  ? 209 ASP   D OD1    1 
ATOM   11804 O  OD2    . ASP   D 2  209 ? 7.817   18.117   30.168   1.00 70.94  ? 209 ASP   D OD2    1 
ATOM   11805 N  N      . ILE   D 2  210 ? 5.466   13.954   32.806   1.00 74.24  ? 210 ILE   D N      1 
ATOM   11806 C  CA     . ILE   D 2  210 ? 4.429   12.934   32.899   1.00 74.17  ? 210 ILE   D CA     1 
ATOM   11807 C  C      . ILE   D 2  210 ? 3.668   13.086   34.205   1.00 85.31  ? 210 ILE   D C      1 
ATOM   11808 O  O      . ILE   D 2  210 ? 2.447   13.301   34.219   1.00 89.23  ? 210 ILE   D O      1 
ATOM   11809 C  CB     . ILE   D 2  210 ? 5.029   11.527   32.778   1.00 71.70  ? 210 ILE   D CB     1 
ATOM   11810 C  CG1    . ILE   D 2  210 ? 5.534   11.270   31.364   1.00 74.62  ? 210 ILE   D CG1    1 
ATOM   11811 C  CG2    . ILE   D 2  210 ? 3.991   10.499   33.160   1.00 73.09  ? 210 ILE   D CG2    1 
ATOM   11812 C  CD1    . ILE   D 2  210 ? 5.604   9.785    31.029   1.00 66.47  ? 210 ILE   D CD1    1 
ATOM   11813 N  N      . CYS   D 2  211 ? 4.390   12.978   35.325   1.00 88.73  ? 211 CYS   D N      1 
ATOM   11814 C  CA     . CYS   D 2  211 ? 3.764   13.021   36.644   1.00 92.85  ? 211 CYS   D CA     1 
ATOM   11815 C  C      . CYS   D 2  211 ? 2.941   14.299   36.834   1.00 93.70  ? 211 CYS   D C      1 
ATOM   11816 O  O      . CYS   D 2  211 ? 1.894   14.274   37.491   1.00 91.09  ? 211 CYS   D O      1 
ATOM   11817 C  CB     . CYS   D 2  211 ? 4.851   12.901   37.724   1.00 91.52  ? 211 CYS   D CB     1 
ATOM   11818 S  SG     . CYS   D 2  211 ? 5.349   11.201   38.212   1.00 80.97  ? 211 CYS   D SG     1 
ATOM   11819 N  N      . PHE   D 2  212 ? 3.386   15.411   36.239   1.00 93.29  ? 212 PHE   D N      1 
ATOM   11820 C  CA     . PHE   D 2  212 ? 2.777   16.720   36.459   1.00 92.57  ? 212 PHE   D CA     1 
ATOM   11821 C  C      . PHE   D 2  212 ? 1.520   16.930   35.623   1.00 92.47  ? 212 PHE   D C      1 
ATOM   11822 O  O      . PHE   D 2  212 ? 0.571   17.576   36.079   1.00 95.12  ? 212 PHE   D O      1 
ATOM   11823 C  CB     . PHE   D 2  212 ? 3.796   17.815   36.142   1.00 93.02  ? 212 PHE   D CB     1 
ATOM   11824 C  CG     . PHE   D 2  212 ? 3.323   19.204   36.464   1.00 103.10 ? 212 PHE   D CG     1 
ATOM   11825 C  CD1    . PHE   D 2  212 ? 2.554   19.446   37.596   1.00 104.45 ? 212 PHE   D CD1    1 
ATOM   11826 C  CD2    . PHE   D 2  212 ? 3.679   20.277   35.654   1.00 104.86 ? 212 PHE   D CD2    1 
ATOM   11827 C  CE1    . PHE   D 2  212 ? 2.132   20.729   37.903   1.00 107.43 ? 212 PHE   D CE1    1 
ATOM   11828 C  CE2    . PHE   D 2  212 ? 3.265   21.562   35.957   1.00 105.43 ? 212 PHE   D CE2    1 
ATOM   11829 C  CZ     . PHE   D 2  212 ? 2.490   21.789   37.080   1.00 107.15 ? 212 PHE   D CZ     1 
ATOM   11830 N  N      . ARG   D 2  213 ? 1.509   16.438   34.386   1.00 88.99  ? 213 ARG   D N      1 
ATOM   11831 C  CA     . ARG   D 2  213 ? 0.378   16.646   33.495   1.00 85.76  ? 213 ARG   D CA     1 
ATOM   11832 C  C      . ARG   D 2  213 ? -0.532  15.428   33.482   1.00 86.96  ? 213 ARG   D C      1 
ATOM   11833 O  O      . ARG   D 2  213 ? -1.703  15.516   33.860   1.00 91.28  ? 213 ARG   D O      1 
ATOM   11834 C  CB     . ARG   D 2  213 ? 0.850   16.970   32.072   1.00 78.99  ? 213 ARG   D CB     1 
ATOM   11835 C  CG     . ARG   D 2  213 ? 1.936   18.038   31.968   1.00 85.04  ? 213 ARG   D CG     1 
ATOM   11836 C  CD     . ARG   D 2  213 ? 3.005   17.579   30.967   1.00 88.66  ? 213 ARG   D CD     1 
ATOM   11837 N  NE     . ARG   D 2  213 ? 3.762   18.656   30.332   1.00 90.65  ? 213 ARG   D NE     1 
ATOM   11838 C  CZ     . ARG   D 2  213 ? 3.336   19.390   29.309   1.00 95.42  ? 213 ARG   D CZ     1 
ATOM   11839 N  NH1    . ARG   D 2  213 ? 2.106   19.270   28.831   1.00 92.26  ? 213 ARG   D NH1    1 
ATOM   11840 N  NH2    . ARG   D 2  213 ? 4.166   20.265   28.748   1.00 91.96  ? 213 ARG   D NH2    1 
ATOM   11841 N  N      . THR   D 2  214 ? -0.009  14.276   33.072   1.00 82.38  ? 214 THR   D N      1 
ATOM   11842 C  CA     . THR   D 2  214 ? -0.869  13.103   32.979   1.00 89.08  ? 214 THR   D CA     1 
ATOM   11843 C  C      . THR   D 2  214 ? -1.266  12.617   34.372   1.00 92.18  ? 214 THR   D C      1 
ATOM   11844 O  O      . THR   D 2  214 ? -2.455  12.557   34.707   1.00 93.84  ? 214 THR   D O      1 
ATOM   11845 C  CB     . THR   D 2  214 ? -0.188  11.995   32.164   1.00 85.15  ? 214 THR   D CB     1 
ATOM   11846 O  OG1    . THR   D 2  214 ? 0.129   12.488   30.852   1.00 74.32  ? 214 THR   D OG1    1 
ATOM   11847 C  CG2    . THR   D 2  214 ? -1.112  10.789   32.031   1.00 76.97  ? 214 THR   D CG2    1 
ATOM   11848 N  N      . LEU   D 2  215 ? -0.280  12.285   35.210   1.00 92.54  ? 215 LEU   D N      1 
ATOM   11849 C  CA     . LEU   D 2  215 ? -0.574  11.894   36.586   1.00 93.62  ? 215 LEU   D CA     1 
ATOM   11850 C  C      . LEU   D 2  215 ? -1.069  13.064   37.430   1.00 96.15  ? 215 LEU   D C      1 
ATOM   11851 O  O      . LEU   D 2  215 ? -1.512  12.846   38.566   1.00 91.45  ? 215 LEU   D O      1 
ATOM   11852 C  CB     . LEU   D 2  215 ? 0.663   11.272   37.249   1.00 89.03  ? 215 LEU   D CB     1 
ATOM   11853 C  CG     . LEU   D 2  215 ? 1.213   9.986    36.634   1.00 86.18  ? 215 LEU   D CG     1 
ATOM   11854 C  CD1    . LEU   D 2  215 ? 0.155   8.889    36.608   1.00 75.98  ? 215 LEU   D CD1    1 
ATOM   11855 C  CD2    . LEU   D 2  215 ? 1.758   10.263   35.245   1.00 83.50  ? 215 LEU   D CD2    1 
ATOM   11856 N  N      . LYS   D 2  216 ? -1.007  14.290   36.903   1.00 96.02  ? 216 LYS   D N      1 
ATOM   11857 C  CA     . LYS   D 2  216 ? -1.381  15.481   37.652   1.00 92.83  ? 216 LYS   D CA     1 
ATOM   11858 C  C      . LYS   D 2  216 ? -0.875  15.378   39.091   1.00 95.09  ? 216 LYS   D C      1 
ATOM   11859 O  O      . LYS   D 2  216 ? -1.637  15.074   40.016   1.00 93.51  ? 216 LYS   D O      1 
ATOM   11860 C  CB     . LYS   D 2  216 ? -2.899  15.686   37.591   1.00 95.38  ? 216 LYS   D CB     1 
ATOM   11861 C  CG     . LYS   D 2  216 ? -3.339  16.797   36.642   1.00 93.37  ? 216 LYS   D CG     1 
ATOM   11862 C  CD     . LYS   D 2  216 ? -2.566  18.085   36.911   1.00 94.27  ? 216 LYS   D CD     1 
ATOM   11863 C  CE     . LYS   D 2  216 ? -2.249  18.832   35.628   1.00 93.05  ? 216 LYS   D CE     1 
ATOM   11864 N  NZ     . LYS   D 2  216 ? -0.852  19.362   35.635   1.00 91.73  ? 216 LYS   D NZ     1 
ATOM   11865 N  N      . LEU   D 2  217 ? 0.427   15.577   39.271   1.00 97.28  ? 217 LEU   D N      1 
ATOM   11866 C  CA     . LEU   D 2  217 ? 1.055   15.693   40.580   1.00 93.00  ? 217 LEU   D CA     1 
ATOM   11867 C  C      . LEU   D 2  217 ? 1.645   17.093   40.630   1.00 98.47  ? 217 LEU   D C      1 
ATOM   11868 O  O      . LEU   D 2  217 ? 2.593   17.394   39.895   1.00 98.15  ? 217 LEU   D O      1 
ATOM   11869 C  CB     . LEU   D 2  217 ? 2.131   14.628   40.776   1.00 88.08  ? 217 LEU   D CB     1 
ATOM   11870 C  CG     . LEU   D 2  217 ? 1.792   13.438   41.658   1.00 88.16  ? 217 LEU   D CG     1 
ATOM   11871 C  CD1    . LEU   D 2  217 ? 0.415   12.917   41.310   1.00 88.52  ? 217 LEU   D CD1    1 
ATOM   11872 C  CD2    . LEU   D 2  217 ? 2.831   12.368   41.433   1.00 90.54  ? 217 LEU   D CD2    1 
ATOM   11873 N  N      . THR   D 2  218 ? 1.066   17.957   41.466   1.00 98.00  ? 218 THR   D N      1 
ATOM   11874 C  CA     . THR   D 2  218 ? 1.529   19.339   41.508   1.00 98.85  ? 218 THR   D CA     1 
ATOM   11875 C  C      . THR   D 2  218 ? 2.971   19.424   41.993   1.00 102.33 ? 218 THR   D C      1 
ATOM   11876 O  O      . THR   D 2  218 ? 3.740   20.280   41.529   1.00 96.08  ? 218 THR   D O      1 
ATOM   11877 C  CB     . THR   D 2  218 ? 0.606   20.160   42.400   1.00 100.02 ? 218 THR   D CB     1 
ATOM   11878 O  OG1    . THR   D 2  218 ? 1.248   21.394   42.750   1.00 104.90 ? 218 THR   D OG1    1 
ATOM   11879 C  CG2    . THR   D 2  218 ? 0.235   19.364   43.658   1.00 100.32 ? 218 THR   D CG2    1 
ATOM   11880 N  N      . THR   D 2  219 ? 3.354   18.534   42.910   1.00 98.00  ? 219 THR   D N      1 
ATOM   11881 C  CA     . THR   D 2  219 ? 4.726   18.406   43.398   1.00 100.68 ? 219 THR   D CA     1 
ATOM   11882 C  C      . THR   D 2  219 ? 5.088   16.927   43.396   1.00 102.53 ? 219 THR   D C      1 
ATOM   11883 O  O      . THR   D 2  219 ? 4.795   16.198   44.357   1.00 97.81  ? 219 THR   D O      1 
ATOM   11884 C  CB     . THR   D 2  219 ? 4.874   18.998   44.796   1.00 99.49  ? 219 THR   D CB     1 
ATOM   11885 O  OG1    . THR   D 2  219 ? 3.647   18.816   45.512   1.00 100.71 ? 219 THR   D OG1    1 
ATOM   11886 C  CG2    . THR   D 2  219 ? 5.222   20.480   44.717   1.00 91.37  ? 219 THR   D CG2    1 
ATOM   11887 N  N      . PRO   D 2  220 ? 5.711   16.442   42.322   1.00 103.21 ? 220 PRO   D N      1 
ATOM   11888 C  CA     . PRO   D 2  220 ? 6.099   15.025   42.265   1.00 95.75  ? 220 PRO   D CA     1 
ATOM   11889 C  C      . PRO   D 2  220 ? 7.406   14.801   43.007   1.00 89.18  ? 220 PRO   D C      1 
ATOM   11890 O  O      . PRO   D 2  220 ? 8.326   15.621   42.951   1.00 86.34  ? 220 PRO   D O      1 
ATOM   11891 C  CB     . PRO   D 2  220 ? 6.256   14.745   40.761   1.00 93.56  ? 220 PRO   D CB     1 
ATOM   11892 C  CG     . PRO   D 2  220 ? 5.942   16.057   40.045   1.00 98.17  ? 220 PRO   D CG     1 
ATOM   11893 C  CD     . PRO   D 2  220 ? 5.972   17.160   41.063   1.00 97.53  ? 220 PRO   D CD     1 
ATOM   11894 N  N      . THR   D 2  221 ? 7.479   13.684   43.716   1.00 83.29  ? 221 THR   D N      1 
ATOM   11895 C  CA     . THR   D 2  221 ? 8.655   13.352   44.506   1.00 84.97  ? 221 THR   D CA     1 
ATOM   11896 C  C      . THR   D 2  221 ? 9.559   12.382   43.752   1.00 82.46  ? 221 THR   D C      1 
ATOM   11897 O  O      . THR   D 2  221 ? 9.125   11.641   42.864   1.00 80.65  ? 221 THR   D O      1 
ATOM   11898 C  CB     . THR   D 2  221 ? 8.256   12.732   45.849   1.00 81.15  ? 221 THR   D CB     1 
ATOM   11899 O  OG1    . THR   D 2  221 ? 7.156   11.829   45.656   1.00 83.75  ? 221 THR   D OG1    1 
ATOM   11900 C  CG2    . THR   D 2  221 ? 7.861   13.811   46.832   1.00 84.54  ? 221 THR   D CG2    1 
ATOM   11901 N  N      . TYR   D 2  222 ? 10.832  12.371   44.138   1.00 76.82  ? 222 TYR   D N      1 
ATOM   11902 C  CA     . TYR   D 2  222 ? 11.709  11.329   43.636   1.00 68.85  ? 222 TYR   D CA     1 
ATOM   11903 C  C      . TYR   D 2  222 ? 11.130  9.940    43.871   1.00 74.63  ? 222 TYR   D C      1 
ATOM   11904 O  O      . TYR   D 2  222 ? 11.705  8.962    43.391   1.00 80.98  ? 222 TYR   D O      1 
ATOM   11905 C  CB     . TYR   D 2  222 ? 13.084  11.423   44.291   1.00 64.44  ? 222 TYR   D CB     1 
ATOM   11906 C  CG     . TYR   D 2  222 ? 14.008  12.447   43.678   1.00 67.79  ? 222 TYR   D CG     1 
ATOM   11907 C  CD1    . TYR   D 2  222 ? 13.947  12.747   42.327   1.00 73.18  ? 222 TYR   D CD1    1 
ATOM   11908 C  CD2    . TYR   D 2  222 ? 14.950  13.114   44.453   1.00 72.11  ? 222 TYR   D CD2    1 
ATOM   11909 C  CE1    . TYR   D 2  222 ? 14.796  13.683   41.769   1.00 74.74  ? 222 TYR   D CE1    1 
ATOM   11910 C  CE2    . TYR   D 2  222 ? 15.800  14.056   43.898   1.00 70.70  ? 222 TYR   D CE2    1 
ATOM   11911 C  CZ     . TYR   D 2  222 ? 15.716  14.330   42.558   1.00 72.44  ? 222 TYR   D CZ     1 
ATOM   11912 O  OH     . TYR   D 2  222 ? 16.551  15.263   41.996   1.00 80.57  ? 222 TYR   D OH     1 
ATOM   11913 N  N      . GLY   D 2  223 ? 10.010  9.820    44.578   1.00 74.25  ? 223 GLY   D N      1 
ATOM   11914 C  CA     . GLY   D 2  223 ? 9.366   8.531    44.740   1.00 74.00  ? 223 GLY   D CA     1 
ATOM   11915 C  C      . GLY   D 2  223 ? 8.238   8.322    43.756   1.00 78.53  ? 223 GLY   D C      1 
ATOM   11916 O  O      . GLY   D 2  223 ? 7.922   7.184    43.394   1.00 82.71  ? 223 GLY   D O      1 
ATOM   11917 N  N      . ASP   D 2  224 ? 7.606   9.419    43.339   1.00 79.27  ? 224 ASP   D N      1 
ATOM   11918 C  CA     . ASP   D 2  224 ? 6.604   9.362    42.285   1.00 79.74  ? 224 ASP   D CA     1 
ATOM   11919 C  C      . ASP   D 2  224 ? 7.255   9.213    40.922   1.00 79.39  ? 224 ASP   D C      1 
ATOM   11920 O  O      . ASP   D 2  224 ? 6.743   8.492    40.056   1.00 75.72  ? 224 ASP   D O      1 
ATOM   11921 C  CB     . ASP   D 2  224 ? 5.747   10.622   42.316   1.00 82.77  ? 224 ASP   D CB     1 
ATOM   11922 C  CG     . ASP   D 2  224 ? 4.541   10.473   43.194   1.00 84.91  ? 224 ASP   D CG     1 
ATOM   11923 O  OD1    . ASP   D 2  224 ? 3.873   9.415    43.113   1.00 82.21  ? 224 ASP   D OD1    1 
ATOM   11924 O  OD2    . ASP   D 2  224 ? 4.277   11.415   43.972   1.00 87.00  ? 224 ASP   D OD2    1 
ATOM   11925 N  N      . LEU   D 2  225 ? 8.366   9.919    40.710   1.00 77.43  ? 225 LEU   D N      1 
ATOM   11926 C  CA     . LEU   D 2  225 ? 9.191   9.670    39.538   1.00 74.38  ? 225 LEU   D CA     1 
ATOM   11927 C  C      . LEU   D 2  225 ? 9.573   8.200    39.471   1.00 75.30  ? 225 LEU   D C      1 
ATOM   11928 O  O      . LEU   D 2  225 ? 9.149   7.472    38.565   1.00 74.67  ? 225 LEU   D O      1 
ATOM   11929 C  CB     . LEU   D 2  225 ? 10.430  10.560   39.589   1.00 66.71  ? 225 LEU   D CB     1 
ATOM   11930 C  CG     . LEU   D 2  225 ? 10.297  11.805   38.738   1.00 68.31  ? 225 LEU   D CG     1 
ATOM   11931 C  CD1    . LEU   D 2  225 ? 8.918   12.386   38.995   1.00 80.01  ? 225 LEU   D CD1    1 
ATOM   11932 C  CD2    . LEU   D 2  225 ? 11.402  12.803   39.067   1.00 66.32  ? 225 LEU   D CD2    1 
ATOM   11933 N  N      . ASN   D 2  226 ? 10.325  7.732    40.470   1.00 71.77  ? 226 ASN   D N      1 
ATOM   11934 C  CA     . ASN   D 2  226 ? 10.863  6.381    40.445   1.00 64.96  ? 226 ASN   D CA     1 
ATOM   11935 C  C      . ASN   D 2  226 ? 9.769   5.327    40.322   1.00 67.08  ? 226 ASN   D C      1 
ATOM   11936 O  O      . ASN   D 2  226 ? 10.062  4.182    39.968   1.00 69.63  ? 226 ASN   D O      1 
ATOM   11937 C  CB     . ASN   D 2  226 ? 11.725  6.161    41.691   1.00 60.87  ? 226 ASN   D CB     1 
ATOM   11938 C  CG     . ASN   D 2  226 ? 13.046  6.994    41.666   1.00 73.11  ? 226 ASN   D CG     1 
ATOM   11939 O  OD1    . ASN   D 2  226 ? 13.467  7.535    40.632   1.00 70.97  ? 226 ASN   D OD1    1 
ATOM   11940 N  ND2    . ASN   D 2  226 ? 13.683  7.105    42.826   1.00 70.42  ? 226 ASN   D ND2    1 
ATOM   11941 N  N      . HIS   D 2  227 ? 8.509   5.682    40.577   1.00 70.35  ? 227 HIS   D N      1 
ATOM   11942 C  CA     . HIS   D 2  227 ? 7.424   4.744    40.290   1.00 74.72  ? 227 HIS   D CA     1 
ATOM   11943 C  C      . HIS   D 2  227 ? 7.277   4.519    38.790   1.00 77.56  ? 227 HIS   D C      1 
ATOM   11944 O  O      . HIS   D 2  227 ? 6.918   3.414    38.355   1.00 74.42  ? 227 HIS   D O      1 
ATOM   11945 C  CB     . HIS   D 2  227 ? 6.104   5.254    40.877   1.00 76.41  ? 227 HIS   D CB     1 
ATOM   11946 C  CG     . HIS   D 2  227 ? 4.936   4.347    40.624   1.00 86.04  ? 227 HIS   D CG     1 
ATOM   11947 N  ND1    . HIS   D 2  227 ? 3.926   4.660    39.733   1.00 81.96  ? 227 HIS   D ND1    1 
ATOM   11948 C  CD2    . HIS   D 2  227 ? 4.604   3.149    41.165   1.00 86.68  ? 227 HIS   D CD2    1 
ATOM   11949 C  CE1    . HIS   D 2  227 ? 3.034   3.684    39.725   1.00 86.08  ? 227 HIS   D CE1    1 
ATOM   11950 N  NE2    . HIS   D 2  227 ? 3.421   2.757    40.585   1.00 93.42  ? 227 HIS   D NE2    1 
ATOM   11951 N  N      . LEU   D 2  228 ? 7.541   5.561    37.993   1.00 74.24  ? 228 LEU   D N      1 
ATOM   11952 C  CA     . LEU   D 2  228 ? 7.513   5.426    36.544   1.00 70.60  ? 228 LEU   D CA     1 
ATOM   11953 C  C      . LEU   D 2  228 ? 8.674   4.556    36.069   1.00 73.08  ? 228 LEU   D C      1 
ATOM   11954 O  O      . LEU   D 2  228 ? 8.483   3.633    35.266   1.00 71.56  ? 228 LEU   D O      1 
ATOM   11955 C  CB     . LEU   D 2  228 ? 7.557   6.814    35.887   1.00 72.15  ? 228 LEU   D CB     1 
ATOM   11956 C  CG     . LEU   D 2  228 ? 6.443   7.831    36.194   1.00 63.57  ? 228 LEU   D CG     1 
ATOM   11957 C  CD1    . LEU   D 2  228 ? 6.664   9.110    35.422   1.00 60.08  ? 228 LEU   D CD1    1 
ATOM   11958 C  CD2    . LEU   D 2  228 ? 5.050   7.279    35.920   1.00 65.12  ? 228 LEU   D CD2    1 
ATOM   11959 N  N      . VAL   D 2  229 ? 9.883   4.813    36.593   1.00 69.37  ? 229 VAL   D N      1 
ATOM   11960 C  CA     . VAL   D 2  229 ? 11.068  4.056    36.190   1.00 64.21  ? 229 VAL   D CA     1 
ATOM   11961 C  C      . VAL   D 2  229 ? 10.911  2.575    36.515   1.00 60.76  ? 229 VAL   D C      1 
ATOM   11962 O  O      . VAL   D 2  229 ? 11.241  1.709    35.699   1.00 64.97  ? 229 VAL   D O      1 
ATOM   11963 C  CB     . VAL   D 2  229 ? 12.334  4.659    36.830   1.00 63.23  ? 229 VAL   D CB     1 
ATOM   11964 C  CG1    . VAL   D 2  229 ? 13.582  3.953    36.328   1.00 61.16  ? 229 VAL   D CG1    1 
ATOM   11965 C  CG2    . VAL   D 2  229 ? 12.436  6.126    36.461   1.00 61.76  ? 229 VAL   D CG2    1 
ATOM   11966 N  N      . SER   D 2  230 ? 10.383  2.251    37.687   1.00 62.38  ? 230 SER   D N      1 
ATOM   11967 C  CA     . SER   D 2  230 ? 10.213  0.839    38.006   1.00 65.99  ? 230 SER   D CA     1 
ATOM   11968 C  C      . SER   D 2  230 ? 9.256   0.159    37.022   1.00 62.72  ? 230 SER   D C      1 
ATOM   11969 O  O      . SER   D 2  230 ? 9.445   -1.013   36.675   1.00 59.52  ? 230 SER   D O      1 
ATOM   11970 C  CB     . SER   D 2  230 ? 9.747   0.687    39.455   1.00 60.87  ? 230 SER   D CB     1 
ATOM   11971 O  OG     . SER   D 2  230 ? 8.336   0.660    39.531   1.00 72.06  ? 230 SER   D OG     1 
ATOM   11972 N  N      . ALA   D 2  231 ? 8.236   0.883    36.544   1.00 64.85  ? 231 ALA   D N      1 
ATOM   11973 C  CA     . ALA   D 2  231 ? 7.310   0.313    35.562   1.00 65.21  ? 231 ALA   D CA     1 
ATOM   11974 C  C      . ALA   D 2  231 ? 8.003   0.073    34.227   1.00 62.65  ? 231 ALA   D C      1 
ATOM   11975 O  O      . ALA   D 2  231 ? 7.859   -0.995   33.624   1.00 56.13  ? 231 ALA   D O      1 
ATOM   11976 C  CB     . ALA   D 2  231 ? 6.110   1.237    35.361   1.00 65.28  ? 231 ALA   D CB     1 
ATOM   11977 N  N      . THR   D 2  232 ? 8.733   1.082    33.741   1.00 58.62  ? 232 THR   D N      1 
ATOM   11978 C  CA     . THR   D 2  232 ? 9.565   0.940    32.554   1.00 56.89  ? 232 THR   D CA     1 
ATOM   11979 C  C      . THR   D 2  232 ? 10.544  -0.226   32.672   1.00 61.85  ? 232 THR   D C      1 
ATOM   11980 O  O      . THR   D 2  232 ? 10.666  -1.044   31.752   1.00 59.34  ? 232 THR   D O      1 
ATOM   11981 C  CB     . THR   D 2  232 ? 10.327  2.238    32.326   1.00 57.90  ? 232 THR   D CB     1 
ATOM   11982 O  OG1    . THR   D 2  232 ? 9.391   3.322    32.265   1.00 61.00  ? 232 THR   D OG1    1 
ATOM   11983 C  CG2    . THR   D 2  232 ? 11.166  2.159    31.036   1.00 53.60  ? 232 THR   D CG2    1 
ATOM   11984 N  N      . MET   D 2  233 ? 11.268  -0.306   33.795   1.00 61.59  ? 233 MET   D N      1 
ATOM   11985 C  CA     . MET   D 2  233 ? 12.352  -1.275   33.899   1.00 59.85  ? 233 MET   D CA     1 
ATOM   11986 C  C      . MET   D 2  233 ? 11.836  -2.696   34.087   1.00 61.28  ? 233 MET   D C      1 
ATOM   11987 O  O      . MET   D 2  233 ? 12.492  -3.653   33.648   1.00 57.68  ? 233 MET   D O      1 
ATOM   11988 C  CB     . MET   D 2  233 ? 13.295  -0.895   35.034   1.00 58.57  ? 233 MET   D CB     1 
ATOM   11989 C  CG     . MET   D 2  233 ? 13.965  0.452    34.851   1.00 63.07  ? 233 MET   D CG     1 
ATOM   11990 S  SD     . MET   D 2  233 ? 15.469  0.610    35.844   1.00 70.28  ? 233 MET   D SD     1 
ATOM   11991 C  CE     . MET   D 2  233 ? 15.716  -1.059   36.463   1.00 57.97  ? 233 MET   D CE     1 
ATOM   11992 N  N      . SER   D 2  234 ? 10.676  -2.869   34.724   1.00 55.67  ? 234 SER   D N      1 
ATOM   11993 C  CA     . SER   D 2  234 ? 10.072  -4.189   34.675   1.00 58.31  ? 234 SER   D CA     1 
ATOM   11994 C  C      . SER   D 2  234 ? 9.673   -4.541   33.241   1.00 64.73  ? 234 SER   D C      1 
ATOM   11995 O  O      . SER   D 2  234 ? 9.729   -5.715   32.855   1.00 65.60  ? 234 SER   D O      1 
ATOM   11996 C  CB     . SER   D 2  234 ? 8.868   -4.265   35.602   1.00 56.10  ? 234 SER   D CB     1 
ATOM   11997 O  OG     . SER   D 2  234 ? 7.969   -5.273   35.167   1.00 62.12  ? 234 SER   D OG     1 
ATOM   11998 N  N      . GLY   D 2  235 ? 9.329   -3.531   32.433   1.00 58.48  ? 235 GLY   D N      1 
ATOM   11999 C  CA     . GLY   D 2  235 ? 8.829   -3.786   31.097   1.00 57.95  ? 235 GLY   D CA     1 
ATOM   12000 C  C      . GLY   D 2  235 ? 9.918   -4.171   30.115   1.00 61.51  ? 235 GLY   D C      1 
ATOM   12001 O  O      . GLY   D 2  235 ? 9.798   -5.188   29.428   1.00 61.09  ? 235 GLY   D O      1 
ATOM   12002 N  N      . VAL   D 2  236 ? 10.999  -3.381   30.044   1.00 59.12  ? 236 VAL   D N      1 
ATOM   12003 C  CA     . VAL   D 2  236 ? 12.054  -3.590   29.052   1.00 55.66  ? 236 VAL   D CA     1 
ATOM   12004 C  C      . VAL   D 2  236 ? 12.909  -4.804   29.400   1.00 59.32  ? 236 VAL   D C      1 
ATOM   12005 O  O      . VAL   D 2  236 ? 13.922  -5.061   28.743   1.00 60.97  ? 236 VAL   D O      1 
ATOM   12006 C  CB     . VAL   D 2  236 ? 12.947  -2.341   28.902   1.00 50.09  ? 236 VAL   D CB     1 
ATOM   12007 C  CG1    . VAL   D 2  236 ? 12.123  -1.098   28.621   1.00 49.68  ? 236 VAL   D CG1    1 
ATOM   12008 C  CG2    . VAL   D 2  236 ? 13.862  -2.168   30.111   1.00 53.08  ? 236 VAL   D CG2    1 
ATOM   12009 N  N      . THR   D 2  237 ? 12.520  -5.554   30.433   1.00 61.55  ? 237 THR   D N      1 
ATOM   12010 C  CA     . THR   D 2  237 ? 13.200  -6.791   30.793   1.00 56.68  ? 237 THR   D CA     1 
ATOM   12011 C  C      . THR   D 2  237 ? 12.263  -7.992   30.809   1.00 60.03  ? 237 THR   D C      1 
ATOM   12012 O  O      . THR   D 2  237 ? 12.710  -9.103   31.115   1.00 59.29  ? 237 THR   D O      1 
ATOM   12013 C  CB     . THR   D 2  237 ? 13.898  -6.656   32.164   1.00 59.87  ? 237 THR   D CB     1 
ATOM   12014 O  OG1    . THR   D 2  237 ? 12.925  -6.428   33.203   1.00 61.54  ? 237 THR   D OG1    1 
ATOM   12015 C  CG2    . THR   D 2  237 ? 14.920  -5.513   32.146   1.00 49.89  ? 237 THR   D CG2    1 
ATOM   12016 N  N      . THR   D 2  238 ? 10.979  -7.807   30.482   1.00 58.09  ? 238 THR   D N      1 
ATOM   12017 C  CA     . THR   D 2  238 ? 10.058  -8.940   30.434   1.00 62.67  ? 238 THR   D CA     1 
ATOM   12018 C  C      . THR   D 2  238 ? 10.615  -10.084  29.597   1.00 62.77  ? 238 THR   D C      1 
ATOM   12019 O  O      . THR   D 2  238 ? 10.473  -11.258  29.957   1.00 66.62  ? 238 THR   D O      1 
ATOM   12020 C  CB     . THR   D 2  238 ? 8.708   -8.504   29.871   1.00 61.55  ? 238 THR   D CB     1 
ATOM   12021 O  OG1    . THR   D 2  238 ? 8.296   -7.302   30.529   1.00 68.97  ? 238 THR   D OG1    1 
ATOM   12022 C  CG2    . THR   D 2  238 ? 7.656   -9.596   30.102   1.00 61.98  ? 238 THR   D CG2    1 
ATOM   12023 N  N      . CYS   D 2  239 ? 11.231  -9.765   28.464   1.00 62.45  ? 239 CYS   D N      1 
ATOM   12024 C  CA     . CYS   D 2  239 ? 11.711  -10.798  27.564   1.00 63.42  ? 239 CYS   D CA     1 
ATOM   12025 C  C      . CYS   D 2  239 ? 13.064  -11.342  27.976   1.00 62.74  ? 239 CYS   D C      1 
ATOM   12026 O  O      . CYS   D 2  239 ? 13.484  -12.374  27.448   1.00 60.97  ? 239 CYS   D O      1 
ATOM   12027 C  CB     . CYS   D 2  239 ? 11.762  -10.251  26.146   1.00 62.96  ? 239 CYS   D CB     1 
ATOM   12028 S  SG     . CYS   D 2  239 ? 10.123  -9.848   25.566   1.00 67.29  ? 239 CYS   D SG     1 
ATOM   12029 N  N      . LEU   D 2  240 ? 13.753  -10.673  28.901   1.00 60.69  ? 240 LEU   D N      1 
ATOM   12030 C  CA     . LEU   D 2  240 ? 14.917  -11.284  29.526   1.00 59.61  ? 240 LEU   D CA     1 
ATOM   12031 C  C      . LEU   D 2  240 ? 14.496  -12.283  30.607   1.00 63.15  ? 240 LEU   D C      1 
ATOM   12032 O  O      . LEU   D 2  240 ? 15.063  -13.380  30.695   1.00 58.03  ? 240 LEU   D O      1 
ATOM   12033 C  CB     . LEU   D 2  240 ? 15.832  -10.198  30.102   1.00 55.92  ? 240 LEU   D CB     1 
ATOM   12034 C  CG     . LEU   D 2  240 ? 16.327  -9.123   29.125   1.00 52.95  ? 240 LEU   D CG     1 
ATOM   12035 C  CD1    . LEU   D 2  240 ? 16.943  -7.961   29.860   1.00 46.54  ? 240 LEU   D CD1    1 
ATOM   12036 C  CD2    . LEU   D 2  240 ? 17.321  -9.678   28.126   1.00 57.22  ? 240 LEU   D CD2    1 
ATOM   12037 N  N      . ARG   D 2  241 ? 13.453  -11.944  31.381   1.00 64.94  ? 241 ARG   D N      1 
ATOM   12038 C  CA     . ARG   D 2  241 ? 13.048  -12.660  32.591   1.00 66.12  ? 241 ARG   D CA     1 
ATOM   12039 C  C      . ARG   D 2  241 ? 12.023  -13.771  32.352   1.00 67.18  ? 241 ARG   D C      1 
ATOM   12040 O  O      . ARG   D 2  241 ? 11.981  -14.743  33.119   1.00 66.06  ? 241 ARG   D O      1 
ATOM   12041 C  CB     . ARG   D 2  241 ? 12.472  -11.667  33.615   1.00 59.67  ? 241 ARG   D CB     1 
ATOM   12042 C  CG     . ARG   D 2  241 ? 13.493  -10.689  34.166   1.00 58.36  ? 241 ARG   D CG     1 
ATOM   12043 C  CD     . ARG   D 2  241 ? 12.908  -9.754   35.208   1.00 60.39  ? 241 ARG   D CD     1 
ATOM   12044 N  NE     . ARG   D 2  241 ? 11.970  -8.758   34.700   1.00 65.15  ? 241 ARG   D NE     1 
ATOM   12045 C  CZ     . ARG   D 2  241 ? 10.679  -8.707   35.007   1.00 66.17  ? 241 ARG   D CZ     1 
ATOM   12046 N  NH1    . ARG   D 2  241 ? 10.089  -9.678   35.682   1.00 64.39  ? 241 ARG   D NH1    1 
ATOM   12047 N  NH2    . ARG   D 2  241 ? 9.960   -7.654   34.625   1.00 64.79  ? 241 ARG   D NH2    1 
ATOM   12048 N  N      . PHE   D 2  242 ? 11.177  -13.653  31.340   1.00 64.77  ? 242 PHE   D N      1 
ATOM   12049 C  CA     . PHE   D 2  242 ? 10.147  -14.666  31.232   1.00 66.10  ? 242 PHE   D CA     1 
ATOM   12050 C  C      . PHE   D 2  242 ? 10.295  -15.464  29.946   1.00 72.99  ? 242 PHE   D C      1 
ATOM   12051 O  O      . PHE   D 2  242 ? 10.745  -14.938  28.920   1.00 71.59  ? 242 PHE   D O      1 
ATOM   12052 C  CB     . PHE   D 2  242 ? 8.748   -14.048  31.268   1.00 71.57  ? 242 PHE   D CB     1 
ATOM   12053 C  CG     . PHE   D 2  242 ? 8.373   -13.475  32.595   1.00 70.58  ? 242 PHE   D CG     1 
ATOM   12054 C  CD1    . PHE   D 2  242 ? 8.024   -14.310  33.644   1.00 70.15  ? 242 PHE   D CD1    1 
ATOM   12055 C  CD2    . PHE   D 2  242 ? 8.351   -12.104  32.789   1.00 65.03  ? 242 PHE   D CD2    1 
ATOM   12056 C  CE1    . PHE   D 2  242 ? 7.674   -13.792  34.856   1.00 72.58  ? 242 PHE   D CE1    1 
ATOM   12057 C  CE2    . PHE   D 2  242 ? 8.009   -11.574  34.006   1.00 66.93  ? 242 PHE   D CE2    1 
ATOM   12058 C  CZ     . PHE   D 2  242 ? 7.669   -12.414  35.041   1.00 74.42  ? 242 PHE   D CZ     1 
ATOM   12059 N  N      . PRO   D 2  243 ? 9.904   -16.734  29.971   1.00 76.57  ? 243 PRO   D N      1 
ATOM   12060 C  CA     . PRO   D 2  243 ? 9.880   -17.523  28.735   1.00 84.07  ? 243 PRO   D CA     1 
ATOM   12061 C  C      . PRO   D 2  243 ? 8.964   -16.876  27.704   1.00 91.19  ? 243 PRO   D C      1 
ATOM   12062 O  O      . PRO   D 2  243 ? 7.899   -16.345  28.040   1.00 94.34  ? 243 PRO   D O      1 
ATOM   12063 C  CB     . PRO   D 2  243 ? 9.339   -18.887  29.193   1.00 83.15  ? 243 PRO   D CB     1 
ATOM   12064 C  CG     . PRO   D 2  243 ? 9.364   -18.858  30.707   1.00 72.32  ? 243 PRO   D CG     1 
ATOM   12065 C  CD     . PRO   D 2  243 ? 9.259   -17.430  31.098   1.00 74.15  ? 243 PRO   D CD     1 
ATOM   12066 N  N      . GLY   D 2  244 ? 9.383   -16.926  26.438   1.00 82.63  ? 244 GLY   D N      1 
ATOM   12067 C  CA     . GLY   D 2  244 ? 8.586   -16.345  25.374   1.00 83.50  ? 244 GLY   D CA     1 
ATOM   12068 C  C      . GLY   D 2  244 ? 8.792   -17.042  24.048   1.00 85.86  ? 244 GLY   D C      1 
ATOM   12069 O  O      . GLY   D 2  244 ? 9.369   -18.132  24.012   1.00 80.69  ? 244 GLY   D O      1 
ATOM   12070 N  N      . GLN   D 2  245 ? 8.318   -16.443  22.949   1.00 87.85  ? 245 GLN   D N      1 
ATOM   12071 C  CA     . GLN   D 2  245 ? 8.693   -16.962  21.636   1.00 82.01  ? 245 GLN   D CA     1 
ATOM   12072 C  C      . GLN   D 2  245 ? 10.175  -16.729  21.385   1.00 75.74  ? 245 GLN   D C      1 
ATOM   12073 O  O      . GLN   D 2  245 ? 10.924  -17.675  21.107   1.00 76.86  ? 245 GLN   D O      1 
ATOM   12074 C  CB     . GLN   D 2  245 ? 7.849   -16.322  20.530   1.00 79.66  ? 245 GLN   D CB     1 
ATOM   12075 C  CG     . GLN   D 2  245 ? 7.466   -17.250  19.343   1.00 79.10  ? 245 GLN   D CG     1 
ATOM   12076 C  CD     . GLN   D 2  245 ? 6.675   -18.530  19.721   1.00 87.42  ? 245 GLN   D CD     1 
ATOM   12077 O  OE1    . GLN   D 2  245 ? 6.768   -19.036  20.853   1.00 84.10  ? 245 GLN   D OE1    1 
ATOM   12078 N  NE2    . GLN   D 2  245 ? 5.868   -19.039  18.761   1.00 73.90  ? 245 GLN   D NE2    1 
ATOM   12079 N  N      . LEU   D 2  246 ? 10.631  -15.486  21.533   1.00 69.86  ? 246 LEU   D N      1 
ATOM   12080 C  CA     . LEU   D 2  246 ? 12.027  -15.156  21.268   1.00 73.38  ? 246 LEU   D CA     1 
ATOM   12081 C  C      . LEU   D 2  246 ? 12.872  -15.304  22.532   1.00 75.09  ? 246 LEU   D C      1 
ATOM   12082 O  O      . LEU   D 2  246 ? 12.497  -14.824  23.611   1.00 76.73  ? 246 LEU   D O      1 
ATOM   12083 C  CB     . LEU   D 2  246 ? 12.164  -13.750  20.669   1.00 64.43  ? 246 LEU   D CB     1 
ATOM   12084 C  CG     . LEU   D 2  246 ? 11.456  -12.509  21.200   1.00 59.80  ? 246 LEU   D CG     1 
ATOM   12085 C  CD1    . LEU   D 2  246 ? 12.339  -11.829  22.191   1.00 62.86  ? 246 LEU   D CD1    1 
ATOM   12086 C  CD2    . LEU   D 2  246 ? 11.152  -11.565  20.065   1.00 55.46  ? 246 LEU   D CD2    1 
ATOM   12087 N  N      . ASN   D 2  247 ? 14.012  -15.987  22.380   1.00 72.66  ? 247 ASN   D N      1 
ATOM   12088 C  CA     . ASN   D 2  247 ? 14.936  -16.315  23.472   1.00 72.32  ? 247 ASN   D CA     1 
ATOM   12089 C  C      . ASN   D 2  247 ? 15.760  -15.085  23.833   1.00 67.39  ? 247 ASN   D C      1 
ATOM   12090 O  O      . ASN   D 2  247 ? 16.983  -15.060  23.676   1.00 74.65  ? 247 ASN   D O      1 
ATOM   12091 C  CB     . ASN   D 2  247 ? 15.865  -17.455  23.052   1.00 74.84  ? 247 ASN   D CB     1 
ATOM   12092 C  CG     . ASN   D 2  247 ? 15.638  -18.742  23.836   1.00 79.09  ? 247 ASN   D CG     1 
ATOM   12093 O  OD1    . ASN   D 2  247 ? 15.462  -18.723  25.067   1.00 77.95  ? 247 ASN   D OD1    1 
ATOM   12094 N  ND2    . ASN   D 2  247 ? 15.623  -19.880  23.112   1.00 65.71  ? 247 ASN   D ND2    1 
ATOM   12095 N  N      . ALA   D 2  248 ? 15.076  -14.048  24.304   1.00 56.11  ? 248 ALA   D N      1 
ATOM   12096 C  CA     . ALA   D 2  248 ? 15.718  -12.745  24.353   1.00 54.31  ? 248 ALA   D CA     1 
ATOM   12097 C  C      . ALA   D 2  248 ? 16.874  -12.757  25.343   1.00 54.27  ? 248 ALA   D C      1 
ATOM   12098 O  O      . ALA   D 2  248 ? 16.795  -13.388  26.399   1.00 56.29  ? 248 ALA   D O      1 
ATOM   12099 C  CB     . ALA   D 2  248 ? 14.706  -11.665  24.714   1.00 62.24  ? 248 ALA   D CB     1 
ATOM   12100 N  N      . ASP   D 2  249 ? 17.966  -12.088  24.969   1.00 46.63  ? 249 ASP   D N      1 
ATOM   12101 C  CA     . ASP   D 2  249 ? 19.092  -11.837  25.854   1.00 46.60  ? 249 ASP   D CA     1 
ATOM   12102 C  C      . ASP   D 2  249 ? 19.731  -10.512  25.447   1.00 44.76  ? 249 ASP   D C      1 
ATOM   12103 O  O      . ASP   D 2  249 ? 19.375  -9.917   24.435   1.00 46.81  ? 249 ASP   D O      1 
ATOM   12104 C  CB     . ASP   D 2  249 ? 20.092  -12.996  25.833   1.00 46.96  ? 249 ASP   D CB     1 
ATOM   12105 C  CG     . ASP   D 2  249 ? 20.701  -13.220  24.475   1.00 48.73  ? 249 ASP   D CG     1 
ATOM   12106 O  OD1    . ASP   D 2  249 ? 21.199  -12.254  23.874   1.00 43.74  ? 249 ASP   D OD1    1 
ATOM   12107 O  OD2    . ASP   D 2  249 ? 20.682  -14.371  23.997   1.00 60.23  ? 249 ASP   D OD2    1 
ATOM   12108 N  N      . LEU   D 2  250 ? 20.683  -10.040  26.245   1.00 45.40  ? 250 LEU   D N      1 
ATOM   12109 C  CA     . LEU   D 2  250 ? 21.138  -8.665   26.078   1.00 46.49  ? 250 LEU   D CA     1 
ATOM   12110 C  C      . LEU   D 2  250 ? 21.820  -8.420   24.740   1.00 45.51  ? 250 LEU   D C      1 
ATOM   12111 O  O      . LEU   D 2  250 ? 21.869  -7.271   24.293   1.00 46.47  ? 250 LEU   D O      1 
ATOM   12112 C  CB     . LEU   D 2  250 ? 22.076  -8.270   27.232   1.00 52.87  ? 250 LEU   D CB     1 
ATOM   12113 C  CG     . LEU   D 2  250 ? 21.403  -7.839   28.553   1.00 50.55  ? 250 LEU   D CG     1 
ATOM   12114 C  CD1    . LEU   D 2  250 ? 22.389  -7.882   29.672   1.00 52.35  ? 250 LEU   D CD1    1 
ATOM   12115 C  CD2    . LEU   D 2  250 ? 20.758  -6.452   28.467   1.00 44.10  ? 250 LEU   D CD2    1 
ATOM   12116 N  N      . ARG   D 2  251 ? 22.344  -9.464   24.091   1.00 48.10  ? 251 ARG   D N      1 
ATOM   12117 C  CA     . ARG   D 2  251 ? 22.996  -9.300   22.792   1.00 45.67  ? 251 ARG   D CA     1 
ATOM   12118 C  C      . ARG   D 2  251 ? 21.997  -9.379   21.639   1.00 46.62  ? 251 ARG   D C      1 
ATOM   12119 O  O      . ARG   D 2  251 ? 22.088  -8.609   20.672   1.00 45.31  ? 251 ARG   D O      1 
ATOM   12120 C  CB     . ARG   D 2  251 ? 24.081  -10.357  22.603   1.00 42.30  ? 251 ARG   D CB     1 
ATOM   12121 C  CG     . ARG   D 2  251 ? 24.805  -10.247  21.266   1.00 42.86  ? 251 ARG   D CG     1 
ATOM   12122 C  CD     . ARG   D 2  251 ? 25.943  -11.259  21.154   1.00 44.64  ? 251 ARG   D CD     1 
ATOM   12123 N  NE     . ARG   D 2  251 ? 27.106  -10.833  21.922   1.00 45.64  ? 251 ARG   D NE     1 
ATOM   12124 C  CZ     . ARG   D 2  251 ? 27.512  -11.404  23.050   1.00 50.23  ? 251 ARG   D CZ     1 
ATOM   12125 N  NH1    . ARG   D 2  251 ? 26.911  -12.481  23.542   1.00 49.98  ? 251 ARG   D NH1    1 
ATOM   12126 N  NH2    . ARG   D 2  251 ? 28.540  -10.875  23.706   1.00 55.35  ? 251 ARG   D NH2    1 
ATOM   12127 N  N      . LYS   D 2  252 ? 21.061  -10.326  21.693   1.00 44.00  ? 252 LYS   D N      1 
ATOM   12128 C  CA     . LYS   D 2  252 ? 20.032  -10.350  20.669   1.00 43.36  ? 252 LYS   D CA     1 
ATOM   12129 C  C      . LYS   D 2  252 ? 19.264  -9.033   20.657   1.00 47.62  ? 252 LYS   D C      1 
ATOM   12130 O  O      . LYS   D 2  252 ? 18.871  -8.541   19.593   1.00 44.10  ? 252 LYS   D O      1 
ATOM   12131 C  CB     . LYS   D 2  252 ? 19.101  -11.535  20.894   1.00 48.61  ? 252 LYS   D CB     1 
ATOM   12132 C  CG     . LYS   D 2  252 ? 19.443  -12.788  20.122   1.00 42.16  ? 252 LYS   D CG     1 
ATOM   12133 C  CD     . LYS   D 2  252 ? 19.122  -13.971  20.997   1.00 48.53  ? 252 LYS   D CD     1 
ATOM   12134 C  CE     . LYS   D 2  252 ? 18.917  -15.240  20.220   1.00 47.75  ? 252 LYS   D CE     1 
ATOM   12135 N  NZ     . LYS   D 2  252 ? 18.161  -16.206  21.081   1.00 55.97  ? 252 LYS   D NZ     1 
ATOM   12136 N  N      . LEU   D 2  253 ? 19.054  -8.434   21.831   1.00 51.26  ? 253 LEU   D N      1 
ATOM   12137 C  CA     . LEU   D 2  253 ? 18.475  -7.094   21.868   1.00 51.86  ? 253 LEU   D CA     1 
ATOM   12138 C  C      . LEU   D 2  253 ? 19.351  -6.113   21.113   1.00 42.32  ? 253 LEU   D C      1 
ATOM   12139 O  O      . LEU   D 2  253 ? 18.872  -5.356   20.267   1.00 40.26  ? 253 LEU   D O      1 
ATOM   12140 C  CB     . LEU   D 2  253 ? 18.288  -6.632   23.313   1.00 57.63  ? 253 LEU   D CB     1 
ATOM   12141 C  CG     . LEU   D 2  253 ? 17.740  -5.212   23.480   1.00 53.38  ? 253 LEU   D CG     1 
ATOM   12142 C  CD1    . LEU   D 2  253 ? 16.291  -5.169   23.047   1.00 47.70  ? 253 LEU   D CD1    1 
ATOM   12143 C  CD2    . LEU   D 2  253 ? 17.918  -4.730   24.917   1.00 43.51  ? 253 LEU   D CD2    1 
ATOM   12144 N  N      . ALA   D 2  254 ? 20.655  -6.142   21.387   1.00 48.71  ? 254 ALA   D N      1 
ATOM   12145 C  CA     . ALA   D 2  254 ? 21.572  -5.170   20.793   1.00 49.76  ? 254 ALA   D CA     1 
ATOM   12146 C  C      . ALA   D 2  254 ? 21.683  -5.354   19.281   1.00 45.29  ? 254 ALA   D C      1 
ATOM   12147 O  O      . ALA   D 2  254 ? 21.558  -4.382   18.526   1.00 44.20  ? 254 ALA   D O      1 
ATOM   12148 C  CB     . ALA   D 2  254 ? 22.946  -5.271   21.462   1.00 45.09  ? 254 ALA   D CB     1 
ATOM   12149 N  N      . VAL   D 2  255 ? 21.923  -6.595   18.825   1.00 43.64  ? 255 VAL   D N      1 
ATOM   12150 C  CA     . VAL   D 2  255 ? 22.036  -6.894   17.393   1.00 41.39  ? 255 VAL   D CA     1 
ATOM   12151 C  C      . VAL   D 2  255 ? 20.857  -6.314   16.612   1.00 44.46  ? 255 VAL   D C      1 
ATOM   12152 O  O      . VAL   D 2  255 ? 21.030  -5.656   15.575   1.00 37.49  ? 255 VAL   D O      1 
ATOM   12153 C  CB     . VAL   D 2  255 ? 22.131  -8.412   17.179   1.00 44.83  ? 255 VAL   D CB     1 
ATOM   12154 C  CG1    . VAL   D 2  255 ? 22.021  -8.748   15.707   1.00 41.31  ? 255 VAL   D CG1    1 
ATOM   12155 C  CG2    . VAL   D 2  255 ? 23.415  -8.945   17.733   1.00 47.40  ? 255 VAL   D CG2    1 
ATOM   12156 N  N      . ASN   D 2  256 ? 19.637  -6.565   17.099   1.00 42.28  ? 256 ASN   D N      1 
ATOM   12157 C  CA     . ASN   D 2  256 ? 18.428  -6.212   16.364   1.00 43.98  ? 256 ASN   D CA     1 
ATOM   12158 C  C      . ASN   D 2  256 ? 18.041  -4.741   16.535   1.00 47.01  ? 256 ASN   D C      1 
ATOM   12159 O  O      . ASN   D 2  256 ? 17.427  -4.162   15.626   1.00 40.30  ? 256 ASN   D O      1 
ATOM   12160 C  CB     . ASN   D 2  256 ? 17.283  -7.140   16.796   1.00 40.12  ? 256 ASN   D CB     1 
ATOM   12161 C  CG     . ASN   D 2  256 ? 17.437  -8.544   16.226   1.00 38.11  ? 256 ASN   D CG     1 
ATOM   12162 O  OD1    . ASN   D 2  256 ? 17.206  -8.752   15.050   1.00 42.26  ? 256 ASN   D OD1    1 
ATOM   12163 N  ND2    . ASN   D 2  256 ? 17.861  -9.498   17.048   1.00 38.67  ? 256 ASN   D ND2    1 
ATOM   12164 N  N      . MET   D 2  257 ? 18.407  -4.122   17.672   1.00 48.20  ? 257 MET   D N      1 
ATOM   12165 C  CA     . MET   D 2  257 ? 18.035  -2.746   18.003   1.00 43.34  ? 257 MET   D CA     1 
ATOM   12166 C  C      . MET   D 2  257 ? 19.051  -1.704   17.537   1.00 43.53  ? 257 MET   D C      1 
ATOM   12167 O  O      . MET   D 2  257 ? 18.670  -0.554   17.314   1.00 45.06  ? 257 MET   D O      1 
ATOM   12168 C  CB     . MET   D 2  257 ? 17.842  -2.615   19.520   1.00 47.10  ? 257 MET   D CB     1 
ATOM   12169 C  CG     . MET   D 2  257 ? 16.416  -2.876   20.093   1.00 43.36  ? 257 MET   D CG     1 
ATOM   12170 S  SD     . MET   D 2  257 ? 15.015  -2.437   19.039   1.00 45.57  ? 257 MET   D SD     1 
ATOM   12171 C  CE     . MET   D 2  257 ? 14.683  -0.782   19.625   1.00 45.04  ? 257 MET   D CE     1 
ATOM   12172 N  N      . VAL   D 2  258 ? 20.320  -2.065   17.364   1.00 44.73  ? 258 VAL   D N      1 
ATOM   12173 C  CA     . VAL   D 2  258 ? 21.377  -1.070   17.167   1.00 44.49  ? 258 VAL   D CA     1 
ATOM   12174 C  C      . VAL   D 2  258 ? 21.984  -1.197   15.779   1.00 43.19  ? 258 VAL   D C      1 
ATOM   12175 O  O      . VAL   D 2  258 ? 22.923  -1.980   15.589   1.00 43.69  ? 258 VAL   D O      1 
ATOM   12176 C  CB     . VAL   D 2  258 ? 22.483  -1.197   18.230   1.00 45.00  ? 258 VAL   D CB     1 
ATOM   12177 C  CG1    . VAL   D 2  258 ? 23.508  -0.084   18.060   1.00 35.21  ? 258 VAL   D CG1    1 
ATOM   12178 C  CG2    . VAL   D 2  258 ? 21.878  -1.190   19.627   1.00 44.01  ? 258 VAL   D CG2    1 
ATOM   12179 N  N      . PRO   D 2  259 ? 21.502  -0.430   14.796   1.00 43.98  ? 259 PRO   D N      1 
ATOM   12180 C  CA     . PRO   D 2  259 ? 22.048  -0.523   13.434   1.00 42.20  ? 259 PRO   D CA     1 
ATOM   12181 C  C      . PRO   D 2  259 ? 23.375  0.196    13.244   1.00 42.67  ? 259 PRO   D C      1 
ATOM   12182 O  O      . PRO   D 2  259 ? 24.012  0.033    12.194   1.00 40.72  ? 259 PRO   D O      1 
ATOM   12183 C  CB     . PRO   D 2  259 ? 20.954  0.141    12.586   1.00 43.95  ? 259 PRO   D CB     1 
ATOM   12184 C  CG     . PRO   D 2  259 ? 20.372  1.175    13.528   1.00 45.75  ? 259 PRO   D CG     1 
ATOM   12185 C  CD     . PRO   D 2  259 ? 20.375  0.516    14.887   1.00 45.26  ? 259 PRO   D CD     1 
ATOM   12186 N  N      . PHE   D 2  260 ? 23.796  1.021    14.193   1.00 41.28  ? 260 PHE   D N      1 
ATOM   12187 C  CA     . PHE   D 2  260 ? 25.090  1.658    14.099   1.00 41.57  ? 260 PHE   D CA     1 
ATOM   12188 C  C      . PHE   D 2  260 ? 25.608  1.709    15.532   1.00 44.41  ? 260 PHE   D C      1 
ATOM   12189 O  O      . PHE   D 2  260 ? 24.838  2.034    16.459   1.00 44.55  ? 260 PHE   D O      1 
ATOM   12190 C  CB     . PHE   D 2  260 ? 25.007  3.042    13.459   1.00 30.92  ? 260 PHE   D CB     1 
ATOM   12191 C  CG     . PHE   D 2  260 ? 24.381  3.015    12.103   1.00 40.84  ? 260 PHE   D CG     1 
ATOM   12192 C  CD1    . PHE   D 2  260 ? 25.070  2.501    11.015   1.00 44.01  ? 260 PHE   D CD1    1 
ATOM   12193 C  CD2    . PHE   D 2  260 ? 23.076  3.449    11.907   1.00 50.82  ? 260 PHE   D CD2    1 
ATOM   12194 C  CE1    . PHE   D 2  260 ? 24.486  2.450    9.753    1.00 46.07  ? 260 PHE   D CE1    1 
ATOM   12195 C  CE2    . PHE   D 2  260 ? 22.473  3.397    10.636   1.00 44.74  ? 260 PHE   D CE2    1 
ATOM   12196 C  CZ     . PHE   D 2  260 ? 23.176  2.900    9.567    1.00 42.05  ? 260 PHE   D CZ     1 
ATOM   12197 N  N      . PRO   D 2  261 ? 26.874  1.355    15.760   1.00 43.79  ? 261 PRO   D N      1 
ATOM   12198 C  CA     . PRO   D 2  261 ? 27.326  1.133    17.153   1.00 44.22  ? 261 PRO   D CA     1 
ATOM   12199 C  C      . PRO   D 2  261 ? 26.991  2.296    18.081   1.00 45.37  ? 261 PRO   D C      1 
ATOM   12200 O  O      . PRO   D 2  261 ? 26.513  2.081    19.206   1.00 35.97  ? 261 PRO   D O      1 
ATOM   12201 C  CB     . PRO   D 2  261 ? 28.845  0.929    17.015   1.00 36.39  ? 261 PRO   D CB     1 
ATOM   12202 C  CG     . PRO   D 2  261 ? 29.161  0.966    15.588   1.00 43.67  ? 261 PRO   D CG     1 
ATOM   12203 C  CD     . PRO   D 2  261 ? 27.954  1.293    14.767   1.00 36.92  ? 261 PRO   D CD     1 
ATOM   12204 N  N      . ARG   D 2  262 ? 27.230  3.532    17.618   1.00 43.87  ? 262 ARG   D N      1 
ATOM   12205 C  CA     . ARG   D 2  262 ? 27.068  4.714    18.455   1.00 45.50  ? 262 ARG   D CA     1 
ATOM   12206 C  C      . ARG   D 2  262 ? 25.603  5.055    18.703   1.00 47.47  ? 262 ARG   D C      1 
ATOM   12207 O  O      . ARG   D 2  262 ? 25.269  5.575    19.776   1.00 50.21  ? 262 ARG   D O      1 
ATOM   12208 C  CB     . ARG   D 2  262 ? 27.797  5.892    17.811   1.00 45.90  ? 262 ARG   D CB     1 
ATOM   12209 C  CG     . ARG   D 2  262 ? 29.283  5.706    17.871   1.00 40.50  ? 262 ARG   D CG     1 
ATOM   12210 C  CD     . ARG   D 2  262 ? 29.993  6.577    16.903   1.00 43.13  ? 262 ARG   D CD     1 
ATOM   12211 N  NE     . ARG   D 2  262 ? 29.575  7.967    16.995   1.00 56.98  ? 262 ARG   D NE     1 
ATOM   12212 C  CZ     . ARG   D 2  262 ? 30.114  8.848    17.829   1.00 60.97  ? 262 ARG   D CZ     1 
ATOM   12213 N  NH1    . ARG   D 2  262 ? 31.044  8.490    18.707   1.00 54.39  ? 262 ARG   D NH1    1 
ATOM   12214 N  NH2    . ARG   D 2  262 ? 29.715  10.117   17.779   1.00 52.75  ? 262 ARG   D NH2    1 
ATOM   12215 N  N      . LEU   D 2  263 ? 24.721  4.769    17.743   1.00 49.21  ? 263 LEU   D N      1 
ATOM   12216 C  CA     . LEU   D 2  263 ? 23.299  5.113    17.837   1.00 52.44  ? 263 LEU   D CA     1 
ATOM   12217 C  C      . LEU   D 2  263 ? 22.527  4.071    18.652   1.00 48.90  ? 263 LEU   D C      1 
ATOM   12218 O  O      . LEU   D 2  263 ? 21.619  3.400    18.158   1.00 46.56  ? 263 LEU   D O      1 
ATOM   12219 C  CB     . LEU   D 2  263 ? 22.709  5.256    16.441   1.00 43.33  ? 263 LEU   D CB     1 
ATOM   12220 C  CG     . LEU   D 2  263 ? 23.509  6.193    15.543   1.00 47.24  ? 263 LEU   D CG     1 
ATOM   12221 C  CD1    . LEU   D 2  263 ? 22.685  6.579    14.316   1.00 45.06  ? 263 LEU   D CD1    1 
ATOM   12222 C  CD2    . LEU   D 2  263 ? 23.927  7.432    16.319   1.00 49.11  ? 263 LEU   D CD2    1 
ATOM   12223 N  N      . HIS   D 2  264 ? 22.891  3.970    19.933   1.00 46.12  ? 264 HIS   D N      1 
ATOM   12224 C  CA     . HIS   D 2  264 ? 22.350  2.953    20.829   1.00 51.86  ? 264 HIS   D CA     1 
ATOM   12225 C  C      . HIS   D 2  264 ? 21.624  3.550    22.032   1.00 53.21  ? 264 HIS   D C      1 
ATOM   12226 O  O      . HIS   D 2  264 ? 21.630  2.966    23.125   1.00 52.68  ? 264 HIS   D O      1 
ATOM   12227 C  CB     . HIS   D 2  264 ? 23.447  1.996    21.301   1.00 46.51  ? 264 HIS   D CB     1 
ATOM   12228 C  CG     . HIS   D 2  264 ? 24.533  2.648    22.103   1.00 51.01  ? 264 HIS   D CG     1 
ATOM   12229 N  ND1    . HIS   D 2  264 ? 25.761  2.970    21.569   1.00 51.44  ? 264 HIS   D ND1    1 
ATOM   12230 C  CD2    . HIS   D 2  264 ? 24.581  3.023    23.403   1.00 54.73  ? 264 HIS   D CD2    1 
ATOM   12231 C  CE1    . HIS   D 2  264 ? 26.516  3.520    22.503   1.00 50.03  ? 264 HIS   D CE1    1 
ATOM   12232 N  NE2    . HIS   D 2  264 ? 25.823  3.562    23.625   1.00 52.57  ? 264 HIS   D NE2    1 
ATOM   12233 N  N      . PHE   D 2  265 ? 20.947  4.692    21.852   1.00 52.93  ? 265 PHE   D N      1 
ATOM   12234 C  CA     . PHE   D 2  265 ? 20.249  5.361    22.954   1.00 51.04  ? 265 PHE   D CA     1 
ATOM   12235 C  C      . PHE   D 2  265 ? 18.745  5.259    22.733   1.00 51.84  ? 265 PHE   D C      1 
ATOM   12236 O  O      . PHE   D 2  265 ? 18.182  5.906    21.842   1.00 60.72  ? 265 PHE   D O      1 
ATOM   12237 C  CB     . PHE   D 2  265 ? 20.718  6.804    23.107   1.00 46.50  ? 265 PHE   D CB     1 
ATOM   12238 C  CG     . PHE   D 2  265 ? 22.137  6.904    23.550   1.00 49.80  ? 265 PHE   D CG     1 
ATOM   12239 C  CD1    . PHE   D 2  265 ? 22.488  6.592    24.861   1.00 55.57  ? 265 PHE   D CD1    1 
ATOM   12240 C  CD2    . PHE   D 2  265 ? 23.135  7.239    22.654   1.00 49.71  ? 265 PHE   D CD2    1 
ATOM   12241 C  CE1    . PHE   D 2  265 ? 23.811  6.645    25.280   1.00 52.34  ? 265 PHE   D CE1    1 
ATOM   12242 C  CE2    . PHE   D 2  265 ? 24.462  7.295    23.063   1.00 53.98  ? 265 PHE   D CE2    1 
ATOM   12243 C  CZ     . PHE   D 2  265 ? 24.800  7.000    24.376   1.00 52.46  ? 265 PHE   D CZ     1 
ATOM   12244 N  N      . PHE   D 2  266 ? 18.107  4.447    23.555   1.00 48.17  ? 266 PHE   D N      1 
ATOM   12245 C  CA     . PHE   D 2  266 ? 16.721  4.083    23.367   1.00 49.65  ? 266 PHE   D CA     1 
ATOM   12246 C  C      . PHE   D 2  266 ? 15.806  5.016    24.133   1.00 52.53  ? 266 PHE   D C      1 
ATOM   12247 O  O      . PHE   D 2  266 ? 16.094  5.381    25.276   1.00 56.08  ? 266 PHE   D O      1 
ATOM   12248 C  CB     . PHE   D 2  266 ? 16.469  2.650    23.837   1.00 50.48  ? 266 PHE   D CB     1 
ATOM   12249 C  CG     . PHE   D 2  266 ? 17.363  1.646    23.199   1.00 48.80  ? 266 PHE   D CG     1 
ATOM   12250 C  CD1    . PHE   D 2  266 ? 18.023  1.945    22.016   1.00 46.61  ? 266 PHE   D CD1    1 
ATOM   12251 C  CD2    . PHE   D 2  266 ? 17.534  0.399    23.770   1.00 43.18  ? 266 PHE   D CD2    1 
ATOM   12252 C  CE1    . PHE   D 2  266 ? 18.845  1.017    21.430   1.00 49.25  ? 266 PHE   D CE1    1 
ATOM   12253 C  CE2    . PHE   D 2  266 ? 18.354  -0.531   23.194   1.00 40.28  ? 266 PHE   D CE2    1 
ATOM   12254 C  CZ     . PHE   D 2  266 ? 19.009  -0.232   22.024   1.00 46.50  ? 266 PHE   D CZ     1 
ATOM   12255 N  N      . MET   D 2  267 ? 14.695  5.384    23.481   1.00 51.32  ? 267 MET   D N      1 
ATOM   12256 C  CA     . MET   D 2  267 ? 13.568  6.059    24.105   1.00 45.77  ? 267 MET   D CA     1 
ATOM   12257 C  C      . MET   D 2  267 ? 12.605  5.022    24.656   1.00 49.60  ? 267 MET   D C      1 
ATOM   12258 O  O      . MET   D 2  267 ? 12.000  4.287    23.873   1.00 49.44  ? 267 MET   D O      1 
ATOM   12259 C  CB     . MET   D 2  267 ? 12.866  6.917    23.082   1.00 53.22  ? 267 MET   D CB     1 
ATOM   12260 C  CG     . MET   D 2  267 ? 11.845  7.871    23.616   1.00 63.66  ? 267 MET   D CG     1 
ATOM   12261 S  SD     . MET   D 2  267 ? 11.134  8.740    22.211   1.00 73.35  ? 267 MET   D SD     1 
ATOM   12262 C  CE     . MET   D 2  267 ? 12.599  9.572    21.580   1.00 62.94  ? 267 MET   D CE     1 
ATOM   12263 N  N      . PRO   D 2  268 ? 12.416  4.924    25.959   1.00 53.45  ? 268 PRO   D N      1 
ATOM   12264 C  CA     . PRO   D 2  268 ? 11.447  3.965    26.494   1.00 45.56  ? 268 PRO   D CA     1 
ATOM   12265 C  C      . PRO   D 2  268 ? 10.048  4.568    26.563   1.00 50.61  ? 268 PRO   D C      1 
ATOM   12266 O  O      . PRO   D 2  268 ? 9.848   5.778    26.449   1.00 53.82  ? 268 PRO   D O      1 
ATOM   12267 C  CB     . PRO   D 2  268 ? 11.983  3.661    27.893   1.00 47.51  ? 268 PRO   D CB     1 
ATOM   12268 C  CG     . PRO   D 2  268 ? 13.324  4.387    27.971   1.00 55.63  ? 268 PRO   D CG     1 
ATOM   12269 C  CD     . PRO   D 2  268 ? 13.262  5.495    27.008   1.00 47.99  ? 268 PRO   D CD     1 
ATOM   12270 N  N      . GLY   D 2  269 ? 9.073   3.687    26.742   1.00 49.80  ? 269 GLY   D N      1 
ATOM   12271 C  CA     . GLY   D 2  269 ? 7.686   4.103    26.772   1.00 54.38  ? 269 GLY   D CA     1 
ATOM   12272 C  C      . GLY   D 2  269 ? 6.854   3.098    27.526   1.00 58.63  ? 269 GLY   D C      1 
ATOM   12273 O  O      . GLY   D 2  269 ? 7.169   1.903    27.555   1.00 59.54  ? 269 GLY   D O      1 
ATOM   12274 N  N      . PHE   D 2  270 ? 5.788   3.591    28.155   1.00 56.70  ? 270 PHE   D N      1 
ATOM   12275 C  CA     . PHE   D 2  270 ? 4.886   2.746    28.919   1.00 59.00  ? 270 PHE   D CA     1 
ATOM   12276 C  C      . PHE   D 2  270 ? 3.454   3.207    28.686   1.00 67.58  ? 270 PHE   D C      1 
ATOM   12277 O  O      . PHE   D 2  270 ? 3.197   4.361    28.329   1.00 64.44  ? 270 PHE   D O      1 
ATOM   12278 C  CB     . PHE   D 2  270 ? 5.233   2.778    30.414   1.00 61.67  ? 270 PHE   D CB     1 
ATOM   12279 C  CG     . PHE   D 2  270 ? 4.564   1.702    31.234   1.00 68.12  ? 270 PHE   D CG     1 
ATOM   12280 C  CD1    . PHE   D 2  270 ? 5.249   0.541    31.578   1.00 70.83  ? 270 PHE   D CD1    1 
ATOM   12281 C  CD2    . PHE   D 2  270 ? 3.276   1.875    31.724   1.00 74.82  ? 270 PHE   D CD2    1 
ATOM   12282 C  CE1    . PHE   D 2  270 ? 4.645   -0.454   32.352   1.00 68.87  ? 270 PHE   D CE1    1 
ATOM   12283 C  CE2    . PHE   D 2  270 ? 2.659   0.871    32.510   1.00 72.46  ? 270 PHE   D CE2    1 
ATOM   12284 C  CZ     . PHE   D 2  270 ? 3.354   -0.287   32.824   1.00 69.60  ? 270 PHE   D CZ     1 
ATOM   12285 N  N      . ALA   D 2  271 ? 2.526   2.267    28.849   1.00 68.87  ? 271 ALA   D N      1 
ATOM   12286 C  CA     . ALA   D 2  271 ? 1.097   2.533    28.809   1.00 69.03  ? 271 ALA   D CA     1 
ATOM   12287 C  C      . ALA   D 2  271 ? 0.424   1.379    29.524   1.00 71.07  ? 271 ALA   D C      1 
ATOM   12288 O  O      . ALA   D 2  271 ? 0.887   0.237    29.397   1.00 71.18  ? 271 ALA   D O      1 
ATOM   12289 C  CB     . ALA   D 2  271 ? 0.560   2.661    27.378   1.00 72.06  ? 271 ALA   D CB     1 
ATOM   12290 N  N      . PRO   D 2  272 ? -0.635  1.628    30.297   1.00 75.40  ? 272 PRO   D N      1 
ATOM   12291 C  CA     . PRO   D 2  272 ? -1.231  2.944    30.557   1.00 72.36  ? 272 PRO   D CA     1 
ATOM   12292 C  C      . PRO   D 2  272 ? -0.586  3.650    31.751   1.00 67.39  ? 272 PRO   D C      1 
ATOM   12293 O  O      . PRO   D 2  272 ? -0.027  3.006    32.629   1.00 66.75  ? 272 PRO   D O      1 
ATOM   12294 C  CB     . PRO   D 2  272 ? -2.698  2.587    30.795   1.00 71.43  ? 272 PRO   D CB     1 
ATOM   12295 C  CG     . PRO   D 2  272 ? -2.639  1.233    31.451   1.00 66.80  ? 272 PRO   D CG     1 
ATOM   12296 C  CD     . PRO   D 2  272 ? -1.429  0.536    30.890   1.00 68.51  ? 272 PRO   D CD     1 
ATOM   12297 N  N      . LEU   D 2  273 ? -0.628  4.978    31.792   1.00 73.27  ? 273 LEU   D N      1 
ATOM   12298 C  CA     . LEU   D 2  273 ? -0.203  5.727    32.972   1.00 71.78  ? 273 LEU   D CA     1 
ATOM   12299 C  C      . LEU   D 2  273 ? -1.427  6.186    33.773   1.00 68.34  ? 273 LEU   D C      1 
ATOM   12300 O  O      . LEU   D 2  273 ? -1.642  5.768    34.917   1.00 71.69  ? 273 LEU   D O      1 
ATOM   12301 C  CB     . LEU   D 2  273 ? 0.642   6.930    32.566   1.00 70.86  ? 273 LEU   D CB     1 
ATOM   12302 C  CG     . LEU   D 2  273 ? 1.608   6.715    31.408   1.00 69.49  ? 273 LEU   D CG     1 
ATOM   12303 C  CD1    . LEU   D 2  273 ? 2.053   8.067    30.875   1.00 72.24  ? 273 LEU   D CD1    1 
ATOM   12304 C  CD2    . LEU   D 2  273 ? 2.799   5.870    31.845   1.00 67.77  ? 273 LEU   D CD2    1 
ATOM   12305 N  N      . LEU   D 2  284 ? -8.536  -1.050   29.646   1.00 91.71  ? 284 LEU   D N      1 
ATOM   12306 C  CA     . LEU   D 2  284 ? -7.941  -0.571   28.394   1.00 88.45  ? 284 LEU   D CA     1 
ATOM   12307 C  C      . LEU   D 2  284 ? -8.048  -1.618   27.276   1.00 87.41  ? 284 LEU   D C      1 
ATOM   12308 O  O      . LEU   D 2  284 ? -8.125  -2.821   27.543   1.00 86.85  ? 284 LEU   D O      1 
ATOM   12309 C  CB     . LEU   D 2  284 ? -6.476  -0.185   28.612   1.00 78.35  ? 284 LEU   D CB     1 
ATOM   12310 C  CG     . LEU   D 2  284 ? -6.071  1.155    28.003   1.00 82.23  ? 284 LEU   D CG     1 
ATOM   12311 C  CD1    . LEU   D 2  284 ? -6.951  2.280    28.540   1.00 88.03  ? 284 LEU   D CD1    1 
ATOM   12312 C  CD2    . LEU   D 2  284 ? -4.606  1.439    28.279   1.00 79.56  ? 284 LEU   D CD2    1 
ATOM   12313 N  N      . THR   D 2  285 ? -8.059  -1.159   26.025   1.00 85.11  ? 285 THR   D N      1 
ATOM   12314 C  CA     . THR   D 2  285 ? -8.120  -2.052   24.876   1.00 83.15  ? 285 THR   D CA     1 
ATOM   12315 C  C      . THR   D 2  285 ? -6.798  -2.057   24.117   1.00 83.66  ? 285 THR   D C      1 
ATOM   12316 O  O      . THR   D 2  285 ? -6.000  -1.111   24.173   1.00 80.10  ? 285 THR   D O      1 
ATOM   12317 C  CB     . THR   D 2  285 ? -9.237  -1.663   23.904   1.00 84.86  ? 285 THR   D CB     1 
ATOM   12318 O  OG1    . THR   D 2  285 ? -9.268  -0.239   23.754   1.00 86.31  ? 285 THR   D OG1    1 
ATOM   12319 C  CG2    . THR   D 2  285 ? -10.582 -2.173   24.409   1.00 81.64  ? 285 THR   D CG2    1 
ATOM   12320 N  N      . VAL   D 2  286 ? -6.600  -3.142   23.375   1.00 82.76  ? 286 VAL   D N      1 
ATOM   12321 C  CA     . VAL   D 2  286 ? -5.381  -3.396   22.615   1.00 75.71  ? 286 VAL   D CA     1 
ATOM   12322 C  C      . VAL   D 2  286 ? -5.097  -2.252   21.645   1.00 74.93  ? 286 VAL   D C      1 
ATOM   12323 O  O      . VAL   D 2  286 ? -3.922  -1.968   21.370   1.00 74.67  ? 286 VAL   D O      1 
ATOM   12324 C  CB     . VAL   D 2  286 ? -5.486  -4.740   21.884   1.00 72.58  ? 286 VAL   D CB     1 
ATOM   12325 C  CG1    . VAL   D 2  286 ? -4.131  -5.175   21.378   1.00 69.06  ? 286 VAL   D CG1    1 
ATOM   12326 C  CG2    . VAL   D 2  286 ? -6.100  -5.784   22.814   1.00 73.55  ? 286 VAL   D CG2    1 
ATOM   12327 N  N      . PRO   D 2  287 ? -6.112  -1.575   21.083   1.00 75.43  ? 287 PRO   D N      1 
ATOM   12328 C  CA     . PRO   D 2  287 ? -5.815  -0.415   20.234   1.00 71.00  ? 287 PRO   D CA     1 
ATOM   12329 C  C      . PRO   D 2  287 ? -5.497  0.828    21.043   1.00 73.33  ? 287 PRO   D C      1 
ATOM   12330 O  O      . PRO   D 2  287 ? -4.680  1.647    20.615   1.00 74.91  ? 287 PRO   D O      1 
ATOM   12331 C  CB     . PRO   D 2  287 ? -7.100  -0.237   19.411   1.00 70.06  ? 287 PRO   D CB     1 
ATOM   12332 C  CG     . PRO   D 2  287 ? -7.769  -1.570   19.456   1.00 70.04  ? 287 PRO   D CG     1 
ATOM   12333 C  CD     . PRO   D 2  287 ? -7.481  -2.066   20.850   1.00 76.91  ? 287 PRO   D CD     1 
ATOM   12334 N  N      . GLU   D 2  288 ? -6.138  1.000    22.203   1.00 77.05  ? 288 GLU   D N      1 
ATOM   12335 C  CA     . GLU   D 2  288 ? -5.799  2.157    23.025   1.00 78.13  ? 288 GLU   D CA     1 
ATOM   12336 C  C      . GLU   D 2  288 ? -4.383  2.025    23.565   1.00 77.01  ? 288 GLU   D C      1 
ATOM   12337 O  O      . GLU   D 2  288 ? -3.605  2.990    23.538   1.00 75.49  ? 288 GLU   D O      1 
ATOM   12338 C  CB     . GLU   D 2  288 ? -6.798  2.335    24.170   1.00 81.87  ? 288 GLU   D CB     1 
ATOM   12339 C  CG     . GLU   D 2  288 ? -8.258  2.317    23.755   1.00 81.87  ? 288 GLU   D CG     1 
ATOM   12340 C  CD     . GLU   D 2  288 ? -9.223  2.450    24.939   1.00 88.99  ? 288 GLU   D CD     1 
ATOM   12341 O  OE1    . GLU   D 2  288 ? -9.192  1.584    25.846   1.00 85.63  ? 288 GLU   D OE1    1 
ATOM   12342 O  OE2    . GLU   D 2  288 ? -10.021 3.419    24.947   1.00 80.23  ? 288 GLU   D OE2    1 
ATOM   12343 N  N      . LEU   D 2  289 ? -4.026  0.832    24.046   1.00 75.59  ? 289 LEU   D N      1 
ATOM   12344 C  CA     . LEU   D 2  289 ? -2.643  0.585    24.432   1.00 74.45  ? 289 LEU   D CA     1 
ATOM   12345 C  C      . LEU   D 2  289 ? -1.704  1.086    23.345   1.00 72.40  ? 289 LEU   D C      1 
ATOM   12346 O  O      . LEU   D 2  289 ? -0.938  2.035    23.548   1.00 71.83  ? 289 LEU   D O      1 
ATOM   12347 C  CB     . LEU   D 2  289 ? -2.435  -0.907   24.688   1.00 66.66  ? 289 LEU   D CB     1 
ATOM   12348 C  CG     . LEU   D 2  289 ? -2.589  -1.398   26.123   1.00 68.45  ? 289 LEU   D CG     1 
ATOM   12349 C  CD1    . LEU   D 2  289 ? -2.682  -2.915   26.171   1.00 70.51  ? 289 LEU   D CD1    1 
ATOM   12350 C  CD2    . LEU   D 2  289 ? -1.426  -0.895   26.951   1.00 71.94  ? 289 LEU   D CD2    1 
ATOM   12351 N  N      . THR   D 2  290 ? -1.819  0.489    22.156   1.00 66.82  ? 290 THR   D N      1 
ATOM   12352 C  CA     . THR   D 2  290 ? -0.912  0.772    21.047   1.00 70.34  ? 290 THR   D CA     1 
ATOM   12353 C  C      . THR   D 2  290 ? -0.854  2.263    20.725   1.00 74.34  ? 290 THR   D C      1 
ATOM   12354 O  O      . THR   D 2  290 ? 0.234   2.831    20.547   1.00 69.86  ? 290 THR   D O      1 
ATOM   12355 C  CB     . THR   D 2  290 ? -1.354  -0.029   19.824   1.00 66.85  ? 290 THR   D CB     1 
ATOM   12356 O  OG1    . THR   D 2  290 ? -1.822  -1.315   20.242   1.00 65.57  ? 290 THR   D OG1    1 
ATOM   12357 C  CG2    . THR   D 2  290 ? -0.215  -0.216   18.871   1.00 64.83  ? 290 THR   D CG2    1 
ATOM   12358 N  N      . GLN   D 2  291 ? -2.019  2.909    20.611   1.00 71.78  ? 291 GLN   D N      1 
ATOM   12359 C  CA     . GLN   D 2  291 ? -2.050  4.351    20.400   1.00 72.94  ? 291 GLN   D CA     1 
ATOM   12360 C  C      . GLN   D 2  291 ? -1.241  5.076    21.471   1.00 75.69  ? 291 GLN   D C      1 
ATOM   12361 O  O      . GLN   D 2  291 ? -0.356  5.880    21.155   1.00 72.12  ? 291 GLN   D O      1 
ATOM   12362 C  CB     . GLN   D 2  291 ? -3.499  4.842    20.386   1.00 77.55  ? 291 GLN   D CB     1 
ATOM   12363 C  CG     . GLN   D 2  291 ? -3.711  6.203    19.714   1.00 86.15  ? 291 GLN   D CG     1 
ATOM   12364 C  CD     . GLN   D 2  291 ? -4.594  6.123    18.480   1.00 88.13  ? 291 GLN   D CD     1 
ATOM   12365 O  OE1    . GLN   D 2  291 ? -4.535  5.151    17.721   1.00 92.78  ? 291 GLN   D OE1    1 
ATOM   12366 N  NE2    . GLN   D 2  291 ? -5.439  7.131    18.290   1.00 82.53  ? 291 GLN   D NE2    1 
ATOM   12367 N  N      . GLN   D 2  292 ? -1.537  4.794    22.749   1.00 73.12  ? 292 GLN   D N      1 
ATOM   12368 C  CA     . GLN   D 2  292 ? -0.829  5.438    23.854   1.00 72.39  ? 292 GLN   D CA     1 
ATOM   12369 C  C      . GLN   D 2  292 ? 0.659   5.101    23.832   1.00 77.84  ? 292 GLN   D C      1 
ATOM   12370 O  O      . GLN   D 2  292 ? 1.508   5.982    24.029   1.00 74.71  ? 292 GLN   D O      1 
ATOM   12371 C  CB     . GLN   D 2  292 ? -1.449  5.016    25.190   1.00 73.00  ? 292 GLN   D CB     1 
ATOM   12372 C  CG     . GLN   D 2  292 ? -2.799  5.672    25.506   1.00 76.09  ? 292 GLN   D CG     1 
ATOM   12373 C  CD     . GLN   D 2  292 ? -3.629  4.892    26.534   1.00 76.11  ? 292 GLN   D CD     1 
ATOM   12374 O  OE1    . GLN   D 2  292 ? -3.118  4.422    27.553   1.00 77.79  ? 292 GLN   D OE1    1 
ATOM   12375 N  NE2    . GLN   D 2  292 ? -4.915  4.743    26.253   1.00 78.10  ? 292 GLN   D NE2    1 
ATOM   12376 N  N      . MET   D 2  293 ? 0.991   3.827    23.586   1.00 78.09  ? 293 MET   D N      1 
ATOM   12377 C  CA     . MET   D 2  293 ? 2.383   3.382    23.616   1.00 73.43  ? 293 MET   D CA     1 
ATOM   12378 C  C      . MET   D 2  293 ? 3.247   4.107    22.584   1.00 74.70  ? 293 MET   D C      1 
ATOM   12379 O  O      . MET   D 2  293 ? 4.458   4.277    22.797   1.00 69.25  ? 293 MET   D O      1 
ATOM   12380 C  CB     . MET   D 2  293 ? 2.441   1.874    23.382   1.00 70.67  ? 293 MET   D CB     1 
ATOM   12381 C  CG     . MET   D 2  293 ? 3.848   1.326    23.244   1.00 67.65  ? 293 MET   D CG     1 
ATOM   12382 S  SD     . MET   D 2  293 ? 3.847   -0.448   22.968   1.00 69.48  ? 293 MET   D SD     1 
ATOM   12383 C  CE     . MET   D 2  293 ? 2.708   -0.594   21.582   1.00 62.63  ? 293 MET   D CE     1 
ATOM   12384 N  N      . PHE   D 2  294 ? 2.666   4.506    21.452   1.00 70.50  ? 294 PHE   D N      1 
ATOM   12385 C  CA     . PHE   D 2  294 ? 3.380   5.307    20.469   1.00 69.63  ? 294 PHE   D CA     1 
ATOM   12386 C  C      . PHE   D 2  294 ? 3.167   6.799    20.674   1.00 72.77  ? 294 PHE   D C      1 
ATOM   12387 O  O      . PHE   D 2  294 ? 3.660   7.600    19.868   1.00 75.52  ? 294 PHE   D O      1 
ATOM   12388 C  CB     . PHE   D 2  294 ? 2.947   4.926    19.053   1.00 74.83  ? 294 PHE   D CB     1 
ATOM   12389 C  CG     . PHE   D 2  294 ? 3.696   3.750    18.469   1.00 71.11  ? 294 PHE   D CG     1 
ATOM   12390 C  CD1    . PHE   D 2  294 ? 3.251   2.451    18.684   1.00 66.17  ? 294 PHE   D CD1    1 
ATOM   12391 C  CD2    . PHE   D 2  294 ? 4.828   3.945    17.683   1.00 65.50  ? 294 PHE   D CD2    1 
ATOM   12392 C  CE1    . PHE   D 2  294 ? 3.920   1.366    18.140   1.00 57.66  ? 294 PHE   D CE1    1 
ATOM   12393 C  CE2    . PHE   D 2  294 ? 5.499   2.860    17.138   1.00 63.54  ? 294 PHE   D CE2    1 
ATOM   12394 C  CZ     . PHE   D 2  294 ? 5.045   1.570    17.374   1.00 58.42  ? 294 PHE   D CZ     1 
ATOM   12395 N  N      . ASP   D 2  295 ? 2.457   7.175    21.741   1.00 74.23  ? 295 ASP   D N      1 
ATOM   12396 C  CA     . ASP   D 2  295 ? 2.134   8.565    22.050   1.00 71.04  ? 295 ASP   D CA     1 
ATOM   12397 C  C      . ASP   D 2  295 ? 3.284   9.236    22.780   1.00 70.47  ? 295 ASP   D C      1 
ATOM   12398 O  O      . ASP   D 2  295 ? 3.722   8.753    23.827   1.00 73.17  ? 295 ASP   D O      1 
ATOM   12399 C  CB     . ASP   D 2  295 ? 0.878   8.621    22.924   1.00 75.66  ? 295 ASP   D CB     1 
ATOM   12400 C  CG     . ASP   D 2  295 ? 0.279   10.020   23.029   1.00 76.50  ? 295 ASP   D CG     1 
ATOM   12401 O  OD1    . ASP   D 2  295 ? 0.975   11.021   22.706   1.00 73.28  ? 295 ASP   D OD1    1 
ATOM   12402 O  OD2    . ASP   D 2  295 ? -0.904  10.099   23.433   1.00 72.63  ? 295 ASP   D OD2    1 
ATOM   12403 N  N      . SER   D 2  296 ? 3.738   10.376   22.253   1.00 66.69  ? 296 SER   D N      1 
ATOM   12404 C  CA     . SER   D 2  296 ? 4.823   11.119   22.884   1.00 60.90  ? 296 SER   D CA     1 
ATOM   12405 C  C      . SER   D 2  296 ? 4.547   11.440   24.346   1.00 64.44  ? 296 SER   D C      1 
ATOM   12406 O  O      . SER   D 2  296 ? 5.484   11.741   25.093   1.00 65.17  ? 296 SER   D O      1 
ATOM   12407 C  CB     . SER   D 2  296 ? 5.047   12.397   22.105   1.00 65.09  ? 296 SER   D CB     1 
ATOM   12408 O  OG     . SER   D 2  296 ? 4.337   12.305   20.883   1.00 73.81  ? 296 SER   D OG     1 
ATOM   12409 N  N      . LYS   D 2  297 ? 3.283   11.394   24.771   1.00 68.20  ? 297 LYS   D N      1 
ATOM   12410 C  CA     . LYS   D 2  297 ? 2.929   11.586   26.172   1.00 69.18  ? 297 LYS   D CA     1 
ATOM   12411 C  C      . LYS   D 2  297 ? 3.292   10.387   27.046   1.00 70.02  ? 297 LYS   D C      1 
ATOM   12412 O  O      . LYS   D 2  297 ? 3.320   10.525   28.279   1.00 66.88  ? 297 LYS   D O      1 
ATOM   12413 C  CB     . LYS   D 2  297 ? 1.426   11.898   26.306   1.00 65.01  ? 297 LYS   D CB     1 
ATOM   12414 C  CG     . LYS   D 2  297 ? 0.923   13.065   25.433   1.00 74.58  ? 297 LYS   D CG     1 
ATOM   12415 C  CD     . LYS   D 2  297 ? -0.565  13.345   25.666   1.00 79.50  ? 297 LYS   D CD     1 
ATOM   12416 C  CE     . LYS   D 2  297 ? -1.434  12.839   24.510   1.00 73.93  ? 297 LYS   D CE     1 
ATOM   12417 N  NZ     . LYS   D 2  297 ? -2.683  12.192   25.017   1.00 65.34  ? 297 LYS   D NZ     1 
ATOM   12418 N  N      . ASN   D 2  298 ? 3.582   9.226    26.451   1.00 64.43  ? 298 ASN   D N      1 
ATOM   12419 C  CA     . ASN   D 2  298 ? 3.927   8.028    27.204   1.00 62.62  ? 298 ASN   D CA     1 
ATOM   12420 C  C      . ASN   D 2  298 ? 5.404   7.675    27.091   1.00 64.17  ? 298 ASN   D C      1 
ATOM   12421 O  O      . ASN   D 2  298 ? 5.810   6.600    27.555   1.00 63.42  ? 298 ASN   D O      1 
ATOM   12422 C  CB     . ASN   D 2  298 ? 3.061   6.857    26.745   1.00 65.28  ? 298 ASN   D CB     1 
ATOM   12423 C  CG     . ASN   D 2  298 ? 1.610   7.052    27.097   1.00 65.05  ? 298 ASN   D CG     1 
ATOM   12424 O  OD1    . ASN   D 2  298 ? 1.045   8.094    26.801   1.00 67.74  ? 298 ASN   D OD1    1 
ATOM   12425 N  ND2    . ASN   D 2  298 ? 0.991   6.049    27.707   1.00 70.24  ? 298 ASN   D ND2    1 
ATOM   12426 N  N      . MET   D 2  299 ? 6.211   8.559    26.494   1.00 59.77  ? 299 MET   D N      1 
ATOM   12427 C  CA     . MET   D 2  299 ? 7.640   8.343    26.273   1.00 63.67  ? 299 MET   D CA     1 
ATOM   12428 C  C      . MET   D 2  299 ? 8.416   8.795    27.507   1.00 66.75  ? 299 MET   D C      1 
ATOM   12429 O  O      . MET   D 2  299 ? 8.211   9.915    27.983   1.00 68.84  ? 299 MET   D O      1 
ATOM   12430 C  CB     . MET   D 2  299 ? 8.127   9.144    25.054   1.00 64.76  ? 299 MET   D CB     1 
ATOM   12431 C  CG     . MET   D 2  299 ? 7.840   8.556    23.650   1.00 61.93  ? 299 MET   D CG     1 
ATOM   12432 S  SD     . MET   D 2  299 ? 7.770   6.751    23.518   1.00 66.55  ? 299 MET   D SD     1 
ATOM   12433 C  CE     . MET   D 2  299 ? 6.223   6.443    22.664   1.00 69.21  ? 299 MET   D CE     1 
ATOM   12434 N  N      . MET   D 2  300 ? 9.324   7.938    28.016   1.00 62.26  ? 300 MET   D N      1 
ATOM   12435 C  CA     . MET   D 2  300 ? 10.151  8.309    29.167   1.00 53.65  ? 300 MET   D CA     1 
ATOM   12436 C  C      . MET   D 2  300 ? 11.390  9.091    28.786   1.00 54.28  ? 300 MET   D C      1 
ATOM   12437 O  O      . MET   D 2  300 ? 12.339  9.135    29.574   1.00 53.29  ? 300 MET   D O      1 
ATOM   12438 C  CB     . MET   D 2  300 ? 10.575  7.080    29.959   1.00 49.96  ? 300 MET   D CB     1 
ATOM   12439 C  CG     . MET   D 2  300 ? 9.444   6.178    30.301   1.00 56.02  ? 300 MET   D CG     1 
ATOM   12440 S  SD     . MET   D 2  300 ? 8.400   6.871    31.582   1.00 59.07  ? 300 MET   D SD     1 
ATOM   12441 C  CE     . MET   D 2  300 ? 7.057   5.673    31.517   1.00 55.10  ? 300 MET   D CE     1 
ATOM   12442 N  N      . ALA   D 2  301 ? 11.417  9.692    27.603   1.00 54.57  ? 301 ALA   D N      1 
ATOM   12443 C  CA     . ALA   D 2  301 ? 12.449  10.652   27.234   1.00 60.60  ? 301 ALA   D CA     1 
ATOM   12444 C  C      . ALA   D 2  301 ? 11.753  11.837   26.597   1.00 61.36  ? 301 ALA   D C      1 
ATOM   12445 O  O      . ALA   D 2  301 ? 10.930  11.657   25.700   1.00 61.92  ? 301 ALA   D O      1 
ATOM   12446 C  CB     . ALA   D 2  301 ? 13.481  10.060   26.266   1.00 56.93  ? 301 ALA   D CB     1 
ATOM   12447 N  N      . ALA   D 2  302 ? 12.068  13.040   27.057   1.00 62.82  ? 302 ALA   D N      1 
ATOM   12448 C  CA     . ALA   D 2  302 ? 11.379  14.212   26.531   1.00 65.28  ? 302 ALA   D CA     1 
ATOM   12449 C  C      . ALA   D 2  302 ? 11.738  14.432   25.072   1.00 63.97  ? 302 ALA   D C      1 
ATOM   12450 O  O      . ALA   D 2  302 ? 12.390  15.427   24.743   1.00 64.33  ? 302 ALA   D O      1 
ATOM   12451 C  CB     . ALA   D 2  302 ? 11.707  15.474   27.340   1.00 67.00  ? 302 ALA   D CB     1 
ATOM   12452 N  N      . CYS   D 2  303 ? 11.312  13.522   24.196   1.00 62.54  ? 303 CYS   D N      1 
ATOM   12453 C  CA     . CYS   D 2  303 ? 11.511  13.665   22.760   1.00 63.49  ? 303 CYS   D CA     1 
ATOM   12454 C  C      . CYS   D 2  303 ? 10.239  13.229   22.046   1.00 63.22  ? 303 CYS   D C      1 
ATOM   12455 O  O      . CYS   D 2  303 ? 9.629   12.228   22.432   1.00 64.10  ? 303 CYS   D O      1 
ATOM   12456 C  CB     . CYS   D 2  303 ? 12.703  12.823   22.290   1.00 65.59  ? 303 CYS   D CB     1 
ATOM   12457 S  SG     . CYS   D 2  303 ? 14.090  12.782   23.468   1.00 66.72  ? 303 CYS   D SG     1 
ATOM   12458 N  N      . ASP   D 2  304 ? 9.835   13.979   21.010   1.00 62.72  ? 304 ASP   D N      1 
ATOM   12459 C  CA     . ASP   D 2  304 ? 8.608   13.661   20.263   1.00 67.99  ? 304 ASP   D CA     1 
ATOM   12460 C  C      . ASP   D 2  304 ? 8.949   12.795   19.053   1.00 61.83  ? 304 ASP   D C      1 
ATOM   12461 O  O      . ASP   D 2  304 ? 9.731   13.229   18.194   1.00 61.85  ? 304 ASP   D O      1 
ATOM   12462 C  CB     . ASP   D 2  304 ? 7.891   14.946   19.827   1.00 68.39  ? 304 ASP   D CB     1 
ATOM   12463 C  CG     . ASP   D 2  304 ? 6.671   14.699   18.911   1.00 67.92  ? 304 ASP   D CG     1 
ATOM   12464 O  OD1    . ASP   D 2  304 ? 5.972   13.661   19.044   1.00 66.28  ? 304 ASP   D OD1    1 
ATOM   12465 O  OD2    . ASP   D 2  304 ? 6.386   15.591   18.073   1.00 71.73  ? 304 ASP   D OD2    1 
ATOM   12466 N  N      . PRO   D 2  305 ? 8.411   11.576   18.946   1.00 57.21  ? 305 PRO   D N      1 
ATOM   12467 C  CA     . PRO   D 2  305 ? 8.773   10.730   17.797   1.00 60.51  ? 305 PRO   D CA     1 
ATOM   12468 C  C      . PRO   D 2  305 ? 8.448   11.379   16.465   1.00 60.00  ? 305 PRO   D C      1 
ATOM   12469 O  O      . PRO   D 2  305 ? 9.214   11.233   15.507   1.00 59.28  ? 305 PRO   D O      1 
ATOM   12470 C  CB     . PRO   D 2  305 ? 7.950   9.457    18.035   1.00 56.68  ? 305 PRO   D CB     1 
ATOM   12471 C  CG     . PRO   D 2  305 ? 7.703   9.440    19.517   1.00 56.55  ? 305 PRO   D CG     1 
ATOM   12472 C  CD     . PRO   D 2  305 ? 7.526   10.876   19.889   1.00 56.97  ? 305 PRO   D CD     1 
ATOM   12473 N  N      . ARG   D 2  306 ? 7.342   12.122   16.385   1.00 58.51  ? 306 ARG   D N      1 
ATOM   12474 C  CA     . ARG   D 2  306 ? 6.921   12.774   15.147   1.00 55.55  ? 306 ARG   D CA     1 
ATOM   12475 C  C      . ARG   D 2  306 ? 7.914   13.823   14.661   1.00 59.75  ? 306 ARG   D C      1 
ATOM   12476 O  O      . ARG   D 2  306 ? 7.722   14.399   13.585   1.00 63.45  ? 306 ARG   D O      1 
ATOM   12477 C  CB     . ARG   D 2  306 ? 5.525   13.386   15.323   1.00 60.71  ? 306 ARG   D CB     1 
ATOM   12478 C  CG     . ARG   D 2  306 ? 4.452   12.405   14.891   1.00 59.71  ? 306 ARG   D CG     1 
ATOM   12479 C  CD     . ARG   D 2  306 ? 3.202   12.336   15.752   1.00 62.18  ? 306 ARG   D CD     1 
ATOM   12480 N  NE     . ARG   D 2  306 ? 2.817   10.932   15.885   1.00 64.88  ? 306 ARG   D NE     1 
ATOM   12481 C  CZ     . ARG   D 2  306 ? 3.006   10.205   16.982   1.00 76.11  ? 306 ARG   D CZ     1 
ATOM   12482 N  NH1    . ARG   D 2  306 ? 3.368   10.764   18.134   1.00 72.12  ? 306 ARG   D NH1    1 
ATOM   12483 N  NH2    . ARG   D 2  306 ? 2.841   8.882    16.921   1.00 72.05  ? 306 ARG   D NH2    1 
ATOM   12484 N  N      . HIS   D 2  307 ? 8.981   14.076   15.421   1.00 58.73  ? 307 HIS   D N      1 
ATOM   12485 C  CA     . HIS   D 2  307 ? 10.016  14.997   14.976   1.00 56.86  ? 307 HIS   D CA     1 
ATOM   12486 C  C      . HIS   D 2  307 ? 11.214  14.278   14.366   1.00 61.03  ? 307 HIS   D C      1 
ATOM   12487 O  O      . HIS   D 2  307 ? 12.072  14.926   13.748   1.00 61.62  ? 307 HIS   D O      1 
ATOM   12488 C  CB     . HIS   D 2  307 ? 10.454  15.890   16.140   1.00 58.96  ? 307 HIS   D CB     1 
ATOM   12489 C  CG     . HIS   D 2  307 ? 9.391   16.845   16.599   1.00 66.05  ? 307 HIS   D CG     1 
ATOM   12490 N  ND1    . HIS   D 2  307 ? 9.145   17.108   17.931   1.00 64.09  ? 307 HIS   D ND1    1 
ATOM   12491 C  CD2    . HIS   D 2  307 ? 8.506   17.595   15.900   1.00 64.93  ? 307 HIS   D CD2    1 
ATOM   12492 C  CE1    . HIS   D 2  307 ? 8.155   17.978   18.030   1.00 65.00  ? 307 HIS   D CE1    1 
ATOM   12493 N  NE2    . HIS   D 2  307 ? 7.751   18.291   16.812   1.00 63.80  ? 307 HIS   D NE2    1 
ATOM   12494 N  N      . GLY   D 2  308 ? 11.273  12.957   14.494   1.00 61.62  ? 308 GLY   D N      1 
ATOM   12495 C  CA     . GLY   D 2  308 ? 12.239  12.160   13.767   1.00 60.38  ? 308 GLY   D CA     1 
ATOM   12496 C  C      . GLY   D 2  308 ? 11.648  10.894   13.169   1.00 59.61  ? 308 GLY   D C      1 
ATOM   12497 O  O      . GLY   D 2  308 ? 10.463  10.844   12.822   1.00 52.86  ? 308 GLY   D O      1 
ATOM   12498 N  N      . ARG   D 2  309 ? 12.478  9.859    13.052   1.00 62.78  ? 309 ARG   D N      1 
ATOM   12499 C  CA     . ARG   D 2  309 ? 12.123  8.622    12.376   1.00 55.21  ? 309 ARG   D CA     1 
ATOM   12500 C  C      . ARG   D 2  309 ? 12.656  7.465    13.199   1.00 50.43  ? 309 ARG   D C      1 
ATOM   12501 O  O      . ARG   D 2  309 ? 13.741  7.559    13.777   1.00 44.45  ? 309 ARG   D O      1 
ATOM   12502 C  CB     . ARG   D 2  309 ? 12.725  8.578    10.970   1.00 55.52  ? 309 ARG   D CB     1 
ATOM   12503 C  CG     . ARG   D 2  309 ? 11.929  9.268    9.878    1.00 53.07  ? 309 ARG   D CG     1 
ATOM   12504 C  CD     . ARG   D 2  309 ? 12.558  8.937    8.542    1.00 50.18  ? 309 ARG   D CD     1 
ATOM   12505 N  NE     . ARG   D 2  309 ? 12.644  10.096   7.668    1.00 60.26  ? 309 ARG   D NE     1 
ATOM   12506 C  CZ     . ARG   D 2  309 ? 11.661  10.493   6.870    1.00 67.04  ? 309 ARG   D CZ     1 
ATOM   12507 N  NH1    . ARG   D 2  309 ? 10.525  9.823    6.797    1.00 64.28  ? 309 ARG   D NH1    1 
