data_9LNL
# 
_entry.id   9LNL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9LNL         pdb_00009lnl 10.2210/pdb9lnl/pdb 
WWPDB D_1300056057 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_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                        9LNL 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-21 
_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         Wang 
_pdbx_contact_author.name_last          Yuxi 
_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 ? 
'Chen, Q.F.' 3 ? 
# 
_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                     'Crystal structure of T2R-TTL-YQVB15 complex' 
_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 ? 
primary 'Chen, Q.F.' 3 ? 
# 
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'    50041.273 2 ? ? ? ? 
2  polymer     man 'Tubulin beta-2B chain'                   49999.887 2 ? ? ? ? 
3  polymer     man Stathmin-4                                16844.162 1 ? ? ? ? 
4  polymer     man 'Tubulin tyrosine ligase'                 44378.496 1 ? ? ? ? 
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    2 ? ? ? ? 
8  non-polymer syn "10',11'-difluoro-12'-methoxyvinblastine" 876.981   1 ? ? ? ? 
9  non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                443.201   2 ? ? ? ? 
10 water       nat water                                     18.015    7 ? ? ? ? 
# 
_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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
A,C ? 
2 'polypeptide(L)' no no 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
D,B ? 
3 'polypeptide(L)' no no 
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
;MADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREV
IQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
E   ? 
4 'polypeptide(L)' no no 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHHHHHH
;
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL
IKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDEREVFLAAYNRRREGREGNVWIAKSSAGAKGEGI
LISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQDKTCHL
TNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFM
VDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQKTSQPTSIFIKLHHHHHH
;
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  "10',11'-difluoro-12'-methoxyvinblastine" A1EPQ 
9  "GUANOSINE-5'-DIPHOSPHATE"                GDP   
10 water                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
1 441 GLU n 
1 442 GLY n 
1 443 GLU n 
1 444 GLY n 
1 445 GLU n 
1 446 GLU n 
1 447 GLU n 
1 448 GLY n 
1 449 GLU n 
1 450 GLU 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 
2 432 GLU n 
2 433 GLN n 
2 434 GLY n 
2 435 GLU n 
2 436 PHE n 
2 437 GLU n 
2 438 GLU n 
2 439 GLU n 
2 440 GLU n 
2 441 GLY n 
2 442 GLU n 
2 443 ASP n 
2 444 GLU n 
2 445 ALA n 
3 1   MET n 
3 2   ALA n 
3 3   ASP n 
3 4   MET n 
3 5   GLU n 
3 6   VAL n 
3 7   ILE n 
3 8   GLU n 
3 9   LEU n 
3 10  ASN n 
3 11  LYS n 
3 12  CYS n 
3 13  THR n 
3 14  SER n 
3 15  GLY n 
3 16  GLN n 
3 17  SER n 
3 18  PHE n 
3 19  GLU n 
3 20  VAL n 
3 21  ILE n 
3 22  LEU n 
3 23  LYS n 
3 24  PRO n 
3 25  PRO n 
3 26  SER n 
3 27  PHE n 
3 28  ASP n 
3 29  GLY n 
3 30  VAL n 
3 31  PRO n 
3 32  GLU n 
3 33  PHE n 
3 34  ASN n 
3 35  ALA n 
3 36  SER n 
3 37  LEU n 
3 38  PRO n 
3 39  ARG n 
3 40  ARG n 
3 41  ARG n 
3 42  ASP n 
3 43  PRO n 
3 44  SER n 
3 45  LEU n 
3 46  GLU n 
3 47  GLU n 
3 48  ILE n 
3 49  GLN n 
3 50  LYS n 
3 51  LYS n 
3 52  LEU n 
3 53  GLU n 
3 54  ALA n 
3 55  ALA n 
3 56  GLU n 
3 57  GLU n 
3 58  ARG n 
3 59  ARG n 
3 60  LYS n 
3 61  TYR n 
3 62  GLN n 
3 63  GLU n 
3 64  ALA n 
3 65  GLU n 
3 66  LEU n 
3 67  LEU n 
3 68  LYS n 
3 69  HIS n 
3 70  LEU n 
3 71  ALA n 
3 72  GLU n 
3 73  LYS n 
3 74  ARG n 
3 75  GLU n 
3 76  HIS n 
3 77  GLU n 
3 78  ARG n 
3 79  GLU n 
3 80  VAL n 
3 81  ILE n 
3 82  GLN n 
3 83  LYS n 
3 84  ALA n 
3 85  ILE n 
3 86  GLU n 
3 87  GLU n 
3 88  ASN n 
3 89  ASN n 
3 90  ASN n 
3 91  PHE n 
3 92  ILE n 
3 93  LYS n 
3 94  MET n 
3 95  ALA n 
3 96  LYS n 
3 97  GLU n 
3 98  LYS n 
3 99  LEU n 
3 100 ALA n 
3 101 GLN n 
3 102 LYS n 
3 103 MET n 
3 104 GLU n 
3 105 SER n 
3 106 ASN n 
3 107 LYS n 
3 108 GLU n 
3 109 ASN n 
3 110 ARG n 
3 111 GLU n 
3 112 ALA n 
3 113 HIS n 
3 114 LEU n 
3 115 ALA n 
3 116 ALA n 
3 117 MET n 
3 118 LEU n 
3 119 GLU n 
3 120 ARG n 
3 121 LEU n 
3 122 GLN n 
3 123 GLU n 
3 124 LYS n 
3 125 ASP n 
3 126 LYS n 
3 127 HIS n 
3 128 ALA n 
3 129 GLU n 
3 130 GLU n 
3 131 VAL n 
3 132 ARG n 
3 133 LYS n 
3 134 ASN n 
3 135 LYS n 
3 136 GLU n 
3 137 LEU n 
3 138 LYS n 
3 139 GLU n 
3 140 GLU n 
3 141 ALA n 
3 142 SER n 
3 143 ARG 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 
4 381 HIS n 
4 382 HIS n 
4 383 HIS n 
4 384 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' 1 450 pig               ? TUBA1B ? ? ? ? ? ? 'Sus scrofa'        9823  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 445 'domestic cattle' ? TUBB2B ? ? ? ? ? ? 'Bos taurus'        9913  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 143 'Norway rat'      ? Stmn4  ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 384 chicken           ? TTL    ? ? ? ? ? ? '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 
A1EPQ non-polymer         . "10',11'-difluoro-12'-methoxyvinblastine" ? 'C47 H58 F2 N4 O10' 876.981 
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 
HOH   non-polymer         . WATER                                     ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                   ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                    ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                ? 'C5 H11 N O2 S'     149.211 
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 438 438 438 ASP ASP A . n 
A 1 439 SER 439 439 439 SER SER A . n 
A 1 440 VAL 440 440 ?   ?   ?   A . n 
A 1 441 GLU 441 441 ?   ?   ?   A . n 
A 1 442 GLY 442 442 ?   ?   ?   A . n 
A 1 443 GLU 443 443 ?   ?   ?   A . n 
A 1 444 GLY 444 444 ?   ?   ?   A . n 
A 1 445 GLU 445 445 ?   ?   ?   A . n 
A 1 446 GLU 446 446 ?   ?   ?   A . n 
A 1 447 GLU 447 447 ?   ?   ?   A . n 
A 1 448 GLY 448 448 ?   ?   ?   A . n 
A 1 449 GLU 449 449 ?   ?   ?   A . n 
A 1 450 GLU 450 450 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET C . n 
B 1 2   ARG 2   2   2   ARG ARG C . n 
B 1 3   GLU 3   3   3   GLU GLU C . n 
B 1 4   CYS 4   4   4   CYS CYS C . n 
B 1 5   ILE 5   5   5   ILE ILE C . n 
B 1 6   SER 6   6   6   SER SER C . n 
B 1 7   ILE 7   7   7   ILE ILE C . n 
B 1 8   HIS 8   8   8   HIS HIS C . n 
B 1 9   VAL 9   9   9   VAL VAL C . n 
B 1 10  GLY 10  10  10  GLY GLY C . n 
B 1 11  GLN 11  11  11  GLN GLN C . n 
B 1 12  ALA 12  12  12  ALA ALA C . n 
B 1 13  GLY 13  13  13  GLY GLY C . n 
B 1 14  VAL 14  14  14  VAL VAL C . n 
B 1 15  GLN 15  15  15  GLN GLN C . n 
B 1 16  ILE 16  16  16  ILE ILE C . n 
B 1 17  GLY 17  17  17  GLY GLY C . n 
B 1 18  ASN 18  18  18  ASN ASN C . n 
B 1 19  ALA 19  19  19  ALA ALA C . n 
B 1 20  CYS 20  20  20  CYS CYS C . n 
B 1 21  TRP 21  21  21  TRP TRP C . n 
B 1 22  GLU 22  22  22  GLU GLU C . n 
B 1 23  LEU 23  23  23  LEU LEU C . n 
B 1 24  TYR 24  24  24  TYR TYR C . n 
B 1 25  CYS 25  25  25  CYS CYS C . n 
B 1 26  LEU 26  26  26  LEU LEU C . n 
B 1 27  GLU 27  27  27  GLU GLU C . n 
B 1 28  HIS 28  28  28  HIS HIS C . n 
B 1 29  GLY 29  29  29  GLY GLY C . n 
B 1 30  ILE 30  30  30  ILE ILE C . n 
B 1 31  GLN 31  31  31  GLN GLN C . n 
B 1 32  PRO 32  32  32  PRO PRO C . n 
B 1 33  ASP 33  33  33  ASP ASP C . n 
B 1 34  GLY 34  34  34  GLY GLY C . n 
B 1 35  GLN 35  35  35  GLN GLN C . n 
B 1 36  MET 36  36  36  MET MET C . n 
B 1 37  PRO 37  37  37  PRO PRO C . n 
B 1 38  SER 38  38  38  SER SER C . n 
B 1 39  ASP 39  39  39  ASP ASP C . n 
B 1 40  LYS 40  40  40  LYS LYS C . n 
B 1 41  THR 41  41  41  THR THR C . n 
B 1 42  ILE 42  42  42  ILE ILE C . n 
B 1 43  GLY 43  43  43  GLY GLY C . n 
B 1 44  GLY 44  44  44  GLY GLY C . n 
B 1 45  GLY 45  45  45  GLY GLY C . n 
B 1 46  ASP 46  46  46  ASP ASP C . n 
B 1 47  ASP 47  47  47  ASP ASP C . n 
B 1 48  SER 48  48  48  SER SER C . n 
B 1 49  PHE 49  49  49  PHE PHE C . n 
B 1 50  ASN 50  50  50  ASN ASN C . n 
B 1 51  THR 51  51  51  THR THR C . n 
B 1 52  PHE 52  52  52  PHE PHE C . n 
B 1 53  PHE 53  53  53  PHE PHE C . n 
B 1 54  SER 54  54  54  SER SER C . n 
B 1 55  GLU 55  55  55  GLU GLU C . n 
B 1 56  THR 56  56  56  THR THR C . n 
B 1 57  GLY 57  57  57  GLY GLY C . n 
B 1 58  ALA 58  58  58  ALA ALA C . n 
B 1 59  GLY 59  59  59  GLY GLY C . n 
B 1 60  LYS 60  60  60  LYS LYS C . n 
B 1 61  HIS 61  61  61  HIS HIS C . n 
B 1 62  VAL 62  62  62  VAL VAL C . n 
B 1 63  PRO 63  63  63  PRO PRO C . n 
B 1 64  ARG 64  64  64  ARG ARG C . n 
B 1 65  ALA 65  65  65  ALA ALA C . n 
B 1 66  VAL 66  66  66  VAL VAL C . n 
B 1 67  PHE 67  67  67  PHE PHE C . n 
B 1 68  VAL 68  68  68  VAL VAL C . n 
B 1 69  ASP 69  69  69  ASP ASP C . n 
B 1 70  LEU 70  70  70  LEU LEU C . n 
B 1 71  GLU 71  71  71  GLU GLU C . n 
B 1 72  PRO 72  72  72  PRO PRO C . n 
B 1 73  THR 73  73  73  THR THR C . n 
B 1 74  VAL 74  74  74  VAL VAL C . n 
B 1 75  ILE 75  75  75  ILE ILE C . n 
B 1 76  ASP 76  76  76  ASP ASP C . n 
B 1 77  GLU 77  77  77  GLU GLU C . n 
B 1 78  VAL 78  78  78  VAL VAL C . n 
B 1 79  ARG 79  79  79  ARG ARG C . n 
B 1 80  THR 80  80  80  THR THR C . n 
B 1 81  GLY 81  81  81  GLY GLY C . n 
B 1 82  THR 82  82  82  THR THR C . n 
B 1 83  TYR 83  83  83  TYR TYR C . n 
B 1 84  ARG 84  84  84  ARG ARG C . n 
B 1 85  GLN 85  85  85  GLN GLN C . n 
B 1 86  LEU 86  86  86  LEU LEU C . n 
B 1 87  PHE 87  87  87  PHE PHE C . n 
B 1 88  HIS 88  88  88  HIS HIS C . n 
B 1 89  PRO 89  89  89  PRO PRO C . n 
B 1 90  GLU 90  90  90  GLU GLU C . n 
B 1 91  GLN 91  91  91  GLN GLN C . n 
B 1 92  LEU 92  92  92  LEU LEU C . n 
B 1 93  ILE 93  93  93  ILE ILE C . n 
B 1 94  THR 94  94  94  THR THR C . n 
B 1 95  GLY 95  95  95  GLY GLY C . n 
B 1 96  LYS 96  96  96  LYS LYS C . n 
B 1 97  GLU 97  97  97  GLU GLU C . n 
B 1 98  ASP 98  98  98  ASP ASP C . n 
B 1 99  ALA 99  99  99  ALA ALA C . n 
B 1 100 ALA 100 100 100 ALA ALA C . n 
B 1 101 ASN 101 101 101 ASN ASN C . n 
B 1 102 ASN 102 102 102 ASN ASN C . n 
B 1 103 TYR 103 103 103 TYR TYR C . n 
B 1 104 ALA 104 104 104 ALA ALA C . n 
B 1 105 ARG 105 105 105 ARG ARG C . n 
B 1 106 GLY 106 106 106 GLY GLY C . n 
B 1 107 HIS 107 107 107 HIS HIS C . n 
B 1 108 TYR 108 108 108 TYR TYR C . n 
B 1 109 THR 109 109 109 THR THR C . n 
B 1 110 ILE 110 110 110 ILE ILE C . n 
B 1 111 GLY 111 111 111 GLY GLY C . n 
B 1 112 LYS 112 112 112 LYS LYS C . n 
B 1 113 GLU 113 113 113 GLU GLU C . n 
B 1 114 ILE 114 114 114 ILE ILE C . n 
B 1 115 ILE 115 115 115 ILE ILE C . n 
B 1 116 ASP 116 116 116 ASP ASP C . n 
B 1 117 LEU 117 117 117 LEU LEU C . n 
B 1 118 VAL 118 118 118 VAL VAL C . n 
B 1 119 LEU 119 119 119 LEU LEU C . n 
B 1 120 ASP 120 120 120 ASP ASP C . n 
B 1 121 ARG 121 121 121 ARG ARG C . n 
B 1 122 ILE 122 122 122 ILE ILE C . n 
B 1 123 ARG 123 123 123 ARG ARG C . n 
B 1 124 LYS 124 124 124 LYS LYS C . n 
B 1 125 LEU 125 125 125 LEU LEU C . n 
B 1 126 ALA 126 126 126 ALA ALA C . n 
B 1 127 ASP 127 127 127 ASP ASP C . n 
B 1 128 GLN 128 128 128 GLN GLN C . n 
B 1 129 CYS 129 129 129 CYS CYS C . n 
B 1 130 THR 130 130 130 THR THR C . n 
B 1 131 GLY 131 131 131 GLY GLY C . n 
B 1 132 LEU 132 132 132 LEU LEU C . n 
B 1 133 GLN 133 133 133 GLN GLN C . n 
B 1 134 GLY 134 134 134 GLY GLY C . n 
B 1 135 PHE 135 135 135 PHE PHE C . n 
B 1 136 LEU 136 136 136 LEU LEU C . n 
B 1 137 VAL 137 137 137 VAL VAL C . n 
B 1 138 PHE 138 138 138 PHE PHE C . n 
B 1 139 HIS 139 139 139 HIS HIS C . n 
B 1 140 SER 140 140 140 SER SER C . n 
B 1 141 PHE 141 141 141 PHE PHE C . n 
B 1 142 GLY 142 142 142 GLY GLY C . n 
B 1 143 GLY 143 143 143 GLY GLY C . n 
B 1 144 GLY 144 144 144 GLY GLY C . n 
B 1 145 THR 145 145 145 THR THR C . n 
B 1 146 GLY 146 146 146 GLY GLY C . n 
B 1 147 SER 147 147 147 SER SER C . n 
B 1 148 GLY 148 148 148 GLY GLY C . n 
B 1 149 PHE 149 149 149 PHE PHE C . n 
B 1 150 THR 150 150 150 THR THR C . n 
B 1 151 SER 151 151 151 SER SER C . n 
B 1 152 LEU 152 152 152 LEU LEU C . n 
B 1 153 LEU 153 153 153 LEU LEU C . n 
B 1 154 MET 154 154 154 MET MET C . n 
B 1 155 GLU 155 155 155 GLU GLU C . n 
B 1 156 ARG 156 156 156 ARG ARG C . n 
B 1 157 LEU 157 157 157 LEU LEU C . n 
B 1 158 SER 158 158 158 SER SER C . n 
B 1 159 VAL 159 159 159 VAL VAL C . n 
B 1 160 ASP 160 160 160 ASP ASP C . n 
B 1 161 TYR 161 161 161 TYR TYR C . n 
B 1 162 GLY 162 162 162 GLY GLY C . n 
B 1 163 LYS 163 163 163 LYS LYS C . n 
B 1 164 LYS 164 164 164 LYS LYS C . n 
B 1 165 SER 165 165 165 SER SER C . n 
B 1 166 LYS 166 166 166 LYS LYS C . n 
B 1 167 LEU 167 167 167 LEU LEU C . n 
B 1 168 GLU 168 168 168 GLU GLU C . n 
B 1 169 PHE 169 169 169 PHE PHE C . n 
B 1 170 SER 170 170 170 SER SER C . n 
B 1 171 ILE 171 171 171 ILE ILE C . n 
B 1 172 TYR 172 172 172 TYR TYR C . n 
B 1 173 PRO 173 173 173 PRO PRO C . n 
B 1 174 ALA 174 174 174 ALA ALA C . n 
B 1 175 PRO 175 175 175 PRO PRO C . n 
B 1 176 GLN 176 176 176 GLN GLN C . n 
B 1 177 VAL 177 177 177 VAL VAL C . n 
B 1 178 SER 178 178 178 SER SER C . n 
B 1 179 THR 179 179 179 THR THR C . n 
B 1 180 ALA 180 180 180 ALA ALA C . n 
B 1 181 VAL 181 181 181 VAL VAL C . n 
B 1 182 VAL 182 182 182 VAL VAL C . n 
B 1 183 GLU 183 183 183 GLU GLU C . n 
B 1 184 PRO 184 184 184 PRO PRO C . n 
B 1 185 TYR 185 185 185 TYR TYR C . n 
B 1 186 ASN 186 186 186 ASN ASN C . n 
B 1 187 SER 187 187 187 SER SER C . n 
B 1 188 ILE 188 188 188 ILE ILE C . n 
B 1 189 LEU 189 189 189 LEU LEU C . n 
B 1 190 THR 190 190 190 THR THR C . n 
B 1 191 THR 191 191 191 THR THR C . n 
B 1 192 HIS 192 192 192 HIS HIS C . n 
B 1 193 THR 193 193 193 THR THR C . n 
B 1 194 THR 194 194 194 THR THR C . n 
B 1 195 LEU 195 195 195 LEU LEU C . n 
B 1 196 GLU 196 196 196 GLU GLU C . n 
B 1 197 HIS 197 197 197 HIS HIS C . n 
B 1 198 SER 198 198 198 SER SER C . n 
B 1 199 ASP 199 199 199 ASP ASP C . n 
B 1 200 CYS 200 200 200 CYS CYS C . n 
B 1 201 ALA 201 201 201 ALA ALA C . n 
B 1 202 PHE 202 202 202 PHE PHE C . n 
B 1 203 MET 203 203 203 MET MET C . n 
B 1 204 VAL 204 204 204 VAL VAL C . n 
B 1 205 ASP 205 205 205 ASP ASP C . n 
B 1 206 ASN 206 206 206 ASN ASN C . n 
B 1 207 GLU 207 207 207 GLU GLU C . n 
B 1 208 ALA 208 208 208 ALA ALA C . n 
B 1 209 ILE 209 209 209 ILE ILE C . n 
B 1 210 TYR 210 210 210 TYR TYR C . n 
B 1 211 ASP 211 211 211 ASP ASP C . n 
B 1 212 ILE 212 212 212 ILE ILE C . n 
B 1 213 CYS 213 213 213 CYS CYS C . n 
B 1 214 ARG 214 214 214 ARG ARG C . n 
B 1 215 ARG 215 215 215 ARG ARG C . n 
B 1 216 ASN 216 216 216 ASN ASN C . n 
B 1 217 LEU 217 217 217 LEU LEU C . n 
B 1 218 ASP 218 218 218 ASP ASP C . n 
B 1 219 ILE 219 219 219 ILE ILE C . n 
B 1 220 GLU 220 220 220 GLU GLU C . n 
B 1 221 ARG 221 221 221 ARG ARG C . n 
B 1 222 PRO 222 222 222 PRO PRO C . n 
B 1 223 THR 223 223 223 THR THR C . n 
B 1 224 TYR 224 224 224 TYR TYR C . n 
B 1 225 THR 225 225 225 THR THR C . n 
B 1 226 ASN 226 226 226 ASN ASN C . n 
B 1 227 LEU 227 227 227 LEU LEU C . n 
B 1 228 ASN 228 228 228 ASN ASN C . n 
B 1 229 ARG 229 229 229 ARG ARG C . n 
B 1 230 LEU 230 230 230 LEU LEU C . n 
B 1 231 ILE 231 231 231 ILE ILE C . n 
B 1 232 SER 232 232 232 SER SER C . n 
B 1 233 GLN 233 233 233 GLN GLN C . n 
B 1 234 ILE 234 234 234 ILE ILE C . n 
B 1 235 VAL 235 235 235 VAL VAL C . n 
B 1 236 SER 236 236 236 SER SER C . n 
B 1 237 SER 237 237 237 SER SER C . n 
B 1 238 ILE 238 238 238 ILE ILE C . n 
B 1 239 THR 239 239 239 THR THR C . n 
B 1 240 ALA 240 240 240 ALA ALA C . n 
B 1 241 SER 241 241 241 SER SER C . n 
B 1 242 LEU 242 242 242 LEU LEU C . n 
B 1 243 ARG 243 243 243 ARG ARG C . n 
B 1 244 PHE 244 244 244 PHE PHE C . n 
B 1 245 ASP 245 245 245 ASP ASP C . n 
B 1 246 GLY 246 246 246 GLY GLY C . n 
B 1 247 ALA 247 247 247 ALA ALA C . n 
B 1 248 LEU 248 248 248 LEU LEU C . n 
B 1 249 ASN 249 249 249 ASN ASN C . n 
B 1 250 VAL 250 250 250 VAL VAL C . n 
B 1 251 ASP 251 251 251 ASP ASP C . n 
B 1 252 LEU 252 252 252 LEU LEU C . n 
B 1 253 THR 253 253 253 THR THR C . n 
B 1 254 GLU 254 254 254 GLU GLU C . n 
B 1 255 PHE 255 255 255 PHE PHE C . n 
B 1 256 GLN 256 256 256 GLN GLN C . n 
B 1 257 THR 257 257 257 THR THR C . n 
B 1 258 ASN 258 258 258 ASN ASN C . n 
B 1 259 LEU 259 259 259 LEU LEU C . n 
B 1 260 VAL 260 260 260 VAL VAL C . n 
B 1 261 PRO 261 261 261 PRO PRO C . n 
B 1 262 TYR 262 262 262 TYR TYR C . n 
B 1 263 PRO 263 263 263 PRO PRO C . n 
B 1 264 ARG 264 264 264 ARG ARG C . n 
B 1 265 ILE 265 265 265 ILE ILE C . n 
B 1 266 HIS 266 266 266 HIS HIS C . n 
B 1 267 PHE 267 267 267 PHE PHE C . n 
B 1 268 PRO 268 268 268 PRO PRO C . n 
B 1 269 LEU 269 269 269 LEU LEU C . n 
B 1 270 ALA 270 270 270 ALA ALA C . n 
B 1 271 THR 271 271 271 THR THR C . n 
B 1 272 TYR 272 272 272 TYR TYR C . n 
B 1 273 ALA 273 273 273 ALA ALA C . n 
B 1 274 PRO 274 274 274 PRO PRO C . n 
B 1 275 VAL 275 275 275 VAL VAL C . n 
B 1 276 ILE 276 276 276 ILE ILE C . n 
B 1 277 SER 277 277 277 SER SER C . n 
B 1 278 ALA 278 278 278 ALA ALA C . n 
B 1 279 GLU 279 279 279 GLU GLU C . n 
B 1 280 LYS 280 280 280 LYS LYS C . n 
B 1 281 ALA 281 281 281 ALA ALA C . n 
B 1 282 TYR 282 282 282 TYR TYR C . n 
B 1 283 HIS 283 283 283 HIS HIS C . n 
B 1 284 GLU 284 284 284 GLU GLU C . n 
B 1 285 GLN 285 285 285 GLN GLN C . n 
B 1 286 LEU 286 286 286 LEU LEU C . n 
B 1 287 SER 287 287 287 SER SER C . n 
B 1 288 VAL 288 288 288 VAL VAL C . n 
B 1 289 ALA 289 289 289 ALA ALA C . n 
B 1 290 GLU 290 290 290 GLU GLU C . n 
B 1 291 ILE 291 291 291 ILE ILE C . n 
B 1 292 THR 292 292 292 THR THR C . n 
B 1 293 ASN 293 293 293 ASN ASN C . n 
B 1 294 ALA 294 294 294 ALA ALA C . n 
B 1 295 CYS 295 295 295 CYS CYS C . n 
B 1 296 PHE 296 296 296 PHE PHE C . n 
B 1 297 GLU 297 297 297 GLU GLU C . n 
B 1 298 PRO 298 298 298 PRO PRO C . n 
B 1 299 ALA 299 299 299 ALA ALA C . n 
B 1 300 ASN 300 300 300 ASN ASN C . n 
B 1 301 GLN 301 301 301 GLN GLN C . n 
B 1 302 MET 302 302 302 MET MET C . n 
B 1 303 VAL 303 303 303 VAL VAL C . n 
B 1 304 LYS 304 304 304 LYS LYS C . n 
B 1 305 CYS 305 305 305 CYS CYS C . n 
B 1 306 ASP 306 306 306 ASP ASP C . n 
B 1 307 PRO 307 307 307 PRO PRO C . n 
B 1 308 ARG 308 308 308 ARG ARG C . n 
B 1 309 HIS 309 309 309 HIS HIS C . n 
B 1 310 GLY 310 310 310 GLY GLY C . n 
B 1 311 LYS 311 311 311 LYS LYS C . n 
B 1 312 TYR 312 312 312 TYR TYR C . n 
B 1 313 MET 313 313 313 MET MET C . n 
B 1 314 ALA 314 314 314 ALA ALA C . n 
B 1 315 CYS 315 315 315 CYS CYS C . n 
B 1 316 CYS 316 316 316 CYS CYS C . n 
B 1 317 LEU 317 317 317 LEU LEU C . n 
B 1 318 LEU 318 318 318 LEU LEU C . n 
B 1 319 TYR 319 319 319 TYR TYR C . n 
B 1 320 ARG 320 320 320 ARG ARG C . n 
B 1 321 GLY 321 321 321 GLY GLY C . n 
B 1 322 ASP 322 322 322 ASP ASP C . n 
B 1 323 VAL 323 323 323 VAL VAL C . n 
B 1 324 VAL 324 324 324 VAL VAL C . n 
B 1 325 PRO 325 325 325 PRO PRO C . n 
B 1 326 LYS 326 326 326 LYS LYS C . n 
B 1 327 ASP 327 327 327 ASP ASP C . n 
B 1 328 VAL 328 328 328 VAL VAL C . n 
B 1 329 ASN 329 329 329 ASN ASN C . n 
B 1 330 ALA 330 330 330 ALA ALA C . n 
B 1 331 ALA 331 331 331 ALA ALA C . n 
B 1 332 ILE 332 332 332 ILE ILE C . n 
B 1 333 ALA 333 333 333 ALA ALA C . n 
B 1 334 THR 334 334 334 THR THR C . n 
B 1 335 ILE 335 335 335 ILE ILE C . n 
B 1 336 LYS 336 336 336 LYS LYS C . n 
B 1 337 THR 337 337 337 THR THR C . n 
B 1 338 LYS 338 338 338 LYS LYS C . n 
B 1 339 ARG 339 339 339 ARG ARG C . n 
B 1 340 SER 340 340 340 SER SER C . n 
B 1 341 ILE 341 341 341 ILE ILE C . n 
B 1 342 GLN 342 342 342 GLN GLN C . n 
B 1 343 PHE 343 343 343 PHE PHE C . n 
B 1 344 VAL 344 344 344 VAL VAL C . n 
B 1 345 ASP 345 345 345 ASP ASP C . n 
B 1 346 TRP 346 346 346 TRP TRP C . n 
B 1 347 CYS 347 347 347 CYS CYS C . n 
B 1 348 PRO 348 348 348 PRO PRO C . n 
B 1 349 THR 349 349 349 THR THR C . n 
B 1 350 GLY 350 350 350 GLY GLY C . n 
B 1 351 PHE 351 351 351 PHE PHE C . n 
B 1 352 LYS 352 352 352 LYS LYS C . n 
B 1 353 VAL 353 353 353 VAL VAL C . n 
B 1 354 GLY 354 354 354 GLY GLY C . n 
B 1 355 ILE 355 355 355 ILE ILE C . n 
B 1 356 ASN 356 356 356 ASN ASN C . n 
B 1 357 TYR 357 357 357 TYR TYR C . n 
B 1 358 GLN 358 358 358 GLN GLN C . n 
B 1 359 PRO 359 359 359 PRO PRO C . n 
B 1 360 PRO 360 360 360 PRO PRO C . n 
B 1 361 THR 361 361 361 THR THR C . n 
B 1 362 VAL 362 362 362 VAL VAL C . n 
B 1 363 VAL 363 363 363 VAL VAL C . n 
B 1 364 PRO 364 364 364 PRO PRO C . n 
B 1 365 GLY 365 365 365 GLY GLY C . n 
B 1 366 GLY 366 366 366 GLY GLY C . n 
B 1 367 ASP 367 367 367 ASP ASP C . n 
B 1 368 LEU 368 368 368 LEU LEU C . n 
B 1 369 ALA 369 369 369 ALA ALA C . n 
B 1 370 LYS 370 370 370 LYS LYS C . n 
B 1 371 VAL 371 371 371 VAL VAL C . n 
B 1 372 GLN 372 372 372 GLN GLN C . n 
B 1 373 ARG 373 373 373 ARG ARG C . n 
B 1 374 ALA 374 374 374 ALA ALA C . n 
B 1 375 VAL 375 375 375 VAL VAL C . n 
B 1 376 CYS 376 376 376 CYS CYS C . n 
B 1 377 MET 377 377 377 MET MET C . n 
B 1 378 LEU 378 378 378 LEU LEU C . n 
B 1 379 SER 379 379 379 SER SER C . n 
B 1 380 ASN 380 380 380 ASN ASN C . n 
B 1 381 THR 381 381 381 THR THR C . n 
B 1 382 THR 382 382 382 THR THR C . n 
B 1 383 ALA 383 383 383 ALA ALA C . n 
B 1 384 ILE 384 384 384 ILE ILE C . n 
B 1 385 ALA 385 385 385 ALA ALA C . n 
B 1 386 GLU 386 386 386 GLU GLU C . n 
B 1 387 ALA 387 387 387 ALA ALA C . n 
B 1 388 TRP 388 388 388 TRP TRP C . n 
B 1 389 ALA 389 389 389 ALA ALA C . n 
B 1 390 ARG 390 390 390 ARG ARG C . n 
B 1 391 LEU 391 391 391 LEU LEU C . n 
B 1 392 ASP 392 392 392 ASP ASP C . n 
B 1 393 HIS 393 393 393 HIS HIS C . n 
B 1 394 LYS 394 394 394 LYS LYS C . n 
B 1 395 PHE 395 395 395 PHE PHE C . n 
B 1 396 ASP 396 396 396 ASP ASP C . n 
B 1 397 LEU 397 397 397 LEU LEU C . n 
B 1 398 MET 398 398 398 MET MET C . n 
B 1 399 TYR 399 399 399 TYR TYR C . n 
B 1 400 ALA 400 400 400 ALA ALA C . n 
B 1 401 LYS 401 401 401 LYS LYS C . n 
B 1 402 ARG 402 402 402 ARG ARG C . n 
B 1 403 ALA 403 403 403 ALA ALA C . n 
B 1 404 PHE 404 404 404 PHE PHE C . n 
B 1 405 VAL 405 405 405 VAL VAL C . n 
B 1 406 HIS 406 406 406 HIS HIS C . n 
B 1 407 TRP 407 407 407 TRP TRP C . n 
B 1 408 TYR 408 408 408 TYR TYR C . n 
B 1 409 VAL 409 409 409 VAL VAL C . n 
B 1 410 GLY 410 410 410 GLY GLY C . n 
B 1 411 GLU 411 411 411 GLU GLU C . n 
B 1 412 GLY 412 412 412 GLY GLY C . n 
B 1 413 MET 413 413 413 MET MET C . n 
B 1 414 GLU 414 414 414 GLU GLU C . n 
B 1 415 GLU 415 415 415 GLU GLU C . n 
B 1 416 GLY 416 416 416 GLY GLY C . n 
B 1 417 GLU 417 417 417 GLU GLU C . n 
B 1 418 PHE 418 418 418 PHE PHE C . n 
B 1 419 SER 419 419 419 SER SER C . n 
B 1 420 GLU 420 420 420 GLU GLU C . n 
B 1 421 ALA 421 421 421 ALA ALA C . n 
B 1 422 ARG 422 422 422 ARG ARG C . n 
B 1 423 GLU 423 423 423 GLU GLU C . n 
B 1 424 ASP 424 424 424 ASP ASP C . n 
B 1 425 MET 425 425 425 MET MET C . n 
B 1 426 ALA 426 426 426 ALA ALA C . n 
B 1 427 ALA 427 427 427 ALA ALA C . n 
B 1 428 LEU 428 428 428 LEU LEU C . n 
B 1 429 GLU 429 429 429 GLU GLU C . n 
B 1 430 LYS 430 430 430 LYS LYS C . n 
B 1 431 ASP 431 431 431 ASP ASP C . n 
B 1 432 TYR 432 432 432 TYR TYR C . n 
B 1 433 GLU 433 433 433 GLU GLU C . n 
B 1 434 GLU 434 434 434 GLU GLU C . n 
B 1 435 VAL 435 435 435 VAL VAL C . n 
B 1 436 GLY 436 436 436 GLY GLY C . n 
B 1 437 VAL 437 437 437 VAL VAL C . n 
B 1 438 ASP 438 438 438 ASP ASP C . n 
B 1 439 SER 439 439 439 SER SER C . n 
B 1 440 VAL 440 440 440 VAL VAL C . n 
B 1 441 GLU 441 441 ?   ?   ?   C . n 
B 1 442 GLY 442 442 ?   ?   ?   C . n 
B 1 443 GLU 443 443 ?   ?   ?   C . n 
B 1 444 GLY 444 444 ?   ?   ?   C . n 
B 1 445 GLU 445 445 ?   ?   ?   C . n 
B 1 446 GLU 446 446 ?   ?   ?   C . n 
B 1 447 GLU 447 447 ?   ?   ?   C . n 
B 1 448 GLY 448 448 ?   ?   ?   C . n 
B 1 449 GLU 449 449 ?   ?   ?   C . n 
B 1 450 GLU 450 450 ?   ?   ?   C . n 
C 2 1   MET 1   1   1   MET MET D . n 
C 2 2   ARG 2   2   2   ARG ARG D . n 
C 2 3   GLU 3   3   3   GLU GLU D . n 
C 2 4   ILE 4   4   4   ILE ILE D . n 
C 2 5   VAL 5   5   5   VAL VAL D . n 
C 2 6   HIS 6   6   6   HIS HIS D . n 
C 2 7   ILE 7   7   7   ILE ILE D . n 
C 2 8   GLN 8   8   8   GLN GLN D . n 
C 2 9   ALA 9   9   9   ALA ALA D . n 
C 2 10  GLY 10  10  10  GLY GLY D . n 
C 2 11  GLN 11  11  11  GLN GLN D . n 
C 2 12  CYS 12  12  12  CYS CYS D . n 
C 2 13  GLY 13  13  13  GLY GLY D . n 
C 2 14  ASN 14  14  14  ASN ASN D . n 
C 2 15  GLN 15  15  15  GLN GLN D . n 
C 2 16  ILE 16  16  16  ILE ILE D . n 
C 2 17  GLY 17  17  17  GLY GLY D . n 
C 2 18  ALA 18  18  18  ALA ALA D . n 
C 2 19  LYS 19  19  19  LYS LYS D . n 
C 2 20  PHE 20  20  20  PHE PHE D . n 
C 2 21  TRP 21  21  21  TRP TRP D . n 
C 2 22  GLU 22  22  22  GLU GLU D . n 
C 2 23  VAL 23  23  23  VAL VAL D . n 
C 2 24  ILE 24  24  24  ILE ILE D . n 
C 2 25  SER 25  25  25  SER SER D . n 
C 2 26  ASP 26  26  26  ASP ASP D . n 
C 2 27  GLU 27  27  27  GLU GLU D . n 
C 2 28  HIS 28  28  28  HIS HIS D . n 
C 2 29  GLY 29  29  29  GLY GLY D . n 
C 2 30  ILE 30  30  30  ILE ILE D . n 
C 2 31  ASP 31  31  31  ASP ASP D . n 
C 2 32  PRO 32  32  32  PRO PRO D . n 
C 2 33  THR 33  33  33  THR THR D . n 
C 2 34  GLY 34  34  34  GLY GLY D . n 
C 2 35  SER 35  35  35  SER SER D . n 
C 2 36  TYR 36  36  36  TYR TYR D . n 
C 2 37  HIS 37  37  37  HIS HIS D . n 
C 2 38  GLY 38  38  38  GLY GLY D . n 
C 2 39  ASP 39  39  39  ASP ASP D . n 
C 2 40  SER 40  40  40  SER SER D . n 
C 2 41  ASP 41  41  41  ASP ASP D . n 
C 2 42  LEU 42  42  42  LEU LEU D . n 
C 2 43  GLN 43  45  45  GLN GLN D . n 
C 2 44  LEU 44  46  46  LEU LEU D . n 
C 2 45  GLU 45  47  47  GLU GLU D . n 
C 2 46  ARG 46  48  48  ARG ARG D . n 
C 2 47  ILE 47  49  49  ILE ILE D . n 
C 2 48  ASN 48  50  50  ASN ASN D . n 
C 2 49  VAL 49  51  51  VAL VAL D . n 
C 2 50  TYR 50  52  52  TYR TYR D . n 
C 2 51  TYR 51  53  53  TYR TYR D . n 
C 2 52  ASN 52  54  54  ASN ASN D . n 
C 2 53  GLU 53  55  55  GLU GLU D . n 
C 2 54  ALA 54  56  56  ALA ALA D . n 
C 2 55  THR 55  57  57  THR THR D . n 
C 2 56  GLY 56  58  58  GLY GLY D . n 
C 2 57  ASN 57  59  59  ASN ASN D . n 
C 2 58  LYS 58  60  60  LYS LYS D . n 
C 2 59  TYR 59  61  61  TYR TYR D . n 
C 2 60  VAL 60  62  62  VAL VAL D . n 
C 2 61  PRO 61  63  63  PRO PRO D . n 
C 2 62  ARG 62  64  64  ARG ARG D . n 
C 2 63  ALA 63  65  65  ALA ALA D . n 
C 2 64  ILE 64  66  66  ILE ILE D . n 
C 2 65  LEU 65  67  67  LEU LEU D . n 
C 2 66  VAL 66  68  68  VAL VAL D . n 
C 2 67  ASP 67  69  69  ASP ASP D . n 
C 2 68  LEU 68  70  70  LEU LEU D . n 
C 2 69  GLU 69  71  71  GLU GLU D . n 
C 2 70  PRO 70  72  72  PRO PRO D . n 
C 2 71  GLY 71  73  73  GLY GLY D . n 
C 2 72  THR 72  74  74  THR THR D . n 
C 2 73  MET 73  75  75  MET MET D . n 
C 2 74  ASP 74  76  76  ASP ASP D . n 
C 2 75  SER 75  77  77  SER SER D . n 
C 2 76  VAL 76  78  78  VAL VAL D . n 
C 2 77  ARG 77  79  79  ARG ARG D . n 
C 2 78  SER 78  80  80  SER SER D . n 
C 2 79  GLY 79  81  81  GLY GLY D . n 
C 2 80  PRO 80  82  82  PRO PRO D . n 
C 2 81  PHE 81  83  83  PHE PHE D . n 
C 2 82  GLY 82  84  84  GLY GLY D . n 
C 2 83  GLN 83  85  85  GLN GLN D . n 
C 2 84  ILE 84  86  86  ILE ILE D . n 
C 2 85  PHE 85  87  87  PHE PHE D . n 
C 2 86  ARG 86  88  88  ARG ARG D . n 
C 2 87  PRO 87  89  89  PRO PRO D . n 
C 2 88  ASP 88  90  90  ASP ASP D . n 
C 2 89  ASN 89  91  91  ASN ASN D . n 
C 2 90  PHE 90  92  92  PHE PHE D . n 
C 2 91  VAL 91  93  93  VAL VAL D . n 
C 2 92  PHE 92  94  94  PHE PHE D . n 
C 2 93  GLY 93  95  95  GLY GLY D . n 
C 2 94  GLN 94  96  96  GLN GLN D . n 
C 2 95  SER 95  97  97  SER SER D . n 
C 2 96  GLY 96  98  98  GLY GLY D . n 
C 2 97  ALA 97  99  99  ALA ALA D . n 
C 2 98  GLY 98  100 100 GLY GLY D . n 
C 2 99  ASN 99  101 101 ASN ASN D . n 
C 2 100 ASN 100 102 102 ASN ASN D . n 
C 2 101 TRP 101 103 103 TRP TRP D . n 
C 2 102 ALA 102 104 104 ALA ALA D . n 
C 2 103 LYS 103 105 105 LYS LYS D . n 
C 2 104 GLY 104 106 106 GLY GLY D . n 
C 2 105 HIS 105 107 107 HIS HIS D . n 
C 2 106 TYR 106 108 108 TYR TYR D . n 
C 2 107 THR 107 109 109 THR THR D . n 
C 2 108 GLU 108 110 110 GLU GLU D . n 
C 2 109 GLY 109 111 111 GLY GLY D . n 
C 2 110 ALA 110 112 112 ALA ALA D . n 
C 2 111 GLU 111 113 113 GLU GLU D . n 
C 2 112 LEU 112 114 114 LEU LEU D . n 
C 2 113 VAL 113 115 115 VAL VAL D . n 
C 2 114 ASP 114 116 116 ASP ASP D . n 
C 2 115 SER 115 117 117 SER SER D . n 
C 2 116 VAL 116 118 118 VAL VAL D . n 
C 2 117 LEU 117 119 119 LEU LEU D . n 
C 2 118 ASP 118 120 120 ASP ASP D . n 
C 2 119 VAL 119 121 121 VAL VAL D . n 
C 2 120 VAL 120 122 122 VAL VAL D . n 
C 2 121 ARG 121 123 123 ARG ARG D . n 
C 2 122 LYS 122 124 124 LYS LYS D . n 
C 2 123 GLU 123 125 125 GLU GLU D . n 
C 2 124 SER 124 126 126 SER SER D . n 
C 2 125 GLU 125 127 127 GLU GLU D . n 
C 2 126 SER 126 128 128 SER SER D . n 
C 2 127 CYS 127 129 129 CYS CYS D . n 
C 2 128 ASP 128 130 130 ASP ASP D . n 
C 2 129 CYS 129 131 131 CYS CYS D . n 
C 2 130 LEU 130 132 132 LEU LEU D . n 
C 2 131 GLN 131 133 133 GLN GLN D . n 
C 2 132 GLY 132 134 134 GLY GLY D . n 
C 2 133 PHE 133 135 135 PHE PHE D . n 
C 2 134 GLN 134 136 136 GLN GLN D . n 
C 2 135 LEU 135 137 137 LEU LEU D . n 
C 2 136 THR 136 138 138 THR THR D . n 
C 2 137 HIS 137 139 139 HIS HIS D . n 
C 2 138 SER 138 140 140 SER SER D . n 
C 2 139 LEU 139 141 141 LEU LEU D . n 
C 2 140 GLY 140 142 142 GLY GLY D . n 
C 2 141 GLY 141 143 143 GLY GLY D . n 
C 2 142 GLY 142 144 144 GLY GLY D . n 
C 2 143 THR 143 145 145 THR THR D . n 
C 2 144 GLY 144 146 146 GLY GLY D . n 
C 2 145 SER 145 147 147 SER SER D . n 
C 2 146 GLY 146 148 148 GLY GLY D . n 
C 2 147 MET 147 149 149 MET MET D . n 
C 2 148 GLY 148 150 150 GLY GLY D . n 
C 2 149 THR 149 151 151 THR THR D . n 
C 2 150 LEU 150 152 152 LEU LEU D . n 
C 2 151 LEU 151 153 153 LEU LEU D . n 
C 2 152 ILE 152 154 154 ILE ILE D . n 
C 2 153 SER 153 155 155 SER SER D . n 
C 2 154 LYS 154 156 156 LYS LYS D . n 
C 2 155 ILE 155 157 157 ILE ILE D . n 
C 2 156 ARG 156 158 158 ARG ARG D . n 
C 2 157 GLU 157 159 159 GLU GLU D . n 
C 2 158 GLU 158 160 160 GLU GLU D . n 
C 2 159 TYR 159 161 161 TYR TYR D . n 
C 2 160 PRO 160 162 162 PRO PRO D . n 
C 2 161 ASP 161 163 163 ASP ASP D . n 
C 2 162 ARG 162 164 164 ARG ARG D . n 
C 2 163 ILE 163 165 165 ILE ILE D . n 
C 2 164 MET 164 166 166 MET MET D . n 
C 2 165 ASN 165 167 167 ASN ASN D . n 
C 2 166 THR 166 168 168 THR THR D . n 
C 2 167 PHE 167 169 169 PHE PHE D . n 
C 2 168 SER 168 170 170 SER SER D . n 
C 2 169 VAL 169 171 171 VAL VAL D . n 
C 2 170 MET 170 172 172 MET MET D . n 
C 2 171 PRO 171 173 173 PRO PRO D . n 
C 2 172 SER 172 174 174 SER SER D . n 
C 2 173 PRO 173 175 175 PRO PRO D . n 
C 2 174 LYS 174 176 176 LYS LYS D . n 
C 2 175 VAL 175 177 177 VAL VAL D . n 
C 2 176 SER 176 178 178 SER SER D . n 
C 2 177 ASP 177 179 179 ASP ASP D . n 
C 2 178 THR 178 180 180 THR THR D . n 
C 2 179 VAL 179 181 181 VAL VAL D . n 
C 2 180 VAL 180 182 182 VAL VAL D . n 
C 2 181 GLU 181 183 183 GLU GLU D . n 
C 2 182 PRO 182 184 184 PRO PRO D . n 
C 2 183 TYR 183 185 185 TYR TYR D . n 
C 2 184 ASN 184 186 186 ASN ASN D . n 
C 2 185 ALA 185 187 187 ALA ALA D . n 
C 2 186 THR 186 188 188 THR THR D . n 
C 2 187 LEU 187 189 189 LEU LEU D . n 
C 2 188 SER 188 190 190 SER SER D . n 
C 2 189 VAL 189 191 191 VAL VAL D . n 
C 2 190 HIS 190 192 192 HIS HIS D . n 
C 2 191 GLN 191 193 193 GLN GLN D . n 
C 2 192 LEU 192 194 194 LEU LEU D . n 
C 2 193 VAL 193 195 195 VAL VAL D . n 
C 2 194 GLU 194 196 196 GLU GLU D . n 
C 2 195 ASN 195 197 197 ASN ASN D . n 
C 2 196 THR 196 198 198 THR THR D . n 
C 2 197 ASP 197 199 199 ASP ASP D . n 
C 2 198 GLU 198 200 200 GLU GLU D . n 
C 2 199 THR 199 201 201 THR THR D . n 
C 2 200 TYR 200 202 202 TYR TYR D . n 
C 2 201 CYS 201 203 203 CYS CYS D . n 
C 2 202 ILE 202 204 204 ILE ILE D . n 
C 2 203 ASP 203 205 205 ASP ASP D . n 
C 2 204 ASN 204 206 206 ASN ASN D . n 
C 2 205 GLU 205 207 207 GLU GLU D . n 
C 2 206 ALA 206 208 208 ALA ALA D . n 
C 2 207 LEU 207 209 209 LEU LEU D . n 
C 2 208 TYR 208 210 210 TYR TYR D . n 
C 2 209 ASP 209 211 211 ASP ASP D . n 
C 2 210 ILE 210 212 212 ILE ILE D . n 
C 2 211 CYS 211 213 213 CYS CYS D . n 
C 2 212 PHE 212 214 214 PHE PHE D . n 
C 2 213 ARG 213 215 215 ARG ARG D . n 
C 2 214 THR 214 216 216 THR THR D . n 
C 2 215 LEU 215 217 217 LEU LEU D . n 
C 2 216 LYS 216 218 218 LYS LYS D . n 
C 2 217 LEU 217 219 219 LEU LEU D . n 
C 2 218 THR 218 220 220 THR THR D . n 
C 2 219 THR 219 221 221 THR THR D . n 
C 2 220 PRO 220 222 222 PRO PRO D . n 
C 2 221 THR 221 223 223 THR THR D . n 
C 2 222 TYR 222 224 224 TYR TYR D . n 
C 2 223 GLY 223 225 225 GLY GLY D . n 
C 2 224 ASP 224 226 226 ASP ASP D . n 
C 2 225 LEU 225 227 227 LEU LEU D . n 
C 2 226 ASN 226 228 228 ASN ASN D . n 
C 2 227 HIS 227 229 229 HIS HIS D . n 
C 2 228 LEU 228 230 230 LEU LEU D . n 
C 2 229 VAL 229 231 231 VAL VAL D . n 
C 2 230 SER 230 232 232 SER SER D . n 
C 2 231 ALA 231 233 233 ALA ALA D . n 
C 2 232 THR 232 234 234 THR THR D . n 
C 2 233 MET 233 235 235 MET MET D . n 
C 2 234 SER 234 236 236 SER SER D . n 
C 2 235 GLY 235 237 237 GLY GLY D . n 
C 2 236 VAL 236 238 238 VAL VAL D . n 
C 2 237 THR 237 239 239 THR THR D . n 
C 2 238 THR 238 240 240 THR THR D . n 
C 2 239 CYS 239 241 241 CYS CYS D . n 
C 2 240 LEU 240 242 242 LEU LEU D . n 
C 2 241 ARG 241 243 243 ARG ARG D . n 
C 2 242 PHE 242 244 244 PHE PHE D . n 
C 2 243 PRO 243 245 245 PRO PRO D . n 
C 2 244 GLY 244 246 246 GLY GLY D . n 
C 2 245 GLN 245 247 247 GLN GLN D . n 
C 2 246 LEU 246 248 248 LEU LEU D . n 
C 2 247 ASN 247 249 249 ASN ASN D . n 
C 2 248 ALA 248 250 250 ALA ALA D . n 
C 2 249 ASP 249 251 251 ASP ASP D . n 
C 2 250 LEU 250 252 252 LEU LEU D . n 
C 2 251 ARG 251 253 253 ARG ARG D . n 
C 2 252 LYS 252 254 254 LYS LYS D . n 
C 2 253 LEU 253 255 255 LEU LEU D . n 
C 2 254 ALA 254 256 256 ALA ALA D . n 
C 2 255 VAL 255 257 257 VAL VAL D . n 
C 2 256 ASN 256 258 258 ASN ASN D . n 
C 2 257 MET 257 259 259 MET MET D . n 
C 2 258 VAL 258 260 260 VAL VAL D . n 
C 2 259 PRO 259 261 261 PRO PRO D . n 
C 2 260 PHE 260 262 262 PHE PHE D . n 
C 2 261 PRO 261 263 263 PRO PRO D . n 
C 2 262 ARG 262 264 264 ARG ARG D . n 
C 2 263 LEU 263 265 265 LEU LEU D . n 
C 2 264 HIS 264 266 266 HIS HIS D . n 
C 2 265 PHE 265 267 267 PHE PHE D . n 
C 2 266 PHE 266 268 268 PHE PHE D . n 
C 2 267 MET 267 269 269 MET MET D . n 
C 2 268 PRO 268 270 270 PRO PRO D . n 
C 2 269 GLY 269 271 271 GLY GLY D . n 
C 2 270 PHE 270 272 272 PHE PHE D . n 
C 2 271 ALA 271 273 273 ALA ALA D . n 
C 2 272 PRO 272 274 274 PRO PRO D . n 
C 2 273 LEU 273 275 275 LEU LEU D . n 
C 2 274 THR 274 276 276 THR THR D . n 
C 2 275 SER 275 277 ?   ?   ?   D . n 
C 2 276 ARG 276 278 ?   ?   ?   D . n 
C 2 277 GLY 277 279 ?   ?   ?   D . n 
C 2 278 SER 278 280 ?   ?   ?   D . n 
C 2 279 GLN 279 281 ?   ?   ?   D . n 
C 2 280 GLN 280 282 ?   ?   ?   D . n 
C 2 281 TYR 281 283 ?   ?   ?   D . n 
C 2 282 ARG 282 284 284 ARG ARG D . n 
C 2 283 ALA 283 285 285 ALA ALA D . n 
C 2 284 LEU 284 286 286 LEU LEU D . n 
C 2 285 THR 285 287 287 THR THR D . n 
C 2 286 VAL 286 288 288 VAL VAL D . n 
C 2 287 PRO 287 289 289 PRO PRO D . n 
C 2 288 GLU 288 290 290 GLU GLU D . n 
C 2 289 LEU 289 291 291 LEU LEU D . n 
C 2 290 THR 290 292 292 THR THR D . n 
C 2 291 GLN 291 293 293 GLN GLN D . n 
C 2 292 GLN 292 294 294 GLN GLN D . n 
C 2 293 MET 293 295 295 MET MET D . n 
C 2 294 PHE 294 296 296 PHE PHE D . n 
C 2 295 ASP 295 297 297 ASP ASP D . n 
C 2 296 SER 296 298 298 SER SER D . n 
C 2 297 LYS 297 299 299 LYS LYS D . n 
C 2 298 ASN 298 300 300 ASN ASN D . n 
C 2 299 MET 299 301 301 MET MET D . n 
C 2 300 MET 300 302 302 MET MET D . n 
C 2 301 ALA 301 303 303 ALA ALA D . n 
C 2 302 ALA 302 304 304 ALA ALA D . n 
C 2 303 CYS 303 305 305 CYS CYS D . n 
C 2 304 ASP 304 306 306 ASP ASP D . n 
C 2 305 PRO 305 307 307 PRO PRO D . n 
C 2 306 ARG 306 308 308 ARG ARG D . n 
C 2 307 HIS 307 309 309 HIS HIS D . n 
C 2 308 GLY 308 310 310 GLY GLY D . n 
C 2 309 ARG 309 311 311 ARG ARG D . n 
C 2 310 TYR 310 312 312 TYR TYR D . n 
C 2 311 LEU 311 313 313 LEU LEU D . n 
C 2 312 THR 312 314 314 THR THR D . n 
C 2 313 VAL 313 315 315 VAL VAL D . n 
C 2 314 ALA 314 316 316 ALA ALA D . n 
C 2 315 ALA 315 317 317 ALA ALA D . n 
C 2 316 ILE 316 318 318 ILE ILE D . n 
C 2 317 PHE 317 319 319 PHE PHE D . n 
C 2 318 ARG 318 320 320 ARG ARG D . n 
C 2 319 GLY 319 321 321 GLY GLY D . n 
C 2 320 ARG 320 322 322 ARG ARG D . n 
C 2 321 MET 321 323 323 MET MET D . n 
C 2 322 SER 322 324 324 SER SER D . n 
C 2 323 MET 323 325 325 MET MET D . n 
C 2 324 LYS 324 326 326 LYS LYS D . n 
C 2 325 GLU 325 327 327 GLU GLU D . n 
C 2 326 VAL 326 328 328 VAL VAL D . n 
C 2 327 ASP 327 329 329 ASP ASP D . n 
C 2 328 GLU 328 330 330 GLU GLU D . n 
C 2 329 GLN 329 331 331 GLN GLN D . n 
C 2 330 MET 330 332 332 MET MET D . n 
C 2 331 LEU 331 333 333 LEU LEU D . n 
C 2 332 ASN 332 334 334 ASN ASN D . n 
C 2 333 VAL 333 335 335 VAL VAL D . n 
C 2 334 GLN 334 336 336 GLN GLN D . n 
C 2 335 ASN 335 337 337 ASN ASN D . n 
C 2 336 LYS 336 338 338 LYS LYS D . n 
C 2 337 ASN 337 339 339 ASN ASN D . n 
C 2 338 SER 338 340 340 SER SER D . n 
C 2 339 SER 339 341 341 SER SER D . n 
C 2 340 TYR 340 342 342 TYR TYR D . n 
C 2 341 PHE 341 343 343 PHE PHE D . n 
C 2 342 VAL 342 344 344 VAL VAL D . n 
C 2 343 GLU 343 345 345 GLU GLU D . n 
C 2 344 TRP 344 346 346 TRP TRP D . n 
C 2 345 ILE 345 347 347 ILE ILE D . n 
C 2 346 PRO 346 348 348 PRO PRO D . n 
C 2 347 ASN 347 349 349 ASN ASN D . n 
C 2 348 ASN 348 350 350 ASN ASN D . n 
C 2 349 VAL 349 351 351 VAL VAL D . n 
C 2 350 LYS 350 352 352 LYS LYS D . n 
C 2 351 THR 351 353 353 THR THR D . n 
C 2 352 ALA 352 354 354 ALA ALA D . n 
C 2 353 VAL 353 355 355 VAL VAL D . n 
C 2 354 CYS 354 356 356 CYS CYS D . n 
C 2 355 ASP 355 357 357 ASP ASP D . n 
C 2 356 ILE 356 358 358 ILE ILE D . n 
C 2 357 PRO 357 359 359 PRO PRO D . n 
C 2 358 PRO 358 360 360 PRO PRO D . n 
C 2 359 ARG 359 369 369 ARG ARG D . n 
C 2 360 GLY 360 370 370 GLY GLY D . n 
C 2 361 LEU 361 371 371 LEU LEU D . n 
C 2 362 LYS 362 372 372 LYS LYS D . n 
C 2 363 MET 363 373 373 MET MET D . n 
C 2 364 SER 364 374 374 SER SER D . n 
C 2 365 ALA 365 375 375 ALA ALA D . n 
C 2 366 THR 366 376 376 THR THR D . n 
C 2 367 PHE 367 377 377 PHE PHE D . n 
C 2 368 ILE 368 378 378 ILE ILE D . n 
C 2 369 GLY 369 379 379 GLY GLY D . n 
C 2 370 ASN 370 380 380 ASN ASN D . n 
C 2 371 SER 371 381 381 SER SER D . n 
C 2 372 THR 372 382 382 THR THR D . n 
C 2 373 ALA 373 383 383 ALA ALA D . n 
C 2 374 ILE 374 384 384 ILE ILE D . n 
C 2 375 GLN 375 385 385 GLN GLN D . n 
C 2 376 GLU 376 386 386 GLU GLU D . n 
C 2 377 LEU 377 387 387 LEU LEU D . n 
C 2 378 PHE 378 388 388 PHE PHE D . n 
C 2 379 LYS 379 389 389 LYS LYS D . n 
C 2 380 ARG 380 390 390 ARG ARG D . n 
C 2 381 ILE 381 391 391 ILE ILE D . n 
C 2 382 SER 382 392 392 SER SER D . n 
C 2 383 GLU 383 393 393 GLU GLU D . n 
C 2 384 GLN 384 394 394 GLN GLN D . n 
C 2 385 PHE 385 395 395 PHE PHE D . n 
C 2 386 THR 386 396 396 THR THR D . n 
C 2 387 ALA 387 397 397 ALA ALA D . n 
C 2 388 MET 388 398 398 MET MET D . n 
C 2 389 PHE 389 399 399 PHE PHE D . n 
C 2 390 ARG 390 400 400 ARG ARG D . n 
C 2 391 ARG 391 401 401 ARG ARG D . n 
C 2 392 LYS 392 402 402 LYS LYS D . n 
C 2 393 ALA 393 403 403 ALA ALA D . n 
C 2 394 PHE 394 404 404 PHE PHE D . n 
C 2 395 LEU 395 405 405 LEU LEU D . n 
C 2 396 HIS 396 406 406 HIS HIS D . n 
C 2 397 TRP 397 407 407 TRP TRP D . n 
C 2 398 TYR 398 408 408 TYR TYR D . n 
C 2 399 THR 399 409 409 THR THR D . n 
C 2 400 GLY 400 410 410 GLY GLY D . n 
C 2 401 GLU 401 411 411 GLU GLU D . n 
C 2 402 GLY 402 412 412 GLY GLY D . n 
C 2 403 MET 403 413 413 MET MET D . n 
C 2 404 ASP 404 414 414 ASP ASP D . n 
C 2 405 GLU 405 415 415 GLU GLU D . n 
C 2 406 MET 406 416 416 MET MET D . n 
C 2 407 GLU 407 417 417 GLU GLU D . n 
C 2 408 PHE 408 418 418 PHE PHE D . n 
C 2 409 THR 409 419 419 THR THR D . n 
C 2 410 GLU 410 420 420 GLU GLU D . n 
C 2 411 ALA 411 421 421 ALA ALA D . n 
C 2 412 GLU 412 422 422 GLU GLU D . n 
C 2 413 SER 413 423 423 SER SER D . n 
C 2 414 ASN 414 424 424 ASN ASN D . n 
C 2 415 MET 415 425 425 MET MET D . n 
C 2 416 ASN 416 426 426 ASN ASN D . n 
C 2 417 ASP 417 427 427 ASP ASP D . n 
C 2 418 LEU 418 428 428 LEU LEU D . n 
C 2 419 VAL 419 429 429 VAL VAL D . n 
C 2 420 SER 420 430 430 SER SER D . n 
C 2 421 GLU 421 431 431 GLU GLU D . n 
C 2 422 TYR 422 432 432 TYR TYR D . n 
C 2 423 GLN 423 433 433 GLN GLN D . n 
C 2 424 GLN 424 434 434 GLN GLN D . n 
C 2 425 TYR 425 435 435 TYR TYR D . n 
C 2 426 GLN 426 436 436 GLN GLN D . n 
C 2 427 ASP 427 437 437 ASP ASP D . n 
C 2 428 ALA 428 438 438 ALA ALA D . n 
C 2 429 THR 429 439 439 THR THR D . n 
C 2 430 ALA 430 440 440 ALA ALA D . n 
C 2 431 ASP 431 441 441 ASP ASP D . n 
C 2 432 GLU 432 442 ?   ?   ?   D . n 
C 2 433 GLN 433 443 ?   ?   ?   D . n 
C 2 434 GLY 434 444 ?   ?   ?   D . n 
C 2 435 GLU 435 445 ?   ?   ?   D . n 
C 2 436 PHE 436 446 ?   ?   ?   D . n 
C 2 437 GLU 437 447 ?   ?   ?   D . n 
C 2 438 GLU 438 448 ?   ?   ?   D . n 
C 2 439 GLU 439 449 ?   ?   ?   D . n 
C 2 440 GLU 440 450 ?   ?   ?   D . n 
C 2 441 GLY 441 451 ?   ?   ?   D . n 
C 2 442 GLU 442 452 ?   ?   ?   D . n 
C 2 443 ASP 443 453 ?   ?   ?   D . n 
C 2 444 GLU 444 454 ?   ?   ?   D . n 
C 2 445 ALA 445 455 ?   ?   ?   D . n 
D 3 1   MET 1   3   ?   ?   ?   E . n 
D 3 2   ALA 2   4   ?   ?   ?   E . n 
D 3 3   ASP 3   5   ?   ?   ?   E . n 
D 3 4   MET 4   6   6   MET MET E . n 
D 3 5   GLU 5   7   7   GLU GLU E . n 
D 3 6   VAL 6   8   8   VAL VAL E . n 
D 3 7   ILE 7   9   9   ILE ILE E . n 
D 3 8   GLU 8   10  10  GLU GLU E . n 
D 3 9   LEU 9   11  11  LEU LEU E . n 
D 3 10  ASN 10  12  12  ASN ASN E . n 
D 3 11  LYS 11  13  13  LYS LYS E . n 
D 3 12  CYS 12  14  14  CYS CYS E . n 
D 3 13  THR 13  15  15  THR THR E . n 
D 3 14  SER 14  16  16  SER SER E . n 
D 3 15  GLY 15  17  17  GLY GLY E . n 
D 3 16  GLN 16  18  18  GLN GLN E . n 
D 3 17  SER 17  19  19  SER SER E . n 
D 3 18  PHE 18  20  20  PHE PHE E . n 
D 3 19  GLU 19  21  21  GLU GLU E . n 
D 3 20  VAL 20  22  22  VAL VAL E . n 
D 3 21  ILE 21  23  23  ILE ILE E . n 
D 3 22  LEU 22  24  24  LEU LEU E . n 
D 3 23  LYS 23  25  25  LYS LYS E . n 
D 3 24  PRO 24  26  26  PRO PRO E . n 
D 3 25  PRO 25  27  27  PRO PRO E . n 
D 3 26  SER 26  28  28  SER SER E . n 
D 3 27  PHE 27  29  ?   ?   ?   E . n 
D 3 28  ASP 28  30  ?   ?   ?   E . n 
D 3 29  GLY 29  31  ?   ?   ?   E . n 
D 3 30  VAL 30  32  ?   ?   ?   E . n 
D 3 31  PRO 31  33  ?   ?   ?   E . n 
D 3 32  GLU 32  34  ?   ?   ?   E . n 
D 3 33  PHE 33  35  ?   ?   ?   E . n 
D 3 34  ASN 34  36  ?   ?   ?   E . n 
D 3 35  ALA 35  37  ?   ?   ?   E . n 
D 3 36  SER 36  38  ?   ?   ?   E . n 
D 3 37  LEU 37  39  ?   ?   ?   E . n 
D 3 38  PRO 38  40  ?   ?   ?   E . n 
D 3 39  ARG 39  41  ?   ?   ?   E . n 
D 3 40  ARG 40  42  ?   ?   ?   E . n 
D 3 41  ARG 41  43  ?   ?   ?   E . n 
D 3 42  ASP 42  44  44  ASP ASP E . n 
D 3 43  PRO 43  45  45  PRO PRO E . n 
D 3 44  SER 44  46  46  SER SER E . n 
D 3 45  LEU 45  47  47  LEU LEU E . n 
D 3 46  GLU 46  48  48  GLU GLU E . n 
D 3 47  GLU 47  49  49  GLU GLU E . n 
D 3 48  ILE 48  50  50  ILE ILE E . n 
D 3 49  GLN 49  51  51  GLN GLN E . n 
D 3 50  LYS 50  52  52  LYS LYS E . n 
D 3 51  LYS 51  53  53  LYS LYS E . n 
D 3 52  LEU 52  54  54  LEU LEU E . n 
D 3 53  GLU 53  55  55  GLU GLU E . n 
D 3 54  ALA 54  56  56  ALA ALA E . n 
D 3 55  ALA 55  57  57  ALA ALA E . n 
D 3 56  GLU 56  58  58  GLU GLU E . n 
D 3 57  GLU 57  59  59  GLU GLU E . n 
D 3 58  ARG 58  60  60  ARG ARG E . n 
D 3 59  ARG 59  61  61  ARG ARG E . n 
D 3 60  LYS 60  62  62  LYS LYS E . n 
D 3 61  TYR 61  63  63  TYR TYR E . n 
D 3 62  GLN 62  64  64  GLN GLN E . n 
D 3 63  GLU 63  65  65  GLU GLU E . n 
D 3 64  ALA 64  66  66  ALA ALA E . n 
D 3 65  GLU 65  67  67  GLU GLU E . n 
D 3 66  LEU 66  68  68  LEU LEU E . n 
D 3 67  LEU 67  69  69  LEU LEU E . n 
D 3 68  LYS 68  70  70  LYS LYS E . n 
D 3 69  HIS 69  71  71  HIS HIS E . n 
D 3 70  LEU 70  72  72  LEU LEU E . n 
D 3 71  ALA 71  73  73  ALA ALA E . n 
D 3 72  GLU 72  74  74  GLU GLU E . n 
D 3 73  LYS 73  75  75  LYS LYS E . n 
D 3 74  ARG 74  76  76  ARG ARG E . n 
D 3 75  GLU 75  77  77  GLU GLU E . n 
D 3 76  HIS 76  78  78  HIS HIS E . n 
D 3 77  GLU 77  79  79  GLU GLU E . n 
D 3 78  ARG 78  80  80  ARG ARG E . n 
D 3 79  GLU 79  81  81  GLU GLU E . n 
D 3 80  VAL 80  82  82  VAL VAL E . n 
D 3 81  ILE 81  83  83  ILE ILE E . n 
D 3 82  GLN 82  84  84  GLN GLN E . n 
D 3 83  LYS 83  85  85  LYS LYS E . n 
D 3 84  ALA 84  86  86  ALA ALA E . n 
D 3 85  ILE 85  87  87  ILE ILE E . n 
D 3 86  GLU 86  88  88  GLU GLU E . n 
D 3 87  GLU 87  89  89  GLU GLU E . n 
D 3 88  ASN 88  90  90  ASN ASN E . n 
D 3 89  ASN 89  91  91  ASN ASN E . n 
D 3 90  ASN 90  92  92  ASN ASN E . n 
D 3 91  PHE 91  93  93  PHE PHE E . n 
D 3 92  ILE 92  94  94  ILE ILE E . n 
D 3 93  LYS 93  95  95  LYS LYS E . n 
D 3 94  MET 94  96  96  MET MET E . n 
D 3 95  ALA 95  97  97  ALA ALA E . n 
D 3 96  LYS 96  98  98  LYS LYS E . n 
D 3 97  GLU 97  99  99  GLU GLU E . n 
D 3 98  LYS 98  100 100 LYS LYS E . n 
D 3 99  LEU 99  101 101 LEU LEU E . n 
D 3 100 ALA 100 102 102 ALA ALA E . n 
D 3 101 GLN 101 103 103 GLN GLN E . n 
D 3 102 LYS 102 104 104 LYS LYS E . n 
D 3 103 MET 103 105 105 MET MET E . n 
D 3 104 GLU 104 106 106 GLU GLU E . n 
D 3 105 SER 105 107 107 SER SER E . n 
D 3 106 ASN 106 108 108 ASN ASN E . n 
D 3 107 LYS 107 109 109 LYS LYS E . n 
D 3 108 GLU 108 110 110 GLU GLU E . n 
D 3 109 ASN 109 111 111 ASN ASN E . n 
D 3 110 ARG 110 112 112 ARG ARG E . n 
D 3 111 GLU 111 113 113 GLU GLU E . n 
D 3 112 ALA 112 114 114 ALA ALA E . n 
D 3 113 HIS 113 115 115 HIS HIS E . n 
D 3 114 LEU 114 116 116 LEU LEU E . n 
D 3 115 ALA 115 117 117 ALA ALA E . n 
D 3 116 ALA 116 118 118 ALA ALA E . n 
D 3 117 MET 117 119 119 MET MET E . n 
D 3 118 LEU 118 120 120 LEU LEU E . n 
D 3 119 GLU 119 121 121 GLU GLU E . n 
D 3 120 ARG 120 122 122 ARG ARG E . n 
D 3 121 LEU 121 123 123 LEU LEU E . n 
D 3 122 GLN 122 124 124 GLN GLN E . n 
D 3 123 GLU 123 125 125 GLU GLU E . n 
D 3 124 LYS 124 126 126 LYS LYS E . n 
D 3 125 ASP 125 127 127 ASP ASP E . n 
D 3 126 LYS 126 128 128 LYS LYS E . n 
D 3 127 HIS 127 129 129 HIS HIS E . n 
D 3 128 ALA 128 130 130 ALA ALA E . n 
D 3 129 GLU 129 131 131 GLU GLU E . n 
D 3 130 GLU 130 132 132 GLU GLU E . n 
D 3 131 VAL 131 133 133 VAL VAL E . n 
D 3 132 ARG 132 134 134 ARG ARG E . n 
D 3 133 LYS 133 135 135 LYS LYS E . n 
D 3 134 ASN 134 136 136 ASN ASN E . n 
D 3 135 LYS 135 137 137 LYS LYS E . n 
D 3 136 GLU 136 138 138 GLU GLU E . n 
D 3 137 LEU 137 139 139 LEU LEU E . n 
D 3 138 LYS 138 140 140 LYS LYS E . n 
D 3 139 GLU 139 141 ?   ?   ?   E . n 
D 3 140 GLU 140 142 ?   ?   ?   E . n 
D 3 141 ALA 141 143 ?   ?   ?   E . n 
D 3 142 SER 142 144 ?   ?   ?   E . n 
D 3 143 ARG 143 145 ?   ?   ?   E . n 
E 4 1   MET 1   1   1   MET MET F . n 
E 4 2   TYR 2   2   2   TYR TYR F . n 
E 4 3   THR 3   3   3   THR THR F . n 
E 4 4   PHE 4   4   4   PHE PHE F . n 
E 4 5   VAL 5   5   5   VAL VAL F . n 
E 4 6   VAL 6   6   6   VAL VAL F . n 
E 4 7   ARG 7   7   7   ARG ARG F . n 
E 4 8   ASP 8   8   8   ASP ASP F . n 
E 4 9   GLU 9   9   9   GLU GLU F . n 
E 4 10  ASN 10  10  10  ASN ASN F . n 
E 4 11  SER 11  11  11  SER SER F . n 
E 4 12  SER 12  12  12  SER SER F . n 
E 4 13  VAL 13  13  13  VAL VAL F . n 
E 4 14  TYR 14  14  14  TYR TYR F . n 
E 4 15  ALA 15  15  15  ALA ALA F . n 
E 4 16  GLU 16  16  16  GLU GLU F . n 
E 4 17  VAL 17  17  17  VAL VAL F . n 
E 4 18  SER 18  18  18  SER SER F . n 
E 4 19  ARG 19  19  19  ARG ARG F . n 
E 4 20  LEU 20  20  20  LEU LEU F . n 
E 4 21  LEU 21  21  21  LEU LEU F . n 
E 4 22  LEU 22  22  22  LEU LEU F . n 
E 4 23  ALA 23  23  23  ALA ALA F . n 
E 4 24  THR 24  24  24  THR THR F . n 
E 4 25  GLY 25  25  25  GLY GLY F . n 
E 4 26  GLN 26  26  26  GLN GLN F . n 
E 4 27  TRP 27  27  27  TRP TRP F . n 
E 4 28  LYS 28  28  28  LYS LYS F . n 
E 4 29  ARG 29  29  29  ARG ARG F . n 
E 4 30  LEU 30  30  30  LEU LEU F . n 
E 4 31  ARG 31  31  31  ARG ARG F . n 
E 4 32  LYS 32  32  32  LYS LYS F . n 
E 4 33  ASP 33  33  33  ASP ASP F . n 
E 4 34  ASN 34  34  34  ASN ASN F . n 
E 4 35  PRO 35  35  35  PRO PRO F . n 
E 4 36  ARG 36  36  36  ARG ARG F . n 
E 4 37  PHE 37  37  37  PHE PHE F . n 
E 4 38  ASN 38  38  38  ASN ASN F . n 
E 4 39  LEU 39  39  39  LEU LEU F . n 
E 4 40  MET 40  40  40  MET MET F . n 
E 4 41  LEU 41  41  41  LEU LEU F . n 
E 4 42  GLY 42  42  42  GLY GLY F . n 
E 4 43  GLU 43  43  43  GLU GLU F . n 
E 4 44  ARG 44  44  44  ARG ARG F . n 
E 4 45  ASN 45  45  45  ASN ASN F . n 
E 4 46  ARG 46  46  46  ARG ARG F . n 
E 4 47  LEU 47  47  47  LEU LEU F . n 
E 4 48  PRO 48  48  48  PRO PRO F . n 
E 4 49  PHE 49  49  49  PHE PHE F . n 
E 4 50  GLY 50  50  50  GLY GLY F . n 
E 4 51  ARG 51  51  51  ARG ARG F . n 
E 4 52  LEU 52  52  52  LEU LEU F . n 
E 4 53  GLY 53  53  53  GLY GLY F . n 
E 4 54  HIS 54  54  54  HIS HIS F . n 
E 4 55  GLU 55  55  55  GLU GLU F . n 
E 4 56  PRO 56  56  56  PRO PRO F . n 
E 4 57  GLY 57  57  57  GLY GLY F . n 
E 4 58  LEU 58  58  58  LEU LEU F . n 
E 4 59  VAL 59  59  59  VAL VAL F . n 
E 4 60  GLN 60  60  60  GLN GLN F . n 
E 4 61  LEU 61  61  61  LEU LEU F . n 
E 4 62  VAL 62  62  62  VAL VAL F . n 
E 4 63  ASN 63  63  63  ASN ASN F . n 
E 4 64  TYR 64  64  64  TYR TYR F . n 
E 4 65  TYR 65  65  65  TYR TYR F . n 
E 4 66  ARG 66  66  66  ARG ARG F . n 
E 4 67  GLY 67  67  67  GLY GLY F . n 
E 4 68  ALA 68  68  68  ALA ALA F . n 
E 4 69  ASP 69  69  69  ASP ASP F . n 
E 4 70  LYS 70  70  70  LYS LYS F . n 
E 4 71  LEU 71  71  71  LEU LEU F . n 
E 4 72  CYS 72  72  72  CYS CYS F . n 
E 4 73  ARG 73  73  73  ARG ARG F . n 
E 4 74  LYS 74  74  74  LYS LYS F . n 
E 4 75  ALA 75  75  75  ALA ALA F . n 
E 4 76  SER 76  76  76  SER SER F . n 
E 4 77  LEU 77  77  77  LEU LEU F . n 
E 4 78  VAL 78  78  78  VAL VAL F . n 
E 4 79  LYS 79  79  79  LYS LYS F . n 
E 4 80  LEU 80  80  80  LEU LEU F . n 
E 4 81  ILE 81  81  81  ILE ILE F . n 
E 4 82  LYS 82  82  82  LYS LYS F . n 
E 4 83  THR 83  83  83  THR THR F . n 
E 4 84  SER 84  84  84  SER SER F . n 
E 4 85  PRO 85  85  85  PRO PRO F . n 
E 4 86  GLU 86  86  86  GLU GLU F . n 
E 4 87  LEU 87  87  87  LEU LEU F . n 
E 4 88  SER 88  88  88  SER SER F . n 
E 4 89  GLU 89  89  89  GLU GLU F . n 
E 4 90  SER 90  90  90  SER SER F . n 
E 4 91  CYS 91  91  91  CYS CYS F . n 
E 4 92  THR 92  92  92  THR THR F . n 
E 4 93  TRP 93  93  93  TRP TRP F . n 
E 4 94  PHE 94  94  94  PHE PHE F . n 
E 4 95  PRO 95  95  95  PRO PRO F . n 
E 4 96  GLU 96  96  96  GLU GLU F . n 
E 4 97  SER 97  97  97  SER SER F . n 
E 4 98  TYR 98  98  98  TYR TYR F . n 
E 4 99  VAL 99  99  99  VAL VAL F . n 
E 4 100 ILE 100 100 100 ILE ILE F . n 
E 4 101 TYR 101 101 101 TYR TYR F . n 
E 4 102 PRO 102 102 102 PRO PRO F . n 
E 4 103 THR 103 103 103 THR THR F . n 
E 4 104 ASN 104 104 ?   ?   ?   F . n 
E 4 105 LEU 105 105 ?   ?   ?   F . n 
E 4 106 LYS 106 106 ?   ?   ?   F . n 
E 4 107 THR 107 107 ?   ?   ?   F . n 
E 4 108 PRO 108 108 ?   ?   ?   F . n 
E 4 109 VAL 109 109 ?   ?   ?   F . n 
E 4 110 ALA 110 110 ?   ?   ?   F . n 
E 4 111 PRO 111 111 ?   ?   ?   F . n 
E 4 112 ALA 112 112 ?   ?   ?   F . n 
E 4 113 GLN 113 113 ?   ?   ?   F . n 
E 4 114 ASN 114 114 ?   ?   ?   F . n 
E 4 115 GLY 115 115 ?   ?   ?   F . n 
E 4 116 ILE 116 116 ?   ?   ?   F . n 
E 4 117 ARG 117 117 ?   ?   ?   F . n 
E 4 118 HIS 118 118 ?   ?   ?   F . n 
E 4 119 LEU 119 119 ?   ?   ?   F . n 
E 4 120 ILE 120 120 ?   ?   ?   F . n 
E 4 121 ASN 121 121 ?   ?   ?   F . n 
E 4 122 ASN 122 122 ?   ?   ?   F . n 
E 4 123 THR 123 123 ?   ?   ?   F . n 
E 4 124 ARG 124 124 ?   ?   ?   F . n 
E 4 125 THR 125 125 125 THR THR F . n 
E 4 126 ASP 126 126 126 ASP ASP F . n 
E 4 127 GLU 127 127 127 GLU GLU F . n 
E 4 128 ARG 128 128 128 ARG ARG F . n 
E 4 129 GLU 129 129 129 GLU GLU F . n 
E 4 130 VAL 130 130 130 VAL VAL F . n 
E 4 131 PHE 131 131 131 PHE PHE F . n 
E 4 132 LEU 132 132 132 LEU LEU F . n 
E 4 133 ALA 133 133 133 ALA ALA F . n 
E 4 134 ALA 134 134 134 ALA ALA F . n 
E 4 135 TYR 135 135 135 TYR TYR F . n 
E 4 136 ASN 136 136 136 ASN ASN F . n 
E 4 137 ARG 137 137 137 ARG ARG F . n 
E 4 138 ARG 138 138 ?   ?   ?   F . n 
E 4 139 ARG 139 139 ?   ?   ?   F . n 
E 4 140 GLU 140 140 ?   ?   ?   F . n 
E 4 141 GLY 141 141 ?   ?   ?   F . n 
E 4 142 ARG 142 142 ?   ?   ?   F . n 
E 4 143 GLU 143 143 ?   ?   ?   F . n 
E 4 144 GLY 144 144 144 GLY GLY F . n 
E 4 145 ASN 145 145 145 ASN ASN F . n 
E 4 146 VAL 146 146 146 VAL VAL F . n 
E 4 147 TRP 147 147 147 TRP TRP F . n 
E 4 148 ILE 148 148 148 ILE ILE F . n 
E 4 149 ALA 149 149 149 ALA ALA F . n 
E 4 150 LYS 150 150 ?   ?   ?   F . n 
E 4 151 SER 151 151 ?   ?   ?   F . n 
E 4 152 SER 152 152 ?   ?   ?   F . n 
E 4 153 ALA 153 153 ?   ?   ?   F . n 
E 4 154 GLY 154 154 ?   ?   ?   F . n 
E 4 155 ALA 155 155 ?   ?   ?   F . n 
E 4 156 LYS 156 156 ?   ?   ?   F . n 
E 4 157 GLY 157 157 ?   ?   ?   F . n 
E 4 158 GLU 158 158 ?   ?   ?   F . n 
E 4 159 GLY 159 159 159 GLY GLY F . n 
E 4 160 ILE 160 160 160 ILE ILE F . n 
E 4 161 LEU 161 161 161 LEU LEU F . n 
E 4 162 ILE 162 162 162 ILE ILE F . n 
E 4 163 SER 163 163 163 SER SER F . n 
E 4 164 SER 164 164 164 SER SER F . n 
E 4 165 GLU 165 165 165 GLU GLU F . n 
E 4 166 ALA 166 166 166 ALA ALA F . n 
E 4 167 SER 167 167 167 SER SER F . n 
E 4 168 GLU 168 168 168 GLU GLU F . n 
E 4 169 LEU 169 169 169 LEU LEU F . n 
E 4 170 LEU 170 170 170 LEU LEU F . n 
E 4 171 ASP 171 171 171 ASP ASP F . n 
E 4 172 PHE 172 172 172 PHE PHE F . n 
E 4 173 ILE 173 173 173 ILE ILE F . n 
E 4 174 ASP 174 174 174 ASP ASP F . n 
E 4 175 GLU 175 175 175 GLU GLU F . n 
E 4 176 GLN 176 176 176 GLN GLN F . n 
E 4 177 GLY 177 177 177 GLY GLY F . n 
E 4 178 GLN 178 178 178 GLN GLN F . n 
E 4 179 VAL 179 179 179 VAL VAL F . n 
E 4 180 HIS 180 180 180 HIS HIS F . n 
E 4 181 VAL 181 181 181 VAL VAL F . n 
E 4 182 ILE 182 182 182 ILE ILE F . n 
E 4 183 GLN 183 183 183 GLN GLN F . n 
E 4 184 LYS 184 184 184 LYS LYS F . n 
E 4 185 TYR 185 185 185 TYR TYR F . n 
E 4 186 LEU 186 186 186 LEU LEU F . n 
E 4 187 GLU 187 187 187 GLU GLU F . n 
E 4 188 LYS 188 188 188 LYS LYS F . n 
E 4 189 PRO 189 189 189 PRO PRO F . n 
E 4 190 LEU 190 190 190 LEU LEU F . n 
E 4 191 LEU 191 191 191 LEU LEU F . n 
E 4 192 LEU 192 192 192 LEU LEU F . n 
E 4 193 GLU 193 193 193 GLU GLU F . n 
E 4 194 PRO 194 194 194 PRO PRO F . n 
E 4 195 GLY 195 195 195 GLY GLY F . n 
E 4 196 HIS 196 196 196 HIS HIS F . n 
E 4 197 ARG 197 197 197 ARG ARG F . n 
E 4 198 LYS 198 198 198 LYS LYS F . n 
E 4 199 PHE 199 199 199 PHE PHE F . n 
E 4 200 ASP 200 200 200 ASP ASP F . n 
E 4 201 ILE 201 201 201 ILE ILE F . n 
E 4 202 ARG 202 202 202 ARG ARG F . n 
E 4 203 SER 203 203 203 SER SER F . n 
E 4 204 TRP 204 204 204 TRP TRP F . n 
E 4 205 VAL 205 205 205 VAL VAL F . n 
E 4 206 LEU 206 206 206 LEU LEU F . n 
E 4 207 VAL 207 207 207 VAL VAL F . n 
E 4 208 ASP 208 208 208 ASP ASP F . n 
E 4 209 HIS 209 209 209 HIS HIS F . n 
E 4 210 LEU 210 210 210 LEU LEU F . n 
E 4 211 TYR 211 211 211 TYR TYR F . n 
E 4 212 ASN 212 212 212 ASN ASN F . n 
E 4 213 ILE 213 213 213 ILE ILE F . n 
E 4 214 TYR 214 214 214 TYR TYR F . n 
E 4 215 LEU 215 215 215 LEU LEU F . n 
E 4 216 TYR 216 216 216 TYR TYR F . n 
E 4 217 ARG 217 217 217 ARG ARG F . n 
E 4 218 GLU 218 218 218 GLU GLU F . n 
E 4 219 GLY 219 219 219 GLY GLY F . n 
E 4 220 VAL 220 220 220 VAL VAL F . n 
E 4 221 LEU 221 221 221 LEU LEU F . n 
E 4 222 ARG 222 222 222 ARG ARG F . n 
E 4 223 THR 223 223 223 THR THR F . n 
E 4 224 SER 224 224 224 SER SER F . n 
E 4 225 SER 225 225 225 SER SER F . n 
E 4 226 GLU 226 226 226 GLU GLU F . n 
E 4 227 PRO 227 227 227 PRO PRO F . n 
E 4 228 TYR 228 228 228 TYR TYR F . n 
E 4 229 ASN 229 229 229 ASN ASN F . n 
E 4 230 SER 230 230 230 SER SER F . n 
E 4 231 ALA 231 231 231 ALA ALA F . n 
E 4 232 ASN 232 232 232 ASN ASN F . n 
E 4 233 PHE 233 233 233 PHE PHE F . n 
E 4 234 GLN 234 234 234 GLN GLN F . n 
E 4 235 ASP 235 235 235 ASP ASP F . n 
E 4 236 LYS 236 236 236 LYS LYS F . n 
E 4 237 THR 237 237 237 THR THR F . n 
E 4 238 CYS 238 238 238 CYS CYS F . n 
E 4 239 HIS 239 239 239 HIS HIS F . n 
E 4 240 LEU 240 240 240 LEU LEU F . n 
E 4 241 THR 241 241 241 THR THR F . n 
E 4 242 ASN 242 242 242 ASN ASN F . n 
E 4 243 HIS 243 243 243 HIS HIS F . n 
E 4 244 CYS 244 244 244 CYS CYS F . n 
E 4 245 ILE 245 245 245 ILE ILE F . n 
E 4 246 GLN 246 246 246 GLN GLN F . n 
E 4 247 LYS 247 247 247 LYS LYS F . n 
E 4 248 GLU 248 248 248 GLU GLU F . n 
E 4 249 TYR 249 249 249 TYR TYR F . n 
E 4 250 SER 250 250 250 SER SER F . n 
E 4 251 LYS 251 251 ?   ?   ?   F . n 
E 4 252 ASN 252 252 ?   ?   ?   F . n 
E 4 253 TYR 253 253 ?   ?   ?   F . n 
E 4 254 GLY 254 254 ?   ?   ?   F . n 
E 4 255 ARG 255 255 255 ARG ARG F . n 
E 4 256 TYR 256 256 256 TYR TYR F . n 
E 4 257 GLU 257 257 257 GLU GLU F . n 
E 4 258 GLU 258 258 258 GLU GLU F . n 
E 4 259 GLY 259 259 259 GLY GLY F . n 
E 4 260 ASN 260 260 260 ASN ASN F . n 
E 4 261 GLU 261 261 261 GLU GLU F . n 
E 4 262 MET 262 262 262 MET MET F . n 
E 4 263 PHE 263 263 263 PHE PHE F . n 
E 4 264 PHE 264 264 264 PHE PHE F . n 
E 4 265 GLU 265 265 265 GLU GLU F . n 
E 4 266 GLU 266 266 266 GLU GLU F . n 
E 4 267 PHE 267 267 267 PHE PHE F . n 
E 4 268 ASN 268 268 268 ASN ASN F . n 
E 4 269 GLN 269 269 269 GLN GLN F . n 
E 4 270 TYR 270 270 270 TYR TYR F . n 
E 4 271 LEU 271 271 271 LEU LEU F . n 
E 4 272 MET 272 272 272 MET MET F . n 
E 4 273 ASP 273 273 273 ASP ASP F . n 
E 4 274 ALA 274 274 274 ALA ALA F . n 
E 4 275 LEU 275 275 275 LEU LEU F . n 
E 4 276 ASN 276 276 276 ASN ASN F . n 
E 4 277 THR 277 277 277 THR THR F . n 
E 4 278 THR 278 278 278 THR THR F . n 
E 4 279 LEU 279 279 279 LEU LEU F . n 
E 4 280 GLU 280 280 280 GLU GLU F . n 
E 4 281 ASN 281 281 281 ASN ASN F . n 
E 4 282 SER 282 282 282 SER SER F . n 
E 4 283 ILE 283 283 283 ILE ILE F . n 
E 4 284 LEU 284 284 284 LEU LEU F . n 
E 4 285 LEU 285 285 285 LEU LEU F . n 
E 4 286 GLN 286 286 286 GLN GLN F . n 
E 4 287 ILE 287 287 287 ILE ILE F . n 
E 4 288 LYS 288 288 288 LYS LYS F . n 
E 4 289 HIS 289 289 289 HIS HIS F . n 
E 4 290 ILE 290 290 290 ILE ILE F . n 
E 4 291 ILE 291 291 291 ILE ILE F . n 
E 4 292 ARG 292 292 292 ARG ARG F . n 
E 4 293 SER 293 293 293 SER SER F . n 
E 4 294 CYS 294 294 294 CYS CYS F . n 
E 4 295 LEU 295 295 295 LEU LEU F . n 
E 4 296 MET 296 296 296 MET MET F . n 
E 4 297 CYS 297 297 297 CYS CYS F . n 
E 4 298 ILE 298 298 298 ILE ILE F . n 
E 4 299 GLU 299 299 299 GLU GLU F . n 
E 4 300 PRO 300 300 300 PRO PRO F . n 
E 4 301 ALA 301 301 301 ALA ALA F . n 
E 4 302 ILE 302 302 302 ILE ILE F . n 
E 4 303 SER 303 303 303 SER SER F . n 
E 4 304 THR 304 304 304 THR THR F . n 
E 4 305 LYS 305 305 305 LYS LYS F . n 
E 4 306 HIS 306 306 306 HIS HIS F . n 
E 4 307 LEU 307 307 307 LEU LEU F . n 
E 4 308 HIS 308 308 308 HIS HIS F . n 
E 4 309 TYR 309 309 309 TYR TYR F . n 
E 4 310 GLN 310 310 310 GLN GLN F . n 
E 4 311 SER 311 311 311 SER SER F . n 
E 4 312 PHE 312 312 312 PHE PHE F . n 
E 4 313 GLN 313 313 313 GLN GLN F . n 
E 4 314 LEU 314 314 314 LEU LEU F . n 
E 4 315 PHE 315 315 315 PHE PHE F . n 
E 4 316 GLY 316 316 316 GLY GLY F . n 
E 4 317 PHE 317 317 317 PHE PHE F . n 
E 4 318 ASP 318 318 318 ASP ASP F . n 
E 4 319 PHE 319 319 319 PHE PHE F . n 
E 4 320 MET 320 320 320 MET MET F . n 
E 4 321 VAL 321 321 321 VAL VAL F . n 
E 4 322 ASP 322 322 322 ASP ASP F . n 
E 4 323 GLU 323 323 323 GLU GLU F . n 
E 4 324 GLU 324 324 324 GLU GLU F . n 
E 4 325 LEU 325 325 325 LEU LEU F . n 
E 4 326 LYS 326 326 326 LYS LYS F . n 
E 4 327 VAL 327 327 327 VAL VAL F . n 
E 4 328 TRP 328 328 328 TRP TRP F . n 
E 4 329 LEU 329 329 329 LEU LEU F . n 
E 4 330 ILE 330 330 330 ILE ILE F . n 
E 4 331 GLU 331 331 331 GLU GLU F . n 
E 4 332 VAL 332 332 332 VAL VAL F . n 
E 4 333 ASN 333 333 333 ASN ASN F . n 
E 4 334 GLY 334 334 334 GLY GLY F . n 
E 4 335 ALA 335 335 335 ALA ALA F . n 
E 4 336 PRO 336 336 336 PRO PRO F . n 
E 4 337 ALA 337 337 337 ALA ALA F . n 
E 4 338 CYS 338 338 338 CYS CYS F . n 
E 4 339 ALA 339 339 339 ALA ALA F . n 
E 4 340 GLN 340 340 340 GLN GLN F . n 
E 4 341 LYS 341 341 341 LYS LYS F . n 
E 4 342 LEU 342 342 342 LEU LEU F . n 
E 4 343 TYR 343 343 343 TYR TYR F . n 
E 4 344 ALA 344 344 344 ALA ALA F . n 
E 4 345 GLU 345 345 345 GLU GLU F . n 
E 4 346 LEU 346 346 346 LEU LEU F . n 
E 4 347 CYS 347 347 347 CYS CYS F . n 
E 4 348 GLN 348 348 348 GLN GLN F . n 
E 4 349 GLY 349 349 349 GLY GLY F . n 
E 4 350 ILE 350 350 350 ILE ILE F . n 
E 4 351 VAL 351 351 351 VAL VAL F . n 
E 4 352 ASP 352 352 352 ASP ASP F . n 
E 4 353 VAL 353 353 353 VAL VAL F . n 
E 4 354 ALA 354 354 354 ALA ALA F . n 
E 4 355 ILE 355 355 355 ILE ILE F . n 
E 4 356 SER 356 356 356 SER SER F . n 
E 4 357 SER 357 357 357 SER SER F . n 
E 4 358 VAL 358 358 358 VAL VAL F . n 
E 4 359 PHE 359 359 359 PHE PHE F . n 
E 4 360 PRO 360 360 360 PRO PRO F . n 
E 4 361 LEU 361 361 361 LEU LEU F . n 
E 4 362 ALA 362 362 362 ALA ALA F . n 
E 4 363 ASP 363 363 ?   ?   ?   F . n 
E 4 364 THR 364 364 ?   ?   ?   F . n 
E 4 365 GLY 365 365 ?   ?   ?   F . n 
E 4 366 GLN 366 366 ?   ?   ?   F . n 
E 4 367 LYS 367 367 ?   ?   ?   F . n 
E 4 368 THR 368 368 ?   ?   ?   F . n 
E 4 369 SER 369 369 ?   ?   ?   F . n 
E 4 370 GLN 370 370 ?   ?   ?   F . n 
E 4 371 PRO 371 371 ?   ?   ?   F . n 
E 4 372 THR 372 372 372 THR THR F . n 
E 4 373 SER 373 373 373 SER SER F . n 
E 4 374 ILE 374 374 374 ILE ILE F . n 
E 4 375 PHE 375 375 375 PHE PHE F . n 
E 4 376 ILE 376 376 376 ILE ILE F . n 
E 4 377 LYS 377 377 377 LYS LYS F . n 
E 4 378 LEU 378 378 378 LEU LEU F . n 
E 4 379 HIS 379 379 379 HIS HIS F . n 
E 4 380 HIS 380 380 380 HIS HIS F . n 
E 4 381 HIS 381 381 ?   ?   ?   F . n 
E 4 382 HIS 382 382 ?   ?   ?   F . n 
E 4 383 HIS 383 383 ?   ?   ?   F . n 
E 4 384 HIS 384 384 ?   ?   ?   F . n 
F 2 1   MET 1   1   1   MET MET B . n 
F 2 2   ARG 2   2   2   ARG ARG B . n 
F 2 3   GLU 3   3   3   GLU GLU B . n 
F 2 4   ILE 4   4   4   ILE ILE B . n 
F 2 5   VAL 5   5   5   VAL VAL B . n 
F 2 6   HIS 6   6   6   HIS HIS B . n 
F 2 7   ILE 7   7   7   ILE ILE B . n 
F 2 8   GLN 8   8   8   GLN GLN B . n 
F 2 9   ALA 9   9   9   ALA ALA B . n 
F 2 10  GLY 10  10  10  GLY GLY B . n 
F 2 11  GLN 11  11  11  GLN GLN B . n 
F 2 12  CYS 12  12  12  CYS CYS B . n 
F 2 13  GLY 13  13  13  GLY GLY B . n 
F 2 14  ASN 14  14  14  ASN ASN B . n 
F 2 15  GLN 15  15  15  GLN GLN B . n 
F 2 16  ILE 16  16  16  ILE ILE B . n 
F 2 17  GLY 17  17  17  GLY GLY B . n 
F 2 18  ALA 18  18  18  ALA ALA B . n 
F 2 19  LYS 19  19  19  LYS LYS B . n 
F 2 20  PHE 20  20  20  PHE PHE B . n 
F 2 21  TRP 21  21  21  TRP TRP B . n 
F 2 22  GLU 22  22  22  GLU GLU B . n 
F 2 23  VAL 23  23  23  VAL VAL B . n 
F 2 24  ILE 24  24  24  ILE ILE B . n 
F 2 25  SER 25  25  25  SER SER B . n 
F 2 26  ASP 26  26  26  ASP ASP B . n 
F 2 27  GLU 27  27  27  GLU GLU B . n 
F 2 28  HIS 28  28  28  HIS HIS B . n 
F 2 29  GLY 29  29  29  GLY GLY B . n 
F 2 30  ILE 30  30  30  ILE ILE B . n 
F 2 31  ASP 31  31  31  ASP ASP B . n 
F 2 32  PRO 32  32  32  PRO PRO B . n 
F 2 33  THR 33  33  33  THR THR B . n 
F 2 34  GLY 34  34  34  GLY GLY B . n 
F 2 35  SER 35  35  35  SER SER B . n 
F 2 36  TYR 36  36  36  TYR TYR B . n 
F 2 37  HIS 37  37  37  HIS HIS B . n 
F 2 38  GLY 38  38  38  GLY GLY B . n 
F 2 39  ASP 39  39  39  ASP ASP B . n 
F 2 40  SER 40  40  40  SER SER B . n 
F 2 41  ASP 41  41  41  ASP ASP B . n 
F 2 42  LEU 42  42  42  LEU LEU B . n 
F 2 43  GLN 43  45  45  GLN GLN B . n 
F 2 44  LEU 44  46  46  LEU LEU B . n 
F 2 45  GLU 45  47  47  GLU GLU B . n 
F 2 46  ARG 46  48  48  ARG ARG B . n 
F 2 47  ILE 47  49  49  ILE ILE B . n 
F 2 48  ASN 48  50  50  ASN ASN B . n 
F 2 49  VAL 49  51  51  VAL VAL B . n 
F 2 50  TYR 50  52  52  TYR TYR B . n 
F 2 51  TYR 51  53  53  TYR TYR B . n 
F 2 52  ASN 52  54  54  ASN ASN B . n 
F 2 53  GLU 53  55  55  GLU GLU B . n 
F 2 54  ALA 54  56  56  ALA ALA B . n 
F 2 55  THR 55  57  57  THR THR B . n 
F 2 56  GLY 56  58  58  GLY GLY B . n 
F 2 57  ASN 57  59  59  ASN ASN B . n 
F 2 58  LYS 58  60  60  LYS LYS B . n 
F 2 59  TYR 59  61  61  TYR TYR B . n 
F 2 60  VAL 60  62  62  VAL VAL B . n 
F 2 61  PRO 61  63  63  PRO PRO B . n 
F 2 62  ARG 62  64  64  ARG ARG B . n 
F 2 63  ALA 63  65  65  ALA ALA B . n 
F 2 64  ILE 64  66  66  ILE ILE B . n 
F 2 65  LEU 65  67  67  LEU LEU B . n 
F 2 66  VAL 66  68  68  VAL VAL B . n 
F 2 67  ASP 67  69  69  ASP ASP B . n 
F 2 68  LEU 68  70  70  LEU LEU B . n 
F 2 69  GLU 69  71  71  GLU GLU B . n 
F 2 70  PRO 70  72  72  PRO PRO B . n 
F 2 71  GLY 71  73  73  GLY GLY B . n 
F 2 72  THR 72  74  74  THR THR B . n 
F 2 73  MET 73  75  75  MET MET B . n 
F 2 74  ASP 74  76  76  ASP ASP B . n 
F 2 75  SER 75  77  77  SER SER B . n 
F 2 76  VAL 76  78  78  VAL VAL B . n 
F 2 77  ARG 77  79  79  ARG ARG B . n 
F 2 78  SER 78  80  80  SER SER B . n 
F 2 79  GLY 79  81  81  GLY GLY B . n 
F 2 80  PRO 80  82  82  PRO PRO B . n 
F 2 81  PHE 81  83  83  PHE PHE B . n 
F 2 82  GLY 82  84  84  GLY GLY B . n 
F 2 83  GLN 83  85  85  GLN GLN B . n 
F 2 84  ILE 84  86  86  ILE ILE B . n 
F 2 85  PHE 85  87  87  PHE PHE B . n 
F 2 86  ARG 86  88  88  ARG ARG B . n 
F 2 87  PRO 87  89  89  PRO PRO B . n 
F 2 88  ASP 88  90  90  ASP ASP B . n 
F 2 89  ASN 89  91  91  ASN ASN B . n 
F 2 90  PHE 90  92  92  PHE PHE B . n 
F 2 91  VAL 91  93  93  VAL VAL B . n 
F 2 92  PHE 92  94  94  PHE PHE B . n 
F 2 93  GLY 93  95  95  GLY GLY B . n 
F 2 94  GLN 94  96  96  GLN GLN B . n 
F 2 95  SER 95  97  97  SER SER B . n 
F 2 96  GLY 96  98  98  GLY GLY B . n 
F 2 97  ALA 97  99  99  ALA ALA B . n 
F 2 98  GLY 98  100 100 GLY GLY B . n 
F 2 99  ASN 99  101 101 ASN ASN B . n 
F 2 100 ASN 100 102 102 ASN ASN B . n 
F 2 101 TRP 101 103 103 TRP TRP B . n 
F 2 102 ALA 102 104 104 ALA ALA B . n 
F 2 103 LYS 103 105 105 LYS LYS B . n 
F 2 104 GLY 104 106 106 GLY GLY B . n 
F 2 105 HIS 105 107 107 HIS HIS B . n 
F 2 106 TYR 106 108 108 TYR TYR B . n 
F 2 107 THR 107 109 109 THR THR B . n 
F 2 108 GLU 108 110 110 GLU GLU B . n 
F 2 109 GLY 109 111 111 GLY GLY B . n 
F 2 110 ALA 110 112 112 ALA ALA B . n 
F 2 111 GLU 111 113 113 GLU GLU B . n 
F 2 112 LEU 112 114 114 LEU LEU B . n 
F 2 113 VAL 113 115 115 VAL VAL B . n 
F 2 114 ASP 114 116 116 ASP ASP B . n 
F 2 115 SER 115 117 117 SER SER B . n 
F 2 116 VAL 116 118 118 VAL VAL B . n 
F 2 117 LEU 117 119 119 LEU LEU B . n 
F 2 118 ASP 118 120 120 ASP ASP B . n 
F 2 119 VAL 119 121 121 VAL VAL B . n 
F 2 120 VAL 120 122 122 VAL VAL B . n 
F 2 121 ARG 121 123 123 ARG ARG B . n 
F 2 122 LYS 122 124 124 LYS LYS B . n 
F 2 123 GLU 123 125 125 GLU GLU B . n 
F 2 124 SER 124 126 126 SER SER B . n 
F 2 125 GLU 125 127 127 GLU GLU B . n 
F 2 126 SER 126 128 128 SER SER B . n 
F 2 127 CYS 127 129 129 CYS CYS B . n 
F 2 128 ASP 128 130 130 ASP ASP B . n 
F 2 129 CYS 129 131 131 CYS CYS B . n 
F 2 130 LEU 130 132 132 LEU LEU B . n 
F 2 131 GLN 131 133 133 GLN GLN B . n 
F 2 132 GLY 132 134 134 GLY GLY B . n 
F 2 133 PHE 133 135 135 PHE PHE B . n 
F 2 134 GLN 134 136 136 GLN GLN B . n 
F 2 135 LEU 135 137 137 LEU LEU B . n 
F 2 136 THR 136 138 138 THR THR B . n 
F 2 137 HIS 137 139 139 HIS HIS B . n 
F 2 138 SER 138 140 140 SER SER B . n 
F 2 139 LEU 139 141 141 LEU LEU B . n 
F 2 140 GLY 140 142 142 GLY GLY B . n 
F 2 141 GLY 141 143 143 GLY GLY B . n 
F 2 142 GLY 142 144 144 GLY GLY B . n 
F 2 143 THR 143 145 145 THR THR B . n 
F 2 144 GLY 144 146 146 GLY GLY B . n 
F 2 145 SER 145 147 147 SER SER B . n 
F 2 146 GLY 146 148 148 GLY GLY B . n 
F 2 147 MET 147 149 149 MET MET B . n 
F 2 148 GLY 148 150 150 GLY GLY B . n 
F 2 149 THR 149 151 151 THR THR B . n 
F 2 150 LEU 150 152 152 LEU LEU B . n 
F 2 151 LEU 151 153 153 LEU LEU B . n 
F 2 152 ILE 152 154 154 ILE ILE B . n 
F 2 153 SER 153 155 155 SER SER B . n 
F 2 154 LYS 154 156 156 LYS LYS B . n 
F 2 155 ILE 155 157 157 ILE ILE B . n 
F 2 156 ARG 156 158 158 ARG ARG B . n 
F 2 157 GLU 157 159 159 GLU GLU B . n 
F 2 158 GLU 158 160 160 GLU GLU B . n 
F 2 159 TYR 159 161 161 TYR TYR B . n 
F 2 160 PRO 160 162 162 PRO PRO B . n 
F 2 161 ASP 161 163 163 ASP ASP B . n 
F 2 162 ARG 162 164 164 ARG ARG B . n 
F 2 163 ILE 163 165 165 ILE ILE B . n 
F 2 164 MET 164 166 166 MET MET B . n 
F 2 165 ASN 165 167 167 ASN ASN B . n 
F 2 166 THR 166 168 168 THR THR B . n 
F 2 167 PHE 167 169 169 PHE PHE B . n 
F 2 168 SER 168 170 170 SER SER B . n 
F 2 169 VAL 169 171 171 VAL VAL B . n 
F 2 170 MET 170 172 172 MET MET B . n 
F 2 171 PRO 171 173 173 PRO PRO B . n 
F 2 172 SER 172 174 174 SER SER B . n 
F 2 173 PRO 173 175 175 PRO PRO B . n 
F 2 174 LYS 174 176 176 LYS LYS B . n 
F 2 175 VAL 175 177 177 VAL VAL B . n 
F 2 176 SER 176 178 178 SER SER B . n 
F 2 177 ASP 177 179 179 ASP ASP B . n 
F 2 178 THR 178 180 180 THR THR B . n 
F 2 179 VAL 179 181 181 VAL VAL B . n 
F 2 180 VAL 180 182 182 VAL VAL B . n 
F 2 181 GLU 181 183 183 GLU GLU B . n 
F 2 182 PRO 182 184 184 PRO PRO B . n 
F 2 183 TYR 183 185 185 TYR TYR B . n 
F 2 184 ASN 184 186 186 ASN ASN B . n 
F 2 185 ALA 185 187 187 ALA ALA B . n 
F 2 186 THR 186 188 188 THR THR B . n 
F 2 187 LEU 187 189 189 LEU LEU B . n 
F 2 188 SER 188 190 190 SER SER B . n 
F 2 189 VAL 189 191 191 VAL VAL B . n 
F 2 190 HIS 190 192 192 HIS HIS B . n 
F 2 191 GLN 191 193 193 GLN GLN B . n 
F 2 192 LEU 192 194 194 LEU LEU B . n 
F 2 193 VAL 193 195 195 VAL VAL B . n 
F 2 194 GLU 194 196 196 GLU GLU B . n 
F 2 195 ASN 195 197 197 ASN ASN B . n 
F 2 196 THR 196 198 198 THR THR B . n 
F 2 197 ASP 197 199 199 ASP ASP B . n 
F 2 198 GLU 198 200 200 GLU GLU B . n 
F 2 199 THR 199 201 201 THR THR B . n 
F 2 200 TYR 200 202 202 TYR TYR B . n 
F 2 201 CYS 201 203 203 CYS CYS B . n 
F 2 202 ILE 202 204 204 ILE ILE B . n 
F 2 203 ASP 203 205 205 ASP ASP B . n 
F 2 204 ASN 204 206 206 ASN ASN B . n 
F 2 205 GLU 205 207 207 GLU GLU B . n 
F 2 206 ALA 206 208 208 ALA ALA B . n 
F 2 207 LEU 207 209 209 LEU LEU B . n 
F 2 208 TYR 208 210 210 TYR TYR B . n 
F 2 209 ASP 209 211 211 ASP ASP B . n 
F 2 210 ILE 210 212 212 ILE ILE B . n 
F 2 211 CYS 211 213 213 CYS CYS B . n 
F 2 212 PHE 212 214 214 PHE PHE B . n 
F 2 213 ARG 213 215 215 ARG ARG B . n 
F 2 214 THR 214 216 216 THR THR B . n 
F 2 215 LEU 215 217 217 LEU LEU B . n 
F 2 216 LYS 216 218 218 LYS LYS B . n 
F 2 217 LEU 217 219 219 LEU LEU B . n 
F 2 218 THR 218 220 220 THR THR B . n 
F 2 219 THR 219 221 221 THR THR B . n 
F 2 220 PRO 220 222 222 PRO PRO B . n 
F 2 221 THR 221 223 223 THR THR B . n 
F 2 222 TYR 222 224 224 TYR TYR B . n 
F 2 223 GLY 223 225 225 GLY GLY B . n 
F 2 224 ASP 224 226 226 ASP ASP B . n 
F 2 225 LEU 225 227 227 LEU LEU B . n 
F 2 226 ASN 226 228 228 ASN ASN B . n 
F 2 227 HIS 227 229 229 HIS HIS B . n 
F 2 228 LEU 228 230 230 LEU LEU B . n 
F 2 229 VAL 229 231 231 VAL VAL B . n 
F 2 230 SER 230 232 232 SER SER B . n 
F 2 231 ALA 231 233 233 ALA ALA B . n 
F 2 232 THR 232 234 234 THR THR B . n 
F 2 233 MET 233 235 235 MET MET B . n 
F 2 234 SER 234 236 236 SER SER B . n 
F 2 235 GLY 235 237 237 GLY GLY B . n 
F 2 236 VAL 236 238 238 VAL VAL B . n 
F 2 237 THR 237 239 239 THR THR B . n 
F 2 238 THR 238 240 240 THR THR B . n 
F 2 239 CYS 239 241 241 CYS CYS B . n 
F 2 240 LEU 240 242 242 LEU LEU B . n 
F 2 241 ARG 241 243 243 ARG ARG B . n 
F 2 242 PHE 242 244 244 PHE PHE B . n 
F 2 243 PRO 243 245 245 PRO PRO B . n 
F 2 244 GLY 244 246 246 GLY GLY B . n 
F 2 245 GLN 245 247 247 GLN GLN B . n 
F 2 246 LEU 246 248 248 LEU LEU B . n 
F 2 247 ASN 247 249 249 ASN ASN B . n 
F 2 248 ALA 248 250 250 ALA ALA B . n 
F 2 249 ASP 249 251 251 ASP ASP B . n 
F 2 250 LEU 250 252 252 LEU LEU B . n 
F 2 251 ARG 251 253 253 ARG ARG B . n 
F 2 252 LYS 252 254 254 LYS LYS B . n 
F 2 253 LEU 253 255 255 LEU LEU B . n 
F 2 254 ALA 254 256 256 ALA ALA B . n 
F 2 255 VAL 255 257 257 VAL VAL B . n 
F 2 256 ASN 256 258 258 ASN ASN B . n 
F 2 257 MET 257 259 259 MET MET B . n 
F 2 258 VAL 258 260 260 VAL VAL B . n 
F 2 259 PRO 259 261 261 PRO PRO B . n 
F 2 260 PHE 260 262 262 PHE PHE B . n 
F 2 261 PRO 261 263 263 PRO PRO B . n 
F 2 262 ARG 262 264 264 ARG ARG B . n 
F 2 263 LEU 263 265 265 LEU LEU B . n 
F 2 264 HIS 264 266 266 HIS HIS B . n 
F 2 265 PHE 265 267 267 PHE PHE B . n 
F 2 266 PHE 266 268 268 PHE PHE B . n 
F 2 267 MET 267 269 269 MET MET B . n 
F 2 268 PRO 268 270 270 PRO PRO B . n 
F 2 269 GLY 269 271 271 GLY GLY B . n 
F 2 270 PHE 270 272 272 PHE PHE B . n 
F 2 271 ALA 271 273 273 ALA ALA B . n 
F 2 272 PRO 272 274 274 PRO PRO B . n 
F 2 273 LEU 273 275 275 LEU LEU B . n 
F 2 274 THR 274 276 276 THR THR B . n 
F 2 275 SER 275 277 277 SER SER B . n 
F 2 276 ARG 276 278 278 ARG ARG B . n 
F 2 277 GLY 277 279 279 GLY GLY B . n 
F 2 278 SER 278 280 280 SER SER B . n 
F 2 279 GLN 279 281 281 GLN GLN B . n 
F 2 280 GLN 280 282 282 GLN GLN B . n 
F 2 281 TYR 281 283 283 TYR TYR B . n 
F 2 282 ARG 282 284 284 ARG ARG B . n 
F 2 283 ALA 283 285 285 ALA ALA B . n 
F 2 284 LEU 284 286 286 LEU LEU B . n 
F 2 285 THR 285 287 287 THR THR B . n 
F 2 286 VAL 286 288 288 VAL VAL B . n 
F 2 287 PRO 287 289 289 PRO PRO B . n 
F 2 288 GLU 288 290 290 GLU GLU B . n 
F 2 289 LEU 289 291 291 LEU LEU B . n 
F 2 290 THR 290 292 292 THR THR B . n 
F 2 291 GLN 291 293 293 GLN GLN B . n 
F 2 292 GLN 292 294 294 GLN GLN B . n 
F 2 293 MET 293 295 295 MET MET B . n 
F 2 294 PHE 294 296 296 PHE PHE B . n 
F 2 295 ASP 295 297 297 ASP ASP B . n 
F 2 296 SER 296 298 298 SER SER B . n 
F 2 297 LYS 297 299 299 LYS LYS B . n 
F 2 298 ASN 298 300 300 ASN ASN B . n 
F 2 299 MET 299 301 301 MET MET B . n 
F 2 300 MET 300 302 302 MET MET B . n 
F 2 301 ALA 301 303 303 ALA ALA B . n 
F 2 302 ALA 302 304 304 ALA ALA B . n 
F 2 303 CYS 303 305 305 CYS CYS B . n 
F 2 304 ASP 304 306 306 ASP ASP B . n 
F 2 305 PRO 305 307 307 PRO PRO B . n 
F 2 306 ARG 306 308 308 ARG ARG B . n 
F 2 307 HIS 307 309 309 HIS HIS B . n 
F 2 308 GLY 308 310 310 GLY GLY B . n 
F 2 309 ARG 309 311 311 ARG ARG B . n 
F 2 310 TYR 310 312 312 TYR TYR B . n 
F 2 311 LEU 311 313 313 LEU LEU B . n 
F 2 312 THR 312 314 314 THR THR B . n 
F 2 313 VAL 313 315 315 VAL VAL B . n 
F 2 314 ALA 314 316 316 ALA ALA B . n 
F 2 315 ALA 315 317 317 ALA ALA B . n 
F 2 316 ILE 316 318 318 ILE ILE B . n 
F 2 317 PHE 317 319 319 PHE PHE B . n 
F 2 318 ARG 318 320 320 ARG ARG B . n 
F 2 319 GLY 319 321 321 GLY GLY B . n 
F 2 320 ARG 320 322 322 ARG ARG B . n 
F 2 321 MET 321 323 323 MET MET B . n 
F 2 322 SER 322 324 324 SER SER B . n 
F 2 323 MET 323 325 325 MET MET B . n 
F 2 324 LYS 324 326 326 LYS LYS B . n 
F 2 325 GLU 325 327 327 GLU GLU B . n 
F 2 326 VAL 326 328 328 VAL VAL B . n 
F 2 327 ASP 327 329 329 ASP ASP B . n 
F 2 328 GLU 328 330 330 GLU GLU B . n 
F 2 329 GLN 329 331 331 GLN GLN B . n 
F 2 330 MET 330 332 332 MET MET B . n 
F 2 331 LEU 331 333 333 LEU LEU B . n 
F 2 332 ASN 332 334 334 ASN ASN B . n 
F 2 333 VAL 333 335 335 VAL VAL B . n 
F 2 334 GLN 334 336 336 GLN GLN B . n 
F 2 335 ASN 335 337 337 ASN ASN B . n 
F 2 336 LYS 336 338 338 LYS LYS B . n 
F 2 337 ASN 337 339 339 ASN ASN B . n 
F 2 338 SER 338 340 340 SER SER B . n 
F 2 339 SER 339 341 341 SER SER B . n 
F 2 340 TYR 340 342 342 TYR TYR B . n 
F 2 341 PHE 341 343 343 PHE PHE B . n 
F 2 342 VAL 342 344 344 VAL VAL B . n 
F 2 343 GLU 343 345 345 GLU GLU B . n 
F 2 344 TRP 344 346 346 TRP TRP B . n 
F 2 345 ILE 345 347 347 ILE ILE B . n 
F 2 346 PRO 346 348 348 PRO PRO B . n 
F 2 347 ASN 347 349 349 ASN ASN B . n 
F 2 348 ASN 348 350 350 ASN ASN B . n 
F 2 349 VAL 349 351 351 VAL VAL B . n 
F 2 350 LYS 350 352 352 LYS LYS B . n 
F 2 351 THR 351 353 353 THR THR B . n 
F 2 352 ALA 352 354 354 ALA ALA B . n 
F 2 353 VAL 353 355 355 VAL VAL B . n 
F 2 354 CYS 354 356 356 CYS CYS B . n 
F 2 355 ASP 355 357 357 ASP ASP B . n 
F 2 356 ILE 356 358 358 ILE ILE B . n 
F 2 357 PRO 357 359 359 PRO PRO B . n 
F 2 358 PRO 358 360 360 PRO PRO B . n 
F 2 359 ARG 359 369 369 ARG ARG B . n 
F 2 360 GLY 360 370 370 GLY GLY B . n 
F 2 361 LEU 361 371 371 LEU LEU B . n 
F 2 362 LYS 362 372 372 LYS LYS B . n 
F 2 363 MET 363 373 373 MET MET B . n 
F 2 364 SER 364 374 374 SER SER B . n 
F 2 365 ALA 365 375 375 ALA ALA B . n 
F 2 366 THR 366 376 376 THR THR B . n 
F 2 367 PHE 367 377 377 PHE PHE B . n 
F 2 368 ILE 368 378 378 ILE ILE B . n 
F 2 369 GLY 369 379 379 GLY GLY B . n 
F 2 370 ASN 370 380 380 ASN ASN B . n 
F 2 371 SER 371 381 381 SER SER B . n 
F 2 372 THR 372 382 382 THR THR B . n 
F 2 373 ALA 373 383 383 ALA ALA B . n 
F 2 374 ILE 374 384 384 ILE ILE B . n 
F 2 375 GLN 375 385 385 GLN GLN B . n 
F 2 376 GLU 376 386 386 GLU GLU B . n 
F 2 377 LEU 377 387 387 LEU LEU B . n 
F 2 378 PHE 378 388 388 PHE PHE B . n 
F 2 379 LYS 379 389 389 LYS LYS B . n 
F 2 380 ARG 380 390 390 ARG ARG B . n 
F 2 381 ILE 381 391 391 ILE ILE B . n 
F 2 382 SER 382 392 392 SER SER B . n 
F 2 383 GLU 383 393 393 GLU GLU B . n 
F 2 384 GLN 384 394 394 GLN GLN B . n 
F 2 385 PHE 385 395 395 PHE PHE B . n 
F 2 386 THR 386 396 396 THR THR B . n 
F 2 387 ALA 387 397 397 ALA ALA B . n 
F 2 388 MET 388 398 398 MET MET B . n 
F 2 389 PHE 389 399 399 PHE PHE B . n 
F 2 390 ARG 390 400 400 ARG ARG B . n 
F 2 391 ARG 391 401 401 ARG ARG B . n 
F 2 392 LYS 392 402 402 LYS LYS B . n 
F 2 393 ALA 393 403 403 ALA ALA B . n 
F 2 394 PHE 394 404 404 PHE PHE B . n 
F 2 395 LEU 395 405 405 LEU LEU B . n 
F 2 396 HIS 396 406 406 HIS HIS B . n 
F 2 397 TRP 397 407 407 TRP TRP B . n 
F 2 398 TYR 398 408 408 TYR TYR B . n 
F 2 399 THR 399 409 409 THR THR B . n 
F 2 400 GLY 400 410 410 GLY GLY B . n 
F 2 401 GLU 401 411 411 GLU GLU B . n 
F 2 402 GLY 402 412 412 GLY GLY B . n 
F 2 403 MET 403 413 413 MET MET B . n 
F 2 404 ASP 404 414 414 ASP ASP B . n 
F 2 405 GLU 405 415 415 GLU GLU B . n 
F 2 406 MET 406 416 416 MET MET B . n 
F 2 407 GLU 407 417 417 GLU GLU B . n 
F 2 408 PHE 408 418 418 PHE PHE B . n 
F 2 409 THR 409 419 419 THR THR B . n 
F 2 410 GLU 410 420 420 GLU GLU B . n 
F 2 411 ALA 411 421 421 ALA ALA B . n 
F 2 412 GLU 412 422 422 GLU GLU B . n 
F 2 413 SER 413 423 423 SER SER B . n 
F 2 414 ASN 414 424 424 ASN ASN B . n 
F 2 415 MET 415 425 425 MET MET B . n 
F 2 416 ASN 416 426 426 ASN ASN B . n 
F 2 417 ASP 417 427 427 ASP ASP B . n 
F 2 418 LEU 418 428 428 LEU LEU B . n 
F 2 419 VAL 419 429 429 VAL VAL B . n 
F 2 420 SER 420 430 430 SER SER B . n 
F 2 421 GLU 421 431 431 GLU GLU B . n 
F 2 422 TYR 422 432 432 TYR TYR B . n 
F 2 423 GLN 423 433 433 GLN GLN B . n 
F 2 424 GLN 424 434 434 GLN GLN B . n 
F 2 425 TYR 425 435 435 TYR TYR B . n 
F 2 426 GLN 426 436 436 GLN GLN B . n 
F 2 427 ASP 427 437 437 ASP ASP B . n 
F 2 428 ALA 428 438 438 ALA ALA B . n 
F 2 429 THR 429 439 ?   ?   ?   B . n 
F 2 430 ALA 430 440 ?   ?   ?   B . n 
F 2 431 ASP 431 441 ?   ?   ?   B . n 
F 2 432 GLU 432 442 ?   ?   ?   B . n 
F 2 433 GLN 433 443 ?   ?   ?   B . n 
F 2 434 GLY 434 444 ?   ?   ?   B . n 
F 2 435 GLU 435 445 ?   ?   ?   B . n 
F 2 436 PHE 436 446 ?   ?   ?   B . n 
F 2 437 GLU 437 447 ?   ?   ?   B . n 
F 2 438 GLU 438 448 ?   ?   ?   B . n 
F 2 439 GLU 439 449 ?   ?   ?   B . n 
F 2 440 GLU 440 450 ?   ?   ?   B . n 
F 2 441 GLY 441 451 ?   ?   ?   B . n 
F 2 442 GLU 442 452 ?   ?   ?   B . n 
F 2 443 ASP 443 453 ?   ?   ?   B . n 
F 2 444 GLU 444 454 ?   ?   ?   B . n 
F 2 445 ALA 445 455 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EPQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EPQ 
_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    1 502 503 CA    CA  A . 
I 5  GTP   1 501 502 GTP   GTP C . 
J 7  MG    1 502 503 MG    MG  C . 
K 6  CA    1 503 504 CA    CA  C . 
L 8  A1EPQ 1 504 502 A1EPQ LIG C . 
M 9  GDP   1 501 501 GDP   GDP D . 
N 7  MG    1 501 502 MG    MG  B . 
O 9  GDP   1 502 501 GDP   GDP B . 
P 10 HOH   1 601 1   HOH   HOH C . 
P 10 HOH   2 602 7   HOH   HOH C . 
P 10 HOH   3 603 3   HOH   HOH C . 
P 10 HOH   4 604 6   HOH   HOH C . 
P 10 HOH   5 605 5   HOH   HOH C . 
Q 10 HOH   1 601 2   HOH   HOH B . 
Q 10 HOH   2 602 4   HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 284 ? CG  ? A GLU 284 CG  
2  1 Y 1 A GLU 284 ? CD  ? A GLU 284 CD  
3  1 Y 1 A GLU 284 ? OE1 ? A GLU 284 OE1 
4  1 Y 1 A GLU 284 ? OE2 ? A GLU 284 OE2 
5  1 Y 0 C THR 194 ? CA  B B THR 194 CA  
6  1 Y 0 C THR 194 ? CB  B B THR 194 CB  
7  1 Y 0 C THR 194 ? OG1 B B THR 194 OG1 
8  1 Y 0 C THR 194 ? CG2 B B THR 194 CG2 
9  1 Y 0 C VAL 363 ? CA  B B VAL 363 CA  
10 1 Y 0 C VAL 363 ? CB  B B VAL 363 CB  
11 1 Y 0 C VAL 363 ? CG1 B B VAL 363 CG1 
12 1 Y 0 C VAL 363 ? CG2 B B VAL 363 CG2 
13 1 Y 0 D THR 240 ? CA  A C THR 238 CA  
14 1 Y 0 D THR 240 ? CB  A C THR 238 CB  
15 1 Y 0 D THR 240 ? OG1 A C THR 238 OG1 
16 1 Y 0 D THR 240 ? CG2 A C THR 238 CG2 
17 1 Y 0 D ILE 318 ? CD1 ? C ILE 316 CD1 
18 1 Y 0 D ASN 334 ? CG  ? C ASN 332 CG  
19 1 Y 1 D LYS 338 ? CG  ? C LYS 336 CG  
20 1 Y 1 D LYS 338 ? CD  ? C LYS 336 CD  
21 1 Y 1 D LYS 338 ? CE  ? C LYS 336 CE  
22 1 Y 1 D LYS 338 ? NZ  ? C LYS 336 NZ  
23 1 Y 0 F LEU 275 ? CA  B E LEU 275 CA  
24 1 Y 0 F LEU 275 ? CB  B E LEU 275 CB  
25 1 Y 0 F LEU 275 ? CG  B E LEU 275 CG  
26 1 Y 0 F LEU 275 ? CD1 B E LEU 275 CD1 
27 1 Y 0 F LEU 275 ? CD2 B E LEU 275 CD2 
28 1 Y 0 F LEU 284 ? CA  B E LEU 284 CA  
29 1 Y 0 F LEU 284 ? CB  B E LEU 284 CB  
30 1 Y 0 F LEU 284 ? CG  B E LEU 284 CG  
31 1 Y 0 F LEU 284 ? CD1 B E LEU 284 CD1 
32 1 Y 0 F LEU 284 ? CD2 B E LEU 284 CD2 
33 1 Y 0 B THR 168 ? CA  B F THR 166 CA  
34 1 Y 0 B THR 168 ? CB  B F THR 166 CB  
35 1 Y 0 B THR 168 ? OG1 B F THR 166 OG1 
36 1 Y 0 B THR 168 ? CG2 B F THR 166 CG2 
37 1 Y 1 B SER 277 ? OG  ? F SER 275 OG  
38 1 Y 1 B SER 280 ? OG  ? F SER 278 OG  
39 1 Y 1 B GLN 281 ? CG  ? F GLN 279 CG  
40 1 Y 1 B GLN 281 ? CD  ? F GLN 279 CD  
41 1 Y 1 B GLN 281 ? OE1 ? F GLN 279 OE1 
42 1 Y 1 B GLN 281 ? NE2 ? F GLN 279 NE2 
43 1 Y 0 B ILE 318 ? CD1 ? F ILE 316 CD1 
44 1 Y 0 B ASN 334 ? CG  ? F ASN 332 CG  
# 
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 ? ? ? '(1.21_5207: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? 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                     9LNL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     105.300 
_cell.length_a_esd                 ? 
_cell.length_b                     156.420 
_cell.length_b_esd                 ? 
_cell.length_c                     184.860 
_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                         9LNL 
_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                   9LNL 
_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             2.91 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.78 
_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, 5% glycerol, 0.1 M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7' 
_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         2024-12-10 
_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   0.97861 
_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        0.97861 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LNL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.85 
_reflns.d_resolution_low                               53.19 
_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                                     71704 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_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                                   0.982 
_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                                    2.85 
_reflns_shell.d_res_low                                     2.90 
_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                             3531 
_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                                  0.497 
_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                                 9LNL 
_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                            2.85 
_refine.ls_d_res_low                             53.18 
_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                     71641 
_refine.ls_number_reflns_R_free                  3499 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.57 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2014 
_refine.ls_R_factor_R_free                       0.2774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1976 
_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                 26.59 
_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                            0.42 
_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        17256 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         187 
_refine_hist.number_atoms_solvent             7 
_refine_hist.number_atoms_total               17450 
_refine_hist.d_res_high                       2.85 
_refine_hist.d_res_low                        53.18 
# 
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' ? 18.269 ? 6654 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 2681 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 3161 ? 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' 2.85 2.89 . . 136 2695 100.00 . . . . 0.2595 . . . . . . . . . . . 0.3135 
'X-RAY DIFFRACTION' 2.89 2.93 . . 123 2703 100.00 . . . . 0.2667 . . . . . . . . . . . 0.3831 
'X-RAY DIFFRACTION' 2.93 2.97 . . 131 2710 100.00 . . . . 0.2628 . . . . . . . . . . . 0.3259 
'X-RAY DIFFRACTION' 2.97 3.02 . . 140 2714 100.00 . . . . 0.2586 . . . . . . . . . . . 0.3652 
'X-RAY DIFFRACTION' 3.02 3.07 . . 151 2675 100.00 . . . . 0.2374 . . . . . . . . . . . 0.3181 
'X-RAY DIFFRACTION' 3.07 3.12 . . 130 2703 100.00 . . . . 0.2355 . . . . . . . . . . . 0.3466 
'X-RAY DIFFRACTION' 3.12 3.18 . . 161 2720 100.00 . . . . 0.2271 . . . . . . . . . . . 0.3178 
'X-RAY DIFFRACTION' 3.18 3.24 . . 131 2695 100.00 . . . . 0.2214 . . . . . . . . . . . 0.3079 
'X-RAY DIFFRACTION' 3.24 3.31 . . 145 2706 100.00 . . . . 0.2261 . . . . . . . . . . . 0.2939 
'X-RAY DIFFRACTION' 3.31 3.38 . . 150 2691 100.00 . . . . 0.2341 . . . . . . . . . . . 0.3221 
'X-RAY DIFFRACTION' 3.38 3.46 . . 158 2689 100.00 . . . . 0.2169 . . . . . . . . . . . 0.3150 
'X-RAY DIFFRACTION' 3.46 3.54 . . 127 2737 100.00 . . . . 0.2038 . . . . . . . . . . . 0.2860 
'X-RAY DIFFRACTION' 3.54 3.64 . . 146 2683 99.00  . . . . 0.2044 . . . . . . . . . . . 0.2961 
'X-RAY DIFFRACTION' 3.64 3.75 . . 140 2707 100.00 . . . . 0.1885 . . . . . . . . . . . 0.2606 
'X-RAY DIFFRACTION' 3.75 3.87 . . 145 2731 100.00 . . . . 0.1793 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 3.87 4.01 . . 128 2747 100.00 . . . . 0.1682 . . . . . . . . . . . 0.2298 
'X-RAY DIFFRACTION' 4.01 4.17 . . 136 2705 100.00 . . . . 0.1785 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 4.17 4.36 . . 123 2762 100.00 . . . . 0.1697 . . . . . . . . . . . 0.2681 
'X-RAY DIFFRACTION' 4.36 4.59 . . 142 2761 100.00 . . . . 0.1606 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 4.59 4.87 . . 142 2738 100.00 . . . . 0.1605 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 4.87 5.25 . . 152 2737 99.00  . . . . 0.1710 . . . . . . . . . . . 0.2550 
'X-RAY DIFFRACTION' 5.25 5.78 . . 125 2736 99.00  . . . . 0.1903 . . . . . . . . . . . 0.2591 
'X-RAY DIFFRACTION' 5.78 6.61 . . 142 2783 100.00 . . . . 0.2086 . . . . . . . . . . . 0.2856 
'X-RAY DIFFRACTION' 6.61 8.32 . . 151 2798 100.00 . . . . 0.1915 . . . . . . . . . . . 0.2360 
# 
_struct.entry_id                     9LNL 
_struct.title                        'Crystal structure of T2R-TTL-YQVB15 complex' 
_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        9LNL 
_struct_keywords.text            'Tubulin inhibitor, 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 1  ? 
C N N 2  ? 
D N N 3  ? 
E N N 4  ? 
F N N 2  ? 
G N N 5  ? 
H N N 6  ? 
I N N 5  ? 
J N N 7  ? 
K N N 6  ? 
L N N 8  ? 
M N N 9  ? 
N N N 7  ? 
O N N 9  ? 
P N N 10 ? 
Q N N 10 ? 
# 
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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEE
;
1  
2 UNP TBB2B_BOVIN      Q6B856     ? 2 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
1  
3 UNP STMN4_RAT        P63043     ? 3 
;DMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKYQEAELLKHLAEKREHEREVIQ
KAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKEEASR
;
49 
4 UNP A0A8V0Z8P0_CHICK A0A8V0Z8P0 ? 4 
;MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLMLGERNRLPFGRLAEMQQQLLEGDQTLVLASSTHPESVDSD
KNHGFGHEPGLVQLVNYYRGADKLCRKASLVKLIKTSPELSESCTWFPESYVIYPTNLKTPVAPAQNGIRHLINNTRTDE
REVFLAAYNRRREGREGNVWIAKSSAGAKGEGILISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPGHRKFDIRSWVLV
DHLYNIYLYREGVLRTSSEPYNSANFQDKTCHLTNHCIQKEYSKNYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQI
KHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLADTGQK
TSQPTSIFIKL
;
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 9LNL A 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
2 1 9LNL C 1 ? 450 ? Q2XVP4     1  ? 450 ? 1 450 
3 2 9LNL D 1 ? 445 ? Q6B856     1  ? 445 ? 1 455 
4 3 9LNL E 3 ? 143 ? P63043     49 ? 189 ? 5 145 
5 4 9LNL F 1 ? 378 ? A0A8V0Z8P0 1  ? 411 ? 1 378 
6 2 9LNL B 1 ? 445 ? Q6B856     1  ? 445 ? 1 455 
# 
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 
4 9LNL MET E 1   ? UNP P63043     ?   ?  'initiating methionine' 3   1  
4 9LNL ALA E 2   ? UNP P63043     ?   ?  'expression tag'        4   2  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ALA 53 deletion                ?   3  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLU 54 deletion                ?   4  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 MET 55 deletion                ?   5  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLN 56 deletion                ?   6  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLN 57 deletion                ?   7  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLN 58 deletion                ?   8  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 LEU 59 deletion                ?   9  
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 LEU 60 deletion                ?   10 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLU 61 deletion                ?   11 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLY 62 deletion                ?   12 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ASP 63 deletion                ?   13 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLN 64 deletion                ?   14 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 THR 65 deletion                ?   15 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 LEU 66 deletion                ?   16 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 VAL 67 deletion                ?   17 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 LEU 68 deletion                ?   18 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ALA 69 deletion                ?   19 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 SER 70 deletion                ?   20 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 SER 71 deletion                ?   21 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 THR 72 deletion                ?   22 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 HIS 73 deletion                ?   23 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 PRO 74 deletion                ?   24 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLU 75 deletion                ?   25 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 SER 76 deletion                ?   26 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 VAL 77 deletion                ?   27 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ASP 78 deletion                ?   28 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 SER 79 deletion                ?   29 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ASP 80 deletion                ?   30 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 LYS 81 deletion                ?   31 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 ASN 82 deletion                ?   32 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 HIS 83 deletion                ?   33 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 GLY 84 deletion                ?   34 
5 9LNL ?   F ?   ? UNP A0A8V0Z8P0 PHE 85 deletion                ?   35 
5 9LNL HIS F 379 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        379 36 
5 9LNL HIS F 380 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        380 37 
5 9LNL HIS F 381 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        381 38 
5 9LNL HIS F 382 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        382 39 
5 9LNL HIS F 383 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        383 40 
5 9LNL HIS F 384 ? UNP A0A8V0Z8P0 ?   ?  'expression tag'        384 41 
# 
_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 
# 
_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  ? HIS A 28  ? GLY A 10  HIS A 28  1 ? 19 
HELX_P HELX_P2   AA2 ASP A 47  ? THR A 51  ? ASP A 47  THR A 51  5 ? 5  
HELX_P HELX_P3   AA3 PRO A 72  ? ARG A 79  ? PRO A 72  ARG A 79  1 ? 8  
HELX_P HELX_P4   AA4 GLY A 81  ? LEU A 86  ? GLY A 81  LEU A 86  5 ? 6  
HELX_P HELX_P5   AA5 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P6   AA6 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P7   AA7 GLY A 111 ? GLU A 113 ? GLY A 111 GLU A 113 5 ? 3  
HELX_P HELX_P8   AA8 ILE A 114 ? GLN A 128 ? ILE A 114 GLN A 128 1 ? 15 
HELX_P HELX_P9   AA9 GLY A 143 ? TYR A 161 ? GLY A 143 TYR A 161 1 ? 19 
HELX_P HELX_P10  AB1 VAL A 182 ? LEU A 195 ? VAL A 182 LEU A 195 1 ? 14 
HELX_P HELX_P11  AB2 GLU A 196 ? SER A 198 ? GLU A 196 SER A 198 5 ? 3  
HELX_P HELX_P12  AB3 ASN A 206 ? ASP A 218 ? ASN A 206 ASP A 218 1 ? 13 
HELX_P HELX_P13  AB4 THR A 223 ? SER A 241 ? THR A 223 SER A 241 1 ? 19 
HELX_P HELX_P14  AB5 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P15  AB6 SER A 287 ? CYS A 295 ? SER A 287 CYS A 295 1 ? 9  
HELX_P HELX_P16  AB7 PHE A 296 ? GLN A 301 ? PHE A 296 GLN A 301 5 ? 6  
HELX_P HELX_P17  AB8 VAL A 324 ? ARG A 339 ? VAL A 324 ARG A 339 1 ? 16 
HELX_P HELX_P18  AB9 THR A 381 ? ALA A 383 ? THR A 381 ALA A 383 5 ? 3  
HELX_P HELX_P19  AC1 ILE A 384 ? ALA A 400 ? ILE A 384 ALA A 400 1 ? 17 
HELX_P HELX_P20  AC2 PHE A 404 ? GLY A 410 ? PHE A 404 GLY A 410 1 ? 7  
HELX_P HELX_P21  AC3 GLU A 414 ? GLY A 436 ? GLU A 414 GLY A 436 1 ? 23 
HELX_P HELX_P22  AC4 GLY B 10  ? GLY B 29  ? GLY C 10  GLY C 29  1 ? 20 
HELX_P HELX_P23  AC5 ASP B 47  ? THR B 51  ? ASP C 47  THR C 51  5 ? 5  
HELX_P HELX_P24  AC6 PRO B 72  ? GLY B 81  ? PRO C 72  GLY C 81  1 ? 10 
HELX_P HELX_P25  AC7 TYR B 83  ? PHE B 87  ? TYR C 83  PHE C 87  5 ? 5  
HELX_P HELX_P26  AC8 HIS B 88  ? GLU B 90  ? HIS C 88  GLU C 90  5 ? 3  
HELX_P HELX_P27  AC9 ASN B 102 ? TYR B 108 ? ASN C 102 TYR C 108 1 ? 7  
HELX_P HELX_P28  AD1 ILE B 110 ? GLU B 113 ? ILE C 110 GLU C 113 5 ? 4  
HELX_P HELX_P29  AD2 ILE B 114 ? ASP B 127 ? ILE C 114 ASP C 127 1 ? 14 
HELX_P HELX_P30  AD3 GLY B 143 ? GLY B 162 ? GLY C 143 GLY C 162 1 ? 20 
HELX_P HELX_P31  AD4 ALA B 174 ? SER B 178 ? ALA C 174 SER C 178 5 ? 5  
HELX_P HELX_P32  AD5 VAL B 182 ? LEU B 195 ? VAL C 182 LEU C 195 1 ? 14 
HELX_P HELX_P33  AD6 GLU B 196 ? SER B 198 ? GLU C 196 SER C 198 5 ? 3  
HELX_P HELX_P34  AD7 ASN B 206 ? ASP B 218 ? ASN C 206 ASP C 218 1 ? 13 
HELX_P HELX_P35  AD8 THR B 223 ? PHE B 244 ? THR C 223 PHE C 244 1 ? 22 
HELX_P HELX_P36  AD9 ASP B 251 ? VAL B 260 ? ASP C 251 VAL C 260 1 ? 10 
HELX_P HELX_P37  AE1 SER B 277 ? TYR B 282 ? SER C 277 TYR C 282 1 ? 6  
HELX_P HELX_P38  AE2 SER B 287 ? CYS B 295 ? SER C 287 CYS C 295 1 ? 9  
HELX_P HELX_P39  AE3 PHE B 296 ? GLN B 301 ? PHE C 296 GLN C 301 5 ? 6  
HELX_P HELX_P40  AE4 ASP B 306 ? GLY B 310 ? ASP C 306 GLY C 310 5 ? 5  
HELX_P HELX_P41  AE5 VAL B 324 ? ARG B 339 ? VAL C 324 ARG C 339 1 ? 16 
HELX_P HELX_P42  AE6 ILE B 384 ? LYS B 401 ? ILE C 384 LYS C 401 1 ? 18 
HELX_P HELX_P43  AE7 PHE B 404 ? GLY B 410 ? PHE C 404 GLY C 410 1 ? 7  
HELX_P HELX_P44  AE8 GLU B 414 ? VAL B 435 ? GLU C 414 VAL C 435 1 ? 22 
HELX_P HELX_P45  AE9 GLY C 10  ? GLY C 29  ? GLY D 10  GLY D 29  1 ? 20 
HELX_P HELX_P46  AF1 ARG C 46  ? VAL C 49  ? ARG D 48  VAL D 51  5 ? 4  
HELX_P HELX_P47  AF2 GLU C 69  ? GLY C 79  ? GLU D 71  GLY D 81  1 ? 11 
HELX_P HELX_P48  AF3 ARG C 86  ? ASP C 88  ? ARG D 88  ASP D 90  5 ? 3  
HELX_P HELX_P49  AF4 ASN C 100 ? TYR C 106 ? ASN D 102 TYR D 108 1 ? 7  
HELX_P HELX_P50  AF5 THR C 107 ? GLU C 125 ? THR D 109 GLU D 127 1 ? 19 
HELX_P HELX_P51  AF6 GLY C 142 ? TYR C 159 ? GLY D 144 TYR D 161 1 ? 18 
HELX_P HELX_P52  AF7 VAL C 180 ? THR C 196 ? VAL D 182 THR D 198 1 ? 17 
HELX_P HELX_P53  AF8 ASN C 204 ? ARG C 213 ? ASN D 206 ARG D 215 1 ? 10 
HELX_P HELX_P54  AF9 THR C 221 ? THR C 237 ? THR D 223 THR D 239 1 ? 17 
HELX_P HELX_P55  AG1 THR C 237 ? PHE C 242 ? THR D 239 PHE D 244 1 ? 6  
HELX_P HELX_P56  AG2 ASP C 249 ? VAL C 258 ? ASP D 251 VAL D 260 1 ? 10 
HELX_P HELX_P57  AG3 THR C 285 ? PHE C 294 ? THR D 287 PHE D 296 1 ? 10 
HELX_P HELX_P58  AG4 ASP C 295 ? MET C 299 ? ASP D 297 MET D 301 5 ? 5  
HELX_P HELX_P59  AG5 ASP C 304 ? GLY C 308 ? ASP D 306 GLY D 310 5 ? 5  
HELX_P HELX_P60  AG6 SER C 322 ? ASN C 337 ? SER D 324 ASN D 339 1 ? 16 
HELX_P HELX_P61  AG7 SER C 338 ? PHE C 341 ? SER D 340 PHE D 343 5 ? 4  
HELX_P HELX_P62  AG8 ILE C 374 ? ARG C 390 ? ILE D 384 ARG D 400 1 ? 17 
HELX_P HELX_P63  AG9 PHE C 394 ? GLU C 401 ? PHE D 404 GLU D 411 1 ? 8  
HELX_P HELX_P64  AH1 GLU C 405 ? ASP C 427 ? GLU D 415 ASP D 437 1 ? 23 
HELX_P HELX_P65  AH2 SER D 44  ? GLU D 136 ? SER E 46  GLU E 138 1 ? 93 
HELX_P HELX_P66  AH3 SER E 11  ? ALA E 23  ? SER F 11  ALA F 23  1 ? 13 
HELX_P HELX_P67  AH4 PRO E 48  ? LEU E 52  ? PRO F 48  LEU F 52  5 ? 5  
HELX_P HELX_P68  AH5 ALA E 68  ? ARG E 73  ? ALA F 68  ARG F 73  1 ? 6  
HELX_P HELX_P69  AH6 ARG E 73  ? SER E 84  ? ARG F 73  SER F 84  1 ? 12 
HELX_P HELX_P70  AH7 GLU E 127 ? TYR E 135 ? GLU F 127 TYR F 135 1 ? 9  
HELX_P HELX_P71  AH8 LEU E 169 ? GLY E 177 ? LEU F 169 GLY F 177 1 ? 9  
HELX_P HELX_P72  AH9 ASN E 242 ? GLU E 248 ? ASN F 242 GLU F 248 1 ? 7  
HELX_P HELX_P73  AI1 GLU E 257 ? GLY E 259 ? GLU F 257 GLY F 259 5 ? 3  
HELX_P HELX_P74  AI2 PHE E 264 ? ALA E 274 ? PHE F 264 ALA F 274 1 ? 11 
HELX_P HELX_P75  AI3 THR E 278 ? ILE E 283 ? THR F 278 ILE F 283 1 ? 6  
HELX_P HELX_P76  AI4 ILE E 283 ? ILE E 298 ? ILE F 283 ILE F 298 1 ? 16 
HELX_P HELX_P77  AI5 ILE E 298 ? SER E 303 ? ILE F 298 SER F 303 1 ? 6  
HELX_P HELX_P78  AI6 ALA E 339 ? LYS E 341 ? ALA F 339 LYS F 341 5 ? 3  
HELX_P HELX_P79  AI7 LEU E 342 ? ALA E 354 ? LEU F 342 ALA F 354 1 ? 13 
HELX_P HELX_P80  AI8 GLY F 10  ? HIS F 28  ? GLY B 10  HIS B 28  1 ? 19 
HELX_P HELX_P81  AI9 SER F 40  ? ARG F 46  ? SER B 40  ARG B 48  1 ? 7  
HELX_P HELX_P82  AJ1 ILE F 47  ? VAL F 49  ? ILE B 49  VAL B 51  5 ? 3  
HELX_P HELX_P83  AJ2 GLU F 69  ? SER F 78  ? GLU B 71  SER B 80  1 ? 10 
HELX_P HELX_P84  AJ3 ARG F 86  ? ASP F 88  ? ARG B 88  ASP B 90  5 ? 3  
HELX_P HELX_P85  AJ4 ASN F 100 ? TYR F 106 ? ASN B 102 TYR B 108 1 ? 7  
HELX_P HELX_P86  AJ5 THR F 107 ? SER F 126 ? THR B 109 SER B 128 1 ? 20 
HELX_P HELX_P87  AJ6 GLY F 142 ? TYR F 159 ? GLY B 144 TYR B 161 1 ? 18 
HELX_P HELX_P88  AJ7 VAL F 180 ? THR F 196 ? VAL B 182 THR B 198 1 ? 17 
HELX_P HELX_P89  AJ8 ASN F 204 ? ARG F 213 ? ASN B 206 ARG B 215 1 ? 10 
HELX_P HELX_P90  AJ9 THR F 221 ? THR F 237 ? THR B 223 THR B 239 1 ? 17 
HELX_P HELX_P91  AK1 THR F 237 ? PHE F 242 ? THR B 239 PHE B 244 1 ? 6  
HELX_P HELX_P92  AK2 ASP F 249 ? VAL F 258 ? ASP B 251 VAL B 260 1 ? 10 
HELX_P HELX_P93  AK3 THR F 285 ? PHE F 294 ? THR B 287 PHE B 296 1 ? 10 
HELX_P HELX_P94  AK4 ASP F 295 ? MET F 299 ? ASP B 297 MET B 301 5 ? 5  
HELX_P HELX_P95  AK5 ASP F 304 ? GLY F 308 ? ASP B 306 GLY B 310 5 ? 5  
HELX_P HELX_P96  AK6 SER F 322 ? ASN F 337 ? SER B 324 ASN B 339 1 ? 16 
HELX_P HELX_P97  AK7 SER F 338 ? PHE F 341 ? SER B 340 PHE B 343 5 ? 4  
HELX_P HELX_P98  AK8 ILE F 374 ? ARG F 390 ? ILE B 384 ARG B 400 1 ? 17 
HELX_P HELX_P99  AK9 LEU F 395 ? GLY F 400 ? LEU B 405 GLY B 410 1 ? 6  
HELX_P HELX_P100 AL1 ASP F 404 ? TYR F 425 ? ASP B 414 TYR B 435 1 ? 22 
# 
_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 ? ? G GTP .   O1G ? ? ? 1_555 N MG . MG ? ? A GTP 501 B MG 501 1_555 ? ? ? ? ? ? ? 2.938 ? ? 
metalc2 metalc ? ? G GTP .   O3G ? ? ? 1_555 N MG . MG ? ? A GTP 501 B MG 501 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc3 metalc ? ? G GTP .   O1B ? ? ? 1_555 N MG . MG ? ? A GTP 501 B MG 501 1_555 ? ? ? ? ? ? ? 2.581 ? ? 
metalc4 metalc ? ? B ASP 47  OD1 ? ? ? 1_555 K CA . CA ? ? C ASP 47  C CA 503 1_555 ? ? ? ? ? ? ? 3.028 ? ? 
metalc5 metalc ? ? B ASP 98  OD1 ? ? ? 1_555 J MG . MG ? ? C ASP 98  C MG 502 1_555 ? ? ? ? ? ? ? 2.902 ? ? 
metalc6 metalc ? ? B ALA 99  N   ? ? ? 1_555 J MG . MG ? ? C ALA 99  C MG 502 1_555 ? ? ? ? ? ? ? 2.731 ? ? 
metalc7 metalc ? ? F LYS 252 NZ  ? ? ? 1_555 N MG . MG ? ? B LYS 254 B MG 501 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
# 
_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 O1G ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 O3G ? G GTP .   ? A GTP 501 ? 1_555 55.7  ? 
2 O1G ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 O1B ? G GTP .   ? A GTP 501 ? 1_555 84.1  ? 
3 O3G ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 O1B ? G GTP .   ? A GTP 501 ? 1_555 76.5  ? 
4 O1G ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 NZ  ? F LYS 252 ? B LYS 254 ? 1_555 132.5 ? 
5 O3G ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 NZ  ? F LYS 252 ? B LYS 254 ? 1_555 100.1 ? 
6 O1B ? G GTP .  ? A GTP 501 ? 1_555 MG ? N MG . ? B MG 501 ? 1_555 NZ  ? F LYS 252 ? B LYS 254 ? 1_555 133.7 ? 
7 OD1 ? B ASP 98 ? C ASP 98  ? 1_555 MG ? J MG . ? C MG 502 ? 1_555 N   ? B ALA 99  ? C ALA 99  ? 1_555 56.3  ? 
# 
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 1.42  
2 ALA 273 B . ? ALA 273 C PRO 274 B ? PRO 274 C 1 -5.36 
3 ALA 271 C . ? ALA 273 D PRO 272 C ? PRO 274 D 1 4.98  
4 GLU 193 E . ? GLU 193 F PRO 194 E ? PRO 194 F 1 3.67  
5 ALA 271 F . ? ALA 273 B PRO 272 F ? PRO 274 B 1 -0.63 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 6  ? 
AA4 ? 6  ? 
AA5 ? 2  ? 
AA6 ? 4  ? 
AA7 ? 10 ? 
AA8 ? 2  ? 
AA9 ? 5  ? 
AB1 ? 4  ? 
AB2 ? 5  ? 
AB3 ? 5  ? 
AB4 ? 10 ? 
AB5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
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  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA5 1 2  ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? anti-parallel 
AA7 8 9  ? anti-parallel 
AA7 9 10 ? parallel      
AA8 1 2  ? anti-parallel 
AA9 1 2  ? parallel      
AA9 2 3  ? parallel      
AA9 3 4  ? parallel      
AA9 4 5  ? parallel      
AB1 1 2  ? anti-parallel 
AB1 2 3  ? anti-parallel 
AB1 3 4  ? anti-parallel 
AB2 1 2  ? anti-parallel 
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB4 1 2  ? parallel      
AB4 2 3  ? parallel      
AB4 3 4  ? parallel      
AB4 4 5  ? parallel      
AB4 5 6  ? parallel      
AB4 6 7  ? parallel      
AB4 7 8  ? anti-parallel 
AB4 8 9  ? anti-parallel 
AB4 9 10 ? parallel      
AB5 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  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 ? SER A 379 ? ARG A 373 SER A 379 
AA3 3  CYS A 316 ? GLY A 321 ? CYS A 316 GLY A 321 
AA3 4  THR A 349 ? ASN A 356 ? THR A 349 ASN A 356 
AA3 5  GLY D 15  ? LYS D 23  ? GLY E 17  LYS E 25  
AA3 6  VAL D 6   ? CYS D 12  ? VAL E 8   CYS E 14  
AA4 1  LEU B 92  ? THR B 94  ? LEU C 92  THR C 94  
AA4 2  ALA B 65  ? ASP B 69  ? ALA C 65  ASP C 69  
AA4 3  CYS B 4   ? VAL B 9   ? CYS C 4   VAL C 9   
AA4 4  GLY B 134 ? SER B 140 ? GLY C 134 SER C 140 
AA4 5  SER B 165 ? TYR B 172 ? SER C 165 TYR C 172 
AA4 6  CYS B 200 ? ASP B 205 ? CYS C 200 ASP C 205 
AA5 1  PHE B 53  ? GLU B 55  ? PHE C 53  GLU C 55  
AA5 2  HIS B 61  ? PRO B 63  ? HIS C 61  PRO C 63  
AA6 1  LEU B 269 ? ALA B 273 ? LEU C 269 ALA C 273 
AA6 2  ARG B 373 ? THR B 381 ? ARG C 373 THR C 381 
AA6 3  TYR B 312 ? GLY B 321 ? TYR C 312 GLY C 321 
AA6 4  PHE B 351 ? ASN B 356 ? PHE C 351 ASN C 356 
AA7 1  PHE C 90  ? PHE C 92  ? PHE D 92  PHE D 94  
AA7 2  ALA C 63  ? ASP C 67  ? ALA D 65  ASP D 69  
AA7 3  VAL C 5   ? ALA C 9   ? VAL D 5   ALA D 9   
AA7 4  GLY C 132 ? SER C 138 ? GLY D 134 SER D 140 
AA7 5  ILE C 163 ? MET C 170 ? ILE D 165 MET D 172 
AA7 6  GLU C 198 ? ASP C 203 ? GLU D 200 ASP D 205 
AA7 7  PHE C 265 ? ALA C 271 ? PHE D 267 ALA D 273 
AA7 8  SER C 364 ? SER C 371 ? SER D 374 SER D 381 
AA7 9  TYR C 310 ? ARG C 318 ? TYR D 312 ARG D 320 
AA7 10 VAL C 349 ? CYS C 354 ? VAL D 351 CYS D 356 
AA8 1  TYR C 51  ? ALA C 54  ? TYR D 53  ALA D 56  
AA8 2  LYS C 58  ? PRO C 61  ? LYS D 60  PRO D 63  
AA9 1  TRP E 27  ? ARG E 29  ? TRP F 27  ARG F 29  
AA9 2  TYR E 2   ? VAL E 5   ? TYR F 2   VAL F 5   
AA9 3  LEU E 39  ? MET E 40  ? LEU F 39  MET F 40  
AA9 4  LEU E 61  ? VAL E 62  ? LEU F 61  VAL F 62  
AA9 5  GLN E 310 ? SER E 311 ? GLN F 310 SER F 311 
AB1 1  SER E 97  ? ILE E 100 ? SER F 97  ILE F 100 
AB1 2  HIS E 180 ? LYS E 184 ? HIS F 180 LYS F 184 
AB1 3  TRP E 147 ? ILE E 148 ? TRP F 147 ILE F 148 
AB1 4  ILE E 162 ? SER E 163 ? ILE F 162 SER F 163 
AB2 1  GLU E 261 ? PHE E 263 ? GLU F 261 PHE F 263 
AB2 2  VAL E 220 ? ARG E 222 ? VAL F 220 ARG F 222 
AB2 3  ILE E 201 ? VAL E 207 ? ILE F 201 VAL F 207 
AB2 4  GLN E 313 ? MET E 320 ? GLN F 313 MET F 320 
AB2 5  TRP E 328 ? ASN E 333 ? TRP F 328 ASN F 333 
AB3 1  GLU E 261 ? PHE E 263 ? GLU F 261 PHE F 263 
AB3 2  VAL E 220 ? ARG E 222 ? VAL F 220 ARG F 222 
AB3 3  ILE E 201 ? VAL E 207 ? ILE F 201 VAL F 207 
AB3 4  ILE E 213 ? TYR E 216 ? ILE F 213 TYR F 216 
AB3 5  PHE E 375 ? LYS E 377 ? PHE F 375 LYS F 377 
AB4 1  PHE F 90  ? PHE F 92  ? PHE B 92  PHE B 94  
AB4 2  ALA F 63  ? ASP F 67  ? ALA B 65  ASP B 69  
AB4 3  ARG F 2   ? ALA F 9   ? ARG B 2   ALA B 9   
AB4 4  CYS F 129 ? SER F 138 ? CYS B 131 SER B 140 
AB4 5  ILE F 163 ? MET F 170 ? ILE B 165 MET B 172 
AB4 6  GLU F 198 ? ASP F 203 ? GLU B 200 ASP B 205 
AB4 7  PHE F 265 ? ALA F 271 ? PHE B 267 ALA B 273 
AB4 8  SER F 364 ? SER F 371 ? SER B 374 SER B 381 
AB4 9  TYR F 310 ? ARG F 318 ? TYR B 312 ARG B 320 
AB4 10 VAL F 349 ? CYS F 354 ? VAL B 351 CYS B 356 
AB5 1  TYR F 51  ? ALA F 54  ? TYR B 53  ALA B 56  
AB5 2  LYS F 58  ? PRO F 61  ? LYS B 60  PRO B 63  
# 
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 SER A 6   ? N SER A 6   
AA1 3 4  N ILE A 7   ? N ILE A 7   O LEU A 136 ? O LEU A 136 
AA1 4 5  N VAL A 137 ? N VAL A 137 O LEU A 167 ? O LEU A 167 
AA1 5 6  N GLU A 168 ? N GLU A 168 O PHE A 202 ? O PHE A 202 
AA2 1 2  N SER A 54  ? N SER A 54  O VAL A 62  ? O VAL A 62  
AA3 1 2  N THR A 271 ? N THR A 271 O MET A 377 ? O MET A 377 
AA3 2 3  O ALA A 374 ? O ALA A 374 N ARG A 320 ? N ARG A 320 
AA3 3 4  N TYR A 319 ? N TYR A 319 O GLY A 354 ? O GLY A 354 
AA3 4 5  N THR A 349 ? N THR A 349 O LEU D 22  ? O LEU E 24  
AA3 5 6  O GLU D 19  ? O GLU E 21  N ILE D 7   ? N ILE E 9   
AA4 1 2  O ILE B 93  ? O ILE C 93  N ASP B 69  ? N ASP C 69  
AA4 2 3  O VAL B 68  ? O VAL C 68  N HIS B 8   ? N HIS C 8   
AA4 3 4  N ILE B 7   ? N ILE C 7   O LEU B 136 ? O LEU C 136 
AA4 4 5  N PHE B 135 ? N PHE C 135 O SER B 165 ? O SER C 165 
AA4 5 6  N GLU B 168 ? N GLU C 168 O CYS B 200 ? O CYS C 200 
AA5 1 2  N SER B 54  ? N SER C 54  O VAL B 62  ? O VAL C 62  
AA6 1 2  N LEU B 269 ? N LEU C 269 O SER B 379 ? O SER C 379 
AA6 2 3  O LEU B 378 ? O LEU C 378 N CYS B 316 ? N CYS C 316 
AA6 3 4  N TYR B 319 ? N TYR C 319 O ASN B 356 ? O ASN C 356 
AA7 1 2  O VAL C 91  ? O VAL D 93  N LEU C 65  ? N LEU D 67  
AA7 2 3  O ILE C 64  ? O ILE D 66  N HIS C 6   ? N HIS D 6   
AA7 3 4  N ILE C 7   ? N ILE D 7   O GLN C 134 ? O GLN D 136 
AA7 4 5  N LEU C 135 ? N LEU D 137 O PHE C 167 ? O PHE D 169 
AA7 5 6  N MET C 170 ? N MET D 172 O ILE C 202 ? O ILE D 204 
AA7 6 7  N THR C 199 ? N THR D 201 O PHE C 266 ? O PHE D 268 
AA7 7 8  N MET C 267 ? N MET D 269 O GLY C 369 ? O GLY D 379 
AA7 8 9  O ILE C 368 ? O ILE D 378 N ALA C 314 ? N ALA D 316 
AA7 9 10 N ALA C 315 ? N ALA D 317 O ALA C 352 ? O ALA D 354 
AA8 1 2  N ASN C 52  ? N ASN D 54  O VAL C 60  ? O VAL D 62  
AA9 1 2  O LYS E 28  ? O LYS F 28  N TYR E 2   ? N TYR F 2   
AA9 2 3  O THR E 3   ? O THR F 3   N LEU E 39  ? N LEU F 39  
AA9 3 4  N MET E 40  ? N MET F 40  O LEU E 61  ? O LEU F 61  
AA9 4 5  N VAL E 62  ? N VAL F 62  O GLN E 310 ? O GLN F 310 
AB1 1 2  N ILE E 100 ? N ILE F 100 O HIS E 180 ? O HIS F 180 
AB1 2 3  O GLN E 183 ? O GLN F 183 N ILE E 148 ? N ILE F 148 
AB1 3 4  N TRP E 147 ? N TRP F 147 O SER E 163 ? O SER F 163 
AB2 1 2  O MET E 262 ? O MET F 262 N LEU E 221 ? N LEU F 221 
AB2 2 3  O VAL E 220 ? O VAL F 220 N ARG E 202 ? N ARG F 202 
AB2 3 4  N VAL E 205 ? N VAL F 205 O PHE E 315 ? O PHE F 315 
AB2 4 5  N MET E 320 ? N MET F 320 O TRP E 328 ? O TRP F 328 
AB3 1 2  O MET E 262 ? O MET F 262 N LEU E 221 ? N LEU F 221 
AB3 2 3  O VAL E 220 ? O VAL F 220 N ARG E 202 ? N ARG F 202 
AB3 3 4  N LEU E 206 ? N LEU F 206 O TYR E 214 ? O TYR F 214 
AB3 4 5  N LEU E 215 ? N LEU F 215 O ILE E 376 ? O ILE F 376 
AB4 1 2  O VAL F 91  ? O VAL B 93  N LEU F 65  ? N LEU B 67  
AB4 2 3  O VAL F 66  ? O VAL B 68  N GLN F 8   ? N GLN B 8   
AB4 3 4  N GLU F 3   ? N GLU B 3   O GLN F 131 ? O GLN B 133 
AB4 4 5  N GLN F 131 ? N GLN B 133 O ILE F 163 ? O ILE B 165 
AB4 5 6  N MET F 170 ? N MET B 172 O ILE F 202 ? O ILE B 204 
AB4 6 7  N THR F 199 ? N THR B 201 O PHE F 266 ? O PHE B 268 
AB4 7 8  N MET F 267 ? N MET B 269 O GLY F 369 ? O GLY B 379 
AB4 8 9  O ASN F 370 ? O ASN B 380 N LEU F 311 ? N LEU B 313 
AB4 9 10 N PHE F 317 ? N PHE B 319 O CYS F 354 ? O CYS B 356 
AB5 1 2  N ALA F 54  ? N ALA B 56  O LYS F 58  ? O LYS B 60  
# 
_pdbx_entry_details.entry_id                   9LNL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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  ? ? O1B   D GDP 501 ? ? 1.30 
2  1 N   B THR 145 ? ? O2B   B GDP 502 ? ? 1.30 
3  1 N   A GLN 11  ? ? O2B   A GTP 501 ? ? 1.30 
4  1 N   D CYS 12  ? ? O2A   D GDP 501 ? ? 1.30 
5  1 OD1 D ASN 228 ? ? N1    D GDP 501 ? ? 1.34 
6  1 C   D GLY 10  ? ? O1B   D GDP 501 ? ? 1.83 
7  1 OG1 A THR 41  ? ? O     A GLY 44  ? ? 1.94 
8  1 NH1 F ARG 128 ? ? OD1   F ASP 174 ? ? 1.96 
9  1 OD1 D ASN 228 ? ? C6    D GDP 501 ? ? 1.99 
10 1 OG1 A THR 145 ? ? O2G   A GTP 501 ? ? 2.01 
11 1 CA  D CYS 12  ? ? O2A   D GDP 501 ? ? 2.09 
12 1 O1A B GDP 502 ? ? O     B HOH 601 ? ? 2.09 
13 1 OG  F SER 88  ? ? OG    F SER 90  ? ? 2.09 
14 1 CA  B THR 145 ? ? O2B   B GDP 502 ? ? 2.10 
15 1 OG  A SER 140 ? ? "O5'" A GTP 501 ? ? 2.11 
16 1 NH1 B ARG 264 ? ? OE1   B GLU 431 ? ? 2.11 
17 1 OE2 B GLU 183 ? ? "O3'" B GDP 502 ? ? 2.12 
18 1 O   F LEU 80  ? ? OG    F SER 84  ? ? 2.13 
19 1 OD1 D ASN 228 ? ? O6    D GDP 501 ? ? 2.13 
20 1 OG1 C THR 41  ? ? OE2   C GLU 55  ? ? 2.14 
21 1 NZ  D LYS 254 ? ? O2G   C GTP 501 ? ? 2.16 
22 1 OH  D TYR 52  ? ? NE2   D GLN 136 ? ? 2.16 
23 1 OH  C TYR 224 ? ? O2A   C GTP 501 ? ? 2.16 
24 1 ND2 D ASN 206 ? ? "O2'" D GDP 501 ? ? 2.17 
25 1 OE2 D GLU 27  ? ? OG    D SER 236 ? ? 2.17 
26 1 CA  D GLN 11  ? ? O1B   D GDP 501 ? ? 2.18 
27 1 CA  A GLN 11  ? ? O2B   A GTP 501 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OG D SER 341 ? ? 1_555 NH2 F ARG 292 ? ? 3_545 2.05 
2 1 OH C TYR 282 ? ? 1_555 OE1 B GLU 411 ? ? 4_455 2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            D 
_pdbx_validate_rmsd_bond.auth_comp_id_1            ASN 
_pdbx_validate_rmsd_bond.auth_seq_id_1             228 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OD1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            D 
_pdbx_validate_rmsd_bond.auth_comp_id_2            ASN 
_pdbx_validate_rmsd_bond.auth_seq_id_2             228 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.391 
_pdbx_validate_rmsd_bond.bond_target_value         1.235 
_pdbx_validate_rmsd_bond.bond_deviation            0.156 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.022 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             D 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              228 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             D 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              228 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             D 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_3              228 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                121.88 
_pdbx_validate_rmsd_angle.angle_target_value         110.60 
_pdbx_validate_rmsd_angle.angle_deviation            11.28 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 41  ? ? -67.72  78.47   
2  1 ASP A 46  ? ? -94.88  58.89   
3  1 VAL A 68  ? ? -160.11 105.61  
4  1 ARG A 79  ? ? -81.14  30.24   
5  1 THR A 80  ? ? -151.10 -20.42  
6  1 ALA A 100 ? ? 33.62   59.74   
7  1 ASN A 101 ? ? 38.68   40.38   
8  1 TYR A 108 ? ? -100.67 -62.49  
9  1 ILE A 110 ? ? 100.74  -38.99  
10 1 ILE A 114 ? ? -150.66 22.05   
11 1 GLN A 128 ? ? -70.77  35.89   
12 1 LEU A 132 ? ? -30.34  126.84  
13 1 TYR A 161 ? ? -142.18 55.05   
14 1 CYS A 200 ? ? -178.14 122.37  
15 1 ASP A 218 ? ? 57.38   15.30   
16 1 ALA A 281 ? ? -44.20  -70.03  
17 1 ALA A 294 ? ? -38.94  -32.54  
18 1 ALA A 314 ? ? 176.71  159.31  
19 1 ALA A 333 ? ? -29.46  -52.39  
20 1 TRP A 346 ? ? -69.43  20.39   
21 1 PRO A 359 ? ? -54.73  170.39  
22 1 PHE A 404 ? ? 69.22   -7.79   
23 1 ARG C 2   ? ? 80.54   41.45   
24 1 THR C 41  ? ? -48.50  86.85   
25 1 ALA C 58  ? ? -59.78  -7.90   
26 1 ASP C 98  ? ? -103.34 -159.60 
27 1 THR C 109 ? ? -163.77 -70.71  
28 1 LYS C 164 ? ? -36.34  141.08  
29 1 CYS C 200 ? ? -170.40 129.28  
30 1 HIS C 283 ? ? 36.66   60.83   
31 1 GLU C 284 ? ? -176.13 84.08   
32 1 ALA C 314 ? ? 173.62  158.44  
33 1 CYS C 315 ? ? -160.82 106.86  
34 1 ASP C 322 ? ? -60.35  85.89   
35 1 ARG C 402 ? ? 57.18   13.89   
36 1 PHE C 404 ? ? 70.65   -9.19   
37 1 GLN D 11  ? ? -62.03  -72.13  
38 1 GLU D 22  ? ? -61.49  -70.88  
39 1 ASP D 39  ? ? -131.74 -62.11  
40 1 ARG D 64  ? ? -60.89  69.85   
41 1 ASP D 69  ? ? 175.82  141.12  
42 1 ARG D 79  ? ? -33.99  -33.21  
43 1 ALA D 99  ? ? 64.14   -52.13  
44 1 ALA D 104 ? ? -39.08  -36.73  
45 1 THR D 109 ? ? -100.27 -88.46  
46 1 LEU D 132 ? ? -55.67  109.77  
47 1 GLN D 133 ? ? -54.98  -81.55  
48 1 ARG D 158 ? ? -65.67  1.86    
49 1 PRO D 175 ? ? -57.47  -3.37   
50 1 TYR D 210 ? ? -61.20  -73.85  
51 1 ASP D 211 ? ? -39.85  -37.81  
52 1 PHE D 214 ? ? -49.23  -70.65  
53 1 ARG D 215 ? ? -73.32  -86.50  
54 1 THR D 221 ? ? 51.29   80.54   
55 1 ASN D 249 ? ? 30.93   67.44   
56 1 PHE D 296 ? ? -95.82  38.95   
57 1 ALA D 304 ? ? -32.87  -37.28  
58 1 ARG D 308 ? ? -66.54  11.18   
59 1 TYR D 312 ? ? -54.37  107.47  
60 1 MET D 323 ? ? -175.84 -179.03 
61 1 ASP D 357 ? ? -61.91  -76.12  
62 1 ILE D 358 ? ? -31.68  98.34   
63 1 LYS D 402 ? ? 39.04   35.21   
64 1 ALA D 403 ? ? -22.08  -71.39  
65 1 GLU E 7   ? ? -171.08 96.74   
66 1 GLU E 10  ? ? 36.63   52.93   
67 1 SER F 12  ? ? -39.19  -39.43  
68 1 ALA F 23  ? ? -60.97  33.35   
69 1 LYS F 32  ? ? -25.91  -38.55  
70 1 ARG F 36  ? ? -87.28  47.37   
71 1 LEU F 87  ? ? -111.59 -70.55  
72 1 SER F 88  ? ? 60.63   -166.81 
73 1 SER F 163 ? ? -172.64 146.62  
74 1 GLU F 168 ? ? 71.08   -32.93  
75 1 LYS F 188 ? ? -107.54 71.00   
76 1 ALA F 231 ? ? 83.08   6.74    
77 1 THR F 237 ? ? -140.91 -67.21  
78 1 CYS F 244 ? ? -60.21  -76.31  
79 1 GLU F 258 ? ? -58.89  105.43  
80 1 LEU F 275 ? ? 57.88   -37.70  
81 1 LEU F 275 ? ? 57.89   -37.76  
82 1 GLN F 313 ? ? -174.09 146.59  
83 1 ILE F 330 ? ? -133.44 -74.10  
84 1 LEU F 361 ? ? -125.99 -69.26  
85 1 GLN B 11  ? ? -55.11  -71.25  
86 1 PRO B 32  ? ? -60.65  7.70    
87 1 HIS B 37  ? ? -142.60 35.71   
88 1 ASP B 39  ? ? -112.79 -83.88  
89 1 SER B 40  ? ? -36.79  124.33  
90 1 SER B 80  ? ? -105.70 40.08   
91 1 ARG B 88  ? ? -49.54  109.21  
92 1 GLN B 96  ? ? -136.52 -50.34  
93 1 THR B 109 ? ? -108.82 -70.16  
94 1 ARG B 215 ? ? -66.06  -92.39  
95 1 LYS B 402 ? ? 39.67   41.97   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    41 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    42 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.15 
# 
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 VAL 440 ? A VAL 440 
2   1 Y 1 A GLU 441 ? A GLU 441 
3   1 Y 1 A GLY 442 ? A GLY 442 
4   1 Y 1 A GLU 443 ? A GLU 443 
5   1 Y 1 A GLY 444 ? A GLY 444 
6   1 Y 1 A GLU 445 ? A GLU 445 
7   1 Y 1 A GLU 446 ? A GLU 446 
8   1 Y 1 A GLU 447 ? A GLU 447 
9   1 Y 1 A GLY 448 ? A GLY 448 
10  1 Y 1 A GLU 449 ? A GLU 449 
11  1 Y 1 A GLU 450 ? A GLU 450 
12  1 Y 1 C GLU 441 ? B GLU 441 
13  1 Y 1 C GLY 442 ? B GLY 442 
14  1 Y 1 C GLU 443 ? B GLU 443 
15  1 Y 1 C GLY 444 ? B GLY 444 
16  1 Y 1 C GLU 445 ? B GLU 445 
17  1 Y 1 C GLU 446 ? B GLU 446 
18  1 Y 1 C GLU 447 ? B GLU 447 
19  1 Y 1 C GLY 448 ? B GLY 448 
20  1 Y 1 C GLU 449 ? B GLU 449 
21  1 Y 1 C GLU 450 ? B GLU 450 
22  1 Y 1 D SER 277 ? C SER 275 
23  1 Y 1 D ARG 278 ? C ARG 276 
24  1 Y 1 D GLY 279 ? C GLY 277 
25  1 Y 1 D SER 280 ? C SER 278 
26  1 Y 1 D GLN 281 ? C GLN 279 
27  1 Y 1 D GLN 282 ? C GLN 280 
28  1 Y 1 D TYR 283 ? C TYR 281 
29  1 Y 1 D GLU 442 ? C GLU 432 
30  1 Y 1 D GLN 443 ? C GLN 433 
31  1 Y 1 D GLY 444 ? C GLY 434 
32  1 Y 1 D GLU 445 ? C GLU 435 
33  1 Y 1 D PHE 446 ? C PHE 436 
34  1 Y 1 D GLU 447 ? C GLU 437 
35  1 Y 1 D GLU 448 ? C GLU 438 
36  1 Y 1 D GLU 449 ? C GLU 439 
37  1 Y 1 D GLU 450 ? C GLU 440 
38  1 Y 1 D GLY 451 ? C GLY 441 
39  1 Y 1 D GLU 452 ? C GLU 442 
40  1 Y 1 D ASP 453 ? C ASP 443 
41  1 Y 1 D GLU 454 ? C GLU 444 
42  1 Y 1 D ALA 455 ? C ALA 445 
43  1 Y 1 E MET 3   ? D MET 1   
44  1 Y 1 E ALA 4   ? D ALA 2   
45  1 Y 1 E ASP 5   ? D ASP 3   
46  1 Y 1 E PHE 29  ? D PHE 27  
47  1 Y 1 E ASP 30  ? D ASP 28  
48  1 Y 1 E GLY 31  ? D GLY 29  
49  1 Y 1 E VAL 32  ? D VAL 30  
50  1 Y 1 E PRO 33  ? D PRO 31  
51  1 Y 1 E GLU 34  ? D GLU 32  
52  1 Y 1 E PHE 35  ? D PHE 33  
53  1 Y 1 E ASN 36  ? D ASN 34  
54  1 Y 1 E ALA 37  ? D ALA 35  
55  1 Y 1 E SER 38  ? D SER 36  
56  1 Y 1 E LEU 39  ? D LEU 37  
57  1 Y 1 E PRO 40  ? D PRO 38  
58  1 Y 1 E ARG 41  ? D ARG 39  
59  1 Y 1 E ARG 42  ? D ARG 40  
60  1 Y 1 E ARG 43  ? D ARG 41  
61  1 Y 1 E GLU 141 ? D GLU 139 
62  1 Y 1 E GLU 142 ? D GLU 140 
63  1 Y 1 E ALA 143 ? D ALA 141 
64  1 Y 1 E SER 144 ? D SER 142 
65  1 Y 1 E ARG 145 ? D ARG 143 
66  1 Y 1 F ASN 104 ? E ASN 104 
67  1 Y 1 F LEU 105 ? E LEU 105 
68  1 Y 1 F LYS 106 ? E LYS 106 
69  1 Y 1 F THR 107 ? E THR 107 
70  1 Y 1 F PRO 108 ? E PRO 108 
71  1 Y 1 F VAL 109 ? E VAL 109 
72  1 Y 1 F ALA 110 ? E ALA 110 
73  1 Y 1 F PRO 111 ? E PRO 111 
74  1 Y 1 F ALA 112 ? E ALA 112 
75  1 Y 1 F GLN 113 ? E GLN 113 
76  1 Y 1 F ASN 114 ? E ASN 114 
77  1 Y 1 F GLY 115 ? E GLY 115 
78  1 Y 1 F ILE 116 ? E ILE 116 
79  1 Y 1 F ARG 117 ? E ARG 117 
80  1 Y 1 F HIS 118 ? E HIS 118 
81  1 Y 1 F LEU 119 ? E LEU 119 
82  1 Y 1 F ILE 120 ? E ILE 120 
83  1 Y 1 F ASN 121 ? E ASN 121 
84  1 Y 1 F ASN 122 ? E ASN 122 
85  1 Y 1 F THR 123 ? E THR 123 
86  1 Y 1 F ARG 124 ? E ARG 124 
87  1 Y 1 F ARG 138 ? E ARG 138 
88  1 Y 1 F ARG 139 ? E ARG 139 
89  1 Y 1 F GLU 140 ? E GLU 140 
90  1 Y 1 F GLY 141 ? E GLY 141 
91  1 Y 1 F ARG 142 ? E ARG 142 
92  1 Y 1 F GLU 143 ? E GLU 143 
93  1 Y 1 F LYS 150 ? E LYS 150 
94  1 Y 1 F SER 151 ? E SER 151 
95  1 Y 1 F SER 152 ? E SER 152 
96  1 Y 1 F ALA 153 ? E ALA 153 
97  1 Y 1 F GLY 154 ? E GLY 154 
98  1 Y 1 F ALA 155 ? E ALA 155 
99  1 Y 1 F LYS 156 ? E LYS 156 
100 1 Y 1 F GLY 157 ? E GLY 157 
101 1 Y 1 F GLU 158 ? E GLU 158 
102 1 Y 1 F LYS 251 ? E LYS 251 
103 1 Y 1 F ASN 252 ? E ASN 252 
104 1 Y 1 F TYR 253 ? E TYR 253 
105 1 Y 1 F GLY 254 ? E GLY 254 
106 1 Y 1 F ASP 363 ? E ASP 363 
107 1 Y 1 F THR 364 ? E THR 364 
108 1 Y 1 F GLY 365 ? E GLY 365 
109 1 Y 1 F GLN 366 ? E GLN 366 
110 1 Y 1 F LYS 367 ? E LYS 367 
111 1 Y 1 F THR 368 ? E THR 368 
112 1 Y 1 F SER 369 ? E SER 369 
113 1 Y 1 F GLN 370 ? E GLN 370 
114 1 Y 1 F PRO 371 ? E PRO 371 
115 1 Y 1 F HIS 381 ? E HIS 381 
116 1 Y 1 F HIS 382 ? E HIS 382 
117 1 Y 1 F HIS 383 ? E HIS 383 
118 1 Y 1 F HIS 384 ? E HIS 384 
119 1 Y 1 B THR 439 ? F THR 429 
120 1 Y 1 B ALA 440 ? F ALA 430 
121 1 Y 1 B ASP 441 ? F ASP 431 
122 1 Y 1 B GLU 442 ? F GLU 432 
123 1 Y 1 B GLN 443 ? F GLN 433 
124 1 Y 1 B GLY 444 ? F GLY 434 
125 1 Y 1 B GLU 445 ? F GLU 435 
126 1 Y 1 B PHE 446 ? F PHE 436 
127 1 Y 1 B GLU 447 ? F GLU 437 
128 1 Y 1 B GLU 448 ? F GLU 438 
129 1 Y 1 B GLU 449 ? F GLU 439 
130 1 Y 1 B GLU 450 ? F GLU 440 
131 1 Y 1 B GLY 451 ? F GLY 441 
132 1 Y 1 B GLU 452 ? F GLU 442 
133 1 Y 1 B ASP 453 ? F ASP 443 
134 1 Y 1 B GLU 454 ? F GLU 444 
135 1 Y 1 B ALA 455 ? F ALA 445 
136 1 N 0 A GTP 501 ? G GTP ?   
137 1 N 0 A CA  502 ? H CA  ?   
138 1 N 0 C GTP 501 ? I GTP ?   
139 1 N 0 C MG  502 ? J MG  ?   
140 1 N 0 C CA  503 ? K CA  ?   
141 1 N 0 D GDP 501 ? M GDP ?   
142 1 N 0 B MG  501 ? N MG  ?   
143 1 N 0 B GDP 502 ? O GDP ?   