ATOM   12508 N  NH2    . ARG   D 2  309 ? 11.826  11.587   6.121    1.00 63.41  ? 309 ARG   D NH2    1 
ATOM   12509 N  N      . TYR   D 2  310 ? 11.892  6.378    13.254   1.00 54.23  ? 310 TYR   D N      1 
ATOM   12510 C  CA     . TYR   D 2  310 ? 12.309  5.196    14.000   1.00 53.26  ? 310 TYR   D CA     1 
ATOM   12511 C  C      . TYR   D 2  310 ? 13.283  4.365    13.174   1.00 50.95  ? 310 TYR   D C      1 
ATOM   12512 O  O      . TYR   D 2  310 ? 12.921  3.859    12.109   1.00 48.37  ? 310 TYR   D O      1 
ATOM   12513 C  CB     . TYR   D 2  310 ? 11.109  4.343    14.380   1.00 45.63  ? 310 TYR   D CB     1 
ATOM   12514 C  CG     . TYR   D 2  310 ? 10.288  4.912    15.491   1.00 56.87  ? 310 TYR   D CG     1 
ATOM   12515 C  CD1    . TYR   D 2  310 ? 10.704  4.807    16.816   1.00 57.38  ? 310 TYR   D CD1    1 
ATOM   12516 C  CD2    . TYR   D 2  310 ? 9.083   5.537    15.230   1.00 56.87  ? 310 TYR   D CD2    1 
ATOM   12517 C  CE1    . TYR   D 2  310 ? 9.934   5.313    17.850   1.00 51.43  ? 310 TYR   D CE1    1 
ATOM   12518 C  CE2    . TYR   D 2  310 ? 8.326   6.051    16.248   1.00 56.97  ? 310 TYR   D CE2    1 
ATOM   12519 C  CZ     . TYR   D 2  310 ? 8.754   5.937    17.551   1.00 54.79  ? 310 TYR   D CZ     1 
ATOM   12520 O  OH     . TYR   D 2  310 ? 7.972   6.448    18.550   1.00 66.45  ? 310 TYR   D OH     1 
ATOM   12521 N  N      . LEU   D 2  311 ? 14.513  4.220    13.666   1.00 48.19  ? 311 LEU   D N      1 
ATOM   12522 C  CA     . LEU   D 2  311 ? 15.400  3.211    13.108   1.00 46.44  ? 311 LEU   D CA     1 
ATOM   12523 C  C      . LEU   D 2  311 ? 14.892  1.813    13.445   1.00 51.44  ? 311 LEU   D C      1 
ATOM   12524 O  O      . LEU   D 2  311 ? 14.797  0.947    12.561   1.00 45.34  ? 311 LEU   D O      1 
ATOM   12525 C  CB     . LEU   D 2  311 ? 16.824  3.407    13.624   1.00 42.14  ? 311 LEU   D CB     1 
ATOM   12526 C  CG     . LEU   D 2  311 ? 17.483  4.762    13.406   1.00 44.92  ? 311 LEU   D CG     1 
ATOM   12527 C  CD1    . LEU   D 2  311 ? 18.807  4.821    14.175   1.00 42.23  ? 311 LEU   D CD1    1 
ATOM   12528 C  CD2    . LEU   D 2  311 ? 17.683  5.026    11.934   1.00 45.28  ? 311 LEU   D CD2    1 
ATOM   12529 N  N      . THR   D 2  312 ? 14.552  1.578    14.722   1.00 51.67  ? 312 THR   D N      1 
ATOM   12530 C  CA     . THR   D 2  312 ? 14.106  0.261    15.174   1.00 48.21  ? 312 THR   D CA     1 
ATOM   12531 C  C      . THR   D 2  312 ? 13.233  0.398    16.416   1.00 41.65  ? 312 THR   D C      1 
ATOM   12532 O  O      . THR   D 2  312 ? 13.421  1.311    17.220   1.00 42.90  ? 312 THR   D O      1 
ATOM   12533 C  CB     . THR   D 2  312 ? 15.291  -0.665   15.480   1.00 44.84  ? 312 THR   D CB     1 
ATOM   12534 O  OG1    . THR   D 2  312 ? 16.048  -0.119   16.566   1.00 47.40  ? 312 THR   D OG1    1 
ATOM   12535 C  CG2    . THR   D 2  312 ? 16.183  -0.836   14.239   1.00 40.28  ? 312 THR   D CG2    1 
ATOM   12536 N  N      . VAL   D 2  313 ? 12.292  -0.530   16.580   1.00 33.57  ? 313 VAL   D N      1 
ATOM   12537 C  CA     . VAL   D 2  313 ? 11.331  -0.473   17.675   1.00 44.79  ? 313 VAL   D CA     1 
ATOM   12538 C  C      . VAL   D 2  313 ? 11.078  -1.873   18.227   1.00 46.50  ? 313 VAL   D C      1 
ATOM   12539 O  O      . VAL   D 2  313 ? 10.957  -2.844   17.474   1.00 42.79  ? 313 VAL   D O      1 
ATOM   12540 C  CB     . VAL   D 2  313 ? 10.000  0.171    17.229   1.00 43.60  ? 313 VAL   D CB     1 
ATOM   12541 C  CG1    . VAL   D 2  313 ? 8.925   -0.075   18.274   1.00 46.22  ? 313 VAL   D CG1    1 
ATOM   12542 C  CG2    . VAL   D 2  313 ? 10.182  1.651    17.021   1.00 45.42  ? 313 VAL   D CG2    1 
ATOM   12543 N  N      . ALA   D 2  314 ? 10.970  -1.969   19.545   1.00 42.95  ? 314 ALA   D N      1 
ATOM   12544 C  CA     . ALA   D 2  314 ? 10.551  -3.194   20.206   1.00 48.71  ? 314 ALA   D CA     1 
ATOM   12545 C  C      . ALA   D 2  314 ? 9.351   -2.873   21.090   1.00 55.48  ? 314 ALA   D C      1 
ATOM   12546 O  O      . ALA   D 2  314 ? 9.298   -1.802   21.697   1.00 52.64  ? 314 ALA   D O      1 
ATOM   12547 C  CB     . ALA   D 2  314 ? 11.687  -3.785   21.034   1.00 49.60  ? 314 ALA   D CB     1 
ATOM   12548 N  N      . ALA   D 2  315 ? 8.386   -3.792   21.164   1.00 58.44  ? 315 ALA   D N      1 
ATOM   12549 C  CA     . ALA   D 2  315 ? 7.141   -3.550   21.899   1.00 56.28  ? 315 ALA   D CA     1 
ATOM   12550 C  C      . ALA   D 2  315 ? 6.812   -4.769   22.750   1.00 55.57  ? 315 ALA   D C      1 
ATOM   12551 O  O      . ALA   D 2  315 ? 6.667   -5.867   22.201   1.00 59.88  ? 315 ALA   D O      1 
ATOM   12552 C  CB     . ALA   D 2  315 ? 5.991   -3.260   20.920   1.00 50.71  ? 315 ALA   D CB     1 
ATOM   12553 N  N      . ILE   D 2  316 ? 6.680   -4.601   24.070   1.00 48.42  ? 316 ILE   D N      1 
ATOM   12554 C  CA     . ILE   D 2  316 ? 6.257   -5.708   24.936   1.00 55.49  ? 316 ILE   D CA     1 
ATOM   12555 C  C      . ILE   D 2  316 ? 4.810   -5.490   25.339   1.00 61.15  ? 316 ILE   D C      1 
ATOM   12556 O  O      . ILE   D 2  316 ? 4.478   -4.474   25.966   1.00 62.85  ? 316 ILE   D O      1 
ATOM   12557 C  CB     . ILE   D 2  316 ? 7.121   -5.876   26.198   1.00 57.47  ? 316 ILE   D CB     1 
ATOM   12558 C  CG1    . ILE   D 2  316 ? 8.607   -5.873   25.885   1.00 50.77  ? 316 ILE   D CG1    1 
ATOM   12559 C  CG2    . ILE   D 2  316 ? 6.739   -7.160   26.936   1.00 52.59  ? 316 ILE   D CG2    1 
ATOM   12560 C  CD1    . ILE   D 2  316 ? 9.240   -4.518   26.039   1.00 55.80  ? 316 ILE   D CD1    1 
ATOM   12561 N  N      . PHE   D 2  317 ? 3.957   -6.457   25.004   1.00 57.46  ? 317 PHE   D N      1 
ATOM   12562 C  CA     . PHE   D 2  317 ? 2.580   -6.491   25.468   1.00 62.46  ? 317 PHE   D CA     1 
ATOM   12563 C  C      . PHE   D 2  317 ? 2.482   -7.493   26.610   1.00 63.85  ? 317 PHE   D C      1 
ATOM   12564 O  O      . PHE   D 2  317 ? 2.900   -8.648   26.465   1.00 61.38  ? 317 PHE   D O      1 
ATOM   12565 C  CB     . PHE   D 2  317 ? 1.631   -6.852   24.324   1.00 62.86  ? 317 PHE   D CB     1 
ATOM   12566 C  CG     . PHE   D 2  317 ? 1.453   -5.743   23.341   1.00 62.77  ? 317 PHE   D CG     1 
ATOM   12567 C  CD1    . PHE   D 2  317 ? 2.336   -5.590   22.283   1.00 60.36  ? 317 PHE   D CD1    1 
ATOM   12568 C  CD2    . PHE   D 2  317 ? 0.428   -4.821   23.498   1.00 62.72  ? 317 PHE   D CD2    1 
ATOM   12569 C  CE1    . PHE   D 2  317 ? 2.190   -4.564   21.386   1.00 59.40  ? 317 PHE   D CE1    1 
ATOM   12570 C  CE2    . PHE   D 2  317 ? 0.273   -3.785   22.608   1.00 61.37  ? 317 PHE   D CE2    1 
ATOM   12571 C  CZ     . PHE   D 2  317 ? 1.161   -3.652   21.549   1.00 66.99  ? 317 PHE   D CZ     1 
ATOM   12572 N  N      . ARG   D 2  318 ? 1.963   -7.040   27.750   1.00 66.50  ? 318 ARG   D N      1 
ATOM   12573 C  CA     . ARG   D 2  318 ? 1.847   -7.856   28.952   1.00 66.11  ? 318 ARG   D CA     1 
ATOM   12574 C  C      . ARG   D 2  318 ? 0.394   -7.906   29.387   1.00 69.44  ? 318 ARG   D C      1 
ATOM   12575 O  O      . ARG   D 2  318 ? -0.262  -6.867   29.533   1.00 70.02  ? 318 ARG   D O      1 
ATOM   12576 C  CB     . ARG   D 2  318 ? 2.704   -7.311   30.088   1.00 67.72  ? 318 ARG   D CB     1 
ATOM   12577 C  CG     . ARG   D 2  318 ? 4.164   -7.171   29.745   1.00 66.90  ? 318 ARG   D CG     1 
ATOM   12578 C  CD     . ARG   D 2  318 ? 4.913   -6.793   30.978   1.00 72.12  ? 318 ARG   D CD     1 
ATOM   12579 N  NE     . ARG   D 2  318 ? 4.886   -7.909   31.912   1.00 72.74  ? 318 ARG   D NE     1 
ATOM   12580 C  CZ     . ARG   D 2  318 ? 5.652   -8.002   32.987   1.00 73.17  ? 318 ARG   D CZ     1 
ATOM   12581 N  NH1    . ARG   D 2  318 ? 6.541   -7.062   33.282   1.00 69.26  ? 318 ARG   D NH1    1 
ATOM   12582 N  NH2    . ARG   D 2  318 ? 5.512   -9.056   33.791   1.00 69.47  ? 318 ARG   D NH2    1 
ATOM   12583 N  N      . GLY   D 2  319 ? -0.092  -9.112   29.604   1.00 66.26  ? 319 GLY   D N      1 
ATOM   12584 C  CA     . GLY   D 2  319 ? -1.467  -9.301   29.958   1.00 66.01  ? 319 GLY   D CA     1 
ATOM   12585 C  C      . GLY   D 2  319 ? -2.037  -10.453  29.174   1.00 72.75  ? 319 GLY   D C      1 
ATOM   12586 O  O      . GLY   D 2  319 ? -1.325  -11.140  28.436   1.00 75.49  ? 319 GLY   D O      1 
ATOM   12587 N  N      . ARG   D 2  320 ? -3.328  -10.675  29.347   1.00 78.99  ? 320 ARG   D N      1 
ATOM   12588 C  CA     . ARG   D 2  320 ? -4.071  -11.693  28.621   1.00 81.80  ? 320 ARG   D CA     1 
ATOM   12589 C  C      . ARG   D 2  320 ? -4.893  -10.961  27.570   1.00 78.31  ? 320 ARG   D C      1 
ATOM   12590 O  O      . ARG   D 2  320 ? -5.778  -10.172  27.909   1.00 82.88  ? 320 ARG   D O      1 
ATOM   12591 C  CB     . ARG   D 2  320 ? -4.953  -12.485  29.581   1.00 83.17  ? 320 ARG   D CB     1 
ATOM   12592 C  CG     . ARG   D 2  320 ? -4.255  -13.655  30.244   1.00 83.15  ? 320 ARG   D CG     1 
ATOM   12593 C  CD     . ARG   D 2  320 ? -4.367  -14.868  29.365   1.00 94.17  ? 320 ARG   D CD     1 
ATOM   12594 N  NE     . ARG   D 2  320 ? -5.700  -15.455  29.462   1.00 102.11 ? 320 ARG   D NE     1 
ATOM   12595 C  CZ     . ARG   D 2  320 ? -6.064  -16.589  28.876   1.00 104.03 ? 320 ARG   D CZ     1 
ATOM   12596 N  NH1    . ARG   D 2  320 ? -5.220  -17.281  28.127   1.00 104.07 ? 320 ARG   D NH1    1 
ATOM   12597 N  NH2    . ARG   D 2  320 ? -7.308  -17.037  29.042   1.00 89.41  ? 320 ARG   D NH2    1 
ATOM   12598 N  N      . MET   D 2  321 ? -4.574  -11.184  26.302   1.00 77.77  ? 321 MET   D N      1 
ATOM   12599 C  CA     . MET   D 2  321 ? -5.177  -10.408  25.225   1.00 78.87  ? 321 MET   D CA     1 
ATOM   12600 C  C      . MET   D 2  321 ? -4.994  -11.172  23.923   1.00 84.88  ? 321 MET   D C      1 
ATOM   12601 O  O      . MET   D 2  321 ? -4.085  -11.996  23.800   1.00 89.02  ? 321 MET   D O      1 
ATOM   12602 C  CB     . MET   D 2  321 ? -4.570  -8.997   25.129   1.00 73.63  ? 321 MET   D CB     1 
ATOM   12603 C  CG     . MET   D 2  321 ? -3.255  -8.921   24.358   1.00 76.66  ? 321 MET   D CG     1 
ATOM   12604 S  SD     . MET   D 2  321 ? -2.076  -7.720   25.022   1.00 84.59  ? 321 MET   D SD     1 
ATOM   12605 C  CE     . MET   D 2  321 ? -1.995  -8.170   26.761   1.00 78.05  ? 321 MET   D CE     1 
ATOM   12606 N  N      . SER   D 2  322 ? -5.880  -10.919  22.963   1.00 86.49  ? 322 SER   D N      1 
ATOM   12607 C  CA     . SER   D 2  322 ? -5.792  -11.597  21.673   1.00 81.53  ? 322 SER   D CA     1 
ATOM   12608 C  C      . SER   D 2  322 ? -4.550  -11.097  20.942   1.00 80.43  ? 322 SER   D C      1 
ATOM   12609 O  O      . SER   D 2  322 ? -4.458  -9.917   20.587   1.00 79.19  ? 322 SER   D O      1 
ATOM   12610 C  CB     . SER   D 2  322 ? -7.055  -11.345  20.853   1.00 80.00  ? 322 SER   D CB     1 
ATOM   12611 O  OG     . SER   D 2  322 ? -7.017  -12.046  19.623   1.00 71.30  ? 322 SER   D OG     1 
ATOM   12612 N  N      . MET   D 2  323 ? -3.573  -11.979  20.731   1.00 74.93  ? 323 MET   D N      1 
ATOM   12613 C  CA     . MET   D 2  323 ? -2.397  -11.544  19.994   1.00 80.42  ? 323 MET   D CA     1 
ATOM   12614 C  C      . MET   D 2  323 ? -2.691  -11.392  18.497   1.00 79.99  ? 323 MET   D C      1 
ATOM   12615 O  O      . MET   D 2  323 ? -1.989  -10.639  17.807   1.00 74.30  ? 323 MET   D O      1 
ATOM   12616 C  CB     . MET   D 2  323 ? -1.226  -12.500  20.269   1.00 85.04  ? 323 MET   D CB     1 
ATOM   12617 C  CG     . MET   D 2  323 ? -0.671  -12.465  21.738   1.00 89.19  ? 323 MET   D CG     1 
ATOM   12618 S  SD     . MET   D 2  323 ? -1.228  -13.801  22.878   1.00 111.64 ? 323 MET   D SD     1 
ATOM   12619 C  CE     . MET   D 2  323 ? -1.019  -13.075  24.515   1.00 80.35  ? 323 MET   D CE     1 
ATOM   12620 N  N      . LYS   D 2  324 ? -3.736  -12.053  17.985   1.00 79.27  ? 324 LYS   D N      1 
ATOM   12621 C  CA     . LYS   D 2  324 ? -4.260  -11.689  16.670   1.00 75.48  ? 324 LYS   D CA     1 
ATOM   12622 C  C      . LYS   D 2  324 ? -4.648  -10.217  16.633   1.00 75.13  ? 324 LYS   D C      1 
ATOM   12623 O  O      . LYS   D 2  324 ? -4.309  -9.495   15.687   1.00 72.10  ? 324 LYS   D O      1 
ATOM   12624 C  CB     . LYS   D 2  324 ? -5.465  -12.555  16.303   1.00 72.22  ? 324 LYS   D CB     1 
ATOM   12625 C  CG     . LYS   D 2  324 ? -6.073  -12.190  14.951   1.00 69.37  ? 324 LYS   D CG     1 
ATOM   12626 C  CD     . LYS   D 2  324 ? -7.333  -12.983  14.663   1.00 76.68  ? 324 LYS   D CD     1 
ATOM   12627 C  CE     . LYS   D 2  324 ? -8.276  -12.204  13.754   1.00 83.56  ? 324 LYS   D CE     1 
ATOM   12628 N  NZ     . LYS   D 2  324 ? -9.718  -12.398  14.092   1.00 79.36  ? 324 LYS   D NZ     1 
ATOM   12629 N  N      . GLU   D 2  325 ? -5.381  -9.755   17.649   1.00 74.19  ? 325 GLU   D N      1 
ATOM   12630 C  CA     . GLU   D 2  325 ? -5.669  -8.327   17.746   1.00 74.25  ? 325 GLU   D CA     1 
ATOM   12631 C  C      . GLU   D 2  325 ? -4.372  -7.524   17.747   1.00 69.81  ? 325 GLU   D C      1 
ATOM   12632 O  O      . GLU   D 2  325 ? -4.203  -6.587   16.953   1.00 62.96  ? 325 GLU   D O      1 
ATOM   12633 C  CB     . GLU   D 2  325 ? -6.507  -8.044   19.001   1.00 75.00  ? 325 GLU   D CB     1 
ATOM   12634 C  CG     . GLU   D 2  325 ? -7.278  -6.724   18.967   1.00 75.96  ? 325 GLU   D CG     1 
ATOM   12635 C  CD     . GLU   D 2  325 ? -8.346  -6.618   20.050   1.00 79.53  ? 325 GLU   D CD     1 
ATOM   12636 O  OE1    . GLU   D 2  325 ? -8.855  -7.663   20.507   1.00 77.24  ? 325 GLU   D OE1    1 
ATOM   12637 O  OE2    . GLU   D 2  325 ? -8.674  -5.480   20.447   1.00 79.97  ? 325 GLU   D OE2    1 
ATOM   12638 N  N      . VAL   D 2  326 ? -3.421  -7.916   18.606   1.00 68.55  ? 326 VAL   D N      1 
ATOM   12639 C  CA     . VAL   D 2  326 ? -2.150  -7.198   18.707   1.00 71.67  ? 326 VAL   D CA     1 
ATOM   12640 C  C      . VAL   D 2  326 ? -1.467  -7.123   17.346   1.00 63.43  ? 326 VAL   D C      1 
ATOM   12641 O  O      . VAL   D 2  326 ? -0.929  -6.075   16.964   1.00 54.22  ? 326 VAL   D O      1 
ATOM   12642 C  CB     . VAL   D 2  326 ? -1.239  -7.857   19.765   1.00 70.50  ? 326 VAL   D CB     1 
ATOM   12643 C  CG1    . VAL   D 2  326 ? 0.201   -7.451   19.560   1.00 60.06  ? 326 VAL   D CG1    1 
ATOM   12644 C  CG2    . VAL   D 2  326 ? -1.678  -7.480   21.165   1.00 70.01  ? 326 VAL   D CG2    1 
ATOM   12645 N  N      . ASP   D 2  327 ? -1.475  -8.234   16.595   1.00 69.48  ? 327 ASP   D N      1 
ATOM   12646 C  CA     . ASP   D 2  327 ? -0.821  -8.262   15.285   1.00 62.76  ? 327 ASP   D CA     1 
ATOM   12647 C  C      . ASP   D 2  327 ? -1.448  -7.251   14.333   1.00 64.16  ? 327 ASP   D C      1 
ATOM   12648 O  O      . ASP   D 2  327 ? -0.737  -6.525   13.629   1.00 58.23  ? 327 ASP   D O      1 
ATOM   12649 C  CB     . ASP   D 2  327 ? -0.893  -9.659   14.680   1.00 59.86  ? 327 ASP   D CB     1 
ATOM   12650 C  CG     . ASP   D 2  327 ? -0.010  -10.643  15.383   1.00 63.92  ? 327 ASP   D CG     1 
ATOM   12651 O  OD1    . ASP   D 2  327 ? 0.743   -10.209  16.272   1.00 67.86  ? 327 ASP   D OD1    1 
ATOM   12652 O  OD2    . ASP   D 2  327 ? -0.051  -11.844  15.030   1.00 67.41  ? 327 ASP   D OD2    1 
ATOM   12653 N  N      . GLU   D 2  328 ? -2.787  -7.202   14.285   1.00 65.47  ? 328 GLU   D N      1 
ATOM   12654 C  CA     . GLU   D 2  328 ? -3.445  -6.207   13.449   1.00 59.64  ? 328 GLU   D CA     1 
ATOM   12655 C  C      . GLU   D 2  328 ? -3.253  -4.808   14.009   1.00 59.45  ? 328 GLU   D C      1 
ATOM   12656 O  O      . GLU   D 2  328 ? -3.120  -3.842   13.250   1.00 59.79  ? 328 GLU   D O      1 
ATOM   12657 C  CB     . GLU   D 2  328 ? -4.936  -6.505   13.306   1.00 64.16  ? 328 GLU   D CB     1 
ATOM   12658 C  CG     . GLU   D 2  328 ? -5.348  -7.964   13.282   1.00 75.90  ? 328 GLU   D CG     1 
ATOM   12659 C  CD     . GLU   D 2  328 ? -6.796  -8.155   13.751   1.00 84.12  ? 328 GLU   D CD     1 
ATOM   12660 O  OE1    . GLU   D 2  328 ? -7.426  -9.155   13.331   1.00 84.74  ? 328 GLU   D OE1    1 
ATOM   12661 O  OE2    . GLU   D 2  328 ? -7.295  -7.312   14.550   1.00 81.17  ? 328 GLU   D OE2    1 
ATOM   12662 N  N      . GLN   D 2  329 ? -3.243  -4.666   15.331   1.00 58.75  ? 329 GLN   D N      1 
ATOM   12663 C  CA     . GLN   D 2  329 ? -3.044  -3.334   15.881   1.00 58.31  ? 329 GLN   D CA     1 
ATOM   12664 C  C      . GLN   D 2  329 ? -1.653  -2.797   15.554   1.00 59.75  ? 329 GLN   D C      1 
ATOM   12665 O  O      . GLN   D 2  329 ? -1.512  -1.621   15.192   1.00 57.59  ? 329 GLN   D O      1 
ATOM   12666 C  CB     . GLN   D 2  329 ? -3.299  -3.343   17.380   1.00 57.36  ? 329 GLN   D CB     1 
ATOM   12667 C  CG     . GLN   D 2  329 ? -4.713  -2.973   17.691   1.00 65.14  ? 329 GLN   D CG     1 
ATOM   12668 C  CD     . GLN   D 2  329 ? -5.299  -2.070   16.629   1.00 69.99  ? 329 GLN   D CD     1 
ATOM   12669 O  OE1    . GLN   D 2  329 ? -4.741  -1.012   16.315   1.00 73.20  ? 329 GLN   D OE1    1 
ATOM   12670 N  NE2    . GLN   D 2  329 ? -6.405  -2.505   16.031   1.00 61.91  ? 329 GLN   D NE2    1 
ATOM   12671 N  N      . MET   D 2  330 ? -0.614  -3.638   15.675   1.00 59.77  ? 330 MET   D N      1 
ATOM   12672 C  CA     . MET   D 2  330 ? 0.747   -3.168   15.425   1.00 56.25  ? 330 MET   D CA     1 
ATOM   12673 C  C      . MET   D 2  330 ? 0.970   -2.917   13.940   1.00 56.76  ? 330 MET   D C      1 
ATOM   12674 O  O      . MET   D 2  330 ? 1.685   -1.982   13.562   1.00 57.72  ? 330 MET   D O      1 
ATOM   12675 C  CB     . MET   D 2  330 ? 1.773   -4.172   15.964   1.00 54.69  ? 330 MET   D CB     1 
ATOM   12676 C  CG     . MET   D 2  330 ? 1.990   -4.152   17.491   1.00 53.25  ? 330 MET   D CG     1 
ATOM   12677 S  SD     . MET   D 2  330 ? 2.698   -2.621   18.158   1.00 56.25  ? 330 MET   D SD     1 
ATOM   12678 C  CE     . MET   D 2  330 ? 3.444   -1.884   16.729   1.00 53.57  ? 330 MET   D CE     1 
ATOM   12679 N  N      . LEU   D 2  331 ? 0.370   -3.748   13.085   1.00 56.28  ? 331 LEU   D N      1 
ATOM   12680 C  CA     . LEU   D 2  331 ? 0.392   -3.494   11.648   1.00 53.33  ? 331 LEU   D CA     1 
ATOM   12681 C  C      . LEU   D 2  331 ? -0.291  -2.171   11.329   1.00 54.14  ? 331 LEU   D C      1 
ATOM   12682 O  O      . LEU   D 2  331 ? 0.152   -1.408   10.460   1.00 44.91  ? 331 LEU   D O      1 
ATOM   12683 C  CB     . LEU   D 2  331 ? -0.307  -4.649   10.936   1.00 55.01  ? 331 LEU   D CB     1 
ATOM   12684 C  CG     . LEU   D 2  331 ? 0.565   -5.859   10.593   1.00 58.18  ? 331 LEU   D CG     1 
ATOM   12685 C  CD1    . LEU   D 2  331 ? -0.319  -7.027   10.155   1.00 50.69  ? 331 LEU   D CD1    1 
ATOM   12686 C  CD2    . LEU   D 2  331 ? 1.608   -5.511   9.532    1.00 53.01  ? 331 LEU   D CD2    1 
ATOM   12687 N  N      . ASN   D 2  332 ? -1.368  -1.875   12.054   1.00 59.67  ? 332 ASN   D N      1 
ATOM   12688 C  CA     . ASN   D 2  332 ? -2.132  -0.663   11.811   1.00 55.85  ? 332 ASN   D CA     1 
ATOM   12689 C  C      . ASN   D 2  332 ? -1.293  0.584    12.058   1.00 57.91  ? 332 ASN   D C      1 
ATOM   12690 O  O      . ASN   D 2  332 ? -1.295  1.508    11.235   1.00 58.75  ? 332 ASN   D O      1 
ATOM   12691 C  CB     . ASN   D 2  332 ? -3.370  -0.670   12.697   1.00 67.42  ? 332 ASN   D CB     1 
ATOM   12692 C  CG     . ASN   D 2  332 ? -4.514  0.113    12.105   1.00 75.05  ? 332 ASN   D CG     1 
ATOM   12693 O  OD1    . ASN   D 2  332 ? -4.550  1.347    12.195   1.00 75.49  ? 332 ASN   D OD1    1 
ATOM   12694 N  ND2    . ASN   D 2  332 ? -5.472  -0.599   11.508   1.00 79.25  ? 332 ASN   D ND2    1 
ATOM   12695 N  N      . VAL   D 2  333 ? -0.562  0.630    13.179   1.00 53.47  ? 333 VAL   D N      1 
ATOM   12696 C  CA     . VAL   D 2  333 ? 0.201   1.834    13.508   1.00 52.59  ? 333 VAL   D CA     1 
ATOM   12697 C  C      . VAL   D 2  333 ? 1.362   2.040    12.535   1.00 49.87  ? 333 VAL   D C      1 
ATOM   12698 O  O      . VAL   D 2  333 ? 1.687   3.183    12.192   1.00 50.48  ? 333 VAL   D O      1 
ATOM   12699 C  CB     . VAL   D 2  333 ? 0.669   1.811    14.981   1.00 53.89  ? 333 VAL   D CB     1 
ATOM   12700 C  CG1    . VAL   D 2  333 ? 1.292   0.483    15.341   1.00 60.68  ? 333 VAL   D CG1    1 
ATOM   12701 C  CG2    . VAL   D 2  333 ? 1.650   2.938    15.274   1.00 52.18  ? 333 VAL   D CG2    1 
ATOM   12702 N  N      . GLN   D 2  334 ? 1.988   0.970    12.034   1.00 47.61  ? 334 GLN   D N      1 
ATOM   12703 C  CA     . GLN   D 2  334 ? 3.034   1.196    11.030   1.00 51.67  ? 334 GLN   D CA     1 
ATOM   12704 C  C      . GLN   D 2  334 ? 2.448   1.693    9.709    1.00 50.21  ? 334 GLN   D C      1 
ATOM   12705 O  O      . GLN   D 2  334 ? 3.026   2.574    9.067    1.00 53.84  ? 334 GLN   D O      1 
ATOM   12706 C  CB     . GLN   D 2  334 ? 3.873   -0.063   10.797   1.00 43.32  ? 334 GLN   D CB     1 
ATOM   12707 C  CG     . GLN   D 2  334 ? 4.380   -0.705   12.056   1.00 48.09  ? 334 GLN   D CG     1 
ATOM   12708 C  CD     . GLN   D 2  334 ? 4.967   -2.057   11.821   1.00 42.44  ? 334 GLN   D CD     1 
ATOM   12709 O  OE1    . GLN   D 2  334 ? 6.010   -2.201   11.176   1.00 46.76  ? 334 GLN   D OE1    1 
ATOM   12710 N  NE2    . GLN   D 2  334 ? 4.282   -3.074   12.311   1.00 40.46  ? 334 GLN   D NE2    1 
ATOM   12711 N  N      . ASN   D 2  335 ? 1.302   1.154    9.284    1.00 55.43  ? 335 ASN   D N      1 
ATOM   12712 C  CA     . ASN   D 2  335 ? 0.653   1.643    8.066    1.00 56.33  ? 335 ASN   D CA     1 
ATOM   12713 C  C      . ASN   D 2  335 ? 0.313   3.124    8.179    1.00 49.24  ? 335 ASN   D C      1 
ATOM   12714 O  O      . ASN   D 2  335 ? 0.799   3.946    7.397    1.00 47.27  ? 335 ASN   D O      1 
ATOM   12715 C  CB     . ASN   D 2  335 ? -0.604  0.821    7.776    1.00 52.62  ? 335 ASN   D CB     1 
ATOM   12716 C  CG     . ASN   D 2  335 ? -0.278  -0.611   7.373    1.00 60.21  ? 335 ASN   D CG     1 
ATOM   12717 O  OD1    . ASN   D 2  335 ? 0.829   -0.901   6.889    1.00 64.88  ? 335 ASN   D OD1    1 
ATOM   12718 N  ND2    . ASN   D 2  335 ? -1.237  -1.525   7.583    1.00 61.49  ? 335 ASN   D ND2    1 
ATOM   12719 N  N      . LYS   D 2  336 ? -0.513  3.482    9.163    1.00 48.61  ? 336 LYS   D N      1 
ATOM   12720 C  CA     . LYS   D 2  336 ? -0.961  4.861    9.348    1.00 53.86  ? 336 LYS   D CA     1 
ATOM   12721 C  C      . LYS   D 2  336 ? 0.157   5.820    9.737    1.00 51.33  ? 336 LYS   D C      1 
ATOM   12722 O  O      . LYS   D 2  336 ? -0.041  7.032    9.644    1.00 51.58  ? 336 LYS   D O      1 
ATOM   12723 C  CB     . LYS   D 2  336 ? -2.047  4.928    10.418   1.00 53.50  ? 336 LYS   D CB     1 
ATOM   12724 C  CG     . LYS   D 2  336 ? -3.282  4.104    10.106   1.00 63.22  ? 336 LYS   D CG     1 
ATOM   12725 C  CD     . LYS   D 2  336 ? -4.135  3.941    11.361   1.00 70.40  ? 336 LYS   D CD     1 
ATOM   12726 C  CE     . LYS   D 2  336 ? -5.607  3.858    11.002   1.00 74.36  ? 336 LYS   D CE     1 
ATOM   12727 N  NZ     . LYS   D 2  336 ? -6.316  2.662    11.523   1.00 73.91  ? 336 LYS   D NZ     1 
ATOM   12728 N  N      . ASN   D 2  337 ? 1.313   5.319    10.175   1.00 52.03  ? 337 ASN   D N      1 
ATOM   12729 C  CA     . ASN   D 2  337 ? 2.418   6.153    10.634   1.00 49.50  ? 337 ASN   D CA     1 
ATOM   12730 C  C      . ASN   D 2  337 ? 3.685   5.916    9.818    1.00 52.49  ? 337 ASN   D C      1 
ATOM   12731 O  O      . ASN   D 2  337 ? 4.796   6.194    10.288   1.00 52.57  ? 337 ASN   D O      1 
ATOM   12732 C  CB     . ASN   D 2  337 ? 2.682   5.901    12.118   1.00 52.48  ? 337 ASN   D CB     1 
ATOM   12733 C  CG     . ASN   D 2  337 ? 1.625   6.525    13.006   1.00 56.39  ? 337 ASN   D CG     1 
ATOM   12734 O  OD1    . ASN   D 2  337 ? 0.786   5.832    13.583   1.00 54.07  ? 337 ASN   D OD1    1 
ATOM   12735 N  ND2    . ASN   D 2  337 ? 1.650   7.851    13.104   1.00 60.65  ? 337 ASN   D ND2    1 
ATOM   12736 N  N      . SER   D 2  338 ? 3.531   5.447    8.583    1.00 51.81  ? 338 SER   D N      1 
ATOM   12737 C  CA     . SER   D 2  338 ? 4.641   4.827    7.872    1.00 48.53  ? 338 SER   D CA     1 
ATOM   12738 C  C      . SER   D 2  338 ? 5.809   5.778    7.675    1.00 49.88  ? 338 SER   D C      1 
ATOM   12739 O  O      . SER   D 2  338 ? 6.958   5.328    7.627    1.00 48.86  ? 338 SER   D O      1 
ATOM   12740 C  CB     . SER   D 2  338 ? 4.164   4.304    6.526    1.00 46.03  ? 338 SER   D CB     1 
ATOM   12741 O  OG     . SER   D 2  338 ? 3.996   5.372    5.614    1.00 52.72  ? 338 SER   D OG     1 
ATOM   12742 N  N      . SER   D 2  339 ? 5.546   7.083    7.537    1.00 50.43  ? 339 SER   D N      1 
ATOM   12743 C  CA     . SER   D 2  339 ? 6.630   8.023    7.277    1.00 46.32  ? 339 SER   D CA     1 
ATOM   12744 C  C      . SER   D 2  339 ? 7.529   8.227    8.482    1.00 50.22  ? 339 SER   D C      1 
ATOM   12745 O  O      . SER   D 2  339 ? 8.526   8.943    8.363    1.00 55.07  ? 339 SER   D O      1 
ATOM   12746 C  CB     . SER   D 2  339 ? 6.096   9.388    6.805    1.00 56.14  ? 339 SER   D CB     1 
ATOM   12747 O  OG     . SER   D 2  339 ? 4.677   9.460    6.730    1.00 56.64  ? 339 SER   D OG     1 
ATOM   12748 N  N      . TYR   D 2  340 ? 7.218   7.617    9.625    1.00 54.85  ? 340 TYR   D N      1 
ATOM   12749 C  CA     . TYR   D 2  340 ? 7.996   7.781    10.849   1.00 51.52  ? 340 TYR   D CA     1 
ATOM   12750 C  C      . TYR   D 2  340 ? 8.838   6.558    11.173   1.00 52.56  ? 340 TYR   D C      1 
ATOM   12751 O  O      . TYR   D 2  340 ? 9.331   6.448    12.302   1.00 54.40  ? 340 TYR   D O      1 
ATOM   12752 C  CB     . TYR   D 2  340 ? 7.074   8.115    12.038   1.00 51.38  ? 340 TYR   D CB     1 
ATOM   12753 C  CG     . TYR   D 2  340 ? 6.339   9.442    11.912   1.00 49.93  ? 340 TYR   D CG     1 
ATOM   12754 C  CD1    . TYR   D 2  340 ? 7.035   10.636   11.915   1.00 49.41  ? 340 TYR   D CD1    1 
ATOM   12755 C  CD2    . TYR   D 2  340 ? 4.954   9.491    11.757   1.00 45.59  ? 340 TYR   D CD2    1 
ATOM   12756 C  CE1    . TYR   D 2  340 ? 6.392   11.841   11.780   1.00 48.65  ? 340 TYR   D CE1    1 
ATOM   12757 C  CE2    . TYR   D 2  340 ? 4.302   10.694   11.628   1.00 47.13  ? 340 TYR   D CE2    1 
ATOM   12758 C  CZ     . TYR   D 2  340 ? 5.035   11.876   11.638   1.00 53.01  ? 340 TYR   D CZ     1 
ATOM   12759 O  OH     . TYR   D 2  340 ? 4.419   13.113   11.515   1.00 56.71  ? 340 TYR   D OH     1 
ATOM   12760 N  N      . PHE   D 2  341 ? 9.011   5.635    10.217   1.00 52.73  ? 341 PHE   D N      1 
ATOM   12761 C  CA     . PHE   D 2  341 ? 9.919   4.494    10.351   1.00 49.24  ? 341 PHE   D CA     1 
ATOM   12762 C  C      . PHE   D 2  341 ? 10.849  4.490    9.153    1.00 46.00  ? 341 PHE   D C      1 
ATOM   12763 O  O      . PHE   D 2  341 ? 10.379  4.513    8.015    1.00 52.24  ? 341 PHE   D O      1 
ATOM   12764 C  CB     . PHE   D 2  341 ? 9.165   3.163    10.416   1.00 41.93  ? 341 PHE   D CB     1 
ATOM   12765 C  CG     . PHE   D 2  341 ? 8.132   3.091    11.502   1.00 44.03  ? 341 PHE   D CG     1 
ATOM   12766 C  CD1    . PHE   D 2  341 ? 6.871   3.652    11.317   1.00 45.19  ? 341 PHE   D CD1    1 
ATOM   12767 C  CD2    . PHE   D 2  341 ? 8.404   2.424    12.700   1.00 46.65  ? 341 PHE   D CD2    1 
ATOM   12768 C  CE1    . PHE   D 2  341 ? 5.898   3.566    12.305   1.00 44.26  ? 341 PHE   D CE1    1 
ATOM   12769 C  CE2    . PHE   D 2  341 ? 7.440   2.338    13.698   1.00 47.81  ? 341 PHE   D CE2    1 
ATOM   12770 C  CZ     . PHE   D 2  341 ? 6.184   2.917    13.496   1.00 48.46  ? 341 PHE   D CZ     1 
ATOM   12771 N  N      . VAL   D 2  342 ? 12.160  4.475    9.388    1.00 42.70  ? 342 VAL   D N      1 
ATOM   12772 C  CA     . VAL   D 2  342 ? 13.061  4.511    8.247    1.00 43.15  ? 342 VAL   D CA     1 
ATOM   12773 C  C      . VAL   D 2  342 ? 12.730  3.356    7.310    1.00 49.76  ? 342 VAL   D C      1 
ATOM   12774 O  O      . VAL   D 2  342 ? 12.545  2.210    7.739    1.00 46.65  ? 342 VAL   D O      1 
ATOM   12775 C  CB     . VAL   D 2  342 ? 14.524  4.475    8.692    1.00 43.59  ? 342 VAL   D CB     1 
ATOM   12776 C  CG1    . VAL   D 2  342 ? 14.938  5.839    9.208    1.00 45.06  ? 342 VAL   D CG1    1 
ATOM   12777 C  CG2    . VAL   D 2  342 ? 14.743  3.364    9.696    1.00 42.25  ? 342 VAL   D CG2    1 
ATOM   12778 N  N      . GLU   D 2  343 ? 12.643  3.664    6.013    1.00 51.47  ? 343 GLU   D N      1 
ATOM   12779 C  CA     . GLU   D 2  343 ? 12.256  2.687    5.004    1.00 51.91  ? 343 GLU   D CA     1 
ATOM   12780 C  C      . GLU   D 2  343 ? 13.378  1.729    4.608    1.00 52.11  ? 343 GLU   D C      1 
ATOM   12781 O  O      . GLU   D 2  343 ? 13.082  0.684    4.020    1.00 56.37  ? 343 GLU   D O      1 
ATOM   12782 C  CB     . GLU   D 2  343 ? 11.754  3.415    3.761    1.00 50.86  ? 343 GLU   D CB     1 
ATOM   12783 C  CG     . GLU   D 2  343 ? 12.710  4.516    3.338    1.00 61.63  ? 343 GLU   D CG     1 
ATOM   12784 C  CD     . GLU   D 2  343 ? 12.404  5.074    1.963    1.00 71.32  ? 343 GLU   D CD     1 
ATOM   12785 O  OE1    . GLU   D 2  343 ? 11.290  4.811    1.440    1.00 69.54  ? 343 GLU   D OE1    1 
ATOM   12786 O  OE2    . GLU   D 2  343 ? 13.302  5.742    1.394    1.00 71.73  ? 343 GLU   D OE2    1 
ATOM   12787 N  N      . TRP   D 2  344 ? 14.640  2.048    4.908    1.00 42.82  ? 344 TRP   D N      1 
ATOM   12788 C  CA     . TRP   D 2  344 ? 15.783  1.222    4.522    1.00 44.70  ? 344 TRP   D CA     1 
ATOM   12789 C  C      . TRP   D 2  344 ? 16.109  0.118    5.543    1.00 45.57  ? 344 TRP   D C      1 
ATOM   12790 O  O      . TRP   D 2  344 ? 17.184  -0.493   5.454    1.00 45.36  ? 344 TRP   D O      1 
ATOM   12791 C  CB     . TRP   D 2  344 ? 17.031  2.106    4.271    1.00 45.95  ? 344 TRP   D CB     1 
ATOM   12792 C  CG     . TRP   D 2  344 ? 17.178  3.302    5.221    1.00 51.72  ? 344 TRP   D CG     1 
ATOM   12793 C  CD1    . TRP   D 2  344 ? 16.648  4.564    5.070    1.00 46.64  ? 344 TRP   D CD1    1 
ATOM   12794 C  CD2    . TRP   D 2  344 ? 17.897  3.322    6.459    1.00 50.37  ? 344 TRP   D CD2    1 
ATOM   12795 N  NE1    . TRP   D 2  344 ? 16.977  5.346    6.143    1.00 44.52  ? 344 TRP   D NE1    1 
ATOM   12796 C  CE2    . TRP   D 2  344 ? 17.744  4.610    7.010    1.00 47.03  ? 344 TRP   D CE2    1 
ATOM   12797 C  CE3    . TRP   D 2  344 ? 18.652  2.370    7.160    1.00 45.71  ? 344 TRP   D CE3    1 
ATOM   12798 C  CZ2    . TRP   D 2  344 ? 18.330  4.973    8.218    1.00 45.60  ? 344 TRP   D CZ2    1 
ATOM   12799 C  CZ3    . TRP   D 2  344 ? 19.219  2.729    8.363    1.00 43.46  ? 344 TRP   D CZ3    1 
ATOM   12800 C  CH2    . TRP   D 2  344 ? 19.057  4.022    8.881    1.00 45.34  ? 344 TRP   D CH2    1 
ATOM   12801 N  N      . ILE   D 2  345 ? 15.222  -0.146   6.503    1.00 42.98  ? 345 ILE   D N      1 
ATOM   12802 C  CA     . ILE   D 2  345 ? 15.374  -1.268   7.435    1.00 41.18  ? 345 ILE   D CA     1 
ATOM   12803 C  C      . ILE   D 2  345 ? 14.049  -2.011   7.525    1.00 39.44  ? 345 ILE   D C      1 
ATOM   12804 O  O      . ILE   D 2  345 ? 13.203  -1.660   8.360    1.00 42.36  ? 345 ILE   D O      1 
ATOM   12805 C  CB     . ILE   D 2  345 ? 15.780  -0.817   8.849    1.00 41.82  ? 345 ILE   D CB     1 
ATOM   12806 C  CG1    . ILE   D 2  345 ? 17.059  -0.001   8.868    1.00 38.16  ? 345 ILE   D CG1    1 
ATOM   12807 C  CG2    . ILE   D 2  345 ? 15.950  -2.016   9.746    1.00 39.48  ? 345 ILE   D CG2    1 
ATOM   12808 C  CD1    . ILE   D 2  345 ? 17.457  0.320    10.283   1.00 39.79  ? 345 ILE   D CD1    1 
ATOM   12809 N  N      . PRO   D 2  346 ? 13.831  -3.041   6.723    1.00 36.68  ? 346 PRO   D N      1 
ATOM   12810 C  CA     . PRO   D 2  346 ? 12.511  -3.677   6.677    1.00 33.80  ? 346 PRO   D CA     1 
ATOM   12811 C  C      . PRO   D 2  346 ? 12.162  -4.351   7.985    1.00 32.31  ? 346 PRO   D C      1 
ATOM   12812 O  O      . PRO   D 2  346 ? 13.024  -4.742   8.767    1.00 34.85  ? 346 PRO   D O      1 
ATOM   12813 C  CB     . PRO   D 2  346 ? 12.655  -4.704   5.555    1.00 29.56  ? 346 PRO   D CB     1 
ATOM   12814 C  CG     . PRO   D 2  346 ? 13.803  -4.189   4.752    1.00 34.04  ? 346 PRO   D CG     1 
ATOM   12815 C  CD     . PRO   D 2  346 ? 14.743  -3.604   5.728    1.00 36.28  ? 346 PRO   D CD     1 
ATOM   12816 N  N      . ASN   D 2  347 ? 10.863  -4.494   8.213    1.00 38.86  ? 347 ASN   D N      1 
ATOM   12817 C  CA     . ASN   D 2  347 ? 10.356  -5.247   9.355    1.00 31.84  ? 347 ASN   D CA     1 
ATOM   12818 C  C      . ASN   D 2  347 ? 11.130  -4.884   10.616   1.00 38.03  ? 347 ASN   D C      1 
ATOM   12819 O  O      . ASN   D 2  347 ? 11.643  -5.735   11.347   1.00 41.22  ? 347 ASN   D O      1 
ATOM   12820 C  CB     . ASN   D 2  347 ? 10.409  -6.734   9.051    1.00 32.30  ? 347 ASN   D CB     1 
ATOM   12821 C  CG     . ASN   D 2  347 ? 10.016  -7.035   7.582    1.00 38.58  ? 347 ASN   D CG     1 
ATOM   12822 O  OD1    . ASN   D 2  347 ? 10.877  -7.245   6.709    1.00 34.65  ? 347 ASN   D OD1    1 
ATOM   12823 N  ND2    . ASN   D 2  347 ? 8.712   -7.020   7.310    1.00 42.84  ? 347 ASN   D ND2    1 
ATOM   12824 N  N      . ASN   D 2  348 ? 11.227  -3.582   10.860   1.00 34.31  ? 348 ASN   D N      1 
ATOM   12825 C  CA     . ASN   D 2  348 ? 12.048  -3.078   11.939   1.00 39.59  ? 348 ASN   D CA     1 
ATOM   12826 C  C      . ASN   D 2  348 ? 11.245  -2.793   13.194   1.00 36.99  ? 348 ASN   D C      1 
ATOM   12827 O  O      . ASN   D 2  348 ? 11.760  -2.135   14.094   1.00 41.04  ? 348 ASN   D O      1 
ATOM   12828 C  CB     . ASN   D 2  348 ? 12.800  -1.828   11.482   1.00 42.30  ? 348 ASN   D CB     1 
ATOM   12829 C  CG     . ASN   D 2  348 ? 11.869  -0.698   11.121   1.00 44.08  ? 348 ASN   D CG     1 
ATOM   12830 O  OD1    . ASN   D 2  348 ? 10.704  -0.922   10.801   1.00 39.28  ? 348 ASN   D OD1    1 
ATOM   12831 N  ND2    . ASN   D 2  348 ? 12.373  0.526    11.190   1.00 43.33  ? 348 ASN   D ND2    1 
ATOM   12832 N  N      . VAL   D 2  349 ? 10.015  -3.293   13.284   1.00 38.70  ? 349 VAL   D N      1 
ATOM   12833 C  CA     . VAL   D 2  349 ? 9.168   -3.173   14.473   1.00 43.22  ? 349 VAL   D CA     1 
ATOM   12834 C  C      . VAL   D 2  349 ? 8.761   -4.581   14.910   1.00 47.30  ? 349 VAL   D C      1 
ATOM   12835 O  O      . VAL   D 2  349 ? 7.874   -5.187   14.294   1.00 46.68  ? 349 VAL   D O      1 
ATOM   12836 C  CB     . VAL   D 2  349 ? 7.926   -2.319   14.211   1.00 36.42  ? 349 VAL   D CB     1 
ATOM   12837 C  CG1    . VAL   D 2  349 ? 7.134   -2.169   15.492   1.00 42.14  ? 349 VAL   D CG1    1 
ATOM   12838 C  CG2    . VAL   D 2  349 ? 8.310   -0.989   13.641   1.00 36.24  ? 349 VAL   D CG2    1 
ATOM   12839 N  N      . LYS   D 2  350 ? 9.370   -5.105   15.980   1.00 42.12  ? 350 LYS   D N      1 
ATOM   12840 C  CA     . LYS   D 2  350 ? 8.996   -6.415   16.503   1.00 47.53  ? 350 LYS   D CA     1 
ATOM   12841 C  C      . LYS   D 2  350 ? 8.170   -6.264   17.766   1.00 45.19  ? 350 LYS   D C      1 
ATOM   12842 O  O      . LYS   D 2  350 ? 8.258   -5.269   18.490   1.00 52.75  ? 350 LYS   D O      1 
ATOM   12843 C  CB     . LYS   D 2  350 ? 10.217  -7.295   16.813   1.00 47.02  ? 350 LYS   D CB     1 
ATOM   12844 C  CG     . LYS   D 2  350 ? 10.160  -8.750   16.338   1.00 51.42  ? 350 LYS   D CG     1 
ATOM   12845 C  CD     . LYS   D 2  350 ? 10.047  -8.864   14.821   1.00 54.90  ? 350 LYS   D CD     1 
ATOM   12846 C  CE     . LYS   D 2  350 ? 11.374  -8.792   14.084   1.00 49.90  ? 350 LYS   D CE     1 
ATOM   12847 N  NZ     . LYS   D 2  350 ? 11.181  -8.392   12.657   1.00 47.80  ? 350 LYS   D NZ     1 
ATOM   12848 N  N      . THR   D 2  351 ? 7.383   -7.289   18.047   1.00 45.69  ? 351 THR   D N      1 
ATOM   12849 C  CA     . THR   D 2  351 ? 6.580   -7.284   19.257   1.00 58.22  ? 351 THR   D CA     1 
ATOM   12850 C  C      . THR   D 2  351 ? 6.652   -8.635   19.958   1.00 56.07  ? 351 THR   D C      1 
ATOM   12851 O  O      . THR   D 2  351 ? 6.912   -9.670   19.336   1.00 53.94  ? 351 THR   D O      1 
ATOM   12852 C  CB     . THR   D 2  351 ? 5.153   -6.896   18.917   1.00 60.10  ? 351 THR   D CB     1 
ATOM   12853 O  OG1    . THR   D 2  351 ? 4.705   -7.724   17.844   1.00 65.87  ? 351 THR   D OG1    1 
ATOM   12854 C  CG2    . THR   D 2  351 ? 5.106   -5.432   18.463   1.00 59.24  ? 351 THR   D CG2    1 
ATOM   12855 N  N      . ALA   D 2  352 ? 6.472   -8.602   21.278   1.00 56.72  ? 352 ALA   D N      1 
ATOM   12856 C  CA     . ALA   D 2  352 ? 6.391   -9.809   22.091   1.00 59.36  ? 352 ALA   D CA     1 
ATOM   12857 C  C      . ALA   D 2  352 ? 5.249   -9.648   23.081   1.00 57.91  ? 352 ALA   D C      1 
ATOM   12858 O  O      . ALA   D 2  352 ? 4.943   -8.531   23.506   1.00 57.87  ? 352 ALA   D O      1 
ATOM   12859 C  CB     . ALA   D 2  352 ? 7.693   -10.086  22.845   1.00 56.99  ? 352 ALA   D CB     1 
ATOM   12860 N  N      . VAL   D 2  353 ? 4.605   -10.762  23.435   1.00 57.06  ? 353 VAL   D N      1 
ATOM   12861 C  CA     . VAL   D 2  353 ? 3.569   -10.762  24.465   1.00 61.62  ? 353 VAL   D CA     1 
ATOM   12862 C  C      . VAL   D 2  353 ? 3.942   -11.767  25.541   1.00 60.52  ? 353 VAL   D C      1 
ATOM   12863 O  O      . VAL   D 2  353 ? 4.339   -12.896  25.231   1.00 54.01  ? 353 VAL   D O      1 
ATOM   12864 C  CB     . VAL   D 2  353 ? 2.175   -11.074  23.898   1.00 61.29  ? 353 VAL   D CB     1 
ATOM   12865 C  CG1    . VAL   D 2  353 ? 1.907   -10.252  22.641   1.00 65.88  ? 353 VAL   D CG1    1 
ATOM   12866 C  CG2    . VAL   D 2  353 ? 2.054   -12.540  23.626   1.00 65.91  ? 353 VAL   D CG2    1 
ATOM   12867 N  N      . CYS   D 2  354 ? 3.813   -11.342  26.801   1.00 59.82  ? 354 CYS   D N      1 
ATOM   12868 C  CA     . CYS   D 2  354 ? 3.953   -12.175  27.989   1.00 63.81  ? 354 CYS   D CA     1 
ATOM   12869 C  C      . CYS   D 2  354 ? 2.630   -12.201  28.760   1.00 68.93  ? 354 CYS   D C      1 
ATOM   12870 O  O      . CYS   D 2  354 ? 1.992   -11.157  28.957   1.00 67.54  ? 354 CYS   D O      1 
ATOM   12871 C  CB     . CYS   D 2  354 ? 5.100   -11.635  28.882   1.00 65.98  ? 354 CYS   D CB     1 
ATOM   12872 S  SG     . CYS   D 2  354 ? 5.286   -12.390  30.533   1.00 62.44  ? 354 CYS   D SG     1 
ATOM   12873 N  N      . ASP   D 2  355 ? 2.231   -13.389  29.224   1.00 68.32  ? 355 ASP   D N      1 
ATOM   12874 C  CA     . ASP   D 2  355 ? 0.901   -13.550  29.814   1.00 70.05  ? 355 ASP   D CA     1 
ATOM   12875 C  C      . ASP   D 2  355 ? 0.742   -12.852  31.166   1.00 75.00  ? 355 ASP   D C      1 
ATOM   12876 O  O      . ASP   D 2  355 ? -0.378  -12.467  31.523   1.00 75.07  ? 355 ASP   D O      1 
ATOM   12877 C  CB     . ASP   D 2  355 ? 0.581   -15.027  29.980   1.00 71.10  ? 355 ASP   D CB     1 
ATOM   12878 C  CG     . ASP   D 2  355 ? 0.072   -15.646  28.719   1.00 80.44  ? 355 ASP   D CG     1 
ATOM   12879 O  OD1    . ASP   D 2  355 ? -0.712  -14.981  28.001   1.00 86.92  ? 355 ASP   D OD1    1 
ATOM   12880 O  OD2    . ASP   D 2  355 ? 0.468   -16.797  28.446   1.00 80.36  ? 355 ASP   D OD2    1 
ATOM   12881 N  N      . ILE   D 2  356 ? 1.813   -12.693  31.938   1.00 70.15  ? 356 ILE   D N      1 
ATOM   12882 C  CA     . ILE   D 2  356 ? 1.731   -12.146  33.289   1.00 68.41  ? 356 ILE   D CA     1 
ATOM   12883 C  C      . ILE   D 2  356 ? 1.959   -10.635  33.231   1.00 71.63  ? 356 ILE   D C      1 
ATOM   12884 O  O      . ILE   D 2  356 ? 3.065   -10.205  32.862   1.00 73.95  ? 356 ILE   D O      1 
ATOM   12885 C  CB     . ILE   D 2  356 ? 2.745   -12.810  34.223   1.00 72.42  ? 356 ILE   D CB     1 
ATOM   12886 C  CG1    . ILE   D 2  356 ? 2.908   -11.954  35.490   1.00 78.06  ? 356 ILE   D CG1    1 
ATOM   12887 C  CG2    . ILE   D 2  356 ? 4.052   -13.046  33.500   1.00 72.99  ? 356 ILE   D CG2    1 
ATOM   12888 C  CD1    . ILE   D 2  356 ? 3.810   -12.571  36.549   1.00 78.83  ? 356 ILE   D CD1    1 
ATOM   12889 N  N      . PRO   D 2  357 ? 0.982   -9.815   33.622   1.00 70.89  ? 357 PRO   D N      1 
ATOM   12890 C  CA     . PRO   D 2  357 ? 1.172   -8.356   33.604   1.00 70.65  ? 357 PRO   D CA     1 
ATOM   12891 C  C      . PRO   D 2  357 ? 1.805   -7.877   34.891   1.00 70.30  ? 357 PRO   D C      1 
ATOM   12892 O  O      . PRO   D 2  357 ? 1.816   -8.610   35.887   1.00 76.78  ? 357 PRO   D O      1 
ATOM   12893 C  CB     . PRO   D 2  357 ? -0.255  -7.806   33.459   1.00 72.55  ? 357 PRO   D CB     1 
ATOM   12894 C  CG     . PRO   D 2  357 ? -1.178  -8.961   33.815   1.00 68.86  ? 357 PRO   D CG     1 
ATOM   12895 C  CD     . PRO   D 2  357 ? -0.370  -10.196  34.058   1.00 69.03  ? 357 PRO   D CD     1 
ATOM   12896 N  N      . PRO   D 2  358 ? 2.329   -6.654   34.913   1.00 71.09  ? 358 PRO   D N      1 
ATOM   12897 C  CA     . PRO   D 2  358 ? 2.896   -6.118   36.158   1.00 80.46  ? 358 PRO   D CA     1 
ATOM   12898 C  C      . PRO   D 2  358 ? 1.834   -6.039   37.249   1.00 84.26  ? 358 PRO   D C      1 
ATOM   12899 O  O      . PRO   D 2  358 ? 0.630   -6.027   36.980   1.00 80.79  ? 358 PRO   D O      1 
ATOM   12900 C  CB     . PRO   D 2  358 ? 3.394   -4.718   35.772   1.00 78.92  ? 358 PRO   D CB     1 
ATOM   12901 C  CG     . PRO   D 2  358 ? 3.123   -4.544   34.321   1.00 78.85  ? 358 PRO   D CG     1 
ATOM   12902 C  CD     . PRO   D 2  358 ? 2.405   -5.726   33.776   1.00 73.60  ? 358 PRO   D CD     1 
ATOM   12903 N  N      . ARG   D 2  359 ? 2.294   -5.973   38.497   1.00 84.40  ? 359 ARG   D N      1 
ATOM   12904 C  CA     . ARG   D 2  359 ? 1.367   -5.865   39.618   1.00 81.98  ? 359 ARG   D CA     1 
ATOM   12905 C  C      . ARG   D 2  359 ? 0.434   -4.685   39.414   1.00 84.16  ? 359 ARG   D C      1 
ATOM   12906 O  O      . ARG   D 2  359 ? 0.884   -3.554   39.198   1.00 85.97  ? 359 ARG   D O      1 
ATOM   12907 C  CB     . ARG   D 2  359 ? 2.126   -5.712   40.939   1.00 78.16  ? 359 ARG   D CB     1 
ATOM   12908 N  N      . GLY   D 2  360 ? -0.870  -4.959   39.456   1.00 78.20  ? 360 GLY   D N      1 
ATOM   12909 C  CA     . GLY   D 2  360 ? -1.871  -3.916   39.476   1.00 82.75  ? 360 GLY   D CA     1 
ATOM   12910 C  C      . GLY   D 2  360 ? -2.329  -3.400   38.130   1.00 87.92  ? 360 GLY   D C      1 
ATOM   12911 O  O      . GLY   D 2  360 ? -3.096  -2.427   38.091   1.00 93.73  ? 360 GLY   D O      1 
ATOM   12912 N  N      . LEU   D 2  361 ? -1.879  -3.998   37.029   1.00 83.30  ? 361 LEU   D N      1 
ATOM   12913 C  CA     . LEU   D 2  361 ? -2.379  -3.669   35.702   1.00 69.52  ? 361 LEU   D CA     1 
ATOM   12914 C  C      . LEU   D 2  361 ? -2.821  -4.957   35.040   1.00 74.93  ? 361 LEU   D C      1 
ATOM   12915 O  O      . LEU   D 2  361 ? -2.052  -5.921   34.981   1.00 80.96  ? 361 LEU   D O      1 
ATOM   12916 C  CB     . LEU   D 2  361 ? -1.324  -2.980   34.846   1.00 72.98  ? 361 LEU   D CB     1 
ATOM   12917 C  CG     . LEU   D 2  361 ? -1.246  -1.460   34.931   1.00 74.82  ? 361 LEU   D CG     1 
ATOM   12918 C  CD1    . LEU   D 2  361 ? -1.274  -0.980   36.373   1.00 78.57  ? 361 LEU   D CD1    1 
ATOM   12919 C  CD2    . LEU   D 2  361 ? -0.002  -0.979   34.220   1.00 74.30  ? 361 LEU   D CD2    1 
ATOM   12920 N  N      . LYS   D 2  362 ? -4.062  -4.978   34.557   1.00 81.58  ? 362 LYS   D N      1 
ATOM   12921 C  CA     . LYS   D 2  362 ? -4.565  -6.162   33.867   1.00 78.13  ? 362 LYS   D CA     1 
ATOM   12922 C  C      . LYS   D 2  362 ? -3.913  -6.306   32.493   1.00 77.12  ? 362 LYS   D C      1 
ATOM   12923 O  O      . LYS   D 2  362 ? -3.749  -7.427   31.990   1.00 72.36  ? 362 LYS   D O      1 
ATOM   12924 C  CB     . LYS   D 2  362 ? -6.090  -6.074   33.757   1.00 73.62  ? 362 LYS   D CB     1 
ATOM   12925 C  CG     . LYS   D 2  362 ? -6.834  -7.404   33.777   1.00 76.12  ? 362 LYS   D CG     1 
ATOM   12926 C  CD     . LYS   D 2  362 ? -8.310  -7.207   33.404   1.00 84.18  ? 362 LYS   D CD     1 
ATOM   12927 C  CE     . LYS   D 2  362 ? -9.036  -6.297   34.410   1.00 79.68  ? 362 LYS   D CE     1 
ATOM   12928 N  NZ     . LYS   D 2  362 ? -9.859  -5.236   33.758   1.00 79.54  ? 362 LYS   D NZ     1 
ATOM   12929 N  N      . MET   D 2  363 ? -3.505  -5.188   31.896   1.00 78.04  ? 363 MET   D N      1 
ATOM   12930 C  CA     . MET   D 2  363 ? -2.860  -5.192   30.592   1.00 76.84  ? 363 MET   D CA     1 
ATOM   12931 C  C      . MET   D 2  363 ? -1.928  -3.996   30.516   1.00 72.78  ? 363 MET   D C      1 
ATOM   12932 O  O      . MET   D 2  363 ? -2.372  -2.858   30.705   1.00 67.82  ? 363 MET   D O      1 
ATOM   12933 C  CB     . MET   D 2  363 ? -3.901  -5.129   29.487   1.00 73.96  ? 363 MET   D CB     1 
ATOM   12934 C  CG     . MET   D 2  363 ? -4.695  -6.405   29.355   1.00 73.66  ? 363 MET   D CG     1 
ATOM   12935 S  SD     . MET   D 2  363 ? -5.398  -6.475   27.718   1.00 88.62  ? 363 MET   D SD     1 
ATOM   12936 C  CE     . MET   D 2  363 ? -5.935  -4.773   27.547   1.00 75.04  ? 363 MET   D CE     1 
ATOM   12937 N  N      . SER   D 2  364 ? -0.650  -4.246   30.250   1.00 68.24  ? 364 SER   D N      1 
ATOM   12938 C  CA     . SER   D 2  364 ? 0.285   -3.161   30.003   1.00 71.33  ? 364 SER   D CA     1 
ATOM   12939 C  C      . SER   D 2  364 ? 0.904   -3.326   28.625   1.00 68.55  ? 364 SER   D C      1 
ATOM   12940 O  O      . SER   D 2  364 ? 0.752   -4.355   27.964   1.00 70.12  ? 364 SER   D O      1 
ATOM   12941 C  CB     . SER   D 2  364 ? 1.379   -3.095   31.081   1.00 71.60  ? 364 SER   D CB     1 
ATOM   12942 O  OG     . SER   D 2  364 ? 2.169   -4.275   31.103   1.00 78.28  ? 364 SER   D OG     1 
ATOM   12943 N  N      . ALA   D 2  365 ? 1.587   -2.272   28.192   1.00 66.58  ? 365 ALA   D N      1 
ATOM   12944 C  CA     . ALA   D 2  365 ? 2.476   -2.313   27.044   1.00 62.43  ? 365 ALA   D CA     1 
ATOM   12945 C  C      . ALA   D 2  365 ? 3.741   -1.574   27.428   1.00 64.51  ? 365 ALA   D C      1 
ATOM   12946 O  O      . ALA   D 2  365 ? 3.678   -0.599   28.179   1.00 69.03  ? 365 ALA   D O      1 
ATOM   12947 C  CB     . ALA   D 2  365 ? 1.847   -1.664   25.809   1.00 63.57  ? 365 ALA   D CB     1 
ATOM   12948 N  N      . THR   D 2  366 ? 4.885   -2.034   26.927   1.00 65.95  ? 366 THR   D N      1 
ATOM   12949 C  CA     . THR   D 2  366 ? 6.139   -1.304   27.087   1.00 61.31  ? 366 THR   D CA     1 
ATOM   12950 C  C      . THR   D 2  366 ? 6.841   -1.178   25.740   1.00 61.23  ? 366 THR   D C      1 
ATOM   12951 O  O      . THR   D 2  366 ? 6.845   -2.117   24.931   1.00 57.82  ? 366 THR   D O      1 
ATOM   12952 C  CB     . THR   D 2  366 ? 7.065   -1.971   28.092   1.00 54.45  ? 366 THR   D CB     1 
ATOM   12953 O  OG1    . THR   D 2  366 ? 6.332   -2.267   29.286   1.00 56.04  ? 366 THR   D OG1    1 
ATOM   12954 C  CG2    . THR   D 2  366 ? 8.200   -1.037   28.420   1.00 55.82  ? 366 THR   D CG2    1 
ATOM   12955 N  N      . PHE   D 2  367 ? 7.457   -0.017   25.517   1.00 53.70  ? 367 PHE   D N      1 
ATOM   12956 C  CA     . PHE   D 2  367 ? 7.888   0.392    24.188   1.00 49.87  ? 367 PHE   D CA     1 
ATOM   12957 C  C      . PHE   D 2  367 ? 9.338   0.847    24.245   1.00 51.09  ? 367 PHE   D C      1 
ATOM   12958 O  O      . PHE   D 2  367 ? 9.634   1.887    24.835   1.00 57.81  ? 367 PHE   D O      1 
ATOM   12959 C  CB     . PHE   D 2  367 ? 6.981   1.506    23.662   1.00 52.89  ? 367 PHE   D CB     1 
ATOM   12960 C  CG     . PHE   D 2  367 ? 7.550   2.280    22.503   1.00 52.59  ? 367 PHE   D CG     1 
ATOM   12961 C  CD1    . PHE   D 2  367 ? 8.425   3.336    22.708   1.00 51.56  ? 367 PHE   D CD1    1 
ATOM   12962 C  CD2    . PHE   D 2  367 ? 7.179   1.972    21.201   1.00 57.16  ? 367 PHE   D CD2    1 
ATOM   12963 C  CE1    . PHE   D 2  367 ? 8.935   4.060    21.624   1.00 58.52  ? 367 PHE   D CE1    1 
ATOM   12964 C  CE2    . PHE   D 2  367 ? 7.678   2.697    20.107   1.00 52.82  ? 367 PHE   D CE2    1 
ATOM   12965 C  CZ     . PHE   D 2  367 ? 8.559   3.743    20.319   1.00 54.12  ? 367 PHE   D CZ     1 
ATOM   12966 N  N      . ILE   D 2  368 ? 10.232  0.094    23.606   1.00 44.35  ? 368 ILE   D N      1 
ATOM   12967 C  CA     . ILE   D 2  368 ? 11.617  0.503    23.410   1.00 43.31  ? 368 ILE   D CA     1 
ATOM   12968 C  C      . ILE   D 2  368 ? 11.802  0.983    21.977   1.00 47.40  ? 368 ILE   D C      1 
ATOM   12969 O  O      . ILE   D 2  368 ? 11.621  0.212    21.030   1.00 51.46  ? 368 ILE   D O      1 
ATOM   12970 C  CB     . ILE   D 2  368 ? 12.582  -0.647   23.703   1.00 41.87  ? 368 ILE   D CB     1 
ATOM   12971 C  CG1    . ILE   D 2  368 ? 12.206  -1.316   25.028   1.00 45.21  ? 368 ILE   D CG1    1 
ATOM   12972 C  CG2    . ILE   D 2  368 ? 13.997  -0.110   23.662   1.00 41.70  ? 368 ILE   D CG2    1 
ATOM   12973 C  CD1    . ILE   D 2  368 ? 12.340  -2.827   25.041   1.00 44.79  ? 368 ILE   D CD1    1 
ATOM   12974 N  N      . GLY   D 2  369 ? 12.212  2.232    21.813   1.00 45.84  ? 369 GLY   D N      1 
ATOM   12975 C  CA     . GLY   D 2  369 ? 12.415  2.799    20.496   1.00 40.45  ? 369 GLY   D CA     1 
ATOM   12976 C  C      . GLY   D 2  369 ? 13.820  3.337    20.321   1.00 38.71  ? 369 GLY   D C      1 
ATOM   12977 O  O      . GLY   D 2  369 ? 14.445  3.813    21.255   1.00 46.19  ? 369 GLY   D O      1 
ATOM   12978 N  N      . ASN   D 2  370 ? 14.315  3.245    19.100   1.00 38.54  ? 370 ASN   D N      1 
ATOM   12979 C  CA     . ASN   D 2  370 ? 15.585  3.838    18.720   1.00 39.23  ? 370 ASN   D CA     1 
ATOM   12980 C  C      . ASN   D 2  370 ? 15.225  4.851    17.658   1.00 44.83  ? 370 ASN   D C      1 
ATOM   12981 O  O      . ASN   D 2  370 ? 15.190  4.529    16.470   1.00 47.65  ? 370 ASN   D O      1 
ATOM   12982 C  CB     . ASN   D 2  370 ? 16.556  2.819    18.209   1.00 43.26  ? 370 ASN   D CB     1 
ATOM   12983 C  CG     . ASN   D 2  370 ? 17.937  3.375    18.054   1.00 42.22  ? 370 ASN   D CG     1 
ATOM   12984 O  OD1    . ASN   D 2  370 ? 18.151  4.585    18.167   1.00 45.32  ? 370 ASN   D OD1    1 
ATOM   12985 N  ND2    . ASN   D 2  370 ? 18.889  2.506    17.785   1.00 43.57  ? 370 ASN   D ND2    1 
ATOM   12986 N  N      . SER   D 2  371 ? 14.950  6.074    18.088   1.00 54.02  ? 371 SER   D N      1 
ATOM   12987 C  CA     . SER   D 2  371 ? 14.452  7.123    17.214   1.00 54.11  ? 371 SER   D CA     1 
ATOM   12988 C  C      . SER   D 2  371 ? 15.499  8.211    17.053   1.00 51.59  ? 371 SER   D C      1 
ATOM   12989 O  O      . SER   D 2  371 ? 16.185  8.558    18.015   1.00 54.55  ? 371 SER   D O      1 
ATOM   12990 C  CB     . SER   D 2  371 ? 13.171  7.732    17.777   1.00 46.58  ? 371 SER   D CB     1 
ATOM   12991 O  OG     . SER   D 2  371 ? 12.947  8.981    17.167   1.00 55.41  ? 371 SER   D OG     1 
ATOM   12992 N  N      . THR   D 2  372 ? 15.612  8.758    15.838   1.00 53.47  ? 372 THR   D N      1 
ATOM   12993 C  CA     . THR   D 2  372 ? 16.510  9.889    15.635   1.00 53.31  ? 372 THR   D CA     1 
ATOM   12994 C  C      . THR   D 2  372 ? 16.021  11.139   16.358   1.00 58.25  ? 372 THR   D C      1 
ATOM   12995 O  O      . THR   D 2  372 ? 16.737  12.147   16.392   1.00 62.60  ? 372 THR   D O      1 
ATOM   12996 C  CB     . THR   D 2  372 ? 16.690  10.183   14.141   1.00 50.37  ? 372 THR   D CB     1 
ATOM   12997 O  OG1    . THR   D 2  372 ? 15.447  10.609   13.575   1.00 51.68  ? 372 THR   D OG1    1 
ATOM   12998 C  CG2    . THR   D 2  372 ? 17.167  8.950    13.409   1.00 49.08  ? 372 THR   D CG2    1 
ATOM   12999 N  N      . ALA   D 2  373 ? 14.821  11.094   16.936   1.00 55.15  ? 373 ALA   D N      1 
ATOM   13000 C  CA     . ALA   D 2  373 ? 14.319  12.202   17.735   1.00 58.82  ? 373 ALA   D CA     1 
ATOM   13001 C  C      . ALA   D 2  373 ? 15.000  12.292   19.095   1.00 62.54  ? 373 ALA   D C      1 
ATOM   13002 O  O      . ALA   D 2  373 ? 14.848  13.316   19.777   1.00 59.19  ? 373 ALA   D O      1 
ATOM   13003 C  CB     . ALA   D 2  373 ? 12.802  12.074   17.920   1.00 56.43  ? 373 ALA   D CB     1 
ATOM   13004 N  N      . ILE   D 2  374 ? 15.730  11.248   19.510   1.00 61.88  ? 374 ILE   D N      1 
ATOM   13005 C  CA     . ILE   D 2  374 ? 16.506  11.322   20.743   1.00 57.54  ? 374 ILE   D CA     1 
ATOM   13006 C  C      . ILE   D 2  374 ? 17.511  12.456   20.686   1.00 57.04  ? 374 ILE   D C      1 
ATOM   13007 O  O      . ILE   D 2  374 ? 17.943  12.945   21.726   1.00 55.30  ? 374 ILE   D O      1 
ATOM   13008 C  CB     . ILE   D 2  374 ? 17.228  10.000   21.041   1.00 56.57  ? 374 ILE   D CB     1 
ATOM   13009 C  CG1    . ILE   D 2  374 ? 17.479  9.891    22.543   1.00 56.71  ? 374 ILE   D CG1    1 
ATOM   13010 C  CG2    . ILE   D 2  374 ? 18.561  9.938    20.276   1.00 53.92  ? 374 ILE   D CG2    1 
ATOM   13011 C  CD1    . ILE   D 2  374 ? 16.367  9.221    23.298   1.00 56.36  ? 374 ILE   D CD1    1 
ATOM   13012 N  N      . GLN   D 2  375 ? 17.903  12.891   19.490   1.00 57.88  ? 375 GLN   D N      1 
ATOM   13013 C  CA     . GLN   D 2  375 ? 18.746  14.073   19.410   1.00 59.98  ? 375 GLN   D CA     1 
ATOM   13014 C  C      . GLN   D 2  375 ? 18.120  15.255   20.147   1.00 62.65  ? 375 GLN   D C      1 
ATOM   13015 O  O      . GLN   D 2  375 ? 18.840  16.162   20.574   1.00 59.42  ? 375 GLN   D O      1 
ATOM   13016 C  CB     . GLN   D 2  375 ? 19.016  14.427   17.949   1.00 56.14  ? 375 GLN   D CB     1 
ATOM   13017 C  CG     . GLN   D 2  375 ? 17.815  15.009   17.260   1.00 56.85  ? 375 GLN   D CG     1 
ATOM   13018 C  CD     . GLN   D 2  375 ? 18.118  15.415   15.843   1.00 60.74  ? 375 GLN   D CD     1 
ATOM   13019 O  OE1    . GLN   D 2  375 ? 19.080  16.144   15.580   1.00 63.14  ? 375 GLN   D OE1    1 
ATOM   13020 N  NE2    . GLN   D 2  375 ? 17.314  14.929   14.912   1.00 58.27  ? 375 GLN   D NE2    1 
ATOM   13021 N  N      . GLU   D 2  376 ? 16.787  15.268   20.297   1.00 64.70  ? 376 GLU   D N      1 
ATOM   13022 C  CA     . GLU   D 2  376 ? 16.126  16.280   21.124   1.00 61.13  ? 376 GLU   D CA     1 
ATOM   13023 C  C      . GLU   D 2  376 ? 16.665  16.256   22.555   1.00 63.53  ? 376 GLU   D C      1 
ATOM   13024 O  O      . GLU   D 2  376 ? 17.198  17.257   23.049   1.00 65.27  ? 376 GLU   D O      1 
ATOM   13025 C  CB     . GLU   D 2  376 ? 14.607  16.064   21.103   1.00 59.23  ? 376 GLU   D CB     1 
ATOM   13026 C  CG     . GLU   D 2  376 ? 13.927  16.501   19.800   1.00 61.11  ? 376 GLU   D CG     1 
ATOM   13027 C  CD     . GLU   D 2  376 ? 12.387  16.475   19.849   1.00 62.43  ? 376 GLU   D CD     1 
ATOM   13028 O  OE1    . GLU   D 2  376 ? 11.792  16.016   20.851   1.00 61.05  ? 376 GLU   D OE1    1 
ATOM   13029 O  OE2    . GLU   D 2  376 ? 11.768  16.908   18.854   1.00 61.50  ? 376 GLU   D OE2    1 
ATOM   13030 N  N      . LEU   D 2  377 ? 16.515  15.116   23.239   1.00 61.03  ? 377 LEU   D N      1 
ATOM   13031 C  CA     . LEU   D 2  377 ? 17.196  14.857   24.511   1.00 59.90  ? 377 LEU   D CA     1 
ATOM   13032 C  C      . LEU   D 2  377 ? 18.635  15.368   24.548   1.00 56.96  ? 377 LEU   D C      1 
ATOM   13033 O  O      . LEU   D 2  377 ? 19.004  16.140   25.429   1.00 63.62  ? 377 LEU   D O      1 
ATOM   13034 C  CB     . LEU   D 2  377 ? 17.165  13.351   24.791   1.00 60.28  ? 377 LEU   D CB     1 
ATOM   13035 C  CG     . LEU   D 2  377 ? 17.712  12.733   26.081   1.00 63.81  ? 377 LEU   D CG     1 
ATOM   13036 C  CD1    . LEU   D 2  377 ? 19.206  12.990   26.255   1.00 64.68  ? 377 LEU   D CD1    1 
ATOM   13037 C  CD2    . LEU   D 2  377 ? 16.920  13.209   27.289   1.00 70.43  ? 377 LEU   D CD2    1 
ATOM   13038 N  N      . PHE   D 2  378 ? 19.477  14.927   23.620   1.00 62.10  ? 378 PHE   D N      1 
ATOM   13039 C  CA     . PHE   D 2  378 ? 20.865  15.365   23.631   1.00 62.70  ? 378 PHE   D CA     1 
ATOM   13040 C  C      . PHE   D 2  378 ? 21.028  16.838   23.287   1.00 62.32  ? 378 PHE   D C      1 
ATOM   13041 O  O      . PHE   D 2  378 ? 22.038  17.430   23.666   1.00 66.40  ? 378 PHE   D O      1 
ATOM   13042 C  CB     . PHE   D 2  378 ? 21.696  14.527   22.663   1.00 60.90  ? 378 PHE   D CB     1 
ATOM   13043 C  CG     . PHE   D 2  378 ? 21.820  13.097   23.074   1.00 64.60  ? 378 PHE   D CG     1 
ATOM   13044 C  CD1    . PHE   D 2  378 ? 22.474  12.757   24.252   1.00 63.68  ? 378 PHE   D CD1    1 
ATOM   13045 C  CD2    . PHE   D 2  378 ? 21.271  12.086   22.292   1.00 60.42  ? 378 PHE   D CD2    1 
ATOM   13046 C  CE1    . PHE   D 2  378 ? 22.594  11.431   24.645   1.00 61.17  ? 378 PHE   D CE1    1 
ATOM   13047 C  CE2    . PHE   D 2  378 ? 21.378  10.759   22.674   1.00 60.20  ? 378 PHE   D CE2    1 
ATOM   13048 C  CZ     . PHE   D 2  378 ? 22.045  10.427   23.855   1.00 63.34  ? 378 PHE   D CZ     1 
ATOM   13049 N  N      . LYS   D 2  379 ? 20.086  17.441   22.562   1.00 60.64  ? 379 LYS   D N      1 
ATOM   13050 C  CA     . LYS   D 2  379 ? 20.233  18.854   22.225   1.00 62.52  ? 379 LYS   D CA     1 
ATOM   13051 C  C      . LYS   D 2  379 ? 19.997  19.735   23.449   1.00 67.83  ? 379 LYS   D C      1 
ATOM   13052 O  O      . LYS   D 2  379 ? 20.690  20.741   23.650   1.00 63.93  ? 379 LYS   D O      1 
ATOM   13053 C  CB     . LYS   D 2  379 ? 19.266  19.231   21.104   1.00 61.55  ? 379 LYS   D CB     1 
ATOM   13054 C  CG     . LYS   D 2  379 ? 19.583  18.621   19.749   1.00 63.13  ? 379 LYS   D CG     1 
ATOM   13055 C  CD     . LYS   D 2  379 ? 19.475  19.656   18.644   1.00 62.80  ? 379 LYS   D CD     1 
ATOM   13056 C  CE     . LYS   D 2  379 ? 18.924  19.055   17.373   1.00 61.89  ? 379 LYS   D CE     1 
ATOM   13057 N  NZ     . LYS   D 2  379 ? 18.603  20.108   16.360   1.00 66.07  ? 379 LYS   D NZ     1 
ATOM   13058 N  N      . ARG   D 2  380 ? 19.014  19.368   24.269   1.00 61.14  ? 380 ARG   D N      1 
ATOM   13059 C  CA     . ARG   D 2  380 ? 18.713  20.112   25.485   1.00 65.83  ? 380 ARG   D CA     1 
ATOM   13060 C  C      . ARG   D 2  380 ? 19.894  20.090   26.456   1.00 72.53  ? 380 ARG   D C      1 
ATOM   13061 O  O      . ARG   D 2  380 ? 20.260  21.127   27.027   1.00 73.01  ? 380 ARG   D O      1 
ATOM   13062 C  CB     . ARG   D 2  380 ? 17.445  19.531   26.117   1.00 63.20  ? 380 ARG   D CB     1 
ATOM   13063 C  CG     . ARG   D 2  380 ? 17.167  19.920   27.518   1.00 57.75  ? 380 ARG   D CG     1 
ATOM   13064 C  CD     . ARG   D 2  380 ? 16.126  18.988   28.093   1.00 66.66  ? 380 ARG   D CD     1 
ATOM   13065 N  NE     . ARG   D 2  380 ? 16.698  17.872   28.840   1.00 74.72  ? 380 ARG   D NE     1 
ATOM   13066 C  CZ     . ARG   D 2  380 ? 16.102  16.699   29.024   1.00 75.52  ? 380 ARG   D CZ     1 
ATOM   13067 N  NH1    . ARG   D 2  380 ? 14.940  16.416   28.457   1.00 72.30  ? 380 ARG   D NH1    1 
ATOM   13068 N  NH2    . ARG   D 2  380 ? 16.684  15.788   29.802   1.00 76.04  ? 380 ARG   D NH2    1 
ATOM   13069 N  N      . ILE   D 2  381 ? 20.510  18.919   26.658   1.00 68.53  ? 381 ILE   D N      1 
ATOM   13070 C  CA     . ILE   D 2  381 ? 21.723  18.875   27.472   1.00 67.98  ? 381 ILE   D CA     1 
ATOM   13071 C  C      . ILE   D 2  381 ? 22.827  19.694   26.815   1.00 71.93  ? 381 ILE   D C      1 
ATOM   13072 O  O      . ILE   D 2  381 ? 23.487  20.504   27.475   1.00 78.67  ? 381 ILE   D O      1 
ATOM   13073 C  CB     . ILE   D 2  381 ? 22.170  17.423   27.725   1.00 64.20  ? 381 ILE   D CB     1 
ATOM   13074 C  CG1    . ILE   D 2  381 ? 21.413  16.848   28.913   1.00 56.41  ? 381 ILE   D CG1    1 
ATOM   13075 C  CG2    . ILE   D 2  381 ? 23.678  17.371   27.992   1.00 58.93  ? 381 ILE   D CG2    1 
ATOM   13076 C  CD1    . ILE   D 2  381 ? 21.069  15.411   28.756   1.00 62.58  ? 381 ILE   D CD1    1 
ATOM   13077 N  N      . SER   D 2  382 ? 23.042  19.513   25.508   1.00 67.57  ? 382 SER   D N      1 
ATOM   13078 C  CA     . SER   D 2  382 ? 24.102  20.268   24.842   1.00 69.44  ? 382 SER   D CA     1 
ATOM   13079 C  C      . SER   D 2  382 ? 23.944  21.761   25.072   1.00 71.24  ? 382 SER   D C      1 
ATOM   13080 O  O      . SER   D 2  382 ? 24.939  22.483   25.182   1.00 75.36  ? 382 SER   D O      1 
ATOM   13081 C  CB     . SER   D 2  382 ? 24.123  19.972   23.338   1.00 71.25  ? 382 SER   D CB     1 
ATOM   13082 O  OG     . SER   D 2  382 ? 25.333  20.408   22.721   1.00 64.31  ? 382 SER   D OG     1 
ATOM   13083 N  N      . GLU   D 2  383 ? 22.708  22.244   25.146   1.00 76.49  ? 383 GLU   D N      1 
ATOM   13084 C  CA     . GLU   D 2  383 ? 22.496  23.681   25.247   1.00 77.16  ? 383 GLU   D CA     1 
ATOM   13085 C  C      . GLU   D 2  383 ? 22.860  24.187   26.631   1.00 80.31  ? 383 GLU   D C      1 
ATOM   13086 O  O      . GLU   D 2  383 ? 23.596  25.171   26.770   1.00 82.36  ? 383 GLU   D O      1 
ATOM   13087 C  CB     . GLU   D 2  383 ? 21.047  24.026   24.926   1.00 75.31  ? 383 GLU   D CB     1 
ATOM   13088 C  CG     . GLU   D 2  383 ? 20.806  25.510   24.915   1.00 83.51  ? 383 GLU   D CG     1 
ATOM   13089 C  CD     . GLU   D 2  383 ? 19.506  25.869   24.261   1.00 90.41  ? 383 GLU   D CD     1 
ATOM   13090 O  OE1    . GLU   D 2  383 ? 18.445  25.494   24.816   1.00 87.14  ? 383 GLU   D OE1    1 
ATOM   13091 O  OE2    . GLU   D 2  383 ? 19.553  26.510   23.180   1.00 95.52  ? 383 GLU   D OE2    1 
ATOM   13092 N  N      . GLN   D 2  384 ? 22.340  23.525   27.667   1.00 74.79  ? 384 GLN   D N      1 
ATOM   13093 C  CA     . GLN   D 2  384 ? 22.659  23.900   29.037   1.00 72.81  ? 384 GLN   D CA     1 
ATOM   13094 C  C      . GLN   D 2  384 ? 24.159  23.800   29.308   1.00 79.43  ? 384 GLN   D C      1 
ATOM   13095 O  O      . GLN   D 2  384 ? 24.735  24.665   29.976   1.00 85.91  ? 384 GLN   D O      1 
ATOM   13096 C  CB     . GLN   D 2  384 ? 21.861  23.015   29.981   1.00 68.57  ? 384 GLN   D CB     1 
ATOM   13097 C  CG     . GLN   D 2  384 ? 20.435  22.876   29.552   1.00 62.47  ? 384 GLN   D CG     1 
ATOM   13098 C  CD     . GLN   D 2  384 ? 19.725  21.792   30.316   1.00 73.15  ? 384 GLN   D CD     1 
ATOM   13099 O  OE1    . GLN   D 2  384 ? 20.367  20.930   30.919   1.00 76.50  ? 384 GLN   D OE1    1 
ATOM   13100 N  NE2    . GLN   D 2  384 ? 18.388  21.819   30.297   1.00 76.81  ? 384 GLN   D NE2    1 
ATOM   13101 N  N      . PHE   D 2  385 ? 24.807  22.755   28.805   1.00 77.89  ? 385 PHE   D N      1 
ATOM   13102 C  CA     . PHE   D 2  385 ? 26.259  22.695   28.814   1.00 76.62  ? 385 PHE   D CA     1 
ATOM   13103 C  C      . PHE   D 2  385 ? 26.821  24.047   28.382   1.00 81.28  ? 385 PHE   D C      1 
ATOM   13104 O  O      . PHE   D 2  385 ? 27.319  24.801   29.221   1.00 88.89  ? 385 PHE   D O      1 
ATOM   13105 C  CB     . PHE   D 2  385 ? 26.750  21.565   27.896   1.00 73.18  ? 385 PHE   D CB     1 
ATOM   13106 C  CG     . PHE   D 2  385 ? 28.243  21.319   27.942   1.00 68.14  ? 385 PHE   D CG     1 
ATOM   13107 C  CD1    . PHE   D 2  385 ? 28.800  20.511   28.922   1.00 69.51  ? 385 PHE   D CD1    1 
ATOM   13108 C  CD2    . PHE   D 2  385 ? 29.082  21.862   26.978   1.00 71.59  ? 385 PHE   D CD2    1 
ATOM   13109 C  CE1    . PHE   D 2  385 ? 30.164  20.274   28.951   1.00 68.00  ? 385 PHE   D CE1    1 
ATOM   13110 C  CE2    . PHE   D 2  385 ? 30.443  21.624   27.004   1.00 66.49  ? 385 PHE   D CE2    1 
ATOM   13111 C  CZ     . PHE   D 2  385 ? 30.983  20.833   27.987   1.00 66.27  ? 385 PHE   D CZ     1 
ATOM   13112 N  N      . THR   D 2  386 ? 26.705  24.390   27.094   1.00 78.59  ? 386 THR   D N      1 
ATOM   13113 C  CA     . THR   D 2  386 ? 27.449  25.525   26.542   1.00 86.10  ? 386 THR   D CA     1 
ATOM   13114 C  C      . THR   D 2  386 ? 27.138  26.848   27.232   1.00 89.71  ? 386 THR   D C      1 
ATOM   13115 O  O      . THR   D 2  386 ? 27.971  27.765   27.188   1.00 89.99  ? 386 THR   D O      1 
ATOM   13116 C  CB     . THR   D 2  386 ? 27.165  25.674   25.054   1.00 84.87  ? 386 THR   D CB     1 
ATOM   13117 O  OG1    . THR   D 2  386 ? 25.788  25.357   24.812   1.00 77.75  ? 386 THR   D OG1    1 
ATOM   13118 C  CG2    . THR   D 2  386 ? 28.068  24.753   24.262   1.00 84.81  ? 386 THR   D CG2    1 
ATOM   13119 N  N      . ALA   D 2  387 ? 25.952  26.982   27.835   1.00 88.31  ? 387 ALA   D N      1 
ATOM   13120 C  CA     . ALA   D 2  387 ? 25.665  28.161   28.646   1.00 86.18  ? 387 ALA   D CA     1 
ATOM   13121 C  C      . ALA   D 2  387 ? 26.672  28.297   29.779   1.00 91.73  ? 387 ALA   D C      1 
ATOM   13122 O  O      . ALA   D 2  387 ? 27.076  29.410   30.134   1.00 98.28  ? 387 ALA   D O      1 
ATOM   13123 C  CB     . ALA   D 2  387 ? 24.241  28.090   29.197   1.00 79.15  ? 387 ALA   D CB     1 
ATOM   13124 N  N      . MET   D 2  388 ? 27.099  27.173   30.352   1.00 85.24  ? 388 MET   D N      1 
ATOM   13125 C  CA     . MET   D 2  388 ? 28.143  27.210   31.364   1.00 86.42  ? 388 MET   D CA     1 
ATOM   13126 C  C      . MET   D 2  388 ? 29.533  27.202   30.736   1.00 88.86  ? 388 MET   D C      1 
ATOM   13127 O  O      . MET   D 2  388 ? 30.393  28.002   31.113   1.00 91.96  ? 388 MET   D O      1 
ATOM   13128 C  CB     . MET   D 2  388 ? 27.962  26.040   32.322   1.00 81.57  ? 388 MET   D CB     1 
ATOM   13129 C  CG     . MET   D 2  388 ? 26.619  26.112   32.988   1.00 86.79  ? 388 MET   D CG     1 
ATOM   13130 S  SD     . MET   D 2  388 ? 26.352  24.946   34.323   1.00 96.83  ? 388 MET   D SD     1 
ATOM   13131 C  CE     . MET   D 2  388 ? 24.553  24.865   34.263   1.00 82.02  ? 388 MET   D CE     1 
ATOM   13132 N  N      . PHE   D 2  389 ? 29.773  26.319   29.767   1.00 88.88  ? 389 PHE   D N      1 
ATOM   13133 C  CA     . PHE   D 2  389 ? 31.128  26.189   29.238   1.00 87.49  ? 389 PHE   D CA     1 
ATOM   13134 C  C      . PHE   D 2  389 ? 31.576  27.446   28.496   1.00 88.48  ? 389 PHE   D C      1 
ATOM   13135 O  O      . PHE   D 2  389 ? 32.764  27.785   28.539   1.00 87.32  ? 389 PHE   D O      1 
ATOM   13136 C  CB     . PHE   D 2  389 ? 31.237  24.955   28.337   1.00 81.75  ? 389 PHE   D CB     1 
ATOM   13137 C  CG     . PHE   D 2  389 ? 32.659  24.568   28.008   1.00 80.50  ? 389 PHE   D CG     1 
ATOM   13138 C  CD1    . PHE   D 2  389 ? 33.503  24.060   28.993   1.00 75.06  ? 389 PHE   D CD1    1 
ATOM   13139 C  CD2    . PHE   D 2  389 ? 33.154  24.722   26.715   1.00 75.50  ? 389 PHE   D CD2    1 
ATOM   13140 C  CE1    . PHE   D 2  389 ? 34.809  23.714   28.694   1.00 74.51  ? 389 PHE   D CE1    1 
ATOM   13141 C  CE2    . PHE   D 2  389 ? 34.458  24.372   26.408   1.00 78.32  ? 389 PHE   D CE2    1 
ATOM   13142 C  CZ     . PHE   D 2  389 ? 35.288  23.865   27.400   1.00 80.91  ? 389 PHE   D CZ     1 
ATOM   13143 N  N      . ARG   D 2  390 ? 30.661  28.151   27.815   1.00 90.65  ? 390 ARG   D N      1 
ATOM   13144 C  CA     . ARG   D 2  390 ? 31.035  29.424   27.196   1.00 92.98  ? 390 ARG   D CA     1 
ATOM   13145 C  C      . ARG   D 2  390 ? 31.557  30.413   28.234   1.00 93.15  ? 390 ARG   D C      1 
ATOM   13146 O  O      . ARG   D 2  390 ? 32.441  31.227   27.931   1.00 82.25  ? 390 ARG   D O      1 
ATOM   13147 C  CB     . ARG   D 2  390 ? 29.842  30.022   26.443   1.00 92.11  ? 390 ARG   D CB     1 
ATOM   13148 C  CG     . ARG   D 2  390 ? 30.012  30.021   24.928   1.00 99.44  ? 390 ARG   D CG     1 
ATOM   13149 C  CD     . ARG   D 2  390 ? 29.418  31.276   24.294   1.00 101.55 ? 390 ARG   D CD     1 
ATOM   13150 N  NE     . ARG   D 2  390 ? 29.540  31.272   22.838   1.00 104.81 ? 390 ARG   D NE     1 
ATOM   13151 C  CZ     . ARG   D 2  390 ? 30.648  31.581   22.175   1.00 103.69 ? 390 ARG   D CZ     1 
ATOM   13152 N  NH1    . ARG   D 2  390 ? 31.765  31.907   22.807   1.00 105.07 ? 390 ARG   D NH1    1 
ATOM   13153 N  NH2    . ARG   D 2  390 ? 30.636  31.562   20.844   1.00 93.34  ? 390 ARG   D NH2    1 
ATOM   13154 N  N      . ARG   D 2  391 ? 31.023  30.335   29.463   1.00 97.19  ? 391 ARG   D N      1 
ATOM   13155 C  CA     . ARG   D 2  391 ? 31.369  31.148   30.628   1.00 93.19  ? 391 ARG   D CA     1 
ATOM   13156 C  C      . ARG   D 2  391 ? 32.607  30.658   31.374   1.00 89.93  ? 391 ARG   D C      1 
ATOM   13157 O  O      . ARG   D 2  391 ? 33.128  31.394   32.215   1.00 90.86  ? 391 ARG   D O      1 
ATOM   13158 C  CB     . ARG   D 2  391 ? 30.204  31.163   31.632   1.00 90.84  ? 391 ARG   D CB     1 
ATOM   13159 C  CG     . ARG   D 2  391 ? 28.929  31.863   31.195   1.00 88.39  ? 391 ARG   D CG     1 
ATOM   13160 C  CD     . ARG   D 2  391 ? 28.074  32.217   32.409   1.00 89.54  ? 391 ARG   D CD     1 
ATOM   13161 N  NE     . ARG   D 2  391 ? 27.559  31.036   33.098   1.00 93.29  ? 391 ARG   D NE     1 
ATOM   13162 C  CZ     . ARG   D 2  391 ? 26.523  31.040   33.928   1.00 95.54  ? 391 ARG   D CZ     1 
ATOM   13163 N  NH1    . ARG   D 2  391 ? 25.866  32.155   34.211   1.00 94.46  ? 391 ARG   D NH1    1 
ATOM   13164 N  NH2    . ARG   D 2  391 ? 26.133  29.896   34.486   1.00 93.42  ? 391 ARG   D NH2    1 
ATOM   13165 N  N      . LYS   D 2  392 ? 33.065  29.433   31.127   1.00 89.88  ? 392 LYS   D N      1 
ATOM   13166 C  CA     . LYS   D 2  392 ? 34.107  28.778   31.909   1.00 86.17  ? 392 LYS   D CA     1 
ATOM   13167 C  C      . LYS   D 2  392 ? 33.658  28.493   33.335   1.00 80.83  ? 392 LYS   D C      1 
ATOM   13168 O  O      . LYS   D 2  392 ? 34.488  28.125   34.165   1.00 85.03  ? 392 LYS   D O      1 
ATOM   13169 C  CB     . LYS   D 2  392 ? 35.401  29.599   31.935   1.00 88.11  ? 392 LYS   D CB     1 
ATOM   13170 C  CG     . LYS   D 2  392 ? 35.967  29.986   30.570   1.00 84.17  ? 392 LYS   D CG     1 
ATOM   13171 C  CD     . LYS   D 2  392 ? 37.060  29.041   30.127   1.00 84.29  ? 392 LYS   D CD     1 
ATOM   13172 C  CE     . LYS   D 2  392 ? 38.153  29.803   29.395   1.00 86.61  ? 392 LYS   D CE     1 
ATOM   13173 N  NZ     . LYS   D 2  392 ? 39.057  28.900   28.623   1.00 85.58  ? 392 LYS   D NZ     1 
ATOM   13174 N  N      . ALA   D 2  393 ? 32.360  28.617   33.627   1.00 78.93  ? 393 ALA   D N      1 
ATOM   13175 C  CA     . ALA   D 2  393 ? 31.837  28.468   34.984   1.00 86.07  ? 393 ALA   D CA     1 
ATOM   13176 C  C      . ALA   D 2  393 ? 32.197  27.122   35.609   1.00 85.70  ? 393 ALA   D C      1 
ATOM   13177 O  O      . ALA   D 2  393 ? 32.126  26.076   34.963   1.00 90.54  ? 393 ALA   D O      1 
ATOM   13178 C  CB     . ALA   D 2  393 ? 30.312  28.636   34.978   1.00 85.02  ? 393 ALA   D CB     1 
ATOM   13179 N  N      . PHE   D 2  394 ? 32.565  27.158   36.889   1.00 90.14  ? 394 PHE   D N      1 
ATOM   13180 C  CA     . PHE   D 2  394 ? 32.825  26.001   37.751   1.00 92.65  ? 394 PHE   D CA     1 
ATOM   13181 C  C      . PHE   D 2  394 ? 33.868  25.047   37.192   1.00 91.21  ? 394 PHE   D C      1 
ATOM   13182 O  O      . PHE   D 2  394 ? 34.015  23.932   37.712   1.00 93.50  ? 394 PHE   D O      1 
ATOM   13183 C  CB     . PHE   D 2  394 ? 31.545  25.221   38.075   1.00 91.41  ? 394 PHE   D CB     1 
ATOM   13184 C  CG     . PHE   D 2  394 ? 30.384  26.094   38.463   1.00 96.24  ? 394 PHE   D CG     1 
ATOM   13185 C  CD1    . PHE   D 2  394 ? 29.744  26.881   37.512   1.00 90.35  ? 394 PHE   D CD1    1 
ATOM   13186 C  CD2    . PHE   D 2  394 ? 29.935  26.133   39.777   1.00 96.61  ? 394 PHE   D CD2    1 
ATOM   13187 C  CE1    . PHE   D 2  394 ? 28.687  27.682   37.859   1.00 96.68  ? 394 PHE   D CE1    1 
ATOM   13188 C  CE2    . PHE   D 2  394 ? 28.870  26.937   40.134   1.00 94.13  ? 394 PHE   D CE2    1 
ATOM   13189 C  CZ     . PHE   D 2  394 ? 28.244  27.711   39.176   1.00 95.40  ? 394 PHE   D CZ     1 
ATOM   13190 N  N      . LEU   D 2  395 ? 34.618  25.465   36.166   1.00 88.88  ? 395 LEU   D N      1 
ATOM   13191 C  CA     . LEU   D 2  395 ? 35.725  24.658   35.660   1.00 90.65  ? 395 LEU   D CA     1 
ATOM   13192 C  C      . LEU   D 2  395 ? 36.700  24.262   36.758   1.00 95.93  ? 395 LEU   D C      1 
ATOM   13193 O  O      . LEU   D 2  395 ? 37.454  23.294   36.589   1.00 94.35  ? 395 LEU   D O      1 
ATOM   13194 C  CB     . LEU   D 2  395 ? 36.478  25.419   34.563   1.00 83.37  ? 395 LEU   D CB     1 
ATOM   13195 C  CG     . LEU   D 2  395 ? 36.156  24.959   33.143   1.00 91.20  ? 395 LEU   D CG     1 
ATOM   13196 C  CD1    . LEU   D 2  395 ? 37.312  25.241   32.184   1.00 87.77  ? 395 LEU   D CD1    1 
ATOM   13197 C  CD2    . LEU   D 2  395 ? 35.791  23.481   33.151   1.00 87.02  ? 395 LEU   D CD2    1 
ATOM   13198 N  N      . HIS   D 2  396 ? 36.701  24.993   37.879   1.00 97.32  ? 396 HIS   D N      1 
ATOM   13199 C  CA     . HIS   D 2  396 ? 37.621  24.692   38.967   1.00 92.57  ? 396 HIS   D CA     1 
ATOM   13200 C  C      . HIS   D 2  396 ? 37.232  23.400   39.680   1.00 94.51  ? 396 HIS   D C      1 
ATOM   13201 O  O      . HIS   D 2  396 ? 38.108  22.638   40.109   1.00 96.70  ? 396 HIS   D O      1 
ATOM   13202 C  CB     . HIS   D 2  396 ? 37.699  25.877   39.945   1.00 97.12  ? 396 HIS   D CB     1 
ATOM   13203 C  CG     . HIS   D 2  396 ? 36.378  26.299   40.529   1.00 102.52 ? 396 HIS   D CG     1 
ATOM   13204 N  ND1    . HIS   D 2  396 ? 35.879  25.777   41.707   1.00 105.89 ? 396 HIS   D ND1    1 
ATOM   13205 C  CD2    . HIS   D 2  396 ? 35.472  27.222   40.119   1.00 95.49  ? 396 HIS   D CD2    1 
ATOM   13206 C  CE1    . HIS   D 2  396 ? 34.715  26.341   41.981   1.00 103.67 ? 396 HIS   D CE1    1 
ATOM   13207 N  NE2    . HIS   D 2  396 ? 34.445  27.222   41.033   1.00 95.77  ? 396 HIS   D NE2    1 
ATOM   13208 N  N      . TRP   D 2  397 ? 35.931  23.117   39.807   1.00 89.97  ? 397 TRP   D N      1 
ATOM   13209 C  CA     . TRP   D 2  397 ? 35.548  21.826   40.369   1.00 94.98  ? 397 TRP   D CA     1 
ATOM   13210 C  C      . TRP   D 2  397 ? 36.140  20.668   39.568   1.00 95.56  ? 397 TRP   D C      1 
ATOM   13211 O  O      . TRP   D 2  397 ? 36.199  19.539   40.075   1.00 94.03  ? 397 TRP   D O      1 
ATOM   13212 C  CB     . TRP   D 2  397 ? 34.023  21.684   40.439   1.00 94.62  ? 397 TRP   D CB     1 
ATOM   13213 C  CG     . TRP   D 2  397 ? 33.331  22.608   41.413   1.00 102.63 ? 397 TRP   D CG     1 
ATOM   13214 C  CD1    . TRP   D 2  397 ? 32.437  23.596   41.102   1.00 104.13 ? 397 TRP   D CD1    1 
ATOM   13215 C  CD2    . TRP   D 2  397 ? 33.448  22.611   42.849   1.00 108.22 ? 397 TRP   D CD2    1 
ATOM   13216 N  NE1    . TRP   D 2  397 ? 32.006  24.224   42.247   1.00 102.94 ? 397 TRP   D NE1    1 
ATOM   13217 C  CE2    . TRP   D 2  397 ? 32.610  23.643   43.332   1.00 108.99 ? 397 TRP   D CE2    1 
ATOM   13218 C  CE3    . TRP   D 2  397 ? 34.185  21.851   43.772   1.00 108.53 ? 397 TRP   D CE3    1 
ATOM   13219 C  CZ2    . TRP   D 2  397 ? 32.489  23.937   44.701   1.00 112.45 ? 397 TRP   D CZ2    1 
ATOM   13220 C  CZ3    . TRP   D 2  397 ? 34.064  22.148   45.137   1.00 110.47 ? 397 TRP   D CZ3    1 
ATOM   13221 C  CH2    . TRP   D 2  397 ? 33.221  23.181   45.583   1.00 110.32 ? 397 TRP   D CH2    1 
ATOM   13222 N  N      . TYR   D 2  398 ? 36.605  20.929   38.341   1.00 92.25  ? 398 TYR   D N      1 
ATOM   13223 C  CA     . TYR   D 2  398 ? 37.076  19.890   37.431   1.00 92.79  ? 398 TYR   D CA     1 
ATOM   13224 C  C      . TYR   D 2  398 ? 38.561  20.014   37.102   1.00 91.82  ? 398 TYR   D C      1 
ATOM   13225 O  O      . TYR   D 2  398 ? 39.311  19.047   37.289   1.00 90.59  ? 398 TYR   D O      1 
ATOM   13226 C  CB     . TYR   D 2  398 ? 36.220  19.908   36.151   1.00 92.53  ? 398 TYR   D CB     1 
ATOM   13227 C  CG     . TYR   D 2  398 ? 34.748  19.670   36.423   1.00 84.92  ? 398 TYR   D CG     1 
ATOM   13228 C  CD1    . TYR   D 2  398 ? 34.276  18.398   36.712   1.00 83.37  ? 398 TYR   D CD1    1 
ATOM   13229 C  CD2    . TYR   D 2  398 ? 33.839  20.716   36.407   1.00 83.82  ? 398 TYR   D CD2    1 
ATOM   13230 C  CE1    . TYR   D 2  398 ? 32.942  18.173   36.973   1.00 81.29  ? 398 TYR   D CE1    1 
ATOM   13231 C  CE2    . TYR   D 2  398 ? 32.498  20.498   36.664   1.00 82.57  ? 398 TYR   D CE2    1 
ATOM   13232 C  CZ     . TYR   D 2  398 ? 32.057  19.226   36.949   1.00 78.22  ? 398 TYR   D CZ     1 
ATOM   13233 O  OH     . TYR   D 2  398 ? 30.726  19.001   37.209   1.00 73.34  ? 398 TYR   D OH     1 
ATOM   13234 N  N      . THR   D 2  399 ? 39.014  21.174   36.602   1.00 89.80  ? 399 THR   D N      1 
ATOM   13235 C  CA     . THR   D 2  399 ? 40.451  21.386   36.414   1.00 86.77  ? 399 THR   D CA     1 
ATOM   13236 C  C      . THR   D 2  399 ? 41.218  21.278   37.732   1.00 88.83  ? 399 THR   D C      1 
ATOM   13237 O  O      . THR   D 2  399 ? 42.404  20.927   37.736   1.00 87.33  ? 399 THR   D O      1 
ATOM   13238 C  CB     . THR   D 2  399 ? 40.711  22.743   35.755   1.00 83.32  ? 399 THR   D CB     1 
ATOM   13239 O  OG1    . THR   D 2  399 ? 39.911  23.755   36.379   1.00 89.26  ? 399 THR   D OG1    1 
ATOM   13240 C  CG2    . THR   D 2  399 ? 40.385  22.686   34.289   1.00 87.93  ? 399 THR   D CG2    1 
ATOM   13241 N  N      . GLY   D 2  400 ? 40.563  21.573   38.856   1.00 86.28  ? 400 GLY   D N      1 
ATOM   13242 C  CA     . GLY   D 2  400 ? 41.193  21.347   40.146   1.00 87.83  ? 400 GLY   D CA     1 
ATOM   13243 C  C      . GLY   D 2  400 ? 41.478  19.882   40.413   1.00 87.42  ? 400 GLY   D C      1 
ATOM   13244 O  O      . GLY   D 2  400 ? 42.554  19.531   40.901   1.00 87.49  ? 400 GLY   D O      1 
ATOM   13245 N  N      . GLU   D 2  401 ? 40.521  19.004   40.094   1.00 86.49  ? 401 GLU   D N      1 
ATOM   13246 C  CA     . GLU   D 2  401 ? 40.745  17.568   40.249   1.00 84.41  ? 401 GLU   D CA     1 
ATOM   13247 C  C      . GLU   D 2  401 ? 41.695  16.990   39.204   1.00 78.73  ? 401 GLU   D C      1 
ATOM   13248 O  O      . GLU   D 2  401 ? 41.951  15.781   39.231   1.00 77.98  ? 401 GLU   D O      1 
ATOM   13249 C  CB     . GLU   D 2  401 ? 39.414  16.827   40.222   1.00 79.45  ? 401 GLU   D CB     1 
ATOM   13250 C  CG     . GLU   D 2  401 ? 38.537  17.174   41.411   1.00 85.43  ? 401 GLU   D CG     1 
ATOM   13251 C  CD     . GLU   D 2  401 ? 38.819  16.289   42.614   1.00 87.48  ? 401 GLU   D CD     1 
ATOM   13252 O  OE1    . GLU   D 2  401 ? 39.819  15.538   42.566   1.00 89.24  ? 401 GLU   D OE1    1 
ATOM   13253 O  OE2    . GLU   D 2  401 ? 38.059  16.357   43.611   1.00 82.15  ? 401 GLU   D OE2    1 
ATOM   13254 N  N      . GLY   D 2  402 ? 42.232  17.815   38.312   1.00 78.31  ? 402 GLY   D N      1 
ATOM   13255 C  CA     . GLY   D 2  402 ? 43.298  17.416   37.419   1.00 84.73  ? 402 GLY   D CA     1 
ATOM   13256 C  C      . GLY   D 2  402 ? 42.936  17.394   35.953   1.00 90.79  ? 402 GLY   D C      1 
ATOM   13257 O  O      . GLY   D 2  402 ? 43.759  16.960   35.137   1.00 95.65  ? 402 GLY   D O      1 
ATOM   13258 N  N      . MET   D 2  403 ? 41.747  17.855   35.590   1.00 85.42  ? 403 MET   D N      1 
ATOM   13259 C  CA     . MET   D 2  403 ? 41.218  17.654   34.253   1.00 87.21  ? 403 MET   D CA     1 
ATOM   13260 C  C      . MET   D 2  403 ? 41.643  18.783   33.330   1.00 86.33  ? 403 MET   D C      1 
ATOM   13261 O  O      . MET   D 2  403 ? 41.727  19.941   33.745   1.00 85.44  ? 403 MET   D O      1 
ATOM   13262 C  CB     . MET   D 2  403 ? 39.692  17.563   34.302   1.00 91.08  ? 403 MET   D CB     1 
ATOM   13263 C  CG     . MET   D 2  403 ? 39.106  16.298   33.700   1.00 87.87  ? 403 MET   D CG     1 
ATOM   13264 S  SD     . MET   D 2  403 ? 37.299  16.322   33.820   1.00 92.37  ? 403 MET   D SD     1 
ATOM   13265 C  CE     . MET   D 2  403 ? 37.081  16.300   35.588   1.00 76.84  ? 403 MET   D CE     1 
ATOM   13266 N  N      . ASP   D 2  404 ? 41.913  18.434   32.074   1.00 92.72  ? 404 ASP   D N      1 
ATOM   13267 C  CA     . ASP   D 2  404 ? 42.204  19.430   31.055   1.00 88.32  ? 404 ASP   D CA     1 
ATOM   13268 C  C      . ASP   D 2  404 ? 40.911  20.059   30.554   1.00 85.43  ? 404 ASP   D C      1 
ATOM   13269 O  O      . ASP   D 2  404 ? 39.834  19.458   30.609   1.00 83.43  ? 404 ASP   D O      1 
ATOM   13270 C  CB     . ASP   D 2  404 ? 42.971  18.805   29.884   1.00 89.75  ? 404 ASP   D CB     1 
ATOM   13271 C  CG     . ASP   D 2  404 ? 43.552  19.849   28.923   1.00 93.71  ? 404 ASP   D CG     1 
ATOM   13272 O  OD1    . ASP   D 2  404 ? 43.246  21.054   29.068   1.00 88.13  ? 404 ASP   D OD1    1 
ATOM   13273 O  OD2    . ASP   D 2  404 ? 44.297  19.452   27.994   1.00 94.59  ? 404 ASP   D OD2    1 
ATOM   13274 N  N      . GLU   D 2  405 ? 41.025  21.301   30.086   1.00 88.81  ? 405 GLU   D N      1 
ATOM   13275 C  CA     . GLU   D 2  405 ? 39.906  21.941   29.408   1.00 84.74  ? 405 GLU   D CA     1 
ATOM   13276 C  C      . GLU   D 2  405 ? 39.613  21.268   28.071   1.00 88.82  ? 405 GLU   D C      1 
ATOM   13277 O  O      . GLU   D 2  405 ? 38.452  21.208   27.649   1.00 89.85  ? 405 GLU   D O      1 
ATOM   13278 C  CB     . GLU   D 2  405 ? 40.207  23.424   29.197   1.00 84.71  ? 405 GLU   D CB     1 
ATOM   13279 C  CG     . GLU   D 2  405 ? 39.055  24.371   29.490   1.00 87.24  ? 405 GLU   D CG     1 
ATOM   13280 C  CD     . GLU   D 2  405 ? 39.252  25.747   28.845   1.00 95.66  ? 405 GLU   D CD     1 
ATOM   13281 O  OE1    . GLU   D 2  405 ? 39.246  25.832   27.590   1.00 93.95  ? 405 GLU   D OE1    1 
ATOM   13282 O  OE2    . GLU   D 2  405 ? 39.415  26.741   29.594   1.00 92.43  ? 405 GLU   D OE2    1 
ATOM   13283 N  N      . MET   D 2  406 ? 40.647  20.764   27.387   1.00 86.12  ? 406 MET   D N      1 
ATOM   13284 C  CA     . MET   D 2  406 ? 40.421  20.036   26.143   1.00 88.14  ? 406 MET   D CA     1 
ATOM   13285 C  C      . MET   D 2  406 ? 39.385  18.930   26.322   1.00 86.11  ? 406 MET   D C      1 
ATOM   13286 O  O      . MET   D 2  406 ? 38.593  18.670   25.412   1.00 86.99  ? 406 MET   D O      1 
ATOM   13287 C  CB     . MET   D 2  406 ? 41.738  19.454   25.619   1.00 87.62  ? 406 MET   D CB     1 
ATOM   13288 C  CG     . MET   D 2  406 ? 42.392  20.292   24.541   1.00 92.62  ? 406 MET   D CG     1 
ATOM   13289 S  SD     . MET   D 2  406 ? 41.426  20.258   23.015   1.00 114.94 ? 406 MET   D SD     1 
ATOM   13290 C  CE     . MET   D 2  406 ? 42.704  20.209   21.754   1.00 103.57 ? 406 MET   D CE     1 
ATOM   13291 N  N      . GLU   D 2  407 ? 39.358  18.293   27.497   1.00 85.13  ? 407 GLU   D N      1 
ATOM   13292 C  CA     . GLU   D 2  407 ? 38.439  17.187   27.760   1.00 78.83  ? 407 GLU   D CA     1 
ATOM   13293 C  C      . GLU   D 2  407 ? 36.974  17.622   27.724   1.00 76.65  ? 407 GLU   D C      1 
ATOM   13294 O  O      . GLU   D 2  407 ? 36.107  16.847   27.314   1.00 78.14  ? 407 GLU   D O      1 
ATOM   13295 C  CB     . GLU   D 2  407 ? 38.788  16.566   29.113   1.00 84.77  ? 407 GLU   D CB     1 
ATOM   13296 C  CG     . GLU   D 2  407 ? 37.983  15.356   29.529   1.00 80.13  ? 407 GLU   D CG     1 
ATOM   13297 C  CD     . GLU   D 2  407 ? 38.771  14.466   30.474   1.00 82.46  ? 407 GLU   D CD     1 
ATOM   13298 O  OE1    . GLU   D 2  407 ? 39.990  14.707   30.640   1.00 82.83  ? 407 GLU   D OE1    1 
ATOM   13299 O  OE2    . GLU   D 2  407 ? 38.169  13.543   31.062   1.00 80.83  ? 407 GLU   D OE2    1 
ATOM   13300 N  N      . PHE   D 2  408 ? 36.668  18.838   28.165   1.00 82.02  ? 408 PHE   D N      1 
ATOM   13301 C  CA     . PHE   D 2  408 ? 35.307  19.343   28.013   1.00 79.48  ? 408 PHE   D CA     1 
ATOM   13302 C  C      . PHE   D 2  408 ? 34.992  19.624   26.547   1.00 83.54  ? 408 PHE   D C      1 
ATOM   13303 O  O      . PHE   D 2  408 ? 33.898  19.301   26.069   1.00 84.95  ? 408 PHE   D O      1 
ATOM   13304 C  CB     . PHE   D 2  408 ? 35.121  20.610   28.845   1.00 80.17  ? 408 PHE   D CB     1 
ATOM   13305 C  CG     . PHE   D 2  408 ? 34.751  20.354   30.276   1.00 74.82  ? 408 PHE   D CG     1 
ATOM   13306 C  CD1    . PHE   D 2  408 ? 35.691  19.881   31.172   1.00 75.58  ? 408 PHE   D CD1    1 
ATOM   13307 C  CD2    . PHE   D 2  408 ? 33.468  20.601   30.724   1.00 71.08  ? 408 PHE   D CD2    1 
ATOM   13308 C  CE1    . PHE   D 2  408 ? 35.360  19.641   32.484   1.00 75.77  ? 408 PHE   D CE1    1 
ATOM   13309 C  CE2    . PHE   D 2  408 ? 33.130  20.366   32.035   1.00 76.46  ? 408 PHE   D CE2    1 
ATOM   13310 C  CZ     . PHE   D 2  408 ? 34.079  19.880   32.918   1.00 78.79  ? 408 PHE   D CZ     1 
ATOM   13311 N  N      . THR   D 2  409 ? 35.939  20.232   25.823   1.00 81.79  ? 409 THR   D N      1 
ATOM   13312 C  CA     . THR   D 2  409 ? 35.774  20.449   24.389   1.00 82.02  ? 409 THR   D CA     1 
ATOM   13313 C  C      . THR   D 2  409 ? 35.486  19.138   23.663   1.00 84.36  ? 409 THR   D C      1 
ATOM   13314 O  O      . THR   D 2  409 ? 34.591  19.067   22.811   1.00 81.46  ? 409 THR   D O      1 
ATOM   13315 C  CB     . THR   D 2  409 ? 37.034  21.102   23.813   1.00 80.54  ? 409 THR   D CB     1 
ATOM   13316 O  OG1    . THR   D 2  409 ? 37.137  22.448   24.284   1.00 85.77  ? 409 THR   D OG1    1 
ATOM   13317 C  CG2    . THR   D 2  409 ? 36.996  21.099   22.290   1.00 75.60  ? 409 THR   D CG2    1 
ATOM   13318 N  N      . GLU   D 2  410 ? 36.255  18.091   23.984   1.00 82.05  ? 410 GLU   D N      1 
ATOM   13319 C  CA     . GLU   D 2  410 ? 36.139  16.815   23.284   1.00 77.87  ? 410 GLU   D CA     1 
ATOM   13320 C  C      . GLU   D 2  410 ? 34.799  16.148   23.580   1.00 76.14  ? 410 GLU   D C      1 
ATOM   13321 O  O      . GLU   D 2  410 ? 34.025  15.851   22.664   1.00 72.63  ? 410 GLU   D O      1 
ATOM   13322 C  CB     . GLU   D 2  410 ? 37.312  15.904   23.663   1.00 75.40  ? 410 GLU   D CB     1 
ATOM   13323 C  CG     . GLU   D 2  410 ? 38.667  16.379   23.114   1.00 82.55  ? 410 GLU   D CG     1 
ATOM   13324 C  CD     . GLU   D 2  410 ? 39.858  15.651   23.738   1.00 89.05  ? 410 GLU   D CD     1 
ATOM   13325 O  OE1    . GLU   D 2  410 ? 39.638  14.725   24.553   1.00 87.99  ? 410 GLU   D OE1    1 
ATOM   13326 O  OE2    . GLU   D 2  410 ? 41.012  16.014   23.421   1.00 89.11  ? 410 GLU   D OE2    1 
ATOM   13327 N  N      . ALA   D 2  411 ? 34.499  15.912   24.860   1.00 73.24  ? 411 ALA   D N      1 
ATOM   13328 C  CA     . ALA   D 2  411 ? 33.179  15.400   25.209   1.00 70.99  ? 411 ALA   D CA     1 
ATOM   13329 C  C      . ALA   D 2  411 ? 32.070  16.194   24.529   1.00 74.70  ? 411 ALA   D C      1 
ATOM   13330 O  O      . ALA   D 2  411 ? 31.009  15.643   24.203   1.00 69.42  ? 411 ALA   D O      1 
ATOM   13331 C  CB     . ALA   D 2  411 ? 32.985  15.429   26.723   1.00 70.98  ? 411 ALA   D CB     1 
ATOM   13332 N  N      . GLU   D 2  412 ? 32.293  17.490   24.311   1.00 77.55  ? 412 GLU   D N      1 
ATOM   13333 C  CA     . GLU   D 2  412 ? 31.274  18.316   23.678   1.00 77.12  ? 412 GLU   D CA     1 
ATOM   13334 C  C      . GLU   D 2  412 ? 31.208  18.062   22.178   1.00 71.64  ? 412 GLU   D C      1 
ATOM   13335 O  O      . GLU   D 2  412 ? 30.124  17.862   21.628   1.00 70.16  ? 412 GLU   D O      1 
ATOM   13336 C  CB     . GLU   D 2  412 ? 31.542  19.792   23.957   1.00 78.45  ? 412 GLU   D CB     1 
ATOM   13337 C  CG     . GLU   D 2  412 ? 30.453  20.703   23.465   1.00 74.46  ? 412 GLU   D CG     1 
ATOM   13338 C  CD     . GLU   D 2  412 ? 30.895  22.135   23.423   1.00 82.02  ? 412 GLU   D CD     1 
ATOM   13339 O  OE1    . GLU   D 2  412 ? 31.938  22.416   22.783   1.00 78.93  ? 412 GLU   D OE1    1 
ATOM   13340 O  OE2    . GLU   D 2  412 ? 30.199  22.970   24.042   1.00 81.93  ? 412 GLU   D OE2    1 
ATOM   13341 N  N      . SER   D 2  413 ? 32.352  18.065   21.495   1.00 69.21  ? 413 SER   D N      1 
ATOM   13342 C  CA     . SER   D 2  413 ? 32.328  17.759   20.071   1.00 70.79  ? 413 SER   D CA     1 
ATOM   13343 C  C      . SER   D 2  413 ? 31.738  16.367   19.820   1.00 70.63  ? 413 SER   D C      1 
ATOM   13344 O  O      . SER   D 2  413 ? 30.935  16.186   18.897   1.00 67.91  ? 413 SER   D O      1 
ATOM   13345 C  CB     . SER   D 2  413 ? 33.738  17.894   19.489   1.00 68.25  ? 413 SER   D CB     1 
ATOM   13346 O  OG     . SER   D 2  413 ? 34.405  16.646   19.430   1.00 77.79  ? 413 SER   D OG     1 
ATOM   13347 N  N      . ASN   D 2  414 ? 32.095  15.383   20.660   1.00 70.81  ? 414 ASN   D N      1 
ATOM   13348 C  CA     . ASN   D 2  414 ? 31.574  14.023   20.515   1.00 64.70  ? 414 ASN   D CA     1 
ATOM   13349 C  C      . ASN   D 2  414 ? 30.049  13.989   20.605   1.00 65.72  ? 414 ASN   D C      1 
ATOM   13350 O  O      . ASN   D 2  414 ? 29.375  13.470   19.710   1.00 65.67  ? 414 ASN   D O      1 
ATOM   13351 C  CB     . ASN   D 2  414 ? 32.187  13.101   21.573   1.00 64.40  ? 414 ASN   D CB     1 
ATOM   13352 C  CG     . ASN   D 2  414 ? 31.945  11.614   21.277   1.00 64.60  ? 414 ASN   D CG     1 
ATOM   13353 O  OD1    . ASN   D 2  414 ? 31.467  11.259   20.207   1.00 65.05  ? 414 ASN   D OD1    1 
ATOM   13354 N  ND2    . ASN   D 2  414 ? 32.248  10.751   22.241   1.00 65.56  ? 414 ASN   D ND2    1 
ATOM   13355 N  N      . MET   D 2  415 ? 29.477  14.524   21.686   1.00 65.37  ? 415 MET   D N      1 
ATOM   13356 C  CA     . MET   D 2  415 ? 28.020  14.562   21.771   1.00 59.65  ? 415 MET   D CA     1 
ATOM   13357 C  C      . MET   D 2  415 ? 27.390  15.368   20.639   1.00 63.60  ? 415 MET   D C      1 
ATOM   13358 O  O      . MET   D 2  415 ? 26.229  15.130   20.287   1.00 60.24  ? 415 MET   D O      1 
ATOM   13359 C  CB     . MET   D 2  415 ? 27.566  15.146   23.093   1.00 59.10  ? 415 MET   D CB     1 
ATOM   13360 C  CG     . MET   D 2  415 ? 26.080  15.054   23.243   1.00 62.56  ? 415 MET   D CG     1 
ATOM   13361 S  SD     . MET   D 2  415 ? 25.465  15.769   24.785   1.00 70.54  ? 415 MET   D SD     1 
ATOM   13362 C  CE     . MET   D 2  415 ? 25.374  14.327   25.840   1.00 60.97  ? 415 MET   D CE     1 
ATOM   13363 N  N      . ASN   D 2  416 ? 28.111  16.347   20.078   1.00 65.73  ? 416 ASN   D N      1 
ATOM   13364 C  CA     . ASN   D 2  416 ? 27.569  17.073   18.931   1.00 62.69  ? 416 ASN   D CA     1 
ATOM   13365 C  C      . ASN   D 2  416 ? 27.533  16.179   17.704   1.00 65.15  ? 416 ASN   D C      1 
ATOM   13366 O  O      . ASN   D 2  416 ? 26.554  16.196   16.950   1.00 63.33  ? 416 ASN   D O      1 
ATOM   13367 C  CB     . ASN   D 2  416 ? 28.380  18.341   18.640   1.00 63.76  ? 416 ASN   D CB     1 
ATOM   13368 C  CG     . ASN   D 2  416 ? 28.004  19.518   19.554   1.00 71.25  ? 416 ASN   D CG     1 
ATOM   13369 O  OD1    . ASN   D 2  416 ? 26.932  19.538   20.184   1.00 70.62  ? 416 ASN   D OD1    1 
ATOM   13370 N  ND2    . ASN   D 2  416 ? 28.893  20.507   19.626   1.00 72.34  ? 416 ASN   D ND2    1 
ATOM   13371 N  N      . ASP   D 2  417 ? 28.594  15.389   17.497   1.00 63.62  ? 417 ASP   D N      1 
ATOM   13372 C  CA     . ASP   D 2  417 ? 28.614  14.412   16.414   1.00 59.67  ? 417 ASP   D CA     1 
ATOM   13373 C  C      . ASP   D 2  417 ? 27.466  13.408   16.542   1.00 56.98  ? 417 ASP   D C      1 
ATOM   13374 O  O      . ASP   D 2  417 ? 26.801  13.079   15.556   1.00 54.30  ? 417 ASP   D O      1 
ATOM   13375 C  CB     . ASP   D 2  417 ? 29.965  13.698   16.407   1.00 59.09  ? 417 ASP   D CB     1 
ATOM   13376 C  CG     . ASP   D 2  417 ? 31.124  14.643   16.130   1.00 67.66  ? 417 ASP   D CG     1 
ATOM   13377 O  OD1    . ASP   D 2  417 ? 30.871  15.788   15.702   1.00 69.64  ? 417 ASP   D OD1    1 
ATOM   13378 O  OD2    . ASP   D 2  417 ? 32.293  14.247   16.341   1.00 72.40  ? 417 ASP   D OD2    1 
ATOM   13379 N  N      . LEU   D 2  418 ? 27.208  12.923   17.756   1.00 61.10  ? 418 LEU   D N      1 
ATOM   13380 C  CA     . LEU   D 2  418 ? 26.153  11.937   17.962   1.00 56.63  ? 418 LEU   D CA     1 
ATOM   13381 C  C      . LEU   D 2  418 ? 24.797  12.459   17.488   1.00 61.13  ? 418 LEU   D C      1 
ATOM   13382 O  O      . LEU   D 2  418 ? 24.020  11.727   16.861   1.00 63.47  ? 418 LEU   D O      1 
ATOM   13383 C  CB     . LEU   D 2  418 ? 26.099  11.557   19.439   1.00 54.97  ? 418 LEU   D CB     1 
ATOM   13384 C  CG     . LEU   D 2  418 ? 25.014  10.540   19.761   1.00 56.21  ? 418 LEU   D CG     1 
ATOM   13385 C  CD1    . LEU   D 2  418 ? 25.418  9.243    19.125   1.00 58.33  ? 418 LEU   D CD1    1 
ATOM   13386 C  CD2    . LEU   D 2  418 ? 24.824  10.388   21.263   1.00 52.05  ? 418 LEU   D CD2    1 
ATOM   13387 N  N      . VAL   D 2  419 ? 24.480  13.717   17.797   1.00 60.34  ? 419 VAL   D N      1 
ATOM   13388 C  CA     . VAL   D 2  419 ? 23.259  14.305   17.260   1.00 60.19  ? 419 VAL   D CA     1 
ATOM   13389 C  C      . VAL   D 2  419 ? 23.373  14.450   15.744   1.00 57.19  ? 419 VAL   D C      1 
ATOM   13390 O  O      . VAL   D 2  419 ? 22.414  14.196   15.006   1.00 60.27  ? 419 VAL   D O      1 
ATOM   13391 C  CB     . VAL   D 2  419 ? 22.955  15.650   17.956   1.00 52.22  ? 419 VAL   D CB     1 
ATOM   13392 C  CG1    . VAL   D 2  419 ? 21.772  16.356   17.297   1.00 55.05  ? 419 VAL   D CG1    1 
ATOM   13393 C  CG2    . VAL   D 2  419 ? 22.649  15.419   19.417   1.00 54.36  ? 419 VAL   D CG2    1 
ATOM   13394 N  N      . SER   D 2  420 ? 24.544  14.858   15.256   1.00 52.75  ? 420 SER   D N      1 
ATOM   13395 C  CA     . SER   D 2  420 ? 24.735  15.004   13.819   1.00 52.88  ? 420 SER   D CA     1 
ATOM   13396 C  C      . SER   D 2  420 ? 24.506  13.688   13.089   1.00 59.78  ? 420 SER   D C      1 
ATOM   13397 O  O      . SER   D 2  420 ? 24.038  13.679   11.941   1.00 54.05  ? 420 SER   D O      1 
ATOM   13398 C  CB     . SER   D 2  420 ? 26.139  15.523   13.527   1.00 52.71  ? 420 SER   D CB     1 
ATOM   13399 O  OG     . SER   D 2  420 ? 26.150  16.221   12.296   1.00 70.06  ? 420 SER   D OG     1 
ATOM   13400 N  N      . GLU   D 2  421 ? 24.838  12.568   13.736   1.00 58.66  ? 421 GLU   D N      1 
ATOM   13401 C  CA     . GLU   D 2  421 ? 24.677  11.272   13.101   1.00 54.73  ? 421 GLU   D CA     1 
ATOM   13402 C  C      . GLU   D 2  421 ? 23.232  10.800   13.172   1.00 54.35  ? 421 GLU   D C      1 
ATOM   13403 O  O      . GLU   D 2  421 ? 22.730  10.210   12.210   1.00 51.54  ? 421 GLU   D O      1 
ATOM   13404 C  CB     . GLU   D 2  421 ? 25.650  10.273   13.725   1.00 51.07  ? 421 GLU   D CB     1 
ATOM   13405 C  CG     . GLU   D 2  421 ? 27.067  10.547   13.243   1.00 55.49  ? 421 GLU   D CG     1 
ATOM   13406 C  CD     . GLU   D 2  421 ? 28.159  10.273   14.278   1.00 60.50  ? 421 GLU   D CD     1 
ATOM   13407 O  OE1    . GLU   D 2  421 ? 27.952  9.418    15.178   1.00 58.73  ? 421 GLU   D OE1    1 
ATOM   13408 O  OE2    . GLU   D 2  421 ? 29.223  10.937   14.182   1.00 59.94  ? 421 GLU   D OE2    1 
ATOM   13409 N  N      . TYR   D 2  422 ? 22.532  11.076   14.276   1.00 53.78  ? 422 TYR   D N      1 
ATOM   13410 C  CA     . TYR   D 2  422 ? 21.095  10.828   14.286   1.00 52.43  ? 422 TYR   D CA     1 
ATOM   13411 C  C      . TYR   D 2  422 ? 20.419  11.571   13.138   1.00 55.10  ? 422 TYR   D C      1 
ATOM   13412 O  O      . TYR   D 2  422 ? 19.599  10.996   12.412   1.00 55.39  ? 422 TYR   D O      1 
ATOM   13413 C  CB     . TYR   D 2  422 ? 20.494  11.216   15.636   1.00 48.74  ? 422 TYR   D CB     1 
ATOM   13414 C  CG     . TYR   D 2  422 ? 20.556  10.102   16.675   1.00 58.38  ? 422 TYR   D CG     1 
ATOM   13415 C  CD1    . TYR   D 2  422 ? 19.852  8.907    16.493   1.00 50.55  ? 422 TYR   D CD1    1 
ATOM   13416 C  CD2    . TYR   D 2  422 ? 21.320  10.242   17.847   1.00 57.82  ? 422 TYR   D CD2    1 
ATOM   13417 C  CE1    . TYR   D 2  422 ? 19.900  7.879    17.450   1.00 50.18  ? 422 TYR   D CE1    1 
ATOM   13418 C  CE2    . TYR   D 2  422 ? 21.374  9.216    18.818   1.00 56.88  ? 422 TYR   D CE2    1 
ATOM   13419 C  CZ     . TYR   D 2  422 ? 20.663  8.033    18.613   1.00 58.83  ? 422 TYR   D CZ     1 
ATOM   13420 O  OH     . TYR   D 2  422 ? 20.705  7.006    19.553   1.00 51.99  ? 422 TYR   D OH     1 
ATOM   13421 N  N      . GLN   D 2  423 ? 20.785  12.836   12.919   1.00 52.18  ? 423 GLN   D N      1 
ATOM   13422 C  CA     . GLN   D 2  423 ? 20.179  13.577   11.819   1.00 54.67  ? 423 GLN   D CA     1 
ATOM   13423 C  C      . GLN   D 2  423 ? 20.514  12.948   10.468   1.00 54.31  ? 423 GLN   D C      1 
ATOM   13424 O  O      . GLN   D 2  423 ? 19.672  12.937   9.561    1.00 50.34  ? 423 GLN   D O      1 
ATOM   13425 C  CB     . GLN   D 2  423 ? 20.625  15.041   11.848   1.00 54.71  ? 423 GLN   D CB     1 
ATOM   13426 C  CG     . GLN   D 2  423 ? 19.870  15.934   10.864   1.00 46.81  ? 423 GLN   D CG     1 
ATOM   13427 C  CD     . GLN   D 2  423 ? 18.373  15.954   11.142   1.00 57.75  ? 423 GLN   D CD     1 
ATOM   13428 O  OE1    . GLN   D 2  423 ? 17.945  15.900   12.300   1.00 61.49  ? 423 GLN   D OE1    1 
ATOM   13429 N  NE2    . GLN   D 2  423 ? 17.570  16.031   10.085   1.00 50.82  ? 423 GLN   D NE2    1 
ATOM   13430 N  N      . GLN   D 2  424 ? 21.740  12.428   10.313   1.00 54.26  ? 424 GLN   D N      1 
ATOM   13431 C  CA     . GLN   D 2  424 ? 22.170  11.856   9.035    1.00 54.88  ? 424 GLN   D CA     1 
ATOM   13432 C  C      . GLN   D 2  424 ? 21.217  10.758   8.556    1.00 54.68  ? 424 GLN   D C      1 
ATOM   13433 O  O      . GLN   D 2  424 ? 20.833  10.729   7.378    1.00 56.47  ? 424 GLN   D O      1 
ATOM   13434 C  CB     . GLN   D 2  424 ? 23.602  11.328   9.163    1.00 52.09  ? 424 GLN   D CB     1 
ATOM   13435 C  CG     . GLN   D 2  424 ? 24.327  11.096   7.841    1.00 58.11  ? 424 GLN   D CG     1 
ATOM   13436 C  CD     . GLN   D 2  424 ? 25.126  9.791    7.815    1.00 66.10  ? 424 GLN   D CD     1 
ATOM   13437 O  OE1    . GLN   D 2  424 ? 25.812  9.453    8.788    1.00 68.64  ? 424 GLN   D OE1    1 
ATOM   13438 N  NE2    . GLN   D 2  424 ? 25.042  9.053    6.699    1.00 60.53  ? 424 GLN   D NE2    1 
ATOM   13439 N  N      . TYR   D 2  425 ? 20.799  9.874    9.467    1.00 47.42  ? 425 TYR   D N      1 
ATOM   13440 C  CA     . TYR   D 2  425 ? 19.921  8.758    9.150    1.00 50.73  ? 425 TYR   D CA     1 
ATOM   13441 C  C      . TYR   D 2  425 ? 18.447  9.107    9.258    1.00 55.00  ? 425 TYR   D C      1 
ATOM   13442 O  O      . TYR   D 2  425 ? 17.599  8.345    8.770    1.00 58.80  ? 425 TYR   D O      1 
ATOM   13443 C  CB     . TYR   D 2  425 ? 20.227  7.561    10.067   1.00 46.45  ? 425 TYR   D CB     1 
ATOM   13444 C  CG     . TYR   D 2  425 ? 21.626  7.031    9.876    1.00 44.92  ? 425 TYR   D CG     1 
ATOM   13445 C  CD1    . TYR   D 2  425 ? 22.077  6.664    8.619    1.00 48.41  ? 425 TYR   D CD1    1 
ATOM   13446 C  CD2    . TYR   D 2  425 ? 22.502  6.921    10.939   1.00 45.47  ? 425 TYR   D CD2    1 
ATOM   13447 C  CE1    . TYR   D 2  425 ? 23.346  6.192    8.431    1.00 52.34  ? 425 TYR   D CE1    1 
ATOM   13448 C  CE2    . TYR   D 2  425 ? 23.781  6.448    10.766   1.00 44.40  ? 425 TYR   D CE2    1 
ATOM   13449 C  CZ     . TYR   D 2  425 ? 24.202  6.086    9.509    1.00 52.71  ? 425 TYR   D CZ     1 
ATOM   13450 O  OH     . TYR   D 2  425 ? 25.477  5.610    9.317    1.00 48.41  ? 425 TYR   D OH     1 
ATOM   13451 N  N      . GLN   D 2  426 ? 18.111  10.218   9.902    1.00 54.46  ? 426 GLN   D N      1 
ATOM   13452 C  CA     . GLN   D 2  426 ? 16.741  10.697   9.808    1.00 56.11  ? 426 GLN   D CA     1 
ATOM   13453 C  C      . GLN   D 2  426 ? 16.462  11.235   8.408    1.00 55.14  ? 426 GLN   D C      1 
ATOM   13454 O  O      . GLN   D 2  426 ? 15.351  11.070   7.886    1.00 49.44  ? 426 GLN   D O      1 
ATOM   13455 C  CB     . GLN   D 2  426 ? 16.492  11.752   10.883   1.00 56.18  ? 426 GLN   D CB     1 
ATOM   13456 C  CG     . GLN   D 2  426 ? 15.058  12.204   10.997   1.00 59.96  ? 426 GLN   D CG     1 
ATOM   13457 C  CD     . GLN   D 2  426 ? 14.913  13.339   11.977   1.00 59.57  ? 426 GLN   D CD     1 
ATOM   13458 O  OE1    . GLN   D 2  426 ? 15.338  13.224   13.124   1.00 62.37  ? 426 GLN   D OE1    1 
ATOM   13459 N  NE2    . GLN   D 2  426 ? 14.310  14.439   11.542   1.00 55.29  ? 426 GLN   D NE2    1 
ATOM   13460 N  N      . ASP   D 2  427 ? 17.482  11.826   7.776    1.00 53.24  ? 427 ASP   D N      1 
ATOM   13461 C  CA     . ASP   D 2  427 ? 17.393  12.358   6.421    1.00 52.70  ? 427 ASP   D CA     1 
ATOM   13462 C  C      . ASP   D 2  427 ? 17.623  11.295   5.362    1.00 53.62  ? 427 ASP   D C      1 
ATOM   13463 O  O      . ASP   D 2  427 ? 17.300  11.529   4.192    1.00 53.75  ? 427 ASP   D O      1 
ATOM   13464 C  CB     . ASP   D 2  427 ? 18.431  13.467   6.213    1.00 55.53  ? 427 ASP   D CB     1 
ATOM   13465 C  CG     . ASP   D 2  427 ? 18.226  14.674   7.131    1.00 60.55  ? 427 ASP   D CG     1 
ATOM   13466 O  OD1    . ASP   D 2  427 ? 17.082  14.867   7.632    1.00 54.70  ? 427 ASP   D OD1    1 
ATOM   13467 O  OD2    . ASP   D 2  427 ? 19.233  15.413   7.354    1.00 54.68  ? 427 ASP   D OD2    1 
ATOM   13468 N  N      . ALA   D 2  428 ? 18.204  10.157   5.739    1.00 57.05  ? 428 ALA   D N      1 
ATOM   13469 C  CA     . ALA   D 2  428 ? 18.506  9.097    4.781    1.00 56.27  ? 428 ALA   D CA     1 
ATOM   13470 C  C      . ALA   D 2  428 ? 17.232  8.532    4.160    1.00 56.16  ? 428 ALA   D C      1 
ATOM   13471 O  O      . ALA   D 2  428 ? 16.230  8.310    4.851    1.00 51.10  ? 428 ALA   D O      1 
ATOM   13472 C  CB     . ALA   D 2  428 ? 19.285  7.970    5.467    1.00 48.19  ? 428 ALA   D CB     1 
ATOM   13473 N  N      . THR   D 2  429 ? 17.296  8.273    2.851    1.00 60.69  ? 429 THR   D N      1 
ATOM   13474 C  CA     . THR   D 2  429 ? 16.246  7.647    2.044    1.00 62.42  ? 429 THR   D CA     1 
ATOM   13475 C  C      . THR   D 2  429 ? 16.777  6.394    1.350    1.00 61.18  ? 429 THR   D C      1 
ATOM   13476 O  O      . THR   D 2  429 ? 17.987  6.158    1.263    1.00 55.50  ? 429 THR   D O      1 
ATOM   13477 C  CB     . THR   D 2  429 ? 15.714  8.605    0.972    1.00 59.41  ? 429 THR   D CB     1 
ATOM   13478 O  OG1    . THR   D 2  429 ? 16.556  8.513    -0.185   1.00 57.52  ? 429 THR   D OG1    1 
ATOM   13479 C  CG2    . THR   D 2  429 ? 15.712  10.037   1.469    1.00 64.12  ? 429 THR   D CG2    1 
ATOM   13480 N  N      . ALA   D 2  430 ? 15.851  5.604    0.805    1.00 65.99  ? 430 ALA   D N      1 
ATOM   13481 C  CA     . ALA   D 2  430 ? 16.238  4.398    0.076    1.00 62.59  ? 430 ALA   D CA     1 
ATOM   13482 C  C      . ALA   D 2  430 ? 16.654  4.700    -1.369   1.00 62.01  ? 430 ALA   D C      1 
ATOM   13483 O  O      . ALA   D 2  430 ? 17.741  4.303    -1.802   1.00 60.80  ? 430 ALA   D O      1 
ATOM   13484 C  CB     . ALA   D 2  430 ? 15.096  3.381    0.117    1.00 54.77  ? 430 ALA   D CB     1 
ATOM   13485 N  N      . ASP   D 2  431 ? 15.812  5.402    -2.129   1.00 71.88  ? 431 ASP   D N      1 
ATOM   13486 C  CA     . ASP   D 2  431 ? 16.059  5.600    -3.567   1.00 78.10  ? 431 ASP   D CA     1 
ATOM   13487 C  C      . ASP   D 2  431 ? 17.231  6.537    -3.841   1.00 71.39  ? 431 ASP   D C      1 
ATOM   13488 O  O      . ASP   D 2  431 ? 18.390  6.158    -3.664   1.00 68.99  ? 431 ASP   D O      1 
ATOM   13489 C  CB     . ASP   D 2  431 ? 14.797  6.133    -4.263   1.00 79.29  ? 431 ASP   D CB     1 
ATOM   13490 N  N      . MET   E 3  1   ? 20.264  -89.797  -93.726  1.00 75.56  ? 6   MET   E N      1 
ATOM   13491 C  CA     . MET   E 3  1   ? 20.471  -90.169  -92.321  1.00 83.97  ? 6   MET   E CA     1 
ATOM   13492 C  C      . MET   E 3  1   ? 21.311  -91.438  -92.211  1.00 85.76  ? 6   MET   E C      1 
ATOM   13493 O  O      . MET   E 3  1   ? 20.828  -92.523  -92.535  1.00 89.32  ? 6   MET   E O      1 
ATOM   13494 C  CB     . MET   E 3  1   ? 19.127  -90.374  -91.605  1.00 86.90  ? 6   MET   E CB     1 
ATOM   13495 C  CG     . MET   E 3  1   ? 19.224  -90.460  -90.073  1.00 86.27  ? 6   MET   E CG     1 
ATOM   13496 S  SD     . MET   E 3  1   ? 17.661  -90.243  -89.164  1.00 87.30  ? 6   MET   E SD     1 
ATOM   13497 C  CE     . MET   E 3  1   ? 17.133  -88.628  -89.721  1.00 66.17  ? 6   MET   E CE     1 
ATOM   13498 N  N      . GLU   E 3  2   ? 22.551  -91.302  -91.719  1.00 81.10  ? 7   GLU   E N      1 
ATOM   13499 C  CA     . GLU   E 3  2   ? 23.564  -92.361  -91.746  1.00 76.20  ? 7   GLU   E CA     1 
ATOM   13500 C  C      . GLU   E 3  2   ? 23.837  -92.882  -90.336  1.00 78.19  ? 7   GLU   E C      1 
ATOM   13501 O  O      . GLU   E 3  2   ? 24.358  -92.140  -89.496  1.00 80.11  ? 7   GLU   E O      1 
ATOM   13502 C  CB     . GLU   E 3  2   ? 24.856  -91.825  -92.365  1.00 77.03  ? 7   GLU   E CB     1 
ATOM   13503 C  CG     . GLU   E 3  2   ? 26.046  -92.801  -92.346  1.00 85.26  ? 7   GLU   E CG     1 
ATOM   13504 C  CD     . GLU   E 3  2   ? 27.290  -92.238  -93.042  1.00 88.38  ? 7   GLU   E CD     1 
ATOM   13505 O  OE1    . GLU   E 3  2   ? 27.516  -91.005  -92.958  1.00 89.03  ? 7   GLU   E OE1    1 
ATOM   13506 O  OE2    . GLU   E 3  2   ? 28.028  -93.027  -93.684  1.00 81.27  ? 7   GLU   E OE2    1 
ATOM   13507 N  N      . VAL   E 3  3   ? 23.510  -94.165  -90.075  1.00 75.21  ? 8   VAL   E N      1 
ATOM   13508 C  CA     . VAL   E 3  3   ? 23.972  -94.839  -88.859  1.00 70.88  ? 8   VAL   E CA     1 
ATOM   13509 C  C      . VAL   E 3  3   ? 25.433  -95.217  -89.053  1.00 71.02  ? 8   VAL   E C      1 
ATOM   13510 O  O      . VAL   E 3  3   ? 25.843  -95.522  -90.175  1.00 75.92  ? 8   VAL   E O      1 
ATOM   13511 C  CB     . VAL   E 3  3   ? 23.117  -96.076  -88.557  1.00 60.68  ? 8   VAL   E CB     1 
ATOM   13512 C  CG1    . VAL   E 3  3   ? 23.921  -97.060  -87.710  1.00 62.34  ? 8   VAL   E CG1    1 
ATOM   13513 C  CG2    . VAL   E 3  3   ? 21.815  -95.673  -87.893  1.00 53.42  ? 8   VAL   E CG2    1 
ATOM   13514 N  N      . ILE   E 3  4   ? 26.245  -95.180  -87.993  1.00 71.23  ? 9   ILE   E N      1 
ATOM   13515 C  CA     . ILE   E 3  4   ? 27.681  -95.215  -88.271  1.00 71.68  ? 9   ILE   E CA     1 
ATOM   13516 C  C      . ILE   E 3  4   ? 28.467  -96.218  -87.446  1.00 74.82  ? 9   ILE   E C      1 
ATOM   13517 O  O      . ILE   E 3  4   ? 29.416  -96.816  -87.964  1.00 90.69  ? 9   ILE   E O      1 
ATOM   13518 C  CB     . ILE   E 3  4   ? 28.339  -93.826  -88.136  1.00 72.12  ? 9   ILE   E CB     1 
ATOM   13519 C  CG1    . ILE   E 3  4   ? 29.228  -93.774  -86.883  1.00 72.72  ? 9   ILE   E CG1    1 
ATOM   13520 C  CG2    . ILE   E 3  4   ? 27.314  -92.705  -88.185  1.00 71.11  ? 9   ILE   E CG2    1 
ATOM   13521 C  CD1    . ILE   E 3  4   ? 30.265  -92.664  -86.917  1.00 73.25  ? 9   ILE   E CD1    1 
ATOM   13522 N  N      . GLU   E 3  5   ? 28.156  -96.410  -86.170  1.00 66.78  ? 10  GLU   E N      1 
ATOM   13523 C  CA     . GLU   E 3  5   ? 29.029  -97.304  -85.405  1.00 70.42  ? 10  GLU   E CA     1 
ATOM   13524 C  C      . GLU   E 3  5   ? 28.247  -98.156  -84.417  1.00 66.38  ? 10  GLU   E C      1 
ATOM   13525 O  O      . GLU   E 3  5   ? 28.513  -98.165  -83.218  1.00 65.71  ? 10  GLU   E O      1 
ATOM   13526 C  CB     . GLU   E 3  5   ? 30.148  -96.539  -84.704  1.00 73.56  ? 10  GLU   E CB     1 
ATOM   13527 C  CG     . GLU   E 3  5   ? 31.394  -96.463  -85.572  1.00 82.17  ? 10  GLU   E CG     1 
ATOM   13528 C  CD     . GLU   E 3  5   ? 32.611  -95.900  -84.854  1.00 89.32  ? 10  GLU   E CD     1 
ATOM   13529 O  OE1    . GLU   E 3  5   ? 33.239  -96.674  -84.085  1.00 90.36  ? 10  GLU   E OE1    1 
ATOM   13530 O  OE2    . GLU   E 3  5   ? 32.955  -94.712  -85.090  1.00 77.41  ? 10  GLU   E OE2    1 
ATOM   13531 N  N      . LEU   E 3  6   ? 27.301  -98.929  -84.953  1.00 64.79  ? 11  LEU   E N      1 
ATOM   13532 C  CA     . LEU   E 3  6   ? 26.521  -99.836  -84.126  1.00 60.65  ? 11  LEU   E CA     1 
ATOM   13533 C  C      . LEU   E 3  6   ? 27.432  -100.794 -83.360  1.00 59.90  ? 11  LEU   E C      1 
ATOM   13534 O  O      . LEU   E 3  6   ? 28.046  -101.683 -83.959  1.00 58.72  ? 11  LEU   E O      1 
ATOM   13535 C  CB     . LEU   E 3  6   ? 25.513  -100.603 -84.983  1.00 53.13  ? 11  LEU   E CB     1 
ATOM   13536 C  CG     . LEU   E 3  6   ? 24.370  -101.214 -84.165  1.00 62.23  ? 11  LEU   E CG     1 
ATOM   13537 C  CD1    . LEU   E 3  6   ? 24.035  -100.335 -82.968  1.00 58.48  ? 11  LEU   E CD1    1 
ATOM   13538 C  CD2    . LEU   E 3  6   ? 23.117  -101.466 -84.996  1.00 65.75  ? 11  LEU   E CD2    1 
ATOM   13539 N  N      . ASN   E 3  7   ? 27.566  -100.587 -82.048  1.00 59.13  ? 12  ASN   E N      1 
ATOM   13540 C  CA     . ASN   E 3  7   ? 28.159  -101.560 -81.141  1.00 57.78  ? 12  ASN   E CA     1 
ATOM   13541 C  C      . ASN   E 3  7   ? 27.057  -102.139 -80.259  1.00 55.19  ? 12  ASN   E C      1 
ATOM   13542 O  O      . ASN   E 3  7   ? 26.289  -101.390 -79.655  1.00 54.06  ? 12  ASN   E O      1 
ATOM   13543 C  CB     . ASN   E 3  7   ? 29.245  -100.936 -80.263  1.00 60.50  ? 12  ASN   E CB     1 
ATOM   13544 C  CG     . ASN   E 3  7   ? 29.895  -101.975 -79.329  1.00 69.32  ? 12  ASN   E CG     1 
ATOM   13545 O  OD1    . ASN   E 3  7   ? 29.468  -102.173 -78.187  1.00 74.62  ? 12  ASN   E OD1    1 
ATOM   13546 N  ND2    . ASN   E 3  7   ? 30.942  -102.620 -79.811  1.00 67.64  ? 12  ASN   E ND2    1 
ATOM   13547 N  N      . LYS   E 3  8   ? 26.976  -103.465 -80.186  1.00 61.62  ? 13  LYS   E N      1 
ATOM   13548 C  CA     . LYS   E 3  8   ? 25.976  -104.147 -79.373  1.00 60.26  ? 13  LYS   E CA     1 
ATOM   13549 C  C      . LYS   E 3  8   ? 26.655  -104.919 -78.246  1.00 65.06  ? 13  LYS   E C      1 
ATOM   13550 O  O      . LYS   E 3  8   ? 27.877  -105.102 -78.216  1.00 65.18  ? 13  LYS   E O      1 
ATOM   13551 C  CB     . LYS   E 3  8   ? 25.116  -105.109 -80.218  1.00 54.37  ? 13  LYS   E CB     1 
ATOM   13552 C  CG     . LYS   E 3  8   ? 24.735  -104.520 -81.555  1.00 56.52  ? 13  LYS   E CG     1 
ATOM   13553 C  CD     . LYS   E 3  8   ? 23.987  -105.480 -82.468  1.00 53.09  ? 13  LYS   E CD     1 
ATOM   13554 C  CE     . LYS   E 3  8   ? 22.529  -105.595 -82.084  1.00 54.81  ? 13  LYS   E CE     1 
ATOM   13555 N  NZ     . LYS   E 3  8   ? 22.019  -106.997 -82.236  1.00 61.09  ? 13  LYS   E NZ     1 
ATOM   13556 N  N      . CYS   E 3  9   ? 25.837  -105.378 -77.317  1.00 61.12  ? 14  CYS   E N      1 
ATOM   13557 C  CA     . CYS   E 3  9   ? 26.277  -106.258 -76.250  1.00 62.87  ? 14  CYS   E CA     1 
ATOM   13558 C  C      . CYS   E 3  9   ? 25.011  -106.747 -75.579  1.00 64.44  ? 14  CYS   E C      1 
ATOM   13559 O  O      . CYS   E 3  9   ? 23.910  -106.527 -76.092  1.00 66.30  ? 14  CYS   E O      1 
ATOM   13560 C  CB     . CYS   E 3  9   ? 27.196  -105.549 -75.254  1.00 64.93  ? 14  CYS   E CB     1 
ATOM   13561 S  SG     . CYS   E 3  9   ? 26.308  -104.388 -74.217  1.00 64.04  ? 14  CYS   E SG     1 
ATOM   13562 N  N      . THR   E 3  10  ? 25.148  -107.377 -74.416  1.00 66.17  ? 15  THR   E N      1 
ATOM   13563 C  CA     . THR   E 3  10  ? 23.944  -107.903 -73.777  1.00 67.69  ? 15  THR   E CA     1 
ATOM   13564 C  C      . THR   E 3  10  ? 23.142  -106.811 -73.075  1.00 62.42  ? 15  THR   E C      1 
ATOM   13565 O  O      . THR   E 3  10  ? 21.912  -106.924 -72.982  1.00 57.67  ? 15  THR   E O      1 
ATOM   13566 C  CB     . THR   E 3  10  ? 24.308  -109.035 -72.804  1.00 63.62  ? 15  THR   E CB     1 
ATOM   13567 O  OG1    . THR   E 3  10  ? 24.476  -110.252 -73.541  1.00 73.10  ? 15  THR   E OG1    1 
ATOM   13568 C  CG2    . THR   E 3  10  ? 23.220  -109.244 -71.790  1.00 59.41  ? 15  THR   E CG2    1 
ATOM   13569 N  N      . SER   E 3  11  ? 23.820  -105.747 -72.609  1.00 67.41  ? 16  SER   E N      1 
ATOM   13570 C  CA     . SER   E 3  11  ? 23.211  -104.672 -71.820  1.00 64.57  ? 16  SER   E CA     1 
ATOM   13571 C  C      . SER   E 3  11  ? 22.376  -103.714 -72.664  1.00 67.54  ? 16  SER   E C      1 
ATOM   13572 O  O      . SER   E 3  11  ? 21.362  -103.187 -72.175  1.00 57.93  ? 16  SER   E O      1 
ATOM   13573 C  CB     . SER   E 3  11  ? 24.296  -103.870 -71.098  1.00 63.32  ? 16  SER   E CB     1 
ATOM   13574 O  OG     . SER   E 3  11  ? 24.322  -104.139 -69.710  1.00 66.89  ? 16  SER   E OG     1 
ATOM   13575 N  N      . GLY   E 3  12  ? 22.812  -103.454 -73.905  1.00 70.23  ? 17  GLY   E N      1 
ATOM   13576 C  CA     . GLY   E 3  12  ? 22.100  -102.628 -74.869  1.00 66.06  ? 17  GLY   E CA     1 
ATOM   13577 C  C      . GLY   E 3  12  ? 22.866  -102.487 -76.170  1.00 63.76  ? 17  GLY   E C      1 
ATOM   13578 O  O      . GLY   E 3  12  ? 23.504  -103.447 -76.616  1.00 63.79  ? 17  GLY   E O      1 
ATOM   13579 N  N      . GLN   E 3  13  ? 22.802  -101.299 -76.781  1.00 57.76  ? 18  GLN   E N      1 
ATOM   13580 C  CA     . GLN   E 3  13  ? 23.565  -100.964 -77.977  1.00 52.09  ? 18  GLN   E CA     1 
ATOM   13581 C  C      . GLN   E 3  13  ? 23.893  -99.476  -77.960  1.00 57.94  ? 18  GLN   E C      1 
ATOM   13582 O  O      . GLN   E 3  13  ? 23.378  -98.708  -77.142  1.00 59.32  ? 18  GLN   E O      1 
ATOM   13583 C  CB     . GLN   E 3  13  ? 22.807  -101.289 -79.264  1.00 54.66  ? 18  GLN   E CB     1 
ATOM   13584 C  CG     . GLN   E 3  13  ? 21.730  -102.361 -79.151  1.00 58.80  ? 18  GLN   E CG     1 
ATOM   13585 C  CD     . GLN   E 3  13  ? 20.905  -102.480 -80.424  1.00 58.00  ? 18  GLN   E CD     1 
ATOM   13586 O  OE1    . GLN   E 3  13  ? 21.294  -101.984 -81.481  1.00 66.56  ? 18  GLN   E OE1    1 
ATOM   13587 N  NE2    . GLN   E 3  13  ? 19.799  -103.186 -80.342  1.00 48.36  ? 18  GLN   E NE2    1 
ATOM   13588 N  N      . SER   E 3  14  ? 24.732  -99.072  -78.908  1.00 52.23  ? 19  SER   E N      1 
ATOM   13589 C  CA     . SER   E 3  14  ? 25.121  -97.680  -79.057  1.00 52.95  ? 19  SER   E CA     1 
ATOM   13590 C  C      . SER   E 3  14  ? 25.390  -97.412  -80.535  1.00 54.59  ? 19  SER   E C      1 
ATOM   13591 O  O      . SER   E 3  14  ? 25.577  -98.338  -81.324  1.00 53.08  ? 19  SER   E O      1 
ATOM   13592 C  CB     . SER   E 3  14  ? 26.343  -97.367  -78.191  1.00 55.21  ? 19  SER   E CB     1 
ATOM   13593 O  OG     . SER   E 3  14  ? 27.544  -97.509  -78.935  1.00 64.26  ? 19  SER   E OG     1 
ATOM   13594 N  N      . PHE   E 3  15  ? 25.389  -96.139  -80.916  1.00 52.21  ? 20  PHE   E N      1 
ATOM   13595 C  CA     . PHE   E 3  15  ? 25.612  -95.806  -82.319  1.00 52.52  ? 20  PHE   E CA     1 
ATOM   13596 C  C      . PHE   E 3  15  ? 25.462  -94.307  -82.517  1.00 52.04  ? 20  PHE   E C      1 
ATOM   13597 O  O      . PHE   E 3  15  ? 24.781  -93.625  -81.750  1.00 57.70  ? 20  PHE   E O      1 
ATOM   13598 C  CB     . PHE   E 3  15  ? 24.641  -96.537  -83.241  1.00 51.03  ? 20  PHE   E CB     1 
ATOM   13599 C  CG     . PHE   E 3  15  ? 23.224  -96.082  -83.102  1.00 53.24  ? 20  PHE   E CG     1 
ATOM   13600 C  CD1    . PHE   E 3  15  ? 22.379  -96.665  -82.156  1.00 54.07  ? 20  PHE   E CD1    1 
ATOM   13601 C  CD2    . PHE   E 3  15  ? 22.724  -95.070  -83.908  1.00 53.05  ? 20  PHE   E CD2    1 
ATOM   13602 C  CE1    . PHE   E 3  15  ? 21.058  -96.247  -82.010  1.00 45.49  ? 20  PHE   E CE1    1 
ATOM   13603 C  CE2    . PHE   E 3  15  ? 21.404  -94.647  -83.775  1.00 56.29  ? 20  PHE   E CE2    1 
ATOM   13604 C  CZ     . PHE   E 3  15  ? 20.572  -95.231  -82.824  1.00 51.75  ? 20  PHE   E CZ     1 
ATOM   13605 N  N      . GLU   E 3  16  ? 26.088  -93.808  -83.570  1.00 56.55  ? 21  GLU   E N      1 
ATOM   13606 C  CA     . GLU   E 3  16  ? 25.946  -92.423  -83.985  1.00 53.10  ? 21  GLU   E CA     1 
ATOM   13607 C  C      . GLU   E 3  16  ? 24.998  -92.343  -85.175  1.00 62.79  ? 21  GLU   E C      1 
ATOM   13608 O  O      . GLU   E 3  16  ? 24.681  -93.349  -85.808  1.00 68.18  ? 21  GLU   E O      1 
ATOM   13609 C  CB     . GLU   E 3  16  ? 27.309  -91.827  -84.328  1.00 54.73  ? 21  GLU   E CB     1 
ATOM   13610 C  CG     . GLU   E 3  16  ? 27.289  -90.342  -84.581  1.00 63.00  ? 21  GLU   E CG     1 
ATOM   13611 C  CD     . GLU   E 3  16  ? 28.676  -89.715  -84.498  1.00 68.09  ? 21  GLU   E CD     1 
ATOM   13612 O  OE1    . GLU   E 3  16  ? 29.631  -90.416  -84.082  1.00 65.02  ? 21  GLU   E OE1    1 
ATOM   13613 O  OE2    . GLU   E 3  16  ? 28.802  -88.514  -84.843  1.00 72.01  ? 21  GLU   E OE2    1 
ATOM   13614 N  N      . VAL   E 3  17  ? 24.515  -91.136  -85.455  1.00 63.81  ? 22  VAL   E N      1 
ATOM   13615 C  CA     . VAL   E 3  17  ? 23.572  -90.933  -86.548  1.00 66.16  ? 22  VAL   E CA     1 
ATOM   13616 C  C      . VAL   E 3  17  ? 23.770  -89.521  -87.082  1.00 68.65  ? 22  VAL   E C      1 
ATOM   13617 O  O      . VAL   E 3  17  ? 23.347  -88.542  -86.456  1.00 71.04  ? 22  VAL   E O      1 
ATOM   13618 C  CB     . VAL   E 3  17  ? 22.116  -91.176  -86.097  1.00 62.98  ? 22  VAL   E CB     1 
ATOM   13619 C  CG1    . VAL   E 3  17  ? 21.790  -90.344  -84.874  1.00 62.38  ? 22  VAL   E CG1    1 
ATOM   13620 C  CG2    . VAL   E 3  17  ? 21.143  -90.851  -87.211  1.00 67.61  ? 22  VAL   E CG2    1 
ATOM   13621 N  N      . ILE   E 3  18  ? 24.415  -89.410  -88.239  1.00 68.38  ? 23  ILE   E N      1 
ATOM   13622 C  CA     . ILE   E 3  18  ? 24.704  -88.121  -88.857  1.00 69.81  ? 23  ILE   E CA     1 
ATOM   13623 C  C      . ILE   E 3  18  ? 23.566  -87.758  -89.798  1.00 68.88  ? 23  ILE   E C      1 
ATOM   13624 O  O      . ILE   E 3  18  ? 23.312  -88.472  -90.769  1.00 78.32  ? 23  ILE   E O      1 
ATOM   13625 C  CB     . ILE   E 3  18  ? 26.036  -88.159  -89.611  1.00 70.76  ? 23  ILE   E CB     1 
ATOM   13626 C  CG1    . ILE   E 3  18  ? 27.097  -88.870  -88.766  1.00 72.09  ? 23  ILE   E CG1    1 
ATOM   13627 C  CG2    . ILE   E 3  18  ? 26.457  -86.755  -89.988  1.00 68.75  ? 23  ILE   E CG2    1 
ATOM   13628 C  CD1    . ILE   E 3  18  ? 27.013  -88.576  -87.273  1.00 72.22  ? 23  ILE   E CD1    1 
ATOM   13629 N  N      . LEU   E 3  19  ? 22.875  -86.655  -89.504  1.00 71.83  ? 24  LEU   E N      1 
ATOM   13630 C  CA     . LEU   E 3  19  ? 21.790  -86.168  -90.356  1.00 75.57  ? 24  LEU   E CA     1 
ATOM   13631 C  C      . LEU   E 3  19  ? 22.301  -85.288  -91.489  1.00 77.73  ? 24  LEU   E C      1 
ATOM   13632 O  O      . LEU   E 3  19  ? 21.609  -85.120  -92.499  1.00 86.15  ? 24  LEU   E O      1 
ATOM   13633 C  CB     . LEU   E 3  19  ? 20.778  -85.368  -89.533  1.00 70.63  ? 24  LEU   E CB     1 
ATOM   13634 C  CG     . LEU   E 3  19  ? 19.804  -86.131  -88.640  1.00 76.80  ? 24  LEU   E CG     1 
ATOM   13635 C  CD1    . LEU   E 3  19  ? 20.526  -86.655  -87.400  1.00 74.15  ? 24  LEU   E CD1    1 
ATOM   13636 C  CD2    . LEU   E 3  19  ? 18.603  -85.257  -88.267  1.00 65.54  ? 24  LEU   E CD2    1 
ATOM   13637 N  N      . LYS   E 3  20  ? 23.490  -84.717  -91.332  1.00 70.12  ? 25  LYS   E N      1 
ATOM   13638 C  CA     . LYS   E 3  20  ? 24.069  -83.714  -92.215  1.00 72.58  ? 25  LYS   E CA     1 
ATOM   13639 C  C      . LYS   E 3  20  ? 25.518  -83.500  -91.790  1.00 77.76  ? 25  LYS   E C      1 
ATOM   13640 O  O      . LYS   E 3  20  ? 25.814  -83.496  -90.585  1.00 77.62  ? 25  LYS   E O      1 
ATOM   13641 C  CB     . LYS   E 3  20  ? 23.311  -82.381  -92.132  1.00 74.59  ? 25  LYS   E CB     1 
ATOM   13642 C  CG     . LYS   E 3  20  ? 21.904  -82.346  -92.745  1.00 84.30  ? 25  LYS   E CG     1 
ATOM   13643 C  CD     . LYS   E 3  20  ? 20.878  -81.724  -91.771  1.00 83.01  ? 25  LYS   E CD     1 
ATOM   13644 C  CE     . LYS   E 3  20  ? 19.465  -81.629  -92.362  1.00 75.60  ? 25  LYS   E CE     1 
ATOM   13645 N  NZ     . LYS   E 3  20  ? 18.514  -82.616  -91.772  1.00 74.55  ? 25  LYS   E NZ     1 
ATOM   13646 N  N      . PRO   E 3  21  ? 26.443  -83.318  -92.729  1.00 86.40  ? 26  PRO   E N      1 
ATOM   13647 C  CA     . PRO   E 3  21  ? 27.829  -83.077  -92.352  1.00 82.59  ? 26  PRO   E CA     1 
ATOM   13648 C  C      . PRO   E 3  21  ? 28.064  -81.613  -92.035  1.00 78.92  ? 26  PRO   E C      1 
ATOM   13649 O  O      . PRO   E 3  21  ? 27.173  -80.783  -92.242  1.00 77.58  ? 26  PRO   E O      1 
ATOM   13650 C  CB     . PRO   E 3  21  ? 28.612  -83.523  -93.603  1.00 75.79  ? 26  PRO   E CB     1 
ATOM   13651 C  CG     . PRO   E 3  21  ? 27.536  -83.727  -94.722  1.00 80.05  ? 26  PRO   E CG     1 
ATOM   13652 C  CD     . PRO   E 3  21  ? 26.256  -83.129  -94.183  1.00 83.97  ? 26  PRO   E CD     1 
ATOM   13653 N  N      . PRO   E 3  22  ? 29.231  -81.266  -91.493  1.00 77.48  ? 27  PRO   E N      1 
ATOM   13654 C  CA     . PRO   E 3  22  ? 29.542  -79.854  -91.229  1.00 83.87  ? 27  PRO   E CA     1 
ATOM   13655 C  C      . PRO   E 3  22  ? 29.380  -79.001  -92.487  1.00 84.88  ? 27  PRO   E C      1 
ATOM   13656 O  O      . PRO   E 3  22  ? 29.218  -79.509  -93.600  1.00 82.03  ? 27  PRO   E O      1 
ATOM   13657 C  CB     . PRO   E 3  22  ? 31.005  -79.901  -90.756  1.00 82.51  ? 27  PRO   E CB     1 
ATOM   13658 C  CG     . PRO   E 3  22  ? 31.170  -81.288  -90.169  1.00 76.38  ? 27  PRO   E CG     1 
ATOM   13659 C  CD     . PRO   E 3  22  ? 30.300  -82.176  -91.040  1.00 77.61  ? 27  PRO   E CD     1 
ATOM   13660 N  N      . SER   E 3  23  ? 29.391  -77.679  -92.286  1.00 87.86  ? 28  SER   E N      1 
ATOM   13661 C  CA     . SER   E 3  23  ? 29.428  -76.694  -93.379  1.00 80.95  ? 28  SER   E CA     1 
ATOM   13662 C  C      . SER   E 3  23  ? 30.696  -75.832  -93.307  1.00 79.44  ? 28  SER   E C      1 
ATOM   13663 O  O      . SER   E 3  23  ? 31.810  -76.345  -93.137  1.00 81.47  ? 28  SER   E O      1 
ATOM   13664 C  CB     . SER   E 3  23  ? 28.191  -75.785  -93.360  1.00 73.71  ? 28  SER   E CB     1 
ATOM   13665 O  OG     . SER   E 3  23  ? 26.986  -76.528  -93.375  1.00 79.07  ? 28  SER   E OG     1 
ATOM   13666 N  N      . ASP   E 3  39  ? 47.382  -74.137  -65.528  1.00 89.11  ? 44  ASP   E N      1 
ATOM   13667 C  CA     . ASP   E 3  39  ? 46.832  -74.232  -64.172  1.00 92.42  ? 44  ASP   E CA     1 
ATOM   13668 C  C      . ASP   E 3  39  ? 47.879  -73.755  -63.158  1.00 90.85  ? 44  ASP   E C      1 
ATOM   13669 O  O      . ASP   E 3  39  ? 49.075  -73.931  -63.385  1.00 92.76  ? 44  ASP   E O      1 
ATOM   13670 C  CB     . ASP   E 3  39  ? 46.381  -75.672  -63.851  1.00 86.45  ? 44  ASP   E CB     1 
ATOM   13671 C  CG     . ASP   E 3  39  ? 45.264  -76.169  -64.779  1.00 84.79  ? 44  ASP   E CG     1 
ATOM   13672 O  OD1    . ASP   E 3  39  ? 44.554  -75.331  -65.384  1.00 76.68  ? 44  ASP   E OD1    1 
ATOM   13673 O  OD2    . ASP   E 3  39  ? 45.094  -77.405  -64.897  1.00 84.78  ? 44  ASP   E OD2    1 
ATOM   13674 N  N      . PRO   E 3  40  ? 47.436  -73.143  -62.058  1.00 90.27  ? 45  PRO   E N      1 
ATOM   13675 C  CA     . PRO   E 3  40  ? 48.379  -72.642  -61.046  1.00 86.07  ? 45  PRO   E CA     1 
ATOM   13676 C  C      . PRO   E 3  40  ? 48.970  -73.760  -60.187  1.00 83.60  ? 45  PRO   E C      1 
ATOM   13677 O  O      . PRO   E 3  40  ? 48.519  -74.909  -60.186  1.00 84.77  ? 45  PRO   E O      1 
ATOM   13678 C  CB     . PRO   E 3  40  ? 47.544  -71.677  -60.188  1.00 77.27  ? 45  PRO   E CB     1 
ATOM   13679 C  CG     . PRO   E 3  40  ? 46.152  -71.745  -60.690  1.00 79.88  ? 45  PRO   E CG     1 
ATOM   13680 C  CD     . PRO   E 3  40  ? 46.049  -72.701  -61.831  1.00 77.94  ? 45  PRO   E CD     1 
ATOM   13681 N  N      . SER   E 3  41  ? 49.993  -73.378  -59.424  1.00 78.93  ? 46  SER   E N      1 
ATOM   13682 C  CA     . SER   E 3  41  ? 50.826  -74.266  -58.624  1.00 72.62  ? 46  SER   E CA     1 
ATOM   13683 C  C      . SER   E 3  41  ? 50.359  -74.351  -57.172  1.00 73.47  ? 46  SER   E C      1 
ATOM   13684 O  O      . SER   E 3  41  ? 49.630  -73.489  -56.677  1.00 76.06  ? 46  SER   E O      1 
ATOM   13685 C  CB     . SER   E 3  41  ? 52.266  -73.772  -58.654  1.00 73.91  ? 46  SER   E CB     1 
ATOM   13686 O  OG     . SER   E 3  41  ? 52.862  -73.922  -57.381  1.00 81.25  ? 46  SER   E OG     1 
ATOM   13687 N  N      . LEU   E 3  42  ? 50.828  -75.392  -56.470  1.00 70.88  ? 47  LEU   E N      1 
ATOM   13688 C  CA     . LEU   E 3  42  ? 50.533  -75.499  -55.040  1.00 70.14  ? 47  LEU   E CA     1 
ATOM   13689 C  C      . LEU   E 3  42  ? 51.053  -74.284  -54.279  1.00 77.39  ? 47  LEU   E C      1 
ATOM   13690 O  O      . LEU   E 3  42  ? 50.379  -73.769  -53.377  1.00 80.51  ? 47  LEU   E O      1 
ATOM   13691 C  CB     . LEU   E 3  42  ? 51.129  -76.779  -54.451  1.00 65.73  ? 47  LEU   E CB     1 
ATOM   13692 C  CG     . LEU   E 3  42  ? 51.025  -76.916  -52.922  1.00 70.42  ? 47  LEU   E CG     1 
ATOM   13693 C  CD1    . LEU   E 3  42  ? 49.719  -76.305  -52.355  1.00 69.07  ? 47  LEU   E CD1    1 
ATOM   13694 C  CD2    . LEU   E 3  42  ? 51.174  -78.371  -52.473  1.00 60.61  ? 47  LEU   E CD2    1 
ATOM   13695 N  N      . GLU   E 3  43  ? 52.258  -73.819  -54.615  1.00 77.39  ? 48  GLU   E N      1 
ATOM   13696 C  CA     . GLU   E 3  43  ? 52.794  -72.631  -53.960  1.00 78.44  ? 48  GLU   E CA     1 
ATOM   13697 C  C      . GLU   E 3  43  ? 51.899  -71.423  -54.211  1.00 77.91  ? 48  GLU   E C      1 
ATOM   13698 O  O      . GLU   E 3  43  ? 51.503  -70.725  -53.268  1.00 79.56  ? 48  GLU   E O      1 
ATOM   13699 C  CB     . GLU   E 3  43  ? 54.218  -72.338  -54.440  1.00 77.24  ? 48  GLU   E CB     1 
ATOM   13700 C  CG     . GLU   E 3  43  ? 54.489  -70.841  -54.550  1.00 85.99  ? 48  GLU   E CG     1 
ATOM   13701 C  CD     . GLU   E 3  43  ? 55.665  -70.485  -55.433  1.00 92.08  ? 48  GLU   E CD     1 
ATOM   13702 O  OE1    . GLU   E 3  43  ? 56.825  -70.571  -54.957  1.00 88.48  ? 48  GLU   E OE1    1 
ATOM   13703 O  OE2    . GLU   E 3  43  ? 55.419  -70.105  -56.603  1.00 91.19  ? 48  GLU   E OE2    1 
ATOM   13704 N  N      . GLU   E 3  44  ? 51.575  -71.154  -55.482  1.00 75.07  ? 49  GLU   E N      1 
ATOM   13705 C  CA     . GLU   E 3  44  ? 50.733  -70.003  -55.798  1.00 73.99  ? 49  GLU   E CA     1 
ATOM   13706 C  C      . GLU   E 3  44  ? 49.391  -70.084  -55.074  1.00 76.25  ? 49  GLU   E C      1 
ATOM   13707 O  O      . GLU   E 3  44  ? 48.840  -69.054  -54.659  1.00 69.17  ? 49  GLU   E O      1 
ATOM   13708 C  CB     . GLU   E 3  44  ? 50.517  -69.908  -57.303  1.00 70.01  ? 49  GLU   E CB     1 
ATOM   13709 C  CG     . GLU   E 3  44  ? 51.756  -70.147  -58.120  1.00 76.95  ? 49  GLU   E CG     1 
ATOM   13710 C  CD     . GLU   E 3  44  ? 51.485  -70.035  -59.607  1.00 83.86  ? 49  GLU   E CD     1 
ATOM   13711 O  OE1    . GLU   E 3  44  ? 51.055  -68.943  -60.054  1.00 85.51  ? 49  GLU   E OE1    1 
ATOM   13712 O  OE2    . GLU   E 3  44  ? 51.675  -71.051  -60.320  1.00 80.16  ? 49  GLU   E OE2    1 
ATOM   13713 N  N      . ILE   E 3  45  ? 48.846  -71.302  -54.919  1.00 73.36  ? 50  ILE   E N      1 
ATOM   13714 C  CA     . ILE   E 3  45  ? 47.635  -71.494  -54.117  1.00 68.13  ? 50  ILE   E CA     1 
ATOM   13715 C  C      . ILE   E 3  45  ? 47.884  -71.054  -52.679  1.00 71.31  ? 50  ILE   E C      1 
ATOM   13716 O  O      . ILE   E 3  45  ? 47.174  -70.196  -52.140  1.00 69.57  ? 50  ILE   E O      1 
ATOM   13717 C  CB     . ILE   E 3  45  ? 47.151  -72.956  -54.188  1.00 68.14  ? 50  ILE   E CB     1 
ATOM   13718 C  CG1    . ILE   E 3  45  ? 46.578  -73.256  -55.572  1.00 68.66  ? 50  ILE   E CG1    1 
ATOM   13719 C  CG2    . ILE   E 3  45  ? 46.131  -73.269  -53.099  1.00 66.50  ? 50  ILE   E CG2    1 
ATOM   13720 C  CD1    . ILE   E 3  45  ? 45.966  -72.037  -56.239  1.00 71.75  ? 50  ILE   E CD1    1 
ATOM   13721 N  N      . GLN   E 3  46  ? 48.915  -71.620  -52.044  1.00 74.64  ? 51  GLN   E N      1 
ATOM   13722 C  CA     . GLN   E 3  46  ? 49.192  -71.275  -50.653  1.00 74.14  ? 51  GLN   E CA     1 
ATOM   13723 C  C      . GLN   E 3  46  ? 49.572  -69.804  -50.495  1.00 73.70  ? 51  GLN   E C      1 
ATOM   13724 O  O      . GLN   E 3  46  ? 49.264  -69.191  -49.463  1.00 64.69  ? 51  GLN   E O      1 
ATOM   13725 C  CB     . GLN   E 3  46  ? 50.278  -72.187  -50.110  1.00 68.54  ? 51  GLN   E CB     1 
ATOM   13726 C  CG     . GLN   E 3  46  ? 49.774  -73.568  -49.849  1.00 73.37  ? 51  GLN   E CG     1 
ATOM   13727 C  CD     . GLN   E 3  46  ? 50.761  -74.382  -49.058  1.00 84.75  ? 51  GLN   E CD     1 
ATOM   13728 O  OE1    . GLN   E 3  46  ? 50.416  -74.999  -48.048  1.00 82.79  ? 51  GLN   E OE1    1 
ATOM   13729 N  NE2    . GLN   E 3  46  ? 52.015  -74.382  -49.509  1.00 88.09  ? 51  GLN   E NE2    1 
ATOM   13730 N  N      . LYS   E 3  47  ? 50.211  -69.209  -51.505  1.00 70.20  ? 52  LYS   E N      1 
ATOM   13731 C  CA     . LYS   E 3  47  ? 50.516  -67.784  -51.430  1.00 75.19  ? 52  LYS   E CA     1 
ATOM   13732 C  C      . LYS   E 3  47  ? 49.233  -66.950  -51.354  1.00 75.02  ? 52  LYS   E C      1 
ATOM   13733 O  O      . LYS   E 3  47  ? 48.940  -66.375  -50.301  1.00 75.90  ? 52  LYS   E O      1 
ATOM   13734 C  CB     . LYS   E 3  47  ? 51.389  -67.348  -52.608  1.00 70.65  ? 52  LYS   E CB     1 
ATOM   13735 C  CG     . LYS   E 3  47  ? 52.307  -66.174  -52.277  1.00 77.53  ? 52  LYS   E CG     1 
ATOM   13736 C  CD     . LYS   E 3  47  ? 52.194  -65.052  -53.309  1.00 74.07  ? 52  LYS   E CD     1 
ATOM   13737 C  CE     . LYS   E 3  47  ? 53.206  -65.262  -54.428  1.00 80.00  ? 52  LYS   E CE     1 
ATOM   13738 N  NZ     . LYS   E 3  47  ? 53.099  -64.235  -55.497  1.00 78.70  ? 52  LYS   E NZ     1 
ATOM   13739 N  N      . LYS   E 3  48  ? 48.452  -66.887  -52.443  1.00 75.75  ? 53  LYS   E N      1 
ATOM   13740 C  CA     . LYS   E 3  48  ? 47.176  -66.159  -52.437  1.00 73.60  ? 53  LYS   E CA     1 
ATOM   13741 C  C      . LYS   E 3  48  ? 46.307  -66.494  -51.218  1.00 69.96  ? 53  LYS   E C      1 
ATOM   13742 O  O      . LYS   E 3  48  ? 45.687  -65.600  -50.632  1.00 64.49  ? 53  LYS   E O      1 
ATOM   13743 C  CB     . LYS   E 3  48  ? 46.408  -66.461  -53.725  1.00 63.50  ? 53  LYS   E CB     1 
ATOM   13744 C  CG     . LYS   E 3  48  ? 45.702  -67.822  -53.706  1.00 65.47  ? 53  LYS   E CG     1 
ATOM   13745 C  CD     . LYS   E 3  48  ? 44.171  -67.723  -53.730  1.00 67.07  ? 53  LYS   E CD     1 
ATOM   13746 C  CE     . LYS   E 3  48  ? 43.576  -68.970  -54.407  1.00 62.03  ? 53  LYS   E CE     1 
ATOM   13747 N  NZ     . LYS   E 3  48  ? 42.169  -68.797  -54.838  1.00 50.09  ? 53  LYS   E NZ     1 
ATOM   13748 N  N      . LEU   E 3  49  ? 46.215  -67.778  -50.845  1.00 66.25  ? 54  LEU   E N      1 
ATOM   13749 C  CA     . LEU   E 3  49  ? 45.484  -68.155  -49.635  1.00 62.70  ? 54  LEU   E CA     1 
ATOM   13750 C  C      . LEU   E 3  49  ? 46.055  -67.466  -48.404  1.00 69.03  ? 54  LEU   E C      1 
ATOM   13751 O  O      . LEU   E 3  49  ? 45.319  -66.884  -47.601  1.00 73.42  ? 54  LEU   E O      1 
ATOM   13752 C  CB     . LEU   E 3  49  ? 45.514  -69.670  -49.436  1.00 63.02  ? 54  LEU   E CB     1 
ATOM   13753 C  CG     . LEU   E 3  49  ? 44.203  -70.419  -49.650  1.00 68.54  ? 54  LEU   E CG     1 
ATOM   13754 C  CD1    . LEU   E 3  49  ? 43.593  -70.067  -51.005  1.00 63.01  ? 54  LEU   E CD1    1 
ATOM   13755 C  CD2    . LEU   E 3  49  ? 44.412  -71.931  -49.509  1.00 62.25  ? 54  LEU   E CD2    1 
ATOM   13756 N  N      . GLU   E 3  50  ? 47.368  -67.543  -48.219  1.00 72.21  ? 55  GLU   E N      1 
ATOM   13757 C  CA     . GLU   E 3  50  ? 47.955  -66.946  -47.032  1.00 69.71  ? 55  GLU   E CA     1 
ATOM   13758 C  C      . GLU   E 3  50  ? 47.964  -65.420  -47.088  1.00 63.99  ? 55  GLU   E C      1 
ATOM   13759 O  O      . GLU   E 3  50  ? 48.108  -64.779  -46.042  1.00 68.73  ? 55  GLU   E O      1 
ATOM   13760 C  CB     . GLU   E 3  50  ? 49.371  -67.487  -46.821  1.00 77.16  ? 55  GLU   E CB     1 
ATOM   13761 C  CG     . GLU   E 3  50  ? 49.451  -68.704  -45.895  1.00 70.77  ? 55  GLU   E CG     1 
ATOM   13762 C  CD     . GLU   E 3  50  ? 50.780  -69.417  -46.017  1.00 76.99  ? 55  GLU   E CD     1 
ATOM   13763 O  OE1    . GLU   E 3  50  ? 51.752  -68.754  -46.444  1.00 69.44  ? 55  GLU   E OE1    1 
ATOM   13764 O  OE2    . GLU   E 3  50  ? 50.853  -70.627  -45.690  1.00 76.86  ? 55  GLU   E OE2    1 
ATOM   13765 N  N      . ALA   E 3  51  ? 47.823  -64.822  -48.270  1.00 55.52  ? 56  ALA   E N      1 
ATOM   13766 C  CA     . ALA   E 3  51  ? 47.628  -63.381  -48.335  1.00 57.77  ? 56  ALA   E CA     1 
ATOM   13767 C  C      . ALA   E 3  51  ? 46.280  -62.979  -47.749  1.00 66.10  ? 56  ALA   E C      1 
ATOM   13768 O  O      . ALA   E 3  51  ? 46.158  -61.916  -47.131  1.00 66.36  ? 56  ALA   E O      1 
ATOM   13769 C  CB     . ALA   E 3  51  ? 47.737  -62.893  -49.776  1.00 55.48  ? 56  ALA   E CB     1 
ATOM   13770 N  N      . ALA   E 3  52  ? 45.254  -63.808  -47.939  1.00 65.55  ? 57  ALA   E N      1 
ATOM   13771 C  CA     . ALA   E 3  52  ? 43.957  -63.499  -47.365  1.00 61.31  ? 57  ALA   E CA     1 
ATOM   13772 C  C      . ALA   E 3  52  ? 43.951  -63.695  -45.854  1.00 62.87  ? 57  ALA   E C      1 
ATOM   13773 O  O      . ALA   E 3  52  ? 43.199  -63.011  -45.155  1.00 64.64  ? 57  ALA   E O      1 
ATOM   13774 C  CB     . ALA   E 3  52  ? 42.872  -64.351  -48.026  1.00 59.35  ? 57  ALA   E CB     1 
ATOM   13775 N  N      . GLU   E 3  53  ? 44.758  -64.622  -45.326  1.00 61.89  ? 58  GLU   E N      1 
ATOM   13776 C  CA     . GLU   E 3  53  ? 44.847  -64.757  -43.875  1.00 63.80  ? 58  GLU   E CA     1 
ATOM   13777 C  C      . GLU   E 3  53  ? 45.673  -63.642  -43.237  1.00 70.05  ? 58  GLU   E C      1 
ATOM   13778 O  O      . GLU   E 3  53  ? 45.489  -63.353  -42.050  1.00 69.24  ? 58  GLU   E O      1 
ATOM   13779 C  CB     . GLU   E 3  53  ? 45.417  -66.124  -43.476  1.00 61.44  ? 58  GLU   E CB     1 
ATOM   13780 C  CG     . GLU   E 3  53  ? 45.963  -66.153  -42.036  1.00 66.15  ? 58  GLU   E CG     1 
ATOM   13781 C  CD     . GLU   E 3  53  ? 45.851  -67.510  -41.351  1.00 73.48  ? 58  GLU   E CD     1 
ATOM   13782 O  OE1    . GLU   E 3  53  ? 44.741  -67.884  -40.917  1.00 81.48  ? 58  GLU   E OE1    1 
ATOM   13783 O  OE2    . GLU   E 3  53  ? 46.877  -68.211  -41.244  1.00 79.75  ? 58  GLU   E OE2    1 
ATOM   13784 N  N      . GLU   E 3  54  ? 46.581  -63.012  -43.984  1.00 69.42  ? 59  GLU   E N      1 
ATOM   13785 C  CA     . GLU   E 3  54  ? 47.219  -61.804  -43.479  1.00 66.55  ? 59  GLU   E CA     1 
ATOM   13786 C  C      . GLU   E 3  54  ? 46.256  -60.628  -43.537  1.00 62.56  ? 59  GLU   E C      1 
ATOM   13787 O  O      . GLU   E 3  54  ? 46.074  -59.921  -42.539  1.00 66.43  ? 59  GLU   E O      1 
ATOM   13788 C  CB     . GLU   E 3  54  ? 48.497  -61.503  -44.264  1.00 70.91  ? 59  GLU   E CB     1 
ATOM   13789 C  CG     . GLU   E 3  54  ? 49.708  -62.291  -43.780  1.00 85.28  ? 59  GLU   E CG     1 
ATOM   13790 C  CD     . GLU   E 3  54  ? 49.609  -62.707  -42.306  1.00 91.98  ? 59  GLU   E CD     1 
ATOM   13791 O  OE1    . GLU   E 3  54  ? 49.268  -61.851  -41.456  1.00 95.91  ? 59  GLU   E OE1    1 
ATOM   13792 O  OE2    . GLU   E 3  54  ? 49.874  -63.892  -41.997  1.00 91.90  ? 59  GLU   E OE2    1 
ATOM   13793 N  N      . ARG   E 3  55  ? 45.626  -60.406  -44.697  1.00 60.51  ? 60  ARG   E N      1 
ATOM   13794 C  CA     . ARG   E 3  55  ? 44.580  -59.391  -44.785  1.00 61.75  ? 60  ARG   E CA     1 
ATOM   13795 C  C      . ARG   E 3  55  ? 43.569  -59.542  -43.646  1.00 61.16  ? 60  ARG   E C      1 
ATOM   13796 O  O      . ARG   E 3  55  ? 43.046  -58.544  -43.141  1.00 58.71  ? 60  ARG   E O      1 
ATOM   13797 C  CB     . ARG   E 3  55  ? 43.890  -59.457  -46.156  1.00 55.95  ? 60  ARG   E CB     1 
ATOM   13798 C  CG     . ARG   E 3  55  ? 44.646  -58.747  -47.276  1.00 50.90  ? 60  ARG   E CG     1 
ATOM   13799 C  CD     . ARG   E 3  55  ? 43.815  -58.523  -48.555  1.00 56.57  ? 60  ARG   E CD     1 
ATOM   13800 N  NE     . ARG   E 3  55  ? 43.463  -59.775  -49.216  1.00 61.76  ? 60  ARG   E NE     1 
ATOM   13801 C  CZ     . ARG   E 3  55  ? 44.341  -60.625  -49.733  1.00 61.01  ? 60  ARG   E CZ     1 
ATOM   13802 N  NH1    . ARG   E 3  55  ? 45.636  -60.360  -49.746  1.00 63.13  ? 60  ARG   E NH1    1 
ATOM   13803 N  NH2    . ARG   E 3  55  ? 43.911  -61.779  -50.228  1.00 59.68  ? 60  ARG   E NH2    1 
ATOM   13804 N  N      . ARG   E 3  56  ? 43.315  -60.773  -43.201  1.00 59.89  ? 61  ARG   E N      1 
ATOM   13805 C  CA     . ARG   E 3  56  ? 42.414  -60.976  -42.072  1.00 58.51  ? 61  ARG   E CA     1 
ATOM   13806 C  C      . ARG   E 3  56  ? 43.049  -60.488  -40.784  1.00 59.27  ? 61  ARG   E C      1 
ATOM   13807 O  O      . ARG   E 3  56  ? 42.460  -59.674  -40.067  1.00 67.75  ? 61  ARG   E O      1 
ATOM   13808 C  CB     . ARG   E 3  56  ? 42.039  -62.453  -41.939  1.00 58.87  ? 61  ARG   E CB     1 
ATOM   13809 C  CG     . ARG   E 3  56  ? 40.764  -62.846  -42.622  1.00 50.03  ? 61  ARG   E CG     1 
ATOM   13810 C  CD     . ARG   E 3  56  ? 40.077  -63.973  -41.868  1.00 55.76  ? 61  ARG   E CD     1 
ATOM   13811 N  NE     . ARG   E 3  56  ? 40.896  -65.173  -41.687  1.00 63.86  ? 61  ARG   E NE     1 
ATOM   13812 C  CZ     . ARG   E 3  56  ? 41.430  -65.892  -42.677  1.00 70.14  ? 61  ARG   E CZ     1 
ATOM   13813 N  NH1    . ARG   E 3  56  ? 41.348  -65.509  -43.952  1.00 53.73  ? 61  ARG   E NH1    1 
ATOM   13814 N  NH2    . ARG   E 3  56  ? 42.073  -67.020  -42.383  1.00 65.56  ? 61  ARG   E NH2    1 
ATOM   13815 N  N      . LYS   E 3  57  ? 44.259  -60.980  -40.474  1.00 66.00  ? 62  LYS   E N      1 
ATOM   13816 C  CA     . LYS   E 3  57  ? 44.930  -60.630  -39.220  1.00 61.98  ? 62  LYS   E CA     1 
ATOM   13817 C  C      . LYS   E 3  57  ? 45.224  -59.137  -39.121  1.00 58.09  ? 62  LYS   E C      1 
ATOM   13818 O  O      . LYS   E 3  57  ? 45.220  -58.584  -38.014  1.00 55.95  ? 62  LYS   E O      1 
ATOM   13819 C  CB     . LYS   E 3  57  ? 46.223  -61.424  -39.061  1.00 58.19  ? 62  LYS   E CB     1 
ATOM   13820 C  CG     . LYS   E 3  57  ? 46.021  -62.780  -38.449  1.00 63.32  ? 62  LYS   E CG     1 
ATOM   13821 C  CD     . LYS   E 3  57  ? 46.912  -63.821  -39.105  1.00 73.05  ? 62  LYS   E CD     1 
ATOM   13822 C  CE     . LYS   E 3  57  ? 48.208  -64.004  -38.314  1.00 86.02  ? 62  LYS   E CE     1 
ATOM   13823 N  NZ     . LYS   E 3  57  ? 49.294  -64.649  -39.111  1.00 83.49  ? 62  LYS   E NZ     1 
ATOM   13824 N  N      . TYR   E 3  58  ? 45.476  -58.463  -40.248  1.00 48.95  ? 63  TYR   E N      1 
ATOM   13825 C  CA     . TYR   E 3  58  ? 45.559  -57.012  -40.196  1.00 51.14  ? 63  TYR   E CA     1 
ATOM   13826 C  C      . TYR   E 3  58  ? 44.239  -56.428  -39.707  1.00 60.13  ? 63  TYR   E C      1 
ATOM   13827 O  O      . TYR   E 3  58  ? 44.166  -55.835  -38.623  1.00 61.12  ? 63  TYR   E O      1 
ATOM   13828 C  CB     . TYR   E 3  58  ? 45.928  -56.436  -41.560  1.00 52.80  ? 63  TYR   E CB     1 
ATOM   13829 C  CG     . TYR   E 3  58  ? 46.045  -54.920  -41.559  1.00 57.84  ? 63  TYR   E CG     1 
ATOM   13830 C  CD1    . TYR   E 3  58  ? 47.219  -54.294  -41.160  1.00 63.15  ? 63  TYR   E CD1    1 
ATOM   13831 C  CD2    . TYR   E 3  58  ? 44.976  -54.115  -41.931  1.00 61.44  ? 63  TYR   E CD2    1 
ATOM   13832 C  CE1    . TYR   E 3  58  ? 47.335  -52.904  -41.145  1.00 68.06  ? 63  TYR   E CE1    1 
ATOM   13833 C  CE2    . TYR   E 3  58  ? 45.080  -52.726  -41.927  1.00 67.71  ? 63  TYR   E CE2    1 
ATOM   13834 C  CZ     . TYR   E 3  58  ? 46.265  -52.124  -41.531  1.00 77.49  ? 63  TYR   E CZ     1 
ATOM   13835 O  OH     . TYR   E 3  58  ? 46.389  -50.745  -41.516  1.00 78.81  ? 63  TYR   E OH     1 
ATOM   13836 N  N      . GLN   E 3  59  ? 43.175  -56.617  -40.493  1.00 58.51  ? 64  GLN   E N      1 
ATOM   13837 C  CA     . GLN   E 3  59  ? 41.859  -56.103  -40.134  1.00 57.75  ? 64  GLN   E CA     1 
ATOM   13838 C  C      . GLN   E 3  59  ? 41.490  -56.426  -38.691  1.00 57.44  ? 64  GLN   E C      1 
ATOM   13839 O  O      . GLN   E 3  59  ? 40.829  -55.619  -38.017  1.00 47.67  ? 64  GLN   E O      1 
ATOM   13840 C  CB     . GLN   E 3  59  ? 40.813  -56.665  -41.096  1.00 57.37  ? 64  GLN   E CB     1 
ATOM   13841 C  CG     . GLN   E 3  59  ? 40.947  -56.141  -42.525  1.00 65.35  ? 64  GLN   E CG     1 
ATOM   13842 C  CD     . GLN   E 3  59  ? 40.313  -57.063  -43.559  1.00 61.36  ? 64  GLN   E CD     1 
ATOM   13843 O  OE1    . GLN   E 3  59  ? 39.536  -57.971  -43.223  1.00 55.72  ? 64  GLN   E OE1    1 
ATOM   13844 N  NE2    . GLN   E 3  59  ? 40.658  -56.843  -44.828  1.00 55.35  ? 64  GLN   E NE2    1 
ATOM   13845 N  N      . GLU   E 3  60  ? 41.908  -57.589  -38.194  1.00 49.98  ? 65  GLU   E N      1 
ATOM   13846 C  CA     . GLU   E 3  60  ? 41.576  -57.920  -36.821  1.00 52.99  ? 65  GLU   E CA     1 
ATOM   13847 C  C      . GLU   E 3  60  ? 42.456  -57.194  -35.822  1.00 62.05  ? 65  GLU   E C      1 
ATOM   13848 O  O      . GLU   E 3  60  ? 42.000  -56.907  -34.707  1.00 64.55  ? 65  GLU   E O      1 
ATOM   13849 C  CB     . GLU   E 3  60  ? 41.697  -59.412  -36.564  1.00 54.81  ? 65  GLU   E CB     1 
ATOM   13850 C  CG     . GLU   E 3  60  ? 41.438  -59.747  -35.105  1.00 59.87  ? 65  GLU   E CG     1 
ATOM   13851 C  CD     . GLU   E 3  60  ? 41.774  -61.173  -34.770  1.00 70.71  ? 65  GLU   E CD     1 
ATOM   13852 O  OE1    . GLU   E 3  60  ? 42.636  -61.754  -35.464  1.00 75.19  ? 65  GLU   E OE1    1 
ATOM   13853 O  OE2    . GLU   E 3  60  ? 41.153  -61.726  -33.834  1.00 70.45  ? 65  GLU   E OE2    1 
ATOM   13854 N  N      . ALA   E 3  61  ? 43.720  -56.927  -36.176  1.00 61.40  ? 66  ALA   E N      1 
ATOM   13855 C  CA     . ALA   E 3  61  ? 44.592  -56.214  -35.250  1.00 59.62  ? 66  ALA   E CA     1 
ATOM   13856 C  C      . ALA   E 3  61  ? 44.223  -54.735  -35.188  1.00 58.34  ? 66  ALA   E C      1 
ATOM   13857 O  O      . ALA   E 3  61  ? 44.306  -54.120  -34.119  1.00 57.58  ? 66  ALA   E O      1 
ATOM   13858 C  CB     . ALA   E 3  61  ? 46.062  -56.417  -35.633  1.00 46.84  ? 66  ALA   E CB     1 
ATOM   13859 N  N      . GLU   E 3  62  ? 43.759  -54.161  -36.298  1.00 55.80  ? 67  GLU   E N      1 
ATOM   13860 C  CA     . GLU   E 3  62  ? 43.180  -52.824  -36.229  1.00 58.08  ? 67  GLU   E CA     1 
ATOM   13861 C  C      . GLU   E 3  62  ? 41.975  -52.794  -35.297  1.00 58.59  ? 67  GLU   E C      1 
ATOM   13862 O  O      . GLU   E 3  62  ? 41.812  -51.853  -34.511  1.00 60.45  ? 67  GLU   E O      1 
ATOM   13863 C  CB     . GLU   E 3  62  ? 42.803  -52.347  -37.627  1.00 58.02  ? 67  GLU   E CB     1 
ATOM   13864 C  CG     . GLU   E 3  62  ? 44.028  -52.211  -38.494  1.00 67.30  ? 67  GLU   E CG     1 
ATOM   13865 C  CD     . GLU   E 3  62  ? 44.979  -51.185  -37.931  1.00 72.64  ? 67  GLU   E CD     1 
ATOM   13866 O  OE1    . GLU   E 3  62  ? 44.744  -49.981  -38.171  1.00 77.36  ? 67  GLU   E OE1    1 
ATOM   13867 O  OE2    . GLU   E 3  62  ? 45.917  -51.572  -37.196  1.00 69.46  ? 67  GLU   E OE2    1 
ATOM   13868 N  N      . LEU   E 3  63  ? 41.115  -53.809  -35.368  1.00 54.81  ? 68  LEU   E N      1 
ATOM   13869 C  CA     . LEU   E 3  63  ? 39.981  -53.846  -34.460  1.00 51.09  ? 68  LEU   E CA     1 
ATOM   13870 C  C      . LEU   E 3  63  ? 40.455  -53.884  -33.017  1.00 56.66  ? 68  LEU   E C      1 
ATOM   13871 O  O      . LEU   E 3  63  ? 39.967  -53.129  -32.166  1.00 54.40  ? 68  LEU   E O      1 
ATOM   13872 C  CB     . LEU   E 3  63  ? 39.098  -55.051  -34.754  1.00 53.51  ? 68  LEU   E CB     1 
ATOM   13873 C  CG     . LEU   E 3  63  ? 38.038  -55.223  -33.658  1.00 53.59  ? 68  LEU   E CG     1 
ATOM   13874 C  CD1    . LEU   E 3  63  ? 36.978  -54.096  -33.695  1.00 49.42  ? 68  LEU   E CD1    1 
ATOM   13875 C  CD2    . LEU   E 3  63  ? 37.409  -56.586  -33.700  1.00 47.37  ? 68  LEU   E CD2    1 
ATOM   13876 N  N      . LEU   E 3  64  ? 41.411  -54.765  -32.724  1.00 52.86  ? 69  LEU   E N      1 
ATOM   13877 C  CA     . LEU   E 3  64  ? 41.954  -54.854  -31.378  1.00 51.19  ? 69  LEU   E CA     1 
ATOM   13878 C  C      . LEU   E 3  64  ? 42.740  -53.603  -30.994  1.00 55.23  ? 69  LEU   E C      1 
ATOM   13879 O  O      . LEU   E 3  64  ? 42.794  -53.254  -29.809  1.00 52.65  ? 69  LEU   E O      1 
ATOM   13880 C  CB     . LEU   E 3  64  ? 42.822  -56.101  -31.264  1.00 48.71  ? 69  LEU   E CB     1 
ATOM   13881 C  CG     . LEU   E 3  64  ? 41.929  -57.329  -31.094  1.00 53.86  ? 69  LEU   E CG     1 
ATOM   13882 C  CD1    . LEU   E 3  64  ? 42.664  -58.417  -30.381  1.00 53.59  ? 69  LEU   E CD1    1 
ATOM   13883 C  CD2    . LEU   E 3  64  ? 40.646  -56.970  -30.337  1.00 48.64  ? 69  LEU   E CD2    1 
ATOM   13884 N  N      . LYS   E 3  65  ? 43.355  -52.915  -31.968  1.00 53.91  ? 70  LYS   E N      1 
ATOM   13885 C  CA     . LYS   E 3  65  ? 44.023  -51.652  -31.661  1.00 53.42  ? 70  LYS   E CA     1 
ATOM   13886 C  C      . LYS   E 3  65  ? 43.008  -50.600  -31.225  1.00 57.42  ? 70  LYS   E C      1 
ATOM   13887 O  O      . LYS   E 3  65  ? 43.170  -49.953  -30.179  1.00 49.96  ? 70  LYS   E O      1 
ATOM   13888 C  CB     . LYS   E 3  65  ? 44.819  -51.157  -32.873  1.00 53.16  ? 70  LYS   E CB     1 
ATOM   13889 C  CG     . LYS   E 3  65  ? 46.047  -50.324  -32.517  1.00 56.21  ? 70  LYS   E CG     1 
ATOM   13890 C  CD     . LYS   E 3  65  ? 46.427  -49.297  -33.590  1.00 63.83  ? 70  LYS   E CD     1 
ATOM   13891 C  CE     . LYS   E 3  65  ? 47.971  -49.196  -33.758  1.00 79.18  ? 70  LYS   E CE     1 
ATOM   13892 N  NZ     . LYS   E 3  65  ? 48.729  -48.648  -32.554  1.00 75.67  ? 70  LYS   E NZ     1 
ATOM   13893 N  N      . HIS   E 3  66  ? 41.952  -50.429  -32.033  1.00 58.32  ? 71  HIS   E N      1 
ATOM   13894 C  CA     . HIS   E 3  66  ? 40.872  -49.484  -31.752  1.00 59.23  ? 71  HIS   E CA     1 
ATOM   13895 C  C      . HIS   E 3  66  ? 40.160  -49.808  -30.432  1.00 52.60  ? 71  HIS   E C      1 
ATOM   13896 O  O      . HIS   E 3  66  ? 39.799  -48.905  -29.672  1.00 45.56  ? 71  HIS   E O      1 
ATOM   13897 C  CB     . HIS   E 3  66  ? 39.907  -49.502  -32.942  1.00 54.79  ? 71  HIS   E CB     1 
ATOM   13898 C  CG     . HIS   E 3  66  ? 38.782  -48.526  -32.849  1.00 60.69  ? 71  HIS   E CG     1 
ATOM   13899 N  ND1    . HIS   E 3  66  ? 37.615  -48.797  -32.163  1.00 60.21  ? 71  HIS   E ND1    1 
ATOM   13900 C  CD2    . HIS   E 3  66  ? 38.631  -47.286  -33.377  1.00 65.43  ? 71  HIS   E CD2    1 
ATOM   13901 C  CE1    . HIS   E 3  66  ? 36.795  -47.764  -32.268  1.00 64.36  ? 71  HIS   E CE1    1 
ATOM   13902 N  NE2    . HIS   E 3  66  ? 37.388  -46.834  -32.998  1.00 68.05  ? 71  HIS   E NE2    1 
ATOM   13903 N  N      . LEU   E 3  67  ? 39.949  -51.086  -30.136  1.00 45.33  ? 72  LEU   E N      1 
ATOM   13904 C  CA     . LEU   E 3  67  ? 39.422  -51.406  -28.822  1.00 51.40  ? 72  LEU   E CA     1 
ATOM   13905 C  C      . LEU   E 3  67  ? 40.388  -50.968  -27.738  1.00 55.41  ? 72  LEU   E C      1 
ATOM   13906 O  O      . LEU   E 3  67  ? 39.972  -50.626  -26.625  1.00 55.62  ? 72  LEU   E O      1 
ATOM   13907 C  CB     . LEU   E 3  67  ? 39.143  -52.903  -28.692  1.00 51.47  ? 72  LEU   E CB     1 
ATOM   13908 C  CG     . LEU   E 3  67  ? 38.028  -53.498  -29.539  1.00 52.47  ? 72  LEU   E CG     1 
ATOM   13909 C  CD1    . LEU   E 3  67  ? 37.594  -54.850  -28.972  1.00 50.35  ? 72  LEU   E CD1    1 
ATOM   13910 C  CD2    . LEU   E 3  67  ? 36.865  -52.532  -29.666  1.00 48.42  ? 72  LEU   E CD2    1 
ATOM   13911 N  N      . ALA   E 3  68  ? 41.687  -50.995  -28.024  1.00 58.49  ? 73  ALA   E N      1 
ATOM   13912 C  CA     . ALA   E 3  68  ? 42.638  -50.675  -26.970  1.00 53.24  ? 73  ALA   E CA     1 
ATOM   13913 C  C      . ALA   E 3  68  ? 42.640  -49.178  -26.692  1.00 52.90  ? 73  ALA   E C      1 
ATOM   13914 O  O      . ALA   E 3  68  ? 42.724  -48.759  -25.528  1.00 48.47  ? 73  ALA   E O      1 
ATOM   13915 C  CB     . ALA   E 3  68  ? 44.022  -51.186  -27.344  1.00 47.68  ? 73  ALA   E CB     1 
ATOM   13916 N  N      . GLU   E 3  69  ? 42.514  -48.364  -27.753  1.00 48.13  ? 74  GLU   E N      1 