# 
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 
A1EPQ C10    C  N N 1   
A1EPQ C13    C  N N 2   
A1EPQ C15    C  Y N 3   
A1EPQ C17    C  Y N 4   
A1EPQ C20    C  Y N 5   
A1EPQ C21    C  N R 6   
A1EPQ C22    C  N N 7   
A1EPQ C24    C  N N 8   
A1EPQ C28    C  N N 9   
A1EPQ C01    C  N N 10  
A1EPQ C04    C  N R 11  
A1EPQ C05    C  N S 12  
A1EPQ C06    C  N R 13  
A1EPQ C07    C  N R 14  
A1EPQ C08    C  N N 15  
A1EPQ C09    C  N N 16  
A1EPQ C12    C  N N 17  
A1EPQ C14    C  N R 18  
A1EPQ C16    C  Y N 19  
A1EPQ C18    C  Y N 20  
A1EPQ C19    C  Y N 21  
A1EPQ C23    C  N N 22  
A1EPQ C25    C  N N 23  
A1EPQ C31    C  N N 24  
A1EPQ C32    C  N N 25  
A1EPQ C35    C  N N 26  
A1EPQ C36    C  N N 27  
A1EPQ C37    C  N R 28  
A1EPQ C38    C  N N 29  
A1EPQ C39    C  N S 30  
A1EPQ C40    C  N N 31  
A1EPQ C42    C  N N 32  
A1EPQ C43    C  N N 33  
A1EPQ C44    C  Y N 34  
A1EPQ C45    C  Y N 35  
A1EPQ C46    C  Y N 36  
A1EPQ C47    C  Y N 37  
A1EPQ C48    C  Y N 38  
A1EPQ C49    C  Y N 39  
A1EPQ C50    C  Y N 40  
A1EPQ C52    C  Y N 41  
A1EPQ C53    C  N S 42  
A1EPQ C54    C  N N 43  
A1EPQ C55    C  N N 44  
A1EPQ C56    C  N N 45  
A1EPQ C58    C  N N 46  
A1EPQ C61    C  N N 47  
A1EPQ F62    F  N N 48  
A1EPQ F63    F  N N 49  
A1EPQ N02    N  N N 50  
A1EPQ N11    N  N N 51  
A1EPQ N41    N  N R 52  
A1EPQ N51    N  Y N 53  
A1EPQ O03    O  N N 54  
A1EPQ O26    O  N N 55  
A1EPQ O27    O  N N 56  
A1EPQ O29    O  N N 57  
A1EPQ O30    O  N N 58  
A1EPQ O33    O  N N 59  
A1EPQ O34    O  N N 60  
A1EPQ O57    O  N N 61  
A1EPQ O59    O  N N 62  
A1EPQ O60    O  N N 63  
A1EPQ H102   H  N N 64  
A1EPQ H131   H  N N 65  
A1EPQ H132   H  N N 66  
A1EPQ H211   H  N N 67  
A1EPQ H222   H  N N 68  
A1EPQ H221   H  N N 69  
A1EPQ H241   H  N N 70  
A1EPQ H242   H  N N 71  
A1EPQ H243   H  N N 72  
A1EPQ H283   H  N N 73  
A1EPQ H281   H  N N 74  
A1EPQ H282   H  N N 75  
A1EPQ H013   H  N N 76  
A1EPQ H012   H  N N 77  
A1EPQ H011   H  N N 78  
A1EPQ H1     H  N N 79  
A1EPQ H061   H  N N 80  
A1EPQ H081   H  N N 81  
A1EPQ H091   H  N N 82  
A1EPQ H121   H  N N 83  
A1EPQ H122   H  N N 84  
A1EPQ H161   H  N N 85  
A1EPQ H191   H  N N 86  
A1EPQ H231   H  N N 87  
A1EPQ H233   H  N N 88  
A1EPQ H232   H  N N 89  
A1EPQ H322   H  N N 90  
A1EPQ H323   H  N N 91  
A1EPQ H321   H  N N 92  
A1EPQ H352   H  N N 93  
A1EPQ H351   H  N N 94  
A1EPQ H353   H  N N 95  
A1EPQ H362   H  N N 96  
A1EPQ H361   H  N N 97  
A1EPQ H371   H  N N 98  
A1EPQ H382   H  N N 99  
A1EPQ H381   H  N N 100 
A1EPQ H401   H  N N 101 
A1EPQ H402   H  N N 102 
A1EPQ H422   H  N N 103 
A1EPQ H421   H  N N 104 
A1EPQ H431   H  N N 105 
A1EPQ H432   H  N N 106 
A1EPQ H491   H  N N 107 
A1EPQ H542   H  N N 108 
A1EPQ H541   H  N N 109 
A1EPQ H551   H  N N 110 
A1EPQ H552   H  N N 111 
A1EPQ H563   H  N N 112 
A1EPQ H562   H  N N 113 
A1EPQ H561   H  N N 114 
A1EPQ H612   H  N N 115 
A1EPQ H613   H  N N 116 
A1EPQ H611   H  N N 117 
A1EPQ H511   H  N N 118 
A1EPQ H291   H  N N 119 
A1EPQ H571   H  N N 120 
A1EPQ H3     H  N N 121 
ALA   N      N  N N 122 
ALA   CA     C  N S 123 
ALA   C      C  N N 124 
ALA   O      O  N N 125 
ALA   CB     C  N N 126 
ALA   OXT    O  N N 127 
ALA   H      H  N N 128 
ALA   H2     H  N N 129 
ALA   HA     H  N N 130 
ALA   HB1    H  N N 131 
ALA   HB2    H  N N 132 
ALA   HB3    H  N N 133 
ALA   HXT    H  N N 134 
ARG   N      N  N N 135 
ARG   CA     C  N S 136 
ARG   C      C  N N 137 
ARG   O      O  N N 138 
ARG   CB     C  N N 139 
ARG   CG     C  N N 140 
ARG   CD     C  N N 141 
ARG   NE     N  N N 142 
ARG   CZ     C  N N 143 
ARG   NH1    N  N N 144 
ARG   NH2    N  N N 145 
ARG   OXT    O  N N 146 
ARG   H      H  N N 147 
ARG   H2     H  N N 148 
ARG   HA     H  N N 149 
ARG   HB2    H  N N 150 
ARG   HB3    H  N N 151 
ARG   HG2    H  N N 152 
ARG   HG3    H  N N 153 
ARG   HD2    H  N N 154 
ARG   HD3    H  N N 155 
ARG   HE     H  N N 156 
ARG   HH11   H  N N 157 
ARG   HH12   H  N N 158 
ARG   HH21   H  N N 159 
ARG   HH22   H  N N 160 
ARG   HXT    H  N N 161 
ASN   N      N  N N 162 
ASN   CA     C  N S 163 
ASN   C      C  N N 164 
ASN   O      O  N N 165 
ASN   CB     C  N N 166 
ASN   CG     C  N N 167 
ASN   OD1    O  N N 168 
ASN   ND2    N  N N 169 
ASN   OXT    O  N N 170 
ASN   H      H  N N 171 
ASN   H2     H  N N 172 
ASN   HA     H  N N 173 
ASN   HB2    H  N N 174 
ASN   HB3    H  N N 175 
ASN   HD21   H  N N 176 
ASN   HD22   H  N N 177 
ASN   HXT    H  N N 178 
ASP   N      N  N N 179 
ASP   CA     C  N S 180 
ASP   C      C  N N 181 
ASP   O      O  N N 182 
ASP   CB     C  N N 183 
ASP   CG     C  N N 184 
ASP   OD1    O  N N 185 
ASP   OD2    O  N N 186 
ASP   OXT    O  N N 187 
ASP   H      H  N N 188 
ASP   H2     H  N N 189 
ASP   HA     H  N N 190 
ASP   HB2    H  N N 191 
ASP   HB3    H  N N 192 
ASP   HD2    H  N N 193 
ASP   HXT    H  N N 194 
CA    CA     CA N N 195 
CYS   N      N  N N 196 
CYS   CA     C  N R 197 
CYS   C      C  N N 198 
CYS   O      O  N N 199 
CYS   CB     C  N N 200 
CYS   SG     S  N N 201 
CYS   OXT    O  N N 202 
CYS   H      H  N N 203 
CYS   H2     H  N N 204 
CYS   HA     H  N N 205 
CYS   HB2    H  N N 206 
CYS   HB3    H  N N 207 
CYS   HG     H  N N 208 
CYS   HXT    H  N N 209 
GDP   PB     P  N N 210 
GDP   O1B    O  N N 211 
GDP   O2B    O  N N 212 
GDP   O3B    O  N N 213 
GDP   O3A    O  N N 214 
GDP   PA     P  N N 215 
GDP   O1A    O  N N 216 
GDP   O2A    O  N N 217 
GDP   "O5'"  O  N N 218 
GDP   "C5'"  C  N N 219 
GDP   "C4'"  C  N R 220 
GDP   "O4'"  O  N N 221 
GDP   "C3'"  C  N S 222 
GDP   "O3'"  O  N N 223 
GDP   "C2'"  C  N R 224 
GDP   "O2'"  O  N N 225 
GDP   "C1'"  C  N R 226 
GDP   N9     N  Y N 227 
GDP   C8     C  Y N 228 
GDP   N7     N  Y N 229 
GDP   C5     C  Y N 230 
GDP   C6     C  N N 231 
GDP   O6     O  N N 232 
GDP   N1     N  N N 233 
GDP   C2     C  N N 234 
GDP   N2     N  N N 235 
GDP   N3     N  N N 236 
GDP   C4     C  Y N 237 
GDP   HOB2   H  N N 238 
GDP   HOB3   H  N N 239 
GDP   HOA2   H  N N 240 
GDP   "H5'"  H  N N 241 
GDP   "H5''" H  N N 242 
GDP   "H4'"  H  N N 243 
GDP   "H3'"  H  N N 244 
GDP   "HO3'" H  N N 245 
GDP   "H2'"  H  N N 246 
GDP   "HO2'" H  N N 247 
GDP   "H1'"  H  N N 248 
GDP   H8     H  N N 249 
GDP   HN1    H  N N 250 
GDP   HN21   H  N N 251 
GDP   HN22   H  N N 252 
GLN   N      N  N N 253 
GLN   CA     C  N S 254 
GLN   C      C  N N 255 
GLN   O      O  N N 256 
GLN   CB     C  N N 257 
GLN   CG     C  N N 258 
GLN   CD     C  N N 259 
GLN   OE1    O  N N 260 
GLN   NE2    N  N N 261 
GLN   OXT    O  N N 262 
GLN   H      H  N N 263 
GLN   H2     H  N N 264 
GLN   HA     H  N N 265 
GLN   HB2    H  N N 266 
GLN   HB3    H  N N 267 
GLN   HG2    H  N N 268 
GLN   HG3    H  N N 269 
GLN   HE21   H  N N 270 
GLN   HE22   H  N N 271 
GLN   HXT    H  N N 272 
GLU   N      N  N N 273 
GLU   CA     C  N S 274 
GLU   C      C  N N 275 
GLU   O      O  N N 276 
GLU   CB     C  N N 277 
GLU   CG     C  N N 278 
GLU   CD     C  N N 279 
GLU   OE1    O  N N 280 
GLU   OE2    O  N N 281 
GLU   OXT    O  N N 282 
GLU   H      H  N N 283 
GLU   H2     H  N N 284 
GLU   HA     H  N N 285 
GLU   HB2    H  N N 286 
GLU   HB3    H  N N 287 
GLU   HG2    H  N N 288 
GLU   HG3    H  N N 289 
GLU   HE2    H  N N 290 
GLU   HXT    H  N N 291 
GLY   N      N  N N 292 
GLY   CA     C  N N 293 
GLY   C      C  N N 294 
GLY   O      O  N N 295 
GLY   OXT    O  N N 296 
GLY   H      H  N N 297 
GLY   H2     H  N N 298 
GLY   HA2    H  N N 299 
GLY   HA3    H  N N 300 
GLY   HXT    H  N N 301 
GTP   PG     P  N N 302 
GTP   O1G    O  N N 303 
GTP   O2G    O  N N 304 
GTP   O3G    O  N N 305 
GTP   O3B    O  N N 306 
GTP   PB     P  N N 307 
GTP   O1B    O  N N 308 
GTP   O2B    O  N N 309 
GTP   O3A    O  N N 310 
GTP   PA     P  N N 311 
GTP   O1A    O  N N 312 
GTP   O2A    O  N N 313 
GTP   "O5'"  O  N N 314 
GTP   "C5'"  C  N N 315 
GTP   "C4'"  C  N R 316 
GTP   "O4'"  O  N N 317 
GTP   "C3'"  C  N S 318 
GTP   "O3'"  O  N N 319 
GTP   "C2'"  C  N R 320 
GTP   "O2'"  O  N N 321 
GTP   "C1'"  C  N R 322 
GTP   N9     N  Y N 323 
GTP   C8     C  Y N 324 
GTP   N7     N  Y N 325 
GTP   C5     C  Y N 326 
GTP   C6     C  N N 327 
GTP   O6     O  N N 328 
GTP   N1     N  N N 329 
GTP   C2     C  N N 330 
GTP   N2     N  N N 331 
GTP   N3     N  N N 332 
GTP   C4     C  Y N 333 
GTP   HOG2   H  N N 334 
GTP   HOG3   H  N N 335 
GTP   HOB2   H  N N 336 
GTP   HOA2   H  N N 337 
GTP   "H5'"  H  N N 338 
GTP   "H5''" H  N N 339 
GTP   "H4'"  H  N N 340 
GTP   "H3'"  H  N N 341 
GTP   "HO3'" H  N N 342 
GTP   "H2'"  H  N N 343 
GTP   "HO2'" H  N N 344 
GTP   "H1'"  H  N N 345 
GTP   H8     H  N N 346 
GTP   HN1    H  N N 347 
GTP   HN21   H  N N 348 
GTP   HN22   H  N N 349 
HIS   N      N  N N 350 
HIS   CA     C  N S 351 
HIS   C      C  N N 352 
HIS   O      O  N N 353 
HIS   CB     C  N N 354 
HIS   CG     C  Y N 355 
HIS   ND1    N  Y N 356 
HIS   CD2    C  Y N 357 
HIS   CE1    C  Y N 358 
HIS   NE2    N  Y N 359 
HIS   OXT    O  N N 360 
HIS   H      H  N N 361 
HIS   H2     H  N N 362 
HIS   HA     H  N N 363 
HIS   HB2    H  N N 364 
HIS   HB3    H  N N 365 
HIS   HD1    H  N N 366 
HIS   HD2    H  N N 367 
HIS   HE1    H  N N 368 
HIS   HE2    H  N N 369 
HIS   HXT    H  N N 370 
HOH   O      O  N N 371 
HOH   H1     H  N N 372 
HOH   H2     H  N N 373 
ILE   N      N  N N 374 
ILE   CA     C  N S 375 
ILE   C      C  N N 376 
ILE   O      O  N N 377 
ILE   CB     C  N S 378 
ILE   CG1    C  N N 379 
ILE   CG2    C  N N 380 
ILE   CD1    C  N N 381 
ILE   OXT    O  N N 382 
ILE   H      H  N N 383 
ILE   H2     H  N N 384 
ILE   HA     H  N N 385 
ILE   HB     H  N N 386 
ILE   HG12   H  N N 387 
ILE   HG13   H  N N 388 
ILE   HG21   H  N N 389 
ILE   HG22   H  N N 390 
ILE   HG23   H  N N 391 
ILE   HD11   H  N N 392 
ILE   HD12   H  N N 393 
ILE   HD13   H  N N 394 
ILE   HXT    H  N N 395 
LEU   N      N  N N 396 
LEU   CA     C  N S 397 
LEU   C      C  N N 398 
LEU   O      O  N N 399 
LEU   CB     C  N N 400 
LEU   CG     C  N N 401 
LEU   CD1    C  N N 402 
LEU   CD2    C  N N 403 
LEU   OXT    O  N N 404 
LEU   H      H  N N 405 
LEU   H2     H  N N 406 
LEU   HA     H  N N 407 
LEU   HB2    H  N N 408 
LEU   HB3    H  N N 409 
LEU   HG     H  N N 410 
LEU   HD11   H  N N 411 
LEU   HD12   H  N N 412 
LEU   HD13   H  N N 413 
LEU   HD21   H  N N 414 
LEU   HD22   H  N N 415 
LEU   HD23   H  N N 416 
LEU   HXT    H  N N 417 
LYS   N      N  N N 418 
LYS   CA     C  N S 419 
LYS   C      C  N N 420 
LYS   O      O  N N 421 
LYS   CB     C  N N 422 
LYS   CG     C  N N 423 
LYS   CD     C  N N 424 
LYS   CE     C  N N 425 
LYS   NZ     N  N N 426 
LYS   OXT    O  N N 427 
LYS   H      H  N N 428 
LYS   H2     H  N N 429 
LYS   HA     H  N N 430 
LYS   HB2    H  N N 431 
LYS   HB3    H  N N 432 
LYS   HG2    H  N N 433 
LYS   HG3    H  N N 434 
LYS   HD2    H  N N 435 
LYS   HD3    H  N N 436 
LYS   HE2    H  N N 437 
LYS   HE3    H  N N 438 
LYS   HZ1    H  N N 439 
LYS   HZ2    H  N N 440 
LYS   HZ3    H  N N 441 
LYS   HXT    H  N N 442 
MET   N      N  N N 443 
MET   CA     C  N S 444 
MET   C      C  N N 445 
MET   O      O  N N 446 
MET   CB     C  N N 447 
MET   CG     C  N N 448 
MET   SD     S  N N 449 
MET   CE     C  N N 450 
MET   OXT    O  N N 451 
MET   H      H  N N 452 
MET   H2     H  N N 453 
MET   HA     H  N N 454 
MET   HB2    H  N N 455 
MET   HB3    H  N N 456 
MET   HG2    H  N N 457 
MET   HG3    H  N N 458 
MET   HE1    H  N N 459 
MET   HE2    H  N N 460 
MET   HE3    H  N N 461 
MET   HXT    H  N N 462 
MG    MG     MG N N 463 
PHE   N      N  N N 464 
PHE   CA     C  N S 465 
PHE   C      C  N N 466 
PHE   O      O  N N 467 
PHE   CB     C  N N 468 
PHE   CG     C  Y N 469 
PHE   CD1    C  Y N 470 
PHE   CD2    C  Y N 471 
PHE   CE1    C  Y N 472 
PHE   CE2    C  Y N 473 
PHE   CZ     C  Y N 474 
PHE   OXT    O  N N 475 
PHE   H      H  N N 476 
PHE   H2     H  N N 477 
PHE   HA     H  N N 478 
PHE   HB2    H  N N 479 
PHE   HB3    H  N N 480 
PHE   HD1    H  N N 481 
PHE   HD2    H  N N 482 
PHE   HE1    H  N N 483 
PHE   HE2    H  N N 484 
PHE   HZ     H  N N 485 
PHE   HXT    H  N N 486 
PRO   N      N  N N 487 
PRO   CA     C  N S 488 
PRO   C      C  N N 489 
PRO   O      O  N N 490 
PRO   CB     C  N N 491 
PRO   CG     C  N N 492 
PRO   CD     C  N N 493 
PRO   OXT    O  N N 494 
PRO   H      H  N N 495 
PRO   HA     H  N N 496 
PRO   HB2    H  N N 497 
PRO   HB3    H  N N 498 
PRO   HG2    H  N N 499 
PRO   HG3    H  N N 500 
PRO   HD2    H  N N 501 
PRO   HD3    H  N N 502 
PRO   HXT    H  N N 503 
SER   N      N  N N 504 
SER   CA     C  N S 505 
SER   C      C  N N 506 
SER   O      O  N N 507 
SER   CB     C  N N 508 
SER   OG     O  N N 509 
SER   OXT    O  N N 510 
SER   H      H  N N 511 
SER   H2     H  N N 512 
SER   HA     H  N N 513 
SER   HB2    H  N N 514 
SER   HB3    H  N N 515 
SER   HG     H  N N 516 
SER   HXT    H  N N 517 
THR   N      N  N N 518 
THR   CA     C  N S 519 
THR   C      C  N N 520 
THR   O      O  N N 521 
THR   CB     C  N R 522 
THR   OG1    O  N N 523 
THR   CG2    C  N N 524 
THR   OXT    O  N N 525 
THR   H      H  N N 526 
THR   H2     H  N N 527 
THR   HA     H  N N 528 
THR   HB     H  N N 529 
THR   HG1    H  N N 530 
THR   HG21   H  N N 531 
THR   HG22   H  N N 532 
THR   HG23   H  N N 533 
THR   HXT    H  N N 534 
TRP   N      N  N N 535 
TRP   CA     C  N S 536 
TRP   C      C  N N 537 
TRP   O      O  N N 538 
TRP   CB     C  N N 539 
TRP   CG     C  Y N 540 
TRP   CD1    C  Y N 541 
TRP   CD2    C  Y N 542 
TRP   NE1    N  Y N 543 
TRP   CE2    C  Y N 544 
TRP   CE3    C  Y N 545 
TRP   CZ2    C  Y N 546 
TRP   CZ3    C  Y N 547 
TRP   CH2    C  Y N 548 
TRP   OXT    O  N N 549 
TRP   H      H  N N 550 
TRP   H2     H  N N 551 
TRP   HA     H  N N 552 
TRP   HB2    H  N N 553 
TRP   HB3    H  N N 554 
TRP   HD1    H  N N 555 
TRP   HE1    H  N N 556 
TRP   HE3    H  N N 557 
TRP   HZ2    H  N N 558 
TRP   HZ3    H  N N 559 
TRP   HH2    H  N N 560 
TRP   HXT    H  N N 561 
TYR   N      N  N N 562 
TYR   CA     C  N S 563 
TYR   C      C  N N 564 
TYR   O      O  N N 565 
TYR   CB     C  N N 566 
TYR   CG     C  Y N 567 
TYR   CD1    C  Y N 568 
TYR   CD2    C  Y N 569 
TYR   CE1    C  Y N 570 
TYR   CE2    C  Y N 571 
TYR   CZ     C  Y N 572 
TYR   OH     O  N N 573 
TYR   OXT    O  N N 574 
TYR   H      H  N N 575 
TYR   H2     H  N N 576 
TYR   HA     H  N N 577 
TYR   HB2    H  N N 578 
TYR   HB3    H  N N 579 
TYR   HD1    H  N N 580 
TYR   HD2    H  N N 581 
TYR   HE1    H  N N 582 
TYR   HE2    H  N N 583 
TYR   HH     H  N N 584 
TYR   HXT    H  N N 585 
VAL   N      N  N N 586 
VAL   CA     C  N S 587 
VAL   C      C  N N 588 
VAL   O      O  N N 589 
VAL   CB     C  N N 590 
VAL   CG1    C  N N 591 
VAL   CG2    C  N N 592 
VAL   OXT    O  N N 593 
VAL   H      H  N N 594 
VAL   H2     H  N N 595 
VAL   HA     H  N N 596 
VAL   HB     H  N N 597 
VAL   HG11   H  N N 598 
VAL   HG12   H  N N 599 
VAL   HG13   H  N N 600 
VAL   HG21   H  N N 601 
VAL   HG22   H  N N 602 
VAL   HG23   H  N N 603 
VAL   HXT    H  N N 604 
# 
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 
A1EPQ C10   C09    sing N N 1   
A1EPQ C10   N11    sing N N 2   
A1EPQ C13   C12    sing N N 3   
A1EPQ C13   C14    sing N N 4   
A1EPQ C15   C20    doub Y N 5   
A1EPQ C15   C14    sing N N 6   
A1EPQ C15   C16    sing Y N 7   
A1EPQ C17   C16    doub Y N 8   
A1EPQ C17   C18    sing Y N 9   
A1EPQ C17   C53    sing N N 10  
A1EPQ C20   C19    sing Y N 11  
A1EPQ C20   N02    sing N N 12  
A1EPQ C21   C07    sing N N 13  
A1EPQ C21   C14    sing N N 14  
A1EPQ C21   N11    sing N N 15  
A1EPQ C22   C07    sing N N 16  
A1EPQ C22   C23    sing N N 17  
A1EPQ C24   N02    sing N N 18  
A1EPQ C28   O27    sing N N 19  
A1EPQ C01   O03    sing N N 20  
A1EPQ C04   C05    sing N N 21  
A1EPQ C04   N02    sing N N 22  
A1EPQ C05   C06    sing N N 23  
A1EPQ C05   C25    sing N N 24  
A1EPQ C05   O29    sing N N 25  
A1EPQ C06   C07    sing N N 26  
A1EPQ C06   O30    sing N N 27  
A1EPQ C07   C08    sing N N 28  
A1EPQ C08   C09    doub N N 29  
A1EPQ C12   N11    sing N N 30  
A1EPQ C18   C19    doub Y N 31  
A1EPQ C18   O34    sing N N 32  
A1EPQ C25   O26    doub N N 33  
A1EPQ C25   O27    sing N N 34  
A1EPQ C31   C32    sing N N 35  
A1EPQ C31   O30    sing N N 36  
A1EPQ C31   O33    doub N N 37  
A1EPQ C35   O34    sing N N 38  
A1EPQ C36   C37    sing N N 39  
A1EPQ C36   C53    sing N N 40  
A1EPQ C37   C38    sing N N 41  
A1EPQ C37   C54    sing N N 42  
A1EPQ C38   C39    sing N N 43  
A1EPQ C39   C40    sing N N 44  
A1EPQ C39   C55    sing N N 45  
A1EPQ C39   O57    sing N N 46  
A1EPQ C40   N41    sing N N 47  
A1EPQ C42   C43    sing N N 48  
A1EPQ C42   N41    sing N N 49  
A1EPQ C43   C44    sing N N 50  
A1EPQ C44   C45    sing Y N 51  
A1EPQ C44   C52    doub Y N 52  
A1EPQ C45   C46    doub Y N 53  
A1EPQ C45   C50    sing Y N 54  
A1EPQ C46   C47    sing Y N 55  
A1EPQ C46   O03    sing N N 56  
A1EPQ C47   C48    doub Y N 57  
A1EPQ C47   F62    sing N N 58  
A1EPQ C48   C49    sing Y N 59  
A1EPQ C48   F63    sing N N 60  
A1EPQ C49   C50    doub Y N 61  
A1EPQ C50   N51    sing Y N 62  
A1EPQ C52   C53    sing N N 63  
A1EPQ C52   N51    sing Y N 64  
A1EPQ C53   C58    sing N N 65  
A1EPQ C54   N41    sing N N 66  
A1EPQ C55   C56    sing N N 67  
A1EPQ C58   O59    doub N N 68  
A1EPQ C58   O60    sing N N 69  
A1EPQ C61   O60    sing N N 70  
A1EPQ C10   H102   sing N N 71  
A1EPQ C13   H131   sing N N 72  
A1EPQ C13   H132   sing N N 73  
A1EPQ C21   H211   sing N N 74  
A1EPQ C22   H222   sing N N 75  
A1EPQ C22   H221   sing N N 76  
A1EPQ C24   H241   sing N N 77  
A1EPQ C24   H242   sing N N 78  
A1EPQ C24   H243   sing N N 79  
A1EPQ C28   H283   sing N N 80  
A1EPQ C28   H281   sing N N 81  
A1EPQ C28   H282   sing N N 82  
A1EPQ C01   H013   sing N N 83  
A1EPQ C01   H012   sing N N 84  
A1EPQ C01   H011   sing N N 85  
A1EPQ C04   H1     sing N N 86  
A1EPQ C06   H061   sing N N 87  
A1EPQ C08   H081   sing N N 88  
A1EPQ C09   H091   sing N N 89  
A1EPQ C12   H121   sing N N 90  
A1EPQ C12   H122   sing N N 91  
A1EPQ C16   H161   sing N N 92  
A1EPQ C19   H191   sing N N 93  
A1EPQ C23   H231   sing N N 94  
A1EPQ C23   H233   sing N N 95  
A1EPQ C23   H232   sing N N 96  
A1EPQ C32   H322   sing N N 97  
A1EPQ C32   H323   sing N N 98  
A1EPQ C32   H321   sing N N 99  
A1EPQ C35   H352   sing N N 100 
A1EPQ C35   H351   sing N N 101 
A1EPQ C35   H353   sing N N 102 
A1EPQ C36   H362   sing N N 103 
A1EPQ C36   H361   sing N N 104 
A1EPQ C37   H371   sing N N 105 
A1EPQ C38   H382   sing N N 106 
A1EPQ C38   H381   sing N N 107 
A1EPQ C40   H401   sing N N 108 
A1EPQ C40   H402   sing N N 109 
A1EPQ C42   H422   sing N N 110 
A1EPQ C42   H421   sing N N 111 
A1EPQ C43   H431   sing N N 112 
A1EPQ C43   H432   sing N N 113 
A1EPQ C49   H491   sing N N 114 
A1EPQ C54   H542   sing N N 115 
A1EPQ C54   H541   sing N N 116 
A1EPQ C55   H551   sing N N 117 
A1EPQ C55   H552   sing N N 118 
A1EPQ C56   H563   sing N N 119 
A1EPQ C56   H562   sing N N 120 
A1EPQ C56   H561   sing N N 121 
A1EPQ C61   H612   sing N N 122 
A1EPQ C61   H613   sing N N 123 
A1EPQ C61   H611   sing N N 124 
A1EPQ N51   H511   sing N N 125 
A1EPQ O29   H291   sing N N 126 
A1EPQ O57   H571   sing N N 127 
A1EPQ C04   C14    sing N N 128 
A1EPQ C10   H3     sing N N 129 
ALA   N     CA     sing N N 130 
ALA   N     H      sing N N 131 
ALA   N     H2     sing N N 132 
ALA   CA    C      sing N N 133 
ALA   CA    CB     sing N N 134 
ALA   CA    HA     sing N N 135 
ALA   C     O      doub N N 136 
ALA   C     OXT    sing N N 137 
ALA   CB    HB1    sing N N 138 
ALA   CB    HB2    sing N N 139 
ALA   CB    HB3    sing N N 140 
ALA   OXT   HXT    sing N N 141 
ARG   N     CA     sing N N 142 
ARG   N     H      sing N N 143 
ARG   N     H2     sing N N 144 
ARG   CA    C      sing N N 145 
ARG   CA    CB     sing N N 146 
ARG   CA    HA     sing N N 147 
ARG   C     O      doub N N 148 
ARG   C     OXT    sing N N 149 
ARG   CB    CG     sing N N 150 
ARG   CB    HB2    sing N N 151 
ARG   CB    HB3    sing N N 152 
ARG   CG    CD     sing N N 153 
ARG   CG    HG2    sing N N 154 
ARG   CG    HG3    sing N N 155 
ARG   CD    NE     sing N N 156 
ARG   CD    HD2    sing N N 157 
ARG   CD    HD3    sing N N 158 
ARG   NE    CZ     sing N N 159 
ARG   NE    HE     sing N N 160 
ARG   CZ    NH1    sing N N 161 
ARG   CZ    NH2    doub N N 162 
ARG   NH1   HH11   sing N N 163 
ARG   NH1   HH12   sing N N 164 
ARG   NH2   HH21   sing N N 165 
ARG   NH2   HH22   sing N N 166 
ARG   OXT   HXT    sing N N 167 
ASN   N     CA     sing N N 168 
ASN   N     H      sing N N 169 
ASN   N     H2     sing N N 170 
ASN   CA    C      sing N N 171 
ASN   CA    CB     sing N N 172 
ASN   CA    HA     sing N N 173 
ASN   C     O      doub N N 174 
ASN   C     OXT    sing N N 175 
ASN   CB    CG     sing N N 176 
ASN   CB    HB2    sing N N 177 
ASN   CB    HB3    sing N N 178 
ASN   CG    OD1    doub N N 179 
ASN   CG    ND2    sing N N 180 
ASN   ND2   HD21   sing N N 181 
ASN   ND2   HD22   sing N N 182 
ASN   OXT   HXT    sing N N 183 
ASP   N     CA     sing N N 184 
ASP   N     H      sing N N 185 
ASP   N     H2     sing N N 186 
ASP   CA    C      sing N N 187 
ASP   CA    CB     sing N N 188 
ASP   CA    HA     sing N N 189 
ASP   C     O      doub N N 190 
ASP   C     OXT    sing N N 191 
ASP   CB    CG     sing N N 192 
ASP   CB    HB2    sing N N 193 
ASP   CB    HB3    sing N N 194 
ASP   CG    OD1    doub N N 195 
ASP   CG    OD2    sing N N 196 
ASP   OD2   HD2    sing N N 197 
ASP   OXT   HXT    sing N N 198 
CYS   N     CA     sing N N 199 
CYS   N     H      sing N N 200 
CYS   N     H2     sing N N 201 
CYS   CA    C      sing N N 202 
CYS   CA    CB     sing N N 203 
CYS   CA    HA     sing N N 204 
CYS   C     O      doub N N 205 
CYS   C     OXT    sing N N 206 
CYS   CB    SG     sing N N 207 
CYS   CB    HB2    sing N N 208 
CYS   CB    HB3    sing N N 209 
CYS   SG    HG     sing N N 210 
CYS   OXT   HXT    sing N N 211 
GDP   PB    O1B    doub N N 212 
GDP   PB    O2B    sing N N 213 
GDP   PB    O3B    sing N N 214 
GDP   PB    O3A    sing N N 215 
GDP   O2B   HOB2   sing N N 216 
GDP   O3B   HOB3   sing N N 217 
GDP   O3A   PA     sing N N 218 
GDP   PA    O1A    doub N N 219 
GDP   PA    O2A    sing N N 220 
GDP   PA    "O5'"  sing N N 221 
GDP   O2A   HOA2   sing N N 222 
GDP   "O5'" "C5'"  sing N N 223 
GDP   "C5'" "C4'"  sing N N 224 
GDP   "C5'" "H5'"  sing N N 225 
GDP   "C5'" "H5''" sing N N 226 
GDP   "C4'" "O4'"  sing N N 227 
GDP   "C4'" "C3'"  sing N N 228 
GDP   "C4'" "H4'"  sing N N 229 
GDP   "O4'" "C1'"  sing N N 230 
GDP   "C3'" "O3'"  sing N N 231 
GDP   "C3'" "C2'"  sing N N 232 
GDP   "C3'" "H3'"  sing N N 233 
GDP   "O3'" "HO3'" sing N N 234 
GDP   "C2'" "O2'"  sing N N 235 
GDP   "C2'" "C1'"  sing N N 236 
GDP   "C2'" "H2'"  sing N N 237 
GDP   "O2'" "HO2'" sing N N 238 
GDP   "C1'" N9     sing N N 239 
GDP   "C1'" "H1'"  sing N N 240 
GDP   N9    C8     sing Y N 241 
GDP   N9    C4     sing Y N 242 
GDP   C8    N7     doub Y N 243 
GDP   C8    H8     sing N N 244 
GDP   N7    C5     sing Y N 245 
GDP   C5    C6     sing N N 246 
GDP   C5    C4     doub Y N 247 
GDP   C6    O6     doub N N 248 
GDP   C6    N1     sing N N 249 
GDP   N1    C2     sing N N 250 
GDP   N1    HN1    sing N N 251 
GDP   C2    N2     sing N N 252 
GDP   C2    N3     doub N N 253 
GDP   N2    HN21   sing N N 254 
GDP   N2    HN22   sing N N 255 
GDP   N3    C4     sing N N 256 
GLN   N     CA     sing N N 257 
GLN   N     H      sing N N 258 
GLN   N     H2     sing N N 259 
GLN   CA    C      sing N N 260 
GLN   CA    CB     sing N N 261 
GLN   CA    HA     sing N N 262 
GLN   C     O      doub N N 263 
GLN   C     OXT    sing N N 264 
GLN   CB    CG     sing N N 265 
GLN   CB    HB2    sing N N 266 
GLN   CB    HB3    sing N N 267 
GLN   CG    CD     sing N N 268 
GLN   CG    HG2    sing N N 269 
GLN   CG    HG3    sing N N 270 
GLN   CD    OE1    doub N N 271 
GLN   CD    NE2    sing N N 272 
GLN   NE2   HE21   sing N N 273 
GLN   NE2   HE22   sing N N 274 
GLN   OXT   HXT    sing N N 275 
GLU   N     CA     sing N N 276 
GLU   N     H      sing N N 277 
GLU   N     H2     sing N N 278 
GLU   CA    C      sing N N 279 
GLU   CA    CB     sing N N 280 
GLU   CA    HA     sing N N 281 
GLU   C     O      doub N N 282 
GLU   C     OXT    sing N N 283 
GLU   CB    CG     sing N N 284 
GLU   CB    HB2    sing N N 285 
GLU   CB    HB3    sing N N 286 
GLU   CG    CD     sing N N 287 
GLU   CG    HG2    sing N N 288 
GLU   CG    HG3    sing N N 289 
GLU   CD    OE1    doub N N 290 
GLU   CD    OE2    sing N N 291 
GLU   OE2   HE2    sing N N 292 
GLU   OXT   HXT    sing N N 293 
GLY   N     CA     sing N N 294 
GLY   N     H      sing N N 295 
GLY   N     H2     sing N N 296 
GLY   CA    C      sing N N 297 
GLY   CA    HA2    sing N N 298 
GLY   CA    HA3    sing N N 299 
GLY   C     O      doub N N 300 
GLY   C     OXT    sing N N 301 
GLY   OXT   HXT    sing N N 302 
GTP   PG    O1G    doub N N 303 
GTP   PG    O2G    sing N N 304 
GTP   PG    O3G    sing N N 305 
GTP   PG    O3B    sing N N 306 
GTP   O2G   HOG2   sing N N 307 
GTP   O3G   HOG3   sing N N 308 
GTP   O3B   PB     sing N N 309 
GTP   PB    O1B    doub N N 310 
GTP   PB    O2B    sing N N 311 
GTP   PB    O3A    sing N N 312 
GTP   O2B   HOB2   sing N N 313 
GTP   O3A   PA     sing N N 314 
GTP   PA    O1A    doub N N 315 
GTP   PA    O2A    sing N N 316 
GTP   PA    "O5'"  sing N N 317 
GTP   O2A   HOA2   sing N N 318 
GTP   "O5'" "C5'"  sing N N 319 
GTP   "C5'" "C4'"  sing N N 320 
GTP   "C5'" "H5'"  sing N N 321 
GTP   "C5'" "H5''" sing N N 322 
GTP   "C4'" "O4'"  sing N N 323 
GTP   "C4'" "C3'"  sing N N 324 
GTP   "C4'" "H4'"  sing N N 325 
GTP   "O4'" "C1'"  sing N N 326 
GTP   "C3'" "O3'"  sing N N 327 
GTP   "C3'" "C2'"  sing N N 328 
GTP   "C3'" "H3'"  sing N N 329 
GTP   "O3'" "HO3'" sing N N 330 
GTP   "C2'" "O2'"  sing N N 331 
GTP   "C2'" "C1'"  sing N N 332 
GTP   "C2'" "H2'"  sing N N 333 
GTP   "O2'" "HO2'" sing N N 334 
GTP   "C1'" N9     sing N N 335 
GTP   "C1'" "H1'"  sing N N 336 
GTP   N9    C8     sing Y N 337 
GTP   N9    C4     sing Y N 338 
GTP   C8    N7     doub Y N 339 
GTP   C8    H8     sing N N 340 
GTP   N7    C5     sing Y N 341 
GTP   C5    C6     sing N N 342 
GTP   C5    C4     doub Y N 343 
GTP   C6    O6     doub N N 344 
GTP   C6    N1     sing N N 345 
GTP   N1    C2     sing N N 346 
GTP   N1    HN1    sing N N 347 
GTP   C2    N2     sing N N 348 
GTP   C2    N3     doub N N 349 
GTP   N2    HN21   sing N N 350 
GTP   N2    HN22   sing N N 351 
GTP   N3    C4     sing N N 352 
HIS   N     CA     sing N N 353 
HIS   N     H      sing N N 354 
HIS   N     H2     sing N N 355 
HIS   CA    C      sing N N 356 
HIS   CA    CB     sing N N 357 
HIS   CA    HA     sing N N 358 
HIS   C     O      doub N N 359 
HIS   C     OXT    sing N N 360 
HIS   CB    CG     sing N N 361 
HIS   CB    HB2    sing N N 362 
HIS   CB    HB3    sing N N 363 
HIS   CG    ND1    sing Y N 364 
HIS   CG    CD2    doub Y N 365 
HIS   ND1   CE1    doub Y N 366 
HIS   ND1   HD1    sing N N 367 
HIS   CD2   NE2    sing Y N 368 
HIS   CD2   HD2    sing N N 369 
HIS   CE1   NE2    sing Y N 370 
HIS   CE1   HE1    sing N N 371 
HIS   NE2   HE2    sing N N 372 
HIS   OXT   HXT    sing N N 373 
HOH   O     H1     sing N N 374 
HOH   O     H2     sing N N 375 
ILE   N     CA     sing N N 376 
ILE   N     H      sing N N 377 
ILE   N     H2     sing N N 378 
ILE   CA    C      sing N N 379 
ILE   CA    CB     sing N N 380 
ILE   CA    HA     sing N N 381 
ILE   C     O      doub N N 382 
ILE   C     OXT    sing N N 383 
ILE   CB    CG1    sing N N 384 
ILE   CB    CG2    sing N N 385 
ILE   CB    HB     sing N N 386 
ILE   CG1   CD1    sing N N 387 
ILE   CG1   HG12   sing N N 388 
ILE   CG1   HG13   sing N N 389 
ILE   CG2   HG21   sing N N 390 
ILE   CG2   HG22   sing N N 391 
ILE   CG2   HG23   sing N N 392 
ILE   CD1   HD11   sing N N 393 
ILE   CD1   HD12   sing N N 394 
ILE   CD1   HD13   sing N N 395 
ILE   OXT   HXT    sing N N 396 
LEU   N     CA     sing N N 397 
LEU   N     H      sing N N 398 
LEU   N     H2     sing N N 399 
LEU   CA    C      sing N N 400 
LEU   CA    CB     sing N N 401 
LEU   CA    HA     sing N N 402 
LEU   C     O      doub N N 403 
LEU   C     OXT    sing N N 404 
LEU   CB    CG     sing N N 405 
LEU   CB    HB2    sing N N 406 
LEU   CB    HB3    sing N N 407 
LEU   CG    CD1    sing N N 408 
LEU   CG    CD2    sing N N 409 
LEU   CG    HG     sing N N 410 
LEU   CD1   HD11   sing N N 411 
LEU   CD1   HD12   sing N N 412 
LEU   CD1   HD13   sing N N 413 
LEU   CD2   HD21   sing N N 414 
LEU   CD2   HD22   sing N N 415 
LEU   CD2   HD23   sing N N 416 
LEU   OXT   HXT    sing N N 417 
LYS   N     CA     sing N N 418 
LYS   N     H      sing N N 419 
LYS   N     H2     sing N N 420 
LYS   CA    C      sing N N 421 
LYS   CA    CB     sing N N 422 
LYS   CA    HA     sing N N 423 
LYS   C     O      doub N N 424 
LYS   C     OXT    sing N N 425 
LYS   CB    CG     sing N N 426 
LYS   CB    HB2    sing N N 427 
LYS   CB    HB3    sing N N 428 
LYS   CG    CD     sing N N 429 
LYS   CG    HG2    sing N N 430 
LYS   CG    HG3    sing N N 431 
LYS   CD    CE     sing N N 432 
LYS   CD    HD2    sing N N 433 
LYS   CD    HD3    sing N N 434 
LYS   CE    NZ     sing N N 435 
LYS   CE    HE2    sing N N 436 
LYS   CE    HE3    sing N N 437 
LYS   NZ    HZ1    sing N N 438 
LYS   NZ    HZ2    sing N N 439 
LYS   NZ    HZ3    sing N N 440 
LYS   OXT   HXT    sing N N 441 
MET   N     CA     sing N N 442 
MET   N     H      sing N N 443 
MET   N     H2     sing N N 444 
MET   CA    C      sing N N 445 
MET   CA    CB     sing N N 446 
MET   CA    HA     sing N N 447 
MET   C     O      doub N N 448 
MET   C     OXT    sing N N 449 
MET   CB    CG     sing N N 450 
MET   CB    HB2    sing N N 451 
MET   CB    HB3    sing N N 452 
MET   CG    SD     sing N N 453 
MET   CG    HG2    sing N N 454 
MET   CG    HG3    sing N N 455 
MET   SD    CE     sing N N 456 
MET   CE    HE1    sing N N 457 
MET   CE    HE2    sing N N 458 
MET   CE    HE3    sing N N 459 
MET   OXT   HXT    sing N N 460 
PHE   N     CA     sing N N 461 
PHE   N     H      sing N N 462 
PHE   N     H2     sing N N 463 
PHE   CA    C      sing N N 464 
PHE   CA    CB     sing N N 465 
PHE   CA    HA     sing N N 466 
PHE   C     O      doub N N 467 
PHE   C     OXT    sing N N 468 
PHE   CB    CG     sing N N 469 
PHE   CB    HB2    sing N N 470 
PHE   CB    HB3    sing N N 471 
PHE   CG    CD1    doub Y N 472 
PHE   CG    CD2    sing Y N 473 
PHE   CD1   CE1    sing Y N 474 
PHE   CD1   HD1    sing N N 475 
PHE   CD2   CE2    doub Y N 476 
PHE   CD2   HD2    sing N N 477 
PHE   CE1   CZ     doub Y N 478 
PHE   CE1   HE1    sing N N 479 
PHE   CE2   CZ     sing Y N 480 
PHE   CE2   HE2    sing N N 481 
PHE   CZ    HZ     sing N N 482 
PHE   OXT   HXT    sing N N 483 
PRO   N     CA     sing N N 484 
PRO   N     CD     sing N N 485 
PRO   N     H      sing N N 486 
PRO   CA    C      sing N N 487 
PRO   CA    CB     sing N N 488 
PRO   CA    HA     sing N N 489 
PRO   C     O      doub N N 490 
PRO   C     OXT    sing N N 491 
PRO   CB    CG     sing N N 492 
PRO   CB    HB2    sing N N 493 
PRO   CB    HB3    sing N N 494 
PRO   CG    CD     sing N N 495 
PRO   CG    HG2    sing N N 496 
PRO   CG    HG3    sing N N 497 
PRO   CD    HD2    sing N N 498 
PRO   CD    HD3    sing N N 499 
PRO   OXT   HXT    sing N N 500 
SER   N     CA     sing N N 501 
SER   N     H      sing N N 502 
SER   N     H2     sing N N 503 
SER   CA    C      sing N N 504 
SER   CA    CB     sing N N 505 
SER   CA    HA     sing N N 506 
SER   C     O      doub N N 507 
SER   C     OXT    sing N N 508 
SER   CB    OG     sing N N 509 
SER   CB    HB2    sing N N 510 
SER   CB    HB3    sing N N 511 
SER   OG    HG     sing N N 512 
SER   OXT   HXT    sing N N 513 
THR   N     CA     sing N N 514 
THR   N     H      sing N N 515 
THR   N     H2     sing N N 516 
THR   CA    C      sing N N 517 
THR   CA    CB     sing N N 518 
THR   CA    HA     sing N N 519 
THR   C     O      doub N N 520 
THR   C     OXT    sing N N 521 
THR   CB    OG1    sing N N 522 
THR   CB    CG2    sing N N 523 
THR   CB    HB     sing N N 524 
THR   OG1   HG1    sing N N 525 
THR   CG2   HG21   sing N N 526 
THR   CG2   HG22   sing N N 527 
THR   CG2   HG23   sing N N 528 
THR   OXT   HXT    sing N N 529 
TRP   N     CA     sing N N 530 
TRP   N     H      sing N N 531 
TRP   N     H2     sing N N 532 
TRP   CA    C      sing N N 533 
TRP   CA    CB     sing N N 534 
TRP   CA    HA     sing N N 535 
TRP   C     O      doub N N 536 
TRP   C     OXT    sing N N 537 
TRP   CB    CG     sing N N 538 
TRP   CB    HB2    sing N N 539 
TRP   CB    HB3    sing N N 540 
TRP   CG    CD1    doub Y N 541 
TRP   CG    CD2    sing Y N 542 
TRP   CD1   NE1    sing Y N 543 
TRP   CD1   HD1    sing N N 544 
TRP   CD2   CE2    doub Y N 545 
TRP   CD2   CE3    sing Y N 546 
TRP   NE1   CE2    sing Y N 547 
TRP   NE1   HE1    sing N N 548 
TRP   CE2   CZ2    sing Y N 549 
TRP   CE3   CZ3    doub Y N 550 
TRP   CE3   HE3    sing N N 551 
TRP   CZ2   CH2    doub Y N 552 
TRP   CZ2   HZ2    sing N N 553 
TRP   CZ3   CH2    sing Y N 554 
TRP   CZ3   HZ3    sing N N 555 
TRP   CH2   HH2    sing N N 556 
TRP   OXT   HXT    sing N N 557 
TYR   N     CA     sing N N 558 
TYR   N     H      sing N N 559 
TYR   N     H2     sing N N 560 
TYR   CA    C      sing N N 561 
TYR   CA    CB     sing N N 562 
TYR   CA    HA     sing N N 563 
TYR   C     O      doub N N 564 
TYR   C     OXT    sing N N 565 
TYR   CB    CG     sing N N 566 
TYR   CB    HB2    sing N N 567 
TYR   CB    HB3    sing N N 568 
TYR   CG    CD1    doub Y N 569 
TYR   CG    CD2    sing Y N 570 
TYR   CD1   CE1    sing Y N 571 
TYR   CD1   HD1    sing N N 572 
TYR   CD2   CE2    doub Y N 573 
TYR   CD2   HD2    sing N N 574 
TYR   CE1   CZ     doub Y N 575 
TYR   CE1   HE1    sing N N 576 
TYR   CE2   CZ     sing Y N 577 
TYR   CE2   HE2    sing N N 578 
TYR   CZ    OH     sing N N 579 
TYR   OH    HH     sing N N 580 
TYR   OXT   HXT    sing N N 581 
VAL   N     CA     sing N N 582 
VAL   N     H      sing N N 583 
VAL   N     H2     sing N N 584 
VAL   CA    C      sing N N 585 
VAL   CA    CB     sing N N 586 
VAL   CA    HA     sing N N 587 
VAL   C     O      doub N N 588 
VAL   C     OXT    sing N N 589 
VAL   CB    CG1    sing N N 590 
VAL   CB    CG2    sing N N 591 
VAL   CB    HB     sing N N 592 
VAL   CG1   HG11   sing N N 593 
VAL   CG1   HG12   sing N N 594 
VAL   CG1   HG13   sing N N 595 
VAL   CG2   HG21   sing N N 596 
VAL   CG2   HG22   sing N N 597 
VAL   CG2   HG23   sing N N 598 
VAL   OXT   HXT    sing N N 599 
# 
_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   8CLE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9LNL 
_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]   0.009497 
_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]   0.006393 
_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]   0.005409 
_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 
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   ? 39.930  101.459 67.888  1.00 51.75  ? 1   MET   A N     1 
ATOM   2     C  CA    . MET   A 1  1   ? 38.989  100.762 67.006  1.00 61.19  ? 1   MET   A CA    1 
ATOM   3     C  C     . MET   A 1  1   ? 39.670  99.560  66.339  1.00 66.32  ? 1   MET   A C     1 
ATOM   4     O  O     . MET   A 1  1   ? 40.819  99.651  65.890  1.00 70.65  ? 1   MET   A O     1 
ATOM   5     C  CB    . MET   A 1  1   ? 38.428  101.720 65.945  1.00 55.66  ? 1   MET   A CB    1 
ATOM   6     C  CG    . MET   A 1  1   ? 37.478  101.059 64.962  1.00 45.88  ? 1   MET   A CG    1 
ATOM   7     S  SD    . MET   A 1  1   ? 38.278  100.333 63.506  1.00 57.80  ? 1   MET   A SD    1 
ATOM   8     C  CE    . MET   A 1  1   ? 38.496  101.743 62.424  1.00 51.23  ? 1   MET   A CE    1 
ATOM   9     N  N     . ARG   A 1  2   ? 38.969  98.430  66.267  1.00 56.39  ? 2   ARG   A N     1 
ATOM   10    C  CA    . ARG   A 1  2   ? 39.550  97.203  65.733  1.00 50.98  ? 2   ARG   A CA    1 
ATOM   11    C  C     . ARG   A 1  2   ? 38.583  96.566  64.747  1.00 51.02  ? 2   ARG   A C     1 
ATOM   12    O  O     . ARG   A 1  2   ? 37.410  96.328  65.067  1.00 47.78  ? 2   ARG   A O     1 
ATOM   13    C  CB    . ARG   A 1  2   ? 39.895  96.217  66.848  1.00 52.45  ? 2   ARG   A CB    1 
ATOM   14    C  CG    . ARG   A 1  2   ? 40.255  96.859  68.171  1.00 48.50  ? 2   ARG   A CG    1 
ATOM   15    C  CD    . ARG   A 1  2   ? 40.710  95.790  69.132  1.00 53.10  ? 2   ARG   A CD    1 
ATOM   16    N  NE    . ARG   A 1  2   ? 41.773  95.004  68.516  1.00 50.74  ? 2   ARG   A NE    1 
ATOM   17    C  CZ    . ARG   A 1  2   ? 42.128  93.786  68.902  1.00 61.01  ? 2   ARG   A CZ    1 
ATOM   18    N  NH1   . ARG   A 1  2   ? 41.525  93.176  69.918  1.00 50.50  ? 2   ARG   A NH1   1 
ATOM   19    N  NH2   . ARG   A 1  2   ? 43.108  93.160  68.249  1.00 63.19  ? 2   ARG   A NH2   1 
ATOM   20    N  N     . GLU   A 1  3   ? 39.089  96.271  63.557  1.00 52.17  ? 3   GLU   A N     1 
ATOM   21    C  CA    . GLU   A 1  3   ? 38.246  95.853  62.452  1.00 47.98  ? 3   GLU   A CA    1 
ATOM   22    C  C     . GLU   A 1  3   ? 37.979  94.352  62.520  1.00 45.71  ? 3   GLU   A C     1 
ATOM   23    O  O     . GLU   A 1  3   ? 38.706  93.584  63.167  1.00 40.40  ? 3   GLU   A O     1 
ATOM   24    C  CB    . GLU   A 1  3   ? 38.908  96.227  61.120  1.00 52.56  ? 3   GLU   A CB    1 
ATOM   25    C  CG    . GLU   A 1  3   ? 39.425  97.700  61.029  1.00 53.85  ? 3   GLU   A CG    1 
ATOM   26    C  CD    . GLU   A 1  3   ? 40.860  97.940  61.579  1.00 53.69  ? 3   GLU   A CD    1 
ATOM   27    O  OE1   . GLU   A 1  3   ? 41.418  97.064  62.297  1.00 49.89  ? 3   GLU   A OE1   1 
ATOM   28    O  OE2   . GLU   A 1  3   ? 41.417  99.029  61.278  1.00 43.38  ? 3   GLU   A OE2   1 
ATOM   29    N  N     . CYS   A 1  4   ? 36.898  93.937  61.861  1.00 49.49  ? 4   CYS   A N     1 
ATOM   30    C  CA    . CYS   A 1  4   ? 36.569  92.524  61.707  1.00 44.48  ? 4   CYS   A CA    1 
ATOM   31    C  C     . CYS   A 1  4   ? 36.296  92.255  60.239  1.00 46.53  ? 4   CYS   A C     1 
ATOM   32    O  O     . CYS   A 1  4   ? 35.639  93.059  59.558  1.00 39.67  ? 4   CYS   A O     1 
ATOM   33    C  CB    . CYS   A 1  4   ? 35.332  92.088  62.524  1.00 43.45  ? 4   CYS   A CB    1 
ATOM   34    S  SG    . CYS   A 1  4   ? 35.326  92.400  64.302  1.00 52.41  ? 4   CYS   A SG    1 
ATOM   35    N  N     . ILE   A 1  5   ? 36.791  91.120  59.757  1.00 37.93  ? 5   ILE   A N     1 
ATOM   36    C  CA    . ILE   A 1  5   ? 36.536  90.699  58.385  1.00 43.33  ? 5   ILE   A CA    1 
ATOM   37    C  C     . ILE   A 1  5   ? 35.400  89.678  58.383  1.00 42.90  ? 5   ILE   A C     1 
ATOM   38    O  O     . ILE   A 1  5   ? 35.438  88.686  59.130  1.00 36.33  ? 5   ILE   A O     1 
ATOM   39    C  CB    . ILE   A 1  5   ? 37.801  90.114  57.736  1.00 43.52  ? 5   ILE   A CB    1 
ATOM   40    C  CG1   . ILE   A 1  5   ? 39.011  91.013  57.986  1.00 36.78  ? 5   ILE   A CG1   1 
ATOM   41    C  CG2   . ILE   A 1  5   ? 37.581  89.939  56.236  1.00 38.64  ? 5   ILE   A CG2   1 
ATOM   42    C  CD1   . ILE   A 1  5   ? 39.137  92.139  57.007  1.00 34.47  ? 5   ILE   A CD1   1 
ATOM   43    N  N     . SER   A 1  6   ? 34.389  89.920  57.547  1.00 40.40  ? 6   SER   A N     1 
ATOM   44    C  CA    . SER   A 1  6   ? 33.326  88.950  57.305  1.00 40.47  ? 6   SER   A CA    1 
ATOM   45    C  C     . SER   A 1  6   ? 33.670  88.121  56.068  1.00 40.83  ? 6   SER   A C     1 
ATOM   46    O  O     . SER   A 1  6   ? 34.127  88.669  55.060  1.00 40.48  ? 6   SER   A O     1 
ATOM   47    C  CB    . SER   A 1  6   ? 31.983  89.658  57.109  1.00 45.49  ? 6   SER   A CB    1 
ATOM   48    O  OG    . SER   A 1  6   ? 31.603  90.461  58.224  1.00 39.39  ? 6   SER   A OG    1 
ATOM   49    N  N     . ILE   A 1  7   ? 33.476  86.804  56.152  1.00 36.32  ? 7   ILE   A N     1 
ATOM   50    C  CA    . ILE   A 1  7   ? 33.753  85.898  55.034  1.00 38.36  ? 7   ILE   A CA    1 
ATOM   51    C  C     . ILE   A 1  7   ? 32.504  85.074  54.773  1.00 40.56  ? 7   ILE   A C     1 
ATOM   52    O  O     . ILE   A 1  7   ? 32.182  84.166  55.557  1.00 40.05  ? 7   ILE   A O     1 
ATOM   53    C  CB    . ILE   A 1  7   ? 34.941  84.955  55.281  1.00 39.59  ? 7   ILE   A CB    1 
ATOM   54    C  CG1   . ILE   A 1  7   ? 36.191  85.678  55.775  1.00 36.19  ? 7   ILE   A CG1   1 
ATOM   55    C  CG2   . ILE   A 1  7   ? 35.275  84.206  53.982  1.00 32.98  ? 7   ILE   A CG2   1 
ATOM   56    C  CD1   . ILE   A 1  7   ? 37.256  84.692  56.248  1.00 28.22  ? 7   ILE   A CD1   1 
ATOM   57    N  N     . HIS   A 1  8   ? 31.840  85.337  53.647  1.00 32.29  ? 8   HIS   A N     1 
ATOM   58    C  CA    . HIS   A 1  8   ? 30.631  84.621  53.265  1.00 29.97  ? 8   HIS   A CA    1 
ATOM   59    C  C     . HIS   A 1  8   ? 30.980  83.559  52.234  1.00 29.45  ? 8   HIS   A C     1 
ATOM   60    O  O     . HIS   A 1  8   ? 31.551  83.881  51.188  1.00 33.06  ? 8   HIS   A O     1 
ATOM   61    C  CB    . HIS   A 1  8   ? 29.604  85.604  52.722  1.00 35.13  ? 8   HIS   A CB    1 
ATOM   62    C  CG    . HIS   A 1  8   ? 29.476  86.845  53.552  1.00 40.44  ? 8   HIS   A CG    1 
ATOM   63    N  ND1   . HIS   A 1  8   ? 28.691  86.906  54.686  1.00 37.81  ? 8   HIS   A ND1   1 
ATOM   64    C  CD2   . HIS   A 1  8   ? 30.053  88.066  53.428  1.00 38.52  ? 8   HIS   A CD2   1 
ATOM   65    C  CE1   . HIS   A 1  8   ? 28.774  88.115  55.214  1.00 36.20  ? 8   HIS   A CE1   1 
ATOM   66    N  NE2   . HIS   A 1  8   ? 29.594  88.839  54.469  1.00 36.81  ? 8   HIS   A NE2   1 
ATOM   67    N  N     . VAL   A 1  9   ? 30.619  82.304  52.519  1.00 27.49  ? 9   VAL   A N     1 
ATOM   68    C  CA    . VAL   A 1  9   ? 31.124  81.139  51.797  1.00 23.67  ? 9   VAL   A CA    1 
ATOM   69    C  C     . VAL   A 1  9   ? 29.954  80.262  51.353  1.00 26.87  ? 9   VAL   A C     1 
ATOM   70    O  O     . VAL   A 1  9   ? 29.122  79.856  52.172  1.00 28.81  ? 9   VAL   A O     1 
ATOM   71    C  CB    . VAL   A 1  9   ? 32.104  80.341  52.672  1.00 21.24  ? 9   VAL   A CB    1 
ATOM   72    C  CG1   . VAL   A 1  9   ? 32.811  79.254  51.876  1.00 32.85  ? 9   VAL   A CG1   1 
ATOM   73    C  CG2   . VAL   A 1  9   ? 33.092  81.284  53.293  1.00 25.63  ? 9   VAL   A CG2   1 
ATOM   74    N  N     . GLY   A 1  10  ? 29.901  79.953  50.060  1.00 27.11  ? 10  GLY   A N     1 
ATOM   75    C  CA    . GLY   A 1  10  ? 28.850  79.116  49.517  1.00 31.05  ? 10  GLY   A CA    1 
ATOM   76    C  C     . GLY   A 1  10  ? 27.560  79.887  49.330  1.00 24.40  ? 10  GLY   A C     1 
ATOM   77    O  O     . GLY   A 1  10  ? 27.422  81.029  49.754  1.00 27.96  ? 10  GLY   A O     1 
ATOM   78    N  N     . GLN   A 1  11  ? 26.579  79.248  48.691  1.00 19.90  ? 11  GLN   A N     1 
ATOM   79    C  CA    . GLN   A 1  11  ? 25.337  79.967  48.418  1.00 24.74  ? 11  GLN   A CA    1 
ATOM   80    C  C     . GLN   A 1  11  ? 24.731  80.548  49.683  1.00 27.04  ? 11  GLN   A C     1 
ATOM   81    O  O     . GLN   A 1  11  ? 24.397  81.737  49.736  1.00 24.87  ? 11  GLN   A O     1 
ATOM   82    C  CB    . GLN   A 1  11  ? 24.310  79.074  47.744  1.00 31.00  ? 11  GLN   A CB    1 
ATOM   83    C  CG    . GLN   A 1  11  ? 22.998  79.799  47.511  1.00 27.14  ? 11  GLN   A CG    1 
ATOM   84    C  CD    . GLN   A 1  11  ? 22.005  78.934  46.763  1.00 30.02  ? 11  GLN   A CD    1 
ATOM   85    O  OE1   . GLN   A 1  11  ? 20.993  78.514  47.316  1.00 27.35  ? 11  GLN   A OE1   1 
ATOM   86    N  NE2   . GLN   A 1  11  ? 22.287  78.668  45.490  1.00 46.11  ? 11  GLN   A NE2   1 
ATOM   87    N  N     . ALA   A 1  12  ? 24.566  79.709  50.714  1.00 27.56  ? 12  ALA   A N     1 
ATOM   88    C  CA    . ALA   A 1  12  ? 23.858  80.137  51.918  1.00 20.12  ? 12  ALA   A CA    1 
ATOM   89    C  C     . ALA   A 1  12  ? 24.567  81.295  52.588  1.00 24.48  ? 12  ALA   A C     1 
ATOM   90    O  O     . ALA   A 1  12  ? 23.947  82.320  52.897  1.00 35.07  ? 12  ALA   A O     1 
ATOM   91    C  CB    . ALA   A 1  12  ? 23.699  78.973  52.896  1.00 24.68  ? 12  ALA   A CB    1 
ATOM   92    N  N     . GLY   A 1  13  ? 25.874  81.157  52.820  1.00 28.75  ? 13  GLY   A N     1 
ATOM   93    C  CA    . GLY   A 1  13  ? 26.604  82.227  53.485  1.00 29.62  ? 13  GLY   A CA    1 
ATOM   94    C  C     . GLY   A 1  13  ? 26.539  83.534  52.720  1.00 28.75  ? 13  GLY   A C     1 
ATOM   95    O  O     . GLY   A 1  13  ? 26.438  84.608  53.316  1.00 24.52  ? 13  GLY   A O     1 
ATOM   96    N  N     . VAL   A 1  14  ? 26.584  83.451  51.384  1.00 30.54  ? 14  VAL   A N     1 
ATOM   97    C  CA    . VAL   A 1  14  ? 26.592  84.635  50.536  1.00 24.64  ? 14  VAL   A CA    1 
ATOM   98    C  C     . VAL   A 1  14  ? 25.220  85.280  50.520  1.00 24.45  ? 14  VAL   A C     1 
ATOM   99    O  O     . VAL   A 1  14  ? 25.101  86.505  50.596  1.00 22.70  ? 14  VAL   A O     1 
ATOM   100   C  CB    . VAL   A 1  14  ? 27.082  84.270  49.120  1.00 20.93  ? 14  VAL   A CB    1 
ATOM   101   C  CG1   . VAL   A 1  14  ? 26.813  85.386  48.118  1.00 21.06  ? 14  VAL   A CG1   1 
ATOM   102   C  CG2   . VAL   A 1  14  ? 28.530  83.990  49.165  1.00 21.67  ? 14  VAL   A CG2   1 
ATOM   103   N  N     . GLN   A 1  15  ? 24.158  84.477  50.443  1.00 27.28  ? 15  GLN   A N     1 
ATOM   104   C  CA    . GLN   A 1  15  ? 22.825  85.075  50.480  1.00 29.97  ? 15  GLN   A CA    1 
ATOM   105   C  C     . GLN   A 1  15  ? 22.514  85.628  51.870  1.00 31.55  ? 15  GLN   A C     1 
ATOM   106   O  O     . GLN   A 1  15  ? 21.845  86.667  51.994  1.00 26.49  ? 15  GLN   A O     1 
ATOM   107   C  CB    . GLN   A 1  15  ? 21.759  84.070  50.041  1.00 23.14  ? 15  GLN   A CB    1 
ATOM   108   C  CG    . GLN   A 1  15  ? 21.987  83.494  48.656  1.00 25.86  ? 15  GLN   A CG    1 
ATOM   109   C  CD    . GLN   A 1  15  ? 20.711  83.027  47.978  1.00 29.08  ? 15  GLN   A CD    1 
ATOM   110   O  OE1   . GLN   A 1  15  ? 19.856  82.376  48.595  1.00 29.14  ? 15  GLN   A OE1   1 
ATOM   111   N  NE2   . GLN   A 1  15  ? 20.567  83.370  46.696  1.00 30.22  ? 15  GLN   A NE2   1 
ATOM   112   N  N     . ILE   A 1  16  ? 22.999  84.965  52.927  1.00 23.36  ? 16  ILE   A N     1 
ATOM   113   C  CA    . ILE   A 1  16  ? 22.825  85.539  54.252  1.00 26.21  ? 16  ILE   A CA    1 
ATOM   114   C  C     . ILE   A 1  16  ? 23.646  86.820  54.382  1.00 30.99  ? 16  ILE   A C     1 
ATOM   115   O  O     . ILE   A 1  16  ? 23.185  87.818  54.952  1.00 29.24  ? 16  ILE   A O     1 
ATOM   116   C  CB    . ILE   A 1  16  ? 23.162  84.505  55.330  1.00 27.99  ? 16  ILE   A CB    1 
ATOM   117   C  CG1   . ILE   A 1  16  ? 22.013  83.521  55.444  1.00 20.52  ? 16  ILE   A CG1   1 
ATOM   118   C  CG2   . ILE   A 1  16  ? 23.376  85.187  56.673  1.00 24.88  ? 16  ILE   A CG2   1 
ATOM   119   C  CD1   . ILE   A 1  16  ? 22.358  82.340  56.243  1.00 20.65  ? 16  ILE   A CD1   1 
ATOM   120   N  N     . GLY   A 1  17  ? 24.845  86.831  53.806  1.00 32.50  ? 17  GLY   A N     1 
ATOM   121   C  CA    . GLY   A 1  17  ? 25.651  88.032  53.686  1.00 31.13  ? 17  GLY   A CA    1 
ATOM   122   C  C     . GLY   A 1  17  ? 24.910  89.289  53.260  1.00 33.30  ? 17  GLY   A C     1 
ATOM   123   O  O     . GLY   A 1  17  ? 24.920  90.288  53.985  1.00 42.05  ? 17  GLY   A O     1 
ATOM   124   N  N     . ASN   A 1  18  ? 24.287  89.291  52.087  1.00 27.72  ? 18  ASN   A N     1 
ATOM   125   C  CA    . ASN   A 1  18  ? 23.606  90.511  51.680  1.00 33.02  ? 18  ASN   A CA    1 
ATOM   126   C  C     . ASN   A 1  18  ? 22.472  90.829  52.626  1.00 37.02  ? 18  ASN   A C     1 
ATOM   127   O  O     . ASN   A 1  18  ? 22.097  91.996  52.784  1.00 36.09  ? 18  ASN   A O     1 
ATOM   128   C  CB    . ASN   A 1  18  ? 23.064  90.386  50.263  1.00 37.74  ? 18  ASN   A CB    1 
ATOM   129   C  CG    . ASN   A 1  18  ? 23.953  89.583  49.394  1.00 30.82  ? 18  ASN   A CG    1 
ATOM   130   O  OD1   . ASN   A 1  18  ? 24.988  90.061  48.930  1.00 41.87  ? 18  ASN   A OD1   1 
ATOM   131   N  ND2   . ASN   A 1  18  ? 23.566  88.337  49.163  1.00 35.13  ? 18  ASN   A ND2   1 
ATOM   132   N  N     . ALA   A 1  19  ? 21.885  89.800  53.230  1.00 34.74  ? 19  ALA   A N     1 
ATOM   133   C  CA    . ALA   A 1  19  ? 20.841  90.049  54.207  1.00 35.07  ? 19  ALA   A CA    1 
ATOM   134   C  C     . ALA   A 1  19  ? 21.391  90.887  55.352  1.00 37.36  ? 19  ALA   A C     1 
ATOM   135   O  O     . ALA   A 1  19  ? 20.815  91.911  55.732  1.00 36.47  ? 19  ALA   A O     1 
ATOM   136   C  CB    . ALA   A 1  19  ? 20.275  88.717  54.696  1.00 28.61  ? 19  ALA   A CB    1 
ATOM   137   N  N     . CYS   A 1  20  ? 22.537  90.487  55.887  1.00 29.83  ? 20  CYS   A N     1 
ATOM   138   C  CA    . CYS   A 1  20  ? 23.162  91.288  56.919  1.00 30.86  ? 20  CYS   A CA    1 
ATOM   139   C  C     . CYS   A 1  20  ? 23.634  92.619  56.355  1.00 31.77  ? 20  CYS   A C     1 
ATOM   140   O  O     . CYS   A 1  20  ? 23.216  93.684  56.818  1.00 34.59  ? 20  CYS   A O     1 
ATOM   141   C  CB    . CYS   A 1  20  ? 24.305  90.500  57.555  1.00 21.94  ? 20  CYS   A CB    1 
ATOM   142   S  SG    . CYS   A 1  20  ? 23.649  88.985  58.280  1.00 30.67  ? 20  CYS   A SG    1 
ATOM   143   N  N     . TRP   A 1  21  ? 24.488  92.583  55.334  1.00 31.47  ? 21  TRP   A N     1 
ATOM   144   C  CA    . TRP   A 1  21  ? 25.133  93.812  54.890  1.00 27.21  ? 21  TRP   A CA    1 
ATOM   145   C  C     . TRP   A 1  21  ? 24.121  94.864  54.475  1.00 32.16  ? 21  TRP   A C     1 
ATOM   146   O  O     . TRP   A 1  21  ? 24.382  96.057  54.646  1.00 35.94  ? 21  TRP   A O     1 
ATOM   147   C  CB    . TRP   A 1  21  ? 26.123  93.512  53.777  1.00 26.37  ? 21  TRP   A CB    1 
ATOM   148   C  CG    . TRP   A 1  21  ? 27.370  92.993  54.356  1.00 36.08  ? 21  TRP   A CG    1 
ATOM   149   C  CD1   . TRP   A 1  21  ? 27.848  91.717  54.289  1.00 36.04  ? 21  TRP   A CD1   1 
ATOM   150   C  CD2   . TRP   A 1  21  ? 28.290  93.727  55.172  1.00 33.02  ? 21  TRP   A CD2   1 
ATOM   151   N  NE1   . TRP   A 1  21  ? 29.023  91.618  54.998  1.00 33.53  ? 21  TRP   A NE1   1 
ATOM   152   C  CE2   . TRP   A 1  21  ? 29.316  92.838  55.547  1.00 30.44  ? 21  TRP   A CE2   1 
ATOM   153   C  CE3   . TRP   A 1  21  ? 28.348  95.050  55.611  1.00 29.70  ? 21  TRP   A CE3   1 
ATOM   154   C  CZ2   . TRP   A 1  21  ? 30.392  93.234  56.331  1.00 35.46  ? 21  TRP   A CZ2   1 
ATOM   155   C  CZ3   . TRP   A 1  21  ? 29.408  95.437  56.397  1.00 36.76  ? 21  TRP   A CZ3   1 
ATOM   156   C  CH2   . TRP   A 1  21  ? 30.417  94.537  56.750  1.00 33.87  ? 21  TRP   A CH2   1 
ATOM   157   N  N     . GLU   A 1  22  ? 22.955  94.453  53.971  1.00 33.21  ? 22  GLU   A N     1 
ATOM   158   C  CA    . GLU   A 1  22  ? 21.887  95.407  53.692  1.00 34.03  ? 22  GLU   A CA    1 
ATOM   159   C  C     . GLU   A 1  22  ? 21.404  96.056  54.983  1.00 42.46  ? 22  GLU   A C     1 
ATOM   160   O  O     . GLU   A 1  22  ? 21.448  97.282  55.139  1.00 42.42  ? 22  GLU   A O     1 
ATOM   161   C  CB    . GLU   A 1  22  ? 20.730  94.708  52.985  1.00 35.46  ? 22  GLU   A CB    1 
ATOM   162   C  CG    . GLU   A 1  22  ? 19.454  95.512  52.969  1.00 39.96  ? 22  GLU   A CG    1 
ATOM   163   C  CD    . GLU   A 1  22  ? 18.255  94.730  52.423  1.00 55.28  ? 22  GLU   A CD    1 
ATOM   164   O  OE1   . GLU   A 1  22  ? 18.085  93.525  52.749  1.00 58.08  ? 22  GLU   A OE1   1 
ATOM   165   O  OE2   . GLU   A 1  22  ? 17.474  95.338  51.660  1.00 62.31  ? 22  GLU   A OE2   1 
ATOM   166   N  N     . LEU   A 1  23  ? 20.963  95.229  55.932  1.00 40.83  ? 23  LEU   A N     1 
ATOM   167   C  CA    . LEU   A 1  23  ? 20.544  95.701  57.245  1.00 34.37  ? 23  LEU   A CA    1 
ATOM   168   C  C     . LEU   A 1  23  ? 21.591  96.617  57.879  1.00 34.82  ? 23  LEU   A C     1 
ATOM   169   O  O     . LEU   A 1  23  ? 21.288  97.760  58.235  1.00 35.08  ? 23  LEU   A O     1 
ATOM   170   C  CB    . LEU   A 1  23  ? 20.261  94.493  58.131  1.00 28.64  ? 23  LEU   A CB    1 
ATOM   171   C  CG    . LEU   A 1  23  ? 19.537  94.800  59.421  1.00 31.60  ? 23  LEU   A CG    1 
ATOM   172   C  CD1   . LEU   A 1  23  ? 18.194  95.465  59.136  1.00 38.02  ? 23  LEU   A CD1   1 
ATOM   173   C  CD2   . LEU   A 1  23  ? 19.367  93.516  60.177  1.00 32.83  ? 23  LEU   A CD2   1 
ATOM   174   N  N     . TYR   A 1  24  ? 22.830  96.123  58.042  1.00 32.64  ? 24  TYR   A N     1 
ATOM   175   C  CA    . TYR   A 1  24  ? 23.938  96.959  58.513  1.00 33.44  ? 24  TYR   A CA    1 
ATOM   176   C  C     . TYR   A 1  24  ? 23.922  98.351  57.875  1.00 46.52  ? 24  TYR   A C     1 
ATOM   177   O  O     . TYR   A 1  24  ? 24.166  99.373  58.535  1.00 37.27  ? 24  TYR   A O     1 
ATOM   178   C  CB    . TYR   A 1  24  ? 25.281  96.291  58.203  1.00 29.06  ? 24  TYR   A CB    1 
ATOM   179   C  CG    . TYR   A 1  24  ? 25.609  95.038  58.973  1.00 33.81  ? 24  TYR   A CG    1 
ATOM   180   C  CD1   . TYR   A 1  24  ? 24.943  94.715  60.144  1.00 31.24  ? 24  TYR   A CD1   1 
ATOM   181   C  CD2   . TYR   A 1  24  ? 26.617  94.186  58.534  1.00 30.42  ? 24  TYR   A CD2   1 
ATOM   182   C  CE1   . TYR   A 1  24  ? 25.254  93.559  60.847  1.00 28.83  ? 24  TYR   A CE1   1 
ATOM   183   C  CE2   . TYR   A 1  24  ? 26.931  93.032  59.225  1.00 32.69  ? 24  TYR   A CE2   1 
ATOM   184   C  CZ    . TYR   A 1  24  ? 26.251  92.726  60.384  1.00 28.86  ? 24  TYR   A CZ    1 
ATOM   185   O  OH    . TYR   A 1  24  ? 26.563  91.577  61.075  1.00 30.31  ? 24  TYR   A OH    1 
ATOM   186   N  N     . CYS   A 1  25  ? 23.676  98.400  56.567  1.00 43.87  ? 25  CYS   A N     1 
ATOM   187   C  CA    . CYS   A 1  25  ? 23.675  99.681  55.879  1.00 35.01  ? 25  CYS   A CA    1 
ATOM   188   C  C     . CYS   A 1  25  ? 22.532  100.561 56.377  1.00 39.39  ? 25  CYS   A C     1 
ATOM   189   O  O     . CYS   A 1  25  ? 22.725  101.751 56.651  1.00 42.43  ? 25  CYS   A O     1 
ATOM   190   C  CB    . CYS   A 1  25  ? 23.605  99.453  54.365  1.00 35.54  ? 25  CYS   A CB    1 
ATOM   191   S  SG    . CYS   A 1  25  ? 25.261  99.110  53.608  1.00 43.48  ? 25  CYS   A SG    1 
ATOM   192   N  N     . LEU   A 1  26  ? 21.335  99.981  56.523  1.00 39.28  ? 26  LEU   A N     1 
ATOM   193   C  CA    . LEU   A 1  26  ? 20.185  100.715 57.051  1.00 39.61  ? 26  LEU   A CA    1 
ATOM   194   C  C     . LEU   A 1  26  ? 20.438  101.224 58.465  1.00 42.17  ? 26  LEU   A C     1 
ATOM   195   O  O     . LEU   A 1  26  ? 20.035  102.337 58.815  1.00 46.49  ? 26  LEU   A O     1 
ATOM   196   C  CB    . LEU   A 1  26  ? 18.952  99.815  57.048  1.00 36.83  ? 26  LEU   A CB    1 
ATOM   197   C  CG    . LEU   A 1  26  ? 18.472  99.389  55.673  1.00 34.92  ? 26  LEU   A CG    1 
ATOM   198   C  CD1   . LEU   A 1  26  ? 17.115  98.693  55.768  1.00 39.31  ? 26  LEU   A CD1   1 
ATOM   199   C  CD2   . LEU   A 1  26  ? 18.410  100.611 54.807  1.00 25.41  ? 26  LEU   A CD2   1 
ATOM   200   N  N     . GLU   A 1  27  ? 21.080  100.410 59.298  1.00 41.37  ? 27  GLU   A N     1 
ATOM   201   C  CA    . GLU   A 1  27  ? 21.264  100.776 60.694  1.00 36.22  ? 27  GLU   A CA    1 
ATOM   202   C  C     . GLU   A 1  27  ? 22.252  101.928 60.836  1.00 39.96  ? 27  GLU   A C     1 
ATOM   203   O  O     . GLU   A 1  27  ? 21.988  102.896 61.560  1.00 39.42  ? 27  GLU   A O     1 
ATOM   204   C  CB    . GLU   A 1  27  ? 21.735  99.558  61.479  1.00 37.10  ? 27  GLU   A CB    1 
ATOM   205   C  CG    . GLU   A 1  27  ? 20.742  98.394  61.540  1.00 33.59  ? 27  GLU   A CG    1 
ATOM   206   C  CD    . GLU   A 1  27  ? 21.274  97.277  62.432  1.00 34.70  ? 27  GLU   A CD    1 
ATOM   207   O  OE1   . GLU   A 1  27  ? 22.496  97.292  62.718  1.00 34.16  ? 27  GLU   A OE1   1 
ATOM   208   O  OE2   . GLU   A 1  27  ? 20.484  96.409  62.868  1.00 31.00  ? 27  GLU   A OE2   1 
ATOM   209   N  N     . HIS   A 1  28  ? 23.404  101.836 60.161  1.00 40.51  ? 28  HIS   A N     1 
ATOM   210   C  CA    . HIS   A 1  28  ? 24.421  102.884 60.201  1.00 34.90  ? 28  HIS   A CA    1 
ATOM   211   C  C     . HIS   A 1  28  ? 24.138  104.035 59.247  1.00 40.82  ? 28  HIS   A C     1 
ATOM   212   O  O     . HIS   A 1  28  ? 24.988  104.929 59.130  1.00 37.00  ? 28  HIS   A O     1 
ATOM   213   C  CB    . HIS   A 1  28  ? 25.803  102.326 59.871  1.00 27.70  ? 28  HIS   A CB    1 
ATOM   214   C  CG    . HIS   A 1  28  ? 26.295  101.304 60.838  1.00 33.32  ? 28  HIS   A CG    1 
ATOM   215   N  ND1   . HIS   A 1  28  ? 26.576  101.602 62.151  1.00 32.85  ? 28  HIS   A ND1   1 
ATOM   216   C  CD2   . HIS   A 1  28  ? 26.593  99.994  60.675  1.00 32.86  ? 28  HIS   A CD2   1 
ATOM   217   C  CE1   . HIS   A 1  28  ? 27.009  100.514 62.762  1.00 35.54  ? 28  HIS   A CE1   1 
ATOM   218   N  NE2   . HIS   A 1  28  ? 27.024  99.523  61.890  1.00 32.61  ? 28  HIS   A NE2   1 
ATOM   219   N  N     . GLY   A 1  29  ? 22.987  104.033 58.563  1.00 37.21  ? 29  GLY   A N     1 
ATOM   220   C  CA    . GLY   A 1  29  ? 22.647  105.080 57.609  1.00 38.08  ? 29  GLY   A CA    1 
ATOM   221   C  C     . GLY   A 1  29  ? 23.637  105.225 56.463  1.00 44.66  ? 29  GLY   A C     1 
ATOM   222   O  O     . GLY   A 1  29  ? 24.102  106.331 56.160  1.00 50.63  ? 29  GLY   A O     1 
ATOM   223   N  N     . ILE   A 1  30  ? 23.984  104.099 55.837  1.00 43.35  ? 30  ILE   A N     1 
ATOM   224   C  CA    . ILE   A 1  30  ? 24.830  104.057 54.650  1.00 44.15  ? 30  ILE   A CA    1 
ATOM   225   C  C     . ILE   A 1  30  ? 23.927  103.794 53.457  1.00 40.64  ? 30  ILE   A C     1 
ATOM   226   O  O     . ILE   A 1  30  ? 22.882  103.158 53.580  1.00 39.34  ? 30  ILE   A O     1 
ATOM   227   C  CB    . ILE   A 1  30  ? 25.935  102.985 54.782  1.00 35.28  ? 30  ILE   A CB    1 
ATOM   228   C  CG1   . ILE   A 1  30  ? 26.821  103.304 55.986  1.00 31.51  ? 30  ILE   A CG1   1 
ATOM   229   C  CG2   . ILE   A 1  30  ? 26.728  102.815 53.483  1.00 30.47  ? 30  ILE   A CG2   1 
ATOM   230   C  CD1   . ILE   A 1  30  ? 28.018  102.344 56.160  1.00 35.59  ? 30  ILE   A CD1   1 
ATOM   231   N  N     . GLN   A 1  31  ? 24.307  104.304 52.301  1.00 54.67  ? 31  GLN   A N     1 
ATOM   232   C  CA    . GLN   A 1  31  ? 23.455  104.164 51.133  1.00 56.30  ? 31  GLN   A CA    1 
ATOM   233   C  C     . GLN   A 1  31  ? 24.009  103.125 50.169  1.00 56.32  ? 31  GLN   A C     1 
ATOM   234   O  O     . GLN   A 1  31  ? 25.173  102.725 50.270  1.00 55.69  ? 31  GLN   A O     1 
ATOM   235   C  CB    . GLN   A 1  31  ? 23.303  105.511 50.428  1.00 54.34  ? 31  GLN   A CB    1 
ATOM   236   C  CG    . GLN   A 1  31  ? 22.280  106.407 51.099  1.00 59.74  ? 31  GLN   A CG    1 
ATOM   237   C  CD    . GLN   A 1  31  ? 22.691  107.870 51.072  1.00 73.46  ? 31  GLN   A CD    1 
ATOM   238   O  OE1   . GLN   A 1  31  ? 23.786  108.210 50.602  1.00 63.55  ? 31  GLN   A OE1   1 
ATOM   239   N  NE2   . GLN   A 1  31  ? 21.817  108.746 51.581  1.00 70.90  ? 31  GLN   A NE2   1 
ATOM   240   N  N     . PRO   A 1  32  ? 23.197  102.658 49.216  1.00 61.59  ? 32  PRO   A N     1 
ATOM   241   C  CA    . PRO   A 1  32  ? 23.663  101.581 48.323  1.00 63.49  ? 32  PRO   A CA    1 
ATOM   242   C  C     . PRO   A 1  32  ? 24.965  101.898 47.585  1.00 66.37  ? 32  PRO   A C     1 
ATOM   243   O  O     . PRO   A 1  32  ? 25.556  100.968 47.013  1.00 64.83  ? 32  PRO   A O     1 
ATOM   244   C  CB    . PRO   A 1  32  ? 22.493  101.399 47.349  1.00 59.20  ? 32  PRO   A CB    1 
ATOM   245   C  CG    . PRO   A 1  32  ? 21.286  101.918 48.120  1.00 54.30  ? 32  PRO   A CG    1 
ATOM   246   C  CD    . PRO   A 1  32  ? 21.813  103.068 48.925  1.00 54.18  ? 32  PRO   A CD    1 
ATOM   247   N  N     . ASP   A 1  33  ? 25.456  103.148 47.616  1.00 57.26  ? 33  ASP   A N     1 
ATOM   248   C  CA    . ASP   A 1  33  ? 26.711  103.497 46.958  1.00 52.39  ? 33  ASP   A CA    1 
ATOM   249   C  C     . ASP   A 1  33  ? 27.847  103.775 47.941  1.00 57.42  ? 33  ASP   A C     1 
ATOM   250   O  O     . ASP   A 1  33  ? 28.839  104.402 47.558  1.00 57.10  ? 33  ASP   A O     1 
ATOM   251   C  CB    . ASP   A 1  33  ? 26.519  104.696 46.032  1.00 50.91  ? 33  ASP   A CB    1 
ATOM   252   C  CG    . ASP   A 1  33  ? 26.070  105.928 46.766  1.00 54.75  ? 33  ASP   A CG    1 
ATOM   253   O  OD1   . ASP   A 1  33  ? 25.867  105.821 47.993  1.00 56.76  ? 33  ASP   A OD1   1 
ATOM   254   O  OD2   . ASP   A 1  33  ? 25.921  107.002 46.124  1.00 52.53  ? 33  ASP   A OD2   1 
ATOM   255   N  N     . GLY   A 1  34  ? 27.727  103.324 49.198  1.00 50.58  ? 34  GLY   A N     1 
ATOM   256   C  CA    . GLY   A 1  34  ? 28.760  103.517 50.205  1.00 54.95  ? 34  GLY   A CA    1 
ATOM   257   C  C     . GLY   A 1  34  ? 28.760  104.868 50.900  1.00 55.75  ? 34  GLY   A C     1 
ATOM   258   O  O     . GLY   A 1  34  ? 29.567  105.078 51.823  1.00 45.35  ? 34  GLY   A O     1 
ATOM   259   N  N     . GLN   A 1  35  ? 27.894  105.789 50.480  1.00 59.13  ? 35  GLN   A N     1 
ATOM   260   C  CA    . GLN   A 1  35  ? 27.818  107.113 51.082  1.00 57.49  ? 35  GLN   A CA    1 
ATOM   261   C  C     . GLN   A 1  35  ? 27.107  107.040 52.428  1.00 60.41  ? 35  GLN   A C     1 
ATOM   262   O  O     . GLN   A 1  35  ? 26.137  106.293 52.592  1.00 55.23  ? 35  GLN   A O     1 
ATOM   263   C  CB    . GLN   A 1  35  ? 27.077  108.073 50.149  1.00 45.21  ? 35  GLN   A CB    1 
ATOM   264   C  CG    . GLN   A 1  35  ? 27.865  108.494 48.952  1.00 37.69  ? 35  GLN   A CG    1 
ATOM   265   C  CD    . GLN   A 1  35  ? 29.078  109.316 49.331  1.00 52.84  ? 35  GLN   A CD    1 
ATOM   266   O  OE1   . GLN   A 1  35  ? 29.064  110.537 49.225  1.00 63.34  ? 35  GLN   A OE1   1 
ATOM   267   N  NE2   . GLN   A 1  35  ? 30.133  108.651 49.783  1.00 56.08  ? 35  GLN   A NE2   1 
ATOM   268   N  N     . MET   A 1  36  ? 27.589  107.828 53.390  1.00 55.36  ? 36  MET   A N     1 
ATOM   269   C  CA    . MET   A 1  36  ? 27.055  107.840 54.752  1.00 46.70  ? 36  MET   A CA    1 
ATOM   270   C  C     . MET   A 1  36  ? 27.097  109.272 55.252  1.00 56.26  ? 36  MET   A C     1 
ATOM   271   O  O     . MET   A 1  36  ? 27.981  109.645 56.033  1.00 60.61  ? 36  MET   A O     1 
ATOM   272   C  CB    . MET   A 1  36  ? 27.870  106.913 55.657  1.00 49.49  ? 36  MET   A CB    1 
ATOM   273   C  CG    . MET   A 1  36  ? 27.467  106.838 57.126  1.00 50.51  ? 36  MET   A CG    1 
ATOM   274   S  SD    . MET   A 1  36  ? 28.852  106.133 58.068  1.00 54.44  ? 36  MET   A SD    1 
ATOM   275   C  CE    . MET   A 1  36  ? 28.056  105.715 59.612  1.00 48.32  ? 36  MET   A CE    1 
ATOM   276   N  N     . PRO   A 1  37  ? 26.143  110.120 54.812  1.00 51.90  ? 37  PRO   A N     1 
ATOM   277   C  CA    . PRO   A 1  37  ? 26.139  111.539 55.222  1.00 53.78  ? 37  PRO   A CA    1 
ATOM   278   C  C     . PRO   A 1  37  ? 26.492  111.785 56.685  1.00 60.50  ? 37  PRO   A C     1 
ATOM   279   O  O     . PRO   A 1  37  ? 27.162  112.770 57.015  1.00 59.76  ? 37  PRO   A O     1 
ATOM   280   C  CB    . PRO   A 1  37  ? 24.698  111.970 54.930  1.00 43.17  ? 37  PRO   A CB    1 
ATOM   281   C  CG    . PRO   A 1  37  ? 24.314  111.128 53.754  1.00 54.96  ? 37  PRO   A CG    1 
ATOM   282   C  CD    . PRO   A 1  37  ? 25.005  109.796 53.936  1.00 53.30  ? 37  PRO   A CD    1 
ATOM   283   N  N     . SER   A 1  38  ? 26.053  110.872 57.558  1.00 65.79  ? 38  SER   A N     1 
ATOM   284   C  CA    . SER   A 1  38  ? 26.221  111.032 59.001  1.00 55.33  ? 38  SER   A CA    1 
ATOM   285   C  C     . SER   A 1  38  ? 27.692  111.024 59.415  1.00 49.47  ? 38  SER   A C     1 
ATOM   286   O  O     . SER   A 1  38  ? 28.095  111.795 60.296  1.00 48.68  ? 38  SER   A O     1 
ATOM   287   C  CB    . SER   A 1  38  ? 25.450  109.925 59.718  1.00 60.01  ? 38  SER   A CB    1 
ATOM   288   O  OG    . SER   A 1  38  ? 24.516  109.322 58.825  1.00 63.48  ? 38  SER   A OG    1 
ATOM   289   N  N     . ASP   A 1  39  ? 28.508  110.147 58.822  1.00 54.08  ? 39  ASP   A N     1 
ATOM   290   C  CA    . ASP   A 1  39  ? 29.938  110.192 59.107  1.00 52.45  ? 39  ASP   A CA    1 
ATOM   291   C  C     . ASP   A 1  39  ? 30.463  111.532 58.653  1.00 59.18  ? 39  ASP   A C     1 
ATOM   292   O  O     . ASP   A 1  39  ? 30.244  111.940 57.507  1.00 62.38  ? 39  ASP   A O     1 
ATOM   293   C  CB    . ASP   A 1  39  ? 30.719  109.062 58.423  1.00 48.08  ? 39  ASP   A CB    1 
ATOM   294   C  CG    . ASP   A 1  39  ? 32.236  109.214 58.595  1.00 54.26  ? 39  ASP   A CG    1 
ATOM   295   O  OD1   . ASP   A 1  39  ? 32.751  110.241 58.146  1.00 60.87  ? 39  ASP   A OD1   1 
ATOM   296   O  OD2   . ASP   A 1  39  ? 32.927  108.345 59.177  1.00 47.35  ? 39  ASP   A OD2   1 
ATOM   297   N  N     . LYS   A 1  40  ? 31.136  112.229 59.559  1.00 60.82  ? 40  LYS   A N     1 
ATOM   298   C  CA    . LYS   A 1  40  ? 31.828  113.447 59.187  1.00 56.56  ? 40  LYS   A CA    1 
ATOM   299   C  C     . LYS   A 1  40  ? 33.325  113.223 58.984  1.00 60.88  ? 40  LYS   A C     1 
ATOM   300   O  O     . LYS   A 1  40  ? 33.973  114.030 58.311  1.00 71.23  ? 40  LYS   A O     1 
ATOM   301   C  CB    . LYS   A 1  40  ? 31.560  114.528 60.238  1.00 43.16  ? 40  LYS   A CB    1 
ATOM   302   C  CG    . LYS   A 1  40  ? 30.065  114.817 60.450  1.00 44.10  ? 40  LYS   A CG    1 
ATOM   303   C  CD    . LYS   A 1  40  ? 29.410  115.290 59.151  1.00 49.68  ? 40  LYS   A CD    1 
ATOM   304   C  CE    . LYS   A 1  40  ? 28.074  116.022 59.355  1.00 37.31  ? 40  LYS   A CE    1 
ATOM   305   N  NZ    . LYS   A 1  40  ? 26.914  115.180 59.758  1.00 38.81  ? 40  LYS   A NZ    1 
ATOM   306   N  N     . THR   A 1  41  ? 33.871  112.122 59.506  1.00 57.47  ? 41  THR   A N     1 
ATOM   307   C  CA    . THR   A 1  41  ? 35.227  111.641 59.223  1.00 56.34  ? 41  THR   A CA    1 
ATOM   308   C  C     . THR   A 1  41  ? 35.340  111.173 57.767  1.00 68.10  ? 41  THR   A C     1 
ATOM   309   O  O     . THR   A 1  41  ? 35.336  109.970 57.482  1.00 70.02  ? 41  THR   A O     1 
ATOM   310   C  CB    . THR   A 1  41  ? 35.540  110.475 60.158  1.00 68.58  ? 41  THR   A CB    1 
ATOM   311   O  OG1   . THR   A 1  41  ? 35.036  109.247 59.577  1.00 59.38  ? 41  THR   A OG1   1 
ATOM   312   C  CG2   . THR   A 1  41  ? 34.882  110.681 61.525  1.00 62.27  ? 41  THR   A CG2   1 
ATOM   313   N  N     . ILE   A 1  42  ? 35.471  112.123 56.834  1.00 62.98  ? 42  ILE   A N     1 
ATOM   314   C  CA    . ILE   A 1  42  ? 35.391  111.818 55.395  1.00 56.47  ? 42  ILE   A CA    1 
ATOM   315   C  C     . ILE   A 1  42  ? 36.700  111.198 54.910  1.00 47.20  ? 42  ILE   A C     1 
ATOM   316   O  O     . ILE   A 1  42  ? 37.691  111.896 54.716  1.00 37.21  ? 42  ILE   A O     1 
ATOM   317   C  CB    . ILE   A 1  42  ? 35.058  113.059 54.559  1.00 44.95  ? 42  ILE   A CB    1 
ATOM   318   C  CG1   . ILE   A 1  42  ? 33.613  113.518 54.758  1.00 51.47  ? 42  ILE   A CG1   1 
ATOM   319   C  CG2   . ILE   A 1  42  ? 35.299  112.748 53.121  1.00 37.50  ? 42  ILE   A CG2   1 
ATOM   320   C  CD1   . ILE   A 1  42  ? 33.474  114.731 55.657  1.00 54.92  ? 42  ILE   A CD1   1 
ATOM   321   N  N     . GLY   A 1  43  ? 36.694  109.898 54.648  1.00 60.96  ? 43  GLY   A N     1 
ATOM   322   C  CA    . GLY   A 1  43  ? 37.906  109.198 54.276  1.00 58.45  ? 43  GLY   A CA    1 
ATOM   323   C  C     . GLY   A 1  43  ? 38.553  108.414 55.398  1.00 59.50  ? 43  GLY   A C     1 
ATOM   324   O  O     . GLY   A 1  43  ? 39.657  107.886 55.201  1.00 54.43  ? 43  GLY   A O     1 
ATOM   325   N  N     . GLY   A 1  44  ? 37.901  108.320 56.560  1.00 60.60  ? 44  GLY   A N     1 
ATOM   326   C  CA    . GLY   A 1  44  ? 38.428  107.533 57.668  1.00 64.51  ? 44  GLY   A CA    1 
ATOM   327   C  C     . GLY   A 1  44  ? 37.689  107.807 58.964  1.00 56.33  ? 44  GLY   A C     1 
ATOM   328   O  O     . GLY   A 1  44  ? 36.491  108.123 58.964  1.00 47.35  ? 44  GLY   A O     1 
ATOM   329   N  N     . GLY   A 1  45  ? 38.421  107.675 60.060  1.00 50.77  ? 45  GLY   A N     1 
ATOM   330   C  CA    . GLY   A 1  45  ? 37.973  107.853 61.433  1.00 57.88  ? 45  GLY   A CA    1 
ATOM   331   C  C     . GLY   A 1  45  ? 37.899  106.504 62.125  1.00 61.07  ? 45  GLY   A C     1 
ATOM   332   O  O     . GLY   A 1  45  ? 37.445  105.515 61.539  1.00 64.17  ? 45  GLY   A O     1 
ATOM   333   N  N     . ASP   A 1  46  ? 38.357  106.447 63.376  1.00 60.70  ? 46  ASP   A N     1 
ATOM   334   C  CA    . ASP   A 1  46  ? 38.247  105.201 64.140  1.00 58.38  ? 46  ASP   A CA    1 
ATOM   335   C  C     . ASP   A 1  46  ? 36.985  105.199 65.006  1.00 58.39  ? 46  ASP   A C     1 
ATOM   336   O  O     . ASP   A 1  46  ? 37.037  105.055 66.227  1.00 74.98  ? 46  ASP   A O     1 
ATOM   337   C  CB    . ASP   A 1  46  ? 39.511  104.946 64.968  1.00 56.30  ? 46  ASP   A CB    1 
ATOM   338   C  CG    . ASP   A 1  46  ? 39.870  106.099 65.875  1.00 68.12  ? 46  ASP   A CG    1 
ATOM   339   O  OD1   . ASP   A 1  46  ? 39.109  107.087 65.905  1.00 74.46  ? 46  ASP   A OD1   1 
ATOM   340   O  OD2   . ASP   A 1  46  ? 40.918  106.017 66.562  1.00 65.64  ? 46  ASP   A OD2   1 
ATOM   341   N  N     . ASP   A 1  47  ? 35.828  105.337 64.347  1.00 45.03  ? 47  ASP   A N     1 
ATOM   342   C  CA    . ASP   A 1  47  ? 34.537  105.232 65.015  1.00 53.94  ? 47  ASP   A CA    1 
ATOM   343   C  C     . ASP   A 1  47  ? 34.148  103.763 65.191  1.00 54.83  ? 47  ASP   A C     1 
ATOM   344   O  O     . ASP   A 1  47  ? 34.683  102.871 64.536  1.00 50.03  ? 47  ASP   A O     1 
ATOM   345   C  CB    . ASP   A 1  47  ? 33.455  105.982 64.233  1.00 53.76  ? 47  ASP   A CB    1 
ATOM   346   C  CG    . ASP   A 1  47  ? 33.675  107.481 64.237  1.00 61.59  ? 47  ASP   A CG    1 
ATOM   347   O  OD1   . ASP   A 1  47  ? 34.372  107.978 65.150  1.00 61.76  ? 47  ASP   A OD1   1 
ATOM   348   O  OD2   . ASP   A 1  47  ? 33.152  108.167 63.335  1.00 69.24  ? 47  ASP   A OD2   1 
ATOM   349   N  N     . SER   A 1  48  ? 33.209  103.507 66.107  1.00 61.07  ? 48  SER   A N     1 
ATOM   350   C  CA    . SER   A 1  48  ? 32.871  102.115 66.395  1.00 43.87  ? 48  SER   A CA    1 
ATOM   351   C  C     . SER   A 1  48  ? 32.364  101.399 65.150  1.00 42.03  ? 48  SER   A C     1 
ATOM   352   O  O     . SER   A 1  48  ? 32.638  100.209 64.967  1.00 38.59  ? 48  SER   A O     1 
ATOM   353   C  CB    . SER   A 1  48  ? 31.847  102.027 67.532  1.00 37.64  ? 48  SER   A CB    1 
ATOM   354   O  OG    . SER   A 1  48  ? 32.413  102.383 68.797  1.00 49.10  ? 48  SER   A OG    1 
ATOM   355   N  N     . PHE   A 1  49  ? 31.654  102.105 64.268  1.00 47.88  ? 49  PHE   A N     1 
ATOM   356   C  CA    . PHE   A 1  49  ? 31.109  101.465 63.078  1.00 42.25  ? 49  PHE   A CA    1 
ATOM   357   C  C     . PHE   A 1  49  ? 32.152  101.242 61.994  1.00 44.38  ? 49  PHE   A C     1 
ATOM   358   O  O     . PHE   A 1  49  ? 31.841  100.612 60.980  1.00 42.78  ? 49  PHE   A O     1 
ATOM   359   C  CB    . PHE   A 1  49  ? 29.943  102.280 62.503  1.00 47.25  ? 49  PHE   A CB    1 
ATOM   360   C  CG    . PHE   A 1  49  ? 30.369  103.490 61.729  1.00 52.43  ? 49  PHE   A CG    1 
ATOM   361   C  CD1   . PHE   A 1  49  ? 30.829  103.371 60.425  1.00 57.79  ? 49  PHE   A CD1   1 
ATOM   362   C  CD2   . PHE   A 1  49  ? 30.295  104.747 62.295  1.00 51.86  ? 49  PHE   A CD2   1 
ATOM   363   C  CE1   . PHE   A 1  49  ? 31.233  104.475 59.710  1.00 57.63  ? 49  PHE   A CE1   1 
ATOM   364   C  CE2   . PHE   A 1  49  ? 30.690  105.854 61.584  1.00 61.45  ? 49  PHE   A CE2   1 
ATOM   365   C  CZ    . PHE   A 1  49  ? 31.163  105.718 60.290  1.00 61.68  ? 49  PHE   A CZ    1 
ATOM   366   N  N     . ASN   A 1  50  ? 33.369  101.754 62.156  1.00 49.10  ? 50  ASN   A N     1 
ATOM   367   C  CA    . ASN   A 1  50  ? 34.394  101.437 61.175  1.00 42.59  ? 50  ASN   A CA    1 
ATOM   368   C  C     . ASN   A 1  50  ? 34.837  99.991  61.264  1.00 37.96  ? 50  ASN   A C     1 
ATOM   369   O  O     . ASN   A 1  50  ? 35.455  99.496  60.325  1.00 49.04  ? 50  ASN   A O     1 
ATOM   370   C  CB    . ASN   A 1  50  ? 35.604  102.356 61.327  1.00 43.09  ? 50  ASN   A CB    1 
ATOM   371   C  CG    . ASN   A 1  50  ? 35.521  103.573 60.434  1.00 52.20  ? 50  ASN   A CG    1 
ATOM   372   O  OD1   . ASN   A 1  50  ? 34.518  104.282 60.426  1.00 55.08  ? 50  ASN   A OD1   1 
ATOM   373   N  ND2   . ASN   A 1  50  ? 36.570  103.811 59.658  1.00 61.48  ? 50  ASN   A ND2   1 
ATOM   374   N  N     . THR   A 1  51  ? 34.535  99.297  62.361  1.00 41.43  ? 51  THR   A N     1 
ATOM   375   C  CA    A THR   A 1  51  ? 34.974  97.909  62.482  0.31 44.26  ? 51  THR   A CA    1 
ATOM   376   C  CA    B THR   A 1  51  ? 34.936  97.898  62.507  0.69 44.37  ? 51  THR   A CA    1 
ATOM   377   C  C     . THR   A 1  51  ? 34.471  97.054  61.321  1.00 42.60  ? 51  THR   A C     1 
ATOM   378   O  O     . THR   A 1  51  ? 35.175  96.135  60.875  1.00 42.15  ? 51  THR   A O     1 
ATOM   379   C  CB    A THR   A 1  51  ? 34.519  97.327  63.824  0.31 41.37  ? 51  THR   A CB    1 
ATOM   380   C  CB    B THR   A 1  51  ? 34.368  97.342  63.816  0.69 41.34  ? 51  THR   A CB    1 
ATOM   381   O  OG1   A THR   A 1  51  ? 33.101  97.129  63.818  0.31 36.85  ? 51  THR   A OG1   1 
ATOM   382   O  OG1   B THR   A 1  51  ? 34.883  98.105  64.910  0.69 40.96  ? 51  THR   A OG1   1 
ATOM   383   C  CG2   A THR   A 1  51  ? 34.883  98.272  64.956  0.31 41.10  ? 51  THR   A CG2   1 
ATOM   384   C  CG2   B THR   A 1  51  ? 34.738  95.871  63.993  0.69 40.17  ? 51  THR   A CG2   1 
ATOM   385   N  N     . PHE   A 1  52  ? 33.283  97.353  60.801  1.00 37.43  ? 52  PHE   A N     1 
ATOM   386   C  CA    . PHE   A 1  52  ? 32.689  96.595  59.717  1.00 32.15  ? 52  PHE   A CA    1 
ATOM   387   C  C     . PHE   A 1  52  ? 32.786  97.288  58.377  1.00 37.05  ? 52  PHE   A C     1 
ATOM   388   O  O     . PHE   A 1  52  ? 32.717  96.605  57.355  1.00 44.54  ? 52  PHE   A O     1 
ATOM   389   C  CB    . PHE   A 1  52  ? 31.215  96.310  60.017  1.00 35.90  ? 52  PHE   A CB    1 
ATOM   390   C  CG    . PHE   A 1  52  ? 31.017  95.158  60.949  1.00 36.37  ? 52  PHE   A CG    1 
ATOM   391   C  CD1   . PHE   A 1  52  ? 31.763  95.059  62.113  1.00 38.03  ? 52  PHE   A CD1   1 
ATOM   392   C  CD2   . PHE   A 1  52  ? 30.118  94.159  60.656  1.00 33.60  ? 52  PHE   A CD2   1 
ATOM   393   C  CE1   . PHE   A 1  52  ? 31.589  94.003  62.966  1.00 36.75  ? 52  PHE   A CE1   1 
ATOM   394   C  CE2   . PHE   A 1  52  ? 29.947  93.096  61.503  1.00 31.76  ? 52  PHE   A CE2   1 
ATOM   395   C  CZ    . PHE   A 1  52  ? 30.681  93.016  62.655  1.00 34.47  ? 52  PHE   A CZ    1 
ATOM   396   N  N     . PHE   A 1  53  ? 32.928  98.615  58.345  1.00 36.92  ? 53  PHE   A N     1 
ATOM   397   C  CA    . PHE   A 1  53  ? 33.122  99.348  57.100  1.00 36.55  ? 53  PHE   A CA    1 
ATOM   398   C  C     . PHE   A 1  53  ? 34.445  100.099 57.125  1.00 39.70  ? 53  PHE   A C     1 
ATOM   399   O  O     . PHE   A 1  53  ? 34.821  100.663 58.156  1.00 44.31  ? 53  PHE   A O     1 
ATOM   400   C  CB    . PHE   A 1  53  ? 32.022  100.356 56.856  1.00 31.58  ? 53  PHE   A CB    1 
ATOM   401   C  CG    . PHE   A 1  53  ? 30.664  99.775  56.759  1.00 33.78  ? 53  PHE   A CG    1 
ATOM   402   C  CD1   . PHE   A 1  53  ? 29.966  99.409  57.885  1.00 38.75  ? 53  PHE   A CD1   1 
ATOM   403   C  CD2   . PHE   A 1  53  ? 30.045  99.660  55.540  1.00 41.67  ? 53  PHE   A CD2   1 
ATOM   404   C  CE1   . PHE   A 1  53  ? 28.673  98.905  57.787  1.00 38.86  ? 53  PHE   A CE1   1 
ATOM   405   C  CE2   . PHE   A 1  53  ? 28.753  99.154  55.437  1.00 41.02  ? 53  PHE   A CE2   1 
ATOM   406   C  CZ    . PHE   A 1  53  ? 28.070  98.778  56.559  1.00 33.68  ? 53  PHE   A CZ    1 
ATOM   407   N  N     . SER   A 1  54  ? 35.142  100.116 55.983  1.00 43.42  ? 54  SER   A N     1 
ATOM   408   C  CA    . SER   A 1  54  ? 36.246  101.037 55.724  1.00 42.74  ? 54  SER   A CA    1 
ATOM   409   C  C     . SER   A 1  54  ? 35.773  102.186 54.831  1.00 42.77  ? 54  SER   A C     1 
ATOM   410   O  O     . SER   A 1  54  ? 34.695  102.138 54.229  1.00 44.53  ? 54  SER   A O     1 
ATOM   411   C  CB    . SER   A 1  54  ? 37.434  100.316 55.081  1.00 40.79  ? 54  SER   A CB    1 
ATOM   412   O  OG    . SER   A 1  54  ? 37.023  99.476  54.014  1.00 52.29  ? 54  SER   A OG    1 
ATOM   413   N  N     . GLU   A 1  55  ? 36.586  103.236 54.757  1.00 46.85  ? 55  GLU   A N     1 
ATOM   414   C  CA    . GLU   A 1  55  ? 36.168  104.466 54.090  1.00 53.91  ? 55  GLU   A CA    1 
ATOM   415   C  C     . GLU   A 1  55  ? 37.056  104.768 52.885  1.00 47.98  ? 55  GLU   A C     1 
ATOM   416   O  O     . GLU   A 1  55  ? 38.279  104.569 52.929  1.00 38.24  ? 55  GLU   A O     1 
ATOM   417   C  CB    . GLU   A 1  55  ? 36.167  105.665 55.076  1.00 54.49  ? 55  GLU   A CB    1 
ATOM   418   C  CG    . GLU   A 1  55  ? 35.252  105.475 56.296  1.00 56.32  ? 55  GLU   A CG    1 
ATOM   419   C  CD    . GLU   A 1  55  ? 34.993  106.760 57.036  1.00 60.34  ? 55  GLU   A CD    1 
ATOM   420   O  OE1   . GLU   A 1  55  ? 35.006  107.814 56.380  1.00 65.60  ? 55  GLU   A OE1   1 
ATOM   421   O  OE2   . GLU   A 1  55  ? 34.784  106.730 58.262  1.00 55.71  ? 55  GLU   A OE2   1 
ATOM   422   N  N     . THR   A 1  56  ? 36.428  105.264 51.814  1.00 47.93  ? 56  THR   A N     1 
ATOM   423   C  CA    . THR   A 1  56  ? 37.126  105.660 50.594  1.00 56.63  ? 56  THR   A CA    1 
ATOM   424   C  C     . THR   A 1  56  ? 37.206  107.180 50.483  1.00 57.57  ? 56  THR   A C     1 
ATOM   425   O  O     . THR   A 1  56  ? 36.203  107.882 50.666  1.00 51.76  ? 56  THR   A O     1 
ATOM   426   C  CB    . THR   A 1  56  ? 36.445  105.090 49.337  1.00 52.79  ? 56  THR   A CB    1 
ATOM   427   O  OG1   . THR   A 1  56  ? 37.423  104.961 48.303  1.00 62.64  ? 56  THR   A OG1   1 
ATOM   428   C  CG2   . THR   A 1  56  ? 35.339  106.012 48.824  1.00 49.15  ? 56  THR   A CG2   1 
ATOM   429   N  N     . GLY   A 1  57  ? 38.402  107.679 50.155  1.00 57.96  ? 57  GLY   A N     1 
ATOM   430   C  CA    . GLY   A 1  57  ? 38.640  109.105 50.018  1.00 42.47  ? 57  GLY   A CA    1 
ATOM   431   C  C     . GLY   A 1  57  ? 37.510  109.874 49.358  1.00 56.23  ? 57  GLY   A C     1 
ATOM   432   O  O     . GLY   A 1  57  ? 37.377  111.084 49.568  1.00 58.28  ? 57  GLY   A O     1 
ATOM   433   N  N     . ALA   A 1  58  ? 36.706  109.186 48.539  1.00 64.25  ? 58  ALA   A N     1 
ATOM   434   C  CA    . ALA   A 1  58  ? 35.518  109.759 47.919  1.00 55.69  ? 58  ALA   A CA    1 
ATOM   435   C  C     . ALA   A 1  58  ? 34.304  109.688 48.823  1.00 63.19  ? 58  ALA   A C     1 
ATOM   436   O  O     . ALA   A 1  58  ? 33.229  110.142 48.416  1.00 68.29  ? 58  ALA   A O     1 
ATOM   437   C  CB    . ALA   A 1  58  ? 35.206  109.049 46.598  1.00 52.76  ? 58  ALA   A CB    1 
ATOM   438   N  N     . GLY   A 1  59  ? 34.448  109.117 50.023  1.00 55.37  ? 59  GLY   A N     1 
ATOM   439   C  CA    . GLY   A 1  59  ? 33.370  109.043 50.984  1.00 48.97  ? 59  GLY   A CA    1 
ATOM   440   C  C     . GLY   A 1  59  ? 32.569  107.766 50.950  1.00 55.94  ? 59  GLY   A C     1 
ATOM   441   O  O     . GLY   A 1  59  ? 31.593  107.646 51.701  1.00 70.56  ? 59  GLY   A O     1 
ATOM   442   N  N     . LYS   A 1  60  ? 32.932  106.815 50.099  1.00 59.38  ? 60  LYS   A N     1 
ATOM   443   C  CA    . LYS   A 1  60  ? 32.269  105.523 50.106  1.00 59.73  ? 60  LYS   A CA    1 
ATOM   444   C  C     . LYS   A 1  60  ? 32.762  104.702 51.292  1.00 53.52  ? 60  LYS   A C     1 
ATOM   445   O  O     . LYS   A 1  60  ? 33.965  104.664 51.585  1.00 38.78  ? 60  LYS   A O     1 
ATOM   446   C  CB    . LYS   A 1  60  ? 32.514  104.767 48.790  1.00 59.69  ? 60  LYS   A CB    1 
ATOM   447   C  CG    . LYS   A 1  60  ? 31.451  103.690 48.469  1.00 55.98  ? 60  LYS   A CG    1 
ATOM   448   C  CD    . LYS   A 1  60  ? 32.053  102.372 47.966  1.00 60.22  ? 60  LYS   A CD    1 
ATOM   449   C  CE    . LYS   A 1  60  ? 32.070  102.295 46.437  1.00 59.72  ? 60  LYS   A CE    1 
ATOM   450   N  NZ    . LYS   A 1  60  ? 32.535  100.959 45.961  1.00 59.86  ? 60  LYS   A NZ    1 
ATOM   451   N  N     . HIS   A 1  61  ? 31.804  104.072 51.987  1.00 57.56  ? 61  HIS   A N     1 
ATOM   452   C  CA    . HIS   A 1  61  ? 32.059  103.108 53.056  1.00 53.31  ? 61  HIS   A CA    1 
ATOM   453   C  C     . HIS   A 1  61  ? 31.894  101.701 52.498  1.00 47.19  ? 61  HIS   A C     1 
ATOM   454   O  O     . HIS   A 1  61  ? 30.817  101.351 52.004  1.00 49.35  ? 61  HIS   A O     1 
ATOM   455   C  CB    . HIS   A 1  61  ? 31.101  103.333 54.225  1.00 54.06  ? 61  HIS   A CB    1 
ATOM   456   C  CG    . HIS   A 1  61  ? 31.213  104.694 54.829  1.00 54.29  ? 61  HIS   A CG    1 
ATOM   457   N  ND1   . HIS   A 1  61  ? 30.711  105.822 54.216  1.00 52.49  ? 61  HIS   A ND1   1 
ATOM   458   C  CD2   . HIS   A 1  61  ? 31.798  105.115 55.975  1.00 58.10  ? 61  HIS   A CD2   1 
ATOM   459   C  CE1   . HIS   A 1  61  ? 30.968  106.877 54.967  1.00 57.94  ? 61  HIS   A CE1   1 
ATOM   460   N  NE2   . HIS   A 1  61  ? 31.627  106.475 56.041  1.00 61.58  ? 61  HIS   A NE2   1 
ATOM   461   N  N     . VAL   A 1  62  ? 32.944  100.898 52.592  1.00 41.96  ? 62  VAL   A N     1 
ATOM   462   C  CA    . VAL   A 1  62  ? 33.021  99.620  51.889  1.00 49.38  ? 62  VAL   A CA    1 
ATOM   463   C  C     . VAL   A 1  62  ? 33.112  98.495  52.914  1.00 46.31  ? 62  VAL   A C     1 
ATOM   464   O  O     . VAL   A 1  62  ? 34.064  98.465  53.705  1.00 46.08  ? 62  VAL   A O     1 
ATOM   465   C  CB    . VAL   A 1  62  ? 34.216  99.577  50.928  1.00 47.37  ? 62  VAL   A CB    1 
ATOM   466   C  CG1   . VAL   A 1  62  ? 34.564  98.131  50.622  1.00 44.83  ? 62  VAL   A CG1   1 
ATOM   467   C  CG2   . VAL   A 1  62  ? 33.888  100.363 49.654  1.00 47.84  ? 62  VAL   A CG2   1 
ATOM   468   N  N     . PRO   A 1  63  ? 32.177  97.547  52.921  1.00 34.62  ? 63  PRO   A N     1 
ATOM   469   C  CA    . PRO   A 1  63  ? 32.240  96.456  53.892  1.00 34.14  ? 63  PRO   A CA    1 
ATOM   470   C  C     . PRO   A 1  63  ? 33.597  95.761  53.911  1.00 40.66  ? 63  PRO   A C     1 
ATOM   471   O  O     . PRO   A 1  63  ? 34.223  95.529  52.872  1.00 41.94  ? 63  PRO   A O     1 
ATOM   472   C  CB    . PRO   A 1  63  ? 31.123  95.524  53.421  1.00 39.36  ? 63  PRO   A CB    1 
ATOM   473   C  CG    . PRO   A 1  63  ? 30.099  96.487  52.884  1.00 36.16  ? 63  PRO   A CG    1 
ATOM   474   C  CD    . PRO   A 1  63  ? 30.899  97.555  52.186  1.00 38.39  ? 63  PRO   A CD    1 
ATOM   475   N  N     . ARG   A 1  64  ? 34.057  95.452  55.127  1.00 32.68  ? 64  ARG   A N     1 
ATOM   476   C  CA    . ARG   A 1  64  ? 35.306  94.740  55.338  1.00 39.50  ? 64  ARG   A CA    1 
ATOM   477   C  C     . ARG   A 1  64  ? 35.082  93.255  55.099  1.00 42.41  ? 64  ARG   A C     1 
ATOM   478   O  O     . ARG   A 1  64  ? 35.417  92.431  55.958  1.00 49.81  ? 64  ARG   A O     1 
ATOM   479   C  CB    . ARG   A 1  64  ? 35.826  94.975  56.765  1.00 41.55  ? 64  ARG   A CB    1 
ATOM   480   C  CG    . ARG   A 1  64  ? 36.321  96.391  57.056  1.00 38.04  ? 64  ARG   A CG    1 
ATOM   481   C  CD    . ARG   A 1  64  ? 36.924  96.531  58.471  1.00 43.93  ? 64  ARG   A CD    1 
ATOM   482   N  NE    . ARG   A 1  64  ? 38.119  97.366  58.459  1.00 39.45  ? 64  ARG   A NE    1 
ATOM   483   C  CZ    . ARG   A 1  64  ? 38.118  98.667  58.205  1.00 41.34  ? 64  ARG   A CZ    1 
ATOM   484   N  NH1   . ARG   A 1  64  ? 36.994  99.341  58.068  1.00 33.19  ? 64  ARG   A NH1   1 
ATOM   485   N  NH2   . ARG   A 1  64  ? 39.279  99.306  58.072  1.00 60.63  ? 64  ARG   A NH2   1 
ATOM   486   N  N     . ALA   A 1  65  ? 34.517  92.892  53.953  1.00 44.46  ? 65  ALA   A N     1 
ATOM   487   C  CA    . ALA   A 1  65  ? 34.049  91.531  53.753  1.00 42.71  ? 65  ALA   A CA    1 
ATOM   488   C  C     . ALA   A 1  65  ? 34.478  91.023  52.391  1.00 42.85  ? 65  ALA   A C     1 
ATOM   489   O  O     . ALA   A 1  65  ? 34.816  91.787  51.482  1.00 41.46  ? 65  ALA   A O     1 
ATOM   490   C  CB    . ALA   A 1  65  ? 32.521  91.431  53.859  1.00 39.60  ? 65  ALA   A CB    1 
ATOM   491   N  N     . VAL   A 1  66  ? 34.468  89.701  52.281  1.00 47.11  ? 66  VAL   A N     1 
ATOM   492   C  CA    A VAL   A 1  66  ? 34.709  89.011  51.024  0.89 45.03  ? 66  VAL   A CA    1 
ATOM   493   C  CA    B VAL   A 1  66  ? 34.717  89.003  51.027  0.11 44.89  ? 66  VAL   A CA    1 
ATOM   494   C  C     . VAL   A 1  66  ? 33.734  87.844  50.924  1.00 44.28  ? 66  VAL   A C     1 
ATOM   495   O  O     . VAL   A 1  66  ? 33.572  87.076  51.881  1.00 39.99  ? 66  VAL   A O     1 
ATOM   496   C  CB    A VAL   A 1  66  ? 36.164  88.522  50.901  0.89 42.96  ? 66  VAL   A CB    1 
ATOM   497   C  CB    B VAL   A 1  66  ? 36.168  88.492  50.929  0.11 42.95  ? 66  VAL   A CB    1 
ATOM   498   C  CG1   A VAL   A 1  66  ? 36.529  87.642  52.064  0.89 37.75  ? 66  VAL   A CG1   1 
ATOM   499   C  CG1   B VAL   A 1  66  ? 36.498  87.583  52.103  0.11 37.99  ? 66  VAL   A CG1   1 
ATOM   500   C  CG2   A VAL   A 1  66  ? 36.342  87.778  49.574  0.89 43.36  ? 66  VAL   A CG2   1 
ATOM   501   C  CG2   B VAL   A 1  66  ? 36.384  87.766  49.606  0.11 43.41  ? 66  VAL   A CG2   1 
ATOM   502   N  N     . PHE   A 1  67  ? 33.069  87.728  49.771  1.00 43.91  ? 67  PHE   A N     1 
ATOM   503   C  CA    . PHE   A 1  67  ? 32.200  86.601  49.461  1.00 41.15  ? 67  PHE   A CA    1 
ATOM   504   C  C     . PHE   A 1  67  ? 32.952  85.639  48.549  1.00 37.58  ? 67  PHE   A C     1 
ATOM   505   O  O     . PHE   A 1  67  ? 33.854  86.041  47.820  1.00 44.42  ? 67  PHE   A O     1 
ATOM   506   C  CB    . PHE   A 1  67  ? 30.923  87.043  48.757  1.00 38.08  ? 67  PHE   A CB    1 
ATOM   507   C  CG    . PHE   A 1  67  ? 30.129  88.092  49.483  1.00 38.97  ? 67  PHE   A CG    1 
ATOM   508   C  CD1   . PHE   A 1  67  ? 30.710  89.278  49.888  1.00 38.59  ? 67  PHE   A CD1   1 
ATOM   509   C  CD2   . PHE   A 1  67  ? 28.766  87.916  49.679  1.00 30.60  ? 67  PHE   A CD2   1 
ATOM   510   C  CE1   . PHE   A 1  67  ? 29.963  90.243  50.511  1.00 40.17  ? 67  PHE   A CE1   1 
ATOM   511   C  CE2   . PHE   A 1  67  ? 28.015  88.871  50.285  1.00 32.83  ? 67  PHE   A CE2   1 
ATOM   512   C  CZ    . PHE   A 1  67  ? 28.609  90.040  50.712  1.00 45.32  ? 67  PHE   A CZ    1 
ATOM   513   N  N     . VAL   A 1  68  ? 32.584  84.364  48.584  1.00 34.21  ? 68  VAL   A N     1 
ATOM   514   C  CA    A VAL   A 1  68  ? 33.274  83.371  47.770  0.25 36.05  ? 68  VAL   A CA    1 
ATOM   515   C  CA    B VAL   A 1  68  ? 33.268  83.380  47.754  0.75 36.02  ? 68  VAL   A CA    1 
ATOM   516   C  C     . VAL   A 1  68  ? 32.413  82.129  47.569  1.00 37.59  ? 68  VAL   A C     1 
ATOM   517   O  O     . VAL   A 1  68  ? 32.268  81.297  48.478  1.00 35.32  ? 68  VAL   A O     1 
ATOM   518   C  CB    A VAL   A 1  68  ? 34.631  82.995  48.392  0.25 36.21  ? 68  VAL   A CB    1 
ATOM   519   C  CB    B VAL   A 1  68  ? 34.648  83.027  48.334  0.75 36.16  ? 68  VAL   A CB    1 
ATOM   520   C  CG1   A VAL   A 1  68  ? 34.479  82.741  49.884  0.25 35.68  ? 68  VAL   A CG1   1 
ATOM   521   C  CG1   B VAL   A 1  68  ? 34.615  83.082  49.847  0.75 35.66  ? 68  VAL   A CG1   1 
ATOM   522   C  CG2   A VAL   A 1  68  ? 35.200  81.766  47.702  0.25 37.33  ? 68  VAL   A CG2   1 
ATOM   523   C  CG2   B VAL   A 1  68  ? 35.074  81.636  47.869  0.75 37.36  ? 68  VAL   A CG2   1 
ATOM   524   N  N     . ASP   A 1  69  ? 31.849  81.991  46.380  1.00 36.00  ? 69  ASP   A N     1 
ATOM   525   C  CA    . ASP   A 1  69  ? 31.152  80.791  45.960  1.00 32.18  ? 69  ASP   A CA    1 
ATOM   526   C  C     . ASP   A 1  69  ? 32.010  80.076  44.919  1.00 34.02  ? 69  ASP   A C     1 
ATOM   527   O  O     . ASP   A 1  69  ? 32.683  80.728  44.117  1.00 38.20  ? 69  ASP   A O     1 
ATOM   528   C  CB    . ASP   A 1  69  ? 29.793  81.180  45.393  1.00 34.96  ? 69  ASP   A CB    1 
ATOM   529   C  CG    . ASP   A 1  69  ? 28.791  80.079  45.481  1.00 36.11  ? 69  ASP   A CG    1 
ATOM   530   O  OD1   . ASP   A 1  69  ? 29.206  78.943  45.828  1.00 29.07  ? 69  ASP   A OD1   1 
ATOM   531   O  OD2   . ASP   A 1  69  ? 27.601  80.369  45.188  1.00 39.72  ? 69  ASP   A OD2   1 
ATOM   532   N  N     . LEU   A 1  70  ? 32.029  78.741  44.947  1.00 35.44  ? 70  LEU   A N     1 
ATOM   533   C  CA    . LEU   A 1  70  ? 32.705  78.003  43.877  1.00 32.22  ? 70  LEU   A CA    1 
ATOM   534   C  C     . LEU   A 1  70  ? 31.927  77.994  42.565  1.00 35.81  ? 70  LEU   A C     1 
ATOM   535   O  O     . LEU   A 1  70  ? 32.410  77.395  41.601  1.00 36.83  ? 70  LEU   A O     1 
ATOM   536   C  CB    . LEU   A 1  70  ? 32.981  76.565  44.292  1.00 18.80  ? 70  LEU   A CB    1 
ATOM   537   C  CG    . LEU   A 1  70  ? 33.980  76.532  45.427  1.00 34.07  ? 70  LEU   A CG    1 
ATOM   538   C  CD1   . LEU   A 1  70  ? 34.222  75.101  45.933  1.00 33.29  ? 70  LEU   A CD1   1 
ATOM   539   C  CD2   . LEU   A 1  70  ? 35.261  77.213  44.963  1.00 37.77  ? 70  LEU   A CD2   1 
ATOM   540   N  N     . GLU   A 1  71  ? 30.761  78.625  42.488  1.00 33.98  ? 71  GLU   A N     1 
ATOM   541   C  CA    . GLU   A 1  71  ? 30.083  78.862  41.223  1.00 36.76  ? 71  GLU   A CA    1 
ATOM   542   C  C     . GLU   A 1  71  ? 29.604  80.306  41.177  1.00 39.30  ? 71  GLU   A C     1 
ATOM   543   O  O     . GLU   A 1  71  ? 29.512  80.972  42.213  1.00 50.50  ? 71  GLU   A O     1 
ATOM   544   C  CB    . GLU   A 1  71  ? 28.913  77.888  41.013  1.00 36.94  ? 71  GLU   A CB    1 
ATOM   545   C  CG    . GLU   A 1  71  ? 27.783  77.981  42.020  1.00 40.11  ? 71  GLU   A CG    1 
ATOM   546   C  CD    . GLU   A 1  71  ? 26.487  78.513  41.418  1.00 42.15  ? 71  GLU   A CD    1 
ATOM   547   O  OE1   . GLU   A 1  71  ? 26.546  79.199  40.383  1.00 33.89  ? 71  GLU   A OE1   1 
ATOM   548   O  OE2   . GLU   A 1  71  ? 25.406  78.253  41.995  1.00 43.94  ? 71  GLU   A OE2   1 
ATOM   549   N  N     . PRO   A 1  72  ? 29.308  80.827  39.986  1.00 35.14  ? 72  PRO   A N     1 
ATOM   550   C  CA    . PRO   A 1  72  ? 29.064  82.265  39.855  1.00 28.41  ? 72  PRO   A CA    1 
ATOM   551   C  C     . PRO   A 1  72  ? 27.629  82.721  39.981  1.00 37.68  ? 72  PRO   A C     1 
ATOM   552   O  O     . PRO   A 1  72  ? 27.406  83.935  40.012  1.00 37.87  ? 72  PRO   A O     1 
ATOM   553   C  CB    . PRO   A 1  72  ? 29.570  82.555  38.440  1.00 37.34  ? 72  PRO   A CB    1 
ATOM   554   C  CG    . PRO   A 1  72  ? 29.288  81.298  37.684  1.00 32.84  ? 72  PRO   A CG    1 
ATOM   555   C  CD    . PRO   A 1  72  ? 29.504  80.175  38.676  1.00 46.43  ? 72  PRO   A CD    1 
ATOM   556   N  N     . THR   A 1  73  ? 26.649  81.821  40.019  1.00 44.01  ? 73  THR   A N     1 
ATOM   557   C  CA    . THR   A 1  73  ? 25.269  82.276  39.859  1.00 40.15  ? 73  THR   A CA    1 
ATOM   558   C  C     . THR   A 1  73  ? 24.874  83.231  40.969  1.00 39.65  ? 73  THR   A C     1 
ATOM   559   O  O     . THR   A 1  73  ? 24.199  84.237  40.723  1.00 45.53  ? 73  THR   A O     1 
ATOM   560   C  CB    . THR   A 1  73  ? 24.297  81.101  39.833  1.00 39.14  ? 73  THR   A CB    1 
ATOM   561   O  OG1   . THR   A 1  73  ? 24.731  80.154  38.864  1.00 56.74  ? 73  THR   A OG1   1 
ATOM   562   C  CG2   . THR   A 1  73  ? 22.915  81.590  39.455  1.00 41.13  ? 73  THR   A CG2   1 
ATOM   563   N  N     . VAL   A 1  74  ? 25.272  82.921  42.201  1.00 42.52  ? 74  VAL   A N     1 
ATOM   564   C  CA    . VAL   A 1  74  ? 24.798  83.682  43.347  1.00 44.51  ? 74  VAL   A CA    1 
ATOM   565   C  C     . VAL   A 1  74  ? 25.565  84.995  43.473  1.00 41.08  ? 74  VAL   A C     1 
ATOM   566   O  O     . VAL   A 1  74  ? 24.971  86.075  43.582  1.00 32.23  ? 74  VAL   A O     1 
ATOM   567   C  CB    . VAL   A 1  74  ? 24.917  82.837  44.626  1.00 38.44  ? 74  VAL   A CB    1 
ATOM   568   C  CG1   . VAL   A 1  74  ? 24.033  83.419  45.699  1.00 32.51  ? 74  VAL   A CG1   1 
ATOM   569   C  CG2   . VAL   A 1  74  ? 24.597  81.356  44.355  1.00 31.71  ? 74  VAL   A CG2   1 
ATOM   570   N  N     . ILE   A 1  75  ? 26.896  84.921  43.462  1.00 28.78  ? 75  ILE   A N     1 
ATOM   571   C  CA    . ILE   A 1  75  ? 27.682  86.128  43.648  1.00 31.29  ? 75  ILE   A CA    1 
ATOM   572   C  C     . ILE   A 1  75  ? 27.418  87.124  42.527  1.00 36.58  ? 75  ILE   A C     1 
ATOM   573   O  O     . ILE   A 1  75  ? 27.558  88.338  42.720  1.00 40.47  ? 75  ILE   A O     1 
ATOM   574   C  CB    . ILE   A 1  75  ? 29.173  85.766  43.769  1.00 35.87  ? 75  ILE   A CB    1 
ATOM   575   C  CG1   . ILE   A 1  75  ? 29.353  84.720  44.882  1.00 39.78  ? 75  ILE   A CG1   1 
ATOM   576   C  CG2   . ILE   A 1  75  ? 30.022  87.025  43.960  1.00 33.70  ? 75  ILE   A CG2   1 
ATOM   577   C  CD1   . ILE   A 1  75  ? 30.721  84.713  45.584  1.00 37.76  ? 75  ILE   A CD1   1 
ATOM   578   N  N     . ASP   A 1  76  ? 27.027  86.634  41.346  1.00 38.09  ? 76  ASP   A N     1 
ATOM   579   C  CA    . ASP   A 1  76  ? 26.661  87.522  40.244  1.00 40.73  ? 76  ASP   A CA    1 
ATOM   580   C  C     . ASP   A 1  76  ? 25.463  88.376  40.608  1.00 43.52  ? 76  ASP   A C     1 
ATOM   581   O  O     . ASP   A 1  76  ? 25.351  89.518  40.149  1.00 52.58  ? 76  ASP   A O     1 
ATOM   582   C  CB    . ASP   A 1  76  ? 26.349  86.718  38.973  1.00 46.34  ? 76  ASP   A CB    1 
ATOM   583   C  CG    . ASP   A 1  76  ? 27.578  86.486  38.086  1.00 41.75  ? 76  ASP   A CG    1 
ATOM   584   O  OD1   . ASP   A 1  76  ? 28.572  87.222  38.241  1.00 38.83  ? 76  ASP   A OD1   1 
ATOM   585   O  OD2   . ASP   A 1  76  ? 27.540  85.577  37.220  1.00 38.55  ? 76  ASP   A OD2   1 
ATOM   586   N  N     . GLU   A 1  77  ? 24.557  87.837  41.429  1.00 49.12  ? 77  GLU   A N     1 
ATOM   587   C  CA    . GLU   A 1  77  ? 23.443  88.632  41.944  1.00 59.03  ? 77  GLU   A CA    1 
ATOM   588   C  C     . GLU   A 1  77  ? 23.922  89.691  42.941  1.00 54.91  ? 77  GLU   A C     1 
ATOM   589   O  O     . GLU   A 1  77  ? 23.225  90.688  43.160  1.00 62.36  ? 77  GLU   A O     1 
ATOM   590   C  CB    . GLU   A 1  77  ? 22.379  87.727  42.597  1.00 59.89  ? 77  GLU   A CB    1 
ATOM   591   C  CG    . GLU   A 1  77  ? 21.836  86.552  41.726  1.00 55.66  ? 77  GLU   A CG    1 
ATOM   592   C  CD    . GLU   A 1  77  ? 21.410  86.961  40.315  1.00 64.62  ? 77  GLU   A CD    1 
ATOM   593   O  OE1   . GLU   A 1  77  ? 20.432  87.739  40.173  1.00 55.70  ? 77  GLU   A OE1   1 
ATOM   594   O  OE2   . GLU   A 1  77  ? 22.063  86.490  39.347  1.00 57.87  ? 77  GLU   A OE2   1 
ATOM   595   N  N     . VAL   A 1  78  ? 25.093  89.493  43.562  1.00 44.99  ? 78  VAL   A N     1 
ATOM   596   C  CA    . VAL   A 1  78  ? 25.668  90.534  44.411  1.00 50.72  ? 78  VAL   A CA    1 
ATOM   597   C  C     . VAL   A 1  78  ? 26.395  91.580  43.564  1.00 55.31  ? 78  VAL   A C     1 
ATOM   598   O  O     . VAL   A 1  78  ? 26.317  92.783  43.840  1.00 58.78  ? 78  VAL   A O     1 
ATOM   599   C  CB    . VAL   A 1  78  ? 26.593  89.931  45.487  1.00 37.98  ? 78  VAL   A CB    1 
ATOM   600   C  CG1   . VAL   A 1  78  ? 27.257  91.032  46.306  1.00 29.25  ? 78  VAL   A CG1   1 
ATOM   601   C  CG2   . VAL   A 1  78  ? 25.811  89.036  46.389  1.00 31.56  ? 78  VAL   A CG2   1 
ATOM   602   N  N     . ARG   A 1  79  ? 27.096  91.160  42.515  1.00 47.22  ? 79  ARG   A N     1 
ATOM   603   C  CA    . ARG   A 1  79  ? 27.661  92.146  41.601  1.00 52.92  ? 79  ARG   A CA    1 
ATOM   604   C  C     . ARG   A 1  79  ? 26.647  92.672  40.584  1.00 56.08  ? 79  ARG   A C     1 
ATOM   605   O  O     . ARG   A 1  79  ? 27.035  93.056  39.483  1.00 51.66  ? 79  ARG   A O     1 
ATOM   606   C  CB    . ARG   A 1  79  ? 28.875  91.571  40.869  1.00 45.71  ? 79  ARG   A CB    1 
ATOM   607   C  CG    . ARG   A 1  79  ? 28.570  90.418  39.974  1.00 44.50  ? 79  ARG   A CG    1 
ATOM   608   C  CD    . ARG   A 1  79  ? 29.599  89.320  40.174  1.00 45.73  ? 79  ARG   A CD    1 
ATOM   609   N  NE    . ARG   A 1  79  ? 30.919  89.860  40.466  1.00 43.54  ? 79  ARG   A NE    1 
ATOM   610   C  CZ    . ARG   A 1  79  ? 32.000  89.119  40.672  1.00 55.82  ? 79  ARG   A CZ    1 
ATOM   611   N  NH1   . ARG   A 1  79  ? 31.952  87.793  40.632  1.00 39.15  ? 79  ARG   A NH1   1 
ATOM   612   N  NH2   . ARG   A 1  79  ? 33.163  89.722  40.914  1.00 69.28  ? 79  ARG   A NH2   1 
ATOM   613   N  N     . THR   A 1  80  ? 25.357  92.727  40.939  1.00 63.95  ? 80  THR   A N     1 
ATOM   614   C  CA    . THR   A 1  80  ? 24.333  93.294  40.060  1.00 63.02  ? 80  THR   A CA    1 
ATOM   615   C  C     . THR   A 1  80  ? 23.152  93.902  40.815  1.00 67.05  ? 80  THR   A C     1 
ATOM   616   O  O     . THR   A 1  80  ? 22.400  94.693  40.238  1.00 71.20  ? 80  THR   A O     1 
ATOM   617   C  CB    . THR   A 1  80  ? 23.785  92.231  39.108  1.00 58.76  ? 80  THR   A CB    1 
ATOM   618   O  OG1   . THR   A 1  80  ? 23.351  91.098  39.874  1.00 57.57  ? 80  THR   A OG1   1 
ATOM   619   C  CG2   . THR   A 1  80  ? 24.825  91.815  38.078  1.00 40.25  ? 80  THR   A CG2   1 
ATOM   620   N  N     . GLY   A 1  81  ? 22.947  93.512  42.076  1.00 69.52  ? 81  GLY   A N     1 
ATOM   621   C  CA    . GLY   A 1  81  ? 21.827  93.985  42.866  1.00 55.21  ? 81  GLY   A CA    1 
ATOM   622   C  C     . GLY   A 1  81  ? 22.027  95.419  43.304  1.00 61.95  ? 81  GLY   A C     1 
ATOM   623   O  O     . GLY   A 1  81  ? 22.940  96.114  42.861  1.00 65.42  ? 81  GLY   A O     1 
ATOM   624   N  N     . THR   A 1  82  ? 21.159  95.867  44.212  1.00 57.98  ? 82  THR   A N     1 
ATOM   625   C  CA    . THR   A 1  82  ? 21.178  97.285  44.561  1.00 61.81  ? 82  THR   A CA    1 
ATOM   626   C  C     . THR   A 1  82  ? 22.516  97.694  45.157  1.00 57.32  ? 82  THR   A C     1 
ATOM   627   O  O     . THR   A 1  82  ? 22.987  98.817  44.934  1.00 64.18  ? 82  THR   A O     1 
ATOM   628   C  CB    . THR   A 1  82  ? 20.056  97.622  45.535  1.00 72.58  ? 82  THR   A CB    1 
ATOM   629   O  OG1   . THR   A 1  82  ? 18.930  96.777  45.276  1.00 69.24  ? 82  THR   A OG1   1 
ATOM   630   C  CG2   . THR   A 1  82  ? 19.660  99.102  45.359  1.00 71.32  ? 82  THR   A CG2   1 
ATOM   631   N  N     . TYR   A 1  83  ? 23.140  96.802  45.923  1.00 50.03  ? 83  TYR   A N     1 
ATOM   632   C  CA    . TYR   A 1  83  ? 24.351  97.121  46.660  1.00 50.72  ? 83  TYR   A CA    1 
ATOM   633   C  C     . TYR   A 1  83  ? 25.620  96.759  45.888  1.00 57.77  ? 83  TYR   A C     1 
ATOM   634   O  O     . TYR   A 1  83  ? 26.698  96.676  46.490  1.00 57.90  ? 83  TYR   A O     1 
ATOM   635   C  CB    . TYR   A 1  83  ? 24.307  96.446  48.042  1.00 46.20  ? 83  TYR   A CB    1 
ATOM   636   C  CG    . TYR   A 1  83  ? 23.246  97.042  48.974  1.00 46.56  ? 83  TYR   A CG    1 
ATOM   637   C  CD1   . TYR   A 1  83  ? 23.457  98.261  49.610  1.00 47.79  ? 83  TYR   A CD1   1 
ATOM   638   C  CD2   . TYR   A 1  83  ? 22.029  96.399  49.195  1.00 38.19  ? 83  TYR   A CD2   1 
ATOM   639   C  CE1   . TYR   A 1  83  ? 22.499  98.819  50.446  1.00 45.68  ? 83  TYR   A CE1   1 
ATOM   640   C  CE2   . TYR   A 1  83  ? 21.055  96.952  50.031  1.00 38.60  ? 83  TYR   A CE2   1 
ATOM   641   C  CZ    . TYR   A 1  83  ? 21.299  98.163  50.663  1.00 46.24  ? 83  TYR   A CZ    1 
ATOM   642   O  OH    . TYR   A 1  83  ? 20.349  98.729  51.510  1.00 46.78  ? 83  TYR   A OH    1 
ATOM   643   N  N     . ARG   A 1  84  ? 25.517  96.579  44.563  1.00 64.65  ? 84  ARG   A N     1 
ATOM   644   C  CA    . ARG   A 1  84  ? 26.697  96.293  43.743  1.00 61.02  ? 84  ARG   A CA    1 
ATOM   645   C  C     . ARG   A 1  84  ? 27.727  97.409  43.847  1.00 59.27  ? 84  ARG   A C     1 
ATOM   646   O  O     . ARG   A 1  84  ? 28.933  97.149  43.944  1.00 56.35  ? 84  ARG   A O     1 
ATOM   647   C  CB    . ARG   A 1  84  ? 26.291  96.078  42.278  1.00 65.64  ? 84  ARG   A CB    1 
ATOM   648   C  CG    . ARG   A 1  84  ? 26.332  97.332  41.382  1.00 59.09  ? 84  ARG   A CG    1 
ATOM   649   C  CD    . ARG   A 1  84  ? 25.075  98.164  41.539  1.00 65.01  ? 84  ARG   A CD    1 
ATOM   650   N  NE    . ARG   A 1  84  ? 23.947  97.555  40.849  1.00 73.46  ? 84  ARG   A NE    1 
ATOM   651   C  CZ    . ARG   A 1  84  ? 23.553  97.885  39.627  1.00 83.12  ? 84  ARG   A CZ    1 
ATOM   652   N  NH1   . ARG   A 1  84  ? 24.150  98.851  38.946  1.00 85.03  ? 84  ARG   A NH1   1 
ATOM   653   N  NH2   . ARG   A 1  84  ? 22.542  97.222  39.070  1.00 86.39  ? 84  ARG   A NH2   1 
ATOM   654   N  N     . GLN   A 1  85  ? 27.270  98.659  43.807  1.00 55.62  ? 85  GLN   A N     1 
ATOM   655   C  CA    . GLN   A 1  85  ? 28.160  99.800  43.973  1.00 62.96  ? 85  GLN   A CA    1 
ATOM   656   C  C     . GLN   A 1  85  ? 28.925  99.739  45.293  1.00 61.58  ? 85  GLN   A C     1 
ATOM   657   O  O     . GLN   A 1  85  ? 30.045  100.253 45.395  1.00 55.45  ? 85  GLN   A O     1 
ATOM   658   C  CB    . GLN   A 1  85  ? 27.307  101.065 43.866  1.00 56.36  ? 85  GLN   A CB    1 
ATOM   659   C  CG    . GLN   A 1  85  ? 25.888  100.784 44.362  1.00 59.56  ? 85  GLN   A CG    1 
ATOM   660   C  CD    . GLN   A 1  85  ? 24.838  101.729 43.799  1.00 77.33  ? 85  GLN   A CD    1 
ATOM   661   O  OE1   . GLN   A 1  85  ? 25.161  102.699 43.102  1.00 74.91  ? 85  GLN   A OE1   1 
ATOM   662   N  NE2   . GLN   A 1  85  ? 23.567  101.443 44.093  1.00 74.36  ? 85  GLN   A NE2   1 
ATOM   663   N  N     . LEU   A 1  86  ? 28.357  99.091  46.293  1.00 57.86  ? 86  LEU   A N     1 
ATOM   664   C  CA    . LEU   A 1  86  ? 28.883  99.194  47.636  1.00 56.10  ? 86  LEU   A CA    1 
ATOM   665   C  C     . LEU   A 1  86  ? 30.100  98.306  47.860  1.00 57.62  ? 86  LEU   A C     1 
ATOM   666   O  O     . LEU   A 1  86  ? 31.046  98.726  48.529  1.00 58.14  ? 86  LEU   A O     1 
ATOM   667   C  CB    . LEU   A 1  86  ? 27.767  98.863  48.620  1.00 54.72  ? 86  LEU   A CB    1 
ATOM   668   C  CG    . LEU   A 1  86  ? 28.089  98.932  50.092  1.00 49.10  ? 86  LEU   A CG    1 
ATOM   669   C  CD1   . LEU   A 1  86  ? 26.987  99.724  50.744  1.00 53.45  ? 86  LEU   A CD1   1 
ATOM   670   C  CD2   . LEU   A 1  86  ? 28.160  97.522  50.633  1.00 43.76  ? 86  LEU   A CD2   1 
ATOM   671   N  N     . PHE   A 1  87  ? 30.112  97.091  47.312  1.00 60.52  ? 87  PHE   A N     1 
ATOM   672   C  CA    . PHE   A 1  87  ? 31.252  96.196  47.484  1.00 53.84  ? 87  PHE   A CA    1 
ATOM   673   C  C     . PHE   A 1  87  ? 32.342  96.524  46.466  1.00 62.77  ? 87  PHE   A C     1 
ATOM   674   O  O     . PHE   A 1  87  ? 32.242  97.466  45.674  1.00 76.93  ? 87  PHE   A O     1 
ATOM   675   C  CB    . PHE   A 1  87  ? 30.824  94.740  47.364  1.00 48.89  ? 87  PHE   A CB    1 
ATOM   676   C  CG    . PHE   A 1  87  ? 29.725  94.347  48.299  1.00 50.26  ? 87  PHE   A CG    1 
ATOM   677   C  CD1   . PHE   A 1  87  ? 30.015  93.811  49.546  1.00 41.07  ? 87  PHE   A CD1   1 
ATOM   678   C  CD2   . PHE   A 1  87  ? 28.396  94.499  47.922  1.00 38.66  ? 87  PHE   A CD2   1 
ATOM   679   C  CE1   . PHE   A 1  87  ? 28.991  93.437  50.404  1.00 45.25  ? 87  PHE   A CE1   1 
ATOM   680   C  CE2   . PHE   A 1  87  ? 27.370  94.123  48.771  1.00 42.87  ? 87  PHE   A CE2   1 
ATOM   681   C  CZ    . PHE   A 1  87  ? 27.667  93.592  50.015  1.00 45.63  ? 87  PHE   A CZ    1 
ATOM   682   N  N     . HIS   A 1  88  ? 33.397  95.720  46.476  1.00 58.63  ? 88  HIS   A N     1 
ATOM   683   C  CA    . HIS   A 1  88  ? 34.575  95.894  45.657  1.00 65.42  ? 88  HIS   A CA    1 
ATOM   684   C  C     . HIS   A 1  88  ? 34.778  94.656  44.790  1.00 69.04  ? 88  HIS   A C     1 
ATOM   685   O  O     . HIS   A 1  88  ? 34.796  93.531  45.312  1.00 70.53  ? 88  HIS   A O     1 
ATOM   686   C  CB    . HIS   A 1  88  ? 35.804  96.142  46.554  1.00 68.38  ? 88  HIS   A CB    1 
ATOM   687   C  CG    . HIS   A 1  88  ? 37.120  95.942  45.865  1.00 80.44  ? 88  HIS   A CG    1 
ATOM   688   N  ND1   . HIS   A 1  88  ? 37.350  96.326  44.559  1.00 83.23  ? 88  HIS   A ND1   1 
ATOM   689   C  CD2   . HIS   A 1  88  ? 38.284  95.409  46.309  1.00 81.96  ? 88  HIS   A CD2   1 
ATOM   690   C  CE1   . HIS   A 1  88  ? 38.594  96.027  44.226  1.00 81.04  ? 88  HIS   A CE1   1 
ATOM   691   N  NE2   . HIS   A 1  88  ? 39.184  95.472  45.271  1.00 80.71  ? 88  HIS   A NE2   1 
ATOM   692   N  N     . PRO   A 1  89  ? 34.916  94.812  43.477  1.00 61.03  ? 89  PRO   A N     1 
ATOM   693   C  CA    . PRO   A 1  89  ? 34.978  93.633  42.594  1.00 62.98  ? 89  PRO   A CA    1 
ATOM   694   C  C     . PRO   A 1  89  ? 35.880  92.516  43.096  1.00 59.05  ? 89  PRO   A C     1 
ATOM   695   O  O     . PRO   A 1  89  ? 35.561  91.333  42.916  1.00 57.06  ? 89  PRO   A O     1 
ATOM   696   C  CB    . PRO   A 1  89  ? 35.500  94.228  41.283  1.00 58.66  ? 89  PRO   A CB    1 
ATOM   697   C  CG    . PRO   A 1  89  ? 34.996  95.636  41.299  1.00 66.15  ? 89  PRO   A CG    1 
ATOM   698   C  CD    . PRO   A 1  89  ? 34.963  96.079  42.735  1.00 68.16  ? 89  PRO   A CD    1 
ATOM   699   N  N     . GLU   A 1  90  ? 37.007  92.866  43.712  1.00 49.50  ? 90  GLU   A N     1 
ATOM   700   C  CA    . GLU   A 1  90  ? 37.972  91.882  44.173  1.00 51.43  ? 90  GLU   A CA    1 
ATOM   701   C  C     . GLU   A 1  90  ? 37.550  91.175  45.458  1.00 55.38  ? 90  GLU   A C     1 
ATOM   702   O  O     . GLU   A 1  90  ? 38.202  90.199  45.843  1.00 48.98  ? 90  GLU   A O     1 
ATOM   703   C  CB    . GLU   A 1  90  ? 39.340  92.541  44.395  1.00 62.37  ? 90  GLU   A CB    1 
ATOM   704   C  CG    . GLU   A 1  90  ? 40.260  92.604  43.180  1.00 74.46  ? 90  GLU   A CG    1 
ATOM   705   C  CD    . GLU   A 1  90  ? 41.743  92.726  43.558  1.00 88.49  ? 90  GLU   A CD    1 
ATOM   706   O  OE1   . GLU   A 1  90  ? 42.611  92.332  42.742  1.00 93.03  ? 90  GLU   A OE1   1 
ATOM   707   O  OE2   . GLU   A 1  90  ? 42.040  93.212  44.676  1.00 92.03  ? 90  GLU   A OE2   1 
ATOM   708   N  N     . GLN   A 1  91  ? 36.512  91.640  46.151  1.00 50.67  ? 91  GLN   A N     1 
ATOM   709   C  CA    . GLN   A 1  91  ? 36.055  90.913  47.327  1.00 52.33  ? 91  GLN   A CA    1 
ATOM   710   C  C     . GLN   A 1  91  ? 34.950  89.914  47.002  1.00 54.02  ? 91  GLN   A C     1 
ATOM   711   O  O     . GLN   A 1  91  ? 34.508  89.181  47.898  1.00 51.08  ? 91  GLN   A O     1 
ATOM   712   C  CB    . GLN   A 1  91  ? 35.597  91.880  48.431  1.00 53.89  ? 91  GLN   A CB    1 
ATOM   713   C  CG    . GLN   A 1  91  ? 35.157  93.256  47.967  1.00 59.11  ? 91  GLN   A CG    1 
ATOM   714   C  CD    . GLN   A 1  91  ? 34.911  94.203  49.128  1.00 59.95  ? 91  GLN   A CD    1 
ATOM   715   O  OE1   . GLN   A 1  91  ? 35.596  94.141  50.149  1.00 64.41  ? 91  GLN   A OE1   1 
ATOM   716   N  NE2   . GLN   A 1  91  ? 33.914  95.068  48.987  1.00 66.71  ? 91  GLN   A NE2   1 
ATOM   717   N  N     . LEU   A 1  92  ? 34.517  89.851  45.745  1.00 50.70  ? 92  LEU   A N     1 
ATOM   718   C  CA    . LEU   A 1  92  ? 33.513  88.900  45.278  1.00 43.94  ? 92  LEU   A CA    1 
ATOM   719   C  C     . LEU   A 1  92  ? 34.222  87.883  44.372  1.00 50.10  ? 92  LEU   A C     1 
ATOM   720   O  O     . LEU   A 1  92  ? 34.334  88.066  43.158  1.00 53.61  ? 92  LEU   A O     1 
ATOM   721   C  CB    . LEU   A 1  92  ? 32.397  89.630  44.564  1.00 44.77  ? 92  LEU   A CB    1 
ATOM   722   C  CG    . LEU   A 1  92  ? 31.789  90.827  45.284  1.00 45.42  ? 92  LEU   A CG    1 
ATOM   723   C  CD1   . LEU   A 1  92  ? 31.428  91.886  44.268  1.00 58.50  ? 92  LEU   A CD1   1 
ATOM   724   C  CD2   . LEU   A 1  92  ? 30.557  90.419  46.052  1.00 41.90  ? 92  LEU   A CD2   1 
ATOM   725   N  N     . ILE   A 1  93  ? 34.707  86.819  44.982  1.00 40.76  ? 93  ILE   A N     1 
ATOM   726   C  CA    . ILE   A 1  93  ? 35.468  85.769  44.324  1.00 35.66  ? 93  ILE   A CA    1 
ATOM   727   C  C     . ILE   A 1  93  ? 34.522  84.669  43.878  1.00 43.61  ? 93  ILE   A C     1 
ATOM   728   O  O     . ILE   A 1  93  ? 33.674  84.219  44.652  1.00 47.00  ? 93  ILE   A O     1 
ATOM   729   C  CB    . ILE   A 1  93  ? 36.528  85.215  45.287  1.00 37.03  ? 93  ILE   A CB    1 
ATOM   730   C  CG1   . ILE   A 1  93  ? 37.289  86.380  45.920  1.00 41.09  ? 93  ILE   A CG1   1 
ATOM   731   C  CG2   . ILE   A 1  93  ? 37.440  84.201  44.570  1.00 37.43  ? 93  ILE   A CG2   1 
ATOM   732   C  CD1   . ILE   A 1  93  ? 38.290  85.961  46.961  1.00 41.31  ? 93  ILE   A CD1   1 
ATOM   733   N  N     . THR   A 1  94  ? 34.678  84.203  42.643  1.00 50.93  ? 94  THR   A N     1 
ATOM   734   C  CA    . THR   A 1  94  ? 33.869  83.090  42.166  1.00 47.10  ? 94  THR   A CA    1 
ATOM   735   C  C     . THR   A 1  94  ? 34.706  82.115  41.345  1.00 37.97  ? 94  THR   A C     1 
ATOM   736   O  O     . THR   A 1  94  ? 35.687  82.496  40.706  1.00 38.62  ? 94  THR   A O     1 
ATOM   737   C  CB    . THR   A 1  94  ? 32.693  83.569  41.316  1.00 42.10  ? 94  THR   A CB    1 
ATOM   738   O  OG1   . THR   A 1  94  ? 32.759  82.899  40.057  1.00 42.21  ? 94  THR   A OG1   1 
ATOM   739   C  CG2   . THR   A 1  94  ? 32.760  85.077  41.106  1.00 35.51  ? 94  THR   A CG2   1 
ATOM   740   N  N     . GLY   A 1  95  ? 34.305  80.847  41.381  1.00 43.04  ? 95  GLY   A N     1 
ATOM   741   C  CA    . GLY   A 1  95  ? 34.798  79.827  40.483  1.00 41.74  ? 95  GLY   A CA    1 
ATOM   742   C  C     . GLY   A 1  95  ? 33.777  79.459  39.423  1.00 40.38  ? 95  GLY   A C     1 
ATOM   743   O  O     . GLY   A 1  95  ? 32.798  80.176  39.190  1.00 41.77  ? 95  GLY   A O     1 
ATOM   744   N  N     . LYS   A 1  96  ? 33.999  78.306  38.782  1.00 48.71  ? 96  LYS   A N     1 
ATOM   745   C  CA    . LYS   A 1  96  ? 33.212  77.874  37.625  1.00 41.72  ? 96  LYS   A CA    1 
ATOM   746   C  C     . LYS   A 1  96  ? 32.343  76.657  37.943  1.00 38.48  ? 96  LYS   A C     1 
ATOM   747   O  O     . LYS   A 1  96  ? 31.122  76.762  37.879  1.00 43.49  ? 96  LYS   A O     1 
ATOM   748   C  CB    . LYS   A 1  96  ? 34.128  77.616  36.419  1.00 50.32  ? 96  LYS   A CB    1 
ATOM   749   C  CG    . LYS   A 1  96  ? 35.191  76.505  36.610  1.00 59.11  ? 96  LYS   A CG    1 
ATOM   750   C  CD    . LYS   A 1  96  ? 36.195  76.922  37.675  1.00 61.62  ? 96  LYS   A CD    1 
ATOM   751   C  CE    . LYS   A 1  96  ? 37.175  75.864  38.095  1.00 70.94  ? 96  LYS   A CE    1 
ATOM   752   N  NZ    . LYS   A 1  96  ? 37.825  76.367  39.327  1.00 71.76  ? 96  LYS   A NZ    1 
ATOM   753   N  N     . GLU   A 1  97  ? 32.926  75.495  38.258  1.00 39.93  ? 97  GLU   A N     1 
ATOM   754   C  CA    . GLU   A 1  97  ? 32.171  74.327  38.722  1.00 43.98  ? 97  GLU   A CA    1 
ATOM   755   C  C     . GLU   A 1  97  ? 32.024  74.379  40.242  1.00 37.06  ? 97  GLU   A C     1 
ATOM   756   O  O     . GLU   A 1  97  ? 32.997  74.635  40.959  1.00 40.91  ? 97  GLU   A O     1 
ATOM   757   C  CB    . GLU   A 1  97  ? 32.860  72.992  38.363  1.00 41.53  ? 97  GLU   A CB    1 
ATOM   758   C  CG    . GLU   A 1  97  ? 32.944  72.559  36.891  1.00 50.55  ? 97  GLU   A CG    1 
ATOM   759   C  CD    . GLU   A 1  97  ? 33.211  71.037  36.714  1.00 56.52  ? 97  GLU   A CD    1 
ATOM   760   O  OE1   . GLU   A 1  97  ? 32.599  70.232  37.450  1.00 46.15  ? 97  GLU   A OE1   1 
ATOM   761   O  OE2   . GLU   A 1  97  ? 34.022  70.644  35.834  1.00 55.04  ? 97  GLU   A OE2   1 
ATOM   762   N  N     . ASP   A 1  98  ? 30.824  74.078  40.740  1.00 37.70  ? 98  ASP   A N     1 
ATOM   763   C  CA    . ASP   A 1  98  ? 30.618  74.055  42.183  1.00 26.49  ? 98  ASP   A CA    1 
ATOM   764   C  C     . ASP   A 1  98  ? 31.016  72.686  42.722  1.00 21.85  ? 98  ASP   A C     1 
ATOM   765   O  O     . ASP   A 1  98  ? 31.689  71.903  42.044  1.00 37.74  ? 98  ASP   A O     1 
ATOM   766   C  CB    . ASP   A 1  98  ? 29.182  74.474  42.538  1.00 25.83  ? 98  ASP   A CB    1 
ATOM   767   C  CG    . ASP   A 1  98  ? 28.134  73.459  42.153  1.00 22.86  ? 98  ASP   A CG    1 
ATOM   768   O  OD1   . ASP   A 1  98  ? 28.312  72.261  42.417  1.00 20.75  ? 98  ASP   A OD1   1 
ATOM   769   O  OD2   . ASP   A 1  98  ? 27.087  73.884  41.630  1.00 31.14  ? 98  ASP   A OD2   1 
ATOM   770   N  N     . ALA   A 1  99  ? 30.615  72.389  43.945  1.00 13.83  ? 99  ALA   A N     1 
ATOM   771   C  CA    . ALA   A 1  99  ? 31.076  71.216  44.667  1.00 17.15  ? 99  ALA   A CA    1 
ATOM   772   C  C     . ALA   A 1  99  ? 30.027  70.115  44.762  1.00 17.73  ? 99  ALA   A C     1 
ATOM   773   O  O     . ALA   A 1  99  ? 30.181  69.204  45.588  1.00 20.49  ? 99  ALA   A O     1 
ATOM   774   C  CB    . ALA   A 1  99  ? 31.544  71.634  46.066  1.00 15.93  ? 99  ALA   A CB    1 
ATOM   775   N  N     . ALA   A 1  100 ? 28.974  70.183  43.945  1.00 13.18  ? 100 ALA   A N     1 
ATOM   776   C  CA    . ALA   A 1  100 ? 27.872  69.225  43.930  1.00 17.74  ? 100 ALA   A CA    1 
ATOM   777   C  C     . ALA   A 1  100 ? 27.529  68.642  45.295  1.00 20.83  ? 100 ALA   A C     1 
ATOM   778   O  O     . ALA   A 1  100 ? 27.575  67.425  45.457  1.00 20.18  ? 100 ALA   A O     1 
ATOM   779   C  CB    . ALA   A 1  100 ? 28.187  68.083  42.973  1.00 22.47  ? 100 ALA   A CB    1 
ATOM   780   N  N     . ASN   A 1  101 ? 27.157  69.486  46.265  1.00 21.77  ? 101 ASN   A N     1 
ATOM   781   C  CA    . ASN   A 1  101 ? 26.831  69.074  47.627  1.00 19.66  ? 101 ASN   A CA    1 
ATOM   782   C  C     . ASN   A 1  101 ? 27.745  67.967  48.136  1.00 24.31  ? 101 ASN   A C     1 
ATOM   783   O  O     . ASN   A 1  101 ? 27.289  67.028  48.803  1.00 18.85  ? 101 ASN   A O     1 
ATOM   784   C  CB    . ASN   A 1  101 ? 25.383  68.603  47.735  1.00 23.62  ? 101 ASN   A CB    1 
ATOM   785   C  CG    . ASN   A 1  101 ? 24.409  69.532  47.049  1.00 29.00  ? 101 ASN   A CG    1 
ATOM   786   O  OD1   . ASN   A 1  101 ? 23.783  69.152  46.056  1.00 32.27  ? 101 ASN   A OD1   1 
ATOM   787   N  ND2   . ASN   A 1  101 ? 24.262  70.748  47.574  1.00 28.50  ? 101 ASN   A ND2   1 
ATOM   788   N  N     . ASN   A 1  102 ? 29.035  68.059  47.827  1.00 25.36  ? 102 ASN   A N     1 
ATOM   789   C  CA    . ASN   A 1  102 ? 29.986  67.020  48.196  1.00 26.37  ? 102 ASN   A CA    1 
ATOM   790   C  C     . ASN   A 1  102 ? 31.137  67.654  48.978  1.00 34.17  ? 102 ASN   A C     1 
ATOM   791   O  O     . ASN   A 1  102 ? 31.978  68.361  48.408  1.00 33.27  ? 102 ASN   A O     1 
ATOM   792   C  CB    . ASN   A 1  102 ? 30.457  66.283  46.950  1.00 18.07  ? 102 ASN   A CB    1 
ATOM   793   C  CG    . ASN   A 1  102 ? 31.438  65.180  47.259  1.00 25.46  ? 102 ASN   A CG    1 
ATOM   794   O  OD1   . ASN   A 1  102 ? 32.211  65.275  48.202  1.00 27.35  ? 102 ASN   A OD1   1 
ATOM   795   N  ND2   . ASN   A 1  102 ? 31.429  64.130  46.445  1.00 22.56  ? 102 ASN   A ND2   1 
ATOM   796   N  N     . TYR   A 1  103 ? 31.155  67.414  50.292  1.00 30.17  ? 103 TYR   A N     1 
ATOM   797   C  CA    . TYR   A 1  103 ? 32.182  68.005  51.138  1.00 29.10  ? 103 TYR   A CA    1 
ATOM   798   C  C     . TYR   A 1  103 ? 33.575  67.765  50.554  1.00 29.97  ? 103 TYR   A C     1 
ATOM   799   O  O     . TYR   A 1  103 ? 34.350  68.711  50.348  1.00 27.08  ? 103 TYR   A O     1 
ATOM   800   C  CB    . TYR   A 1  103 ? 32.064  67.440  52.565  1.00 29.51  ? 103 TYR   A CB    1 
ATOM   801   C  CG    . TYR   A 1  103 ? 33.272  67.756  53.404  1.00 31.16  ? 103 TYR   A CG    1 
ATOM   802   C  CD1   . TYR   A 1  103 ? 33.458  69.030  53.922  1.00 30.77  ? 103 TYR   A CD1   1 
ATOM   803   C  CD2   . TYR   A 1  103 ? 34.248  66.802  53.636  1.00 29.94  ? 103 TYR   A CD2   1 
ATOM   804   C  CE1   . TYR   A 1  103 ? 34.572  69.344  54.665  1.00 33.25  ? 103 TYR   A CE1   1 
ATOM   805   C  CE2   . TYR   A 1  103 ? 35.370  67.101  54.375  1.00 33.70  ? 103 TYR   A CE2   1 
ATOM   806   C  CZ    . TYR   A 1  103 ? 35.531  68.378  54.891  1.00 36.32  ? 103 TYR   A CZ    1 
ATOM   807   O  OH    . TYR   A 1  103 ? 36.657  68.685  55.622  1.00 32.75  ? 103 TYR   A OH    1 
ATOM   808   N  N     . ALA   A 1  104 ? 33.903  66.490  50.272  1.00 34.73  ? 104 ALA   A N     1 
ATOM   809   C  CA    . ALA   A 1  104 ? 35.232  66.127  49.763  1.00 33.64  ? 104 ALA   A CA    1 
ATOM   810   C  C     . ALA   A 1  104 ? 35.570  66.886  48.486  1.00 28.94  ? 104 ALA   A C     1 
ATOM   811   O  O     . ALA   A 1  104 ? 36.712  67.321  48.290  1.00 27.57  ? 104 ALA   A O     1 
ATOM   812   C  CB    . ALA   A 1  104 ? 35.322  64.623  49.506  1.00 24.18  ? 104 ALA   A CB    1 
ATOM   813   N  N     . ARG   A 1  105 ? 34.591  67.067  47.608  1.00 25.21  ? 105 ARG   A N     1 
ATOM   814   C  CA    . ARG   A 1  105 ? 34.851  67.846  46.410  1.00 27.19  ? 105 ARG   A CA    1 
ATOM   815   C  C     . ARG   A 1  105 ? 35.256  69.270  46.763  1.00 26.15  ? 105 ARG   A C     1 
ATOM   816   O  O     . ARG   A 1  105 ? 36.294  69.748  46.323  1.00 42.03  ? 105 ARG   A O     1 
ATOM   817   C  CB    . ARG   A 1  105 ? 33.632  67.818  45.500  1.00 25.61  ? 105 ARG   A CB    1 
ATOM   818   C  CG    . ARG   A 1  105 ? 33.761  68.637  44.269  1.00 27.59  ? 105 ARG   A CG    1 
ATOM   819   C  CD    . ARG   A 1  105 ? 32.583  68.323  43.410  1.00 23.59  ? 105 ARG   A CD    1 
ATOM   820   N  NE    . ARG   A 1  105 ? 32.998  67.497  42.292  1.00 26.36  ? 105 ARG   A NE    1 
ATOM   821   C  CZ    . ARG   A 1  105 ? 33.150  67.978  41.071  1.00 36.37  ? 105 ARG   A CZ    1 
ATOM   822   N  NH1   . ARG   A 1  105 ? 32.857  69.244  40.789  1.00 27.11  ? 105 ARG   A NH1   1 
ATOM   823   N  NH2   . ARG   A 1  105 ? 33.604  67.175  40.113  1.00 31.15  ? 105 ARG   A NH2   1 
ATOM   824   N  N     . GLY   A 1  106 ? 34.481  69.957  47.593  1.00 26.34  ? 106 GLY   A N     1 
ATOM   825   C  CA    . GLY   A 1  106 ? 34.827  71.339  47.885  1.00 26.73  ? 106 GLY   A CA    1 
ATOM   826   C  C     . GLY   A 1  106 ? 36.051  71.516  48.773  1.00 28.43  ? 106 GLY   A C     1 
ATOM   827   O  O     . GLY   A 1  106 ? 36.669  72.587  48.753  1.00 33.40  ? 106 GLY   A O     1 
ATOM   828   N  N     . HIS   A 1  107 ? 36.396  70.505  49.573  1.00 26.20  ? 107 HIS   A N     1 
ATOM   829   C  CA    . HIS   A 1  107 ? 37.596  70.584  50.405  1.00 31.18  ? 107 HIS   A CA    1 
ATOM   830   C  C     . HIS   A 1  107 ? 38.868  70.297  49.607  1.00 44.23  ? 107 HIS   A C     1 
ATOM   831   O  O     . HIS   A 1  107 ? 39.855  71.040  49.704  1.00 52.51  ? 107 HIS   A O     1 
ATOM   832   C  CB    . HIS   A 1  107 ? 37.487  69.600  51.561  1.00 32.54  ? 107 HIS   A CB    1 
ATOM   833   C  CG    . HIS   A 1  107 ? 38.517  69.792  52.632  1.00 32.96  ? 107 HIS   A CG    1 
ATOM   834   N  ND1   . HIS   A 1  107 ? 38.460  70.824  53.547  1.00 38.31  ? 107 HIS   A ND1   1 
ATOM   835   C  CD2   . HIS   A 1  107 ? 39.591  69.044  52.974  1.00 32.49  ? 107 HIS   A CD2   1 
ATOM   836   C  CE1   . HIS   A 1  107 ? 39.466  70.711  54.396  1.00 46.79  ? 107 HIS   A CE1   1 
ATOM   837   N  NE2   . HIS   A 1  107 ? 40.164  69.635  54.075  1.00 45.50  ? 107 HIS   A NE2   1 
ATOM   838   N  N     . TYR   A 1  108 ? 38.867  69.215  48.816  1.00 32.88  ? 108 TYR   A N     1 
ATOM   839   C  CA    . TYR   A 1  108 ? 40.057  68.760  48.113  1.00 27.42  ? 108 TYR   A CA    1 
ATOM   840   C  C     . TYR   A 1  108 ? 40.075  69.168  46.634  1.00 39.14  ? 108 TYR   A C     1 
ATOM   841   O  O     . TYR   A 1  108 ? 40.947  69.918  46.193  1.00 45.72  ? 108 TYR   A O     1 
ATOM   842   C  CB    . TYR   A 1  108 ? 40.151  67.246  48.289  1.00 24.88  ? 108 TYR   A CB    1 
ATOM   843   C  CG    . TYR   A 1  108 ? 40.186  66.741  49.727  1.00 27.82  ? 108 TYR   A CG    1 
ATOM   844   C  CD1   . TYR   A 1  108 ? 41.377  66.699  50.450  1.00 35.94  ? 108 TYR   A CD1   1 
ATOM   845   C  CD2   . TYR   A 1  108 ? 39.045  66.255  50.349  1.00 32.91  ? 108 TYR   A CD2   1 
ATOM   846   C  CE1   . TYR   A 1  108 ? 41.425  66.219  51.763  1.00 23.33  ? 108 TYR   A CE1   1 
ATOM   847   C  CE2   . TYR   A 1  108 ? 39.084  65.764  51.655  1.00 25.56  ? 108 TYR   A CE2   1 
ATOM   848   C  CZ    . TYR   A 1  108 ? 40.281  65.752  52.350  1.00 26.90  ? 108 TYR   A CZ    1 
ATOM   849   O  OH    . TYR   A 1  108 ? 40.329  65.279  53.638  1.00 30.87  ? 108 TYR   A OH    1 
ATOM   850   N  N     . THR   A 1  109 ? 39.116  68.690  45.858  1.00 34.55  ? 109 THR   A N     1 
ATOM   851   C  CA    . THR   A 1  109 ? 39.020  68.958  44.427  1.00 30.82  ? 109 THR   A CA    1 
ATOM   852   C  C     . THR   A 1  109 ? 38.308  70.285  44.209  1.00 47.56  ? 109 THR   A C     1 
ATOM   853   O  O     . THR   A 1  109 ? 37.082  70.362  44.352  1.00 56.77  ? 109 THR   A O     1 
ATOM   854   C  CB    . THR   A 1  109 ? 38.208  67.849  43.755  1.00 38.58  ? 109 THR   A CB    1 
ATOM   855   O  OG1   . THR   A 1  109 ? 38.636  66.559  44.218  1.00 36.12  ? 109 THR   A OG1   1 
ATOM   856   C  CG2   . THR   A 1  109 ? 38.249  67.963  42.231  1.00 30.99  ? 109 THR   A CG2   1 
ATOM   857   N  N     . ILE   A 1  110 ? 39.034  71.316  43.802  1.00 44.52  ? 110 ILE   A N     1 
ATOM   858   C  CA    . ILE   A 1  110 ? 38.427  72.641  43.610  1.00 51.28  ? 110 ILE   A CA    1 
ATOM   859   C  C     . ILE   A 1  110 ? 38.763  73.492  44.825  1.00 45.57  ? 110 ILE   A C     1 
ATOM   860   O  O     . ILE   A 1  110 ? 39.035  74.690  44.697  1.00 44.80  ? 110 ILE   A O     1 
ATOM   861   C  CB    . ILE   A 1  110 ? 36.893  72.619  43.386  1.00 38.43  ? 110 ILE   A CB    1 
ATOM   862   C  CG1   . ILE   A 1  110 ? 36.489  71.769  42.171  1.00 47.50  ? 110 ILE   A CG1   1 
ATOM   863   C  CG2   . ILE   A 1  110 ? 36.379  74.023  43.155  1.00 42.67  ? 110 ILE   A CG2   1 
ATOM   864   C  CD1   . ILE   A 1  110 ? 35.035  71.959  41.737  1.00 41.55  ? 110 ILE   A CD1   1 
ATOM   865   N  N     . GLY   A 1  111 ? 38.741  72.889  46.012  1.00 46.06  ? 111 GLY   A N     1 
ATOM   866   C  CA    . GLY   A 1  111 ? 39.215  73.589  47.191  1.00 47.61  ? 111 GLY   A CA    1 
ATOM   867   C  C     . GLY   A 1  111 ? 40.646  74.052  46.992  1.00 55.01  ? 111 GLY   A C     1 
ATOM   868   O  O     . GLY   A 1  111 ? 40.906  75.249  46.801  1.00 55.03  ? 111 GLY   A O     1 
ATOM   869   N  N     . LYS   A 1  112 ? 41.579  73.094  47.022  1.00 52.24  ? 112 LYS   A N     1 
ATOM   870   C  CA    . LYS   A 1  112 ? 42.965  73.312  46.617  1.00 54.09  ? 112 LYS   A CA    1 
ATOM   871   C  C     . LYS   A 1  112 ? 43.082  74.272  45.440  1.00 46.22  ? 112 LYS   A C     1 
ATOM   872   O  O     . LYS   A 1  112 ? 43.944  75.154  45.424  1.00 54.32  ? 112 LYS   A O     1 
ATOM   873   C  CB    . LYS   A 1  112 ? 43.619  71.983  46.241  1.00 47.80  ? 112 LYS   A CB    1 
ATOM   874   C  CG    . LYS   A 1  112 ? 44.721  72.149  45.210  1.00 52.52  ? 112 LYS   A CG    1 
ATOM   875   C  CD    . LYS   A 1  112 ? 44.935  70.899  44.349  1.00 60.58  ? 112 LYS   A CD    1 
ATOM   876   C  CE    . LYS   A 1  112 ? 43.895  70.784  43.217  1.00 50.34  ? 112 LYS   A CE    1 
ATOM   877   N  NZ    . LYS   A 1  112 ? 44.167  71.697  42.058  1.00 50.02  ? 112 LYS   A NZ    1 
ATOM   878   N  N     . GLU   A 1  113 ? 42.207  74.114  44.455  1.00 49.26  ? 113 GLU   A N     1 
ATOM   879   C  CA    . GLU   A 1  113 ? 42.336  74.890  43.229  1.00 56.70  ? 113 GLU   A CA    1 
ATOM   880   C  C     . GLU   A 1  113 ? 42.018  76.369  43.420  1.00 49.33  ? 113 GLU   A C     1 
ATOM   881   O  O     . GLU   A 1  113 ? 42.247  77.152  42.494  1.00 53.96  ? 113 GLU   A O     1 
ATOM   882   C  CB    . GLU   A 1  113 ? 41.440  74.292  42.134  1.00 53.25  ? 113 GLU   A CB    1 
ATOM   883   C  CG    . GLU   A 1  113 ? 41.441  75.059  40.811  1.00 61.22  ? 113 GLU   A CG    1 
ATOM   884   C  CD    . GLU   A 1  113 ? 40.246  74.727  39.902  1.00 74.95  ? 113 GLU   A CD    1 
ATOM   885   O  OE1   . GLU   A 1  113 ? 39.617  73.658  40.048  1.00 64.53  ? 113 GLU   A OE1   1 
ATOM   886   O  OE2   . GLU   A 1  113 ? 39.925  75.549  39.023  1.00 76.10  ? 113 GLU   A OE2   1 
ATOM   887   N  N     . ILE   A 1  114 ? 41.491  76.786  44.573  1.00 47.69  ? 114 ILE   A N     1 
ATOM   888   C  CA    . ILE   A 1  114 ? 41.160  78.206  44.714  1.00 53.03  ? 114 ILE   A CA    1 
ATOM   889   C  C     . ILE   A 1  114 ? 41.264  78.672  46.155  1.00 43.30  ? 114 ILE   A C     1 
ATOM   890   O  O     . ILE   A 1  114 ? 40.677  79.693  46.516  1.00 48.66  ? 114 ILE   A O     1 
ATOM   891   C  CB    . ILE   A 1  114 ? 39.757  78.536  44.156  1.00 55.43  ? 114 ILE   A CB    1 
ATOM   892   C  CG1   . ILE   A 1  114 ? 39.589  80.039  43.939  1.00 44.18  ? 114 ILE   A CG1   1 
ATOM   893   C  CG2   . ILE   A 1  114 ? 38.646  78.091  45.109  1.00 44.08  ? 114 ILE   A CG2   1 
ATOM   894   C  CD1   . ILE   A 1  114 ? 38.162  80.401  43.690  1.00 35.88  ? 114 ILE   A CD1   1 
ATOM   895   N  N     . ILE   A 1  115 ? 42.026  77.962  46.980  1.00 48.20  ? 115 ILE   A N     1 
ATOM   896   C  CA    . ILE   A 1  115 ? 42.292  78.444  48.333  1.00 47.84  ? 115 ILE   A CA    1 
ATOM   897   C  C     . ILE   A 1  115 ? 43.223  79.647  48.310  1.00 49.03  ? 115 ILE   A C     1 
ATOM   898   O  O     . ILE   A 1  115 ? 42.910  80.702  48.868  1.00 47.00  ? 115 ILE   A O     1 
ATOM   899   C  CB    . ILE   A 1  115 ? 42.851  77.315  49.222  1.00 40.00  ? 115 ILE   A CB    1 
ATOM   900   C  CG1   . ILE   A 1  115 ? 43.267  77.894  50.568  1.00 40.71  ? 115 ILE   A CG1   1 
ATOM   901   C  CG2   . ILE   A 1  115 ? 44.004  76.629  48.564  1.00 49.01  ? 115 ILE   A CG2   1 
ATOM   902   C  CD1   . ILE   A 1  115 ? 42.124  78.152  51.490  1.00 35.84  ? 115 ILE   A CD1   1 
ATOM   903   N  N     . ASP   A 1  116 ? 44.367  79.522  47.635  1.00 51.32  ? 116 ASP   A N     1 
ATOM   904   C  CA    . ASP   A 1  116 ? 45.339  80.610  47.647  1.00 46.26  ? 116 ASP   A CA    1 
ATOM   905   C  C     . ASP   A 1  116 ? 44.746  81.904  47.096  1.00 41.24  ? 116 ASP   A C     1 
ATOM   906   O  O     . ASP   A 1  116 ? 44.939  82.976  47.676  1.00 44.24  ? 116 ASP   A O     1 
ATOM   907   C  CB    . ASP   A 1  116 ? 46.598  80.204  46.881  1.00 39.43  ? 116 ASP   A CB    1 
ATOM   908   C  CG    . ASP   A 1  116 ? 47.325  79.042  47.537  1.00 50.97  ? 116 ASP   A CG    1 
ATOM   909   O  OD1   . ASP   A 1  116 ? 47.540  79.069  48.774  1.00 48.72  ? 116 ASP   A OD1   1 
ATOM   910   O  OD2   . ASP   A 1  116 ? 47.685  78.092  46.815  1.00 71.22  ? 116 ASP   A OD2   1 
ATOM   911   N  N     . LEU   A 1  117 ? 44.009  81.836  45.992  1.00 41.56  ? 117 LEU   A N     1 
ATOM   912   C  CA    . LEU   A 1  117 ? 43.413  83.070  45.490  1.00 41.59  ? 117 LEU   A CA    1 
ATOM   913   C  C     . LEU   A 1  117 ? 42.503  83.699  46.536  1.00 48.62  ? 117 LEU   A C     1 
ATOM   914   O  O     . LEU   A 1  117 ? 42.413  84.935  46.619  1.00 39.52  ? 117 LEU   A O     1 
ATOM   915   C  CB    . LEU   A 1  117 ? 42.647  82.807  44.202  1.00 30.69  ? 117 LEU   A CB    1 
ATOM   916   C  CG    . LEU   A 1  117 ? 41.676  83.919  43.822  1.00 42.55  ? 117 LEU   A CG    1 
ATOM   917   C  CD1   . LEU   A 1  117 ? 42.396  85.247  43.688  1.00 46.26  ? 117 LEU   A CD1   1 
ATOM   918   C  CD2   . LEU   A 1  117 ? 40.927  83.554  42.554  1.00 42.50  ? 117 LEU   A CD2   1 
ATOM   919   N  N     . VAL   A 1  118 ? 41.849  82.861  47.360  1.00 54.69  ? 118 VAL   A N     1 
ATOM   920   C  CA    . VAL   A 1  118 ? 40.991  83.356  48.440  1.00 43.51  ? 118 VAL   A CA    1 
ATOM   921   C  C     . VAL   A 1  118 ? 41.840  83.924  49.568  1.00 39.53  ? 118 VAL   A C     1 
ATOM   922   O  O     . VAL   A 1  118 ? 41.625  85.057  50.012  1.00 36.10  ? 118 VAL   A O     1 
ATOM   923   C  CB    . VAL   A 1  118 ? 40.035  82.247  48.940  1.00 41.41  ? 118 VAL   A CB    1 
ATOM   924   C  CG1   . VAL   A 1  118 ? 39.704  82.383  50.431  1.00 45.14  ? 118 VAL   A CG1   1 
ATOM   925   C  CG2   . VAL   A 1  118 ? 38.732  82.285  48.159  1.00 44.75  ? 118 VAL   A CG2   1 
ATOM   926   N  N     . LEU   A 1  119 ? 42.831  83.157  50.029  1.00 41.05  ? 119 LEU   A N     1 
ATOM   927   C  CA    . LEU   A 1  119 ? 43.701  83.637  51.095  1.00 31.76  ? 119 LEU   A CA    1 
ATOM   928   C  C     . LEU   A 1  119 ? 44.350  84.959  50.719  1.00 42.13  ? 119 LEU   A C     1 
ATOM   929   O  O     . LEU   A 1  119 ? 44.332  85.913  51.504  1.00 51.96  ? 119 LEU   A O     1 
ATOM   930   C  CB    . LEU   A 1  119 ? 44.764  82.601  51.416  1.00 34.01  ? 119 LEU   A CB    1 
ATOM   931   C  CG    . LEU   A 1  119 ? 44.262  81.542  52.375  1.00 36.20  ? 119 LEU   A CG    1 
ATOM   932   C  CD1   . LEU   A 1  119 ? 45.414  80.709  52.885  1.00 43.72  ? 119 LEU   A CD1   1 
ATOM   933   C  CD2   . LEU   A 1  119 ? 43.549  82.232  53.487  1.00 34.60  ? 119 LEU   A CD2   1 
ATOM   934   N  N     . ASP   A 1  120 ? 44.946  85.032  49.529  1.00 44.71  ? 120 ASP   A N     1 
ATOM   935   C  CA    . ASP   A 1  120 ? 45.492  86.293  49.038  1.00 41.82  ? 120 ASP   A CA    1 
ATOM   936   C  C     . ASP   A 1  120 ? 44.423  87.373  49.138  1.00 45.75  ? 120 ASP   A C     1 
ATOM   937   O  O     . ASP   A 1  120 ? 44.579  88.334  49.894  1.00 46.99  ? 120 ASP   A O     1 
ATOM   938   C  CB    . ASP   A 1  120 ? 45.981  86.174  47.586  1.00 56.43  ? 120 ASP   A CB    1 
ATOM   939   C  CG    . ASP   A 1  120 ? 47.460  85.771  47.471  1.00 67.26  ? 120 ASP   A CG    1 
ATOM   940   O  OD1   . ASP   A 1  120 ? 48.068  85.330  48.478  1.00 61.08  ? 120 ASP   A OD1   1 
ATOM   941   O  OD2   . ASP   A 1  120 ? 48.014  85.901  46.355  1.00 71.53  ? 120 ASP   A OD2   1 
ATOM   942   N  N     . ARG   A 1  121 ? 43.324  87.219  48.385  1.00 53.38  ? 121 ARG   A N     1 
ATOM   943   C  CA    . ARG   A 1  121 ? 42.265  88.229  48.370  1.00 49.46  ? 121 ARG   A CA    1 
ATOM   944   C  C     . ARG   A 1  121 ? 41.884  88.685  49.780  1.00 46.49  ? 121 ARG   A C     1 
ATOM   945   O  O     . ARG   A 1  121 ? 41.406  89.813  49.963  1.00 36.91  ? 121 ARG   A O     1 
ATOM   946   C  CB    . ARG   A 1  121 ? 41.046  87.676  47.630  1.00 46.07  ? 121 ARG   A CB    1 
ATOM   947   C  CG    . ARG   A 1  121 ? 40.130  88.738  47.072  1.00 49.16  ? 121 ARG   A CG    1 
ATOM   948   C  CD    . ARG   A 1  121 ? 40.815  89.542  45.961  1.00 61.80  ? 121 ARG   A CD    1 
ATOM   949   N  NE    . ARG   A 1  121 ? 40.311  89.216  44.630  1.00 67.79  ? 121 ARG   A NE    1 
ATOM   950   C  CZ    . ARG   A 1  121 ? 41.032  88.662  43.663  1.00 70.06  ? 121 ARG   A CZ    1 
ATOM   951   N  NH1   . ARG   A 1  121 ? 42.310  88.365  43.837  1.00 67.92  ? 121 ARG   A NH1   1 
ATOM   952   N  NH2   . ARG   A 1  121 ? 40.457  88.407  42.490  1.00 68.67  ? 121 ARG   A NH2   1 
ATOM   953   N  N     . ILE   A 1  122 ? 42.112  87.828  50.782  1.00 46.08  ? 122 ILE   A N     1 
ATOM   954   C  CA    . ILE   A 1  122 ? 41.758  88.126  52.170  1.00 43.27  ? 122 ILE   A CA    1 
ATOM   955   C  C     . ILE   A 1  122 ? 42.842  88.972  52.836  1.00 41.07  ? 122 ILE   A C     1 
ATOM   956   O  O     . ILE   A 1  122 ? 42.540  89.981  53.482  1.00 32.31  ? 122 ILE   A O     1 
ATOM   957   C  CB    . ILE   A 1  122 ? 41.497  86.809  52.940  1.00 34.18  ? 122 ILE   A CB    1 
ATOM   958   C  CG1   . ILE   A 1  122 ? 39.998  86.462  52.951  1.00 29.72  ? 122 ILE   A CG1   1 
ATOM   959   C  CG2   . ILE   A 1  122 ? 42.169  86.826  54.334  1.00 29.09  ? 122 ILE   A CG2   1 
ATOM   960   C  CD1   . ILE   A 1  122 ? 39.685  85.069  53.456  1.00 31.38  ? 122 ILE   A CD1   1 
ATOM   961   N  N     . ARG   A 1  123 ? 44.118  88.570  52.692  1.00 42.63  ? 123 ARG   A N     1 
ATOM   962   C  CA    . ARG   A 1  123 ? 45.237  89.396  53.154  1.00 41.76  ? 123 ARG   A CA    1 
ATOM   963   C  C     . ARG   A 1  123 ? 45.153  90.833  52.649  1.00 42.32  ? 123 ARG   A C     1 
ATOM   964   O  O     . ARG   A 1  123 ? 45.596  91.759  53.339  1.00 38.47  ? 123 ARG   A O     1 
ATOM   965   C  CB    . ARG   A 1  123 ? 46.572  88.806  52.708  1.00 38.10  ? 123 ARG   A CB    1 
ATOM   966   C  CG    . ARG   A 1  123 ? 47.746  89.606  53.199  1.00 33.00  ? 123 ARG   A CG    1 
ATOM   967   C  CD    . ARG   A 1  123 ? 48.055  89.236  54.632  1.00 40.77  ? 123 ARG   A CD    1 
ATOM   968   N  NE    . ARG   A 1  123 ? 48.858  88.022  54.711  1.00 48.27  ? 123 ARG   A NE    1 
ATOM   969   C  CZ    . ARG   A 1  123 ? 48.951  87.248  55.784  1.00 64.62  ? 123 ARG   A CZ    1 
ATOM   970   N  NH1   . ARG   A 1  123 ? 48.268  87.510  56.889  1.00 53.92  ? 123 ARG   A NH1   1 
ATOM   971   N  NH2   . ARG   A 1  123 ? 49.746  86.180  55.747  1.00 72.14  ? 123 ARG   A NH2   1 
ATOM   972   N  N     . LYS   A 1  124 ? 44.632  91.039  51.434  1.00 37.39  ? 124 LYS   A N     1 
ATOM   973   C  CA    . LYS   A 1  124 ? 44.398  92.395  50.960  1.00 32.48  ? 124 LYS   A CA    1 
ATOM   974   C  C     . LYS   A 1  124 ? 43.657  93.221  52.017  1.00 45.12  ? 124 LYS   A C     1 
ATOM   975   O  O     . LYS   A 1  124 ? 44.047  94.357  52.313  1.00 51.28  ? 124 LYS   A O     1 
ATOM   976   C  CB    . LYS   A 1  124 ? 43.620  92.356  49.637  1.00 39.77  ? 124 LYS   A CB    1 
ATOM   977   C  CG    . LYS   A 1  124 ? 44.210  93.204  48.484  1.00 42.64  ? 124 LYS   A CG    1 
ATOM   978   C  CD    . LYS   A 1  124 ? 45.366  92.462  47.751  1.00 45.81  ? 124 LYS   A CD    1 
ATOM   979   C  CE    . LYS   A 1  124 ? 46.001  93.295  46.635  1.00 39.54  ? 124 LYS   A CE    1 
ATOM   980   N  NZ    . LYS   A 1  124 ? 46.283  92.477  45.414  1.00 36.25  ? 124 LYS   A NZ    1 
ATOM   981   N  N     . LEU   A 1  125 ? 42.597  92.653  52.616  1.00 44.55  ? 125 LEU   A N     1 
ATOM   982   C  CA    . LEU   A 1  125 ? 41.790  93.371  53.602  1.00 41.89  ? 125 LEU   A CA    1 
ATOM   983   C  C     . LEU   A 1  125 ? 42.491  93.476  54.950  1.00 43.09  ? 125 LEU   A C     1 
ATOM   984   O  O     . LEU   A 1  125 ? 42.262  94.439  55.691  1.00 49.05  ? 125 LEU   A O     1 
ATOM   985   C  CB    . LEU   A 1  125 ? 40.433  92.681  53.798  1.00 36.83  ? 125 LEU   A CB    1 
ATOM   986   C  CG    . LEU   A 1  125 ? 39.324  92.761  52.743  1.00 33.68  ? 125 LEU   A CG    1 
ATOM   987   C  CD1   . LEU   A 1  125 ? 38.283  91.715  53.006  1.00 46.22  ? 125 LEU   A CD1   1 
ATOM   988   C  CD2   . LEU   A 1  125 ? 38.675  94.109  52.723  1.00 44.13  ? 125 LEU   A CD2   1 
ATOM   989   N  N     . ALA   A 1  126 ? 43.324  92.494  55.290  1.00 36.14  ? 126 ALA   A N     1 
ATOM   990   C  CA    . ALA   A 1  126 ? 44.028  92.514  56.564  1.00 41.61  ? 126 ALA   A CA    1 
ATOM   991   C  C     . ALA   A 1  126 ? 45.057  93.646  56.632  1.00 55.82  ? 126 ALA   A C     1 
ATOM   992   O  O     . ALA   A 1  126 ? 45.450  94.051  57.736  1.00 68.71  ? 126 ALA   A O     1 
ATOM   993   C  CB    . ALA   A 1  126 ? 44.680  91.144  56.801  1.00 30.22  ? 126 ALA   A CB    1 
ATOM   994   N  N     . ASP   A 1  127 ? 45.464  94.191  55.478  1.00 51.97  ? 127 ASP   A N     1 
ATOM   995   C  CA    . ASP   A 1  127 ? 46.478  95.242  55.426  1.00 47.50  ? 127 ASP   A CA    1 
ATOM   996   C  C     . ASP   A 1  127 ? 45.893  96.612  55.746  1.00 57.40  ? 127 ASP   A C     1 
ATOM   997   O  O     . ASP   A 1  127 ? 46.440  97.337  56.588  1.00 67.77  ? 127 ASP   A O     1 
ATOM   998   C  CB    . ASP   A 1  127 ? 47.141  95.258  54.056  1.00 45.70  ? 127 ASP   A CB    1 
ATOM   999   C  CG    . ASP   A 1  127 ? 47.905  93.988  53.775  1.00 54.56  ? 127 ASP   A CG    1 
ATOM   1000  O  OD1   . ASP   A 1  127 ? 48.072  93.205  54.744  1.00 56.50  ? 127 ASP   A OD1   1 
ATOM   1001  O  OD2   . ASP   A 1  127 ? 48.328  93.771  52.605  1.00 43.71  ? 127 ASP   A OD2   1 
ATOM   1002  N  N     . GLN   A 1  128 ? 44.789  96.995  55.083  1.00 53.37  ? 128 GLN   A N     1 
ATOM   1003  C  CA    . GLN   A 1  128 ? 44.097  98.252  55.403  1.00 59.67  ? 128 GLN   A CA    1 
ATOM   1004  C  C     . GLN   A 1  128 ? 43.386  98.171  56.757  1.00 52.64  ? 128 GLN   A C     1 
ATOM   1005  O  O     . GLN   A 1  128 ? 42.300  98.733  56.941  1.00 48.65  ? 128 GLN   A O     1 
ATOM   1006  C  CB    . GLN   A 1  128 ? 43.100  98.637  54.298  1.00 54.69  ? 128 GLN   A CB    1 
ATOM   1007  C  CG    . GLN   A 1  128 ? 42.406  97.469  53.589  1.00 58.57  ? 128 GLN   A CG    1 
ATOM   1008  C  CD    . GLN   A 1  128 ? 41.175  97.900  52.770  1.00 68.97  ? 128 GLN   A CD    1 
ATOM   1009  O  OE1   . GLN   A 1  128 ? 40.419  97.060  52.267  1.00 70.34  ? 128 GLN   A OE1   1 
ATOM   1010  N  NE2   . GLN   A 1  128 ? 40.965  99.211  52.653  1.00 68.67  ? 128 GLN   A NE2   1 
ATOM   1011  N  N     . CYS   A 1  129 ? 44.011  97.465  57.700  1.00 47.06  ? 129 CYS   A N     1 
ATOM   1012  C  CA    . CYS   A 1  129 ? 43.470  97.146  59.013  1.00 44.97  ? 129 CYS   A CA    1 
ATOM   1013  C  C     . CYS   A 1  129 ? 44.539  97.489  60.035  1.00 52.28  ? 129 CYS   A C     1 
ATOM   1014  O  O     . CYS   A 1  129 ? 45.585  96.828  60.078  1.00 52.96  ? 129 CYS   A O     1 
ATOM   1015  C  CB    . CYS   A 1  129 ? 43.115  95.655  59.131  1.00 45.95  ? 129 CYS   A CB    1 
ATOM   1016  S  SG    . CYS   A 1  129 ? 41.465  95.165  58.623  1.00 52.39  ? 129 CYS   A SG    1 
ATOM   1017  N  N     . THR   A 1  130 ? 44.275  98.497  60.871  1.00 44.36  ? 130 THR   A N     1 
ATOM   1018  C  CA    . THR   A 1  130 ? 45.260  98.879  61.882  1.00 38.47  ? 130 THR   A CA    1 
ATOM   1019  C  C     . THR   A 1  130 ? 45.346  97.861  63.019  1.00 44.21  ? 130 THR   A C     1 
ATOM   1020  O  O     . THR   A 1  130 ? 46.418  97.688  63.612  1.00 44.87  ? 130 THR   A O     1 
ATOM   1021  C  CB    . THR   A 1  130 ? 44.939  100.269 62.441  1.00 38.36  ? 130 THR   A CB    1 
ATOM   1022  O  OG1   . THR   A 1  130 ? 43.939  100.158 63.463  1.00 59.57  ? 130 THR   A OG1   1 
ATOM   1023  C  CG2   . THR   A 1  130 ? 44.398  101.166 61.347  1.00 37.03  ? 130 THR   A CG2   1 
ATOM   1024  N  N     . GLY   A 1  131 ? 44.250  97.172  63.338  1.00 48.16  ? 131 GLY   A N     1 
ATOM   1025  C  CA    . GLY   A 1  131 ? 44.279  96.221  64.433  1.00 44.95  ? 131 GLY   A CA    1 
ATOM   1026  C  C     . GLY   A 1  131 ? 43.269  95.100  64.335  1.00 51.77  ? 131 GLY   A C     1 
ATOM   1027  O  O     . GLY   A 1  131 ? 42.651  94.712  65.339  1.00 53.00  ? 131 GLY   A O     1 
ATOM   1028  N  N     . LEU   A 1  132 ? 43.107  94.574  63.119  1.00 49.30  ? 132 LEU   A N     1 
ATOM   1029  C  CA    . LEU   A 1  132 ? 42.270  93.408  62.861  1.00 50.75  ? 132 LEU   A CA    1 
ATOM   1030  C  C     . LEU   A 1  132 ? 42.220  92.460  64.050  1.00 46.35  ? 132 LEU   A C     1 
ATOM   1031  O  O     . LEU   A 1  132 ? 43.259  92.025  64.558  1.00 39.18  ? 132 LEU   A O     1 
ATOM   1032  C  CB    . LEU   A 1  132 ? 42.775  92.646  61.641  1.00 54.91  ? 132 LEU   A CB    1 
ATOM   1033  C  CG    . LEU   A 1  132 ? 42.040  91.326  61.412  1.00 48.48  ? 132 LEU   A CG    1 
ATOM   1034  C  CD1   . LEU   A 1  132 ? 40.877  91.587  60.478  1.00 44.43  ? 132 LEU   A CD1   1 
ATOM   1035  C  CD2   . LEU   A 1  132 ? 42.978  90.262  60.866  1.00 37.13  ? 132 LEU   A CD2   1 
ATOM   1036  N  N     . GLN   A 1  133 ? 41.011  92.125  64.488  1.00 46.03  ? 133 GLN   A N     1 
ATOM   1037  C  CA    . GLN   A 1  133 ? 40.838  91.185  65.580  1.00 47.28  ? 133 GLN   A CA    1 
ATOM   1038  C  C     . GLN   A 1  133 ? 40.406  89.799  65.128  1.00 40.56  ? 133 GLN   A C     1 
ATOM   1039  O  O     . GLN   A 1  133 ? 40.619  88.829  65.861  1.00 41.05  ? 133 GLN   A O     1 
ATOM   1040  C  CB    . GLN   A 1  133 ? 39.819  91.732  66.581  1.00 44.73  ? 133 GLN   A CB    1 
ATOM   1041  C  CG    . GLN   A 1  133 ? 38.636  92.371  65.905  1.00 49.52  ? 133 GLN   A CG    1 
ATOM   1042  C  CD    . GLN   A 1  133 ? 37.629  92.876  66.900  1.00 44.48  ? 133 GLN   A CD    1 
ATOM   1043  O  OE1   . GLN   A 1  133 ? 37.507  92.344  68.006  1.00 41.08  ? 133 GLN   A OE1   1 
ATOM   1044  N  NE2   . GLN   A 1  133 ? 36.895  93.907  66.515  1.00 48.04  ? 133 GLN   A NE2   1 
ATOM   1045  N  N     . GLY   A 1  134 ? 39.823  89.669  63.950  1.00 48.58  ? 134 GLY   A N     1 
ATOM   1046  C  CA    . GLY   A 1  134 ? 39.461  88.341  63.505  1.00 44.91  ? 134 GLY   A CA    1 
ATOM   1047  C  C     . GLY   A 1  134 ? 38.345  88.380  62.477  1.00 45.38  ? 134 GLY   A C     1 
ATOM   1048  O  O     . GLY   A 1  134 ? 38.091  89.409  61.836  1.00 44.64  ? 134 GLY   A O     1 
ATOM   1049  N  N     . PHE   A 1  135 ? 37.689  87.228  62.343  1.00 45.16  ? 135 PHE   A N     1 
ATOM   1050  C  CA    . PHE   A 1  135 ? 36.786  86.988  61.234  1.00 40.11  ? 135 PHE   A CA    1 
ATOM   1051  C  C     . PHE   A 1  135 ? 35.488  86.384  61.735  1.00 35.75  ? 135 PHE   A C     1 
ATOM   1052  O  O     . PHE   A 1  135 ? 35.456  85.644  62.725  1.00 29.91  ? 135 PHE   A O     1 
ATOM   1053  C  CB    . PHE   A 1  135 ? 37.395  86.031  60.166  1.00 35.75  ? 135 PHE   A CB    1 
ATOM   1054  C  CG    . PHE   A 1  135 ? 38.891  86.150  59.991  1.00 38.49  ? 135 PHE   A CG    1 
ATOM   1055  C  CD1   . PHE   A 1  135 ? 39.443  87.188  59.253  1.00 29.24  ? 135 PHE   A CD1   1 
ATOM   1056  C  CD2   . PHE   A 1  135 ? 39.747  85.199  60.555  1.00 40.08  ? 135 PHE   A CD2   1 
ATOM   1057  C  CE1   . PHE   A 1  135 ? 40.815  87.284  59.099  1.00 30.01  ? 135 PHE   A CE1   1 
ATOM   1058  C  CE2   . PHE   A 1  135 ? 41.131  85.291  60.397  1.00 29.41  ? 135 PHE   A CE2   1 
ATOM   1059  C  CZ    . PHE   A 1  135 ? 41.659  86.325  59.669  1.00 29.27  ? 135 PHE   A CZ    1 
ATOM   1060  N  N     . LEU   A 1  136 ? 34.426  86.729  61.016  1.00 39.00  ? 136 LEU   A N     1 
ATOM   1061  C  CA    A LEU   A 1  136 ? 33.122  86.089  61.125  0.95 35.05  ? 136 LEU   A CA    1 
ATOM   1062  C  CA    B LEU   A 1  136 ? 33.127  86.083  61.128  0.05 35.05  ? 136 LEU   A CA    1 
ATOM   1063  C  C     . LEU   A 1  136 ? 32.886  85.312  59.836  1.00 35.01  ? 136 LEU   A C     1 
ATOM   1064  O  O     . LEU   A 1  136 ? 32.938  85.889  58.745  1.00 38.00  ? 136 LEU   A O     1 
ATOM   1065  C  CB    A LEU   A 1  136 ? 32.023  87.132  61.350  0.95 34.51  ? 136 LEU   A CB    1 
ATOM   1066  C  CB    B LEU   A 1  136 ? 32.023  87.112  61.372  0.05 34.47  ? 136 LEU   A CB    1 
ATOM   1067  C  CG    A LEU   A 1  136 ? 32.081  88.029  62.599  0.95 31.26  ? 136 LEU   A CG    1 
ATOM   1068  C  CG    B LEU   A 1  136 ? 32.271  88.108  62.509  0.05 31.68  ? 136 LEU   A CG    1 
ATOM   1069  C  CD1   A LEU   A 1  136 ? 33.269  88.958  62.593  0.95 29.15  ? 136 LEU   A CD1   1 
ATOM   1070  C  CD1   B LEU   A 1  136 ? 31.104  89.073  62.635  0.05 30.80  ? 136 LEU   A CD1   1 
ATOM   1071  C  CD2   A LEU   A 1  136 ? 30.813  88.830  62.690  0.95 29.71  ? 136 LEU   A CD2   1 
ATOM   1072  C  CD2   B LEU   A 1  136 ? 32.521  87.387  63.826  0.05 32.30  ? 136 LEU   A CD2   1 
ATOM   1073  N  N     . VAL   A 1  137 ? 32.646  84.012  59.953  1.00 35.90  ? 137 VAL   A N     1 
ATOM   1074  C  CA    . VAL   A 1  137 ? 32.492  83.146  58.787  1.00 36.88  ? 137 VAL   A CA    1 
ATOM   1075  C  C     . VAL   A 1  137 ? 31.029  82.718  58.669  1.00 37.84  ? 137 VAL   A C     1 
ATOM   1076  O  O     . VAL   A 1  137 ? 30.494  82.070  59.577  1.00 36.78  ? 137 VAL   A O     1 
ATOM   1077  C  CB    . VAL   A 1  137 ? 33.427  81.934  58.884  1.00 31.19  ? 137 VAL   A CB    1 
ATOM   1078  C  CG1   . VAL   A 1  137 ? 33.159  80.951  57.747  1.00 26.07  ? 137 VAL   A CG1   1 
ATOM   1079  C  CG2   . VAL   A 1  137 ? 34.859  82.402  58.865  1.00 30.68  ? 137 VAL   A CG2   1 
ATOM   1080  N  N     . PHE   A 1  138 ? 30.387  83.071  57.546  1.00 34.36  ? 138 PHE   A N     1 
ATOM   1081  C  CA    . PHE   A 1  138 ? 28.993  82.717  57.266  1.00 30.20  ? 138 PHE   A CA    1 
ATOM   1082  C  C     . PHE   A 1  138 ? 28.928  81.592  56.232  1.00 30.24  ? 138 PHE   A C     1 
ATOM   1083  O  O     . PHE   A 1  138 ? 29.345  81.778  55.088  1.00 27.87  ? 138 PHE   A O     1 
ATOM   1084  C  CB    . PHE   A 1  138 ? 28.205  83.915  56.737  1.00 22.61  ? 138 PHE   A CB    1 
ATOM   1085  C  CG    . PHE   A 1  138 ? 28.126  85.061  57.675  1.00 28.31  ? 138 PHE   A CG    1 
ATOM   1086  C  CD1   . PHE   A 1  138 ? 29.185  85.930  57.816  1.00 35.75  ? 138 PHE   A CD1   1 
ATOM   1087  C  CD2   . PHE   A 1  138 ? 26.973  85.311  58.390  1.00 32.38  ? 138 PHE   A CD2   1 
ATOM   1088  C  CE1   . PHE   A 1  138 ? 29.100  87.023  58.676  1.00 34.63  ? 138 PHE   A CE1   1 
ATOM   1089  C  CE2   . PHE   A 1  138 ? 26.889  86.402  59.257  1.00 34.66  ? 138 PHE   A CE2   1 
ATOM   1090  C  CZ    . PHE   A 1  138 ? 27.954  87.255  59.398  1.00 28.43  ? 138 PHE   A CZ    1 
ATOM   1091  N  N     . HIS   A 1  139 ? 28.353  80.453  56.614  1.00 32.88  ? 139 HIS   A N     1 
ATOM   1092  C  CA    . HIS   A 1  139 ? 28.214  79.328  55.699  1.00 24.20  ? 139 HIS   A CA    1 
ATOM   1093  C  C     . HIS   A 1  139 ? 27.068  78.418  56.131  1.00 28.99  ? 139 HIS   A C     1 
ATOM   1094  O  O     . HIS   A 1  139 ? 26.573  78.485  57.267  1.00 31.48  ? 139 HIS   A O     1 
ATOM   1095  C  CB    . HIS   A 1  139 ? 29.506  78.525  55.632  1.00 25.04  ? 139 HIS   A CB    1 
ATOM   1096  C  CG    . HIS   A 1  139 ? 29.936  77.942  56.950  1.00 26.53  ? 139 HIS   A CG    1 
ATOM   1097  N  ND1   . HIS   A 1  139 ? 29.807  76.603  57.257  1.00 22.52  ? 139 HIS   A ND1   1 
ATOM   1098  C  CD2   . HIS   A 1  139 ? 30.532  78.513  58.022  1.00 25.16  ? 139 HIS   A CD2   1 
ATOM   1099  C  CE1   . HIS   A 1  139 ? 30.307  76.375  58.455  1.00 19.82  ? 139 HIS   A CE1   1 
ATOM   1100  N  NE2   . HIS   A 1  139 ? 30.756  77.518  58.940  1.00 21.28  ? 139 HIS   A NE2   1 
ATOM   1101  N  N     . SER   A 1  140 ? 26.665  77.547  55.208  1.00 25.13  ? 140 SER   A N     1 
ATOM   1102  C  CA    . SER   A 1  140 ? 25.829  76.388  55.495  1.00 25.44  ? 140 SER   A CA    1 
ATOM   1103  C  C     . SER   A 1  140 ? 26.688  75.161  55.812  1.00 23.16  ? 140 SER   A C     1 
ATOM   1104  O  O     . SER   A 1  140 ? 27.841  75.059  55.395  1.00 27.64  ? 140 SER   A O     1 
ATOM   1105  C  CB    . SER   A 1  140 ? 24.916  76.070  54.310  1.00 27.40  ? 140 SER   A CB    1 
ATOM   1106  O  OG    . SER   A 1  140 ? 25.623  75.442  53.250  1.00 23.84  ? 140 SER   A OG    1 
ATOM   1107  N  N     . PHE   A 1  141 ? 26.104  74.221  56.566  1.00 28.26  ? 141 PHE   A N     1 
ATOM   1108  C  CA    . PHE   A 1  141 ? 26.725  72.913  56.774  1.00 25.96  ? 141 PHE   A CA    1 
ATOM   1109  C  C     . PHE   A 1  141 ? 26.552  71.989  55.561  1.00 30.89  ? 141 PHE   A C     1 
ATOM   1110  O  O     . PHE   A 1  141 ? 27.442  71.191  55.261  1.00 30.19  ? 141 PHE   A O     1 
ATOM   1111  C  CB    . PHE   A 1  141 ? 26.114  72.208  57.983  1.00 21.44  ? 141 PHE   A CB    1 
ATOM   1112  C  CG    . PHE   A 1  141 ? 26.605  72.675  59.304  1.00 23.39  ? 141 PHE   A CG    1 
ATOM   1113  C  CD1   . PHE   A 1  141 ? 27.489  73.718  59.422  1.00 27.58  ? 141 PHE   A CD1   1 
ATOM   1114  C  CD2   . PHE   A 1  141 ? 26.180  72.028  60.465  1.00 21.87  ? 141 PHE   A CD2   1 
ATOM   1115  C  CE1   . PHE   A 1  141 ? 27.937  74.106  60.697  1.00 26.90  ? 141 PHE   A CE1   1 
ATOM   1116  C  CE2   . PHE   A 1  141 ? 26.621  72.422  61.720  1.00 19.27  ? 141 PHE   A CE2   1 
ATOM   1117  C  CZ    . PHE   A 1  141 ? 27.494  73.456  61.836  1.00 15.37  ? 141 PHE   A CZ    1 
ATOM   1118  N  N     . GLY   A 1  142 ? 25.408  72.063  54.865  1.00 24.18  ? 142 GLY   A N     1 
ATOM   1119  C  CA    . GLY   A 1  142 ? 25.020  70.992  53.955  1.00 25.42  ? 142 GLY   A CA    1 
ATOM   1120  C  C     . GLY   A 1  142 ? 25.604  71.012  52.554  1.00 28.34  ? 142 GLY   A C     1 
ATOM   1121  O  O     . GLY   A 1  142 ? 25.814  69.950  51.961  1.00 27.25  ? 142 GLY   A O     1 
ATOM   1122  N  N     . GLY   A 1  143 ? 25.870  72.184  52.002  1.00 24.40  ? 143 GLY   A N     1 
ATOM   1123  C  CA    . GLY   A 1  143 ? 26.364  72.256  50.644  1.00 25.63  ? 143 GLY   A CA    1 
ATOM   1124  C  C     . GLY   A 1  143 ? 27.836  71.881  50.487  1.00 27.50  ? 143 GLY   A C     1 
ATOM   1125  O  O     . GLY   A 1  143 ? 28.590  71.712  51.449  1.00 29.80  ? 143 GLY   A O     1 
ATOM   1126  N  N     . GLY   A 1  144 ? 28.249  71.747  49.218  1.00 29.71  ? 144 GLY   A N     1 
ATOM   1127  C  CA    . GLY   A 1  144 ? 29.623  71.410  48.888  1.00 25.83  ? 144 GLY   A CA    1 
ATOM   1128  C  C     . GLY   A 1  144 ? 30.630  72.452  49.355  1.00 33.67  ? 144 GLY   A C     1 
ATOM   1129  O  O     . GLY   A 1  144 ? 31.486  72.161  50.207  1.00 31.24  ? 144 GLY   A O     1 
ATOM   1130  N  N     . THR   A 1  145 ? 30.548  73.660  48.783  1.00 26.16  ? 145 THR   A N     1 
ATOM   1131  C  CA    . THR   A 1  145 ? 31.382  74.769  49.223  1.00 19.20  ? 145 THR   A CA    1 
ATOM   1132  C  C     . THR   A 1  145 ? 31.198  75.038  50.712  1.00 28.86  ? 145 THR   A C     1 
ATOM   1133  O  O     . THR   A 1  145 ? 32.162  75.034  51.485  1.00 35.02  ? 145 THR   A O     1 
ATOM   1134  C  CB    . THR   A 1  145 ? 31.040  76.024  48.426  1.00 24.42  ? 145 THR   A CB    1 
ATOM   1135  O  OG1   . THR   A 1  145 ? 30.866  75.701  47.044  1.00 25.54  ? 145 THR   A OG1   1 
ATOM   1136  C  CG2   . THR   A 1  145 ? 32.142  77.050  48.556  1.00 32.83  ? 145 THR   A CG2   1 
ATOM   1137  N  N     . GLY   A 1  146 ? 29.957  75.285  51.129  1.00 32.52  ? 146 GLY   A N     1 
ATOM   1138  C  CA    . GLY   A 1  146 ? 29.710  75.730  52.495  1.00 28.12  ? 146 GLY   A CA    1 
ATOM   1139  C  C     . GLY   A 1  146 ? 30.380  74.866  53.544  1.00 25.36  ? 146 GLY   A C     1 
ATOM   1140  O  O     . GLY   A 1  146 ? 30.917  75.370  54.531  1.00 28.11  ? 146 GLY   A O     1 
ATOM   1141  N  N     . SER   A 1  147 ? 30.358  73.556  53.351  1.00 26.89  ? 147 SER   A N     1 
ATOM   1142  C  CA    . SER   A 1  147 ? 30.977  72.637  54.297  1.00 31.76  ? 147 SER   A CA    1 
ATOM   1143  C  C     . SER   A 1  147 ? 32.466  72.422  54.013  1.00 33.13  ? 147 SER   A C     1 
ATOM   1144  O  O     . SER   A 1  147 ? 33.297  72.524  54.923  1.00 30.79  ? 147 SER   A O     1 
ATOM   1145  C  CB    . SER   A 1  147 ? 30.229  71.294  54.270  1.00 32.09  ? 147 SER   A CB    1 
ATOM   1146  O  OG    . SER   A 1  147 ? 30.115  70.785  52.944  1.00 30.37  ? 147 SER   A OG    1 
ATOM   1147  N  N     . GLY   A 1  148 ? 32.817  72.136  52.759  1.00 29.53  ? 148 GLY   A N     1 
ATOM   1148  C  CA    . GLY   A 1  148 ? 34.140  71.651  52.437  1.00 28.13  ? 148 GLY   A CA    1 
ATOM   1149  C  C     . GLY   A 1  148 ? 35.186  72.712  52.170  1.00 33.22  ? 148 GLY   A C     1 
ATOM   1150  O  O     . GLY   A 1  148 ? 36.356  72.531  52.524  1.00 39.02  ? 148 GLY   A O     1 
ATOM   1151  N  N     . PHE   A 1  149 ? 34.818  73.813  51.524  1.00 24.68  ? 149 PHE   A N     1 
ATOM   1152  C  CA    . PHE   A 1  149 ? 35.798  74.878  51.408  1.00 29.28  ? 149 PHE   A CA    1 
ATOM   1153  C  C     . PHE   A 1  149 ? 36.041  75.546  52.755  1.00 38.66  ? 149 PHE   A C     1 
ATOM   1154  O  O     . PHE   A 1  149 ? 37.191  75.729  53.179  1.00 35.35  ? 149 PHE   A O     1 
ATOM   1155  C  CB    . PHE   A 1  149 ? 35.359  75.913  50.400  1.00 30.25  ? 149 PHE   A CB    1 
ATOM   1156  C  CG    . PHE   A 1  149 ? 36.423  76.899  50.098  1.00 32.05  ? 149 PHE   A CG    1 
ATOM   1157  C  CD1   . PHE   A 1  149 ? 37.592  76.494  49.480  1.00 38.29  ? 149 PHE   A CD1   1 
ATOM   1158  C  CD2   . PHE   A 1  149 ? 36.276  78.216  50.445  1.00 35.30  ? 149 PHE   A CD2   1 
ATOM   1159  C  CE1   . PHE   A 1  149 ? 38.589  77.403  49.191  1.00 46.76  ? 149 PHE   A CE1   1 
ATOM   1160  C  CE2   . PHE   A 1  149 ? 37.263  79.133  50.155  1.00 45.75  ? 149 PHE   A CE2   1 
ATOM   1161  C  CZ    . PHE   A 1  149 ? 38.425  78.730  49.524  1.00 42.60  ? 149 PHE   A CZ    1 
ATOM   1162  N  N     . THR   A 1  150 ? 34.960  75.921  53.438  1.00 39.01  ? 150 THR   A N     1 
ATOM   1163  C  CA    . THR   A 1  150 ? 35.069  76.636  54.703  1.00 30.14  ? 150 THR   A CA    1 
ATOM   1164  C  C     . THR   A 1  150 ? 36.061  75.968  55.645  1.00 27.71  ? 150 THR   A C     1 
ATOM   1165  O  O     . THR   A 1  150 ? 36.916  76.635  56.235  1.00 29.35  ? 150 THR   A O     1 
ATOM   1166  C  CB    . THR   A 1  150 ? 33.694  76.739  55.351  1.00 28.51  ? 150 THR   A CB    1 
ATOM   1167  O  OG1   . THR   A 1  150 ? 32.931  77.764  54.687  1.00 27.69  ? 150 THR   A OG1   1 
ATOM   1168  C  CG2   . THR   A 1  150 ? 33.851  77.050  56.819  1.00 26.93  ? 150 THR   A CG2   1 
ATOM   1169  N  N     . SER   A 1  151 ? 35.967  74.646  55.794  1.00 28.49  ? 151 SER   A N     1 
ATOM   1170  C  CA    . SER   A 1  151 ? 36.891  73.940  56.680  1.00 29.22  ? 151 SER   A CA    1 
ATOM   1171  C  C     . SER   A 1  151 ? 38.323  74.026  56.164  1.00 40.94  ? 151 SER   A C     1 
ATOM   1172  O  O     . SER   A 1  151 ? 39.270  74.151  56.950  1.00 43.60  ? 151 SER   A O     1 
ATOM   1173  C  CB    . SER   A 1  151 ? 36.466  72.479  56.844  1.00 32.25  ? 151 SER   A CB    1 
ATOM   1174  O  OG    . SER   A 1  151 ? 36.852  71.676  55.742  1.00 29.14  ? 151 SER   A OG    1 
ATOM   1175  N  N     . LEU   A 1  152 ? 38.502  73.932  54.845  1.00 43.40  ? 152 LEU   A N     1 
ATOM   1176  C  CA    . LEU   A 1  152 ? 39.788  74.255  54.241  1.00 38.53  ? 152 LEU   A CA    1 
ATOM   1177  C  C     . LEU   A 1  152 ? 40.230  75.666  54.620  1.00 38.36  ? 152 LEU   A C     1 
ATOM   1178  O  O     . LEU   A 1  152 ? 41.338  75.865  55.136  1.00 46.76  ? 152 LEU   A O     1 
ATOM   1179  C  CB    . LEU   A 1  152 ? 39.694  74.111  52.723  1.00 36.29  ? 152 LEU   A CB    1 
ATOM   1180  C  CG    . LEU   A 1  152 ? 40.947  74.528  51.961  1.00 33.49  ? 152 LEU   A CG    1 
ATOM   1181  C  CD1   . LEU   A 1  152 ? 42.133  73.670  52.416  1.00 32.82  ? 152 LEU   A CD1   1 
ATOM   1182  C  CD2   . LEU   A 1  152 ? 40.703  74.441  50.457  1.00 36.15  ? 152 LEU   A CD2   1 
ATOM   1183  N  N     . LEU   A 1  153 ? 39.370  76.662  54.374  1.00 35.14  ? 153 LEU   A N     1 
ATOM   1184  C  CA    . LEU   A 1  153 ? 39.736  78.048  54.663  1.00 36.30  ? 153 LEU   A CA    1 
ATOM   1185  C  C     . LEU   A 1  153 ? 39.994  78.260  56.153  1.00 32.08  ? 153 LEU   A C     1 
ATOM   1186  O  O     . LEU   A 1  153 ? 40.905  79.008  56.524  1.00 35.22  ? 153 LEU   A O     1 
ATOM   1187  C  CB    . LEU   A 1  153 ? 38.645  78.997  54.159  1.00 32.69  ? 153 LEU   A CB    1 
ATOM   1188  C  CG    . LEU   A 1  153 ? 38.867  80.493  54.370  1.00 33.01  ? 153 LEU   A CG    1 
ATOM   1189  C  CD1   . LEU   A 1  153 ? 40.336  80.756  54.294  1.00 36.20  ? 153 LEU   A CD1   1 
ATOM   1190  C  CD2   . LEU   A 1  153 ? 38.115  81.346  53.334  1.00 34.18  ? 153 LEU   A CD2   1 
ATOM   1191  N  N     . MET   A 1  154 ? 39.208  77.607  57.023  1.00 30.19  ? 154 MET   A N     1 
ATOM   1192  C  CA    . MET   A 1  154 ? 39.418  77.726  58.469  1.00 36.43  ? 154 MET   A CA    1 
ATOM   1193  C  C     . MET   A 1  154 ? 40.802  77.232  58.902  1.00 42.64  ? 154 MET   A C     1 
ATOM   1194  O  O     . MET   A 1  154 ? 41.310  77.652  59.948  1.00 36.34  ? 154 MET   A O     1 
ATOM   1195  C  CB    . MET   A 1  154 ? 38.340  76.953  59.238  1.00 29.78  ? 154 MET   A CB    1 
ATOM   1196  C  CG    . MET   A 1  154 ? 36.964  77.559  59.206  1.00 34.19  ? 154 MET   A CG    1 
ATOM   1197  S  SD    . MET   A 1  154 ? 36.889  79.200  59.973  1.00 31.07  ? 154 MET   A SD    1 
ATOM   1198  C  CE    . MET   A 1  154 ? 36.186  78.889  61.544  1.00 17.46  ? 154 MET   A CE    1 
ATOM   1199  N  N     . GLU   A 1  155 ? 41.417  76.324  58.143  1.00 48.31  ? 155 GLU   A N     1 
ATOM   1200  C  CA    . GLU   A 1  155 ? 42.718  75.806  58.552  1.00 44.65  ? 155 GLU   A CA    1 
ATOM   1201  C  C     . GLU   A 1  155 ? 43.846  76.693  58.041  1.00 43.04  ? 155 GLU   A C     1 
ATOM   1202  O  O     . GLU   A 1  155 ? 44.840  76.911  58.744  1.00 40.46  ? 155 GLU   A O     1 
ATOM   1203  C  CB    . GLU   A 1  155 ? 42.887  74.366  58.067  1.00 42.18  ? 155 GLU   A CB    1 
ATOM   1204  C  CG    . GLU   A 1  155 ? 42.253  73.307  58.971  1.00 45.93  ? 155 GLU   A CG    1 
ATOM   1205  C  CD    . GLU   A 1  155 ? 42.348  71.903  58.387  1.00 53.00  ? 155 GLU   A CD    1 
ATOM   1206  O  OE1   . GLU   A 1  155 ? 42.270  71.796  57.135  1.00 46.87  ? 155 GLU   A OE1   1 
ATOM   1207  O  OE2   . GLU   A 1  155 ? 42.506  70.928  59.177  1.00 43.88  ? 155 GLU   A OE2   1 
ATOM   1208  N  N     . ARG   A 1  156 ? 43.724  77.208  56.817  1.00 46.69  ? 156 ARG   A N     1 
ATOM   1209  C  CA    . ARG   A 1  156 ? 44.679  78.221  56.390  1.00 53.95  ? 156 ARG   A CA    1 
ATOM   1210  C  C     . ARG   A 1  156 ? 44.594  79.454  57.285  1.00 49.00  ? 156 ARG   A C     1 
ATOM   1211  O  O     . ARG   A 1  156 ? 45.611  80.113  57.537  1.00 45.74  ? 156 ARG   A O     1 
ATOM   1212  C  CB    . ARG   A 1  156 ? 44.454  78.580  54.915  1.00 43.15  ? 156 ARG   A CB    1 
ATOM   1213  C  CG    . ARG   A 1  156 ? 45.224  77.687  53.930  1.00 48.14  ? 156 ARG   A CG    1 
ATOM   1214  C  CD    . ARG   A 1  156 ? 46.726  78.026  53.837  1.00 47.36  ? 156 ARG   A CD    1 
ATOM   1215  N  NE    . ARG   A 1  156 ? 47.198  78.034  52.452  1.00 51.92  ? 156 ARG   A NE    1 
ATOM   1216  C  CZ    . ARG   A 1  156 ? 47.381  76.948  51.702  1.00 64.90  ? 156 ARG   A CZ    1 
ATOM   1217  N  NH1   . ARG   A 1  156 ? 47.132  75.730  52.170  1.00 64.08  ? 156 ARG   A NH1   1 
ATOM   1218  N  NH2   . ARG   A 1  156 ? 47.820  77.084  50.449  1.00 55.15  ? 156 ARG   A NH2   1 
ATOM   1219  N  N     . LEU   A 1  157 ? 43.405  79.768  57.804  1.00 43.81  ? 157 LEU   A N     1 
ATOM   1220  C  CA    . LEU   A 1  157 ? 43.294  80.968  58.625  1.00 44.05  ? 157 LEU   A CA    1 
ATOM   1221  C  C     . LEU   A 1  157 ? 43.973  80.774  59.979  1.00 44.22  ? 157 LEU   A C     1 
ATOM   1222  O  O     . LEU   A 1  157 ? 44.616  81.695  60.487  1.00 46.55  ? 157 LEU   A O     1 
ATOM   1223  C  CB    . LEU   A 1  157 ? 41.829  81.377  58.774  1.00 38.09  ? 157 LEU   A CB    1 
ATOM   1224  C  CG    . LEU   A 1  157 ? 41.173  81.980  57.525  1.00 38.38  ? 157 LEU   A CG    1 
ATOM   1225  C  CD1   . LEU   A 1  157 ? 39.856  82.704  57.851  1.00 28.76  ? 157 LEU   A CD1   1 
ATOM   1226  C  CD2   . LEU   A 1  157 ? 42.148  82.909  56.792  1.00 40.96  ? 157 LEU   A CD2   1 
ATOM   1227  N  N     . SER   A 1  158 ? 43.875  79.579  60.565  1.00 38.73  ? 158 SER   A N     1 
ATOM   1228  C  CA    . SER   A 1  158 ? 44.600  79.311  61.803  1.00 37.86  ? 158 SER   A CA    1 
ATOM   1229  C  C     . SER   A 1  158 ? 46.105  79.318  61.592  1.00 49.11  ? 158 SER   A C     1 
ATOM   1230  O  O     . SER   A 1  158 ? 46.869  79.496  62.549  1.00 65.60  ? 158 SER   A O     1 
ATOM   1231  C  CB    . SER   A 1  158 ? 44.180  77.969  62.392  1.00 43.39  ? 158 SER   A CB    1 
ATOM   1232  O  OG    . SER   A 1  158 ? 42.855  78.026  62.877  1.00 44.48  ? 158 SER   A OG    1 
ATOM   1233  N  N     . VAL   A 1  159 ? 46.537  79.104  60.361  1.00 53.27  ? 159 VAL   A N     1 
ATOM   1234  C  CA    . VAL   A 1  159 ? 47.942  79.203  60.008  1.00 54.15  ? 159 VAL   A CA    1 
ATOM   1235  C  C     . VAL   A 1  159 ? 48.326  80.658  59.757  1.00 53.05  ? 159 VAL   A C     1 
ATOM   1236  O  O     . VAL   A 1  159 ? 49.225  81.203  60.406  1.00 52.56  ? 159 VAL   A O     1 
ATOM   1237  C  CB    . VAL   A 1  159 ? 48.197  78.309  58.777  1.00 57.30  ? 159 VAL   A CB    1 
ATOM   1238  C  CG1   . VAL   A 1  159 ? 49.371  78.828  57.946  1.00 52.14  ? 159 VAL   A CG1   1 
ATOM   1239  C  CG2   . VAL   A 1  159 ? 48.364  76.839  59.201  1.00 48.76  ? 159 VAL   A CG2   1 
ATOM   1240  N  N     . ASP   A 1  160 ? 47.615  81.320  58.843  1.00 52.63  ? 160 ASP   A N     1 
ATOM   1241  C  CA    . ASP   A 1  160 ? 47.962  82.670  58.411  1.00 51.94  ? 160 ASP   A CA    1 
ATOM   1242  C  C     . ASP   A 1  160 ? 47.761  83.742  59.481  1.00 55.47  ? 160 ASP   A C     1 
ATOM   1243  O  O     . ASP   A 1  160 ? 48.366  84.814  59.365  1.00 61.16  ? 160 ASP   A O     1 
ATOM   1244  C  CB    . ASP   A 1  160 ? 47.127  83.050  57.191  1.00 54.67  ? 160 ASP   A CB    1 
ATOM   1245  C  CG    . ASP   A 1  160 ? 47.752  82.613  55.892  1.00 59.27  ? 160 ASP   A CG    1 
ATOM   1246  O  OD1   . ASP   A 1  160 ? 48.254  81.459  55.830  1.00 53.38  ? 160 ASP   A OD1   1 
ATOM   1247  O  OD2   . ASP   A 1  160 ? 47.720  83.435  54.939  1.00 50.59  ? 160 ASP   A OD2   1 
ATOM   1248  N  N     . TYR   A 1  161 ? 46.902  83.516  60.486  1.00 59.66  ? 161 TYR   A N     1 
ATOM   1249  C  CA    . TYR   A 1  161 ? 46.531  84.556  61.464  1.00 48.44  ? 161 TYR   A CA    1 
ATOM   1250  C  C     . TYR   A 1  161 ? 46.377  83.979  62.878  1.00 51.15  ? 161 TYR   A C     1 
ATOM   1251  O  O     . TYR   A 1  161 ? 45.364  84.158  63.546  1.00 53.97  ? 161 TYR   A O     1 
ATOM   1252  C  CB    . TYR   A 1  161 ? 45.235  85.251  61.057  1.00 30.97  ? 161 TYR   A CB    1 
ATOM   1253  C  CG    . TYR   A 1  161 ? 45.219  85.850  59.678  1.00 39.66  ? 161 TYR   A CG    1 
ATOM   1254  C  CD1   . TYR   A 1  161 ? 45.050  85.062  58.560  1.00 48.79  ? 161 TYR   A CD1   1 
ATOM   1255  C  CD2   . TYR   A 1  161 ? 45.321  87.217  59.493  1.00 43.19  ? 161 TYR   A CD2   1 
ATOM   1256  C  CE1   . TYR   A 1  161 ? 45.016  85.613  57.284  1.00 46.94  ? 161 TYR   A CE1   1 
ATOM   1257  C  CE2   . TYR   A 1  161 ? 45.284  87.779  58.220  1.00 45.01  ? 161 TYR   A CE2   1 
ATOM   1258  C  CZ    . TYR   A 1  161 ? 45.133  86.971  57.119  1.00 42.18  ? 161 TYR   A CZ    1 
ATOM   1259  O  OH    . TYR   A 1  161 ? 45.093  87.527  55.853  1.00 47.66  ? 161 TYR   A OH    1 
ATOM   1260  N  N     . GLY   A 1  162 ? 47.422  83.307  63.365  1.00 53.77  ? 162 GLY   A N     1 
ATOM   1261  C  CA    . GLY   A 1  162 ? 47.304  82.527  64.595  1.00 59.87  ? 162 GLY   A CA    1 
ATOM   1262  C  C     . GLY   A 1  162 ? 46.633  83.251  65.756  1.00 46.38  ? 162 GLY   A C     1 
ATOM   1263  O  O     . GLY   A 1  162 ? 45.796  82.678  66.456  1.00 44.57  ? 162 GLY   A O     1 
ATOM   1264  N  N     . LYS   A 1  163 ? 47.016  84.502  66.010  1.00 54.98  ? 163 LYS   A N     1 
ATOM   1265  C  CA    . LYS   A 1  163 ? 46.500  85.183  67.202  1.00 67.42  ? 163 LYS   A CA    1 
ATOM   1266  C  C     . LYS   A 1  163 ? 45.103  85.783  66.990  1.00 66.13  ? 163 LYS   A C     1 
ATOM   1267  O  O     . LYS   A 1  163 ? 44.650  86.577  67.831  1.00 52.98  ? 163 LYS   A O     1 
ATOM   1268  C  CB    . LYS   A 1  163 ? 47.471  86.279  67.696  1.00 52.11  ? 163 LYS   A CB    1 
ATOM   1269  C  CG    . LYS   A 1  163 ? 48.746  86.536  66.877  1.00 49.94  ? 163 LYS   A CG    1 
ATOM   1270  C  CD    . LYS   A 1  163 ? 48.478  87.389  65.644  1.00 51.22  ? 163 LYS   A CD    1 
ATOM   1271  C  CE    . LYS   A 1  163 ? 48.420  86.533  64.377  1.00 45.25  ? 163 LYS   A CE    1 
ATOM   1272  N  NZ    . LYS   A 1  163 ? 47.839  87.275  63.240  1.00 42.42  ? 163 LYS   A NZ    1 
ATOM   1273  N  N     . LYS   A 1  164 ? 44.406  85.398  65.917  1.00 54.95  ? 164 LYS   A N     1 
ATOM   1274  C  CA    . LYS   A 1  164 ? 43.144  86.015  65.536  1.00 49.47  ? 164 LYS   A CA    1 
ATOM   1275  C  C     . LYS   A 1  164 ? 41.947  85.140  65.902  1.00 49.22  ? 164 LYS   A C     1 
ATOM   1276  O  O     . LYS   A 1  164 ? 42.019  83.906  65.907  1.00 51.07  ? 164 LYS   A O     1 
ATOM   1277  C  CB    . LYS   A 1  164 ? 43.125  86.324  64.037  1.00 46.69  ? 164 LYS   A CB    1 
ATOM   1278  C  CG    . LYS   A 1  164 ? 43.522  87.746  63.691  1.00 46.35  ? 164 LYS   A CG    1 
ATOM   1279  C  CD    . LYS   A 1  164 ? 44.860  88.126  64.306  1.00 51.75  ? 164 LYS   A CD    1 
ATOM   1280  C  CE    . LYS   A 1  164 ? 45.217  89.568  63.976  1.00 56.08  ? 164 LYS   A CE    1 
ATOM   1281  N  NZ    . LYS   A 1  164 ? 45.666  90.328  65.170  1.00 62.84  ? 164 LYS   A NZ    1 
ATOM   1282  N  N     . SER   A 1  165 ? 40.839  85.810  66.212  1.00 49.38  ? 165 SER   A N     1 
ATOM   1283  C  CA    . SER   A 1  165 ? 39.582  85.158  66.543  1.00 44.54  ? 165 SER   A CA    1 
ATOM   1284  C  C     . SER   A 1  165 ? 38.807  84.796  65.277  1.00 44.48  ? 165 SER   A C     1 
ATOM   1285  O  O     . SER   A 1  165 ? 38.862  85.497  64.256  1.00 44.30  ? 165 SER   A O     1 
ATOM   1286  C  CB    . SER   A 1  165 ? 38.728  86.078  67.421  1.00 39.25  ? 165 SER   A CB    1 
ATOM   1287  O  OG    . SER   A 1  165 ? 38.668  85.604  68.754  1.00 40.09  ? 165 SER   A OG    1 
ATOM   1288  N  N     . LYS   A 1  166 ? 38.065  83.694  65.356  1.00 38.22  ? 166 LYS   A N     1 
ATOM   1289  C  CA    . LYS   A 1  166 ? 37.175  83.285  64.274  1.00 34.28  ? 166 LYS   A CA    1 
ATOM   1290  C  C     . LYS   A 1  166 ? 35.837  82.881  64.866  1.00 35.04  ? 166 LYS   A C     1 
ATOM   1291  O  O     . LYS   A 1  166 ? 35.773  81.977  65.711  1.00 34.26  ? 166 LYS   A O     1 
ATOM   1292  C  CB    . LYS   A 1  166 ? 37.781  82.136  63.471  1.00 31.28  ? 166 LYS   A CB    1 
ATOM   1293  C  CG    . LYS   A 1  166 ? 38.889  82.586  62.507  1.00 41.29  ? 166 LYS   A CG    1 
ATOM   1294  C  CD    . LYS   A 1  166 ? 39.772  81.427  62.070  1.00 30.73  ? 166 LYS   A CD    1 
ATOM   1295  C  CE    . LYS   A 1  166 ? 40.472  80.802  63.270  1.00 38.92  ? 166 LYS   A CE    1 
ATOM   1296  N  NZ    . LYS   A 1  166 ? 40.981  79.476  62.868  1.00 32.92  ? 166 LYS   A NZ    1 
ATOM   1297  N  N     . LEU   A 1  167 ? 34.782  83.574  64.437  1.00 33.48  ? 167 LEU   A N     1 
ATOM   1298  C  CA    . LEU   A 1  167 ? 33.402  83.274  64.806  1.00 36.98  ? 167 LEU   A CA    1 
ATOM   1299  C  C     . LEU   A 1  167 ? 32.659  82.694  63.613  1.00 36.75  ? 167 LEU   A C     1 
ATOM   1300  O  O     . LEU   A 1  167 ? 32.938  83.033  62.456  1.00 40.11  ? 167 LEU   A O     1 
ATOM   1301  C  CB    . LEU   A 1  167 ? 32.645  84.520  65.287  1.00 34.90  ? 167 LEU   A CB    1 
ATOM   1302  C  CG    . LEU   A 1  167 ? 32.709  84.948  66.754  1.00 36.18  ? 167 LEU   A CG    1 
ATOM   1303  C  CD1   . LEU   A 1  167 ? 34.130  85.301  67.179  1.00 30.07  ? 167 LEU   A CD1   1 
ATOM   1304  C  CD2   . LEU   A 1  167 ? 31.762  86.125  66.977  1.00 28.97  ? 167 LEU   A CD2   1 
ATOM   1305  N  N     . GLU   A 1  168 ? 31.684  81.847  63.900  1.00 32.84  ? 168 GLU   A N     1 
ATOM   1306  C  CA    . GLU   A 1  168 ? 30.885  81.235  62.854  1.00 29.33  ? 168 GLU   A CA    1 
ATOM   1307  C  C     . GLU   A 1  168 ? 29.418  81.565  63.023  1.00 29.17  ? 168 GLU   A C     1 
ATOM   1308  O  O     . GLU   A 1  168 ? 28.876  81.508  64.135  1.00 31.77  ? 168 GLU   A O     1 
ATOM   1309  C  CB    . GLU   A 1  168 ? 31.039  79.741  62.861  1.00 28.13  ? 168 GLU   A CB    1 
ATOM   1310  C  CG    . GLU   A 1  168 ? 32.320  79.281  62.296  1.00 24.66  ? 168 GLU   A CG    1 
ATOM   1311  C  CD    . GLU   A 1  168 ? 32.365  77.796  62.265  1.00 21.57  ? 168 GLU   A CD    1 
ATOM   1312  O  OE1   . GLU   A 1  168 ? 32.630  77.197  63.320  1.00 25.45  ? 168 GLU   A OE1   1 
ATOM   1313  O  OE2   . GLU   A 1  168 ? 32.085  77.228  61.198  1.00 22.57  ? 168 GLU   A OE2   1 
ATOM   1314  N  N     . PHE   A 1  169 ? 28.783  81.878  61.909  1.00 27.67  ? 169 PHE   A N     1 
ATOM   1315  C  CA    . PHE   A 1  169 ? 27.337  81.750  61.753  1.00 28.31  ? 169 PHE   A CA    1 
ATOM   1316  C  C     . PHE   A 1  169 ? 27.103  80.586  60.808  1.00 21.58  ? 169 PHE   A C     1 
ATOM   1317  O  O     . PHE   A 1  169 ? 27.473  80.658  59.634  1.00 28.20  ? 169 PHE   A O     1 
ATOM   1318  C  CB    . PHE   A 1  169 ? 26.731  83.051  61.239  1.00 24.76  ? 169 PHE   A CB    1 
ATOM   1319  C  CG    . PHE   A 1  169 ? 26.859  84.152  62.217  1.00 26.41  ? 169 PHE   A CG    1 
ATOM   1320  C  CD1   . PHE   A 1  169 ? 27.989  84.956  62.218  1.00 29.06  ? 169 PHE   A CD1   1 
ATOM   1321  C  CD2   . PHE   A 1  169 ? 25.891  84.330  63.202  1.00 18.22  ? 169 PHE   A CD2   1 
ATOM   1322  C  CE1   . PHE   A 1  169 ? 28.133  85.960  63.156  1.00 33.41  ? 169 PHE   A CE1   1 
ATOM   1323  C  CE2   . PHE   A 1  169 ? 26.019  85.312  64.126  1.00 22.77  ? 169 PHE   A CE2   1 
ATOM   1324  C  CZ    . PHE   A 1  169 ? 27.147  86.135  64.116  1.00 31.53  ? 169 PHE   A CZ    1 
ATOM   1325  N  N     . SER   A 1  170 ? 26.537  79.500  61.323  1.00 23.72  ? 170 SER   A N     1 
ATOM   1326  C  CA    . SER   A 1  170 ? 26.464  78.234  60.593  1.00 23.82  ? 170 SER   A CA    1 
ATOM   1327  C  C     . SER   A 1  170 ? 25.028  77.747  60.520  1.00 27.78  ? 170 SER   A C     1 
ATOM   1328  O  O     . SER   A 1  170 ? 24.339  77.659  61.545  1.00 25.78  ? 170 SER   A O     1 
ATOM   1329  C  CB    . SER   A 1  170 ? 27.319  77.154  61.243  1.00 18.40  ? 170 SER   A CB    1 
ATOM   1330  O  OG    . SER   A 1  170 ? 28.641  77.610  61.454  1.00 23.87  ? 170 SER   A OG    1 
ATOM   1331  N  N     . ILE   A 1  171 ? 24.598  77.399  59.312  1.00 30.33  ? 171 ILE   A N     1 
ATOM   1332  C  CA    . ILE   A 1  171 ? 23.214  77.040  59.023  1.00 25.40  ? 171 ILE   A CA    1 
ATOM   1333  C  C     . ILE   A 1  171 ? 23.100  75.517  59.033  1.00 22.35  ? 171 ILE   A C     1 
ATOM   1334  O  O     . ILE   A 1  171 ? 23.581  74.839  58.118  1.00 24.59  ? 171 ILE   A O     1 
ATOM   1335  C  CB    . ILE   A 1  171 ? 22.762  77.632  57.680  1.00 19.68  ? 171 ILE   A CB    1 
ATOM   1336  C  CG1   . ILE   A 1  171 ? 22.947  79.147  57.692  1.00 18.32  ? 171 ILE   A CG1   1 
ATOM   1337  C  CG2   . ILE   A 1  171 ? 21.312  77.283  57.408  1.00 20.82  ? 171 ILE   A CG2   1 
ATOM   1338  C  CD1   . ILE   A 1  171 ? 22.035  79.880  58.669  1.00 19.45  ? 171 ILE   A CD1   1 
ATOM   1339  N  N     . TYR   A 1  172 ? 22.456  74.977  60.068  1.00 18.44  ? 172 TYR   A N     1 
ATOM   1340  C  CA    . TYR   A 1  172 ? 22.229  73.556  60.317  1.00 19.12  ? 172 TYR   A CA    1 
ATOM   1341  C  C     . TYR   A 1  172 ? 21.145  73.049  59.375  1.00 17.73  ? 172 TYR   A C     1 
ATOM   1342  O  O     . TYR   A 1  172 ? 20.168  73.758  59.155  1.00 17.50  ? 172 TYR   A O     1 
ATOM   1343  C  CB    . TYR   A 1  172 ? 21.805  73.372  61.764  1.00 16.59  ? 172 TYR   A CB    1 
ATOM   1344  C  CG    . TYR   A 1  172 ? 21.567  71.971  62.284  1.00 16.13  ? 172 TYR   A CG    1 
ATOM   1345  C  CD1   . TYR   A 1  172 ? 20.345  71.346  62.105  1.00 17.95  ? 172 TYR   A CD1   1 
ATOM   1346  C  CD2   . TYR   A 1  172 ? 22.530  71.314  63.037  1.00 13.30  ? 172 TYR   A CD2   1 
ATOM   1347  C  CE1   . TYR   A 1  172 ? 20.106  70.096  62.621  1.00 17.45  ? 172 TYR   A CE1   1 
ATOM   1348  C  CE2   . TYR   A 1  172 ? 22.294  70.062  63.560  1.00 14.97  ? 172 TYR   A CE2   1 
ATOM   1349  C  CZ    . TYR   A 1  172 ? 21.080  69.457  63.342  1.00 18.33  ? 172 TYR   A CZ    1 
ATOM   1350  O  OH    . TYR   A 1  172 ? 20.818  68.202  63.833  1.00 23.17  ? 172 TYR   A OH    1 
ATOM   1351  N  N     . PRO   A 1  173 ? 21.283  71.837  58.814  1.00 16.86  ? 173 PRO   A N     1 
ATOM   1352  C  CA    . PRO   A 1  173 ? 20.430  71.448  57.686  1.00 13.28  ? 173 PRO   A CA    1 
ATOM   1353  C  C     . PRO   A 1  173 ? 19.053  71.027  58.148  1.00 20.92  ? 173 PRO   A C     1 
ATOM   1354  O  O     . PRO   A 1  173 ? 18.898  70.372  59.186  1.00 27.11  ? 173 PRO   A O     1 
ATOM   1355  C  CB    . PRO   A 1  173 ? 21.180  70.265  57.056  1.00 10.79  ? 173 PRO   A CB    1 
ATOM   1356  C  CG    . PRO   A 1  173 ? 22.324  69.976  57.975  1.00 16.12  ? 173 PRO   A CG    1 
ATOM   1357  C  CD    . PRO   A 1  173 ? 22.071  70.687  59.261  1.00 16.77  ? 173 PRO   A CD    1 
ATOM   1358  N  N     . ALA   A 1  174 ? 18.042  71.430  57.368  1.00 18.77  ? 174 ALA   A N     1 
ATOM   1359  C  CA    . ALA   A 1  174 ? 16.665  71.008  57.569  1.00 15.27  ? 174 ALA   A CA    1 
ATOM   1360  C  C     . ALA   A 1  174 ? 16.083  70.555  56.238  1.00 27.81  ? 174 ALA   A C     1 
ATOM   1361  O  O     . ALA   A 1  174 ? 16.337  71.179  55.192  1.00 25.81  ? 174 ALA   A O     1 
ATOM   1362  C  CB    . ALA   A 1  174 ? 15.819  72.133  58.151  1.00 16.49  ? 174 ALA   A CB    1 
ATOM   1363  N  N     . PRO   A 1  175 ? 15.320  69.461  56.236  1.00 29.84  ? 175 PRO   A N     1 
ATOM   1364  C  CA    . PRO   A 1  175 ? 14.842  68.924  54.959  1.00 24.30  ? 175 PRO   A CA    1 
ATOM   1365  C  C     . PRO   A 1  175 ? 13.798  69.795  54.297  1.00 23.51  ? 175 PRO   A C     1 
ATOM   1366  O  O     . PRO   A 1  175 ? 13.689  69.761  53.067  1.00 38.51  ? 175 PRO   A O     1 
ATOM   1367  C  CB    . PRO   A 1  175 ? 14.275  67.552  55.346  1.00 24.63  ? 175 PRO   A CB    1 
ATOM   1368  C  CG    . PRO   A 1  175 ? 14.786  67.266  56.697  1.00 19.59  ? 175 PRO   A CG    1 
ATOM   1369  C  CD    . PRO   A 1  175 ? 14.959  68.587  57.359  1.00 23.58  ? 175 PRO   A CD    1 
ATOM   1370  N  N     . GLN   A 1  176 ? 13.041  70.590  55.053  1.00 24.33  ? 176 GLN   A N     1 
ATOM   1371  C  CA    . GLN   A 1  176 ? 12.037  71.445  54.426  1.00 25.47  ? 176 GLN   A CA    1 
ATOM   1372  C  C     . GLN   A 1  176 ? 12.645  72.403  53.408  1.00 23.16  ? 176 GLN   A C     1 
ATOM   1373  O  O     . GLN   A 1  176 ? 11.908  72.980  52.605  1.00 33.64  ? 176 GLN   A O     1 
ATOM   1374  C  CB    . GLN   A 1  176 ? 11.265  72.263  55.476  1.00 24.43  ? 176 GLN   A CB    1 
ATOM   1375  C  CG    . GLN   A 1  176 ? 11.098  71.590  56.819  1.00 28.51  ? 176 GLN   A CG    1 
ATOM   1376  C  CD    . GLN   A 1  176 ? 9.668   71.653  57.314  1.00 37.82  ? 176 GLN   A CD    1 
ATOM   1377  O  OE1   . GLN   A 1  176 ? 8.744   71.306  56.582  1.00 48.40  ? 176 GLN   A OE1   1 
ATOM   1378  N  NE2   . GLN   A 1  176 ? 9.472   72.096  58.562  1.00 44.19  ? 176 GLN   A NE2   1 
ATOM   1379  N  N     . VAL   A 1  177 ? 13.956  72.624  53.439  1.00 26.11  ? 177 VAL   A N     1 
ATOM   1380  C  CA    . VAL   A 1  177 ? 14.575  73.536  52.482  1.00 25.46  ? 177 VAL   A CA    1 
ATOM   1381  C  C     . VAL   A 1  177 ? 15.896  72.980  51.967  1.00 25.81  ? 177 VAL   A C     1 
ATOM   1382  O  O     . VAL   A 1  177 ? 16.554  73.613  51.137  1.00 33.62  ? 177 VAL   A O     1 
ATOM   1383  C  CB    . VAL   A 1  177 ? 14.775  74.931  53.094  1.00 22.19  ? 177 VAL   A CB    1 
ATOM   1384  C  CG1   . VAL   A 1  177 ? 13.449  75.533  53.436  1.00 25.66  ? 177 VAL   A CG1   1 
ATOM   1385  C  CG2   . VAL   A 1  177 ? 15.621  74.838  54.337  1.00 28.49  ? 177 VAL   A CG2   1 
ATOM   1386  N  N     . SER   A 1  178 ? 16.290  71.798  52.437  1.00 31.79  ? 178 SER   A N     1 
ATOM   1387  C  CA    . SER   A 1  178 ? 17.555  71.202  52.014  1.00 35.21  ? 178 SER   A CA    1 
ATOM   1388  C  C     . SER   A 1  178 ? 17.423  70.632  50.607  1.00 33.15  ? 178 SER   A C     1 
ATOM   1389  O  O     . SER   A 1  178 ? 16.405  70.030  50.264  1.00 37.07  ? 178 SER   A O     1 
ATOM   1390  C  CB    . SER   A 1  178 ? 18.006  70.111  53.006  1.00 30.19  ? 178 SER   A CB    1 
ATOM   1391  O  OG    . SER   A 1  178 ? 17.343  68.873  52.796  1.00 38.41  ? 178 SER   A OG    1 
ATOM   1392  N  N     . THR   A 1  179 ? 18.456  70.829  49.785  1.00 35.15  ? 179 THR   A N     1 
ATOM   1393  C  CA    . THR   A 1  179 ? 18.461  70.325  48.413  1.00 36.33  ? 179 THR   A CA    1 
ATOM   1394  C  C     . THR   A 1  179 ? 19.398  69.133  48.216  1.00 36.12  ? 179 THR   A C     1 
ATOM   1395  O  O     . THR   A 1  179 ? 19.759  68.830  47.068  1.00 32.38  ? 179 THR   A O     1 
ATOM   1396  C  CB    . THR   A 1  179 ? 18.837  71.426  47.412  1.00 40.12  ? 179 THR   A CB    1 
ATOM   1397  O  OG1   . THR   A 1  179 ? 19.731  72.382  48.017  1.00 39.60  ? 179 THR   A OG1   1 
ATOM   1398  C  CG2   . THR   A 1  179 ? 17.584  72.115  46.841  1.00 43.89  ? 179 THR   A CG2   1 
ATOM   1399  N  N     . ALA   A 1  180 ? 19.800  68.451  49.299  1.00 28.87  ? 180 ALA   A N     1 
ATOM   1400  C  CA    . ALA   A 1  180 ? 20.678  67.287  49.181  1.00 28.02  ? 180 ALA   A CA    1 
ATOM   1401  C  C     . ALA   A 1  180 ? 20.398  66.316  50.310  1.00 23.43  ? 180 ALA   A C     1 
ATOM   1402  O  O     . ALA   A 1  180 ? 20.060  66.736  51.416  1.00 31.43  ? 180 ALA   A O     1 
ATOM   1403  C  CB    . ALA   A 1  180 ? 22.166  67.678  49.185  1.00 28.93  ? 180 ALA   A CB    1 
ATOM   1404  N  N     . VAL   A 1  181 ? 20.533  65.016  50.028  1.00 20.07  ? 181 VAL   A N     1 
ATOM   1405  C  CA    . VAL   A 1  181 ? 20.312  64.016  51.070  1.00 17.34  ? 181 VAL   A CA    1 
ATOM   1406  C  C     . VAL   A 1  181 ? 21.620  63.636  51.771  1.00 20.71  ? 181 VAL   A C     1 
ATOM   1407  O  O     . VAL   A 1  181 ? 21.591  63.091  52.886  1.00 17.82  ? 181 VAL   A O     1 
ATOM   1408  C  CB    . VAL   A 1  181 ? 19.526  62.818  50.478  1.00 14.95  ? 181 VAL   A CB    1 
ATOM   1409  C  CG1   . VAL   A 1  181 ? 19.150  63.084  49.048  1.00 25.99  ? 181 VAL   A CG1   1 
ATOM   1410  C  CG2   . VAL   A 1  181 ? 20.233  61.508  50.579  1.00 13.91  ? 181 VAL   A CG2   1 
ATOM   1411  N  N     . VAL   A 1  182 ? 22.769  63.966  51.189  1.00 22.73  ? 182 VAL   A N     1 
ATOM   1412  C  CA    . VAL   A 1  182 ? 24.048  63.715  51.849  1.00 21.93  ? 182 VAL   A CA    1 
ATOM   1413  C  C     . VAL   A 1  182 ? 24.391  64.800  52.868  1.00 28.07  ? 182 VAL   A C     1 
ATOM   1414  O  O     . VAL   A 1  182 ? 25.507  64.828  53.391  1.00 25.89  ? 182 VAL   A O     1 
ATOM   1415  C  CB    . VAL   A 1  182 ? 25.194  63.603  50.830  1.00 15.30  ? 182 VAL   A CB    1 
ATOM   1416  C  CG1   . VAL   A 1  182 ? 25.007  62.397  49.983  1.00 21.95  ? 182 VAL   A CG1   1 
ATOM   1417  C  CG2   . VAL   A 1  182 ? 25.269  64.856  49.975  1.00 15.82  ? 182 VAL   A CG2   1 
ATOM   1418  N  N     . GLU   A 1  183 ? 23.461  65.704  53.165  1.00 27.76  ? 183 GLU   A N     1 
ATOM   1419  C  CA    . GLU   A 1  183 ? 23.817  66.835  54.023  1.00 24.39  ? 183 GLU   A CA    1 
ATOM   1420  C  C     . GLU   A 1  183 ? 24.397  66.410  55.365  1.00 27.64  ? 183 GLU   A C     1 
ATOM   1421  O  O     . GLU   A 1  183 ? 25.399  67.009  55.789  1.00 31.07  ? 183 GLU   A O     1 
ATOM   1422  C  CB    . GLU   A 1  183 ? 22.600  67.739  54.226  1.00 22.78  ? 183 GLU   A CB    1 
ATOM   1423  C  CG    . GLU   A 1  183 ? 21.937  68.143  52.934  1.00 24.94  ? 183 GLU   A CG    1 
ATOM   1424  C  CD    . GLU   A 1  183 ? 21.581  69.596  52.930  1.00 29.95  ? 183 GLU   A CD    1 
ATOM   1425  O  OE1   . GLU   A 1  183 ? 22.141  70.317  53.773  1.00 29.21  ? 183 GLU   A OE1   1 
ATOM   1426  O  OE2   . GLU   A 1  183 ? 20.744  70.023  52.108  1.00 37.19  ? 183 GLU   A OE2   1 
ATOM   1427  N  N     . PRO   A 1  184 ? 23.854  65.410  56.064  1.00 24.82  ? 184 PRO   A N     1 
ATOM   1428  C  CA    . PRO   A 1  184 ? 24.490  64.983  57.323  1.00 24.52  ? 184 PRO   A CA    1 
ATOM   1429  C  C     . PRO   A 1  184 ? 25.948  64.595  57.169  1.00 28.73  ? 184 PRO   A C     1 
ATOM   1430  O  O     . PRO   A 1  184 ? 26.763  64.909  58.041  1.00 34.95  ? 184 PRO   A O     1 
ATOM   1431  C  CB    . PRO   A 1  184 ? 23.623  63.796  57.754  1.00 22.24  ? 184 PRO   A CB    1 
ATOM   1432  C  CG    . PRO   A 1  184 ? 22.298  64.077  57.141  1.00 19.14  ? 184 PRO   A CG    1 
ATOM   1433  C  CD    . PRO   A 1  184 ? 22.561  64.747  55.842  1.00 17.17  ? 184 PRO   A CD    1 
ATOM   1434  N  N     . TYR   A 1  185 ? 26.300  63.897  56.090  1.00 28.58  ? 185 TYR   A N     1 
ATOM   1435  C  CA    . TYR   A 1  185 ? 27.700  63.631  55.782  1.00 23.13  ? 185 TYR   A CA    1 
ATOM   1436  C  C     . TYR   A 1  185 ? 28.530  64.906  55.820  1.00 25.71  ? 185 TYR   A C     1 
ATOM   1437  O  O     . TYR   A 1  185 ? 29.516  65.007  56.549  1.00 32.52  ? 185 TYR   A O     1 
ATOM   1438  C  CB    . TYR   A 1  185 ? 27.792  62.996  54.402  1.00 27.73  ? 185 TYR   A CB    1 
ATOM   1439  C  CG    . TYR   A 1  185 ? 27.491  61.543  54.418  1.00 23.11  ? 185 TYR   A CG    1 
ATOM   1440  C  CD1   . TYR   A 1  185 ? 27.230  60.910  55.616  1.00 16.21  ? 185 TYR   A CD1   1 
ATOM   1441  C  CD2   . TYR   A 1  185 ? 27.496  60.796  53.239  1.00 17.88  ? 185 TYR   A CD2   1 
ATOM   1442  C  CE1   . TYR   A 1  185 ? 26.973  59.576  55.657  1.00 22.60  ? 185 TYR   A CE1   1 
ATOM   1443  C  CE2   . TYR   A 1  185 ? 27.238  59.442  53.265  1.00 15.64  ? 185 TYR   A CE2   1 
ATOM   1444  C  CZ    . TYR   A 1  185 ? 26.977  58.828  54.486  1.00 20.21  ? 185 TYR   A CZ    1 
ATOM   1445  O  OH    . TYR   A 1  185 ? 26.696  57.473  54.574  1.00 18.59  ? 185 TYR   A OH    1 
ATOM   1446  N  N     . ASN   A 1  186 ? 28.139  65.891  55.019  1.00 25.78  ? 186 ASN   A N     1 
ATOM   1447  C  CA    . ASN   A 1  186 ? 28.894  67.131  54.923  1.00 24.59  ? 186 ASN   A CA    1 
ATOM   1448  C  C     . ASN   A 1  186 ? 28.923  67.887  56.242  1.00 27.87  ? 186 ASN   A C     1 
ATOM   1449  O  O     . ASN   A 1  186 ? 29.897  68.588  56.534  1.00 32.56  ? 186 ASN   A O     1 
ATOM   1450  C  CB    . ASN   A 1  186 ? 28.295  68.027  53.842  1.00 27.03  ? 186 ASN   A CB    1 
ATOM   1451  C  CG    . ASN   A 1  186 ? 28.333  67.409  52.440  1.00 27.52  ? 186 ASN   A CG    1 
ATOM   1452  O  OD1   . ASN   A 1  186 ? 28.985  66.389  52.178  1.00 22.14  ? 186 ASN   A OD1   1 
ATOM   1453  N  ND2   . ASN   A 1  186 ? 27.648  68.069  51.518  1.00 28.23  ? 186 ASN   A ND2   1 
ATOM   1454  N  N     . SER   A 1  187 ? 27.862  67.788  57.038  1.00 33.33  ? 187 SER   A N     1 
ATOM   1455  C  CA    . SER   A 1  187 ? 27.799  68.545  58.287  1.00 29.83  ? 187 SER   A CA    1 
ATOM   1456  C  C     . SER   A 1  187 ? 28.777  68.004  59.314  1.00 26.24  ? 187 SER   A C     1 
ATOM   1457  O  O     . SER   A 1  187 ? 29.516  68.774  59.928  1.00 32.12  ? 187 SER   A O     1 