ATOM   13917 C  CA     . GLU   E 3  69  ? 42.255  -46.937  -27.594  1.00 48.79  ? 74  GLU   E CA     1 
ATOM   13918 C  C      . GLU   E 3  69  ? 41.034  -46.705  -26.720  1.00 50.96  ? 74  GLU   E C      1 
ATOM   13919 O  O      . GLU   E 3  69  ? 41.033  -45.822  -25.858  1.00 54.47  ? 74  GLU   E O      1 
ATOM   13920 C  CB     . GLU   E 3  69  ? 42.035  -46.268  -28.953  1.00 49.07  ? 74  GLU   E CB     1 
ATOM   13921 C  CG     . GLU   E 3  69  ? 43.267  -45.914  -29.748  1.00 55.89  ? 74  GLU   E CG     1 
ATOM   13922 C  CD     . GLU   E 3  69  ? 42.945  -45.665  -31.222  1.00 73.96  ? 74  GLU   E CD     1 
ATOM   13923 O  OE1    . GLU   E 3  69  ? 41.789  -45.940  -31.627  1.00 77.81  ? 74  GLU   E OE1    1 
ATOM   13924 O  OE2    . GLU   E 3  69  ? 43.837  -45.204  -31.983  1.00 76.41  ? 74  GLU   E OE2    1 
ATOM   13925 N  N      . LYS   E 3  70  ? 39.971  -47.479  -26.939  1.00 51.77  ? 75  LYS   E N      1 
ATOM   13926 C  CA     . LYS   E 3  70  ? 38.746  -47.251  -26.183  1.00 50.53  ? 75  LYS   E CA     1 
ATOM   13927 C  C      . LYS   E 3  70  ? 38.975  -47.462  -24.688  1.00 52.22  ? 75  LYS   E C      1 
ATOM   13928 O  O      . LYS   E 3  70  ? 38.437  -46.710  -23.871  1.00 54.84  ? 75  LYS   E O      1 
ATOM   13929 C  CB     . LYS   E 3  70  ? 37.618  -48.148  -26.708  1.00 46.27  ? 75  LYS   E CB     1 
ATOM   13930 C  CG     . LYS   E 3  70  ? 36.236  -47.671  -26.326  1.00 54.61  ? 75  LYS   E CG     1 
ATOM   13931 C  CD     . LYS   E 3  70  ? 35.448  -48.739  -25.524  1.00 56.94  ? 75  LYS   E CD     1 
ATOM   13932 C  CE     . LYS   E 3  70  ? 34.020  -48.257  -25.134  1.00 47.56  ? 75  LYS   E CE     1 
ATOM   13933 N  NZ     . LYS   E 3  70  ? 34.042  -46.999  -24.308  1.00 45.85  ? 75  LYS   E NZ     1 
ATOM   13934 N  N      . ARG   E 3  71  ? 39.779  -48.466  -24.303  1.00 49.83  ? 76  ARG   E N      1 
ATOM   13935 C  CA     . ARG   E 3  71  ? 40.042  -48.690  -22.882  1.00 47.19  ? 76  ARG   E CA     1 
ATOM   13936 C  C      . ARG   E 3  71  ? 40.947  -47.613  -22.304  1.00 48.67  ? 76  ARG   E C      1 
ATOM   13937 O  O      . ARG   E 3  71  ? 40.846  -47.279  -21.122  1.00 46.63  ? 76  ARG   E O      1 
ATOM   13938 C  CB     . ARG   E 3  71  ? 40.684  -50.059  -22.657  1.00 49.52  ? 76  ARG   E CB     1 
ATOM   13939 C  CG     . ARG   E 3  71  ? 40.122  -51.153  -23.510  1.00 55.37  ? 76  ARG   E CG     1 
ATOM   13940 C  CD     . ARG   E 3  71  ? 39.065  -51.958  -22.772  1.00 56.15  ? 76  ARG   E CD     1 
ATOM   13941 N  NE     . ARG   E 3  71  ? 38.335  -52.829  -23.689  1.00 61.61  ? 76  ARG   E NE     1 
ATOM   13942 C  CZ     . ARG   E 3  71  ? 37.192  -52.523  -24.295  1.00 55.93  ? 76  ARG   E CZ     1 
ATOM   13943 N  NH1    . ARG   E 3  71  ? 36.561  -51.379  -24.064  1.00 46.87  ? 76  ARG   E NH1    1 
ATOM   13944 N  NH2    . ARG   E 3  71  ? 36.663  -53.394  -25.150  1.00 57.37  ? 76  ARG   E NH2    1 
ATOM   13945 N  N      . GLU   E 3  72  ? 41.874  -47.100  -23.102  1.00 52.28  ? 77  GLU   E N      1 
ATOM   13946 C  CA     . GLU   E 3  72  ? 42.670  -45.967  -22.662  1.00 50.81  ? 77  GLU   E CA     1 
ATOM   13947 C  C      . GLU   E 3  72  ? 41.760  -44.813  -22.274  1.00 50.29  ? 77  GLU   E C      1 
ATOM   13948 O  O      . GLU   E 3  72  ? 41.919  -44.206  -21.210  1.00 53.65  ? 77  GLU   E O      1 
ATOM   13949 C  CB     . GLU   E 3  72  ? 43.621  -45.567  -23.784  1.00 57.85  ? 77  GLU   E CB     1 
ATOM   13950 C  CG     . GLU   E 3  72  ? 44.775  -44.708  -23.383  1.00 71.13  ? 77  GLU   E CG     1 
ATOM   13951 C  CD     . GLU   E 3  72  ? 45.701  -44.452  -24.544  1.00 81.76  ? 77  GLU   E CD     1 
ATOM   13952 O  OE1    . GLU   E 3  72  ? 45.707  -45.278  -25.495  1.00 82.83  ? 77  GLU   E OE1    1 
ATOM   13953 O  OE2    . GLU   E 3  72  ? 46.403  -43.414  -24.514  1.00 88.22  ? 77  GLU   E OE2    1 
ATOM   13954 N  N      . HIS   E 3  73  ? 40.770  -44.530  -23.122  1.00 47.41  ? 78  HIS   E N      1 
ATOM   13955 C  CA     . HIS   E 3  73  ? 39.755  -43.526  -22.827  1.00 43.97  ? 78  HIS   E CA     1 
ATOM   13956 C  C      . HIS   E 3  73  ? 38.950  -43.871  -21.576  1.00 49.62  ? 78  HIS   E C      1 
ATOM   13957 O  O      . HIS   E 3  73  ? 38.751  -43.021  -20.705  1.00 50.59  ? 78  HIS   E O      1 
ATOM   13958 C  CB     . HIS   E 3  73  ? 38.828  -43.402  -24.019  1.00 38.49  ? 78  HIS   E CB     1 
ATOM   13959 C  CG     . HIS   E 3  73  ? 37.737  -42.414  -23.819  1.00 40.55  ? 78  HIS   E CG     1 
ATOM   13960 N  ND1    . HIS   E 3  73  ? 37.981  -41.075  -23.629  1.00 42.77  ? 78  HIS   E ND1    1 
ATOM   13961 C  CD2    . HIS   E 3  73  ? 36.395  -42.562  -23.789  1.00 45.97  ? 78  HIS   E CD2    1 
ATOM   13962 C  CE1    . HIS   E 3  73  ? 36.835  -40.438  -23.487  1.00 35.66  ? 78  HIS   E CE1    1 
ATOM   13963 N  NE2    . HIS   E 3  73  ? 35.856  -41.317  -23.584  1.00 40.78  ? 78  HIS   E NE2    1 
ATOM   13964 N  N      . GLU   E 3  74  ? 38.463  -45.113  -21.478  1.00 45.55  ? 79  GLU   E N      1 
ATOM   13965 C  CA     . GLU   E 3  74  ? 37.658  -45.523  -20.330  1.00 44.51  ? 79  GLU   E CA     1 
ATOM   13966 C  C      . GLU   E 3  74  ? 38.371  -45.270  -19.012  1.00 50.14  ? 79  GLU   E C      1 
ATOM   13967 O  O      . GLU   E 3  74  ? 37.727  -44.922  -18.010  1.00 48.97  ? 79  GLU   E O      1 
ATOM   13968 C  CB     . GLU   E 3  74  ? 37.291  -47.002  -20.427  1.00 42.75  ? 79  GLU   E CB     1 
ATOM   13969 C  CG     . GLU   E 3  74  ? 36.444  -47.318  -21.631  1.00 49.58  ? 79  GLU   E CG     1 
ATOM   13970 C  CD     . GLU   E 3  74  ? 36.327  -48.805  -21.931  1.00 50.16  ? 79  GLU   E CD     1 
ATOM   13971 O  OE1    . GLU   E 3  74  ? 37.016  -49.638  -21.283  1.00 41.57  ? 79  GLU   E OE1    1 
ATOM   13972 O  OE2    . GLU   E 3  74  ? 35.492  -49.122  -22.808  1.00 52.21  ? 79  GLU   E OE2    1 
ATOM   13973 N  N      . ARG   E 3  75  ? 39.694  -45.469  -18.972  1.00 49.60  ? 80  ARG   E N      1 
ATOM   13974 C  CA     . ARG   E 3  75  ? 40.377  -45.209  -17.714  1.00 51.37  ? 80  ARG   E CA     1 
ATOM   13975 C  C      . ARG   E 3  75  ? 40.685  -43.720  -17.553  1.00 51.49  ? 80  ARG   E C      1 
ATOM   13976 O  O      . ARG   E 3  75  ? 40.721  -43.237  -16.421  1.00 48.54  ? 80  ARG   E O      1 
ATOM   13977 C  CB     . ARG   E 3  75  ? 41.631  -46.093  -17.570  1.00 52.68  ? 80  ARG   E CB     1 
ATOM   13978 C  CG     . ARG   E 3  75  ? 42.871  -45.670  -18.333  1.00 57.81  ? 80  ARG   E CG     1 
ATOM   13979 C  CD     . ARG   E 3  75  ? 44.102  -46.579  -18.052  1.00 67.63  ? 80  ARG   E CD     1 
ATOM   13980 N  NE     . ARG   E 3  75  ? 43.781  -48.007  -18.079  1.00 74.13  ? 80  ARG   E NE     1 
ATOM   13981 C  CZ     . ARG   E 3  75  ? 43.983  -48.809  -19.123  1.00 84.45  ? 80  ARG   E CZ     1 
ATOM   13982 N  NH1    . ARG   E 3  75  ? 44.456  -48.347  -20.277  1.00 72.94  ? 80  ARG   E NH1    1 
ATOM   13983 N  NH2    . ARG   E 3  75  ? 43.681  -50.106  -19.017  1.00 85.54  ? 80  ARG   E NH2    1 
ATOM   13984 N  N      . GLU   E 3  76  ? 40.820  -42.959  -18.652  1.00 47.43  ? 81  GLU   E N      1 
ATOM   13985 C  CA     . GLU   E 3  76  ? 40.999  -41.513  -18.518  1.00 45.21  ? 81  GLU   E CA     1 
ATOM   13986 C  C      . GLU   E 3  76  ? 39.759  -40.824  -17.964  1.00 48.68  ? 81  GLU   E C      1 
ATOM   13987 O  O      . GLU   E 3  76  ? 39.881  -39.832  -17.233  1.00 49.75  ? 81  GLU   E O      1 
ATOM   13988 C  CB     . GLU   E 3  76  ? 41.369  -40.879  -19.850  1.00 41.59  ? 81  GLU   E CB     1 
ATOM   13989 C  CG     . GLU   E 3  76  ? 42.799  -41.144  -20.212  1.00 56.39  ? 81  GLU   E CG     1 
ATOM   13990 C  CD     . GLU   E 3  76  ? 43.146  -40.764  -21.645  1.00 65.95  ? 81  GLU   E CD     1 
ATOM   13991 O  OE1    . GLU   E 3  76  ? 42.552  -39.773  -22.151  1.00 70.45  ? 81  GLU   E OE1    1 
ATOM   13992 O  OE2    . GLU   E 3  76  ? 43.998  -41.479  -22.252  1.00 57.29  ? 81  GLU   E OE2    1 
ATOM   13993 N  N      . VAL   E 3  77  ? 38.564  -41.319  -18.295  1.00 45.46  ? 82  VAL   E N      1 
ATOM   13994 C  CA     . VAL   E 3  77  ? 37.351  -40.692  -17.784  1.00 43.33  ? 82  VAL   E CA     1 
ATOM   13995 C  C      . VAL   E 3  77  ? 37.210  -40.955  -16.281  1.00 45.23  ? 82  VAL   E C      1 
ATOM   13996 O  O      . VAL   E 3  77  ? 36.896  -40.044  -15.503  1.00 42.53  ? 82  VAL   E O      1 
ATOM   13997 C  CB     . VAL   E 3  77  ? 36.134  -41.160  -18.616  1.00 39.98  ? 82  VAL   E CB     1 
ATOM   13998 C  CG1    . VAL   E 3  77  ? 34.780  -40.947  -17.918  1.00 31.57  ? 82  VAL   E CG1    1 
ATOM   13999 C  CG2    . VAL   E 3  77  ? 36.130  -40.411  -19.923  1.00 41.63  ? 82  VAL   E CG2    1 
ATOM   14000 N  N      . ILE   E 3  78  ? 37.480  -42.180  -15.833  1.00 40.99  ? 83  ILE   E N      1 
ATOM   14001 C  CA     . ILE   E 3  78  ? 37.382  -42.427  -14.398  1.00 42.93  ? 83  ILE   E CA     1 
ATOM   14002 C  C      . ILE   E 3  78  ? 38.502  -41.714  -13.640  1.00 48.60  ? 83  ILE   E C      1 
ATOM   14003 O  O      . ILE   E 3  78  ? 38.321  -41.334  -12.478  1.00 49.05  ? 83  ILE   E O      1 
ATOM   14004 C  CB     . ILE   E 3  78  ? 37.387  -43.932  -14.118  1.00 40.62  ? 83  ILE   E CB     1 
ATOM   14005 C  CG1    . ILE   E 3  78  ? 36.840  -44.209  -12.721  1.00 38.31  ? 83  ILE   E CG1    1 
ATOM   14006 C  CG2    . ILE   E 3  78  ? 38.799  -44.492  -14.356  1.00 39.19  ? 83  ILE   E CG2    1 
ATOM   14007 C  CD1    . ILE   E 3  78  ? 36.719  -45.685  -12.400  1.00 40.82  ? 83  ILE   E CD1    1 
ATOM   14008 N  N      . GLN   E 3  79  ? 39.673  -41.518  -14.269  1.00 47.21  ? 84  GLN   E N      1 
ATOM   14009 C  CA     . GLN   E 3  79  ? 40.720  -40.715  -13.634  1.00 49.00  ? 84  GLN   E CA     1 
ATOM   14010 C  C      . GLN   E 3  79  ? 40.308  -39.245  -13.515  1.00 46.92  ? 84  GLN   E C      1 
ATOM   14011 O  O      . GLN   E 3  79  ? 40.748  -38.555  -12.589  1.00 49.13  ? 84  GLN   E O      1 
ATOM   14012 C  CB     . GLN   E 3  79  ? 42.058  -40.822  -14.393  1.00 44.72  ? 84  GLN   E CB     1 
ATOM   14013 C  CG     . GLN   E 3  79  ? 42.877  -42.119  -14.195  1.00 53.82  ? 84  GLN   E CG     1 
ATOM   14014 C  CD     . GLN   E 3  79  ? 44.018  -42.323  -15.254  1.00 71.11  ? 84  GLN   E CD     1 
ATOM   14015 O  OE1    . GLN   E 3  79  ? 44.646  -43.399  -15.319  1.00 73.78  ? 84  GLN   E OE1    1 
ATOM   14016 N  NE2    . GLN   E 3  79  ? 44.283  -41.287  -16.068  1.00 58.73  ? 84  GLN   E NE2    1 
ATOM   14017 N  N      . LYS   E 3  80  ? 39.487  -38.747  -14.440  1.00 41.83  ? 85  LYS   E N      1 
ATOM   14018 C  CA     . LYS   E 3  80  ? 39.033  -37.365  -14.365  1.00 37.68  ? 85  LYS   E CA     1 
ATOM   14019 C  C      . LYS   E 3  80  ? 37.998  -37.192  -13.257  1.00 43.90  ? 85  LYS   E C      1 
ATOM   14020 O  O      . LYS   E 3  80  ? 38.097  -36.268  -12.439  1.00 48.48  ? 85  LYS   E O      1 
ATOM   14021 C  CB     . LYS   E 3  80  ? 38.484  -36.940  -15.725  1.00 33.61  ? 85  LYS   E CB     1 
ATOM   14022 C  CG     . LYS   E 3  80  ? 38.417  -35.454  -15.937  1.00 47.18  ? 85  LYS   E CG     1 
ATOM   14023 C  CD     . LYS   E 3  80  ? 38.131  -35.095  -17.407  1.00 51.70  ? 85  LYS   E CD     1 
ATOM   14024 C  CE     . LYS   E 3  80  ? 37.274  -33.808  -17.493  1.00 58.74  ? 85  LYS   E CE     1 
ATOM   14025 N  NZ     . LYS   E 3  80  ? 36.825  -33.461  -18.872  1.00 52.98  ? 85  LYS   E NZ     1 
ATOM   14026 N  N      . ALA   E 3  81  ? 37.012  -38.090  -13.192  1.00 38.43  ? 86  ALA   E N      1 
ATOM   14027 C  CA     . ALA   E 3  81  ? 36.008  -38.003  -12.141  1.00 40.49  ? 86  ALA   E CA     1 
ATOM   14028 C  C      . ALA   E 3  81  ? 36.646  -38.034  -10.754  1.00 47.52  ? 86  ALA   E C      1 
ATOM   14029 O  O      . ALA   E 3  81  ? 36.151  -37.389  -9.822   1.00 48.89  ? 86  ALA   E O      1 
ATOM   14030 C  CB     . ALA   E 3  81  ? 35.003  -39.136  -12.283  1.00 41.35  ? 86  ALA   E CB     1 
ATOM   14031 N  N      . ILE   E 3  82  ? 37.720  -38.810  -10.595  1.00 47.88  ? 87  ILE   E N      1 
ATOM   14032 C  CA     . ILE   E 3  82  ? 38.477  -38.824  -9.347   1.00 41.04  ? 87  ILE   E CA     1 
ATOM   14033 C  C      . ILE   E 3  82  ? 39.231  -37.517  -9.182   1.00 42.30  ? 87  ILE   E C      1 
ATOM   14034 O  O      . ILE   E 3  82  ? 39.143  -36.861  -8.145   1.00 43.27  ? 87  ILE   E O      1 
ATOM   14035 C  CB     . ILE   E 3  82  ? 39.442  -40.024  -9.311   1.00 40.83  ? 87  ILE   E CB     1 
ATOM   14036 C  CG1    . ILE   E 3  82  ? 38.673  -41.344  -9.256   1.00 34.29  ? 87  ILE   E CG1    1 
ATOM   14037 C  CG2    . ILE   E 3  82  ? 40.415  -39.862  -8.140   1.00 37.65  ? 87  ILE   E CG2    1 
ATOM   14038 C  CD1    . ILE   E 3  82  ? 39.523  -42.542  -9.075   1.00 33.94  ? 87  ILE   E CD1    1 
ATOM   14039 N  N      . GLU   E 3  83  ? 39.992  -37.124  -10.208  1.00 46.69  ? 88  GLU   E N      1 
ATOM   14040 C  CA     . GLU   E 3  83  ? 40.721  -35.862  -10.160  1.00 46.21  ? 88  GLU   E CA     1 
ATOM   14041 C  C      . GLU   E 3  83  ? 39.813  -34.745  -9.693   1.00 48.52  ? 88  GLU   E C      1 
ATOM   14042 O  O      . GLU   E 3  83  ? 40.218  -33.899  -8.894   1.00 48.01  ? 88  GLU   E O      1 
ATOM   14043 C  CB     . GLU   E 3  83  ? 41.301  -35.521  -11.537  1.00 44.16  ? 88  GLU   E CB     1 
ATOM   14044 C  CG     . GLU   E 3  83  ? 42.141  -34.259  -11.577  1.00 48.30  ? 88  GLU   E CG     1 
ATOM   14045 C  CD     . GLU   E 3  83  ? 43.449  -34.388  -10.793  1.00 63.55  ? 88  GLU   E CD     1 
ATOM   14046 O  OE1    . GLU   E 3  83  ? 43.441  -34.190  -9.545   1.00 53.98  ? 88  GLU   E OE1    1 
ATOM   14047 O  OE2    . GLU   E 3  83  ? 44.489  -34.697  -11.432  1.00 75.13  ? 88  GLU   E OE2    1 
ATOM   14048 N  N      . GLU   E 3  84  ? 38.569  -34.737  -10.165  1.00 51.90  ? 89  GLU   E N      1 
ATOM   14049 C  CA     . GLU   E 3  84  ? 37.728  -33.587  -9.887   1.00 51.57  ? 89  GLU   E CA     1 
ATOM   14050 C  C      . GLU   E 3  84  ? 36.995  -33.732  -8.571   1.00 45.86  ? 89  GLU   E C      1 
ATOM   14051 O  O      . GLU   E 3  84  ? 36.842  -32.738  -7.857   1.00 46.99  ? 89  GLU   E O      1 
ATOM   14052 C  CB     . GLU   E 3  84  ? 36.763  -33.335  -11.047  1.00 49.34  ? 89  GLU   E CB     1 
ATOM   14053 C  CG     . GLU   E 3  84  ? 37.460  -32.579  -12.170  1.00 55.85  ? 89  GLU   E CG     1 
ATOM   14054 C  CD     . GLU   E 3  84  ? 36.562  -32.300  -13.352  1.00 69.15  ? 89  GLU   E CD     1 
ATOM   14055 O  OE1    . GLU   E 3  84  ? 35.328  -32.375  -13.165  1.00 70.63  ? 89  GLU   E OE1    1 
ATOM   14056 O  OE2    . GLU   E 3  84  ? 37.088  -31.999  -14.461  1.00 62.48  ? 89  GLU   E OE2    1 
ATOM   14057 N  N      . ASN   E 3  85  ? 36.562  -34.947  -8.211   1.00 48.33  ? 90  ASN   E N      1 
ATOM   14058 C  CA     . ASN   E 3  85  ? 36.042  -35.131  -6.863   1.00 46.42  ? 90  ASN   E CA     1 
ATOM   14059 C  C      . ASN   E 3  85  ? 37.086  -34.720  -5.844   1.00 48.96  ? 90  ASN   E C      1 
ATOM   14060 O  O      . ASN   E 3  85  ? 36.749  -34.177  -4.786   1.00 46.78  ? 90  ASN   E O      1 
ATOM   14061 C  CB     . ASN   E 3  85  ? 35.617  -36.577  -6.604   1.00 42.19  ? 90  ASN   E CB     1 
ATOM   14062 C  CG     . ASN   E 3  85  ? 34.975  -36.761  -5.194   1.00 61.83  ? 90  ASN   E CG     1 
ATOM   14063 O  OD1    . ASN   E 3  85  ? 34.084  -35.996  -4.806   1.00 64.95  ? 90  ASN   E OD1    1 
ATOM   14064 N  ND2    . ASN   E 3  85  ? 35.425  -37.765  -4.439   1.00 64.45  ? 90  ASN   E ND2    1 
ATOM   14065 N  N      . ASN   E 3  86  ? 38.361  -34.947  -6.164   1.00 50.73  ? 91  ASN   E N      1 
ATOM   14066 C  CA     . ASN   E 3  86  ? 39.446  -34.641  -5.241   1.00 49.62  ? 91  ASN   E CA     1 
ATOM   14067 C  C      . ASN   E 3  86  ? 39.747  -33.152  -5.219   1.00 51.00  ? 91  ASN   E C      1 
ATOM   14068 O  O      . ASN   E 3  86  ? 39.802  -32.540  -4.144   1.00 52.20  ? 91  ASN   E O      1 
ATOM   14069 C  CB     . ASN   E 3  86  ? 40.691  -35.437  -5.613   1.00 40.41  ? 91  ASN   E CB     1 
ATOM   14070 C  CG     . ASN   E 3  86  ? 40.647  -36.810  -5.066   1.00 41.00  ? 91  ASN   E CG     1 
ATOM   14071 O  OD1    . ASN   E 3  86  ? 39.774  -37.112  -4.257   1.00 45.33  ? 91  ASN   E OD1    1 
ATOM   14072 N  ND2    . ASN   E 3  86  ? 41.570  -37.668  -5.498   1.00 40.75  ? 91  ASN   E ND2    1 
ATOM   14073 N  N      . ASN   E 3  87  ? 39.949  -32.553  -6.395   1.00 45.55  ? 92  ASN   E N      1 
ATOM   14074 C  CA     . ASN   E 3  87  ? 40.225  -31.130  -6.427   1.00 48.86  ? 92  ASN   E CA     1 
ATOM   14075 C  C      . ASN   E 3  87  ? 39.127  -30.358  -5.696   1.00 52.49  ? 92  ASN   E C      1 
ATOM   14076 O  O      . ASN   E 3  87  ? 39.373  -29.288  -5.136   1.00 53.10  ? 92  ASN   E O      1 
ATOM   14077 C  CB     . ASN   E 3  87  ? 40.389  -30.667  -7.875   1.00 45.20  ? 92  ASN   E CB     1 
ATOM   14078 C  CG     . ASN   E 3  87  ? 40.304  -29.155  -8.006   1.00 67.48  ? 92  ASN   E CG     1 
ATOM   14079 O  OD1    . ASN   E 3  87  ? 41.325  -28.462  -8.004   1.00 75.08  ? 92  ASN   E OD1    1 
ATOM   14080 N  ND2    . ASN   E 3  87  ? 39.078  -28.631  -8.117   1.00 70.71  ? 92  ASN   E ND2    1 
ATOM   14081 N  N      . PHE   E 3  88  ? 37.922  -30.909  -5.655   1.00 51.87  ? 93  PHE   E N      1 
ATOM   14082 C  CA     . PHE   E 3  88  ? 36.815  -30.235  -5.003   1.00 48.58  ? 93  PHE   E CA     1 
ATOM   14083 C  C      . PHE   E 3  88  ? 36.891  -30.382  -3.488   1.00 49.29  ? 93  PHE   E C      1 
ATOM   14084 O  O      . PHE   E 3  88  ? 36.655  -29.412  -2.764   1.00 50.81  ? 93  PHE   E O      1 
ATOM   14085 C  CB     . PHE   E 3  88  ? 35.494  -30.783  -5.534   1.00 41.81  ? 93  PHE   E CB     1 
ATOM   14086 C  CG     . PHE   E 3  88  ? 34.304  -30.320  -4.774   1.00 44.88  ? 93  PHE   E CG     1 
ATOM   14087 C  CD1    . PHE   E 3  88  ? 33.748  -29.074  -5.033   1.00 48.83  ? 93  PHE   E CD1    1 
ATOM   14088 C  CD2    . PHE   E 3  88  ? 33.734  -31.128  -3.800   1.00 39.87  ? 93  PHE   E CD2    1 
ATOM   14089 C  CE1    . PHE   E 3  88  ? 32.642  -28.645  -4.334   1.00 44.60  ? 93  PHE   E CE1    1 
ATOM   14090 C  CE2    . PHE   E 3  88  ? 32.645  -30.705  -3.093   1.00 46.88  ? 93  PHE   E CE2    1 
ATOM   14091 C  CZ     . PHE   E 3  88  ? 32.090  -29.458  -3.358   1.00 44.78  ? 93  PHE   E CZ     1 
ATOM   14092 N  N      . ILE   E 3  89  ? 37.181  -31.578  -2.976   1.00 42.15  ? 94  ILE   E N      1 
ATOM   14093 C  CA     . ILE   E 3  89  ? 37.453  -31.674  -1.548   1.00 46.39  ? 94  ILE   E CA     1 
ATOM   14094 C  C      . ILE   E 3  89  ? 38.634  -30.779  -1.166   1.00 51.43  ? 94  ILE   E C      1 
ATOM   14095 O  O      . ILE   E 3  89  ? 38.625  -30.145  -0.100   1.00 41.76  ? 94  ILE   E O      1 
ATOM   14096 C  CB     . ILE   E 3  89  ? 37.683  -33.134  -1.117   1.00 48.23  ? 94  ILE   E CB     1 
ATOM   14097 C  CG1    . ILE   E 3  89  ? 36.387  -33.941  -1.209   1.00 44.83  ? 94  ILE   E CG1    1 
ATOM   14098 C  CG2    . ILE   E 3  89  ? 38.277  -33.194  0.280    1.00 43.06  ? 94  ILE   E CG2    1 
ATOM   14099 C  CD1    . ILE   E 3  89  ? 36.601  -35.435  -1.116   1.00 46.80  ? 94  ILE   E CD1    1 
ATOM   14100 N  N      . LYS   E 3  90  ? 39.654  -30.691  -2.037   1.00 50.70  ? 95  LYS   E N      1 
ATOM   14101 C  CA     . LYS   E 3  90  ? 40.830  -29.868  -1.753   1.00 50.32  ? 95  LYS   E CA     1 
ATOM   14102 C  C      . LYS   E 3  90  ? 40.449  -28.403  -1.584   1.00 54.56  ? 95  LYS   E C      1 
ATOM   14103 O  O      . LYS   E 3  90  ? 40.731  -27.781  -0.550   1.00 54.95  ? 95  LYS   E O      1 
ATOM   14104 C  CB     . LYS   E 3  90  ? 41.872  -30.005  -2.869   1.00 54.10  ? 95  LYS   E CB     1 
ATOM   14105 C  CG     . LYS   E 3  90  ? 43.229  -29.347  -2.510   1.00 66.05  ? 95  LYS   E CG     1 
ATOM   14106 C  CD     . LYS   E 3  90  ? 44.317  -29.390  -3.615   1.00 60.48  ? 95  LYS   E CD     1 
ATOM   14107 C  CE     . LYS   E 3  90  ? 44.469  -28.060  -4.361   1.00 71.01  ? 95  LYS   E CE     1 
ATOM   14108 N  NZ     . LYS   E 3  90  ? 45.876  -27.516  -4.357   1.00 69.90  ? 95  LYS   E NZ     1 
ATOM   14109 N  N      . MET   E 3  91  ? 39.837  -27.829  -2.617   1.00 52.34  ? 96  MET   E N      1 
ATOM   14110 C  CA     . MET   E 3  91  ? 39.583  -26.401  -2.647   1.00 45.19  ? 96  MET   E CA     1 
ATOM   14111 C  C      . MET   E 3  91  ? 38.577  -26.003  -1.590   1.00 48.83  ? 96  MET   E C      1 
ATOM   14112 O  O      . MET   E 3  91  ? 38.636  -24.883  -1.076   1.00 53.04  ? 96  MET   E O      1 
ATOM   14113 C  CB     . MET   E 3  91  ? 39.108  -26.005  -4.036   1.00 53.49  ? 96  MET   E CB     1 
ATOM   14114 C  CG     . MET   E 3  91  ? 40.240  -25.545  -4.937   1.00 64.97  ? 96  MET   E CG     1 
ATOM   14115 S  SD     . MET   E 3  91  ? 39.627  -25.003  -6.533   1.00 99.72  ? 96  MET   E SD     1 
ATOM   14116 C  CE     . MET   E 3  91  ? 40.759  -25.810  -7.678   1.00 79.98  ? 96  MET   E CE     1 
ATOM   14117 N  N      . ALA   E 3  92  ? 37.661  -26.898  -1.239   1.00 41.26  ? 97  ALA   E N      1 
ATOM   14118 C  CA     . ALA   E 3  92  ? 36.817  -26.650  -0.081   1.00 38.35  ? 97  ALA   E CA     1 
ATOM   14119 C  C      . ALA   E 3  92  ? 37.658  -26.588  1.185    1.00 48.33  ? 97  ALA   E C      1 
ATOM   14120 O  O      . ALA   E 3  92  ? 37.677  -25.569  1.885    1.00 48.41  ? 97  ALA   E O      1 
ATOM   14121 C  CB     . ALA   E 3  92  ? 35.751  -27.729  0.043    1.00 39.66  ? 97  ALA   E CB     1 
ATOM   14122 N  N      . LYS   E 3  93  ? 38.378  -27.677  1.483    1.00 48.94  ? 98  LYS   E N      1 
ATOM   14123 C  CA     . LYS   E 3  93  ? 39.267  -27.698  2.638    1.00 40.92  ? 98  LYS   E CA     1 
ATOM   14124 C  C      . LYS   E 3  93  ? 40.116  -26.441  2.703    1.00 48.60  ? 98  LYS   E C      1 
ATOM   14125 O  O      . LYS   E 3  93  ? 40.302  -25.861  3.781    1.00 56.61  ? 98  LYS   E O      1 
ATOM   14126 C  CB     . LYS   E 3  93  ? 40.150  -28.933  2.606    1.00 40.61  ? 98  LYS   E CB     1 
ATOM   14127 C  CG     . LYS   E 3  93  ? 40.328  -29.586  3.953    1.00 47.32  ? 98  LYS   E CG     1 
ATOM   14128 C  CD     . LYS   E 3  93  ? 41.620  -30.379  4.004    1.00 48.53  ? 98  LYS   E CD     1 
ATOM   14129 C  CE     . LYS   E 3  93  ? 41.787  -31.080  5.335    1.00 40.71  ? 98  LYS   E CE     1 
ATOM   14130 N  NZ     . LYS   E 3  93  ? 41.251  -32.475  5.296    1.00 57.09  ? 98  LYS   E NZ     1 
ATOM   14131 N  N      . GLU   E 3  94  ? 40.627  -25.983  1.569    1.00 46.68  ? 99  GLU   E N      1 
ATOM   14132 C  CA     . GLU   E 3  94  ? 41.487  -24.809  1.651    1.00 53.49  ? 99  GLU   E CA     1 
ATOM   14133 C  C      . GLU   E 3  94  ? 40.674  -23.544  1.855    1.00 50.76  ? 99  GLU   E C      1 
ATOM   14134 O  O      . GLU   E 3  94  ? 41.023  -22.718  2.696    1.00 53.94  ? 99  GLU   E O      1 
ATOM   14135 C  CB     . GLU   E 3  94  ? 42.381  -24.692  0.417    1.00 51.76  ? 99  GLU   E CB     1 
ATOM   14136 C  CG     . GLU   E 3  94  ? 43.618  -25.556  0.520    1.00 58.04  ? 99  GLU   E CG     1 
ATOM   14137 C  CD     . GLU   E 3  94  ? 44.243  -25.828  -0.835   1.00 73.39  ? 99  GLU   E CD     1 
ATOM   14138 O  OE1    . GLU   E 3  94  ? 43.772  -25.218  -1.830   1.00 74.95  ? 99  GLU   E OE1    1 
ATOM   14139 O  OE2    . GLU   E 3  94  ? 45.177  -26.668  -0.905   1.00 69.03  ? 99  GLU   E OE2    1 
ATOM   14140 N  N      . LYS   E 3  95  ? 39.586  -23.376  1.096    1.00 54.01  ? 100 LYS   E N      1 
ATOM   14141 C  CA     . LYS   E 3  95  ? 38.726  -22.210  1.276    1.00 50.68  ? 100 LYS   E CA     1 
ATOM   14142 C  C      . LYS   E 3  95  ? 38.289  -22.068  2.732    1.00 54.77  ? 100 LYS   E C      1 
ATOM   14143 O  O      . LYS   E 3  95  ? 38.232  -20.954  3.259    1.00 55.72  ? 100 LYS   E O      1 
ATOM   14144 C  CB     . LYS   E 3  95  ? 37.512  -22.299  0.344    1.00 47.30  ? 100 LYS   E CB     1 
ATOM   14145 C  CG     . LYS   E 3  95  ? 37.656  -21.532  -0.988   1.00 56.30  ? 100 LYS   E CG     1 
ATOM   14146 C  CD     . LYS   E 3  95  ? 36.839  -22.206  -2.129   1.00 69.29  ? 100 LYS   E CD     1 
ATOM   14147 C  CE     . LYS   E 3  95  ? 37.001  -21.557  -3.535   1.00 73.54  ? 100 LYS   E CE     1 
ATOM   14148 N  NZ     . LYS   E 3  95  ? 35.680  -21.053  -4.082   1.00 69.83  ? 100 LYS   E NZ     1 
ATOM   14149 N  N      . LEU   E 3  96  ? 37.999  -23.188  3.404    1.00 52.38  ? 101 LEU   E N      1 
ATOM   14150 C  CA     . LEU   E 3  96  ? 37.644  -23.149  4.822    1.00 52.11  ? 101 LEU   E CA     1 
ATOM   14151 C  C      . LEU   E 3  96  ? 38.791  -22.594  5.658    1.00 55.19  ? 101 LEU   E C      1 
ATOM   14152 O  O      . LEU   E 3  96  ? 38.630  -21.609  6.388    1.00 50.19  ? 101 LEU   E O      1 
ATOM   14153 C  CB     . LEU   E 3  96  ? 37.272  -24.552  5.323    1.00 48.41  ? 101 LEU   E CB     1 
ATOM   14154 C  CG     . LEU   E 3  96  ? 35.839  -24.711  5.828    1.00 50.07  ? 101 LEU   E CG     1 
ATOM   14155 C  CD1    . LEU   E 3  96  ? 35.654  -26.006  6.617    1.00 43.98  ? 101 LEU   E CD1    1 
ATOM   14156 C  CD2    . LEU   E 3  96  ? 35.391  -23.479  6.623    1.00 53.32  ? 101 LEU   E CD2    1 
ATOM   14157 N  N      . ALA   E 3  97  ? 39.961  -23.235  5.572    1.00 56.93  ? 102 ALA   E N      1 
ATOM   14158 C  CA     . ALA   E 3  97  ? 41.076  -22.853  6.427    1.00 50.02  ? 102 ALA   E CA     1 
ATOM   14159 C  C      . ALA   E 3  97  ? 41.461  -21.401  6.195    1.00 51.68  ? 102 ALA   E C      1 
ATOM   14160 O  O      . ALA   E 3  97  ? 41.696  -20.654  7.150    1.00 55.12  ? 102 ALA   E O      1 
ATOM   14161 C  CB     . ALA   E 3  97  ? 42.258  -23.781  6.191    1.00 38.99  ? 102 ALA   E CB     1 
ATOM   14162 N  N      . GLN   E 3  98  ? 41.504  -20.969  4.939    1.00 50.35  ? 103 GLN   E N      1 
ATOM   14163 C  CA     . GLN   E 3  98  ? 41.719  -19.550  4.681    1.00 58.97  ? 103 GLN   E CA     1 
ATOM   14164 C  C      . GLN   E 3  98  ? 40.707  -18.693  5.445    1.00 57.78  ? 103 GLN   E C      1 
ATOM   14165 O  O      . GLN   E 3  98  ? 41.083  -17.787  6.197    1.00 53.87  ? 103 GLN   E O      1 
ATOM   14166 C  CB     . GLN   E 3  98  ? 41.668  -19.270  3.176    1.00 56.68  ? 103 GLN   E CB     1 
ATOM   14167 C  CG     . GLN   E 3  98  ? 42.521  -20.248  2.347    1.00 72.06  ? 103 GLN   E CG     1 
ATOM   14168 C  CD     . GLN   E 3  98  ? 43.206  -19.592  1.136    1.00 81.69  ? 103 GLN   E CD     1 
ATOM   14169 O  OE1    . GLN   E 3  98  ? 43.961  -20.245  0.397    1.00 83.14  ? 103 GLN   E OE1    1 
ATOM   14170 N  NE2    . GLN   E 3  98  ? 42.936  -18.305  0.929    1.00 76.69  ? 103 GLN   E NE2    1 
ATOM   14171 N  N      . LYS   E 3  99  ? 39.416  -18.999  5.304    1.00 56.83  ? 104 LYS   E N      1 
ATOM   14172 C  CA     . LYS   E 3  99  ? 38.393  -18.206  5.980    1.00 53.40  ? 104 LYS   E CA     1 
ATOM   14173 C  C      . LYS   E 3  99  ? 38.551  -18.268  7.498    1.00 52.45  ? 104 LYS   E C      1 
ATOM   14174 O  O      . LYS   E 3  99  ? 38.591  -17.232  8.162    1.00 52.65  ? 104 LYS   E O      1 
ATOM   14175 C  CB     . LYS   E 3  99  ? 37.000  -18.670  5.553    1.00 58.65  ? 104 LYS   E CB     1 
ATOM   14176 C  CG     . LYS   E 3  99  ? 36.196  -17.644  4.750    1.00 62.16  ? 104 LYS   E CG     1 
ATOM   14177 C  CD     . LYS   E 3  99  ? 35.100  -18.318  3.911    1.00 69.92  ? 104 LYS   E CD     1 
ATOM   14178 C  CE     . LYS   E 3  99  ? 34.183  -19.219  4.757    1.00 64.68  ? 104 LYS   E CE     1 
ATOM   14179 N  NZ     . LYS   E 3  99  ? 32.904  -19.551  4.064    1.00 52.92  ? 104 LYS   E NZ     1 
ATOM   14180 N  N      . MET   E 3  100 ? 38.663  -19.470  8.071    1.00 57.18  ? 105 MET   E N      1 
ATOM   14181 C  CA     . MET   E 3  100 ? 38.815  -19.573  9.525    1.00 50.35  ? 105 MET   E CA     1 
ATOM   14182 C  C      . MET   E 3  100 ? 40.047  -18.828  10.029   1.00 55.76  ? 105 MET   E C      1 
ATOM   14183 O  O      . MET   E 3  100 ? 40.048  -18.335  11.157   1.00 53.90  ? 105 MET   E O      1 
ATOM   14184 C  CB     . MET   E 3  100 ? 38.868  -21.040  9.962    1.00 50.81  ? 105 MET   E CB     1 
ATOM   14185 C  CG     . MET   E 3  100 ? 37.522  -21.798  9.811    1.00 67.37  ? 105 MET   E CG     1 
ATOM   14186 S  SD     . MET   E 3  100 ? 35.977  -20.826  10.003   1.00 68.11  ? 105 MET   E SD     1 
ATOM   14187 C  CE     . MET   E 3  100 ? 35.267  -21.499  11.529   1.00 51.08  ? 105 MET   E CE     1 
ATOM   14188 N  N      . GLU   E 3  101 ? 41.102  -18.716  9.216    1.00 62.28  ? 106 GLU   E N      1 
ATOM   14189 C  CA     . GLU   E 3  101 ? 42.303  -18.024  9.683    1.00 59.93  ? 106 GLU   E CA     1 
ATOM   14190 C  C      . GLU   E 3  101 ? 42.164  -16.512  9.549    1.00 58.39  ? 106 GLU   E C      1 
ATOM   14191 O  O      . GLU   E 3  101 ? 42.487  -15.764  10.480   1.00 57.66  ? 106 GLU   E O      1 
ATOM   14192 C  CB     . GLU   E 3  101 ? 43.544  -18.520  8.933    1.00 56.18  ? 106 GLU   E CB     1 
ATOM   14193 C  CG     . GLU   E 3  101 ? 44.887  -18.220  9.637    1.00 65.97  ? 106 GLU   E CG     1 
ATOM   14194 C  CD     . GLU   E 3  101 ? 44.975  -18.707  11.106   1.00 71.70  ? 106 GLU   E CD     1 
ATOM   14195 O  OE1    . GLU   E 3  101 ? 44.186  -19.592  11.531   1.00 68.51  ? 106 GLU   E OE1    1 
ATOM   14196 O  OE2    . GLU   E 3  101 ? 45.844  -18.182  11.844   1.00 75.92  ? 106 GLU   E OE2    1 
ATOM   14197 N  N      . SER   E 3  102 ? 41.675  -16.040  8.405    1.00 55.30  ? 107 SER   E N      1 
ATOM   14198 C  CA     . SER   E 3  102 ? 41.432  -14.611  8.261    1.00 53.59  ? 107 SER   E CA     1 
ATOM   14199 C  C      . SER   E 3  102 ? 40.422  -14.109  9.302    1.00 56.16  ? 107 SER   E C      1 
ATOM   14200 O  O      . SER   E 3  102 ? 40.426  -12.924  9.661    1.00 53.79  ? 107 SER   E O      1 
ATOM   14201 C  CB     . SER   E 3  102 ? 40.989  -14.330  6.815    1.00 48.96  ? 107 SER   E CB     1 
ATOM   14202 O  OG     . SER   E 3  102 ? 40.093  -13.237  6.696    1.00 60.33  ? 107 SER   E OG     1 
ATOM   14203 N  N      . ASN   E 3  103 ? 39.604  -15.004  9.851    1.00 57.46  ? 108 ASN   E N      1 
ATOM   14204 C  CA     . ASN   E 3  103 ? 38.590  -14.610  10.816   1.00 51.11  ? 108 ASN   E CA     1 
ATOM   14205 C  C      . ASN   E 3  103 ? 39.150  -14.468  12.220   1.00 54.47  ? 108 ASN   E C      1 
ATOM   14206 O  O      . ASN   E 3  103 ? 38.686  -13.611  12.972   1.00 54.24  ? 108 ASN   E O      1 
ATOM   14207 C  CB     . ASN   E 3  103 ? 37.469  -15.635  10.848   1.00 53.87  ? 108 ASN   E CB     1 
ATOM   14208 C  CG     . ASN   E 3  103 ? 36.135  -14.994  10.923   1.00 59.09  ? 108 ASN   E CG     1 
ATOM   14209 O  OD1    . ASN   E 3  103 ? 35.654  -14.433  9.932    1.00 55.59  ? 108 ASN   E OD1    1 
ATOM   14210 N  ND2    . ASN   E 3  103 ? 35.531  -15.016  12.117   1.00 63.06  ? 108 ASN   E ND2    1 
ATOM   14211 N  N      . LYS   E 3  104 ? 40.098  -15.331  12.614   1.00 56.79  ? 109 LYS   E N      1 
ATOM   14212 C  CA     . LYS   E 3  104 ? 40.735  -15.172  13.917   1.00 56.53  ? 109 LYS   E CA     1 
ATOM   14213 C  C      . LYS   E 3  104 ? 41.547  -13.880  13.957   1.00 55.86  ? 109 LYS   E C      1 
ATOM   14214 O  O      . LYS   E 3  104 ? 41.472  -13.121  14.927   1.00 59.71  ? 109 LYS   E O      1 
ATOM   14215 C  CB     . LYS   E 3  104 ? 41.598  -16.401  14.241   1.00 55.23  ? 109 LYS   E CB     1 
ATOM   14216 C  CG     . LYS   E 3  104 ? 41.858  -16.649  15.741   1.00 58.81  ? 109 LYS   E CG     1 
ATOM   14217 C  CD     . LYS   E 3  104 ? 42.471  -18.045  16.015   1.00 66.52  ? 109 LYS   E CD     1 
ATOM   14218 C  CE     . LYS   E 3  104 ? 43.957  -18.129  15.643   1.00 65.68  ? 109 LYS   E CE     1 
ATOM   14219 N  NZ     . LYS   E 3  104 ? 44.461  -19.523  15.478   1.00 70.35  ? 109 LYS   E NZ     1 
ATOM   14220 N  N      . GLU   E 3  105 ? 42.279  -13.578  12.890   1.00 53.50  ? 110 GLU   E N      1 
ATOM   14221 C  CA     . GLU   E 3  105 ? 43.039  -12.335  12.864   1.00 56.00  ? 110 GLU   E CA     1 
ATOM   14222 C  C      . GLU   E 3  105 ? 42.121  -11.120  12.906   1.00 56.09  ? 110 GLU   E C      1 
ATOM   14223 O  O      . GLU   E 3  105 ? 42.376  -10.170  13.652   1.00 60.26  ? 110 GLU   E O      1 
ATOM   14224 C  CB     . GLU   E 3  105 ? 43.925  -12.304  11.633   1.00 53.76  ? 110 GLU   E CB     1 
ATOM   14225 C  CG     . GLU   E 3  105 ? 44.590  -13.641  11.419   1.00 66.81  ? 110 GLU   E CG     1 
ATOM   14226 C  CD     . GLU   E 3  105 ? 45.478  -13.689  10.196   1.00 81.49  ? 110 GLU   E CD     1 
ATOM   14227 O  OE1    . GLU   E 3  105 ? 45.310  -12.816  9.303    1.00 81.98  ? 110 GLU   E OE1    1 
ATOM   14228 O  OE2    . GLU   E 3  105 ? 46.342  -14.603  10.138   1.00 79.84  ? 110 GLU   E OE2    1 
ATOM   14229 N  N      . ASN   E 3  106 ? 41.044  -11.131  12.125   1.00 56.13  ? 111 ASN   E N      1 
ATOM   14230 C  CA     . ASN   E 3  106 ? 40.136  -9.990   12.112   1.00 53.55  ? 111 ASN   E CA     1 
ATOM   14231 C  C      . ASN   E 3  106 ? 39.486  -9.780   13.474   1.00 54.24  ? 111 ASN   E C      1 
ATOM   14232 O  O      . ASN   E 3  106 ? 39.549  -8.684   14.041   1.00 52.37  ? 111 ASN   E O      1 
ATOM   14233 C  CB     . ASN   E 3  106 ? 39.084  -10.184  11.028   1.00 50.40  ? 111 ASN   E CB     1 
ATOM   14234 C  CG     . ASN   E 3  106 ? 39.650  -9.958   9.661    1.00 45.78  ? 111 ASN   E CG     1 
ATOM   14235 O  OD1    . ASN   E 3  106 ? 40.789  -9.525   9.543    1.00 54.22  ? 111 ASN   E OD1    1 
ATOM   14236 N  ND2    . ASN   E 3  106 ? 38.874  -10.245  8.618    1.00 43.46  ? 111 ASN   E ND2    1 
ATOM   14237 N  N      . ARG   E 3  107 ? 38.855  -10.823  14.017   1.00 51.02  ? 112 ARG   E N      1 
ATOM   14238 C  CA     . ARG   E 3  107 ? 38.196  -10.680  15.309   1.00 52.28  ? 112 ARG   E CA     1 
ATOM   14239 C  C      . ARG   E 3  107 ? 39.189  -10.270  16.391   1.00 53.41  ? 112 ARG   E C      1 
ATOM   14240 O  O      . ARG   E 3  107 ? 38.904  -9.374   17.197   1.00 53.38  ? 112 ARG   E O      1 
ATOM   14241 C  CB     . ARG   E 3  107 ? 37.475  -11.977  15.685   1.00 49.79  ? 112 ARG   E CB     1 
ATOM   14242 C  CG     . ARG   E 3  107 ? 36.747  -11.891  17.021   1.00 51.83  ? 112 ARG   E CG     1 
ATOM   14243 C  CD     . ARG   E 3  107 ? 35.800  -13.056  17.257   1.00 47.80  ? 112 ARG   E CD     1 
ATOM   14244 N  NE     . ARG   E 3  107 ? 34.925  -12.795  18.395   1.00 52.84  ? 112 ARG   E NE     1 
ATOM   14245 C  CZ     . ARG   E 3  107 ? 35.232  -13.087  19.653   1.00 55.75  ? 112 ARG   E CZ     1 
ATOM   14246 N  NH1    . ARG   E 3  107 ? 36.367  -13.692  19.964   1.00 57.14  ? 112 ARG   E NH1    1 
ATOM   14247 N  NH2    . ARG   E 3  107 ? 34.385  -12.758  20.623   1.00 55.54  ? 112 ARG   E NH2    1 
ATOM   14248 N  N      . GLU   E 3  108 ? 40.368  -10.897  16.415   1.00 58.05  ? 113 GLU   E N      1 
ATOM   14249 C  CA     . GLU   E 3  108 ? 41.406  -10.487  17.359   1.00 58.34  ? 113 GLU   E CA     1 
ATOM   14250 C  C      . GLU   E 3  108 ? 41.818  -9.040   17.116   1.00 53.99  ? 113 GLU   E C      1 
ATOM   14251 O  O      . GLU   E 3  108 ? 41.772  -8.206   18.027   1.00 57.51  ? 113 GLU   E O      1 
ATOM   14252 C  CB     . GLU   E 3  108 ? 42.616  -11.426  17.273   1.00 57.08  ? 113 GLU   E CB     1 
ATOM   14253 C  CG     . GLU   E 3  108 ? 42.427  -12.753  18.025   1.00 62.10  ? 113 GLU   E CG     1 
ATOM   14254 C  CD     . GLU   E 3  108 ? 43.555  -13.756  17.781   1.00 69.10  ? 113 GLU   E CD     1 
ATOM   14255 O  OE1    . GLU   E 3  108 ? 44.478  -13.452  16.991   1.00 71.99  ? 113 GLU   E OE1    1 
ATOM   14256 O  OE2    . GLU   E 3  108 ? 43.501  -14.868  18.359   1.00 74.10  ? 113 GLU   E OE2    1 
ATOM   14257 N  N      . ALA   E 3  109 ? 42.207  -8.715   15.884   1.00 47.72  ? 114 ALA   E N      1 
ATOM   14258 C  CA     . ALA   E 3  109 ? 42.573  -7.337   15.582   1.00 50.65  ? 114 ALA   E CA     1 
ATOM   14259 C  C      . ALA   E 3  109 ? 41.549  -6.360   16.138   1.00 56.25  ? 114 ALA   E C      1 
ATOM   14260 O  O      . ALA   E 3  109 ? 41.916  -5.289   16.634   1.00 56.76  ? 114 ALA   E O      1 
ATOM   14261 C  CB     . ALA   E 3  109 ? 42.726  -7.150   14.076   1.00 50.30  ? 114 ALA   E CB     1 
ATOM   14262 N  N      . HIS   E 3  110 ? 40.259  -6.723   16.088   1.00 52.47  ? 115 HIS   E N      1 
ATOM   14263 C  CA     . HIS   E 3  110 ? 39.214  -5.845   16.607   1.00 53.30  ? 115 HIS   E CA     1 
ATOM   14264 C  C      . HIS   E 3  110 ? 39.229  -5.813   18.132   1.00 58.57  ? 115 HIS   E C      1 
ATOM   14265 O  O      . HIS   E 3  110 ? 39.194  -4.738   18.740   1.00 58.58  ? 115 HIS   E O      1 
ATOM   14266 C  CB     . HIS   E 3  110 ? 37.838  -6.276   16.094   1.00 56.39  ? 115 HIS   E CB     1 
ATOM   14267 C  CG     . HIS   E 3  110 ? 37.488  -5.706   14.750   1.00 69.66  ? 115 HIS   E CG     1 
ATOM   14268 N  ND1    . HIS   E 3  110 ? 38.015  -6.194   13.569   1.00 66.46  ? 115 HIS   E ND1    1 
ATOM   14269 C  CD2    . HIS   E 3  110 ? 36.690  -4.666   14.401   1.00 76.82  ? 115 HIS   E CD2    1 
ATOM   14270 C  CE1    . HIS   E 3  110 ? 37.544  -5.493   12.551   1.00 64.79  ? 115 HIS   E CE1    1 
ATOM   14271 N  NE2    . HIS   E 3  110 ? 36.740  -4.557   13.028   1.00 73.96  ? 115 HIS   E NE2    1 
ATOM   14272 N  N      . LEU   E 3  111 ? 39.277  -6.975   18.776   1.00 55.49  ? 116 LEU   E N      1 
ATOM   14273 C  CA     . LEU   E 3  111 ? 39.359  -6.956   20.232   1.00 55.65  ? 116 LEU   E CA     1 
ATOM   14274 C  C      . LEU   E 3  111 ? 40.618  -6.242   20.705   1.00 58.61  ? 116 LEU   E C      1 
ATOM   14275 O  O      . LEU   E 3  111 ? 40.605  -5.604   21.761   1.00 61.23  ? 116 LEU   E O      1 
ATOM   14276 C  CB     . LEU   E 3  111 ? 39.284  -8.379   20.789   1.00 51.34  ? 116 LEU   E CB     1 
ATOM   14277 C  CG     . LEU   E 3  111 ? 37.843  -8.859   20.955   1.00 58.62  ? 116 LEU   E CG     1 
ATOM   14278 C  CD1    . LEU   E 3  111 ? 37.753  -10.228  21.600   1.00 63.34  ? 116 LEU   E CD1    1 
ATOM   14279 C  CD2    . LEU   E 3  111 ? 37.034  -7.843   21.761   1.00 58.41  ? 116 LEU   E CD2    1 
ATOM   14280 N  N      . ALA   E 3  112 ? 41.710  -6.310   19.936   1.00 59.36  ? 117 ALA   E N      1 
ATOM   14281 C  CA     . ALA   E 3  112 ? 42.923  -5.609   20.346   1.00 56.28  ? 117 ALA   E CA     1 
ATOM   14282 C  C      . ALA   E 3  112 ? 42.738  -4.106   20.250   1.00 60.10  ? 117 ALA   E C      1 
ATOM   14283 O  O      . ALA   E 3  112 ? 43.196  -3.362   21.120   1.00 63.00  ? 117 ALA   E O      1 
ATOM   14284 C  CB     . ALA   E 3  112 ? 44.113  -6.044   19.501   1.00 50.78  ? 117 ALA   E CB     1 
ATOM   14285 N  N      . ALA   E 3  113 ? 42.059  -3.645   19.201   1.00 58.71  ? 118 ALA   E N      1 
ATOM   14286 C  CA     . ALA   E 3  113 ? 41.840  -2.216   19.047   1.00 53.47  ? 118 ALA   E CA     1 
ATOM   14287 C  C      . ALA   E 3  113 ? 41.045  -1.671   20.213   1.00 55.83  ? 118 ALA   E C      1 
ATOM   14288 O  O      . ALA   E 3  113 ? 41.312  -0.564   20.685   1.00 64.82  ? 118 ALA   E O      1 
ATOM   14289 C  CB     . ALA   E 3  113 ? 41.128  -1.932   17.726   1.00 46.78  ? 118 ALA   E CB     1 
ATOM   14290 N  N      . MET   E 3  114 ? 40.069  -2.446   20.696   1.00 59.10  ? 119 MET   E N      1 
ATOM   14291 C  CA     . MET   E 3  114 ? 39.201  -2.008   21.787   1.00 57.91  ? 119 MET   E CA     1 
ATOM   14292 C  C      . MET   E 3  114 ? 39.989  -1.817   23.068   1.00 63.81  ? 119 MET   E C      1 
ATOM   14293 O  O      . MET   E 3  114 ? 39.820  -0.813   23.770   1.00 63.10  ? 119 MET   E O      1 
ATOM   14294 C  CB     . MET   E 3  114 ? 38.099  -3.034   22.010   1.00 54.55  ? 119 MET   E CB     1 
ATOM   14295 C  CG     . MET   E 3  114 ? 36.973  -2.611   22.948   1.00 65.09  ? 119 MET   E CG     1 
ATOM   14296 S  SD     . MET   E 3  114 ? 35.814  -3.999   23.241   1.00 80.76  ? 119 MET   E SD     1 
ATOM   14297 C  CE     . MET   E 3  114 ? 35.704  -4.695   21.584   1.00 56.87  ? 119 MET   E CE     1 
ATOM   14298 N  N      . LEU   E 3  115 ? 40.842  -2.795   23.392   1.00 62.31  ? 120 LEU   E N      1 
ATOM   14299 C  CA     . LEU   E 3  115 ? 41.697  -2.724   24.572   1.00 62.27  ? 120 LEU   E CA     1 
ATOM   14300 C  C      . LEU   E 3  115 ? 42.718  -1.595   24.458   1.00 61.76  ? 120 LEU   E C      1 
ATOM   14301 O  O      . LEU   E 3  115 ? 42.862  -0.784   25.378   1.00 65.61  ? 120 LEU   E O      1 
ATOM   14302 C  CB     . LEU   E 3  115 ? 42.386  -4.075   24.779   1.00 60.32  ? 120 LEU   E CB     1 
ATOM   14303 C  CG     . LEU   E 3  115 ? 41.420  -5.253   24.971   1.00 57.69  ? 120 LEU   E CG     1 
ATOM   14304 C  CD1    . LEU   E 3  115 ? 42.157  -6.566   24.914   1.00 67.63  ? 120 LEU   E CD1    1 
ATOM   14305 C  CD2    . LEU   E 3  115 ? 40.690  -5.147   26.286   1.00 57.08  ? 120 LEU   E CD2    1 
ATOM   14306 N  N      . GLU   E 3  116 ? 43.433  -1.513   23.339   1.00 65.26  ? 121 GLU   E N      1 
ATOM   14307 C  CA     . GLU   E 3  116 ? 44.436  -0.459   23.204   1.00 71.63  ? 121 GLU   E CA     1 
ATOM   14308 C  C      . GLU   E 3  116 ? 43.856  0.906    23.532   1.00 71.06  ? 121 GLU   E C      1 
ATOM   14309 O  O      . GLU   E 3  116 ? 44.553  1.765    24.082   1.00 80.06  ? 121 GLU   E O      1 
ATOM   14310 C  CB     . GLU   E 3  116 ? 45.037  -0.438   21.799   1.00 69.69  ? 121 GLU   E CB     1 
ATOM   14311 C  CG     . GLU   E 3  116 ? 46.422  0.193    21.746   1.00 79.26  ? 121 GLU   E CG     1 
ATOM   14312 C  CD     . GLU   E 3  116 ? 46.769  0.752    20.372   1.00 98.20  ? 121 GLU   E CD     1 
ATOM   14313 O  OE1    . GLU   E 3  116 ? 45.889  0.703    19.482   1.00 101.79 ? 121 GLU   E OE1    1 
ATOM   14314 O  OE2    . GLU   E 3  116 ? 47.921  1.222    20.174   1.00 92.68  ? 121 GLU   E OE2    1 
ATOM   14315 N  N      . ARG   E 3  117 ? 42.586  1.129    23.216   1.00 64.89  ? 122 ARG   E N      1 
ATOM   14316 C  CA     . ARG   E 3  117 ? 42.011  2.428    23.538   1.00 64.56  ? 122 ARG   E CA     1 
ATOM   14317 C  C      . ARG   E 3  117 ? 41.413  2.456    24.934   1.00 66.26  ? 122 ARG   E C      1 
ATOM   14318 O  O      . ARG   E 3  117 ? 41.409  3.510    25.571   1.00 79.31  ? 122 ARG   E O      1 
ATOM   14319 C  CB     . ARG   E 3  117 ? 40.975  2.836    22.483   1.00 64.31  ? 122 ARG   E CB     1 
ATOM   14320 C  CG     . ARG   E 3  117 ? 39.577  2.310    22.698   1.00 73.79  ? 122 ARG   E CG     1 
ATOM   14321 C  CD     . ARG   E 3  117 ? 38.660  2.667    21.525   1.00 73.03  ? 122 ARG   E CD     1 
ATOM   14322 N  NE     . ARG   E 3  117 ? 39.012  1.956    20.296   1.00 79.37  ? 122 ARG   E NE     1 
ATOM   14323 C  CZ     . ARG   E 3  117 ? 38.361  0.895    19.820   1.00 74.34  ? 122 ARG   E CZ     1 
ATOM   14324 N  NH1    . ARG   E 3  117 ? 37.315  0.383    20.451   1.00 73.40  ? 122 ARG   E NH1    1 
ATOM   14325 N  NH2    . ARG   E 3  117 ? 38.771  0.334    18.684   1.00 60.61  ? 122 ARG   E NH2    1 
ATOM   14326 N  N      . LEU   E 3  118 ? 40.947  1.322    25.448   1.00 62.12  ? 123 LEU   E N      1 
ATOM   14327 C  CA     . LEU   E 3  118 ? 40.525  1.279    26.841   1.00 64.03  ? 123 LEU   E CA     1 
ATOM   14328 C  C      . LEU   E 3  118 ? 41.705  1.496    27.784   1.00 71.89  ? 123 LEU   E C      1 
ATOM   14329 O  O      . LEU   E 3  118 ? 41.527  2.004    28.900   1.00 73.30  ? 123 LEU   E O      1 
ATOM   14330 C  CB     . LEU   E 3  118 ? 39.844  -0.055   27.136   1.00 59.76  ? 123 LEU   E CB     1 
ATOM   14331 C  CG     . LEU   E 3  118 ? 38.331  -0.114   26.960   1.00 62.00  ? 123 LEU   E CG     1 
ATOM   14332 C  CD1    . LEU   E 3  118 ? 37.789  -1.412   27.547   1.00 65.03  ? 123 LEU   E CD1    1 
ATOM   14333 C  CD2    . LEU   E 3  118 ? 37.663  1.091    27.598   1.00 64.30  ? 123 LEU   E CD2    1 
ATOM   14334 N  N      . GLN   E 3  119 ? 42.913  1.117    27.360   1.00 70.63  ? 124 GLN   E N      1 
ATOM   14335 C  CA     . GLN   E 3  119 ? 44.095  1.306    28.191   1.00 73.85  ? 124 GLN   E CA     1 
ATOM   14336 C  C      . GLN   E 3  119 ? 44.705  2.686    28.011   1.00 75.25  ? 124 GLN   E C      1 
ATOM   14337 O  O      . GLN   E 3  119 ? 45.081  3.330    28.996   1.00 77.62  ? 124 GLN   E O      1 
ATOM   14338 C  CB     . GLN   E 3  119 ? 45.135  0.229    27.895   1.00 68.53  ? 124 GLN   E CB     1 
ATOM   14339 C  CG     . GLN   E 3  119 ? 44.676  -1.159   28.310   1.00 69.69  ? 124 GLN   E CG     1 
ATOM   14340 C  CD     . GLN   E 3  119 ? 45.278  -2.254   27.444   1.00 70.33  ? 124 GLN   E CD     1 
ATOM   14341 O  OE1    . GLN   E 3  119 ? 45.907  -1.979   26.415   1.00 74.07  ? 124 GLN   E OE1    1 
ATOM   14342 N  NE2    . GLN   E 3  119 ? 45.067  -3.501   27.842   1.00 63.72  ? 124 GLN   E NE2    1 
ATOM   14343 N  N      . GLU   E 3  120 ? 44.799  3.167    26.774   1.00 72.43  ? 125 GLU   E N      1 
ATOM   14344 C  CA     . GLU   E 3  120 ? 45.131  4.571    26.593   1.00 76.61  ? 125 GLU   E CA     1 
ATOM   14345 C  C      . GLU   E 3  120 ? 44.223  5.455    27.451   1.00 74.33  ? 125 GLU   E C      1 
ATOM   14346 O  O      . GLU   E 3  120 ? 44.616  6.559    27.835   1.00 75.18  ? 125 GLU   E O      1 
ATOM   14347 C  CB     . GLU   E 3  120 ? 45.061  4.924    25.100   1.00 75.03  ? 125 GLU   E CB     1 
ATOM   14348 C  CG     . GLU   E 3  120 ? 44.941  6.411    24.779   1.00 82.91  ? 125 GLU   E CG     1 
ATOM   14349 C  CD     . GLU   E 3  120 ? 45.984  7.281    25.483   1.00 91.62  ? 125 GLU   E CD     1 
ATOM   14350 O  OE1    . GLU   E 3  120 ? 46.759  6.747    26.312   1.00 91.35  ? 125 GLU   E OE1    1 
ATOM   14351 O  OE2    . GLU   E 3  120 ? 46.010  8.510    25.218   1.00 89.44  ? 125 GLU   E OE2    1 
ATOM   14352 N  N      . LYS   E 3  121 ? 43.022  4.972    27.790   1.00 77.86  ? 126 LYS   E N      1 
ATOM   14353 C  CA     . LYS   E 3  121 ? 42.173  5.654    28.766   1.00 74.48  ? 126 LYS   E CA     1 
ATOM   14354 C  C      . LYS   E 3  121 ? 42.760  5.579    30.172   1.00 77.71  ? 126 LYS   E C      1 
ATOM   14355 O  O      . LYS   E 3  121 ? 42.645  6.536    30.945   1.00 81.91  ? 126 LYS   E O      1 
ATOM   14356 C  CB     . LYS   E 3  121 ? 40.770  5.045    28.750   1.00 72.60  ? 126 LYS   E CB     1 
ATOM   14357 C  CG     . LYS   E 3  121 ? 39.678  5.957    28.228   1.00 75.81  ? 126 LYS   E CG     1 
ATOM   14358 C  CD     . LYS   E 3  121 ? 38.325  5.578    28.844   1.00 75.97  ? 126 LYS   E CD     1 
ATOM   14359 C  CE     . LYS   E 3  121 ? 37.288  6.692    28.696   1.00 70.48  ? 126 LYS   E CE     1 
ATOM   14360 N  NZ     . LYS   E 3  121 ? 37.349  7.665    29.836   1.00 75.89  ? 126 LYS   E NZ     1 
ATOM   14361 N  N      . ASP   E 3  122 ? 43.374  4.446    30.530   1.00 74.46  ? 127 ASP   E N      1 
ATOM   14362 C  CA     . ASP   E 3  122 ? 43.993  4.319    31.848   1.00 77.09  ? 127 ASP   E CA     1 
ATOM   14363 C  C      . ASP   E 3  122 ? 45.235  5.198    31.964   1.00 75.57  ? 127 ASP   E C      1 
ATOM   14364 O  O      . ASP   E 3  122 ? 45.518  5.749    33.030   1.00 73.76  ? 127 ASP   E O      1 
ATOM   14365 C  CB     . ASP   E 3  122 ? 44.330  2.849    32.117   1.00 76.35  ? 127 ASP   E CB     1 
ATOM   14366 C  CG     . ASP   E 3  122 ? 43.099  2.031    32.500   1.00 87.22  ? 127 ASP   E CG     1 
ATOM   14367 O  OD1    . ASP   E 3  122 ? 43.084  0.793    32.265   1.00 77.68  ? 127 ASP   E OD1    1 
ATOM   14368 O  OD2    . ASP   E 3  122 ? 42.142  2.637    33.040   1.00 91.37  ? 127 ASP   E OD2    1 
ATOM   14369 N  N      . LYS   E 3  123 ? 45.991  5.330    30.875   1.00 74.98  ? 128 LYS   E N      1 
ATOM   14370 C  CA     . LYS   E 3  123 ? 47.138  6.225    30.869   1.00 71.52  ? 128 LYS   E CA     1 
ATOM   14371 C  C      . LYS   E 3  123 ? 46.704  7.672    31.072   1.00 81.47  ? 128 LYS   E C      1 
ATOM   14372 O  O      . LYS   E 3  123 ? 47.403  8.446    31.738   1.00 91.06  ? 128 LYS   E O      1 
ATOM   14373 C  CB     . LYS   E 3  123 ? 47.908  6.064    29.559   1.00 74.98  ? 128 LYS   E CB     1 
ATOM   14374 C  CG     . LYS   E 3  123 ? 49.167  6.908    29.448   1.00 85.71  ? 128 LYS   E CG     1 
ATOM   14375 C  CD     . LYS   E 3  123 ? 49.837  7.074    30.812   1.00 91.80  ? 128 LYS   E CD     1 
ATOM   14376 C  CE     . LYS   E 3  123 ? 50.901  8.153    30.777   1.00 92.76  ? 128 LYS   E CE     1 
ATOM   14377 N  NZ     . LYS   E 3  123 ? 52.119  7.648    30.097   1.00 101.30 ? 128 LYS   E NZ     1 
ATOM   14378 N  N      . HIS   E 3  124 ? 45.555  8.060    30.505   1.00 76.66  ? 129 HIS   E N      1 
ATOM   14379 C  CA     . HIS   E 3  124 ? 45.031  9.410    30.695   1.00 75.19  ? 129 HIS   E CA     1 
ATOM   14380 C  C      . HIS   E 3  124 ? 44.481  9.626    32.100   1.00 77.05  ? 129 HIS   E C      1 
ATOM   14381 O  O      . HIS   E 3  124 ? 44.402  10.768   32.553   1.00 72.02  ? 129 HIS   E O      1 
ATOM   14382 C  CB     . HIS   E 3  124 ? 43.947  9.697    29.654   1.00 75.59  ? 129 HIS   E CB     1 
ATOM   14383 C  CG     . HIS   E 3  124 ? 43.114  10.917   29.943   1.00 80.06  ? 129 HIS   E CG     1 
ATOM   14384 N  ND1    . HIS   E 3  124 ? 43.318  12.129   29.311   1.00 77.88  ? 129 HIS   E ND1    1 
ATOM   14385 C  CD2    . HIS   E 3  124 ? 42.057  11.100   30.772   1.00 71.32  ? 129 HIS   E CD2    1 
ATOM   14386 C  CE1    . HIS   E 3  124 ? 42.428  13.005   29.744   1.00 67.98  ? 129 HIS   E CE1    1 
ATOM   14387 N  NE2    . HIS   E 3  124 ? 41.652  12.407   30.631   1.00 68.40  ? 129 HIS   E NE2    1 
ATOM   14388 N  N      . ALA   E 3  125 ? 44.083  8.565    32.794   1.00 77.17  ? 130 ALA   E N      1 
ATOM   14389 C  CA     . ALA   E 3  125 ? 43.704  8.712    34.189   1.00 76.26  ? 130 ALA   E CA     1 
ATOM   14390 C  C      . ALA   E 3  125 ? 44.916  8.793    35.104   1.00 85.00  ? 130 ALA   E C      1 
ATOM   14391 O  O      . ALA   E 3  125 ? 44.796  9.309    36.222   1.00 85.30  ? 130 ALA   E O      1 
ATOM   14392 C  CB     . ALA   E 3  125 ? 42.803  7.558    34.626   1.00 81.86  ? 130 ALA   E CB     1 
ATOM   14393 N  N      . GLU   E 3  126 ? 46.074  8.281    34.666   1.00 86.12  ? 131 GLU   E N      1 
ATOM   14394 C  CA     . GLU   E 3  126 ? 47.318  8.588    35.366   1.00 87.50  ? 131 GLU   E CA     1 
ATOM   14395 C  C      . GLU   E 3  126 ? 47.678  10.055   35.180   1.00 87.63  ? 131 GLU   E C      1 
ATOM   14396 O  O      . GLU   E 3  126 ? 47.853  10.793   36.156   1.00 90.14  ? 131 GLU   E O      1 
ATOM   14397 C  CB     . GLU   E 3  126 ? 48.467  7.696    34.877   1.00 82.25  ? 131 GLU   E CB     1 
ATOM   14398 C  CG     . GLU   E 3  126 ? 48.283  6.193    35.046   1.00 83.42  ? 131 GLU   E CG     1 
ATOM   14399 C  CD     . GLU   E 3  126 ? 47.687  5.764    36.381   1.00 83.54  ? 131 GLU   E CD     1 
ATOM   14400 O  OE1    . GLU   E 3  126 ? 47.074  6.584    37.091   1.00 82.37  ? 131 GLU   E OE1    1 
ATOM   14401 O  OE2    . GLU   E 3  126 ? 47.831  4.572    36.722   1.00 87.98  ? 131 GLU   E OE2    1 
ATOM   14402 N  N      . GLU   E 3  127 ? 47.774  10.499   33.928   1.00 83.27  ? 132 GLU   E N      1 
ATOM   14403 C  CA     . GLU   E 3  127 ? 48.129  11.886   33.667   1.00 88.93  ? 132 GLU   E CA     1 
ATOM   14404 C  C      . GLU   E 3  127 ? 47.222  12.851   34.416   1.00 91.43  ? 132 GLU   E C      1 
ATOM   14405 O  O      . GLU   E 3  127 ? 47.679  13.891   34.901   1.00 98.26  ? 132 GLU   E O      1 
ATOM   14406 C  CB     . GLU   E 3  127 ? 48.077  12.160   32.173   1.00 89.32  ? 132 GLU   E CB     1 
ATOM   14407 C  CG     . GLU   E 3  127 ? 49.186  11.479   31.430   1.00 97.63  ? 132 GLU   E CG     1 
ATOM   14408 C  CD     . GLU   E 3  127 ? 49.332  12.021   30.033   1.00 113.25 ? 132 GLU   E CD     1 
ATOM   14409 O  OE1    . GLU   E 3  127 ? 48.683  13.051   29.727   1.00 109.92 ? 132 GLU   E OE1    1 
ATOM   14410 O  OE2    . GLU   E 3  127 ? 50.095  11.418   29.246   1.00 116.90 ? 132 GLU   E OE2    1 
ATOM   14411 N  N      . VAL   E 3  128 ? 45.932  12.528   34.522   1.00 91.69  ? 133 VAL   E N      1 
ATOM   14412 C  CA     . VAL   E 3  128 ? 44.998  13.449   35.165   1.00 88.66  ? 133 VAL   E CA     1 
ATOM   14413 C  C      . VAL   E 3  128 ? 45.253  13.504   36.666   1.00 89.50  ? 133 VAL   E C      1 
ATOM   14414 O  O      . VAL   E 3  128 ? 45.264  14.586   37.264   1.00 91.34  ? 133 VAL   E O      1 
ATOM   14415 C  CB     . VAL   E 3  128 ? 43.543  13.054   34.837   1.00 80.77  ? 133 VAL   E CB     1 
ATOM   14416 C  CG1    . VAL   E 3  128 ? 43.297  11.609   35.217   1.00 84.87  ? 133 VAL   E CG1    1 
ATOM   14417 C  CG2    . VAL   E 3  128 ? 42.546  13.965   35.553   1.00 78.27  ? 133 VAL   E CG2    1 
ATOM   14418 N  N      . ARG   E 3  129 ? 45.476  12.343   37.295   1.00 85.89  ? 134 ARG   E N      1 
ATOM   14419 C  CA     . ARG   E 3  129 ? 45.752  12.303   38.730   1.00 85.50  ? 134 ARG   E CA     1 
ATOM   14420 C  C      . ARG   E 3  129 ? 47.113  12.915   39.054   1.00 92.64  ? 134 ARG   E C      1 
ATOM   14421 O  O      . ARG   E 3  129 ? 47.274  13.575   40.090   1.00 93.20  ? 134 ARG   E O      1 
ATOM   14422 C  CB     . ARG   E 3  129 ? 45.682  10.860   39.230   1.00 82.58  ? 134 ARG   E CB     1 
ATOM   14423 C  CG     . ARG   E 3  129 ? 44.290  10.366   39.582   1.00 77.61  ? 134 ARG   E CG     1 
ATOM   14424 C  CD     . ARG   E 3  129 ? 44.352  8.976    40.205   1.00 79.80  ? 134 ARG   E CD     1 
ATOM   14425 N  NE     . ARG   E 3  129 ? 44.851  7.978    39.267   1.00 82.43  ? 134 ARG   E NE     1 
ATOM   14426 C  CZ     . ARG   E 3  129 ? 44.088  7.224    38.489   1.00 79.94  ? 134 ARG   E CZ     1 
ATOM   14427 N  NH1    . ARG   E 3  129 ? 42.769  7.292    38.539   1.00 74.98  ? 134 ARG   E NH1    1 
ATOM   14428 N  NH2    . ARG   E 3  129 ? 44.665  6.380    37.640   1.00 87.14  ? 134 ARG   E NH2    1 
ATOM   14429 N  N      . LYS   E 3  130 ? 48.107  12.693   38.189   1.00 91.70  ? 135 LYS   E N      1 
ATOM   14430 C  CA     . LYS   E 3  130 ? 49.403  13.333   38.351   1.00 91.25  ? 135 LYS   E CA     1 
ATOM   14431 C  C      . LYS   E 3  130 ? 49.347  14.842   38.138   1.00 94.91  ? 135 LYS   E C      1 
ATOM   14432 O  O      . LYS   E 3  130 ? 50.315  15.531   38.468   1.00 103.09 ? 135 LYS   E O      1 
ATOM   14433 C  CB     . LYS   E 3  130 ? 50.423  12.714   37.393   1.00 92.28  ? 135 LYS   E CB     1 
ATOM   14434 C  CG     . LYS   E 3  130 ? 51.059  11.440   37.911   1.00 94.81  ? 135 LYS   E CG     1 
ATOM   14435 C  CD     . LYS   E 3  130 ? 52.502  11.302   37.446   1.00 101.39 ? 135 LYS   E CD     1 
ATOM   14436 C  CE     . LYS   E 3  130 ? 53.403  12.388   38.034   1.00 99.72  ? 135 LYS   E CE     1 
ATOM   14437 N  NZ     . LYS   E 3  130 ? 54.804  12.237   37.534   1.00 97.03  ? 135 LYS   E NZ     1 
ATOM   14438 N  N      . ASN   E 3  131 ? 48.260  15.378   37.592   1.00 89.41  ? 136 ASN   E N      1 
ATOM   14439 C  CA     . ASN   E 3  131 ? 48.161  16.828   37.502   1.00 91.22  ? 136 ASN   E CA     1 
ATOM   14440 C  C      . ASN   E 3  131 ? 47.672  17.436   38.812   1.00 95.12  ? 136 ASN   E C      1 
ATOM   14441 O  O      . ASN   E 3  131 ? 48.166  18.487   39.234   1.00 96.26  ? 136 ASN   E O      1 
ATOM   14442 C  CB     . ASN   E 3  131 ? 47.250  17.221   36.347   1.00 91.29  ? 136 ASN   E CB     1 
ATOM   14443 C  CG     . ASN   E 3  131 ? 48.028  17.671   35.141   1.00 92.69  ? 136 ASN   E CG     1 
ATOM   14444 O  OD1    . ASN   E 3  131 ? 49.014  17.036   34.755   1.00 90.57  ? 136 ASN   E OD1    1 
ATOM   14445 N  ND2    . ASN   E 3  131 ? 47.596  18.771   34.530   1.00 90.75  ? 136 ASN   E ND2    1 
ATOM   14446 N  N      . LYS   E 3  132 ? 46.711  16.788   39.472   1.00 92.61  ? 137 LYS   E N      1 
ATOM   14447 C  CA     . LYS   E 3  132 ? 46.267  17.266   40.774   1.00 94.57  ? 137 LYS   E CA     1 
ATOM   14448 C  C      . LYS   E 3  132 ? 47.335  17.107   41.848   1.00 100.27 ? 137 LYS   E C      1 
ATOM   14449 O  O      . LYS   E 3  132 ? 47.231  17.749   42.900   1.00 105.84 ? 137 LYS   E O      1 
ATOM   14450 C  CB     . LYS   E 3  132 ? 44.992  16.543   41.210   1.00 88.06  ? 137 LYS   E CB     1 
ATOM   14451 C  CG     . LYS   E 3  132 ? 44.179  17.303   42.238   1.00 84.82  ? 137 LYS   E CG     1 
ATOM   14452 C  CD     . LYS   E 3  132 ? 42.993  16.488   42.701   1.00 82.65  ? 137 LYS   E CD     1 
ATOM   14453 C  CE     . LYS   E 3  132 ? 43.343  15.632   43.903   1.00 86.43  ? 137 LYS   E CE     1 
ATOM   14454 N  NZ     . LYS   E 3  132 ? 42.113  15.072   44.527   1.00 84.42  ? 137 LYS   E NZ     1 
ATOM   14455 N  N      . GLU   E 3  133 ? 48.343  16.258   41.627   1.00 99.18  ? 138 GLU   E N      1 
ATOM   14456 C  CA     . GLU   E 3  133 ? 49.491  16.230   42.526   1.00 103.13 ? 138 GLU   E CA     1 
ATOM   14457 C  C      . GLU   E 3  133 ? 50.485  17.348   42.226   1.00 102.58 ? 138 GLU   E C      1 
ATOM   14458 O  O      . GLU   E 3  133 ? 51.330  17.646   43.075   1.00 106.78 ? 138 GLU   E O      1 
ATOM   14459 C  CB     . GLU   E 3  133 ? 50.186  14.870   42.460   1.00 103.70 ? 138 GLU   E CB     1 
ATOM   14460 C  CG     . GLU   E 3  133 ? 50.194  14.109   43.776   1.00 106.53 ? 138 GLU   E CG     1 
ATOM   14461 C  CD     . GLU   E 3  133 ? 50.645  12.664   43.609   1.00 113.28 ? 138 GLU   E CD     1 
ATOM   14462 O  OE1    . GLU   E 3  133 ? 49.859  11.754   43.956   1.00 113.99 ? 138 GLU   E OE1    1 
ATOM   14463 O  OE2    . GLU   E 3  133 ? 51.778  12.436   43.127   1.00 110.64 ? 138 GLU   E OE2    1 
ATOM   14464 N  N      . LEU   E 3  134 ? 50.404  17.964   41.042   1.00 98.48  ? 139 LEU   E N      1 
ATOM   14465 C  CA     . LEU   E 3  134 ? 51.075  19.227   40.753   1.00 98.04  ? 139 LEU   E CA     1 
ATOM   14466 C  C      . LEU   E 3  134 ? 50.256  20.430   41.201   1.00 103.95 ? 139 LEU   E C      1 
ATOM   14467 O  O      . LEU   E 3  134 ? 50.542  21.559   40.788   1.00 102.50 ? 139 LEU   E O      1 
ATOM   14468 C  CB     . LEU   E 3  134 ? 51.391  19.338   39.262   1.00 97.34  ? 139 LEU   E CB     1 
ATOM   14469 C  CG     . LEU   E 3  134 ? 52.557  18.492   38.742   1.00 101.19 ? 139 LEU   E CG     1 
ATOM   14470 C  CD1    . LEU   E 3  134 ? 53.883  19.168   39.066   1.00 95.58  ? 139 LEU   E CD1    1 
ATOM   14471 C  CD2    . LEU   E 3  134 ? 52.523  17.069   39.301   1.00 100.47 ? 139 LEU   E CD2    1 
ATOM   14472 N  N      . LYS   E 3  135 ? 49.228  20.200   42.011   1.00 107.19 ? 140 LYS   E N      1 
ATOM   14473 C  CA     . LYS   E 3  135 ? 48.492  21.248   42.700   1.00 104.44 ? 140 LYS   E CA     1 
ATOM   14474 C  C      . LYS   E 3  135 ? 49.059  21.507   44.087   1.00 106.39 ? 140 LYS   E C      1 
ATOM   14475 O  O      . LYS   E 3  135 ? 48.998  22.639   44.578   1.00 110.96 ? 140 LYS   E O      1 
ATOM   14476 C  CB     . LYS   E 3  135 ? 47.018  20.847   42.804   1.00 102.60 ? 140 LYS   E CB     1 
ATOM   14477 C  CG     . LYS   E 3  135 ? 46.008  21.942   42.534   1.00 101.06 ? 140 LYS   E CG     1 
ATOM   14478 C  CD     . LYS   E 3  135 ? 44.675  21.586   43.194   1.00 97.25  ? 140 LYS   E CD     1 
ATOM   14479 C  CE     . LYS   E 3  135 ? 43.668  22.719   43.100   1.00 90.95  ? 140 LYS   E CE     1 
ATOM   14480 N  NZ     . LYS   E 3  135 ? 42.385  22.354   43.763   1.00 85.06  ? 140 LYS   E NZ     1 
ATOM   14481 N  N      . GLU   E 3  136 ? 49.634  20.486   44.715   1.00 108.37 ? 141 GLU   E N      1 
ATOM   14482 C  CA     . GLU   E 3  136 ? 50.104  20.604   46.094   1.00 116.00 ? 141 GLU   E CA     1 
ATOM   14483 C  C      . GLU   E 3  136 ? 51.633  20.598   46.165   1.00 106.73 ? 141 GLU   E C      1 
ATOM   14484 O  O      . GLU   E 3  136 ? 52.316  20.616   45.140   1.00 98.43  ? 141 GLU   E O      1 
ATOM   14485 C  CB     . GLU   E 3  136 ? 49.536  19.469   46.963   1.00 120.80 ? 141 GLU   E CB     1 
ATOM   14486 C  CG     . GLU   E 3  136 ? 48.194  18.850   46.503   1.00 118.92 ? 141 GLU   E CG     1 
ATOM   14487 C  CD     . GLU   E 3  136 ? 47.139  19.870   46.086   1.00 114.98 ? 141 GLU   E CD     1 
ATOM   14488 O  OE1    . GLU   E 3  136 ? 47.328  21.082   46.346   1.00 118.78 ? 141 GLU   E OE1    1 
ATOM   14489 O  OE2    . GLU   E 3  136 ? 46.118  19.446   45.496   1.00 105.67 ? 141 GLU   E OE2    1 
ATOM   14490 N  N      . MET   F 4  1   ? -4.683  -56.434  -59.010  1.00 70.75  ? 1   MET   F N      1 
ATOM   14491 C  CA     . MET   F 4  1   ? -3.977  -55.472  -59.843  1.00 77.51  ? 1   MET   F CA     1 
ATOM   14492 C  C      . MET   F 4  1   ? -2.761  -56.093  -60.515  1.00 76.39  ? 1   MET   F C      1 
ATOM   14493 O  O      . MET   F 4  1   ? -1.840  -56.602  -59.859  1.00 74.12  ? 1   MET   F O      1 
ATOM   14494 C  CB     . MET   F 4  1   ? -3.507  -54.253  -59.042  1.00 71.25  ? 1   MET   F CB     1 
ATOM   14495 C  CG     . MET   F 4  1   ? -4.426  -53.046  -59.109  1.00 76.67  ? 1   MET   F CG     1 
ATOM   14496 S  SD     . MET   F 4  1   ? -3.434  -51.537  -59.123  1.00 95.53  ? 1   MET   F SD     1 
ATOM   14497 C  CE     . MET   F 4  1   ? -4.648  -50.306  -59.573  1.00 79.17  ? 1   MET   F CE     1 
ATOM   14498 N  N      . TYR   F 4  2   ? -2.756  -56.017  -61.835  1.00 69.55  ? 2   TYR   F N      1 
ATOM   14499 C  CA     . TYR   F 4  2   ? -1.601  -56.434  -62.595  1.00 67.34  ? 2   TYR   F CA     1 
ATOM   14500 C  C      . TYR   F 4  2   ? -0.570  -55.313  -62.609  1.00 70.01  ? 2   TYR   F C      1 
ATOM   14501 O  O      . TYR   F 4  2   ? -0.841  -54.174  -62.212  1.00 69.02  ? 2   TYR   F O      1 
ATOM   14502 C  CB     . TYR   F 4  2   ? -2.034  -56.845  -63.995  1.00 63.86  ? 2   TYR   F CB     1 
ATOM   14503 C  CG     . TYR   F 4  2   ? -3.228  -57.766  -63.938  1.00 63.77  ? 2   TYR   F CG     1 
ATOM   14504 C  CD1    . TYR   F 4  2   ? -3.125  -59.018  -63.355  1.00 57.87  ? 2   TYR   F CD1    1 
ATOM   14505 C  CD2    . TYR   F 4  2   ? -4.467  -57.376  -64.442  1.00 64.12  ? 2   TYR   F CD2    1 
ATOM   14506 C  CE1    . TYR   F 4  2   ? -4.212  -59.856  -63.283  1.00 58.53  ? 2   TYR   F CE1    1 
ATOM   14507 C  CE2    . TYR   F 4  2   ? -5.563  -58.217  -64.380  1.00 56.51  ? 2   TYR   F CE2    1 
ATOM   14508 C  CZ     . TYR   F 4  2   ? -5.427  -59.450  -63.803  1.00 57.48  ? 2   TYR   F CZ     1 
ATOM   14509 O  OH     . TYR   F 4  2   ? -6.503  -60.287  -63.724  1.00 58.76  ? 2   TYR   F OH     1 
ATOM   14510 N  N      . THR   F 4  3   ? 0.640   -55.656  -63.038  1.00 64.87  ? 3   THR   F N      1 
ATOM   14511 C  CA     . THR   F 4  3   ? 1.727   -54.697  -63.073  1.00 66.06  ? 3   THR   F CA     1 
ATOM   14512 C  C      . THR   F 4  3   ? 2.466   -54.836  -64.392  1.00 65.13  ? 3   THR   F C      1 
ATOM   14513 O  O      . THR   F 4  3   ? 2.451   -55.893  -65.030  1.00 63.63  ? 3   THR   F O      1 
ATOM   14514 C  CB     . THR   F 4  3   ? 2.702   -54.890  -61.912  1.00 63.67  ? 3   THR   F CB     1 
ATOM   14515 O  OG1    . THR   F 4  3   ? 3.709   -55.828  -62.306  1.00 61.67  ? 3   THR   F OG1    1 
ATOM   14516 C  CG2    . THR   F 4  3   ? 1.971   -55.409  -60.683  1.00 65.98  ? 3   THR   F CG2    1 
ATOM   14517 N  N      . PHE   F 4  4   ? 3.128   -53.752  -64.789  1.00 62.76  ? 4   PHE   F N      1 
ATOM   14518 C  CA     . PHE   F 4  4   ? 3.800   -53.733  -66.073  1.00 64.11  ? 4   PHE   F CA     1 
ATOM   14519 C  C      . PHE   F 4  4   ? 4.847   -52.632  -66.075  1.00 64.77  ? 4   PHE   F C      1 
ATOM   14520 O  O      . PHE   F 4  4   ? 4.671   -51.596  -65.438  1.00 67.80  ? 4   PHE   F O      1 
ATOM   14521 C  CB     . PHE   F 4  4   ? 2.785   -53.556  -67.208  1.00 69.06  ? 4   PHE   F CB     1 
ATOM   14522 C  CG     . PHE   F 4  4   ? 2.317   -52.138  -67.411  1.00 71.90  ? 4   PHE   F CG     1 
ATOM   14523 C  CD1    . PHE   F 4  4   ? 2.979   -51.290  -68.303  1.00 73.31  ? 4   PHE   F CD1    1 
ATOM   14524 C  CD2    . PHE   F 4  4   ? 1.196   -51.662  -66.744  1.00 69.45  ? 4   PHE   F CD2    1 
ATOM   14525 C  CE1    . PHE   F 4  4   ? 2.538   -49.988  -68.509  1.00 72.73  ? 4   PHE   F CE1    1 
ATOM   14526 C  CE2    . PHE   F 4  4   ? 0.755   -50.361  -66.942  1.00 69.65  ? 4   PHE   F CE2    1 
ATOM   14527 C  CZ     . PHE   F 4  4   ? 1.426   -49.524  -67.826  1.00 70.73  ? 4   PHE   F CZ     1 
ATOM   14528 N  N      . VAL   F 4  5   ? 5.952   -52.890  -66.767  1.00 67.87  ? 5   VAL   F N      1 
ATOM   14529 C  CA     . VAL   F 4  5   ? 7.009   -51.912  -66.963  1.00 64.19  ? 5   VAL   F CA     1 
ATOM   14530 C  C      . VAL   F 4  5   ? 6.983   -51.477  -68.423  1.00 67.63  ? 5   VAL   F C      1 
ATOM   14531 O  O      . VAL   F 4  5   ? 6.291   -52.059  -69.254  1.00 71.62  ? 5   VAL   F O      1 
ATOM   14532 C  CB     . VAL   F 4  5   ? 8.394   -52.466  -66.584  1.00 67.70  ? 5   VAL   F CB     1 
ATOM   14533 C  CG1    . VAL   F 4  5   ? 8.356   -53.112  -65.209  1.00 64.30  ? 5   VAL   F CG1    1 
ATOM   14534 C  CG2    . VAL   F 4  5   ? 8.867   -53.448  -67.647  1.00 67.61  ? 5   VAL   F CG2    1 
ATOM   14535 N  N      . VAL   F 4  6   ? 7.763   -50.445  -68.734  1.00 72.01  ? 6   VAL   F N      1 
ATOM   14536 C  CA     . VAL   F 4  6   ? 7.779   -49.831  -70.058  1.00 67.23  ? 6   VAL   F CA     1 
ATOM   14537 C  C      . VAL   F 4  6   ? 9.227   -49.580  -70.454  1.00 67.09  ? 6   VAL   F C      1 
ATOM   14538 O  O      . VAL   F 4  6   ? 9.978   -48.950  -69.704  1.00 80.49  ? 6   VAL   F O      1 
ATOM   14539 C  CB     . VAL   F 4  6   ? 6.966   -48.519  -70.078  1.00 67.57  ? 6   VAL   F CB     1 
ATOM   14540 C  CG1    . VAL   F 4  6   ? 7.343   -47.681  -71.275  1.00 67.44  ? 6   VAL   F CG1    1 
ATOM   14541 C  CG2    . VAL   F 4  6   ? 5.451   -48.813  -70.049  1.00 60.52  ? 6   VAL   F CG2    1 
ATOM   14542 N  N      . ARG   F 4  7   ? 9.626   -50.070  -71.628  1.00 66.62  ? 7   ARG   F N      1 
ATOM   14543 C  CA     . ARG   F 4  7   ? 11.029  -50.014  -72.022  1.00 67.60  ? 7   ARG   F CA     1 
ATOM   14544 C  C      . ARG   F 4  7   ? 11.270  -49.571  -73.464  1.00 69.64  ? 7   ARG   F C      1 
ATOM   14545 O  O      . ARG   F 4  7   ? 12.426  -49.582  -73.912  1.00 62.33  ? 7   ARG   F O      1 
ATOM   14546 C  CB     . ARG   F 4  7   ? 11.681  -51.378  -71.773  1.00 65.41  ? 7   ARG   F CB     1 
ATOM   14547 C  CG     . ARG   F 4  7   ? 11.478  -51.849  -70.336  1.00 70.48  ? 7   ARG   F CG     1 
ATOM   14548 C  CD     . ARG   F 4  7   ? 11.819  -53.320  -70.158  1.00 69.20  ? 7   ARG   F CD     1 
ATOM   14549 N  NE     . ARG   F 4  7   ? 13.206  -53.627  -70.486  1.00 65.02  ? 7   ARG   F NE     1 
ATOM   14550 C  CZ     . ARG   F 4  7   ? 14.177  -53.750  -69.592  1.00 66.04  ? 7   ARG   F CZ     1 
ATOM   14551 N  NH1    . ARG   F 4  7   ? 13.957  -53.531  -68.306  1.00 68.05  ? 7   ARG   F NH1    1 
ATOM   14552 N  NH2    . ARG   F 4  7   ? 15.396  -54.110  -70.000  1.00 61.07  ? 7   ARG   F NH2    1 
ATOM   14553 N  N      . ASP   F 4  8   ? 10.229  -49.173  -74.196  1.00 72.70  ? 8   ASP   F N      1 
ATOM   14554 C  CA     . ASP   F 4  8   ? 10.355  -48.508  -75.492  1.00 72.80  ? 8   ASP   F CA     1 
ATOM   14555 C  C      . ASP   F 4  8   ? 9.566   -47.220  -75.359  1.00 77.20  ? 8   ASP   F C      1 
ATOM   14556 O  O      . ASP   F 4  8   ? 8.341   -47.227  -75.503  1.00 80.01  ? 8   ASP   F O      1 
ATOM   14557 C  CB     . ASP   F 4  8   ? 9.824   -49.367  -76.636  1.00 72.23  ? 8   ASP   F CB     1 
ATOM   14558 C  CG     . ASP   F 4  8   ? 10.423  -48.989  -77.978  1.00 82.06  ? 8   ASP   F CG     1 
ATOM   14559 O  OD1    . ASP   F 4  8   ? 11.516  -48.376  -78.007  1.00 86.64  ? 8   ASP   F OD1    1 
ATOM   14560 O  OD2    . ASP   F 4  8   ? 9.799   -49.309  -79.012  1.00 84.20  ? 8   ASP   F OD2    1 
ATOM   14561 N  N      . GLU   F 4  9   ? 10.260  -46.125  -75.043  1.00 81.15  ? 9   GLU   F N      1 
ATOM   14562 C  CA     . GLU   F 4  9   ? 9.579   -44.852  -74.837  1.00 82.24  ? 9   GLU   F CA     1 
ATOM   14563 C  C      . GLU   F 4  9   ? 9.137   -44.208  -76.145  1.00 86.27  ? 9   GLU   F C      1 
ATOM   14564 O  O      . GLU   F 4  9   ? 8.286   -43.315  -76.117  1.00 88.80  ? 9   GLU   F O      1 
ATOM   14565 C  CB     . GLU   F 4  9   ? 10.474  -43.888  -74.054  1.00 82.15  ? 9   GLU   F CB     1 
ATOM   14566 C  CG     . GLU   F 4  9   ? 10.739  -44.305  -72.611  1.00 80.34  ? 9   GLU   F CG     1 
ATOM   14567 C  CD     . GLU   F 4  9   ? 9.486   -44.275  -71.745  1.00 86.44  ? 9   GLU   F CD     1 
ATOM   14568 O  OE1    . GLU   F 4  9   ? 8.466   -43.702  -72.183  1.00 83.02  ? 9   GLU   F OE1    1 
ATOM   14569 O  OE2    . GLU   F 4  9   ? 9.515   -44.835  -70.624  1.00 92.88  ? 9   GLU   F OE2    1 
ATOM   14570 N  N      . ASN   F 4  10  ? 9.674   -44.650  -77.280  1.00 83.66  ? 10  ASN   F N      1 
ATOM   14571 C  CA     . ASN   F 4  10  ? 9.279   -44.151  -78.588  1.00 78.59  ? 10  ASN   F CA     1 
ATOM   14572 C  C      . ASN   F 4  10  ? 8.070   -44.874  -79.170  1.00 80.55  ? 10  ASN   F C      1 
ATOM   14573 O  O      . ASN   F 4  10  ? 7.662   -44.562  -80.293  1.00 82.11  ? 10  ASN   F O      1 
ATOM   14574 C  CB     . ASN   F 4  10  ? 10.447  -44.281  -79.566  1.00 80.46  ? 10  ASN   F CB     1 
ATOM   14575 C  CG     . ASN   F 4  10  ? 11.681  -43.573  -79.087  1.00 82.15  ? 10  ASN   F CG     1 
ATOM   14576 O  OD1    . ASN   F 4  10  ? 11.817  -43.265  -77.903  1.00 87.17  ? 10  ASN   F OD1    1 
ATOM   14577 N  ND2    . ASN   F 4  10  ? 12.606  -43.322  -80.005  1.00 86.05  ? 10  ASN   F ND2    1 
ATOM   14578 N  N      . SER   F 4  11  ? 7.503   -45.844  -78.463  1.00 80.20  ? 11  SER   F N      1 
ATOM   14579 C  CA     . SER   F 4  11  ? 6.425   -46.656  -79.025  1.00 77.99  ? 11  SER   F CA     1 
ATOM   14580 C  C      . SER   F 4  11  ? 5.140   -45.831  -79.029  1.00 77.85  ? 11  SER   F C      1 
ATOM   14581 O  O      . SER   F 4  11  ? 4.419   -45.758  -78.022  1.00 73.48  ? 11  SER   F O      1 
ATOM   14582 C  CB     . SER   F 4  11  ? 6.266   -47.958  -78.240  1.00 80.27  ? 11  SER   F CB     1 
ATOM   14583 O  OG     . SER   F 4  11  ? 5.214   -48.779  -78.732  1.00 67.10  ? 11  SER   F OG     1 
ATOM   14584 N  N      . SER   F 4  12  ? 4.853   -45.205  -80.178  1.00 73.69  ? 12  SER   F N      1 
ATOM   14585 C  CA     . SER   F 4  12  ? 3.569   -44.533  -80.369  1.00 75.81  ? 12  SER   F CA     1 
ATOM   14586 C  C      . SER   F 4  12  ? 2.404   -45.424  -79.929  1.00 77.33  ? 12  SER   F C      1 
ATOM   14587 O  O      . SER   F 4  12  ? 1.471   -44.968  -79.252  1.00 73.27  ? 12  SER   F O      1 
ATOM   14588 C  CB     . SER   F 4  12  ? 3.422   -44.125  -81.840  1.00 71.84  ? 12  SER   F CB     1 
ATOM   14589 O  OG     . SER   F 4  12  ? 4.576   -44.472  -82.599  1.00 66.85  ? 12  SER   F OG     1 
ATOM   14590 N  N      . VAL   F 4  13  ? 2.464   -46.713  -80.279  1.00 79.22  ? 13  VAL   F N      1 
ATOM   14591 C  CA     . VAL   F 4  13  ? 1.346   -47.621  -80.030  1.00 77.26  ? 13  VAL   F CA     1 
ATOM   14592 C  C      . VAL   F 4  13  ? 1.238   -47.960  -78.548  1.00 75.43  ? 13  VAL   F C      1 
ATOM   14593 O  O      . VAL   F 4  13  ? 0.166   -47.844  -77.944  1.00 76.37  ? 13  VAL   F O      1 
ATOM   14594 C  CB     . VAL   F 4  13  ? 1.498   -48.893  -80.883  1.00 73.25  ? 13  VAL   F CB     1 
ATOM   14595 C  CG1    . VAL   F 4  13  ? 0.623   -50.009  -80.325  1.00 71.23  ? 13  VAL   F CG1    1 
ATOM   14596 C  CG2    . VAL   F 4  13  ? 1.156   -48.608  -82.327  1.00 67.78  ? 13  VAL   F CG2    1 
ATOM   14597 N  N      . TYR   F 4  14  ? 2.335   -48.414  -77.944  1.00 74.43  ? 14  TYR   F N      1 
ATOM   14598 C  CA     . TYR   F 4  14  ? 2.275   -48.866  -76.560  1.00 75.62  ? 14  TYR   F CA     1 
ATOM   14599 C  C      . TYR   F 4  14  ? 2.350   -47.702  -75.581  1.00 81.86  ? 14  TYR   F C      1 
ATOM   14600 O  O      . TYR   F 4  14  ? 1.987   -47.862  -74.408  1.00 78.22  ? 14  TYR   F O      1 
ATOM   14601 C  CB     . TYR   F 4  14  ? 3.376   -49.908  -76.316  1.00 73.16  ? 14  TYR   F CB     1 
ATOM   14602 C  CG     . TYR   F 4  14  ? 3.128   -51.162  -77.132  1.00 70.09  ? 14  TYR   F CG     1 
ATOM   14603 C  CD1    . TYR   F 4  14  ? 2.129   -52.063  -76.769  1.00 68.08  ? 14  TYR   F CD1    1 
ATOM   14604 C  CD2    . TYR   F 4  14  ? 3.841   -51.411  -78.302  1.00 63.10  ? 14  TYR   F CD2    1 
ATOM   14605 C  CE1    . TYR   F 4  14  ? 1.868   -53.197  -77.534  1.00 66.97  ? 14  TYR   F CE1    1 
ATOM   14606 C  CE2    . TYR   F 4  14  ? 3.586   -52.531  -79.073  1.00 58.73  ? 14  TYR   F CE2    1 
ATOM   14607 C  CZ     . TYR   F 4  14  ? 2.598   -53.428  -78.688  1.00 65.96  ? 14  TYR   F CZ     1 
ATOM   14608 O  OH     . TYR   F 4  14  ? 2.346   -54.563  -79.446  1.00 59.58  ? 14  TYR   F OH     1 
ATOM   14609 N  N      . ALA   F 4  15  ? 2.793   -46.533  -76.048  1.00 84.31  ? 15  ALA   F N      1 
ATOM   14610 C  CA     . ALA   F 4  15  ? 2.429   -45.300  -75.373  1.00 74.92  ? 15  ALA   F CA     1 
ATOM   14611 C  C      . ALA   F 4  15  ? 0.944   -45.326  -75.036  1.00 75.81  ? 15  ALA   F C      1 
ATOM   14612 O  O      . ALA   F 4  15  ? 0.545   -45.033  -73.906  1.00 80.55  ? 15  ALA   F O      1 
ATOM   14613 C  CB     . ALA   F 4  15  ? 2.779   -44.104  -76.258  1.00 67.76  ? 15  ALA   F CB     1 
ATOM   14614 N  N      . GLU   F 4  16  ? 0.108   -45.705  -76.007  1.00 78.96  ? 16  GLU   F N      1 
ATOM   14615 C  CA     . GLU   F 4  16  ? -1.337  -45.723  -75.777  1.00 83.55  ? 16  GLU   F CA     1 
ATOM   14616 C  C      . GLU   F 4  16  ? -1.779  -46.963  -75.013  1.00 81.27  ? 16  GLU   F C      1 
ATOM   14617 O  O      . GLU   F 4  16  ? -2.706  -46.895  -74.197  1.00 81.39  ? 16  GLU   F O      1 
ATOM   14618 C  CB     . GLU   F 4  16  ? -2.095  -45.634  -77.102  1.00 83.82  ? 16  GLU   F CB     1 
ATOM   14619 C  CG     . GLU   F 4  16  ? -2.721  -44.271  -77.360  1.00 87.37  ? 16  GLU   F CG     1 
ATOM   14620 C  CD     . GLU   F 4  16  ? -4.009  -44.074  -76.598  1.00 89.12  ? 16  GLU   F CD     1 