ATOM   1458  C  CB    . SER   A 1  187 ? 26.380  68.529  58.855  1.00 28.71  ? 187 SER   A CB    1 
ATOM   1459  O  OG    . SER   A 1  187 ? 25.543  69.343  58.061  1.00 31.44  ? 187 SER   A OG    1 
ATOM   1460  N  N     . ILE   A 1  188 ? 28.777  66.683  59.533  1.00 30.62  ? 188 ILE   A N     1 
ATOM   1461  C  CA    . ILE   A 1  188 ? 29.707  66.063  60.483  1.00 32.10  ? 188 ILE   A CA    1 
ATOM   1462  C  C     . ILE   A 1  188 ? 31.150  66.272  60.037  1.00 33.28  ? 188 ILE   A C     1 
ATOM   1463  O  O     . ILE   A 1  188 ? 32.008  66.698  60.821  1.00 34.26  ? 188 ILE   A O     1 
ATOM   1464  C  CB    . ILE   A 1  188 ? 29.408  64.562  60.636  1.00 29.39  ? 188 ILE   A CB    1 
ATOM   1465  C  CG1   . ILE   A 1  188 ? 28.437  64.288  61.787  1.00 25.76  ? 188 ILE   A CG1   1 
ATOM   1466  C  CG2   . ILE   A 1  188 ? 30.711  63.838  60.858  1.00 26.96  ? 188 ILE   A CG2   1 
ATOM   1467  C  CD1   . ILE   A 1  188 ? 27.136  64.995  61.673  1.00 26.22  ? 188 ILE   A CD1   1 
ATOM   1468  N  N     . LEU   A 1  189 ? 31.444  65.940  58.774  1.00 29.29  ? 189 LEU   A N     1 
ATOM   1469  C  CA    . LEU   A 1  189 ? 32.766  66.186  58.202  1.00 27.83  ? 189 LEU   A CA    1 
ATOM   1470  C  C     . LEU   A 1  189 ? 33.258  67.606  58.480  1.00 31.13  ? 189 LEU   A C     1 
ATOM   1471  O  O     . LEU   A 1  189 ? 34.366  67.797  58.994  1.00 31.91  ? 189 LEU   A O     1 
ATOM   1472  C  CB    . LEU   A 1  189 ? 32.744  65.925  56.693  1.00 32.07  ? 189 LEU   A CB    1 
ATOM   1473  C  CG    . LEU   A 1  189 ? 32.612  64.494  56.154  1.00 29.36  ? 189 LEU   A CG    1 
ATOM   1474  C  CD1   . LEU   A 1  189 ? 32.287  64.574  54.704  1.00 27.88  ? 189 LEU   A CD1   1 
ATOM   1475  C  CD2   . LEU   A 1  189 ? 33.877  63.655  56.376  1.00 28.56  ? 189 LEU   A CD2   1 
ATOM   1476  N  N     . THR   A 1  190 ? 32.461  68.624  58.137  1.00 28.55  ? 190 THR   A N     1 
ATOM   1477  C  CA    . THR   A 1  190 ? 32.994  69.982  58.262  1.00 33.22  ? 190 THR   A CA    1 
ATOM   1478  C  C     . THR   A 1  190 ? 33.066  70.462  59.696  1.00 29.87  ? 190 THR   A C     1 
ATOM   1479  O  O     . THR   A 1  190 ? 33.909  71.314  60.003  1.00 24.81  ? 190 THR   A O     1 
ATOM   1480  C  CB    . THR   A 1  190 ? 32.169  70.995  57.502  1.00 29.07  ? 190 THR   A CB    1 
ATOM   1481  O  OG1   . THR   A 1  190 ? 32.956  72.186  57.355  1.00 19.73  ? 190 THR   A OG1   1 
ATOM   1482  C  CG2   . THR   A 1  190 ? 30.940  71.302  58.313  1.00 23.30  ? 190 THR   A CG2   1 
ATOM   1483  N  N     . THR   A 1  191 ? 32.164  69.971  60.557  1.00 33.69  ? 191 THR   A N     1 
ATOM   1484  C  CA    . THR   A 1  191 ? 32.223  70.276  61.988  1.00 32.04  ? 191 THR   A CA    1 
ATOM   1485  C  C     . THR   A 1  191 ? 33.504  69.728  62.589  1.00 27.45  ? 191 THR   A C     1 
ATOM   1486  O  O     . THR   A 1  191 ? 34.215  70.427  63.314  1.00 31.92  ? 191 THR   A O     1 
ATOM   1487  C  CB    . THR   A 1  191 ? 31.000  69.695  62.729  1.00 33.15  ? 191 THR   A CB    1 
ATOM   1488  O  OG1   . THR   A 1  191 ? 29.775  70.148  62.130  1.00 27.74  ? 191 THR   A OG1   1 
ATOM   1489  C  CG2   . THR   A 1  191 ? 31.000  70.106  64.183  1.00 25.90  ? 191 THR   A CG2   1 
ATOM   1490  N  N     . HIS   A 1  192 ? 33.829  68.478  62.273  1.00 32.40  ? 192 HIS   A N     1 
ATOM   1491  C  CA    . HIS   A 1  192 ? 35.046  67.864  62.788  1.00 35.39  ? 192 HIS   A CA    1 
ATOM   1492  C  C     . HIS   A 1  192 ? 36.270  68.685  62.415  1.00 33.11  ? 192 HIS   A C     1 
ATOM   1493  O  O     . HIS   A 1  192 ? 36.944  69.269  63.266  1.00 41.84  ? 192 HIS   A O     1 
ATOM   1494  C  CB    . HIS   A 1  192 ? 35.157  66.443  62.240  1.00 34.86  ? 192 HIS   A CB    1 
ATOM   1495  C  CG    . HIS   A 1  192 ? 36.527  65.864  62.356  1.00 43.13  ? 192 HIS   A CG    1 
ATOM   1496  N  ND1   . HIS   A 1  192 ? 37.172  65.719  63.567  1.00 31.99  ? 192 HIS   A ND1   1 
ATOM   1497  C  CD2   . HIS   A 1  192 ? 37.381  65.401  61.411  1.00 40.63  ? 192 HIS   A CD2   1 
ATOM   1498  C  CE1   . HIS   A 1  192 ? 38.360  65.178  63.364  1.00 38.22  ? 192 HIS   A CE1   1 
ATOM   1499  N  NE2   . HIS   A 1  192 ? 38.512  64.975  62.065  1.00 46.15  ? 192 HIS   A NE2   1 
ATOM   1500  N  N     . THR   A 1  193 ? 36.560  68.743  61.128  1.00 36.12  ? 193 THR   A N     1 
ATOM   1501  C  CA    . THR   A 1  193 ? 37.715  69.484  60.663  1.00 36.91  ? 193 THR   A CA    1 
ATOM   1502  C  C     . THR   A 1  193 ? 37.714  70.923  61.166  1.00 30.64  ? 193 THR   A C     1 
ATOM   1503  O  O     . THR   A 1  193 ? 38.783  71.486  61.406  1.00 34.99  ? 193 THR   A O     1 
ATOM   1504  C  CB    . THR   A 1  193 ? 37.760  69.422  59.128  1.00 40.21  ? 193 THR   A CB    1 
ATOM   1505  O  OG1   . THR   A 1  193 ? 38.006  68.065  58.707  1.00 31.89  ? 193 THR   A OG1   1 
ATOM   1506  C  CG2   . THR   A 1  193 ? 38.840  70.364  58.541  1.00 38.22  ? 193 THR   A CG2   1 
ATOM   1507  N  N     . THR   A 1  194 ? 36.552  71.548  61.330  1.00 33.75  ? 194 THR   A N     1 
ATOM   1508  C  CA    . THR   A 1  194 ? 36.582  72.963  61.708  1.00 36.81  ? 194 THR   A CA    1 
ATOM   1509  C  C     . THR   A 1  194 ? 36.622  73.193  63.218  1.00 32.80  ? 194 THR   A C     1 
ATOM   1510  O  O     . THR   A 1  194 ? 37.010  74.286  63.647  1.00 28.42  ? 194 THR   A O     1 
ATOM   1511  C  CB    . THR   A 1  194 ? 35.391  73.727  61.108  1.00 29.09  ? 194 THR   A CB    1 
ATOM   1512  O  OG1   . THR   A 1  194 ? 35.393  73.566  59.684  1.00 33.81  ? 194 THR   A OG1   1 
ATOM   1513  C  CG2   . THR   A 1  194 ? 35.482  75.224  61.440  1.00 20.31  ? 194 THR   A CG2   1 
ATOM   1514  N  N     . LEU   A 1  195 ? 36.318  72.168  64.024  1.00 32.89  ? 195 LEU   A N     1 
ATOM   1515  C  CA    . LEU   A 1  195 ? 36.015  72.375  65.439  1.00 31.55  ? 195 LEU   A CA    1 
ATOM   1516  C  C     . LEU   A 1  195 ? 37.129  73.109  66.177  1.00 37.41  ? 195 LEU   A C     1 
ATOM   1517  O  O     . LEU   A 1  195 ? 36.852  73.962  67.028  1.00 40.07  ? 195 LEU   A O     1 
ATOM   1518  C  CB    . LEU   A 1  195 ? 35.713  71.037  66.109  1.00 23.71  ? 195 LEU   A CB    1 
ATOM   1519  C  CG    . LEU   A 1  195 ? 34.871  71.108  67.383  1.00 28.01  ? 195 LEU   A CG    1 
ATOM   1520  C  CD1   . LEU   A 1  195 ? 33.637  71.950  67.183  1.00 32.93  ? 195 LEU   A CD1   1 
ATOM   1521  C  CD2   . LEU   A 1  195 ? 34.455  69.722  67.858  1.00 29.47  ? 195 LEU   A CD2   1 
ATOM   1522  N  N     . GLU   A 1  196 ? 38.394  72.805  65.862  1.00 42.53  ? 196 GLU   A N     1 
ATOM   1523  C  CA    . GLU   A 1  196 ? 39.533  73.406  66.559  1.00 33.24  ? 196 GLU   A CA    1 
ATOM   1524  C  C     . GLU   A 1  196 ? 39.964  74.742  65.983  1.00 28.39  ? 196 GLU   A C     1 
ATOM   1525  O  O     . GLU   A 1  196 ? 40.853  75.379  66.546  1.00 41.81  ? 196 GLU   A O     1 
ATOM   1526  C  CB    . GLU   A 1  196 ? 40.741  72.467  66.553  1.00 34.75  ? 196 GLU   A CB    1 
ATOM   1527  C  CG    . GLU   A 1  196 ? 40.627  71.299  67.522  1.00 44.83  ? 196 GLU   A CG    1 
ATOM   1528  C  CD    . GLU   A 1  196 ? 41.256  71.572  68.881  1.00 72.44  ? 196 GLU   A CD    1 
ATOM   1529  O  OE1   . GLU   A 1  196 ? 41.569  72.750  69.188  1.00 71.10  ? 196 GLU   A OE1   1 
ATOM   1530  O  OE2   . GLU   A 1  196 ? 41.444  70.597  69.648  1.00 86.21  ? 196 GLU   A OE2   1 
ATOM   1531  N  N     . HIS   A 1  197 ? 39.359  75.198  64.901  1.00 35.96  ? 197 HIS   A N     1 
ATOM   1532  C  CA    . HIS   A 1  197 ? 39.740  76.470  64.314  1.00 31.95  ? 197 HIS   A CA    1 
ATOM   1533  C  C     . HIS   A 1  197 ? 38.678  77.546  64.503  1.00 34.01  ? 197 HIS   A C     1 
ATOM   1534  O  O     . HIS   A 1  197 ? 38.859  78.666  64.018  1.00 39.80  ? 197 HIS   A O     1 
ATOM   1535  C  CB    . HIS   A 1  197 ? 40.055  76.296  62.818  1.00 39.82  ? 197 HIS   A CB    1 
ATOM   1536  C  CG    . HIS   A 1  197 ? 41.049  75.212  62.521  1.00 34.86  ? 197 HIS   A CG    1 
ATOM   1537  N  ND1   . HIS   A 1  197 ? 40.830  73.889  62.841  1.00 38.72  ? 197 HIS   A ND1   1 
ATOM   1538  C  CD2   . HIS   A 1  197 ? 42.250  75.249  61.903  1.00 37.32  ? 197 HIS   A CD2   1 
ATOM   1539  C  CE1   . HIS   A 1  197 ? 41.860  73.159  62.452  1.00 37.25  ? 197 HIS   A CE1   1 
ATOM   1540  N  NE2   . HIS   A 1  197 ? 42.735  73.961  61.877  1.00 48.42  ? 197 HIS   A NE2   1 
ATOM   1541  N  N     . SER   A 1  198 ? 37.580  77.245  65.193  1.00 37.36  ? 198 SER   A N     1 
ATOM   1542  C  CA    . SER   A 1  198 ? 36.503  78.200  65.425  1.00 35.93  ? 198 SER   A CA    1 
ATOM   1543  C  C     . SER   A 1  198 ? 36.360  78.479  66.923  1.00 41.24  ? 198 SER   A C     1 
ATOM   1544  O  O     . SER   A 1  198 ? 36.211  77.550  67.735  1.00 31.11  ? 198 SER   A O     1 
ATOM   1545  C  CB    . SER   A 1  198 ? 35.181  77.686  64.830  1.00 33.77  ? 198 SER   A CB    1 
ATOM   1546  O  OG    . SER   A 1  198 ? 34.080  78.537  65.129  1.00 31.09  ? 198 SER   A OG    1 
ATOM   1547  N  N     . ASP   A 1  199 ? 36.396  79.766  67.275  1.00 33.14  ? 199 ASP   A N     1 
ATOM   1548  C  CA    . ASP   A 1  199 ? 36.331  80.206  68.659  1.00 31.18  ? 199 ASP   A CA    1 
ATOM   1549  C  C     . ASP   A 1  199 ? 34.905  80.274  69.201  1.00 32.49  ? 199 ASP   A C     1 
ATOM   1550  O  O     . ASP   A 1  199 ? 34.716  80.387  70.420  1.00 32.25  ? 199 ASP   A O     1 
ATOM   1551  C  CB    . ASP   A 1  199 ? 37.000  81.575  68.765  1.00 36.40  ? 199 ASP   A CB    1 
ATOM   1552  C  CG    . ASP   A 1  199 ? 38.463  81.529  68.414  1.00 32.26  ? 199 ASP   A CG    1 
ATOM   1553  O  OD1   . ASP   A 1  199 ? 39.172  80.782  69.121  1.00 24.37  ? 199 ASP   A OD1   1 
ATOM   1554  O  OD2   . ASP   A 1  199 ? 38.885  82.209  67.441  1.00 27.44  ? 199 ASP   A OD2   1 
ATOM   1555  N  N     . CYS   A 1  200 ? 33.898  80.214  68.338  1.00 32.03  ? 200 CYS   A N     1 
ATOM   1556  C  CA    . CYS   A 1  200 ? 32.532  80.437  68.776  1.00 30.90  ? 200 CYS   A CA    1 
ATOM   1557  C  C     . CYS   A 1  200 ? 31.616  80.257  67.581  1.00 29.61  ? 200 CYS   A C     1 
ATOM   1558  O  O     . CYS   A 1  200 ? 31.771  80.951  66.569  1.00 33.59  ? 200 CYS   A O     1 
ATOM   1559  C  CB    . CYS   A 1  200 ? 32.389  81.840  69.363  1.00 28.68  ? 200 CYS   A CB    1 
ATOM   1560  S  SG    . CYS   A 1  200 ? 30.838  82.149  70.178  1.00 24.28  ? 200 CYS   A SG    1 
ATOM   1561  N  N     . ALA   A 1  201 ? 30.659  79.346  67.674  1.00 22.50  ? 201 ALA   A N     1 
ATOM   1562  C  CA    . ALA   A 1  201 ? 29.789  79.046  66.553  1.00 21.12  ? 201 ALA   A CA    1 
ATOM   1563  C  C     . ALA   A 1  201 ? 28.353  79.379  66.912  1.00 24.20  ? 201 ALA   A C     1 
ATOM   1564  O  O     . ALA   A 1  201 ? 27.853  78.925  67.947  1.00 24.61  ? 201 ALA   A O     1 
ATOM   1565  C  CB    . ALA   A 1  201 ? 29.915  77.574  66.180  1.00 28.98  ? 201 ALA   A CB    1 
ATOM   1566  N  N     . PHE   A 1  202 ? 27.682  80.144  66.051  1.00 21.76  ? 202 PHE   A N     1 
ATOM   1567  C  CA    . PHE   A 1  202 ? 26.237  80.351  66.177  1.00 26.62  ? 202 PHE   A CA    1 
ATOM   1568  C  C     . PHE   A 1  202 ? 25.523  79.525  65.111  1.00 25.36  ? 202 PHE   A C     1 
ATOM   1569  O  O     . PHE   A 1  202 ? 25.509  79.895  63.935  1.00 23.87  ? 202 PHE   A O     1 
ATOM   1570  C  CB    . PHE   A 1  202 ? 25.876  81.827  66.071  1.00 25.23  ? 202 PHE   A CB    1 
ATOM   1571  C  CG    . PHE   A 1  202 ? 26.522  82.678  67.121  1.00 23.80  ? 202 PHE   A CG    1 
ATOM   1572  C  CD1   . PHE   A 1  202 ? 26.026  82.697  68.409  1.00 21.56  ? 202 PHE   A CD1   1 
ATOM   1573  C  CD2   . PHE   A 1  202 ? 27.640  83.434  66.823  1.00 18.98  ? 202 PHE   A CD2   1 
ATOM   1574  C  CE1   . PHE   A 1  202 ? 26.626  83.461  69.367  1.00 25.08  ? 202 PHE   A CE1   1 
ATOM   1575  C  CE2   . PHE   A 1  202 ? 28.238  84.194  67.778  1.00 19.12  ? 202 PHE   A CE2   1 
ATOM   1576  C  CZ    . PHE   A 1  202 ? 27.733  84.217  69.050  1.00 20.98  ? 202 PHE   A CZ    1 
ATOM   1577  N  N     . MET   A 1  203 ? 24.930  78.409  65.527  1.00 24.36  ? 203 MET   A N     1 
ATOM   1578  C  CA    . MET   A 1  203 ? 24.202  77.515  64.625  1.00 20.86  ? 203 MET   A CA    1 
ATOM   1579  C  C     . MET   A 1  203 ? 22.743  77.937  64.531  1.00 21.20  ? 203 MET   A C     1 
ATOM   1580  O  O     . MET   A 1  203 ? 21.959  77.730  65.460  1.00 22.72  ? 203 MET   A O     1 
ATOM   1581  C  CB    . MET   A 1  203 ? 24.256  76.071  65.108  1.00 21.60  ? 203 MET   A CB    1 
ATOM   1582  C  CG    . MET   A 1  203 ? 25.496  75.303  64.790  1.00 20.70  ? 203 MET   A CG    1 
ATOM   1583  S  SD    . MET   A 1  203 ? 25.015  73.597  65.048  1.00 42.13  ? 203 MET   A SD    1 
ATOM   1584  C  CE    . MET   A 1  203 ? 24.516  73.630  66.741  1.00 20.91  ? 203 MET   A CE    1 
ATOM   1585  N  N     . VAL   A 1  204 ? 22.355  78.451  63.389  1.00 27.28  ? 204 VAL   A N     1 
ATOM   1586  C  CA    . VAL   A 1  204 ? 20.956  78.679  63.087  1.00 22.12  ? 204 VAL   A CA    1 
ATOM   1587  C  C     . VAL   A 1  204 ? 20.444  77.453  62.328  1.00 25.07  ? 204 VAL   A C     1 
ATOM   1588  O  O     . VAL   A 1  204 ? 20.932  77.128  61.233  1.00 24.52  ? 204 VAL   A O     1 
ATOM   1589  C  CB    . VAL   A 1  204 ? 20.785  79.983  62.295  1.00 25.20  ? 204 VAL   A CB    1 
ATOM   1590  C  CG1   . VAL   A 1  204 ? 19.330  80.283  62.004  1.00 26.90  ? 204 VAL   A CG1   1 
ATOM   1591  C  CG2   . VAL   A 1  204 ? 21.439  81.118  63.078  1.00 18.90  ? 204 VAL   A CG2   1 
ATOM   1592  N  N     . ASP   A 1  205 ? 19.497  76.743  62.944  1.00 25.62  ? 205 ASP   A N     1 
ATOM   1593  C  CA    . ASP   A 1  205 ? 18.830  75.598  62.336  1.00 19.33  ? 205 ASP   A CA    1 
ATOM   1594  C  C     . ASP   A 1  205 ? 17.716  76.091  61.422  1.00 19.64  ? 205 ASP   A C     1 
ATOM   1595  O  O     . ASP   A 1  205 ? 16.771  76.729  61.890  1.00 21.21  ? 205 ASP   A O     1 
ATOM   1596  C  CB    . ASP   A 1  205 ? 18.265  74.698  63.429  1.00 18.63  ? 205 ASP   A CB    1 
ATOM   1597  C  CG    . ASP   A 1  205 ? 17.676  73.429  62.884  1.00 25.77  ? 205 ASP   A CG    1 
ATOM   1598  O  OD1   . ASP   A 1  205 ? 17.423  73.401  61.664  1.00 25.46  ? 205 ASP   A OD1   1 
ATOM   1599  O  OD2   . ASP   A 1  205 ? 17.460  72.464  63.668  1.00 23.44  ? 205 ASP   A OD2   1 
ATOM   1600  N  N     . ASN   A 1  206 ? 17.831  75.804  60.121  1.00 24.18  ? 206 ASN   A N     1 
ATOM   1601  C  CA    . ASN   A 1  206 ? 16.820  76.233  59.153  1.00 22.37  ? 206 ASN   A CA    1 
ATOM   1602  C  C     . ASN   A 1  206 ? 15.421  75.835  59.598  1.00 23.50  ? 206 ASN   A C     1 
ATOM   1603  O  O     . ASN   A 1  206 ? 14.472  76.612  59.434  1.00 24.26  ? 206 ASN   A O     1 
ATOM   1604  C  CB    . ASN   A 1  206 ? 17.105  75.634  57.774  1.00 17.35  ? 206 ASN   A CB    1 
ATOM   1605  C  CG    . ASN   A 1  206 ? 17.928  76.550  56.883  1.00 18.76  ? 206 ASN   A CG    1 
ATOM   1606  O  OD1   . ASN   A 1  206 ? 17.959  77.762  57.057  1.00 18.92  ? 206 ASN   A OD1   1 
ATOM   1607  N  ND2   . ASN   A 1  206 ? 18.588  75.960  55.898  1.00 26.11  ? 206 ASN   A ND2   1 
ATOM   1608  N  N     . GLU   A 1  207 ? 15.271  74.618  60.142  1.00 18.77  ? 207 GLU   A N     1 
ATOM   1609  C  CA    . GLU   A 1  207 ? 13.980  74.180  60.676  1.00 20.40  ? 207 GLU   A CA    1 
ATOM   1610  C  C     . GLU   A 1  207 ? 13.409  75.183  61.680  1.00 28.09  ? 207 GLU   A C     1 
ATOM   1611  O  O     . GLU   A 1  207 ? 12.216  75.500  61.646  1.00 29.95  ? 207 GLU   A O     1 
ATOM   1612  C  CB    . GLU   A 1  207 ? 14.114  72.801  61.328  1.00 18.39  ? 207 GLU   A CB    1 
ATOM   1613  C  CG    . GLU   A 1  207 ? 12.925  72.421  62.200  1.00 13.62  ? 207 GLU   A CG    1 
ATOM   1614  C  CD    . GLU   A 1  207 ? 13.267  71.393  63.290  1.00 24.08  ? 207 GLU   A CD    1 
ATOM   1615  O  OE1   . GLU   A 1  207 ? 14.068  71.713  64.221  1.00 28.88  ? 207 GLU   A OE1   1 
ATOM   1616  O  OE2   . GLU   A 1  207 ? 12.735  70.259  63.212  1.00 22.66  ? 207 GLU   A OE2   1 
ATOM   1617  N  N     . ALA   A 1  208 ? 14.240  75.696  62.585  1.00 22.41  ? 208 ALA   A N     1 
ATOM   1618  C  CA    . ALA   A 1  208 ? 13.721  76.651  63.549  1.00 18.91  ? 208 ALA   A CA    1 
ATOM   1619  C  C     . ALA   A 1  208 ? 13.304  77.954  62.866  1.00 21.15  ? 208 ALA   A C     1 
ATOM   1620  O  O     . ALA   A 1  208 ? 12.168  78.405  63.018  1.00 26.26  ? 208 ALA   A O     1 
ATOM   1621  C  CB    . ALA   A 1  208 ? 14.745  76.888  64.657  1.00 19.58  ? 208 ALA   A CB    1 
ATOM   1622  N  N     . ILE   A 1  209 ? 14.187  78.568  62.089  1.00 20.33  ? 209 ILE   A N     1 
ATOM   1623  C  CA    . ILE   A 1  209 ? 13.793  79.807  61.428  1.00 21.34  ? 209 ILE   A CA    1 
ATOM   1624  C  C     . ILE   A 1  209 ? 12.487  79.613  60.673  1.00 26.58  ? 209 ILE   A C     1 
ATOM   1625  O  O     . ILE   A 1  209 ? 11.626  80.503  60.653  1.00 26.77  ? 209 ILE   A O     1 
ATOM   1626  C  CB    . ILE   A 1  209 ? 14.914  80.303  60.498  1.00 22.63  ? 209 ILE   A CB    1 
ATOM   1627  C  CG1   . ILE   A 1  209 ? 16.145  80.576  61.319  1.00 24.66  ? 209 ILE   A CG1   1 
ATOM   1628  C  CG2   . ILE   A 1  209 ? 14.523  81.606  59.879  1.00 32.56  ? 209 ILE   A CG2   1 
ATOM   1629  C  CD1   . ILE   A 1  209 ? 15.775  81.076  62.702  1.00 25.09  ? 209 ILE   A CD1   1 
ATOM   1630  N  N     . TYR   A 1  210 ? 12.304  78.421  60.080  1.00 30.56  ? 210 TYR   A N     1 
ATOM   1631  C  CA    . TYR   A 1  210 ? 11.209  78.167  59.145  1.00 24.12  ? 210 TYR   A CA    1 
ATOM   1632  C  C     . TYR   A 1  210 ? 9.857   78.164  59.842  1.00 24.86  ? 210 TYR   A C     1 
ATOM   1633  O  O     . TYR   A 1  210 ? 8.889   78.732  59.327  1.00 28.69  ? 210 TYR   A O     1 
ATOM   1634  C  CB    . TYR   A 1  210 ? 11.449  76.835  58.451  1.00 19.85  ? 210 TYR   A CB    1 
ATOM   1635  C  CG    . TYR   A 1  210 ? 10.541  76.523  57.285  1.00 21.51  ? 210 TYR   A CG    1 
ATOM   1636  C  CD1   . TYR   A 1  210 ? 10.842  76.975  56.005  1.00 22.57  ? 210 TYR   A CD1   1 
ATOM   1637  C  CD2   . TYR   A 1  210 ? 9.401   75.735  57.458  1.00 27.00  ? 210 TYR   A CD2   1 
ATOM   1638  C  CE1   . TYR   A 1  210 ? 10.016  76.683  54.928  1.00 26.77  ? 210 TYR   A CE1   1 
ATOM   1639  C  CE2   . TYR   A 1  210 ? 8.574   75.425  56.398  1.00 22.27  ? 210 TYR   A CE2   1 
ATOM   1640  C  CZ    . TYR   A 1  210 ? 8.880   75.904  55.136  1.00 29.89  ? 210 TYR   A CZ    1 
ATOM   1641  O  OH    . TYR   A 1  210 ? 8.050   75.602  54.079  1.00 34.69  ? 210 TYR   A OH    1 
ATOM   1642  N  N     . ASP   A 1  211 ? 9.765   77.520  61.004  1.00 27.99  ? 211 ASP   A N     1 
ATOM   1643  C  CA    . ASP   A 1  211 ? 8.528   77.573  61.789  1.00 35.35  ? 211 ASP   A CA    1 
ATOM   1644  C  C     . ASP   A 1  211 ? 8.283   78.955  62.375  1.00 28.12  ? 211 ASP   A C     1 
ATOM   1645  O  O     . ASP   A 1  211 ? 7.132   79.385  62.491  1.00 28.96  ? 211 ASP   A O     1 
ATOM   1646  C  CB    . ASP   A 1  211 ? 8.558   76.555  62.925  1.00 41.73  ? 211 ASP   A CB    1 
ATOM   1647  C  CG    . ASP   A 1  211 ? 7.806   75.309  62.592  1.00 52.40  ? 211 ASP   A CG    1 
ATOM   1648  O  OD1   . ASP   A 1  211 ? 7.830   74.923  61.394  1.00 55.09  ? 211 ASP   A OD1   1 
ATOM   1649  O  OD2   . ASP   A 1  211 ? 7.163   74.755  63.515  1.00 64.03  ? 211 ASP   A OD2   1 
ATOM   1650  N  N     . ILE   A 1  212 ? 9.339   79.641  62.808  1.00 26.66  ? 212 ILE   A N     1 
ATOM   1651  C  CA    . ILE   A 1  212 ? 9.181   81.012  63.272  1.00 22.31  ? 212 ILE   A CA    1 
ATOM   1652  C  C     . ILE   A 1  212 ? 8.536   81.865  62.191  1.00 34.22  ? 212 ILE   A C     1 
ATOM   1653  O  O     . ILE   A 1  212 ? 7.680   82.715  62.475  1.00 37.46  ? 212 ILE   A O     1 
ATOM   1654  C  CB    . ILE   A 1  212 ? 10.535  81.589  63.696  1.00 18.53  ? 212 ILE   A CB    1 
ATOM   1655  C  CG1   . ILE   A 1  212 ? 10.940  81.028  65.050  1.00 17.79  ? 212 ILE   A CG1   1 
ATOM   1656  C  CG2   . ILE   A 1  212 ? 10.459  83.094  63.723  1.00 21.32  ? 212 ILE   A CG2   1 
ATOM   1657  C  CD1   . ILE   A 1  212 ? 12.420  81.156  65.299  1.00 17.26  ? 212 ILE   A CD1   1 
ATOM   1658  N  N     . CYS   A 1  213 ? 8.939   81.656  60.931  1.00 40.27  ? 213 CYS   A N     1 
ATOM   1659  C  CA    . CYS   A 1  213 ? 8.347   82.388  59.815  1.00 28.95  ? 213 CYS   A CA    1 
ATOM   1660  C  C     . CYS   A 1  213 ? 6.922   81.949  59.555  1.00 28.53  ? 213 CYS   A C     1 
ATOM   1661  O  O     . CYS   A 1  213 ? 6.081   82.761  59.159  1.00 32.77  ? 213 CYS   A O     1 
ATOM   1662  C  CB    . CYS   A 1  213 ? 9.174   82.176  58.564  1.00 21.34  ? 213 CYS   A CB    1 
ATOM   1663  S  SG    . CYS   A 1  213 ? 10.666  83.086  58.588  1.00 32.66  ? 213 CYS   A SG    1 
ATOM   1664  N  N     . ARG   A 1  214 ? 6.645   80.657  59.729  1.00 31.19  ? 214 ARG   A N     1 
ATOM   1665  C  CA    . ARG   A 1  214 ? 5.304   80.138  59.481  1.00 31.43  ? 214 ARG   A CA    1 
ATOM   1666  C  C     . ARG   A 1  214 ? 4.348   80.579  60.585  1.00 32.78  ? 214 ARG   A C     1 
ATOM   1667  O  O     . ARG   A 1  214 ? 3.350   81.258  60.321  1.00 33.66  ? 214 ARG   A O     1 
ATOM   1668  C  CB    . ARG   A 1  214 ? 5.352   78.612  59.363  1.00 31.47  ? 214 ARG   A CB    1 
ATOM   1669  C  CG    . ARG   A 1  214 ? 4.650   78.053  58.146  1.00 39.52  ? 214 ARG   A CG    1 
ATOM   1670  C  CD    . ARG   A 1  214 ? 5.497   77.014  57.450  1.00 40.73  ? 214 ARG   A CD    1 
ATOM   1671  N  NE    . ARG   A 1  214 ? 4.997   75.645  57.583  1.00 45.47  ? 214 ARG   A NE    1 
ATOM   1672  C  CZ    . ARG   A 1  214 ? 5.540   74.704  58.351  1.00 40.27  ? 214 ARG   A CZ    1 
ATOM   1673  N  NH1   . ARG   A 1  214 ? 6.557   74.966  59.161  1.00 42.59  ? 214 ARG   A NH1   1 
ATOM   1674  N  NH2   . ARG   A 1  214 ? 5.062   73.464  58.292  1.00 32.15  ? 214 ARG   A NH2   1 
ATOM   1675  N  N     . ARG   A 1  215 ? 4.676   80.255  61.842  1.00 33.16  ? 215 ARG   A N     1 
ATOM   1676  C  CA    . ARG   A 1  215 ? 3.781   80.565  62.955  1.00 33.53  ? 215 ARG   A CA    1 
ATOM   1677  C  C     . ARG   A 1  215 ? 3.670   82.071  63.178  1.00 36.21  ? 215 ARG   A C     1 
ATOM   1678  O  O     . ARG   A 1  215 ? 2.569   82.628  63.195  1.00 47.49  ? 215 ARG   A O     1 
ATOM   1679  C  CB    . ARG   A 1  215 ? 4.249   79.864  64.235  1.00 27.49  ? 215 ARG   A CB    1 
ATOM   1680  C  CG    . ARG   A 1  215 ? 4.308   78.316  64.167  1.00 33.89  ? 215 ARG   A CG    1 
ATOM   1681  C  CD    . ARG   A 1  215 ? 4.797   77.704  65.495  1.00 45.59  ? 215 ARG   A CD    1 
ATOM   1682  N  NE    . ARG   A 1  215 ? 5.658   78.637  66.225  1.00 38.15  ? 215 ARG   A NE    1 
ATOM   1683  C  CZ    . ARG   A 1  215 ? 6.973   78.517  66.379  1.00 35.60  ? 215 ARG   A CZ    1 
ATOM   1684  N  NH1   . ARG   A 1  215 ? 7.632   77.426  65.996  1.00 32.60  ? 215 ARG   A NH1   1 
ATOM   1685  N  NH2   . ARG   A 1  215 ? 7.650   79.521  66.925  1.00 40.73  ? 215 ARG   A NH2   1 
ATOM   1686  N  N     . ASN   A 1  216 ? 4.796   82.754  63.345  1.00 36.32  ? 216 ASN   A N     1 
ATOM   1687  C  CA    . ASN   A 1  216 ? 4.746   84.130  63.821  1.00 32.53  ? 216 ASN   A CA    1 
ATOM   1688  C  C     . ASN   A 1  216 ? 4.578   85.163  62.722  1.00 32.51  ? 216 ASN   A C     1 
ATOM   1689  O  O     . ASN   A 1  216 ? 4.187   86.291  63.017  1.00 35.41  ? 216 ASN   A O     1 
ATOM   1690  C  CB    . ASN   A 1  216 ? 6.005   84.461  64.615  1.00 29.32  ? 216 ASN   A CB    1 
ATOM   1691  C  CG    . ASN   A 1  216 ? 6.027   83.791  65.953  1.00 30.88  ? 216 ASN   A CG    1 
ATOM   1692  O  OD1   . ASN   A 1  216 ? 5.611   82.646  66.103  1.00 31.32  ? 216 ASN   A OD1   1 
ATOM   1693  N  ND2   . ASN   A 1  216 ? 6.493   84.516  66.951  1.00 43.24  ? 216 ASN   A ND2   1 
ATOM   1694  N  N     . LEU   A 1  217 ? 4.864   84.832  61.475  1.00 32.47  ? 217 LEU   A N     1 
ATOM   1695  C  CA    . LEU   A 1  217 ? 4.711   85.813  60.412  1.00 37.42  ? 217 LEU   A CA    1 
ATOM   1696  C  C     . LEU   A 1  217 ? 3.666   85.397  59.391  1.00 38.39  ? 217 LEU   A C     1 
ATOM   1697  O  O     . LEU   A 1  217 ? 3.586   86.007  58.324  1.00 36.00  ? 217 LEU   A O     1 
ATOM   1698  C  CB    . LEU   A 1  217 ? 6.048   86.074  59.718  1.00 37.59  ? 217 LEU   A CB    1 
ATOM   1699  C  CG    . LEU   A 1  217 ? 7.124   86.601  60.648  1.00 35.86  ? 217 LEU   A CG    1 
ATOM   1700  C  CD1   . LEU   A 1  217 ? 8.322   87.003  59.835  1.00 37.69  ? 217 LEU   A CD1   1 
ATOM   1701  C  CD2   . LEU   A 1  217 ? 6.557   87.770  61.374  1.00 36.16  ? 217 LEU   A CD2   1 
ATOM   1702  N  N     . ASP   A 1  218 ? 2.869   84.375  59.687  1.00 38.02  ? 218 ASP   A N     1 
ATOM   1703  C  CA    . ASP   A 1  218 ? 1.767   83.948  58.827  1.00 41.30  ? 218 ASP   A CA    1 
ATOM   1704  C  C     . ASP   A 1  218 ? 2.226   83.591  57.415  1.00 34.09  ? 218 ASP   A C     1 
ATOM   1705  O  O     . ASP   A 1  218 ? 1.399   83.471  56.508  1.00 44.57  ? 218 ASP   A O     1 
ATOM   1706  C  CB    . ASP   A 1  218 ? 0.666   85.014  58.756  1.00 37.55  ? 218 ASP   A CB    1 
ATOM   1707  C  CG    . ASP   A 1  218 ? 0.319   85.609  60.125  1.00 48.95  ? 218 ASP   A CG    1 
ATOM   1708  O  OD1   . ASP   A 1  218 ? 0.213   84.817  61.099  1.00 39.87  ? 218 ASP   A OD1   1 
ATOM   1709  O  OD2   . ASP   A 1  218 ? 0.151   86.869  60.214  1.00 40.43  ? 218 ASP   A OD2   1 
ATOM   1710  N  N     . ILE   A 1  219 ? 3.523   83.398  57.203  1.00 35.34  ? 219 ILE   A N     1 
ATOM   1711  C  CA    . ILE   A 1  219 ? 4.052   83.100  55.871  1.00 39.12  ? 219 ILE   A CA    1 
ATOM   1712  C  C     . ILE   A 1  219 ? 3.833   81.620  55.555  1.00 37.72  ? 219 ILE   A C     1 
ATOM   1713  O  O     . ILE   A 1  219 ? 4.397   80.743  56.215  1.00 35.81  ? 219 ILE   A O     1 
ATOM   1714  C  CB    . ILE   A 1  219 ? 5.540   83.473  55.789  1.00 36.56  ? 219 ILE   A CB    1 
ATOM   1715  C  CG1   . ILE   A 1  219 ? 5.711   84.999  55.753  1.00 32.97  ? 219 ILE   A CG1   1 
ATOM   1716  C  CG2   . ILE   A 1  219 ? 6.197   82.776  54.626  1.00 25.64  ? 219 ILE   A CG2   1 
ATOM   1717  C  CD1   . ILE   A 1  219 ? 7.018   85.491  56.340  1.00 27.44  ? 219 ILE   A CD1   1 
ATOM   1718  N  N     . GLU   A 1  220 ? 3.023   81.337  54.533  1.00 45.65  ? 220 GLU   A N     1 
ATOM   1719  C  CA    . GLU   A 1  220 ? 2.659   79.962  54.176  1.00 34.71  ? 220 GLU   A CA    1 
ATOM   1720  C  C     . GLU   A 1  220 ? 3.852   79.033  53.989  1.00 38.05  ? 220 GLU   A C     1 
ATOM   1721  O  O     . GLU   A 1  220 ? 4.010   78.067  54.743  1.00 44.24  ? 220 GLU   A O     1 
ATOM   1722  C  CB    . GLU   A 1  220 ? 1.824   79.953  52.894  1.00 39.28  ? 220 GLU   A CB    1 
ATOM   1723  C  CG    . GLU   A 1  220 ? 0.405   80.491  53.065  1.00 46.55  ? 220 GLU   A CG    1 
ATOM   1724  C  CD    . GLU   A 1  220 ? -0.650  79.468  52.706  1.00 58.71  ? 220 GLU   A CD    1 
ATOM   1725  O  OE1   . GLU   A 1  220 ? -0.748  79.166  51.497  1.00 59.68  ? 220 GLU   A OE1   1 
ATOM   1726  O  OE2   . GLU   A 1  220 ? -1.350  78.952  53.624  1.00 55.90  ? 220 GLU   A OE2   1 
ATOM   1727  N  N     . ARG   A 1  221 ? 4.680   79.291  52.974  1.00 31.38  ? 221 ARG   A N     1 
ATOM   1728  C  CA    . ARG   A 1  221 ? 5.798   78.417  52.625  1.00 24.65  ? 221 ARG   A CA    1 
ATOM   1729  C  C     . ARG   A 1  221 ? 7.029   79.310  52.545  1.00 27.74  ? 221 ARG   A C     1 
ATOM   1730  O  O     . ARG   A 1  221 ? 7.363   79.849  51.478  1.00 30.41  ? 221 ARG   A O     1 
ATOM   1731  C  CB    . ARG   A 1  221 ? 5.519   77.664  51.320  1.00 32.44  ? 221 ARG   A CB    1 
ATOM   1732  C  CG    . ARG   A 1  221 ? 6.365   76.394  51.043  1.00 32.09  ? 221 ARG   A CG    1 
ATOM   1733  C  CD    . ARG   A 1  221 ? 7.838   76.690  50.743  1.00 29.62  ? 221 ARG   A CD    1 
ATOM   1734  N  NE    . ARG   A 1  221 ? 8.541   75.551  50.157  1.00 34.93  ? 221 ARG   A NE    1 
ATOM   1735  C  CZ    . ARG   A 1  221 ? 9.853   75.343  50.230  1.00 43.38  ? 221 ARG   A CZ    1 
ATOM   1736  N  NH1   . ARG   A 1  221 ? 10.653  76.165  50.896  1.00 31.31  ? 221 ARG   A NH1   1 
ATOM   1737  N  NH2   . ARG   A 1  221 ? 10.376  74.277  49.628  1.00 51.87  ? 221 ARG   A NH2   1 
ATOM   1738  N  N     . PRO   A 1  222 ? 7.735   79.488  53.658  1.00 25.53  ? 222 PRO   A N     1 
ATOM   1739  C  CA    . PRO   A 1  222 ? 8.818   80.472  53.685  1.00 24.73  ? 222 PRO   A CA    1 
ATOM   1740  C  C     . PRO   A 1  222 ? 9.837   80.242  52.581  1.00 28.97  ? 222 PRO   A C     1 
ATOM   1741  O  O     . PRO   A 1  222 ? 10.248  79.109  52.303  1.00 21.47  ? 222 PRO   A O     1 
ATOM   1742  C  CB    . PRO   A 1  222 ? 9.437   80.273  55.074  1.00 24.67  ? 222 PRO   A CB    1 
ATOM   1743  C  CG    . PRO   A 1  222 ? 8.333   79.717  55.906  1.00 24.59  ? 222 PRO   A CG    1 
ATOM   1744  C  CD    . PRO   A 1  222 ? 7.539   78.848  54.971  1.00 30.77  ? 222 PRO   A CD    1 
ATOM   1745  N  N     . THR   A 1  223 ? 10.250  81.342  51.961  1.00 30.83  ? 223 THR   A N     1 
ATOM   1746  C  CA    . THR   A 1  223 ? 11.323  81.316  50.981  1.00 23.73  ? 223 THR   A CA    1 
ATOM   1747  C  C     . THR   A 1  223 ? 12.639  81.647  51.662  1.00 22.88  ? 223 THR   A C     1 
ATOM   1748  O  O     . THR   A 1  223 ? 12.679  82.037  52.829  1.00 33.06  ? 223 THR   A O     1 
ATOM   1749  C  CB    . THR   A 1  223 ? 11.039  82.301  49.847  1.00 26.52  ? 223 THR   A CB    1 
ATOM   1750  O  OG1   . THR   A 1  223 ? 11.419  83.632  50.235  1.00 25.72  ? 223 THR   A OG1   1 
ATOM   1751  C  CG2   . THR   A 1  223 ? 9.557   82.263  49.511  1.00 23.43  ? 223 THR   A CG2   1 
ATOM   1752  N  N     . TYR   A 1  224 ? 13.737  81.485  50.925  1.00 24.98  ? 224 TYR   A N     1 
ATOM   1753  C  CA    . TYR   A 1  224 ? 15.027  81.838  51.505  1.00 23.68  ? 224 TYR   A CA    1 
ATOM   1754  C  C     . TYR   A 1  224 ? 15.066  83.304  51.889  1.00 28.62  ? 224 TYR   A C     1 
ATOM   1755  O  O     . TYR   A 1  224 ? 15.767  83.674  52.833  1.00 36.00  ? 224 TYR   A O     1 
ATOM   1756  C  CB    . TYR   A 1  224 ? 16.172  81.540  50.546  1.00 25.07  ? 224 TYR   A CB    1 
ATOM   1757  C  CG    . TYR   A 1  224 ? 16.616  80.108  50.444  1.00 21.00  ? 224 TYR   A CG    1 
ATOM   1758  C  CD1   . TYR   A 1  224 ? 16.662  79.268  51.555  1.00 19.30  ? 224 TYR   A CD1   1 
ATOM   1759  C  CD2   . TYR   A 1  224 ? 17.029  79.608  49.227  1.00 24.27  ? 224 TYR   A CD2   1 
ATOM   1760  C  CE1   . TYR   A 1  224 ? 17.085  77.950  51.433  1.00 20.34  ? 224 TYR   A CE1   1 
ATOM   1761  C  CE2   . TYR   A 1  224 ? 17.462  78.308  49.094  1.00 23.79  ? 224 TYR   A CE2   1 
ATOM   1762  C  CZ    . TYR   A 1  224 ? 17.486  77.476  50.182  1.00 25.11  ? 224 TYR   A CZ    1 
ATOM   1763  O  OH    . TYR   A 1  224 ? 17.911  76.174  49.962  1.00 31.94  ? 224 TYR   A OH    1 
ATOM   1764  N  N     . THR   A 1  225 ? 14.320  84.157  51.185  1.00 27.43  ? 225 THR   A N     1 
ATOM   1765  C  CA    . THR   A 1  225 ? 14.313  85.570  51.555  1.00 36.54  ? 225 THR   A CA    1 
ATOM   1766  C  C     . THR   A 1  225 ? 13.824  85.765  52.987  1.00 35.32  ? 225 THR   A C     1 
ATOM   1767  O  O     . THR   A 1  225 ? 14.491  86.416  53.797  1.00 37.99  ? 225 THR   A O     1 
ATOM   1768  C  CB    . THR   A 1  225 ? 13.456  86.385  50.590  1.00 38.06  ? 225 THR   A CB    1 
ATOM   1769  O  OG1   . THR   A 1  225 ? 14.108  86.447  49.319  1.00 33.84  ? 225 THR   A OG1   1 
ATOM   1770  C  CG2   . THR   A 1  225 ? 13.271  87.810  51.149  1.00 38.35  ? 225 THR   A CG2   1 
ATOM   1771  N  N     . ASN   A 1  226 ? 12.643  85.231  53.312  1.00 30.58  ? 226 ASN   A N     1 
ATOM   1772  C  CA    . ASN   A 1  226 ? 12.146  85.330  54.677  1.00 28.23  ? 226 ASN   A CA    1 
ATOM   1773  C  C     . ASN   A 1  226 ? 13.184  84.810  55.653  1.00 35.52  ? 226 ASN   A C     1 
ATOM   1774  O  O     . ASN   A 1  226 ? 13.624  85.534  56.551  1.00 36.71  ? 226 ASN   A O     1 
ATOM   1775  C  CB    . ASN   A 1  226 ? 10.843  84.551  54.820  1.00 34.13  ? 226 ASN   A CB    1 
ATOM   1776  C  CG    . ASN   A 1  226 ? 9.923   84.758  53.647  1.00 34.31  ? 226 ASN   A CG    1 
ATOM   1777  O  OD1   . ASN   A 1  226 ? 9.424   83.798  53.033  1.00 28.11  ? 226 ASN   A OD1   1 
ATOM   1778  N  ND2   . ASN   A 1  226 ? 9.703   86.024  53.311  1.00 30.55  ? 226 ASN   A ND2   1 
ATOM   1779  N  N     . LEU   A 1  227 ? 13.604  83.555  55.477  1.00 32.33  ? 227 LEU   A N     1 
ATOM   1780  C  CA    . LEU   A 1  227 ? 14.590  82.979  56.379  1.00 25.87  ? 227 LEU   A CA    1 
ATOM   1781  C  C     . LEU   A 1  227 ? 15.777  83.914  56.548  1.00 28.89  ? 227 LEU   A C     1 
ATOM   1782  O  O     . LEU   A 1  227 ? 16.178  84.240  57.671  1.00 29.23  ? 227 LEU   A O     1 
ATOM   1783  C  CB    . LEU   A 1  227 ? 15.054  81.625  55.855  1.00 26.91  ? 227 LEU   A CB    1 
ATOM   1784  C  CG    . LEU   A 1  227 ? 13.997  80.578  55.517  1.00 26.25  ? 227 LEU   A CG    1 
ATOM   1785  C  CD1   . LEU   A 1  227 ? 14.647  79.204  55.422  1.00 19.58  ? 227 LEU   A CD1   1 
ATOM   1786  C  CD2   . LEU   A 1  227 ? 12.914  80.587  56.568  1.00 27.31  ? 227 LEU   A CD2   1 
ATOM   1787  N  N     . ASN   A 1  228 ? 16.341  84.373  55.433  1.00 29.26  ? 228 ASN   A N     1 
ATOM   1788  C  CA    . ASN   A 1  228 ? 17.579  85.139  55.503  1.00 31.80  ? 228 ASN   A CA    1 
ATOM   1789  C  C     . ASN   A 1  228 ? 17.372  86.517  56.130  1.00 26.15  ? 228 ASN   A C     1 
ATOM   1790  O  O     . ASN   A 1  228 ? 18.290  87.033  56.772  1.00 25.85  ? 228 ASN   A O     1 
ATOM   1791  C  CB    . ASN   A 1  228 ? 18.220  85.242  54.110  1.00 26.18  ? 228 ASN   A CB    1 
ATOM   1792  C  CG    . ASN   A 1  228 ? 18.812  83.908  53.639  1.00 29.26  ? 228 ASN   A CG    1 
ATOM   1793  O  OD1   . ASN   A 1  228 ? 18.910  82.945  54.408  1.00 26.56  ? 228 ASN   A OD1   1 
ATOM   1794  N  ND2   . ASN   A 1  228 ? 19.211  83.852  52.369  1.00 32.42  ? 228 ASN   A ND2   1 
ATOM   1795  N  N     . ARG   A 1  229 ? 16.187  87.113  55.998  1.00 24.52  ? 229 ARG   A N     1 
ATOM   1796  C  CA    . ARG   A 1  229 ? 15.934  88.390  56.670  1.00 27.38  ? 229 ARG   A CA    1 
ATOM   1797  C  C     . ARG   A 1  229 ? 15.909  88.231  58.187  1.00 27.36  ? 229 ARG   A C     1 
ATOM   1798  O  O     . ARG   A 1  229 ? 16.521  89.021  58.912  1.00 32.02  ? 229 ARG   A O     1 
ATOM   1799  C  CB    . ARG   A 1  229 ? 14.627  89.000  56.182  1.00 26.65  ? 229 ARG   A CB    1 
ATOM   1800  C  CG    . ARG   A 1  229 ? 14.712  89.557  54.791  1.00 29.74  ? 229 ARG   A CG    1 
ATOM   1801  C  CD    . ARG   A 1  229 ? 13.790  90.720  54.650  1.00 38.27  ? 229 ARG   A CD    1 
ATOM   1802  N  NE    . ARG   A 1  229 ? 14.234  91.590  53.576  1.00 43.40  ? 229 ARG   A NE    1 
ATOM   1803  C  CZ    . ARG   A 1  229 ? 13.622  91.700  52.410  1.00 43.35  ? 229 ARG   A CZ    1 
ATOM   1804  N  NH1   . ARG   A 1  229 ? 12.504  91.033  52.153  1.00 35.96  ? 229 ARG   A NH1   1 
ATOM   1805  N  NH2   . ARG   A 1  229 ? 14.144  92.501  51.483  1.00 41.34  ? 229 ARG   A NH2   1 
ATOM   1806  N  N     . LEU   A 1  230 ? 15.198  87.221  58.685  1.00 23.76  ? 230 LEU   A N     1 
ATOM   1807  C  CA    . LEU   A 1  230 ? 15.208  86.935  60.114  1.00 25.55  ? 230 LEU   A CA    1 
ATOM   1808  C  C     . LEU   A 1  230 ? 16.616  86.628  60.605  1.00 26.75  ? 230 LEU   A C     1 
ATOM   1809  O  O     . LEU   A 1  230 ? 17.028  87.102  61.668  1.00 35.36  ? 230 LEU   A O     1 
ATOM   1810  C  CB    . LEU   A 1  230 ? 14.252  85.771  60.428  1.00 26.34  ? 230 LEU   A CB    1 
ATOM   1811  C  CG    . LEU   A 1  230 ? 13.852  85.508  61.887  1.00 24.97  ? 230 LEU   A CG    1 
ATOM   1812  C  CD1   . LEU   A 1  230 ? 13.225  86.741  62.529  1.00 23.58  ? 230 LEU   A CD1   1 
ATOM   1813  C  CD2   . LEU   A 1  230 ? 12.944  84.305  62.007  1.00 20.67  ? 230 LEU   A CD2   1 
ATOM   1814  N  N     . ILE   A 1  231 ? 17.382  85.844  59.851  1.00 29.65  ? 231 ILE   A N     1 
ATOM   1815  C  CA    . ILE   A 1  231 ? 18.735  85.561  60.312  1.00 26.77  ? 231 ILE   A CA    1 
ATOM   1816  C  C     . ILE   A 1  231 ? 19.563  86.834  60.422  1.00 29.08  ? 231 ILE   A C     1 
ATOM   1817  O  O     . ILE   A 1  231 ? 20.524  86.886  61.195  1.00 35.82  ? 231 ILE   A O     1 
ATOM   1818  C  CB    . ILE   A 1  231 ? 19.435  84.545  59.404  1.00 27.93  ? 231 ILE   A CB    1 
ATOM   1819  C  CG1   . ILE   A 1  231 ? 18.551  83.322  59.149  1.00 25.19  ? 231 ILE   A CG1   1 
ATOM   1820  C  CG2   . ILE   A 1  231 ? 20.741  84.133  60.055  1.00 23.22  ? 231 ILE   A CG2   1 
ATOM   1821  C  CD1   . ILE   A 1  231 ? 19.176  82.397  58.157  1.00 25.22  ? 231 ILE   A CD1   1 
ATOM   1822  N  N     . SER   A 1  232 ? 19.217  87.877  59.663  1.00 30.92  ? 232 SER   A N     1 
ATOM   1823  C  CA    . SER   A 1  232 ? 19.988  89.121  59.694  1.00 30.94  ? 232 SER   A CA    1 
ATOM   1824  C  C     . SER   A 1  232 ? 19.685  89.957  60.918  1.00 29.56  ? 232 SER   A C     1 
ATOM   1825  O  O     . SER   A 1  232 ? 20.556  90.706  61.377  1.00 34.31  ? 232 SER   A O     1 
ATOM   1826  C  CB    . SER   A 1  232 ? 19.705  89.969  58.461  1.00 34.49  ? 232 SER   A CB    1 
ATOM   1827  O  OG    . SER   A 1  232 ? 19.505  89.152  57.329  1.00 42.07  ? 232 SER   A OG    1 
ATOM   1828  N  N     . GLN   A 1  233 ? 18.455  89.877  61.422  1.00 26.22  ? 233 GLN   A N     1 
ATOM   1829  C  CA    . GLN   A 1  233 ? 18.126  90.499  62.702  1.00 30.67  ? 233 GLN   A CA    1 
ATOM   1830  C  C     . GLN   A 1  233 ? 18.931  89.869  63.835  1.00 28.67  ? 233 GLN   A C     1 
ATOM   1831  O  O     . GLN   A 1  233 ? 19.668  90.559  64.546  1.00 27.98  ? 233 GLN   A O     1 
ATOM   1832  C  CB    . GLN   A 1  233 ? 16.627  90.373  62.973  1.00 30.53  ? 233 GLN   A CB    1 
ATOM   1833  C  CG    . GLN   A 1  233 ? 15.750  91.101  62.002  1.00 27.89  ? 233 GLN   A CG    1 
ATOM   1834  C  CD    . GLN   A 1  233 ? 15.818  92.590  62.182  1.00 34.16  ? 233 GLN   A CD    1 
ATOM   1835  O  OE1   . GLN   A 1  233 ? 15.657  93.088  63.291  1.00 48.72  ? 233 GLN   A OE1   1 
ATOM   1836  N  NE2   . GLN   A 1  233 ? 16.043  93.316  61.095  1.00 36.27  ? 233 GLN   A NE2   1 
ATOM   1837  N  N     . ILE   A 1  234 ? 18.809  88.550  64.009  1.00 23.67  ? 234 ILE   A N     1 
ATOM   1838  C  CA    . ILE   A 1  234 ? 19.587  87.858  65.032  1.00 25.31  ? 234 ILE   A CA    1 
ATOM   1839  C  C     . ILE   A 1  234 ? 21.075  88.130  64.835  1.00 25.89  ? 234 ILE   A C     1 
ATOM   1840  O  O     . ILE   A 1  234 ? 21.783  88.460  65.784  1.00 26.76  ? 234 ILE   A O     1 
ATOM   1841  C  CB    . ILE   A 1  234 ? 19.268  86.346  65.027  1.00 29.76  ? 234 ILE   A CB    1 
ATOM   1842  C  CG1   . ILE   A 1  234 ? 17.807  86.101  65.341  1.00 26.64  ? 234 ILE   A CG1   1 
ATOM   1843  C  CG2   . ILE   A 1  234 ? 20.050  85.579  66.071  1.00 27.00  ? 234 ILE   A CG2   1 
ATOM   1844  C  CD1   . ILE   A 1  234 ? 16.899  86.534  64.262  1.00 31.84  ? 234 ILE   A CD1   1 
ATOM   1845  N  N     . VAL   A 1  235 ? 21.576  88.023  63.598  1.00 27.57  ? 235 VAL   A N     1 
ATOM   1846  C  CA    . VAL   A 1  235 ? 23.003  88.280  63.385  1.00 29.75  ? 235 VAL   A CA    1 
ATOM   1847  C  C     . VAL   A 1  235 ? 23.358  89.710  63.780  1.00 31.42  ? 235 VAL   A C     1 
ATOM   1848  O  O     . VAL   A 1  235 ? 24.423  89.963  64.355  1.00 34.25  ? 235 VAL   A O     1 
ATOM   1849  C  CB    . VAL   A 1  235 ? 23.422  87.986  61.931  1.00 25.91  ? 235 VAL   A CB    1 
ATOM   1850  C  CG1   . VAL   A 1  235 ? 24.853  88.422  61.709  1.00 22.47  ? 235 VAL   A CG1   1 
ATOM   1851  C  CG2   . VAL   A 1  235 ? 23.306  86.516  61.646  1.00 28.02  ? 235 VAL   A CG2   1 
ATOM   1852  N  N     . SER   A 1  236 ? 22.485  90.667  63.467  1.00 30.21  ? 236 SER   A N     1 
ATOM   1853  C  CA    . SER   A 1  236 ? 22.757  92.059  63.797  1.00 23.58  ? 236 SER   A CA    1 
ATOM   1854  C  C     . SER   A 1  236 ? 22.728  92.304  65.304  1.00 27.69  ? 236 SER   A C     1 
ATOM   1855  O  O     . SER   A 1  236 ? 23.405  93.211  65.796  1.00 36.26  ? 236 SER   A O     1 
ATOM   1856  C  CB    . SER   A 1  236 ? 21.744  92.952  63.086  1.00 30.03  ? 236 SER   A CB    1 
ATOM   1857  O  OG    . SER   A 1  236 ? 21.803  94.289  63.564  1.00 35.26  ? 236 SER   A OG    1 
ATOM   1858  N  N     . SER   A 1  237 ? 21.949  91.525  66.056  1.00 28.49  ? 237 SER   A N     1 
ATOM   1859  C  CA    . SER   A 1  237 ? 21.988  91.618  67.517  1.00 30.71  ? 237 SER   A CA    1 
ATOM   1860  C  C     . SER   A 1  237 ? 23.317  91.110  68.075  1.00 33.49  ? 237 SER   A C     1 
ATOM   1861  O  O     . SER   A 1  237 ? 23.886  91.719  68.996  1.00 35.07  ? 237 SER   A O     1 
ATOM   1862  C  CB    . SER   A 1  237 ? 20.842  90.813  68.124  1.00 31.75  ? 237 SER   A CB    1 
ATOM   1863  O  OG    . SER   A 1  237 ? 19.679  90.890  67.336  1.00 27.41  ? 237 SER   A OG    1 
ATOM   1864  N  N     . ILE   A 1  238 ? 23.804  89.976  67.545  1.00 25.32  ? 238 ILE   A N     1 
ATOM   1865  C  CA    . ILE   A 1  238 ? 25.084  89.409  67.953  1.00 23.42  ? 238 ILE   A CA    1 
ATOM   1866  C  C     . ILE   A 1  238 ? 26.243  90.349  67.630  1.00 30.84  ? 238 ILE   A C     1 
ATOM   1867  O  O     . ILE   A 1  238 ? 27.246  90.376  68.360  1.00 34.97  ? 238 ILE   A O     1 
ATOM   1868  C  CB    . ILE   A 1  238 ? 25.311  88.041  67.293  1.00 21.62  ? 238 ILE   A CB    1 
ATOM   1869  C  CG1   . ILE   A 1  238 ? 24.413  86.995  67.895  1.00 28.18  ? 238 ILE   A CG1   1 
ATOM   1870  C  CG2   . ILE   A 1  238 ? 26.713  87.573  67.571  1.00 29.86  ? 238 ILE   A CG2   1 
ATOM   1871  C  CD1   . ILE   A 1  238 ? 22.998  87.238  67.712  1.00 33.78  ? 238 ILE   A CD1   1 
ATOM   1872  N  N     . THR   A 1  239 ? 26.147  91.125  66.542  1.00 23.36  ? 239 THR   A N     1 
ATOM   1873  C  CA    . THR   A 1  239 ? 27.252  91.988  66.134  1.00 27.80  ? 239 THR   A CA    1 
ATOM   1874  C  C     . THR   A 1  239 ? 27.039  93.460  66.448  1.00 33.68  ? 239 THR   A C     1 
ATOM   1875  O  O     . THR   A 1  239 ? 27.982  94.243  66.287  1.00 38.09  ? 239 THR   A O     1 
ATOM   1876  C  CB    . THR   A 1  239 ? 27.534  91.873  64.629  1.00 30.54  ? 239 THR   A CB    1 
ATOM   1877  O  OG1   . THR   A 1  239 ? 26.356  92.226  63.889  1.00 28.76  ? 239 THR   A OG1   1 
ATOM   1878  C  CG2   . THR   A 1  239 ? 28.021  90.468  64.260  1.00 26.00  ? 239 THR   A CG2   1 
ATOM   1879  N  N     . ALA   A 1  240 ? 25.833  93.861  66.862  1.00 33.00  ? 240 ALA   A N     1 
ATOM   1880  C  CA    . ALA   A 1  240 ? 25.603  95.254  67.223  1.00 25.22  ? 240 ALA   A CA    1 
ATOM   1881  C  C     . ALA   A 1  240 ? 26.700  95.774  68.140  1.00 32.18  ? 240 ALA   A C     1 
ATOM   1882  O  O     . ALA   A 1  240 ? 27.205  96.887  67.946  1.00 33.97  ? 240 ALA   A O     1 
ATOM   1883  C  CB    . ALA   A 1  240 ? 24.240  95.399  67.881  1.00 22.31  ? 240 ALA   A CB    1 
ATOM   1884  N  N     . SER   A 1  241 ? 27.118  94.962  69.118  1.00 29.90  ? 241 SER   A N     1 
ATOM   1885  C  CA    . SER   A 1  241 ? 28.099  95.420  70.099  1.00 27.02  ? 241 SER   A CA    1 
ATOM   1886  C  C     . SER   A 1  241 ? 29.457  95.759  69.488  1.00 32.99  ? 241 SER   A C     1 
ATOM   1887  O  O     . SER   A 1  241 ? 30.238  96.472  70.123  1.00 41.61  ? 241 SER   A O     1 
ATOM   1888  C  CB    . SER   A 1  241 ? 28.288  94.382  71.221  1.00 32.06  ? 241 SER   A CB    1 
ATOM   1889  O  OG    . SER   A 1  241 ? 28.496  93.051  70.752  1.00 38.23  ? 241 SER   A OG    1 
ATOM   1890  N  N     . LEU   A 1  242 ? 29.768  95.273  68.288  1.00 36.54  ? 242 LEU   A N     1 
ATOM   1891  C  CA    . LEU   A 1  242 ? 31.062  95.545  67.674  1.00 29.44  ? 242 LEU   A CA    1 
ATOM   1892  C  C     . LEU   A 1  242 ? 31.063  96.806  66.830  1.00 34.71  ? 242 LEU   A C     1 
ATOM   1893  O  O     . LEU   A 1  242 ? 32.126  97.180  66.328  1.00 35.16  ? 242 LEU   A O     1 
ATOM   1894  C  CB    . LEU   A 1  242 ? 31.489  94.375  66.791  1.00 26.39  ? 242 LEU   A CB    1 
ATOM   1895  C  CG    . LEU   A 1  242 ? 31.506  92.981  67.394  1.00 24.78  ? 242 LEU   A CG    1 
ATOM   1896  C  CD1   . LEU   A 1  242 ? 31.538  91.935  66.296  1.00 26.11  ? 242 LEU   A CD1   1 
ATOM   1897  C  CD2   . LEU   A 1  242 ? 32.742  92.859  68.233  1.00 36.33  ? 242 LEU   A CD2   1 
ATOM   1898  N  N     . ARG   A 1  243 ? 29.902  97.452  66.653  1.00 30.88  ? 243 ARG   A N     1 
ATOM   1899  C  CA    . ARG   A 1  243 ? 29.728  98.546  65.705  1.00 33.18  ? 243 ARG   A CA    1 
ATOM   1900  C  C     . ARG   A 1  243 ? 29.049  99.735  66.357  1.00 38.77  ? 243 ARG   A C     1 
ATOM   1901  O  O     . ARG   A 1  243 ? 28.752  100.732 65.676  1.00 34.03  ? 243 ARG   A O     1 
ATOM   1902  C  CB    . ARG   A 1  243 ? 28.900  98.091  64.484  1.00 26.79  ? 243 ARG   A CB    1 
ATOM   1903  C  CG    . ARG   A 1  243 ? 29.072  96.629  64.144  1.00 27.32  ? 243 ARG   A CG    1 
ATOM   1904  C  CD    . ARG   A 1  243 ? 28.166  96.194  63.009  1.00 31.72  ? 243 ARG   A CD    1 
ATOM   1905  N  NE    . ARG   A 1  243 ? 26.967  95.494  63.460  1.00 29.48  ? 243 ARG   A NE    1 
ATOM   1906  C  CZ    . ARG   A 1  243 ? 25.733  95.945  63.282  1.00 31.01  ? 243 ARG   A CZ    1 
ATOM   1907  N  NH1   . ARG   A 1  243 ? 25.497  97.091  62.656  1.00 28.84  ? 243 ARG   A NH1   1 
ATOM   1908  N  NH2   . ARG   A 1  243 ? 24.710  95.229  63.739  1.00 27.27  ? 243 ARG   A NH2   1 
ATOM   1909  N  N     . PHE   A 1  244 ? 28.775  99.644  67.650  1.00 30.31  ? 244 PHE   A N     1 
ATOM   1910  C  CA    . PHE   A 1  244 ? 28.121  100.702 68.377  1.00 26.33  ? 244 PHE   A CA    1 
ATOM   1911  C  C     . PHE   A 1  244 ? 28.882  100.933 69.669  1.00 34.74  ? 244 PHE   A C     1 
ATOM   1912  O  O     . PHE   A 1  244 ? 29.733  100.131 70.073  1.00 38.99  ? 244 PHE   A O     1 
ATOM   1913  C  CB    . PHE   A 1  244 ? 26.654  100.354 68.633  1.00 36.62  ? 244 PHE   A CB    1 
ATOM   1914  C  CG    . PHE   A 1  244 ? 25.814  100.286 67.373  1.00 35.61  ? 244 PHE   A CG    1 
ATOM   1915  C  CD1   . PHE   A 1  244 ? 25.333  101.436 66.783  1.00 32.94  ? 244 PHE   A CD1   1 
ATOM   1916  C  CD2   . PHE   A 1  244 ? 25.497  99.073  66.790  1.00 31.20  ? 244 PHE   A CD2   1 
ATOM   1917  C  CE1   . PHE   A 1  244 ? 24.580  101.373 65.637  1.00 23.30  ? 244 PHE   A CE1   1 
ATOM   1918  C  CE2   . PHE   A 1  244 ? 24.732  99.022  65.654  1.00 24.87  ? 244 PHE   A CE2   1 
ATOM   1919  C  CZ    . PHE   A 1  244 ? 24.278  100.172 65.083  1.00 25.61  ? 244 PHE   A CZ    1 
ATOM   1920  N  N     . ASP   A 1  245 ? 28.597  102.065 70.299  1.00 37.76  ? 245 ASP   A N     1 
ATOM   1921  C  CA    . ASP   A 1  245 ? 29.263  102.421 71.538  1.00 33.56  ? 245 ASP   A CA    1 
ATOM   1922  C  C     . ASP   A 1  245 ? 28.708  101.553 72.658  1.00 44.57  ? 245 ASP   A C     1 
ATOM   1923  O  O     . ASP   A 1  245 ? 27.493  101.509 72.875  1.00 41.79  ? 245 ASP   A O     1 
ATOM   1924  C  CB    . ASP   A 1  245 ? 29.051  103.901 71.826  1.00 41.02  ? 245 ASP   A CB    1 
ATOM   1925  C  CG    . ASP   A 1  245 ? 29.844  104.384 73.016  1.00 44.41  ? 245 ASP   A CG    1 
ATOM   1926  O  OD1   . ASP   A 1  245 ? 30.865  103.742 73.346  1.00 43.26  ? 245 ASP   A OD1   1 
ATOM   1927  O  OD2   . ASP   A 1  245 ? 29.437  105.398 73.626  1.00 41.99  ? 245 ASP   A OD2   1 
ATOM   1928  N  N     . GLY   A 1  246 ? 29.593  100.841 73.348  1.00 42.94  ? 246 GLY   A N     1 
ATOM   1929  C  CA    . GLY   A 1  246 ? 29.176  99.976  74.434  1.00 37.38  ? 246 GLY   A CA    1 
ATOM   1930  C  C     . GLY   A 1  246 ? 30.369  99.565  75.269  1.00 40.39  ? 246 GLY   A C     1 
ATOM   1931  O  O     . GLY   A 1  246 ? 31.512  99.933  74.985  1.00 37.92  ? 246 GLY   A O     1 
ATOM   1932  N  N     . ALA   A 1  247 ? 30.081  98.804  76.329  1.00 33.63  ? 247 ALA   A N     1 
ATOM   1933  C  CA    . ALA   A 1  247 ? 31.123  98.208  77.152  1.00 38.70  ? 247 ALA   A CA    1 
ATOM   1934  C  C     . ALA   A 1  247 ? 31.092  96.683  77.142  1.00 36.22  ? 247 ALA   A C     1 
ATOM   1935  O  O     . ALA   A 1  247 ? 32.068  96.060  77.578  1.00 40.64  ? 247 ALA   A O     1 
ATOM   1936  C  CB    . ALA   A 1  247 ? 31.026  98.713  78.606  1.00 33.54  ? 247 ALA   A CB    1 
ATOM   1937  N  N     . LEU   A 1  248 ? 30.010  96.074  76.658  1.00 32.46  ? 248 LEU   A N     1 
ATOM   1938  C  CA    . LEU   A 1  248 ? 29.825  94.630  76.639  1.00 34.89  ? 248 LEU   A CA    1 
ATOM   1939  C  C     . LEU   A 1  248 ? 29.940  94.122  75.202  1.00 41.78  ? 248 LEU   A C     1 
ATOM   1940  O  O     . LEU   A 1  248 ? 29.365  94.722  74.276  1.00 32.80  ? 248 LEU   A O     1 
ATOM   1941  C  CB    . LEU   A 1  248 ? 28.465  94.249  77.236  1.00 26.84  ? 248 LEU   A CB    1 
ATOM   1942  C  CG    . LEU   A 1  248 ? 27.940  92.840  76.938  1.00 25.64  ? 248 LEU   A CG    1 
ATOM   1943  C  CD1   . LEU   A 1  248 ? 28.620  91.787  77.802  1.00 25.04  ? 248 LEU   A CD1   1 
ATOM   1944  C  CD2   . LEU   A 1  248 ? 26.435  92.758  77.090  1.00 29.38  ? 248 LEU   A CD2   1 
ATOM   1945  N  N     . ASN   A 1  249 ? 30.688  93.016  75.034  1.00 31.84  ? 249 ASN   A N     1 
ATOM   1946  C  CA    . ASN   A 1  249 ? 30.981  92.403  73.736  1.00 34.17  ? 249 ASN   A CA    1 
ATOM   1947  C  C     . ASN   A 1  249 ? 31.602  93.408  72.756  1.00 40.10  ? 249 ASN   A C     1 
ATOM   1948  O  O     . ASN   A 1  249 ? 31.134  93.586  71.625  1.00 34.84  ? 249 ASN   A O     1 
ATOM   1949  C  CB    . ASN   A 1  249 ? 29.724  91.737  73.161  1.00 34.00  ? 249 ASN   A CB    1 
ATOM   1950  C  CG    . ASN   A 1  249 ? 29.315  90.502  73.957  1.00 26.00  ? 249 ASN   A CG    1 
ATOM   1951  O  OD1   . ASN   A 1  249 ? 30.115  89.945  74.700  1.00 20.20  ? 249 ASN   A OD1   1 
ATOM   1952  N  ND2   . ASN   A 1  249 ? 28.071  90.073  73.800  1.00 23.64  ? 249 ASN   A ND2   1 
ATOM   1953  N  N     . VAL   A 1  250 ? 32.683  94.060  73.206  1.00 37.31  ? 250 VAL   A N     1 
ATOM   1954  C  CA    . VAL   A 1  250 ? 33.328  95.129  72.441  1.00 35.87  ? 250 VAL   A CA    1 
ATOM   1955  C  C     . VAL   A 1  250 ? 34.286  94.597  71.382  1.00 41.21  ? 250 VAL   A C     1 
ATOM   1956  O  O     . VAL   A 1  250 ? 34.608  95.324  70.435  1.00 42.47  ? 250 VAL   A O     1 
ATOM   1957  C  CB    . VAL   A 1  250 ? 34.132  96.090  73.340  1.00 40.05  ? 250 VAL   A CB    1 
ATOM   1958  C  CG1   . VAL   A 1  250 ? 34.391  97.404  72.621  1.00 42.07  ? 250 VAL   A CG1   1 
ATOM   1959  C  CG2   . VAL   A 1  250 ? 33.444  96.331  74.660  1.00 36.64  ? 250 VAL   A CG2   1 
ATOM   1960  N  N     . ASP   A 1  251 ? 34.786  93.371  71.542  1.00 44.00  ? 251 ASP   A N     1 
ATOM   1961  C  CA    . ASP   A 1  251 ? 35.682  92.742  70.580  1.00 40.58  ? 251 ASP   A CA    1 
ATOM   1962  C  C     . ASP   A 1  251 ? 35.548  91.229  70.720  1.00 45.79  ? 251 ASP   A C     1 
ATOM   1963  O  O     . ASP   A 1  251 ? 35.062  90.726  71.738  1.00 39.11  ? 251 ASP   A O     1 
ATOM   1964  C  CB    . ASP   A 1  251 ? 37.137  93.174  70.780  1.00 39.68  ? 251 ASP   A CB    1 
ATOM   1965  C  CG    . ASP   A 1  251 ? 37.871  92.307  71.808  1.00 56.77  ? 251 ASP   A CG    1 
ATOM   1966  O  OD1   . ASP   A 1  251 ? 37.381  92.173  72.957  1.00 58.96  ? 251 ASP   A OD1   1 
ATOM   1967  O  OD2   . ASP   A 1  251 ? 38.942  91.749  71.462  1.00 59.61  ? 251 ASP   A OD2   1 
ATOM   1968  N  N     . LEU   A 1  252 ? 36.035  90.510  69.696  1.00 48.38  ? 252 LEU   A N     1 
ATOM   1969  C  CA    . LEU   A 1  252 ? 35.671  89.105  69.492  1.00 40.94  ? 252 LEU   A CA    1 
ATOM   1970  C  C     . LEU   A 1  252 ? 36.188  88.190  70.600  1.00 37.02  ? 252 LEU   A C     1 
ATOM   1971  O  O     . LEU   A 1  252 ? 35.542  87.185  70.924  1.00 33.92  ? 252 LEU   A O     1 
ATOM   1972  C  CB    . LEU   A 1  252 ? 36.191  88.631  68.134  1.00 40.35  ? 252 LEU   A CB    1 
ATOM   1973  C  CG    . LEU   A 1  252 ? 35.728  89.415  66.913  1.00 28.71  ? 252 LEU   A CG    1 
ATOM   1974  C  CD1   . LEU   A 1  252 ? 36.440  88.890  65.697  1.00 27.96  ? 252 LEU   A CD1   1 
ATOM   1975  C  CD2   . LEU   A 1  252 ? 34.203  89.341  66.761  1.00 32.17  ? 252 LEU   A CD2   1 
ATOM   1976  N  N     . THR   A 1  253 ? 37.347  88.493  71.177  1.00 34.36  ? 253 THR   A N     1 
ATOM   1977  C  CA    . THR   A 1  253 ? 37.799  87.708  72.321  1.00 39.86  ? 253 THR   A CA    1 
ATOM   1978  C  C     . THR   A 1  253 ? 36.764  87.735  73.440  1.00 42.53  ? 253 THR   A C     1 
ATOM   1979  O  O     . THR   A 1  253 ? 36.547  86.731  74.132  1.00 41.06  ? 253 THR   A O     1 
ATOM   1980  C  CB    . THR   A 1  253 ? 39.146  88.230  72.822  1.00 45.65  ? 253 THR   A CB    1 
ATOM   1981  O  OG1   . THR   A 1  253 ? 39.601  89.281  71.955  1.00 50.20  ? 253 THR   A OG1   1 
ATOM   1982  C  CG2   . THR   A 1  253 ? 40.187  87.099  72.861  1.00 39.38  ? 253 THR   A CG2   1 
ATOM   1983  N  N     . GLU   A 1  254 ? 36.103  88.875  73.624  1.00 45.62  ? 254 GLU   A N     1 
ATOM   1984  C  CA    . GLU   A 1  254 ? 35.087  88.962  74.663  1.00 41.78  ? 254 GLU   A CA    1 
ATOM   1985  C  C     . GLU   A 1  254 ? 33.971  87.948  74.446  1.00 35.39  ? 254 GLU   A C     1 
ATOM   1986  O  O     . GLU   A 1  254 ? 33.400  87.443  75.420  1.00 35.37  ? 254 GLU   A O     1 
ATOM   1987  C  CB    . GLU   A 1  254 ? 34.525  90.380  74.718  1.00 38.51  ? 254 GLU   A CB    1 
ATOM   1988  C  CG    . GLU   A 1  254 ? 34.003  90.753  76.079  1.00 39.51  ? 254 GLU   A CG    1 
ATOM   1989  C  CD    . GLU   A 1  254 ? 33.329  92.105  76.082  1.00 47.59  ? 254 GLU   A CD    1 
ATOM   1990  O  OE1   . GLU   A 1  254 ? 33.779  92.987  75.314  1.00 47.23  ? 254 GLU   A OE1   1 
ATOM   1991  O  OE2   . GLU   A 1  254 ? 32.343  92.280  76.844  1.00 46.25  ? 254 GLU   A OE2   1 
ATOM   1992  N  N     . PHE   A 1  255 ? 33.648  87.636  73.183  1.00 30.21  ? 255 PHE   A N     1 
ATOM   1993  C  CA    . PHE   A 1  255 ? 32.607  86.650  72.905  1.00 31.12  ? 255 PHE   A CA    1 
ATOM   1994  C  C     . PHE   A 1  255 ? 32.947  85.283  73.512  1.00 40.40  ? 255 PHE   A C     1 
ATOM   1995  O  O     . PHE   A 1  255 ? 32.085  84.636  74.125  1.00 33.36  ? 255 PHE   A O     1 
ATOM   1996  C  CB    . PHE   A 1  255 ? 32.385  86.525  71.397  1.00 35.61  ? 255 PHE   A CB    1 
ATOM   1997  C  CG    . PHE   A 1  255 ? 31.431  87.545  70.814  1.00 34.22  ? 255 PHE   A CG    1 
ATOM   1998  C  CD1   . PHE   A 1  255 ? 30.077  87.290  70.760  1.00 24.16  ? 255 PHE   A CD1   1 
ATOM   1999  C  CD2   . PHE   A 1  255 ? 31.902  88.730  70.259  1.00 34.84  ? 255 PHE   A CD2   1 
ATOM   2000  C  CE1   . PHE   A 1  255 ? 29.205  88.202  70.200  1.00 27.00  ? 255 PHE   A CE1   1 
ATOM   2001  C  CE2   . PHE   A 1  255 ? 31.031  89.651  69.701  1.00 26.62  ? 255 PHE   A CE2   1 
ATOM   2002  C  CZ    . PHE   A 1  255 ? 29.685  89.384  69.669  1.00 28.70  ? 255 PHE   A CZ    1 
ATOM   2003  N  N     . GLN   A 1  256 ? 34.190  84.812  73.346  1.00 35.47  ? 256 GLN   A N     1 
ATOM   2004  C  CA    . GLN   A 1  256 ? 34.511  83.509  73.905  1.00 30.22  ? 256 GLN   A CA    1 
ATOM   2005  C  C     . GLN   A 1  256 ? 34.685  83.588  75.413  1.00 33.77  ? 256 GLN   A C     1 
ATOM   2006  O  O     . GLN   A 1  256 ? 34.353  82.639  76.129  1.00 33.87  ? 256 GLN   A O     1 
ATOM   2007  C  CB    . GLN   A 1  256 ? 35.759  82.939  73.241  1.00 34.44  ? 256 GLN   A CB    1 
ATOM   2008  C  CG    . GLN   A 1  256 ? 37.056  83.538  73.726  1.00 43.60  ? 256 GLN   A CG    1 
ATOM   2009  C  CD    . GLN   A 1  256 ? 38.167  83.482  72.668  1.00 52.63  ? 256 GLN   A CD    1 
ATOM   2010  O  OE1   . GLN   A 1  256 ? 38.070  84.106  71.599  1.00 47.23  ? 256 GLN   A OE1   1 
ATOM   2011  N  NE2   . GLN   A 1  256 ? 39.231  82.742  72.970  1.00 60.42  ? 256 GLN   A NE2   1 
ATOM   2012  N  N     . THR   A 1  257 ? 35.169  84.720  75.919  1.00 40.21  ? 257 THR   A N     1 
ATOM   2013  C  CA    . THR   A 1  257 ? 35.238  84.898  77.367  1.00 36.83  ? 257 THR   A CA    1 
ATOM   2014  C  C     . THR   A 1  257 ? 33.848  84.885  77.992  1.00 34.54  ? 257 THR   A C     1 
ATOM   2015  O  O     . THR   A 1  257 ? 33.651  84.351  79.090  1.00 46.48  ? 257 THR   A O     1 
ATOM   2016  C  CB    . THR   A 1  257 ? 35.955  86.204  77.699  1.00 25.55  ? 257 THR   A CB    1 
ATOM   2017  O  OG1   . THR   A 1  257 ? 37.368  85.990  77.653  1.00 24.46  ? 257 THR   A OG1   1 
ATOM   2018  C  CG2   . THR   A 1  257 ? 35.568  86.641  79.075  1.00 28.54  ? 257 THR   A CG2   1 
ATOM   2019  N  N     . ASN   A 1  258 ? 32.876  85.476  77.317  1.00 32.30  ? 258 ASN   A N     1 
ATOM   2020  C  CA    . ASN   A 1  258 ? 31.549  85.597  77.887  1.00 34.15  ? 258 ASN   A CA    1 
ATOM   2021  C  C     . ASN   A 1  258 ? 30.706  84.356  77.673  1.00 31.07  ? 258 ASN   A C     1 
ATOM   2022  O  O     . ASN   A 1  258 ? 29.918  83.993  78.553  1.00 38.28  ? 258 ASN   A O     1 
ATOM   2023  C  CB    . ASN   A 1  258 ? 30.845  86.828  77.301  1.00 38.26  ? 258 ASN   A CB    1 
ATOM   2024  C  CG    . ASN   A 1  258 ? 31.248  88.109  78.009  1.00 33.48  ? 258 ASN   A CG    1 
ATOM   2025  O  OD1   . ASN   A 1  258 ? 31.691  88.066  79.148  1.00 42.88  ? 258 ASN   A OD1   1 
ATOM   2026  N  ND2   . ASN   A 1  258 ? 31.105  89.237  77.345  1.00 25.37  ? 258 ASN   A ND2   1 
ATOM   2027  N  N     . LEU   A 1  259 ? 30.865  83.676  76.542  1.00 32.43  ? 259 LEU   A N     1 
ATOM   2028  C  CA    . LEU   A 1  259 ? 29.977  82.577  76.206  1.00 31.19  ? 259 LEU   A CA    1 
ATOM   2029  C  C     . LEU   A 1  259 ? 30.629  81.207  76.266  1.00 29.17  ? 259 LEU   A C     1 
ATOM   2030  O  O     . LEU   A 1  259 ? 29.900  80.212  76.321  1.00 25.20  ? 259 LEU   A O     1 
ATOM   2031  C  CB    . LEU   A 1  259 ? 29.390  82.783  74.799  1.00 31.78  ? 259 LEU   A CB    1 
ATOM   2032  C  CG    . LEU   A 1  259 ? 28.726  84.137  74.552  1.00 30.47  ? 259 LEU   A CG    1 
ATOM   2033  C  CD1   . LEU   A 1  259 ? 28.270  84.296  73.096  1.00 29.06  ? 259 LEU   A CD1   1 
ATOM   2034  C  CD2   . LEU   A 1  259 ? 27.567  84.313  75.527  1.00 28.78  ? 259 LEU   A CD2   1 
ATOM   2035  N  N     . VAL   A 1  260 ? 31.958  81.120  76.263  1.00 27.10  ? 260 VAL   A N     1 
ATOM   2036  C  CA    . VAL   A 1  260 ? 32.602  79.833  76.000  1.00 34.93  ? 260 VAL   A CA    1 
ATOM   2037  C  C     . VAL   A 1  260 ? 33.664  79.475  77.035  1.00 35.92  ? 260 VAL   A C     1 
ATOM   2038  O  O     . VAL   A 1  260 ? 34.869  79.593  76.751  1.00 38.35  ? 260 VAL   A O     1 
ATOM   2039  C  CB    . VAL   A 1  260 ? 33.211  79.808  74.591  1.00 24.86  ? 260 VAL   A CB    1 
ATOM   2040  C  CG1   . VAL   A 1  260 ? 33.672  78.419  74.262  1.00 22.66  ? 260 VAL   A CG1   1 
ATOM   2041  C  CG2   . VAL   A 1  260 ? 32.188  80.297  73.585  1.00 27.97  ? 260 VAL   A CG2   1 
ATOM   2042  N  N     . PRO   A 1  261 ? 33.269  78.983  78.213  1.00 30.18  ? 261 PRO   A N     1 
ATOM   2043  C  CA    . PRO   A 1  261 ? 34.274  78.482  79.167  1.00 33.80  ? 261 PRO   A CA    1 
ATOM   2044  C  C     . PRO   A 1  261 ? 35.120  77.341  78.609  1.00 37.98  ? 261 PRO   A C     1 
ATOM   2045  O  O     . PRO   A 1  261 ? 36.345  77.346  78.774  1.00 42.25  ? 261 PRO   A O     1 
ATOM   2046  C  CB    . PRO   A 1  261 ? 33.418  78.024  80.367  1.00 43.82  ? 261 PRO   A CB    1 
ATOM   2047  C  CG    . PRO   A 1  261 ? 32.052  78.568  80.149  1.00 37.97  ? 261 PRO   A CG    1 
ATOM   2048  C  CD    . PRO   A 1  261 ? 31.900  78.688  78.656  1.00 41.47  ? 261 PRO   A CD    1 
ATOM   2049  N  N     . TYR   A 1  262 ? 34.468  76.283  77.927  1.00 43.14  ? 262 TYR   A N     1 
ATOM   2050  C  CA    . TYR   A 1  262 ? 35.253  75.214  77.320  1.00 35.48  ? 262 TYR   A CA    1 
ATOM   2051  C  C     . TYR   A 1  262 ? 35.416  75.432  75.829  1.00 41.61  ? 262 TYR   A C     1 
ATOM   2052  O  O     . TYR   A 1  262 ? 34.508  75.920  75.160  1.00 40.72  ? 262 TYR   A O     1 
ATOM   2053  C  CB    . TYR   A 1  262 ? 34.589  73.869  77.546  1.00 44.49  ? 262 TYR   A CB    1 
ATOM   2054  C  CG    . TYR   A 1  262 ? 34.594  73.496  79.009  1.00 51.48  ? 262 TYR   A CG    1 
ATOM   2055  C  CD1   . TYR   A 1  262 ? 33.762  74.114  79.888  1.00 58.14  ? 262 TYR   A CD1   1 
ATOM   2056  C  CD2   . TYR   A 1  262 ? 35.459  72.551  79.491  1.00 66.96  ? 262 TYR   A CD2   1 
ATOM   2057  C  CE1   . TYR   A 1  262 ? 33.756  73.803  81.238  1.00 72.03  ? 262 TYR   A CE1   1 
ATOM   2058  C  CE2   . TYR   A 1  262 ? 35.504  72.195  80.845  1.00 78.25  ? 262 TYR   A CE2   1 
ATOM   2059  C  CZ    . TYR   A 1  262 ? 34.628  72.838  81.726  1.00 73.63  ? 262 TYR   A CZ    1 
ATOM   2060  O  OH    . TYR   A 1  262 ? 34.607  72.523  83.060  1.00 58.84  ? 262 TYR   A OH    1 
ATOM   2061  N  N     . PRO   A 1  263 ? 36.571  75.081  75.276  1.00 52.82  ? 263 PRO   A N     1 
ATOM   2062  C  CA    A PRO   A 1  263 ? 36.796  75.394  73.857  0.86 44.59  ? 263 PRO   A CA    1 
ATOM   2063  C  CA    B PRO   A 1  263 ? 36.817  75.370  73.855  0.14 44.56  ? 263 PRO   A CA    1 
ATOM   2064  C  C     . PRO   A 1  263 ? 35.939  74.566  72.913  1.00 37.36  ? 263 PRO   A C     1 
ATOM   2065  O  O     . PRO   A 1  263 ? 35.524  75.088  71.870  1.00 43.93  ? 263 PRO   A O     1 
ATOM   2066  C  CB    A PRO   A 1  263 ? 38.296  75.122  73.671  0.86 46.10  ? 263 PRO   A CB    1 
ATOM   2067  C  CB    B PRO   A 1  263 ? 38.302  75.022  73.689  0.14 46.09  ? 263 PRO   A CB    1 
ATOM   2068  C  CG    A PRO   A 1  263 ? 38.868  75.343  75.046  0.86 45.92  ? 263 PRO   A CG    1 
ATOM   2069  C  CG    B PRO   A 1  263 ? 38.540  73.955  74.709  0.14 47.49  ? 263 PRO   A CG    1 
ATOM   2070  C  CD    A PRO   A 1  263 ? 37.824  74.769  75.980  0.86 48.99  ? 263 PRO   A CD    1 
ATOM   2071  C  CD    B PRO   A 1  263 ? 37.677  74.330  75.894  0.14 47.92  ? 263 PRO   A CD    1 
ATOM   2072  N  N     . ARG   A 1  264 ? 35.638  73.302  73.246  1.00 44.29  ? 264 ARG   A N     1 
ATOM   2073  C  CA    . ARG   A 1  264 ? 34.808  72.485  72.349  1.00 47.01  ? 264 ARG   A CA    1 
ATOM   2074  C  C     . ARG   A 1  264 ? 33.322  72.817  72.459  1.00 39.09  ? 264 ARG   A C     1 
ATOM   2075  O  O     . ARG   A 1  264 ? 32.608  72.804  71.455  1.00 36.67  ? 264 ARG   A O     1 
ATOM   2076  C  CB    . ARG   A 1  264 ? 35.010  71.003  72.626  1.00 40.01  ? 264 ARG   A CB    1 
ATOM   2077  C  CG    . ARG   A 1  264 ? 36.364  70.491  72.223  1.00 35.67  ? 264 ARG   A CG    1 
ATOM   2078  C  CD    . ARG   A 1  264 ? 36.548  69.092  72.785  1.00 39.27  ? 264 ARG   A CD    1 
ATOM   2079  N  NE    . ARG   A 1  264 ? 35.638  68.143  72.157  1.00 39.25  ? 264 ARG   A NE    1 
ATOM   2080  C  CZ    . ARG   A 1  264 ? 35.727  67.768  70.890  1.00 37.22  ? 264 ARG   A CZ    1 
ATOM   2081  N  NH1   . ARG   A 1  264 ? 36.633  68.293  70.074  1.00 28.61  ? 264 ARG   A NH1   1 
ATOM   2082  N  NH2   . ARG   A 1  264 ? 34.894  66.839  70.430  1.00 35.01  ? 264 ARG   A NH2   1 
ATOM   2083  N  N     . ILE   A 1  265 ? 32.832  73.095  73.659  1.00 37.83  ? 265 ILE   A N     1 
ATOM   2084  C  CA    . ILE   A 1  265 ? 31.463  73.555  73.827  1.00 31.79  ? 265 ILE   A CA    1 
ATOM   2085  C  C     . ILE   A 1  265 ? 31.355  75.035  73.485  1.00 26.90  ? 265 ILE   A C     1 
ATOM   2086  O  O     . ILE   A 1  265 ? 31.134  75.863  74.372  1.00 37.41  ? 265 ILE   A O     1 
ATOM   2087  C  CB    . ILE   A 1  265 ? 31.003  73.305  75.269  1.00 35.34  ? 265 ILE   A CB    1 
ATOM   2088  C  CG1   . ILE   A 1  265 ? 31.733  72.092  75.847  1.00 37.46  ? 265 ILE   A CG1   1 
ATOM   2089  C  CG2   . ILE   A 1  265 ? 29.513  73.136  75.310  1.00 35.22  ? 265 ILE   A CG2   1 
ATOM   2090  C  CD1   . ILE   A 1  265 ? 31.527  70.812  75.074  1.00 39.12  ? 265 ILE   A CD1   1 
ATOM   2091  N  N     . HIS   A 1  266 ? 31.522  75.392  72.220  1.00 26.75  ? 266 HIS   A N     1 
ATOM   2092  C  CA    . HIS   A 1  266 ? 31.504  76.790  71.802  1.00 28.88  ? 266 HIS   A CA    1 
ATOM   2093  C  C     . HIS   A 1  266 ? 30.340  77.112  70.854  1.00 28.99  ? 266 HIS   A C     1 
ATOM   2094  O  O     . HIS   A 1  266 ? 30.460  77.945  69.943  1.00 27.90  ? 266 HIS   A O     1 
ATOM   2095  C  CB    . HIS   A 1  266 ? 32.841  77.153  71.169  1.00 31.45  ? 266 HIS   A CB    1 
ATOM   2096  C  CG    . HIS   A 1  266 ? 33.176  76.336  69.962  1.00 37.69  ? 266 HIS   A CG    1 
ATOM   2097  N  ND1   . HIS   A 1  266 ? 33.954  75.202  70.028  1.00 33.85  ? 266 HIS   A ND1   1 
ATOM   2098  C  CD2   . HIS   A 1  266 ? 32.834  76.485  68.658  1.00 35.45  ? 266 HIS   A CD2   1 
ATOM   2099  C  CE1   . HIS   A 1  266 ? 34.091  74.696  68.815  1.00 38.45  ? 266 HIS   A CE1   1 
ATOM   2100  N  NE2   . HIS   A 1  266 ? 33.424  75.457  67.965  1.00 39.74  ? 266 HIS   A NE2   1 
ATOM   2101  N  N     . PHE   A 1  267 ? 29.188  76.463  71.082  1.00 28.71  ? 267 PHE   A N     1 
ATOM   2102  C  CA    . PHE   A 1  267 ? 27.982  76.647  70.279  1.00 27.25  ? 267 PHE   A CA    1 
ATOM   2103  C  C     . PHE   A 1  267 ? 26.912  77.220  71.202  1.00 29.80  ? 267 PHE   A C     1 
ATOM   2104  O  O     . PHE   A 1  267 ? 26.112  76.477  71.802  1.00 33.06  ? 267 PHE   A O     1 
ATOM   2105  C  CB    . PHE   A 1  267 ? 27.538  75.340  69.622  1.00 23.46  ? 267 PHE   A CB    1 
ATOM   2106  C  CG    . PHE   A 1  267 ? 28.577  74.739  68.718  1.00 26.88  ? 267 PHE   A CG    1 
ATOM   2107  C  CD1   . PHE   A 1  267 ? 29.615  73.973  69.236  1.00 31.60  ? 267 PHE   A CD1   1 
ATOM   2108  C  CD2   . PHE   A 1  267 ? 28.528  74.942  67.353  1.00 23.16  ? 267 PHE   A CD2   1 
ATOM   2109  C  CE1   . PHE   A 1  267 ? 30.588  73.418  68.397  1.00 23.31  ? 267 PHE   A CE1   1 
ATOM   2110  C  CE2   . PHE   A 1  267 ? 29.475  74.399  66.526  1.00 17.67  ? 267 PHE   A CE2   1 
ATOM   2111  C  CZ    . PHE   A 1  267 ? 30.501  73.628  67.044  1.00 24.59  ? 267 PHE   A CZ    1 
ATOM   2112  N  N     . PRO   A 1  268 ? 26.895  78.539  71.367  1.00 22.37  ? 268 PRO   A N     1 
ATOM   2113  C  CA    . PRO   A 1  268 ? 25.821  79.175  72.132  1.00 24.81  ? 268 PRO   A CA    1 
ATOM   2114  C  C     . PRO   A 1  268 ? 24.508  79.186  71.356  1.00 20.70  ? 268 PRO   A C     1 
ATOM   2115  O  O     . PRO   A 1  268 ? 24.473  79.388  70.139  1.00 22.13  ? 268 PRO   A O     1 
ATOM   2116  C  CB    . PRO   A 1  268 ? 26.347  80.603  72.359  1.00 28.18  ? 268 PRO   A CB    1 
ATOM   2117  C  CG    . PRO   A 1  268 ? 27.804  80.561  71.988  1.00 23.78  ? 268 PRO   A CG    1 
ATOM   2118  C  CD    . PRO   A 1  268 ? 27.909  79.510  70.945  1.00 24.94  ? 268 PRO   A CD    1 
ATOM   2119  N  N     . LEU   A 1  269 ? 23.425  78.977  72.091  1.00 19.92  ? 269 LEU   A N     1 
ATOM   2120  C  CA    . LEU   A 1  269 ? 22.071  78.994  71.556  1.00 17.54  ? 269 LEU   A CA    1 
ATOM   2121  C  C     . LEU   A 1  269 ? 21.535  80.415  71.583  1.00 20.54  ? 269 LEU   A C     1 
ATOM   2122  O  O     . LEU   A 1  269 ? 21.537  81.076  72.630  1.00 22.41  ? 269 LEU   A O     1 
ATOM   2123  C  CB    . LEU   A 1  269 ? 21.177  78.067  72.379  1.00 14.54  ? 269 LEU   A CB    1 
ATOM   2124  C  CG    . LEU   A 1  269 ? 19.680  78.150  72.199  1.00 15.31  ? 269 LEU   A CG    1 
ATOM   2125  C  CD1   . LEU   A 1  269 ? 19.231  77.373  70.976  1.00 22.84  ? 269 LEU   A CD1   1 
ATOM   2126  C  CD2   . LEU   A 1  269 ? 19.060  77.567  73.410  1.00 16.77  ? 269 LEU   A CD2   1 
ATOM   2127  N  N     . ALA   A 1  270 ? 21.100  80.886  70.428  1.00 21.66  ? 270 ALA   A N     1 
ATOM   2128  C  CA    . ALA   A 1  270 ? 20.579  82.231  70.277  1.00 16.36  ? 270 ALA   A CA    1 
ATOM   2129  C  C     . ALA   A 1  270 ? 19.065  82.160  70.291  1.00 19.36  ? 270 ALA   A C     1 
ATOM   2130  O  O     . ALA   A 1  270 ? 18.472  81.253  69.700  1.00 21.88  ? 270 ALA   A O     1 
ATOM   2131  C  CB    . ALA   A 1  270 ? 21.064  82.876  68.979  1.00 20.90  ? 270 ALA   A CB    1 
ATOM   2132  N  N     . THR   A 1  271 ? 18.445  83.096  71.008  1.00 21.25  ? 271 THR   A N     1 
ATOM   2133  C  CA    . THR   A 1  271 ? 16.995  83.143  71.146  1.00 20.84  ? 271 THR   A CA    1 
ATOM   2134  C  C     . THR   A 1  271 ? 16.576  84.593  71.017  1.00 24.41  ? 271 THR   A C     1 
ATOM   2135  O  O     . THR   A 1  271 ? 17.194  85.464  71.635  1.00 26.81  ? 271 THR   A O     1 
ATOM   2136  C  CB    . THR   A 1  271 ? 16.511  82.575  72.482  1.00 18.27  ? 271 THR   A CB    1 
ATOM   2137  O  OG1   . THR   A 1  271 ? 17.118  81.296  72.731  1.00 25.96  ? 271 THR   A OG1   1 
ATOM   2138  C  CG2   . THR   A 1  271 ? 15.010  82.410  72.426  1.00 20.52  ? 271 THR   A CG2   1 
ATOM   2139  N  N     . TYR   A 1  272 ? 15.543  84.853  70.212  1.00 16.79  ? 272 TYR   A N     1 
ATOM   2140  C  CA    . TYR   A 1  272 ? 15.207  86.212  69.825  1.00 18.45  ? 272 TYR   A CA    1 
ATOM   2141  C  C     . TYR   A 1  272 ? 13.703  86.421  69.922  1.00 25.63  ? 272 TYR   A C     1 
ATOM   2142  O  O     . TYR   A 1  272 ? 12.916  85.483  69.765  1.00 25.07  ? 272 TYR   A O     1 
ATOM   2143  C  CB    . TYR   A 1  272 ? 15.713  86.484  68.407  1.00 20.73  ? 272 TYR   A CB    1 
ATOM   2144  C  CG    . TYR   A 1  272 ? 15.507  87.873  67.896  1.00 20.39  ? 272 TYR   A CG    1 
ATOM   2145  C  CD1   . TYR   A 1  272 ? 14.372  88.200  67.207  1.00 18.99  ? 272 TYR   A CD1   1 
ATOM   2146  C  CD2   . TYR   A 1  272 ? 16.460  88.853  68.084  1.00 24.57  ? 272 TYR   A CD2   1 
ATOM   2147  C  CE1   . TYR   A 1  272 ? 14.175  89.462  66.719  1.00 18.60  ? 272 TYR   A CE1   1 
ATOM   2148  C  CE2   . TYR   A 1  272 ? 16.267  90.137  67.589  1.00 24.71  ? 272 TYR   A CE2   1 
ATOM   2149  C  CZ    . TYR   A 1  272 ? 15.112  90.434  66.906  1.00 24.90  ? 272 TYR   A CZ    1 
ATOM   2150  O  OH    . TYR   A 1  272 ? 14.875  91.701  66.400  1.00 35.87  ? 272 TYR   A OH    1 
ATOM   2151  N  N     . ALA   A 1  273 ? 13.311  87.671  70.191  1.00 31.60  ? 273 ALA   A N     1 
ATOM   2152  C  CA    . ALA   A 1  273 ? 11.914  88.062  70.353  1.00 22.27  ? 273 ALA   A CA    1 
ATOM   2153  C  C     . ALA   A 1  273 ? 11.835  89.575  70.548  1.00 25.24  ? 273 ALA   A C     1 
ATOM   2154  O  O     . ALA   A 1  273 ? 12.783  90.177  71.075  1.00 28.77  ? 273 ALA   A O     1 
ATOM   2155  C  CB    . ALA   A 1  273 ? 11.292  87.306  71.524  1.00 15.44  ? 273 ALA   A CB    1 
ATOM   2156  N  N     . PRO   A 1  274 ? 10.735  90.236  70.137  1.00 27.49  ? 274 PRO   A N     1 
ATOM   2157  C  CA    . PRO   A 1  274 ? 9.515   89.698  69.518  1.00 31.65  ? 274 PRO   A CA    1 
ATOM   2158  C  C     . PRO   A 1  274 ? 9.638   89.557  67.993  1.00 27.47  ? 274 PRO   A C     1 
ATOM   2159  O  O     . PRO   A 1  274 ? 10.326  90.327  67.328  1.00 22.65  ? 274 PRO   A O     1 
ATOM   2160  C  CB    . PRO   A 1  274 ? 8.466   90.754  69.893  1.00 25.76  ? 274 PRO   A CB    1 
ATOM   2161  C  CG    . PRO   A 1  274 ? 9.239   92.034  69.759  1.00 25.90  ? 274 PRO   A CG    1 
ATOM   2162  C  CD    . PRO   A 1  274 ? 10.653  91.706  70.254  1.00 25.73  ? 274 PRO   A CD    1 
ATOM   2163  N  N     . VAL   A 1  275 ? 8.976   88.571  67.405  1.00 26.86  ? 275 VAL   A N     1 
ATOM   2164  C  CA    . VAL   A 1  275 ? 8.907   88.428  65.961  1.00 24.98  ? 275 VAL   A CA    1 
ATOM   2165  C  C     . VAL   A 1  275 ? 7.443   88.541  65.571  1.00 26.51  ? 275 VAL   A C     1 
ATOM   2166  O  O     . VAL   A 1  275 ? 6.672   87.587  65.753  1.00 26.30  ? 275 VAL   A O     1 
ATOM   2167  C  CB    . VAL   A 1  275 ? 9.510   87.107  65.481  1.00 22.35  ? 275 VAL   A CB    1 
ATOM   2168  C  CG1   . VAL   A 1  275 ? 8.998   86.774  64.108  1.00 24.55  ? 275 VAL   A CG1   1 
ATOM   2169  C  CG2   . VAL   A 1  275 ? 11.014  87.212  65.452  1.00 23.03  ? 275 VAL   A CG2   1 
ATOM   2170  N  N     . ILE   A 1  276 ? 7.073   89.701  65.010  1.00 26.77  ? 276 ILE   A N     1 
ATOM   2171  C  CA    . ILE   A 1  276 ? 5.702   90.091  64.688  1.00 31.61  ? 276 ILE   A CA    1 
ATOM   2172  C  C     . ILE   A 1  276 ? 5.551   90.360  63.189  1.00 26.09  ? 276 ILE   A C     1 
ATOM   2173  O  O     . ILE   A 1  276 ? 6.459   90.870  62.530  1.00 36.47  ? 276 ILE   A O     1 
ATOM   2174  C  CB    . ILE   A 1  276 ? 5.291   91.344  65.503  1.00 37.27  ? 276 ILE   A CB    1 
ATOM   2175  C  CG1   . ILE   A 1  276 ? 5.576   91.159  66.997  1.00 30.37  ? 276 ILE   A CG1   1 
ATOM   2176  C  CG2   . ILE   A 1  276 ? 3.836   91.697  65.272  1.00 43.54  ? 276 ILE   A CG2   1 
ATOM   2177  C  CD1   . ILE   A 1  276 ? 4.895   89.966  67.618  1.00 35.93  ? 276 ILE   A CD1   1 
ATOM   2178  N  N     . SER   A 1  277 ? 4.366   90.056  62.668  1.00 31.90  ? 277 SER   A N     1 
ATOM   2179  C  CA    . SER   A 1  277 ? 4.034   90.304  61.268  1.00 36.41  ? 277 SER   A CA    1 
ATOM   2180  C  C     . SER   A 1  277 ? 3.834   91.791  61.009  1.00 45.70  ? 277 SER   A C     1 
ATOM   2181  O  O     . SER   A 1  277 ? 3.013   92.431  61.669  1.00 53.42  ? 277 SER   A O     1 
ATOM   2182  C  CB    . SER   A 1  277 ? 2.758   89.545  60.902  1.00 32.16  ? 277 SER   A CB    1 
ATOM   2183  O  OG    . SER   A 1  277 ? 2.359   89.772  59.568  1.00 36.37  ? 277 SER   A OG    1 
ATOM   2184  N  N     . ALA   A 1  278 ? 4.557   92.350  60.031  1.00 41.66  ? 278 ALA   A N     1 
ATOM   2185  C  CA    . ALA   A 1  278 ? 4.328   93.760  59.714  1.00 47.05  ? 278 ALA   A CA    1 
ATOM   2186  C  C     . ALA   A 1  278 ? 2.865   94.014  59.376  1.00 53.93  ? 278 ALA   A C     1 
ATOM   2187  O  O     . ALA   A 1  278 ? 2.329   95.088  59.681  1.00 62.91  ? 278 ALA   A O     1 
ATOM   2188  C  CB    . ALA   A 1  278 ? 5.225   94.221  58.565  1.00 38.51  ? 278 ALA   A CB    1 
ATOM   2189  N  N     . GLU   A 1  279 ? 2.200   93.026  58.782  1.00 52.57  ? 279 GLU   A N     1 
ATOM   2190  C  CA    . GLU   A 1  279 ? 0.801   93.131  58.397  1.00 61.58  ? 279 GLU   A CA    1 
ATOM   2191  C  C     . GLU   A 1  279 ? -0.168  92.937  59.553  1.00 62.06  ? 279 GLU   A C     1 
ATOM   2192  O  O     . GLU   A 1  279 ? -1.378  93.047  59.336  1.00 68.59  ? 279 GLU   A O     1 
ATOM   2193  C  CB    . GLU   A 1  279 ? 0.482   92.104  57.313  1.00 58.53  ? 279 GLU   A CB    1 
ATOM   2194  C  CG    . GLU   A 1  279 ? 1.547   92.020  56.250  1.00 65.21  ? 279 GLU   A CG    1 
ATOM   2195  C  CD    . GLU   A 1  279 ? 0.972   91.881  54.863  1.00 75.84  ? 279 GLU   A CD    1 
ATOM   2196  O  OE1   . GLU   A 1  279 ? 0.750   92.928  54.213  1.00 83.39  ? 279 GLU   A OE1   1 
ATOM   2197  O  OE2   . GLU   A 1  279 ? 0.733   90.730  54.433  1.00 76.37  ? 279 GLU   A OE2   1 
ATOM   2198  N  N     . LYS   A 1  280 ? 0.310   92.619  60.752  1.00 63.04  ? 280 LYS   A N     1 
ATOM   2199  C  CA    . LYS   A 1  280 ? -0.597  92.456  61.879  1.00 59.11  ? 280 LYS   A CA    1 
ATOM   2200  C  C     . LYS   A 1  280 ? -1.372  93.749  62.059  1.00 65.87  ? 280 LYS   A C     1 
ATOM   2201  O  O     . LYS   A 1  280 ? -0.770  94.819  62.219  1.00 57.76  ? 280 LYS   A O     1 
ATOM   2202  C  CB    . LYS   A 1  280 ? 0.181   92.100  63.147  1.00 59.76  ? 280 LYS   A CB    1 
ATOM   2203  C  CG    . LYS   A 1  280 ? -0.661  91.916  64.396  1.00 63.80  ? 280 LYS   A CG    1 
ATOM   2204  C  CD    . LYS   A 1  280 ? -0.523  90.511  64.955  1.00 68.18  ? 280 LYS   A CD    1 
ATOM   2205  C  CE    . LYS   A 1  280 ? -1.359  90.318  66.210  1.00 65.14  ? 280 LYS   A CE    1 
ATOM   2206  N  NZ    . LYS   A 1  280 ? -1.070  89.014  66.868  1.00 62.74  ? 280 LYS   A NZ    1 
ATOM   2207  N  N     . ALA   A 1  281 ? -2.705  93.651  61.975  1.00 69.05  ? 281 ALA   A N     1 
ATOM   2208  C  CA    . ALA   A 1  281 ? -3.572  94.817  62.072  1.00 66.18  ? 281 ALA   A CA    1 
ATOM   2209  C  C     . ALA   A 1  281 ? -3.099  95.698  63.215  1.00 79.55  ? 281 ALA   A C     1 
ATOM   2210  O  O     . ALA   A 1  281 ? -2.545  96.783  62.992  1.00 87.90  ? 281 ALA   A O     1 
ATOM   2211  C  CB    . ALA   A 1  281 ? -5.026  94.400  62.273  1.00 65.88  ? 281 ALA   A CB    1 
ATOM   2212  N  N     . TYR   A 1  282 ? -3.283  95.222  64.443  1.00 71.51  ? 282 TYR   A N     1 
ATOM   2213  C  CA    . TYR   A 1  282 ? -2.697  95.865  65.605  1.00 77.93  ? 282 TYR   A CA    1 
ATOM   2214  C  C     . TYR   A 1  282 ? -2.020  94.806  66.459  1.00 74.21  ? 282 TYR   A C     1 
ATOM   2215  O  O     . TYR   A 1  282 ? -2.493  93.666  66.531  1.00 66.02  ? 282 TYR   A O     1 
ATOM   2216  C  CB    . TYR   A 1  282 ? -3.750  96.638  66.427  1.00 83.96  ? 282 TYR   A CB    1 
ATOM   2217  C  CG    . TYR   A 1  282 ? -3.203  97.160  67.737  1.00 84.71  ? 282 TYR   A CG    1 
ATOM   2218  C  CD1   . TYR   A 1  282 ? -2.302  98.207  67.764  1.00 81.72  ? 282 TYR   A CD1   1 
ATOM   2219  C  CD2   . TYR   A 1  282 ? -3.570  96.591  68.940  1.00 87.14  ? 282 TYR   A CD2   1 
ATOM   2220  C  CE1   . TYR   A 1  282 ? -1.775  98.689  68.958  1.00 80.51  ? 282 TYR   A CE1   1 
ATOM   2221  C  CE2   . TYR   A 1  282 ? -2.998  97.016  70.135  1.00 88.22  ? 282 TYR   A CE2   1 
ATOM   2222  C  CZ    . TYR   A 1  282 ? -2.148  98.110  70.151  1.00 78.93  ? 282 TYR   A CZ    1 
ATOM   2223  O  OH    . TYR   A 1  282 ? -1.645  98.560  71.357  1.00 80.77  ? 282 TYR   A OH    1 
ATOM   2224  N  N     . HIS   A 1  283 ? -0.900  95.188  67.087  1.00 78.27  ? 283 HIS   A N     1 
ATOM   2225  C  CA    . HIS   A 1  283 ? -0.234  94.369  68.096  1.00 68.57  ? 283 HIS   A CA    1 
ATOM   2226  C  C     . HIS   A 1  283 ? -0.016  95.197  69.349  1.00 68.89  ? 283 HIS   A C     1 
ATOM   2227  O  O     . HIS   A 1  283 ? 0.660   96.231  69.306  1.00 75.28  ? 283 HIS   A O     1 
ATOM   2228  C  CB    . HIS   A 1  283 ? 1.110   93.813  67.613  1.00 62.26  ? 283 HIS   A CB    1 
ATOM   2229  C  CG    . HIS   A 1  283 ? 1.407   92.449  68.156  1.00 69.06  ? 283 HIS   A CG    1 
ATOM   2230  N  ND1   . HIS   A 1  283 ? 0.854   91.300  67.624  1.00 67.29  ? 283 HIS   A ND1   1 
ATOM   2231  C  CD2   . HIS   A 1  283 ? 2.157   92.050  69.212  1.00 69.81  ? 283 HIS   A CD2   1 
ATOM   2232  C  CE1   . HIS   A 1  283 ? 1.267   90.252  68.314  1.00 63.08  ? 283 HIS   A CE1   1 
ATOM   2233  N  NE2   . HIS   A 1  283 ? 2.056   90.678  69.286  1.00 72.76  ? 283 HIS   A NE2   1 
ATOM   2234  N  N     . GLU   A 1  284 ? -0.578  94.735  70.460  1.00 69.79  ? 284 GLU   A N     1 
ATOM   2235  C  CA    . GLU   A 1  284 ? -0.232  95.291  71.761  1.00 70.11  ? 284 GLU   A CA    1 
ATOM   2236  C  C     . GLU   A 1  284 ? 1.262   95.086  72.009  1.00 71.13  ? 284 GLU   A C     1 
ATOM   2237  O  O     . GLU   A 1  284 ? 1.739   93.946  72.015  1.00 68.46  ? 284 GLU   A O     1 
ATOM   2238  C  CB    . GLU   A 1  284 ? -1.077  94.617  72.849  1.00 38.16  ? 284 GLU   A CB    1 
ATOM   2239  N  N     . GLN   A 1  285 ? 2.010   96.185  72.182  1.00 63.69  ? 285 GLN   A N     1 
ATOM   2240  C  CA    . GLN   A 1  285 ? 3.460   96.077  72.338  1.00 57.29  ? 285 GLN   A CA    1 
ATOM   2241  C  C     . GLN   A 1  285 ? 3.832   95.168  73.506  1.00 51.27  ? 285 GLN   A C     1 
ATOM   2242  O  O     . GLN   A 1  285 ? 3.200   95.183  74.568  1.00 54.04  ? 285 GLN   A O     1 
ATOM   2243  C  CB    . GLN   A 1  285 ? 4.100   97.458  72.534  1.00 59.26  ? 285 GLN   A CB    1 
ATOM   2244  C  CG    . GLN   A 1  285 ? 4.272   98.284  71.248  1.00 66.76  ? 285 GLN   A CG    1 
ATOM   2245  C  CD    . GLN   A 1  285 ? 5.133   97.604  70.173  1.00 59.65  ? 285 GLN   A CD    1 
ATOM   2246  O  OE1   . GLN   A 1  285 ? 5.061   97.967  69.003  1.00 56.26  ? 285 GLN   A OE1   1 
ATOM   2247  N  NE2   . GLN   A 1  285 ? 5.941   96.619  70.568  1.00 59.08  ? 285 GLN   A NE2   1 
ATOM   2248  N  N     . LEU   A 1  286 ? 4.877   94.376  73.299  1.00 46.15  ? 286 LEU   A N     1 
ATOM   2249  C  CA    . LEU   A 1  286 ? 5.391   93.513  74.349  1.00 47.06  ? 286 LEU   A CA    1 
ATOM   2250  C  C     . LEU   A 1  286 ? 6.334   94.281  75.279  1.00 42.44  ? 286 LEU   A C     1 
ATOM   2251  O  O     . LEU   A 1  286 ? 7.054   95.193  74.859  1.00 42.31  ? 286 LEU   A O     1 
ATOM   2252  C  CB    . LEU   A 1  286 ? 6.122   92.312  73.745  1.00 45.46  ? 286 LEU   A CB    1 
ATOM   2253  C  CG    . LEU   A 1  286 ? 5.328   91.333  72.887  1.00 35.45  ? 286 LEU   A CG    1 
ATOM   2254  C  CD1   . LEU   A 1  286 ? 4.074   90.898  73.612  1.00 36.01  ? 286 LEU   A CD1   1 
ATOM   2255  C  CD2   . LEU   A 1  286 ? 5.011   91.964  71.535  1.00 45.48  ? 286 LEU   A CD2   1 
ATOM   2256  N  N     . SER   A 1  287 ? 6.347   93.876  76.545  1.00 32.61  ? 287 SER   A N     1 
ATOM   2257  C  CA    . SER   A 1  287 ? 7.110   94.534  77.597  1.00 30.18  ? 287 SER   A CA    1 
ATOM   2258  C  C     . SER   A 1  287 ? 8.469   93.873  77.785  1.00 32.04  ? 287 SER   A C     1 
ATOM   2259  O  O     . SER   A 1  287 ? 8.717   92.770  77.304  1.00 36.44  ? 287 SER   A O     1 
ATOM   2260  C  CB    . SER   A 1  287 ? 6.333   94.480  78.905  1.00 36.04  ? 287 SER   A CB    1 
ATOM   2261  O  OG    . SER   A 1  287 ? 6.204   93.132  79.336  1.00 40.43  ? 287 SER   A OG    1 
ATOM   2262  N  N     . VAL   A 1  288 ? 9.349   94.546  78.533  1.00 31.97  ? 288 VAL   A N     1 
ATOM   2263  C  CA    . VAL   A 1  288 ? 10.641  93.945  78.875  1.00 28.11  ? 288 VAL   A CA    1 
ATOM   2264  C  C     . VAL   A 1  288 ? 10.432  92.597  79.556  1.00 33.15  ? 288 VAL   A C     1 
ATOM   2265  O  O     . VAL   A 1  288 ? 11.105  91.604  79.251  1.00 32.81  ? 288 VAL   A O     1 
ATOM   2266  C  CB    . VAL   A 1  288 ? 11.467  94.898  79.755  1.00 22.76  ? 288 VAL   A CB    1 
ATOM   2267  C  CG1   . VAL   A 1  288 ? 12.663  94.183  80.344  1.00 17.67  ? 288 VAL   A CG1   1 
ATOM   2268  C  CG2   . VAL   A 1  288 ? 11.893  96.087  78.948  1.00 30.94  ? 288 VAL   A CG2   1 
ATOM   2269  N  N     . ALA   A 1  289 ? 9.490   92.535  80.490  1.00 31.13  ? 289 ALA   A N     1 
ATOM   2270  C  CA    . ALA   A 1  289 ? 9.180   91.241  81.073  1.00 30.52  ? 289 ALA   A CA    1 
ATOM   2271  C  C     . ALA   A 1  289 ? 8.773   90.258  79.985  1.00 36.72  ? 289 ALA   A C     1 
ATOM   2272  O  O     . ALA   A 1  289 ? 9.327   89.161  79.892  1.00 43.88  ? 289 ALA   A O     1 
ATOM   2273  C  CB    . ALA   A 1  289 ? 8.088   91.377  82.126  1.00 24.41  ? 289 ALA   A CB    1 
ATOM   2274  N  N     . GLU   A 1  290 ? 7.839   90.654  79.119  1.00 31.39  ? 290 GLU   A N     1 
ATOM   2275  C  CA    . GLU   A 1  290 ? 7.273   89.700  78.165  1.00 37.20  ? 290 GLU   A CA    1 
ATOM   2276  C  C     . GLU   A 1  290 ? 8.306   89.219  77.143  1.00 31.55  ? 290 GLU   A C     1 
ATOM   2277  O  O     . GLU   A 1  290 ? 8.345   88.026  76.820  1.00 29.13  ? 290 GLU   A O     1 
ATOM   2278  C  CB    . GLU   A 1  290 ? 6.071   90.311  77.445  1.00 41.53  ? 290 GLU   A CB    1 
ATOM   2279  C  CG    . GLU   A 1  290 ? 4.944   90.802  78.334  1.00 39.37  ? 290 GLU   A CG    1 
ATOM   2280  C  CD    . GLU   A 1  290 ? 3.886   91.518  77.522  1.00 45.14  ? 290 GLU   A CD    1 
ATOM   2281  O  OE1   . GLU   A 1  290 ? 4.182   92.623  77.006  1.00 46.77  ? 290 GLU   A OE1   1 
ATOM   2282  O  OE2   . GLU   A 1  290 ? 2.775   90.961  77.374  1.00 46.05  ? 290 GLU   A OE2   1 
ATOM   2283  N  N     . ILE   A 1  291 ? 9.141   90.120  76.609  1.00 31.16  ? 291 ILE   A N     1 
ATOM   2284  C  CA    . ILE   A 1  291 ? 10.148  89.687  75.638  1.00 28.40  ? 291 ILE   A CA    1 
ATOM   2285  C  C     . ILE   A 1  291 ? 11.220  88.832  76.317  1.00 33.69  ? 291 ILE   A C     1 
ATOM   2286  O  O     . ILE   A 1  291 ? 11.679  87.824  75.759  1.00 31.87  ? 291 ILE   A O     1 
ATOM   2287  C  CB    . ILE   A 1  291 ? 10.779  90.885  74.899  1.00 22.95  ? 291 ILE   A CB    1 
ATOM   2288  C  CG1   . ILE   A 1  291 ? 11.649  91.731  75.834  1.00 25.34  ? 291 ILE   A CG1   1 
ATOM   2289  C  CG2   . ILE   A 1  291 ? 9.744   91.713  74.204  1.00 24.90  ? 291 ILE   A CG2   1 
ATOM   2290  C  CD1   . ILE   A 1  291 ? 12.392  92.856  75.123  1.00 28.53  ? 291 ILE   A CD1   1 
ATOM   2291  N  N     . THR   A 1  292 ? 11.627  89.206  77.531  1.00 28.87  ? 292 THR   A N     1 
ATOM   2292  C  CA    . THR   A 1  292 ? 12.673  88.443  78.199  1.00 26.75  ? 292 THR   A CA    1 
ATOM   2293  C  C     . THR   A 1  292 ? 12.200  87.036  78.539  1.00 34.34  ? 292 THR   A C     1 
ATOM   2294  O  O     . THR   A 1  292 ? 12.986  86.076  78.483  1.00 33.05  ? 292 THR   A O     1 
ATOM   2295  C  CB    . THR   A 1  292 ? 13.147  89.170  79.451  1.00 20.13  ? 292 THR   A CB    1 
ATOM   2296  O  OG1   . THR   A 1  292 ? 13.788  90.390  79.065  1.00 33.55  ? 292 THR   A OG1   1 
ATOM   2297  C  CG2   . THR   A 1  292 ? 14.139  88.335  80.177  1.00 14.12  ? 292 THR   A CG2   1 
ATOM   2298  N  N     . ASN   A 1  293 ? 10.924  86.883  78.900  1.00 33.65  ? 293 ASN   A N     1 
ATOM   2299  C  CA    . ASN   A 1  293 ? 10.429  85.545  79.180  1.00 33.15  ? 293 ASN   A CA    1 
ATOM   2300  C  C     . ASN   A 1  293 ? 10.450  84.702  77.910  1.00 36.56  ? 293 ASN   A C     1 
ATOM   2301  O  O     . ASN   A 1  293 ? 10.991  83.590  77.898  1.00 35.68  ? 293 ASN   A O     1 
ATOM   2302  C  CB    . ASN   A 1  293 ? 9.030   85.606  79.787  1.00 31.78  ? 293 ASN   A CB    1 
ATOM   2303  C  CG    . ASN   A 1  293 ? 8.644   84.305  80.469  1.00 38.47  ? 293 ASN   A CG    1 
ATOM   2304  O  OD1   . ASN   A 1  293 ? 9.480   83.642  81.085  1.00 39.01  ? 293 ASN   A OD1   1 
ATOM   2305  N  ND2   . ASN   A 1  293 ? 7.380   83.920  80.340  1.00 43.25  ? 293 ASN   A ND2   1 
ATOM   2306  N  N     . ALA   A 1  294 ? 9.910   85.247  76.815  1.00 29.18  ? 294 ALA   A N     1 
ATOM   2307  C  CA    . ALA   A 1  294 ? 9.949   84.622  75.499  1.00 23.11  ? 294 ALA   A CA    1 
ATOM   2308  C  C     . ALA   A 1  294 ? 11.289  83.941  75.242  1.00 31.29  ? 294 ALA   A C     1 
ATOM   2309  O  O     . ALA   A 1  294 ? 11.354  82.931  74.539  1.00 33.03  ? 294 ALA   A O     1 
ATOM   2310  C  CB    . ALA   A 1  294 ? 9.691   85.667  74.418  1.00 21.52  ? 294 ALA   A CB    1 
ATOM   2311  N  N     . CYS   A 1  295 ? 12.374  84.486  75.788  1.00 26.12  ? 295 CYS   A N     1 
ATOM   2312  C  CA    . CYS   A 1  295 ? 13.696  83.924  75.553  1.00 26.13  ? 295 CYS   A CA    1 
ATOM   2313  C  C     . CYS   A 1  295 ? 13.878  82.530  76.133  1.00 23.78  ? 295 CYS   A C     1 
ATOM   2314  O  O     . CYS   A 1  295 ? 14.895  81.888  75.847  1.00 29.60  ? 295 CYS   A O     1 
ATOM   2315  C  CB    . CYS   A 1  295 ? 14.774  84.850  76.128  1.00 30.48  ? 295 CYS   A CB    1 
ATOM   2316  S  SG    . CYS   A 1  295 ? 15.007  86.378  75.219  1.00 31.70  ? 295 CYS   A SG    1 
ATOM   2317  N  N     . PHE   A 1  296 ? 12.959  82.052  76.951  1.00 19.11  ? 296 PHE   A N     1 
ATOM   2318  C  CA    . PHE   A 1  296 ? 13.083  80.714  77.509  1.00 25.30  ? 296 PHE   A CA    1 
ATOM   2319  C  C     . PHE   A 1  296 ? 12.093  79.729  76.907  1.00 30.18  ? 296 PHE   A C     1 
ATOM   2320  O  O     . PHE   A 1  296 ? 12.104  78.559  77.281  1.00 27.39  ? 296 PHE   A O     1 
ATOM   2321  C  CB    . PHE   A 1  296 ? 12.968  80.775  79.037  1.00 24.76  ? 296 PHE   A CB    1 
ATOM   2322  C  CG    . PHE   A 1  296 ? 14.054  81.597  79.654  1.00 28.51  ? 296 PHE   A CG    1 
ATOM   2323  C  CD1   . PHE   A 1  296 ? 13.912  82.972  79.769  1.00 29.43  ? 296 PHE   A CD1   1 
ATOM   2324  C  CD2   . PHE   A 1  296 ? 15.266  81.015  80.028  1.00 30.91  ? 296 PHE   A CD2   1 
ATOM   2325  C  CE1   . PHE   A 1  296 ? 14.938  83.742  80.283  1.00 28.60  ? 296 PHE   A CE1   1 
ATOM   2326  C  CE2   . PHE   A 1  296 ? 16.298  81.785  80.555  1.00 26.50  ? 296 PHE   A CE2   1 
ATOM   2327  C  CZ    . PHE   A 1  296 ? 16.130  83.145  80.686  1.00 28.29  ? 296 PHE   A CZ    1 
ATOM   2328  N  N     . GLU   A 1  297 ? 11.282  80.166  75.948  1.00 32.03  ? 297 GLU   A N     1 
ATOM   2329  C  CA    . GLU   A 1  297 ? 10.388  79.305  75.195  1.00 30.90  ? 297 GLU   A CA    1 
ATOM   2330  C  C     . GLU   A 1  297 ? 11.135  78.680  74.019  1.00 37.53  ? 297 GLU   A C     1 
ATOM   2331  O  O     . GLU   A 1  297 ? 11.684  79.418  73.183  1.00 36.09  ? 297 GLU   A O     1 
ATOM   2332  C  CB    . GLU   A 1  297 ? 9.202   80.103  74.679  1.00 24.92  ? 297 GLU   A CB    1 
ATOM   2333  C  CG    . GLU   A 1  297 ? 8.158   80.376  75.720  1.00 42.27  ? 297 GLU   A CG    1 
ATOM   2334  C  CD    . GLU   A 1  297 ? 7.615   79.104  76.325  1.00 50.84  ? 297 GLU   A CD    1 
ATOM   2335  O  OE1   . GLU   A 1  297 ? 8.073   78.013  75.920  1.00 55.11  ? 297 GLU   A OE1   1 
ATOM   2336  O  OE2   . GLU   A 1  297 ? 6.732   79.194  77.205  1.00 62.80  ? 297 GLU   A OE2   1 
ATOM   2337  N  N     . PRO   A 1  298 ? 11.163  77.360  73.889  1.00 31.74  ? 298 PRO   A N     1 
ATOM   2338  C  CA    . PRO   A 1  298 ? 11.948  76.768  72.811  1.00 22.88  ? 298 PRO   A CA    1 
ATOM   2339  C  C     . PRO   A 1  298 ? 11.482  77.259  71.453  1.00 20.41  ? 298 PRO   A C     1 
ATOM   2340  O  O     . PRO   A 1  298 ? 12.259  77.200  70.498  1.00 27.85  ? 298 PRO   A O     1 
ATOM   2341  C  CB    . PRO   A 1  298 ? 11.723  75.258  73.006  1.00 31.92  ? 298 PRO   A CB    1 
ATOM   2342  C  CG    . PRO   A 1  298 ? 11.292  75.121  74.429  1.00 29.81  ? 298 PRO   A CG    1 
ATOM   2343  C  CD    . PRO   A 1  298 ? 10.423  76.332  74.633  1.00 31.76  ? 298 PRO   A CD    1 
ATOM   2344  N  N     . ALA   A 1  299 ? 10.253  77.762  71.346  1.00 19.67  ? 299 ALA   A N     1 
ATOM   2345  C  CA    . ALA   A 1  299 ? 9.705   78.148  70.045  1.00 20.99  ? 299 ALA   A CA    1 
ATOM   2346  C  C     . ALA   A 1  299 ? 10.235  79.484  69.536  1.00 23.16  ? 299 ALA   A C     1 
ATOM   2347  O  O     . ALA   A 1  299 ? 9.797   79.962  68.486  1.00 18.94  ? 299 ALA   A O     1 
ATOM   2348  C  CB    . ALA   A 1  299 ? 8.183   78.194  70.105  1.00 19.54  ? 299 ALA   A CB    1 
ATOM   2349  N  N     . ASN   A 1  300 ? 11.188  80.098  70.227  1.00 25.62  ? 300 ASN   A N     1 
ATOM   2350  C  CA    . ASN   A 1  300 ? 11.842  81.281  69.704  1.00 21.52  ? 300 ASN   A CA    1 
ATOM   2351  C  C     . ASN   A 1  300 ? 13.325  81.083  69.477  1.00 22.69  ? 300 ASN   A C     1 
ATOM   2352  O  O     . ASN   A 1  300 ? 13.996  82.028  69.052  1.00 30.03  ? 300 ASN   A O     1 
ATOM   2353  C  CB    . ASN   A 1  300 ? 11.636  82.455  70.660  1.00 24.30  ? 300 ASN   A CB    1 
ATOM   2354  C  CG    . ASN   A 1  300 ? 10.210  82.582  71.080  1.00 21.86  ? 300 ASN   A CG    1 
ATOM   2355  O  OD1   . ASN   A 1  300 ? 9.306   82.401  70.267  1.00 24.88  ? 300 ASN   A OD1   1 
ATOM   2356  N  ND2   . ASN   A 1  300 ? 9.986   82.888  72.338  1.00 25.26  ? 300 ASN   A ND2   1 
ATOM   2357  N  N     . GLN   A 1  301 ? 13.853  79.900  69.752  1.00 16.66  ? 301 GLN   A N     1 
ATOM   2358  C  CA    . GLN   A 1  301 ? 15.283  79.700  69.705  1.00 19.05  ? 301 GLN   A CA    1 
ATOM   2359  C  C     . GLN   A 1  301 ? 15.705  79.387  68.279  1.00 19.89  ? 301 GLN   A C     1 
ATOM   2360  O  O     . GLN   A 1  301 ? 14.912  78.897  67.475  1.00 25.63  ? 301 GLN   A O     1 
ATOM   2361  C  CB    . GLN   A 1  301 ? 15.694  78.570  70.655  1.00 23.18  ? 301 GLN   A CB    1 
ATOM   2362  C  CG    . GLN   A 1  301 ? 14.833  78.440  71.884  1.00 18.10  ? 301 GLN   A CG    1 
ATOM   2363  C  CD    . GLN   A 1  301 ? 15.253  77.270  72.768  1.00 23.27  ? 301 GLN   A CD    1 
ATOM   2364  O  OE1   . GLN   A 1  301 ? 15.617  76.214  72.281  1.00 28.48  ? 301 GLN   A OE1   1 
ATOM   2365  N  NE2   . GLN   A 1  301 ? 15.203  77.460  74.073  1.00 26.16  ? 301 GLN   A NE2   1 
ATOM   2366  N  N     . MET   A 1  302 ? 16.970  79.671  67.959  1.00 23.59  ? 302 MET   A N     1 
ATOM   2367  C  CA    . MET   A 1  302 ? 17.420  79.289  66.612  1.00 19.61  ? 302 MET   A CA    1 
ATOM   2368  C  C     . MET   A 1  302 ? 17.614  77.826  66.473  1.00 19.10  ? 302 MET   A C     1 
ATOM   2369  O  O     . MET   A 1  302 ? 18.111  77.405  65.443  1.00 20.81  ? 302 MET   A O     1 
ATOM   2370  C  CB    . MET   A 1  302 ? 18.726  79.985  66.239  1.00 22.62  ? 302 MET   A CB    1 
ATOM   2371  C  CG    . MET   A 1  302 ? 18.692  81.492  66.331  1.00 25.58  ? 302 MET   A CG    1 
ATOM   2372  S  SD    . MET   A 1  302 ? 17.118  82.170  65.801  1.00 43.66  ? 302 MET   A SD    1 
ATOM   2373  C  CE    . MET   A 1  302 ? 17.713  83.233  64.510  1.00 34.88  ? 302 MET   A CE    1 
ATOM   2374  N  N     . VAL   A 1  303 ? 17.234  77.036  67.469  1.00 19.14  ? 303 VAL   A N     1 
ATOM   2375  C  CA    . VAL   A 1  303 ? 17.476  75.599  67.493  1.00 24.79  ? 303 VAL   A CA    1 
ATOM   2376  C  C     . VAL   A 1  303 ? 16.428  75.019  68.428  1.00 25.13  ? 303 VAL   A C     1 
ATOM   2377  O  O     . VAL   A 1  303 ? 16.377  75.381  69.607  1.00 29.81  ? 303 VAL   A O     1 
ATOM   2378  C  CB    . VAL   A 1  303 ? 18.908  75.253  67.967  1.00 22.71  ? 303 VAL   A CB    1 
ATOM   2379  C  CG1   . VAL   A 1  303 ? 19.069  73.751  68.207  1.00 15.65  ? 303 VAL   A CG1   1 
ATOM   2380  C  CG2   . VAL   A 1  303 ? 19.922  75.741  66.976  1.00 18.33  ? 303 VAL   A CG2   1 
ATOM   2381  N  N     . LYS   A 1  304 ? 15.561  74.151  67.917  1.00 26.95  ? 304 LYS   A N     1 
ATOM   2382  C  CA    . LYS   A 1  304 ? 14.549  73.566  68.779  1.00 23.68  ? 304 LYS   A CA    1 
ATOM   2383  C  C     . LYS   A 1  304 ? 15.225  72.575  69.708  1.00 25.55  ? 304 LYS   A C     1 
ATOM   2384  O  O     . LYS   A 1  304 ? 15.847  71.609  69.254  1.00 33.90  ? 304 LYS   A O     1 
ATOM   2385  C  CB    . LYS   A 1  304 ? 13.474  72.888  67.952  1.00 22.86  ? 304 LYS   A CB    1 
ATOM   2386  C  CG    . LYS   A 1  304 ? 12.954  73.737  66.838  1.00 21.49  ? 304 LYS   A CG    1 
ATOM   2387  C  CD    . LYS   A 1  304 ? 11.467  73.489  66.637  1.00 21.44  ? 304 LYS   A CD    1 
ATOM   2388  C  CE    . LYS   A 1  304 ? 10.912  74.359  65.536  1.00 25.58  ? 304 LYS   A CE    1 
ATOM   2389  N  NZ    . LYS   A 1  304 ? 9.452   74.148  65.378  1.00 45.38  ? 304 LYS   A NZ    1 
ATOM   2390  N  N     . CYS   A 1  305 ? 15.133  72.825  71.003  1.00 23.07  ? 305 CYS   A N     1 
ATOM   2391  C  CA    . CYS   A 1  305 ? 15.723  71.930  71.988  1.00 23.81  ? 305 CYS   A CA    1 
ATOM   2392  C  C     . CYS   A 1  305 ? 15.263  72.415  73.348  1.00 25.58  ? 305 CYS   A C     1 
ATOM   2393  O  O     . CYS   A 1  305 ? 14.762  73.530  73.487  1.00 22.76  ? 305 CYS   A O     1 
ATOM   2394  C  CB    . CYS   A 1  305 ? 17.248  71.906  71.889  1.00 27.70  ? 305 CYS   A CB    1 
ATOM   2395  S  SG    . CYS   A 1  305 ? 18.064  73.485  72.271  1.00 26.29  ? 305 CYS   A SG    1 
ATOM   2396  N  N     . ASP   A 1  306 ? 15.442  71.573  74.352  1.00 28.08  ? 306 ASP   A N     1 
ATOM   2397  C  CA    . ASP   A 1  306 ? 14.888  71.873  75.667  1.00 30.32  ? 306 ASP   A CA    1 
ATOM   2398  C  C     . ASP   A 1  306 ? 16.017  72.211  76.619  1.00 25.02  ? 306 ASP   A C     1 
ATOM   2399  O  O     . ASP   A 1  306 ? 16.699  71.301  77.115  1.00 32.91  ? 306 ASP   A O     1 
ATOM   2400  C  CB    . ASP   A 1  306 ? 14.068  70.689  76.199  1.00 25.95  ? 306 ASP   A CB    1 
ATOM   2401  C  CG    . ASP   A 1  306 ? 13.021  71.115  77.205  1.00 28.31  ? 306 ASP   A CG    1 
ATOM   2402  O  OD1   . ASP   A 1  306 ? 13.168  72.197  77.820  1.00 30.52  ? 306 ASP   A OD1   1 
ATOM   2403  O  OD2   . ASP   A 1  306 ? 12.041  70.372  77.384  1.00 28.33  ? 306 ASP   A OD2   1 
ATOM   2404  N  N     . PRO   A 1  307 ? 16.259  73.494  76.908  1.00 24.89  ? 307 PRO   A N     1 
ATOM   2405  C  CA    . PRO   A 1  307 ? 17.285  73.845  77.902  1.00 27.67  ? 307 PRO   A CA    1 
ATOM   2406  C  C     . PRO   A 1  307 ? 16.919  73.492  79.346  1.00 24.99  ? 307 PRO   A C     1 
ATOM   2407  O  O     . PRO   A 1  307 ? 17.770  73.660  80.227  1.00 35.05  ? 307 PRO   A O     1 
ATOM   2408  C  CB    . PRO   A 1  307 ? 17.446  75.368  77.728  1.00 17.79  ? 307 PRO   A CB    1 
ATOM   2409  C  CG    . PRO   A 1  307 ? 16.853  75.695  76.471  1.00 21.23  ? 307 PRO   A CG    1 
ATOM   2410  C  CD    . PRO   A 1  307 ? 15.731  74.695  76.246  1.00 28.54  ? 307 PRO   A CD    1 
ATOM   2411  N  N     . ARG   A 1  308 ? 15.698  73.038  79.636  1.00 25.82  ? 308 ARG   A N     1 
ATOM   2412  C  CA    . ARG   A 1  308 ? 15.434  72.599  81.000  1.00 31.88  ? 308 ARG   A CA    1 
ATOM   2413  C  C     . ARG   A 1  308 ? 16.184  71.322  81.307  1.00 38.12  ? 308 ARG   A C     1 
ATOM   2414  O  O     . ARG   A 1  308 ? 16.403  71.001  82.476  1.00 44.25  ? 308 ARG   A O     1 
ATOM   2415  C  CB    . ARG   A 1  308 ? 13.948  72.363  81.247  1.00 24.20  ? 308 ARG   A CB    1 
ATOM   2416  C  CG    . ARG   A 1  308 ? 13.055  73.552  81.077  1.00 21.83  ? 308 ARG   A CG    1 
ATOM   2417  C  CD    . ARG   A 1  308 ? 11.596  73.103  81.140  1.00 22.36  ? 308 ARG   A CD    1 
ATOM   2418  N  NE    . ARG   A 1  308 ? 11.320  72.169  80.059  1.00 26.48  ? 308 ARG   A NE    1 
ATOM   2419  C  CZ    . ARG   A 1  308 ? 10.152  71.589  79.838  1.00 24.77  ? 308 ARG   A CZ    1 
ATOM   2420  N  NH1   . ARG   A 1  308 ? 9.116   71.807  80.621  1.00 22.82  ? 308 ARG   A NH1   1 
ATOM   2421  N  NH2   . ARG   A 1  308 ? 10.023  70.767  78.802  1.00 23.55  ? 308 ARG   A NH2   1 
ATOM   2422  N  N     . HIS   A 1  309 ? 16.572  70.584  80.281  1.00 30.68  ? 309 HIS   A N     1 
ATOM   2423  C  CA    . HIS   A 1  309 ? 17.252  69.317  80.451  1.00 31.05  ? 309 HIS   A CA    1 
ATOM   2424  C  C     . HIS   A 1  309 ? 18.674  69.535  79.944  1.00 40.80  ? 309 HIS   A C     1 
ATOM   2425  O  O     . HIS   A 1  309 ? 19.028  69.208  78.810  1.00 48.36  ? 309 HIS   A O     1 
ATOM   2426  C  CB    . HIS   A 1  309 ? 16.502  68.231  79.735  1.00 30.19  ? 309 HIS   A CB    1 
ATOM   2427  C  CG    . HIS   A 1  309 ? 15.099  68.057  80.230  1.00 34.24  ? 309 HIS   A CG    1 
ATOM   2428  N  ND1   . HIS   A 1  309 ? 14.010  68.647  79.621  1.00 34.49  ? 309 HIS   A ND1   1 
ATOM   2429  C  CD2   . HIS   A 1  309 ? 14.610  67.381  81.298  1.00 36.26  ? 309 HIS   A CD2   1 
ATOM   2430  C  CE1   . HIS   A 1  309 ? 12.910  68.326  80.280  1.00 28.71  ? 309 HIS   A CE1   1 
ATOM   2431  N  NE2   . HIS   A 1  309 ? 13.247  67.567  81.308  1.00 33.21  ? 309 HIS   A NE2   1 
ATOM   2432  N  N     . GLY   A 1  310 ? 19.482  70.104  80.817  1.00 42.63  ? 310 GLY   A N     1 
ATOM   2433  C  CA    . GLY   A 1  310 ? 20.762  70.687  80.473  1.00 33.55  ? 310 GLY   A CA    1 
ATOM   2434  C  C     . GLY   A 1  310 ? 21.075  71.823  81.422  1.00 35.53  ? 310 GLY   A C     1 
ATOM   2435  O  O     . GLY   A 1  310 ? 20.208  72.370  82.098  1.00 38.85  ? 310 GLY   A O     1 
ATOM   2436  N  N     . LYS   A 1  311 ? 22.347  72.162  81.484  1.00 36.49  ? 311 LYS   A N     1 
ATOM   2437  C  CA    . LYS   A 1  311 ? 22.804  73.207  82.370  1.00 25.45  ? 311 LYS   A CA    1 
ATOM   2438  C  C     . LYS   A 1  311 ? 23.348  74.348  81.531  1.00 29.92  ? 311 LYS   A C     1 
ATOM   2439  O  O     . LYS   A 1  311 ? 23.609  74.190  80.336  1.00 31.87  ? 311 LYS   A O     1 
ATOM   2440  C  CB    . LYS   A 1  311 ? 23.852  72.663  83.339  1.00 33.61  ? 311 LYS   A CB    1 
ATOM   2441  C  CG    . LYS   A 1  311 ? 23.301  71.538  84.243  1.00 42.14  ? 311 LYS   A CG    1 
ATOM   2442  C  CD    . LYS   A 1  311 ? 24.182  71.263  85.466  1.00 47.77  ? 311 LYS   A CD    1 
ATOM   2443  C  CE    . LYS   A 1  311 ? 24.627  69.805  85.551  1.00 57.26  ? 311 LYS   A CE    1 
ATOM   2444  N  NZ    . LYS   A 1  311 ? 25.837  69.571  86.408  1.00 52.40  ? 311 LYS   A NZ    1 
ATOM   2445  N  N     . TYR   A 1  312 ? 23.473  75.515  82.156  1.00 35.14  ? 312 TYR   A N     1 
ATOM   2446  C  CA    . TYR   A 1  312 ? 24.021  76.705  81.519  1.00 30.81  ? 312 TYR   A CA    1 
ATOM   2447  C  C     . TYR   A 1  312 ? 25.455  76.931  81.971  1.00 27.05  ? 312 TYR   A C     1 
ATOM   2448  O  O     . TYR   A 1  312 ? 25.856  76.533  83.064  1.00 31.22  ? 312 TYR   A O     1 
ATOM   2449  C  CB    . TYR   A 1  312 ? 23.208  77.955  81.850  1.00 23.53  ? 312 TYR   A CB    1 
ATOM   2450  C  CG    . TYR   A 1  312 ? 21.848  78.061  81.217  1.00 29.39  ? 312 TYR   A CG    1 
ATOM   2451  C  CD1   . TYR   A 1  312 ? 20.788  77.314  81.678  1.00 29.16  ? 312 TYR   A CD1   1 
ATOM   2452  C  CD2   . TYR   A 1  312 ? 21.614  78.963  80.181  1.00 32.27  ? 312 TYR   A CD2   1 
ATOM   2453  C  CE1   . TYR   A 1  312 ? 19.531  77.426  81.097  1.00 30.05  ? 312 TYR   A CE1   1 
ATOM   2454  C  CE2   . TYR   A 1  312 ? 20.368  79.095  79.607  1.00 27.47  ? 312 TYR   A CE2   1 
ATOM   2455  C  CZ    . TYR   A 1  312 ? 19.326  78.323  80.068  1.00 32.80  ? 312 TYR   A CZ    1 
ATOM   2456  O  OH    . TYR   A 1  312 ? 18.077  78.448  79.485  1.00 42.50  ? 312 TYR   A OH    1 
ATOM   2457  N  N     . MET   A 1  313 ? 26.217  77.581  81.108  1.00 27.74  ? 313 MET   A N     1 
ATOM   2458  C  CA    . MET   A 1  313 ? 27.577  77.991  81.396  1.00 27.26  ? 313 MET   A CA    1 
ATOM   2459  C  C     . MET   A 1  313 ? 27.780  79.458  81.069  1.00 30.84  ? 313 MET   A C     1 
ATOM   2460  O  O     . MET   A 1  313 ? 28.906  79.955  81.170  1.00 34.18  ? 313 MET   A O     1 
ATOM   2461  C  CB    . MET   A 1  313 ? 28.588  77.159  80.593  1.00 33.33  ? 313 MET   A CB    1 
ATOM   2462  C  CG    . MET   A 1  313 ? 28.475  75.656  80.726  1.00 29.89  ? 313 MET   A CG    1 
ATOM   2463  S  SD    . MET   A 1  313 ? 29.296  74.896  79.299  1.00 36.01  ? 313 MET   A SD    1 
ATOM   2464  C  CE    . MET   A 1  313 ? 27.907  74.650  78.208  1.00 26.30  ? 313 MET   A CE    1 
ATOM   2465  N  N     . ALA   A 1  314 ? 26.732  80.149  80.639  1.00 28.93  ? 314 ALA   A N     1 
ATOM   2466  C  CA    . ALA   A 1  314 ? 26.795  81.563  80.320  1.00 32.73  ? 314 ALA   A CA    1 
ATOM   2467  C  C     . ALA   A 1  314 ? 25.436  81.997  79.784  1.00 35.61  ? 314 ALA   A C     1 
ATOM   2468  O  O     . ALA   A 1  314 ? 24.617  81.174  79.362  1.00 34.78  ? 314 ALA   A O     1 
ATOM   2469  C  CB    . ALA   A 1  314 ? 27.903  81.875  79.307  1.00 23.69  ? 314 ALA   A CB    1 
ATOM   2470  N  N     . CYS   A 1  315 ? 25.194  83.302  79.852  1.00 34.49  ? 315 CYS   A N     1 
ATOM   2471  C  CA    A CYS   A 1  315 ? 23.968  83.891  79.332  0.64 28.74  ? 315 CYS   A CA    1 
ATOM   2472  C  CA    B CYS   A 1  315 ? 23.967  83.897  79.342  0.36 28.81  ? 315 CYS   A CA    1 
ATOM   2473  C  C     . CYS   A 1  315 ? 24.243  85.360  79.053  1.00 30.55  ? 315 CYS   A C     1 
ATOM   2474  O  O     . CYS   A 1  315 ? 24.925  86.025  79.837  1.00 37.27  ? 315 CYS   A O     1 
ATOM   2475  C  CB    A CYS   A 1  315 ? 22.811  83.725  80.328  0.64 29.95  ? 315 CYS   A CB    1 
ATOM   2476  C  CB    B CYS   A 1  315 ? 22.820  83.765  80.346  0.36 30.01  ? 315 CYS   A CB    1 
ATOM   2477  S  SG    A CYS   A 1  315 ? 21.186  83.248  79.624  0.64 38.38  ? 315 CYS   A SG    1 
ATOM   2478  S  SG    B CYS   A 1  315 ? 21.925  82.197  80.289  0.36 34.87  ? 315 CYS   A SG    1 
ATOM   2479  N  N     . CYS   A 1  316 ? 23.738  85.854  77.934  1.00 27.68  ? 316 CYS   A N     1 
ATOM   2480  C  CA    A CYS   A 1  316 ? 23.818  87.267  77.604  0.69 25.60  ? 316 CYS   A CA    1 
ATOM   2481  C  CA    B CYS   A 1  316 ? 23.820  87.266  77.611  0.31 25.29  ? 316 CYS   A CA    1 
ATOM   2482  C  C     . CYS   A 1  316 ? 22.473  87.733  77.088  1.00 28.94  ? 316 CYS   A C     1 
ATOM   2483  O  O     . CYS   A 1  316 ? 21.818  87.034  76.308  1.00 32.53  ? 316 CYS   A O     1 
ATOM   2484  C  CB    A CYS   A 1  316 ? 24.873  87.546  76.563  0.69 25.83  ? 316 CYS   A CB    1 
ATOM   2485  C  CB    B CYS   A 1  316 ? 24.910  87.544  76.587  0.31 25.88  ? 316 CYS   A CB    1 
ATOM   2486  S  SG    A CYS   A 1  316 ? 26.533  87.375  77.163  0.69 29.15  ? 316 CYS   A SG    1 
ATOM   2487  S  SG    B CYS   A 1  316 ? 25.272  89.290  76.384  0.31 29.91  ? 316 CYS   A SG    1 
ATOM   2488  N  N     . LEU   A 1  317 ? 22.062  88.905  77.529  1.00 29.71  ? 317 LEU   A N     1 
ATOM   2489  C  CA    . LEU   A 1  317 ? 20.834  89.515  77.058  1.00 22.95  ? 317 LEU   A CA    1 
ATOM   2490  C  C     . LEU   A 1  317 ? 21.209  90.769  76.275  1.00 25.60  ? 317 LEU   A C     1 
ATOM   2491  O  O     . LEU   A 1  317 ? 21.859  91.675  76.810  1.00 24.47  ? 317 LEU   A O     1 
ATOM   2492  C  CB    . LEU   A 1  317 ? 19.897  89.808  78.228  1.00 20.24  ? 317 LEU   A CB    1 
ATOM   2493  C  CG    . LEU   A 1  317 ? 19.305  88.513  78.792  1.00 32.30  ? 317 LEU   A CG    1 
ATOM   2494  C  CD1   . LEU   A 1  317 ? 18.895  88.708  80.233  1.00 33.54  ? 317 LEU   A CD1   1 
ATOM   2495  C  CD2   . LEU   A 1  317 ? 18.111  87.988  77.944  1.00 22.60  ? 317 LEU   A CD2   1 
ATOM   2496  N  N     . LEU   A 1  318 ? 20.830  90.798  75.002  1.00 24.22  ? 318 LEU   A N     1 
ATOM   2497  C  CA    . LEU   A 1  318 ? 21.137  91.911  74.113  1.00 25.12  ? 318 LEU   A CA    1 
ATOM   2498  C  C     . LEU   A 1  318 ? 19.814  92.569  73.768  1.00 24.80  ? 318 LEU   A C     1 
ATOM   2499  O  O     . LEU   A 1  318 ? 19.074  92.065  72.918  1.00 30.93  ? 318 LEU   A O     1 
ATOM   2500  C  CB    . LEU   A 1  318 ? 21.884  91.437  72.865  1.00 25.43  ? 318 LEU   A CB    1 
ATOM   2501  C  CG    . LEU   A 1  318 ? 23.144  90.617  73.168  1.00 26.98  ? 318 LEU   A CG    1 
ATOM   2502  C  CD1   . LEU   A 1  318 ? 23.911  90.280  71.903  1.00 21.76  ? 318 LEU   A CD1   1 
ATOM   2503  C  CD2   . LEU   A 1  318 ? 24.023  91.333  74.198  1.00 20.71  ? 318 LEU   A CD2   1 
ATOM   2504  N  N     . TYR   A 1  319 ? 19.521  93.692  74.429  1.00 21.07  ? 319 TYR   A N     1 
ATOM   2505  C  CA    . TYR   A 1  319 ? 18.279  94.417  74.197  1.00 22.49  ? 319 TYR   A CA    1 
ATOM   2506  C  C     . TYR   A 1  319 ? 18.507  95.530  73.196  1.00 22.80  ? 319 TYR   A C     1 
ATOM   2507  O  O     . TYR   A 1  319 ? 19.527  96.212  73.226  1.00 28.17  ? 319 TYR   A O     1 
ATOM   2508  C  CB    . TYR   A 1  319 ? 17.728  95.022  75.486  1.00 22.49  ? 319 TYR   A CB    1 
ATOM   2509  C  CG    . TYR   A 1  319 ? 17.278  94.015  76.512  1.00 22.08  ? 319 TYR   A CG    1 
ATOM   2510  C  CD1   . TYR   A 1  319 ? 15.980  93.533  76.510  1.00 18.84  ? 319 TYR   A CD1   1 
ATOM   2511  C  CD2   . TYR   A 1  319 ? 18.168  93.541  77.489  1.00 21.52  ? 319 TYR   A CD2   1 
ATOM   2512  C  CE1   . TYR   A 1  319 ? 15.571  92.610  77.456  1.00 24.95  ? 319 TYR   A CE1   1 
ATOM   2513  C  CE2   . TYR   A 1  319 ? 17.778  92.620  78.427  1.00 21.09  ? 319 TYR   A CE2   1 
ATOM   2514  C  CZ    . TYR   A 1  319 ? 16.476  92.159  78.414  1.00 26.35  ? 319 TYR   A CZ    1 
ATOM   2515  O  OH    . TYR   A 1  319 ? 16.080  91.246  79.355  1.00 19.92  ? 319 TYR   A OH    1 
ATOM   2516  N  N     . ARG   A 1  320 ? 17.552  95.702  72.297  1.00 27.47  ? 320 ARG   A N     1 
ATOM   2517  C  CA    . ARG   A 1  320 ? 17.564  96.816  71.362  1.00 32.28  ? 320 ARG   A CA    1 
ATOM   2518  C  C     . ARG   A 1  320 ? 16.243  97.535  71.501  1.00 36.40  ? 320 ARG   A C     1 
ATOM   2519  O  O     . ARG   A 1  320 ? 15.183  96.921  71.327  1.00 29.81  ? 320 ARG   A O     1 
ATOM   2520  C  CB    . ARG   A 1  320 ? 17.759  96.366  69.918  1.00 28.16  ? 320 ARG   A CB    1 
ATOM   2521  C  CG    . ARG   A 1  320 ? 19.111  95.815  69.654  1.00 31.72  ? 320 ARG   A CG    1 
ATOM   2522  C  CD    . ARG   A 1  320 ? 19.193  95.305  68.226  1.00 37.10  ? 320 ARG   A CD    1 
ATOM   2523  N  NE    . ARG   A 1  320 ? 19.650  96.350  67.319  1.00 24.10  ? 320 ARG   A NE    1 
ATOM   2524  C  CZ    . ARG   A 1  320 ? 20.482  96.139  66.314  1.00 27.08  ? 320 ARG   A CZ    1 
ATOM   2525  N  NH1   . ARG   A 1  320 ? 20.933  94.927  66.036  1.00 31.63  ? 320 ARG   A NH1   1 
ATOM   2526  N  NH2   . ARG   A 1  320 ? 20.877  97.170  65.573  1.00 32.00  ? 320 ARG   A NH2   1 
ATOM   2527  N  N     . GLY   A 1  321 ? 16.316  98.830  71.814  1.00 32.75  ? 321 GLY   A N     1 
ATOM   2528  C  CA    . GLY   A 1  321 ? 15.145  99.670  71.910  1.00 35.48  ? 321 GLY   A CA    1 
ATOM   2529  C  C     . GLY   A 1  321 ? 15.034  100.286 73.297  1.00 38.57  ? 321 GLY   A C     1 
ATOM   2530  O  O     . GLY   A 1  321 ? 16.001  100.764 73.856  1.00 39.35  ? 321 GLY   A O     1 
ATOM   2531  N  N     . ASP   A 1  322 ? 13.808  100.250 73.823  1.00 38.45  ? 322 ASP   A N     1 
ATOM   2532  C  CA    . ASP   A 1  322 ? 13.433  101.072 74.970  1.00 34.04  ? 322 ASP   A CA    1 
ATOM   2533  C  C     . ASP   A 1  322 ? 13.514  100.204 76.220  1.00 32.23  ? 322 ASP   A C     1 
ATOM   2534  O  O     . ASP   A 1  322 ? 12.516  99.682  76.727  1.00 31.53  ? 322 ASP   A O     1 
ATOM   2535  C  CB    . ASP   A 1  322 ? 12.042  101.657 74.736  1.00 32.27  ? 322 ASP   A CB    1 
ATOM   2536  C  CG    . ASP   A 1  322 ? 11.443  102.223 75.968  1.00 40.19  ? 322 ASP   A CG    1 
ATOM   2537  O  OD1   . ASP   A 1  322 ? 12.075  103.138 76.536  1.00 43.51  ? 322 ASP   A OD1   1 
ATOM   2538  O  OD2   . ASP   A 1  322 ? 10.349  101.755 76.363  1.00 43.51  ? 322 ASP   A OD2   1 
ATOM   2539  N  N     . VAL   A 1  323 ? 14.733  100.021 76.708  1.00 26.57  ? 323 VAL   A N     1 
ATOM   2540  C  CA    . VAL   A 1  323 ? 14.917  99.149  77.856  1.00 29.49  ? 323 VAL   A CA    1 
ATOM   2541  C  C     . VAL   A 1  323 ? 15.796  99.843  78.883  1.00 31.74  ? 323 VAL   A C     1 
ATOM   2542  O  O     . VAL   A 1  323 ? 16.675  100.642 78.550  1.00 32.72  ? 323 VAL   A O     1 
ATOM   2543  C  CB    . VAL   A 1  323 ? 15.509  97.783  77.456  1.00 26.95  ? 323 VAL   A CB    1 
ATOM   2544  C  CG1   . VAL   A 1  323 ? 15.648  96.883  78.680  1.00 17.20  ? 323 VAL   A CG1   1 
ATOM   2545  C  CG2   . VAL   A 1  323 ? 14.651  97.128  76.372  1.00 21.50  ? 323 VAL   A CG2   1 
ATOM   2546  N  N     . VAL   A 1  324 ? 15.525  99.549  80.153  1.00 41.15  ? 324 VAL   A N     1 
ATOM   2547  C  CA    . VAL   A 1  324 ? 16.330  100.064 81.264  1.00 37.06  ? 324 VAL   A CA    1 
ATOM   2548  C  C     . VAL   A 1  324 ? 16.490  98.965  82.301  1.00 35.68  ? 324 VAL   A C     1 
ATOM   2549  O  O     . VAL   A 1  324 ? 15.591  98.164  82.528  1.00 32.32  ? 324 VAL   A O     1 
ATOM   2550  C  CB    . VAL   A 1  324 ? 15.685  101.289 81.930  1.00 34.69  ? 324 VAL   A CB    1 
ATOM   2551  C  CG1   . VAL   A 1  324 ? 15.754  102.465 81.000  1.00 30.62  ? 324 VAL   A CG1   1 
ATOM   2552  C  CG2   . VAL   A 1  324 ? 14.234  100.957 82.377  1.00 33.37  ? 324 VAL   A CG2   1 
ATOM   2553  N  N     . PRO   A 1  325 ? 17.650  98.967  82.971  1.00 33.29  ? 325 PRO   A N     1 
ATOM   2554  C  CA    . PRO   A 1  325 ? 17.985  97.823  83.841  1.00 28.63  ? 325 PRO   A CA    1 
ATOM   2555  C  C     . PRO   A 1  325 ? 16.900  97.479  84.841  1.00 34.89  ? 325 PRO   A C     1 
ATOM   2556  O  O     . PRO   A 1  325 ? 16.607  96.292  85.023  1.00 38.61  ? 325 PRO   A O     1 
ATOM   2557  C  CB    . PRO   A 1  325 ? 19.287  98.282  84.504  1.00 28.85  ? 325 PRO   A CB    1 
ATOM   2558  C  CG    . PRO   A 1  325 ? 19.927  99.174  83.454  1.00 34.79  ? 325 PRO   A CG    1 
ATOM   2559  C  CD    . PRO   A 1  325 ? 18.754  99.930  82.859  1.00 32.62  ? 325 PRO   A CD    1 
ATOM   2560  N  N     . LYS   A 1  326 ? 16.275  98.478  85.471  1.00 38.95  ? 326 LYS   A N     1 
ATOM   2561  C  CA    . LYS   A 1  326 ? 15.213  98.234  86.443  1.00 37.49  ? 326 LYS   A CA    1 
ATOM   2562  C  C     . LYS   A 1  326 ? 14.235  97.158  85.967  1.00 38.28  ? 326 LYS   A C     1 
ATOM   2563  O  O     . LYS   A 1  326 ? 13.986  96.166  86.666  1.00 37.28  ? 326 LYS   A O     1 
ATOM   2564  C  CB    . LYS   A 1  326 ? 14.482  99.552  86.738  1.00 44.12  ? 326 LYS   A CB    1 
ATOM   2565  C  CG    . LYS   A 1  326 ? 13.032  99.386  87.197  1.00 53.36  ? 326 LYS   A CG    1 
ATOM   2566  C  CD    . LYS   A 1  326 ? 12.354  100.735 87.481  1.00 66.51  ? 326 LYS   A CD    1 
ATOM   2567  C  CE    . LYS   A 1  326 ? 11.544  101.268 86.284  1.00 61.68  ? 326 LYS   A CE    1 
ATOM   2568  N  NZ    . LYS   A 1  326 ? 11.327  102.748 86.340  1.00 48.60  ? 326 LYS   A NZ    1 
ATOM   2569  N  N     . ASP   A 1  327 ? 13.690  97.340  84.759  1.00 31.43  ? 327 ASP   A N     1 
ATOM   2570  C  CA    . ASP   A 1  327 ? 12.832  96.325  84.159  1.00 27.80  ? 327 ASP   A CA    1 
ATOM   2571  C  C     . ASP   A 1  327 ? 13.572  95.016  83.932  1.00 34.46  ? 327 ASP   A C     1 
ATOM   2572  O  O     . ASP   A 1  327 ? 13.044  93.941  84.247  1.00 40.35  ? 327 ASP   A O     1 
ATOM   2573  C  CB    . ASP   A 1  327 ? 12.277  96.828  82.834  1.00 43.24  ? 327 ASP   A CB    1 
ATOM   2574  C  CG    . ASP   A 1  327 ? 11.695  98.215  82.942  1.00 46.01  ? 327 ASP   A CG    1 
ATOM   2575  O  OD1   . ASP   A 1  327 ? 11.311  98.563  84.081  1.00 38.45  ? 327 ASP   A OD1   1 
ATOM   2576  O  OD2   . ASP   A 1  327 ? 11.631  98.934  81.905  1.00 37.15  ? 327 ASP   A OD2   1 
ATOM   2577  N  N     . VAL   A 1  328 ? 14.787  95.072  83.372  1.00 32.79  ? 328 VAL   A N     1 
ATOM   2578  C  CA    . VAL   A 1  328 ? 15.540  93.838  83.109  1.00 33.13  ? 328 VAL   A CA    1 
ATOM   2579  C  C     . VAL   A 1  328 ? 15.709  93.007  84.386  1.00 34.94  ? 328 VAL   A C     1 
ATOM   2580  O  O     . VAL   A 1  328 ? 15.331  91.835  84.433  1.00 40.69  ? 328 VAL   A O     1 
ATOM   2581  C  CB    . VAL   A 1  328 ? 16.900  94.135  82.455  1.00 28.98  ? 328 VAL   A CB    1 
ATOM   2582  C  CG1   . VAL   A 1  328 ? 17.646  92.811  82.279  1.00 30.48  ? 328 VAL   A CG1   1 
ATOM   2583  C  CG2   . VAL   A 1  328 ? 16.727  94.841  81.093  1.00 24.25  ? 328 VAL   A CG2   1 
ATOM   2584  N  N     . ASN   A 1  329 ? 16.300  93.584  85.434  1.00 34.91  ? 329 ASN   A N     1 
ATOM   2585  C  CA    . ASN   A 1  329 ? 16.399  92.862  86.706  1.00 39.69  ? 329 ASN   A CA    1 
ATOM   2586  C  C     . ASN   A 1  329 ? 15.033  92.416  87.214  1.00 36.09  ? 329 ASN   A C     1 
ATOM   2587  O  O     . ASN   A 1  329 ? 14.844  91.267  87.618  1.00 34.90  ? 329 ASN   A O     1 
ATOM   2588  C  CB    . ASN   A 1  329 ? 17.076  93.740  87.749  1.00 43.43  ? 329 ASN   A CB    1 
ATOM   2589  C  CG    . ASN   A 1  329 ? 18.394  94.255  87.273  1.00 53.24  ? 329 ASN   A CG    1 
ATOM   2590  O  OD1   . ASN   A 1  329 ? 19.060  93.611  86.456  1.00 51.75  ? 329 ASN   A OD1   1 
ATOM   2591  N  ND2   . ASN   A 1  329 ? 18.785  95.431  87.758  1.00 54.26  ? 329 ASN   A ND2   1 
ATOM   2592  N  N     . ALA   A 1  330 ? 14.076  93.332  87.245  1.00 30.98  ? 330 ALA   A N     1 
ATOM   2593  C  CA    . ALA   A 1  330 ? 12.722  92.948  87.609  1.00 37.04  ? 330 ALA   A CA    1 
ATOM   2594  C  C     . ALA   A 1  330 ? 12.301  91.659  86.909  1.00 40.93  ? 330 ALA   A C     1 
ATOM   2595  O  O     . ALA   A 1  330 ? 11.864  90.699  87.555  1.00 42.04  ? 330 ALA   A O     1 
ATOM   2596  C  CB    . ALA   A 1  330 ? 11.766  94.088  87.270  1.00 38.88  ? 330 ALA   A CB    1 
ATOM   2597  N  N     . ALA   A 1  331 ? 12.435  91.625  85.579  1.00 36.56  ? 331 ALA   A N     1 
ATOM   2598  C  CA    . ALA   A 1  331 ? 12.000  90.468  84.801  1.00 33.64  ? 331 ALA   A CA    1 
ATOM   2599  C  C     . ALA   A 1  331 ? 12.817  89.222  85.147  1.00 35.69  ? 331 ALA   A C     1 
ATOM   2600  O  O     . ALA   A 1  331 ? 12.259  88.144  85.363  1.00 38.75  ? 331 ALA   A O     1 
ATOM   2601  C  CB    . ALA   A 1  331 ? 12.091  90.785  83.306  1.00 28.10  ? 331 ALA   A CB    1 
ATOM   2602  N  N     . ILE   A 1  332 ? 14.145  89.348  85.196  1.00 35.52  ? 332 ILE   A N     1 
ATOM   2603  C  CA    . ILE   A 1  332 ? 14.993  88.231  85.607  1.00 30.14  ? 332 ILE   A CA    1 
ATOM   2604  C  C     . ILE   A 1  332 ? 14.475  87.627  86.902  1.00 36.22  ? 332 ILE   A C     1 
ATOM   2605  O  O     . ILE   A 1  332 ? 14.118  86.447  86.961  1.00 46.91  ? 332 ILE   A O     1 
ATOM   2606  C  CB    . ILE   A 1  332 ? 16.448  88.690  85.753  1.00 24.35  ? 332 ILE   A CB    1 
ATOM   2607  C  CG1   . ILE   A 1  332 ? 16.946  89.173  84.399  1.00 30.12  ? 332 ILE   A CG1   1 
ATOM   2608  C  CG2   . ILE   A 1  332 ? 17.282  87.570  86.337  1.00 23.73  ? 332 ILE   A CG2   1 
ATOM   2609  C  CD1   . ILE   A 1  332 ? 18.369  89.676  84.399  1.00 33.63  ? 332 ILE   A CD1   1 
ATOM   2610  N  N     . ALA   A 1  333 ? 14.440  88.431  87.959  1.00 36.03  ? 333 ALA   A N     1 
ATOM   2611  C  CA    . ALA   A 1  333 ? 13.807  88.077  89.224  1.00 40.74  ? 333 ALA   A CA    1 
ATOM   2612  C  C     . ALA   A 1  333 ? 12.636  87.112  89.055  1.00 44.25  ? 333 ALA   A C     1 
ATOM   2613  O  O     . ALA   A 1  333 ? 12.575  86.054  89.692  1.00 49.66  ? 333 ALA   A O     1 
ATOM   2614  C  CB    . ALA   A 1  333 ? 13.310  89.348  89.917  1.00 35.76  ? 333 ALA   A CB    1 
ATOM   2615  N  N     . THR   A 1  334 ? 11.706  87.469  88.183  1.00 35.68  ? 334 THR   A N     1 
ATOM   2616  C  CA    . THR   A 1  334 ? 10.426  86.793  88.161  1.00 36.84  ? 334 THR   A CA    1 
ATOM   2617  C  C     . THR   A 1  334 ? 10.447  85.540  87.292  1.00 48.20  ? 334 THR   A C     1 
ATOM   2618  O  O     . THR   A 1  334 ? 9.821   84.534  87.657  1.00 47.20  ? 334 THR   A O     1 
ATOM   2619  C  CB    . THR   A 1  334 ? 9.339   87.785  87.716  1.00 45.44  ? 334 THR   A CB    1 
ATOM   2620  O  OG1   . THR   A 1  334 ? 8.080   87.399  88.277  1.00 44.30  ? 334 THR   A OG1   1 
ATOM   2621  C  CG2   . THR   A 1  334 ? 9.217   87.861  86.186  1.00 45.41  ? 334 THR   A CG2   1 
ATOM   2622  N  N     . ILE   A 1  335 ? 11.165  85.562  86.158  1.00 48.80  ? 335 ILE   A N     1 
ATOM   2623  C  CA    . ILE   A 1  335 ? 11.330  84.323  85.399  1.00 48.74  ? 335 ILE   A CA    1 
ATOM   2624  C  C     . ILE   A 1  335 ? 12.220  83.367  86.175  1.00 44.65  ? 335 ILE   A C     1 
ATOM   2625  O  O     . ILE   A 1  335 ? 12.055  82.148  86.069  1.00 47.66  ? 335 ILE   A O     1 
ATOM   2626  C  CB    . ILE   A 1  335 ? 11.885  84.551  83.975  1.00 36.57  ? 335 ILE   A CB    1 
ATOM   2627  C  CG1   . ILE   A 1  335 ? 13.385  84.823  84.022  1.00 45.40  ? 335 ILE   A CG1   1 
ATOM   2628  C  CG2   . ILE   A 1  335 ? 11.163  85.676  83.247  1.00 47.71  ? 335 ILE   A CG2   1 
ATOM   2629  C  CD1   . ILE   A 1  335 ? 14.242  83.572  83.962  1.00 39.78  ? 335 ILE   A CD1   1 
ATOM   2630  N  N     . LYS   A 1  336 ? 13.155  83.892  86.980  1.00 36.26  ? 336 LYS   A N     1 
ATOM   2631  C  CA    . LYS   A 1  336 ? 14.024  83.026  87.777  1.00 47.25  ? 336 LYS   A CA    1 
ATOM   2632  C  C     . LYS   A 1  336 ? 13.229  82.021  88.604  1.00 57.02  ? 336 LYS   A C     1 
ATOM   2633  O  O     . LYS   A 1  336 ? 13.671  80.879  88.793  1.00 50.25  ? 336 LYS   A O     1 
ATOM   2634  C  CB    . LYS   A 1  336 ? 14.921  83.856  88.693  1.00 41.51  ? 336 LYS   A CB    1 
ATOM   2635  C  CG    . LYS   A 1  336 ? 16.392  83.738  88.333  1.00 56.20  ? 336 LYS   A CG    1 
ATOM   2636  C  CD    . LYS   A 1  336 ? 16.823  82.276  88.149  1.00 56.43  ? 336 LYS   A CD    1 
ATOM   2637  C  CE    . LYS   A 1  336 ? 17.273  81.637  89.471  1.00 54.87  ? 336 LYS   A CE    1 
ATOM   2638  N  NZ    . LYS   A 1  336 ? 17.315  80.148  89.389  1.00 49.06  ? 336 LYS   A NZ    1 
ATOM   2639  N  N     . THR   A 1  337 ? 12.061  82.431  89.117  1.00 54.25  ? 337 THR   A N     1 
ATOM   2640  C  CA    . THR   A 1  337 ? 11.214  81.522  89.883  1.00 54.40  ? 337 THR   A CA    1 
ATOM   2641  C  C     . THR   A 1  337 ? 10.426  80.584  88.969  1.00 53.11  ? 337 THR   A C     1 
ATOM   2642  O  O     . THR   A 1  337 ? 10.505  79.361  89.114  1.00 61.91  ? 337 THR   A O     1 
ATOM   2643  C  CB    . THR   A 1  337 ? 10.265  82.315  90.794  1.00 57.52  ? 337 THR   A CB    1 
ATOM   2644  O  OG1   . THR   A 1  337 ? 9.348   83.087  90.002  1.00 60.40  ? 337 THR   A OG1   1 
ATOM   2645  C  CG2   . THR   A 1  337 ? 11.049  83.240  91.736  1.00 37.45  ? 337 THR   A CG2   1 
ATOM   2646  N  N     . LYS   A 1  338 ? 9.693   81.138  87.998  1.00 56.44  ? 338 LYS   A N     1 
ATOM   2647  C  CA    . LYS   A 1  338 ? 8.792   80.334  87.172  1.00 53.66  ? 338 LYS   A CA    1 
ATOM   2648  C  C     . LYS   A 1  338 ? 9.533   79.274  86.350  1.00 57.05  ? 338 LYS   A C     1 
ATOM   2649  O  O     . LYS   A 1  338 ? 9.056   78.140  86.229  1.00 59.54  ? 338 LYS   A O     1 
ATOM   2650  C  CB    . LYS   A 1  338 ? 7.973   81.255  86.262  1.00 54.23  ? 338 LYS   A CB    1 
ATOM   2651  C  CG    . LYS   A 1  338 ? 6.484   81.372  86.635  1.00 59.06  ? 338 LYS   A CG    1 
ATOM   2652  C  CD    . LYS   A 1  338 ? 6.244   82.133  87.952  1.00 59.52  ? 338 LYS   A CD    1 
ATOM   2653  C  CE    . LYS   A 1  338 ? 4.836   81.860  88.497  1.00 56.28  ? 338 LYS   A CE    1 
ATOM   2654  N  NZ    . LYS   A 1  338 ? 3.765   82.176  87.510  1.00 52.26  ? 338 LYS   A NZ    1 
ATOM   2655  N  N     . ARG   A 1  339 ? 10.688  79.609  85.774  1.00 52.73  ? 339 ARG   A N     1 
ATOM   2656  C  CA    . ARG   A 1  339 ? 11.389  78.725  84.849  1.00 45.16  ? 339 ARG   A CA    1 
ATOM   2657  C  C     . ARG   A 1  339 ? 12.448  77.877  85.558  1.00 49.83  ? 339 ARG   A C     1 
ATOM   2658  O  O     . ARG   A 1  339 ? 12.811  78.115  86.714  1.00 52.33  ? 339 ARG   A O     1 
ATOM   2659  C  CB    . ARG   A 1  339 ? 12.047  79.540  83.737  1.00 39.19  ? 339 ARG   A CB    1 
ATOM   2660  C  CG    . ARG   A 1  339 ? 11.079  80.342  82.903  1.00 44.07  ? 339 ARG   A CG    1 
ATOM   2661  C  CD    . ARG   A 1  339 ? 10.411  79.472  81.859  1.00 52.94  ? 339 ARG   A CD    1 
ATOM   2662  N  NE    . ARG   A 1  339 ? 9.796   80.273  80.804  1.00 56.90  ? 339 ARG   A NE    1 
ATOM   2663  C  CZ    . ARG   A 1  339 ? 9.125   79.773  79.771  1.00 53.93  ? 339 ARG   A CZ    1 
ATOM   2664  N  NH1   . ARG   A 1  339 ? 8.984   78.464  79.604  1.00 56.70  ? 339 ARG   A NH1   1 
ATOM   2665  N  NH2   . ARG   A 1  339 ? 8.574   80.606  78.885  1.00 41.58  ? 339 ARG   A NH2   1 
ATOM   2666  N  N     . SER   A 1  340 ? 12.963  76.876  84.825  1.00 49.18  ? 340 SER   A N     1 
ATOM   2667  C  CA    . SER   A 1  340 ? 14.001  75.968  85.319  1.00 42.39  ? 340 SER   A CA    1 
ATOM   2668  C  C     . SER   A 1  340 ? 15.311  76.355  84.654  1.00 36.94  ? 340 SER   A C     1 
ATOM   2669  O  O     . SER   A 1  340 ? 15.495  76.127  83.454  1.00 40.52  ? 340 SER   A O     1 
ATOM   2670  C  CB    . SER   A 1  340 ? 13.652  74.516  85.018  1.00 34.76  ? 340 SER   A CB    1 
ATOM   2671  O  OG    . SER   A 1  340 ? 12.245  74.385  84.908  1.00 39.63  ? 340 SER   A OG    1 
ATOM   2672  N  N     . ILE   A 1  341 ? 16.213  76.957  85.425  1.00 38.27  ? 341 ILE   A N     1 
ATOM   2673  C  CA    . ILE   A 1  341 ? 17.381  77.611  84.845  1.00 35.30  ? 341 ILE   A CA    1 
ATOM   2674  C  C     . ILE   A 1  341 ? 18.583  77.342  85.730  1.00 33.46  ? 341 ILE   A C     1 
ATOM   2675  O  O     . ILE   A 1  341 ? 19.074  78.246  86.422  1.00 40.34  ? 341 ILE   A O     1 
ATOM   2676  C  CB    . ILE   A 1  341 ? 17.145  79.126  84.661  1.00 31.42  ? 341 ILE   A CB    1 
ATOM   2677  C  CG1   . ILE   A 1  341 ? 15.900  79.376  83.793  1.00 34.22  ? 341 ILE   A CG1   1 
ATOM   2678  C  CG2   . ILE   A 1  341 ? 18.339  79.773  84.036  1.00 22.44  ? 341 ILE   A CG2   1 
ATOM   2679  C  CD1   . ILE   A 1  341 ? 15.678  80.806  83.417  1.00 32.01  ? 341 ILE   A CD1   1 
ATOM   2680  N  N     . GLN   A 1  342 ? 19.069  76.101  85.698  1.00 35.81  ? 342 GLN   A N     1 
ATOM   2681  C  CA    . GLN   A 1  342 ? 20.212  75.668  86.493  1.00 37.98  ? 342 GLN   A CA    1 
ATOM   2682  C  C     . GLN   A 1  342 ? 21.497  75.813  85.682  1.00 30.96  ? 342 GLN   A C     1 
ATOM   2683  O  O     . GLN   A 1  342 ? 21.592  75.281  84.573  1.00 35.30  ? 342 GLN   A O     1 
ATOM   2684  C  CB    . GLN   A 1  342 ? 20.033  74.220  86.945  1.00 38.36  ? 342 GLN   A CB    1 
ATOM   2685  C  CG    . GLN   A 1  342 ? 21.308  73.608  87.474  1.00 52.34  ? 342 GLN   A CG    1 
ATOM   2686  C  CD    . GLN   A 1  342 ? 21.056  72.346  88.263  1.00 71.88  ? 342 GLN   A CD    1 
ATOM   2687  O  OE1   . GLN   A 1  342 ? 19.903  72.019  88.570  1.00 72.15  ? 342 GLN   A OE1   1 
ATOM   2688  N  NE2   . GLN   A 1  342 ? 22.133  71.622  88.599  1.00 65.13  ? 342 GLN   A NE2   1 
ATOM   2689  N  N     . PHE   A 1  343 ? 22.469  76.548  86.224  1.00 27.83  ? 343 PHE   A N     1 
ATOM   2690  C  CA    . PHE   A 1  343 ? 23.812  76.615  85.661  1.00 29.12  ? 343 PHE   A CA    1 
ATOM   2691  C  C     . PHE   A 1  343 ? 24.645  75.470  86.232  1.00 38.62  ? 343 PHE   A C     1 
ATOM   2692  O  O     . PHE   A 1  343 ? 24.218  74.742  87.133  1.00 44.67  ? 343 PHE   A O     1 
ATOM   2693  C  CB    . PHE   A 1  343 ? 24.495  77.967  85.972  1.00 30.36  ? 343 PHE   A CB    1 
ATOM   2694  C  CG    . PHE   A 1  343 ? 23.976  79.152  85.165  1.00 25.90  ? 343 PHE   A CG    1 
ATOM   2695  C  CD1   . PHE   A 1  343 ? 22.697  79.661  85.370  1.00 29.33  ? 343 PHE   A CD1   1 
ATOM   2696  C  CD2   . PHE   A 1  343 ? 24.790  79.785  84.237  1.00 29.14  ? 343 PHE   A CD2   1 
ATOM   2697  C  CE1   . PHE   A 1  343 ? 22.225  80.739  84.632  1.00 29.50  ? 343 PHE   A CE1   1 
ATOM   2698  C  CE2   . PHE   A 1  343 ? 24.327  80.882  83.493  1.00 30.31  ? 343 PHE   A CE2   1 
ATOM   2699  C  CZ    . PHE   A 1  343 ? 23.043  81.352  83.689  1.00 28.29  ? 343 PHE   A CZ    1 
ATOM   2700  N  N     . VAL   A 1  344 ? 25.848  75.321  85.720  1.00 40.49  ? 344 VAL   A N     1 
ATOM   2701  C  CA    . VAL   A 1  344 ? 26.753  74.314  86.259  1.00 44.31  ? 344 VAL   A CA    1 
ATOM   2702  C  C     . VAL   A 1  344 ? 27.498  74.905  87.442  1.00 49.80  ? 344 VAL   A C     1 
ATOM   2703  O  O     . VAL   A 1  344 ? 27.742  76.115  87.496  1.00 49.98  ? 344 VAL   A O     1 
ATOM   2704  C  CB    . VAL   A 1  344 ? 27.706  73.807  85.170  1.00 39.14  ? 344 VAL   A CB    1 
ATOM   2705  C  CG1   . VAL   A 1  344 ? 26.925  72.946  84.229  1.00 40.41  ? 344 VAL   A CG1   1 
ATOM   2706  C  CG2   . VAL   A 1  344 ? 28.336  74.985  84.434  1.00 36.67  ? 344 VAL   A CG2   1 
ATOM   2707  N  N     . ASP   A 1  345 ? 27.854  74.051  88.412  1.00 55.16  ? 345 ASP   A N     1 
ATOM   2708  C  CA    . ASP   A 1  345 ? 28.290  74.571  89.712  1.00 56.10  ? 345 ASP   A CA    1 
ATOM   2709  C  C     . ASP   A 1  345 ? 29.495  75.488  89.564  1.00 53.17  ? 345 ASP   A C     1 
ATOM   2710  O  O     . ASP   A 1  345 ? 29.531  76.583  90.133  1.00 54.44  ? 345 ASP   A O     1 
ATOM   2711  C  CB    . ASP   A 1  345 ? 28.600  73.434  90.682  1.00 39.57  ? 345 ASP   A CB    1 
ATOM   2712  C  CG    . ASP   A 1  345 ? 27.508  72.372  90.713  1.00 53.60  ? 345 ASP   A CG    1 
ATOM   2713  O  OD1   . ASP   A 1  345 ? 26.303  72.714  90.705  1.00 48.19  ? 345 ASP   A OD1   1 
ATOM   2714  O  OD2   . ASP   A 1  345 ? 27.868  71.170  90.768  1.00 59.55  ? 345 ASP   A OD2   1 
ATOM   2715  N  N     . TRP   A 1  346 ? 30.474  75.081  88.777  1.00 45.79  ? 346 TRP   A N     1 
ATOM   2716  C  CA    . TRP   A 1  346 ? 31.668  75.890  88.604  1.00 50.00  ? 346 TRP   A CA    1 
ATOM   2717  C  C     . TRP   A 1  346 ? 31.402  77.179  87.818  1.00 53.58  ? 346 TRP   A C     1 
ATOM   2718  O  O     . TRP   A 1  346 ? 32.337  77.788  87.282  1.00 41.35  ? 346 TRP   A O     1 
ATOM   2719  C  CB    . TRP   A 1  346 ? 32.727  75.045  87.914  1.00 60.11  ? 346 TRP   A CB    1 
ATOM   2720  C  CG    . TRP   A 1  346 ? 32.213  74.527  86.619  1.00 66.05  ? 346 TRP   A CG    1 
ATOM   2721  C  CD1   . TRP   A 1  346 ? 31.513  73.365  86.406  1.00 68.92  ? 346 TRP   A CD1   1 
ATOM   2722  C  CD2   . TRP   A 1  346 ? 32.322  75.171  85.344  1.00 67.96  ? 346 TRP   A CD2   1 
ATOM   2723  N  NE1   . TRP   A 1  346 ? 31.202  73.244  85.072  1.00 63.59  ? 346 TRP   A NE1   1 
ATOM   2724  C  CE2   . TRP   A 1  346 ? 31.688  74.337  84.400  1.00 65.77  ? 346 TRP   A CE2   1 
ATOM   2725  C  CE3   . TRP   A 1  346 ? 32.909  76.370  84.905  1.00 69.87  ? 346 TRP   A CE3   1 
ATOM   2726  C  CZ2   . TRP   A 1  346 ? 31.611  74.671  83.046  1.00 67.09  ? 346 TRP   A CZ2   1 
ATOM   2727  C  CZ3   . TRP   A 1  346 ? 32.846  76.696  83.554  1.00 64.40  ? 346 TRP   A CZ3   1 
ATOM   2728  C  CH2   . TRP   A 1  346 ? 32.196  75.854  82.643  1.00 67.78  ? 346 TRP   A CH2   1 
ATOM   2729  N  N     . CYS   A 1  347 ? 30.140  77.617  87.759  1.00 51.97  ? 347 CYS   A N     1 
ATOM   2730  C  CA    . CYS   A 1  347 ? 29.741  78.839  87.048  1.00 51.35  ? 347 CYS   A CA    1 
ATOM   2731  C  C     . CYS   A 1  347 ? 28.707  79.581  87.877  1.00 47.25  ? 347 CYS   A C     1 
ATOM   2732  O  O     . CYS   A 1  347 ? 27.796  78.955  88.450  1.00 46.17  ? 347 CYS   A O     1 
ATOM   2733  C  CB    . CYS   A 1  347 ? 29.143  78.572  85.659  1.00 51.30  ? 347 CYS   A CB    1 
ATOM   2734  S  SG    . CYS   A 1  347 ? 30.301  78.298  84.303  1.00 59.61  ? 347 CYS   A SG    1 
ATOM   2735  N  N     . PRO   A 1  348 ? 28.801  80.905  87.936  1.00 43.96  ? 348 PRO   A N     1 
ATOM   2736  C  CA    . PRO   A 1  348 ? 27.824  81.668  88.717  1.00 37.50  ? 348 PRO   A CA    1 
ATOM   2737  C  C     . PRO   A 1  348 ? 26.499  81.687  87.994  1.00 35.90  ? 348 PRO   A C     1 
ATOM   2738  O  O     . PRO   A 1  348 ? 26.451  81.716  86.765  1.00 43.05  ? 348 PRO   A O     1 
ATOM   2739  C  CB    . PRO   A 1  348 ? 28.441  83.068  88.807  1.00 40.89  ? 348 PRO   A CB    1 
ATOM   2740  C  CG    . PRO   A 1  348 ? 29.344  83.164  87.593  1.00 43.92  ? 348 PRO   A CG    1 
ATOM   2741  C  CD    . PRO   A 1  348 ? 29.807  81.763  87.283  1.00 47.53  ? 348 PRO   A CD    1 
ATOM   2742  N  N     . THR   A 1  349 ? 25.418  81.632  88.757  1.00 37.02  ? 349 THR   A N     1 
ATOM   2743  C  CA    . THR   A 1  349 ? 24.092  81.818  88.182  1.00 35.84  ? 349 THR   A CA    1 
ATOM   2744  C  C     . THR   A 1  349 ? 23.920  83.310  87.958  1.00 41.38  ? 349 THR   A C     1 
ATOM   2745  O  O     . THR   A 1  349 ? 23.733  84.067  88.909  1.00 46.87  ? 349 THR   A O     1 
ATOM   2746  C  CB    . THR   A 1  349 ? 23.013  81.255  89.096  1.00 37.00  ? 349 THR   A CB    1 
ATOM   2747  O  OG1   . THR   A 1  349 ? 22.968  79.822  88.967  1.00 39.19  ? 349 THR   A OG1   1 
ATOM   2748  C  CG2   . THR   A 1  349 ? 21.668  81.849  88.731  1.00 39.02  ? 349 THR   A CG2   1 
ATOM   2749  N  N     . GLY   A 1  350 ? 24.011  83.747  86.703  1.00 43.16  ? 350 GLY   A N     1 
ATOM   2750  C  CA    . GLY   A 1  350 ? 23.955  85.172  86.416  1.00 44.42  ? 350 GLY   A CA    1 
ATOM   2751  C  C     . GLY   A 1  350 ? 23.871  85.467  84.934  1.00 42.66  ? 350 GLY   A C     1 
ATOM   2752  O  O     . GLY   A 1  350 ? 24.169  84.621  84.085  1.00 46.84  ? 350 GLY   A O     1 
ATOM   2753  N  N     . PHE   A 1  351 ? 23.469  86.709  84.642  1.00 41.61  ? 351 PHE   A N     1 
ATOM   2754  C  CA    . PHE   A 1  351 ? 23.209  87.203  83.293  1.00 39.15  ? 351 PHE   A CA    1 
ATOM   2755  C  C     . PHE   A 1  351 ? 24.064  88.430  83.009  1.00 35.74  ? 351 PHE   A C     1 
ATOM   2756  O  O     . PHE   A 1  351 ? 24.154  89.336  83.839  1.00 39.71  ? 351 PHE   A O     1 
ATOM   2757  C  CB    . PHE   A 1  351 ? 21.725  87.586  83.118  1.00 37.88  ? 351 PHE   A CB    1 
ATOM   2758  C  CG    . PHE   A 1  351 ? 20.790  86.418  83.143  1.00 39.39  ? 351 PHE   A CG    1 
ATOM   2759  C  CD1   . PHE   A 1  351 ? 20.386  85.859  84.339  1.00 35.51  ? 351 PHE   A CD1   1 
ATOM   2760  C  CD2   . PHE   A 1  351 ? 20.309  85.874  81.961  1.00 41.56  ? 351 PHE   A CD2   1 
ATOM   2761  C  CE1   . PHE   A 1  351 ? 19.535  84.769  84.354  1.00 28.03  ? 351 PHE   A CE1   1 
ATOM   2762  C  CE2   . PHE   A 1  351 ? 19.446  84.781  81.978  1.00 36.92  ? 351 PHE   A CE2   1 
ATOM   2763  C  CZ    . PHE   A 1  351 ? 19.062  84.232  83.181  1.00 23.33  ? 351 PHE   A CZ    1 
ATOM   2764  N  N     . LYS   A 1  352 ? 24.679  88.483  81.838  1.00 27.04  ? 352 LYS   A N     1 
ATOM   2765  C  CA    . LYS   A 1  352 ? 25.264  89.726  81.365  1.00 24.78  ? 352 LYS   A CA    1 
ATOM   2766  C  C     . LYS   A 1  352 ? 24.265  90.393  80.433  1.00 33.63  ? 352 LYS   A C     1 
ATOM   2767  O  O     . LYS   A 1  352 ? 23.696  89.737  79.553  1.00 28.82  ? 352 LYS   A O     1 
ATOM   2768  C  CB    . LYS   A 1  352 ? 26.588  89.500  80.647  1.00 25.75  ? 352 LYS   A CB    1 
ATOM   2769  C  CG    . LYS   A 1  352 ? 27.687  89.108  81.554  1.00 30.00  ? 352 LYS   A CG    1 
ATOM   2770  C  CD    . LYS   A 1  352 ? 29.028  89.451  80.959  1.00 34.40  ? 352 LYS   A CD    1 
ATOM   2771  C  CE    . LYS   A 1  352 ? 30.088  88.680  81.714  1.00 31.83  ? 352 LYS   A CE    1 
ATOM   2772  N  NZ    . LYS   A 1  352 ? 29.376  87.582  82.432  1.00 34.74  ? 352 LYS   A NZ    1 
ATOM   2773  N  N     . VAL   A 1  353 ? 24.046  91.688  80.631  1.00 34.34  ? 353 VAL   A N     1 
ATOM   2774  C  CA    . VAL   A 1  353 ? 23.015  92.416  79.912  1.00 32.09  ? 353 VAL   A CA    1 
ATOM   2775  C  C     . VAL   A 1  353 ? 23.649  93.572  79.142  1.00 33.80  ? 353 VAL   A C     1 
ATOM   2776  O  O     . VAL   A 1  353 ? 24.613  94.201  79.602  1.00 31.25  ? 353 VAL   A O     1 
ATOM   2777  C  CB    . VAL   A 1  353 ? 21.917  92.893  80.887  1.00 32.34  ? 353 VAL   A CB    1 
ATOM   2778  C  CG1   . VAL   A 1  353 ? 20.790  93.645  80.141  1.00 30.25  ? 353 VAL   A CG1   1 
ATOM   2779  C  CG2   . VAL   A 1  353 ? 21.364  91.692  81.637  1.00 24.92  ? 353 VAL   A CG2   1 
ATOM   2780  N  N     . GLY   A 1  354 ? 23.125  93.818  77.944  1.00 26.85  ? 354 GLY   A N     1 
ATOM   2781  C  CA    . GLY   A 1  354 ? 23.519  94.959  77.152  1.00 23.68  ? 354 GLY   A CA    1 
ATOM   2782  C  C     . GLY   A 1  354 ? 22.304  95.588  76.515  1.00 26.30  ? 354 GLY   A C     1 
ATOM   2783  O  O     . GLY   A 1  354 ? 21.401  94.869  76.077  1.00 26.63  ? 354 GLY   A O     1 
ATOM   2784  N  N     . ILE   A 1  355 ? 22.246  96.919  76.472  1.00 25.33  ? 355 ILE   A N     1 
ATOM   2785  C  CA    . ILE   A 1  355 ? 21.103  97.619  75.906  1.00 25.61  ? 355 ILE   A CA    1 
ATOM   2786  C  C     . ILE   A 1  355 ? 21.587  98.668  74.922  1.00 31.36  ? 355 ILE   A C     1 
ATOM   2787  O  O     . ILE   A 1  355 ? 22.382  99.547  75.277  1.00 36.15  ? 355 ILE   A O     1 
ATOM   2788  C  CB    . ILE   A 1  355 ? 20.232  98.279  76.976  1.00 27.97  ? 355 ILE   A CB    1 
ATOM   2789  C  CG1   . ILE   A 1  355 ? 20.054  97.357  78.187  1.00 23.03  ? 355 ILE   A CG1   1 
ATOM   2790  C  CG2   . ILE   A 1  355 ? 18.897  98.653  76.350  1.00 23.44  ? 355 ILE   A CG2   1 
ATOM   2791  C  CD1   . ILE   A 1  355 ? 18.995  97.848  79.205  1.00 25.26  ? 355 ILE   A CD1   1 
ATOM   2792  N  N     . ASN   A 1  356 ? 21.092  98.584  73.697  1.00 31.69  ? 356 ASN   A N     1 
ATOM   2793  C  CA    . ASN   A 1  356 ? 21.271  99.619  72.695  1.00 35.80  ? 356 ASN   A CA    1 
ATOM   2794  C  C     . ASN   A 1  356 ? 19.934  100.332 72.562  1.00 34.23  ? 356 ASN   A C     1 
ATOM   2795  O  O     . ASN   A 1  356 ? 18.914  99.689  72.278  1.00 28.26  ? 356 ASN   A O     1 
ATOM   2796  C  CB    . ASN   A 1  356 ? 21.719  99.010  71.367  1.00 30.50  ? 356 ASN   A CB    1 
ATOM   2797  C  CG    . ASN   A 1  356 ? 22.772  99.839  70.670  1.00 44.23  ? 356 ASN   A CG    1 
ATOM   2798  O  OD1   . ASN   A 1  356 ? 22.457  100.862 70.047  1.00 51.85  ? 356 ASN   A OD1   1 
ATOM   2799  N  ND2   . ASN   A 1  356 ? 24.037  99.402  70.762  1.00 44.11  ? 356 ASN   A ND2   1 
ATOM   2800  N  N     . TYR   A 1  357 ? 19.934  101.646 72.808  1.00 32.66  ? 357 TYR   A N     1 
ATOM   2801  C  CA    . TYR   A 1  357 ? 18.676  102.375 72.947  1.00 34.29  ? 357 TYR   A CA    1 
ATOM   2802  C  C     . TYR   A 1  357 ? 17.887  102.446 71.650  1.00 38.26  ? 357 TYR   A C     1 
ATOM   2803  O  O     . TYR   A 1  357 ? 16.671  102.673 71.701  1.00 38.76  ? 357 TYR   A O     1 
ATOM   2804  C  CB    . TYR   A 1  357 ? 18.930  103.787 73.475  1.00 30.87  ? 357 TYR   A CB    1 
ATOM   2805  C  CG    . TYR   A 1  357 ? 19.223  103.826 74.949  1.00 39.30  ? 357 TYR   A CG    1 
ATOM   2806  C  CD1   . TYR   A 1  357 ? 18.365  103.221 75.866  1.00 35.39  ? 357 TYR   A CD1   1 
ATOM   2807  C  CD2   . TYR   A 1  357 ? 20.364  104.439 75.431  1.00 42.70  ? 357 TYR   A CD2   1 
ATOM   2808  C  CE1   . TYR   A 1  357 ? 18.633  103.243 77.213  1.00 34.83  ? 357 TYR   A CE1   1 
ATOM   2809  C  CE2   . TYR   A 1  357 ? 20.636  104.466 76.786  1.00 45.16  ? 357 TYR   A CE2   1 
ATOM   2810  C  CZ    . TYR   A 1  357 ? 19.769  103.872 77.670  1.00 39.78  ? 357 TYR   A CZ    1 
ATOM   2811  O  OH    . TYR   A 1  357 ? 20.057  103.904 79.019  1.00 38.30  ? 357 TYR   A OH    1 
ATOM   2812  N  N     . GLN   A 1  358 ? 18.544  102.242 70.497  1.00 35.10  ? 358 GLN   A N     1 
ATOM   2813  C  CA    . GLN   A 1  358 ? 17.891  102.356 69.196  1.00 45.48  ? 358 GLN   A CA    1 
ATOM   2814  C  C     . GLN   A 1  358 ? 17.127  101.090 68.817  1.00 47.86  ? 358 GLN   A C     1 
ATOM   2815  O  O     . GLN   A 1  358 ? 17.749  100.050 68.554  1.00 43.41  ? 358 GLN   A O     1 
ATOM   2816  C  CB    . GLN   A 1  358 ? 18.921  102.673 68.115  1.00 45.94  ? 358 GLN   A CB    1 
ATOM   2817  C  CG    . GLN   A 1  358 ? 18.281  103.140 66.842  1.00 48.06  ? 358 GLN   A CG    1 
ATOM   2818  C  CD    . GLN   A 1  358 ? 17.382  104.335 67.089  1.00 64.25  ? 358 GLN   A CD    1 
ATOM   2819  O  OE1   . GLN   A 1  358 ? 16.239  104.387 66.613  1.00 63.09  ? 358 GLN   A OE1   1 
ATOM   2820  N  NE2   . GLN   A 1  358 ? 17.892  105.303 67.855  1.00 60.54  ? 358 GLN   A NE2   1 
ATOM   2821  N  N     . PRO   A 1  359 ? 15.793  101.142 68.741  1.00 50.53  ? 359 PRO   A N     1 
ATOM   2822  C  CA    . PRO   A 1  359 ? 15.003  99.911  68.535  1.00 39.84  ? 359 PRO   A CA    1 
ATOM   2823  C  C     . PRO   A 1  359 ? 15.480  99.174  67.301  1.00 39.45  ? 359 PRO   A C     1 
ATOM   2824  O  O     . PRO   A 1  359 ? 16.273  99.721  66.521  1.00 36.20  ? 359 PRO   A O     1 
ATOM   2825  C  CB    . PRO   A 1  359 ? 13.562  100.426 68.350  1.00 36.62  ? 359 PRO   A CB    1 
ATOM   2826  C  CG    . PRO   A 1  359 ? 13.548  101.797 68.939  1.00 37.99  ? 359 PRO   A CG    1 
ATOM   2827  C  CD    . PRO   A 1  359 ? 14.944  102.350 68.732  1.00 49.16  ? 359 PRO   A CD    1 
ATOM   2828  N  N     . PRO   A 1  360 ? 15.009  97.946  67.076  1.00 45.82  ? 360 PRO   A N     1 
ATOM   2829  C  CA    . PRO   A 1  360 ? 15.506  97.176  65.932  1.00 38.83  ? 360 PRO   A CA    1 
ATOM   2830  C  C     . PRO   A 1  360 ? 15.073  97.809  64.617  1.00 37.83  ? 360 PRO   A C     1 
ATOM   2831  O  O     . PRO   A 1  360 ? 13.943  98.281  64.477  1.00 35.38  ? 360 PRO   A O     1 
ATOM   2832  C  CB    . PRO   A 1  360 ? 14.879  95.791  66.136  1.00 31.19  ? 360 PRO   A CB    1 
ATOM   2833  C  CG    . PRO   A 1  360 ? 14.395  95.784  67.569  1.00 34.82  ? 360 PRO   A CG    1 
ATOM   2834  C  CD    . PRO   A 1  360 ? 13.991  97.194  67.829  1.00 37.62  ? 360 PRO   A CD    1 
ATOM   2835  N  N     . THR   A 1  361 ? 16.006  97.850  63.665  1.00 40.91  ? 361 THR   A N     1 
ATOM   2836  C  CA    . THR   A 1  361 ? 15.720  98.341  62.322  1.00 40.93  ? 361 THR   A CA    1 
ATOM   2837  C  C     . THR   A 1  361 ? 15.123  97.226  61.482  1.00 48.89  ? 361 THR   A C     1 
ATOM   2838  O  O     . THR   A 1  361 ? 15.618  96.095  61.493  1.00 55.42  ? 361 THR   A O     1 
ATOM   2839  C  CB    . THR   A 1  361 ? 16.991  98.842  61.636  1.00 37.28  ? 361 THR   A CB    1 
ATOM   2840  O  OG1   . THR   A 1  361 ? 17.411  100.086 62.210  1.00 33.57  ? 361 THR   A OG1   1 
ATOM   2841  C  CG2   . THR   A 1  361 ? 16.729  99.024  60.167  1.00 41.93  ? 361 THR   A CG2   1 
ATOM   2842  N  N     . VAL   A 1  362 ? 14.064  97.541  60.747  1.00 43.82  ? 362 VAL   A N     1 
ATOM   2843  C  CA    . VAL   A 1  362 ? 13.442  96.575  59.851  1.00 50.31  ? 362 VAL   A CA    1 
ATOM   2844  C  C     . VAL   A 1  362 ? 13.643  97.034  58.417  1.00 52.46  ? 362 VAL   A C     1 
ATOM   2845  O  O     . VAL   A 1  362 ? 13.564  98.232  58.107  1.00 44.50  ? 362 VAL   A O     1 
ATOM   2846  C  CB    . VAL   A 1  362 ? 11.941  96.356  60.130  1.00 46.94  ? 362 VAL   A CB    1 
ATOM   2847  C  CG1   . VAL   A 1  362 ? 11.687  96.132  61.611  1.00 54.55  ? 362 VAL   A CG1   1 
ATOM   2848  C  CG2   . VAL   A 1  362 ? 11.122  97.504  59.581  1.00 39.23  ? 362 VAL   A CG2   1 
ATOM   2849  N  N     . VAL   A 1  363 ? 13.904  96.064  57.548  1.00 48.51  ? 363 VAL   A N     1 
ATOM   2850  C  CA    . VAL   A 1  363 ? 13.982  96.269  56.109  1.00 38.92  ? 363 VAL   A CA    1 
ATOM   2851  C  C     . VAL   A 1  363 ? 12.608  96.713  55.626  1.00 39.82  ? 363 VAL   A C     1 
ATOM   2852  O  O     . VAL   A 1  363 ? 11.631  95.965  55.779  1.00 37.64  ? 363 VAL   A O     1 
ATOM   2853  C  CB    . VAL   A 1  363 ? 14.464  94.988  55.409  1.00 40.71  ? 363 VAL   A CB    1 
ATOM   2854  C  CG1   . VAL   A 1  363 ? 13.907  94.873  53.999  1.00 42.31  ? 363 VAL   A CG1   1 
ATOM   2855  C  CG2   . VAL   A 1  363 ? 15.963  94.972  55.381  1.00 43.30  ? 363 VAL   A CG2   1 
ATOM   2856  N  N     . PRO   A 1  364 ? 12.480  97.918  55.066  1.00 48.70  ? 364 PRO   A N     1 
ATOM   2857  C  CA    . PRO   A 1  364 ? 11.167  98.380  54.595  1.00 43.26  ? 364 PRO   A CA    1 
ATOM   2858  C  C     . PRO   A 1  364 ? 10.544  97.355  53.663  1.00 41.81  ? 364 PRO   A C     1 
ATOM   2859  O  O     . PRO   A 1  364 ? 11.223  96.756  52.825  1.00 39.47  ? 364 PRO   A O     1 
ATOM   2860  C  CB    . PRO   A 1  364 ? 11.494  99.689  53.869  1.00 38.53  ? 364 PRO   A CB    1 
ATOM   2861  C  CG    . PRO   A 1  364 ? 12.755  100.144 54.489  1.00 33.30  ? 364 PRO   A CG    1 
ATOM   2862  C  CD    . PRO   A 1  364 ? 13.538  98.898  54.777  1.00 39.47  ? 364 PRO   A CD    1 
ATOM   2863  N  N     . GLY   A 1  365 ? 9.242   97.135  53.831  1.00 44.76  ? 365 GLY   A N     1 
ATOM   2864  C  CA    . GLY   A 1  365 ? 8.559   96.093  53.087  1.00 57.29  ? 365 GLY   A CA    1 
ATOM   2865  C  C     . GLY   A 1  365 ? 8.969   94.660  53.399  1.00 66.62  ? 365 GLY   A C     1 
ATOM   2866  O  O     . GLY   A 1  365 ? 8.474   93.737  52.737  1.00 59.60  ? 365 GLY   A O     1 
ATOM   2867  N  N     . GLY   A 1  366 ? 9.862   94.434  54.359  1.00 63.86  ? 366 GLY   A N     1 
ATOM   2868  C  CA    . GLY   A 1  366 ? 10.118  93.093  54.839  1.00 45.14  ? 366 GLY   A CA    1 
ATOM   2869  C  C     . GLY   A 1  366 ? 8.880   92.518  55.513  1.00 45.85  ? 366 GLY   A C     1 
ATOM   2870  O  O     . GLY   A 1  366 ? 7.772   93.047  55.420  1.00 43.60  ? 366 GLY   A O     1 
ATOM   2871  N  N     . ASP   A 1  367 ? 9.090   91.407  56.223  1.00 44.93  ? 367 ASP   A N     1 
ATOM   2872  C  CA    . ASP   A 1  367 ? 8.005   90.710  56.904  1.00 35.51  ? 367 ASP   A CA    1 
ATOM   2873  C  C     . ASP   A 1  367 ? 7.852   91.106  58.366  1.00 39.75  ? 367 ASP   A C     1 
ATOM   2874  O  O     . ASP   A 1  367 ? 6.801   90.834  58.951  1.00 41.15  ? 367 ASP   A O     1 
ATOM   2875  C  CB    . ASP   A 1  367 ? 8.207   89.184  56.844  1.00 43.51  ? 367 ASP   A CB    1 
ATOM   2876  C  CG    . ASP   A 1  367 ? 8.520   88.665  55.436  1.00 51.17  ? 367 ASP   A CG    1 
ATOM   2877  O  OD1   . ASP   A 1  367 ? 7.612   88.677  54.577  1.00 47.45  ? 367 ASP   A OD1   1 
ATOM   2878  O  OD2   . ASP   A 1  367 ? 9.677   88.239  55.195  1.00 48.07  ? 367 ASP   A OD2   1 
ATOM   2879  N  N     . LEU   A 1  368 ? 8.864   91.726  58.970  1.00 37.93  ? 368 LEU   A N     1 
ATOM   2880  C  CA    . LEU   A 1  368 ? 8.853   91.992  60.401  1.00 35.48  ? 368 LEU   A CA    1 
ATOM   2881  C  C     . LEU   A 1  368 ? 8.360   93.402  60.683  1.00 39.90  ? 368 LEU   A C     1 
ATOM   2882  O  O     . LEU   A 1  368 ? 8.763   94.366  60.027  1.00 41.27  ? 368 LEU   A O     1 
ATOM   2883  C  CB    . LEU   A 1  368 ? 10.247  91.810  61.008  1.00 38.92  ? 368 LEU   A CB    1 
ATOM   2884  C  CG    . LEU   A 1  368 ? 10.946  90.467  60.794  1.00 43.82  ? 368 LEU   A CG    1 
ATOM   2885  C  CD1   . LEU   A 1  368 ? 12.430  90.546  61.152  1.00 32.99  ? 368 LEU   A CD1   1 
ATOM   2886  C  CD2   . LEU   A 1  368 ? 10.234  89.353  61.575  1.00 45.18  ? 368 LEU   A CD2   1 
ATOM   2887  N  N     . ALA   A 1  369 ? 7.497   93.511  61.681  1.00 43.63  ? 369 ALA   A N     1 
ATOM   2888  C  CA    . ALA   A 1  369 ? 6.995   94.795  62.127  1.00 40.43  ? 369 ALA   A CA    1 
ATOM   2889  C  C     . ALA   A 1  369 ? 8.014   95.471  63.039  1.00 33.50  ? 369 ALA   A C     1 
ATOM   2890  O  O     . ALA   A 1  369 ? 8.808   94.813  63.717  1.00 35.22  ? 369 ALA   A O     1 
ATOM   2891  C  CB    . ALA   A 1  369 ? 5.655   94.606  62.847  1.00 34.73  ? 369 ALA   A CB    1 
ATOM   2892  N  N     . LYS   A 1  370 ? 7.999   96.798  63.036  1.00 35.39  ? 370 LYS   A N     1 
ATOM   2893  C  CA    . LYS   A 1  370 ? 8.812   97.538  63.985  1.00 33.37  ? 370 LYS   A CA    1 
ATOM   2894  C  C     . LYS   A 1  370 ? 8.253   97.330  65.379  1.00 40.61  ? 370 LYS   A C     1 
ATOM   2895  O  O     . LYS   A 1  370 ? 7.041   97.209  65.560  1.00 48.25  ? 370 LYS   A O     1 
ATOM   2896  C  CB    . LYS   A 1  370 ? 8.840   99.020  63.632  1.00 36.33  ? 370 LYS   A CB    1 
ATOM   2897  C  CG    . LYS   A 1  370 ? 9.874   99.365  62.557  1.00 40.44  ? 370 LYS   A CG    1 
ATOM   2898  C  CD    . LYS   A 1  370 ? 9.547   100.681 61.848  1.00 40.56  ? 370 LYS   A CD    1 
ATOM   2899  C  CE    . LYS   A 1  370 ? 8.223   100.569 61.075  1.00 42.72  ? 370 LYS   A CE    1 
ATOM   2900  N  NZ    . LYS   A 1  370 ? 7.852   101.821 60.350  1.00 44.69  ? 370 LYS   A NZ    1 
ATOM   2901  N  N     . VAL   A 1  371 ? 9.145   97.253  66.362  1.00 36.55  ? 371 VAL   A N     1 
ATOM   2902  C  CA    . VAL   A 1  371 ? 8.780   96.948  67.737  1.00 34.14  ? 371 VAL   A CA    1 
ATOM   2903  C  C     . VAL   A 1  371 ? 9.530   97.909  68.639  1.00 37.99  ? 371 VAL   A C     1 
ATOM   2904  O  O     . VAL   A 1  371 ? 10.690  98.244  68.374  1.00 35.70  ? 371 VAL   A O     1 
ATOM   2905  C  CB    . VAL   A 1  371 ? 9.103   95.487  68.113  1.00 31.25  ? 371 VAL   A CB    1 
ATOM   2906  C  CG1   . VAL   A 1  371 ? 8.254   94.520  67.306  1.00 29.98  ? 371 VAL   A CG1   1 
ATOM   2907  C  CG2   . VAL   A 1  371 ? 10.566  95.221  67.905  1.00 28.05  ? 371 VAL   A CG2   1 
ATOM   2908  N  N     . GLN   A 1  372 ? 8.868   98.343  69.715  1.00 36.88  ? 372 GLN   A N     1 
ATOM   2909  C  CA    A GLN   A 1  372 ? 9.485   99.346  70.572  0.58 40.42  ? 372 GLN   A CA    1 
ATOM   2910  C  CA    B GLN   A 1  372 ? 9.453   99.329  70.619  0.42 40.43  ? 372 GLN   A CA    1 
ATOM   2911  C  C     . GLN   A 1  372 ? 10.726  98.823  71.287  1.00 41.00  ? 372 GLN   A C     1 
ATOM   2912  O  O     . GLN   A 1  372 ? 11.546  99.633  71.745  1.00 36.25  ? 372 GLN   A O     1 
ATOM   2913  C  CB    A GLN   A 1  372 ? 8.465   99.878  71.574  0.58 44.86  ? 372 GLN   A CB    1 
ATOM   2914  C  CB    B GLN   A 1  372 ? 8.425   99.733  71.683  0.42 44.86  ? 372 GLN   A CB    1 
ATOM   2915  C  CG    A GLN   A 1  372 ? 7.261   100.546 70.917  0.58 49.19  ? 372 GLN   A CG    1 
ATOM   2916  C  CG    B GLN   A 1  372 ? 7.276   100.581 71.148  0.42 49.34  ? 372 GLN   A CG    1 
ATOM   2917  C  CD    A GLN   A 1  372 ? 7.621   101.777 70.089  0.58 45.05  ? 372 GLN   A CD    1 
ATOM   2918  C  CD    B GLN   A 1  372 ? 6.085   100.649 72.101  0.42 52.04  ? 372 GLN   A CD    1 
ATOM   2919  O  OE1   A GLN   A 1  372 ? 8.792   102.140 69.948  0.58 35.98  ? 372 GLN   A OE1   1 
ATOM   2920  O  OE1   B GLN   A 1  372 ? 6.136   100.145 73.227  0.42 48.89  ? 372 GLN   A OE1   1 
ATOM   2921  N  NE2   A GLN   A 1  372 ? 6.602   102.425 69.538  0.58 47.15  ? 372 GLN   A NE2   1 
ATOM   2922  N  NE2   B GLN   A 1  372 ? 5.000   101.264 71.640  0.42 55.60  ? 372 GLN   A NE2   1 
ATOM   2923  N  N     . ARG   A 1  373 ? 10.902  97.504  71.368  1.00 41.37  ? 373 ARG   A N     1 
ATOM   2924  C  CA    . ARG   A 1  373 ? 12.062  96.906  72.018  1.00 35.13  ? 373 ARG   A CA    1 
ATOM   2925  C  C     . ARG   A 1  373 ? 12.118  95.429  71.662  1.00 35.91  ? 373 ARG   A C     1 
ATOM   2926  O  O     . ARG   A 1  373 ? 11.093  94.806  71.362  1.00 31.64  ? 373 ARG   A O     1 
ATOM   2927  C  CB    . ARG   A 1  373 ? 12.021  97.087  73.545  1.00 32.62  ? 373 ARG   A CB    1 
ATOM   2928  C  CG    . ARG   A 1  373 ? 10.811  96.464  74.228  1.00 30.05  ? 373 ARG   A CG    1 
ATOM   2929  C  CD    . ARG   A 1  373 ? 10.524  97.101  75.599  1.00 34.02  ? 373 ARG   A CD    1 
ATOM   2930  N  NE    . ARG   A 1  373 ? 9.830   98.386  75.503  1.00 41.27  ? 373 ARG   A NE    1 
ATOM   2931  C  CZ    . ARG   A 1  373 ? 8.526   98.525  75.288  1.00 42.23  ? 373 ARG   A CZ    1 
ATOM   2932  N  NH1   . ARG   A 1  373 ? 7.743   97.477  75.104  1.00 38.74  ? 373 ARG   A NH1   1 
ATOM   2933  N  NH2   . ARG   A 1  373 ? 7.996   99.748  75.252  1.00 38.89  ? 373 ARG   A NH2   1 
ATOM   2934  N  N     . ALA   A 1  374 ? 13.329  94.881  71.718  1.00 33.71  ? 374 ALA   A N     1 
ATOM   2935  C  CA    . ALA   A 1  374 ? 13.585  93.507  71.332  1.00 25.04  ? 374 ALA   A CA    1 
ATOM   2936  C  C     . ALA   A 1  374 ? 14.814  93.006  72.076  1.00 27.50  ? 374 ALA   A C     1 
ATOM   2937  O  O     . ALA   A 1  374 ? 15.654  93.783  72.536  1.00 28.27  ? 374 ALA   A O     1 
ATOM   2938  C  CB    . ALA   A 1  374 ? 13.791  93.388  69.824  1.00 29.11  ? 374 ALA   A CB    1 
ATOM   2939  N  N     . VAL   A 1  375 ? 14.931  91.694  72.177  1.00 25.08  ? 375 VAL   A N     1 
ATOM   2940  C  CA    . VAL   A 1  375 ? 16.042  91.118  72.909  1.00 22.51  ? 375 VAL   A CA    1 
ATOM   2941  C  C     . VAL   A 1  375 ? 16.559  89.911  72.140  1.00 26.67  ? 375 VAL   A C     1 
ATOM   2942  O  O     . VAL   A 1  375 ? 15.786  89.173  71.519  1.00 28.01  ? 375 VAL   A O     1 
ATOM   2943  C  CB    . VAL   A 1  375 ? 15.612  90.770  74.348  1.00 22.21  ? 375 VAL   A CB    1 
ATOM   2944  C  CG1   . VAL   A 1  375 ? 14.489  89.727  74.340  1.00 24.53  ? 375 VAL   A CG1   1 
ATOM   2945  C  CG2   . VAL   A 1  375 ? 16.798  90.350  75.193  1.00 17.85  ? 375 VAL   A CG2   1 
ATOM   2946  N  N     . CYS   A 1  376 ? 17.877  89.743  72.138  1.00 28.96  ? 376 CYS   A N     1 
ATOM   2947  C  CA    . CYS   A 1  376 ? 18.509  88.491  71.753  1.00 25.21  ? 376 CYS   A CA    1 
ATOM   2948  C  C     . CYS   A 1  376 ? 19.257  87.948  72.966  1.00 22.96  ? 376 CYS   A C     1 
ATOM   2949  O  O     . CYS   A 1  376 ? 20.089  88.652  73.551  1.00 21.18  ? 376 CYS   A O     1 
ATOM   2950  C  CB    . CYS   A 1  376 ? 19.460  88.679  70.565  1.00 27.36  ? 376 CYS   A CB    1 
ATOM   2951  S  SG    . CYS   A 1  376 ? 19.995  87.099  69.823  1.00 24.83  ? 376 CYS   A SG    1 
ATOM   2952  N  N     . MET   A 1  377 ? 18.942  86.710  73.355  1.00 23.09  ? 377 MET   A N     1 
ATOM   2953  C  CA    . MET   A 1  377 ? 19.673  86.014  74.408  1.00 20.77  ? 377 MET   A CA    1 
ATOM   2954  C  C     . MET   A 1  377 ? 20.760  85.148  73.779  1.00 30.47  ? 377 MET   A C     1 
ATOM   2955  O  O     . MET   A 1  377 ? 20.576  84.592  72.691  1.00 32.07  ? 377 MET   A O     1 
ATOM   2956  C  CB    . MET   A 1  377 ? 18.727  85.155  75.247  1.00 16.32  ? 377 MET   A CB    1 
ATOM   2957  C  CG    . MET   A 1  377 ? 19.364  84.534  76.494  1.00 26.65  ? 377 MET   A CG    1 
ATOM   2958  S  SD    . MET   A 1  377 ? 18.206  83.784  77.621  1.00 24.45  ? 377 MET   A SD    1 
ATOM   2959  C  CE    . MET   A 1  377 ? 17.537  85.310  78.335  1.00 35.22  ? 377 MET   A CE    1 
ATOM   2960  N  N     . LEU   A 1  378 ? 21.909  85.058  74.441  1.00 28.96  ? 378 LEU   A N     1 
ATOM   2961  C  CA    . LEU   A 1  378 ? 22.987  84.173  74.002  1.00 22.05  ? 378 LEU   A CA    1 
ATOM   2962  C  C     . LEU   A 1  378 ? 23.353  83.261  75.167  1.00 26.94  ? 378 LEU   A C     1 
ATOM   2963  O  O     . LEU   A 1  378 ? 24.417  83.383  75.766  1.00 35.50  ? 378 LEU   A O     1 
ATOM   2964  C  CB    . LEU   A 1  378 ? 24.223  84.961  73.472  1.00 25.73  ? 378 LEU   A CB    1 
ATOM   2965  C  CG    . LEU   A 1  378 ? 24.066  85.937  72.284  1.00 29.77  ? 378 LEU   A CG    1 
ATOM   2966  C  CD1   . LEU   A 1  378 ? 25.411  86.520  71.915  1.00 33.55  ? 378 LEU   A CD1   1 
ATOM   2967  C  CD2   . LEU   A 1  378 ? 23.407  85.338  71.061  1.00 16.06  ? 378 LEU   A CD2   1 
ATOM   2968  N  N     . SER   A 1  379 ? 22.451  82.346  75.489  1.00 31.07  ? 379 SER   A N     1 
ATOM   2969  C  CA    . SER   A 1  379 ? 22.749  81.265  76.411  1.00 27.06  ? 379 SER   A CA    1 
ATOM   2970  C  C     . SER   A 1  379 ? 23.674  80.249  75.755  1.00 22.42  ? 379 SER   A C     1 
ATOM   2971  O  O     . SER   A 1  379 ? 23.554  79.976  74.561  1.00 26.19  ? 379 SER   A O     1 
ATOM   2972  C  CB    . SER   A 1  379 ? 21.451  80.581  76.838  1.00 24.87  ? 379 SER   A CB    1 
ATOM   2973  O  OG    . SER   A 1  379 ? 20.593  80.385  75.716  1.00 27.95  ? 379 SER   A OG    1 
ATOM   2974  N  N     . ASN   A 1  380 ? 24.608  79.702  76.541  1.00 23.78  ? 380 ASN   A N     1 
ATOM   2975  C  CA    . ASN   A 1  380 ? 25.399  78.515  76.193  1.00 22.58  ? 380 ASN   A CA    1 
ATOM   2976  C  C     . ASN   A 1  380 ? 24.875  77.373  77.060  1.00 26.04  ? 380 ASN   A C     1 
ATOM   2977  O  O     . ASN   A 1  380 ? 25.357  77.123  78.163  1.00 29.41  ? 380 ASN   A O     1 
ATOM   2978  C  CB    . ASN   A 1  380 ? 26.899  78.735  76.405  1.00 28.62  ? 380 ASN   A CB    1 
ATOM   2979  C  CG    . ASN   A 1  380 ? 27.748  77.542  75.960  1.00 25.82  ? 380 ASN   A CG    1 
ATOM   2980  O  OD1   . ASN   A 1  380 ? 27.326  76.400  76.058  1.00 27.01  ? 380 ASN   A OD1   1 
ATOM   2981  N  ND2   . ASN   A 1  380 ? 28.950  77.814  75.481  1.00 23.35  ? 380 ASN   A ND2   1 
ATOM   2982  N  N     . THR   A 1  381 ? 23.868  76.685  76.561  1.00 31.32  ? 381 THR   A N     1 
ATOM   2983  C  CA    . THR   A 1  381 ? 23.295  75.557  77.263  1.00 32.06  ? 381 THR   A CA    1 
ATOM   2984  C  C     . THR   A 1  381 ? 23.724  74.270  76.571  1.00 35.83  ? 381 THR   A C     1 
ATOM   2985  O  O     . THR   A 1  381 ? 23.871  74.228  75.340  1.00 27.56  ? 381 THR   A O     1 
ATOM   2986  C  CB    . THR   A 1  381 ? 21.777  75.668  77.306  1.00 21.99  ? 381 THR   A CB    1 
ATOM   2987  O  OG1   . THR   A 1  381 ? 21.201  74.453  77.823  1.00 26.84  ? 381 THR   A OG1   1 
ATOM   2988  C  CG2   . THR   A 1  381 ? 21.271  75.974  75.933  1.00 22.03  ? 381 THR   A CG2   1 
ATOM   2989  N  N     . THR   A 1  382 ? 23.969  73.239  77.385  1.00 36.01  ? 382 THR   A N     1 
ATOM   2990  C  CA    . THR   A 1  382 ? 24.279  71.925  76.853  1.00 25.27  ? 382 THR   A CA    1 
ATOM   2991  C  C     . THR   A 1  382 ? 23.126  71.378  76.032  1.00 31.37  ? 382 THR   A C     1 
ATOM   2992  O  O     . THR   A 1  382 ? 23.348  70.518  75.170  1.00 43.16  ? 382 THR   A O     1 
ATOM   2993  C  CB    . THR   A 1  382 ? 24.623  70.957  77.993  1.00 31.23  ? 382 THR   A CB    1 
ATOM   2994  O  OG1   . THR   A 1  382 ? 23.448  70.653  78.761  1.00 32.96  ? 382 THR   A OG1   1 
ATOM   2995  C  CG2   . THR   A 1  382 ? 25.668  71.567  78.900  1.00 31.30  ? 382 THR   A CG2   1 
ATOM   2996  N  N     . ALA   A 1  383 ? 21.908  71.880  76.253  1.00 20.18  ? 383 ALA   A N     1 
ATOM   2997  C  CA    . ALA   A 1  383 ? 20.752  71.377  75.523  1.00 20.78  ? 383 ALA   A CA    1 
ATOM   2998  C  C     . ALA   A 1  383 ? 20.917  71.434  74.003  1.00 22.95  ? 383 ALA   A C     1 
ATOM   2999  O  O     . ALA   A 1  383 ? 20.246  70.671  73.298  1.00 25.57  ? 383 ALA   A O     1 
ATOM   3000  C  CB    . ALA   A 1  383 ? 19.505  72.146  75.937  1.00 30.00  ? 383 ALA   A CB    1 
ATOM   3001  N  N     . ILE   A 1  384 ? 21.792  72.296  73.471  1.00 27.17  ? 384 ILE   A N     1 
ATOM   3002  C  CA    . ILE   A 1  384 ? 22.026  72.320  72.033  1.00 23.40  ? 384 ILE   A CA    1 
ATOM   3003  C  C     . ILE   A 1  384 ? 22.668  71.033  71.527  1.00 24.89  ? 384 ILE   A C     1 
ATOM   3004  O  O     . ILE   A 1  384 ? 22.700  70.796  70.310  1.00 24.32  ? 384 ILE   A O     1 
ATOM   3005  C  CB    . ILE   A 1  384 ? 22.869  73.551  71.602  1.00 25.90  ? 384 ILE   A CB    1 
ATOM   3006  C  CG1   . ILE   A 1  384 ? 22.465  73.988  70.174  1.00 22.97  ? 384 ILE   A CG1   1 
ATOM   3007  C  CG2   . ILE   A 1  384 ? 24.359  73.255  71.656  1.00 16.41  ? 384 ILE   A CG2   1 
ATOM   3008  C  CD1   . ILE   A 1  384 ? 22.943  75.377  69.760  1.00 16.38  ? 384 ILE   A CD1   1 
ATOM   3009  N  N     . ALA   A 1  385 ? 23.160  70.169  72.414  1.00 23.27  ? 385 ALA   A N     1 
ATOM   3010  C  CA    . ALA   A 1  385 ? 23.680  68.902  71.904  1.00 25.36  ? 385 ALA   A CA    1 
ATOM   3011  C  C     . ALA   A 1  385 ? 22.579  68.092  71.240  1.00 27.56  ? 385 ALA   A C     1 
ATOM   3012  O  O     . ALA   A 1  385 ? 22.858  67.279  70.351  1.00 34.85  ? 385 ALA   A O     1 
ATOM   3013  C  CB    . ALA   A 1  385 ? 24.343  68.090  73.017  1.00 28.51  ? 385 ALA   A CB    1 
ATOM   3014  N  N     . GLU   A 1  386 ? 21.325  68.294  71.651  1.00 23.23  ? 386 GLU   A N     1 
ATOM   3015  C  CA    . GLU   A 1  386 ? 20.204  67.680  70.953  1.00 19.56  ? 386 GLU   A CA    1 
ATOM   3016  C  C     . GLU   A 1  386 ? 20.425  67.760  69.444  1.00 21.71  ? 386 GLU   A C     1 
ATOM   3017  O  O     . GLU   A 1  386 ? 20.176  66.793  68.738  1.00 22.49  ? 386 GLU   A O     1 
ATOM   3018  C  CB    . GLU   A 1  386 ? 18.883  68.355  71.351  1.00 19.68  ? 386 GLU   A CB    1 
ATOM   3019  C  CG    . GLU   A 1  386 ? 18.254  67.828  72.642  1.00 25.74  ? 386 GLU   A CG    1 
ATOM   3020  C  CD    . GLU   A 1  386 ? 17.055  68.642  73.155  1.00 36.71  ? 386 GLU   A CD    1 
ATOM   3021  O  OE1   . GLU   A 1  386 ? 16.139  68.931  72.345  1.00 33.73  ? 386 GLU   A OE1   1 
ATOM   3022  O  OE2   . GLU   A 1  386 ? 17.031  68.982  74.376  1.00 37.05  ? 386 GLU   A OE2   1 
ATOM   3023  N  N     . ALA   A 1  387 ? 20.928  68.891  68.938  1.00 25.08  ? 387 ALA   A N     1 
ATOM   3024  C  CA    . ALA   A 1  387 ? 21.078  69.057  67.495  1.00 20.35  ? 387 ALA   A CA    1 
ATOM   3025  C  C     . ALA   A 1  387 ? 22.128  68.115  66.941  1.00 25.59  ? 387 ALA   A C     1 
ATOM   3026  O  O     . ALA   A 1  387 ? 22.000  67.632  65.811  1.00 24.97  ? 387 ALA   A O     1 
ATOM   3027  C  CB    . ALA   A 1  387 ? 21.456  70.489  67.156  1.00 9.52   ? 387 ALA   A CB    1 
ATOM   3028  N  N     . TRP   A 1  388 ? 23.192  67.878  67.714  1.00 27.60  ? 388 TRP   A N     1 
ATOM   3029  C  CA    . TRP   A 1  388 ? 24.249  66.965  67.303  1.00 22.31  ? 388 TRP   A CA    1 
ATOM   3030  C  C     . TRP   A 1  388 ? 23.764  65.529  67.355  1.00 24.04  ? 388 TRP   A C     1 
ATOM   3031  O  O     . TRP   A 1  388 ? 24.042  64.735  66.446  1.00 25.09  ? 388 TRP   A O     1 
ATOM   3032  C  CB    . TRP   A 1  388 ? 25.482  67.133  68.198  1.00 26.04  ? 388 TRP   A CB    1 
ATOM   3033  C  CG    . TRP   A 1  388 ? 26.181  68.486  68.142  1.00 25.31  ? 388 TRP   A CG    1 
ATOM   3034  C  CD1   . TRP   A 1  388 ? 26.601  69.230  69.204  1.00 27.56  ? 388 TRP   A CD1   1 
ATOM   3035  C  CD2   . TRP   A 1  388 ? 26.556  69.223  66.968  1.00 23.66  ? 388 TRP   A CD2   1 
ATOM   3036  N  NE1   . TRP   A 1  388 ? 27.214  70.383  68.767  1.00 28.03  ? 388 TRP   A NE1   1 
ATOM   3037  C  CE2   . TRP   A 1  388 ? 27.184  70.410  67.401  1.00 21.88  ? 388 TRP   A CE2   1 
ATOM   3038  C  CE3   . TRP   A 1  388 ? 26.418  68.997  65.595  1.00 25.81  ? 388 TRP   A CE3   1 
ATOM   3039  C  CZ2   . TRP   A 1  388 ? 27.662  71.369  66.514  1.00 24.85  ? 388 TRP   A CZ2   1 
ATOM   3040  C  CZ3   . TRP   A 1  388 ? 26.895  69.950  64.715  1.00 26.56  ? 388 TRP   A CZ3   1 
ATOM   3041  C  CH2   . TRP   A 1  388 ? 27.517  71.116  65.177  1.00 28.46  ? 388 TRP   A CH2   1 
ATOM   3042  N  N     . ALA   A 1  389 ? 23.034  65.177  68.408  1.00 19.25  ? 389 ALA   A N     1 
ATOM   3043  C  CA    . ALA   A 1  389 ? 22.534  63.814  68.504  1.00 20.97  ? 389 ALA   A CA    1 
ATOM   3044  C  C     . ALA   A 1  389 ? 21.695  63.452  67.288  1.00 24.67  ? 389 ALA   A C     1 
ATOM   3045  O  O     . ALA   A 1  389 ? 21.827  62.355  66.736  1.00 30.55  ? 389 ALA   A O     1 
ATOM   3046  C  CB    . ALA   A 1  389 ? 21.725  63.628  69.781  1.00 17.31  ? 389 ALA   A CB    1 
ATOM   3047  N  N     . ARG   A 1  390 ? 20.821  64.353  66.847  1.00 24.67  ? 390 ARG   A N     1 
ATOM   3048  C  CA    . ARG   A 1  390 ? 19.948  63.987  65.741  1.00 24.63  ? 390 ARG   A CA    1 
ATOM   3049  C  C     . ARG   A 1  390 ? 20.708  63.977  64.420  1.00 24.58  ? 390 ARG   A C     1 
ATOM   3050  O  O     . ARG   A 1  390 ? 20.517  63.076  63.601  1.00 25.26  ? 390 ARG   A O     1 
ATOM   3051  C  CB    . ARG   A 1  390 ? 18.727  64.905  65.686  1.00 20.78  ? 390 ARG   A CB    1 
ATOM   3052  C  CG    . ARG   A 1  390 ? 18.958  66.355  65.996  1.00 24.46  ? 390 ARG   A CG    1 
ATOM   3053  C  CD    . ARG   A 1  390 ? 17.608  67.016  66.262  1.00 28.22  ? 390 ARG   A CD    1 
ATOM   3054  N  NE    . ARG   A 1  390 ? 17.114  67.693  65.072  1.00 26.94  ? 390 ARG   A NE    1 
ATOM   3055  C  CZ    . ARG   A 1  390 ? 17.267  68.988  64.838  1.00 25.07  ? 390 ARG   A CZ    1 
ATOM   3056  N  NH1   . ARG   A 1  390 ? 17.839  69.786  65.724  1.00 32.74  ? 390 ARG   A NH1   1 
ATOM   3057  N  NH2   . ARG   A 1  390 ? 16.822  69.496  63.694  1.00 28.80  ? 390 ARG   A NH2   1 
ATOM   3058  N  N     . LEU   A 1  391 ? 21.591  64.948  64.200  1.00 25.39  ? 391 LEU   A N     1 
ATOM   3059  C  CA    . LEU   A 1  391 ? 22.413  64.932  62.998  1.00 18.71  ? 391 LEU   A CA    1 
ATOM   3060  C  C     . LEU   A 1  391 ? 23.307  63.699  62.962  1.00 26.02  ? 391 LEU   A C     1 
ATOM   3061  O  O     . LEU   A 1  391 ? 23.395  63.023  61.932  1.00 27.45  ? 391 LEU   A O     1 
ATOM   3062  C  CB    . LEU   A 1  391 ? 23.242  66.201  62.933  1.00 18.29  ? 391 LEU   A CB    1 
ATOM   3063  C  CG    . LEU   A 1  391 ? 23.995  66.448  61.647  1.00 24.10  ? 391 LEU   A CG    1 
ATOM   3064  C  CD1   . LEU   A 1  391 ? 22.990  66.835  60.539  1.00 20.80  ? 391 LEU   A CD1   1 
ATOM   3065  C  CD2   . LEU   A 1  391 ? 25.042  67.544  61.871  1.00 25.88  ? 391 LEU   A CD2   1 
ATOM   3066  N  N     . ASP   A 1  392 ? 23.957  63.368  64.091  1.00 22.74  ? 392 ASP   A N     1 
ATOM   3067  C  CA    . ASP   A 1  392 ? 24.806  62.171  64.151  1.00 26.54  ? 392 ASP   A CA    1 
ATOM   3068  C  C     . ASP   A 1  392 ? 24.018  60.878  63.902  1.00 24.59  ? 392 ASP   A C     1 
ATOM   3069  O  O     . ASP   A 1  392 ? 24.548  59.906  63.355  1.00 26.54  ? 392 ASP   A O     1 
ATOM   3070  C  CB    . ASP   A 1  392 ? 25.510  62.094  65.508  1.00 26.49  ? 392 ASP   A CB    1 
ATOM   3071  C  CG    . ASP   A 1  392 ? 26.633  63.100  65.652  1.00 31.26  ? 392 ASP   A CG    1 
ATOM   3072  O  OD1   . ASP   A 1  392 ? 27.033  63.747  64.667  1.00 32.85  ? 392 ASP   A OD1   1 
ATOM   3073  O  OD2   . ASP   A 1  392 ? 27.120  63.244  66.778  1.00 32.35  ? 392 ASP   A OD2   1 
ATOM   3074  N  N     . HIS   A 1  393 ? 22.763  60.831  64.327  1.00 23.10  ? 393 HIS   A N     1 
ATOM   3075  C  CA    . HIS   A 1  393 ? 21.944  59.655  64.070  1.00 21.59  ? 393 HIS   A CA    1 
ATOM   3076  C  C     . HIS   A 1  393 ? 21.705  59.467  62.574  1.00 26.39  ? 393 HIS   A C     1 
ATOM   3077  O  O     . HIS   A 1  393 ? 21.791  58.348  62.060  1.00 31.75  ? 393 HIS   A O     1 
ATOM   3078  C  CB    . HIS   A 1  393 ? 20.624  59.798  64.816  1.00 19.57  ? 393 HIS   A CB    1 
ATOM   3079  C  CG    . HIS   A 1  393 ? 19.669  58.667  64.606  1.00 26.59  ? 393 HIS   A CG    1 
ATOM   3080  N  ND1   . HIS   A 1  393 ? 19.963  57.369  64.963  1.00 32.34  ? 393 HIS   A ND1   1 
ATOM   3081  C  CD2   . HIS   A 1  393 ? 18.405  58.647  64.115  1.00 23.03  ? 393 HIS   A CD2   1 
ATOM   3082  C  CE1   . HIS   A 1  393 ? 18.923  56.599  64.695  1.00 26.83  ? 393 HIS   A CE1   1 
ATOM   3083  N  NE2   . HIS   A 1  393 ? 17.967  57.348  64.175  1.00 19.64  ? 393 HIS   A NE2   1 
ATOM   3084  N  N     . LYS   A 1  394 ? 21.377  60.551  61.859  1.00 23.13  ? 394 LYS   A N     1 
ATOM   3085  C  CA    . LYS   A 1  394 ? 21.180  60.453  60.419  1.00 21.66  ? 394 LYS   A CA    1 
ATOM   3086  C  C     . LYS   A 1  394 ? 22.452  59.988  59.737  1.00 27.11  ? 394 LYS   A C     1 
ATOM   3087  O  O     . LYS   A 1  394 ? 22.416  59.128  58.846  1.00 26.45  ? 394 LYS   A O     1 
ATOM   3088  C  CB    . LYS   A 1  394 ? 20.729  61.798  59.858  1.00 21.03  ? 394 LYS   A CB    1 
ATOM   3089  C  CG    . LYS   A 1  394 ? 19.305  62.104  60.220  1.00 20.09  ? 394 LYS   A CG    1 
ATOM   3090  C  CD    . LYS   A 1  394 ? 18.900  63.473  59.807  1.00 16.40  ? 394 LYS   A CD    1 
ATOM   3091  C  CE    . LYS   A 1  394 ? 17.422  63.659  60.068  1.00 30.56  ? 394 LYS   A CE    1 
ATOM   3092  N  NZ    . LYS   A 1  394 ? 16.634  62.483  59.559  1.00 42.44  ? 394 LYS   A NZ    1 
ATOM   3093  N  N     . PHE   A 1  395 ? 23.592  60.533  60.164  1.00 24.46  ? 395 PHE   A N     1 
ATOM   3094  C  CA    . PHE   A 1  395 ? 24.879  60.054  59.680  1.00 26.71  ? 395 PHE   A CA    1 
ATOM   3095  C  C     . PHE   A 1  395 ? 24.997  58.542  59.855  1.00 27.55  ? 395 PHE   A C     1 
ATOM   3096  O  O     . PHE   A 1  395 ? 25.341  57.820  58.909  1.00 26.88  ? 395 PHE   A O     1 
ATOM   3097  C  CB    . PHE   A 1  395 ? 25.995  60.790  60.419  1.00 26.45  ? 395 PHE   A CB    1 
ATOM   3098  C  CG    . PHE   A 1  395 ? 27.385  60.467  59.937  1.00 23.25  ? 395 PHE   A CG    1 
ATOM   3099  C  CD1   . PHE   A 1  395 ? 28.014  59.298  60.323  1.00 20.33  ? 395 PHE   A CD1   1 
ATOM   3100  C  CD2   . PHE   A 1  395 ? 28.076  61.363  59.136  1.00 29.40  ? 395 PHE   A CD2   1 
ATOM   3101  C  CE1   . PHE   A 1  395 ? 29.290  59.031  59.901  1.00 26.49  ? 395 PHE   A CE1   1 
ATOM   3102  C  CE2   . PHE   A 1  395 ? 29.358  61.090  58.701  1.00 20.46  ? 395 PHE   A CE2   1 
ATOM   3103  C  CZ    . PHE   A 1  395 ? 29.959  59.932  59.083  1.00 20.91  ? 395 PHE   A CZ    1 
ATOM   3104  N  N     . ASP   A 1  396 ? 24.673  58.046  61.058  1.00 21.89  ? 396 ASP   A N     1 
ATOM   3105  C  CA    . ASP   A 1  396 ? 24.853  56.632  61.370  1.00 23.11  ? 396 ASP   A CA    1 
ATOM   3106  C  C     . ASP   A 1  396 ? 23.977  55.740  60.483  1.00 27.55  ? 396 ASP   A C     1 
ATOM   3107  O  O     . ASP   A 1  396 ? 24.437  54.692  60.004  1.00 25.87  ? 396 ASP   A O     1 
ATOM   3108  C  CB    . ASP   A 1  396 ? 24.570  56.386  62.856  1.00 21.58  ? 396 ASP   A CB    1 
ATOM   3109  C  CG    . ASP   A 1  396 ? 25.642  56.990  63.780  1.00 30.14  ? 396 ASP   A CG    1 
ATOM   3110  O  OD1   . ASP   A 1  396 ? 26.579  57.669  63.306  1.00 31.55  ? 396 ASP   A OD1   1 
ATOM   3111  O  OD2   . ASP   A 1  396 ? 25.554  56.781  65.002  1.00 42.35  ? 396 ASP   A OD2   1 
ATOM   3112  N  N     . LEU   A 1  397 ? 22.726  56.150  60.229  1.00 25.48  ? 397 LEU   A N     1 
ATOM   3113  C  CA    . LEU   A 1  397 ? 21.819  55.334  59.424  1.00 21.08  ? 397 LEU   A CA    1 
ATOM   3114  C  C     . LEU   A 1  397 ? 22.366  55.118  58.022  1.00 22.15  ? 397 LEU   A C     1 
ATOM   3115  O  O     . LEU   A 1  397 ? 22.225  54.028  57.455  1.00 23.25  ? 397 LEU   A O     1 
ATOM   3116  C  CB    . LEU   A 1  397 ? 20.433  55.982  59.364  1.00 21.66  ? 397 LEU   A CB    1 
ATOM   3117  C  CG    . LEU   A 1  397 ? 19.606  55.870  60.652  1.00 16.98  ? 397 LEU   A CG    1 
ATOM   3118  C  CD1   . LEU   A 1  397 ? 18.457  56.852  60.708  1.00 9.68   ? 397 LEU   A CD1   1 
ATOM   3119  C  CD2   . LEU   A 1  397 ? 19.110  54.474  60.828  1.00 18.49  ? 397 LEU   A CD2   1 
ATOM   3120  N  N     . MET   A 1  398 ? 23.001  56.141  57.454  1.00 22.38  ? 398 MET   A N     1 
ATOM   3121  C  CA    . MET   A 1  398 ? 23.507  56.099  56.088  1.00 24.14  ? 398 MET   A CA    1 
ATOM   3122  C  C     . MET   A 1  398 ? 24.875  55.452  55.981  1.00 23.60  ? 398 MET   A C     1 
ATOM   3123  O  O     . MET   A 1  398 ? 25.140  54.740  55.012  1.00 24.58  ? 398 MET   A O     1 
ATOM   3124  C  CB    . MET   A 1  398 ? 23.590  57.511  55.513  1.00 22.10  ? 398 MET   A CB    1 
ATOM   3125  C  CG    . MET   A 1  398 ? 22.270  58.179  55.310  1.00 19.22  ? 398 MET   A CG    1 
ATOM   3126  S  SD    . MET   A 1  398 ? 22.473  59.250  53.901  1.00 27.05  ? 398 MET   A SD    1 
ATOM   3127  C  CE    . MET   A 1  398 ? 23.220  60.665  54.700  1.00 23.99  ? 398 MET   A CE    1 
ATOM   3128  N  N     . TYR   A 1  399 ? 25.761  55.708  56.946  1.00 27.28  ? 399 TYR   A N     1 
ATOM   3129  C  CA    . TYR   A 1  399 ? 27.122  55.201  56.838  1.00 23.23  ? 399 TYR   A CA    1 
ATOM   3130  C  C     . TYR   A 1  399 ? 27.174  53.722  57.167  1.00 19.65  ? 399 TYR   A C     1 
ATOM   3131  O  O     . TYR   A 1  399 ? 28.044  53.005  56.673  1.00 19.46  ? 399 TYR   A O     1 
ATOM   3132  C  CB    . TYR   A 1  399 ? 28.045  56.008  57.747  1.00 21.17  ? 399 TYR   A CB    1 
ATOM   3133  C  CG    . TYR   A 1  399 ? 29.528  55.795  57.544  1.00 25.09  ? 399 TYR   A CG    1 
ATOM   3134  C  CD1   . TYR   A 1  399 ? 30.195  56.407  56.494  1.00 29.07  ? 399 TYR   A CD1   1 
ATOM   3135  C  CD2   . TYR   A 1  399 ? 30.272  55.006  58.424  1.00 24.35  ? 399 TYR   A CD2   1 
ATOM   3136  C  CE1   . TYR   A 1  399 ? 31.556  56.224  56.307  1.00 29.68  ? 399 TYR   A CE1   1 
ATOM   3137  C  CE2   . TYR   A 1  399 ? 31.621  54.815  58.245  1.00 24.68  ? 399 TYR   A CE2   1 
ATOM   3138  C  CZ    . TYR   A 1  399 ? 32.264  55.433  57.187  1.00 35.35  ? 399 TYR   A CZ    1 
ATOM   3139  O  OH    . TYR   A 1  399 ? 33.623  55.263  56.999  1.00 47.02  ? 399 TYR   A OH    1 
ATOM   3140  N  N     . ALA   A 1  400 ? 26.227  53.237  57.957  1.00 19.80  ? 400 ALA   A N     1 
ATOM   3141  C  CA    . ALA   A 1  400 ? 26.156  51.802  58.195  1.00 22.46  ? 400 ALA   A CA    1 
ATOM   3142  C  C     . ALA   A 1  400 ? 25.996  51.029  56.893  1.00 16.38  ? 400 ALA   A C     1 
ATOM   3143  O  O     . ALA   A 1  400 ? 26.436  49.884  56.782  1.00 17.80  ? 400 ALA   A O     1 
ATOM   3144  C  CB    . ALA   A 1  400 ? 24.999  51.497  59.150  1.00 19.39  ? 400 ALA   A CB    1 
ATOM   3145  N  N     . LYS   A 1  401 ? 25.313  51.611  55.922  1.00 18.28  ? 401 LYS   A N     1 
ATOM   3146  C  CA    . LYS   A 1  401 ? 25.131  50.979  54.625  1.00 25.89  ? 401 LYS   A CA    1 
ATOM   3147  C  C     . LYS   A 1  401 ? 26.125  51.492  53.586  1.00 21.86  ? 401 LYS   A C     1 
ATOM   3148  O  O     . LYS   A 1  401 ? 26.150  50.995  52.453  1.00 28.29  ? 401 LYS   A O     1 
ATOM   3149  C  CB    . LYS   A 1  401 ? 23.687  51.176  54.135  1.00 16.66  ? 401 LYS   A CB    1 
ATOM   3150  C  CG    . LYS   A 1  401 ? 22.737  50.023  54.477  1.00 16.61  ? 401 LYS   A CG    1 
ATOM   3151  C  CD    . LYS   A 1  401 ? 22.399  49.940  55.980  1.00 20.70  ? 401 LYS   A CD    1 
ATOM   3152  C  CE    . LYS   A 1  401 ? 21.237  48.973  56.208  1.00 26.04  ? 401 LYS   A CE    1 
ATOM   3153  N  NZ    . LYS   A 1  401 ? 20.436  49.193  57.468  1.00 30.48  ? 401 LYS   A NZ    1 
ATOM   3154  N  N     . ARG   A 1  402 ? 26.949  52.454  53.956  1.00 17.17  ? 402 ARG   A N     1 
ATOM   3155  C  CA    . ARG   A 1  402 ? 27.917  53.097  53.094  1.00 20.92  ? 402 ARG   A CA    1 
ATOM   3156  C  C     . ARG   A 1  402 ? 27.251  53.885  51.982  1.00 23.50  ? 402 ARG   A C     1 
ATOM   3157  O  O     . ARG   A 1  402 ? 27.912  54.252  51.001  1.00 23.33  ? 402 ARG   A O     1 
ATOM   3158  C  CB    . ARG   A 1  402 ? 28.899  52.083  52.519  1.00 20.88  ? 402 ARG   A CB    1 
ATOM   3159  C  CG    . ARG   A 1  402 ? 29.947  51.630  53.518  1.00 20.78  ? 402 ARG   A CG    1 
ATOM   3160  C  CD    . ARG   A 1  402 ? 30.613  52.836  54.110  1.00 35.57  ? 402 ARG   A CD    1 
ATOM   3161  N  NE    . ARG   A 1  402 ? 31.743  52.488  54.959  1.00 37.75  ? 402 ARG   A NE    1 
ATOM   3162  C  CZ    . ARG   A 1  402 ? 31.635  52.051  56.202  1.00 33.10  ? 402 ARG   A CZ    1 
ATOM   3163  N  NH1   . ARG   A 1  402 ? 30.457  51.847  56.762  1.00 28.70  ? 402 ARG   A NH1   1 
ATOM   3164  N  NH2   . ARG   A 1  402 ? 32.741  51.805  56.898  1.00 42.75  ? 402 ARG   A NH2   1 
ATOM   3165  N  N     . ALA   A 1  403 ? 25.959  54.170  52.114  1.00 26.32  ? 403 ALA   A N     1 
ATOM   3166  C  CA    . ALA   A 1  403 ? 25.237  54.939  51.111  1.00 26.47  ? 403 ALA   A CA    1 
ATOM   3167  C  C     . ALA   A 1  403 ? 26.034  56.180  50.761  1.00 19.91  ? 403 ALA   A C     1 
ATOM   3168  O  O     . ALA   A 1  403 ? 26.565  56.838  51.648  1.00 23.33  ? 403 ALA   A O     1 
ATOM   3169  C  CB    . ALA   A 1  403 ? 23.854  55.313  51.657  1.00 25.96  ? 403 ALA   A CB    1 
ATOM   3170  N  N     . PHE   A 1  404 ? 26.186  56.447  49.462  1.00 21.92  ? 404 PHE   A N     1 
ATOM   3171  C  CA    . PHE   A 1  404 ? 26.776  57.696  48.980  1.00 15.95  ? 404 PHE   A CA    1 
ATOM   3172  C  C     . PHE   A 1  404 ? 28.268  57.887  49.239  1.00 20.20  ? 404 PHE   A C     1 
ATOM   3173  O  O     . PHE   A 1  404 ? 28.856  58.853  48.743  1.00 24.11  ? 404 PHE   A O     1 
ATOM   3174  C  CB    . PHE   A 1  404 ? 26.032  58.867  49.592  1.00 15.98  ? 404 PHE   A CB    1 
ATOM   3175  C  CG    . PHE   A 1  404 ? 24.629  58.946  49.150  1.00 26.82  ? 404 PHE   A CG    1 
ATOM   3176  C  CD1   . PHE   A 1  404 ? 24.322  59.454  47.887  1.00 20.65  ? 404 PHE   A CD1   1 
ATOM   3177  C  CD2   . PHE   A 1  404 ? 23.606  58.472  49.964  1.00 21.93  ? 404 PHE   A CD2   1 
ATOM   3178  C  CE1   . PHE   A 1  404 ? 23.022  59.517  47.462  1.00 18.40  ? 404 PHE   A CE1   1 
ATOM   3179  C  CE2   . PHE   A 1  404 ? 22.305  58.520  49.535  1.00 18.66  ? 404 PHE   A CE2   1 
ATOM   3180  C  CZ    . PHE   A 1  404 ? 22.011  59.047  48.284  1.00 18.92  ? 404 PHE   A CZ    1 
ATOM   3181  N  N     . VAL   A 1  405 ? 28.892  56.996  50.013  1.00 21.13  ? 405 VAL   A N     1 
ATOM   3182  C  CA    . VAL   A 1  405 ? 30.278  57.210  50.428  1.00 21.70  ? 405 VAL   A CA    1 
ATOM   3183  C  C     . VAL   A 1  405 ? 31.184  57.314  49.216  1.00 22.59  ? 405 VAL   A C     1 
ATOM   3184  O  O     . VAL   A 1  405 ? 32.141  58.104  49.194  1.00 24.14  ? 405 VAL   A O     1 
ATOM   3185  C  CB    . VAL   A 1  405 ? 30.738  56.078  51.378  1.00 24.09  ? 405 VAL   A CB    1 
ATOM   3186  C  CG1   . VAL   A 1  405 ? 32.168  56.256  51.743  1.00 29.35  ? 405 VAL   A CG1   1 
ATOM   3187  C  CG2   . VAL   A 1  405 ? 29.885  56.032  52.628  1.00 20.36  ? 405 VAL   A CG2   1 
ATOM   3188  N  N     . HIS   A 1  406 ? 30.888  56.538  48.178  1.00 25.95  ? 406 HIS   A N     1 
ATOM   3189  C  CA    . HIS   A 1  406 ? 31.754  56.510  47.013  1.00 22.58  ? 406 HIS   A CA    1 
ATOM   3190  C  C     . HIS   A 1  406 ? 31.891  57.883  46.355  1.00 21.74  ? 406 HIS   A C     1 
ATOM   3191  O  O     . HIS   A 1  406 ? 32.876  58.113  45.646  1.00 28.50  ? 406 HIS   A O     1 
ATOM   3192  C  CB    . HIS   A 1  406 ? 31.226  55.461  46.026  1.00 20.68  ? 406 HIS   A CB    1 
ATOM   3193  C  CG    . HIS   A 1  406 ? 29.859  55.771  45.498  1.00 23.58  ? 406 HIS   A CG    1 
ATOM   3194  N  ND1   . HIS   A 1  406 ? 29.643  56.250  44.222  1.00 19.70  ? 406 HIS   A ND1   1 
ATOM   3195  C  CD2   . HIS   A 1  406 ? 28.644  55.704  46.088  1.00 20.42  ? 406 HIS   A CD2   1 
ATOM   3196  C  CE1   . HIS   A 1  406 ? 28.354  56.462  44.051  1.00 21.13  ? 406 HIS   A CE1   1 
ATOM   3197  N  NE2   . HIS   A 1  406 ? 27.726  56.135  45.167  1.00 20.07  ? 406 HIS   A NE2   1 
ATOM   3198  N  N     . TRP   A 1  407 ? 30.945  58.807  46.561  1.00 17.62  ? 407 TRP   A N     1 
ATOM   3199  C  CA    . TRP   A 1  407 ? 31.100  60.120  45.926  1.00 22.78  ? 407 TRP   A CA    1 
ATOM   3200  C  C     . TRP   A 1  407 ? 32.248  60.900  46.556  1.00 24.31  ? 407 TRP   A C     1 
ATOM   3201  O  O     . TRP   A 1  407 ? 32.964  61.636  45.865  1.00 17.50  ? 407 TRP   A O     1 
ATOM   3202  C  CB    . TRP   A 1  407 ? 29.804  60.944  45.999  1.00 15.79  ? 407 TRP   A CB    1 
ATOM   3203  C  CG    . TRP   A 1  407 ? 28.682  60.469  45.122  1.00 19.14  ? 407 TRP   A CG    1 
ATOM   3204  C  CD1   . TRP   A 1  407 ? 27.570  59.799  45.523  1.00 19.57  ? 407 TRP   A CD1   1 
ATOM   3205  C  CD2   . TRP   A 1  407 ? 28.566  60.619  43.693  1.00 17.80  ? 407 TRP   A CD2   1 
ATOM   3206  N  NE1   . TRP   A 1  407 ? 26.761  59.544  44.444  1.00 21.79  ? 407 TRP   A NE1   1 
ATOM   3207  C  CE2   . TRP   A 1  407 ? 27.356  60.027  43.310  1.00 23.97  ? 407 TRP   A CE2   1 
ATOM   3208  C  CE3   . TRP   A 1  407 ? 29.365  61.189  42.713  1.00 16.14  ? 407 TRP   A CE3   1 
ATOM   3209  C  CZ2   . TRP   A 1  407 ? 26.929  59.989  41.979  1.00 34.64  ? 407 TRP   A CZ2   1 
ATOM   3210  C  CZ3   . TRP   A 1  407 ? 28.944  61.150  41.398  1.00 18.21  ? 407 TRP   A CZ3   1 
ATOM   3211  C  CH2   . TRP   A 1  407 ? 27.743  60.553  41.039  1.00 26.65  ? 407 TRP   A CH2   1 
ATOM   3212  N  N     . TYR   A 1  408 ? 32.421  60.760  47.876  1.00 26.79  ? 408 TYR   A N     1 
ATOM   3213  C  CA    . TYR   A 1  408 ? 33.493  61.439  48.586  1.00 22.89  ? 408 TYR   A CA    1 
ATOM   3214  C  C     . TYR   A 1  408 ? 34.812  60.725  48.348  1.00 28.15  ? 408 TYR   A C     1 
ATOM   3215  O  O     . TYR   A 1  408 ? 35.836  61.367  48.079  1.00 23.85  ? 408 TYR   A O     1 
ATOM   3216  C  CB    . TYR   A 1  408 ? 33.170  61.497  50.081  1.00 26.22  ? 408 TYR   A CB    1 
ATOM   3217  C  CG    . TYR   A 1  408 ? 31.876  62.210  50.434  1.00 25.68  ? 408 TYR   A CG    1 
ATOM   3218  C  CD1   . TYR   A 1  408 ? 31.830  63.595  50.521  1.00 31.61  ? 408 TYR   A CD1   1 
ATOM   3219  C  CD2   . TYR   A 1  408 ? 30.712  61.509  50.692  1.00 24.19  ? 408 TYR   A CD2   1 
ATOM   3220  C  CE1   . TYR   A 1  408 ? 30.663  64.273  50.838  1.00 27.59  ? 408 TYR   A CE1   1 
ATOM   3221  C  CE2   . TYR   A 1  408 ? 29.527  62.179  51.017  1.00 28.68  ? 408 TYR   A CE2   1 
ATOM   3222  C  CZ    . TYR   A 1  408 ? 29.514  63.564  51.083  1.00 30.04  ? 408 TYR   A CZ    1 
ATOM   3223  O  OH    . TYR   A 1  408 ? 28.367  64.255  51.399  1.00 25.31  ? 408 TYR   A OH    1 
ATOM   3224  N  N     . VAL   A 1  409 ? 34.787  59.392  48.416  1.00 24.37  ? 409 VAL   A N     1 
ATOM   3225  C  CA    . VAL   A 1  409 ? 35.988  58.606  48.158  1.00 24.29  ? 409 VAL   A CA    1 
ATOM   3226  C  C     . VAL   A 1  409 ? 36.506  58.862  46.748  1.00 25.72  ? 409 VAL   A C     1 
ATOM   3227  O  O     . VAL   A 1  409 ? 37.706  59.064  46.534  1.00 29.13  ? 409 VAL   A O     1 
ATOM   3228  C  CB    . VAL   A 1  409 ? 35.697  57.118  48.383  1.00 18.37  ? 409 VAL   A CB    1 
ATOM   3229  C  CG1   . VAL   A 1  409 ? 36.773  56.309  47.756  1.00 19.70  ? 409 VAL   A CG1   1 
ATOM   3230  C  CG2   . VAL   A 1  409 ? 35.597  56.833  49.839  1.00 15.45  ? 409 VAL   A CG2   1 
ATOM   3231  N  N     . GLY   A 1  410 ? 35.614  58.850  45.764  1.00 21.22  ? 410 GLY   A N     1 
ATOM   3232  C  CA    . GLY   A 1  410 ? 36.031  59.088  44.406  1.00 25.03  ? 410 GLY   A CA    1 
ATOM   3233  C  C     . GLY   A 1  410 ? 36.682  60.429  44.195  1.00 26.48  ? 410 GLY   A C     1 
ATOM   3234  O  O     . GLY   A 1  410 ? 37.331  60.639  43.164  1.00 37.20  ? 410 GLY   A O     1 
ATOM   3235  N  N     . GLU   A 1  411 ? 36.514  61.353  45.129  1.00 28.48  ? 411 GLU   A N     1 
ATOM   3236  C  CA    . GLU   A 1  411 ? 37.221  62.621  45.037  1.00 34.59  ? 411 GLU   A CA    1 
ATOM   3237  C  C     . GLU   A 1  411 ? 38.581  62.581  45.740  1.00 37.94  ? 411 GLU   A C     1 
ATOM   3238  O  O     . GLU   A 1  411 ? 39.350  63.547  45.655  1.00 40.51  ? 411 GLU   A O     1 
ATOM   3239  C  CB    . GLU   A 1  411 ? 36.336  63.738  45.587  1.00 24.00  ? 411 GLU   A CB    1 
ATOM   3240  C  CG    . GLU   A 1  411 ? 35.116  64.009  44.727  1.00 21.44  ? 411 GLU   A CG    1 
ATOM   3241  C  CD    . GLU   A 1  411 ? 35.433  64.839  43.500  1.00 29.61  ? 411 GLU   A CD    1 
ATOM   3242  O  OE1   . GLU   A 1  411 ? 36.640  65.027  43.225  1.00 29.58  ? 411 GLU   A OE1   1 
ATOM   3243  O  OE2   . GLU   A 1  411 ? 34.487  65.317  42.820  1.00 29.87  ? 411 GLU   A OE2   1 
ATOM   3244  N  N     . GLY   A 1  412 ? 38.913  61.465  46.381  1.00 27.77  ? 412 GLY   A N     1 
ATOM   3245  C  CA    . GLY   A 1  412 ? 40.179  61.278  47.048  1.00 33.46  ? 412 GLY   A CA    1 
ATOM   3246  C  C     . GLY   A 1  412 ? 40.049  61.117  48.541  1.00 37.35  ? 412 GLY   A C     1 
ATOM   3247  O  O     . GLY   A 1  412 ? 40.932  60.525  49.167  1.00 46.97  ? 412 GLY   A O     1 
ATOM   3248  N  N     . MET   A 1  413 ? 38.970  61.630  49.125  1.00 29.55  ? 413 MET   A N     1 
ATOM   3249  C  CA    . MET   A 1  413 ? 38.719  61.463  50.543  1.00 25.66  ? 413 MET   A CA    1 
ATOM   3250  C  C     . MET   A 1  413 ? 38.755  59.986  50.933  1.00 28.28  ? 413 MET   A C     1 
ATOM   3251  O  O     . MET   A 1  413 ? 38.232  59.120  50.234  1.00 29.81  ? 413 MET   A O     1 
ATOM   3252  C  CB    . MET   A 1  413 ? 37.363  62.088  50.888  1.00 27.50  ? 413 MET   A CB    1 
ATOM   3253  C  CG    . MET   A 1  413 ? 37.361  62.926  52.150  1.00 30.11  ? 413 MET   A CG    1 
ATOM   3254  S  SD    . MET   A 1  413 ? 35.756  63.106  52.966  1.00 32.74  ? 413 MET   A SD    1 
ATOM   3255  C  CE    . MET   A 1  413 ? 35.425  61.433  53.487  1.00 26.94  ? 413 MET   A CE    1 
ATOM   3256  N  N     . GLU   A 1  414 ? 39.364  59.694  52.065  1.00 32.91  ? 414 GLU   A N     1 
ATOM   3257  C  CA    . GLU   A 1  414 ? 39.498  58.315  52.490  1.00 31.72  ? 414 GLU   A CA    1 
ATOM   3258  C  C     . GLU   A 1  414 ? 38.382  57.931  53.443  1.00 31.47  ? 414 GLU   A C     1 
ATOM   3259  O  O     . GLU   A 1  414 ? 38.013  58.690  54.339  1.00 32.93  ? 414 GLU   A O     1 
ATOM   3260  C  CB    . GLU   A 1  414 ? 40.846  58.086  53.167  1.00 43.47  ? 414 GLU   A CB    1 
ATOM   3261  C  CG    . GLU   A 1  414 ? 42.041  58.758  52.485  1.00 47.61  ? 414 GLU   A CG    1 
ATOM   3262  C  CD    . GLU   A 1  414 ? 43.335  58.413  53.198  1.00 65.00  ? 414 GLU   A CD    1 
ATOM   3263  O  OE1   . GLU   A 1  414 ? 43.642  57.199  53.274  1.00 60.19  ? 414 GLU   A OE1   1 
ATOM   3264  O  OE2   . GLU   A 1  414 ? 44.015  59.339  53.712  1.00 65.32  ? 414 GLU   A OE2   1 
ATOM   3265  N  N     . GLU   A 1  415 ? 37.872  56.724  53.258  1.00 28.49  ? 415 GLU   A N     1 
ATOM   3266  C  CA    . GLU   A 1  415 ? 36.763  56.260  54.064  1.00 27.41  ? 415 GLU   A CA    1 
ATOM   3267  C  C     . GLU   A 1  415 ? 36.960  56.571  55.536  1.00 38.88  ? 415 GLU   A C     1 
ATOM   3268  O  O     . GLU   A 1  415 ? 35.985  56.799  56.260  1.00 46.61  ? 415 GLU   A O     1 
ATOM   3269  C  CB    . GLU   A 1  415 ? 36.601  54.761  53.865  1.00 32.08  ? 415 GLU   A CB    1 
ATOM   3270  C  CG    . GLU   A 1  415 ? 35.364  54.178  54.471  1.00 37.28  ? 415 GLU   A CG    1 
ATOM   3271  C  CD    . GLU   A 1  415 ? 34.645  53.297  53.477  1.00 48.68  ? 415 GLU   A CD    1 
ATOM   3272  O  OE1   . GLU   A 1  415 ? 34.666  53.652  52.275  1.00 43.33  ? 415 GLU   A OE1   1 
ATOM   3273  O  OE2   . GLU   A 1  415 ? 34.094  52.245  53.887  1.00 52.21  ? 415 GLU   A OE2   1 
ATOM   3274  N  N     . GLY   A 1  416 ? 38.205  56.574  56.009  1.00 31.31  ? 416 GLY   A N     1 
ATOM   3275  C  CA    . GLY   A 1  416 ? 38.432  56.746  57.431  1.00 22.04  ? 416 GLY   A CA    1 
ATOM   3276  C  C     . GLY   A 1  416 ? 38.119  58.142  57.923  1.00 31.17  ? 416 GLY   A C     1 
ATOM   3277  O  O     . GLY   A 1  416 ? 37.664  58.311  59.052  1.00 38.47  ? 416 GLY   A O     1 
ATOM   3278  N  N     . GLU   A 1  417 ? 38.354  59.163  57.093  1.00 31.61  ? 417 GLU   A N     1 
ATOM   3279  C  CA    . GLU   A 1  417 ? 37.968  60.515  57.483  1.00 26.85  ? 417 GLU   A CA    1 
ATOM   3280  C  C     . GLU   A 1  417 ? 36.488  60.604  57.811  1.00 35.95  ? 417 GLU   A C     1 
ATOM   3281  O  O     . GLU   A 1  417 ? 36.065  61.556  58.474  1.00 45.16  ? 417 GLU   A O     1 
ATOM   3282  C  CB    . GLU   A 1  417 ? 38.305  61.519  56.384  1.00 23.90  ? 417 GLU   A CB    1 
ATOM   3283  C  CG    . GLU   A 1  417 ? 37.808  62.921  56.684  1.00 19.41  ? 417 GLU   A CG    1 
ATOM   3284  C  CD    . GLU   A 1  417 ? 38.344  63.942  55.717  1.00 29.49  ? 417 GLU   A CD    1 
ATOM   3285  O  OE1   . GLU   A 1  417 ? 39.043  63.534  54.761  1.00 27.89  ? 417 GLU   A OE1   1 
ATOM   3286  O  OE2   . GLU   A 1  417 ? 38.072  65.152  55.907  1.00 40.36  ? 417 GLU   A OE2   1 
ATOM   3287  N  N     . PHE   A 1  418 ? 35.688  59.648  57.340  1.00 37.04  ? 418 PHE   A N     1 
ATOM   3288  C  CA    . PHE   A 1  418 ? 34.305  59.558  57.783  1.00 28.86  ? 418 PHE   A CA    1 
ATOM   3289  C  C     . PHE   A 1  418 ? 34.239  59.101  59.238  1.00 30.93  ? 418 PHE   A C     1 
ATOM   3290  O  O     . PHE   A 1  418 ? 33.571  59.731  60.065  1.00 36.13  ? 418 PHE   A O     1 
ATOM   3291  C  CB    . PHE   A 1  418 ? 33.518  58.602  56.881  1.00 24.28  ? 418 PHE   A CB    1 
ATOM   3292  C  CG    . PHE   A 1  418 ? 32.880  59.249  55.673  1.00 20.79  ? 418 PHE   A CG    1 
ATOM   3293  C  CD1   . PHE   A 1  418 ? 31.642  59.833  55.753  1.00 20.44  ? 418 PHE   A CD1   1 
ATOM   3294  C  CD2   . PHE   A 1  418 ? 33.490  59.204  54.436  1.00 34.14  ? 418 PHE   A CD2   1 
ATOM   3295  C  CE1   . PHE   A 1  418 ? 31.045  60.413  54.641  1.00 20.06  ? 418 PHE   A CE1   1 
ATOM   3296  C  CE2   . PHE   A 1  418 ? 32.888  59.772  53.317  1.00 30.09  ? 418 PHE   A CE2   1 
ATOM   3297  C  CZ    . PHE   A 1  418 ? 31.670  60.381  53.430  1.00 25.89  ? 418 PHE   A CZ    1 
ATOM   3298  N  N     . SER   A 1  419 ? 34.926  58.008  59.582  1.00 26.88  ? 419 SER   A N     1 
ATOM   3299  C  CA    . SER   A 1  419 ? 34.759  57.478  60.937  1.00 30.07  ? 419 SER   A CA    1 
ATOM   3300  C  C     . SER   A 1  419 ? 35.463  58.352  61.967  1.00 40.69  ? 419 SER   A C     1 
ATOM   3301  O  O     . SER   A 1  419 ? 34.966  58.505  63.092  1.00 43.86  ? 419 SER   A O     1 
ATOM   3302  C  CB    . SER   A 1  419 ? 35.255  56.032  61.031  1.00 27.30  ? 419 SER   A CB    1 
ATOM   3303  O  OG    . SER   A 1  419 ? 36.308  55.781  60.107  1.00 46.21  ? 419 SER   A OG    1 
ATOM   3304  N  N     . GLU   A 1  420 ? 36.611  58.936  61.607  1.00 36.29  ? 420 GLU   A N     1 
ATOM   3305  C  CA    A GLU   A 1  420 ? 37.303  59.835  62.521  0.61 33.29  ? 420 GLU   A CA    1 
ATOM   3306  C  CA    B GLU   A 1  420 ? 37.292  59.820  62.542  0.39 33.30  ? 420 GLU   A CA    1 
ATOM   3307  C  C     . GLU   A 1  420 ? 36.528  61.136  62.706  1.00 34.82  ? 420 GLU   A C     1 
ATOM   3308  O  O     . GLU   A 1  420 ? 36.511  61.704  63.805  1.00 38.97  ? 420 GLU   A O     1 
ATOM   3309  C  CB    A GLU   A 1  420 ? 38.722  60.108  62.012  0.61 32.45  ? 420 GLU   A CB    1 
ATOM   3310  C  CB    B GLU   A 1  420 ? 38.746  60.041  62.090  0.39 32.44  ? 420 GLU   A CB    1 
ATOM   3311  C  CG    A GLU   A 1  420 ? 38.898  61.403  61.227  0.61 32.76  ? 420 GLU   A CG    1 
ATOM   3312  C  CG    B GLU   A 1  420 ? 39.792  59.882  63.217  0.39 32.39  ? 420 GLU   A CG    1 
ATOM   3313  C  CD    A GLU   A 1  420 ? 40.353  61.699  60.962  0.61 27.85  ? 420 GLU   A CD    1 
ATOM   3314  C  CD    B GLU   A 1  420 ? 40.992  59.005  62.845  0.39 28.74  ? 420 GLU   A CD    1 
ATOM   3315  O  OE1   A GLU   A 1  420 ? 41.095  60.721  60.740  0.61 28.16  ? 420 GLU   A OE1   1 
ATOM   3316  O  OE1   B GLU   A 1  420 ? 41.071  58.539  61.688  0.39 26.39  ? 420 GLU   A OE1   1 
ATOM   3317  O  OE2   A GLU   A 1  420 ? 40.748  62.888  60.993  0.61 19.44  ? 420 GLU   A OE2   1 
ATOM   3318  O  OE2   B GLU   A 1  420 ? 41.856  58.779  63.725  0.39 24.36  ? 420 GLU   A OE2   1 
ATOM   3319  N  N     . ALA   A 1  421 ? 35.863  61.619  61.651  1.00 35.23  ? 421 ALA   A N     1 
ATOM   3320  C  CA    . ALA   A 1  421 ? 34.972  62.765  61.809  1.00 34.61  ? 421 ALA   A CA    1 
ATOM   3321  C  C     . ALA   A 1  421 ? 33.829  62.424  62.750  1.00 35.19  ? 421 ALA   A C     1 
ATOM   3322  O  O     . ALA   A 1  421 ? 33.536  63.172  63.686  1.00 36.46  ? 421 ALA   A O     1 
ATOM   3323  C  CB    . ALA   A 1  421 ? 34.423  63.216  60.458  1.00 29.42  ? 421 ALA   A CB    1 
ATOM   3324  N  N     . ARG   A 1  422 ? 33.171  61.285  62.522  1.00 31.78  ? 422 ARG   A N     1 
ATOM   3325  C  CA    . ARG   A 1  422 ? 32.028  60.909  63.352  1.00 28.23  ? 422 ARG   A CA    1 
ATOM   3326  C  C     . ARG   A 1  422 ? 32.451  60.617  64.778  1.00 33.52  ? 422 ARG   A C     1 
ATOM   3327  O  O     . ARG   A 1  422 ? 31.727  60.945  65.723  1.00 36.72  ? 422 ARG   A O     1 
ATOM   3328  C  CB    . ARG   A 1  422 ? 31.317  59.693  62.764  1.00 25.57  ? 422 ARG   A CB    1 
ATOM   3329  C  CG    . ARG   A 1  422 ? 30.276  59.071  63.679  1.00 20.26  ? 422 ARG   A CG    1 
ATOM   3330  C  CD    . ARG   A 1  422 ? 29.071  59.990  63.845  1.00 26.26  ? 422 ARG   A CD    1 
ATOM   3331  N  NE    . ARG   A 1  422 ? 27.993  59.351  64.589  1.00 29.02  ? 422 ARG   A NE    1 
ATOM   3332  C  CZ    . ARG   A 1  422 ? 27.912  59.321  65.915  1.00 37.11  ? 422 ARG   A CZ    1 
ATOM   3333  N  NH1   . ARG   A 1  422 ? 28.822  59.908  66.679  1.00 30.25  ? 422 ARG   A NH1   1 
ATOM   3334  N  NH2   . ARG   A 1  422 ? 26.893  58.686  66.489  1.00 35.35  ? 422 ARG   A NH2   1 
ATOM   3335  N  N     . GLU   A 1  423 ? 33.605  59.969  64.956  1.00 43.40  ? 423 GLU   A N     1 
ATOM   3336  C  CA    . GLU   A 1  423 ? 34.064  59.642  66.303  1.00 37.77  ? 423 GLU   A CA    1 
ATOM   3337  C  C     . GLU   A 1  423 ? 34.330  60.906  67.115  1.00 34.26  ? 423 GLU   A C     1 
ATOM   3338  O  O     . GLU   A 1  423 ? 34.035  60.956  68.314  1.00 36.94  ? 423 GLU   A O     1 
ATOM   3339  C  CB    . GLU   A 1  423 ? 35.310  58.758  66.233  1.00 33.14  ? 423 GLU   A CB    1 
ATOM   3340  C  CG    . GLU   A 1  423 ? 35.811  58.293  67.612  1.00 56.42  ? 423 GLU   A CG    1 
ATOM   3341  C  CD    . GLU   A 1  423 ? 34.710  57.721  68.520  1.00 60.86  ? 423 GLU   A CD    1 
ATOM   3342  O  OE1   . GLU   A 1  423 ? 34.202  56.616  68.222  1.00 57.85  ? 423 GLU   A OE1   1 
ATOM   3343  O  OE2   . GLU   A 1  423 ? 34.358  58.375  69.534  1.00 50.77  ? 423 GLU   A OE2   1 
ATOM   3344  N  N     . ASP   A 1  424 ? 34.876  61.941  66.473  1.00 28.58  ? 424 ASP   A N     1 
ATOM   3345  C  CA    . ASP   A 1  424 ? 35.021  63.240  67.117  1.00 25.26  ? 424 ASP   A CA    1 
ATOM   3346  C  C     . ASP   A 1  424 ? 33.671  63.780  67.579  1.00 29.53  ? 424 ASP   A C     1 
ATOM   3347  O  O     . ASP   A 1  424 ? 33.568  64.400  68.644  1.00 32.01  ? 424 ASP   A O     1 
ATOM   3348  C  CB    . ASP   A 1  424 ? 35.692  64.208  66.138  1.00 30.05  ? 424 ASP   A CB    1 
ATOM   3349  C  CG    . ASP   A 1  424 ? 36.078  65.516  66.777  1.00 33.24  ? 424 ASP   A CG    1 
ATOM   3350  O  OD1   . ASP   A 1  424 ? 36.072  65.574  68.018  1.00 39.77  ? 424 ASP   A OD1   1 
ATOM   3351  O  OD2   . ASP   A 1  424 ? 36.395  66.484  66.045  1.00 45.94  ? 424 ASP   A OD2   1 
ATOM   3352  N  N     . MET   A 1  425 ? 32.624  63.572  66.780  1.00 27.79  ? 425 MET   A N     1 
ATOM   3353  C  CA    . MET   A 1  425 ? 31.295  64.012  67.179  1.00 21.71  ? 425 MET   A CA    1 
ATOM   3354  C  C     . MET   A 1  425 ? 30.839  63.283  68.431  1.00 29.04  ? 425 MET   A C     1 
ATOM   3355  O  O     . MET   A 1  425 ? 30.133  63.846  69.276  1.00 31.25  ? 425 MET   A O     1 
ATOM   3356  C  CB    . MET   A 1  425 ? 30.304  63.766  66.047  1.00 27.28  ? 425 MET   A CB    1 
ATOM   3357  C  CG    . MET   A 1  425 ? 30.564  64.572  64.810  1.00 29.77  ? 425 MET   A CG    1 
ATOM   3358  S  SD    . MET   A 1  425 ? 30.450  66.293  65.192  1.00 31.41  ? 425 MET   A SD    1 
ATOM   3359  C  CE    . MET   A 1  425 ? 28.919  66.319  66.086  1.00 25.78  ? 425 MET   A CE    1 
ATOM   3360  N  N     . ALA   A 1  426 ? 31.193  62.010  68.550  1.00 35.52  ? 426 ALA   A N     1 
ATOM   3361  C  CA    . ALA   A 1  426 ? 30.805  61.277  69.742  1.00 30.08  ? 426 ALA   A CA    1 
ATOM   3362  C  C     . ALA   A 1  426 ? 31.502  61.854  70.970  1.00 34.46  ? 426 ALA   A C     1 
ATOM   3363  O  O     . ALA   A 1  426 ? 30.871  62.051  72.015  1.00 38.70  ? 426 ALA   A O     1 
ATOM   3364  C  CB    . ALA   A 1  426 ? 31.117  59.801  69.541  1.00 27.02  ? 426 ALA   A CB    1 
ATOM   3365  N  N     . ALA   A 1  427 ? 32.799  62.147  70.858  1.00 29.96  ? 427 ALA   A N     1 
ATOM   3366  C  CA    . ALA   A 1  427 ? 33.483  62.936  71.877  1.00 34.48  ? 427 ALA   A CA    1 
ATOM   3367  C  C     . ALA   A 1  427 ? 32.685  64.184  72.227  1.00 29.47  ? 427 ALA   A C     1 
ATOM   3368  O  O     . ALA   A 1  427 ? 32.345  64.418  73.384  1.00 27.08  ? 427 ALA   A O     1 
ATOM   3369  C  CB    . ALA   A 1  427 ? 34.876  63.322  71.385  1.00 37.34  ? 427 ALA   A CB    1 
ATOM   3370  N  N     . LEU   A 1  428 ? 32.361  64.988  71.216  1.00 35.58  ? 428 LEU   A N     1 
ATOM   3371  C  CA    . LEU   A 1  428 ? 31.582  66.205  71.431  1.00 32.48  ? 428 LEU   A CA    1 
ATOM   3372  C  C     . LEU   A 1  428 ? 30.307  65.935  72.226  1.00 31.66  ? 428 LEU   A C     1 
ATOM   3373  O  O     . LEU   A 1  428 ? 30.036  66.610  73.222  1.00 37.38  ? 428 LEU   A O     1 
ATOM   3374  C  CB    . LEU   A 1  428 ? 31.241  66.848  70.089  1.00 26.21  ? 428 LEU   A CB    1 
ATOM   3375  C  CG    . LEU   A 1  428 ? 30.618  68.228  70.214  1.00 31.68  ? 428 LEU   A CG    1 
ATOM   3376  C  CD1   . LEU   A 1  428 ? 31.701  69.196  70.659  1.00 30.66  ? 428 LEU   A CD1   1 
ATOM   3377  C  CD2   . LEU   A 1  428 ? 29.930  68.660  68.904  1.00 27.82  ? 428 LEU   A CD2   1 
ATOM   3378  N  N     . GLU   A 1  429 ? 29.485  64.973  71.781  1.00 34.63  ? 429 GLU   A N     1 
ATOM   3379  C  CA    . GLU   A 1  429 ? 28.252  64.685  72.512  1.00 30.67  ? 429 GLU   A CA    1 
ATOM   3380  C  C     . GLU   A 1  429 ? 28.560  64.238  73.932  1.00 37.85  ? 429 GLU   A C     1 
ATOM   3381  O  O     . GLU   A 1  429 ? 27.794  64.535  74.851  1.00 42.60  ? 429 GLU   A O     1 
ATOM   3382  C  CB    . GLU   A 1  429 ? 27.413  63.619  71.793  1.00 20.68  ? 429 GLU   A CB    1 
ATOM   3383  C  CG    . GLU   A 1  429 ? 26.887  64.009  70.396  1.00 25.39  ? 429 GLU   A CG    1 
ATOM   3384  C  CD    . GLU   A 1  429 ? 25.749  63.080  69.893  1.00 41.70  ? 429 GLU   A CD    1 
ATOM   3385  O  OE1   . GLU   A 1  429 ? 24.749  62.896  70.641  1.00 36.89  ? 429 GLU   A OE1   1 
ATOM   3386  O  OE2   . GLU   A 1  429 ? 25.859  62.518  68.759  1.00 37.30  ? 429 GLU   A OE2   1 
ATOM   3387  N  N     . LYS   A 1  430 ? 29.694  63.555  74.135  1.00 38.99  ? 430 LYS   A N     1 
ATOM   3388  C  CA    . LYS   A 1  430 ? 30.052  63.047  75.459  1.00 39.62  ? 430 LYS   A CA    1 
ATOM   3389  C  C     . LYS   A 1  430 ? 30.376  64.190  76.418  1.00 40.08  ? 430 LYS   A C     1 
ATOM   3390  O  O     . LYS   A 1  430 ? 29.898  64.208  77.558  1.00 40.56  ? 430 LYS   A O     1 
ATOM   3391  C  CB    . LYS   A 1  430 ? 31.242  62.083  75.348  1.00 46.80  ? 430 LYS   A CB    1 
ATOM   3392  C  CG    . LYS   A 1  430 ? 31.557  61.310  76.641  1.00 57.12  ? 430 LYS   A CG    1 
ATOM   3393  C  CD    . LYS   A 1  430 ? 32.942  60.625  76.633  1.00 56.04  ? 430 LYS   A CD    1 
ATOM   3394  C  CE    . LYS   A 1  430 ? 32.967  59.346  75.795  1.00 53.70  ? 430 LYS   A CE    1 
ATOM   3395  N  NZ    . LYS   A 1  430 ? 33.888  58.328  76.369  1.00 57.83  ? 430 LYS   A NZ    1 
ATOM   3396  N  N     . ASP   A 1  431 ? 31.202  65.145  75.972  1.00 36.42  ? 431 ASP   A N     1 
ATOM   3397  C  CA    . ASP   A 1  431 ? 31.508  66.319  76.784  1.00 37.81  ? 431 ASP   A CA    1 
ATOM   3398  C  C     . ASP   A 1  431 ? 30.234  67.060  77.182  1.00 41.59  ? 431 ASP   A C     1 
ATOM   3399  O  O     . ASP   A 1  431 ? 30.076  67.465  78.342  1.00 38.27  ? 431 ASP   A O     1 
ATOM   3400  C  CB    . ASP   A 1  431 ? 32.444  67.276  76.034  1.00 35.00  ? 431 ASP   A CB    1 
ATOM   3401  C  CG    . ASP   A 1  431 ? 33.584  66.574  75.314  1.00 42.22  ? 431 ASP   A CG    1 
ATOM   3402  O  OD1   . ASP   A 1  431 ? 34.078  65.530  75.805  1.00 51.76  ? 431 ASP   A OD1   1 
ATOM   3403  O  OD2   . ASP   A 1  431 ? 33.999  67.090  74.248  1.00 39.42  ? 431 ASP   A OD2   1 
ATOM   3404  N  N     . TYR   A 1  432 ? 29.324  67.285  76.221  1.00 39.23  ? 432 TYR   A N     1 
ATOM   3405  C  CA    . TYR   A 1  432 ? 28.078  67.966  76.554  1.00 37.29  ? 432 TYR   A CA    1 
ATOM   3406  C  C     . TYR   A 1  432 ? 27.348  67.213  77.654  1.00 40.36  ? 432 TYR   A C     1 
ATOM   3407  O  O     . TYR   A 1  432 ? 26.717  67.824  78.526  1.00 45.29  ? 432 TYR   A O     1 
ATOM   3408  C  CB    . TYR   A 1  432 ? 27.184  68.127  75.319  1.00 31.16  ? 432 TYR   A CB    1 
ATOM   3409  C  CG    . TYR   A 1  432 ? 27.455  69.368  74.478  1.00 31.95  ? 432 TYR   A CG    1 
ATOM   3410  C  CD1   . TYR   A 1  432 ? 26.866  70.583  74.782  1.00 34.43  ? 432 TYR   A CD1   1 
ATOM   3411  C  CD2   . TYR   A 1  432 ? 28.266  69.312  73.350  1.00 31.31  ? 432 TYR   A CD2   1 
ATOM   3412  C  CE1   . TYR   A 1  432 ? 27.101  71.712  74.004  1.00 29.63  ? 432 TYR   A CE1   1 
ATOM   3413  C  CE2   . TYR   A 1  432 ? 28.498  70.440  72.561  1.00 31.91  ? 432 TYR   A CE2   1 
ATOM   3414  C  CZ    . TYR   A 1  432 ? 27.922  71.640  72.897  1.00 31.82  ? 432 TYR   A CZ    1 
ATOM   3415  O  OH    . TYR   A 1  432 ? 28.166  72.769  72.136  1.00 37.25  ? 432 TYR   A OH    1 
ATOM   3416  N  N     . GLU   A 1  433 ? 27.452  65.885  77.648  1.00 43.32  ? 433 GLU   A N     1 
ATOM   3417  C  CA    . GLU   A 1  433 ? 26.745  65.081  78.639  1.00 45.50  ? 433 GLU   A CA    1 
ATOM   3418  C  C     . GLU   A 1  433 ? 27.395  65.216  80.009  1.00 45.42  ? 433 GLU   A C     1 
ATOM   3419  O  O     . GLU   A 1  433 ? 26.707  65.438  81.011  1.00 51.68  ? 433 GLU   A O     1 
ATOM   3420  C  CB    . GLU   A 1  433 ? 26.698  63.623  78.185  1.00 39.20  ? 433 GLU   A CB    1 
ATOM   3421  C  CG    . GLU   A 1  433 ? 26.260  62.663  79.254  1.00 56.68  ? 433 GLU   A CG    1 
ATOM   3422  C  CD    . GLU   A 1  433 ? 25.203  61.684  78.788  1.00 67.72  ? 433 GLU   A CD    1 
ATOM   3423  O  OE1   . GLU   A 1  433 ? 24.423  62.030  77.882  1.00 69.24  ? 433 GLU   A OE1   1 
ATOM   3424  O  OE2   . GLU   A 1  433 ? 25.149  60.561  79.334  1.00 84.11  ? 433 GLU   A OE2   1 
ATOM   3425  N  N     . GLU   A 1  434 ? 28.725  65.087  80.066  1.00 48.80  ? 434 GLU   A N     1 
ATOM   3426  C  CA    . GLU   A 1  434 ? 29.456  65.283  81.312  1.00 47.75  ? 434 GLU   A CA    1 
ATOM   3427  C  C     . GLU   A 1  434 ? 29.094  66.621  81.942  1.00 45.69  ? 434 GLU   A C     1 
ATOM   3428  O  O     . GLU   A 1  434 ? 28.537  66.677  83.044  1.00 44.55  ? 434 GLU   A O     1 
ATOM   3429  C  CB    . GLU   A 1  434 ? 30.963  65.198  81.054  1.00 42.08  ? 434 GLU   A CB    1 
ATOM   3430  C  CG    . GLU   A 1  434 ? 31.575  63.848  81.362  1.00 57.05  ? 434 GLU   A CG    1 
ATOM   3431  C  CD    . GLU   A 1  434 ? 32.555  63.400  80.286  1.00 74.16  ? 434 GLU   A CD    1 
ATOM   3432  O  OE1   . GLU   A 1  434 ? 33.329  64.254  79.794  1.00 75.78  ? 434 GLU   A OE1   1 
ATOM   3433  O  OE2   . GLU   A 1  434 ? 32.542  62.195  79.926  1.00 64.95  ? 434 GLU   A OE2   1 
ATOM   3434  N  N     . VAL   A 1  435 ? 29.391  67.713  81.239  1.00 42.14  ? 435 VAL   A N     1 
ATOM   3435  C  CA    . VAL   A 1  435 ? 29.163  69.058  81.754  1.00 48.86  ? 435 VAL   A CA    1 
ATOM   3436  C  C     . VAL   A 1  435 ? 27.756  69.212  82.325  1.00 51.48  ? 435 VAL   A C     1 
ATOM   3437  O  O     . VAL   A 1  435 ? 27.582  69.421  83.533  1.00 59.64  ? 435 VAL   A O     1 
ATOM   3438  C  CB    . VAL   A 1  435 ? 29.418  70.104  80.663  1.00 36.86  ? 435 VAL   A CB    1 
ATOM   3439  C  CG1   . VAL   A 1  435 ? 29.024  71.483  81.178  1.00 33.48  ? 435 VAL   A CG1   1 
ATOM   3440  C  CG2   . VAL   A 1  435 ? 30.872  70.053  80.259  1.00 27.11  ? 435 VAL   A CG2   1 
ATOM   3441  N  N     . GLY   A 1  436 ? 26.750  69.122  81.468  1.00 42.85  ? 436 GLY   A N     1 
ATOM   3442  C  CA    . GLY   A 1  436 ? 25.374  69.302  81.873  1.00 47.18  ? 436 GLY   A CA    1 
ATOM   3443  C  C     . GLY   A 1  436 ? 24.757  68.013  82.349  1.00 53.04  ? 436 GLY   A C     1 
ATOM   3444  O  O     . GLY   A 1  436 ? 25.450  67.050  82.685  1.00 63.93  ? 436 GLY   A O     1 
ATOM   3445  N  N     . VAL   A 1  437 ? 23.426  68.005  82.394  1.00 51.66  ? 437 VAL   A N     1 
ATOM   3446  C  CA    . VAL   A 1  437 ? 22.691  66.746  82.434  1.00 74.86  ? 437 VAL   A CA    1 
ATOM   3447  C  C     . VAL   A 1  437 ? 23.267  65.869  83.538  1.00 76.93  ? 437 VAL   A C     1 
ATOM   3448  O  O     . VAL   A 1  437 ? 23.626  64.710  83.302  1.00 78.76  ? 437 VAL   A O     1 
ATOM   3449  C  CB    . VAL   A 1  437 ? 22.752  66.023  81.067  1.00 81.83  ? 437 VAL   A CB    1 
ATOM   3450  C  CG1   . VAL   A 1  437 ? 21.919  64.749  81.094  1.00 68.57  ? 437 VAL   A CG1   1 
ATOM   3451  C  CG2   . VAL   A 1  437 ? 22.308  66.953  79.897  1.00 76.18  ? 437 VAL   A CG2   1 
ATOM   3452  N  N     . ASP   A 1  438 ? 23.407  66.434  84.732  1.00 82.00  ? 438 ASP   A N     1 
ATOM   3453  C  CA    . ASP   A 1  438 ? 23.832  65.712  85.928  1.00 85.90  ? 438 ASP   A CA    1 
ATOM   3454  C  C     . ASP   A 1  438 ? 22.769  65.689  87.010  1.00 93.67  ? 438 ASP   A C     1 
ATOM   3455  O  O     . ASP   A 1  438 ? 22.570  64.649  87.642  1.00 106.29 ? 438 ASP   A O     1 
ATOM   3456  C  CB    . ASP   A 1  438 ? 25.116  66.330  86.518  1.00 85.34  ? 438 ASP   A CB    1 
ATOM   3457  C  CG    . ASP   A 1  438 ? 26.361  65.984  85.713  1.00 88.41  ? 438 ASP   A CG    1 
ATOM   3458  O  OD1   . ASP   A 1  438 ? 26.312  65.003  84.934  1.00 77.84  ? 438 ASP   A OD1   1 
ATOM   3459  O  OD2   . ASP   A 1  438 ? 27.389  66.690  85.870  1.00 84.81  ? 438 ASP   A OD2   1 
ATOM   3460  N  N     . SER   A 1  439 ? 22.084  66.812  87.232  1.00 87.81  ? 439 SER   A N     1 
ATOM   3461  C  CA    . SER   A 1  439 ? 21.075  66.953  88.280  1.00 89.35  ? 439 SER   A CA    1 
ATOM   3462  C  C     . SER   A 1  439 ? 19.795  67.607  87.755  1.00 82.71  ? 439 SER   A C     1 
ATOM   3463  O  O     . SER   A 1  439 ? 19.394  68.685  88.203  1.00 75.75  ? 439 SER   A O     1 
ATOM   3464  C  CB    . SER   A 1  439 ? 21.639  67.771  89.449  1.00 104.35 ? 439 SER   A CB    1 
ATOM   3465  O  OG    . SER   A 1  439 ? 22.121  69.039  89.019  1.00 96.80  ? 439 SER   A OG    1 
ATOM   3466  N  N     . MET   B 1  1   ? 20.550  50.165  -4.015  1.00 54.80  ? 1   MET   C N     1 
ATOM   3467  C  CA    . MET   B 1  1   ? 21.163  49.598  -2.807  1.00 50.94  ? 1   MET   C CA    1 
ATOM   3468  C  C     . MET   B 1  1   ? 20.213  48.717  -1.980  1.00 49.85  ? 1   MET   C C     1 
ATOM   3469  O  O     . MET   B 1  1   ? 19.028  49.047  -1.768  1.00 48.53  ? 1   MET   C O     1 
ATOM   3470  C  CB    . MET   B 1  1   ? 21.733  50.705  -1.918  1.00 52.08  ? 1   MET   C CB    1 
ATOM   3471  C  CG    . MET   B 1  1   ? 22.416  50.169  -0.650  1.00 54.09  ? 1   MET   C CG    1 
ATOM   3472  S  SD    . MET   B 1  1   ? 23.873  51.112  -0.144  1.00 66.32  ? 1   MET   C SD    1 
ATOM   3473  C  CE    . MET   B 1  1   ? 23.350  52.783  -0.568  1.00 62.27  ? 1   MET   C CE    1 
ATOM   3474  N  N     . ARG   B 1  2   ? 20.790  47.612  -1.494  1.00 44.38  ? 2   ARG   C N     1 
ATOM   3475  C  CA    . ARG   B 1  2   ? 20.048  46.487  -0.955  1.00 32.77  ? 2   ARG   C CA    1 
ATOM   3476  C  C     . ARG   B 1  2   ? 19.587  45.683  -2.148  1.00 31.47  ? 2   ARG   C C     1 
ATOM   3477  O  O     . ARG   B 1  2   ? 18.452  45.203  -2.168  1.00 41.37  ? 2   ARG   C O     1 
ATOM   3478  C  CB    . ARG   B 1  2   ? 18.872  46.933  -0.094  1.00 40.77  ? 2   ARG   C CB    1 
ATOM   3479  C  CG    . ARG   B 1  2   ? 19.263  47.350  1.338   1.00 63.16  ? 2   ARG   C CG    1 
ATOM   3480  C  CD    . ARG   B 1  2   ? 18.287  48.441  1.859   1.00 73.97  ? 2   ARG   C CD    1 
ATOM   3481  N  NE    . ARG   B 1  2   ? 18.056  49.437  0.814   1.00 75.99  ? 2   ARG   C NE    1 
ATOM   3482  C  CZ    . ARG   B 1  2   ? 18.646  50.627  0.749   1.00 69.78  ? 2   ARG   C CZ    1 
ATOM   3483  N  NH1   . ARG   B 1  2   ? 19.381  51.096  1.751   1.00 60.42  ? 2   ARG   C NH1   1 
ATOM   3484  N  NH2   . ARG   B 1  2   ? 18.505  51.358  -0.356  1.00 55.22  ? 2   ARG   C NH2   1 
ATOM   3485  N  N     . GLU   B 1  3   ? 20.472  45.528  -3.136  1.00 30.00  ? 3   GLU   C N     1 
ATOM   3486  C  CA    . GLU   B 1  3   ? 20.154  44.806  -4.355  1.00 30.74  ? 3   GLU   C CA    1 
ATOM   3487  C  C     . GLU   B 1  3   ? 20.298  43.308  -4.132  1.00 29.90  ? 3   GLU   C C     1 
ATOM   3488  O  O     . GLU   B 1  3   ? 21.178  42.876  -3.380  1.00 24.42  ? 3   GLU   C O     1 
ATOM   3489  C  CB    . GLU   B 1  3   ? 21.078  45.234  -5.493  1.00 31.38  ? 3   GLU   C CB    1 
ATOM   3490  C  CG    . GLU   B 1  3   ? 20.898  46.660  -5.958  1.00 34.60  ? 3   GLU   C CG    1 
ATOM   3491  C  CD    . GLU   B 1  3   ? 22.077  47.538  -5.598  1.00 37.79  ? 3   GLU   C CD    1 
ATOM   3492  O  OE1   . GLU   B 1  3   ? 22.751  47.240  -4.585  1.00 35.67  ? 3   GLU   C OE1   1 
ATOM   3493  O  OE2   . GLU   B 1  3   ? 22.331  48.514  -6.334  1.00 34.46  ? 3   GLU   C OE2   1 
ATOM   3494  N  N     . CYS   B 1  4   ? 19.437  42.525  -4.816  1.00 27.65  ? 4   CYS   C N     1 
ATOM   3495  C  CA    A CYS   B 1  4   ? 19.454  41.067  -4.773  0.46 23.53  ? 4   CYS   C CA    1 
ATOM   3496  C  CA    B CYS   B 1  4   ? 19.441  41.063  -4.770  0.54 23.50  ? 4   CYS   C CA    1 
ATOM   3497  C  C     . CYS   B 1  4   ? 19.525  40.519  -6.189  1.00 21.85  ? 4   CYS   C C     1 
ATOM   3498  O  O     . CYS   B 1  4   ? 18.772  40.952  -7.057  1.00 28.11  ? 4   CYS   C O     1 
ATOM   3499  C  CB    A CYS   B 1  4   ? 18.212  40.522  -4.068  0.46 23.00  ? 4   CYS   C CB    1 
ATOM   3500  C  CB    B CYS   B 1  4   ? 18.178  40.504  -4.094  0.54 22.98  ? 4   CYS   C CB    1 
ATOM   3501  S  SG    A CYS   B 1  4   ? 18.092  38.729  -4.065  0.46 21.03  ? 4   CYS   C SG    1 
ATOM   3502  S  SG    B CYS   B 1  4   ? 17.993  40.752  -2.293  0.54 28.81  ? 4   CYS   C SG    1 
ATOM   3503  N  N     . ILE   B 1  5   ? 20.425  39.560  -6.416  1.00 23.64  ? 5   ILE   C N     1 
ATOM   3504  C  CA    . ILE   B 1  5   ? 20.641  38.930  -7.721  1.00 21.52  ? 5   ILE   C CA    1 
ATOM   3505  C  C     . ILE   B 1  5   ? 20.063  37.520  -7.701  1.00 21.36  ? 5   ILE   C C     1 
ATOM   3506  O  O     . ILE   B 1  5   ? 20.520  36.666  -6.924  1.00 24.21  ? 5   ILE   C O     1 
ATOM   3507  C  CB    . ILE   B 1  5   ? 22.135  38.864  -8.093  1.00 26.21  ? 5   ILE   C CB    1 
ATOM   3508  C  CG1   . ILE   B 1  5   ? 22.759  40.253  -8.112  1.00 19.16  ? 5   ILE   C CG1   1 
ATOM   3509  C  CG2   . ILE   B 1  5   ? 22.323  38.130  -9.441  1.00 14.97  ? 5   ILE   C CG2   1 
ATOM   3510  C  CD1   . ILE   B 1  5   ? 24.156  40.275  -8.623  1.00 19.62  ? 5   ILE   C CD1   1 
ATOM   3511  N  N     . SER   B 1  6   ? 19.101  37.261  -8.589  1.00 23.40  ? 6   SER   C N     1 
ATOM   3512  C  CA    . SER   B 1  6   ? 18.591  35.911  -8.798  1.00 19.55  ? 6   SER   C CA    1 
ATOM   3513  C  C     . SER   B 1  6   ? 19.463  35.167  -9.798  1.00 26.25  ? 6   SER   C C     1 
ATOM   3514  O  O     . SER   B 1  6   ? 19.987  35.751  -10.749 1.00 34.52  ? 6   SER   C O     1 
ATOM   3515  C  CB    . SER   B 1  6   ? 17.158  35.944  -9.299  1.00 20.06  ? 6   SER   C CB    1 
ATOM   3516  O  OG    . SER   B 1  6   ? 16.278  36.360  -8.280  1.00 29.40  ? 6   SER   C OG    1 
ATOM   3517  N  N     . ILE   B 1  7   ? 19.628  33.873  -9.578  1.00 22.15  ? 7   ILE   C N     1 
ATOM   3518  C  CA    . ILE   B 1  7   ? 20.380  33.020  -10.483 1.00 18.71  ? 7   ILE   C CA    1 
ATOM   3519  C  C     . ILE   B 1  7   ? 19.545  31.783  -10.695 1.00 19.46  ? 7   ILE   C C     1 
ATOM   3520  O  O     . ILE   B 1  7   ? 19.123  31.157  -9.722  1.00 25.46  ? 7   ILE   C O     1 
ATOM   3521  C  CB    . ILE   B 1  7   ? 21.762  32.656  -9.922  1.00 20.36  ? 7   ILE   C CB    1 
ATOM   3522  C  CG1   . ILE   B 1  7   ? 22.574  33.925  -9.668  1.00 19.46  ? 7   ILE   C CG1   1 
ATOM   3523  C  CG2   . ILE   B 1  7   ? 22.490  31.723  -10.860 1.00 19.08  ? 7   ILE   C CG2   1 
ATOM   3524  C  CD1   . ILE   B 1  7   ? 23.921  33.643  -9.160  1.00 14.74  ? 7   ILE   C CD1   1 
ATOM   3525  N  N     . HIS   B 1  8   ? 19.272  31.461  -11.954 1.00 18.66  ? 8   HIS   C N     1 
ATOM   3526  C  CA    . HIS   B 1  8   ? 18.357  30.399  -12.341 1.00 21.14  ? 8   HIS   C CA    1 
ATOM   3527  C  C     . HIS   B 1  8   ? 19.160  29.322  -13.066 1.00 22.12  ? 8   HIS   C C     1 
ATOM   3528  O  O     . HIS   B 1  8   ? 19.711  29.570  -14.148 1.00 23.65  ? 8   HIS   C O     1 
ATOM   3529  C  CB    . HIS   B 1  8   ? 17.226  30.965  -13.217 1.00 23.43  ? 8   HIS   C CB    1 
ATOM   3530  C  CG    . HIS   B 1  8   ? 16.483  32.105  -12.587 1.00 20.97  ? 8   HIS   C CG    1 
ATOM   3531  N  ND1   . HIS   B 1  8   ? 15.366  31.926  -11.796 1.00 22.14  ? 8   HIS   C ND1   1 
ATOM   3532  C  CD2   . HIS   B 1  8   ? 16.721  33.440  -12.602 1.00 26.20  ? 8   HIS   C CD2   1 
ATOM   3533  C  CE1   . HIS   B 1  8   ? 14.943  33.102  -11.357 1.00 27.24  ? 8   HIS   C CE1   1 
ATOM   3534  N  NE2   . HIS   B 1  8   ? 15.748  34.039  -11.834 1.00 27.44  ? 8   HIS   C NE2   1 
ATOM   3535  N  N     . VAL   B 1  9   ? 19.220  28.135  -12.476 1.00 12.94  ? 9   VAL   C N     1 
ATOM   3536  C  CA    . VAL   B 1  9   ? 20.141  27.092  -12.893 1.00 16.18  ? 9   VAL   C CA    1 
ATOM   3537  C  C     . VAL   B 1  9   ? 19.355  25.872  -13.349 1.00 19.05  ? 9   VAL   C C     1 
ATOM   3538  O  O     . VAL   B 1  9   ? 18.602  25.291  -12.562 1.00 27.88  ? 9   VAL   C O     1 
ATOM   3539  C  CB    . VAL   B 1  9   ? 21.100  26.708  -11.761 1.00 20.32  ? 9   VAL   C CB    1 
ATOM   3540  C  CG1   . VAL   B 1  9   ? 21.829  25.404  -12.115 1.00 22.00  ? 9   VAL   C CG1   1 
ATOM   3541  C  CG2   . VAL   B 1  9   ? 22.069  27.832  -11.494 1.00 22.44  ? 9   VAL   C CG2   1 
ATOM   3542  N  N     . GLY   B 1  10  ? 19.581  25.444  -14.594 1.00 14.98  ? 10  GLY   C N     1 
ATOM   3543  C  CA    . GLY   B 1  10  ? 18.870  24.309  -15.153 1.00 15.52  ? 10  GLY   C CA    1 
ATOM   3544  C  C     . GLY   B 1  10  ? 17.394  24.592  -15.443 1.00 23.44  ? 10  GLY   C C     1 
ATOM   3545  O  O     . GLY   B 1  10  ? 16.865  25.702  -15.258 1.00 25.86  ? 10  GLY   C O     1 
ATOM   3546  N  N     . GLN   B 1  11  ? 16.707  23.545  -15.901 1.00 16.70  ? 11  GLN   C N     1 
ATOM   3547  C  CA    . GLN   B 1  11  ? 15.363  23.755  -16.428 1.00 18.08  ? 11  GLN   C CA    1 
ATOM   3548  C  C     . GLN   B 1  11  ? 14.398  24.195  -15.330 1.00 21.01  ? 11  GLN   C C     1 
ATOM   3549  O  O     . GLN   B 1  11  ? 13.648  25.161  -15.502 1.00 20.26  ? 11  GLN   C O     1 
ATOM   3550  C  CB    . GLN   B 1  11  ? 14.864  22.500  -17.128 1.00 14.53  ? 11  GLN   C CB    1 
ATOM   3551  C  CG    . GLN   B 1  11  ? 13.505  22.685  -17.738 1.00 18.80  ? 11  GLN   C CG    1 
ATOM   3552  C  CD    . GLN   B 1  11  ? 12.940  21.384  -18.265 1.00 24.89  ? 11  GLN   C CD    1 
ATOM   3553  O  OE1   . GLN   B 1  11  ? 13.494  20.794  -19.196 1.00 29.86  ? 11  GLN   C OE1   1 
ATOM   3554  N  NE2   . GLN   B 1  11  ? 11.831  20.924  -17.677 1.00 17.54  ? 11  GLN   C NE2   1 
ATOM   3555  N  N     . ALA   B 1  12  ? 14.394  23.499  -14.190 1.00 19.41  ? 12  ALA   C N     1 
ATOM   3556  C  CA    . ALA   B 1  12  ? 13.480  23.883  -13.123 1.00 13.04  ? 12  ALA   C CA    1 
ATOM   3557  C  C     . ALA   B 1  12  ? 13.732  25.318  -12.711 1.00 20.66  ? 12  ALA   C C     1 
ATOM   3558  O  O     . ALA   B 1  12  ? 12.799  26.126  -12.629 1.00 27.92  ? 12  ALA   C O     1 
ATOM   3559  C  CB    . ALA   B 1  12  ? 13.603  22.946  -11.922 1.00 17.98  ? 12  ALA   C CB    1 
ATOM   3560  N  N     . GLY   B 1  13  ? 14.995  25.663  -12.475 1.00 15.23  ? 13  GLY   C N     1 
ATOM   3561  C  CA    . GLY   B 1  13  ? 15.328  27.035  -12.182 1.00 17.41  ? 13  GLY   C CA    1 
ATOM   3562  C  C     . GLY   B 1  13  ? 14.871  27.963  -13.282 1.00 19.34  ? 13  GLY   C C     1 
ATOM   3563  O  O     . GLY   B 1  13  ? 14.148  28.912  -12.987 1.00 21.54  ? 13  GLY   C O     1 
ATOM   3564  N  N     . VAL   B 1  14  ? 15.253  27.701  -14.543 1.00 18.32  ? 14  VAL   C N     1 
ATOM   3565  C  CA    . VAL   B 1  14  ? 14.947  28.653  -15.615 1.00 20.91  ? 14  VAL   C CA    1 
ATOM   3566  C  C     . VAL   B 1  14  ? 13.446  28.844  -15.752 1.00 19.28  ? 14  VAL   C C     1 
ATOM   3567  O  O     . VAL   B 1  14  ? 12.956  29.971  -15.777 1.00 21.52  ? 14  VAL   C O     1 
ATOM   3568  C  CB    . VAL   B 1  14  ? 15.557  28.216  -16.957 1.00 20.82  ? 14  VAL   C CB    1 
ATOM   3569  C  CG1   . VAL   B 1  14  ? 15.082  29.131  -18.016 1.00 15.79  ? 14  VAL   C CG1   1 
ATOM   3570  C  CG2   . VAL   B 1  14  ? 17.064  28.268  -16.908 1.00 22.69  ? 14  VAL   C CG2   1 
ATOM   3571  N  N     . GLN   B 1  15  ? 12.694  27.745  -15.852 1.00 23.35  ? 15  GLN   C N     1 
ATOM   3572  C  CA    . GLN   B 1  15  ? 11.248  27.846  -16.042 1.00 23.94  ? 15  GLN   C CA    1 
ATOM   3573  C  C     . GLN   B 1  15  ? 10.546  28.431  -14.814 1.00 26.62  ? 15  GLN   C C     1 
ATOM   3574  O  O     . GLN   B 1  15  ? 9.657   29.283  -14.945 1.00 32.24  ? 15  GLN   C O     1 
ATOM   3575  C  CB    . GLN   B 1  15  ? 10.666  26.486  -16.393 1.00 22.79  ? 15  GLN   C CB    1 
ATOM   3576  C  CG    . GLN   B 1  15  ? 11.495  25.758  -17.389 1.00 23.16  ? 15  GLN   C CG    1 
ATOM   3577  C  CD    . GLN   B 1  15  ? 10.662  24.982  -18.384 1.00 29.99  ? 15  GLN   C CD    1 
ATOM   3578  O  OE1   . GLN   B 1  15  ? 10.124  23.928  -18.050 1.00 31.51  ? 15  GLN   C OE1   1 
ATOM   3579  N  NE2   . GLN   B 1  15  ? 10.571  25.485  -19.626 1.00 24.51  ? 15  GLN   C NE2   1 
ATOM   3580  N  N     . ILE   B 1  16  ? 10.925  28.018  -13.609 1.00 22.31  ? 16  ILE   C N     1 
ATOM   3581  C  CA    . ILE   B 1  16  ? 10.428  28.766  -12.455 1.00 25.15  ? 16  ILE   C CA    1 
ATOM   3582  C  C     . ILE   B 1  16  ? 10.823  30.240  -12.574 1.00 26.86  ? 16  ILE   C C     1 
ATOM   3583  O  O     . ILE   B 1  16  ? 10.025  31.140  -12.287 1.00 28.51  ? 16  ILE   C O     1 
ATOM   3584  C  CB    . ILE   B 1  16  ? 10.934  28.143  -11.142 1.00 20.88  ? 16  ILE   C CB    1 
ATOM   3585  C  CG1   . ILE   B 1  16  ? 10.180  26.857  -10.815 1.00 20.09  ? 16  ILE   C CG1   1 
ATOM   3586  C  CG2   . ILE   B 1  16  ? 10.747  29.101  -10.016 1.00 22.19  ? 16  ILE   C CG2   1 
ATOM   3587  C  CD1   . ILE   B 1  16  ? 10.862  26.063  -9.792  1.00 18.48  ? 16  ILE   C CD1   1 
ATOM   3588  N  N     . GLY   B 1  17  ? 12.055  30.510  -13.019 1.00 22.79  ? 17  GLY   C N     1 
ATOM   3589  C  CA    . GLY   B 1  17  ? 12.501  31.889  -13.154 1.00 23.92  ? 17  GLY   C CA    1 
ATOM   3590  C  C     . GLY   B 1  17  ? 11.632  32.705  -14.093 1.00 29.49  ? 17  GLY   C C     1 
ATOM   3591  O  O     . GLY   B 1  17  ? 11.258  33.841  -13.786 1.00 34.96  ? 17  GLY   C O     1 
ATOM   3592  N  N     . ASN   B 1  18  ? 11.309  32.147  -15.255 1.00 23.03  ? 18  ASN   C N     1 
ATOM   3593  C  CA    . ASN   B 1  18  ? 10.427  32.843  -16.184 1.00 30.48  ? 18  ASN   C CA    1 
ATOM   3594  C  C     . ASN   B 1  18  ? 9.067   33.144  -15.566 1.00 30.67  ? 18  ASN   C C     1 
ATOM   3595  O  O     . ASN   B 1  18  ? 8.485   34.210  -15.813 1.00 27.18  ? 18  ASN   C O     1 
ATOM   3596  C  CB    . ASN   B 1  18  ? 10.249  32.007  -17.446 1.00 29.56  ? 18  ASN   C CB    1 
ATOM   3597  C  CG    . ASN   B 1  18  ? 11.403  32.145  -18.368 1.00 35.51  ? 18  ASN   C CG    1 
ATOM   3598  O  OD1   . ASN   B 1  18  ? 11.697  33.244  -18.873 1.00 45.26  ? 18  ASN   C OD1   1 
ATOM   3599  N  ND2   . ASN   B 1  18  ? 12.093  31.043  -18.592 1.00 29.01  ? 18  ASN   C ND2   1 
ATOM   3600  N  N     . ALA   B 1  19  ? 8.515   32.187  -14.814 1.00 19.59  ? 19  ALA   C N     1 
ATOM   3601  C  CA    . ALA   B 1  19  ? 7.264   32.429  -14.112 1.00 23.03  ? 19  ALA   C CA    1 
ATOM   3602  C  C     . ALA   B 1  19  ? 7.412   33.554  -13.089 1.00 28.31  ? 19  ALA   C C     1 
ATOM   3603  O  O     . ALA   B 1  19  ? 6.557   34.440  -12.997 1.00 25.70  ? 19  ALA   C O     1 
ATOM   3604  C  CB    . ALA   B 1  19  ? 6.802   31.142  -13.434 1.00 26.62  ? 19  ALA   C CB    1 
ATOM   3605  N  N     . CYS   B 1  20  ? 8.496   33.526  -12.301 1.00 29.53  ? 20  CYS   C N     1 
ATOM   3606  C  CA    . CYS   B 1  20  ? 8.731   34.554  -11.295 1.00 27.86  ? 20  CYS   C CA    1 
ATOM   3607  C  C     . CYS   B 1  20  ? 8.854   35.939  -11.915 1.00 29.54  ? 20  CYS   C C     1 
ATOM   3608  O  O     . CYS   B 1  20  ? 8.338   36.926  -11.370 1.00 28.59  ? 20  CYS   C O     1 
ATOM   3609  C  CB    . CYS   B 1  20  ? 10.002  34.230  -10.518 1.00 28.84  ? 20  CYS   C CB    1 
ATOM   3610  S  SG    . CYS   B 1  20  ? 9.754   33.144  -9.163  1.00 38.40  ? 20  CYS   C SG    1 
ATOM   3611  N  N     . TRP   B 1  21  ? 9.567   36.046  -13.035 1.00 27.68  ? 21  TRP   C N     1 
ATOM   3612  C  CA    . TRP   B 1  21  ? 9.866   37.374  -13.545 1.00 24.14  ? 21  TRP   C CA    1 
ATOM   3613  C  C     . TRP   B 1  21  ? 8.673   37.978  -14.265 1.00 25.04  ? 21  TRP   C C     1 
ATOM   3614  O  O     . TRP   B 1  21  ? 8.461   39.194  -14.190 1.00 32.54  ? 21  TRP   C O     1 
ATOM   3615  C  CB    . TRP   B 1  21  ? 11.115  37.327  -14.423 1.00 22.64  ? 21  TRP   C CB    1 
ATOM   3616  C  CG    . TRP   B 1  21  ? 12.376  37.288  -13.579 1.00 23.75  ? 21  TRP   C CG    1 
ATOM   3617  C  CD1   . TRP   B 1  21  ? 13.174  36.208  -13.343 1.00 29.07  ? 21  TRP   C CD1   1 
ATOM   3618  C  CD2   . TRP   B 1  21  ? 12.939  38.372  -12.825 1.00 23.85  ? 21  TRP   C CD2   1 
ATOM   3619  N  NE1   . TRP   B 1  21  ? 14.210  36.555  -12.508 1.00 34.89  ? 21  TRP   C NE1   1 
ATOM   3620  C  CE2   . TRP   B 1  21  ? 14.085  37.879  -12.174 1.00 27.08  ? 21  TRP   C CE2   1 
ATOM   3621  C  CE3   . TRP   B 1  21  ? 12.590  39.718  -12.645 1.00 23.47  ? 21  TRP   C CE3   1 
ATOM   3622  C  CZ2   . TRP   B 1  21  ? 14.886  38.684  -11.361 1.00 26.27  ? 21  TRP   C CZ2   1 
ATOM   3623  C  CZ3   . TRP   B 1  21  ? 13.392  40.516  -11.836 1.00 22.08  ? 21  TRP   C CZ3   1 
ATOM   3624  C  CH2   . TRP   B 1  21  ? 14.523  40.000  -11.209 1.00 21.92  ? 21  TRP   C CH2   1 
ATOM   3625  N  N     . GLU   B 1  22  ? 7.852   37.153  -14.913 1.00 26.42  ? 22  GLU   C N     1 
ATOM   3626  C  CA    . GLU   B 1  22  ? 6.631   37.669  -15.520 1.00 25.50  ? 22  GLU   C CA    1 
ATOM   3627  C  C     . GLU   B 1  22  ? 5.693   38.193  -14.460 1.00 28.12  ? 22  GLU   C C     1 
ATOM   3628  O  O     . GLU   B 1  22  ? 4.985   39.185  -14.673 1.00 35.94  ? 22  GLU   C O     1 
ATOM   3629  C  CB    . GLU   B 1  22  ? 5.936   36.581  -16.330 1.00 32.21  ? 22  GLU   C CB    1 
ATOM   3630  C  CG    . GLU   B 1  22  ? 4.461   36.875  -16.563 1.00 38.62  ? 22  GLU   C CG    1 
ATOM   3631  C  CD    . GLU   B 1  22  ? 3.838   35.977  -17.616 1.00 47.57  ? 22  GLU   C CD    1 
ATOM   3632  O  OE1   . GLU   B 1  22  ? 4.181   34.772  -17.645 1.00 39.03  ? 22  GLU   C OE1   1 
ATOM   3633  O  OE2   . GLU   B 1  22  ? 3.010   36.487  -18.413 1.00 48.43  ? 22  GLU   C OE2   1 
ATOM   3634  N  N     . LEU   B 1  23  ? 5.656   37.511  -13.316 1.00 23.20  ? 23  LEU   C N     1 
ATOM   3635  C  CA    . LEU   B 1  23  ? 4.838   37.958  -12.206 1.00 22.35  ? 23  LEU   C CA    1 
ATOM   3636  C  C     . LEU   B 1  23  ? 5.352   39.281  -11.646 1.00 28.35  ? 23  LEU   C C     1 
ATOM   3637  O  O     . LEU   B 1  23  ? 4.559   40.184  -11.356 1.00 27.66  ? 23  LEU   C O     1 
ATOM   3638  C  CB    . LEU   B 1  23  ? 4.816   36.885  -11.128 1.00 19.20  ? 23  LEU   C CB    1 
ATOM   3639  C  CG    . LEU   B 1  23  ? 3.894   37.201  -9.958  1.00 23.53  ? 23  LEU   C CG    1 
ATOM   3640  C  CD1   . LEU   B 1  23  ? 2.472   37.384  -10.456 1.00 22.99  ? 23  LEU   C CD1   1 
ATOM   3641  C  CD2   . LEU   B 1  23  ? 3.988   36.111  -8.904  1.00 27.01  ? 23  LEU   C CD2   1 
ATOM   3642  N  N     . TYR   B 1  24  ? 6.677   39.423  -11.491 1.00 24.70  ? 24  TYR   C N     1 
ATOM   3643  C  CA    . TYR   B 1  24  ? 7.211   40.663  -10.934 1.00 25.37  ? 24  TYR   C CA    1 
ATOM   3644  C  C     . TYR   B 1  24  ? 6.845   41.859  -11.808 1.00 29.92  ? 24  TYR   C C     1 
ATOM   3645  O  O     . TYR   B 1  24  ? 6.451   42.919  -11.297 1.00 27.20  ? 24  TYR   C O     1 
ATOM   3646  C  CB    . TYR   B 1  24  ? 8.727   40.577  -10.774 1.00 28.01  ? 24  TYR   C CB    1 
ATOM   3647  C  CG    . TYR   B 1  24  ? 9.253   39.580  -9.759  1.00 28.91  ? 24  TYR   C CG    1 
ATOM   3648  C  CD1   . TYR   B 1  24  ? 8.472   39.119  -8.709  1.00 27.36  ? 24  TYR   C CD1   1 
ATOM   3649  C  CD2   . TYR   B 1  24  ? 10.556  39.121  -9.847  1.00 28.68  ? 24  TYR   C CD2   1 
ATOM   3650  C  CE1   . TYR   B 1  24  ? 8.985   38.213  -7.792  1.00 20.56  ? 24  TYR   C CE1   1 
ATOM   3651  C  CE2   . TYR   B 1  24  ? 11.066  38.220  -8.952  1.00 25.00  ? 24  TYR   C CE2   1 
ATOM   3652  C  CZ    . TYR   B 1  24  ? 10.280  37.771  -7.933  1.00 23.82  ? 24  TYR   C CZ    1 
ATOM   3653  O  OH    . TYR   B 1  24  ? 10.818  36.879  -7.046  1.00 32.58  ? 24  TYR   C OH    1 
ATOM   3654  N  N     . CYS   B 1  25  ? 6.967   41.716  -13.133 1.00 35.34  ? 25  CYS   C N     1 
ATOM   3655  C  CA    . CYS   B 1  25  ? 6.611   42.821  -14.019 1.00 31.98  ? 25  CYS   C CA    1 
ATOM   3656  C  C     . CYS   B 1  25  ? 5.162   43.231  -13.812 1.00 30.41  ? 25  CYS   C C     1 
ATOM   3657  O  O     . CYS   B 1  25  ? 4.859   44.417  -13.671 1.00 33.65  ? 25  CYS   C O     1 
ATOM   3658  C  CB    . CYS   B 1  25  ? 6.860   42.447  -15.478 1.00 28.91  ? 25  CYS   C CB    1 
ATOM   3659  S  SG    . CYS   B 1  25  ? 8.595   42.330  -15.897 1.00 32.20  ? 25  CYS   C SG    1 
ATOM   3660  N  N     . LEU   B 1  26  ? 4.247   42.258  -13.784 1.00 29.75  ? 26  LEU   C N     1 
ATOM   3661  C  CA    . LEU   B 1  26  ? 2.838   42.592  -13.595 1.00 28.90  ? 26  LEU   C CA    1 
ATOM   3662  C  C     . LEU   B 1  26  ? 2.598   43.250  -12.248 1.00 30.38  ? 26  LEU   C C     1 
ATOM   3663  O  O     . LEU   B 1  26  ? 1.692   44.075  -12.108 1.00 39.82  ? 26  LEU   C O     1 
ATOM   3664  C  CB    . LEU   B 1  26  ? 1.989   41.336  -13.731 1.00 32.82  ? 26  LEU   C CB    1 
ATOM   3665  C  CG    . LEU   B 1  26  ? 2.014   40.826  -15.160 1.00 35.53  ? 26  LEU   C CG    1 
ATOM   3666  C  CD1   . LEU   B 1  26  ? 1.401   39.444  -15.223 1.00 34.75  ? 26  LEU   C CD1   1 
ATOM   3667  C  CD2   . LEU   B 1  26  ? 1.255   41.834  -16.024 1.00 27.84  ? 26  LEU   C CD2   1 
ATOM   3668  N  N     . GLU   B 1  27  ? 3.393   42.899  -11.245 1.00 28.68  ? 27  GLU   C N     1 
ATOM   3669  C  CA    . GLU   B 1  27  ? 3.234   43.517  -9.943  1.00 24.05  ? 27  GLU   C CA    1 
ATOM   3670  C  C     . GLU   B 1  27  ? 3.781   44.932  -9.933  1.00 28.74  ? 27  GLU   C C     1 
ATOM   3671  O  O     . GLU   B 1  27  ? 3.262   45.784  -9.204  1.00 29.67  ? 27  GLU   C O     1 
ATOM   3672  C  CB    . GLU   B 1  27  ? 3.946   42.689  -8.880  1.00 28.03  ? 27  GLU   C CB    1 
ATOM   3673  C  CG    . GLU   B 1  27  ? 3.553   41.243  -8.827  1.00 25.64  ? 27  GLU   C CG    1 
ATOM   3674  C  CD    . GLU   B 1  27  ? 3.951   40.645  -7.520  1.00 34.34  ? 27  GLU   C CD    1 
ATOM   3675  O  OE1   . GLU   B 1  27  ? 4.880   41.217  -6.898  1.00 28.62  ? 27  GLU   C OE1   1 
ATOM   3676  O  OE2   . GLU   B 1  27  ? 3.319   39.635  -7.114  1.00 40.38  ? 27  GLU   C OE2   1 
ATOM   3677  N  N     . HIS   B 1  28  ? 4.837   45.190  -10.712 1.00 26.44  ? 28  HIS   C N     1 
ATOM   3678  C  CA    . HIS   B 1  28  ? 5.508   46.485  -10.759 1.00 25.95  ? 28  HIS   C CA    1 
ATOM   3679  C  C     . HIS   B 1  28  ? 5.102   47.377  -11.943 1.00 28.12  ? 28  HIS   C C     1 
ATOM   3680  O  O     . HIS   B 1  28  ? 5.635   48.483  -12.072 1.00 39.12  ? 28  HIS   C O     1 
ATOM   3681  C  CB    . HIS   B 1  28  ? 7.031   46.277  -10.772 1.00 23.42  ? 28  HIS   C CB    1 
ATOM   3682  C  CG    . HIS   B 1  28  ? 7.574   45.768  -9.469  1.00 26.93  ? 28  HIS   C CG    1 
ATOM   3683  N  ND1   . HIS   B 1  28  ? 7.361   46.414  -8.269  1.00 32.10  ? 28  HIS   C ND1   1 
ATOM   3684  C  CD2   . HIS   B 1  28  ? 8.308   44.671  -9.176  1.00 25.49  ? 28  HIS   C CD2   1 
ATOM   3685  C  CE1   . HIS   B 1  28  ? 7.927   45.729  -7.292  1.00 26.55  ? 28  HIS   C CE1   1 
ATOM   3686  N  NE2   . HIS   B 1  28  ? 8.500   44.663  -7.814  1.00 28.42  ? 28  HIS   C NE2   1 
ATOM   3687  N  N     . GLY   B 1  29  ? 4.195   46.947  -12.811 1.00 19.66  ? 29  GLY   C N     1 
ATOM   3688  C  CA    . GLY   B 1  29  ? 3.893   47.758  -13.978 1.00 22.41  ? 29  GLY   C CA    1 
ATOM   3689  C  C     . GLY   B 1  29  ? 4.972   47.831  -15.044 1.00 30.08  ? 29  GLY   C C     1 
ATOM   3690  O  O     . GLY   B 1  29  ? 5.186   48.904  -15.628 1.00 27.19  ? 29  GLY   C O     1 
ATOM   3691  N  N     . ILE   B 1  30  ? 5.639   46.716  -15.342 1.00 31.98  ? 30  ILE   C N     1 
ATOM   3692  C  CA    . ILE   B 1  30  ? 6.713   46.682  -16.329 1.00 30.36  ? 30  ILE   C CA    1 
ATOM   3693  C  C     . ILE   B 1  30  ? 6.221   45.932  -17.558 1.00 30.74  ? 30  ILE   C C     1 
ATOM   3694  O  O     . ILE   B 1  30  ? 5.742   44.800  -17.451 1.00 40.83  ? 30  ILE   C O     1 
ATOM   3695  C  CB    . ILE   B 1  30  ? 7.983   46.043  -15.744 1.00 32.75  ? 30  ILE   C CB    1 
ATOM   3696  C  CG1   . ILE   B 1  30  ? 8.485   46.881  -14.544 1.00 32.66  ? 30  ILE   C CG1   1 
ATOM   3697  C  CG2   . ILE   B 1  30  ? 9.045   45.877  -16.816 1.00 31.14  ? 30  ILE   C CG2   1 
ATOM   3698  C  CD1   . ILE   B 1  30  ? 9.569   46.206  -13.708 1.00 22.32  ? 30  ILE   C CD1   1 
ATOM   3699  N  N     . GLN   B 1  31  ? 6.314   46.570  -18.718 1.00 30.93  ? 31  GLN   C N     1 
ATOM   3700  C  CA    . GLN   B 1  31  ? 5.937   45.925  -19.954 1.00 35.37  ? 31  GLN   C CA    1 
ATOM   3701  C  C     . GLN   B 1  31  ? 6.974   44.875  -20.286 1.00 37.74  ? 31  GLN   C C     1 
ATOM   3702  O  O     . GLN   B 1  31  ? 8.000   44.775  -19.612 1.00 35.94  ? 31  GLN   C O     1 
ATOM   3703  C  CB    . GLN   B 1  31  ? 5.827   46.943  -21.084 1.00 38.63  ? 31  GLN   C CB    1 
ATOM   3704  C  CG    . GLN   B 1  31  ? 5.078   48.211  -20.701 1.00 44.17  ? 31  GLN   C CG    1 
ATOM   3705  C  CD    . GLN   B 1  31  ? 5.535   49.418  -21.509 1.00 54.30  ? 31  GLN   C CD    1 
ATOM   3706  O  OE1   . GLN   B 1  31  ? 6.285   49.288  -22.495 1.00 48.46  ? 31  GLN   C OE1   1 
ATOM   3707  N  NE2   . GLN   B 1  31  ? 5.091   50.608  -21.091 1.00 56.25  ? 31  GLN   C NE2   1 
ATOM   3708  N  N     . PRO   B 1  32  ? 6.713   44.052  -21.310 1.00 35.86  ? 32  PRO   C N     1 
ATOM   3709  C  CA    . PRO   B 1  32  ? 7.710   43.063  -21.752 1.00 26.50  ? 32  PRO   C CA    1 
ATOM   3710  C  C     . PRO   B 1  32  ? 8.872   43.659  -22.502 1.00 33.80  ? 32  PRO   C C     1 
ATOM   3711  O  O     . PRO   B 1  32  ? 9.820   42.926  -22.801 1.00 43.40  ? 32  PRO   C O     1 
ATOM   3712  C  CB    . PRO   B 1  32  ? 6.899   42.132  -22.652 1.00 27.33  ? 32  PRO   C CB    1 
ATOM   3713  C  CG    . PRO   B 1  32  ? 5.501   42.284  -22.170 1.00 17.59  ? 32  PRO   C CG    1 
ATOM   3714  C  CD    . PRO   B 1  32  ? 5.368   43.720  -21.792 1.00 26.42  ? 32  PRO   C CD    1 
ATOM   3715  N  N     . ASP   B 1  33  ? 8.826   44.950  -22.827 1.00 41.76  ? 33  ASP   C N     1 
ATOM   3716  C  CA    . ASP   B 1  33  ? 9.962   45.662  -23.391 1.00 43.52  ? 33  ASP   C CA    1 
ATOM   3717  C  C     . ASP   B 1  33  ? 10.735  46.425  -22.327 1.00 38.09  ? 33  ASP   C C     1 
ATOM   3718  O  O     . ASP   B 1  33  ? 11.613  47.227  -22.663 1.00 47.71  ? 33  ASP   C O     1 
ATOM   3719  C  CB    . ASP   B 1  33  ? 9.503   46.609  -24.507 1.00 37.38  ? 33  ASP   C CB    1 
ATOM   3720  C  CG    . ASP   B 1  33  ? 8.839   47.855  -23.978 1.00 39.05  ? 33  ASP   C CG    1 
ATOM   3721  O  OD1   . ASP   B 1  33  ? 8.319   47.823  -22.848 1.00 43.30  ? 33  ASP   C OD1   1 
ATOM   3722  O  OD2   . ASP   B 1  33  ? 8.832   48.869  -24.698 1.00 48.70  ? 33  ASP   C OD2   1 
ATOM   3723  N  N     . GLY   B 1  34  ? 10.420  46.198  -21.053 1.00 39.23  ? 34  GLY   C N     1 
ATOM   3724  C  CA    . GLY   B 1  34  ? 11.171  46.762  -19.954 1.00 39.91  ? 34  GLY   C CA    1 
ATOM   3725  C  C     . GLY   B 1  34  ? 10.794  48.174  -19.568 1.00 37.16  ? 34  GLY   C C     1 
ATOM   3726  O  O     . GLY   B 1  34  ? 11.388  48.720  -18.634 1.00 31.78  ? 34  GLY   C O     1 
ATOM   3727  N  N     . GLN   B 1  35  ? 9.839   48.788  -20.256 1.00 41.51  ? 35  GLN   C N     1 
ATOM   3728  C  CA    . GLN   B 1  35  ? 9.450   50.150  -19.926 1.00 41.58  ? 35  GLN   C CA    1 
ATOM   3729  C  C     . GLN   B 1  35  ? 8.433   50.116  -18.791 1.00 40.26  ? 35  GLN   C C     1 
ATOM   3730  O  O     . GLN   B 1  35  ? 7.504   49.300  -18.796 1.00 42.41  ? 35  GLN   C O     1 
ATOM   3731  C  CB    . GLN   B 1  35  ? 8.874   50.879  -21.151 1.00 37.12  ? 35  GLN   C CB    1 
ATOM   3732  C  CG    . GLN   B 1  35  ? 9.827   51.019  -22.340 1.00 36.01  ? 35  GLN   C CG    1 
ATOM   3733  C  CD    . GLN   B 1  35  ? 10.976  51.988  -22.083 1.00 44.31  ? 35  GLN   C CD    1 
ATOM   3734  O  OE1   . GLN   B 1  35  ? 10.779  53.076  -21.525 1.00 44.13  ? 35  GLN   C OE1   1 
ATOM   3735  N  NE2   . GLN   B 1  35  ? 12.186  51.597  -22.499 1.00 42.26  ? 35  GLN   C NE2   1 
ATOM   3736  N  N     . MET   B 1  36  ? 8.636   51.000  -17.800 1.00 40.04  ? 36  MET   C N     1 
ATOM   3737  C  CA    . MET   B 1  36  ? 7.763   51.161  -16.636 1.00 33.51  ? 36  MET   C CA    1 
ATOM   3738  C  C     . MET   B 1  36  ? 7.239   52.594  -16.573 1.00 36.58  ? 36  MET   C C     1 
ATOM   3739  O  O     . MET   B 1  36  ? 7.775   53.418  -15.820 1.00 38.41  ? 36  MET   C O     1 
ATOM   3740  C  CB    . MET   B 1  36  ? 8.504   50.817  -15.347 1.00 36.49  ? 36  MET   C CB    1 
ATOM   3741  C  CG    . MET   B 1  36  ? 7.663   50.973  -14.097 1.00 36.06  ? 36  MET   C CG    1 
ATOM   3742  S  SD    . MET   B 1  36  ? 8.701   50.883  -12.647 1.00 49.33  ? 36  MET   C SD    1 
ATOM   3743  C  CE    . MET   B 1  36  ? 9.260   49.199  -12.701 1.00 40.36  ? 36  MET   C CE    1 
ATOM   3744  N  N     . PRO   B 1  37  ? 6.168   52.931  -17.346 1.00 46.18  ? 37  PRO   C N     1 
ATOM   3745  C  CA    . PRO   B 1  37  ? 5.634   54.305  -17.330 1.00 43.10  ? 37  PRO   C CA    1 
ATOM   3746  C  C     . PRO   B 1  37  ? 5.666   54.975  -15.966 1.00 40.88  ? 37  PRO   C C     1 
ATOM   3747  O  O     . PRO   B 1  37  ? 6.090   56.130  -15.852 1.00 30.36  ? 37  PRO   C O     1 
ATOM   3748  C  CB    . PRO   B 1  37  ? 4.197   54.105  -17.809 1.00 37.06  ? 37  PRO   C CB    1 
ATOM   3749  C  CG    . PRO   B 1  37  ? 4.310   52.942  -18.761 1.00 33.00  ? 37  PRO   C CG    1 
ATOM   3750  C  CD    . PRO   B 1  37  ? 5.388   52.050  -18.239 1.00 38.26  ? 37  PRO   C CD    1 
ATOM   3751  N  N     . SER   B 1  38  ? 5.240   54.228  -14.937 1.00 44.18  ? 38  SER   C N     1 
ATOM   3752  C  CA    . SER   B 1  38  ? 5.180   54.728  -13.563 1.00 41.12  ? 38  SER   C CA    1 
ATOM   3753  C  C     . SER   B 1  38  ? 6.499   55.321  -13.081 1.00 46.03  ? 38  SER   C C     1 
ATOM   3754  O  O     . SER   B 1  38  ? 6.497   56.262  -12.274 1.00 53.91  ? 38  SER   C O     1 
ATOM   3755  C  CB    . SER   B 1  38  ? 4.764   53.597  -12.616 1.00 45.67  ? 38  SER   C CB    1 
ATOM   3756  O  OG    . SER   B 1  38  ? 5.322   53.776  -11.311 1.00 46.99  ? 38  SER   C OG    1 
ATOM   3757  N  N     . ASP   B 1  39  ? 7.629   54.778  -13.533 1.00 43.24  ? 39  ASP   C N     1 
ATOM   3758  C  CA    . ASP   B 1  39  ? 8.932   55.178  -13.009 1.00 36.90  ? 39  ASP   C CA    1 
ATOM   3759  C  C     . ASP   B 1  39  ? 9.362   56.498  -13.639 1.00 46.23  ? 39  ASP   C C     1 
ATOM   3760  O  O     . ASP   B 1  39  ? 9.439   56.611  -14.867 1.00 52.85  ? 39  ASP   C O     1 
ATOM   3761  C  CB    . ASP   B 1  39  ? 9.970   54.092  -13.274 1.00 29.78  ? 39  ASP   C CB    1 
ATOM   3762  C  CG    . ASP   B 1  39  ? 11.328  54.445  -12.735 1.00 39.98  ? 39  ASP   C CG    1 
ATOM   3763  O  OD1   . ASP   B 1  39  ? 11.493  55.536  -12.173 1.00 46.01  ? 39  ASP   C OD1   1 
ATOM   3764  O  OD2   . ASP   B 1  39  ? 12.251  53.632  -12.855 1.00 41.88  ? 39  ASP   C OD2   1 
ATOM   3765  N  N     . LYS   B 1  40  ? 9.652   57.491  -12.796 1.00 50.34  ? 40  LYS   C N     1 
ATOM   3766  C  CA    . LYS   B 1  40  ? 10.185  58.769  -13.254 1.00 45.01  ? 40  LYS   C CA    1 
ATOM   3767  C  C     . LYS   B 1  40  ? 11.709  58.824  -13.200 1.00 47.93  ? 40  LYS   C C     1 
ATOM   3768  O  O     . LYS   B 1  40  ? 12.321  59.485  -14.048 1.00 54.04  ? 40  LYS   C O     1 
ATOM   3769  C  CB    . LYS   B 1  40  ? 9.573   59.897  -12.424 1.00 36.83  ? 40  LYS   C CB    1 
ATOM   3770  C  CG    . LYS   B 1  40  ? 8.069   59.786  -12.377 1.00 35.67  ? 40  LYS   C CG    1 
ATOM   3771  C  CD    . LYS   B 1  40  ? 7.545   59.424  -13.767 1.00 33.33  ? 40  LYS   C CD    1 
ATOM   3772  C  CE    . LYS   B 1  40  ? 6.059   59.355  -13.755 1.00 36.23  ? 40  LYS   C CE    1 
ATOM   3773  N  NZ    . LYS   B 1  40  ? 5.538   60.182  -12.631 1.00 54.06  ? 40  LYS   C NZ    1 
ATOM   3774  N  N     . THR   B 1  41  ? 12.320  58.152  -12.213 1.00 44.82  ? 41  THR   C N     1 
ATOM   3775  C  CA    . THR   B 1  41  ? 13.739  57.796  -12.169 1.00 46.10  ? 41  THR   C CA    1 
ATOM   3776  C  C     . THR   B 1  41  ? 14.247  57.152  -13.460 1.00 50.20  ? 41  THR   C C     1 
ATOM   3777  O  O     . THR   B 1  41  ? 14.280  55.917  -13.540 1.00 47.12  ? 41  THR   C O     1 
ATOM   3778  C  CB    . THR   B 1  41  ? 13.997  56.795  -11.026 1.00 51.71  ? 41  THR   C CB    1 
ATOM   3779  O  OG1   . THR   B 1  41  ? 13.773  55.431  -11.480 1.00 31.99  ? 41  THR   C OG1   1 
ATOM   3780  C  CG2   . THR   B 1  41  ? 13.101  57.107  -9.823  1.00 54.51  ? 41  THR   C CG2   1 
ATOM   3781  N  N     . ILE   B 1  42  ? 14.682  57.951  -14.451 1.00 46.34  ? 42  ILE   C N     1 
ATOM   3782  C  CA    . ILE   B 1  42  ? 15.179  57.432  -15.730 1.00 39.98  ? 42  ILE   C CA    1 
ATOM   3783  C  C     . ILE   B 1  42  ? 16.678  57.169  -15.643 1.00 37.28  ? 42  ILE   C C     1 
ATOM   3784  O  O     . ILE   B 1  42  ? 17.452  58.034  -15.221 1.00 43.73  ? 42  ILE   C O     1 
ATOM   3785  C  CB    . ILE   B 1  42  ? 14.876  58.409  -16.872 1.00 41.04  ? 42  ILE   C CB    1 
ATOM   3786  C  CG1   . ILE   B 1  42  ? 13.371  58.652  -16.984 1.00 38.14  ? 42  ILE   C CG1   1 
ATOM   3787  C  CG2   . ILE   B 1  42  ? 15.434  57.877  -18.166 1.00 34.72  ? 42  ILE   C CG2   1 
ATOM   3788  C  CD1   . ILE   B 1  42  ? 13.025  59.681  -17.981 1.00 27.92  ? 42  ILE   C CD1   1 
ATOM   3789  N  N     . GLY   B 1  43  ? 17.096  55.987  -16.070 1.00 36.32  ? 43  GLY   C N     1 
ATOM   3790  C  CA    . GLY   B 1  43  ? 18.479  55.586  -15.972 1.00 41.07  ? 43  GLY   C CA    1 
ATOM   3791  C  C     . GLY   B 1  43  ? 18.873  54.987  -14.633 1.00 46.59  ? 43  GLY   C C     1 
ATOM   3792  O  O     . GLY   B 1  43  ? 19.794  54.159  -14.572 1.00 42.73  ? 43  GLY   C O     1 
ATOM   3793  N  N     . GLY   B 1  44  ? 18.207  55.386  -13.565 1.00 36.92  ? 44  GLY   C N     1 
ATOM   3794  C  CA    . GLY   B 1  44  ? 18.443  54.799  -12.271 1.00 34.93  ? 44  GLY   C CA    1 
ATOM   3795  C  C     . GLY   B 1  44  ? 17.333  55.148  -11.317 1.00 42.02  ? 44  GLY   C C     1 
ATOM   3796  O  O     . GLY   B 1  44  ? 16.221  55.480  -11.728 1.00 43.21  ? 44  GLY   C O     1 
ATOM   3797  N  N     . GLY   B 1  45  ? 17.656  55.095  -10.037 1.00 40.42  ? 45  GLY   C N     1 
ATOM   3798  C  CA    . GLY   B 1  45  ? 16.714  55.282  -8.948  1.00 42.86  ? 45  GLY   C CA    1 
ATOM   3799  C  C     . GLY   B 1  45  ? 17.048  54.349  -7.799  1.00 49.83  ? 45  GLY   C C     1 
ATOM   3800  O  O     . GLY   B 1  45  ? 17.744  53.340  -7.947  1.00 45.81  ? 45  GLY   C O     1 
ATOM   3801  N  N     . ASP   B 1  46  ? 16.563  54.712  -6.605  1.00 44.13  ? 46  ASP   C N     1 
ATOM   3802  C  CA    . ASP   B 1  46  ? 16.681  53.842  -5.440  1.00 44.65  ? 46  ASP   C CA    1 
ATOM   3803  C  C     . ASP   B 1  46  ? 15.306  53.397  -4.942  1.00 43.46  ? 46  ASP   C C     1 
ATOM   3804  O  O     . ASP   B 1  46  ? 15.135  53.095  -3.757  1.00 39.99  ? 46  ASP   C O     1 
ATOM   3805  C  CB    . ASP   B 1  46  ? 17.489  54.500  -4.314  1.00 41.57  ? 46  ASP   C CB    1 
ATOM   3806  C  CG    . ASP   B 1  46  ? 18.584  53.566  -3.757  1.00 60.34  ? 46  ASP   C CG    1 
ATOM   3807  O  OD1   . ASP   B 1  46  ? 19.290  53.932  -2.782  1.00 65.31  ? 46  ASP   C OD1   1 
ATOM   3808  O  OD2   . ASP   B 1  46  ? 18.751  52.456  -4.324  1.00 64.11  ? 46  ASP   C OD2   1 
ATOM   3809  N  N     . ASP   B 1  47  ? 14.322  53.322  -5.839  1.00 35.96  ? 47  ASP   C N     1 
ATOM   3810  C  CA    . ASP   B 1  47  ? 13.017  52.824  -5.448  1.00 33.41  ? 47  ASP   C CA    1 
ATOM   3811  C  C     . ASP   B 1  47  ? 13.148  51.363  -5.011  1.00 36.74  ? 47  ASP   C C     1 
ATOM   3812  O  O     . ASP   B 1  47  ? 14.174  50.713  -5.223  1.00 31.72  ? 47  ASP   C O     1 
ATOM   3813  C  CB    . ASP   B 1  47  ? 12.005  52.981  -6.585  1.00 30.82  ? 47  ASP   C CB    1 
ATOM   3814  C  CG    . ASP   B 1  47  ? 11.846  54.434  -7.052  1.00 48.54  ? 47  ASP   C CG    1 
ATOM   3815  O  OD1   . ASP   B 1  47  ? 11.408  55.287  -6.246  1.00 43.30  ? 47  ASP   C OD1   1 
ATOM   3816  O  OD2   . ASP   B 1  47  ? 12.152  54.724  -8.236  1.00 57.47  ? 47  ASP   C OD2   1 
ATOM   3817  N  N     . SER   B 1  48  ? 12.099  50.860  -4.354  1.00 33.34  ? 48  SER   C N     1 
ATOM   3818  C  CA    . SER   B 1  48  ? 12.166  49.518  -3.788  1.00 25.40  ? 48  SER   C CA    1 
ATOM   3819  C  C     . SER   B 1  48  ? 12.291  48.460  -4.874  1.00 33.47  ? 48  SER   C C     1 
ATOM   3820  O  O     . SER   B 1  48  ? 13.085  47.515  -4.737  1.00 31.01  ? 48  SER   C O     1 
ATOM   3821  C  CB    . SER   B 1  48  ? 10.948  49.254  -2.911  1.00 29.98  ? 48  SER   C CB    1 
ATOM   3822  O  OG    . SER   B 1  48  ? 11.052  49.961  -1.686  1.00 42.45  ? 48  SER   C OG    1 
ATOM   3823  N  N     . PHE   B 1  49  ? 11.528  48.604  -5.969  1.00 30.13  ? 49  PHE   C N     1 
ATOM   3824  C  CA    . PHE   B 1  49  ? 11.635  47.651  -7.075  1.00 32.12  ? 49  PHE   C CA    1 
ATOM   3825  C  C     . PHE   B 1  49  ? 13.047  47.596  -7.660  1.00 30.40  ? 49  PHE   C C     1 
ATOM   3826  O  O     . PHE   B 1  49  ? 13.400  46.626  -8.342  1.00 23.68  ? 49  PHE   C O     1 
ATOM   3827  C  CB    . PHE   B 1  49  ? 10.620  47.993  -8.170  1.00 35.10  ? 49  PHE   C CB    1 
ATOM   3828  C  CG    . PHE   B 1  49  ? 10.831  49.345  -8.802  1.00 40.95  ? 49  PHE   C CG    1 
ATOM   3829  C  CD1   . PHE   B 1  49  ? 11.696  49.498  -9.874  1.00 32.63  ? 49  PHE   C CD1   1 
ATOM   3830  C  CD2   . PHE   B 1  49  ? 10.162  50.460  -8.322  1.00 38.03  ? 49  PHE   C CD2   1 
ATOM   3831  C  CE1   . PHE   B 1  49  ? 11.890  50.734  -10.435 1.00 35.22  ? 49  PHE   C CE1   1 
ATOM   3832  C  CE2   . PHE   B 1  49  ? 10.352  51.700  -8.893  1.00 31.67  ? 49  PHE   C CE2   1 
ATOM   3833  C  CZ    . PHE   B 1  49  ? 11.219  51.840  -9.940  1.00 35.57  ? 49  PHE   C CZ    1 
ATOM   3834  N  N     . ASN   B 1  50  ? 13.865  48.609  -7.400  1.00 31.84  ? 50  ASN   C N     1 
ATOM   3835  C  CA    . ASN   B 1  50  ? 15.229  48.623  -7.901  1.00 30.32  ? 50  ASN   C CA    1 
ATOM   3836  C  C     . ASN   B 1  50  ? 16.101  47.567  -7.243  1.00 20.62  ? 50  ASN   C C     1 
ATOM   3837  O  O     . ASN   B 1  50  ? 17.231  47.347  -7.692  1.00 25.48  ? 50  ASN   C O     1 
ATOM   3838  C  CB    . ASN   B 1  50  ? 15.829  50.023  -7.710  1.00 31.81  ? 50  ASN   C CB    1 
ATOM   3839  C  CG    . ASN   B 1  50  ? 15.414  50.985  -8.816  1.00 37.24  ? 50  ASN   C CG    1 
ATOM   3840  O  OD1   . ASN   B 1  50  ? 14.802  52.029  -8.577  1.00 41.20  ? 50  ASN   C OD1   1 
ATOM   3841  N  ND2   . ASN   B 1  50  ? 15.745  50.623  -10.041 1.00 29.61  ? 50  ASN   C ND2   1 
ATOM   3842  N  N     . THR   B 1  51  ? 15.616  46.915  -6.193  1.00 20.70  ? 51  THR   C N     1 
ATOM   3843  C  CA    . THR   B 1  51  ? 16.382  45.828  -5.592  1.00 28.56  ? 51  THR   C CA    1 
ATOM   3844  C  C     . THR   B 1  51  ? 16.439  44.609  -6.509  1.00 31.11  ? 51  THR   C C     1 
ATOM   3845  O  O     . THR   B 1  51  ? 17.370  43.800  -6.411  1.00 34.05  ? 51  THR   C O     1 
ATOM   3846  C  CB    . THR   B 1  51  ? 15.779  45.456  -4.232  1.00 29.23  ? 51  THR   C CB    1 
ATOM   3847  O  OG1   . THR   B 1  51  ? 14.504  44.836  -4.420  1.00 26.32  ? 51  THR   C OG1   1 
ATOM   3848  C  CG2   . THR   B 1  51  ? 15.572  46.704  -3.374  1.00 24.45  ? 51  THR   C CG2   1 
ATOM   3849  N  N     . PHE   B 1  52  ? 15.478  44.487  -7.421  1.00 26.51  ? 52  PHE   C N     1 
ATOM   3850  C  CA    . PHE   B 1  52  ? 15.450  43.416  -8.389  1.00 22.92  ? 52  PHE   C CA    1 
ATOM   3851  C  C     . PHE   B 1  52  ? 15.568  43.860  -9.847  1.00 26.78  ? 52  PHE   C C     1 
ATOM   3852  O  O     . PHE   B 1  52  ? 15.711  42.992  -10.716 1.00 30.30  ? 52  PHE   C O     1 
ATOM   3853  C  CB    . PHE   B 1  52  ? 14.156  42.618  -8.227  1.00 24.66  ? 52  PHE   C CB    1 
ATOM   3854  C  CG    . PHE   B 1  52  ? 14.197  41.605  -7.120  1.00 30.79  ? 52  PHE   C CG    1 
ATOM   3855  C  CD1   . PHE   B 1  52  ? 14.349  41.999  -5.804  1.00 26.87  ? 52  PHE   C CD1   1 
ATOM   3856  C  CD2   . PHE   B 1  52  ? 14.041  40.252  -7.398  1.00 26.15  ? 52  PHE   C CD2   1 
ATOM   3857  C  CE1   . PHE   B 1  52  ? 14.363  41.055  -4.787  1.00 25.86  ? 52  PHE   C CE1   1 
ATOM   3858  C  CE2   . PHE   B 1  52  ? 14.044  39.303  -6.372  1.00 30.93  ? 52  PHE   C CE2   1 
ATOM   3859  C  CZ    . PHE   B 1  52  ? 14.212  39.706  -5.071  1.00 23.82  ? 52  PHE   C CZ    1 
ATOM   3860  N  N     . PHE   B 1  53  ? 15.494  45.160  -10.153 1.00 22.29  ? 53  PHE   C N     1 
ATOM   3861  C  CA    . PHE   B 1  53  ? 15.536  45.646  -11.534 1.00 27.64  ? 53  PHE   C CA    1 
ATOM   3862  C  C     . PHE   B 1  53  ? 16.540  46.794  -11.667 1.00 29.74  ? 53  PHE   C C     1 
ATOM   3863  O  O     . PHE   B 1  53  ? 16.409  47.825  -10.997 1.00 27.03  ? 53  PHE   C O     1 
ATOM   3864  C  CB    . PHE   B 1  53  ? 14.153  46.126  -12.007 1.00 26.79  ? 53  PHE   C CB    1 
ATOM   3865  C  CG    . PHE   B 1  53  ? 13.130  45.052  -12.130 1.00 17.32  ? 53  PHE   C CG    1 
ATOM   3866  C  CD1   . PHE   B 1  53  ? 13.014  44.328  -13.284 1.00 25.21  ? 53  PHE   C CD1   1 
ATOM   3867  C  CD2   . PHE   B 1  53  ? 12.255  44.790  -11.100 1.00 25.19  ? 53  PHE   C CD2   1 
ATOM   3868  C  CE1   . PHE   B 1  53  ? 12.055  43.347  -13.410 1.00 29.48  ? 53  PHE   C CE1   1 
ATOM   3869  C  CE2   . PHE   B 1  53  ? 11.304  43.796  -11.193 1.00 20.98  ? 53  PHE   C CE2   1 
ATOM   3870  C  CZ    . PHE   B 1  53  ? 11.195  43.078  -12.358 1.00 28.02  ? 53  PHE   C CZ    1 
ATOM   3871  N  N     . SER   B 1  54  ? 17.517  46.638  -12.554 1.00 28.21  ? 54  SER   C N     1 
ATOM   3872  C  CA    . SER   B 1  54  ? 18.353  47.766  -12.919 1.00 27.97  ? 54  SER   C CA    1 
ATOM   3873  C  C     . SER   B 1  54  ? 17.642  48.595  -13.994 1.00 36.75  ? 54  SER   C C     1 
ATOM   3874  O  O     . SER   B 1  54  ? 16.680  48.144  -14.612 1.00 39.64  ? 54  SER   C O     1 
ATOM   3875  C  CB    . SER   B 1  54  ? 19.717  47.279  -13.392 1.00 22.21  ? 54  SER   C CB    1 
ATOM   3876  O  OG    . SER   B 1  54  ? 19.636  46.673  -14.660 1.00 36.67  ? 54  SER   C OG    1 
ATOM   3877  N  N     . GLU   B 1  55  ? 18.099  49.833  -14.188 1.00 38.76  ? 55  GLU   C N     1 
ATOM   3878  C  CA    . GLU   B 1  55  ? 17.505  50.760  -15.147 1.00 36.29  ? 55  GLU   C CA    1 
ATOM   3879  C  C     . GLU   B 1  55  ? 18.557  51.138  -16.189 1.00 36.60  ? 55  GLU   C C     1 
ATOM   3880  O  O     . GLU   B 1  55  ? 19.695  51.448  -15.824 1.00 46.53  ? 55  GLU   C O     1 
ATOM   3881  C  CB    . GLU   B 1  55  ? 16.992  52.037  -14.445 1.00 35.21  ? 55  GLU   C CB    1 
ATOM   3882  C  CG    . GLU   B 1  55  ? 15.921  51.898  -13.348 1.00 24.98  ? 55  GLU   C CG    1 
ATOM   3883  C  CD    . GLU   B 1  55  ? 15.048  53.168  -13.255 1.00 37.96  ? 55  GLU   C CD    1 
ATOM   3884  O  OE1   . GLU   B 1  55  ? 14.862  53.791  -14.320 1.00 47.07  ? 55  GLU   C OE1   1 
ATOM   3885  O  OE2   . GLU   B 1  55  ? 14.543  53.560  -12.168 1.00 31.27  ? 55  GLU   C OE2   1 
ATOM   3886  N  N     . THR   B 1  56  ? 18.195  51.119  -17.481 1.00 41.28  ? 56  THR   C N     1 
ATOM   3887  C  CA    . THR   B 1  56  ? 19.054  51.683  -18.529 1.00 38.40  ? 56  THR   C CA    1 
ATOM   3888  C  C     . THR   B 1  56  ? 18.653  53.129  -18.837 1.00 36.74  ? 56  THR   C C     1 
ATOM   3889  O  O     . THR   B 1  56  ? 17.541  53.569  -18.533 1.00 36.10  ? 56  THR   C O     1 
ATOM   3890  C  CB    . THR   B 1  56  ? 19.023  50.865  -19.838 1.00 36.33  ? 56  THR   C CB    1 
ATOM   3891  O  OG1   . THR   B 1  56  ? 17.821  51.144  -20.574 1.00 42.87  ? 56  THR   C OG1   1 
ATOM   3892  C  CG2   . THR   B 1  56  ? 19.150  49.361  -19.585 1.00 27.88  ? 56  THR   C CG2   1 
ATOM   3893  N  N     . GLY   B 1  57  ? 19.590  53.878  -19.437 1.00 47.21  ? 57  GLY   C N     1 
ATOM   3894  C  CA    . GLY   B 1  57  ? 19.260  55.223  -19.902 1.00 41.40  ? 57  GLY   C CA    1 
ATOM   3895  C  C     . GLY   B 1  57  ? 17.985  55.243  -20.725 1.00 42.28  ? 57  GLY   C C     1 
ATOM   3896  O  O     . GLY   B 1  57  ? 17.094  56.070  -20.499 1.00 33.35  ? 57  GLY   C O     1 
ATOM   3897  N  N     . ALA   B 1  58  ? 17.861  54.296  -21.661 1.00 37.18  ? 58  ALA   C N     1 
ATOM   3898  C  CA    . ALA   B 1  58  ? 16.659  54.168  -22.475 1.00 42.72  ? 58  ALA   C CA    1 
ATOM   3899  C  C     . ALA   B 1  58  ? 15.401  53.915  -21.647 1.00 41.37  ? 58  ALA   C C     1 
ATOM   3900  O  O     . ALA   B 1  58  ? 14.298  53.923  -22.206 1.00 41.20  ? 58  ALA   C O     1 
ATOM   3901  C  CB    . ALA   B 1  58  ? 16.851  53.046  -23.510 1.00 42.80  ? 58  ALA   C CB    1 
ATOM   3902  N  N     . GLY   B 1  59  ? 15.529  53.680  -20.345 1.00 39.98  ? 59  GLY   C N     1 
ATOM   3903  C  CA    . GLY   B 1  59  ? 14.358  53.437  -19.526 1.00 40.36  ? 59  GLY   C CA    1 
ATOM   3904  C  C     . GLY   B 1  59  ? 13.858  52.008  -19.516 1.00 44.82  ? 59  GLY   C C     1 
ATOM   3905  O  O     . GLY   B 1  59  ? 12.677  51.778  -19.201 1.00 37.06  ? 59  GLY   C O     1 
ATOM   3906  N  N     . LYS   B 1  60  ? 14.717  51.041  -19.859 1.00 31.26  ? 60  LYS   C N     1 
ATOM   3907  C  CA    . LYS   B 1  60  ? 14.385  49.628  -19.756 1.00 35.13  ? 60  LYS   C CA    1 
ATOM   3908  C  C     . LYS   B 1  60  ? 14.729  49.145  -18.344 1.00 35.47  ? 60  LYS   C C     1 
ATOM   3909  O  O     . LYS   B 1  60  ? 15.873  49.275  -17.896 1.00 32.37  ? 60  LYS   C O     1 
ATOM   3910  C  CB    . LYS   B 1  60  ? 15.127  48.829  -20.834 1.00 34.09  ? 60  LYS   C CB    1 
ATOM   3911  C  CG    . LYS   B 1  60  ? 15.110  47.310  -20.654 1.00 31.74  ? 60  LYS   C CG    1 
ATOM   3912  C  CD    . LYS   B 1  60  ? 14.975  46.545  -21.969 1.00 29.62  ? 60  LYS   C CD    1 
ATOM   3913  C  CE    . LYS   B 1  60  ? 16.335  46.077  -22.478 1.00 42.40  ? 60  LYS   C CE    1 
ATOM   3914  N  NZ    . LYS   B 1  60  ? 16.254  44.837  -23.299 1.00 39.75  ? 60  LYS   C NZ    1 
ATOM   3915  N  N     . HIS   B 1  61  ? 13.728  48.630  -17.630 1.00 27.30  ? 61  HIS   C N     1 
ATOM   3916  C  CA    . HIS   B 1  61  ? 13.941  47.985  -16.339 1.00 29.34  ? 61  HIS   C CA    1 
ATOM   3917  C  C     . HIS   B 1  61  ? 14.315  46.527  -16.580 1.00 31.16  ? 61  HIS   C C     1 
ATOM   3918  O  O     . HIS   B 1  61  ? 13.581  45.785  -17.236 1.00 36.59  ? 61  HIS   C O     1 
ATOM   3919  C  CB    . HIS   B 1  61  ? 12.702  48.097  -15.453 1.00 25.17  ? 61  HIS   C CB    1 
ATOM   3920  C  CG    . HIS   B 1  61  ? 12.343  49.507  -15.093 1.00 33.03  ? 61  HIS   C CG    1 
ATOM   3921  N  ND1   . HIS   B 1  61  ? 11.986  50.449  -16.033 1.00 36.51  ? 61  HIS   C ND1   1 
ATOM   3922  C  CD2   . HIS   B 1  61  ? 12.282  50.136  -13.895 1.00 35.04  ? 61  HIS   C CD2   1 
ATOM   3923  C  CE1   . HIS   B 1  61  ? 11.716  51.595  -15.433 1.00 31.68  ? 61  HIS   C CE1   1 
ATOM   3924  N  NE2   . HIS   B 1  61  ? 11.882  51.431  -14.134 1.00 34.50  ? 61  HIS   C NE2   1 
ATOM   3925  N  N     . VAL   B 1  62  ? 15.473  46.123  -16.056 1.00 26.52  ? 62  VAL   C N     1 
ATOM   3926  C  CA    . VAL   B 1  62  ? 16.141  44.897  -16.455 1.00 28.97  ? 62  VAL   C CA    1 
ATOM   3927  C  C     . VAL   B 1  62  ? 16.295  44.020  -15.218 1.00 31.94  ? 62  VAL   C C     1 
ATOM   3928  O  O     . VAL   B 1  62  ? 16.853  44.474  -14.219 1.00 30.57  ? 62  VAL   C O     1 
ATOM   3929  C  CB    . VAL   B 1  62  ? 17.517  45.178  -17.092 1.00 31.79  ? 62  VAL   C CB    1 
ATOM   3930  C  CG1   . VAL   B 1  62  ? 18.074  43.928  -17.755 1.00 31.64  ? 62  VAL   C CG1   1 
ATOM   3931  C  CG2   . VAL   B 1  62  ? 17.402  46.330  -18.096 1.00 37.29  ? 62  VAL   C CG2   1 
ATOM   3932  N  N     . PRO   B 1  63  ? 15.800  42.780  -15.223 1.00 26.64  ? 63  PRO   C N     1 
ATOM   3933  C  CA    . PRO   B 1  63  ? 16.003  41.918  -14.061 1.00 23.57  ? 63  PRO   C CA    1 
ATOM   3934  C  C     . PRO   B 1  63  ? 17.485  41.755  -13.753 1.00 29.63  ? 63  PRO   C C     1 
ATOM   3935  O  O     . PRO   B 1  63  ? 18.315  41.595  -14.657 1.00 33.67  ? 63  PRO   C O     1 
ATOM   3936  C  CB    . PRO   B 1  63  ? 15.368  40.593  -14.493 1.00 27.85  ? 63  PRO   C CB    1 
ATOM   3937  C  CG    . PRO   B 1  63  ? 14.398  40.960  -15.540 1.00 25.22  ? 63  PRO   C CG    1 
ATOM   3938  C  CD    . PRO   B 1  63  ? 15.012  42.103  -16.268 1.00 34.53  ? 63  PRO   C CD    1 
ATOM   3939  N  N     . ARG   B 1  64  ? 17.812  41.826  -12.457 1.00 26.02  ? 64  ARG   C N     1 
ATOM   3940  C  CA    . ARG   B 1  64  ? 19.166  41.576  -11.964 1.00 19.96  ? 64  ARG   C CA    1 
ATOM   3941  C  C     . ARG   B 1  64  ? 19.380  40.074  -11.812 1.00 25.38  ? 64  ARG   C C     1 
ATOM   3942  O  O     . ARG   B 1  64  ? 19.586  39.557  -10.724 1.00 29.94  ? 64  ARG   C O     1 
ATOM   3943  C  CB    . ARG   B 1  64  ? 19.397  42.288  -10.637 1.00 23.11  ? 64  ARG   C CB    1 
ATOM   3944  C  CG    . ARG   B 1  64  ? 19.170  43.782  -10.593 1.00 24.14  ? 64  ARG   C CG    1 
ATOM   3945  C  CD    . ARG   B 1  64  ? 19.355  44.298  -9.171  1.00 28.96  ? 64  ARG   C CD    1 
ATOM   3946  N  NE    . ARG   B 1  64  ? 19.197  45.745  -9.058  1.00 28.32  ? 64  ARG   C NE    1 
ATOM   3947  C  CZ    . ARG   B 1  64  ? 20.089  46.631  -9.477  1.00 26.30  ? 64  ARG   C CZ    1 
ATOM   3948  N  NH1   . ARG   B 1  64  ? 21.208  46.252  -10.082 1.00 21.61  ? 64  ARG   C NH1   1 
ATOM   3949  N  NH2   . ARG   B 1  64  ? 19.852  47.925  -9.281  1.00 25.40  ? 64  ARG   C NH2   1 
ATOM   3950  N  N     . ALA   B 1  65  ? 19.296  39.366  -12.928 1.00 25.90  ? 65  ALA   C N     1 
ATOM   3951  C  CA    . ALA   B 1  65  ? 19.248  37.919  -12.881 1.00 21.48  ? 65  ALA   C CA    1 
ATOM   3952  C  C     . ALA   B 1  65  ? 20.055  37.327  -14.026 1.00 26.33  ? 65  ALA   C C     1 
ATOM   3953  O  O     . ALA   B 1  65  ? 20.184  37.918  -15.103 1.00 25.04  ? 65  ALA   C O     1 
ATOM   3954  C  CB    . ALA   B 1  65  ? 17.799  37.439  -12.929 1.00 28.42  ? 65  ALA   C CB    1 
ATOM   3955  N  N     . VAL   B 1  66  ? 20.620  36.159  -13.767 1.00 29.01  ? 66  VAL   C N     1 
ATOM   3956  C  CA    . VAL   B 1  66  ? 21.301  35.365  -14.776 1.00 32.37  ? 66  VAL   C CA    1 
ATOM   3957  C  C     . VAL   B 1  66  ? 20.564  34.047  -14.888 1.00 27.05  ? 66  VAL   C C     1 
ATOM   3958  O  O     . VAL   B 1  66  ? 20.223  33.439  -13.872 1.00 32.67  ? 66  VAL   C O     1 
ATOM   3959  C  CB    . VAL   B 1  66  ? 22.780  35.115  -14.423 1.00 27.23  ? 66  VAL   C CB    1 
ATOM   3960  C  CG1   . VAL   B 1  66  ? 23.257  33.858  -15.104 1.00 29.62  ? 66  VAL   C CG1   1 
ATOM   3961  C  CG2   . VAL   B 1  66  ? 23.623  36.261  -14.853 1.00 22.81  ? 66  VAL   C CG2   1 
ATOM   3962  N  N     . PHE   B 1  67  ? 20.315  33.616  -16.114 1.00 27.63  ? 67  PHE   C N     1 
ATOM   3963  C  CA    . PHE   B 1  67  ? 19.857  32.264  -16.395 1.00 29.54  ? 67  PHE   C CA    1 
ATOM   3964  C  C     . PHE   B 1  67  ? 21.027  31.448  -16.915 1.00 24.49  ? 67  PHE   C C     1 
ATOM   3965  O  O     . PHE   B 1  67  ? 21.816  31.931  -17.719 1.00 28.96  ? 67  PHE   C O     1 
ATOM   3966  C  CB    . PHE   B 1  67  ? 18.723  32.275  -17.409 1.00 26.39  ? 67  PHE   C CB    1 
ATOM   3967  C  CG    . PHE   B 1  67  ? 17.488  32.924  -16.893 1.00 24.97  ? 67  PHE   C CG    1 
ATOM   3968  C  CD1   . PHE   B 1  67  ? 17.488  34.251  -16.536 1.00 29.59  ? 67  PHE   C CD1   1 
ATOM   3969  C  CD2   . PHE   B 1  67  ? 16.329  32.209  -16.755 1.00 27.89  ? 67  PHE   C CD2   1 
ATOM   3970  C  CE1   . PHE   B 1  67  ? 16.339  34.849  -16.055 1.00 36.80  ? 67  PHE   C CE1   1 
ATOM   3971  C  CE2   . PHE   B 1  67  ? 15.185  32.799  -16.268 1.00 27.41  ? 67  PHE   C CE2   1 
ATOM   3972  C  CZ    . PHE   B 1  67  ? 15.185  34.115  -15.920 1.00 30.97  ? 67  PHE   C CZ    1 
ATOM   3973  N  N     . VAL   B 1  68  ? 21.162  30.224  -16.434 1.00 20.41  ? 68  VAL   C N     1 
ATOM   3974  C  CA    A VAL   B 1  68  ? 22.299  29.385  -16.786 0.45 19.33  ? 68  VAL   C CA    1 
ATOM   3975  C  CA    B VAL   B 1  68  ? 22.296  29.389  -16.797 0.55 19.46  ? 68  VAL   C CA    1 
ATOM   3976  C  C     . VAL   B 1  68  ? 21.806  27.954  -16.901 1.00 19.97  ? 68  VAL   C C     1 
ATOM   3977  O  O     . VAL   B 1  68  ? 21.318  27.387  -15.922 1.00 22.76  ? 68  VAL   C O     1 
ATOM   3978  C  CB    A VAL   B 1  68  ? 23.431  29.483  -15.747 0.45 21.90  ? 68  VAL   C CB    1 
ATOM   3979  C  CB    B VAL   B 1  68  ? 23.455  29.507  -15.787 0.55 21.75  ? 68  VAL   C CB    1 
ATOM   3980  C  CG1   A VAL   B 1  68  ? 24.577  28.543  -16.097 0.45 22.10  ? 68  VAL   C CG1   1 
ATOM   3981  C  CG1   B VAL   B 1  68  ? 22.939  29.434  -14.364 0.55 20.67  ? 68  VAL   C CG1   1 
ATOM   3982  C  CG2   A VAL   B 1  68  ? 23.919  30.907  -15.651 0.45 22.85  ? 68  VAL   C CG2   1 
ATOM   3983  C  CG2   B VAL   B 1  68  ? 24.504  28.431  -16.030 0.55 22.09  ? 68  VAL   C CG2   1 
ATOM   3984  N  N     . ASP   B 1  69  ? 21.912  27.377  -18.089 1.00 29.11  ? 69  ASP   C N     1 
ATOM   3985  C  CA    . ASP   B 1  69  ? 21.601  25.972  -18.314 1.00 23.56  ? 69  ASP   C CA    1 
ATOM   3986  C  C     . ASP   B 1  69  ? 22.727  25.366  -19.131 1.00 22.15  ? 69  ASP   C C     1 
ATOM   3987  O  O     . ASP   B 1  69  ? 23.308  26.030  -19.996 1.00 22.54  ? 69  ASP   C O     1 
ATOM   3988  C  CB    . ASP   B 1  69  ? 20.260  25.787  -19.033 1.00 19.47  ? 69  ASP   C CB    1 
ATOM   3989  C  CG    . ASP   B 1  69  ? 19.707  24.383  -18.881 1.00 21.75  ? 69  ASP   C CG    1 
ATOM   3990  O  OD1   . ASP   B 1  69  ? 20.348  23.567  -18.161 1.00 16.65  ? 69  ASP   C OD1   1 
ATOM   3991  O  OD2   . ASP   B 1  69  ? 18.644  24.099  -19.496 1.00 22.08  ? 69  ASP   C OD2   1 
ATOM   3992  N  N     . LEU   B 1  70  ? 23.052  24.117  -18.839 1.00 19.25  ? 70  LEU   C N     1 
ATOM   3993  C  CA    . LEU   B 1  70  ? 24.080  23.435  -19.606 1.00 19.87  ? 70  LEU   C CA    1 
ATOM   3994  C  C     . LEU   B 1  70  ? 23.605  23.010  -20.993 1.00 24.66  ? 70  LEU   C C     1 
ATOM   3995  O  O     . LEU   B 1  70  ? 24.407  22.453  -21.752 1.00 28.68  ? 70  LEU   C O     1 
ATOM   3996  C  CB    . LEU   B 1  70  ? 24.592  22.217  -18.835 1.00 21.64  ? 70  LEU   C CB    1 
ATOM   3997  C  CG    . LEU   B 1  70  ? 25.421  22.478  -17.573 1.00 21.55  ? 70  LEU   C CG    1 
ATOM   3998  C  CD1   . LEU   B 1  70  ? 26.444  21.380  -17.358 1.00 22.22  ? 70  LEU   C CD1   1 
ATOM   3999  C  CD2   . LEU   B 1  70  ? 26.087  23.842  -17.616 1.00 20.32  ? 70  LEU   C CD2   1 
ATOM   4000  N  N     . GLU   B 1  71  ? 22.345  23.261  -21.351 1.00 18.25  ? 71  GLU   C N     1 
ATOM   4001  C  CA    . GLU   B 1  71  ? 21.866  23.025  -22.704 1.00 24.34  ? 71  GLU   C CA    1 
ATOM   4002  C  C     . GLU   B 1  71  ? 20.863  24.105  -23.106 1.00 30.40  ? 71  GLU   C C     1 
ATOM   4003  O  O     . GLU   B 1  71  ? 20.173  24.670  -22.242 1.00 37.77  ? 71  GLU   C O     1 
ATOM   4004  C  CB    . GLU   B 1  71  ? 21.261  21.622  -22.841 1.00 24.31  ? 71  GLU   C CB    1 
ATOM   4005  C  CG    . GLU   B 1  71  ? 20.059  21.347  -22.019 1.00 18.21  ? 71  GLU   C CG    1 
ATOM   4006  C  CD    . GLU   B 1  71  ? 18.797  21.395  -22.829 1.00 24.77  ? 71  GLU   C CD    1 
ATOM   4007  O  OE1   . GLU   B 1  71  ? 18.899  21.581  -24.060 1.00 36.46  ? 71  GLU   C OE1   1 
ATOM   4008  O  OE2   . GLU   B 1  71  ? 17.703  21.233  -22.246 1.00 26.50  ? 71  GLU   C OE2   1 
ATOM   4009  N  N     . PRO   B 1  72  ? 20.750  24.411  -24.430 1.00 24.97  ? 72  PRO   C N     1 
ATOM   4010  C  CA    . PRO   B 1  72  ? 20.109  25.663  -24.850 1.00 25.24  ? 72  PRO   C CA    1 
ATOM   4011  C  C     . PRO   B 1  72  ? 18.591  25.667  -24.994 1.00 30.79  ? 72  PRO   C C     1 
ATOM   4012  O  O     . PRO   B 1  72  ? 17.989  26.749  -25.029 1.00 26.15  ? 72  PRO   C O     1 
ATOM   4013  C  CB    . PRO   B 1  72  ? 20.771  25.926  -26.208 1.00 29.32  ? 72  PRO   C CB    1 
ATOM   4014  C  CG    . PRO   B 1  72  ? 21.013  24.602  -26.731 1.00 25.31  ? 72  PRO   C CG    1 
ATOM   4015  C  CD    . PRO   B 1  72  ? 21.449  23.768  -25.555 1.00 24.00  ? 72  PRO   C CD    1 
ATOM   4016  N  N     . THR   B 1  73  ? 17.942  24.509  -25.097 1.00 24.55  ? 73  THR   C N     1 
ATOM   4017  C  CA    . THR   B 1  73  ? 16.533  24.527  -25.480 1.00 24.99  ? 73  THR   C CA    1 
ATOM   4018  C  C     . THR   B 1  73  ? 15.686  25.339  -24.507 1.00 31.06  ? 73  THR   C C     1 
ATOM   4019  O  O     . THR   B 1  73  ? 14.869  26.166  -24.935 1.00 39.84  ? 73  THR   C O     1 
ATOM   4020  C  CB    . THR   B 1  73  ? 16.005  23.115  -25.603 1.00 26.79  ? 73  THR   C CB    1 
ATOM   4021  O  OG1   . THR   B 1  73  ? 16.427  22.389  -24.455 1.00 36.38  ? 73  THR   C OG1   1 
ATOM   4022  C  CG2   . THR   B 1  73  ? 16.583  22.482  -26.844 1.00 29.72  ? 73  THR   C CG2   1 
ATOM   4023  N  N     . VAL   B 1  74  ? 15.858  25.123  -23.195 1.00 31.19  ? 74  VAL   C N     1 
ATOM   4024  C  CA    . VAL   B 1  74  ? 14.944  25.732  -22.224 1.00 25.85  ? 74  VAL   C CA    1 
ATOM   4025  C  C     . VAL   B 1  74  ? 15.122  27.247  -22.193 1.00 31.10  ? 74  VAL   C C     1 
ATOM   4026  O  O     . VAL   B 1  74  ? 14.150  28.007  -22.142 1.00 32.32  ? 74  VAL   C O     1 
ATOM   4027  C  CB    . VAL   B 1  74  ? 15.156  25.128  -20.827 1.00 27.82  ? 74  VAL   C CB    1 
ATOM   4028  C  CG1   . VAL   B 1  74  ? 14.046  25.563  -19.890 1.00 22.49  ? 74  VAL   C CG1   1 
ATOM   4029  C  CG2   . VAL   B 1  74  ? 15.267  23.601  -20.889 1.00 35.10  ? 74  VAL   C CG2   1 
ATOM   4030  N  N     . ILE   B 1  75  ? 16.370  27.708  -22.202 1.00 27.87  ? 75  ILE   C N     1 
ATOM   4031  C  CA    . ILE   B 1  75  ? 16.628  29.141  -22.195 1.00 23.03  ? 75  ILE   C CA    1 
ATOM   4032  C  C     . ILE   B 1  75  ? 16.282  29.752  -23.552 1.00 29.76  ? 75  ILE   C C     1 
ATOM   4033  O  O     . ILE   B 1  75  ? 15.665  30.821  -23.616 1.00 29.37  ? 75  ILE   C O     1 
ATOM   4034  C  CB    . ILE   B 1  75  ? 18.093  29.389  -21.770 1.00 24.44  ? 75  ILE   C CB    1 
ATOM   4035  C  CG1   . ILE   B 1  75  ? 18.171  29.481  -20.235 1.00 22.05  ? 75  ILE   C CG1   1 
ATOM   4036  C  CG2   . ILE   B 1  75  ? 18.744  30.589  -22.514 1.00 20.50  ? 75  ILE   C CG2   1 
ATOM   4037  C  CD1   . ILE   B 1  75  ? 19.524  29.115  -19.623 1.00 23.59  ? 75  ILE   C CD1   1 
ATOM   4038  N  N     . ASP   B 1  76  ? 16.643  29.071  -24.658 1.00 30.86  ? 76  ASP   C N     1 
ATOM   4039  C  CA    . ASP   B 1  76  ? 16.262  29.523  -26.003 1.00 27.55  ? 76  ASP   C CA    1 
ATOM   4040  C  C     . ASP   B 1  76  ? 14.804  29.957  -26.050 1.00 26.71  ? 76  ASP   C C     1 
ATOM   4041  O  O     . ASP   B 1  76  ? 14.443  30.849  -26.823 1.00 33.17  ? 76  ASP   C O     1 
ATOM   4042  C  CB    . ASP   B 1  76  ? 16.488  28.412  -27.055 1.00 26.07  ? 76  ASP   C CB    1 
ATOM   4043  C  CG    . ASP   B 1  76  ? 17.967  28.240  -27.479 1.00 27.55  ? 76  ASP   C CG    1 
ATOM   4044  O  OD1   . ASP   B 1  76  ? 18.839  29.082  -27.155 1.00 31.97  ? 76  ASP   C OD1   1 
ATOM   4045  O  OD2   . ASP   B 1  76  ? 18.259  27.232  -28.154 1.00 28.65  ? 76  ASP   C OD2   1 
ATOM   4046  N  N     . GLU   B 1  77  ? 13.950  29.333  -25.240 1.00 25.45  ? 77  GLU   C N     1 
ATOM   4047  C  CA    . GLU   B 1  77  ? 12.560  29.752  -25.162 1.00 31.91  ? 77  GLU   C CA    1 
ATOM   4048  C  C     . GLU   B 1  77  ? 12.416  31.131  -24.528 1.00 34.84  ? 77  GLU   C C     1 
ATOM   4049  O  O     . GLU   B 1  77  ? 11.528  31.899  -24.918 1.00 43.86  ? 77  GLU   C O     1 
ATOM   4050  C  CB    . GLU   B 1  77  ? 11.760  28.718  -24.385 1.00 32.13  ? 77  GLU   C CB    1 
ATOM   4051  C  CG    . GLU   B 1  77  ? 11.953  27.323  -24.908 1.00 35.20  ? 77  GLU   C CG    1 
ATOM   4052  C  CD    . GLU   B 1  77  ? 10.767  26.849  -25.708 1.00 47.74  ? 77  GLU   C CD    1 
ATOM   4053  O  OE1   . GLU   B 1  77  ? 10.633  27.243  -26.901 1.00 47.06  ? 77  GLU   C OE1   1 
ATOM   4054  O  OE2   . GLU   B 1  77  ? 9.964   26.086  -25.127 1.00 50.89  ? 77  GLU   C OE2   1 
ATOM   4055  N  N     . VAL   B 1  78  ? 13.262  31.471  -23.560 1.00 26.93  ? 78  VAL   C N     1 
ATOM   4056  C  CA    . VAL   B 1  78  ? 13.274  32.843  -23.063 1.00 32.64  ? 78  VAL   C CA    1 
ATOM   4057  C  C     . VAL   B 1  78  ? 13.714  33.799  -24.162 1.00 34.90  ? 78  VAL   C C     1 
ATOM   4058  O  O     . VAL   B 1  78  ? 13.027  34.778  -24.464 1.00 44.38  ? 78  VAL   C O     1 
ATOM   4059  C  CB    . VAL   B 1  78  ? 14.175  32.972  -21.828 1.00 30.96  ? 78  VAL   C CB    1 
ATOM   4060  C  CG1   . VAL   B 1  78  ? 14.060  34.365  -21.265 1.00 23.54  ? 78  VAL   C CG1   1 
ATOM   4061  C  CG2   . VAL   B 1  78  ? 13.808  31.909  -20.799 1.00 26.07  ? 78  VAL   C CG2   1 
ATOM   4062  N  N     . ARG   B 1  79  ? 14.862  33.525  -24.777 1.00 35.63  ? 79  ARG   C N     1 
ATOM   4063  C  CA    . ARG   B 1  79  ? 15.402  34.313  -25.880 1.00 30.17  ? 79  ARG   C CA    1 
ATOM   4064  C  C     . ARG   B 1  79  ? 14.353  34.744  -26.900 1.00 37.08  ? 79  ARG   C C     1 
ATOM   4065  O  O     . ARG   B 1  79  ? 14.391  35.880  -27.391 1.00 33.30  ? 79  ARG   C O     1 
ATOM   4066  C  CB    . ARG   B 1  79  ? 16.514  33.524  -26.566 1.00 23.53  ? 79  ARG   C CB    1 
ATOM   4067  C  CG    . ARG   B 1  79  ? 17.865  33.661  -25.835 1.00 26.38  ? 79  ARG   C CG    1 
ATOM   4068  C  CD    . ARG   B 1  79  ? 18.785  32.456  -26.044 1.00 25.28  ? 79  ARG   C CD    1 
ATOM   4069  N  NE    . ARG   B 1  79  ? 20.058  32.641  -25.357 1.00 31.47  ? 79  ARG   C NE    1 
ATOM   4070  C  CZ    . ARG   B 1  79  ? 20.949  31.678  -25.166 1.00 31.00  ? 79  ARG   C CZ    1 
ATOM   4071  N  NH1   . ARG   B 1  79  ? 20.755  30.456  -25.639 1.00 30.98  ? 79  ARG   C NH1   1 
ATOM   4072  N  NH2   . ARG   B 1  79  ? 22.054  31.942  -24.469 1.00 24.56  ? 79  ARG   C NH2   1 
ATOM   4073  N  N     . THR   B 1  80  ? 13.394  33.867  -27.200 1.00 39.97  ? 80  THR   C N     1 
ATOM   4074  C  CA    . THR   B 1  80  ? 12.386  34.122  -28.221 1.00 37.83  ? 80  THR   C CA    1 
ATOM   4075  C  C     . THR   B 1  80  ? 10.978  34.314  -27.664 1.00 42.80  ? 80  THR   C C     1 
ATOM   4076  O  O     . THR   B 1  80  ? 10.043  34.513  -28.447 1.00 48.21  ? 80  THR   C O     1 
ATOM   4077  C  CB    . THR   B 1  80  ? 12.375  32.973  -29.227 1.00 37.17  ? 80  THR   C CB    1 
ATOM   4078  O  OG1   . THR   B 1  80  ? 12.038  31.760  -28.543 1.00 41.55  ? 80  THR   C OG1   1 
ATOM   4079  C  CG2   . THR   B 1  80  ? 13.749  32.815  -29.868 1.00 38.90  ? 80  THR   C CG2   1 
ATOM   4080  N  N     . GLY   B 1  81  ? 10.794  34.273  -26.348 1.00 37.25  ? 81  GLY   C N     1 
ATOM   4081  C  CA    . GLY   B 1  81  ? 9.472   34.367  -25.761 1.00 41.90  ? 81  GLY   C CA    1 
ATOM   4082  C  C     . GLY   B 1  81  ? 8.938   35.783  -25.676 1.00 48.72  ? 81  GLY   C C     1 
ATOM   4083  O  O     . GLY   B 1  81  ? 9.423   36.710  -26.330 1.00 54.46  ? 81  GLY   C O     1 
ATOM   4084  N  N     . THR   B 1  82  ? 7.903   35.943  -24.850 1.00 44.55  ? 82  THR   C N     1 
ATOM   4085  C  CA    . THR   B 1  82  ? 7.263   37.242  -24.681 1.00 29.48  ? 82  THR   C CA    1 
ATOM   4086  C  C     . THR   B 1  82  ? 8.165   38.250  -23.995 1.00 41.77  ? 82  THR   C C     1 
ATOM   4087  O  O     . THR   B 1  82  ? 7.871   39.453  -24.026 1.00 39.34  ? 82  THR   C O     1 
ATOM   4088  C  CB    . THR   B 1  82  ? 5.990   37.085  -23.864 1.00 37.10  ? 82  THR   C CB    1 
ATOM   4089  O  OG1   . THR   B 1  82  ? 5.247   35.974  -24.376 1.00 50.09  ? 82  THR   C OG1   1 
ATOM   4090  C  CG2   . THR   B 1  82  ? 5.144   38.370  -23.918 1.00 42.68  ? 82  THR   C CG2   1 
ATOM   4091  N  N     . TYR   B 1  83  ? 9.248   37.784  -23.369 1.00 46.29  ? 83  TYR   C N     1 
ATOM   4092  C  CA    . TYR   B 1  83  ? 10.094  38.630  -22.539 1.00 41.98  ? 83  TYR   C CA    1 
ATOM   4093  C  C     . TYR   B 1  83  ? 11.503  38.777  -23.106 1.00 41.49  ? 83  TYR   C C     1 
ATOM   4094  O  O     . TYR   B 1  83  ? 12.353  39.405  -22.472 1.00 47.85  ? 83  TYR   C O     1 
ATOM   4095  C  CB    . TYR   B 1  83  ? 10.092  38.092  -21.096 1.00 32.23  ? 83  TYR   C CB    1 
ATOM   4096  C  CG    . TYR   B 1  83  ? 8.772   38.407  -20.430 1.00 29.84  ? 83  TYR   C CG    1 
ATOM   4097  C  CD1   . TYR   B 1  83  ? 7.687   37.531  -20.515 1.00 35.89  ? 83  TYR   C CD1   1 
ATOM   4098  C  CD2   . TYR   B 1  83  ? 8.578   39.627  -19.792 1.00 36.56  ? 83  TYR   C CD2   1 
ATOM   4099  C  CE1   . TYR   B 1  83  ? 6.441   37.850  -19.937 1.00 35.53  ? 83  TYR   C CE1   1 
ATOM   4100  C  CE2   . TYR   B 1  83  ? 7.347   39.966  -19.208 1.00 32.26  ? 83  TYR   C CE2   1 
ATOM   4101  C  CZ    . TYR   B 1  83  ? 6.279   39.081  -19.285 1.00 41.96  ? 83  TYR   C CZ    1 
ATOM   4102  O  OH    . TYR   B 1  83  ? 5.065   39.431  -18.706 1.00 44.95  ? 83  TYR   C OH    1 
ATOM   4103  N  N     . ARG   B 1  84  ? 11.746  38.274  -24.317 1.00 38.85  ? 84  ARG   C N     1 
ATOM   4104  C  CA    . ARG   B 1  84  ? 13.045  38.402  -24.970 1.00 42.29  ? 84  ARG   C CA    1 
ATOM   4105  C  C     . ARG   B 1  84  ? 13.683  39.779  -24.802 1.00 47.75  ? 84  ARG   C C     1 
ATOM   4106  O  O     . ARG   B 1  84  ? 14.870  39.890  -24.465 1.00 45.31  ? 84  ARG   C O     1 
ATOM   4107  C  CB    . ARG   B 1  84  ? 12.899  38.073  -26.461 1.00 47.92  ? 84  ARG   C CB    1 
ATOM   4108  C  CG    . ARG   B 1  84  ? 11.807  38.856  -27.165 1.00 50.21  ? 84  ARG   C CG    1 
ATOM   4109  C  CD    . ARG   B 1  84  ? 11.606  38.405  -28.612 1.00 54.39  ? 84  ARG   C CD    1 
ATOM   4110  N  NE    . ARG   B 1  84  ? 11.163  39.538  -29.417 1.00 68.50  ? 84  ARG   C NE    1 
ATOM   4111  C  CZ    . ARG   B 1  84  ? 9.936   40.046  -29.388 1.00 77.60  ? 84  ARG   C CZ    1 
ATOM   4112  N  NH1   . ARG   B 1  84  ? 8.975   39.497  -28.657 1.00 74.01  ? 84  ARG   C NH1   1 
ATOM   4113  N  NH2   . ARG   B 1  84  ? 9.665   41.135  -30.107 1.00 70.14  ? 84  ARG   C NH2   1 
ATOM   4114  N  N     . GLN   B 1  85  ? 12.922  40.845  -25.060 1.00 51.87  ? 85  GLN   C N     1 
ATOM   4115  C  CA    . GLN   B 1  85  ? 13.528  42.169  -24.952 1.00 46.13  ? 85  GLN   C CA    1 
ATOM   4116  C  C     . GLN   B 1  85  ? 13.782  42.566  -23.516 1.00 40.41  ? 85  GLN   C C     1 
ATOM   4117  O  O     . GLN   B 1  85  ? 14.277  43.673  -23.262 1.00 48.12  ? 85  GLN   C O     1 
ATOM   4118  C  CB    . GLN   B 1  85  ? 12.666  43.228  -25.654 1.00 51.01  ? 85  GLN   C CB    1 
ATOM   4119  C  CG    . GLN   B 1  85  ? 11.174  42.904  -25.746 1.00 63.00  ? 85  GLN   C CG    1 
ATOM   4120  C  CD    . GLN   B 1  85  ? 10.462  43.745  -26.811 1.00 73.49  ? 85  GLN   C CD    1 
ATOM   4121  O  OE1   . GLN   B 1  85  ? 11.005  44.748  -27.293 1.00 67.87  ? 85  GLN   C OE1   1 
ATOM   4122  N  NE2   . GLN   B 1  85  ? 9.245   43.334  -27.185 1.00 64.46  ? 85  GLN   C NE2   1 
ATOM   4123  N  N     . LEU   B 1  86  ? 13.487  41.684  -22.572 1.00 34.37  ? 86  LEU   C N     1 
ATOM   4124  C  CA    . LEU   B 1  86  ? 13.626  42.040  -21.172 1.00 39.22  ? 86  LEU   C CA    1 
ATOM   4125  C  C     . LEU   B 1  86  ? 15.024  41.796  -20.617 1.00 39.66  ? 86  LEU   C C     1 
ATOM   4126  O  O     . LEU   B 1  86  ? 15.445  42.520  -19.707 1.00 42.49  ? 86  LEU   C O     1 
ATOM   4127  C  CB    . LEU   B 1  86  ? 12.605  41.273  -20.337 1.00 39.87  ? 86  LEU   C CB    1 
ATOM   4128  C  CG    . LEU   B 1  86  ? 12.593  41.835  -18.934 1.00 38.55  ? 86  LEU   C CG    1 
ATOM   4129  C  CD1   . LEU   B 1  86  ? 12.560  43.362  -19.083 1.00 31.76  ? 86  LEU   C CD1   1 
ATOM   4130  C  CD2   . LEU   B 1  86  ? 11.385  41.290  -18.205 1.00 32.02  ? 86  LEU   C CD2   1 
ATOM   4131  N  N     . PHE   B 1  87  ? 15.751  40.808  -21.138 1.00 32.02  ? 87  PHE   C N     1 
ATOM   4132  C  CA    . PHE   B 1  87  ? 17.066  40.445  -20.632 1.00 33.79  ? 87  PHE   C CA    1 
ATOM   4133  C  C     . PHE   B 1  87  ? 18.145  40.815  -21.636 1.00 43.42  ? 87  PHE   C C     1 
ATOM   4134  O  O     . PHE   B 1  87  ? 17.992  40.564  -22.836 1.00 49.09  ? 87  PHE   C O     1 
ATOM   4135  C  CB    . PHE   B 1  87  ? 17.140  38.940  -20.348 1.00 36.60  ? 87  PHE   C CB    1 
ATOM   4136  C  CG    . PHE   B 1  87  ? 16.012  38.432  -19.496 1.00 41.35  ? 87  PHE   C CG    1 
ATOM   4137  C  CD1   . PHE   B 1  87  ? 14.790  38.113  -20.066 1.00 29.36  ? 87  PHE   C CD1   1 
ATOM   4138  C  CD2   . PHE   B 1  87  ? 16.169  38.288  -18.115 1.00 32.19  ? 87  PHE   C CD2   1 
ATOM   4139  C  CE1   . PHE   B 1  87  ? 13.747  37.666  -19.278 1.00 31.42  ? 87  PHE   C CE1   1 
ATOM   4140  C  CE2   . PHE   B 1  87  ? 15.132  37.828  -17.329 1.00 30.16  ? 87  PHE   C CE2   1 
ATOM   4141  C  CZ    . PHE   B 1  87  ? 13.922  37.520  -17.906 1.00 29.99  ? 87  PHE   C CZ    1 
ATOM   4142  N  N     . HIS   B 1  88  ? 19.249  41.387  -21.149 1.00 44.32  ? 88  HIS   C N     1 
ATOM   4143  C  CA    . HIS   B 1  88  ? 20.424  41.503  -22.002 1.00 37.70  ? 88  HIS   C CA    1 
ATOM   4144  C  C     . HIS   B 1  88  ? 20.848  40.104  -22.430 1.00 38.64  ? 88  HIS   C C     1 
ATOM   4145  O  O     . HIS   B 1  88  ? 20.908  39.194  -21.592 1.00 40.25  ? 88  HIS   C O     1 
ATOM   4146  C  CB    . HIS   B 1  88  ? 21.592  42.209  -21.312 1.00 32.40  ? 88  HIS   C CB    1 
ATOM   4147  C  CG    . HIS   B 1  88  ? 22.772  42.448  -22.214 1.00 38.42  ? 88  HIS   C CG    1 
ATOM   4148  N  ND1   . HIS   B 1  88  ? 23.561  41.426  -22.700 1.00 42.67  ? 88  HIS   C ND1   1 
ATOM   4149  C  CD2   . HIS   B 1  88  ? 23.291  43.592  -22.723 1.00 39.60  ? 88  HIS   C CD2   1 
ATOM   4150  C  CE1   . HIS   B 1  88  ? 24.516  41.928  -23.464 1.00 45.69  ? 88  HIS   C CE1   1 
ATOM   4151  N  NE2   . HIS   B 1  88  ? 24.374  43.241  -23.495 1.00 49.03  ? 88  HIS   C NE2   1 
ATOM   4152  N  N     . PRO   B 1  89  ? 21.120  39.889  -23.699 1.00 42.53  ? 89  PRO   C N     1 
ATOM   4153  C  CA    . PRO   B 1  89  ? 21.553  38.567  -24.163 1.00 39.13  ? 89  PRO   C CA    1 
ATOM   4154  C  C     . PRO   B 1  89  ? 22.532  37.873  -23.228 1.00 38.36  ? 89  PRO   C C     1 
ATOM   4155  O  O     . PRO   B 1  89  ? 22.410  36.670  -22.971 1.00 42.97  ? 89  PRO   C O     1 
ATOM   4156  C  CB    . PRO   B 1  89  ? 22.206  38.890  -25.509 1.00 33.39  ? 89  PRO   C CB    1 
ATOM   4157  C  CG    . PRO   B 1  89  ? 21.410  40.046  -25.996 1.00 40.27  ? 89  PRO   C CG    1 
ATOM   4158  C  CD    . PRO   B 1  89  ? 21.075  40.872  -24.792 1.00 39.46  ? 89  PRO   C CD    1 
ATOM   4159  N  N     . GLU   B 1  90  ? 23.508  38.626  -22.716 1.00 38.89  ? 90  GLU   C N     1 
ATOM   4160  C  CA    . GLU   B 1  90  ? 24.590  38.026  -21.945 1.00 39.91  ? 90  GLU   C CA    1 
ATOM   4161  C  C     . GLU   B 1  90  ? 24.107  37.425  -20.638 1.00 34.98  ? 90  GLU   C C     1 
ATOM   4162  O  O     . GLU   B 1  90  ? 24.851  36.645  -20.033 1.00 36.17  ? 90  GLU   C O     1 
ATOM   4163  C  CB    . GLU   B 1  90  ? 25.688  39.055  -21.653 1.00 38.94  ? 90  GLU   C CB    1 
ATOM   4164  C  CG    . GLU   B 1  90  ? 26.593  39.389  -22.819 1.00 45.54  ? 90  GLU   C CG    1 
ATOM   4165  C  CD    . GLU   B 1  90  ? 27.728  40.306  -22.393 1.00 67.74  ? 90  GLU   C CD    1 
ATOM   4166  O  OE1   . GLU   B 1  90  ? 27.518  41.106  -21.450 1.00 65.81  ? 90  GLU   C OE1   1 
ATOM   4167  O  OE2   . GLU   B 1  90  ? 28.833  40.215  -22.980 1.00 72.47  ? 90  GLU   C OE2   1 
ATOM   4168  N  N     . GLN   B 1  91  ? 22.901  37.797  -20.166 1.00 34.30  ? 91  GLN   C N     1 
ATOM   4169  C  CA    . GLN   B 1  91  ? 22.282  37.180  -18.985 1.00 38.77  ? 91  GLN   C CA    1 
ATOM   4170  C  C     . GLN   B 1  91  ? 21.648  35.815  -19.287 1.00 37.45  ? 91  GLN   C C     1 
ATOM   4171  O  O     . GLN   B 1  91  ? 21.007  35.226  -18.407 1.00 32.58  ? 91  GLN   C O     1 
ATOM   4172  C  CB    . GLN   B 1  91  ? 21.195  38.081  -18.375 1.00 30.94  ? 91  GLN   C CB    1 
ATOM   4173  C  CG    . GLN   B 1  91  ? 21.376  39.574  -18.451 1.00 25.06  ? 91  GLN   C CG    1 
ATOM   4174  C  CD    . GLN   B 1  91  ? 20.182  40.325  -17.849 1.00 30.97  ? 91  GLN   C CD    1 
ATOM   4175  O  OE1   . GLN   B 1  91  ? 19.777  41.367  -18.359 1.00 36.24  ? 91  GLN   C OE1   1 
ATOM   4176  N  NE2   . GLN   B 1  91  ? 19.616  39.792  -16.765 1.00 21.72  ? 91  GLN   C NE2   1 
ATOM   4177  N  N     . LEU   B 1  92  ? 21.768  35.329  -20.517 1.00 32.30  ? 92  LEU   C N     1 
ATOM   4178  C  CA    . LEU   B 1  92  ? 21.254  34.032  -20.920 1.00 31.06  ? 92  LEU   C CA    1 
ATOM   4179  C  C     . LEU   B 1  92  ? 22.459  33.208  -21.370 1.00 30.01  ? 92  LEU   C C     1 
ATOM   4180  O  O     . LEU   B 1  92  ? 23.078  33.507  -22.398 1.00 38.20  ? 92  LEU   C O     1 
ATOM   4181  C  CB    . LEU   B 1  92  ? 20.192  34.186  -22.016 1.00 30.26  ? 92  LEU   C CB    1 
ATOM   4182  C  CG    . LEU   B 1  92  ? 19.014  35.158  -21.789 1.00 30.39  ? 92  LEU   C CG    1 
ATOM   4183  C  CD1   . LEU   B 1  92  ? 17.784  34.723  -22.564 1.00 33.38  ? 92  LEU   C CD1   1 
ATOM   4184  C  CD2   . LEU   B 1  92  ? 18.643  35.365  -20.322 1.00 32.44  ? 92  LEU   C CD2   1 
ATOM   4185  N  N     . ILE   B 1  93  ? 22.791  32.184  -20.590 1.00 21.96  ? 93  ILE   C N     1 
ATOM   4186  C  CA    . ILE   B 1  93  ? 24.045  31.451  -20.690 1.00 23.74  ? 93  ILE   C CA    1 
ATOM   4187  C  C     . ILE   B 1  93  ? 23.697  29.986  -20.827 1.00 26.96  ? 93  ILE   C C     1 
ATOM   4188  O  O     . ILE   B 1  93  ? 23.003  29.436  -19.967 1.00 26.79  ? 93  ILE   C O     1 
ATOM   4189  C  CB    . ILE   B 1  93  ? 24.940  31.663  -19.456 1.00 26.95  ? 93  ILE   C CB    1 
ATOM   4190  C  CG1   . ILE   B 1  93  ? 25.182  33.154  -19.201 1.00 28.17  ? 93  ILE   C CG1   1 
ATOM   4191  C  CG2   . ILE   B 1  93  ? 26.249  30.858  -19.568 1.00 21.24  ? 93  ILE   C CG2   1 
ATOM   4192  C  CD1   . ILE   B 1  93  ? 26.138  33.398  -18.094 1.00 31.37  ? 93  ILE   C CD1   1 
ATOM   4193  N  N     . THR   B 1  94  ? 24.200  29.348  -21.883 1.00 28.90  ? 94  THR   C N     1 
ATOM   4194  C  CA    . THR   B 1  94  ? 23.811  27.992  -22.231 1.00 27.37  ? 94  THR   C CA    1 
ATOM   4195  C  C     . THR   B 1  94  ? 25.015  27.240  -22.776 1.00 24.34  ? 94  THR   C C     1 
ATOM   4196  O  O     . THR   B 1  94  ? 25.925  27.840  -23.342 1.00 29.98  ? 94  THR   C O     1 
ATOM   4197  C  CB    . THR   B 1  94  ? 22.691  28.002  -23.272 1.00 32.40  ? 94  THR   C CB    1 
ATOM   4198  O  OG1   . THR   B 1  94  ? 23.236  28.396  -24.529 1.00 29.55  ? 94  THR   C OG1   1 
ATOM   4199  C  CG2   . THR   B 1  94  ? 21.596  29.003  -22.886 1.00 33.96  ? 94  THR   C CG2   1 
ATOM   4200  N  N     . GLY   B 1  95  ? 25.016  25.919  -22.592 1.00 28.32  ? 95  GLY   C N     1 
ATOM   4201  C  CA    . GLY   B 1  95  ? 25.958  25.034  -23.240 1.00 29.10  ? 95  GLY   C CA    1 
ATOM   4202  C  C     . GLY   B 1  95  ? 25.311  24.169  -24.323 1.00 33.39  ? 95  GLY   C C     1 
ATOM   4203  O  O     . GLY   B 1  95  ? 24.105  24.200  -24.569 1.00 33.21  ? 95  GLY   C O     1 
ATOM   4204  N  N     . LYS   B 1  96  ? 26.152  23.361  -24.972 1.00 32.52  ? 96  LYS   C N     1 
ATOM   4205  C  CA    . LYS   B 1  96  ? 25.674  22.538  -26.080 1.00 36.39  ? 96  LYS   C CA    1 
ATOM   4206  C  C     . LYS   B 1  96  ? 25.173  21.162  -25.637 1.00 41.40  ? 96  LYS   C C     1 
ATOM   4207  O  O     . LYS   B 1  96  ? 24.293  20.588  -26.296 1.00 45.66  ? 96  LYS   C O     1 
ATOM   4208  C  CB    . LYS   B 1  96  ? 26.778  22.390  -27.134 1.00 40.24  ? 96  LYS   C CB    1 
ATOM   4209  C  CG    . LYS   B 1  96  ? 26.673  23.380  -28.306 1.00 46.30  ? 96  LYS   C CG    1 
ATOM   4210  C  CD    . LYS   B 1  96  ? 28.047  23.844  -28.814 1.00 45.13  ? 96  LYS   C CD    1 
ATOM   4211  C  CE    . LYS   B 1  96  ? 27.882  24.941  -29.855 1.00 57.76  ? 96  LYS   C CE    1 
ATOM   4212  N  NZ    . LYS   B 1  96  ? 29.119  25.730  -30.088 1.00 56.88  ? 96  LYS   C NZ    1 
ATOM   4213  N  N     . GLU   B 1  97  ? 25.705  20.629  -24.538 1.00 31.07  ? 97  GLU   C N     1 
ATOM   4214  C  CA    . GLU   B 1  97  ? 25.334  19.326  -24.015 1.00 29.61  ? 97  GLU   C CA    1 
ATOM   4215  C  C     . GLU   B 1  97  ? 25.135  19.469  -22.511 1.00 30.37  ? 97  GLU   C C     1 
ATOM   4216  O  O     . GLU   B 1  97  ? 25.806  20.275  -21.859 1.00 33.95  ? 97  GLU   C O     1 
ATOM   4217  C  CB    . GLU   B 1  97  ? 26.422  18.263  -24.378 1.00 28.08  ? 97  GLU   C CB    1 
ATOM   4218  C  CG    . GLU   B 1  97  ? 26.642  17.115  -23.377 1.00 31.17  ? 97  GLU   C CG    1 
ATOM   4219  C  CD    . GLU   B 1  97  ? 27.455  15.950  -23.949 1.00 46.90  ? 97  GLU   C CD    1 
ATOM   4220  O  OE1   . GLU   B 1  97  ? 28.557  16.165  -24.503 1.00 49.76  ? 97  GLU   C OE1   1 
ATOM   4221  O  OE2   . GLU   B 1  97  ? 26.976  14.800  -23.848 1.00 61.89  ? 97  GLU   C OE2   1 
ATOM   4222  N  N     . ASP   B 1  98  ? 24.213  18.692  -21.958 1.00 24.73  ? 98  ASP   C N     1 
ATOM   4223  C  CA    . ASP   B 1  98  ? 23.780  18.941  -20.597 1.00 22.86  ? 98  ASP   C CA    1 
ATOM   4224  C  C     . ASP   B 1  98  ? 24.411  17.928  -19.639 1.00 25.32  ? 98  ASP   C C     1 
ATOM   4225  O  O     . ASP   B 1  98  ? 25.439  17.309  -19.945 1.00 26.39  ? 98  ASP   C O     1 
ATOM   4226  C  CB    . ASP   B 1  98  ? 22.237  18.968  -20.541 1.00 18.25  ? 98  ASP   C CB    1 
ATOM   4227  C  CG    . ASP   B 1  98  ? 21.595  17.579  -20.638 1.00 24.96  ? 98  ASP   C CG    1 
ATOM   4228  O  OD1   . ASP   B 1  98  ? 22.229  16.564  -20.250 1.00 24.41  ? 98  ASP   C OD1   1 
ATOM   4229  O  OD2   . ASP   B 1  98  ? 20.430  17.506  -21.109 1.00 26.35  ? 98  ASP   C OD2   1 
ATOM   4230  N  N     . ALA   B 1  99  ? 23.801  17.766  -18.469 1.00 22.06  ? 99  ALA   C N     1 
ATOM   4231  C  CA    . ALA   B 1  99  ? 24.390  17.035  -17.369 1.00 22.81  ? 99  ALA   C CA    1 
ATOM   4232  C  C     . ALA   B 1  99  ? 23.819  15.642  -17.217 1.00 23.55  ? 99  ALA   C C     1 
ATOM   4233  O  O     . ALA   B 1  99  ? 24.215  14.929  -16.291 1.00 28.69  ? 99  ALA   C O     1 
ATOM   4234  C  CB    . ALA   B 1  99  ? 24.202  17.818  -16.076 1.00 21.52  ? 99  ALA   C CB    1 
ATOM   4235  N  N     . ALA   B 1  100 ? 22.884  15.251  -18.079 1.00 20.40  ? 100 ALA   C N     1 
ATOM   4236  C  CA    . ALA   B 1  100 ? 22.373  13.875  -18.141 1.00 22.47  ? 100 ALA   C CA    1 
ATOM   4237  C  C     . ALA   B 1  100 ? 21.881  13.393  -16.793 1.00 25.50  ? 100 ALA   C C     1 
ATOM   4238  O  O     . ALA   B 1  100 ? 22.114  12.244  -16.413 1.00 25.62  ? 100 ALA   C O     1 
ATOM   4239  C  CB    . ALA   B 1  100 ? 23.423  12.898  -18.682 1.00 20.11  ? 100 ALA   C CB    1 
ATOM   4240  N  N     . ASN   B 1  101 ? 21.199  14.268  -16.055 1.00 24.18  ? 101 ASN   C N     1 
ATOM   4241  C  CA    . ASN   B 1  101 ? 20.684  13.889  -14.737 1.00 25.58  ? 101 ASN   C CA    1 
ATOM   4242  C  C     . ASN   B 1  101 ? 21.754  13.214  -13.877 1.00 25.97  ? 101 ASN   C C     1 
ATOM   4243  O  O     . ASN   B 1  101 ? 21.440  12.344  -13.060 1.00 22.93  ? 101 ASN   C O     1 
ATOM   4244  C  CB    . ASN   B 1  101 ? 19.466  12.974  -14.867 1.00 22.64  ? 101 ASN   C CB    1 
ATOM   4245  C  CG    . ASN   B 1  101 ? 18.249  13.702  -15.367 1.00 31.26  ? 101 ASN   C CG    1 
ATOM   4246  O  OD1   . ASN   B 1  101 ? 17.816  13.506  -16.500 1.00 32.61  ? 101 ASN   C OD1   1 
ATOM   4247  N  ND2   . ASN   B 1  101 ? 17.679  14.559  -14.515 1.00 31.12  ? 101 ASN   C ND2   1 
ATOM   4248  N  N     . ASN   B 1  102 ? 23.023  13.608  -14.062 1.00 22.92  ? 102 ASN   C N     1 
ATOM   4249  C  CA    . ASN   B 1  102 ? 24.167  13.079  -13.316 1.00 24.42  ? 102 ASN   C CA    1 
ATOM   4250  C  C     . ASN   B 1  102 ? 24.858  14.236  -12.599 1.00 28.57  ? 102 ASN   C C     1 
ATOM   4251  O  O     . ASN   B 1  102 ? 25.495  15.077  -13.250 1.00 30.17  ? 102 ASN   C O     1 
ATOM   4252  C  CB    . ASN   B 1  102 ? 25.149  12.357  -14.249 1.00 22.26  ? 102 ASN   C CB    1 
ATOM   4253  C  CG    . ASN   B 1  102 ? 26.408  11.823  -13.517 1.00 26.97  ? 102 ASN   C CG    1 
ATOM   4254  O  OD1   . ASN   B 1  102 ? 26.799  12.326  -12.455 1.00 30.93  ? 102 ASN   C OD1   1 
ATOM   4255  N  ND2   . ASN   B 1  102 ? 27.042  10.796  -14.097 1.00 25.23  ? 102 ASN   C ND2   1 
ATOM   4256  N  N     . TYR   B 1  103 ? 24.764  14.259  -11.258 1.00 26.33  ? 103 TYR   C N     1 
ATOM   4257  C  CA    . TYR   B 1  103 ? 25.420  15.313  -10.479 1.00 27.12  ? 103 TYR   C CA    1 
ATOM   4258  C  C     . TYR   B 1  103 ? 26.861  15.517  -10.928 1.00 25.90  ? 103 TYR   C C     1 
ATOM   4259  O  O     . TYR   B 1  103 ? 27.313  16.657  -11.088 1.00 28.63  ? 103 TYR   C O     1 
ATOM   4260  C  CB    . TYR   B 1  103 ? 25.351  14.990  -8.984  1.00 18.19  ? 103 TYR   C CB    1 
ATOM   4261  C  CG    . TYR   B 1  103 ? 26.189  15.877  -8.065  1.00 29.32  ? 103 TYR   C CG    1 
ATOM   4262  C  CD1   . TYR   B 1  103 ? 27.547  15.630  -7.877  1.00 27.24  ? 103 TYR   C CD1   1 
ATOM   4263  C  CD2   . TYR   B 1  103 ? 25.620  16.933  -7.351  1.00 30.56  ? 103 TYR   C CD2   1 
ATOM   4264  C  CE1   . TYR   B 1  103 ? 28.315  16.401  -7.037  1.00 19.79  ? 103 TYR   C CE1   1 
ATOM   4265  C  CE2   . TYR   B 1  103 ? 26.400  17.725  -6.493  1.00 28.43  ? 103 TYR   C CE2   1 
ATOM   4266  C  CZ    . TYR   B 1  103 ? 27.750  17.441  -6.345  1.00 26.07  ? 103 TYR   C CZ    1 
ATOM   4267  O  OH    . TYR   B 1  103 ? 28.560  18.193  -5.512  1.00 25.65  ? 103 TYR   C OH    1 
ATOM   4268  N  N     . ALA   B 1  104 ? 27.586  14.424  -11.175 1.00 25.88  ? 104 ALA   C N     1 
ATOM   4269  C  CA    . ALA   B 1  104 ? 28.992  14.545  -11.547 1.00 26.06  ? 104 ALA   C CA    1 
ATOM   4270  C  C     . ALA   B 1  104 ? 29.175  15.356  -12.823 1.00 27.81  ? 104 ALA   C C     1 
ATOM   4271  O  O     . ALA   B 1  104 ? 30.122  16.143  -12.937 1.00 32.12  ? 104 ALA   C O     1 
ATOM   4272  C  CB    . ALA   B 1  104 ? 29.612  13.166  -11.703 1.00 28.55  ? 104 ALA   C CB    1 
ATOM   4273  N  N     . ARG   B 1  105 ? 28.288  15.180  -13.798 1.00 28.42  ? 105 ARG   C N     1 
ATOM   4274  C  CA    . ARG   B 1  105 ? 28.396  15.962  -15.025 1.00 28.94  ? 105 ARG   C CA    1 
ATOM   4275  C  C     . ARG   B 1  105 ? 28.242  17.452  -14.745 1.00 32.61  ? 105 ARG   C C     1 
ATOM   4276  O  O     . ARG   B 1  105 ? 29.015  18.277  -15.253 1.00 30.70  ? 105 ARG   C O     1 
ATOM   4277  C  CB    . ARG   B 1  105 ? 27.343  15.510  -16.026 1.00 32.60  ? 105 ARG   C CB    1 
ATOM   4278  C  CG    . ARG   B 1  105 ? 27.671  14.212  -16.689 1.00 31.20  ? 105 ARG   C CG    1 
ATOM   4279  C  CD    . ARG   B 1  105 ? 26.899  14.048  -17.996 1.00 29.47  ? 105 ARG   C CD    1 
ATOM   4280  N  NE    . ARG   B 1  105 ? 27.675  13.189  -18.880 1.00 32.26  ? 105 ARG   C NE    1 
ATOM   4281  C  CZ    . ARG   B 1  105 ? 28.316  13.607  -19.957 1.00 27.95  ? 105 ARG   C CZ    1 
ATOM   4282  N  NH1   . ARG   B 1  105 ? 28.150  14.834  -20.425 1.00 24.20  ? 105 ARG   C NH1   1 
ATOM   4283  N  NH2   . ARG   B 1  105 ? 29.140  12.769  -20.580 1.00 33.55  ? 105 ARG   C NH2   1 
ATOM   4284  N  N     . GLY   B 1  106 ? 27.220  17.816  -13.958 1.00 35.25  ? 106 GLY   C N     1 
ATOM   4285  C  CA    . GLY   B 1  106 ? 26.947  19.207  -13.643 1.00 25.30  ? 106 GLY   C CA    1 
ATOM   4286  C  C     . GLY   B 1  106 ? 28.019  19.863  -12.809 1.00 25.12  ? 106 GLY   C C     1 
ATOM   4287  O  O     . GLY   B 1  106 ? 28.188  21.080  -12.894 1.00 28.51  ? 106 GLY   C O     1 
ATOM   4288  N  N     . HIS   B 1  107 ? 28.771  19.089  -12.031 1.00 26.70  ? 107 HIS   C N     1 
ATOM   4289  C  CA    . HIS   B 1  107 ? 29.770  19.668  -11.142 1.00 33.74  ? 107 HIS   C CA    1 
ATOM   4290  C  C     . HIS   B 1  107 ? 31.166  19.734  -11.753 1.00 34.34  ? 107 HIS   C C     1 
ATOM   4291  O  O     . HIS   B 1  107 ? 31.804  20.779  -11.665 1.00 42.94  ? 107 HIS   C O     1 
ATOM   4292  C  CB    . HIS   B 1  107 ? 29.819  18.905  -9.813  1.00 31.25  ? 107 HIS   C CB    1 
ATOM   4293  C  CG    . HIS   B 1  107 ? 30.655  19.577  -8.764  1.00 33.33  ? 107 HIS   C CG    1 
ATOM   4294  N  ND1   . HIS   B 1  107 ? 30.213  19.775  -7.477  1.00 41.92  ? 107 HIS   C ND1   1 
ATOM   4295  C  CD2   . HIS   B 1  107 ? 31.914  20.074  -8.804  1.00 40.36  ? 107 HIS   C CD2   1 
ATOM   4296  C  CE1   . HIS   B 1  107 ? 31.157  20.375  -6.771  1.00 46.39  ? 107 HIS   C CE1   1 
ATOM   4297  N  NE2   . HIS   B 1  107 ? 32.202  20.565  -7.553  1.00 44.79  ? 107 HIS   C NE2   1 
ATOM   4298  N  N     . TYR   B 1  108 ? 31.687  18.636  -12.330 1.00 39.35  ? 108 TYR   C N     1 
ATOM   4299  C  CA    . TYR   B 1  108 ? 33.054  18.640  -12.902 1.00 47.08  ? 108 TYR   C CA    1 
ATOM   4300  C  C     . TYR   B 1  108 ? 33.160  17.703  -14.106 1.00 53.07  ? 108 TYR   C C     1 
ATOM   4301  O  O     . TYR   B 1  108 ? 33.831  16.661  -14.057 1.00 58.85  ? 108 TYR   C O     1 
ATOM   4302  C  CB    . TYR   B 1  108 ? 34.150  18.259  -11.898 1.00 63.34  ? 108 TYR   C CB    1 
ATOM   4303  C  CG    . TYR   B 1  108 ? 33.786  17.566  -10.580 1.00 53.83  ? 108 TYR   C CG    1 
ATOM   4304  C  CD1   . TYR   B 1  108 ? 32.779  16.611  -10.491 1.00 45.17  ? 108 TYR   C CD1   1 
ATOM   4305  C  CD2   . TYR   B 1  108 ? 34.505  17.865  -9.423  1.00 52.62  ? 108 TYR   C CD2   1 
ATOM   4306  C  CE1   . TYR   B 1  108 ? 32.475  16.011  -9.260  1.00 42.09  ? 108 TYR   C CE1   1 
ATOM   4307  C  CE2   . TYR   B 1  108 ? 34.216  17.282  -8.217  1.00 50.98  ? 108 TYR   C CE2   1 
ATOM   4308  C  CZ    . TYR   B 1  108 ? 33.217  16.358  -8.127  1.00 43.36  ? 108 TYR   C CZ    1 
ATOM   4309  O  OH    . TYR   B 1  108 ? 32.994  15.805  -6.883  1.00 40.40  ? 108 TYR   C OH    1 
ATOM   4310  N  N     . THR   B 1  109 ? 32.533  18.100  -15.209 1.00 41.91  ? 109 THR   C N     1 
ATOM   4311  C  CA    . THR   B 1  109 ? 32.713  17.412  -16.483 1.00 26.52  ? 109 THR   C CA    1 
ATOM   4312  C  C     . THR   B 1  109 ? 32.192  18.370  -17.524 1.00 30.77  ? 109 THR   C C     1 
ATOM   4313  O  O     . THR   B 1  109 ? 32.971  18.977  -18.258 1.00 38.43  ? 109 THR   C O     1 
ATOM   4314  C  CB    . THR   B 1  109 ? 31.979  16.069  -16.558 1.00 26.58  ? 109 THR   C CB    1 
ATOM   4315  O  OG1   . THR   B 1  109 ? 32.838  15.003  -16.136 1.00 25.27  ? 109 THR   C OG1   1 
ATOM   4316  C  CG2   . THR   B 1  109 ? 31.564  15.792  -17.976 1.00 35.32  ? 109 THR   C CG2   1 
ATOM   4317  N  N     . ILE   B 1  110 ? 30.879  18.556  -17.553 1.00 26.33  ? 110 ILE   C N     1 
ATOM   4318  C  CA    . ILE   B 1  110 ? 30.341  19.659  -18.325 1.00 27.51  ? 110 ILE   C CA    1 
ATOM   4319  C  C     . ILE   B 1  110 ? 30.483  20.950  -17.546 1.00 41.30  ? 110 ILE   C C     1 
ATOM   4320  O  O     . ILE   B 1  110 ? 30.863  21.987  -18.107 1.00 40.61  ? 110 ILE   C O     1 
ATOM   4321  C  CB    . ILE   B 1  110 ? 28.874  19.394  -18.697 1.00 27.92  ? 110 ILE   C CB    1 
ATOM   4322  C  CG1   . ILE   B 1  110 ? 28.735  17.978  -19.232 1.00 34.60  ? 110 ILE   C CG1   1 
ATOM   4323  C  CG2   . ILE   B 1  110 ? 28.376  20.421  -19.713 1.00 19.53  ? 110 ILE   C CG2   1 
ATOM   4324  C  CD1   . ILE   B 1  110 ? 29.791  17.636  -20.241 1.00 26.52  ? 110 ILE   C CD1   1 
ATOM   4325  N  N     . GLY   B 1  111 ? 30.178  20.908  -16.244 1.00 40.99  ? 111 GLY   C N     1 
ATOM   4326  C  CA    . GLY   B 1  111 ? 30.071  22.143  -15.484 1.00 34.02  ? 111 GLY   C CA    1 
ATOM   4327  C  C     . GLY   B 1  111 ? 31.358  22.929  -15.521 1.00 36.43  ? 111 GLY   C C     1 
ATOM   4328  O  O     . GLY   B 1  111 ? 31.368  24.115  -15.864 1.00 34.59  ? 111 GLY   C O     1 
ATOM   4329  N  N     . LYS   B 1  112 ? 32.475  22.251  -15.237 1.00 40.45  ? 112 LYS   C N     1 
ATOM   4330  C  CA    . LYS   B 1  112 ? 33.757  22.931  -15.163 1.00 35.32  ? 112 LYS   C CA    1 
ATOM   4331  C  C     . LYS   B 1  112 ? 34.032  23.782  -16.390 1.00 30.63  ? 112 LYS   C C     1 
ATOM   4332  O  O     . LYS   B 1  112 ? 34.726  24.792  -16.276 1.00 42.94  ? 112 LYS   C O     1 
ATOM   4333  C  CB    . LYS   B 1  112 ? 34.881  21.916  -14.925 1.00 41.65  ? 112 LYS   C CB    1 
ATOM   4334  C  CG    . LYS   B 1  112 ? 35.137  20.899  -16.018 1.00 46.01  ? 112 LYS   C CG    1 
ATOM   4335  C  CD    . LYS   B 1  112 ? 36.539  20.339  -15.829 1.00 46.86  ? 112 LYS   C CD    1 
ATOM   4336  C  CE    . LYS   B 1  112 ? 36.725  18.958  -16.413 1.00 48.71  ? 112 LYS   C CE    1 
ATOM   4337  N  NZ    . LYS   B 1  112 ? 37.233  18.018  -15.341 1.00 42.65  ? 112 LYS   C NZ    1 
ATOM   4338  N  N     . GLU   B 1  113 ? 33.461  23.456  -17.541 1.00 34.69  ? 113 GLU   C N     1 
ATOM   4339  C  CA    . GLU   B 1  113 ? 33.801  24.202  -18.744 1.00 29.28  ? 113 GLU   C CA    1 
ATOM   4340  C  C     . GLU   B 1  113 ? 32.927  25.418  -18.962 1.00 24.23  ? 113 GLU   C C     1 
ATOM   4341  O  O     . GLU   B 1  113 ? 33.093  26.099  -19.974 1.00 39.73  ? 113 GLU   C O     1 
ATOM   4342  C  CB    . GLU   B 1  113 ? 33.727  23.316  -19.999 1.00 33.04  ? 113 GLU   C CB    1 
ATOM   4343  C  CG    . GLU   B 1  113 ? 34.443  21.968  -19.917 1.00 41.64  ? 113 GLU   C CG    1 
ATOM   4344  C  CD    . GLU   B 1  113 ? 35.975  22.065  -19.820 1.00 63.96  ? 113 GLU   C CD    1 
ATOM   4345  O  OE1   . GLU   B 1  113 ? 36.624  22.502  -20.804 1.00 62.22  ? 113 GLU   C OE1   1 
ATOM   4346  O  OE2   . GLU   B 1  113 ? 36.525  21.675  -18.755 1.00 62.63  ? 113 GLU   C OE2   1 
ATOM   4347  N  N     . ILE   B 1  114 ? 31.988  25.728  -18.073 1.00 26.46  ? 114 ILE   C N     1 
ATOM   4348  C  CA    . ILE   B 1  114 ? 31.188  26.935  -18.244 1.00 22.37  ? 114 ILE   C CA    1 
ATOM   4349  C  C     . ILE   B 1  114 ? 31.107  27.781  -16.981 1.00 26.33  ? 114 ILE   C C     1 
ATOM   4350  O  O     . ILE   B 1  114 ? 30.550  28.879  -17.023 1.00 23.76  ? 114 ILE   C O     1 
ATOM   4351  C  CB    . ILE   B 1  114 ? 29.775  26.614  -18.773 1.00 20.61  ? 114 ILE   C CB    1 
ATOM   4352  C  CG1   . ILE   B 1  114 ? 29.175  27.852  -19.421 1.00 24.35  ? 114 ILE   C CG1   1 
ATOM   4353  C  CG2   . ILE   B 1  114 ? 28.854  26.109  -17.682 1.00 21.24  ? 114 ILE   C CG2   1 
ATOM   4354  C  CD1   . ILE   B 1  114 ? 27.714  27.699  -19.720 1.00 26.16  ? 114 ILE   C CD1   1 
ATOM   4355  N  N     . ILE   B 1  115 ? 31.693  27.325  -15.862 1.00 31.50  ? 115 ILE   C N     1 
ATOM   4356  C  CA    . ILE   B 1  115 ? 31.632  28.066  -14.598 1.00 24.99  ? 115 ILE   C CA    1 
ATOM   4357  C  C     . ILE   B 1  115 ? 32.190  29.488  -14.745 1.00 26.76  ? 115 ILE   C C     1 
ATOM   4358  O  O     . ILE   B 1  115 ? 31.566  30.456  -14.310 1.00 27.49  ? 115 ILE   C O     1 
ATOM   4359  C  CB    . ILE   B 1  115 ? 32.364  27.291  -13.497 1.00 18.89  ? 115 ILE   C CB    1 
ATOM   4360  C  CG1   . ILE   B 1  115 ? 32.275  28.050  -12.182 1.00 28.06  ? 115 ILE   C CG1   1 
ATOM   4361  C  CG2   . ILE   B 1  115 ? 33.791  27.110  -13.876 1.00 26.71  ? 115 ILE   C CG2   1 
ATOM   4362  C  CD1   . ILE   B 1  115 ? 30.855  28.292  -11.700 1.00 28.64  ? 115 ILE   C CD1   1 
ATOM   4363  N  N     . ASP   B 1  116 ? 33.373  29.642  -15.349 1.00 29.55  ? 116 ASP   C N     1 
ATOM   4364  C  CA    . ASP   B 1  116 ? 33.995  30.966  -15.396 1.00 23.47  ? 116 ASP   C CA    1 
ATOM   4365  C  C     . ASP   B 1  116 ? 33.135  31.952  -16.173 1.00 27.80  ? 116 ASP   C C     1 
ATOM   4366  O  O     . ASP   B 1  116 ? 32.846  33.053  -15.684 1.00 26.50  ? 116 ASP   C O     1 
ATOM   4367  C  CB    . ASP   B 1  116 ? 35.394  30.890  -15.999 1.00 17.74  ? 116 ASP   C CB    1 
ATOM   4368  C  CG    . ASP   B 1  116 ? 36.223  29.808  -15.393 1.00 23.56  ? 116 ASP   C CG    1 
ATOM   4369  O  OD1   . ASP   B 1  116 ? 36.543  29.892  -14.180 1.00 23.17  ? 116 ASP   C OD1   1 
ATOM   4370  O  OD2   . ASP   B 1  116 ? 36.524  28.844  -16.132 1.00 35.42  ? 116 ASP   C OD2   1 
ATOM   4371  N  N     . LEU   B 1  117 ? 32.734  31.593  -17.398 1.00 29.27  ? 117 LEU   C N     1 
ATOM   4372  C  CA    . LEU   B 1  117 ? 31.728  32.406  -18.084 1.00 25.48  ? 117 LEU   C CA    1 
ATOM   4373  C  C     . LEU   B 1  117 ? 30.644  32.805  -17.094 1.00 25.97  ? 117 LEU   C C     1 
ATOM   4374  O  O     . LEU   B 1  117 ? 30.373  33.995  -16.893 1.00 29.82  ? 117 LEU   C O     1 
ATOM   4375  C  CB    . LEU   B 1  117 ? 31.121  31.648  -19.274 1.00 22.05  ? 117 LEU   C CB    1 
ATOM   4376  C  CG    . LEU   B 1  117 ? 30.399  32.449  -20.369 1.00 32.84  ? 117 LEU   C CG    1 
ATOM   4377  C  CD1   . LEU   B 1  117 ? 30.292  33.952  -20.087 1.00 30.87  ? 117 LEU   C CD1   1 
ATOM   4378  C  CD2   . LEU   B 1  117 ? 31.072  32.226  -21.715 1.00 40.39  ? 117 LEU   C CD2   1 
ATOM   4379  N  N     . VAL   B 1  118 ? 30.071  31.815  -16.403 1.00 25.01  ? 118 VAL   C N     1 
ATOM   4380  C  CA    . VAL   B 1  118 ? 28.932  32.065  -15.518 1.00 24.28  ? 118 VAL   C CA    1 
ATOM   4381  C  C     . VAL   B 1  118 ? 29.301  33.068  -14.420 1.00 25.40  ? 118 VAL   C C     1 
ATOM   4382  O  O     . VAL   B 1  118 ? 28.654  34.111  -14.268 1.00 23.61  ? 118 VAL   C O     1 
ATOM   4383  C  CB    . VAL   B 1  118 ? 28.409  30.730  -14.950 1.00 22.39  ? 118 VAL   C CB    1 
ATOM   4384  C  CG1   . VAL   B 1  118 ? 27.451  30.962  -13.799 1.00 19.22  ? 118 VAL   C CG1   1 
ATOM   4385  C  CG2   . VAL   B 1  118 ? 27.728  29.911  -16.071 1.00 24.12  ? 118 VAL   C CG2   1 
ATOM   4386  N  N     . LEU   B 1  119 ? 30.355  32.782  -13.650 1.00 26.25  ? 119 LEU   C N     1 
ATOM   4387  C  CA    . LEU   B 1  119 ? 30.777  33.723  -12.617 1.00 26.32  ? 119 LEU   C CA    1 
ATOM   4388  C  C     . LEU   B 1  119 ? 31.129  35.084  -13.219 1.00 29.92  ? 119 LEU   C C     1 
ATOM   4389  O  O     . LEU   B 1  119 ? 30.790  36.131  -12.645 1.00 25.29  ? 119 LEU   C O     1 
ATOM   4390  C  CB    . LEU   B 1  119 ? 31.949  33.148  -11.814 1.00 18.84  ? 119 LEU   C CB    1 
ATOM   4391  C  CG    . LEU   B 1  119 ? 31.601  31.964  -10.899 1.00 24.25  ? 119 LEU   C CG    1 
ATOM   4392  C  CD1   . LEU   B 1  119 ? 32.835  31.244  -10.447 1.00 28.63  ? 119 LEU   C CD1   1 
ATOM   4393  C  CD2   . LEU   B 1  119 ? 30.846  32.411  -9.682  1.00 28.33  ? 119 LEU   C CD2   1 
ATOM   4394  N  N     . ASP   B 1  120 ? 31.777  35.104  -14.392 1.00 25.90  ? 120 ASP   C N     1 
ATOM   4395  C  CA    A ASP   B 1  120 ? 32.115  36.381  -15.024 0.43 27.54  ? 120 ASP   C CA    1 
ATOM   4396  C  CA    B ASP   B 1  120 ? 32.121  36.395  -14.977 0.57 27.55  ? 120 ASP   C CA    1 
ATOM   4397  C  C     . ASP   B 1  120 ? 30.865  37.213  -15.290 1.00 29.25  ? 120 ASP   C C     1 
ATOM   4398  O  O     . ASP   B 1  120 ? 30.825  38.414  -14.998 1.00 27.53  ? 120 ASP   C O     1 
ATOM   4399  C  CB    A ASP   B 1  120 ? 32.890  36.147  -16.320 0.43 27.78  ? 120 ASP   C CB    1 
ATOM   4400  C  CB    B ASP   B 1  120 ? 33.014  36.211  -16.208 0.57 27.69  ? 120 ASP   C CB    1 
ATOM   4401  C  CG    A ASP   B 1  120 ? 33.018  37.408  -17.163 0.43 25.32  ? 120 ASP   C CG    1 
ATOM   4402  C  CG    B ASP   B 1  120 ? 34.489  35.918  -15.842 0.57 26.40  ? 120 ASP   C CG    1 
ATOM   4403  O  OD1   A ASP   B 1  120 ? 33.656  38.374  -16.694 0.43 28.23  ? 120 ASP   C OD1   1 
ATOM   4404  O  OD1   B ASP   B 1  120 ? 34.792  35.683  -14.651 0.57 23.27  ? 120 ASP   C OD1   1 
ATOM   4405  O  OD2   A ASP   B 1  120 ? 32.485  37.433  -18.295 0.43 24.91  ? 120 ASP   C OD2   1 
ATOM   4406  O  OD2   B ASP   B 1  120 ? 35.351  35.916  -16.751 0.57 26.49  ? 120 ASP   C OD2   1 
ATOM   4407  N  N     . ARG   B 1  121 ? 29.811  36.581  -15.840 1.00 31.56  ? 121 ARG   C N     1 
ATOM   4408  C  CA    . ARG   B 1  121 ? 28.553  37.309  -16.057 1.00 30.39  ? 121 ARG   C CA    1 
ATOM   4409  C  C     . ARG   B 1  121 ? 27.918  37.753  -14.740 1.00 32.38  ? 121 ARG   C C     1 
ATOM   4410  O  O     . ARG   B 1  121 ? 27.397  38.871  -14.651 1.00 29.36  ? 121 ARG   C O     1 
ATOM   4411  C  CB    . ARG   B 1  121 ? 27.550  36.462  -16.833 1.00 27.22  ? 121 ARG   C CB    1 
ATOM   4412  C  CG    . ARG   B 1  121 ? 28.033  35.994  -18.176 1.00 34.75  ? 121 ARG   C CG    1 
ATOM   4413  C  CD    . ARG   B 1  121 ? 27.941  37.094  -19.217 1.00 38.73  ? 121 ARG   C CD    1 
ATOM   4414  N  NE    . ARG   B 1  121 ? 28.830  36.792  -20.329 1.00 44.48  ? 121 ARG   C NE    1 
ATOM   4415  C  CZ    . ARG   B 1  121 ? 28.493  36.082  -21.395 1.00 41.83  ? 121 ARG   C CZ    1 
ATOM   4416  N  NH1   . ARG   B 1  121 ? 27.263  35.617  -21.559 1.00 37.55  ? 121 ARG   C NH1   1 
ATOM   4417  N  NH2   . ARG   B 1  121 ? 29.413  35.833  -22.320 1.00 44.33  ? 121 ARG   C NH2   1 
ATOM   4418  N  N     . ILE   B 1  122 ? 27.898  36.873  -13.722 1.00 28.35  ? 122 ILE   C N     1 
ATOM   4419  C  CA    . ILE   B 1  122 ? 27.406  37.267  -12.399 1.00 28.53  ? 122 ILE   C CA    1 
ATOM   4420  C  C     . ILE   B 1  122 ? 28.161  38.495  -11.908 1.00 33.60  ? 122 ILE   C C     1 
ATOM   4421  O  O     . ILE   B 1  122 ? 27.582  39.407  -11.294 1.00 28.48  ? 122 ILE   C O     1 
ATOM   4422  C  CB    . ILE   B 1  122 ? 27.548  36.106  -11.396 1.00 25.86  ? 122 ILE   C CB    1 
ATOM   4423  C  CG1   . ILE   B 1  122 ? 26.670  34.923  -11.767 1.00 21.42  ? 122 ILE   C CG1   1 
ATOM   4424  C  CG2   . ILE   B 1  122 ? 27.293  36.580  -9.940  1.00 19.22  ? 122 ILE   C CG2   1 
ATOM   4425  C  CD1   . ILE   B 1  122 ? 26.737  33.830  -10.717 1.00 20.70  ? 122 ILE   C CD1   1 
ATOM   4426  N  N     . ARG   B 1  123 ? 29.477  38.521  -12.167 1.00 31.00  ? 123 ARG   C N     1 
ATOM   4427  C  CA    . ARG   B 1  123 ? 30.327  39.619  -11.738 1.00 26.57  ? 123 ARG   C CA    1 
ATOM   4428  C  C     . ARG   B 1  123 ? 29.961  40.921  -12.446 1.00 31.11  ? 123 ARG   C C     1 
ATOM   4429  O  O     . ARG   B 1  123 ? 29.951  41.987  -11.819 1.00 32.97  ? 123 ARG   C O     1 
ATOM   4430  C  CB    . ARG   B 1  123 ? 31.781  39.234  -11.978 1.00 27.11  ? 123 ARG   C CB    1 
ATOM   4431  C  CG    . ARG   B 1  123 ? 32.778  40.353  -11.820 1.00 35.73  ? 123 ARG   C CG    1 
ATOM   4432  C  CD    . ARG   B 1  123 ? 32.517  41.203  -10.584 1.00 32.42  ? 123 ARG   C CD    1 
ATOM   4433  N  NE    . ARG   B 1  123 ? 32.855  40.532  -9.335  1.00 38.11  ? 123 ARG   C NE    1 
ATOM   4434  C  CZ    . ARG   B 1  123 ? 32.907  41.148  -8.161  1.00 44.26  ? 123 ARG   C CZ    1 
ATOM   4435  N  NH1   . ARG   B 1  123 ? 32.662  42.454  -8.054  1.00 37.24  ? 123 ARG   C NH1   1 
ATOM   4436  N  NH2   . ARG   B 1  123 ? 33.216  40.443  -7.071  1.00 29.90  ? 123 ARG   C NH2   1 
ATOM   4437  N  N     . LYS   B 1  124 ? 29.634  40.862  -13.744 1.00 31.03  ? 124 LYS   C N     1 
ATOM   4438  C  CA    . LYS   B 1  124 ? 29.165  42.065  -14.434 1.00 31.62  ? 124 LYS   C CA    1 
ATOM   4439  C  C     . LYS   B 1  124 ? 27.913  42.620  -13.766 1.00 38.16  ? 124 LYS   C C     1 
ATOM   4440  O  O     . LYS   B 1  124 ? 27.710  43.842  -13.734 1.00 41.53  ? 124 LYS   C O     1 
ATOM   4441  C  CB    . LYS   B 1  124 ? 28.910  41.767  -15.922 1.00 31.69  ? 124 LYS   C CB    1 
ATOM   4442  C  CG    . LYS   B 1  124 ? 28.528  43.006  -16.800 1.00 58.17  ? 124 LYS   C CG    1 
ATOM   4443  C  CD    . LYS   B 1  124 ? 28.028  42.684  -18.272 1.00 63.26  ? 124 LYS   C CD    1 
ATOM   4444  C  CE    . LYS   B 1  124 ? 26.496  42.416  -18.351 1.00 49.66  ? 124 LYS   C CE    1 
ATOM   4445  N  NZ    . LYS   B 1  124 ? 25.885  42.519  -19.702 1.00 40.42  ? 124 LYS   C NZ    1 
ATOM   4446  N  N     . LEU   B 1  125 ? 27.087  41.735  -13.191 1.00 32.47  ? 125 LEU   C N     1 
ATOM   4447  C  CA    . LEU   B 1  125 ? 25.875  42.159  -12.502 1.00 26.03  ? 125 LEU   C CA    1 
ATOM   4448  C  C     . LEU   B 1  125 ? 26.195  42.771  -11.143 1.00 28.72  ? 125 LEU   C C     1 
ATOM   4449  O  O     . LEU   B 1  125 ? 25.623  43.806  -10.769 1.00 32.92  ? 125 LEU   C O     1 
ATOM   4450  C  CB    . LEU   B 1  125 ? 24.912  40.969  -12.371 1.00 19.50  ? 125 LEU   C CB    1 
ATOM   4451  C  CG    . LEU   B 1  125 ? 23.838  40.956  -13.469 1.00 21.97  ? 125 LEU   C CG    1 
ATOM   4452  C  CD1   . LEU   B 1  125 ? 23.123  39.636  -13.709 1.00 20.51  ? 125 LEU   C CD1   1 
ATOM   4453  C  CD2   . LEU   B 1  125 ? 22.853  42.031  -13.167 1.00 31.90  ? 125 LEU   C CD2   1 
ATOM   4454  N  N     . ALA   B 1  126 ? 27.113  42.152  -10.395 1.00 28.28  ? 126 ALA   C N     1 
ATOM   4455  C  CA    . ALA   B 1  126 ? 27.420  42.627  -9.046  1.00 36.69  ? 126 ALA   C CA    1 
ATOM   4456  C  C     . ALA   B 1  126 ? 27.919  44.064  -9.048  1.00 33.41  ? 126 ALA   C C     1 
ATOM   4457  O  O     . ALA   B 1  126 ? 27.701  44.792  -8.079  1.00 33.17  ? 126 ALA   C O     1 
ATOM   4458  C  CB    . ALA   B 1  126 ? 28.455  41.716  -8.379  1.00 27.53  ? 126 ALA   C CB    1 
ATOM   4459  N  N     . ASP   B 1  127 ? 28.579  44.491  -10.122 1.00 39.99  ? 127 ASP   C N     1 
ATOM   4460  C  CA    . ASP   B 1  127 ? 29.233  45.796  -10.159 1.00 36.78  ? 127 ASP   C CA    1 
ATOM   4461  C  C     . ASP   B 1  127 ? 28.286  46.942  -10.505 1.00 41.29  ? 127 ASP   C C     1 
ATOM   4462  O  O     . ASP   B 1  127 ? 28.684  48.108  -10.377 1.00 40.98  ? 127 ASP   C O     1 
ATOM   4463  C  CB    . ASP   B 1  127 ? 30.387  45.791  -11.161 1.00 29.94  ? 127 ASP   C CB    1 
ATOM   4464  C  CG    . ASP   B 1  127 ? 31.532  44.852  -10.772 1.00 38.83  ? 127 ASP   C CG    1 
ATOM   4465  O  OD1   . ASP   B 1  127 ? 31.519  44.177  -9.697  1.00 34.80  ? 127 ASP   C OD1   1 
ATOM   4466  O  OD2   . ASP   B 1  127 ? 32.475  44.799  -11.589 1.00 31.61  ? 127 ASP   C OD2   1 
ATOM   4467  N  N     . GLN   B 1  128 ? 27.064  46.660  -10.957 1.00 39.54  ? 128 GLN   C N     1 
ATOM   4468  C  CA    . GLN   B 1  128 ? 26.060  47.713  -11.048 1.00 39.24  ? 128 GLN   C CA    1 
ATOM   4469  C  C     . GLN   B 1  128 ? 25.410  48.006  -9.705  1.00 40.02  ? 128 GLN   C C     1 
ATOM   4470  O  O     . GLN   B 1  128 ? 24.514  48.859  -9.628  1.00 45.68  ? 128 GLN   C O     1 
ATOM   4471  C  CB    . GLN   B 1  128 ? 24.983  47.333  -12.050 1.00 33.85  ? 128 GLN   C CB    1 
ATOM   4472  C  CG    . GLN   B 1  128 ? 25.506  46.901  -13.392 1.00 47.63  ? 128 GLN   C CG    1 
ATOM   4473  C  CD    . GLN   B 1  128 ? 24.373  46.442  -14.285 1.00 57.27  ? 128 GLN   C CD    1 
ATOM   4474  O  OE1   . GLN   B 1  128 ? 23.326  45.997  -13.793 1.00 65.80  ? 128 GLN   C OE1   1 
ATOM   4475  N  NE2   . GLN   B 1  128 ? 24.559  46.566  -15.599 1.00 63.61  ? 128 GLN   C NE2   1 
ATOM   4476  N  N     . CYS   B 1  129 ? 25.859  47.330  -8.654  1.00 39.90  ? 129 CYS   C N     1 
ATOM   4477  C  CA    . CYS   B 1  129 ? 25.211  47.344  -7.355  1.00 43.51  ? 129 CYS   C CA    1 
ATOM   4478  C  C     . CYS   B 1  129 ? 25.983  48.272  -6.433  1.00 43.01  ? 129 CYS   C C     1 
ATOM   4479  O  O     . CYS   B 1  129 ? 27.193  48.104  -6.242  1.00 49.87  ? 129 CYS   C O     1 
ATOM   4480  C  CB    . CYS   B 1  129 ? 25.150  45.931  -6.763  1.00 50.19  ? 129 CYS   C CB    1 
ATOM   4481  S  SG    . CYS   B 1  129 ? 24.034  44.738  -7.607  1.00 32.67  ? 129 CYS   C SG    1 
ATOM   4482  N  N     . THR   B 1  130 ? 25.288  49.241  -5.862  1.00 36.90  ? 130 THR   C N     1 
ATOM   4483  C  CA    . THR   B 1  130 ? 25.930  50.049  -4.846  1.00 40.83  ? 130 THR   C CA    1 
ATOM   4484  C  C     . THR   B 1  130 ? 25.846  49.413  -3.465  1.00 40.10  ? 130 THR   C C     1 
ATOM   4485  O  O     . THR   B 1  130 ? 26.586  49.819  -2.565  1.00 45.02  ? 130 THR   C O     1 
ATOM   4486  C  CB    . THR   B 1  130 ? 25.328  51.461  -4.853  1.00 41.25  ? 130 THR   C CB    1 
ATOM   4487  O  OG1   . THR   B 1  130 ? 23.951  51.409  -4.473  1.00 50.93  ? 130 THR   C OG1   1 
ATOM   4488  C  CG2   . THR   B 1  130 ? 25.425  52.050  -6.245  1.00 34.63  ? 130 THR   C CG2   1 
ATOM   4489  N  N     . GLY   B 1  131 ? 25.000  48.406  -3.283  1.00 44.76  ? 131 GLY   C N     1 
ATOM   4490  C  CA    . GLY   B 1  131 ? 24.883  47.763  -1.990  1.00 36.18  ? 131 GLY   C CA    1 
ATOM   4491  C  C     . GLY   B 1  131 ? 24.385  46.335  -2.059  1.00 33.83  ? 131 GLY   C C     1 
ATOM   4492  O  O     . GLY   B 1  131 ? 23.409  45.997  -1.385  1.00 30.88  ? 131 GLY   C O     1 
ATOM   4493  N  N     . LEU   B 1  132 ? 25.034  45.496  -2.869  1.00 33.01  ? 132 LEU   C N     1 
ATOM   4494  C  CA    . LEU   B 1  132 ? 24.655  44.097  -3.008  1.00 25.52  ? 132 LEU   C CA    1 
ATOM   4495  C  C     . LEU   B 1  132 ? 24.358  43.473  -1.657  1.00 25.87  ? 132 LEU   C C     1 
ATOM   4496  O  O     . LEU   B 1  132 ? 25.236  43.372  -0.795  1.00 24.03  ? 132 LEU   C O     1 
ATOM   4497  C  CB    . LEU   B 1  132 ? 25.767  43.325  -3.693  1.00 19.30  ? 132 LEU   C CB    1 
ATOM   4498  C  CG    . LEU   B 1  132 ? 25.290  41.962  -4.127  1.00 23.10  ? 132 LEU   C CG    1 
ATOM   4499  C  CD1   . LEU   B 1  132 ? 24.027  42.093  -4.977  1.00 20.65  ? 132 LEU   C CD1   1 
ATOM   4500  C  CD2   . LEU   B 1  132 ? 26.398  41.344  -4.915  1.00 23.45  ? 132 LEU   C CD2   1 
ATOM   4501  N  N     . GLN   B 1  133 ? 23.104  43.090  -1.463  1.00 26.30  ? 133 GLN   C N     1 
ATOM   4502  C  CA    . GLN   B 1  133 ? 22.717  42.357  -0.274  1.00 24.57  ? 133 GLN   C CA    1 
ATOM   4503  C  C     . GLN   B 1  133 ? 23.040  40.875  -0.422  1.00 24.48  ? 133 GLN   C C     1 
ATOM   4504  O  O     . GLN   B 1  133 ? 23.711  40.312  0.446   1.00 25.21  ? 133 GLN   C O     1 
ATOM   4505  C  CB    . GLN   B 1  133 ? 21.232  42.576  0.013   1.00 29.57  ? 133 GLN   C CB    1 
ATOM   4506  C  CG    . GLN   B 1  133 ? 20.831  42.323  1.457   1.00 42.10  ? 133 GLN   C CG    1 
ATOM   4507  C  CD    . GLN   B 1  133 ? 19.326  42.126  1.606   1.00 56.61  ? 133 GLN   C CD    1 
ATOM   4508  O  OE1   . GLN   B 1  133 ? 18.583  43.079  1.853   1.00 65.09  ? 133 GLN   C OE1   1 
ATOM   4509  N  NE2   . GLN   B 1  133 ? 18.871  40.880  1.454   1.00 55.60  ? 133 GLN   C NE2   1 
ATOM   4510  N  N     . GLY   B 1  134 ? 22.607  40.239  -1.513  1.00 26.69  ? 134 GLY   C N     1 
ATOM   4511  C  CA    . GLY   B 1  134 ? 23.059  38.886  -1.796  1.00 22.97  ? 134 GLY   C CA    1 
ATOM   4512  C  C     . GLY   B 1  134 ? 22.357  38.257  -2.992  1.00 22.78  ? 134 GLY   C C     1 
ATOM   4513  O  O     . GLY   B 1  134 ? 21.785  38.948  -3.835  1.00 20.69  ? 134 GLY   C O     1 
ATOM   4514  N  N     . PHE   B 1  135 ? 22.396  36.918  -3.015  1.00 21.97  ? 135 PHE   C N     1 
ATOM   4515  C  CA    . PHE   B 1  135 ? 21.999  36.071  -4.133  1.00 24.56  ? 135 PHE   C CA    1 
ATOM   4516  C  C     . PHE   B 1  135 ? 20.763  35.229  -3.805  1.00 26.53  ? 135 PHE   C C     1 
ATOM   4517  O  O     . PHE   B 1  135 ? 20.618  34.753  -2.677  1.00 20.17  ? 135 PHE   C O     1 
ATOM   4518  C  CB    . PHE   B 1  135 ? 23.168  35.141  -4.493  1.00 25.64  ? 135 PHE   C CB    1 
ATOM   4519  C  CG    . PHE   B 1  135 ? 24.352  35.865  -5.040  1.00 27.33  ? 135 PHE   C CG    1 
ATOM   4520  C  CD1   . PHE   B 1  135 ? 24.407  36.211  -6.387  1.00 27.51  ? 135 PHE   C CD1   1 
ATOM   4521  C  CD2   . PHE   B 1  135 ? 25.392  36.234  -4.212  1.00 22.24  ? 135 PHE   C CD2   1 
ATOM   4522  C  CE1   . PHE   B 1  135 ? 25.483  36.890  -6.894  1.00 26.43  ? 135 PHE   C CE1   1 
ATOM   4523  C  CE2   . PHE   B 1  135 ? 26.474  36.928  -4.711  1.00 22.48  ? 135 PHE   C CE2   1 
ATOM   4524  C  CZ    . PHE   B 1  135 ? 26.522  37.252  -6.051  1.00 24.78  ? 135 PHE   C CZ    1 
ATOM   4525  N  N     . LEU   B 1  136 ? 19.879  35.036  -4.802  1.00 21.68  ? 136 LEU   C N     1 
ATOM   4526  C  CA    . LEU   B 1  136 ? 18.806  34.035  -4.769  1.00 20.46  ? 136 LEU   C CA    1 
ATOM   4527  C  C     . LEU   B 1  136 ? 19.062  33.014  -5.866  1.00 23.25  ? 136 LEU   C C     1 
ATOM   4528  O  O     . LEU   B 1  136 ? 19.112  33.383  -7.044  1.00 26.32  ? 136 LEU   C O     1 
ATOM   4529  C  CB    . LEU   B 1  136 ? 17.419  34.640  -5.000  1.00 22.38  ? 136 LEU   C CB    1 
ATOM   4530  C  CG    . LEU   B 1  136 ? 16.895  35.865  -4.271  1.00 21.73  ? 136 LEU   C CG    1 
ATOM   4531  C  CD1   . LEU   B 1  136 ? 15.438  36.078  -4.660  1.00 25.07  ? 136 LEU   C CD1   1 
ATOM   4532  C  CD2   . LEU   B 1  136 ? 17.042  35.700  -2.790  1.00 15.35  ? 136 LEU   C CD2   1 
ATOM   4533  N  N     . VAL   B 1  137 ? 19.172  31.736  -5.499  1.00 16.39  ? 137 VAL   C N     1 
ATOM   4534  C  CA    . VAL   B 1  137 ? 19.531  30.685  -6.445  1.00 14.32  ? 137 VAL   C CA    1 
ATOM   4535  C  C     . VAL   B 1  137 ? 18.358  29.730  -6.568  1.00 18.98  ? 137 VAL   C C     1 
ATOM   4536  O  O     . VAL   B 1  137 ? 17.906  29.169  -5.568  1.00 20.48  ? 137 VAL   C O     1 
ATOM   4537  C  CB    . VAL   B 1  137 ? 20.796  29.942  -6.008  1.00 19.18  ? 137 VAL   C CB    1 
ATOM   4538  C  CG1   . VAL   B 1  137 ? 21.058  28.737  -6.905  1.00 22.70  ? 137 VAL   C CG1   1 
ATOM   4539  C  CG2   . VAL   B 1  137 ? 21.962  30.891  -5.995  1.00 14.40  ? 137 VAL   C CG2   1 
ATOM   4540  N  N     . PHE   B 1  138 ? 17.852  29.564  -7.788  1.00 24.47  ? 138 PHE   C N     1 
ATOM   4541  C  CA    . PHE   B 1  138 ? 16.686  28.731  -8.074  1.00 20.82  ? 138 PHE   C CA    1 
ATOM   4542  C  C     . PHE   B 1  138 ? 17.148  27.494  -8.840  1.00 21.57  ? 138 PHE   C C     1 
ATOM   4543  O  O     . PHE   B 1  138 ? 17.769  27.618  -9.897  1.00 24.68  ? 138 PHE   C O     1 
ATOM   4544  C  CB    . PHE   B 1  138 ? 15.661  29.498  -8.902  1.00 15.86  ? 138 PHE   C CB    1 
ATOM   4545  C  CG    . PHE   B 1  138 ? 15.122  30.724  -8.245  1.00 17.42  ? 138 PHE   C CG    1 
ATOM   4546  C  CD1   . PHE   B 1  138 ? 15.936  31.814  -7.984  1.00 23.00  ? 138 PHE   C CD1   1 
ATOM   4547  C  CD2   . PHE   B 1  138 ? 13.773  30.833  -7.968  1.00 19.91  ? 138 PHE   C CD2   1 
ATOM   4548  C  CE1   . PHE   B 1  138 ? 15.425  32.984  -7.371  1.00 22.29  ? 138 PHE   C CE1   1 
ATOM   4549  C  CE2   . PHE   B 1  138 ? 13.258  32.000  -7.378  1.00 21.07  ? 138 PHE   C CE2   1 
ATOM   4550  C  CZ    . PHE   B 1  138 ? 14.093  33.070  -7.080  1.00 18.39  ? 138 PHE   C CZ    1 
ATOM   4551  N  N     . HIS   B 1  139 ? 16.848  26.307  -8.330  1.00 20.53  ? 139 HIS   C N     1 
ATOM   4552  C  CA    . HIS   B 1  139 ? 17.364  25.106  -8.984  1.00 23.10  ? 139 HIS   C CA    1 
ATOM   4553  C  C     . HIS   B 1  139 ? 16.537  23.915  -8.539  1.00 23.02  ? 139 HIS   C C     1 
ATOM   4554  O  O     . HIS   B 1  139 ? 15.787  23.986  -7.568  1.00 30.00  ? 139 HIS   C O     1 
ATOM   4555  C  CB    . HIS   B 1  139 ? 18.848  24.877  -8.661  1.00 18.84  ? 139 HIS   C CB    1 
ATOM   4556  C  CG    . HIS   B 1  139 ? 19.124  24.707  -7.196  1.00 19.13  ? 139 HIS   C CG    1 
ATOM   4557  N  ND1   . HIS   B 1  139 ? 19.552  23.519  -6.652  1.00 25.54  ? 139 HIS   C ND1   1 
ATOM   4558  C  CD2   . HIS   B 1  139 ? 19.009  25.572  -6.158  1.00 24.39  ? 139 HIS   C CD2   1 
ATOM   4559  C  CE1   . HIS   B 1  139 ? 19.698  23.663  -5.345  1.00 25.91  ? 139 HIS   C CE1   1 
ATOM   4560  N  NE2   . HIS   B 1  139 ? 19.371  24.899  -5.019  1.00 18.90  ? 139 HIS   C NE2   1 
ATOM   4561  N  N     . SER   B 1  140 ? 16.696  22.820  -9.251  1.00 19.80  ? 140 SER   C N     1 
ATOM   4562  C  CA    . SER   B 1  140 ? 16.100  21.562  -8.847  1.00 26.23  ? 140 SER   C CA    1 
ATOM   4563  C  C     . SER   B 1  140 ? 17.084  20.726  -8.018  1.00 22.48  ? 140 SER   C C     1 
ATOM   4564  O  O     . SER   B 1  140 ? 18.305  20.871  -8.116  1.00 20.24  ? 140 SER   C O     1 
ATOM   4565  C  CB    . SER   B 1  140 ? 15.648  20.794  -10.091 1.00 21.44  ? 140 SER   C CB    1 
ATOM   4566  O  OG    . SER   B 1  140 ? 16.778  20.369  -10.819 1.00 26.89  ? 140 SER   C OG    1 
ATOM   4567  N  N     . PHE   B 1  141 ? 16.535  19.842  -7.190  1.00 19.62  ? 141 PHE   C N     1 
ATOM   4568  C  CA    . PHE   B 1  141 ? 17.384  18.891  -6.478  1.00 21.10  ? 141 PHE   C CA    1 
ATOM   4569  C  C     . PHE   B 1  141 ? 17.898  17.811  -7.411  1.00 27.20  ? 141 PHE   C C     1 
ATOM   4570  O  O     . PHE   B 1  141 ? 19.073  17.423  -7.339  1.00 30.36  ? 141 PHE   C O     1 
ATOM   4571  C  CB    . PHE   B 1  141 ? 16.616  18.223  -5.339  1.00 20.97  ? 141 PHE   C CB    1 
ATOM   4572  C  CG    . PHE   B 1  141 ? 16.768  18.899  -4.046  1.00 22.53  ? 141 PHE   C CG    1 
ATOM   4573  C  CD1   . PHE   B 1  141 ? 17.713  19.892  -3.878  1.00 17.06  ? 141 PHE   C CD1   1 
ATOM   4574  C  CD2   . PHE   B 1  141 ? 15.984  18.529  -2.973  1.00 27.74  ? 141 PHE   C CD2   1 
ATOM   4575  C  CE1   . PHE   B 1  141 ? 17.840  20.522  -2.673  1.00 19.18  ? 141 PHE   C CE1   1 
ATOM   4576  C  CE2   . PHE   B 1  141 ? 16.123  19.152  -1.741  1.00 28.10  ? 141 PHE   C CE2   1 
ATOM   4577  C  CZ    . PHE   B 1  141 ? 17.048  20.152  -1.593  1.00 22.46  ? 141 PHE   C CZ    1 
ATOM   4578  N  N     . GLY   B 1  142 ? 17.017  17.303  -8.283  1.00 25.90  ? 142 GLY   C N     1 
ATOM   4579  C  CA    . GLY   B 1  142 ? 17.227  16.052  -8.991  1.00 21.23  ? 142 GLY   C CA    1 
ATOM   4580  C  C     . GLY   B 1  142 ? 17.826  16.144  -10.385 1.00 28.54  ? 142 GLY   C C     1 
ATOM   4581  O  O     . GLY   B 1  142 ? 18.402  15.156  -10.866 1.00 30.17  ? 142 GLY   C O     1 
ATOM   4582  N  N     . GLY   B 1  143 ? 17.689  17.297  -11.059 1.00 23.49  ? 143 GLY   C N     1 
ATOM   4583  C  CA    . GLY   B 1  143 ? 18.346  17.459  -12.342 1.00 25.17  ? 143 GLY   C CA    1 
ATOM   4584  C  C     . GLY   B 1  143 ? 19.853  17.302  -12.241 1.00 20.06  ? 143 GLY   C C     1 
ATOM   4585  O  O     . GLY   B 1  143 ? 20.404  17.306  -11.141 1.00 20.83  ? 143 GLY   C O     1 
ATOM   4586  N  N     . GLY   B 1  144 ? 20.542  17.155  -13.367 1.00 26.02  ? 144 GLY   C N     1 
ATOM   4587  C  CA    . GLY   B 1  144 ? 21.982  17.011  -13.290 1.00 25.73  ? 144 GLY   C CA    1 
ATOM   4588  C  C     . GLY   B 1  144 ? 22.693  18.341  -13.171 1.00 22.03  ? 144 GLY   C C     1 
ATOM   4589  O  O     . GLY   B 1  144 ? 23.725  18.452  -12.506 1.00 25.02  ? 144 GLY   C O     1 
ATOM   4590  N  N     . THR   B 1  145 ? 22.165  19.345  -13.859 1.00 20.87  ? 145 THR   C N     1 
ATOM   4591  C  CA    . THR   B 1  145 ? 22.671  20.701  -13.751 1.00 15.48  ? 145 THR   C CA    1 
ATOM   4592  C  C     . THR   B 1  145 ? 22.139  21.365  -12.503 1.00 20.02  ? 145 THR   C C     1 
ATOM   4593  O  O     . THR   B 1  145 ? 22.888  22.048  -11.789 1.00 24.32  ? 145 THR   C O     1 
ATOM   4594  C  CB    . THR   B 1  145 ? 22.269  21.495  -14.987 1.00 11.96  ? 145 THR   C CB    1 
ATOM   4595  O  OG1   . THR   B 1  145 ? 22.761  20.813  -16.140 1.00 24.20  ? 145 THR   C OG1   1 
ATOM   4596  C  CG2   . THR   B 1  145 ? 22.831  22.851  -14.969 1.00 15.28  ? 145 THR   C CG2   1 
ATOM   4597  N  N     . GLY   B 1  146 ? 20.854  21.152  -12.214 1.00 22.68  ? 146 GLY   C N     1 
ATOM   4598  C  CA    . GLY   B 1  146 ? 20.237  21.797  -11.063 1.00 22.26  ? 146 GLY   C CA    1 
ATOM   4599  C  C     . GLY   B 1  146 ? 20.849  21.376  -9.744  1.00 19.58  ? 146 GLY   C C     1 
ATOM   4600  O  O     . GLY   B 1  146 ? 20.817  22.127  -8.767  1.00 25.03  ? 146 GLY   C O     1 
ATOM   4601  N  N     . SER   B 1  147 ? 21.434  20.186  -9.695  1.00 19.06  ? 147 SER   C N     1 
ATOM   4602  C  CA    . SER   B 1  147 ? 22.103  19.737  -8.485  1.00 25.30  ? 147 SER   C CA    1 
ATOM   4603  C  C     . SER   B 1  147 ? 23.595  20.044  -8.533  1.00 25.21  ? 147 SER   C C     1 
ATOM   4604  O  O     . SER   B 1  147 ? 24.113  20.747  -7.657  1.00 24.53  ? 147 SER   C O     1 
ATOM   4605  C  CB    . SER   B 1  147 ? 21.852  18.232  -8.251  1.00 22.44  ? 147 SER   C CB    1 
ATOM   4606  O  OG    . SER   B 1  147 ? 22.403  17.455  -9.297  1.00 26.21  ? 147 SER   C OG    1 
ATOM   4607  N  N     . GLY   B 1  148 ? 24.286  19.551  -9.568  1.00 21.80  ? 148 GLY   C N     1 
ATOM   4608  C  CA    . GLY   B 1  148 ? 25.741  19.595  -9.583  1.00 23.70  ? 148 GLY   C CA    1 
ATOM   4609  C  C     . GLY   B 1  148 ? 26.337  20.926  -9.979  1.00 21.92  ? 148 GLY   C C     1 
ATOM   4610  O  O     . GLY   B 1  148 ? 27.411  21.286  -9.499  1.00 25.77  ? 148 GLY   C O     1 
ATOM   4611  N  N     . PHE   B 1  149 ? 25.675  21.671  -10.857 1.00 23.65  ? 149 PHE   C N     1 
ATOM   4612  C  CA    . PHE   B 1  149 ? 26.225  22.965  -11.225 1.00 21.29  ? 149 PHE   C CA    1 
ATOM   4613  C  C     . PHE   B 1  149 ? 25.861  24.034  -10.205 1.00 23.79  ? 149 PHE   C C     1 
ATOM   4614  O  O     . PHE   B 1  149 ? 26.658  24.937  -9.944  1.00 23.36  ? 149 PHE   C O     1 
ATOM   4615  C  CB    . PHE   B 1  149 ? 25.760  23.365  -12.631 1.00 19.36  ? 149 PHE   C CB    1 
ATOM   4616  C  CG    . PHE   B 1  149 ? 26.424  24.592  -13.138 1.00 21.60  ? 149 PHE   C CG    1 
ATOM   4617  C  CD1   . PHE   B 1  149 ? 27.699  24.528  -13.670 1.00 25.17  ? 149 PHE   C CD1   1 
ATOM   4618  C  CD2   . PHE   B 1  149 ? 25.809  25.830  -13.024 1.00 22.94  ? 149 PHE   C CD2   1 
ATOM   4619  C  CE1   . PHE   B 1  149 ? 28.347  25.688  -14.111 1.00 24.64  ? 149 PHE   C CE1   1 
ATOM   4620  C  CE2   . PHE   B 1  149 ? 26.445  26.977  -13.468 1.00 24.12  ? 149 PHE   C CE2   1 
ATOM   4621  C  CZ    . PHE   B 1  149 ? 27.715  26.905  -14.015 1.00 20.30  ? 149 PHE   C CZ    1 
ATOM   4622  N  N     . THR   B 1  150 ? 24.666  23.955  -9.620  1.00 27.81  ? 150 THR   C N     1 
ATOM   4623  C  CA    . THR   B 1  150 ? 24.330  24.856  -8.522  1.00 22.10  ? 150 THR   C CA    1 
ATOM   4624  C  C     . THR   B 1  150 ? 25.332  24.725  -7.375  1.00 24.65  ? 150 THR   C C     1 
ATOM   4625  O  O     . THR   B 1  150 ? 25.704  25.727  -6.762  1.00 23.69  ? 150 THR   C O     1 
ATOM   4626  C  CB    . THR   B 1  150 ? 22.905  24.585  -8.045  1.00 21.53  ? 150 THR   C CB    1 
ATOM   4627  O  OG1   . THR   B 1  150 ? 22.052  24.437  -9.183  1.00 22.18  ? 150 THR   C OG1   1 
ATOM   4628  C  CG2   . THR   B 1  150 ? 22.402  25.745  -7.204  1.00 25.50  ? 150 THR   C CG2   1 
ATOM   4629  N  N     . SER   B 1  151 ? 25.808  23.502  -7.098  1.00 23.26  ? 151 SER   C N     1 
ATOM   4630  C  CA    A SER   B 1  151 ? 26.753  23.311  -6.005  0.24 20.69  ? 151 SER   C CA    1 
ATOM   4631  C  CA    B SER   B 1  151 ? 26.763  23.285  -6.016  0.76 20.52  ? 151 SER   C CA    1 
ATOM   4632  C  C     . SER   B 1  151 ? 28.110  23.917  -6.340  1.00 23.76  ? 151 SER   C C     1 
ATOM   4633  O  O     . SER   B 1  151 ? 28.657  24.702  -5.556  1.00 29.16  ? 151 SER   C O     1 
ATOM   4634  C  CB    A SER   B 1  151 ? 26.889  21.826  -5.679  0.24 25.98  ? 151 SER   C CB    1 
ATOM   4635  C  CB    B SER   B 1  151 ? 26.936  21.786  -5.769  0.76 26.09  ? 151 SER   C CB    1 
ATOM   4636  O  OG    A SER   B 1  151 ? 27.636  21.153  -6.676  0.24 25.69  ? 151 SER   C OG    1 
ATOM   4637  O  OG    B SER   B 1  151 ? 25.816  21.219  -5.110  0.76 27.19  ? 151 SER   C OG    1 
ATOM   4638  N  N     . LEU   B 1  152 ? 28.676  23.553  -7.489  1.00 27.24  ? 152 LEU   C N     1 
ATOM   4639  C  CA    . LEU   B 1  152 ? 29.915  24.167  -7.947  1.00 26.20  ? 152 LEU   C CA    1 
ATOM   4640  C  C     . LEU   B 1  152 ? 29.822  25.685  -7.885  1.00 23.41  ? 152 LEU   C C     1 
ATOM   4641  O  O     . LEU   B 1  152 ? 30.744  26.353  -7.399  1.00 27.36  ? 152 LEU   C O     1 
ATOM   4642  C  CB    . LEU   B 1  152 ? 30.236  23.702  -9.378  1.00 27.98  ? 152 LEU   C CB    1 
ATOM   4643  C  CG    . LEU   B 1  152 ? 31.413  24.420  -10.068 1.00 26.25  ? 152 LEU   C CG    1 
ATOM   4644  C  CD1   . LEU   B 1  152 ? 32.727  24.130  -9.321  1.00 20.91  ? 152 LEU   C CD1   1 
ATOM   4645  C  CD2   . LEU   B 1  152 ? 31.512  24.099  -11.569 1.00 19.20  ? 152 LEU   C CD2   1 
ATOM   4646  N  N     . LEU   B 1  153 ? 28.697  26.242  -8.346  1.00 22.61  ? 153 LEU   C N     1 
ATOM   4647  C  CA    . LEU   B 1  153 ? 28.481  27.689  -8.311  1.00 21.72  ? 153 LEU   C CA    1 
ATOM   4648  C  C     . LEU   B 1  153 ? 28.421  28.234  -6.888  1.00 23.23  ? 153 LEU   C C     1 
ATOM   4649  O  O     . LEU   B 1  153 ? 28.966  29.310  -6.608  1.00 23.31  ? 153 LEU   C O     1 
ATOM   4650  C  CB    . LEU   B 1  153 ? 27.188  28.033  -9.028  1.00 22.55  ? 153 LEU   C CB    1 
ATOM   4651  C  CG    . LEU   B 1  153 ? 26.836  29.509  -8.944  1.00 19.25  ? 153 LEU   C CG    1 
ATOM   4652  C  CD1   . LEU   B 1  153 ? 27.569  30.289  -10.043 1.00 19.41  ? 153 LEU   C CD1   1 
ATOM   4653  C  CD2   . LEU   B 1  153 ? 25.353  29.620  -9.063  1.00 18.63  ? 153 LEU   C CD2   1 
ATOM   4654  N  N     . MET   B 1  154 ? 27.702  27.549  -5.995  1.00 21.42  ? 154 MET   C N     1 
ATOM   4655  C  CA    . MET   B 1  154 ? 27.674  27.978  -4.606  1.00 21.25  ? 154 MET   C CA    1 
ATOM   4656  C  C     . MET   B 1  154 ? 29.091  28.042  -4.054  1.00 28.06  ? 154 MET   C C     1 
ATOM   4657  O  O     . MET   B 1  154 ? 29.516  29.087  -3.542  1.00 30.17  ? 154 MET   C O     1 
ATOM   4658  C  CB    . MET   B 1  154 ? 26.785  27.054  -3.757  1.00 20.70  ? 154 MET   C CB    1 
ATOM   4659  C  CG    . MET   B 1  154 ? 25.269  27.103  -4.074  1.00 17.24  ? 154 MET   C CG    1 
ATOM   4660  S  SD    . MET   B 1  154 ? 24.377  28.643  -3.782  1.00 26.07  ? 154 MET   C SD    1 
ATOM   4661  C  CE    . MET   B 1  154 ? 24.111  28.497  -1.991  1.00 19.23  ? 154 MET   C CE    1 
ATOM   4662  N  N     . GLU   B 1  155 ? 29.857  26.943  -4.176  1.00 24.24  ? 155 GLU   C N     1 
ATOM   4663  C  CA    . GLU   B 1  155 ? 31.245  26.982  -3.708  1.00 24.10  ? 155 GLU   C CA    1 
ATOM   4664  C  C     . GLU   B 1  155 ? 32.003  28.139  -4.346  1.00 25.61  ? 155 GLU   C C     1 
ATOM   4665  O  O     . GLU   B 1  155 ? 32.900  28.718  -3.728  1.00 27.84  ? 155 GLU   C O     1 
ATOM   4666  C  CB    . GLU   B 1  155 ? 31.977  25.672  -4.009  1.00 22.92  ? 155 GLU   C CB    1 
ATOM   4667  C  CG    . GLU   B 1  155 ? 31.578  24.483  -3.164  1.00 23.24  ? 155 GLU   C CG    1 
ATOM   4668  C  CD    . GLU   B 1  155 ? 31.892  23.136  -3.819  1.00 34.22  ? 155 GLU   C CD    1 
ATOM   4669  O  OE1   . GLU   B 1  155 ? 32.530  23.091  -4.901  1.00 45.07  ? 155 GLU   C OE1   1 
ATOM   4670  O  OE2   . GLU   B 1  155 ? 31.484  22.101  -3.251  1.00 34.64  ? 155 GLU   C OE2   1 
ATOM   4671  N  N     . ARG   B 1  156 ? 31.645  28.507  -5.572  1.00 23.07  ? 156 ARG   C N     1 
ATOM   4672  C  CA    . ARG   B 1  156 ? 32.424  29.528  -6.249  1.00 25.28  ? 156 ARG   C CA    1 
ATOM   4673  C  C     . ARG   B 1  156 ? 32.005  30.926  -5.824  1.00 30.27  ? 156 ARG   C C     1 
ATOM   4674  O  O     . ARG   B 1  156 ? 32.856  31.816  -5.719  1.00 28.84  ? 156 ARG   C O     1 
ATOM   4675  C  CB    . ARG   B 1  156 ? 32.323  29.346  -7.764  1.00 28.62  ? 156 ARG   C CB    1 
ATOM   4676  C  CG    . ARG   B 1  156 ? 33.295  28.275  -8.277  1.00 29.28  ? 156 ARG   C CG    1 
ATOM   4677  C  CD    . ARG   B 1  156 ? 34.746  28.681  -7.960  1.00 34.75  ? 156 ARG   C CD    1 
ATOM   4678  N  NE    . ARG   B 1  156 ? 35.247  29.614  -8.960  1.00 33.13  ? 156 ARG   C NE    1 
ATOM   4679  C  CZ    . ARG   B 1  156 ? 35.548  29.259  -10.202 1.00 32.05  ? 156 ARG   C CZ    1 
ATOM   4680  N  NH1   . ARG   B 1  156 ? 35.513  27.986  -10.584 1.00 29.47  ? 156 ARG   C NH1   1 
ATOM   4681  N  NH2   . ARG   B 1  156 ? 35.860  30.202  -11.088 1.00 21.36  ? 156 ARG   C NH2   1 
ATOM   4682  N  N     . LEU   B 1  157 ? 30.705  31.137  -5.577  1.00 30.09  ? 157 LEU   C N     1 
ATOM   4683  C  CA    . LEU   B 1  157 ? 30.244  32.411  -5.042  1.00 20.78  ? 157 LEU   C CA    1 
ATOM   4684  C  C     . LEU   B 1  157 ? 30.696  32.609  -3.594  1.00 26.59  ? 157 LEU   C C     1 
ATOM   4685  O  O     . LEU   B 1  157 ? 30.847  33.748  -3.143  1.00 30.56  ? 157 LEU   C O     1 
ATOM   4686  C  CB    . LEU   B 1  157 ? 28.725  32.494  -5.153  1.00 22.50  ? 157 LEU   C CB    1 
ATOM   4687  C  CG    . LEU   B 1  157 ? 28.102  32.460  -6.551  1.00 26.00  ? 157 LEU   C CG    1 
ATOM   4688  C  CD1   . LEU   B 1  157 ? 26.575  32.366  -6.511  1.00 17.96  ? 157 LEU   C CD1   1 
ATOM   4689  C  CD2   . LEU   B 1  157 ? 28.503  33.703  -7.278  1.00 26.10  ? 157 LEU   C CD2   1 
ATOM   4690  N  N     . SER   B 1  158 ? 30.924  31.529  -2.843  1.00 27.90  ? 158 SER   C N     1 
ATOM   4691  C  CA    . SER   B 1  158 ? 31.486  31.693  -1.501  1.00 33.28  ? 158 SER   C CA    1 
ATOM   4692  C  C     . SER   B 1  158 ? 32.920  32.195  -1.567  1.00 34.23  ? 158 SER   C C     1 
ATOM   4693  O  O     . SER   B 1  158 ? 33.338  33.014  -0.739  1.00 30.58  ? 158 SER   C O     1 
ATOM   4694  C  CB    . SER   B 1  158 ? 31.436  30.377  -0.724  1.00 27.92  ? 158 SER   C CB    1 
ATOM   4695  O  OG    . SER   B 1  158 ? 30.167  30.172  -0.150  1.00 24.33  ? 158 SER   C OG    1 
ATOM   4696  N  N     . VAL   B 1  159 ? 33.695  31.686  -2.528  1.00 33.15  ? 159 VAL   C N     1 
ATOM   4697  C  CA    . VAL   B 1  159 ? 35.056  32.169  -2.734  1.00 32.06  ? 159 VAL   C CA    1 
ATOM   4698  C  C     . VAL   B 1  159 ? 35.039  33.607  -3.242  1.00 29.54  ? 159 VAL   C C     1 
ATOM   4699  O  O     . VAL   B 1  159 ? 35.748  34.472  -2.718  1.00 42.84  ? 159 VAL   C O     1 
ATOM   4700  C  CB    . VAL   B 1  159 ? 35.809  31.232  -3.695  1.00 35.60  ? 159 VAL   C CB    1 
ATOM   4701  C  CG1   . VAL   B 1  159 ? 36.603  32.035  -4.738  1.00 26.00  ? 159 VAL   C CG1   1 
ATOM   4702  C  CG2   . VAL   B 1  159 ? 36.690  30.239  -2.912  1.00 31.57  ? 159 VAL   C CG2   1 
ATOM   4703  N  N     . ASP   B 1  160 ? 34.207  33.888  -4.246  1.00 26.35  ? 160 ASP   C N     1 
ATOM   4704  C  CA    . ASP   B 1  160 ? 34.195  35.186  -4.908  1.00 23.15  ? 160 ASP   C CA    1 
ATOM   4705  C  C     . ASP   B 1  160 ? 33.530  36.283  -4.085  1.00 28.27  ? 160 ASP   C C     1 
ATOM   4706  O  O     . ASP   B 1  160 ? 33.763  37.464  -4.361  1.00 39.35  ? 160 ASP   C O     1 
ATOM   4707  C  CB    . ASP   B 1  160 ? 33.485  35.079  -6.260  1.00 25.81  ? 160 ASP   C CB    1 
ATOM   4708  C  CG    . ASP   B 1  160 ? 34.417  34.619  -7.407  1.00 39.33  ? 160 ASP   C CG    1 
ATOM   4709  O  OD1   . ASP   B 1  160 ? 35.198  33.642  -7.235  1.00 37.58  ? 160 ASP   C OD1   1 
ATOM   4710  O  OD2   . ASP   B 1  160 ? 34.338  35.239  -8.499  1.00 29.18  ? 160 ASP   C OD2   1 
ATOM   4711  N  N     . TYR   B 1  161 ? 32.712  35.937  -3.087  1.00 26.66  ? 161 TYR   C N     1 
ATOM   4712  C  CA    . TYR   B 1  161 ? 31.913  36.922  -2.362  1.00 23.13  ? 161 TYR   C CA    1 
ATOM   4713  C  C     . TYR   B 1  161 ? 31.884  36.681  -0.853  1.00 30.80  ? 161 TYR   C C     1 
ATOM   4714  O  O     . TYR   B 1  161 ? 31.055  37.282  -0.156  1.00 30.14  ? 161 TYR   C O     1 
ATOM   4715  C  CB    . TYR   B 1  161 ? 30.476  36.940  -2.897  1.00 21.66  ? 161 TYR   C CB    1 
ATOM   4716  C  CG    . TYR   B 1  161 ? 30.348  37.420  -4.320  1.00 24.13  ? 161 TYR   C CG    1 
ATOM   4717  C  CD1   . TYR   B 1  161 ? 30.231  38.762  -4.602  1.00 17.64  ? 161 TYR   C CD1   1 
ATOM   4718  C  CD2   . TYR   B 1  161 ? 30.346  36.525  -5.394  1.00 25.02  ? 161 TYR   C CD2   1 
ATOM   4719  C  CE1   . TYR   B 1  161 ? 30.120  39.211  -5.909  1.00 21.60  ? 161 TYR   C CE1   1 
ATOM   4720  C  CE2   . TYR   B 1  161 ? 30.235  36.971  -6.716  1.00 16.67  ? 161 TYR   C CE2   1 
ATOM   4721  C  CZ    . TYR   B 1  161 ? 30.117  38.319  -6.960  1.00 20.29  ? 161 TYR   C CZ    1 
ATOM   4722  O  OH    . TYR   B 1  161 ? 30.002  38.810  -8.247  1.00 26.61  ? 161 TYR   C OH    1 
ATOM   4723  N  N     . GLY   B 1  162 ? 32.742  35.812  -0.333  1.00 31.44  ? 162 GLY   C N     1 
ATOM   4724  C  CA    . GLY   B 1  162 ? 32.724  35.539  1.094   1.00 40.95  ? 162 GLY   C CA    1 
ATOM   4725  C  C     . GLY   B 1  162 ? 31.330  35.227  1.614   1.00 46.39  ? 162 GLY   C C     1 
ATOM   4726  O  O     . GLY   B 1  162 ? 30.549  34.499  0.978   1.00 50.26  ? 162 GLY   C O     1 
ATOM   4727  N  N     . LYS   B 1  163 ? 30.997  35.810  2.774   1.00 41.52  ? 163 LYS   C N     1 
ATOM   4728  C  CA    . LYS   B 1  163 ? 29.801  35.465  3.541   1.00 42.02  ? 163 LYS   C CA    1 
ATOM   4729  C  C     . LYS   B 1  163 ? 28.541  36.217  3.088   1.00 51.32  ? 163 LYS   C C     1 
ATOM   4730  O  O     . LYS   B 1  163 ? 27.449  35.940  3.616   1.00 47.65  ? 163 LYS   C O     1 
ATOM   4731  C  CB    . LYS   B 1  163 ? 30.061  35.710  5.038   1.00 48.08  ? 163 LYS   C CB    1 
ATOM   4732  C  CG    . LYS   B 1  163 ? 31.077  34.753  5.672   1.00 43.42  ? 163 LYS   C CG    1 
ATOM   4733  C  CD    . LYS   B 1  163 ? 30.595  33.315  5.596   1.00 39.57  ? 163 LYS   C CD    1 
ATOM   4734  C  CE    . LYS   B 1  163 ? 31.331  32.454  6.601   1.00 43.22  ? 163 LYS   C CE    1 
ATOM   4735  N  NZ    . LYS   B 1  163 ? 30.544  31.248  6.981   1.00 29.85  ? 163 LYS   C NZ    1 
ATOM   4736  N  N     . LYS   B 1  164 ? 28.673  37.154  2.135   1.00 36.99  ? 164 LYS   C N     1 
ATOM   4737  C  CA    . LYS   B 1  164 ? 27.544  37.738  1.415   1.00 26.33  ? 164 LYS   C CA    1 
ATOM   4738  C  C     . LYS   B 1  164 ? 26.445  36.712  1.150   1.00 30.07  ? 164 LYS   C C     1 
ATOM   4739  O  O     . LYS   B 1  164 ? 26.712  35.565  0.774   1.00 33.24  ? 164 LYS   C O     1 
ATOM   4740  C  CB    . LYS   B 1  164 ? 28.049  38.317  0.096   1.00 26.68  ? 164 LYS   C CB    1 
ATOM   4741  C  CG    . LYS   B 1  164 ? 26.967  38.812  -0.791  1.00 23.93  ? 164 LYS   C CG    1 
ATOM   4742  C  CD    . LYS   B 1  164 ? 27.270  40.205  -1.196  1.00 25.55  ? 164 LYS   C CD    1 
ATOM   4743  C  CE    . LYS   B 1  164 ? 27.411  41.111  0.011   1.00 24.95  ? 164 LYS   C CE    1 
ATOM   4744  N  NZ    . LYS   B 1  164 ? 27.756  42.499  -0.430  1.00 34.58  ? 164 LYS   C NZ    1 
ATOM   4745  N  N     . SER   B 1  165 ? 25.201  37.162  1.276   1.00 26.97  ? 165 SER   C N     1 
ATOM   4746  C  CA    . SER   B 1  165 ? 24.081  36.255  1.502   1.00 22.05  ? 165 SER   C CA    1 
ATOM   4747  C  C     . SER   B 1  165 ? 23.728  35.449  0.257   1.00 23.72  ? 165 SER   C C     1 
ATOM   4748  O  O     . SER   B 1  165 ? 23.637  35.991  -0.845  1.00 28.69  ? 165 SER   C O     1 
ATOM   4749  C  CB    . SER   B 1  165 ? 22.857  37.050  1.959   1.00 23.62  ? 165 SER   C CB    1 
ATOM   4750  O  OG    . SER   B 1  165 ? 21.937  36.239  2.663   1.00 26.92  ? 165 SER   C OG    1 
ATOM   4751  N  N     . LYS   B 1  166 ? 23.497  34.148  0.452   1.00 23.85  ? 166 LYS   C N     1 
ATOM   4752  C  CA    . LYS   B 1  166 ? 22.988  33.249  -0.579  1.00 18.06  ? 166 LYS   C CA    1 
ATOM   4753  C  C     . LYS   B 1  166 ? 21.737  32.533  -0.062  1.00 21.24  ? 166 LYS   C C     1 
ATOM   4754  O  O     . LYS   B 1  166 ? 21.822  31.716  0.853   1.00 27.36  ? 166 LYS   C O     1 
ATOM   4755  C  CB    . LYS   B 1  166 ? 24.071  32.263  -0.996  1.00 17.00  ? 166 LYS   C CB    1 
ATOM   4756  C  CG    . LYS   B 1  166 ? 25.266  32.946  -1.697  1.00 25.62  ? 166 LYS   C CG    1 
ATOM   4757  C  CD    . LYS   B 1  166 ? 26.491  32.025  -1.914  1.00 21.39  ? 166 LYS   C CD    1 
ATOM   4758  C  CE    . LYS   B 1  166 ? 27.464  32.102  -0.720  1.00 38.37  ? 166 LYS   C CE    1 
ATOM   4759  N  NZ    . LYS   B 1  166 ? 28.085  33.488  -0.531  1.00 45.17  ? 166 LYS   C NZ    1 
ATOM   4760  N  N     . LEU   B 1  167 ? 20.571  32.866  -0.626  1.00 20.31  ? 167 LEU   C N     1 
ATOM   4761  C  CA    . LEU   B 1  167 ? 19.304  32.190  -0.374  1.00 14.05  ? 167 LEU   C CA    1 
ATOM   4762  C  C     . LEU   B 1  167 ? 18.990  31.259  -1.539  1.00 20.08  ? 167 LEU   C C     1 
ATOM   4763  O  O     . LEU   B 1  167 ? 19.236  31.592  -2.702  1.00 23.61  ? 167 LEU   C O     1 
ATOM   4764  C  CB    . LEU   B 1  167 ? 18.156  33.200  -0.193  1.00 14.50  ? 167 LEU   C CB    1 
ATOM   4765  C  CG    . LEU   B 1  167 ? 17.753  33.800  1.180   1.00 20.55  ? 167 LEU   C CG    1 
ATOM   4766  C  CD1   . LEU   B 1  167 ? 18.921  34.193  2.083   1.00 21.61  ? 167 LEU   C CD1   1 
ATOM   4767  C  CD2   . LEU   B 1  167 ? 16.892  35.003  0.976   1.00 13.36  ? 167 LEU   C CD2   1 
ATOM   4768  N  N     . GLU   B 1  168 ? 18.428  30.098  -1.223  1.00 25.06  ? 168 GLU   C N     1 
ATOM   4769  C  CA    . GLU   B 1  168 ? 18.102  29.058  -2.186  1.00 17.40  ? 168 GLU   C CA    1 
ATOM   4770  C  C     . GLU   B 1  168 ? 16.599  28.840  -2.266  1.00 20.17  ? 168 GLU   C C     1 
ATOM   4771  O  O     . GLU   B 1  168 ? 15.890  28.925  -1.253  1.00 19.89  ? 168 GLU   C O     1 
ATOM   4772  C  CB    . GLU   B 1  168 ? 18.710  27.720  -1.799  1.00 19.78  ? 168 GLU   C CB    1 
ATOM   4773  C  CG    . GLU   B 1  168 ? 20.159  27.523  -2.022  1.00 17.48  ? 168 GLU   C CG    1 
ATOM   4774  C  CD    . GLU   B 1  168 ? 20.547  26.118  -1.609  1.00 21.96  ? 168 GLU   C CD    1 
ATOM   4775  O  OE1   . GLU   B 1  168 ? 20.567  25.842  -0.382  1.00 31.10  ? 168 GLU   C OE1   1 
ATOM   4776  O  OE2   . GLU   B 1  168 ? 20.782  25.282  -2.505  1.00 20.81  ? 168 GLU   C OE2   1 
ATOM   4777  N  N     . PHE   B 1  169 ? 16.136  28.501  -3.485  1.00 20.82  ? 169 PHE   C N     1 
ATOM   4778  C  CA    . PHE   B 1  169 ? 14.795  27.980  -3.771  1.00 15.08  ? 169 PHE   C CA    1 
ATOM   4779  C  C     . PHE   B 1  169 ? 15.027  26.646  -4.468  1.00 25.77  ? 169 PHE   C C     1 
ATOM   4780  O  O     . PHE   B 1  169 ? 15.265  26.618  -5.682  1.00 33.18  ? 169 PHE   C O     1 
ATOM   4781  C  CB    . PHE   B 1  169 ? 13.995  28.922  -4.662  1.00 11.97  ? 169 PHE   C CB    1 
ATOM   4782  C  CG    . PHE   B 1  169 ? 13.331  30.066  -3.936  1.00 21.53  ? 169 PHE   C CG    1 
ATOM   4783  C  CD1   . PHE   B 1  169 ? 12.103  29.895  -3.305  1.00 24.19  ? 169 PHE   C CD1   1 
ATOM   4784  C  CD2   . PHE   B 1  169 ? 13.924  31.327  -3.893  1.00 19.10  ? 169 PHE   C CD2   1 
ATOM   4785  C  CE1   . PHE   B 1  169 ? 11.495  30.959  -2.626  1.00 23.52  ? 169 PHE   C CE1   1 
ATOM   4786  C  CE2   . PHE   B 1  169 ? 13.315  32.391  -3.221  1.00 15.24  ? 169 PHE   C CE2   1 
ATOM   4787  C  CZ    . PHE   B 1  169 ? 12.106  32.206  -2.601  1.00 17.63  ? 169 PHE   C CZ    1 
ATOM   4788  N  N     . SER   B 1  170 ? 14.991  25.539  -3.721  1.00 22.26  ? 170 SER   C N     1 
ATOM   4789  C  CA    . SER   B 1  170 ? 15.325  24.227  -4.272  1.00 19.55  ? 170 SER   C CA    1 
ATOM   4790  C  C     . SER   B 1  170 ? 14.061  23.415  -4.542  1.00 23.52  ? 170 SER   C C     1 
ATOM   4791  O  O     . SER   B 1  170 ? 13.209  23.274  -3.658  1.00 26.99  ? 170 SER   C O     1 
ATOM   4792  C  CB    . SER   B 1  170 ? 16.235  23.452  -3.322  1.00 19.48  ? 170 SER   C CB    1 
ATOM   4793  O  OG    . SER   B 1  170 ? 16.888  24.314  -2.407  1.00 27.12  ? 170 SER   C OG    1 
ATOM   4794  N  N     . ILE   B 1  171 ? 13.955  22.854  -5.747  1.00 22.88  ? 171 ILE   C N     1 
ATOM   4795  C  CA    . ILE   B 1  171 ? 12.843  21.976  -6.097  1.00 18.38  ? 171 ILE   C CA    1 
ATOM   4796  C  C     . ILE   B 1  171 ? 13.196  20.541  -5.755  1.00 23.46  ? 171 ILE   C C     1 
ATOM   4797  O  O     . ILE   B 1  171 ? 14.118  19.960  -6.337  1.00 34.37  ? 171 ILE   C O     1 
ATOM   4798  C  CB    . ILE   B 1  171 ? 12.483  22.089  -7.574  1.00 14.82  ? 171 ILE   C CB    1 
ATOM   4799  C  CG1   . ILE   B 1  171 ? 12.328  23.553  -7.948  1.00 19.87  ? 171 ILE   C CG1   1 
ATOM   4800  C  CG2   . ILE   B 1  171 ? 11.232  21.319  -7.795  1.00 18.97  ? 171 ILE   C CG2   1 
ATOM   4801  C  CD1   . ILE   B 1  171 ? 11.432  24.324  -6.995  1.00 22.66  ? 171 ILE   C CD1   1 
ATOM   4802  N  N     . TYR   B 1  172 ? 12.438  19.960  -4.851  1.00 21.08  ? 172 TYR   C N     1 
ATOM   4803  C  CA    . TYR   B 1  172 ? 12.512  18.655  -4.207  1.00 23.33  ? 172 TYR   C CA    1 
ATOM   4804  C  C     . TYR   B 1  172 ? 11.698  17.629  -4.999  1.00 22.53  ? 172 TYR   C C     1 
ATOM   4805  O  O     . TYR   B 1  172 ? 10.602  17.949  -5.484  1.00 23.50  ? 172 TYR   C O     1 
ATOM   4806  C  CB    . TYR   B 1  172 ? 11.983  18.774  -2.778  1.00 22.20  ? 172 TYR   C CB    1 
ATOM   4807  C  CG    . TYR   B 1  172 ? 11.909  17.526  -1.938  1.00 19.38  ? 172 TYR   C CG    1 
ATOM   4808  C  CD1   . TYR   B 1  172 ? 10.835  16.652  -2.047  1.00 17.89  ? 172 TYR   C CD1   1 
ATOM   4809  C  CD2   . TYR   B 1  172 ? 12.890  17.248  -0.998  1.00 19.56  ? 172 TYR   C CD2   1 
ATOM   4810  C  CE1   . TYR   B 1  172 ? 10.757  15.531  -1.250  1.00 18.22  ? 172 TYR   C CE1   1 
ATOM   4811  C  CE2   . TYR   B 1  172 ? 12.814  16.130  -0.203  1.00 19.71  ? 172 TYR   C CE2   1 
ATOM   4812  C  CZ    . TYR   B 1  172 ? 11.747  15.282  -0.327  1.00 15.90  ? 172 TYR   C CZ    1 
ATOM   4813  O  OH    . TYR   B 1  172 ? 11.683  14.177  0.476   1.00 18.21  ? 172 TYR   C OH    1 
ATOM   4814  N  N     . PRO   B 1  173 ? 12.208  16.400  -5.136  1.00 18.04  ? 173 PRO   C N     1 
ATOM   4815  C  CA    . PRO   B 1  173 ? 11.668  15.486  -6.154  1.00 16.13  ? 173 PRO   C CA    1 
ATOM   4816  C  C     . PRO   B 1  173 ? 10.305  14.925  -5.789  1.00 16.46  ? 173 PRO   C C     1 
ATOM   4817  O  O     . PRO   B 1  173 ? 10.003  14.658  -4.629  1.00 21.70  ? 173 PRO   C O     1 
ATOM   4818  C  CB    . PRO   B 1  173 ? 12.726  14.381  -6.237  1.00 21.66  ? 173 PRO   C CB    1 
ATOM   4819  C  CG    . PRO   B 1  173 ? 13.950  14.915  -5.529  1.00 21.55  ? 173 PRO   C CG    1 
ATOM   4820  C  CD    . PRO   B 1  173 ? 13.424  15.868  -4.499  1.00 28.11  ? 173 PRO   C CD    1 
ATOM   4821  N  N     . ALA   B 1  174 ? 9.471   14.772  -6.801  1.00 23.08  ? 174 ALA   C N     1 
ATOM   4822  C  CA    . ALA   B 1  174 ? 8.171   14.140  -6.675  1.00 23.65  ? 174 ALA   C CA    1 
ATOM   4823  C  C     . ALA   B 1  174 ? 8.017   13.170  -7.840  1.00 28.85  ? 174 ALA   C C     1 
ATOM   4824  O  O     . ALA   B 1  174 ? 8.244   13.553  -9.010  1.00 29.11  ? 174 ALA   C O     1 
ATOM   4825  C  CB    . ALA   B 1  174 ? 7.041   15.170  -6.679  1.00 19.18  ? 174 ALA   C CB    1 
ATOM   4826  N  N     . PRO   B 1  175 ? 7.639   11.918  -7.582  1.00 25.60  ? 175 PRO   C N     1 
ATOM   4827  C  CA    . PRO   B 1  175 ? 7.670   10.913  -8.653  1.00 26.12  ? 175 PRO   C CA    1 
ATOM   4828  C  C     . PRO   B 1  175 ? 6.604   11.140  -9.713  1.00 29.16  ? 175 PRO   C C     1 
ATOM   4829  O  O     . PRO   B 1  175 ? 6.699   10.558  -10.798 1.00 27.48  ? 175 PRO   C O     1 
ATOM   4830  C  CB    . PRO   B 1  175 ? 7.436   9.610   -7.893  1.00 18.67  ? 175 PRO   C CB    1 
ATOM   4831  C  CG    . PRO   B 1  175 ? 6.441   10.036  -6.856  1.00 26.42  ? 175 PRO   C CG    1 
ATOM   4832  C  CD    . PRO   B 1  175 ? 6.812   11.467  -6.451  1.00 24.40  ? 175 PRO   C CD    1 
ATOM   4833  N  N     . GLN   B 1  176 ? 5.596   11.976  -9.427  1.00 34.85  ? 176 GLN   C N     1 
ATOM   4834  C  CA    . GLN   B 1  176 ? 4.570   12.310  -10.410 1.00 30.38  ? 176 GLN   C CA    1 
ATOM   4835  C  C     . GLN   B 1  176 ? 5.138   13.028  -11.625 1.00 25.50  ? 176 GLN   C C     1 
ATOM   4836  O  O     . GLN   B 1  176 ? 4.572   12.913  -12.714 1.00 30.95  ? 176 GLN   C O     1 
ATOM   4837  C  CB    . GLN   B 1  176 ? 3.492   13.191  -9.785  1.00 26.06  ? 176 GLN   C CB    1 
ATOM   4838  C  CG    . GLN   B 1  176 ? 2.582   12.491  -8.833  1.00 25.27  ? 176 GLN   C CG    1 
ATOM   4839  C  CD    . GLN   B 1  176 ? 3.027   12.586  -7.395  1.00 27.74  ? 176 GLN   C CD    1 
ATOM   4840  O  OE1   . GLN   B 1  176 ? 4.206   12.786  -7.101  1.00 26.43  ? 176 GLN   C OE1   1 
ATOM   4841  N  NE2   . GLN   B 1  176 ? 2.069   12.443  -6.478  1.00 33.31  ? 176 GLN   C NE2   1 
ATOM   4842  N  N     . VAL   B 1  177 ? 6.212   13.808  -11.461 1.00 35.16  ? 177 VAL   C N     1 
ATOM   4843  C  CA    . VAL   B 1  177 ? 6.739   14.635  -12.548 1.00 31.78  ? 177 VAL   C CA    1 
ATOM   4844  C  C     . VAL   B 1  177 ? 8.255   14.547  -12.606 1.00 25.61  ? 177 VAL   C C     1 
ATOM   4845  O  O     . VAL   B 1  177 ? 8.921   15.540  -12.917 1.00 44.41  ? 177 VAL   C O     1 
ATOM   4846  C  CB    . VAL   B 1  177 ? 6.313   16.115  -12.401 1.00 31.18  ? 177 VAL   C CB    1 
ATOM   4847  C  CG1   . VAL   B 1  177 ? 4.816   16.286  -12.554 1.00 35.73  ? 177 VAL   C CG1   1 
ATOM   4848  C  CG2   . VAL   B 1  177 ? 6.761   16.662  -11.063 1.00 28.30  ? 177 VAL   C CG2   1 
ATOM   4849  N  N     . SER   B 1  178 ? 8.823   13.390  -12.295 1.00 22.20  ? 178 SER   C N     1 
ATOM   4850  C  CA    . SER   B 1  178 ? 10.274  13.255  -12.178 1.00 32.44  ? 178 SER   C CA    1 
ATOM   4851  C  C     . SER   B 1  178 ? 10.853  12.358  -13.269 1.00 36.00  ? 178 SER   C C     1 
ATOM   4852  O  O     . SER   B 1  178 ? 10.253  11.343  -13.648 1.00 39.96  ? 178 SER   C O     1 
ATOM   4853  C  CB    . SER   B 1  178 ? 10.665  12.711  -10.802 1.00 33.22  ? 178 SER   C CB    1 
ATOM   4854  O  OG    . SER   B 1  178 ? 10.225  11.382  -10.668 1.00 33.08  ? 178 SER   C OG    1 
ATOM   4855  N  N     . THR   B 1  179 ? 12.048  12.718  -13.747 1.00 33.66  ? 179 THR   C N     1 
ATOM   4856  C  CA    . THR   B 1  179 ? 12.539  12.226  -15.033 1.00 30.12  ? 179 THR   C CA    1 
ATOM   4857  C  C     . THR   B 1  179 ? 13.811  11.396  -14.910 1.00 30.73  ? 179 THR   C C     1 
ATOM   4858  O  O     . THR   B 1  179 ? 14.498  11.189  -15.920 1.00 39.67  ? 179 THR   C O     1 
ATOM   4859  C  CB    . THR   B 1  179 ? 12.769  13.392  -16.013 1.00 35.25  ? 179 THR   C CB    1 
ATOM   4860  O  OG1   . THR   B 1  179 ? 13.648  14.382  -15.434 1.00 28.05  ? 179 THR   C OG1   1 
ATOM   4861  C  CG2   . THR   B 1  179 ? 11.421  14.047  -16.419 1.00 33.14  ? 179 THR   C CG2   1 
ATOM   4862  N  N     . ALA   B 1  180 ? 14.125  10.894  -13.708 1.00 28.03  ? 180 ALA   C N     1 
ATOM   4863  C  CA    . ALA   B 1  180 ? 15.400  10.229  -13.461 1.00 19.60  ? 180 ALA   C CA    1 
ATOM   4864  C  C     . ALA   B 1  180 ? 15.418  9.472   -12.137 1.00 23.36  ? 180 ALA   C C     1 
ATOM   4865  O  O     . ALA   B 1  180 ? 15.071  10.023  -11.089 1.00 22.06  ? 180 ALA   C O     1 
ATOM   4866  C  CB    . ALA   B 1  180 ? 16.544  11.248  -13.490 1.00 25.02  ? 180 ALA   C CB    1 
ATOM   4867  N  N     . VAL   B 1  181 ? 15.842  8.206   -12.175 1.00 26.34  ? 181 VAL   C N     1 
ATOM   4868  C  CA    . VAL   B 1  181 ? 15.755  7.346   -11.002 1.00 22.90  ? 181 VAL   C CA    1 
ATOM   4869  C  C     . VAL   B 1  181 ? 16.785  7.714   -9.950  1.00 23.27  ? 181 VAL   C C     1 
ATOM   4870  O  O     . VAL   B 1  181 ? 16.620  7.368   -8.773  1.00 29.50  ? 181 VAL   C O     1 
ATOM   4871  C  CB    . VAL   B 1  181 ? 15.895  5.888   -11.458 1.00 22.41  ? 181 VAL   C CB    1 
ATOM   4872  C  CG1   . VAL   B 1  181 ? 15.843  4.935   -10.272 1.00 22.38  ? 181 VAL   C CG1   1 
ATOM   4873  C  CG2   . VAL   B 1  181 ? 14.783  5.579   -12.431 1.00 25.33  ? 181 VAL   C CG2   1 
ATOM   4874  N  N     . VAL   B 1  182 ? 17.834  8.419   -10.347 1.00 22.95  ? 182 VAL   C N     1 
ATOM   4875  C  CA    . VAL   B 1  182 ? 18.909  8.800   -9.446  1.00 21.29  ? 182 VAL   C CA    1 
ATOM   4876  C  C     . VAL   B 1  182 ? 18.651  10.178  -8.828  1.00 23.58  ? 182 VAL   C C     1 
ATOM   4877  O  O     . VAL   B 1  182 ? 19.564  10.783  -8.274  1.00 28.97  ? 182 VAL   C O     1 
ATOM   4878  C  CB    . VAL   B 1  182 ? 20.291  8.735   -10.138 1.00 23.50  ? 182 VAL   C CB    1 
ATOM   4879  C  CG1   . VAL   B 1  182 ? 20.606  7.308   -10.567 1.00 22.09  ? 182 VAL   C CG1   1 
ATOM   4880  C  CG2   . VAL   B 1  182 ? 20.356  9.640   -11.342 1.00 20.77  ? 182 VAL   C CG2   1 
ATOM   4881  N  N     . GLU   B 1  183 ? 17.417  10.684  -8.900  1.00 24.85  ? 183 GLU   C N     1 
ATOM   4882  C  CA    . GLU   B 1  183 ? 17.101  11.941  -8.221  1.00 21.41  ? 183 GLU   C CA    1 
ATOM   4883  C  C     . GLU   B 1  183 ? 17.473  11.889  -6.730  1.00 25.27  ? 183 GLU   C C     1 
ATOM   4884  O  O     . GLU   B 1  183 ? 18.031  12.882  -6.222  1.00 27.57  ? 183 GLU   C O     1 
ATOM   4885  C  CB    . GLU   B 1  183 ? 15.619  12.314  -8.461  1.00 19.85  ? 183 GLU   C CB    1 
ATOM   4886  C  CG    . GLU   B 1  183 ? 15.403  13.606  -9.320  1.00 21.95  ? 183 GLU   C CG    1 
ATOM   4887  C  CD    . GLU   B 1  183 ? 14.073  13.651  -10.124 1.00 29.92  ? 183 GLU   C CD    1 
ATOM   4888  O  OE1   . GLU   B 1  183 ? 13.633  14.753  -10.537 1.00 30.81  ? 183 GLU   C OE1   1 
ATOM   4889  O  OE2   . GLU   B 1  183 ? 13.457  12.595  -10.363 1.00 38.27  ? 183 GLU   C OE2   1 
ATOM   4890  N  N     . PRO   B 1  184 ? 17.276  10.774  -6.003  1.00 24.78  ? 184 PRO   C N     1 
ATOM   4891  C  CA    . PRO   B 1  184 ? 17.809  10.712  -4.626  1.00 21.77  ? 184 PRO   C CA    1 
ATOM   4892  C  C     . PRO   B 1  184 ? 19.291  11.011  -4.512  1.00 25.64  ? 184 PRO   C C     1 
ATOM   4893  O  O     . PRO   B 1  184 ? 19.686  11.685  -3.554  1.00 24.95  ? 184 PRO   C O     1 
ATOM   4894  C  CB    . PRO   B 1  184 ? 17.508  9.278   -4.195  1.00 15.16  ? 184 PRO   C CB    1 
ATOM   4895  C  CG    . PRO   B 1  184 ? 16.376  8.877   -5.043  1.00 27.55  ? 184 PRO   C CG    1 
ATOM   4896  C  CD    . PRO   B 1  184 ? 16.569  9.533   -6.365  1.00 18.55  ? 184 PRO   C CD    1 
ATOM   4897  N  N     . TYR   B 1  185 ? 20.134  10.515  -5.431  1.00 22.95  ? 185 TYR   C N     1 
ATOM   4898  C  CA    . TYR   B 1  185 ? 21.574  10.750  -5.295  1.00 28.09  ? 185 TYR   C CA    1 
ATOM   4899  C  C     . TYR   B 1  185 ? 21.897  12.222  -5.488  1.00 25.21  ? 185 TYR   C C     1 
ATOM   4900  O  O     . TYR   B 1  185 ? 22.653  12.818  -4.709  1.00 23.26  ? 185 TYR   C O     1 
ATOM   4901  C  CB    . TYR   B 1  185 ? 22.392  9.926   -6.299  1.00 30.83  ? 185 TYR   C CB    1 
ATOM   4902  C  CG    . TYR   B 1  185 ? 22.480  8.426   -6.065  1.00 29.10  ? 185 TYR   C CG    1 
ATOM   4903  C  CD1   . TYR   B 1  185 ? 22.151  7.853   -4.838  1.00 22.82  ? 185 TYR   C CD1   1 
ATOM   4904  C  CD2   . TYR   B 1  185 ? 22.884  7.584   -7.093  1.00 23.85  ? 185 TYR   C CD2   1 
ATOM   4905  C  CE1   . TYR   B 1  185 ? 22.227  6.473   -4.652  1.00 26.07  ? 185 TYR   C CE1   1 
ATOM   4906  C  CE2   . TYR   B 1  185 ? 22.959  6.221   -6.920  1.00 25.97  ? 185 TYR   C CE2   1 
ATOM   4907  C  CZ    . TYR   B 1  185 ? 22.636  5.660   -5.705  1.00 31.41  ? 185 TYR   C CZ    1 
ATOM   4908  O  OH    . TYR   B 1  185 ? 22.727  4.288   -5.568  1.00 29.87  ? 185 TYR   C OH    1 
ATOM   4909  N  N     . ASN   B 1  186 ? 21.362  12.821  -6.544  1.00 22.35  ? 186 ASN   C N     1 
ATOM   4910  C  CA    . ASN   B 1  186 ? 21.692  14.211  -6.811  1.00 21.77  ? 186 ASN   C CA    1 
ATOM   4911  C  C     . ASN   B 1  186 ? 21.200  15.093  -5.681  1.00 24.96  ? 186 ASN   C C     1 
ATOM   4912  O  O     . ASN   B 1  186 ? 21.889  16.031  -5.269  1.00 30.58  ? 186 ASN   C O     1 
ATOM   4913  C  CB    . ASN   B 1  186 ? 21.088  14.653  -8.139  1.00 22.81  ? 186 ASN   C CB    1 
ATOM   4914  C  CG    . ASN   B 1  186 ? 21.496  13.763  -9.291  1.00 19.98  ? 186 ASN   C CG    1 
ATOM   4915  O  OD1   . ASN   B 1  186 ? 22.542  13.130  -9.258  1.00 22.95  ? 186 ASN   C OD1   1 
ATOM   4916  N  ND2   . ASN   B 1  186 ? 20.666  13.714  -10.321 1.00 21.47  ? 186 ASN   C ND2   1 
ATOM   4917  N  N     . SER   B 1  187 ? 20.003  14.807  -5.169  1.00 30.25  ? 187 SER   C N     1 
ATOM   4918  C  CA    . SER   B 1  187 ? 19.485  15.526  -4.008  1.00 21.67  ? 187 SER   C CA    1 
ATOM   4919  C  C     . SER   B 1  187 ? 20.478  15.499  -2.857  1.00 23.19  ? 187 SER   C C     1 
ATOM   4920  O  O     . SER   B 1  187 ? 20.833  16.554  -2.314  1.00 25.39  ? 187 SER   C O     1 
ATOM   4921  C  CB    . SER   B 1  187 ? 18.159  14.920  -3.567  1.00 20.62  ? 187 SER   C CB    1 
ATOM   4922  O  OG    . SER   B 1  187 ? 17.219  15.009  -4.609  1.00 31.59  ? 187 SER   C OG    1 
ATOM   4923  N  N     . ILE   B 1  188 ? 20.930  14.299  -2.463  1.00 19.64  ? 188 ILE   C N     1 
ATOM   4924  C  CA    . ILE   B 1  188 ? 21.741  14.174  -1.256  1.00 15.51  ? 188 ILE   C CA    1 
ATOM   4925  C  C     . ILE   B 1  188 ? 23.143  14.684  -1.511  1.00 18.47  ? 188 ILE   C C     1 
ATOM   4926  O  O     . ILE   B 1  188 ? 23.775  15.250  -0.609  1.00 20.06  ? 188 ILE   C O     1 
ATOM   4927  C  CB    . ILE   B 1  188 ? 21.749  12.726  -0.731  1.00 18.65  ? 188 ILE   C CB    1 
ATOM   4928  C  CG1   . ILE   B 1  188 ? 20.522  12.442  0.128   1.00 18.20  ? 188 ILE   C CG1   1 
ATOM   4929  C  CG2   . ILE   B 1  188 ? 22.955  12.480  0.119   1.00 22.69  ? 188 ILE   C CG2   1 
ATOM   4930  C  CD1   . ILE   B 1  188 ? 19.190  12.533  -0.609  1.00 21.84  ? 188 ILE   C CD1   1 
ATOM   4931  N  N     . LEU   B 1  189 ? 23.654  14.534  -2.736  1.00 21.85  ? 189 LEU   C N     1 
ATOM   4932  C  CA    . LEU   B 1  189 ? 24.957  15.115  -3.039  1.00 17.26  ? 189 LEU   C CA    1 
ATOM   4933  C  C     . LEU   B 1  189 ? 24.902  16.633  -2.941  1.00 18.97  ? 189 LEU   C C     1 
ATOM   4934  O  O     . LEU   B 1  189 ? 25.653  17.237  -2.173  1.00 25.83  ? 189 LEU   C O     1 
ATOM   4935  C  CB    . LEU   B 1  189 ? 25.447  14.664  -4.412  1.00 21.53  ? 189 LEU   C CB    1 
ATOM   4936  C  CG    . LEU   B 1  189 ? 25.866  13.193  -4.525  1.00 19.56  ? 189 LEU   C CG    1 
ATOM   4937  C  CD1   . LEU   B 1  189 ? 26.274  12.919  -5.931  1.00 21.34  ? 189 LEU   C CD1   1 
ATOM   4938  C  CD2   . LEU   B 1  189 ? 27.008  12.856  -3.608  1.00 19.72  ? 189 LEU   C CD2   1 
ATOM   4939  N  N     . THR   B 1  190 ? 23.977  17.267  -3.659  1.00 16.46  ? 190 THR   C N     1 
ATOM   4940  C  CA    . THR   B 1  190 ? 23.928  18.732  -3.677  1.00 20.33  ? 190 THR   C CA    1 
ATOM   4941  C  C     . THR   B 1  190 ? 23.628  19.318  -2.296  1.00 17.89  ? 190 THR   C C     1 
ATOM   4942  O  O     . THR   B 1  190 ? 24.281  20.268  -1.862  1.00 17.37  ? 190 THR   C O     1 
ATOM   4943  C  CB    . THR   B 1  190 ? 22.898  19.211  -4.697  1.00 22.33  ? 190 THR   C CB    1 
ATOM   4944  O  OG1   . THR   B 1  190 ? 22.966  20.631  -4.787  1.00 23.48  ? 190 THR   C OG1   1 
ATOM   4945  C  CG2   . THR   B 1  190 ? 21.472  18.794  -4.279  1.00 19.16  ? 190 THR   C CG2   1 
ATOM   4946  N  N     . THR   B 1  191 ? 22.631  18.778  -1.592  1.00 25.39  ? 191 THR   C N     1 
ATOM   4947  C  CA    . THR   B 1  191 ? 22.327  19.260  -0.247  1.00 22.38  ? 191 THR   C CA    1 
ATOM   4948  C  C     . THR   B 1  191 ? 23.553  19.200  0.658   1.00 23.10  ? 191 THR   C C     1 
ATOM   4949  O  O     . THR   B 1  191 ? 23.795  20.125  1.444   1.00 27.27  ? 191 THR   C O     1 
ATOM   4950  C  CB    . THR   B 1  191 ? 21.176  18.451  0.359   1.00 23.14  ? 191 THR   C CB    1 
ATOM   4951  O  OG1   . THR   B 1  191 ? 19.914  18.939  -0.136  1.00 27.47  ? 191 THR   C OG1   1 
ATOM   4952  C  CG2   . THR   B 1  191 ? 21.218  18.525  1.895   1.00 17.68  ? 191 THR   C CG2   1 
ATOM   4953  N  N     . HIS   B 1  192 ? 24.334  18.115  0.568   1.00 19.60  ? 192 HIS   C N     1 
ATOM   4954  C  CA    . HIS   B 1  192 ? 25.564  17.998  1.351   1.00 19.48  ? 192 HIS   C CA    1 
ATOM   4955  C  C     . HIS   B 1  192 ? 26.587  19.050  0.951   1.00 21.69  ? 192 HIS   C C     1 
ATOM   4956  O  O     . HIS   B 1  192 ? 27.149  19.752  1.796   1.00 26.92  ? 192 HIS   C O     1 
ATOM   4957  C  CB    . HIS   B 1  192 ? 26.176  16.621  1.164   1.00 21.02  ? 192 HIS   C CB    1 
ATOM   4958  C  CG    . HIS   B 1  192 ? 27.610  16.544  1.593   1.00 26.94  ? 192 HIS   C CG    1 
ATOM   4959  N  ND1   . HIS   B 1  192 ? 28.037  16.956  2.840   1.00 23.15  ? 192 HIS   C ND1   1 
ATOM   4960  C  CD2   . HIS   B 1  192 ? 28.714  16.088  0.948   1.00 25.65  ? 192 HIS   C CD2   1 
ATOM   4961  C  CE1   . HIS   B 1  192 ? 29.338  16.738  2.947   1.00 26.63  ? 192 HIS   C CE1   1 
ATOM   4962  N  NE2   . HIS   B 1  192 ? 29.774  16.211  1.815   1.00 24.08  ? 192 HIS   C NE2   1 
ATOM   4963  N  N     . THR   B 1  193 ? 26.875  19.136  -0.339  1.00 22.38  ? 193 THR   C N     1 
ATOM   4964  C  CA    . THR   B 1  193 ? 27.891  20.020  -0.875  1.00 21.27  ? 193 THR   C CA    1 
ATOM   4965  C  C     . THR   B 1  193 ? 27.517  21.489  -0.786  1.00 19.97  ? 193 THR   C C     1 
ATOM   4966  O  O     . THR   B 1  193 ? 28.404  22.346  -0.850  1.00 20.26  ? 193 THR   C O     1 
ATOM   4967  C  CB    . THR   B 1  193 ? 28.158  19.620  -2.320  1.00 28.99  ? 193 THR   C CB    1 
ATOM   4968  O  OG1   . THR   B 1  193 ? 29.031  18.474  -2.342  1.00 29.10  ? 193 THR   C OG1   1 
ATOM   4969  C  CG2   . THR   B 1  193 ? 28.747  20.778  -3.102  1.00 30.46  ? 193 THR   C CG2   1 
ATOM   4970  N  N     . THR   B 1  194 ? 26.249  21.802  -0.586  1.00 18.77  ? 194 THR   C N     1 
ATOM   4971  C  CA    A THR   B 1  194 ? 25.798  23.178  -0.493  1.00 19.29  ? 194 THR   C CA    1 
ATOM   4972  C  CA    B THR   B 1  194 ? 25.807  23.183  -0.492  0.00 19.55  ? 194 THR   C CA    1 
ATOM   4973  C  C     . THR   B 1  194 ? 25.517  23.629  0.934   1.00 20.97  ? 194 THR   C C     1 
ATOM   4974  O  O     . THR   B 1  194 ? 25.329  24.833  1.162   1.00 22.91  ? 194 THR   C O     1 
ATOM   4975  C  CB    A THR   B 1  194 ? 24.547  23.357  -1.374  1.00 16.23  ? 194 THR   C CB    1 
ATOM   4976  C  CB    B THR   B 1  194 ? 24.551  23.400  -1.353  0.00 16.37  ? 194 THR   C CB    1 
ATOM   4977  O  OG1   A THR   B 1  194 ? 24.955  23.517  -2.737  1.00 20.74  ? 194 THR   C OG1   1 
ATOM   4978  O  OG1   B THR   B 1  194 ? 24.805  22.943  -2.687  0.00 20.91  ? 194 THR   C OG1   1 
ATOM   4979  C  CG2   A THR   B 1  194 ? 23.687  24.519  -0.964  1.00 15.34  ? 194 THR   C CG2   1 
ATOM   4980  C  CG2   B THR   B 1  194 ? 24.173  24.874  -1.392  0.00 18.49  ? 194 THR   C CG2   1 
ATOM   4981  N  N     . LEU   B 1  195 ? 25.506  22.712  1.903   1.00 21.21  ? 195 LEU   C N     1 
ATOM   4982  C  CA    . LEU   B 1  195 ? 24.970  23.066  3.214   1.00 17.77  ? 195 LEU   C CA    1 
ATOM   4983  C  C     . LEU   B 1  195 ? 25.650  24.305  3.773   1.00 17.89  ? 195 LEU   C C     1 
ATOM   4984  O  O     . LEU   B 1  195 ? 24.973  25.243  4.195   1.00 28.04  ? 195 LEU   C O     1 
ATOM   4985  C  CB    . LEU   B 1  195 ? 25.064  21.886  4.184   1.00 13.34  ? 195 LEU   C CB    1 
ATOM   4986  C  CG    . LEU   B 1  195 ? 24.026  21.907  5.311   1.00 10.09  ? 195 LEU   C CG    1 
ATOM   4987  C  CD1   . LEU   B 1  195 ? 22.656  22.196  4.775   1.00 12.85  ? 195 LEU   C CD1   1 
ATOM   4988  C  CD2   . LEU   B 1  195 ? 24.011  20.605  6.065   1.00 13.35  ? 195 LEU   C CD2   1 
ATOM   4989  N  N     . GLU   B 1  196 ? 26.980  24.360  3.739   1.00 21.96  ? 196 GLU   C N     1 
ATOM   4990  C  CA    . GLU   B 1  196 ? 27.686  25.452  4.402   1.00 18.53  ? 196 GLU   C CA    1 
ATOM   4991  C  C     . GLU   B 1  196 ? 27.821  26.678  3.536   1.00 17.24  ? 196 GLU   C C     1 
ATOM   4992  O  O     . GLU   B 1  196 ? 28.369  27.682  3.997   1.00 21.47  ? 196 GLU   C O     1 
ATOM   4993  C  CB    . GLU   B 1  196 ? 29.075  25.017  4.887   1.00 25.28  ? 196 GLU   C CB    1 
ATOM   4994  C  CG    . GLU   B 1  196 ? 30.085  24.734  3.799   1.00 28.67  ? 196 GLU   C CG    1 
ATOM   4995  C  CD    . GLU   B 1  196 ? 31.351  24.090  4.350   1.00 43.24  ? 196 GLU   C CD    1 
ATOM   4996  O  OE1   . GLU   B 1  196 ? 31.747  24.425  5.488   1.00 48.81  ? 196 GLU   C OE1   1 
ATOM   4997  O  OE2   . GLU   B 1  196 ? 31.941  23.236  3.651   1.00 56.75  ? 196 GLU   C OE2   1 
ATOM   4998  N  N     . HIS   B 1  197 ? 27.328  26.632  2.314   1.00 16.64  ? 197 HIS   C N     1 
ATOM   4999  C  CA    . HIS   B 1  197 ? 27.347  27.799  1.467   1.00 14.84  ? 197 HIS   C CA    1 
ATOM   5000  C  C     . HIS   B 1  197 ? 25.993  28.469  1.367   1.00 17.89  ? 197 HIS   C C     1 
ATOM   5001  O  O     . HIS   B 1  197 ? 25.893  29.533  0.753   1.00 29.10  ? 197 HIS   C O     1 
ATOM   5002  C  CB    . HIS   B 1  197 ? 27.869  27.425  0.070   1.00 19.45  ? 197 HIS   C CB    1 
ATOM   5003  C  CG    . HIS   B 1  197 ? 29.246  26.844  0.092   1.00 21.36  ? 197 HIS   C CG    1 
ATOM   5004  N  ND1   . HIS   B 1  197 ? 30.363  27.590  0.406   1.00 22.82  ? 197 HIS   C ND1   1 
ATOM   5005  C  CD2   . HIS   B 1  197 ? 29.680  25.580  -0.110  1.00 20.34  ? 197 HIS   C CD2   1 
ATOM   5006  C  CE1   . HIS   B 1  197 ? 31.428  26.813  0.374   1.00 24.86  ? 197 HIS   C CE1   1 
ATOM   5007  N  NE2   . HIS   B 1  197 ? 31.041  25.589  0.063   1.00 22.77  ? 197 HIS   C NE2   1 
ATOM   5008  N  N     . SER   B 1  198 ? 24.955  27.893  1.949   1.00 19.46  ? 198 SER   C N     1 
ATOM   5009  C  CA    . SER   B 1  198 ? 23.634  28.491  1.906   1.00 19.47  ? 198 SER   C CA    1 
ATOM   5010  C  C     . SER   B 1  198 ? 23.285  29.110  3.255   1.00 20.99  ? 198 SER   C C     1 
ATOM   5011  O  O     . SER   B 1  198 ? 23.663  28.598  4.307   1.00 25.45  ? 198 SER   C O     1 
ATOM   5012  C  CB    . SER   B 1  198 ? 22.587  27.453  1.505   1.00 20.38  ? 198 SER   C CB    1 
ATOM   5013  O  OG    . SER   B 1  198 ? 21.381  28.101  1.119   1.00 21.01  ? 198 SER   C OG    1 
ATOM   5014  N  N     . ASP   B 1  199 ? 22.563  30.221  3.218   1.00 25.31  ? 199 ASP   C N     1 
ATOM   5015  C  CA    . ASP   B 1  199 ? 22.117  30.891  4.433   1.00 25.68  ? 199 ASP   C CA    1 
ATOM   5016  C  C     . ASP   B 1  199 ? 20.678  30.566  4.811   1.00 28.07  ? 199 ASP   C C     1 
ATOM   5017  O  O     . ASP   B 1  199 ? 20.297  30.692  5.987   1.00 26.10  ? 199 ASP   C O     1 
ATOM   5018  C  CB    . ASP   B 1  199 ? 22.261  32.406  4.268   1.00 28.43  ? 199 ASP   C CB    1 
ATOM   5019  C  CG    . ASP   B 1  199 ? 23.676  32.819  4.012   1.00 33.53  ? 199 ASP   C CG    1 
ATOM   5020  O  OD1   . ASP   B 1  199 ? 24.548  32.548  4.871   1.00 50.71  ? 199 ASP   C OD1   1 
ATOM   5021  O  OD2   . ASP   B 1  199 ? 23.926  33.396  2.936   1.00 37.76  ? 199 ASP   C OD2   1 
ATOM   5022  N  N     . CYS   B 1  200 ? 19.885  30.138  3.834   1.00 24.04  ? 200 CYS   C N     1 
ATOM   5023  C  CA    . CYS   B 1  200 ? 18.452  29.978  3.980   1.00 18.84  ? 200 CYS   C CA    1 
ATOM   5024  C  C     . CYS   B 1  200 ? 17.959  29.251  2.738   1.00 23.13  ? 200 CYS   C C     1 
ATOM   5025  O  O     . CYS   B 1  200 ? 18.302  29.640  1.622   1.00 25.59  ? 200 CYS   C O     1 
ATOM   5026  C  CB    . CYS   B 1  200 ? 17.801  31.344  4.138   1.00 20.91  ? 200 CYS   C CB    1 
ATOM   5027  S  SG    . CYS   B 1  200 ? 16.080  31.299  4.544   1.00 28.03  ? 200 CYS   C SG    1 
ATOM   5028  N  N     . ALA   B 1  201 ? 17.193  28.177  2.905   1.00 29.61  ? 201 ALA   C N     1 
ATOM   5029  C  CA    . ALA   B 1  201 ? 16.728  27.368  1.784   1.00 20.90  ? 201 ALA   C CA    1 
ATOM   5030  C  C     . ALA   B 1  201 ? 15.241  27.100  1.934   1.00 25.52  ? 201 ALA   C C     1 
ATOM   5031  O  O     . ALA   B 1  201 ? 14.803  26.502  2.925   1.00 23.53  ? 201 ALA   C O     1 
ATOM   5032  C  CB    . ALA   B 1  201 ? 17.494  26.052  1.699   1.00 20.91  ? 201 ALA   C CB    1 
ATOM   5033  N  N     . PHE   B 1  202 ? 14.468  27.543  0.958   1.00 23.18  ? 202 PHE   C N     1 
ATOM   5034  C  CA    . PHE   B 1  202 ? 13.065  27.190  0.876   1.00 20.33  ? 202 PHE   C CA    1 
ATOM   5035  C  C     . PHE   B 1  202 ? 12.948  26.011  -0.092  1.00 26.21  ? 202 PHE   C C     1 
ATOM   5036  O  O     . PHE   B 1  202 ? 13.119  26.174  -1.308  1.00 23.63  ? 202 PHE   C O     1 
ATOM   5037  C  CB    . PHE   B 1  202 ? 12.224  28.384  0.433   1.00 17.68  ? 202 PHE   C CB    1 
ATOM   5038  C  CG    . PHE   B 1  202 ? 12.538  29.657  1.161   1.00 18.06  ? 202 PHE   C CG    1 
ATOM   5039  C  CD1   . PHE   B 1  202 ? 13.495  30.520  0.682   1.00 17.62  ? 202 PHE   C CD1   1 
ATOM   5040  C  CD2   . PHE   B 1  202 ? 11.858  29.999  2.302   1.00 15.83  ? 202 PHE   C CD2   1 
ATOM   5041  C  CE1   . PHE   B 1  202 ? 13.771  31.685  1.347   1.00 18.39  ? 202 PHE   C CE1   1 
ATOM   5042  C  CE2   . PHE   B 1  202 ? 12.141  31.151  2.970   1.00 17.33  ? 202 PHE   C CE2   1 
ATOM   5043  C  CZ    . PHE   B 1  202 ? 13.098  32.000  2.488   1.00 20.00  ? 202 PHE   C CZ    1 
ATOM   5044  N  N     . MET   B 1  203 ? 12.692  24.821  0.456   1.00 17.42  ? 203 MET   C N     1 
ATOM   5045  C  CA    . MET   B 1  203 ? 12.396  23.663  -0.363  1.00 16.37  ? 203 MET   C CA    1 
ATOM   5046  C  C     . MET   B 1  203 ? 10.951  23.696  -0.842  1.00 15.89  ? 203 MET   C C     1 
ATOM   5047  O  O     . MET   B 1  203 ? 10.043  24.071  -0.101  1.00 18.21  ? 203 MET   C O     1 
ATOM   5048  C  CB    . MET   B 1  203 ? 12.662  22.382  0.428   1.00 19.43  ? 203 MET   C CB    1 
ATOM   5049  C  CG    . MET   B 1  203 ? 14.127  22.152  0.761   1.00 22.21  ? 203 MET   C CG    1 
ATOM   5050  S  SD    . MET   B 1  203 ? 14.424  20.470  1.334   1.00 25.83  ? 203 MET   C SD    1 
ATOM   5051  C  CE    . MET   B 1  203 ? 13.334  20.419  2.748   1.00 22.94  ? 203 MET   C CE    1 
ATOM   5052  N  N     . VAL   B 1  204 ? 10.738  23.279  -2.082  1.00 21.14  ? 204 VAL   C N     1 
ATOM   5053  C  CA    . VAL   B 1  204 ? 9.409   23.188  -2.688  1.00 20.92  ? 204 VAL   C CA    1 
ATOM   5054  C  C     . VAL   B 1  204 ? 9.195   21.745  -3.113  1.00 22.98  ? 204 VAL   C C     1 
ATOM   5055  O  O     . VAL   B 1  204 ? 9.767   21.297  -4.119  1.00 19.95  ? 204 VAL   C O     1 
ATOM   5056  C  CB    . VAL   B 1  204 ? 9.245   24.117  -3.900  1.00 22.25  ? 204 VAL   C CB    1 
ATOM   5057  C  CG1   . VAL   B 1  204 ? 7.785   24.249  -4.258  1.00 19.47  ? 204 VAL   C CG1   1 
ATOM   5058  C  CG2   . VAL   B 1  204 ? 9.876   25.481  -3.659  1.00 24.46  ? 204 VAL   C CG2   1 
ATOM   5059  N  N     . ASP   B 1  205 ? 8.354   21.025  -2.373  1.00 22.15  ? 205 ASP   C N     1 
ATOM   5060  C  CA    . ASP   B 1  205 ? 8.050   19.629  -2.693  1.00 24.46  ? 205 ASP   C CA    1 
ATOM   5061  C  C     . ASP   B 1  205 ? 7.152   19.587  -3.928  1.00 26.39  ? 205 ASP   C C     1 
ATOM   5062  O  O     . ASP   B 1  205 ? 6.005   20.046  -3.890  1.00 27.00  ? 205 ASP   C O     1 
ATOM   5063  C  CB    . ASP   B 1  205 ? 7.394   18.939  -1.489  1.00 22.82  ? 205 ASP   C CB    1 
ATOM   5064  C  CG    . ASP   B 1  205 ? 7.186   17.436  -1.704  1.00 24.94  ? 205 ASP   C CG    1 
ATOM   5065  O  OD1   . ASP   B 1  205 ? 7.338   17.004  -2.870  1.00 25.73  ? 205 ASP   C OD1   1 
ATOM   5066  O  OD2   . ASP   B 1  205 ? 6.898   16.692  -0.718  1.00 19.73  ? 205 ASP   C OD2   1 
ATOM   5067  N  N     . ASN   B 1  206 ? 7.662   19.053  -5.040  1.00 27.43  ? 206 ASN   C N     1 
ATOM   5068  C  CA    . ASN   B 1  206 ? 6.825   19.005  -6.240  1.00 28.18  ? 206 ASN   C CA    1 
ATOM   5069  C  C     . ASN   B 1  206 ? 5.510   18.282  -5.956  1.00 29.93  ? 206 ASN   C C     1 
ATOM   5070  O  O     . ASN   B 1  206 ? 4.445   18.696  -6.437  1.00 32.93  ? 206 ASN   C O     1 
ATOM   5071  C  CB    . ASN   B 1  206 ? 7.577   18.362  -7.409  1.00 18.37  ? 206 ASN   C CB    1 
ATOM   5072  C  CG    . ASN   B 1  206 ? 8.122   19.399  -8.381  1.00 22.69  ? 206 ASN   C CG    1 
ATOM   5073  O  OD1   . ASN   B 1  206 ? 7.890   20.595  -8.204  1.00 23.17  ? 206 ASN   C OD1   1 
ATOM   5074  N  ND2   . ASN   B 1  206 ? 8.861   18.952  -9.402  1.00 22.15  ? 206 ASN   C ND2   1 
ATOM   5075  N  N     . GLU   B 1  207 ? 5.552   17.226  -5.143  1.00 20.97  ? 207 GLU   C N     1 
ATOM   5076  C  CA    . GLU   B 1  207 ? 4.312   16.563  -4.801  1.00 20.98  ? 207 GLU   C CA    1 
ATOM   5077  C  C     . GLU   B 1  207 ? 3.427   17.470  -3.956  1.00 23.79  ? 207 GLU   C C     1 
ATOM   5078  O  O     . GLU   B 1  207 ? 2.209   17.300  -3.956  1.00 24.01  ? 207 GLU   C O     1 
ATOM   5079  C  CB    . GLU   B 1  207 ? 4.617   15.236  -4.099  1.00 21.41  ? 207 GLU   C CB    1 
ATOM   5080  C  CG    . GLU   B 1  207 ? 3.422   14.327  -3.871  1.00 25.25  ? 207 GLU   C CG    1 