ATOM   14621 O  OE1    . GLU   F 4  16  ? -5.006  -44.719  -76.981  1.00 90.31  ? 16  GLU   F OE1    1 
ATOM   14622 O  OE2    . GLU   F 4  16  ? -4.036  -43.270  -75.634  1.00 88.98  ? 16  GLU   F OE2    1 
ATOM   14623 N  N      . VAL   F 4  17  ? -1.146  -48.106  -75.274  1.00 81.67  ? 17  VAL   F N      1 
ATOM   14624 C  CA     . VAL   F 4  17  ? -1.428  -49.291  -74.470  1.00 81.22  ? 17  VAL   F CA     1 
ATOM   14625 C  C      . VAL   F 4  17  ? -1.164  -48.996  -72.998  1.00 81.69  ? 17  VAL   F C      1 
ATOM   14626 O  O      . VAL   F 4  17  ? -1.968  -49.354  -72.127  1.00 85.39  ? 17  VAL   F O      1 
ATOM   14627 C  CB     . VAL   F 4  17  ? -0.604  -50.495  -74.971  1.00 82.09  ? 17  VAL   F CB     1 
ATOM   14628 C  CG1    . VAL   F 4  17  ? -0.602  -51.624  -73.933  1.00 78.31  ? 17  VAL   F CG1    1 
ATOM   14629 C  CG2    . VAL   F 4  17  ? -1.136  -50.989  -76.319  1.00 76.30  ? 17  VAL   F CG2    1 
ATOM   14630 N  N      . SER   F 4  18  ? -0.041  -48.326  -72.700  1.00 75.74  ? 18  SER   F N      1 
ATOM   14631 C  CA     . SER   F 4  18  ? 0.260   -47.949  -71.320  1.00 76.66  ? 18  SER   F CA     1 
ATOM   14632 C  C      . SER   F 4  18  ? -0.834  -47.066  -70.746  1.00 79.48  ? 18  SER   F C      1 
ATOM   14633 O  O      . SER   F 4  18  ? -1.346  -47.328  -69.649  1.00 78.16  ? 18  SER   F O      1 
ATOM   14634 C  CB     . SER   F 4  18  ? 1.598   -47.225  -71.240  1.00 72.91  ? 18  SER   F CB     1 
ATOM   14635 O  OG     . SER   F 4  18  ? 2.577   -47.905  -71.997  1.00 82.71  ? 18  SER   F OG     1 
ATOM   14636 N  N      . ARG   F 4  19  ? -1.203  -46.012  -71.484  1.00 81.41  ? 19  ARG   F N      1 
ATOM   14637 C  CA     . ARG   F 4  19  ? -2.253  -45.098  -71.045  1.00 80.55  ? 19  ARG   F CA     1 
ATOM   14638 C  C      . ARG   F 4  19  ? -3.519  -45.858  -70.683  1.00 80.42  ? 19  ARG   F C      1 
ATOM   14639 O  O      . ARG   F 4  19  ? -3.973  -45.826  -69.532  1.00 83.73  ? 19  ARG   F O      1 
ATOM   14640 C  CB     . ARG   F 4  19  ? -2.543  -44.054  -72.129  1.00 83.84  ? 19  ARG   F CB     1 
ATOM   14641 C  CG     . ARG   F 4  19  ? -1.879  -42.712  -71.873  1.00 86.96  ? 19  ARG   F CG     1 
ATOM   14642 C  CD     . ARG   F 4  19  ? -2.092  -41.694  -72.980  1.00 89.05  ? 19  ARG   F CD     1 
ATOM   14643 N  NE     . ARG   F 4  19  ? -1.658  -42.151  -74.300  1.00 95.02  ? 19  ARG   F NE     1 
ATOM   14644 C  CZ     . ARG   F 4  19  ? -0.533  -41.765  -74.895  1.00 93.25  ? 19  ARG   F CZ     1 
ATOM   14645 N  NH1    . ARG   F 4  19  ? 0.371   -41.038  -74.255  1.00 89.75  ? 19  ARG   F NH1    1 
ATOM   14646 N  NH2    . ARG   F 4  19  ? -0.307  -42.120  -76.162  1.00 81.07  ? 19  ARG   F NH2    1 
ATOM   14647 N  N      . LEU   F 4  20  ? -4.096  -46.560  -71.662  1.00 81.67  ? 20  LEU   F N      1 
ATOM   14648 C  CA     . LEU   F 4  20  ? -5.363  -47.242  -71.423  1.00 85.29  ? 20  LEU   F CA     1 
ATOM   14649 C  C      . LEU   F 4  20  ? -5.239  -48.229  -70.273  1.00 84.01  ? 20  LEU   F C      1 
ATOM   14650 O  O      . LEU   F 4  20  ? -6.148  -48.342  -69.441  1.00 80.43  ? 20  LEU   F O      1 
ATOM   14651 C  CB     . LEU   F 4  20  ? -5.831  -47.954  -72.697  1.00 89.74  ? 20  LEU   F CB     1 
ATOM   14652 C  CG     . LEU   F 4  20  ? -5.562  -47.247  -74.032  1.00 89.08  ? 20  LEU   F CG     1 
ATOM   14653 C  CD1    . LEU   F 4  20  ? -5.575  -48.255  -75.182  1.00 79.97  ? 20  LEU   F CD1    1 
ATOM   14654 C  CD2    . LEU   F 4  20  ? -6.544  -46.088  -74.285  1.00 89.09  ? 20  LEU   F CD2    1 
ATOM   14655 N  N      . LEU   F 4  21  ? -4.111  -48.942  -70.205  1.00 83.74  ? 21  LEU   F N      1 
ATOM   14656 C  CA     . LEU   F 4  21  ? -3.931  -49.952  -69.168  1.00 83.88  ? 21  LEU   F CA     1 
ATOM   14657 C  C      . LEU   F 4  21  ? -4.108  -49.351  -67.780  1.00 81.37  ? 21  LEU   F C      1 
ATOM   14658 O  O      . LEU   F 4  21  ? -4.853  -49.885  -66.945  1.00 80.44  ? 21  LEU   F O      1 
ATOM   14659 C  CB     . LEU   F 4  21  ? -2.557  -50.611  -69.310  1.00 79.45  ? 21  LEU   F CB     1 
ATOM   14660 C  CG     . LEU   F 4  21  ? -2.567  -51.927  -70.088  1.00 73.21  ? 21  LEU   F CG     1 
ATOM   14661 C  CD1    . LEU   F 4  21  ? -1.178  -52.539  -70.135  1.00 72.39  ? 21  LEU   F CD1    1 
ATOM   14662 C  CD2    . LEU   F 4  21  ? -3.581  -52.902  -69.489  1.00 71.84  ? 21  LEU   F CD2    1 
ATOM   14663 N  N      . LEU   F 4  22  ? -3.439  -48.228  -67.519  1.00 78.78  ? 22  LEU   F N      1 
ATOM   14664 C  CA     . LEU   F 4  22  ? -3.559  -47.587  -66.217  1.00 78.25  ? 22  LEU   F CA     1 
ATOM   14665 C  C      . LEU   F 4  22  ? -5.005  -47.208  -65.934  1.00 82.10  ? 22  LEU   F C      1 
ATOM   14666 O  O      . LEU   F 4  22  ? -5.526  -47.455  -64.838  1.00 81.47  ? 22  LEU   F O      1 
ATOM   14667 C  CB     . LEU   F 4  22  ? -2.642  -46.369  -66.172  1.00 70.28  ? 22  LEU   F CB     1 
ATOM   14668 C  CG     . LEU   F 4  22  ? -1.188  -46.844  -66.145  1.00 76.46  ? 22  LEU   F CG     1 
ATOM   14669 C  CD1    . LEU   F 4  22  ? -0.182  -45.706  -66.307  1.00 70.39  ? 22  LEU   F CD1    1 
ATOM   14670 C  CD2    . LEU   F 4  22  ? -0.924  -47.658  -64.869  1.00 73.72  ? 22  LEU   F CD2    1 
ATOM   14671 N  N      . ALA   F 4  23  ? -5.684  -46.647  -66.936  1.00 76.54  ? 23  ALA   F N      1 
ATOM   14672 C  CA     . ALA   F 4  23  ? -7.017  -46.102  -66.746  1.00 74.22  ? 23  ALA   F CA     1 
ATOM   14673 C  C      . ALA   F 4  23  ? -8.048  -47.183  -66.435  1.00 79.35  ? 23  ALA   F C      1 
ATOM   14674 O  O      . ALA   F 4  23  ? -9.228  -46.879  -66.228  1.00 77.60  ? 23  ALA   F O      1 
ATOM   14675 C  CB     . ALA   F 4  23  ? -7.432  -45.298  -67.974  1.00 72.44  ? 23  ALA   F CB     1 
ATOM   14676 N  N      . THR   F 4  24  ? -7.629  -48.447  -66.394  1.00 81.30  ? 24  THR   F N      1 
ATOM   14677 C  CA     . THR   F 4  24  ? -8.533  -49.485  -65.909  1.00 83.58  ? 24  THR   F CA     1 
ATOM   14678 C  C      . THR   F 4  24  ? -8.585  -49.542  -64.392  1.00 84.50  ? 24  THR   F C      1 
ATOM   14679 O  O      . THR   F 4  24  ? -9.531  -50.120  -63.837  1.00 80.12  ? 24  THR   F O      1 
ATOM   14680 C  CB     . THR   F 4  24  ? -8.140  -50.869  -66.442  1.00 82.80  ? 24  THR   F CB     1 
ATOM   14681 O  OG1    . THR   F 4  24  ? -7.803  -50.781  -67.829  1.00 78.81  ? 24  THR   F OG1    1 
ATOM   14682 C  CG2    . THR   F 4  24  ? -9.298  -51.838  -66.270  1.00 81.27  ? 24  THR   F CG2    1 
ATOM   14683 N  N      . GLY   F 4  25  ? -7.589  -48.961  -63.718  1.00 88.23  ? 25  GLY   F N      1 
ATOM   14684 C  CA     . GLY   F 4  25  ? -7.518  -48.979  -62.269  1.00 86.19  ? 25  GLY   F CA     1 
ATOM   14685 C  C      . GLY   F 4  25  ? -7.196  -50.361  -61.745  1.00 86.79  ? 25  GLY   F C      1 
ATOM   14686 O  O      . GLY   F 4  25  ? -7.303  -50.636  -60.543  1.00 82.45  ? 25  GLY   F O      1 
ATOM   14687 N  N      . GLN   F 4  26  ? -6.819  -51.253  -62.662  1.00 84.76  ? 26  GLN   F N      1 
ATOM   14688 C  CA     . GLN   F 4  26  ? -6.389  -52.601  -62.313  1.00 81.30  ? 26  GLN   F CA     1 
ATOM   14689 C  C      . GLN   F 4  26  ? -4.981  -52.900  -62.820  1.00 77.32  ? 26  GLN   F C      1 
ATOM   14690 O  O      . GLN   F 4  26  ? -4.514  -54.039  -62.690  1.00 79.02  ? 26  GLN   F O      1 
ATOM   14691 C  CB     . GLN   F 4  26  ? -7.383  -53.640  -62.847  1.00 80.12  ? 26  GLN   F CB     1 
ATOM   14692 C  CG     . GLN   F 4  26  ? -8.848  -53.255  -62.715  1.00 78.03  ? 26  GLN   F CG     1 
ATOM   14693 C  CD     . GLN   F 4  26  ? -9.771  -54.434  -62.972  1.00 79.00  ? 26  GLN   F CD     1 
ATOM   14694 O  OE1    . GLN   F 4  26  ? -9.455  -55.566  -62.612  1.00 74.09  ? 26  GLN   F OE1    1 
ATOM   14695 N  NE2    . GLN   F 4  26  ? -10.905 -54.178  -63.620  1.00 82.10  ? 26  GLN   F NE2    1 
ATOM   14696 N  N      . TRP   F 4  27  ? -4.291  -51.909  -63.385  1.00 74.07  ? 27  TRP   F N      1 
ATOM   14697 C  CA     . TRP   F 4  27  ? -2.920  -52.068  -63.844  1.00 76.30  ? 27  TRP   F CA     1 
ATOM   14698 C  C      . TRP   F 4  27  ? -2.040  -50.995  -63.215  1.00 74.55  ? 27  TRP   F C      1 
ATOM   14699 O  O      . TRP   F 4  27  ? -2.471  -49.861  -63.004  1.00 76.95  ? 27  TRP   F O      1 
ATOM   14700 C  CB     . TRP   F 4  27  ? -2.832  -51.995  -65.384  1.00 76.73  ? 27  TRP   F CB     1 
ATOM   14701 C  CG     . TRP   F 4  27  ? -3.118  -53.305  -66.028  1.00 78.19  ? 27  TRP   F CG     1 
ATOM   14702 C  CD1    . TRP   F 4  27  ? -4.347  -53.796  -66.388  1.00 80.54  ? 27  TRP   F CD1    1 
ATOM   14703 C  CD2    . TRP   F 4  27  ? -2.165  -54.316  -66.373  1.00 74.59  ? 27  TRP   F CD2    1 
ATOM   14704 N  NE1    . TRP   F 4  27  ? -4.212  -55.051  -66.946  1.00 79.32  ? 27  TRP   F NE1    1 
ATOM   14705 C  CE2    . TRP   F 4  27  ? -2.883  -55.391  -66.949  1.00 76.79  ? 27  TRP   F CE2    1 
ATOM   14706 C  CE3    . TRP   F 4  27  ? -0.777  -54.413  -66.264  1.00 69.17  ? 27  TRP   F CE3    1 
ATOM   14707 C  CZ2    . TRP   F 4  27  ? -2.254  -56.547  -67.408  1.00 68.40  ? 27  TRP   F CZ2    1 
ATOM   14708 C  CZ3    . TRP   F 4  27  ? -0.161  -55.553  -66.717  1.00 68.49  ? 27  TRP   F CZ3    1 
ATOM   14709 C  CH2    . TRP   F 4  27  ? -0.898  -56.610  -67.281  1.00 64.92  ? 27  TRP   F CH2    1 
ATOM   14710 N  N      . LYS   F 4  28  ? -0.796  -51.349  -62.931  1.00 67.57  ? 28  LYS   F N      1 
ATOM   14711 C  CA     . LYS   F 4  28  ? 0.116   -50.424  -62.279  1.00 66.67  ? 28  LYS   F CA     1 
ATOM   14712 C  C      . LYS   F 4  28  ? 1.448   -50.469  -63.006  1.00 66.44  ? 28  LYS   F C      1 
ATOM   14713 O  O      . LYS   F 4  28  ? 1.956   -51.553  -63.297  1.00 71.58  ? 28  LYS   F O      1 
ATOM   14714 C  CB     . LYS   F 4  28  ? 0.279   -50.777  -60.791  1.00 69.60  ? 28  LYS   F CB     1 
ATOM   14715 C  CG     . LYS   F 4  28  ? 1.522   -50.179  -60.108  1.00 76.45  ? 28  LYS   F CG     1 
ATOM   14716 C  CD     . LYS   F 4  28  ? 1.409   -50.145  -58.568  1.00 78.24  ? 28  LYS   F CD     1 
ATOM   14717 C  CE     . LYS   F 4  28  ? 1.287   -51.554  -57.967  1.00 74.52  ? 28  LYS   F CE     1 
ATOM   14718 N  NZ     . LYS   F 4  28  ? 2.414   -51.894  -57.042  1.00 69.69  ? 28  LYS   F NZ     1 
ATOM   14719 N  N      . ARG   F 4  29  ? 2.000   -49.305  -63.321  1.00 62.64  ? 29  ARG   F N      1 
ATOM   14720 C  CA     . ARG   F 4  29  ? 3.310   -49.223  -63.955  1.00 66.17  ? 29  ARG   F CA     1 
ATOM   14721 C  C      . ARG   F 4  29  ? 4.398   -49.206  -62.886  1.00 65.10  ? 29  ARG   F C      1 
ATOM   14722 O  O      . ARG   F 4  29  ? 4.333   -48.410  -61.949  1.00 70.01  ? 29  ARG   F O      1 
ATOM   14723 C  CB     . ARG   F 4  29  ? 3.408   -47.974  -64.829  1.00 64.34  ? 29  ARG   F CB     1 
ATOM   14724 C  CG     . ARG   F 4  29  ? 4.361   -48.119  -65.982  1.00 66.29  ? 29  ARG   F CG     1 
ATOM   14725 C  CD     . ARG   F 4  29  ? 4.629   -46.807  -66.681  1.00 57.62  ? 29  ARG   F CD     1 
ATOM   14726 N  NE     . ARG   F 4  29  ? 6.057   -46.634  -66.885  1.00 62.52  ? 29  ARG   F NE     1 
ATOM   14727 C  CZ     . ARG   F 4  29  ? 6.580   -45.836  -67.800  1.00 72.79  ? 29  ARG   F CZ     1 
ATOM   14728 N  NH1    . ARG   F 4  29  ? 5.811   -45.103  -68.591  1.00 70.71  ? 29  ARG   F NH1    1 
ATOM   14729 N  NH2    . ARG   F 4  29  ? 7.905   -45.781  -67.933  1.00 78.47  ? 29  ARG   F NH2    1 
ATOM   14730 N  N      . LEU   F 4  30  ? 5.380   -50.095  -63.016  1.00 63.00  ? 30  LEU   F N      1 
ATOM   14731 C  CA     . LEU   F 4  30  ? 6.525   -50.142  -62.122  1.00 59.11  ? 30  LEU   F CA     1 
ATOM   14732 C  C      . LEU   F 4  30  ? 7.724   -49.470  -62.785  1.00 68.79  ? 30  LEU   F C      1 
ATOM   14733 O  O      . LEU   F 4  30  ? 7.653   -48.991  -63.923  1.00 68.62  ? 30  LEU   F O      1 
ATOM   14734 C  CB     . LEU   F 4  30  ? 6.847   -51.587  -61.736  1.00 62.49  ? 30  LEU   F CB     1 
ATOM   14735 C  CG     . LEU   F 4  30  ? 5.712   -52.544  -61.347  1.00 62.20  ? 30  LEU   F CG     1 
ATOM   14736 C  CD1    . LEU   F 4  30  ? 6.103   -53.981  -61.623  1.00 56.67  ? 30  LEU   F CD1    1 
ATOM   14737 C  CD2    . LEU   F 4  30  ? 5.338   -52.396  -59.885  1.00 64.13  ? 30  LEU   F CD2    1 
ATOM   14738 N  N      . ARG   F 4  31  ? 8.844   -49.431  -62.061  1.00 72.03  ? 31  ARG   F N      1 
ATOM   14739 C  CA     . ARG   F 4  31  ? 10.062  -48.884  -62.646  1.00 75.77  ? 31  ARG   F CA     1 
ATOM   14740 C  C      . ARG   F 4  31  ? 10.636  -49.846  -63.674  1.00 76.50  ? 31  ARG   F C      1 
ATOM   14741 O  O      . ARG   F 4  31  ? 10.583  -51.067  -63.511  1.00 79.91  ? 31  ARG   F O      1 
ATOM   14742 C  CB     . ARG   F 4  31  ? 11.116  -48.593  -61.581  1.00 74.40  ? 31  ARG   F CB     1 
ATOM   14743 C  CG     . ARG   F 4  31  ? 12.280  -47.763  -62.137  1.00 85.74  ? 31  ARG   F CG     1 
ATOM   14744 C  CD     . ARG   F 4  31  ? 11.780  -46.431  -62.743  1.00 87.63  ? 31  ARG   F CD     1 
ATOM   14745 N  NE     . ARG   F 4  31  ? 11.835  -46.384  -64.204  1.00 85.76  ? 31  ARG   F NE     1 
ATOM   14746 C  CZ     . ARG   F 4  31  ? 10.909  -45.827  -64.979  1.00 87.92  ? 31  ARG   F CZ     1 
ATOM   14747 N  NH1    . ARG   F 4  31  ? 9.808   -45.284  -64.471  1.00 82.46  ? 31  ARG   F NH1    1 
ATOM   14748 N  NH2    . ARG   F 4  31  ? 11.093  -45.811  -66.298  1.00 86.81  ? 31  ARG   F NH2    1 
ATOM   14749 N  N      . LYS   F 4  32  ? 11.208  -49.280  -64.734  1.00 72.62  ? 32  LYS   F N      1 
ATOM   14750 C  CA     . LYS   F 4  32  ? 11.604  -50.088  -65.880  1.00 77.91  ? 32  LYS   F CA     1 
ATOM   14751 C  C      . LYS   F 4  32  ? 12.403  -51.321  -65.461  1.00 79.53  ? 32  LYS   F C      1 
ATOM   14752 O  O      . LYS   F 4  32  ? 12.271  -52.394  -66.070  1.00 75.23  ? 32  LYS   F O      1 
ATOM   14753 C  CB     . LYS   F 4  32  ? 12.414  -49.234  -66.849  1.00 82.28  ? 32  LYS   F CB     1 
ATOM   14754 C  CG     . LYS   F 4  32  ? 13.740  -48.750  -66.294  1.00 81.03  ? 32  LYS   F CG     1 
ATOM   14755 C  CD     . LYS   F 4  32  ? 14.549  -48.135  -67.420  1.00 82.69  ? 32  LYS   F CD     1 
ATOM   14756 C  CE     . LYS   F 4  32  ? 13.611  -47.621  -68.510  1.00 82.20  ? 32  LYS   F CE     1 
ATOM   14757 N  NZ     . LYS   F 4  32  ? 14.302  -46.725  -69.472  1.00 83.01  ? 32  LYS   F NZ     1 
ATOM   14758 N  N      . ASP   F 4  33  ? 13.222  -51.191  -64.413  1.00 79.10  ? 33  ASP   F N      1 
ATOM   14759 C  CA     . ASP   F 4  33  ? 14.106  -52.249  -63.929  1.00 78.76  ? 33  ASP   F CA     1 
ATOM   14760 C  C      . ASP   F 4  33  ? 13.460  -53.097  -62.829  1.00 77.42  ? 33  ASP   F C      1 
ATOM   14761 O  O      . ASP   F 4  33  ? 14.045  -54.093  -62.392  1.00 74.68  ? 33  ASP   F O      1 
ATOM   14762 C  CB     . ASP   F 4  33  ? 15.426  -51.580  -63.490  1.00 78.13  ? 33  ASP   F CB     1 
ATOM   14763 C  CG     . ASP   F 4  33  ? 16.396  -52.487  -62.714  1.00 91.95  ? 33  ASP   F CG     1 
ATOM   14764 O  OD1    . ASP   F 4  33  ? 16.015  -53.480  -62.059  1.00 90.42  ? 33  ASP   F OD1    1 
ATOM   14765 O  OD2    . ASP   F 4  33  ? 17.623  -52.221  -62.823  1.00 86.98  ? 33  ASP   F OD2    1 
ATOM   14766 N  N      . ASN   F 4  34  ? 12.244  -52.774  -62.422  1.00 76.86  ? 34  ASN   F N      1 
ATOM   14767 C  CA     . ASN   F 4  34  ? 11.529  -53.620  -61.474  1.00 72.97  ? 34  ASN   F CA     1 
ATOM   14768 C  C      . ASN   F 4  34  ? 11.247  -54.996  -62.081  1.00 70.70  ? 34  ASN   F C      1 
ATOM   14769 O  O      . ASN   F 4  34  ? 10.596  -55.080  -63.134  1.00 68.80  ? 34  ASN   F O      1 
ATOM   14770 C  CB     . ASN   F 4  34  ? 10.241  -52.936  -61.061  1.00 64.83  ? 34  ASN   F CB     1 
ATOM   14771 C  CG     . ASN   F 4  34  ? 9.700   -53.500  -59.792  1.00 65.36  ? 34  ASN   F CG     1 
ATOM   14772 O  OD1    . ASN   F 4  34  ? 9.828   -54.703  -59.551  1.00 68.26  ? 34  ASN   F OD1    1 
ATOM   14773 N  ND2    . ASN   F 4  34  ? 9.074   -52.658  -58.967  1.00 64.59  ? 34  ASN   F ND2    1 
ATOM   14774 N  N      . PRO   F 4  35  ? 11.694  -56.095  -61.462  1.00 69.14  ? 35  PRO   F N      1 
ATOM   14775 C  CA     . PRO   F 4  35  ? 11.513  -57.420  -62.081  1.00 71.08  ? 35  PRO   F CA     1 
ATOM   14776 C  C      . PRO   F 4  35  ? 10.150  -58.028  -61.824  1.00 67.51  ? 35  PRO   F C      1 
ATOM   14777 O  O      . PRO   F 4  35  ? 9.796   -59.036  -62.456  1.00 62.63  ? 35  PRO   F O      1 
ATOM   14778 C  CB     . PRO   F 4  35  ? 12.594  -58.259  -61.400  1.00 55.01  ? 35  PRO   F CB     1 
ATOM   14779 C  CG     . PRO   F 4  35  ? 12.575  -57.729  -60.015  1.00 64.25  ? 35  PRO   F CG     1 
ATOM   14780 C  CD     . PRO   F 4  35  ? 12.347  -56.215  -60.149  1.00 69.59  ? 35  PRO   F CD     1 
ATOM   14781 N  N      . ARG   F 4  36  ? 9.396   -57.461  -60.892  1.00 67.09  ? 36  ARG   F N      1 
ATOM   14782 C  CA     . ARG   F 4  36  ? 8.151   -58.055  -60.435  1.00 65.88  ? 36  ARG   F CA     1 
ATOM   14783 C  C      . ARG   F 4  36  ? 6.974   -57.555  -61.255  1.00 61.97  ? 36  ARG   F C      1 
ATOM   14784 O  O      . ARG   F 4  36  ? 5.965   -57.096  -60.725  1.00 61.45  ? 36  ARG   F O      1 
ATOM   14785 C  CB     . ARG   F 4  36  ? 7.979   -57.761  -58.954  1.00 68.16  ? 36  ARG   F CB     1 
ATOM   14786 C  CG     . ARG   F 4  36  ? 9.253   -58.032  -58.151  1.00 72.09  ? 36  ARG   F CG     1 
ATOM   14787 C  CD     . ARG   F 4  36  ? 8.920   -58.064  -56.686  1.00 79.10  ? 36  ARG   F CD     1 
ATOM   14788 N  NE     . ARG   F 4  36  ? 8.375   -59.367  -56.326  1.00 81.55  ? 36  ARG   F NE     1 
ATOM   14789 C  CZ     . ARG   F 4  36  ? 9.099   -60.403  -55.928  1.00 77.32  ? 36  ARG   F CZ     1 
ATOM   14790 N  NH1    . ARG   F 4  36  ? 10.396  -60.284  -55.685  1.00 68.61  ? 36  ARG   F NH1    1 
ATOM   14791 N  NH2    . ARG   F 4  36  ? 8.498   -61.581  -55.742  1.00 70.12  ? 36  ARG   F NH2    1 
ATOM   14792 N  N      . PHE   F 4  37  ? 7.110   -57.668  -62.574  1.00 63.37  ? 37  PHE   F N      1 
ATOM   14793 C  CA     . PHE   F 4  37  ? 6.093   -57.246  -63.523  1.00 62.26  ? 37  PHE   F CA     1 
ATOM   14794 C  C      . PHE   F 4  37  ? 5.349   -58.448  -64.096  1.00 61.66  ? 37  PHE   F C      1 
ATOM   14795 O  O      . PHE   F 4  37  ? 5.901   -59.546  -64.209  1.00 57.52  ? 37  PHE   F O      1 
ATOM   14796 C  CB     . PHE   F 4  37  ? 6.721   -56.443  -64.661  1.00 56.77  ? 37  PHE   F CB     1 
ATOM   14797 C  CG     . PHE   F 4  37  ? 7.672   -57.233  -65.486  1.00 59.16  ? 37  PHE   F CG     1 
ATOM   14798 C  CD1    . PHE   F 4  37  ? 7.220   -58.054  -66.497  1.00 61.95  ? 37  PHE   F CD1    1 
ATOM   14799 C  CD2    . PHE   F 4  37  ? 9.029   -57.167  -65.245  1.00 62.40  ? 37  PHE   F CD2    1 
ATOM   14800 C  CE1    . PHE   F 4  37  ? 8.111   -58.792  -67.253  1.00 58.37  ? 37  PHE   F CE1    1 
ATOM   14801 C  CE2    . PHE   F 4  37  ? 9.920   -57.893  -66.001  1.00 52.84  ? 37  PHE   F CE2    1 
ATOM   14802 C  CZ     . PHE   F 4  37  ? 9.460   -58.704  -67.006  1.00 53.72  ? 37  PHE   F CZ     1 
ATOM   14803 N  N      . ASN   F 4  38  ? 4.080   -58.220  -64.456  1.00 62.27  ? 38  ASN   F N      1 
ATOM   14804 C  CA     . ASN   F 4  38  ? 3.321   -59.173  -65.255  1.00 58.79  ? 38  ASN   F CA     1 
ATOM   14805 C  C      . ASN   F 4  38  ? 3.604   -58.994  -66.745  1.00 61.53  ? 38  ASN   F C      1 
ATOM   14806 O  O      . ASN   F 4  38  ? 3.661   -59.975  -67.501  1.00 55.97  ? 38  ASN   F O      1 
ATOM   14807 C  CB     . ASN   F 4  38  ? 1.825   -59.012  -64.981  1.00 54.68  ? 38  ASN   F CB     1 
ATOM   14808 C  CG     . ASN   F 4  38  ? 1.445   -59.372  -63.545  1.00 66.50  ? 38  ASN   F CG     1 
ATOM   14809 O  OD1    . ASN   F 4  38  ? 0.746   -58.620  -62.853  1.00 63.47  ? 38  ASN   F OD1    1 
ATOM   14810 N  ND2    . ASN   F 4  38  ? 1.899   -60.532  -63.093  1.00 68.45  ? 38  ASN   F ND2    1 
ATOM   14811 N  N      . LEU   F 4  39  ? 3.798   -57.754  -67.184  1.00 59.59  ? 39  LEU   F N      1 
ATOM   14812 C  CA     . LEU   F 4  39  ? 3.739   -57.418  -68.599  1.00 59.26  ? 39  LEU   F CA     1 
ATOM   14813 C  C      . LEU   F 4  39  ? 4.937   -56.563  -68.953  1.00 56.21  ? 39  LEU   F C      1 
ATOM   14814 O  O      . LEU   F 4  39  ? 5.114   -55.487  -68.382  1.00 61.60  ? 39  LEU   F O      1 
ATOM   14815 C  CB     . LEU   F 4  39  ? 2.441   -56.671  -68.931  1.00 57.72  ? 39  LEU   F CB     1 
ATOM   14816 C  CG     . LEU   F 4  39  ? 2.325   -56.167  -70.372  1.00 61.57  ? 39  LEU   F CG     1 
ATOM   14817 C  CD1    . LEU   F 4  39  ? 2.023   -57.311  -71.340  1.00 57.61  ? 39  LEU   F CD1    1 
ATOM   14818 C  CD2    . LEU   F 4  39  ? 1.270   -55.088  -70.462  1.00 61.29  ? 39  LEU   F CD2    1 
ATOM   14819 N  N      . MET   F 4  40  ? 5.741   -57.018  -69.894  1.00 51.17  ? 40  MET   F N      1 
ATOM   14820 C  CA     . MET   F 4  40  ? 6.862   -56.228  -70.387  1.00 59.37  ? 40  MET   F CA     1 
ATOM   14821 C  C      . MET   F 4  40  ? 6.507   -55.665  -71.755  1.00 62.88  ? 40  MET   F C      1 
ATOM   14822 O  O      . MET   F 4  40  ? 6.526   -56.393  -72.753  1.00 61.31  ? 40  MET   F O      1 
ATOM   14823 C  CB     . MET   F 4  40  ? 8.152   -57.036  -70.487  1.00 50.43  ? 40  MET   F CB     1 
ATOM   14824 C  CG     . MET   F 4  40  ? 9.190   -56.293  -71.277  1.00 50.53  ? 40  MET   F CG     1 
ATOM   14825 S  SD     . MET   F 4  40  ? 10.856  -56.858  -70.991  1.00 59.65  ? 40  MET   F SD     1 
ATOM   14826 C  CE     . MET   F 4  40  ? 10.873  -56.871  -69.208  1.00 57.85  ? 40  MET   F CE     1 
ATOM   14827 N  N      . LEU   F 4  41  ? 6.195   -54.374  -71.804  1.00 59.86  ? 41  LEU   F N      1 
ATOM   14828 C  CA     . LEU   F 4  41  ? 6.241   -53.637  -73.062  1.00 59.44  ? 41  LEU   F CA     1 
ATOM   14829 C  C      . LEU   F 4  41  ? 7.706   -53.297  -73.303  1.00 62.69  ? 41  LEU   F C      1 
ATOM   14830 O  O      . LEU   F 4  41  ? 8.227   -52.333  -72.747  1.00 72.19  ? 41  LEU   F O      1 
ATOM   14831 C  CB     . LEU   F 4  41  ? 5.356   -52.403  -72.994  1.00 58.94  ? 41  LEU   F CB     1 
ATOM   14832 C  CG     . LEU   F 4  41  ? 3.948   -52.749  -72.529  1.00 62.00  ? 41  LEU   F CG     1 
ATOM   14833 C  CD1    . LEU   F 4  41  ? 3.073   -51.504  -72.392  1.00 67.43  ? 41  LEU   F CD1    1 
ATOM   14834 C  CD2    . LEU   F 4  41  ? 3.334   -53.761  -73.479  1.00 61.01  ? 41  LEU   F CD2    1 
ATOM   14835 N  N      . GLY   F 4  42  ? 8.386   -54.105  -74.123  1.00 59.37  ? 42  GLY   F N      1 
ATOM   14836 C  CA     . GLY   F 4  42  ? 9.833   -54.150  -74.127  1.00 58.72  ? 42  GLY   F CA     1 
ATOM   14837 C  C      . GLY   F 4  42  ? 10.487  -53.227  -75.137  1.00 57.58  ? 42  GLY   F C      1 
ATOM   14838 O  O      . GLY   F 4  42  ? 9.839   -52.565  -75.942  1.00 61.55  ? 42  GLY   F O      1 
ATOM   14839 N  N      . GLU   F 4  43  ? 11.815  -53.199  -75.079  1.00 57.87  ? 43  GLU   F N      1 
ATOM   14840 C  CA     . GLU   F 4  43  ? 12.618  -52.435  -76.017  1.00 59.63  ? 43  GLU   F CA     1 
ATOM   14841 C  C      . GLU   F 4  43  ? 12.662  -53.141  -77.371  1.00 59.86  ? 43  GLU   F C      1 
ATOM   14842 O  O      . GLU   F 4  43  ? 12.268  -54.293  -77.513  1.00 60.53  ? 43  GLU   F O      1 
ATOM   14843 C  CB     . GLU   F 4  43  ? 14.034  -52.233  -75.469  1.00 54.79  ? 43  GLU   F CB     1 
ATOM   14844 C  CG     . GLU   F 4  43  ? 14.817  -53.520  -75.175  1.00 61.47  ? 43  GLU   F CG     1 
ATOM   14845 C  CD     . GLU   F 4  43  ? 14.918  -53.842  -73.675  1.00 63.57  ? 43  GLU   F CD     1 
ATOM   14846 O  OE1    . GLU   F 4  43  ? 13.860  -53.953  -73.011  1.00 57.16  ? 43  GLU   F OE1    1 
ATOM   14847 O  OE2    . GLU   F 4  43  ? 16.054  -53.976  -73.157  1.00 64.07  ? 43  GLU   F OE2    1 
ATOM   14848 N  N      . ARG   F 4  44  ? 13.159  -52.430  -78.381  1.00 69.98  ? 44  ARG   F N      1 
ATOM   14849 C  CA     . ARG   F 4  44  ? 13.201  -52.965  -79.737  1.00 69.58  ? 44  ARG   F CA     1 
ATOM   14850 C  C      . ARG   F 4  44  ? 14.469  -53.765  -80.024  1.00 68.28  ? 44  ARG   F C      1 
ATOM   14851 O  O      . ARG   F 4  44  ? 14.421  -54.745  -80.771  1.00 73.67  ? 44  ARG   F O      1 
ATOM   14852 C  CB     . ARG   F 4  44  ? 13.060  -51.835  -80.763  1.00 73.13  ? 44  ARG   F CB     1 
ATOM   14853 C  CG     . ARG   F 4  44  ? 11.637  -51.611  -81.284  1.00 71.41  ? 44  ARG   F CG     1 
ATOM   14854 C  CD     . ARG   F 4  44  ? 11.532  -50.328  -82.123  1.00 80.26  ? 44  ARG   F CD     1 
ATOM   14855 N  NE     . ARG   F 4  44  ? 12.074  -50.470  -83.473  1.00 78.67  ? 44  ARG   F NE     1 
ATOM   14856 C  CZ     . ARG   F 4  44  ? 11.854  -49.614  -84.466  1.00 86.25  ? 44  ARG   F CZ     1 
ATOM   14857 N  NH1    . ARG   F 4  44  ? 11.078  -48.552  -84.310  1.00 82.47  ? 44  ARG   F NH1    1 
ATOM   14858 N  NH2    . ARG   F 4  44  ? 12.436  -49.824  -85.646  1.00 89.29  ? 44  ARG   F NH2    1 
ATOM   14859 N  N      . ASN   F 4  45  ? 15.608  -53.374  -79.472  1.00 67.85  ? 45  ASN   F N      1 
ATOM   14860 C  CA     . ASN   F 4  45  ? 16.835  -54.128  -79.668  1.00 73.01  ? 45  ASN   F CA     1 
ATOM   14861 C  C      . ASN   F 4  45  ? 17.301  -54.715  -78.340  1.00 74.70  ? 45  ASN   F C      1 
ATOM   14862 O  O      . ASN   F 4  45  ? 17.127  -54.110  -77.279  1.00 74.51  ? 45  ASN   F O      1 
ATOM   14863 C  CB     . ASN   F 4  45  ? 17.946  -53.259  -80.289  1.00 74.04  ? 45  ASN   F CB     1 
ATOM   14864 C  CG     . ASN   F 4  45  ? 19.037  -52.876  -79.284  1.00 82.07  ? 45  ASN   F CG     1 
ATOM   14865 O  OD1    . ASN   F 4  45  ? 18.756  -52.327  -78.214  1.00 85.34  ? 45  ASN   F OD1    1 
ATOM   14866 N  ND2    . ASN   F 4  45  ? 20.287  -53.193  -79.618  1.00 76.53  ? 45  ASN   F ND2    1 
ATOM   14867 N  N      . ARG   F 4  46  ? 17.882  -55.912  -78.413  1.00 72.79  ? 46  ARG   F N      1 
ATOM   14868 C  CA     . ARG   F 4  46  ? 18.421  -56.599  -77.241  1.00 70.62  ? 46  ARG   F CA     1 
ATOM   14869 C  C      . ARG   F 4  46  ? 17.406  -56.683  -76.102  1.00 68.06  ? 46  ARG   F C      1 
ATOM   14870 O  O      . ARG   F 4  46  ? 17.766  -56.612  -74.921  1.00 65.63  ? 46  ARG   F O      1 
ATOM   14871 C  CB     . ARG   F 4  46  ? 19.715  -55.935  -76.761  1.00 79.40  ? 46  ARG   F CB     1 
ATOM   14872 C  CG     . ARG   F 4  46  ? 20.707  -56.910  -76.132  1.00 81.98  ? 46  ARG   F CG     1 
ATOM   14873 C  CD     . ARG   F 4  46  ? 22.110  -56.336  -76.139  1.00 86.50  ? 46  ARG   F CD     1 
ATOM   14874 N  NE     . ARG   F 4  46  ? 22.664  -56.267  -77.486  1.00 83.99  ? 46  ARG   F NE     1 
ATOM   14875 C  CZ     . ARG   F 4  46  ? 23.386  -57.224  -78.056  1.00 84.76  ? 46  ARG   F CZ     1 
ATOM   14876 N  NH1    . ARG   F 4  46  ? 23.648  -58.364  -77.432  1.00 71.58  ? 46  ARG   F NH1    1 
ATOM   14877 N  NH2    . ARG   F 4  46  ? 23.868  -57.027  -79.281  1.00 91.84  ? 46  ARG   F NH2    1 
ATOM   14878 N  N      . LEU   F 4  47  ? 16.130  -56.834  -76.441  1.00 60.52  ? 47  LEU   F N      1 
ATOM   14879 C  CA     . LEU   F 4  47  ? 15.151  -57.166  -75.423  1.00 56.58  ? 47  LEU   F CA     1 
ATOM   14880 C  C      . LEU   F 4  47  ? 15.612  -58.425  -74.692  1.00 59.71  ? 47  LEU   F C      1 
ATOM   14881 O  O      . LEU   F 4  47  ? 15.965  -59.417  -75.347  1.00 59.52  ? 47  LEU   F O      1 
ATOM   14882 C  CB     . LEU   F 4  47  ? 13.786  -57.388  -76.061  1.00 56.03  ? 47  LEU   F CB     1 
ATOM   14883 C  CG     . LEU   F 4  47  ? 12.612  -57.459  -75.096  1.00 54.27  ? 47  LEU   F CG     1 
ATOM   14884 C  CD1    . LEU   F 4  47  ? 11.297  -57.249  -75.848  1.00 53.66  ? 47  LEU   F CD1    1 
ATOM   14885 C  CD2    . LEU   F 4  47  ? 12.625  -58.790  -74.362  1.00 51.10  ? 47  LEU   F CD2    1 
ATOM   14886 N  N      . PRO   F 4  48  ? 15.636  -58.428  -73.342  1.00 59.74  ? 48  PRO   F N      1 
ATOM   14887 C  CA     . PRO   F 4  48  ? 16.279  -59.538  -72.587  1.00 51.81  ? 48  PRO   F CA     1 
ATOM   14888 C  C      . PRO   F 4  48  ? 15.377  -60.755  -72.369  1.00 50.66  ? 48  PRO   F C      1 
ATOM   14889 O  O      . PRO   F 4  48  ? 14.940  -61.077  -71.254  1.00 52.08  ? 48  PRO   F O      1 
ATOM   14890 C  CB     . PRO   F 4  48  ? 16.664  -58.844  -71.279  1.00 53.19  ? 48  PRO   F CB     1 
ATOM   14891 C  CG     . PRO   F 4  48  ? 15.568  -57.818  -71.063  1.00 52.30  ? 48  PRO   F CG     1 
ATOM   14892 C  CD     . PRO   F 4  48  ? 15.129  -57.371  -72.444  1.00 59.16  ? 48  PRO   F CD     1 
ATOM   14893 N  N      . PHE   F 4  49  ? 15.097  -61.490  -73.449  1.00 54.61  ? 49  PHE   F N      1 
ATOM   14894 C  CA     . PHE   F 4  49  ? 14.122  -62.577  -73.376  1.00 47.46  ? 49  PHE   F CA     1 
ATOM   14895 C  C      . PHE   F 4  49  ? 14.535  -63.665  -72.387  1.00 48.04  ? 49  PHE   F C      1 
ATOM   14896 O  O      . PHE   F 4  49  ? 13.671  -64.320  -71.799  1.00 52.92  ? 49  PHE   F O      1 
ATOM   14897 C  CB     . PHE   F 4  49  ? 13.909  -63.195  -74.757  1.00 46.52  ? 49  PHE   F CB     1 
ATOM   14898 C  CG     . PHE   F 4  49  ? 13.111  -62.344  -75.707  1.00 44.90  ? 49  PHE   F CG     1 
ATOM   14899 C  CD1    . PHE   F 4  49  ? 11.740  -62.221  -75.568  1.00 43.02  ? 49  PHE   F CD1    1 
ATOM   14900 C  CD2    . PHE   F 4  49  ? 13.729  -61.708  -76.774  1.00 46.37  ? 49  PHE   F CD2    1 
ATOM   14901 C  CE1    . PHE   F 4  49  ? 10.991  -61.465  -76.470  1.00 44.64  ? 49  PHE   F CE1    1 
ATOM   14902 C  CE2    . PHE   F 4  49  ? 12.998  -60.949  -77.674  1.00 44.82  ? 49  PHE   F CE2    1 
ATOM   14903 C  CZ     . PHE   F 4  49  ? 11.626  -60.827  -77.521  1.00 48.95  ? 49  PHE   F CZ     1 
ATOM   14904 N  N      . GLY   F 4  50  ? 15.836  -63.895  -72.200  1.00 49.74  ? 50  GLY   F N      1 
ATOM   14905 C  CA     . GLY   F 4  50  ? 16.301  -64.932  -71.290  1.00 45.17  ? 50  GLY   F CA     1 
ATOM   14906 C  C      . GLY   F 4  50  ? 16.020  -64.672  -69.819  1.00 49.13  ? 50  GLY   F C      1 
ATOM   14907 O  O      . GLY   F 4  50  ? 16.269  -65.548  -68.981  1.00 44.64  ? 50  GLY   F O      1 
ATOM   14908 N  N      . ARG   F 4  51  ? 15.507  -63.487  -69.493  1.00 50.22  ? 51  ARG   F N      1 
ATOM   14909 C  CA     . ARG   F 4  51  ? 15.158  -63.117  -68.133  1.00 52.54  ? 51  ARG   F CA     1 
ATOM   14910 C  C      . ARG   F 4  51  ? 13.663  -63.174  -67.859  1.00 51.41  ? 51  ARG   F C      1 
ATOM   14911 O  O      . ARG   F 4  51  ? 13.267  -63.029  -66.698  1.00 59.39  ? 51  ARG   F O      1 
ATOM   14912 C  CB     . ARG   F 4  51  ? 15.687  -61.707  -67.822  1.00 54.85  ? 51  ARG   F CB     1 
ATOM   14913 C  CG     . ARG   F 4  51  ? 17.048  -61.718  -67.136  1.00 58.44  ? 51  ARG   F CG     1 
ATOM   14914 C  CD     . ARG   F 4  51  ? 17.956  -60.551  -67.530  1.00 57.33  ? 51  ARG   F CD     1 
ATOM   14915 N  NE     . ARG   F 4  51  ? 17.333  -59.254  -67.294  1.00 55.96  ? 51  ARG   F NE     1 
ATOM   14916 C  CZ     . ARG   F 4  51  ? 17.848  -58.100  -67.695  1.00 58.42  ? 51  ARG   F CZ     1 
ATOM   14917 N  NH1    . ARG   F 4  51  ? 19.024  -58.042  -68.310  1.00 52.66  ? 51  ARG   F NH1    1 
ATOM   14918 N  NH2    . ARG   F 4  51  ? 17.170  -56.978  -67.471  1.00 62.23  ? 51  ARG   F NH2    1 
ATOM   14919 N  N      . LEU   F 4  52  ? 12.825  -63.391  -68.873  1.00 47.11  ? 52  LEU   F N      1 
ATOM   14920 C  CA     . LEU   F 4  52  ? 11.385  -63.461  -68.636  1.00 52.60  ? 52  LEU   F CA     1 
ATOM   14921 C  C      . LEU   F 4  52  ? 10.981  -64.858  -68.165  1.00 48.19  ? 52  LEU   F C      1 
ATOM   14922 O  O      . LEU   F 4  52  ? 11.645  -65.852  -68.473  1.00 52.51  ? 52  LEU   F O      1 
ATOM   14923 C  CB     . LEU   F 4  52  ? 10.619  -63.076  -69.896  1.00 47.83  ? 52  LEU   F CB     1 
ATOM   14924 C  CG     . LEU   F 4  52  ? 11.096  -61.748  -70.489  1.00 48.20  ? 52  LEU   F CG     1 
ATOM   14925 C  CD1    . LEU   F 4  52  ? 10.594  -61.592  -71.911  1.00 50.68  ? 52  LEU   F CD1    1 
ATOM   14926 C  CD2    . LEU   F 4  52  ? 10.627  -60.575  -69.631  1.00 50.82  ? 52  LEU   F CD2    1 
ATOM   14927 N  N      . GLY   F 4  53  ? 9.906   -64.917  -67.379  1.00 46.55  ? 53  GLY   F N      1 
ATOM   14928 C  CA     . GLY   F 4  53  ? 9.387   -66.182  -66.880  1.00 40.61  ? 53  GLY   F CA     1 
ATOM   14929 C  C      . GLY   F 4  53  ? 10.241  -66.907  -65.859  1.00 46.46  ? 53  GLY   F C      1 
ATOM   14930 O  O      . GLY   F 4  53  ? 10.259  -68.142  -65.846  1.00 45.50  ? 53  GLY   F O      1 
ATOM   14931 N  N      . HIS   F 4  54  ? 10.954  -66.183  -64.993  1.00 52.02  ? 54  HIS   F N      1 
ATOM   14932 C  CA     . HIS   F 4  54  ? 11.627  -66.822  -63.863  1.00 48.26  ? 54  HIS   F CA     1 
ATOM   14933 C  C      . HIS   F 4  54  ? 11.271  -66.161  -62.537  1.00 48.38  ? 54  HIS   F C      1 
ATOM   14934 O  O      . HIS   F 4  54  ? 12.080  -66.159  -61.616  1.00 48.00  ? 54  HIS   F O      1 
ATOM   14935 C  CB     . HIS   F 4  54  ? 13.143  -66.808  -64.011  1.00 48.17  ? 54  HIS   F CB     1 
ATOM   14936 C  CG     . HIS   F 4  54  ? 13.654  -67.463  -65.249  1.00 50.49  ? 54  HIS   F CG     1 
ATOM   14937 N  ND1    . HIS   F 4  54  ? 13.970  -68.805  -65.301  1.00 44.44  ? 54  HIS   F ND1    1 
ATOM   14938 C  CD2    . HIS   F 4  54  ? 13.957  -66.950  -66.467  1.00 45.75  ? 54  HIS   F CD2    1 
ATOM   14939 C  CE1    . HIS   F 4  54  ? 14.415  -69.095  -66.512  1.00 47.92  ? 54  HIS   F CE1    1 
ATOM   14940 N  NE2    . HIS   F 4  54  ? 14.425  -67.987  -67.235  1.00 45.30  ? 54  HIS   F NE2    1 
ATOM   14941 N  N      . GLU   F 4  55  ? 10.082  -65.590  -62.419  1.00 56.63  ? 55  GLU   F N      1 
ATOM   14942 C  CA     . GLU   F 4  55  ? 9.689   -64.926  -61.181  1.00 50.70  ? 55  GLU   F CA     1 
ATOM   14943 C  C      . GLU   F 4  55  ? 8.598   -65.748  -60.524  1.00 48.93  ? 55  GLU   F C      1 
ATOM   14944 O  O      . GLU   F 4  55  ? 7.452   -65.731  -61.000  1.00 50.83  ? 55  GLU   F O      1 
ATOM   14945 C  CB     . GLU   F 4  55  ? 9.188   -63.504  -61.452  1.00 52.84  ? 55  GLU   F CB     1 
ATOM   14946 C  CG     . GLU   F 4  55  ? 10.268  -62.447  -61.488  1.00 50.38  ? 55  GLU   F CG     1 
ATOM   14947 C  CD     . GLU   F 4  55  ? 11.139  -62.457  -60.249  1.00 59.53  ? 55  GLU   F CD     1 
ATOM   14948 O  OE1    . GLU   F 4  55  ? 10.678  -62.924  -59.178  1.00 61.99  ? 55  GLU   F OE1    1 
ATOM   14949 O  OE2    . GLU   F 4  55  ? 12.286  -61.972  -60.336  1.00 64.29  ? 55  GLU   F OE2    1 
ATOM   14950 N  N      . PRO   F 4  56  ? 8.885   -66.475  -59.451  1.00 48.33  ? 56  PRO   F N      1 
ATOM   14951 C  CA     . PRO   F 4  56  ? 7.850   -67.319  -58.846  1.00 51.11  ? 56  PRO   F CA     1 
ATOM   14952 C  C      . PRO   F 4  56  ? 6.596   -66.516  -58.525  1.00 52.62  ? 56  PRO   F C      1 
ATOM   14953 O  O      . PRO   F 4  56  ? 6.663   -65.369  -58.082  1.00 56.94  ? 56  PRO   F O      1 
ATOM   14954 C  CB     . PRO   F 4  56  ? 8.527   -67.881  -57.584  1.00 54.38  ? 56  PRO   F CB     1 
ATOM   14955 C  CG     . PRO   F 4  56  ? 9.871   -67.224  -57.483  1.00 47.49  ? 56  PRO   F CG     1 
ATOM   14956 C  CD     . PRO   F 4  56  ? 10.206  -66.678  -58.839  1.00 51.47  ? 56  PRO   F CD     1 
ATOM   14957 N  N      . GLY   F 4  57  ? 5.442   -67.117  -58.806  1.00 55.22  ? 57  GLY   F N      1 
ATOM   14958 C  CA     . GLY   F 4  57  ? 4.171   -66.457  -58.600  1.00 55.31  ? 57  GLY   F CA     1 
ATOM   14959 C  C      . GLY   F 4  57  ? 3.868   -65.289  -59.513  1.00 59.48  ? 57  GLY   F C      1 
ATOM   14960 O  O      . GLY   F 4  57  ? 2.990   -64.481  -59.201  1.00 62.10  ? 57  GLY   F O      1 
ATOM   14961 N  N      . LEU   F 4  58  ? 4.561   -65.168  -60.640  1.00 59.41  ? 58  LEU   F N      1 
ATOM   14962 C  CA     . LEU   F 4  58  ? 4.304   -64.093  -61.593  1.00 57.74  ? 58  LEU   F CA     1 
ATOM   14963 C  C      . LEU   F 4  58  ? 4.144   -64.696  -62.978  1.00 59.58  ? 58  LEU   F C      1 
ATOM   14964 O  O      . LEU   F 4  58  ? 5.106   -65.229  -63.539  1.00 65.21  ? 58  LEU   F O      1 
ATOM   14965 C  CB     . LEU   F 4  58  ? 5.433   -63.065  -61.579  1.00 60.35  ? 58  LEU   F CB     1 
ATOM   14966 C  CG     . LEU   F 4  58  ? 5.223   -61.907  -60.614  1.00 61.07  ? 58  LEU   F CG     1 
ATOM   14967 C  CD1    . LEU   F 4  58  ? 6.213   -60.785  -60.904  1.00 57.12  ? 58  LEU   F CD1    1 
ATOM   14968 C  CD2    . LEU   F 4  58  ? 3.787   -61.432  -60.728  1.00 59.41  ? 58  LEU   F CD2    1 
ATOM   14969 N  N      . VAL   F 4  59  ? 2.932   -64.633  -63.520  1.00 58.94  ? 59  VAL   F N      1 
ATOM   14970 C  CA     . VAL   F 4  59  ? 2.716   -64.950  -64.926  1.00 56.32  ? 59  VAL   F CA     1 
ATOM   14971 C  C      . VAL   F 4  59  ? 3.218   -63.768  -65.743  1.00 57.23  ? 59  VAL   F C      1 
ATOM   14972 O  O      . VAL   F 4  59  ? 2.713   -62.650  -65.601  1.00 59.44  ? 59  VAL   F O      1 
ATOM   14973 C  CB     . VAL   F 4  59  ? 1.239   -65.236  -65.217  1.00 53.99  ? 59  VAL   F CB     1 
ATOM   14974 C  CG1    . VAL   F 4  59  ? 0.977   -65.220  -66.724  1.00 44.44  ? 59  VAL   F CG1    1 
ATOM   14975 C  CG2    . VAL   F 4  59  ? 0.829   -66.550  -64.597  1.00 51.53  ? 59  VAL   F CG2    1 
ATOM   14976 N  N      . GLN   F 4  60  ? 4.227   -64.002  -66.579  1.00 50.82  ? 60  GLN   F N      1 
ATOM   14977 C  CA     . GLN   F 4  60  ? 4.876   -62.926  -67.308  1.00 53.59  ? 60  GLN   F CA     1 
ATOM   14978 C  C      . GLN   F 4  60  ? 4.562   -63.032  -68.793  1.00 49.90  ? 60  GLN   F C      1 
ATOM   14979 O  O      . GLN   F 4  60  ? 4.552   -64.127  -69.360  1.00 52.44  ? 60  GLN   F O      1 
ATOM   14980 C  CB     . GLN   F 4  60  ? 6.385   -62.936  -67.055  1.00 51.37  ? 60  GLN   F CB     1 
ATOM   14981 C  CG     . GLN   F 4  60  ? 6.730   -62.543  -65.634  1.00 51.84  ? 60  GLN   F CG     1 
ATOM   14982 C  CD     . GLN   F 4  60  ? 8.198   -62.219  -65.428  1.00 53.50  ? 60  GLN   F CD     1 
ATOM   14983 O  OE1    . GLN   F 4  60  ? 9.069   -62.807  -66.078  1.00 52.04  ? 60  GLN   F OE1    1 
ATOM   14984 N  NE2    . GLN   F 4  60  ? 8.481   -61.259  -64.527  1.00 45.47  ? 60  GLN   F NE2    1 
ATOM   14985 N  N      . LEU   F 4  61  ? 4.279   -61.882  -69.402  1.00 57.78  ? 61  LEU   F N      1 
ATOM   14986 C  CA     . LEU   F 4  61  ? 3.880   -61.751  -70.798  1.00 54.89  ? 61  LEU   F CA     1 
ATOM   14987 C  C      . LEU   F 4  61  ? 4.630   -60.568  -71.389  1.00 47.92  ? 61  LEU   F C      1 
ATOM   14988 O  O      . LEU   F 4  61  ? 4.883   -59.582  -70.698  1.00 52.47  ? 61  LEU   F O      1 
ATOM   14989 C  CB     . LEU   F 4  61  ? 2.355   -61.545  -70.916  1.00 52.95  ? 61  LEU   F CB     1 
ATOM   14990 C  CG     . LEU   F 4  61  ? 1.694   -61.192  -72.246  1.00 52.28  ? 61  LEU   F CG     1 
ATOM   14991 C  CD1    . LEU   F 4  61  ? 1.825   -62.334  -73.244  1.00 55.26  ? 61  LEU   F CD1    1 
ATOM   14992 C  CD2    . LEU   F 4  61  ? 0.239   -60.881  -72.017  1.00 50.35  ? 61  LEU   F CD2    1 
ATOM   14993 N  N      . VAL   F 4  62  ? 5.007   -60.663  -72.655  1.00 50.08  ? 62  VAL   F N      1 
ATOM   14994 C  CA     . VAL   F 4  62  ? 5.786   -59.605  -73.287  1.00 54.00  ? 62  VAL   F CA     1 
ATOM   14995 C  C      . VAL   F 4  62  ? 5.201   -59.370  -74.676  1.00 56.23  ? 62  VAL   F C      1 
ATOM   14996 O  O      . VAL   F 4  62  ? 4.519   -60.228  -75.245  1.00 54.45  ? 62  VAL   F O      1 
ATOM   14997 C  CB     . VAL   F 4  62  ? 7.301   -59.947  -73.337  1.00 49.77  ? 62  VAL   F CB     1 
ATOM   14998 C  CG1    . VAL   F 4  62  ? 7.526   -61.352  -73.907  1.00 53.26  ? 62  VAL   F CG1    1 
ATOM   14999 C  CG2    . VAL   F 4  62  ? 8.124   -58.881  -74.061  1.00 44.59  ? 62  VAL   F CG2    1 
ATOM   15000 N  N      . ASN   F 4  63  ? 5.430   -58.163  -75.198  1.00 56.08  ? 63  ASN   F N      1 
ATOM   15001 C  CA     . ASN   F 4  63  ? 4.801   -57.700  -76.429  1.00 55.55  ? 63  ASN   F CA     1 
ATOM   15002 C  C      . ASN   F 4  63  ? 5.714   -57.863  -77.646  1.00 53.79  ? 63  ASN   F C      1 
ATOM   15003 O  O      . ASN   F 4  63  ? 5.583   -57.117  -78.624  1.00 51.99  ? 63  ASN   F O      1 
ATOM   15004 C  CB     . ASN   F 4  63  ? 4.374   -56.240  -76.287  1.00 56.64  ? 63  ASN   F CB     1 
ATOM   15005 C  CG     . ASN   F 4  63  ? 5.568   -55.286  -76.317  1.00 57.91  ? 63  ASN   F CG     1 
ATOM   15006 O  OD1    . ASN   F 4  63  ? 6.677   -55.661  -75.938  1.00 56.93  ? 63  ASN   F OD1    1 
ATOM   15007 N  ND2    . ASN   F 4  63  ? 5.356   -54.077  -76.807  1.00 52.95  ? 63  ASN   F ND2    1 
ATOM   15008 N  N      . TYR   F 4  64  ? 6.639   -58.823  -77.604  1.00 49.96  ? 64  TYR   F N      1 
ATOM   15009 C  CA     . TYR   F 4  64  ? 7.430   -59.194  -78.772  1.00 51.88  ? 64  TYR   F CA     1 
ATOM   15010 C  C      . TYR   F 4  64  ? 7.612   -60.706  -78.798  1.00 50.46  ? 64  TYR   F C      1 
ATOM   15011 O  O      . TYR   F 4  64  ? 7.438   -61.384  -77.783  1.00 51.22  ? 64  TYR   F O      1 
ATOM   15012 C  CB     . TYR   F 4  64  ? 8.793   -58.497  -78.787  1.00 46.73  ? 64  TYR   F CB     1 
ATOM   15013 C  CG     . TYR   F 4  64  ? 8.727   -57.102  -79.355  1.00 56.32  ? 64  TYR   F CG     1 
ATOM   15014 C  CD1    . TYR   F 4  64  ? 8.889   -56.882  -80.718  1.00 58.51  ? 64  TYR   F CD1    1 
ATOM   15015 C  CD2    . TYR   F 4  64  ? 8.492   -55.998  -78.529  1.00 59.89  ? 64  TYR   F CD2    1 
ATOM   15016 C  CE1    . TYR   F 4  64  ? 8.823   -55.602  -81.254  1.00 65.04  ? 64  TYR   F CE1    1 
ATOM   15017 C  CE2    . TYR   F 4  64  ? 8.421   -54.712  -79.051  1.00 57.92  ? 64  TYR   F CE2    1 
ATOM   15018 C  CZ     . TYR   F 4  64  ? 8.585   -54.518  -80.418  1.00 64.96  ? 64  TYR   F CZ     1 
ATOM   15019 O  OH     . TYR   F 4  64  ? 8.519   -53.248  -80.965  1.00 64.91  ? 64  TYR   F OH     1 
ATOM   15020 N  N      . TYR   F 4  65  ? 7.962   -61.227  -79.986  1.00 52.32  ? 65  TYR   F N      1 
ATOM   15021 C  CA     . TYR   F 4  65  ? 8.175   -62.655  -80.234  1.00 44.93  ? 65  TYR   F CA     1 
ATOM   15022 C  C      . TYR   F 4  65  ? 9.652   -62.880  -80.543  1.00 47.74  ? 65  TYR   F C      1 
ATOM   15023 O  O      . TYR   F 4  65  ? 10.125  -62.523  -81.629  1.00 50.71  ? 65  TYR   F O      1 
ATOM   15024 C  CB     . TYR   F 4  65  ? 7.301   -63.139  -81.391  1.00 47.52  ? 65  TYR   F CB     1 
ATOM   15025 C  CG     . TYR   F 4  65  ? 6.033   -63.890  -80.992  1.00 46.42  ? 65  TYR   F CG     1 
ATOM   15026 C  CD1    . TYR   F 4  65  ? 6.067   -65.252  -80.708  1.00 46.64  ? 65  TYR   F CD1    1 
ATOM   15027 C  CD2    . TYR   F 4  65  ? 4.811   -63.243  -80.918  1.00 41.36  ? 65  TYR   F CD2    1 
ATOM   15028 C  CE1    . TYR   F 4  65  ? 4.931   -65.940  -80.336  1.00 45.44  ? 65  TYR   F CE1    1 
ATOM   15029 C  CE2    . TYR   F 4  65  ? 3.654   -63.928  -80.548  1.00 44.65  ? 65  TYR   F CE2    1 
ATOM   15030 C  CZ     . TYR   F 4  65  ? 3.721   -65.280  -80.269  1.00 48.36  ? 65  TYR   F CZ     1 
ATOM   15031 O  OH     . TYR   F 4  65  ? 2.590   -65.983  -79.902  1.00 49.24  ? 65  TYR   F OH     1 
ATOM   15032 N  N      . ARG   F 4  66  ? 10.378  -63.454  -79.585  1.00 47.82  ? 66  ARG   F N      1 
ATOM   15033 C  CA     . ARG   F 4  66  ? 11.763  -63.843  -79.812  1.00 44.88  ? 66  ARG   F CA     1 
ATOM   15034 C  C      . ARG   F 4  66  ? 11.870  -64.684  -81.077  1.00 50.68  ? 66  ARG   F C      1 
ATOM   15035 O  O      . ARG   F 4  66  ? 11.162  -65.687  -81.238  1.00 53.98  ? 66  ARG   F O      1 
ATOM   15036 C  CB     . ARG   F 4  66  ? 12.291  -64.625  -78.608  1.00 43.55  ? 66  ARG   F CB     1 
ATOM   15037 C  CG     . ARG   F 4  66  ? 13.796  -64.804  -78.561  1.00 37.13  ? 66  ARG   F CG     1 
ATOM   15038 C  CD     . ARG   F 4  66  ? 14.196  -65.459  -77.260  1.00 38.05  ? 66  ARG   F CD     1 
ATOM   15039 N  NE     . ARG   F 4  66  ? 15.636  -65.506  -77.063  1.00 44.18  ? 66  ARG   F NE     1 
ATOM   15040 C  CZ     . ARG   F 4  66  ? 16.261  -66.411  -76.321  1.00 46.29  ? 66  ARG   F CZ     1 
ATOM   15041 N  NH1    . ARG   F 4  66  ? 15.592  -67.341  -75.660  1.00 47.49  ? 66  ARG   F NH1    1 
ATOM   15042 N  NH2    . ARG   F 4  66  ? 17.590  -66.387  -76.247  1.00 40.69  ? 66  ARG   F NH2    1 
ATOM   15043 N  N      . GLY   F 4  67  ? 12.762  -64.275  -81.973  1.00 47.12  ? 67  GLY   F N      1 
ATOM   15044 C  CA     . GLY   F 4  67  ? 12.889  -64.879  -83.274  1.00 47.07  ? 67  GLY   F CA     1 
ATOM   15045 C  C      . GLY   F 4  67  ? 12.112  -64.184  -84.377  1.00 55.76  ? 67  GLY   F C      1 
ATOM   15046 O  O      . GLY   F 4  67  ? 12.416  -64.403  -85.556  1.00 55.53  ? 67  GLY   F O      1 
ATOM   15047 N  N      . ALA   F 4  68  ? 11.131  -63.341  -84.030  1.00 54.29  ? 68  ALA   F N      1 
ATOM   15048 C  CA     . ALA   F 4  68  ? 10.302  -62.693  -85.045  1.00 56.37  ? 68  ALA   F CA     1 
ATOM   15049 C  C      . ALA   F 4  68  ? 11.117  -61.881  -86.043  1.00 61.88  ? 68  ALA   F C      1 
ATOM   15050 O  O      . ALA   F 4  68  ? 10.665  -61.660  -87.172  1.00 57.11  ? 68  ALA   F O      1 
ATOM   15051 C  CB     . ALA   F 4  68  ? 9.276   -61.787  -84.374  1.00 58.75  ? 68  ALA   F CB     1 
ATOM   15052 N  N      . ASP   F 4  69  ? 12.312  -61.443  -85.652  1.00 63.84  ? 69  ASP   F N      1 
ATOM   15053 C  CA     . ASP   F 4  69  ? 13.149  -60.629  -86.523  1.00 66.24  ? 69  ASP   F CA     1 
ATOM   15054 C  C      . ASP   F 4  69  ? 13.367  -61.282  -87.877  1.00 64.43  ? 69  ASP   F C      1 
ATOM   15055 O  O      . ASP   F 4  69  ? 13.583  -60.582  -88.874  1.00 63.08  ? 69  ASP   F O      1 
ATOM   15056 C  CB     . ASP   F 4  69  ? 14.483  -60.402  -85.833  1.00 64.45  ? 69  ASP   F CB     1 
ATOM   15057 C  CG     . ASP   F 4  69  ? 14.906  -61.615  -85.041  1.00 63.33  ? 69  ASP   F CG     1 
ATOM   15058 O  OD1    . ASP   F 4  69  ? 14.332  -61.819  -83.945  1.00 63.13  ? 69  ASP   F OD1    1 
ATOM   15059 O  OD2    . ASP   F 4  69  ? 15.787  -62.366  -85.513  1.00 63.34  ? 69  ASP   F OD2    1 
ATOM   15060 N  N      . LYS   F 4  70  ? 13.335  -62.620  -87.929  1.00 66.86  ? 70  LYS   F N      1 
ATOM   15061 C  CA     . LYS   F 4  70  ? 13.598  -63.329  -89.179  1.00 67.34  ? 70  LYS   F CA     1 
ATOM   15062 C  C      . LYS   F 4  70  ? 12.613  -62.924  -90.270  1.00 71.08  ? 70  LYS   F C      1 
ATOM   15063 O  O      . LYS   F 4  70  ? 12.939  -63.003  -91.461  1.00 72.13  ? 70  LYS   F O      1 
ATOM   15064 C  CB     . LYS   F 4  70  ? 13.561  -64.841  -88.931  1.00 64.65  ? 70  LYS   F CB     1 
ATOM   15065 C  CG     . LYS   F 4  70  ? 14.946  -65.502  -88.817  1.00 69.20  ? 70  LYS   F CG     1 
ATOM   15066 C  CD     . LYS   F 4  70  ? 14.825  -66.988  -88.450  1.00 75.62  ? 70  LYS   F CD     1 
ATOM   15067 C  CE     . LYS   F 4  70  ? 16.087  -67.516  -87.761  1.00 77.28  ? 70  LYS   F CE     1 
ATOM   15068 N  NZ     . LYS   F 4  70  ? 16.949  -68.343  -88.669  1.00 80.54  ? 70  LYS   F NZ     1 
ATOM   15069 N  N      . LEU   F 4  71  ? 11.429  -62.453  -89.884  1.00 67.73  ? 71  LEU   F N      1 
ATOM   15070 C  CA     . LEU   F 4  71  ? 10.422  -61.994  -90.823  1.00 62.30  ? 71  LEU   F CA     1 
ATOM   15071 C  C      . LEU   F 4  71  ? 10.455  -60.491  -91.051  1.00 66.59  ? 71  LEU   F C      1 
ATOM   15072 O  O      . LEU   F 4  71  ? 9.838   -60.018  -92.009  1.00 70.88  ? 71  LEU   F O      1 
ATOM   15073 C  CB     . LEU   F 4  71  ? 9.029   -62.392  -90.317  1.00 60.16  ? 71  LEU   F CB     1 
ATOM   15074 C  CG     . LEU   F 4  71  ? 7.870   -62.584  -91.287  1.00 55.54  ? 71  LEU   F CG     1 
ATOM   15075 C  CD1    . LEU   F 4  71  ? 7.877   -63.980  -91.831  1.00 53.19  ? 71  LEU   F CD1    1 
ATOM   15076 C  CD2    . LEU   F 4  71  ? 6.576   -62.299  -90.576  1.00 54.55  ? 71  LEU   F CD2    1 
ATOM   15077 N  N      . CYS   F 4  72  ? 11.158  -59.729  -90.204  1.00 70.48  ? 72  CYS   F N      1 
ATOM   15078 C  CA     . CYS   F 4  72  ? 11.083  -58.272  -90.203  1.00 69.13  ? 72  CYS   F CA     1 
ATOM   15079 C  C      . CYS   F 4  72  ? 12.401  -57.598  -90.576  1.00 71.77  ? 72  CYS   F C      1 
ATOM   15080 O  O      . CYS   F 4  72  ? 12.595  -56.420  -90.263  1.00 74.97  ? 72  CYS   F O      1 
ATOM   15081 C  CB     . CYS   F 4  72  ? 10.619  -57.767  -88.840  1.00 65.83  ? 72  CYS   F CB     1 
ATOM   15082 S  SG     . CYS   F 4  72  ? 9.141   -58.578  -88.205  1.00 63.20  ? 72  CYS   F SG     1 
ATOM   15083 N  N      . ARG   F 4  73  ? 13.310  -58.313  -91.230  1.00 68.77  ? 73  ARG   F N      1 
ATOM   15084 C  CA     . ARG   F 4  73  ? 14.575  -57.754  -91.688  1.00 67.25  ? 73  ARG   F CA     1 
ATOM   15085 C  C      . ARG   F 4  73  ? 14.740  -58.114  -93.155  1.00 71.55  ? 73  ARG   F C      1 
ATOM   15086 O  O      . ARG   F 4  73  ? 14.737  -59.298  -93.507  1.00 73.59  ? 73  ARG   F O      1 
ATOM   15087 C  CB     . ARG   F 4  73  ? 15.750  -58.279  -90.856  1.00 68.13  ? 73  ARG   F CB     1 
ATOM   15088 C  CG     . ARG   F 4  73  ? 16.192  -57.342  -89.723  1.00 76.22  ? 73  ARG   F CG     1 
ATOM   15089 C  CD     . ARG   F 4  73  ? 15.086  -57.202  -88.678  1.00 80.08  ? 73  ARG   F CD     1 
ATOM   15090 N  NE     . ARG   F 4  73  ? 15.481  -56.473  -87.476  1.00 79.55  ? 73  ARG   F NE     1 
ATOM   15091 C  CZ     . ARG   F 4  73  ? 14.672  -56.250  -86.447  1.00 81.49  ? 73  ARG   F CZ     1 
ATOM   15092 N  NH1    . ARG   F 4  73  ? 13.418  -56.681  -86.447  1.00 75.25  ? 73  ARG   F NH1    1 
ATOM   15093 N  NH2    . ARG   F 4  73  ? 15.129  -55.574  -85.395  1.00 88.42  ? 73  ARG   F NH2    1 
ATOM   15094 N  N      . LYS   F 4  74  ? 14.875  -57.095  -94.006  1.00 72.82  ? 74  LYS   F N      1 
ATOM   15095 C  CA     . LYS   F 4  74  ? 14.901  -57.316  -95.447  1.00 71.78  ? 74  LYS   F CA     1 
ATOM   15096 C  C      . LYS   F 4  74  ? 15.687  -58.576  -95.827  1.00 74.74  ? 74  LYS   F C      1 
ATOM   15097 O  O      . LYS   F 4  74  ? 15.165  -59.461  -96.511  1.00 74.49  ? 74  LYS   F O      1 
ATOM   15098 C  CB     . LYS   F 4  74  ? 15.468  -56.072  -96.145  1.00 79.59  ? 74  LYS   F CB     1 
ATOM   15099 C  CG     . LYS   F 4  74  ? 15.034  -54.727  -95.534  1.00 78.06  ? 74  LYS   F CG     1 
ATOM   15100 C  CD     . LYS   F 4  74  ? 15.552  -53.538  -96.364  1.00 79.90  ? 74  LYS   F CD     1 
ATOM   15101 C  CE     . LYS   F 4  74  ? 16.780  -52.860  -95.728  1.00 83.16  ? 74  LYS   F CE     1 
ATOM   15102 N  NZ     . LYS   F 4  74  ? 17.562  -52.024  -96.696  1.00 82.59  ? 74  LYS   F NZ     1 
ATOM   15103 N  N      . ALA   F 4  75  ? 16.929  -58.700  -95.350  1.00 76.15  ? 75  ALA   F N      1 
ATOM   15104 C  CA     . ALA   F 4  75  ? 17.785  -59.799  -95.794  1.00 73.70  ? 75  ALA   F CA     1 
ATOM   15105 C  C      . ALA   F 4  75  ? 17.311  -61.155  -95.263  1.00 74.32  ? 75  ALA   F C      1 
ATOM   15106 O  O      . ALA   F 4  75  ? 17.405  -62.171  -95.965  1.00 77.01  ? 75  ALA   F O      1 
ATOM   15107 C  CB     . ALA   F 4  75  ? 19.229  -59.528  -95.379  1.00 70.03  ? 75  ALA   F CB     1 
ATOM   15108 N  N      . SER   F 4  76  ? 16.818  -61.205  -94.023  1.00 74.41  ? 76  SER   F N      1 
ATOM   15109 C  CA     . SER   F 4  76  ? 16.369  -62.472  -93.445  1.00 73.75  ? 76  SER   F CA     1 
ATOM   15110 C  C      . SER   F 4  76  ? 15.004  -62.904  -93.974  1.00 75.50  ? 76  SER   F C      1 
ATOM   15111 O  O      . SER   F 4  76  ? 14.745  -64.109  -94.099  1.00 71.16  ? 76  SER   F O      1 
ATOM   15112 C  CB     . SER   F 4  76  ? 16.304  -62.355  -91.928  1.00 71.88  ? 76  SER   F CB     1 
ATOM   15113 O  OG     . SER   F 4  76  ? 15.814  -61.073  -91.568  1.00 70.20  ? 76  SER   F OG     1 
ATOM   15114 N  N      . LEU   F 4  77  ? 14.119  -61.940  -94.262  1.00 69.61  ? 77  LEU   F N      1 
ATOM   15115 C  CA     . LEU   F 4  77  ? 12.844  -62.255  -94.899  1.00 69.78  ? 77  LEU   F CA     1 
ATOM   15116 C  C      . LEU   F 4  77  ? 13.045  -62.952  -96.244  1.00 74.14  ? 77  LEU   F C      1 
ATOM   15117 O  O      . LEU   F 4  77  ? 12.275  -63.851  -96.608  1.00 70.97  ? 77  LEU   F O      1 
ATOM   15118 C  CB     . LEU   F 4  77  ? 12.026  -60.980  -95.079  1.00 67.71  ? 77  LEU   F CB     1 
ATOM   15119 C  CG     . LEU   F 4  77  ? 10.766  -61.244  -95.889  1.00 69.42  ? 77  LEU   F CG     1 
ATOM   15120 C  CD1    . LEU   F 4  77  ? 9.802   -62.038  -95.037  1.00 60.79  ? 77  LEU   F CD1    1 
ATOM   15121 C  CD2    . LEU   F 4  77  ? 10.141  -59.945  -96.364  1.00 72.90  ? 77  LEU   F CD2    1 
ATOM   15122 N  N      . VAL   F 4  78  ? 14.068  -62.538  -97.003  1.00 73.78  ? 78  VAL   F N      1 
ATOM   15123 C  CA     . VAL   F 4  78  ? 14.404  -63.216  -98.253  1.00 69.13  ? 78  VAL   F CA     1 
ATOM   15124 C  C      . VAL   F 4  78  ? 14.902  -64.628  -97.977  1.00 70.44  ? 78  VAL   F C      1 
ATOM   15125 O  O      . VAL   F 4  78  ? 14.437  -65.596  -98.591  1.00 70.03  ? 78  VAL   F O      1 
ATOM   15126 C  CB     . VAL   F 4  78  ? 15.436  -62.397  -99.048  1.00 77.07  ? 78  VAL   F CB     1 
ATOM   15127 C  CG1    . VAL   F 4  78  ? 16.213  -63.288  -100.015 1.00 74.59  ? 78  VAL   F CG1    1 
ATOM   15128 C  CG2    . VAL   F 4  78  ? 14.744  -61.258  -99.792  1.00 79.94  ? 78  VAL   F CG2    1 
ATOM   15129 N  N      . LYS   F 4  79  ? 15.850  -64.773  -97.047  1.00 67.36  ? 79  LYS   F N      1 
ATOM   15130 C  CA     . LYS   F 4  79  ? 16.331  -66.111  -96.720  1.00 71.27  ? 79  LYS   F CA     1 
ATOM   15131 C  C      . LYS   F 4  79  ? 15.190  -67.016  -96.268  1.00 75.51  ? 79  LYS   F C      1 
ATOM   15132 O  O      . LYS   F 4  79  ? 15.197  -68.221  -96.550  1.00 76.43  ? 79  LYS   F O      1 
ATOM   15133 C  CB     . LYS   F 4  79  ? 17.412  -66.056  -95.642  1.00 75.67  ? 79  LYS   F CB     1 
ATOM   15134 C  CG     . LYS   F 4  79  ? 17.986  -67.443  -95.323  1.00 80.52  ? 79  LYS   F CG     1 
ATOM   15135 C  CD     . LYS   F 4  79  ? 19.263  -67.392  -94.487  1.00 78.36  ? 79  LYS   F CD     1 
ATOM   15136 C  CE     . LYS   F 4  79  ? 19.567  -68.767  -93.858  1.00 78.27  ? 79  LYS   F CE     1 
ATOM   15137 N  NZ     . LYS   F 4  79  ? 19.775  -68.740  -92.367  1.00 75.33  ? 79  LYS   F NZ     1 
ATOM   15138 N  N      . LEU   F 4  80  ? 14.203  -66.457  -95.557  1.00 73.12  ? 80  LEU   F N      1 
ATOM   15139 C  CA     . LEU   F 4  80  ? 13.091  -67.273  -95.077  1.00 70.89  ? 80  LEU   F CA     1 
ATOM   15140 C  C      . LEU   F 4  80  ? 12.242  -67.779  -96.236  1.00 73.83  ? 80  LEU   F C      1 
ATOM   15141 O  O      . LEU   F 4  80  ? 11.822  -68.942  -96.244  1.00 72.05  ? 80  LEU   F O      1 
ATOM   15142 C  CB     . LEU   F 4  80  ? 12.242  -66.474  -94.087  1.00 66.45  ? 80  LEU   F CB     1 
ATOM   15143 C  CG     . LEU   F 4  80  ? 11.048  -67.251  -93.541  1.00 68.05  ? 80  LEU   F CG     1 
ATOM   15144 C  CD1    . LEU   F 4  80  ? 11.467  -68.146  -92.392  1.00 67.63  ? 80  LEU   F CD1    1 
ATOM   15145 C  CD2    . LEU   F 4  80  ? 9.921   -66.326  -93.128  1.00 61.19  ? 80  LEU   F CD2    1 
ATOM   15146 N  N      . ILE   F 4  81  ? 12.003  -66.921  -97.236  1.00 76.30  ? 81  ILE   F N      1 
ATOM   15147 C  CA     . ILE   F 4  81  ? 11.164  -67.286  -98.376  1.00 73.67  ? 81  ILE   F CA     1 
ATOM   15148 C  C      . ILE   F 4  81  ? 11.808  -68.398  -99.202  1.00 73.83  ? 81  ILE   F C      1 
ATOM   15149 O  O      . ILE   F 4  81  ? 11.131  -69.337  -99.631  1.00 77.67  ? 81  ILE   F O      1 
ATOM   15150 C  CB     . ILE   F 4  81  ? 10.873  -66.044  -99.235  1.00 72.46  ? 81  ILE   F CB     1 
ATOM   15151 C  CG1    . ILE   F 4  81  ? 10.139  -64.978  -98.422  1.00 70.55  ? 81  ILE   F CG1    1 
ATOM   15152 C  CG2    . ILE   F 4  81  ? 10.032  -66.416  -100.428 1.00 68.56  ? 81  ILE   F CG2    1 
ATOM   15153 C  CD1    . ILE   F 4  81  ? 8.815   -65.427  -97.914  1.00 69.53  ? 81  ILE   F CD1    1 
ATOM   15154 N  N      . LYS   F 4  82  ? 13.122  -68.320  -99.436  1.00 73.66  ? 82  LYS   F N      1 
ATOM   15155 C  CA     . LYS   F 4  82  ? 13.764  -69.324  -100.288 1.00 77.45  ? 82  LYS   F CA     1 
ATOM   15156 C  C      . LYS   F 4  82  ? 13.959  -70.659  -99.573  1.00 79.45  ? 82  LYS   F C      1 
ATOM   15157 O  O      . LYS   F 4  82  ? 13.772  -71.716  -100.183 1.00 80.84  ? 82  LYS   F O      1 
ATOM   15158 C  CB     . LYS   F 4  82  ? 15.114  -68.820  -100.809 1.00 68.74  ? 82  LYS   F CB     1 
ATOM   15159 C  CG     . LYS   F 4  82  ? 15.153  -67.339  -101.108 1.00 74.72  ? 82  LYS   F CG     1 
ATOM   15160 C  CD     . LYS   F 4  82  ? 16.393  -66.947  -101.891 1.00 72.98  ? 82  LYS   F CD     1 
ATOM   15161 C  CE     . LYS   F 4  82  ? 16.039  -66.037  -103.072 1.00 74.32  ? 82  LYS   F CE     1 
ATOM   15162 N  NZ     . LYS   F 4  82  ? 15.675  -64.646  -102.682 1.00 74.78  ? 82  LYS   F NZ     1 
ATOM   15163 N  N      . THR   F 4  83  ? 14.340  -70.643  -98.292  1.00 78.42  ? 83  THR   F N      1 
ATOM   15164 C  CA     . THR   F 4  83  ? 14.732  -71.887  -97.630  1.00 78.32  ? 83  THR   F CA     1 
ATOM   15165 C  C      . THR   F 4  83  ? 13.546  -72.650  -97.051  1.00 78.89  ? 83  THR   F C      1 
ATOM   15166 O  O      . THR   F 4  83  ? 13.496  -73.882  -97.155  1.00 80.21  ? 83  THR   F O      1 
ATOM   15167 C  CB     . THR   F 4  83  ? 15.754  -71.617  -96.519  1.00 79.68  ? 83  THR   F CB     1 
ATOM   15168 O  OG1    . THR   F 4  83  ? 15.440  -70.380  -95.866  1.00 85.57  ? 83  THR   F OG1    1 
ATOM   15169 C  CG2    . THR   F 4  83  ? 17.167  -71.549  -97.088  1.00 69.31  ? 83  THR   F CG2    1 
ATOM   15170 N  N      . SER   F 4  84  ? 12.595  -71.960  -96.436  1.00 78.57  ? 84  SER   F N      1 
ATOM   15171 C  CA     . SER   F 4  84  ? 11.414  -72.643  -95.910  1.00 75.67  ? 84  SER   F CA     1 
ATOM   15172 C  C      . SER   F 4  84  ? 10.614  -73.260  -97.050  1.00 76.59  ? 84  SER   F C      1 
ATOM   15173 O  O      . SER   F 4  84  ? 10.127  -72.524  -97.918  1.00 81.29  ? 84  SER   F O      1 
ATOM   15174 C  CB     . SER   F 4  84  ? 10.535  -71.677  -95.127  1.00 69.29  ? 84  SER   F CB     1 
ATOM   15175 O  OG     . SER   F 4  84  ? 11.285  -70.931  -94.189  1.00 73.59  ? 84  SER   F OG     1 
ATOM   15176 N  N      . PRO   F 4  85  ? 10.447  -74.584  -97.095  1.00 77.22  ? 85  PRO   F N      1 
ATOM   15177 C  CA     . PRO   F 4  85  ? 9.586   -75.169  -98.139  1.00 80.57  ? 85  PRO   F CA     1 
ATOM   15178 C  C      . PRO   F 4  85  ? 8.146   -74.686  -98.076  1.00 75.66  ? 85  PRO   F C      1 
ATOM   15179 O  O      . PRO   F 4  85  ? 7.499   -74.576  -99.122  1.00 78.46  ? 85  PRO   F O      1 
ATOM   15180 C  CB     . PRO   F 4  85  ? 9.688   -76.681  -97.874  1.00 82.97  ? 85  PRO   F CB     1 
ATOM   15181 C  CG     . PRO   F 4  85  ? 10.968  -76.848  -97.093  1.00 84.20  ? 85  PRO   F CG     1 
ATOM   15182 C  CD     . PRO   F 4  85  ? 11.051  -75.617  -96.236  1.00 80.07  ? 85  PRO   F CD     1 
ATOM   15183 N  N      . GLU   F 4  86  ? 7.625   -74.400  -96.878  1.00 80.15  ? 86  GLU   F N      1 
ATOM   15184 C  CA     . GLU   F 4  86  ? 6.256   -73.900  -96.749  1.00 79.93  ? 86  GLU   F CA     1 
ATOM   15185 C  C      . GLU   F 4  86  ? 6.014   -72.692  -97.641  1.00 78.73  ? 86  GLU   F C      1 
ATOM   15186 O  O      . GLU   F 4  86  ? 4.937   -72.550  -98.231  1.00 76.07  ? 86  GLU   F O      1 
ATOM   15187 C  CB     . GLU   F 4  86  ? 5.949   -73.542  -95.293  1.00 75.26  ? 86  GLU   F CB     1 
ATOM   15188 C  CG     . GLU   F 4  86  ? 4.909   -72.432  -95.191  1.00 79.34  ? 86  GLU   F CG     1 
ATOM   15189 C  CD     . GLU   F 4  86  ? 3.920   -72.598  -94.025  1.00 80.26  ? 86  GLU   F CD     1 
ATOM   15190 O  OE1    . GLU   F 4  86  ? 2.915   -71.833  -94.008  1.00 73.61  ? 86  GLU   F OE1    1 
ATOM   15191 O  OE2    . GLU   F 4  86  ? 4.142   -73.479  -93.146  1.00 73.08  ? 86  GLU   F OE2    1 
ATOM   15192 N  N      . LEU   F 4  87  ? 7.005   -71.805  -97.737  1.00 81.38  ? 87  LEU   F N      1 
ATOM   15193 C  CA     . LEU   F 4  87  ? 6.946   -70.658  -98.635  1.00 81.83  ? 87  LEU   F CA     1 
ATOM   15194 C  C      . LEU   F 4  87  ? 7.403   -71.035  -100.041 1.00 83.67  ? 87  LEU   F C      1 
ATOM   15195 O  O      . LEU   F 4  87  ? 6.759   -70.673  -101.036 1.00 84.25  ? 87  LEU   F O      1 
ATOM   15196 C  CB     . LEU   F 4  87  ? 7.807   -69.529  -98.066  1.00 76.92  ? 87  LEU   F CB     1 
ATOM   15197 C  CG     . LEU   F 4  87  ? 7.387   -69.188  -96.637  1.00 78.59  ? 87  LEU   F CG     1 
ATOM   15198 C  CD1    . LEU   F 4  87  ? 7.837   -67.796  -96.217  1.00 73.70  ? 87  LEU   F CD1    1 
ATOM   15199 C  CD2    . LEU   F 4  87  ? 5.870   -69.351  -96.502  1.00 65.94  ? 87  LEU   F CD2    1 
ATOM   15200 N  N      . SER   F 4  88  ? 8.502   -71.777  -100.138 1.00 81.83  ? 88  SER   F N      1 
ATOM   15201 C  CA     . SER   F 4  88  ? 9.008   -72.216  -101.431 1.00 87.26  ? 88  SER   F CA     1 
ATOM   15202 C  C      . SER   F 4  88  ? 9.674   -71.088  -102.201 1.00 93.13  ? 88  SER   F C      1 
ATOM   15203 O  O      . SER   F 4  88  ? 9.165   -69.960  -102.251 1.00 92.66  ? 88  SER   F O      1 
ATOM   15204 C  CB     . SER   F 4  88  ? 7.887   -72.807  -102.281 1.00 88.41  ? 88  SER   F CB     1 
ATOM   15205 O  OG     . SER   F 4  88  ? 8.336   -73.065  -103.595 1.00 91.53  ? 88  SER   F OG     1 
ATOM   15206 N  N      . GLU   F 4  89  ? 10.795  -71.410  -102.841 1.00 93.79  ? 89  GLU   F N      1 
ATOM   15207 C  CA     . GLU   F 4  89  ? 11.461  -70.485  -103.746 1.00 100.01 ? 89  GLU   F CA     1 
ATOM   15208 C  C      . GLU   F 4  89  ? 10.528  -70.005  -104.858 1.00 104.52 ? 89  GLU   F C      1 
ATOM   15209 O  O      . GLU   F 4  89  ? 10.891  -69.119  -105.642 1.00 106.27 ? 89  GLU   F O      1 
ATOM   15210 C  CB     . GLU   F 4  89  ? 12.711  -71.154  -104.330 1.00 100.33 ? 89  GLU   F CB     1 
ATOM   15211 C  CG     . GLU   F 4  89  ? 12.438  -72.396  -105.160 1.00 104.80 ? 89  GLU   F CG     1 
ATOM   15212 C  CD     . GLU   F 4  89  ? 12.793  -72.224  -106.630 1.00 114.63 ? 89  GLU   F CD     1 
ATOM   15213 O  OE1    . GLU   F 4  89  ? 13.062  -71.077  -107.055 1.00 114.14 ? 89  GLU   F OE1    1 
ATOM   15214 O  OE2    . GLU   F 4  89  ? 12.811  -73.240  -107.360 1.00 114.62 ? 89  GLU   F OE2    1 
ATOM   15215 N  N      . SER   F 4  90  ? 9.324   -70.576  -104.930 1.00 103.87 ? 90  SER   F N      1 
ATOM   15216 C  CA     . SER   F 4  90  ? 8.394   -70.291  -106.013 1.00 100.47 ? 90  SER   F CA     1 
ATOM   15217 C  C      . SER   F 4  90  ? 7.182   -69.457  -105.607 1.00 99.38  ? 90  SER   F C      1 
ATOM   15218 O  O      . SER   F 4  90  ? 6.346   -69.179  -106.475 1.00 101.76 ? 90  SER   F O      1 
ATOM   15219 C  CB     . SER   F 4  90  ? 7.900   -71.601  -106.648 1.00 97.92  ? 90  SER   F CB     1 
ATOM   15220 O  OG     . SER   F 4  90  ? 7.758   -72.643  -105.695 1.00 100.94 ? 90  SER   F OG     1 
ATOM   15221 N  N      . CYS   F 4  91  ? 7.036   -69.065  -104.333 1.00 97.93  ? 91  CYS   F N      1 
ATOM   15222 C  CA     . CYS   F 4  91  ? 5.793   -68.414  -103.919 1.00 87.62  ? 91  CYS   F CA     1 
ATOM   15223 C  C      . CYS   F 4  91  ? 5.480   -67.273  -104.871 1.00 87.14  ? 91  CYS   F C      1 
ATOM   15224 O  O      . CYS   F 4  91  ? 6.372   -66.528  -105.289 1.00 85.75  ? 91  CYS   F O      1 
ATOM   15225 C  CB     . CYS   F 4  91  ? 5.862   -67.885  -102.485 1.00 80.55  ? 91  CYS   F CB     1 
ATOM   15226 S  SG     . CYS   F 4  91  ? 7.210   -66.798  -102.181 1.00 85.77  ? 91  CYS   F SG     1 
ATOM   15227 N  N      . THR   F 4  92  ? 4.212   -67.158  -105.227 1.00 81.44  ? 92  THR   F N      1 
ATOM   15228 C  CA     . THR   F 4  92  ? 3.784   -66.252  -106.273 1.00 73.40  ? 92  THR   F CA     1 
ATOM   15229 C  C      . THR   F 4  92  ? 3.499   -64.851  -105.769 1.00 77.20  ? 92  THR   F C      1 
ATOM   15230 O  O      . THR   F 4  92  ? 3.075   -64.008  -106.565 1.00 77.11  ? 92  THR   F O      1 
ATOM   15231 C  CB     . THR   F 4  92  ? 2.537   -66.812  -106.931 1.00 78.15  ? 92  THR   F CB     1 
ATOM   15232 O  OG1    . THR   F 4  92  ? 1.383   -66.340  -106.223 1.00 81.73  ? 92  THR   F OG1    1 
ATOM   15233 C  CG2    . THR   F 4  92  ? 2.566   -68.320  -106.862 1.00 73.54  ? 92  THR   F CG2    1 
ATOM   15234 N  N      . TRP   F 4  93  ? 3.701   -64.588  -104.475 1.00 77.81  ? 93  TRP   F N      1 
ATOM   15235 C  CA     . TRP   F 4  93  ? 3.380   -63.303  -103.868 1.00 71.40  ? 93  TRP   F CA     1 
ATOM   15236 C  C      . TRP   F 4  93  ? 4.614   -62.536  -103.418 1.00 73.54  ? 93  TRP   F C      1 
ATOM   15237 O  O      . TRP   F 4  93  ? 4.474   -61.458  -102.822 1.00 71.61  ? 93  TRP   F O      1 
ATOM   15238 C  CB     . TRP   F 4  93  ? 2.439   -63.501  -102.673 1.00 70.76  ? 93  TRP   F CB     1 
ATOM   15239 C  CG     . TRP   F 4  93  ? 2.834   -64.655  -101.813 1.00 73.72  ? 93  TRP   F CG     1 
ATOM   15240 C  CD1    . TRP   F 4  93  ? 2.464   -65.952  -101.971 1.00 69.78  ? 93  TRP   F CD1    1 
ATOM   15241 C  CD2    . TRP   F 4  93  ? 3.700   -64.617  -100.672 1.00 75.44  ? 93  TRP   F CD2    1 
ATOM   15242 N  NE1    . TRP   F 4  93  ? 3.040   -66.727  -101.001 1.00 74.62  ? 93  TRP   F NE1    1 
ATOM   15243 C  CE2    . TRP   F 4  93  ? 3.808   -65.933  -100.191 1.00 77.73  ? 93  TRP   F CE2    1 
ATOM   15244 C  CE3    . TRP   F 4  93  ? 4.391   -63.595  -100.010 1.00 73.46  ? 93  TRP   F CE3    1 
ATOM   15245 C  CZ2    . TRP   F 4  93  ? 4.574   -66.261  -99.075  1.00 78.39  ? 93  TRP   F CZ2    1 
ATOM   15246 C  CZ3    . TRP   F 4  93  ? 5.155   -63.919  -98.907  1.00 74.22  ? 93  TRP   F CZ3    1 
ATOM   15247 C  CH2    . TRP   F 4  93  ? 5.238   -65.243  -98.448  1.00 79.30  ? 93  TRP   F CH2    1 
ATOM   15248 N  N      . PHE   F 4  94  ? 5.814   -63.053  -103.668 1.00 69.99  ? 94  PHE   F N      1 
ATOM   15249 C  CA     . PHE   F 4  94  ? 7.002   -62.309  -103.298 1.00 75.71  ? 94  PHE   F CA     1 
ATOM   15250 C  C      . PHE   F 4  94  ? 7.781   -61.926  -104.549 1.00 74.79  ? 94  PHE   F C      1 
ATOM   15251 O  O      . PHE   F 4  94  ? 7.963   -62.764  -105.444 1.00 69.85  ? 94  PHE   F O      1 
ATOM   15252 C  CB     . PHE   F 4  94  ? 7.900   -63.112  -102.333 1.00 72.96  ? 94  PHE   F CB     1 
ATOM   15253 C  CG     . PHE   F 4  94  ? 8.882   -62.260  -101.562 1.00 70.74  ? 94  PHE   F CG     1 
ATOM   15254 C  CD1    . PHE   F 4  94  ? 8.468   -61.088  -100.937 1.00 71.16  ? 94  PHE   F CD1    1 
ATOM   15255 C  CD2    . PHE   F 4  94  ? 10.215  -62.642  -101.446 1.00 64.79  ? 94  PHE   F CD2    1 
ATOM   15256 C  CE1    . PHE   F 4  94  ? 9.369   -60.303  -100.226 1.00 68.10  ? 94  PHE   F CE1    1 
ATOM   15257 C  CE2    . PHE   F 4  94  ? 11.116  -61.863  -100.743 1.00 65.23  ? 94  PHE   F CE2    1 
ATOM   15258 C  CZ     . PHE   F 4  94  ? 10.692  -60.695  -100.132 1.00 67.31  ? 94  PHE   F CZ     1 
ATOM   15259 N  N      . PRO   F 4  95  ? 8.213   -60.674  -104.669 1.00 77.23  ? 95  PRO   F N      1 
ATOM   15260 C  CA     . PRO   F 4  95  ? 9.074   -60.291  -105.791 1.00 81.92  ? 95  PRO   F CA     1 
ATOM   15261 C  C      . PRO   F 4  95  ? 10.427  -60.983  -105.724 1.00 86.67  ? 95  PRO   F C      1 
ATOM   15262 O  O      . PRO   F 4  95  ? 10.921  -61.331  -104.650 1.00 83.36  ? 95  PRO   F O      1 
ATOM   15263 C  CB     . PRO   F 4  95  ? 9.217   -58.774  -105.618 1.00 83.27  ? 95  PRO   F CB     1 
ATOM   15264 C  CG     . PRO   F 4  95  ? 7.990   -58.368  -104.849 1.00 77.63  ? 95  PRO   F CG     1 
ATOM   15265 C  CD     . PRO   F 4  95  ? 7.750   -59.504  -103.902 1.00 76.29  ? 95  PRO   F CD     1 
ATOM   15266 N  N      . GLU   F 4  96  ? 11.024  -61.190  -106.900 1.00 93.79  ? 96  GLU   F N      1 
ATOM   15267 C  CA     . GLU   F 4  96  ? 12.375  -61.740  -106.985 1.00 90.55  ? 96  GLU   F CA     1 
ATOM   15268 C  C      . GLU   F 4  96  ? 13.336  -60.932  -106.129 1.00 91.64  ? 96  GLU   F C      1 
ATOM   15269 O  O      . GLU   F 4  96  ? 13.378  -59.704  -106.223 1.00 94.98  ? 96  GLU   F O      1 
ATOM   15270 C  CB     . GLU   F 4  96  ? 12.853  -61.726  -108.432 1.00 97.09  ? 96  GLU   F CB     1 
ATOM   15271 C  CG     . GLU   F 4  96  ? 13.915  -62.748  -108.733 1.00 97.83  ? 96  GLU   F CG     1 
ATOM   15272 C  CD     . GLU   F 4  96  ? 13.703  -63.417  -110.072 1.00 95.62  ? 96  GLU   F CD     1 
ATOM   15273 O  OE1    . GLU   F 4  96  ? 12.553  -63.427  -110.566 1.00 95.36  ? 96  GLU   F OE1    1 
ATOM   15274 O  OE2    . GLU   F 4  96  ? 14.689  -63.936  -110.629 1.00 98.48  ? 96  GLU   F OE2    1 
ATOM   15275 N  N      . SER   F 4  97  ? 14.119  -61.623  -105.304 1.00 92.54  ? 97  SER   F N      1 
ATOM   15276 C  CA     . SER   F 4  97  ? 15.008  -60.952  -104.365 1.00 95.19  ? 97  SER   F CA     1 
ATOM   15277 C  C      . SER   F 4  97  ? 16.311  -61.721  -104.213 1.00 97.58  ? 97  SER   F C      1 
ATOM   15278 O  O      . SER   F 4  97  ? 16.318  -62.955  -104.159 1.00 91.04  ? 97  SER   F O      1 
ATOM   15279 C  CB     . SER   F 4  97  ? 14.349  -60.790  -102.990 1.00 87.80  ? 97  SER   F CB     1 
ATOM   15280 O  OG     . SER   F 4  97  ? 13.051  -60.243  -103.111 1.00 85.33  ? 97  SER   F OG     1 
ATOM   15281 N  N      . TYR   F 4  98  ? 17.411  -60.975  -104.126 1.00 102.81 ? 98  TYR   F N      1 
ATOM   15282 C  CA     . TYR   F 4  98  ? 18.722  -61.538  -103.851 1.00 102.45 ? 98  TYR   F CA     1 
ATOM   15283 C  C      . TYR   F 4  98  ? 19.397  -60.724  -102.755 1.00 107.89 ? 98  TYR   F C      1 
ATOM   15284 O  O      . TYR   F 4  98  ? 19.166  -59.514  -102.624 1.00 103.32 ? 98  TYR   F O      1 
ATOM   15285 C  CB     . TYR   F 4  98  ? 19.584  -61.563  -105.114 1.00 107.05 ? 98  TYR   F CB     1 
ATOM   15286 C  CG     . TYR   F 4  98  ? 18.900  -62.257  -106.264 1.00 107.13 ? 98  TYR   F CG     1 
ATOM   15287 C  CD1    . TYR   F 4  98  ? 17.988  -61.581  -107.065 1.00 102.76 ? 98  TYR   F CD1    1 
ATOM   15288 C  CD2    . TYR   F 4  98  ? 19.157  -63.589  -106.546 1.00 108.70 ? 98  TYR   F CD2    1 
ATOM   15289 C  CE1    . TYR   F 4  98  ? 17.355  -62.213  -108.108 1.00 99.40  ? 98  TYR   F CE1    1 
ATOM   15290 C  CE2    . TYR   F 4  98  ? 18.531  -64.228  -107.592 1.00 108.23 ? 98  TYR   F CE2    1 
ATOM   15291 C  CZ     . TYR   F 4  98  ? 17.629  -63.536  -108.367 1.00 103.61 ? 98  TYR   F CZ     1 
ATOM   15292 O  OH     . TYR   F 4  98  ? 17.000  -64.175  -109.406 1.00 103.89 ? 98  TYR   F OH     1 
ATOM   15293 N  N      . VAL   F 4  99  ? 20.212  -61.408  -101.952 1.00 106.28 ? 99  VAL   F N      1 
ATOM   15294 C  CA     . VAL   F 4  99  ? 21.018  -60.772  -100.915 1.00 107.24 ? 99  VAL   F CA     1 
ATOM   15295 C  C      . VAL   F 4  99  ? 22.445  -60.661  -101.438 1.00 111.70 ? 99  VAL   F C      1 
ATOM   15296 O  O      . VAL   F 4  99  ? 23.104  -61.677  -101.699 1.00 111.32 ? 99  VAL   F O      1 
ATOM   15297 C  CB     . VAL   F 4  99  ? 20.970  -61.559  -99.597  1.00 105.46 ? 99  VAL   F CB     1 
ATOM   15298 C  CG1    . VAL   F 4  99  ? 21.335  -60.648  -98.431  1.00 102.80 ? 99  VAL   F CG1    1 
ATOM   15299 C  CG2    . VAL   F 4  99  ? 19.605  -62.190  -99.395  1.00 97.43  ? 99  VAL   F CG2    1 
ATOM   15300 N  N      . ILE   F 4  100 ? 22.913  -59.430  -101.618 1.00 113.11 ? 100 ILE   F N      1 
ATOM   15301 C  CA     . ILE   F 4  100 ? 24.262  -59.152  -102.093 1.00 119.60 ? 100 ILE   F CA     1 
ATOM   15302 C  C      . ILE   F 4  100 ? 24.972  -58.342  -101.016 1.00 120.77 ? 100 ILE   F C      1 
ATOM   15303 O  O      . ILE   F 4  100 ? 24.459  -57.308  -100.568 1.00 116.97 ? 100 ILE   F O      1 
ATOM   15304 C  CB     . ILE   F 4  100 ? 24.261  -58.401  -103.440 1.00 113.85 ? 100 ILE   F CB     1 
ATOM   15305 C  CG1    . ILE   F 4  100 ? 23.126  -58.880  -104.353 1.00 98.55  ? 100 ILE   F CG1    1 
ATOM   15306 C  CG2    . ILE   F 4  100 ? 25.598  -58.593  -104.156 1.00 115.40 ? 100 ILE   F CG2    1 
ATOM   15307 C  CD1    . ILE   F 4  100 ? 23.332  -60.263  -104.913 1.00 101.71 ? 100 ILE   F CD1    1 
ATOM   15308 N  N      . TYR   F 4  101 ? 26.137  -58.825  -100.590 1.00 120.59 ? 101 TYR   F N      1 
ATOM   15309 C  CA     . TYR   F 4  101 ? 26.933  -58.174  -99.564  1.00 121.80 ? 101 TYR   F CA     1 
ATOM   15310 C  C      . TYR   F 4  101 ? 27.919  -57.201  -100.196 1.00 122.82 ? 101 TYR   F C      1 
ATOM   15311 O  O      . TYR   F 4  101 ? 28.277  -57.343  -101.368 1.00 125.79 ? 101 TYR   F O      1 
ATOM   15312 C  CB     . TYR   F 4  101 ? 27.681  -59.223  -98.745  1.00 119.56 ? 101 TYR   F CB     1 
ATOM   15313 C  CG     . TYR   F 4  101 ? 26.808  -60.090  -97.860  1.00 115.30 ? 101 TYR   F CG     1 
ATOM   15314 C  CD1    . TYR   F 4  101 ? 25.729  -59.557  -97.170  1.00 117.41 ? 101 TYR   F CD1    1 
ATOM   15315 C  CD2    . TYR   F 4  101 ? 27.074  -61.444  -97.707  1.00 114.48 ? 101 TYR   F CD2    1 
ATOM   15316 C  CE1    . TYR   F 4  101 ? 24.939  -60.348  -96.356  1.00 112.19 ? 101 TYR   F CE1    1 
ATOM   15317 C  CE2    . TYR   F 4  101 ? 26.290  -62.239  -96.896  1.00 112.26 ? 101 TYR   F CE2    1 
ATOM   15318 C  CZ     . TYR   F 4  101 ? 25.228  -61.685  -96.224  1.00 107.91 ? 101 TYR   F CZ     1 
ATOM   15319 O  OH     . TYR   F 4  101 ? 24.450  -62.478  -95.421  1.00 106.15 ? 101 TYR   F OH     1 
ATOM   15320 N  N      . PRO   F 4  102 ? 28.370  -56.181  -99.449  1.00 123.45 ? 102 PRO   F N      1 
ATOM   15321 C  CA     . PRO   F 4  102 ? 29.359  -55.244  -100.004 1.00 131.46 ? 102 PRO   F CA     1 
ATOM   15322 C  C      . PRO   F 4  102 ? 30.801  -55.492  -99.563  1.00 129.93 ? 102 PRO   F C      1 
ATOM   15323 O  O      . PRO   F 4  102 ? 31.177  -55.146  -98.438  1.00 129.46 ? 102 PRO   F O      1 
ATOM   15324 C  CB     . PRO   F 4  102 ? 28.862  -53.891  -99.487  1.00 134.07 ? 102 PRO   F CB     1 