ATOM   5081  C  CD    . GLU   B 1  207 ? 3.811   12.992  -3.279  1.00 28.11  ? 207 GLU   C CD    1 
ATOM   5082  O  OE1   . GLU   B 1  207 ? 4.764   12.376  -3.786  1.00 34.67  ? 207 GLU   C OE1   1 
ATOM   5083  O  OE2   . GLU   B 1  207 ? 3.181   12.557  -2.300  1.00 31.12  ? 207 GLU   C OE2   1 
ATOM   5084  N  N     . ALA   B 1  208 ? 3.997   18.454  -3.257  1.00 25.43  ? 208 ALA   C N     1 
ATOM   5085  C  CA    . ALA   B 1  208 ? 3.158   19.343  -2.454  1.00 26.61  ? 208 ALA   C CA    1 
ATOM   5086  C  C     . ALA   B 1  208 ? 2.369   20.283  -3.350  1.00 26.96  ? 208 ALA   C C     1 
ATOM   5087  O  O     . ALA   B 1  208 ? 1.141   20.390  -3.237  1.00 24.30  ? 208 ALA   C O     1 
ATOM   5088  C  CB    . ALA   B 1  208 ? 4.004   20.133  -1.453  1.00 19.27  ? 208 ALA   C CB    1 
ATOM   5089  N  N     . ILE   B 1  209 ? 3.073   20.955  -4.258  1.00 26.79  ? 209 ILE   C N     1 
ATOM   5090  C  CA    . ILE   B 1  209 ? 2.449   21.814  -5.257  1.00 30.10  ? 209 ILE   C CA    1 
ATOM   5091  C  C     . ILE   B 1  209 ? 1.535   21.006  -6.173  1.00 26.77  ? 209 ILE   C C     1 
ATOM   5092  O  O     . ILE   B 1  209 ? 0.465   21.479  -6.576  1.00 27.95  ? 209 ILE   C O     1 
ATOM   5093  C  CB    . ILE   B 1  209 ? 3.543   22.548  -6.054  1.00 31.12  ? 209 ILE   C CB    1 
ATOM   5094  C  CG1   . ILE   B 1  209 ? 3.909   23.859  -5.374  1.00 27.92  ? 209 ILE   C CG1   1 
ATOM   5095  C  CG2   . ILE   B 1  209 ? 3.084   22.797  -7.465  1.00 35.58  ? 209 ILE   C CG2   1 
ATOM   5096  C  CD1   . ILE   B 1  209 ? 4.395   23.726  -3.950  1.00 26.19  ? 209 ILE   C CD1   1 
ATOM   5097  N  N     . TYR   B 1  210 ? 1.948   19.781  -6.517  1.00 23.78  ? 210 TYR   C N     1 
ATOM   5098  C  CA    . TYR   B 1  210 ? 1.138   18.902  -7.356  1.00 25.41  ? 210 TYR   C CA    1 
ATOM   5099  C  C     . TYR   B 1  210 ? -0.230  18.611  -6.731  1.00 25.00  ? 210 TYR   C C     1 
ATOM   5100  O  O     . TYR   B 1  210 ? -1.269  18.926  -7.312  1.00 31.63  ? 210 TYR   C O     1 
ATOM   5101  C  CB    . TYR   B 1  210 ? 1.904   17.613  -7.614  1.00 25.74  ? 210 TYR   C CB    1 
ATOM   5102  C  CG    . TYR   B 1  210 ? 1.402   16.872  -8.809  1.00 28.97  ? 210 TYR   C CG    1 
ATOM   5103  C  CD1   . TYR   B 1  210 ? 1.764   17.270  -10.102 1.00 34.73  ? 210 TYR   C CD1   1 
ATOM   5104  C  CD2   . TYR   B 1  210 ? 0.571   15.768  -8.665  1.00 33.17  ? 210 TYR   C CD2   1 
ATOM   5105  C  CE1   . TYR   B 1  210 ? 1.299   16.590  -11.226 1.00 35.47  ? 210 TYR   C CE1   1 
ATOM   5106  C  CE2   . TYR   B 1  210 ? 0.099   15.080  -9.780  1.00 40.27  ? 210 TYR   C CE2   1 
ATOM   5107  C  CZ    . TYR   B 1  210 ? 0.458   15.502  -11.054 1.00 39.22  ? 210 TYR   C CZ    1 
ATOM   5108  O  OH    . TYR   B 1  210 ? -0.009  14.821  -12.147 1.00 38.97  ? 210 TYR   C OH    1 
ATOM   5109  N  N     . ASP   B 1  211 ? -0.258  17.996  -5.549  1.00 28.71  ? 211 ASP   C N     1 
ATOM   5110  C  CA    . ASP   B 1  211 ? -1.534  17.759  -4.877  1.00 25.44  ? 211 ASP   C CA    1 
ATOM   5111  C  C     . ASP   B 1  211 ? -2.349  19.041  -4.741  1.00 30.66  ? 211 ASP   C C     1 
ATOM   5112  O  O     . ASP   B 1  211 ? -3.543  19.053  -5.060  1.00 38.55  ? 211 ASP   C O     1 
ATOM   5113  C  CB    . ASP   B 1  211 ? -1.314  17.145  -3.501  1.00 29.09  ? 211 ASP   C CB    1 
ATOM   5114  C  CG    . ASP   B 1  211 ? -0.761  15.766  -3.565  1.00 34.89  ? 211 ASP   C CG    1 
ATOM   5115  O  OD1   . ASP   B 1  211 ? -1.005  15.091  -4.587  1.00 40.58  ? 211 ASP   C OD1   1 
ATOM   5116  O  OD2   . ASP   B 1  211 ? -0.086  15.359  -2.590  1.00 32.18  ? 211 ASP   C OD2   1 
ATOM   5117  N  N     . ILE   B 1  212 ? -1.731  20.125  -4.234  1.00 27.60  ? 212 ILE   C N     1 
ATOM   5118  C  CA    . ILE   B 1  212 ? -2.418  21.424  -4.120  1.00 27.91  ? 212 ILE   C CA    1 
ATOM   5119  C  C     . ILE   B 1  212 ? -3.130  21.790  -5.417  1.00 27.60  ? 212 ILE   C C     1 
ATOM   5120  O  O     . ILE   B 1  212 ? -4.275  22.253  -5.412  1.00 25.73  ? 212 ILE   C O     1 
ATOM   5121  C  CB    . ILE   B 1  212 ? -1.432  22.542  -3.727  1.00 28.87  ? 212 ILE   C CB    1 
ATOM   5122  C  CG1   . ILE   B 1  212 ? -0.802  22.305  -2.349  1.00 26.60  ? 212 ILE   C CG1   1 
ATOM   5123  C  CG2   . ILE   B 1  212 ? -2.142  23.877  -3.746  1.00 25.11  ? 212 ILE   C CG2   1 
ATOM   5124  C  CD1   . ILE   B 1  212 ? -1.510  23.014  -1.231  1.00 26.16  ? 212 ILE   C CD1   1 
ATOM   5125  N  N     . CYS   B 1  213 ? -2.456  21.605  -6.550  1.00 28.42  ? 213 CYS   C N     1 
ATOM   5126  C  CA    . CYS   B 1  213 ? -3.059  21.957  -7.831  1.00 29.09  ? 213 CYS   C CA    1 
ATOM   5127  C  C     . CYS   B 1  213 ? -4.213  21.031  -8.187  1.00 32.21  ? 213 CYS   C C     1 
ATOM   5128  O  O     . CYS   B 1  213 ? -5.212  21.467  -8.779  1.00 32.94  ? 213 CYS   C O     1 
ATOM   5129  C  CB    . CYS   B 1  213 ? -2.000  21.926  -8.924  1.00 28.38  ? 213 CYS   C CB    1 
ATOM   5130  S  SG    . CYS   B 1  213 ? -0.940  23.348  -8.882  1.00 27.28  ? 213 CYS   C SG    1 
ATOM   5131  N  N     . ARG   B 1  214 ? -4.087  19.745  -7.862  1.00 32.11  ? 214 ARG   C N     1 
ATOM   5132  C  CA    . ARG   B 1  214 ? -5.209  18.837  -8.054  1.00 29.90  ? 214 ARG   C CA    1 
ATOM   5133  C  C     . ARG   B 1  214 ? -6.356  19.188  -7.111  1.00 37.08  ? 214 ARG   C C     1 
ATOM   5134  O  O     . ARG   B 1  214 ? -7.467  19.494  -7.561  1.00 42.57  ? 214 ARG   C O     1 
ATOM   5135  C  CB    . ARG   B 1  214 ? -4.750  17.399  -7.863  1.00 24.18  ? 214 ARG   C CB    1 
ATOM   5136  C  CG    . ARG   B 1  214 ? -4.020  16.851  -9.044  1.00 29.12  ? 214 ARG   C CG    1 
ATOM   5137  C  CD    . ARG   B 1  214 ? -3.882  15.342  -8.968  1.00 41.58  ? 214 ARG   C CD    1 
ATOM   5138  N  NE    . ARG   B 1  214 ? -2.911  14.929  -7.960  1.00 47.61  ? 214 ARG   C NE    1 
ATOM   5139  C  CZ    . ARG   B 1  214 ? -2.654  13.667  -7.639  1.00 49.96  ? 214 ARG   C CZ    1 
ATOM   5140  N  NH1   . ARG   B 1  214 ? -3.299  12.659  -8.217  1.00 43.98  ? 214 ARG   C NH1   1 
ATOM   5141  N  NH2   . ARG   B 1  214 ? -1.731  13.411  -6.715  1.00 40.86  ? 214 ARG   C NH2   1 
ATOM   5142  N  N     . ARG   B 1  215 ? -6.093  19.194  -5.793  1.00 35.93  ? 215 ARG   C N     1 
ATOM   5143  C  CA    . ARG   B 1  215 ? -7.148  19.328  -4.787  1.00 39.34  ? 215 ARG   C CA    1 
ATOM   5144  C  C     . ARG   B 1  215 ? -7.684  20.741  -4.635  1.00 35.40  ? 215 ARG   C C     1 
ATOM   5145  O  O     . ARG   B 1  215 ? -8.709  20.914  -3.969  1.00 40.51  ? 215 ARG   C O     1 
ATOM   5146  C  CB    . ARG   B 1  215 ? -6.673  18.875  -3.404  1.00 41.78  ? 215 ARG   C CB    1 
ATOM   5147  C  CG    . ARG   B 1  215 ? -6.394  17.378  -3.206  1.00 59.32  ? 215 ARG   C CG    1 
ATOM   5148  C  CD    . ARG   B 1  215 ? -5.988  17.125  -1.736  1.00 71.99  ? 215 ARG   C CD    1 
ATOM   5149  N  NE    . ARG   B 1  215 ? -5.448  15.793  -1.475  1.00 86.15  ? 215 ARG   C NE    1 
ATOM   5150  C  CZ    . ARG   B 1  215 ? -4.409  15.254  -2.105  1.00 69.74  ? 215 ARG   C CZ    1 
ATOM   5151  N  NH1   . ARG   B 1  215 ? -3.853  15.843  -3.157  1.00 50.04  ? 215 ARG   C NH1   1 
ATOM   5152  N  NH2   . ARG   B 1  215 ? -3.919  14.091  -1.671  1.00 50.61  ? 215 ARG   C NH2   1 
ATOM   5153  N  N     . ASN   B 1  216 ? -7.023  21.749  -5.200  1.00 36.25  ? 216 ASN   C N     1 
ATOM   5154  C  CA    . ASN   B 1  216 ? -7.358  23.139  -4.906  1.00 33.54  ? 216 ASN   C CA    1 
ATOM   5155  C  C     . ASN   B 1  216 ? -7.733  23.952  -6.129  1.00 38.36  ? 216 ASN   C C     1 
ATOM   5156  O  O     . ASN   B 1  216 ? -8.449  24.952  -5.993  1.00 42.04  ? 216 ASN   C O     1 
ATOM   5157  C  CB    . ASN   B 1  216 ? -6.183  23.847  -4.203  1.00 40.03  ? 216 ASN   C CB    1 
ATOM   5158  C  CG    . ASN   B 1  216 ? -6.268  23.790  -2.678  1.00 33.05  ? 216 ASN   C CG    1 
ATOM   5159  O  OD1   . ASN   B 1  216 ? -5.689  22.915  -2.036  1.00 25.99  ? 216 ASN   C OD1   1 
ATOM   5160  N  ND2   . ASN   B 1  216 ? -6.959  24.758  -2.099  1.00 40.57  ? 216 ASN   C ND2   1 
ATOM   5161  N  N     . LEU   B 1  217 ? -7.251  23.571  -7.309  1.00 35.23  ? 217 LEU   C N     1 
ATOM   5162  C  CA    . LEU   B 1  217 ? -7.618  24.213  -8.557  1.00 28.58  ? 217 LEU   C CA    1 
ATOM   5163  C  C     . LEU   B 1  217 ? -8.364  23.275  -9.495  1.00 40.06  ? 217 LEU   C C     1 
ATOM   5164  O  O     . LEU   B 1  217 ? -8.658  23.665  -10.634 1.00 39.76  ? 217 LEU   C O     1 
ATOM   5165  C  CB    . LEU   B 1  217 ? -6.364  24.757  -9.247  1.00 33.45  ? 217 LEU   C CB    1 
ATOM   5166  C  CG    . LEU   B 1  217 ? -5.714  25.839  -8.381  1.00 39.25  ? 217 LEU   C CG    1 
ATOM   5167  C  CD1   . LEU   B 1  217 ? -4.409  26.334  -8.976  1.00 38.77  ? 217 LEU   C CD1   1 
ATOM   5168  C  CD2   . LEU   B 1  217 ? -6.677  27.000  -8.163  1.00 38.19  ? 217 LEU   C CD2   1 
ATOM   5169  N  N     . ASP   B 1  218 ? -8.667  22.048  -9.053  1.00 39.63  ? 218 ASP   C N     1 
ATOM   5170  C  CA    . ASP   B 1  218 ? -9.346  21.032  -9.870  1.00 44.90  ? 218 ASP   C CA    1 
ATOM   5171  C  C     . ASP   B 1  218 ? -8.688  20.869  -11.248 1.00 49.35  ? 218 ASP   C C     1 
ATOM   5172  O  O     . ASP   B 1  218 ? -9.339  20.513  -12.242 1.00 41.76  ? 218 ASP   C O     1 
ATOM   5173  C  CB    . ASP   B 1  218 ? -10.843 21.337  -9.964  1.00 35.52  ? 218 ASP   C CB    1 
ATOM   5174  C  CG    . ASP   B 1  218 ? -11.518 21.309  -8.589  1.00 52.57  ? 218 ASP   C CG    1 
ATOM   5175  O  OD1   . ASP   B 1  218 ? -11.630 20.200  -8.005  1.00 59.81  ? 218 ASP   C OD1   1 
ATOM   5176  O  OD2   . ASP   B 1  218 ? -11.899 22.391  -8.068  1.00 48.07  ? 218 ASP   C OD2   1 
ATOM   5177  N  N     . ILE   B 1  219 ? -7.374  21.116  -11.294 1.00 50.08  ? 219 ILE   C N     1 
ATOM   5178  C  CA    . ILE   B 1  219 ? -6.547  20.741  -12.437 1.00 41.95  ? 219 ILE   C CA    1 
ATOM   5179  C  C     . ILE   B 1  219 ? -6.351  19.234  -12.386 1.00 39.80  ? 219 ILE   C C     1 
ATOM   5180  O  O     . ILE   B 1  219 ? -5.882  18.685  -11.384 1.00 34.65  ? 219 ILE   C O     1 
ATOM   5181  C  CB    . ILE   B 1  219 ? -5.205  21.492  -12.428 1.00 38.23  ? 219 ILE   C CB    1 
ATOM   5182  C  CG1   . ILE   B 1  219 ? -5.412  22.962  -12.769 1.00 42.75  ? 219 ILE   C CG1   1 
ATOM   5183  C  CG2   . ILE   B 1  219 ? -4.232  20.918  -13.443 1.00 37.14  ? 219 ILE   C CG2   1 
ATOM   5184  C  CD1   . ILE   B 1  219 ? -4.412  23.894  -12.117 1.00 44.27  ? 219 ILE   C CD1   1 
ATOM   5185  N  N     . GLU   B 1  220 ? -6.723  18.562  -13.471 1.00 49.70  ? 220 GLU   C N     1 
ATOM   5186  C  CA    . GLU   B 1  220 ? -6.812  17.108  -13.472 1.00 36.65  ? 220 GLU   C CA    1 
ATOM   5187  C  C     . GLU   B 1  220 ? -5.427  16.468  -13.424 1.00 35.22  ? 220 GLU   C C     1 
ATOM   5188  O  O     . GLU   B 1  220 ? -5.160  15.613  -12.572 1.00 35.55  ? 220 GLU   C O     1 
ATOM   5189  C  CB    . GLU   B 1  220 ? -7.626  16.685  -14.698 1.00 41.56  ? 220 GLU   C CB    1 
ATOM   5190  C  CG    . GLU   B 1  220 ? -8.653  17.806  -15.066 1.00 69.95  ? 220 GLU   C CG    1 
ATOM   5191  C  CD    . GLU   B 1  220 ? -9.901  17.313  -15.808 1.00 84.95  ? 220 GLU   C CD    1 
ATOM   5192  O  OE1   . GLU   B 1  220 ? -9.793  16.250  -16.462 1.00 74.56  ? 220 GLU   C OE1   1 
ATOM   5193  O  OE2   . GLU   B 1  220 ? -10.975 17.988  -15.735 1.00 53.88  ? 220 GLU   C OE2   1 
ATOM   5194  N  N     . ARG   B 1  221 ? -4.520  16.885  -14.311 1.00 39.24  ? 221 ARG   C N     1 
ATOM   5195  C  CA    . ARG   B 1  221 ? -3.136  16.397  -14.325 1.00 42.05  ? 221 ARG   C CA    1 
ATOM   5196  C  C     . ARG   B 1  221 ? -2.228  17.611  -14.485 1.00 46.36  ? 221 ARG   C C     1 
ATOM   5197  O  O     . ARG   B 1  221 ? -1.872  17.997  -15.612 1.00 45.91  ? 221 ARG   C O     1 
ATOM   5198  C  CB    . ARG   B 1  221 ? -2.919  15.352  -15.424 1.00 34.83  ? 221 ARG   C CB    1 
ATOM   5199  C  CG    . ARG   B 1  221 ? -1.474  15.101  -15.793 1.00 36.25  ? 221 ARG   C CG    1 
ATOM   5200  C  CD    . ARG   B 1  221 ? -0.722  14.302  -14.746 1.00 37.53  ? 221 ARG   C CD    1 
ATOM   5201  N  NE    . ARG   B 1  221 ? 0.614   13.873  -15.171 1.00 43.07  ? 221 ARG   C NE    1 
ATOM   5202  C  CZ    . ARG   B 1  221 ? 1.670   14.674  -15.296 1.00 49.59  ? 221 ARG   C CZ    1 
ATOM   5203  N  NH1   . ARG   B 1  221 ? 1.571   15.985  -15.127 1.00 50.11  ? 221 ARG   C NH1   1 
ATOM   5204  N  NH2   . ARG   B 1  221 ? 2.857   14.149  -15.589 1.00 40.12  ? 221 ARG   C NH2   1 
ATOM   5205  N  N     . PRO   B 1  222 ? -1.850  18.253  -13.370 1.00 43.41  ? 222 PRO   C N     1 
ATOM   5206  C  CA    . PRO   B 1  222 ? -1.136  19.533  -13.449 1.00 28.32  ? 222 PRO   C CA    1 
ATOM   5207  C  C     . PRO   B 1  222 ? 0.203   19.407  -14.144 1.00 30.54  ? 222 PRO   C C     1 
ATOM   5208  O  O     . PRO   B 1  222 ? 0.863   18.369  -14.094 1.00 30.32  ? 222 PRO   C O     1 
ATOM   5209  C  CB    . PRO   B 1  222 ? -0.967  19.938  -11.980 1.00 30.93  ? 222 PRO   C CB    1 
ATOM   5210  C  CG    . PRO   B 1  222 ? -1.333  18.729  -11.170 1.00 32.95  ? 222 PRO   C CG    1 
ATOM   5211  C  CD    . PRO   B 1  222 ? -2.281  17.943  -11.994 1.00 38.70  ? 222 PRO   C CD    1 
ATOM   5212  N  N     . THR   B 1  223 ? 0.591   20.485  -14.812 1.00 31.16  ? 223 THR   C N     1 
ATOM   5213  C  CA    . THR   B 1  223 ? 1.820   20.541  -15.589 1.00 32.25  ? 223 THR   C CA    1 
ATOM   5214  C  C     . THR   B 1  223 ? 2.820   21.480  -14.932 1.00 34.03  ? 223 THR   C C     1 
ATOM   5215  O  O     . THR   B 1  223 ? 2.496   22.213  -13.992 1.00 33.02  ? 223 THR   C O     1 
ATOM   5216  C  CB    . THR   B 1  223 ? 1.530   21.014  -17.006 1.00 28.52  ? 223 THR   C CB    1 
ATOM   5217  O  OG1   . THR   B 1  223 ? 0.921   22.304  -16.944 1.00 28.94  ? 223 THR   C OG1   1 
ATOM   5218  C  CG2   . THR   B 1  223 ? 0.595   20.053  -17.691 1.00 28.34  ? 223 THR   C CG2   1 
ATOM   5219  N  N     . TYR   B 1  224 ? 4.059   21.466  -15.438 1.00 28.68  ? 224 TYR   C N     1 
ATOM   5220  C  CA    . TYR   B 1  224 ? 5.015   22.453  -14.943 1.00 27.17  ? 224 TYR   C CA    1 
ATOM   5221  C  C     . TYR   B 1  224 ? 4.438   23.864  -14.993 1.00 27.83  ? 224 TYR   C C     1 
ATOM   5222  O  O     . TYR   B 1  224 ? 4.721   24.676  -14.110 1.00 26.12  ? 224 TYR   C O     1 
ATOM   5223  C  CB    . TYR   B 1  224 ? 6.305   22.394  -15.737 1.00 17.87  ? 224 TYR   C CB    1 
ATOM   5224  C  CG    . TYR   B 1  224 ? 7.119   21.155  -15.495 1.00 20.67  ? 224 TYR   C CG    1 
ATOM   5225  C  CD1   . TYR   B 1  224 ? 7.039   20.447  -14.297 1.00 13.63  ? 224 TYR   C CD1   1 
ATOM   5226  C  CD2   . TYR   B 1  224 ? 7.988   20.702  -16.471 1.00 19.34  ? 224 TYR   C CD2   1 
ATOM   5227  C  CE1   . TYR   B 1  224 ? 7.814   19.328  -14.105 1.00 16.85  ? 224 TYR   C CE1   1 
ATOM   5228  C  CE2   . TYR   B 1  224 ? 8.741   19.581  -16.296 1.00 15.68  ? 224 TYR   C CE2   1 
ATOM   5229  C  CZ    . TYR   B 1  224 ? 8.664   18.904  -15.129 1.00 17.10  ? 224 TYR   C CZ    1 
ATOM   5230  O  OH    . TYR   B 1  224 ? 9.461   17.795  -15.016 1.00 25.36  ? 224 TYR   C OH    1 
ATOM   5231  N  N     . THR   B 1  225 ? 3.618   24.177  -16.003 1.00 30.19  ? 225 THR   C N     1 
ATOM   5232  C  CA    . THR   B 1  225 ? 3.101   25.538  -16.106 1.00 29.57  ? 225 THR   C CA    1 
ATOM   5233  C  C     . THR   B 1  225 ? 2.114   25.816  -14.986 1.00 32.10  ? 225 THR   C C     1 
ATOM   5234  O  O     . THR   B 1  225 ? 2.113   26.911  -14.411 1.00 30.48  ? 225 THR   C O     1 
ATOM   5235  C  CB    . THR   B 1  225 ? 2.462   25.783  -17.481 1.00 26.04  ? 225 THR   C CB    1 
ATOM   5236  O  OG1   . THR   B 1  225 ? 3.483   25.753  -18.493 1.00 28.66  ? 225 THR   C OG1   1 
ATOM   5237  C  CG2   . THR   B 1  225 ? 1.719   27.153  -17.522 1.00 21.33  ? 225 THR   C CG2   1 
ATOM   5238  N  N     . ASN   B 1  226 ? 1.254   24.843  -14.686 1.00 28.00  ? 226 ASN   C N     1 
ATOM   5239  C  CA    . ASN   B 1  226 ? 0.478   24.821  -13.456 1.00 28.39  ? 226 ASN   C CA    1 
ATOM   5240  C  C     . ASN   B 1  226 ? 1.384   25.065  -12.242 1.00 36.48  ? 226 ASN   C C     1 
ATOM   5241  O  O     . ASN   B 1  226 ? 1.312   26.104  -11.567 1.00 32.42  ? 226 ASN   C O     1 
ATOM   5242  C  CB    . ASN   B 1  226 ? -0.234  23.466  -13.311 1.00 30.60  ? 226 ASN   C CB    1 
ATOM   5243  C  CG    . ASN   B 1  226 ? -1.313  23.235  -14.365 1.00 34.85  ? 226 ASN   C CG    1 
ATOM   5244  O  OD1   . ASN   B 1  226 ? -1.461  22.130  -14.913 1.00 35.53  ? 226 ASN   C OD1   1 
ATOM   5245  N  ND2   . ASN   B 1  226 ? -2.104  24.260  -14.614 1.00 33.74  ? 226 ASN   C ND2   1 
ATOM   5246  N  N     . LEU   B 1  227 ? 2.250   24.089  -11.956 1.00 37.27  ? 227 LEU   C N     1 
ATOM   5247  C  CA    . LEU   B 1  227 ? 3.104   24.159  -10.772 1.00 28.44  ? 227 LEU   C CA    1 
ATOM   5248  C  C     . LEU   B 1  227 ? 3.828   25.488  -10.685 1.00 31.88  ? 227 LEU   C C     1 
ATOM   5249  O  O     . LEU   B 1  227 ? 3.796   26.165  -9.651  1.00 39.20  ? 227 LEU   C O     1 
ATOM   5250  C  CB    . LEU   B 1  227 ? 4.123   23.022  -10.791 1.00 28.30  ? 227 LEU   C CB    1 
ATOM   5251  C  CG    . LEU   B 1  227 ? 3.619   21.637  -10.407 1.00 25.46  ? 227 LEU   C CG    1 
ATOM   5252  C  CD1   . LEU   B 1  227 ? 2.323   21.387  -11.081 1.00 27.13  ? 227 LEU   C CD1   1 
ATOM   5253  C  CD2   . LEU   B 1  227 ? 4.643   20.586  -10.794 1.00 18.82  ? 227 LEU   C CD2   1 
ATOM   5254  N  N     . ASN   B 1  228 ? 4.494   25.876  -11.774 1.00 36.92  ? 228 ASN   C N     1 
ATOM   5255  C  CA    . ASN   B 1  228 ? 5.397   27.014  -11.718 1.00 23.67  ? 228 ASN   C CA    1 
ATOM   5256  C  C     . ASN   B 1  228 ? 4.636   28.287  -11.407 1.00 32.61  ? 228 ASN   C C     1 
ATOM   5257  O  O     . ASN   B 1  228 ? 5.134   29.139  -10.665 1.00 36.66  ? 228 ASN   C O     1 
ATOM   5258  C  CB    . ASN   B 1  228 ? 6.182   27.131  -13.022 1.00 22.32  ? 228 ASN   C CB    1 
ATOM   5259  C  CG    . ASN   B 1  228 ? 7.278   26.083  -13.132 1.00 26.06  ? 228 ASN   C CG    1 
ATOM   5260  O  OD1   . ASN   B 1  228 ? 7.542   25.374  -12.178 1.00 33.44  ? 228 ASN   C OD1   1 
ATOM   5261  N  ND2   . ASN   B 1  228 ? 7.934   26.000  -14.278 1.00 27.70  ? 228 ASN   C ND2   1 
ATOM   5262  N  N     . ARG   B 1  229 ? 3.406   28.419  -11.923 1.00 34.28  ? 229 ARG   C N     1 
ATOM   5263  C  CA    . ARG   B 1  229 ? 2.577   29.570  -11.567 1.00 32.87  ? 229 ARG   C CA    1 
ATOM   5264  C  C     . ARG   B 1  229 ? 2.391   29.674  -10.059 1.00 36.67  ? 229 ARG   C C     1 
ATOM   5265  O  O     . ARG   B 1  229 ? 2.420   30.775  -9.498  1.00 40.21  ? 229 ARG   C O     1 
ATOM   5266  C  CB    . ARG   B 1  229 ? 1.222   29.479  -12.251 1.00 27.66  ? 229 ARG   C CB    1 
ATOM   5267  C  CG    . ARG   B 1  229 ? 1.046   30.400  -13.448 1.00 41.46  ? 229 ARG   C CG    1 
ATOM   5268  C  CD    . ARG   B 1  229 ? 1.681   29.875  -14.747 1.00 51.58  ? 229 ARG   C CD    1 
ATOM   5269  N  NE    . ARG   B 1  229 ? 1.097   30.529  -15.919 1.00 58.26  ? 229 ARG   C NE    1 
ATOM   5270  C  CZ    . ARG   B 1  229 ? -0.048  30.164  -16.485 1.00 54.95  ? 229 ARG   C CZ    1 
ATOM   5271  N  NH1   . ARG   B 1  229 ? -0.741  29.125  -16.042 1.00 51.86  ? 229 ARG   C NH1   1 
ATOM   5272  N  NH2   . ARG   B 1  229 ? -0.516  30.865  -17.514 1.00 55.22  ? 229 ARG   C NH2   1 
ATOM   5273  N  N     . LEU   B 1  230 ? 2.211   28.540  -9.381  1.00 28.93  ? 230 LEU   C N     1 
ATOM   5274  C  CA    . LEU   B 1  230 ? 1.930   28.579  -7.950  1.00 33.05  ? 230 LEU   C CA    1 
ATOM   5275  C  C     . LEU   B 1  230 ? 3.188   28.846  -7.131  1.00 34.11  ? 230 LEU   C C     1 
ATOM   5276  O  O     . LEU   B 1  230 ? 3.136   29.545  -6.108  1.00 32.97  ? 230 LEU   C O     1 
ATOM   5277  C  CB    . LEU   B 1  230 ? 1.275   27.267  -7.514  1.00 37.66  ? 230 LEU   C CB    1 
ATOM   5278  C  CG    . LEU   B 1  230 ? 0.747   27.152  -6.086  1.00 26.42  ? 230 LEU   C CG    1 
ATOM   5279  C  CD1   . LEU   B 1  230 ? -0.314  28.190  -5.849  1.00 28.26  ? 230 LEU   C CD1   1 
ATOM   5280  C  CD2   . LEU   B 1  230 ? 0.204   25.781  -5.920  1.00 25.54  ? 230 LEU   C CD2   1 
ATOM   5281  N  N     . ILE   B 1  231 ? 4.320   28.279  -7.552  1.00 33.28  ? 231 ILE   C N     1 
ATOM   5282  C  CA    . ILE   B 1  231 ? 5.590   28.603  -6.913  1.00 27.67  ? 231 ILE   C CA    1 
ATOM   5283  C  C     . ILE   B 1  231 ? 5.894   30.096  -7.026  1.00 31.62  ? 231 ILE   C C     1 
ATOM   5284  O  O     . ILE   B 1  231 ? 6.489   30.695  -6.119  1.00 29.10  ? 231 ILE   C O     1 
ATOM   5285  C  CB    . ILE   B 1  231 ? 6.696   27.749  -7.539  1.00 24.95  ? 231 ILE   C CB    1 
ATOM   5286  C  CG1   . ILE   B 1  231 ? 6.159   26.338  -7.787  1.00 26.64  ? 231 ILE   C CG1   1 
ATOM   5287  C  CG2   . ILE   B 1  231 ? 7.912   27.747  -6.642  1.00 23.89  ? 231 ILE   C CG2   1 
ATOM   5288  C  CD1   . ILE   B 1  231 ? 7.226   25.352  -8.148  1.00 22.34  ? 231 ILE   C CD1   1 
ATOM   5289  N  N     . SER   B 1  232 ? 5.476   30.727  -8.124  1.00 30.34  ? 232 SER   C N     1 
ATOM   5290  C  CA    . SER   B 1  232 ? 5.768   32.143  -8.316  1.00 28.52  ? 232 SER   C CA    1 
ATOM   5291  C  C     . SER   B 1  232 ? 5.038   33.009  -7.295  1.00 32.95  ? 232 SER   C C     1 
ATOM   5292  O  O     . SER   B 1  232 ? 5.610   33.967  -6.757  1.00 30.82  ? 232 SER   C O     1 
ATOM   5293  C  CB    . SER   B 1  232 ? 5.389   32.556  -9.732  1.00 39.38  ? 232 SER   C CB    1 
ATOM   5294  O  OG    . SER   B 1  232 ? 5.639   31.500  -10.650 1.00 47.41  ? 232 SER   C OG    1 
ATOM   5295  N  N     . GLN   B 1  233 ? 3.767   32.709  -7.035  1.00 31.45  ? 233 GLN   C N     1 
ATOM   5296  C  CA    . GLN   B 1  233 ? 3.091   33.351  -5.918  1.00 27.28  ? 233 GLN   C CA    1 
ATOM   5297  C  C     . GLN   B 1  233 ? 3.922   33.221  -4.643  1.00 27.26  ? 233 GLN   C C     1 
ATOM   5298  O  O     . GLN   B 1  233 ? 4.202   34.210  -3.955  1.00 29.35  ? 233 GLN   C O     1 
ATOM   5299  C  CB    . GLN   B 1  233 ? 1.699   32.744  -5.750  1.00 23.84  ? 233 GLN   C CB    1 
ATOM   5300  C  CG    . GLN   B 1  233 ? 0.874   32.815  -7.025  1.00 25.92  ? 233 GLN   C CG    1 
ATOM   5301  C  CD    . GLN   B 1  233 ? 0.741   34.234  -7.536  1.00 27.25  ? 233 GLN   C CD    1 
ATOM   5302  O  OE1   . GLN   B 1  233 ? 1.113   35.165  -6.844  1.00 28.03  ? 233 GLN   C OE1   1 
ATOM   5303  N  NE2   . GLN   B 1  233 ? 0.200   34.404  -8.750  1.00 34.37  ? 233 GLN   C NE2   1 
ATOM   5304  N  N     . ILE   B 1  234 ? 4.366   32.011  -4.328  1.00 29.22  ? 234 ILE   C N     1 
ATOM   5305  C  CA    . ILE   B 1  234 ? 5.029   31.827  -3.047  1.00 29.69  ? 234 ILE   C CA    1 
ATOM   5306  C  C     . ILE   B 1  234 ? 6.399   32.505  -3.046  1.00 29.46  ? 234 ILE   C C     1 
ATOM   5307  O  O     . ILE   B 1  234 ? 6.789   33.139  -2.059  1.00 30.33  ? 234 ILE   C O     1 
ATOM   5308  C  CB    . ILE   B 1  234 ? 5.083   30.328  -2.715  1.00 24.53  ? 234 ILE   C CB    1 
ATOM   5309  C  CG1   . ILE   B 1  234 ? 3.645   29.785  -2.704  1.00 25.13  ? 234 ILE   C CG1   1 
ATOM   5310  C  CG2   . ILE   B 1  234 ? 5.715   30.121  -1.375  1.00 23.13  ? 234 ILE   C CG2   1 
ATOM   5311  C  CD1   . ILE   B 1  234 ? 3.444   28.380  -3.218  1.00 25.94  ? 234 ILE   C CD1   1 
ATOM   5312  N  N     . VAL   B 1  235 ? 7.127   32.444  -4.162  1.00 27.54  ? 235 VAL   C N     1 
ATOM   5313  C  CA    . VAL   B 1  235 ? 8.384   33.190  -4.241  1.00 28.36  ? 235 VAL   C CA    1 
ATOM   5314  C  C     . VAL   B 1  235 ? 8.122   34.686  -4.084  1.00 27.43  ? 235 VAL   C C     1 
ATOM   5315  O  O     . VAL   B 1  235 ? 8.742   35.363  -3.256  1.00 27.48  ? 235 VAL   C O     1 
ATOM   5316  C  CB    . VAL   B 1  235 ? 9.125   32.890  -5.560  1.00 25.18  ? 235 VAL   C CB    1 
ATOM   5317  C  CG1   . VAL   B 1  235 ? 10.336  33.780  -5.661  1.00 19.46  ? 235 VAL   C CG1   1 
ATOM   5318  C  CG2   . VAL   B 1  235 ? 9.534   31.422  -5.658  1.00 18.63  ? 235 VAL   C CG2   1 
ATOM   5319  N  N     . SER   B 1  236 ? 7.205   35.224  -4.895  1.00 31.84  ? 236 SER   C N     1 
ATOM   5320  C  CA    . SER   B 1  236 ? 6.872   36.642  -4.828  1.00 23.57  ? 236 SER   C CA    1 
ATOM   5321  C  C     . SER   B 1  236 ? 6.421   37.046  -3.431  1.00 26.60  ? 236 SER   C C     1 
ATOM   5322  O  O     . SER   B 1  236 ? 6.766   38.135  -2.953  1.00 31.24  ? 236 SER   C O     1 
ATOM   5323  C  CB    . SER   B 1  236 ? 5.788   36.964  -5.856  1.00 25.94  ? 236 SER   C CB    1 
ATOM   5324  O  OG    . SER   B 1  236 ? 5.158   38.198  -5.550  1.00 29.27  ? 236 SER   C OG    1 
ATOM   5325  N  N     . SER   B 1  237 ? 5.630   36.197  -2.765  1.00 27.91  ? 237 SER   C N     1 
ATOM   5326  C  CA    . SER   B 1  237 ? 5.265   36.460  -1.375  1.00 25.45  ? 237 SER   C CA    1 
ATOM   5327  C  C     . SER   B 1  237 ? 6.507   36.694  -0.534  1.00 26.72  ? 237 SER   C C     1 
ATOM   5328  O  O     . SER   B 1  237 ? 6.598   37.673  0.212   1.00 30.75  ? 237 SER   C O     1 
ATOM   5329  C  CB    . SER   B 1  237 ? 4.472   35.285  -0.806  1.00 25.67  ? 237 SER   C CB    1 
ATOM   5330  O  OG    . SER   B 1  237 ? 3.138   35.303  -1.255  1.00 27.94  ? 237 SER   C OG    1 
ATOM   5331  N  N     . ILE   B 1  238 ? 7.476   35.786  -0.652  1.00 26.02  ? 238 ILE   C N     1 
ATOM   5332  C  CA    . ILE   B 1  238 ? 8.690   35.835  0.148   1.00 26.03  ? 238 ILE   C CA    1 
ATOM   5333  C  C     . ILE   B 1  238 ? 9.518   37.066  -0.211  1.00 33.21  ? 238 ILE   C C     1 
ATOM   5334  O  O     . ILE   B 1  238 ? 10.114  37.713  0.663   1.00 36.85  ? 238 ILE   C O     1 
ATOM   5335  C  CB    . ILE   B 1  238 ? 9.457   34.510  -0.053  1.00 25.45  ? 238 ILE   C CB    1 
ATOM   5336  C  CG1   . ILE   B 1  238 ? 8.608   33.343  0.462   1.00 19.88  ? 238 ILE   C CG1   1 
ATOM   5337  C  CG2   . ILE   B 1  238 ? 10.842  34.527  0.593   1.00 24.37  ? 238 ILE   C CG2   1 
ATOM   5338  C  CD1   . ILE   B 1  238 ? 9.234   32.010  0.271   1.00 26.34  ? 238 ILE   C CD1   1 
ATOM   5339  N  N     . THR   B 1  239 ? 9.535   37.428  -1.492  1.00 24.27  ? 239 THR   C N     1 
ATOM   5340  C  CA    . THR   B 1  239 ? 10.385  38.481  -2.023  1.00 24.75  ? 239 THR   C CA    1 
ATOM   5341  C  C     . THR   B 1  239 ? 9.689   39.828  -2.114  1.00 26.90  ? 239 THR   C C     1 
ATOM   5342  O  O     . THR   B 1  239 ? 10.324  40.816  -2.493  1.00 25.71  ? 239 THR   C O     1 
ATOM   5343  C  CB    . THR   B 1  239 ? 10.872  38.089  -3.416  1.00 30.50  ? 239 THR   C CB    1 
ATOM   5344  O  OG1   . THR   B 1  239 ? 9.743   37.695  -4.210  1.00 36.81  ? 239 THR   C OG1   1 
ATOM   5345  C  CG2   . THR   B 1  239 ? 11.870  36.933  -3.361  1.00 24.49  ? 239 THR   C CG2   1 
ATOM   5346  N  N     . ALA   B 1  240 ? 8.393   39.889  -1.828  1.00 26.24  ? 240 ALA   C N     1 
ATOM   5347  C  CA    . ALA   B 1  240 ? 7.699   41.165  -1.945  1.00 26.16  ? 240 ALA   C CA    1 
ATOM   5348  C  C     . ALA   B 1  240 ? 8.168   42.155  -0.891  1.00 30.16  ? 240 ALA   C C     1 
ATOM   5349  O  O     . ALA   B 1  240 ? 8.156   43.369  -1.128  1.00 30.96  ? 240 ALA   C O     1 
ATOM   5350  C  CB    . ALA   B 1  240 ? 6.197   40.957  -1.838  1.00 18.24  ? 240 ALA   C CB    1 
ATOM   5351  N  N     . SER   B 1  241 ? 8.563   41.653  0.281   1.00 37.23  ? 241 SER   C N     1 
ATOM   5352  C  CA    . SER   B 1  241 ? 9.064   42.508  1.346   1.00 34.95  ? 241 SER   C CA    1 
ATOM   5353  C  C     . SER   B 1  241 ? 10.289  43.288  0.908   1.00 37.74  ? 241 SER   C C     1 
ATOM   5354  O  O     . SER   B 1  241 ? 10.504  44.410  1.393   1.00 39.31  ? 241 SER   C O     1 
ATOM   5355  C  CB    . SER   B 1  241 ? 9.378   41.659  2.571   1.00 38.15  ? 241 SER   C CB    1 
ATOM   5356  O  OG    . SER   B 1  241 ? 9.900   40.391  2.189   1.00 46.71  ? 241 SER   C OG    1 
ATOM   5357  N  N     . LEU   B 1  242 ? 11.071  42.722  -0.023  1.00 30.42  ? 242 LEU   C N     1 
ATOM   5358  C  CA    . LEU   B 1  242 ? 12.230  43.373  -0.618  1.00 26.46  ? 242 LEU   C CA    1 
ATOM   5359  C  C     . LEU   B 1  242 ? 11.890  44.312  -1.757  1.00 27.13  ? 242 LEU   C C     1 
ATOM   5360  O  O     . LEU   B 1  242 ? 12.673  45.221  -2.036  1.00 35.69  ? 242 LEU   C O     1 
ATOM   5361  C  CB    . LEU   B 1  242 ? 13.194  42.334  -1.160  1.00 22.52  ? 242 LEU   C CB    1 
ATOM   5362  C  CG    . LEU   B 1  242 ? 14.028  41.598  -0.136  1.00 28.43  ? 242 LEU   C CG    1 
ATOM   5363  C  CD1   . LEU   B 1  242 ? 14.220  40.190  -0.626  1.00 33.25  ? 242 LEU   C CD1   1 
ATOM   5364  C  CD2   . LEU   B 1  242 ? 15.370  42.299  -0.004  1.00 39.71  ? 242 LEU   C CD2   1 
ATOM   5365  N  N     . ARG   B 1  243 ? 10.752  44.112  -2.423  1.00 33.16  ? 243 ARG   C N     1 
ATOM   5366  C  CA    . ARG   B 1  243 ? 10.421  44.847  -3.635  1.00 28.98  ? 243 ARG   C CA    1 
ATOM   5367  C  C     . ARG   B 1  243 ? 9.401   45.949  -3.410  1.00 37.44  ? 243 ARG   C C     1 
ATOM   5368  O  O     . ARG   B 1  243 ? 9.335   46.884  -4.228  1.00 33.55  ? 243 ARG   C O     1 
ATOM   5369  C  CB    . ARG   B 1  243 ? 9.900   43.877  -4.703  1.00 30.94  ? 243 ARG   C CB    1 
ATOM   5370  C  CG    . ARG   B 1  243 ? 10.945  42.836  -5.111  1.00 27.30  ? 243 ARG   C CG    1 
ATOM   5371  C  CD    . ARG   B 1  243 ? 10.386  41.792  -6.043  1.00 32.60  ? 243 ARG   C CD    1 
ATOM   5372  N  NE    . ARG   B 1  243 ? 9.427   40.900  -5.401  1.00 32.47  ? 243 ARG   C NE    1 
ATOM   5373  C  CZ    . ARG   B 1  243 ? 8.126   40.906  -5.647  1.00 27.93  ? 243 ARG   C CZ    1 
ATOM   5374  N  NH1   . ARG   B 1  243 ? 7.588   41.767  -6.500  1.00 25.15  ? 243 ARG   C NH1   1 
ATOM   5375  N  NH2   . ARG   B 1  243 ? 7.348   40.020  -5.031  1.00 27.91  ? 243 ARG   C NH2   1 
ATOM   5376  N  N     . PHE   B 1  244 ? 8.617   45.860  -2.326  1.00 31.94  ? 244 PHE   C N     1 
ATOM   5377  C  CA    . PHE   B 1  244 ? 7.626   46.874  -1.970  1.00 31.87  ? 244 PHE   C CA    1 
ATOM   5378  C  C     . PHE   B 1  244 ? 7.866   47.342  -0.549  1.00 44.09  ? 244 PHE   C C     1 
ATOM   5379  O  O     . PHE   B 1  244 ? 7.871   46.530  0.381   1.00 53.03  ? 244 PHE   C O     1 
ATOM   5380  C  CB    . PHE   B 1  244 ? 6.209   46.326  -2.079  1.00 33.04  ? 244 PHE   C CB    1 
ATOM   5381  C  CG    . PHE   B 1  244 ? 5.805   46.010  -3.459  1.00 40.11  ? 244 PHE   C CG    1 
ATOM   5382  C  CD1   . PHE   B 1  244 ? 5.562   47.025  -4.357  1.00 30.28  ? 244 PHE   C CD1   1 
ATOM   5383  C  CD2   . PHE   B 1  244 ? 5.675   44.695  -3.870  1.00 33.32  ? 244 PHE   C CD2   1 
ATOM   5384  C  CE1   . PHE   B 1  244 ? 5.197   46.735  -5.634  1.00 33.57  ? 244 PHE   C CE1   1 
ATOM   5385  C  CE2   . PHE   B 1  244 ? 5.306   44.406  -5.161  1.00 33.11  ? 244 PHE   C CE2   1 
ATOM   5386  C  CZ    . PHE   B 1  244 ? 5.061   45.427  -6.043  1.00 28.61  ? 244 PHE   C CZ    1 
ATOM   5387  N  N     . ASP   B 1  245 ? 8.011   48.639  -0.358  1.00 42.17  ? 245 ASP   C N     1 
ATOM   5388  C  CA    . ASP   B 1  245 ? 8.137   49.100  1.010   1.00 49.80  ? 245 ASP   C CA    1 
ATOM   5389  C  C     . ASP   B 1  245 ? 6.823   49.682  1.516   1.00 49.62  ? 245 ASP   C C     1 
ATOM   5390  O  O     . ASP   B 1  245 ? 5.975   50.152  0.753   1.00 37.86  ? 245 ASP   C O     1 
ATOM   5391  C  CB    . ASP   B 1  245 ? 9.271   50.108  1.161   1.00 52.58  ? 245 ASP   C CB    1 
ATOM   5392  C  CG    . ASP   B 1  245 ? 10.310  49.643  2.169   1.00 66.29  ? 245 ASP   C CG    1 
ATOM   5393  O  OD1   . ASP   B 1  245 ? 11.526  49.821  1.903   1.00 77.78  ? 245 ASP   C OD1   1 
ATOM   5394  O  OD2   . ASP   B 1  245 ? 9.911   49.071  3.214   1.00 65.86  ? 245 ASP   C OD2   1 
ATOM   5395  N  N     . GLY   B 1  246 ? 6.658   49.614  2.824   1.00 54.91  ? 246 GLY   C N     1 
ATOM   5396  C  CA    . GLY   B 1  246 ? 5.477   50.150  3.454   1.00 49.44  ? 246 GLY   C CA    1 
ATOM   5397  C  C     . GLY   B 1  246 ? 5.664   50.164  4.949   1.00 41.87  ? 246 GLY   C C     1 
ATOM   5398  O  O     . GLY   B 1  246 ? 6.477   49.415  5.500   1.00 39.42  ? 246 GLY   C O     1 
ATOM   5399  N  N     . ALA   B 1  247 ? 4.903   51.051  5.595   1.00 35.59  ? 247 ALA   C N     1 
ATOM   5400  C  CA    . ALA   B 1  247 ? 4.916   51.179  7.043   1.00 34.47  ? 247 ALA   C CA    1 
ATOM   5401  C  C     . ALA   B 1  247 ? 5.028   49.819  7.748   1.00 48.32  ? 247 ALA   C C     1 
ATOM   5402  O  O     . ALA   B 1  247 ? 5.941   49.589  8.556   1.00 47.03  ? 247 ALA   C O     1 
ATOM   5403  C  CB    . ALA   B 1  247 ? 3.647   51.918  7.477   1.00 37.21  ? 247 ALA   C CB    1 
ATOM   5404  N  N     . LEU   B 1  248 ? 4.117   48.897  7.436   1.00 38.62  ? 248 LEU   C N     1 
ATOM   5405  C  CA    . LEU   B 1  248 ? 4.058   47.615  8.121   1.00 33.04  ? 248 LEU   C CA    1 
ATOM   5406  C  C     . LEU   B 1  248 ? 4.869   46.525  7.432   1.00 31.47  ? 248 LEU   C C     1 
ATOM   5407  O  O     . LEU   B 1  248 ? 4.935   45.403  7.948   1.00 30.46  ? 248 LEU   C O     1 
ATOM   5408  C  CB    . LEU   B 1  248 ? 2.600   47.172  8.272   1.00 34.13  ? 248 LEU   C CB    1 
ATOM   5409  C  CG    . LEU   B 1  248 ? 1.735   48.318  8.795   1.00 34.83  ? 248 LEU   C CG    1 
ATOM   5410  C  CD1   . LEU   B 1  248 ? 0.424   47.822  9.372   1.00 32.44  ? 248 LEU   C CD1   1 
ATOM   5411  C  CD2   . LEU   B 1  248 ? 2.523   49.085  9.837   1.00 39.92  ? 248 LEU   C CD2   1 
ATOM   5412  N  N     . ASN   B 1  249 ? 5.500   46.831  6.298   1.00 38.82  ? 249 ASN   C N     1 
ATOM   5413  C  CA    . ASN   B 1  249 ? 6.377   45.873  5.629   1.00 39.60  ? 249 ASN   C CA    1 
ATOM   5414  C  C     . ASN   B 1  249 ? 7.573   45.502  6.510   1.00 37.96  ? 249 ASN   C C     1 
ATOM   5415  O  O     . ASN   B 1  249 ? 8.135   46.349  7.210   1.00 43.33  ? 249 ASN   C O     1 
ATOM   5416  C  CB    . ASN   B 1  249 ? 6.867   46.465  4.309   1.00 40.87  ? 249 ASN   C CB    1 
ATOM   5417  C  CG    . ASN   B 1  249 ? 7.565   45.448  3.456   1.00 49.94  ? 249 ASN   C CG    1 
ATOM   5418  O  OD1   . ASN   B 1  249 ? 6.964   44.435  3.076   1.00 45.83  ? 249 ASN   C OD1   1 
ATOM   5419  N  ND2   . ASN   B 1  249 ? 8.842   45.693  3.156   1.00 46.12  ? 249 ASN   C ND2   1 
ATOM   5420  N  N     . VAL   B 1  250 ? 7.974   44.231  6.472   1.00 28.09  ? 250 VAL   C N     1 
ATOM   5421  C  CA    . VAL   B 1  250 ? 9.159   43.767  7.186   1.00 32.72  ? 250 VAL   C CA    1 
ATOM   5422  C  C     . VAL   B 1  250 ? 10.037  42.983  6.219   1.00 42.09  ? 250 VAL   C C     1 
ATOM   5423  O  O     . VAL   B 1  250 ? 9.566   42.028  5.593   1.00 47.38  ? 250 VAL   C O     1 
ATOM   5424  C  CB    . VAL   B 1  250 ? 8.795   42.898  8.404   1.00 31.40  ? 250 VAL   C CB    1 
ATOM   5425  C  CG1   . VAL   B 1  250 ? 10.055  42.384  9.065   1.00 24.88  ? 250 VAL   C CG1   1 
ATOM   5426  C  CG2   . VAL   B 1  250 ? 7.929   43.680  9.380   1.00 25.09  ? 250 VAL   C CG2   1 
ATOM   5427  N  N     . ASP   B 1  251 ? 11.311  43.375  6.108   1.00 53.00  ? 251 ASP   C N     1 
ATOM   5428  C  CA    . ASP   B 1  251 ? 12.226  42.756  5.145   1.00 50.38  ? 251 ASP   C CA    1 
ATOM   5429  C  C     . ASP   B 1  251 ? 12.296  41.247  5.346   1.00 49.09  ? 251 ASP   C C     1 
ATOM   5430  O  O     . ASP   B 1  251 ? 12.188  40.748  6.472   1.00 42.75  ? 251 ASP   C O     1 
ATOM   5431  C  CB    . ASP   B 1  251 ? 13.638  43.340  5.281   1.00 49.11  ? 251 ASP   C CB    1 
ATOM   5432  C  CG    . ASP   B 1  251 ? 13.765  44.743  4.674   1.00 68.62  ? 251 ASP   C CG    1 
ATOM   5433  O  OD1   . ASP   B 1  251 ? 12.742  45.455  4.545   1.00 72.64  ? 251 ASP   C OD1   1 
ATOM   5434  O  OD2   . ASP   B 1  251 ? 14.901  45.132  4.317   1.00 75.99  ? 251 ASP   C OD2   1 
ATOM   5435  N  N     . LEU   B 1  252 ? 12.491  40.516  4.235   1.00 43.22  ? 252 LEU   C N     1 
ATOM   5436  C  CA    . LEU   B 1  252 ? 12.721  39.079  4.343   1.00 34.66  ? 252 LEU   C CA    1 
ATOM   5437  C  C     . LEU   B 1  252 ? 13.987  38.778  5.123   1.00 28.45  ? 252 LEU   C C     1 
ATOM   5438  O  O     . LEU   B 1  252 ? 14.118  37.676  5.656   1.00 33.97  ? 252 LEU   C O     1 
ATOM   5439  C  CB    . LEU   B 1  252 ? 12.800  38.423  2.962   1.00 42.93  ? 252 LEU   C CB    1 
ATOM   5440  C  CG    . LEU   B 1  252 ? 13.402  37.006  2.927   1.00 32.90  ? 252 LEU   C CG    1 
ATOM   5441  C  CD1   . LEU   B 1  252 ? 12.561  35.992  3.720   1.00 17.00  ? 252 LEU   C CD1   1 
ATOM   5442  C  CD2   . LEU   B 1  252 ? 13.664  36.548  1.479   1.00 23.87  ? 252 LEU   C CD2   1 
ATOM   5443  N  N     . THR   B 1  253 ? 14.911  39.742  5.207   1.00 34.22  ? 253 THR   C N     1 
ATOM   5444  C  CA    . THR   B 1  253 ? 16.080  39.626  6.082   1.00 37.65  ? 253 THR   C CA    1 
ATOM   5445  C  C     . THR   B 1  253 ? 15.695  39.562  7.551   1.00 32.43  ? 253 THR   C C     1 
ATOM   5446  O  O     . THR   B 1  253 ? 16.303  38.815  8.323   1.00 34.95  ? 253 THR   C O     1 
ATOM   5447  C  CB    . THR   B 1  253 ? 17.010  40.816  5.906   1.00 38.72  ? 253 THR   C CB    1 
ATOM   5448  O  OG1   . THR   B 1  253 ? 17.775  40.674  4.710   1.00 36.86  ? 253 THR   C OG1   1 
ATOM   5449  C  CG2   . THR   B 1  253 ? 17.942  40.883  7.102   1.00 46.23  ? 253 THR   C CG2   1 
ATOM   5450  N  N     . GLU   B 1  254 ? 14.744  40.399  7.970   1.00 34.93  ? 254 GLU   C N     1 
ATOM   5451  C  CA    . GLU   B 1  254 ? 14.319  40.397  9.369   1.00 33.69  ? 254 GLU   C CA    1 
ATOM   5452  C  C     . GLU   B 1  254 ? 13.643  39.083  9.744   1.00 37.47  ? 254 GLU   C C     1 
ATOM   5453  O  O     . GLU   B 1  254 ? 13.863  38.558  10.846  1.00 46.88  ? 254 GLU   C O     1 
ATOM   5454  C  CB    . GLU   B 1  254 ? 13.386  41.582  9.649   1.00 36.51  ? 254 GLU   C CB    1 
ATOM   5455  C  CG    . GLU   B 1  254 ? 13.907  42.899  9.066   1.00 52.71  ? 254 GLU   C CG    1 
ATOM   5456  C  CD    . GLU   B 1  254 ? 13.055  44.101  9.422   1.00 45.58  ? 254 GLU   C CD    1 
ATOM   5457  O  OE1   . GLU   B 1  254 ? 13.044  44.451  10.635  1.00 42.90  ? 254 GLU   C OE1   1 
ATOM   5458  O  OE2   . GLU   B 1  254 ? 12.419  44.684  8.487   1.00 34.66  ? 254 GLU   C OE2   1 
ATOM   5459  N  N     . PHE   B 1  255 ? 12.809  38.531  8.855   1.00 31.83  ? 255 PHE   C N     1 
ATOM   5460  C  CA    . PHE   B 1  255 ? 12.268  37.208  9.129   1.00 24.12  ? 255 PHE   C CA    1 
ATOM   5461  C  C     . PHE   B 1  255 ? 13.383  36.186  9.262   1.00 25.07  ? 255 PHE   C C     1 
ATOM   5462  O  O     . PHE   B 1  255 ? 13.260  35.248  10.056  1.00 21.29  ? 255 PHE   C O     1 
ATOM   5463  C  CB    . PHE   B 1  255 ? 11.273  36.799  8.044   1.00 27.15  ? 255 PHE   C CB    1 
ATOM   5464  C  CG    . PHE   B 1  255 ? 10.004  37.602  8.064   1.00 27.54  ? 255 PHE   C CG    1 
ATOM   5465  C  CD1   . PHE   B 1  255 ? 9.108   37.468  9.108   1.00 30.70  ? 255 PHE   C CD1   1 
ATOM   5466  C  CD2   . PHE   B 1  255 ? 9.708   38.488  7.050   1.00 26.90  ? 255 PHE   C CD2   1 
ATOM   5467  C  CE1   . PHE   B 1  255 ? 7.944   38.205  9.133   1.00 29.00  ? 255 PHE   C CE1   1 
ATOM   5468  C  CE2   . PHE   B 1  255 ? 8.548   39.220  7.066   1.00 23.68  ? 255 PHE   C CE2   1 
ATOM   5469  C  CZ    . PHE   B 1  255 ? 7.669   39.088  8.101   1.00 26.89  ? 255 PHE   C CZ    1 
ATOM   5470  N  N     . GLN   B 1  256 ? 14.499  36.381  8.543   1.00 22.15  ? 256 GLN   C N     1 
ATOM   5471  C  CA    . GLN   B 1  256 ? 15.566  35.380  8.534   1.00 24.01  ? 256 GLN   C CA    1 
ATOM   5472  C  C     . GLN   B 1  256 ? 16.237  35.255  9.894   1.00 26.58  ? 256 GLN   C C     1 
ATOM   5473  O  O     . GLN   B 1  256 ? 16.557  34.143  10.334  1.00 25.56  ? 256 GLN   C O     1 
ATOM   5474  C  CB    . GLN   B 1  256 ? 16.594  35.721  7.472   1.00 22.61  ? 256 GLN   C CB    1 
ATOM   5475  C  CG    . GLN   B 1  256 ? 17.573  34.602  7.183   1.00 29.51  ? 256 GLN   C CG    1 
ATOM   5476  C  CD    . GLN   B 1  256 ? 18.457  34.922  5.983   1.00 40.78  ? 256 GLN   C CD    1 
ATOM   5477  O  OE1   . GLN   B 1  256 ? 17.965  35.488  4.997   1.00 36.28  ? 256 GLN   C OE1   1 
ATOM   5478  N  NE2   . GLN   B 1  256 ? 19.766  34.578  6.060   1.00 24.55  ? 256 GLN   C NE2   1 
ATOM   5479  N  N     . THR   B 1  257 ? 16.461  36.384  10.573  1.00 27.11  ? 257 THR   C N     1 
ATOM   5480  C  CA    . THR   B 1  257 ? 17.029  36.353  11.918  1.00 26.80  ? 257 THR   C CA    1 
ATOM   5481  C  C     . THR   B 1  257 ? 16.232  35.451  12.838  1.00 21.75  ? 257 THR   C C     1 
ATOM   5482  O  O     . THR   B 1  257 ? 16.798  34.808  13.728  1.00 21.15  ? 257 THR   C O     1 
ATOM   5483  C  CB    . THR   B 1  257 ? 17.076  37.752  12.522  1.00 27.30  ? 257 THR   C CB    1 
ATOM   5484  O  OG1   . THR   B 1  257 ? 17.619  38.669  11.568  1.00 27.40  ? 257 THR   C OG1   1 
ATOM   5485  C  CG2   . THR   B 1  257 ? 17.955  37.742  13.764  1.00 18.76  ? 257 THR   C CG2   1 
ATOM   5486  N  N     . ASN   B 1  258 ? 14.910  35.419  12.665  1.00 23.82  ? 258 ASN   C N     1 
ATOM   5487  C  CA    . ASN   B 1  258 ? 14.077  34.548  13.485  1.00 23.32  ? 258 ASN   C CA    1 
ATOM   5488  C  C     . ASN   B 1  258 ? 14.010  33.137  12.940  1.00 19.89  ? 258 ASN   C C     1 
ATOM   5489  O  O     . ASN   B 1  258 ? 13.763  32.214  13.718  1.00 24.82  ? 258 ASN   C O     1 
ATOM   5490  C  CB    . ASN   B 1  258 ? 12.660  35.109  13.615  1.00 23.47  ? 258 ASN   C CB    1 
ATOM   5491  C  CG    . ASN   B 1  258 ? 12.572  36.278  14.588  1.00 24.92  ? 258 ASN   C CG    1 
ATOM   5492  O  OD1   . ASN   B 1  258 ? 13.477  37.091  14.694  1.00 30.30  ? 258 ASN   C OD1   1 
ATOM   5493  N  ND2   . ASN   B 1  258 ? 11.474  36.358  15.299  1.00 24.65  ? 258 ASN   C ND2   1 
ATOM   5494  N  N     . LEU   B 1  259 ? 14.288  32.953  11.642  1.00 22.68  ? 259 LEU   C N     1 
ATOM   5495  C  CA    . LEU   B 1  259 ? 14.114  31.676  10.956  1.00 22.27  ? 259 LEU   C CA    1 
ATOM   5496  C  C     . LEU   B 1  259 ? 15.310  30.745  11.117  1.00 21.18  ? 259 LEU   C C     1 
ATOM   5497  O  O     . LEU   B 1  259 ? 15.153  29.524  10.956  1.00 29.54  ? 259 LEU   C O     1 
ATOM   5498  C  CB    . LEU   B 1  259 ? 13.829  31.916  9.459   1.00 20.85  ? 259 LEU   C CB    1 
ATOM   5499  C  CG    . LEU   B 1  259 ? 12.382  32.342  9.182   1.00 17.44  ? 259 LEU   C CG    1 
ATOM   5500  C  CD1   . LEU   B 1  259 ? 12.135  32.888  7.819   1.00 12.91  ? 259 LEU   C CD1   1 
ATOM   5501  C  CD2   . LEU   B 1  259 ? 11.462  31.199  9.471   1.00 19.93  ? 259 LEU   C CD2   1 
ATOM   5502  N  N     . VAL   B 1  260 ? 16.482  31.274  11.448  1.00 16.53  ? 260 VAL   C N     1 
ATOM   5503  C  CA    . VAL   B 1  260 ? 17.689  30.451  11.487  1.00 20.74  ? 260 VAL   C CA    1 
ATOM   5504  C  C     . VAL   B 1  260 ? 18.326  30.475  12.872  1.00 20.00  ? 260 VAL   C C     1 
ATOM   5505  O  O     . VAL   B 1  260 ? 19.131  31.365  13.173  1.00 19.13  ? 260 VAL   C O     1 
ATOM   5506  C  CB    . VAL   B 1  260 ? 18.701  30.912  10.430  1.00 16.09  ? 260 VAL   C CB    1 
ATOM   5507  C  CG1   . VAL   B 1  260 ? 19.798  29.917  10.357  1.00 12.71  ? 260 VAL   C CG1   1 
ATOM   5508  C  CG2   . VAL   B 1  260 ? 18.025  31.043  9.089   1.00 17.21  ? 260 VAL   C CG2   1 
ATOM   5509  N  N     . PRO   B 1  261 ? 18.043  29.512  13.715  1.00 18.38  ? 261 PRO   C N     1 
ATOM   5510  C  CA    . PRO   B 1  261 ? 18.578  29.557  15.080  1.00 22.34  ? 261 PRO   C CA    1 
ATOM   5511  C  C     . PRO   B 1  261 ? 19.998  29.027  15.121  1.00 19.80  ? 261 PRO   C C     1 
ATOM   5512  O  O     . PRO   B 1  261 ? 20.777  29.329  16.027  1.00 23.77  ? 261 PRO   C O     1 
ATOM   5513  C  CB    . PRO   B 1  261 ? 17.615  28.650  15.856  1.00 20.00  ? 261 PRO   C CB    1 
ATOM   5514  C  CG    . PRO   B 1  261 ? 17.286  27.581  14.851  1.00 18.84  ? 261 PRO   C CG    1 
ATOM   5515  C  CD    . PRO   B 1  261 ? 17.236  28.303  13.484  1.00 24.26  ? 261 PRO   C CD    1 
ATOM   5516  N  N     . TYR   B 1  262 ? 20.326  28.187  14.161  1.00 17.19  ? 262 TYR   C N     1 
ATOM   5517  C  CA    . TYR   B 1  262 ? 21.667  27.647  14.033  1.00 19.80  ? 262 TYR   C CA    1 
ATOM   5518  C  C     . TYR   B 1  262 ? 21.953  27.566  12.545  1.00 15.96  ? 262 TYR   C C     1 
ATOM   5519  O  O     . TYR   B 1  262 ? 21.024  27.485  11.738  1.00 13.64  ? 262 TYR   C O     1 
ATOM   5520  C  CB    . TYR   B 1  262 ? 21.805  26.274  14.703  1.00 12.71  ? 262 TYR   C CB    1 
ATOM   5521  C  CG    . TYR   B 1  262 ? 21.300  26.211  16.122  1.00 15.14  ? 262 TYR   C CG    1 
ATOM   5522  C  CD1   . TYR   B 1  262 ? 19.956  25.901  16.412  1.00 23.02  ? 262 TYR   C CD1   1 
ATOM   5523  C  CD2   . TYR   B 1  262 ? 22.152  26.444  17.178  1.00 13.38  ? 262 TYR   C CD2   1 
ATOM   5524  C  CE1   . TYR   B 1  262 ? 19.499  25.833  17.728  1.00 12.59  ? 262 TYR   C CE1   1 
ATOM   5525  C  CE2   . TYR   B 1  262 ? 21.710  26.382  18.478  1.00 11.93  ? 262 TYR   C CE2   1 
ATOM   5526  C  CZ    . TYR   B 1  262 ? 20.402  26.066  18.746  1.00 15.22  ? 262 TYR   C CZ    1 
ATOM   5527  O  OH    . TYR   B 1  262 ? 20.022  26.017  20.053  1.00 20.65  ? 262 TYR   C OH    1 
ATOM   5528  N  N     . PRO   B 1  263 ? 23.222  27.654  12.144  1.00 20.91  ? 263 PRO   C N     1 
ATOM   5529  C  CA    . PRO   B 1  263 ? 23.496  27.751  10.705  1.00 16.92  ? 263 PRO   C CA    1 
ATOM   5530  C  C     . PRO   B 1  263 ? 22.941  26.570  9.906   1.00 18.83  ? 263 PRO   C C     1 
ATOM   5531  O  O     . PRO   B 1  263 ? 22.450  26.780  8.791   1.00 12.23  ? 263 PRO   C O     1 
ATOM   5532  C  CB    . PRO   B 1  263 ? 25.028  27.870  10.672  1.00 7.80   ? 263 PRO   C CB    1 
ATOM   5533  C  CG    . PRO   B 1  263 ? 25.342  28.523  11.972  1.00 10.64  ? 263 PRO   C CG    1 
ATOM   5534  C  CD    . PRO   B 1  263 ? 24.451  27.836  12.935  1.00 17.37  ? 263 PRO   C CD    1 
ATOM   5535  N  N     . ARG   B 1  264 ? 22.937  25.342  10.465  1.00 23.95  ? 264 ARG   C N     1 
ATOM   5536  C  CA    . ARG   B 1  264 ? 22.487  24.183  9.690   1.00 19.87  ? 264 ARG   C CA    1 
ATOM   5537  C  C     . ARG   B 1  264 ? 20.961  24.004  9.693   1.00 20.40  ? 264 ARG   C C     1 
ATOM   5538  O  O     . ARG   B 1  264 ? 20.427  23.337  8.798   1.00 19.13  ? 264 ARG   C O     1 
ATOM   5539  C  CB    . ARG   B 1  264 ? 23.180  22.912  10.192  1.00 15.25  ? 264 ARG   C CB    1 
ATOM   5540  C  CG    . ARG   B 1  264 ? 24.614  22.768  9.749   1.00 9.83   ? 264 ARG   C CG    1 
ATOM   5541  C  CD    . ARG   B 1  264 ? 25.344  21.690  10.538  1.00 11.21  ? 264 ARG   C CD    1 
ATOM   5542  N  NE    . ARG   B 1  264 ? 24.705  20.393  10.369  1.00 17.62  ? 264 ARG   C NE    1 
ATOM   5543  C  CZ    . ARG   B 1  264 ? 24.975  19.560  9.370   1.00 22.60  ? 264 ARG   C CZ    1 
ATOM   5544  N  NH1   . ARG   B 1  264 ? 25.868  19.863  8.435   1.00 15.89  ? 264 ARG   C NH1   1 
ATOM   5545  N  NH2   . ARG   B 1  264 ? 24.330  18.398  9.302   1.00 15.11  ? 264 ARG   C NH2   1 
ATOM   5546  N  N     . ILE   B 1  265 ? 20.248  24.565  10.667  1.00 14.74  ? 265 ILE   C N     1 
ATOM   5547  C  CA    . ILE   B 1  265 ? 18.774  24.575  10.635  1.00 14.21  ? 265 ILE   C CA    1 
ATOM   5548  C  C     . ILE   B 1  265 ? 18.379  25.869  9.933   1.00 16.82  ? 265 ILE   C C     1 
ATOM   5549  O  O     . ILE   B 1  265 ? 18.003  26.868  10.548  1.00 22.18  ? 265 ILE   C O     1 
ATOM   5550  C  CB    . ILE   B 1  265 ? 18.177  24.455  12.039  1.00 15.93  ? 265 ILE   C CB    1 
ATOM   5551  C  CG1   . ILE   B 1  265 ? 18.758  23.236  12.724  1.00 16.35  ? 265 ILE   C CG1   1 
ATOM   5552  C  CG2   . ILE   B 1  265 ? 16.648  24.390  12.051  1.00 14.08  ? 265 ILE   C CG2   1 
ATOM   5553  C  CD1   . ILE   B 1  265 ? 19.810  23.677  13.655  1.00 16.00  ? 265 ILE   C CD1   1 
ATOM   5554  N  N     . HIS   B 1  266 ? 18.484  25.857  8.609   1.00 16.49  ? 266 HIS   C N     1 
ATOM   5555  C  CA    . HIS   B 1  266 ? 18.151  27.029  7.814   1.00 13.95  ? 266 HIS   C CA    1 
ATOM   5556  C  C     . HIS   B 1  266 ? 17.150  26.689  6.716   1.00 16.81  ? 266 HIS   C C     1 
ATOM   5557  O  O     . HIS   B 1  266 ? 17.146  27.334  5.667   1.00 15.32  ? 266 HIS   C O     1 
ATOM   5558  C  CB    . HIS   B 1  266 ? 19.403  27.693  7.223   1.00 15.92  ? 266 HIS   C CB    1 
ATOM   5559  C  CG    . HIS   B 1  266 ? 20.098  26.878  6.165   1.00 22.53  ? 266 HIS   C CG    1 
ATOM   5560  N  ND1   . HIS   B 1  266 ? 21.379  26.390  6.318   1.00 22.23  ? 266 HIS   C ND1   1 
ATOM   5561  C  CD2   . HIS   B 1  266 ? 19.696  26.476  4.936   1.00 20.25  ? 266 HIS   C CD2   1 
ATOM   5562  C  CE1   . HIS   B 1  266 ? 21.735  25.728  5.233   1.00 16.91  ? 266 HIS   C CE1   1 
ATOM   5563  N  NE2   . HIS   B 1  266 ? 20.729  25.760  4.380   1.00 24.72  ? 266 HIS   C NE2   1 
ATOM   5564  N  N     . PHE   B 1  267 ? 16.257  25.725  6.951   1.00 19.02  ? 267 PHE   C N     1 
ATOM   5565  C  CA    . PHE   B 1  267 ? 15.222  25.390  5.972   1.00 17.47  ? 267 PHE   C CA    1 
ATOM   5566  C  C     . PHE   B 1  267 ? 13.826  25.704  6.493   1.00 21.41  ? 267 PHE   C C     1 
ATOM   5567  O  O     . PHE   B 1  267 ? 13.254  24.898  7.245   1.00 29.58  ? 267 PHE   C O     1 
ATOM   5568  C  CB    . PHE   B 1  267 ? 15.320  23.919  5.595   1.00 15.69  ? 267 PHE   C CB    1 
ATOM   5569  C  CG    . PHE   B 1  267 ? 16.694  23.485  5.152   1.00 20.19  ? 267 PHE   C CG    1 
ATOM   5570  C  CD1   . PHE   B 1  267 ? 17.660  23.130  6.092   1.00 17.10  ? 267 PHE   C CD1   1 
ATOM   5571  C  CD2   . PHE   B 1  267 ? 17.012  23.404  3.792   1.00 13.98  ? 267 PHE   C CD2   1 
ATOM   5572  C  CE1   . PHE   B 1  267 ? 18.899  22.722  5.686   1.00 21.64  ? 267 PHE   C CE1   1 
ATOM   5573  C  CE2   . PHE   B 1  267 ? 18.266  22.998  3.382   1.00 12.08  ? 267 PHE   C CE2   1 
ATOM   5574  C  CZ    . PHE   B 1  267 ? 19.210  22.661  4.320   1.00 20.87  ? 267 PHE   C CZ    1 
ATOM   5575  N  N     . PRO   B 1  268 ? 13.234  26.843  6.138   1.00 20.85  ? 268 PRO   C N     1 
ATOM   5576  C  CA    . PRO   B 1  268 ? 11.866  27.113  6.572   1.00 21.46  ? 268 PRO   C CA    1 
ATOM   5577  C  C     . PRO   B 1  268 ? 10.874  26.340  5.729   1.00 22.52  ? 268 PRO   C C     1 
ATOM   5578  O  O     . PRO   B 1  268 ? 11.085  26.103  4.539   1.00 30.08  ? 268 PRO   C O     1 
ATOM   5579  C  CB    . PRO   B 1  268 ? 11.701  28.630  6.359   1.00 15.10  ? 268 PRO   C CB    1 
ATOM   5580  C  CG    . PRO   B 1  268 ? 13.019  29.156  6.093   1.00 14.53  ? 268 PRO   C CG    1 
ATOM   5581  C  CD    . PRO   B 1  268 ? 13.829  28.031  5.508   1.00 22.42  ? 268 PRO   C CD    1 
ATOM   5582  N  N     . LEU   B 1  269 ? 9.776   25.959  6.372   1.00 17.06  ? 269 LEU   C N     1 
ATOM   5583  C  CA    . LEU   B 1  269 ? 8.618   25.411  5.697   1.00 16.81  ? 269 LEU   C CA    1 
ATOM   5584  C  C     . LEU   B 1  269 ? 7.699   26.554  5.307   1.00 21.38  ? 269 LEU   C C     1 
ATOM   5585  O  O     . LEU   B 1  269 ? 7.323   27.356  6.161   1.00 28.85  ? 269 LEU   C O     1 
ATOM   5586  C  CB    . LEU   B 1  269 ? 7.885   24.446  6.619   1.00 20.94  ? 269 LEU   C CB    1 
ATOM   5587  C  CG    . LEU   B 1  269 ? 6.678   23.782  5.980   1.00 26.52  ? 269 LEU   C CG    1 
ATOM   5588  C  CD1   . LEU   B 1  269 ? 7.216   22.917  4.880   1.00 27.54  ? 269 LEU   C CD1   1 
ATOM   5589  C  CD2   . LEU   B 1  269 ? 5.880   22.952  6.981   1.00 19.41  ? 269 LEU   C CD2   1 
ATOM   5590  N  N     . ALA   B 1  270 ? 7.339   26.638  4.031   1.00 19.87  ? 270 ALA   C N     1 
ATOM   5591  C  CA    . ALA   B 1  270 ? 6.487   27.718  3.561   1.00 16.78  ? 270 ALA   C CA    1 
ATOM   5592  C  C     . ALA   B 1  270 ? 5.100   27.180  3.312   1.00 25.74  ? 270 ALA   C C     1 
ATOM   5593  O  O     . ALA   B 1  270 ? 4.926   26.013  2.963   1.00 27.48  ? 270 ALA   C O     1 
ATOM   5594  C  CB    . ALA   B 1  270 ? 7.009   28.354  2.282   1.00 23.99  ? 270 ALA   C CB    1 
ATOM   5595  N  N     . THR   B 1  271 ? 4.111   28.047  3.508   1.00 28.52  ? 271 THR   C N     1 
ATOM   5596  C  CA    . THR   B 1  271 ? 2.699   27.667  3.471   1.00 28.04  ? 271 THR   C CA    1 
ATOM   5597  C  C     . THR   B 1  271 ? 1.939   28.873  2.949   1.00 25.34  ? 271 THR   C C     1 
ATOM   5598  O  O     . THR   B 1  271 ? 2.018   29.947  3.548   1.00 29.25  ? 271 THR   C O     1 
ATOM   5599  C  CB    . THR   B 1  271 ? 2.171   27.269  4.864   1.00 32.53  ? 271 THR   C CB    1 
ATOM   5600  O  OG1   . THR   B 1  271 ? 2.758   26.034  5.306   1.00 34.44  ? 271 THR   C OG1   1 
ATOM   5601  C  CG2   . THR   B 1  271 ? 0.672   27.111  4.831   1.00 34.91  ? 271 THR   C CG2   1 
ATOM   5602  N  N     . TYR   B 1  272 ? 1.224   28.706  1.844   1.00 20.09  ? 272 TYR   C N     1 
ATOM   5603  C  CA    . TYR   B 1  272 ? 0.568   29.806  1.152   1.00 22.72  ? 272 TYR   C CA    1 
ATOM   5604  C  C     . TYR   B 1  272 ? -0.946  29.596  1.137   1.00 25.71  ? 272 TYR   C C     1 
ATOM   5605  O  O     . TYR   B 1  272 ? -1.418  28.471  0.953   1.00 34.35  ? 272 TYR   C O     1 
ATOM   5606  C  CB    . TYR   B 1  272 ? 1.107   29.920  -0.280  1.00 23.33  ? 272 TYR   C CB    1 
ATOM   5607  C  CG    . TYR   B 1  272 ? 0.538   31.063  -1.060  1.00 19.88  ? 272 TYR   C CG    1 
ATOM   5608  C  CD1   . TYR   B 1  272 ? 0.998   32.342  -0.858  1.00 21.01  ? 272 TYR   C CD1   1 
ATOM   5609  C  CD2   . TYR   B 1  272 ? -0.465  30.864  -1.988  1.00 24.34  ? 272 TYR   C CD2   1 
ATOM   5610  C  CE1   . TYR   B 1  272 ? 0.483   33.395  -1.546  1.00 24.71  ? 272 TYR   C CE1   1 
ATOM   5611  C  CE2   . TYR   B 1  272 ? -1.002  31.925  -2.702  1.00 24.82  ? 272 TYR   C CE2   1 
ATOM   5612  C  CZ    . TYR   B 1  272 ? -0.515  33.193  -2.475  1.00 25.93  ? 272 TYR   C CZ    1 
ATOM   5613  O  OH    . TYR   B 1  272 ? -1.005  34.291  -3.161  1.00 26.27  ? 272 TYR   C OH    1 
ATOM   5614  N  N     . ALA   B 1  273 ? -1.704  30.674  1.343   1.00 20.12  ? 273 ALA   C N     1 
ATOM   5615  C  CA    . ALA   B 1  273 ? -3.159  30.668  1.229   1.00 21.20  ? 273 ALA   C CA    1 
ATOM   5616  C  C     . ALA   B 1  273 ? -3.606  32.048  0.774   1.00 20.94  ? 273 ALA   C C     1 
ATOM   5617  O  O     . ALA   B 1  273 ? -2.903  33.027  1.027   1.00 24.47  ? 273 ALA   C O     1 
ATOM   5618  C  CB    . ALA   B 1  273 ? -3.830  30.312  2.555   1.00 18.25  ? 273 ALA   C CB    1 
ATOM   5619  N  N     . PRO   B 1  274 ? -4.732  32.163  0.068   1.00 21.61  ? 274 PRO   C N     1 
ATOM   5620  C  CA    . PRO   B 1  274 ? -5.617  31.128  -0.463  1.00 18.90  ? 274 PRO   C CA    1 
ATOM   5621  C  C     . PRO   B 1  274 ? -5.113  30.631  -1.799  1.00 25.79  ? 274 PRO   C C     1 
ATOM   5622  O  O     . PRO   B 1  274 ? -4.545  31.415  -2.563  1.00 29.21  ? 274 PRO   C O     1 
ATOM   5623  C  CB    . PRO   B 1  274 ? -6.936  31.879  -0.630  1.00 20.87  ? 274 PRO   C CB    1 
ATOM   5624  C  CG    . PRO   B 1  274 ? -6.477  33.244  -1.103  1.00 26.48  ? 274 PRO   C CG    1 
ATOM   5625  C  CD    . PRO   B 1  274 ? -5.175  33.506  -0.358  1.00 25.09  ? 274 PRO   C CD    1 
ATOM   5626  N  N     . VAL   B 1  275 ? -5.276  29.345  -2.097  1.00 32.88  ? 275 VAL   C N     1 
ATOM   5627  C  CA    . VAL   B 1  275 ? -5.140  28.811  -3.451  1.00 29.31  ? 275 VAL   C CA    1 
ATOM   5628  C  C     . VAL   B 1  275 ? -6.522  28.316  -3.850  1.00 32.77  ? 275 VAL   C C     1 
ATOM   5629  O  O     . VAL   B 1  275 ? -6.978  27.248  -3.413  1.00 30.23  ? 275 VAL   C O     1 
ATOM   5630  C  CB    . VAL   B 1  275 ? -4.092  27.703  -3.555  1.00 27.41  ? 275 VAL   C CB    1 
ATOM   5631  C  CG1   . VAL   B 1  275 ? -3.888  27.344  -5.004  1.00 29.57  ? 275 VAL   C CG1   1 
ATOM   5632  C  CG2   . VAL   B 1  275 ? -2.780  28.165  -2.937  1.00 28.42  ? 275 VAL   C CG2   1 
ATOM   5633  N  N     . ILE   B 1  276 ? -7.190  29.105  -4.682  1.00 33.36  ? 276 ILE   C N     1 
ATOM   5634  C  CA    . ILE   B 1  276 ? -8.609  28.966  -4.943  1.00 31.10  ? 276 ILE   C CA    1 
ATOM   5635  C  C     . ILE   B 1  276 ? -8.840  29.289  -6.407  1.00 37.14  ? 276 ILE   C C     1 
ATOM   5636  O  O     . ILE   B 1  276 ? -8.128  30.106  -6.999  1.00 33.21  ? 276 ILE   C O     1 
ATOM   5637  C  CB    . ILE   B 1  276 ? -9.419  29.900  -4.018  1.00 39.50  ? 276 ILE   C CB    1 
ATOM   5638  C  CG1   . ILE   B 1  276 ? -10.863 29.428  -3.893  1.00 50.73  ? 276 ILE   C CG1   1 
ATOM   5639  C  CG2   . ILE   B 1  276 ? -9.346  31.326  -4.520  1.00 42.81  ? 276 ILE   C CG2   1 
ATOM   5640  C  CD1   . ILE   B 1  276 ? -10.984 28.002  -3.361  1.00 51.62  ? 276 ILE   C CD1   1 
ATOM   5641  N  N     . SER   B 1  277 ? -9.827  28.627  -6.999  1.00 44.65  ? 277 SER   C N     1 
ATOM   5642  C  CA    . SER   B 1  277 ? -10.184 28.883  -8.388  1.00 35.35  ? 277 SER   C CA    1 
ATOM   5643  C  C     . SER   B 1  277 ? -11.104 30.093  -8.501  1.00 35.59  ? 277 SER   C C     1 
ATOM   5644  O  O     . SER   B 1  277 ? -11.847 30.413  -7.573  1.00 31.66  ? 277 SER   C O     1 
ATOM   5645  C  CB    . SER   B 1  277 ? -10.872 27.661  -8.979  1.00 35.08  ? 277 SER   C CB    1 
ATOM   5646  O  OG    . SER   B 1  277 ? -12.053 27.366  -8.256  1.00 39.08  ? 277 SER   C OG    1 
ATOM   5647  N  N     . ALA   B 1  278 ? -11.053 30.774  -9.651  1.00 39.52  ? 278 ALA   C N     1 
ATOM   5648  C  CA    . ALA   B 1  278 ? -12.019 31.846  -9.888  1.00 38.44  ? 278 ALA   C CA    1 
ATOM   5649  C  C     . ALA   B 1  278 ? -13.444 31.322  -9.741  1.00 35.97  ? 278 ALA   C C     1 
ATOM   5650  O  O     . ALA   B 1  278 ? -14.282 31.930  -9.064  1.00 29.74  ? 278 ALA   C O     1 
ATOM   5651  C  CB    . ALA   B 1  278 ? -11.814 32.467  -11.271 1.00 33.31  ? 278 ALA   C CB    1 
ATOM   5652  N  N     . GLU   B 1  279 ? -13.725 30.170  -10.348 1.00 35.24  ? 279 GLU   C N     1 
ATOM   5653  C  CA    . GLU   B 1  279 ? -15.039 29.561  -10.199 1.00 40.30  ? 279 GLU   C CA    1 
ATOM   5654  C  C     . GLU   B 1  279 ? -15.497 29.565  -8.734  1.00 40.57  ? 279 GLU   C C     1 
ATOM   5655  O  O     . GLU   B 1  279 ? -16.682 29.781  -8.448  1.00 39.13  ? 279 GLU   C O     1 
ATOM   5656  C  CB    . GLU   B 1  279 ? -15.010 28.138  -10.781 1.00 44.72  ? 279 GLU   C CB    1 
ATOM   5657  C  CG    . GLU   B 1  279 ? -14.790 28.028  -12.320 1.00 39.72  ? 279 GLU   C CG    1 
ATOM   5658  C  CD    . GLU   B 1  279 ? -13.344 28.265  -12.777 1.00 50.18  ? 279 GLU   C CD    1 
ATOM   5659  O  OE1   . GLU   B 1  279 ? -12.406 28.088  -11.971 1.00 43.72  ? 279 GLU   C OE1   1 
ATOM   5660  O  OE2   . GLU   B 1  279 ? -13.140 28.633  -13.958 1.00 51.67  ? 279 GLU   C OE2   1 
ATOM   5661  N  N     . LYS   B 1  280 ? -14.557 29.390  -7.789  1.00 45.24  ? 280 LYS   C N     1 
ATOM   5662  C  CA    . LYS   B 1  280 ? -14.867 29.210  -6.369  1.00 42.74  ? 280 LYS   C CA    1 
ATOM   5663  C  C     . LYS   B 1  280 ? -14.564 30.415  -5.473  1.00 46.75  ? 280 LYS   C C     1 
ATOM   5664  O  O     . LYS   B 1  280 ? -15.031 30.438  -4.327  1.00 42.03  ? 280 LYS   C O     1 
ATOM   5665  C  CB    . LYS   B 1  280 ? -14.106 28.008  -5.814  1.00 34.99  ? 280 LYS   C CB    1 
ATOM   5666  C  CG    . LYS   B 1  280 ? -14.914 27.170  -4.846  1.00 48.81  ? 280 LYS   C CG    1 
ATOM   5667  C  CD    . LYS   B 1  280 ? -15.893 26.242  -5.578  1.00 60.99  ? 280 LYS   C CD    1 
ATOM   5668  C  CE    . LYS   B 1  280 ? -15.186 25.301  -6.570  1.00 69.00  ? 280 LYS   C CE    1 
ATOM   5669  N  NZ    . LYS   B 1  280 ? -14.300 24.253  -5.963  1.00 72.91  ? 280 LYS   C NZ    1 
ATOM   5670  N  N     . ALA   B 1  281 ? -13.773 31.393  -5.925  1.00 46.54  ? 281 ALA   C N     1 
ATOM   5671  C  CA    . ALA   B 1  281 ? -13.631 32.625  -5.157  1.00 41.70  ? 281 ALA   C CA    1 
ATOM   5672  C  C     . ALA   B 1  281 ? -14.723 33.620  -5.476  1.00 41.48  ? 281 ALA   C C     1 
ATOM   5673  O  O     . ALA   B 1  281 ? -14.769 34.682  -4.848  1.00 45.23  ? 281 ALA   C O     1 
ATOM   5674  C  CB    . ALA   B 1  281 ? -12.274 33.284  -5.409  1.00 38.81  ? 281 ALA   C CB    1 
ATOM   5675  N  N     . TYR   B 1  282 ? -15.581 33.311  -6.445  1.00 39.44  ? 282 TYR   C N     1 
ATOM   5676  C  CA    . TYR   B 1  282 ? -16.683 34.194  -6.794  1.00 36.46  ? 282 TYR   C CA    1 
ATOM   5677  C  C     . TYR   B 1  282 ? -17.718 34.202  -5.677  1.00 38.03  ? 282 TYR   C C     1 
ATOM   5678  O  O     . TYR   B 1  282 ? -17.981 33.170  -5.049  1.00 47.13  ? 282 TYR   C O     1 
ATOM   5679  C  CB    . TYR   B 1  282 ? -17.302 33.741  -8.111  1.00 37.62  ? 282 TYR   C CB    1 
ATOM   5680  C  CG    . TYR   B 1  282 ? -18.445 34.581  -8.624  1.00 36.08  ? 282 TYR   C CG    1 
ATOM   5681  C  CD1   . TYR   B 1  282 ? -18.244 35.897  -9.039  1.00 38.18  ? 282 TYR   C CD1   1 
ATOM   5682  C  CD2   . TYR   B 1  282 ? -19.721 34.047  -8.725  1.00 35.22  ? 282 TYR   C CD2   1 
ATOM   5683  C  CE1   . TYR   B 1  282 ? -19.293 36.669  -9.523  1.00 23.46  ? 282 TYR   C CE1   1 
ATOM   5684  C  CE2   . TYR   B 1  282 ? -20.766 34.801  -9.205  1.00 39.88  ? 282 TYR   C CE2   1 
ATOM   5685  C  CZ    . TYR   B 1  282 ? -20.544 36.111  -9.609  1.00 34.05  ? 282 TYR   C CZ    1 
ATOM   5686  O  OH    . TYR   B 1  282 ? -21.600 36.853  -10.089 1.00 43.61  ? 282 TYR   C OH    1 
ATOM   5687  N  N     . HIS   B 1  283 ? -18.298 35.374  -5.429  1.00 38.54  ? 283 HIS   C N     1 
ATOM   5688  C  CA    . HIS   B 1  283 ? -19.227 35.602  -4.313  1.00 51.92  ? 283 HIS   C CA    1 
ATOM   5689  C  C     . HIS   B 1  283 ? -18.781 34.804  -3.089  1.00 51.54  ? 283 HIS   C C     1 
ATOM   5690  O  O     . HIS   B 1  283 ? -19.471 33.914  -2.590  1.00 59.49  ? 283 HIS   C O     1 
ATOM   5691  C  CB    . HIS   B 1  283 ? -20.678 35.254  -4.683  1.00 49.87  ? 283 HIS   C CB    1 
ATOM   5692  C  CG    . HIS   B 1  283 ? -21.315 36.195  -5.664  1.00 44.76  ? 283 HIS   C CG    1 
ATOM   5693  N  ND1   . HIS   B 1  283 ? -20.822 37.460  -5.928  1.00 40.71  ? 283 HIS   C ND1   1 
ATOM   5694  C  CD2   . HIS   B 1  283 ? -22.412 36.051  -6.448  1.00 36.91  ? 283 HIS   C CD2   1 
ATOM   5695  C  CE1   . HIS   B 1  283 ? -21.581 38.051  -6.834  1.00 40.90  ? 283 HIS   C CE1   1 
ATOM   5696  N  NE2   . HIS   B 1  283 ? -22.556 37.219  -7.164  1.00 44.10  ? 283 HIS   C NE2   1 
ATOM   5697  N  N     . GLU   B 1  284 ? -17.582 35.118  -2.628  1.00 49.15  ? 284 GLU   C N     1 
ATOM   5698  C  CA    . GLU   B 1  284 ? -17.023 34.346  -1.536  1.00 52.70  ? 284 GLU   C CA    1 
ATOM   5699  C  C     . GLU   B 1  284 ? -15.692 34.940  -1.112  1.00 54.15  ? 284 GLU   C C     1 
ATOM   5700  O  O     . GLU   B 1  284 ? -14.641 34.485  -1.569  1.00 61.88  ? 284 GLU   C O     1 
ATOM   5701  C  CB    . GLU   B 1  284 ? -16.870 32.887  -1.958  1.00 50.59  ? 284 GLU   C CB    1 
ATOM   5702  C  CG    . GLU   B 1  284 ? -17.062 31.915  -0.813  1.00 58.38  ? 284 GLU   C CG    1 
ATOM   5703  C  CD    . GLU   B 1  284 ? -15.755 31.579  -0.156  1.00 66.32  ? 284 GLU   C CD    1 
ATOM   5704  O  OE1   . GLU   B 1  284 ? -14.771 31.369  -0.909  1.00 67.59  ? 284 GLU   C OE1   1 
ATOM   5705  O  OE2   . GLU   B 1  284 ? -15.703 31.549  1.096   1.00 68.78  ? 284 GLU   C OE2   1 
ATOM   5706  N  N     . GLN   B 1  285 ? -15.723 35.959  -0.252  1.00 50.28  ? 285 GLN   C N     1 
ATOM   5707  C  CA    . GLN   B 1  285 ? -14.482 36.599  0.136   1.00 47.84  ? 285 GLN   C CA    1 
ATOM   5708  C  C     . GLN   B 1  285 ? -13.754 35.762  1.186   1.00 43.05  ? 285 GLN   C C     1 
ATOM   5709  O  O     . GLN   B 1  285 ? -14.336 34.915  1.869   1.00 46.33  ? 285 GLN   C O     1 
ATOM   5710  C  CB    . GLN   B 1  285 ? -14.735 38.009  0.657   1.00 49.81  ? 285 GLN   C CB    1 
ATOM   5711  C  CG    . GLN   B 1  285 ? -13.529 38.931  0.461   1.00 56.91  ? 285 GLN   C CG    1 
ATOM   5712  C  CD    . GLN   B 1  285 ? -13.155 39.113  -1.013  1.00 56.26  ? 285 GLN   C CD    1 
ATOM   5713  O  OE1   . GLN   B 1  285 ? -12.061 38.695  -1.461  1.00 53.09  ? 285 GLN   C OE1   1 
ATOM   5714  N  NE2   . GLN   B 1  285 ? -14.063 39.747  -1.776  1.00 41.64  ? 285 GLN   C NE2   1 
ATOM   5715  N  N     . LEU   B 1  286 ? -12.455 36.006  1.299   1.00 40.05  ? 286 LEU   C N     1 
ATOM   5716  C  CA    . LEU   B 1  286 ? -11.563 35.200  2.125   1.00 41.87  ? 286 LEU   C CA    1 
ATOM   5717  C  C     . LEU   B 1  286 ? -10.870 36.140  3.103   1.00 38.75  ? 286 LEU   C C     1 
ATOM   5718  O  O     . LEU   B 1  286 ? -10.095 37.012  2.696   1.00 39.47  ? 286 LEU   C O     1 
ATOM   5719  C  CB    . LEU   B 1  286 ? -10.570 34.440  1.243   1.00 49.58  ? 286 LEU   C CB    1 
ATOM   5720  C  CG    . LEU   B 1  286 ? -11.145 33.965  -0.118  1.00 48.26  ? 286 LEU   C CG    1 
ATOM   5721  C  CD1   . LEU   B 1  286 ? -11.025 35.018  -1.258  1.00 26.68  ? 286 LEU   C CD1   1 
ATOM   5722  C  CD2   . LEU   B 1  286 ? -10.597 32.599  -0.549  1.00 38.88  ? 286 LEU   C CD2   1 
ATOM   5723  N  N     . SER   B 1  287 ? -11.169 35.972  4.381   1.00 33.24  ? 287 SER   C N     1 
ATOM   5724  C  CA    . SER   B 1  287 ? -10.806 36.906  5.432   1.00 29.26  ? 287 SER   C CA    1 
ATOM   5725  C  C     . SER   B 1  287 ? -9.432  36.601  6.004   1.00 31.56  ? 287 SER   C C     1 
ATOM   5726  O  O     . SER   B 1  287 ? -8.932  35.480  5.908   1.00 31.45  ? 287 SER   C O     1 
ATOM   5727  C  CB    . SER   B 1  287 ? -11.811 36.820  6.560   1.00 36.03  ? 287 SER   C CB    1 
ATOM   5728  O  OG    . SER   B 1  287 ? -11.543 35.631  7.290   1.00 37.84  ? 287 SER   C OG    1 
ATOM   5729  N  N     . VAL   B 1  288 ? -8.858  37.606  6.677   1.00 31.84  ? 288 VAL   C N     1 
ATOM   5730  C  CA    . VAL   B 1  288 ? -7.558  37.442  7.325   1.00 30.02  ? 288 VAL   C CA    1 
ATOM   5731  C  C     . VAL   B 1  288 ? -7.557  36.226  8.256   1.00 34.99  ? 288 VAL   C C     1 
ATOM   5732  O  O     . VAL   B 1  288 ? -6.552  35.511  8.366   1.00 33.86  ? 288 VAL   C O     1 
ATOM   5733  C  CB    . VAL   B 1  288 ? -7.172  38.740  8.060   1.00 24.77  ? 288 VAL   C CB    1 
ATOM   5734  C  CG1   . VAL   B 1  288 ? -6.006  38.520  9.009   1.00 19.42  ? 288 VAL   C CG1   1 
ATOM   5735  C  CG2   . VAL   B 1  288 ? -6.831  39.792  7.052   1.00 27.13  ? 288 VAL   C CG2   1 
ATOM   5736  N  N     . ALA   B 1  289 ? -8.690  35.946  8.915   1.00 35.49  ? 289 ALA   C N     1 
ATOM   5737  C  CA    . ALA   B 1  289 ? -8.763  34.766  9.778   1.00 29.89  ? 289 ALA   C CA    1 
ATOM   5738  C  C     . ALA   B 1  289 ? -8.784  33.468  8.972   1.00 35.53  ? 289 ALA   C C     1 
ATOM   5739  O  O     . ALA   B 1  289 ? -8.211  32.454  9.392   1.00 36.05  ? 289 ALA   C O     1 
ATOM   5740  C  CB    . ALA   B 1  289 ? -9.993  34.852  10.672  1.00 28.05  ? 289 ALA   C CB    1 
ATOM   5741  N  N     . GLU   B 1  290 ? -9.410  33.478  7.801   1.00 38.33  ? 290 GLU   C N     1 
ATOM   5742  C  CA    . GLU   B 1  290 ? -9.507  32.241  7.035   1.00 37.53  ? 290 GLU   C CA    1 
ATOM   5743  C  C     . GLU   B 1  290 ? -8.165  31.864  6.425   1.00 32.35  ? 290 GLU   C C     1 
ATOM   5744  O  O     . GLU   B 1  290 ? -7.796  30.682  6.407   1.00 36.41  ? 290 GLU   C O     1 
ATOM   5745  C  CB    . GLU   B 1  290 ? -10.584 32.378  5.959   1.00 36.07  ? 290 GLU   C CB    1 
ATOM   5746  C  CG    . GLU   B 1  290 ? -11.864 32.984  6.502   1.00 41.69  ? 290 GLU   C CG    1 
ATOM   5747  C  CD    . GLU   B 1  290 ? -12.982 33.019  5.495   1.00 45.72  ? 290 GLU   C CD    1 
ATOM   5748  O  OE1   . GLU   B 1  290 ? -12.748 33.429  4.332   1.00 61.84  ? 290 GLU   C OE1   1 
ATOM   5749  O  OE2   . GLU   B 1  290 ? -14.102 32.629  5.879   1.00 44.46  ? 290 GLU   C OE2   1 
ATOM   5750  N  N     . ILE   B 1  291 ? -7.418  32.857  5.929   1.00 30.06  ? 291 ILE   C N     1 
ATOM   5751  C  CA    . ILE   B 1  291 ? -6.126  32.591  5.300   1.00 26.43  ? 291 ILE   C CA    1 
ATOM   5752  C  C     . ILE   B 1  291 ? -5.047  32.319  6.340   1.00 28.00  ? 291 ILE   C C     1 
ATOM   5753  O  O     . ILE   B 1  291 ? -4.090  31.590  6.064   1.00 23.21  ? 291 ILE   C O     1 
ATOM   5754  C  CB    . ILE   B 1  291 ? -5.717  33.752  4.373   1.00 29.76  ? 291 ILE   C CB    1 
ATOM   5755  C  CG1   . ILE   B 1  291 ? -5.552  35.061  5.151   1.00 19.41  ? 291 ILE   C CG1   1 
ATOM   5756  C  CG2   . ILE   B 1  291 ? -6.709  33.896  3.237   1.00 22.89  ? 291 ILE   C CG2   1 
ATOM   5757  C  CD1   . ILE   B 1  291 ? -5.187  36.198  4.260   1.00 22.13  ? 291 ILE   C CD1   1 
ATOM   5758  N  N     . THR   B 1  292 ? -5.172  32.889  7.546   1.00 32.33  ? 292 THR   C N     1 
ATOM   5759  C  CA    . THR   B 1  292 ? -4.265  32.516  8.632   1.00 27.07  ? 292 THR   C CA    1 
ATOM   5760  C  C     . THR   B 1  292 ? -4.472  31.065  9.053   1.00 25.22  ? 292 THR   C C     1 
ATOM   5761  O  O     . THR   B 1  292 ? -3.506  30.317  9.226   1.00 25.17  ? 292 THR   C O     1 
ATOM   5762  C  CB    . THR   B 1  292 ? -4.443  33.434  9.837   1.00 25.63  ? 292 THR   C CB    1 
ATOM   5763  O  OG1   . THR   B 1  292 ? -4.168  34.789  9.470   1.00 30.02  ? 292 THR   C OG1   1 
ATOM   5764  C  CG2   . THR   B 1  292 ? -3.474  33.023  10.904  1.00 29.86  ? 292 THR   C CG2   1 
ATOM   5765  N  N     . ASN   B 1  293 ? -5.730  30.648  9.232   1.00 24.93  ? 293 ASN   C N     1 
ATOM   5766  C  CA    . ASN   B 1  293 ? -6.003  29.243  9.521   1.00 24.58  ? 293 ASN   C CA    1 
ATOM   5767  C  C     . ASN   B 1  293 ? -5.442  28.340  8.429   1.00 28.18  ? 293 ASN   C C     1 
ATOM   5768  O  O     . ASN   B 1  293 ? -4.759  27.348  8.715   1.00 30.71  ? 293 ASN   C O     1 
ATOM   5769  C  CB    . ASN   B 1  293 ? -7.504  29.017  9.681   1.00 26.66  ? 293 ASN   C CB    1 
ATOM   5770  C  CG    . ASN   B 1  293 ? -8.057  29.601  10.970  1.00 51.11  ? 293 ASN   C CG    1 
ATOM   5771  O  OD1   . ASN   B 1  293 ? -7.377  29.626  12.003  1.00 52.13  ? 293 ASN   C OD1   1 
ATOM   5772  N  ND2   . ASN   B 1  293 ? -9.304  30.078  10.918  1.00 49.36  ? 293 ASN   C ND2   1 
ATOM   5773  N  N     . ALA   B 1  294 ? -5.745  28.653  7.170   1.00 22.92  ? 294 ALA   C N     1 
ATOM   5774  C  CA    . ALA   B 1  294 ? -5.175  27.968  6.017   1.00 22.32  ? 294 ALA   C CA    1 
ATOM   5775  C  C     . ALA   B 1  294 ? -3.701  27.623  6.191   1.00 29.94  ? 294 ALA   C C     1 
ATOM   5776  O  O     . ALA   B 1  294 ? -3.285  26.517  5.839   1.00 31.57  ? 294 ALA   C O     1 
ATOM   5777  C  CB    . ALA   B 1  294 ? -5.350  28.822  4.769   1.00 20.14  ? 294 ALA   C CB    1 
ATOM   5778  N  N     . CYS   B 1  295 ? -2.905  28.556  6.738   1.00 31.94  ? 295 CYS   C N     1 
ATOM   5779  C  CA    . CYS   B 1  295 ? -1.462  28.350  6.863   1.00 23.61  ? 295 CYS   C CA    1 
ATOM   5780  C  C     . CYS   B 1  295 ? -1.093  27.203  7.785   1.00 24.52  ? 295 CYS   C C     1 
ATOM   5781  O  O     . CYS   B 1  295 ? 0.062   26.775  7.751   1.00 30.85  ? 295 CYS   C O     1 
ATOM   5782  C  CB    . CYS   B 1  295 ? -0.773  29.608  7.377   1.00 25.06  ? 295 CYS   C CB    1 
ATOM   5783  S  SG    . CYS   B 1  295 ? -1.008  31.037  6.339   1.00 35.79  ? 295 CYS   C SG    1 
ATOM   5784  N  N     . PHE   B 1  296 ? -2.027  26.710  8.608   1.00 21.98  ? 296 PHE   C N     1 
ATOM   5785  C  CA    . PHE   B 1  296 ? -1.755  25.684  9.607   1.00 21.19  ? 296 PHE   C CA    1 
ATOM   5786  C  C     . PHE   B 1  296 ? -2.442  24.362  9.308   1.00 27.09  ? 296 PHE   C C     1 
ATOM   5787  O  O     . PHE   B 1  296 ? -2.358  23.441  10.122  1.00 27.04  ? 296 PHE   C O     1 
ATOM   5788  C  CB    . PHE   B 1  296 ? -2.145  26.180  11.003  1.00 25.70  ? 296 PHE   C CB    1 
ATOM   5789  C  CG    . PHE   B 1  296 ? -1.184  27.185  11.566  1.00 29.63  ? 296 PHE   C CG    1 
ATOM   5790  C  CD1   . PHE   B 1  296 ? 0.024   26.768  12.127  1.00 27.09  ? 296 PHE   C CD1   1 
ATOM   5791  C  CD2   . PHE   B 1  296 ? -1.454  28.540  11.502  1.00 20.74  ? 296 PHE   C CD2   1 
ATOM   5792  C  CE1   . PHE   B 1  296 ? 0.940   27.686  12.629  1.00 21.44  ? 296 PHE   C CE1   1 
ATOM   5793  C  CE2   . PHE   B 1  296 ? -0.545  29.458  12.007  1.00 22.36  ? 296 PHE   C CE2   1 
ATOM   5794  C  CZ    . PHE   B 1  296 ? 0.649   29.031  12.576  1.00 22.75  ? 296 PHE   C CZ    1 
ATOM   5795  N  N     . GLU   B 1  297 ? -3.138  24.257  8.179   1.00 33.54  ? 297 GLU   C N     1 
ATOM   5796  C  CA    . GLU   B 1  297 ? -3.528  22.956  7.627   1.00 33.11  ? 297 GLU   C CA    1 
ATOM   5797  C  C     . GLU   B 1  297 ? -2.311  22.312  6.973   1.00 37.24  ? 297 GLU   C C     1 
ATOM   5798  O  O     . GLU   B 1  297 ? -1.704  22.928  6.086   1.00 34.49  ? 297 GLU   C O     1 
ATOM   5799  C  CB    . GLU   B 1  297 ? -4.625  23.118  6.579   1.00 33.64  ? 297 GLU   C CB    1 
ATOM   5800  C  CG    . GLU   B 1  297 ? -5.810  23.968  6.991   1.00 45.74  ? 297 GLU   C CG    1 
ATOM   5801  C  CD    . GLU   B 1  297 ? -6.692  23.267  8.007   1.00 58.28  ? 297 GLU   C CD    1 
ATOM   5802  O  OE1   . GLU   B 1  297 ? -6.753  22.011  7.984   1.00 53.07  ? 297 GLU   C OE1   1 
ATOM   5803  O  OE2   . GLU   B 1  297 ? -7.309  23.978  8.835   1.00 54.29  ? 297 GLU   C OE2   1 
ATOM   5804  N  N     . PRO   B 1  298 ? -1.910  21.097  7.362   1.00 34.61  ? 298 PRO   C N     1 
ATOM   5805  C  CA    . PRO   B 1  298 ? -0.692  20.533  6.767   1.00 33.57  ? 298 PRO   C CA    1 
ATOM   5806  C  C     . PRO   B 1  298 ? -0.783  20.339  5.258   1.00 34.54  ? 298 PRO   C C     1 
ATOM   5807  O  O     . PRO   B 1  298 ? 0.254   20.167  4.614   1.00 43.20  ? 298 PRO   C O     1 
ATOM   5808  C  CB    . PRO   B 1  298 ? -0.510  19.211  7.520   1.00 35.76  ? 298 PRO   C CB    1 
ATOM   5809  C  CG    . PRO   B 1  298 ? -1.085  19.497  8.870   1.00 37.12  ? 298 PRO   C CG    1 
ATOM   5810  C  CD    . PRO   B 1  298 ? -2.348  20.293  8.515   1.00 45.50  ? 298 PRO   C CD    1 
ATOM   5811  N  N     . ALA   B 1  299 ? -1.961  20.427  4.656   1.00 32.23  ? 299 ALA   C N     1 
ATOM   5812  C  CA    . ALA   B 1  299 ? -2.083  20.221  3.222   1.00 31.83  ? 299 ALA   C CA    1 
ATOM   5813  C  C     . ALA   B 1  299 ? -2.043  21.518  2.429   1.00 35.91  ? 299 ALA   C C     1 
ATOM   5814  O  O     . ALA   B 1  299 ? -2.530  21.553  1.292   1.00 40.01  ? 299 ALA   C O     1 
ATOM   5815  C  CB    . ALA   B 1  299 ? -3.368  19.456  2.907   1.00 43.11  ? 299 ALA   C CB    1 
ATOM   5816  N  N     . ASN   B 1  300 ? -1.519  22.596  3.007   1.00 34.82  ? 300 ASN   C N     1 
ATOM   5817  C  CA    . ASN   B 1  300 ? -1.221  23.796  2.234   1.00 32.99  ? 300 ASN   C CA    1 
ATOM   5818  C  C     . ASN   B 1  300 ? 0.274   24.069  2.157   1.00 35.16  ? 300 ASN   C C     1 
ATOM   5819  O  O     . ASN   B 1  300 ? 0.676   25.178  1.798   1.00 40.19  ? 300 ASN   C O     1 
ATOM   5820  C  CB    . ASN   B 1  300 ? -1.922  25.018  2.814   1.00 29.86  ? 300 ASN   C CB    1 
ATOM   5821  C  CG    . ASN   B 1  300 ? -3.368  25.047  2.505   1.00 27.03  ? 300 ASN   C CG    1 
ATOM   5822  O  OD1   . ASN   B 1  300 ? -3.814  24.525  1.491   1.00 30.96  ? 300 ASN   C OD1   1 
ATOM   5823  N  ND2   . ASN   B 1  300 ? -4.127  25.682  3.371   1.00 35.91  ? 300 ASN   C ND2   1 
ATOM   5824  N  N     . GLN   B 1  301 ? 1.100   23.084  2.495   1.00 29.92  ? 301 GLN   C N     1 
ATOM   5825  C  CA    . GLN   B 1  301 ? 2.522   23.301  2.650   1.00 30.07  ? 301 GLN   C CA    1 
ATOM   5826  C  C     . GLN   B 1  301 ? 3.237   23.137  1.317   1.00 33.82  ? 301 GLN   C C     1 
ATOM   5827  O  O     . GLN   B 1  301 ? 2.727   22.488  0.403   1.00 42.14  ? 301 GLN   C O     1 
ATOM   5828  C  CB    . GLN   B 1  301 ? 3.057   22.348  3.711   1.00 23.81  ? 301 GLN   C CB    1 
ATOM   5829  C  CG    . GLN   B 1  301 ? 2.631   22.845  5.093   1.00 31.69  ? 301 GLN   C CG    1 
ATOM   5830  C  CD    . GLN   B 1  301 ? 2.642   21.779  6.169   1.00 34.73  ? 301 GLN   C CD    1 
ATOM   5831  O  OE1   . GLN   B 1  301 ? 2.408   22.062  7.352   1.00 37.59  ? 301 GLN   C OE1   1 
ATOM   5832  N  NE2   . GLN   B 1  301 ? 2.898   20.546  5.769   1.00 29.64  ? 301 GLN   C NE2   1 
ATOM   5833  N  N     . MET   B 1  302 ? 4.391   23.807  1.180   1.00 35.21  ? 302 MET   C N     1 
ATOM   5834  C  CA    . MET   B 1  302 ? 5.261   23.576  0.027   1.00 23.82  ? 302 MET   C CA    1 
ATOM   5835  C  C     . MET   B 1  302 ? 6.048   22.298  0.174   1.00 23.24  ? 302 MET   C C     1 
ATOM   5836  O  O     . MET   B 1  302 ? 6.508   21.764  -0.834  1.00 28.72  ? 302 MET   C O     1 
ATOM   5837  C  CB    . MET   B 1  302 ? 6.265   24.712  -0.184  1.00 25.67  ? 302 MET   C CB    1 
ATOM   5838  C  CG    . MET   B 1  302 ? 5.748   25.924  -0.931  1.00 34.31  ? 302 MET   C CG    1 
ATOM   5839  S  SD    . MET   B 1  302 ? 4.161   26.497  -0.255  1.00 68.56  ? 302 MET   C SD    1 
ATOM   5840  C  CE    . MET   B 1  302 ? 3.021   25.936  -1.515  1.00 35.13  ? 302 MET   C CE    1 
ATOM   5841  N  N     . VAL   B 1  303 ? 6.229   21.809  1.395   1.00 17.92  ? 303 VAL   C N     1 
ATOM   5842  C  CA    . VAL   B 1  303 ? 6.889   20.530  1.634   1.00 28.09  ? 303 VAL   C CA    1 
ATOM   5843  C  C     . VAL   B 1  303 ? 5.951   19.651  2.447   1.00 26.29  ? 303 VAL   C C     1 
ATOM   5844  O  O     . VAL   B 1  303 ? 5.397   20.099  3.458   1.00 29.34  ? 303 VAL   C O     1 
ATOM   5845  C  CB    . VAL   B 1  303 ? 8.244   20.698  2.352   1.00 21.79  ? 303 VAL   C CB    1 
ATOM   5846  C  CG1   . VAL   B 1  303 ? 8.869   19.325  2.639   1.00 17.14  ? 303 VAL   C CG1   1 
ATOM   5847  C  CG2   . VAL   B 1  303 ? 9.178   21.565  1.516   1.00 19.53  ? 303 VAL   C CG2   1 
ATOM   5848  N  N     . LYS   B 1  304 ? 5.790   18.403  2.008   1.00 21.06  ? 304 LYS   C N     1 
ATOM   5849  C  CA    . LYS   B 1  304 ? 4.956   17.416  2.684   1.00 15.91  ? 304 LYS   C CA    1 
ATOM   5850  C  C     . LYS   B 1  304 ? 5.677   16.843  3.902   1.00 20.15  ? 304 LYS   C C     1 
ATOM   5851  O  O     . LYS   B 1  304 ? 6.735   16.222  3.763   1.00 22.43  ? 304 LYS   C O     1 
ATOM   5852  C  CB    . LYS   B 1  304 ? 4.574   16.302  1.708   1.00 18.22  ? 304 LYS   C CB    1 
ATOM   5853  C  CG    . LYS   B 1  304 ? 3.399   16.628  0.774   1.00 17.88  ? 304 LYS   C CG    1 
ATOM   5854  C  CD    . LYS   B 1  304 ? 3.154   15.538  -0.276  1.00 24.53  ? 304 LYS   C CD    1 
ATOM   5855  C  CE    . LYS   B 1  304 ? 1.675   15.289  -0.544  1.00 25.18  ? 304 LYS   C CE    1 
ATOM   5856  N  NZ    . LYS   B 1  304 ? 1.315   13.904  -0.066  1.00 34.21  ? 304 LYS   C NZ    1 
ATOM   5857  N  N     . CYS   B 1  305 ? 5.063   17.008  5.081   1.00 17.37  ? 305 CYS   C N     1 
ATOM   5858  C  CA    . CYS   B 1  305 ? 5.569   16.706  6.419   1.00 18.75  ? 305 CYS   C CA    1 
ATOM   5859  C  C     . CYS   B 1  305 ? 4.438   17.079  7.378   1.00 25.06  ? 305 CYS   C C     1 
ATOM   5860  O  O     . CYS   B 1  305 ? 3.439   17.667  6.949   1.00 25.46  ? 305 CYS   C O     1 
ATOM   5861  C  CB    . CYS   B 1  305 ? 6.837   17.497  6.739   1.00 19.24  ? 305 CYS   C CB    1 
ATOM   5862  S  SG    . CYS   B 1  305 ? 6.565   19.300  6.800   1.00 22.09  ? 305 CYS   C SG    1 
ATOM   5863  N  N     . ASP   B 1  306 ? 4.586   16.752  8.671   1.00 17.01  ? 306 ASP   C N     1 
ATOM   5864  C  CA    . ASP   B 1  306 ? 3.537   17.115  9.631   1.00 28.76  ? 306 ASP   C CA    1 
ATOM   5865  C  C     . ASP   B 1  306 ? 4.023   17.993  10.770  1.00 31.56  ? 306 ASP   C C     1 
ATOM   5866  O  O     . ASP   B 1  306 ? 4.505   17.485  11.799  1.00 29.99  ? 306 ASP   C O     1 
ATOM   5867  C  CB    . ASP   B 1  306 ? 2.835   15.895  10.208  1.00 34.18  ? 306 ASP   C CB    1 
ATOM   5868  C  CG    . ASP   B 1  306 ? 1.490   16.261  10.831  1.00 46.37  ? 306 ASP   C CG    1 
ATOM   5869  O  OD1   . ASP   B 1  306 ? 1.060   17.444  10.702  1.00 45.26  ? 306 ASP   C OD1   1 
ATOM   5870  O  OD2   . ASP   B 1  306 ? 0.853   15.374  11.438  1.00 55.55  ? 306 ASP   C OD2   1 
ATOM   5871  N  N     . PRO   B 1  307 ? 3.830   19.304  10.665  1.00 30.36  ? 307 PRO   C N     1 
ATOM   5872  C  CA    . PRO   B 1  307 ? 4.308   20.210  11.715  1.00 31.59  ? 307 PRO   C CA    1 
ATOM   5873  C  C     . PRO   B 1  307 ? 3.569   20.070  13.044  1.00 39.68  ? 307 PRO   C C     1 
ATOM   5874  O  O     . PRO   B 1  307 ? 4.142   20.453  14.081  1.00 37.24  ? 307 PRO   C O     1 
ATOM   5875  C  CB    . PRO   B 1  307 ? 4.084   21.586  11.095  1.00 26.36  ? 307 PRO   C CB    1 
ATOM   5876  C  CG    . PRO   B 1  307 ? 2.956   21.348  10.100  1.00 27.90  ? 307 PRO   C CG    1 
ATOM   5877  C  CD    . PRO   B 1  307 ? 3.177   20.010  9.551   1.00 23.39  ? 307 PRO   C CD    1 
ATOM   5878  N  N     . ARG   B 1  308 ? 2.319   19.562  13.040  1.00 36.16  ? 308 ARG   C N     1 
ATOM   5879  C  CA    . ARG   B 1  308 ? 1.554   19.350  14.271  1.00 38.13  ? 308 ARG   C CA    1 
ATOM   5880  C  C     . ARG   B 1  308 ? 2.125   18.220  15.101  1.00 40.09  ? 308 ARG   C C     1 
ATOM   5881  O  O     . ARG   B 1  308 ? 1.766   18.104  16.279  1.00 52.36  ? 308 ARG   C O     1 
ATOM   5882  C  CB    . ARG   B 1  308 ? 0.070   19.029  14.012  1.00 35.28  ? 308 ARG   C CB    1 
ATOM   5883  C  CG    . ARG   B 1  308 ? -0.580  19.672  12.772  1.00 48.94  ? 308 ARG   C CG    1 
ATOM   5884  C  CD    . ARG   B 1  308 ? -2.005  19.116  12.511  1.00 64.05  ? 308 ARG   C CD    1 
ATOM   5885  N  NE    . ARG   B 1  308 ? -2.058  17.692  12.164  1.00 72.65  ? 308 ARG   C NE    1 
ATOM   5886  C  CZ    . ARG   B 1  308 ? -2.064  16.685  13.039  1.00 64.55  ? 308 ARG   C CZ    1 
ATOM   5887  N  NH1   . ARG   B 1  308 ? -1.960  16.893  14.348  1.00 53.15  ? 308 ARG   C NH1   1 
ATOM   5888  N  NH2   . ARG   B 1  308 ? -2.173  15.434  12.591  1.00 50.59  ? 308 ARG   C NH2   1 
ATOM   5889  N  N     . HIS   B 1  309 ? 2.983   17.388  14.510  1.00 33.60  ? 309 HIS   C N     1 
ATOM   5890  C  CA    . HIS   B 1  309 ? 3.710   16.348  15.223  1.00 36.06  ? 309 HIS   C CA    1 
ATOM   5891  C  C     . HIS   B 1  309 ? 5.205   16.653  15.271  1.00 36.09  ? 309 HIS   C C     1 
ATOM   5892  O  O     . HIS   B 1  309 ? 6.043   15.744  15.198  1.00 33.66  ? 309 HIS   C O     1 
ATOM   5893  C  CB    . HIS   B 1  309 ? 3.441   14.974  14.605  1.00 39.34  ? 309 HIS   C CB    1 
ATOM   5894  C  CG    . HIS   B 1  309 ? 2.099   14.397  14.971  1.00 56.24  ? 309 HIS   C CG    1 
ATOM   5895  N  ND1   . HIS   B 1  309 ? 1.299   13.725  14.068  1.00 52.03  ? 309 HIS   C ND1   1 
ATOM   5896  C  CD2   . HIS   B 1  309 ? 1.422   14.388  16.149  1.00 52.01  ? 309 HIS   C CD2   1 
ATOM   5897  C  CE1   . HIS   B 1  309 ? 0.184   13.341  14.670  1.00 54.47  ? 309 HIS   C CE1   1 
ATOM   5898  N  NE2   . HIS   B 1  309 ? 0.231   13.735  15.932  1.00 54.84  ? 309 HIS   C NE2   1 
ATOM   5899  N  N     . GLY   B 1  310 ? 5.537   17.939  15.389  1.00 29.96  ? 310 GLY   C N     1 
ATOM   5900  C  CA    . GLY   B 1  310 ? 6.887   18.417  15.627  1.00 30.00  ? 310 GLY   C CA    1 
ATOM   5901  C  C     . GLY   B 1  310 ? 6.823   19.789  16.262  1.00 35.29  ? 310 GLY   C C     1 
ATOM   5902  O  O     . GLY   B 1  310 ? 5.741   20.330  16.494  1.00 45.83  ? 310 GLY   C O     1 
ATOM   5903  N  N     . LYS   B 1  311 ? 7.990   20.368  16.535  1.00 23.38  ? 311 LYS   C N     1 
ATOM   5904  C  CA    . LYS   B 1  311 ? 8.040   21.608  17.290  1.00 28.86  ? 311 LYS   C CA    1 
ATOM   5905  C  C     . LYS   B 1  311 ? 8.420   22.776  16.396  1.00 25.12  ? 311 LYS   C C     1 
ATOM   5906  O  O     . LYS   B 1  311 ? 9.303   22.661  15.546  1.00 26.84  ? 311 LYS   C O     1 
ATOM   5907  C  CB    . LYS   B 1  311 ? 9.008   21.486  18.465  1.00 29.53  ? 311 LYS   C CB    1 
ATOM   5908  C  CG    . LYS   B 1  311 ? 8.491   20.527  19.545  1.00 35.09  ? 311 LYS   C CG    1 
ATOM   5909  C  CD    . LYS   B 1  311 ? 9.408   20.426  20.730  1.00 31.89  ? 311 LYS   C CD    1 
ATOM   5910  C  CE    . LYS   B 1  311 ? 9.033   19.265  21.608  1.00 36.54  ? 311 LYS   C CE    1 
ATOM   5911  N  NZ    . LYS   B 1  311 ? 9.658   19.365  22.968  1.00 42.01  ? 311 LYS   C NZ    1 
ATOM   5912  N  N     . TYR   B 1  312 ? 7.731   23.896  16.602  1.00 34.14  ? 312 TYR   C N     1 
ATOM   5913  C  CA    . TYR   B 1  312 ? 8.044   25.156  15.946  1.00 25.42  ? 312 TYR   C CA    1 
ATOM   5914  C  C     . TYR   B 1  312 ? 9.195   25.841  16.653  1.00 26.27  ? 312 TYR   C C     1 
ATOM   5915  O  O     . TYR   B 1  312 ? 9.173   25.992  17.875  1.00 24.49  ? 312 TYR   C O     1 
ATOM   5916  C  CB    . TYR   B 1  312 ? 6.833   26.086  15.963  1.00 24.02  ? 312 TYR   C CB    1 
ATOM   5917  C  CG    . TYR   B 1  312 ? 5.742   25.676  15.021  1.00 26.81  ? 312 TYR   C CG    1 
ATOM   5918  C  CD1   . TYR   B 1  312 ? 4.770   24.779  15.418  1.00 33.94  ? 312 TYR   C CD1   1 
ATOM   5919  C  CD2   . TYR   B 1  312 ? 5.683   26.182  13.734  1.00 24.92  ? 312 TYR   C CD2   1 
ATOM   5920  C  CE1   . TYR   B 1  312 ? 3.777   24.393  14.570  1.00 38.42  ? 312 TYR   C CE1   1 
ATOM   5921  C  CE2   . TYR   B 1  312 ? 4.677   25.807  12.874  1.00 27.27  ? 312 TYR   C CE2   1 
ATOM   5922  C  CZ    . TYR   B 1  312 ? 3.722   24.905  13.300  1.00 27.86  ? 312 TYR   C CZ    1 
ATOM   5923  O  OH    . TYR   B 1  312 ? 2.704   24.491  12.472  1.00 25.05  ? 312 TYR   C OH    1 
ATOM   5924  N  N     . MET   B 1  313 ? 10.187  26.270  15.879  1.00 23.53  ? 313 MET   C N     1 
ATOM   5925  C  CA    . MET   B 1  313 ? 11.263  27.121  16.357  1.00 19.56  ? 313 MET   C CA    1 
ATOM   5926  C  C     . MET   B 1  313 ? 11.103  28.557  15.901  1.00 23.26  ? 313 MET   C C     1 
ATOM   5927  O  O     . MET   B 1  313 ? 11.948  29.402  16.217  1.00 26.80  ? 313 MET   C O     1 
ATOM   5928  C  CB    . MET   B 1  313 ? 12.602  26.587  15.874  1.00 16.92  ? 313 MET   C CB    1 
ATOM   5929  C  CG    . MET   B 1  313 ? 13.061  25.430  16.651  1.00 18.72  ? 313 MET   C CG    1 
ATOM   5930  S  SD    . MET   B 1  313 ? 14.280  24.520  15.747  1.00 26.86  ? 313 MET   C SD    1 
ATOM   5931  C  CE    . MET   B 1  313 ? 13.185  23.764  14.561  1.00 21.06  ? 313 MET   C CE    1 
ATOM   5932  N  N     . ALA   B 1  314 ? 10.051  28.847  15.148  1.00 28.89  ? 314 ALA   C N     1 
ATOM   5933  C  CA    . ALA   B 1  314 ? 9.772   30.168  14.611  1.00 20.80  ? 314 ALA   C CA    1 
ATOM   5934  C  C     . ALA   B 1  314 ? 8.583   30.016  13.694  1.00 23.08  ? 314 ALA   C C     1 
ATOM   5935  O  O     . ALA   B 1  314 ? 8.297   28.927  13.188  1.00 21.99  ? 314 ALA   C O     1 
ATOM   5936  C  CB    . ALA   B 1  314 ? 10.937  30.754  13.842  1.00 20.51  ? 314 ALA   C CB    1 
ATOM   5937  N  N     . CYS   B 1  315 ? 7.912   31.131  13.466  1.00 31.17  ? 315 CYS   C N     1 
ATOM   5938  C  CA    . CYS   B 1  315 ? 6.669   31.115  12.719  1.00 23.60  ? 315 CYS   C CA    1 
ATOM   5939  C  C     . CYS   B 1  315 ? 6.432   32.538  12.236  1.00 21.40  ? 315 CYS   C C     1 
ATOM   5940  O  O     . CYS   B 1  315 ? 6.116   33.423  13.037  1.00 13.47  ? 315 CYS   C O     1 
ATOM   5941  C  CB    . CYS   B 1  315 ? 5.546   30.609  13.603  1.00 24.16  ? 315 CYS   C CB    1 
ATOM   5942  S  SG    . CYS   B 1  315 ? 4.145   30.169  12.663  1.00 42.98  ? 315 CYS   C SG    1 
ATOM   5943  N  N     . CYS   B 1  316 ? 6.626   32.755  10.939  1.00 22.23  ? 316 CYS   C N     1 
ATOM   5944  C  CA    . CYS   B 1  316 ? 6.544   34.078  10.337  1.00 21.03  ? 316 CYS   C CA    1 
ATOM   5945  C  C     . CYS   B 1  316 ? 5.416   34.119  9.317   1.00 25.19  ? 316 CYS   C C     1 
ATOM   5946  O  O     . CYS   B 1  316 ? 5.379   33.317  8.373   1.00 25.29  ? 316 CYS   C O     1 
ATOM   5947  C  CB    . CYS   B 1  316 ? 7.859   34.486  9.654   1.00 19.21  ? 316 CYS   C CB    1 
ATOM   5948  S  SG    . CYS   B 1  316 ? 9.305   34.467  10.704  1.00 18.66  ? 316 CYS   C SG    1 
ATOM   5949  N  N     . LEU   B 1  317 ? 4.531   35.088  9.489   1.00 21.32  ? 317 LEU   C N     1 
ATOM   5950  C  CA    . LEU   B 1  317 ? 3.402   35.307  8.610   1.00 19.67  ? 317 LEU   C CA    1 
ATOM   5951  C  C     . LEU   B 1  317 ? 3.665   36.567  7.802   1.00 19.54  ? 317 LEU   C C     1 
ATOM   5952  O  O     . LEU   B 1  317 ? 3.788   37.656  8.363   1.00 19.21  ? 317 LEU   C O     1 
ATOM   5953  C  CB    . LEU   B 1  317 ? 2.116   35.429  9.429   1.00 26.04  ? 317 LEU   C CB    1 
ATOM   5954  C  CG    . LEU   B 1  317 ? 1.725   34.187  10.220  1.00 18.49  ? 317 LEU   C CG    1 
ATOM   5955  C  CD1   . LEU   B 1  317 ? 1.017   34.644  11.400  1.00 14.44  ? 317 LEU   C CD1   1 
ATOM   5956  C  CD2   . LEU   B 1  317 ? 0.835   33.271  9.381   1.00 19.77  ? 317 LEU   C CD2   1 
ATOM   5957  N  N     . LEU   B 1  318 ? 3.739   36.421  6.487   1.00 29.02  ? 318 LEU   C N     1 
ATOM   5958  C  CA    . LEU   B 1  318 ? 3.958   37.543  5.579   1.00 24.19  ? 318 LEU   C CA    1 
ATOM   5959  C  C     . LEU   B 1  318 ? 2.644   37.807  4.853   1.00 23.89  ? 318 LEU   C C     1 
ATOM   5960  O  O     . LEU   B 1  318 ? 2.339   37.146  3.864   1.00 26.14  ? 318 LEU   C O     1 
ATOM   5961  C  CB    . LEU   B 1  318 ? 5.090   37.243  4.605   1.00 15.90  ? 318 LEU   C CB    1 
ATOM   5962  C  CG    . LEU   B 1  318 ? 6.494   36.993  5.120   1.00 17.75  ? 318 LEU   C CG    1 
ATOM   5963  C  CD1   . LEU   B 1  318 ? 6.496   36.174  6.395   1.00 20.73  ? 318 LEU   C CD1   1 
ATOM   5964  C  CD2   . LEU   B 1  318 ? 7.241   36.243  4.044   1.00 20.80  ? 318 LEU   C CD2   1 
ATOM   5965  N  N     . TYR   B 1  319 ? 1.862   38.761  5.352   1.00 28.12  ? 319 TYR   C N     1 
ATOM   5966  C  CA    . TYR   B 1  319 ? 0.594   39.121  4.732   1.00 22.94  ? 319 TYR   C CA    1 
ATOM   5967  C  C     . TYR   B 1  319 ? 0.828   40.107  3.609   1.00 22.30  ? 319 TYR   C C     1 
ATOM   5968  O  O     . TYR   B 1  319 ? 1.784   40.889  3.642   1.00 27.72  ? 319 TYR   C O     1 
ATOM   5969  C  CB    . TYR   B 1  319 ? -0.354  39.761  5.752   1.00 21.24  ? 319 TYR   C CB    1 
ATOM   5970  C  CG    . TYR   B 1  319 ? -0.803  38.838  6.868   1.00 23.53  ? 319 TYR   C CG    1 
ATOM   5971  C  CD1   . TYR   B 1  319 ? -1.869  37.967  6.689   1.00 28.21  ? 319 TYR   C CD1   1 
ATOM   5972  C  CD2   . TYR   B 1  319 ? -0.163  38.830  8.096   1.00 19.43  ? 319 TYR   C CD2   1 
ATOM   5973  C  CE1   . TYR   B 1  319 ? -2.287  37.116  7.712   1.00 23.30  ? 319 TYR   C CE1   1 
ATOM   5974  C  CE2   . TYR   B 1  319 ? -0.581  37.991  9.123   1.00 22.78  ? 319 TYR   C CE2   1 
ATOM   5975  C  CZ    . TYR   B 1  319 ? -1.647  37.143  8.921   1.00 21.78  ? 319 TYR   C CZ    1 
ATOM   5976  O  OH    . TYR   B 1  319 ? -2.067  36.304  9.918   1.00 28.03  ? 319 TYR   C OH    1 
ATOM   5977  N  N     . ARG   B 1  320 ? -0.071  40.094  2.624   1.00 27.10  ? 320 ARG   C N     1 
ATOM   5978  C  CA    . ARG   B 1  320 ? -0.097  41.153  1.619   1.00 27.59  ? 320 ARG   C CA    1 
ATOM   5979  C  C     . ARG   B 1  320 ? -1.527  41.473  1.206   1.00 27.61  ? 320 ARG   C C     1 
ATOM   5980  O  O     . ARG   B 1  320 ? -2.371  40.572  1.072   1.00 26.90  ? 320 ARG   C O     1 
ATOM   5981  C  CB    . ARG   B 1  320 ? 0.742   40.798  0.376   1.00 27.35  ? 320 ARG   C CB    1 
ATOM   5982  C  CG    . ARG   B 1  320 ? 0.198   39.711  -0.485  1.00 25.54  ? 320 ARG   C CG    1 
ATOM   5983  C  CD    . ARG   B 1  320 ? 1.243   39.296  -1.488  1.00 33.36  ? 320 ARG   C CD    1 
ATOM   5984  N  NE    . ARG   B 1  320 ? 1.766   40.439  -2.223  1.00 33.44  ? 320 ARG   C NE    1 
ATOM   5985  C  CZ    . ARG   B 1  320 ? 2.611   40.339  -3.237  1.00 30.58  ? 320 ARG   C CZ    1 
ATOM   5986  N  NH1   . ARG   B 1  320 ? 3.071   39.167  -3.640  1.00 28.79  ? 320 ARG   C NH1   1 
ATOM   5987  N  NH2   . ARG   B 1  320 ? 2.993   41.438  -3.872  1.00 27.47  ? 320 ARG   C NH2   1 
ATOM   5988  N  N     . GLY   B 1  321 ? -1.778  42.775  1.019   1.00 24.98  ? 321 GLY   C N     1 
ATOM   5989  C  CA    . GLY   B 1  321 ? -3.038  43.306  0.534   1.00 28.06  ? 321 GLY   C CA    1 
ATOM   5990  C  C     . GLY   B 1  321 ? -3.950  43.863  1.613   1.00 30.21  ? 321 GLY   C C     1 
ATOM   5991  O  O     . GLY   B 1  321 ? -3.485  44.313  2.663   1.00 29.90  ? 321 GLY   C O     1 
ATOM   5992  N  N     . ASP   B 1  322 ? -5.261  43.815  1.375   1.00 31.67  ? 322 ASP   C N     1 
ATOM   5993  C  CA    . ASP   B 1  322 ? -6.215  44.329  2.341   1.00 29.38  ? 322 ASP   C CA    1 
ATOM   5994  C  C     . ASP   B 1  322 ? -6.068  43.565  3.648   1.00 24.37  ? 322 ASP   C C     1 
ATOM   5995  O  O     . ASP   B 1  322 ? -6.751  42.566  3.871   1.00 27.85  ? 322 ASP   C O     1 
ATOM   5996  C  CB    . ASP   B 1  322 ? -7.637  44.243  1.777   1.00 29.14  ? 322 ASP   C CB    1 
ATOM   5997  C  CG    . ASP   B 1  322 ? -8.678  44.821  2.716   1.00 39.48  ? 322 ASP   C CG    1 
ATOM   5998  O  OD1   . ASP   B 1  322 ? -8.379  45.825  3.394   1.00 46.77  ? 322 ASP   C OD1   1 
ATOM   5999  O  OD2   . ASP   B 1  322 ? -9.803  44.273  2.763   1.00 41.63  ? 322 ASP   C OD2   1 
ATOM   6000  N  N     . VAL   B 1  323 ? -5.146  44.012  4.493   1.00 24.27  ? 323 VAL   C N     1 
ATOM   6001  C  CA    . VAL   B 1  323 ? -4.903  43.409  5.800   1.00 28.74  ? 323 VAL   C CA    1 
ATOM   6002  C  C     . VAL   B 1  323 ? -4.488  44.503  6.776   1.00 32.34  ? 323 VAL   C C     1 
ATOM   6003  O  O     . VAL   B 1  323 ? -3.533  45.242  6.520   1.00 40.30  ? 323 VAL   C O     1 
ATOM   6004  C  CB    . VAL   B 1  323 ? -3.818  42.326  5.728   1.00 24.87  ? 323 VAL   C CB    1 
ATOM   6005  C  CG1   . VAL   B 1  323 ? -3.482  41.825  7.117   1.00 26.01  ? 323 VAL   C CG1   1 
ATOM   6006  C  CG2   . VAL   B 1  323 ? -4.277  41.188  4.854   1.00 28.25  ? 323 VAL   C CG2   1 
ATOM   6007  N  N     . VAL   B 1  324 ? -5.185  44.602  7.902   1.00 28.75  ? 324 VAL   C N     1 
ATOM   6008  C  CA    . VAL   B 1  324 ? -4.816  45.598  8.908   1.00 30.75  ? 324 VAL   C CA    1 
ATOM   6009  C  C     . VAL   B 1  324 ? -4.321  44.953  10.195  1.00 26.28  ? 324 VAL   C C     1 
ATOM   6010  O  O     . VAL   B 1  324 ? -4.810  43.882  10.590  1.00 22.97  ? 324 VAL   C O     1 
ATOM   6011  C  CB    . VAL   B 1  324 ? -6.000  46.503  9.250   1.00 34.92  ? 324 VAL   C CB    1 
ATOM   6012  C  CG1   . VAL   B 1  324 ? -6.299  47.418  8.119   1.00 17.84  ? 324 VAL   C CG1   1 
ATOM   6013  C  CG2   . VAL   B 1  324 ? -7.190  45.616  9.611   1.00 35.70  ? 324 VAL   C CG2   1 
ATOM   6014  N  N     . PRO   B 1  325 ? -3.408  45.604  10.901  1.00 27.01  ? 325 PRO   C N     1 
ATOM   6015  C  CA    . PRO   B 1  325 ? -2.938  45.079  12.191  1.00 23.68  ? 325 PRO   C CA    1 
ATOM   6016  C  C     . PRO   B 1  325 ? -4.030  44.455  13.022  1.00 24.42  ? 325 PRO   C C     1 
ATOM   6017  O  O     . PRO   B 1  325 ? -3.901  43.285  13.398  1.00 24.62  ? 325 PRO   C O     1 
ATOM   6018  C  CB    . PRO   B 1  325 ? -2.350  46.312  12.869  1.00 18.05  ? 325 PRO   C CB    1 
ATOM   6019  C  CG    . PRO   B 1  325 ? -1.732  47.059  11.703  1.00 20.04  ? 325 PRO   C CG    1 
ATOM   6020  C  CD    . PRO   B 1  325 ? -2.667  46.807  10.495  1.00 25.21  ? 325 PRO   C CD    1 
ATOM   6021  N  N     . LYS   B 1  326 ? -5.121  45.175  13.299  1.00 28.29  ? 326 LYS   C N     1 
ATOM   6022  C  CA    . LYS   B 1  326 ? -6.093  44.616  14.239  1.00 31.77  ? 326 LYS   C CA    1 
ATOM   6023  C  C     . LYS   B 1  326 ? -6.611  43.269  13.746  1.00 25.70  ? 326 LYS   C C     1 
ATOM   6024  O  O     . LYS   B 1  326 ? -6.840  42.359  14.549  1.00 25.34  ? 326 LYS   C O     1 
ATOM   6025  C  CB    . LYS   B 1  326 ? -7.243  45.593  14.505  1.00 25.51  ? 326 LYS   C CB    1 
ATOM   6026  C  CG    . LYS   B 1  326 ? -7.902  45.358  15.859  1.00 36.12  ? 326 LYS   C CG    1 
ATOM   6027  C  CD    . LYS   B 1  326 ? -9.228  46.109  16.024  1.00 51.64  ? 326 LYS   C CD    1 
ATOM   6028  C  CE    . LYS   B 1  326 ? -10.354 45.172  16.508  1.00 54.98  ? 326 LYS   C CE    1 
ATOM   6029  N  NZ    . LYS   B 1  326 ? -11.428 45.881  17.272  1.00 66.88  ? 326 LYS   C NZ    1 
ATOM   6030  N  N     . ASP   B 1  327 ? -6.746  43.107  12.425  1.00 26.70  ? 327 ASP   C N     1 
ATOM   6031  C  CA    . ASP   B 1  327 ? -7.214  41.843  11.863  1.00 28.64  ? 327 ASP   C CA    1 
ATOM   6032  C  C     . ASP   B 1  327 ? -6.269  40.700  12.218  1.00 33.38  ? 327 ASP   C C     1 
ATOM   6033  O  O     . ASP   B 1  327 ? -6.681  39.681  12.795  1.00 25.00  ? 327 ASP   C O     1 
ATOM   6034  C  CB    . ASP   B 1  327 ? -7.340  41.971  10.345  1.00 41.92  ? 327 ASP   C CB    1 
ATOM   6035  C  CG    . ASP   B 1  327 ? -8.647  42.601  9.911   1.00 48.87  ? 327 ASP   C CG    1 
ATOM   6036  O  OD1   . ASP   B 1  327 ? -9.638  42.471  10.672  1.00 39.12  ? 327 ASP   C OD1   1 
ATOM   6037  O  OD2   . ASP   B 1  327 ? -8.671  43.199  8.799   1.00 48.73  ? 327 ASP   C OD2   1 
ATOM   6038  N  N     . VAL   B 1  328 ? -4.988  40.858  11.854  1.00 28.78  ? 328 VAL   C N     1 
ATOM   6039  C  CA    . VAL   B 1  328 ? -3.971  39.839  12.097  1.00 21.67  ? 328 VAL   C CA    1 
ATOM   6040  C  C     . VAL   B 1  328 ? -3.921  39.424  13.568  1.00 25.18  ? 328 VAL   C C     1 
ATOM   6041  O  O     . VAL   B 1  328 ? -3.818  38.231  13.881  1.00 19.31  ? 328 VAL   C O     1 
ATOM   6042  C  CB    . VAL   B 1  328 ? -2.611  40.349  11.598  1.00 20.67  ? 328 VAL   C CB    1 
ATOM   6043  C  CG1   . VAL   B 1  328 ? -1.547  39.322  11.869  1.00 21.01  ? 328 VAL   C CG1   1 
ATOM   6044  C  CG2   . VAL   B 1  328 ? -2.707  40.723  10.136  1.00 16.63  ? 328 VAL   C CG2   1 
ATOM   6045  N  N     . ASN   B 1  329 ? -3.989  40.393  14.498  1.00 26.96  ? 329 ASN   C N     1 
ATOM   6046  C  CA    . ASN   B 1  329 ? -4.026  40.050  15.926  1.00 22.46  ? 329 ASN   C CA    1 
ATOM   6047  C  C     . ASN   B 1  329 ? -5.114  39.035  16.223  1.00 21.36  ? 329 ASN   C C     1 
ATOM   6048  O  O     . ASN   B 1  329 ? -4.823  37.900  16.610  1.00 24.25  ? 329 ASN   C O     1 
ATOM   6049  C  CB    . ASN   B 1  329 ? -4.283  41.255  16.819  1.00 24.25  ? 329 ASN   C CB    1 
ATOM   6050  C  CG    . ASN   B 1  329 ? -3.086  42.137  16.977  1.00 27.95  ? 329 ASN   C CG    1 
ATOM   6051  O  OD1   . ASN   B 1  329 ? -2.575  42.345  18.075  1.00 36.50  ? 329 ASN   C OD1   1 
ATOM   6052  N  ND2   . ASN   B 1  329 ? -2.644  42.685  15.884  1.00 29.69  ? 329 ASN   C ND2   1 
ATOM   6053  N  N     . ALA   B 1  330 ? -6.371  39.445  16.050  1.00 22.23  ? 330 ALA   C N     1 
ATOM   6054  C  CA    . ALA   B 1  330 ? -7.510  38.550  16.245  1.00 23.70  ? 330 ALA   C CA    1 
ATOM   6055  C  C     . ALA   B 1  330 ? -7.263  37.151  15.670  1.00 26.72  ? 330 ALA   C C     1 
ATOM   6056  O  O     . ALA   B 1  330 ? -7.515  36.147  16.347  1.00 30.72  ? 330 ALA   C O     1 
ATOM   6057  C  CB    . ALA   B 1  330 ? -8.760  39.166  15.626  1.00 14.90  ? 330 ALA   C CB    1 
ATOM   6058  N  N     . ALA   B 1  331 ? -6.724  37.081  14.446  1.00 23.95  ? 331 ALA   C N     1 
ATOM   6059  C  CA    . ALA   B 1  331 ? -6.559  35.802  13.770  1.00 25.34  ? 331 ALA   C CA    1 
ATOM   6060  C  C     . ALA   B 1  331 ? -5.540  34.918  14.485  1.00 29.64  ? 331 ALA   C C     1 
ATOM   6061  O  O     . ALA   B 1  331 ? -5.766  33.712  14.640  1.00 29.70  ? 331 ALA   C O     1 
ATOM   6062  C  CB    . ALA   B 1  331 ? -6.166  36.036  12.311  1.00 25.94  ? 331 ALA   C CB    1 
ATOM   6063  N  N     . ILE   B 1  332 ? -4.407  35.494  14.921  1.00 27.57  ? 332 ILE   C N     1 
ATOM   6064  C  CA    . ILE   B 1  332 ? -3.389  34.695  15.614  1.00 24.97  ? 332 ILE   C CA    1 
ATOM   6065  C  C     . ILE   B 1  332 ? -3.885  34.253  16.984  1.00 30.08  ? 332 ILE   C C     1 
ATOM   6066  O  O     . ILE   B 1  332 ? -3.430  33.231  17.521  1.00 32.32  ? 332 ILE   C O     1 
ATOM   6067  C  CB    . ILE   B 1  332 ? -2.058  35.460  15.746  1.00 24.25  ? 332 ILE   C CB    1 
ATOM   6068  C  CG1   . ILE   B 1  332 ? -1.525  35.838  14.360  1.00 27.00  ? 332 ILE   C CG1   1 
ATOM   6069  C  CG2   . ILE   B 1  332 ? -1.023  34.599  16.505  1.00 22.09  ? 332 ILE   C CG2   1 
ATOM   6070  C  CD1   . ILE   B 1  332 ? -0.095  36.324  14.369  1.00 18.77  ? 332 ILE   C CD1   1 
ATOM   6071  N  N     . ALA   B 1  333 ? -4.802  35.020  17.580  1.00 29.99  ? 333 ALA   C N     1 
ATOM   6072  C  CA    . ALA   B 1  333 ? -5.358  34.664  18.876  1.00 23.22  ? 333 ALA   C CA    1 
ATOM   6073  C  C     . ALA   B 1  333 ? -6.024  33.306  18.811  1.00 28.90  ? 333 ALA   C C     1 
ATOM   6074  O  O     . ALA   B 1  333 ? -5.744  32.415  19.622  1.00 33.38  ? 333 ALA   C O     1 
ATOM   6075  C  CB    . ALA   B 1  333 ? -6.358  35.727  19.293  1.00 25.30  ? 333 ALA   C CB    1 
ATOM   6076  N  N     . THR   B 1  334 ? -6.919  33.144  17.835  1.00 31.95  ? 334 THR   C N     1 
ATOM   6077  C  CA    . THR   B 1  334 ? -7.584  31.876  17.551  1.00 31.31  ? 334 THR   C CA    1 
ATOM   6078  C  C     . THR   B 1  334 ? -6.607  30.719  17.466  1.00 37.19  ? 334 THR   C C     1 
ATOM   6079  O  O     . THR   B 1  334 ? -6.775  29.695  18.143  1.00 40.18  ? 334 THR   C O     1 
ATOM   6080  C  CB    . THR   B 1  334 ? -8.326  31.993  16.234  1.00 31.64  ? 334 THR   C CB    1 
ATOM   6081  O  OG1   . THR   B 1  334 ? -9.319  33.018  16.348  1.00 36.24  ? 334 THR   C OG1   1 
ATOM   6082  C  CG2   . THR   B 1  334 ? -8.953  30.665  15.881  1.00 30.12  ? 334 THR   C CG2   1 
ATOM   6083  N  N     . ILE   B 1  335 ? -5.602  30.853  16.590  1.00 29.89  ? 335 ILE   C N     1 
ATOM   6084  C  CA    . ILE   B 1  335 ? -4.598  29.803  16.411  1.00 33.24  ? 335 ILE   C CA    1 
ATOM   6085  C  C     . ILE   B 1  335 ? -4.013  29.394  17.756  1.00 35.80  ? 335 ILE   C C     1 
ATOM   6086  O  O     . ILE   B 1  335 ? -4.035  28.216  18.131  1.00 41.26  ? 335 ILE   C O     1 
ATOM   6087  C  CB    . ILE   B 1  335 ? -3.503  30.265  15.425  1.00 38.79  ? 335 ILE   C CB    1 
ATOM   6088  C  CG1   . ILE   B 1  335 ? -3.844  29.866  13.993  1.00 35.09  ? 335 ILE   C CG1   1 
ATOM   6089  C  CG2   . ILE   B 1  335 ? -2.175  29.614  15.722  1.00 43.09  ? 335 ILE   C CG2   1 
ATOM   6090  C  CD1   . ILE   B 1  335 ? -5.077  30.515  13.451  1.00 39.10  ? 335 ILE   C CD1   1 
ATOM   6091  N  N     . LYS   B 1  336 ? -3.493  30.367  18.513  1.00 41.37  ? 336 LYS   C N     1 
ATOM   6092  C  CA    . LYS   B 1  336 ? -2.755  30.042  19.731  1.00 44.31  ? 336 LYS   C CA    1 
ATOM   6093  C  C     . LYS   B 1  336 ? -3.611  29.317  20.759  1.00 44.07  ? 336 LYS   C C     1 
ATOM   6094  O  O     . LYS   B 1  336 ? -3.061  28.645  21.636  1.00 50.22  ? 336 LYS   C O     1 
ATOM   6095  C  CB    . LYS   B 1  336 ? -2.154  31.308  20.349  1.00 40.59  ? 336 LYS   C CB    1 
ATOM   6096  C  CG    . LYS   B 1  336 ? -0.672  31.527  20.022  1.00 42.41  ? 336 LYS   C CG    1 
ATOM   6097  C  CD    . LYS   B 1  336 ? 0.044   32.324  21.124  1.00 43.66  ? 336 LYS   C CD    1 
ATOM   6098  C  CE    . LYS   B 1  336 ? -0.007  33.835  20.896  1.00 37.39  ? 336 LYS   C CE    1 
ATOM   6099  N  NZ    . LYS   B 1  336 ? 0.748   34.581  21.965  1.00 38.09  ? 336 LYS   C NZ    1 
ATOM   6100  N  N     . THR   B 1  337 ? -4.934  29.435  20.679  1.00 39.70  ? 337 THR   C N     1 
ATOM   6101  C  CA    . THR   B 1  337 ? -5.806  28.724  21.604  1.00 42.26  ? 337 THR   C CA    1 
ATOM   6102  C  C     . THR   B 1  337 ? -6.262  27.376  21.053  1.00 51.28  ? 337 THR   C C     1 
ATOM   6103  O  O     . THR   B 1  337 ? -6.159  26.353  21.738  1.00 62.17  ? 337 THR   C O     1 
ATOM   6104  C  CB    . THR   B 1  337 ? -7.032  29.573  21.934  1.00 46.24  ? 337 THR   C CB    1 
ATOM   6105  O  OG1   . THR   B 1  337 ? -7.977  29.464  20.869  1.00 37.54  ? 337 THR   C OG1   1 
ATOM   6106  C  CG2   . THR   B 1  337 ? -6.649  31.033  22.109  1.00 53.36  ? 337 THR   C CG2   1 
ATOM   6107  N  N     . LYS   B 1  338 ? -6.753  27.349  19.816  1.00 49.64  ? 338 LYS   C N     1 
ATOM   6108  C  CA    . LYS   B 1  338 ? -7.443  26.178  19.289  1.00 51.26  ? 338 LYS   C CA    1 
ATOM   6109  C  C     . LYS   B 1  338 ? -6.561  25.317  18.379  1.00 60.10  ? 338 LYS   C C     1 
ATOM   6110  O  O     . LYS   B 1  338 ? -7.085  24.517  17.594  1.00 63.08  ? 338 LYS   C O     1 
ATOM   6111  C  CB    . LYS   B 1  338 ? -8.719  26.616  18.554  1.00 46.85  ? 338 LYS   C CB    1 
ATOM   6112  C  CG    . LYS   B 1  338 ? -9.737  27.327  19.446  1.00 54.81  ? 338 LYS   C CG    1 
ATOM   6113  C  CD    . LYS   B 1  338 ? -11.167 26.827  19.231  1.00 59.43  ? 338 LYS   C CD    1 
ATOM   6114  C  CE    . LYS   B 1  338 ? -11.742 26.101  20.478  1.00 50.71  ? 338 LYS   C CE    1 
ATOM   6115  N  NZ    . LYS   B 1  338 ? -13.138 25.586  20.239  1.00 53.47  ? 338 LYS   C NZ    1 
ATOM   6116  N  N     . ARG   B 1  339 ? -5.234  25.442  18.468  1.00 58.84  ? 339 ARG   C N     1 
ATOM   6117  C  CA    . ARG   B 1  339 ? -4.363  24.674  17.585  1.00 56.17  ? 339 ARG   C CA    1 
ATOM   6118  C  C     . ARG   B 1  339 ? -3.141  24.157  18.332  1.00 67.38  ? 339 ARG   C C     1 
ATOM   6119  O  O     . ARG   B 1  339 ? -2.690  24.737  19.331  1.00 63.63  ? 339 ARG   C O     1 
ATOM   6120  C  CB    . ARG   B 1  339 ? -3.923  25.480  16.351  1.00 50.76  ? 339 ARG   C CB    1 
ATOM   6121  C  CG    . ARG   B 1  339 ? -4.861  25.289  15.149  1.00 68.38  ? 339 ARG   C CG    1 
ATOM   6122  C  CD    . ARG   B 1  339 ? -4.482  26.176  13.954  1.00 71.41  ? 339 ARG   C CD    1 
ATOM   6123  N  NE    . ARG   B 1  339 ? -5.498  26.195  12.898  1.00 64.27  ? 339 ARG   C NE    1 
ATOM   6124  C  CZ    . ARG   B 1  339 ? -5.682  25.223  12.011  1.00 66.45  ? 339 ARG   C CZ    1 
ATOM   6125  N  NH1   . ARG   B 1  339 ? -4.974  24.100  12.055  1.00 70.67  ? 339 ARG   C NH1   1 
ATOM   6126  N  NH2   . ARG   B 1  339 ? -6.603  25.379  11.060  1.00 60.52  ? 339 ARG   C NH2   1 
ATOM   6127  N  N     . SER   B 1  340 ? -2.627  23.033  17.823  1.00 77.46  ? 340 SER   C N     1 
ATOM   6128  C  CA    . SER   B 1  340 ? -1.453  22.357  18.380  1.00 83.16  ? 340 SER   C CA    1 
ATOM   6129  C  C     . SER   B 1  340 ? -0.177  22.938  17.771  1.00 72.65  ? 340 SER   C C     1 
ATOM   6130  O  O     . SER   B 1  340 ? 0.570   22.280  17.038  1.00 71.24  ? 340 SER   C O     1 
ATOM   6131  C  CB    . SER   B 1  340 ? -1.543  20.848  18.151  1.00 73.32  ? 340 SER   C CB    1 
ATOM   6132  O  OG    . SER   B 1  340 ? -2.091  20.564  16.872  1.00 66.97  ? 340 SER   C OG    1 
ATOM   6133  N  N     . ILE   B 1  341 ? 0.055   24.208  18.075  1.00 59.08  ? 341 ILE   C N     1 
ATOM   6134  C  CA    . ILE   B 1  341 ? 1.288   24.871  17.685  1.00 60.89  ? 341 ILE   C CA    1 
ATOM   6135  C  C     . ILE   B 1  341 ? 2.126   24.975  18.958  1.00 53.35  ? 341 ILE   C C     1 
ATOM   6136  O  O     . ILE   B 1  341 ? 1.894   25.829  19.814  1.00 48.15  ? 341 ILE   C O     1 
ATOM   6137  C  CB    . ILE   B 1  341 ? 1.022   26.212  16.981  1.00 45.58  ? 341 ILE   C CB    1 
ATOM   6138  C  CG1   . ILE   B 1  341 ? 2.275   27.075  16.911  1.00 42.19  ? 341 ILE   C CG1   1 
ATOM   6139  C  CG2   . ILE   B 1  341 ? -0.192  26.949  17.556  1.00 54.22  ? 341 ILE   C CG2   1 
ATOM   6140  C  CD1   . ILE   B 1  341 ? 2.115   28.225  15.949  1.00 42.40  ? 341 ILE   C CD1   1 
ATOM   6141  N  N     . GLN   B 1  342 ? 3.073   24.046  19.099  1.00 52.96  ? 342 GLN   C N     1 
ATOM   6142  C  CA    . GLN   B 1  342 ? 3.937   23.923  20.262  1.00 51.76  ? 342 GLN   C CA    1 
ATOM   6143  C  C     . GLN   B 1  342 ? 5.346   24.395  19.925  1.00 45.04  ? 342 GLN   C C     1 
ATOM   6144  O  O     . GLN   B 1  342 ? 5.977   23.863  19.004  1.00 36.56  ? 342 GLN   C O     1 
ATOM   6145  C  CB    . GLN   B 1  342 ? 3.985   22.470  20.734  1.00 49.68  ? 342 GLN   C CB    1 
ATOM   6146  C  CG    . GLN   B 1  342 ? 4.926   22.287  21.908  1.00 58.74  ? 342 GLN   C CG    1 
ATOM   6147  C  CD    . GLN   B 1  342 ? 5.536   20.904  22.004  1.00 68.94  ? 342 GLN   C CD    1 
ATOM   6148  O  OE1   . GLN   B 1  342 ? 5.548   20.152  21.051  1.00 75.53  ? 342 GLN   C OE1   1 
ATOM   6149  N  NE2   . GLN   B 1  342 ? 6.126   20.608  23.143  1.00 72.05  ? 342 GLN   C NE2   1 
ATOM   6150  N  N     . PHE   B 1  343 ? 5.859   25.345  20.699  1.00 36.79  ? 343 PHE   C N     1 
ATOM   6151  C  CA    . PHE   B 1  343 ? 7.183   25.885  20.432  1.00 31.58  ? 343 PHE   C CA    1 
ATOM   6152  C  C     . PHE   B 1  343 ? 8.248   25.190  21.271  1.00 27.04  ? 343 PHE   C C     1 
ATOM   6153  O  O     . PHE   B 1  343 ? 7.977   24.656  22.352  1.00 31.06  ? 343 PHE   C O     1 
ATOM   6154  C  CB    . PHE   B 1  343 ? 7.210   27.396  20.683  1.00 26.78  ? 343 PHE   C CB    1 
ATOM   6155  C  CG    . PHE   B 1  343 ? 6.626   28.203  19.551  1.00 31.49  ? 343 PHE   C CG    1 
ATOM   6156  C  CD1   . PHE   B 1  343 ? 5.250   28.340  19.413  1.00 33.11  ? 343 PHE   C CD1   1 
ATOM   6157  C  CD2   . PHE   B 1  343 ? 7.451   28.793  18.601  1.00 27.71  ? 343 PHE   C CD2   1 
ATOM   6158  C  CE1   . PHE   B 1  343 ? 4.701   29.081  18.369  1.00 26.59  ? 343 PHE   C CE1   1 
ATOM   6159  C  CE2   . PHE   B 1  343 ? 6.910   29.541  17.574  1.00 29.72  ? 343 PHE   C CE2   1 
ATOM   6160  C  CZ    . PHE   B 1  343 ? 5.523   29.681  17.461  1.00 31.52  ? 343 PHE   C CZ    1 
ATOM   6161  N  N     . VAL   B 1  344 ? 9.470   25.184  20.751  1.00 23.05  ? 344 VAL   C N     1 
ATOM   6162  C  CA    . VAL   B 1  344 ? 10.569  24.708  21.557  1.00 20.99  ? 344 VAL   C CA    1 
ATOM   6163  C  C     . VAL   B 1  344 ? 10.649  25.581  22.806  1.00 28.92  ? 344 VAL   C C     1 
ATOM   6164  O  O     . VAL   B 1  344 ? 10.145  26.712  22.837  1.00 28.02  ? 344 VAL   C O     1 
ATOM   6165  C  CB    . VAL   B 1  344 ? 11.888  24.721  20.765  1.00 23.48  ? 344 VAL   C CB    1 
ATOM   6166  C  CG1   . VAL   B 1  344 ? 11.899  23.618  19.730  1.00 19.52  ? 344 VAL   C CG1   1 
ATOM   6167  C  CG2   . VAL   B 1  344 ? 12.114  26.065  20.089  1.00 22.16  ? 344 VAL   C CG2   1 
ATOM   6168  N  N     . ASP   B 1  345 ? 11.268  25.037  23.866  1.00 31.31  ? 345 ASP   C N     1 
ATOM   6169  C  CA    . ASP   B 1  345 ? 11.365  25.808  25.107  1.00 30.07  ? 345 ASP   C CA    1 
ATOM   6170  C  C     . ASP   B 1  345 ? 12.397  26.918  25.031  1.00 33.10  ? 345 ASP   C C     1 
ATOM   6171  O  O     . ASP   B 1  345 ? 12.408  27.794  25.906  1.00 37.54  ? 345 ASP   C O     1 
ATOM   6172  C  CB    . ASP   B 1  345 ? 11.670  24.910  26.322  1.00 23.81  ? 345 ASP   C CB    1 
ATOM   6173  C  CG    . ASP   B 1  345 ? 13.043  24.254  26.253  1.00 39.11  ? 345 ASP   C CG    1 
ATOM   6174  O  OD1   . ASP   B 1  345 ? 13.949  24.841  25.606  1.00 37.35  ? 345 ASP   C OD1   1 
ATOM   6175  O  OD2   . ASP   B 1  345 ? 13.208  23.142  26.833  1.00 32.10  ? 345 ASP   C OD2   1 
ATOM   6176  N  N     . TRP   B 1  346 ? 13.258  26.910  24.020  1.00 30.98  ? 346 TRP   C N     1 
ATOM   6177  C  CA    . TRP   B 1  346 ? 14.278  27.937  23.900  1.00 27.63  ? 346 TRP   C CA    1 
ATOM   6178  C  C     . TRP   B 1  346 ? 13.901  29.031  22.920  1.00 26.03  ? 346 TRP   C C     1 
ATOM   6179  O  O     . TRP   B 1  346 ? 14.708  29.929  22.668  1.00 22.91  ? 346 TRP   C O     1 
ATOM   6180  C  CB    . TRP   B 1  346 ? 15.615  27.313  23.503  1.00 29.36  ? 346 TRP   C CB    1 
ATOM   6181  C  CG    . TRP   B 1  346 ? 15.573  26.377  22.335  1.00 28.69  ? 346 TRP   C CG    1 
ATOM   6182  C  CD1   . TRP   B 1  346 ? 15.477  25.024  22.383  1.00 24.07  ? 346 TRP   C CD1   1 
ATOM   6183  C  CD2   . TRP   B 1  346 ? 15.677  26.727  20.939  1.00 27.98  ? 346 TRP   C CD2   1 
ATOM   6184  N  NE1   . TRP   B 1  346 ? 15.513  24.502  21.107  1.00 25.63  ? 346 TRP   C NE1   1 
ATOM   6185  C  CE2   . TRP   B 1  346 ? 15.626  25.529  20.205  1.00 25.28  ? 346 TRP   C CE2   1 
ATOM   6186  C  CE3   . TRP   B 1  346 ? 15.828  27.938  20.246  1.00 22.90  ? 346 TRP   C CE3   1 
ATOM   6187  C  CZ2   . TRP   B 1  346 ? 15.695  25.507  18.817  1.00 22.68  ? 346 TRP   C CZ2   1 
ATOM   6188  C  CZ3   . TRP   B 1  346 ? 15.894  27.911  18.876  1.00 19.51  ? 346 TRP   C CZ3   1 
ATOM   6189  C  CH2   . TRP   B 1  346 ? 15.828  26.709  18.176  1.00 23.47  ? 346 TRP   C CH2   1 
ATOM   6190  N  N     . CYS   B 1  347 ? 12.695  28.989  22.363  1.00 31.94  ? 347 CYS   C N     1 
ATOM   6191  C  CA    . CYS   B 1  347 ? 12.217  30.029  21.462  1.00 34.71  ? 347 CYS   C CA    1 
ATOM   6192  C  C     . CYS   B 1  347 ? 10.941  30.555  22.087  1.00 43.48  ? 347 CYS   C C     1 
ATOM   6193  O  O     . CYS   B 1  347 ? 9.835   30.204  21.655  1.00 50.84  ? 347 CYS   C O     1 
ATOM   6194  C  CB    . CYS   B 1  347 ? 11.969  29.520  20.048  1.00 25.72  ? 347 CYS   C CB    1 
ATOM   6195  S  SG    . CYS   B 1  347 ? 11.293  30.795  19.000  1.00 40.14  ? 347 CYS   C SG    1 
ATOM   6196  N  N     . PRO   B 1  348 ? 11.053  31.410  23.095  1.00 55.16  ? 348 PRO   C N     1 
ATOM   6197  C  CA    . PRO   B 1  348 ? 9.850   31.760  23.861  1.00 70.99  ? 348 PRO   C CA    1 
ATOM   6198  C  C     . PRO   B 1  348 ? 8.815   32.472  23.004  1.00 69.31  ? 348 PRO   C C     1 
ATOM   6199  O  O     . PRO   B 1  348 ? 7.609   32.209  23.131  1.00 62.81  ? 348 PRO   C O     1 
ATOM   6200  C  CB    . PRO   B 1  348 ? 10.407  32.634  24.995  1.00 62.03  ? 348 PRO   C CB    1 
ATOM   6201  C  CG    . PRO   B 1  348 ? 11.649  33.261  24.409  1.00 64.21  ? 348 PRO   C CG    1 
ATOM   6202  C  CD    . PRO   B 1  348 ? 12.193  32.300  23.386  1.00 56.77  ? 348 PRO   C CD    1 
ATOM   6203  N  N     . THR   B 1  349 ? 9.261   33.322  22.084  1.00 60.92  ? 349 THR   C N     1 
ATOM   6204  C  CA    . THR   B 1  349 ? 8.357   34.078  21.222  1.00 69.87  ? 349 THR   C CA    1 
ATOM   6205  C  C     . THR   B 1  349 ? 8.694   33.781  19.761  1.00 52.07  ? 349 THR   C C     1 
ATOM   6206  O  O     . THR   B 1  349 ? 9.608   34.386  19.195  1.00 51.14  ? 349 THR   C O     1 
ATOM   6207  C  CB    . THR   B 1  349 ? 8.465   35.558  21.537  1.00 65.01  ? 349 THR   C CB    1 
ATOM   6208  O  OG1   . THR   B 1  349 ? 9.854   35.907  21.583  1.00 67.13  ? 349 THR   C OG1   1 
ATOM   6209  C  CG2   . THR   B 1  349 ? 7.808   35.854  22.883  1.00 38.75  ? 349 THR   C CG2   1 
ATOM   6210  N  N     . GLY   B 1  350 ? 7.950   32.859  19.154  1.00 36.87  ? 350 GLY   C N     1 
ATOM   6211  C  CA    . GLY   B 1  350 ? 8.231   32.456  17.790  1.00 44.05  ? 350 GLY   C CA    1 
ATOM   6212  C  C     . GLY   B 1  350 ? 7.495   33.232  16.712  1.00 39.67  ? 350 GLY   C C     1 
ATOM   6213  O  O     . GLY   B 1  350 ? 7.956   33.291  15.561  1.00 31.30  ? 350 GLY   C O     1 
ATOM   6214  N  N     . PHE   B 1  351 ? 6.369   33.854  17.084  1.00 33.34  ? 351 PHE   C N     1 
ATOM   6215  C  CA    . PHE   B 1  351 ? 5.443   34.456  16.126  1.00 28.56  ? 351 PHE   C CA    1 
ATOM   6216  C  C     . PHE   B 1  351 ? 5.900   35.842  15.690  1.00 28.19  ? 351 PHE   C C     1 
ATOM   6217  O  O     . PHE   B 1  351 ? 6.078   36.724  16.533  1.00 30.95  ? 351 PHE   C O     1 
ATOM   6218  C  CB    . PHE   B 1  351 ? 4.059   34.539  16.739  1.00 26.27  ? 351 PHE   C CB    1 
ATOM   6219  C  CG    . PHE   B 1  351 ? 3.167   33.458  16.290  1.00 32.85  ? 351 PHE   C CG    1 
ATOM   6220  C  CD1   . PHE   B 1  351 ? 2.986   33.237  14.941  1.00 29.36  ? 351 PHE   C CD1   1 
ATOM   6221  C  CD2   . PHE   B 1  351 ? 2.534   32.636  17.199  1.00 33.71  ? 351 PHE   C CD2   1 
ATOM   6222  C  CE1   . PHE   B 1  351 ? 2.154   32.233  14.502  1.00 31.98  ? 351 PHE   C CE1   1 
ATOM   6223  C  CE2   . PHE   B 1  351 ? 1.715   31.627  16.765  1.00 38.12  ? 351 PHE   C CE2   1 
ATOM   6224  C  CZ    . PHE   B 1  351 ? 1.520   31.420  15.404  1.00 21.91  ? 351 PHE   C CZ    1 
ATOM   6225  N  N     . LYS   B 1  352 ? 6.046   36.042  14.369  1.00 22.82  ? 352 LYS   C N     1 
ATOM   6226  C  CA    . LYS   B 1  352 ? 6.530   37.280  13.772  1.00 17.48  ? 352 LYS   C CA    1 
ATOM   6227  C  C     . LYS   B 1  352 ? 5.734   37.568  12.507  1.00 21.36  ? 352 LYS   C C     1 
ATOM   6228  O  O     . LYS   B 1  352 ? 5.486   36.660  11.715  1.00 20.44  ? 352 LYS   C O     1 
ATOM   6229  C  CB    . LYS   B 1  352 ? 8.021   37.175  13.455  1.00 15.85  ? 352 LYS   C CB    1 
ATOM   6230  C  CG    . LYS   B 1  352 ? 8.609   38.377  12.727  1.00 21.72  ? 352 LYS   C CG    1 
ATOM   6231  C  CD    . LYS   B 1  352 ? 10.135  38.293  12.643  1.00 25.82  ? 352 LYS   C CD    1 
ATOM   6232  C  CE    . LYS   B 1  352 ? 10.760  39.635  12.265  1.00 25.27  ? 352 LYS   C CE    1 
ATOM   6233  N  NZ    . LYS   B 1  352 ? 10.780  40.651  13.365  1.00 22.97  ? 352 LYS   C NZ    1 
ATOM   6234  N  N     . VAL   B 1  353 ? 5.347   38.830  12.303  1.00 24.59  ? 353 VAL   C N     1 
ATOM   6235  C  CA    . VAL   B 1  353 ? 4.365   39.187  11.279  1.00 21.43  ? 353 VAL   C CA    1 
ATOM   6236  C  C     . VAL   B 1  353 ? 4.717   40.512  10.593  1.00 19.85  ? 353 VAL   C C     1 
ATOM   6237  O  O     . VAL   B 1  353 ? 5.113   41.487  11.238  1.00 21.00  ? 353 VAL   C O     1 
ATOM   6238  C  CB    . VAL   B 1  353 ? 2.955   39.259  11.894  1.00 23.62  ? 353 VAL   C CB    1 
ATOM   6239  C  CG1   . VAL   B 1  353 ? 2.660   38.010  12.712  1.00 19.39  ? 353 VAL   C CG1   1 
ATOM   6240  C  CG2   . VAL   B 1  353 ? 2.828   40.501  12.754  1.00 20.19  ? 353 VAL   C CG2   1 
ATOM   6241  N  N     . GLY   B 1  354 ? 4.547   40.551  9.274   1.00 20.99  ? 354 GLY   C N     1 
ATOM   6242  C  CA    . GLY   B 1  354 ? 4.563   41.803  8.548   1.00 17.38  ? 354 GLY   C CA    1 
ATOM   6243  C  C     . GLY   B 1  354 ? 3.415   41.832  7.561   1.00 18.66  ? 354 GLY   C C     1 
ATOM   6244  O  O     . GLY   B 1  354 ? 2.877   40.800  7.174   1.00 21.37  ? 354 GLY   C O     1 
ATOM   6245  N  N     . ILE   B 1  355 ? 3.048   43.039  7.159   1.00 22.31  ? 355 ILE   C N     1 
ATOM   6246  C  CA    . ILE   B 1  355 ? 1.933   43.283  6.254   1.00 19.80  ? 355 ILE   C CA    1 
ATOM   6247  C  C     . ILE   B 1  355 ? 2.460   44.083  5.081   1.00 25.94  ? 355 ILE   C C     1 
ATOM   6248  O  O     . ILE   B 1  355 ? 2.957   45.202  5.260   1.00 27.76  ? 355 ILE   C O     1 
ATOM   6249  C  CB    . ILE   B 1  355 ? 0.789   44.049  6.934   1.00 19.06  ? 355 ILE   C CB    1 
ATOM   6250  C  CG1   . ILE   B 1  355 ? 0.098   43.193  7.985   1.00 19.33  ? 355 ILE   C CG1   1 
ATOM   6251  C  CG2   . ILE   B 1  355 ? -0.244  44.489  5.928   1.00 22.32  ? 355 ILE   C CG2   1 
ATOM   6252  C  CD1   . ILE   B 1  355 ? -1.217  43.791  8.416   1.00 24.52  ? 355 ILE   C CD1   1 
ATOM   6253  N  N     . ASN   B 1  356 ? 2.340   43.528  3.885   1.00 30.15  ? 356 ASN   C N     1 
ATOM   6254  C  CA    . ASN   B 1  356 ? 2.761   44.216  2.671   1.00 30.79  ? 356 ASN   C CA    1 
ATOM   6255  C  C     . ASN   B 1  356 ? 1.518   44.726  1.942   1.00 34.38  ? 356 ASN   C C     1 
ATOM   6256  O  O     . ASN   B 1  356 ? 0.696   43.935  1.473   1.00 35.15  ? 356 ASN   C O     1 
ATOM   6257  C  CB    . ASN   B 1  356 ? 3.582   43.281  1.799   1.00 27.26  ? 356 ASN   C CB    1 
ATOM   6258  C  CG    . ASN   B 1  356 ? 4.126   43.969  0.603   1.00 39.87  ? 356 ASN   C CG    1 
ATOM   6259  O  OD1   . ASN   B 1  356 ? 5.135   44.643  0.713   1.00 52.04  ? 356 ASN   C OD1   1 
ATOM   6260  N  ND2   . ASN   B 1  356 ? 3.459   43.842  -0.545  1.00 43.63  ? 356 ASN   C ND2   1 
ATOM   6261  N  N     . TYR   B 1  357 ? 1.383   46.048  1.840   1.00 32.13  ? 357 TYR   C N     1 
ATOM   6262  C  CA    . TYR   B 1  357 ? 0.116   46.601  1.385   1.00 27.79  ? 357 TYR   C CA    1 
ATOM   6263  C  C     . TYR   B 1  357 ? -0.188  46.211  -0.050  1.00 35.50  ? 357 TYR   C C     1 
ATOM   6264  O  O     . TYR   B 1  357 ? -1.361  46.134  -0.427  1.00 38.91  ? 357 TYR   C O     1 
ATOM   6265  C  CB    . TYR   B 1  357 ? 0.123   48.118  1.558   1.00 30.72  ? 357 TYR   C CB    1 
ATOM   6266  C  CG    . TYR   B 1  357 ? -0.079  48.509  3.017   1.00 50.82  ? 357 TYR   C CG    1 
ATOM   6267  C  CD1   . TYR   B 1  357 ? -0.897  47.732  3.853   1.00 44.66  ? 357 TYR   C CD1   1 
ATOM   6268  C  CD2   . TYR   B 1  357 ? 0.554   49.633  3.572   1.00 43.30  ? 357 TYR   C CD2   1 
ATOM   6269  C  CE1   . TYR   B 1  357 ? -1.088  48.061  5.186   1.00 41.01  ? 357 TYR   C CE1   1 
ATOM   6270  C  CE2   . TYR   B 1  357 ? 0.369   49.971  4.909   1.00 41.41  ? 357 TYR   C CE2   1 
ATOM   6271  C  CZ    . TYR   B 1  357 ? -0.454  49.180  5.709   1.00 50.56  ? 357 TYR   C CZ    1 
ATOM   6272  O  OH    . TYR   B 1  357 ? -0.651  49.506  7.032   1.00 59.56  ? 357 TYR   C OH    1 
ATOM   6273  N  N     . GLN   B 1  358 ? 0.833   45.935  -0.851  1.00 30.43  ? 358 GLN   C N     1 
ATOM   6274  C  CA    . GLN   B 1  358 ? 0.617   45.663  -2.267  1.00 28.71  ? 358 GLN   C CA    1 
ATOM   6275  C  C     . GLN   B 1  358 ? -0.198  44.389  -2.479  1.00 34.25  ? 358 GLN   C C     1 
ATOM   6276  O  O     . GLN   B 1  358 ? 0.162   43.335  -1.945  1.00 36.46  ? 358 GLN   C O     1 
ATOM   6277  C  CB    . GLN   B 1  358 ? 1.945   45.533  -2.966  1.00 32.69  ? 358 GLN   C CB    1 
ATOM   6278  C  CG    . GLN   B 1  358 ? 1.787   45.598  -4.437  1.00 40.55  ? 358 GLN   C CG    1 
ATOM   6279  C  CD    . GLN   B 1  358 ? 1.593   47.017  -4.861  1.00 48.13  ? 358 GLN   C CD    1 
ATOM   6280  O  OE1   . GLN   B 1  358 ? 1.919   47.926  -4.096  1.00 48.12  ? 358 GLN   C OE1   1 
ATOM   6281  N  NE2   . GLN   B 1  358 ? 1.063   47.233  -6.072  1.00 47.87  ? 358 GLN   C NE2   1 
ATOM   6282  N  N     . PRO   B 1  359 ? -1.255  44.422  -3.290  1.00 43.15  ? 359 PRO   C N     1 
ATOM   6283  C  CA    . PRO   B 1  359 ? -2.148  43.245  -3.404  1.00 37.24  ? 359 PRO   C CA    1 
ATOM   6284  C  C     . PRO   B 1  359 ? -1.583  42.213  -4.362  1.00 35.29  ? 359 PRO   C C     1 
ATOM   6285  O  O     . PRO   B 1  359 ? -0.784  42.539  -5.253  1.00 38.54  ? 359 PRO   C O     1 
ATOM   6286  C  CB    . PRO   B 1  359 ? -3.456  43.843  -3.940  1.00 29.74  ? 359 PRO   C CB    1 
ATOM   6287  C  CG    . PRO   B 1  359 ? -2.985  44.994  -4.769  1.00 37.75  ? 359 PRO   C CG    1 
ATOM   6288  C  CD    . PRO   B 1  359 ? -1.698  45.528  -4.159  1.00 38.51  ? 359 PRO   C CD    1 
ATOM   6289  N  N     . PRO   B 1  360 ? -1.962  40.950  -4.202  1.00 35.95  ? 360 PRO   C N     1 
ATOM   6290  C  CA    . PRO   B 1  360 ? -1.443  39.912  -5.100  1.00 43.51  ? 360 PRO   C CA    1 
ATOM   6291  C  C     . PRO   B 1  360 ? -2.094  39.992  -6.474  1.00 36.04  ? 360 PRO   C C     1 
ATOM   6292  O  O     . PRO   B 1  360 ? -3.309  40.140  -6.602  1.00 44.52  ? 360 PRO   C O     1 
ATOM   6293  C  CB    . PRO   B 1  360 ? -1.798  38.607  -4.372  1.00 41.58  ? 360 PRO   C CB    1 
ATOM   6294  C  CG    . PRO   B 1  360 ? -2.981  38.975  -3.488  1.00 29.73  ? 360 PRO   C CG    1 
ATOM   6295  C  CD    . PRO   B 1  360 ? -2.824  40.407  -3.131  1.00 29.35  ? 360 PRO   C CD    1 
ATOM   6296  N  N     . THR   B 1  361 ? -1.276  39.921  -7.509  1.00 35.30  ? 361 THR   C N     1 
ATOM   6297  C  CA    . THR   B 1  361 ? -1.809  39.843  -8.855  1.00 38.95  ? 361 THR   C CA    1 
ATOM   6298  C  C     . THR   B 1  361 ? -1.710  38.417  -9.367  1.00 33.33  ? 361 THR   C C     1 
ATOM   6299  O  O     . THR   B 1  361 ? -0.997  37.571  -8.827  1.00 30.80  ? 361 THR   C O     1 
ATOM   6300  C  CB    . THR   B 1  361 ? -1.085  40.793  -9.822  1.00 47.20  ? 361 THR   C CB    1 
ATOM   6301  O  OG1   . THR   B 1  361 ? 0.324   40.808  -9.548  1.00 29.63  ? 361 THR   C OG1   1 
ATOM   6302  C  CG2   . THR   B 1  361 ? -1.664  42.210  -9.740  1.00 61.95  ? 361 THR   C CG2   1 
ATOM   6303  N  N     . VAL   B 1  362 ? -2.446  38.162  -10.434 1.00 37.06  ? 362 VAL   C N     1 
ATOM   6304  C  CA    . VAL   B 1  362 ? -2.453  36.862  -11.076 1.00 30.83  ? 362 VAL   C CA    1 
ATOM   6305  C  C     . VAL   B 1  362 ? -2.103  37.069  -12.536 1.00 34.70  ? 362 VAL   C C     1 
ATOM   6306  O  O     . VAL   B 1  362 ? -2.473  38.079  -13.141 1.00 36.27  ? 362 VAL   C O     1 
ATOM   6307  C  CB    . VAL   B 1  362 ? -3.807  36.148  -10.913 1.00 35.98  ? 362 VAL   C CB    1 
ATOM   6308  C  CG1   . VAL   B 1  362 ? -3.828  35.352  -9.615  1.00 38.34  ? 362 VAL   C CG1   1 
ATOM   6309  C  CG2   . VAL   B 1  362 ? -4.938  37.154  -10.937 1.00 33.98  ? 362 VAL   C CG2   1 
ATOM   6310  N  N     . VAL   B 1  363 ? -1.351  36.130  -13.079 1.00 39.78  ? 363 VAL   C N     1 
ATOM   6311  C  CA    A VAL   B 1  363 ? -0.926  36.200  -14.471 1.00 37.16  ? 363 VAL   C CA    1 
ATOM   6312  C  CA    B VAL   B 1  363 ? -0.924  36.195  -14.477 0.00 37.41  ? 363 VAL   C CA    1 
ATOM   6313  C  C     . VAL   B 1  363 ? -2.141  35.936  -15.376 1.00 37.86  ? 363 VAL   C C     1 
ATOM   6314  O  O     . VAL   B 1  363 ? -2.894  34.992  -15.110 1.00 42.38  ? 363 VAL   C O     1 
ATOM   6315  C  CB    A VAL   B 1  363 ? 0.193   35.189  -14.721 1.00 39.00  ? 363 VAL   C CB    1 
ATOM   6316  C  CB    B VAL   B 1  363 ? 0.183   35.174  -14.744 0.00 39.11  ? 363 VAL   C CB    1 
ATOM   6317  C  CG1   A VAL   B 1  363 ? -0.198  34.155  -15.784 1.00 42.08  ? 363 VAL   C CG1   1 
ATOM   6318  C  CG1   B VAL   B 1  363 ? -0.318  33.760  -14.469 0.00 42.22  ? 363 VAL   C CG1   1 
ATOM   6319  C  CG2   A VAL   B 1  363 ? 1.485   35.912  -15.060 1.00 34.13  ? 363 VAL   C CG2   1 
ATOM   6320  C  CG2   B VAL   B 1  363 ? 0.703   35.298  -16.168 0.00 41.25  ? 363 VAL   C CG2   1 
ATOM   6321  N  N     . PRO   B 1  364 ? -2.360  36.735  -16.415 1.00 52.37  ? 364 PRO   C N     1 
ATOM   6322  C  CA    . PRO   B 1  364 ? -3.525  36.489  -17.287 1.00 50.62  ? 364 PRO   C CA    1 
ATOM   6323  C  C     . PRO   B 1  364 ? -3.662  35.017  -17.669 1.00 42.51  ? 364 PRO   C C     1 
ATOM   6324  O  O     . PRO   B 1  364 ? -2.678  34.318  -17.919 1.00 36.73  ? 364 PRO   C O     1 
ATOM   6325  C  CB    . PRO   B 1  364 ? -3.240  37.369  -18.516 1.00 53.34  ? 364 PRO   C CB    1 
ATOM   6326  C  CG    . PRO   B 1  364 ? -1.792  37.847  -18.373 1.00 51.68  ? 364 PRO   C CG    1 
ATOM   6327  C  CD    . PRO   B 1  364 ? -1.561  37.880  -16.884 1.00 52.53  ? 364 PRO   C CD    1 
ATOM   6328  N  N     . GLY   B 1  365 ? -4.902  34.543  -17.700 1.00 39.47  ? 365 GLY   C N     1 
ATOM   6329  C  CA    . GLY   B 1  365 ? -5.151  33.184  -18.151 1.00 44.96  ? 365 GLY   C CA    1 
ATOM   6330  C  C     . GLY   B 1  365 ? -4.506  32.127  -17.287 1.00 44.04  ? 365 GLY   C C     1 
ATOM   6331  O  O     . GLY   B 1  365 ? -4.034  31.105  -17.800 1.00 52.26  ? 365 GLY   C O     1 
ATOM   6332  N  N     . GLY   B 1  366 ? -4.446  32.368  -15.981 1.00 46.11  ? 366 GLY   C N     1 
ATOM   6333  C  CA    . GLY   B 1  366 ? -3.984  31.384  -15.032 1.00 44.35  ? 366 GLY   C CA    1 
ATOM   6334  C  C     . GLY   B 1  366 ? -5.139  30.668  -14.352 1.00 44.80  ? 366 GLY   C C     1 
ATOM   6335  O  O     . GLY   B 1  366 ? -6.313  30.840  -14.690 1.00 46.54  ? 366 GLY   C O     1 
ATOM   6336  N  N     . ASP   B 1  367 ? -4.781  29.843  -13.370 1.00 40.16  ? 367 ASP   C N     1 
ATOM   6337  C  CA    . ASP   B 1  367 ? -5.759  29.102  -12.589 1.00 38.80  ? 367 ASP   C CA    1 
ATOM   6338  C  C     . ASP   B 1  367 ? -6.063  29.751  -11.248 1.00 40.29  ? 367 ASP   C C     1 
ATOM   6339  O  O     . ASP   B 1  367 ? -7.221  29.734  -10.816 1.00 42.60  ? 367 ASP   C O     1 
ATOM   6340  C  CB    . ASP   B 1  367 ? -5.263  27.675  -12.395 1.00 41.99  ? 367 ASP   C CB    1 
ATOM   6341  C  CG    . ASP   B 1  367 ? -4.647  27.114  -13.674 1.00 58.62  ? 367 ASP   C CG    1 
ATOM   6342  O  OD1   . ASP   B 1  367 ? -5.414  26.571  -14.508 1.00 64.41  ? 367 ASP   C OD1   1 
ATOM   6343  O  OD2   . ASP   B 1  367 ? -3.410  27.267  -13.874 1.00 50.13  ? 367 ASP   C OD2   1 
ATOM   6344  N  N     . LEU   B 1  368 ? -5.070  30.371  -10.612 1.00 35.91  ? 368 LEU   C N     1 
ATOM   6345  C  CA    . LEU   B 1  368 ? -5.308  31.086  -9.368  1.00 31.01  ? 368 LEU   C CA    1 
ATOM   6346  C  C     . LEU   B 1  368 ? -6.284  32.234  -9.583  1.00 36.08  ? 368 LEU   C C     1 
ATOM   6347  O  O     . LEU   B 1  368 ? -6.180  32.991  -10.554 1.00 38.13  ? 368 LEU   C O     1 
ATOM   6348  C  CB    . LEU   B 1  368 ? -3.996  31.626  -8.804  1.00 28.81  ? 368 LEU   C CB    1 
ATOM   6349  C  CG    . LEU   B 1  368 ? -3.272  30.751  -7.783  1.00 33.53  ? 368 LEU   C CG    1 
ATOM   6350  C  CD1   . LEU   B 1  368 ? -3.885  29.338  -7.724  1.00 34.67  ? 368 LEU   C CD1   1 
ATOM   6351  C  CD2   . LEU   B 1  368 ? -1.759  30.711  -8.066  1.00 25.00  ? 368 LEU   C CD2   1 
ATOM   6352  N  N     . ALA   B 1  369 ? -7.244  32.354  -8.668  1.00 39.73  ? 369 ALA   C N     1 
ATOM   6353  C  CA    . ALA   B 1  369 ? -8.110  33.521  -8.626  1.00 39.90  ? 369 ALA   C CA    1 
ATOM   6354  C  C     . ALA   B 1  369 ? -7.331  34.717  -8.128  1.00 38.52  ? 369 ALA   C C     1 
ATOM   6355  O  O     . ALA   B 1  369 ? -6.338  34.575  -7.407  1.00 37.81  ? 369 ALA   C O     1 
ATOM   6356  C  CB    . ALA   B 1  369 ? -9.304  33.298  -7.700  1.00 38.31  ? 369 ALA   C CB    1 
ATOM   6357  N  N     . LYS   B 1  370 ? -7.789  35.905  -8.513  1.00 37.91  ? 370 LYS   C N     1 
ATOM   6358  C  CA    . LYS   B 1  370 ? -7.226  37.135  -7.974  1.00 36.13  ? 370 LYS   C CA    1 
ATOM   6359  C  C     . LYS   B 1  370 ? -7.970  37.454  -6.679  1.00 32.69  ? 370 LYS   C C     1 
ATOM   6360  O  O     . LYS   B 1  370 ? -9.158  37.784  -6.706  1.00 34.00  ? 370 LYS   C O     1 
ATOM   6361  C  CB    . LYS   B 1  370 ? -7.324  38.278  -8.975  1.00 28.17  ? 370 LYS   C CB    1 
ATOM   6362  C  CG    . LYS   B 1  370 ? -6.283  39.360  -8.727  1.00 32.88  ? 370 LYS   C CG    1 
ATOM   6363  C  CD    . LYS   B 1  370 ? -6.412  40.569  -9.641  1.00 30.89  ? 370 LYS   C CD    1 
ATOM   6364  C  CE    . LYS   B 1  370 ? -6.796  41.829  -8.870  1.00 47.12  ? 370 LYS   C CE    1 
ATOM   6365  N  NZ    . LYS   B 1  370 ? -5.638  42.616  -8.355  1.00 58.13  ? 370 LYS   C NZ    1 
ATOM   6366  N  N     . VAL   B 1  371 ? -7.277  37.348  -5.541  1.00 37.87  ? 371 VAL   C N     1 
ATOM   6367  C  CA    . VAL   B 1  371 ? -7.880  37.586  -4.234  1.00 34.65  ? 371 VAL   C CA    1 
ATOM   6368  C  C     . VAL   B 1  371 ? -7.438  38.943  -3.697  1.00 33.50  ? 371 VAL   C C     1 
ATOM   6369  O  O     . VAL   B 1  371 ? -6.455  39.543  -4.149  1.00 35.56  ? 371 VAL   C O     1 
ATOM   6370  C  CB    . VAL   B 1  371 ? -7.541  36.472  -3.231  1.00 25.47  ? 371 VAL   C CB    1 
ATOM   6371  C  CG1   . VAL   B 1  371 ? -8.164  35.173  -3.661  1.00 24.52  ? 371 VAL   C CG1   1 
ATOM   6372  C  CG2   . VAL   B 1  371 ? -6.060  36.335  -3.115  1.00 34.72  ? 371 VAL   C CG2   1 
ATOM   6373  N  N     . GLN   B 1  372 ? -8.191  39.441  -2.712  1.00 34.59  ? 372 GLN   C N     1 
ATOM   6374  C  CA    . GLN   B 1  372 ? -7.918  40.766  -2.155  1.00 38.91  ? 372 GLN   C CA    1 
ATOM   6375  C  C     . GLN   B 1  372 ? -6.724  40.754  -1.199  1.00 34.18  ? 372 GLN   C C     1 
ATOM   6376  O  O     . GLN   B 1  372 ? -5.897  41.668  -1.215  1.00 35.11  ? 372 GLN   C O     1 
ATOM   6377  C  CB    . GLN   B 1  372 ? -9.173  41.301  -1.449  1.00 40.81  ? 372 GLN   C CB    1 
ATOM   6378  C  CG    . GLN   B 1  372 ? -9.993  42.290  -2.301  1.00 44.49  ? 372 GLN   C CG    1 
ATOM   6379  C  CD    . GLN   B 1  372 ? -11.304 42.751  -1.634  1.00 52.92  ? 372 GLN   C CD    1 
ATOM   6380  O  OE1   . GLN   B 1  372 ? -12.111 41.932  -1.147  1.00 45.03  ? 372 GLN   C OE1   1 
ATOM   6381  N  NE2   . GLN   B 1  372 ? -11.522 44.079  -1.619  1.00 44.70  ? 372 GLN   C NE2   1 
ATOM   6382  N  N     . ARG   B 1  373 ? -6.610  39.729  -0.372  1.00 33.02  ? 373 ARG   C N     1 
ATOM   6383  C  CA    . ARG   B 1  373 ? -5.575  39.656  0.640   1.00 29.26  ? 373 ARG   C CA    1 
ATOM   6384  C  C     . ARG   B 1  373 ? -5.043  38.233  0.658   1.00 29.39  ? 373 ARG   C C     1 
ATOM   6385  O  O     . ARG   B 1  373 ? -5.807  37.286  0.474   1.00 34.38  ? 373 ARG   C O     1 
ATOM   6386  C  CB    . ARG   B 1  373 ? -6.149  40.029  1.994   1.00 27.62  ? 373 ARG   C CB    1 
ATOM   6387  C  CG    . ARG   B 1  373 ? -7.025  38.926  2.567   1.00 22.48  ? 373 ARG   C CG    1 
ATOM   6388  C  CD    . ARG   B 1  373 ? -8.128  39.528  3.391   1.00 28.77  ? 373 ARG   C CD    1 
ATOM   6389  N  NE    . ARG   B 1  373 ? -8.844  40.550  2.636   1.00 33.40  ? 373 ARG   C NE    1 
ATOM   6390  C  CZ    . ARG   B 1  373 ? -10.086 40.416  2.186   1.00 39.78  ? 373 ARG   C CZ    1 
ATOM   6391  N  NH1   . ARG   B 1  373 ? -10.794 39.322  2.431   1.00 31.74  ? 373 ARG   C NH1   1 
ATOM   6392  N  NH2   . ARG   B 1  373 ? -10.635 41.407  1.479   1.00 35.53  ? 373 ARG   C NH2   1 
ATOM   6393  N  N     . ALA   B 1  374 ? -3.741  38.080  0.866   1.00 28.54  ? 374 ALA   C N     1 
ATOM   6394  C  CA    . ALA   B 1  374 ? -3.101  36.774  0.778   1.00 25.79  ? 374 ALA   C CA    1 
ATOM   6395  C  C     . ALA   B 1  374 ? -2.008  36.692  1.836   1.00 23.86  ? 374 ALA   C C     1 
ATOM   6396  O  O     . ALA   B 1  374 ? -1.626  37.696  2.445   1.00 28.27  ? 374 ALA   C O     1 
ATOM   6397  C  CB    . ALA   B 1  374 ? -2.530  36.521  -0.620  1.00 21.65  ? 374 ALA   C CB    1 
ATOM   6398  N  N     . VAL   B 1  375 ? -1.505  35.485  2.061   1.00 14.92  ? 375 VAL   C N     1 
ATOM   6399  C  CA    . VAL   B 1  375 ? -0.607  35.246  3.180   1.00 18.62  ? 375 VAL   C CA    1 
ATOM   6400  C  C     . VAL   B 1  375 ? 0.351   34.107  2.834   1.00 23.36  ? 375 VAL   C C     1 
ATOM   6401  O  O     . VAL   B 1  375 ? -0.029  33.110  2.211   1.00 26.05  ? 375 VAL   C O     1 
ATOM   6402  C  CB    . VAL   B 1  375 ? -1.395  34.936  4.469   1.00 21.48  ? 375 VAL   C CB    1 
ATOM   6403  C  CG1   . VAL   B 1  375 ? -2.055  33.589  4.346   1.00 18.61  ? 375 VAL   C CG1   1 
ATOM   6404  C  CG2   . VAL   B 1  375 ? -0.469  34.992  5.698   1.00 21.50  ? 375 VAL   C CG2   1 
ATOM   6405  N  N     . CYS   B 1  376 ? 1.604   34.263  3.243   1.00 17.14  ? 376 CYS   C N     1 
ATOM   6406  C  CA    . CYS   B 1  376 ? 2.587   33.207  3.135   1.00 17.61  ? 376 CYS   C CA    1 
ATOM   6407  C  C     . CYS   B 1  376 ? 3.225   33.039  4.505   1.00 21.58  ? 376 CYS   C C     1 
ATOM   6408  O  O     . CYS   B 1  376 ? 3.655   34.020  5.120   1.00 21.36  ? 376 CYS   C O     1 
ATOM   6409  C  CB    . CYS   B 1  376 ? 3.644   33.522  2.070   1.00 16.22  ? 376 CYS   C CB    1 
ATOM   6410  S  SG    . CYS   B 1  376 ? 4.916   32.265  2.009   1.00 20.45  ? 376 CYS   C SG    1 
ATOM   6411  N  N     . MET   B 1  377 ? 3.279   31.811  4.993   1.00 20.16  ? 377 MET   C N     1 
ATOM   6412  C  CA    . MET   B 1  377 ? 3.866   31.563  6.291   1.00 21.06  ? 377 MET   C CA    1 
ATOM   6413  C  C     . MET   B 1  377 ? 5.185   30.833  6.124   1.00 28.88  ? 377 MET   C C     1 
ATOM   6414  O  O     . MET   B 1  377 ? 5.253   29.792  5.455   1.00 29.43  ? 377 MET   C O     1 
ATOM   6415  C  CB    . MET   B 1  377 ? 2.938   30.767  7.196   1.00 19.70  ? 377 MET   C CB    1 
ATOM   6416  C  CG    . MET   B 1  377 ? 3.500   30.708  8.571   1.00 24.03  ? 377 MET   C CG    1 
ATOM   6417  S  SD    . MET   B 1  377 ? 2.426   29.951  9.771   1.00 25.38  ? 377 MET   C SD    1 
ATOM   6418  C  CE    . MET   B 1  377 ? 2.964   28.281  9.615   1.00 22.12  ? 377 MET   C CE    1 
ATOM   6419  N  N     . LEU   B 1  378 ? 6.229   31.409  6.715   1.00 29.29  ? 378 LEU   C N     1 
ATOM   6420  C  CA    . LEU   B 1  378 ? 7.539   30.783  6.829   1.00 23.21  ? 378 LEU   C CA    1 
ATOM   6421  C  C     . LEU   B 1  378 ? 7.642   30.314  8.271   1.00 18.61  ? 378 LEU   C C     1 
ATOM   6422  O  O     . LEU   B 1  378 ? 7.601   31.125  9.203   1.00 21.65  ? 378 LEU   C O     1 
ATOM   6423  C  CB    . LEU   B 1  378 ? 8.660   31.761  6.454   1.00 20.59  ? 378 LEU   C CB    1 
ATOM   6424  C  CG    . LEU   B 1  378 ? 8.547   32.326  5.024   1.00 26.18  ? 378 LEU   C CG    1 
ATOM   6425  C  CD1   . LEU   B 1  378 ? 9.415   33.563  4.761   1.00 21.28  ? 378 LEU   C CD1   1 
ATOM   6426  C  CD2   . LEU   B 1  378 ? 8.810   31.218  3.982   1.00 22.23  ? 378 LEU   C CD2   1 
ATOM   6427  N  N     . SER   B 1  379 ? 7.705   29.008  8.456   1.00 19.30  ? 379 SER   C N     1 
ATOM   6428  C  CA    . SER   B 1  379 ? 7.854   28.415  9.773   1.00 21.25  ? 379 SER   C CA    1 
ATOM   6429  C  C     . SER   B 1  379 ? 9.097   27.554  9.734   1.00 21.55  ? 379 SER   C C     1 
ATOM   6430  O  O     . SER   B 1  379 ? 9.429   26.985  8.694   1.00 23.54  ? 379 SER   C O     1 
ATOM   6431  C  CB    . SER   B 1  379 ? 6.620   27.592  10.196  1.00 16.31  ? 379 SER   C CB    1 
ATOM   6432  O  OG    . SER   B 1  379 ? 5.884   27.136  9.077   1.00 25.85  ? 379 SER   C OG    1 
ATOM   6433  N  N     . ASN   B 1  380 ? 9.820   27.534  10.837  1.00 19.46  ? 380 ASN   C N     1 
ATOM   6434  C  CA    . ASN   B 1  380 ? 10.965  26.662  11.005  1.00 20.56  ? 380 ASN   C CA    1 
ATOM   6435  C  C     . ASN   B 1  380 ? 10.484  25.602  11.984  1.00 25.18  ? 380 ASN   C C     1 
ATOM   6436  O  O     . ASN   B 1  380 ? 10.318  25.878  13.174  1.00 24.95  ? 380 ASN   C O     1 
ATOM   6437  C  CB    . ASN   B 1  380 ? 12.179  27.441  11.503  1.00 21.97  ? 380 ASN   C CB    1 
ATOM   6438  C  CG    . ASN   B 1  380 ? 13.381  26.554  11.765  1.00 31.06  ? 380 ASN   C CG    1 
ATOM   6439  O  OD1   . ASN   B 1  380 ? 13.853  26.469  12.901  1.00 22.03  ? 380 ASN   C OD1   1 
ATOM   6440  N  ND2   . ASN   B 1  380 ? 13.886  25.886  10.717  1.00 37.21  ? 380 ASN   C ND2   1 
ATOM   6441  N  N     . THR   B 1  381 ? 10.192  24.409  11.473  1.00 24.57  ? 381 THR   C N     1 
ATOM   6442  C  CA    . THR   B 1  381 ? 9.689   23.318  12.296  1.00 16.86  ? 381 THR   C CA    1 
ATOM   6443  C  C     . THR   B 1  381 ? 10.551  22.088  12.086  1.00 20.20  ? 381 THR   C C     1 
ATOM   6444  O  O     . THR   B 1  381 ? 10.971  21.810  10.958  1.00 28.46  ? 381 THR   C O     1 
ATOM   6445  C  CB    . THR   B 1  381 ? 8.233   22.973  11.969  1.00 21.34  ? 381 THR   C CB    1 
ATOM   6446  O  OG1   . THR   B 1  381 ? 7.866   21.770  12.671  1.00 32.95  ? 381 THR   C OG1   1 
ATOM   6447  C  CG2   . THR   B 1  381 ? 8.015   22.792  10.465  1.00 13.06  ? 381 THR   C CG2   1 
ATOM   6448  N  N     . THR   B 1  382 ? 10.805  21.345  13.166  1.00 15.88  ? 382 THR   C N     1 
ATOM   6449  C  CA    . THR   B 1  382 ? 11.555  20.097  13.053  1.00 16.05  ? 382 THR   C CA    1 
ATOM   6450  C  C     . THR   B 1  382 ? 10.955  19.133  12.042  1.00 23.97  ? 382 THR   C C     1 
ATOM   6451  O  O     . THR   B 1  382 ? 11.628  18.164  11.648  1.00 21.30  ? 382 THR   C O     1 
ATOM   6452  C  CB    . THR   B 1  382 ? 11.625  19.372  14.390  1.00 15.37  ? 382 THR   C CB    1 
ATOM   6453  O  OG1   . THR   B 1  382 ? 10.299  19.104  14.872  1.00 16.98  ? 382 THR   C OG1   1 
ATOM   6454  C  CG2   . THR   B 1  382 ? 12.389  20.179  15.388  1.00 19.05  ? 382 THR   C CG2   1 
ATOM   6455  N  N     . ALA   B 1  383 ? 9.704   19.358  11.629  1.00 22.49  ? 383 ALA   C N     1 
ATOM   6456  C  CA    . ALA   B 1  383 ? 9.046   18.410  10.741  1.00 20.30  ? 383 ALA   C CA    1 
ATOM   6457  C  C     . ALA   B 1  383 ? 9.599   18.458  9.326   1.00 27.36  ? 383 ALA   C C     1 
ATOM   6458  O  O     . ALA   B 1  383 ? 9.428   17.486  8.582   1.00 31.83  ? 383 ALA   C O     1 
ATOM   6459  C  CB    . ALA   B 1  383 ? 7.545   18.658  10.722  1.00 26.62  ? 383 ALA   C CB    1 
ATOM   6460  N  N     . ILE   B 1  384 ? 10.238  19.560  8.921   1.00 22.21  ? 384 ILE   C N     1 
ATOM   6461  C  CA    . ILE   B 1  384 ? 10.828  19.624  7.592   1.00 16.08  ? 384 ILE   C CA    1 
ATOM   6462  C  C     . ILE   B 1  384 ? 11.826  18.469  7.522   1.00 22.93  ? 384 ILE   C C     1 
ATOM   6463  O  O     . ILE   B 1  384 ? 12.224  18.022  6.438   1.00 20.13  ? 384 ILE   C O     1 
ATOM   6464  C  CB    . ILE   B 1  384 ? 11.490  20.999  7.318   1.00 21.61  ? 384 ILE   C CB    1 
ATOM   6465  C  CG1   . ILE   B 1  384 ? 11.603  21.284  5.815   1.00 17.85  ? 384 ILE   C CG1   1 
ATOM   6466  C  CG2   . ILE   B 1  384 ? 12.902  21.111  7.911   1.00 17.92  ? 384 ILE   C CG2   1 
ATOM   6467  C  CD1   . ILE   B 1  384 ? 10.372  21.881  5.200   1.00 17.55  ? 384 ILE   C CD1   1 
ATOM   6468  N  N     . ALA   B 1  385 ? 12.248  17.971  8.690   1.00 24.14  ? 385 ALA   C N     1 
ATOM   6469  C  CA    . ALA   B 1  385 ? 13.242  16.905  8.690   1.00 23.04  ? 385 ALA   C CA    1 
ATOM   6470  C  C     . ALA   B 1  385 ? 12.698  15.647  8.045   1.00 20.99  ? 385 ALA   C C     1 
ATOM   6471  O  O     . ALA   B 1  385 ? 13.471  14.843  7.524   1.00 22.60  ? 385 ALA   C O     1 
ATOM   6472  C  CB    . ALA   B 1  385 ? 13.721  16.628  10.107  1.00 17.16  ? 385 ALA   C CB    1 
ATOM   6473  N  N     . GLU   B 1  386 ? 11.377  15.493  8.011   1.00 23.34  ? 386 GLU   C N     1 
ATOM   6474  C  CA    . GLU   B 1  386 ? 10.787  14.325  7.371   1.00 23.63  ? 386 GLU   C CA    1 
ATOM   6475  C  C     . GLU   B 1  386 ? 11.150  14.252  5.896   1.00 21.45  ? 386 GLU   C C     1 
ATOM   6476  O  O     . GLU   B 1  386 ? 11.389  13.165  5.370   1.00 23.84  ? 386 GLU   C O     1 
ATOM   6477  C  CB    . GLU   B 1  386 ? 9.274   14.345  7.525   1.00 20.99  ? 386 GLU   C CB    1 
ATOM   6478  C  CG    . GLU   B 1  386 ? 8.757   14.421  8.920   1.00 15.84  ? 386 GLU   C CG    1 
ATOM   6479  C  CD    . GLU   B 1  386 ? 7.266   14.561  8.903   1.00 28.65  ? 386 GLU   C CD    1 
ATOM   6480  O  OE1   . GLU   B 1  386 ? 6.644   13.965  7.983   1.00 31.09  ? 386 GLU   C OE1   1 
ATOM   6481  O  OE2   . GLU   B 1  386 ? 6.716   15.276  9.781   1.00 31.99  ? 386 GLU   C OE2   1 
ATOM   6482  N  N     . ALA   B 1  387 ? 11.175  15.391  5.207   1.00 19.06  ? 387 ALA   C N     1 
ATOM   6483  C  CA    . ALA   B 1  387 ? 11.552  15.379  3.798   1.00 20.81  ? 387 ALA   C CA    1 
ATOM   6484  C  C     . ALA   B 1  387 ? 12.955  14.824  3.623   1.00 23.79  ? 387 ALA   C C     1 
ATOM   6485  O  O     . ALA   B 1  387 ? 13.210  14.025  2.708   1.00 25.81  ? 387 ALA   C O     1 
ATOM   6486  C  CB    . ALA   B 1  387 ? 11.463  16.784  3.200   1.00 23.84  ? 387 ALA   C CB    1 
ATOM   6487  N  N     . TRP   B 1  388 ? 13.875  15.221  4.506   1.00 21.31  ? 388 TRP   C N     1 
ATOM   6488  C  CA    . TRP   B 1  388 ? 15.221  14.659  4.476   1.00 19.90  ? 388 TRP   C CA    1 
ATOM   6489  C  C     . TRP   B 1  388 ? 15.183  13.143  4.623   1.00 21.87  ? 388 TRP   C C     1 
ATOM   6490  O  O     . TRP   B 1  388 ? 15.839  12.418  3.868   1.00 23.69  ? 388 TRP   C O     1 
ATOM   6491  C  CB    . TRP   B 1  388 ? 16.084  15.267  5.581   1.00 23.22  ? 388 TRP   C CB    1 
ATOM   6492  C  CG    . TRP   B 1  388 ? 16.293  16.756  5.495   1.00 22.23  ? 388 TRP   C CG    1 
ATOM   6493  C  CD1   . TRP   B 1  388 ? 16.184  17.666  6.521   1.00 21.35  ? 388 TRP   C CD1   1 
ATOM   6494  C  CD2   . TRP   B 1  388 ? 16.652  17.503  4.336   1.00 17.77  ? 388 TRP   C CD2   1 
ATOM   6495  N  NE1   . TRP   B 1  388 ? 16.461  18.928  6.063   1.00 24.08  ? 388 TRP   C NE1   1 
ATOM   6496  C  CE2   . TRP   B 1  388 ? 16.747  18.857  4.725   1.00 22.01  ? 388 TRP   C CE2   1 
ATOM   6497  C  CE3   . TRP   B 1  388 ? 16.911  17.162  3.011   1.00 22.53  ? 388 TRP   C CE3   1 
ATOM   6498  C  CZ2   . TRP   B 1  388 ? 17.092  19.865  3.834   1.00 25.81  ? 388 TRP   C CZ2   1 
ATOM   6499  C  CZ3   . TRP   B 1  388 ? 17.255  18.171  2.123   1.00 29.74  ? 388 TRP   C CZ3   1 
ATOM   6500  C  CH2   . TRP   B 1  388 ? 17.346  19.503  2.540   1.00 25.51  ? 388 TRP   C CH2   1 
ATOM   6501  N  N     . ALA   B 1  389 ? 14.414  12.637  5.586   1.00 24.57  ? 389 ALA   C N     1 
ATOM   6502  C  CA    . ALA   B 1  389 ? 14.392  11.195  5.801   1.00 26.23  ? 389 ALA   C CA    1 
ATOM   6503  C  C     . ALA   B 1  389 ? 13.911  10.457  4.553   1.00 26.96  ? 389 ALA   C C     1 
ATOM   6504  O  O     . ALA   B 1  389 ? 14.535  9.490   4.104   1.00 26.97  ? 389 ALA   C O     1 
ATOM   6505  C  CB    . ALA   B 1  389 ? 13.518  10.866  6.998   1.00 15.47  ? 389 ALA   C CB    1 
ATOM   6506  N  N     . ARG   B 1  390 ? 12.812  10.907  3.964   1.00 18.77  ? 390 ARG   C N     1 
ATOM   6507  C  CA    . ARG   B 1  390 ? 12.325  10.234  2.776   1.00 19.92  ? 390 ARG   C CA    1 
ATOM   6508  C  C     . ARG   B 1  390 ? 13.410  10.132  1.703   1.00 28.04  ? 390 ARG   C C     1 
ATOM   6509  O  O     . ARG   B 1  390 ? 13.622  9.061   1.115   1.00 28.50  ? 390 ARG   C O     1 
ATOM   6510  C  CB    . ARG   B 1  390 ? 11.083  10.954  2.264   1.00 19.80  ? 390 ARG   C CB    1 
ATOM   6511  C  CG    . ARG   B 1  390 ? 9.940   10.862  3.238   1.00 14.61  ? 390 ARG   C CG    1 
ATOM   6512  C  CD    . ARG   B 1  390 ? 8.632   11.134  2.589   1.00 8.84   ? 390 ARG   C CD    1 
ATOM   6513  N  NE    . ARG   B 1  390 ? 8.533   12.462  2.006   1.00 12.77  ? 390 ARG   C NE    1 
ATOM   6514  C  CZ    . ARG   B 1  390 ? 8.284   13.557  2.711   1.00 22.47  ? 390 ARG   C CZ    1 
ATOM   6515  N  NH1   . ARG   B 1  390 ? 8.217   13.522  4.033   1.00 22.62  ? 390 ARG   C NH1   1 
ATOM   6516  N  NH2   . ARG   B 1  390 ? 8.079   14.712  2.075   1.00 19.76  ? 390 ARG   C NH2   1 
ATOM   6517  N  N     . LEU   B 1  391 ? 14.118  11.233  1.435   1.00 25.32  ? 391 LEU   C N     1 
ATOM   6518  C  CA    . LEU   B 1  391 ? 15.203  11.162  0.459   1.00 26.09  ? 391 LEU   C CA    1 
ATOM   6519  C  C     . LEU   B 1  391 ? 16.304  10.239  0.952   1.00 26.95  ? 391 LEU   C C     1 
ATOM   6520  O  O     . LEU   B 1  391 ? 16.805  9.389   0.203   1.00 26.53  ? 391 LEU   C O     1 
ATOM   6521  C  CB    . LEU   B 1  391 ? 15.773  12.549  0.153   1.00 23.29  ? 391 LEU   C CB    1 
ATOM   6522  C  CG    . LEU   B 1  391 ? 15.200  13.259  -1.072  1.00 26.24  ? 391 LEU   C CG    1 
ATOM   6523  C  CD1   . LEU   B 1  391 ? 15.770  14.646  -1.219  1.00 30.42  ? 391 LEU   C CD1   1 
ATOM   6524  C  CD2   . LEU   B 1  391 ? 15.404  12.468  -2.331  1.00 22.25  ? 391 LEU   C CD2   1 
ATOM   6525  N  N     . ASP   B 1  392 ? 16.694  10.387  2.222   1.00 26.45  ? 392 ASP   C N     1 
ATOM   6526  C  CA    . ASP   B 1  392 ? 17.739  9.530   2.770   1.00 23.23  ? 392 ASP   C CA    1 
ATOM   6527  C  C     . ASP   B 1  392 ? 17.351  8.054   2.689   1.00 27.64  ? 392 ASP   C C     1 
ATOM   6528  O  O     . ASP   B 1  392 ? 18.218  7.176   2.569   1.00 26.69  ? 392 ASP   C O     1 
ATOM   6529  C  CB    . ASP   B 1  392 ? 18.044  9.950   4.196   1.00 19.25  ? 392 ASP   C CB    1 
ATOM   6530  C  CG    . ASP   B 1  392 ? 18.840  11.218  4.249   1.00 29.05  ? 392 ASP   C CG    1 
ATOM   6531  O  OD1   . ASP   B 1  392 ? 19.529  11.485  3.248   1.00 24.85  ? 392 ASP   C OD1   1 
ATOM   6532  O  OD2   . ASP   B 1  392 ? 18.789  11.944  5.274   1.00 33.92  ? 392 ASP   C OD2   1 
ATOM   6533  N  N     . HIS   B 1  393 ? 16.054  7.761   2.704   1.00 31.67  ? 393 HIS   C N     1 
ATOM   6534  C  CA    . HIS   B 1  393 ? 15.642  6.374   2.585   1.00 28.95  ? 393 HIS   C CA    1 
ATOM   6535  C  C     . HIS   B 1  393 ? 15.794  5.871   1.153   1.00 31.46  ? 393 HIS   C C     1 
ATOM   6536  O  O     . HIS   B 1  393 ? 16.341  4.781   0.929   1.00 31.76  ? 393 HIS   C O     1 
ATOM   6537  C  CB    . HIS   B 1  393 ? 14.205  6.187   3.058   1.00 24.41  ? 393 HIS   C CB    1 
ATOM   6538  C  CG    . HIS   B 1  393 ? 13.791  4.758   3.029   1.00 32.04  ? 393 HIS   C CG    1 
ATOM   6539  N  ND1   . HIS   B 1  393 ? 14.585  3.761   3.553   1.00 36.39  ? 393 HIS   C ND1   1 
ATOM   6540  C  CD2   . HIS   B 1  393 ? 12.728  4.140   2.466   1.00 30.52  ? 393 HIS   C CD2   1 
ATOM   6541  C  CE1   . HIS   B 1  393 ? 14.008  2.592   3.347   1.00 39.88  ? 393 HIS   C CE1   1 
ATOM   6542  N  NE2   . HIS   B 1  393 ? 12.883  2.793   2.685   1.00 31.21  ? 393 HIS   C NE2   1 
ATOM   6543  N  N     . LYS   B 1  394 ? 15.291  6.638   0.170   1.00 23.87  ? 394 LYS   C N     1 
ATOM   6544  C  CA    . LYS   B 1  394 ? 15.475  6.242   -1.222  1.00 19.30  ? 394 LYS   C CA    1 
ATOM   6545  C  C     . LYS   B 1  394 ? 16.953  6.135   -1.551  1.00 21.72  ? 394 LYS   C C     1 
ATOM   6546  O  O     . LYS   B 1  394 ? 17.379  5.191   -2.223  1.00 22.05  ? 394 LYS   C O     1 
ATOM   6547  C  CB    . LYS   B 1  394 ? 14.764  7.221   -2.152  1.00 17.38  ? 394 LYS   C CB    1 
ATOM   6548  C  CG    . LYS   B 1  394 ? 13.291  6.867   -2.301  1.00 20.27  ? 394 LYS   C CG    1 
ATOM   6549  C  CD    . LYS   B 1  394 ? 12.372  8.054   -2.548  1.00 13.97  ? 394 LYS   C CD    1 
ATOM   6550  C  CE    . LYS   B 1  394 ? 10.911  7.576   -2.640  1.00 22.18  ? 394 LYS   C CE    1 
ATOM   6551  N  NZ    . LYS   B 1  394 ? 9.957   8.589   -3.205  1.00 26.00  ? 394 LYS   C NZ    1 
ATOM   6552  N  N     . PHE   B 1  395 ? 17.764  7.057   -1.033  1.00 20.58  ? 395 PHE   C N     1 
ATOM   6553  C  CA    . PHE   B 1  395 ? 19.199  6.957   -1.233  1.00 18.34  ? 395 PHE   C CA    1 
ATOM   6554  C  C     . PHE   B 1  395 ? 19.741  5.635   -0.687  1.00 26.61  ? 395 PHE   C C     1 
ATOM   6555  O  O     . PHE   B 1  395 ? 20.478  4.917   -1.373  1.00 23.89  ? 395 PHE   C O     1 
ATOM   6556  C  CB    . PHE   B 1  395 ? 19.877  8.154   -0.583  1.00 19.57  ? 395 PHE   C CB    1 
ATOM   6557  C  CG    . PHE   B 1  395 ? 21.388  8.124   -0.654  1.00 26.59  ? 395 PHE   C CG    1 
ATOM   6558  C  CD1   . PHE   B 1  395 ? 22.129  7.345   0.243   1.00 23.50  ? 395 PHE   C CD1   1 
ATOM   6559  C  CD2   . PHE   B 1  395 ? 22.071  8.902   -1.589  1.00 20.34  ? 395 PHE   C CD2   1 
ATOM   6560  C  CE1   . PHE   B 1  395 ? 23.512  7.335   0.200   1.00 21.19  ? 395 PHE   C CE1   1 
ATOM   6561  C  CE2   . PHE   B 1  395 ? 23.458  8.904   -1.630  1.00 18.45  ? 395 PHE   C CE2   1 
ATOM   6562  C  CZ    . PHE   B 1  395 ? 24.182  8.126   -0.748  1.00 20.46  ? 395 PHE   C CZ    1 
ATOM   6563  N  N     . ASP   B 1  396 ? 19.386  5.292   0.554   1.00 29.62  ? 396 ASP   C N     1 
ATOM   6564  C  CA    . ASP   B 1  396 ? 20.005  4.136   1.195   1.00 24.10  ? 396 ASP   C CA    1 
ATOM   6565  C  C     . ASP   B 1  396 ? 19.727  2.862   0.414   1.00 26.22  ? 396 ASP   C C     1 
ATOM   6566  O  O     . ASP   B 1  396 ? 20.607  1.995   0.296   1.00 25.72  ? 396 ASP   C O     1 
ATOM   6567  C  CB    . ASP   B 1  396 ? 19.504  3.995   2.628   1.00 24.13  ? 396 ASP   C CB    1 
ATOM   6568  C  CG    . ASP   B 1  396 ? 20.047  5.053   3.551   1.00 27.98  ? 396 ASP   C CG    1 
ATOM   6569  O  OD1   . ASP   B 1  396 ? 21.145  5.580   3.293   1.00 39.51  ? 396 ASP   C OD1   1 
ATOM   6570  O  OD2   . ASP   B 1  396 ? 19.375  5.354   4.553   1.00 28.49  ? 396 ASP   C OD2   1 
ATOM   6571  N  N     . LEU   B 1  397 ? 18.503  2.729   -0.121  1.00 22.75  ? 397 LEU   C N     1 
ATOM   6572  C  CA    . LEU   B 1  397 ? 18.122  1.510   -0.833  1.00 24.69  ? 397 LEU   C CA    1 
ATOM   6573  C  C     . LEU   B 1  397 ? 19.065  1.234   -2.002  1.00 31.40  ? 397 LEU   C C     1 
ATOM   6574  O  O     . LEU   B 1  397 ? 19.651  0.150   -2.097  1.00 32.96  ? 397 LEU   C O     1 
ATOM   6575  C  CB    . LEU   B 1  397 ? 16.681  1.610   -1.317  1.00 19.54  ? 397 LEU   C CB    1 
ATOM   6576  C  CG    . LEU   B 1  397 ? 15.643  1.522   -0.206  1.00 20.21  ? 397 LEU   C CG    1 
ATOM   6577  C  CD1   . LEU   B 1  397 ? 14.241  1.345   -0.735  1.00 19.91  ? 397 LEU   C CD1   1 
ATOM   6578  C  CD2   . LEU   B 1  397 ? 16.021  0.368   0.672   1.00 18.16  ? 397 LEU   C CD2   1 
ATOM   6579  N  N     . MET   B 1  398 ? 19.252  2.230   -2.877  1.00 30.16  ? 398 MET   C N     1 
ATOM   6580  C  CA    . MET   B 1  398 ? 20.112  2.078   -4.048  1.00 23.15  ? 398 MET   C CA    1 
ATOM   6581  C  C     . MET   B 1  398 ? 21.582  1.974   -3.666  1.00 25.89  ? 398 MET   C C     1 
ATOM   6582  O  O     . MET   B 1  398 ? 22.303  1.097   -4.155  1.00 27.49  ? 398 MET   C O     1 
ATOM   6583  C  CB    . MET   B 1  398 ? 19.901  3.252   -4.993  1.00 23.08  ? 398 MET   C CB    1 
ATOM   6584  C  CG    . MET   B 1  398 ? 18.498  3.343   -5.560  1.00 21.40  ? 398 MET   C CG    1 
ATOM   6585  S  SD    . MET   B 1  398 ? 18.335  4.661   -6.798  1.00 34.60  ? 398 MET   C SD    1 
ATOM   6586  C  CE    . MET   B 1  398 ? 18.369  6.118   -5.773  1.00 19.38  ? 398 MET   C CE    1 
ATOM   6587  N  N     . TYR   B 1  399 ? 22.060  2.873   -2.806  1.00 29.38  ? 399 TYR   C N     1 
ATOM   6588  C  CA    . TYR   B 1  399 ? 23.489  2.859   -2.501  1.00 26.15  ? 399 TYR   C CA    1 
ATOM   6589  C  C     . TYR   B 1  399 ? 23.902  1.591   -1.760  1.00 30.46  ? 399 TYR   C C     1 
ATOM   6590  O  O     . TYR   B 1  399 ? 25.075  1.202   -1.809  1.00 35.36  ? 399 TYR   C O     1 
ATOM   6591  C  CB    . TYR   B 1  399 ? 23.887  4.088   -1.707  1.00 14.60  ? 399 TYR   C CB    1 
ATOM   6592  C  CG    . TYR   B 1  399 ? 25.369  4.261   -1.678  1.00 19.34  ? 399 TYR   C CG    1 
ATOM   6593  C  CD1   . TYR   B 1  399 ? 26.040  4.884   -2.716  1.00 22.89  ? 399 TYR   C CD1   1 
ATOM   6594  C  CD2   . TYR   B 1  399 ? 26.111  3.776   -0.624  1.00 23.06  ? 399 TYR   C CD2   1 
ATOM   6595  C  CE1   . TYR   B 1  399 ? 27.418  5.022   -2.686  1.00 23.61  ? 399 TYR   C CE1   1 
ATOM   6596  C  CE2   . TYR   B 1  399 ? 27.466  3.918   -0.572  1.00 18.96  ? 399 TYR   C CE2   1 
ATOM   6597  C  CZ    . TYR   B 1  399 ? 28.126  4.539   -1.599  1.00 29.15  ? 399 TYR   C CZ    1 
ATOM   6598  O  OH    . TYR   B 1  399 ? 29.500  4.648   -1.519  1.00 33.40  ? 399 TYR   C OH    1 
ATOM   6599  N  N     . ALA   B 1  400 ? 22.962  0.919   -1.090  1.00 30.10  ? 400 ALA   C N     1 
ATOM   6600  C  CA    . ALA   B 1  400 ? 23.288  -0.364  -0.483  1.00 26.73  ? 400 ALA   C CA    1 
ATOM   6601  C  C     . ALA   B 1  400 ? 23.668  -1.397  -1.542  1.00 33.92  ? 400 ALA   C C     1 
ATOM   6602  O  O     . ALA   B 1  400 ? 24.409  -2.341  -1.253  1.00 40.11  ? 400 ALA   C O     1 
ATOM   6603  C  CB    . ALA   B 1  400 ? 22.105  -0.851  0.358   1.00 28.94  ? 400 ALA   C CB    1 
ATOM   6604  N  N     . LYS   B 1  401 ? 23.153  -1.254  -2.763  1.00 25.28  ? 401 LYS   C N     1 
ATOM   6605  C  CA    . LYS   B 1  401 ? 23.482  -2.161  -3.852  1.00 28.98  ? 401 LYS   C CA    1 
ATOM   6606  C  C     . LYS   B 1  401 ? 24.365  -1.489  -4.886  1.00 30.15  ? 401 LYS   C C     1 
ATOM   6607  O  O     . LYS   B 1  401 ? 24.588  -2.056  -5.958  1.00 32.50  ? 401 LYS   C O     1 
ATOM   6608  C  CB    . LYS   B 1  401 ? 22.216  -2.718  -4.523  1.00 27.92  ? 401 LYS   C CB    1 
ATOM   6609  C  CG    . LYS   B 1  401 ? 21.319  -3.538  -3.596  1.00 32.90  ? 401 LYS   C CG    1 
ATOM   6610  C  CD    . LYS   B 1  401 ? 22.131  -4.211  -2.485  1.00 38.53  ? 401 LYS   C CD    1 
ATOM   6611  C  CE    . LYS   B 1  401 ? 21.332  -4.351  -1.198  1.00 32.67  ? 401 LYS   C CE    1 
ATOM   6612  N  NZ    . LYS   B 1  401 ? 19.921  -4.629  -1.530  1.00 30.94  ? 401 LYS   C NZ    1 
ATOM   6613  N  N     . ARG   B 1  402 ? 24.866  -0.297  -4.589  1.00 26.63  ? 402 ARG   C N     1 
ATOM   6614  C  CA    . ARG   B 1  402 ? 25.691  0.496   -5.496  1.00 28.85  ? 402 ARG   C CA    1 
ATOM   6615  C  C     . ARG   B 1  402 ? 25.016  0.798   -6.832  1.00 27.04  ? 402 ARG   C C     1 
ATOM   6616  O  O     . ARG   B 1  402 ? 25.688  1.255   -7.767  1.00 31.45  ? 402 ARG   C O     1 
ATOM   6617  C  CB    . ARG   B 1  402 ? 27.035  -0.172  -5.756  1.00 17.53  ? 402 ARG   C CB    1 
ATOM   6618  C  CG    . ARG   B 1  402 ? 28.154  0.446   -4.968  1.00 26.53  ? 402 ARG   C CG    1 
ATOM   6619  C  CD    . ARG   B 1  402 ? 27.664  0.844   -3.568  1.00 30.82  ? 402 ARG   C CD    1 
ATOM   6620  N  NE    . ARG   B 1  402 ? 28.779  1.011   -2.642  1.00 35.45  ? 402 ARG   C NE    1 
ATOM   6621  C  CZ    . ARG   B 1  402 ? 28.677  1.008   -1.318  1.00 31.54  ? 402 ARG   C CZ    1 
ATOM   6622  N  NH1   . ARG   B 1  402 ? 27.509  0.874   -0.710  1.00 21.85  ? 402 ARG   C NH1   1 
ATOM   6623  N  NH2   . ARG   B 1  402 ? 29.778  1.145   -0.587  1.00 36.73  ? 402 ARG   C NH2   1 
ATOM   6624  N  N     . ALA   B 1  403 ? 23.708  0.586   -6.949  1.00 22.39  ? 403 ALA   C N     1 
ATOM   6625  C  CA    . ALA   B 1  403 ? 23.040  0.756   -8.233  1.00 25.83  ? 403 ALA   C CA    1 
ATOM   6626  C  C     . ALA   B 1  403 ? 23.232  2.163   -8.768  1.00 25.18  ? 403 ALA   C C     1 
ATOM   6627  O  O     . ALA   B 1  403 ? 23.051  3.142   -8.038  1.00 36.61  ? 403 ALA   C O     1 
ATOM   6628  C  CB    . ALA   B 1  403 ? 21.549  0.461   -8.090  1.00 29.25  ? 403 ALA   C CB    1 
ATOM   6629  N  N     . PHE   B 1  404 ? 23.579  2.259   -10.052 1.00 20.51  ? 404 PHE   C N     1 
ATOM   6630  C  CA    . PHE   B 1  404 ? 23.753  3.528   -10.760 1.00 19.88  ? 404 PHE   C CA    1 
ATOM   6631  C  C     . PHE   B 1  404 ? 24.995  4.265   -10.292 1.00 20.87  ? 404 PHE   C C     1 
ATOM   6632  O  O     . PHE   B 1  404 ? 25.390  5.266   -10.886 1.00 23.78  ? 404 PHE   C O     1 
ATOM   6633  C  CB    . PHE   B 1  404 ? 22.548  4.447   -10.592 1.00 17.54  ? 404 PHE   C CB    1 
ATOM   6634  C  CG    . PHE   B 1  404 ? 21.275  3.896   -11.144 1.00 24.16  ? 404 PHE   C CG    1 
ATOM   6635  C  CD1   . PHE   B 1  404 ? 20.919  4.125   -12.470 1.00 25.97  ? 404 PHE   C CD1   1 
ATOM   6636  C  CD2   . PHE   B 1  404 ? 20.400  3.182   -10.328 1.00 25.75  ? 404 PHE   C CD2   1 
ATOM   6637  C  CE1   . PHE   B 1  404 ? 19.716  3.628   -12.989 1.00 28.44  ? 404 PHE   C CE1   1 
ATOM   6638  C  CE2   . PHE   B 1  404 ? 19.199  2.676   -10.837 1.00 26.62  ? 404 PHE   C CE2   1 
ATOM   6639  C  CZ    . PHE   B 1  404 ? 18.857  2.898   -12.167 1.00 28.59  ? 404 PHE   C CZ    1 
ATOM   6640  N  N     . VAL   B 1  405 ? 25.624  3.789   -9.223  1.00 22.36  ? 405 VAL   C N     1 
ATOM   6641  C  CA    . VAL   B 1  405 ? 26.790  4.493   -8.729  1.00 21.36  ? 405 VAL   C CA    1 
ATOM   6642  C  C     . VAL   B 1  405 ? 27.889  4.525   -9.785  1.00 25.70  ? 405 VAL   C C     1 
ATOM   6643  O  O     . VAL   B 1  405 ? 28.728  5.434   -9.787  1.00 27.91  ? 405 VAL   C O     1 
ATOM   6644  C  CB    . VAL   B 1  405 ? 27.260  3.860   -7.397  1.00 20.04  ? 405 VAL   C CB    1 
ATOM   6645  C  CG1   . VAL   B 1  405 ? 28.594  4.422   -6.984  1.00 21.70  ? 405 VAL   C CG1   1 
ATOM   6646  C  CG2   . VAL   B 1  405 ? 26.242  4.114   -6.309  1.00 19.22  ? 405 VAL   C CG2   1 
ATOM   6647  N  N     . HIS   B 1  406 ? 27.900  3.564   -10.713 1.00 28.77  ? 406 HIS   C N     1 
ATOM   6648  C  CA    . HIS   B 1  406 ? 28.985  3.556   -11.696 1.00 25.49  ? 406 HIS   C CA    1 
ATOM   6649  C  C     . HIS   B 1  406 ? 28.922  4.772   -12.609 1.00 23.05  ? 406 HIS   C C     1 
ATOM   6650  O  O     . HIS   B 1  406 ? 29.965  5.271   -13.024 1.00 25.00  ? 406 HIS   C O     1 
ATOM   6651  C  CB    . HIS   B 1  406 ? 28.984  2.252   -12.512 1.00 23.58  ? 406 HIS   C CB    1 
ATOM   6652  C  CG    . HIS   B 1  406 ? 27.793  2.076   -13.400 1.00 22.27  ? 406 HIS   C CG    1 
ATOM   6653  N  ND1   . HIS   B 1  406 ? 27.864  2.209   -14.769 1.00 22.78  ? 406 HIS   C ND1   1 
ATOM   6654  C  CD2   . HIS   B 1  406 ? 26.505  1.763   -13.119 1.00 27.56  ? 406 HIS   C CD2   1 
ATOM   6655  C  CE1   . HIS   B 1  406 ? 26.669  1.998   -15.294 1.00 31.58  ? 406 HIS   C CE1   1 
ATOM   6656  N  NE2   . HIS   B 1  406 ? 25.826  1.722   -14.313 1.00 33.06  ? 406 HIS   C NE2   1 
ATOM   6657  N  N     . TRP   B 1  407 ? 27.722  5.275   -12.916 1.00 23.43  ? 407 TRP   C N     1 
ATOM   6658  C  CA    . TRP   B 1  407 ? 27.616  6.507   -13.693 1.00 23.40  ? 407 TRP   C CA    1 
ATOM   6659  C  C     . TRP   B 1  407 ? 28.368  7.654   -13.038 1.00 23.94  ? 407 TRP   C C     1 
ATOM   6660  O  O     . TRP   B 1  407 ? 28.937  8.504   -13.727 1.00 20.77  ? 407 TRP   C O     1 
ATOM   6661  C  CB    . TRP   B 1  407 ? 26.149  6.887   -13.893 1.00 23.74  ? 407 TRP   C CB    1 
ATOM   6662  C  CG    . TRP   B 1  407 ? 25.450  5.892   -14.759 1.00 30.53  ? 407 TRP   C CG    1 
ATOM   6663  C  CD1   . TRP   B 1  407 ? 24.682  4.852   -14.345 1.00 31.12  ? 407 TRP   C CD1   1 
ATOM   6664  C  CD2   . TRP   B 1  407 ? 25.516  5.798   -16.193 1.00 26.98  ? 407 TRP   C CD2   1 
ATOM   6665  N  NE1   . TRP   B 1  407 ? 24.254  4.120   -15.427 1.00 33.53  ? 407 TRP   C NE1   1 
ATOM   6666  C  CE2   . TRP   B 1  407 ? 24.753  4.682   -16.571 1.00 32.21  ? 407 TRP   C CE2   1 
ATOM   6667  C  CE3   . TRP   B 1  407 ? 26.149  6.545   -17.185 1.00 20.65  ? 407 TRP   C CE3   1 
ATOM   6668  C  CZ2   . TRP   B 1  407 ? 24.585  4.308   -17.903 1.00 37.33  ? 407 TRP   C CZ2   1 
ATOM   6669  C  CZ3   . TRP   B 1  407 ? 25.983  6.172   -18.498 1.00 29.68  ? 407 TRP   C CZ3   1 
ATOM   6670  C  CH2   . TRP   B 1  407 ? 25.208  5.063   -18.848 1.00 31.79  ? 407 TRP   C CH2   1 
ATOM   6671  N  N     . TYR   B 1  408 ? 28.385  7.699   -11.716 1.00 23.04  ? 408 TYR   C N     1 
ATOM   6672  C  CA    . TYR   B 1  408 ? 29.038  8.819   -11.061 1.00 24.22  ? 408 TYR   C CA    1 
ATOM   6673  C  C     . TYR   B 1  408 ? 30.546  8.616   -11.022 1.00 24.35  ? 408 TYR   C C     1 
ATOM   6674  O  O     . TYR   B 1  408 ? 31.316  9.542   -11.304 1.00 21.75  ? 408 TYR   C O     1 
ATOM   6675  C  CB    . TYR   B 1  408 ? 28.453  9.001   -9.657  1.00 21.42  ? 408 TYR   C CB    1 
ATOM   6676  C  CG    . TYR   B 1  408 ? 26.996  9.410   -9.664  1.00 24.43  ? 408 TYR   C CG    1 
ATOM   6677  C  CD1   . TYR   B 1  408 ? 26.012  8.507   -10.016 1.00 20.66  ? 408 TYR   C CD1   1 
ATOM   6678  C  CD2   . TYR   B 1  408 ? 26.606  10.705  -9.317  1.00 30.13  ? 408 TYR   C CD2   1 
ATOM   6679  C  CE1   . TYR   B 1  408 ? 24.679  8.869   -10.020 1.00 21.59  ? 408 TYR   C CE1   1 
ATOM   6680  C  CE2   . TYR   B 1  408 ? 25.268  11.078  -9.310  1.00 24.80  ? 408 TYR   C CE2   1 
ATOM   6681  C  CZ    . TYR   B 1  408 ? 24.307  10.155  -9.663  1.00 26.92  ? 408 TYR   C CZ    1 
ATOM   6682  O  OH    . TYR   B 1  408 ? 22.976  10.515  -9.670  1.00 26.27  ? 408 TYR   C OH    1 
ATOM   6683  N  N     . VAL   B 1  409 ? 30.970  7.394   -10.696 1.00 26.01  ? 409 VAL   C N     1 
ATOM   6684  C  CA    . VAL   B 1  409 ? 32.390  7.077   -10.593 1.00 22.21  ? 409 VAL   C CA    1 
ATOM   6685  C  C     . VAL   B 1  409 ? 33.094  7.322   -11.916 1.00 23.51  ? 409 VAL   C C     1 
ATOM   6686  O  O     . VAL   B 1  409 ? 34.237  7.794   -11.948 1.00 31.90  ? 409 VAL   C O     1 
ATOM   6687  C  CB    . VAL   B 1  409 ? 32.576  5.620   -10.141 1.00 22.52  ? 409 VAL   C CB    1 
ATOM   6688  C  CG1   . VAL   B 1  409 ? 34.005  5.183   -10.413 1.00 22.51  ? 409 VAL   C CG1   1 
ATOM   6689  C  CG2   . VAL   B 1  409 ? 32.182  5.441   -8.683  1.00 13.46  ? 409 VAL   C CG2   1 
ATOM   6690  N  N     . GLY   B 1  410 ? 32.427  7.000   -13.023 1.00 20.40  ? 410 GLY   C N     1 
ATOM   6691  C  CA    . GLY   B 1  410 ? 32.994  7.100   -14.342 1.00 21.98  ? 410 GLY   C CA    1 
ATOM   6692  C  C     . GLY   B 1  410 ? 33.219  8.508   -14.818 1.00 29.72  ? 410 GLY   C C     1 
ATOM   6693  O  O     . GLY   B 1  410 ? 33.882  8.705   -15.840 1.00 39.14  ? 410 GLY   C O     1 
ATOM   6694  N  N     . GLU   B 1  411 ? 32.683  9.490   -14.108 1.00 35.10  ? 411 GLU   C N     1 
ATOM   6695  C  CA    . GLU   B 1  411 ? 32.962  10.886  -14.385 1.00 27.63  ? 411 GLU   C CA    1 
ATOM   6696  C  C     . GLU   B 1  411 ? 33.806  11.524  -13.282 1.00 29.31  ? 411 GLU   C C     1 
ATOM   6697  O  O     . GLU   B 1  411 ? 33.814  12.754  -13.141 1.00 39.18  ? 411 GLU   C O     1 
ATOM   6698  C  CB    . GLU   B 1  411 ? 31.648  11.632  -14.577 1.00 27.53  ? 411 GLU   C CB    1 
ATOM   6699  C  CG    . GLU   B 1  411 ? 30.739  10.999  -15.609 1.00 25.91  ? 411 GLU   C CG    1 
ATOM   6700  C  CD    . GLU   B 1  411 ? 30.829  11.702  -16.926 1.00 29.05  ? 411 GLU   C CD    1 
ATOM   6701  O  OE1   . GLU   B 1  411 ? 31.713  12.568  -17.056 1.00 37.23  ? 411 GLU   C OE1   1 
ATOM   6702  O  OE2   . GLU   B 1  411 ? 30.005  11.420  -17.811 1.00 22.47  ? 411 GLU   C OE2   1 
ATOM   6703  N  N     . GLY   B 1  412 ? 34.509  10.712  -12.489 1.00 20.70  ? 412 GLY   C N     1 
ATOM   6704  C  CA    . GLY   B 1  412 ? 35.380  11.246  -11.459 1.00 29.77  ? 412 GLY   C CA    1 
ATOM   6705  C  C     . GLY   B 1  412 ? 35.062  10.818  -10.038 1.00 32.41  ? 412 GLY   C C     1 
ATOM   6706  O  O     . GLY   B 1  412 ? 35.943  10.334  -9.327  1.00 38.59  ? 412 GLY   C O     1 
ATOM   6707  N  N     . MET   B 1  413 ? 33.811  10.983  -9.611  1.00 29.53  ? 413 MET   C N     1 
ATOM   6708  C  CA    . MET   B 1  413 ? 33.464  10.804  -8.206  1.00 34.78  ? 413 MET   C CA    1 
ATOM   6709  C  C     . MET   B 1  413 ? 33.971  9.461   -7.671  1.00 28.54  ? 413 MET   C C     1 
ATOM   6710  O  O     . MET   B 1  413 ? 34.082  8.475   -8.401  1.00 27.68  ? 413 MET   C O     1 
ATOM   6711  C  CB    . MET   B 1  413 ? 31.944  10.957  -8.036  1.00 26.22  ? 413 MET   C CB    1 
ATOM   6712  C  CG    . MET   B 1  413 ? 31.463  12.336  -8.516  1.00 29.94  ? 413 MET   C CG    1 
ATOM   6713  S  SD    . MET   B 1  413 ? 29.815  12.839  -7.991  1.00 23.22  ? 413 MET   C SD    1 
ATOM   6714  C  CE    . MET   B 1  413 ? 29.895  12.570  -6.180  1.00 30.62  ? 413 MET   C CE    1 
ATOM   6715  N  N     . GLU   B 1  414 ? 34.353  9.449   -6.397  1.00 27.01  ? 414 GLU   C N     1 
ATOM   6716  C  CA    . GLU   B 1  414 ? 34.718  8.223   -5.707  1.00 26.90  ? 414 GLU   C CA    1 
ATOM   6717  C  C     . GLU   B 1  414 ? 33.542  7.803   -4.860  1.00 28.95  ? 414 GLU   C C     1 
ATOM   6718  O  O     . GLU   B 1  414 ? 32.582  8.547   -4.686  1.00 37.19  ? 414 GLU   C O     1 
ATOM   6719  C  CB    . GLU   B 1  414 ? 35.966  8.407   -4.840  1.00 25.57  ? 414 GLU   C CB    1 
ATOM   6720  C  CG    . GLU   B 1  414 ? 37.165  9.010   -5.582  1.00 33.10  ? 414 GLU   C CG    1 
ATOM   6721  C  CD    . GLU   B 1  414 ? 38.284  9.317   -4.636  1.00 44.24  ? 414 GLU   C CD    1 
ATOM   6722  O  OE1   . GLU   B 1  414 ? 38.064  9.131   -3.422  1.00 56.22  ? 414 GLU   C OE1   1 
ATOM   6723  O  OE2   . GLU   B 1  414 ? 39.373  9.740   -5.082  1.00 43.09  ? 414 GLU   C OE2   1 
ATOM   6724  N  N     . GLU   B 1  415 ? 33.600  6.585   -4.345  1.00 32.28  ? 415 GLU   C N     1 
ATOM   6725  C  CA    . GLU   B 1  415 ? 32.529  6.179   -3.454  1.00 29.04  ? 415 GLU   C CA    1 
ATOM   6726  C  C     . GLU   B 1  415 ? 32.510  7.023   -2.177  1.00 32.96  ? 415 GLU   C C     1 
ATOM   6727  O  O     . GLU   B 1  415 ? 31.474  7.100   -1.509  1.00 36.53  ? 415 GLU   C O     1 
ATOM   6728  C  CB    . GLU   B 1  415 ? 32.661  4.687   -3.142  1.00 31.31  ? 415 GLU   C CB    1 
ATOM   6729  C  CG    . GLU   B 1  415 ? 31.713  3.808   -3.949  1.00 38.80  ? 415 GLU   C CG    1 
ATOM   6730  C  CD    . GLU   B 1  415 ? 31.880  2.338   -3.643  1.00 38.56  ? 415 GLU   C CD    1 
ATOM   6731  O  OE1   . GLU   B 1  415 ? 32.515  2.002   -2.625  1.00 44.02  ? 415 GLU   C OE1   1 
ATOM   6732  O  OE2   . GLU   B 1  415 ? 31.383  1.515   -4.430  1.00 35.69  ? 415 GLU   C OE2   1 
ATOM   6733  N  N     . GLY   B 1  416 ? 33.622  7.690   -1.847  1.00 34.35  ? 416 GLY   C N     1 
ATOM   6734  C  CA    . GLY   B 1  416 ? 33.704  8.461   -0.613  1.00 25.14  ? 416 GLY   C CA    1 
ATOM   6735  C  C     . GLY   B 1  416 ? 32.888  9.740   -0.594  1.00 24.21  ? 416 GLY   C C     1 
ATOM   6736  O  O     . GLY   B 1  416 ? 32.448  10.181  0.466   1.00 26.54  ? 416 GLY   C O     1 
ATOM   6737  N  N     . GLU   B 1  417 ? 32.674  10.371  -1.746  1.00 23.85  ? 417 GLU   C N     1 
ATOM   6738  C  CA    A GLU   B 1  417 ? 31.818  11.550  -1.720  0.43 29.14  ? 417 GLU   C CA    1 
ATOM   6739  C  CA    B GLU   B 1  417 ? 31.815  11.547  -1.769  0.57 29.14  ? 417 GLU   C CA    1 
ATOM   6740  C  C     . GLU   B 1  417 ? 30.358  11.174  -1.491  1.00 34.88  ? 417 GLU   C C     1 
ATOM   6741  O  O     . GLU   B 1  417 ? 29.593  11.987  -0.948  1.00 36.34  ? 417 GLU   C O     1 
ATOM   6742  C  CB    A GLU   B 1  417 ? 31.965  12.375  -2.998  0.43 26.27  ? 417 GLU   C CB    1 
ATOM   6743  C  CB    B GLU   B 1  417 ? 31.978  12.261  -3.111  0.57 26.25  ? 417 GLU   C CB    1 
ATOM   6744  C  CG    A GLU   B 1  417 ? 31.311  13.758  -2.888  0.43 24.35  ? 417 GLU   C CG    1 
ATOM   6745  C  CG    B GLU   B 1  417 ? 33.435  12.290  -3.591  0.57 24.23  ? 417 GLU   C CG    1 
ATOM   6746  C  CD    A GLU   B 1  417 ? 31.702  14.681  -4.024  0.43 24.92  ? 417 GLU   C CD    1 
ATOM   6747  C  CD    B GLU   B 1  417 ? 33.597  12.935  -4.953  0.57 24.64  ? 417 GLU   C CD    1 
ATOM   6748  O  OE1   A GLU   B 1  417 ? 32.496  14.241  -4.880  0.43 26.66  ? 417 GLU   C OE1   1 
ATOM   6749  O  OE1   B GLU   B 1  417 ? 33.082  14.052  -5.135  0.57 27.05  ? 417 GLU   C OE1   1 
ATOM   6750  O  OE2   A GLU   B 1  417 ? 31.228  15.841  -4.062  0.43 23.17  ? 417 GLU   C OE2   1 
ATOM   6751  O  OE2   B GLU   B 1  417 ? 34.226  12.325  -5.842  0.57 20.23  ? 417 GLU   C OE2   1 
ATOM   6752  N  N     . PHE   B 1  418 ? 29.958  9.952   -1.856  1.00 26.00  ? 418 PHE   C N     1 
ATOM   6753  C  CA    . PHE   B 1  418 ? 28.610  9.479   -1.551  1.00 24.57  ? 418 PHE   C CA    1 
ATOM   6754  C  C     . PHE   B 1  418 ? 28.446  9.240   -0.059  1.00 23.92  ? 418 PHE   C C     1 
ATOM   6755  O  O     . PHE   B 1  418 ? 27.571  9.824   0.587   1.00 25.44  ? 418 PHE   C O     1 
ATOM   6756  C  CB    . PHE   B 1  418 ? 28.303  8.193   -2.326  1.00 31.50  ? 418 PHE   C CB    1 
ATOM   6757  C  CG    . PHE   B 1  418 ? 27.838  8.417   -3.751  1.00 27.89  ? 418 PHE   C CG    1 
ATOM   6758  C  CD1   . PHE   B 1  418 ? 28.735  8.730   -4.748  1.00 20.20  ? 418 PHE   C CD1   1 
ATOM   6759  C  CD2   . PHE   B 1  418 ? 26.509  8.289   -4.087  1.00 25.89  ? 418 PHE   C CD2   1 
ATOM   6760  C  CE1   . PHE   B 1  418 ? 28.317  8.928   -6.027  1.00 22.35  ? 418 PHE   C CE1   1 
ATOM   6761  C  CE2   . PHE   B 1  418 ? 26.087  8.478   -5.400  1.00 23.99  ? 418 PHE   C CE2   1 
ATOM   6762  C  CZ    . PHE   B 1  418 ? 26.996  8.793   -6.359  1.00 26.15  ? 418 PHE   C CZ    1 
ATOM   6763  N  N     . SER   B 1  419 ? 29.271  8.367   0.511   1.00 26.77  ? 419 SER   C N     1 
ATOM   6764  C  CA    . SER   B 1  419 ? 29.168  8.122   1.946   1.00 30.85  ? 419 SER   C CA    1 
ATOM   6765  C  C     . SER   B 1  419 ? 29.258  9.427   2.734   1.00 25.90  ? 419 SER   C C     1 
ATOM   6766  O  O     . SER   B 1  419 ? 28.461  9.670   3.645   1.00 29.31  ? 419 SER   C O     1 
ATOM   6767  C  CB    . SER   B 1  419 ? 30.241  7.128   2.391   1.00 24.42  ? 419 SER   C CB    1 
ATOM   6768  O  OG    . SER   B 1  419 ? 31.530  7.589   2.029   1.00 37.28  ? 419 SER   C OG    1 
ATOM   6769  N  N     . GLU   B 1  420 ? 30.179  10.306  2.358   1.00 25.47  ? 420 GLU   C N     1 
ATOM   6770  C  CA    . GLU   B 1  420 ? 30.329  11.564  3.076   1.00 22.78  ? 420 GLU   C CA    1 
ATOM   6771  C  C     . GLU   B 1  420 ? 29.071  12.429  2.964   1.00 26.74  ? 420 GLU   C C     1 
ATOM   6772  O  O     . GLU   B 1  420 ? 28.593  12.972  3.966   1.00 25.35  ? 420 GLU   C O     1 
ATOM   6773  C  CB    . GLU   B 1  420 ? 31.578  12.265  2.553   1.00 26.28  ? 420 GLU   C CB    1 
ATOM   6774  C  CG    . GLU   B 1  420 ? 31.719  13.744  2.806   1.00 33.53  ? 420 GLU   C CG    1 
ATOM   6775  C  CD    . GLU   B 1  420 ? 32.950  14.278  2.095   1.00 50.85  ? 420 GLU   C CD    1 
ATOM   6776  O  OE1   . GLU   B 1  420 ? 34.028  13.643  2.245   1.00 46.29  ? 420 GLU   C OE1   1 
ATOM   6777  O  OE2   . GLU   B 1  420 ? 32.830  15.284  1.355   1.00 43.61  ? 420 GLU   C OE2   1 
ATOM   6778  N  N     . ALA   B 1  421 ? 28.489  12.539  1.768   1.00 23.61  ? 421 ALA   C N     1 
ATOM   6779  C  CA    . ALA   B 1  421 ? 27.243  13.297  1.651   1.00 23.28  ? 421 ALA   C CA    1 
ATOM   6780  C  C     . ALA   B 1  421 ? 26.143  12.711  2.525   1.00 27.82  ? 421 ALA   C C     1 
ATOM   6781  O  O     . ALA   B 1  421 ? 25.369  13.455  3.136   1.00 28.41  ? 421 ALA   C O     1 
ATOM   6782  C  CB    . ALA   B 1  421 ? 26.769  13.341  0.207   1.00 22.52  ? 421 ALA   C CB    1 
ATOM   6783  N  N     . ARG   B 1  422 ? 26.038  11.379  2.573   1.00 21.82  ? 422 ARG   C N     1 
ATOM   6784  C  CA    . ARG   B 1  422 ? 24.988  10.755  3.362   1.00 18.47  ? 422 ARG   C CA    1 
ATOM   6785  C  C     . ARG   B 1  422 ? 25.266  10.907  4.861   1.00 29.48  ? 422 ARG   C C     1 
ATOM   6786  O  O     . ARG   B 1  422 ? 24.338  11.108  5.666   1.00 29.44  ? 422 ARG   C O     1 
ATOM   6787  C  CB    . ARG   B 1  422 ? 24.853  9.288   2.957   1.00 17.89  ? 422 ARG   C CB    1 
ATOM   6788  C  CG    . ARG   B 1  422 ? 23.779  8.489   3.678   1.00 13.69  ? 422 ARG   C CG    1 
ATOM   6789  C  CD    . ARG   B 1  422 ? 22.365  8.878   3.231   1.00 26.68  ? 422 ARG   C CD    1 
ATOM   6790  N  NE    . ARG   B 1  422 ? 21.363  8.220   4.060   1.00 23.30  ? 422 ARG   C NE    1 
ATOM   6791  C  CZ    . ARG   B 1  422 ? 21.056  8.603   5.293   1.00 27.85  ? 422 ARG   C CZ    1 
ATOM   6792  N  NH1   . ARG   B 1  422 ? 21.593  9.690   5.840   1.00 21.74  ? 422 ARG   C NH1   1 
ATOM   6793  N  NH2   . ARG   B 1  422 ? 20.210  7.866   6.005   1.00 23.48  ? 422 ARG   C NH2   1 
ATOM   6794  N  N     . GLU   B 1  423 ? 26.535  10.843  5.263   1.00 25.74  ? 423 GLU   C N     1 
ATOM   6795  C  CA    . GLU   B 1  423 ? 26.821  11.044  6.675   1.00 24.77  ? 423 GLU   C CA    1 
ATOM   6796  C  C     . GLU   B 1  423 ? 26.441  12.459  7.104   1.00 26.43  ? 423 GLU   C C     1 
ATOM   6797  O  O     . GLU   B 1  423 ? 25.935  12.666  8.205   1.00 24.65  ? 423 GLU   C O     1 
ATOM   6798  C  CB    . GLU   B 1  423 ? 28.285  10.732  6.972   1.00 25.22  ? 423 GLU   C CB    1 
ATOM   6799  C  CG    . GLU   B 1  423 ? 28.404  9.503   7.841   1.00 44.57  ? 423 GLU   C CG    1 
ATOM   6800  C  CD    . GLU   B 1  423 ? 27.473  9.580   9.068   1.00 62.33  ? 423 GLU   C CD    1 
ATOM   6801  O  OE1   . GLU   B 1  423 ? 27.132  10.721  9.487   1.00 53.92  ? 423 GLU   C OE1   1 
ATOM   6802  O  OE2   . GLU   B 1  423 ? 27.080  8.508   9.614   1.00 60.05  ? 423 GLU   C OE2   1 
ATOM   6803  N  N     . ASP   B 1  424 ? 26.639  13.446  6.234   1.00 27.07  ? 424 ASP   C N     1 
ATOM   6804  C  CA    . ASP   B 1  424 ? 26.147  14.780  6.534   1.00 17.48  ? 424 ASP   C CA    1 
ATOM   6805  C  C     . ASP   B 1  424 ? 24.647  14.752  6.757   1.00 24.08  ? 424 ASP   C C     1 
ATOM   6806  O  O     . ASP   B 1  424 ? 24.152  15.262  7.770   1.00 25.05  ? 424 ASP   C O     1 
ATOM   6807  C  CB    . ASP   B 1  424 ? 26.489  15.736  5.399   1.00 23.48  ? 424 ASP   C CB    1 
ATOM   6808  C  CG    . ASP   B 1  424 ? 26.707  17.168  5.879   1.00 27.54  ? 424 ASP   C CG    1 
ATOM   6809  O  OD1   . ASP   B 1  424 ? 26.673  17.392  7.121   1.00 22.58  ? 424 ASP   C OD1   1 
ATOM   6810  O  OD2   . ASP   B 1  424 ? 26.933  18.052  5.002   1.00 20.27  ? 424 ASP   C OD2   1 
ATOM   6811  N  N     . MET   B 1  425 ? 23.903  14.166  5.807   1.00 20.25  ? 425 MET   C N     1 
ATOM   6812  C  CA    . MET   B 1  425 ? 22.449  14.093  5.934   1.00 20.19  ? 425 MET   C CA    1 
ATOM   6813  C  C     . MET   B 1  425 ? 22.046  13.462  7.257   1.00 21.04  ? 425 MET   C C     1 
ATOM   6814  O  O     . MET   B 1  425 ? 21.038  13.840  7.862   1.00 19.41  ? 425 MET   C O     1 
ATOM   6815  C  CB    . MET   B 1  425 ? 21.843  13.299  4.774   1.00 19.77  ? 425 MET   C CB    1 
ATOM   6816  C  CG    . MET   B 1  425 ? 21.940  13.995  3.437   1.00 20.14  ? 425 MET   C CG    1 
ATOM   6817  S  SD    . MET   B 1  425 ? 21.538  15.740  3.513   1.00 28.17  ? 425 MET   C SD    1 
ATOM   6818  C  CE    . MET   B 1  425 ? 19.774  15.694  3.937   1.00 17.71  ? 425 MET   C CE    1 
ATOM   6819  N  N     . ALA   B 1  426 ? 22.816  12.485  7.716   1.00 22.06  ? 426 ALA   C N     1 
ATOM   6820  C  CA    . ALA   B 1  426 ? 22.512  11.873  8.998   1.00 19.63  ? 426 ALA   C CA    1 
ATOM   6821  C  C     . ALA   B 1  426 ? 22.674  12.876  10.141  1.00 21.38  ? 426 ALA   C C     1 
ATOM   6822  O  O     . ALA   B 1  426 ? 21.862  12.913  11.073  1.00 22.31  ? 426 ALA   C O     1 
ATOM   6823  C  CB    . ALA   B 1  426 ? 23.404  10.650  9.185   1.00 23.35  ? 426 ALA   C CB    1 
ATOM   6824  N  N     . ALA   B 1  427 ? 23.714  13.706  10.082  1.00 24.53  ? 427 ALA   C N     1 
ATOM   6825  C  CA    . ALA   B 1  427 ? 23.873  14.770  11.064  1.00 20.08  ? 427 ALA   C CA    1 
ATOM   6826  C  C     . ALA   B 1  427 ? 22.693  15.721  11.012  1.00 18.81  ? 427 ALA   C C     1 
ATOM   6827  O  O     . ALA   B 1  427 ? 22.032  15.967  12.021  1.00 25.80  ? 427 ALA   C O     1 
ATOM   6828  C  CB    . ALA   B 1  427 ? 25.176  15.519  10.813  1.00 18.42  ? 427 ALA   C CB    1 
ATOM   6829  N  N     . LEU   B 1  428 ? 22.400  16.244  9.830   1.00 17.29  ? 428 LEU   C N     1 
ATOM   6830  C  CA    . LEU   B 1  428 ? 21.277  17.155  9.670   1.00 16.84  ? 428 LEU   C CA    1 
ATOM   6831  C  C     . LEU   B 1  428 ? 19.999  16.581  10.275  1.00 21.98  ? 428 LEU   C C     1 
ATOM   6832  O  O     . LEU   B 1  428 ? 19.178  17.312  10.854  1.00 25.15  ? 428 LEU   C O     1 
ATOM   6833  C  CB    . LEU   B 1  428 ? 21.097  17.454  8.187   1.00 13.71  ? 428 LEU   C CB    1 
ATOM   6834  C  CG    . LEU   B 1  428 ? 20.186  18.596  7.828   1.00 12.38  ? 428 LEU   C CG    1 
ATOM   6835  C  CD1   . LEU   B 1  428 ? 20.698  19.816  8.468   1.00 13.92  ? 428 LEU   C CD1   1 
ATOM   6836  C  CD2   . LEU   B 1  428 ? 20.149  18.725  6.332   1.00 18.79  ? 428 LEU   C CD2   1 
ATOM   6837  N  N     . GLU   B 1  429 ? 19.803  15.272  10.148  1.00 19.38  ? 429 GLU   C N     1 
ATOM   6838  C  CA    . GLU   B 1  429 ? 18.620  14.672  10.744  1.00 17.17  ? 429 GLU   C CA    1 
ATOM   6839  C  C     . GLU   B 1  429 ? 18.758  14.622  12.247  1.00 18.70  ? 429 GLU   C C     1 
ATOM   6840  O  O     . GLU   B 1  429 ? 17.804  14.923  12.966  1.00 22.49  ? 429 GLU   C O     1 
ATOM   6841  C  CB    . GLU   B 1  429 ? 18.365  13.271  10.166  1.00 19.40  ? 429 GLU   C CB    1 
ATOM   6842  C  CG    . GLU   B 1  429 ? 17.615  13.300  8.817   1.00 24.87  ? 429 GLU   C CG    1 
ATOM   6843  C  CD    . GLU   B 1  429 ? 17.126  11.942  8.376   1.00 30.77  ? 429 GLU   C CD    1 
ATOM   6844  O  OE1   . GLU   B 1  429 ? 16.691  11.159  9.243   1.00 35.12  ? 429 GLU   C OE1   1 
ATOM   6845  O  OE2   . GLU   B 1  429 ? 17.185  11.654  7.158   1.00 33.73  ? 429 GLU   C OE2   1 
ATOM   6846  N  N     . LYS   B 1  430 ? 19.947  14.264  12.743  1.00 21.30  ? 430 LYS   C N     1 
ATOM   6847  C  CA    . LYS   B 1  430 ? 20.160  14.237  14.188  1.00 26.16  ? 430 LYS   C CA    1 
ATOM   6848  C  C     . LYS   B 1  430 ? 20.075  15.638  14.771  1.00 24.52  ? 430 LYS   C C     1 
ATOM   6849  O  O     . LYS   B 1  430 ? 19.552  15.828  15.875  1.00 26.74  ? 430 LYS   C O     1 
ATOM   6850  C  CB    . LYS   B 1  430 ? 21.510  13.597  14.531  1.00 25.78  ? 430 LYS   C CB    1 
ATOM   6851  C  CG    . LYS   B 1  430 ? 21.451  12.610  15.693  1.00 28.54  ? 430 LYS   C CG    1 
ATOM   6852  C  CD    . LYS   B 1  430 ? 22.685  12.704  16.557  1.00 35.43  ? 430 LYS   C CD    1 
ATOM   6853  C  CE    . LYS   B 1  430 ? 22.333  12.635  18.051  1.00 52.17  ? 430 LYS   C CE    1 
ATOM   6854  N  NZ    . LYS   B 1  430 ? 21.892  11.273  18.500  1.00 50.33  ? 430 LYS   C NZ    1 
ATOM   6855  N  N     . ASP   B 1  431 ? 20.587  16.626  14.039  1.00 17.88  ? 431 ASP   C N     1 
ATOM   6856  C  CA    . ASP   B 1  431 ? 20.467  18.013  14.452  1.00 18.74  ? 431 ASP   C CA    1 
ATOM   6857  C  C     . ASP   B 1  431 ? 19.004  18.427  14.607  1.00 25.82  ? 431 ASP   C C     1 
ATOM   6858  O  O     . ASP   B 1  431 ? 18.621  19.049  15.610  1.00 25.30  ? 431 ASP   C O     1 
ATOM   6859  C  CB    . ASP   B 1  431 ? 21.159  18.898  13.436  1.00 16.24  ? 431 ASP   C CB    1 
ATOM   6860  C  CG    . ASP   B 1  431 ? 22.650  18.721  13.423  1.00 22.81  ? 431 ASP   C CG    1 
ATOM   6861  O  OD1   . ASP   B 1  431 ? 23.247  18.275  14.434  1.00 34.34  ? 431 ASP   C OD1   1 
ATOM   6862  O  OD2   . ASP   B 1  431 ? 23.232  19.074  12.382  1.00 23.01  ? 431 ASP   C OD2   1 
ATOM   6863  N  N     . TYR   B 1  432 ? 18.168  18.117  13.610  1.00 18.98  ? 432 TYR   C N     1 
ATOM   6864  C  CA    . TYR   B 1  432 ? 16.763  18.496  13.717  1.00 18.41  ? 432 TYR   C CA    1 
ATOM   6865  C  C     . TYR   B 1  432 ? 16.084  17.771  14.877  1.00 22.27  ? 432 TYR   C C     1 
ATOM   6866  O  O     . TYR   B 1  432 ? 15.156  18.305  15.489  1.00 25.49  ? 432 TYR   C O     1 
ATOM   6867  C  CB    . TYR   B 1  432 ? 16.048  18.253  12.379  1.00 19.28  ? 432 TYR   C CB    1 
ATOM   6868  C  CG    . TYR   B 1  432 ? 16.083  19.463  11.463  1.00 25.67  ? 432 TYR   C CG    1 
ATOM   6869  C  CD1   . TYR   B 1  432 ? 15.228  20.523  11.676  1.00 23.09  ? 432 TYR   C CD1   1 
ATOM   6870  C  CD2   . TYR   B 1  432 ? 16.980  19.561  10.405  1.00 25.97  ? 432 TYR   C CD2   1 
ATOM   6871  C  CE1   . TYR   B 1  432 ? 15.253  21.632  10.881  1.00 19.14  ? 432 TYR   C CE1   1 
ATOM   6872  C  CE2   . TYR   B 1  432 ? 17.004  20.700  9.590   1.00 22.60  ? 432 TYR   C CE2   1 
ATOM   6873  C  CZ    . TYR   B 1  432 ? 16.132  21.734  9.847   1.00 19.29  ? 432 TYR   C CZ    1 
ATOM   6874  O  OH    . TYR   B 1  432 ? 16.098  22.894  9.090   1.00 26.36  ? 432 TYR   C OH    1 
ATOM   6875  N  N     . GLU   B 1  433 ? 16.565  16.578  15.222  1.00 25.61  ? 433 GLU   C N     1 
ATOM   6876  C  CA    . GLU   B 1  433 ? 16.139  15.889  16.444  1.00 27.24  ? 433 GLU   C CA    1 
ATOM   6877  C  C     . GLU   B 1  433 ? 16.543  16.671  17.686  1.00 29.61  ? 433 GLU   C C     1 
ATOM   6878  O  O     . GLU   B 1  433 ? 15.715  16.954  18.561  1.00 32.52  ? 433 GLU   C O     1 
ATOM   6879  C  CB    . GLU   B 1  433 ? 16.782  14.498  16.491  1.00 27.39  ? 433 GLU   C CB    1 
ATOM   6880  C  CG    . GLU   B 1  433 ? 15.877  13.313  16.788  1.00 37.85  ? 433 GLU   C CG    1 
ATOM   6881  C  CD    . GLU   B 1  433 ? 16.560  11.973  16.449  1.00 55.25  ? 433 GLU   C CD    1 
ATOM   6882  O  OE1   . GLU   B 1  433 ? 17.610  11.643  17.067  1.00 53.06  ? 433 GLU   C OE1   1 
ATOM   6883  O  OE2   . GLU   B 1  433 ? 16.051  11.264  15.543  1.00 55.18  ? 433 GLU   C OE2   1 
ATOM   6884  N  N     . GLU   B 1  434 ? 17.838  16.991  17.785  1.00 26.83  ? 434 GLU   C N     1 
ATOM   6885  C  CA    . GLU   B 1  434 ? 18.387  17.643  18.963  1.00 24.70  ? 434 GLU   C CA    1 
ATOM   6886  C  C     . GLU   B 1  434 ? 17.651  18.941  19.270  1.00 28.00  ? 434 GLU   C C     1 
ATOM   6887  O  O     . GLU   B 1  434 ? 17.163  19.132  20.386  1.00 30.49  ? 434 GLU   C O     1 
ATOM   6888  C  CB    . GLU   B 1  434 ? 19.885  17.892  18.761  1.00 26.59  ? 434 GLU   C CB    1 
ATOM   6889  C  CG    . GLU   B 1  434 ? 20.785  16.709  19.126  1.00 23.12  ? 434 GLU   C CG    1 
ATOM   6890  C  CD    . GLU   B 1  434 ? 22.188  16.842  18.561  1.00 45.11  ? 434 GLU   C CD    1 
ATOM   6891  O  OE1   . GLU   B 1  434 ? 22.608  17.986  18.272  1.00 52.21  ? 434 GLU   C OE1   1 
ATOM   6892  O  OE2   . GLU   B 1  434 ? 22.871  15.803  18.378  1.00 57.05  ? 434 GLU   C OE2   1 
ATOM   6893  N  N     . VAL   B 1  435 ? 17.549  19.847  18.294  1.00 26.66  ? 435 VAL   C N     1 
ATOM   6894  C  CA    . VAL   B 1  435 ? 16.963  21.149  18.589  1.00 23.77  ? 435 VAL   C CA    1 
ATOM   6895  C  C     . VAL   B 1  435 ? 15.555  20.996  19.143  1.00 24.86  ? 435 VAL   C C     1 
ATOM   6896  O  O     . VAL   B 1  435 ? 15.010  21.931  19.740  1.00 31.32  ? 435 VAL   C O     1 
ATOM   6897  C  CB    . VAL   B 1  435 ? 16.970  22.079  17.340  1.00 23.98  ? 435 VAL   C CB    1 
ATOM   6898  C  CG1   . VAL   B 1  435 ? 18.307  22.050  16.649  1.00 14.80  ? 435 VAL   C CG1   1 
ATOM   6899  C  CG2   . VAL   B 1  435 ? 15.860  21.720  16.374  1.00 24.41  ? 435 VAL   C CG2   1 
ATOM   6900  N  N     . GLY   B 1  436 ? 14.952  19.834  18.985  1.00 24.92  ? 436 GLY   C N     1 
ATOM   6901  C  CA    . GLY   B 1  436 ? 13.564  19.697  19.380  1.00 28.28  ? 436 GLY   C CA    1 
ATOM   6902  C  C     . GLY   B 1  436 ? 13.419  19.254  20.812  1.00 27.00  ? 436 GLY   C C     1 
ATOM   6903  O  O     . GLY   B 1  436 ? 12.384  19.485  21.447  1.00 30.28  ? 436 GLY   C O     1 
ATOM   6904  N  N     . VAL   B 1  437 ? 14.462  18.598  21.322  1.00 22.76  ? 437 VAL   C N     1 
ATOM   6905  C  CA    . VAL   B 1  437 ? 14.441  18.104  22.690  1.00 24.40  ? 437 VAL   C CA    1 
ATOM   6906  C  C     . VAL   B 1  437 ? 14.365  19.255  23.680  1.00 24.79  ? 437 VAL   C C     1 
ATOM   6907  O  O     . VAL   B 1  437 ? 15.054  20.276  23.532  1.00 24.57  ? 437 VAL   C O     1 
ATOM   6908  C  CB    . VAL   B 1  437 ? 15.697  17.267  22.965  1.00 26.94  ? 437 VAL   C CB    1 
ATOM   6909  C  CG1   . VAL   B 1  437 ? 15.912  17.152  24.471  1.00 25.77  ? 437 VAL   C CG1   1 
ATOM   6910  C  CG2   . VAL   B 1  437 ? 15.604  15.916  22.294  1.00 21.67  ? 437 VAL   C CG2   1 
ATOM   6911  N  N     . ASP   B 1  438 ? 13.537  19.090  24.711  1.00 23.90  ? 438 ASP   C N     1 
ATOM   6912  C  CA    . ASP   B 1  438 ? 13.494  20.087  25.765  1.00 26.01  ? 438 ASP   C CA    1 
ATOM   6913  C  C     . ASP   B 1  438 ? 14.828  20.100  26.503  1.00 34.21  ? 438 ASP   C C     1 
ATOM   6914  O  O     . ASP   B 1  438 ? 15.616  19.159  26.419  1.00 35.56  ? 438 ASP   C O     1 
ATOM   6915  C  CB    . ASP   B 1  438 ? 12.335  19.812  26.712  1.00 28.59  ? 438 ASP   C CB    1 
ATOM   6916  C  CG    . ASP   B 1  438 ? 10.976  20.147  26.090  1.00 48.95  ? 438 ASP   C CG    1 
ATOM   6917  O  OD1   . ASP   B 1  438 ? 10.924  20.998  25.158  1.00 45.63  ? 438 ASP   C OD1   1 
ATOM   6918  O  OD2   . ASP   B 1  438 ? 9.958   19.561  26.538  1.00 56.91  ? 438 ASP   C OD2   1 
ATOM   6919  N  N     . SER   B 1  439 ? 15.110  21.200  27.189  1.00 33.87  ? 439 SER   C N     1 
ATOM   6920  C  CA    . SER   B 1  439 ? 16.401  21.335  27.847  1.00 36.25  ? 439 SER   C CA    1 
ATOM   6921  C  C     . SER   B 1  439 ? 16.239  21.149  29.348  1.00 45.66  ? 439 SER   C C     1 
ATOM   6922  O  O     . SER   B 1  439 ? 15.170  20.756  29.827  1.00 44.68  ? 439 SER   C O     1 
ATOM   6923  C  CB    . SER   B 1  439 ? 17.034  22.687  27.517  1.00 41.45  ? 439 SER   C CB    1 
ATOM   6924  O  OG    . SER   B 1  439 ? 16.064  23.623  27.085  1.00 32.88  ? 439 SER   C OG    1 
ATOM   6925  N  N     . VAL   B 1  440 ? 17.316  21.417  30.098  1.00 59.44  ? 440 VAL   C N     1 
ATOM   6926  C  CA    . VAL   B 1  440 ? 17.302  21.409  31.575  1.00 71.79  ? 440 VAL   C CA    1 
ATOM   6927  C  C     . VAL   B 1  440 ? 18.205  22.524  32.108  1.00 72.90  ? 440 VAL   C C     1 
ATOM   6928  O  O     . VAL   B 1  440 ? 18.502  22.591  33.306  1.00 85.69  ? 440 VAL   C O     1 
ATOM   6929  C  CB    . VAL   B 1  440 ? 17.733  20.031  32.148  1.00 68.11  ? 440 VAL   C CB    1 
ATOM   6930  C  CG1   . VAL   B 1  440 ? 19.120  19.687  31.650  1.00 63.87  ? 440 VAL   C CG1   1 
ATOM   6931  C  CG2   . VAL   B 1  440 ? 17.669  20.004  33.697  1.00 52.42  ? 440 VAL   C CG2   1 
ATOM   6932  N  N     . MET   C 2  1   ? 21.344  20.610  -31.606 1.00 59.64  ? 1   MET   D N     1 
ATOM   6933  C  CA    . MET   C 2  1   ? 20.974  19.266  -32.022 1.00 54.27  ? 1   MET   D CA    1 
ATOM   6934  C  C     . MET   C 2  1   ? 21.820  18.201  -31.277 1.00 63.40  ? 1   MET   D C     1 
ATOM   6935  O  O     . MET   C 2  1   ? 22.926  18.473  -30.812 1.00 58.71  ? 1   MET   D O     1 
ATOM   6936  C  CB    . MET   C 2  1   ? 21.123  19.143  -33.542 1.00 53.25  ? 1   MET   D CB    1 
ATOM   6937  C  CG    . MET   C 2  1   ? 21.056  20.503  -34.267 1.00 74.31  ? 1   MET   D CG    1 
ATOM   6938  S  SD    . MET   C 2  1   ? 20.780  20.378  -36.059 1.00 110.33 ? 1   MET   D SD    1 
ATOM   6939  C  CE    . MET   C 2  1   ? 20.922  22.076  -36.627 1.00 82.97  ? 1   MET   D CE    1 
ATOM   6940  N  N     . ARG   C 2  2   ? 21.289  16.991  -31.137 1.00 55.31  ? 2   ARG   D N     1 
ATOM   6941  C  CA    . ARG   C 2  2   ? 22.008  15.874  -30.533 1.00 42.26  ? 2   ARG   D CA    1 
ATOM   6942  C  C     . ARG   C 2  2   ? 21.955  14.746  -31.562 1.00 48.06  ? 2   ARG   D C     1 
ATOM   6943  O  O     . ARG   C 2  2   ? 21.095  13.868  -31.512 1.00 44.16  ? 2   ARG   D O     1 
ATOM   6944  C  CB    . ARG   C 2  2   ? 21.399  15.471  -29.183 1.00 39.54  ? 2   ARG   D CB    1 
ATOM   6945  C  CG    . ARG   C 2  2   ? 21.391  16.562  -28.121 1.00 38.36  ? 2   ARG   D CG    1 
ATOM   6946  C  CD    . ARG   C 2  2   ? 22.773  16.808  -27.526 1.00 42.05  ? 2   ARG   D CD    1 
ATOM   6947  N  NE    . ARG   C 2  2   ? 23.473  15.560  -27.244 1.00 46.14  ? 2   ARG   D NE    1 
ATOM   6948  C  CZ    . ARG   C 2  2   ? 23.384  14.887  -26.104 1.00 45.73  ? 2   ARG   D CZ    1 
ATOM   6949  N  NH1   . ARG   C 2  2   ? 22.651  15.332  -25.096 1.00 48.34  ? 2   ARG   D NH1   1 
ATOM   6950  N  NH2   . ARG   C 2  2   ? 24.047  13.740  -25.969 1.00 36.39  ? 2   ARG   D NH2   1 
ATOM   6951  N  N     . GLU   C 2  3   ? 22.878  14.789  -32.519 1.00 51.16  ? 3   GLU   D N     1 
ATOM   6952  C  CA    . GLU   C 2  3   ? 22.843  13.859  -33.638 1.00 41.96  ? 3   GLU   D CA    1 
ATOM   6953  C  C     . GLU   C 2  3   ? 23.220  12.452  -33.206 1.00 44.05  ? 3   GLU   D C     1 
ATOM   6954  O  O     . GLU   C 2  3   ? 24.257  12.234  -32.568 1.00 37.29  ? 3   GLU   D O     1 
ATOM   6955  C  CB    . GLU   C 2  3   ? 23.786  14.320  -34.740 1.00 39.07  ? 3   GLU   D CB    1 
ATOM   6956  C  CG    . GLU   C 2  3   ? 23.462  15.672  -35.269 1.00 44.03  ? 3   GLU   D CG    1 
ATOM   6957  C  CD    . GLU   C 2  3   ? 24.240  16.761  -34.576 1.00 49.94  ? 3   GLU   D CD    1 
ATOM   6958  O  OE1   . GLU   C 2  3   ? 24.931  16.467  -33.576 1.00 41.34  ? 3   GLU   D OE1   1 
ATOM   6959  O  OE2   . GLU   C 2  3   ? 24.170  17.919  -35.045 1.00 57.92  ? 3   GLU   D OE2   1 
ATOM   6960  N  N     . ILE   C 2  4   ? 22.377  11.501  -33.576 1.00 48.02  ? 4   ILE   D N     1 
ATOM   6961  C  CA    . ILE   C 2  4   ? 22.688  10.081  -33.497 1.00 42.78  ? 4   ILE   D CA    1 
ATOM   6962  C  C     . ILE   C 2  4   ? 23.150  9.620   -34.875 1.00 35.82  ? 4   ILE   D C     1 
ATOM   6963  O  O     . ILE   C 2  4   ? 22.699  10.125  -35.914 1.00 30.58  ? 4   ILE   D O     1 
ATOM   6964  C  CB    . ILE   C 2  4   ? 21.476  9.257   -33.009 1.00 33.55  ? 4   ILE   D CB    1 
ATOM   6965  C  CG1   . ILE   C 2  4   ? 20.942  9.801   -31.689 1.00 36.87  ? 4   ILE   D CG1   1 
ATOM   6966  C  CG2   . ILE   C 2  4   ? 21.856  7.824   -32.840 1.00 33.80  ? 4   ILE   D CG2   1 
ATOM   6967  C  CD1   . ILE   C 2  4   ? 19.758  9.020   -31.149 1.00 36.96  ? 4   ILE   D CD1   1 
ATOM   6968  N  N     . VAL   C 2  5   ? 24.068  8.657   -34.884 1.00 31.31  ? 5   VAL   D N     1 
ATOM   6969  C  CA    . VAL   C 2  5   ? 24.618  8.085   -36.105 1.00 36.35  ? 5   VAL   D CA    1 
ATOM   6970  C  C     . VAL   C 2  5   ? 24.238  6.609   -36.151 1.00 40.75  ? 5   VAL   D C     1 
ATOM   6971  O  O     . VAL   C 2  5   ? 24.402  5.888   -35.155 1.00 28.83  ? 5   VAL   D O     1 
ATOM   6972  C  CB    . VAL   C 2  5   ? 26.145  8.300   -36.191 1.00 38.88  ? 5   VAL   D CB    1 
ATOM   6973  C  CG1   . VAL   C 2  5   ? 26.855  7.124   -36.861 1.00 37.23  ? 5   VAL   D CG1   1 
ATOM   6974  C  CG2   . VAL   C 2  5   ? 26.430  9.575   -36.961 1.00 38.50  ? 5   VAL   D CG2   1 
ATOM   6975  N  N     . HIS   C 2  6   ? 23.716  6.174   -37.308 1.00 38.85  ? 6   HIS   D N     1 
ATOM   6976  C  CA    . HIS   C 2  6   ? 23.161  4.839   -37.511 1.00 38.90  ? 6   HIS   D CA    1 
ATOM   6977  C  C     . HIS   C 2  6   ? 24.070  4.012   -38.406 1.00 44.76  ? 6   HIS   D C     1 
ATOM   6978  O  O     . HIS   C 2  6   ? 24.493  4.482   -39.471 1.00 46.28  ? 6   HIS   D O     1 
ATOM   6979  C  CB    . HIS   C 2  6   ? 21.773  4.920   -38.143 1.00 39.40  ? 6   HIS   D CB    1 
ATOM   6980  C  CG    . HIS   C 2  6   ? 21.194  3.586   -38.500 1.00 46.23  ? 6   HIS   D CG    1 
ATOM   6981  N  ND1   . HIS   C 2  6   ? 20.187  2.989   -37.770 1.00 45.70  ? 6   HIS   D ND1   1 
ATOM   6982  C  CD2   . HIS   C 2  6   ? 21.495  2.723   -39.500 1.00 51.40  ? 6   HIS   D CD2   1 
ATOM   6983  C  CE1   . HIS   C 2  6   ? 19.891  1.819   -38.309 1.00 51.54  ? 6   HIS   D CE1   1 
ATOM   6984  N  NE2   . HIS   C 2  6   ? 20.668  1.635   -39.361 1.00 50.67  ? 6   HIS   D NE2   1 
ATOM   6985  N  N     . ILE   C 2  7   ? 24.326  2.769   -37.990 1.00 38.35  ? 7   ILE   D N     1 
ATOM   6986  C  CA    . ILE   C 2  7   ? 25.226  1.855   -38.695 1.00 43.32  ? 7   ILE   D CA    1 
ATOM   6987  C  C     . ILE   C 2  7   ? 24.548  0.490   -38.739 1.00 48.41  ? 7   ILE   D C     1 
ATOM   6988  O  O     . ILE   C 2  7   ? 24.681  -0.323  -37.817 1.00 50.15  ? 7   ILE   D O     1 
ATOM   6989  C  CB    . ILE   C 2  7   ? 26.606  1.756   -38.036 1.00 34.52  ? 7   ILE   D CB    1 
ATOM   6990  C  CG1   . ILE   C 2  7   ? 27.391  3.052   -38.162 1.00 35.96  ? 7   ILE   D CG1   1 
ATOM   6991  C  CG2   . ILE   C 2  7   ? 27.424  0.648   -38.667 1.00 35.86  ? 7   ILE   D CG2   1 
ATOM   6992  C  CD1   . ILE   C 2  7   ? 28.735  2.957   -37.469 1.00 39.55  ? 7   ILE   D CD1   1 
ATOM   6993  N  N     . GLN   C 2  8   ? 23.814  0.227   -39.815 1.00 48.19  ? 8   GLN   D N     1 
ATOM   6994  C  CA    . GLN   C 2  8   ? 23.206  -1.075  -40.062 1.00 50.43  ? 8   GLN   D CA    1 
ATOM   6995  C  C     . GLN   C 2  8   ? 24.176  -1.946  -40.846 1.00 48.70  ? 8   GLN   D C     1 
ATOM   6996  O  O     . GLN   C 2  8   ? 24.673  -1.533  -41.898 1.00 54.48  ? 8   GLN   D O     1 
ATOM   6997  C  CB    . GLN   C 2  8   ? 21.907  -0.914  -40.847 1.00 51.25  ? 8   GLN   D CB    1 
ATOM   6998  C  CG    . GLN   C 2  8   ? 22.113  -0.241  -42.184 1.00 44.52  ? 8   GLN   D CG    1 
ATOM   6999  C  CD    . GLN   C 2  8   ? 20.813  0.227   -42.780 1.00 54.82  ? 8   GLN   D CD    1 
ATOM   7000  O  OE1   . GLN   C 2  8   ? 20.478  -0.111  -43.926 1.00 56.72  ? 8   GLN   D OE1   1 
ATOM   7001  N  NE2   . GLN   C 2  8   ? 20.058  1.012   -42.002 1.00 44.29  ? 8   GLN   D NE2   1 
ATOM   7002  N  N     . ALA   C 2  9   ? 24.444  -3.146  -40.347 1.00 41.70  ? 9   ALA   D N     1 
ATOM   7003  C  CA    . ALA   C 2  9   ? 25.504  -3.948  -40.927 1.00 44.01  ? 9   ALA   D CA    1 
ATOM   7004  C  C     . ALA   C 2  9   ? 25.052  -5.387  -41.096 1.00 53.78  ? 9   ALA   D C     1 
ATOM   7005  O  O     . ALA   C 2  9   ? 24.388  -5.951  -40.219 1.00 45.95  ? 9   ALA   D O     1 
ATOM   7006  C  CB    . ALA   C 2  9   ? 26.770  -3.905  -40.071 1.00 43.12  ? 9   ALA   D CB    1 
ATOM   7007  N  N     . GLY   C 2  10  ? 25.430  -5.970  -42.237 1.00 52.00  ? 10  GLY   D N     1 
ATOM   7008  C  CA    . GLY   C 2  10  ? 25.196  -7.368  -42.513 1.00 46.40  ? 10  GLY   D CA    1 
ATOM   7009  C  C     . GLY   C 2  10  ? 23.846  -7.615  -43.148 1.00 51.75  ? 10  GLY   D C     1 
ATOM   7010  O  O     . GLY   C 2  10  ? 23.067  -6.700  -43.465 1.00 44.77  ? 10  GLY   D O     1 
ATOM   7011  N  N     . GLN   C 2  11  ? 23.573  -8.907  -43.341 1.00 53.86  ? 11  GLN   D N     1 
ATOM   7012  C  CA    . GLN   C 2  11  ? 22.316  -9.335  -43.937 1.00 55.25  ? 11  GLN   D CA    1 
ATOM   7013  C  C     . GLN   C 2  11  ? 21.162  -8.901  -43.044 1.00 55.93  ? 11  GLN   D C     1 
ATOM   7014  O  O     . GLN   C 2  11  ? 20.431  -7.958  -43.378 1.00 47.32  ? 11  GLN   D O     1 
ATOM   7015  C  CB    . GLN   C 2  11  ? 22.313  -10.851 -44.147 1.00 61.73  ? 11  GLN   D CB    1 
ATOM   7016  C  CG    . GLN   C 2  11  ? 21.202  -11.360 -45.047 1.00 61.46  ? 11  GLN   D CG    1 
ATOM   7017  C  CD    . GLN   C 2  11  ? 20.987  -12.870 -44.929 1.00 65.67  ? 11  GLN   D CD    1 
ATOM   7018  O  OE1   . GLN   C 2  11  ? 21.927  -13.646 -44.695 1.00 68.92  ? 11  GLN   D OE1   1 
ATOM   7019  N  NE2   . GLN   C 2  11  ? 19.738  -13.289 -45.081 1.00 61.01  ? 11  GLN   D NE2   1 
ATOM   7020  N  N     . CYS   C 2  12  ? 21.013  -9.565  -41.891 1.00 53.49  ? 12  CYS   D N     1 
ATOM   7021  C  CA    . CYS   C 2  12  ? 19.927  -9.213  -40.983 1.00 53.92  ? 12  CYS   D CA    1 
ATOM   7022  C  C     . CYS   C 2  12  ? 19.947  -7.736  -40.627 1.00 53.42  ? 12  CYS   D C     1 
ATOM   7023  O  O     . CYS   C 2  12  ? 18.911  -7.061  -40.676 1.00 50.27  ? 12  CYS   D O     1 
ATOM   7024  C  CB    . CYS   C 2  12  ? 19.993  -10.032 -39.699 1.00 58.57  ? 12  CYS   D CB    1 
ATOM   7025  S  SG    . CYS   C 2  12  ? 18.966  -9.253  -38.434 1.00 46.03  ? 12  CYS   D SG    1 
ATOM   7026  N  N     . GLY   C 2  13  ? 21.111  -7.230  -40.212 1.00 54.49  ? 13  GLY   D N     1 
ATOM   7027  C  CA    . GLY   C 2  13  ? 21.192  -5.840  -39.792 1.00 49.02  ? 13  GLY   D CA    1 
ATOM   7028  C  C     . GLY   C 2  13  ? 20.671  -4.880  -40.844 1.00 47.56  ? 13  GLY   D C     1 
ATOM   7029  O  O     . GLY   C 2  13  ? 19.873  -3.984  -40.551 1.00 39.52  ? 13  GLY   D O     1 
ATOM   7030  N  N     . ASN   C 2  14  ? 21.109  -5.064  -42.094 1.00 54.14  ? 14  ASN   D N     1 
ATOM   7031  C  CA    . ASN   C 2  14  ? 20.770  -4.110  -43.142 1.00 50.77  ? 14  ASN   D CA    1 
ATOM   7032  C  C     . ASN   C 2  14  ? 19.289  -4.152  -43.483 1.00 50.52  ? 14  ASN   D C     1 
ATOM   7033  O  O     . ASN   C 2  14  ? 18.727  -3.145  -43.940 1.00 46.68  ? 14  ASN   D O     1 
ATOM   7034  C  CB    . ASN   C 2  14  ? 21.623  -4.388  -44.371 1.00 46.21  ? 14  ASN   D CB    1 
ATOM   7035  C  CG    . ASN   C 2  14  ? 22.619  -3.300  -44.625 1.00 46.95  ? 14  ASN   D CG    1 
ATOM   7036  O  OD1   . ASN   C 2  14  ? 22.270  -2.111  -44.629 1.00 44.58  ? 14  ASN   D OD1   1 
ATOM   7037  N  ND2   . ASN   C 2  14  ? 23.875  -3.685  -44.817 1.00 44.22  ? 14  ASN   D ND2   1 
ATOM   7038  N  N     . GLN   C 2  15  ? 18.645  -5.302  -43.255 1.00 54.56  ? 15  GLN   D N     1 
ATOM   7039  C  CA    . GLN   C 2  15  ? 17.229  -5.457  -43.570 1.00 55.21  ? 15  GLN   D CA    1 
ATOM   7040  C  C     . GLN   C 2  15  ? 16.347  -4.737  -42.550 1.00 59.02  ? 15  GLN   D C     1 
ATOM   7041  O  O     . GLN   C 2  15  ? 15.456  -3.961  -42.923 1.00 55.86  ? 15  GLN   D O     1 
ATOM   7042  C  CB    . GLN   C 2  15  ? 16.884  -6.946  -43.647 1.00 52.25  ? 15  GLN   D CB    1 
ATOM   7043  C  CG    . GLN   C 2  15  ? 16.568  -7.421  -45.056 1.00 52.82  ? 15  GLN   D CG    1 
ATOM   7044  C  CD    . GLN   C 2  15  ? 15.533  -6.528  -45.755 1.00 60.67  ? 15  GLN   D CD    1 
ATOM   7045  O  OE1   . GLN   C 2  15  ? 14.442  -6.274  -45.225 1.00 48.58  ? 15  GLN   D OE1   1 
ATOM   7046  N  NE2   . GLN   C 2  15  ? 15.883  -6.040  -46.946 1.00 64.86  ? 15  GLN   D NE2   1 
ATOM   7047  N  N     . ILE   C 2  16  ? 16.583  -4.975  -41.254 1.00 55.87  ? 16  ILE   D N     1 
ATOM   7048  C  CA    . ILE   C 2  16  ? 15.731  -4.362  -40.238 1.00 51.47  ? 16  ILE   D CA    1 
ATOM   7049  C  C     . ILE   C 2  16  ? 16.014  -2.873  -40.135 1.00 49.99  ? 16  ILE   D C     1 
ATOM   7050  O  O     . ILE   C 2  16  ? 15.121  -2.086  -39.805 1.00 52.18  ? 16  ILE   D O     1 
ATOM   7051  C  CB    . ILE   C 2  16  ? 15.881  -5.065  -38.872 1.00 51.74  ? 16  ILE   D CB    1 
ATOM   7052  C  CG1   . ILE   C 2  16  ? 16.938  -4.398  -38.002 1.00 49.84  ? 16  ILE   D CG1   1 
ATOM   7053  C  CG2   . ILE   C 2  16  ? 16.243  -6.545  -39.029 1.00 56.54  ? 16  ILE   D CG2   1 
ATOM   7054  C  CD1   . ILE   C 2  16  ? 17.271  -5.241  -36.784 1.00 52.12  ? 16  ILE   D CD1   1 
ATOM   7055  N  N     . GLY   C 2  17  ? 17.245  -2.454  -40.426 1.00 46.67  ? 17  GLY   D N     1 
ATOM   7056  C  CA    . GLY   C 2  17  ? 17.533  -1.036  -40.485 1.00 48.57  ? 17  GLY   D CA    1 
ATOM   7057  C  C     . GLY   C 2  17  ? 16.893  -0.328  -41.662 1.00 51.16  ? 17  GLY   D C     1 
ATOM   7058  O  O     . GLY   C 2  17  ? 16.695  0.893   -41.615 1.00 49.91  ? 17  GLY   D O     1 
ATOM   7059  N  N     . ALA   C 2  18  ? 16.564  -1.061  -42.721 1.00 49.62  ? 18  ALA   D N     1 
ATOM   7060  C  CA    . ALA   C 2  18  ? 15.949  -0.410  -43.869 1.00 57.54  ? 18  ALA   D CA    1 
ATOM   7061  C  C     . ALA   C 2  18  ? 14.485  -0.057  -43.591 1.00 54.75  ? 18  ALA   D C     1 
ATOM   7062  O  O     . ALA   C 2  18  ? 14.014  1.021   -43.987 1.00 41.33  ? 18  ALA   D O     1 
ATOM   7063  C  CB    . ALA   C 2  18  ? 16.093  -1.306  -45.102 1.00 55.10  ? 18  ALA   D CB    1 
ATOM   7064  N  N     . LYS   C 2  19  ? 13.759  -0.949  -42.900 1.00 51.87  ? 19  LYS   D N     1 
ATOM   7065  C  CA    . LYS   C 2  19  ? 12.381  -0.654  -42.507 1.00 54.93  ? 19  LYS   D CA    1 
ATOM   7066  C  C     . LYS   C 2  19  ? 12.341  0.460   -41.480 1.00 51.86  ? 19  LYS   D C     1 
ATOM   7067  O  O     . LYS   C 2  19  ? 11.479  1.344   -41.536 1.00 46.05  ? 19  LYS   D O     1 
ATOM   7068  C  CB    . LYS   C 2  19  ? 11.709  -1.910  -41.947 1.00 48.79  ? 19  LYS   D CB    1 
ATOM   7069  C  CG    . LYS   C 2  19  ? 11.974  -3.135  -42.814 1.00 60.68  ? 19  LYS   D CG    1 
ATOM   7070  C  CD    . LYS   C 2  19  ? 11.235  -4.415  -42.365 1.00 65.87  ? 19  LYS   D CD    1 
ATOM   7071  C  CE    . LYS   C 2  19  ? 11.848  -5.688  -43.020 1.00 67.86  ? 19  LYS   D CE    1 
ATOM   7072  N  NZ    . LYS   C 2  19  ? 10.891  -6.717  -43.467 1.00 72.59  ? 19  LYS   D NZ    1 
ATOM   7073  N  N     . PHE   C 2  20  ? 13.259  0.422   -40.524 1.00 46.90  ? 20  PHE   D N     1 
ATOM   7074  C  CA    . PHE   C 2  20  ? 13.341  1.499   -39.557 1.00 44.42  ? 20  PHE   D CA    1 
ATOM   7075  C  C     . PHE   C 2  20  ? 13.367  2.843   -40.261 1.00 47.37  ? 20  PHE   D C     1 
ATOM   7076  O  O     . PHE   C 2  20  ? 12.630  3.763   -39.890 1.00 52.15  ? 20  PHE   D O     1 
ATOM   7077  C  CB    . PHE   C 2  20  ? 14.573  1.312   -38.664 1.00 55.14  ? 20  PHE   D CB    1 
ATOM   7078  C  CG    . PHE   C 2  20  ? 14.913  2.516   -37.847 1.00 47.08  ? 20  PHE   D CG    1 
ATOM   7079  C  CD1   . PHE   C 2  20  ? 14.146  2.865   -36.748 1.00 46.71  ? 20  PHE   D CD1   1 
ATOM   7080  C  CD2   . PHE   C 2  20  ? 15.995  3.304   -38.186 1.00 42.20  ? 20  PHE   D CD2   1 
ATOM   7081  C  CE1   . PHE   C 2  20  ? 14.455  3.981   -35.996 1.00 40.49  ? 20  PHE   D CE1   1 
ATOM   7082  C  CE2   . PHE   C 2  20  ? 16.312  4.419   -37.448 1.00 44.58  ? 20  PHE   D CE2   1 
ATOM   7083  C  CZ    . PHE   C 2  20  ? 15.543  4.760   -36.347 1.00 46.10  ? 20  PHE   D CZ    1 
ATOM   7084  N  N     . TRP   C 2  21  ? 14.203  2.980   -41.297 1.00 48.01  ? 21  TRP   D N     1 
ATOM   7085  C  CA    . TRP   C 2  21  ? 14.286  4.280   -41.957 1.00 38.24  ? 21  TRP   D CA    1 
ATOM   7086  C  C     . TRP   C 2  21  ? 13.015  4.581   -42.718 1.00 39.11  ? 21  TRP   D C     1 
ATOM   7087  O  O     . TRP   C 2  21  ? 12.666  5.752   -42.906 1.00 44.19  ? 21  TRP   D O     1 
ATOM   7088  C  CB    . TRP   C 2  21  ? 15.500  4.342   -42.866 1.00 33.70  ? 21  TRP   D CB    1 
ATOM   7089  C  CG    . TRP   C 2  21  ? 16.733  4.522   -42.089 1.00 37.85  ? 21  TRP   D CG    1 
ATOM   7090  C  CD1   . TRP   C 2  21  ? 17.694  3.590   -41.851 1.00 42.61  ? 21  TRP   D CD1   1 
ATOM   7091  C  CD2   . TRP   C 2  21  ? 17.132  5.704   -41.384 1.00 34.66  ? 21  TRP   D CD2   1 
ATOM   7092  N  NE1   . TRP   C 2  21  ? 18.679  4.124   -41.055 1.00 42.76  ? 21  TRP   D NE1   1 
ATOM   7093  C  CE2   . TRP   C 2  21  ? 18.357  5.422   -40.759 1.00 34.18  ? 21  TRP   D CE2   1 
ATOM   7094  C  CE3   . TRP   C 2  21  ? 16.574  6.980   -41.236 1.00 43.77  ? 21  TRP   D CE3   1 
ATOM   7095  C  CZ2   . TRP   C 2  21  ? 19.034  6.358   -39.995 1.00 37.88  ? 21  TRP   D CZ2   1 
ATOM   7096  C  CZ3   . TRP   C 2  21  ? 17.253  7.919   -40.481 1.00 42.64  ? 21  TRP   D CZ3   1 
ATOM   7097  C  CH2   . TRP   C 2  21  ? 18.470  7.600   -39.866 1.00 38.72  ? 21  TRP   D CH2   1 
ATOM   7098  N  N     . GLU   C 2  22  ? 12.305  3.540   -43.144 1.00 48.25  ? 22  GLU   D N     1 
ATOM   7099  C  CA    . GLU   C 2  22  ? 10.981  3.709   -43.719 1.00 51.54  ? 22  GLU   D CA    1 
ATOM   7100  C  C     . GLU   C 2  22  ? 10.087  4.325   -42.658 1.00 49.49  ? 22  GLU   D C     1 
ATOM   7101  O  O     . GLU   C 2  22  ? 9.770   5.517   -42.722 1.00 46.28  ? 22  GLU   D O     1 
ATOM   7102  C  CB    . GLU   C 2  22  ? 10.418  2.367   -44.208 1.00 56.32  ? 22  GLU   D CB    1 
ATOM   7103  C  CG    . GLU   C 2  22  ? 11.286  1.642   -45.253 1.00 68.64  ? 22  GLU   D CG    1 
ATOM   7104  C  CD    . GLU   C 2  22  ? 10.755  0.249   -45.620 1.00 77.35  ? 22  GLU   D CD    1 
ATOM   7105  O  OE1   . GLU   C 2  22  ? 9.613   -0.077  -45.215 1.00 79.52  ? 22  GLU   D OE1   1 
ATOM   7106  O  OE2   . GLU   C 2  22  ? 11.480  -0.519  -46.307 1.00 62.59  ? 22  GLU   D OE2   1 
ATOM   7107  N  N     . VAL   C 2  23  ? 9.756   3.526   -41.636 1.00 55.02  ? 23  VAL   D N     1 
ATOM   7108  C  CA    . VAL   C 2  23  ? 8.739   3.902   -40.653 1.00 49.56  ? 23  VAL   D CA    1 
ATOM   7109  C  C     . VAL   C 2  23  ? 8.962   5.315   -40.137 1.00 50.80  ? 23  VAL   D C     1 
ATOM   7110  O  O     . VAL   C 2  23  ? 8.052   6.152   -40.175 1.00 55.21  ? 23  VAL   D O     1 
ATOM   7111  C  CB    . VAL   C 2  23  ? 8.709   2.897   -39.489 1.00 48.20  ? 23  VAL   D CB    1 
ATOM   7112  C  CG1   . VAL   C 2  23  ? 7.556   3.243   -38.569 1.00 57.35  ? 23  VAL   D CG1   1 
ATOM   7113  C  CG2   . VAL   C 2  23  ? 8.602   1.455   -40.001 1.00 51.13  ? 23  VAL   D CG2   1 
ATOM   7114  N  N     . ILE   C 2  24  ? 10.161  5.594   -39.605 1.00 49.46  ? 24  ILE   D N     1 
ATOM   7115  C  CA    . ILE   C 2  24  ? 10.380  6.888   -38.953 1.00 49.83  ? 24  ILE   D CA    1 
ATOM   7116  C  C     . ILE   C 2  24  ? 10.386  8.001   -39.983 1.00 43.63  ? 24  ILE   D C     1 
ATOM   7117  O  O     . ILE   C 2  24  ? 9.896   9.103   -39.724 1.00 42.86  ? 24  ILE   D O     1 
ATOM   7118  C  CB    . ILE   C 2  24  ? 11.674  6.899   -38.112 1.00 52.78  ? 24  ILE   D CB    1 
ATOM   7119  C  CG1   . ILE   C 2  24  ? 12.895  7.257   -38.969 1.00 50.23  ? 24  ILE   D CG1   1 
ATOM   7120  C  CG2   . ILE   C 2  24  ? 11.878  5.562   -37.402 1.00 51.87  ? 24  ILE   D CG2   1 
ATOM   7121  C  CD1   . ILE   C 2  24  ? 14.182  7.412   -38.176 1.00 38.11  ? 24  ILE   D CD1   1 
ATOM   7122  N  N     . SER   C 2  25  ? 10.931  7.737   -41.169 1.00 47.52  ? 25  SER   D N     1 
ATOM   7123  C  CA    . SER   C 2  25  ? 10.844  8.732   -42.230 1.00 52.29  ? 25  SER   D CA    1 
ATOM   7124  C  C     . SER   C 2  25  ? 9.387   9.071   -42.546 1.00 55.77  ? 25  SER   D C     1 
ATOM   7125  O  O     . SER   C 2  25  ? 9.071   10.220  -42.886 1.00 52.86  ? 25  SER   D O     1 
ATOM   7126  C  CB    . SER   C 2  25  ? 11.587  8.228   -43.470 1.00 46.80  ? 25  SER   D CB    1 
ATOM   7127  O  OG    . SER   C 2  25  ? 12.315  9.283   -44.080 1.00 52.17  ? 25  SER   D OG    1 
ATOM   7128  N  N     . ASP   C 2  26  ? 8.486   8.091   -42.410 1.00 56.01  ? 26  ASP   D N     1 
ATOM   7129  C  CA    . ASP   C 2  26  ? 7.062   8.330   -42.625 1.00 47.03  ? 26  ASP   D CA    1 
ATOM   7130  C  C     . ASP   C 2  26  ? 6.472   9.188   -41.509 1.00 55.28  ? 26  ASP   D C     1 
ATOM   7131  O  O     . ASP   C 2  26  ? 5.823   10.204  -41.780 1.00 68.08  ? 26  ASP   D O     1 
ATOM   7132  C  CB    . ASP   C 2  26  ? 6.330   6.988   -42.760 1.00 56.57  ? 26  ASP   D CB    1 
ATOM   7133  C  CG    . ASP   C 2  26  ? 5.187   6.819   -41.767 1.00 62.09  ? 26  ASP   D CG    1 
ATOM   7134  O  OD1   . ASP   C 2  26  ? 4.160   7.517   -41.928 1.00 54.92  ? 26  ASP   D OD1   1 
ATOM   7135  O  OD2   . ASP   C 2  26  ? 5.310   5.966   -40.849 1.00 58.35  ? 26  ASP   D OD2   1 
ATOM   7136  N  N     . GLU   C 2  27  ? 6.711   8.816   -40.244 1.00 50.03  ? 27  GLU   D N     1 
ATOM   7137  C  CA    . GLU   C 2  27  ? 6.195   9.613   -39.131 1.00 48.87  ? 27  GLU   D CA    1 
ATOM   7138  C  C     . GLU   C 2  27  ? 6.612   11.077  -39.237 1.00 43.88  ? 27  GLU   D C     1 
ATOM   7139  O  O     . GLU   C 2  27  ? 5.849   11.967  -38.852 1.00 46.98  ? 27  GLU   D O     1 
ATOM   7140  C  CB    . GLU   C 2  27  ? 6.663   9.031   -37.791 1.00 46.29  ? 27  GLU   D CB    1 
ATOM   7141  C  CG    . GLU   C 2  27  ? 6.222   7.604   -37.513 1.00 48.77  ? 27  GLU   D CG    1 
ATOM   7142  C  CD    . GLU   C 2  27  ? 6.789   7.055   -36.212 1.00 48.62  ? 27  GLU   D CD    1 
ATOM   7143  O  OE1   . GLU   C 2  27  ? 7.499   7.812   -35.508 1.00 40.67  ? 27  GLU   D OE1   1 
ATOM   7144  O  OE2   . GLU   C 2  27  ? 6.520   5.869   -35.898 1.00 44.54  ? 27  GLU   D OE2   1 
ATOM   7145  N  N     . HIS   C 2  28  ? 7.808   11.347  -39.755 1.00 41.66  ? 28  HIS   D N     1 
ATOM   7146  C  CA    . HIS   C 2  28  ? 8.367   12.690  -39.753 1.00 50.64  ? 28  HIS   D CA    1 
ATOM   7147  C  C     . HIS   C 2  28  ? 8.012   13.498  -40.992 1.00 58.29  ? 28  HIS   D C     1 
ATOM   7148  O  O     . HIS   C 2  28  ? 8.187   14.723  -40.983 1.00 60.59  ? 28  HIS   D O     1 
ATOM   7149  C  CB    . HIS   C 2  28  ? 9.893   12.632  -39.618 1.00 53.22  ? 28  HIS   D CB    1 
ATOM   7150  C  CG    . HIS   C 2  28  ? 10.370  12.269  -38.244 1.00 48.30  ? 28  HIS   D CG    1 
ATOM   7151  N  ND1   . HIS   C 2  28  ? 10.551  13.203  -37.246 1.00 45.88  ? 28  HIS   D ND1   1 
ATOM   7152  C  CD2   . HIS   C 2  28  ? 10.719  11.076  -37.708 1.00 45.35  ? 28  HIS   D CD2   1 
ATOM   7153  C  CE1   . HIS   C 2  28  ? 10.982  12.599  -36.155 1.00 49.39  ? 28  HIS   D CE1   1 
ATOM   7154  N  NE2   . HIS   C 2  28  ? 11.092  11.307  -36.408 1.00 42.25  ? 28  HIS   D NE2   1 
ATOM   7155  N  N     . GLY   C 2  29  ? 7.539   12.853  -42.053 1.00 58.24  ? 29  GLY   D N     1 
ATOM   7156  C  CA    . GLY   C 2  29  ? 7.135   13.573  -43.245 1.00 60.66  ? 29  GLY   D CA    1 
ATOM   7157  C  C     . GLY   C 2  29  ? 8.264   13.740  -44.236 1.00 64.01  ? 29  GLY   D C     1 
ATOM   7158  O  O     . GLY   C 2  29  ? 8.429   14.815  -44.816 1.00 70.42  ? 29  GLY   D O     1 
ATOM   7159  N  N     . ILE   C 2  30  ? 9.048   12.682  -44.433 1.00 62.79  ? 30  ILE   D N     1 
ATOM   7160  C  CA    . ILE   C 2  30  ? 10.163  12.663  -45.375 1.00 65.90  ? 30  ILE   D CA    1 
ATOM   7161  C  C     . ILE   C 2  30  ? 9.873   11.602  -46.428 1.00 65.39  ? 30  ILE   D C     1 
ATOM   7162  O  O     . ILE   C 2  30  ? 9.735   10.416  -46.097 1.00 60.19  ? 30  ILE   D O     1 
ATOM   7163  C  CB    . ILE   C 2  30  ? 11.492  12.367  -44.666 1.00 55.48  ? 30  ILE   D CB    1 
ATOM   7164  C  CG1   . ILE   C 2  30  ? 11.682  13.306  -43.477 1.00 58.32  ? 30  ILE   D CG1   1 
ATOM   7165  C  CG2   . ILE   C 2  30  ? 12.640  12.481  -45.637 1.00 57.79  ? 30  ILE   D CG2   1 
ATOM   7166  C  CD1   . ILE   C 2  30  ? 11.473  14.758  -43.813 1.00 62.06  ? 30  ILE   D CD1   1 
ATOM   7167  N  N     . ASP   C 2  31  ? 9.780   12.016  -47.688 1.00 67.09  ? 31  ASP   D N     1 
ATOM   7168  C  CA    . ASP   C 2  31  ? 9.580   11.085  -48.797 1.00 75.93  ? 31  ASP   D CA    1 
ATOM   7169  C  C     . ASP   C 2  31  ? 10.918  10.558  -49.297 1.00 74.75  ? 31  ASP   D C     1 
ATOM   7170  O  O     . ASP   C 2  31  ? 11.983  11.078  -48.947 1.00 75.52  ? 31  ASP   D O     1 
ATOM   7171  C  CB    . ASP   C 2  31  ? 8.795   11.766  -49.921 1.00 68.09  ? 31  ASP   D CB    1 
ATOM   7172  C  CG    . ASP   C 2  31  ? 9.457   13.038  -50.427 1.00 71.55  ? 31  ASP   D CG    1 
ATOM   7173  O  OD1   . ASP   C 2  31  ? 10.629  13.286  -50.079 1.00 79.25  ? 31  ASP   D OD1   1 
ATOM   7174  O  OD2   . ASP   C 2  31  ? 8.794   13.802  -51.162 1.00 66.56  ? 31  ASP   D OD2   1 
ATOM   7175  N  N     . PRO   C 2  32  ? 10.907  9.496   -50.130 1.00 69.73  ? 32  PRO   D N     1 
ATOM   7176  C  CA    . PRO   C 2  32  ? 12.177  8.903   -50.587 1.00 73.19  ? 32  PRO   D CA    1 
ATOM   7177  C  C     . PRO   C 2  32  ? 13.067  9.858   -51.374 1.00 74.31  ? 32  PRO   D C     1 
ATOM   7178  O  O     . PRO   C 2  32  ? 14.169  9.474   -51.786 1.00 74.44  ? 32  PRO   D O     1 
ATOM   7179  C  CB    . PRO   C 2  32  ? 11.721  7.723   -51.455 1.00 66.26  ? 32  PRO   D CB    1 
ATOM   7180  C  CG    . PRO   C 2  32  ? 10.389  7.360   -50.916 1.00 62.97  ? 32  PRO   D CG    1 
ATOM   7181  C  CD    . PRO   C 2  32  ? 9.749   8.657   -50.487 1.00 62.36  ? 32  PRO   D CD    1 
ATOM   7182  N  N     . THR   C 2  33  ? 12.614  11.098  -51.576 1.00 66.18  ? 33  THR   D N     1 
ATOM   7183  C  CA    . THR   C 2  33  ? 13.375  12.107  -52.300 1.00 69.33  ? 33  THR   D CA    1 
ATOM   7184  C  C     . THR   C 2  33  ? 14.020  13.136  -51.374 1.00 74.91  ? 33  THR   D C     1 
ATOM   7185  O  O     . THR   C 2  33  ? 14.527  14.159  -51.855 1.00 72.65  ? 33  THR   D O     1 
ATOM   7186  C  CB    . THR   C 2  33  ? 12.476  12.809  -53.322 1.00 70.12  ? 33  THR   D CB    1 
ATOM   7187  O  OG1   . THR   C 2  33  ? 11.809  13.919  -52.708 1.00 76.64  ? 33  THR   D OG1   1 
ATOM   7188  C  CG2   . THR   C 2  33  ? 11.429  11.849  -53.838 1.00 69.39  ? 33  THR   D CG2   1 
ATOM   7189  N  N     . GLY   C 2  34  ? 14.012  12.886  -50.062 1.00 74.32  ? 34  GLY   D N     1 
ATOM   7190  C  CA    . GLY   C 2  34  ? 14.535  13.821  -49.085 1.00 72.03  ? 34  GLY   D CA    1 
ATOM   7191  C  C     . GLY   C 2  34  ? 13.662  15.027  -48.802 1.00 73.93  ? 34  GLY   D C     1 
ATOM   7192  O  O     . GLY   C 2  34  ? 14.103  15.934  -48.085 1.00 76.89  ? 34  GLY   D O     1 
ATOM   7193  N  N     . SER   C 2  35  ? 12.447  15.078  -49.339 1.00 78.11  ? 35  SER   D N     1 
ATOM   7194  C  CA    . SER   C 2  35  ? 11.567  16.225  -49.155 1.00 81.18  ? 35  SER   D CA    1 
ATOM   7195  C  C     . SER   C 2  35  ? 10.704  16.039  -47.910 1.00 74.38  ? 35  SER   D C     1 
ATOM   7196  O  O     . SER   C 2  35  ? 10.486  14.922  -47.432 1.00 69.36  ? 35  SER   D O     1 
ATOM   7197  C  CB    . SER   C 2  35  ? 10.668  16.435  -50.385 1.00 75.78  ? 35  SER   D CB    1 
ATOM   7198  O  OG    . SER   C 2  35  ? 11.374  16.354  -51.618 1.00 67.47  ? 35  SER   D OG    1 
ATOM   7199  N  N     . TYR   C 2  36  ? 10.192  17.152  -47.399 1.00 68.68  ? 36  TYR   D N     1 
ATOM   7200  C  CA    . TYR   C 2  36  ? 9.306   17.135  -46.243 1.00 70.08  ? 36  TYR   D CA    1 
ATOM   7201  C  C     . TYR   C 2  36  ? 7.878   17.433  -46.696 1.00 70.19  ? 36  TYR   D C     1 
ATOM   7202  O  O     . TYR   C 2  36  ? 7.529   18.588  -46.974 1.00 60.39  ? 36  TYR   D O     1 
ATOM   7203  C  CB    . TYR   C 2  36  ? 9.779   18.123  -45.183 1.00 66.75  ? 36  TYR   D CB    1 
ATOM   7204  C  CG    . TYR   C 2  36  ? 8.794   18.311  -44.058 1.00 68.50  ? 36  TYR   D CG    1 
ATOM   7205  C  CD1   . TYR   C 2  36  ? 8.577   17.310  -43.118 1.00 64.69  ? 36  TYR   D CD1   1 
ATOM   7206  C  CD2   . TYR   C 2  36  ? 8.085   19.500  -43.928 1.00 72.21  ? 36  TYR   D CD2   1 
ATOM   7207  C  CE1   . TYR   C 2  36  ? 7.672   17.490  -42.088 1.00 67.51  ? 36  TYR   D CE1   1 
ATOM   7208  C  CE2   . TYR   C 2  36  ? 7.185   19.686  -42.904 1.00 74.96  ? 36  TYR   D CE2   1 
ATOM   7209  C  CZ    . TYR   C 2  36  ? 6.981   18.680  -41.991 1.00 68.74  ? 36  TYR   D CZ    1 
ATOM   7210  O  OH    . TYR   C 2  36  ? 6.077   18.874  -40.982 1.00 67.81  ? 36  TYR   D OH    1 
ATOM   7211  N  N     . HIS   C 2  37  ? 7.051   16.385  -46.747 1.00 74.80  ? 37  HIS   D N     1 
ATOM   7212  C  CA    . HIS   C 2  37  ? 5.636   16.474  -47.093 1.00 69.78  ? 37  HIS   D CA    1 
ATOM   7213  C  C     . HIS   C 2  37  ? 4.717   16.180  -45.903 1.00 78.33  ? 37  HIS   D C     1 
ATOM   7214  O  O     . HIS   C 2  37  ? 3.617   15.651  -46.080 1.00 80.79  ? 37  HIS   D O     1 
ATOM   7215  C  CB    . HIS   C 2  37  ? 5.313   15.530  -48.250 1.00 74.48  ? 37  HIS   D CB    1 
ATOM   7216  C  CG    . HIS   C 2  37  ? 5.677   16.077  -49.599 1.00 94.06  ? 37  HIS   D CG    1 
ATOM   7217  N  ND1   . HIS   C 2  37  ? 6.056   17.389  -49.794 1.00 85.43  ? 37  HIS   D ND1   1 
ATOM   7218  C  CD2   . HIS   C 2  37  ? 5.711   15.491  -50.821 1.00 89.13  ? 37  HIS   D CD2   1 
ATOM   7219  C  CE1   . HIS   C 2  37  ? 6.312   17.587  -51.075 1.00 87.70  ? 37  HIS   D CE1   1 
ATOM   7220  N  NE2   . HIS   C 2  37  ? 6.111   16.451  -51.720 1.00 90.86  ? 37  HIS   D NE2   1 
ATOM   7221  N  N     . GLY   C 2  38  ? 5.153   16.516  -44.685 1.00 83.87  ? 38  GLY   D N     1 
ATOM   7222  C  CA    . GLY   C 2  38  ? 4.315   16.448  -43.500 1.00 75.49  ? 38  GLY   D CA    1 
ATOM   7223  C  C     . GLY   C 2  38  ? 3.673   17.788  -43.198 1.00 78.85  ? 38  GLY   D C     1 
ATOM   7224  O  O     . GLY   C 2  38  ? 3.623   18.683  -44.046 1.00 79.28  ? 38  GLY   D O     1 
ATOM   7225  N  N     . ASP   C 2  39  ? 3.189   17.936  -41.957 1.00 82.71  ? 39  ASP   D N     1 
ATOM   7226  C  CA    . ASP   C 2  39  ? 2.434   19.137  -41.592 1.00 81.83  ? 39  ASP   D CA    1 
ATOM   7227  C  C     . ASP   C 2  39  ? 2.885   19.796  -40.281 1.00 87.69  ? 39  ASP   D C     1 
ATOM   7228  O  O     . ASP   C 2  39  ? 3.333   20.949  -40.300 1.00 90.45  ? 39  ASP   D O     1 
ATOM   7229  C  CB    . ASP   C 2  39  ? 0.931   18.816  -41.550 1.00 70.31  ? 39  ASP   D CB    1 
ATOM   7230  C  CG    . ASP   C 2  39  ? 0.605   17.573  -40.727 1.00 74.73  ? 39  ASP   D CG    1 
ATOM   7231  O  OD1   . ASP   C 2  39  ? 1.385   17.218  -39.820 1.00 79.65  ? 39  ASP   D OD1   1 
ATOM   7232  O  OD2   . ASP   C 2  39  ? -0.445  16.949  -40.988 1.00 61.31  ? 39  ASP   D OD2   1 
ATOM   7233  N  N     . SER   C 2  40  ? 2.780   19.096  -39.146 1.00 87.53  ? 40  SER   D N     1 
ATOM   7234  C  CA    . SER   C 2  40  ? 3.081   19.689  -37.840 1.00 82.52  ? 40  SER   D CA    1 
ATOM   7235  C  C     . SER   C 2  40  ? 4.584   19.791  -37.596 1.00 78.55  ? 40  SER   D C     1 
ATOM   7236  O  O     . SER   C 2  40  ? 5.343   18.871  -37.915 1.00 77.22  ? 40  SER   D O     1 
ATOM   7237  C  CB    . SER   C 2  40  ? 2.455   18.858  -36.720 1.00 76.36  ? 40  SER   D CB    1 
ATOM   7238  O  OG    . SER   C 2  40  ? 3.305   17.780  -36.357 1.00 77.67  ? 40  SER   D OG    1 
ATOM   7239  N  N     . ASP   C 2  41  ? 5.013   20.898  -36.984 1.00 67.42  ? 41  ASP   D N     1 
ATOM   7240  C  CA    . ASP   C 2  41  ? 6.435   21.051  -36.690 1.00 72.22  ? 41  ASP   D CA    1 
ATOM   7241  C  C     . ASP   C 2  41  ? 6.934   20.091  -35.624 1.00 71.73  ? 41  ASP   D C     1 
ATOM   7242  O  O     . ASP   C 2  41  ? 8.146   20.043  -35.385 1.00 73.29  ? 41  ASP   D O     1 
ATOM   7243  C  CB    . ASP   C 2  41  ? 6.742   22.472  -36.244 1.00 78.44  ? 41  ASP   D CB    1 
ATOM   7244  C  CG    . ASP   C 2  41  ? 6.176   23.488  -37.177 1.00 73.48  ? 41  ASP   D CG    1 
ATOM   7245  O  OD1   . ASP   C 2  41  ? 4.939   23.466  -37.365 1.00 78.83  ? 41  ASP   D OD1   1 
ATOM   7246  O  OD2   . ASP   C 2  41  ? 6.961   24.294  -37.717 1.00 57.66  ? 41  ASP   D OD2   1 
ATOM   7247  N  N     . LEU   C 2  42  ? 6.042   19.346  -34.971 1.00 67.99  ? 42  LEU   D N     1 
ATOM   7248  C  CA    . LEU   C 2  42  ? 6.480   18.358  -33.991 1.00 66.47  ? 42  LEU   D CA    1 
ATOM   7249  C  C     . LEU   C 2  42  ? 7.302   17.252  -34.638 1.00 67.69  ? 42  LEU   D C     1 
ATOM   7250  O  O     . LEU   C 2  42  ? 8.120   16.612  -33.964 1.00 69.92  ? 42  LEU   D O     1 
ATOM   7251  C  CB    . LEU   C 2  42  ? 5.273   17.768  -33.262 1.00 66.07  ? 42  LEU   D CB    1 
ATOM   7252  C  CG    . LEU   C 2  42  ? 4.540   18.795  -32.406 1.00 68.78  ? 42  LEU   D CG    1 
ATOM   7253  C  CD1   . LEU   C 2  42  ? 5.542   19.564  -31.556 1.00 64.01  ? 42  LEU   D CD1   1 
ATOM   7254  C  CD2   . LEU   C 2  42  ? 3.729   19.748  -33.282 1.00 76.30  ? 42  LEU   D CD2   1 
ATOM   7255  N  N     . GLN   C 2  43  ? 7.108   17.011  -35.934 1.00 61.72  ? 45  GLN   D N     1 
ATOM   7256  C  CA    . GLN   C 2  43  ? 7.932   16.035  -36.626 1.00 58.54  ? 45  GLN   D CA    1 
ATOM   7257  C  C     . GLN   C 2  43  ? 9.229   16.641  -37.142 1.00 55.99  ? 45  GLN   D C     1 
ATOM   7258  O  O     . GLN   C 2  43  ? 10.196  15.909  -37.371 1.00 54.49  ? 45  GLN   D O     1 
ATOM   7259  C  CB    . GLN   C 2  43  ? 7.138   15.408  -37.770 1.00 60.96  ? 45  GLN   D CB    1 
ATOM   7260  C  CG    . GLN   C 2  43  ? 6.282   16.398  -38.537 1.00 67.21  ? 45  GLN   D CG    1 
ATOM   7261  C  CD    . GLN   C 2  43  ? 5.275   15.723  -39.460 1.00 69.92  ? 45  GLN   D CD    1 
ATOM   7262  O  OE1   . GLN   C 2  43  ? 4.552   16.388  -40.201 1.00 71.89  ? 45  GLN   D OE1   1 
ATOM   7263  N  NE2   . GLN   C 2  43  ? 5.228   14.397  -39.418 1.00 60.46  ? 45  GLN   D NE2   1 
ATOM   7264  N  N     . LEU   C 2  44  ? 9.287   17.953  -37.306 1.00 49.93  ? 46  LEU   D N     1 
ATOM   7265  C  CA    . LEU   C 2  44  ? 10.499  18.598  -37.782 1.00 53.37  ? 46  LEU   D CA    1 
ATOM   7266  C  C     . LEU   C 2  44  ? 11.372  19.137  -36.651 1.00 63.67  ? 46  LEU   D C     1 
ATOM   7267  O  O     . LEU   C 2  44  ? 12.454  19.670  -36.919 1.00 67.72  ? 46  LEU   D O     1 
ATOM   7268  C  CB    . LEU   C 2  44  ? 10.139  19.733  -38.749 1.00 51.75  ? 46  LEU   D CB    1 
ATOM   7269  C  CG    . LEU   C 2  44  ? 10.998  19.821  -40.017 1.00 60.86  ? 46  LEU   D CG    1 
ATOM   7270  C  CD1   . LEU   C 2  44  ? 10.762  18.635  -40.960 1.00 56.42  ? 46  LEU   D CD1   1 
ATOM   7271  C  CD2   . LEU   C 2  44  ? 10.782  21.150  -40.731 1.00 71.07  ? 46  LEU   D CD2   1 
ATOM   7272  N  N     . GLU   C 2  45  ? 10.948  19.003  -35.393 1.00 62.80  ? 47  GLU   D N     1 
ATOM   7273  C  CA    . GLU   C 2  45  ? 11.633  19.709  -34.314 1.00 52.28  ? 47  GLU   D CA    1 
ATOM   7274  C  C     . GLU   C 2  45  ? 12.941  19.021  -33.936 1.00 48.53  ? 47  GLU   D C     1 
ATOM   7275  O  O     . GLU   C 2  45  ? 14.007  19.645  -33.929 1.00 44.84  ? 47  GLU   D O     1 
ATOM   7276  C  CB    . GLU   C 2  45  ? 10.706  19.837  -33.102 1.00 63.97  ? 47  GLU   D CB    1 
ATOM   7277  C  CG    . GLU   C 2  45  ? 11.282  20.689  -31.968 1.00 64.39  ? 47  GLU   D CG    1 
ATOM   7278  C  CD    . GLU   C 2  45  ? 10.234  21.545  -31.275 1.00 68.88  ? 47  GLU   D CD    1 
ATOM   7279  O  OE1   . GLU   C 2  45  ? 9.195   20.995  -30.837 1.00 73.41  ? 47  GLU   D OE1   1 
ATOM   7280  O  OE2   . GLU   C 2  45  ? 10.455  22.772  -31.176 1.00 58.99  ? 47  GLU   D OE2   1 
ATOM   7281  N  N     . ARG   C 2  46  ? 12.875  17.734  -33.595 1.00 56.39  ? 48  ARG   D N     1 
ATOM   7282  C  CA    . ARG   C 2  46  ? 14.072  16.934  -33.368 1.00 51.75  ? 48  ARG   D CA    1 
ATOM   7283  C  C     . ARG   C 2  46  ? 14.527  16.217  -34.631 1.00 49.81  ? 48  ARG   D C     1 
ATOM   7284  O  O     . ARG   C 2  46  ? 15.126  15.136  -34.535 1.00 39.70  ? 48  ARG   D O     1 
ATOM   7285  C  CB    . ARG   C 2  46  ? 13.840  15.911  -32.249 1.00 46.95  ? 48  ARG   D CB    1 
ATOM   7286  C  CG    . ARG   C 2  46  ? 12.991  16.370  -31.069 1.00 37.61  ? 48  ARG   D CG    1 
ATOM   7287  C  CD    . ARG   C 2  46  ? 13.789  17.120  -30.018 1.00 38.93  ? 48  ARG   D CD    1 
ATOM   7288  N  NE    . ARG   C 2  46  ? 14.901  16.352  -29.454 1.00 62.06  ? 48  ARG   D NE    1 
ATOM   7289  C  CZ    . ARG   C 2  46  ? 14.779  15.245  -28.721 1.00 55.94  ? 48  ARG   D CZ    1 
ATOM   7290  N  NH1   . ARG   C 2  46  ? 13.596  14.698  -28.479 1.00 46.93  ? 48  ARG   D NH1   1 
ATOM   7291  N  NH2   . ARG   C 2  46  ? 15.875  14.659  -28.238 1.00 44.94  ? 48  ARG   D NH2   1 
ATOM   7292  N  N     . ILE   C 2  47  ? 14.235  16.778  -35.813 1.00 52.68  ? 49  ILE   D N     1 
ATOM   7293  C  CA    . ILE   C 2  47  ? 14.471  16.061  -37.063 1.00 50.52  ? 49  ILE   D CA    1 
ATOM   7294  C  C     . ILE   C 2  47  ? 15.949  15.756  -37.251 1.00 56.38  ? 49  ILE   D C     1 
ATOM   7295  O  O     . ILE   C 2  47  ? 16.303  14.806  -37.952 1.00 56.22  ? 49  ILE   D O     1 
ATOM   7296  C  CB    . ILE   C 2  47  ? 13.902  16.856  -38.264 1.00 50.75  ? 49  ILE   D CB    1 
ATOM   7297  C  CG1   . ILE   C 2  47  ? 13.844  15.994  -39.531 1.00 46.23  ? 49  ILE   D CG1   1 
ATOM   7298  C  CG2   . ILE   C 2  47  ? 14.745  18.101  -38.538 1.00 55.44  ? 49  ILE   D CG2   1 
ATOM   7299  C  CD1   . ILE   C 2  47  ? 13.133  14.677  -39.362 1.00 44.88  ? 49  ILE   D CD1   1 
ATOM   7300  N  N     . ASN   C 2  48  ? 16.827  16.524  -36.618 1.00 51.94  ? 50  ASN   D N     1 
ATOM   7301  C  CA    . ASN   C 2  48  ? 18.254  16.418  -36.863 1.00 46.20  ? 50  ASN   D CA    1 
ATOM   7302  C  C     . ASN   C 2  48  ? 18.914  15.337  -36.028 1.00 51.10  ? 50  ASN   D C     1 
ATOM   7303  O  O     . ASN   C 2  48  ? 20.134  15.164  -36.116 1.00 55.26  ? 50  ASN   D O     1 
ATOM   7304  C  CB    . ASN   C 2  48  ? 18.910  17.770  -36.608 1.00 60.95  ? 50  ASN   D CB    1 
ATOM   7305  C  CG    . ASN   C 2  48  ? 18.039  18.927  -37.082 1.00 80.02  ? 50  ASN   D CG    1 
ATOM   7306  O  OD1   . ASN   C 2  48  ? 17.220  19.446  -36.315 1.00 76.63  ? 50  ASN   D OD1   1 
ATOM   7307  N  ND2   . ASN   C 2  48  ? 18.199  19.328  -38.352 1.00 74.92  ? 50  ASN   D ND2   1 
ATOM   7308  N  N     . VAL   C 2  49  ? 18.137  14.591  -35.243 1.00 51.44  ? 51  VAL   D N     1 
ATOM   7309  C  CA    . VAL   C 2  49  ? 18.693  13.492  -34.459 1.00 42.93  ? 51  VAL   D CA    1 
ATOM   7310  C  C     . VAL   C 2  49  ? 19.039  12.321  -35.357 1.00 42.03  ? 51  VAL   D C     1 
ATOM   7311  O  O     . VAL   C 2  49  ? 19.883  11.488  -35.013 1.00 44.85  ? 51  VAL   D O     1 
ATOM   7312  C  CB    . VAL   C 2  49  ? 17.698  13.074  -33.371 1.00 24.83  ? 51  VAL   D CB    1 
ATOM   7313  C  CG1   . VAL   C 2  49  ? 18.265  11.935  -32.582 1.00 35.16  ? 51  VAL   D CG1   1 
ATOM   7314  C  CG2   . VAL   C 2  49  ? 17.379  14.246  -32.492 1.00 27.51  ? 51  VAL   D CG2   1 
ATOM   7315  N  N     . TYR   C 2  50  ? 18.399  12.241  -36.517 1.00 46.68  ? 52  TYR   D N     1 
ATOM   7316  C  CA    . TYR   C 2  50  ? 18.602  11.160  -37.458 1.00 39.66  ? 52  TYR   D CA    1 
ATOM   7317  C  C     . TYR   C 2  50  ? 18.732  11.660  -38.889 1.00 45.25  ? 52  TYR   D C     1 
ATOM   7318  O  O     . TYR   C 2  50  ? 18.907  10.843  -39.797 1.00 53.84  ? 52  TYR   D O     1 
ATOM   7319  C  CB    . TYR   C 2  50  ? 17.441  10.162  -37.370 1.00 32.46  ? 52  TYR   D CB    1 
ATOM   7320  C  CG    . TYR   C 2  50  ? 17.455  9.209   -36.191 1.00 39.16  ? 52  TYR   D CG    1 
ATOM   7321  C  CD1   . TYR   C 2  50  ? 18.320  8.116   -36.161 1.00 39.10  ? 52  TYR   D CD1   1 
ATOM   7322  C  CD2   . TYR   C 2  50  ? 16.554  9.358   -35.136 1.00 44.66  ? 52  TYR   D CD2   1 
ATOM   7323  C  CE1   . TYR   C 2  50  ? 18.318  7.219   -35.097 1.00 33.77  ? 52  TYR   D CE1   1 
ATOM   7324  C  CE2   . TYR   C 2  50  ? 16.549  8.465   -34.054 1.00 33.68  ? 52  TYR   D CE2   1 
ATOM   7325  C  CZ    . TYR   C 2  50  ? 17.431  7.400   -34.042 1.00 35.61  ? 52  TYR   D CZ    1 
ATOM   7326  O  OH    . TYR   C 2  50  ? 17.420  6.510   -32.982 1.00 35.46  ? 52  TYR   D OH    1 
ATOM   7327  N  N     . TYR   C 2  51  ? 18.641  12.970  -39.120 1.00 42.93  ? 53  TYR   D N     1 
ATOM   7328  C  CA    . TYR   C 2  51  ? 18.638  13.543  -40.461 1.00 47.87  ? 53  TYR   D CA    1 
ATOM   7329  C  C     . TYR   C 2  51  ? 19.643  14.682  -40.529 1.00 44.54  ? 53  TYR   D C     1 
ATOM   7330  O  O     . TYR   C 2  51  ? 19.657  15.549  -39.649 1.00 49.48  ? 53  TYR   D O     1 
ATOM   7331  C  CB    . TYR   C 2  51  ? 17.226  14.042  -40.851 1.00 45.34  ? 53  TYR   D CB    1 
ATOM   7332  C  CG    . TYR   C 2  51  ? 16.275  12.889  -41.076 1.00 51.27  ? 53  TYR   D CG    1 
ATOM   7333  C  CD1   . TYR   C 2  51  ? 16.308  12.174  -42.259 1.00 58.88  ? 53  TYR   D CD1   1 
ATOM   7334  C  CD2   . TYR   C 2  51  ? 15.393  12.468  -40.091 1.00 48.16  ? 53  TYR   D CD2   1 
ATOM   7335  C  CE1   . TYR   C 2  51  ? 15.479  11.094  -42.476 1.00 52.39  ? 53  TYR   D CE1   1 
ATOM   7336  C  CE2   . TYR   C 2  51  ? 14.560  11.376  -40.302 1.00 52.25  ? 53  TYR   D CE2   1 
ATOM   7337  C  CZ    . TYR   C 2  51  ? 14.618  10.700  -41.503 1.00 51.03  ? 53  TYR   D CZ    1 
ATOM   7338  O  OH    . TYR   C 2  51  ? 13.816  9.623   -41.751 1.00 48.43  ? 53  TYR   D OH    1 
ATOM   7339  N  N     . ASN   C 2  52  ? 20.501  14.663  -41.553 1.00 50.19  ? 54  ASN   D N     1 
ATOM   7340  C  CA    . ASN   C 2  52  ? 21.276  15.843  -41.936 1.00 57.49  ? 54  ASN   D CA    1 
ATOM   7341  C  C     . ASN   C 2  52  ? 20.427  16.670  -42.900 1.00 62.34  ? 54  ASN   D C     1 
ATOM   7342  O  O     . ASN   C 2  52  ? 19.741  16.115  -43.766 1.00 65.23  ? 54  ASN   D O     1 
ATOM   7343  C  CB    . ASN   C 2  52  ? 22.615  15.478  -42.602 1.00 55.37  ? 54  ASN   D CB    1 
ATOM   7344  C  CG    . ASN   C 2  52  ? 23.382  14.363  -41.873 1.00 54.48  ? 54  ASN   D CG    1 
ATOM   7345  O  OD1   . ASN   C 2  52  ? 23.858  14.554  -40.756 1.00 60.80  ? 54  ASN   D OD1   1 
ATOM   7346  N  ND2   . ASN   C 2  52  ? 23.543  13.212  -42.534 1.00 48.58  ? 54  ASN   D ND2   1 
ATOM   7347  N  N     . GLU   C 2  53  ? 20.456  17.995  -42.741 1.00 63.57  ? 55  GLU   D N     1 
ATOM   7348  C  CA    . GLU   C 2  53  ? 19.610  18.885  -43.542 1.00 72.68  ? 55  GLU   D CA    1 
ATOM   7349  C  C     . GLU   C 2  53  ? 20.395  19.322  -44.780 1.00 76.82  ? 55  GLU   D C     1 
ATOM   7350  O  O     . GLU   C 2  53  ? 21.142  20.306  -44.748 1.00 60.21  ? 55  GLU   D O     1 
ATOM   7351  C  CB    . GLU   C 2  53  ? 19.131  20.075  -42.714 1.00 70.54  ? 55  GLU   D CB    1 
ATOM   7352  C  CG    . GLU   C 2  53  ? 17.949  20.825  -43.331 1.00 76.26  ? 55  GLU   D CG    1 
ATOM   7353  C  CD    . GLU   C 2  53  ? 17.385  21.904  -42.421 1.00 77.14  ? 55  GLU   D CD    1 
ATOM   7354  O  OE1   . GLU   C 2  53  ? 17.616  21.818  -41.194 1.00 76.75  ? 55  GLU   D OE1   1 
ATOM   7355  O  OE2   . GLU   C 2  53  ? 16.708  22.830  -42.934 1.00 72.80  ? 55  GLU   D OE2   1 
ATOM   7356  N  N     . ALA   C 2  54  ? 20.187  18.601  -45.889 1.00 87.34  ? 56  ALA   D N     1 
ATOM   7357  C  CA    . ALA   C 2  54  ? 20.935  18.758  -47.129 1.00 83.79  ? 56  ALA   D CA    1 
ATOM   7358  C  C     . ALA   C 2  54  ? 20.379  19.897  -47.982 1.00 83.36  ? 56  ALA   D C     1 
ATOM   7359  O  O     . ALA   C 2  54  ? 19.362  20.525  -47.667 1.00 88.92  ? 56  ALA   D O     1 
ATOM   7360  C  CB    . ALA   C 2  54  ? 20.926  17.449  -47.921 1.00 72.53  ? 56  ALA   D CB    1 
ATOM   7361  N  N     . THR   C 2  55  ? 21.057  20.151  -49.096 1.00 84.09  ? 57  THR   D N     1 
ATOM   7362  C  CA    . THR   C 2  55  ? 20.697  21.262  -49.964 1.00 87.93  ? 57  THR   D CA    1 
ATOM   7363  C  C     . THR   C 2  55  ? 19.307  21.067  -50.559 1.00 78.85  ? 57  THR   D C     1 
ATOM   7364  O  O     . THR   C 2  55  ? 18.807  19.947  -50.681 1.00 82.08  ? 57  THR   D O     1 
ATOM   7365  C  CB    . THR   C 2  55  ? 21.739  21.412  -51.067 1.00 89.94  ? 57  THR   D CB    1 
ATOM   7366  O  OG1   . THR   C 2  55  ? 23.000  21.748  -50.468 1.00 90.49  ? 57  THR   D OG1   1 
ATOM   7367  C  CG2   . THR   C 2  55  ? 21.325  22.499  -52.068 1.00 88.06  ? 57  THR   D CG2   1 
ATOM   7368  N  N     . GLY   C 2  56  ? 18.687  22.181  -50.933 1.00 72.04  ? 58  GLY   D N     1 
ATOM   7369  C  CA    . GLY   C 2  56  ? 17.292  22.158  -51.335 1.00 77.52  ? 58  GLY   D CA    1 
ATOM   7370  C  C     . GLY   C 2  56  ? 16.377  21.694  -50.223 1.00 82.90  ? 58  GLY   D C     1 
ATOM   7371  O  O     . GLY   C 2  56  ? 15.454  20.908  -50.471 1.00 84.61  ? 58  GLY   D O     1 
ATOM   7372  N  N     . ASN   C 2  57  ? 16.624  22.150  -48.991 1.00 74.83  ? 59  ASN   D N     1 
ATOM   7373  C  CA    . ASN   C 2  57  ? 15.825  21.731  -47.845 1.00 84.13  ? 59  ASN   D CA    1 
ATOM   7374  C  C     . ASN   C 2  57  ? 15.642  20.214  -47.804 1.00 87.31  ? 59  ASN   D C     1 
ATOM   7375  O  O     . ASN   C 2  57  ? 14.593  19.718  -47.371 1.00 82.90  ? 59  ASN   D O     1 
ATOM   7376  C  CB    . ASN   C 2  57  ? 14.464  22.429  -47.875 1.00 82.36  ? 59  ASN   D CB    1 
ATOM   7377  C  CG    . ASN   C 2  57  ? 14.516  23.829  -47.320 1.00 72.06  ? 59  ASN   D CG    1 
ATOM   7378  O  OD1   . ASN   C 2  57  ? 15.591  24.341  -47.010 1.00 79.60  ? 59  ASN   D OD1   1 
ATOM   7379  N  ND2   . ASN   C 2  57  ? 13.350  24.457  -47.181 1.00 59.45  ? 59  ASN   D ND2   1 
ATOM   7380  N  N     . LYS   C 2  58  ? 16.640  19.469  -48.271 1.00 77.17  ? 60  LYS   D N     1 
ATOM   7381  C  CA    . LYS   C 2  58  ? 16.548  18.019  -48.263 1.00 74.83  ? 60  LYS   D CA    1 
ATOM   7382  C  C     . LYS   C 2  58  ? 16.997  17.479  -46.907 1.00 74.93  ? 60  LYS   D C     1 
ATOM   7383  O  O     . LYS   C 2  58  ? 17.558  18.201  -46.080 1.00 77.71  ? 60  LYS   D O     1 
ATOM   7384  C  CB    . LYS   C 2  58  ? 17.375  17.422  -49.401 1.00 86.52  ? 60  LYS   D CB    1 
ATOM   7385  C  CG    . LYS   C 2  58  ? 16.555  17.012  -50.633 1.00 84.78  ? 60  LYS   D CG    1 
ATOM   7386  C  CD    . LYS   C 2  58  ? 17.460  16.632  -51.821 1.00 92.45  ? 60  LYS   D CD    1 
ATOM   7387  C  CE    . LYS   C 2  58  ? 18.690  15.800  -51.400 1.00 91.50  ? 60  LYS   D CE    1 
ATOM   7388  N  NZ    . LYS   C 2  58  ? 18.368  14.476  -50.768 1.00 81.00  ? 60  LYS   D NZ    1 
ATOM   7389  N  N     . TYR   C 2  59  ? 16.725  16.192  -46.676 1.00 70.80  ? 61  TYR   D N     1 
ATOM   7390  C  CA    . TYR   C 2  59  ? 16.988  15.540  -45.392 1.00 59.49  ? 61  TYR   D CA    1 
ATOM   7391  C  C     . TYR   C 2  59  ? 17.582  14.168  -45.674 1.00 56.28  ? 61  TYR   D C     1 
ATOM   7392  O  O     . TYR   C 2  59  ? 16.866  13.270  -46.123 1.00 55.73  ? 61  TYR   D O     1 
ATOM   7393  C  CB    . TYR   C 2  59  ? 15.708  15.408  -44.558 1.00 51.84  ? 61  TYR   D CB    1 
ATOM   7394  C  CG    . TYR   C 2  59  ? 15.182  16.704  -43.999 1.00 48.45  ? 61  TYR   D CG    1 
ATOM   7395  C  CD1   . TYR   C 2  59  ? 15.932  17.442  -43.093 1.00 60.07  ? 61  TYR   D CD1   1 
ATOM   7396  C  CD2   . TYR   C 2  59  ? 13.937  17.179  -44.353 1.00 47.95  ? 61  TYR   D CD2   1 
ATOM   7397  C  CE1   . TYR   C 2  59  ? 15.464  18.620  -42.570 1.00 51.79  ? 61  TYR   D CE1   1 
ATOM   7398  C  CE2   . TYR   C 2  59  ? 13.456  18.359  -43.838 1.00 48.73  ? 61  TYR   D CE2   1 
ATOM   7399  C  CZ    . TYR   C 2  59  ? 14.224  19.079  -42.944 1.00 58.39  ? 61  TYR   D CZ    1 
ATOM   7400  O  OH    . TYR   C 2  59  ? 13.753  20.267  -42.415 1.00 72.05  ? 61  TYR   D OH    1 
ATOM   7401  N  N     . VAL   C 2  60  ? 18.868  13.994  -45.410 1.00 52.30  ? 62  VAL   D N     1 
ATOM   7402  C  CA    . VAL   C 2  60  ? 19.552  12.723  -45.646 1.00 53.49  ? 62  VAL   D CA    1 
ATOM   7403  C  C     . VAL   C 2  60  ? 19.632  11.964  -44.333 1.00 50.35  ? 62  VAL   D C     1 
ATOM   7404  O  O     . VAL   C 2  60  ? 20.044  12.543  -43.318 1.00 50.63  ? 62  VAL   D O     1 
ATOM   7405  C  CB    . VAL   C 2  60  ? 20.957  12.917  -46.234 1.00 50.11  ? 62  VAL   D CB    1 
ATOM   7406  C  CG1   . VAL   C 2  60  ? 21.331  11.678  -47.016 1.00 51.75  ? 62  VAL   D CG1   1 
ATOM   7407  C  CG2   . VAL   C 2  60  ? 21.012  14.164  -47.087 1.00 56.39  ? 62  VAL   D CG2   1 
ATOM   7408  N  N     . PRO   C 2  61  ? 19.258  10.691  -44.297 1.00 46.10  ? 63  PRO   D N     1 
ATOM   7409  C  CA    . PRO   C 2  61  ? 19.472  9.910   -43.078 1.00 49.86  ? 63  PRO   D CA    1 
ATOM   7410  C  C     . PRO   C 2  61  ? 20.956  9.772   -42.805 1.00 47.33  ? 63  PRO   D C     1 
ATOM   7411  O  O     . PRO   C 2  61  ? 21.710  9.221   -43.613 1.00 45.65  ? 63  PRO   D O     1 
ATOM   7412  C  CB    . PRO   C 2  61  ? 18.819  8.556   -43.387 1.00 45.15  ? 63  PRO   D CB    1 
ATOM   7413  C  CG    . PRO   C 2  61  ? 18.605  8.538   -44.846 1.00 55.63  ? 63  PRO   D CG    1 
ATOM   7414  C  CD    . PRO   C 2  61  ? 18.477  9.963   -45.300 1.00 51.73  ? 63  PRO   D CD    1 
ATOM   7415  N  N     . ARG   C 2  62  ? 21.373  10.296  -41.656 1.00 48.37  ? 64  ARG   D N     1 
ATOM   7416  C  CA    . ARG   C 2  62  ? 22.714  10.029  -41.167 1.00 41.71  ? 64  ARG   D CA    1 
ATOM   7417  C  C     . ARG   C 2  62  ? 22.854  8.527   -40.954 1.00 44.13  ? 64  ARG   D C     1 
ATOM   7418  O  O     . ARG   C 2  62  ? 22.925  8.058   -39.812 1.00 42.49  ? 64  ARG   D O     1 
ATOM   7419  C  CB    . ARG   C 2  62  ? 22.978  10.810  -39.885 1.00 38.64  ? 64  ARG   D CB    1 
ATOM   7420  C  CG    . ARG   C 2  62  ? 24.426  11.155  -39.685 1.00 42.36  ? 64  ARG   D CG    1 
ATOM   7421  C  CD    . ARG   C 2  62  ? 24.665  11.861  -38.366 1.00 42.80  ? 64  ARG   D CD    1 
ATOM   7422  N  NE    . ARG   C 2  62  ? 23.997  13.154  -38.306 1.00 40.99  ? 64  ARG   D NE    1 
ATOM   7423  C  CZ    . ARG   C 2  62  ? 22.778  13.352  -37.826 1.00 37.91  ? 64  ARG   D CZ    1 
ATOM   7424  N  NH1   . ARG   C 2  62  ? 22.042  12.349  -37.371 1.00 36.31  ? 64  ARG   D NH1   1 
ATOM   7425  N  NH2   . ARG   C 2  62  ? 22.290  14.588  -37.793 1.00 37.43  ? 64  ARG   D NH2   1 
ATOM   7426  N  N     . ALA   C 2  63  ? 22.883  7.766   -42.054 1.00 46.04  ? 65  ALA   D N     1 
ATOM   7427  C  CA    . ALA   C 2  63  ? 22.940  6.312   -42.024 1.00 42.79  ? 65  ALA   D CA    1 
ATOM   7428  C  C     . ALA   C 2  63  ? 24.178  5.816   -42.761 1.00 45.54  ? 65  ALA   D C     1 
ATOM   7429  O  O     . ALA   C 2  63  ? 24.539  6.351   -43.812 1.00 53.12  ? 65  ALA   D O     1 
ATOM   7430  C  CB    . ALA   C 2  63  ? 21.686  5.710   -42.656 1.00 38.38  ? 65  ALA   D CB    1 
ATOM   7431  N  N     . ILE   C 2  64  ? 24.828  4.800   -42.198 1.00 42.49  ? 66  ILE   D N     1 
ATOM   7432  C  CA    . ILE   C 2  64  ? 25.979  4.132   -42.799 1.00 39.03  ? 66  ILE   D CA    1 
ATOM   7433  C  C     . ILE   C 2  64  ? 25.597  2.668   -42.997 1.00 48.40  ? 66  ILE   D C     1 
ATOM   7434  O  O     . ILE   C 2  64  ? 25.390  1.940   -42.017 1.00 43.84  ? 66  ILE   D O     1 
ATOM   7435  C  CB    . ILE   C 2  64  ? 27.236  4.248   -41.917 1.00 42.87  ? 66  ILE   D CB    1 
ATOM   7436  C  CG1   . ILE   C 2  64  ? 27.677  5.701   -41.766 1.00 44.06  ? 66  ILE   D CG1   1 
ATOM   7437  C  CG2   . ILE   C 2  64  ? 28.378  3.378   -42.445 1.00 42.59  ? 66  ILE   D CG2   1 
ATOM   7438  C  CD1   . ILE   C 2  64  ? 28.631  5.915   -40.574 1.00 41.18  ? 66  ILE   D CD1   1 
ATOM   7439  N  N     . LEU   C 2  65  ? 25.514  2.233   -44.256 1.00 54.65  ? 67  LEU   D N     1 
ATOM   7440  C  CA    . LEU   C 2  65  ? 25.090  0.880   -44.601 1.00 47.22  ? 67  LEU   D CA    1 
ATOM   7441  C  C     . LEU   C 2  65  ? 26.308  0.041   -44.958 1.00 44.41  ? 67  LEU   D C     1 
ATOM   7442  O  O     . LEU   C 2  65  ? 27.090  0.439   -45.823 1.00 45.66  ? 67  LEU   D O     1 
ATOM   7443  C  CB    . LEU   C 2  65  ? 24.097  0.913   -45.758 1.00 34.91  ? 67  LEU   D CB    1 
ATOM   7444  C  CG    . LEU   C 2  65  ? 22.939  1.895   -45.572 1.00 35.44  ? 67  LEU   D CG    1 
ATOM   7445  C  CD1   . LEU   C 2  65  ? 23.279  3.321   -45.964 1.00 33.16  ? 67  LEU   D CD1   1 
ATOM   7446  C  CD2   . LEU   C 2  65  ? 21.737  1.403   -46.340 1.00 50.66  ? 67  LEU   D CD2   1 
ATOM   7447  N  N     . VAL   C 2  66  ? 26.461  -1.118  -44.297 1.00 41.21  ? 68  VAL   D N     1 
ATOM   7448  C  CA    . VAL   C 2  66  ? 27.661  -1.950  -44.371 1.00 44.28  ? 68  VAL   D CA    1 
ATOM   7449  C  C     . VAL   C 2  66  ? 27.276  -3.405  -44.623 1.00 52.60  ? 68  VAL   D C     1 
ATOM   7450  O  O     . VAL   C 2  66  ? 26.201  -3.852  -44.215 1.00 57.57  ? 68  VAL   D O     1 
ATOM   7451  C  CB    . VAL   C 2  66  ? 28.502  -1.852  -43.072 1.00 49.37  ? 68  VAL   D CB    1 
ATOM   7452  C  CG1   . VAL   C 2  66  ? 29.794  -2.686  -43.193 1.00 54.48  ? 68  VAL   D CG1   1 
ATOM   7453  C  CG2   . VAL   C 2  66  ? 28.791  -0.397  -42.700 1.00 35.05  ? 68  VAL   D CG2   1 
ATOM   7454  N  N     . ASP   C 2  67  ? 28.180  -4.156  -45.278 1.00 58.91  ? 69  ASP   D N     1 
ATOM   7455  C  CA    . ASP   C 2  67  ? 28.031  -5.595  -45.538 1.00 54.22  ? 69  ASP   D CA    1 
ATOM   7456  C  C     . ASP   C 2  67  ? 29.184  -6.117  -46.391 1.00 54.88  ? 69  ASP   D C     1 
ATOM   7457  O  O     . ASP   C 2  67  ? 29.624  -5.435  -47.318 1.00 54.89  ? 69  ASP   D O     1 
ATOM   7458  C  CB    . ASP   C 2  67  ? 26.703  -5.902  -46.250 1.00 53.21  ? 69  ASP   D CB    1 
ATOM   7459  C  CG    . ASP   C 2  67  ? 26.234  -7.370  -46.070 1.00 54.36  ? 69  ASP   D CG    1 
ATOM   7460  O  OD1   . ASP   C 2  67  ? 26.956  -8.195  -45.453 1.00 52.27  ? 69  ASP   D OD1   1 
ATOM   7461  O  OD2   . ASP   C 2  67  ? 25.114  -7.688  -46.543 1.00 44.66  ? 69  ASP   D OD2   1 
ATOM   7462  N  N     . LEU   C 2  68  ? 29.673  -7.324  -46.100 1.00 51.67  ? 70  LEU   D N     1 
ATOM   7463  C  CA    . LEU   C 2  68  ? 30.671  -7.988  -46.932 1.00 51.55  ? 70  LEU   D CA    1 
ATOM   7464  C  C     . LEU   C 2  68  ? 30.060  -8.679  -48.167 1.00 63.75  ? 70  LEU   D C     1 
ATOM   7465  O  O     . LEU   C 2  68  ? 30.720  -9.512  -48.802 1.00 65.28  ? 70  LEU   D O     1 
ATOM   7466  C  CB    . LEU   C 2  68  ? 31.451  -9.009  -46.102 1.00 49.96  ? 70  LEU   D CB    1 
ATOM   7467  C  CG    . LEU   C 2  68  ? 32.119  -8.534  -44.818 1.00 45.36  ? 70  LEU   D CG    1 
ATOM   7468  C  CD1   . LEU   C 2  68  ? 32.823  -9.678  -44.154 1.00 42.19  ? 70  LEU   D CD1   1 
ATOM   7469  C  CD2   . LEU   C 2  68  ? 33.090  -7.398  -45.099 1.00 55.89  ? 70  LEU   D CD2   1 
ATOM   7470  N  N     . GLU   C 2  69  ? 28.816  -8.354  -48.517 1.00 59.49  ? 71  GLU   D N     1 
ATOM   7471  C  CA    . GLU   C 2  69  ? 28.100  -8.988  -49.615 1.00 61.55  ? 71  GLU   D CA    1 
ATOM   7472  C  C     . GLU   C 2  69  ? 27.263  -7.950  -50.337 1.00 68.85  ? 71  GLU   D C     1 
ATOM   7473  O  O     . GLU   C 2  69  ? 26.196  -7.568  -49.843 1.00 70.00  ? 71  GLU   D O     1 
ATOM   7474  C  CB    . GLU   C 2  69  ? 27.187  -10.098 -49.107 1.00 64.67  ? 71  GLU   D CB    1 
ATOM   7475  C  CG    . GLU   C 2  69  ? 27.873  -11.421 -48.914 1.00 72.87  ? 71  GLU   D CG    1 
ATOM   7476  C  CD    . GLU   C 2  69  ? 27.537  -12.393 -50.019 1.00 81.22  ? 71  GLU   D CD    1 
ATOM   7477  O  OE1   . GLU   C 2  69  ? 26.790  -12.015 -50.949 1.00 80.97  ? 71  GLU   D OE1   1 
ATOM   7478  O  OE2   . GLU   C 2  69  ? 28.027  -13.541 -49.949 1.00 81.30  ? 71  GLU   D OE2   1 
ATOM   7479  N  N     . PRO   C 2  70  ? 27.685  -7.498  -51.516 1.00 75.06  ? 72  PRO   D N     1 
ATOM   7480  C  CA    . PRO   C 2  70  ? 26.979  -6.377  -52.160 1.00 79.21  ? 72  PRO   D CA    1 
ATOM   7481  C  C     . PRO   C 2  70  ? 25.516  -6.662  -52.433 1.00 77.36  ? 72  PRO   D C     1 
ATOM   7482  O  O     . PRO   C 2  70  ? 24.764  -5.720  -52.707 1.00 88.64  ? 72  PRO   D O     1 
ATOM   7483  C  CB    . PRO   C 2  70  ? 27.767  -6.158  -53.459 1.00 80.72  ? 72  PRO   D CB    1 
ATOM   7484  C  CG    . PRO   C 2  70  ? 28.453  -7.458  -53.710 1.00 82.00  ? 72  PRO   D CG    1 
ATOM   7485  C  CD    . PRO   C 2  70  ? 28.737  -8.071  -52.365 1.00 67.23  ? 72  PRO   D CD    1 
ATOM   7486  N  N     . GLY   C 2  71  ? 25.085  -7.918  -52.354 1.00 72.62  ? 73  GLY   D N     1 
ATOM   7487  C  CA    . GLY   C 2  71  ? 23.686  -8.247  -52.543 1.00 71.71  ? 73  GLY   D CA    1 
ATOM   7488  C  C     . GLY   C 2  71  ? 22.759  -7.367  -51.734 1.00 79.77  ? 73  GLY   D C     1 
ATOM   7489  O  O     . GLY   C 2  71  ? 21.906  -6.666  -52.289 1.00 86.19  ? 73  GLY   D O     1 
ATOM   7490  N  N     . THR   C 2  72  ? 22.936  -7.386  -50.411 1.00 82.93  ? 74  THR   D N     1 
ATOM   7491  C  CA    . THR   C 2  72  ? 22.085  -6.602  -49.521 1.00 82.17  ? 74  THR   D CA    1 
ATOM   7492  C  C     . THR   C 2  72  ? 22.095  -5.118  -49.899 1.00 83.30  ? 74  THR   D C     1 
ATOM   7493  O  O     . THR   C 2  72  ? 21.038  -4.476  -49.973 1.00 82.76  ? 74  THR   D O     1 
ATOM   7494  C  CB    . THR   C 2  72  ? 22.542  -6.817  -48.074 1.00 73.48  ? 74  THR   D CB    1 
ATOM   7495  O  OG1   . THR   C 2  72  ? 23.885  -6.337  -47.913 1.00 59.47  ? 74  THR   D OG1   1 
ATOM   7496  C  CG2   . THR   C 2  72  ? 22.506  -8.315  -47.719 1.00 62.40  ? 74  THR   D CG2   1 
ATOM   7497  N  N     . MET   C 2  73  ? 23.283  -4.565  -50.174 1.00 74.89  ? 75  MET   D N     1 
ATOM   7498  C  CA    . MET   C 2  73  ? 23.407  -3.134  -50.459 1.00 82.83  ? 75  MET   D CA    1 
ATOM   7499  C  C     . MET   C 2  73  ? 22.515  -2.699  -51.625 1.00 77.89  ? 75  MET   D C     1 
ATOM   7500  O  O     . MET   C 2  73  ? 21.846  -1.658  -51.556 1.00 73.59  ? 75  MET   D O     1 
ATOM   7501  C  CB    . MET   C 2  73  ? 24.878  -2.786  -50.743 1.00 87.38  ? 75  MET   D CB    1 
ATOM   7502  C  CG    . MET   C 2  73  ? 25.493  -1.672  -49.857 1.00 82.90  ? 75  MET   D CG    1 
ATOM   7503  S  SD    . MET   C 2  73  ? 25.719  -2.057  -48.100 1.00 71.70  ? 75  MET   D SD    1 
ATOM   7504  C  CE    . MET   C 2  73  ? 26.884  -3.402  -48.100 1.00 57.14  ? 75  MET   D CE    1 
ATOM   7505  N  N     . ASP   C 2  74  ? 22.498  -3.472  -52.710 1.00 76.46  ? 76  ASP   D N     1 
ATOM   7506  C  CA    . ASP   C 2  74  ? 21.797  -3.022  -53.909 1.00 84.91  ? 76  ASP   D CA    1 
ATOM   7507  C  C     . ASP   C 2  74  ? 20.285  -3.092  -53.720 1.00 80.57  ? 76  ASP   D C     1 
ATOM   7508  O  O     . ASP   C 2  74  ? 19.561  -2.161  -54.105 1.00 68.00  ? 76  ASP   D O     1 
ATOM   7509  C  CB    . ASP   C 2  74  ? 22.246  -3.857  -55.110 1.00 86.76  ? 76  ASP   D CB    1 
ATOM   7510  C  CG    . ASP   C 2  74  ? 23.725  -4.225  -55.044 1.00 86.25  ? 76  ASP   D CG    1 
ATOM   7511  O  OD1   . ASP   C 2  74  ? 24.556  -3.348  -54.714 1.00 85.27  ? 76  ASP   D OD1   1 
ATOM   7512  O  OD2   . ASP   C 2  74  ? 24.057  -5.399  -55.306 1.00 87.38  ? 76  ASP   D OD2   1 
ATOM   7513  N  N     . SER   C 2  75  ? 19.801  -4.188  -53.120 1.00 75.35  ? 77  SER   D N     1 
ATOM   7514  C  CA    . SER   C 2  75  ? 18.380  -4.356  -52.811 1.00 74.42  ? 77  SER   D CA    1 
ATOM   7515  C  C     . SER   C 2  75  ? 17.812  -3.133  -52.101 1.00 78.27  ? 77  SER   D C     1 
ATOM   7516  O  O     . SER   C 2  75  ? 16.830  -2.524  -52.547 1.00 70.44  ? 77  SER   D O     1 
ATOM   7517  C  CB    . SER   C 2  75  ? 18.193  -5.601  -51.944 1.00 71.47  ? 77  SER   D CB    1 
ATOM   7518  O  OG    . SER   C 2  75  ? 18.938  -5.501  -50.740 1.00 67.12  ? 77  SER   D OG    1 
ATOM   7519  N  N     . VAL   C 2  76  ? 18.410  -2.789  -50.963 1.00 77.08  ? 78  VAL   D N     1 
ATOM   7520  C  CA    . VAL   C 2  76  ? 18.108  -1.570  -50.229 1.00 71.55  ? 78  VAL   D CA    1 
ATOM   7521  C  C     . VAL   C 2  76  ? 18.047  -0.394  -51.193 1.00 76.93  ? 78  VAL   D C     1 
ATOM   7522  O  O     . VAL   C 2  76  ? 16.969  0.162   -51.439 1.00 78.27  ? 78  VAL   D O     1 
ATOM   7523  C  CB    . VAL   C 2  76  ? 19.155  -1.344  -49.128 1.00 67.01  ? 78  VAL   D CB    1 
ATOM   7524  C  CG1   . VAL   C 2  76  ? 19.142  0.099   -48.664 1.00 62.05  ? 78  VAL   D CG1   1 
ATOM   7525  C  CG2   . VAL   C 2  76  ? 18.906  -2.309  -47.973 1.00 62.18  ? 78  VAL   D CG2   1 
ATOM   7526  N  N     . ARG   C 2  77  ? 19.203  -0.022  -51.752 1.00 80.58  ? 79  ARG   D N     1 
ATOM   7527  C  CA    . ARG   C 2  77  ? 19.330  1.036   -52.752 1.00 71.45  ? 79  ARG   D CA    1 
ATOM   7528  C  C     . ARG   C 2  77  ? 18.112  1.092   -53.664 1.00 75.08  ? 79  ARG   D C     1 
ATOM   7529  O  O     . ARG   C 2  77  ? 17.708  2.173   -54.103 1.00 77.22  ? 79  ARG   D O     1 
ATOM   7530  C  CB    . ARG   C 2  77  ? 20.597  0.816   -53.582 1.00 63.72  ? 79  ARG   D CB    1 
ATOM   7531  C  CG    . ARG   C 2  77  ? 21.351  2.080   -53.945 1.00 65.79  ? 79  ARG   D CG    1 
ATOM   7532  C  CD    . ARG   C 2  77  ? 22.449  1.797   -54.972 1.00 70.66  ? 79  ARG   D CD    1 
ATOM   7533  N  NE    . ARG   C 2  77  ? 23.631  1.157   -54.403 1.00 61.54  ? 79  ARG   D NE    1 
ATOM   7534  C  CZ    . ARG   C 2  77  ? 24.753  1.796   -54.097 1.00 64.42  ? 79  ARG   D CZ    1 
ATOM   7535  N  NH1   . ARG   C 2  77  ? 24.870  3.106   -54.265 1.00 71.16  ? 79  ARG   D NH1   1 
ATOM   7536  N  NH2   . ARG   C 2  77  ? 25.784  1.106   -53.613 1.00 62.52  ? 79  ARG   D NH2   1 
ATOM   7537  N  N     . SER   C 2  78  ? 17.512  -0.076  -53.932 1.00 77.54  ? 80  SER   D N     1 
ATOM   7538  C  CA    . SER   C 2  78  ? 16.381  -0.189  -54.851 1.00 76.58  ? 80  SER   D CA    1 
ATOM   7539  C  C     . SER   C 2  78  ? 15.044  0.070   -54.157 1.00 77.87  ? 80  SER   D C     1 
ATOM   7540  O  O     . SER   C 2  78  ? 14.215  0.846   -54.651 1.00 65.27  ? 80  SER   D O     1 
ATOM   7541  C  CB    . SER   C 2  78  ? 16.389  -1.578  -55.486 1.00 74.12  ? 80  SER   D CB    1 
ATOM   7542  O  OG    . SER   C 2  78  ? 17.708  -1.941  -55.859 1.00 74.96  ? 80  SER   D OG    1 
ATOM   7543  N  N     . GLY   C 2  79  ? 14.810  -0.592  -53.027 1.00 81.97  ? 81  GLY   D N     1 
ATOM   7544  C  CA    . GLY   C 2  79  ? 13.591  -0.413  -52.279 1.00 82.73  ? 81  GLY   D CA    1 
ATOM   7545  C  C     . GLY   C 2  79  ? 13.373  1.039   -51.905 1.00 83.50  ? 81  GLY   D C     1 
ATOM   7546  O  O     . GLY   C 2  79  ? 14.311  1.846   -51.888 1.00 80.85  ? 81  GLY   D O     1 
ATOM   7547  N  N     . PRO   C 2  80  ? 12.131  1.398   -51.576 1.00 89.11  ? 82  PRO   D N     1 
ATOM   7548  C  CA    . PRO   C 2  80  ? 11.830  2.806   -51.301 1.00 84.44  ? 82  PRO   D CA    1 
ATOM   7549  C  C     . PRO   C 2  80  ? 12.624  3.275   -50.097 1.00 89.41  ? 82  PRO   D C     1 
ATOM   7550  O  O     . PRO   C 2  80  ? 12.751  2.564   -49.096 1.00 76.66  ? 82  PRO   D O     1 
ATOM   7551  C  CB    . PRO   C 2  80  ? 10.323  2.803   -51.028 1.00 73.88  ? 82  PRO   D CB    1 
ATOM   7552  C  CG    . PRO   C 2  80  ? 10.087  1.457   -50.423 1.00 84.93  ? 82  PRO   D CG    1 
ATOM   7553  C  CD    . PRO   C 2  80  ? 11.046  0.509   -51.121 1.00 88.59  ? 82  PRO   D CD    1 
ATOM   7554  N  N     . PHE   C 2  81  ? 13.175  4.479   -50.214 1.00 92.81  ? 83  PHE   D N     1 
ATOM   7555  C  CA    . PHE   C 2  81  ? 14.072  5.068   -49.234 1.00 78.70  ? 83  PHE   D CA    1 
ATOM   7556  C  C     . PHE   C 2  81  ? 15.455  4.445   -49.307 1.00 78.78  ? 83  PHE   D C     1 
ATOM   7557  O  O     . PHE   C 2  81  ? 16.329  4.792   -48.489 1.00 73.61  ? 83  PHE   D O     1 
ATOM   7558  C  CB    . PHE   C 2  81  ? 13.499  4.970   -47.815 1.00 66.78  ? 83  PHE   D CB    1 
ATOM   7559  C  CG    . PHE   C 2  81  ? 12.179  5.663   -47.665 1.00 63.71  ? 83  PHE   D CG    1 
ATOM   7560  C  CD1   . PHE   C 2  81  ? 12.118  7.046   -47.564 1.00 68.44  ? 83  PHE   D CD1   1 
ATOM   7561  C  CD2   . PHE   C 2  81  ? 11.000  4.943   -47.659 1.00 66.99  ? 83  PHE   D CD2   1 
ATOM   7562  C  CE1   . PHE   C 2  81  ? 10.905  7.699   -47.437 1.00 63.93  ? 83  PHE   D CE1   1 
ATOM   7563  C  CE2   . PHE   C 2  81  ? 9.783   5.586   -47.523 1.00 68.90  ? 83  PHE   D CE2   1 
ATOM   7564  C  CZ    . PHE   C 2  81  ? 9.737   6.968   -47.410 1.00 66.82  ? 83  PHE   D CZ    1 
ATOM   7565  N  N     . GLY   C 2  82  ? 15.683  3.528   -50.252 1.00 72.70  ? 84  GLY   D N     1 
ATOM   7566  C  CA    . GLY   C 2  82  ? 17.025  3.142   -50.634 1.00 76.06  ? 84  GLY   D CA    1 
ATOM   7567  C  C     . GLY   C 2  82  ? 17.743  4.189   -51.451 1.00 74.73  ? 84  GLY   D C     1 
ATOM   7568  O  O     . GLY   C 2  82  ? 18.972  4.115   -51.585 1.00 75.92  ? 84  GLY   D O     1 
ATOM   7569  N  N     . GLN   C 2  83  ? 16.999  5.168   -51.977 1.00 68.42  ? 85  GLN   D N     1 
ATOM   7570  C  CA    . GLN   C 2  83  ? 17.520  6.266   -52.782 1.00 73.48  ? 85  GLN   D CA    1 
ATOM   7571  C  C     . GLN   C 2  83  ? 17.661  7.558   -51.993 1.00 69.83  ? 85  GLN   D C     1 
ATOM   7572  O  O     . GLN   C 2  83  ? 18.157  8.548   -52.539 1.00 74.81  ? 85  GLN   D O     1 
ATOM   7573  C  CB    . GLN   C 2  83  ? 16.613  6.538   -53.999 1.00 81.46  ? 85  GLN   D CB    1 
ATOM   7574  C  CG    . GLN   C 2  83  ? 15.877  5.320   -54.584 1.00 90.79  ? 85  GLN   D CG    1 
ATOM   7575  C  CD    . GLN   C 2  83  ? 14.685  4.870   -53.736 1.00 92.56  ? 85  GLN   D CD    1 
ATOM   7576  O  OE1   . GLN   C 2  83  ? 14.393  5.452   -52.684 1.00 91.82  ? 85  GLN   D OE1   1 
ATOM   7577  N  NE2   . GLN   C 2  83  ? 13.998  3.822   -54.190 1.00 82.35  ? 85  GLN   D NE2   1 
ATOM   7578  N  N     . ILE   C 2  84  ? 17.199  7.587   -50.745 1.00 76.69  ? 86  ILE   D N     1 
ATOM   7579  C  CA    . ILE   C 2  84  ? 17.400  8.751   -49.887 1.00 78.79  ? 86  ILE   D CA    1 
ATOM   7580  C  C     . ILE   C 2  84  ? 18.718  8.660   -49.124 1.00 65.25  ? 86  ILE   D C     1 
ATOM   7581  O  O     . ILE   C 2  84  ? 19.251  9.694   -48.689 1.00 55.26  ? 86  ILE   D O     1 
ATOM   7582  C  CB    . ILE   C 2  84  ? 16.207  8.904   -48.922 1.00 77.19  ? 86  ILE   D CB    1 
ATOM   7583  C  CG1   . ILE   C 2  84  ? 16.210  10.275  -48.243 1.00 65.99  ? 86  ILE   D CG1   1 
ATOM   7584  C  CG2   . ILE   C 2  84  ? 16.195  7.770   -47.885 1.00 63.04  ? 86  ILE   D CG2   1 
ATOM   7585  C  CD1   . ILE   C 2  84  ? 15.084  10.429  -47.247 1.00 62.11  ? 86  ILE   D CD1   1 
ATOM   7586  N  N     . PHE   C 2  85  ? 19.264  7.456   -48.971 1.00 52.75  ? 87  PHE   D N     1 
ATOM   7587  C  CA    . PHE   C 2  85  ? 20.569  7.282   -48.371 1.00 58.35  ? 87  PHE   D CA    1 
ATOM   7588  C  C     . PHE   C 2  85  ? 21.626  8.062   -49.159 1.00 68.67  ? 87  PHE   D C     1 
ATOM   7589  O  O     . PHE   C 2  85  ? 21.436  8.417   -50.324 1.00 74.57  ? 87  PHE   D O     1 
ATOM   7590  C  CB    . PHE   C 2  85  ? 20.899  5.789   -48.301 1.00 66.73  ? 87  PHE   D CB    1 
ATOM   7591  C  CG    . PHE   C 2  85  ? 19.970  4.999   -47.393 1.00 69.03  ? 87  PHE   D CG    1 
ATOM   7592  C  CD1   . PHE   C 2  85  ? 19.414  5.585   -46.264 1.00 61.70  ? 87  PHE   D CD1   1 
ATOM   7593  C  CD2   . PHE   C 2  85  ? 19.661  3.674   -47.662 1.00 66.52  ? 87  PHE   D CD2   1 
ATOM   7594  C  CE1   . PHE   C 2  85  ? 18.571  4.869   -45.422 1.00 52.02  ? 87  PHE   D CE1   1 
ATOM   7595  C  CE2   . PHE   C 2  85  ? 18.810  2.955   -46.818 1.00 66.07  ? 87  PHE   D CE2   1 
ATOM   7596  C  CZ    . PHE   C 2  85  ? 18.268  3.555   -45.701 1.00 57.17  ? 87  PHE   D CZ    1 
ATOM   7597  N  N     . ARG   C 2  86  ? 22.750  8.355   -48.497 1.00 72.48  ? 88  ARG   D N     1 
ATOM   7598  C  CA    . ARG   C 2  86  ? 23.868  9.040   -49.141 1.00 67.86  ? 88  ARG   D CA    1 
ATOM   7599  C  C     . ARG   C 2  86  ? 24.794  8.016   -49.790 1.00 69.15  ? 88  ARG   D C     1 
ATOM   7600  O  O     . ARG   C 2  86  ? 25.415  7.217   -49.071 1.00 65.93  ? 88  ARG   D O     1 
ATOM   7601  C  CB    . ARG   C 2  86  ? 24.636  9.879   -48.132 1.00 65.44  ? 88  ARG   D CB    1 
ATOM   7602  C  CG    . ARG   C 2  86  ? 26.153  9.786   -48.260 1.00 65.57  ? 88  ARG   D CG    1 
ATOM   7603  C  CD    . ARG   C 2  86  ? 26.863  10.750  -47.332 1.00 56.75  ? 88  ARG   D CD    1 
ATOM   7604  N  NE    . ARG   C 2  86  ? 26.278  12.081  -47.428 1.00 62.93  ? 88  ARG   D NE    1 
ATOM   7605  C  CZ    . ARG   C 2  86  ? 25.330  12.544  -46.623 1.00 71.50  ? 88  ARG   D CZ    1 
ATOM   7606  N  NH1   . ARG   C 2  86  ? 24.859  11.817  -45.615 1.00 70.79  ? 88  ARG   D NH1   1 
ATOM   7607  N  NH2   . ARG   C 2  86  ? 24.839  13.763  -46.835 1.00 62.07  ? 88  ARG   D NH2   1 
ATOM   7608  N  N     . PRO   C 2  87  ? 24.955  8.026   -51.119 1.00 71.37  ? 89  PRO   D N     1 
ATOM   7609  C  CA    . PRO   C 2  87  ? 25.594  6.878   -51.797 1.00 66.18  ? 89  PRO   D CA    1 
ATOM   7610  C  C     . PRO   C 2  87  ? 26.981  6.569   -51.287 1.00 60.83  ? 89  PRO   D C     1 
ATOM   7611  O  O     . PRO   C 2  87  ? 27.367  5.394   -51.221 1.00 56.45  ? 89  PRO   D O     1 
ATOM   7612  C  CB    . PRO   C 2  87  ? 25.632  7.309   -53.269 1.00 65.29  ? 89  PRO   D CB    1 
ATOM   7613  C  CG    . PRO   C 2  87  ? 24.668  8.452   -53.376 1.00 77.75  ? 89  PRO   D CG    1 
ATOM   7614  C  CD    . PRO   C 2  87  ? 24.677  9.136   -52.042 1.00 78.08  ? 89  PRO   D CD    1 
ATOM   7615  N  N     . ASP   C 2  88  ? 27.747  7.599   -50.931 1.00 61.15  ? 90  ASP   D N     1 
ATOM   7616  C  CA    . ASP   C 2  88  ? 29.056  7.421   -50.323 1.00 52.46  ? 90  ASP   D CA    1 
ATOM   7617  C  C     . ASP   C 2  88  ? 28.990  6.766   -48.946 1.00 56.25  ? 90  ASP   D C     1 
ATOM   7618  O  O     . ASP   C 2  88  ? 30.041  6.510   -48.356 1.00 54.67  ? 90  ASP   D O     1 
ATOM   7619  C  CB    . ASP   C 2  88  ? 29.764  8.775   -50.237 1.00 57.00  ? 90  ASP   D CB    1 
ATOM   7620  C  CG    . ASP   C 2  88  ? 28.817  9.950   -50.480 1.00 73.36  ? 90  ASP   D CG    1 
ATOM   7621  O  OD1   . ASP   C 2  88  ? 27.878  9.828   -51.308 1.00 67.20  ? 90  ASP   D OD1   1 
ATOM   7622  O  OD2   . ASP   C 2  88  ? 29.015  11.005  -49.837 1.00 83.98  ? 90  ASP   D OD2   1 
ATOM   7623  N  N     . ASN   C 2  89  ? 27.799  6.486   -48.413 1.00 63.11  ? 91  ASN   D N     1 
ATOM   7624  C  CA    . ASN   C 2  89  ? 27.692  5.762   -47.152 1.00 58.39  ? 91  ASN   D CA    1 
ATOM   7625  C  C     . ASN   C 2  89  ? 27.479  4.260   -47.346 1.00 54.29  ? 91  ASN   D C     1 
ATOM   7626  O  O     . ASN   C 2  89  ? 27.563  3.503   -46.372 1.00 51.29  ? 91  ASN   D O     1 
ATOM   7627  C  CB    . ASN   C 2  89  ? 26.565  6.353   -46.287 1.00 52.32  ? 91  ASN   D CB    1 
ATOM   7628  C  CG    . ASN   C 2  89  ? 26.925  7.713   -45.694 1.00 55.63  ? 91  ASN   D CG    1 
ATOM   7629  O  OD1   . ASN   C 2  89  ? 27.791  8.414   -46.209 1.00 67.32  ? 91  ASN   D OD1   1 
ATOM   7630  N  ND2   . ASN   C 2  89  ? 26.254  8.091   -44.615 1.00 49.12  ? 91  ASN   D ND2   1 
ATOM   7631  N  N     . PHE   C 2  90  ? 27.206  3.807   -48.569 1.00 62.67  ? 92  PHE   D N     1 
ATOM   7632  C  CA    . PHE   C 2  90  ? 27.166  2.376   -48.872 1.00 57.27  ? 92  PHE   D CA    1 
ATOM   7633  C  C     . PHE   C 2  90  ? 28.605  1.885   -48.923 1.00 52.57  ? 92  PHE   D C     1 
ATOM   7634  O  O     . PHE   C 2  90  ? 29.282  2.003   -49.942 1.00 61.01  ? 92  PHE   D O     1 
ATOM   7635  C  CB    . PHE   C 2  90  ? 26.463  2.102   -50.193 1.00 56.17  ? 92  PHE   D CB    1 
ATOM   7636  C  CG    . PHE   C 2  90  ? 24.996  2.427   -50.206 1.00 55.80  ? 92  PHE   D CG    1 
ATOM   7637  C  CD1   . PHE   C 2  90  ? 24.552  3.742   -50.269 1.00 57.78  ? 92  PHE   D CD1   1 
ATOM   7638  C  CD2   . PHE   C 2  90  ? 24.058  1.411   -50.223 1.00 55.07  ? 92  PHE   D CD2   1 
ATOM   7639  C  CE1   . PHE   C 2  90  ? 23.188  4.032   -50.316 1.00 60.98  ? 92  PHE   D CE1   1 
ATOM   7640  C  CE2   . PHE   C 2  90  ? 22.695  1.699   -50.270 1.00 60.62  ? 92  PHE   D CE2   1 
ATOM   7641  C  CZ    . PHE   C 2  90  ? 22.262  3.010   -50.320 1.00 56.46  ? 92  PHE   D CZ    1 
ATOM   7642  N  N     . VAL   C 2  91  ? 29.083  1.350   -47.804 1.00 49.44  ? 93  VAL   D N     1 
ATOM   7643  C  CA    . VAL   C 2  91  ? 30.391  0.716   -47.709 1.00 40.96  ? 93  VAL   D CA    1 
ATOM   7644  C  C     . VAL   C 2  91  ? 30.161  -0.789  -47.695 1.00 55.14  ? 93  VAL   D C     1 
ATOM   7645  O  O     . VAL   C 2  91  ? 29.670  -1.339  -46.700 1.00 53.87  ? 93  VAL   D O     1 
ATOM   7646  C  CB    . VAL   C 2  91  ? 31.152  1.171   -46.458 1.00 40.40  ? 93  VAL   D CB    1 
ATOM   7647  C  CG1   . VAL   C 2  91  ? 32.502  0.468   -46.369 1.00 39.62  ? 93  VAL   D CG1   1 
ATOM   7648  C  CG2   . VAL   C 2  91  ? 31.315  2.664   -46.458 1.00 40.31  ? 93  VAL   D CG2   1 
ATOM   7649  N  N     . PHE   C 2  92  ? 30.518  -1.468  -48.793 1.00 59.96  ? 94  PHE   D N     1 
ATOM   7650  C  CA    . PHE   C 2  92  ? 30.221  -2.886  -48.942 1.00 57.15  ? 94  PHE   D CA    1 
ATOM   7651  C  C     . PHE   C 2  92  ? 31.416  -3.673  -49.453 1.00 51.75  ? 94  PHE   D C     1 
ATOM   7652  O  O     . PHE   C 2  92  ? 32.091  -3.255  -50.393 1.00 58.49  ? 94  PHE   D O     1 
ATOM   7653  C  CB    . PHE   C 2  92  ? 29.027  -3.101  -49.885 1.00 65.88  ? 94  PHE   D CB    1 
ATOM   7654  C  CG    . PHE   C 2  92  ? 29.199  -2.531  -51.262 1.00 70.84  ? 94  PHE   D CG    1 
ATOM   7655  C  CD1   . PHE   C 2  92  ? 29.373  -3.378  -52.348 1.00 77.96  ? 94  PHE   D CD1   1 
ATOM   7656  C  CD2   . PHE   C 2  92  ? 29.118  -1.164  -51.489 1.00 70.91  ? 94  PHE   D CD2   1 
ATOM   7657  C  CE1   . PHE   C 2  92  ? 29.512  -2.867  -53.637 1.00 78.27  ? 94  PHE   D CE1   1 
ATOM   7658  C  CE2   . PHE   C 2  92  ? 29.254  -0.645  -52.775 1.00 72.04  ? 94  PHE   D CE2   1 
ATOM   7659  C  CZ    . PHE   C 2  92  ? 29.458  -1.499  -53.847 1.00 73.42  ? 94  PHE   D CZ    1 
ATOM   7660  N  N     . GLY   C 2  93  ? 31.651  -4.833  -48.841 1.00 60.96  ? 95  GLY   D N     1 
ATOM   7661  C  CA    . GLY   C 2  93  ? 32.669  -5.751  -49.306 1.00 70.30  ? 95  GLY   D CA    1 
ATOM   7662  C  C     . GLY   C 2  93  ? 32.127  -6.798  -50.267 1.00 62.94  ? 95  GLY   D C     1 
ATOM   7663  O  O     . GLY   C 2  93  ? 30.946  -6.837  -50.605 1.00 70.85  ? 95  GLY   D O     1 
ATOM   7664  N  N     . GLN   C 2  94  ? 33.020  -7.672  -50.717 1.00 60.90  ? 96  GLN   D N     1 
ATOM   7665  C  CA    . GLN   C 2  94  ? 32.641  -8.669  -51.705 1.00 64.98  ? 96  GLN   D CA    1 
ATOM   7666  C  C     . GLN   C 2  94  ? 32.914  -10.097 -51.271 1.00 72.35  ? 96  GLN   D C     1 
ATOM   7667  O  O     . GLN   C 2  94  ? 32.358  -11.017 -51.880 1.00 58.26  ? 96  GLN   D O     1 
ATOM   7668  C  CB    . GLN   C 2  94  ? 33.365  -8.414  -53.036 1.00 61.31  ? 96  GLN   D CB    1 
ATOM   7669  C  CG    . GLN   C 2  94  ? 33.688  -6.942  -53.319 1.00 64.46  ? 96  GLN   D CG    1 
ATOM   7670  C  CD    . GLN   C 2  94  ? 32.452  -6.083  -53.557 1.00 75.87  ? 96  GLN   D CD    1 
ATOM   7671  O  OE1   . GLN   C 2  94  ? 31.603  -6.407  -54.396 1.00 87.38  ? 96  GLN   D OE1   1 
ATOM   7672  N  NE2   . GLN   C 2  94  ? 32.347  -4.976  -52.818 1.00 63.19  ? 96  GLN   D NE2   1 
ATOM   7673  N  N     . SER   C 2  95  ? 33.722  -10.308 -50.227 1.00 82.23  ? 97  SER   D N     1 
ATOM   7674  C  CA    . SER   C 2  95  ? 34.130  -11.661 -49.847 1.00 95.32  ? 97  SER   D CA    1 
ATOM   7675  C  C     . SER   C 2  95  ? 32.925  -12.528 -49.483 1.00 93.63  ? 97  SER   D C     1 
ATOM   7676  O  O     . SER   C 2  95  ? 32.692  -13.576 -50.100 1.00 92.47  ? 97  SER   D O     1 
ATOM   7677  C  CB    . SER   C 2  95  ? 35.132  -11.604 -48.689 1.00 84.55  ? 97  SER   D CB    1 
ATOM   7678  O  OG    . SER   C 2  95  ? 36.016  -12.716 -48.728 1.00 84.67  ? 97  SER   D OG    1 
ATOM   7679  N  N     . GLY   C 2  96  ? 32.161  -12.122 -48.462 1.00 79.36  ? 98  GLY   D N     1 
ATOM   7680  C  CA    . GLY   C 2  96  ? 30.946  -12.842 -48.109 1.00 79.16  ? 98  GLY   D CA    1 
ATOM   7681  C  C     . GLY   C 2  96  ? 30.696  -13.182 -46.646 1.00 80.21  ? 98  GLY   D C     1 
ATOM   7682  O  O     . GLY   C 2  96  ? 29.534  -13.346 -46.253 1.00 77.09  ? 98  GLY   D O     1 
ATOM   7683  N  N     . ALA   C 2  97  ? 31.750  -13.317 -45.829 1.00 72.13  ? 99  ALA   D N     1 
ATOM   7684  C  CA    . ALA   C 2  97  ? 31.591  -13.659 -44.414 1.00 64.76  ? 99  ALA   D CA    1 
ATOM   7685  C  C     . ALA   C 2  97  ? 30.985  -15.044 -44.245 1.00 60.97  ? 99  ALA   D C     1 
ATOM   7686  O  O     . ALA   C 2  97  ? 31.518  -15.886 -43.511 1.00 51.90  ? 99  ALA   D O     1 
ATOM   7687  C  CB    . ALA   C 2  97  ? 30.715  -12.631 -43.692 1.00 56.53  ? 99  ALA   D CB    1 
ATOM   7688  N  N     . GLY   C 2  98  ? 29.860  -15.276 -44.914 1.00 60.20  ? 100 GLY   D N     1 
ATOM   7689  C  CA    . GLY   C 2  98  ? 29.218  -16.567 -44.891 1.00 59.36  ? 100 GLY   D CA    1 
ATOM   7690  C  C     . GLY   C 2  98  ? 29.016  -17.051 -43.477 1.00 56.80  ? 100 GLY   D C     1 
ATOM   7691  O  O     . GLY   C 2  98  ? 29.699  -17.983 -43.026 1.00 46.67  ? 100 GLY   D O     1 
ATOM   7692  N  N     . ASN   C 2  99  ? 28.097  -16.391 -42.769 1.00 56.13  ? 101 ASN   D N     1 
ATOM   7693  C  CA    . ASN   C 2  99  ? 27.662  -16.816 -41.443 1.00 60.02  ? 101 ASN   D CA    1 
ATOM   7694  C  C     . ASN   C 2  99  ? 28.837  -17.302 -40.595 1.00 52.74  ? 101 ASN   D C     1 
ATOM   7695  O  O     . ASN   C 2  99  ? 28.724  -18.315 -39.893 1.00 50.60  ? 101 ASN   D O     1 
ATOM   7696  C  CB    . ASN   C 2  99  ? 26.590  -17.912 -41.568 1.00 53.82  ? 101 ASN   D CB    1 
ATOM   7697  C  CG    . ASN   C 2  99  ? 25.267  -17.400 -42.157 1.00 50.91  ? 101 ASN   D CG    1 
ATOM   7698  O  OD1   . ASN   C 2  99  ? 25.227  -16.658 -43.134 1.00 47.34  ? 101 ASN   D OD1   1 
ATOM   7699  N  ND2   . ASN   C 2  99  ? 24.176  -17.812 -41.548 1.00 68.50  ? 101 ASN   D ND2   1 
ATOM   7700  N  N     . ASN   C 2  100 ? 29.976  -16.605 -40.679 1.00 59.03  ? 102 ASN   D N     1 
ATOM   7701  C  CA    . ASN   C 2  100 ? 31.182  -16.937 -39.918 1.00 66.77  ? 102 ASN   D CA    1 
ATOM   7702  C  C     . ASN   C 2  100 ? 31.589  -15.723 -39.090 1.00 66.08  ? 102 ASN   D C     1 
ATOM   7703  O  O     . ASN   C 2  100 ? 31.851  -14.644 -39.634 1.00 58.84  ? 102 ASN   D O     1 
ATOM   7704  C  CB    . ASN   C 2  100 ? 32.334  -17.384 -40.834 1.00 59.27  ? 102 ASN   D CB    1 
ATOM   7705  C  CG    . ASN   C 2  100 ? 33.431  -18.161 -40.079 1.00 59.76  ? 102 ASN   D CG    1 
ATOM   7706  O  OD1   . ASN   C 2  100 ? 33.489  -18.122 -38.857 1.00 64.56  ? 102 ASN   D OD1   1 
ATOM   7707  N  ND2   . ASN   C 2  100 ? 34.304  -18.856 -40.812 1.00 59.04  ? 102 ASN   D ND2   1 
ATOM   7708  N  N     . TRP   C 2  101 ? 31.625  -15.896 -37.771 1.00 68.80  ? 103 TRP   D N     1 
ATOM   7709  C  CA    . TRP   C 2  101 ? 32.054  -14.808 -36.909 1.00 70.71  ? 103 TRP   D CA    1 
ATOM   7710  C  C     . TRP   C 2  101 ? 33.480  -14.443 -37.296 1.00 57.96  ? 103 TRP   D C     1 
ATOM   7711  O  O     . TRP   C 2  101 ? 33.714  -13.356 -37.835 1.00 61.31  ? 103 TRP   D O     1 
ATOM   7712  C  CB    . TRP   C 2  101 ? 31.936  -15.197 -35.422 1.00 66.51  ? 103 TRP   D CB    1 
ATOM   7713  C  CG    . TRP   C 2  101 ? 31.876  -14.008 -34.458 1.00 56.01  ? 103 TRP   D CG    1 
ATOM   7714  C  CD1   . TRP   C 2  101 ? 30.822  -13.147 -34.267 1.00 47.03  ? 103 TRP   D CD1   1 
ATOM   7715  C  CD2   . TRP   C 2  101 ? 32.920  -13.563 -33.569 1.00 55.83  ? 103 TRP   D CD2   1 
ATOM   7716  N  NE1   . TRP   C 2  101 ? 31.153  -12.198 -33.320 1.00 49.02  ? 103 TRP   D NE1   1 
ATOM   7717  C  CE2   . TRP   C 2  101 ? 32.430  -12.436 -32.877 1.00 50.11  ? 103 TRP   D CE2   1 
ATOM   7718  C  CE3   . TRP   C 2  101 ? 34.225  -14.006 -33.299 1.00 48.06  ? 103 TRP   D CE3   1 
ATOM   7719  C  CZ2   . TRP   C 2  101 ? 33.195  -11.759 -31.932 1.00 46.58  ? 103 TRP   D CZ2   1 
ATOM   7720  C  CZ3   . TRP   C 2  101 ? 34.973  -13.338 -32.359 1.00 39.77  ? 103 TRP   D CZ3   1 
ATOM   7721  C  CH2   . TRP   C 2  101 ? 34.458  -12.231 -31.683 1.00 47.45  ? 103 TRP   D CH2   1 
ATOM   7722  N  N     . ALA   C 2  102 ? 34.422  -15.363 -37.075 1.00 52.23  ? 104 ALA   D N     1 
ATOM   7723  C  CA    . ALA   C 2  102 ? 35.833  -15.122 -37.364 1.00 50.88  ? 104 ALA   D CA    1 
ATOM   7724  C  C     . ALA   C 2  102 ? 36.033  -14.334 -38.654 1.00 53.57  ? 104 ALA   D C     1 
ATOM   7725  O  O     . ALA   C 2  102 ? 36.927  -13.490 -38.741 1.00 57.08  ? 104 ALA   D O     1 
ATOM   7726  C  CB    . ALA   C 2  102 ? 36.595  -16.442 -37.448 1.00 49.21  ? 104 ALA   D CB    1 
ATOM   7727  N  N     . LYS   C 2  103 ? 35.203  -14.592 -39.661 1.00 56.33  ? 105 LYS   D N     1 
ATOM   7728  C  CA    . LYS   C 2  103 ? 35.358  -13.886 -40.926 1.00 62.34  ? 105 LYS   D CA    1 
ATOM   7729  C  C     . LYS   C 2  103 ? 35.029  -12.405 -40.779 1.00 59.46  ? 105 LYS   D C     1 
ATOM   7730  O  O     . LYS   C 2  103 ? 35.739  -11.551 -41.320 1.00 65.87  ? 105 LYS   D O     1 
ATOM   7731  C  CB    . LYS   C 2  103 ? 34.471  -14.525 -41.997 1.00 73.57  ? 105 LYS   D CB    1 
ATOM   7732  C  CG    . LYS   C 2  103 ? 34.737  -16.010 -42.271 1.00 67.24  ? 105 LYS   D CG    1 
ATOM   7733  C  CD    . LYS   C 2  103 ? 35.760  -16.214 -43.368 1.00 63.30  ? 105 LYS   D CD    1 
ATOM   7734  C  CE    . LYS   C 2  103 ? 35.510  -17.513 -44.115 1.00 66.66  ? 105 LYS   D CE    1 
ATOM   7735  N  NZ    . LYS   C 2  103 ? 34.863  -17.285 -45.445 1.00 65.38  ? 105 LYS   D NZ    1 
ATOM   7736  N  N     . GLY   C 2  104 ? 33.950  -12.080 -40.060 1.00 62.73  ? 106 GLY   D N     1 
ATOM   7737  C  CA    . GLY   C 2  104 ? 33.549  -10.690 -39.898 1.00 65.23  ? 106 GLY   D CA    1 
ATOM   7738  C  C     . GLY   C 2  104 ? 34.301  -9.921  -38.825 1.00 57.51  ? 106 GLY   D C     1 
ATOM   7739  O  O     . GLY   C 2  104 ? 34.333  -8.688  -38.875 1.00 59.86  ? 106 GLY   D O     1 
ATOM   7740  N  N     . HIS   C 2  105 ? 34.914  -10.613 -37.865 1.00 43.49  ? 107 HIS   D N     1 
ATOM   7741  C  CA    . HIS   C 2  105 ? 35.594  -9.954  -36.759 1.00 50.79  ? 107 HIS   D CA    1 
ATOM   7742  C  C     . HIS   C 2  105 ? 37.093  -9.805  -36.976 1.00 56.52  ? 107 HIS   D C     1 
ATOM   7743  O  O     . HIS   C 2  105 ? 37.648  -8.736  -36.690 1.00 58.53  ? 107 HIS   D O     1 
ATOM   7744  C  CB    . HIS   C 2  105 ? 35.356  -10.722 -35.452 1.00 50.04  ? 107 HIS   D CB    1 
ATOM   7745  C  CG    . HIS   C 2  105 ? 35.456  -9.870  -34.220 1.00 50.47  ? 107 HIS   D CG    1 
ATOM   7746  N  ND1   . HIS   C 2  105 ? 34.586  -8.830  -33.959 1.00 53.44  ? 107 HIS   D ND1   1 
ATOM   7747  C  CD2   . HIS   C 2  105 ? 36.317  -9.907  -33.176 1.00 47.03  ? 107 HIS   D CD2   1 
ATOM   7748  C  CE1   . HIS   C 2  105 ? 34.909  -8.265  -32.809 1.00 46.18  ? 107 HIS   D CE1   1 
ATOM   7749  N  NE2   . HIS   C 2  105 ? 35.954  -8.902  -32.313 1.00 45.19  ? 107 HIS   D NE2   1 
ATOM   7750  N  N     . TYR   C 2  106 ? 37.761  -10.848 -37.471 1.00 55.84  ? 108 TYR   D N     1 
ATOM   7751  C  CA    . TYR   C 2  106 ? 39.217  -10.921 -37.511 1.00 56.40  ? 108 TYR   D CA    1 
ATOM   7752  C  C     . TYR   C 2  106 ? 39.814  -10.767 -38.902 1.00 56.69  ? 108 TYR   D C     1 
ATOM   7753  O  O     . TYR   C 2  106 ? 40.748  -9.979  -39.086 1.00 48.72  ? 108 TYR   D O     1 
ATOM   7754  C  CB    . TYR   C 2  106 ? 39.673  -12.248 -36.905 1.00 50.30  ? 108 TYR   D CB    1 
ATOM   7755  C  CG    . TYR   C 2  106 ? 39.503  -12.285 -35.417 1.00 54.70  ? 108 TYR   D CG    1 
ATOM   7756  C  CD1   . TYR   C 2  106 ? 39.641  -11.137 -34.665 1.00 51.26  ? 108 TYR   D CD1   1 
ATOM   7757  C  CD2   . TYR   C 2  106 ? 39.205  -13.469 -34.762 1.00 57.81  ? 108 TYR   D CD2   1 
ATOM   7758  C  CE1   . TYR   C 2  106 ? 39.489  -11.163 -33.295 1.00 62.05  ? 108 TYR   D CE1   1 
ATOM   7759  C  CE2   . TYR   C 2  106 ? 39.051  -13.510 -33.397 1.00 59.33  ? 108 TYR   D CE2   1 
ATOM   7760  C  CZ    . TYR   C 2  106 ? 39.191  -12.353 -32.660 1.00 63.25  ? 108 TYR   D CZ    1 
ATOM   7761  O  OH    . TYR   C 2  106 ? 39.038  -12.385 -31.285 1.00 60.09  ? 108 TYR   D OH    1 
ATOM   7762  N  N     . THR   C 2  107 ? 39.314  -11.519 -39.883 1.00 61.85  ? 109 THR   D N     1 
ATOM   7763  C  CA    . THR   C 2  107 ? 39.909  -11.520 -41.213 1.00 57.54  ? 109 THR   D CA    1 
ATOM   7764  C  C     . THR   C 2  107 ? 39.125  -10.637 -42.182 1.00 57.49  ? 109 THR   D C     1 
ATOM   7765  O  O     . THR   C 2  107 ? 39.428  -9.447  -42.325 1.00 61.90  ? 109 THR   D O     1 
ATOM   7766  C  CB    . THR   C 2  107 ? 40.010  -12.945 -41.761 1.00 59.07  ? 109 THR   D CB    1 
ATOM   7767  O  OG1   . THR   C 2  107 ? 38.693  -13.468 -41.967 1.00 68.48  ? 109 THR   D OG1   1 
ATOM   7768  C  CG2   . THR   C 2  107 ? 40.798  -13.862 -40.799 1.00 44.63  ? 109 THR   D CG2   1 
ATOM   7769  N  N     . GLU   C 2  108 ? 38.114  -11.198 -42.852 1.00 57.19  ? 110 GLU   D N     1 
ATOM   7770  C  CA    . GLU   C 2  108 ? 37.486  -10.471 -43.953 1.00 60.28  ? 110 GLU   D CA    1 
ATOM   7771  C  C     . GLU   C 2  108 ? 36.798  -9.193  -43.491 1.00 61.92  ? 110 GLU   D C     1 
ATOM   7772  O  O     . GLU   C 2  108 ? 36.637  -8.258  -44.284 1.00 57.43  ? 110 GLU   D O     1 
ATOM   7773  C  CB    . GLU   C 2  108 ? 36.500  -11.375 -44.685 1.00 66.29  ? 110 GLU   D CB    1 
ATOM   7774  C  CG    . GLU   C 2  108 ? 37.177  -12.286 -45.677 1.00 67.17  ? 110 GLU   D CG    1 
ATOM   7775  C  CD    . GLU   C 2  108 ? 36.490  -13.612 -45.769 1.00 77.50  ? 110 GLU   D CD    1 
ATOM   7776  O  OE1   . GLU   C 2  108 ? 35.260  -13.616 -46.000 1.00 80.63  ? 110 GLU   D OE1   1 
ATOM   7777  O  OE2   . GLU   C 2  108 ? 37.175  -14.643 -45.581 1.00 77.97  ? 110 GLU   D OE2   1 
ATOM   7778  N  N     . GLY   C 2  109 ? 36.390  -9.126  -42.224 1.00 69.02  ? 111 GLY   D N     1 
ATOM   7779  C  CA    . GLY   C 2  109 ? 35.801  -7.911  -41.683 1.00 59.94  ? 111 GLY   D CA    1 
ATOM   7780  C  C     . GLY   C 2  109 ? 36.843  -6.863  -41.346 1.00 56.90  ? 111 GLY   D C     1 
ATOM   7781  O  O     . GLY   C 2  109 ? 36.654  -5.670  -41.627 1.00 55.94  ? 111 GLY   D O     1 
ATOM   7782  N  N     . ALA   C 2  110 ? 37.958  -7.322  -40.756 1.00 53.49  ? 112 ALA   D N     1 
ATOM   7783  C  CA    . ALA   C 2  110 ? 39.049  -6.436  -40.352 1.00 52.01  ? 112 ALA   D CA    1 
ATOM   7784  C  C     . ALA   C 2  110 ? 39.610  -5.639  -41.522 1.00 56.93  ? 112 ALA   D C     1 
ATOM   7785  O  O     . ALA   C 2  110 ? 40.033  -4.489  -41.351 1.00 50.48  ? 112 ALA   D O     1 
ATOM   7786  C  CB    . ALA   C 2  110 ? 40.160  -7.253  -39.699 1.00 48.86  ? 112 ALA   D CB    1 
ATOM   7787  N  N     . GLU   C 2  111 ? 39.635  -6.234  -42.713 1.00 55.34  ? 113 GLU   D N     1 
ATOM   7788  C  CA    . GLU   C 2  111 ? 40.135  -5.520  -43.877 1.00 56.18  ? 113 GLU   D CA    1 
ATOM   7789  C  C     . GLU   C 2  111 ? 39.220  -4.352  -44.249 1.00 61.21  ? 113 GLU   D C     1 
ATOM   7790  O  O     . GLU   C 2  111 ? 39.692  -3.237  -44.510 1.00 68.57  ? 113 GLU   D O     1 
ATOM   7791  C  CB    . GLU   C 2  111 ? 40.287  -6.503  -45.032 1.00 63.08  ? 113 GLU   D CB    1 
ATOM   7792  C  CG    . GLU   C 2  111 ? 40.882  -7.843  -44.608 1.00 54.28  ? 113 GLU   D CG    1 
ATOM   7793  C  CD    . GLU   C 2  111 ? 40.836  -8.893  -45.725 1.00 75.01  ? 113 GLU   D CD    1 
ATOM   7794  O  OE1   . GLU   C 2  111 ? 40.098  -8.689  -46.719 1.00 82.87  ? 113 GLU   D OE1   1 
ATOM   7795  O  OE2   . GLU   C 2  111 ? 41.535  -9.927  -45.610 1.00 69.98  ? 113 GLU   D OE2   1 
ATOM   7796  N  N     . LEU   C 2  112 ? 37.907  -4.573  -44.255 1.00 58.45  ? 114 LEU   D N     1 
ATOM   7797  C  CA    . LEU   C 2  112 ? 37.002  -3.512  -44.683 1.00 61.76  ? 114 LEU   D CA    1 
ATOM   7798  C  C     . LEU   C 2  112 ? 36.774  -2.475  -43.587 1.00 59.14  ? 114 LEU   D C     1 
ATOM   7799  O  O     . LEU   C 2  112 ? 36.636  -1.280  -43.885 1.00 54.06  ? 114 LEU   D O     1 
ATOM   7800  C  CB    . LEU   C 2  112 ? 35.671  -4.118  -45.135 1.00 60.56  ? 114 LEU   D CB    1 
ATOM   7801  C  CG    . LEU   C 2  112 ? 34.449  -3.197  -45.216 1.00 59.93  ? 114 LEU   D CG    1 
ATOM   7802  C  CD1   . LEU   C 2  112 ? 34.606  -2.108  -46.277 1.00 56.64  ? 114 LEU   D CD1   1 
ATOM   7803  C  CD2   . LEU   C 2  112 ? 33.181  -4.027  -45.442 1.00 63.62  ? 114 LEU   D CD2   1 
ATOM   7804  N  N     . VAL   C 2  113 ? 36.739  -2.912  -42.324 1.00 59.23  ? 115 VAL   D N     1 
ATOM   7805  C  CA    . VAL   C 2  113 ? 36.342  -2.077  -41.191 1.00 55.70  ? 115 VAL   D CA    1 
ATOM   7806  C  C     . VAL   C 2  113 ? 36.856  -0.650  -41.347 1.00 48.15  ? 115 VAL   D C     1 
ATOM   7807  O  O     . VAL   C 2  113 ? 36.089  0.316   -41.249 1.00 46.26  ? 115 VAL   D O     1 
ATOM   7808  C  CB    . VAL   C 2  113 ? 36.834  -2.687  -39.870 1.00 47.09  ? 115 VAL   D CB    1 
ATOM   7809  C  CG1   . VAL   C 2  113 ? 38.320  -2.933  -39.937 1.00 46.22  ? 115 VAL   D CG1   1 
ATOM   7810  C  CG2   . VAL   C 2  113 ? 36.507  -1.756  -38.726 1.00 46.41  ? 115 VAL   D CG2   1 
ATOM   7811  N  N     . ASP   C 2  114 ? 38.156  -0.508  -41.598 1.00 47.31  ? 116 ASP   D N     1 
ATOM   7812  C  CA    . ASP   C 2  114 ? 38.726  0.818   -41.779 1.00 45.36  ? 116 ASP   D CA    1 
ATOM   7813  C  C     . ASP   C 2  114 ? 37.961  1.608   -42.830 1.00 49.72  ? 116 ASP   D C     1 
ATOM   7814  O  O     . ASP   C 2  114 ? 37.693  2.805   -42.659 1.00 39.21  ? 116 ASP   D O     1 
ATOM   7815  C  CB    . ASP   C 2  114 ? 40.194  0.681   -42.147 1.00 42.04  ? 116 ASP   D CB    1 
ATOM   7816  C  CG    . ASP   C 2  114 ? 41.059  0.489   -40.938 1.00 41.93  ? 116 ASP   D CG    1 
ATOM   7817  O  OD1   . ASP   C 2  114 ? 40.761  1.144   -39.934 1.00 39.85  ? 116 ASP   D OD1   1 
ATOM   7818  O  OD2   . ASP   C 2  114 ? 42.019  -0.305  -40.971 1.00 58.01  ? 116 ASP   D OD2   1 
ATOM   7819  N  N     . SER   C 2  115 ? 37.589  0.951   -43.925 1.00 56.74  ? 117 SER   D N     1 
ATOM   7820  C  CA    . SER   C 2  115 ? 36.750  1.611   -44.913 1.00 50.60  ? 117 SER   D CA    1 
ATOM   7821  C  C     . SER   C 2  115 ? 35.511  2.204   -44.252 1.00 48.32  ? 117 SER   D C     1 
ATOM   7822  O  O     . SER   C 2  115 ? 35.173  3.370   -44.487 1.00 42.96  ? 117 SER   D O     1 
ATOM   7823  C  CB    . SER   C 2  115 ? 36.390  0.617   -46.015 1.00 50.47  ? 117 SER   D CB    1 
ATOM   7824  O  OG    . SER   C 2  115 ? 37.534  -0.160  -46.355 1.00 56.82  ? 117 SER   D OG    1 
ATOM   7825  N  N     . VAL   C 2  116 ? 34.855  1.423   -43.374 1.00 50.78  ? 118 VAL   D N     1 
ATOM   7826  C  CA    . VAL   C 2  116 ? 33.631  1.873   -42.699 1.00 47.02  ? 118 VAL   D CA    1 
ATOM   7827  C  C     . VAL   C 2  116 ? 33.923  3.043   -41.765 1.00 45.12  ? 118 VAL   D C     1 
ATOM   7828  O  O     . VAL   C 2  116 ? 33.249  4.084   -41.808 1.00 36.56  ? 118 VAL   D O     1 
ATOM   7829  C  CB    . VAL   C 2  116 ? 32.979  0.714   -41.924 1.00 47.40  ? 118 VAL   D CB    1 
ATOM   7830  C  CG1   . VAL   C 2  116 ? 31.725  1.212   -41.153 1.00 43.48  ? 118 VAL   D CG1   1 
ATOM   7831  C  CG2   . VAL   C 2  116 ? 32.643  -0.440  -42.847 1.00 48.78  ? 118 VAL   D CG2   1 
ATOM   7832  N  N     . LEU   C 2  117 ? 34.913  2.869   -40.880 1.00 42.70  ? 119 LEU   D N     1 
ATOM   7833  C  CA    . LEU   C 2  117 ? 35.243  3.906   -39.911 1.00 42.06  ? 119 LEU   D CA    1 
ATOM   7834  C  C     . LEU   C 2  117 ? 35.473  5.247   -40.593 1.00 41.41  ? 119 LEU   D C     1 
ATOM   7835  O  O     . LEU   C 2  117 ? 35.104  6.295   -40.054 1.00 45.71  ? 119 LEU   D O     1 
ATOM   7836  C  CB    . LEU   C 2  117 ? 36.467  3.481   -39.104 1.00 36.03  ? 119 LEU   D CB    1 
ATOM   7837  C  CG    . LEU   C 2  117 ? 36.308  2.178   -38.322 1.00 36.35  ? 119 LEU   D CG    1 
ATOM   7838  C  CD1   . LEU   C 2  117 ? 37.567  1.813   -37.574 1.00 31.49  ? 119 LEU   D CD1   1 
ATOM   7839  C  CD2   . LEU   C 2  117 ? 35.151  2.307   -37.358 1.00 43.11  ? 119 LEU   D CD2   1 
ATOM   7840  N  N     . ASP   C 2  118 ? 36.071  5.238   -41.785 1.00 41.50  ? 120 ASP   D N     1 
ATOM   7841  C  CA    . ASP   C 2  118 ? 36.260  6.487   -42.517 1.00 45.95  ? 120 ASP   D CA    1 
ATOM   7842  C  C     . ASP   C 2  118 ? 34.930  7.189   -42.769 1.00 43.55  ? 120 ASP   D C     1 
ATOM   7843  O  O     . ASP   C 2  118 ? 34.868  8.419   -42.749 1.00 46.71  ? 120 ASP   D O     1 
ATOM   7844  C  CB    . ASP   C 2  118 ? 36.985  6.234   -43.845 1.00 53.10  ? 120 ASP   D CB    1 
ATOM   7845  C  CG    . ASP   C 2  118 ? 38.506  6.292   -43.722 1.00 50.49  ? 120 ASP   D CG    1 
ATOM   7846  O  OD1   . ASP   C 2  118 ? 39.021  6.940   -42.783 1.00 47.84  ? 120 ASP   D OD1   1 
ATOM   7847  O  OD2   . ASP   C 2  118 ? 39.186  5.690   -44.585 1.00 51.99  ? 120 ASP   D OD2   1 
ATOM   7848  N  N     . VAL   C 2  119 ? 33.856  6.431   -43.020 1.00 49.86  ? 121 VAL   D N     1 
ATOM   7849  C  CA    . VAL   C 2  119 ? 32.561  7.056   -43.289 1.00 46.11  ? 121 VAL   D CA    1 
ATOM   7850  C  C     . VAL   C 2  119 ? 31.916  7.527   -41.997 1.00 43.71  ? 121 VAL   D C     1 
ATOM   7851  O  O     . VAL   C 2  119 ? 31.339  8.622   -41.948 1.00 39.28  ? 121 VAL   D O     1 
ATOM   7852  C  CB    . VAL   C 2  119 ? 31.632  6.099   -44.059 1.00 43.39  ? 121 VAL   D CB    1 
ATOM   7853  C  CG1   . VAL   C 2  119 ? 30.944  6.838   -45.203 1.00 35.52  ? 121 VAL   D CG1   1 
ATOM   7854  C  CG2   . VAL   C 2  119 ? 32.389  4.843   -44.512 1.00 40.15  ? 121 VAL   D CG2   1 
ATOM   7855  N  N     . VAL   C 2  120 ? 31.973  6.697   -40.947 1.00 38.66  ? 122 VAL   D N     1 
ATOM   7856  C  CA    . VAL   C 2  120 ? 31.495  7.134   -39.638 1.00 38.17  ? 122 VAL   D CA    1 
ATOM   7857  C  C     . VAL   C 2  120 ? 32.107  8.494   -39.287 1.00 47.50  ? 122 VAL   D C     1 
ATOM   7858  O  O     . VAL   C 2  120 ? 31.389  9.470   -39.014 1.00 46.10  ? 122 VAL   D O     1 
ATOM   7859  C  CB    . VAL   C 2  120 ? 31.799  6.060   -38.573 1.00 48.58  ? 122 VAL   D CB    1 
ATOM   7860  C  CG1   . VAL   C 2  120 ? 31.068  6.322   -37.246 1.00 39.94  ? 122 VAL   D CG1   1 
ATOM   7861  C  CG2   . VAL   C 2  120 ? 31.422  4.681   -39.089 1.00 41.75  ? 122 VAL   D CG2   1 
ATOM   7862  N  N     . ARG   C 2  121 ? 33.442  8.598   -39.376 1.00 46.09  ? 123 ARG   D N     1 
ATOM   7863  C  CA    . ARG   C 2  121 ? 34.135  9.856   -39.075 1.00 38.54  ? 123 ARG   D CA    1 
ATOM   7864  C  C     . ARG   C 2  121 ? 33.550  11.033  -39.851 1.00 44.05  ? 123 ARG   D C     1 
ATOM   7865  O  O     . ARG   C 2  121 ? 33.177  12.056  -39.265 1.00 45.51  ? 123 ARG   D O     1 
ATOM   7866  C  CB    . ARG   C 2  121 ? 35.632  9.742   -39.377 1.00 43.11  ? 123 ARG   D CB    1 
ATOM   7867  C  CG    . ARG   C 2  121 ? 36.427  8.787   -38.500 1.00 43.77  ? 123 ARG   D CG    1 
ATOM   7868  C  CD    . ARG   C 2  121 ? 37.872  8.639   -39.010 1.00 40.42  ? 123 ARG   D CD    1 
ATOM   7869  N  NE    . ARG   C 2  121 ? 38.637  7.676   -38.221 1.00 42.45  ? 123 ARG   D NE    1 
ATOM   7870  C  CZ    . ARG   C 2  121 ? 39.127  6.525   -38.674 1.00 47.39  ? 123 ARG   D CZ    1 
ATOM   7871  N  NH1   . ARG   C 2  121 ? 39.001  6.166   -39.946 1.00 46.83  ? 123 ARG   D NH1   1 
ATOM   7872  N  NH2   . ARG   C 2  121 ? 39.768  5.714   -37.832 1.00 44.47  ? 123 ARG   D NH2   1 
ATOM   7873  N  N     . LYS   C 2  122 ? 33.478  10.919  -41.181 1.00 49.50  ? 124 LYS   D N     1 
ATOM   7874  C  CA    . LYS   C 2  122 ? 32.919  12.014  -41.975 1.00 52.82  ? 124 LYS   D CA    1 
ATOM   7875  C  C     . LYS   C 2  122 ? 31.548  12.426  -41.448 1.00 51.26  ? 124 LYS   D C     1 
ATOM   7876  O  O     . LYS   C 2  122 ? 31.138  13.586  -41.585 1.00 55.35  ? 124 LYS   D O     1 
ATOM   7877  C  CB    . LYS   C 2  122 ? 32.837  11.604  -43.454 1.00 47.14  ? 124 LYS   D CB    1 
ATOM   7878  C  CG    . LYS   C 2  122 ? 32.477  12.723  -44.419 1.00 45.45  ? 124 LYS   D CG    1 
ATOM   7879  C  CD    . LYS   C 2  122 ? 33.547  13.809  -44.430 1.00 60.16  ? 124 LYS   D CD    1 
ATOM   7880  C  CE    . LYS   C 2  122 ? 34.928  13.273  -44.811 1.00 57.85  ? 124 LYS   D CE    1 
ATOM   7881  N  NZ    . LYS   C 2  122 ? 35.867  14.382  -45.194 1.00 50.94  ? 124 LYS   D NZ    1 
ATOM   7882  N  N     . GLU   C 2  123 ? 30.833  11.488  -40.831 1.00 46.30  ? 125 GLU   D N     1 
ATOM   7883  C  CA    . GLU   C 2  123 ? 29.528  11.798  -40.277 1.00 43.91  ? 125 GLU   D CA    1 
ATOM   7884  C  C     . GLU   C 2  123 ? 29.649  12.390  -38.884 1.00 46.18  ? 125 GLU   D C     1 
ATOM   7885  O  O     . GLU   C 2  123 ? 28.996  13.393  -38.578 1.00 49.99  ? 125 GLU   D O     1 
ATOM   7886  C  CB    . GLU   C 2  123 ? 28.671  10.547  -40.277 1.00 34.33  ? 125 GLU   D CB    1 
ATOM   7887  C  CG    . GLU   C 2  123 ? 28.110  10.232  -41.630 1.00 36.73  ? 125 GLU   D CG    1 
ATOM   7888  C  CD    . GLU   C 2  123 ? 26.948  11.119  -41.991 1.00 40.59  ? 125 GLU   D CD    1 
ATOM   7889  O  OE1   . GLU   C 2  123 ? 26.638  12.029  -41.198 1.00 37.39  ? 125 GLU   D OE1   1 
ATOM   7890  O  OE2   . GLU   C 2  123 ? 26.340  10.897  -43.065 1.00 51.26  ? 125 GLU   D OE2   1 
ATOM   7891  N  N     . SER   C 2  124 ? 30.496  11.805  -38.039 1.00 38.12  ? 126 SER   D N     1 
ATOM   7892  C  CA    . SER   C 2  124 ? 30.728  12.387  -36.718 1.00 42.17  ? 126 SER   D CA    1 
ATOM   7893  C  C     . SER   C 2  124 ? 31.303  13.797  -36.820 1.00 49.64  ? 126 SER   D C     1 
ATOM   7894  O  O     . SER   C 2  124 ? 30.948  14.676  -36.026 1.00 47.97  ? 126 SER   D O     1 
ATOM   7895  C  CB    . SER   C 2  124 ? 31.662  11.496  -35.899 1.00 36.10  ? 126 SER   D CB    1 
ATOM   7896  O  OG    . SER   C 2  124 ? 31.135  10.192  -35.740 1.00 26.58  ? 126 SER   D OG    1 
ATOM   7897  N  N     . GLU   C 2  125 ? 32.181  14.042  -37.801 1.00 52.15  ? 127 GLU   D N     1 
ATOM   7898  C  CA    . GLU   C 2  125 ? 32.947  15.286  -37.836 1.00 54.29  ? 127 GLU   D CA    1 
ATOM   7899  C  C     . GLU   C 2  125 ? 32.116  16.502  -38.227 1.00 48.99  ? 127 GLU   D C     1 
ATOM   7900  O  O     . GLU   C 2  125 ? 32.627  17.622  -38.161 1.00 59.99  ? 127 GLU   D O     1 
ATOM   7901  C  CB    . GLU   C 2  125 ? 34.133  15.149  -38.795 1.00 62.23  ? 127 GLU   D CB    1 
ATOM   7902  C  CG    . GLU   C 2  125 ? 33.739  15.125  -40.284 1.00 73.03  ? 127 GLU   D CG    1 
ATOM   7903  C  CD    . GLU   C 2  125 ? 34.944  15.088  -41.235 1.00 75.19  ? 127 GLU   D CD    1 
ATOM   7904  O  OE1   . GLU   C 2  125 ? 35.807  14.184  -41.101 1.00 75.84  ? 127 GLU   D OE1   1 
ATOM   7905  O  OE2   . GLU   C 2  125 ? 35.022  15.971  -42.117 1.00 67.50  ? 127 GLU   D OE2   1 
ATOM   7906  N  N     . SER   C 2  126 ? 30.868  16.324  -38.639 1.00 51.19  ? 128 SER   D N     1 
ATOM   7907  C  CA    . SER   C 2  126 ? 29.985  17.441  -38.949 1.00 52.62  ? 128 SER   D CA    1 
ATOM   7908  C  C     . SER   C 2  126 ? 28.894  17.603  -37.903 1.00 58.52  ? 128 SER   D C     1 
ATOM   7909  O  O     . SER   C 2  126 ? 27.949  18.370  -38.114 1.00 60.51  ? 128 SER   D O     1 
ATOM   7910  C  CB    . SER   C 2  126 ? 29.360  17.250  -40.334 1.00 55.00  ? 128 SER   D CB    1 
ATOM   7911  O  OG    . SER   C 2  126 ? 29.681  15.966  -40.860 1.00 57.30  ? 128 SER   D OG    1 
ATOM   7912  N  N     . CYS   C 2  127 ? 28.987  16.878  -36.793 1.00 52.50  ? 129 CYS   D N     1 
ATOM   7913  C  CA    . CYS   C 2  127 ? 27.922  16.841  -35.807 1.00 45.13  ? 129 CYS   D CA    1 
ATOM   7914  C  C     . CYS   C 2  127 ? 28.081  17.989  -34.825 1.00 47.28  ? 129 CYS   D C     1 
ATOM   7915  O  O     . CYS   C 2  127 ? 29.149  18.163  -34.231 1.00 48.91  ? 129 CYS   D O     1 
ATOM   7916  C  CB    . CYS   C 2  127 ? 27.926  15.508  -35.058 1.00 43.96  ? 129 CYS   D CB    1 
ATOM   7917  S  SG    . CYS   C 2  127 ? 27.061  14.190  -35.883 1.00 42.01  ? 129 CYS   D SG    1 
ATOM   7918  N  N     . ASP   C 2  128 ? 27.009  18.763  -34.656 1.00 50.98  ? 130 ASP   D N     1 
ATOM   7919  C  CA    . ASP   C 2  128 ? 26.946  19.769  -33.600 1.00 41.10  ? 130 ASP   D CA    1 
ATOM   7920  C  C     . ASP   C 2  128 ? 27.343  19.166  -32.259 1.00 42.54  ? 130 ASP   D C     1 
ATOM   7921  O  O     . ASP   C 2  128 ? 28.314  19.599  -31.635 1.00 37.85  ? 130 ASP   D O     1 
ATOM   7922  C  CB    . ASP   C 2  128 ? 25.530  20.360  -33.545 1.00 45.14  ? 130 ASP   D CB    1 
ATOM   7923  C  CG    . ASP   C 2  128 ? 25.361  21.397  -32.449 1.00 59.98  ? 130 ASP   D CG    1 
ATOM   7924  O  OD1   . ASP   C 2  128 ? 26.365  21.726  -31.777 1.00 61.42  ? 130 ASP   D OD1   1 
ATOM   7925  O  OD2   . ASP   C 2  128 ? 24.215  21.881  -32.258 1.00 55.03  ? 130 ASP   D OD2   1 
ATOM   7926  N  N     . CYS   C 2  129 ? 26.604  18.128  -31.812 1.00 48.49  ? 131 CYS   D N     1 
ATOM   7927  C  CA    . CYS   C 2  129 ? 26.769  17.494  -30.490 1.00 45.23  ? 131 CYS   D CA    1 
ATOM   7928  C  C     . CYS   C 2  129 ? 26.431  16.005  -30.620 1.00 44.65  ? 131 CYS   D C     1 
ATOM   7929  O  O     . CYS   C 2  129 ? 25.338  15.550  -30.261 1.00 47.01  ? 131 CYS   D O     1 
ATOM   7930  C  CB    . CYS   C 2  129 ? 25.897  18.160  -29.425 1.00 46.58  ? 131 CYS   D CB    1 
ATOM   7931  S  SG    . CYS   C 2  129 ? 25.937  17.400  -27.778 1.00 57.58  ? 131 CYS   D SG    1 
ATOM   7932  N  N     . LEU   C 2  130 ? 27.398  15.234  -31.121 1.00 40.35  ? 132 LEU   D N     1 
ATOM   7933  C  CA    . LEU   C 2  130 ? 27.160  13.813  -31.347 1.00 40.81  ? 132 LEU   D CA    1 
ATOM   7934  C  C     . LEU   C 2  130 ? 26.697  13.114  -30.076 1.00 45.53  ? 132 LEU   D C     1 
ATOM   7935  O  O     . LEU   C 2  130 ? 27.462  12.955  -29.120 1.00 48.31  ? 132 LEU   D O     1 
ATOM   7936  C  CB    . LEU   C 2  130 ? 28.410  13.125  -31.893 1.00 38.37  ? 132 LEU   D CB    1 
ATOM   7937  C  CG    . LEU   C 2  130 ? 28.305  11.601  -31.992 1.00 34.20  ? 132 LEU   D CG    1 
ATOM   7938  C  CD1   . LEU   C 2  130 ? 27.279  11.200  -33.034 1.00 45.15  ? 132 LEU   D CD1   1 
ATOM   7939  C  CD2   . LEU   C 2  130 ? 29.644  11.006  -32.307 1.00 31.25  ? 132 LEU   D CD2   1 
ATOM   7940  N  N     . GLN   C 2  131 ? 25.432  12.718  -30.055 1.00 45.46  ? 133 GLN   D N     1 
ATOM   7941  C  CA    . GLN   C 2  131 ? 24.911  11.861  -29.006 1.00 38.73  ? 133 GLN   D CA    1 
ATOM   7942  C  C     . GLN   C 2  131 ? 25.733  10.586  -28.884 1.00 41.52  ? 133 GLN   D C     1 
ATOM   7943  O  O     . GLN   C 2  131 ? 26.611  10.477  -28.027 1.00 52.33  ? 133 GLN   D O     1 
ATOM   7944  C  CB    . GLN   C 2  131 ? 23.466  11.521  -29.320 1.00 38.90  ? 133 GLN   D CB    1 
ATOM   7945  C  CG    . GLN   C 2  131 ? 22.519  11.811  -28.221 1.00 40.61  ? 133 GLN   D CG    1 
ATOM   7946  C  CD    . GLN   C 2  131 ? 21.164  11.352  -28.590 1.00 31.45  ? 133 GLN   D CD    1 
ATOM   7947  O  OE1   . GLN   C 2  131 ? 20.561  11.878  -29.514 1.00 35.99  ? 133 GLN   D OE1   1 
ATOM   7948  N  NE2   . GLN   C 2  131 ? 20.689  10.328  -27.919 1.00 29.36  ? 133 GLN   D NE2   1 
ATOM   7949  N  N     . GLY   C 2  132 ? 25.460  9.614   -29.741 1.00 38.75  ? 134 GLY   D N     1 
ATOM   7950  C  CA    . GLY   C 2  132 ? 26.202  8.373   -29.735 1.00 35.33  ? 134 GLY   D CA    1 
ATOM   7951  C  C     . GLY   C 2  132 ? 25.943  7.600   -31.012 1.00 41.27  ? 134 GLY   D C     1 
ATOM   7952  O  O     . GLY   C 2  132 ? 25.685  8.209   -32.056 1.00 37.82  ? 134 GLY   D O     1 
ATOM   7953  N  N     . PHE   C 2  133 ? 25.974  6.260   -30.931 1.00 40.66  ? 135 PHE   D N     1 
ATOM   7954  C  CA    . PHE   C 2  133 ? 25.913  5.373   -32.089 1.00 38.93  ? 135 PHE   D CA    1 
ATOM   7955  C  C     . PHE   C 2  133 ? 24.817  4.331   -31.910 1.00 37.02  ? 135 PHE   D C     1 
ATOM   7956  O  O     . PHE   C 2  133 ? 24.492  3.945   -30.783 1.00 30.08  ? 135 PHE   D O     1 
ATOM   7957  C  CB    . PHE   C 2  133 ? 27.270  4.691   -32.316 1.00 33.25  ? 135 PHE   D CB    1 
ATOM   7958  C  CG    . PHE   C 2  133 ? 28.366  5.655   -32.644 1.00 38.42  ? 135 PHE   D CG    1 
ATOM   7959  C  CD1   . PHE   C 2  133 ? 28.614  6.025   -33.951 1.00 39.11  ? 135 PHE   D CD1   1 
ATOM   7960  C  CD2   . PHE   C 2  133 ? 29.122  6.226   -31.643 1.00 35.44  ? 135 PHE   D CD2   1 
ATOM   7961  C  CE1   . PHE   C 2  133 ? 29.609  6.922   -34.255 1.00 37.54  ? 135 PHE   D CE1   1 
ATOM   7962  C  CE2   . PHE   C 2  133 ? 30.118  7.127   -31.949 1.00 38.33  ? 135 PHE   D CE2   1 
ATOM   7963  C  CZ    . PHE   C 2  133 ? 30.360  7.474   -33.251 1.00 33.70  ? 135 PHE   D CZ    1 
ATOM   7964  N  N     . GLN   C 2  134 ? 24.286  3.846   -33.046 1.00 35.39  ? 136 GLN   D N     1 
ATOM   7965  C  CA    . GLN   C 2  134 ? 23.063  3.037   -33.105 1.00 27.66  ? 136 GLN   D CA    1 
ATOM   7966  C  C     . GLN   C 2  134 ? 23.254  1.944   -34.156 1.00 34.30  ? 136 GLN   D C     1 
ATOM   7967  O  O     . GLN   C 2  134 ? 23.164  2.212   -35.356 1.00 46.83  ? 136 GLN   D O     1 
ATOM   7968  C  CB    . GLN   C 2  134 ? 21.869  3.922   -33.448 1.00 27.82  ? 136 GLN   D CB    1 
ATOM   7969  C  CG    . GLN   C 2  134 ? 20.501  3.271   -33.345 1.00 31.90  ? 136 GLN   D CG    1 
ATOM   7970  C  CD    . GLN   C 2  134 ? 19.358  4.210   -33.741 1.00 41.55  ? 136 GLN   D CD    1 
ATOM   7971  O  OE1   . GLN   C 2  134 ? 19.116  4.438   -34.925 1.00 45.23  ? 136 GLN   D OE1   1 
ATOM   7972  N  NE2   . GLN   C 2  134 ? 18.647  4.748   -32.749 1.00 35.63  ? 136 GLN   D NE2   1 
ATOM   7973  N  N     . LEU   C 2  135 ? 23.469  0.706   -33.719 1.00 35.32  ? 137 LEU   D N     1 
ATOM   7974  C  CA    . LEU   C 2  135 ? 23.801  -0.397  -34.614 1.00 33.06  ? 137 LEU   D CA    1 
ATOM   7975  C  C     . LEU   C 2  135 ? 22.676  -1.424  -34.676 1.00 43.52  ? 137 LEU   D C     1 
ATOM   7976  O  O     . LEU   C 2  135 ? 22.224  -1.917  -33.637 1.00 47.40  ? 137 LEU   D O     1 
ATOM   7977  C  CB    . LEU   C 2  135 ? 25.083  -1.080  -34.147 1.00 34.46  ? 137 LEU   D CB    1 
ATOM   7978  C  CG    . LEU   C 2  135 ? 25.189  -2.516  -34.641 1.00 41.61  ? 137 LEU   D CG    1 
ATOM   7979  C  CD1   . LEU   C 2  135 ? 25.329  -2.496  -36.167 1.00 46.73  ? 137 LEU   D CD1   1 
ATOM   7980  C  CD2   . LEU   C 2  135 ? 26.350  -3.256  -33.982 1.00 34.35  ? 137 LEU   D CD2   1 
ATOM   7981  N  N     . THR   C 2  136 ? 22.239  -1.758  -35.895 1.00 52.82  ? 138 THR   D N     1 
ATOM   7982  C  CA    . THR   C 2  136 ? 21.348  -2.889  -36.149 1.00 42.42  ? 138 THR   D CA    1 
ATOM   7983  C  C     . THR   C 2  136 ? 22.167  -4.024  -36.738 1.00 38.60  ? 138 THR   D C     1 
ATOM   7984  O  O     . THR   C 2  136 ? 23.014  -3.797  -37.603 1.00 37.79  ? 138 THR   D O     1 
ATOM   7985  C  CB    . THR   C 2  136 ? 20.233  -2.531  -37.138 1.00 45.08  ? 138 THR   D CB    1 
ATOM   7986  O  OG1   . THR   C 2  136 ? 20.823  -2.070  -38.358 1.00 44.15  ? 138 THR   D OG1   1 
ATOM   7987  C  CG2   . THR   C 2  136 ? 19.313  -1.455  -36.598 1.00 43.23  ? 138 THR   D CG2   1 
ATOM   7988  N  N     . HIS   C 2  137 ? 21.901  -5.245  -36.291 1.00 46.04  ? 139 HIS   D N     1 
ATOM   7989  C  CA    . HIS   C 2  137 ? 22.677  -6.389  -36.769 1.00 51.40  ? 139 HIS   D CA    1 
ATOM   7990  C  C     . HIS   C 2  137 ? 22.130  -7.643  -36.106 1.00 48.65  ? 139 HIS   D C     1 
ATOM   7991  O  O     . HIS   C 2  137 ? 21.539  -7.577  -35.025 1.00 51.30  ? 139 HIS   D O     1 
ATOM   7992  C  CB    . HIS   C 2  137 ? 24.166  -6.241  -36.448 1.00 41.39  ? 139 HIS   D CB    1 
ATOM   7993  C  CG    . HIS   C 2  137 ? 24.467  -6.301  -34.985 1.00 37.92  ? 139 HIS   D CG    1 
ATOM   7994  N  ND1   . HIS   C 2  137 ? 25.619  -6.867  -34.486 1.00 47.95  ? 139 HIS   D ND1   1 
ATOM   7995  C  CD2   . HIS   C 2  137 ? 23.764  -5.871  -33.913 1.00 38.19  ? 139 HIS   D CD2   1 
ATOM   7996  C  CE1   . HIS   C 2  137 ? 25.608  -6.796  -33.166 1.00 42.08  ? 139 HIS   D CE1   1 
ATOM   7997  N  NE2   . HIS   C 2  137 ? 24.491  -6.198  -32.793 1.00 42.30  ? 139 HIS   D NE2   1 
ATOM   7998  N  N     . SER   C 2  138 ? 22.333  -8.783  -36.749 1.00 36.57  ? 140 SER   D N     1 
ATOM   7999  C  CA    . SER   C 2  138 ? 21.941  -10.028 -36.114 1.00 38.88  ? 140 SER   D CA    1 
ATOM   8000  C  C     . SER   C 2  138 ? 23.156  -10.634 -35.439 1.00 41.14  ? 140 SER   D C     1 
ATOM   8001  O  O     . SER   C 2  138 ? 24.292  -10.244 -35.705 1.00 45.87  ? 140 SER   D O     1 
ATOM   8002  C  CB    . SER   C 2  138 ? 21.329  -11.014 -37.112 1.00 47.16  ? 140 SER   D CB    1 
ATOM   8003  O  OG    . SER   C 2  138 ? 22.330  -11.705 -37.842 1.00 63.61  ? 140 SER   D OG    1 
ATOM   8004  N  N     . LEU   C 2  139 ? 22.902  -11.584 -34.537 1.00 43.03  ? 141 LEU   D N     1 
ATOM   8005  C  CA    . LEU   C 2  139 ? 23.958  -12.197 -33.749 1.00 43.77  ? 141 LEU   D CA    1 
ATOM   8006  C  C     . LEU   C 2  139 ? 24.262  -13.625 -34.157 1.00 47.51  ? 141 LEU   D C     1 
ATOM   8007  O  O     . LEU   C 2  139 ? 25.181  -14.224 -33.586 1.00 50.34  ? 141 LEU   D O     1 
ATOM   8008  C  CB    . LEU   C 2  139 ? 23.607  -12.183 -32.252 1.00 45.84  ? 141 LEU   D CB    1 
ATOM   8009  C  CG    . LEU   C 2  139 ? 23.273  -10.865 -31.558 1.00 40.77  ? 141 LEU   D CG    1 
ATOM   8010  C  CD1   . LEU   C 2  139 ? 23.272  -11.050 -30.046 1.00 44.07  ? 141 LEU   D CD1   1 
ATOM   8011  C  CD2   . LEU   C 2  139 ? 24.254  -9.784  -31.982 1.00 41.20  ? 141 LEU   D CD2   1 
ATOM   8012  N  N     . GLY   C 2  140 ? 23.512  -14.192 -35.100 1.00 44.81  ? 142 GLY   D N     1 
ATOM   8013  C  CA    . GLY   C 2  140 ? 23.819  -15.517 -35.620 1.00 57.43  ? 142 GLY   D CA    1 
ATOM   8014  C  C     . GLY   C 2  140 ? 24.349  -15.495 -37.045 1.00 63.51  ? 142 GLY   D C     1 
ATOM   8015  O  O     . GLY   C 2  140 ? 25.191  -16.327 -37.414 1.00 56.49  ? 142 GLY   D O     1 
ATOM   8016  N  N     . GLY   C 2  141 ? 23.850  -14.532 -37.841 1.00 62.85  ? 143 GLY   D N     1 
ATOM   8017  C  CA    . GLY   C 2  141 ? 24.253  -14.265 -39.214 1.00 58.64  ? 143 GLY   D CA    1 
ATOM   8018  C  C     . GLY   C 2  141 ? 25.726  -13.931 -39.399 1.00 65.00  ? 143 GLY   D C     1 
ATOM   8019  O  O     . GLY   C 2  141 ? 26.538  -14.101 -38.478 1.00 50.37  ? 143 GLY   D O     1 
ATOM   8020  N  N     . GLY   C 2  142 ? 26.081  -13.427 -40.586 1.00 66.73  ? 144 GLY   D N     1 
ATOM   8021  C  CA    . GLY   C 2  142 ? 27.469  -13.464 -41.004 1.00 62.31  ? 144 GLY   D CA    1 
ATOM   8022  C  C     . GLY   C 2  142 ? 28.311  -12.256 -40.661 1.00 60.55  ? 144 GLY   D C     1 
ATOM   8023  O  O     . GLY   C 2  142 ? 29.204  -12.307 -39.793 1.00 42.09  ? 144 GLY   D O     1 
ATOM   8024  N  N     . THR   C 2  143 ? 28.038  -11.160 -41.371 1.00 59.73  ? 145 THR   D N     1 
ATOM   8025  C  CA    . THR   C 2  143 ? 28.855  -9.965  -41.205 1.00 51.52  ? 145 THR   D CA    1 
ATOM   8026  C  C     . THR   C 2  143 ? 28.511  -9.251  -39.909 1.00 55.16  ? 145 THR   D C     1 
ATOM   8027  O  O     . THR   C 2  143 ? 29.393  -9.004  -39.077 1.00 57.94  ? 145 THR   D O     1 
ATOM   8028  C  CB    . THR   C 2  143 ? 28.677  -9.015  -42.388 1.00 41.83  ? 145 THR   D CB    1 
ATOM   8029  O  OG1   . THR   C 2  143 ? 29.056  -9.669  -43.601 1.00 50.36  ? 145 THR   D OG1   1 
ATOM   8030  C  CG2   . THR   C 2  143 ? 29.555  -7.844  -42.211 1.00 46.01  ? 145 THR   D CG2   1 
ATOM   8031  N  N     . GLY   C 2  144 ? 27.220  -8.930  -39.716 1.00 57.76  ? 146 GLY   D N     1 
ATOM   8032  C  CA    . GLY   C 2  144 ? 26.804  -8.115  -38.577 1.00 50.06  ? 146 GLY   D CA    1 
ATOM   8033  C  C     . GLY   C 2  144 ? 27.180  -8.687  -37.220 1.00 50.77  ? 146 GLY   D C     1 
ATOM   8034  O  O     . GLY   C 2  144 ? 27.416  -7.935  -36.268 1.00 44.28  ? 146 GLY   D O     1 
ATOM   8035  N  N     . SER   C 2  145 ? 27.229  -10.016 -37.103 1.00 49.04  ? 147 SER   D N     1 
ATOM   8036  C  CA    . SER   C 2  145 ? 27.664  -10.616 -35.849 1.00 43.00  ? 147 SER   D CA    1 
ATOM   8037  C  C     . SER   C 2  145 ? 29.141  -10.344 -35.583 1.00 41.06  ? 147 SER   D C     1 
ATOM   8038  O  O     . SER   C 2  145 ? 29.549  -10.189 -34.431 1.00 50.23  ? 147 SER   D O     1 
ATOM   8039  C  CB    . SER   C 2  145 ? 27.392  -12.119 -35.863 1.00 52.93  ? 147 SER   D CB    1 
ATOM   8040  O  OG    . SER   C 2  145 ? 27.686  -12.690 -34.596 1.00 52.97  ? 147 SER   D OG    1 
ATOM   8041  N  N     . GLY   C 2  146 ? 29.957  -10.273 -36.625 1.00 53.04  ? 148 GLY   D N     1 
ATOM   8042  C  CA    . GLY   C 2  146 ? 31.395  -10.167 -36.432 1.00 56.05  ? 148 GLY   D CA    1 
ATOM   8043  C  C     . GLY   C 2  146 ? 31.983  -8.797  -36.716 1.00 52.62  ? 148 GLY   D C     1 
ATOM   8044  O  O     . GLY   C 2  146 ? 32.795  -8.280  -35.937 1.00 47.35  ? 148 GLY   D O     1 
ATOM   8045  N  N     . MET   C 2  147 ? 31.594  -8.208  -37.846 1.00 45.34  ? 149 MET   D N     1 
ATOM   8046  C  CA    . MET   C 2  147 ? 32.040  -6.857  -38.159 1.00 51.40  ? 149 MET   D CA    1 
ATOM   8047  C  C     . MET   C 2  147 ? 31.357  -5.823  -37.263 1.00 51.92  ? 149 MET   D C     1 
ATOM   8048  O  O     . MET   C 2  147 ? 31.950  -4.774  -36.954 1.00 43.41  ? 149 MET   D O     1 
ATOM   8049  C  CB    . MET   C 2  147 ? 31.766  -6.558  -39.636 1.00 51.43  ? 149 MET   D CB    1 
ATOM   8050  C  CG    . MET   C 2  147 ? 32.988  -6.414  -40.527 1.00 43.62  ? 149 MET   D CG    1 
ATOM   8051  S  SD    . MET   C 2  147 ? 32.557  -5.486  -42.003 1.00 54.51  ? 149 MET   D SD    1 
ATOM   8052  C  CE    . MET   C 2  147 ? 32.707  -3.807  -41.426 1.00 39.04  ? 149 MET   D CE    1 
ATOM   8053  N  N     . GLY   C 2  148 ? 30.110  -6.094  -36.857 1.00 49.22  ? 150 GLY   D N     1 
ATOM   8054  C  CA    . GLY   C 2  148 ? 29.411  -5.175  -35.980 1.00 42.17  ? 150 GLY   D CA    1 
ATOM   8055  C  C     . GLY   C 2  148 ? 30.039  -5.127  -34.603 1.00 41.74  ? 150 GLY   D C     1 
ATOM   8056  O  O     . GLY   C 2  148 ? 30.241  -4.049  -34.041 1.00 36.12  ? 150 GLY   D O     1 
ATOM   8057  N  N     . THR   C 2  149 ? 30.376  -6.290  -34.048 1.00 41.19  ? 151 THR   D N     1 
ATOM   8058  C  CA    . THR   C 2  149 ? 31.078  -6.287  -32.773 1.00 41.50  ? 151 THR   D CA    1 
ATOM   8059  C  C     . THR   C 2  149 ? 32.493  -5.740  -32.927 1.00 43.62  ? 151 THR   D C     1 
ATOM   8060  O  O     . THR   C 2  149 ? 33.050  -5.180  -31.974 1.00 47.36  ? 151 THR   D O     1 
ATOM   8061  C  CB    . THR   C 2  149 ? 31.075  -7.693  -32.172 1.00 44.94  ? 151 THR   D CB    1 
ATOM   8062  O  OG1   . THR   C 2  149 ? 31.211  -8.658  -33.219 1.00 51.94  ? 151 THR   D OG1   1 
ATOM   8063  C  CG2   . THR   C 2  149 ? 29.761  -7.944  -31.439 1.00 41.99  ? 151 THR   D CG2   1 
ATOM   8064  N  N     . LEU   C 2  150 ? 33.071  -5.857  -34.125 1.00 44.73  ? 152 LEU   D N     1 
ATOM   8065  C  CA    . LEU   C 2  150 ? 34.340  -5.193  -34.411 1.00 47.88  ? 152 LEU   D CA    1 
ATOM   8066  C  C     . LEU   C 2  150 ? 34.168  -3.683  -34.499 1.00 40.58  ? 152 LEU   D C     1 
ATOM   8067  O  O     . LEU   C 2  150 ? 34.896  -2.929  -33.850 1.00 45.79  ? 152 LEU   D O     1 
ATOM   8068  C  CB    . LEU   C 2  150 ? 34.943  -5.729  -35.710 1.00 55.80  ? 152 LEU   D CB    1 
ATOM   8069  C  CG    . LEU   C 2  150 ? 36.417  -5.391  -35.958 1.00 51.75  ? 152 LEU   D CG    1 
ATOM   8070  C  CD1   . LEU   C 2  150 ? 37.289  -6.015  -34.858 1.00 41.28  ? 152 LEU   D CD1   1 
ATOM   8071  C  CD2   . LEU   C 2  150 ? 36.824  -5.896  -37.336 1.00 49.93  ? 152 LEU   D CD2   1 
ATOM   8072  N  N     . LEU   C 2  151 ? 33.227  -3.217  -35.315 1.00 39.26  ? 153 LEU   D N     1 
ATOM   8073  C  CA    . LEU   C 2  151 ? 32.982  -1.781  -35.377 1.00 41.44  ? 153 LEU   D CA    1 
ATOM   8074  C  C     . LEU   C 2  151 ? 32.775  -1.189  -33.989 1.00 41.02  ? 153 LEU   D C     1 
ATOM   8075  O  O     . LEU   C 2  151 ? 33.252  -0.083  -33.701 1.00 38.62  ? 153 LEU   D O     1 
ATOM   8076  C  CB    . LEU   C 2  151 ? 31.776  -1.500  -36.262 1.00 35.11  ? 153 LEU   D CB    1 
ATOM   8077  C  CG    . LEU   C 2  151 ? 32.096  -1.862  -37.692 1.00 36.47  ? 153 LEU   D CG    1 
ATOM   8078  C  CD1   . LEU   C 2  151 ? 30.825  -2.126  -38.451 1.00 49.24  ? 153 LEU   D CD1   1 
ATOM   8079  C  CD2   . LEU   C 2  151 ? 32.843  -0.693  -38.289 1.00 43.29  ? 153 LEU   D CD2   1 
ATOM   8080  N  N     . ILE   C 2  152 ? 32.071  -1.913  -33.110 1.00 41.19  ? 154 ILE   D N     1 
ATOM   8081  C  CA    . ILE   C 2  152 ? 31.783  -1.391  -31.774 1.00 35.66  ? 154 ILE   D CA    1 
ATOM   8082  C  C     . ILE   C 2  152 ? 33.076  -1.139  -31.015 1.00 35.74  ? 154 ILE   D C     1 
ATOM   8083  O  O     . ILE   C 2  152 ? 33.305  -0.041  -30.503 1.00 41.70  ? 154 ILE   D O     1 
ATOM   8084  C  CB    . ILE   C 2  152 ? 30.846  -2.338  -31.005 1.00 36.07  ? 154 ILE   D CB    1 
ATOM   8085  C  CG1   . ILE   C 2  152 ? 29.420  -2.215  -31.534 1.00 34.85  ? 154 ILE   D CG1   1 
ATOM   8086  C  CG2   . ILE   C 2  152 ? 30.844  -1.990  -29.538 1.00 41.72  ? 154 ILE   D CG2   1 
ATOM   8087  C  CD1   . ILE   C 2  152 ? 28.595  -3.462  -31.342 1.00 33.33  ? 154 ILE   D CD1   1 
ATOM   8088  N  N     . SER   C 2  153 ? 33.945  -2.148  -30.934 1.00 35.66  ? 155 SER   D N     1 
ATOM   8089  C  CA    A SER   C 2  153 ? 35.236  -1.936  -30.296 0.62 34.75  ? 155 SER   D CA    1 
ATOM   8090  C  CA    B SER   C 2  153 ? 35.242  -1.940  -30.300 0.38 34.84  ? 155 SER   D CA    1 
ATOM   8091  C  C     . SER   C 2  153 ? 36.042  -0.854  -31.008 1.00 35.66  ? 155 SER   D C     1 
ATOM   8092  O  O     . SER   C 2  153 ? 36.778  -0.098  -30.364 1.00 40.11  ? 155 SER   D O     1 
ATOM   8093  C  CB    A SER   C 2  153 ? 35.997  -3.254  -30.245 0.62 38.37  ? 155 SER   D CB    1 
ATOM   8094  C  CB    B SER   C 2  153 ? 36.032  -3.241  -30.284 0.38 38.39  ? 155 SER   D CB    1 
ATOM   8095  O  OG    A SER   C 2  153 ? 35.268  -4.215  -29.490 0.62 41.87  ? 155 SER   D OG    1 
ATOM   8096  O  OG    B SER   C 2  153 ? 36.446  -3.577  -31.595 0.38 39.22  ? 155 SER   D OG    1 
ATOM   8097  N  N     . LYS   C 2  154 ? 35.914  -0.752  -32.322 1.00 36.06  ? 156 LYS   D N     1 
ATOM   8098  C  CA    . LYS   C 2  154 ? 36.655  0.280   -33.028 1.00 37.87  ? 156 LYS   D CA    1 
ATOM   8099  C  C     . LYS   C 2  154 ? 36.067  1.657   -32.771 1.00 36.51  ? 156 LYS   D C     1 
ATOM   8100  O  O     . LYS   C 2  154 ? 36.809  2.632   -32.633 1.00 43.63  ? 156 LYS   D O     1 
ATOM   8101  C  CB    . LYS   C 2  154 ? 36.695  -0.023  -34.526 1.00 41.60  ? 156 LYS   D CB    1 
ATOM   8102  C  CG    . LYS   C 2  154 ? 38.003  -0.655  -34.968 1.00 35.86  ? 156 LYS   D CG    1 
ATOM   8103  C  CD    . LYS   C 2  154 ? 38.430  -1.677  -33.935 1.00 40.80  ? 156 LYS   D CD    1 
ATOM   8104  C  CE    . LYS   C 2  154 ? 39.796  -2.259  -34.242 1.00 44.27  ? 156 LYS   D CE    1 
ATOM   8105  N  NZ    . LYS   C 2  154 ? 40.872  -1.235  -34.244 1.00 43.16  ? 156 LYS   D NZ    1 
ATOM   8106  N  N     . ILE   C 2  155 ? 34.743  1.772   -32.719 1.00 38.85  ? 157 ILE   D N     1 
ATOM   8107  C  CA    . ILE   C 2  155 ? 34.141  3.085   -32.480 1.00 42.02  ? 157 ILE   D CA    1 
ATOM   8108  C  C     . ILE   C 2  155 ? 34.343  3.515   -31.027 1.00 38.68  ? 157 ILE   D C     1 
ATOM   8109  O  O     . ILE   C 2  155 ? 34.677  4.669   -30.746 1.00 32.04  ? 157 ILE   D O     1 
ATOM   8110  C  CB    . ILE   C 2  155 ? 32.657  3.060   -32.887 1.00 33.71  ? 157 ILE   D CB    1 
ATOM   8111  C  CG1   . ILE   C 2  155 ? 32.546  2.773   -34.391 1.00 28.65  ? 157 ILE   D CG1   1 
ATOM   8112  C  CG2   . ILE   C 2  155 ? 31.975  4.351   -32.519 1.00 30.75  ? 157 ILE   D CG2   1 
ATOM   8113  C  CD1   . ILE   C 2  155 ? 31.186  3.101   -34.994 1.00 39.92  ? 157 ILE   D CD1   1 
ATOM   8114  N  N     . ARG   C 2  156 ? 34.177  2.587   -30.089 1.00 40.03  ? 158 ARG   D N     1 
ATOM   8115  C  CA    . ARG   C 2  156 ? 34.488  2.811   -28.689 1.00 38.01  ? 158 ARG   D CA    1 
ATOM   8116  C  C     . ARG   C 2  156 ? 35.980  3.029   -28.434 1.00 46.25  ? 158 ARG   D C     1 
ATOM   8117  O  O     . ARG   C 2  156 ? 36.368  3.205   -27.276 1.00 55.81  ? 158 ARG   D O     1 
ATOM   8118  C  CB    . ARG   C 2  156 ? 33.963  1.637   -27.870 1.00 31.14  ? 158 ARG   D CB    1 
ATOM   8119  C  CG    . ARG   C 2  156 ? 33.438  2.034   -26.510 1.00 43.14  ? 158 ARG   D CG    1 
ATOM   8120  C  CD    . ARG   C 2  156 ? 32.878  0.829   -25.801 1.00 47.77  ? 158 ARG   D CD    1 
ATOM   8121  N  NE    . ARG   C 2  156 ? 32.453  1.070   -24.424 1.00 45.98  ? 158 ARG   D NE    1 
ATOM   8122  C  CZ    . ARG   C 2  156 ? 31.401  1.801   -24.071 1.00 42.29  ? 158 ARG   D CZ    1 
ATOM   8123  N  NH1   . ARG   C 2  156 ? 30.774  2.589   -24.941 1.00 24.50  ? 158 ARG   D NH1   1 
ATOM   8124  N  NH2   . ARG   C 2  156 ? 30.963  1.735   -22.817 1.00 39.66  ? 158 ARG   D NH2   1 
ATOM   8125  N  N     . GLU   C 2  157 ? 36.814  3.033   -29.471 1.00 42.42  ? 159 GLU   D N     1 
ATOM   8126  C  CA    . GLU   C 2  157 ? 38.202  3.470   -29.379 1.00 37.25  ? 159 GLU   D CA    1 
ATOM   8127  C  C     . GLU   C 2  157 ? 38.389  4.901   -29.834 1.00 38.57  ? 159 GLU   D C     1 
ATOM   8128  O  O     . GLU   C 2  157 ? 39.365  5.540   -29.444 1.00 42.47  ? 159 GLU   D O     1 
ATOM   8129  C  CB    . GLU   C 2  157 ? 39.106  2.582   -30.242 1.00 43.16  ? 159 GLU   D CB    1 
ATOM   8130  C  CG    . GLU   C 2  157 ? 40.218  1.808   -29.525 1.00 49.91  ? 159 GLU   D CG    1 
ATOM   8131  C  CD    . GLU   C 2  157 ? 41.051  0.978   -30.509 1.00 59.74  ? 159 GLU   D CD    1 
ATOM   8132  O  OE1   . GLU   C 2  157 ? 40.463  0.147   -31.236 1.00 54.95  ? 159 GLU   D OE1   1 
ATOM   8133  O  OE2   . GLU   C 2  157 ? 42.287  1.171   -30.573 1.00 66.42  ? 159 GLU   D OE2   1 
ATOM   8134  N  N     . GLU   C 2  158 ? 37.505  5.401   -30.695 1.00 40.19  ? 160 GLU   D N     1 
ATOM   8135  C  CA    . GLU   C 2  158 ? 37.575  6.775   -31.164 1.00 35.45  ? 160 GLU   D CA    1 
ATOM   8136  C  C     . GLU   C 2  158 ? 36.566  7.671   -30.490 1.00 43.22  ? 160 GLU   D C     1 
ATOM   8137  O  O     . GLU   C 2  158 ? 36.664  8.895   -30.620 1.00 49.69  ? 160 GLU   D O     1 
ATOM   8138  C  CB    . GLU   C 2  158 ? 37.352  6.859   -32.675 1.00 29.67  ? 160 GLU   D CB    1 
ATOM   8139  C  CG    . GLU   C 2  158 ? 38.583  6.541   -33.474 1.00 44.23  ? 160 GLU   D CG    1 
ATOM   8140  C  CD    . GLU   C 2  158 ? 38.420  6.869   -34.941 1.00 54.68  ? 160 GLU   D CD    1 
ATOM   8141  O  OE1   . GLU   C 2  158 ? 37.978  8.007   -35.229 1.00 52.77  ? 160 GLU   D OE1   1 
ATOM   8142  O  OE2   . GLU   C 2  158 ? 38.726  5.992   -35.795 1.00 46.44  ? 160 GLU   D OE2   1 
ATOM   8143  N  N     . TYR   C 2  159 ? 35.587  7.100   -29.816 1.00 48.43  ? 161 TYR   D N     1 
ATOM   8144  C  CA    . TYR   C 2  159 ? 34.561  7.912   -29.187 1.00 43.70  ? 161 TYR   D CA    1 
ATOM   8145  C  C     . TYR   C 2  159 ? 34.226  7.325   -27.834 1.00 37.26  ? 161 TYR   D C     1 
ATOM   8146  O  O     . TYR   C 2  159 ? 33.045  7.173   -27.518 1.00 45.45  ? 161 TYR   D O     1 
ATOM   8147  C  CB    . TYR   C 2  159 ? 33.305  7.972   -30.050 1.00 38.06  ? 161 TYR   D CB    1 
ATOM   8148  C  CG    . TYR   C 2  159 ? 33.562  8.459   -31.452 1.00 39.78  ? 161 TYR   D CG    1 
ATOM   8149  C  CD1   . TYR   C 2  159 ? 33.516  9.811   -31.750 1.00 39.50  ? 161 TYR   D CD1   1 
ATOM   8150  C  CD2   . TYR   C 2  159 ? 33.843  7.570   -32.480 1.00 40.72  ? 161 TYR   D CD2   1 
ATOM   8151  C  CE1   . TYR   C 2  159 ? 33.747  10.272  -33.037 1.00 48.66  ? 161 TYR   D CE1   1 
ATOM   8152  C  CE2   . TYR   C 2  159 ? 34.086  8.026   -33.771 1.00 42.49  ? 161 TYR   D CE2   1 
ATOM   8153  C  CZ    . TYR   C 2  159 ? 34.033  9.378   -34.041 1.00 43.86  ? 161 TYR   D CZ    1 
ATOM   8154  O  OH    . TYR   C 2  159 ? 34.262  9.856   -35.309 1.00 47.03  ? 161 TYR   D OH    1 
ATOM   8155  N  N     . PRO   C 2  160 ? 35.226  7.008   -27.009 1.00 34.62  ? 162 PRO   D N     1 
ATOM   8156  C  CA    . PRO   C 2  160 ? 34.964  6.231   -25.785 1.00 47.26  ? 162 PRO   D CA    1 
ATOM   8157  C  C     . PRO   C 2  160 ? 33.908  6.839   -24.868 1.00 41.88  ? 162 PRO   D C     1 
ATOM   8158  O  O     . PRO   C 2  160 ? 33.400  6.128   -23.994 1.00 42.65  ? 162 PRO   D O     1 
ATOM   8159  C  CB    . PRO   C 2  160 ? 36.334  6.190   -25.101 1.00 43.03  ? 162 PRO   D CB    1 
ATOM   8160  C  CG    . PRO   C 2  160 ? 36.995  7.421   -25.583 1.00 46.73  ? 162 PRO   D CG    1 
ATOM   8161  C  CD    . PRO   C 2  160 ? 36.578  7.574   -27.012 1.00 37.38  ? 162 PRO   D CD    1 
ATOM   8162  N  N     . ASP   C 2  161 ? 33.542  8.103   -25.067 1.00 42.46  ? 163 ASP   D N     1 
ATOM   8163  C  CA    . ASP   C 2  161 ? 32.610  8.818   -24.207 1.00 42.21  ? 163 ASP   D CA    1 
ATOM   8164  C  C     . ASP   C 2  161 ? 31.339  9.247   -24.942 1.00 48.15  ? 163 ASP   D C     1 
ATOM   8165  O  O     . ASP   C 2  161 ? 30.728  10.252  -24.569 1.00 49.49  ? 163 ASP   D O     1 
ATOM   8166  C  CB    . ASP   C 2  161 ? 33.289  10.041  -23.602 1.00 38.80  ? 163 ASP   D CB    1 
ATOM   8167  C  CG    . ASP   C 2  161 ? 33.671  11.075  -24.658 1.00 58.09  ? 163 ASP   D CG    1 
ATOM   8168  O  OD1   . ASP   C 2  161 ? 33.536  10.801  -25.881 1.00 46.36  ? 163 ASP   D OD1   1 
ATOM   8169  O  OD2   . ASP   C 2  161 ? 34.113  12.176  -24.263 1.00 72.05  ? 163 ASP   D OD2   1 
ATOM   8170  N  N     . ARG   C 2  162 ? 30.953  8.529   -26.000 1.00 39.02  ? 164 ARG   D N     1 
ATOM   8171  C  CA    . ARG   C 2  162 ? 29.639  8.636   -26.626 1.00 37.26  ? 164 ARG   D CA    1 
ATOM   8172  C  C     . ARG   C 2  162 ? 28.873  7.345   -26.346 1.00 33.04  ? 164 ARG   D C     1 
ATOM   8173  O  O     . ARG   C 2  162 ? 29.432  6.363   -25.854 1.00 32.85  ? 164 ARG   D O     1 
ATOM   8174  C  CB    . ARG   C 2  162 ? 29.752  8.899   -28.136 1.00 37.18  ? 164 ARG   D CB    1 
ATOM   8175  C  CG    . ARG   C 2  162 ? 30.463  10.185  -28.527 1.00 30.51  ? 164 ARG   D CG    1 
ATOM   8176  C  CD    . ARG   C 2  162 ? 29.625  11.418  -28.204 1.00 46.84  ? 164 ARG   D CD    1 
ATOM   8177  N  NE    . ARG   C 2  162 ? 30.009  12.060  -26.945 1.00 68.43  ? 164 ARG   D NE    1 
ATOM   8178  C  CZ    . ARG   C 2  162 ? 29.169  12.666  -26.106 1.00 63.22  ? 164 ARG   D CZ    1 
ATOM   8179  N  NH1   . ARG   C 2  162 ? 27.861  12.686  -26.332 1.00 58.34  ? 164 ARG   D NH1   1 
ATOM   8180  N  NH2   . ARG   C 2  162 ? 29.654  13.245  -24.998 1.00 56.62  ? 164 ARG   D NH2   1 
ATOM   8181  N  N     . ILE   C 2  163 ? 27.580  7.340   -26.639 1.00 32.87  ? 165 ILE   D N     1 
ATOM   8182  C  CA    . ILE   C 2  163 ? 26.719  6.237   -26.222 1.00 28.63  ? 165 ILE   D CA    1 
ATOM   8183  C  C     . ILE   C 2  163 ? 26.633  5.205   -27.346 1.00 32.17  ? 165 ILE   D C     1 
ATOM   8184  O  O     . ILE   C 2  163 ? 26.252  5.530   -28.476 1.00 36.52  ? 165 ILE   D O     1 
ATOM   8185  C  CB    . ILE   C 2  163 ? 25.332  6.755   -25.819 1.00 28.51  ? 165 ILE   D CB    1 
ATOM   8186  C  CG1   . ILE   C 2  163 ? 25.404  7.449   -24.457 1.00 26.77  ? 165 ILE   D CG1   1 
ATOM   8187  C  CG2   . ILE   C 2  163 ? 24.315  5.639   -25.816 1.00 28.66  ? 165 ILE   D CG2   1 
ATOM   8188  C  CD1   . ILE   C 2  163 ? 25.714  6.536   -23.327 1.00 21.39  ? 165 ILE   D CD1   1 
ATOM   8189  N  N     . MET   C 2  164 ? 26.992  3.955   -27.036 1.00 28.86  ? 166 MET   D N     1 
ATOM   8190  C  CA    . MET   C 2  164 ? 27.012  2.852   -27.996 1.00 27.17  ? 166 MET   D CA    1 
ATOM   8191  C  C     . MET   C 2  164 ? 25.721  2.056   -27.848 1.00 33.67  ? 166 MET   D C     1 
ATOM   8192  O  O     . MET   C 2  164 ? 25.540  1.328   -26.865 1.00 38.78  ? 166 MET   D O     1 
ATOM   8193  C  CB    . MET   C 2  164 ? 28.237  1.965   -27.761 1.00 37.02  ? 166 MET   D CB    1 
ATOM   8194  C  CG    . MET   C 2  164 ? 28.444  0.828   -28.770 1.00 33.32  ? 166 MET   D CG    1 
ATOM   8195  S  SD    . MET   C 2  164 ? 28.409  1.454   -30.461 1.00 42.35  ? 166 MET   D SD    1 
ATOM   8196  C  CE    . MET   C 2  164 ? 29.903  2.454   -30.553 1.00 29.13  ? 166 MET   D CE    1 
ATOM   8197  N  N     . ASN   C 2  165 ? 24.822  2.199   -28.812 1.00 30.68  ? 167 ASN   D N     1 
ATOM   8198  C  CA    . ASN   C 2  165 ? 23.516  1.549   -28.791 1.00 35.11  ? 167 ASN   D CA    1 
ATOM   8199  C  C     . ASN   C 2  165 ? 23.529  0.363   -29.748 1.00 37.72  ? 167 ASN   D C     1 
ATOM   8200  O  O     . ASN   C 2  165 ? 24.290  0.347   -30.716 1.00 45.98  ? 167 ASN   D O     1 
ATOM   8201  C  CB    . ASN   C 2  165 ? 22.433  2.556   -29.202 1.00 40.49  ? 167 ASN   D CB    1 
ATOM   8202  C  CG    . ASN   C 2  165 ? 21.025  2.072   -28.926 1.00 35.69  ? 167 ASN   D CG    1 
ATOM   8203  O  OD1   . ASN   C 2  165 ? 20.814  1.243   -28.046 1.00 40.11  ? 167 ASN   D OD1   1 
ATOM   8204  N  ND2   . ASN   C 2  165 ? 20.045  2.615   -29.663 1.00 26.09  ? 167 ASN   D ND2   1 
ATOM   8205  N  N     . THR   C 2  166 ? 22.705  -0.644  -29.480 1.00 40.32  ? 168 THR   D N     1 
ATOM   8206  C  CA    . THR   C 2  166 ? 22.547  -1.705  -30.472 1.00 41.76  ? 168 THR   D CA    1 
ATOM   8207  C  C     . THR   C 2  166 ? 21.132  -2.258  -30.470 1.00 43.96  ? 168 THR   D C     1 
ATOM   8208  O  O     . THR   C 2  166 ? 20.489  -2.364  -29.417 1.00 35.99  ? 168 THR   D O     1 
ATOM   8209  C  CB    . THR   C 2  166 ? 23.507  -2.879  -30.263 1.00 33.16  ? 168 THR   D CB    1 
ATOM   8210  O  OG1   . THR   C 2  166 ? 23.300  -3.428  -28.957 1.00 38.44  ? 168 THR   D OG1   1 
ATOM   8211  C  CG2   . THR   C 2  166 ? 24.954  -2.448  -30.440 1.00 31.48  ? 168 THR   D CG2   1 
ATOM   8212  N  N     . PHE   C 2  167 ? 20.663  -2.590  -31.676 1.00 45.81  ? 169 PHE   D N     1 
ATOM   8213  C  CA    . PHE   C 2  167 ? 19.530  -3.477  -31.924 1.00 37.71  ? 169 PHE   D CA    1 
ATOM   8214  C  C     . PHE   C 2  167 ? 20.119  -4.803  -32.394 1.00 38.37  ? 169 PHE   D C     1 
ATOM   8215  O  O     . PHE   C 2  167 ? 20.446  -4.970  -33.569 1.00 45.10  ? 169 PHE   D O     1 
ATOM   8216  C  CB    . PHE   C 2  167 ? 18.606  -2.879  -32.929 1.00 28.41  ? 169 PHE   D CB    1 
ATOM   8217  C  CG    . PHE   C 2  167 ? 17.942  -1.645  -32.438 1.00 34.57  ? 169 PHE   D CG    1 
ATOM   8218  C  CD1   . PHE   C 2  167 ? 18.642  -0.453  -32.360 1.00 33.08  ? 169 PHE   D CD1   1 
ATOM   8219  C  CD2   . PHE   C 2  167 ? 16.616  -1.672  -32.022 1.00 38.29  ? 169 PHE   D CD2   1 
ATOM   8220  C  CE1   . PHE   C 2  167 ? 18.018  0.710   -31.891 1.00 37.01  ? 169 PHE   D CE1   1 
ATOM   8221  C  CE2   . PHE   C 2  167 ? 15.992  -0.516  -31.544 1.00 36.39  ? 169 PHE   D CE2   1 
ATOM   8222  C  CZ    . PHE   C 2  167 ? 16.691  0.677   -31.490 1.00 29.15  ? 169 PHE   D CZ    1 
ATOM   8223  N  N     . SER   C 2  168 ? 20.285  -5.729  -31.451 1.00 28.01  ? 170 SER   D N     1 
ATOM   8224  C  CA    . SER   C 2  168 ? 20.956  -6.996  -31.687 1.00 33.54  ? 170 SER   D CA    1 
ATOM   8225  C  C     . SER   C 2  168 ? 19.899  -8.090  -31.799 1.00 46.24  ? 170 SER   D C     1 
ATOM   8226  O  O     . SER   C 2  168 ? 19.212  -8.390  -30.817 1.00 53.57  ? 170 SER   D O     1 
ATOM   8227  C  CB    . SER   C 2  168 ? 21.943  -7.281  -30.560 1.00 34.64  ? 170 SER   D CB    1 
ATOM   8228  O  OG    . SER   C 2  168 ? 22.989  -6.330  -30.592 1.00 37.32  ? 170 SER   D OG    1 
ATOM   8229  N  N     . VAL   C 2  169 ? 19.775  -8.688  -32.995 1.00 46.73  ? 171 VAL   D N     1 
ATOM   8230  C  CA    . VAL   C 2  169 ? 18.704  -9.633  -33.330 1.00 37.72  ? 171 VAL   D CA    1 
ATOM   8231  C  C     . VAL   C 2  169 ? 19.191  -11.057 -33.112 1.00 45.02  ? 171 VAL   D C     1 
ATOM   8232  O  O     . VAL   C 2  169 ? 20.231  -11.456 -33.654 1.00 50.75  ? 171 VAL   D O     1 
ATOM   8233  C  CB    . VAL   C 2  169 ? 18.228  -9.458  -34.776 1.00 38.88  ? 171 VAL   D CB    1 
ATOM   8234  C  CG1   . VAL   C 2  169 ? 17.225  -10.523 -35.077 1.00 49.43  ? 171 VAL   D CG1   1 
ATOM   8235  C  CG2   . VAL   C 2  169 ? 17.624  -8.072  -34.985 1.00 41.61  ? 171 VAL   D CG2   1 
ATOM   8236  N  N     . MET   C 2  170 ? 18.401  -11.852 -32.355 1.00 44.70  ? 172 MET   D N     1 
ATOM   8237  C  CA    . MET   C 2  170 ? 18.901  -13.032 -31.656 1.00 49.33  ? 172 MET   D CA    1 
ATOM   8238  C  C     . MET   C 2  170 ? 18.450  -14.311 -32.343 1.00 51.33  ? 172 MET   D C     1 
ATOM   8239  O  O     . MET   C 2  170 ? 17.316  -14.388 -32.834 1.00 54.63  ? 172 MET   D O     1 
ATOM   8240  C  CB    . MET   C 2  170 ? 18.411  -13.060 -30.200 1.00 59.14  ? 172 MET   D CB    1 
ATOM   8241  C  CG    . MET   C 2  170 ? 18.661  -11.779 -29.413 1.00 49.93  ? 172 MET   D CG    1 
ATOM   8242  S  SD    . MET   C 2  170 ? 20.301  -11.815 -28.696 0.47 42.12  ? 172 MET   D SD    1 
ATOM   8243  C  CE    . MET   C 2  170 ? 20.492  -13.585 -28.473 1.00 47.29  ? 172 MET   D CE    1 
ATOM   8244  N  N     . PRO   C 2  171 ? 19.305  -15.335 -32.353 1.00 58.41  ? 173 PRO   D N     1 
ATOM   8245  C  CA    . PRO   C 2  171 ? 18.979  -16.567 -33.085 1.00 61.17  ? 173 PRO   D CA    1 
ATOM   8246  C  C     . PRO   C 2  171 ? 17.855  -17.375 -32.446 1.00 55.62  ? 173 PRO   D C     1 
ATOM   8247  O  O     . PRO   C 2  171 ? 17.784  -17.528 -31.223 1.00 52.39  ? 173 PRO   D O     1 
ATOM   8248  C  CB    . PRO   C 2  171 ? 20.303  -17.349 -33.068 1.00 60.53  ? 173 PRO   D CB    1 
ATOM   8249  C  CG    . PRO   C 2  171 ? 21.091  -16.780 -31.943 1.00 51.01  ? 173 PRO   D CG    1 
ATOM   8250  C  CD    . PRO   C 2  171 ? 20.696  -15.330 -31.865 1.00 55.29  ? 173 PRO   D CD    1 
ATOM   8251  N  N     . SER   C 2  172 ? 16.992  -17.922 -33.305 1.00 66.15  ? 174 SER   D N     1 
ATOM   8252  C  CA    . SER   C 2  172 ? 16.001  -18.929 -32.918 1.00 70.38  ? 174 SER   D CA    1 
ATOM   8253  C  C     . SER   C 2  172 ? 16.087  -20.108 -33.882 1.00 64.45  ? 174 SER   D C     1 
ATOM   8254  O  O     . SER   C 2  172 ? 15.885  -19.926 -35.102 1.00 64.55  ? 174 SER   D O     1 
ATOM   8255  C  CB    . SER   C 2  172 ? 14.584  -18.345 -32.909 1.00 66.29  ? 174 SER   D CB    1 
ATOM   8256  O  OG    . SER   C 2  172 ? 13.624  -19.333 -32.554 1.00 62.63  ? 174 SER   D OG    1 
ATOM   8257  N  N     . PRO   C 2  173 ? 16.340  -21.329 -33.402 1.00 60.81  ? 175 PRO   D N     1 
ATOM   8258  C  CA    . PRO   C 2  173 ? 16.355  -22.486 -34.318 1.00 60.29  ? 175 PRO   D CA    1 
ATOM   8259  C  C     . PRO   C 2  173 ? 15.046  -22.658 -35.074 1.00 58.10  ? 175 PRO   D C     1 
ATOM   8260  O  O     . PRO   C 2  173 ? 14.946  -23.559 -35.921 1.00 61.33  ? 175 PRO   D O     1 
ATOM   8261  C  CB    . PRO   C 2  173 ? 16.630  -23.682 -33.388 1.00 54.20  ? 175 PRO   D CB    1 
ATOM   8262  C  CG    . PRO   C 2  173 ? 17.144  -23.072 -32.101 1.00 56.08  ? 175 PRO   D CG    1 
ATOM   8263  C  CD    . PRO   C 2  173 ? 16.478  -21.730 -31.991 1.00 58.53  ? 175 PRO   D CD    1 
ATOM   8264  N  N     . LYS   C 2  174 ? 14.049  -21.827 -34.788 1.00 53.39  ? 176 LYS   D N     1 
ATOM   8265  C  CA    . LYS   C 2  174 ? 12.771  -21.834 -35.471 1.00 59.85  ? 176 LYS   D CA    1 
ATOM   8266  C  C     . LYS   C 2  174 ? 12.726  -20.825 -36.605 1.00 57.26  ? 176 LYS   D C     1 
ATOM   8267  O  O     . LYS   C 2  174 ? 11.696  -20.721 -37.279 1.00 57.40  ? 176 LYS   D O     1 
ATOM   8268  C  CB    . LYS   C 2  174 ? 11.626  -21.528 -34.488 1.00 61.36  ? 176 LYS   D CB    1 
ATOM   8269  C  CG    . LYS   C 2  174 ? 11.608  -22.314 -33.172 1.00 60.58  ? 176 LYS   D CG    1 
ATOM   8270  C  CD    . LYS   C 2  174 ? 10.462  -21.790 -32.270 1.00 66.72  ? 176 LYS   D CD    1 
ATOM   8271  C  CE    . LYS   C 2  174 ? 10.583  -22.255 -30.810 1.00 59.44  ? 176 LYS   D CE    1 
ATOM   8272  N  NZ    . LYS   C 2  174 ? 9.551   -21.654 -29.899 1.00 62.77  ? 176 LYS   D NZ    1 
ATOM   8273  N  N     . VAL   C 2  175 ? 13.796  -20.062 -36.821 1.00 53.07  ? 177 VAL   D N     1 
ATOM   8274  C  CA    . VAL   C 2  175 ? 13.758  -19.007 -37.829 1.00 65.40  ? 177 VAL   D CA    1 
ATOM   8275  C  C     . VAL   C 2  175 ? 14.949  -19.129 -38.776 1.00 67.26  ? 177 VAL   D C     1 
ATOM   8276  O  O     . VAL   C 2  175 ? 14.859  -18.734 -39.945 1.00 69.02  ? 177 VAL   D O     1 
ATOM   8277  C  CB    . VAL   C 2  175 ? 13.691  -17.613 -37.176 1.00 62.60  ? 177 VAL   D CB    1 
ATOM   8278  C  CG1   . VAL   C 2  175 ? 14.009  -16.533 -38.191 1.00 63.30  ? 177 VAL   D CG1   1 
ATOM   8279  C  CG2   . VAL   C 2  175 ? 12.297  -17.373 -36.599 1.00 57.64  ? 177 VAL   D CG2   1 
ATOM   8280  N  N     . SER   C 2  176 ? 16.063  -19.690 -38.292 1.00 62.99  ? 178 SER   D N     1 
ATOM   8281  C  CA    . SER   C 2  176 ? 17.205  -20.024 -39.138 1.00 68.88  ? 178 SER   D CA    1 
ATOM   8282  C  C     . SER   C 2  176 ? 17.803  -21.355 -38.706 1.00 79.86  ? 178 SER   D C     1 
ATOM   8283  O  O     . SER   C 2  176 ? 17.793  -21.718 -37.524 1.00 63.67  ? 178 SER   D O     1 
ATOM   8284  C  CB    . SER   C 2  176 ? 18.320  -18.965 -39.107 1.00 71.12  ? 178 SER   D CB    1 
ATOM   8285  O  OG    . SER   C 2  176 ? 17.882  -17.708 -39.589 1.00 78.40  ? 178 SER   D OG    1 
ATOM   8286  N  N     . ASP   C 2  177 ? 18.365  -22.059 -39.686 1.00 96.41  ? 179 ASP   D N     1 
ATOM   8287  C  CA    . ASP   C 2  177 ? 18.917  -23.391 -39.493 1.00 89.65  ? 179 ASP   D CA    1 
ATOM   8288  C  C     . ASP   C 2  177 ? 20.440  -23.426 -39.502 1.00 82.35  ? 179 ASP   D C     1 
ATOM   8289  O  O     . ASP   C 2  177 ? 21.023  -24.438 -39.096 1.00 71.97  ? 179 ASP   D O     1 
ATOM   8290  C  CB    . ASP   C 2  177 ? 18.379  -24.331 -40.582 1.00 84.38  ? 179 ASP   D CB    1 
ATOM   8291  C  CG    . ASP   C 2  177 ? 18.170  -23.615 -41.923 1.00 99.81  ? 179 ASP   D CG    1 
ATOM   8292  O  OD1   . ASP   C 2  177 ? 17.758  -22.428 -41.921 1.00 91.98  ? 179 ASP   D OD1   1 
ATOM   8293  O  OD2   . ASP   C 2  177 ? 18.423  -24.241 -42.978 1.00 105.19 ? 179 ASP   D OD2   1 
ATOM   8294  N  N     . THR   C 2  178 ? 21.085  -22.354 -39.961 1.00 78.99  ? 180 THR   D N     1 
ATOM   8295  C  CA    . THR   C 2  178 ? 22.538  -22.262 -39.966 1.00 68.29  ? 180 THR   D CA    1 
ATOM   8296  C  C     . THR   C 2  178 ? 23.085  -22.691 -38.616 1.00 66.25  ? 180 THR   D C     1 
ATOM   8297  O  O     . THR   C 2  178 ? 22.738  -22.119 -37.584 1.00 81.10  ? 180 THR   D O     1 
ATOM   8298  C  CB    . THR   C 2  178 ? 22.944  -20.828 -40.307 1.00 70.25  ? 180 THR   D CB    1 
ATOM   8299  O  OG1   . THR   C 2  178 ? 21.897  -19.930 -39.907 1.00 82.41  ? 180 THR   D OG1   1 
ATOM   8300  C  CG2   . THR   C 2  178 ? 23.124  -20.681 -41.796 1.00 69.86  ? 180 THR   D CG2   1 
ATOM   8301  N  N     . VAL   C 2  179 ? 23.918  -23.728 -38.619 1.00 74.55  ? 181 VAL   D N     1 
ATOM   8302  C  CA    . VAL   C 2  179 ? 24.189  -24.463 -37.389 1.00 74.07  ? 181 VAL   D CA    1 
ATOM   8303  C  C     . VAL   C 2  179 ? 25.112  -23.708 -36.435 1.00 73.07  ? 181 VAL   D C     1 
ATOM   8304  O  O     . VAL   C 2  179 ? 25.095  -23.974 -35.224 1.00 71.96  ? 181 VAL   D O     1 
ATOM   8305  C  CB    . VAL   C 2  179 ? 24.768  -25.850 -37.743 1.00 75.49  ? 181 VAL   D CB    1 
ATOM   8306  C  CG1   . VAL   C 2  179 ? 24.767  -26.788 -36.523 1.00 64.96  ? 181 VAL   D CG1   1 
ATOM   8307  C  CG2   . VAL   C 2  179 ? 23.998  -26.451 -38.906 1.00 59.56  ? 181 VAL   D CG2   1 
ATOM   8308  N  N     . VAL   C 2  180 ? 25.921  -22.773 -36.931 1.00 70.12  ? 182 VAL   D N     1 
ATOM   8309  C  CA    . VAL   C 2  180 ? 26.904  -22.119 -36.067 1.00 74.84  ? 182 VAL   D CA    1 
ATOM   8310  C  C     . VAL   C 2  180 ? 26.320  -20.870 -35.412 1.00 65.59  ? 182 VAL   D C     1 
ATOM   8311  O  O     . VAL   C 2  180 ? 27.061  -19.948 -35.049 1.00 69.64  ? 182 VAL   D O     1 
ATOM   8312  C  CB    . VAL   C 2  180 ? 28.200  -21.766 -36.834 1.00 72.98  ? 182 VAL   D CB    1 
ATOM   8313  C  CG1   . VAL   C 2  180 ? 29.161  -22.941 -36.833 1.00 64.98  ? 182 VAL   D CG1   1 
ATOM   8314  C  CG2   . VAL   C 2  180 ? 27.902  -21.280 -38.266 1.00 63.63  ? 182 VAL   D CG2   1 
ATOM   8315  N  N     . GLU   C 2  181 ? 25.001  -20.823 -35.242 1.00 61.20  ? 183 GLU   D N     1 
ATOM   8316  C  CA    . GLU   C 2  181 ? 24.438  -19.576 -34.744 1.00 64.10  ? 183 GLU   D CA    1 
ATOM   8317  C  C     . GLU   C 2  181 ? 24.680  -19.421 -33.237 1.00 57.78  ? 183 GLU   D C     1 
ATOM   8318  O  O     . GLU   C 2  181 ? 25.000  -18.313 -32.795 1.00 48.59  ? 183 GLU   D O     1 
ATOM   8319  C  CB    . GLU   C 2  181 ? 22.959  -19.469 -35.131 1.00 55.82  ? 183 GLU   D CB    1 
ATOM   8320  C  CG    . GLU   C 2  181 ? 22.774  -19.163 -36.633 1.00 53.04  ? 183 GLU   D CG    1 
ATOM   8321  C  CD    . GLU   C 2  181 ? 21.429  -18.522 -36.982 1.00 58.16  ? 183 GLU   D CD    1 
ATOM   8322  O  OE1   . GLU   C 2  181 ? 20.596  -18.323 -36.078 1.00 64.65  ? 183 GLU   D OE1   1 
ATOM   8323  O  OE2   . GLU   C 2  181 ? 21.203  -18.204 -38.165 1.00 55.01  ? 183 GLU   D OE2   1 
ATOM   8324  N  N     . PRO   C 2  182 ? 24.580  -20.483 -32.406 1.00 63.02  ? 184 PRO   D N     1 
ATOM   8325  C  CA    . PRO   C 2  182 ? 25.038  -20.346 -31.013 1.00 52.04  ? 184 PRO   D CA    1 
ATOM   8326  C  C     . PRO   C 2  182 ? 26.430  -19.742 -30.935 1.00 53.74  ? 184 PRO   D C     1 
ATOM   8327  O  O     . PRO   C 2  182 ? 26.591  -18.646 -30.396 1.00 61.67  ? 184 PRO   D O     1 
ATOM   8328  C  CB    . PRO   C 2  182 ? 25.009  -21.783 -30.466 1.00 45.59  ? 184 PRO   D CB    1 
ATOM   8329  C  CG    . PRO   C 2  182 ? 24.272  -22.599 -31.475 1.00 56.64  ? 184 PRO   D CG    1 
ATOM   8330  C  CD    . PRO   C 2  182 ? 23.781  -21.704 -32.594 1.00 62.27  ? 184 PRO   D CD    1 
ATOM   8331  N  N     . TYR   C 2  183 ? 27.439  -20.436 -31.465 1.00 57.19  ? 185 TYR   D N     1 
ATOM   8332  C  CA    . TYR   C 2  183 ? 28.774  -19.853 -31.588 1.00 58.62  ? 185 TYR   D CA    1 
ATOM   8333  C  C     . TYR   C 2  183 ? 28.717  -18.364 -31.951 1.00 52.73  ? 185 TYR   D C     1 
ATOM   8334  O  O     . TYR   C 2  183 ? 29.345  -17.522 -31.300 1.00 49.04  ? 185 TYR   D O     1 
ATOM   8335  C  CB    . TYR   C 2  183 ? 29.580  -20.609 -32.657 1.00 64.08  ? 185 TYR   D CB    1 
ATOM   8336  C  CG    . TYR   C 2  183 ? 29.966  -22.045 -32.342 1.00 65.02  ? 185 TYR   D CG    1 
ATOM   8337  C  CD1   . TYR   C 2  183 ? 30.238  -22.455 -31.041 1.00 64.57  ? 185 TYR   D CD1   1 
ATOM   8338  C  CD2   . TYR   C 2  183 ? 30.078  -22.987 -33.361 1.00 65.40  ? 185 TYR   D CD2   1 
ATOM   8339  C  CE1   . TYR   C 2  183 ? 30.600  -23.761 -30.762 1.00 62.12  ? 185 TYR   D CE1   1 
ATOM   8340  C  CE2   . TYR   C 2  183 ? 30.432  -24.294 -33.090 1.00 65.61  ? 185 TYR   D CE2   1 
ATOM   8341  C  CZ    . TYR   C 2  183 ? 30.692  -24.674 -31.791 1.00 62.82  ? 185 TYR   D CZ    1 
ATOM   8342  O  OH    . TYR   C 2  183 ? 31.041  -25.973 -31.521 1.00 56.57  ? 185 TYR   D OH    1 
ATOM   8343  N  N     . ASN   C 2  184 ? 27.977  -18.024 -33.009 1.00 51.09  ? 186 ASN   D N     1 
ATOM   8344  C  CA    . ASN   C 2  184 ? 27.954  -16.642 -33.481 1.00 54.28  ? 186 ASN   D CA    1 
ATOM   8345  C  C     . ASN   C 2  184 ? 27.378  -15.702 -32.431 1.00 58.19  ? 186 ASN   D C     1 
ATOM   8346  O  O     . ASN   C 2  184 ? 27.868  -14.580 -32.247 1.00 54.82  ? 186 ASN   D O     1 
ATOM   8347  C  CB    . ASN   C 2  184 ? 27.150  -16.545 -34.774 1.00 51.18  ? 186 ASN   D CB    1 
ATOM   8348  C  CG    . ASN   C 2  184 ? 28.010  -16.708 -35.995 1.00 57.05  ? 186 ASN   D CG    1 
ATOM   8349  O  OD1   . ASN   C 2  184 ? 28.990  -17.463 -35.983 1.00 51.88  ? 186 ASN   D OD1   1 
ATOM   8350  N  ND2   . ASN   C 2  184 ? 27.664  -15.986 -37.060 1.00 59.70  ? 186 ASN   D ND2   1 
ATOM   8351  N  N     . ALA   C 2  185 ? 26.319  -16.137 -31.749 1.00 59.86  ? 187 ALA   D N     1 
ATOM   8352  C  CA    . ALA   C 2  185 ? 25.700  -15.315 -30.720 1.00 49.48  ? 187 ALA   D CA    1 
ATOM   8353  C  C     . ALA   C 2  185 ? 26.631  -15.153 -29.525 1.00 49.42  ? 187 ALA   D C     1 
ATOM   8354  O  O     . ALA   C 2  185 ? 26.949  -14.029 -29.116 1.00 48.87  ? 187 ALA   D O     1 
ATOM   8355  C  CB    . ALA   C 2  185 ? 24.363  -15.931 -30.301 1.00 49.51  ? 187 ALA   D CB    1 
ATOM   8356  N  N     . THR   C 2  186 ? 27.090  -16.265 -28.956 1.00 39.54  ? 188 THR   D N     1 
ATOM   8357  C  CA    . THR   C 2  186 ? 27.910  -16.180 -27.754 1.00 43.40  ? 188 THR   D CA    1 
ATOM   8358  C  C     . THR   C 2  186 ? 29.133  -15.292 -27.988 1.00 49.40  ? 188 THR   D C     1 
ATOM   8359  O  O     . THR   C 2  186 ? 29.283  -14.241 -27.353 1.00 49.56  ? 188 THR   D O     1 
ATOM   8360  C  CB    . THR   C 2  186 ? 28.293  -17.586 -27.286 1.00 39.00  ? 188 THR   D CB    1 
ATOM   8361  O  OG1   . THR   C 2  186 ? 27.113  -18.248 -26.824 1.00 43.73  ? 188 THR   D OG1   1 
ATOM   8362  C  CG2   . THR   C 2  186 ? 29.271  -17.526 -26.132 1.00 46.69  ? 188 THR   D CG2   1 
ATOM   8363  N  N     . LEU   C 2  187 ? 30.004  -15.687 -28.921 1.00 54.41  ? 189 LEU   D N     1 
ATOM   8364  C  CA    . LEU   C 2  187 ? 31.117  -14.828 -29.331 1.00 50.65  ? 189 LEU   D CA    1 
ATOM   8365  C  C     . LEU   C 2  187 ? 30.680  -13.375 -29.535 1.00 46.87  ? 189 LEU   D C     1 
ATOM   8366  O  O     . LEU   C 2  187 ? 31.407  -12.445 -29.172 1.00 48.43  ? 189 LEU   D O     1 
ATOM   8367  C  CB    . LEU   C 2  187 ? 31.737  -15.366 -30.621 1.00 47.52  ? 189 LEU   D CB    1 
ATOM   8368  C  CG    . LEU   C 2  187 ? 32.304  -16.776 -30.655 1.00 43.11  ? 189 LEU   D CG    1 
ATOM   8369  C  CD1   . LEU   C 2  187 ? 32.690  -17.082 -32.099 1.00 44.33  ? 189 LEU   D CD1   1 
ATOM   8370  C  CD2   . LEU   C 2  187 ? 33.494  -16.938 -29.675 1.00 40.19  ? 189 LEU   D CD2   1 
ATOM   8371  N  N     . SER   C 2  188 ? 29.503  -13.159 -30.127 1.00 41.13  ? 190 SER   D N     1 
ATOM   8372  C  CA    . SER   C 2  188 ? 29.017  -11.798 -30.321 1.00 43.53  ? 190 SER   D CA    1 
ATOM   8373  C  C     . SER   C 2  188 ? 28.628  -11.147 -28.987 1.00 48.73  ? 190 SER   D C     1 
ATOM   8374  O  O     . SER   C 2  188 ? 28.914  -9.964  -28.762 1.00 42.21  ? 190 SER   D O     1 
ATOM   8375  C  CB    . SER   C 2  188 ? 27.839  -11.823 -31.302 1.00 42.59  ? 190 SER   D CB    1 
ATOM   8376  O  OG    . SER   C 2  188 ? 27.582  -10.557 -31.890 1.00 38.02  ? 190 SER   D OG    1 
ATOM   8377  N  N     . VAL   C 2  189 ? 27.996  -11.912 -28.083 1.00 47.76  ? 191 VAL   D N     1 
ATOM   8378  C  CA    . VAL   C 2  189 ? 27.464  -11.362 -26.836 1.00 36.59  ? 191 VAL   D CA    1 
ATOM   8379  C  C     . VAL   C 2  189 ? 28.585  -11.041 -25.868 1.00 39.91  ? 191 VAL   D C     1 
ATOM   8380  O  O     . VAL   C 2  189 ? 28.497  -10.076 -25.096 1.00 41.87  ? 191 VAL   D O     1 
ATOM   8381  C  CB    . VAL   C 2  189 ? 26.441  -12.341 -26.221 1.00 42.26  ? 191 VAL   D CB    1 
ATOM   8382  C  CG1   . VAL   C 2  189 ? 26.176  -12.008 -24.774 1.00 38.37  ? 191 VAL   D CG1   1 
ATOM   8383  C  CG2   . VAL   C 2  189 ? 25.131  -12.321 -27.017 1.00 40.39  ? 191 VAL   D CG2   1 
ATOM   8384  N  N     . HIS   C 2  190 ? 29.646  -11.848 -25.885 1.00 45.92  ? 192 HIS   D N     1 
ATOM   8385  C  CA    . HIS   C 2  190 ? 30.852  -11.567 -25.115 1.00 38.60  ? 192 HIS   D CA    1 
ATOM   8386  C  C     . HIS   C 2  190 ? 31.460  -10.229 -25.511 1.00 40.47  ? 192 HIS   D C     1 
ATOM   8387  O  O     . HIS   C 2  190 ? 32.077  -9.557  -24.679 1.00 44.37  ? 192 HIS   D O     1 
ATOM   8388  C  CB    . HIS   C 2  190 ? 31.823  -12.720 -25.324 1.00 41.57  ? 192 HIS   D CB    1 
ATOM   8389  C  CG    . HIS   C 2  190 ? 33.225  -12.446 -24.889 1.00 50.27  ? 192 HIS   D CG    1 
ATOM   8390  N  ND1   . HIS   C 2  190 ? 33.743  -12.929 -23.708 1.00 45.80  ? 192 HIS   D ND1   1 
ATOM   8391  C  CD2   . HIS   C 2  190 ? 34.240  -11.800 -25.509 1.00 54.02  ? 192 HIS   D CD2   1 
ATOM   8392  C  CE1   . HIS   C 2  190 ? 35.010  -12.571 -23.607 1.00 54.97  ? 192 HIS   D CE1   1 
ATOM   8393  N  NE2   . HIS   C 2  190 ? 35.336  -11.883 -24.687 1.00 53.89  ? 192 HIS   D NE2   1 
ATOM   8394  N  N     . GLN   C 2  191 ? 31.287  -9.822  -26.771 1.00 43.48  ? 193 GLN   D N     1 
ATOM   8395  C  CA    . GLN   C 2  191 ? 31.573  -8.443  -27.170 1.00 43.12  ? 193 GLN   D CA    1 
ATOM   8396  C  C     . GLN   C 2  191 ? 30.604  -7.464  -26.511 1.00 37.04  ? 193 GLN   D C     1 
ATOM   8397  O  O     . GLN   C 2  191 ? 31.022  -6.512  -25.844 1.00 32.39  ? 193 GLN   D O     1 
ATOM   8398  C  CB    . GLN   C 2  191 ? 31.487  -8.294  -28.697 1.00 43.78  ? 193 GLN   D CB    1 
ATOM   8399  C  CG    . GLN   C 2  191 ? 32.570  -8.969  -29.491 1.00 41.36  ? 193 GLN   D CG    1 
ATOM   8400  C  CD    . GLN   C 2  191 ? 33.933  -8.598  -29.004 1.00 43.41  ? 193 GLN   D CD    1 
ATOM   8401  O  OE1   . GLN   C 2  191 ? 34.380  -7.465  -29.187 1.00 44.77  ? 193 GLN   D OE1   1 
ATOM   8402  N  NE2   . GLN   C 2  191 ? 34.606  -9.546  -28.362 1.00 38.44  ? 193 GLN   D NE2   1 
ATOM   8403  N  N     . LEU   C 2  192 ? 29.298  -7.684  -26.706 1.00 37.13  ? 194 LEU   D N     1 
ATOM   8404  C  CA    . LEU   C 2  192 ? 28.292  -6.716  -26.284 1.00 37.62  ? 194 LEU   D CA    1 
ATOM   8405  C  C     . LEU   C 2  192 ? 28.297  -6.495  -24.764 1.00 39.71  ? 194 LEU   D C     1 
ATOM   8406  O  O     . LEU   C 2  192 ? 28.029  -5.377  -24.298 1.00 33.43  ? 194 LEU   D O     1 
ATOM   8407  C  CB    . LEU   C 2  192 ? 26.910  -7.165  -26.773 1.00 31.66  ? 194 LEU   D CB    1 
ATOM   8408  C  CG    . LEU   C 2  192 ? 26.635  -7.204  -28.283 1.00 29.98  ? 194 LEU   D CG    1 
ATOM   8409  C  CD1   . LEU   C 2  192 ? 25.252  -7.782  -28.503 1.00 32.75  ? 194 LEU   D CD1   1 
ATOM   8410  C  CD2   . LEU   C 2  192 ? 26.729  -5.839  -28.960 1.00 25.73  ? 194 LEU   D CD2   1 
ATOM   8411  N  N     . VAL   C 2  193 ? 28.605  -7.524  -23.969 1.00 34.27  ? 195 VAL   D N     1 
ATOM   8412  C  CA    . VAL   C 2  193 ? 28.600  -7.311  -22.530 1.00 32.45  ? 195 VAL   D CA    1 
ATOM   8413  C  C     . VAL   C 2  193 ? 29.610  -6.248  -22.121 1.00 42.16  ? 195 VAL   D C     1 
ATOM   8414  O  O     . VAL   C 2  193 ? 29.419  -5.577  -21.102 1.00 42.26  ? 195 VAL   D O     1 
ATOM   8415  C  CB    . VAL   C 2  193 ? 28.855  -8.630  -21.775 1.00 36.81  ? 195 VAL   D CB    1 
ATOM   8416  C  CG1   . VAL   C 2  193 ? 29.735  -8.392  -20.541 1.00 37.38  ? 195 VAL   D CG1   1 
ATOM   8417  C  CG2   . VAL   C 2  193 ? 27.545  -9.214  -21.341 1.00 37.98  ? 195 VAL   D CG2   1 
ATOM   8418  N  N     . GLU   C 2  194 ? 30.678  -6.058  -22.904 1.00 39.42  ? 196 GLU   D N     1 
ATOM   8419  C  CA    . GLU   C 2  194 ? 31.774  -5.189  -22.504 1.00 32.47  ? 196 GLU   D CA    1 
ATOM   8420  C  C     . GLU   C 2  194 ? 31.814  -3.858  -23.242 1.00 37.07  ? 196 GLU   D C     1 
ATOM   8421  O  O     . GLU   C 2  194 ? 32.439  -2.919  -22.741 1.00 48.73  ? 196 GLU   D O     1 
ATOM   8422  C  CB    . GLU   C 2  194 ? 33.123  -5.902  -22.706 1.00 26.99  ? 196 GLU   D CB    1 
ATOM   8423  C  CG    . GLU   C 2  194 ? 33.122  -7.373  -22.328 1.00 36.34  ? 196 GLU   D CG    1 
ATOM   8424  C  CD    . GLU   C 2  194 ? 33.483  -7.643  -20.857 1.00 46.39  ? 196 GLU   D CD    1 
ATOM   8425  O  OE1   . GLU   C 2  194 ? 34.197  -6.810  -20.251 1.00 47.28  ? 196 GLU   D OE1   1 
ATOM   8426  O  OE2   . GLU   C 2  194 ? 33.060  -8.696  -20.310 1.00 42.67  ? 196 GLU   D OE2   1 
ATOM   8427  N  N     . ASN   C 2  195 ? 31.160  -3.733  -24.399 1.00 33.54  ? 197 ASN   D N     1 
ATOM   8428  C  CA    . ASN   C 2  195 ? 31.413  -2.589  -25.268 1.00 34.88  ? 197 ASN   D CA    1 
ATOM   8429  C  C     . ASN   C 2  195 ? 30.158  -1.874  -25.776 1.00 35.83  ? 197 ASN   D C     1 
ATOM   8430  O  O     . ASN   C 2  195 ? 30.281  -0.984  -26.634 1.00 32.32  ? 197 ASN   D O     1 
ATOM   8431  C  CB    . ASN   C 2  195 ? 32.290  -3.020  -26.449 1.00 33.30  ? 197 ASN   D CB    1 
ATOM   8432  C  CG    . ASN   C 2  195 ? 33.779  -3.018  -26.101 1.00 45.95  ? 197 ASN   D CG    1 
ATOM   8433  O  OD1   . ASN   C 2  195 ? 34.474  -2.039  -26.364 1.00 53.28  ? 197 ASN   D OD1   1 
ATOM   8434  N  ND2   . ASN   C 2  195 ? 34.268  -4.104  -25.498 1.00 36.76  ? 197 ASN   D ND2   1 
ATOM   8435  N  N     . THR   C 2  196 ? 28.963  -2.206  -25.266 1.00 33.24  ? 198 THR   D N     1 
ATOM   8436  C  CA    . THR   C 2  196 ? 27.769  -1.402  -25.523 1.00 37.17  ? 198 THR   D CA    1 
ATOM   8437  C  C     . THR   C 2  196 ? 27.190  -0.871  -24.217 1.00 27.96  ? 198 THR   D C     1 
ATOM   8438  O  O     . THR   C 2  196 ? 27.336  -1.478  -23.156 1.00 33.39  ? 198 THR   D O     1 
ATOM   8439  C  CB    . THR   C 2  196 ? 26.667  -2.176  -26.279 1.00 34.51  ? 198 THR   D CB    1 
ATOM   8440  O  OG1   . THR   C 2  196 ? 26.406  -3.419  -25.618 1.00 38.97  ? 198 THR   D OG1   1 
ATOM   8441  C  CG2   . THR   C 2  196 ? 27.057  -2.425  -27.726 1.00 27.81  ? 198 THR   D CG2   1 
ATOM   8442  N  N     . ASP   C 2  197 ? 26.528  0.273   -24.304 1.00 23.65  ? 199 ASP   D N     1 
ATOM   8443  C  CA    . ASP   C 2  197 ? 25.892  0.847   -23.129 1.00 26.21  ? 199 ASP   D CA    1 
ATOM   8444  C  C     . ASP   C 2  197 ? 24.454  0.371   -22.968 1.00 33.20  ? 199 ASP   D C     1 
ATOM   8445  O  O     . ASP   C 2  197 ? 24.002  0.117   -21.844 1.00 31.04  ? 199 ASP   D O     1 
ATOM   8446  C  CB    . ASP   C 2  197 ? 25.942  2.373   -23.209 1.00 30.76  ? 199 ASP   D CB    1 
ATOM   8447  C  CG    . ASP   C 2  197 ? 27.361  2.898   -23.290 1.00 34.16  ? 199 ASP   D CG    1 
ATOM   8448  O  OD1   . ASP   C 2  197 ? 28.200  2.499   -22.441 1.00 29.18  ? 199 ASP   D OD1   1 
ATOM   8449  O  OD2   . ASP   C 2  197 ? 27.633  3.693   -24.218 1.00 29.94  ? 199 ASP   D OD2   1 
ATOM   8450  N  N     . GLU   C 2  198 ? 23.731  0.237   -24.076 1.00 33.91  ? 200 GLU   D N     1 
ATOM   8451  C  CA    . GLU   C 2  198 ? 22.348  -0.224  -24.043 1.00 35.20  ? 200 GLU   D CA    1 
ATOM   8452  C  C     . GLU   C 2  198 ? 22.052  -1.054  -25.290 1.00 38.72  ? 200 GLU   D C     1 
ATOM   8453  O  O     . GLU   C 2  198 ? 22.235  -0.587  -26.422 1.00 37.88  ? 200 GLU   D O     1 
ATOM   8454  C  CB    . GLU   C 2  198 ? 21.400  0.965   -23.927 1.00 28.50  ? 200 GLU   D CB    1 
ATOM   8455  C  CG    . GLU   C 2  198 ? 21.834  2.137   -24.768 1.00 29.57  ? 200 GLU   D CG    1 
ATOM   8456  C  CD    . GLU   C 2  198 ? 21.308  3.443   -24.235 1.00 31.72  ? 200 GLU   D CD    1 
ATOM   8457  O  OE1   . GLU   C 2  198 ? 21.115  3.551   -23.013 1.00 42.12  ? 200 GLU   D OE1   1 
ATOM   8458  O  OE2   . GLU   C 2  198 ? 21.084  4.371   -25.029 1.00 31.65  ? 200 GLU   D OE2   1 
ATOM   8459  N  N     . THR   C 2  199 ? 21.584  -2.283  -25.069 1.00 38.68  ? 201 THR   D N     1 
ATOM   8460  C  CA    . THR   C 2  199 ? 21.329  -3.263  -26.119 1.00 42.44  ? 201 THR   D CA    1 
ATOM   8461  C  C     . THR   C 2  199 ? 19.885  -3.741  -26.018 1.00 35.73  ? 201 THR   D C     1 
ATOM   8462  O  O     . THR   C 2  199 ? 19.510  -4.385  -25.031 1.00 34.36  ? 201 THR   D O     1 
ATOM   8463  C  CB    . THR   C 2  199 ? 22.303  -4.448  -26.002 1.00 40.81  ? 201 THR   D CB    1 
ATOM   8464  O  OG1   . THR   C 2  199 ? 23.658  -3.984  -26.151 1.00 35.06  ? 201 THR   D OG1   1 
ATOM   8465  C  CG2   . THR   C 2  199 ? 22.007  -5.501  -27.046 1.00 29.30  ? 201 THR   D CG2   1 
ATOM   8466  N  N     . TYR   C 2  200 ? 19.082  -3.415  -27.032 1.00 31.86  ? 202 TYR   D N     1 
ATOM   8467  C  CA    . TYR   C 2  200 ? 17.754  -4.001  -27.215 1.00 34.36  ? 202 TYR   D CA    1 
ATOM   8468  C  C     . TYR   C 2  200 ? 17.888  -5.449  -27.709 1.00 47.13  ? 202 TYR   D C     1 
ATOM   8469  O  O     . TYR   C 2  200 ? 18.121  -5.695  -28.902 1.00 43.85  ? 202 TYR   D O     1 
ATOM   8470  C  CB    . TYR   C 2  200 ? 16.945  -3.176  -28.207 1.00 29.39  ? 202 TYR   D CB    1 
ATOM   8471  C  CG    . TYR   C 2  200 ? 16.685  -1.753  -27.770 1.00 37.40  ? 202 TYR   D CG    1 
ATOM   8472  C  CD1   . TYR   C 2  200 ? 15.623  -1.452  -26.914 1.00 33.26  ? 202 TYR   D CD1   1 
ATOM   8473  C  CD2   . TYR   C 2  200 ? 17.486  -0.699  -28.222 1.00 36.83  ? 202 TYR   D CD2   1 
ATOM   8474  C  CE1   . TYR   C 2  200 ? 15.381  -0.152  -26.497 1.00 32.87  ? 202 TYR   D CE1   1 
ATOM   8475  C  CE2   . TYR   C 2  200 ? 17.251  0.611   -27.811 1.00 30.61  ? 202 TYR   D CE2   1 
ATOM   8476  C  CZ    . TYR   C 2  200 ? 16.194  0.872   -26.947 1.00 38.54  ? 202 TYR   D CZ    1 
ATOM   8477  O  OH    . TYR   C 2  200 ? 15.943  2.162   -26.537 1.00 49.01  ? 202 TYR   D OH    1 
ATOM   8478  N  N     . CYS   C 2  201 ? 17.733  -6.421  -26.794 1.00 33.29  ? 203 CYS   D N     1 
ATOM   8479  C  CA    . CYS   C 2  201 ? 17.547  -7.824  -27.162 1.00 35.53  ? 203 CYS   D CA    1 
ATOM   8480  C  C     . CYS   C 2  201 ? 16.327  -8.043  -28.047 1.00 41.98  ? 203 CYS   D C     1 
ATOM   8481  O  O     . CYS   C 2  201 ? 15.192  -7.945  -27.573 1.00 41.43  ? 203 CYS   D O     1 
ATOM   8482  C  CB    . CYS   C 2  201 ? 17.375  -8.699  -25.929 1.00 38.65  ? 203 CYS   D CB    1 
ATOM   8483  S  SG    . CYS   C 2  201 ? 18.795  -8.782  -24.880 1.00 58.93  ? 203 CYS   D SG    1 
ATOM   8484  N  N     . ILE   C 2  202 ? 16.540  -8.381  -29.312 1.00 44.07  ? 204 ILE   D N     1 
ATOM   8485  C  CA    . ILE   C 2  202 ? 15.457  -8.699  -30.237 1.00 46.02  ? 204 ILE   D CA    1 
ATOM   8486  C  C     . ILE   C 2  202 ? 15.541  -10.186 -30.578 1.00 44.08  ? 204 ILE   D C     1 
ATOM   8487  O  O     . ILE   C 2  202 ? 16.423  -10.608 -31.334 1.00 52.03  ? 204 ILE   D O     1 
ATOM   8488  C  CB    . ILE   C 2  202 ? 15.522  -7.818  -31.486 1.00 39.81  ? 204 ILE   D CB    1 
ATOM   8489  C  CG1   . ILE   C 2  202 ? 15.012  -6.429  -31.130 1.00 33.66  ? 204 ILE   D CG1   1 
ATOM   8490  C  CG2   . ILE   C 2  202 ? 14.741  -8.439  -32.624 1.00 40.09  ? 204 ILE   D CG2   1 
ATOM   8491  C  CD1   . ILE   C 2  202 ? 15.221  -5.447  -32.208 1.00 30.67  ? 204 ILE   D CD1   1 
ATOM   8492  N  N     . ASP   C 2  203 ? 14.621  -10.982 -30.026 1.00 44.47  ? 205 ASP   D N     1 
ATOM   8493  C  CA    . ASP   C 2  203 ? 14.669  -12.443 -30.095 1.00 54.61  ? 205 ASP   D CA    1 
ATOM   8494  C  C     . ASP   C 2  203 ? 13.783  -12.916 -31.246 1.00 51.64  ? 205 ASP   D C     1 
ATOM   8495  O  O     . ASP   C 2  203 ? 12.572  -12.672 -31.249 1.00 54.27  ? 205 ASP   D O     1 
ATOM   8496  C  CB    . ASP   C 2  203 ? 14.222  -13.073 -28.764 1.00 56.39  ? 205 ASP   D CB    1 
ATOM   8497  C  CG    . ASP   C 2  203 ? 14.833  -14.477 -28.504 1.00 55.71  ? 205 ASP   D CG    1 
ATOM   8498  O  OD1   . ASP   C 2  203 ? 15.222  -15.184 -29.463 1.00 58.88  ? 205 ASP   D OD1   1 
ATOM   8499  O  OD2   . ASP   C 2  203 ? 14.901  -14.886 -27.320 1.00 43.03  ? 205 ASP   D OD2   1 
ATOM   8500  N  N     . ASN   C 2  204 ? 14.388  -13.576 -32.232 1.00 58.58  ? 206 ASN   D N     1 
ATOM   8501  C  CA    . ASN   C 2  204 ? 13.580  -14.199 -33.271 1.00 61.60  ? 206 ASN   D CA    1 
ATOM   8502  C  C     . ASN   C 2  204 ? 12.749  -15.341 -32.708 1.00 61.43  ? 206 ASN   D C     1 
ATOM   8503  O  O     . ASN   C 2  204 ? 11.655  -15.612 -33.219 1.00 56.10  ? 206 ASN   D O     1 
ATOM   8504  C  CB    . ASN   C 2  204 ? 14.468  -14.670 -34.418 1.00 49.78  ? 206 ASN   D CB    1 
ATOM   8505  C  CG    . ASN   C 2  204 ? 14.750  -13.574 -35.389 1.00 46.13  ? 206 ASN   D CG    1 
ATOM   8506  O  OD1   . ASN   C 2  204 ? 14.586  -12.408 -35.073 1.00 55.00  ? 206 ASN   D OD1   1 
ATOM   8507  N  ND2   . ASN   C 2  204 ? 15.148  -13.932 -36.586 1.00 59.89  ? 206 ASN   D ND2   1 
ATOM   8508  N  N     . GLU   C 2  205 ? 13.238  -16.002 -31.651 1.00 58.62  ? 207 GLU   D N     1 
ATOM   8509  C  CA    . GLU   C 2  205 ? 12.411  -16.968 -30.934 1.00 61.51  ? 207 GLU   D CA    1 
ATOM   8510  C  C     . GLU   C 2  205 ? 11.098  -16.328 -30.519 1.00 55.46  ? 207 GLU   D C     1 
ATOM   8511  O  O     . GLU   C 2  205 ? 10.021  -16.896 -30.721 1.00 60.74  ? 207 GLU   D O     1 
ATOM   8512  C  CB    . GLU   C 2  205 ? 13.148  -17.514 -29.707 1.00 53.94  ? 207 GLU   D CB    1 
ATOM   8513  C  CG    . GLU   C 2  205 ? 12.298  -18.468 -28.859 1.00 57.28  ? 207 GLU   D CG    1 
ATOM   8514  C  CD    . GLU   C 2  205 ? 12.743  -19.919 -28.943 1.00 62.47  ? 207 GLU   D CD    1 
ATOM   8515  O  OE1   . GLU   C 2  205 ? 13.493  -20.278 -29.886 1.00 58.63  ? 207 GLU   D OE1   1 
ATOM   8516  O  OE2   . GLU   C 2  205 ? 12.334  -20.704 -28.057 1.00 67.01  ? 207 GLU   D OE2   1 
ATOM   8517  N  N     . ALA   C 2  206 ? 11.170  -15.134 -29.943 1.00 51.01  ? 208 ALA   D N     1 
ATOM   8518  C  CA    . ALA   C 2  206 ? 9.949   -14.428 -29.595 1.00 54.24  ? 208 ALA   D CA    1 
ATOM   8519  C  C     . ALA   C 2  206 ? 9.209   -13.960 -30.848 1.00 57.98  ? 208 ALA   D C     1 
ATOM   8520  O  O     . ALA   C 2  206 ? 7.981   -14.089 -30.935 1.00 56.89  ? 208 ALA   D O     1 
ATOM   8521  C  CB    . ALA   C 2  206 ? 10.276  -13.260 -28.662 1.00 50.41  ? 208 ALA   D CB    1 
ATOM   8522  N  N     . LEU   C 2  207 ? 9.935   -13.432 -31.839 1.00 59.85  ? 209 LEU   D N     1 
ATOM   8523  C  CA    . LEU   C 2  207 ? 9.279   -12.917 -33.041 1.00 57.49  ? 209 LEU   D CA    1 
ATOM   8524  C  C     . LEU   C 2  207 ? 8.441   -13.990 -33.722 1.00 66.10  ? 209 LEU   D C     1 
ATOM   8525  O  O     . LEU   C 2  207 ? 7.335   -13.717 -34.207 1.00 65.38  ? 209 LEU   D O     1 
ATOM   8526  C  CB    . LEU   C 2  207 ? 10.323  -12.381 -34.005 1.00 54.83  ? 209 LEU   D CB    1 
ATOM   8527  C  CG    . LEU   C 2  207 ? 10.771  -10.964 -33.738 1.00 53.34  ? 209 LEU   D CG    1 
ATOM   8528  C  CD1   . LEU   C 2  207 ? 12.141  -10.847 -34.290 1.00 48.87  ? 209 LEU   D CD1   1 
ATOM   8529  C  CD2   . LEU   C 2  207 ? 9.826   -9.984  -34.411 1.00 53.48  ? 209 LEU   D CD2   1 
ATOM   8530  N  N     . TYR   C 2  208 ? 8.974   -15.211 -33.796 1.00 67.38  ? 210 TYR   D N     1 
ATOM   8531  C  CA    . TYR   C 2  208 ? 8.277   -16.376 -34.323 1.00 61.61  ? 210 TYR   D CA    1 
ATOM   8532  C  C     . TYR   C 2  208 ? 7.043   -16.647 -33.476 1.00 66.15  ? 210 TYR   D C     1 
ATOM   8533  O  O     . TYR   C 2  208 ? 5.917   -16.355 -33.894 1.00 64.99  ? 210 TYR   D O     1 
ATOM   8534  C  CB    . TYR   C 2  208 ? 9.236   -17.570 -34.322 1.00 66.48  ? 210 TYR   D CB    1 
ATOM   8535  C  CG    . TYR   C 2  208 ? 8.715   -18.864 -34.881 1.00 71.82  ? 210 TYR   D CG    1 
ATOM   8536  C  CD1   . TYR   C 2  208 ? 7.729   -19.586 -34.222 1.00 74.51  ? 210 TYR   D CD1   1 
ATOM   8537  C  CD2   . TYR   C 2  208 ? 9.252   -19.397 -36.044 1.00 74.59  ? 210 TYR   D CD2   1 
ATOM   8538  C  CE1   . TYR   C 2  208 ? 7.264   -20.788 -34.728 1.00 83.55  ? 210 TYR   D CE1   1 
ATOM   8539  C  CE2   . TYR   C 2  208 ? 8.798   -20.601 -36.559 1.00 79.93  ? 210 TYR   D CE2   1 
ATOM   8540  C  CZ    . TYR   C 2  208 ? 7.806   -21.294 -35.899 1.00 85.25  ? 210 TYR   D CZ    1 
ATOM   8541  O  OH    . TYR   C 2  208 ? 7.357   -22.492 -36.411 1.00 76.05  ? 210 TYR   D OH    1 
ATOM   8542  N  N     . ASP   C 2  209 ? 7.261   -17.174 -32.266 1.00 67.99  ? 211 ASP   D N     1 
ATOM   8543  C  CA    . ASP   C 2  209 ? 6.200   -17.557 -31.341 1.00 59.88  ? 211 ASP   D CA    1 
ATOM   8544  C  C     . ASP   C 2  209 ? 5.058   -16.548 -31.345 1.00 59.91  ? 211 ASP   D C     1 
ATOM   8545  O  O     . ASP   C 2  209 ? 3.885   -16.928 -31.259 1.00 65.72  ? 211 ASP   D O     1 
ATOM   8546  C  CB    . ASP   C 2  209 ? 6.772   -17.727 -29.932 1.00 52.36  ? 211 ASP   D CB    1 
ATOM   8547  C  CG    . ASP   C 2  209 ? 7.678   -18.939 -29.817 1.00 68.52  ? 211 ASP   D CG    1 
ATOM   8548  O  OD1   . ASP   C 2  209 ? 7.836   -19.627 -30.848 1.00 68.89  ? 211 ASP   D OD1   1 
ATOM   8549  O  OD2   . ASP   C 2  209 ? 8.224   -19.213 -28.713 1.00 69.51  ? 211 ASP   D OD2   1 
ATOM   8550  N  N     . ILE   C 2  210 ? 5.383   -15.262 -31.456 1.00 55.33  ? 212 ILE   D N     1 
ATOM   8551  C  CA    . ILE   C 2  210 ? 4.340   -14.242 -31.507 1.00 59.45  ? 212 ILE   D CA    1 
ATOM   8552  C  C     . ILE   C 2  210 ? 3.640   -14.273 -32.858 1.00 64.61  ? 212 ILE   D C     1 
ATOM   8553  O  O     . ILE   C 2  210 ? 2.408   -14.218 -32.940 1.00 70.66  ? 212 ILE   D O     1 
ATOM   8554  C  CB    . ILE   C 2  210 ? 4.925   -12.850 -31.204 1.00 62.69  ? 212 ILE   D CB    1 
ATOM   8555  C  CG1   . ILE   C 2  210 ? 5.512   -12.798 -29.776 1.00 72.84  ? 212 ILE   D CG1   1 
ATOM   8556  C  CG2   . ILE   C 2  210 ? 3.881   -11.758 -31.458 1.00 52.30  ? 212 ILE   D CG2   1 
ATOM   8557  C  CD1   . ILE   C 2  210 ? 4.733   -13.621 -28.698 1.00 66.00  ? 212 ILE   D CD1   1 
ATOM   8558  N  N     . CYS   C 2  211 ? 4.418   -14.372 -33.937 1.00 70.33  ? 213 CYS   D N     1 
ATOM   8559  C  CA    . CYS   C 2  211 ? 3.847   -14.486 -35.276 1.00 66.62  ? 213 CYS   D CA    1 
ATOM   8560  C  C     . CYS   C 2  211 ? 2.999   -15.749 -35.411 1.00 70.01  ? 213 CYS   D C     1 
ATOM   8561  O  O     . CYS   C 2  211 ? 1.793   -15.688 -35.687 1.00 67.15  ? 213 CYS   D O     1 
ATOM   8562  C  CB    . CYS   C 2  211 ? 4.974   -14.479 -36.307 1.00 56.29  ? 213 CYS   D CB    1 
ATOM   8563  S  SG    . CYS   C 2  211 ? 5.634   -12.855 -36.623 1.00 74.09  ? 213 CYS   D SG    1 
ATOM   8564  N  N     . PHE   C 2  212 ? 3.628   -16.910 -35.216 1.00 64.41  ? 214 PHE   D N     1 
ATOM   8565  C  CA    . PHE   C 2  212 ? 3.017   -18.229 -35.330 1.00 67.57  ? 214 PHE   D CA    1 
ATOM   8566  C  C     . PHE   C 2  212 ? 1.714   -18.310 -34.553 1.00 77.55  ? 214 PHE   D C     1 
ATOM   8567  O  O     . PHE   C 2  212 ? 0.622   -18.386 -35.128 1.00 77.84  ? 214 PHE   D O     1 
ATOM   8568  C  CB    . PHE   C 2  212 ? 3.986   -19.288 -34.799 1.00 76.00  ? 214 PHE   D CB    1 
ATOM   8569  C  CG    . PHE   C 2  212 ? 3.558   -20.708 -35.070 1.00 95.01  ? 214 PHE   D CG    1 
ATOM   8570  C  CD1   . PHE   C 2  212 ? 2.758   -21.008 -36.166 1.00 91.60  ? 214 PHE   D CD1   1 
ATOM   8571  C  CD2   . PHE   C 2  212 ? 3.963   -21.749 -34.232 1.00 88.84  ? 214 PHE   D CD2   1 
ATOM   8572  C  CE1   . PHE   C 2  212 ? 2.371   -22.310 -36.424 1.00 89.45  ? 214 PHE   D CE1   1 
ATOM   8573  C  CE2   . PHE   C 2  212 ? 3.574   -23.063 -34.487 1.00 74.01  ? 214 PHE   D CE2   1 
ATOM   8574  C  CZ    . PHE   C 2  212 ? 2.778   -23.339 -35.582 1.00 78.26  ? 214 PHE   D CZ    1 
ATOM   8575  N  N     . ARG   C 2  213 ? 1.848   -18.304 -33.228 1.00 81.45  ? 215 ARG   D N     1 
ATOM   8576  C  CA    . ARG   C 2  213 ? 0.737   -18.389 -32.297 1.00 73.68  ? 215 ARG   D CA    1 
ATOM   8577  C  C     . ARG   C 2  213 ? -0.047  -17.086 -32.250 1.00 73.25  ? 215 ARG   D C     1 
ATOM   8578  O  O     . ARG   C 2  213 ? -1.033  -16.930 -32.977 1.00 81.51  ? 215 ARG   D O     1 
ATOM   8579  C  CB    . ARG   C 2  213 ? 1.250   -18.750 -30.905 1.00 71.46  ? 215 ARG   D CB    1 
ATOM   8580  C  CG    . ARG   C 2  213 ? 2.163   -19.960 -30.881 1.00 75.99  ? 215 ARG   D CG    1 
ATOM   8581  C  CD    . ARG   C 2  213 ? 2.719   -20.126 -29.494 1.00 77.48  ? 215 ARG   D CD    1 
ATOM   8582  N  NE    . ARG   C 2  213 ? 3.072   -18.825 -28.938 1.00 88.71  ? 215 ARG   D NE    1 
ATOM   8583  C  CZ    . ARG   C 2  213 ? 3.779   -18.645 -27.830 1.00 89.63  ? 215 ARG   D CZ    1 
ATOM   8584  N  NH1   . ARG   C 2  213 ? 4.231   -19.671 -27.125 1.00 85.82  ? 215 ARG   D NH1   1 
ATOM   8585  N  NH2   . ARG   C 2  213 ? 4.045   -17.402 -27.423 1.00 80.47  ? 215 ARG   D NH2   1 
ATOM   8586  N  N     . THR   C 2  214 ? 0.381   -16.141 -31.409 1.00 69.62  ? 216 THR   D N     1 
ATOM   8587  C  CA    . THR   C 2  214 ? -0.496  -15.021 -31.075 1.00 75.37  ? 216 THR   D CA    1 
ATOM   8588  C  C     . THR   C 2  214 ? -1.031  -14.322 -32.323 1.00 69.72  ? 216 THR   D C     1 
ATOM   8589  O  O     . THR   C 2  214 ? -2.178  -13.864 -32.342 1.00 72.06  ? 216 THR   D O     1 
ATOM   8590  C  CB    . THR   C 2  214 ? 0.225   -14.026 -30.163 1.00 69.18  ? 216 THR   D CB    1 
ATOM   8591  O  OG1   . THR   C 2  214 ? 0.597   -14.671 -28.934 1.00 69.32  ? 216 THR   D OG1   1 
ATOM   8592  C  CG2   . THR   C 2  214 ? -0.694  -12.864 -29.845 1.00 68.95  ? 216 THR   D CG2   1 
ATOM   8593  N  N     . LEU   C 2  215 ? -0.234  -14.255 -33.385 1.00 71.22  ? 217 LEU   D N     1 
ATOM   8594  C  CA    . LEU   C 2  215 ? -0.651  -13.571 -34.601 1.00 68.83  ? 217 LEU   D CA    1 
ATOM   8595  C  C     . LEU   C 2  215 ? -1.239  -14.511 -35.646 1.00 77.11  ? 217 LEU   D C     1 
ATOM   8596  O  O     . LEU   C 2  215 ? -1.594  -14.057 -36.741 1.00 77.78  ? 217 LEU   D O     1 
ATOM   8597  C  CB    . LEU   C 2  215 ? 0.525   -12.798 -35.196 1.00 71.38  ? 217 LEU   D CB    1 
ATOM   8598  C  CG    . LEU   C 2  215 ? 0.496   -11.284 -34.976 1.00 66.99  ? 217 LEU   D CG    1 
ATOM   8599  C  CD1   . LEU   C 2  215 ? 1.812   -10.683 -35.432 1.00 75.33  ? 217 LEU   D CD1   1 
ATOM   8600  C  CD2   . LEU   C 2  215 ? -0.680  -10.640 -35.709 1.00 52.61  ? 217 LEU   D CD2   1 
ATOM   8601  N  N     . LYS   C 2  216 ? -1.368  -15.801 -35.335 1.00 80.41  ? 218 LYS   D N     1 
ATOM   8602  C  CA    . LYS   C 2  216 ? -2.043  -16.759 -36.211 1.00 82.51  ? 218 LYS   D CA    1 
ATOM   8603  C  C     . LYS   C 2  216 ? -1.449  -16.701 -37.610 1.00 80.11  ? 218 LYS   D C     1 
ATOM   8604  O  O     . LYS   C 2  216 ? -2.143  -16.475 -38.604 1.00 74.10  ? 218 LYS   D O     1 
ATOM   8605  C  CB    . LYS   C 2  216 ? -3.559  -16.515 -36.258 1.00 86.32  ? 218 LYS   D CB    1 
ATOM   8606  C  CG    . LYS   C 2  216 ? -4.236  -16.219 -34.912 1.00 78.20  ? 218 LYS   D CG    1 
ATOM   8607  C  CD    . LYS   C 2  216 ? -3.848  -17.223 -33.835 1.00 74.20  ? 218 LYS   D CD    1 
ATOM   8608  C  CE    . LYS   C 2  216 ? -4.092  -18.646 -34.285 1.00 70.53  ? 218 LYS   D CE    1 
ATOM   8609  N  NZ    . LYS   C 2  216 ? -3.760  -19.599 -33.201 1.00 77.61  ? 218 LYS   D NZ    1 
ATOM   8610  N  N     . LEU   C 2  217 ? -0.134  -16.861 -37.670 1.00 85.44  ? 219 LEU   D N     1 
ATOM   8611  C  CA    . LEU   C 2  217 ? 0.594   -16.903 -38.929 1.00 80.07  ? 219 LEU   D CA    1 
ATOM   8612  C  C     . LEU   C 2  217 ? 1.365   -18.208 -38.918 1.00 75.60  ? 219 LEU   D C     1 
ATOM   8613  O  O     . LEU   C 2  217 ? 2.502   -18.274 -38.450 1.00 74.37  ? 219 LEU   D O     1 
ATOM   8614  C  CB    . LEU   C 2  217 ? 1.531   -15.714 -39.115 1.00 81.68  ? 219 LEU   D CB    1 
ATOM   8615  C  CG    . LEU   C 2  217 ? 0.927   -14.316 -39.213 1.00 74.85  ? 219 LEU   D CG    1 
ATOM   8616  C  CD1   . LEU   C 2  217 ? 1.990   -13.353 -39.737 1.00 68.96  ? 219 LEU   D CD1   1 
ATOM   8617  C  CD2   . LEU   C 2  217 ? -0.326  -14.331 -40.083 1.00 66.63  ? 219 LEU   D CD2   1 
ATOM   8618  N  N     . THR   C 2  218 ? 0.738   -19.258 -39.420 1.00 87.29  ? 220 THR   D N     1 
ATOM   8619  C  CA    . THR   C 2  218 ? 1.519   -20.412 -39.820 1.00 84.03  ? 220 THR   D CA    1 
ATOM   8620  C  C     . THR   C 2  218 ? 2.542   -19.970 -40.859 1.00 78.46  ? 220 THR   D C     1 
ATOM   8621  O  O     . THR   C 2  218 ? 2.234   -19.180 -41.756 1.00 84.24  ? 220 THR   D O     1 
ATOM   8622  C  CB    . THR   C 2  218 ? 0.614   -21.493 -40.389 1.00 78.13  ? 220 THR   D CB    1 
ATOM   8623  O  OG1   . THR   C 2  218 ? 1.330   -22.734 -40.418 1.00 74.83  ? 220 THR   D OG1   1 
ATOM   8624  C  CG2   . THR   C 2  218 ? 0.170   -21.107 -41.793 1.00 75.25  ? 220 THR   D CG2   1 
ATOM   8625  N  N     . THR   C 2  219 ? 3.771   -20.473 -40.717 1.00 71.49  ? 221 THR   D N     1 
ATOM   8626  C  CA    . THR   C 2  219 ? 4.968   -20.101 -41.478 1.00 73.19  ? 221 THR   D CA    1 
ATOM   8627  C  C     . THR   C 2  219 ? 5.209   -18.591 -41.502 1.00 82.47  ? 221 THR   D C     1 
ATOM   8628  O  O     . THR   C 2  219 ? 4.892   -17.911 -42.494 1.00 69.87  ? 221 THR   D O     1 
ATOM   8629  C  CB    . THR   C 2  219 ? 4.932   -20.645 -42.909 1.00 61.13  ? 221 THR   D CB    1 
ATOM   8630  O  OG1   . THR   C 2  219 ? 6.168   -20.311 -43.540 1.00 67.64  ? 221 THR   D OG1   1 
ATOM   8631  C  CG2   . THR   C 2  219 ? 3.794   -20.059 -43.739 1.00 64.87  ? 221 THR   D CG2   1 
ATOM   8632  N  N     . PRO   C 2  220 ? 5.792   -18.038 -40.432 1.00 80.48  ? 222 PRO   D N     1 
ATOM   8633  C  CA    . PRO   C 2  220 ? 6.102   -16.603 -40.422 1.00 73.83  ? 222 PRO   D CA    1 
ATOM   8634  C  C     . PRO   C 2  220 ? 7.198   -16.248 -41.428 1.00 71.16  ? 222 PRO   D C     1 
ATOM   8635  O  O     . PRO   C 2  220 ? 8.214   -16.939 -41.535 1.00 73.06  ? 222 PRO   D O     1 
ATOM   8636  C  CB    . PRO   C 2  220 ? 6.552   -16.355 -38.972 1.00 70.73  ? 222 PRO   D CB    1 
ATOM   8637  C  CG    . PRO   C 2  220 ? 6.901   -17.723 -38.400 1.00 52.29  ? 222 PRO   D CG    1 
ATOM   8638  C  CD    . PRO   C 2  220 ? 6.034   -18.685 -39.123 1.00 64.50  ? 222 PRO   D CD    1 
ATOM   8639  N  N     . THR   C 2  221 ? 6.987   -15.151 -42.167 1.00 66.19  ? 223 THR   D N     1 
ATOM   8640  C  CA    . THR   C 2  221 ? 7.982   -14.637 -43.111 1.00 66.31  ? 223 THR   D CA    1 
ATOM   8641  C  C     . THR   C 2  221 ? 8.835   -13.537 -42.479 1.00 72.53  ? 223 THR   D C     1 
ATOM   8642  O  O     . THR   C 2  221 ? 8.322   -12.703 -41.727 1.00 70.72  ? 223 THR   D O     1 
ATOM   8643  C  CB    . THR   C 2  221 ? 7.302   -14.085 -44.368 1.00 62.54  ? 223 THR   D CB    1 
ATOM   8644  O  OG1   . THR   C 2  221 ? 8.255   -13.350 -45.146 1.00 73.54  ? 223 THR   D OG1   1 
ATOM   8645  C  CG2   . THR   C 2  221 ? 6.137   -13.169 -44.002 1.00 69.24  ? 223 THR   D CG2   1 
ATOM   8646  N  N     . TYR   C 2  222 ? 10.138  -13.519 -42.812 1.00 72.00  ? 224 TYR   D N     1 
ATOM   8647  C  CA    . TYR   C 2  222 ? 11.039  -12.499 -42.261 1.00 58.85  ? 224 TYR   D CA    1 
ATOM   8648  C  C     . TYR   C 2  222 ? 10.405  -11.119 -42.314 1.00 60.73  ? 224 TYR   D C     1 
ATOM   8649  O  O     . TYR   C 2  222 ? 10.404  -10.383 -41.322 1.00 76.55  ? 224 TYR   D O     1 
ATOM   8650  C  CB    . TYR   C 2  222 ? 12.381  -12.470 -42.995 1.00 49.68  ? 224 TYR   D CB    1 
ATOM   8651  C  CG    . TYR   C 2  222 ? 13.393  -13.464 -42.480 1.00 51.92  ? 224 TYR   D CG    1 
ATOM   8652  C  CD1   . TYR   C 2  222 ? 13.643  -13.610 -41.127 1.00 52.73  ? 224 TYR   D CD1   1 
ATOM   8653  C  CD2   . TYR   C 2  222 ? 14.085  -14.275 -43.357 1.00 53.41  ? 224 TYR   D CD2   1 
ATOM   8654  C  CE1   . TYR   C 2  222 ? 14.580  -14.529 -40.674 1.00 56.90  ? 224 TYR   D CE1   1 
ATOM   8655  C  CE2   . TYR   C 2  222 ? 15.005  -15.188 -42.917 1.00 46.77  ? 224 TYR   D CE2   1 
ATOM   8656  C  CZ    . TYR   C 2  222 ? 15.254  -15.321 -41.586 1.00 53.86  ? 224 TYR   D CZ    1 
ATOM   8657  O  OH    . TYR   C 2  222 ? 16.188  -16.257 -41.194 1.00 48.27  ? 224 TYR   D OH    1 
ATOM   8658  N  N     . GLY   C 2  223 ? 9.865   -10.742 -43.460 1.00 52.20  ? 225 GLY   D N     1 
ATOM   8659  C  CA    . GLY   C 2  223 ? 9.134   -9.493  -43.506 1.00 55.82  ? 225 GLY   D CA    1 
ATOM   8660  C  C     . GLY   C 2  223 ? 8.076   -9.422  -42.427 1.00 60.59  ? 225 GLY   D C     1 
ATOM   8661  O  O     . GLY   C 2  223 ? 7.770   -8.339  -41.923 1.00 63.66  ? 225 GLY   D O     1 
ATOM   8662  N  N     . ASP   C 2  224 ? 7.514   -10.575 -42.044 1.00 56.54  ? 226 ASP   D N     1 
ATOM   8663  C  CA    . ASP   C 2  224 ? 6.559   -10.613 -40.937 1.00 69.23  ? 226 ASP   D CA    1 
ATOM   8664  C  C     . ASP   C 2  224 ? 7.257   -10.442 -39.589 1.00 65.98  ? 226 ASP   D C     1 
ATOM   8665  O  O     . ASP   C 2  224 ? 6.920   -9.525  -38.824 1.00 58.86  ? 226 ASP   D O     1 
ATOM   8666  C  CB    . ASP   C 2  224 ? 5.764   -11.920 -40.964 1.00 77.62  ? 226 ASP   D CB    1 
ATOM   8667  C  CG    . ASP   C 2  224 ? 4.436   -11.780 -41.679 1.00 79.33  ? 226 ASP   D CG    1 
ATOM   8668  O  OD1   . ASP   C 2  224 ? 3.930   -10.636 -41.815 1.00 85.04  ? 226 ASP   D OD1   1 
ATOM   8669  O  OD2   . ASP   C 2  224 ? 3.897   -12.832 -42.083 1.00 74.18  ? 226 ASP   D OD2   1 
ATOM   8670  N  N     . LEU   C 2  225 ? 8.225   -11.330 -39.271 1.00 59.09  ? 227 LEU   D N     1 
ATOM   8671  C  CA    . LEU   C 2  225 ? 9.077   -11.113 -38.103 1.00 60.07  ? 227 LEU   D CA    1 
ATOM   8672  C  C     . LEU   C 2  225 ? 9.556   -9.674  -38.115 1.00 65.51  ? 227 LEU   D C     1 
ATOM   8673  O  O     . LEU   C 2  225 ? 9.792   -9.048  -37.098 1.00 67.59  ? 227 LEU   D O     1 
ATOM   8674  C  CB    . LEU   C 2  225 ? 10.282  -12.053 -38.115 1.00 56.70  ? 227 LEU   D CB    1 
ATOM   8675  C  CG    . LEU   C 2  225 ? 9.933   -13.538 -38.137 1.00 64.76  ? 227 LEU   D CG    1 
ATOM   8676  C  CD1   . LEU   C 2  225 ? 11.107  -14.410 -37.655 1.00 54.53  ? 227 LEU   D CD1   1 
ATOM   8677  C  CD2   . LEU   C 2  225 ? 8.672   -13.832 -37.337 1.00 59.01  ? 227 LEU   D CD2   1 
ATOM   8678  N  N     . ASN   C 2  226 ? 9.615   -9.092  -39.240 1.00 64.49  ? 228 ASN   D N     1 
ATOM   8679  C  CA    . ASN   C 2  226 ? 10.349  -7.819  -39.201 1.00 57.82  ? 228 ASN   D CA    1 
ATOM   8680  C  C     . ASN   C 2  226 ? 9.385   -6.714  -39.363 1.00 60.32  ? 228 ASN   D C     1 
ATOM   8681  O  O     . ASN   C 2  226 ? 9.739   -5.569  -39.720 1.00 66.05  ? 228 ASN   D O     1 
ATOM   8682  C  CB    . ASN   C 2  226 ? 11.505  -7.476  -40.256 1.00 53.77  ? 228 ASN   D CB    1 
ATOM   8683  C  CG    . ASN   C 2  226 ? 12.791  -8.029  -39.863 1.00 59.34  ? 228 ASN   D CG    1 
ATOM   8684  O  OD1   . ASN   C 2  226 ? 13.416  -9.163  -40.371 1.00 58.19  ? 228 ASN   D OD1   1 
ATOM   8685  N  ND2   . ASN   C 2  226 ? 13.447  -7.154  -39.093 1.00 85.40  ? 228 ASN   D ND2   1 
ATOM   8686  N  N     . HIS   C 2  227 ? 8.108   -7.019  -39.373 1.00 59.72  ? 229 HIS   D N     1 
ATOM   8687  C  CA    . HIS   C 2  227 ? 7.105   -6.035  -39.004 1.00 61.27  ? 229 HIS   D CA    1 
ATOM   8688  C  C     . HIS   C 2  227 ? 7.033   -5.796  -37.506 1.00 57.06  ? 229 HIS   D C     1 
ATOM   8689  O  O     . HIS   C 2  227 ? 6.671   -4.693  -37.074 1.00 52.23  ? 229 HIS   D O     1 
ATOM   8690  C  CB    . HIS   C 2  227 ? 5.741   -6.503  -39.482 1.00 64.38  ? 229 HIS   D CB    1 
ATOM   8691  C  CG    . HIS   C 2  227 ? 4.762   -5.438  -39.508 1.00 67.05  ? 229 HIS   D CG    1 
ATOM   8692  N  ND1   . HIS   C 2  227 ? 4.943   -4.308  -40.270 1.00 71.93  ? 229 HIS   D ND1   1 
ATOM   8693  C  CD2   . HIS   C 2  227 ? 3.628   -5.283  -38.810 1.00 58.16  ? 229 HIS   D CD2   1 
ATOM   8694  C  CE1   . HIS   C 2  227 ? 3.916   -3.513  -40.074 1.00 76.87  ? 229 HIS   D CE1   1 
ATOM   8695  N  NE2   . HIS   C 2  227 ? 3.107   -4.082  -39.194 1.00 79.87  ? 229 HIS   D NE2   1 
ATOM   8696  N  N     . LEU   C 2  228 ? 7.351   -6.808  -36.701 1.00 61.00  ? 230 LEU   D N     1 
ATOM   8697  C  CA    . LEU   C 2  228 ? 7.446   -6.575  -35.266 1.00 57.50  ? 230 LEU   D CA    1 
ATOM   8698  C  C     . LEU   C 2  228 ? 8.677   -5.725  -34.945 1.00 59.19  ? 230 LEU   D C     1 
ATOM   8699  O  O     . LEU   C 2  228 ? 8.621   -4.848  -34.075 1.00 61.88  ? 230 LEU   D O     1 
ATOM   8700  C  CB    . LEU   C 2  228 ? 7.462   -7.908  -34.489 1.00 54.95  ? 230 LEU   D CB    1 
ATOM   8701  C  CG    . LEU   C 2  228 ? 6.348   -8.972  -34.633 1.00 52.15  ? 230 LEU   D CG    1 
ATOM   8702  C  CD1   . LEU   C 2  228 ? 6.643   -10.225 -33.794 1.00 47.80  ? 230 LEU   D CD1   1 
ATOM   8703  C  CD2   . LEU   C 2  228 ? 4.952   -8.451  -34.308 1.00 48.07  ? 230 LEU   D CD2   1 