ATOM   15325 C  CG     . PRO   F 4  102 ? 28.291  -54.224  -98.145  1.00 130.01 ? 102 PRO   F CG     1 
ATOM   15326 C  CD     . PRO   F 4  102 ? 27.720  -55.631  -98.246  1.00 125.05 ? 102 PRO   F CD     1 
ATOM   15327 N  N      . THR   F 4  103 ? 31.612  -56.087  -100.436 1.00 128.75 ? 103 THR   F N      1 
ATOM   15328 C  CA     . THR   F 4  103 ? 33.069  -56.092  -100.282 1.00 123.30 ? 103 THR   F CA     1 
ATOM   15329 C  C      . THR   F 4  103 ? 33.673  -55.766  -101.639 1.00 117.59 ? 103 THR   F C      1 
ATOM   15330 O  O      . THR   F 4  103 ? 32.949  -55.616  -102.626 1.00 105.10 ? 103 THR   F O      1 
ATOM   15331 C  CB     . THR   F 4  103 ? 33.642  -57.449  -99.770  1.00 115.82 ? 103 THR   F CB     1 
ATOM   15332 O  OG1    . THR   F 4  103 ? 32.778  -58.017  -98.777  1.00 117.83 ? 103 THR   F OG1    1 
ATOM   15333 C  CG2    . THR   F 4  103 ? 35.022  -57.253  -99.168  1.00 109.60 ? 103 THR   F CG2    1 
ATOM   15334 N  N      . VAL   F 4  130 ? 23.093  -65.354  -108.007 1.00 128.74 ? 130 VAL   F N      1 
ATOM   15335 C  CA     . VAL   F 4  130 ? 22.339  -65.621  -109.225 1.00 125.14 ? 130 VAL   F CA     1 
ATOM   15336 C  C      . VAL   F 4  130 ? 21.601  -64.389  -109.699 1.00 125.81 ? 130 VAL   F C      1 
ATOM   15337 O  O      . VAL   F 4  130 ? 20.818  -64.477  -110.645 1.00 129.78 ? 130 VAL   F O      1 
ATOM   15338 C  CB     . VAL   F 4  130 ? 21.337  -66.771  -109.038 1.00 124.46 ? 130 VAL   F CB     1 
ATOM   15339 C  CG1    . VAL   F 4  130 ? 20.900  -67.319  -110.395 1.00 127.92 ? 130 VAL   F CG1    1 
ATOM   15340 C  CG2    . VAL   F 4  130 ? 21.941  -67.867  -108.185 1.00 124.20 ? 130 VAL   F CG2    1 
ATOM   15341 N  N      . PHE   F 4  131 ? 21.827  -63.248  -109.040 1.00 123.02 ? 131 PHE   F N      1 
ATOM   15342 C  CA     . PHE   F 4  131 ? 21.226  -62.002  -109.504 1.00 122.12 ? 131 PHE   F CA     1 
ATOM   15343 C  C      . PHE   F 4  131 ? 21.487  -61.815  -110.993 1.00 131.23 ? 131 PHE   F C      1 
ATOM   15344 O  O      . PHE   F 4  131 ? 20.561  -61.804  -111.812 1.00 132.11 ? 131 PHE   F O      1 
ATOM   15345 C  CB     . PHE   F 4  131 ? 21.789  -60.810  -108.731 1.00 116.73 ? 131 PHE   F CB     1 
ATOM   15346 C  CG     . PHE   F 4  131 ? 21.366  -59.471  -109.292 1.00 123.49 ? 131 PHE   F CG     1 
ATOM   15347 C  CD1    . PHE   F 4  131 ? 22.043  -58.321  -108.927 1.00 124.32 ? 131 PHE   F CD1    1 
ATOM   15348 C  CD2    . PHE   F 4  131 ? 20.272  -59.352  -110.140 1.00 123.57 ? 131 PHE   F CD2    1 
ATOM   15349 C  CE1    . PHE   F 4  131 ? 21.672  -57.086  -109.432 1.00 123.22 ? 131 PHE   F CE1    1 
ATOM   15350 C  CE2    . PHE   F 4  131 ? 19.894  -58.125  -110.642 1.00 125.40 ? 131 PHE   F CE2    1 
ATOM   15351 C  CZ     . PHE   F 4  131 ? 20.583  -56.986  -110.280 1.00 124.15 ? 131 PHE   F CZ     1 
ATOM   15352 N  N      . LEU   F 4  132 ? 22.760  -61.645  -111.352 1.00 136.87 ? 132 LEU   F N      1 
ATOM   15353 C  CA     . LEU   F 4  132 ? 23.119  -61.391  -112.742 1.00 135.78 ? 132 LEU   F CA     1 
ATOM   15354 C  C      . LEU   F 4  132 ? 22.488  -62.427  -113.667 1.00 137.07 ? 132 LEU   F C      1 
ATOM   15355 O  O      . LEU   F 4  132 ? 21.908  -62.081  -114.704 1.00 139.54 ? 132 LEU   F O      1 
ATOM   15356 C  CB     . LEU   F 4  132 ? 24.643  -61.380  -112.876 1.00 131.72 ? 132 LEU   F CB     1 
ATOM   15357 C  CG     . LEU   F 4  132 ? 25.340  -60.498  -111.832 1.00 129.12 ? 132 LEU   F CG     1 
ATOM   15358 C  CD1    . LEU   F 4  132 ? 26.846  -60.591  -111.972 1.00 125.23 ? 132 LEU   F CD1    1 
ATOM   15359 C  CD2    . LEU   F 4  132 ? 24.876  -59.047  -111.907 1.00 124.71 ? 132 LEU   F CD2    1 
ATOM   15360 N  N      . ALA   F 4  133 ? 22.559  -63.704  -113.279 1.00 134.04 ? 133 ALA   F N      1 
ATOM   15361 C  CA     . ALA   F 4  133 ? 22.038  -64.790  -114.107 1.00 137.57 ? 133 ALA   F CA     1 
ATOM   15362 C  C      . ALA   F 4  133 ? 20.604  -64.524  -114.560 1.00 141.35 ? 133 ALA   F C      1 
ATOM   15363 O  O      . ALA   F 4  133 ? 20.295  -64.583  -115.755 1.00 147.65 ? 133 ALA   F O      1 
ATOM   15364 C  CB     . ALA   F 4  133 ? 22.124  -66.117  -113.345 1.00 135.03 ? 133 ALA   F CB     1 
ATOM   15365 N  N      . ALA   F 4  134 ? 19.708  -64.236  -113.614 1.00 134.60 ? 134 ALA   F N      1 
ATOM   15366 C  CA     . ALA   F 4  134 ? 18.321  -63.981  -113.985 1.00 133.94 ? 134 ALA   F CA     1 
ATOM   15367 C  C      . ALA   F 4  134 ? 18.171  -62.622  -114.663 1.00 140.32 ? 134 ALA   F C      1 
ATOM   15368 O  O      . ALA   F 4  134 ? 17.390  -62.479  -115.611 1.00 144.08 ? 134 ALA   F O      1 
ATOM   15369 C  CB     . ALA   F 4  134 ? 17.422  -64.087  -112.757 1.00 128.20 ? 134 ALA   F CB     1 
ATOM   15370 N  N      . TYR   F 4  135 ? 18.914  -61.614  -114.196 1.00 139.36 ? 135 TYR   F N      1 
ATOM   15371 C  CA     . TYR   F 4  135 ? 18.944  -60.322  -114.878 1.00 139.88 ? 135 TYR   F CA     1 
ATOM   15372 C  C      . TYR   F 4  135 ? 19.328  -60.489  -116.350 1.00 143.29 ? 135 TYR   F C      1 
ATOM   15373 O  O      . TYR   F 4  135 ? 18.884  -59.712  -117.204 1.00 142.05 ? 135 TYR   F O      1 
ATOM   15374 C  CB     . TYR   F 4  135 ? 19.903  -59.390  -114.116 1.00 134.03 ? 135 TYR   F CB     1 
ATOM   15375 C  CG     . TYR   F 4  135 ? 20.114  -57.971  -114.631 1.00 133.96 ? 135 TYR   F CG     1 
ATOM   15376 C  CD1    . TYR   F 4  135 ? 19.622  -57.548  -115.857 1.00 134.61 ? 135 TYR   F CD1    1 
ATOM   15377 C  CD2    . TYR   F 4  135 ? 20.799  -57.044  -113.856 1.00 132.24 ? 135 TYR   F CD2    1 
ATOM   15378 C  CE1    . TYR   F 4  135 ? 19.827  -56.257  -116.305 1.00 134.10 ? 135 TYR   F CE1    1 
ATOM   15379 C  CE2    . TYR   F 4  135 ? 21.002  -55.748  -114.294 1.00 130.39 ? 135 TYR   F CE2    1 
ATOM   15380 C  CZ     . TYR   F 4  135 ? 20.517  -55.360  -115.518 1.00 131.37 ? 135 TYR   F CZ     1 
ATOM   15381 O  OH     . TYR   F 4  135 ? 20.722  -54.068  -115.949 1.00 125.80 ? 135 TYR   F OH     1 
ATOM   15382 N  N      . ASN   F 4  136 ? 20.118  -61.516  -116.675 1.00 143.27 ? 136 ASN   F N      1 
ATOM   15383 C  CA     . ASN   F 4  136 ? 20.505  -61.749  -118.062 1.00 142.72 ? 136 ASN   F CA     1 
ATOM   15384 C  C      . ASN   F 4  136 ? 19.491  -62.599  -118.818 1.00 144.32 ? 136 ASN   F C      1 
ATOM   15385 O  O      . ASN   F 4  136 ? 19.249  -62.348  -120.003 1.00 147.77 ? 136 ASN   F O      1 
ATOM   15386 C  CB     . ASN   F 4  136 ? 21.894  -62.388  -118.127 1.00 142.03 ? 136 ASN   F CB     1 
ATOM   15387 C  CG     . ASN   F 4  136 ? 23.006  -61.390  -117.862 1.00 142.54 ? 136 ASN   F CG     1 
ATOM   15388 O  OD1    . ASN   F 4  136 ? 22.755  -60.270  -117.425 1.00 139.91 ? 136 ASN   F OD1    1 
ATOM   15389 N  ND2    . ASN   F 4  136 ? 24.241  -61.784  -118.154 1.00 143.93 ? 136 ASN   F ND2    1 
ATOM   15390 N  N      . ARG   F 4  137 ? 18.880  -63.596  -118.170 1.00 145.35 ? 137 ARG   F N      1 
ATOM   15391 C  CA     . ARG   F 4  137 ? 17.723  -64.230  -118.793 1.00 146.42 ? 137 ARG   F CA     1 
ATOM   15392 C  C      . ARG   F 4  137 ? 16.657  -63.191  -119.114 1.00 147.26 ? 137 ARG   F C      1 
ATOM   15393 O  O      . ARG   F 4  137 ? 15.922  -63.333  -120.099 1.00 147.11 ? 137 ARG   F O      1 
ATOM   15394 C  CB     . ARG   F 4  137 ? 17.126  -65.310  -117.890 1.00 146.82 ? 137 ARG   F CB     1 
ATOM   15395 C  CG     . ARG   F 4  137 ? 18.115  -66.188  -117.145 1.00 145.97 ? 137 ARG   F CG     1 
ATOM   15396 C  CD     . ARG   F 4  137 ? 17.816  -67.650  -117.368 1.00 148.15 ? 137 ARG   F CD     1 
ATOM   15397 N  NE     . ARG   F 4  137 ? 19.033  -68.451  -117.345 1.00 150.46 ? 137 ARG   F NE     1 
ATOM   15398 C  CZ     . ARG   F 4  137 ? 19.215  -69.564  -118.042 1.00 147.27 ? 137 ARG   F CZ     1 
ATOM   15399 N  NH1    . ARG   F 4  137 ? 18.304  -70.002  -118.895 1.00 145.02 ? 137 ARG   F NH1    1 
ATOM   15400 N  NH2    . ARG   F 4  137 ? 20.330  -70.267  -117.860 1.00 144.97 ? 137 ARG   F NH2    1 
ATOM   15401 N  N      . ARG   F 4  138 ? 16.544  -62.153  -118.277 1.00 146.12 ? 138 ARG   F N      1 
ATOM   15402 C  CA     . ARG   F 4  138 ? 15.720  -60.996  -118.613 1.00 144.99 ? 138 ARG   F CA     1 
ATOM   15403 C  C      . ARG   F 4  138 ? 16.346  -60.181  -119.742 1.00 147.15 ? 138 ARG   F C      1 
ATOM   15404 O  O      . ARG   F 4  138 ? 15.648  -59.783  -120.683 1.00 150.21 ? 138 ARG   F O      1 
ATOM   15405 C  CB     . ARG   F 4  138 ? 15.479  -60.137  -117.367 1.00 141.03 ? 138 ARG   F CB     1 
ATOM   15406 C  CG     . ARG   F 4  138 ? 14.451  -60.773  -116.435 1.00 142.97 ? 138 ARG   F CG     1 
ATOM   15407 C  CD     . ARG   F 4  138 ? 13.119  -60.851  -117.179 1.00 147.59 ? 138 ARG   F CD     1 
ATOM   15408 N  NE     . ARG   F 4  138 ? 11.938  -60.807  -116.319 1.00 146.26 ? 138 ARG   F NE     1 
ATOM   15409 C  CZ     . ARG   F 4  138 ? 11.470  -59.717  -115.726 1.00 135.92 ? 138 ARG   F CZ     1 
ATOM   15410 N  NH1    . ARG   F 4  138 ? 12.183  -58.608  -115.668 1.00 132.92 ? 138 ARG   F NH1    1 
ATOM   15411 N  NH2    . ARG   F 4  138 ? 10.263  -59.747  -115.162 1.00 130.19 ? 138 ARG   F NH2    1 
ATOM   15412 N  N      . ARG   F 4  139 ? 17.663  -59.955  -119.693 1.00 143.30 ? 139 ARG   F N      1 
ATOM   15413 C  CA     . ARG   F 4  139 ? 18.335  -59.301  -120.817 1.00 143.53 ? 139 ARG   F CA     1 
ATOM   15414 C  C      . ARG   F 4  139 ? 18.031  -60.013  -122.129 1.00 145.13 ? 139 ARG   F C      1 
ATOM   15415 O  O      . ARG   F 4  139 ? 17.789  -59.367  -123.159 1.00 140.00 ? 139 ARG   F O      1 
ATOM   15416 C  CB     . ARG   F 4  139 ? 19.846  -59.260  -120.594 1.00 141.35 ? 139 ARG   F CB     1 
ATOM   15417 C  CG     . ARG   F 4  139 ? 20.624  -58.924  -121.865 1.00 137.10 ? 139 ARG   F CG     1 
ATOM   15418 C  CD     . ARG   F 4  139 ? 22.092  -58.647  -121.596 1.00 131.38 ? 139 ARG   F CD     1 
ATOM   15419 N  NE     . ARG   F 4  139 ? 22.250  -57.516  -120.687 1.00 126.97 ? 139 ARG   F NE     1 
ATOM   15420 C  CZ     . ARG   F 4  139 ? 23.413  -57.004  -120.308 1.00 119.42 ? 139 ARG   F CZ     1 
ATOM   15421 N  NH1    . ARG   F 4  139 ? 24.554  -57.425  -120.831 1.00 113.34 ? 139 ARG   F NH1    1 
ATOM   15422 N  NH2    . ARG   F 4  139 ? 23.431  -56.048  -119.379 1.00 116.50 ? 139 ARG   F NH2    1 
ATOM   15423 N  N      . GLU   F 4  140 ? 18.036  -61.350  -122.103 1.00 147.00 ? 140 GLU   F N      1 
ATOM   15424 C  CA     . GLU   F 4  140 ? 17.755  -62.150  -123.289 1.00 146.14 ? 140 GLU   F CA     1 
ATOM   15425 C  C      . GLU   F 4  140 ? 16.338  -61.945  -123.800 1.00 144.15 ? 140 GLU   F C      1 
ATOM   15426 O  O      . GLU   F 4  140 ? 16.081  -62.173  -124.985 1.00 144.79 ? 140 GLU   F O      1 
ATOM   15427 C  CB     . GLU   F 4  140 ? 17.989  -63.630  -122.991 1.00 143.83 ? 140 GLU   F CB     1 
ATOM   15428 C  CG     . GLU   F 4  140 ? 19.366  -63.927  -122.424 1.00 143.67 ? 140 GLU   F CG     1 
ATOM   15429 C  CD     . GLU   F 4  140 ? 19.848  -65.326  -122.745 1.00 143.09 ? 140 GLU   F CD     1 
ATOM   15430 O  OE1    . GLU   F 4  140 ? 20.922  -65.708  -122.233 1.00 140.04 ? 140 GLU   F OE1    1 
ATOM   15431 O  OE2    . GLU   F 4  140 ? 19.159  -66.040  -123.505 1.00 141.87 ? 140 GLU   F OE2    1 
ATOM   15432 N  N      . GLY   F 4  141 ? 15.415  -61.530  -122.941 1.00 141.51 ? 141 GLY   F N      1 
ATOM   15433 C  CA     . GLY   F 4  141 ? 14.103  -61.120  -123.379 1.00 142.23 ? 141 GLY   F CA     1 
ATOM   15434 C  C      . GLY   F 4  141 ? 13.918  -59.625  -123.485 1.00 141.73 ? 141 GLY   F C      1 
ATOM   15435 O  O      . GLY   F 4  141 ? 12.830  -59.182  -123.864 1.00 135.65 ? 141 GLY   F O      1 
ATOM   15436 N  N      . ARG   F 4  142 ? 14.947  -58.833  -123.162 1.00 140.98 ? 142 ARG   F N      1 
ATOM   15437 C  CA     . ARG   F 4  142 ? 14.824  -57.375  -123.063 1.00 141.13 ? 142 ARG   F CA     1 
ATOM   15438 C  C      . ARG   F 4  142 ? 13.601  -56.971  -122.235 1.00 144.82 ? 142 ARG   F C      1 
ATOM   15439 O  O      . ARG   F 4  142 ? 13.010  -55.905  -122.441 1.00 142.99 ? 142 ARG   F O      1 
ATOM   15440 C  CB     . ARG   F 4  142 ? 14.783  -56.730  -124.450 1.00 141.90 ? 142 ARG   F CB     1 
ATOM   15441 C  CG     . ARG   F 4  142 ? 14.895  -55.209  -124.449 1.00 136.51 ? 142 ARG   F CG     1 
ATOM   15442 C  CD     . ARG   F 4  142 ? 15.347  -54.697  -125.808 1.00 132.95 ? 142 ARG   F CD     1 
ATOM   15443 N  NE     . ARG   F 4  142 ? 14.417  -55.080  -126.868 1.00 131.98 ? 142 ARG   F NE     1 
ATOM   15444 C  CZ     . ARG   F 4  142 ? 14.606  -54.847  -128.162 1.00 134.05 ? 142 ARG   F CZ     1 
ATOM   15445 N  NH1    . ARG   F 4  142 ? 15.657  -54.172  -128.599 1.00 134.07 ? 142 ARG   F NH1    1 
ATOM   15446 N  NH2    . ARG   F 4  142 ? 13.710  -55.293  -129.040 1.00 134.85 ? 142 ARG   F NH2    1 
ATOM   15447 N  N      . GLU   F 4  143 ? 13.214  -57.831  -121.291 1.00 147.59 ? 143 GLU   F N      1 
ATOM   15448 C  CA     . GLU   F 4  143 ? 12.093  -57.563  -120.403 1.00 141.75 ? 143 GLU   F CA     1 
ATOM   15449 C  C      . GLU   F 4  143 ? 12.460  -56.473  -119.401 1.00 134.63 ? 143 GLU   F C      1 
ATOM   15450 O  O      . GLU   F 4  143 ? 13.633  -56.129  -119.214 1.00 133.85 ? 143 GLU   F O      1 
ATOM   15451 C  CB     . GLU   F 4  143 ? 11.686  -58.836  -119.656 1.00 140.36 ? 143 GLU   F CB     1 
ATOM   15452 C  CG     . GLU   F 4  143 ? 11.258  -59.997  -120.549 1.00 141.24 ? 143 GLU   F CG     1 
ATOM   15453 C  CD     . GLU   F 4  143 ? 10.882  -61.237  -119.756 1.00 142.05 ? 143 GLU   F CD     1 
ATOM   15454 O  OE1    . GLU   F 4  143 ? 9.808   -61.232  -119.118 1.00 146.21 ? 143 GLU   F OE1    1 
ATOM   15455 O  OE2    . GLU   F 4  143 ? 11.657  -62.218  -119.778 1.00 139.01 ? 143 GLU   F OE2    1 
ATOM   15456 N  N      . GLY   F 4  144 ? 11.435  -55.924  -118.754 1.00 127.32 ? 144 GLY   F N      1 
ATOM   15457 C  CA     . GLY   F 4  144 ? 11.676  -54.977  -117.686 1.00 122.68 ? 144 GLY   F CA     1 
ATOM   15458 C  C      . GLY   F 4  144 ? 12.804  -55.466  -116.806 1.00 124.19 ? 144 GLY   F C      1 
ATOM   15459 O  O      . GLY   F 4  144 ? 12.860  -56.650  -116.467 1.00 128.28 ? 144 GLY   F O      1 
ATOM   15460 N  N      . ASN   F 4  145 ? 13.737  -54.587  -116.464 1.00 121.61 ? 145 ASN   F N      1 
ATOM   15461 C  CA     . ASN   F 4  145 ? 14.836  -54.972  -115.593 1.00 123.71 ? 145 ASN   F CA     1 
ATOM   15462 C  C      . ASN   F 4  145 ? 15.130  -53.859  -114.603 1.00 121.23 ? 145 ASN   F C      1 
ATOM   15463 O  O      . ASN   F 4  145 ? 16.289  -53.554  -114.303 1.00 124.72 ? 145 ASN   F O      1 
ATOM   15464 C  CB     . ASN   F 4  145 ? 16.078  -55.341  -116.399 1.00 127.83 ? 145 ASN   F CB     1 
ATOM   15465 C  CG     . ASN   F 4  145 ? 16.427  -56.818  -116.290 1.00 131.79 ? 145 ASN   F CG     1 
ATOM   15466 O  OD1    . ASN   F 4  145 ? 16.212  -57.448  -115.254 1.00 127.21 ? 145 ASN   F OD1    1 
ATOM   15467 N  ND2    . ASN   F 4  145 ? 16.940  -57.384  -117.376 1.00 137.18 ? 145 ASN   F ND2    1 
ATOM   15468 N  N      . VAL   F 4  146 ? 14.077  -53.230  -114.095 1.00 114.87 ? 146 VAL   F N      1 
ATOM   15469 C  CA     . VAL   F 4  146 ? 14.212  -52.296  -112.986 1.00 117.91 ? 146 VAL   F CA     1 
ATOM   15470 C  C      . VAL   F 4  146 ? 14.230  -53.079  -111.681 1.00 116.07 ? 146 VAL   F C      1 
ATOM   15471 O  O      . VAL   F 4  146 ? 13.650  -54.166  -111.579 1.00 113.15 ? 146 VAL   F O      1 
ATOM   15472 C  CB     . VAL   F 4  146 ? 13.074  -51.259  -113.008 1.00 114.41 ? 146 VAL   F CB     1 
ATOM   15473 C  CG1    . VAL   F 4  146 ? 13.376  -50.112  -112.037 1.00 113.17 ? 146 VAL   F CG1    1 
ATOM   15474 C  CG2    . VAL   F 4  146 ? 12.850  -50.755  -114.427 1.00 115.10 ? 146 VAL   F CG2    1 
ATOM   15475 N  N      . TRP   F 4  147 ? 14.922  -52.541  -110.678 1.00 112.17 ? 147 TRP   F N      1 
ATOM   15476 C  CA     . TRP   F 4  147 ? 15.023  -53.181  -109.373 1.00 108.01 ? 147 TRP   F CA     1 
ATOM   15477 C  C      . TRP   F 4  147 ? 14.993  -52.087  -108.312 1.00 108.91 ? 147 TRP   F C      1 
ATOM   15478 O  O      . TRP   F 4  147 ? 14.712  -50.922  -108.610 1.00 111.72 ? 147 TRP   F O      1 
ATOM   15479 C  CB     . TRP   F 4  147 ? 16.281  -54.056  -109.294 1.00 108.95 ? 147 TRP   F CB     1 
ATOM   15480 C  CG     . TRP   F 4  147 ? 16.348  -55.128  -110.345 1.00 110.83 ? 147 TRP   F CG     1 
ATOM   15481 C  CD1    . TRP   F 4  147 ? 16.593  -54.958  -111.677 1.00 115.35 ? 147 TRP   F CD1    1 
ATOM   15482 C  CD2    . TRP   F 4  147 ? 16.182  -56.536  -110.148 1.00 113.16 ? 147 TRP   F CD2    1 
ATOM   15483 N  NE1    . TRP   F 4  147 ? 16.581  -56.169  -112.323 1.00 119.28 ? 147 TRP   F NE1    1 
ATOM   15484 C  CE2    . TRP   F 4  147 ? 16.333  -57.155  -111.406 1.00 118.00 ? 147 TRP   F CE2    1 
ATOM   15485 C  CE3    . TRP   F 4  147 ? 15.919  -57.333  -109.031 1.00 109.87 ? 147 TRP   F CE3    1 
ATOM   15486 C  CZ2    . TRP   F 4  147 ? 16.228  -58.532  -111.577 1.00 120.52 ? 147 TRP   F CZ2    1 
ATOM   15487 C  CZ3    . TRP   F 4  147 ? 15.813  -58.699  -109.203 1.00 110.05 ? 147 TRP   F CZ3    1 
ATOM   15488 C  CH2    . TRP   F 4  147 ? 15.967  -59.285  -110.466 1.00 114.86 ? 147 TRP   F CH2    1 
ATOM   15489 N  N      . ILE   F 4  148 ? 15.294  -52.466  -107.064 1.00 111.73 ? 148 ILE   F N      1 
ATOM   15490 C  CA     . ILE   F 4  148 ? 15.224  -51.564  -105.917 1.00 109.12 ? 148 ILE   F CA     1 
ATOM   15491 C  C      . ILE   F 4  148 ? 16.197  -52.062  -104.847 1.00 107.64 ? 148 ILE   F C      1 
ATOM   15492 O  O      . ILE   F 4  148 ? 16.695  -53.191  -104.913 1.00 105.06 ? 148 ILE   F O      1 
ATOM   15493 C  CB     . ILE   F 4  148 ? 13.769  -51.465  -105.381 1.00 102.66 ? 148 ILE   F CB     1 
ATOM   15494 C  CG1    . ILE   F 4  148 ? 13.689  -50.632  -104.097 1.00 98.00  ? 148 ILE   F CG1    1 
ATOM   15495 C  CG2    . ILE   F 4  148 ? 13.156  -52.860  -105.216 1.00 101.35 ? 148 ILE   F CG2    1 
ATOM   15496 C  CD1    . ILE   F 4  148 ? 14.281  -49.257  -104.227 1.00 101.89 ? 148 ILE   F CD1    1 
ATOM   15497 N  N      . ALA   F 4  149 ? 16.478  -51.202  -103.861 1.00 104.32 ? 149 ALA   F N      1 
ATOM   15498 C  CA     . ALA   F 4  149 ? 17.468  -51.471  -102.802 1.00 103.67 ? 149 ALA   F CA     1 
ATOM   15499 C  C      . ALA   F 4  149 ? 16.896  -52.210  -101.582 1.00 104.09 ? 149 ALA   F C      1 
ATOM   15500 O  O      . ALA   F 4  149 ? 17.550  -52.314  -100.528 1.00 100.86 ? 149 ALA   F O      1 
ATOM   15501 C  CB     . ALA   F 4  149 ? 18.105  -50.168  -102.345 1.00 96.63  ? 149 ALA   F CB     1 
ATOM   15502 N  N      . LEU   F 4  161 ? 17.425  -45.407  -104.736 1.00 101.12 ? 161 LEU   F N      1 
ATOM   15503 C  CA     . LEU   F 4  161 ? 17.983  -46.749  -104.724 1.00 100.54 ? 161 LEU   F CA     1 
ATOM   15504 C  C      . LEU   F 4  161 ? 17.509  -47.607  -105.928 1.00 110.54 ? 161 LEU   F C      1 
ATOM   15505 O  O      . LEU   F 4  161 ? 17.936  -48.751  -106.079 1.00 110.42 ? 161 LEU   F O      1 
ATOM   15506 C  CB     . LEU   F 4  161 ? 17.646  -47.425  -103.384 1.00 100.12 ? 161 LEU   F CB     1 
ATOM   15507 C  CG     . LEU   F 4  161 ? 16.399  -46.984  -102.600 1.00 95.09  ? 161 LEU   F CG     1 
ATOM   15508 C  CD1    . LEU   F 4  161 ? 15.899  -48.093  -101.701 1.00 88.04  ? 161 LEU   F CD1    1 
ATOM   15509 C  CD2    . LEU   F 4  161 ? 16.654  -45.734  -101.779 1.00 87.15  ? 161 LEU   F CD2    1 
ATOM   15510 N  N      . ILE   F 4  162 ? 16.658  -47.041  -106.799 1.00 114.97 ? 162 ILE   F N      1 
ATOM   15511 C  CA     . ILE   F 4  162 ? 16.134  -47.743  -107.976 1.00 118.02 ? 162 ILE   F CA     1 
ATOM   15512 C  C      . ILE   F 4  162 ? 17.003  -47.448  -109.197 1.00 125.61 ? 162 ILE   F C      1 
ATOM   15513 O  O      . ILE   F 4  162 ? 17.278  -46.281  -109.505 1.00 127.09 ? 162 ILE   F O      1 
ATOM   15514 C  CB     . ILE   F 4  162 ? 14.676  -47.339  -108.259 1.00 113.90 ? 162 ILE   F CB     1 
ATOM   15515 C  CG1    . ILE   F 4  162 ? 13.828  -47.382  -106.991 1.00 103.00 ? 162 ILE   F CG1    1 
ATOM   15516 C  CG2    . ILE   F 4  162 ? 14.085  -48.222  -109.353 1.00 111.89 ? 162 ILE   F CG2    1 
ATOM   15517 C  CD1    . ILE   F 4  162 ? 12.512  -46.675  -107.138 1.00 93.90  ? 162 ILE   F CD1    1 
ATOM   15518 N  N      . SER   F 4  163 ? 17.397  -48.503  -109.922 1.00 126.15 ? 163 SER   F N      1 
ATOM   15519 C  CA     . SER   F 4  163 ? 18.201  -48.384  -111.139 1.00 129.77 ? 163 SER   F CA     1 
ATOM   15520 C  C      . SER   F 4  163 ? 17.615  -49.288  -112.217 1.00 125.04 ? 163 SER   F C      1 
ATOM   15521 O  O      . SER   F 4  163 ? 16.570  -49.917  -112.029 1.00 121.66 ? 163 SER   F O      1 
ATOM   15522 C  CB     . SER   F 4  163 ? 19.675  -48.744  -110.891 1.00 133.22 ? 163 SER   F CB     1 
ATOM   15523 O  OG     . SER   F 4  163 ? 20.240  -47.967  -109.850 1.00 133.28 ? 163 SER   F OG     1 
ATOM   15524 N  N      . SER   F 4  164 ? 18.300  -49.353  -113.360 1.00 127.33 ? 164 SER   F N      1 
ATOM   15525 C  CA     . SER   F 4  164 ? 17.906  -50.242  -114.448 1.00 127.07 ? 164 SER   F CA     1 
ATOM   15526 C  C      . SER   F 4  164 ? 19.100  -51.059  -114.913 1.00 125.30 ? 164 SER   F C      1 
ATOM   15527 O  O      . SER   F 4  164 ? 18.950  -52.202  -115.356 1.00 124.42 ? 164 SER   F O      1 
ATOM   15528 C  CB     . SER   F 4  164 ? 17.322  -49.455  -115.624 1.00 124.45 ? 164 SER   F CB     1 
ATOM   15529 O  OG     . SER   F 4  164 ? 16.205  -48.679  -115.232 1.00 122.33 ? 164 SER   F OG     1 
ATOM   15530 N  N      . GLU   F 4  165 ? 20.285  -50.467  -114.837 1.00 130.26 ? 165 GLU   F N      1 
ATOM   15531 C  CA     . GLU   F 4  165 ? 21.533  -51.162  -115.114 1.00 137.06 ? 165 GLU   F CA     1 
ATOM   15532 C  C      . GLU   F 4  165 ? 22.107  -51.656  -113.794 1.00 135.74 ? 165 GLU   F C      1 
ATOM   15533 O  O      . GLU   F 4  165 ? 22.140  -50.908  -112.809 1.00 136.41 ? 165 GLU   F O      1 
ATOM   15534 C  CB     . GLU   F 4  165 ? 22.535  -50.245  -115.824 1.00 137.69 ? 165 GLU   F CB     1 
ATOM   15535 C  CG     . GLU   F 4  165 ? 22.312  -50.065  -117.331 1.00 135.48 ? 165 GLU   F CG     1 
ATOM   15536 C  CD     . GLU   F 4  165 ? 22.892  -51.202  -118.171 1.00 137.00 ? 165 GLU   F CD     1 
ATOM   15537 O  OE1    . GLU   F 4  165 ? 23.763  -51.947  -117.672 1.00 136.10 ? 165 GLU   F OE1    1 
ATOM   15538 O  OE2    . GLU   F 4  165 ? 22.484  -51.340  -119.345 1.00 134.35 ? 165 GLU   F OE2    1 
ATOM   15539 N  N      . ALA   F 4  166 ? 22.539  -52.918  -113.773 1.00 131.74 ? 166 ALA   F N      1 
ATOM   15540 C  CA     . ALA   F 4  166 ? 23.130  -53.479  -112.564 1.00 133.66 ? 166 ALA   F CA     1 
ATOM   15541 C  C      . ALA   F 4  166 ? 24.208  -52.556  -111.998 1.00 141.13 ? 166 ALA   F C      1 
ATOM   15542 O  O      . ALA   F 4  166 ? 24.050  -51.994  -110.908 1.00 142.10 ? 166 ALA   F O      1 
ATOM   15543 C  CB     . ALA   F 4  166 ? 23.692  -54.874  -112.852 1.00 130.25 ? 166 ALA   F CB     1 
ATOM   15544 N  N      . SER   F 4  167 ? 25.307  -52.372  -112.739 1.00 140.68 ? 167 SER   F N      1 
ATOM   15545 C  CA     . SER   F 4  167 ? 26.455  -51.597  -112.273 1.00 139.94 ? 167 SER   F CA     1 
ATOM   15546 C  C      . SER   F 4  167 ? 26.023  -50.349  -111.510 1.00 143.76 ? 167 SER   F C      1 
ATOM   15547 O  O      . SER   F 4  167 ? 26.656  -49.965  -110.519 1.00 143.24 ? 167 SER   F O      1 
ATOM   15548 C  CB     . SER   F 4  167 ? 27.350  -51.215  -113.453 1.00 138.52 ? 167 SER   F CB     1 
ATOM   15549 O  OG     . SER   F 4  167 ? 27.774  -52.369  -114.154 1.00 137.19 ? 167 SER   F OG     1 
ATOM   15550 N  N      . GLU   F 4  168 ? 24.936  -49.719  -111.964 1.00 144.01 ? 168 GLU   F N      1 
ATOM   15551 C  CA     . GLU   F 4  168 ? 24.367  -48.582  -111.246 1.00 143.81 ? 168 GLU   F CA     1 
ATOM   15552 C  C      . GLU   F 4  168 ? 24.004  -48.967  -109.813 1.00 141.95 ? 168 GLU   F C      1 
ATOM   15553 O  O      . GLU   F 4  168 ? 24.326  -48.248  -108.859 1.00 137.72 ? 168 GLU   F O      1 
ATOM   15554 C  CB     . GLU   F 4  168 ? 23.142  -48.062  -112.010 1.00 140.59 ? 168 GLU   F CB     1 
ATOM   15555 C  CG     . GLU   F 4  168 ? 22.350  -46.930  -111.351 1.00 141.63 ? 168 GLU   F CG     1 
ATOM   15556 C  CD     . GLU   F 4  168 ? 23.205  -45.756  -110.903 1.00 141.87 ? 168 GLU   F CD     1 
ATOM   15557 O  OE1    . GLU   F 4  168 ? 22.922  -44.617  -111.336 1.00 142.25 ? 168 GLU   F OE1    1 
ATOM   15558 O  OE2    . GLU   F 4  168 ? 24.141  -45.961  -110.104 1.00 141.43 ? 168 GLU   F OE2    1 
ATOM   15559 N  N      . LEU   F 4  169 ? 23.349  -50.117  -109.646 1.00 143.02 ? 169 LEU   F N      1 
ATOM   15560 C  CA     . LEU   F 4  169 ? 22.899  -50.547  -108.326 1.00 141.68 ? 169 LEU   F CA     1 
ATOM   15561 C  C      . LEU   F 4  169 ? 24.039  -51.154  -107.507 1.00 144.59 ? 169 LEU   F C      1 
ATOM   15562 O  O      . LEU   F 4  169 ? 24.368  -50.647  -106.428 1.00 146.14 ? 169 LEU   F O      1 
ATOM   15563 C  CB     . LEU   F 4  169 ? 21.738  -51.538  -108.465 1.00 134.50 ? 169 LEU   F CB     1 
ATOM   15564 N  N      . LEU   F 4  170 ? 24.657  -52.241  -108.005 1.00 143.80 ? 170 LEU   F N      1 
ATOM   15565 C  CA     . LEU   F 4  170 ? 25.687  -52.949  -107.233 1.00 140.36 ? 170 LEU   F CA     1 
ATOM   15566 C  C      . LEU   F 4  170 ? 26.738  -52.005  -106.665 1.00 143.56 ? 170 LEU   F C      1 
ATOM   15567 O  O      . LEU   F 4  170 ? 27.288  -52.267  -105.589 1.00 142.16 ? 170 LEU   F O      1 
ATOM   15568 C  CB     . LEU   F 4  170 ? 26.369  -54.038  -108.078 1.00 132.06 ? 170 LEU   F CB     1 
ATOM   15569 C  CG     . LEU   F 4  170 ? 25.526  -55.175  -108.676 1.00 127.57 ? 170 LEU   F CG     1 
ATOM   15570 C  CD1    . LEU   F 4  170 ? 24.604  -54.682  -109.771 1.00 131.97 ? 170 LEU   F CD1    1 
ATOM   15571 C  CD2    . LEU   F 4  170 ? 26.396  -56.334  -109.186 1.00 114.67 ? 170 LEU   F CD2    1 
ATOM   15572 N  N      . ASP   F 4  171 ? 27.028  -50.905  -107.363 1.00 145.23 ? 171 ASP   F N      1 
ATOM   15573 C  CA     . ASP   F 4  171 ? 27.961  -49.909  -106.853 1.00 145.39 ? 171 ASP   F CA     1 
ATOM   15574 C  C      . ASP   F 4  171 ? 27.383  -49.092  -105.701 1.00 144.70 ? 171 ASP   F C      1 
ATOM   15575 O  O      . ASP   F 4  171 ? 28.146  -48.418  -105.002 1.00 143.08 ? 171 ASP   F O      1 
ATOM   15576 C  CB     . ASP   F 4  171 ? 28.392  -48.985  -107.993 1.00 145.59 ? 171 ASP   F CB     1 
ATOM   15577 C  CG     . ASP   F 4  171 ? 29.886  -48.748  -108.016 1.00 146.65 ? 171 ASP   F CG     1 
ATOM   15578 O  OD1    . ASP   F 4  171 ? 30.541  -48.990  -106.979 1.00 146.42 ? 171 ASP   F OD1    1 
ATOM   15579 O  OD2    . ASP   F 4  171 ? 30.408  -48.345  -109.078 1.00 145.72 ? 171 ASP   F OD2    1 
ATOM   15580 N  N      . PHE   F 4  172 ? 26.063  -49.138  -105.487 1.00 144.62 ? 172 PHE   F N      1 
ATOM   15581 C  CA     . PHE   F 4  172 ? 25.436  -48.400  -104.391 1.00 141.03 ? 172 PHE   F CA     1 
ATOM   15582 C  C      . PHE   F 4  172 ? 25.602  -49.120  -103.058 1.00 145.26 ? 172 PHE   F C      1 
ATOM   15583 O  O      . PHE   F 4  172 ? 25.917  -48.484  -102.045 1.00 144.90 ? 172 PHE   F O      1 
ATOM   15584 C  CB     . PHE   F 4  172 ? 23.954  -48.177  -104.693 1.00 135.36 ? 172 PHE   F CB     1 
ATOM   15585 C  CG     . PHE   F 4  172 ? 23.243  -47.262  -103.718 1.00 132.53 ? 172 PHE   F CG     1 
ATOM   15586 C  CD1    . PHE   F 4  172 ? 23.929  -46.598  -102.716 1.00 135.21 ? 172 PHE   F CD1    1 
ATOM   15587 C  CD2    . PHE   F 4  172 ? 21.872  -47.079  -103.806 1.00 131.98 ? 172 PHE   F CD2    1 
ATOM   15588 C  CE1    . PHE   F 4  172 ? 23.271  -45.773  -101.826 1.00 134.21 ? 172 PHE   F CE1    1 
ATOM   15589 C  CE2    . PHE   F 4  172 ? 21.204  -46.250  -102.911 1.00 130.86 ? 172 PHE   F CE2    1 
ATOM   15590 C  CZ     . PHE   F 4  172 ? 21.906  -45.597  -101.922 1.00 133.65 ? 172 PHE   F CZ     1 
ATOM   15591 N  N      . ILE   F 4  173 ? 25.396  -50.441  -103.034 1.00 149.00 ? 173 ILE   F N      1 
ATOM   15592 C  CA     . ILE   F 4  173 ? 25.435  -51.181  -101.771 1.00 148.86 ? 173 ILE   F CA     1 
ATOM   15593 C  C      . ILE   F 4  173 ? 26.798  -51.039  -101.106 1.00 147.75 ? 173 ILE   F C      1 
ATOM   15594 O  O      . ILE   F 4  173 ? 26.895  -50.888  -99.880  1.00 143.90 ? 173 ILE   F O      1 
ATOM   15595 C  CB     . ILE   F 4  173 ? 25.066  -52.662  -101.994 1.00 147.11 ? 173 ILE   F CB     1 
ATOM   15596 C  CG1    . ILE   F 4  173 ? 25.948  -53.290  -103.078 1.00 145.70 ? 173 ILE   F CG1    1 
ATOM   15597 C  CG2    . ILE   F 4  173 ? 23.588  -52.809  -102.336 1.00 142.37 ? 173 ILE   F CG2    1 
ATOM   15598 C  CD1    . ILE   F 4  173 ? 25.584  -54.729  -103.396 1.00 137.56 ? 173 ILE   F CD1    1 
ATOM   15599 N  N      . ASP   F 4  174 ? 27.872  -51.092  -101.901 1.00 150.10 ? 174 ASP   F N      1 
ATOM   15600 C  CA     . ASP   F 4  174 ? 29.215  -50.888  -101.371 1.00 146.57 ? 174 ASP   F CA     1 
ATOM   15601 C  C      . ASP   F 4  174 ? 29.451  -49.446  -100.940 1.00 144.73 ? 174 ASP   F C      1 
ATOM   15602 O  O      . ASP   F 4  174 ? 30.294  -49.206  -100.070 1.00 145.10 ? 174 ASP   F O      1 
ATOM   15603 C  CB     . ASP   F 4  174 ? 30.252  -51.307  -102.412 1.00 140.60 ? 174 ASP   F CB     1 
ATOM   15604 C  CG     . ASP   F 4  174 ? 29.894  -52.608  -103.089 1.00 138.74 ? 174 ASP   F CG     1 
ATOM   15605 O  OD1    . ASP   F 4  174 ? 30.108  -53.676  -102.479 1.00 136.94 ? 174 ASP   F OD1    1 
ATOM   15606 O  OD2    . ASP   F 4  174 ? 29.381  -52.562  -104.225 1.00 140.49 ? 174 ASP   F OD2    1 
ATOM   15607 N  N      . GLU   F 4  175 ? 28.724  -48.486  -101.522 1.00 146.25 ? 175 GLU   F N      1 
ATOM   15608 C  CA     . GLU   F 4  175 ? 28.804  -47.093  -101.096 1.00 146.18 ? 175 GLU   F CA     1 
ATOM   15609 C  C      . GLU   F 4  175 ? 28.209  -46.864  -99.713  1.00 145.19 ? 175 GLU   F C      1 
ATOM   15610 O  O      . GLU   F 4  175 ? 28.350  -45.761  -99.174  1.00 144.05 ? 175 GLU   F O      1 
ATOM   15611 C  CB     . GLU   F 4  175 ? 28.104  -46.185  -102.112 1.00 143.92 ? 175 GLU   F CB     1 
ATOM   15612 C  CG     . GLU   F 4  175 ? 28.855  -46.048  -103.419 1.00 144.25 ? 175 GLU   F CG     1 
ATOM   15613 C  CD     . GLU   F 4  175 ? 30.353  -46.171  -103.229 1.00 144.84 ? 175 GLU   F CD     1 
ATOM   15614 O  OE1    . GLU   F 4  175 ? 30.902  -45.437  -102.381 1.00 145.12 ? 175 GLU   F OE1    1 
ATOM   15615 O  OE2    . GLU   F 4  175 ? 30.978  -47.009  -103.914 1.00 141.54 ? 175 GLU   F OE2    1 
ATOM   15616 N  N      . GLN   F 4  176 ? 27.543  -47.866  -99.138  1.00 147.63 ? 176 GLN   F N      1 
ATOM   15617 C  CA     . GLN   F 4  176 ? 27.021  -47.806  -97.777  1.00 145.11 ? 176 GLN   F CA     1 
ATOM   15618 C  C      . GLN   F 4  176 ? 27.797  -48.676  -96.803  1.00 141.66 ? 176 GLN   F C      1 
ATOM   15619 O  O      . GLN   F 4  176 ? 28.083  -48.235  -95.687  1.00 139.28 ? 176 GLN   F O      1 
ATOM   15620 C  CB     . GLN   F 4  176 ? 25.541  -48.213  -97.754  1.00 143.23 ? 176 GLN   F CB     1 
ATOM   15621 C  CG     . GLN   F 4  176 ? 24.658  -47.389  -98.685  1.00 141.15 ? 176 GLN   F CG     1 
ATOM   15622 C  CD     . GLN   F 4  176 ? 24.585  -45.928  -98.275  1.00 139.77 ? 176 GLN   F CD     1 
ATOM   15623 O  OE1    . GLN   F 4  176 ? 25.221  -45.509  -97.308  1.00 138.41 ? 176 GLN   F OE1    1 
ATOM   15624 N  NE2    . GLN   F 4  176 ? 23.807  -45.146  -99.011  1.00 136.96 ? 176 GLN   F NE2    1 
ATOM   15625 N  N      . GLY   F 4  177 ? 28.151  -49.900  -97.199  1.00 140.39 ? 177 GLY   F N      1 
ATOM   15626 C  CA     . GLY   F 4  177 ? 28.984  -50.781  -96.407  1.00 138.90 ? 177 GLY   F CA     1 
ATOM   15627 C  C      . GLY   F 4  177 ? 28.248  -51.925  -95.740  1.00 140.59 ? 177 GLY   F C      1 
ATOM   15628 O  O      . GLY   F 4  177 ? 28.890  -52.920  -95.370  1.00 137.96 ? 177 GLY   F O      1 
ATOM   15629 N  N      . GLN   F 4  178 ? 26.926  -51.817  -95.570  1.00 143.32 ? 178 GLN   F N      1 
ATOM   15630 C  CA     . GLN   F 4  178 ? 26.117  -52.837  -94.914  1.00 139.33 ? 178 GLN   F CA     1 
ATOM   15631 C  C      . GLN   F 4  178 ? 25.462  -53.758  -95.946  1.00 136.77 ? 178 GLN   F C      1 
ATOM   15632 O  O      . GLN   F 4  178 ? 25.563  -53.557  -97.160  1.00 137.95 ? 178 GLN   F O      1 
ATOM   15633 C  CB     . GLN   F 4  178 ? 25.049  -52.201  -94.017  1.00 129.53 ? 178 GLN   F CB     1 
ATOM   15634 C  CG     . GLN   F 4  178 ? 25.590  -51.434  -92.829  1.00 131.54 ? 178 GLN   F CG     1 
ATOM   15635 C  CD     . GLN   F 4  178 ? 25.566  -49.936  -93.049  1.00 139.61 ? 178 GLN   F CD     1 
ATOM   15636 O  OE1    . GLN   F 4  178 ? 26.036  -49.441  -94.076  1.00 142.58 ? 178 GLN   F OE1    1 
ATOM   15637 N  NE2    . GLN   F 4  178 ? 25.013  -49.203  -92.087  1.00 136.68 ? 178 GLN   F NE2    1 
ATOM   15638 N  N      . VAL   F 4  179 ? 24.774  -54.788  -95.444  1.00 132.06 ? 179 VAL   F N      1 
ATOM   15639 C  CA     . VAL   F 4  179 ? 24.070  -55.719  -96.315  1.00 124.46 ? 179 VAL   F CA     1 
ATOM   15640 C  C      . VAL   F 4  179 ? 22.853  -55.035  -96.916  1.00 127.19 ? 179 VAL   F C      1 
ATOM   15641 O  O      . VAL   F 4  179 ? 22.122  -54.305  -96.231  1.00 126.74 ? 179 VAL   F O      1 
ATOM   15642 C  CB     . VAL   F 4  179 ? 23.642  -56.980  -95.548  1.00 123.12 ? 179 VAL   F CB     1 
ATOM   15643 C  CG1    . VAL   F 4  179 ? 22.955  -57.955  -96.495  1.00 112.04 ? 179 VAL   F CG1    1 
ATOM   15644 C  CG2    . VAL   F 4  179 ? 24.826  -57.614  -94.842  1.00 122.35 ? 179 VAL   F CG2    1 
ATOM   15645 N  N      . HIS   F 4  180 ? 22.621  -55.280  -98.198  1.00 126.41 ? 180 HIS   F N      1 
ATOM   15646 C  CA     . HIS   F 4  180 ? 21.424  -54.804  -98.867  1.00 120.34 ? 180 HIS   F CA     1 
ATOM   15647 C  C      . HIS   F 4  180 ? 20.797  -55.961  -99.630  1.00 112.80 ? 180 HIS   F C      1 
ATOM   15648 O  O      . HIS   F 4  180 ? 21.403  -57.022  -99.810  1.00 112.39 ? 180 HIS   F O      1 
ATOM   15649 C  CB     . HIS   F 4  180 ? 21.731  -53.623  -99.801  1.00 118.23 ? 180 HIS   F CB     1 
ATOM   15650 C  CG     . HIS   F 4  180 ? 21.486  -52.283  -99.174  1.00 125.06 ? 180 HIS   F CG     1 
ATOM   15651 N  ND1    . HIS   F 4  180 ? 20.376  -52.014  -98.400  1.00 124.21 ? 180 HIS   F ND1    1 
ATOM   15652 C  CD2    . HIS   F 4  180 ? 22.222  -51.146  -99.183  1.00 127.40 ? 180 HIS   F CD2    1 
ATOM   15653 C  CE1    . HIS   F 4  180 ? 20.431  -50.764  -97.975  1.00 119.04 ? 180 HIS   F CE1    1 
ATOM   15654 N  NE2    . HIS   F 4  180 ? 21.540  -50.215  -98.437  1.00 118.45 ? 180 HIS   F NE2    1 
ATOM   15655 N  N      . VAL   F 4  181 ? 19.552  -55.756  -100.041 1.00 108.91 ? 181 VAL   F N      1 
ATOM   15656 C  CA     . VAL   F 4  181 ? 18.832  -56.721  -100.857 1.00 108.88 ? 181 VAL   F CA     1 
ATOM   15657 C  C      . VAL   F 4  181 ? 18.178  -55.959  -101.997 1.00 107.54 ? 181 VAL   F C      1 
ATOM   15658 O  O      . VAL   F 4  181 ? 17.802  -54.790  -101.853 1.00 102.46 ? 181 VAL   F O      1 
ATOM   15659 C  CB     . VAL   F 4  181 ? 17.787  -57.517  -100.041 1.00 104.17 ? 181 VAL   F CB     1 
ATOM   15660 C  CG1    . VAL   F 4  181 ? 16.839  -56.572  -99.308  1.00 89.86  ? 181 VAL   F CG1    1 
ATOM   15661 C  CG2    . VAL   F 4  181 ? 17.023  -58.493  -100.941 1.00 102.38 ? 181 VAL   F CG2    1 
ATOM   15662 N  N      . ILE   F 4  182 ? 18.057  -56.626  -103.141 1.00 103.00 ? 182 ILE   F N      1 
ATOM   15663 C  CA     . ILE   F 4  182 ? 17.534  -56.020  -104.360 1.00 108.05 ? 182 ILE   F CA     1 
ATOM   15664 C  C      . ILE   F 4  182 ? 16.408  -56.880  -104.904 1.00 106.27 ? 182 ILE   F C      1 
ATOM   15665 O  O      . ILE   F 4  182 ? 16.483  -58.114  -104.870 1.00 102.19 ? 182 ILE   F O      1 
ATOM   15666 C  CB     . ILE   F 4  182 ? 18.630  -55.863  -105.424 1.00 112.58 ? 182 ILE   F CB     1 
ATOM   15667 C  CG1    . ILE   F 4  182 ? 19.466  -57.141  -105.434 1.00 111.74 ? 182 ILE   F CG1    1 
ATOM   15668 C  CG2    . ILE   F 4  182 ? 19.463  -54.609  -105.178 1.00 110.29 ? 182 ILE   F CG2    1 
ATOM   15669 C  CD1    . ILE   F 4  182 ? 20.290  -57.331  -106.661 1.00 110.16 ? 182 ILE   F CD1    1 
ATOM   15670 N  N      . GLN   F 4  183 ? 15.411  -56.220  -105.486 1.00 104.38 ? 183 GLN   F N      1 
ATOM   15671 C  CA     . GLN   F 4  183 ? 14.127  -56.840  -105.759 1.00 105.95 ? 183 GLN   F CA     1 
ATOM   15672 C  C      . GLN   F 4  183 ? 13.534  -56.288  -107.040 1.00 107.61 ? 183 GLN   F C      1 
ATOM   15673 O  O      . GLN   F 4  183 ? 13.640  -55.088  -107.322 1.00 108.15 ? 183 GLN   F O      1 
ATOM   15674 C  CB     . GLN   F 4  183 ? 13.148  -56.590  -104.612 1.00 101.34 ? 183 GLN   F CB     1 
ATOM   15675 C  CG     . GLN   F 4  183 ? 12.250  -57.748  -104.304 1.00 90.99  ? 183 GLN   F CG     1 
ATOM   15676 C  CD     . GLN   F 4  183 ? 11.339  -57.430  -103.158 1.00 90.14  ? 183 GLN   F CD     1 
ATOM   15677 O  OE1    . GLN   F 4  183 ? 11.248  -56.275  -102.724 1.00 86.73  ? 183 GLN   F OE1    1 
ATOM   15678 N  NE2    . GLN   F 4  183 ? 10.678  -58.454  -102.629 1.00 88.89  ? 183 GLN   F NE2    1 
ATOM   15679 N  N      . LYS   F 4  184 ? 12.891  -57.175  -107.797 1.00 104.18 ? 184 LYS   F N      1 
ATOM   15680 C  CA     . LYS   F 4  184 ? 12.172  -56.783  -108.996 1.00 102.44 ? 184 LYS   F CA     1 
ATOM   15681 C  C      . LYS   F 4  184 ? 11.251  -55.618  -108.672 1.00 104.01 ? 184 LYS   F C      1 
ATOM   15682 O  O      . LYS   F 4  184 ? 10.288  -55.778  -107.918 1.00 105.40 ? 184 LYS   F O      1 
ATOM   15683 C  CB     . LYS   F 4  184 ? 11.377  -57.964  -109.550 1.00 96.59  ? 184 LYS   F CB     1 
ATOM   15684 N  N      . TYR   F 4  185 ? 11.558  -54.437  -109.197 1.00 104.31 ? 185 TYR   F N      1 
ATOM   15685 C  CA     . TYR   F 4  185 ? 10.619  -53.336  -109.084 1.00 101.18 ? 185 TYR   F CA     1 
ATOM   15686 C  C      . TYR   F 4  185 ? 9.365   -53.675  -109.880 1.00 105.47 ? 185 TYR   F C      1 
ATOM   15687 O  O      . TYR   F 4  185 ? 9.438   -54.306  -110.939 1.00 106.53 ? 185 TYR   F O      1 
ATOM   15688 C  CB     . TYR   F 4  185 ? 11.243  -52.039  -109.588 1.00 100.16 ? 185 TYR   F CB     1 
ATOM   15689 C  CG     . TYR   F 4  185 ? 10.501  -50.832  -109.097 1.00 99.56  ? 185 TYR   F CG     1 
ATOM   15690 C  CD1    . TYR   F 4  185 ? 9.612   -50.167  -109.916 1.00 96.85  ? 185 TYR   F CD1    1 
ATOM   15691 C  CD2    . TYR   F 4  185 ? 10.685  -50.360  -107.807 1.00 102.51 ? 185 TYR   F CD2    1 
ATOM   15692 C  CE1    . TYR   F 4  185 ? 8.926   -49.063  -109.467 1.00 99.99  ? 185 TYR   F CE1    1 
ATOM   15693 C  CE2    . TYR   F 4  185 ? 10.008  -49.255  -107.348 1.00 100.54 ? 185 TYR   F CE2    1 
ATOM   15694 C  CZ     . TYR   F 4  185 ? 9.129   -48.609  -108.181 1.00 99.97  ? 185 TYR   F CZ     1 
ATOM   15695 O  OH     . TYR   F 4  185 ? 8.449   -47.508  -107.719 1.00 104.15 ? 185 TYR   F OH     1 
ATOM   15696 N  N      . LEU   F 4  186 ? 8.206   -53.277  -109.350 1.00 101.80 ? 186 LEU   F N      1 
ATOM   15697 C  CA     . LEU   F 4  186 ? 6.913   -53.575  -109.964 1.00 99.06  ? 186 LEU   F CA     1 
ATOM   15698 C  C      . LEU   F 4  186 ? 6.607   -52.456  -110.952 1.00 96.72  ? 186 LEU   F C      1 
ATOM   15699 O  O      . LEU   F 4  186 ? 5.915   -51.478  -110.657 1.00 95.27  ? 186 LEU   F O      1 
ATOM   15700 C  CB     . LEU   F 4  186 ? 5.829   -53.725  -108.905 1.00 98.47  ? 186 LEU   F CB     1 
ATOM   15701 C  CG     . LEU   F 4  186 ? 6.141   -54.748  -107.807 1.00 99.02  ? 186 LEU   F CG     1 
ATOM   15702 C  CD1    . LEU   F 4  186 ? 5.007   -54.844  -106.787 1.00 89.59  ? 186 LEU   F CD1    1 
ATOM   15703 C  CD2    . LEU   F 4  186 ? 6.457   -56.114  -108.401 1.00 89.64  ? 186 LEU   F CD2    1 
ATOM   15704 N  N      . GLU   F 4  187 ? 7.160   -52.619  -112.155 1.00 97.75  ? 187 GLU   F N      1 
ATOM   15705 C  CA     . GLU   F 4  187 ? 7.089   -51.571  -113.163 1.00 97.68  ? 187 GLU   F CA     1 
ATOM   15706 C  C      . GLU   F 4  187 ? 5.645   -51.212  -113.488 1.00 94.94  ? 187 GLU   F C      1 
ATOM   15707 O  O      . GLU   F 4  187 ? 5.335   -50.041  -113.736 1.00 97.33  ? 187 GLU   F O      1 
ATOM   15708 C  CB     . GLU   F 4  187 ? 7.853   -52.012  -114.418 1.00 102.53 ? 187 GLU   F CB     1 
ATOM   15709 C  CG     . GLU   F 4  187 ? 9.336   -52.338  -114.165 1.00 103.88 ? 187 GLU   F CG     1 
ATOM   15710 C  CD     . GLU   F 4  187 ? 9.991   -53.137  -115.287 1.00 104.57 ? 187 GLU   F CD     1 
ATOM   15711 O  OE1    . GLU   F 4  187 ? 9.261   -53.738  -116.098 1.00 106.96 ? 187 GLU   F OE1    1 
ATOM   15712 O  OE2    . GLU   F 4  187 ? 11.240  -53.163  -115.358 1.00 109.12 ? 187 GLU   F OE2    1 
ATOM   15713 N  N      . LYS   F 4  188 ? 4.737   -52.199  -113.462 1.00 92.14  ? 188 LYS   F N      1 
ATOM   15714 C  CA     . LYS   F 4  188 ? 3.339   -51.941  -113.786 1.00 86.60  ? 188 LYS   F CA     1 
ATOM   15715 C  C      . LYS   F 4  188 ? 2.447   -52.029  -112.547 1.00 85.93  ? 188 LYS   F C      1 
ATOM   15716 O  O      . LYS   F 4  188 ? 1.688   -52.995  -112.393 1.00 82.10  ? 188 LYS   F O      1 
ATOM   15717 C  CB     . LYS   F 4  188 ? 2.865   -52.907  -114.878 1.00 83.13  ? 188 LYS   F CB     1 
ATOM   15718 C  CG     . LYS   F 4  188 ? 1.693   -52.365  -115.702 1.00 92.33  ? 188 LYS   F CG     1 
ATOM   15719 C  CD     . LYS   F 4  188 ? 1.712   -52.851  -117.157 1.00 92.36  ? 188 LYS   F CD     1 
ATOM   15720 C  CE     . LYS   F 4  188 ? 1.686   -51.675  -118.157 1.00 93.11  ? 188 LYS   F CE     1 
ATOM   15721 N  NZ     . LYS   F 4  188 ? 0.412   -50.873  -118.200 1.00 87.35  ? 188 LYS   F NZ     1 
ATOM   15722 N  N      . PRO   F 4  189 ? 2.487   -51.035  -111.661 1.00 82.92  ? 189 PRO   F N      1 
ATOM   15723 C  CA     . PRO   F 4  189 ? 1.629   -51.058  -110.477 1.00 77.81  ? 189 PRO   F CA     1 
ATOM   15724 C  C      . PRO   F 4  189 ? 0.233   -50.548  -110.779 1.00 81.48  ? 189 PRO   F C      1 
ATOM   15725 O  O      . PRO   F 4  189 ? -0.025  -49.915  -111.800 1.00 88.52  ? 189 PRO   F O      1 
ATOM   15726 C  CB     . PRO   F 4  189 ? 2.344   -50.106  -109.519 1.00 84.46  ? 189 PRO   F CB     1 
ATOM   15727 C  CG     . PRO   F 4  189 ? 2.899   -49.077  -110.438 1.00 89.29  ? 189 PRO   F CG     1 
ATOM   15728 C  CD     . PRO   F 4  189 ? 3.298   -49.807  -111.709 1.00 86.99  ? 189 PRO   F CD     1 
ATOM   15729 N  N      . LEU   F 4  190 ? -0.673  -50.835  -109.855 1.00 82.66  ? 190 LEU   F N      1 
ATOM   15730 C  CA     . LEU   F 4  190 ? -2.029  -50.320  -109.934 1.00 81.27  ? 190 LEU   F CA     1 
ATOM   15731 C  C      . LEU   F 4  190 ? -2.025  -48.861  -109.503 1.00 87.44  ? 190 LEU   F C      1 
ATOM   15732 O  O      . LEU   F 4  190 ? -1.556  -48.535  -108.408 1.00 94.99  ? 190 LEU   F O      1 
ATOM   15733 C  CB     . LEU   F 4  190 ? -2.965  -51.142  -109.046 1.00 73.95  ? 190 LEU   F CB     1 
ATOM   15734 C  CG     . LEU   F 4  190 ? -4.463  -50.902  -109.243 1.00 76.54  ? 190 LEU   F CG     1 
ATOM   15735 C  CD1    . LEU   F 4  190 ? -5.092  -51.994  -110.115 1.00 74.04  ? 190 LEU   F CD1    1 
ATOM   15736 C  CD2    . LEU   F 4  190 ? -5.173  -50.789  -107.907 1.00 74.39  ? 190 LEU   F CD2    1 
ATOM   15737 N  N      . LEU   F 4  191 ? -2.541  -47.979  -110.358 1.00 87.80  ? 191 LEU   F N      1 
ATOM   15738 C  CA     . LEU   F 4  191 ? -2.514  -46.544  -110.098 1.00 91.70  ? 191 LEU   F CA     1 
ATOM   15739 C  C      . LEU   F 4  191 ? -3.929  -46.003  -109.983 1.00 88.91  ? 191 LEU   F C      1 
ATOM   15740 O  O      . LEU   F 4  191 ? -4.740  -46.172  -110.898 1.00 90.63  ? 191 LEU   F O      1 
ATOM   15741 C  CB     . LEU   F 4  191 ? -1.757  -45.800  -111.195 1.00 93.49  ? 191 LEU   F CB     1 
ATOM   15742 C  CG     . LEU   F 4  191 ? -0.493  -46.505  -111.679 1.00 95.61  ? 191 LEU   F CG     1 
ATOM   15743 C  CD1    . LEU   F 4  191 ? -0.846  -47.441  -112.817 1.00 95.24  ? 191 LEU   F CD1    1 
ATOM   15744 C  CD2    . LEU   F 4  191 ? 0.553   -45.499  -112.115 1.00 100.12 ? 191 LEU   F CD2    1 
ATOM   15745 N  N      . LEU   F 4  192 ? -4.213  -45.347  -108.865 1.00 86.21  ? 192 LEU   F N      1 
ATOM   15746 C  CA     . LEU   F 4  192 ? -5.522  -44.749  -108.664 1.00 85.67  ? 192 LEU   F CA     1 
ATOM   15747 C  C      . LEU   F 4  192 ? -5.720  -43.566  -109.598 1.00 91.90  ? 192 LEU   F C      1 
ATOM   15748 O  O      . LEU   F 4  192 ? -4.791  -42.800  -109.862 1.00 96.24  ? 192 LEU   F O      1 
ATOM   15749 C  CB     . LEU   F 4  192 ? -5.674  -44.275  -107.226 1.00 88.74  ? 192 LEU   F CB     1 
ATOM   15750 C  CG     . LEU   F 4  192 ? -5.647  -45.309  -106.115 1.00 92.74  ? 192 LEU   F CG     1 
ATOM   15751 C  CD1    . LEU   F 4  192 ? -4.241  -45.837  -105.940 1.00 95.59  ? 192 LEU   F CD1    1 
ATOM   15752 C  CD2    . LEU   F 4  192 ? -6.143  -44.665  -104.854 1.00 82.32  ? 192 LEU   F CD2    1 
ATOM   15753 N  N      . GLU   F 4  193 ? -6.939  -43.408  -110.089 1.00 94.23  ? 193 GLU   F N      1 
ATOM   15754 C  CA     . GLU   F 4  193 ? -7.296  -42.199  -110.806 1.00 93.23  ? 193 GLU   F CA     1 
ATOM   15755 C  C      . GLU   F 4  193 ? -8.447  -41.516  -110.078 1.00 91.17  ? 193 GLU   F C      1 
ATOM   15756 O  O      . GLU   F 4  193 ? -9.293  -42.193  -109.488 1.00 90.77  ? 193 GLU   F O      1 
ATOM   15757 C  CB     . GLU   F 4  193 ? -7.693  -42.500  -112.258 1.00 90.98  ? 193 GLU   F CB     1 
ATOM   15758 C  CG     . GLU   F 4  193 ? -6.831  -43.541  -112.975 1.00 85.65  ? 193 GLU   F CG     1 
ATOM   15759 C  CD     . GLU   F 4  193 ? -5.446  -43.023  -113.343 1.00 92.47  ? 193 GLU   F CD     1 
ATOM   15760 O  OE1    . GLU   F 4  193 ? -5.184  -41.823  -113.126 1.00 94.99  ? 193 GLU   F OE1    1 
ATOM   15761 O  OE2    . GLU   F 4  193 ? -4.620  -43.810  -113.864 1.00 93.75  ? 193 GLU   F OE2    1 
ATOM   15762 N  N      . PRO   F 4  194 ? -8.503  -40.184  -110.080 1.00 92.96  ? 194 PRO   F N      1 
ATOM   15763 C  CA     . PRO   F 4  194 ? -7.626  -39.236  -110.770 1.00 94.71  ? 194 PRO   F CA     1 
ATOM   15764 C  C      . PRO   F 4  194 ? -6.265  -39.081  -110.105 1.00 99.23  ? 194 PRO   F C      1 
ATOM   15765 O  O      . PRO   F 4  194 ? -6.174  -38.840  -108.906 1.00 103.67 ? 194 PRO   F O      1 
ATOM   15766 C  CB     . PRO   F 4  194 ? -8.436  -37.937  -110.709 1.00 102.13 ? 194 PRO   F CB     1 
ATOM   15767 C  CG     . PRO   F 4  194 ? -9.156  -38.031  -109.400 1.00 96.83  ? 194 PRO   F CG     1 
ATOM   15768 C  CD     . PRO   F 4  194 ? -9.505  -39.490  -109.249 1.00 98.60  ? 194 PRO   F CD     1 
ATOM   15769 N  N      . GLY   F 4  195 ? -5.182  -39.207  -110.864 1.00 97.35  ? 195 GLY   F N      1 
ATOM   15770 C  CA     . GLY   F 4  195 ? -3.862  -38.977  -110.320 1.00 92.26  ? 195 GLY   F CA     1 
ATOM   15771 C  C      . GLY   F 4  195 ? -2.786  -39.793  -111.000 1.00 96.52  ? 195 GLY   F C      1 
ATOM   15772 O  O      . GLY   F 4  195 ? -1.637  -39.356  -111.097 1.00 104.12 ? 195 GLY   F O      1 
ATOM   15773 N  N      . HIS   F 4  196 ? -3.139  -40.987  -111.464 1.00 95.74  ? 196 HIS   F N      1 
ATOM   15774 C  CA     . HIS   F 4  196 ? -2.166  -41.958  -111.961 1.00 98.14  ? 196 HIS   F CA     1 
ATOM   15775 C  C      . HIS   F 4  196 ? -1.023  -42.132  -110.951 1.00 102.69 ? 196 HIS   F C      1 
ATOM   15776 O  O      . HIS   F 4  196 ? 0.135   -41.790  -111.196 1.00 104.79 ? 196 HIS   F O      1 
ATOM   15777 C  CB     . HIS   F 4  196 ? -1.657  -41.538  -113.341 1.00 92.62  ? 196 HIS   F CB     1 
ATOM   15778 C  CG     . HIS   F 4  196 ? -1.531  -42.678  -114.304 1.00 97.33  ? 196 HIS   F CG     1 
ATOM   15779 N  ND1    . HIS   F 4  196 ? -2.584  -43.512  -114.612 1.00 95.70  ? 196 HIS   F ND1    1 
ATOM   15780 C  CD2    . HIS   F 4  196 ? -0.475  -43.122  -115.027 1.00 96.79  ? 196 HIS   F CD2    1 
ATOM   15781 C  CE1    . HIS   F 4  196 ? -2.183  -44.421  -115.483 1.00 102.21 ? 196 HIS   F CE1    1 
ATOM   15782 N  NE2    . HIS   F 4  196 ? -0.907  -44.206  -115.753 1.00 99.13  ? 196 HIS   F NE2    1 
ATOM   15783 N  N      . ARG   F 4  197 ? -1.393  -42.716  -109.803 1.00 102.41 ? 197 ARG   F N      1 
ATOM   15784 C  CA     . ARG   F 4  197 ? -0.644  -42.602  -108.554 1.00 100.34 ? 197 ARG   F CA     1 
ATOM   15785 C  C      . ARG   F 4  197 ? -0.408  -43.959  -107.901 1.00 100.84 ? 197 ARG   F C      1 
ATOM   15786 O  O      . ARG   F 4  197 ? -1.307  -44.806  -107.855 1.00 97.50  ? 197 ARG   F O      1 
ATOM   15787 C  CB     . ARG   F 4  197 ? -1.402  -41.693  -107.584 1.00 96.28  ? 197 ARG   F CB     1 
ATOM   15788 C  CG     . ARG   F 4  197 ? -2.463  -40.874  -108.285 1.00 98.08  ? 197 ARG   F CG     1 
ATOM   15789 C  CD     . ARG   F 4  197 ? -3.556  -40.413  -107.363 1.00 100.65 ? 197 ARG   F CD     1 
ATOM   15790 N  NE     . ARG   F 4  197 ? -3.042  -40.133  -106.033 1.00 99.22  ? 197 ARG   F NE     1 
ATOM   15791 C  CZ     . ARG   F 4  197 ? -3.793  -40.095  -104.944 1.00 103.40 ? 197 ARG   F CZ     1 
ATOM   15792 N  NH1    . ARG   F 4  197 ? -5.097  -40.325  -104.993 1.00 93.70  ? 197 ARG   F NH1    1 
ATOM   15793 N  NH2    . ARG   F 4  197 ? -3.220  -39.829  -103.774 1.00 105.87 ? 197 ARG   F NH2    1 
ATOM   15794 N  N      . LYS   F 4  198 ? 0.799   -44.138  -107.362 1.00 98.97  ? 198 LYS   F N      1 
ATOM   15795 C  CA     . LYS   F 4  198 ? 1.206   -45.340  -106.653 1.00 92.36  ? 198 LYS   F CA     1 
ATOM   15796 C  C      . LYS   F 4  198 ? 0.609   -45.369  -105.244 1.00 98.31  ? 198 LYS   F C      1 
ATOM   15797 O  O      . LYS   F 4  198 ? 0.059   -44.380  -104.749 1.00 96.90  ? 198 LYS   F O      1 
ATOM   15798 C  CB     . LYS   F 4  198 ? 2.730   -45.411  -106.588 1.00 88.29  ? 198 LYS   F CB     1 
ATOM   15799 C  CG     . LYS   F 4  198 ? 3.301   -46.803  -106.488 1.00 91.94  ? 198 LYS   F CG     1 
ATOM   15800 C  CD     . LYS   F 4  198 ? 4.815   -46.750  -106.368 1.00 97.55  ? 198 LYS   F CD     1 
ATOM   15801 C  CE     . LYS   F 4  198 ? 5.494   -47.729  -107.310 1.00 94.69  ? 198 LYS   F CE     1 
ATOM   15802 N  NZ     . LYS   F 4  198 ? 5.282   -49.136  -106.893 1.00 91.26  ? 198 LYS   F NZ     1 
ATOM   15803 N  N      . PHE   F 4  199 ? 0.720   -46.529  -104.593 1.00 100.63 ? 199 PHE   F N      1 
ATOM   15804 C  CA     . PHE   F 4  199 ? 0.337   -46.686  -103.190 1.00 96.28  ? 199 PHE   F CA     1 
ATOM   15805 C  C      . PHE   F 4  199 ? 0.886   -48.016  -102.676 1.00 91.37  ? 199 PHE   F C      1 
ATOM   15806 O  O      . PHE   F 4  199 ? 1.298   -48.883  -103.453 1.00 83.57  ? 199 PHE   F O      1 
ATOM   15807 C  CB     . PHE   F 4  199 ? -1.185  -46.615  -103.009 1.00 88.17  ? 199 PHE   F CB     1 
ATOM   15808 C  CG     . PHE   F 4  199 ? -1.894  -47.882  -103.394 1.00 92.76  ? 199 PHE   F CG     1 
ATOM   15809 C  CD1    . PHE   F 4  199 ? -2.562  -47.976  -104.601 1.00 96.10  ? 199 PHE   F CD1    1 
ATOM   15810 C  CD2    . PHE   F 4  199 ? -1.902  -48.976  -102.550 1.00 84.77  ? 199 PHE   F CD2    1 
ATOM   15811 C  CE1    . PHE   F 4  199 ? -3.215  -49.136  -104.958 1.00 90.60  ? 199 PHE   F CE1    1 
ATOM   15812 C  CE2    . PHE   F 4  199 ? -2.544  -50.135  -102.905 1.00 80.00  ? 199 PHE   F CE2    1 
ATOM   15813 C  CZ     . PHE   F 4  199 ? -3.203  -50.217  -104.105 1.00 83.17  ? 199 PHE   F CZ     1 
ATOM   15814 N  N      . ASP   F 4  200 ? 0.879   -48.162  -101.346 1.00 92.67  ? 200 ASP   F N      1 
ATOM   15815 C  CA     . ASP   F 4  200 ? 1.050   -49.449  -100.677 1.00 84.17  ? 200 ASP   F CA     1 
ATOM   15816 C  C      . ASP   F 4  200 ? -0.035  -49.610  -99.617  1.00 80.12  ? 200 ASP   F C      1 
ATOM   15817 O  O      . ASP   F 4  200 ? -0.656  -48.635  -99.178  1.00 80.36  ? 200 ASP   F O      1 
ATOM   15818 C  CB     . ASP   F 4  200 ? 2.461   -49.630  -100.048 1.00 84.95  ? 200 ASP   F CB     1 
ATOM   15819 C  CG     . ASP   F 4  200 ? 2.812   -48.567  -99.001  1.00 86.57  ? 200 ASP   F CG     1 
ATOM   15820 O  OD1    . ASP   F 4  200 ? 2.026   -48.324  -98.060  1.00 83.85  ? 200 ASP   F OD1    1 
ATOM   15821 O  OD2    . ASP   F 4  200 ? 3.920   -48.002  -99.098  1.00 91.57  ? 200 ASP   F OD2    1 
ATOM   15822 N  N      . ILE   F 4  201 ? -0.279  -50.865  -99.228  1.00 77.39  ? 201 ILE   F N      1 
ATOM   15823 C  CA     . ILE   F 4  201 ? -1.258  -51.204  -98.194  1.00 78.92  ? 201 ILE   F CA     1 
ATOM   15824 C  C      . ILE   F 4  201 ? -0.509  -51.682  -96.955  1.00 73.26  ? 201 ILE   F C      1 
ATOM   15825 O  O      . ILE   F 4  201 ? 0.353   -52.567  -97.048  1.00 70.39  ? 201 ILE   F O      1 
ATOM   15826 C  CB     . ILE   F 4  201 ? -2.265  -52.273  -98.672  1.00 72.55  ? 201 ILE   F CB     1 
ATOM   15827 C  CG1    . ILE   F 4  201 ? -2.622  -52.081  -100.152 1.00 72.74  ? 201 ILE   F CG1    1 
ATOM   15828 C  CG2    . ILE   F 4  201 ? -3.529  -52.239  -97.807  1.00 69.67  ? 201 ILE   F CG2    1 
ATOM   15829 C  CD1    . ILE   F 4  201 ? -3.765  -52.958  -100.655 1.00 64.24  ? 201 ILE   F CD1    1 
ATOM   15830 N  N      . ARG   F 4  202 ? -0.826  -51.084  -95.800  1.00 69.67  ? 202 ARG   F N      1 
ATOM   15831 C  CA     . ARG   F 4  202 ? -0.376  -51.580  -94.504  1.00 68.57  ? 202 ARG   F CA     1 
ATOM   15832 C  C      . ARG   F 4  202 ? -1.564  -52.171  -93.770  1.00 68.52  ? 202 ARG   F C      1 
ATOM   15833 O  O      . ARG   F 4  202 ? -2.515  -51.451  -93.444  1.00 65.56  ? 202 ARG   F O      1 
ATOM   15834 C  CB     . ARG   F 4  202 ? 0.256   -50.501  -93.624  1.00 69.58  ? 202 ARG   F CB     1 
ATOM   15835 C  CG     . ARG   F 4  202 ? 0.073   -50.842  -92.124  1.00 67.24  ? 202 ARG   F CG     1 
ATOM   15836 C  CD     . ARG   F 4  202 ? 1.236   -50.435  -91.248  1.00 66.03  ? 202 ARG   F CD     1 
ATOM   15837 N  NE     . ARG   F 4  202 ? 2.512   -50.890  -91.788  1.00 69.44  ? 202 ARG   F NE     1 
ATOM   15838 C  CZ     . ARG   F 4  202 ? 3.685   -50.367  -91.452  1.00 72.78  ? 202 ARG   F CZ     1 
ATOM   15839 N  NH1    . ARG   F 4  202 ? 3.777   -49.412  -90.539  1.00 71.49  ? 202 ARG   F NH1    1 
ATOM   15840 N  NH2    . ARG   F 4  202 ? 4.790   -50.806  -92.054  1.00 72.89  ? 202 ARG   F NH2    1 
ATOM   15841 N  N      . SER   F 4  203 ? -1.499  -53.471  -93.501  1.00 69.50  ? 203 SER   F N      1 
ATOM   15842 C  CA     . SER   F 4  203 ? -2.428  -54.140  -92.607  1.00 63.29  ? 203 SER   F CA     1 
ATOM   15843 C  C      . SER   F 4  203 ? -1.724  -54.395  -91.282  1.00 63.93  ? 203 SER   F C      1 
ATOM   15844 O  O      . SER   F 4  203 ? -0.544  -54.768  -91.252  1.00 62.93  ? 203 SER   F O      1 
ATOM   15845 C  CB     . SER   F 4  203 ? -2.927  -55.459  -93.208  1.00 64.82  ? 203 SER   F CB     1 
ATOM   15846 O  OG     . SER   F 4  203 ? -3.495  -55.300  -94.501  1.00 55.68  ? 203 SER   F OG     1 
ATOM   15847 N  N      . TRP   F 4  204 ? -2.436  -54.161  -90.190  1.00 58.40  ? 204 TRP   F N      1 
ATOM   15848 C  CA     . TRP   F 4  204 ? -1.902  -54.394  -88.860  1.00 56.99  ? 204 TRP   F CA     1 
ATOM   15849 C  C      . TRP   F 4  204 ? -2.379  -55.763  -88.383  1.00 59.07  ? 204 TRP   F C      1 
ATOM   15850 O  O      . TRP   F 4  204 ? -3.582  -56.053  -88.387  1.00 56.49  ? 204 TRP   F O      1 
ATOM   15851 C  CB     . TRP   F 4  204 ? -2.312  -53.263  -87.906  1.00 66.22  ? 204 TRP   F CB     1 
ATOM   15852 C  CG     . TRP   F 4  204 ? -1.579  -51.974  -88.229  1.00 65.13  ? 204 TRP   F CG     1 
ATOM   15853 C  CD1    . TRP   F 4  204 ? -0.286  -51.674  -87.922  1.00 67.91  ? 204 TRP   F CD1    1 
ATOM   15854 C  CD2    . TRP   F 4  204 ? -2.079  -50.856  -88.973  1.00 66.94  ? 204 TRP   F CD2    1 
ATOM   15855 N  NE1    . TRP   F 4  204 ? 0.048   -50.437  -88.414  1.00 72.15  ? 204 TRP   F NE1    1 
ATOM   15856 C  CE2    . TRP   F 4  204 ? -1.037  -49.913  -89.063  1.00 72.20  ? 204 TRP   F CE2    1 
ATOM   15857 C  CE3    . TRP   F 4  204 ? -3.306  -50.558  -89.567  1.00 67.10  ? 204 TRP   F CE3    1 
ATOM   15858 C  CZ2    . TRP   F 4  204 ? -1.184  -48.696  -89.722  1.00 73.73  ? 204 TRP   F CZ2    1 
ATOM   15859 C  CZ3    . TRP   F 4  204 ? -3.450  -49.347  -90.217  1.00 71.93  ? 204 TRP   F CZ3    1 
ATOM   15860 C  CH2    . TRP   F 4  204 ? -2.397  -48.430  -90.287  1.00 73.42  ? 204 TRP   F CH2    1 
ATOM   15861 N  N      . VAL   F 4  205 ? -1.438  -56.615  -88.005  1.00 59.69  ? 205 VAL   F N      1 
ATOM   15862 C  CA     . VAL   F 4  205 ? -1.741  -57.984  -87.612  1.00 60.15  ? 205 VAL   F CA     1 
ATOM   15863 C  C      . VAL   F 4  205 ? -1.246  -58.185  -86.188  1.00 56.34  ? 205 VAL   F C      1 
ATOM   15864 O  O      . VAL   F 4  205 ? -0.141  -57.752  -85.849  1.00 58.48  ? 205 VAL   F O      1 
ATOM   15865 C  CB     . VAL   F 4  205 ? -1.107  -58.991  -88.591  1.00 58.61  ? 205 VAL   F CB     1 
ATOM   15866 C  CG1    . VAL   F 4  205 ? -1.139  -60.407  -88.029  1.00 58.87  ? 205 VAL   F CG1    1 
ATOM   15867 C  CG2    . VAL   F 4  205 ? -1.838  -58.933  -89.935  1.00 55.35  ? 205 VAL   F CG2    1 
ATOM   15868 N  N      . LEU   F 4  206 ? -2.067  -58.819  -85.353  1.00 53.77  ? 206 LEU   F N      1 
ATOM   15869 C  CA     . LEU   F 4  206 ? -1.730  -59.099  -83.961  1.00 55.76  ? 206 LEU   F CA     1 
ATOM   15870 C  C      . LEU   F 4  206 ? -1.721  -60.606  -83.723  1.00 56.34  ? 206 LEU   F C      1 
ATOM   15871 O  O      . LEU   F 4  206 ? -2.714  -61.288  -83.994  1.00 56.70  ? 206 LEU   F O      1 
ATOM   15872 C  CB     . LEU   F 4  206 ? -2.725  -58.422  -83.003  1.00 59.24  ? 206 LEU   F CB     1 
ATOM   15873 C  CG     . LEU   F 4  206 ? -2.505  -58.601  -81.493  1.00 59.88  ? 206 LEU   F CG     1 
ATOM   15874 C  CD1    . LEU   F 4  206 ? -1.290  -57.812  -81.012  1.00 60.05  ? 206 LEU   F CD1    1 
ATOM   15875 C  CD2    . LEU   F 4  206 ? -3.748  -58.210  -80.692  1.00 63.42  ? 206 LEU   F CD2    1 
ATOM   15876 N  N      . VAL   F 4  207 ? -0.607  -61.122  -83.212  1.00 56.31  ? 207 VAL   F N      1 
ATOM   15877 C  CA     . VAL   F 4  207 ? -0.483  -62.522  -82.813  1.00 52.17  ? 207 VAL   F CA     1 
ATOM   15878 C  C      . VAL   F 4  207 ? -0.490  -62.568  -81.288  1.00 51.45  ? 207 VAL   F C      1 
ATOM   15879 O  O      . VAL   F 4  207 ? 0.336   -61.908  -80.645  1.00 50.04  ? 207 VAL   F O      1 
ATOM   15880 C  CB     . VAL   F 4  207 ? 0.798   -63.165  -83.371  1.00 46.45  ? 207 VAL   F CB     1 
ATOM   15881 C  CG1    . VAL   F 4  207 ? 0.714   -64.666  -83.241  1.00 49.77  ? 207 VAL   F CG1    1 
ATOM   15882 C  CG2    . VAL   F 4  207 ? 1.019   -62.785  -84.804  1.00 44.11  ? 207 VAL   F CG2    1 
ATOM   15883 N  N      . ASP   F 4  208 ? -1.405  -63.349  -80.710  1.00 46.53  ? 208 ASP   F N      1 
ATOM   15884 C  CA     . ASP   F 4  208 ? -1.531  -63.425  -79.263  1.00 51.20  ? 208 ASP   F CA     1 
ATOM   15885 C  C      . ASP   F 4  208 ? -0.719  -64.599  -78.701  1.00 53.05  ? 208 ASP   F C      1 
ATOM   15886 O  O      . ASP   F 4  208 ? -0.039  -65.334  -79.421  1.00 45.93  ? 208 ASP   F O      1 
ATOM   15887 C  CB     . ASP   F 4  208 ? -3.010  -63.485  -78.850  1.00 55.29  ? 208 ASP   F CB     1 
ATOM   15888 C  CG     . ASP   F 4  208 ? -3.743  -64.746  -79.340  1.00 56.49  ? 208 ASP   F CG     1 
ATOM   15889 O  OD1    . ASP   F 4  208 ? -3.091  -65.689  -79.798  1.00 52.93  ? 208 ASP   F OD1    1 
ATOM   15890 O  OD2    . ASP   F 4  208 ? -5.000  -64.791  -79.268  1.00 64.43  ? 208 ASP   F OD2    1 
ATOM   15891 N  N      . HIS   F 4  209 ? -0.762  -64.752  -77.377  1.00 56.95  ? 209 HIS   F N      1 
ATOM   15892 C  CA     . HIS   F 4  209 ? 0.037   -65.788  -76.729  1.00 56.08  ? 209 HIS   F CA     1 
ATOM   15893 C  C      . HIS   F 4  209 ? -0.362  -67.184  -77.185  1.00 55.60  ? 209 HIS   F C      1 
ATOM   15894 O  O      . HIS   F 4  209 ? 0.439   -68.119  -77.077  1.00 58.50  ? 209 HIS   F O      1 
ATOM   15895 C  CB     . HIS   F 4  209 ? -0.113  -65.687  -75.215  1.00 53.39  ? 209 HIS   F CB     1 
ATOM   15896 C  CG     . HIS   F 4  209 ? -1.507  -65.939  -74.747  1.00 54.69  ? 209 HIS   F CG     1 
ATOM   15897 N  ND1    . HIS   F 4  209 ? -2.488  -64.973  -74.786  1.00 60.25  ? 209 HIS   F ND1    1 
ATOM   15898 C  CD2    . HIS   F 4  209 ? -2.100  -67.061  -74.282  1.00 53.54  ? 209 HIS   F CD2    1 
ATOM   15899 C  CE1    . HIS   F 4  209 ? -3.619  -65.481  -74.333  1.00 58.20  ? 209 HIS   F CE1    1 
ATOM   15900 N  NE2    . HIS   F 4  209 ? -3.411  -66.747  -74.024  1.00 59.47  ? 209 HIS   F NE2    1 
ATOM   15901 N  N      . LEU   F 4  210 ? -1.598  -67.352  -77.654  1.00 53.00  ? 210 LEU   F N      1 
ATOM   15902 C  CA     . LEU   F 4  210 ? -2.098  -68.629  -78.152  1.00 56.30  ? 210 LEU   F CA     1 
ATOM   15903 C  C      . LEU   F 4  210 ? -1.767  -68.860  -79.622  1.00 56.79  ? 210 LEU   F C      1 
ATOM   15904 O  O      . LEU   F 4  210 ? -2.063  -69.935  -80.151  1.00 57.14  ? 210 LEU   F O      1 
ATOM   15905 C  CB     . LEU   F 4  210 ? -3.616  -68.708  -77.959  1.00 61.45  ? 210 LEU   F CB     1 
ATOM   15906 C  CG     . LEU   F 4  210 ? -4.152  -68.547  -76.541  1.00 53.69  ? 210 LEU   F CG     1 
ATOM   15907 C  CD1    . LEU   F 4  210 ? -5.640  -68.724  -76.539  1.00 52.66  ? 210 LEU   F CD1    1 
ATOM   15908 C  CD2    . LEU   F 4  210 ? -3.508  -69.590  -75.705  1.00 52.35  ? 210 LEU   F CD2    1 
ATOM   15909 N  N      . TYR   F 4  211 ? -1.152  -67.876  -80.276  1.00 56.51  ? 211 TYR   F N      1 
ATOM   15910 C  CA     . TYR   F 4  211 ? -0.835  -67.852  -81.705  1.00 51.71  ? 211 TYR   F CA     1 
ATOM   15911 C  C      . TYR   F 4  211 ? -2.071  -67.786  -82.602  1.00 55.12  ? 211 TYR   F C      1 
ATOM   15912 O  O      . TYR   F 4  211 ? -1.991  -68.111  -83.799  1.00 52.36  ? 211 TYR   F O      1 
ATOM   15913 C  CB     . TYR   F 4  211 ? 0.057   -69.018  -82.119  1.00 46.12  ? 211 TYR   F CB     1 
ATOM   15914 C  CG     . TYR   F 4  211 ? 1.098   -68.577  -83.127  1.00 48.04  ? 211 TYR   F CG     1 
ATOM   15915 C  CD1    . TYR   F 4  211 ? 2.319   -68.040  -82.711  1.00 48.34  ? 211 TYR   F CD1    1 
ATOM   15916 C  CD2    . TYR   F 4  211 ? 0.859   -68.674  -84.494  1.00 50.17  ? 211 TYR   F CD2    1 
ATOM   15917 C  CE1    . TYR   F 4  211 ? 3.274   -67.627  -83.629  1.00 47.82  ? 211 TYR   F CE1    1 
ATOM   15918 C  CE2    . TYR   F 4  211 ? 1.811   -68.269  -85.418  1.00 50.85  ? 211 TYR   F CE2    1 
ATOM   15919 C  CZ     . TYR   F 4  211 ? 3.014   -67.747  -84.978  1.00 48.99  ? 211 TYR   F CZ     1 
ATOM   15920 O  OH     . TYR   F 4  211 ? 3.953   -67.338  -85.890  1.00 49.56  ? 211 TYR   F OH     1 
ATOM   15921 N  N      . ASN   F 4  212 ? -3.211  -67.354  -82.066  1.00 49.89  ? 212 ASN   F N      1 
ATOM   15922 C  CA     . ASN   F 4  212 ? -4.237  -66.802  -82.934  1.00 57.11  ? 212 ASN   F CA     1 
ATOM   15923 C  C      . ASN   F 4  212 ? -3.637  -65.645  -83.745  1.00 53.82  ? 212 ASN   F C      1 
ATOM   15924 O  O      . ASN   F 4  212 ? -2.783  -64.902  -83.259  1.00 53.50  ? 212 ASN   F O      1 
ATOM   15925 C  CB     . ASN   F 4  212 ? -5.435  -66.343  -82.101  1.00 59.31  ? 212 ASN   F CB     1 
ATOM   15926 C  CG     . ASN   F 4  212 ? -6.129  -67.501  -81.408  1.00 65.95  ? 212 ASN   F CG     1 
ATOM   15927 O  OD1    . ASN   F 4  212 ? -6.331  -68.543  -82.016  1.00 66.32  ? 212 ASN   F OD1    1 
ATOM   15928 N  ND2    . ASN   F 4  212 ? -6.505  -67.322  -80.135  1.00 67.88  ? 212 ASN   F ND2    1 
ATOM   15929 N  N      . ILE   F 4  213 ? -4.037  -65.531  -85.009  1.00 53.69  ? 213 ILE   F N      1 
ATOM   15930 C  CA     . ILE   F 4  213 ? -3.578  -64.470  -85.901  1.00 50.56  ? 213 ILE   F CA     1 
ATOM   15931 C  C      . ILE   F 4  213 ? -4.751  -63.531  -86.147  1.00 56.10  ? 213 ILE   F C      1 
ATOM   15932 O  O      . ILE   F 4  213 ? -5.788  -63.953  -86.671  1.00 59.55  ? 213 ILE   F O      1 
ATOM   15933 C  CB     . ILE   F 4  213 ? -3.034  -65.034  -87.220  1.00 48.72  ? 213 ILE   F CB     1 
ATOM   15934 C  CG1    . ILE   F 4  213 ? -1.707  -65.735  -86.980  1.00 46.45  ? 213 ILE   F CG1    1 
ATOM   15935 C  CG2    . ILE   F 4  213 ? -2.875  -63.937  -88.253  1.00 51.67  ? 213 ILE   F CG2    1 
ATOM   15936 C  CD1    . ILE   F 4  213 ? -1.404  -66.801  -87.992  1.00 54.19  ? 213 ILE   F CD1    1 
ATOM   15937 N  N      . TYR   F 4  214 ? -4.606  -62.269  -85.746  1.00 57.01  ? 214 TYR   F N      1 
ATOM   15938 C  CA     . TYR   F 4  214 ? -5.698  -61.300  -85.781  1.00 57.83  ? 214 TYR   F CA     1 
ATOM   15939 C  C      . TYR   F 4  214 ? -5.336  -60.185  -86.752  1.00 61.55  ? 214 TYR   F C      1 
ATOM   15940 O  O      . TYR   F 4  214 ? -4.369  -59.446  -86.525  1.00 60.36  ? 214 TYR   F O      1 
ATOM   15941 C  CB     . TYR   F 4  214 ? -5.983  -60.722  -84.392  1.00 57.43  ? 214 TYR   F CB     1 
ATOM   15942 C  CG     . TYR   F 4  214 ? -6.616  -61.676  -83.392  1.00 60.23  ? 214 TYR   F CG     1 
ATOM   15943 C  CD1    . TYR   F 4  214 ? -7.977  -61.944  -83.403  1.00 61.84  ? 214 TYR   F CD1    1 
ATOM   15944 C  CD2    . TYR   F 4  214 ? -5.844  -62.293  -82.414  1.00 67.09  ? 214 TYR   F CD2    1 
ATOM   15945 C  CE1    . TYR   F 4  214 ? -8.550  -62.814  -82.466  1.00 59.88  ? 214 TYR   F CE1    1 
ATOM   15946 C  CE2    . TYR   F 4  214 ? -6.406  -63.165  -81.484  1.00 68.10  ? 214 TYR   F CE2    1 
ATOM   15947 C  CZ     . TYR   F 4  214 ? -7.758  -63.417  -81.516  1.00 66.38  ? 214 TYR   F CZ     1 
ATOM   15948 O  OH     . TYR   F 4  214 ? -8.297  -64.280  -80.593  1.00 73.10  ? 214 TYR   F OH     1 
ATOM   15949 N  N      . LEU   F 4  215 ? -6.105  -60.079  -87.833  1.00 63.51  ? 215 LEU   F N      1 
ATOM   15950 C  CA     . LEU   F 4  215 ? -5.994  -58.986  -88.784  1.00 59.69  ? 215 LEU   F CA     1 
ATOM   15951 C  C      . LEU   F 4  215 ? -6.933  -57.864  -88.361  1.00 62.35  ? 215 LEU   F C      1 
ATOM   15952 O  O      . LEU   F 4  215 ? -8.105  -58.110  -88.050  1.00 64.33  ? 215 LEU   F O      1 
ATOM   15953 C  CB     . LEU   F 4  215 ? -6.340  -59.471  -90.188  1.00 55.86  ? 215 LEU   F CB     1 
ATOM   15954 C  CG     . LEU   F 4  215 ? -6.308  -58.431  -91.301  1.00 57.48  ? 215 LEU   F CG     1 
ATOM   15955 C  CD1    . LEU   F 4  215 ? -4.888  -57.961  -91.515  1.00 61.54  ? 215 LEU   F CD1    1 
ATOM   15956 C  CD2    . LEU   F 4  215 ? -6.852  -59.044  -92.565  1.00 50.67  ? 215 LEU   F CD2    1 
ATOM   15957 N  N      . TYR   F 4  216 ? -6.410  -56.642  -88.319  1.00 60.99  ? 216 TYR   F N      1 
ATOM   15958 C  CA     . TYR   F 4  216 ? -7.229  -55.482  -87.995  1.00 66.24  ? 216 TYR   F CA     1 
ATOM   15959 C  C      . TYR   F 4  216 ? -8.069  -55.104  -89.212  1.00 69.40  ? 216 TYR   F C      1 
ATOM   15960 O  O      . TYR   F 4  216 ? -7.588  -55.134  -90.351  1.00 65.70  ? 216 TYR   F O      1 
ATOM   15961 C  CB     . TYR   F 4  216 ? -6.333  -54.318  -87.546  1.00 68.03  ? 216 TYR   F CB     1 
ATOM   15962 C  CG     . TYR   F 4  216 ? -7.032  -53.010  -87.176  1.00 70.81  ? 216 TYR   F CG     1 
ATOM   15963 C  CD1    . TYR   F 4  216 ? -8.264  -52.994  -86.521  1.00 67.81  ? 216 TYR   F CD1    1 
ATOM   15964 C  CD2    . TYR   F 4  216 ? -6.446  -51.787  -87.495  1.00 69.05  ? 216 TYR   F CD2    1 
ATOM   15965 C  CE1    . TYR   F 4  216 ? -8.888  -51.789  -86.195  1.00 70.06  ? 216 TYR   F CE1    1 
ATOM   15966 C  CE2    . TYR   F 4  216 ? -7.060  -50.588  -87.179  1.00 70.27  ? 216 TYR   F CE2    1 
ATOM   15967 C  CZ     . TYR   F 4  216 ? -8.279  -50.583  -86.532  1.00 71.54  ? 216 TYR   F CZ     1 
ATOM   15968 O  OH     . TYR   F 4  216 ? -8.872  -49.365  -86.232  1.00 65.21  ? 216 TYR   F OH     1 
ATOM   15969 N  N      . ARG   F 4  217 ? -9.344  -54.784  -88.970  1.00 67.81  ? 217 ARG   F N      1 
ATOM   15970 C  CA     . ARG   F 4  217 ? -10.252 -54.507  -90.079  1.00 68.21  ? 217 ARG   F CA     1 
ATOM   15971 C  C      . ARG   F 4  217 ? -9.861  -53.227  -90.814  1.00 74.33  ? 217 ARG   F C      1 
ATOM   15972 O  O      . ARG   F 4  217 ? -9.913  -53.176  -92.052  1.00 78.26  ? 217 ARG   F O      1 
ATOM   15973 C  CB     . ARG   F 4  217 ? -11.688 -54.451  -89.570  1.00 66.20  ? 217 ARG   F CB     1 
ATOM   15974 C  CG     . ARG   F 4  217 ? -12.115 -55.807  -89.034  1.00 74.76  ? 217 ARG   F CG     1 
ATOM   15975 C  CD     . ARG   F 4  217 ? -13.613 -56.053  -89.064  1.00 79.74  ? 217 ARG   F CD     1 
ATOM   15976 N  NE     . ARG   F 4  217 ? -13.902 -57.484  -89.154  1.00 80.90  ? 217 ARG   F NE     1 
ATOM   15977 C  CZ     . ARG   F 4  217 ? -14.505 -58.195  -88.208  1.00 86.80  ? 217 ARG   F CZ     1 
ATOM   15978 N  NH1    . ARG   F 4  217 ? -14.893 -57.643  -87.066  1.00 89.32  ? 217 ARG   F NH1    1 
ATOM   15979 N  NH2    . ARG   F 4  217 ? -14.726 -59.495  -88.412  1.00 81.94  ? 217 ARG   F NH2    1 
ATOM   15980 N  N      . GLU   F 4  218 ? -9.431  -52.199  -90.082  1.00 69.90  ? 218 GLU   F N      1 
ATOM   15981 C  CA     . GLU   F 4  218 ? -8.943  -50.979  -90.719  1.00 71.94  ? 218 GLU   F CA     1 
ATOM   15982 C  C      . GLU   F 4  218 ? -7.555  -51.217  -91.307  1.00 68.77  ? 218 GLU   F C      1 
ATOM   15983 O  O      . GLU   F 4  218 ? -6.618  -51.589  -90.592  1.00 70.33  ? 218 GLU   F O      1 
ATOM   15984 C  CB     . GLU   F 4  218 ? -8.903  -49.823  -89.717  1.00 70.17  ? 218 GLU   F CB     1 
ATOM   15985 C  CG     . GLU   F 4  218 ? -10.227 -49.474  -89.059  1.00 67.21  ? 218 GLU   F CG     1 
ATOM   15986 C  CD     . GLU   F 4  218 ? -11.398 -49.514  -90.026  1.00 74.34  ? 218 GLU   F CD     1 
ATOM   15987 O  OE1    . GLU   F 4  218 ? -11.177 -49.279  -91.241  1.00 71.07  ? 218 GLU   F OE1    1 
ATOM   15988 O  OE2    . GLU   F 4  218 ? -12.536 -49.792  -89.566  1.00 70.61  ? 218 GLU   F OE2    1 
ATOM   15989 N  N      . GLY   F 4  219 ? -7.424  -51.021  -92.614  1.00 63.13  ? 219 GLY   F N      1 
ATOM   15990 C  CA     . GLY   F 4  219 ? -6.135  -50.919  -93.249  1.00 65.77  ? 219 GLY   F CA     1 
ATOM   15991 C  C      . GLY   F 4  219 ? -5.875  -49.488  -93.667  1.00 75.17  ? 219 GLY   F C      1 
ATOM   15992 O  O      . GLY   F 4  219 ? -6.669  -48.584  -93.397  1.00 79.16  ? 219 GLY   F O      1 
ATOM   15993 N  N      . VAL   F 4  220 ? -4.748  -49.291  -94.347  1.00 72.99  ? 220 VAL   F N      1 
ATOM   15994 C  CA     . VAL   F 4  220 ? -4.419  -47.961  -94.844  1.00 79.47  ? 220 VAL   F CA     1 
ATOM   15995 C  C      . VAL   F 4  220 ? -3.616  -48.068  -96.132  1.00 82.06  ? 220 VAL   F C      1 
ATOM   15996 O  O      . VAL   F 4  220 ? -2.712  -48.898  -96.259  1.00 78.03  ? 220 VAL   F O      1 
ATOM   15997 C  CB     . VAL   F 4  220 ? -3.656  -47.126  -93.799  1.00 83.69  ? 220 VAL   F CB     1 
ATOM   15998 C  CG1    . VAL   F 4  220 ? -2.152  -47.413  -93.880  1.00 73.55  ? 220 VAL   F CG1    1 
ATOM   15999 C  CG2    . VAL   F 4  220 ? -3.955  -45.647  -94.021  1.00 85.53  ? 220 VAL   F CG2    1 
ATOM   16000 N  N      . LEU   F 4  221 ? -3.956  -47.199  -97.084  1.00 87.67  ? 221 LEU   F N      1 
ATOM   16001 C  CA     . LEU   F 4  221 ? -3.199  -47.018  -98.315  1.00 86.84  ? 221 LEU   F CA     1 
ATOM   16002 C  C      . LEU   F 4  221 ? -2.363  -45.755  -98.179  1.00 89.44  ? 221 LEU   F C      1 
ATOM   16003 O  O      . LEU   F 4  221 ? -2.909  -44.659  -98.021  1.00 93.11  ? 221 LEU   F O      1 
ATOM   16004 C  CB     . LEU   F 4  221 ? -4.130  -46.902  -99.518  1.00 86.49  ? 221 LEU   F CB     1 
ATOM   16005 C  CG     . LEU   F 4  221 ? -4.620  -48.182  -100.172 1.00 83.44  ? 221 LEU   F CG     1 
ATOM   16006 C  CD1    . LEU   F 4  221 ? -5.986  -48.497  -99.624  1.00 83.53  ? 221 LEU   F CD1    1 
ATOM   16007 C  CD2    . LEU   F 4  221 ? -4.685  -48.003  -101.680 1.00 84.31  ? 221 LEU   F CD2    1 
ATOM   16008 N  N      . ARG   F 4  222 ? -1.047  -45.908  -98.233  1.00 92.05  ? 222 ARG   F N      1 
ATOM   16009 C  CA     . ARG   F 4  222 ? -0.132  -44.770  -98.222  1.00 97.31  ? 222 ARG   F CA     1 
ATOM   16010 C  C      . ARG   F 4  222 ? 0.127   -44.418  -99.685  1.00 100.63 ? 222 ARG   F C      1 
ATOM   16011 O  O      . ARG   F 4  222 ? 0.853   -45.126  -100.391 1.00 97.46  ? 222 ARG   F O      1 
ATOM   16012 C  CB     . ARG   F 4  222 ? 1.141   -45.112  -97.449  1.00 95.79  ? 222 ARG   F CB     1 
ATOM   16013 C  CG     . ARG   F 4  222 ? 0.877   -46.000  -96.239  1.00 87.89  ? 222 ARG   F CG     1 
ATOM   16014 C  CD     . ARG   F 4  222 ? 2.100   -46.251  -95.397  1.00 89.05  ? 222 ARG   F CD     1 
ATOM   16015 N  NE     . ARG   F 4  222 ? 2.500   -47.646  -95.505  1.00 79.93  ? 222 ARG   F NE     1 
ATOM   16016 C  CZ     . ARG   F 4  222 ? 3.683   -48.117  -95.142  1.00 84.24  ? 222 ARG   F CZ     1 
ATOM   16017 N  NH1    . ARG   F 4  222 ? 4.547   -47.376  -94.464  1.00 87.83  ? 222 ARG   F NH1    1 
ATOM   16018 N  NH2    . ARG   F 4  222 ? 4.014   -49.359  -95.478  1.00 86.86  ? 222 ARG   F NH2    1 
ATOM   16019 N  N      . THR   F 4  223 ? -0.490  -43.331  -100.145 1.00 103.79 ? 223 THR   F N      1 
ATOM   16020 C  CA     . THR   F 4  223 ? -0.596  -43.009  -101.562 1.00 104.18 ? 223 THR   F CA     1 
ATOM   16021 C  C      . THR   F 4  223 ? 0.361   -41.890  -101.955 1.00 106.78 ? 223 THR   F C      1 
ATOM   16022 O  O      . THR   F 4  223 ? 0.486   -40.883  -101.250 1.00 106.66 ? 223 THR   F O      1 
ATOM   16023 C  CB     . THR   F 4  223 ? -2.029  -42.596  -101.902 1.00 104.41 ? 223 THR   F CB     1 
ATOM   16024 O  OG1    . THR   F 4  223 ? -2.178  -41.185  -101.698 1.00 107.90 ? 223 THR   F OG1    1 
ATOM   16025 C  CG2    . THR   F 4  223 ? -3.022  -43.332  -101.007 1.00 97.99  ? 223 THR   F CG2    1 
ATOM   16026 N  N      . SER   F 4  224 ? 1.033   -42.073  -103.090 1.00 110.24 ? 224 SER   F N      1 
ATOM   16027 C  CA     . SER   F 4  224 ? 1.813   -41.002  -103.695 1.00 114.47 ? 224 SER   F CA     1 
ATOM   16028 C  C      . SER   F 4  224 ? 0.882   -40.040  -104.430 1.00 114.78 ? 224 SER   F C      1 