ATOM   8704  N  N     . VAL   C 2  229 ? 9.793   -5.949  -35.654 1.00 58.88  ? 231 VAL   D N     1 
ATOM   8705  C  CA    . VAL   C 2  229 ? 11.009  -5.196  -35.355 1.00 48.95  ? 231 VAL   D CA    1 
ATOM   8706  C  C     . VAL   C 2  229 ? 10.838  -3.727  -35.718 1.00 49.41  ? 231 VAL   D C     1 
ATOM   8707  O  O     . VAL   C 2  229 ? 11.507  -2.863  -35.140 1.00 43.17  ? 231 VAL   D O     1 
ATOM   8708  C  CB    . VAL   C 2  229 ? 12.242  -5.801  -36.061 1.00 45.68  ? 231 VAL   D CB    1 
ATOM   8709  C  CG1   . VAL   C 2  229 ? 13.468  -4.925  -35.830 1.00 44.32  ? 231 VAL   D CG1   1 
ATOM   8710  C  CG2   . VAL   C 2  229 ? 12.530  -7.216  -35.575 1.00 35.68  ? 231 VAL   D CG2   1 
ATOM   8711  N  N     . SER   C 2  230 ? 9.945   -3.409  -36.662 1.00 49.18  ? 232 SER   D N     1 
ATOM   8712  C  CA    . SER   C 2  230 ? 9.773   -2.018  -37.073 1.00 53.51  ? 232 SER   D CA    1 
ATOM   8713  C  C     . SER   C 2  230 ? 8.816   -1.245  -36.164 1.00 61.64  ? 232 SER   D C     1 
ATOM   8714  O  O     . SER   C 2  230 ? 8.924   -0.014  -36.075 1.00 60.99  ? 232 SER   D O     1 
ATOM   8715  C  CB    . SER   C 2  230 ? 9.325   -1.946  -38.546 1.00 52.67  ? 232 SER   D CB    1 
ATOM   8716  O  OG    . SER   C 2  230 ? 7.914   -1.890  -38.726 1.00 63.93  ? 232 SER   D OG    1 
ATOM   8717  N  N     . ALA   C 2  231 ? 7.909   -1.934  -35.463 1.00 58.06  ? 233 ALA   D N     1 
ATOM   8718  C  CA    . ALA   C 2  231 ? 7.037   -1.266  -34.498 1.00 56.52  ? 233 ALA   D CA    1 
ATOM   8719  C  C     . ALA   C 2  231 ? 7.765   -0.993  -33.188 1.00 53.20  ? 233 ALA   D C     1 
ATOM   8720  O  O     . ALA   C 2  231 ? 7.651   0.099   -32.615 1.00 49.82  ? 233 ALA   D O     1 
ATOM   8721  C  CB    . ALA   C 2  231 ? 5.793   -2.114  -34.238 1.00 55.58  ? 233 ALA   D CB    1 
ATOM   8722  N  N     . THR   C 2  232 ? 8.516   -1.986  -32.713 1.00 45.36  ? 234 THR   D N     1 
ATOM   8723  C  CA    . THR   C 2  232 ? 9.348   -1.805  -31.533 1.00 44.37  ? 234 THR   D CA    1 
ATOM   8724  C  C     . THR   C 2  232 ? 10.395  -0.716  -31.729 1.00 52.77  ? 234 THR   D C     1 
ATOM   8725  O  O     . THR   C 2  232 ? 10.734  -0.010  -30.774 1.00 61.10  ? 234 THR   D O     1 
ATOM   8726  C  CB    . THR   C 2  232 ? 10.019  -3.124  -31.186 1.00 45.68  ? 234 THR   D CB    1 
ATOM   8727  O  OG1   . THR   C 2  232 ? 9.089   -4.191  -31.422 1.00 50.13  ? 234 THR   D OG1   1 
ATOM   8728  C  CG2   . THR   C 2  232 ? 10.466  -3.136  -29.731 1.00 51.45  ? 234 THR   D CG2   1 
ATOM   8729  N  N     . MET   C 2  233 ? 10.909  -0.552  -32.954 1.00 55.21  ? 235 MET   D N     1 
ATOM   8730  C  CA    . MET   C 2  233 ? 11.944  0.453   -33.193 1.00 42.31  ? 235 MET   D CA    1 
ATOM   8731  C  C     . MET   C 2  233 ? 11.377  1.863   -33.170 1.00 43.59  ? 235 MET   D C     1 
ATOM   8732  O  O     . MET   C 2  233 ? 11.996  2.782   -32.617 1.00 46.02  ? 235 MET   D O     1 
ATOM   8733  C  CB    . MET   C 2  233 ? 12.642  0.204   -34.522 1.00 45.03  ? 235 MET   D CB    1 
ATOM   8734  C  CG    . MET   C 2  233 ? 13.966  -0.488  -34.367 1.00 48.87  ? 235 MET   D CG    1 
ATOM   8735  S  SD    . MET   C 2  233 ? 14.831  -0.783  -35.914 1.00 48.89  ? 235 MET   D SD    1 
ATOM   8736  C  CE    . MET   C 2  233 ? 15.458  -2.424  -35.506 1.00 39.76  ? 235 MET   D CE    1 
ATOM   8737  N  N     . SER   C 2  234 ? 10.214  2.070   -33.785 1.00 44.73  ? 236 SER   D N     1 
ATOM   8738  C  CA    . SER   C 2  234 ? 9.582   3.375   -33.664 1.00 44.42  ? 236 SER   D CA    1 
ATOM   8739  C  C     . SER   C 2  234 ? 9.248   3.676   -32.209 1.00 49.22  ? 236 SER   D C     1 
ATOM   8740  O  O     . SER   C 2  234 ? 9.298   4.839   -31.781 1.00 43.77  ? 236 SER   D O     1 
ATOM   8741  C  CB    . SER   C 2  234 ? 8.327   3.442   -34.529 1.00 39.94  ? 236 SER   D CB    1 
ATOM   8742  O  OG    . SER   C 2  234 ? 7.793   4.759   -34.535 1.00 46.23  ? 236 SER   D OG    1 
ATOM   8743  N  N     . GLY   C 2  235 ? 8.931   2.639   -31.431 1.00 47.44  ? 237 GLY   D N     1 
ATOM   8744  C  CA    . GLY   C 2  235 ? 8.576   2.799   -30.033 1.00 49.21  ? 237 GLY   D CA    1 
ATOM   8745  C  C     . GLY   C 2  235 ? 9.731   3.296   -29.190 1.00 50.83  ? 237 GLY   D C     1 
ATOM   8746  O  O     . GLY   C 2  235 ? 9.668   4.378   -28.587 1.00 47.89  ? 237 GLY   D O     1 
ATOM   8747  N  N     . VAL   C 2  236 ? 10.814  2.518   -29.162 1.00 43.33  ? 238 VAL   D N     1 
ATOM   8748  C  CA    . VAL   C 2  236 ? 11.954  2.884   -28.339 1.00 43.12  ? 238 VAL   D CA    1 
ATOM   8749  C  C     . VAL   C 2  236 ? 12.662  4.139   -28.822 1.00 41.87  ? 238 VAL   D C     1 
ATOM   8750  O  O     . VAL   C 2  236 ? 13.360  4.776   -28.027 1.00 44.87  ? 238 VAL   D O     1 
ATOM   8751  C  CB    . VAL   C 2  236 ? 12.935  1.717   -28.276 1.00 39.63  ? 238 VAL   D CB    1 
ATOM   8752  C  CG1   . VAL   C 2  236 ? 12.188  0.474   -27.857 1.00 29.09  ? 238 VAL   D CG1   1 
ATOM   8753  C  CG2   . VAL   C 2  236 ? 13.602  1.566   -29.631 1.00 37.40  ? 238 VAL   D CG2   1 
ATOM   8754  N  N     . THR   C 2  237 ? 12.534  4.518   -30.093 1.00 40.28  ? 239 THR   D N     1 
ATOM   8755  C  CA    . THR   C 2  237 ? 13.150  5.774   -30.503 1.00 42.82  ? 239 THR   D CA    1 
ATOM   8756  C  C     . THR   C 2  237 ? 12.201  6.958   -30.411 1.00 46.24  ? 239 THR   D C     1 
ATOM   8757  O  O     . THR   C 2  237 ? 12.618  8.075   -30.739 1.00 43.79  ? 239 THR   D O     1 
ATOM   8758  C  CB    . THR   C 2  237 ? 13.732  5.703   -31.937 1.00 33.69  ? 239 THR   D CB    1 
ATOM   8759  O  OG1   . THR   C 2  237 ? 12.689  5.747   -32.923 1.00 36.00  ? 239 THR   D OG1   1 
ATOM   8760  C  CG2   . THR   C 2  237 ? 14.546  4.457   -32.124 1.00 32.40  ? 239 THR   D CG2   1 
ATOM   8761  N  N     . THR   C 2  238 ? 10.953  6.769   -29.969 1.00 37.71  ? 240 THR   D N     1 
ATOM   8762  C  CA    A THR   C 2  238 ? 10.015  7.888   -29.944 0.00 40.50  ? 240 THR   D CA    1 
ATOM   8763  C  CA    B THR   C 2  238 ? 10.027  7.894   -29.966 1.00 40.24  ? 240 THR   D CA    1 
ATOM   8764  C  C     . THR   C 2  238 ? 10.560  9.036   -29.102 1.00 45.22  ? 240 THR   D C     1 
ATOM   8765  O  O     . THR   C 2  238 ? 10.704  10.168  -29.585 1.00 44.96  ? 240 THR   D O     1 
ATOM   8766  C  CB    A THR   C 2  238 ? 8.652   7.432   -29.420 0.00 43.20  ? 240 THR   D CB    1 
ATOM   8767  C  CB    B THR   C 2  238 ? 8.636   7.438   -29.530 1.00 43.10  ? 240 THR   D CB    1 
ATOM   8768  O  OG1   A THR   C 2  238 ? 8.165   6.351   -30.226 0.00 48.13  ? 240 THR   D OG1   1 
ATOM   8769  O  OG1   B THR   C 2  238 ? 8.147   6.512   -30.501 1.00 50.48  ? 240 THR   D OG1   1 
ATOM   8770  C  CG2   A THR   C 2  238 ? 7.654   8.577   -29.478 0.00 40.62  ? 240 THR   D CG2   1 
ATOM   8771  C  CG2   B THR   C 2  238 ? 7.676   8.588   -29.494 1.00 40.29  ? 240 THR   D CG2   1 
ATOM   8772  N  N     . CYS   C 2  239 ? 10.907  8.756   -27.836 1.00 49.18  ? 241 CYS   D N     1 
ATOM   8773  C  CA    A CYS   C 2  239 ? 11.420  9.804   -26.952 0.61 40.02  ? 241 CYS   D CA    1 
ATOM   8774  C  CA    B CYS   C 2  239 ? 11.419  9.801   -26.950 0.39 40.03  ? 241 CYS   D CA    1 
ATOM   8775  C  C     . CYS   C 2  239 ? 12.610  10.558  -27.545 1.00 42.94  ? 241 CYS   D C     1 
ATOM   8776  O  O     . CYS   C 2  239 ? 12.869  11.704  -27.142 1.00 42.04  ? 241 CYS   D O     1 
ATOM   8777  C  CB    A CYS   C 2  239 ? 11.812  9.208   -25.599 0.61 37.70  ? 241 CYS   D CB    1 
ATOM   8778  C  CB    B CYS   C 2  239 ? 11.798  9.204   -25.584 0.39 37.72  ? 241 CYS   D CB    1 
ATOM   8779  S  SG    A CYS   C 2  239 ? 10.450  8.396   -24.739 0.61 35.69  ? 241 CYS   D SG    1 
ATOM   8780  S  SG    B CYS   C 2  239 ? 12.713  7.626   -25.606 0.39 40.92  ? 241 CYS   D SG    1 
ATOM   8781  N  N     . LEU   C 2  240 ? 13.342  9.955   -28.493 1.00 38.64  ? 242 LEU   D N     1 
ATOM   8782  C  CA    . LEU   C 2  240 ? 14.495  10.625  -29.091 1.00 31.54  ? 242 LEU   D CA    1 
ATOM   8783  C  C     . LEU   C 2  240 ? 14.099  11.541  -30.245 1.00 35.92  ? 242 LEU   D C     1 
ATOM   8784  O  O     . LEU   C 2  240 ? 14.748  12.567  -30.458 1.00 34.70  ? 242 LEU   D O     1 
ATOM   8785  C  CB    . LEU   C 2  240 ? 15.520  9.591   -29.569 1.00 30.47  ? 242 LEU   D CB    1 
ATOM   8786  C  CG    . LEU   C 2  240 ? 15.839  8.426   -28.609 1.00 28.79  ? 242 LEU   D CG    1 
ATOM   8787  C  CD1   . LEU   C 2  240 ? 16.702  7.366   -29.277 1.00 18.32  ? 242 LEU   D CD1   1 
ATOM   8788  C  CD2   . LEU   C 2  240 ? 16.499  8.910   -27.323 1.00 22.26  ? 242 LEU   D CD2   1 
ATOM   8789  N  N     . ARG   C 2  241 ? 13.016  11.216  -30.962 1.00 46.23  ? 243 ARG   D N     1 
ATOM   8790  C  CA    . ARG   C 2  241 ? 12.641  11.884  -32.214 1.00 45.39  ? 243 ARG   D CA    1 
ATOM   8791  C  C     . ARG   C 2  241 ? 11.548  12.931  -32.063 1.00 48.08  ? 243 ARG   D C     1 
ATOM   8792  O  O     . ARG   C 2  241 ? 11.355  13.743  -32.982 1.00 48.16  ? 243 ARG   D O     1 
ATOM   8793  C  CB    . ARG   C 2  241 ? 12.183  10.851  -33.254 1.00 36.27  ? 243 ARG   D CB    1 
ATOM   8794  C  CG    . ARG   C 2  241 ? 13.255  9.830   -33.532 1.00 41.63  ? 243 ARG   D CG    1 
ATOM   8795  C  CD    . ARG   C 2  241 ? 12.839  8.840   -34.567 1.00 47.00  ? 243 ARG   D CD    1 
ATOM   8796  N  NE    . ARG   C 2  241 ? 11.832  7.887   -34.118 1.00 39.92  ? 243 ARG   D NE    1 
ATOM   8797  C  CZ    . ARG   C 2  241 ? 10.548  7.960   -34.442 1.00 41.61  ? 243 ARG   D CZ    1 
ATOM   8798  N  NH1   . ARG   C 2  241 ? 10.055  9.020   -35.062 1.00 42.03  ? 243 ARG   D NH1   1 
ATOM   8799  N  NH2   . ARG   C 2  241 ? 9.745   6.938   -34.153 1.00 39.52  ? 243 ARG   D NH2   1 
ATOM   8800  N  N     . PHE   C 2  242 ? 10.829  12.928  -30.944 1.00 41.29  ? 244 PHE   D N     1 
ATOM   8801  C  CA    . PHE   C 2  242 ? 9.841   13.953  -30.692 1.00 39.46  ? 244 PHE   D CA    1 
ATOM   8802  C  C     . PHE   C 2  242 ? 10.128  14.624  -29.355 1.00 43.08  ? 244 PHE   D C     1 
ATOM   8803  O  O     . PHE   C 2  242 ? 10.677  13.992  -28.446 1.00 45.69  ? 244 PHE   D O     1 
ATOM   8804  C  CB    . PHE   C 2  242 ? 8.427   13.359  -30.691 1.00 51.74  ? 244 PHE   D CB    1 
ATOM   8805  C  CG    . PHE   C 2  242 ? 8.041   12.685  -31.990 1.00 49.90  ? 244 PHE   D CG    1 
ATOM   8806  C  CD1   . PHE   C 2  242 ? 7.563   13.427  -33.057 1.00 44.69  ? 244 PHE   D CD1   1 
ATOM   8807  C  CD2   . PHE   C 2  242 ? 8.140   11.307  -32.131 1.00 45.18  ? 244 PHE   D CD2   1 
ATOM   8808  C  CE1   . PHE   C 2  242 ? 7.199   12.814  -34.231 1.00 43.18  ? 244 PHE   D CE1   1 
ATOM   8809  C  CE2   . PHE   C 2  242 ? 7.777   10.689  -33.311 1.00 47.56  ? 244 PHE   D CE2   1 
ATOM   8810  C  CZ    . PHE   C 2  242 ? 7.307   11.447  -34.364 1.00 43.60  ? 244 PHE   D CZ    1 
ATOM   8811  N  N     . PRO   C 2  243 ? 9.770   15.901  -29.203 1.00 47.81  ? 245 PRO   D N     1 
ATOM   8812  C  CA    . PRO   C 2  243 ? 10.126  16.630  -27.977 1.00 44.09  ? 245 PRO   D CA    1 
ATOM   8813  C  C     . PRO   C 2  243 ? 9.447   16.034  -26.755 1.00 46.79  ? 245 PRO   D C     1 
ATOM   8814  O  O     . PRO   C 2  243 ? 8.323   15.535  -26.827 1.00 52.11  ? 245 PRO   D O     1 
ATOM   8815  C  CB    . PRO   C 2  243 ? 9.633   18.052  -28.251 1.00 42.71  ? 245 PRO   D CB    1 
ATOM   8816  C  CG    . PRO   C 2  243 ? 8.587   17.892  -29.297 1.00 47.49  ? 245 PRO   D CG    1 
ATOM   8817  C  CD    . PRO   C 2  243 ? 8.952   16.709  -30.122 1.00 44.79  ? 245 PRO   D CD    1 
ATOM   8818  N  N     . GLY   C 2  244 ? 10.147  16.088  -25.627 1.00 50.74  ? 246 GLY   D N     1 
ATOM   8819  C  CA    . GLY   C 2  244 ? 9.648   15.468  -24.412 1.00 50.46  ? 246 GLY   D CA    1 
ATOM   8820  C  C     . GLY   C 2  244 ? 10.640  15.604  -23.275 1.00 53.36  ? 246 GLY   D C     1 
ATOM   8821  O  O     . GLY   C 2  244 ? 11.673  16.266  -23.395 1.00 59.27  ? 246 GLY   D O     1 
ATOM   8822  N  N     . GLN   C 2  245 ? 10.309  14.959  -22.160 1.00 52.36  ? 247 GLN   D N     1 
ATOM   8823  C  CA    . GLN   C 2  245 ? 11.093  15.036  -20.933 1.00 48.89  ? 247 GLN   D CA    1 
ATOM   8824  C  C     . GLN   C 2  245 ? 11.794  13.730  -20.603 1.00 43.55  ? 247 GLN   D C     1 
ATOM   8825  O  O     . GLN   C 2  245 ? 13.005  13.716  -20.365 1.00 43.66  ? 247 GLN   D O     1 
ATOM   8826  C  CB    . GLN   C 2  245 ? 10.190  15.426  -19.752 1.00 49.87  ? 247 GLN   D CB    1 
ATOM   8827  C  CG    . GLN   C 2  245 ? 9.531   16.788  -19.876 1.00 49.57  ? 247 GLN   D CG    1 
ATOM   8828  C  CD    . GLN   C 2  245 ? 10.509  17.931  -19.680 1.00 43.54  ? 247 GLN   D CD    1 
ATOM   8829  O  OE1   . GLN   C 2  245 ? 11.010  18.152  -18.568 1.00 42.45  ? 247 GLN   D OE1   1 
ATOM   8830  N  NE2   . GLN   C 2  245 ? 10.791  18.661  -20.758 1.00 33.46  ? 247 GLN   D NE2   1 
ATOM   8831  N  N     . LEU   C 2  246 ? 11.036  12.638  -20.575 1.00 34.91  ? 248 LEU   D N     1 
ATOM   8832  C  CA    . LEU   C 2  246 ? 11.547  11.324  -20.211 1.00 35.58  ? 248 LEU   D CA    1 
ATOM   8833  C  C     . LEU   C 2  246 ? 12.491  10.793  -21.285 1.00 36.57  ? 248 LEU   D C     1 
ATOM   8834  O  O     . LEU   C 2  246 ? 12.158  10.804  -22.475 1.00 41.44  ? 248 LEU   D O     1 
ATOM   8835  C  CB    . LEU   C 2  246 ? 10.376  10.357  -20.037 1.00 41.02  ? 248 LEU   D CB    1 
ATOM   8836  C  CG    . LEU   C 2  246 ? 10.296  9.342   -18.904 1.00 34.28  ? 248 LEU   D CG    1 
ATOM   8837  C  CD1   . LEU   C 2  246 ? 11.677  8.823   -18.568 1.00 32.94  ? 248 LEU   D CD1   1 
ATOM   8838  C  CD2   . LEU   C 2  246 ? 9.589   9.954   -17.688 1.00 40.50  ? 248 LEU   D CD2   1 
ATOM   8839  N  N     . ASN   C 2  247 ? 13.654  10.296  -20.854 1.00 35.99  ? 249 ASN   D N     1 
ATOM   8840  C  CA    . ASN   C 2  247 ? 14.673  9.725   -21.727 1.00 31.32  ? 249 ASN   D CA    1 
ATOM   8841  C  C     . ASN   C 2  247 ? 14.689  10.371  -23.109 1.00 36.48  ? 249 ASN   D C     1 
ATOM   8842  O  O     . ASN   C 2  247 ? 14.345  9.727   -24.105 1.00 38.69  ? 249 ASN   D O     1 
ATOM   8843  C  CB    . ASN   C 2  247 ? 14.454  8.228   -21.860 1.00 27.76  ? 249 ASN   D CB    1 
ATOM   8844  C  CG    . ASN   C 2  247 ? 14.301  7.554   -20.540 1.00 28.78  ? 249 ASN   D CG    1 
ATOM   8845  O  OD1   . ASN   C 2  247 ? 15.033  7.838   -19.595 1.00 32.82  ? 249 ASN   D OD1   1 
ATOM   8846  N  ND2   . ASN   C 2  247 ? 13.347  6.640   -20.456 1.00 39.12  ? 249 ASN   D ND2   1 
ATOM   8847  N  N     . ALA   C 2  248 ? 15.071  11.637  -23.187 1.00 24.76  ? 250 ALA   D N     1 
ATOM   8848  C  CA    . ALA   C 2  248 ? 15.103  12.298  -24.474 1.00 29.67  ? 250 ALA   D CA    1 
ATOM   8849  C  C     . ALA   C 2  248 ? 16.406  12.067  -25.223 1.00 38.93  ? 250 ALA   D C     1 
ATOM   8850  O  O     . ALA   C 2  248 ? 16.467  12.376  -26.421 1.00 42.64  ? 250 ALA   D O     1 
ATOM   8851  C  CB    . ALA   C 2  248 ? 14.866  13.801  -24.314 1.00 37.11  ? 250 ALA   D CB    1 
ATOM   8852  N  N     . ASP   C 2  249 ? 17.442  11.533  -24.566 1.00 25.57  ? 251 ASP   D N     1 
ATOM   8853  C  CA    . ASP   C 2  249 ? 18.676  11.213  -25.264 1.00 25.30  ? 251 ASP   D CA    1 
ATOM   8854  C  C     . ASP   C 2  249 ? 19.237  9.871   -24.793 1.00 28.83  ? 251 ASP   D C     1 
ATOM   8855  O  O     . ASP   C 2  249 ? 18.883  9.348   -23.736 1.00 26.27  ? 251 ASP   D O     1 
ATOM   8856  C  CB    . ASP   C 2  249 ? 19.724  12.328  -25.115 1.00 21.18  ? 251 ASP   D CB    1 
ATOM   8857  C  CG    . ASP   C 2  249 ? 20.192  12.495  -23.717 1.00 23.09  ? 251 ASP   D CG    1 
ATOM   8858  O  OD1   . ASP   C 2  249 ? 20.908  11.611  -23.201 1.00 28.52  ? 251 ASP   D OD1   1 
ATOM   8859  O  OD2   . ASP   C 2  249 ? 19.862  13.528  -23.123 1.00 31.02  ? 251 ASP   D OD2   1 
ATOM   8860  N  N     . LEU   C 2  250 ? 20.137  9.325   -25.617 1.00 32.76  ? 252 LEU   D N     1 
ATOM   8861  C  CA    . LEU   C 2  250 ? 20.728  8.016   -25.388 1.00 25.81  ? 252 LEU   D CA    1 
ATOM   8862  C  C     . LEU   C 2  250 ? 21.389  7.896   -24.024 1.00 33.52  ? 252 LEU   D C     1 
ATOM   8863  O  O     . LEU   C 2  250 ? 21.479  6.778   -23.492 1.00 34.70  ? 252 LEU   D O     1 
ATOM   8864  C  CB    . LEU   C 2  250 ? 21.733  7.712   -26.500 1.00 27.41  ? 252 LEU   D CB    1 
ATOM   8865  C  CG    . LEU   C 2  250 ? 21.088  7.276   -27.828 1.00 34.28  ? 252 LEU   D CG    1 
ATOM   8866  C  CD1   . LEU   C 2  250 ? 22.052  7.396   -29.000 1.00 31.60  ? 252 LEU   D CD1   1 
ATOM   8867  C  CD2   . LEU   C 2  250 ? 20.533  5.849   -27.744 1.00 23.20  ? 252 LEU   D CD2   1 
ATOM   8868  N  N     . ARG   C 2  251 ? 21.825  9.015   -23.432 1.00 35.47  ? 253 ARG   D N     1 
ATOM   8869  C  CA    . ARG   C 2  251 ? 22.544  8.982   -22.161 1.00 31.19  ? 253 ARG   D CA    1 
ATOM   8870  C  C     . ARG   C 2  251 ? 21.607  9.111   -20.962 1.00 25.13  ? 253 ARG   D C     1 
ATOM   8871  O  O     . ARG   C 2  251 ? 21.676  8.305   -20.031 1.00 20.58  ? 253 ARG   D O     1 
ATOM   8872  C  CB    . ARG   C 2  251 ? 23.608  10.076  -22.119 1.00 26.03  ? 253 ARG   D CB    1 
ATOM   8873  C  CG    . ARG   C 2  251 ? 24.394  10.110  -20.809 1.00 28.40  ? 253 ARG   D CG    1 
ATOM   8874  C  CD    . ARG   C 2  251 ? 25.288  11.352  -20.756 1.00 29.98  ? 253 ARG   D CD    1 
ATOM   8875  N  NE    . ARG   C 2  251 ? 26.195  11.318  -21.894 1.00 37.81  ? 253 ARG   D NE    1 
ATOM   8876  C  CZ    . ARG   C 2  251 ? 27.105  10.371  -22.060 1.00 36.34  ? 253 ARG   D CZ    1 
ATOM   8877  N  NH1   . ARG   C 2  251 ? 27.312  9.444   -21.131 1.00 24.43  ? 253 ARG   D NH1   1 
ATOM   8878  N  NH2   . ARG   C 2  251 ? 27.814  10.342  -23.187 1.00 37.39  ? 253 ARG   D NH2   1 
ATOM   8879  N  N     . LYS   C 2  252 ? 20.738  10.122  -20.952 1.00 24.85  ? 254 LYS   D N     1 
ATOM   8880  C  CA    . LYS   C 2  252 ? 19.717  10.174  -19.910 1.00 27.39  ? 254 LYS   D CA    1 
ATOM   8881  C  C     . LYS   C 2  252 ? 18.970  8.845   -19.832 1.00 31.49  ? 254 LYS   D C     1 
ATOM   8882  O  O     . LYS   C 2  252 ? 18.729  8.312   -18.739 1.00 30.20  ? 254 LYS   D O     1 
ATOM   8883  C  CB    . LYS   C 2  252 ? 18.744  11.326  -20.172 1.00 19.60  ? 254 LYS   D CB    1 
ATOM   8884  C  CG    . LYS   C 2  252 ? 19.381  12.675  -20.096 1.00 14.69  ? 254 LYS   D CG    1 
ATOM   8885  C  CD    . LYS   C 2  252 ? 18.465  13.653  -19.396 1.00 16.99  ? 254 LYS   D CD    1 
ATOM   8886  C  CE    . LYS   C 2  252 ? 18.769  15.093  -19.744 1.00 28.06  ? 254 LYS   D CE    1 
ATOM   8887  N  NZ    . LYS   C 2  252 ? 17.824  16.027  -19.104 1.00 33.34  ? 254 LYS   D NZ    1 
ATOM   8888  N  N     . LEU   C 2  253 ? 18.613  8.289   -20.993 1.00 28.50  ? 255 LEU   D N     1 
ATOM   8889  C  CA    . LEU   C 2  253 ? 18.027  6.957   -21.041 1.00 26.54  ? 255 LEU   D CA    1 
ATOM   8890  C  C     . LEU   C 2  253 ? 18.885  5.940   -20.288 1.00 28.27  ? 255 LEU   D C     1 
ATOM   8891  O  O     . LEU   C 2  253 ? 18.389  5.211   -19.419 1.00 27.78  ? 255 LEU   D O     1 
ATOM   8892  C  CB    . LEU   C 2  253 ? 17.841  6.534   -22.502 1.00 30.38  ? 255 LEU   D CB    1 
ATOM   8893  C  CG    . LEU   C 2  253 ? 17.308  5.110   -22.764 1.00 35.27  ? 255 LEU   D CG    1 
ATOM   8894  C  CD1   . LEU   C 2  253 ? 15.817  5.012   -22.417 1.00 23.58  ? 255 LEU   D CD1   1 
ATOM   8895  C  CD2   . LEU   C 2  253 ? 17.617  4.578   -24.193 1.00 22.03  ? 255 LEU   D CD2   1 
ATOM   8896  N  N     . ALA   C 2  254 ? 20.178  5.859   -20.622 1.00 25.46  ? 256 ALA   D N     1 
ATOM   8897  C  CA    . ALA   C 2  254 ? 21.012  4.815   -20.032 1.00 23.93  ? 256 ALA   D CA    1 
ATOM   8898  C  C     . ALA   C 2  254 ? 21.199  5.016   -18.528 1.00 30.04  ? 256 ALA   D C     1 
ATOM   8899  O  O     . ALA   C 2  254 ? 21.325  4.029   -17.785 1.00 28.35  ? 256 ALA   D O     1 
ATOM   8900  C  CB    . ALA   C 2  254 ? 22.361  4.761   -20.744 1.00 24.55  ? 256 ALA   D CB    1 
ATOM   8901  N  N     . VAL   C 2  255 ? 21.211  6.275   -18.060 1.00 27.36  ? 257 VAL   D N     1 
ATOM   8902  C  CA    . VAL   C 2  255 ? 21.268  6.567   -16.629 1.00 22.23  ? 257 VAL   D CA    1 
ATOM   8903  C  C     . VAL   C 2  255 ? 19.969  6.173   -15.945 1.00 26.55  ? 257 VAL   D C     1 
ATOM   8904  O  O     . VAL   C 2  255 ? 19.962  5.847   -14.751 1.00 35.13  ? 257 VAL   D O     1 
ATOM   8905  C  CB    . VAL   C 2  255 ? 21.587  8.054   -16.398 1.00 25.20  ? 257 VAL   D CB    1 
ATOM   8906  C  CG1   . VAL   C 2  255 ? 21.617  8.382   -14.929 1.00 20.47  ? 257 VAL   D CG1   1 
ATOM   8907  C  CG2   . VAL   C 2  255 ? 22.914  8.413   -17.032 1.00 33.06  ? 257 VAL   D CG2   1 
ATOM   8908  N  N     . ASN   C 2  256 ? 18.855  6.158   -16.682 1.00 32.54  ? 258 ASN   D N     1 
ATOM   8909  C  CA    . ASN   C 2  256 ? 17.594  5.671   -16.122 1.00 28.77  ? 258 ASN   D CA    1 
ATOM   8910  C  C     . ASN   C 2  256 ? 17.446  4.151   -16.204 1.00 27.65  ? 258 ASN   D C     1 
ATOM   8911  O  O     . ASN   C 2  256 ? 16.758  3.562   -15.363 1.00 34.76  ? 258 ASN   D O     1 
ATOM   8912  C  CB    . ASN   C 2  256 ? 16.420  6.342   -16.824 1.00 23.97  ? 258 ASN   D CB    1 
ATOM   8913  C  CG    . ASN   C 2  256 ? 16.087  7.673   -16.224 1.00 27.26  ? 258 ASN   D CG    1 
ATOM   8914  O  OD1   . ASN   C 2  256 ? 16.573  7.992   -15.144 1.00 28.98  ? 258 ASN   D OD1   1 
ATOM   8915  N  ND2   . ASN   C 2  256 ? 15.264  8.470   -16.916 1.00 22.10  ? 258 ASN   D ND2   1 
ATOM   8916  N  N     . MET   C 2  257 ? 18.090  3.489   -17.176 1.00 29.86  ? 259 MET   D N     1 
ATOM   8917  C  CA    . MET   C 2  257 ? 17.840  2.075   -17.441 1.00 26.05  ? 259 MET   D CA    1 
ATOM   8918  C  C     . MET   C 2  257 ? 18.944  1.120   -17.002 1.00 25.83  ? 259 MET   D C     1 
ATOM   8919  O  O     . MET   C 2  257 ? 18.648  -0.049  -16.758 1.00 32.81  ? 259 MET   D O     1 
ATOM   8920  C  CB    . MET   C 2  257 ? 17.576  1.866   -18.936 1.00 30.53  ? 259 MET   D CB    1 
ATOM   8921  C  CG    . MET   C 2  257 ? 16.397  2.671   -19.463 1.00 35.93  ? 259 MET   D CG    1 
ATOM   8922  S  SD    . MET   C 2  257 ? 14.836  2.124   -18.778 1.00 39.68  ? 259 MET   D SD    1 
ATOM   8923  C  CE    . MET   C 2  257 ? 15.075  0.353   -18.939 1.00 28.42  ? 259 MET   D CE    1 
ATOM   8924  N  N     . VAL   C 2  258 ? 20.191  1.564   -16.880 1.00 27.82  ? 260 VAL   D N     1 
ATOM   8925  C  CA    . VAL   C 2  258 ? 21.264  0.629   -16.547 1.00 26.23  ? 260 VAL   D CA    1 
ATOM   8926  C  C     . VAL   C 2  258 ? 21.801  0.847   -15.138 1.00 30.20  ? 260 VAL   D C     1 
ATOM   8927  O  O     . VAL   C 2  258 ? 22.648  1.725   -14.927 1.00 32.16  ? 260 VAL   D O     1 
ATOM   8928  C  CB    . VAL   C 2  258 ? 22.414  0.730   -17.549 1.00 24.73  ? 260 VAL   D CB    1 
ATOM   8929  C  CG1   . VAL   C 2  258 ? 23.543  -0.202  -17.112 1.00 25.77  ? 260 VAL   D CG1   1 
ATOM   8930  C  CG2   . VAL   C 2  258 ? 21.927  0.400   -18.933 1.00 25.33  ? 260 VAL   D CG2   1 
ATOM   8931  N  N     . PRO   C 2  259 ? 21.380  0.058   -14.152 1.00 25.92  ? 261 PRO   D N     1 
ATOM   8932  C  CA    . PRO   C 2  259 ? 21.902  0.263   -12.791 1.00 24.89  ? 261 PRO   D CA    1 
ATOM   8933  C  C     . PRO   C 2  259 ? 23.273  -0.330  -12.583 1.00 27.18  ? 261 PRO   D C     1 
ATOM   8934  O  O     . PRO   C 2  259 ? 23.925  -0.006  -11.577 1.00 29.63  ? 261 PRO   D O     1 
ATOM   8935  C  CB    . PRO   C 2  259 ? 20.866  -0.435  -11.897 1.00 27.79  ? 261 PRO   D CB    1 
ATOM   8936  C  CG    . PRO   C 2  259 ? 20.289  -1.529  -12.810 1.00 31.69  ? 261 PRO   D CG    1 
ATOM   8937  C  CD    . PRO   C 2  259 ? 20.346  -0.989  -14.229 1.00 24.66  ? 261 PRO   D CD    1 
ATOM   8938  N  N     . PHE   C 2  260 ? 23.713  -1.214  -13.482 1.00 30.06  ? 262 PHE   D N     1 
ATOM   8939  C  CA    . PHE   C 2  260 ? 24.993  -1.901  -13.393 1.00 26.27  ? 262 PHE   D CA    1 
ATOM   8940  C  C     . PHE   C 2  260 ? 25.472  -2.068  -14.814 1.00 28.31  ? 262 PHE   D C     1 
ATOM   8941  O  O     . PHE   C 2  260 ? 24.683  -2.464  -15.682 1.00 30.45  ? 262 PHE   D O     1 
ATOM   8942  C  CB    . PHE   C 2  260 ? 24.902  -3.254  -12.707 1.00 21.37  ? 262 PHE   D CB    1 
ATOM   8943  C  CG    . PHE   C 2  260 ? 24.344  -3.169  -11.352 1.00 27.79  ? 262 PHE   D CG    1 
ATOM   8944  C  CD1   . PHE   C 2  260 ? 25.136  -2.777  -10.294 1.00 27.87  ? 262 PHE   D CD1   1 
ATOM   8945  C  CD2   . PHE   C 2  260 ? 23.002  -3.409  -11.135 1.00 31.99  ? 262 PHE   D CD2   1 
ATOM   8946  C  CE1   . PHE   C 2  260 ? 24.603  -2.663  -9.033  1.00 28.53  ? 262 PHE   D CE1   1 
ATOM   8947  C  CE2   . PHE   C 2  260 ? 22.473  -3.282  -9.878  1.00 28.91  ? 262 PHE   D CE2   1 
ATOM   8948  C  CZ    . PHE   C 2  260 ? 23.278  -2.924  -8.828  1.00 24.75  ? 262 PHE   D CZ    1 
ATOM   8949  N  N     . PRO   C 2  261 ? 26.737  -1.770  -15.084 1.00 29.21  ? 263 PRO   D N     1 
ATOM   8950  C  CA    . PRO   C 2  261 ? 27.143  -1.600  -16.481 1.00 26.05  ? 263 PRO   D CA    1 
ATOM   8951  C  C     . PRO   C 2  261 ? 26.837  -2.815  -17.338 1.00 25.55  ? 263 PRO   D C     1 
ATOM   8952  O  O     . PRO   C 2  261 ? 26.211  -2.671  -18.398 1.00 22.59  ? 263 PRO   D O     1 
ATOM   8953  C  CB    . PRO   C 2  261 ? 28.641  -1.307  -16.353 1.00 22.56  ? 263 PRO   D CB    1 
ATOM   8954  C  CG    . PRO   C 2  261 ? 28.795  -0.757  -15.001 1.00 22.15  ? 263 PRO   D CG    1 
ATOM   8955  C  CD    . PRO   C 2  261 ? 27.850  -1.529  -14.159 1.00 28.84  ? 263 PRO   D CD    1 
ATOM   8956  N  N     . ARG   C 2  262 ? 27.214  -4.018  -16.881 1.00 26.54  ? 264 ARG   D N     1 
ATOM   8957  C  CA    . ARG   C 2  262 ? 27.078  -5.206  -17.722 1.00 27.74  ? 264 ARG   D CA    1 
ATOM   8958  C  C     . ARG   C 2  262 ? 25.616  -5.479  -18.047 1.00 29.09  ? 264 ARG   D C     1 
ATOM   8959  O  O     . ARG   C 2  262 ? 25.284  -5.843  -19.180 1.00 36.93  ? 264 ARG   D O     1 
ATOM   8960  C  CB    . ARG   C 2  262 ? 27.725  -6.424  -17.049 1.00 21.70  ? 264 ARG   D CB    1 
ATOM   8961  C  CG    . ARG   C 2  262 ? 29.245  -6.445  -17.132 1.00 15.73  ? 264 ARG   D CG    1 
ATOM   8962  C  CD    . ARG   C 2  262 ? 29.864  -7.366  -16.115 1.00 25.78  ? 264 ARG   D CD    1 
ATOM   8963  N  NE    . ARG   C 2  262 ? 29.386  -8.737  -16.235 1.00 43.92  ? 264 ARG   D NE    1 
ATOM   8964  C  CZ    . ARG   C 2  262 ? 30.000  -9.689  -16.926 1.00 46.82  ? 264 ARG   D CZ    1 
ATOM   8965  N  NH1   . ARG   C 2  262 ? 31.152  -9.470  -17.534 1.00 41.92  ? 264 ARG   D NH1   1 
ATOM   8966  N  NH2   . ARG   C 2  262 ? 29.436  -10.888 -17.018 1.00 48.21  ? 264 ARG   D NH2   1 
ATOM   8967  N  N     . LEU   C 2  263 ? 24.726  -5.286  -17.072 1.00 24.84  ? 265 LEU   D N     1 
ATOM   8968  C  CA    . LEU   C 2  263 ? 23.296  -5.524  -17.243 1.00 23.16  ? 265 LEU   D CA    1 
ATOM   8969  C  C     . LEU   C 2  263 ? 22.675  -4.385  -18.057 1.00 33.50  ? 265 LEU   D C     1 
ATOM   8970  O  O     . LEU   C 2  263 ? 21.946  -3.534  -17.541 1.00 33.14  ? 265 LEU   D O     1 
ATOM   8971  C  CB    . LEU   C 2  263 ? 22.629  -5.664  -15.885 1.00 24.54  ? 265 LEU   D CB    1 
ATOM   8972  C  CG    . LEU   C 2  263 ? 23.392  -6.450  -14.819 1.00 23.36  ? 265 LEU   D CG    1 
ATOM   8973  C  CD1   . LEU   C 2  263 ? 22.516  -6.655  -13.650 1.00 29.72  ? 265 LEU   D CD1   1 
ATOM   8974  C  CD2   . LEU   C 2  263 ? 23.859  -7.777  -15.351 1.00 35.59  ? 265 LEU   D CD2   1 
ATOM   8975  N  N     . HIS   C 2  264 ? 22.982  -4.383  -19.370 1.00 31.07  ? 266 HIS   D N     1 
ATOM   8976  C  CA    . HIS   C 2  264 ? 22.478  -3.379  -20.308 1.00 30.15  ? 266 HIS   D CA    1 
ATOM   8977  C  C     . HIS   C 2  264 ? 21.660  -4.003  -21.444 1.00 39.05  ? 266 HIS   D C     1 
ATOM   8978  O  O     . HIS   C 2  264 ? 21.564  -3.428  -22.538 1.00 36.48  ? 266 HIS   D O     1 
ATOM   8979  C  CB    . HIS   C 2  264 ? 23.616  -2.511  -20.874 1.00 30.72  ? 266 HIS   D CB    1 
ATOM   8980  C  CG    . HIS   C 2  264 ? 24.726  -3.277  -21.546 1.00 32.04  ? 266 HIS   D CG    1 
ATOM   8981  N  ND1   . HIS   C 2  264 ? 25.958  -3.473  -20.958 1.00 24.71  ? 266 HIS   D ND1   1 
ATOM   8982  C  CD2   . HIS   C 2  264 ? 24.800  -3.863  -22.767 1.00 33.34  ? 266 HIS   D CD2   1 
ATOM   8983  C  CE1   . HIS   C 2  264 ? 26.732  -4.164  -21.773 1.00 28.28  ? 266 HIS   D CE1   1 
ATOM   8984  N  NE2   . HIS   C 2  264 ? 26.051  -4.421  -22.876 1.00 30.98  ? 266 HIS   D NE2   1 
ATOM   8985  N  N     . PHE   C 2  265 ? 21.035  -5.158  -21.197 1.00 35.53  ? 267 PHE   D N     1 
ATOM   8986  C  CA    . PHE   C 2  265 ? 20.188  -5.824  -22.188 1.00 35.82  ? 267 PHE   D CA    1 
ATOM   8987  C  C     . PHE   C 2  265 ? 18.729  -5.720  -21.758 1.00 35.76  ? 267 PHE   D C     1 
ATOM   8988  O  O     . PHE   C 2  265 ? 18.387  -6.052  -20.617 1.00 42.21  ? 267 PHE   D O     1 
ATOM   8989  C  CB    . PHE   C 2  265 ? 20.619  -7.292  -22.381 1.00 36.65  ? 267 PHE   D CB    1 
ATOM   8990  C  CG    . PHE   C 2  265 ? 22.105  -7.449  -22.614 1.00 36.33  ? 267 PHE   D CG    1 
ATOM   8991  C  CD1   . PHE   C 2  265 ? 22.633  -7.389  -23.894 1.00 30.26  ? 267 PHE   D CD1   1 
ATOM   8992  C  CD2   . PHE   C 2  265 ? 22.976  -7.596  -21.545 1.00 34.25  ? 267 PHE   D CD2   1 
ATOM   8993  C  CE1   . PHE   C 2  265 ? 23.977  -7.504  -24.096 1.00 29.35  ? 267 PHE   D CE1   1 
ATOM   8994  C  CE2   . PHE   C 2  265 ? 24.327  -7.706  -21.755 1.00 29.76  ? 267 PHE   D CE2   1 
ATOM   8995  C  CZ    . PHE   C 2  265 ? 24.823  -7.658  -23.027 1.00 28.69  ? 267 PHE   D CZ    1 
ATOM   8996  N  N     . PHE   C 2  266 ? 17.880  -5.244  -22.667 1.00 34.37  ? 268 PHE   D N     1 
ATOM   8997  C  CA    . PHE   C 2  266 ? 16.490  -4.914  -22.383 1.00 39.16  ? 268 PHE   D CA    1 
ATOM   8998  C  C     . PHE   C 2  266 ? 15.534  -5.850  -23.131 1.00 49.90  ? 268 PHE   D C     1 
ATOM   8999  O  O     . PHE   C 2  266 ? 15.871  -6.402  -24.184 1.00 44.62  ? 268 PHE   D O     1 
ATOM   9000  C  CB    . PHE   C 2  266 ? 16.182  -3.459  -22.778 1.00 29.98  ? 268 PHE   D CB    1 
ATOM   9001  C  CG    . PHE   C 2  266 ? 17.238  -2.442  -22.354 1.00 36.08  ? 268 PHE   D CG    1 
ATOM   9002  C  CD1   . PHE   C 2  266 ? 17.911  -2.553  -21.135 1.00 32.75  ? 268 PHE   D CD1   1 
ATOM   9003  C  CD2   . PHE   C 2  266 ? 17.537  -1.349  -23.179 1.00 31.22  ? 268 PHE   D CD2   1 
ATOM   9004  C  CE1   . PHE   C 2  266 ? 18.874  -1.612  -20.760 1.00 29.25  ? 268 PHE   D CE1   1 
ATOM   9005  C  CE2   . PHE   C 2  266 ? 18.492  -0.411  -22.807 1.00 29.04  ? 268 PHE   D CE2   1 
ATOM   9006  C  CZ    . PHE   C 2  266 ? 19.161  -0.543  -21.599 1.00 30.26  ? 268 PHE   D CZ    1 
ATOM   9007  N  N     . MET   C 2  267 ? 14.322  -6.030  -22.579 1.00 53.05  ? 269 MET   D N     1 
ATOM   9008  C  CA    . MET   C 2  267 ? 13.251  -6.734  -23.286 1.00 37.48  ? 269 MET   D CA    1 
ATOM   9009  C  C     . MET   C 2  267 ? 12.336  -5.700  -23.914 1.00 38.79  ? 269 MET   D C     1 
ATOM   9010  O  O     . MET   C 2  267 ? 11.703  -4.936  -23.171 1.00 40.15  ? 269 MET   D O     1 
ATOM   9011  C  CB    . MET   C 2  267 ? 12.455  -7.635  -22.337 1.00 34.55  ? 269 MET   D CB    1 
ATOM   9012  C  CG    . MET   C 2  267 ? 13.229  -8.851  -21.774 1.00 46.15  ? 269 MET   D CG    1 
ATOM   9013  S  SD    . MET   C 2  267 ? 12.239  -9.987  -20.739 1.00 54.21  ? 269 MET   D SD    1 
ATOM   9014  C  CE    . MET   C 2  267 ? 10.608  -9.558  -21.327 1.00 44.59  ? 269 MET   D CE    1 
ATOM   9015  N  N     . PRO   C 2  268 ? 12.232  -5.605  -25.240 1.00 41.88  ? 270 PRO   D N     1 
ATOM   9016  C  CA    . PRO   C 2  268 ? 11.285  -4.654  -25.828 1.00 39.62  ? 270 PRO   D CA    1 
ATOM   9017  C  C     . PRO   C 2  268 ? 9.906   -5.276  -25.932 1.00 39.51  ? 270 PRO   D C     1 
ATOM   9018  O  O     . PRO   C 2  268 ? 9.752   -6.499  -25.961 1.00 37.16  ? 270 PRO   D O     1 
ATOM   9019  C  CB    . PRO   C 2  268 ? 11.874  -4.358  -27.215 1.00 24.71  ? 270 PRO   D CB    1 
ATOM   9020  C  CG    . PRO   C 2  268 ? 12.968  -5.408  -27.418 1.00 35.45  ? 270 PRO   D CG    1 
ATOM   9021  C  CD    . PRO   C 2  268 ? 12.905  -6.385  -26.284 1.00 37.64  ? 270 PRO   D CD    1 
ATOM   9022  N  N     . GLY   C 2  269 ? 8.904   -4.410  -25.963 1.00 37.21  ? 271 GLY   D N     1 
ATOM   9023  C  CA    . GLY   C 2  269 ? 7.520   -4.843  -25.906 1.00 38.47  ? 271 GLY   D CA    1 
ATOM   9024  C  C     . GLY   C 2  269 ? 6.637   -3.842  -26.608 1.00 44.95  ? 271 GLY   D C     1 
ATOM   9025  O  O     . GLY   C 2  269 ? 6.956   -2.650  -26.679 1.00 49.86  ? 271 GLY   D O     1 
ATOM   9026  N  N     . PHE   C 2  270 ? 5.514   -4.329  -27.132 1.00 38.18  ? 272 PHE   D N     1 
ATOM   9027  C  CA    . PHE   C 2  270 ? 4.686   -3.494  -27.984 1.00 45.36  ? 272 PHE   D CA    1 
ATOM   9028  C  C     . PHE   C 2  270 ? 3.230   -3.935  -27.874 1.00 52.99  ? 272 PHE   D C     1 
ATOM   9029  O  O     . PHE   C 2  270 ? 2.935   -5.084  -27.526 1.00 57.87  ? 272 PHE   D O     1 
ATOM   9030  C  CB    . PHE   C 2  270 ? 5.189   -3.546  -29.434 1.00 45.66  ? 272 PHE   D CB    1 
ATOM   9031  C  CG    . PHE   C 2  270 ? 4.611   -2.478  -30.299 1.00 56.54  ? 272 PHE   D CG    1 
ATOM   9032  C  CD1   . PHE   C 2  270 ? 4.955   -1.140  -30.098 1.00 60.03  ? 272 PHE   D CD1   1 
ATOM   9033  C  CD2   . PHE   C 2  270 ? 3.703   -2.794  -31.300 1.00 52.03  ? 272 PHE   D CD2   1 
ATOM   9034  C  CE1   . PHE   C 2  270 ? 4.398   -0.126  -30.895 1.00 67.46  ? 272 PHE   D CE1   1 
ATOM   9035  C  CE2   . PHE   C 2  270 ? 3.145   -1.798  -32.107 1.00 54.17  ? 272 PHE   D CE2   1 
ATOM   9036  C  CZ    . PHE   C 2  270 ? 3.490   -0.461  -31.905 1.00 69.10  ? 272 PHE   D CZ    1 
ATOM   9037  N  N     . ALA   C 2  271 ? 2.320   -2.990  -28.147 1.00 47.80  ? 273 ALA   D N     1 
ATOM   9038  C  CA    . ALA   C 2  271 ? 0.871   -3.158  -28.086 1.00 50.16  ? 273 ALA   D CA    1 
ATOM   9039  C  C     . ALA   C 2  271 ? 0.261   -1.939  -28.757 1.00 55.21  ? 273 ALA   D C     1 
ATOM   9040  O  O     . ALA   C 2  271 ? 0.726   -0.819  -28.499 1.00 53.89  ? 273 ALA   D O     1 
ATOM   9041  C  CB    . ALA   C 2  271 ? 0.347   -3.296  -26.643 1.00 51.33  ? 273 ALA   D CB    1 
ATOM   9042  N  N     . PRO   C 2  272 ? -0.765  -2.099  -29.623 1.00 59.96  ? 274 PRO   D N     1 
ATOM   9043  C  CA    . PRO   C 2  272 ? -1.501  -3.324  -29.981 1.00 48.70  ? 274 PRO   D CA    1 
ATOM   9044  C  C     . PRO   C 2  272 ? -0.633  -4.353  -30.681 1.00 50.78  ? 274 PRO   D C     1 
ATOM   9045  O  O     . PRO   C 2  272 ? 0.319   -3.989  -31.352 1.00 56.73  ? 274 PRO   D O     1 
ATOM   9046  C  CB    . PRO   C 2  272 ? -2.596  -2.809  -30.926 1.00 60.89  ? 274 PRO   D CB    1 
ATOM   9047  C  CG    . PRO   C 2  272 ? -2.612  -1.300  -30.781 1.00 57.26  ? 274 PRO   D CG    1 
ATOM   9048  C  CD    . PRO   C 2  272 ? -1.208  -0.954  -30.438 1.00 61.55  ? 274 PRO   D CD    1 
ATOM   9049  N  N     . LEU   C 2  273 ? -0.936  -5.642  -30.556 1.00 54.40  ? 275 LEU   D N     1 
ATOM   9050  C  CA    . LEU   C 2  273 ? -0.158  -6.699  -31.205 1.00 58.67  ? 275 LEU   D CA    1 
ATOM   9051  C  C     . LEU   C 2  273 ? -0.758  -7.008  -32.579 1.00 63.63  ? 275 LEU   D C     1 
ATOM   9052  O  O     . LEU   C 2  273 ? -1.712  -7.784  -32.692 1.00 67.49  ? 275 LEU   D O     1 
ATOM   9053  C  CB    . LEU   C 2  273 ? -0.126  -7.943  -30.326 1.00 56.90  ? 275 LEU   D CB    1 
ATOM   9054  C  CG    . LEU   C 2  273 ? 1.254   -8.342  -29.830 1.00 46.35  ? 275 LEU   D CG    1 
ATOM   9055  C  CD1   . LEU   C 2  273 ? 1.281   -9.805  -29.400 1.00 52.03  ? 275 LEU   D CD1   1 
ATOM   9056  C  CD2   . LEU   C 2  273 ? 2.241   -8.078  -30.922 1.00 39.82  ? 275 LEU   D CD2   1 
ATOM   9057  N  N     . THR   C 2  274 ? -0.204  -6.397  -33.629 1.00 70.45  ? 276 THR   D N     1 
ATOM   9058  C  CA    . THR   C 2  274 ? -0.597  -6.706  -35.012 1.00 71.16  ? 276 THR   D CA    1 
ATOM   9059  C  C     . THR   C 2  274 ? 0.630   -7.068  -35.845 1.00 69.17  ? 276 THR   D C     1 
ATOM   9060  O  O     . THR   C 2  274 ? 0.872   -8.237  -36.140 1.00 69.22  ? 276 THR   D O     1 
ATOM   9061  C  CB    . THR   C 2  274 ? -1.332  -5.529  -35.710 1.00 57.28  ? 276 THR   D CB    1 
ATOM   9062  O  OG1   . THR   C 2  274 ? -0.496  -4.363  -35.704 1.00 65.83  ? 276 THR   D OG1   1 
ATOM   9063  C  CG2   . THR   C 2  274 ? -2.668  -5.230  -35.038 1.00 50.52  ? 276 THR   D CG2   1 
ATOM   9064  N  N     . ARG   C 2  282 ? -8.669  -3.715  -34.372 1.00 67.65  ? 284 ARG   D N     1 
ATOM   9065  C  CA    . ARG   C 2  282 ? -9.462  -2.917  -33.432 1.00 95.02  ? 284 ARG   D CA    1 
ATOM   9066  C  C     . ARG   C 2  282 ? -8.600  -2.257  -32.330 1.00 95.93  ? 284 ARG   D C     1 
ATOM   9067  O  O     . ARG   C 2  282 ? -7.488  -2.711  -32.030 1.00 90.24  ? 284 ARG   D O     1 
ATOM   9068  C  CB    . ARG   C 2  282 ? -10.561 -3.778  -32.797 1.00 85.65  ? 284 ARG   D CB    1 
ATOM   9069  C  CG    . ARG   C 2  282 ? -11.347 -4.629  -33.787 1.00 81.32  ? 284 ARG   D CG    1 
ATOM   9070  C  CD    . ARG   C 2  282 ? -11.892 -3.827  -34.960 1.00 83.38  ? 284 ARG   D CD    1 
ATOM   9071  N  NE    . ARG   C 2  282 ? -12.644 -2.653  -34.536 1.00 85.88  ? 284 ARG   D NE    1 
ATOM   9072  C  CZ    . ARG   C 2  282 ? -13.370 -1.889  -35.345 1.00 92.08  ? 284 ARG   D CZ    1 
ATOM   9073  N  NH1   . ARG   C 2  282 ? -13.520 -2.184  -36.628 1.00 87.32  ? 284 ARG   D NH1   1 
ATOM   9074  N  NH2   . ARG   C 2  282 ? -13.958 -0.800  -34.855 1.00 69.38  ? 284 ARG   D NH2   1 
ATOM   9075  N  N     . ALA   C 2  283 ? -9.132  -1.190  -31.729 1.00 89.89  ? 285 ALA   D N     1 
ATOM   9076  C  CA    . ALA   C 2  283 ? -8.380  -0.308  -30.843 1.00 85.03  ? 285 ALA   D CA    1 
ATOM   9077  C  C     . ALA   C 2  283 ? -8.673  -0.623  -29.378 1.00 90.47  ? 285 ALA   D C     1 
ATOM   9078  O  O     . ALA   C 2  283 ? -9.833  -0.802  -28.991 1.00 87.25  ? 285 ALA   D O     1 
ATOM   9079  C  CB    . ALA   C 2  283 ? -8.716  1.156   -31.138 1.00 65.80  ? 285 ALA   D CB    1 
ATOM   9080  N  N     . LEU   C 2  284 ? -7.621  -0.672  -28.560 1.00 76.74  ? 286 LEU   D N     1 
ATOM   9081  C  CA    . LEU   C 2  284 ? -7.749  -1.082  -27.171 1.00 62.02  ? 286 LEU   D CA    1 
ATOM   9082  C  C     . LEU   C 2  284 ? -7.638  0.111   -26.233 1.00 65.07  ? 286 LEU   D C     1 
ATOM   9083  O  O     . LEU   C 2  284 ? -7.232  1.210   -26.624 1.00 66.42  ? 286 LEU   D O     1 
ATOM   9084  C  CB    . LEU   C 2  284 ? -6.711  -2.149  -26.797 1.00 56.66  ? 286 LEU   D CB    1 
ATOM   9085  C  CG    . LEU   C 2  284 ? -5.227  -1.841  -26.930 1.00 65.55  ? 286 LEU   D CG    1 
ATOM   9086  C  CD1   . LEU   C 2  284 ? -4.422  -3.010  -26.386 1.00 50.38  ? 286 LEU   D CD1   1 
ATOM   9087  C  CD2   . LEU   C 2  284 ? -4.860  -1.557  -28.383 1.00 66.07  ? 286 LEU   D CD2   1 
ATOM   9088  N  N     . THR   C 2  285 ? -8.030  -0.130  -24.983 1.00 66.68  ? 287 THR   D N     1 
ATOM   9089  C  CA    . THR   C 2  285 ? -8.168  0.887   -23.950 1.00 70.83  ? 287 THR   D CA    1 
ATOM   9090  C  C     . THR   C 2  285 ? -6.854  1.113   -23.231 1.00 58.72  ? 287 THR   D C     1 
ATOM   9091  O  O     . THR   C 2  285 ? -5.953  0.266   -23.259 1.00 53.71  ? 287 THR   D O     1 
ATOM   9092  C  CB    . THR   C 2  285 ? -9.231  0.488   -22.919 1.00 65.17  ? 287 THR   D CB    1 
ATOM   9093  O  OG1   . THR   C 2  285 ? -9.180  -0.926  -22.705 1.00 55.39  ? 287 THR   D OG1   1 
ATOM   9094  C  CG2   . THR   C 2  285 ? -10.644 0.925   -23.352 1.00 61.42  ? 287 THR   D CG2   1 
ATOM   9095  N  N     . VAL   C 2  286 ? -6.754  2.259   -22.552 1.00 59.47  ? 288 VAL   D N     1 
ATOM   9096  C  CA    . VAL   C 2  286 ? -5.562  2.594   -21.774 1.00 59.47  ? 288 VAL   D CA    1 
ATOM   9097  C  C     . VAL   C 2  286 ? -5.257  1.485   -20.753 1.00 54.55  ? 288 VAL   D C     1 
ATOM   9098  O  O     . VAL   C 2  286 ? -4.081  1.156   -20.563 1.00 53.68  ? 288 VAL   D O     1 
ATOM   9099  C  CB    . VAL   C 2  286 ? -5.667  3.959   -21.152 1.00 51.54  ? 288 VAL   D CB    1 
ATOM   9100  C  CG1   . VAL   C 2  286 ? -4.449  4.232   -20.299 1.00 51.52  ? 288 VAL   D CG1   1 
ATOM   9101  C  CG2   . VAL   C 2  286 ? -5.816  5.029   -22.227 1.00 57.87  ? 288 VAL   D CG2   1 
ATOM   9102  N  N     . PRO   C 2  287 ? -6.243  0.930   -20.054 1.00 50.66  ? 289 PRO   D N     1 
ATOM   9103  C  CA    . PRO   C 2  287 ? -5.949  -0.251  -19.225 1.00 49.64  ? 289 PRO   D CA    1 
ATOM   9104  C  C     . PRO   C 2  287 ? -5.450  -1.456  -20.016 1.00 53.80  ? 289 PRO   D C     1 
ATOM   9105  O  O     . PRO   C 2  287 ? -4.585  -2.194  -19.523 1.00 52.20  ? 289 PRO   D O     1 
ATOM   9106  C  CB    . PRO   C 2  287 ? -7.293  -0.508  -18.541 1.00 46.57  ? 289 PRO   D CB    1 
ATOM   9107  C  CG    . PRO   C 2  287 ? -7.873  0.888   -18.401 1.00 50.06  ? 289 PRO   D CG    1 
ATOM   9108  C  CD    . PRO   C 2  287 ? -7.520  1.564   -19.683 1.00 51.23  ? 289 PRO   D CD    1 
ATOM   9109  N  N     . GLU   C 2  288 ? -5.958  -1.678  -21.234 1.00 56.17  ? 290 GLU   D N     1 
ATOM   9110  C  CA    . GLU   C 2  288 ? -5.503  -2.820  -22.029 1.00 56.72  ? 290 GLU   D CA    1 
ATOM   9111  C  C     . GLU   C 2  288 ? -4.111  -2.574  -22.604 1.00 60.19  ? 290 GLU   D C     1 
ATOM   9112  O  O     . GLU   C 2  288 ? -3.273  -3.489  -22.647 1.00 59.69  ? 290 GLU   D O     1 
ATOM   9113  C  CB    . GLU   C 2  288 ? -6.491  -3.121  -23.157 1.00 55.23  ? 290 GLU   D CB    1 
ATOM   9114  C  CG    . GLU   C 2  288 ? -7.754  -3.875  -22.750 1.00 50.97  ? 290 GLU   D CG    1 
ATOM   9115  C  CD    . GLU   C 2  288 ? -8.921  -3.606  -23.701 1.00 58.05  ? 290 GLU   D CD    1 
ATOM   9116  O  OE1   . GLU   C 2  288 ? -8.831  -2.662  -24.513 1.00 60.06  ? 290 GLU   D OE1   1 
ATOM   9117  O  OE2   . GLU   C 2  288 ? -9.936  -4.328  -23.631 1.00 59.82  ? 290 GLU   D OE2   1 
ATOM   9118  N  N     . LEU   C 2  289 ? -3.850  -1.349  -23.073 1.00 56.67  ? 291 LEU   D N     1 
ATOM   9119  C  CA    . LEU   C 2  289 ? -2.489  -1.006  -23.459 1.00 57.62  ? 291 LEU   D CA    1 
ATOM   9120  C  C     . LEU   C 2  289 ? -1.544  -1.334  -22.325 1.00 60.12  ? 291 LEU   D C     1 
ATOM   9121  O  O     . LEU   C 2  289 ? -0.470  -1.911  -22.538 1.00 66.29  ? 291 LEU   D O     1 
ATOM   9122  C  CB    . LEU   C 2  289 ? -2.389  0.474   -23.829 1.00 49.80  ? 291 LEU   D CB    1 
ATOM   9123  C  CG    . LEU   C 2  289 ? -2.933  0.831   -25.209 1.00 47.42  ? 291 LEU   D CG    1 
ATOM   9124  C  CD1   . LEU   C 2  289 ? -2.866  2.331   -25.502 1.00 50.05  ? 291 LEU   D CD1   1 
ATOM   9125  C  CD2   . LEU   C 2  289 ? -2.169  0.043   -26.239 1.00 51.50  ? 291 LEU   D CD2   1 
ATOM   9126  N  N     . THR   C 2  290 ? -1.963  -1.021  -21.099 1.00 56.59  ? 292 THR   D N     1 
ATOM   9127  C  CA    . THR   C 2  290 ? -1.080  -1.179  -19.954 1.00 61.90  ? 292 THR   D CA    1 
ATOM   9128  C  C     . THR   C 2  290 ? -0.940  -2.642  -19.552 1.00 61.21  ? 292 THR   D C     1 
ATOM   9129  O  O     . THR   C 2  290 ? 0.156   -3.080  -19.190 1.00 70.98  ? 292 THR   D O     1 
ATOM   9130  C  CB    . THR   C 2  290 ? -1.573  -0.342  -18.771 1.00 48.19  ? 292 THR   D CB    1 
ATOM   9131  O  OG1   . THR   C 2  290 ? -1.762  1.019   -19.178 1.00 42.56  ? 292 THR   D OG1   1 
ATOM   9132  C  CG2   . THR   C 2  290 ? -0.544  -0.368  -17.673 1.00 50.26  ? 292 THR   D CG2   1 
ATOM   9133  N  N     . GLN   C 2  291 ? -2.025  -3.419  -19.594 1.00 61.84  ? 293 GLN   D N     1 
ATOM   9134  C  CA    . GLN   C 2  291 ? -1.888  -4.802  -19.144 1.00 65.22  ? 293 GLN   D CA    1 
ATOM   9135  C  C     . GLN   C 2  291 ? -1.156  -5.649  -20.177 1.00 68.55  ? 293 GLN   D C     1 
ATOM   9136  O  O     . GLN   C 2  291 ? -0.324  -6.489  -19.814 1.00 57.73  ? 293 GLN   D O     1 
ATOM   9137  C  CB    . GLN   C 2  291 ? -3.249  -5.415  -18.818 1.00 62.51  ? 293 GLN   D CB    1 
ATOM   9138  C  CG    . GLN   C 2  291 ? -3.217  -6.394  -17.641 1.00 62.60  ? 293 GLN   D CG    1 
ATOM   9139  C  CD    . GLN   C 2  291 ? -3.120  -5.688  -16.276 1.00 89.43  ? 293 GLN   D CD    1 
ATOM   9140  O  OE1   . GLN   C 2  291 ? -3.085  -4.455  -16.203 1.00 83.49  ? 293 GLN   D OE1   1 
ATOM   9141  N  NE2   . GLN   C 2  291 ? -3.082  -6.472  -15.192 1.00 82.01  ? 293 GLN   D NE2   1 
ATOM   9142  N  N     . GLN   C 2  292 ? -1.434  -5.440  -21.466 1.00 60.45  ? 294 GLN   D N     1 
ATOM   9143  C  CA    . GLN   C 2  292 ? -0.711  -6.189  -22.485 1.00 61.87  ? 294 GLN   D CA    1 
ATOM   9144  C  C     . GLN   C 2  292 ? 0.789   -5.964  -22.356 1.00 66.81  ? 294 GLN   D C     1 
ATOM   9145  O  O     . GLN   C 2  292 ? 1.574   -6.919  -22.276 1.00 63.87  ? 294 GLN   D O     1 
ATOM   9146  C  CB    . GLN   C 2  292 ? -1.199  -5.782  -23.867 1.00 61.37  ? 294 GLN   D CB    1 
ATOM   9147  C  CG    . GLN   C 2  292 ? -2.076  -6.812  -24.508 1.00 59.39  ? 294 GLN   D CG    1 
ATOM   9148  C  CD    . GLN   C 2  292 ? -2.753  -6.269  -25.742 1.00 71.71  ? 294 GLN   D CD    1 
ATOM   9149  O  OE1   . GLN   C 2  292 ? -3.625  -5.403  -25.645 1.00 67.52  ? 294 GLN   D OE1   1 
ATOM   9150  N  NE2   . GLN   C 2  292 ? -2.342  -6.755  -26.917 1.00 64.48  ? 294 GLN   D NE2   1 
ATOM   9151  N  N     . MET   C 2  293 ? 1.191   -4.694  -22.313 1.00 66.43  ? 295 MET   D N     1 
ATOM   9152  C  CA    . MET   C 2  293 ? 2.566   -4.217  -22.221 1.00 60.57  ? 295 MET   D CA    1 
ATOM   9153  C  C     . MET   C 2  293 ? 3.446   -5.022  -21.265 1.00 54.96  ? 295 MET   D C     1 
ATOM   9154  O  O     . MET   C 2  293 ? 4.605   -5.305  -21.587 1.00 61.25  ? 295 MET   D O     1 
ATOM   9155  C  CB    . MET   C 2  293 ? 2.546   -2.748  -21.792 1.00 61.65  ? 295 MET   D CB    1 
ATOM   9156  C  CG    . MET   C 2  293 ? 3.365   -1.807  -22.644 1.00 49.80  ? 295 MET   D CG    1 
ATOM   9157  S  SD    . MET   C 2  293 ? 3.345   -0.145  -21.947 1.00 53.73  ? 295 MET   D SD    1 
ATOM   9158  C  CE    . MET   C 2  293 ? 4.101   -0.441  -20.357 1.00 52.75  ? 295 MET   D CE    1 
ATOM   9159  N  N     . PHE   C 2  294 ? 2.929   -5.389  -20.091 1.00 54.69  ? 296 PHE   D N     1 
ATOM   9160  C  CA    . PHE   C 2  294 ? 3.697   -6.154  -19.098 1.00 58.64  ? 296 PHE   D CA    1 
ATOM   9161  C  C     . PHE   C 2  294 ? 3.444   -7.666  -19.180 1.00 61.99  ? 296 PHE   D C     1 
ATOM   9162  O  O     . PHE   C 2  294 ? 3.382   -8.361  -18.151 1.00 52.51  ? 296 PHE   D O     1 
ATOM   9163  C  CB    . PHE   C 2  294 ? 3.375   -5.633  -17.701 1.00 58.98  ? 296 PHE   D CB    1 
ATOM   9164  C  CG    . PHE   C 2  294 ? 3.863   -4.232  -17.426 1.00 43.66  ? 296 PHE   D CG    1 
ATOM   9165  C  CD1   . PHE   C 2  294 ? 5.113   -4.020  -16.868 1.00 44.08  ? 296 PHE   D CD1   1 
ATOM   9166  C  CD2   . PHE   C 2  294 ? 3.064   -3.140  -17.684 1.00 36.54  ? 296 PHE   D CD2   1 
ATOM   9167  C  CE1   . PHE   C 2  294 ? 5.554   -2.750  -16.600 1.00 37.53  ? 296 PHE   D CE1   1 
ATOM   9168  C  CE2   . PHE   C 2  294 ? 3.504   -1.871  -17.408 1.00 35.88  ? 296 PHE   D CE2   1 
ATOM   9169  C  CZ    . PHE   C 2  294 ? 4.747   -1.676  -16.871 1.00 32.13  ? 296 PHE   D CZ    1 
ATOM   9170  N  N     . ASP   C 2  295 ? 3.316   -8.204  -20.395 1.00 73.54  ? 297 ASP   D N     1 
ATOM   9171  C  CA    . ASP   C 2  295 ? 2.810   -9.553  -20.635 1.00 66.04  ? 297 ASP   D CA    1 
ATOM   9172  C  C     . ASP   C 2  295 ? 3.712   -10.274 -21.627 1.00 64.69  ? 297 ASP   D C     1 
ATOM   9173  O  O     . ASP   C 2  295 ? 3.979   -9.746  -22.712 1.00 68.68  ? 297 ASP   D O     1 
ATOM   9174  C  CB    . ASP   C 2  295 ? 1.380   -9.480  -21.182 1.00 64.63  ? 297 ASP   D CB    1 
ATOM   9175  C  CG    . ASP   C 2  295 ? 0.801   -10.834 -21.485 1.00 70.51  ? 297 ASP   D CG    1 
ATOM   9176  O  OD1   . ASP   C 2  295 ? 1.003   -11.742 -20.649 1.00 68.74  ? 297 ASP   D OD1   1 
ATOM   9177  O  OD2   . ASP   C 2  295 ? 0.134   -10.975 -22.543 1.00 66.06  ? 297 ASP   D OD2   1 
ATOM   9178  N  N     . SER   C 2  296 ? 4.152   -11.489 -21.275 1.00 50.19  ? 298 SER   D N     1 
ATOM   9179  C  CA    . SER   C 2  296 ? 5.049   -12.243 -22.156 1.00 54.68  ? 298 SER   D CA    1 
ATOM   9180  C  C     . SER   C 2  296 ? 4.563   -12.298 -23.605 1.00 49.37  ? 298 SER   D C     1 
ATOM   9181  O  O     . SER   C 2  296 ? 5.378   -12.317 -24.528 1.00 47.42  ? 298 SER   D O     1 
ATOM   9182  C  CB    . SER   C 2  296 ? 5.240   -13.661 -21.623 1.00 52.82  ? 298 SER   D CB    1 
ATOM   9183  O  OG    . SER   C 2  296 ? 5.708   -13.635 -20.284 0.62 61.75  ? 298 SER   D OG    1 
ATOM   9184  N  N     . LYS   C 2  297 ? 3.248   -12.317 -23.827 1.00 60.01  ? 299 LYS   D N     1 
ATOM   9185  C  CA    . LYS   C 2  297 ? 2.688   -12.372 -25.175 1.00 61.77  ? 299 LYS   D CA    1 
ATOM   9186  C  C     . LYS   C 2  297 ? 3.013   -11.139 -26.016 1.00 60.54  ? 299 LYS   D C     1 
ATOM   9187  O  O     . LYS   C 2  297 ? 2.821   -11.178 -27.237 1.00 60.91  ? 299 LYS   D O     1 
ATOM   9188  C  CB    . LYS   C 2  297 ? 1.165   -12.562 -25.098 1.00 74.73  ? 299 LYS   D CB    1 
ATOM   9189  C  CG    . LYS   C 2  297 ? 0.706   -14.015 -24.843 1.00 77.86  ? 299 LYS   D CG    1 
ATOM   9190  C  CD    . LYS   C 2  297 ? -0.818  -14.145 -24.597 1.00 72.97  ? 299 LYS   D CD    1 
ATOM   9191  C  CE    . LYS   C 2  297 ? -1.674  -13.395 -25.645 1.00 78.96  ? 299 LYS   D CE    1 
ATOM   9192  N  NZ    . LYS   C 2  297 ? -1.491  -13.862 -27.060 1.00 78.46  ? 299 LYS   D NZ    1 
ATOM   9193  N  N     . ASN   C 2  298 ? 3.493   -10.052 -25.408 1.00 59.44  ? 300 ASN   D N     1 
ATOM   9194  C  CA    . ASN   C 2  298 ? 3.869   -8.853  -26.151 1.00 51.37  ? 300 ASN   D CA    1 
ATOM   9195  C  C     . ASN   C 2  298 ? 5.335   -8.481  -25.985 1.00 49.30  ? 300 ASN   D C     1 
ATOM   9196  O  O     . ASN   C 2  298 ? 5.719   -7.368  -26.362 1.00 47.50  ? 300 ASN   D O     1 
ATOM   9197  C  CB    . ASN   C 2  298 ? 3.005   -7.665  -25.745 1.00 45.57  ? 300 ASN   D CB    1 
ATOM   9198  C  CG    . ASN   C 2  298 ? 1.579   -7.855  -26.110 1.00 53.06  ? 300 ASN   D CG    1 
ATOM   9199  O  OD1   . ASN   C 2  298 ? 0.896   -8.684  -25.518 1.00 60.62  ? 300 ASN   D OD1   1 
ATOM   9200  N  ND2   . ASN   C 2  298 ? 1.100   -7.083  -27.083 1.00 52.06  ? 300 ASN   D ND2   1 
ATOM   9201  N  N     . MET   C 2  299 ? 6.160   -9.374  -25.440 1.00 39.36  ? 301 MET   D N     1 
ATOM   9202  C  CA    . MET   C 2  299 ? 7.596   -9.155  -25.342 1.00 45.73  ? 301 MET   D CA    1 
ATOM   9203  C  C     . MET   C 2  299 ? 8.303   -9.553  -26.641 1.00 54.77  ? 301 MET   D C     1 
ATOM   9204  O  O     . MET   C 2  299 ? 7.880   -10.473 -27.350 1.00 57.54  ? 301 MET   D O     1 
ATOM   9205  C  CB    . MET   C 2  299 ? 8.189   -9.949  -24.169 1.00 52.87  ? 301 MET   D CB    1 
ATOM   9206  C  CG    . MET   C 2  299 ? 7.538   -9.707  -22.778 1.00 60.12  ? 301 MET   D CG    1 
ATOM   9207  S  SD    . MET   C 2  299 ? 7.983   -8.224  -21.824 1.00 44.11  ? 301 MET   D SD    1 
ATOM   9208  C  CE    . MET   C 2  299 ? 7.183   -6.906  -22.756 1.00 39.27  ? 301 MET   D CE    1 
ATOM   9209  N  N     . MET   C 2  300 ? 9.392   -8.846  -26.953 1.00 49.81  ? 302 MET   D N     1 
ATOM   9210  C  CA    . MET   C 2  300 ? 10.239  -9.203  -28.081 1.00 39.26  ? 302 MET   D CA    1 
ATOM   9211  C  C     . MET   C 2  300 ? 11.456  -9.995  -27.649 1.00 42.90  ? 302 MET   D C     1 
ATOM   9212  O  O     . MET   C 2  300 ? 12.445  -10.034 -28.381 1.00 41.91  ? 302 MET   D O     1 
ATOM   9213  C  CB    . MET   C 2  300 ? 10.693  -7.967  -28.854 1.00 33.60  ? 302 MET   D CB    1 
ATOM   9214  C  CG    . MET   C 2  300 ? 9.589   -7.026  -29.240 1.00 36.64  ? 302 MET   D CG    1 
ATOM   9215  S  SD    . MET   C 2  300 ? 8.339   -7.755  -30.287 1.00 49.71  ? 302 MET   D SD    1 
ATOM   9216  C  CE    . MET   C 2  300 ? 7.166   -6.389  -30.415 1.00 38.26  ? 302 MET   D CE    1 
ATOM   9217  N  N     . ALA   C 2  301 ? 11.417  -10.602 -26.468 1.00 44.67  ? 303 ALA   D N     1 
ATOM   9218  C  CA    . ALA   C 2  301 ? 12.461  -11.518 -26.044 1.00 42.89  ? 303 ALA   D CA    1 
ATOM   9219  C  C     . ALA   C 2  301 ? 11.771  -12.675 -25.353 1.00 49.96  ? 303 ALA   D C     1 
ATOM   9220  O  O     . ALA   C 2  301 ? 10.886  -12.452 -24.521 1.00 52.70  ? 303 ALA   D O     1 
ATOM   9221  C  CB    . ALA   C 2  301 ? 13.470  -10.853 -25.107 1.00 39.39  ? 303 ALA   D CB    1 
ATOM   9222  N  N     . ALA   C 2  302 ? 12.167  -13.899 -25.718 1.00 46.55  ? 304 ALA   D N     1 
ATOM   9223  C  CA    . ALA   C 2  302 ? 11.628  -15.147 -25.177 1.00 47.72  ? 304 ALA   D CA    1 
ATOM   9224  C  C     . ALA   C 2  302 ? 11.198  -15.076 -23.714 1.00 55.82  ? 304 ALA   D C     1 
ATOM   9225  O  O     . ALA   C 2  302 ? 10.183  -15.665 -23.332 1.00 78.01  ? 304 ALA   D O     1 
ATOM   9226  C  CB    . ALA   C 2  302 ? 12.660  -16.270 -25.323 1.00 48.78  ? 304 ALA   D CB    1 
ATOM   9227  N  N     . CYS   C 2  303 ? 11.945  -14.341 -22.900 1.00 51.31  ? 305 CYS   D N     1 
ATOM   9228  C  CA    . CYS   C 2  303 ? 11.877  -14.466 -21.449 1.00 52.91  ? 305 CYS   D CA    1 
ATOM   9229  C  C     . CYS   C 2  303 ? 10.486  -14.154 -20.880 1.00 49.78  ? 305 CYS   D C     1 
ATOM   9230  O  O     . CYS   C 2  303 ? 9.695   -13.393 -21.448 1.00 46.22  ? 305 CYS   D O     1 
ATOM   9231  C  CB    . CYS   C 2  303 ? 12.933  -13.551 -20.848 1.00 47.38  ? 305 CYS   D CB    1 
ATOM   9232  S  SG    . CYS   C 2  303 ? 14.243  -13.271 -22.051 1.00 62.36  ? 305 CYS   D SG    1 
ATOM   9233  N  N     . ASP   C 2  304 ? 10.197  -14.762 -19.725 1.00 48.70  ? 306 ASP   D N     1 
ATOM   9234  C  CA    . ASP   C 2  304 ? 8.950   -14.532 -18.998 1.00 57.63  ? 306 ASP   D CA    1 
ATOM   9235  C  C     . ASP   C 2  304 ? 9.180   -13.518 -17.883 1.00 58.62  ? 306 ASP   D C     1 
ATOM   9236  O  O     . ASP   C 2  304 ? 9.965   -13.802 -16.957 1.00 49.93  ? 306 ASP   D O     1 
ATOM   9237  C  CB    . ASP   C 2  304 ? 8.428   -15.850 -18.419 1.00 56.19  ? 306 ASP   D CB    1 
ATOM   9238  C  CG    . ASP   C 2  304 ? 7.058   -15.712 -17.757 1.00 54.02  ? 306 ASP   D CG    1 
ATOM   9239  O  OD1   . ASP   C 2  304 ? 6.948   -14.974 -16.759 1.00 49.95  ? 306 ASP   D OD1   1 
ATOM   9240  O  OD2   . ASP   C 2  304 ? 6.091   -16.345 -18.241 1.00 58.01  ? 306 ASP   D OD2   1 
ATOM   9241  N  N     . PRO   C 2  305 ? 8.526   -12.345 -17.912 1.00 49.79  ? 307 PRO   D N     1 
ATOM   9242  C  CA    . PRO   C 2  305 ? 8.798   -11.329 -16.874 1.00 36.58  ? 307 PRO   D CA    1 
ATOM   9243  C  C     . PRO   C 2  305 ? 8.569   -11.832 -15.456 1.00 41.39  ? 307 PRO   D C     1 
ATOM   9244  O  O     . PRO   C 2  305 ? 9.417   -11.624 -14.578 1.00 42.01  ? 307 PRO   D O     1 
ATOM   9245  C  CB    . PRO   C 2  305 ? 7.842   -10.199 -17.250 1.00 32.60  ? 307 PRO   D CB    1 
ATOM   9246  C  CG    . PRO   C 2  305 ? 7.613   -10.368 -18.700 1.00 48.05  ? 307 PRO   D CG    1 
ATOM   9247  C  CD    . PRO   C 2  305 ? 7.615   -11.844 -18.950 1.00 53.40  ? 307 PRO   D CD    1 
ATOM   9248  N  N     . ARG   C 2  306 ? 7.458   -12.510 -15.209 1.00 41.32  ? 308 ARG   D N     1 
ATOM   9249  C  CA    . ARG   C 2  306 ? 7.142   -13.091 -13.901 1.00 33.59  ? 308 ARG   D CA    1 
ATOM   9250  C  C     . ARG   C 2  306 ? 8.105   -14.253 -13.489 1.00 43.17  ? 308 ARG   D C     1 
ATOM   9251  O  O     . ARG   C 2  306 ? 7.819   -14.975 -12.519 1.00 42.96  ? 308 ARG   D O     1 
ATOM   9252  C  CB    . ARG   C 2  306 ? 5.687   -13.562 -13.888 1.00 30.42  ? 308 ARG   D CB    1 
ATOM   9253  C  CG    . ARG   C 2  306 ? 4.774   -12.571 -14.615 1.00 43.51  ? 308 ARG   D CG    1 
ATOM   9254  C  CD    . ARG   C 2  306 ? 3.399   -12.493 -14.081 1.00 45.32  ? 308 ARG   D CD    1 
ATOM   9255  N  NE    . ARG   C 2  306 ? 2.861   -11.144 -14.236 1.00 55.93  ? 308 ARG   D NE    1 
ATOM   9256  C  CZ    . ARG   C 2  306 ? 2.092   -10.551 -13.322 1.00 78.21  ? 308 ARG   D CZ    1 
ATOM   9257  N  NH1   . ARG   C 2  306 ? 1.724   -11.184 -12.198 1.00 67.15  ? 308 ARG   D NH1   1 
ATOM   9258  N  NH2   . ARG   C 2  306 ? 1.671   -9.300  -13.541 1.00 83.01  ? 308 ARG   D NH2   1 
ATOM   9259  N  N     . HIS   C 2  307 ? 9.230   -14.519 -14.150 1.00 38.86  ? 309 HIS   D N     1 
ATOM   9260  C  CA    . HIS   C 2  307 ? 10.202  -15.461 -13.616 1.00 36.39  ? 309 HIS   D CA    1 
ATOM   9261  C  C     . HIS   C 2  307 ? 11.425  -14.745 -13.090 1.00 39.43  ? 309 HIS   D C     1 
ATOM   9262  O  O     . HIS   C 2  307 ? 12.411  -15.389 -12.707 1.00 43.95  ? 309 HIS   D O     1 
ATOM   9263  C  CB    . HIS   C 2  307 ? 10.615  -16.489 -14.669 1.00 49.60  ? 309 HIS   D CB    1 
ATOM   9264  C  CG    . HIS   C 2  307 ? 9.481   -17.311 -15.214 1.00 51.16  ? 309 HIS   D CG    1 
ATOM   9265  N  ND1   . HIS   C 2  307 ? 9.632   -18.165 -16.284 1.00 43.19  ? 309 HIS   D ND1   1 
ATOM   9266  C  CD2   . HIS   C 2  307 ? 8.182   -17.409 -14.841 1.00 52.62  ? 309 HIS   D CD2   1 
ATOM   9267  C  CE1   . HIS   C 2  307 ? 8.478   -18.755 -16.544 1.00 50.18  ? 309 HIS   D CE1   1 
ATOM   9268  N  NE2   . HIS   C 2  307 ? 7.581   -18.315 -15.682 1.00 44.30  ? 309 HIS   D NE2   1 
ATOM   9269  N  N     . GLY   C 2  308 ? 11.387  -13.430 -13.088 1.00 44.33  ? 310 GLY   D N     1 
ATOM   9270  C  CA    . GLY   C 2  308 ? 12.460  -12.642 -12.534 1.00 46.23  ? 310 GLY   D CA    1 
ATOM   9271  C  C     . GLY   C 2  308 ? 11.931  -11.299 -12.130 1.00 51.66  ? 310 GLY   D C     1 
ATOM   9272  O  O     . GLY   C 2  308 ? 10.722  -11.110 -11.982 1.00 52.34  ? 310 GLY   D O     1 
ATOM   9273  N  N     . ARG   C 2  309 ? 12.841  -10.346 -11.975 1.00 49.49  ? 311 ARG   D N     1 
ATOM   9274  C  CA    . ARG   C 2  309 ? 12.466  -9.027  -11.497 1.00 45.65  ? 311 ARG   D CA    1 
ATOM   9275  C  C     . ARG   C 2  309 ? 12.988  -7.951  -12.437 1.00 40.86  ? 311 ARG   D C     1 
ATOM   9276  O  O     . ARG   C 2  309 ? 14.166  -7.949  -12.814 1.00 39.54  ? 311 ARG   D O     1 
ATOM   9277  C  CB    . ARG   C 2  309 ? 12.966  -8.821  -10.054 1.00 40.51  ? 311 ARG   D CB    1 
ATOM   9278  C  CG    . ARG   C 2  309 ? 12.190  -9.654  -9.041  1.00 43.17  ? 311 ARG   D CG    1 
ATOM   9279  C  CD    . ARG   C 2  309 ? 12.417  -9.212  -7.610  1.00 41.81  ? 311 ARG   D CD    1 
ATOM   9280  N  NE    . ARG   C 2  309 ? 12.874  -10.312 -6.768  1.00 52.41  ? 311 ARG   D NE    1 
ATOM   9281  C  CZ    . ARG   C 2  309 ? 12.110  -11.014 -5.934  1.00 59.46  ? 311 ARG   D CZ    1 
ATOM   9282  N  NH1   . ARG   C 2  309 ? 10.811  -10.777 -5.807  1.00 47.62  ? 311 ARG   D NH1   1 
ATOM   9283  N  NH2   . ARG   C 2  309 ? 12.668  -11.976 -5.198  1.00 52.78  ? 311 ARG   D NH2   1 
ATOM   9284  N  N     . TYR   C 2  310 ? 12.082  -7.065  -12.832 1.00 38.17  ? 312 TYR   D N     1 
ATOM   9285  C  CA    . TYR   C 2  310 ? 12.386  -5.764  -13.409 1.00 35.81  ? 312 TYR   D CA    1 
ATOM   9286  C  C     . TYR   C 2  310 ? 13.311  -4.886  -12.559 1.00 39.55  ? 312 TYR   D C     1 
ATOM   9287  O  O     . TYR   C 2  310 ? 12.876  -4.360  -11.527 1.00 33.29  ? 312 TYR   D O     1 
ATOM   9288  C  CB    . TYR   C 2  310 ? 11.086  -5.015  -13.621 1.00 28.11  ? 312 TYR   D CB    1 
ATOM   9289  C  CG    . TYR   C 2  310 ? 10.223  -5.549  -14.715 1.00 30.90  ? 312 TYR   D CG    1 
ATOM   9290  C  CD1   . TYR   C 2  310 ? 10.755  -5.890  -15.936 1.00 35.00  ? 312 TYR   D CD1   1 
ATOM   9291  C  CD2   . TYR   C 2  310 ? 8.854   -5.692  -14.533 1.00 34.28  ? 312 TYR   D CD2   1 
ATOM   9292  C  CE1   . TYR   C 2  310 ? 9.947   -6.365  -16.960 1.00 37.89  ? 312 TYR   D CE1   1 
ATOM   9293  C  CE2   . TYR   C 2  310 ? 8.037   -6.172  -15.549 1.00 34.04  ? 312 TYR   D CE2   1 
ATOM   9294  C  CZ    . TYR   C 2  310 ? 8.590   -6.500  -16.758 1.00 37.95  ? 312 TYR   D CZ    1 
ATOM   9295  O  OH    . TYR   C 2  310 ? 7.784   -6.959  -17.769 1.00 40.35  ? 312 TYR   D OH    1 
ATOM   9296  N  N     . LEU   C 2  311 ? 14.580  -4.718  -12.993 1.00 39.98  ? 313 LEU   D N     1 
ATOM   9297  C  CA    . LEU   C 2  311 ? 15.492  -3.725  -12.404 1.00 30.26  ? 313 LEU   D CA    1 
ATOM   9298  C  C     . LEU   C 2  311 ? 15.058  -2.300  -12.733 1.00 30.57  ? 313 LEU   D C     1 
ATOM   9299  O  O     . LEU   C 2  311 ? 15.190  -1.390  -11.902 1.00 29.44  ? 313 LEU   D O     1 
ATOM   9300  C  CB    . LEU   C 2  311 ? 16.933  -3.934  -12.898 1.00 21.02  ? 313 LEU   D CB    1 
ATOM   9301  C  CG    . LEU   C 2  311 ? 17.697  -5.201  -12.545 1.00 28.10  ? 313 LEU   D CG    1 
ATOM   9302  C  CD1   . LEU   C 2  311 ? 19.042  -5.233  -13.248 1.00 32.82  ? 313 LEU   D CD1   1 
ATOM   9303  C  CD2   . LEU   C 2  311 ? 17.889  -5.298  -11.046 1.00 32.23  ? 313 LEU   D CD2   1 
ATOM   9304  N  N     . THR   C 2  312 ? 14.585  -2.083  -13.960 1.00 30.97  ? 314 THR   D N     1 
ATOM   9305  C  CA    . THR   C 2  312 ? 14.051  -0.801  -14.402 1.00 28.50  ? 314 THR   D CA    1 
ATOM   9306  C  C     . THR   C 2  312 ? 13.059  -1.056  -15.515 1.00 27.72  ? 314 THR   D C     1 
ATOM   9307  O  O     . THR   C 2  312 ? 13.016  -2.134  -16.101 1.00 33.20  ? 314 THR   D O     1 
ATOM   9308  C  CB    . THR   C 2  312 ? 15.116  0.128   -14.955 1.00 28.01  ? 314 THR   D CB    1 
ATOM   9309  O  OG1   . THR   C 2  312 ? 15.750  -0.545  -16.041 1.00 25.83  ? 314 THR   D OG1   1 
ATOM   9310  C  CG2   . THR   C 2  312 ? 16.139  0.487   -13.886 1.00 28.98  ? 314 THR   D CG2   1 
ATOM   9311  N  N     . VAL   C 2  313 ? 12.280  -0.037  -15.826 1.00 24.89  ? 315 VAL   D N     1 
ATOM   9312  C  CA    . VAL   C 2  313 ? 11.306  -0.113  -16.903 1.00 26.83  ? 315 VAL   D CA    1 
ATOM   9313  C  C     . VAL   C 2  313 ? 11.053  1.299   -17.358 1.00 25.29  ? 315 VAL   D C     1 
ATOM   9314  O  O     . VAL   C 2  313 ? 10.922  2.203   -16.535 1.00 22.69  ? 315 VAL   D O     1 
ATOM   9315  C  CB    . VAL   C 2  313 ? 9.977   -0.766  -16.453 1.00 30.81  ? 315 VAL   D CB    1 
ATOM   9316  C  CG1   . VAL   C 2  313 ? 8.857   -0.472  -17.462 1.00 27.29  ? 315 VAL   D CG1   1 
ATOM   9317  C  CG2   . VAL   C 2  313 ? 10.147  -2.268  -16.209 1.00 31.68  ? 315 VAL   D CG2   1 
ATOM   9318  N  N     . ALA   C 2  314 ? 10.996  1.492   -18.664 1.00 29.24  ? 316 ALA   D N     1 
ATOM   9319  C  CA    . ALA   C 2  314 ? 10.452  2.718   -19.216 1.00 26.63  ? 316 ALA   D CA    1 
ATOM   9320  C  C     . ALA   C 2  314 ? 9.221   2.349   -20.033 1.00 34.54  ? 316 ALA   D C     1 
ATOM   9321  O  O     . ALA   C 2  314 ? 9.149   1.255   -20.600 1.00 36.33  ? 316 ALA   D O     1 
ATOM   9322  C  CB    . ALA   C 2  314 ? 11.496  3.457   -20.057 1.00 24.26  ? 316 ALA   D CB    1 
ATOM   9323  N  N     . ALA   C 2  315 ? 8.236   3.247   -20.063 1.00 34.03  ? 317 ALA   D N     1 
ATOM   9324  C  CA    . ALA   C 2  315 ? 6.961   3.006   -20.733 1.00 28.68  ? 317 ALA   D CA    1 
ATOM   9325  C  C     . ALA   C 2  315 ? 6.621   4.235   -21.553 1.00 34.88  ? 317 ALA   D C     1 
ATOM   9326  O  O     . ALA   C 2  315 ? 6.400   5.308   -20.986 1.00 45.28  ? 317 ALA   D O     1 
ATOM   9327  C  CB    . ALA   C 2  315 ? 5.847   2.712   -19.726 1.00 26.54  ? 317 ALA   D CB    1 
ATOM   9328  N  N     . ILE   C 2  316 ? 6.564   4.088   -22.881 1.00 36.62  ? 318 ILE   D N     1 
ATOM   9329  C  CA    . ILE   C 2  316 ? 6.103   5.162   -23.760 1.00 33.23  ? 318 ILE   D CA    1 
ATOM   9330  C  C     . ILE   C 2  316 ? 4.672   4.870   -24.174 1.00 37.18  ? 318 ILE   D C     1 
ATOM   9331  O  O     . ILE   C 2  316 ? 4.332   3.727   -24.495 1.00 46.58  ? 318 ILE   D O     1 
ATOM   9332  C  CB    . ILE   C 2  316 ? 6.992   5.328   -25.004 1.00 27.39  ? 318 ILE   D CB    1 
ATOM   9333  C  CG1   . ILE   C 2  316 ? 8.462   5.318   -24.618 1.00 38.96  ? 318 ILE   D CG1   1 
ATOM   9334  C  CG2   . ILE   C 2  316 ? 6.655   6.627   -25.710 1.00 27.87  ? 318 ILE   D CG2   1 
ATOM   9335  C  CD1   . ILE   C 2  316 ? 9.049   3.924   -24.498 0.00 36.74  ? 318 ILE   D CD1   1 
ATOM   9336  N  N     . PHE   C 2  317 ? 3.835   5.906   -24.171 1.00 34.23  ? 319 PHE   D N     1 
ATOM   9337  C  CA    . PHE   C 2  317 ? 2.464   5.850   -24.651 1.00 30.41  ? 319 PHE   D CA    1 
ATOM   9338  C  C     . PHE   C 2  317 ? 2.318   6.838   -25.791 1.00 39.19  ? 319 PHE   D C     1 
ATOM   9339  O  O     . PHE   C 2  317 ? 2.740   7.991   -25.673 1.00 44.60  ? 319 PHE   D O     1 
ATOM   9340  C  CB    . PHE   C 2  317 ? 1.474   6.188   -23.537 1.00 32.02  ? 319 PHE   D CB    1 
ATOM   9341  C  CG    . PHE   C 2  317 ? 1.256   5.075   -22.572 1.00 32.77  ? 319 PHE   D CG    1 
ATOM   9342  C  CD1   . PHE   C 2  317 ? 2.059   4.936   -21.456 1.00 36.41  ? 319 PHE   D CD1   1 
ATOM   9343  C  CD2   . PHE   C 2  317 ? 0.251   4.165   -22.776 1.00 33.30  ? 319 PHE   D CD2   1 
ATOM   9344  C  CE1   . PHE   C 2  317 ? 1.865   3.899   -20.558 1.00 36.26  ? 319 PHE   D CE1   1 
ATOM   9345  C  CE2   . PHE   C 2  317 ? 0.050   3.128   -21.883 1.00 45.94  ? 319 PHE   D CE2   1 
ATOM   9346  C  CZ    . PHE   C 2  317 ? 0.862   2.996   -20.769 1.00 36.74  ? 319 PHE   D CZ    1 
ATOM   9347  N  N     . ARG   C 2  318 ? 1.719   6.393   -26.886 1.00 44.25  ? 320 ARG   D N     1 
ATOM   9348  C  CA    . ARG   C 2  318 ? 1.588   7.217   -28.077 1.00 46.96  ? 320 ARG   D CA    1 
ATOM   9349  C  C     . ARG   C 2  318 ? 0.136   7.242   -28.532 1.00 49.86  ? 320 ARG   D C     1 
ATOM   9350  O  O     . ARG   C 2  318 ? -0.556  6.218   -28.511 1.00 45.49  ? 320 ARG   D O     1 
ATOM   9351  C  CB    . ARG   C 2  318 ? 2.485   6.701   -29.193 1.00 43.80  ? 320 ARG   D CB    1 
ATOM   9352  C  CG    . ARG   C 2  318 ? 3.730   5.979   -28.694 1.00 48.87  ? 320 ARG   D CG    1 
ATOM   9353  C  CD    . ARG   C 2  318 ? 4.544   5.507   -29.863 1.00 48.93  ? 320 ARG   D CD    1 
ATOM   9354  N  NE    . ARG   C 2  318 ? 4.694   6.591   -30.823 1.00 50.88  ? 320 ARG   D NE    1 
ATOM   9355  C  CZ    . ARG   C 2  318 ? 5.190   6.449   -32.042 1.00 55.14  ? 320 ARG   D CZ    1 
ATOM   9356  N  NH1   . ARG   C 2  318 ? 5.574   5.264   -32.495 1.00 48.86  ? 320 ARG   D NH1   1 
ATOM   9357  N  NH2   . ARG   C 2  318 ? 5.309   7.522   -32.823 1.00 53.59  ? 320 ARG   D NH2   1 
ATOM   9358  N  N     . GLY   C 2  319 ? -0.312  8.413   -28.948 1.00 47.96  ? 321 GLY   D N     1 
ATOM   9359  C  CA    . GLY   C 2  319 ? -1.683  8.614   -29.358 1.00 52.24  ? 321 GLY   D CA    1 
ATOM   9360  C  C     . GLY   C 2  319 ? -2.435  9.496   -28.380 1.00 57.97  ? 321 GLY   D C     1 
ATOM   9361  O  O     . GLY   C 2  319 ? -2.036  9.686   -27.229 1.00 57.78  ? 321 GLY   D O     1 
ATOM   9362  N  N     . ARG   C 2  320 ? -3.549  10.048  -28.859 1.00 61.03  ? 322 ARG   D N     1 
ATOM   9363  C  CA    . ARG   C 2  320 ? -4.356  10.925  -28.021 1.00 61.17  ? 322 ARG   D CA    1 
ATOM   9364  C  C     . ARG   C 2  320 ? -5.095  10.107  -26.964 1.00 52.86  ? 322 ARG   D C     1 
ATOM   9365  O  O     . ARG   C 2  320 ? -5.694  9.071   -27.268 1.00 59.64  ? 322 ARG   D O     1 
ATOM   9366  C  CB    . ARG   C 2  320 ? -5.336  11.723  -28.877 1.00 63.83  ? 322 ARG   D CB    1 
ATOM   9367  C  CG    . ARG   C 2  320 ? -5.694  13.075  -28.270 1.00 66.70  ? 322 ARG   D CG    1 
ATOM   9368  C  CD    . ARG   C 2  320 ? -4.433  13.868  -27.952 1.00 74.56  ? 322 ARG   D CD    1 
ATOM   9369  N  NE    . ARG   C 2  320 ? -4.701  15.036  -27.120 1.00 87.59  ? 322 ARG   D NE    1 
ATOM   9370  C  CZ    . ARG   C 2  320 ? -3.766  15.734  -26.488 1.00 90.78  ? 322 ARG   D CZ    1 
ATOM   9371  N  NH1   . ARG   C 2  320 ? -2.486  15.409  -26.573 1.00 76.62  ? 322 ARG   D NH1   1 
ATOM   9372  N  NH2   . ARG   C 2  320 ? -4.122  16.783  -25.750 1.00 88.17  ? 322 ARG   D NH2   1 
ATOM   9373  N  N     . MET   C 2  321 ? -5.028  10.561  -25.718 1.00 51.23  ? 323 MET   D N     1 
ATOM   9374  C  CA    . MET   C 2  321 ? -5.580  9.840   -24.575 1.00 45.81  ? 323 MET   D CA    1 
ATOM   9375  C  C     . MET   C 2  321 ? -5.398  10.726  -23.349 1.00 54.25  ? 323 MET   D C     1 
ATOM   9376  O  O     . MET   C 2  321 ? -4.866  11.839  -23.434 1.00 56.56  ? 323 MET   D O     1 
ATOM   9377  C  CB    . MET   C 2  321 ? -4.898  8.489   -24.374 1.00 40.48  ? 323 MET   D CB    1 
ATOM   9378  C  CG    . MET   C 2  321 ? -3.451  8.616   -23.898 1.00 38.37  ? 323 MET   D CG    1 
ATOM   9379  S  SD    . MET   C 2  321 ? -2.472  7.116   -24.073 1.00 50.99  ? 323 MET   D SD    1 
ATOM   9380  C  CE    . MET   C 2  321 ? -2.271  7.028   -25.857 1.00 55.83  ? 323 MET   D CE    1 
ATOM   9381  N  N     . SER   C 2  322 ? -5.833  10.210  -22.198 1.00 52.60  ? 324 SER   D N     1 
ATOM   9382  C  CA    . SER   C 2  322 ? -5.809  10.937  -20.933 1.00 39.61  ? 324 SER   D CA    1 
ATOM   9383  C  C     . SER   C 2  322 ? -4.539  10.573  -20.177 1.00 44.33  ? 324 SER   D C     1 
ATOM   9384  O  O     . SER   C 2  322 ? -4.386  9.443   -19.702 1.00 41.46  ? 324 SER   D O     1 
ATOM   9385  C  CB    . SER   C 2  322 ? -7.035  10.614  -20.087 1.00 39.90  ? 324 SER   D CB    1 
ATOM   9386  O  OG    . SER   C 2  322 ? -6.874  11.100  -18.761 1.00 43.43  ? 324 SER   D OG    1 
ATOM   9387  N  N     . MET   C 2  323 ? -3.637  11.539  -20.045 1.00 48.90  ? 325 MET   D N     1 
ATOM   9388  C  CA    . MET   C 2  323 ? -2.471  11.312  -19.207 1.00 47.67  ? 325 MET   D CA    1 
ATOM   9389  C  C     . MET   C 2  323 ? -2.887  10.962  -17.777 1.00 51.60  ? 325 MET   D C     1 
ATOM   9390  O  O     . MET   C 2  323 ? -2.230  10.144  -17.115 1.00 50.21  ? 325 MET   D O     1 
ATOM   9391  C  CB    . MET   C 2  323 ? -1.568  12.545  -19.255 1.00 40.64  ? 325 MET   D CB    1 
ATOM   9392  C  CG    . MET   C 2  323 ? -0.120  12.251  -18.978 1.00 42.71  ? 325 MET   D CG    1 
ATOM   9393  S  SD    . MET   C 2  323 ? 0.939   13.685  -19.182 1.00 74.40  ? 325 MET   D SD    1 
ATOM   9394  C  CE    . MET   C 2  323 ? -0.019  15.015  -18.436 1.00 44.14  ? 325 MET   D CE    1 
ATOM   9395  N  N     . LYS   C 2  324 ? -3.996  11.542  -17.295 1.00 52.26  ? 326 LYS   D N     1 
ATOM   9396  C  CA    . LYS   C 2  324 ? -4.490  11.207  -15.963 1.00 43.66  ? 326 LYS   D CA    1 
ATOM   9397  C  C     . LYS   C 2  324 ? -4.862  9.735   -15.870 1.00 43.44  ? 326 LYS   D C     1 
ATOM   9398  O  O     . LYS   C 2  324 ? -4.684  9.114   -14.814 1.00 45.10  ? 326 LYS   D O     1 
ATOM   9399  C  CB    . LYS   C 2  324 ? -5.699  12.074  -15.614 1.00 40.35  ? 326 LYS   D CB    1 
ATOM   9400  C  CG    . LYS   C 2  324 ? -6.151  11.925  -14.178 1.00 45.70  ? 326 LYS   D CG    1 
ATOM   9401  C  CD    . LYS   C 2  324 ? -7.660  11.840  -14.062 1.00 50.75  ? 326 LYS   D CD    1 
ATOM   9402  C  CE    . LYS   C 2  324 ? -8.081  11.701  -12.605 1.00 60.17  ? 326 LYS   D CE    1 
ATOM   9403  N  NZ    . LYS   C 2  324 ? -9.313  12.471  -12.261 1.00 74.14  ? 326 LYS   D NZ    1 
ATOM   9404  N  N     . GLU   C 2  325 ? -5.380  9.162   -16.960 1.00 40.78  ? 327 GLU   D N     1 
ATOM   9405  C  CA    . GLU   C 2  325 ? -5.669  7.729   -16.996 1.00 46.84  ? 327 GLU   D CA    1 
ATOM   9406  C  C     . GLU   C 2  325 ? -4.384  6.912   -17.041 1.00 45.35  ? 327 GLU   D C     1 
ATOM   9407  O  O     . GLU   C 2  325 ? -4.261  5.892   -16.347 1.00 37.65  ? 327 GLU   D O     1 
ATOM   9408  C  CB    . GLU   C 2  325 ? -6.551  7.402   -18.209 1.00 46.96  ? 327 GLU   D CB    1 
ATOM   9409  C  CG    . GLU   C 2  325 ? -6.824  5.917   -18.422 1.00 44.09  ? 327 GLU   D CG    1 
ATOM   9410  C  CD    . GLU   C 2  325 ? -8.092  5.681   -19.216 1.00 57.26  ? 327 GLU   D CD    1 
ATOM   9411  O  OE1   . GLU   C 2  325 ? -8.974  6.568   -19.168 1.00 57.30  ? 327 GLU   D OE1   1 
ATOM   9412  O  OE2   . GLU   C 2  325 ? -8.208  4.622   -19.885 1.00 62.55  ? 327 GLU   D OE2   1 
ATOM   9413  N  N     . VAL   C 2  326 ? -3.428  7.335   -17.880 1.00 43.28  ? 328 VAL   D N     1 
ATOM   9414  C  CA    . VAL   C 2  326 ? -2.136  6.663   -17.960 1.00 41.11  ? 328 VAL   D CA    1 
ATOM   9415  C  C     . VAL   C 2  326 ? -1.500  6.608   -16.582 1.00 38.94  ? 328 VAL   D C     1 
ATOM   9416  O  O     . VAL   C 2  326 ? -0.992  5.564   -16.150 1.00 39.61  ? 328 VAL   D O     1 
ATOM   9417  C  CB    . VAL   C 2  326 ? -1.226  7.384   -18.976 1.00 46.64  ? 328 VAL   D CB    1 
ATOM   9418  C  CG1   . VAL   C 2  326 ? -0.034  6.513   -19.355 1.00 35.91  ? 328 VAL   D CG1   1 
ATOM   9419  C  CG2   . VAL   C 2  326 ? -2.018  7.814   -20.206 1.00 39.04  ? 328 VAL   D CG2   1 
ATOM   9420  N  N     . ASP   C 2  327 ? -1.544  7.729   -15.860 1.00 36.99  ? 329 ASP   D N     1 
ATOM   9421  C  CA    . ASP   C 2  327 ? -0.940  7.787   -14.536 1.00 33.61  ? 329 ASP   D CA    1 
ATOM   9422  C  C     . ASP   C 2  327 ? -1.591  6.787   -13.588 1.00 32.89  ? 329 ASP   D C     1 
ATOM   9423  O  O     . ASP   C 2  327 ? -0.903  5.970   -12.969 1.00 32.46  ? 329 ASP   D O     1 
ATOM   9424  C  CB    . ASP   C 2  327 ? -1.036  9.207   -14.002 1.00 34.74  ? 329 ASP   D CB    1 
ATOM   9425  C  CG    . ASP   C 2  327 ? -0.166  10.168  -14.775 1.00 37.60  ? 329 ASP   D CG    1 
ATOM   9426  O  OD1   . ASP   C 2  327 ? 0.478   9.717   -15.735 1.00 36.08  ? 329 ASP   D OD1   1 
ATOM   9427  O  OD2   . ASP   C 2  327 ? -0.107  11.368  -14.423 1.00 47.97  ? 329 ASP   D OD2   1 
ATOM   9428  N  N     . GLU   C 2  328 ? -2.924  6.831   -13.473 1.00 40.37  ? 330 GLU   D N     1 
ATOM   9429  C  CA    . GLU   C 2  328 ? -3.641  5.853   -12.656 1.00 39.51  ? 330 GLU   D CA    1 
ATOM   9430  C  C     . GLU   C 2  328 ? -3.342  4.433   -13.117 1.00 39.01  ? 330 GLU   D C     1 
ATOM   9431  O  O     . GLU   C 2  328 ? -3.244  3.507   -12.300 1.00 40.09  ? 330 GLU   D O     1 
ATOM   9432  C  CB    . GLU   C 2  328 ? -5.155  6.098   -12.708 1.00 38.06  ? 330 GLU   D CB    1 
ATOM   9433  C  CG    . GLU   C 2  328 ? -5.716  7.343   -12.012 1.00 42.58  ? 330 GLU   D CG    1 
ATOM   9434  C  CD    . GLU   C 2  328 ? -7.097  7.740   -12.568 1.00 61.89  ? 330 GLU   D CD    1 
ATOM   9435  O  OE1   . GLU   C 2  328 ? -7.738  6.905   -13.254 1.00 63.14  ? 330 GLU   D OE1   1 
ATOM   9436  O  OE2   . GLU   C 2  328 ? -7.545  8.887   -12.339 1.00 47.19  ? 330 GLU   D OE2   1 
ATOM   9437  N  N     . GLN   C 2  329 ? -3.211  4.232   -14.425 1.00 39.97  ? 331 GLN   D N     1 
ATOM   9438  C  CA    . GLN   C 2  329 ? -3.100  2.861   -14.908 1.00 42.28  ? 331 GLN   D CA    1 
ATOM   9439  C  C     . GLN   C 2  329 ? -1.686  2.330   -14.743 1.00 37.81  ? 331 GLN   D C     1 
ATOM   9440  O  O     . GLN   C 2  329 ? -1.504  1.159   -14.391 1.00 39.76  ? 331 GLN   D O     1 
ATOM   9441  C  CB    . GLN   C 2  329 ? -3.570  2.766   -16.359 1.00 43.69  ? 331 GLN   D CB    1 
ATOM   9442  C  CG    . GLN   C 2  329 ? -5.077  2.927   -16.511 1.00 44.31  ? 331 GLN   D CG    1 
ATOM   9443  C  CD    . GLN   C 2  329 ? -5.846  2.041   -15.551 1.00 48.16  ? 331 GLN   D CD    1 
ATOM   9444  O  OE1   . GLN   C 2  329 ? -5.511  0.873   -15.362 1.00 49.00  ? 331 GLN   D OE1   1 
ATOM   9445  N  NE2   . GLN   C 2  329 ? -6.873  2.600   -14.923 1.00 52.38  ? 331 GLN   D NE2   1 
ATOM   9446  N  N     . MET   C 2  330 ? -0.673  3.171   -14.969 1.00 38.83  ? 332 MET   D N     1 
ATOM   9447  C  CA    . MET   C 2  330 ? 0.689   2.757   -14.645 1.00 34.43  ? 332 MET   D CA    1 
ATOM   9448  C  C     . MET   C 2  330 ? 0.852   2.548   -13.134 1.00 38.58  ? 332 MET   D C     1 
ATOM   9449  O  O     . MET   C 2  330 ? 1.633   1.688   -12.695 1.00 31.16  ? 332 MET   D O     1 
ATOM   9450  C  CB    . MET   C 2  330 ? 1.684   3.789   -15.181 1.00 27.72  ? 332 MET   D CB    1 
ATOM   9451  C  CG    . MET   C 2  330 ? 1.963   3.681   -16.666 1.00 34.87  ? 332 MET   D CG    1 
ATOM   9452  S  SD    . MET   C 2  330 ? 2.545   2.040   -17.144 1.00 40.89  ? 332 MET   D SD    1 
ATOM   9453  C  CE    . MET   C 2  330 ? 4.150   1.986   -16.322 1.00 27.37  ? 332 MET   D CE    1 
ATOM   9454  N  N     . LEU   C 2  331 ? 0.104   3.311   -12.326 1.00 37.42  ? 333 LEU   D N     1 
ATOM   9455  C  CA    . LEU   C 2  331 ? 0.117   3.110   -10.882 1.00 30.49  ? 333 LEU   D CA    1 
ATOM   9456  C  C     . LEU   C 2  331 ? -0.413  1.736   -10.502 1.00 36.65  ? 333 LEU   D C     1 
ATOM   9457  O  O     . LEU   C 2  331 ? 0.196   1.042   -9.681  1.00 35.77  ? 333 LEU   D O     1 
ATOM   9458  C  CB    . LEU   C 2  331 ? -0.689  4.208   -10.189 1.00 29.84  ? 333 LEU   D CB    1 
ATOM   9459  C  CG    . LEU   C 2  331 ? 0.161   5.438   -9.882  1.00 27.53  ? 333 LEU   D CG    1 
ATOM   9460  C  CD1   . LEU   C 2  331 ? -0.627  6.519   -9.179  1.00 23.99  ? 333 LEU   D CD1   1 
ATOM   9461  C  CD2   . LEU   C 2  331 ? 1.331   4.988   -9.052  1.00 15.50  ? 333 LEU   D CD2   1 
ATOM   9462  N  N     . ASN   C 2  332 ? -1.550  1.319   -11.076 1.00 36.12  ? 334 ASN   D N     1 
ATOM   9463  C  CA    . ASN   C 2  332 ? -2.120  0.047   -10.637 1.00 35.68  ? 334 ASN   D CA    1 
ATOM   9464  C  C     . ASN   C 2  332 ? -1.291  -1.136  -11.138 1.00 35.54  ? 334 ASN   D C     1 
ATOM   9465  O  O     . ASN   C 2  332 ? -1.217  -2.159  -10.451 1.00 30.48  ? 334 ASN   D O     1 
ATOM   9466  C  CB    . ASN   C 2  332 ? -3.620  -0.036  -11.013 1.00 30.89  ? 334 ASN   D CB    1 
ATOM   9467  C  CG    . ASN   C 2  332 ? -3.885  -0.654  -12.367 0.00 42.03  ? 334 ASN   D CG    1 
ATOM   9468  O  OD1   . ASN   C 2  332 ? -3.555  -0.071  -13.402 1.00 54.45  ? 334 ASN   D OD1   1 
ATOM   9469  N  ND2   . ASN   C 2  332 ? -4.549  -1.814  -12.369 1.00 47.95  ? 334 ASN   D ND2   1 
ATOM   9470  N  N     . VAL   C 2  333 ? -0.581  -1.000  -12.264 1.00 36.05  ? 335 VAL   D N     1 
ATOM   9471  C  CA    . VAL   C 2  333 ? 0.327   -2.075  -12.653 1.00 30.94  ? 335 VAL   D CA    1 
ATOM   9472  C  C     . VAL   C 2  333 ? 1.307   -2.354  -11.530 1.00 32.03  ? 335 VAL   D C     1 
ATOM   9473  O  O     . VAL   C 2  333 ? 1.444   -3.487  -11.062 1.00 36.77  ? 335 VAL   D O     1 
ATOM   9474  C  CB    . VAL   C 2  333 ? 1.065   -1.743  -13.957 1.00 35.59  ? 335 VAL   D CB    1 
ATOM   9475  C  CG1   . VAL   C 2  333 ? 2.036   -2.857  -14.271 1.00 34.63  ? 335 VAL   D CG1   1 
ATOM   9476  C  CG2   . VAL   C 2  333 ? 0.098   -1.606  -15.085 1.00 36.35  ? 335 VAL   D CG2   1 
ATOM   9477  N  N     . GLN   C 2  334 ? 1.975   -1.316  -11.052 1.00 37.37  ? 336 GLN   D N     1 
ATOM   9478  C  CA    . GLN   C 2  334 ? 3.001   -1.506  -10.037 1.00 32.40  ? 336 GLN   D CA    1 
ATOM   9479  C  C     . GLN   C 2  334 ? 2.410   -1.998  -8.719  1.00 35.75  ? 336 GLN   D C     1 
ATOM   9480  O  O     . GLN   C 2  334 ? 2.944   -2.936  -8.112  1.00 34.10  ? 336 GLN   D O     1 
ATOM   9481  C  CB    . GLN   C 2  334 ? 3.753   -0.201  -9.860  1.00 28.08  ? 336 GLN   D CB    1 
ATOM   9482  C  CG    . GLN   C 2  334 ? 4.209   0.372   -11.189 1.00 26.21  ? 336 GLN   D CG    1 
ATOM   9483  C  CD    . GLN   C 2  334 ? 5.009   1.620   -11.015 1.00 24.21  ? 336 GLN   D CD    1 
ATOM   9484  O  OE1   . GLN   C 2  334 ? 6.190   1.576   -10.634 1.00 23.48  ? 336 GLN   D OE1   1 
ATOM   9485  N  NE2   . GLN   C 2  334 ? 4.373   2.760   -11.272 1.00 25.59  ? 336 GLN   D NE2   1 
ATOM   9486  N  N     . ASN   C 2  335 ? 1.303   -1.394  -8.267  1.00 37.44  ? 337 ASN   D N     1 
ATOM   9487  C  CA    . ASN   C 2  335 ? 0.619   -1.887  -7.071  1.00 32.55  ? 337 ASN   D CA    1 
ATOM   9488  C  C     . ASN   C 2  335 ? 0.342   -3.385  -7.173  1.00 42.00  ? 337 ASN   D C     1 
ATOM   9489  O  O     . ASN   C 2  335 ? 0.816   -4.179  -6.344  1.00 38.64  ? 337 ASN   D O     1 
ATOM   9490  C  CB    . ASN   C 2  335 ? -0.681  -1.116  -6.850  1.00 34.69  ? 337 ASN   D CB    1 
ATOM   9491  C  CG    . ASN   C 2  335 ? -0.446  0.350   -6.486  1.00 55.49  ? 337 ASN   D CG    1 
ATOM   9492  O  OD1   . ASN   C 2  335 ? 0.657   0.736   -6.068  1.00 53.25  ? 337 ASN   D OD1   1 
ATOM   9493  N  ND2   . ASN   C 2  335 ? -1.490  1.176   -6.642  0.74 41.20  ? 337 ASN   D ND2   1 
ATOM   9494  N  N     . LYS   C 2  336 ? -0.420  -3.795  -8.199  1.00 31.40  ? 338 LYS   D N     1 
ATOM   9495  C  CA    . LYS   C 2  336 ? -0.881  -5.174  -8.294  1.00 33.72  ? 338 LYS   D CA    1 
ATOM   9496  C  C     . LYS   C 2  336 ? 0.223   -6.149  -8.714  1.00 41.13  ? 338 LYS   D C     1 
ATOM   9497  O  O     . LYS   C 2  336 ? 0.031   -7.364  -8.582  1.00 43.04  ? 338 LYS   D O     1 
ATOM   9498  C  CB    . LYS   C 2  336 ? -2.099  -5.253  -9.233  1.00 24.27  ? 338 LYS   D CB    1 
ATOM   9499  N  N     . ASN   C 2  337 ? 1.389   -5.658  -9.158  1.00 41.40  ? 339 ASN   D N     1 
ATOM   9500  C  CA    . ASN   C 2  337 ? 2.534   -6.508  -9.498  1.00 37.20  ? 339 ASN   D CA    1 
ATOM   9501  C  C     . ASN   C 2  337 ? 3.783   -6.116  -8.714  1.00 45.01  ? 339 ASN   D C     1 
ATOM   9502  O  O     . ASN   C 2  337 ? 4.885   -6.070  -9.278  1.00 44.54  ? 339 ASN   D O     1 
ATOM   9503  C  CB    . ASN   C 2  337 ? 2.853   -6.436  -10.991 1.00 38.96  ? 339 ASN   D CB    1 
ATOM   9504  C  CG    . ASN   C 2  337 ? 1.671   -6.798  -11.858 1.00 44.96  ? 339 ASN   D CG    1 
ATOM   9505  O  OD1   . ASN   C 2  337 ? 0.925   -7.721  -11.543 1.00 52.24  ? 339 ASN   D OD1   1 
ATOM   9506  N  ND2   . ASN   C 2  337 ? 1.496   -6.078  -12.963 1.00 54.15  ? 339 ASN   D ND2   1 
ATOM   9507  N  N     . SER   C 2  338 ? 3.613   -5.871  -7.407  1.00 44.76  ? 340 SER   D N     1 
ATOM   9508  C  CA    . SER   C 2  338 ? 4.688   -5.370  -6.549  1.00 34.07  ? 340 SER   D CA    1 
ATOM   9509  C  C     . SER   C 2  338 ? 5.923   -6.271  -6.560  1.00 37.12  ? 340 SER   D C     1 
ATOM   9510  O  O     . SER   C 2  338 ? 7.059   -5.785  -6.499  1.00 43.59  ? 340 SER   D O     1 
ATOM   9511  C  CB    . SER   C 2  338 ? 4.163   -5.227  -5.122  1.00 39.18  ? 340 SER   D CB    1 
ATOM   9512  O  OG    . SER   C 2  338 ? 3.664   -6.475  -4.647  1.00 45.97  ? 340 SER   D OG    1 
ATOM   9513  N  N     . SER   C 2  339 ? 5.730   -7.586  -6.616  1.00 44.77  ? 341 SER   D N     1 
ATOM   9514  C  CA    . SER   C 2  339 ? 6.857   -8.497  -6.451  1.00 39.46  ? 341 SER   D CA    1 
ATOM   9515  C  C     . SER   C 2  339 ? 7.833   -8.452  -7.630  1.00 42.85  ? 341 SER   D C     1 
ATOM   9516  O  O     . SER   C 2  339 ? 9.030   -8.711  -7.447  1.00 37.02  ? 341 SER   D O     1 
ATOM   9517  C  CB    . SER   C 2  339 ? 6.332   -9.912  -6.251  1.00 41.66  ? 341 SER   D CB    1 
ATOM   9518  O  OG    . SER   C 2  339 ? 5.216   -9.892  -5.382  1.00 38.36  ? 341 SER   D OG    1 
ATOM   9519  N  N     . TYR   C 2  340 ? 7.364   -8.143  -8.843  1.00 31.50  ? 342 TYR   D N     1 
ATOM   9520  C  CA    . TYR   C 2  340 ? 8.240   -8.238  -10.004 1.00 41.34  ? 342 TYR   D CA    1 
ATOM   9521  C  C     . TYR   C 2  340 ? 8.969   -6.934  -10.297 1.00 45.89  ? 342 TYR   D C     1 
ATOM   9522  O  O     . TYR   C 2  340 ? 9.288   -6.643  -11.463 1.00 42.53  ? 342 TYR   D O     1 
ATOM   9523  C  CB    . TYR   C 2  340 ? 7.450   -8.719  -11.219 1.00 38.50  ? 342 TYR   D CB    1 
ATOM   9524  C  CG    . TYR   C 2  340 ? 6.665   -9.997  -10.959 1.00 47.38  ? 342 TYR   D CG    1 
ATOM   9525  C  CD1   . TYR   C 2  340 ? 7.298   -11.217 -10.794 1.00 38.23  ? 342 TYR   D CD1   1 
ATOM   9526  C  CD2   . TYR   C 2  340 ? 5.294   -9.969  -10.864 1.00 48.60  ? 342 TYR   D CD2   1 
ATOM   9527  C  CE1   . TYR   C 2  340 ? 6.581   -12.385 -10.550 1.00 43.33  ? 342 TYR   D CE1   1 
ATOM   9528  C  CE2   . TYR   C 2  340 ? 4.560   -11.117 -10.591 1.00 45.45  ? 342 TYR   D CE2   1 
ATOM   9529  C  CZ    . TYR   C 2  340 ? 5.194   -12.336 -10.464 1.00 43.44  ? 342 TYR   D CZ    1 
ATOM   9530  O  OH    . TYR   C 2  340 ? 4.395   -13.433 -10.222 1.00 38.97  ? 342 TYR   D OH    1 
ATOM   9531  N  N     . PHE   C 2  341 ? 9.230   -6.144  -9.258  1.00 41.95  ? 343 PHE   D N     1 
ATOM   9532  C  CA    . PHE   C 2  341 ? 9.984   -4.903  -9.345  1.00 37.11  ? 343 PHE   D CA    1 
ATOM   9533  C  C     . PHE   C 2  341 ? 10.921  -4.858  -8.150  1.00 30.80  ? 343 PHE   D C     1 
ATOM   9534  O  O     . PHE   C 2  341 ? 10.455  -4.850  -7.010  1.00 32.00  ? 343 PHE   D O     1 
ATOM   9535  C  CB    . PHE   C 2  341 ? 9.058   -3.687  -9.308  1.00 32.53  ? 343 PHE   D CB    1 
ATOM   9536  C  CG    . PHE   C 2  341 ? 8.189   -3.502  -10.524 1.00 28.70  ? 343 PHE   D CG    1 
ATOM   9537  C  CD1   . PHE   C 2  341 ? 6.967   -4.126  -10.622 1.00 29.71  ? 343 PHE   D CD1   1 
ATOM   9538  C  CD2   . PHE   C 2  341 ? 8.558   -2.610  -11.524 1.00 31.21  ? 343 PHE   D CD2   1 
ATOM   9539  C  CE1   . PHE   C 2  341 ? 6.151   -3.901  -11.731 1.00 36.64  ? 343 PHE   D CE1   1 
ATOM   9540  C  CE2   . PHE   C 2  341 ? 7.755   -2.396  -12.633 1.00 24.65  ? 343 PHE   D CE2   1 
ATOM   9541  C  CZ    . PHE   C 2  341 ? 6.556   -3.032  -12.741 1.00 26.88  ? 343 PHE   D CZ    1 
ATOM   9542  N  N     . VAL   C 2  342 ? 12.232  -4.822  -8.400  1.00 28.73  ? 344 VAL   D N     1 
ATOM   9543  C  CA    . VAL   C 2  342 ? 13.178  -4.699  -7.297  1.00 33.38  ? 344 VAL   D CA    1 
ATOM   9544  C  C     . VAL   C 2  342 ? 12.718  -3.618  -6.319  1.00 30.90  ? 344 VAL   D C     1 
ATOM   9545  O  O     . VAL   C 2  342 ? 12.327  -2.512  -6.707  1.00 32.97  ? 344 VAL   D O     1 
ATOM   9546  C  CB    . VAL   C 2  342 ? 14.595  -4.398  -7.817  1.00 24.20  ? 344 VAL   D CB    1 
ATOM   9547  C  CG1   . VAL   C 2  342 ? 15.293  -5.664  -8.195  1.00 33.08  ? 344 VAL   D CG1   1 
ATOM   9548  C  CG2   . VAL   C 2  342 ? 14.524  -3.456  -8.989  1.00 25.27  ? 344 VAL   D CG2   1 
ATOM   9549  N  N     . GLU   C 2  343 ? 12.764  -3.943  -5.037  1.00 28.93  ? 345 GLU   D N     1 
ATOM   9550  C  CA    . GLU   C 2  343 ? 12.380  -3.001  -4.005  1.00 26.23  ? 345 GLU   D CA    1 
ATOM   9551  C  C     . GLU   C 2  343 ? 13.528  -2.093  -3.584  1.00 30.34  ? 345 GLU   D C     1 
ATOM   9552  O  O     . GLU   C 2  343 ? 13.291  -1.095  -2.897  1.00 35.36  ? 345 GLU   D O     1 
ATOM   9553  C  CB    . GLU   C 2  343 ? 11.831  -3.768  -2.793  1.00 26.48  ? 345 GLU   D CB    1 
ATOM   9554  C  CG    . GLU   C 2  343 ? 12.682  -4.984  -2.430  1.00 41.92  ? 345 GLU   D CG    1 
ATOM   9555  C  CD    . GLU   C 2  343 ? 12.707  -5.309  -0.938  1.00 50.57  ? 345 GLU   D CD    1 
ATOM   9556  O  OE1   . GLU   C 2  343 ? 11.633  -5.313  -0.291  1.00 50.18  ? 345 GLU   D OE1   1 
ATOM   9557  O  OE2   . GLU   C 2  343 ? 13.818  -5.568  -0.418  1.00 54.02  ? 345 GLU   D OE2   1 
ATOM   9558  N  N     . TRP   C 2  344 ? 14.761  -2.400  -3.960  1.00 27.17  ? 346 TRP   D N     1 
ATOM   9559  C  CA    . TRP   C 2  344 ? 15.865  -1.523  -3.598  1.00 32.11  ? 346 TRP   D CA    1 
ATOM   9560  C  C     . TRP   C 2  344 ? 16.216  -0.505  -4.687  1.00 32.03  ? 346 TRP   D C     1 
ATOM   9561  O  O     . TRP   C 2  344 ? 17.256  0.153   -4.571  1.00 32.74  ? 346 TRP   D O     1 
ATOM   9562  C  CB    . TRP   C 2  344 ? 17.098  -2.348  -3.232  1.00 34.14  ? 346 TRP   D CB    1 
ATOM   9563  C  CG    . TRP   C 2  344 ? 17.251  -3.494  -4.117  1.00 30.88  ? 346 TRP   D CG    1 
ATOM   9564  C  CD1   . TRP   C 2  344 ? 16.638  -4.684  -3.998  1.00 36.51  ? 346 TRP   D CD1   1 
ATOM   9565  C  CD2   . TRP   C 2  344 ? 18.057  -3.563  -5.293  1.00 39.09  ? 346 TRP   D CD2   1 
ATOM   9566  N  NE1   . TRP   C 2  344 ? 17.007  -5.512  -5.028  1.00 52.91  ? 346 TRP   D NE1   1 
ATOM   9567  C  CE2   . TRP   C 2  344 ? 17.880  -4.846  -5.842  1.00 41.98  ? 346 TRP   D CE2   1 
ATOM   9568  C  CE3   . TRP   C 2  344 ? 18.915  -2.665  -5.935  1.00 39.90  ? 346 TRP   D CE3   1 
ATOM   9569  C  CZ2   . TRP   C 2  344 ? 18.524  -5.260  -6.996  1.00 33.11  ? 346 TRP   D CZ2   1 
ATOM   9570  C  CZ3   . TRP   C 2  344 ? 19.548  -3.072  -7.083  1.00 36.45  ? 346 TRP   D CZ3   1 
ATOM   9571  C  CH2   . TRP   C 2  344 ? 19.354  -4.363  -7.599  1.00 40.18  ? 346 TRP   D CH2   1 
ATOM   9572  N  N     . ILE   C 2  345 ? 15.391  -0.371  -5.723  1.00 23.30  ? 347 ILE   D N     1 
ATOM   9573  C  CA    . ILE   C 2  345 ? 15.420  0.769   -6.629  1.00 21.34  ? 347 ILE   D CA    1 
ATOM   9574  C  C     . ILE   C 2  345 ? 14.045  1.428   -6.629  1.00 22.45  ? 347 ILE   D C     1 
ATOM   9575  O  O     . ILE   C 2  345 ? 13.133  0.991   -7.325  1.00 21.69  ? 347 ILE   D O     1 
ATOM   9576  C  CB    . ILE   C 2  345 ? 15.820  0.360   -8.053  1.00 21.25  ? 347 ILE   D CB    1 
ATOM   9577  C  CG1   . ILE   C 2  345 ? 17.250  -0.144  -8.086  1.00 24.23  ? 347 ILE   D CG1   1 
ATOM   9578  C  CG2   . ILE   C 2  345 ? 15.623  1.533   -8.969  1.00 21.07  ? 347 ILE   D CG2   1 
ATOM   9579  C  CD1   . ILE   C 2  345 ? 17.611  -0.737  -9.412  1.00 22.32  ? 347 ILE   D CD1   1 
ATOM   9580  N  N     . PRO   C 2  346 ? 13.869  2.513   -5.889  1.00 21.49  ? 348 PRO   D N     1 
ATOM   9581  C  CA    . PRO   C 2  346 ? 12.567  3.176   -5.866  1.00 17.63  ? 348 PRO   D CA    1 
ATOM   9582  C  C     . PRO   C 2  346 ? 12.258  3.858   -7.191  1.00 19.64  ? 348 PRO   D C     1 
ATOM   9583  O  O     . PRO   C 2  346 ? 13.145  4.220   -7.971  1.00 23.32  ? 348 PRO   D O     1 
ATOM   9584  C  CB    . PRO   C 2  346 ? 12.710  4.209   -4.744  1.00 12.95  ? 348 PRO   D CB    1 
ATOM   9585  C  CG    . PRO   C 2  346 ? 13.973  3.904   -4.081  1.00 20.62  ? 348 PRO   D CG    1 
ATOM   9586  C  CD    . PRO   C 2  346 ? 14.847  3.208   -5.049  1.00 18.70  ? 348 PRO   D CD    1 
ATOM   9587  N  N     . ASN   C 2  347 ? 10.963  4.035   -7.422  1.00 18.38  ? 349 ASN   D N     1 
ATOM   9588  C  CA    . ASN   C 2  347 ? 10.429  4.782   -8.555  1.00 20.99  ? 349 ASN   D CA    1 
ATOM   9589  C  C     . ASN   C 2  347 ? 11.208  4.490   -9.831  1.00 25.98  ? 349 ASN   D C     1 
ATOM   9590  O  O     . ASN   C 2  347 ? 11.734  5.389   -10.491 1.00 22.48  ? 349 ASN   D O     1 
ATOM   9591  C  CB    . ASN   C 2  347 ? 10.424  6.272   -8.250  1.00 21.10  ? 349 ASN   D CB    1 
ATOM   9592  C  CG    . ASN   C 2  347 ? 9.994   6.568   -6.827  1.00 21.61  ? 349 ASN   D CG    1 
ATOM   9593  O  OD1   . ASN   C 2  347 ? 10.821  6.651   -5.935  1.00 18.80  ? 349 ASN   D OD1   1 
ATOM   9594  N  ND2   . ASN   C 2  347 ? 8.696   6.728   -6.614  1.00 18.91  ? 349 ASN   D ND2   1 
ATOM   9595  N  N     . ASN   C 2  348 ? 11.254  3.200   -10.192 1.00 23.78  ? 350 ASN   D N     1 
ATOM   9596  C  CA    . ASN   C 2  348 ? 12.093  2.760   -11.298 1.00 21.80  ? 350 ASN   D CA    1 
ATOM   9597  C  C     . ASN   C 2  348 ? 11.291  2.462   -12.569 1.00 25.28  ? 350 ASN   D C     1 
ATOM   9598  O  O     . ASN   C 2  348 ? 11.794  1.789   -13.471 1.00 29.65  ? 350 ASN   D O     1 
ATOM   9599  C  CB    . ASN   C 2  348 ? 12.926  1.557   -10.861 1.00 20.35  ? 350 ASN   D CB    1 
ATOM   9600  C  CG    . ASN   C 2  348 ? 12.090  0.336   -10.621 1.00 27.25  ? 350 ASN   D CG    1 
ATOM   9601  O  OD1   . ASN   C 2  348 ? 10.886  0.339   -10.880 1.00 29.00  ? 350 ASN   D OD1   1 
ATOM   9602  N  ND2   . ASN   C 2  348 ? 12.725  -0.738  -10.144 1.00 26.31  ? 350 ASN   D ND2   1 
ATOM   9603  N  N     . VAL   C 2  349 ? 10.057  2.950   -12.656 1.00 29.89  ? 351 VAL   D N     1 
ATOM   9604  C  CA    . VAL   C 2  349 ? 9.199   2.786   -13.837 1.00 24.57  ? 351 VAL   D CA    1 
ATOM   9605  C  C     . VAL   C 2  349 ? 8.836   4.195   -14.303 1.00 28.48  ? 351 VAL   D C     1 
ATOM   9606  O  O     . VAL   C 2  349 ? 7.900   4.834   -13.791 1.00 25.40  ? 351 VAL   D O     1 
ATOM   9607  C  CB    . VAL   C 2  349 ? 7.947   1.945   -13.548 1.00 21.79  ? 351 VAL   D CB    1 
ATOM   9608  C  CG1   . VAL   C 2  349 ? 6.965   1.984   -14.723 1.00 18.28  ? 351 VAL   D CG1   1 
ATOM   9609  C  CG2   . VAL   C 2  349 ? 8.312   0.526   -13.189 1.00 18.77  ? 351 VAL   D CG2   1 
ATOM   9610  N  N     . LYS   C 2  350 ? 9.596   4.695   -15.274 1.00 25.90  ? 352 LYS   D N     1 
ATOM   9611  C  CA    . LYS   C 2  350 ? 9.351   5.985   -15.903 1.00 30.58  ? 352 LYS   D CA    1 
ATOM   9612  C  C     . LYS   C 2  350 ? 8.373   5.845   -17.077 1.00 29.98  ? 352 LYS   D C     1 
ATOM   9613  O  O     . LYS   C 2  350 ? 8.345   4.820   -17.762 1.00 29.35  ? 352 LYS   D O     1 
ATOM   9614  C  CB    . LYS   C 2  350 ? 10.684  6.586   -16.352 1.00 26.14  ? 352 LYS   D CB    1 
ATOM   9615  C  CG    . LYS   C 2  350 ? 11.510  7.086   -15.188 1.00 25.23  ? 352 LYS   D CG    1 
ATOM   9616  C  CD    . LYS   C 2  350 ? 10.640  7.948   -14.282 1.00 27.15  ? 352 LYS   D CD    1 
ATOM   9617  C  CE    . LYS   C 2  350 ? 11.376  8.408   -13.022 1.00 31.85  ? 352 LYS   D CE    1 
ATOM   9618  N  NZ    . LYS   C 2  350 ? 12.054  7.290   -12.306 1.00 27.98  ? 352 LYS   D NZ    1 
ATOM   9619  N  N     . THR   C 2  351 ? 7.536   6.869   -17.279 1.00 24.25  ? 353 THR   D N     1 
ATOM   9620  C  CA    . THR   C 2  351 ? 6.495   6.822   -18.302 1.00 29.45  ? 353 THR   D CA    1 
ATOM   9621  C  C     . THR   C 2  351 ? 6.529   8.103   -19.117 1.00 33.78  ? 353 THR   D C     1 
ATOM   9622  O  O     . THR   C 2  351 ? 6.564   9.197   -18.548 1.00 31.38  ? 353 THR   D O     1 
ATOM   9623  C  CB    . THR   C 2  351 ? 5.069   6.661   -17.726 1.00 32.04  ? 353 THR   D CB    1 
ATOM   9624  O  OG1   . THR   C 2  351 ? 4.974   5.510   -16.884 1.00 35.01  ? 353 THR   D OG1   1 
ATOM   9625  C  CG2   . THR   C 2  351 ? 4.085   6.469   -18.856 1.00 35.30  ? 353 THR   D CG2   1 
ATOM   9626  N  N     . ALA   C 2  352 ? 6.490   7.963   -20.444 1.00 35.74  ? 354 ALA   D N     1 
ATOM   9627  C  CA    . ALA   C 2  352 ? 6.344   9.073   -21.372 1.00 33.83  ? 354 ALA   D CA    1 
ATOM   9628  C  C     . ALA   C 2  352 ? 4.967   9.007   -22.023 1.00 40.85  ? 354 ALA   D C     1 
ATOM   9629  O  O     . ALA   C 2  352 ? 4.308   7.963   -22.003 1.00 40.93  ? 354 ALA   D O     1 
ATOM   9630  C  CB    . ALA   C 2  352 ? 7.444   9.047   -22.436 1.00 31.37  ? 354 ALA   D CB    1 
ATOM   9631  N  N     . VAL   C 2  353 ? 4.515   10.150  -22.563 1.00 39.46  ? 355 VAL   D N     1 
ATOM   9632  C  CA    . VAL   C 2  353 ? 3.259   10.236  -23.313 1.00 39.26  ? 355 VAL   D CA    1 
ATOM   9633  C  C     . VAL   C 2  353 ? 3.458   11.135  -24.523 1.00 46.56  ? 355 VAL   D C     1 
ATOM   9634  O  O     . VAL   C 2  353 ? 3.420   12.364  -24.395 1.00 45.06  ? 355 VAL   D O     1 
ATOM   9635  C  CB    . VAL   C 2  353 ? 2.095   10.781  -22.461 1.00 41.54  ? 355 VAL   D CB    1 
ATOM   9636  C  CG1   . VAL   C 2  353 ? 1.452   9.690   -21.594 1.00 38.34  ? 355 VAL   D CG1   1 
ATOM   9637  C  CG2   . VAL   C 2  353 ? 2.557   11.958  -21.626 1.00 53.20  ? 355 VAL   D CG2   1 
ATOM   9638  N  N     . CYS   C 2  354 ? 3.647   10.539  -25.703 1.00 51.58  ? 356 CYS   D N     1 
ATOM   9639  C  CA    . CYS   C 2  354 ? 3.835   11.285  -26.946 1.00 51.22  ? 356 CYS   D CA    1 
ATOM   9640  C  C     . CYS   C 2  354 ? 2.551   11.241  -27.763 1.00 47.60  ? 356 CYS   D C     1 
ATOM   9641  O  O     . CYS   C 2  354 ? 1.974   10.165  -27.958 1.00 44.93  ? 356 CYS   D O     1 
ATOM   9642  C  CB    . CYS   C 2  354 ? 5.005   10.723  -27.761 1.00 38.61  ? 356 CYS   D CB    1 
ATOM   9643  S  SG    . CYS   C 2  354 ? 5.159   11.394  -29.436 1.00 51.55  ? 356 CYS   D SG    1 
ATOM   9644  N  N     . ASP   C 2  355 ? 2.116   12.408  -28.241 1.00 46.49  ? 357 ASP   D N     1 
ATOM   9645  C  CA    . ASP   C 2  355 ? 0.875   12.527  -28.999 1.00 46.93  ? 357 ASP   D CA    1 
ATOM   9646  C  C     . ASP   C 2  355 ? 0.896   11.726  -30.295 1.00 55.75  ? 357 ASP   D C     1 
ATOM   9647  O  O     . ASP   C 2  355 ? 0.260   10.669  -30.379 1.00 58.76  ? 357 ASP   D O     1 
ATOM   9648  C  CB    . ASP   C 2  355 ? 0.583   13.993  -29.305 1.00 56.75  ? 357 ASP   D CB    1 
ATOM   9649  C  CG    . ASP   C 2  355 ? -0.002  14.720  -28.119 1.00 70.92  ? 357 ASP   D CG    1 
ATOM   9650  O  OD1   . ASP   C 2  355 ? -0.546  14.041  -27.221 1.00 80.09  ? 357 ASP   D OD1   1 
ATOM   9651  O  OD2   . ASP   C 2  355 ? 0.069   15.964  -28.081 1.00 72.90  ? 357 ASP   D OD2   1 
ATOM   9652  N  N     . ILE   C 2  356 ? 1.599   12.237  -31.308 1.00 55.36  ? 358 ILE   D N     1 
ATOM   9653  C  CA    . ILE   C 2  356 ? 1.767   11.613  -32.626 1.00 50.99  ? 358 ILE   D CA    1 
ATOM   9654  C  C     . ILE   C 2  356 ? 1.760   10.087  -32.544 1.00 51.13  ? 358 ILE   D C     1 
ATOM   9655  O  O     . ILE   C 2  356 ? 2.804   9.478   -32.257 1.00 54.07  ? 358 ILE   D O     1 
ATOM   9656  C  CB    . ILE   C 2  356 ? 3.071   12.090  -33.293 1.00 55.85  ? 358 ILE   D CB    1 
ATOM   9657  C  CG1   . ILE   C 2  356 ? 3.155   13.619  -33.310 1.00 55.46  ? 358 ILE   D CG1   1 
ATOM   9658  C  CG2   . ILE   C 2  356 ? 3.210   11.516  -34.703 1.00 57.20  ? 358 ILE   D CG2   1 
ATOM   9659  C  CD1   . ILE   C 2  356 ? 3.706   14.231  -32.022 1.00 50.81  ? 358 ILE   D CD1   1 
ATOM   9660  N  N     . PRO   C 2  357 ? 0.635   9.428   -32.821 1.00 51.99  ? 359 PRO   D N     1 
ATOM   9661  C  CA    . PRO   C 2  357 ? 0.593   7.965   -32.747 1.00 50.09  ? 359 PRO   D CA    1 
ATOM   9662  C  C     . PRO   C 2  357 ? 1.487   7.360   -33.807 1.00 52.52  ? 359 PRO   D C     1 
ATOM   9663  O  O     . PRO   C 2  357 ? 2.024   8.082   -34.658 1.00 58.04  ? 359 PRO   D O     1 
ATOM   9664  C  CB    . PRO   C 2  357 ? -0.885  7.628   -33.012 1.00 48.53  ? 359 PRO   D CB    1 
ATOM   9665  C  CG    . PRO   C 2  357 ? -1.626  8.939   -32.910 1.00 49.72  ? 359 PRO   D CG    1 
ATOM   9666  C  CD    . PRO   C 2  357 ? -0.640  9.993   -33.292 1.00 55.77  ? 359 PRO   D CD    1 
ATOM   9667  N  N     . PRO   C 2  358 ? 1.688   6.044   -33.782 1.00 54.31  ? 360 PRO   D N     1 
ATOM   9668  C  CA    . PRO   C 2  358 ? 2.399   5.384   -34.885 1.00 61.29  ? 360 PRO   D CA    1 
ATOM   9669  C  C     . PRO   C 2  358 ? 1.442   5.168   -36.048 1.00 67.09  ? 360 PRO   D C     1 
ATOM   9670  O  O     . PRO   C 2  358 ? 0.343   4.644   -35.861 1.00 68.68  ? 360 PRO   D O     1 
ATOM   9671  C  CB    . PRO   C 2  358 ? 2.849   4.053   -34.273 1.00 54.92  ? 360 PRO   D CB    1 
ATOM   9672  C  CG    . PRO   C 2  358 ? 1.848   3.780   -33.207 1.00 55.68  ? 360 PRO   D CG    1 
ATOM   9673  C  CD    . PRO   C 2  358 ? 1.369   5.115   -32.686 1.00 53.24  ? 360 PRO   D CD    1 
ATOM   9674  N  N     . ARG   C 2  359 ? 1.850   5.601   -37.246 1.00 75.94  ? 369 ARG   D N     1 
ATOM   9675  C  CA    . ARG   C 2  359 ? 1.027   5.468   -38.450 1.00 69.99  ? 369 ARG   D CA    1 
ATOM   9676  C  C     . ARG   C 2  359 ? 0.404   4.076   -38.532 1.00 69.21  ? 369 ARG   D C     1 
ATOM   9677  O  O     . ARG   C 2  359 ? 1.118   3.083   -38.700 1.00 68.19  ? 369 ARG   D O     1 
ATOM   9678  C  CB    . ARG   C 2  359 ? 1.877   5.754   -39.686 1.00 63.51  ? 369 ARG   D CB    1 
ATOM   9679  C  CG    . ARG   C 2  359 ? 1.230   5.478   -41.021 1.00 69.05  ? 369 ARG   D CG    1 
ATOM   9680  C  CD    . ARG   C 2  359 ? 1.583   4.096   -41.542 1.00 72.60  ? 369 ARG   D CD    1 
ATOM   9681  N  NE    . ARG   C 2  359 ? 1.981   4.124   -42.946 1.00 90.57  ? 369 ARG   D NE    1 
ATOM   9682  C  CZ    . ARG   C 2  359 ? 2.146   3.045   -43.706 1.00 102.73 ? 369 ARG   D CZ    1 
ATOM   9683  N  NH1   . ARG   C 2  359 ? 1.920   1.825   -43.239 1.00 95.72  ? 369 ARG   D NH1   1 
ATOM   9684  N  NH2   . ARG   C 2  359 ? 2.540   3.194   -44.971 1.00 94.09  ? 369 ARG   D NH2   1 
ATOM   9685  N  N     . GLY   C 2  360 ? -0.913  3.973   -38.381 1.00 55.45  ? 370 GLY   D N     1 
ATOM   9686  C  CA    . GLY   C 2  360 ? -1.503  2.647   -38.318 1.00 62.79  ? 370 GLY   D CA    1 
ATOM   9687  C  C     . GLY   C 2  360 ? -2.337  2.332   -37.086 1.00 72.79  ? 370 GLY   D C     1 
ATOM   9688  O  O     . GLY   C 2  360 ? -3.297  1.557   -37.165 1.00 68.14  ? 370 GLY   D O     1 
ATOM   9689  N  N     . LEU   C 2  361 ? -1.986  2.917   -35.941 1.00 73.36  ? 371 LEU   D N     1 
ATOM   9690  C  CA    . LEU   C 2  361 ? -2.732  2.746   -34.700 1.00 54.97  ? 371 LEU   D CA    1 
ATOM   9691  C  C     . LEU   C 2  361 ? -3.131  4.117   -34.169 1.00 59.12  ? 371 LEU   D C     1 
ATOM   9692  O  O     . LEU   C 2  361 ? -2.449  5.112   -34.427 1.00 62.63  ? 371 LEU   D O     1 
ATOM   9693  C  CB    . LEU   C 2  361 ? -1.904  1.991   -33.657 1.00 50.60  ? 371 LEU   D CB    1 
ATOM   9694  C  CG    . LEU   C 2  361 ? -1.266  0.684   -34.132 1.00 58.15  ? 371 LEU   D CG    1 
ATOM   9695  C  CD1   . LEU   C 2  361 ? -0.126  0.254   -33.221 1.00 60.94  ? 371 LEU   D CD1   1 
ATOM   9696  C  CD2   . LEU   C 2  361 ? -2.298  -0.412  -34.223 1.00 67.85  ? 371 LEU   D CD2   1 
ATOM   9697  N  N     . LYS   C 2  362 ? -4.250  4.184   -33.446 1.00 60.08  ? 372 LYS   D N     1 
ATOM   9698  C  CA    . LYS   C 2  362 ? -4.625  5.443   -32.811 1.00 66.34  ? 372 LYS   D CA    1 
ATOM   9699  C  C     . LYS   C 2  362 ? -4.131  5.527   -31.373 1.00 62.35  ? 372 LYS   D C     1 
ATOM   9700  O  O     . LYS   C 2  362 ? -4.108  6.620   -30.795 1.00 49.55  ? 372 LYS   D O     1 
ATOM   9701  C  CB    . LYS   C 2  362 ? -6.146  5.635   -32.861 1.00 60.21  ? 372 LYS   D CB    1 
ATOM   9702  C  CG    . LYS   C 2  362 ? -6.593  7.067   -32.629 1.00 59.01  ? 372 LYS   D CG    1 
ATOM   9703  C  CD    . LYS   C 2  362 ? -5.792  8.057   -33.468 1.00 61.84  ? 372 LYS   D CD    1 
ATOM   9704  C  CE    . LYS   C 2  362 ? -6.197  9.493   -33.135 1.00 74.75  ? 372 LYS   D CE    1 
ATOM   9705  N  NZ    . LYS   C 2  362 ? -5.256  10.519  -33.677 1.00 56.05  ? 372 LYS   D NZ    1 
ATOM   9706  N  N     . MET   C 2  363 ? -3.713  4.395   -30.808 1.00 59.97  ? 373 MET   D N     1 
ATOM   9707  C  CA    . MET   C 2  363 ? -3.195  4.304   -29.450 1.00 52.26  ? 373 MET   D CA    1 
ATOM   9708  C  C     . MET   C 2  363 ? -2.203  3.157   -29.409 1.00 60.40  ? 373 MET   D C     1 
ATOM   9709  O  O     . MET   C 2  363 ? -2.564  2.023   -29.739 1.00 63.00  ? 373 MET   D O     1 
ATOM   9710  C  CB    . MET   C 2  363 ? -4.321  4.064   -28.452 1.00 57.47  ? 373 MET   D CB    1 
ATOM   9711  C  CG    . MET   C 2  363 ? -5.354  5.171   -28.403 1.00 59.75  ? 373 MET   D CG    1 
ATOM   9712  S  SD    . MET   C 2  363 ? -5.572  5.736   -26.709 1.00 63.72  ? 373 MET   D SD    1 
ATOM   9713  C  CE    . MET   C 2  363 ? -5.774  4.154   -25.874 1.00 63.85  ? 373 MET   D CE    1 
ATOM   9714  N  N     . SER   C 2  364 ? -0.965  3.443   -29.009 1.00 58.35  ? 374 SER   D N     1 
ATOM   9715  C  CA    . SER   C 2  364 ? 0.093   2.442   -28.985 1.00 48.75  ? 374 SER   D CA    1 
ATOM   9716  C  C     . SER   C 2  364 ? 0.838   2.534   -27.662 1.00 48.09  ? 374 SER   D C     1 
ATOM   9717  O  O     . SER   C 2  364 ? 0.757   3.539   -26.950 1.00 43.09  ? 374 SER   D O     1 
ATOM   9718  C  CB    . SER   C 2  364 ? 1.059   2.631   -30.161 1.00 54.69  ? 374 SER   D CB    1 
ATOM   9719  O  OG    . SER   C 2  364 ? 2.218   1.827   -30.004 1.00 65.49  ? 374 SER   D OG    1 
ATOM   9720  N  N     . ALA   C 2  365 ? 1.577   1.477   -27.333 1.00 45.31  ? 375 ALA   D N     1 
ATOM   9721  C  CA    . ALA   C 2  365 ? 2.323   1.453   -26.080 1.00 39.43  ? 375 ALA   D CA    1 
ATOM   9722  C  C     . ALA   C 2  365 ? 3.582   0.627   -26.265 1.00 44.87  ? 375 ALA   D C     1 
ATOM   9723  O  O     . ALA   C 2  365 ? 3.504   -0.557  -26.603 1.00 50.25  ? 375 ALA   D O     1 
ATOM   9724  C  CB    . ALA   C 2  365 ? 1.475   0.900   -24.939 1.00 34.09  ? 375 ALA   D CB    1 
ATOM   9725  N  N     . THR   C 2  366 ? 4.737   1.240   -26.037 1.00 40.53  ? 376 THR   D N     1 
ATOM   9726  C  CA    . THR   C 2  366 ? 6.016   0.565   -26.181 1.00 39.06  ? 376 THR   D CA    1 
ATOM   9727  C  C     . THR   C 2  366 ? 6.626   0.339   -24.801 1.00 38.73  ? 376 THR   D C     1 
ATOM   9728  O  O     . THR   C 2  366 ? 6.521   1.190   -23.914 1.00 32.72  ? 376 THR   D O     1 
ATOM   9729  C  CB    . THR   C 2  366 ? 6.956   1.383   -27.074 1.00 41.65  ? 376 THR   D CB    1 
ATOM   9730  O  OG1   . THR   C 2  366 ? 6.182   2.179   -27.984 1.00 44.75  ? 376 THR   D OG1   1 
ATOM   9731  C  CG2   . THR   C 2  366 ? 7.864   0.480   -27.874 1.00 38.07  ? 376 THR   D CG2   1 
ATOM   9732  N  N     . PHE   C 2  367 ? 7.245   -0.818  -24.618 1.00 36.92  ? 377 PHE   D N     1 
ATOM   9733  C  CA    . PHE   C 2  367 ? 7.748   -1.245  -23.325 1.00 31.28  ? 377 PHE   D CA    1 
ATOM   9734  C  C     . PHE   C 2  367 ? 9.240   -1.507  -23.447 1.00 35.93  ? 377 PHE   D C     1 
ATOM   9735  O  O     . PHE   C 2  367 ? 9.684   -2.194  -24.370 1.00 40.50  ? 377 PHE   D O     1 
ATOM   9736  C  CB    . PHE   C 2  367 ? 6.994   -2.493  -22.859 1.00 32.07  ? 377 PHE   D CB    1 
ATOM   9737  C  CG    . PHE   C 2  367 ? 7.632   -3.220  -21.701 1.00 26.74  ? 377 PHE   D CG    1 
ATOM   9738  C  CD1   . PHE   C 2  367 ? 8.587   -4.187  -21.916 1.00 32.15  ? 377 PHE   D CD1   1 
ATOM   9739  C  CD2   . PHE   C 2  367 ? 7.226   -2.983  -20.406 1.00 38.77  ? 377 PHE   D CD2   1 
ATOM   9740  C  CE1   . PHE   C 2  367 ? 9.160   -4.879  -20.859 1.00 39.51  ? 377 PHE   D CE1   1 
ATOM   9741  C  CE2   . PHE   C 2  367 ? 7.789   -3.678  -19.332 1.00 45.74  ? 377 PHE   D CE2   1 
ATOM   9742  C  CZ    . PHE   C 2  367 ? 8.756   -4.628  -19.560 1.00 42.15  ? 377 PHE   D CZ    1 
ATOM   9743  N  N     . ILE   C 2  368 ? 10.014  -0.938  -22.534 1.00 30.39  ? 378 ILE   D N     1 
ATOM   9744  C  CA    . ILE   C 2  368 ? 11.446  -1.174  -22.453 1.00 25.55  ? 378 ILE   D CA    1 
ATOM   9745  C  C     . ILE   C 2  368 ? 11.705  -1.627  -21.028 1.00 34.76  ? 378 ILE   D C     1 
ATOM   9746  O  O     . ILE   C 2  368 ? 11.518  -0.846  -20.081 1.00 35.98  ? 378 ILE   D O     1 
ATOM   9747  C  CB    . ILE   C 2  368 ? 12.274  0.072   -22.792 1.00 28.71  ? 378 ILE   D CB    1 
ATOM   9748  C  CG1   . ILE   C 2  368 ? 11.844  0.672   -24.138 1.00 32.83  ? 378 ILE   D CG1   1 
ATOM   9749  C  CG2   . ILE   C 2  368 ? 13.741  -0.260  -22.809 1.00 23.13  ? 378 ILE   D CG2   1 
ATOM   9750  C  CD1   . ILE   C 2  368 ? 12.724  1.823   -24.622 1.00 34.28  ? 378 ILE   D CD1   1 
ATOM   9751  N  N     . GLY   C 2  369 ? 12.103  -2.891  -20.868 1.00 28.63  ? 379 GLY   D N     1 
ATOM   9752  C  CA    . GLY   C 2  369 ? 12.298  -3.453  -19.552 1.00 26.12  ? 379 GLY   D CA    1 
ATOM   9753  C  C     . GLY   C 2  369 ? 13.654  -4.083  -19.318 1.00 33.40  ? 379 GLY   D C     1 
ATOM   9754  O  O     . GLY   C 2  369 ? 14.110  -4.917  -20.106 1.00 41.39  ? 379 GLY   D O     1 
ATOM   9755  N  N     . ASN   C 2  370 ? 14.302  -3.700  -18.223 1.00 27.40  ? 380 ASN   D N     1 
ATOM   9756  C  CA    . ASN   C 2  370 ? 15.535  -4.335  -17.771 1.00 22.82  ? 380 ASN   D CA    1 
ATOM   9757  C  C     . ASN   C 2  370 ? 15.187  -5.386  -16.716 1.00 35.49  ? 380 ASN   D C     1 
ATOM   9758  O  O     . ASN   C 2  370 ? 15.530  -5.279  -15.539 1.00 32.12  ? 380 ASN   D O     1 
ATOM   9759  C  CB    . ASN   C 2  370 ? 16.493  -3.281  -17.237 1.00 25.55  ? 380 ASN   D CB    1 
ATOM   9760  C  CG    . ASN   C 2  370 ? 17.922  -3.760  -17.168 1.00 35.01  ? 380 ASN   D CG    1 
ATOM   9761  O  OD1   . ASN   C 2  370 ? 18.209  -4.959  -17.267 1.00 36.86  ? 380 ASN   D OD1   1 
ATOM   9762  N  ND2   . ASN   C 2  370 ? 18.837  -2.817  -16.977 1.00 28.26  ? 380 ASN   D ND2   1 
ATOM   9763  N  N     . SER   C 2  371 ? 14.461  -6.412  -17.162 1.00 40.64  ? 381 SER   D N     1 
ATOM   9764  C  CA    . SER   C 2  371 ? 14.118  -7.527  -16.288 1.00 35.60  ? 381 SER   D CA    1 
ATOM   9765  C  C     . SER   C 2  371 ? 15.311  -8.461  -16.108 1.00 34.24  ? 381 SER   D C     1 
ATOM   9766  O  O     . SER   C 2  371 ? 16.137  -8.623  -17.008 1.00 36.34  ? 381 SER   D O     1 
ATOM   9767  C  CB    . SER   C 2  371 ? 12.942  -8.312  -16.857 1.00 29.84  ? 381 SER   D CB    1 
ATOM   9768  O  OG    . SER   C 2  371 ? 12.781  -9.522  -16.150 1.00 36.55  ? 381 SER   D OG    1 
ATOM   9769  N  N     . THR   C 2  372 ? 15.408  -9.074  -14.928 1.00 37.89  ? 382 THR   D N     1 
ATOM   9770  C  CA    . THR   C 2  372 ? 16.393  -10.139 -14.761 1.00 41.50  ? 382 THR   D CA    1 
ATOM   9771  C  C     . THR   C 2  372 ? 15.947  -11.435 -15.420 1.00 42.50  ? 382 THR   D C     1 
ATOM   9772  O  O     . THR   C 2  372 ? 16.743  -12.379 -15.514 1.00 46.48  ? 382 THR   D O     1 
ATOM   9773  C  CB    . THR   C 2  372 ? 16.697  -10.411 -13.279 1.00 36.07  ? 382 THR   D CB    1 
ATOM   9774  O  OG1   . THR   C 2  372 ? 15.521  -10.897 -12.621 1.00 38.33  ? 382 THR   D OG1   1 
ATOM   9775  C  CG2   . THR   C 2  372 ? 17.211  -9.155  -12.583 1.00 34.21  ? 382 THR   D CG2   1 
ATOM   9776  N  N     . ALA   C 2  373 ? 14.694  -11.505 -15.868 1.00 35.14  ? 383 ALA   D N     1 
ATOM   9777  C  CA    . ALA   C 2  373 ? 14.257  -12.668 -16.615 1.00 36.30  ? 383 ALA   D CA    1 
ATOM   9778  C  C     . ALA   C 2  373 ? 15.002  -12.801 -17.951 1.00 49.61  ? 383 ALA   D C     1 
ATOM   9779  O  O     . ALA   C 2  373 ? 15.054  -13.907 -18.511 1.00 53.97  ? 383 ALA   D O     1 
ATOM   9780  C  CB    . ALA   C 2  373 ? 12.742  -12.600 -16.815 1.00 34.42  ? 383 ALA   D CB    1 
ATOM   9781  N  N     . ILE   C 2  374 ? 15.616  -11.721 -18.458 1.00 41.51  ? 384 ILE   D N     1 
ATOM   9782  C  CA    A ILE   C 2  374 ? 16.389  -11.783 -19.694 0.02 43.11  ? 384 ILE   D CA    1 
ATOM   9783  C  CA    B ILE   C 2  374 ? 16.382  -11.789 -19.698 0.98 42.93  ? 384 ILE   D CA    1 
ATOM   9784  C  C     . ILE   C 2  374 ? 17.415  -12.908 -19.620 1.00 45.61  ? 384 ILE   D C     1 
ATOM   9785  O  O     . ILE   C 2  374 ? 17.908  -13.372 -20.649 1.00 47.18  ? 384 ILE   D O     1 
ATOM   9786  C  CB    A ILE   C 2  374 ? 17.072  -10.436 -19.990 0.02 43.97  ? 384 ILE   D CB    1 
ATOM   9787  C  CB    B ILE   C 2  374 ? 17.051  -10.439 -20.017 0.98 44.12  ? 384 ILE   D CB    1 
ATOM   9788  C  CG1   A ILE   C 2  374 ? 17.476  -10.355 -21.465 0.02 41.17  ? 384 ILE   D CG1   1 
ATOM   9789  C  CG1   B ILE   C 2  374 ? 17.544  -10.408 -21.474 0.98 40.98  ? 384 ILE   D CG1   1 
ATOM   9790  C  CG2   A ILE   C 2  374 ? 18.295  -10.255 -19.103 0.02 42.69  ? 384 ILE   D CG2   1 
ATOM   9791  C  CG2   B ILE   C 2  374 ? 18.196  -10.145 -19.030 0.98 43.07  ? 384 ILE   D CG2   1 
ATOM   9792  C  CD1   A ILE   C 2  374 ? 16.303  -10.309 -22.422 0.02 40.89  ? 384 ILE   D CD1   1 
ATOM   9793  C  CD1   B ILE   C 2  374 ? 16.484  -10.010 -22.479 0.98 39.04  ? 384 ILE   D CD1   1 
ATOM   9794  N  N     . GLN   C 2  375 ? 17.767  -13.337 -18.403 1.00 42.29  ? 385 GLN   D N     1 
ATOM   9795  C  CA    . GLN   C 2  375 ? 18.672  -14.472 -18.253 1.00 46.48  ? 385 GLN   D CA    1 
ATOM   9796  C  C     . GLN   C 2  375 ? 18.136  -15.702 -18.972 1.00 54.62  ? 385 GLN   D C     1 
ATOM   9797  O  O     . GLN   C 2  375 ? 18.909  -16.593 -19.347 1.00 52.86  ? 385 GLN   D O     1 
ATOM   9798  C  CB    . GLN   C 2  375 ? 18.881  -14.790 -16.769 1.00 47.13  ? 385 GLN   D CB    1 
ATOM   9799  C  CG    . GLN   C 2  375 ? 17.704  -15.525 -16.110 1.00 45.08  ? 385 GLN   D CG    1 
ATOM   9800  C  CD    . GLN   C 2  375 ? 18.004  -15.975 -14.686 1.00 49.03  ? 385 GLN   D CD    1 
ATOM   9801  O  OE1   . GLN   C 2  375 ? 18.287  -17.148 -14.439 1.00 44.45  ? 385 GLN   D OE1   1 
ATOM   9802  N  NE2   . GLN   C 2  375 ? 17.953  -15.038 -13.744 1.00 45.98  ? 385 GLN   D NE2   1 
ATOM   9803  N  N     . GLU   C 2  376 ? 16.814  -15.774 -19.156 1.00 55.73  ? 386 GLU   D N     1 
ATOM   9804  C  CA    . GLU   C 2  376 ? 16.206  -16.928 -19.812 1.00 57.88  ? 386 GLU   D CA    1 
ATOM   9805  C  C     . GLU   C 2  376 ? 16.634  -17.043 -21.267 1.00 63.06  ? 386 GLU   D C     1 
ATOM   9806  O  O     . GLU   C 2  376 ? 16.650  -18.150 -21.818 1.00 58.80  ? 386 GLU   D O     1 
ATOM   9807  C  CB    . GLU   C 2  376 ? 14.680  -16.840 -19.703 1.00 48.93  ? 386 GLU   D CB    1 
ATOM   9808  C  CG    . GLU   C 2  376 ? 14.189  -16.977 -18.275 1.00 46.70  ? 386 GLU   D CG    1 
ATOM   9809  C  CD    . GLU   C 2  376 ? 12.769  -17.446 -18.173 1.00 42.06  ? 386 GLU   D CD    1 
ATOM   9810  O  OE1   . GLU   C 2  376 ? 11.904  -16.866 -18.868 1.00 34.45  ? 386 GLU   D OE1   1 
ATOM   9811  O  OE2   . GLU   C 2  376 ? 12.535  -18.399 -17.388 1.00 46.43  ? 386 GLU   D OE2   1 
ATOM   9812  N  N     . LEU   C 2  377 ? 16.968  -15.915 -21.903 1.00 64.47  ? 387 LEU   D N     1 
ATOM   9813  C  CA    . LEU   C 2  377 ? 17.368  -15.904 -23.308 1.00 55.26  ? 387 LEU   D CA    1 
ATOM   9814  C  C     . LEU   C 2  377 ? 18.853  -16.229 -23.451 1.00 50.18  ? 387 LEU   D C     1 
ATOM   9815  O  O     . LEU   C 2  377 ? 19.236  -17.035 -24.302 1.00 56.90  ? 387 LEU   D O     1 
ATOM   9816  C  CB    . LEU   C 2  377 ? 17.008  -14.546 -23.927 1.00 49.22  ? 387 LEU   D CB    1 
ATOM   9817  C  CG    . LEU   C 2  377 ? 17.595  -13.910 -25.188 1.00 44.75  ? 387 LEU   D CG    1 
ATOM   9818  C  CD1   . LEU   C 2  377 ? 16.968  -12.523 -25.361 1.00 41.14  ? 387 LEU   D CD1   1 
ATOM   9819  C  CD2   . LEU   C 2  377 ? 19.102  -13.773 -25.102 1.00 41.50  ? 387 LEU   D CD2   1 
ATOM   9820  N  N     . PHE   C 2  378 ? 19.705  -15.629 -22.621 1.00 41.36  ? 388 PHE   D N     1 
ATOM   9821  C  CA    . PHE   C 2  378 ? 21.101  -16.049 -22.609 1.00 46.80  ? 388 PHE   D CA    1 
ATOM   9822  C  C     . PHE   C 2  378 ? 21.238  -17.477 -22.128 1.00 48.84  ? 388 PHE   D C     1 
ATOM   9823  O  O     . PHE   C 2  378 ? 22.312  -18.069 -22.269 1.00 53.44  ? 388 PHE   D O     1 
ATOM   9824  C  CB    . PHE   C 2  378 ? 21.967  -15.134 -21.724 1.00 50.94  ? 388 PHE   D CB    1 
ATOM   9825  C  CG    . PHE   C 2  378 ? 21.996  -13.706 -22.176 1.00 46.93  ? 388 PHE   D CG    1 
ATOM   9826  C  CD1   . PHE   C 2  378 ? 22.648  -13.353 -23.348 1.00 39.92  ? 388 PHE   D CD1   1 
ATOM   9827  C  CD2   . PHE   C 2  378 ? 21.350  -12.722 -21.441 1.00 41.29  ? 388 PHE   D CD2   1 
ATOM   9828  C  CE1   . PHE   C 2  378 ? 22.661  -12.058 -23.780 1.00 32.54  ? 388 PHE   D CE1   1 
ATOM   9829  C  CE2   . PHE   C 2  378 ? 21.354  -11.420 -21.862 1.00 40.89  ? 388 PHE   D CE2   1 
ATOM   9830  C  CZ    . PHE   C 2  378 ? 22.016  -11.083 -23.032 1.00 46.29  ? 388 PHE   D CZ    1 
ATOM   9831  N  N     . LYS   C 2  379 ? 20.189  -18.032 -21.529 1.00 50.93  ? 389 LYS   D N     1 
ATOM   9832  C  CA    . LYS   C 2  379 ? 20.272  -19.415 -21.085 1.00 54.79  ? 389 LYS   D CA    1 
ATOM   9833  C  C     . LYS   C 2  379 ? 19.992  -20.360 -22.239 1.00 53.62  ? 389 LYS   D C     1 
ATOM   9834  O  O     . LYS   C 2  379 ? 20.657  -21.394 -22.373 1.00 59.42  ? 389 LYS   D O     1 
ATOM   9835  C  CB    . LYS   C 2  379 ? 19.301  -19.661 -19.931 1.00 52.33  ? 389 LYS   D CB    1 
ATOM   9836  C  CG    . LYS   C 2  379 ? 19.976  -19.910 -18.604 1.00 46.26  ? 389 LYS   D CG    1 
ATOM   9837  C  CD    . LYS   C 2  379 ? 18.942  -20.057 -17.526 1.00 52.81  ? 389 LYS   D CD    1 
ATOM   9838  C  CE    . LYS   C 2  379 ? 19.576  -20.091 -16.167 1.00 46.31  ? 389 LYS   D CE    1 
ATOM   9839  N  NZ    . LYS   C 2  379 ? 18.496  -20.037 -15.149 1.00 58.62  ? 389 LYS   D NZ    1 
ATOM   9840  N  N     . ARG   C 2  380 ? 19.017  -20.012 -23.081 1.00 49.06  ? 390 ARG   D N     1 
ATOM   9841  C  CA    . ARG   C 2  380 ? 18.758  -20.789 -24.286 1.00 48.09  ? 390 ARG   D CA    1 
ATOM   9842  C  C     . ARG   C 2  380 ? 20.010  -20.856 -25.150 1.00 57.49  ? 390 ARG   D C     1 
ATOM   9843  O  O     . ARG   C 2  380 ? 20.506  -21.943 -25.470 1.00 61.31  ? 390 ARG   D O     1 
ATOM   9844  C  CB    . ARG   C 2  380 ? 17.582  -20.184 -25.060 1.00 35.91  ? 390 ARG   D CB    1 
ATOM   9845  C  CG    . ARG   C 2  380 ? 17.124  -21.023 -26.218 1.00 42.62  ? 390 ARG   D CG    1 
ATOM   9846  C  CD    . ARG   C 2  380 ? 15.796  -20.561 -26.765 1.00 49.87  ? 390 ARG   D CD    1 
ATOM   9847  N  NE    . ARG   C 2  380 ? 15.892  -19.449 -27.701 1.00 49.09  ? 390 ARG   D NE    1 
ATOM   9848  C  CZ    . ARG   C 2  380 ? 15.823  -18.169 -27.362 1.00 54.60  ? 390 ARG   D CZ    1 
ATOM   9849  N  NH1   . ARG   C 2  380 ? 15.793  -17.789 -26.095 1.00 57.81  ? 390 ARG   D NH1   1 
ATOM   9850  N  NH2   . ARG   C 2  380 ? 15.767  -17.245 -28.318 1.00 52.89  ? 390 ARG   D NH2   1 
ATOM   9851  N  N     . ILE   C 2  381 ? 20.558  -19.692 -25.508 1.00 62.11  ? 391 ILE   D N     1 
ATOM   9852  C  CA    . ILE   C 2  381 ? 21.741  -19.652 -26.363 1.00 53.23  ? 391 ILE   D CA    1 
ATOM   9853  C  C     . ILE   C 2  381 ? 22.872  -20.457 -25.746 1.00 50.67  ? 391 ILE   D C     1 
ATOM   9854  O  O     . ILE   C 2  381 ? 23.562  -21.214 -26.441 1.00 54.15  ? 391 ILE   D O     1 
ATOM   9855  C  CB    . ILE   C 2  381 ? 22.162  -18.197 -26.629 1.00 41.33  ? 391 ILE   D CB    1 
ATOM   9856  C  CG1   . ILE   C 2  381 ? 21.333  -17.619 -27.774 1.00 37.17  ? 391 ILE   D CG1   1 
ATOM   9857  C  CG2   . ILE   C 2  381 ? 23.655  -18.123 -26.925 1.00 43.52  ? 391 ILE   D CG2   1 
ATOM   9858  C  CD1   . ILE   C 2  381 ? 19.845  -17.754 -27.579 1.00 43.55  ? 391 ILE   D CD1   1 
ATOM   9859  N  N     . SER   C 2  382 ? 23.079  -20.316 -24.436 1.00 46.58  ? 392 SER   D N     1 
ATOM   9860  C  CA    . SER   C 2  382 ? 24.201  -21.003 -23.808 1.00 54.20  ? 392 SER   D CA    1 
ATOM   9861  C  C     . SER   C 2  382 ? 24.037  -22.518 -23.871 1.00 61.32  ? 392 SER   D C     1 
ATOM   9862  O  O     . SER   C 2  382 ? 25.035  -23.247 -23.873 1.00 58.70  ? 392 SER   D O     1 
ATOM   9863  C  CB    . SER   C 2  382 ? 24.367  -20.541 -22.363 1.00 49.61  ? 392 SER   D CB    1 
ATOM   9864  O  OG    . SER   C 2  382 ? 25.587  -21.020 -21.828 1.00 55.49  ? 392 SER   D OG    1 
ATOM   9865  N  N     . GLU   C 2  383 ? 22.795  -23.012 -23.928 1.00 66.23  ? 393 GLU   D N     1 
ATOM   9866  C  CA    . GLU   C 2  383 ? 22.569  -24.446 -24.095 1.00 61.08  ? 393 GLU   D CA    1 
ATOM   9867  C  C     . GLU   C 2  383 ? 23.007  -24.886 -25.483 1.00 57.88  ? 393 GLU   D C     1 
ATOM   9868  O  O     . GLU   C 2  383 ? 23.979  -25.636 -25.631 1.00 62.33  ? 393 GLU   D O     1 
ATOM   9869  C  CB    . GLU   C 2  383 ? 21.094  -24.781 -23.855 1.00 65.59  ? 393 GLU   D CB    1 
ATOM   9870  C  CG    . GLU   C 2  383 ? 20.824  -26.150 -23.233 1.00 65.26  ? 393 GLU   D CG    1 
ATOM   9871  C  CD    . GLU   C 2  383 ? 19.339  -26.358 -22.918 1.00 72.21  ? 393 GLU   D CD    1 
ATOM   9872  O  OE1   . GLU   C 2  383 ? 18.484  -25.696 -23.559 1.00 58.43  ? 393 GLU   D OE1   1 
ATOM   9873  O  OE2   . GLU   C 2  383 ? 19.028  -27.178 -22.022 1.00 79.65  ? 393 GLU   D OE2   1 
ATOM   9874  N  N     . GLN   C 2  384 ? 22.313  -24.392 -26.515 1.00 54.57  ? 394 GLN   D N     1 
ATOM   9875  C  CA    . GLN   C 2  384 ? 22.738  -24.549 -27.904 1.00 58.44  ? 394 GLN   D CA    1 
ATOM   9876  C  C     . GLN   C 2  384 ? 24.265  -24.495 -28.054 1.00 58.82  ? 394 GLN   D C     1 
ATOM   9877  O  O     . GLN   C 2  384 ? 24.874  -25.411 -28.613 1.00 67.46  ? 394 GLN   D O     1 
ATOM   9878  C  CB    . GLN   C 2  384 ? 22.055  -23.478 -28.773 1.00 45.90  ? 394 GLN   D CB    1 
ATOM   9879  C  CG    . GLN   C 2  384 ? 20.525  -23.530 -28.741 1.00 46.64  ? 394 GLN   D CG    1 
ATOM   9880  C  CD    . GLN   C 2  384 ? 19.869  -22.360 -29.473 1.00 63.28  ? 394 GLN   D CD    1 
ATOM   9881  O  OE1   . GLN   C 2  384 ? 20.549  -21.463 -29.977 1.00 78.41  ? 394 GLN   D OE1   1 
ATOM   9882  N  NE2   . GLN   C 2  384 ? 18.542  -22.364 -29.530 1.00 57.55  ? 394 GLN   D NE2   1 
ATOM   9883  N  N     . PHE   C 2  385 ? 24.902  -23.442 -27.535 1.00 56.50  ? 395 PHE   D N     1 
ATOM   9884  C  CA    . PHE   C 2  385 ? 26.360  -23.334 -27.590 1.00 59.30  ? 395 PHE   D CA    1 
ATOM   9885  C  C     . PHE   C 2  385 ? 27.051  -24.563 -26.979 1.00 63.69  ? 395 PHE   D C     1 
ATOM   9886  O  O     . PHE   C 2  385 ? 27.890  -25.201 -27.627 1.00 59.07  ? 395 PHE   D O     1 
ATOM   9887  C  CB    . PHE   C 2  385 ? 26.804  -22.043 -26.888 1.00 54.00  ? 395 PHE   D CB    1 
ATOM   9888  C  CG    . PHE   C 2  385 ? 28.295  -21.798 -26.916 1.00 44.90  ? 395 PHE   D CG    1 
ATOM   9889  C  CD1   . PHE   C 2  385 ? 29.127  -22.356 -25.953 1.00 49.69  ? 395 PHE   D CD1   1 
ATOM   9890  C  CD2   . PHE   C 2  385 ? 28.855  -20.983 -27.887 1.00 48.28  ? 395 PHE   D CD2   1 
ATOM   9891  C  CE1   . PHE   C 2  385 ? 30.491  -22.121 -25.969 1.00 49.34  ? 395 PHE   D CE1   1 
ATOM   9892  C  CE2   . PHE   C 2  385 ? 30.211  -20.742 -27.903 1.00 50.02  ? 395 PHE   D CE2   1 
ATOM   9893  C  CZ    . PHE   C 2  385 ? 31.031  -21.307 -26.939 1.00 43.88  ? 395 PHE   D CZ    1 
ATOM   9894  N  N     . THR   C 2  386 ? 26.727  -24.903 -25.718 1.00 63.42  ? 396 THR   D N     1 
ATOM   9895  C  CA    . THR   C 2  386 ? 27.470  -25.971 -25.038 1.00 71.64  ? 396 THR   D CA    1 
ATOM   9896  C  C     . THR   C 2  386 ? 27.141  -27.346 -25.609 1.00 78.44  ? 396 THR   D C     1 
ATOM   9897  O  O     . THR   C 2  386 ? 27.925  -28.292 -25.436 1.00 79.58  ? 396 THR   D O     1 
ATOM   9898  C  CB    . THR   C 2  386 ? 27.206  -25.972 -23.529 1.00 64.60  ? 396 THR   D CB    1 
ATOM   9899  O  OG1   . THR   C 2  386 ? 27.664  -24.743 -22.958 1.00 69.82  ? 396 THR   D OG1   1 
ATOM   9900  C  CG2   . THR   C 2  386 ? 27.970  -27.111 -22.871 1.00 58.22  ? 396 THR   D CG2   1 
ATOM   9901  N  N     . ALA   C 2  387 ? 25.981  -27.484 -26.259 1.00 71.14  ? 397 ALA   D N     1 
ATOM   9902  C  CA    . ALA   C 2  387 ? 25.703  -28.680 -27.044 1.00 58.60  ? 397 ALA   D CA    1 
ATOM   9903  C  C     . ALA   C 2  387 ? 26.794  -28.897 -28.079 1.00 73.87  ? 397 ALA   D C     1 
ATOM   9904  O  O     . ALA   C 2  387 ? 27.477  -29.926 -28.076 1.00 85.76  ? 397 ALA   D O     1 
ATOM   9905  C  CB    . ALA   C 2  387 ? 24.339  -28.560 -27.721 1.00 52.61  ? 397 ALA   D CB    1 
ATOM   9906  N  N     . MET   C 2  388 ? 26.988  -27.907 -28.958 1.00 72.45  ? 398 MET   D N     1 
ATOM   9907  C  CA    . MET   C 2  388 ? 28.030  -27.978 -29.978 1.00 70.91  ? 398 MET   D CA    1 
ATOM   9908  C  C     . MET   C 2  388 ? 29.429  -27.916 -29.362 1.00 72.99  ? 398 MET   D C     1 
ATOM   9909  O  O     . MET   C 2  388 ? 30.268  -28.785 -29.619 1.00 74.91  ? 398 MET   D O     1 
ATOM   9910  C  CB    . MET   C 2  388 ? 27.831  -26.852 -31.000 1.00 61.72  ? 398 MET   D CB    1 
ATOM   9911  C  CG    . MET   C 2  388 ? 26.398  -26.732 -31.511 1.00 58.96  ? 398 MET   D CG    1 
ATOM   9912  S  SD    . MET   C 2  388 ? 26.246  -25.822 -33.068 1.00 82.44  ? 398 MET   D SD    1 
ATOM   9913  C  CE    . MET   C 2  388 ? 24.454  -25.742 -33.248 1.00 49.80  ? 398 MET   D CE    1 
ATOM   9914  N  N     . PHE   C 2  389 ? 29.707  -26.897 -28.546 1.00 72.30  ? 399 PHE   D N     1 
ATOM   9915  C  CA    . PHE   C 2  389 ? 31.088  -26.687 -28.118 1.00 73.87  ? 399 PHE   D CA    1 
ATOM   9916  C  C     . PHE   C 2  389 ? 31.656  -27.868 -27.340 1.00 76.75  ? 399 PHE   D C     1 
ATOM   9917  O  O     . PHE   C 2  389 ? 32.882  -28.007 -27.249 1.00 77.88  ? 399 PHE   D O     1 
ATOM   9918  C  CB    . PHE   C 2  389 ? 31.224  -25.427 -27.263 1.00 64.44  ? 399 PHE   D CB    1 
ATOM   9919  C  CG    . PHE   C 2  389 ? 32.616  -25.217 -26.751 1.00 58.89  ? 399 PHE   D CG    1 
ATOM   9920  C  CD1   . PHE   C 2  389 ? 33.595  -24.688 -27.580 1.00 55.11  ? 399 PHE   D CD1   1 
ATOM   9921  C  CD2   . PHE   C 2  389 ? 32.960  -25.598 -25.462 1.00 67.91  ? 399 PHE   D CD2   1 
ATOM   9922  C  CE1   . PHE   C 2  389 ? 34.880  -24.508 -27.120 1.00 62.23  ? 399 PHE   D CE1   1 
ATOM   9923  C  CE2   . PHE   C 2  389 ? 34.247  -25.427 -24.990 1.00 70.00  ? 399 PHE   D CE2   1 
ATOM   9924  C  CZ    . PHE   C 2  389 ? 35.209  -24.878 -25.819 1.00 71.11  ? 399 PHE   D CZ    1 
ATOM   9925  N  N     . ARG   C 2  390 ? 30.805  -28.706 -26.752 1.00 78.42  ? 400 ARG   D N     1 
ATOM   9926  C  CA    . ARG   C 2  390 ? 31.332  -29.865 -26.042 1.00 85.82  ? 400 ARG   D CA    1 
ATOM   9927  C  C     . ARG   C 2  390 ? 32.156  -30.756 -26.965 1.00 89.29  ? 400 ARG   D C     1 
ATOM   9928  O  O     . ARG   C 2  390 ? 33.145  -31.359 -26.526 1.00 83.07  ? 400 ARG   D O     1 
ATOM   9929  C  CB    . ARG   C 2  390 ? 30.191  -30.649 -25.387 1.00 83.64  ? 400 ARG   D CB    1 
ATOM   9930  C  CG    . ARG   C 2  390 ? 29.982  -30.309 -23.919 1.00 79.83  ? 400 ARG   D CG    1 
ATOM   9931  C  CD    . ARG   C 2  390 ? 31.215  -30.678 -23.083 1.00 90.03  ? 400 ARG   D CD    1 
ATOM   9932  N  NE    . ARG   C 2  390 ? 32.342  -29.769 -23.283 1.00 100.11 ? 400 ARG   D NE    1 
ATOM   9933  C  CZ    . ARG   C 2  390 ? 33.616  -30.136 -23.377 1.00 96.56  ? 400 ARG   D CZ    1 
ATOM   9934  N  NH1   . ARG   C 2  390 ? 33.980  -31.407 -23.300 1.00 90.64  ? 400 ARG   D NH1   1 
ATOM   9935  N  NH2   . ARG   C 2  390 ? 34.547  -29.204 -23.579 1.00 92.75  ? 400 ARG   D NH2   1 
ATOM   9936  N  N     . ARG   C 2  391 ? 31.796  -30.796 -28.254 1.00 93.48  ? 401 ARG   D N     1 
ATOM   9937  C  CA    . ARG   C 2  391 ? 32.372  -31.683 -29.259 1.00 79.46  ? 401 ARG   D CA    1 
ATOM   9938  C  C     . ARG   C 2  391 ? 32.917  -30.894 -30.452 1.00 76.20  ? 401 ARG   D C     1 
ATOM   9939  O  O     . ARG   C 2  391 ? 32.933  -31.390 -31.581 1.00 75.28  ? 401 ARG   D O     1 
ATOM   9940  C  CB    . ARG   C 2  391 ? 31.328  -32.699 -29.725 1.00 71.07  ? 401 ARG   D CB    1 
ATOM   9941  C  CG    . ARG   C 2  391 ? 30.000  -32.040 -30.125 1.00 76.66  ? 401 ARG   D CG    1 
ATOM   9942  C  CD    . ARG   C 2  391 ? 28.913  -33.028 -30.563 1.00 78.11  ? 401 ARG   D CD    1 
ATOM   9943  N  NE    . ARG   C 2  391 ? 27.613  -32.375 -30.696 1.00 75.14  ? 401 ARG   D NE    1 
ATOM   9944  C  CZ    . ARG   C 2  391 ? 27.218  -31.685 -31.758 1.00 75.73  ? 401 ARG   D CZ    1 
ATOM   9945  N  NH1   . ARG   C 2  391 ? 27.990  -31.554 -32.822 1.00 76.02  ? 401 ARG   D NH1   1 
ATOM   9946  N  NH2   . ARG   C 2  391 ? 26.018  -31.105 -31.749 1.00 71.69  ? 401 ARG   D NH2   1 
ATOM   9947  N  N     . LYS   C 2  392 ? 33.337  -29.650 -30.213 1.00 74.25  ? 402 LYS   D N     1 
ATOM   9948  C  CA    . LYS   C 2  392 ? 33.999  -28.797 -31.198 1.00 70.60  ? 402 LYS   D CA    1 
ATOM   9949  C  C     . LYS   C 2  392 ? 33.416  -28.919 -32.607 1.00 68.13  ? 402 LYS   D C     1 
ATOM   9950  O  O     . LYS   C 2  392 ? 34.149  -28.802 -33.598 1.00 66.04  ? 402 LYS   D O     1 
ATOM   9951  C  CB    . LYS   C 2  392 ? 35.496  -29.108 -31.208 1.00 68.00  ? 402 LYS   D CB    1 
ATOM   9952  C  CG    . LYS   C 2  392 ? 35.962  -29.839 -29.957 1.00 82.65  ? 402 LYS   D CG    1 
ATOM   9953  C  CD    . LYS   C 2  392 ? 37.453  -30.157 -29.996 1.00 88.55  ? 402 LYS   D CD    1 
ATOM   9954  C  CE    . LYS   C 2  392 ? 37.842  -31.121 -28.880 1.00 93.83  ? 402 LYS   D CE    1 
ATOM   9955  N  NZ    . LYS   C 2  392 ? 37.551  -30.583 -27.517 1.00 95.29  ? 402 LYS   D NZ    1 
ATOM   9956  N  N     . ALA   C 2  393 ? 32.097  -29.116 -32.696 1.00 65.69  ? 403 ALA   D N     1 
ATOM   9957  C  CA    . ALA   C 2  393 ? 31.352  -29.232 -33.948 1.00 68.02  ? 403 ALA   D CA    1 
ATOM   9958  C  C     . ALA   C 2  393 ? 32.045  -28.605 -35.156 1.00 79.77  ? 403 ALA   D C     1 
ATOM   9959  O  O     . ALA   C 2  393 ? 32.497  -29.318 -36.056 1.00 100.76 ? 403 ALA   D O     1 
ATOM   9960  C  CB    . ALA   C 2  393 ? 29.963  -28.614 -33.791 1.00 73.89  ? 403 ALA   D CB    1 
ATOM   9961  N  N     . PHE   C 2  394 ? 32.108  -27.281 -35.219 1.00 74.02  ? 404 PHE   D N     1 
ATOM   9962  C  CA    . PHE   C 2  394 ? 32.687  -26.611 -36.375 1.00 65.81  ? 404 PHE   D CA    1 
ATOM   9963  C  C     . PHE   C 2  394 ? 33.802  -25.680 -35.928 1.00 65.79  ? 404 PHE   D C     1 
ATOM   9964  O  O     . PHE   C 2  394 ? 34.102  -24.691 -36.603 1.00 70.02  ? 404 PHE   D O     1 
ATOM   9965  C  CB    . PHE   C 2  394 ? 31.619  -25.857 -37.169 1.00 70.10  ? 404 PHE   D CB    1 
ATOM   9966  C  CG    . PHE   C 2  394 ? 30.469  -26.726 -37.628 1.00 75.02  ? 404 PHE   D CG    1 
ATOM   9967  C  CD1   . PHE   C 2  394 ? 30.178  -26.848 -38.981 1.00 83.34  ? 404 PHE   D CD1   1 
ATOM   9968  C  CD2   . PHE   C 2  394 ? 29.663  -27.400 -36.715 1.00 78.48  ? 404 PHE   D CD2   1 
ATOM   9969  C  CE1   . PHE   C 2  394 ? 29.117  -27.650 -39.418 1.00 75.85  ? 404 PHE   D CE1   1 
ATOM   9970  C  CE2   . PHE   C 2  394 ? 28.621  -28.205 -37.134 1.00 74.91  ? 404 PHE   D CE2   1 
ATOM   9971  C  CZ    . PHE   C 2  394 ? 28.336  -28.324 -38.486 1.00 77.11  ? 404 PHE   D CZ    1 
ATOM   9972  N  N     . LEU   C 2  395 ? 34.440  -26.008 -34.797 1.00 62.00  ? 405 LEU   D N     1 
ATOM   9973  C  CA    . LEU   C 2  395 ? 35.489  -25.159 -34.245 1.00 64.45  ? 405 LEU   D CA    1 
ATOM   9974  C  C     . LEU   C 2  395 ? 36.642  -24.944 -35.222 1.00 68.36  ? 405 LEU   D C     1 
ATOM   9975  O  O     . LEU   C 2  395 ? 37.360  -23.941 -35.110 1.00 72.11  ? 405 LEU   D O     1 
ATOM   9976  C  CB    . LEU   C 2  395 ? 35.991  -25.744 -32.924 1.00 57.75  ? 405 LEU   D CB    1 
ATOM   9977  C  CG    . LEU   C 2  395 ? 35.354  -25.072 -31.696 1.00 59.54  ? 405 LEU   D CG    1 
ATOM   9978  C  CD1   . LEU   C 2  395 ? 33.894  -25.472 -31.507 1.00 63.54  ? 405 LEU   D CD1   1 
ATOM   9979  C  CD2   . LEU   C 2  395 ? 36.158  -25.330 -30.436 1.00 66.71  ? 405 LEU   D CD2   1 
ATOM   9980  N  N     . HIS   C 2  396 ? 36.824  -25.843 -36.192 1.00 70.12  ? 406 HIS   D N     1 
ATOM   9981  C  CA    . HIS   C 2  396 ? 37.835  -25.625 -37.222 1.00 68.19  ? 406 HIS   D CA    1 
ATOM   9982  C  C     . HIS   C 2  396 ? 37.504  -24.413 -38.082 1.00 65.67  ? 406 HIS   D C     1 
ATOM   9983  O  O     . HIS   C 2  396 ? 38.417  -23.727 -38.550 1.00 66.33  ? 406 HIS   D O     1 
ATOM   9984  C  CB    . HIS   C 2  396 ? 37.984  -26.874 -38.098 1.00 83.89  ? 406 HIS   D CB    1 
ATOM   9985  C  CG    . HIS   C 2  396 ? 36.795  -27.158 -38.975 1.00 82.07  ? 406 HIS   D CG    1 
ATOM   9986  N  ND1   . HIS   C 2  396 ? 35.591  -27.611 -38.478 1.00 86.82  ? 406 HIS   D ND1   1 
ATOM   9987  C  CD2   . HIS   C 2  396 ? 36.635  -27.079 -40.319 1.00 80.29  ? 406 HIS   D CD2   1 
ATOM   9988  C  CE1   . HIS   C 2  396 ? 34.736  -27.779 -39.472 1.00 84.35  ? 406 HIS   D CE1   1 
ATOM   9989  N  NE2   . HIS   C 2  396 ? 35.344  -27.461 -40.601 1.00 76.12  ? 406 HIS   D NE2   1 
ATOM   9990  N  N     . TRP   C 2  397 ? 36.212  -24.142 -38.316 1.00 61.03  ? 407 TRP   D N     1 
ATOM   9991  C  CA    . TRP   C 2  397 ? 35.816  -22.949 -39.068 1.00 64.86  ? 407 TRP   D CA    1 
ATOM   9992  C  C     . TRP   C 2  397 ? 36.413  -21.690 -38.461 1.00 67.94  ? 407 TRP   D C     1 
ATOM   9993  O  O     . TRP   C 2  397 ? 36.798  -20.757 -39.182 1.00 68.56  ? 407 TRP   D O     1 
ATOM   9994  C  CB    . TRP   C 2  397 ? 34.295  -22.801 -39.096 1.00 65.81  ? 407 TRP   D CB    1 
ATOM   9995  C  CG    . TRP   C 2  397 ? 33.576  -23.577 -40.144 1.00 81.54  ? 407 TRP   D CG    1 
ATOM   9996  C  CD1   . TRP   C 2  397 ? 34.070  -24.601 -40.906 1.00 85.75  ? 407 TRP   D CD1   1 
ATOM   9997  C  CD2   . TRP   C 2  397 ? 32.212  -23.396 -40.546 1.00 81.39  ? 407 TRP   D CD2   1 
ATOM   9998  N  NE1   . TRP   C 2  397 ? 33.090  -25.070 -41.754 1.00 86.22  ? 407 TRP   D NE1   1 
ATOM   9999  C  CE2   . TRP   C 2  397 ? 31.943  -24.344 -41.553 1.00 78.06  ? 407 TRP   D CE2   1 
ATOM   10000 C  CE3   . TRP   C 2  397 ? 31.191  -22.524 -40.151 1.00 77.21  ? 407 TRP   D CE3   1 
ATOM   10001 C  CZ2   . TRP   C 2  397 ? 30.697  -24.443 -42.167 1.00 62.32  ? 407 TRP   D CZ2   1 
ATOM   10002 C  CZ3   . TRP   C 2  397 ? 29.950  -22.623 -40.774 1.00 74.99  ? 407 TRP   D CZ3   1 
ATOM   10003 C  CH2   . TRP   C 2  397 ? 29.716  -23.575 -41.766 1.00 57.85  ? 407 TRP   D CH2   1 
ATOM   10004 N  N     . TYR   C 2  398 ? 36.455  -21.637 -37.126 1.00 65.96  ? 408 TYR   D N     1 
ATOM   10005 C  CA    . TYR   C 2  398 ? 36.952  -20.491 -36.379 1.00 57.75  ? 408 TYR   D CA    1 
ATOM   10006 C  C     . TYR   C 2  398 ? 38.440  -20.608 -36.090 1.00 54.17  ? 408 TYR   D C     1 
ATOM   10007 O  O     . TYR   C 2  398 ? 39.141  -19.589 -36.100 1.00 56.43  ? 408 TYR   D O     1 
ATOM   10008 C  CB    . TYR   C 2  398 ? 36.149  -20.319 -35.071 1.00 66.06  ? 408 TYR   D CB    1 
ATOM   10009 C  CG    . TYR   C 2  398 ? 34.652  -20.134 -35.303 1.00 58.30  ? 408 TYR   D CG    1 
ATOM   10010 C  CD1   . TYR   C 2  398 ? 34.146  -18.924 -35.756 1.00 61.63  ? 408 TYR   D CD1   1 
ATOM   10011 C  CD2   . TYR   C 2  398 ? 33.753  -21.173 -35.093 1.00 56.99  ? 408 TYR   D CD2   1 
ATOM   10012 C  CE1   . TYR   C 2  398 ? 32.792  -18.754 -35.995 1.00 67.12  ? 408 TYR   D CE1   1 
ATOM   10013 C  CE2   . TYR   C 2  398 ? 32.393  -21.006 -35.333 1.00 58.30  ? 408 TYR   D CE2   1 
ATOM   10014 C  CZ    . TYR   C 2  398 ? 31.923  -19.795 -35.784 1.00 58.17  ? 408 TYR   D CZ    1 
ATOM   10015 O  OH    . TYR   C 2  398 ? 30.582  -19.601 -36.028 1.00 53.02  ? 408 TYR   D OH    1 
ATOM   10016 N  N     . THR   C 2  399 ? 38.952  -21.824 -35.854 1.00 56.54  ? 409 THR   D N     1 
ATOM   10017 C  CA    . THR   C 2  399 ? 40.398  -21.983 -35.684 1.00 57.85  ? 409 THR   D CA    1 
ATOM   10018 C  C     . THR   C 2  399 ? 41.133  -21.660 -36.978 1.00 56.85  ? 409 THR   D C     1 
ATOM   10019 O  O     . THR   C 2  399 ? 42.160  -20.975 -36.963 1.00 51.52  ? 409 THR   D O     1 
ATOM   10020 C  CB    . THR   C 2  399 ? 40.752  -23.400 -35.230 1.00 57.26  ? 409 THR   D CB    1 
ATOM   10021 O  OG1   . THR   C 2  399 ? 39.705  -23.916 -34.404 1.00 65.58  ? 409 THR   D OG1   1 
ATOM   10022 C  CG2   . THR   C 2  399 ? 42.064  -23.393 -34.445 1.00 43.00  ? 409 THR   D CG2   1 
ATOM   10023 N  N     . GLY   C 2  400 ? 40.603  -22.131 -38.110 1.00 59.55  ? 410 GLY   D N     1 
ATOM   10024 C  CA    . GLY   C 2  400 ? 41.236  -21.872 -39.394 1.00 53.19  ? 410 GLY   D CA    1 
ATOM   10025 C  C     . GLY   C 2  400 ? 41.346  -20.396 -39.729 1.00 54.71  ? 410 GLY   D C     1 
ATOM   10026 O  O     . GLY   C 2  400 ? 42.382  -19.934 -40.215 1.00 56.17  ? 410 GLY   D O     1 
ATOM   10027 N  N     . GLU   C 2  401 ? 40.275  -19.640 -39.502 1.00 59.00  ? 411 GLU   D N     1 
ATOM   10028 C  CA    . GLU   C 2  401 ? 40.362  -18.194 -39.648 1.00 52.94  ? 411 GLU   D CA    1 
ATOM   10029 C  C     . GLU   C 2  401 ? 41.218  -17.536 -38.568 1.00 51.86  ? 411 GLU   D C     1 
ATOM   10030 O  O     . GLU   C 2  401 ? 41.445  -16.326 -38.648 1.00 49.97  ? 411 GLU   D O     1 
ATOM   10031 C  CB    . GLU   C 2  401 ? 38.960  -17.607 -39.667 1.00 55.33  ? 411 GLU   D CB    1 
ATOM   10032 C  CG    . GLU   C 2  401 ? 38.140  -18.109 -40.853 1.00 60.08  ? 411 GLU   D CG    1 
ATOM   10033 C  CD    . GLU   C 2  401 ? 38.558  -17.462 -42.162 1.00 66.43  ? 411 GLU   D CD    1 
ATOM   10034 O  OE1   . GLU   C 2  401 ? 39.082  -16.328 -42.131 1.00 68.36  ? 411 GLU   D OE1   1 
ATOM   10035 O  OE2   . GLU   C 2  401 ? 38.364  -18.083 -43.228 1.00 78.82  ? 411 GLU   D OE2   1 
ATOM   10036 N  N     . GLY   C 2  402 ? 41.708  -18.294 -37.580 1.00 48.64  ? 412 GLY   D N     1 
ATOM   10037 C  CA    . GLY   C 2  402 ? 42.760  -17.807 -36.706 1.00 51.43  ? 412 GLY   D CA    1 
ATOM   10038 C  C     . GLY   C 2  402 ? 42.747  -18.189 -35.231 1.00 63.37  ? 412 GLY   D C     1 
ATOM   10039 O  O     . GLY   C 2  402 ? 43.803  -18.170 -34.590 1.00 61.46  ? 412 GLY   D O     1 
ATOM   10040 N  N     . MET   C 2  403 ? 41.592  -18.550 -34.669 1.00 60.26  ? 413 MET   D N     1 
ATOM   10041 C  CA    . MET   C 2  403 ? 41.436  -18.469 -33.219 1.00 62.15  ? 413 MET   D CA    1 
ATOM   10042 C  C     . MET   C 2  403 ? 41.931  -19.722 -32.499 1.00 59.11  ? 413 MET   D C     1 
ATOM   10043 O  O     . MET   C 2  403 ? 42.488  -20.651 -33.095 1.00 59.29  ? 413 MET   D O     1 
ATOM   10044 C  CB    . MET   C 2  403 ? 39.979  -18.221 -32.837 1.00 59.58  ? 413 MET   D CB    1 
ATOM   10045 C  CG    . MET   C 2  403 ? 39.269  -17.126 -33.605 1.00 54.92  ? 413 MET   D CG    1 
ATOM   10046 S  SD    . MET   C 2  403 ? 37.556  -17.170 -33.081 1.00 53.89  ? 413 MET   D SD    1 
ATOM   10047 C  CE    . MET   C 2  403 ? 36.744  -16.489 -34.520 1.00 42.41  ? 413 MET   D CE    1 
ATOM   10048 N  N     . ASP   C 2  404 ? 41.717  -19.724 -31.179 1.00 57.60  ? 414 ASP   D N     1 
ATOM   10049 C  CA    . ASP   C 2  404 ? 42.053  -20.810 -30.269 1.00 60.36  ? 414 ASP   D CA    1 
ATOM   10050 C  C     . ASP   C 2  404 ? 40.801  -21.236 -29.528 1.00 56.45  ? 414 ASP   D C     1 
ATOM   10051 O  O     . ASP   C 2  404 ? 39.769  -20.566 -29.565 1.00 57.61  ? 414 ASP   D O     1 
ATOM   10052 C  CB    . ASP   C 2  404 ? 43.142  -20.413 -29.263 1.00 54.13  ? 414 ASP   D CB    1 
ATOM   10053 C  CG    . ASP   C 2  404 ? 42.906  -19.037 -28.646 1.00 75.90  ? 414 ASP   D CG    1 
ATOM   10054 O  OD1   . ASP   C 2  404 ? 42.659  -18.065 -29.399 1.00 80.23  ? 414 ASP   D OD1   1 
ATOM   10055 O  OD2   . ASP   C 2  404 ? 42.954  -18.927 -27.399 1.00 82.31  ? 414 ASP   D OD2   1 
ATOM   10056 N  N     . GLU   C 2  405 ? 40.888  -22.375 -28.856 1.00 61.23  ? 415 GLU   D N     1 
ATOM   10057 C  CA    . GLU   C 2  405 ? 39.691  -22.869 -28.193 1.00 68.10  ? 415 GLU   D CA    1 
ATOM   10058 C  C     . GLU   C 2  405 ? 39.277  -21.960 -27.039 1.00 70.40  ? 415 GLU   D C     1 
ATOM   10059 O  O     . GLU   C 2  405 ? 38.077  -21.815 -26.772 1.00 67.24  ? 415 GLU   D O     1 
ATOM   10060 C  CB    . GLU   C 2  405 ? 39.903  -24.312 -27.727 1.00 62.98  ? 415 GLU   D CB    1 
ATOM   10061 C  CG    . GLU   C 2  405 ? 39.293  -25.350 -28.674 1.00 76.67  ? 415 GLU   D CG    1 
ATOM   10062 C  CD    . GLU   C 2  405 ? 39.820  -26.760 -28.430 1.00 95.52  ? 415 GLU   D CD    1 
ATOM   10063 O  OE1   . GLU   C 2  405 ? 39.696  -27.623 -29.337 1.00 92.61  ? 415 GLU   D OE1   1 
ATOM   10064 O  OE2   . GLU   C 2  405 ? 40.368  -26.995 -27.330 1.00 94.69  ? 415 GLU   D OE2   1 
ATOM   10065 N  N     . MET   C 2  406 ? 40.239  -21.302 -26.381 1.00 63.96  ? 416 MET   D N     1 
ATOM   10066 C  CA    . MET   C 2  406 ? 39.921  -20.530 -25.179 1.00 60.75  ? 416 MET   D CA    1 
ATOM   10067 C  C     . MET   C 2  406 ? 38.975  -19.376 -25.474 1.00 64.62  ? 416 MET   D C     1 
ATOM   10068 O  O     . MET   C 2  406 ? 38.111  -19.037 -24.651 1.00 56.98  ? 416 MET   D O     1 
ATOM   10069 C  CB    . MET   C 2  406 ? 41.195  -20.004 -24.536 1.00 56.06  ? 416 MET   D CB    1 
ATOM   10070 C  CG    . MET   C 2  406 ? 41.375  -20.487 -23.128 1.00 66.23  ? 416 MET   D CG    1 
ATOM   10071 S  SD    . MET   C 2  406 ? 42.731  -19.647 -22.311 1.00 95.07  ? 416 MET   D SD    1 
ATOM   10072 C  CE    . MET   C 2  406 ? 42.063  -17.992 -22.157 1.00 78.39  ? 416 MET   D CE    1 
ATOM   10073 N  N     . GLU   C 2  407 ? 39.122  -18.758 -26.639 1.00 66.60  ? 417 GLU   D N     1 
ATOM   10074 C  CA    . GLU   C 2  407 ? 38.262  -17.641 -26.991 1.00 68.00  ? 417 GLU   D CA    1 
ATOM   10075 C  C     . GLU   C 2  407 ? 36.819  -18.114 -27.053 1.00 59.91  ? 417 GLU   D C     1 
ATOM   10076 O  O     . GLU   C 2  407 ? 35.885  -17.313 -27.150 1.00 60.25  ? 417 GLU   D O     1 
ATOM   10077 C  CB    . GLU   C 2  407 ? 38.704  -17.028 -28.315 1.00 60.30  ? 417 GLU   D CB    1 
ATOM   10078 C  CG    . GLU   C 2  407 ? 37.886  -15.853 -28.731 1.00 53.27  ? 417 GLU   D CG    1 
ATOM   10079 C  CD    . GLU   C 2  407 ? 38.656  -14.943 -29.634 1.00 62.77  ? 417 GLU   D CD    1 
ATOM   10080 O  OE1   . GLU   C 2  407 ? 39.888  -15.133 -29.744 1.00 68.08  ? 417 GLU   D OE1   1 
ATOM   10081 O  OE2   . GLU   C 2  407 ? 38.023  -14.045 -30.233 1.00 62.97  ? 417 GLU   D OE2   1 
ATOM   10082 N  N     . PHE   C 2  408 ? 36.626  -19.424 -27.033 1.00 57.01  ? 418 PHE   D N     1 
ATOM   10083 C  CA    . PHE   C 2  408 ? 35.273  -19.918 -26.863 1.00 60.58  ? 418 PHE   D CA    1 
ATOM   10084 C  C     . PHE   C 2  408 ? 34.957  -20.116 -25.384 1.00 60.38  ? 418 PHE   D C     1 
ATOM   10085 O  O     . PHE   C 2  408 ? 33.902  -19.679 -24.914 1.00 60.90  ? 418 PHE   D O     1 
ATOM   10086 C  CB    . PHE   C 2  408 ? 35.075  -21.203 -27.680 1.00 56.34  ? 418 PHE   D CB    1 
ATOM   10087 C  CG    . PHE   C 2  408 ? 34.782  -20.950 -29.140 1.00 52.73  ? 418 PHE   D CG    1 
ATOM   10088 C  CD1   . PHE   C 2  408 ? 35.730  -20.358 -29.963 1.00 58.56  ? 418 PHE   D CD1   1 
ATOM   10089 C  CD2   . PHE   C 2  408 ? 33.566  -21.295 -29.683 1.00 47.66  ? 418 PHE   D CD2   1 
ATOM   10090 C  CE1   . PHE   C 2  408 ? 35.462  -20.118 -31.300 1.00 50.62  ? 418 PHE   D CE1   1 
ATOM   10091 C  CE2   . PHE   C 2  408 ? 33.293  -21.053 -31.018 1.00 52.33  ? 418 PHE   D CE2   1 
ATOM   10092 C  CZ    . PHE   C 2  408 ? 34.240  -20.466 -31.827 1.00 51.15  ? 418 PHE   D CZ    1 
ATOM   10093 N  N     . THR   C 2  409 ? 35.870  -20.728 -24.625 1.00 55.91  ? 419 THR   D N     1 
ATOM   10094 C  CA    . THR   C 2  409 ? 35.674  -20.807 -23.183 1.00 58.57  ? 419 THR   D CA    1 
ATOM   10095 C  C     . THR   C 2  409 ? 35.441  -19.414 -22.595 1.00 62.90  ? 419 THR   D C     1 
ATOM   10096 O  O     . THR   C 2  409 ? 34.467  -19.194 -21.864 1.00 56.11  ? 419 THR   D O     1 
ATOM   10097 C  CB    . THR   C 2  409 ? 36.872  -21.492 -22.512 1.00 50.76  ? 419 THR   D CB    1 
ATOM   10098 O  OG1   . THR   C 2  409 ? 38.080  -21.072 -23.147 1.00 67.53  ? 419 THR   D OG1   1 
ATOM   10099 C  CG2   . THR   C 2  409 ? 36.764  -23.019 -22.563 1.00 40.82  ? 419 THR   D CG2   1 
ATOM   10100 N  N     . GLU   C 2  410 ? 36.317  -18.453 -22.929 1.00 59.86  ? 420 GLU   D N     1 
ATOM   10101 C  CA    . GLU   C 2  410 ? 36.172  -17.087 -22.423 1.00 52.69  ? 420 GLU   D CA    1 
ATOM   10102 C  C     . GLU   C 2  410 ? 34.779  -16.530 -22.703 1.00 55.66  ? 420 GLU   D C     1 
ATOM   10103 O  O     . GLU   C 2  410 ? 34.130  -15.976 -21.811 1.00 59.27  ? 420 GLU   D O     1 
ATOM   10104 C  CB    . GLU   C 2  410 ? 37.232  -16.169 -23.035 1.00 59.63  ? 420 GLU   D CB    1 
ATOM   10105 C  CG    . GLU   C 2  410 ? 38.686  -16.482 -22.672 1.00 69.45  ? 420 GLU   D CG    1 
ATOM   10106 C  CD    . GLU   C 2  410 ? 39.642  -15.380 -23.132 1.00 82.43  ? 420 GLU   D CD    1 
ATOM   10107 O  OE1   . GLU   C 2  410 ? 39.174  -14.228 -23.301 1.00 86.96  ? 420 GLU   D OE1   1 
ATOM   10108 O  OE2   . GLU   C 2  410 ? 40.848  -15.661 -23.331 1.00 76.56  ? 420 GLU   D OE2   1 
ATOM   10109 N  N     . ALA   C 2  411 ? 34.302  -16.657 -23.944 1.00 52.84  ? 421 ALA   D N     1 
ATOM   10110 C  CA    . ALA   C 2  411 ? 32.945  -16.216 -24.256 1.00 53.86  ? 421 ALA   D CA    1 
ATOM   10111 C  C     . ALA   C 2  411 ? 31.924  -16.979 -23.427 1.00 52.35  ? 421 ALA   D C     1 
ATOM   10112 O  O     . ALA   C 2  411 ? 30.974  -16.398 -22.897 1.00 45.55  ? 421 ALA   D O     1 
ATOM   10113 C  CB    . ALA   C 2  411 ? 32.651  -16.382 -25.750 1.00 41.47  ? 421 ALA   D CB    1 
ATOM   10114 N  N     . GLU   C 2  412 ? 32.104  -18.290 -23.308 1.00 56.83  ? 422 GLU   D N     1 
ATOM   10115 C  CA    . GLU   C 2  412 ? 31.171  -19.093 -22.533 1.00 59.25  ? 422 GLU   D CA    1 
ATOM   10116 C  C     . GLU   C 2  412 ? 31.142  -18.639 -21.074 1.00 63.61  ? 422 GLU   D C     1 
ATOM   10117 O  O     . GLU   C 2  412 ? 30.074  -18.351 -20.519 1.00 57.65  ? 422 GLU   D O     1 
ATOM   10118 C  CB    . GLU   C 2  412 ? 31.554  -20.569 -22.647 1.00 56.64  ? 422 GLU   D CB    1 
ATOM   10119 C  CG    . GLU   C 2  412 ? 30.414  -21.531 -22.400 1.00 52.55  ? 422 GLU   D CG    1 
ATOM   10120 C  CD    . GLU   C 2  412 ? 30.817  -22.964 -22.641 1.00 63.59  ? 422 GLU   D CD    1 
ATOM   10121 O  OE1   . GLU   C 2  412 ? 31.815  -23.413 -22.032 1.00 67.82  ? 422 GLU   D OE1   1 
ATOM   10122 O  OE2   . GLU   C 2  412 ? 30.146  -23.634 -23.458 1.00 70.52  ? 422 GLU   D OE2   1 
ATOM   10123 N  N     . SER   C 2  413 ? 32.307  -18.563 -20.431 1.00 57.52  ? 423 SER   D N     1 
ATOM   10124 C  CA    . SER   C 2  413 ? 32.293  -18.232 -19.017 1.00 55.16  ? 423 SER   D CA    1 
ATOM   10125 C  C     . SER   C 2  413 ? 31.994  -16.762 -18.775 1.00 57.97  ? 423 SER   D C     1 
ATOM   10126 O  O     . SER   C 2  413 ? 31.498  -16.422 -17.696 1.00 59.13  ? 423 SER   D O     1 
ATOM   10127 C  CB    . SER   C 2  413 ? 33.611  -18.635 -18.357 1.00 58.73  ? 423 SER   D CB    1 
ATOM   10128 O  OG    . SER   C 2  413 ? 33.508  -19.945 -17.808 1.00 68.45  ? 423 SER   D OG    1 
ATOM   10129 N  N     . ASN   C 2  414 ? 32.268  -15.884 -19.746 1.00 58.44  ? 424 ASN   D N     1 
ATOM   10130 C  CA    . ASN   C 2  414 ? 31.854  -14.489 -19.601 1.00 53.31  ? 424 ASN   D CA    1 
ATOM   10131 C  C     . ASN   C 2  414 ? 30.337  -14.367 -19.649 1.00 49.21  ? 424 ASN   D C     1 
ATOM   10132 O  O     . ASN   C 2  414 ? 29.753  -13.609 -18.872 1.00 54.32  ? 424 ASN   D O     1 
ATOM   10133 C  CB    . ASN   C 2  414 ? 32.500  -13.613 -20.684 1.00 62.51  ? 424 ASN   D CB    1 
ATOM   10134 C  CG    . ASN   C 2  414 ? 32.155  -12.105 -20.545 1.00 56.59  ? 424 ASN   D CG    1 
ATOM   10135 O  OD1   . ASN   C 2  414 ? 31.994  -11.583 -19.436 1.00 55.26  ? 424 ASN   D OD1   1 
ATOM   10136 N  ND2   . ASN   C 2  414 ? 32.065  -11.408 -21.690 1.00 45.30  ? 424 ASN   D ND2   1 
ATOM   10137 N  N     . MET   C 2  415 ? 29.680  -15.109 -20.548 1.00 48.49  ? 425 MET   D N     1 
ATOM   10138 C  CA    . MET   C 2  415 ? 28.226  -15.022 -20.651 1.00 43.58  ? 425 MET   D CA    1 
ATOM   10139 C  C     . MET   C 2  415 ? 27.533  -15.720 -19.490 1.00 44.48  ? 425 MET   D C     1 
ATOM   10140 O  O     . MET   C 2  415 ? 26.403  -15.368 -19.147 1.00 42.09  ? 425 MET   D O     1 
ATOM   10141 C  CB    . MET   C 2  415 ? 27.741  -15.614 -21.973 1.00 43.40  ? 425 MET   D CB    1 
ATOM   10142 C  CG    . MET   C 2  415 ? 26.274  -15.334 -22.264 1.00 47.10  ? 425 MET   D CG    1 
ATOM   10143 S  SD    . MET   C 2  415 ? 25.738  -15.951 -23.875 1.00 55.10  ? 425 MET   D SD    1 
ATOM   10144 C  CE    . MET   C 2  415 ? 25.991  -17.720 -23.647 1.00 54.45  ? 425 MET   D CE    1 
ATOM   10145 N  N     . ASN   C 2  416 ? 28.176  -16.710 -18.875 1.00 50.41  ? 426 ASN   D N     1 
ATOM   10146 C  CA    . ASN   C 2  416 ? 27.557  -17.354 -17.723 1.00 46.16  ? 426 ASN   D CA    1 
ATOM   10147 C  C     . ASN   C 2  416 ? 27.590  -16.436 -16.500 1.00 47.25  ? 426 ASN   D C     1 
ATOM   10148 O  O     . ASN   C 2  416 ? 26.609  -16.359 -15.752 1.00 50.49  ? 426 ASN   D O     1 
ATOM   10149 C  CB    . ASN   C 2  416 ? 28.238  -18.697 -17.461 1.00 55.30  ? 426 ASN   D CB    1 
ATOM   10150 C  CG    . ASN   C 2  416 ? 28.056  -19.679 -18.623 1.00 63.88  ? 426 ASN   D CG    1 
ATOM   10151 O  OD1   . ASN   C 2  416 ? 26.973  -19.767 -19.215 1.00 58.35  ? 426 ASN   D OD1   1 
ATOM   10152 N  ND2   . ASN   C 2  416 ? 29.121  -20.406 -18.963 1.00 65.97  ? 426 ASN   D ND2   1 
ATOM   10153 N  N     . ASP   C 2  417 ? 28.699  -15.720 -16.286 1.00 42.79  ? 427 ASP   D N     1 
ATOM   10154 C  CA    . ASP   C 2  417 ? 28.691  -14.557 -15.407 1.00 36.35  ? 427 ASP   D CA    1 
ATOM   10155 C  C     . ASP   C 2  417 ? 27.406  -13.741 -15.573 1.00 41.38  ? 427 ASP   D C     1 
ATOM   10156 O  O     . ASP   C 2  417 ? 26.662  -13.519 -14.611 1.00 41.59  ? 427 ASP   D O     1 
ATOM   10157 C  CB    . ASP   C 2  417 ? 29.902  -13.661 -15.697 1.00 46.82  ? 427 ASP   D CB    1 
ATOM   10158 C  CG    . ASP   C 2  417 ? 31.233  -14.364 -15.511 1.00 53.82  ? 427 ASP   D CG    1 
ATOM   10159 O  OD1   . ASP   C 2  417 ? 31.274  -15.424 -14.845 1.00 50.15  ? 427 ASP   D OD1   1 
ATOM   10160 O  OD2   . ASP   C 2  417 ? 32.242  -13.823 -16.029 1.00 51.28  ? 427 ASP   D OD2   1 
ATOM   10161 N  N     . LEU   C 2  418 ? 27.133  -13.284 -16.803 1.00 38.61  ? 428 LEU   D N     1 
ATOM   10162 C  CA    . LEU   C 2  418 ? 26.014  -12.376 -17.040 1.00 37.60  ? 428 LEU   D CA    1 
ATOM   10163 C  C     . LEU   C 2  418 ? 24.702  -12.913 -16.481 1.00 45.04  ? 428 LEU   D C     1 
ATOM   10164 O  O     . LEU   C 2  418 ? 23.827  -12.132 -16.087 1.00 46.52  ? 428 LEU   D O     1 
ATOM   10165 C  CB    . LEU   C 2  418 ? 25.859  -12.089 -18.533 1.00 24.45  ? 428 LEU   D CB    1 
ATOM   10166 C  CG    . LEU   C 2  418 ? 24.922  -10.899 -18.753 1.00 31.29  ? 428 LEU   D CG    1 
ATOM   10167 C  CD1   . LEU   C 2  418 ? 25.549  -9.663  -18.154 1.00 40.00  ? 428 LEU   D CD1   1 
ATOM   10168 C  CD2   . LEU   C 2  418 ? 24.530  -10.653 -20.199 1.00 33.67  ? 428 LEU   D CD2   1 
ATOM   10169 N  N     . VAL   C 2  419 ? 24.540  -14.233 -16.446 1.00 40.15  ? 429 VAL   D N     1 
ATOM   10170 C  CA    . VAL   C 2  419 ? 23.337  -14.821 -15.871 1.00 38.31  ? 429 VAL   D CA    1 
ATOM   10171 C  C     . VAL   C 2  419 ? 23.457  -14.907 -14.355 1.00 38.04  ? 429 VAL   D C     1 
ATOM   10172 O  O     . VAL   C 2  419 ? 22.562  -14.477 -13.622 1.00 41.06  ? 429 VAL   D O     1 
ATOM   10173 C  CB    . VAL   C 2  419 ? 23.072  -16.202 -16.504 1.00 44.17  ? 429 VAL   D CB    1 
ATOM   10174 C  CG1   . VAL   C 2  419 ? 21.769  -16.816 -15.983 1.00 40.92  ? 429 VAL   D CG1   1 
ATOM   10175 C  CG2   . VAL   C 2  419 ? 23.041  -16.079 -18.008 1.00 41.34  ? 429 VAL   D CG2   1 
ATOM   10176 N  N     . SER   C 2  420 ? 24.562  -15.466 -13.858 1.00 36.76  ? 430 SER   D N     1 
ATOM   10177 C  CA    . SER   C 2  420 ? 24.773  -15.497 -12.418 1.00 42.58  ? 430 SER   D CA    1 
ATOM   10178 C  C     . SER   C 2  420 ? 24.552  -14.119 -11.807 1.00 51.51  ? 430 SER   D C     1 
ATOM   10179 O  O     . SER   C 2  420 ? 24.095  -14.010 -10.661 1.00 51.68  ? 430 SER   D O     1 
ATOM   10180 C  CB    . SER   C 2  420 ? 26.185  -15.992 -12.096 1.00 43.10  ? 430 SER   D CB    1 
ATOM   10181 O  OG    . SER   C 2  420 ? 26.616  -16.976 -13.014 1.00 52.59  ? 430 SER   D OG    1 
ATOM   10182 N  N     . GLU   C 2  421 ? 24.867  -13.058 -12.558 1.00 50.10  ? 431 GLU   D N     1 
ATOM   10183 C  CA    . GLU   C 2  421 ? 24.669  -11.702 -12.059 1.00 46.29  ? 431 GLU   D CA    1 
ATOM   10184 C  C     . GLU   C 2  421 ? 23.193  -11.331 -12.062 1.00 39.97  ? 431 GLU   D C     1 
ATOM   10185 O  O     . GLU   C 2  421 ? 22.659  -10.890 -11.042 1.00 47.34  ? 431 GLU   D O     1 
ATOM   10186 C  CB    . GLU   C 2  421 ? 25.495  -10.713 -12.886 1.00 49.17  ? 431 GLU   D CB    1 
ATOM   10187 C  CG    . GLU   C 2  421 ? 27.011  -10.945 -12.754 1.00 46.43  ? 431 GLU   D CG    1 
ATOM   10188 C  CD    . GLU   C 2  421 ? 27.827  -10.195 -13.793 1.00 46.20  ? 431 GLU   D CD    1 
ATOM   10189 O  OE1   . GLU   C 2  421 ? 27.339  -9.179  -14.339 1.00 49.45  ? 431 GLU   D OE1   1 
ATOM   10190 O  OE2   . GLU   C 2  421 ? 28.967  -10.628 -14.061 1.00 45.90  ? 431 GLU   D OE2   1 
ATOM   10191 N  N     . TYR   C 2  422 ? 22.508  -11.522 -13.191 1.00 35.25  ? 432 TYR   D N     1 
ATOM   10192 C  CA    . TYR   C 2  422 ? 21.082  -11.219 -13.237 1.00 31.15  ? 432 TYR   D CA    1 
ATOM   10193 C  C     . TYR   C 2  422 ? 20.337  -11.916 -12.118 1.00 39.87  ? 432 TYR   D C     1 
ATOM   10194 O  O     . TYR   C 2  422 ? 19.301  -11.425 -11.652 1.00 47.03  ? 432 TYR   D O     1 
ATOM   10195 C  CB    . TYR   C 2  422 ? 20.490  -11.627 -14.583 1.00 35.33  ? 432 TYR   D CB    1 
ATOM   10196 C  CG    . TYR   C 2  422 ? 20.570  -10.535 -15.622 1.00 39.47  ? 432 TYR   D CG    1 
ATOM   10197 C  CD1   . TYR   C 2  422 ? 19.871  -9.354  -15.436 1.00 36.25  ? 432 TYR   D CD1   1 
ATOM   10198 C  CD2   . TYR   C 2  422 ? 21.319  -10.689 -16.796 1.00 28.98  ? 432 TYR   D CD2   1 
ATOM   10199 C  CE1   . TYR   C 2  422 ? 19.919  -8.345  -16.358 1.00 36.85  ? 432 TYR   D CE1   1 
ATOM   10200 C  CE2   . TYR   C 2  422 ? 21.368  -9.678  -17.735 1.00 31.90  ? 432 TYR   D CE2   1 
ATOM   10201 C  CZ    . TYR   C 2  422 ? 20.665  -8.499  -17.501 1.00 35.42  ? 432 TYR   D CZ    1 
ATOM   10202 O  OH    . TYR   C 2  422 ? 20.660  -7.443  -18.381 1.00 34.98  ? 432 TYR   D OH    1 
ATOM   10203 N  N     . GLN   C 2  423 ? 20.832  -13.072 -11.690 1.00 40.11  ? 433 GLN   D N     1 
ATOM   10204 C  CA    . GLN   C 2  423 ? 20.227  -13.763 -10.564 1.00 39.06  ? 433 GLN   D CA    1 
ATOM   10205 C  C     . GLN   C 2  423 ? 20.608  -13.072 -9.261  1.00 42.69  ? 433 GLN   D C     1 
ATOM   10206 O  O     . GLN   C 2  423 ? 19.746  -12.789 -8.423  1.00 44.86  ? 433 GLN   D O     1 
ATOM   10207 C  CB    . GLN   C 2  423 ? 20.658  -15.236 -10.567 1.00 37.73  ? 433 GLN   D CB    1 
ATOM   10208 C  CG    . GLN   C 2  423 ? 19.855  -16.137 -9.635  1.00 32.10  ? 433 GLN   D CG    1 
ATOM   10209 C  CD    . GLN   C 2  423 ? 18.413  -16.286 -10.070 1.00 39.41  ? 433 GLN   D CD    1 
ATOM   10210 O  OE1   . GLN   C 2  423 ? 18.107  -16.299 -11.267 1.00 37.00  ? 433 GLN   D OE1   1 
ATOM   10211 N  NE2   . GLN   C 2  423 ? 17.515  -16.395 -9.096  1.00 35.76  ? 433 GLN   D NE2   1 
ATOM   10212 N  N     . GLN   C 2  424 ? 21.897  -12.759 -9.103  1.00 42.24  ? 434 GLN   D N     1 
ATOM   10213 C  CA    . GLN   C 2  424 ? 22.392  -12.143 -7.877  1.00 45.25  ? 434 GLN   D CA    1 
ATOM   10214 C  C     . GLN   C 2  424 ? 21.528  -10.960 -7.462  1.00 43.72  ? 434 GLN   D C     1 
ATOM   10215 O  O     . GLN   C 2  424 ? 21.272  -10.755 -6.268  1.00 48.98  ? 434 GLN   D O     1 
ATOM   10216 C  CB    . GLN   C 2  424 ? 23.850  -11.709 -8.071  1.00 48.25  ? 434 GLN   D CB    1 
ATOM   10217 C  CG    . GLN   C 2  424 ? 24.580  -11.362 -6.781  1.00 48.50  ? 434 GLN   D CG    1 
ATOM   10218 C  CD    . GLN   C 2  424 ? 25.350  -10.052 -6.875  1.00 59.99  ? 434 GLN   D CD    1 
ATOM   10219 O  OE1   . GLN   C 2  424 ? 26.122  -9.842  -7.814  1.00 65.96  ? 434 GLN   D OE1   1 
ATOM   10220 N  NE2   . GLN   C 2  424 ? 25.138  -9.158  -5.898  1.00 61.13  ? 434 GLN   D NE2   1 
ATOM   10221 N  N     . TYR   C 2  425 ? 21.052  -10.185 -8.435  1.00 33.39  ? 435 TYR   D N     1 
ATOM   10222 C  CA    . TYR   C 2  425 ? 20.226  -9.017  -8.163  1.00 34.45  ? 435 TYR   D CA    1 
ATOM   10223 C  C     . TYR   C 2  425 ? 18.735  -9.341  -8.127  1.00 43.06  ? 435 TYR   D C     1 
ATOM   10224 O  O     . TYR   C 2  425 ? 17.969  -8.632  -7.459  1.00 50.85  ? 435 TYR   D O     1 
ATOM   10225 C  CB    . TYR   C 2  425 ? 20.519  -7.925  -9.201  1.00 34.07  ? 435 TYR   D CB    1 
ATOM   10226 C  CG    . TYR   C 2  425 ? 21.887  -7.312  -9.021  1.00 29.78  ? 435 TYR   D CG    1 
ATOM   10227 C  CD1   . TYR   C 2  425 ? 22.157  -6.528  -7.925  1.00 34.41  ? 435 TYR   D CD1   1 
ATOM   10228 C  CD2   . TYR   C 2  425 ? 22.907  -7.527  -9.931  1.00 26.44  ? 435 TYR   D CD2   1 
ATOM   10229 C  CE1   . TYR   C 2  425 ? 23.393  -5.971  -7.723  1.00 35.09  ? 435 TYR   D CE1   1 
ATOM   10230 C  CE2   . TYR   C 2  425 ? 24.161  -6.969  -9.737  1.00 32.31  ? 435 TYR   D CE2   1 
ATOM   10231 C  CZ    . TYR   C 2  425 ? 24.398  -6.194  -8.614  1.00 36.78  ? 435 TYR   D CZ    1 
ATOM   10232 O  OH    . TYR   C 2  425 ? 25.624  -5.602  -8.369  1.00 36.01  ? 435 TYR   D OH    1 
ATOM   10233 N  N     . GLN   C 2  426 ? 18.307  -10.402 -8.814  1.00 36.77  ? 436 GLN   D N     1 
ATOM   10234 C  CA    . GLN   C 2  426 ? 16.937  -10.873 -8.669  1.00 33.69  ? 436 GLN   D CA    1 
ATOM   10235 C  C     . GLN   C 2  426 ? 16.686  -11.437 -7.268  1.00 44.19  ? 436 GLN   D C     1 
ATOM   10236 O  O     . GLN   C 2  426 ? 15.598  -11.265 -6.701  1.00 42.52  ? 436 GLN   D O     1 
ATOM   10237 C  CB    . GLN   C 2  426 ? 16.666  -11.910 -9.742  1.00 38.09  ? 436 GLN   D CB    1 
ATOM   10238 C  CG    . GLN   C 2  426 ? 15.370  -12.625 -9.579  1.00 44.17  ? 436 GLN   D CG    1 
ATOM   10239 C  CD    . GLN   C 2  426 ? 15.122  -13.565 -10.718 1.00 38.00  ? 436 GLN   D CD    1 
ATOM   10240 O  OE1   . GLN   C 2  426 ? 15.200  -13.177 -11.875 1.00 41.34  ? 436 GLN   D OE1   1 
ATOM   10241 N  NE2   . GLN   C 2  426 ? 14.833  -14.816 -10.401 1.00 37.74  ? 436 GLN   D NE2   1 
ATOM   10242 N  N     . ASP   C 2  427 ? 17.688  -12.105 -6.691  1.00 41.96  ? 437 ASP   D N     1 
ATOM   10243 C  CA    . ASP   C 2  427 ? 17.624  -12.640 -5.338  1.00 38.65  ? 437 ASP   D CA    1 
ATOM   10244 C  C     . ASP   C 2  427 ? 17.849  -11.585 -4.266  1.00 45.30  ? 437 ASP   D C     1 
ATOM   10245 O  O     . ASP   C 2  427 ? 17.689  -11.894 -3.082  1.00 51.06  ? 437 ASP   D O     1 
ATOM   10246 C  CB    . ASP   C 2  427 ? 18.680  -13.739 -5.137  1.00 43.14  ? 437 ASP   D CB    1 
ATOM   10247 C  CG    . ASP   C 2  427 ? 18.386  -15.020 -5.917  1.00 45.47  ? 437 ASP   D CG    1 
ATOM   10248 O  OD1   . ASP   C 2  427 ? 17.270  -15.164 -6.492  1.00 43.91  ? 437 ASP   D OD1   1 
ATOM   10249 O  OD2   . ASP   C 2  427 ? 19.300  -15.886 -5.934  1.00 31.66  ? 437 ASP   D OD2   1 
ATOM   10250 N  N     . ALA   C 2  428 ? 18.236  -10.369 -4.633  1.00 46.26  ? 438 ALA   D N     1 
ATOM   10251 C  CA    . ALA   C 2  428 ? 18.606  -9.383  -3.629  1.00 43.84  ? 438 ALA   D CA    1 
ATOM   10252 C  C     . ALA   C 2  428 ? 17.363  -8.850  -2.909  1.00 49.75  ? 438 ALA   D C     1 
ATOM   10253 O  O     . ALA   C 2  428 ? 16.223  -9.022  -3.359  1.00 52.59  ? 438 ALA   D O     1 
ATOM   10254 C  CB    . ALA   C 2  428 ? 19.404  -8.245  -4.271  1.00 43.49  ? 438 ALA   D CB    1 
ATOM   10255 N  N     . THR   C 2  429 ? 17.603  -8.177  -1.776  1.00 56.00  ? 439 THR   D N     1 
ATOM   10256 C  CA    . THR   C 2  429 ? 16.541  -7.723  -0.885  1.00 45.27  ? 439 THR   D CA    1 
ATOM   10257 C  C     . THR   C 2  429 ? 16.938  -6.419  -0.203  1.00 51.21  ? 439 THR   D C     1 
ATOM   10258 O  O     . THR   C 2  429 ? 18.035  -5.891  -0.399  1.00 52.60  ? 439 THR   D O     1 
ATOM   10259 C  CB    . THR   C 2  429 ? 16.244  -8.770  0.178   1.00 43.43  ? 439 THR   D CB    1 
ATOM   10260 O  OG1   . THR   C 2  429 ? 17.487  -9.270  0.690   1.00 58.38  ? 439 THR   D OG1   1 
ATOM   10261 C  CG2   . THR   C 2  429 ? 15.448  -9.895  -0.412  1.00 40.46  ? 439 THR   D CG2   1 
ATOM   10262 N  N     . ALA   C 2  430 ? 16.018  -5.921  0.633   1.00 61.79  ? 440 ALA   D N     1 
ATOM   10263 C  CA    . ALA   C 2  430 ? 16.288  -4.792  1.517   1.00 44.79  ? 440 ALA   D CA    1 
ATOM   10264 C  C     . ALA   C 2  430 ? 17.596  -4.961  2.281   1.00 57.80  ? 440 ALA   D C     1 
ATOM   10265 O  O     . ALA   C 2  430 ? 18.329  -3.988  2.485   1.00 64.23  ? 440 ALA   D O     1 
ATOM   10266 C  CB    . ALA   C 2  430 ? 15.131  -4.632  2.497   1.00 56.67  ? 440 ALA   D CB    1 
ATOM   10267 N  N     . ASP   C 2  431 ? 17.909  -6.180  2.722   1.00 70.22  ? 441 ASP   D N     1 
ATOM   10268 C  CA    . ASP   C 2  431 ? 19.197  -6.430  3.401   1.00 70.93  ? 441 ASP   D CA    1 
ATOM   10269 C  C     . ASP   C 2  431 ? 19.985  -7.612  2.814   1.00 65.72  ? 441 ASP   D C     1 
ATOM   10270 O  O     . ASP   C 2  431 ? 20.896  -7.425  1.994   1.00 62.92  ? 441 ASP   D O     1 
ATOM   10271 C  CB    . ASP   C 2  431 ? 18.954  -6.655  4.889   1.00 65.22  ? 441 ASP   D CB    1 
ATOM   10272 C  CG    . ASP   C 2  431 ? 17.820  -5.803  5.411   1.00 68.43  ? 441 ASP   D CG    1 
ATOM   10273 O  OD1   . ASP   C 2  431 ? 16.687  -5.925  4.871   1.00 52.91  ? 441 ASP   D OD1   1 
ATOM   10274 O  OD2   . ASP   C 2  431 ? 18.073  -5.002  6.339   1.00 70.04  ? 441 ASP   D OD2   1 
ATOM   10275 N  N     . MET   D 3  4   ? 20.192  89.546  91.900  1.00 75.04  ? 6   MET   E N     1 
ATOM   10276 C  CA    . MET   D 3  4   ? 20.196  90.182  93.209  1.00 60.11  ? 6   MET   E CA    1 
ATOM   10277 C  C     . MET   D 3  4   ? 21.550  90.841  93.468  1.00 65.16  ? 6   MET   E C     1 
ATOM   10278 O  O     . MET   D 3  4   ? 21.966  90.939  94.616  1.00 84.83  ? 6   MET   E O     1 
ATOM   10279 C  CB    . MET   D 3  4   ? 19.875  89.152  94.303  1.00 57.93  ? 6   MET   E CB    1 
ATOM   10280 C  CG    . MET   D 3  4   ? 19.761  89.721  95.723  1.00 68.45  ? 6   MET   E CG    1 
ATOM   10281 S  SD    . MET   D 3  4   ? 19.214  88.529  96.988  1.00 86.29  ? 6   MET   E SD    1 
ATOM   10282 C  CE    . MET   D 3  4   ? 20.692  87.576  97.359  1.00 49.14  ? 6   MET   E CE    1 
ATOM   10283 N  N     . GLU   D 3  5   ? 22.227  91.299  92.404  1.00 56.86  ? 7   GLU   E N     1 
ATOM   10284 C  CA    . GLU   D 3  5   ? 23.538  91.944  92.512  1.00 53.70  ? 7   GLU   E CA    1 
ATOM   10285 C  C     . GLU   D 3  5   ? 23.979  92.559  91.190  1.00 56.88  ? 7   GLU   E C     1 
ATOM   10286 O  O     . GLU   D 3  5   ? 24.546  91.850  90.357  1.00 58.10  ? 7   GLU   E O     1 
ATOM   10287 C  CB    . GLU   D 3  5   ? 24.603  90.935  92.958  1.00 55.23  ? 7   GLU   E CB    1 
ATOM   10288 C  CG    . GLU   D 3  5   ? 25.327  91.279  94.255  1.00 62.81  ? 7   GLU   E CG    1 
ATOM   10289 C  CD    . GLU   D 3  5   ? 26.794  91.635  94.061  1.00 72.81  ? 7   GLU   E CD    1 
ATOM   10290 O  OE1   . GLU   D 3  5   ? 27.537  90.823  93.463  1.00 66.56  ? 7   GLU   E OE1   1 
ATOM   10291 O  OE2   . GLU   D 3  5   ? 27.204  92.733  94.511  1.00 74.72  ? 7   GLU   E OE2   1 
ATOM   10292 N  N     . VAL   D 3  6   ? 23.765  93.864  90.984  1.00 58.90  ? 8   VAL   E N     1 
ATOM   10293 C  CA    . VAL   D 3  6   ? 24.154  94.529  89.736  1.00 45.04  ? 8   VAL   E CA    1 
ATOM   10294 C  C     . VAL   D 3  6   ? 25.618  94.944  89.800  1.00 44.87  ? 8   VAL   E C     1 
ATOM   10295 O  O     . VAL   D 3  6   ? 26.037  95.636  90.728  1.00 49.34  ? 8   VAL   E O     1 
ATOM   10296 C  CB    . VAL   D 3  6   ? 23.262  95.747  89.441  1.00 38.25  ? 8   VAL   E CB    1 
ATOM   10297 C  CG1   . VAL   D 3  6   ? 23.955  96.671  88.451  1.00 38.97  ? 8   VAL   E CG1   1 
ATOM   10298 C  CG2   . VAL   D 3  6   ? 21.918  95.302  88.894  1.00 34.64  ? 8   VAL   E CG2   1 
ATOM   10299 N  N     . ILE   D 3  7   ? 26.384  94.556  88.784  1.00 51.61  ? 9   ILE   E N     1 
ATOM   10300 C  CA    . ILE   D 3  7   ? 27.821  94.777  88.718  1.00 46.99  ? 9   ILE   E CA    1 
ATOM   10301 C  C     . ILE   D 3  7   ? 28.140  95.646  87.506  1.00 50.53  ? 9   ILE   E C     1 
ATOM   10302 O  O     . ILE   D 3  7   ? 27.364  95.722  86.549  1.00 46.17  ? 9   ILE   E O     1 
ATOM   10303 C  CB    . ILE   D 3  7   ? 28.564  93.420  88.673  1.00 53.83  ? 9   ILE   E CB    1 
ATOM   10304 C  CG1   . ILE   D 3  7   ? 28.753  92.890  90.092  1.00 56.66  ? 9   ILE   E CG1   1 
ATOM   10305 C  CG2   . ILE   D 3  7   ? 29.908  93.518  87.957  1.00 55.63  ? 9   ILE   E CG2   1 
ATOM   10306 C  CD1   . ILE   D 3  7   ? 29.686  93.759  90.912  1.00 68.13  ? 9   ILE   E CD1   1 
ATOM   10307 N  N     . GLU   D 3  8   ? 29.261  96.355  87.589  1.00 51.48  ? 10  GLU   E N     1 
ATOM   10308 C  CA    . GLU   D 3  8   ? 29.872  97.091  86.479  1.00 53.25  ? 10  GLU   E CA    1 
ATOM   10309 C  C     . GLU   D 3  8   ? 28.856  97.742  85.536  1.00 42.92  ? 10  GLU   E C     1 
ATOM   10310 O  O     . GLU   D 3  8   ? 28.921  97.598  84.318  1.00 45.55  ? 10  GLU   E O     1 
ATOM   10311 C  CB    . GLU   D 3  8   ? 30.811  96.180  85.702  1.00 54.93  ? 10  GLU   E CB    1 
ATOM   10312 C  CG    . GLU   D 3  8   ? 31.953  95.652  86.551  1.00 69.35  ? 10  GLU   E CG    1 
ATOM   10313 C  CD    . GLU   D 3  8   ? 32.407  94.270  86.121  1.00 80.35  ? 10  GLU   E CD    1 
ATOM   10314 O  OE1   . GLU   D 3  8   ? 31.912  93.782  85.079  1.00 86.40  ? 10  GLU   E OE1   1 
ATOM   10315 O  OE2   . GLU   D 3  8   ? 33.251  93.673  86.829  1.00 77.68  ? 10  GLU   E OE2   1 
ATOM   10316 N  N     . LEU   D 3  9   ? 27.946  98.519  86.111  1.00 41.76  ? 11  LEU   E N     1 
ATOM   10317 C  CA    . LEU   D 3  9   ? 27.038  99.326  85.299  1.00 46.51  ? 11  LEU   E CA    1 
ATOM   10318 C  C     . LEU   D 3  9   ? 27.833  100.350 84.482  1.00 48.61  ? 11  LEU   E C     1 
ATOM   10319 O  O     . LEU   D 3  9   ? 28.456  101.246 85.057  1.00 53.68  ? 11  LEU   E O     1 
ATOM   10320 C  CB    . LEU   D 3  9   ? 26.029  100.019 86.205  1.00 47.11  ? 11  LEU   E CB    1 
ATOM   10321 C  CG    . LEU   D 3  9   ? 25.092  100.879 85.378  1.00 45.77  ? 11  LEU   E CG    1 
ATOM   10322 C  CD1   . LEU   D 3  9   ? 24.534  99.997  84.275  1.00 36.80  ? 11  LEU   E CD1   1 
ATOM   10323 C  CD2   . LEU   D 3  9   ? 24.000  101.467 86.233  1.00 59.36  ? 11  LEU   E CD2   1 
ATOM   10324 N  N     . ASN   D 3  10  ? 27.811  100.237 83.145  1.00 48.51  ? 12  ASN   E N     1 
ATOM   10325 C  CA    . ASN   D 3  10  ? 28.517  101.150 82.240  1.00 42.64  ? 12  ASN   E CA    1 
ATOM   10326 C  C     . ASN   D 3  10  ? 27.510  101.841 81.326  1.00 41.31  ? 12  ASN   E C     1 
ATOM   10327 O  O     . ASN   D 3  10  ? 26.749  101.174 80.615  1.00 47.27  ? 12  ASN   E O     1 
ATOM   10328 C  CB    . ASN   D 3  10  ? 29.570  100.414 81.404  1.00 37.23  ? 12  ASN   E CB    1 
ATOM   10329 C  CG    . ASN   D 3  10  ? 30.823  100.052 82.209  1.00 52.00  ? 12  ASN   E CG    1 
ATOM   10330 O  OD1   . ASN   D 3  10  ? 31.281  98.905  82.205  1.00 56.04  ? 12  ASN   E OD1   1 
ATOM   10331 N  ND2   . ASN   D 3  10  ? 31.391  101.045 82.893  1.00 55.14  ? 12  ASN   E ND2   1 
ATOM   10332 N  N     . LYS   D 3  11  ? 27.513  103.171 81.332  1.00 49.48  ? 13  LYS   E N     1 
ATOM   10333 C  CA    . LYS   D 3  11  ? 26.494  103.964 80.652  1.00 47.44  ? 13  LYS   E CA    1 
ATOM   10334 C  C     . LYS   D 3  11  ? 27.117  104.851 79.580  1.00 44.15  ? 13  LYS   E C     1 
ATOM   10335 O  O     . LYS   D 3  11  ? 28.216  105.382 79.754  1.00 45.76  ? 13  LYS   E O     1 
ATOM   10336 C  CB    . LYS   D 3  11  ? 25.698  104.825 81.659  1.00 46.41  ? 13  LYS   E CB    1 
ATOM   10337 C  CG    . LYS   D 3  11  ? 24.586  104.056 82.411  1.00 43.22  ? 13  LYS   E CG    1 
ATOM   10338 C  CD    . LYS   D 3  11  ? 24.316  104.647 83.770  1.00 44.19  ? 13  LYS   E CD    1 
ATOM   10339 C  CE    . LYS   D 3  11  ? 23.752  106.061 83.675  1.00 51.53  ? 13  LYS   E CE    1 
ATOM   10340 N  NZ    . LYS   D 3  11  ? 22.264  106.122 83.566  1.00 41.07  ? 13  LYS   E NZ    1 
ATOM   10341 N  N     . CYS   D 3  12  ? 26.408  104.993 78.464  1.00 47.01  ? 14  CYS   E N     1 
ATOM   10342 C  CA    . CYS   D 3  12  ? 26.820  105.840 77.350  1.00 45.48  ? 14  CYS   E CA    1 
ATOM   10343 C  C     . CYS   D 3  12  ? 25.554  106.234 76.606  1.00 50.08  ? 14  CYS   E C     1 
ATOM   10344 O  O     . CYS   D 3  12  ? 24.482  105.677 76.849  1.00 60.05  ? 14  CYS   E O     1 
ATOM   10345 C  CB    . CYS   D 3  12  ? 27.784  105.122 76.413  1.00 49.50  ? 14  CYS   E CB    1 
ATOM   10346 S  SG    . CYS   D 3  12  ? 26.921  103.970 75.347  1.00 46.74  ? 14  CYS   E SG    1 
ATOM   10347 N  N     . THR   D 3  13  ? 25.681  107.188 75.680  1.00 50.40  ? 15  THR   E N     1 
ATOM   10348 C  CA    . THR   D 3  13  ? 24.478  107.680 75.006  1.00 50.81  ? 15  THR   E CA    1 
ATOM   10349 C  C     . THR   D 3  13  ? 23.814  106.620 74.118  1.00 60.53  ? 15  THR   E C     1 
ATOM   10350 O  O     . THR   D 3  13  ? 22.641  106.788 73.759  1.00 50.66  ? 15  THR   E O     1 
ATOM   10351 C  CB    . THR   D 3  13  ? 24.778  108.925 74.160  1.00 51.68  ? 15  THR   E CB    1 
ATOM   10352 O  OG1   . THR   D 3  13  ? 25.781  109.728 74.791  1.00 48.56  ? 15  THR   E OG1   1 
ATOM   10353 C  CG2   . THR   D 3  13  ? 23.513  109.754 74.004  1.00 56.95  ? 15  THR   E CG2   1 
ATOM   10354 N  N     . SER   D 3  14  ? 24.533  105.543 73.750  1.00 54.19  ? 16  SER   E N     1 
ATOM   10355 C  CA    . SER   D 3  14  ? 23.961  104.462 72.947  1.00 48.93  ? 16  SER   E CA    1 
ATOM   10356 C  C     . SER   D 3  14  ? 23.147  103.467 73.782  1.00 57.61  ? 16  SER   E C     1 
ATOM   10357 O  O     . SER   D 3  14  ? 22.226  102.825 73.251  1.00 52.69  ? 16  SER   E O     1 
ATOM   10358 C  CB    . SER   D 3  14  ? 25.072  103.703 72.207  1.00 53.30  ? 16  SER   E CB    1 
ATOM   10359 O  OG    . SER   D 3  14  ? 25.222  104.119 70.859  1.00 60.06  ? 16  SER   E OG    1 
ATOM   10360 N  N     . GLY   D 3  15  ? 23.474  103.301 75.057  1.00 52.75  ? 17  GLY   E N     1 
ATOM   10361 C  CA    . GLY   D 3  15  ? 22.798  102.323 75.888  1.00 47.95  ? 17  GLY   E CA    1 
ATOM   10362 C  C     . GLY   D 3  15  ? 23.661  101.981 77.085  1.00 50.47  ? 17  GLY   E C     1 
ATOM   10363 O  O     . GLY   D 3  15  ? 24.724  102.560 77.285  1.00 60.16  ? 17  GLY   E O     1 
ATOM   10364 N  N     . GLN   D 3  16  ? 23.182  101.022 77.875  1.00 46.38  ? 18  GLN   E N     1 
ATOM   10365 C  CA    . GLN   D 3  16  ? 23.864  100.642 79.108  1.00 42.69  ? 18  GLN   E CA    1 
ATOM   10366 C  C     . GLN   D 3  16  ? 24.291  99.181  79.061  1.00 45.47  ? 18  GLN   E C     1 
ATOM   10367 O  O     . GLN   D 3  16  ? 23.794  98.392  78.246  1.00 44.91  ? 18  GLN   E O     1 
ATOM   10368 C  CB    . GLN   D 3  16  ? 22.978  100.863 80.339  1.00 38.34  ? 18  GLN   E CB    1 
ATOM   10369 C  CG    . GLN   D 3  16  ? 22.135  102.132 80.327  1.00 38.78  ? 18  GLN   E CG    1 
ATOM   10370 C  CD    . GLN   D 3  16  ? 21.379  102.301 81.624  1.00 39.62  ? 18  GLN   E CD    1 
ATOM   10371 O  OE1   . GLN   D 3  16  ? 21.857  101.889 82.684  1.00 37.61  ? 18  GLN   E OE1   1 
ATOM   10372 N  NE2   . GLN   D 3  16  ? 20.185  102.889 81.549  1.00 34.72  ? 18  GLN   E NE2   1 
ATOM   10373 N  N     . SER   D 3  17  ? 25.210  98.825  79.966  1.00 36.29  ? 19  SER   E N     1 
ATOM   10374 C  CA    . SER   D 3  17  ? 25.743  97.470  80.058  1.00 38.79  ? 19  SER   E CA    1 
ATOM   10375 C  C     . SER   D 3  17  ? 26.077  97.144  81.512  1.00 37.61  ? 19  SER   E C     1 
ATOM   10376 O  O     . SER   D 3  17  ? 26.663  97.962  82.220  1.00 37.09  ? 19  SER   E O     1 
ATOM   10377 C  CB    . SER   D 3  17  ? 26.990  97.304  79.173  1.00 38.15  ? 19  SER   E CB    1 
ATOM   10378 O  OG    . SER   D 3  17  ? 28.102  96.808  79.924  1.00 44.40  ? 19  SER   E OG    1 
ATOM   10379 N  N     . PHE   D 3  18  ? 25.737  95.935  81.942  1.00 33.17  ? 20  PHE   E N     1 
ATOM   10380 C  CA    . PHE   D 3  18  ? 25.906  95.552  83.338  1.00 32.34  ? 20  PHE   E CA    1 
ATOM   10381 C  C     . PHE   D 3  18  ? 25.794  94.033  83.467  1.00 33.03  ? 20  PHE   E C     1 
ATOM   10382 O  O     . PHE   D 3  18  ? 25.367  93.333  82.543  1.00 38.17  ? 20  PHE   E O     1 
ATOM   10383 C  CB    . PHE   D 3  18  ? 24.878  96.253  84.240  1.00 31.77  ? 20  PHE   E CB    1 
ATOM   10384 C  CG    . PHE   D 3  18  ? 23.449  95.845  83.983  1.00 29.75  ? 20  PHE   E CG    1 
ATOM   10385 C  CD1   . PHE   D 3  18  ? 22.702  96.457  82.981  1.00 35.05  ? 20  PHE   E CD1   1 
ATOM   10386 C  CD2   . PHE   D 3  18  ? 22.844  94.870  84.749  1.00 26.82  ? 20  PHE   E CD2   1 
ATOM   10387 C  CE1   . PHE   D 3  18  ? 21.383  96.098  82.747  1.00 26.36  ? 20  PHE   E CE1   1 
ATOM   10388 C  CE2   . PHE   D 3  18  ? 21.520  94.509  84.513  1.00 28.90  ? 20  PHE   E CE2   1 
ATOM   10389 C  CZ    . PHE   D 3  18  ? 20.797  95.133  83.510  1.00 26.27  ? 20  PHE   E CZ    1 
ATOM   10390 N  N     . GLU   D 3  19  ? 26.182  93.533  84.634  1.00 26.48  ? 21  GLU   E N     1 
ATOM   10391 C  CA    . GLU   D 3  19  ? 26.086  92.124  84.975  1.00 33.75  ? 21  GLU   E CA    1 
ATOM   10392 C  C     . GLU   D 3  19  ? 25.188  91.964  86.198  1.00 38.94  ? 21  GLU   E C     1 
ATOM   10393 O  O     . GLU   D 3  19  ? 25.305  92.721  87.163  1.00 41.47  ? 21  GLU   E O     1 
ATOM   10394 C  CB    . GLU   D 3  19  ? 27.471  91.558  85.247  1.00 34.04  ? 21  GLU   E CB    1 
ATOM   10395 C  CG    . GLU   D 3  19  ? 27.536  90.071  85.270  1.00 30.37  ? 21  GLU   E CG    1 
ATOM   10396 C  CD    . GLU   D 3  19  ? 28.940  89.592  85.006  1.00 49.24  ? 21  GLU   E CD    1 
ATOM   10397 O  OE1   . GLU   D 3  19  ? 29.795  90.456  84.675  1.00 48.23  ? 21  GLU   E OE1   1 
ATOM   10398 O  OE2   . GLU   D 3  19  ? 29.189  88.367  85.131  1.00 52.90  ? 21  GLU   E OE2   1 
ATOM   10399 N  N     . VAL   D 3  20  ? 24.287  90.992  86.161  1.00 34.05  ? 22  VAL   E N     1 
ATOM   10400 C  CA    . VAL   D 3  20  ? 23.404  90.731  87.282  1.00 31.86  ? 22  VAL   E CA    1 
ATOM   10401 C  C     . VAL   D 3  20  ? 23.571  89.263  87.643  1.00 38.85  ? 22  VAL   E C     1 
ATOM   10402 O  O     . VAL   D 3  20  ? 23.187  88.384  86.866  1.00 40.34  ? 22  VAL   E O     1 
ATOM   10403 C  CB    . VAL   D 3  20  ? 21.938  91.071  86.974  1.00 38.39  ? 22  VAL   E CB    1 
ATOM   10404 C  CG1   . VAL   D 3  20  ? 21.475  90.375  85.710  1.00 41.80  ? 22  VAL   E CG1   1 
ATOM   10405 C  CG2   . VAL   D 3  20  ? 21.036  90.700  88.154  1.00 40.07  ? 22  VAL   E CG2   1 
ATOM   10406 N  N     . ILE   D 3  21  ? 24.157  88.999  88.818  1.00 51.21  ? 23  ILE   E N     1 
ATOM   10407 C  CA    . ILE   D 3  21  ? 24.332  87.649  89.343  1.00 50.82  ? 23  ILE   E CA    1 
ATOM   10408 C  C     . ILE   D 3  21  ? 23.321  87.393  90.447  1.00 45.34  ? 23  ILE   E C     1 
ATOM   10409 O  O     . ILE   D 3  21  ? 23.007  88.284  91.242  1.00 48.47  ? 23  ILE   E O     1 
ATOM   10410 C  CB    . ILE   D 3  21  ? 25.771  87.437  89.845  1.00 44.20  ? 23  ILE   E CB    1 
ATOM   10411 C  CG1   . ILE   D 3  21  ? 25.854  86.217  90.759  1.00 52.09  ? 23  ILE   E CG1   1 
ATOM   10412 C  CG2   . ILE   D 3  21  ? 26.289  88.676  90.490  1.00 49.00  ? 23  ILE   E CG2   1 
ATOM   10413 C  CD1   . ILE   D 3  21  ? 27.326  85.802  91.049  1.00 66.96  ? 23  ILE   E CD1   1 
ATOM   10414 N  N     . LEU   D 3  22  ? 22.806  86.172  90.491  1.00 51.71  ? 24  LEU   E N     1 
ATOM   10415 C  CA    . LEU   D 3  22  ? 21.781  85.775  91.445  1.00 51.28  ? 24  LEU   E CA    1 
ATOM   10416 C  C     . LEU   D 3  22  ? 22.275  84.786  92.491  1.00 56.17  ? 24  LEU   E C     1 
ATOM   10417 O  O     . LEU   D 3  22  ? 21.722  84.747  93.593  1.00 68.13  ? 24  LEU   E O     1 
ATOM   10418 C  CB    . LEU   D 3  22  ? 20.588  85.163  90.701  1.00 48.43  ? 24  LEU   E CB    1 
ATOM   10419 C  CG    . LEU   D 3  22  ? 20.000  85.997  89.560  1.00 54.42  ? 24  LEU   E CG    1 
ATOM   10420 C  CD1   . LEU   D 3  22  ? 19.187  85.138  88.600  1.00 36.90  ? 24  LEU   E CD1   1 
ATOM   10421 C  CD2   . LEU   D 3  22  ? 19.144  87.123  90.125  1.00 59.32  ? 24  LEU   E CD2   1 
ATOM   10422 N  N     . LYS   D 3  23  ? 23.304  83.994  92.173  1.00 51.92  ? 25  LYS   E N     1 
ATOM   10423 C  CA    . LYS   D 3  23  ? 23.885  82.994  93.054  1.00 56.33  ? 25  LYS   E CA    1 
ATOM   10424 C  C     . LYS   D 3  23  ? 25.330  82.819  92.605  1.00 62.50  ? 25  LYS   E C     1 
ATOM   10425 O  O     . LYS   D 3  23  ? 25.583  82.805  91.393  1.00 66.79  ? 25  LYS   E O     1 
ATOM   10426 C  CB    . LYS   D 3  23  ? 23.133  81.653  92.987  1.00 50.69  ? 25  LYS   E CB    1 
ATOM   10427 C  CG    . LYS   D 3  23  ? 21.608  81.778  93.071  1.00 55.55  ? 25  LYS   E CG    1 
ATOM   10428 C  CD    . LYS   D 3  23  ? 20.893  80.427  92.970  1.00 59.01  ? 25  LYS   E CD    1 
ATOM   10429 C  CE    . LYS   D 3  23  ? 19.388  80.643  92.927  1.00 63.85  ? 25  LYS   E CE    1 
ATOM   10430 N  NZ    . LYS   D 3  23  ? 19.080  82.092  93.112  1.00 58.15  ? 25  LYS   E NZ    1 
ATOM   10431 N  N     . PRO   D 3  24  ? 26.292  82.717  93.521  1.00 62.00  ? 26  PRO   E N     1 
ATOM   10432 C  CA    . PRO   D 3  24  ? 27.706  82.530  93.109  1.00 62.79  ? 26  PRO   E CA    1 
ATOM   10433 C  C     . PRO   D 3  24  ? 28.043  81.056  92.929  1.00 62.22  ? 26  PRO   E C     1 
ATOM   10434 O  O     . PRO   D 3  24  ? 27.328  80.180  93.438  1.00 65.59  ? 26  PRO   E O     1 
ATOM   10435 C  CB    . PRO   D 3  24  ? 28.500  83.153  94.271  1.00 65.89  ? 26  PRO   E CB    1 
ATOM   10436 C  CG    . PRO   D 3  24  ? 27.454  83.853  95.153  1.00 69.90  ? 26  PRO   E CG    1 
ATOM   10437 C  CD    . PRO   D 3  24  ? 26.175  83.118  94.930  1.00 54.95  ? 26  PRO   E CD    1 
ATOM   10438 N  N     . PRO   D 3  25  ? 29.137  80.734  92.229  1.00 57.44  ? 27  PRO   E N     1 
ATOM   10439 C  CA    . PRO   D 3  25  ? 29.420  79.321  91.885  1.00 59.07  ? 27  PRO   E CA    1 
ATOM   10440 C  C     . PRO   D 3  25  ? 29.624  78.415  93.098  1.00 64.55  ? 27  PRO   E C     1 
ATOM   10441 O  O     . PRO   D 3  25  ? 30.536  78.626  93.907  1.00 75.68  ? 27  PRO   E O     1 
ATOM   10442 C  CB    . PRO   D 3  25  ? 30.701  79.411  91.032  1.00 53.75  ? 27  PRO   E CB    1 
ATOM   10443 C  CG    . PRO   D 3  25  ? 31.319  80.731  91.375  1.00 56.50  ? 27  PRO   E CG    1 
ATOM   10444 C  CD    . PRO   D 3  25  ? 30.158  81.653  91.689  1.00 59.33  ? 27  PRO   E CD    1 
ATOM   10445 N  N     . SER   D 3  26  ? 28.788  77.371  93.192  1.00 50.20  ? 28  SER   E N     1 
ATOM   10446 C  CA    . SER   D 3  26  ? 28.975  76.240  94.130  1.00 52.34  ? 28  SER   E CA    1 
ATOM   10447 C  C     . SER   D 3  26  ? 30.238  75.379  93.877  1.00 60.04  ? 28  SER   E C     1 
ATOM   10448 O  O     . SER   D 3  26  ? 31.387  75.851  93.880  1.00 53.90  ? 28  SER   E O     1 
ATOM   10449 C  CB    . SER   D 3  26  ? 27.746  75.307  94.091  1.00 56.50  ? 28  SER   E CB    1 
ATOM   10450 O  OG    . SER   D 3  26  ? 26.584  75.926  93.529  1.00 50.34  ? 28  SER   E OG    1 
ATOM   10451 N  N     . ASP   D 3  42  ? 46.903  71.697  66.126  1.00 57.29  ? 44  ASP   E N     1 
ATOM   10452 C  CA    . ASP   D 3  42  ? 46.629  72.768  65.168  1.00 74.68  ? 44  ASP   E CA    1 
ATOM   10453 C  C     . ASP   D 3  42  ? 47.648  72.730  64.033  1.00 78.86  ? 44  ASP   E C     1 
ATOM   10454 O  O     . ASP   D 3  42  ? 48.786  73.183  64.201  1.00 78.43  ? 44  ASP   E O     1 
ATOM   10455 C  CB    . ASP   D 3  42  ? 46.638  74.141  65.857  1.00 84.12  ? 44  ASP   E CB    1 
ATOM   10456 C  CG    . ASP   D 3  42  ? 45.864  75.206  65.069  1.00 80.13  ? 44  ASP   E CG    1 
ATOM   10457 O  OD1   . ASP   D 3  42  ? 46.459  75.808  64.138  1.00 67.92  ? 44  ASP   E OD1   1 
ATOM   10458 O  OD2   . ASP   D 3  42  ? 44.662  75.427  65.379  1.00 61.73  ? 44  ASP   E OD2   1 
ATOM   10459 N  N     . PRO   D 3  43  ? 47.220  72.198  62.867  1.00 77.47  ? 45  PRO   E N     1 
ATOM   10460 C  CA    . PRO   D 3  43  ? 48.168  71.892  61.783  1.00 71.80  ? 45  PRO   E CA    1 
ATOM   10461 C  C     . PRO   D 3  43  ? 48.767  73.103  61.074  1.00 65.83  ? 45  PRO   E C     1 
ATOM   10462 O  O     . PRO   D 3  43  ? 48.464  74.258  61.395  1.00 63.37  ? 45  PRO   E O     1 
ATOM   10463 C  CB    . PRO   D 3  43  ? 47.327  71.044  60.818  1.00 69.77  ? 45  PRO   E CB    1 
ATOM   10464 C  CG    . PRO   D 3  43  ? 45.909  71.380  61.127  1.00 62.31  ? 45  PRO   E CG    1 
ATOM   10465 C  CD    . PRO   D 3  43  ? 45.862  71.698  62.583  1.00 72.90  ? 45  PRO   E CD    1 
ATOM   10466 N  N     . SER   D 3  44  ? 49.604  72.815  60.071  1.00 59.05  ? 46  SER   E N     1 
ATOM   10467 C  CA    . SER   D 3  44  ? 50.556  73.749  59.485  1.00 52.56  ? 46  SER   E CA    1 
ATOM   10468 C  C     . SER   D 3  44  ? 50.470  73.713  57.968  1.00 51.63  ? 46  SER   E C     1 
ATOM   10469 O  O     . SER   D 3  44  ? 50.099  72.692  57.385  1.00 58.38  ? 46  SER   E O     1 
ATOM   10470 C  CB    . SER   D 3  44  ? 51.954  73.365  59.909  1.00 67.17  ? 46  SER   E CB    1 
ATOM   10471 O  OG    . SER   D 3  44  ? 52.027  71.950  60.002  1.00 62.33  ? 46  SER   E OG    1 
ATOM   10472 N  N     . LEU   D 3  45  ? 50.844  74.820  57.314  1.00 57.42  ? 47  LEU   E N     1 
ATOM   10473 C  CA    . LEU   D 3  45  ? 50.744  74.852  55.853  1.00 51.07  ? 47  LEU   E CA    1 
ATOM   10474 C  C     . LEU   D 3  45  ? 51.407  73.631  55.241  1.00 55.21  ? 47  LEU   E C     1 
ATOM   10475 O  O     . LEU   D 3  45  ? 50.976  73.149  54.189  1.00 58.30  ? 47  LEU   E O     1 
ATOM   10476 C  CB    . LEU   D 3  45  ? 51.360  76.133  55.287  1.00 37.94  ? 47  LEU   E CB    1 
ATOM   10477 C  CG    . LEU   D 3  45  ? 51.386  76.253  53.762  1.00 42.96  ? 47  LEU   E CG    1 
ATOM   10478 C  CD1   . LEU   D 3  45  ? 50.102  75.704  53.186  1.00 56.11  ? 47  LEU   E CD1   1 
ATOM   10479 C  CD2   . LEU   D 3  45  ? 51.592  77.687  53.290  1.00 32.52  ? 47  LEU   E CD2   1 
ATOM   10480 N  N     . GLU   D 3  46  ? 52.435  73.105  55.906  1.00 58.81  ? 48  GLU   E N     1 
ATOM   10481 C  CA    . GLU   D 3  46  ? 53.087  71.884  55.454  1.00 56.33  ? 48  GLU   E CA    1 
ATOM   10482 C  C     . GLU   D 3  46  ? 52.144  70.693  55.557  1.00 54.77  ? 48  GLU   E C     1 
ATOM   10483 O  O     . GLU   D 3  46  ? 51.804  70.066  54.550  1.00 58.14  ? 48  GLU   E O     1 
ATOM   10484 C  CB    . GLU   D 3  46  ? 54.358  71.657  56.273  1.00 64.53  ? 48  GLU   E CB    1 
ATOM   10485 C  CG    . GLU   D 3  46  ? 55.070  70.340  56.017  1.00 71.31  ? 48  GLU   E CG    1 
ATOM   10486 C  CD    . GLU   D 3  46  ? 56.193  70.102  57.022  1.00 89.74  ? 48  GLU   E CD    1 
ATOM   10487 O  OE1   . GLU   D 3  46  ? 56.499  71.039  57.798  1.00 88.90  ? 48  GLU   E OE1   1 
ATOM   10488 O  OE2   . GLU   D 3  46  ? 56.762  68.987  57.042  1.00 85.38  ? 48  GLU   E OE2   1 
ATOM   10489 N  N     . GLU   D 3  47  ? 51.694  70.374  56.771  1.00 60.13  ? 49  GLU   E N     1 
ATOM   10490 C  CA    . GLU   D 3  47  ? 50.780  69.248  56.942  1.00 58.10  ? 49  GLU   E CA    1 
ATOM   10491 C  C     . GLU   D 3  47  ? 49.491  69.439  56.155  1.00 62.19  ? 49  GLU   E C     1 
ATOM   10492 O  O     . GLU   D 3  47  ? 48.834  68.454  55.801  1.00 60.77  ? 49  GLU   E O     1 
ATOM   10493 C  CB    . GLU   D 3  47  ? 50.451  69.037  58.422  1.00 54.32  ? 49  GLU   E CB    1 
ATOM   10494 C  CG    . GLU   D 3  47  ? 51.494  68.254  59.195  1.00 69.99  ? 49  GLU   E CG    1 
ATOM   10495 C  CD    . GLU   D 3  47  ? 52.022  69.028  60.376  1.00 77.67  ? 49  GLU   E CD    1 
ATOM   10496 O  OE1   . GLU   D 3  47  ? 51.191  69.610  61.106  1.00 75.32  ? 49  GLU   E OE1   1 
ATOM   10497 O  OE2   . GLU   D 3  47  ? 53.264  69.068  60.558  1.00 78.32  ? 49  GLU   E OE2   1 
ATOM   10498 N  N     . ILE   D 3  48  ? 49.095  70.690  55.900  1.00 58.22  ? 50  ILE   E N     1 
ATOM   10499 C  CA    . ILE   D 3  48  ? 47.902  70.938  55.097  1.00 50.46  ? 50  ILE   E CA    1 
ATOM   10500 C  C     . ILE   D 3  48  ? 48.144  70.492  53.665  1.00 51.69  ? 50  ILE   E C     1 
ATOM   10501 O  O     . ILE   D 3  48  ? 47.336  69.769  53.072  1.00 47.50  ? 50  ILE   E O     1 
ATOM   10502 C  CB    . ILE   D 3  48  ? 47.495  72.422  55.177  1.00 48.86  ? 50  ILE   E CB    1 
ATOM   10503 C  CG1   . ILE   D 3  48  ? 46.898  72.743  56.542  1.00 44.47  ? 50  ILE   E CG1   1 
ATOM   10504 C  CG2   . ILE   D 3  48  ? 46.481  72.805  54.096  1.00 47.83  ? 50  ILE   E CG2   1 
ATOM   10505 C  CD1   . ILE   D 3  48  ? 46.223  74.053  56.563  1.00 42.08  ? 50  ILE   E CD1   1 
ATOM   10506 N  N     . GLN   D 3  49  ? 49.286  70.881  53.104  1.00 58.94  ? 51  GLN   E N     1 
ATOM   10507 C  CA    . GLN   D 3  49  ? 49.599  70.490  51.740  1.00 53.30  ? 51  GLN   E CA    1 
ATOM   10508 C  C     . GLN   D 3  49  ? 49.884  68.994  51.638  1.00 52.82  ? 51  GLN   E C     1 
ATOM   10509 O  O     . GLN   D 3  49  ? 49.509  68.354  50.653  1.00 45.41  ? 51  GLN   E O     1 
ATOM   10510 C  CB    . GLN   D 3  49  ? 50.766  71.322  51.232  1.00 49.67  ? 51  GLN   E CB    1 
ATOM   10511 C  CG    . GLN   D 3  49  ? 50.299  72.483  50.376  1.00 67.32  ? 51  GLN   E CG    1 
ATOM   10512 C  CD    . GLN   D 3  49  ? 49.217  72.058  49.381  1.00 78.45  ? 51  GLN   E CD    1 
ATOM   10513 O  OE1   . GLN   D 3  49  ? 48.982  70.856  49.155  1.00 60.60  ? 51  GLN   E OE1   1 
ATOM   10514 N  NE2   . GLN   D 3  49  ? 48.550  73.045  48.785  1.00 81.90  ? 51  GLN   E NE2   1 