ATOM   16029 O  O      . SER   F 4  224 ? -0.077  -40.463  -105.088 1.00 110.03 ? 224 SER   F O      1 
ATOM   16030 C  CB     . SER   F 4  224 ? 2.864   -41.584  -104.647 1.00 108.69 ? 224 SER   F CB     1 
ATOM   16031 O  OG     . SER   F 4  224 ? 3.134   -40.735  -105.745 1.00 107.73 ? 224 SER   F OG     1 
ATOM   16032 N  N      . SER   F 4  225 ? 1.142   -38.737  -104.279 1.00 117.44 ? 225 SER   F N      1 
ATOM   16033 C  CA     . SER   F 4  225 ? 0.396   -37.693  -104.975 1.00 114.81 ? 225 SER   F CA     1 
ATOM   16034 C  C      . SER   F 4  225 ? 1.019   -37.329  -106.316 1.00 113.19 ? 225 SER   F C      1 
ATOM   16035 O  O      . SER   F 4  225 ? 0.690   -36.281  -106.881 1.00 116.68 ? 225 SER   F O      1 
ATOM   16036 C  CB     . SER   F 4  225 ? 0.290   -36.440  -104.100 1.00 110.33 ? 225 SER   F CB     1 
ATOM   16037 O  OG     . SER   F 4  225 ? 0.184   -36.782  -102.730 1.00 106.01 ? 225 SER   F OG     1 
ATOM   16038 N  N      . GLU   F 4  226 ? 1.905   -38.171  -106.839 1.00 109.72 ? 226 GLU   F N      1 
ATOM   16039 C  CA     . GLU   F 4  226 ? 2.757   -37.803  -107.962 1.00 113.92 ? 226 GLU   F CA     1 
ATOM   16040 C  C      . GLU   F 4  226 ? 2.615   -38.840  -109.071 1.00 113.99 ? 226 GLU   F C      1 
ATOM   16041 O  O      . GLU   F 4  226 ? 2.970   -40.017  -108.862 1.00 112.31 ? 226 GLU   F O      1 
ATOM   16042 C  CB     . GLU   F 4  226 ? 4.210   -37.673  -107.488 1.00 118.37 ? 226 GLU   F CB     1 
ATOM   16043 C  CG     . GLU   F 4  226 ? 4.390   -36.925  -106.145 1.00 118.69 ? 226 GLU   F CG     1 
ATOM   16044 C  CD     . GLU   F 4  226 ? 3.756   -35.526  -106.118 1.00 119.86 ? 226 GLU   F CD     1 
ATOM   16045 O  OE1    . GLU   F 4  226 ? 3.143   -35.151  -105.088 1.00 114.23 ? 226 GLU   F OE1    1 
ATOM   16046 O  OE2    . GLU   F 4  226 ? 3.876   -34.793  -107.121 1.00 121.51 ? 226 GLU   F OE2    1 
ATOM   16047 N  N      . PRO   F 4  227 ? 2.105   -38.462  -110.259 1.00 114.73 ? 227 PRO   F N      1 
ATOM   16048 C  CA     . PRO   F 4  227 ? 1.876   -39.448  -111.331 1.00 108.50 ? 227 PRO   F CA     1 
ATOM   16049 C  C      . PRO   F 4  227 ? 3.097   -40.294  -111.664 1.00 108.84 ? 227 PRO   F C      1 
ATOM   16050 O  O      . PRO   F 4  227 ? 4.086   -39.808  -112.221 1.00 111.73 ? 227 PRO   F O      1 
ATOM   16051 C  CB     . PRO   F 4  227 ? 1.462   -38.585  -112.530 1.00 110.43 ? 227 PRO   F CB     1 
ATOM   16052 C  CG     . PRO   F 4  227 ? 1.041   -37.282  -111.968 1.00 110.34 ? 227 PRO   F CG     1 
ATOM   16053 C  CD     . PRO   F 4  227 ? 1.658   -37.106  -110.616 1.00 111.35 ? 227 PRO   F CD     1 
ATOM   16054 N  N      . TYR   F 4  228 ? 3.022   -41.573  -111.318 1.00 112.17 ? 228 TYR   F N      1 
ATOM   16055 C  CA     . TYR   F 4  228 ? 4.073   -42.534  -111.622 1.00 111.37 ? 228 TYR   F CA     1 
ATOM   16056 C  C      . TYR   F 4  228 ? 4.560   -42.365  -113.059 1.00 113.11 ? 228 TYR   F C      1 
ATOM   16057 O  O      . TYR   F 4  228 ? 3.787   -42.531  -114.007 1.00 118.29 ? 228 TYR   F O      1 
ATOM   16058 C  CB     . TYR   F 4  228 ? 3.514   -43.943  -111.379 1.00 98.31  ? 228 TYR   F CB     1 
ATOM   16059 C  CG     . TYR   F 4  228 ? 4.484   -45.084  -111.548 1.00 101.47 ? 228 TYR   F CG     1 
ATOM   16060 C  CD1    . TYR   F 4  228 ? 4.700   -45.659  -112.792 1.00 102.37 ? 228 TYR   F CD1    1 
ATOM   16061 C  CD2    . TYR   F 4  228 ? 5.173   -45.597  -110.462 1.00 102.13 ? 228 TYR   F CD2    1 
ATOM   16062 C  CE1    . TYR   F 4  228 ? 5.585   -46.710  -112.954 1.00 99.35  ? 228 TYR   F CE1    1 
ATOM   16063 C  CE2    . TYR   F 4  228 ? 6.063   -46.651  -110.615 1.00 103.03 ? 228 TYR   F CE2    1 
ATOM   16064 C  CZ     . TYR   F 4  228 ? 6.266   -47.201  -111.868 1.00 98.45  ? 228 TYR   F CZ     1 
ATOM   16065 O  OH     . TYR   F 4  228 ? 7.147   -48.247  -112.045 1.00 94.19  ? 228 TYR   F OH     1 
ATOM   16066 N  N      . ASN   F 4  229 ? 5.830   -41.989  -113.232 1.00 106.01 ? 229 ASN   F N      1 
ATOM   16067 C  CA     . ASN   F 4  229 ? 6.422   -41.860  -114.561 1.00 115.69 ? 229 ASN   F CA     1 
ATOM   16068 C  C      . ASN   F 4  229 ? 7.472   -42.949  -114.734 1.00 116.74 ? 229 ASN   F C      1 
ATOM   16069 O  O      . ASN   F 4  229 ? 8.336   -43.128  -113.871 1.00 121.19 ? 229 ASN   F O      1 
ATOM   16070 C  CB     . ASN   F 4  229 ? 6.998   -40.448  -114.794 1.00 124.28 ? 229 ASN   F CB     1 
ATOM   16071 C  CG     . ASN   F 4  229 ? 8.391   -40.235  -114.192 1.00 129.00 ? 229 ASN   F CG     1 
ATOM   16072 O  OD1    . ASN   F 4  229 ? 9.358   -40.887  -114.581 1.00 131.64 ? 229 ASN   F OD1    1 
ATOM   16073 N  ND2    . ASN   F 4  229 ? 8.492   -39.297  -113.251 1.00 123.68 ? 229 ASN   F ND2    1 
ATOM   16074 N  N      . SER   F 4  230 ? 7.373   -43.692  -115.836 1.00 112.96 ? 230 SER   F N      1 
ATOM   16075 C  CA     . SER   F 4  230 ? 8.164   -44.908  -115.988 1.00 117.21 ? 230 SER   F CA     1 
ATOM   16076 C  C      . SER   F 4  230 ? 9.650   -44.595  -116.175 1.00 128.58 ? 230 SER   F C      1 
ATOM   16077 O  O      . SER   F 4  230 ? 10.487  -45.011  -115.367 1.00 133.37 ? 230 SER   F O      1 
ATOM   16078 C  CB     . SER   F 4  230 ? 7.616   -45.738  -117.152 1.00 114.92 ? 230 SER   F CB     1 
ATOM   16079 O  OG     . SER   F 4  230 ? 8.600   -46.604  -117.688 1.00 117.71 ? 230 SER   F OG     1 
ATOM   16080 N  N      . ALA   F 4  231 ? 9.999   -43.847  -117.228 1.00 128.00 ? 231 ALA   F N      1 
ATOM   16081 C  CA     . ALA   F 4  231 ? 11.408  -43.695  -117.599 1.00 127.70 ? 231 ALA   F CA     1 
ATOM   16082 C  C      . ALA   F 4  231 ? 12.251  -43.118  -116.464 1.00 132.98 ? 231 ALA   F C      1 
ATOM   16083 O  O      . ALA   F 4  231 ? 13.386  -43.558  -116.238 1.00 132.21 ? 231 ALA   F O      1 
ATOM   16084 C  CB     . ALA   F 4  231 ? 11.533  -42.820  -118.847 1.00 125.53 ? 231 ALA   F CB     1 
ATOM   16085 N  N      . ASN   F 4  232 ? 11.719  -42.132  -115.738 1.00 133.20 ? 232 ASN   F N      1 
ATOM   16086 C  CA     . ASN   F 4  232 ? 12.480  -41.434  -114.697 1.00 134.95 ? 232 ASN   F CA     1 
ATOM   16087 C  C      . ASN   F 4  232 ? 12.313  -42.146  -113.352 1.00 138.39 ? 232 ASN   F C      1 
ATOM   16088 O  O      . ASN   F 4  232 ? 11.516  -41.754  -112.492 1.00 134.90 ? 232 ASN   F O      1 
ATOM   16089 C  CB     . ASN   F 4  232 ? 12.046  -39.978  -114.613 1.00 136.29 ? 232 ASN   F CB     1 
ATOM   16090 C  CG     . ASN   F 4  232 ? 13.014  -39.128  -113.819 1.00 135.59 ? 232 ASN   F CG     1 
ATOM   16091 O  OD1    . ASN   F 4  232 ? 12.647  -38.552  -112.793 1.00 135.24 ? 232 ASN   F OD1    1 
ATOM   16092 N  ND2    . ASN   F 4  232 ? 14.254  -39.030  -114.299 1.00 130.24 ? 232 ASN   F ND2    1 
ATOM   16093 N  N      . PHE   F 4  233 ? 13.117  -43.200  -113.159 1.00 138.47 ? 233 PHE   F N      1 
ATOM   16094 C  CA     . PHE   F 4  233 ? 13.083  -43.981  -111.926 1.00 135.73 ? 233 PHE   F CA     1 
ATOM   16095 C  C      . PHE   F 4  233 ? 13.758  -43.275  -110.752 1.00 137.43 ? 233 PHE   F C      1 
ATOM   16096 O  O      . PHE   F 4  233 ? 13.683  -43.775  -109.623 1.00 135.13 ? 233 PHE   F O      1 
ATOM   16097 C  CB     . PHE   F 4  233 ? 13.718  -45.368  -112.151 1.00 134.28 ? 233 PHE   F CB     1 
ATOM   16098 C  CG     . PHE   F 4  233 ? 15.070  -45.335  -112.841 1.00 141.74 ? 233 PHE   F CG     1 
ATOM   16099 C  CD1    . PHE   F 4  233 ? 16.236  -45.074  -112.121 1.00 140.97 ? 233 PHE   F CD1    1 
ATOM   16100 C  CD2    . PHE   F 4  233 ? 15.177  -45.586  -114.208 1.00 141.26 ? 233 PHE   F CD2    1 
ATOM   16101 C  CE1    . PHE   F 4  233 ? 17.484  -45.055  -112.757 1.00 138.58 ? 233 PHE   F CE1    1 
ATOM   16102 C  CE2    . PHE   F 4  233 ? 16.417  -45.566  -114.847 1.00 134.45 ? 233 PHE   F CE2    1 
ATOM   16103 C  CZ     . PHE   F 4  233 ? 17.570  -45.301  -114.119 1.00 133.91 ? 233 PHE   F CZ     1 
ATOM   16104 N  N      . GLN   F 4  234 ? 14.409  -42.134  -110.990 1.00 136.80 ? 234 GLN   F N      1 
ATOM   16105 C  CA     . GLN   F 4  234 ? 14.955  -41.284  -109.941 1.00 134.14 ? 234 GLN   F CA     1 
ATOM   16106 C  C      . GLN   F 4  234 ? 13.938  -40.245  -109.466 1.00 132.56 ? 234 GLN   F C      1 
ATOM   16107 O  O      . GLN   F 4  234 ? 14.319  -39.212  -108.913 1.00 129.87 ? 234 GLN   F O      1 
ATOM   16108 C  CB     . GLN   F 4  234 ? 16.253  -40.623  -110.442 1.00 128.82 ? 234 GLN   F CB     1 
ATOM   16109 C  CG     . GLN   F 4  234 ? 16.883  -39.497  -109.595 1.00 126.53 ? 234 GLN   F CG     1 
ATOM   16110 C  CD     . GLN   F 4  234 ? 16.819  -39.750  -108.103 1.00 129.28 ? 234 GLN   F CD     1 
ATOM   16111 O  OE1    . GLN   F 4  234 ? 17.546  -40.579  -107.569 1.00 129.54 ? 234 GLN   F OE1    1 
ATOM   16112 N  NE2    . GLN   F 4  234 ? 15.934  -39.032  -107.419 1.00 129.12 ? 234 GLN   F NE2    1 
ATOM   16113 N  N      . ASP   F 4  235 ? 12.649  -40.493  -109.669 1.00 129.74 ? 235 ASP   F N      1 
ATOM   16114 C  CA     . ASP   F 4  235 ? 11.616  -39.583  -109.179 1.00 132.27 ? 235 ASP   F CA     1 
ATOM   16115 C  C      . ASP   F 4  235 ? 11.021  -40.131  -107.880 1.00 129.46 ? 235 ASP   F C      1 
ATOM   16116 O  O      . ASP   F 4  235 ? 9.920   -40.686  -107.838 1.00 125.76 ? 235 ASP   F O      1 
ATOM   16117 C  CB     . ASP   F 4  235 ? 10.547  -39.367  -110.246 1.00 132.95 ? 235 ASP   F CB     1 
ATOM   16118 C  CG     . ASP   F 4  235 ? 9.625   -38.202  -109.920 1.00 132.54 ? 235 ASP   F CG     1 
ATOM   16119 O  OD1    . ASP   F 4  235 ? 10.033  -37.321  -109.122 1.00 127.82 ? 235 ASP   F OD1    1 
ATOM   16120 O  OD2    . ASP   F 4  235 ? 8.506   -38.159  -110.477 1.00 130.06 ? 235 ASP   F OD2    1 
ATOM   16121 N  N      . LYS   F 4  236 ? 11.789  -39.977  -106.800 1.00 128.12 ? 236 LYS   F N      1 
ATOM   16122 C  CA     . LYS   F 4  236 ? 11.296  -40.327  -105.476 1.00 121.20 ? 236 LYS   F CA     1 
ATOM   16123 C  C      . LYS   F 4  236 ? 9.992   -39.578  -105.205 1.00 122.75 ? 236 LYS   F C      1 
ATOM   16124 O  O      . LYS   F 4  236 ? 9.716   -38.555  -105.842 1.00 119.65 ? 236 LYS   F O      1 
ATOM   16125 C  CB     . LYS   F 4  236 ? 12.350  -40.010  -104.413 1.00 115.62 ? 236 LYS   F CB     1 
ATOM   16126 N  N      . THR   F 4  237 ? 9.176   -40.094  -104.277 1.00 123.85 ? 237 THR   F N      1 
ATOM   16127 C  CA     . THR   F 4  237 ? 7.857   -39.550  -103.925 1.00 123.36 ? 237 THR   F CA     1 
ATOM   16128 C  C      . THR   F 4  237 ? 6.777   -40.031  -104.894 1.00 124.36 ? 237 THR   F C      1 
ATOM   16129 O  O      . THR   F 4  237 ? 5.604   -40.148  -104.515 1.00 120.98 ? 237 THR   F O      1 
ATOM   16130 C  CB     . THR   F 4  237 ? 7.868   -38.011  -103.865 1.00 121.12 ? 237 THR   F CB     1 
ATOM   16131 O  OG1    . THR   F 4  237 ? 8.479   -37.580  -102.644 1.00 116.14 ? 237 THR   F OG1    1 
ATOM   16132 C  CG2    . THR   F 4  237 ? 6.457   -37.451  -103.905 1.00 117.19 ? 237 THR   F CG2    1 
ATOM   16133 N  N      . CYS   F 4  238 ? 7.157   -40.305  -106.147 1.00 123.85 ? 238 CYS   F N      1 
ATOM   16134 C  CA     . CYS   F 4  238 ? 6.266   -40.940  -107.111 1.00 118.90 ? 238 CYS   F CA     1 
ATOM   16135 C  C      . CYS   F 4  238 ? 6.490   -42.443  -107.215 1.00 117.35 ? 238 CYS   F C      1 
ATOM   16136 O  O      . CYS   F 4  238 ? 5.599   -43.156  -107.695 1.00 115.47 ? 238 CYS   F O      1 
ATOM   16137 C  CB     . CYS   F 4  238 ? 6.430   -40.303  -108.500 1.00 117.79 ? 238 CYS   F CB     1 
ATOM   16138 S  SG     . CYS   F 4  238 ? 7.095   -41.400  -109.795 1.00 115.25 ? 238 CYS   F SG     1 
ATOM   16139 N  N      . HIS   F 4  239 ? 7.648   -42.933  -106.762 1.00 117.03 ? 239 HIS   F N      1 
ATOM   16140 C  CA     . HIS   F 4  239 ? 7.953   -44.358  -106.721 1.00 116.34 ? 239 HIS   F CA     1 
ATOM   16141 C  C      . HIS   F 4  239 ? 7.966   -44.936  -105.315 1.00 109.79 ? 239 HIS   F C      1 
ATOM   16142 O  O      . HIS   F 4  239 ? 7.627   -46.109  -105.143 1.00 104.37 ? 239 HIS   F O      1 
ATOM   16143 C  CB     . HIS   F 4  239 ? 9.316   -44.641  -107.373 1.00 115.80 ? 239 HIS   F CB     1 
ATOM   16144 C  CG     . HIS   F 4  239 ? 9.335   -44.444  -108.858 1.00 120.38 ? 239 HIS   F CG     1 
ATOM   16145 N  ND1    . HIS   F 4  239 ? 8.219   -44.617  -109.649 1.00 117.24 ? 239 HIS   F ND1    1 
ATOM   16146 C  CD2    . HIS   F 4  239 ? 10.341  -44.097  -109.697 1.00 124.70 ? 239 HIS   F CD2    1 
ATOM   16147 C  CE1    . HIS   F 4  239 ? 8.536   -44.380  -110.910 1.00 117.76 ? 239 HIS   F CE1    1 
ATOM   16148 N  NE2    . HIS   F 4  239 ? 9.818   -44.063  -110.966 1.00 123.75 ? 239 HIS   F NE2    1 
ATOM   16149 N  N      . LEU   F 4  240 ? 8.360   -44.145  -104.314 1.00 112.18 ? 240 LEU   F N      1 
ATOM   16150 C  CA     . LEU   F 4  240 ? 8.438   -44.576  -102.921 1.00 107.44 ? 240 LEU   F CA     1 
ATOM   16151 C  C      . LEU   F 4  240 ? 7.279   -43.949  -102.156 1.00 108.22 ? 240 LEU   F C      1 
ATOM   16152 O  O      . LEU   F 4  240 ? 7.253   -42.732  -101.946 1.00 108.48 ? 240 LEU   F O      1 
ATOM   16153 C  CB     . LEU   F 4  240 ? 9.779   -44.184  -102.308 1.00 98.05  ? 240 LEU   F CB     1 
ATOM   16154 N  N      . THR   F 4  241 ? 6.329   -44.780  -101.734 1.00 105.39 ? 241 THR   F N      1 
ATOM   16155 C  CA     . THR   F 4  241 ? 5.119   -44.313  -101.057 1.00 108.76 ? 241 THR   F CA     1 
ATOM   16156 C  C      . THR   F 4  241 ? 5.291   -44.217  -99.548  1.00 108.98 ? 241 THR   F C      1 
ATOM   16157 O  O      . THR   F 4  241 ? 4.394   -44.593  -98.788  1.00 107.29 ? 241 THR   F O      1 
ATOM   16158 C  CB     . THR   F 4  241 ? 3.949   -45.226  -101.408 1.00 103.53 ? 241 THR   F CB     1 
ATOM   16159 O  OG1    . THR   F 4  241 ? 3.931   -46.347  -100.518 1.00 102.43 ? 241 THR   F OG1    1 
ATOM   16160 C  CG2    . THR   F 4  241 ? 4.065   -45.724  -102.837 1.00 101.89 ? 241 THR   F CG2    1 
ATOM   16161 N  N      . ASN   F 4  242 ? 6.425   -43.703  -99.080  1.00 110.99 ? 242 ASN   F N      1 
ATOM   16162 C  CA     . ASN   F 4  242 ? 6.672   -43.583  -97.649  1.00 114.59 ? 242 ASN   F CA     1 
ATOM   16163 C  C      . ASN   F 4  242 ? 5.995   -42.320  -97.132  1.00 118.99 ? 242 ASN   F C      1 
ATOM   16164 O  O      . ASN   F 4  242 ? 6.207   -41.231  -97.678  1.00 119.77 ? 242 ASN   F O      1 
ATOM   16165 C  CB     . ASN   F 4  242 ? 8.172   -43.553  -97.371  1.00 114.16 ? 242 ASN   F CB     1 
ATOM   16166 C  CG     . ASN   F 4  242 ? 8.858   -44.858  -97.735  1.00 117.92 ? 242 ASN   F CG     1 
ATOM   16167 O  OD1    . ASN   F 4  242 ? 8.754   -45.329  -98.874  1.00 115.03 ? 242 ASN   F OD1    1 
ATOM   16168 N  ND2    . ASN   F 4  242 ? 9.568   -45.449  -96.773  1.00 119.46 ? 242 ASN   F ND2    1 
ATOM   16169 N  N      . HIS   F 4  243 ? 5.170   -42.461  -96.089  1.00 117.90 ? 243 HIS   F N      1 
ATOM   16170 C  CA     . HIS   F 4  243 ? 4.461   -41.303  -95.553  1.00 118.94 ? 243 HIS   F CA     1 
ATOM   16171 C  C      . HIS   F 4  243 ? 5.436   -40.186  -95.201  1.00 117.65 ? 243 HIS   F C      1 
ATOM   16172 O  O      . HIS   F 4  243 ? 5.209   -39.015  -95.529  1.00 117.05 ? 243 HIS   F O      1 
ATOM   16173 C  CB     . HIS   F 4  243 ? 3.636   -41.703  -94.326  1.00 117.20 ? 243 HIS   F CB     1 
ATOM   16174 C  CG     . HIS   F 4  243 ? 2.869   -40.568  -93.721  1.00 119.99 ? 243 HIS   F CG     1 
ATOM   16175 N  ND1    . HIS   F 4  243 ? 3.486   -39.485  -93.132  1.00 118.13 ? 243 HIS   F ND1    1 
ATOM   16176 C  CD2    . HIS   F 4  243 ? 1.537   -40.350  -93.608  1.00 117.91 ? 243 HIS   F CD2    1 
ATOM   16177 C  CE1    . HIS   F 4  243 ? 2.568   -38.645  -92.688  1.00 119.96 ? 243 HIS   F CE1    1 
ATOM   16178 N  NE2    . HIS   F 4  243 ? 1.378   -39.147  -92.963  1.00 120.82 ? 243 HIS   F NE2    1 
ATOM   16179 N  N      . CYS   F 4  244 ? 6.530   -40.541  -94.525  1.00 121.11 ? 244 CYS   F N      1 
ATOM   16180 C  CA     . CYS   F 4  244 ? 7.577   -39.576  -94.206  1.00 121.77 ? 244 CYS   F CA     1 
ATOM   16181 C  C      . CYS   F 4  244 ? 8.094   -38.897  -95.467  1.00 116.60 ? 244 CYS   F C      1 
ATOM   16182 O  O      . CYS   F 4  244 ? 8.079   -37.666  -95.580  1.00 117.08 ? 244 CYS   F O      1 
ATOM   16183 C  CB     . CYS   F 4  244 ? 8.715   -40.283  -93.470  1.00 121.89 ? 244 CYS   F CB     1 
ATOM   16184 S  SG     . CYS   F 4  244 ? 8.405   -42.051  -93.214  1.00 124.41 ? 244 CYS   F SG     1 
ATOM   16185 N  N      . ILE   F 4  245 ? 8.542   -39.700  -96.439  1.00 112.63 ? 245 ILE   F N      1 
ATOM   16186 C  CA     . ILE   F 4  245 ? 9.108   -39.182  -97.683  1.00 113.94 ? 245 ILE   F CA     1 
ATOM   16187 C  C      . ILE   F 4  245 ? 8.243   -38.080  -98.284  1.00 114.31 ? 245 ILE   F C      1 
ATOM   16188 O  O      . ILE   F 4  245 ? 8.749   -37.196  -98.988  1.00 114.30 ? 245 ILE   F O      1 
ATOM   16189 C  CB     . ILE   F 4  245 ? 9.336   -40.337  -98.680  1.00 114.69 ? 245 ILE   F CB     1 
ATOM   16190 C  CG1    . ILE   F 4  245 ? 10.666  -41.042  -98.384  1.00 116.33 ? 245 ILE   F CG1    1 
ATOM   16191 C  CG2    . ILE   F 4  245 ? 9.280   -39.839  -100.118 1.00 113.64 ? 245 ILE   F CG2    1 
ATOM   16192 C  CD1    . ILE   F 4  245 ? 11.266  -40.702  -97.018  1.00 113.62 ? 245 ILE   F CD1    1 
ATOM   16193 N  N      . GLN   F 4  246 ? 6.934   -38.100  -98.018  1.00 113.62 ? 246 GLN   F N      1 
ATOM   16194 C  CA     . GLN   F 4  246 ? 6.049   -37.008  -98.426  1.00 108.71 ? 246 GLN   F CA     1 
ATOM   16195 C  C      . GLN   F 4  246 ? 6.217   -35.847  -97.441  1.00 110.07 ? 246 GLN   F C      1 
ATOM   16196 O  O      . GLN   F 4  246 ? 5.373   -35.558  -96.588  1.00 106.16 ? 246 GLN   F O      1 
ATOM   16197 C  CB     . GLN   F 4  246 ? 4.607   -37.488  -98.526  1.00 110.94 ? 246 GLN   F CB     1 
ATOM   16198 C  CG     . GLN   F 4  246 ? 4.462   -38.922  -99.061  1.00 113.32 ? 246 GLN   F CG     1 
ATOM   16199 C  CD     . GLN   F 4  246 ? 4.304   -39.004  -100.587 1.00 113.66 ? 246 GLN   F CD     1 
ATOM   16200 O  OE1    . GLN   F 4  246 ? 3.186   -38.986  -101.108 1.00 109.46 ? 246 GLN   F OE1    1 
ATOM   16201 N  NE2    . GLN   F 4  246 ? 5.423   -39.130  -101.299 1.00 110.59 ? 246 GLN   F NE2    1 
ATOM   16202 N  N      . LYS   F 4  247 ? 7.358   -35.176  -97.585  1.00 111.93 ? 247 LYS   F N      1 
ATOM   16203 C  CA     . LYS   F 4  247 ? 7.777   -34.086  -96.716  1.00 106.35 ? 247 LYS   F CA     1 
ATOM   16204 C  C      . LYS   F 4  247 ? 7.265   -32.745  -97.244  1.00 104.01 ? 247 LYS   F C      1 
ATOM   16205 O  O      . LYS   F 4  247 ? 6.057   -32.549  -97.407  1.00 104.30 ? 247 LYS   F O      1 
ATOM   16206 C  CB     . LYS   F 4  247 ? 9.309   -34.078  -96.592  1.00 95.57  ? 247 LYS   F CB     1 
ATOM   16207 C  CG     . LYS   F 4  247 ? 10.026  -33.477  -97.794  1.00 97.53  ? 247 LYS   F CG     1 
ATOM   16208 C  CD     . LYS   F 4  247 ? 9.649   -34.190  -99.096  1.00 95.93  ? 247 LYS   F CD     1 
ATOM   16209 C  CE     . LYS   F 4  247 ? 10.167  -33.462  -100.332 1.00 86.80  ? 247 LYS   F CE     1 
ATOM   16210 N  NZ     . LYS   F 4  247 ? 9.518   -33.955  -101.578 1.00 74.94  ? 247 LYS   F NZ     1 
ATOM   16211 N  N      . TYR   F 4  253 ? 1.064   -33.310  -101.733 1.00 92.52  ? 253 TYR   F N      1 
ATOM   16212 C  CA     . TYR   F 4  253 ? 0.777   -33.888  -100.428 1.00 98.45  ? 253 TYR   F CA     1 
ATOM   16213 C  C      . TYR   F 4  253 ? -0.523  -33.333  -99.862  1.00 108.67 ? 253 TYR   F C      1 
ATOM   16214 O  O      . TYR   F 4  253 ? -0.656  -32.123  -99.690  1.00 111.63 ? 253 TYR   F O      1 
ATOM   16215 C  CB     . TYR   F 4  253 ? 1.922   -33.614  -99.452  1.00 105.73 ? 253 TYR   F CB     1 
ATOM   16216 C  CG     . TYR   F 4  253 ? 1.716   -34.189  -98.062  1.00 106.19 ? 253 TYR   F CG     1 
ATOM   16217 C  CD1    . TYR   F 4  253 ? 1.017   -33.484  -97.088  1.00 102.05 ? 253 TYR   F CD1    1 
ATOM   16218 C  CD2    . TYR   F 4  253 ? 2.242   -35.428  -97.720  1.00 107.81 ? 253 TYR   F CD2    1 
ATOM   16219 C  CE1    . TYR   F 4  253 ? 0.832   -34.007  -95.822  1.00 103.67 ? 253 TYR   F CE1    1 
ATOM   16220 C  CE2    . TYR   F 4  253 ? 2.065   -35.957  -96.457  1.00 110.48 ? 253 TYR   F CE2    1 
ATOM   16221 C  CZ     . TYR   F 4  253 ? 1.359   -35.244  -95.510  1.00 109.25 ? 253 TYR   F CZ     1 
ATOM   16222 O  OH     . TYR   F 4  253 ? 1.180   -35.776  -94.252  1.00 106.11 ? 253 TYR   F OH     1 
ATOM   16223 N  N      . GLY   F 4  254 ? -1.468  -34.222  -99.545  1.00 110.34 ? 254 GLY   F N      1 
ATOM   16224 C  CA     . GLY   F 4  254 ? -2.761  -33.831  -99.012  1.00 107.62 ? 254 GLY   F CA     1 
ATOM   16225 C  C      . GLY   F 4  254 ? -3.789  -33.463  -100.056 1.00 104.74 ? 254 GLY   F C      1 
ATOM   16226 O  O      . GLY   F 4  254 ? -4.953  -33.215  -99.702  1.00 98.93  ? 254 GLY   F O      1 
ATOM   16227 N  N      . ARG   F 4  255 ? -3.398  -33.427  -101.328 1.00 106.16 ? 255 ARG   F N      1 
ATOM   16228 C  CA     . ARG   F 4  255 ? -4.274  -33.055  -102.429 1.00 109.54 ? 255 ARG   F CA     1 
ATOM   16229 C  C      . ARG   F 4  255 ? -5.494  -33.966  -102.473 1.00 109.43 ? 255 ARG   F C      1 
ATOM   16230 O  O      . ARG   F 4  255 ? -6.607  -33.540  -102.138 1.00 110.29 ? 255 ARG   F O      1 
ATOM   16231 C  CB     . ARG   F 4  255 ? -3.493  -33.114  -103.750 1.00 110.00 ? 255 ARG   F CB     1 
ATOM   16232 C  CG     . ARG   F 4  255 ? -4.238  -32.619  -104.990 1.00 111.63 ? 255 ARG   F CG     1 
ATOM   16233 C  CD     . ARG   F 4  255 ? -3.304  -32.588  -106.204 1.00 111.94 ? 255 ARG   F CD     1 
ATOM   16234 N  NE     . ARG   F 4  255 ? -4.004  -32.340  -107.462 1.00 117.27 ? 255 ARG   F NE     1 
ATOM   16235 C  CZ     . ARG   F 4  255 ? -3.469  -32.518  -108.665 1.00 114.48 ? 255 ARG   F CZ     1 
ATOM   16236 N  NH1    . ARG   F 4  255 ? -2.236  -32.973  -108.811 1.00 112.41 ? 255 ARG   F NH1    1 
ATOM   16237 N  NH2    . ARG   F 4  255 ? -4.193  -32.241  -109.747 1.00 109.81 ? 255 ARG   F NH2    1 
ATOM   16238 N  N      . TYR   F 4  256 ? -5.281  -35.232  -102.861 1.00 107.29 ? 256 TYR   F N      1 
ATOM   16239 C  CA     . TYR   F 4  256 ? -6.383  -36.154  -103.131 1.00 105.19 ? 256 TYR   F CA     1 
ATOM   16240 C  C      . TYR   F 4  256 ? -6.966  -36.778  -101.863 1.00 105.84 ? 256 TYR   F C      1 
ATOM   16241 O  O      . TYR   F 4  256 ? -8.176  -37.047  -101.809 1.00 98.53  ? 256 TYR   F O      1 
ATOM   16242 C  CB     . TYR   F 4  256 ? -5.913  -37.258  -104.084 1.00 105.56 ? 256 TYR   F CB     1 
ATOM   16243 C  CG     . TYR   F 4  256 ? -5.199  -36.766  -105.331 1.00 108.85 ? 256 TYR   F CG     1 
ATOM   16244 C  CD1    . TYR   F 4  256 ? -3.840  -36.462  -105.305 1.00 109.55 ? 256 TYR   F CD1    1 
ATOM   16245 C  CD2    . TYR   F 4  256 ? -5.879  -36.627  -106.541 1.00 109.31 ? 256 TYR   F CD2    1 
ATOM   16246 C  CE1    . TYR   F 4  256 ? -3.178  -36.018  -106.449 1.00 113.99 ? 256 TYR   F CE1    1 
ATOM   16247 C  CE2    . TYR   F 4  256 ? -5.226  -36.181  -107.689 1.00 110.24 ? 256 TYR   F CE2    1 
ATOM   16248 C  CZ     . TYR   F 4  256 ? -3.877  -35.877  -107.637 1.00 113.36 ? 256 TYR   F CZ     1 
ATOM   16249 O  OH     . TYR   F 4  256 ? -3.221  -35.430  -108.767 1.00 111.61 ? 256 TYR   F OH     1 
ATOM   16250 N  N      . GLU   F 4  257 ? -6.131  -37.033  -100.853 1.00 107.55 ? 257 GLU   F N      1 
ATOM   16251 C  CA     . GLU   F 4  257 ? -6.593  -37.566  -99.580  1.00 102.62 ? 257 GLU   F CA     1 
ATOM   16252 C  C      . GLU   F 4  257 ? -5.730  -37.009  -98.462  1.00 101.65 ? 257 GLU   F C      1 
ATOM   16253 O  O      . GLU   F 4  257 ? -4.535  -36.756  -98.648  1.00 100.07 ? 257 GLU   F O      1 
ATOM   16254 C  CB     . GLU   F 4  257 ? -6.555  -39.097  -99.537  1.00 99.58  ? 257 GLU   F CB     1 
ATOM   16255 C  CG     . GLU   F 4  257 ? -6.815  -39.788  -100.857 1.00 102.58 ? 257 GLU   F CG     1 
ATOM   16256 C  CD     . GLU   F 4  257 ? -5.549  -39.961  -101.685 1.00 104.50 ? 257 GLU   F CD     1 
ATOM   16257 O  OE1    . GLU   F 4  257 ? -4.463  -40.128  -101.081 1.00 103.93 ? 257 GLU   F OE1    1 
ATOM   16258 O  OE2    . GLU   F 4  257 ? -5.647  -39.961  -102.937 1.00 98.94  ? 257 GLU   F OE2    1 
ATOM   16259 N  N      . GLU   F 4  258 ? -6.352  -36.850  -97.292  1.00 101.16 ? 258 GLU   F N      1 
ATOM   16260 C  CA     . GLU   F 4  258 ? -5.686  -36.289  -96.121  1.00 100.36 ? 258 GLU   F CA     1 
ATOM   16261 C  C      . GLU   F 4  258 ? -4.481  -37.130  -95.699  1.00 102.51 ? 258 GLU   F C      1 
ATOM   16262 O  O      . GLU   F 4  258 ? -4.618  -38.313  -95.372  1.00 102.24 ? 258 GLU   F O      1 
ATOM   16263 C  CB     . GLU   F 4  258 ? -6.679  -36.179  -94.968  1.00 94.27  ? 258 GLU   F CB     1 
ATOM   16264 C  CG     . GLU   F 4  258 ? -6.000  -35.959  -93.642  1.00 101.80 ? 258 GLU   F CG     1 
ATOM   16265 C  CD     . GLU   F 4  258 ? -6.644  -34.865  -92.831  1.00 111.06 ? 258 GLU   F CD     1 
ATOM   16266 O  OE1    . GLU   F 4  258 ? -7.894  -34.836  -92.775  1.00 114.16 ? 258 GLU   F OE1    1 
ATOM   16267 O  OE2    . GLU   F 4  258 ? -5.901  -34.039  -92.252  1.00 109.27 ? 258 GLU   F OE2    1 
ATOM   16268 N  N      . GLY   F 4  259 ? -3.305  -36.503  -95.683  1.00 104.78 ? 259 GLY   F N      1 
ATOM   16269 C  CA     . GLY   F 4  259 ? -2.073  -37.179  -95.313  1.00 102.78 ? 259 GLY   F CA     1 
ATOM   16270 C  C      . GLY   F 4  259 ? -1.625  -38.240  -96.291  1.00 103.74 ? 259 GLY   F C      1 
ATOM   16271 O  O      . GLY   F 4  259 ? -0.958  -39.199  -95.888  1.00 106.31 ? 259 GLY   F O      1 
ATOM   16272 N  N      . ASN   F 4  260 ? -1.959  -38.087  -97.575  1.00 103.39 ? 260 ASN   F N      1 
ATOM   16273 C  CA     . ASN   F 4  260 ? -1.713  -39.119  -98.579  1.00 103.87 ? 260 ASN   F CA     1 
ATOM   16274 C  C      . ASN   F 4  260 ? -2.113  -40.489  -98.042  1.00 105.24 ? 260 ASN   F C      1 
ATOM   16275 O  O      . ASN   F 4  260 ? -1.398  -41.481  -98.227  1.00 102.89 ? 260 ASN   F O      1 
ATOM   16276 C  CB     . ASN   F 4  260 ? -0.247  -39.125  -99.019  1.00 103.09 ? 260 ASN   F CB     1 
ATOM   16277 C  CG     . ASN   F 4  260 ? 0.140   -37.878  -99.766  1.00 105.44 ? 260 ASN   F CG     1 
ATOM   16278 O  OD1    . ASN   F 4  260 ? -0.581  -36.879  -99.739  1.00 108.52 ? 260 ASN   F OD1    1 
ATOM   16279 N  ND2    . ASN   F 4  260 ? 1.278   -37.928  -100.454 1.00 102.15 ? 260 ASN   F ND2    1 
ATOM   16280 N  N      . GLU   F 4  261 ? -3.259  -40.549  -97.374  1.00 103.10 ? 261 GLU   F N      1 
ATOM   16281 C  CA     . GLU   F 4  261 ? -3.695  -41.751  -96.682  1.00 99.55  ? 261 GLU   F CA     1 
ATOM   16282 C  C      . GLU   F 4  261 ? -5.147  -42.013  -97.042  1.00 97.30  ? 261 GLU   F C      1 
ATOM   16283 O  O      . GLU   F 4  261 ? -6.012  -41.163  -96.798  1.00 96.69  ? 261 GLU   F O      1 
ATOM   16284 C  CB     . GLU   F 4  261 ? -3.539  -41.594  -95.167  1.00 102.88 ? 261 GLU   F CB     1 
ATOM   16285 C  CG     . GLU   F 4  261 ? -2.171  -41.949  -94.631  1.00 101.77 ? 261 GLU   F CG     1 
ATOM   16286 C  CD     . GLU   F 4  261 ? -2.116  -41.856  -93.116  1.00 106.00 ? 261 GLU   F CD     1 
ATOM   16287 O  OE1    . GLU   F 4  261 ? -3.190  -41.676  -92.486  1.00 90.89  ? 261 GLU   F OE1    1 
ATOM   16288 O  OE2    . GLU   F 4  261 ? -0.996  -41.953  -92.562  1.00 113.37 ? 261 GLU   F OE2    1 
ATOM   16289 N  N      . MET   F 4  262 ? -5.414  -43.185  -97.617  1.00 93.91  ? 262 MET   F N      1 
ATOM   16290 C  CA     . MET   F 4  262 ? -6.768  -43.610  -97.948  1.00 91.47  ? 262 MET   F CA     1 
ATOM   16291 C  C      . MET   F 4  262 ? -7.111  -44.859  -97.148  1.00 88.32  ? 262 MET   F C      1 
ATOM   16292 O  O      . MET   F 4  262 ? -6.456  -45.898  -97.302  1.00 86.82  ? 262 MET   F O      1 
ATOM   16293 C  CB     . MET   F 4  262 ? -6.915  -43.881  -99.443  1.00 91.72  ? 262 MET   F CB     1 
ATOM   16294 C  CG     . MET   F 4  262 ? -8.278  -44.448  -99.835  1.00 91.31  ? 262 MET   F CG     1 
ATOM   16295 S  SD     . MET   F 4  262 ? -8.455  -44.479  -101.624 1.00 85.24  ? 262 MET   F SD     1 
ATOM   16296 C  CE     . MET   F 4  262 ? -6.736  -44.481  -102.084 1.00 86.62  ? 262 MET   F CE     1 
ATOM   16297 N  N      . PHE   F 4  263 ? -8.135  -44.751  -96.301  1.00 84.09  ? 263 PHE   F N      1 
ATOM   16298 C  CA     . PHE   F 4  263 ? -8.626  -45.865  -95.509  1.00 83.54  ? 263 PHE   F CA     1 
ATOM   16299 C  C      . PHE   F 4  263 ? -9.457  -46.801  -96.391  1.00 85.60  ? 263 PHE   F C      1 
ATOM   16300 O  O      . PHE   F 4  263 ? -9.551  -46.630  -97.611  1.00 81.76  ? 263 PHE   F O      1 
ATOM   16301 C  CB     . PHE   F 4  263 ? -9.415  -45.346  -94.307  1.00 88.24  ? 263 PHE   F CB     1 
ATOM   16302 C  CG     . PHE   F 4  263 ? -8.577  -44.559  -93.325  1.00 93.38  ? 263 PHE   F CG     1 
ATOM   16303 C  CD1    . PHE   F 4  263 ? -9.121  -43.494  -92.614  1.00 92.11  ? 263 PHE   F CD1    1 
ATOM   16304 C  CD2    . PHE   F 4  263 ? -7.241  -44.886  -93.112  1.00 88.38  ? 263 PHE   F CD2    1 
ATOM   16305 C  CE1    . PHE   F 4  263 ? -8.345  -42.770  -91.723  1.00 89.96  ? 263 PHE   F CE1    1 
ATOM   16306 C  CE2    . PHE   F 4  263 ? -6.467  -44.169  -92.215  1.00 87.59  ? 263 PHE   F CE2    1 
ATOM   16307 C  CZ     . PHE   F 4  263 ? -7.019  -43.112  -91.519  1.00 90.79  ? 263 PHE   F CZ     1 
ATOM   16308 N  N      . PHE   F 4  264 ? -10.074 -47.812  -95.769  1.00 83.10  ? 264 PHE   F N      1 
ATOM   16309 C  CA     . PHE   F 4  264 ? -10.601 -48.924  -96.557  1.00 81.52  ? 264 PHE   F CA     1 
ATOM   16310 C  C      . PHE   F 4  264 ? -11.962 -48.619  -97.158  1.00 81.63  ? 264 PHE   F C      1 
ATOM   16311 O  O      . PHE   F 4  264 ? -12.255 -49.076  -98.271  1.00 82.11  ? 264 PHE   F O      1 
ATOM   16312 C  CB     . PHE   F 4  264 ? -10.674 -50.196  -95.710  1.00 74.66  ? 264 PHE   F CB     1 
ATOM   16313 C  CG     . PHE   F 4  264 ? -9.447  -51.047  -95.808  1.00 71.69  ? 264 PHE   F CG     1 
ATOM   16314 C  CD1    . PHE   F 4  264 ? -8.388  -50.656  -96.604  1.00 66.71  ? 264 PHE   F CD1    1 
ATOM   16315 C  CD2    . PHE   F 4  264 ? -9.342  -52.223  -95.092  1.00 71.62  ? 264 PHE   F CD2    1 
ATOM   16316 C  CE1    . PHE   F 4  264 ? -7.254  -51.423  -96.693  1.00 65.94  ? 264 PHE   F CE1    1 
ATOM   16317 C  CE2    . PHE   F 4  264 ? -8.218  -52.994  -95.183  1.00 66.08  ? 264 PHE   F CE2    1 
ATOM   16318 C  CZ     . PHE   F 4  264 ? -7.168  -52.591  -95.986  1.00 64.17  ? 264 PHE   F CZ     1 
ATOM   16319 N  N      . GLU   F 4  265 ? -12.802 -47.863  -96.449  1.00 80.50  ? 265 GLU   F N      1 
ATOM   16320 C  CA     . GLU   F 4  265 ? -14.110 -47.521  -96.991  1.00 80.28  ? 265 GLU   F CA     1 
ATOM   16321 C  C      . GLU   F 4  265 ? -13.970 -46.775  -98.310  1.00 84.13  ? 265 GLU   F C      1 
ATOM   16322 O  O      . GLU   F 4  265 ? -14.657 -47.081  -99.294  1.00 81.29  ? 265 GLU   F O      1 
ATOM   16323 C  CB     . GLU   F 4  265 ? -14.887 -46.687  -95.984  1.00 82.00  ? 265 GLU   F CB     1 
ATOM   16324 C  CG     . GLU   F 4  265 ? -15.995 -45.891  -96.609  1.00 87.80  ? 265 GLU   F CG     1 
ATOM   16325 C  CD     . GLU   F 4  265 ? -16.841 -45.188  -95.572  1.00 98.04  ? 265 GLU   F CD     1 
ATOM   16326 O  OE1    . GLU   F 4  265 ? -16.393 -44.135  -95.054  1.00 99.23  ? 265 GLU   F OE1    1 
ATOM   16327 O  OE2    . GLU   F 4  265 ? -17.953 -45.695  -95.281  1.00 95.90  ? 265 GLU   F OE2    1 
ATOM   16328 N  N      . GLU   F 4  266 ? -13.066 -45.798  -98.347  1.00 83.27  ? 266 GLU   F N      1 
ATOM   16329 C  CA     . GLU   F 4  266 ? -12.850 -45.033  -99.566  1.00 85.11  ? 266 GLU   F CA     1 
ATOM   16330 C  C      . GLU   F 4  266 ? -12.338 -45.928  -100.689 1.00 81.10  ? 266 GLU   F C      1 
ATOM   16331 O  O      . GLU   F 4  266 ? -12.883 -45.914  -101.797 1.00 84.33  ? 266 GLU   F O      1 
ATOM   16332 C  CB     . GLU   F 4  266 ? -11.886 -43.876  -99.279  1.00 91.60  ? 266 GLU   F CB     1 
ATOM   16333 C  CG     . GLU   F 4  266 ? -11.191 -43.276  -100.497 1.00 90.25  ? 266 GLU   F CG     1 
ATOM   16334 C  CD     . GLU   F 4  266 ? -11.183 -41.748  -100.478 1.00 99.21  ? 266 GLU   F CD     1 
ATOM   16335 O  OE1    . GLU   F 4  266 ? -11.193 -41.150  -99.378  1.00 101.34 ? 266 GLU   F OE1    1 
ATOM   16336 O  OE2    . GLU   F 4  266 ? -11.141 -41.140  -101.569 1.00 105.90 ? 266 GLU   F OE2    1 
ATOM   16337 N  N      . PHE   F 4  267 ? -11.309 -46.741  -100.414 1.00 83.82  ? 267 PHE   F N      1 
ATOM   16338 C  CA     . PHE   F 4  267 ? -10.640 -47.489  -101.483 1.00 79.08  ? 267 PHE   F CA     1 
ATOM   16339 C  C      . PHE   F 4  267 ? -11.515 -48.615  -102.023 1.00 80.39  ? 267 PHE   F C      1 
ATOM   16340 O  O      . PHE   F 4  267 ? -11.505 -48.883  -103.231 1.00 76.75  ? 267 PHE   F O      1 
ATOM   16341 C  CB     . PHE   F 4  267 ? -9.303  -48.046  -100.994 1.00 77.06  ? 267 PHE   F CB     1 
ATOM   16342 C  CG     . PHE   F 4  267 ? -8.597  -48.914  -102.005 1.00 79.39  ? 267 PHE   F CG     1 
ATOM   16343 C  CD1    . PHE   F 4  267 ? -7.894  -48.356  -103.055 1.00 80.80  ? 267 PHE   F CD1    1 
ATOM   16344 C  CD2    . PHE   F 4  267 ? -8.636  -50.297  -101.900 1.00 79.71  ? 267 PHE   F CD2    1 
ATOM   16345 C  CE1    . PHE   F 4  267 ? -7.239  -49.161  -103.989 1.00 82.00  ? 267 PHE   F CE1    1 
ATOM   16346 C  CE2    . PHE   F 4  267 ? -7.982  -51.106  -102.827 1.00 80.24  ? 267 PHE   F CE2    1 
ATOM   16347 C  CZ     . PHE   F 4  267 ? -7.283  -50.538  -103.873 1.00 79.69  ? 267 PHE   F CZ     1 
ATOM   16348 N  N      . ASN   F 4  268 ? -12.264 -49.301  -101.152 1.00 74.69  ? 268 ASN   F N      1 
ATOM   16349 C  CA     . ASN   F 4  268 ? -13.187 -50.319  -101.646 1.00 73.22  ? 268 ASN   F CA     1 
ATOM   16350 C  C      . ASN   F 4  268 ? -14.213 -49.699  -102.588 1.00 75.82  ? 268 ASN   F C      1 
ATOM   16351 O  O      . ASN   F 4  268 ? -14.451 -50.207  -103.692 1.00 72.32  ? 268 ASN   F O      1 
ATOM   16352 C  CB     . ASN   F 4  268 ? -13.872 -51.030  -100.477 1.00 71.91  ? 268 ASN   F CB     1 
ATOM   16353 C  CG     . ASN   F 4  268 ? -15.019 -51.919  -100.927 1.00 66.44  ? 268 ASN   F CG     1 
ATOM   16354 O  OD1    . ASN   F 4  268 ? -14.816 -53.039  -101.413 1.00 67.59  ? 268 ASN   F OD1    1 
ATOM   16355 N  ND2    . ASN   F 4  268 ? -16.232 -51.415  -100.782 1.00 58.96  ? 268 ASN   F ND2    1 
ATOM   16356 N  N      . GLN   F 4  269 ? -14.815 -48.581  -102.170 1.00 76.50  ? 269 GLN   F N      1 
ATOM   16357 C  CA     . GLN   F 4  269 ? -15.730 -47.847  -103.041 1.00 76.95  ? 269 GLN   F CA     1 
ATOM   16358 C  C      . GLN   F 4  269 ? -15.101 -47.531  -104.390 1.00 75.88  ? 269 GLN   F C      1 
ATOM   16359 O  O      . GLN   F 4  269 ? -15.755 -47.667  -105.430 1.00 74.80  ? 269 GLN   F O      1 
ATOM   16360 C  CB     . GLN   F 4  269 ? -16.173 -46.548  -102.372 1.00 80.60  ? 269 GLN   F CB     1 
ATOM   16361 C  CG     . GLN   F 4  269 ? -17.331 -45.864  -103.066 1.00 73.46  ? 269 GLN   F CG     1 
ATOM   16362 C  CD     . GLN   F 4  269 ? -18.662 -46.486  -102.709 1.00 82.21  ? 269 GLN   F CD     1 
ATOM   16363 O  OE1    . GLN   F 4  269 ? -19.353 -47.024  -103.571 1.00 86.25  ? 269 GLN   F OE1    1 
ATOM   16364 N  NE2    . GLN   F 4  269 ? -19.023 -46.433  -101.430 1.00 79.92  ? 269 GLN   F NE2    1 
ATOM   16365 N  N      . TYR   F 4  270 ? -13.843 -47.077  -104.398 1.00 73.41  ? 270 TYR   F N      1 
ATOM   16366 C  CA     . TYR   F 4  270 ? -13.202 -46.758  -105.671 1.00 73.76  ? 270 TYR   F CA     1 
ATOM   16367 C  C      . TYR   F 4  270 ? -13.039 -48.000  -106.537 1.00 79.70  ? 270 TYR   F C      1 
ATOM   16368 O  O      . TYR   F 4  270 ? -13.201 -47.935  -107.763 1.00 78.79  ? 270 TYR   F O      1 
ATOM   16369 C  CB     . TYR   F 4  270 ? -11.844 -46.110  -105.453 1.00 69.94  ? 270 TYR   F CB     1 
ATOM   16370 C  CG     . TYR   F 4  270 ? -10.966 -46.178  -106.691 1.00 74.63  ? 270 TYR   F CG     1 
ATOM   16371 C  CD1    . TYR   F 4  270 ? -11.185 -45.322  -107.772 1.00 78.33  ? 270 TYR   F CD1    1 
ATOM   16372 C  CD2    . TYR   F 4  270 ? -9.921  -47.093  -106.784 1.00 71.64  ? 270 TYR   F CD2    1 
ATOM   16373 C  CE1    . TYR   F 4  270 ? -10.384 -45.368  -108.905 1.00 78.57  ? 270 TYR   F CE1    1 
ATOM   16374 C  CE2    . TYR   F 4  270 ? -9.119  -47.150  -107.915 1.00 79.95  ? 270 TYR   F CE2    1 
ATOM   16375 C  CZ     . TYR   F 4  270 ? -9.352  -46.282  -108.975 1.00 82.28  ? 270 TYR   F CZ     1 
ATOM   16376 O  OH     . TYR   F 4  270 ? -8.551  -46.331  -110.101 1.00 79.29  ? 270 TYR   F OH     1 
ATOM   16377 N  N      . LEU   F 4  271 ? -12.681 -49.134  -105.919 1.00 83.11  ? 271 LEU   F N      1 
ATOM   16378 C  CA     . LEU   F 4  271 ? -12.608 -50.403  -106.643 1.00 76.90  ? 271 LEU   F CA     1 
ATOM   16379 C  C      . LEU   F 4  271 ? -13.961 -50.759  -107.243 1.00 74.11  ? 271 LEU   F C      1 
ATOM   16380 O  O      . LEU   F 4  271 ? -14.068 -51.104  -108.428 1.00 68.30  ? 271 LEU   F O      1 
ATOM   16381 C  CB     . LEU   F 4  271 ? -12.146 -51.511  -105.696 1.00 74.24  ? 271 LEU   F CB     1 
ATOM   16382 C  CG     . LEU   F 4  271 ? -10.672 -51.644  -105.328 1.00 70.83  ? 271 LEU   F CG     1 
ATOM   16383 C  CD1    . LEU   F 4  271 ? -10.538 -52.668  -104.225 1.00 69.42  ? 271 LEU   F CD1    1 
ATOM   16384 C  CD2    . LEU   F 4  271 ? -9.858  -52.053  -106.536 1.00 65.40  ? 271 LEU   F CD2    1 
ATOM   16385 N  N      . MET   F 4  272 ? -15.007 -50.672  -106.419 1.00 69.86  ? 272 MET   F N      1 
ATOM   16386 C  CA     . MET   F 4  272 ? -16.362 -50.961  -106.858 1.00 66.35  ? 272 MET   F CA     1 
ATOM   16387 C  C      . MET   F 4  272 ? -16.740 -50.117  -108.071 1.00 72.78  ? 272 MET   F C      1 
ATOM   16388 O  O      . MET   F 4  272 ? -17.170 -50.652  -109.102 1.00 73.97  ? 272 MET   F O      1 
ATOM   16389 C  CB     . MET   F 4  272 ? -17.311 -50.713  -105.687 1.00 70.87  ? 272 MET   F CB     1 
ATOM   16390 C  CG     . MET   F 4  272 ? -17.583 -51.934  -104.834 1.00 66.16  ? 272 MET   F CG     1 
ATOM   16391 S  SD     . MET   F 4  272 ? -18.943 -51.637  -103.696 1.00 79.51  ? 272 MET   F SD     1 
ATOM   16392 C  CE     . MET   F 4  272 ? -19.768 -53.252  -103.687 1.00 69.42  ? 272 MET   F CE     1 
ATOM   16393 N  N      . ASP   F 4  273 ? -16.576 -48.791  -107.964 1.00 78.81  ? 273 ASP   F N      1 
ATOM   16394 C  CA     . ASP   F 4  273 ? -16.899 -47.870  -109.058 1.00 69.68  ? 273 ASP   F CA     1 
ATOM   16395 C  C      . ASP   F 4  273 ? -15.949 -48.048  -110.236 1.00 69.35  ? 273 ASP   F C      1 
ATOM   16396 O  O      . ASP   F 4  273 ? -16.375 -48.303  -111.366 1.00 74.41  ? 273 ASP   F O      1 
ATOM   16397 C  CB     . ASP   F 4  273 ? -16.833 -46.423  -108.563 1.00 64.05  ? 273 ASP   F CB     1 
ATOM   16398 C  CG     . ASP   F 4  273 ? -17.876 -46.102  -107.498 1.00 70.12  ? 273 ASP   F CG     1 
ATOM   16399 O  OD1    . ASP   F 4  273 ? -18.970 -46.711  -107.492 1.00 67.13  ? 273 ASP   F OD1    1 
ATOM   16400 O  OD2    . ASP   F 4  273 ? -17.595 -45.213  -106.664 1.00 76.98  ? 273 ASP   F OD2    1 
ATOM   16401 N  N      . ALA   F 4  274 ? -14.652 -47.905  -109.990 1.00 62.32  ? 274 ALA   F N      1 
ATOM   16402 C  CA     . ALA   F 4  274 ? -13.696 -47.881  -111.085 1.00 67.83  ? 274 ALA   F CA     1 
ATOM   16403 C  C      . ALA   F 4  274 ? -13.401 -49.264  -111.651 1.00 72.80  ? 274 ALA   F C      1 
ATOM   16404 O  O      . ALA   F 4  274 ? -13.037 -49.375  -112.827 1.00 77.98  ? 274 ALA   F O      1 
ATOM   16405 C  CB     . ALA   F 4  274 ? -12.392 -47.224  -110.626 1.00 77.06  ? 274 ALA   F CB     1 
ATOM   16406 N  N      . LEU   F 4  275 ? -13.523 -50.326  -110.850 1.00 75.09  ? 275 LEU   F N      1 
ATOM   16407 C  CA     . LEU   F 4  275 ? -13.149 -51.654  -111.321 1.00 72.96  ? 275 LEU   F CA     1 
ATOM   16408 C  C      . LEU   F 4  275 ? -14.268 -52.691  -111.254 1.00 70.99  ? 275 LEU   F C      1 
ATOM   16409 O  O      . LEU   F 4  275 ? -14.087 -53.801  -111.778 1.00 70.07  ? 275 LEU   F O      1 
ATOM   16410 C  CB     . LEU   F 4  275 ? -11.917 -52.158  -110.550 1.00 69.52  ? 275 LEU   F CB     1 
ATOM   16411 C  CG     . LEU   F 4  275 ? -10.623 -51.416  -110.909 1.00 67.27  ? 275 LEU   F CG     1 
ATOM   16412 C  CD1    . LEU   F 4  275 ? -9.401  -52.207  -110.492 1.00 58.54  ? 275 LEU   F CD1    1 
ATOM   16413 C  CD2    . LEU   F 4  275 ? -10.569 -51.101  -112.398 1.00 67.40  ? 275 LEU   F CD2    1 
ATOM   16414 N  N      . ASN   F 4  276 ? -15.425 -52.352  -110.677 1.00 69.15  ? 276 ASN   F N      1 
ATOM   16415 C  CA     . ASN   F 4  276 ? -16.570 -53.262  -110.574 1.00 72.76  ? 276 ASN   F CA     1 
ATOM   16416 C  C      . ASN   F 4  276 ? -16.268 -54.444  -109.654 1.00 73.86  ? 276 ASN   F C      1 
ATOM   16417 O  O      . ASN   F 4  276 ? -16.860 -55.520  -109.782 1.00 73.48  ? 276 ASN   F O      1 
ATOM   16418 C  CB     . ASN   F 4  276 ? -17.023 -53.757  -111.956 1.00 71.27  ? 276 ASN   F CB     1 
ATOM   16419 C  CG     . ASN   F 4  276 ? -18.375 -54.473  -111.919 1.00 70.86  ? 276 ASN   F CG     1 
ATOM   16420 O  OD1    . ASN   F 4  276 ? -19.159 -54.323  -110.970 1.00 67.54  ? 276 ASN   F OD1    1 
ATOM   16421 N  ND2    . ASN   F 4  276 ? -18.644 -55.266  -112.953 1.00 64.77  ? 276 ASN   F ND2    1 
ATOM   16422 N  N      . THR   F 4  277 ? -15.341 -54.253  -108.720 1.00 69.70  ? 277 THR   F N      1 
ATOM   16423 C  CA     . THR   F 4  277 ? -15.001 -55.296  -107.768 1.00 65.73  ? 277 THR   F CA     1 
ATOM   16424 C  C      . THR   F 4  277 ? -15.067 -54.762  -106.347 1.00 64.66  ? 277 THR   F C      1 
ATOM   16425 O  O      . THR   F 4  277 ? -15.636 -53.693  -106.100 1.00 65.97  ? 277 THR   F O      1 
ATOM   16426 C  CB     . THR   F 4  277 ? -13.615 -55.862  -108.068 1.00 64.07  ? 277 THR   F CB     1 
ATOM   16427 O  OG1    . THR   F 4  277 ? -13.516 -57.193  -107.540 1.00 64.28  ? 277 THR   F OG1    1 
ATOM   16428 C  CG2    . THR   F 4  277 ? -12.539 -54.978  -107.464 1.00 67.91  ? 277 THR   F CG2    1 
ATOM   16429 N  N      . THR   F 4  278 ? -14.495 -55.508  -105.407 1.00 64.06  ? 278 THR   F N      1 
ATOM   16430 C  CA     . THR   F 4  278 ? -14.508 -55.149  -103.998 1.00 64.49  ? 278 THR   F CA     1 
ATOM   16431 C  C      . THR   F 4  278 ? -13.139 -55.414  -103.403 1.00 61.31  ? 278 THR   F C      1 
ATOM   16432 O  O      . THR   F 4  278 ? -12.327 -56.158  -103.963 1.00 58.40  ? 278 THR   F O      1 
ATOM   16433 C  CB     . THR   F 4  278 ? -15.562 -55.929  -103.233 1.00 62.27  ? 278 THR   F CB     1 
ATOM   16434 O  OG1    . THR   F 4  278 ? -15.210 -57.321  -103.257 1.00 58.89  ? 278 THR   F OG1    1 
ATOM   16435 C  CG2    . THR   F 4  278 ? -16.923 -55.725  -103.868 1.00 61.32  ? 278 THR   F CG2    1 
ATOM   16436 N  N      . LEU   F 4  279 ? -12.897 -54.792  -102.248 1.00 62.47  ? 279 LEU   F N      1 
ATOM   16437 C  CA     . LEU   F 4  279 ? -11.593 -54.917  -101.598 1.00 67.28  ? 279 LEU   F CA     1 
ATOM   16438 C  C      . LEU   F 4  279 ? -11.330 -56.354  -101.147 1.00 65.47  ? 279 LEU   F C      1 
ATOM   16439 O  O      . LEU   F 4  279 ? -10.256 -56.914  -101.422 1.00 57.78  ? 279 LEU   F O      1 
ATOM   16440 C  CB     . LEU   F 4  279 ? -11.508 -53.945  -100.420 1.00 59.90  ? 279 LEU   F CB     1 
ATOM   16441 C  CG     . LEU   F 4  279 ? -10.190 -53.966  -99.663  1.00 59.64  ? 279 LEU   F CG     1 
ATOM   16442 C  CD1    . LEU   F 4  279 ? -9.007  -53.946  -100.631 1.00 55.45  ? 279 LEU   F CD1    1 
ATOM   16443 C  CD2    . LEU   F 4  279 ? -10.170 -52.783  -98.721  1.00 61.03  ? 279 LEU   F CD2    1 
ATOM   16444 N  N      . GLU   F 4  280 ? -12.303 -56.958  -100.446 1.00 60.03  ? 280 GLU   F N      1 
ATOM   16445 C  CA     . GLU   F 4  280 ? -12.268 -58.372  -100.097 1.00 57.12  ? 280 GLU   F CA     1 
ATOM   16446 C  C      . GLU   F 4  280 ? -11.824 -59.242  -101.270 1.00 60.42  ? 280 GLU   F C      1 
ATOM   16447 O  O      . GLU   F 4  280 ? -10.812 -59.945  -101.187 1.00 66.22  ? 280 GLU   F O      1 
ATOM   16448 C  CB     . GLU   F 4  280 ? -13.648 -58.817  -99.607  1.00 70.15  ? 280 GLU   F CB     1 
ATOM   16449 C  CG     . GLU   F 4  280 ? -13.664 -60.212  -99.010  1.00 67.68  ? 280 GLU   F CG     1 
ATOM   16450 C  CD     . GLU   F 4  280 ? -12.777 -60.311  -97.775  1.00 73.74  ? 280 GLU   F CD     1 
ATOM   16451 O  OE1    . GLU   F 4  280 ? -12.962 -59.513  -96.814  1.00 67.97  ? 280 GLU   F OE1    1 
ATOM   16452 O  OE2    . GLU   F 4  280 ? -11.872 -61.176  -97.788  1.00 69.92  ? 280 GLU   F OE2    1 
ATOM   16453 N  N      . ASN   F 4  281 ? -12.562 -59.207  -102.382 1.00 58.09  ? 281 ASN   F N      1 
ATOM   16454 C  CA     . ASN   F 4  281 ? -12.304 -60.164  -103.457 1.00 58.48  ? 281 ASN   F CA     1 
ATOM   16455 C  C      . ASN   F 4  281 ? -10.972 -59.892  -104.154 1.00 58.78  ? 281 ASN   F C      1 
ATOM   16456 O  O      . ASN   F 4  281 ? -10.147 -60.803  -104.313 1.00 58.18  ? 281 ASN   F O      1 
ATOM   16457 C  CB     . ASN   F 4  281 ? -13.458 -60.154  -104.458 1.00 58.97  ? 281 ASN   F CB     1 
ATOM   16458 C  CG     . ASN   F 4  281 ? -14.762 -60.660  -103.859 1.00 60.31  ? 281 ASN   F CG     1 
ATOM   16459 O  OD1    . ASN   F 4  281 ? -15.053 -60.445  -102.674 1.00 62.41  ? 281 ASN   F OD1    1 
ATOM   16460 N  ND2    . ASN   F 4  281 ? -15.545 -61.360  -104.671 1.00 56.07  ? 281 ASN   F ND2    1 
ATOM   16461 N  N      . SER   F 4  282 ? -10.736 -58.641  -104.565 1.00 56.96  ? 282 SER   F N      1 
ATOM   16462 C  CA     . SER   F 4  282 ? -9.577  -58.331  -105.403 1.00 62.20  ? 282 SER   F CA     1 
ATOM   16463 C  C      . SER   F 4  282 ? -8.250  -58.330  -104.640 1.00 63.15  ? 282 SER   F C      1 
ATOM   16464 O  O      . SER   F 4  282 ? -7.209  -58.665  -105.229 1.00 58.36  ? 282 SER   F O      1 
ATOM   16465 C  CB     . SER   F 4  282 ? -9.776  -56.978  -106.085 1.00 61.48  ? 282 SER   F CB     1 
ATOM   16466 O  OG     . SER   F 4  282 ? -10.203 -55.999  -105.148 1.00 63.13  ? 282 SER   F OG     1 
ATOM   16467 N  N      . ILE   F 4  283 ? -8.252  -57.948  -103.354 1.00 55.82  ? 283 ILE   F N      1 
ATOM   16468 C  CA     . ILE   F 4  283 ? -7.000  -57.779  -102.616 1.00 63.56  ? 283 ILE   F CA     1 
ATOM   16469 C  C      . ILE   F 4  283 ? -6.988  -58.532  -101.280 1.00 62.37  ? 283 ILE   F C      1 
ATOM   16470 O  O      . ILE   F 4  283 ? -6.005  -59.213  -100.958 1.00 56.67  ? 283 ILE   F O      1 
ATOM   16471 C  CB     . ILE   F 4  283 ? -6.695  -56.282  -102.392 1.00 69.31  ? 283 ILE   F CB     1 
ATOM   16472 C  CG1    . ILE   F 4  283 ? -6.520  -55.551  -103.728 1.00 67.09  ? 283 ILE   F CG1    1 
ATOM   16473 C  CG2    . ILE   F 4  283 ? -5.441  -56.098  -101.520 1.00 66.74  ? 283 ILE   F CG2    1 
ATOM   16474 C  CD1    . ILE   F 4  283 ? -7.154  -54.165  -103.748 1.00 68.19  ? 283 ILE   F CD1    1 
ATOM   16475 N  N      . LEU   F 4  284 ? -8.064  -58.421  -100.490 1.00 53.17  ? 284 LEU   F N      1 
ATOM   16476 C  CA     . LEU   F 4  284 ? -7.986  -58.897  -99.112  1.00 55.60  ? 284 LEU   F CA     1 
ATOM   16477 C  C      . LEU   F 4  284 ? -7.791  -60.414  -99.034  1.00 60.65  ? 284 LEU   F C      1 
ATOM   16478 O  O      . LEU   F 4  284 ? -7.018  -60.903  -98.200  1.00 59.61  ? 284 LEU   F O      1 
ATOM   16479 C  CB     . LEU   F 4  284 ? -9.223  -58.481  -98.325  1.00 59.12  ? 284 LEU   F CB     1 
ATOM   16480 C  CG     . LEU   F 4  284 ? -8.893  -57.807  -96.983  1.00 59.17  ? 284 LEU   F CG     1 
ATOM   16481 C  CD1    . LEU   F 4  284 ? -8.120  -56.507  -97.203  1.00 51.30  ? 284 LEU   F CD1    1 
ATOM   16482 C  CD2    . LEU   F 4  284 ? -10.135 -57.563  -96.148  1.00 66.42  ? 284 LEU   F CD2    1 
ATOM   16483 N  N      . LEU   F 4  285 ? -8.483  -61.182  -99.875  1.00 60.88  ? 285 LEU   F N      1 
ATOM   16484 C  CA     . LEU   F 4  285 ? -8.246  -62.624  -99.891  1.00 60.01  ? 285 LEU   F CA     1 
ATOM   16485 C  C      . LEU   F 4  285 ? -6.754  -62.937  -99.967  1.00 57.32  ? 285 LEU   F C      1 
ATOM   16486 O  O      . LEU   F 4  285 ? -6.241  -63.761  -99.205  1.00 60.49  ? 285 LEU   F O      1 
ATOM   16487 C  CB     . LEU   F 4  285 ? -8.997  -63.280  -101.055 1.00 59.90  ? 285 LEU   F CB     1 
ATOM   16488 C  CG     . LEU   F 4  285 ? -10.424 -63.808  -100.835 1.00 55.20  ? 285 LEU   F CG     1 
ATOM   16489 C  CD1    . LEU   F 4  285 ? -10.774 -64.795  -101.919 1.00 56.49  ? 285 LEU   F CD1    1 
ATOM   16490 C  CD2    . LEU   F 4  285 ? -10.611 -64.436  -99.465  1.00 56.57  ? 285 LEU   F CD2    1 
ATOM   16491 N  N      . GLN   F 4  286 ? -6.032  -62.270  -100.865 1.00 58.76  ? 286 GLN   F N      1 
ATOM   16492 C  CA     . GLN   F 4  286 ? -4.611  -62.564  -101.035 1.00 57.88  ? 286 GLN   F CA     1 
ATOM   16493 C  C      . GLN   F 4  286 ? -3.778  -62.074  -99.857  1.00 56.29  ? 286 GLN   F C      1 
ATOM   16494 O  O      . GLN   F 4  286 ? -2.692  -62.613  -99.600  1.00 53.22  ? 286 GLN   F O      1 
ATOM   16495 C  CB     . GLN   F 4  286 ? -4.084  -61.914  -102.315 1.00 63.25  ? 286 GLN   F CB     1 
ATOM   16496 C  CG     . GLN   F 4  286 ? -4.917  -62.103  -103.559 1.00 58.98  ? 286 GLN   F CG     1 
ATOM   16497 C  CD     . GLN   F 4  286 ? -4.199  -61.592  -104.780 1.00 61.55  ? 286 GLN   F CD     1 
ATOM   16498 O  OE1    . GLN   F 4  286 ? -3.016  -61.881  -104.993 1.00 58.96  ? 286 GLN   F OE1    1 
ATOM   16499 N  NE2    . GLN   F 4  286 ? -4.887  -60.757  -105.554 1.00 66.03  ? 286 GLN   F NE2    1 
ATOM   16500 N  N      . ILE   F 4  287 ? -4.234  -61.021  -99.171  1.00 56.30  ? 287 ILE   F N      1 
ATOM   16501 C  CA     . ILE   F 4  287 ? -3.487  -60.514  -98.026  1.00 56.32  ? 287 ILE   F CA     1 
ATOM   16502 C  C      . ILE   F 4  287 ? -3.598  -61.491  -96.872  1.00 56.56  ? 287 ILE   F C      1 
ATOM   16503 O  O      . ILE   F 4  287 ? -2.613  -61.785  -96.185  1.00 54.37  ? 287 ILE   F O      1 
ATOM   16504 C  CB     . ILE   F 4  287 ? -3.986  -59.117  -97.608  1.00 57.75  ? 287 ILE   F CB     1 
ATOM   16505 C  CG1    . ILE   F 4  287 ? -3.524  -58.033  -98.582  1.00 60.28  ? 287 ILE   F CG1    1 
ATOM   16506 C  CG2    . ILE   F 4  287 ? -3.482  -58.762  -96.219  1.00 53.34  ? 287 ILE   F CG2    1 
ATOM   16507 C  CD1    . ILE   F 4  287 ? -4.114  -56.669  -98.251  1.00 56.35  ? 287 ILE   F CD1    1 
ATOM   16508 N  N      . LYS   F 4  288 ? -4.804  -62.002  -96.632  1.00 54.16  ? 288 LYS   F N      1 
ATOM   16509 C  CA     . LYS   F 4  288 ? -4.975  -62.939  -95.539  1.00 50.13  ? 288 LYS   F CA     1 
ATOM   16510 C  C      . LYS   F 4  288 ? -4.254  -64.243  -95.836  1.00 53.23  ? 288 LYS   F C      1 
ATOM   16511 O  O      . LYS   F 4  288 ? -3.817  -64.934  -94.906  1.00 55.50  ? 288 LYS   F O      1 
ATOM   16512 C  CB     . LYS   F 4  288 ? -6.464  -63.145  -95.261  1.00 53.54  ? 288 LYS   F CB     1 
ATOM   16513 C  CG     . LYS   F 4  288 ? -7.117  -61.862  -94.741  1.00 52.28  ? 288 LYS   F CG     1 
ATOM   16514 C  CD     . LYS   F 4  288 ? -8.629  -61.943  -94.672  1.00 47.71  ? 288 LYS   F CD     1 
ATOM   16515 C  CE     . LYS   F 4  288 ? -9.242  -62.424  -95.963  1.00 58.10  ? 288 LYS   F CE     1 
ATOM   16516 N  NZ     . LYS   F 4  288 ? -10.730 -62.380  -95.854  1.00 62.66  ? 288 LYS   F NZ     1 
ATOM   16517 N  N      . HIS   F 4  289 ? -4.065  -64.565  -97.119  1.00 50.66  ? 289 HIS   F N      1 
ATOM   16518 C  CA     . HIS   F 4  289 ? -3.272  -65.741  -97.466  1.00 56.14  ? 289 HIS   F CA     1 
ATOM   16519 C  C      . HIS   F 4  289 ? -1.792  -65.521  -97.154  1.00 55.20  ? 289 HIS   F C      1 
ATOM   16520 O  O      . HIS   F 4  289 ? -1.098  -66.450  -96.711  1.00 47.49  ? 289 HIS   F O      1 
ATOM   16521 C  CB     . HIS   F 4  289 ? -3.453  -66.108  -98.945  1.00 49.23  ? 289 HIS   F CB     1 
ATOM   16522 C  CG     . HIS   F 4  289 ? -2.549  -67.210  -99.389  1.00 42.94  ? 289 HIS   F CG     1 
ATOM   16523 N  ND1    . HIS   F 4  289 ? -2.789  -68.532  -99.086  1.00 53.31  ? 289 HIS   F ND1    1 
ATOM   16524 C  CD2    . HIS   F 4  289 ? -1.359  -67.184  -100.029 1.00 47.57  ? 289 HIS   F CD2    1 
ATOM   16525 C  CE1    . HIS   F 4  289 ? -1.804  -69.277  -99.555  1.00 49.25  ? 289 HIS   F CE1    1 
ATOM   16526 N  NE2    . HIS   F 4  289 ? -0.925  -68.482  -100.136 1.00 45.24  ? 289 HIS   F NE2    1 
ATOM   16527 N  N      . ILE   F 4  290 ? -1.295  -64.298  -97.377  1.00 56.71  ? 290 ILE   F N      1 
ATOM   16528 C  CA     . ILE   F 4  290 ? 0.121   -64.009  -97.161  1.00 57.47  ? 290 ILE   F CA     1 
ATOM   16529 C  C      . ILE   F 4  290 ? 0.425   -63.887  -95.674  1.00 52.07  ? 290 ILE   F C      1 
ATOM   16530 O  O      . ILE   F 4  290 ? 1.363   -64.509  -95.165  1.00 49.36  ? 290 ILE   F O      1 
ATOM   16531 C  CB     . ILE   F 4  290 ? 0.548   -62.745  -97.938  1.00 59.39  ? 290 ILE   F CB     1 
ATOM   16532 C  CG1    . ILE   F 4  290 ? 0.181   -62.888  -99.419  1.00 59.38  ? 290 ILE   F CG1    1 
ATOM   16533 C  CG2    . ILE   F 4  290 ? 2.046   -62.522  -97.793  1.00 58.40  ? 290 ILE   F CG2    1 
ATOM   16534 C  CD1    . ILE   F 4  290 ? 0.128   -61.587  -100.172 1.00 58.97  ? 290 ILE   F CD1    1 
ATOM   16535 N  N      . ILE   F 4  291 ? -0.357  -63.090  -94.950  1.00 51.38  ? 291 ILE   F N      1 
ATOM   16536 C  CA     . ILE   F 4  291 ? -0.171  -63.028  -93.504  1.00 52.32  ? 291 ILE   F CA     1 
ATOM   16537 C  C      . ILE   F 4  291 ? -0.214  -64.428  -92.912  1.00 53.63  ? 291 ILE   F C      1 
ATOM   16538 O  O      . ILE   F 4  291 ? 0.689   -64.837  -92.173  1.00 55.60  ? 291 ILE   F O      1 
ATOM   16539 C  CB     . ILE   F 4  291 ? -1.225  -62.121  -92.857  1.00 53.93  ? 291 ILE   F CB     1 
ATOM   16540 C  CG1    . ILE   F 4  291 ? -0.978  -60.677  -93.275  1.00 55.84  ? 291 ILE   F CG1    1 
ATOM   16541 C  CG2    . ILE   F 4  291 ? -1.192  -62.288  -91.341  1.00 49.89  ? 291 ILE   F CG2    1 
ATOM   16542 C  CD1    . ILE   F 4  291 ? -2.252  -59.959  -93.646  1.00 57.54  ? 291 ILE   F CD1    1 
ATOM   16543 N  N      . ARG   F 4  292 ? -1.264  -65.190  -93.241  1.00 55.81  ? 292 ARG   F N      1 
ATOM   16544 C  CA     . ARG   F 4  292 ? -1.380  -66.546  -92.713  1.00 54.17  ? 292 ARG   F CA     1 
ATOM   16545 C  C      . ARG   F 4  292 ? -0.152  -67.371  -93.064  1.00 49.77  ? 292 ARG   F C      1 
ATOM   16546 O  O      . ARG   F 4  292 ? 0.390   -68.087  -92.218  1.00 51.88  ? 292 ARG   F O      1 
ATOM   16547 C  CB     . ARG   F 4  292 ? -2.643  -67.233  -93.244  1.00 58.59  ? 292 ARG   F CB     1 
ATOM   16548 C  CG     . ARG   F 4  292 ? -3.272  -68.247  -92.284  1.00 62.19  ? 292 ARG   F CG     1 
ATOM   16549 C  CD     . ARG   F 4  292 ? -4.345  -69.144  -92.957  1.00 67.75  ? 292 ARG   F CD     1 
ATOM   16550 N  NE     . ARG   F 4  292 ? -5.195  -68.471  -93.937  1.00 69.07  ? 292 ARG   F NE     1 
ATOM   16551 C  CZ     . ARG   F 4  292 ? -6.187  -67.640  -93.633  1.00 70.91  ? 292 ARG   F CZ     1 
ATOM   16552 N  NH1    . ARG   F 4  292 ? -6.384  -67.227  -92.387  1.00 76.42  ? 292 ARG   F NH1    1 
ATOM   16553 N  NH2    . ARG   F 4  292 ? -7.005  -67.217  -94.601  1.00 60.19  ? 292 ARG   F NH2    1 
ATOM   16554 N  N      . SER   F 4  293 ? 0.323   -67.267  -94.298  1.00 50.24  ? 293 SER   F N      1 
ATOM   16555 C  CA     . SER   F 4  293 ? 1.412   -68.139  -94.720  1.00 51.40  ? 293 SER   F CA     1 
ATOM   16556 C  C      . SER   F 4  293 ? 2.718   -67.772  -94.030  1.00 55.93  ? 293 SER   F C      1 
ATOM   16557 O  O      . SER   F 4  293 ? 3.423   -68.649  -93.518  1.00 62.31  ? 293 SER   F O      1 
ATOM   16558 C  CB     . SER   F 4  293 ? 1.557   -68.084  -96.231  1.00 55.40  ? 293 SER   F CB     1 
ATOM   16559 O  OG     . SER   F 4  293 ? 0.337   -68.489  -96.828  1.00 60.72  ? 293 SER   F OG     1 
ATOM   16560 N  N      . CYS   F 4  294 ? 3.060   -66.481  -94.003  1.00 52.88  ? 294 CYS   F N      1 
ATOM   16561 C  CA     . CYS   F 4  294 ? 4.287   -66.057  -93.328  1.00 57.75  ? 294 CYS   F CA     1 
ATOM   16562 C  C      . CYS   F 4  294 ? 4.304   -66.484  -91.863  1.00 60.06  ? 294 CYS   F C      1 
ATOM   16563 O  O      . CYS   F 4  294 ? 5.335   -66.950  -91.351  1.00 54.80  ? 294 CYS   F O      1 
ATOM   16564 C  CB     . CYS   F 4  294 ? 4.456   -64.542  -93.416  1.00 51.71  ? 294 CYS   F CB     1 
ATOM   16565 S  SG     . CYS   F 4  294 ? 4.823   -63.950  -95.034  1.00 66.14  ? 294 CYS   F SG     1 
ATOM   16566 N  N      . LEU   F 4  295 ? 3.184   -66.302  -91.160  1.00 54.65  ? 295 LEU   F N      1 
ATOM   16567 C  CA     . LEU   F 4  295 ? 3.203   -66.563  -89.731  1.00 53.04  ? 295 LEU   F CA     1 
ATOM   16568 C  C      . LEU   F 4  295 ? 3.038   -68.046  -89.425  1.00 52.63  ? 295 LEU   F C      1 
ATOM   16569 O  O      . LEU   F 4  295 ? 3.562   -68.511  -88.412  1.00 56.89  ? 295 LEU   F O      1 
ATOM   16570 C  CB     . LEU   F 4  295 ? 2.143   -65.706  -89.023  1.00 52.53  ? 295 LEU   F CB     1 
ATOM   16571 C  CG     . LEU   F 4  295 ? 2.454   -64.194  -89.109  1.00 49.12  ? 295 LEU   F CG     1 
ATOM   16572 C  CD1    . LEU   F 4  295 ? 1.302   -63.290  -88.666  1.00 44.22  ? 295 LEU   F CD1    1 
ATOM   16573 C  CD2    . LEU   F 4  295 ? 3.733   -63.831  -88.355  1.00 49.17  ? 295 LEU   F CD2    1 
ATOM   16574 N  N      . MET   F 4  296 ? 2.358   -68.815  -90.289  1.00 58.59  ? 296 MET   F N      1 
ATOM   16575 C  CA     . MET   F 4  296 ? 2.368   -70.272  -90.132  1.00 58.36  ? 296 MET   F CA     1 
ATOM   16576 C  C      . MET   F 4  296 ? 3.778   -70.828  -90.307  1.00 60.68  ? 296 MET   F C      1 
ATOM   16577 O  O      . MET   F 4  296 ? 4.179   -71.761  -89.605  1.00 60.93  ? 296 MET   F O      1 
ATOM   16578 C  CB     . MET   F 4  296 ? 1.420   -70.948  -91.125  1.00 55.03  ? 296 MET   F CB     1 
ATOM   16579 C  CG     . MET   F 4  296 ? -0.065  -70.639  -90.964  1.00 58.64  ? 296 MET   F CG     1 
ATOM   16580 S  SD     . MET   F 4  296 ? -0.484  -69.939  -89.358  1.00 86.98  ? 296 MET   F SD     1 
ATOM   16581 C  CE     . MET   F 4  296 ? -0.031  -71.242  -88.204  1.00 68.00  ? 296 MET   F CE     1 
ATOM   16582 N  N      . CYS   F 4  297 ? 4.550   -70.261  -91.235  1.00 60.31  ? 297 CYS   F N      1 
ATOM   16583 C  CA     . CYS   F 4  297 ? 5.915   -70.719  -91.447  1.00 58.23  ? 297 CYS   F CA     1 
ATOM   16584 C  C      . CYS   F 4  297 ? 6.708   -70.719  -90.143  1.00 58.71  ? 297 CYS   F C      1 
ATOM   16585 O  O      . CYS   F 4  297 ? 7.209   -71.764  -89.711  1.00 63.60  ? 297 CYS   F O      1 
ATOM   16586 C  CB     . CYS   F 4  297 ? 6.599   -69.849  -92.508  1.00 63.00  ? 297 CYS   F CB     1 
ATOM   16587 S  SG     . CYS   F 4  297 ? 8.173   -70.527  -93.123  1.00 62.41  ? 297 CYS   F SG     1 
ATOM   16588 N  N      . ILE   F 4  298 ? 6.834   -69.556  -89.495  1.00 51.51  ? 298 ILE   F N      1 
ATOM   16589 C  CA     . ILE   F 4  298 ? 7.755   -69.425  -88.365  1.00 58.72  ? 298 ILE   F CA     1 
ATOM   16590 C  C      . ILE   F 4  298 ? 7.117   -69.805  -87.028  1.00 57.43  ? 298 ILE   F C      1 
ATOM   16591 O  O      . ILE   F 4  298 ? 7.711   -69.572  -85.968  1.00 54.39  ? 298 ILE   F O      1 
ATOM   16592 C  CB     . ILE   F 4  298 ? 8.329   -67.997  -88.265  1.00 60.69  ? 298 ILE   F CB     1 
ATOM   16593 C  CG1    . ILE   F 4  298 ? 7.205   -66.956  -88.313  1.00 56.09  ? 298 ILE   F CG1    1 
ATOM   16594 C  CG2    . ILE   F 4  298 ? 9.363   -67.756  -89.358  1.00 66.83  ? 298 ILE   F CG2    1 
ATOM   16595 C  CD1    . ILE   F 4  298 ? 7.546   -65.684  -87.601  1.00 52.68  ? 298 ILE   F CD1    1 
ATOM   16596 N  N      . GLU   F 4  299 ? 5.915   -70.381  -87.049  1.00 54.33  ? 299 GLU   F N      1 
ATOM   16597 C  CA     . GLU   F 4  299 ? 5.298   -70.765  -85.784  1.00 54.15  ? 299 GLU   F CA     1 
ATOM   16598 C  C      . GLU   F 4  299 ? 6.156   -71.734  -84.967  1.00 54.61  ? 299 GLU   F C      1 
ATOM   16599 O  O      . GLU   F 4  299 ? 6.241   -71.553  -83.739  1.00 53.78  ? 299 GLU   F O      1 
ATOM   16600 C  CB     . GLU   F 4  299 ? 3.899   -71.349  -86.016  1.00 51.79  ? 299 GLU   F CB     1 
ATOM   16601 C  CG     . GLU   F 4  299 ? 3.329   -71.921  -84.732  1.00 50.52  ? 299 GLU   F CG     1 
ATOM   16602 C  CD     . GLU   F 4  299 ? 1.827   -72.059  -84.742  1.00 62.05  ? 299 GLU   F CD     1 
ATOM   16603 O  OE1    . GLU   F 4  299 ? 1.234   -72.030  -85.840  1.00 74.26  ? 299 GLU   F OE1    1 
ATOM   16604 O  OE2    . GLU   F 4  299 ? 1.223   -72.177  -83.648  1.00 65.21  ? 299 GLU   F OE2    1 
ATOM   16605 N  N      . PRO   F 4  300 ? 6.798   -72.755  -85.541  1.00 57.15  ? 300 PRO   F N      1 
ATOM   16606 C  CA     . PRO   F 4  300 ? 7.631   -73.633  -84.698  1.00 55.54  ? 300 PRO   F CA     1 
ATOM   16607 C  C      . PRO   F 4  300 ? 8.822   -72.920  -84.085  1.00 47.42  ? 300 PRO   F C      1 
ATOM   16608 O  O      . PRO   F 4  300 ? 9.305   -73.332  -83.026  1.00 50.71  ? 300 PRO   F O      1 
ATOM   16609 C  CB     . PRO   F 4  300 ? 8.072   -74.746  -85.666  1.00 53.56  ? 300 PRO   F CB     1 
ATOM   16610 C  CG     . PRO   F 4  300 ? 7.074   -74.706  -86.758  1.00 56.93  ? 300 PRO   F CG     1 
ATOM   16611 C  CD     . PRO   F 4  300 ? 6.715   -73.254  -86.921  1.00 53.52  ? 300 PRO   F CD     1 
ATOM   16612 N  N      . ALA   F 4  301 ? 9.318   -71.861  -84.715  1.00 47.75  ? 301 ALA   F N      1 
ATOM   16613 C  CA     . ALA   F 4  301 ? 10.504  -71.188  -84.209  1.00 47.59  ? 301 ALA   F CA     1 
ATOM   16614 C  C      . ALA   F 4  301 ? 10.195  -70.199  -83.087  1.00 51.56  ? 301 ALA   F C      1 
ATOM   16615 O  O      . ALA   F 4  301 ? 11.088  -69.908  -82.268  1.00 52.65  ? 301 ALA   F O      1 
ATOM   16616 C  CB     . ALA   F 4  301 ? 11.229  -70.481  -85.356  1.00 40.56  ? 301 ALA   F CB     1 
ATOM   16617 N  N      . ILE   F 4  302 ? 8.964   -69.689  -83.004  1.00 47.02  ? 302 ILE   F N      1 
ATOM   16618 C  CA     . ILE   F 4  302 ? 8.684   -68.593  -82.088  1.00 50.26  ? 302 ILE   F CA     1 
ATOM   16619 C  C      . ILE   F 4  302 ? 7.499   -68.840  -81.170  1.00 46.42  ? 302 ILE   F C      1 
ATOM   16620 O  O      . ILE   F 4  302 ? 7.239   -68.022  -80.280  1.00 49.37  ? 302 ILE   F O      1 
ATOM   16621 C  CB     . ILE   F 4  302 ? 8.497   -67.277  -82.857  1.00 49.43  ? 302 ILE   F CB     1 
ATOM   16622 C  CG1    . ILE   F 4  302 ? 7.141   -67.256  -83.537  1.00 48.57  ? 302 ILE   F CG1    1 
ATOM   16623 C  CG2    . ILE   F 4  302 ? 9.595   -67.110  -83.855  1.00 44.42  ? 302 ILE   F CG2    1 
ATOM   16624 C  CD1    . ILE   F 4  302 ? 6.792   -65.907  -84.095  1.00 45.94  ? 302 ILE   F CD1    1 
ATOM   16625 N  N      . SER   F 4  303 ? 6.773   -69.936  -81.330  1.00 48.60  ? 303 SER   F N      1 
ATOM   16626 C  CA     . SER   F 4  303 ? 5.640   -70.177  -80.446  1.00 47.36  ? 303 SER   F CA     1 
ATOM   16627 C  C      . SER   F 4  303 ? 6.089   -70.200  -78.979  1.00 48.67  ? 303 SER   F C      1 
ATOM   16628 O  O      . SER   F 4  303 ? 7.140   -70.758  -78.639  1.00 43.98  ? 303 SER   F O      1 
ATOM   16629 C  CB     . SER   F 4  303 ? 4.962   -71.487  -80.823  1.00 44.30  ? 303 SER   F CB     1 
ATOM   16630 O  OG     . SER   F 4  303 ? 3.967   -71.843  -79.874  1.00 53.13  ? 303 SER   F OG     1 
ATOM   16631 N  N      . THR   F 4  304 ? 5.296   -69.572  -78.108  1.00 45.51  ? 304 THR   F N      1 
ATOM   16632 C  CA     . THR   F 4  304 ? 5.505   -69.629  -76.661  1.00 50.50  ? 304 THR   F CA     1 
ATOM   16633 C  C      . THR   F 4  304 ? 4.440   -70.495  -75.974  1.00 55.36  ? 304 THR   F C      1 
ATOM   16634 O  O      . THR   F 4  304 ? 3.994   -70.199  -74.864  1.00 57.13  ? 304 THR   F O      1 
ATOM   16635 C  CB     . THR   F 4  304 ? 5.558   -68.216  -76.057  1.00 50.36  ? 304 THR   F CB     1 
ATOM   16636 O  OG1    . THR   F 4  304 ? 4.242   -67.674  -75.910  1.00 48.17  ? 304 THR   F OG1    1 
ATOM   16637 C  CG2    . THR   F 4  304 ? 6.412   -67.267  -76.916  1.00 41.41  ? 304 THR   F CG2    1 
ATOM   16638 N  N      . LYS   F 4  305 ? 4.055   -71.605  -76.626  1.00 58.99  ? 305 LYS   F N      1 
ATOM   16639 C  CA     . LYS   F 4  305 ? 2.952   -72.452  -76.167  1.00 54.77  ? 305 LYS   F CA     1 
ATOM   16640 C  C      . LYS   F 4  305 ? 3.301   -73.213  -74.896  1.00 56.56  ? 305 LYS   F C      1 
ATOM   16641 O  O      . LYS   F 4  305 ? 2.465   -73.328  -73.994  1.00 60.82  ? 305 LYS   F O      1 
ATOM   16642 C  CB     . LYS   F 4  305 ? 2.561   -73.444  -77.264  1.00 61.57  ? 305 LYS   F CB     1 
ATOM   16643 C  CG     . LYS   F 4  305 ? 1.124   -73.957  -77.194  1.00 66.82  ? 305 LYS   F CG     1 
ATOM   16644 C  CD     . LYS   F 4  305 ? 0.110   -72.843  -77.543  1.00 69.78  ? 305 LYS   F CD     1 
ATOM   16645 C  CE     . LYS   F 4  305 ? 0.191   -72.454  -79.037  1.00 74.10  ? 305 LYS   F CE     1 
ATOM   16646 N  NZ     . LYS   F 4  305 ? -1.082  -71.945  -79.634  1.00 73.73  ? 305 LYS   F NZ     1 
ATOM   16647 N  N      . HIS   F 4  306 ? 4.502   -73.782  -74.813  1.00 57.14  ? 306 HIS   F N      1 
ATOM   16648 C  CA     . HIS   F 4  306 ? 4.925   -74.453  -73.590  1.00 61.61  ? 306 HIS   F CA     1 
ATOM   16649 C  C      . HIS   F 4  306 ? 6.012   -73.692  -72.853  1.00 57.16  ? 306 HIS   F C      1 
ATOM   16650 O  O      . HIS   F 4  306 ? 6.579   -74.219  -71.892  1.00 57.52  ? 306 HIS   F O      1 
ATOM   16651 C  CB     . HIS   F 4  306 ? 5.397   -75.874  -73.897  1.00 71.48  ? 306 HIS   F CB     1 
ATOM   16652 C  CG     . HIS   F 4  306 ? 4.459   -76.631  -74.779  1.00 75.54  ? 306 HIS   F CG     1 
ATOM   16653 N  ND1    . HIS   F 4  306 ? 3.178   -76.962  -74.385  1.00 73.01  ? 306 HIS   F ND1    1 
ATOM   16654 C  CD2    . HIS   F 4  306 ? 4.617   -77.139  -76.025  1.00 79.08  ? 306 HIS   F CD2    1 
ATOM   16655 C  CE1    . HIS   F 4  306 ? 2.579   -77.625  -75.358  1.00 79.93  ? 306 HIS   F CE1    1 
ATOM   16656 N  NE2    . HIS   F 4  306 ? 3.432   -77.750  -76.362  1.00 90.28  ? 306 HIS   F NE2    1 
ATOM   16657 N  N      . LEU   F 4  307 ? 6.324   -72.476  -73.293  1.00 55.41  ? 307 LEU   F N      1 
ATOM   16658 C  CA     . LEU   F 4  307 ? 7.410   -71.697  -72.732  1.00 50.63  ? 307 LEU   F CA     1 
ATOM   16659 C  C      . LEU   F 4  307 ? 7.032   -71.177  -71.348  1.00 49.35  ? 307 LEU   F C      1 
ATOM   16660 O  O      . LEU   F 4  307 ? 5.860   -71.158  -70.960  1.00 45.73  ? 307 LEU   F O      1 
ATOM   16661 C  CB     . LEU   F 4  307 ? 7.759   -70.539  -73.664  1.00 49.43  ? 307 LEU   F CB     1 
ATOM   16662 C  CG     . LEU   F 4  307 ? 9.079   -70.570  -74.436  1.00 45.26  ? 307 LEU   F CG     1 
ATOM   16663 C  CD1    . LEU   F 4  307 ? 9.448   -69.171  -74.867  1.00 46.52  ? 307 LEU   F CD1    1 
ATOM   16664 C  CD2    . LEU   F 4  307 ? 10.200  -71.183  -73.633  1.00 45.91  ? 307 LEU   F CD2    1 
ATOM   16665 N  N      . HIS   F 4  308 ? 8.063   -70.757  -70.595  1.00 49.63  ? 308 HIS   F N      1 
ATOM   16666 C  CA     . HIS   F 4  308 ? 7.908   -70.257  -69.229  1.00 46.82  ? 308 HIS   F CA     1 
ATOM   16667 C  C      . HIS   F 4  308 ? 7.500   -68.787  -69.162  1.00 46.60  ? 308 HIS   F C      1 
ATOM   16668 O  O      . HIS   F 4  308 ? 7.095   -68.318  -68.094  1.00 50.73  ? 308 HIS   F O      1 
ATOM   16669 C  CB     . HIS   F 4  308 ? 9.205   -70.458  -68.441  1.00 41.89  ? 308 HIS   F CB     1 
ATOM   16670 C  CG     . HIS   F 4  308 ? 10.454  -70.197  -69.232  1.00 47.67  ? 308 HIS   F CG     1 
ATOM   16671 N  ND1    . HIS   F 4  308 ? 10.924  -71.069  -70.196  1.00 47.45  ? 308 HIS   F ND1    1 
ATOM   16672 C  CD2    . HIS   F 4  308 ? 11.350  -69.181  -69.176  1.00 43.95  ? 308 HIS   F CD2    1 
ATOM   16673 C  CE1    . HIS   F 4  308 ? 12.045  -70.594  -70.709  1.00 45.57  ? 308 HIS   F CE1    1 
ATOM   16674 N  NE2    . HIS   F 4  308 ? 12.323  -69.449  -70.112  1.00 52.85  ? 308 HIS   F NE2    1 
ATOM   16675 N  N      . TYR   F 4  309 ? 7.637   -68.049  -70.256  1.00 41.63  ? 309 TYR   F N      1 
ATOM   16676 C  CA     . TYR   F 4  309 ? 7.033   -66.745  -70.452  1.00 44.66  ? 309 TYR   F CA     1 
ATOM   16677 C  C      . TYR   F 4  309 ? 6.266   -66.794  -71.766  1.00 49.70  ? 309 TYR   F C      1 
ATOM   16678 O  O      . TYR   F 4  309 ? 6.319   -67.790  -72.502  1.00 48.05  ? 309 TYR   F O      1 
ATOM   16679 C  CB     . TYR   F 4  309 ? 8.086   -65.635  -70.490  1.00 50.15  ? 309 TYR   F CB     1 
ATOM   16680 C  CG     . TYR   F 4  309 ? 8.872   -65.637  -71.779  1.00 48.92  ? 309 TYR   F CG     1 
ATOM   16681 C  CD1    . TYR   F 4  309 ? 8.408   -64.961  -72.917  1.00 44.45  ? 309 TYR   F CD1    1 
ATOM   16682 C  CD2    . TYR   F 4  309 ? 10.068  -66.330  -71.867  1.00 41.42  ? 309 TYR   F CD2    1 
ATOM   16683 C  CE1    . TYR   F 4  309 ? 9.135   -64.981  -74.094  1.00 45.73  ? 309 TYR   F CE1    1 
ATOM   16684 C  CE2    . TYR   F 4  309 ? 10.790  -66.356  -73.031  1.00 42.21  ? 309 TYR   F CE2    1 
ATOM   16685 C  CZ     . TYR   F 4  309 ? 10.334  -65.687  -74.140  1.00 46.83  ? 309 TYR   F CZ     1 
ATOM   16686 O  OH     . TYR   F 4  309 ? 11.094  -65.741  -75.292  1.00 49.53  ? 309 TYR   F OH     1 
ATOM   16687 N  N      . GLN   F 4  310 ? 5.582   -65.698  -72.091  1.00 47.73  ? 310 GLN   F N      1 
ATOM   16688 C  CA     . GLN   F 4  310 ? 4.722   -65.671  -73.264  1.00 50.03  ? 310 GLN   F CA     1 
ATOM   16689 C  C      . GLN   F 4  310 ? 4.914   -64.389  -74.050  1.00 53.13  ? 310 GLN   F C      1 
ATOM   16690 O  O      . GLN   F 4  310 ? 5.248   -63.332  -73.497  1.00 48.50  ? 310 GLN   F O      1 
ATOM   16691 C  CB     . GLN   F 4  310 ? 3.270   -65.814  -72.901  1.00 44.88  ? 310 GLN   F CB     1 
ATOM   16692 C  CG     . GLN   F 4  310 ? 3.064   -66.932  -71.940  1.00 55.00  ? 310 GLN   F CG     1 
ATOM   16693 C  CD     . GLN   F 4  310 ? 2.076   -67.928  -72.447  1.00 58.40  ? 310 GLN   F CD     1 
ATOM   16694 O  OE1    . GLN   F 4  310 ? 2.287   -68.560  -73.499  1.00 57.44  ? 310 GLN   F OE1    1 
ATOM   16695 N  NE2    . GLN   F 4  310 ? 0.966   -68.081  -71.708  1.00 51.82  ? 310 GLN   F NE2    1 
ATOM   16696 N  N      . SER   F 4  311 ? 4.694   -64.512  -75.358  1.00 49.22  ? 311 SER   F N      1 
ATOM   16697 C  CA     . SER   F 4  311 ? 4.817   -63.417  -76.295  1.00 46.10  ? 311 SER   F CA     1 
ATOM   16698 C  C      . SER   F 4  311 ? 3.479   -63.178  -76.972  1.00 50.17  ? 311 SER   F C      1 
ATOM   16699 O  O      . SER   F 4  311 ? 2.731   -64.120  -77.248  1.00 48.56  ? 311 SER   F O      1 
ATOM   16700 C  CB     . SER   F 4  311 ? 5.877   -63.718  -77.344  1.00 46.47  ? 311 SER   F CB     1 
ATOM   16701 O  OG     . SER   F 4  311 ? 7.141   -63.999  -76.749  1.00 52.83  ? 311 SER   F OG     1 
ATOM   16702 N  N      . PHE   F 4  312 ? 3.159   -61.909  -77.170  1.00 49.32  ? 312 PHE   F N      1 
ATOM   16703 C  CA     . PHE   F 4  312 ? 2.336   -61.472  -78.274  1.00 47.43  ? 312 PHE   F CA     1 
ATOM   16704 C  C      . PHE   F 4  312 ? 3.156   -60.439  -79.031  1.00 50.01  ? 312 PHE   F C      1 
ATOM   16705 O  O      . PHE   F 4  312 ? 4.233   -60.046  -78.593  1.00 51.29  ? 312 PHE   F O      1 
ATOM   16706 C  CB     . PHE   F 4  312 ? 0.984   -60.924  -77.801  1.00 52.03  ? 312 PHE   F CB     1 
ATOM   16707 C  CG     . PHE   F 4  312 ? 1.069   -59.625  -77.062  1.00 57.96  ? 312 PHE   F CG     1 
ATOM   16708 C  CD1    . PHE   F 4  312 ? 1.283   -59.606  -75.690  1.00 59.31  ? 312 PHE   F CD1    1 
ATOM   16709 C  CD2    . PHE   F 4  312 ? 0.890   -58.420  -77.727  1.00 55.94  ? 312 PHE   F CD2    1 
ATOM   16710 C  CE1    . PHE   F 4  312 ? 1.352   -58.407  -75.000  1.00 62.90  ? 312 PHE   F CE1    1 
ATOM   16711 C  CE2    . PHE   F 4  312 ? 0.952   -57.216  -77.041  1.00 57.94  ? 312 PHE   F CE2    1 
ATOM   16712 C  CZ     . PHE   F 4  312 ? 1.188   -57.206  -75.682  1.00 63.17  ? 312 PHE   F CZ     1 
ATOM   16713 N  N      . GLN   F 4  313 ? 2.690   -60.053  -80.212  1.00 53.19  ? 313 GLN   F N      1 
ATOM   16714 C  CA     . GLN   F 4  313 ? 3.384   -59.021  -80.967  1.00 54.56  ? 313 GLN   F CA     1 
ATOM   16715 C  C      . GLN   F 4  313 ? 2.421   -58.464  -81.999  1.00 58.98  ? 313 GLN   F C      1 
ATOM   16716 O  O      . GLN   F 4  313 ? 1.504   -59.158  -82.446  1.00 58.18  ? 313 GLN   F O      1 
ATOM   16717 C  CB     . GLN   F 4  313 ? 4.665   -59.542  -81.635  1.00 49.59  ? 313 GLN   F CB     1 
ATOM   16718 C  CG     . GLN   F 4  313 ? 5.485   -58.441  -82.330  1.00 48.96  ? 313 GLN   F CG     1 
ATOM   16719 C  CD     . GLN   F 4  313 ? 6.855   -58.912  -82.832  1.00 49.83  ? 313 GLN   F CD     1 
ATOM   16720 O  OE1    . GLN   F 4  313 ? 7.327   -59.992  -82.476  1.00 48.01  ? 313 GLN   F OE1    1 
ATOM   16721 N  NE2    . GLN   F 4  313 ? 7.482   -58.107  -83.683  1.00 51.18  ? 313 GLN   F NE2    1 
ATOM   16722 N  N      . LEU   F 4  314 ? 2.610   -57.186  -82.326  1.00 62.82  ? 314 LEU   F N      1 
ATOM   16723 C  CA     . LEU   F 4  314 ? 1.865   -56.504  -83.378  1.00 55.99  ? 314 LEU   F CA     1 
ATOM   16724 C  C      . LEU   F 4  314 ? 2.798   -56.326  -84.562  1.00 53.52  ? 314 LEU   F C      1 
ATOM   16725 O  O      . LEU   F 4  314 ? 3.951   -55.931  -84.385  1.00 60.94  ? 314 LEU   F O      1 
ATOM   16726 C  CB     . LEU   F 4  314 ? 1.329   -55.147  -82.908  1.00 53.67  ? 314 LEU   F CB     1 
ATOM   16727 C  CG     . LEU   F 4  314 ? 0.613   -54.239  -83.919  1.00 63.46  ? 314 LEU   F CG     1 
ATOM   16728 C  CD1    . LEU   F 4  314 ? -0.866  -54.623  -84.061  1.00 61.79  ? 314 LEU   F CD1    1 
ATOM   16729 C  CD2    . LEU   F 4  314 ? 0.745   -52.765  -83.550  1.00 63.58  ? 314 LEU   F CD2    1 
ATOM   16730 N  N      . PHE   F 4  315 ? 2.317   -56.656  -85.755  1.00 55.75  ? 315 PHE   F N      1 
ATOM   16731 C  CA     . PHE   F 4  315 ? 3.096   -56.535  -86.974  1.00 55.00  ? 315 PHE   F CA     1 
ATOM   16732 C  C      . PHE   F 4  315 ? 2.395   -55.579  -87.923  1.00 58.00  ? 315 PHE   F C      1 
ATOM   16733 O  O      . PHE   F 4  315 ? 1.167   -55.454  -87.912  1.00 59.56  ? 315 PHE   F O      1 
ATOM   16734 C  CB     . PHE   F 4  315 ? 3.292   -57.897  -87.661  1.00 50.01  ? 315 PHE   F CB     1 
ATOM   16735 C  CG     . PHE   F 4  315 ? 3.921   -58.930  -86.780  1.00 50.92  ? 315 PHE   F CG     1 
ATOM   16736 C  CD1    . PHE   F 4  315 ? 3.152   -59.670  -85.897  1.00 50.84  ? 315 PHE   F CD1    1 
ATOM   16737 C  CD2    . PHE   F 4  315 ? 5.283   -59.154  -86.820  1.00 52.38  ? 315 PHE   F CD2    1 
ATOM   16738 C  CE1    . PHE   F 4  315 ? 3.732   -60.611  -85.083  1.00 48.34  ? 315 PHE   F CE1    1 
ATOM   16739 C  CE2    . PHE   F 4  315 ? 5.872   -60.089  -86.001  1.00 47.70  ? 315 PHE   F CE2    1 
ATOM   16740 C  CZ     . PHE   F 4  315 ? 5.096   -60.815  -85.130  1.00 48.10  ? 315 PHE   F CZ     1 
ATOM   16741 N  N      . GLY   F 4  316 ? 3.188   -54.890  -88.729  1.00 57.55  ? 316 GLY   F N      1 
ATOM   16742 C  CA     . GLY   F 4  316 ? 2.633   -54.177  -89.850  1.00 59.58  ? 316 GLY   F CA     1 
ATOM   16743 C  C      . GLY   F 4  316 ? 3.072   -54.840  -91.134  1.00 65.78  ? 316 GLY   F C      1 
ATOM   16744 O  O      . GLY   F 4  316 ? 4.274   -54.932  -91.409  1.00 64.85  ? 316 GLY   F O      1 
ATOM   16745 N  N      . PHE   F 4  317 ? 2.116   -55.331  -91.919  1.00 65.56  ? 317 PHE   F N      1 
ATOM   16746 C  CA     . PHE   F 4  317 ? 2.411   -55.942  -93.208  1.00 63.63  ? 317 PHE   F CA     1 
ATOM   16747 C  C      . PHE   F 4  317 ? 2.194   -54.906  -94.301  1.00 68.61  ? 317 PHE   F C      1 
ATOM   16748 O  O      . PHE   F 4  317 ? 1.172   -54.204  -94.298  1.00 66.88  ? 317 PHE   F O      1 
ATOM   16749 C  CB     . PHE   F 4  317 ? 1.531   -57.168  -93.449  1.00 60.38  ? 317 PHE   F CB     1 
ATOM   16750 C  CG     . PHE   F 4  317 ? 1.959   -58.386  -92.676  1.00 63.71  ? 317 PHE   F CG     1 
ATOM   16751 C  CD1    . PHE   F 4  317 ? 1.673   -58.502  -91.322  1.00 59.84  ? 317 PHE   F CD1    1 
ATOM   16752 C  CD2    . PHE   F 4  317 ? 2.649   -59.419  -93.300  1.00 64.28  ? 317 PHE   F CD2    1 
ATOM   16753 C  CE1    . PHE   F 4  317 ? 2.071   -59.623  -90.605  1.00 58.07  ? 317 PHE   F CE1    1 
ATOM   16754 C  CE2    . PHE   F 4  317 ? 3.040   -60.548  -92.592  1.00 57.60  ? 317 PHE   F CE2    1 
ATOM   16755 C  CZ     . PHE   F 4  317 ? 2.755   -60.649  -91.247  1.00 54.64  ? 317 PHE   F CZ     1 
ATOM   16756 N  N      . ASP   F 4  318 ? 3.151   -54.811  -95.229  1.00 64.11  ? 318 ASP   F N      1 
ATOM   16757 C  CA     . ASP   F 4  318 ? 3.141   -53.810  -96.293  1.00 66.12  ? 318 ASP   F CA     1 
ATOM   16758 C  C      . ASP   F 4  318 ? 3.023   -54.515  -97.637  1.00 65.60  ? 318 ASP   F C      1 
ATOM   16759 O  O      . ASP   F 4  318 ? 3.902   -55.308  -97.997  1.00 66.69  ? 318 ASP   F O      1 
ATOM   16760 C  CB     . ASP   F 4  318 ? 4.412   -52.946  -96.261  1.00 71.67  ? 318 ASP   F CB     1 
ATOM   16761 C  CG     . ASP   F 4  318 ? 4.572   -52.134  -94.960  1.00 74.72  ? 318 ASP   F CG     1 
ATOM   16762 O  OD1    . ASP   F 4  318 ? 3.579   -51.906  -94.230  1.00 70.42  ? 318 ASP   F OD1    1 
ATOM   16763 O  OD2    . ASP   F 4  318 ? 5.715   -51.693  -94.688  1.00 83.11  ? 318 ASP   F OD2    1 
ATOM   16764 N  N      . PHE   F 4  319 ? 1.962   -54.199  -98.395  1.00 66.64  ? 319 PHE   F N      1 
ATOM   16765 C  CA     . PHE   F 4  319 ? 1.688   -54.861  -99.669  1.00 69.67  ? 319 PHE   F CA     1 
ATOM   16766 C  C      . PHE   F 4  319 ? 1.675   -53.892  -100.853 1.00 74.09  ? 319 PHE   F C      1 
ATOM   16767 O  O      . PHE   F 4  319 ? 1.398   -52.694  -100.718 1.00 71.82  ? 319 PHE   F O      1 
ATOM   16768 C  CB     . PHE   F 4  319 ? 0.346   -55.611  -99.640  1.00 67.71  ? 319 PHE   F CB     1 
ATOM   16769 C  CG     . PHE   F 4  319 ? 0.236   -56.644  -98.545  1.00 66.35  ? 319 PHE   F CG     1 
ATOM   16770 C  CD1    . PHE   F 4  319 ? 0.688   -57.949  -98.754  1.00 61.98  ? 319 PHE   F CD1    1 
ATOM   16771 C  CD2    . PHE   F 4  319 ? -0.343  -56.320  -97.318  1.00 63.63  ? 319 PHE   F CD2    1 
ATOM   16772 C  CE1    . PHE   F 4  319 ? 0.580   -58.911  -97.757  1.00 60.19  ? 319 PHE   F CE1    1 
ATOM   16773 C  CE2    . PHE   F 4  319 ? -0.459  -57.274  -96.316  1.00 63.93  ? 319 PHE   F CE2    1 
ATOM   16774 C  CZ     . PHE   F 4  319 ? 0.008   -58.574  -96.537  1.00 62.39  ? 319 PHE   F CZ     1 
ATOM   16775 N  N      . MET   F 4  320 ? 1.955   -54.464  -102.028 1.00 77.89  ? 320 MET   F N      1 
ATOM   16776 C  CA     . MET   F 4  320 ? 1.970   -53.785  -103.324 1.00 75.95  ? 320 MET   F CA     1 
ATOM   16777 C  C      . MET   F 4  320 ? 0.959   -54.481  -104.234 1.00 73.89  ? 320 MET   F C      1 
ATOM   16778 O  O      . MET   F 4  320 ? 1.099   -55.678  -104.509 1.00 73.08  ? 320 MET   F O      1 
ATOM   16779 C  CB     . MET   F 4  320 ? 3.383   -53.844  -103.934 1.00 77.98  ? 320 MET   F CB     1 
ATOM   16780 C  CG     . MET   F 4  320 ? 3.791   -52.694  -104.855 1.00 84.21  ? 320 MET   F CG     1 
ATOM   16781 S  SD     . MET   F 4  320 ? 3.017   -51.110  -104.455 1.00 99.29  ? 320 MET   F SD     1 
ATOM   16782 C  CE     . MET   F 4  320 ? 4.092   -50.488  -103.164 1.00 88.35  ? 320 MET   F CE     1 
ATOM   16783 N  N      . VAL   F 4  321 ? -0.064  -53.754  -104.683 1.00 73.59  ? 321 VAL   F N      1 
ATOM   16784 C  CA     . VAL   F 4  321 ? -1.062  -54.297  -105.603 1.00 68.45  ? 321 VAL   F CA     1 
ATOM   16785 C  C      . VAL   F 4  321 ? -0.681  -53.885  -107.015 1.00 71.42  ? 321 VAL   F C      1 
ATOM   16786 O  O      . VAL   F 4  321 ? -0.588  -52.689  -107.306 1.00 80.03  ? 321 VAL   F O      1 
ATOM   16787 C  CB     . VAL   F 4  321 ? -2.478  -53.806  -105.269 1.00 68.83  ? 321 VAL   F CB     1 
ATOM   16788 C  CG1    . VAL   F 4  321 ? -3.479  -54.522  -106.150 1.00 71.60  ? 321 VAL   F CG1    1 
ATOM   16789 C  CG2    . VAL   F 4  321 ? -2.804  -54.023  -103.810 1.00 63.49  ? 321 VAL   F CG2    1 
ATOM   16790 N  N      . ASP   F 4  322 ? -0.476  -54.858  -107.902 1.00 70.77  ? 322 ASP   F N      1 
ATOM   16791 C  CA     . ASP   F 4  322 ? -0.115  -54.533  -109.277 1.00 72.35  ? 322 ASP   F CA     1 
ATOM   16792 C  C      . ASP   F 4  322 ? -1.371  -54.282  -110.129 1.00 75.47  ? 322 ASP   F C      1 
ATOM   16793 O  O      . ASP   F 4  322 ? -2.507  -54.281  -109.641 1.00 71.31  ? 322 ASP   F O      1 
ATOM   16794 C  CB     . ASP   F 4  322 ? 0.800   -55.619  -109.867 1.00 68.74  ? 322 ASP   F CB     1 
ATOM   16795 C  CG     . ASP   F 4  322 ? 0.063   -56.907  -110.264 1.00 66.69  ? 322 ASP   F CG     1 
ATOM   16796 O  OD1    . ASP   F 4  322 ? -1.184  -56.955  -110.271 1.00 67.74  ? 322 ASP   F OD1    1 
ATOM   16797 O  OD2    . ASP   F 4  322 ? 0.757   -57.888  -110.592 1.00 60.01  ? 322 ASP   F OD2    1 
ATOM   16798 N  N      . GLU   F 4  323 ? -1.152  -54.053  -111.433 1.00 79.22  ? 323 GLU   F N      1 
ATOM   16799 C  CA     . GLU   F 4  323 ? -2.230  -53.639  -112.336 1.00 79.81  ? 323 GLU   F CA     1 
ATOM   16800 C  C      . GLU   F 4  323 ? -3.249  -54.749  -112.572 1.00 76.10  ? 323 GLU   F C      1 
ATOM   16801 O  O      . GLU   F 4  323 ? -4.430  -54.466  -112.805 1.00 70.81  ? 323 GLU   F O      1 
ATOM   16802 C  CB     . GLU   F 4  323 ? -1.640  -53.192  -113.672 1.00 84.09  ? 323 GLU   F CB     1 
ATOM   16803 C  CG     . GLU   F 4  323 ? -2.302  -51.981  -114.310 1.00 88.85  ? 323 GLU   F CG     1 
ATOM   16804 C  CD     . GLU   F 4  323 ? -1.691  -51.660  -115.664 1.00 99.52  ? 323 GLU   F CD     1 
ATOM   16805 O  OE1    . GLU   F 4  323 ? -0.994  -52.545  -116.215 1.00 100.43 ? 323 GLU   F OE1    1 
ATOM   16806 O  OE2    . GLU   F 4  323 ? -1.901  -50.533  -116.173 1.00 103.40 ? 323 GLU   F OE2    1 
ATOM   16807 N  N      . GLU   F 4  324 ? -2.810  -56.008  -112.541 1.00 78.06  ? 324 GLU   F N      1 
ATOM   16808 C  CA     . GLU   F 4  324 ? -3.682  -57.168  -112.672 1.00 72.70  ? 324 GLU   F CA     1 
ATOM   16809 C  C      . GLU   F 4  324 ? -4.439  -57.485  -111.390 1.00 65.20  ? 324 GLU   F C      1 
ATOM   16810 O  O      . GLU   F 4  324 ? -5.102  -58.522  -111.318 1.00 65.10  ? 324 GLU   F O      1 
ATOM   16811 C  CB     . GLU   F 4  324 ? -2.861  -58.384  -113.104 1.00 74.05  ? 324 GLU   F CB     1 
ATOM   16812 C  CG     . GLU   F 4  324 ? -1.913  -58.094  -114.252 1.00 76.68  ? 324 GLU   F CG     1 
ATOM   16813 C  CD     . GLU   F 4  324 ? -2.022  -59.109  -115.375 1.00 90.52  ? 324 GLU   F CD     1 
ATOM   16814 O  OE1    . GLU   F 4  324 ? -1.315  -60.145  -115.323 1.00 86.25  ? 324 GLU   F OE1    1 
ATOM   16815 O  OE2    . GLU   F 4  324 ? -2.823  -58.868  -116.310 1.00 96.92  ? 324 GLU   F OE2    1 
ATOM   16816 N  N      . LEU   F 4  325 ? -4.364  -56.619  -110.382 1.00 65.62  ? 325 LEU   F N      1 
ATOM   16817 C  CA     . LEU   F 4  325 ? -5.033  -56.862  -109.109 1.00 66.94  ? 325 LEU   F CA     1 
ATOM   16818 C  C      . LEU   F 4  325 ? -4.431  -58.075  -108.402 1.00 66.76  ? 325 LEU   F C      1 
ATOM   16819 O  O      . LEU   F 4  325 ? -5.138  -58.948  -107.892 1.00 61.38  ? 325 LEU   F O      1 
ATOM   16820 C  CB     . LEU   F 4  325 ? -6.535  -57.022  -109.302 1.00 56.88  ? 325 LEU   F CB     1 
ATOM   16821 C  CG     . LEU   F 4  325 ? -7.271  -55.697  -109.268 1.00 60.31  ? 325 LEU   F CG     1 
ATOM   16822 C  CD1    . LEU   F 4  325 ? -8.712  -55.901  -109.695 1.00 63.51  ? 325 LEU   F CD1    1 
ATOM   16823 C  CD2    . LEU   F 4  325 ? -7.191  -55.060  -107.883 1.00 58.48  ? 325 LEU   F CD2    1 
ATOM   16824 N  N      . LYS   F 4  326 ? -3.107  -58.129  -108.396 1.00 64.62  ? 326 LYS   F N      1 
ATOM   16825 C  CA     . LYS   F 4  326 ? -2.344  -59.141  -107.692 1.00 62.79  ? 326 LYS   F CA     1 
ATOM   16826 C  C      . LYS   F 4  326 ? -1.611  -58.468  -106.546 1.00 67.12  ? 326 LYS   F C      1 
ATOM   16827 O  O      . LYS   F 4  326 ? -1.039  -57.387  -106.723 1.00 67.74  ? 326 LYS   F O      1 
ATOM   16828 C  CB     . LYS   F 4  326 ? -1.347  -59.823  -108.627 1.00 62.74  ? 326 LYS   F CB     1 
ATOM   16829 C  CG     . LYS   F 4  326 ? -0.177  -60.467  -107.921 1.00 63.27  ? 326 LYS   F CG     1 
ATOM   16830 C  CD     . LYS   F 4  326 ? 0.122   -61.837  -108.492 1.00 64.91  ? 326 LYS   F CD     1 
ATOM   16831 C  CE     . LYS   F 4  326 ? 1.587   -62.197  -108.303 1.00 68.15  ? 326 LYS   F CE     1 
ATOM   16832 N  NZ     . LYS   F 4  326 ? 1.899   -63.618  -108.656 1.00 67.05  ? 326 LYS   F NZ     1 
ATOM   16833 N  N      . VAL   F 4  327 ? -1.645  -59.100  -105.364 1.00 67.22  ? 327 VAL   F N      1 
ATOM   16834 C  CA     . VAL   F 4  327 ? -1.087  -58.520  -104.145 1.00 65.40  ? 327 VAL   F CA     1 
ATOM   16835 C  C      . VAL   F 4  327 ? 0.322   -59.043  -103.931 1.00 63.83  ? 327 VAL   F C      1 
ATOM   16836 O  O      . VAL   F 4  327 ? 0.605   -60.227  -104.145 1.00 67.10  ? 327 VAL   F O      1 
ATOM   16837 C  CB     . VAL   F 4  327 ? -1.973  -58.811  -102.924 1.00 60.56  ? 327 VAL   F CB     1 
ATOM   16838 C  CG1    . VAL   F 4  327 ? -1.334  -58.215  -101.671 1.00 55.27  ? 327 VAL   F CG1    1 
ATOM   16839 C  CG2    . VAL   F 4  327 ? -3.400  -58.266  -103.159 1.00 57.00  ? 327 VAL   F CG2    1 
ATOM   16840 N  N      . TRP   F 4  328 ? 1.214   -58.159  -103.513 1.00 66.51  ? 328 TRP   F N      1 
ATOM   16841 C  CA     . TRP   F 4  328 ? 2.611   -58.510  -103.327 1.00 69.44  ? 328 TRP   F CA     1 
ATOM   16842 C  C      . TRP   F 4  328 ? 3.052   -58.087  -101.931 1.00 69.74  ? 328 TRP   F C      1 
ATOM   16843 O  O      . TRP   F 4  328 ? 2.635   -57.040  -101.423 1.00 66.54  ? 328 TRP   F O      1 
ATOM   16844 C  CB     . TRP   F 4  328 ? 3.516   -57.844  -104.400 1.00 72.40  ? 328 TRP   F CB     1 
ATOM   16845 C  CG     . TRP   F 4  328 ? 3.226   -58.232  -105.841 1.00 72.28  ? 328 TRP   F CG     1 
ATOM   16846 C  CD1    . TRP   F 4  328 ? 2.248   -57.717  -106.656 1.00 71.63  ? 328 TRP   F CD1    1 
ATOM   16847 C  CD2    . TRP   F 4  328 ? 3.938   -59.191  -106.637 1.00 71.97  ? 328 TRP   F CD2    1 
ATOM   16848 N  NE1    . TRP   F 4  328 ? 2.306   -58.305  -107.902 1.00 66.85  ? 328 TRP   F NE1    1 
ATOM   16849 C  CE2    . TRP   F 4  328 ? 3.330   -59.213  -107.914 1.00 65.27  ? 328 TRP   F CE2    1 
ATOM   16850 C  CE3    . TRP   F 4  328 ? 5.024   -60.036  -106.393 1.00 71.10  ? 328 TRP   F CE3    1 
ATOM   16851 C  CZ2    . TRP   F 4  328 ? 3.770   -60.048  -108.934 1.00 63.64  ? 328 TRP   F CZ2    1 
ATOM   16852 C  CZ3    . TRP   F 4  328 ? 5.459   -60.864  -107.408 1.00 70.42  ? 328 TRP   F CZ3    1 
ATOM   16853 C  CH2    . TRP   F 4  328 ? 4.831   -60.868  -108.663 1.00 66.59  ? 328 TRP   F CH2    1 
ATOM   16854 N  N      . LEU   F 4  329 ? 3.896   -58.905  -101.316 1.00 70.39  ? 329 LEU   F N      1 
ATOM   16855 C  CA     . LEU   F 4  329 ? 4.453   -58.611  -100.006 1.00 71.39  ? 329 LEU   F CA     1 
ATOM   16856 C  C      . LEU   F 4  329 ? 5.813   -57.952  -100.187 1.00 74.54  ? 329 LEU   F C      1 
ATOM   16857 O  O      . LEU   F 4  329 ? 6.715   -58.532  -100.802 1.00 77.64  ? 329 LEU   F O      1 
ATOM   16858 C  CB     . LEU   F 4  329 ? 4.577   -59.881  -99.161  1.00 69.26  ? 329 LEU   F CB     1 
ATOM   16859 C  CG     . LEU   F 4  329 ? 5.446   -59.740  -97.910  1.00 62.85  ? 329 LEU   F CG     1 
ATOM   16860 C  CD1    . LEU   F 4  329 ? 4.768   -58.828  -96.898  1.00 63.57  ? 329 LEU   F CD1    1 
ATOM   16861 C  CD2    . LEU   F 4  329 ? 5.729   -61.094  -97.312  1.00 62.82  ? 329 LEU   F CD2    1 
ATOM   16862 N  N      . ILE   F 4  330 ? 5.964   -56.751  -99.640  1.00 75.99  ? 330 ILE   F N      1 
ATOM   16863 C  CA     . ILE   F 4  330 ? 7.226   -56.032  -99.745  1.00 76.69  ? 330 ILE   F CA     1 
ATOM   16864 C  C      . ILE   F 4  330 ? 8.043   -56.233  -98.475  1.00 74.45  ? 330 ILE   F C      1 
ATOM   16865 O  O      . ILE   F 4  330 ? 9.031   -56.973  -98.473  1.00 75.35  ? 330 ILE   F O      1 
ATOM   16866 C  CB     . ILE   F 4  330 ? 6.976   -54.540  -100.017 1.00 80.65  ? 330 ILE   F CB     1 
ATOM   16867 C  CG1    . ILE   F 4  330 ? 5.913   -54.390  -101.107 1.00 75.13  ? 330 ILE   F CG1    1 
ATOM   16868 C  CG2    . ILE   F 4  330 ? 8.279   -53.853  -100.385 1.00 88.74  ? 330 ILE   F CG2    1 
ATOM   16869 C  CD1    . ILE   F 4  330 ? 6.361   -54.922  -102.458 1.00 82.53  ? 330 ILE   F CD1    1 
ATOM   16870 N  N      . GLU   F 4  331 ? 7.626   -55.578  -97.391  1.00 74.00  ? 331 GLU   F N      1 
ATOM   16871 C  CA     . GLU   F 4  331 ? 8.326   -55.565  -96.111  1.00 80.99  ? 331 GLU   F CA     1 
ATOM   16872 C  C      . GLU   F 4  331 ? 7.359   -56.040  -95.026  1.00 79.17  ? 331 GLU   F C      1 
ATOM   16873 O  O      . GLU   F 4  331 ? 6.154   -55.781  -95.112  1.00 72.89  ? 331 GLU   F O      1 
ATOM   16874 C  CB     . GLU   F 4  331 ? 8.869   -54.125  -95.806  1.00 79.03  ? 331 GLU   F CB     1 
ATOM   16875 C  CG     . GLU   F 4  331 ? 9.632   -53.901  -94.483  1.00 82.16  ? 331 GLU   F CG     1 
ATOM   16876 C  CD     . GLU   F 4  331 ? 9.484   -52.471  -93.935  1.00 91.04  ? 331 GLU   F CD     1 
ATOM   16877 O  OE1    . GLU   F 4  331 ? 8.540   -51.764  -94.351  1.00 91.47  ? 331 GLU   F OE1    1 
ATOM   16878 O  OE2    . GLU   F 4  331 ? 10.307  -52.051  -93.085  1.00 92.49  ? 331 GLU   F OE2    1 
ATOM   16879 N  N      . VAL   F 4  332 ? 7.870   -56.769  -94.029  1.00 73.52  ? 332 VAL   F N      1 
ATOM   16880 C  CA     . VAL   F 4  332 ? 7.127   -57.056  -92.799  1.00 74.30  ? 332 VAL   F CA     1 
ATOM   16881 C  C      . VAL   F 4  332 ? 7.791   -56.292  -91.666  1.00 71.28  ? 332 VAL   F C      1 
ATOM   16882 O  O      . VAL   F 4  332 ? 8.954   -56.552  -91.336  1.00 72.68  ? 332 VAL   F O      1 
ATOM   16883 C  CB     . VAL   F 4  332 ? 7.075   -58.557  -92.475  1.00 71.52  ? 332 VAL   F CB     1 
ATOM   16884 C  CG1    . VAL   F 4  332 ? 5.910   -58.849  -91.518  1.00 60.86  ? 332 VAL   F CG1    1 
ATOM   16885 C  CG2    . VAL   F 4  332 ? 6.989   -59.393  -93.754  1.00 68.49  ? 332 VAL   F CG2    1 
ATOM   16886 N  N      . ASN   F 4  333 ? 7.056   -55.364  -91.059  1.00 71.16  ? 333 ASN   F N      1 
ATOM   16887 C  CA     . ASN   F 4  333 ? 7.621   -54.448  -90.077  1.00 71.73  ? 333 ASN   F CA     1 
ATOM   16888 C  C      . ASN   F 4  333 ? 7.263   -54.925  -88.673  1.00 67.83  ? 333 ASN   F C      1 
ATOM   16889 O  O      . ASN   F 4  333 ? 6.079   -55.070  -88.340  1.00 64.75  ? 333 ASN   F O      1 
ATOM   16890 C  CB     . ASN   F 4  333 ? 7.134   -53.015  -90.322  1.00 72.84  ? 333 ASN   F CB     1 
ATOM   16891 C  CG     . ASN   F 4  333 ? 7.612   -52.033  -89.239  1.00 83.14  ? 333 ASN   F CG     1 
ATOM   16892 O  OD1    . ASN   F 4  333 ? 6.810   -51.508  -88.459  1.00 81.18  ? 333 ASN   F OD1    1 
ATOM   16893 N  ND2    . ASN   F 4  333 ? 8.924   -51.790  -89.187  1.00 85.50  ? 333 ASN   F ND2    1 
ATOM   16894 N  N      . GLY   F 4  334 ? 8.291   -55.154  -87.850  1.00 69.88  ? 334 GLY   F N      1 
ATOM   16895 C  CA     . GLY   F 4  334 ? 8.127   -55.689  -86.503  1.00 70.68  ? 334 GLY   F CA     1 
ATOM   16896 C  C      . GLY   F 4  334 ? 7.837   -54.679  -85.410  1.00 74.34  ? 334 GLY   F C      1 
ATOM   16897 O  O      . GLY   F 4  334 ? 7.435   -55.076  -84.307  1.00 65.21  ? 334 GLY   F O      1 
ATOM   16898 N  N      . ALA   F 4  335 ? 8.038   -53.385  -85.683  1.00 80.98  ? 335 ALA   F N      1 
ATOM   16899 C  CA     . ALA   F 4  335 ? 7.819   -52.307  -84.711  1.00 79.42  ? 335 ALA   F CA     1 
ATOM   16900 C  C      . ALA   F 4  335 ? 6.970   -51.222  -85.368  1.00 74.18  ? 335 ALA   F C      1 
ATOM   16901 O  O      . ALA   F 4  335 ? 7.454   -50.132  -85.697  1.00 77.43  ? 335 ALA   F O      1 
ATOM   16902 C  CB     . ALA   F 4  335 ? 9.149   -51.748  -84.198  1.00 73.40  ? 335 ALA   F CB     1 
ATOM   16903 N  N      . PRO   F 4  336 ? 5.684   -51.495  -85.568  1.00 73.84  ? 336 PRO   F N      1 
ATOM   16904 C  CA     . PRO   F 4  336 ? 4.878   -50.696  -86.490  1.00 76.87  ? 336 PRO   F CA     1 
ATOM   16905 C  C      . PRO   F 4  336 ? 4.144   -49.559  -85.804  1.00 79.55  ? 336 PRO   F C      1 
ATOM   16906 O  O      . PRO   F 4  336 ? 3.590   -49.703  -84.711  1.00 77.28  ? 336 PRO   F O      1 
ATOM   16907 C  CB     . PRO   F 4  336 ? 3.867   -51.721  -87.017  1.00 69.14  ? 336 PRO   F CB     1 
ATOM   16908 C  CG     . PRO   F 4  336 ? 3.768   -52.751  -85.931  1.00 66.95  ? 336 PRO   F CG     1 
ATOM   16909 C  CD     . PRO   F 4  336 ? 4.868   -52.526  -84.921  1.00 74.22  ? 336 PRO   F CD     1 
ATOM   16910 N  N      . ALA   F 4  337 ? 4.130   -48.416  -86.489  1.00 79.52  ? 337 ALA   F N      1 
ATOM   16911 C  CA     . ALA   F 4  337 ? 3.329   -47.276  -86.081  1.00 72.42  ? 337 ALA   F CA     1 
ATOM   16912 C  C      . ALA   F 4  337 ? 1.958   -47.396  -86.716  1.00 75.66  ? 337 ALA   F C      1 
ATOM   16913 O  O      . ALA   F 4  337 ? 1.840   -47.817  -87.870  1.00 81.56  ? 337 ALA   F O      1 
ATOM   16914 C  CB     . ALA   F 4  337 ? 3.995   -45.968  -86.503  1.00 72.79  ? 337 ALA   F CB     1 
ATOM   16915 N  N      . CYS   F 4  338 ? 0.922   -47.057  -85.954  1.00 71.94  ? 338 CYS   F N      1 
ATOM   16916 C  CA     . CYS   F 4  338 ? -0.431  -47.030  -86.491  1.00 72.33  ? 338 CYS   F CA     1 
ATOM   16917 C  C      . CYS   F 4  338 ? -0.730  -45.658  -87.090  1.00 82.96  ? 338 CYS   F C      1 
ATOM   16918 O  O      . CYS   F 4  338 ? 0.030   -44.706  -86.916  1.00 92.61  ? 338 CYS   F O      1 
ATOM   16919 C  CB     . CYS   F 4  338 ? -1.453  -47.366  -85.410  1.00 71.81  ? 338 CYS   F CB     1 
ATOM   16920 S  SG     . CYS   F 4  338 ? -3.174  -47.340  -85.983  1.00 86.20  ? 338 CYS   F SG     1 
ATOM   16921 N  N      . ALA   F 4  339 ? -1.848  -45.561  -87.814  1.00 85.12  ? 339 ALA   F N      1 
ATOM   16922 C  CA     . ALA   F 4  339 ? -2.303  -44.288  -88.364  1.00 83.83  ? 339 ALA   F CA     1 
ATOM   16923 C  C      . ALA   F 4  339 ? -3.264  -43.635  -87.379  1.00 82.74  ? 339 ALA   F C      1 
ATOM   16924 O  O      . ALA   F 4  339 ? -4.133  -44.306  -86.811  1.00 78.24  ? 339 ALA   F O      1 
ATOM   16925 C  CB     . ALA   F 4  339 ? -2.975  -44.482  -89.727  1.00 84.61  ? 339 ALA   F CB     1 
ATOM   16926 N  N      . GLN   F 4  340 ? -3.110  -42.313  -87.202  1.00 83.41  ? 340 GLN   F N      1 
ATOM   16927 C  CA     . GLN   F 4  340 ? -3.690  -41.624  -86.050  1.00 80.57  ? 340 GLN   F CA     1 
ATOM   16928 C  C      . GLN   F 4  340 ? -5.172  -41.922  -85.875  1.00 79.10  ? 340 GLN   F C      1 
ATOM   16929 O  O      . GLN   F 4  340 ? -5.640  -42.109  -84.746  1.00 73.98  ? 340 GLN   F O      1 
ATOM   16930 C  CB     . GLN   F 4  340 ? -3.469  -40.117  -86.170  1.00 83.66  ? 340 GLN   F CB     1 
ATOM   16931 C  CG     . GLN   F 4  340 ? -2.392  -39.579  -85.242  1.00 82.92  ? 340 GLN   F CG     1 
ATOM   16932 C  CD     . GLN   F 4  340 ? -0.993  -40.020  -85.664  1.00 89.44  ? 340 GLN   F CD     1 
ATOM   16933 O  OE1    . GLN   F 4  340 ? -0.782  -40.454  -86.802  1.00 87.66  ? 340 GLN   F OE1    1 
ATOM   16934 N  NE2    . GLN   F 4  340 ? -0.035  -39.919  -84.745  1.00 83.79  ? 340 GLN   F NE2    1 
ATOM   16935 N  N      . LYS   F 4  341 ? -5.933  -41.968  -86.974  1.00 82.34  ? 341 LYS   F N      1 
ATOM   16936 C  CA     . LYS   F 4  341 ? -7.379  -42.130  -86.843  1.00 83.78  ? 341 LYS   F CA     1 
ATOM   16937 C  C      . LYS   F 4  341 ? -7.738  -43.399  -86.081  1.00 84.18  ? 341 LYS   F C      1 
ATOM   16938 O  O      . LYS   F 4  341 ? -8.809  -43.469  -85.465  1.00 86.17  ? 341 LYS   F O      1 
ATOM   16939 C  CB     . LYS   F 4  341 ? -8.056  -42.137  -88.221  1.00 82.75  ? 341 LYS   F CB     1 
ATOM   16940 C  CG     . LYS   F 4  341 ? -9.525  -42.591  -88.149  1.00 87.34  ? 341 LYS   F CG     1 
ATOM   16941 C  CD     . LYS   F 4  341 ? -10.247 -42.441  -89.480  1.00 88.17  ? 341 LYS   F CD     1 
ATOM   16942 C  CE     . LYS   F 4  341 ? -11.647 -43.039  -89.457  1.00 85.03  ? 341 LYS   F CE     1 
ATOM   16943 N  NZ     . LYS   F 4  341 ? -12.057 -43.481  -90.826  1.00 81.36  ? 341 LYS   F NZ     1 
ATOM   16944 N  N      . LEU   F 4  342 ? -6.854  -44.406  -86.109  1.00 83.01  ? 342 LEU   F N      1 
ATOM   16945 C  CA     . LEU   F 4  342 ? -7.152  -45.738  -85.600  1.00 80.40  ? 342 LEU   F CA     1 
ATOM   16946 C  C      . LEU   F 4  342 ? -6.491  -46.064  -84.266  1.00 82.28  ? 342 LEU   F C      1 
ATOM   16947 O  O      . LEU   F 4  342 ? -6.939  -47.005  -83.599  1.00 81.54  ? 342 LEU   F O      1 
ATOM   16948 C  CB     . LEU   F 4  342 ? -6.740  -46.794  -86.640  1.00 78.32  ? 342 LEU   F CB     1 
ATOM   16949 C  CG     . LEU   F 4  342 ? -7.173  -46.447  -88.070  1.00 77.03  ? 342 LEU   F CG     1 
ATOM   16950 C  CD1    . LEU   F 4  342 ? -6.540  -47.369  -89.110  1.00 68.80  ? 342 LEU   F CD1    1 
ATOM   16951 C  CD2    . LEU   F 4  342 ? -8.697  -46.497  -88.159  1.00 73.60  ? 342 LEU   F CD2    1 
ATOM   16952 N  N      . TYR   F 4  343 ? -5.455  -45.311  -83.859  1.00 80.92  ? 343 TYR   F N      1 
ATOM   16953 C  CA     . TYR   F 4  343 ? -4.777  -45.545  -82.583  1.00 74.39  ? 343 TYR   F CA     1 
ATOM   16954 C  C      . TYR   F 4  343 ? -5.749  -45.881  -81.464  1.00 76.60  ? 343 TYR   F C      1 
ATOM   16955 O  O      . TYR   F 4  343 ? -5.575  -46.869  -80.744  1.00 77.95  ? 343 TYR   F O      1 
ATOM   16956 C  CB     . TYR   F 4  343 ? -3.955  -44.322  -82.193  1.00 72.76  ? 343 TYR   F CB     1 
ATOM   16957 C  CG     . TYR   F 4  343 ? -2.530  -44.388  -82.657  1.00 72.91  ? 343 TYR   F CG     1 
ATOM   16958 C  CD1    . TYR   F 4  343 ? -1.561  -45.022  -81.897  1.00 80.73  ? 343 TYR   F CD1    1 
ATOM   16959 C  CD2    . TYR   F 4  343 ? -2.148  -43.821  -83.852  1.00 75.57  ? 343 TYR   F CD2    1 
ATOM   16960 C  CE1    . TYR   F 4  343 ? -0.240  -45.085  -82.319  1.00 74.22  ? 343 TYR   F CE1    1 
ATOM   16961 C  CE2    . TYR   F 4  343 ? -0.836  -43.878  -84.282  1.00 78.70  ? 343 TYR   F CE2    1 
ATOM   16962 C  CZ     . TYR   F 4  343 ? 0.116   -44.513  -83.514  1.00 74.30  ? 343 TYR   F CZ     1 
ATOM   16963 O  OH     . TYR   F 4  343 ? 1.429   -44.571  -83.947  1.00 74.94  ? 343 TYR   F OH     1 
ATOM   16964 N  N      . ALA   F 4  344 ? -6.783  -45.062  -81.298  1.00 82.55  ? 344 ALA   F N      1 
ATOM   16965 C  CA     . ALA   F 4  344 ? -7.799  -45.370  -80.300  1.00 82.73  ? 344 ALA   F CA     1 
ATOM   16966 C  C      . ALA   F 4  344 ? -8.313  -46.793  -80.473  1.00 83.37  ? 344 ALA   F C      1 
ATOM   16967 O  O      . ALA   F 4  344 ? -8.358  -47.568  -79.510  1.00 86.45  ? 344 ALA   F O      1 
ATOM   16968 C  CB     . ALA   F 4  344 ? -8.948  -44.362  -80.382  1.00 77.87  ? 344 ALA   F CB     1 
ATOM   16969 N  N      . GLU   F 4  345 ? -8.686  -47.170  -81.703  1.00 82.19  ? 345 GLU   F N      1 
ATOM   16970 C  CA     . GLU   F 4  345 ? -9.320  -48.474  -81.887  1.00 82.25  ? 345 GLU   F CA     1 
ATOM   16971 C  C      . GLU   F 4  345 ? -8.311  -49.608  -81.736  1.00 78.94  ? 345 GLU   F C      1 
ATOM   16972 O  O      . GLU   F 4  345 ? -8.557  -50.572  -80.999  1.00 75.49  ? 345 GLU   F O      1 
ATOM   16973 C  CB     . GLU   F 4  345 ? -10.033 -48.562  -83.242  1.00 73.73  ? 345 GLU   F CB     1 
ATOM   16974 C  CG     . GLU   F 4  345 ? -11.022 -49.728  -83.290  1.00 68.82  ? 345 GLU   F CG     1 
ATOM   16975 C  CD     . GLU   F 4  345 ? -11.946 -49.730  -84.494  1.00 70.13  ? 345 GLU   F CD     1 
ATOM   16976 O  OE1    . GLU   F 4  345 ? -11.521 -49.402  -85.626  1.00 68.99  ? 345 GLU   F OE1    1 
ATOM   16977 O  OE2    . GLU   F 4  345 ? -13.124 -50.067  -84.291  1.00 64.42  ? 345 GLU   F OE2    1 
ATOM   16978 N  N      . LEU   F 4  346 ? -7.161  -49.506  -82.410  1.00 73.87  ? 346 LEU   F N      1 
ATOM   16979 C  CA     . LEU   F 4  346 ? -6.238  -50.637  -82.422  1.00 77.37  ? 346 LEU   F CA     1 
ATOM   16980 C  C      . LEU   F 4  346 ? -5.602  -50.877  -81.049  1.00 79.16  ? 346 LEU   F C      1 
ATOM   16981 O  O      . LEU   F 4  346 ? -5.404  -52.031  -80.649  1.00 77.74  ? 346 LEU   F O      1 
ATOM   16982 C  CB     . LEU   F 4  346 ? -5.166  -50.440  -83.496  1.00 71.92  ? 346 LEU   F CB     1 
ATOM   16983 C  CG     . LEU   F 4  346 ? -4.079  -51.518  -83.438  1.00 72.02  ? 346 LEU   F CG     1 
ATOM   16984 C  CD1    . LEU   F 4  346 ? -4.702  -52.897  -83.603  1.00 69.23  ? 346 LEU   F CD1    1 
ATOM   16985 C  CD2    . LEU   F 4  346 ? -2.983  -51.281  -84.474  1.00 69.06  ? 346 LEU   F CD2    1 
ATOM   16986 N  N      . CYS   F 4  347 ? -5.272  -49.816  -80.306  1.00 77.25  ? 347 CYS   F N      1 
ATOM   16987 C  CA     . CYS   F 4  347 ? -4.644  -50.033  -79.006  1.00 71.54  ? 347 CYS   F CA     1 
ATOM   16988 C  C      . CYS   F 4  347 ? -5.637  -50.565  -77.975  1.00 74.70  ? 347 CYS   F C      1 
ATOM   16989 O  O      . CYS   F 4  347 ? -5.242  -51.274  -77.044  1.00 79.41  ? 347 CYS   F O      1 
ATOM   16990 C  CB     . CYS   F 4  347 ? -4.002  -48.746  -78.518  1.00 69.69  ? 347 CYS   F CB     1 
ATOM   16991 S  SG     . CYS   F 4  347 ? -2.753  -48.118  -79.629  1.00 78.16  ? 347 CYS   F SG     1 
ATOM   16992 N  N      . GLN   F 4  348 ? -6.918  -50.237  -78.106  1.00 72.41  ? 348 GLN   F N      1 
ATOM   16993 C  CA     . GLN   F 4  348 ? -7.901  -50.882  -77.246  1.00 72.08  ? 348 GLN   F CA     1 
ATOM   16994 C  C      . GLN   F 4  348 ? -8.082  -52.352  -77.614  1.00 75.16  ? 348 GLN   F C      1 
ATOM   16995 O  O      . GLN   F 4  348 ? -8.380  -53.177  -76.742  1.00 71.56  ? 348 GLN   F O      1 
ATOM   16996 C  CB     . GLN   F 4  348 ? -9.233  -50.135  -77.323  1.00 71.77  ? 348 GLN   F CB     1 
ATOM   16997 C  CG     . GLN   F 4  348 ? -10.401 -50.869  -76.683  1.00 66.74  ? 348 GLN   F CG     1 
ATOM   16998 C  CD     . GLN   F 4  348 ? -10.234 -51.095  -75.195  1.00 71.79  ? 348 GLN   F CD     1 
ATOM   16999 O  OE1    . GLN   F 4  348 ? -10.658 -52.124  -74.675  1.00 76.57  ? 348 GLN   F OE1    1 
ATOM   17000 N  NE2    . GLN   F 4  348 ? -9.626  -50.132  -74.497  1.00 75.76  ? 348 GLN   F NE2    1 
ATOM   17001 N  N      . GLY   F 4  349 ? -7.906  -52.697  -78.896  1.00 76.13  ? 349 GLY   F N      1 
ATOM   17002 C  CA     . GLY   F 4  349 ? -8.024  -54.085  -79.312  1.00 71.21  ? 349 GLY   F CA     1 
ATOM   17003 C  C      . GLY   F 4  349 ? -6.850  -54.942  -78.893  1.00 72.03  ? 349 GLY   F C      1 
ATOM   17004 O  O      . GLY   F 4  349 ? -7.025  -56.128  -78.593  1.00 72.38  ? 349 GLY   F O      1 
ATOM   17005 N  N      . ILE   F 4  350 ? -5.642  -54.366  -78.876  1.00 68.70  ? 350 ILE   F N      1 
ATOM   17006 C  CA     . ILE   F 4  350 ? -4.499  -55.046  -78.276  1.00 66.67  ? 350 ILE   F CA     1 
ATOM   17007 C  C      . ILE   F 4  350 ? -4.827  -55.445  -76.846  1.00 67.55  ? 350 ILE   F C      1 
ATOM   17008 O  O      . ILE   F 4  350 ? -4.631  -56.594  -76.435  1.00 67.25  ? 350 ILE   F O      1 
ATOM   17009 C  CB     . ILE   F 4  350 ? -3.249  -54.150  -78.321  1.00 69.18  ? 350 ILE   F CB     1 
ATOM   17010 C  CG1    . ILE   F 4  350 ? -2.557  -54.231  -79.676  1.00 68.58  ? 350 ILE   F CG1    1 
ATOM   17011 C  CG2    . ILE   F 4  350 ? -2.276  -54.538  -77.214  1.00 65.74  ? 350 ILE   F CG2    1 
ATOM   17012 C  CD1    . ILE   F 4  350 ? -1.857  -52.959  -80.062  1.00 66.62  ? 350 ILE   F CD1    1 
ATOM   17013 N  N      . VAL   F 4  351 ? -5.336  -54.494  -76.064  1.00 67.22  ? 351 VAL   F N      1 
ATOM   17014 C  CA     . VAL   F 4  351 ? -5.574  -54.754  -74.648  1.00 69.16  ? 351 VAL   F CA     1 
ATOM   17015 C  C      . VAL   F 4  351 ? -6.565  -55.897  -74.476  1.00 67.52  ? 351 VAL   F C      1 
ATOM   17016 O  O      . VAL   F 4  351 ? -6.404  -56.752  -73.601  1.00 67.69  ? 351 VAL   F O      1 
ATOM   17017 C  CB     . VAL   F 4  351 ? -6.055  -53.470  -73.942  1.00 65.56  ? 351 VAL   F CB     1 
ATOM   17018 C  CG1    . VAL   F 4  351 ? -6.584  -53.796  -72.567  1.00 54.41  ? 351 VAL   F CG1    1 
ATOM   17019 C  CG2    . VAL   F 4  351 ? -4.930  -52.429  -73.885  1.00 65.24  ? 351 VAL   F CG2    1 
ATOM   17020 N  N      . ASP   F 4  352 ? -7.604  -55.935  -75.305  1.00 68.67  ? 352 ASP   F N      1 
ATOM   17021 C  CA     . ASP   F 4  352 ? -8.603  -56.984  -75.152  1.00 69.04  ? 352 ASP   F CA     1 
ATOM   17022 C  C      . ASP   F 4  352 ? -8.026  -58.336  -75.537  1.00 68.63  ? 352 ASP   F C      1 
ATOM   17023 O  O      . ASP   F 4  352 ? -8.119  -59.310  -74.778  1.00 65.52  ? 352 ASP   F O      1 
ATOM   17024 C  CB     . ASP   F 4  352 ? -9.838  -56.680  -76.008  1.00 76.57  ? 352 ASP   F CB     1 
ATOM   17025 C  CG     . ASP   F 4  352 ? -10.378 -55.259  -75.807  1.00 80.79  ? 352 ASP   F CG     1 
ATOM   17026 O  OD1    . ASP   F 4  352 ? -10.021 -54.617  -74.787  1.00 77.39  ? 352 ASP   F OD1    1 
ATOM   17027 O  OD2    . ASP   F 4  352 ? -11.167 -54.797  -76.677  1.00 74.69  ? 352 ASP   F OD2    1 
ATOM   17028 N  N      . VAL   F 4  353 ? -7.412  -58.408  -76.713  1.00 65.82  ? 353 VAL   F N      1 
ATOM   17029 C  CA     . VAL   F 4  353 ? -7.095  -59.699  -77.306  1.00 67.66  ? 353 VAL   F CA     1 
ATOM   17030 C  C      . VAL   F 4  353 ? -5.762  -60.247  -76.790  1.00 68.59  ? 353 VAL   F C      1 
ATOM   17031 O  O      . VAL   F 4  353 ? -5.623  -61.458  -76.579  1.00 67.27  ? 353 VAL   F O      1 
ATOM   17032 C  CB     . VAL   F 4  353 ? -7.110  -59.563  -78.838  1.00 71.17  ? 353 VAL   F CB     1 
ATOM   17033 C  CG1    . VAL   F 4  353 ? -6.684  -60.865  -79.505  1.00 64.42  ? 353 VAL   F CG1    1 
ATOM   17034 C  CG2    . VAL   F 4  353 ? -8.485  -59.107  -79.313  1.00 62.38  ? 353 VAL   F CG2    1 
ATOM   17035 N  N      . ALA   F 4  354 ? -4.759  -59.379  -76.592  1.00 64.96  ? 354 ALA   F N      1 
ATOM   17036 C  CA     . ALA   F 4  354 ? -3.411  -59.819  -76.249  1.00 60.22  ? 354 ALA   F CA     1 
ATOM   17037 C  C      . ALA   F 4  354 ? -3.074  -59.719  -74.768  1.00 61.63  ? 354 ALA   F C      1 
ATOM   17038 O  O      . ALA   F 4  354 ? -2.185  -60.444  -74.311  1.00 64.28  ? 354 ALA   F O      1 
ATOM   17039 C  CB     . ALA   F 4  354 ? -2.367  -59.018  -77.038  1.00 56.92  ? 354 ALA   F CB     1 
ATOM   17040 N  N      . ILE   F 4  355 ? -3.745  -58.860  -74.007  1.00 59.02  ? 355 ILE   F N      1 
ATOM   17041 C  CA     . ILE   F 4  355 ? -3.336  -58.526  -72.651  1.00 58.31  ? 355 ILE   F CA     1 
ATOM   17042 C  C      . ILE   F 4  355 ? -4.369  -58.960  -71.623  1.00 60.05  ? 355 ILE   F C      1 
ATOM   17043 O  O      . ILE   F 4  355 ? -4.025  -59.572  -70.616  1.00 65.67  ? 355 ILE   F O      1 
ATOM   17044 C  CB     . ILE   F 4  355 ? -3.019  -57.022  -72.514  1.00 60.06  ? 355 ILE   F CB     1 
ATOM   17045 C  CG1    . ILE   F 4  355 ? -1.875  -56.635  -73.462  1.00 61.12  ? 355 ILE   F CG1    1 
ATOM   17046 C  CG2    . ILE   F 4  355 ? -2.712  -56.700  -71.059  1.00 62.65  ? 355 ILE   F CG2    1 
ATOM   17047 C  CD1    . ILE   F 4  355 ? -1.262  -55.266  -73.202  1.00 61.86  ? 355 ILE   F CD1    1 
ATOM   17048 N  N      . SER   F 4  356 ? -5.633  -58.619  -71.833  1.00 61.34  ? 356 SER   F N      1 
ATOM   17049 C  CA     . SER   F 4  356 ? -6.657  -59.079  -70.901  1.00 59.64  ? 356 SER   F CA     1 
ATOM   17050 C  C      . SER   F 4  356 ? -7.017  -60.536  -71.114  1.00 60.38  ? 356 SER   F C      1 
ATOM   17051 O  O      . SER   F 4  356 ? -7.628  -61.144  -70.229  1.00 61.29  ? 356 SER   F O      1 
ATOM   17052 C  CB     . SER   F 4  356 ? -7.922  -58.226  -71.006  1.00 59.95  ? 356 SER   F CB     1 
ATOM   17053 O  OG     . SER   F 4  356 ? -7.618  -56.851  -70.853  1.00 66.31  ? 356 SER   F OG     1 
ATOM   17054 N  N      . SER   F 4  357 ? -6.673  -61.104  -72.271  1.00 61.75  ? 357 SER   F N      1 
ATOM   17055 C  CA     . SER   F 4  357 ? -6.858  -62.534  -72.460  1.00 53.04  ? 357 SER   F CA     1 
ATOM   17056 C  C      . SER   F 4  357 ? -6.119  -63.301  -71.383  1.00 63.00  ? 357 SER   F C      1 
ATOM   17057 O  O      . SER   F 4  357 ? -6.640  -64.285  -70.841  1.00 64.80  ? 357 SER   F O      1 
ATOM   17058 C  CB     . SER   F 4  357 ? -6.349  -62.943  -73.829  1.00 59.66  ? 357 SER   F CB     1 
ATOM   17059 O  OG     . SER   F 4  357 ? -5.206  -62.177  -74.143  1.00 68.34  ? 357 SER   F OG     1 
ATOM   17060 N  N      . VAL   F 4  358 ? -4.907  -62.844  -71.054  1.00 61.49  ? 358 VAL   F N      1 
ATOM   17061 C  CA     . VAL   F 4  358 ? -4.044  -63.479  -70.063  1.00 59.00  ? 358 VAL   F CA     1 
ATOM   17062 C  C      . VAL   F 4  358 ? -4.303  -62.966  -68.653  1.00 54.86  ? 358 VAL   F C      1 
ATOM   17063 O  O      . VAL   F 4  358 ? -4.238  -63.742  -67.702  1.00 57.61  ? 358 VAL   F O      1 
ATOM   17064 C  CB     . VAL   F 4  358 ? -2.566  -63.287  -70.459  1.00 58.32  ? 358 VAL   F CB     1 
ATOM   17065 C  CG1    . VAL   F 4  358 ? -1.680  -64.177  -69.631  1.00 53.57  ? 358 VAL   F CG1    1 
ATOM   17066 C  CG2    . VAL   F 4  358 ? -2.368  -63.623  -71.915  1.00 57.02  ? 358 VAL   F CG2    1 
ATOM   17067 N  N      . PHE   F 4  359 ? -4.591  -61.674  -68.477  1.00 58.43  ? 359 PHE   F N      1 
ATOM   17068 C  CA     . PHE   F 4  359 ? -4.757  -61.059  -67.158  1.00 57.22  ? 359 PHE   F CA     1 
ATOM   17069 C  C      . PHE   F 4  359 ? -6.151  -60.443  -67.064  1.00 58.18  ? 359 PHE   F C      1 
ATOM   17070 O  O      . PHE   F 4  359 ? -6.309  -59.231  -67.267  1.00 64.31  ? 359 PHE   F O      1 
ATOM   17071 C  CB     . PHE   F 4  359 ? -3.685  -60.004  -66.910  1.00 51.59  ? 359 PHE   F CB     1 
ATOM   17072 C  CG     . PHE   F 4  359 ? -2.283  -60.493  -67.115  1.00 59.35  ? 359 PHE   F CG     1 
ATOM   17073 C  CD1    . PHE   F 4  359 ? -1.673  -61.323  -66.178  1.00 57.34  ? 359 PHE   F CD1    1 
ATOM   17074 C  CD2    . PHE   F 4  359 ? -1.561  -60.115  -68.244  1.00 60.54  ? 359 PHE   F CD2    1 
ATOM   17075 C  CE1    . PHE   F 4  359 ? -0.369  -61.764  -66.362  1.00 55.10  ? 359 PHE   F CE1    1 
ATOM   17076 C  CE2    . PHE   F 4  359 ? -0.254  -60.554  -68.437  1.00 58.84  ? 359 PHE   F CE2    1 
ATOM   17077 C  CZ     . PHE   F 4  359 ? 0.342   -61.378  -67.497  1.00 59.95  ? 359 PHE   F CZ     1 
ATOM   17078 N  N      . PRO   F 4  360 ? -7.187  -61.244  -66.779  1.00 60.39  ? 360 PRO   F N      1 
ATOM   17079 C  CA     . PRO   F 4  360 ? -8.572  -60.742  -66.907  1.00 63.31  ? 360 PRO   F CA     1 
ATOM   17080 C  C      . PRO   F 4  360 ? -8.978  -59.732  -65.834  1.00 68.12  ? 360 PRO   F C      1 
ATOM   17081 O  O      . PRO   F 4  360 ? -8.641  -59.867  -64.653  1.00 71.67  ? 360 PRO   F O      1 
ATOM   17082 C  CB     . PRO   F 4  360 ? -9.423  -62.015  -66.820  1.00 57.74  ? 360 PRO   F CB     1 
ATOM   17083 C  CG     . PRO   F 4  360 ? -8.525  -63.053  -66.220  1.00 58.93  ? 360 PRO   F CG     1 
ATOM   17084 C  CD     . PRO   F 4  360 ? -7.137  -62.709  -66.637  1.00 57.15  ? 360 PRO   F CD     1 
ATOM   17085 N  N      . LEU   F 4  361 ? -9.743  -58.724  -66.264  1.00 73.51  ? 361 LEU   F N      1 
ATOM   17086 C  CA     . LEU   F 4  361 ? -10.173 -57.607  -65.411  1.00 72.56  ? 361 LEU   F CA     1 
ATOM   17087 C  C      . LEU   F 4  361 ? -11.585 -57.789  -64.847  1.00 75.36  ? 361 LEU   F C      1 
ATOM   17088 O  O      . LEU   F 4  361 ? -11.852 -58.712  -64.071  1.00 76.25  ? 361 LEU   F O      1 
ATOM   17089 C  CB     . LEU   F 4  361 ? -10.117 -56.299  -66.192  1.00 68.20  ? 361 LEU   F CB     1 
ATOM   17090 C  CG     . LEU   F 4  361 ? -8.757  -55.891  -66.757  1.00 73.36  ? 361 LEU   F CG     1 
ATOM   17091 C  CD1    . LEU   F 4  361 ? -8.978  -54.848  -67.819  1.00 67.69  ? 361 LEU   F CD1    1 
ATOM   17092 C  CD2    . LEU   F 4  361 ? -7.802  -55.383  -65.667  1.00 76.67  ? 361 LEU   F CD2    1 
ATOM   17093 N  N      . THR   F 4  372 ? -18.694 -57.749  -83.892  1.00 98.49  ? 372 THR   F N      1 
ATOM   17094 C  CA     . THR   F 4  372 ? -18.359 -57.172  -82.591  1.00 108.33 ? 372 THR   F CA     1 
ATOM   17095 C  C      . THR   F 4  372 ? -16.877 -56.783  -82.538  1.00 107.90 ? 372 THR   F C      1 
ATOM   17096 O  O      . THR   F 4  372 ? -16.540 -55.620  -82.296  1.00 106.53 ? 372 THR   F O      1 
ATOM   17097 C  CB     . THR   F 4  372 ? -18.675 -58.149  -81.421  1.00 112.18 ? 372 THR   F CB     1 
ATOM   17098 O  OG1    . THR   F 4  372 ? -20.064 -58.506  -81.442  1.00 109.96 ? 372 THR   F OG1    1 
ATOM   17099 C  CG2    . THR   F 4  372 ? -18.341 -57.510  -80.071  1.00 97.98  ? 372 THR   F CG2    1 
ATOM   17100 N  N      . SER   F 4  373 ? -16.004 -57.761  -82.785  1.00 104.30 ? 373 SER   F N      1 
ATOM   17101 C  CA     . SER   F 4  373 ? -14.562 -57.572  -82.678  1.00 92.04  ? 373 SER   F CA     1 
ATOM   17102 C  C      . SER   F 4  373 ? -14.000 -56.773  -83.858  1.00 84.87  ? 373 SER   F C      1 
ATOM   17103 O  O      . SER   F 4  373 ? -14.563 -56.758  -84.958  1.00 81.09  ? 373 SER   F O      1 
ATOM   17104 C  CB     . SER   F 4  373 ? -13.861 -58.929  -82.575  1.00 84.51  ? 373 SER   F CB     1 
ATOM   17105 O  OG     . SER   F 4  373 ? -12.457 -58.779  -82.446  1.00 83.65  ? 373 SER   F OG     1 
ATOM   17106 N  N      . ILE   F 4  374 ? -12.863 -56.110  -83.612  1.00 83.93  ? 374 ILE   F N      1 
ATOM   17107 C  CA     . ILE   F 4  374 ? -12.201 -55.233  -84.580  1.00 75.30  ? 374 ILE   F CA     1 
ATOM   17108 C  C      . ILE   F 4  374 ? -11.155 -55.994  -85.385  1.00 73.36  ? 374 ILE   F C      1 
ATOM   17109 O  O      . ILE   F 4  374 ? -10.388 -55.388  -86.148  1.00 70.95  ? 374 ILE   F O      1 
ATOM   17110 C  CB     . ILE   F 4  374 ? -11.547 -54.020  -83.890  1.00 72.32  ? 374 ILE   F CB     1 
ATOM   17111 C  CG1    . ILE   F 4  374 ? -10.430 -54.468  -82.940  1.00 67.67  ? 374 ILE   F CG1    1 
ATOM   17112 C  CG2    . ILE   F 4  374 ? -12.576 -53.204  -83.131  1.00 72.76  ? 374 ILE   F CG2    1 
ATOM   17113 C  CD1    . ILE   F 4  374 ? -9.180  -53.601  -82.999  1.00 66.70  ? 374 ILE   F CD1    1 
ATOM   17114 N  N      . PHE   F 4  375 ? -11.099 -57.318  -85.205  1.00 72.50  ? 375 PHE   F N      1 
ATOM   17115 C  CA     . PHE   F 4  375 ? -10.141 -58.175  -85.891  1.00 70.31  ? 375 PHE   F CA     1 
ATOM   17116 C  C      . PHE   F 4  375 ? -10.856 -59.282  -86.666  1.00 72.38  ? 375 PHE   F C      1 
ATOM   17117 O  O      . PHE   F 4  375 ? -12.006 -59.638  -86.380  1.00 66.94  ? 375 PHE   F O      1 
ATOM   17118 C  CB     . PHE   F 4  375 ? -9.150  -58.832  -84.914  1.00 66.32  ? 375 PHE   F CB     1 
ATOM   17119 C  CG     . PHE   F 4  375 ? -8.276  -57.868  -84.148  1.00 63.73  ? 375 PHE   F CG     1 
ATOM   17120 C  CD1    . PHE   F 4  375 ? -7.328  -57.101  -84.791  1.00 65.12  ? 375 PHE   F CD1    1 
ATOM   17121 C  CD2    . PHE   F 4  375 ? -8.364  -57.785  -82.772  1.00 66.59  ? 375 PHE   F CD2    1 
ATOM   17122 C  CE1    . PHE   F 4  375 ? -6.509  -56.253  -84.085  1.00 58.59  ? 375 PHE   F CE1    1 
ATOM   17123 C  CE2    . PHE   F 4  375 ? -7.547  -56.937  -82.058  1.00 62.71  ? 375 PHE   F CE2    1 
ATOM   17124 C  CZ     . PHE   F 4  375 ? -6.619  -56.171  -82.720  1.00 65.93  ? 375 PHE   F CZ     1 
ATOM   17125 N  N      . ILE   F 4  376 ? -10.150 -59.829  -87.658  1.00 66.61  ? 376 ILE   F N      1 
ATOM   17126 C  CA     . ILE   F 4  376 ? -10.561 -61.037  -88.368  1.00 61.19  ? 376 ILE   F CA     1 
ATOM   17127 C  C      . ILE   F 4  376 ? -9.575  -62.130  -87.984  1.00 61.33  ? 376 ILE   F C      1 
ATOM   17128 O  O      . ILE   F 4  376 ? -8.388  -62.041  -88.316  1.00 64.47  ? 376 ILE   F O      1 
ATOM   17129 C  CB     . ILE   F 4  376 ? -10.582 -60.839  -89.892  1.00 63.23  ? 376 ILE   F CB     1 
ATOM   17130 C  CG1    . ILE   F 4  376 ? -11.229 -59.509  -90.271  1.00 68.36  ? 376 ILE   F CG1    1 
ATOM   17131 C  CG2    . ILE   F 4  376 ? -11.267 -61.997  -90.593  1.00 62.72  ? 376 ILE   F CG2    1 
ATOM   17132 C  CD1    . ILE   F 4  376 ? -10.511 -58.812  -91.416  1.00 72.03  ? 376 ILE   F CD1    1 
ATOM   17133 N  N      . LYS   F 4  377 ? -10.038 -63.158  -87.280  1.00 60.41  ? 377 LYS   F N      1 
ATOM   17134 C  CA     . LYS   F 4  377 ? -9.164  -64.280  -86.965  1.00 55.67  ? 377 LYS   F CA     1 
ATOM   17135 C  C      . LYS   F 4  377 ? -8.766  -64.986  -88.259  1.00 58.22  ? 377 LYS   F C      1 
ATOM   17136 O  O      . LYS   F 4  377 ? -9.633  -65.397  -89.037  1.00 63.70  ? 377 LYS   F O      1 
ATOM   17137 C  CB     . LYS   F 4  377 ? -9.864  -65.237  -86.004  1.00 60.91  ? 377 LYS   F CB     1 
ATOM   17138 C  CG     . LYS   F 4  377 ? -8.917  -66.183  -85.261  1.00 68.69  ? 377 LYS   F CG     1 
ATOM   17139 C  CD     . LYS   F 4  377 ? -9.519  -66.711  -83.948  1.00 73.18  ? 377 LYS   F CD     1 
ATOM   17140 C  CE     . LYS   F 4  377 ? -9.263  -68.214  -83.753  1.00 75.19  ? 377 LYS   F CE     1 
ATOM   17141 N  NZ     . LYS   F 4  377 ? -9.538  -68.673  -82.343  1.00 75.16  ? 377 LYS   F NZ     1 
ATOM   17142 N  N      . LEU   F 4  378 ? -7.462  -65.098  -88.518  1.00 54.91  ? 378 LEU   F N      1 
ATOM   17143 C  CA     . LEU   F 4  378 ? -6.965  -65.801  -89.699  1.00 57.30  ? 378 LEU   F CA     1 
ATOM   17144 C  C      . LEU   F 4  378 ? -6.684  -67.255  -89.323  1.00 65.66  ? 378 LEU   F C      1 
ATOM   17145 O  O      . LEU   F 4  378 ? -5.760  -67.545  -88.551  1.00 66.70  ? 378 LEU   F O      1 
ATOM   17146 C  CB     . LEU   F 4  378 ? -5.727  -65.115  -90.285  1.00 55.60  ? 378 LEU   F CB     1 
ATOM   17147 C  CG     . LEU   F 4  378 ? -5.873  -63.672  -90.811  1.00 50.86  ? 378 LEU   F CG     1 
ATOM   17148 C  CD1    . LEU   F 4  378 ? -4.633  -63.188  -91.533  1.00 46.32  ? 378 LEU   F CD1    1 
ATOM   17149 C  CD2    . LEU   F 4  378 ? -7.053  -63.558  -91.714  1.00 47.27  ? 378 LEU   F CD2    1 
ATOM   17150 N  N      . HIS   F 4  379 ? -7.484  -68.163  -89.889  1.00 74.95  ? 379 HIS   F N      1 
ATOM   17151 C  CA     . HIS   F 4  379 ? -7.613  -69.539  -89.416  1.00 80.88  ? 379 HIS   F CA     1 
ATOM   17152 C  C      . HIS   F 4  379 ? -6.582  -70.460  -90.061  1.00 90.09  ? 379 HIS   F C      1 
ATOM   17153 O  O      . HIS   F 4  379 ? -6.374  -70.424  -91.278  1.00 92.23  ? 379 HIS   F O      1 
ATOM   17154 C  CB     . HIS   F 4  379 ? -9.017  -70.072  -89.713  1.00 84.29  ? 379 HIS   F CB     1 
ATOM   17155 C  CG     . HIS   F 4  379 ? -10.042 -69.673  -88.698  1.00 85.32  ? 379 HIS   F CG     1 
ATOM   17156 N  ND1    . HIS   F 4  379 ? -11.359 -69.421  -89.026  1.00 79.70  ? 379 HIS   F ND1    1 
ATOM   17157 C  CD2    . HIS   F 4  379 ? -9.941  -69.476  -87.362  1.00 84.90  ? 379 HIS   F CD2    1 
ATOM   17158 C  CE1    . HIS   F 4  379 ? -12.023 -69.086  -87.933  1.00 88.68  ? 379 HIS   F CE1    1 
ATOM   17159 N  NE2    . HIS   F 4  379 ? -11.185 -69.112  -86.910  1.00 87.46  ? 379 HIS   F NE2    1 
ATOM   17160 N  N      . HIS   F 4  380 ? -5.967  -71.306  -89.233  1.00 90.94  ? 380 HIS   F N      1 
ATOM   17161 C  CA     . HIS   F 4  380 ? -4.945  -72.265  -89.649  1.00 93.87  ? 380 HIS   F CA     1 
ATOM   17162 C  C      . HIS   F 4  380 ? -5.289  -73.671  -89.112  1.00 106.48 ? 380 HIS   F C      1 
ATOM   17163 O  O      . HIS   F 4  380 ? -4.571  -74.656  -89.335  1.00 105.87 ? 380 HIS   F O      1 
ATOM   17164 C  CB     . HIS   F 4  380 ? -3.563  -71.809  -89.155  1.00 94.30  ? 380 HIS   F CB     1 
ATOM   17165 C  CG     . HIS   F 4  380 ? -3.566  -71.238  -87.762  1.00 91.75  ? 380 HIS   F CG     1 
ATOM   17166 N  ND1    . HIS   F 4  380 ? -4.250  -70.086  -87.432  1.00 91.40  ? 380 HIS   F ND1    1 
ATOM   17167 C  CD2    . HIS   F 4  380 ? -2.936  -71.637  -86.628  1.00 84.11  ? 380 HIS   F CD2    1 
ATOM   17168 C  CE1    . HIS   F 4  380 ? -4.065  -69.815  -86.151  1.00 84.72  ? 380 HIS   F CE1    1 
ATOM   17169 N  NE2    . HIS   F 4  380 ? -3.268  -70.738  -85.642  1.00 81.52  ? 380 HIS   F NE2    1 
HETATM 17170 P  PG     . GTP   G 5  .   ? 27.233  -73.727  -46.310  0.00 42.95  ? 501 GTP   A PG     1 
HETATM 17171 O  O1G    . GTP   G 5  .   ? 26.988  -72.262  -46.581  0.00 42.42  ? 501 GTP   A O1G    1 
HETATM 17172 O  O2G    . GTP   G 5  .   ? 26.029  -74.326  -45.622  0.00 44.81  ? 501 GTP   A O2G    1 
HETATM 17173 O  O3G    . GTP   G 5  .   ? 28.449  -73.884  -45.428  0.00 42.87  ? 501 GTP   A O3G    1 
HETATM 17174 O  O3B    . GTP   G 5  .   ? 27.479  -74.472  -47.716  0.00 42.88  ? 501 GTP   A O3B    1 
HETATM 17175 P  PB     . GTP   G 5  .   ? 26.470  -75.625  -48.210  0.00 43.04  ? 501 GTP   A PB     1 
HETATM 17176 O  O1B    . GTP   G 5  .   ? 27.085  -76.345  -49.386  0.00 42.97  ? 501 GTP   A O1B    1 
HETATM 17177 O  O2B    . GTP   G 5  .   ? 26.146  -76.586  -47.092  0.00 44.33  ? 501 GTP   A O2B    1 
HETATM 17178 O  O3A    . GTP   G 5  .   ? 25.152  -74.831  -48.690  0.00 43.47  ? 501 GTP   A O3A    1 
HETATM 17179 P  PA     . GTP   G 5  .   ? 24.115  -75.515  -49.716  0.00 42.91  ? 501 GTP   A PA     1 
HETATM 17180 O  O1A    . GTP   G 5  .   ? 24.692  -76.803  -50.253  0.00 42.48  ? 501 GTP   A O1A    1 
HETATM 17181 O  O2A    . GTP   G 5  .   ? 22.792  -75.763  -49.033  0.00 43.00  ? 501 GTP   A O2A    1 
HETATM 17182 O  "O5'"  . GTP   G 5  .   ? 23.949  -74.444  -50.909  0.00 43.00  ? 501 GTP   A "O5'"  1 
HETATM 17183 C  "C5'"  . GTP   G 5  .   ? 22.828  -73.588  -50.967  0.00 44.27  ? 501 GTP   A "C5'"  1 
HETATM 17184 C  "C4'"  . GTP   G 5  .   ? 21.937  -73.979  -52.141  0.00 44.41  ? 501 GTP   A "C4'"  1 
HETATM 17185 O  "O4'"  . GTP   G 5  .   ? 21.978  -75.378  -52.329  0.00 43.31  ? 501 GTP   A "O4'"  1 
HETATM 17186 C  "C3'"  . GTP   G 5  .   ? 20.484  -73.609  -51.893  0.00 46.83  ? 501 GTP   A "C3'"  1 
HETATM 17187 O  "O3'"  . GTP   G 5  .   ? 20.097  -72.565  -52.756  0.00 47.54  ? 501 GTP   A "O3'"  1 
HETATM 17188 C  "C2'"  . GTP   G 5  .   ? 19.686  -74.858  -52.213  0.00 45.18  ? 501 GTP   A "C2'"  1 
HETATM 17189 O  "O2'"  . GTP   G 5  .   ? 18.725  -74.594  -53.208  0.00 44.29  ? 501 GTP   A "O2'"  1 
HETATM 17190 C  "C1'"  . GTP   G 5  .   ? 20.708  -75.874  -52.700  0.00 43.06  ? 501 GTP   A "C1'"  1 
HETATM 17191 N  N9     . GTP   G 5  .   ? 20.486  -77.179  -52.053  0.00 42.75  ? 501 GTP   A N9     1 
HETATM 17192 C  C8     . GTP   G 5  .   ? 20.790  -77.509  -50.758  0.00 42.89  ? 501 GTP   A C8     1 
HETATM 17193 N  N7     . GTP   G 5  .   ? 20.443  -78.799  -50.552  0.00 43.11  ? 501 GTP   A N7     1 
HETATM 17194 C  C5     . GTP   G 5  .   ? 19.930  -79.300  -51.698  0.00 42.93  ? 501 GTP   A C5     1 
HETATM 17195 C  C6     . GTP   G 5  .   ? 19.431  -80.552  -52.032  0.00 42.90  ? 501 GTP   A C6     1 
HETATM 17196 O  O6     . GTP   G 5  .   ? 19.405  -81.452  -51.194  0.00 44.15  ? 501 GTP   A O6     1 
HETATM 17197 N  N1     . GTP   G 5  .   ? 18.964  -80.780  -53.310  0.00 42.70  ? 501 GTP   A N1     1 
HETATM 17198 C  C2     . GTP   G 5  .   ? 18.996  -79.766  -54.246  0.00 41.29  ? 501 GTP   A C2     1 
HETATM 17199 N  N2     . GTP   G 5  .   ? 18.546  -79.984  -55.478  0.00 41.22  ? 501 GTP   A N2     1 
HETATM 17200 N  N3     . GTP   G 5  .   ? 19.494  -78.524  -53.905  0.00 41.09  ? 501 GTP   A N3     1 
HETATM 17201 C  C4     . GTP   G 5  .   ? 19.954  -78.293  -52.651  0.00 42.24  ? 501 GTP   A C4     1 
HETATM 17202 CA CA     . CA    H 6  .   ? 33.767  -108.877 -58.843  0.00 71.95  ? 502 CA    A CA     1 
HETATM 17203 MG MG     . MG    I 7  .   ? 25.614  -76.915  -44.715  0.00 50.14  ? 503 MG    A MG     1 
HETATM 17204 P  PB     . GDP   J 8  .   ? 18.635  -49.447  -15.686  0.00 36.22  ? 501 GDP   B PB     1 
HETATM 17205 O  O1B    . GDP   J 8  .   ? 19.076  -50.294  -16.856  0.00 35.94  ? 501 GDP   B O1B    1 
HETATM 17206 O  O2B    . GDP   J 8  .   ? 18.135  -50.325  -14.564  0.00 38.60  ? 501 GDP   B O2B    1 
HETATM 17207 O  O3B    . GDP   J 8  .   ? 19.805  -48.636  -15.183  0.00 34.58  ? 501 GDP   B O3B    1 
HETATM 17208 O  O3A    . GDP   J 8  .   ? 17.465  -48.444  -16.151  0.00 37.91  ? 501 GDP   B O3A    1 
HETATM 17209 P  PA     . GDP   J 8  .   ? 16.212  -48.978  -17.010  0.00 39.16  ? 501 GDP   B PA     1 
HETATM 17210 O  O1A    . GDP   J 8  .   ? 16.528  -50.309  -17.650  0.00 37.79  ? 501 GDP   B O1A    1 
HETATM 17211 O  O2A    . GDP   J 8  .   ? 14.985  -49.096  -16.143  0.00 40.73  ? 501 GDP   B O2A    1 
HETATM 17212 O  "O5'"  . GDP   J 8  .   ? 15.982  -47.838  -18.123  0.00 38.11  ? 501 GDP   B "O5'"  1 
HETATM 17213 C  "C5'"  . GDP   J 8  .   ? 14.769  -47.090  -18.121  0.00 39.83  ? 501 GDP   B "C5'"  1 
HETATM 17214 C  "C4'"  . GDP   J 8  .   ? 14.143  -47.087  -19.508  0.00 39.29  ? 501 GDP   B "C4'"  1 
HETATM 17215 O  "O4'"  . GDP   J 8  .   ? 13.825  -48.436  -19.853  0.00 38.54  ? 501 GDP   B "O4'"  1 
HETATM 17216 C  "C3'"  . GDP   J 8  .   ? 12.846  -46.295  -19.508  0.00 41.13  ? 501 GDP   B "C3'"  1 
HETATM 17217 O  "O3'"  . GDP   J 8  .   ? 12.835  -45.371  -20.600  0.00 41.09  ? 501 GDP   B "O3'"  1 
HETATM 17218 C  "C2'"  . GDP   J 8  .   ? 11.739  -47.314  -19.686  0.00 40.30  ? 501 GDP   B "C2'"  1 
HETATM 17219 O  "O2'"  . GDP   J 8  .   ? 10.802  -46.868  -20.671  0.00 40.28  ? 501 GDP   B "O2'"  1 
HETATM 17220 C  "C1'"  . GDP   J 8  .   ? 12.433  -48.588  -20.139  0.00 38.38  ? 501 GDP   B "C1'"  1 
HETATM 17221 N  N9     . GDP   J 8  .   ? 11.906  -49.759  -19.398  0.00 37.90  ? 501 GDP   B N9     1 
HETATM 17222 C  C8     . GDP   J 8  .   ? 12.164  -50.055  -18.110  0.00 38.31  ? 501 GDP   B C8     1 
HETATM 17223 N  N7     . GDP   J 8  .   ? 11.535  -51.198  -17.734  0.00 38.50  ? 501 GDP   B N7     1 
HETATM 17224 C  C5     . GDP   J 8  .   ? 10.858  -51.656  -18.803  0.00 38.00  ? 501 GDP   B C5     1 
HETATM 17225 C  C6     . GDP   J 8  .   ? 9.985   -52.816  -19.099  0.00 39.17  ? 501 GDP   B C6     1 
HETATM 17226 O  O6     . GDP   J 8  .   ? 9.726   -53.667  -18.221  0.00 40.82  ? 501 GDP   B O6     1 
HETATM 17227 N  N1     . GDP   J 8  .   ? 9.483   -52.924  -20.335  0.00 40.00  ? 501 GDP   B N1     1 
HETATM 17228 C  C2     . GDP   J 8  .   ? 9.745   -52.023  -21.301  0.00 38.42  ? 501 GDP   B C2     1 
HETATM 17229 N  N2     . GDP   J 8  .   ? 9.196   -52.207  -22.526  0.00 39.17  ? 501 GDP   B N2     1 
HETATM 17230 N  N3     . GDP   J 8  .   ? 10.535  -50.937  -21.101  0.00 37.40  ? 501 GDP   B N3     1 
HETATM 17231 C  C4     . GDP   J 8  .   ? 11.108  -50.706  -19.897  0.00 37.32  ? 501 GDP   B C4     1 
HETATM 17232 O  O1     . MES   K 9  .   ? 30.578  -56.481  -33.721  0.00 40.61  ? 502 MES   B O1     1 
HETATM 17233 C  C2     . MES   K 9  .   ? 30.188  -57.618  -32.955  0.00 39.51  ? 502 MES   B C2     1 
HETATM 17234 C  C3     . MES   K 9  .   ? 31.086  -58.818  -33.241  0.00 40.00  ? 502 MES   B C3     1 
HETATM 17235 N  N4     . MES   K 9  .   ? 31.190  -58.984  -34.685  0.00 40.61  ? 502 MES   B N4     1 
HETATM 17236 C  C5     . MES   K 9  .   ? 31.541  -57.821  -35.485  0.00 40.70  ? 502 MES   B C5     1 
HETATM 17237 C  C6     . MES   K 9  .   ? 30.536  -56.738  -35.121  0.00 40.45  ? 502 MES   B C6     1 
HETATM 17238 C  C7     . MES   K 9  .   ? 31.727  -60.256  -35.141  0.00 41.55  ? 502 MES   B C7     1 
HETATM 17239 C  C8     . MES   K 9  .   ? 31.384  -60.346  -36.623  0.00 41.20  ? 502 MES   B C8     1 
HETATM 17240 S  S      . MES   K 9  .   ? 32.207  -61.631  -37.282  0.00 42.61  ? 502 MES   B S      1 
HETATM 17241 O  O1S    . MES   K 9  .   ? 31.617  -61.969  -38.597  0.00 42.18  ? 502 MES   B O1S    1 
HETATM 17242 O  O2S    . MES   K 9  .   ? 33.636  -61.286  -37.458  0.00 43.09  ? 502 MES   B O2S    1 
HETATM 17243 O  O3S    . MES   K 9  .   ? 32.077  -62.797  -36.381  0.00 43.68  ? 502 MES   B O3S    1 
HETATM 17244 O  O1     . MES   L 9  .   ? 4.637   -53.375  -48.494  0.00 57.21  ? 503 MES   B O1     1 
HETATM 17245 C  C2     . MES   L 9  .   ? 3.904   -54.313  -47.709  0.00 56.38  ? 503 MES   B C2     1 
HETATM 17246 C  C3     . MES   L 9  .   ? 2.553   -53.744  -47.287  0.00 57.20  ? 503 MES   B C3     1 
HETATM 17247 N  N4     . MES   L 9  .   ? 2.775   -52.425  -46.710  0.00 56.70  ? 503 MES   B N4     1 
HETATM 17248 C  C5     . MES   L 9  .   ? 3.575   -51.464  -47.456  0.00 57.12  ? 503 MES   B C5     1 
HETATM 17249 C  C6     . MES   L 9  .   ? 4.885   -52.163  -47.788  0.00 57.10  ? 503 MES   B C6     1 
HETATM 17250 C  C7     . MES   L 9  .   ? 1.691   -51.875  -45.910  0.00 55.85  ? 503 MES   B C7     1 
HETATM 17251 C  C8     . MES   L 9  .   ? 2.334   -51.326  -44.642  0.00 55.05  ? 503 MES   B C8     1 
HETATM 17252 S  S      . MES   L 9  .   ? 1.284   -50.250  -43.934  0.00 54.66  ? 503 MES   B S      1 
HETATM 17253 O  O1S    . MES   L 9  .   ? 1.913   -48.911  -43.875  0.00 54.40  ? 503 MES   B O1S    1 
HETATM 17254 O  O2S    . MES   L 9  .   ? 0.040   -50.174  -44.733  0.00 55.11  ? 503 MES   B O2S    1 
HETATM 17255 O  O3S    . MES   L 9  .   ? 0.977   -50.694  -42.556  0.00 54.19  ? 503 MES   B O3S    1 
HETATM 17256 MG MG     . MG    M 7  .   ? 14.029  -47.189  -14.318  0.00 45.62  ? 504 MG    B MG     1 
HETATM 17257 N  N12    . A1D6D N 10 .   ? 17.889  -66.599  -41.772  1.00 42.44  ? 505 A1D6D B N12    1 
HETATM 17258 C  C13    . A1D6D N 10 .   ? 19.143  -67.266  -41.717  1.00 46.41  ? 505 A1D6D B C13    1 
HETATM 17259 C  C17    . A1D6D N 10 .   ? 18.233  -66.190  -44.116  1.00 39.78  ? 505 A1D6D B C17    1 
HETATM 17260 C  C20    . A1D6D N 10 .   ? 16.872  -63.755  -44.005  1.00 37.57  ? 505 A1D6D B C20    1 
HETATM 17261 C  C21    . A1D6D N 10 .   ? 17.404  -64.202  -45.232  1.00 41.11  ? 505 A1D6D B C21    1 
HETATM 17262 C  C22    . A1D6D N 10 .   ? 18.089  -65.408  -45.284  1.00 36.62  ? 505 A1D6D B C22    1 
HETATM 17263 C  C24    . A1D6D N 10 .   ? 16.472  -62.287  -46.227  1.00 38.92  ? 505 A1D6D B C24    1 
HETATM 17264 C  C01    . A1D6D N 10 .   ? 13.524  -66.485  -41.932  1.00 47.03  ? 505 A1D6D B C01    1 
HETATM 17265 C  C02    . A1D6D N 10 .   ? 12.825  -66.456  -40.735  1.00 46.35  ? 505 A1D6D B C02    1 
HETATM 17266 C  C03    . A1D6D N 10 .   ? 13.528  -66.479  -39.540  1.00 49.87  ? 505 A1D6D B C03    1 
HETATM 17267 C  C04    . A1D6D N 10 .   ? 14.949  -66.508  -39.505  1.00 48.46  ? 505 A1D6D B C04    1 
HETATM 17268 C  C05    . A1D6D N 10 .   ? 15.635  -66.523  -40.674  1.00 43.81  ? 505 A1D6D B C05    1 
HETATM 17269 C  C06    . A1D6D N 10 .   ? 14.919  -66.515  -41.909  1.00 43.47  ? 505 A1D6D B C06    1 
HETATM 17270 C  C07    . A1D6D N 10 .   ? 17.052  -66.561  -40.579  1.00 41.79  ? 505 A1D6D B C07    1 
HETATM 17271 C  C09    . A1D6D N 10 .   ? 16.923  -66.567  -38.228  1.00 48.17  ? 505 A1D6D B C09    1 
HETATM 17272 C  C14    . A1D6D N 10 .   ? 19.475  -68.094  -42.987  1.00 41.65  ? 505 A1D6D B C14    1 
HETATM 17273 C  C18    . A1D6D N 10 .   ? 17.703  -65.754  -42.934  1.00 37.30  ? 505 A1D6D B C18    1 
HETATM 17274 C  C19    . A1D6D N 10 .   ? 17.018  -64.526  -42.872  1.00 37.55  ? 505 A1D6D B C19    1 
HETATM 17275 F  F25    . A1D6D N 10 .   ? 12.825  -66.478  -43.109  1.00 47.83  ? 505 A1D6D B F25    1 
HETATM 17276 N  N08    . A1D6D N 10 .   ? 17.622  -66.581  -39.364  1.00 49.95  ? 505 A1D6D B N08    1 
HETATM 17277 N  N10    . A1D6D N 10 .   ? 15.605  -66.533  -38.294  1.00 57.43  ? 505 A1D6D B N10    1 
HETATM 17278 N  N16    . A1D6D N 10 .   ? 18.972  -67.483  -44.189  1.00 40.86  ? 505 A1D6D B N16    1 
HETATM 17279 O  O15    . A1D6D N 10 .   ? 20.081  -69.110  -42.962  1.00 44.01  ? 505 A1D6D B O15    1 
HETATM 17280 O  O23    . A1D6D N 10 .   ? 17.270  -63.434  -46.404  1.00 40.40  ? 505 A1D6D B O23    1 
HETATM 17281 CL CL11   . A1D6D N 10 .   ? 17.721  -66.598  -36.647  1.00 132.02 ? 505 A1D6D B CL11   1 
HETATM 17282 H  H131   . A1D6D N 10 .   ? 19.921  -66.523  -41.579  1.00 55.69  ? 505 A1D6D B H131   1 
HETATM 17283 H  H132   . A1D6D N 10 .   ? 19.137  -67.936  -40.863  1.00 55.69  ? 505 A1D6D B H132   1 
HETATM 17284 H  H201   . A1D6D N 10 .   ? 16.350  -62.808  -43.953  1.00 45.09  ? 505 A1D6D B H201   1 
HETATM 17285 H  H221   . A1D6D N 10 .   ? 18.512  -65.749  -46.221  1.00 43.95  ? 505 A1D6D B H221   1 
HETATM 17286 H  H243   . A1D6D N 10 .   ? 17.052  -61.515  -45.729  1.00 46.71  ? 505 A1D6D B H243   1 
HETATM 17287 H  H242   . A1D6D N 10 .   ? 15.606  -62.538  -45.620  1.00 46.71  ? 505 A1D6D B H242   1 
HETATM 17288 H  H241   . A1D6D N 10 .   ? 16.141  -61.923  -47.197  1.00 46.71  ? 505 A1D6D B H241   1 
HETATM 17289 H  H021   . A1D6D N 10 .   ? 11.743  -66.416  -40.733  1.00 55.63  ? 505 A1D6D B H021   1 
HETATM 17290 H  H031   . A1D6D N 10 .   ? 12.979  -66.476  -38.607  1.00 59.85  ? 505 A1D6D B H031   1 
HETATM 17291 H  H061   . A1D6D N 10 .   ? 15.467  -66.532  -42.843  1.00 52.17  ? 505 A1D6D B H061   1 
HETATM 17292 H  H191   . A1D6D N 10 .   ? 16.604  -64.186  -41.930  1.00 45.06  ? 505 A1D6D B H191   1 
HETATM 17293 H  H161   . A1D6D N 10 .   ? 19.118  -67.926  -45.074  1.00 49.04  ? 505 A1D6D B H161   1 
HETATM 17294 P  PG     . GTP   O 5  .   ? 20.273  -18.563  16.729   0.00 35.62  ? 501 GTP   C PG     1 
HETATM 17295 O  O1G    . GTP   O 5  .   ? 20.140  -17.155  16.200   0.00 36.49  ? 501 GTP   C O1G    1 
HETATM 17296 O  O2G    . GTP   O 5  .   ? 21.678  -18.764  17.247   0.00 36.53  ? 501 GTP   C O2G    1 
HETATM 17297 O  O3G    . GTP   O 5  .   ? 19.275  -18.786  17.840   0.00 37.10  ? 501 GTP   C O3G    1 
HETATM 17298 O  O3B    . GTP   O 5  .   ? 19.991  -19.592  15.523   0.00 34.26  ? 501 GTP   C O3B    1 
HETATM 17299 P  PB     . GTP   O 5  .   ? 18.603  -20.406  15.447   0.00 33.25  ? 501 GTP   C PB     1 
HETATM 17300 O  O1B    . GTP   O 5  .   ? 18.690  -21.405  14.318   0.00 32.75  ? 501 GTP   C O1B    1 
HETATM 17301 O  O2B    . GTP   O 5  .   ? 18.314  -21.098  16.758   0.00 33.79  ? 501 GTP   C O2B    1 
HETATM 17302 O  O3A    . GTP   O 5  .   ? 17.474  -19.305  15.113   0.00 33.47  ? 501 GTP   C O3A    1 
HETATM 17303 P  PA     . GTP   O 5  .   ? 16.119  -19.722  14.344   0.00 32.74  ? 501 GTP   C PA     1 
HETATM 17304 O  O1A    . GTP   O 5  .   ? 16.190  -21.168  13.913   0.00 31.81  ? 501 GTP   C O1A    1 
HETATM 17305 O  O2A    . GTP   O 5  .   ? 14.916  -19.488  15.227   0.00 33.88  ? 501 GTP   C O2A    1 
HETATM 17306 O  "O5'"  . GTP   O 5  .   ? 16.070  -18.766  13.048   0.00 33.26  ? 501 GTP   C "O5'"  1 
HETATM 17307 C  "C5'"  . GTP   O 5  .   ? 15.130  -17.718  12.948   0.00 34.84  ? 501 GTP   C "C5'"  1 
HETATM 17308 C  "C4'"  . GTP   O 5  .   ? 14.031  -18.089  11.958   0.00 35.05  ? 501 GTP   C "C4'"  1 
HETATM 17309 O  "O4'"  . GTP   O 5  .   ? 13.643  -19.435  12.150   0.00 33.84  ? 501 GTP   C "O4'"  1 
HETATM 17310 C  "C3'"  . GTP   O 5  .   ? 12.787  -17.237  12.151   0.00 38.00  ? 501 GTP   C "C3'"  1 
HETATM 17311 O  "O3'"  . GTP   O 5  .   ? 12.587  -16.417  11.024   0.00 38.42  ? 501 GTP   C "O3'"  1 
HETATM 17312 C  "C2'"  . GTP   O 5  .   ? 11.638  -18.218  12.275   0.00 36.62  ? 501 GTP   C "C2'"  1 
HETATM 17313 O  "O2'"  . GTP   O 5  .   ? 10.619  -17.913  11.351   0.00 36.52  ? 501 GTP   C "O2'"  1 
HETATM 17314 C  "C1'"  . GTP   O 5  .   ? 12.247  -19.582  11.987   0.00 33.94  ? 501 GTP   C "C1'"  1 
HETATM 17315 N  N9     . GTP   O 5  .   ? 11.741  -20.583  12.941   0.00 33.74  ? 501 GTP   C N9     1 
HETATM 17316 C  C8     . GTP   O 5  .   ? 12.131  -20.737  14.245   0.00 33.91  ? 501 GTP   C C8     1 
HETATM 17317 N  N7     . GTP   O 5  .   ? 11.442  -21.771  14.779   0.00 34.10  ? 501 GTP   C N7     1 
HETATM 17318 C  C5     . GTP   O 5  .   ? 10.625  -22.285  13.833   0.00 34.35  ? 501 GTP   C C5     1 
HETATM 17319 C  C6     . GTP   O 5  .   ? 9.719   -23.337  13.847   0.00 34.86  ? 501 GTP   C C6     1 
HETATM 17320 O  O6     . GTP   O 5  .   ? 9.552   -23.995  14.872   0.00 35.75  ? 501 GTP   C O6     1 
HETATM 17321 N  N1     . GTP   O 5  .   ? 9.008   -23.641  12.705   0.00 35.03  ? 501 GTP   C N1     1 
HETATM 17322 C  C2     . GTP   O 5  .   ? 9.201   -22.899  11.558   0.00 33.40  ? 501 GTP   C C2     1 
HETATM 17323 N  N2     . GTP   O 5  .   ? 8.515   -23.190  10.456   0.00 33.25  ? 501 GTP   C N2     1 
HETATM 17324 N  N3     . GTP   O 5  .   ? 10.103  -21.854  11.551   0.00 33.18  ? 501 GTP   C N3     1 
HETATM 17325 C  C4     . GTP   O 5  .   ? 10.805  -21.550  12.670   0.00 33.70  ? 501 GTP   C C4     1 
HETATM 17326 CA CA     . CA    P 6  .   ? 13.866  -54.830  10.731   0.00 59.98  ? 502 CA    C CA     1 
HETATM 17327 MG MG     . MG    Q 7  .   ? 18.624  -20.171  19.171   0.00 39.63  ? 503 MG    C MG     1 
HETATM 17328 P  PB     . GDP   R 8  .   ? 25.166  10.337   44.092   0.00 80.60  ? 501 GDP   D PB     1 
HETATM 17329 O  O1B    . GDP   R 8  .   ? 26.658  10.157   43.937   0.00 79.29  ? 501 GDP   D O1B    1 
HETATM 17330 O  O2B    . GDP   R 8  .   ? 24.540  8.979    44.341   0.00 80.51  ? 501 GDP   D O2B    1 
HETATM 17331 O  O3B    . GDP   R 8  .   ? 24.859  11.249   45.259   0.00 82.41  ? 501 GDP   D O3B    1 
HETATM 17332 O  O3A    . GDP   R 8  .   ? 24.553  10.940   42.726   0.00 80.68  ? 501 GDP   D O3A    1 
HETATM 17333 P  PA     . GDP   R 8  .   ? 23.052  11.520   42.723   0.00 81.04  ? 501 GDP   D PA     1 
HETATM 17334 O  O1A    . GDP   R 8  .   ? 22.088  10.366   42.585   0.00 79.76  ? 501 GDP   D O1A    1 
HETATM 17335 O  O2A    . GDP   R 8  .   ? 22.793  12.311   43.980   0.00 81.76  ? 501 GDP   D O2A    1 
HETATM 17336 O  "O5'"  . GDP   R 8  .   ? 22.932  12.483   41.443   0.00 80.08  ? 501 GDP   D "O5'"  1 
HETATM 17337 C  "C5'"  . GDP   R 8  .   ? 22.021  13.576   41.518   0.00 79.98  ? 501 GDP   D "C5'"  1 
HETATM 17338 C  "C4'"  . GDP   R 8  .   ? 21.098  13.602   40.305   0.00 78.90  ? 501 GDP   D "C4'"  1 
HETATM 17339 O  "O4'"  . GDP   R 8  .   ? 20.380  12.368   40.243   0.00 77.69  ? 501 GDP   D "O4'"  1 
HETATM 17340 C  "C3'"  . GDP   R 8  .   ? 20.070  14.716   40.432   0.00 79.54  ? 501 GDP   D "C3'"  1 
HETATM 17341 O  "O3'"  . GDP   R 8  .   ? 20.111  15.551   39.275   0.00 80.44  ? 501 GDP   D "O3'"  1 
HETATM 17342 C  "C2'"  . GDP   R 8  .   ? 18.717  14.043   40.507   0.00 78.08  ? 501 GDP   D "C2'"  1 
HETATM 17343 O  "O2'"  . GDP   R 8  .   ? 17.814  14.634   39.568   0.00 78.45  ? 501 GDP   D "O2'"  1 
HETATM 17344 C  "C1'"  . GDP   R 8  .   ? 18.970  12.586   40.162   0.00 76.81  ? 501 GDP   D "C1'"  1 
HETATM 17345 N  N9     . GDP   R 8  .   ? 18.281  11.706   41.137   0.00 75.68  ? 501 GDP   D N9     1 
HETATM 17346 C  C8     . GDP   R 8  .   ? 18.690  11.463   42.396   0.00 76.39  ? 501 GDP   D C8     1 
HETATM 17347 N  N7     . GDP   R 8  .   ? 17.844  10.611   43.029   0.00 75.12  ? 501 GDP   D N7     1 
HETATM 17348 C  C5     . GDP   R 8  .   ? 16.868  10.293   42.159   0.00 73.90  ? 501 GDP   D C5     1 
HETATM 17349 C  C6     . GDP   R 8  .   ? 15.656  9.441    42.179   0.00 73.08  ? 501 GDP   D C6     1 
HETATM 17350 O  O6     . GDP   R 8  .   ? 15.339  8.795    43.201   0.00 73.36  ? 501 GDP   D O6     1 
HETATM 17351 N  N1     . GDP   R 8  .   ? 14.910  9.385    41.068   0.00 72.20  ? 501 GDP   D N1     1 
HETATM 17352 C  C2     . GDP   R 8  .   ? 15.226  10.069   39.952   0.00 72.09  ? 501 GDP   D C2     1 
HETATM 17353 N  N2     . GDP   R 8  .   ? 14.418  9.956    38.871   0.00 71.07  ? 501 GDP   D N2     1 
HETATM 17354 N  N3     . GDP   R 8  .   ? 16.321  10.868   39.863   0.00 73.27  ? 501 GDP   D N3     1 
HETATM 17355 C  C4     . GDP   R 8  .   ? 17.161  11.016   40.914   0.00 74.17  ? 501 GDP   D C4     1 
HETATM 17356 N  N12    . A1D6D S 10 .   ? 14.673  -8.748   20.727   1.00 57.11  ? 502 A1D6D D N12    1 
HETATM 17357 C  C13    . A1D6D S 10 .   ? 15.607  -9.813   20.598   1.00 50.69  ? 502 A1D6D D C13    1 
HETATM 17358 C  C17    . A1D6D S 10 .   ? 14.413  -8.612   18.298   1.00 48.47  ? 502 A1D6D D C17    1 
HETATM 17359 C  C20    . A1D6D S 10 .   ? 13.940  -5.874   18.365   1.00 44.51  ? 502 A1D6D D C20    1 
HETATM 17360 C  C21    . A1D6D S 10 .   ? 13.936  -6.534   17.133   1.00 46.07  ? 502 A1D6D D C21    1 
HETATM 17361 C  C22    . A1D6D S 10 .   ? 14.163  -7.904   17.091   1.00 44.01  ? 502 A1D6D D C22    1 
HETATM 17362 C  C24    . A1D6D S 10 .   ? 12.409  -5.836   15.508   1.00 55.58  ? 502 A1D6D D C24    1 
HETATM 17363 C  C01    . A1D6D S 10 .   ? 10.575  -7.449   21.460   1.00 56.98  ? 502 A1D6D D C01    1 
HETATM 17364 C  C02    . A1D6D S 10 .   ? 10.195  -7.072   22.742   1.00 57.96  ? 502 A1D6D D C02    1 
HETATM 17365 C  C03    . A1D6D S 10 .   ? 11.122  -7.120   23.774   1.00 57.74  ? 502 A1D6D D C03    1 
HETATM 17366 C  C04    . A1D6D S 10 .   ? 12.458  -7.540   23.526   1.00 63.01  ? 502 A1D6D D C04    1 
HETATM 17367 C  C05    . A1D6D S 10 .   ? 12.839  -7.908   22.266   1.00 65.49  ? 502 A1D6D D C05    1 
HETATM 17368 C  C06    . A1D6D S 10 .   ? 11.871  -7.873   21.217   1.00 60.93  ? 502 A1D6D D C06    1 
HETATM 17369 C  C07    . A1D6D S 10 .   ? 14.195  -8.325   22.049   1.00 62.86  ? 502 A1D6D D C07    1 
HETATM 17370 C  C09    . A1D6D S 10 .   ? 14.601  -7.982   24.322   1.00 64.36  ? 502 A1D6D D C09    1 
HETATM 17371 C  C14    . A1D6D S 10 .   ? 15.264  -10.750  19.409   1.00 48.64  ? 502 A1D6D D C14    1 
HETATM 17372 C  C18    . A1D6D S 10 .   ? 14.423  -7.966   19.510   1.00 53.04  ? 502 A1D6D D C18    1 
HETATM 17373 C  C19    . A1D6D S 10 .   ? 14.178  -6.572   19.542   1.00 47.72  ? 502 A1D6D D C19    1 
HETATM 17374 F  F25    . A1D6D S 10 .   ? 9.689   -7.422   20.435   1.00 57.91  ? 502 A1D6D D F25    1 
HETATM 17375 N  N08    . A1D6D S 10 .   ? 15.014  -8.343   23.101   1.00 66.96  ? 502 A1D6D D N08    1 
HETATM 17376 N  N10    . A1D6D S 10 .   ? 13.360  -7.588   24.544   1.00 66.86  ? 502 A1D6D D N10    1 
HETATM 17377 N  N16    . A1D6D S 10 .   ? 14.667  -10.073  18.276   1.00 48.92  ? 502 A1D6D D N16    1 
HETATM 17378 O  O15    . A1D6D S 10 .   ? 15.478  -11.920  19.404   1.00 54.97  ? 502 A1D6D D O15    1 
HETATM 17379 O  O23    . A1D6D S 10 .   ? 13.724  -5.794   15.964   1.00 44.60  ? 502 A1D6D D O23    1 
HETATM 17380 CL CL11   . A1D6D S 10 .   ? 15.734  -8.017   25.689   1.00 132.02 ? 502 A1D6D D CL11   1 
HETATM 17381 H  H131   . A1D6D S 10 .   ? 16.596  -9.395   20.442   1.00 60.83  ? 502 A1D6D D H131   1 
HETATM 17382 H  H132   . A1D6D S 10 .   ? 15.607  -10.393  21.515   1.00 60.83  ? 502 A1D6D D H132   1 
HETATM 17383 H  H201   . A1D6D S 10 .   ? 13.756  -4.807   18.402   1.00 53.41  ? 502 A1D6D D H201   1 
HETATM 17384 H  H221   . A1D6D S 10 .   ? 14.150  -8.430   16.144   1.00 52.81  ? 502 A1D6D D H221   1 
HETATM 17385 H  H243   . A1D6D S 10 .   ? 12.233  -5.004   14.832   1.00 66.70  ? 502 A1D6D D H243   1 
HETATM 17386 H  H242   . A1D6D S 10 .   ? 11.730  -5.765   16.354   1.00 66.70  ? 502 A1D6D D H242   1 
HETATM 17387 H  H241   . A1D6D S 10 .   ? 12.237  -6.772   14.983   1.00 66.70  ? 502 A1D6D D H241   1 
HETATM 17388 H  H021   . A1D6D S 10 .   ? 9.181   -6.743   22.936   1.00 69.56  ? 502 A1D6D D H021   1 
HETATM 17389 H  H031   . A1D6D S 10 .   ? 10.825  -6.835   24.775   1.00 69.30  ? 502 A1D6D D H031   1 
HETATM 17390 H  H061   . A1D6D S 10 .   ? 12.154  -8.183   20.219   1.00 73.12  ? 502 A1D6D D H061   1 
HETATM 17391 H  H191   . A1D6D S 10 .   ? 14.176  -6.047   20.489   1.00 57.27  ? 502 A1D6D D H191   1 
HETATM 17392 H  H161   . A1D6D S 10 .   ? 14.422  -10.602  17.462   1.00 58.70  ? 502 A1D6D D H161   1 
HETATM 17393 P  PG     . ACP   T 11 .   ? 8.329   -48.910  -93.411  0.00 96.69  ? 401 ACP   F PG     1 
HETATM 17394 O  O1G    . ACP   T 11 .   ? 7.146   -49.680  -93.901  0.00 91.33  ? 401 ACP   F O1G    1 
HETATM 17395 O  O2G    . ACP   T 11 .   ? 7.931   -47.772  -92.447  0.00 97.27  ? 401 ACP   F O2G    1 
HETATM 17396 O  O3G    . ACP   T 11 .   ? 9.361   -49.797  -92.681  0.00 94.66  ? 401 ACP   F O3G    1 
HETATM 17397 P  PB     . ACP   T 11 .   ? 9.848   -49.368  -95.947  0.00 100.51 ? 401 ACP   F PB     1 
HETATM 17398 O  O1B    . ACP   T 11 .   ? 8.731   -50.298  -96.354  0.00 98.34  ? 401 ACP   F O1B    1 
HETATM 17399 O  O2B    . ACP   T 11 .   ? 11.046  -50.125  -95.299  0.00 99.26  ? 401 ACP   F O2B    1 
HETATM 17400 C  C3B    . ACP   T 11 .   ? 9.205   -48.131  -94.770  0.00 101.19 ? 401 ACP   F C3B    1 
HETATM 17401 P  PA     . ACP   T 11 .   ? 10.794  -49.572  -98.392  0.00 105.48 ? 401 ACP   F PA     1 
HETATM 17402 O  O1A    . ACP   T 11 .   ? 9.756   -50.591  -98.647  0.00 103.10 ? 401 ACP   F O1A    1 
HETATM 17403 O  O2A    . ACP   T 11 .   ? 12.145  -50.163  -97.980  0.00 105.74 ? 401 ACP   F O2A    1 
HETATM 17404 O  O3A    . ACP   T 11 .   ? 10.363  -48.563  -97.242  0.00 104.70 ? 401 ACP   F O3A    1 
HETATM 17405 O  "O5'"  . ACP   T 11 .   ? 11.004  -48.562  -99.591  0.00 106.04 ? 401 ACP   F "O5'"  1 
HETATM 17406 C  "C5'"  . ACP   T 11 .   ? 10.734  -48.939  -100.957 0.00 104.97 ? 401 ACP   F "C5'"  1 
HETATM 17407 C  "C4'"  . ACP   T 11 .   ? 9.353   -48.490  -101.363 0.00 104.49 ? 401 ACP   F "C4'"  1 
HETATM 17408 O  "O4'"  . ACP   T 11 .   ? 9.285   -48.659  -102.794 0.00 103.72 ? 401 ACP   F "O4'"  1 
HETATM 17409 C  "C3'"  . ACP   T 11 .   ? 8.316   -49.467  -100.829 0.00 103.63 ? 401 ACP   F "C3'"  1 
HETATM 17410 O  "O3'"  . ACP   T 11 .   ? 7.748   -48.839  -99.686  0.00 104.53 ? 401 ACP   F "O3'"  1 
HETATM 17411 C  "C2'"  . ACP   T 11 .   ? 7.252   -49.430  -101.918 0.00 102.37 ? 401 ACP   F "C2'"  1 
HETATM 17412 O  "O2'"  . ACP   T 11 .   ? 6.628   -48.155  -101.857 0.00 103.02 ? 401 ACP   F "O2'"  1 
HETATM 17413 C  "C1'"  . ACP   T 11 .   ? 8.137   -49.398  -103.161 0.00 102.30 ? 401 ACP   F "C1'"  1 
HETATM 17414 N  N9     . ACP   T 11 .   ? 8.601   -50.735  -103.516 0.00 100.62 ? 401 ACP   F N9     1 
HETATM 17415 C  C8     . ACP   T 11 .   ? 9.280   -51.628  -102.726 0.00 99.55  ? 401 ACP   F C8     1 
HETATM 17416 N  N7     . ACP   T 11 .   ? 9.570   -52.758  -103.320 0.00 98.36  ? 401 ACP   F N7     1 
HETATM 17417 C  C5     . ACP   T 11 .   ? 9.052   -52.597  -104.594 0.00 99.40  ? 401 ACP   F C5     1 
HETATM 17418 C  C6     . ACP   T 11 .   ? 9.030   -53.437  -105.721 0.00 99.44  ? 401 ACP   F C6     1 
HETATM 17419 N  N6     . ACP   T 11 .   ? 9.564   -54.662  -105.749 0.00 98.70  ? 401 ACP   F N6     1 
HETATM 17420 N  N1     . ACP   T 11 .   ? 8.431   -52.972  -106.835 0.00 99.82  ? 401 ACP   F N1     1 
HETATM 17421 C  C2     . ACP   T 11 .   ? 7.896   -51.749  -106.819 0.00 99.37  ? 401 ACP   F C2     1 
HETATM 17422 N  N3     . ACP   T 11 .   ? 7.854   -50.868  -105.820 0.00 99.66  ? 401 ACP   F N3     1 
HETATM 17423 C  C4     . ACP   T 11 .   ? 8.452   -51.355  -104.729 0.00 99.76  ? 401 ACP   F C4     1 
HETATM 17424 H  H3B1   . ACP   T 11 .   ? 8.597   -47.537  -95.237  0.00 121.44 ? 401 ACP   F H3B1   1 
HETATM 17425 H  H3B2   . ACP   T 11 .   ? 9.948   -47.618  -94.414  0.00 121.44 ? 401 ACP   F H3B2   1 
HETATM 17426 H  "H5'1" . ACP   T 11 .   ? 10.792  -49.904  -101.042 0.00 125.97 ? 401 ACP   F "H5'1" 1 
HETATM 17427 H  "H5'2" . ACP   T 11 .   ? 11.388  -48.524  -101.541 0.00 125.97 ? 401 ACP   F "H5'2" 1 
HETATM 17428 H  "H4'"  . ACP   T 11 .   ? 9.152   -47.573  -101.118 0.00 125.39 ? 401 ACP   F "H4'"  1 
HETATM 17429 H  "H3'"  . ACP   T 11 .   ? 8.677   -50.356  -100.691 0.00 124.36 ? 401 ACP   F "H3'"  1 
HETATM 17430 H  "HO3'" . ACP   T 11 .   ? 6.913   -48.998  -99.701  0.00 125.44 ? 401 ACP   F "HO3'" 1 
HETATM 17431 H  "H2'"  . ACP   T 11 .   ? 6.652   -50.192  -101.891 0.00 122.85 ? 401 ACP   F "H2'"  1 
HETATM 17432 H  "HO2'" . ACP   T 11 .   ? 5.844   -48.253  -102.173 0.00 123.63 ? 401 ACP   F "HO2'" 1 
HETATM 17433 H  "H1'"  . ACP   T 11 .   ? 7.683   -48.965  -103.901 0.00 122.77 ? 401 ACP   F "H1'"  1 
HETATM 17434 H  H8     . ACP   T 11 .   ? 9.514   -51.446  -101.844 0.00 119.47 ? 401 ACP   F H8     1 
HETATM 17435 H  HN61   . ACP   T 11 .   ? 10.216  -54.858  -105.224 0.00 118.44 ? 401 ACP   F HN61   1 
HETATM 17436 H  HN62   . ACP   T 11 .   ? 9.254   -55.251  -106.293 0.00 118.44 ? 401 ACP   F HN62   1 
HETATM 17437 H  H2     . ACP   T 11 .   ? 7.498   -51.475  -107.614 0.00 119.25 ? 401 ACP   F H2     1 
# 