ATOM   10515 N  N     . LYS   D 3  50  ? 50.534  68.416  52.650  1.00 57.65  ? 52  LYS   E N     1 
ATOM   10516 C  CA    . LYS   D 3  50  ? 50.706  66.967  52.699  1.00 56.34  ? 52  LYS   E CA    1 
ATOM   10517 C  C     . LYS   D 3  50  ? 49.377  66.223  52.626  1.00 53.73  ? 52  LYS   E C     1 
ATOM   10518 O  O     . LYS   D 3  50  ? 49.372  65.018  52.371  1.00 52.95  ? 52  LYS   E O     1 
ATOM   10519 C  CB    . LYS   D 3  50  ? 51.438  66.561  53.987  1.00 52.32  ? 52  LYS   E CB    1 
ATOM   10520 C  CG    . LYS   D 3  50  ? 52.520  65.482  53.830  1.00 52.80  ? 52  LYS   E CG    1 
ATOM   10521 C  CD    . LYS   D 3  50  ? 53.893  66.114  53.531  1.00 61.78  ? 52  LYS   E CD    1 
ATOM   10522 C  CE    . LYS   D 3  50  ? 55.038  65.127  53.728  1.00 47.76  ? 52  LYS   E CE    1 
ATOM   10523 N  NZ    . LYS   D 3  50  ? 55.043  64.041  52.698  1.00 54.96  ? 52  LYS   E NZ    1 
ATOM   10524 N  N     . LYS   D 3  51  ? 48.256  66.895  52.876  1.00 56.62  ? 53  LYS   E N     1 
ATOM   10525 C  CA    . LYS   D 3  51  ? 46.964  66.228  52.990  1.00 51.66  ? 53  LYS   E CA    1 
ATOM   10526 C  C     . LYS   D 3  51  ? 46.091  66.464  51.770  1.00 45.38  ? 53  LYS   E C     1 
ATOM   10527 O  O     . LYS   D 3  51  ? 45.420  65.536  51.305  1.00 41.98  ? 53  LYS   E O     1 
ATOM   10528 C  CB    . LYS   D 3  51  ? 46.248  66.687  54.276  1.00 42.91  ? 53  LYS   E CB    1 
ATOM   10529 C  CG    . LYS   D 3  51  ? 44.716  66.798  54.207  1.00 47.71  ? 53  LYS   E CG    1 
ATOM   10530 C  CD    . LYS   D 3  51  ? 44.177  67.774  55.277  1.00 52.06  ? 53  LYS   E CD    1 
ATOM   10531 C  CE    . LYS   D 3  51  ? 42.660  67.938  55.243  1.00 37.84  ? 53  LYS   E CE    1 
ATOM   10532 N  NZ    . LYS   D 3  51  ? 42.096  68.209  56.587  1.00 35.54  ? 53  LYS   E NZ    1 
ATOM   10533 N  N     . LEU   D 3  52  ? 46.103  67.681  51.227  1.00 37.21  ? 54  LEU   E N     1 
ATOM   10534 C  CA    . LEU   D 3  52  ? 45.449  67.907  49.949  1.00 39.54  ? 54  LEU   E CA    1 
ATOM   10535 C  C     . LEU   D 3  52  ? 46.055  67.024  48.858  1.00 54.64  ? 54  LEU   E C     1 
ATOM   10536 O  O     . LEU   D 3  52  ? 45.336  66.500  47.994  1.00 57.33  ? 54  LEU   E O     1 
ATOM   10537 C  CB    . LEU   D 3  52  ? 45.543  69.381  49.557  1.00 38.42  ? 54  LEU   E CB    1 
ATOM   10538 C  CG    . LEU   D 3  52  ? 44.876  70.434  50.436  1.00 36.29  ? 54  LEU   E CG    1 
ATOM   10539 C  CD1   . LEU   D 3  52  ? 45.930  71.162  51.213  1.00 42.15  ? 54  LEU   E CD1   1 
ATOM   10540 C  CD2   . LEU   D 3  52  ? 44.085  71.416  49.601  1.00 37.73  ? 54  LEU   E CD2   1 
ATOM   10541 N  N     . GLU   D 3  53  ? 47.375  66.828  48.891  1.00 53.84  ? 55  GLU   E N     1 
ATOM   10542 C  CA    . GLU   D 3  53  ? 48.043  66.167  47.774  1.00 51.02  ? 55  GLU   E CA    1 
ATOM   10543 C  C     . GLU   D 3  53  ? 47.861  64.660  47.830  1.00 50.83  ? 55  GLU   E C     1 
ATOM   10544 O  O     . GLU   D 3  53  ? 47.684  64.011  46.791  1.00 52.38  ? 55  GLU   E O     1 
ATOM   10545 C  CB    . GLU   D 3  53  ? 49.523  66.536  47.755  1.00 58.97  ? 55  GLU   E CB    1 
ATOM   10546 C  CG    . GLU   D 3  53  ? 49.773  67.940  47.238  1.00 56.80  ? 55  GLU   E CG    1 
ATOM   10547 C  CD    . GLU   D 3  53  ? 51.201  68.374  47.416  1.00 62.58  ? 55  GLU   E CD    1 
ATOM   10548 O  OE1   . GLU   D 3  53  ? 51.995  67.579  47.972  1.00 69.52  ? 55  GLU   E OE1   1 
ATOM   10549 O  OE2   . GLU   D 3  53  ? 51.524  69.510  47.000  1.00 68.83  ? 55  GLU   E OE2   1 
ATOM   10550 N  N     . ALA   D 3  54  ? 47.906  64.087  49.031  1.00 44.18  ? 56  ALA   E N     1 
ATOM   10551 C  CA    . ALA   D 3  54  ? 47.510  62.697  49.203  1.00 48.26  ? 56  ALA   E CA    1 
ATOM   10552 C  C     . ALA   D 3  54  ? 46.140  62.405  48.586  1.00 55.40  ? 56  ALA   E C     1 
ATOM   10553 O  O     . ALA   D 3  54  ? 45.844  61.251  48.248  1.00 51.24  ? 56  ALA   E O     1 
ATOM   10554 C  CB    . ALA   D 3  54  ? 47.511  62.358  50.693  1.00 43.36  ? 56  ALA   E CB    1 
ATOM   10555 N  N     . ALA   D 3  55  ? 45.305  63.431  48.421  1.00 54.57  ? 57  ALA   E N     1 
ATOM   10556 C  CA    . ALA   D 3  55  ? 43.977  63.280  47.851  1.00 50.76  ? 57  ALA   E CA    1 
ATOM   10557 C  C     . ALA   D 3  55  ? 43.978  63.360  46.326  1.00 46.43  ? 57  ALA   E C     1 
ATOM   10558 O  O     . ALA   D 3  55  ? 43.223  62.630  45.675  1.00 50.61  ? 57  ALA   E O     1 
ATOM   10559 C  CB    . ALA   D 3  55  ? 43.038  64.333  48.442  1.00 43.61  ? 57  ALA   E CB    1 
ATOM   10560 N  N     . GLU   D 3  56  ? 44.790  64.225  45.716  1.00 47.36  ? 58  GLU   E N     1 
ATOM   10561 C  CA    . GLU   D 3  56  ? 44.851  64.178  44.256  1.00 51.66  ? 58  GLU   E CA    1 
ATOM   10562 C  C     . GLU   D 3  56  ? 45.642  62.970  43.782  1.00 48.62  ? 58  GLU   E C     1 
ATOM   10563 O  O     . GLU   D 3  56  ? 45.388  62.451  42.692  1.00 42.69  ? 58  GLU   E O     1 
ATOM   10564 C  CB    . GLU   D 3  56  ? 45.456  65.450  43.681  1.00 41.57  ? 58  GLU   E CB    1 
ATOM   10565 C  CG    . GLU   D 3  56  ? 46.888  65.311  43.327  1.00 46.16  ? 58  GLU   E CG    1 
ATOM   10566 C  CD    . GLU   D 3  56  ? 47.575  66.650  43.366  1.00 65.05  ? 58  GLU   E CD    1 
ATOM   10567 O  OE1   . GLU   D 3  56  ? 48.729  66.725  43.855  1.00 63.80  ? 58  GLU   E OE1   1 
ATOM   10568 O  OE2   . GLU   D 3  56  ? 46.913  67.639  42.945  1.00 66.72  ? 58  GLU   E OE2   1 
ATOM   10569 N  N     . GLU   D 3  57  ? 46.610  62.518  44.575  1.00 52.51  ? 59  GLU   E N     1 
ATOM   10570 C  CA    . GLU   D 3  57  ? 47.294  61.278  44.240  1.00 54.86  ? 59  GLU   E CA    1 
ATOM   10571 C  C     . GLU   D 3  57  ? 46.311  60.102  44.226  1.00 52.35  ? 59  GLU   E C     1 
ATOM   10572 O  O     . GLU   D 3  57  ? 46.373  59.254  43.329  1.00 57.76  ? 59  GLU   E O     1 
ATOM   10573 C  CB    . GLU   D 3  57  ? 48.472  61.050  45.205  1.00 56.87  ? 59  GLU   E CB    1 
ATOM   10574 C  CG    . GLU   D 3  57  ? 49.717  61.962  44.927  1.00 61.63  ? 59  GLU   E CG    1 
ATOM   10575 C  CD    . GLU   D 3  57  ? 50.749  62.059  46.102  1.00 76.67  ? 59  GLU   E CD    1 
ATOM   10576 O  OE1   . GLU   D 3  57  ? 50.995  61.055  46.821  1.00 64.03  ? 59  GLU   E OE1   1 
ATOM   10577 O  OE2   . GLU   D 3  57  ? 51.330  63.157  46.299  1.00 69.63  ? 59  GLU   E OE2   1 
ATOM   10578 N  N     . ARG   D 3  58  ? 45.374  60.044  45.183  1.00 47.53  ? 60  ARG   E N     1 
ATOM   10579 C  CA    . ARG   D 3  58  ? 44.345  59.001  45.141  1.00 45.47  ? 60  ARG   E CA    1 
ATOM   10580 C  C     . ARG   D 3  58  ? 43.358  59.249  43.998  1.00 43.54  ? 60  ARG   E C     1 
ATOM   10581 O  O     . ARG   D 3  58  ? 43.029  58.341  43.223  1.00 36.49  ? 60  ARG   E O     1 
ATOM   10582 C  CB    . ARG   D 3  58  ? 43.613  58.930  46.486  1.00 40.09  ? 60  ARG   E CB    1 
ATOM   10583 C  CG    . ARG   D 3  58  ? 44.342  58.101  47.554  1.00 47.50  ? 60  ARG   E CG    1 
ATOM   10584 C  CD    . ARG   D 3  58  ? 43.533  57.921  48.862  1.00 51.76  ? 60  ARG   E CD    1 
ATOM   10585 N  NE    . ARG   D 3  58  ? 43.206  59.200  49.483  1.00 53.64  ? 60  ARG   E NE    1 
ATOM   10586 C  CZ    . ARG   D 3  58  ? 44.027  59.890  50.261  1.00 49.29  ? 60  ARG   E CZ    1 
ATOM   10587 N  NH1   . ARG   D 3  58  ? 45.202  59.409  50.620  1.00 49.24  ? 60  ARG   E NH1   1 
ATOM   10588 N  NH2   . ARG   D 3  58  ? 43.670  61.102  50.667  1.00 48.51  ? 60  ARG   E NH2   1 
ATOM   10589 N  N     . ARG   D 3  59  ? 42.889  60.488  43.874  1.00 46.75  ? 61  ARG   E N     1 
ATOM   10590 C  CA    . ARG   D 3  59  ? 41.981  60.854  42.796  1.00 39.87  ? 61  ARG   E CA    1 
ATOM   10591 C  C     . ARG   D 3  59  ? 42.598  60.579  41.421  1.00 42.23  ? 61  ARG   E C     1 
ATOM   10592 O  O     . ARG   D 3  59  ? 41.908  60.104  40.509  1.00 41.85  ? 61  ARG   E O     1 
ATOM   10593 C  CB    . ARG   D 3  59  ? 41.597  62.326  42.973  1.00 36.36  ? 61  ARG   E CB    1 
ATOM   10594 C  CG    . ARG   D 3  59  ? 40.620  62.873  41.984  1.00 38.92  ? 61  ARG   E CG    1 
ATOM   10595 C  CD    . ARG   D 3  59  ? 40.490  64.391  42.088  1.00 40.38  ? 61  ARG   E CD    1 
ATOM   10596 N  NE    . ARG   D 3  59  ? 40.575  64.846  43.469  1.00 49.15  ? 61  ARG   E NE    1 
ATOM   10597 C  CZ    . ARG   D 3  59  ? 41.573  65.576  43.954  1.00 53.15  ? 61  ARG   E CZ    1 
ATOM   10598 N  NH1   . ARG   D 3  59  ? 42.544  66.028  43.173  1.00 55.03  ? 61  ARG   E NH1   1 
ATOM   10599 N  NH2   . ARG   D 3  59  ? 41.600  65.859  45.254  1.00 46.88  ? 61  ARG   E NH2   1 
ATOM   10600 N  N     . LYS   D 3  60  ? 43.893  60.873  41.243  1.00 46.28  ? 62  LYS   E N     1 
ATOM   10601 C  CA    . LYS   D 3  60  ? 44.507  60.633  39.938  1.00 38.28  ? 62  LYS   E CA    1 
ATOM   10602 C  C     . LYS   D 3  60  ? 44.818  59.157  39.734  1.00 39.75  ? 62  LYS   E C     1 
ATOM   10603 O  O     . LYS   D 3  60  ? 44.821  58.679  38.595  1.00 44.75  ? 62  LYS   E O     1 
ATOM   10604 C  CB    . LYS   D 3  60  ? 45.784  61.474  39.745  1.00 35.35  ? 62  LYS   E CB    1 
ATOM   10605 C  CG    . LYS   D 3  60  ? 45.584  63.009  39.851  1.00 41.72  ? 62  LYS   E CG    1 
ATOM   10606 C  CD    . LYS   D 3  60  ? 46.503  63.845  38.937  1.00 35.00  ? 62  LYS   E CD    1 
ATOM   10607 C  CE    . LYS   D 3  60  ? 47.982  63.484  39.035  1.00 33.96  ? 62  LYS   E CE    1 
ATOM   10608 N  NZ    . LYS   D 3  60  ? 48.647  63.793  40.345  1.00 42.30  ? 62  LYS   E NZ    1 
ATOM   10609 N  N     . TYR   D 3  61  ? 45.079  58.416  40.807  1.00 31.20  ? 63  TYR   E N     1 
ATOM   10610 C  CA    . TYR   D 3  61  ? 45.275  56.982  40.664  1.00 33.23  ? 63  TYR   E CA    1 
ATOM   10611 C  C     . TYR   D 3  61  ? 43.987  56.316  40.215  1.00 36.16  ? 63  TYR   E C     1 
ATOM   10612 O  O     . TYR   D 3  61  ? 43.983  55.490  39.295  1.00 39.19  ? 63  TYR   E O     1 
ATOM   10613 C  CB    . TYR   D 3  61  ? 45.762  56.394  41.985  1.00 33.88  ? 63  TYR   E CB    1 
ATOM   10614 C  CG    . TYR   D 3  61  ? 45.859  54.887  42.030  1.00 30.07  ? 63  TYR   E CG    1 
ATOM   10615 C  CD1   . TYR   D 3  61  ? 46.960  54.229  41.501  1.00 48.72  ? 63  TYR   E CD1   1 
ATOM   10616 C  CD2   . TYR   D 3  61  ? 44.863  54.119  42.609  1.00 48.53  ? 63  TYR   E CD2   1 
ATOM   10617 C  CE1   . TYR   D 3  61  ? 47.062  52.835  41.540  1.00 51.90  ? 63  TYR   E CE1   1 
ATOM   10618 C  CE2   . TYR   D 3  61  ? 44.958  52.734  42.658  1.00 48.58  ? 63  TYR   E CE2   1 
ATOM   10619 C  CZ    . TYR   D 3  61  ? 46.061  52.093  42.120  1.00 45.14  ? 63  TYR   E CZ    1 
ATOM   10620 O  OH    . TYR   D 3  61  ? 46.168  50.714  42.165  1.00 37.49  ? 63  TYR   E OH    1 
ATOM   10621 N  N     . GLN   D 3  62  ? 42.873  56.688  40.835  1.00 39.58  ? 64  GLN   E N     1 
ATOM   10622 C  CA    . GLN   D 3  62  ? 41.599  56.100  40.448  1.00 39.95  ? 64  GLN   E CA    1 
ATOM   10623 C  C     . GLN   D 3  62  ? 41.326  56.312  38.966  1.00 33.54  ? 64  GLN   E C     1 
ATOM   10624 O  O     . GLN   D 3  62  ? 40.858  55.406  38.270  1.00 33.08  ? 64  GLN   E O     1 
ATOM   10625 C  CB    . GLN   D 3  62  ? 40.482  56.688  41.309  1.00 27.35  ? 64  GLN   E CB    1 
ATOM   10626 C  CG    . GLN   D 3  62  ? 40.434  56.044  42.678  1.00 51.55  ? 64  GLN   E CG    1 
ATOM   10627 C  CD    . GLN   D 3  62  ? 40.158  57.040  43.766  1.00 55.89  ? 64  GLN   E CD    1 
ATOM   10628 O  OE1   . GLN   D 3  62  ? 39.428  58.020  43.551  1.00 50.91  ? 64  GLN   E OE1   1 
ATOM   10629 N  NE2   . GLN   D 3  62  ? 40.756  56.816  44.946  1.00 41.64  ? 64  GLN   E NE2   1 
ATOM   10630 N  N     . GLU   D 3  63  ? 41.619  57.498  38.461  1.00 24.70  ? 65  GLU   E N     1 
ATOM   10631 C  CA    . GLU   D 3  63  ? 41.324  57.754  37.069  1.00 27.36  ? 65  GLU   E CA    1 
ATOM   10632 C  C     . GLU   D 3  63  ? 42.253  56.957  36.175  1.00 38.86  ? 65  GLU   E C     1 
ATOM   10633 O  O     . GLU   D 3  63  ? 41.841  56.462  35.118  1.00 37.67  ? 65  GLU   E O     1 
ATOM   10634 C  CB    . GLU   D 3  63  ? 41.446  59.238  36.786  1.00 32.49  ? 65  GLU   E CB    1 
ATOM   10635 C  CG    . GLU   D 3  63  ? 40.472  59.689  35.769  1.00 31.51  ? 65  GLU   E CG    1 
ATOM   10636 C  CD    . GLU   D 3  63  ? 40.751  61.088  35.327  1.00 39.50  ? 65  GLU   E CD    1 
ATOM   10637 O  OE1   . GLU   D 3  63  ? 41.933  61.347  34.976  1.00 33.60  ? 65  GLU   E OE1   1 
ATOM   10638 O  OE2   . GLU   D 3  63  ? 39.787  61.907  35.344  1.00 39.90  ? 65  GLU   E OE2   1 
ATOM   10639 N  N     . ALA   D 3  64  ? 43.516  56.831  36.585  1.00 43.88  ? 66  ALA   E N     1 
ATOM   10640 C  CA    . ALA   D 3  64  ? 44.449  55.957  35.894  1.00 40.94  ? 66  ALA   E CA    1 
ATOM   10641 C  C     . ALA   D 3  64  ? 43.854  54.561  35.721  1.00 34.57  ? 66  ALA   E C     1 
ATOM   10642 O  O     . ALA   D 3  64  ? 43.625  54.100  34.596  1.00 39.20  ? 66  ALA   E O     1 
ATOM   10643 C  CB    . ALA   D 3  64  ? 45.769  55.922  36.661  1.00 36.44  ? 66  ALA   E CB    1 
ATOM   10644 N  N     . GLU   D 3  65  ? 43.567  53.881  36.829  1.00 32.79  ? 67  GLU   E N     1 
ATOM   10645 C  CA    . GLU   D 3  65  ? 42.963  52.554  36.725  1.00 39.89  ? 67  GLU   E CA    1 
ATOM   10646 C  C     . GLU   D 3  65  ? 41.738  52.543  35.812  1.00 46.06  ? 67  GLU   E C     1 
ATOM   10647 O  O     . GLU   D 3  65  ? 41.484  51.539  35.132  1.00 47.35  ? 67  GLU   E O     1 
ATOM   10648 C  CB    . GLU   D 3  65  ? 42.584  52.029  38.107  1.00 28.67  ? 67  GLU   E CB    1 
ATOM   10649 C  CG    . GLU   D 3  65  ? 43.152  50.650  38.402  1.00 39.73  ? 67  GLU   E CG    1 
ATOM   10650 C  CD    . GLU   D 3  65  ? 44.633  50.687  38.711  1.00 53.61  ? 67  GLU   E CD    1 
ATOM   10651 O  OE1   . GLU   D 3  65  ? 45.422  51.181  37.870  1.00 63.39  ? 67  GLU   E OE1   1 
ATOM   10652 O  OE2   . GLU   D 3  65  ? 45.011  50.234  39.814  1.00 53.95  ? 67  GLU   E OE2   1 
ATOM   10653 N  N     . LEU   D 3  66  ? 40.974  53.642  35.775  1.00 38.85  ? 68  LEU   E N     1 
ATOM   10654 C  CA    . LEU   D 3  66  ? 39.776  53.690  34.943  1.00 33.50  ? 68  LEU   E CA    1 
ATOM   10655 C  C     . LEU   D 3  66  ? 40.140  53.794  33.468  1.00 35.85  ? 68  LEU   E C     1 
ATOM   10656 O  O     . LEU   D 3  66  ? 39.685  52.993  32.647  1.00 39.13  ? 68  LEU   E O     1 
ATOM   10657 C  CB    . LEU   D 3  66  ? 38.882  54.863  35.349  1.00 34.35  ? 68  LEU   E CB    1 
ATOM   10658 C  CG    . LEU   D 3  66  ? 37.895  55.175  34.220  1.00 35.80  ? 68  LEU   E CG    1 
ATOM   10659 C  CD1   . LEU   D 3  66  ? 36.903  54.037  34.102  1.00 33.63  ? 68  LEU   E CD1   1 
ATOM   10660 C  CD2   . LEU   D 3  66  ? 37.191  56.508  34.364  1.00 30.19  ? 68  LEU   E CD2   1 
ATOM   10661 N  N     . LEU   D 3  67  ? 40.946  54.791  33.104  1.00 34.97  ? 69  LEU   E N     1 
ATOM   10662 C  CA    . LEU   D 3  67  ? 41.477  54.822  31.748  1.00 35.00  ? 69  LEU   E CA    1 
ATOM   10663 C  C     . LEU   D 3  67  ? 42.146  53.507  31.388  1.00 37.35  ? 69  LEU   E C     1 
ATOM   10664 O  O     . LEU   D 3  67  ? 42.120  53.104  30.222  1.00 41.42  ? 69  LEU   E O     1 
ATOM   10665 C  CB    . LEU   D 3  67  ? 42.466  55.973  31.579  1.00 18.75  ? 69  LEU   E CB    1 
ATOM   10666 C  CG    . LEU   D 3  67  ? 41.717  57.298  31.646  1.00 29.17  ? 69  LEU   E CG    1 
ATOM   10667 C  CD1   . LEU   D 3  67  ? 42.649  58.466  31.573  1.00 24.03  ? 69  LEU   E CD1   1 
ATOM   10668 C  CD2   . LEU   D 3  67  ? 40.669  57.396  30.546  1.00 30.76  ? 69  LEU   E CD2   1 
ATOM   10669 N  N     . LYS   D 3  68  ? 42.754  52.829  32.364  1.00 34.61  ? 70  LYS   E N     1 
ATOM   10670 C  CA    . LYS   D 3  68  ? 43.469  51.588  32.079  1.00 40.18  ? 70  LYS   E CA    1 
ATOM   10671 C  C     . LYS   D 3  68  ? 42.502  50.491  31.655  1.00 45.98  ? 70  LYS   E C     1 
ATOM   10672 O  O     . LYS   D 3  68  ? 42.710  49.817  30.638  1.00 43.10  ? 70  LYS   E O     1 
ATOM   10673 C  CB    . LYS   D 3  68  ? 44.271  51.154  33.307  1.00 43.38  ? 70  LYS   E CB    1 
ATOM   10674 C  CG    . LYS   D 3  68  ? 45.028  49.846  33.144  1.00 44.34  ? 70  LYS   E CG    1 
ATOM   10675 C  CD    . LYS   D 3  68  ? 45.306  49.190  34.490  1.00 57.55  ? 70  LYS   E CD    1 
ATOM   10676 C  CE    . LYS   D 3  68  ? 45.910  47.796  34.321  1.00 58.13  ? 70  LYS   E CE    1 
ATOM   10677 N  NZ    . LYS   D 3  68  ? 47.391  47.800  34.118  1.00 48.42  ? 70  LYS   E NZ    1 
ATOM   10678 N  N     . HIS   D 3  69  ? 41.446  50.283  32.441  1.00 51.78  ? 71  HIS   E N     1 
ATOM   10679 C  CA    . HIS   D 3  69  ? 40.327  49.448  32.021  1.00 43.75  ? 71  HIS   E CA    1 
ATOM   10680 C  C     . HIS   D 3  69  ? 39.879  49.800  30.599  1.00 33.79  ? 71  HIS   E C     1 
ATOM   10681 O  O     . HIS   D 3  69  ? 39.993  48.990  29.675  1.00 34.68  ? 71  HIS   E O     1 
ATOM   10682 C  CB    . HIS   D 3  69  ? 39.189  49.631  33.033  1.00 47.01  ? 71  HIS   E CB    1 
ATOM   10683 C  CG    . HIS   D 3  69  ? 38.273  48.453  33.164  1.00 61.03  ? 71  HIS   E CG    1 
ATOM   10684 N  ND1   . HIS   D 3  69  ? 37.047  48.385  32.531  1.00 65.84  ? 71  HIS   E ND1   1 
ATOM   10685 C  CD2   . HIS   D 3  69  ? 38.386  47.314  33.888  1.00 62.43  ? 71  HIS   E CD2   1 
ATOM   10686 C  CE1   . HIS   D 3  69  ? 36.451  47.250  32.849  1.00 67.77  ? 71  HIS   E CE1   1 
ATOM   10687 N  NE2   . HIS   D 3  69  ? 37.244  46.579  33.666  1.00 76.08  ? 71  HIS   E NE2   1 
ATOM   10688 N  N     . LEU   D 3  70  ? 39.397  51.031  30.408  1.00 30.07  ? 72  LEU   E N     1 
ATOM   10689 C  CA    . LEU   D 3  70  ? 38.924  51.481  29.101  1.00 32.63  ? 72  LEU   E CA    1 
ATOM   10690 C  C     . LEU   D 3  70  ? 39.930  51.262  27.976  1.00 34.04  ? 72  LEU   E C     1 
ATOM   10691 O  O     . LEU   D 3  70  ? 39.529  51.183  26.815  1.00 35.48  ? 72  LEU   E O     1 
ATOM   10692 C  CB    . LEU   D 3  70  ? 38.568  52.969  29.139  1.00 31.81  ? 72  LEU   E CB    1 
ATOM   10693 C  CG    . LEU   D 3  70  ? 37.368  53.388  29.961  1.00 31.11  ? 72  LEU   E CG    1 
ATOM   10694 C  CD1   . LEU   D 3  70  ? 37.120  54.861  29.715  1.00 34.05  ? 72  LEU   E CD1   1 
ATOM   10695 C  CD2   . LEU   D 3  70  ? 36.157  52.547  29.584  1.00 26.89  ? 72  LEU   E CD2   1 
ATOM   10696 N  N     . ALA   D 3  71  ? 41.225  51.216  28.265  1.00 36.96  ? 73  ALA   E N     1 
ATOM   10697 C  CA    . ALA   D 3  71  ? 42.160  50.962  27.181  1.00 30.42  ? 73  ALA   E CA    1 
ATOM   10698 C  C     . ALA   D 3  71  ? 42.305  49.472  26.914  1.00 34.50  ? 73  ALA   E C     1 
ATOM   10699 O  O     . ALA   D 3  71  ? 42.602  49.073  25.782  1.00 34.87  ? 73  ALA   E O     1 
ATOM   10700 C  CB    . ALA   D 3  71  ? 43.508  51.596  27.486  1.00 22.31  ? 73  ALA   E CB    1 
ATOM   10701 N  N     . GLU   D 3  72  ? 42.089  48.638  27.929  1.00 34.26  ? 74  GLU   E N     1 
ATOM   10702 C  CA    . GLU   D 3  72  ? 41.845  47.228  27.666  1.00 28.65  ? 74  GLU   E CA    1 
ATOM   10703 C  C     . GLU   D 3  72  ? 40.655  47.055  26.721  1.00 35.01  ? 74  GLU   E C     1 
ATOM   10704 O  O     . GLU   D 3  72  ? 40.731  46.302  25.744  1.00 35.57  ? 74  GLU   E O     1 
ATOM   10705 C  CB    . GLU   D 3  72  ? 41.616  46.484  28.982  1.00 31.14  ? 74  GLU   E CB    1 
ATOM   10706 C  CG    . GLU   D 3  72  ? 42.839  46.405  29.882  1.00 38.88  ? 74  GLU   E CG    1 
ATOM   10707 C  CD    . GLU   D 3  72  ? 42.547  45.760  31.244  1.00 46.36  ? 74  GLU   E CD    1 
ATOM   10708 O  OE1   . GLU   D 3  72  ? 41.364  45.498  31.543  1.00 43.76  ? 74  GLU   E OE1   1 
ATOM   10709 O  OE2   . GLU   D 3  72  ? 43.505  45.515  32.019  1.00 51.15  ? 74  GLU   E OE2   1 
ATOM   10710 N  N     . LYS   D 3  73  ? 39.543  47.754  26.995  1.00 38.36  ? 75  LYS   E N     1 
ATOM   10711 C  CA    . LYS   D 3  73  ? 38.339  47.629  26.166  1.00 34.67  ? 75  LYS   E CA    1 
ATOM   10712 C  C     . LYS   D 3  73  ? 38.644  47.897  24.696  1.00 35.41  ? 75  LYS   E C     1 
ATOM   10713 O  O     . LYS   D 3  73  ? 38.125  47.206  23.811  1.00 29.68  ? 75  LYS   E O     1 
ATOM   10714 C  CB    . LYS   D 3  73  ? 37.241  48.585  26.660  1.00 22.55  ? 75  LYS   E CB    1 
ATOM   10715 C  CG    . LYS   D 3  73  ? 36.068  47.901  27.335  1.00 38.89  ? 75  LYS   E CG    1 
ATOM   10716 C  CD    . LYS   D 3  73  ? 36.516  46.782  28.303  1.00 35.44  ? 75  LYS   E CD    1 
ATOM   10717 C  CE    . LYS   D 3  73  ? 35.378  46.292  29.231  1.00 44.24  ? 75  LYS   E CE    1 
ATOM   10718 N  NZ    . LYS   D 3  73  ? 34.160  45.674  28.558  1.00 43.39  ? 75  LYS   E NZ    1 
ATOM   10719 N  N     . ARG   D 3  74  ? 39.478  48.909  24.420  1.00 31.31  ? 76  ARG   E N     1 
ATOM   10720 C  CA    . ARG   D 3  74  ? 39.910  49.183  23.054  1.00 30.30  ? 76  ARG   E CA    1 
ATOM   10721 C  C     . ARG   D 3  74  ? 40.689  48.009  22.476  1.00 35.35  ? 76  ARG   E C     1 
ATOM   10722 O  O     . ARG   D 3  74  ? 40.623  47.738  21.275  1.00 35.67  ? 76  ARG   E O     1 
ATOM   10723 C  CB    . ARG   D 3  74  ? 40.782  50.434  23.022  1.00 40.06  ? 76  ARG   E CB    1 
ATOM   10724 C  CG    . ARG   D 3  74  ? 40.247  51.618  23.795  1.00 41.26  ? 76  ARG   E CG    1 
ATOM   10725 C  CD    . ARG   D 3  74  ? 39.220  52.408  22.989  1.00 39.05  ? 76  ARG   E CD    1 
ATOM   10726 N  NE    . ARG   D 3  74  ? 38.220  52.975  23.885  1.00 40.07  ? 76  ARG   E NE    1 
ATOM   10727 C  CZ    . ARG   D 3  74  ? 37.041  52.426  24.132  1.00 37.07  ? 76  ARG   E CZ    1 
ATOM   10728 N  NH1   . ARG   D 3  74  ? 36.634  51.345  23.493  1.00 36.96  ? 76  ARG   E NH1   1 
ATOM   10729 N  NH2   . ARG   D 3  74  ? 36.250  52.977  25.045  1.00 41.16  ? 76  ARG   E NH2   1 
ATOM   10730 N  N     . GLU   D 3  75  ? 41.458  47.320  23.317  1.00 39.45  ? 77  GLU   E N     1 
ATOM   10731 C  CA    . GLU   D 3  75  ? 42.298  46.228  22.850  1.00 33.98  ? 77  GLU   E CA    1 
ATOM   10732 C  C     . GLU   D 3  75  ? 41.449  45.035  22.441  1.00 34.28  ? 77  GLU   E C     1 
ATOM   10733 O  O     . GLU   D 3  75  ? 41.673  44.425  21.390  1.00 41.62  ? 77  GLU   E O     1 
ATOM   10734 C  CB    . GLU   D 3  75  ? 43.282  45.864  23.957  1.00 35.66  ? 77  GLU   E CB    1 
ATOM   10735 C  CG    . GLU   D 3  75  ? 44.224  44.744  23.646  1.00 44.85  ? 77  GLU   E CG    1 
ATOM   10736 C  CD    . GLU   D 3  75  ? 45.270  44.562  24.728  1.00 51.88  ? 77  GLU   E CD    1 
ATOM   10737 O  OE1   . GLU   D 3  75  ? 45.410  45.472  25.582  1.00 50.86  ? 77  GLU   E OE1   1 
ATOM   10738 O  OE2   . GLU   D 3  75  ? 45.944  43.506  24.720  1.00 54.76  ? 77  GLU   E OE2   1 
ATOM   10739 N  N     . HIS   D 3  76  ? 40.451  44.711  23.252  1.00 34.24  ? 78  HIS   E N     1 
ATOM   10740 C  CA    . HIS   D 3  76  ? 39.515  43.648  22.921  1.00 27.12  ? 78  HIS   E CA    1 
ATOM   10741 C  C     . HIS   D 3  76  ? 38.671  43.993  21.696  1.00 32.47  ? 78  HIS   E C     1 
ATOM   10742 O  O     . HIS   D 3  76  ? 38.319  43.106  20.916  1.00 32.04  ? 78  HIS   E O     1 
ATOM   10743 C  CB    . HIS   D 3  76  ? 38.624  43.390  24.120  1.00 18.56  ? 78  HIS   E CB    1 
ATOM   10744 C  CG    . HIS   D 3  76  ? 37.470  42.499  23.826  1.00 27.29  ? 78  HIS   E CG    1 
ATOM   10745 N  ND1   . HIS   D 3  76  ? 37.595  41.131  23.736  1.00 27.68  ? 78  HIS   E ND1   1 
ATOM   10746 C  CD2   . HIS   D 3  76  ? 36.165  42.775  23.601  1.00 28.52  ? 78  HIS   E CD2   1 
ATOM   10747 C  CE1   . HIS   D 3  76  ? 36.414  40.602  23.472  1.00 25.37  ? 78  HIS   E CE1   1 
ATOM   10748 N  NE2   . HIS   D 3  76  ? 35.531  41.578  23.380  1.00 23.54  ? 78  HIS   E NE2   1 
ATOM   10749 N  N     . GLU   D 3  77  ? 38.303  45.268  21.531  1.00 30.55  ? 79  GLU   E N     1 
ATOM   10750 C  CA    . GLU   D 3  77  ? 37.520  45.684  20.370  1.00 24.41  ? 79  GLU   E CA    1 
ATOM   10751 C  C     . GLU   D 3  77  ? 38.261  45.412  19.070  1.00 28.00  ? 79  GLU   E C     1 
ATOM   10752 O  O     . GLU   D 3  77  ? 37.649  45.016  18.068  1.00 24.61  ? 79  GLU   E O     1 
ATOM   10753 C  CB    . GLU   D 3  77  ? 37.185  47.170  20.467  1.00 25.72  ? 79  GLU   E CB    1 
ATOM   10754 C  CG    . GLU   D 3  77  ? 36.350  47.519  21.679  1.00 30.19  ? 79  GLU   E CG    1 
ATOM   10755 C  CD    . GLU   D 3  77  ? 36.175  49.010  21.889  1.00 31.08  ? 79  GLU   E CD    1 
ATOM   10756 O  OE1   . GLU   D 3  77  ? 36.861  49.832  21.229  1.00 32.32  ? 79  GLU   E OE1   1 
ATOM   10757 O  OE2   . GLU   D 3  77  ? 35.334  49.359  22.735  1.00 38.05  ? 79  GLU   E OE2   1 
ATOM   10758 N  N     . ARG   D 3  78  ? 39.571  45.691  19.055  1.00 33.82  ? 80  ARG   E N     1 
ATOM   10759 C  CA    . ARG   D 3  78  ? 40.426  45.327  17.932  1.00 25.75  ? 80  ARG   E CA    1 
ATOM   10760 C  C     . ARG   D 3  78  ? 40.422  43.816  17.727  1.00 38.24  ? 80  ARG   E C     1 
ATOM   10761 O  O     . ARG   D 3  78  ? 40.210  43.322  16.608  1.00 33.81  ? 80  ARG   E O     1 
ATOM   10762 C  CB    . ARG   D 3  78  ? 41.855  45.821  18.187  1.00 28.85  ? 80  ARG   E CB    1 
ATOM   10763 C  CG    . ARG   D 3  78  ? 42.155  47.291  17.874  1.00 47.88  ? 80  ARG   E CG    1 
ATOM   10764 C  CD    . ARG   D 3  78  ? 43.687  47.599  17.876  1.00 48.36  ? 80  ARG   E CD    1 
ATOM   10765 N  NE    . ARG   D 3  78  ? 44.333  47.264  19.145  1.00 63.79  ? 80  ARG   E NE    1 
ATOM   10766 C  CZ    . ARG   D 3  78  ? 44.489  48.101  20.169  1.00 64.91  ? 80  ARG   E CZ    1 
ATOM   10767 N  NH1   . ARG   D 3  78  ? 44.096  49.368  20.101  1.00 56.43  ? 80  ARG   E NH1   1 
ATOM   10768 N  NH2   . ARG   D 3  78  ? 45.051  47.654  21.294  1.00 55.59  ? 80  ARG   E NH2   1 
ATOM   10769 N  N     . GLU   D 3  79  ? 40.652  43.062  18.815  1.00 30.43  ? 81  GLU   E N     1 
ATOM   10770 C  CA    . GLU   D 3  79  ? 40.739  41.609  18.722  1.00 24.39  ? 81  GLU   E CA    1 
ATOM   10771 C  C     . GLU   D 3  79  ? 39.501  40.991  18.090  1.00 31.15  ? 81  GLU   E C     1 
ATOM   10772 O  O     . GLU   D 3  79  ? 39.606  39.986  17.380  1.00 44.10  ? 81  GLU   E O     1 
ATOM   10773 C  CB    . GLU   D 3  79  ? 40.979  41.014  20.103  1.00 28.02  ? 81  GLU   E CB    1 
ATOM   10774 C  CG    . GLU   D 3  79  ? 42.414  41.209  20.579  1.00 29.43  ? 81  GLU   E CG    1 
ATOM   10775 C  CD    . GLU   D 3  79  ? 42.610  40.820  22.014  1.00 40.99  ? 81  GLU   E CD    1 
ATOM   10776 O  OE1   . GLU   D 3  79  ? 41.595  40.480  22.673  1.00 47.42  ? 81  GLU   E OE1   1 
ATOM   10777 O  OE2   . GLU   D 3  79  ? 43.773  40.870  22.485  1.00 48.81  ? 81  GLU   E OE2   1 
ATOM   10778 N  N     . VAL   D 3  80  ? 38.324  41.567  18.332  1.00 36.60  ? 82  VAL   E N     1 
ATOM   10779 C  CA    . VAL   D 3  80  ? 37.090  40.981  17.818  1.00 28.30  ? 82  VAL   E CA    1 
ATOM   10780 C  C     . VAL   D 3  80  ? 36.986  41.180  16.312  1.00 28.88  ? 82  VAL   E C     1 
ATOM   10781 O  O     . VAL   D 3  80  ? 36.706  40.230  15.574  1.00 33.29  ? 82  VAL   E O     1 
ATOM   10782 C  CB    . VAL   D 3  80  ? 35.877  41.563  18.559  1.00 27.02  ? 82  VAL   E CB    1 
ATOM   10783 C  CG1   . VAL   D 3  80  ? 34.599  41.167  17.877  1.00 24.71  ? 82  VAL   E CG1   1 
ATOM   10784 C  CG2   . VAL   D 3  80  ? 35.888  41.095  19.990  1.00 26.28  ? 82  VAL   E CG2   1 
ATOM   10785 N  N     . ILE   D 3  81  ? 37.237  42.402  15.827  1.00 25.38  ? 83  ILE   E N     1 
ATOM   10786 C  CA    . ILE   D 3  81  ? 37.123  42.657  14.393  1.00 23.03  ? 83  ILE   E CA    1 
ATOM   10787 C  C     . ILE   D 3  81  ? 38.235  41.986  13.602  1.00 30.87  ? 83  ILE   E C     1 
ATOM   10788 O  O     . ILE   D 3  81  ? 38.078  41.769  12.394  1.00 34.64  ? 83  ILE   E O     1 
ATOM   10789 C  CB    . ILE   D 3  81  ? 37.116  44.160  14.070  1.00 20.54  ? 83  ILE   E CB    1 
ATOM   10790 C  CG1   . ILE   D 3  81  ? 36.779  44.378  12.596  1.00 24.23  ? 83  ILE   E CG1   1 
ATOM   10791 C  CG2   . ILE   D 3  81  ? 38.468  44.758  14.349  1.00 27.70  ? 83  ILE   E CG2   1 
ATOM   10792 C  CD1   . ILE   D 3  81  ? 36.566  45.822  12.233  1.00 31.16  ? 83  ILE   E CD1   1 
ATOM   10793 N  N     . GLN   D 3  82  ? 39.376  41.684  14.231  1.00 30.97  ? 84  GLN   E N     1 
ATOM   10794 C  CA    . GLN   D 3  82  ? 40.398  40.928  13.522  1.00 30.90  ? 84  GLN   E CA    1 
ATOM   10795 C  C     . GLN   D 3  82  ? 40.026  39.446  13.486  1.00 36.75  ? 84  GLN   E C     1 
ATOM   10796 O  O     . GLN   D 3  82  ? 40.425  38.727  12.563  1.00 39.40  ? 84  GLN   E O     1 
ATOM   10797 C  CB    . GLN   D 3  82  ? 41.789  41.162  14.153  1.00 29.79  ? 84  GLN   E CB    1 
ATOM   10798 C  CG    . GLN   D 3  82  ? 42.430  42.579  13.910  1.00 37.97  ? 84  GLN   E CG    1 
ATOM   10799 C  CD    . GLN   D 3  82  ? 43.227  42.756  12.549  1.00 61.71  ? 84  GLN   E CD    1 
ATOM   10800 O  OE1   . GLN   D 3  82  ? 42.900  42.154  11.506  1.00 46.32  ? 84  GLN   E OE1   1 
ATOM   10801 N  NE2   . GLN   D 3  82  ? 44.270  43.603  12.583  1.00 46.71  ? 84  GLN   E NE2   1 
ATOM   10802 N  N     . LYS   D 3  83  ? 39.226  38.986  14.448  1.00 31.58  ? 85  LYS   E N     1 
ATOM   10803 C  CA    . LYS   D 3  83  ? 38.741  37.613  14.418  1.00 30.77  ? 85  LYS   E CA    1 
ATOM   10804 C  C     . LYS   D 3  83  ? 37.700  37.421  13.311  1.00 32.84  ? 85  LYS   E C     1 
ATOM   10805 O  O     . LYS   D 3  83  ? 37.810  36.503  12.491  1.00 38.21  ? 85  LYS   E O     1 
ATOM   10806 C  CB    . LYS   D 3  83  ? 38.180  37.260  15.795  1.00 31.85  ? 85  LYS   E CB    1 
ATOM   10807 C  CG    . LYS   D 3  83  ? 38.022  35.772  16.058  1.00 41.41  ? 85  LYS   E CG    1 
ATOM   10808 C  CD    . LYS   D 3  83  ? 37.523  35.538  17.480  1.00 48.01  ? 85  LYS   E CD    1 
ATOM   10809 C  CE    . LYS   D 3  83  ? 37.012  34.116  17.675  1.00 57.51  ? 85  LYS   E CE    1 
ATOM   10810 N  NZ    . LYS   D 3  83  ? 36.470  33.920  19.055  1.00 47.52  ? 85  LYS   E NZ    1 
ATOM   10811 N  N     . ALA   D 3  84  ? 36.681  38.281  13.268  1.00 25.28  ? 86  ALA   E N     1 
ATOM   10812 C  CA    . ALA   D 3  84  ? 35.710  38.242  12.179  1.00 27.02  ? 86  ALA   E CA    1 
ATOM   10813 C  C     . ALA   D 3  84  ? 36.395  38.177  10.819  1.00 32.85  ? 86  ALA   E C     1 
ATOM   10814 O  O     . ALA   D 3  84  ? 36.021  37.368  9.963   1.00 37.79  ? 86  ALA   E O     1 
ATOM   10815 C  CB    . ALA   D 3  84  ? 34.780  39.461  12.244  1.00 24.76  ? 86  ALA   E CB    1 
ATOM   10816 N  N     . ILE   D 3  85  ? 37.382  39.048  10.587  1.00 31.47  ? 87  ILE   E N     1 
ATOM   10817 C  CA    . ILE   D 3  85  ? 38.120  39.009  9.326   1.00 27.26  ? 87  ILE   E CA    1 
ATOM   10818 C  C     . ILE   D 3  85  ? 38.796  37.658  9.149   1.00 30.85  ? 87  ILE   E C     1 
ATOM   10819 O  O     . ILE   D 3  85  ? 38.794  37.091  8.051   1.00 25.80  ? 87  ILE   E O     1 
ATOM   10820 C  CB    . ILE   D 3  85  ? 39.152  40.147  9.249   1.00 27.82  ? 87  ILE   E CB    1 
ATOM   10821 C  CG1   . ILE   D 3  85  ? 38.576  41.473  9.687   1.00 31.32  ? 87  ILE   E CG1   1 
ATOM   10822 C  CG2   . ILE   D 3  85  ? 39.596  40.347  7.828   1.00 27.76  ? 87  ILE   E CG2   1 
ATOM   10823 C  CD1   . ILE   D 3  85  ? 39.357  42.605  9.072   1.00 28.01  ? 87  ILE   E CD1   1 
ATOM   10824 N  N     . GLU   D 3  86  ? 39.402  37.131  10.230  1.00 32.81  ? 88  GLU   E N     1 
ATOM   10825 C  CA    . GLU   D 3  86  ? 40.231  35.931  10.129  1.00 25.84  ? 88  GLU   E CA    1 
ATOM   10826 C  C     . GLU   D 3  86  ? 39.383  34.695  9.876   1.00 40.58  ? 88  GLU   E C     1 
ATOM   10827 O  O     . GLU   D 3  86  ? 39.814  33.764  9.181   1.00 43.27  ? 88  GLU   E O     1 
ATOM   10828 C  CB    . GLU   D 3  86  ? 41.058  35.753  11.394  1.00 32.79  ? 88  GLU   E CB    1 
ATOM   10829 C  CG    . GLU   D 3  86  ? 41.965  34.524  11.387  1.00 45.25  ? 88  GLU   E CG    1 
ATOM   10830 C  CD    . GLU   D 3  86  ? 43.044  34.621  10.325  1.00 62.25  ? 88  GLU   E CD    1 
ATOM   10831 O  OE1   . GLU   D 3  86  ? 43.418  35.767  10.001  1.00 57.40  ? 88  GLU   E OE1   1 
ATOM   10832 O  OE2   . GLU   D 3  86  ? 43.502  33.570  9.805   1.00 64.96  ? 88  GLU   E OE2   1 
ATOM   10833 N  N     . GLU   D 3  87  ? 38.182  34.657  10.444  1.00 41.11  ? 89  GLU   E N     1 
ATOM   10834 C  CA    . GLU   D 3  87  ? 37.288  33.548  10.163  1.00 40.62  ? 89  GLU   E CA    1 
ATOM   10835 C  C     . GLU   D 3  87  ? 36.650  33.711  8.793   1.00 33.51  ? 89  GLU   E C     1 
ATOM   10836 O  O     . GLU   D 3  87  ? 36.446  32.727  8.078   1.00 36.61  ? 89  GLU   E O     1 
ATOM   10837 C  CB    . GLU   D 3  87  ? 36.240  33.430  11.273  1.00 42.19  ? 89  GLU   E CB    1 
ATOM   10838 C  CG    . GLU   D 3  87  ? 36.665  32.449  12.350  1.00 53.89  ? 89  GLU   E CG    1 
ATOM   10839 C  CD    . GLU   D 3  87  ? 36.224  32.845  13.744  1.00 68.00  ? 89  GLU   E CD    1 
ATOM   10840 O  OE1   . GLU   D 3  87  ? 35.280  33.661  13.875  1.00 64.01  ? 89  GLU   E OE1   1 
ATOM   10841 O  OE2   . GLU   D 3  87  ? 36.830  32.328  14.713  1.00 67.93  ? 89  GLU   E OE2   1 
ATOM   10842 N  N     . ASN   D 3  88  ? 36.349  34.944  8.398   1.00 33.14  ? 90  ASN   E N     1 
ATOM   10843 C  CA    . ASN   D 3  88  ? 35.788  35.152  7.073   1.00 36.62  ? 90  ASN   E CA    1 
ATOM   10844 C  C     . ASN   D 3  88  ? 36.814  34.791  5.997   1.00 39.15  ? 90  ASN   E C     1 
ATOM   10845 O  O     . ASN   D 3  88  ? 36.481  34.178  4.973   1.00 34.79  ? 90  ASN   E O     1 
ATOM   10846 C  CB    . ASN   D 3  88  ? 35.312  36.599  6.948   1.00 29.02  ? 90  ASN   E CB    1 
ATOM   10847 C  CG    . ASN   D 3  88  ? 34.010  36.724  6.179   1.00 50.28  ? 90  ASN   E CG    1 
ATOM   10848 O  OD1   . ASN   D 3  88  ? 33.974  36.569  4.945   1.00 47.80  ? 90  ASN   E OD1   1 
ATOM   10849 N  ND2   . ASN   D 3  88  ? 32.924  37.013  6.903   1.00 59.57  ? 90  ASN   E ND2   1 
ATOM   10850 N  N     . ASN   D 3  89  ? 38.079  35.130  6.230   1.00 39.65  ? 91  ASN   E N     1 
ATOM   10851 C  CA    . ASN   D 3  89  ? 39.113  34.740  5.284   1.00 32.92  ? 91  ASN   E CA    1 
ATOM   10852 C  C     . ASN   D 3  89  ? 39.365  33.243  5.342   1.00 35.83  ? 91  ASN   E C     1 
ATOM   10853 O  O     . ASN   D 3  89  ? 39.479  32.584  4.304   1.00 43.12  ? 91  ASN   E O     1 
ATOM   10854 C  CB    . ASN   D 3  89  ? 40.384  35.541  5.550   1.00 32.35  ? 91  ASN   E CB    1 
ATOM   10855 C  CG    . ASN   D 3  89  ? 40.296  36.951  4.970   1.00 31.78  ? 91  ASN   E CG    1 
ATOM   10856 O  OD1   . ASN   D 3  89  ? 39.392  37.233  4.178   1.00 31.06  ? 91  ASN   E OD1   1 
ATOM   10857 N  ND2   . ASN   D 3  89  ? 41.226  37.832  5.347   1.00 27.95  ? 91  ASN   E ND2   1 
ATOM   10858 N  N     . ASN   D 3  90  ? 39.415  32.680  6.544   1.00 44.63  ? 92  ASN   E N     1 
ATOM   10859 C  CA    . ASN   D 3  90  ? 39.642  31.244  6.680   1.00 41.41  ? 92  ASN   E CA    1 
ATOM   10860 C  C     . ASN   D 3  90  ? 38.640  30.438  5.862   1.00 36.75  ? 92  ASN   E C     1 
ATOM   10861 O  O     . ASN   D 3  90  ? 38.987  29.407  5.278   1.00 35.54  ? 92  ASN   E O     1 
ATOM   10862 C  CB    . ASN   D 3  90  ? 39.564  30.867  8.156   1.00 47.40  ? 92  ASN   E CB    1 
ATOM   10863 C  CG    . ASN   D 3  90  ? 40.727  30.057  8.592   1.00 59.84  ? 92  ASN   E CG    1 
ATOM   10864 O  OD1   . ASN   D 3  90  ? 41.865  30.497  8.459   1.00 80.68  ? 92  ASN   E OD1   1 
ATOM   10865 N  ND2   . ASN   D 3  90  ? 40.468  28.863  9.111   1.00 60.41  ? 92  ASN   E ND2   1 
ATOM   10866 N  N     . PHE   D 3  91  ? 37.387  30.897  5.811   1.00 37.58  ? 93  PHE   E N     1 
ATOM   10867 C  CA    . PHE   D 3  91  ? 36.323  30.164  5.129   1.00 36.08  ? 93  PHE   E CA    1 
ATOM   10868 C  C     . PHE   D 3  91  ? 36.336  30.399  3.622   1.00 31.32  ? 93  PHE   E C     1 
ATOM   10869 O  O     . PHE   D 3  91  ? 35.953  29.510  2.856   1.00 36.54  ? 93  PHE   E O     1 
ATOM   10870 C  CB    . PHE   D 3  91  ? 34.969  30.548  5.738   1.00 29.76  ? 93  PHE   E CB    1 
ATOM   10871 C  CG    . PHE   D 3  91  ? 33.788  30.227  4.870   1.00 31.64  ? 93  PHE   E CG    1 
ATOM   10872 C  CD1   . PHE   D 3  91  ? 33.153  28.999  4.969   1.00 32.85  ? 93  PHE   E CD1   1 
ATOM   10873 C  CD2   . PHE   D 3  91  ? 33.303  31.164  3.966   1.00 29.64  ? 93  PHE   E CD2   1 
ATOM   10874 C  CE1   . PHE   D 3  91  ? 32.071  28.701  4.172   1.00 32.76  ? 93  PHE   E CE1   1 
ATOM   10875 C  CE2   . PHE   D 3  91  ? 32.220  30.876  3.162   1.00 31.77  ? 93  PHE   E CE2   1 
ATOM   10876 C  CZ    . PHE   D 3  91  ? 31.598  29.641  3.263   1.00 33.84  ? 93  PHE   E CZ    1 
ATOM   10877 N  N     . ILE   D 3  92  ? 36.742  31.583  3.172   1.00 27.63  ? 94  ILE   E N     1 
ATOM   10878 C  CA    . ILE   D 3  92  ? 37.026  31.739  1.754   1.00 33.35  ? 94  ILE   E CA    1 
ATOM   10879 C  C     . ILE   D 3  92  ? 38.165  30.815  1.338   1.00 36.96  ? 94  ILE   E C     1 
ATOM   10880 O  O     . ILE   D 3  92  ? 38.158  30.271  0.228   1.00 34.40  ? 94  ILE   E O     1 
ATOM   10881 C  CB    . ILE   D 3  92  ? 37.331  33.214  1.439   1.00 34.26  ? 94  ILE   E CB    1 
ATOM   10882 C  CG1   . ILE   D 3  92  ? 36.035  34.030  1.478   1.00 34.23  ? 94  ILE   E CG1   1 
ATOM   10883 C  CG2   . ILE   D 3  92  ? 38.074  33.351  0.130   1.00 28.36  ? 94  ILE   E CG2   1 
ATOM   10884 C  CD1   . ILE   D 3  92  ? 36.229  35.439  2.038   1.00 38.31  ? 94  ILE   E CD1   1 
ATOM   10885 N  N     . LYS   D 3  93  ? 39.129  30.574  2.236   1.00 34.99  ? 95  LYS   E N     1 
ATOM   10886 C  CA    . LYS   D 3  93  ? 40.357  29.880  1.856   1.00 35.55  ? 95  LYS   E CA    1 
ATOM   10887 C  C     . LYS   D 3  93  ? 40.206  28.359  1.883   1.00 41.97  ? 95  LYS   E C     1 
ATOM   10888 O  O     . LYS   D 3  93  ? 40.595  27.676  0.926   1.00 39.25  ? 95  LYS   E O     1 
ATOM   10889 C  CB    . LYS   D 3  93  ? 41.506  30.318  2.759   1.00 36.66  ? 95  LYS   E CB    1 
ATOM   10890 C  CG    . LYS   D 3  93  ? 42.700  29.381  2.728   1.00 41.95  ? 95  LYS   E CG    1 
ATOM   10891 C  CD    . LYS   D 3  93  ? 44.020  30.119  2.966   1.00 48.48  ? 95  LYS   E CD    1 
ATOM   10892 C  CE    . LYS   D 3  93  ? 45.150  29.156  3.336   1.00 60.30  ? 95  LYS   E CE    1 
ATOM   10893 N  NZ    . LYS   D 3  93  ? 46.494  29.788  3.159   1.00 56.79  ? 95  LYS   E NZ    1 
ATOM   10894 N  N     . MET   D 3  94  ? 39.688  27.795  2.979   1.00 43.58  ? 96  MET   E N     1 
ATOM   10895 C  CA    . MET   D 3  94  ? 39.369  26.370  2.948   1.00 42.11  ? 96  MET   E CA    1 
ATOM   10896 C  C     . MET   D 3  94  ? 38.425  26.068  1.799   1.00 32.09  ? 96  MET   E C     1 
ATOM   10897 O  O     . MET   D 3  94  ? 38.480  24.987  1.212   1.00 30.75  ? 96  MET   E O     1 
ATOM   10898 C  CB    . MET   D 3  94  ? 38.747  25.903  4.273   1.00 51.24  ? 96  MET   E CB    1 
ATOM   10899 C  CG    . MET   D 3  94  ? 39.737  25.615  5.425   1.00 55.17  ? 96  MET   E CG    1 
ATOM   10900 S  SD    . MET   D 3  94  ? 41.381  25.026  4.931   1.00 85.86  ? 96  MET   E SD    1 
ATOM   10901 C  CE    . MET   D 3  94  ? 41.021  23.493  4.033   1.00 56.59  ? 96  MET   E CE    1 
ATOM   10902 N  N     . ALA   D 3  95  ? 37.559  27.017  1.465   1.00 33.90  ? 97  ALA   E N     1 
ATOM   10903 C  CA    . ALA   D 3  95  ? 36.682  26.849  0.316   1.00 36.49  ? 97  ALA   E CA    1 
ATOM   10904 C  C     . ALA   D 3  95  ? 37.499  26.750  -0.954  1.00 38.68  ? 97  ALA   E C     1 
ATOM   10905 O  O     . ALA   D 3  95  ? 37.371  25.786  -1.715  1.00 43.31  ? 97  ALA   E O     1 
ATOM   10906 C  CB    . ALA   D 3  95  ? 35.700  28.018  0.225   1.00 32.23  ? 97  ALA   E CB    1 
ATOM   10907 N  N     . LYS   D 3  96  ? 38.363  27.741  -1.188  1.00 36.12  ? 98  LYS   E N     1 
ATOM   10908 C  CA    . LYS   D 3  96  ? 39.190  27.751  -2.385  1.00 31.05  ? 98  LYS   E CA    1 
ATOM   10909 C  C     . LYS   D 3  96  ? 40.025  26.480  -2.495  1.00 34.23  ? 98  LYS   E C     1 
ATOM   10910 O  O     . LYS   D 3  96  ? 40.267  25.998  -3.603  1.00 45.79  ? 98  LYS   E O     1 
ATOM   10911 C  CB    . LYS   D 3  96  ? 40.077  28.992  -2.379  1.00 28.32  ? 98  LYS   E CB    1 
ATOM   10912 C  CG    . LYS   D 3  96  ? 40.359  29.616  -3.733  1.00 28.68  ? 98  LYS   E CG    1 
ATOM   10913 C  CD    . LYS   D 3  96  ? 40.958  31.010  -3.573  1.00 30.83  ? 98  LYS   E CD    1 
ATOM   10914 C  CE    . LYS   D 3  96  ? 40.901  31.816  -4.864  1.00 38.62  ? 98  LYS   E CE    1 
ATOM   10915 N  NZ    . LYS   D 3  96  ? 40.643  33.287  -4.620  1.00 34.57  ? 98  LYS   E NZ    1 
ATOM   10916 N  N     . GLU   D 3  97  ? 40.461  25.911  -1.372  1.00 35.83  ? 99  GLU   E N     1 
ATOM   10917 C  CA    . GLU   D 3  97  ? 41.273  24.699  -1.428  1.00 33.91  ? 99  GLU   E CA    1 
ATOM   10918 C  C     . GLU   D 3  97  ? 40.429  23.508  -1.841  1.00 38.69  ? 99  GLU   E C     1 
ATOM   10919 O  O     . GLU   D 3  97  ? 40.701  22.865  -2.861  1.00 51.32  ? 99  GLU   E O     1 
ATOM   10920 C  CB    . GLU   D 3  97  ? 41.956  24.437  -0.082  1.00 36.95  ? 99  GLU   E CB    1 
ATOM   10921 C  CG    . GLU   D 3  97  ? 43.263  25.206  0.109   1.00 48.25  ? 99  GLU   E CG    1 
ATOM   10922 C  CD    . GLU   D 3  97  ? 43.732  25.306  1.577   1.00 59.78  ? 99  GLU   E CD    1 
ATOM   10923 O  OE1   . GLU   D 3  97  ? 43.550  24.340  2.372   1.00 41.95  ? 99  GLU   E OE1   1 
ATOM   10924 O  OE2   . GLU   D 3  97  ? 44.300  26.368  1.930   1.00 54.33  ? 99  GLU   E OE2   1 
ATOM   10925 N  N     . LYS   D 3  98  ? 39.399  23.188  -1.054  1.00 42.90  ? 100 LYS   E N     1 
ATOM   10926 C  CA    . LYS   D 3  98  ? 38.517  22.082  -1.414  1.00 45.63  ? 100 LYS   E CA    1 
ATOM   10927 C  C     . LYS   D 3  98  ? 38.065  22.180  -2.871  1.00 42.40  ? 100 LYS   E C     1 
ATOM   10928 O  O     . LYS   D 3  98  ? 38.019  21.177  -3.587  1.00 42.81  ? 100 LYS   E O     1 
ATOM   10929 C  CB    . LYS   D 3  98  ? 37.320  22.047  -0.468  1.00 44.42  ? 100 LYS   E CB    1 
ATOM   10930 C  CG    . LYS   D 3  98  ? 37.512  21.119  0.707   1.00 47.76  ? 100 LYS   E CG    1 
ATOM   10931 C  CD    . LYS   D 3  98  ? 36.693  21.569  1.906   1.00 54.55  ? 100 LYS   E CD    1 
ATOM   10932 C  CE    . LYS   D 3  98  ? 37.561  22.384  2.884   1.00 56.06  ? 100 LYS   E CE    1 
ATOM   10933 N  NZ    . LYS   D 3  98  ? 36.851  22.759  4.160   1.00 54.74  ? 100 LYS   E NZ    1 
ATOM   10934 N  N     . LEU   D 3  99  ? 37.761  23.386  -3.339  1.00 40.25  ? 101 LEU   E N     1 
ATOM   10935 C  CA    . LEU   D 3  99  ? 37.383  23.548  -4.738  1.00 42.53  ? 101 LEU   E CA    1 
ATOM   10936 C  C     . LEU   D 3  99  ? 38.436  22.976  -5.677  1.00 46.93  ? 101 LEU   E C     1 
ATOM   10937 O  O     . LEU   D 3  99  ? 38.106  22.409  -6.726  1.00 55.73  ? 101 LEU   E O     1 
ATOM   10938 C  CB    . LEU   D 3  99  ? 37.150  25.026  -5.053  1.00 35.75  ? 101 LEU   E CB    1 
ATOM   10939 C  CG    . LEU   D 3  99  ? 35.710  25.406  -5.389  1.00 42.59  ? 101 LEU   E CG    1 
ATOM   10940 C  CD1   . LEU   D 3  99  ? 35.676  26.789  -6.027  1.00 33.03  ? 101 LEU   E CD1   1 
ATOM   10941 C  CD2   . LEU   D 3  99  ? 35.025  24.346  -6.265  1.00 40.04  ? 101 LEU   E CD2   1 
ATOM   10942 N  N     . ALA   D 3  100 ? 39.708  23.142  -5.339  1.00 35.80  ? 102 ALA   E N     1 
ATOM   10943 C  CA    . ALA   D 3  100 ? 40.748  22.672  -6.233  1.00 36.46  ? 102 ALA   E CA    1 
ATOM   10944 C  C     . ALA   D 3  100 ? 41.169  21.241  -5.906  1.00 48.31  ? 102 ALA   E C     1 
ATOM   10945 O  O     . ALA   D 3  100 ? 41.433  20.447  -6.815  1.00 52.25  ? 102 ALA   E O     1 
ATOM   10946 C  CB    . ALA   D 3  100 ? 41.943  23.624  -6.184  1.00 33.22  ? 102 ALA   E CB    1 
ATOM   10947 N  N     . GLN   D 3  101 ? 41.226  20.876  -4.628  1.00 46.54  ? 103 GLN   E N     1 
ATOM   10948 C  CA    . GLN   D 3  101 ? 41.448  19.473  -4.308  1.00 47.11  ? 103 GLN   E CA    1 
ATOM   10949 C  C     . GLN   D 3  101 ? 40.351  18.584  -4.886  1.00 49.54  ? 103 GLN   E C     1 
ATOM   10950 O  O     . GLN   D 3  101 ? 40.606  17.424  -5.228  1.00 51.71  ? 103 GLN   E O     1 
ATOM   10951 C  CB    . GLN   D 3  101 ? 41.546  19.289  -2.800  1.00 43.79  ? 103 GLN   E CB    1 
ATOM   10952 C  CG    . GLN   D 3  101 ? 41.272  17.863  -2.357  1.00 59.91  ? 103 GLN   E CG    1 
ATOM   10953 C  CD    . GLN   D 3  101 ? 39.955  17.720  -1.592  1.00 75.01  ? 103 GLN   E CD    1 
ATOM   10954 O  OE1   . GLN   D 3  101 ? 39.755  18.344  -0.535  1.00 70.99  ? 103 GLN   E OE1   1 
ATOM   10955 N  NE2   . GLN   D 3  101 ? 39.050  16.891  -2.122  1.00 67.51  ? 103 GLN   E NE2   1 
ATOM   10956 N  N     . LYS   D 3  102 ? 39.127  19.105  -5.003  1.00 53.27  ? 104 LYS   E N     1 
ATOM   10957 C  CA    . LYS   D 3  102 ? 38.032  18.343  -5.601  1.00 50.72  ? 104 LYS   E CA    1 
ATOM   10958 C  C     . LYS   D 3  102 ? 38.167  18.263  -7.122  1.00 47.55  ? 104 LYS   E C     1 
ATOM   10959 O  O     . LYS   D 3  102 ? 37.949  17.200  -7.706  1.00 47.77  ? 104 LYS   E O     1 
ATOM   10960 C  CB    . LYS   D 3  102 ? 36.679  18.969  -5.215  1.00 54.33  ? 104 LYS   E CB    1 
ATOM   10961 C  CG    . LYS   D 3  102 ? 35.871  18.233  -4.124  1.00 46.65  ? 104 LYS   E CG    1 
ATOM   10962 C  CD    . LYS   D 3  102 ? 34.650  19.045  -3.603  1.00 43.23  ? 104 LYS   E CD    1 
ATOM   10963 C  CE    . LYS   D 3  102 ? 33.528  19.248  -4.631  1.00 45.86  ? 104 LYS   E CE    1 
ATOM   10964 N  NZ    . LYS   D 3  102 ? 32.155  19.309  -4.001  1.00 31.24  ? 104 LYS   E NZ    1 
ATOM   10965 N  N     . MET   D 3  103 ? 38.520  19.372  -7.778  1.00 48.45  ? 105 MET   E N     1 
ATOM   10966 C  CA    . MET   D 3  103 ? 38.604  19.420  -9.232  1.00 41.05  ? 105 MET   E CA    1 
ATOM   10967 C  C     . MET   D 3  103 ? 39.854  18.760  -9.782  1.00 46.19  ? 105 MET   E C     1 
ATOM   10968 O  O     . MET   D 3  103 ? 39.890  18.445  -10.978 1.00 48.69  ? 105 MET   E O     1 
ATOM   10969 C  CB    . MET   D 3  103 ? 38.563  20.867  -9.726  1.00 42.83  ? 105 MET   E CB    1 
ATOM   10970 C  CG    . MET   D 3  103 ? 37.407  21.157  -10.686 1.00 68.22  ? 105 MET   E CG    1 
ATOM   10971 S  SD    . MET   D 3  103 ? 35.768  20.716  -10.032 1.00 57.12  ? 105 MET   E SD    1 
ATOM   10972 C  CE    . MET   D 3  103 ? 35.777  21.613  -8.465  1.00 48.53  ? 105 MET   E CE    1 
ATOM   10973 N  N     . GLU   D 3  104 ? 40.883  18.562  -8.959  1.00 45.70  ? 106 GLU   E N     1 
ATOM   10974 C  CA    . GLU   D 3  104 ? 42.062  17.879  -9.465  1.00 42.84  ? 106 GLU   E CA    1 
ATOM   10975 C  C     . GLU   D 3  104 ? 41.926  16.373  -9.296  1.00 42.47  ? 106 GLU   E C     1 
ATOM   10976 O  O     . GLU   D 3  104 ? 42.083  15.619  -10.263 1.00 42.85  ? 106 GLU   E O     1 
ATOM   10977 C  CB    . GLU   D 3  104 ? 43.328  18.404  -8.781  1.00 41.71  ? 106 GLU   E CB    1 
ATOM   10978 C  CG    . GLU   D 3  104 ? 44.598  18.399  -9.683  1.00 60.87  ? 106 GLU   E CG    1 
ATOM   10979 C  CD    . GLU   D 3  104 ? 44.352  18.908  -11.134 1.00 76.17  ? 106 GLU   E CD    1 
ATOM   10980 O  OE1   . GLU   D 3  104 ? 43.263  19.465  -11.422 1.00 78.24  ? 106 GLU   E OE1   1 
ATOM   10981 O  OE2   . GLU   D 3  104 ? 45.257  18.743  -11.992 1.00 70.66  ? 106 GLU   E OE2   1 
ATOM   10982 N  N     . SER   D 3  105 ? 41.603  15.920  -8.087  1.00 42.40  ? 107 SER   E N     1 
ATOM   10983 C  CA    . SER   D 3  105 ? 41.326  14.502  -7.890  1.00 44.10  ? 107 SER   E CA    1 
ATOM   10984 C  C     . SER   D 3  105 ? 40.269  13.997  -8.877  1.00 45.61  ? 107 SER   E C     1 
ATOM   10985 O  O     . SER   D 3  105 ? 40.350  12.863  -9.369  1.00 39.71  ? 107 SER   E O     1 
ATOM   10986 C  CB    . SER   D 3  105 ? 40.876  14.260  -6.452  1.00 40.03  ? 107 SER   E CB    1 
ATOM   10987 O  OG    . SER   D 3  105 ? 39.463  14.120  -6.392  1.00 46.50  ? 107 SER   E OG    1 
ATOM   10988 N  N     . ASN   D 3  106 ? 39.263  14.825  -9.170  1.00 37.41  ? 108 ASN   E N     1 
ATOM   10989 C  CA    . ASN   D 3  106 ? 38.230  14.441  -10.122 1.00 39.34  ? 108 ASN   E CA    1 
ATOM   10990 C  C     . ASN   D 3  106 ? 38.811  14.312  -11.523 1.00 51.77  ? 108 ASN   E C     1 
ATOM   10991 O  O     . ASN   D 3  106 ? 38.549  13.326  -12.222 1.00 48.71  ? 108 ASN   E O     1 
ATOM   10992 C  CB    . ASN   D 3  106 ? 37.093  15.465  -10.088 1.00 47.61  ? 108 ASN   E CB    1 
ATOM   10993 C  CG    . ASN   D 3  106 ? 36.015  15.181  -11.110 1.00 51.22  ? 108 ASN   E CG    1 
ATOM   10994 O  OD1   . ASN   D 3  106 ? 36.031  15.722  -12.226 1.00 59.27  ? 108 ASN   E OD1   1 
ATOM   10995 N  ND2   . ASN   D 3  106 ? 35.067  14.331  -10.739 1.00 47.97  ? 108 ASN   E ND2   1 
ATOM   10996 N  N     . LYS   D 3  107 ? 39.621  15.294  -11.943 1.00 50.95  ? 109 LYS   E N     1 
ATOM   10997 C  CA    . LYS   D 3  107 ? 40.236  15.240  -13.270 1.00 48.66  ? 109 LYS   E CA    1 
ATOM   10998 C  C     . LYS   D 3  107 ? 41.094  13.991  -13.432 1.00 42.80  ? 109 LYS   E C     1 
ATOM   10999 O  O     . LYS   D 3  107 ? 41.053  13.331  -14.478 1.00 44.82  ? 109 LYS   E O     1 
ATOM   11000 C  CB    . LYS   D 3  107 ? 41.078  16.497  -13.526 1.00 49.35  ? 109 LYS   E CB    1 
ATOM   11001 C  CG    . LYS   D 3  107 ? 41.604  16.621  -14.956 1.00 44.64  ? 109 LYS   E CG    1 
ATOM   11002 C  CD    . LYS   D 3  107 ? 42.832  17.541  -15.069 1.00 47.83  ? 109 LYS   E CD    1 
ATOM   11003 C  CE    . LYS   D 3  107 ? 43.328  17.600  -16.506 1.00 41.20  ? 109 LYS   E CE    1 
ATOM   11004 N  NZ    . LYS   D 3  107 ? 44.306  18.683  -16.715 1.00 60.93  ? 109 LYS   E NZ    1 
ATOM   11005 N  N     . GLU   D 3  108 ? 41.886  13.655  -12.411 1.00 41.59  ? 110 GLU   E N     1 
ATOM   11006 C  CA    . GLU   D 3  108 ? 42.808  12.537  -12.541 1.00 38.89  ? 110 GLU   E CA    1 
ATOM   11007 C  C     . GLU   D 3  108 ? 42.086  11.202  -12.515 1.00 44.92  ? 110 GLU   E C     1 
ATOM   11008 O  O     . GLU   D 3  108 ? 42.621  10.217  -13.032 1.00 53.84  ? 110 GLU   E O     1 
ATOM   11009 C  CB    . GLU   D 3  108 ? 43.870  12.590  -11.443 1.00 32.09  ? 110 GLU   E CB    1 
ATOM   11010 C  CG    . GLU   D 3  108 ? 43.409  12.159  -10.090 1.00 46.01  ? 110 GLU   E CG    1 
ATOM   11011 C  CD    . GLU   D 3  108 ? 44.490  12.324  -9.027  1.00 67.42  ? 110 GLU   E CD    1 
ATOM   11012 O  OE1   . GLU   D 3  108 ? 45.612  12.765  -9.377  1.00 66.30  ? 110 GLU   E OE1   1 
ATOM   11013 O  OE2   . GLU   D 3  108 ? 44.215  12.019  -7.840  1.00 72.65  ? 110 GLU   E OE2   1 
ATOM   11014 N  N     . ASN   D 3  109 ? 40.877  11.158  -11.952 1.00 45.90  ? 111 ASN   E N     1 
ATOM   11015 C  CA    . ASN   D 3  109 ? 40.111  9.918   -11.871 1.00 43.27  ? 111 ASN   E CA    1 
ATOM   11016 C  C     . ASN   D 3  109 ? 39.393  9.608   -13.179 1.00 47.12  ? 111 ASN   E C     1 
ATOM   11017 O  O     . ASN   D 3  109 ? 39.530  8.507   -13.727 1.00 46.86  ? 111 ASN   E O     1 
ATOM   11018 C  CB    . ASN   D 3  109 ? 39.108  10.005  -10.725 1.00 36.33  ? 111 ASN   E CB    1 
ATOM   11019 C  CG    . ASN   D 3  109 ? 39.725  9.705   -9.409  1.00 38.90  ? 111 ASN   E CG    1 
ATOM   11020 O  OD1   . ASN   D 3  109 ? 39.431  10.359  -8.416  1.00 51.94  ? 111 ASN   E OD1   1 
ATOM   11021 N  ND2   . ASN   D 3  109 ? 40.607  8.711   -9.384  1.00 54.65  ? 111 ASN   E ND2   1 
ATOM   11022 N  N     . ARG   D 3  110 ? 38.592  10.559  -13.678 1.00 39.22  ? 112 ARG   E N     1 
ATOM   11023 C  CA    . ARG   D 3  110 ? 37.938  10.356  -14.963 1.00 39.84  ? 112 ARG   E CA    1 
ATOM   11024 C  C     . ARG   D 3  110 ? 38.957  9.950   -16.020 1.00 55.12  ? 112 ARG   E C     1 
ATOM   11025 O  O     . ARG   D 3  110 ? 38.669  9.116   -16.890 1.00 56.07  ? 112 ARG   E O     1 
ATOM   11026 C  CB    . ARG   D 3  110 ? 37.177  11.619  -15.391 1.00 43.29  ? 112 ARG   E CB    1 
ATOM   11027 C  CG    . ARG   D 3  110 ? 36.179  11.375  -16.544 1.00 38.46  ? 112 ARG   E CG    1 
ATOM   11028 C  CD    . ARG   D 3  110 ? 35.432  12.624  -16.988 1.00 34.22  ? 112 ARG   E CD    1 
ATOM   11029 N  NE    . ARG   D 3  110 ? 34.716  12.376  -18.233 1.00 36.69  ? 112 ARG   E NE    1 
ATOM   11030 C  CZ    . ARG   D 3  110 ? 35.026  12.908  -19.411 1.00 54.78  ? 112 ARG   E CZ    1 
ATOM   11031 N  NH1   . ARG   D 3  110 ? 35.972  13.828  -19.532 1.00 57.85  ? 112 ARG   E NH1   1 
ATOM   11032 N  NH2   . ARG   D 3  110 ? 34.367  12.511  -20.497 1.00 63.08  ? 112 ARG   E NH2   1 
ATOM   11033 N  N     . GLU   D 3  111 ? 40.168  10.504  -15.944 1.00 47.63  ? 113 GLU   E N     1 
ATOM   11034 C  CA    . GLU   D 3  111 ? 41.176  10.144  -16.926 1.00 41.97  ? 113 GLU   E CA    1 
ATOM   11035 C  C     . GLU   D 3  111 ? 41.750  8.759   -16.647 1.00 51.51  ? 113 GLU   E C     1 
ATOM   11036 O  O     . GLU   D 3  111 ? 41.891  7.955   -17.574 1.00 47.72  ? 113 GLU   E O     1 
ATOM   11037 C  CB    . GLU   D 3  111 ? 42.249  11.225  -16.978 1.00 50.43  ? 113 GLU   E CB    1 
ATOM   11038 C  CG    . GLU   D 3  111 ? 41.827  12.392  -17.890 1.00 55.99  ? 113 GLU   E CG    1 
ATOM   11039 C  CD    . GLU   D 3  111 ? 42.516  13.705  -17.554 1.00 60.09  ? 113 GLU   E CD    1 
ATOM   11040 O  OE1   . GLU   D 3  111 ? 43.668  13.657  -17.060 1.00 56.71  ? 113 GLU   E OE1   1 
ATOM   11041 O  OE2   . GLU   D 3  111 ? 41.901  14.780  -17.782 1.00 56.29  ? 113 GLU   E OE2   1 
ATOM   11042 N  N     . ALA   D 3  112 ? 42.032  8.435   -15.379 1.00 52.77  ? 114 ALA   E N     1 
ATOM   11043 C  CA    . ALA   D 3  112 ? 42.456  7.075   -15.048 1.00 48.32  ? 114 ALA   E CA    1 
ATOM   11044 C  C     . ALA   D 3  112 ? 41.414  6.053   -15.493 1.00 52.84  ? 114 ALA   E C     1 
ATOM   11045 O  O     . ALA   D 3  112 ? 41.754  5.029   -16.098 1.00 57.64  ? 114 ALA   E O     1 
ATOM   11046 C  CB    . ALA   D 3  112 ? 42.732  6.942   -13.549 1.00 32.47  ? 114 ALA   E CB    1 
ATOM   11047 N  N     . HIS   D 3  113 ? 40.136  6.306   -15.185 1.00 56.70  ? 115 HIS   E N     1 
ATOM   11048 C  CA    . HIS   D 3  113 ? 39.066  5.414   -15.636 1.00 60.09  ? 115 HIS   E CA    1 
ATOM   11049 C  C     . HIS   D 3  113 ? 39.051  5.308   -17.156 1.00 58.62  ? 115 HIS   E C     1 
ATOM   11050 O  O     . HIS   D 3  113 ? 38.873  4.215   -17.711 1.00 53.50  ? 115 HIS   E O     1 
ATOM   11051 C  CB    . HIS   D 3  113 ? 37.709  5.908   -15.104 1.00 55.04  ? 115 HIS   E CB    1 
ATOM   11052 C  CG    . HIS   D 3  113 ? 36.512  5.370   -15.848 1.00 70.45  ? 115 HIS   E CG    1 
ATOM   11053 N  ND1   . HIS   D 3  113 ? 35.674  4.406   -15.321 1.00 71.74  ? 115 HIS   E ND1   1 
ATOM   11054 C  CD2   . HIS   D 3  113 ? 36.004  5.674   -17.071 1.00 66.55  ? 115 HIS   E CD2   1 
ATOM   11055 C  CE1   . HIS   D 3  113 ? 34.710  4.135   -16.187 1.00 54.86  ? 115 HIS   E CE1   1 
ATOM   11056 N  NE2   . HIS   D 3  113 ? 34.889  4.888   -17.259 1.00 58.73  ? 115 HIS   E NE2   1 
ATOM   11057 N  N     . LEU   D 3  114 ? 39.255  6.440   -17.843 1.00 56.32  ? 116 LEU   E N     1 
ATOM   11058 C  CA    . LEU   D 3  114 ? 39.192  6.472   -19.303 1.00 51.73  ? 116 LEU   E CA    1 
ATOM   11059 C  C     . LEU   D 3  114 ? 40.415  5.807   -19.934 1.00 56.10  ? 116 LEU   E C     1 
ATOM   11060 O  O     . LEU   D 3  114 ? 40.278  5.043   -20.898 1.00 54.82  ? 116 LEU   E O     1 
ATOM   11061 C  CB    . LEU   D 3  114 ? 39.050  7.919   -19.787 1.00 47.34  ? 116 LEU   E CB    1 
ATOM   11062 C  CG    . LEU   D 3  114 ? 38.511  8.115   -21.207 1.00 55.53  ? 116 LEU   E CG    1 
ATOM   11063 C  CD1   . LEU   D 3  114 ? 36.980  8.190   -21.215 1.00 49.64  ? 116 LEU   E CD1   1 
ATOM   11064 C  CD2   . LEU   D 3  114 ? 39.151  9.315   -21.918 1.00 63.66  ? 116 LEU   E CD2   1 
ATOM   11065 N  N     . ALA   D 3  115 ? 41.620  6.091   -19.419 1.00 56.58  ? 117 ALA   E N     1 
ATOM   11066 C  CA    . ALA   D 3  115 ? 42.821  5.413   -19.911 1.00 49.06  ? 117 ALA   E CA    1 
ATOM   11067 C  C     . ALA   D 3  115 ? 42.634  3.905   -19.905 1.00 55.57  ? 117 ALA   E C     1 
ATOM   11068 O  O     . ALA   D 3  115 ? 42.842  3.232   -20.926 1.00 58.38  ? 117 ALA   E O     1 
ATOM   11069 C  CB    . ALA   D 3  115 ? 44.041  5.785   -19.065 1.00 42.07  ? 117 ALA   E CB    1 
ATOM   11070 N  N     . ALA   D 3  116 ? 42.260  3.359   -18.744 1.00 47.42  ? 118 ALA   E N     1 
ATOM   11071 C  CA    . ALA   D 3  116 ? 41.923  1.947   -18.620 1.00 50.80  ? 118 ALA   E CA    1 
ATOM   11072 C  C     . ALA   D 3  116 ? 41.117  1.444   -19.812 1.00 50.05  ? 118 ALA   E C     1 
ATOM   11073 O  O     . ALA   D 3  116 ? 41.454  0.420   -20.410 1.00 48.74  ? 118 ALA   E O     1 
ATOM   11074 C  CB    . ALA   D 3  116 ? 41.151  1.724   -17.315 1.00 45.13  ? 118 ALA   E CB    1 
ATOM   11075 N  N     . MET   D 3  117 ? 40.055  2.176   -20.185 1.00 52.85  ? 119 MET   E N     1 
ATOM   11076 C  CA    . MET   D 3  117 ? 39.112  1.695   -21.193 1.00 48.53  ? 119 MET   E CA    1 
ATOM   11077 C  C     . MET   D 3  117 ? 39.714  1.681   -22.592 1.00 56.65  ? 119 MET   E C     1 
ATOM   11078 O  O     . MET   D 3  117 ? 39.236  0.933   -23.456 1.00 67.95  ? 119 MET   E O     1 
ATOM   11079 C  CB    . MET   D 3  117 ? 37.828  2.533   -21.186 1.00 44.02  ? 119 MET   E CB    1 
ATOM   11080 C  CG    . MET   D 3  117 ? 37.228  2.763   -22.576 1.00 46.91  ? 119 MET   E CG    1 
ATOM   11081 S  SD    . MET   D 3  117 ? 35.584  3.533   -22.676 1.00 65.49  ? 119 MET   E SD    1 
ATOM   11082 C  CE    . MET   D 3  117 ? 35.706  4.815   -21.428 1.00 57.73  ? 119 MET   E CE    1 
ATOM   11083 N  N     . LEU   D 3  118 ? 40.736  2.494   -22.854 1.00 47.75  ? 120 LEU   E N     1 
ATOM   11084 C  CA    . LEU   D 3  118 ? 41.430  2.373   -24.130 1.00 51.77  ? 120 LEU   E CA    1 
ATOM   11085 C  C     . LEU   D 3  118 ? 42.588  1.385   -24.063 1.00 57.16  ? 120 LEU   E C     1 
ATOM   11086 O  O     . LEU   D 3  118 ? 42.911  0.749   -25.077 1.00 52.88  ? 120 LEU   E O     1 
ATOM   11087 C  CB    . LEU   D 3  118 ? 41.938  3.736   -24.602 1.00 50.13  ? 120 LEU   E CB    1 
ATOM   11088 C  CG    . LEU   D 3  118 ? 40.971  4.681   -25.317 1.00 40.38  ? 120 LEU   E CG    1 
ATOM   11089 C  CD1   . LEU   D 3  118 ? 39.900  5.251   -24.390 1.00 46.43  ? 120 LEU   E CD1   1 
ATOM   11090 C  CD2   . LEU   D 3  118 ? 41.775  5.791   -25.956 1.00 56.92  ? 120 LEU   E CD2   1 
ATOM   11091 N  N     . GLU   D 3  119 ? 43.222  1.244   -22.891 1.00 58.67  ? 121 GLU   E N     1 
ATOM   11092 C  CA    . GLU   D 3  119 ? 44.217  0.190   -22.717 1.00 61.55  ? 121 GLU   E CA    1 
ATOM   11093 C  C     . GLU   D 3  119 ? 43.605  -1.176  -22.996 1.00 59.16  ? 121 GLU   E C     1 
ATOM   11094 O  O     . GLU   D 3  119 ? 44.263  -2.057  -23.554 1.00 59.69  ? 121 GLU   E O     1 
ATOM   11095 C  CB    . GLU   D 3  119 ? 44.804  0.248   -21.304 1.00 56.27  ? 121 GLU   E CB    1 
ATOM   11096 C  CG    . GLU   D 3  119 ? 46.302  0.018   -21.213 1.00 60.29  ? 121 GLU   E CG    1 
ATOM   11097 C  CD    . GLU   D 3  119 ? 46.694  -1.454  -21.190 1.00 79.10  ? 121 GLU   E CD    1 
ATOM   11098 O  OE1   . GLU   D 3  119 ? 45.789  -2.316  -21.256 1.00 81.80  ? 121 GLU   E OE1   1 
ATOM   11099 O  OE2   . GLU   D 3  119 ? 47.913  -1.749  -21.101 1.00 83.51  ? 121 GLU   E OE2   1 
ATOM   11100 N  N     . ARG   D 3  120 ? 42.339  -1.367  -22.625 1.00 55.40  ? 122 ARG   E N     1 
ATOM   11101 C  CA    . ARG   D 3  120 ? 41.654  -2.611  -22.952 1.00 59.08  ? 122 ARG   E CA    1 
ATOM   11102 C  C     . ARG   D 3  120 ? 41.442  -2.724  -24.457 1.00 62.18  ? 122 ARG   E C     1 
ATOM   11103 O  O     . ARG   D 3  120 ? 41.885  -3.689  -25.092 1.00 57.86  ? 122 ARG   E O     1 
ATOM   11104 C  CB    . ARG   D 3  120 ? 40.319  -2.689  -22.200 1.00 51.72  ? 122 ARG   E CB    1 
ATOM   11105 C  CG    . ARG   D 3  120 ? 40.370  -3.494  -20.902 1.00 54.39  ? 122 ARG   E CG    1 
ATOM   11106 C  CD    . ARG   D 3  120 ? 38.994  -3.645  -20.250 1.00 64.94  ? 122 ARG   E CD    1 
ATOM   11107 N  NE    . ARG   D 3  120 ? 38.389  -2.367  -19.880 1.00 81.27  ? 122 ARG   E NE    1 
ATOM   11108 C  CZ    . ARG   D 3  120 ? 38.706  -1.660  -18.798 1.00 77.69  ? 122 ARG   E CZ    1 
ATOM   11109 N  NH1   . ARG   D 3  120 ? 39.644  -2.064  -17.953 1.00 72.78  ? 122 ARG   E NH1   1 
ATOM   11110 N  NH2   . ARG   D 3  120 ? 38.072  -0.513  -18.562 1.00 67.67  ? 122 ARG   E NH2   1 
ATOM   11111 N  N     . LEU   D 3  121 ? 40.774  -1.725  -25.047 1.00 66.98  ? 123 LEU   E N     1 
ATOM   11112 C  CA    . LEU   D 3  121 ? 40.539  -1.713  -26.487 1.00 59.52  ? 123 LEU   E CA    1 
ATOM   11113 C  C     . LEU   D 3  121 ? 41.818  -1.938  -27.268 1.00 62.70  ? 123 LEU   E C     1 
ATOM   11114 O  O     . LEU   D 3  121 ? 41.760  -2.337  -28.436 1.00 67.70  ? 123 LEU   E O     1 
ATOM   11115 C  CB    . LEU   D 3  121 ? 39.895  -0.388  -26.915 1.00 50.31  ? 123 LEU   E CB    1 
ATOM   11116 C  CG    . LEU   D 3  121 ? 38.527  -0.151  -26.280 1.00 45.42  ? 123 LEU   E CG    1 
ATOM   11117 C  CD1   . LEU   D 3  121 ? 37.612  0.580   -27.229 1.00 47.60  ? 123 LEU   E CD1   1 
ATOM   11118 C  CD2   . LEU   D 3  121 ? 37.919  -1.463  -25.867 1.00 39.64  ? 123 LEU   E CD2   1 
ATOM   11119 N  N     . GLN   D 3  122 ? 42.973  -1.705  -26.651 1.00 59.93  ? 124 GLN   E N     1 
ATOM   11120 C  CA    . GLN   D 3  122 ? 44.231  -1.865  -27.351 1.00 62.19  ? 124 GLN   E CA    1 
ATOM   11121 C  C     . GLN   D 3  122 ? 44.881  -3.222  -27.127 1.00 71.62  ? 124 GLN   E C     1 
ATOM   11122 O  O     . GLN   D 3  122 ? 45.772  -3.595  -27.898 1.00 82.03  ? 124 GLN   E O     1 
ATOM   11123 C  CB    . GLN   D 3  122 ? 45.183  -0.744  -26.955 1.00 53.80  ? 124 GLN   E CB    1 
ATOM   11124 C  CG    . GLN   D 3  122 ? 44.697  0.590   -27.482 1.00 59.05  ? 124 GLN   E CG    1 
ATOM   11125 C  CD    . GLN   D 3  122 ? 45.384  1.762   -26.813 1.00 67.82  ? 124 GLN   E CD    1 
ATOM   11126 O  OE1   . GLN   D 3  122 ? 46.052  1.603   -25.779 1.00 59.86  ? 124 GLN   E OE1   1 
ATOM   11127 N  NE2   . GLN   D 3  122 ? 45.222  2.954   -27.393 1.00 57.79  ? 124 GLN   E NE2   1 
ATOM   11128 N  N     . GLU   D 3  123 ? 44.460  -3.976  -26.112 1.00 67.18  ? 125 GLU   E N     1 
ATOM   11129 C  CA    . GLU   D 3  123 ? 44.826  -5.385  -26.070 1.00 61.76  ? 125 GLU   E CA    1 
ATOM   11130 C  C     . GLU   D 3  123 ? 43.900  -6.215  -26.928 1.00 68.22  ? 125 GLU   E C     1 
ATOM   11131 O  O     . GLU   D 3  123 ? 44.241  -7.350  -27.277 1.00 71.69  ? 125 GLU   E O     1 
ATOM   11132 C  CB    . GLU   D 3  123 ? 44.809  -5.926  -24.643 1.00 57.82  ? 125 GLU   E CB    1 
ATOM   11133 C  CG    . GLU   D 3  123 ? 45.726  -5.189  -23.681 1.00 76.19  ? 125 GLU   E CG    1 
ATOM   11134 C  CD    . GLU   D 3  123 ? 47.155  -5.020  -24.204 1.00 83.60  ? 125 GLU   E CD    1 
ATOM   11135 O  OE1   . GLU   D 3  123 ? 47.379  -4.993  -25.435 1.00 86.77  ? 125 GLU   E OE1   1 
ATOM   11136 O  OE2   . GLU   D 3  123 ? 48.067  -4.897  -23.358 1.00 94.25  ? 125 GLU   E OE2   1 
ATOM   11137 N  N     . LYS   D 3  124 ? 42.722  -5.680  -27.240 1.00 56.34  ? 126 LYS   E N     1 
ATOM   11138 C  CA    . LYS   D 3  124 ? 41.912  -6.277  -28.283 1.00 58.00  ? 126 LYS   E CA    1 
ATOM   11139 C  C     . LYS   D 3  124 ? 42.672  -6.284  -29.601 1.00 65.68  ? 126 LYS   E C     1 
ATOM   11140 O  O     . LYS   D 3  124 ? 42.644  -7.273  -30.340 1.00 67.82  ? 126 LYS   E O     1 
ATOM   11141 C  CB    . LYS   D 3  124 ? 40.596  -5.517  -28.419 1.00 56.03  ? 126 LYS   E CB    1 
ATOM   11142 C  CG    . LYS   D 3  124 ? 39.445  -6.167  -27.704 1.00 49.37  ? 126 LYS   E CG    1 
ATOM   11143 C  CD    . LYS   D 3  124 ? 38.122  -5.811  -28.376 1.00 54.88  ? 126 LYS   E CD    1 
ATOM   11144 C  CE    . LYS   D 3  124 ? 37.059  -6.882  -28.127 1.00 50.30  ? 126 LYS   E CE    1 
ATOM   11145 N  NZ    . LYS   D 3  124 ? 36.751  -7.056  -26.666 1.00 55.82  ? 126 LYS   E NZ    1 
ATOM   11146 N  N     . ASP   D 3  125 ? 43.380  -5.195  -29.900 1.00 67.66  ? 127 ASP   E N     1 
ATOM   11147 C  CA    . ASP   D 3  125 ? 44.115  -5.115  -31.156 1.00 66.46  ? 127 ASP   E CA    1 
ATOM   11148 C  C     . ASP   D 3  125 ? 45.233  -6.151  -31.198 1.00 66.19  ? 127 ASP   E C     1 
ATOM   11149 O  O     . ASP   D 3  125 ? 45.253  -7.032  -32.066 1.00 62.30  ? 127 ASP   E O     1 
ATOM   11150 C  CB    . ASP   D 3  125 ? 44.646  -3.695  -31.356 1.00 60.64  ? 127 ASP   E CB    1 
ATOM   11151 C  CG    . ASP   D 3  125 ? 43.525  -2.701  -31.643 1.00 65.05  ? 127 ASP   E CG    1 
ATOM   11152 O  OD1   . ASP   D 3  125 ? 42.364  -3.158  -31.731 1.00 56.53  ? 127 ASP   E OD1   1 
ATOM   11153 O  OD2   . ASP   D 3  125 ? 43.786  -1.481  -31.774 1.00 65.27  ? 127 ASP   E OD2   1 
ATOM   11154 N  N     . LYS   D 3  126 ? 46.158  -6.089  -30.240 1.00 71.87  ? 128 LYS   E N     1 
ATOM   11155 C  CA    . LYS   D 3  126 ? 47.297  -7.000  -30.284 1.00 71.96  ? 128 LYS   E CA    1 
ATOM   11156 C  C     . LYS   D 3  126 ? 46.846  -8.455  -30.308 1.00 71.33  ? 128 LYS   E C     1 
ATOM   11157 O  O     . LYS   D 3  126 ? 47.502  -9.299  -30.928 1.00 79.60  ? 128 LYS   E O     1 
ATOM   11158 C  CB    . LYS   D 3  126 ? 48.234  -6.751  -29.109 1.00 63.96  ? 128 LYS   E CB    1 
ATOM   11159 C  CG    . LYS   D 3  126 ? 47.733  -7.289  -27.807 1.00 67.31  ? 128 LYS   E CG    1 
ATOM   11160 C  CD    . LYS   D 3  126 ? 48.897  -7.464  -26.859 1.00 73.78  ? 128 LYS   E CD    1 
ATOM   11161 C  CE    . LYS   D 3  126 ? 49.944  -6.400  -27.108 1.00 73.16  ? 128 LYS   E CE    1 
ATOM   11162 N  NZ    . LYS   D 3  126 ? 51.259  -6.800  -26.547 1.00 71.89  ? 128 LYS   E NZ    1 
ATOM   11163 N  N     . HIS   D 3  127 ? 45.727  -8.774  -29.649 1.00 74.14  ? 129 HIS   E N     1 
ATOM   11164 C  CA    . HIS   D 3  127 ? 45.207  -10.138 -29.729 1.00 67.00  ? 129 HIS   E CA    1 
ATOM   11165 C  C     . HIS   D 3  127 ? 44.616  -10.428 -31.107 1.00 68.53  ? 129 HIS   E C     1 
ATOM   11166 O  O     . HIS   D 3  127 ? 44.800  -11.527 -31.641 1.00 71.70  ? 129 HIS   E O     1 
ATOM   11167 C  CB    . HIS   D 3  127 ? 44.172  -10.386 -28.637 1.00 60.04  ? 129 HIS   E CB    1 
ATOM   11168 C  CG    . HIS   D 3  127 ? 43.180  -11.459 -28.974 1.00 67.41  ? 129 HIS   E CG    1 
ATOM   11169 N  ND1   . HIS   D 3  127 ? 43.428  -12.801 -28.769 1.00 69.11  ? 129 HIS   E ND1   1 
ATOM   11170 C  CD2   . HIS   D 3  127 ? 41.929  -11.385 -29.493 1.00 68.76  ? 129 HIS   E CD2   1 
ATOM   11171 C  CE1   . HIS   D 3  127 ? 42.375  -13.505 -29.150 1.00 68.51  ? 129 HIS   E CE1   1 
ATOM   11172 N  NE2   . HIS   D 3  127 ? 41.452  -12.670 -29.594 1.00 59.78  ? 129 HIS   E NE2   1 
ATOM   11173 N  N     . ALA   D 3  128 ? 43.911  -9.463  -31.710 1.00 62.85  ? 130 ALA   E N     1 
ATOM   11174 C  CA    . ALA   D 3  128 ? 43.381  -9.703  -33.050 1.00 59.73  ? 130 ALA   E CA    1 
ATOM   11175 C  C     . ALA   D 3  128 ? 44.502  -9.837  -34.070 1.00 67.59  ? 130 ALA   E C     1 
ATOM   11176 O  O     . ALA   D 3  128 ? 44.350  -10.547 -35.072 1.00 65.64  ? 130 ALA   E O     1 
ATOM   11177 C  CB    . ALA   D 3  128 ? 42.422  -8.590  -33.463 1.00 51.70  ? 130 ALA   E CB    1 
ATOM   11178 N  N     . GLU   D 3  129 ? 45.628  -9.162  -33.837 1.00 69.58  ? 131 GLU   E N     1 
ATOM   11179 C  CA    . GLU   D 3  129 ? 46.807  -9.386  -34.663 1.00 69.44  ? 131 GLU   E CA    1 
ATOM   11180 C  C     . GLU   D 3  129 ? 47.288  -10.827 -34.533 1.00 64.43  ? 131 GLU   E C     1 
ATOM   11181 O  O     . GLU   D 3  129 ? 47.475  -11.525 -35.536 1.00 68.00  ? 131 GLU   E O     1 
ATOM   11182 C  CB    . GLU   D 3  129 ? 47.903  -8.399  -34.270 1.00 63.31  ? 131 GLU   E CB    1 
ATOM   11183 C  CG    . GLU   D 3  129 ? 47.534  -6.963  -34.545 1.00 67.43  ? 131 GLU   E CG    1 
ATOM   11184 C  CD    . GLU   D 3  129 ? 48.331  -6.386  -35.691 1.00 87.55  ? 131 GLU   E CD    1 
ATOM   11185 O  OE1   . GLU   D 3  129 ? 49.571  -6.561  -35.681 1.00 89.71  ? 131 GLU   E OE1   1 
ATOM   11186 O  OE2   . GLU   D 3  129 ? 47.725  -5.777  -36.605 1.00 85.89  ? 131 GLU   E OE2   1 
ATOM   11187 N  N     . GLU   D 3  130 ? 47.472  -11.292 -33.295 1.00 60.23  ? 132 GLU   E N     1 
ATOM   11188 C  CA    . GLU   D 3  130 ? 47.858  -12.678 -33.047 1.00 62.25  ? 132 GLU   E CA    1 
ATOM   11189 C  C     . GLU   D 3  130 ? 46.900  -13.669 -33.693 1.00 67.78  ? 132 GLU   E C     1 
ATOM   11190 O  O     . GLU   D 3  130 ? 47.318  -14.761 -34.097 1.00 68.06  ? 132 GLU   E O     1 
ATOM   11191 C  CB    . GLU   D 3  130 ? 47.924  -12.946 -31.544 1.00 64.15  ? 132 GLU   E CB    1 
ATOM   11192 C  CG    . GLU   D 3  130 ? 49.281  -12.713 -30.914 1.00 68.44  ? 132 GLU   E CG    1 
ATOM   11193 C  CD    . GLU   D 3  130 ? 49.273  -12.987 -29.420 1.00 83.71  ? 132 GLU   E CD    1 
ATOM   11194 O  OE1   . GLU   D 3  130 ? 48.256  -12.658 -28.764 1.00 88.47  ? 132 GLU   E OE1   1 
ATOM   11195 O  OE2   . GLU   D 3  130 ? 50.276  -13.537 -28.905 1.00 80.64  ? 132 GLU   E OE2   1 
ATOM   11196 N  N     . VAL   D 3  131 ? 45.612  -13.326 -33.783 1.00 70.62  ? 133 VAL   E N     1 
ATOM   11197 C  CA    . VAL   D 3  131 ? 44.656  -14.246 -34.393 1.00 62.90  ? 133 VAL   E CA    1 
ATOM   11198 C  C     . VAL   D 3  131 ? 44.923  -14.365 -35.888 1.00 66.63  ? 133 VAL   E C     1 
ATOM   11199 O  O     . VAL   D 3  131 ? 44.871  -15.464 -36.456 1.00 66.39  ? 133 VAL   E O     1 
ATOM   11200 C  CB    . VAL   D 3  131 ? 43.211  -13.804 -34.087 1.00 55.11  ? 133 VAL   E CB    1 
ATOM   11201 C  CG1   . VAL   D 3  131 ? 42.220  -14.512 -34.980 1.00 55.98  ? 133 VAL   E CG1   1 
ATOM   11202 C  CG2   . VAL   D 3  131 ? 42.881  -14.100 -32.637 1.00 60.00  ? 133 VAL   E CG2   1 
ATOM   11203 N  N     . ARG   D 3  132 ? 45.247  -13.243 -36.546 1.00 63.45  ? 134 ARG   E N     1 
ATOM   11204 C  CA    . ARG   D 3  132 ? 45.606  -13.303 -37.960 1.00 61.84  ? 134 ARG   E CA    1 
ATOM   11205 C  C     . ARG   D 3  132 ? 46.982  -13.930 -38.161 1.00 70.08  ? 134 ARG   E C     1 
ATOM   11206 O  O     . ARG   D 3  132 ? 47.191  -14.658 -39.140 1.00 71.53  ? 134 ARG   E O     1 
ATOM   11207 C  CB    . ARG   D 3  132 ? 45.544  -11.908 -38.577 1.00 61.95  ? 134 ARG   E CB    1 
ATOM   11208 C  CG    . ARG   D 3  132 ? 44.126  -11.441 -38.938 1.00 57.58  ? 134 ARG   E CG    1 
ATOM   11209 C  CD    . ARG   D 3  132 ? 44.116  -9.975  -39.423 1.00 56.33  ? 134 ARG   E CD    1 
ATOM   11210 N  NE    . ARG   D 3  132 ? 44.631  -9.062  -38.408 1.00 69.91  ? 134 ARG   E NE    1 
ATOM   11211 C  CZ    . ARG   D 3  132 ? 43.905  -8.550  -37.423 1.00 69.51  ? 134 ARG   E CZ    1 
ATOM   11212 N  NH1   . ARG   D 3  132 ? 42.604  -8.779  -37.331 1.00 56.89  ? 134 ARG   E NH1   1 
ATOM   11213 N  NH2   . ARG   D 3  132 ? 44.501  -7.799  -36.500 1.00 71.90  ? 134 ARG   E NH2   1 
ATOM   11214 N  N     . LYS   D 3  133 ? 47.919  -13.682 -37.241 1.00 63.79  ? 135 LYS   E N     1 
ATOM   11215 C  CA    . LYS   D 3  133 ? 49.224  -14.327 -37.297 1.00 64.96  ? 135 LYS   E CA    1 
ATOM   11216 C  C     . LYS   D 3  133 ? 49.159  -15.822 -36.998 1.00 70.04  ? 135 LYS   E C     1 
ATOM   11217 O  O     . LYS   D 3  133 ? 50.116  -16.546 -37.294 1.00 73.57  ? 135 LYS   E O     1 
ATOM   11218 C  CB    . LYS   D 3  133 ? 50.180  -13.651 -36.326 1.00 67.40  ? 135 LYS   E CB    1 
ATOM   11219 C  CG    . LYS   D 3  133 ? 51.421  -13.090 -36.993 1.00 80.15  ? 135 LYS   E CG    1 
ATOM   11220 C  CD    . LYS   D 3  133 ? 52.476  -14.162 -37.198 1.00 77.34  ? 135 LYS   E CD    1 
ATOM   11221 C  CE    . LYS   D 3  133 ? 53.643  -13.619 -38.001 1.00 84.69  ? 135 LYS   E CE    1 
ATOM   11222 N  NZ    . LYS   D 3  133 ? 54.791  -14.561 -37.977 1.00 84.89  ? 135 LYS   E NZ    1 
ATOM   11223 N  N     . ASN   D 3  134 ? 48.070  -16.306 -36.413 1.00 69.59  ? 136 ASN   E N     1 
ATOM   11224 C  CA    . ASN   D 3  134 ? 47.911  -17.751 -36.308 1.00 75.45  ? 136 ASN   E CA    1 
ATOM   11225 C  C     . ASN   D 3  134 ? 47.379  -18.339 -37.615 1.00 75.61  ? 136 ASN   E C     1 
ATOM   11226 O  O     . ASN   D 3  134 ? 47.876  -19.371 -38.085 1.00 76.45  ? 136 ASN   E O     1 
ATOM   11227 C  CB    . ASN   D 3  134 ? 46.990  -18.099 -35.136 1.00 70.57  ? 136 ASN   E CB    1 
ATOM   11228 C  CG    . ASN   D 3  134 ? 47.429  -19.355 -34.400 1.00 78.69  ? 136 ASN   E CG    1 
ATOM   11229 O  OD1   . ASN   D 3  134 ? 48.626  -19.650 -34.299 1.00 85.67  ? 136 ASN   E OD1   1 
ATOM   11230 N  ND2   . ASN   D 3  134 ? 46.459  -20.103 -33.878 1.00 76.06  ? 136 ASN   E ND2   1 
ATOM   11231 N  N     . LYS   D 3  135 ? 46.376  -17.697 -38.217 1.00 67.80  ? 137 LYS   E N     1 
ATOM   11232 C  CA    . LYS   D 3  135 ? 45.877  -18.138 -39.513 1.00 59.25  ? 137 LYS   E CA    1 
ATOM   11233 C  C     . LYS   D 3  135 ? 47.025  -18.298 -40.492 1.00 74.01  ? 137 LYS   E C     1 
ATOM   11234 O  O     . LYS   D 3  135 ? 47.269  -19.388 -41.023 1.00 82.96  ? 137 LYS   E O     1 
ATOM   11235 C  CB    . LYS   D 3  135 ? 44.858  -17.133 -40.044 1.00 56.86  ? 137 LYS   E CB    1 
ATOM   11236 C  CG    . LYS   D 3  135 ? 44.359  -17.417 -41.426 1.00 42.42  ? 137 LYS   E CG    1 
ATOM   11237 C  CD    . LYS   D 3  135 ? 43.175  -16.527 -41.743 1.00 45.28  ? 137 LYS   E CD    1 
ATOM   11238 C  CE    . LYS   D 3  135 ? 42.151  -17.273 -42.552 1.00 43.46  ? 137 LYS   E CE    1 
ATOM   11239 N  NZ    . LYS   D 3  135 ? 41.637  -16.462 -43.689 1.00 55.59  ? 137 LYS   E NZ    1 
ATOM   11240 N  N     . GLU   D 3  136 ? 47.755  -17.207 -40.718 1.00 78.59  ? 138 GLU   E N     1 
ATOM   11241 C  CA    . GLU   D 3  136 ? 48.949  -17.187 -41.553 1.00 78.41  ? 138 GLU   E CA    1 
ATOM   11242 C  C     . GLU   D 3  136 ? 49.864  -18.383 -41.304 1.00 81.29  ? 138 GLU   E C     1 
ATOM   11243 O  O     . GLU   D 3  136 ? 50.567  -18.823 -42.219 1.00 85.80  ? 138 GLU   E O     1 
ATOM   11244 C  CB    . GLU   D 3  136 ? 49.725  -15.894 -41.314 1.00 78.10  ? 138 GLU   E CB    1 
ATOM   11245 C  CG    . GLU   D 3  136 ? 50.827  -15.657 -42.308 1.00 84.99  ? 138 GLU   E CG    1 
ATOM   11246 C  CD    . GLU   D 3  136 ? 50.292  -15.394 -43.699 1.00 92.16  ? 138 GLU   E CD    1 
ATOM   11247 O  OE1   . GLU   D 3  136 ? 49.451  -16.183 -44.193 1.00 83.89  ? 138 GLU   E OE1   1 
ATOM   11248 O  OE2   . GLU   D 3  136 ? 50.710  -14.381 -44.292 1.00 99.95  ? 138 GLU   E OE2   1 
ATOM   11249 N  N     . LEU   D 3  137 ? 49.865  -18.916 -40.076 1.00 76.43  ? 139 LEU   E N     1 
ATOM   11250 C  CA    . LEU   D 3  137 ? 50.742  -20.035 -39.749 1.00 68.16  ? 139 LEU   E CA    1 
ATOM   11251 C  C     . LEU   D 3  137 ? 50.469  -21.278 -40.589 1.00 86.74  ? 139 LEU   E C     1 
ATOM   11252 O  O     . LEU   D 3  137 ? 51.285  -22.205 -40.560 1.00 100.65 ? 139 LEU   E O     1 
ATOM   11253 C  CB    . LEU   D 3  137 ? 50.628  -20.392 -38.273 1.00 62.13  ? 139 LEU   E CB    1 
ATOM   11254 C  CG    . LEU   D 3  137 ? 51.246  -19.326 -37.381 1.00 75.67  ? 139 LEU   E CG    1 
ATOM   11255 C  CD1   . LEU   D 3  137 ? 51.165  -19.747 -35.919 1.00 76.84  ? 139 LEU   E CD1   1 
ATOM   11256 C  CD2   . LEU   D 3  137 ? 52.688  -19.032 -37.814 1.00 62.20  ? 139 LEU   E CD2   1 
ATOM   11257 N  N     . LYS   D 3  138 ? 49.356  -21.337 -41.325 1.00 79.43  ? 140 LYS   E N     1 
ATOM   11258 C  CA    . LYS   D 3  138 ? 49.130  -22.446 -42.260 1.00 75.70  ? 140 LYS   E CA    1 
ATOM   11259 C  C     . LYS   D 3  138 ? 50.392  -22.718 -43.110 1.00 85.84  ? 140 LYS   E C     1 
ATOM   11260 O  O     . LYS   D 3  138 ? 50.434  -23.623 -43.951 1.00 85.83  ? 140 LYS   E O     1 
ATOM   11261 C  CB    . LYS   D 3  138 ? 47.925  -22.148 -43.157 1.00 73.18  ? 140 LYS   E CB    1 
ATOM   11262 C  CG    . LYS   D 3  138 ? 48.078  -20.921 -44.048 1.00 69.45  ? 140 LYS   E CG    1 
ATOM   11263 C  CD    . LYS   D 3  138 ? 49.032  -21.180 -45.211 1.00 64.43  ? 140 LYS   E CD    1 
ATOM   11264 C  CE    . LYS   D 3  138 ? 50.093  -20.087 -45.302 1.00 75.14  ? 140 LYS   E CE    1 
ATOM   11265 N  NZ    . LYS   D 3  138 ? 51.492  -20.632 -45.263 1.00 75.44  ? 140 LYS   E NZ    1 
ATOM   11266 N  N     . MET   E 4  1   ? -5.634  57.115  59.625  1.00 55.13  ? 1   MET   F N     1 
ATOM   11267 C  CA    . MET   E 4  1   ? -4.516  56.232  59.958  1.00 57.13  ? 1   MET   F CA    1 
ATOM   11268 C  C     . MET   E 4  1   ? -3.553  56.901  60.937  1.00 46.69  ? 1   MET   F C     1 
ATOM   11269 O  O     . MET   E 4  1   ? -3.372  58.108  60.908  1.00 50.47  ? 1   MET   F O     1 
ATOM   11270 C  CB    . MET   E 4  1   ? -3.766  55.812  58.679  1.00 64.41  ? 1   MET   F CB    1 
ATOM   11271 C  CG    . MET   E 4  1   ? -2.484  54.984  58.921  1.00 57.58  ? 1   MET   F CG    1 
ATOM   11272 S  SD    . MET   E 4  1   ? -1.503  54.689  57.421  1.00 77.61  ? 1   MET   F SD    1 
ATOM   11273 C  CE    . MET   E 4  1   ? 0.060   54.114  58.093  1.00 56.90  ? 1   MET   F CE    1 
ATOM   11274 N  N     . TYR   E 4  2   ? -2.933  56.119  61.810  1.00 42.06  ? 2   TYR   F N     1 
ATOM   11275 C  CA    . TYR   E 4  2   ? -1.862  56.635  62.641  1.00 36.36  ? 2   TYR   F CA    1 
ATOM   11276 C  C     . TYR   E 4  2   ? -0.773  55.587  62.711  1.00 40.69  ? 2   TYR   F C     1 
ATOM   11277 O  O     . TYR   E 4  2   ? -1.003  54.405  62.444  1.00 43.49  ? 2   TYR   F O     1 
ATOM   11278 C  CB    . TYR   E 4  2   ? -2.333  56.993  64.039  1.00 37.70  ? 2   TYR   F CB    1 
ATOM   11279 C  CG    . TYR   E 4  2   ? -3.385  58.069  64.053  1.00 43.49  ? 2   TYR   F CG    1 
ATOM   11280 C  CD1   . TYR   E 4  2   ? -3.087  59.346  63.613  1.00 35.24  ? 2   TYR   F CD1   1 
ATOM   11281 C  CD2   . TYR   E 4  2   ? -4.671  57.814  64.529  1.00 38.77  ? 2   TYR   F CD2   1 
ATOM   11282 C  CE1   . TYR   E 4  2   ? -4.025  60.346  63.648  1.00 32.07  ? 2   TYR   F CE1   1 
ATOM   11283 C  CE2   . TYR   E 4  2   ? -5.621  58.801  64.556  1.00 36.72  ? 2   TYR   F CE2   1 
ATOM   11284 C  CZ    . TYR   E 4  2   ? -5.294  60.077  64.104  1.00 36.55  ? 2   TYR   F CZ    1 
ATOM   11285 O  OH    . TYR   E 4  2   ? -6.227  61.101  64.106  1.00 32.64  ? 2   TYR   F OH    1 
ATOM   11286 N  N     . THR   E 4  3   ? 0.421   56.030  63.057  1.00 33.86  ? 3   THR   F N     1 
ATOM   11287 C  CA    . THR   E 4  3   ? 1.562   55.134  63.084  1.00 41.62  ? 3   THR   F CA    1 
ATOM   11288 C  C     . THR   E 4  3   ? 2.269   55.220  64.428  1.00 45.60  ? 3   THR   F C     1 
ATOM   11289 O  O     . THR   E 4  3   ? 2.490   56.314  64.963  1.00 42.55  ? 3   THR   F O     1 
ATOM   11290 C  CB    . THR   E 4  3   ? 2.530   55.456  61.952  1.00 41.62  ? 3   THR   F CB    1 
ATOM   11291 O  OG1   . THR   E 4  3   ? 2.450   56.853  61.648  1.00 41.73  ? 3   THR   F OG1   1 
ATOM   11292 C  CG2   . THR   E 4  3   ? 2.171   54.654  60.720  1.00 41.48  ? 3   THR   F CG2   1 
ATOM   11293 N  N     . PHE   E 4  4   ? 2.619   54.056  64.967  1.00 39.26  ? 4   PHE   F N     1 
ATOM   11294 C  CA    . PHE   E 4  4   ? 3.408   53.974  66.177  1.00 33.23  ? 4   PHE   F CA    1 
ATOM   11295 C  C     . PHE   E 4  4   ? 4.522   52.962  65.973  1.00 40.86  ? 4   PHE   F C     1 
ATOM   11296 O  O     . PHE   E 4  4   ? 4.377   52.019  65.191  1.00 42.15  ? 4   PHE   F O     1 
ATOM   11297 C  CB    . PHE   E 4  4   ? 2.538   53.591  67.388  1.00 39.55  ? 4   PHE   F CB    1 
ATOM   11298 C  CG    . PHE   E 4  4   ? 2.028   52.157  67.374  1.00 44.47  ? 4   PHE   F CG    1 
ATOM   11299 C  CD1   . PHE   E 4  4   ? 0.912   51.807  66.622  1.00 38.79  ? 4   PHE   F CD1   1 
ATOM   11300 C  CD2   . PHE   E 4  4   ? 2.647   51.170  68.159  1.00 46.73  ? 4   PHE   F CD2   1 
ATOM   11301 C  CE1   . PHE   E 4  4   ? 0.434   50.508  66.625  1.00 44.70  ? 4   PHE   F CE1   1 
ATOM   11302 C  CE2   . PHE   E 4  4   ? 2.179   49.858  68.168  1.00 45.93  ? 4   PHE   F CE2   1 
ATOM   11303 C  CZ    . PHE   E 4  4   ? 1.065   49.527  67.405  1.00 49.99  ? 4   PHE   F CZ    1 
ATOM   11304 N  N     . VAL   E 4  5   ? 5.641   53.183  66.669  1.00 41.68  ? 5   VAL   F N     1 
ATOM   11305 C  CA    . VAL   E 4  5   ? 6.688   52.178  66.830  1.00 40.73  ? 5   VAL   F CA    1 
ATOM   11306 C  C     . VAL   E 4  5   ? 6.652   51.693  68.272  1.00 40.00  ? 5   VAL   F C     1 
ATOM   11307 O  O     . VAL   E 4  5   ? 6.079   52.337  69.152  1.00 43.67  ? 5   VAL   F O     1 
ATOM   11308 C  CB    . VAL   E 4  5   ? 8.096   52.705  66.479  1.00 45.43  ? 5   VAL   F CB    1 
ATOM   11309 C  CG1   . VAL   E 4  5   ? 8.090   53.379  65.110  1.00 48.99  ? 5   VAL   F CG1   1 
ATOM   11310 C  CG2   . VAL   E 4  5   ? 8.609   53.653  67.575  1.00 42.29  ? 5   VAL   F CG2   1 
ATOM   11311 N  N     . VAL   E 4  6   ? 7.295   50.553  68.519  1.00 39.79  ? 6   VAL   F N     1 
ATOM   11312 C  CA    . VAL   E 4  6   ? 7.399   49.973  69.857  1.00 40.09  ? 6   VAL   F CA    1 
ATOM   11313 C  C     . VAL   E 4  6   ? 8.873   49.773  70.181  1.00 37.86  ? 6   VAL   F C     1 
ATOM   11314 O  O     . VAL   E 4  6   ? 9.610   49.189  69.380  1.00 47.01  ? 6   VAL   F O     1 
ATOM   11315 C  CB    . VAL   E 4  6   ? 6.634   48.637  69.959  1.00 32.34  ? 6   VAL   F CB    1 
ATOM   11316 C  CG1   . VAL   E 4  6   ? 7.184   47.798  71.092  1.00 36.13  ? 6   VAL   F CG1   1 
ATOM   11317 C  CG2   . VAL   E 4  6   ? 5.139   48.883  70.134  1.00 33.34  ? 6   VAL   F CG2   1 
ATOM   11318 N  N     . ARG   E 4  7   ? 9.311   50.257  71.351  1.00 35.18  ? 7   ARG   F N     1 
ATOM   11319 C  CA    . ARG   E 4  7   ? 10.736  50.176  71.659  1.00 36.02  ? 7   ARG   F CA    1 
ATOM   11320 C  C     . ARG   E 4  7   ? 11.046  49.716  73.081  1.00 43.10  ? 7   ARG   F C     1 
ATOM   11321 O  O     . ARG   E 4  7   ? 12.186  49.893  73.535  1.00 47.17  ? 7   ARG   F O     1 
ATOM   11322 C  CB    . ARG   E 4  7   ? 11.423  51.519  71.426  1.00 39.82  ? 7   ARG   F CB    1 
ATOM   11323 C  CG    . ARG   E 4  7   ? 11.368  51.991  69.991  1.00 39.42  ? 7   ARG   F CG    1 
ATOM   11324 C  CD    . ARG   E 4  7   ? 11.547  53.476  69.931  1.00 35.26  ? 7   ARG   F CD    1 
ATOM   11325 N  NE    . ARG   E 4  7   ? 12.857  53.880  70.423  1.00 39.73  ? 7   ARG   F NE    1 
ATOM   11326 C  CZ    . ARG   E 4  7   ? 13.961  53.856  69.688  1.00 41.60  ? 7   ARG   F CZ    1 
ATOM   11327 N  NH1   . ARG   E 4  7   ? 13.949  53.399  68.444  1.00 41.09  ? 7   ARG   F NH1   1 
ATOM   11328 N  NH2   . ARG   E 4  7   ? 15.102  54.308  70.210  1.00 36.00  ? 7   ARG   F NH2   1 
ATOM   11329 N  N     . ASP   E 4  8   ? 10.072  49.119  73.786  1.00 43.59  ? 8   ASP   F N     1 
ATOM   11330 C  CA    . ASP   E 4  8   ? 10.271  48.444  75.075  1.00 40.58  ? 8   ASP   F CA    1 
ATOM   11331 C  C     . ASP   E 4  8   ? 9.385   47.203  75.016  1.00 55.17  ? 8   ASP   F C     1 
ATOM   11332 O  O     . ASP   E 4  8   ? 8.208   47.252  75.395  1.00 56.64  ? 8   ASP   F O     1 
ATOM   11333 C  CB    . ASP   E 4  8   ? 9.914   49.342  76.256  1.00 45.26  ? 8   ASP   F CB    1 
ATOM   11334 C  CG    . ASP   E 4  8   ? 10.099  48.654  77.632  1.00 48.96  ? 8   ASP   F CG    1 
ATOM   11335 O  OD1   . ASP   E 4  8   ? 10.406  47.447  77.695  1.00 50.21  ? 8   ASP   F OD1   1 
ATOM   11336 O  OD2   . ASP   E 4  8   ? 9.945   49.349  78.663  1.00 51.04  ? 8   ASP   F OD2   1 
ATOM   11337 N  N     . GLU   E 4  9   ? 9.961   46.085  74.527  1.00 62.31  ? 9   GLU   F N     1 
ATOM   11338 C  CA    . GLU   E 4  9   ? 9.243   44.801  74.383  1.00 57.57  ? 9   GLU   F CA    1 
ATOM   11339 C  C     . GLU   E 4  9   ? 8.962   44.098  75.733  1.00 57.36  ? 9   GLU   F C     1 
ATOM   11340 O  O     . GLU   E 4  9   ? 8.478   42.965  75.743  1.00 70.28  ? 9   GLU   F O     1 
ATOM   11341 C  CB    . GLU   E 4  9   ? 10.023  43.867  73.457  1.00 49.77  ? 9   GLU   F CB    1 
ATOM   11342 C  CG    . GLU   E 4  9   ? 9.151   43.142  72.442  1.00 62.10  ? 9   GLU   F CG    1 
ATOM   11343 C  CD    . GLU   E 4  9   ? 9.017   43.903  71.145  1.00 57.75  ? 9   GLU   F CD    1 
ATOM   11344 O  OE1   . GLU   E 4  9   ? 9.989   44.608  70.785  1.00 47.92  ? 9   GLU   F OE1   1 
ATOM   11345 O  OE2   . GLU   E 4  9   ? 7.950   43.790  70.486  1.00 52.78  ? 9   GLU   F OE2   1 
ATOM   11346 N  N     . ASN   E 4  10  ? 9.259   44.761  76.851  1.00 53.13  ? 10  ASN   F N     1 
ATOM   11347 C  CA    . ASN   E 4  10  ? 9.049   44.221  78.187  1.00 52.48  ? 10  ASN   F CA    1 
ATOM   11348 C  C     . ASN   E 4  10  ? 7.891   44.892  78.905  1.00 57.79  ? 10  ASN   F C     1 
ATOM   11349 O  O     . ASN   E 4  10  ? 7.774   44.784  80.131  1.00 68.15  ? 10  ASN   F O     1 
ATOM   11350 C  CB    . ASN   E 4  10  ? 10.322  44.363  79.012  1.00 47.13  ? 10  ASN   F CB    1 
ATOM   11351 C  CG    . ASN   E 4  10  ? 11.477  43.640  78.388  1.00 63.57  ? 10  ASN   F CG    1 
ATOM   11352 O  OD1   . ASN   E 4  10  ? 11.331  43.017  77.331  1.00 58.06  ? 10  ASN   F OD1   1 
ATOM   11353 N  ND2   . ASN   E 4  10  ? 12.640  43.714  79.028  1.00 80.01  ? 10  ASN   F ND2   1 
ATOM   11354 N  N     . SER   E 4  11  ? 7.033   45.584  78.169  1.00 54.95  ? 11  SER   F N     1 
ATOM   11355 C  CA    . SER   E 4  11  ? 5.948   46.344  78.773  1.00 47.17  ? 11  SER   F CA    1 
ATOM   11356 C  C     . SER   E 4  11  ? 4.679   45.518  78.632  1.00 44.86  ? 11  SER   F C     1 
ATOM   11357 O  O     . SER   E 4  11  ? 3.965   45.595  77.629  1.00 44.12  ? 11  SER   F O     1 
ATOM   11358 C  CB    . SER   E 4  11  ? 5.813   47.721  78.131  1.00 48.59  ? 11  SER   F CB    1 
ATOM   11359 O  OG    . SER   E 4  11  ? 4.942   48.550  78.871  1.00 31.11  ? 11  SER   F OG    1 
ATOM   11360 N  N     . SER   E 4  12  ? 4.406   44.711  79.654  1.00 51.34  ? 12  SER   F N     1 
ATOM   11361 C  CA    . SER   E 4  12  ? 3.073   44.153  79.835  1.00 53.79  ? 12  SER   F CA    1 
ATOM   11362 C  C     . SER   E 4  12  ? 2.028   45.214  79.486  1.00 51.44  ? 12  SER   F C     1 
ATOM   11363 O  O     . SER   E 4  12  ? 1.019   44.929  78.834  1.00 47.63  ? 12  SER   F O     1 
ATOM   11364 C  CB    . SER   E 4  12  ? 2.904   43.656  81.279  1.00 53.34  ? 12  SER   F CB    1 
ATOM   11365 O  OG    . SER   E 4  12  ? 3.654   44.442  82.206  1.00 61.23  ? 12  SER   F OG    1 
ATOM   11366 N  N     . VAL   E 4  13  ? 2.299   46.456  79.877  1.00 54.65  ? 13  VAL   F N     1 
ATOM   11367 C  CA    . VAL   E 4  13  ? 1.290   47.501  79.810  1.00 51.10  ? 13  VAL   F CA    1 
ATOM   11368 C  C     . VAL   E 4  13  ? 1.161   48.056  78.399  1.00 45.67  ? 13  VAL   F C     1 
ATOM   11369 O  O     . VAL   E 4  13  ? 0.053   48.153  77.863  1.00 47.83  ? 13  VAL   F O     1 
ATOM   11370 C  CB    . VAL   E 4  13  ? 1.621   48.597  80.832  1.00 53.02  ? 13  VAL   F CB    1 
ATOM   11371 C  CG1   . VAL   E 4  13  ? 0.360   49.380  81.159  1.00 55.83  ? 13  VAL   F CG1   1 
ATOM   11372 C  CG2   . VAL   E 4  13  ? 2.246   47.963  82.088  1.00 46.39  ? 13  VAL   F CG2   1 
ATOM   11373 N  N     . TYR   E 4  14  ? 2.271   48.429  77.761  1.00 50.00  ? 14  TYR   F N     1 
ATOM   11374 C  CA    . TYR   E 4  14  ? 2.168   48.962  76.402  1.00 50.23  ? 14  TYR   F CA    1 
ATOM   11375 C  C     . TYR   E 4  14  ? 2.216   47.881  75.330  1.00 46.97  ? 14  TYR   F C     1 
ATOM   11376 O  O     . TYR   E 4  14  ? 2.072   48.199  74.147  1.00 50.03  ? 14  TYR   F O     1 
ATOM   11377 C  CB    . TYR   E 4  14  ? 3.237   50.030  76.145  1.00 43.26  ? 14  TYR   F CB    1 
ATOM   11378 C  CG    . TYR   E 4  14  ? 2.944   51.304  76.913  1.00 46.48  ? 14  TYR   F CG    1 
ATOM   11379 C  CD1   . TYR   E 4  14  ? 2.003   52.218  76.460  1.00 45.15  ? 14  TYR   F CD1   1 
ATOM   11380 C  CD2   . TYR   E 4  14  ? 3.564   51.557  78.122  1.00 39.21  ? 14  TYR   F CD2   1 
ATOM   11381 C  CE1   . TYR   E 4  14  ? 1.713   53.365  77.184  1.00 39.07  ? 14  TYR   F CE1   1 
ATOM   11382 C  CE2   . TYR   E 4  14  ? 3.284   52.681  78.842  1.00 41.94  ? 14  TYR   F CE2   1 
ATOM   11383 C  CZ    . TYR   E 4  14  ? 2.365   53.598  78.378  1.00 46.21  ? 14  TYR   F CZ    1 
ATOM   11384 O  OH    . TYR   E 4  14  ? 2.118   54.741  79.131  1.00 44.65  ? 14  TYR   F OH    1 
ATOM   11385 N  N     . ALA   E 4  15  ? 2.392   46.616  75.713  1.00 44.82  ? 15  ALA   F N     1 
ATOM   11386 C  CA    . ALA   E 4  15  ? 1.965   45.530  74.840  1.00 41.27  ? 15  ALA   F CA    1 
ATOM   11387 C  C     . ALA   E 4  15  ? 0.449   45.495  74.701  1.00 47.34  ? 15  ALA   F C     1 
ATOM   11388 O  O     . ALA   E 4  15  ? -0.077  45.137  73.640  1.00 51.23  ? 15  ALA   F O     1 
ATOM   11389 C  CB    . ALA   E 4  15  ? 2.463   44.196  75.376  1.00 37.21  ? 15  ALA   F CB    1 
ATOM   11390 N  N     . GLU   E 4  16  ? -0.275  45.842  75.759  1.00 46.04  ? 16  GLU   F N     1 
ATOM   11391 C  CA    . GLU   E 4  16  ? -1.719  45.907  75.628  1.00 47.65  ? 16  GLU   F CA    1 
ATOM   11392 C  C     . GLU   E 4  16  ? -2.109  47.080  74.755  1.00 53.74  ? 16  GLU   F C     1 
ATOM   11393 O  O     . GLU   E 4  16  ? -3.011  46.965  73.917  1.00 52.92  ? 16  GLU   F O     1 
ATOM   11394 C  CB    . GLU   E 4  16  ? -2.374  46.008  77.004  1.00 54.97  ? 16  GLU   F CB    1 
ATOM   11395 C  CG    . GLU   E 4  16  ? -3.896  45.816  77.025  1.00 57.27  ? 16  GLU   F CG    1 
ATOM   11396 C  CD    . GLU   E 4  16  ? -4.353  44.456  76.490  1.00 66.39  ? 16  GLU   F CD    1 
ATOM   11397 O  OE1   . GLU   E 4  16  ? -3.494  43.596  76.174  1.00 71.35  ? 16  GLU   F OE1   1 
ATOM   11398 O  OE2   . GLU   E 4  16  ? -5.584  44.252  76.378  1.00 72.43  ? 16  GLU   F OE2   1 
ATOM   11399 N  N     . VAL   E 4  17  ? -1.404  48.203  74.914  1.00 55.73  ? 17  VAL   F N     1 
ATOM   11400 C  CA    . VAL   E 4  17  ? -1.721  49.403  74.144  1.00 56.33  ? 17  VAL   F CA    1 
ATOM   11401 C  C     . VAL   E 4  17  ? -1.542  49.140  72.650  1.00 54.87  ? 17  VAL   F C     1 
ATOM   11402 O  O     . VAL   E 4  17  ? -2.436  49.424  71.841  1.00 54.87  ? 17  VAL   F O     1 
ATOM   11403 C  CB    . VAL   E 4  17  ? -0.869  50.595  74.623  1.00 55.58  ? 17  VAL   F CB    1 
ATOM   11404 C  CG1   . VAL   E 4  17  ? -1.419  51.915  74.060  1.00 50.54  ? 17  VAL   F CG1   1 
ATOM   11405 C  CG2   . VAL   E 4  17  ? -0.808  50.627  76.143  1.00 51.01  ? 17  VAL   F CG2   1 
ATOM   11406 N  N     . SER   E 4  18  ? -0.384  48.600  72.255  1.00 49.04  ? 18  SER   F N     1 
ATOM   11407 C  CA    . SER   E 4  18  ? -0.188  48.327  70.835  1.00 52.24  ? 18  SER   F CA    1 
ATOM   11408 C  C     . SER   E 4  18  ? -1.184  47.290  70.334  1.00 52.50  ? 18  SER   F C     1 
ATOM   11409 O  O     . SER   E 4  18  ? -1.677  47.400  69.205  1.00 52.91  ? 18  SER   F O     1 
ATOM   11410 C  CB    . SER   E 4  18  ? 1.253   47.894  70.546  1.00 54.42  ? 18  SER   F CB    1 
ATOM   11411 O  OG    . SER   E 4  18  ? 1.769   47.017  71.533  1.00 49.83  ? 18  SER   F OG    1 
ATOM   11412 N  N     . ARG   E 4  19  ? -1.514  46.292  71.166  1.00 52.43  ? 19  ARG   F N     1 
ATOM   11413 C  CA    . ARG   E 4  19  ? -2.510  45.296  70.770  1.00 53.28  ? 19  ARG   F CA    1 
ATOM   11414 C  C     . ARG   E 4  19  ? -3.859  45.947  70.497  1.00 52.28  ? 19  ARG   F C     1 
ATOM   11415 O  O     . ARG   E 4  19  ? -4.544  45.598  69.526  1.00 59.81  ? 19  ARG   F O     1 
ATOM   11416 C  CB    . ARG   E 4  19  ? -2.658  44.216  71.846  1.00 60.61  ? 19  ARG   F CB    1 
ATOM   11417 C  CG    . ARG   E 4  19  ? -3.663  43.120  71.469  1.00 62.95  ? 19  ARG   F CG    1 
ATOM   11418 C  CD    . ARG   E 4  19  ? -3.993  42.164  72.625  1.00 72.73  ? 19  ARG   F CD    1 
ATOM   11419 N  NE    . ARG   E 4  19  ? -5.029  42.682  73.514  1.00 79.49  ? 19  ARG   F NE    1 
ATOM   11420 C  CZ    . ARG   E 4  19  ? -6.303  42.853  73.176  1.00 83.46  ? 19  ARG   F CZ    1 
ATOM   11421 N  NH1   . ARG   E 4  19  ? -6.742  42.580  71.954  1.00 72.71  ? 19  ARG   F NH1   1 
ATOM   11422 N  NH2   . ARG   E 4  19  ? -7.157  43.323  74.084  1.00 75.16  ? 19  ARG   F NH2   1 
ATOM   11423 N  N     . LEU   E 4  20  ? -4.269  46.883  71.355  1.00 55.02  ? 20  LEU   F N     1 
ATOM   11424 C  CA    . LEU   E 4  20  ? -5.528  47.584  71.138  1.00 52.59  ? 20  LEU   F CA    1 
ATOM   11425 C  C     . LEU   E 4  20  ? -5.458  48.452  69.888  1.00 55.13  ? 20  LEU   F C     1 
ATOM   11426 O  O     . LEU   E 4  20  ? -6.326  48.365  69.011  1.00 51.74  ? 20  LEU   F O     1 
ATOM   11427 C  CB    . LEU   E 4  20  ? -5.877  48.428  72.363  1.00 54.42  ? 20  LEU   F CB    1 
ATOM   11428 C  CG    . LEU   E 4  20  ? -6.506  47.758  73.587  1.00 58.49  ? 20  LEU   F CG    1 
ATOM   11429 C  CD1   . LEU   E 4  20  ? -5.760  46.482  73.957  1.00 62.13  ? 20  LEU   F CD1   1 
ATOM   11430 C  CD2   . LEU   E 4  20  ? -6.586  48.742  74.785  1.00 45.29  ? 20  LEU   F CD2   1 
ATOM   11431 N  N     . LEU   E 4  21  ? -4.423  49.291  69.787  1.00 51.06  ? 21  LEU   F N     1 
ATOM   11432 C  CA    . LEU   E 4  21  ? -4.318  50.212  68.660  1.00 50.27  ? 21  LEU   F CA    1 
ATOM   11433 C  C     . LEU   E 4  21  ? -4.454  49.467  67.337  1.00 51.72  ? 21  LEU   F C     1 
ATOM   11434 O  O     . LEU   E 4  21  ? -5.325  49.782  66.513  1.00 45.64  ? 21  LEU   F O     1 
ATOM   11435 C  CB    . LEU   E 4  21  ? -2.991  50.978  68.726  1.00 50.52  ? 21  LEU   F CB    1 
ATOM   11436 C  CG    . LEU   E 4  21  ? -2.776  52.030  69.822  1.00 49.83  ? 21  LEU   F CG    1 
ATOM   11437 C  CD1   . LEU   E 4  21  ? -1.302  52.469  69.847  1.00 43.43  ? 21  LEU   F CD1   1 
ATOM   11438 C  CD2   . LEU   E 4  21  ? -3.689  53.232  69.646  1.00 35.94  ? 21  LEU   F CD2   1 
ATOM   11439 N  N     . LEU   E 4  22  ? -3.602  48.456  67.127  1.00 48.14  ? 22  LEU   F N     1 
ATOM   11440 C  CA    . LEU   E 4  22  ? -3.695  47.643  65.917  1.00 55.19  ? 22  LEU   F CA    1 
ATOM   11441 C  C     . LEU   E 4  22  ? -5.119  47.141  65.709  1.00 54.36  ? 22  LEU   F C     1 
ATOM   11442 O  O     . LEU   E 4  22  ? -5.722  47.356  64.650  1.00 53.01  ? 22  LEU   F O     1 
ATOM   11443 C  CB    . LEU   E 4  22  ? -2.703  46.474  65.982  1.00 51.06  ? 22  LEU   F CB    1 
ATOM   11444 C  CG    . LEU   E 4  22  ? -1.214  46.834  65.847  1.00 51.18  ? 22  LEU   F CG    1 
ATOM   11445 C  CD1   . LEU   E 4  22  ? -0.325  45.659  66.234  1.00 37.37  ? 22  LEU   F CD1   1 
ATOM   11446 C  CD2   . LEU   E 4  22  ? -0.862  47.354  64.448  1.00 36.08  ? 22  LEU   F CD2   1 
ATOM   11447 N  N     . ALA   E 4  23  ? -5.691  46.506  66.728  1.00 57.63  ? 23  ALA   F N     1 
ATOM   11448 C  CA    . ALA   E 4  23  ? -7.033  45.949  66.614  1.00 56.74  ? 23  ALA   F CA    1 
ATOM   11449 C  C     . ALA   E 4  23  ? -8.088  47.017  66.319  1.00 49.20  ? 23  ALA   F C     1 
ATOM   11450 O  O     . ALA   E 4  23  ? -9.232  46.905  66.770  1.00 55.81  ? 23  ALA   F O     1 
ATOM   11451 C  CB    . ALA   E 4  23  ? -7.378  45.180  67.893  1.00 44.71  ? 23  ALA   F CB    1 
ATOM   11452 N  N     . THR   E 4  24  ? -7.720  48.056  65.566  1.00 49.60  ? 24  THR   F N     1 
ATOM   11453 C  CA    . THR   E 4  24  ? -8.682  49.070  65.142  1.00 50.72  ? 24  THR   F CA    1 
ATOM   11454 C  C     . THR   E 4  24  ? -8.584  49.425  63.670  1.00 55.41  ? 24  THR   F C     1 
ATOM   11455 O  O     . THR   E 4  24  ? -9.333  50.301  63.218  1.00 53.69  ? 24  THR   F O     1 
ATOM   11456 C  CB    . THR   E 4  24  ? -8.515  50.363  65.951  1.00 49.26  ? 24  THR   F CB    1 
ATOM   11457 O  OG1   . THR   E 4  24  ? -7.239  50.949  65.665  1.00 47.58  ? 24  THR   F OG1   1 
ATOM   11458 C  CG2   . THR   E 4  24  ? -8.596  50.082  67.439  1.00 48.31  ? 24  THR   F CG2   1 
ATOM   11459 N  N     . GLY   E 4  25  ? -7.698  48.788  62.908  1.00 42.08  ? 25  GLY   F N     1 
ATOM   11460 C  CA    . GLY   E 4  25  ? -7.460  49.177  61.539  1.00 55.38  ? 25  GLY   F CA    1 
ATOM   11461 C  C     . GLY   E 4  25  ? -7.068  50.626  61.343  1.00 63.33  ? 25  GLY   F C     1 
ATOM   11462 O  O     . GLY   E 4  25  ? -6.795  51.029  60.204  1.00 70.01  ? 25  GLY   F O     1 
ATOM   11463 N  N     . GLN   E 4  26  ? -7.021  51.419  62.412  1.00 55.10  ? 26  GLN   F N     1 
ATOM   11464 C  CA    . GLN   E 4  26  ? -6.656  52.820  62.340  1.00 51.76  ? 26  GLN   F CA    1 
ATOM   11465 C  C     . GLN   E 4  26  ? -5.218  53.079  62.762  1.00 50.03  ? 26  GLN   F C     1 
ATOM   11466 O  O     . GLN   E 4  26  ? -4.765  54.225  62.663  1.00 44.13  ? 26  GLN   F O     1 
ATOM   11467 C  CB    . GLN   E 4  26  ? -7.603  53.652  63.213  1.00 51.84  ? 26  GLN   F CB    1 
ATOM   11468 C  CG    . GLN   E 4  26  ? -9.076  53.449  62.898  1.00 50.28  ? 26  GLN   F CG    1 
ATOM   11469 C  CD    . GLN   E 4  26  ? -9.837  54.772  62.759  1.00 56.45  ? 26  GLN   F CD    1 
ATOM   11470 O  OE1   . GLN   E 4  26  ? -10.848 55.011  63.436  1.00 54.34  ? 26  GLN   F OE1   1 
ATOM   11471 N  NE2   . GLN   E 4  26  ? -9.366  55.625  61.850  1.00 53.96  ? 26  GLN   F NE2   1 
ATOM   11472 N  N     . TRP   E 4  27  ? -4.489  52.049  63.205  1.00 48.12  ? 27  TRP   F N     1 
ATOM   11473 C  CA    . TRP   E 4  27  ? -3.115  52.184  63.678  1.00 46.17  ? 27  TRP   F CA    1 
ATOM   11474 C  C     . TRP   E 4  27  ? -2.269  51.098  63.042  1.00 42.94  ? 27  TRP   F C     1 
ATOM   11475 O  O     . TRP   E 4  27  ? -2.617  49.919  63.141  1.00 51.36  ? 27  TRP   F O     1 
ATOM   11476 C  CB    . TRP   E 4  27  ? -3.037  52.093  65.217  1.00 41.29  ? 27  TRP   F CB    1 
ATOM   11477 C  CG    . TRP   E 4  27  ? -3.348  53.399  65.856  1.00 42.17  ? 27  TRP   F CG    1 
ATOM   11478 C  CD1   . TRP   E 4  27  ? -4.588  53.943  66.062  1.00 40.38  ? 27  TRP   F CD1   1 
ATOM   11479 C  CD2   . TRP   E 4  27  ? -2.401  54.372  66.314  1.00 45.99  ? 27  TRP   F CD2   1 
ATOM   11480 N  NE1   . TRP   E 4  27  ? -4.468  55.189  66.641  1.00 43.54  ? 27  TRP   F NE1   1 
ATOM   11481 C  CE2   . TRP   E 4  27  ? -3.137  55.476  66.805  1.00 46.41  ? 27  TRP   F CE2   1 
ATOM   11482 C  CE3   . TRP   E 4  27  ? -1.005  54.415  66.363  1.00 40.64  ? 27  TRP   F CE3   1 
ATOM   11483 C  CZ2   . TRP   E 4  27  ? -2.517  56.609  67.338  1.00 40.24  ? 27  TRP   F CZ2   1 
ATOM   11484 C  CZ3   . TRP   E 4  27  ? -0.396  55.534  66.892  1.00 39.18  ? 27  TRP   F CZ3   1 
ATOM   11485 C  CH2   . TRP   E 4  27  ? -1.150  56.618  67.372  1.00 41.23  ? 27  TRP   F CH2   1 
ATOM   11486 N  N     . LYS   E 4  28  ? -1.192  51.493  62.356  1.00 40.91  ? 28  LYS   F N     1 
ATOM   11487 C  CA    . LYS   E 4  28  ? -0.169  50.570  61.877  1.00 43.38  ? 28  LYS   F CA    1 
ATOM   11488 C  C     . LYS   E 4  28  ? 1.073   50.696  62.757  1.00 47.87  ? 28  LYS   F C     1 
ATOM   11489 O  O     . LYS   E 4  28  ? 1.373   51.774  63.276  1.00 52.10  ? 28  LYS   F O     1 
ATOM   11490 C  CB    . LYS   E 4  28  ? 0.199   50.843  60.410  1.00 47.54  ? 28  LYS   F CB    1 
ATOM   11491 C  CG    . LYS   E 4  28  ? 0.868   49.631  59.694  1.00 70.51  ? 28  LYS   F CG    1 
ATOM   11492 C  CD    . LYS   E 4  28  ? 2.285   49.891  59.091  1.00 61.53  ? 28  LYS   F CD    1 
ATOM   11493 C  CE    . LYS   E 4  28  ? 2.980   48.567  58.640  1.00 60.82  ? 28  LYS   F CE    1 
ATOM   11494 N  NZ    . LYS   E 4  28  ? 4.438   48.647  58.194  1.00 33.71  ? 28  LYS   F NZ    1 
ATOM   11495 N  N     . ARG   E 4  29  ? 1.796   49.586  62.932  1.00 48.98  ? 29  ARG   F N     1 
ATOM   11496 C  CA    . ARG   E 4  29  ? 3.051   49.589  63.685  1.00 43.46  ? 29  ARG   F CA    1 
ATOM   11497 C  C     . ARG   E 4  29  ? 4.225   49.542  62.708  1.00 42.59  ? 29  ARG   F C     1 
ATOM   11498 O  O     . ARG   E 4  29  ? 4.445   48.539  62.021  1.00 44.32  ? 29  ARG   F O     1 
ATOM   11499 C  CB    . ARG   E 4  29  ? 3.135   48.426  64.672  1.00 39.82  ? 29  ARG   F CB    1 
ATOM   11500 C  CG    . ARG   E 4  29  ? 4.529   48.312  65.327  1.00 39.05  ? 29  ARG   F CG    1 
ATOM   11501 C  CD    . ARG   E 4  29  ? 4.619   47.171  66.352  1.00 44.24  ? 29  ARG   F CD    1 
ATOM   11502 N  NE    . ARG   E 4  29  ? 5.991   46.899  66.777  1.00 43.90  ? 29  ARG   F NE    1 
ATOM   11503 C  CZ    . ARG   E 4  29  ? 6.327   46.055  67.746  1.00 38.40  ? 29  ARG   F CZ    1 
ATOM   11504 N  NH1   . ARG   E 4  29  ? 5.411   45.396  68.435  1.00 44.81  ? 29  ARG   F NH1   1 
ATOM   11505 N  NH2   . ARG   E 4  29  ? 7.614   45.868  68.032  1.00 44.26  ? 29  ARG   F NH2   1 
ATOM   11506 N  N     . LEU   E 4  30  ? 4.980   50.629  62.660  1.00 45.48  ? 30  LEU   F N     1 
ATOM   11507 C  CA    . LEU   E 4  30  ? 6.183   50.715  61.856  1.00 43.23  ? 30  LEU   F CA    1 
ATOM   11508 C  C     . LEU   E 4  30  ? 7.290   49.923  62.539  1.00 47.48  ? 30  LEU   F C     1 
ATOM   11509 O  O     . LEU   E 4  30  ? 7.115   49.392  63.639  1.00 50.94  ? 30  LEU   F O     1 
ATOM   11510 C  CB    . LEU   E 4  30  ? 6.581   52.179  61.654  1.00 35.42  ? 30  LEU   F CB    1 
ATOM   11511 C  CG    . LEU   E 4  30  ? 5.472   53.152  61.222  1.00 33.96  ? 30  LEU   F CG    1 
ATOM   11512 C  CD1   . LEU   E 4  30  ? 5.952   54.582  61.208  1.00 33.89  ? 30  LEU   F CD1   1 
ATOM   11513 C  CD2   . LEU   E 4  30  ? 4.921   52.783  59.867  1.00 41.19  ? 30  LEU   F CD2   1 
ATOM   11514 N  N     . ARG   E 4  31  ? 8.448   49.840  61.888  1.00 46.31  ? 31  ARG   F N     1 
ATOM   11515 C  CA    . ARG   E 4  31  ? 9.612   49.242  62.523  1.00 51.70  ? 31  ARG   F CA    1 
ATOM   11516 C  C     . ARG   E 4  31  ? 10.351  50.294  63.347  1.00 53.98  ? 31  ARG   F C     1 
ATOM   11517 O  O     . ARG   E 4  31  ? 10.649  51.387  62.852  1.00 57.77  ? 31  ARG   F O     1 
ATOM   11518 C  CB    . ARG   E 4  31  ? 10.542  48.616  61.481  1.00 57.04  ? 31  ARG   F CB    1 
ATOM   11519 C  CG    . ARG   E 4  31  ? 11.862  48.085  62.068  1.00 70.20  ? 31  ARG   F CG    1 
ATOM   11520 C  CD    . ARG   E 4  31  ? 11.679  47.462  63.475  1.00 67.60  ? 31  ARG   F CD    1 
ATOM   11521 N  NE    . ARG   E 4  31  ? 11.392  46.031  63.452  1.00 76.24  ? 31  ARG   F NE    1 
ATOM   11522 C  CZ    . ARG   E 4  31  ? 10.892  45.346  64.476  1.00 84.52  ? 31  ARG   F CZ    1 
ATOM   11523 N  NH1   . ARG   E 4  31  ? 10.581  45.938  65.621  1.00 71.78  ? 31  ARG   F NH1   1 
ATOM   11524 N  NH2   . ARG   E 4  31  ? 10.700  44.033  64.347  1.00 82.95  ? 31  ARG   F NH2   1 
ATOM   11525 N  N     . LYS   E 4  32  ? 10.649  49.947  64.604  1.00 48.34  ? 32  LYS   F N     1 
ATOM   11526 C  CA    . LYS   E 4  32  ? 11.295  50.789  65.613  1.00 50.03  ? 32  LYS   F CA    1 
ATOM   11527 C  C     . LYS   E 4  32  ? 12.185  51.899  65.058  1.00 56.59  ? 32  LYS   F C     1 
ATOM   11528 O  O     . LYS   E 4  32  ? 12.221  53.003  65.615  1.00 55.37  ? 32  LYS   F O     1 
ATOM   11529 C  CB    . LYS   E 4  32  ? 12.130  49.913  66.558  1.00 54.12  ? 32  LYS   F CB    1 
ATOM   11530 C  CG    . LYS   E 4  32  ? 13.364  49.302  65.892  1.00 65.71  ? 32  LYS   F CG    1 
ATOM   11531 C  CD    . LYS   E 4  32  ? 14.532  49.113  66.867  1.00 67.27  ? 32  LYS   F CD    1 
ATOM   11532 C  CE    . LYS   E 4  32  ? 15.897  49.281  66.170  1.00 65.15  ? 32  LYS   F CE    1 
ATOM   11533 N  NZ    . LYS   E 4  32  ? 16.089  50.635  65.546  1.00 50.77  ? 32  LYS   F NZ    1 
ATOM   11534 N  N     . ASP   E 4  33  ? 12.923  51.612  63.983  1.00 55.44  ? 33  ASP   F N     1 
ATOM   11535 C  CA    . ASP   E 4  33  ? 13.864  52.552  63.386  1.00 50.48  ? 33  ASP   F CA    1 
ATOM   11536 C  C     . ASP   E 4  33  ? 13.233  53.432  62.308  1.00 50.90  ? 33  ASP   F C     1 
ATOM   11537 O  O     . ASP   E 4  33  ? 13.911  54.331  61.780  1.00 40.58  ? 33  ASP   F O     1 
ATOM   11538 C  CB    . ASP   E 4  33  ? 15.043  51.782  62.781  1.00 68.03  ? 33  ASP   F CB    1 
ATOM   11539 C  CG    . ASP   E 4  33  ? 16.400  52.383  63.139  1.00 71.19  ? 33  ASP   F CG    1 
ATOM   11540 O  OD1   . ASP   E 4  33  ? 16.474  53.218  64.073  1.00 53.48  ? 33  ASP   F OD1   1 
ATOM   11541 O  OD2   . ASP   E 4  33  ? 17.401  52.004  62.479  1.00 84.34  ? 33  ASP   F OD2   1 
ATOM   11542 N  N     . ASN   E 4  34  ? 11.974  53.183  61.949  1.00 49.36  ? 34  ASN   F N     1 
ATOM   11543 C  CA    . ASN   E 4  34  ? 11.288  54.065  61.016  1.00 45.75  ? 34  ASN   F CA    1 
ATOM   11544 C  C     . ASN   E 4  34  ? 10.902  55.342  61.745  1.00 47.41  ? 34  ASN   F C     1 
ATOM   11545 O  O     . ASN   E 4  34  ? 10.184  55.279  62.749  1.00 50.93  ? 34  ASN   F O     1 
ATOM   11546 C  CB    . ASN   E 4  34  ? 10.058  53.399  60.425  1.00 42.12  ? 34  ASN   F CB    1 
ATOM   11547 C  CG    . ASN   E 4  34  ? 9.378   54.256  59.360  1.00 37.98  ? 34  ASN   F CG    1 
ATOM   11548 O  OD1   . ASN   E 4  34  ? 8.172   54.152  59.155  1.00 41.96  ? 34  ASN   F OD1   1 
ATOM   11549 N  ND2   . ASN   E 4  34  ? 10.149  55.094  58.673  1.00 46.83  ? 34  ASN   F ND2   1 
ATOM   11550 N  N     . PRO   E 4  35  ? 11.375  56.507  61.305  1.00 45.87  ? 35  PRO   F N     1 
ATOM   11551 C  CA    . PRO   E 4  35  ? 11.104  57.742  62.046  1.00 37.32  ? 35  PRO   F CA    1 
ATOM   11552 C  C     . PRO   E 4  35  ? 9.725   58.332  61.799  1.00 42.02  ? 35  PRO   F C     1 
ATOM   11553 O  O     . PRO   E 4  35  ? 9.332   59.257  62.526  1.00 36.84  ? 35  PRO   F O     1 
ATOM   11554 C  CB    . PRO   E 4  35  ? 12.205  58.679  61.535  1.00 39.86  ? 35  PRO   F CB    1 
ATOM   11555 C  CG    . PRO   E 4  35  ? 12.470  58.210  60.152  1.00 33.41  ? 35  PRO   F CG    1 
ATOM   11556 C  CD    . PRO   E 4  35  ? 12.281  56.728  60.160  1.00 37.10  ? 35  PRO   F CD    1 
ATOM   11557 N  N     . ARG   E 4  36  ? 8.986   57.831  60.811  1.00 43.98  ? 36  ARG   F N     1 
ATOM   11558 C  CA    . ARG   E 4  36  ? 7.770   58.487  60.332  1.00 39.98  ? 36  ARG   F CA    1 
ATOM   11559 C  C     . ARG   E 4  36  ? 6.529   58.074  61.121  1.00 44.70  ? 36  ARG   F C     1 
ATOM   11560 O  O     . ARG   E 4  36  ? 5.467   57.779  60.551  1.00 48.43  ? 36  ARG   F O     1 
ATOM   11561 C  CB    . ARG   E 4  36  ? 7.604   58.213  58.844  1.00 32.20  ? 36  ARG   F CB    1 
ATOM   11562 C  CG    . ARG   E 4  36  ? 8.441   59.136  58.031  1.00 39.69  ? 36  ARG   F CG    1 
ATOM   11563 C  CD    . ARG   E 4  36  ? 8.636   58.705  56.586  1.00 50.58  ? 36  ARG   F CD    1 
ATOM   11564 N  NE    . ARG   E 4  36  ? 9.636   59.577  55.983  1.00 42.82  ? 36  ARG   F NE    1 
ATOM   11565 C  CZ    . ARG   E 4  36  ? 9.459   60.878  55.798  1.00 44.46  ? 36  ARG   F CZ    1 
ATOM   11566 N  NH1   . ARG   E 4  36  ? 8.284   61.448  56.021  1.00 44.38  ? 36  ARG   F NH1   1 
ATOM   11567 N  NH2   . ARG   E 4  36  ? 10.491  61.629  55.397  1.00 38.18  ? 36  ARG   F NH2   1 
ATOM   11568 N  N     . PHE   E 4  37  ? 6.655   58.097  62.450  1.00 40.03  ? 37  PHE   F N     1 
ATOM   11569 C  CA    . PHE   E 4  37  ? 5.627   57.644  63.376  1.00 37.86  ? 37  PHE   F CA    1 
ATOM   11570 C  C     . PHE   E 4  37  ? 4.912   58.825  64.029  1.00 39.91  ? 37  PHE   F C     1 
ATOM   11571 O  O     . PHE   E 4  37  ? 5.465   59.925  64.145  1.00 33.37  ? 37  PHE   F O     1 
ATOM   11572 C  CB    . PHE   E 4  37  ? 6.253   56.782  64.460  1.00 33.35  ? 37  PHE   F CB    1 
ATOM   11573 C  CG    . PHE   E 4  37  ? 7.235   57.525  65.286  1.00 33.54  ? 37  PHE   F CG    1 
ATOM   11574 C  CD1   . PHE   E 4  37  ? 6.829   58.240  66.401  1.00 34.65  ? 37  PHE   F CD1   1 
ATOM   11575 C  CD2   . PHE   E 4  37  ? 8.565   57.549  64.940  1.00 37.32  ? 37  PHE   F CD2   1 
ATOM   11576 C  CE1   . PHE   E 4  37  ? 7.745   58.951  67.171  1.00 29.26  ? 37  PHE   F CE1   1 
ATOM   11577 C  CE2   . PHE   E 4  37  ? 9.484   58.258  65.715  1.00 32.66  ? 37  PHE   F CE2   1 
ATOM   11578 C  CZ    . PHE   E 4  37  ? 9.065   58.954  66.828  1.00 20.60  ? 37  PHE   F CZ    1 
ATOM   11579 N  N     . ASN   E 4  38  ? 3.668   58.579  64.474  1.00 33.10  ? 38  ASN   F N     1 
ATOM   11580 C  CA    . ASN   E 4  38  ? 2.973   59.542  65.325  1.00 29.16  ? 38  ASN   F CA    1 
ATOM   11581 C  C     . ASN   E 4  38  ? 3.220   59.281  66.797  1.00 33.41  ? 38  ASN   F C     1 
ATOM   11582 O  O     . ASN   E 4  38  ? 3.318   60.222  67.589  1.00 41.67  ? 38  ASN   F O     1 
ATOM   11583 C  CB    . ASN   E 4  38  ? 1.461   59.503  65.118  1.00 37.22  ? 38  ASN   F CB    1 
ATOM   11584 C  CG    . ASN   E 4  38  ? 1.054   59.792  63.715  1.00 38.83  ? 38  ASN   F CG    1 
ATOM   11585 O  OD1   . ASN   E 4  38  ? 0.788   58.869  62.935  1.00 38.07  ? 38  ASN   F OD1   1 
ATOM   11586 N  ND2   . ASN   E 4  38  ? 0.970   61.082  63.378  1.00 30.79  ? 38  ASN   F ND2   1 
ATOM   11587 N  N     . LEU   E 4  39  ? 3.273   58.016  67.185  1.00 31.90  ? 39  LEU   F N     1 
ATOM   11588 C  CA    . LEU   E 4  39  ? 3.348   57.627  68.581  1.00 30.52  ? 39  LEU   F CA    1 
ATOM   11589 C  C     . LEU   E 4  39  ? 4.584   56.764  68.803  1.00 34.77  ? 39  LEU   F C     1 
ATOM   11590 O  O     . LEU   E 4  39  ? 4.868   55.859  68.011  1.00 41.27  ? 39  LEU   F O     1 
ATOM   11591 C  CB    . LEU   E 4  39  ? 2.081   56.875  68.993  1.00 27.36  ? 39  LEU   F CB    1 
ATOM   11592 C  CG    . LEU   E 4  39  ? 2.169   56.262  70.383  1.00 30.80  ? 39  LEU   F CG    1 
ATOM   11593 C  CD1   . LEU   E 4  39  ? 1.886   57.333  71.444  1.00 33.62  ? 39  LEU   F CD1   1 
ATOM   11594 C  CD2   . LEU   E 4  39  ? 1.231   55.078  70.533  1.00 36.20  ? 39  LEU   F CD2   1 
ATOM   11595 N  N     . MET   E 4  40  ? 5.328   57.050  69.863  1.00 27.01  ? 40  MET   F N     1 
ATOM   11596 C  CA    . MET   E 4  40  ? 6.475   56.240  70.236  1.00 24.08  ? 40  MET   F CA    1 
ATOM   11597 C  C     . MET   E 4  40  ? 6.213   55.678  71.616  1.00 33.11  ? 40  MET   F C     1 
ATOM   11598 O  O     . MET   E 4  40  ? 6.217   56.416  72.607  1.00 33.64  ? 40  MET   F O     1 
ATOM   11599 C  CB    . MET   E 4  40  ? 7.777   57.028  70.220  1.00 27.86  ? 40  MET   F CB    1 
ATOM   11600 C  CG    . MET   E 4  40  ? 8.853   56.410  71.098  1.00 21.38  ? 40  MET   F CG    1 
ATOM   11601 S  SD    . MET   E 4  40  ? 10.501  57.004  70.666  1.00 22.43  ? 40  MET   F SD    1 
ATOM   11602 C  CE    . MET   E 4  40  ? 11.260  56.929  72.300  1.00 38.85  ? 40  MET   F CE    1 
ATOM   11603 N  N     . LEU   E 4  41  ? 6.006   54.372  71.675  1.00 42.01  ? 41  LEU   F N     1 
ATOM   11604 C  CA    . LEU   E 4  41  ? 5.852   53.683  72.940  1.00 38.34  ? 41  LEU   F CA    1 
ATOM   11605 C  C     . LEU   E 4  41  ? 7.184   53.439  73.646  1.00 40.88  ? 41  LEU   F C     1 
ATOM   11606 O  O     . LEU   E 4  41  ? 7.208   52.711  74.642  1.00 57.20  ? 41  LEU   F O     1 
ATOM   11607 C  CB    . LEU   E 4  41  ? 5.090   52.388  72.707  1.00 36.31  ? 41  LEU   F CB    1 
ATOM   11608 C  CG    . LEU   E 4  41  ? 3.724   52.732  72.117  1.00 31.61  ? 41  LEU   F CG    1 
ATOM   11609 C  CD1   . LEU   E 4  41  ? 2.906   51.474  71.868  1.00 45.48  ? 41  LEU   F CD1   1 
ATOM   11610 C  CD2   . LEU   E 4  41  ? 3.002   53.681  73.024  1.00 27.91  ? 41  LEU   F CD2   1 
ATOM   11611 N  N     . GLY   E 4  42  ? 8.279   54.006  73.138  1.00 34.93  ? 42  GLY   F N     1 
ATOM   11612 C  CA    . GLY   E 4  42  ? 9.424   54.453  73.930  1.00 38.67  ? 42  GLY   F CA    1 
ATOM   11613 C  C     . GLY   E 4  42  ? 10.125  53.549  74.929  1.00 35.90  ? 42  GLY   F C     1 
ATOM   11614 O  O     . GLY   E 4  42  ? 9.490   52.889  75.754  1.00 43.14  ? 42  GLY   F O     1 
ATOM   11615 N  N     . GLU   E 4  43  ? 11.450  53.552  74.901  1.00 32.39  ? 43  GLU   F N     1 
ATOM   11616 C  CA    . GLU   E 4  43  ? 12.208  52.620  75.718  1.00 40.72  ? 43  GLU   F CA    1 
ATOM   11617 C  C     . GLU   E 4  43  ? 12.341  53.124  77.157  1.00 45.88  ? 43  GLU   F C     1 
ATOM   11618 O  O     . GLU   E 4  43  ? 12.051  54.281  77.468  1.00 51.89  ? 43  GLU   F O     1 
ATOM   11619 C  CB    . GLU   E 4  43  ? 13.582  52.357  75.094  1.00 36.60  ? 43  GLU   F CB    1 
ATOM   11620 C  CG    . GLU   E 4  43  ? 14.455  53.566  74.857  1.00 36.95  ? 43  GLU   F CG    1 
ATOM   11621 C  CD    . GLU   E 4  43  ? 14.579  53.944  73.382  1.00 38.29  ? 43  GLU   F CD    1 
ATOM   11622 O  OE1   . GLU   E 4  43  ? 13.535  54.028  72.697  1.00 38.63  ? 43  GLU   F OE1   1 
ATOM   11623 O  OE2   . GLU   E 4  43  ? 15.722  54.166  72.915  1.00 33.55  ? 43  GLU   F OE2   1 
ATOM   11624 N  N     . ARG   E 4  44  ? 12.766  52.226  78.051  1.00 55.74  ? 44  ARG   F N     1 
ATOM   11625 C  CA    . ARG   E 4  44  ? 12.804  52.607  79.460  1.00 61.22  ? 44  ARG   F CA    1 
ATOM   11626 C  C     . ARG   E 4  44  ? 14.021  53.466  79.776  1.00 54.45  ? 44  ARG   F C     1 
ATOM   11627 O  O     . ARG   E 4  44  ? 13.939  54.374  80.613  1.00 69.00  ? 44  ARG   F O     1 
ATOM   11628 C  CB    . ARG   E 4  44  ? 12.773  51.367  80.364  1.00 61.96  ? 44  ARG   F CB    1 
ATOM   11629 C  CG    . ARG   E 4  44  ? 12.127  51.599  81.763  1.00 82.49  ? 44  ARG   F CG    1 
ATOM   11630 C  CD    . ARG   E 4  44  ? 12.891  52.646  82.643  1.00 93.96  ? 44  ARG   F CD    1 
ATOM   11631 N  NE    . ARG   E 4  44  ? 12.630  52.524  84.080  1.00 85.50  ? 44  ARG   F NE    1 
ATOM   11632 C  CZ    . ARG   E 4  44  ? 11.890  53.370  84.790  1.00 90.00  ? 44  ARG   F CZ    1 
ATOM   11633 N  NH1   . ARG   E 4  44  ? 11.286  54.407  84.220  1.00 78.56  ? 44  ARG   F NH1   1 
ATOM   11634 N  NH2   . ARG   E 4  44  ? 11.763  53.179  86.106  1.00 80.99  ? 44  ARG   F NH2   1 
ATOM   11635 N  N     . ASN   E 4  45  ? 15.148  53.208  79.129  1.00 45.43  ? 45  ASN   F N     1 
ATOM   11636 C  CA    . ASN   E 4  45  ? 16.380  53.899  79.474  1.00 54.78  ? 45  ASN   F CA    1 
ATOM   11637 C  C     . ASN   E 4  45  ? 17.002  54.556  78.244  1.00 48.40  ? 45  ASN   F C     1 
ATOM   11638 O  O     . ASN   E 4  45  ? 16.994  53.997  77.144  1.00 38.95  ? 45  ASN   F O     1 
ATOM   11639 C  CB    . ASN   E 4  45  ? 17.378  52.934  80.136  1.00 59.57  ? 45  ASN   F CB    1 
ATOM   11640 C  CG    . ASN   E 4  45  ? 18.325  53.643  81.080  1.00 71.27  ? 45  ASN   F CG    1 
ATOM   11641 O  OD1   . ASN   E 4  45  ? 17.912  54.520  81.840  1.00 79.66  ? 45  ASN   F OD1   1 
ATOM   11642 N  ND2   . ASN   E 4  45  ? 19.601  53.274  81.035  1.00 61.56  ? 45  ASN   F ND2   1 
ATOM   11643 N  N     . ARG   E 4  46  ? 17.551  55.749  78.443  1.00 51.88  ? 46  ARG   F N     1 
ATOM   11644 C  CA    . ARG   E 4  46  ? 18.159  56.516  77.359  1.00 40.59  ? 46  ARG   F CA    1 
ATOM   11645 C  C     . ARG   E 4  46  ? 17.228  56.595  76.152  1.00 42.49  ? 46  ARG   F C     1 
ATOM   11646 O  O     . ARG   E 4  46  ? 17.638  56.408  75.004  1.00 44.38  ? 46  ARG   F O     1 
ATOM   11647 C  CB    . ARG   E 4  46  ? 19.516  55.936  76.971  1.00 49.26  ? 46  ARG   F CB    1 
ATOM   11648 C  CG    . ARG   E 4  46  ? 20.414  55.559  78.162  1.00 62.03  ? 46  ARG   F CG    1 
ATOM   11649 C  CD    . ARG   E 4  46  ? 21.885  55.762  77.817  1.00 56.51  ? 46  ARG   F CD    1 
ATOM   11650 N  NE    . ARG   E 4  46  ? 22.172  57.175  77.597  1.00 65.97  ? 46  ARG   F NE    1 
ATOM   11651 C  CZ    . ARG   E 4  46  ? 23.146  57.647  76.831  1.00 63.98  ? 46  ARG   F CZ    1 
ATOM   11652 N  NH1   . ARG   E 4  46  ? 23.942  56.841  76.147  1.00 75.81  ? 46  ARG   F NH1   1 
ATOM   11653 N  NH2   . ARG   E 4  46  ? 23.323  58.961  76.747  1.00 54.30  ? 46  ARG   F NH2   1 
ATOM   11654 N  N     . LEU   E 4  47  ? 15.957  56.872  76.420  1.00 42.87  ? 47  LEU   F N     1 
ATOM   11655 C  CA    . LEU   E 4  47  ? 14.996  57.134  75.359  1.00 32.65  ? 47  LEU   F CA    1 
ATOM   11656 C  C     . LEU   E 4  47  ? 15.377  58.439  74.668  1.00 33.63  ? 47  LEU   F C     1 
ATOM   11657 O  O     . LEU   E 4  47  ? 15.612  59.443  75.350  1.00 41.17  ? 47  LEU   F O     1 
ATOM   11658 C  CB    . LEU   E 4  47  ? 13.582  57.207  75.948  1.00 32.45  ? 47  LEU   F CB    1 
ATOM   11659 C  CG    . LEU   E 4  47  ? 12.344  57.586  75.126  1.00 35.59  ? 47  LEU   F CG    1 
ATOM   11660 C  CD1   . LEU   E 4  47  ? 11.058  57.320  75.907  1.00 25.22  ? 47  LEU   F CD1   1 
ATOM   11661 C  CD2   . LEU   E 4  47  ? 12.386  59.034  74.629  1.00 31.22  ? 47  LEU   F CD2   1 
ATOM   11662 N  N     . PRO   E 4  48  ? 15.450  58.473  73.338  1.00 36.80  ? 48  PRO   F N     1 
ATOM   11663 C  CA    . PRO   E 4  48  ? 16.076  59.615  72.620  1.00 34.87  ? 48  PRO   F CA    1 
ATOM   11664 C  C     . PRO   E 4  48  ? 15.165  60.828  72.451  1.00 34.68  ? 48  PRO   F C     1 
ATOM   11665 O  O     . PRO   E 4  48  ? 14.792  61.239  71.327  1.00 32.54  ? 48  PRO   F O     1 
ATOM   11666 C  CB    . PRO   E 4  48  ? 16.454  58.981  71.277  1.00 35.38  ? 48  PRO   F CB    1 
ATOM   11667 C  CG    . PRO   E 4  48  ? 15.387  57.963  71.056  1.00 35.93  ? 48  PRO   F CG    1 
ATOM   11668 C  CD    . PRO   E 4  48  ? 15.006  57.414  72.415  1.00 36.53  ? 48  PRO   F CD    1 
ATOM   11669 N  N     . PHE   E 4  49  ? 14.802  61.443  73.584  1.00 33.76  ? 49  PHE   F N     1 
ATOM   11670 C  CA    . PHE   E 4  49  ? 13.919  62.610  73.556  1.00 29.52  ? 49  PHE   F CA    1 
ATOM   11671 C  C     . PHE   E 4  49  ? 14.419  63.667  72.578  1.00 30.45  ? 49  PHE   F C     1 
ATOM   11672 O  O     . PHE   E 4  49  ? 13.618  64.355  71.930  1.00 36.22  ? 49  PHE   F O     1 
ATOM   11673 C  CB    . PHE   E 4  49  ? 13.775  63.210  74.966  1.00 30.14  ? 49  PHE   F CB    1 
ATOM   11674 C  CG    . PHE   E 4  49  ? 12.882  62.413  75.888  1.00 28.51  ? 49  PHE   F CG    1 
ATOM   11675 C  CD1   . PHE   E 4  49  ? 11.515  62.427  75.725  1.00 23.39  ? 49  PHE   F CD1   1 
ATOM   11676 C  CD2   . PHE   E 4  49  ? 13.418  61.649  76.906  1.00 27.32  ? 49  PHE   F CD2   1 
ATOM   11677 C  CE1   . PHE   E 4  49  ? 10.708  61.685  76.552  1.00 27.56  ? 49  PHE   F CE1   1 
ATOM   11678 C  CE2   . PHE   E 4  49  ? 12.616  60.913  77.734  1.00 25.24  ? 49  PHE   F CE2   1 
ATOM   11679 C  CZ    . PHE   E 4  49  ? 11.258  60.928  77.566  1.00 27.93  ? 49  PHE   F CZ    1 
ATOM   11680 N  N     . GLY   E 4  50  ? 15.740  63.806  72.449  1.00 27.74  ? 50  GLY   F N     1 
ATOM   11681 C  CA    . GLY   E 4  50  ? 16.280  64.840  71.585  1.00 29.92  ? 50  GLY   F CA    1 
ATOM   11682 C  C     . GLY   E 4  50  ? 15.764  64.774  70.162  1.00 25.53  ? 50  GLY   F C     1 
ATOM   11683 O  O     . GLY   E 4  50  ? 15.724  65.795  69.464  1.00 21.66  ? 50  GLY   F O     1 
ATOM   11684 N  N     . ARG   E 4  51  ? 15.366  63.575  69.719  1.00 24.68  ? 51  ARG   F N     1 
ATOM   11685 C  CA    . ARG   E 4  51  ? 15.009  63.281  68.340  1.00 27.25  ? 51  ARG   F CA    1 
ATOM   11686 C  C     . ARG   E 4  51  ? 13.521  63.408  68.083  1.00 30.10  ? 51  ARG   F C     1 
ATOM   11687 O  O     . ARG   E 4  51  ? 13.093  63.282  66.931  1.00 30.78  ? 51  ARG   F O     1 
ATOM   11688 C  CB    . ARG   E 4  51  ? 15.464  61.864  67.960  1.00 25.56  ? 51  ARG   F CB    1 
ATOM   11689 C  CG    . ARG   E 4  51  ? 16.965  61.604  68.171  1.00 33.47  ? 51  ARG   F CG    1 
ATOM   11690 C  CD    . ARG   E 4  51  ? 17.575  60.760  67.047  1.00 28.52  ? 51  ARG   F CD    1 
ATOM   11691 N  NE    . ARG   E 4  51  ? 17.058  59.396  67.014  1.00 32.94  ? 51  ARG   F NE    1 
ATOM   11692 C  CZ    . ARG   E 4  51  ? 17.481  58.425  67.813  1.00 37.26  ? 51  ARG   F CZ    1 
ATOM   11693 N  NH1   . ARG   E 4  51  ? 18.410  58.645  68.729  1.00 43.64  ? 51  ARG   F NH1   1 
ATOM   11694 N  NH2   . ARG   E 4  51  ? 16.955  57.207  67.697  1.00 32.57  ? 51  ARG   F NH2   1 
ATOM   11695 N  N     . LEU   E 4  52  ? 12.728  63.645  69.121  1.00 28.90  ? 52  LEU   F N     1 
ATOM   11696 C  CA    . LEU   E 4  52  ? 11.288  63.676  68.963  1.00 25.10  ? 52  LEU   F CA    1 
ATOM   11697 C  C     . LEU   E 4  52  ? 10.849  65.047  68.453  1.00 22.66  ? 52  LEU   F C     1 
ATOM   11698 O  O     . LEU   E 4  52  ? 11.559  66.049  68.571  1.00 28.08  ? 52  LEU   F O     1 
ATOM   11699 C  CB    . LEU   E 4  52  ? 10.595  63.315  70.289  1.00 20.22  ? 52  LEU   F CB    1 
ATOM   11700 C  CG    . LEU   E 4  52  ? 10.763  61.857  70.759  1.00 22.86  ? 52  LEU   F CG    1 
ATOM   11701 C  CD1   . LEU   E 4  52  ? 10.370  61.704  72.208  1.00 24.68  ? 52  LEU   F CD1   1 
ATOM   11702 C  CD2   . LEU   E 4  52  ? 10.014  60.830  69.879  1.00 15.83  ? 52  LEU   F CD2   1 
ATOM   11703 N  N     . GLY   E 4  53  ? 9.672   65.076  67.848  1.00 17.48  ? 53  GLY   F N     1 
ATOM   11704 C  CA    . GLY   E 4  53  ? 9.149   66.341  67.402  1.00 19.40  ? 53  GLY   F CA    1 
ATOM   11705 C  C     . GLY   E 4  53  ? 9.992   67.073  66.384  1.00 25.79  ? 53  GLY   F C     1 
ATOM   11706 O  O     . GLY   E 4  53  ? 10.126  68.296  66.477  1.00 30.13  ? 53  GLY   F O     1 
ATOM   11707 N  N     . HIS   E 4  54  ? 10.532  66.371  65.376  1.00 32.77  ? 54  HIS   F N     1 
ATOM   11708 C  CA    . HIS   E 4  54  ? 11.140  67.089  64.263  1.00 26.59  ? 54  HIS   F CA    1 
ATOM   11709 C  C     . HIS   E 4  54  ? 10.630  66.695  62.870  1.00 39.78  ? 54  HIS   F C     1 
ATOM   11710 O  O     . HIS   E 4  54  ? 10.902  67.431  61.915  1.00 43.73  ? 54  HIS   F O     1 
ATOM   11711 C  CB    . HIS   E 4  54  ? 12.672  66.967  64.311  1.00 24.77  ? 54  HIS   F CB    1 
ATOM   11712 C  CG    . HIS   E 4  54  ? 13.309  67.688  65.469  1.00 27.41  ? 54  HIS   F CG    1 
ATOM   11713 N  ND1   . HIS   E 4  54  ? 13.660  69.021  65.420  1.00 26.36  ? 54  HIS   F ND1   1 
ATOM   11714 C  CD2   . HIS   E 4  54  ? 13.670  67.253  66.702  1.00 28.25  ? 54  HIS   F CD2   1 
ATOM   11715 C  CE1   . HIS   E 4  54  ? 14.192  69.376  66.578  1.00 31.83  ? 54  HIS   F CE1   1 
ATOM   11716 N  NE2   . HIS   E 4  54  ? 14.222  68.319  67.370  1.00 28.01  ? 54  HIS   F NE2   1 
ATOM   11717 N  N     . GLU   E 4  55  ? 9.874   65.606  62.720  1.00 36.16  ? 55  GLU   F N     1 
ATOM   11718 C  CA    . GLU   E 4  55  ? 9.304   65.230  61.411  1.00 25.03  ? 55  GLU   F CA    1 
ATOM   11719 C  C     . GLU   E 4  55  ? 8.191   66.175  60.970  1.00 35.05  ? 55  GLU   F C     1 
ATOM   11720 O  O     . GLU   E 4  55  ? 7.108   66.144  61.568  1.00 44.92  ? 55  GLU   F O     1 
ATOM   11721 C  CB    . GLU   E 4  55  ? 8.727   63.822  61.481  1.00 29.19  ? 55  GLU   F CB    1 
ATOM   11722 C  CG    . GLU   E 4  55  ? 9.753   62.751  61.656  1.00 36.97  ? 55  GLU   F CG    1 
ATOM   11723 C  CD    . GLU   E 4  55  ? 10.804  62.827  60.577  1.00 43.55  ? 55  GLU   F CD    1 
ATOM   11724 O  OE1   . GLU   E 4  55  ? 10.564  63.540  59.559  1.00 38.47  ? 55  GLU   F OE1   1 
ATOM   11725 O  OE2   . GLU   E 4  55  ? 11.866  62.179  60.757  1.00 43.86  ? 55  GLU   F OE2   1 
ATOM   11726 N  N     . PRO   E 4  56  ? 8.370   66.999  59.941  1.00 37.05  ? 56  PRO   F N     1 
ATOM   11727 C  CA    . PRO   E 4  56  ? 7.216   67.766  59.451  1.00 32.09  ? 56  PRO   F CA    1 
ATOM   11728 C  C     . PRO   E 4  56  ? 6.099   66.840  58.961  1.00 34.51  ? 56  PRO   F C     1 
ATOM   11729 O  O     . PRO   E 4  56  ? 6.303   65.665  58.635  1.00 38.72  ? 56  PRO   F O     1 
ATOM   11730 C  CB    . PRO   E 4  56  ? 7.804   68.624  58.319  1.00 21.80  ? 56  PRO   F CB    1 
ATOM   11731 C  CG    . PRO   E 4  56  ? 9.174   68.032  58.028  1.00 22.52  ? 56  PRO   F CG    1 
ATOM   11732 C  CD    . PRO   E 4  56  ? 9.631   67.395  59.282  1.00 25.30  ? 56  PRO   F CD    1 
ATOM   11733 N  N     . GLY   E 4  57  ? 4.885   67.377  58.935  1.00 30.54  ? 57  GLY   F N     1 
ATOM   11734 C  CA    . GLY   E 4  57  ? 3.734   66.600  58.552  1.00 30.02  ? 57  GLY   F CA    1 
ATOM   11735 C  C     . GLY   E 4  57  ? 3.244   65.640  59.606  1.00 34.55  ? 57  GLY   F C     1 
ATOM   11736 O  O     . GLY   E 4  57  ? 2.082   65.225  59.555  1.00 30.69  ? 57  GLY   F O     1 
ATOM   11737 N  N     . LEU   E 4  58  ? 4.087   65.274  60.563  1.00 35.75  ? 58  LEU   F N     1 
ATOM   11738 C  CA    . LEU   E 4  58  ? 3.724   64.349  61.624  1.00 30.70  ? 58  LEU   F CA    1 
ATOM   11739 C  C     . LEU   E 4  58  ? 3.597   65.098  62.942  1.00 33.13  ? 58  LEU   F C     1 
ATOM   11740 O  O     . LEU   E 4  58  ? 4.398   65.985  63.243  1.00 26.64  ? 58  LEU   F O     1 
ATOM   11741 C  CB    . LEU   E 4  58  ? 4.765   63.244  61.780  1.00 30.59  ? 58  LEU   F CB    1 
ATOM   11742 C  CG    . LEU   E 4  58  ? 5.008   62.301  60.611  1.00 33.45  ? 58  LEU   F CG    1 
ATOM   11743 C  CD1   . LEU   E 4  58  ? 6.340   61.571  60.811  1.00 29.91  ? 58  LEU   F CD1   1 
ATOM   11744 C  CD2   . LEU   E 4  58  ? 3.854   61.331  60.501  1.00 29.14  ? 58  LEU   F CD2   1 
ATOM   11745 N  N     . VAL   E 4  59  ? 2.572   64.744  63.705  1.00 33.39  ? 59  VAL   F N     1 
ATOM   11746 C  CA    . VAL   E 4  59  ? 2.444   65.106  65.105  1.00 16.94  ? 59  VAL   F CA    1 
ATOM   11747 C  C     . VAL   E 4  59  ? 2.935   63.912  65.900  1.00 25.05  ? 59  VAL   F C     1 
ATOM   11748 O  O     . VAL   E 4  59  ? 2.523   62.777  65.638  1.00 38.33  ? 59  VAL   F O     1 
ATOM   11749 C  CB    . VAL   E 4  59  ? 0.989   65.455  65.440  1.00 20.68  ? 59  VAL   F CB    1 
ATOM   11750 C  CG1   . VAL   E 4  59  ? 0.763   65.519  66.925  1.00 16.50  ? 59  VAL   F CG1   1 
ATOM   11751 C  CG2   . VAL   E 4  59  ? 0.591   66.767  64.745  1.00 27.74  ? 59  VAL   F CG2   1 
ATOM   11752 N  N     . GLN   E 4  60  ? 3.833   64.147  66.845  1.00 26.11  ? 60  GLN   F N     1 
ATOM   11753 C  CA    . GLN   E 4  60  ? 4.484   63.057  67.550  1.00 23.19  ? 60  GLN   F CA    1 
ATOM   11754 C  C     . GLN   E 4  60  ? 4.223   63.091  69.054  1.00 30.81  ? 60  GLN   F C     1 
ATOM   11755 O  O     . GLN   E 4  60  ? 4.283   64.147  69.700  1.00 29.62  ? 60  GLN   F O     1 
ATOM   11756 C  CB    . GLN   E 4  60  ? 5.960   63.072  67.264  1.00 24.30  ? 60  GLN   F CB    1 
ATOM   11757 C  CG    . GLN   E 4  60  ? 6.288   62.778  65.807  1.00 28.57  ? 60  GLN   F CG    1 
ATOM   11758 C  CD    . GLN   E 4  60  ? 7.767   62.507  65.618  1.00 25.17  ? 60  GLN   F CD    1 
ATOM   11759 O  OE1   . GLN   E 4  60  ? 8.609   63.229  66.153  1.00 26.57  ? 60  GLN   F OE1   1 
ATOM   11760 N  NE2   . GLN   E 4  60  ? 8.092   61.455  64.884  1.00 23.42  ? 60  GLN   F NE2   1 
ATOM   11761 N  N     . LEU   E 4  61  ? 3.942   61.908  69.595  1.00 29.40  ? 61  LEU   F N     1 
ATOM   11762 C  CA    . LEU   E 4  61  ? 3.584   61.694  70.985  1.00 24.92  ? 61  LEU   F CA    1 
ATOM   11763 C  C     . LEU   E 4  61  ? 4.458   60.586  71.527  1.00 31.06  ? 61  LEU   F C     1 
ATOM   11764 O  O     . LEU   E 4  61  ? 4.657   59.577  70.851  1.00 37.16  ? 61  LEU   F O     1 
ATOM   11765 C  CB    . LEU   E 4  61  ? 2.123   61.294  71.099  1.00 28.73  ? 61  LEU   F CB    1 
ATOM   11766 C  CG    . LEU   E 4  61  ? 1.420   61.184  72.441  1.00 29.11  ? 61  LEU   F CG    1 
ATOM   11767 C  CD1   . LEU   E 4  61  ? 1.646   62.445  73.298  1.00 23.00  ? 61  LEU   F CD1   1 
ATOM   11768 C  CD2   . LEU   E 4  61  ? -0.056  60.951  72.133  1.00 29.45  ? 61  LEU   F CD2   1 
ATOM   11769 N  N     . VAL   E 4  62  ? 4.994   60.770  72.730  1.00 24.69  ? 62  VAL   F N     1 
ATOM   11770 C  CA    . VAL   E 4  62  ? 5.790   59.737  73.374  1.00 22.97  ? 62  VAL   F CA    1 
ATOM   11771 C  C     . VAL   E 4  62  ? 5.194   59.506  74.748  1.00 29.93  ? 62  VAL   F C     1 
ATOM   11772 O  O     . VAL   E 4  62  ? 4.604   60.410  75.342  1.00 36.15  ? 62  VAL   F O     1 
ATOM   11773 C  CB    . VAL   E 4  62  ? 7.282   60.113  73.469  1.00 26.78  ? 62  VAL   F CB    1 
ATOM   11774 C  CG1   . VAL   E 4  62  ? 7.450   61.353  74.311  1.00 24.27  ? 62  VAL   F CG1   1 
ATOM   11775 C  CG2   . VAL   E 4  62  ? 8.099   58.955  74.020  1.00 23.26  ? 62  VAL   F CG2   1 
ATOM   11776 N  N     . ASN   E 4  63  ? 5.337   58.281  75.249  1.00 31.78  ? 63  ASN   F N     1 
ATOM   11777 C  CA    . ASN   E 4  63  ? 4.651   57.845  76.459  1.00 28.30  ? 63  ASN   F CA    1 
ATOM   11778 C  C     . ASN   E 4  63  ? 5.522   57.985  77.704  1.00 37.00  ? 63  ASN   F C     1 
ATOM   11779 O  O     . ASN   E 4  63  ? 5.355   57.226  78.673  1.00 37.74  ? 63  ASN   F O     1 
ATOM   11780 C  CB    . ASN   E 4  63  ? 4.165   56.404  76.302  1.00 36.85  ? 63  ASN   F CB    1 
ATOM   11781 C  CG    . ASN   E 4  63  ? 5.311   55.383  76.245  1.00 40.21  ? 63  ASN   F CG    1 
ATOM   11782 O  OD1   . ASN   E 4  63  ? 6.470   55.718  75.967  1.00 36.12  ? 63  ASN   F OD1   1 
ATOM   11783 N  ND2   . ASN   E 4  63  ? 4.974   54.117  76.493  1.00 39.55  ? 63  ASN   F ND2   1 
ATOM   11784 N  N     . TYR   E 4  64  ? 6.435   58.960  77.704  1.00 34.19  ? 64  TYR   F N     1 
ATOM   11785 C  CA    . TYR   E 4  64  ? 7.204   59.319  78.884  1.00 28.55  ? 64  TYR   F CA    1 
ATOM   11786 C  C     . TYR   E 4  64  ? 7.397   60.823  78.936  1.00 29.58  ? 64  TYR   F C     1 
ATOM   11787 O  O     . TYR   E 4  64  ? 7.425   61.493  77.905  1.00 33.07  ? 64  TYR   F O     1 
ATOM   11788 C  CB    . TYR   E 4  64  ? 8.565   58.651  78.897  1.00 24.06  ? 64  TYR   F CB    1 
ATOM   11789 C  CG    . TYR   E 4  64  ? 8.489   57.196  79.234  1.00 31.10  ? 64  TYR   F CG    1 
ATOM   11790 C  CD1   . TYR   E 4  64  ? 8.188   56.260  78.261  1.00 30.31  ? 64  TYR   F CD1   1 
ATOM   11791 C  CD2   . TYR   E 4  64  ? 8.714   56.753  80.536  1.00 36.93  ? 64  TYR   F CD2   1 
ATOM   11792 C  CE1   . TYR   E 4  64  ? 8.110   54.917  78.567  1.00 37.06  ? 64  TYR   F CE1   1 
ATOM   11793 C  CE2   . TYR   E 4  64  ? 8.646   55.417  80.858  1.00 39.43  ? 64  TYR   F CE2   1 
ATOM   11794 C  CZ    . TYR   E 4  64  ? 8.344   54.499  79.865  1.00 42.95  ? 64  TYR   F CZ    1 
ATOM   11795 O  OH    . TYR   E 4  64  ? 8.279   53.156  80.163  1.00 43.73  ? 64  TYR   F OH    1 
ATOM   11796 N  N     . TYR   E 4  65  ? 7.528   61.348  80.155  1.00 33.38  ? 65  TYR   F N     1 
ATOM   11797 C  CA    . TYR   E 4  65  ? 7.928   62.734  80.393  1.00 28.21  ? 65  TYR   F CA    1 
ATOM   11798 C  C     . TYR   E 4  65  ? 9.422   62.796  80.707  1.00 21.95  ? 65  TYR   F C     1 
ATOM   11799 O  O     . TYR   E 4  65  ? 9.844   62.416  81.798  1.00 22.02  ? 65  TYR   F O     1 
ATOM   11800 C  CB    . TYR   E 4  65  ? 7.132   63.337  81.545  1.00 24.67  ? 65  TYR   F CB    1 
ATOM   11801 C  CG    . TYR   E 4  65  ? 5.806   63.913  81.161  1.00 26.20  ? 65  TYR   F CG    1 
ATOM   11802 C  CD1   . TYR   E 4  65  ? 5.710   65.201  80.650  1.00 28.52  ? 65  TYR   F CD1   1 
ATOM   11803 C  CD2   . TYR   E 4  65  ? 4.646   63.187  81.326  1.00 24.88  ? 65  TYR   F CD2   1 
ATOM   11804 C  CE1   . TYR   E 4  65  ? 4.488   65.743  80.311  1.00 25.89  ? 65  TYR   F CE1   1 
ATOM   11805 C  CE2   . TYR   E 4  65  ? 3.427   63.718  80.972  1.00 27.39  ? 65  TYR   F CE2   1 
ATOM   11806 C  CZ    . TYR   E 4  65  ? 3.355   64.996  80.475  1.00 22.24  ? 65  TYR   F CZ    1 
ATOM   11807 O  OH    . TYR   E 4  65  ? 2.136   65.519  80.142  1.00 26.78  ? 65  TYR   F OH    1 
ATOM   11808 N  N     . ARG   E 4  66  ? 10.214  63.284  79.761  1.00 21.14  ? 66  ARG   F N     1 
ATOM   11809 C  CA    . ARG   E 4  66  ? 11.606  63.639  80.013  1.00 25.22  ? 66  ARG   F CA    1 
ATOM   11810 C  C     . ARG   E 4  66  ? 11.749  64.392  81.328  1.00 29.62  ? 66  ARG   F C     1 
ATOM   11811 O  O     . ARG   E 4  66  ? 11.133  65.442  81.529  1.00 40.88  ? 66  ARG   F O     1 
ATOM   11812 C  CB    . ARG   E 4  66  ? 12.134  64.498  78.866  1.00 26.09  ? 66  ARG   F CB    1 
ATOM   11813 C  CG    . ARG   E 4  66  ? 13.581  64.918  78.974  1.00 23.48  ? 66  ARG   F CG    1 
ATOM   11814 C  CD    . ARG   E 4  66  ? 14.258  64.609  77.647  1.00 30.81  ? 66  ARG   F CD    1 
ATOM   11815 N  NE    . ARG   E 4  66  ? 15.534  65.284  77.446  1.00 27.62  ? 66  ARG   F NE    1 
ATOM   11816 C  CZ    . ARG   E 4  66  ? 15.675  66.407  76.759  1.00 27.69  ? 66  ARG   F CZ    1 
ATOM   11817 N  NH1   . ARG   E 4  66  ? 14.633  67.013  76.212  1.00 27.76  ? 66  ARG   F NH1   1 
ATOM   11818 N  NH2   . ARG   E 4  66  ? 16.888  66.939  76.624  1.00 37.46  ? 66  ARG   F NH2   1 
ATOM   11819 N  N     . GLY   E 4  67  ? 12.561  63.858  82.229  1.00 26.38  ? 67  GLY   F N     1 
ATOM   11820 C  CA    . GLY   E 4  67  ? 12.733  64.460  83.522  1.00 24.96  ? 67  GLY   F CA    1 
ATOM   11821 C  C     . GLY   E 4  67  ? 11.756  64.010  84.576  1.00 29.75  ? 67  GLY   F C     1 
ATOM   11822 O  O     . GLY   E 4  67  ? 11.843  64.493  85.709  1.00 40.80  ? 67  GLY   F O     1 
ATOM   11823 N  N     . ALA   E 4  68  ? 10.814  63.120  84.245  1.00 33.24  ? 68  ALA   F N     1 
ATOM   11824 C  CA    . ALA   E 4  68  ? 9.970   62.516  85.273  1.00 34.40  ? 68  ALA   F CA    1 
ATOM   11825 C  C     . ALA   E 4  68  ? 10.734  61.524  86.138  1.00 38.94  ? 68  ALA   F C     1 
ATOM   11826 O  O     . ALA   E 4  68  ? 10.181  61.043  87.132  1.00 41.19  ? 68  ALA   F O     1 
ATOM   11827 C  CB    . ALA   E 4  68  ? 8.757   61.823  84.651  1.00 27.66  ? 68  ALA   F CB    1 
ATOM   11828 N  N     . ASP   E 4  69  ? 11.991  61.227  85.798  1.00 36.28  ? 69  ASP   F N     1 
ATOM   11829 C  CA    . ASP   E 4  69  ? 12.805  60.345  86.626  1.00 37.78  ? 69  ASP   F CA    1 
ATOM   11830 C  C     . ASP   E 4  69  ? 13.117  60.963  87.984  1.00 40.22  ? 69  ASP   F C     1 
ATOM   11831 O  O     . ASP   E 4  69  ? 13.436  60.236  88.930  1.00 49.77  ? 69  ASP   F O     1 
ATOM   11832 C  CB    . ASP   E 4  69  ? 14.099  60.013  85.892  1.00 37.94  ? 69  ASP   F CB    1 
ATOM   11833 C  CG    . ASP   E 4  69  ? 14.721  61.241  85.263  1.00 45.19  ? 69  ASP   F CG    1 
ATOM   11834 O  OD1   . ASP   E 4  69  ? 15.245  62.105  86.001  1.00 42.81  ? 69  ASP   F OD1   1 
ATOM   11835 O  OD2   . ASP   E 4  69  ? 14.648  61.360  84.019  1.00 59.58  ? 69  ASP   F OD2   1 
ATOM   11836 N  N     . LYS   E 4  70  ? 13.077  62.294  88.096  1.00 37.46  ? 70  LYS   F N     1 
ATOM   11837 C  CA    . LYS   E 4  70  ? 13.301  62.927  89.395  1.00 41.94  ? 70  LYS   F CA    1 
ATOM   11838 C  C     . LYS   E 4  70  ? 12.288  62.432  90.426  1.00 40.84  ? 70  LYS   F C     1 
ATOM   11839 O  O     . LYS   E 4  70  ? 12.626  62.220  91.597  1.00 42.17  ? 70  LYS   F O     1 
ATOM   11840 C  CB    . LYS   E 4  70  ? 13.223  64.452  89.266  1.00 37.00  ? 70  LYS   F CB    1 
ATOM   11841 C  CG    . LYS   E 4  70  ? 13.845  65.031  88.014  1.00 44.26  ? 70  LYS   F CG    1 
ATOM   11842 C  CD    . LYS   E 4  70  ? 15.339  65.293  88.156  1.00 55.16  ? 70  LYS   F CD    1 
ATOM   11843 C  CE    . LYS   E 4  70  ? 15.874  66.035  86.929  1.00 58.53  ? 70  LYS   F CE    1 
ATOM   11844 N  NZ    . LYS   E 4  70  ? 17.288  66.456  87.101  1.00 58.50  ? 70  LYS   F NZ    1 
ATOM   11845 N  N     . LEU   E 4  71  ? 11.039  62.237  90.001  1.00 38.47  ? 71  LEU   F N     1 
ATOM   11846 C  CA    . LEU   E 4  71  ? 9.981   61.696  90.846  1.00 41.43  ? 71  LEU   F CA    1 
ATOM   11847 C  C     . LEU   E 4  71  ? 10.127  60.203  91.117  1.00 45.06  ? 71  LEU   F C     1 
ATOM   11848 O  O     . LEU   E 4  71  ? 9.602   59.712  92.124  1.00 39.65  ? 71  LEU   F O     1 
ATOM   11849 C  CB    . LEU   E 4  71  ? 8.641   61.928  90.165  1.00 37.50  ? 71  LEU   F CB    1 
ATOM   11850 C  CG    . LEU   E 4  71  ? 7.451   62.161  91.044  1.00 31.01  ? 71  LEU   F CG    1 
ATOM   11851 C  CD1   . LEU   E 4  71  ? 7.793   63.325  91.921  1.00 37.02  ? 71  LEU   F CD1   1 
ATOM   11852 C  CD2   . LEU   E 4  71  ? 6.331   62.506  90.118  1.00 38.65  ? 71  LEU   F CD2   1 
ATOM   11853 N  N     . CYS   E 4  72  ? 10.829  59.480  90.239  1.00 51.76  ? 72  CYS   F N     1 
ATOM   11854 C  CA    . CYS   E 4  72  ? 10.723  58.030  90.123  1.00 42.86  ? 72  CYS   F CA    1 
ATOM   11855 C  C     . CYS   E 4  72  ? 12.013  57.287  90.451  1.00 42.06  ? 72  CYS   F C     1 
ATOM   11856 O  O     . CYS   E 4  72  ? 12.082  56.072  90.227  1.00 42.66  ? 72  CYS   F O     1 
ATOM   11857 C  CB    . CYS   E 4  72  ? 10.254  57.672  88.711  1.00 32.04  ? 72  CYS   F CB    1 
ATOM   11858 S  SG    . CYS   E 4  72  ? 8.612   58.353  88.289  1.00 35.45  ? 72  CYS   F SG    1 
ATOM   11859 N  N     . ARG   E 4  73  ? 13.032  57.977  90.965  1.00 43.73  ? 73  ARG   F N     1 
ATOM   11860 C  CA    . ARG   E 4  73  ? 14.260  57.368  91.465  1.00 49.95  ? 73  ARG   F CA    1 
ATOM   11861 C  C     . ARG   E 4  73  ? 14.432  57.745  92.932  1.00 46.43  ? 73  ARG   F C     1 
ATOM   11862 O  O     . ARG   E 4  73  ? 14.423  58.932  93.270  1.00 44.95  ? 73  ARG   F O     1 
ATOM   11863 C  CB    . ARG   E 4  73  ? 15.481  57.830  90.662  1.00 51.59  ? 73  ARG   F CB    1 
ATOM   11864 C  CG    . ARG   E 4  73  ? 15.527  57.365  89.216  1.00 50.85  ? 73  ARG   F CG    1 
ATOM   11865 C  CD    . ARG   E 4  73  ? 15.299  55.867  89.072  1.00 56.31  ? 73  ARG   F CD    1 
ATOM   11866 N  NE    . ARG   E 4  73  ? 15.653  55.403  87.735  1.00 71.65  ? 73  ARG   F NE    1 
ATOM   11867 C  CZ    . ARG   E 4  73  ? 14.856  55.468  86.676  1.00 67.42  ? 73  ARG   F CZ    1 
ATOM   11868 N  NH1   . ARG   E 4  73  ? 13.632  55.972  86.759  1.00 54.15  ? 73  ARG   F NH1   1 
ATOM   11869 N  NH2   . ARG   E 4  73  ? 15.299  55.017  85.503  1.00 74.17  ? 73  ARG   F NH2   1 
ATOM   11870 N  N     . LYS   E 4  74  ? 14.618  56.739  93.791  1.00 43.28  ? 74  LYS   F N     1 
ATOM   11871 C  CA    . LYS   E 4  74  ? 14.471  56.943  95.234  1.00 46.88  ? 74  LYS   F CA    1 
ATOM   11872 C  C     . LYS   E 4  74  ? 15.373  58.064  95.746  1.00 46.59  ? 74  LYS   F C     1 
ATOM   11873 O  O     . LYS   E 4  74  ? 14.925  58.956  96.473  1.00 44.06  ? 74  LYS   F O     1 
ATOM   11874 C  CB    . LYS   E 4  74  ? 14.739  55.629  95.980  1.00 52.81  ? 74  LYS   F CB    1 
ATOM   11875 C  CG    . LYS   E 4  74  ? 13.536  54.656  95.940  1.00 58.21  ? 74  LYS   F CG    1 
ATOM   11876 C  CD    . LYS   E 4  74  ? 13.908  53.167  95.944  1.00 43.92  ? 74  LYS   F CD    1 
ATOM   11877 C  CE    . LYS   E 4  74  ? 12.744  52.318  95.423  1.00 51.16  ? 74  LYS   F CE    1 
ATOM   11878 N  NZ    . LYS   E 4  74  ? 13.036  50.843  95.335  1.00 67.96  ? 74  LYS   F NZ    1 
ATOM   11879 N  N     . ALA   E 4  75  ? 16.645  58.046  95.371  1.00 49.21  ? 75  ALA   F N     1 
ATOM   11880 C  CA    . ALA   E 4  75  ? 17.540  59.099  95.830  1.00 47.25  ? 75  ALA   F CA    1 
ATOM   11881 C  C     . ALA   E 4  75  ? 17.133  60.471  95.284  1.00 51.07  ? 75  ALA   F C     1 
ATOM   11882 O  O     . ALA   E 4  75  ? 17.274  61.491  95.973  1.00 46.49  ? 75  ALA   F O     1 
ATOM   11883 C  CB    . ALA   E 4  75  ? 18.973  58.757  95.426  1.00 53.79  ? 75  ALA   F CB    1 
ATOM   11884 N  N     . SER   E 4  76  ? 16.648  60.522  94.039  1.00 52.45  ? 76  SER   F N     1 
ATOM   11885 C  CA    . SER   E 4  76  ? 16.228  61.789  93.447  1.00 43.08  ? 76  SER   F CA    1 
ATOM   11886 C  C     . SER   E 4  76  ? 14.959  62.319  94.110  1.00 46.28  ? 76  SER   F C     1 
ATOM   11887 O  O     . SER   E 4  76  ? 14.924  63.470  94.557  1.00 49.67  ? 76  SER   F O     1 
ATOM   11888 C  CB    . SER   E 4  76  ? 16.033  61.610  91.947  1.00 50.47  ? 76  SER   F CB    1 
ATOM   11889 O  OG    . SER   E 4  76  ? 17.146  60.933  91.396  1.00 62.15  ? 76  SER   F OG    1 
ATOM   11890 N  N     . LEU   E 4  77  ? 13.906  61.491  94.186  1.00 39.95  ? 77  LEU   F N     1 
ATOM   11891 C  CA    . LEU   E 4  77  ? 12.677  61.865  94.885  1.00 37.94  ? 77  LEU   F CA    1 
ATOM   11892 C  C     . LEU   E 4  77  ? 12.973  62.565  96.197  1.00 48.74  ? 77  LEU   F C     1 
ATOM   11893 O  O     . LEU   E 4  77  ? 12.535  63.699  96.433  1.00 45.46  ? 77  LEU   F O     1 
ATOM   11894 C  CB    . LEU   E 4  77  ? 11.826  60.620  95.145  1.00 43.90  ? 77  LEU   F CB    1 
ATOM   11895 C  CG    . LEU   E 4  77  ? 10.576  60.695  96.032  1.00 37.83  ? 77  LEU   F CG    1 
ATOM   11896 C  CD1   . LEU   E 4  77  ? 9.655   61.829  95.619  1.00 41.30  ? 77  LEU   F CD1   1 
ATOM   11897 C  CD2   . LEU   E 4  77  ? 9.829   59.375  95.949  1.00 40.92  ? 77  LEU   F CD2   1 
ATOM   11898 N  N     . VAL   E 4  78  ? 13.721  61.886  97.069  1.00 49.51  ? 78  VAL   F N     1 
ATOM   11899 C  CA    . VAL   E 4  78  ? 14.161  62.487  98.326  1.00 46.04  ? 78  VAL   F CA    1 
ATOM   11900 C  C     . VAL   E 4  78  ? 14.647  63.916  98.093  1.00 50.74  ? 78  VAL   F C     1 
ATOM   11901 O  O     . VAL   E 4  78  ? 14.093  64.879  98.635  1.00 51.26  ? 78  VAL   F O     1 
ATOM   11902 C  CB    . VAL   E 4  78  ? 15.249  61.618  98.979  1.00 46.69  ? 78  VAL   F CB    1 
ATOM   11903 C  CG1   . VAL   E 4  78  ? 15.819  62.302  100.214 1.00 49.58  ? 78  VAL   F CG1   1 
ATOM   11904 C  CG2   . VAL   E 4  78  ? 14.680  60.260  99.310  1.00 49.04  ? 78  VAL   F CG2   1 
ATOM   11905 N  N     . LYS   E 4  79  ? 15.695  64.076  97.278  1.00 51.76  ? 79  LYS   F N     1 
ATOM   11906 C  CA    . LYS   E 4  79  ? 16.234  65.416  97.069  1.00 56.46  ? 79  LYS   F CA    1 
ATOM   11907 C  C     . LYS   E 4  79  ? 15.163  66.354  96.537  1.00 47.77  ? 79  LYS   F C     1 
ATOM   11908 O  O     . LYS   E 4  79  ? 15.157  67.544  96.869  1.00 41.42  ? 79  LYS   F O     1 
ATOM   11909 C  CB    . LYS   E 4  79  ? 17.434  65.366  96.118  1.00 58.45  ? 79  LYS   F CB    1 
ATOM   11910 C  CG    . LYS   E 4  79  ? 18.096  66.726  95.861  1.00 55.57  ? 79  LYS   F CG    1 
ATOM   11911 C  CD    . LYS   E 4  79  ? 18.758  66.781  94.481  1.00 55.31  ? 79  LYS   F CD    1 
ATOM   11912 C  CE    . LYS   E 4  79  ? 18.352  68.049  93.728  1.00 57.01  ? 79  LYS   F CE    1 
ATOM   11913 N  NZ    . LYS   E 4  79  ? 16.859  68.180  93.560  1.00 53.82  ? 79  LYS   F NZ    1 
ATOM   11914 N  N     . LEU   E 4  80  ? 14.233  65.824  95.740  1.00 44.37  ? 80  LEU   F N     1 
ATOM   11915 C  CA    . LEU   E 4  80  ? 13.162  66.641  95.178  1.00 42.52  ? 80  LEU   F CA    1 
ATOM   11916 C  C     . LEU   E 4  80  ? 12.274  67.200  96.275  1.00 46.78  ? 80  LEU   F C     1 
ATOM   11917 O  O     . LEU   E 4  80  ? 12.006  68.404  96.319  1.00 48.57  ? 80  LEU   F O     1 
ATOM   11918 C  CB    . LEU   E 4  80  ? 12.338  65.816  94.188  1.00 37.29  ? 80  LEU   F CB    1 
ATOM   11919 C  CG    . LEU   E 4  80  ? 11.088  66.471  93.599  1.00 39.82  ? 80  LEU   F CG    1 
ATOM   11920 C  CD1   . LEU   E 4  80  ? 11.411  67.777  92.898  1.00 27.36  ? 80  LEU   F CD1   1 
ATOM   11921 C  CD2   . LEU   E 4  80  ? 10.354  65.508  92.674  1.00 40.81  ? 80  LEU   F CD2   1 
ATOM   11922 N  N     . ILE   E 4  81  ? 11.802  66.330  97.172  1.00 47.87  ? 81  ILE   F N     1 
ATOM   11923 C  CA    . ILE   E 4  81  ? 10.974  66.780  98.287  1.00 45.57  ? 81  ILE   F CA    1 
ATOM   11924 C  C     . ILE   E 4  81  ? 11.751  67.752  99.160  1.00 50.29  ? 81  ILE   F C     1 
ATOM   11925 O  O     . ILE   E 4  81  ? 11.252  68.819  99.536  1.00 55.15  ? 81  ILE   F O     1 
ATOM   11926 C  CB    . ILE   E 4  81  ? 10.481  65.577  99.109  1.00 45.68  ? 81  ILE   F CB    1 
ATOM   11927 C  CG1   . ILE   E 4  81  ? 9.959   64.474  98.204  1.00 40.92  ? 81  ILE   F CG1   1 
ATOM   11928 C  CG2   . ILE   E 4  81  ? 9.403   66.005  100.072 1.00 48.21  ? 81  ILE   F CG2   1 
ATOM   11929 C  CD1   . ILE   E 4  81  ? 9.356   63.343  98.959  1.00 42.37  ? 81  ILE   F CD1   1 
ATOM   11930 N  N     . LYS   E 4  82  ? 12.991  67.397  99.497  1.00 45.12  ? 82  LYS   F N     1 
ATOM   11931 C  CA    . LYS   E 4  82  ? 13.747  68.191  100.457 1.00 52.71  ? 82  LYS   F CA    1 
ATOM   11932 C  C     . LYS   E 4  82  ? 13.991  69.606  99.940  1.00 59.55  ? 82  LYS   F C     1 
ATOM   11933 O  O     . LYS   E 4  82  ? 13.934  70.574  100.707 1.00 59.51  ? 82  LYS   F O     1 
ATOM   11934 C  CB    . LYS   E 4  82  ? 15.067  67.490  100.789 1.00 61.87  ? 82  LYS   F CB    1 
ATOM   11935 C  CG    . LYS   E 4  82  ? 14.905  66.005  101.164 1.00 68.26  ? 82  LYS   F CG    1 
ATOM   11936 C  CD    . LYS   E 4  82  ? 16.090  65.440  101.959 1.00 65.25  ? 82  LYS   F CD    1 
ATOM   11937 C  CE    . LYS   E 4  82  ? 16.127  65.983  103.380 1.00 67.60  ? 82  LYS   F CE    1 
ATOM   11938 N  NZ    . LYS   E 4  82  ? 17.179  65.325  104.210 1.00 78.57  ? 82  LYS   F NZ    1 
ATOM   11939 N  N     . THR   E 4  83  ? 14.236  69.750  98.637  1.00 60.61  ? 83  THR   F N     1 
ATOM   11940 C  CA    . THR   E 4  83  ? 14.618  71.036  98.065  1.00 49.33  ? 83  THR   F CA    1 
ATOM   11941 C  C     . THR   E 4  83  ? 13.407  71.855  97.603  1.00 55.36  ? 83  THR   F C     1 
ATOM   11942 O  O     . THR   E 4  83  ? 13.296  73.033  97.948  1.00 62.79  ? 83  THR   F O     1 
ATOM   11943 C  CB    . THR   E 4  83  ? 15.604  70.812  96.915  1.00 55.06  ? 83  THR   F CB    1 
ATOM   11944 O  OG1   . THR   E 4  83  ? 14.987  70.031  95.879  1.00 60.26  ? 83  THR   F OG1   1 
ATOM   11945 C  CG2   . THR   E 4  83  ? 16.823  70.069  97.427  1.00 39.27  ? 83  THR   F CG2   1 
ATOM   11946 N  N     . SER   E 4  84  ? 12.475  71.255  96.844  1.00 50.06  ? 84  SER   F N     1 
ATOM   11947 C  CA    . SER   E 4  84  ? 11.335  71.985  96.280  1.00 49.18  ? 84  SER   F CA    1 
ATOM   11948 C  C     . SER   E 4  84  ? 10.518  72.705  97.339  1.00 61.42  ? 84  SER   F C     1 
ATOM   11949 O  O     . SER   E 4  84  ? 9.860   72.044  98.150  1.00 62.89  ? 84  SER   F O     1 
ATOM   11950 C  CB    . SER   E 4  84  ? 10.411  71.032  95.529  1.00 41.65  ? 84  SER   F CB    1 
ATOM   11951 O  OG    . SER   E 4  84  ? 11.139  69.899  95.073  1.00 55.19  ? 84  SER   F OG    1 
ATOM   11952 N  N     . PRO   E 4  85  ? 10.494  74.038  97.349  1.00 65.54  ? 85  PRO   F N     1 
ATOM   11953 C  CA    . PRO   E 4  85  ? 9.676   74.733  98.351  1.00 52.12  ? 85  PRO   F CA    1 
ATOM   11954 C  C     . PRO   E 4  85  ? 8.236   74.253  98.375  1.00 55.87  ? 85  PRO   F C     1 
ATOM   11955 O  O     . PRO   E 4  85  ? 7.589   74.336  99.428  1.00 63.13  ? 85  PRO   F O     1 
ATOM   11956 C  CB    . PRO   E 4  85  ? 9.769   76.206  97.928  1.00 49.67  ? 85  PRO   F CB    1 
ATOM   11957 C  CG    . PRO   E 4  85  ? 10.983  76.306  97.066  1.00 54.42  ? 85  PRO   F CG    1 
ATOM   11958 C  CD    . PRO   E 4  85  ? 11.069  74.965  96.358  1.00 70.39  ? 85  PRO   F CD    1 
ATOM   11959 N  N     . GLU   E 4  86  ? 7.712   73.742  97.249  1.00 63.51  ? 86  GLU   F N     1 
ATOM   11960 C  CA    . GLU   E 4  86  ? 6.323   73.276  97.207  1.00 59.10  ? 86  GLU   F CA    1 
ATOM   11961 C  C     . GLU   E 4  86  ? 6.100   72.101  98.149  1.00 57.68  ? 86  GLU   F C     1 
ATOM   11962 O  O     . GLU   E 4  86  ? 4.977   71.869  98.607  1.00 57.20  ? 86  GLU   F O     1 
ATOM   11963 C  CB    . GLU   E 4  86  ? 5.927   72.857  95.780  1.00 49.80  ? 86  GLU   F CB    1 
ATOM   11964 C  CG    . GLU   E 4  86  ? 6.421   73.745  94.638  1.00 43.60  ? 86  GLU   F CG    1 
ATOM   11965 C  CD    . GLU   E 4  86  ? 5.479   73.716  93.406  1.00 63.48  ? 86  GLU   F CD    1 
ATOM   11966 O  OE1   . GLU   E 4  86  ? 4.394   73.081  93.450  1.00 55.22  ? 86  GLU   F OE1   1 
ATOM   11967 O  OE2   . GLU   E 4  86  ? 5.819   74.338  92.376  1.00 66.83  ? 86  GLU   F OE2   1 
ATOM   11968 N  N     . LEU   E 4  87  ? 7.154   71.330  98.409  1.00 63.87  ? 87  LEU   F N     1 
ATOM   11969 C  CA    . LEU   E 4  87  ? 7.085   70.141  99.249  1.00 63.76  ? 87  LEU   F CA    1 
ATOM   11970 C  C     . LEU   E 4  87  ? 7.854   70.382  100.540 1.00 63.75  ? 87  LEU   F C     1 
ATOM   11971 O  O     . LEU   E 4  87  ? 7.243   70.529  101.603 1.00 63.20  ? 87  LEU   F O     1 
ATOM   11972 C  CB    . LEU   E 4  87  ? 7.623   68.929  98.477  1.00 50.19  ? 87  LEU   F CB    1 
ATOM   11973 C  CG    . LEU   E 4  87  ? 7.033   68.817  97.066  1.00 40.93  ? 87  LEU   F CG    1 
ATOM   11974 C  CD1   . LEU   E 4  87  ? 7.502   67.571  96.342  1.00 37.13  ? 87  LEU   F CD1   1 
ATOM   11975 C  CD2   . LEU   E 4  87  ? 5.530   68.858  97.119  1.00 26.05  ? 87  LEU   F CD2   1 
ATOM   11976 N  N     . SER   E 4  88  ? 9.188   70.452  100.469 1.00 70.02  ? 88  SER   F N     1 
ATOM   11977 C  CA    . SER   E 4  88  ? 10.055  70.836  101.583 1.00 78.10  ? 88  SER   F CA    1 
ATOM   11978 C  C     . SER   E 4  88  ? 9.918   69.888  102.767 1.00 83.16  ? 88  SER   F C     1 
ATOM   11979 O  O     . SER   E 4  88  ? 9.358   68.794  102.633 1.00 86.03  ? 88  SER   F O     1 
ATOM   11980 C  CB    . SER   E 4  88  ? 9.758   72.271  102.035 1.00 76.96  ? 88  SER   F CB    1 
ATOM   11981 O  OG    . SER   E 4  88  ? 8.600   72.321  102.852 1.00 68.00  ? 88  SER   F OG    1 
ATOM   11982 N  N     . GLU   E 4  89  ? 10.451  70.292  103.927 1.00 79.96  ? 89  GLU   F N     1 
ATOM   11983 C  CA    . GLU   E 4  89  ? 10.208  69.547  105.156 1.00 81.36  ? 89  GLU   F CA    1 
ATOM   11984 C  C     . GLU   E 4  89  ? 8.807   69.788  105.701 1.00 89.71  ? 89  GLU   F C     1 
ATOM   11985 O  O     . GLU   E 4  89  ? 8.341   69.012  106.545 1.00 89.16  ? 89  GLU   F O     1 
ATOM   11986 C  CB    . GLU   E 4  89  ? 11.249  69.900  106.214 1.00 84.34  ? 89  GLU   F CB    1 
ATOM   11987 C  CG    . GLU   E 4  89  ? 12.591  69.218  106.001 1.00 88.51  ? 89  GLU   F CG    1 
ATOM   11988 C  CD    . GLU   E 4  89  ? 13.275  69.668  104.727 1.00 82.98  ? 89  GLU   F CD    1 
ATOM   11989 O  OE1   . GLU   E 4  89  ? 12.573  70.097  103.794 1.00 88.11  ? 89  GLU   F OE1   1 
ATOM   11990 O  OE2   . GLU   E 4  89  ? 14.522  69.627  104.671 1.00 90.64  ? 89  GLU   F OE2   1 
ATOM   11991 N  N     . SER   E 4  90  ? 8.128   70.844  105.239 1.00 92.57  ? 90  SER   F N     1 
ATOM   11992 C  CA    . SER   E 4  90  ? 6.685   70.939  105.449 1.00 96.48  ? 90  SER   F CA    1 
ATOM   11993 C  C     . SER   E 4  90  ? 5.984   69.643  105.049 1.00 90.00  ? 90  SER   F C     1 
ATOM   11994 O  O     . SER   E 4  90  ? 4.936   69.300  105.608 1.00 89.93  ? 90  SER   F O     1 
ATOM   11995 C  CB    . SER   E 4  90  ? 6.119   72.132  104.672 1.00 88.41  ? 90  SER   F CB    1 
ATOM   11996 O  OG    . SER   E 4  90  ? 6.575   72.128  103.332 1.00 83.41  ? 90  SER   F OG    1 
ATOM   11997 N  N     . CYS   E 4  91  ? 6.566   68.894  104.118 1.00 79.83  ? 91  CYS   F N     1 
ATOM   11998 C  CA    . CYS   E 4  91  ? 6.024   67.607  103.715 1.00 72.14  ? 91  CYS   F CA    1 
ATOM   11999 C  C     . CYS   E 4  91  ? 5.851   66.683  104.916 1.00 68.92  ? 91  CYS   F C     1 
ATOM   12000 O  O     . CYS   E 4  91  ? 6.820   66.377  105.619 1.00 63.07  ? 91  CYS   F O     1 
ATOM   12001 C  CB    . CYS   E 4  91  ? 6.955   66.975  102.685 1.00 64.73  ? 91  CYS   F CB    1 
ATOM   12002 S  SG    . CYS   E 4  91  ? 6.245   65.581  101.803 1.00 72.08  ? 91  CYS   F SG    1 
ATOM   12003 N  N     . THR   E 4  92  ? 4.609   66.227  105.135 1.00 63.71  ? 92  THR   F N     1 
ATOM   12004 C  CA    . THR   E 4  92  ? 4.267   65.328  106.235 1.00 58.96  ? 92  THR   F CA    1 
ATOM   12005 C  C     . THR   E 4  92  ? 3.711   63.984  105.781 1.00 53.16  ? 92  THR   F C     1 
ATOM   12006 O  O     . THR   E 4  92  ? 3.214   63.228  106.622 1.00 44.58  ? 92  THR   F O     1 
ATOM   12007 C  CB    . THR   E 4  92  ? 3.248   65.981  107.158 1.00 55.02  ? 92  THR   F CB    1 
ATOM   12008 O  OG1   . THR   E 4  92  ? 2.094   66.352  106.390 1.00 48.87  ? 92  THR   F OG1   1 
ATOM   12009 C  CG2   . THR   E 4  92  ? 3.858   67.196  107.828 1.00 58.59  ? 92  THR   F CG2   1 
ATOM   12010 N  N     . TRP   E 4  93  ? 3.761   63.679  104.485 1.00 50.37  ? 93  TRP   F N     1 
ATOM   12011 C  CA    . TRP   E 4  93  ? 3.357   62.388  103.945 1.00 40.42  ? 93  TRP   F CA    1 
ATOM   12012 C  C     . TRP   E 4  93  ? 4.537   61.628  103.351 1.00 50.86  ? 93  TRP   F C     1 
ATOM   12013 O  O     . TRP   E 4  93  ? 4.332   60.617  102.658 1.00 50.09  ? 93  TRP   F O     1 
ATOM   12014 C  CB    . TRP   E 4  93  ? 2.258   62.578  102.890 1.00 44.02  ? 93  TRP   F CB    1 
ATOM   12015 C  CG    . TRP   E 4  93  ? 2.461   63.817  102.001 1.00 52.52  ? 93  TRP   F CG    1 
ATOM   12016 C  CD1   . TRP   E 4  93  ? 1.827   65.015  102.126 1.00 52.18  ? 93  TRP   F CD1   1 
ATOM   12017 C  CD2   . TRP   E 4  93  ? 3.365   63.962  100.880 1.00 49.62  ? 93  TRP   F CD2   1 
ATOM   12018 N  NE1   . TRP   E 4  93  ? 2.269   65.894  101.161 1.00 56.33  ? 93  TRP   F NE1   1 
ATOM   12019 C  CE2   . TRP   E 4  93  ? 3.215   65.275  100.388 1.00 54.54  ? 93  TRP   F CE2   1 
ATOM   12020 C  CE3   . TRP   E 4  93  ? 4.285   63.114  100.257 1.00 43.08  ? 93  TRP   F CE3   1 
ATOM   12021 C  CZ2   . TRP   E 4  93  ? 3.947   65.757  99.298  1.00 47.06  ? 93  TRP   F CZ2   1 
ATOM   12022 C  CZ3   . TRP   E 4  93  ? 5.010   63.597  99.179  1.00 49.70  ? 93  TRP   F CZ3   1 
ATOM   12023 C  CH2   . TRP   E 4  93  ? 4.835   64.905  98.709  1.00 46.79  ? 93  TRP   F CH2   1 
ATOM   12024 N  N     . PHE   E 4  94  ? 5.766   62.097  103.578 1.00 43.98  ? 94  PHE   F N     1 
ATOM   12025 C  CA    . PHE   E 4  94  ? 6.944   61.368  103.129 1.00 50.85  ? 94  PHE   F CA    1 
ATOM   12026 C  C     . PHE   E 4  94  ? 7.742   60.930  104.344 1.00 50.15  ? 94  PHE   F C     1 
ATOM   12027 O  O     . PHE   E 4  94  ? 8.138   61.784  105.154 1.00 49.15  ? 94  PHE   F O     1 
ATOM   12028 C  CB    . PHE   E 4  94  ? 7.829   62.200  102.196 1.00 56.89  ? 94  PHE   F CB    1 
ATOM   12029 C  CG    . PHE   E 4  94  ? 8.836   61.372  101.425 1.00 52.34  ? 94  PHE   F CG    1 
ATOM   12030 C  CD1   . PHE   E 4  94  ? 8.411   60.297  100.651 1.00 47.46  ? 94  PHE   F CD1   1 
ATOM   12031 C  CD2   . PHE   E 4  94  ? 10.194  61.661  101.475 1.00 43.71  ? 94  PHE   F CD2   1 
ATOM   12032 C  CE1   . PHE   E 4  94  ? 9.320   59.521  99.949  1.00 44.44  ? 94  PHE   F CE1   1 
ATOM   12033 C  CE2   . PHE   E 4  94  ? 11.103  60.891  100.762 1.00 40.52  ? 94  PHE   F CE2   1 
ATOM   12034 C  CZ    . PHE   E 4  94  ? 10.664  59.819  100.003 1.00 39.15  ? 94  PHE   F CZ    1 
ATOM   12035 N  N     . PRO   E 4  95  ? 7.981   59.633  104.527 1.00 55.72  ? 95  PRO   F N     1 
ATOM   12036 C  CA    . PRO   E 4  95  ? 8.877   59.189  105.599 1.00 55.91  ? 95  PRO   F CA    1 
ATOM   12037 C  C     . PRO   E 4  95  ? 10.185  59.962  105.561 1.00 52.77  ? 95  PRO   F C     1 
ATOM   12038 O  O     . PRO   E 4  95  ? 10.648  60.383  104.499 1.00 51.64  ? 95  PRO   F O     1 
ATOM   12039 C  CB    . PRO   E 4  95  ? 9.091   57.705  105.287 1.00 50.95  ? 95  PRO   F CB    1 
ATOM   12040 C  CG    . PRO   E 4  95  ? 7.805   57.296  104.645 1.00 56.79  ? 95  PRO   F CG    1 
ATOM   12041 C  CD    . PRO   E 4  95  ? 7.339   58.499  103.838 1.00 51.33  ? 95  PRO   F CD    1 
ATOM   12042 N  N     . GLU   E 4  96  ? 10.769  60.161  106.743 1.00 58.46  ? 96  GLU   F N     1 
ATOM   12043 C  CA    . GLU   E 4  96  ? 12.016  60.911  106.859 1.00 64.06  ? 96  GLU   F CA    1 
ATOM   12044 C  C     . GLU   E 4  96  ? 13.156  60.148  106.181 1.00 71.38  ? 96  GLU   F C     1 
ATOM   12045 O  O     . GLU   E 4  96  ? 13.416  58.982  106.510 1.00 72.76  ? 96  GLU   F O     1 
ATOM   12046 C  CB    . GLU   E 4  96  ? 12.330  61.172  108.331 1.00 59.82  ? 96  GLU   F CB    1 
ATOM   12047 C  CG    . GLU   E 4  96  ? 13.781  61.490  108.588 1.00 61.21  ? 96  GLU   F CG    1 
ATOM   12048 C  CD    . GLU   E 4  96  ? 14.097  61.658  110.052 1.00 66.08  ? 96  GLU   F CD    1 
ATOM   12049 O  OE1   . GLU   E 4  96  ? 13.285  62.286  110.763 1.00 62.19  ? 96  GLU   F OE1   1 
ATOM   12050 O  OE2   . GLU   E 4  96  ? 15.156  61.152  110.487 1.00 77.85  ? 96  GLU   F OE2   1 
ATOM   12051 N  N     . SER   E 4  97  ? 13.844  60.807  105.244 1.00 61.87  ? 97  SER   F N     1 
ATOM   12052 C  CA    . SER   E 4  97  ? 14.779  60.120  104.365 1.00 64.25  ? 97  SER   F CA    1 
ATOM   12053 C  C     . SER   E 4  97  ? 16.054  60.937  104.165 1.00 65.92  ? 97  SER   F C     1 
ATOM   12054 O  O     . SER   E 4  97  ? 16.074  62.163  104.313 1.00 61.16  ? 97  SER   F O     1 
ATOM   12055 C  CB    . SER   E 4  97  ? 14.129  59.815  103.003 1.00 61.06  ? 97  SER   F CB    1 
ATOM   12056 O  OG    . SER   E 4  97  ? 13.134  58.801  103.103 1.00 52.26  ? 97  SER   F OG    1 
ATOM   12057 N  N     . TYR   E 4  98  ? 17.126  60.221  103.819 1.00 67.92  ? 98  TYR   F N     1 
ATOM   12058 C  CA    . TYR   E 4  98  ? 18.414  60.800  103.470 1.00 64.59  ? 98  TYR   F CA    1 
ATOM   12059 C  C     . TYR   E 4  98  ? 19.034  59.948  102.370 1.00 68.79  ? 98  TYR   F C     1 
ATOM   12060 O  O     . TYR   E 4  98  ? 18.689  58.775  102.205 1.00 65.04  ? 98  TYR   F O     1 
ATOM   12061 C  CB    . TYR   E 4  98  ? 19.354  60.868  104.676 1.00 67.67  ? 98  TYR   F CB    1 
ATOM   12062 C  CG    . TYR   E 4  98  ? 18.709  61.394  105.933 1.00 74.71  ? 98  TYR   F CG    1 
ATOM   12063 C  CD1   . TYR   E 4  98  ? 18.056  60.537  106.812 1.00 75.65  ? 98  TYR   F CD1   1 
ATOM   12064 C  CD2   . TYR   E 4  98  ? 18.745  62.750  106.246 1.00 79.40  ? 98  TYR   F CD2   1 
ATOM   12065 C  CE1   . TYR   E 4  98  ? 17.460  61.014  107.968 1.00 72.06  ? 98  TYR   F CE1   1 
ATOM   12066 C  CE2   . TYR   E 4  98  ? 18.155  63.235  107.401 1.00 68.17  ? 98  TYR   F CE2   1 
ATOM   12067 C  CZ    . TYR   E 4  98  ? 17.517  62.361  108.255 1.00 72.10  ? 98  TYR   F CZ    1 
ATOM   12068 O  OH    . TYR   E 4  98  ? 16.931  62.837  109.402 1.00 80.18  ? 98  TYR   F OH    1 
ATOM   12069 N  N     . VAL   E 4  99  ? 19.951  60.549  101.607 1.00 79.43  ? 99  VAL   F N     1 
ATOM   12070 C  CA    . VAL   E 4  99  ? 20.660  59.861  100.527 1.00 75.68  ? 99  VAL   F CA    1 
ATOM   12071 C  C     . VAL   E 4  99  ? 22.044  59.471  101.024 1.00 77.82  ? 99  VAL   F C     1 
ATOM   12072 O  O     . VAL   E 4  99  ? 22.770  60.302  101.588 1.00 73.18  ? 99  VAL   F O     1 
ATOM   12073 C  CB    . VAL   E 4  99  ? 20.757  60.740  99.270  1.00 65.62  ? 99  VAL   F CB    1 
ATOM   12074 C  CG1   . VAL   E 4  99  ? 19.467  60.687  98.488  1.00 59.09  ? 99  VAL   F CG1   1 
ATOM   12075 C  CG2   . VAL   E 4  99  ? 21.064  62.170  99.661  1.00 77.90  ? 99  VAL   F CG2   1 
ATOM   12076 N  N     . ILE   E 4  100 ? 22.409  58.209  100.827 1.00 79.91  ? 100 ILE   F N     1 
ATOM   12077 C  CA    . ILE   E 4  100 ? 23.684  57.690  101.300 1.00 80.25  ? 100 ILE   F CA    1 
ATOM   12078 C  C     . ILE   E 4  100 ? 24.407  57.056  100.121 1.00 84.61  ? 100 ILE   F C     1 
ATOM   12079 O  O     . ILE   E 4  100 ? 23.777  56.553  99.185  1.00 85.25  ? 100 ILE   F O     1 
ATOM   12080 C  CB    . ILE   E 4  100 ? 23.500  56.674  102.454 1.00 74.25  ? 100 ILE   F CB    1 
ATOM   12081 C  CG1   . ILE   E 4  100 ? 22.576  57.236  103.545 1.00 75.14  ? 100 ILE   F CG1   1 
ATOM   12082 C  CG2   . ILE   E 4  100 ? 24.835  56.287  103.039 1.00 81.06  ? 100 ILE   F CG2   1 
ATOM   12083 C  CD1   . ILE   E 4  100 ? 23.215  58.247  104.481 1.00 78.06  ? 100 ILE   F CD1   1 
ATOM   12084 N  N     . TYR   E 4  101 ? 25.744  57.097  100.161 1.00 88.77  ? 101 TYR   F N     1 
ATOM   12085 C  CA    . TYR   E 4  101 ? 26.559  56.553  99.086  1.00 93.56  ? 101 TYR   F CA    1 
ATOM   12086 C  C     . TYR   E 4  101 ? 27.537  55.507  99.610  1.00 93.13  ? 101 TYR   F C     1 
ATOM   12087 O  O     . TYR   E 4  101 ? 28.111  55.687  100.692 1.00 84.52  ? 101 TYR   F O     1 
ATOM   12088 C  CB    . TYR   E 4  101 ? 27.370  57.647  98.382  1.00 94.04  ? 101 TYR   F CB    1 
ATOM   12089 C  CG    . TYR   E 4  101 ? 26.608  58.866  97.939  1.00 86.19  ? 101 TYR   F CG    1 
ATOM   12090 C  CD1   . TYR   E 4  101 ? 26.294  59.873  98.843  1.00 88.87  ? 101 TYR   F CD1   1 
ATOM   12091 C  CD2   . TYR   E 4  101 ? 26.249  59.037  96.608  1.00 80.92  ? 101 TYR   F CD2   1 
ATOM   12092 C  CE1   . TYR   E 4  101 ? 25.617  61.007  98.441  1.00 88.77  ? 101 TYR   F CE1   1 
ATOM   12093 C  CE2   . TYR   E 4  101 ? 25.577  60.168  96.192  1.00 91.16  ? 101 TYR   F CE2   1 
ATOM   12094 C  CZ    . TYR   E 4  101 ? 25.261  61.150  97.117  1.00 92.65  ? 101 TYR   F CZ    1 
ATOM   12095 O  OH    . TYR   E 4  101 ? 24.588  62.281  96.721  1.00 92.91  ? 101 TYR   F OH    1 
ATOM   12096 N  N     . PRO   E 4  102 ? 27.770  54.425  98.860  1.00 91.33  ? 102 PRO   F N     1 
ATOM   12097 C  CA    . PRO   E 4  102 ? 28.822  53.478  99.245  1.00 94.03  ? 102 PRO   F CA    1 
ATOM   12098 C  C     . PRO   E 4  102 ? 30.200  54.123  99.180  1.00 97.24  ? 102 PRO   F C     1 
ATOM   12099 O  O     . PRO   E 4  102 ? 30.411  55.135  98.507  1.00 105.88 ? 102 PRO   F O     1 
ATOM   12100 C  CB    . PRO   E 4  102 ? 28.680  52.342  98.218  1.00 96.71  ? 102 PRO   F CB    1 
ATOM   12101 C  CG    . PRO   E 4  102 ? 27.993  52.963  97.052  1.00 99.08  ? 102 PRO   F CG    1 
ATOM   12102 C  CD    . PRO   E 4  102 ? 27.072  54.004  97.632  1.00 94.88  ? 102 PRO   F CD    1 
ATOM   12103 N  N     . THR   E 4  103 ? 31.146  53.511  99.896  1.00 95.36  ? 103 THR   F N     1 
ATOM   12104 C  CA    . THR   E 4  103 ? 32.531  53.988  100.009 1.00 91.05  ? 103 THR   F CA    1 
ATOM   12105 C  C     . THR   E 4  103 ? 32.620  55.519  99.965  1.00 92.06  ? 103 THR   F C     1 
ATOM   12106 O  O     . THR   E 4  103 ? 33.705  56.097  99.911  1.00 84.87  ? 103 THR   F O     1 
ATOM   12107 C  CB    . THR   E 4  103 ? 33.449  53.373  98.900  1.00 90.56  ? 103 THR   F CB    1 
ATOM   12108 O  OG1   . THR   E 4  103 ? 32.922  53.660  97.597  1.00 96.65  ? 103 THR   F OG1   1 
ATOM   12109 C  CG2   . THR   E 4  103 ? 33.581  51.856  99.070  1.00 82.74  ? 103 THR   F CG2   1 
ATOM   12110 N  N     . THR   E 4  125 ? 26.476  66.733  99.644  1.00 82.09  ? 125 THR   F N     1 
ATOM   12111 C  CA    . THR   E 4  125 ? 25.222  66.103  99.242  1.00 89.45  ? 125 THR   F CA    1 
ATOM   12112 C  C     . THR   E 4  125 ? 24.998  64.784  99.957  1.00 93.35  ? 125 THR   F C     1 
ATOM   12113 O  O     . THR   E 4  125 ? 23.914  64.207  99.855  1.00 86.54  ? 125 THR   F O     1 
ATOM   12114 C  CB    . THR   E 4  125 ? 25.164  65.822  97.732  1.00 85.48  ? 125 THR   F CB    1 
ATOM   12115 O  OG1   . THR   E 4  125 ? 25.858  66.852  97.020  1.00 89.92  ? 125 THR   F OG1   1 
ATOM   12116 C  CG2   . THR   E 4  125 ? 23.718  65.763  97.263  1.00 69.59  ? 125 THR   F CG2   1 
ATOM   12117 N  N     . ASP   E 4  126 ? 26.035  64.298  100.644 1.00 95.81  ? 126 ASP   F N     1 
ATOM   12118 C  CA    . ASP   E 4  126 ? 25.931  63.084  101.445 1.00 89.75  ? 126 ASP   F CA    1 
ATOM   12119 C  C     . ASP   E 4  126 ? 25.292  63.429  102.785 1.00 86.38  ? 126 ASP   F C     1 
ATOM   12120 O  O     . ASP   E 4  126 ? 25.678  64.409  103.432 1.00 92.70  ? 126 ASP   F O     1 
ATOM   12121 C  CB    . ASP   E 4  126 ? 27.315  62.460  101.647 1.00 94.28  ? 126 ASP   F CB    1 
ATOM   12122 C  CG    . ASP   E 4  126 ? 27.256  60.965  101.939 1.00 91.75  ? 126 ASP   F CG    1 
ATOM   12123 O  OD1   . ASP   E 4  126 ? 26.175  60.372  101.762 1.00 87.41  ? 126 ASP   F OD1   1 
ATOM   12124 O  OD2   . ASP   E 4  126 ? 28.289  60.383  102.342 1.00 87.56  ? 126 ASP   F OD2   1 
ATOM   12125 N  N     . GLU   E 4  127 ? 24.297  62.644  103.193 1.00 80.65  ? 127 GLU   F N     1 
ATOM   12126 C  CA    . GLU   E 4  127 ? 23.541  62.927  104.408 1.00 91.67  ? 127 GLU   F CA    1 
ATOM   12127 C  C     . GLU   E 4  127 ? 23.783  61.876  105.491 1.00 93.23  ? 127 GLU   F C     1 
ATOM   12128 O  O     . GLU   E 4  127 ? 22.899  61.597  106.308 1.00 91.94  ? 127 GLU   F O     1 
ATOM   12129 C  CB    . GLU   E 4  127 ? 22.046  63.039  104.102 1.00 88.99  ? 127 GLU   F CB    1 
ATOM   12130 C  CG    . GLU   E 4  127 ? 21.680  64.014  102.973 1.00 83.74  ? 127 GLU   F CG    1 
ATOM   12131 C  CD    . GLU   E 4  127 ? 20.173  64.306  102.881 1.00 80.42  ? 127 GLU   F CD    1 
ATOM   12132 O  OE1   . GLU   E 4  127 ? 19.675  65.149  103.666 1.00 68.83  ? 127 GLU   F OE1   1 
ATOM   12133 O  OE2   . GLU   E 4  127 ? 19.488  63.694  102.024 1.00 75.60  ? 127 GLU   F OE2   1 
ATOM   12134 N  N     . ARG   E 4  128 ? 24.985  61.296  105.519 1.00 90.18  ? 128 ARG   F N     1 
ATOM   12135 C  CA    . ARG   E 4  128 ? 25.283  60.259  106.504 1.00 91.52  ? 128 ARG   F CA    1 
ATOM   12136 C  C     . ARG   E 4  128 ? 25.413  60.847  107.901 1.00 88.05  ? 128 ARG   F C     1 
ATOM   12137 O  O     . ARG   E 4  128 ? 24.776  60.370  108.847 1.00 89.26  ? 128 ARG   F O     1 
ATOM   12138 C  CB    . ARG   E 4  128 ? 26.553  59.521  106.108 1.00 89.68  ? 128 ARG   F CB    1 
ATOM   12139 C  CG    . ARG   E 4  128 ? 26.462  58.956  104.718 1.00 86.19  ? 128 ARG   F CG    1 
ATOM   12140 C  CD    . ARG   E 4  128 ? 27.170  57.652  104.636 1.00 84.42  ? 128 ARG   F CD    1 
ATOM   12141 N  NE    . ARG   E 4  128 ? 28.578  57.796  104.961 1.00 89.50  ? 128 ARG   F NE    1 
ATOM   12142 C  CZ    . ARG   E 4  128 ? 29.410  56.773  105.069 1.00 105.24 ? 128 ARG   F CZ    1 
ATOM   12143 N  NH1   . ARG   E 4  128 ? 28.995  55.530  104.893 1.00 99.69  ? 128 ARG   F NH1   1 
ATOM   12144 N  NH2   . ARG   E 4  128 ? 30.686  57.002  105.366 1.00 114.17 ? 128 ARG   F NH2   1 
ATOM   12145 N  N     . GLU   E 4  129 ? 26.245  61.880  108.050 1.00 83.25  ? 129 GLU   F N     1 
ATOM   12146 C  CA    . GLU   E 4  129 ? 26.277  62.636  109.299 1.00 98.72  ? 129 GLU   F CA    1 
ATOM   12147 C  C     . GLU   E 4  129 ? 24.894  63.173  109.650 1.00 99.49  ? 129 GLU   F C     1 
ATOM   12148 O  O     . GLU   E 4  129 ? 24.413  62.999  110.777 1.00 101.24 ? 129 GLU   F O     1 
ATOM   12149 C  CB    . GLU   E 4  129 ? 27.282  63.786  109.197 1.00 103.19 ? 129 GLU   F CB    1 
ATOM   12150 C  CG    . GLU   E 4  129 ? 28.735  63.383  109.417 1.00 100.10 ? 129 GLU   F CG    1 
ATOM   12151 C  CD    . GLU   E 4  129 ? 28.991  62.872  110.820 1.00 107.54 ? 129 GLU   F CD    1 
ATOM   12152 O  OE1   . GLU   E 4  129 ? 28.235  61.994  111.287 1.00 104.16 ? 129 GLU   F OE1   1 
ATOM   12153 O  OE2   . GLU   E 4  129 ? 29.947  63.357  111.460 1.00 117.98 ? 129 GLU   F OE2   1 
ATOM   12154 N  N     . VAL   E 4  130 ? 24.238  63.835  108.695 1.00 93.58  ? 130 VAL   F N     1 
ATOM   12155 C  CA    . VAL   E 4  130 ? 22.923  64.403  108.960 1.00 92.50  ? 130 VAL   F CA    1 
ATOM   12156 C  C     . VAL   E 4  130 ? 21.909  63.328  109.351 1.00 95.78  ? 130 VAL   F C     1 
ATOM   12157 O  O     . VAL   E 4  130 ? 20.925  63.633  110.039 1.00 88.11  ? 130 VAL   F O     1 
ATOM   12158 C  CB    . VAL   E 4  130 ? 22.456  65.211  107.732 1.00 89.99  ? 130 VAL   F CB    1 
ATOM   12159 C  CG1   . VAL   E 4  130 ? 21.449  66.263  108.140 1.00 75.32  ? 130 VAL   F CG1   1 
ATOM   12160 C  CG2   . VAL   E 4  130 ? 23.651  65.860  107.045 1.00 95.49  ? 130 VAL   F CG2   1 
ATOM   12161 N  N     . PHE   E 4  131 ? 22.139  62.066  108.948 1.00 94.64  ? 131 PHE   F N     1 
ATOM   12162 C  CA    . PHE   E 4  131 ? 21.210  60.974  109.265 1.00 93.75  ? 131 PHE   F CA    1 
ATOM   12163 C  C     . PHE   E 4  131 ? 21.255  60.613  110.747 1.00 95.59  ? 131 PHE   F C     1 
ATOM   12164 O  O     . PHE   E 4  131 ? 20.233  60.645  111.446 1.00 89.76  ? 131 PHE   F O     1 
ATOM   12165 C  CB    . PHE   E 4  131 ? 21.523  59.731  108.418 1.00 89.94  ? 131 PHE   F CB    1 
ATOM   12166 C  CG    . PHE   E 4  131 ? 21.036  58.431  109.038 1.00 92.20  ? 131 PHE   F CG    1 
ATOM   12167 C  CD1   . PHE   E 4  131 ? 19.677  58.170  109.169 1.00 89.52  ? 131 PHE   F CD1   1 
ATOM   12168 C  CD2   . PHE   E 4  131 ? 21.933  57.481  109.496 1.00 84.18  ? 131 PHE   F CD2   1 
ATOM   12169 C  CE1   . PHE   E 4  131 ? 19.226  56.992  109.741 1.00 84.56  ? 131 PHE   F CE1   1 
ATOM   12170 C  CE2   . PHE   E 4  131 ? 21.485  56.302  110.060 1.00 85.88  ? 131 PHE   F CE2   1 
ATOM   12171 C  CZ    . PHE   E 4  131 ? 20.130  56.058  110.182 1.00 89.48  ? 131 PHE   F CZ    1 
ATOM   12172 N  N     . LEU   E 4  132 ? 22.431  60.214  111.229 1.00 93.69  ? 132 LEU   F N     1 
ATOM   12173 C  CA    . LEU   E 4  132 ? 22.603  59.966  112.651 1.00 86.88  ? 132 LEU   F CA    1 
ATOM   12174 C  C     . LEU   E 4  132 ? 22.064  61.129  113.474 1.00 89.36  ? 132 LEU   F C     1 
ATOM   12175 O  O     . LEU   E 4  132 ? 21.403  60.922  114.498 1.00 94.06  ? 132 LEU   F O     1 
ATOM   12176 C  CB    . LEU   E 4  132 ? 24.080  59.717  112.930 1.00 81.67  ? 132 LEU   F CB    1 
ATOM   12177 C  CG    . LEU   E 4  132 ? 24.579  58.591  112.027 1.00 78.31  ? 132 LEU   F CG    1 
ATOM   12178 C  CD1   . LEU   E 4  132 ? 26.011  58.835  111.608 1.00 78.53  ? 132 LEU   F CD1   1 
ATOM   12179 C  CD2   . LEU   E 4  132 ? 24.441  57.249  112.723 1.00 72.12  ? 132 LEU   F CD2   1 
ATOM   12180 N  N     . ALA   E 4  133 ? 22.317  62.360  113.013 1.00 91.96  ? 133 ALA   F N     1 
ATOM   12181 C  CA    . ALA   E 4  133 ? 21.817  63.583  113.643 1.00 91.61  ? 133 ALA   F CA    1 
ATOM   12182 C  C     . ALA   E 4  133 ? 20.415  63.435  114.235 1.00 97.75  ? 133 ALA   F C     1 
ATOM   12183 O  O     . ALA   E 4  133 ? 20.166  63.829  115.381 1.00 99.96  ? 133 ALA   F O     1 
ATOM   12184 C  CB    . ALA   E 4  133 ? 21.838  64.724  112.620 1.00 81.22  ? 133 ALA   F CB    1 
ATOM   12185 N  N     . ALA   E 4  134 ? 19.478  62.892  113.463 1.00 95.52  ? 134 ALA   F N     1 
ATOM   12186 C  CA    . ALA   E 4  134 ? 18.160  62.606  114.006 1.00 88.55  ? 134 ALA   F CA    1 
ATOM   12187 C  C     . ALA   E 4  134 ? 18.069  61.216  114.623 1.00 90.86  ? 134 ALA   F C     1 
ATOM   12188 O  O     . ALA   E 4  134 ? 17.095  60.938  115.331 1.00 96.86  ? 134 ALA   F O     1 
ATOM   12189 C  CB    . ALA   E 4  134 ? 17.089  62.765  112.924 1.00 86.56  ? 134 ALA   F CB    1 
ATOM   12190 N  N     . TYR   E 4  135 ? 19.055  60.344  114.384 1.00 89.05  ? 135 TYR   F N     1 
ATOM   12191 C  CA    . TYR   E 4  135 ? 19.087  59.018  115.006 1.00 93.76  ? 135 TYR   F CA    1 
ATOM   12192 C  C     . TYR   E 4  135 ? 19.471  59.176  116.476 1.00 94.91  ? 135 TYR   F C     1 
ATOM   12193 O  O     . TYR   E 4  135 ? 20.651  59.319  116.823 1.00 81.94  ? 135 TYR   F O     1 
ATOM   12194 C  CB    . TYR   E 4  135 ? 20.056  58.097  114.270 1.00 84.19  ? 135 TYR   F CB    1 
ATOM   12195 C  CG    . TYR   E 4  135 ? 19.977  56.637  114.688 1.00 80.32  ? 135 TYR   F CG    1 
ATOM   12196 C  CD1   . TYR   E 4  135 ? 19.102  56.214  115.687 1.00 84.65  ? 135 TYR   F CD1   1 
ATOM   12197 C  CD2   . TYR   E 4  135 ? 20.786  55.682  114.085 1.00 85.23  ? 135 TYR   F CD2   1 
ATOM   12198 C  CE1   . TYR   E 4  135 ? 19.035  54.878  116.070 1.00 90.60  ? 135 TYR   F CE1   1 
ATOM   12199 C  CE2   . TYR   E 4  135 ? 20.727  54.346  114.458 1.00 92.46  ? 135 TYR   F CE2   1 
ATOM   12200 C  CZ    . TYR   E 4  135 ? 19.853  53.947  115.448 1.00 95.03  ? 135 TYR   F CZ    1 
ATOM   12201 O  OH    . TYR   E 4  135 ? 19.805  52.612  115.804 1.00 83.02  ? 135 TYR   F OH    1 
ATOM   12202 N  N     . ASN   E 4  136 ? 18.468  59.155  117.352 1.00 90.87  ? 136 ASN   F N     1 
ATOM   12203 C  CA    . ASN   E 4  136 ? 18.727  59.343  118.771 1.00 96.00  ? 136 ASN   F CA    1 
ATOM   12204 C  C     . ASN   E 4  136 ? 17.463  59.046  119.570 1.00 91.51  ? 136 ASN   F C     1 
ATOM   12205 O  O     . ASN   E 4  136 ? 16.352  58.980  119.030 1.00 75.03  ? 136 ASN   F O     1 
ATOM   12206 C  CB    . ASN   E 4  136 ? 19.240  60.763  119.072 1.00 92.58  ? 136 ASN   F CB    1 
ATOM   12207 C  CG    . ASN   E 4  136 ? 18.263  61.845  118.644 1.00 87.34  ? 136 ASN   F CG    1 
ATOM   12208 O  OD1   . ASN   E 4  136 ? 17.156  61.940  119.171 1.00 81.43  ? 136 ASN   F OD1   1 
ATOM   12209 N  ND2   . ASN   E 4  136 ? 18.673  62.671  117.690 1.00 84.84  ? 136 ASN   F ND2   1 
ATOM   12210 N  N     . ARG   E 4  137 ? 17.670  58.874  120.874 1.00 94.86  ? 137 ARG   F N     1 
ATOM   12211 C  CA    . ARG   E 4  137 ? 16.638  58.506  121.831 1.00 88.74  ? 137 ARG   F CA    1 
ATOM   12212 C  C     . ARG   E 4  137 ? 16.521  59.546  122.948 1.00 76.85  ? 137 ARG   F C     1 
ATOM   12213 O  O     . ARG   E 4  137 ? 17.001  60.670  122.821 1.00 77.48  ? 137 ARG   F O     1 
ATOM   12214 C  CB    . ARG   E 4  137 ? 16.956  57.127  122.421 1.00 85.88  ? 137 ARG   F CB    1 
ATOM   12215 C  CG    . ARG   E 4  137 ? 16.165  56.750  123.661 1.00 80.64  ? 137 ARG   F CG    1 
ATOM   12216 C  CD    . ARG   E 4  137 ? 14.670  56.797  123.408 1.00 84.28  ? 137 ARG   F CD    1 
ATOM   12217 N  NE    . ARG   E 4  137 ? 14.160  58.158  123.508 1.00 78.22  ? 137 ARG   F NE    1 
ATOM   12218 C  CZ    . ARG   E 4  137 ? 12.943  58.532  123.145 1.00 78.83  ? 137 ARG   F CZ    1 
ATOM   12219 N  NH1   . ARG   E 4  137 ? 12.072  57.665  122.648 1.00 88.85  ? 137 ARG   F NH1   1 
ATOM   12220 N  NH2   . ARG   E 4  137 ? 12.592  59.810  123.278 1.00 59.63  ? 137 ARG   F NH2   1 
ATOM   12221 N  N     . GLY   E 4  144 ? 11.931  55.587  119.787 1.00 44.89  ? 144 GLY   F N     1 
ATOM   12222 C  CA    . GLY   E 4  144 ? 12.182  54.321  119.112 1.00 79.44  ? 144 GLY   F CA    1 
ATOM   12223 C  C     . GLY   E 4  144 ? 12.516  54.485  117.638 1.00 79.12  ? 144 GLY   F C     1 
ATOM   12224 O  O     . GLY   E 4  144 ? 11.801  55.169  116.918 1.00 83.31  ? 144 GLY   F O     1 
ATOM   12225 N  N     . ASN   E 4  145 ? 13.596  53.864  117.166 1.00 76.61  ? 145 ASN   F N     1 
ATOM   12226 C  CA    . ASN   E 4  145 ? 14.186  54.234  115.880 1.00 78.21  ? 145 ASN   F CA    1 
ATOM   12227 C  C     . ASN   E 4  145 ? 14.474  53.002  115.024 1.00 77.39  ? 145 ASN   F C     1 
ATOM   12228 O  O     . ASN   E 4  145 ? 15.527  52.377  115.170 1.00 85.33  ? 145 ASN   F O     1 
ATOM   12229 C  CB    . ASN   E 4  145 ? 15.458  55.052  116.106 1.00 81.01  ? 145 ASN   F CB    1 
ATOM   12230 C  CG    . ASN   E 4  145 ? 15.224  56.274  117.003 1.00 95.31  ? 145 ASN   F CG    1 
ATOM   12231 O  OD1   . ASN   E 4  145 ? 14.082  56.648  117.293 1.00 93.63  ? 145 ASN   F OD1   1 
ATOM   12232 N  ND2   . ASN   E 4  145 ? 16.314  56.905  117.438 1.00 89.84  ? 145 ASN   F ND2   1 
ATOM   12233 N  N     . VAL   E 4  146 ? 13.560  52.673  114.108 1.00 72.95  ? 146 VAL   F N     1 
ATOM   12234 C  CA    . VAL   E 4  146 ? 13.776  51.638  113.102 1.00 75.21  ? 146 VAL   F CA    1 
ATOM   12235 C  C     . VAL   E 4  146 ? 13.756  52.280  111.720 1.00 78.22  ? 146 VAL   F C     1 
ATOM   12236 O  O     . VAL   E 4  146 ? 12.900  53.127  111.428 1.00 75.56  ? 146 VAL   F O     1 
ATOM   12237 C  CB    . VAL   E 4  146 ? 12.717  50.518  113.178 1.00 66.16  ? 146 VAL   F CB    1 
ATOM   12238 C  CG1   . VAL   E 4  146 ? 13.104  49.359  112.264 1.00 67.64  ? 146 VAL   F CG1   1 
ATOM   12239 C  CG2   . VAL   E 4  146 ? 12.530  50.062  114.598 1.00 72.46  ? 146 VAL   F CG2   1 
ATOM   12240 N  N     . TRP   E 4  147 ? 14.677  51.847  110.858 1.00 74.62  ? 147 TRP   F N     1 
ATOM   12241 C  CA    . TRP   E 4  147 ? 14.783  52.396  109.510 1.00 74.83  ? 147 TRP   F CA    1 
ATOM   12242 C  C     . TRP   E 4  147 ? 14.894  51.291  108.458 1.00 69.88  ? 147 TRP   F C     1 
ATOM   12243 O  O     . TRP   E 4  147 ? 14.696  50.113  108.776 1.00 74.59  ? 147 TRP   F O     1 
ATOM   12244 C  CB    . TRP   E 4  147 ? 15.977  53.343  109.430 1.00 77.47  ? 147 TRP   F CB    1 
ATOM   12245 C  CG    . TRP   E 4  147 ? 16.085  54.270  110.614 1.00 80.09  ? 147 TRP   F CG    1 
ATOM   12246 C  CD1   . TRP   E 4  147 ? 16.479  53.939  111.880 1.00 90.58  ? 147 TRP   F CD1   1 
ATOM   12247 C  CD2   . TRP   E 4  147 ? 15.817  55.678  110.638 1.00 80.03  ? 147 TRP   F CD2   1 
ATOM   12248 N  NE1   . TRP   E 4  147 ? 16.461  55.048  112.693 1.00 88.48  ? 147 TRP   F NE1   1 
ATOM   12249 C  CE2   . TRP   E 4  147 ? 16.065  56.130  111.954 1.00 81.88  ? 147 TRP   F CE2   1 
ATOM   12250 C  CE3   . TRP   E 4  147 ? 15.390  56.601  109.678 1.00 80.77  ? 147 TRP   F CE3   1 
ATOM   12251 C  CZ2   . TRP   E 4  147 ? 15.900  57.460  112.331 1.00 81.89  ? 147 TRP   F CZ2   1 
ATOM   12252 C  CZ3   . TRP   E 4  147 ? 15.225  57.922  110.055 1.00 77.46  ? 147 TRP   F CZ3   1 
ATOM   12253 C  CH2   . TRP   E 4  147 ? 15.479  58.338  111.372 1.00 75.57  ? 147 TRP   F CH2   1 
ATOM   12254 N  N     . ILE   E 4  148 ? 15.208  51.655  107.211 1.00 70.81  ? 148 ILE   F N     1 
ATOM   12255 C  CA    . ILE   E 4  148 ? 15.177  50.713  106.090 1.00 71.30  ? 148 ILE   F CA    1 
ATOM   12256 C  C     . ILE   E 4  148 ? 16.160  51.162  105.004 1.00 64.53  ? 148 ILE   F C     1 
ATOM   12257 O  O     . ILE   E 4  148 ? 16.535  52.331  104.927 1.00 64.13  ? 148 ILE   F O     1 
ATOM   12258 C  CB    . ILE   E 4  148 ? 13.737  50.584  105.529 1.00 59.55  ? 148 ILE   F CB    1 
ATOM   12259 C  CG1   . ILE   E 4  148 ? 13.644  49.421  104.544 1.00 59.39  ? 148 ILE   F CG1   1 
ATOM   12260 C  CG2   . ILE   E 4  148 ? 13.319  51.864  104.849 1.00 48.86  ? 148 ILE   F CG2   1 
ATOM   12261 C  CD1   . ILE   E 4  148 ? 12.248  49.066  104.156 1.00 39.66  ? 148 ILE   F CD1   1 
ATOM   12262 N  N     . ALA   E 4  149 ? 16.554  50.226  104.140 1.00 63.18  ? 149 ALA   F N     1 
ATOM   12263 C  CA    . ALA   E 4  149 ? 17.530  50.487  103.078 1.00 57.95  ? 149 ALA   F CA    1 
ATOM   12264 C  C     . ALA   E 4  149 ? 16.916  50.478  101.666 1.00 68.10  ? 149 ALA   F C     1 
ATOM   12265 O  O     . ALA   E 4  149 ? 17.375  51.180  100.748 1.00 65.72  ? 149 ALA   F O     1 
ATOM   12266 C  CB    . ALA   E 4  149 ? 18.645  49.476  103.167 1.00 57.81  ? 149 ALA   F CB    1 
ATOM   12267 N  N     . GLY   E 4  159 ? 17.956  41.758  97.967  1.00 70.58  ? 159 GLY   F N     1 
ATOM   12268 C  CA    . GLY   E 4  159 ? 16.890  42.599  98.484  1.00 73.78  ? 159 GLY   F CA    1 
ATOM   12269 C  C     . GLY   E 4  159 ? 17.366  43.914  99.074  1.00 75.41  ? 159 GLY   F C     1 
ATOM   12270 O  O     . GLY   E 4  159 ? 18.157  44.633  98.450  1.00 70.37  ? 159 GLY   F O     1 
ATOM   12271 N  N     . ILE   E 4  160 ? 16.881  44.211  100.288 1.00 84.15  ? 160 ILE   F N     1 
ATOM   12272 C  CA    . ILE   E 4  160 ? 17.190  45.442  101.017 1.00 89.15  ? 160 ILE   F CA    1 
ATOM   12273 C  C     . ILE   E 4  160 ? 17.221  45.133  102.512 1.00 84.93  ? 160 ILE   F C     1 
ATOM   12274 O  O     . ILE   E 4  160 ? 16.643  44.147  102.973 1.00 85.38  ? 160 ILE   F O     1 
ATOM   12275 C  CB    . ILE   E 4  160 ? 16.161  46.559  100.703 1.00 83.35  ? 160 ILE   F CB    1 
ATOM   12276 C  CG1   . ILE   E 4  160 ? 16.578  47.319  99.444  1.00 88.26  ? 160 ILE   F CG1   1 
ATOM   12277 C  CG2   . ILE   E 4  160 ? 15.988  47.505  101.883 1.00 73.59  ? 160 ILE   F CG2   1 
ATOM   12278 C  CD1   . ILE   E 4  160 ? 17.947  47.954  99.559  1.00 88.56  ? 160 ILE   F CD1   1 
ATOM   12279 N  N     . LEU   E 4  161 ? 17.895  45.991  103.282 1.00 81.79  ? 161 LEU   F N     1 
ATOM   12280 C  CA    . LEU   E 4  161 ? 18.131  45.750  104.705 1.00 88.69  ? 161 LEU   F CA    1 
ATOM   12281 C  C     . LEU   E 4  161 ? 17.274  46.664  105.583 1.00 84.67  ? 161 LEU   F C     1 
ATOM   12282 O  O     . LEU   E 4  161 ? 17.394  47.891  105.502 1.00 85.84  ? 161 LEU   F O     1 
ATOM   12283 C  CB    . LEU   E 4  161 ? 19.607  45.951  105.043 1.00 85.99  ? 161 LEU   F CB    1 
ATOM   12284 C  CG    . LEU   E 4  161 ? 19.817  45.944  106.556 1.00 79.21  ? 161 LEU   F CG    1 
ATOM   12285 C  CD1   . LEU   E 4  161 ? 19.436  44.580  107.091 1.00 80.98  ? 161 LEU   F CD1   1 
ATOM   12286 C  CD2   . LEU   E 4  161 ? 21.237  46.327  106.943 1.00 81.63  ? 161 LEU   F CD2   1 
ATOM   12287 N  N     . ILE   E 4  162 ? 16.433  46.059  106.452 1.00 82.45  ? 162 ILE   F N     1 
ATOM   12288 C  CA    . ILE   E 4  162 ? 15.740  46.760  107.540 1.00 81.60  ? 162 ILE   F CA    1 
ATOM   12289 C  C     . ILE   E 4  162 ? 16.479  46.478  108.842 1.00 86.00  ? 162 ILE   F C     1 
ATOM   12290 O  O     . ILE   E 4  162 ? 16.870  45.331  109.106 1.00 89.69  ? 162 ILE   F O     1 
ATOM   12291 C  CB    . ILE   E 4  162 ? 14.264  46.323  107.680 1.00 78.11  ? 162 ILE   F CB    1 
ATOM   12292 C  CG1   . ILE   E 4  162 ? 13.655  45.871  106.353 1.00 79.45  ? 162 ILE   F CG1   1 
ATOM   12293 C  CG2   . ILE   E 4  162 ? 13.429  47.428  108.307 1.00 69.93  ? 162 ILE   F CG2   1 
ATOM   12294 C  CD1   . ILE   E 4  162 ? 12.292  45.205  106.516 1.00 70.80  ? 162 ILE   F CD1   1 
ATOM   12295 N  N     . SER   E 4  163 ? 16.651  47.505  109.671 1.00 79.06  ? 163 SER   F N     1 
ATOM   12296 C  CA    . SER   E 4  163 ? 17.301  47.322  110.964 1.00 68.38  ? 163 SER   F CA    1 
ATOM   12297 C  C     . SER   E 4  163 ? 17.198  48.608  111.766 1.00 78.00  ? 163 SER   F C     1 
ATOM   12298 O  O     . SER   E 4  163 ? 17.227  49.706  111.209 1.00 84.51  ? 163 SER   F O     1 
ATOM   12299 C  CB    . SER   E 4  163 ? 18.773  46.919  110.809 1.00 77.74  ? 163 SER   F CB    1 
ATOM   12300 O  OG    . SER   E 4  163 ? 19.420  46.782  112.070 1.00 96.18  ? 163 SER   F OG    1 
ATOM   12301 N  N     . SER   E 4  164 ? 17.085  48.453  113.080 1.00 86.02  ? 164 SER   F N     1 
ATOM   12302 C  CA    . SER   E 4  164 ? 16.982  49.574  114.002 1.00 85.62  ? 164 SER   F CA    1 
ATOM   12303 C  C     . SER   E 4  164 ? 18.344  50.089  114.458 1.00 89.98  ? 164 SER   F C     1 
ATOM   12304 O  O     . SER   E 4  164 ? 18.411  50.927  115.366 1.00 83.37  ? 164 SER   F O     1 
ATOM   12305 C  CB    . SER   E 4  164 ? 16.142  49.166  115.216 1.00 91.34  ? 164 SER   F CB    1 
ATOM   12306 O  OG    . SER   E 4  164 ? 16.467  47.849  115.642 1.00 92.92  ? 164 SER   F OG    1 
ATOM   12307 N  N     . GLU   E 4  165 ? 19.425  49.607  113.856 1.00 87.08  ? 165 GLU   F N     1 
ATOM   12308 C  CA    . GLU   E 4  165 ? 20.774  49.969  114.258 1.00 94.11  ? 165 GLU   F CA    1 
ATOM   12309 C  C     . GLU   E 4  165 ? 21.488  50.618  113.087 1.00 97.76  ? 165 GLU   F C     1 
ATOM   12310 O  O     . GLU   E 4  165 ? 21.438  50.099  111.966 1.00 97.81  ? 165 GLU   F O     1 
ATOM   12311 C  CB    . GLU   E 4  165 ? 21.558  48.744  114.727 1.00 106.77 ? 165 GLU   F CB    1 
ATOM   12312 C  CG    . GLU   E 4  165 ? 22.824  49.093  115.499 1.00 111.76 ? 165 GLU   F CG    1 
ATOM   12313 C  CD    . GLU   E 4  165 ? 22.529  49.794  116.816 1.00 103.32 ? 165 GLU   F CD    1 
ATOM   12314 O  OE1   . GLU   E 4  165 ? 23.111  50.871  117.063 1.00 102.84 ? 165 GLU   F OE1   1 
ATOM   12315 O  OE2   . GLU   E 4  165 ? 21.715  49.271  117.602 1.00 104.95 ? 165 GLU   F OE2   1 
ATOM   12316 N  N     . ALA   E 4  166 ? 22.155  51.745  113.351 1.00 98.90  ? 166 ALA   F N     1 
ATOM   12317 C  CA    . ALA   E 4  166 ? 22.890  52.442  112.299 1.00 103.20 ? 166 ALA   F CA    1 
ATOM   12318 C  C     . ALA   E 4  166 ? 23.956  51.537  111.685 1.00 105.78 ? 166 ALA   F C     1 
ATOM   12319 O  O     . ALA   E 4  166 ? 23.961  51.293  110.472 1.00 107.16 ? 166 ALA   F O     1 
ATOM   12320 C  CB    . ALA   E 4  166 ? 23.507  53.729  112.851 1.00 89.86  ? 166 ALA   F CB    1 
ATOM   12321 N  N     . SER   E 4  167 ? 24.870  51.027  112.507 1.00 106.88 ? 167 SER   F N     1 
ATOM   12322 C  CA    . SER   E 4  167 ? 25.806  50.021  112.028 1.00 108.08 ? 167 SER   F CA    1 
ATOM   12323 C  C     . SER   E 4  167 ? 25.043  48.846  111.414 1.00 111.02 ? 167 SER   F C     1 
ATOM   12324 O  O     . SER   E 4  167 ? 23.843  48.655  111.648 1.00 111.07 ? 167 SER   F O     1 
ATOM   12325 C  CB    . SER   E 4  167 ? 26.715  49.547  113.168 1.00 115.95 ? 167 SER   F CB    1 
ATOM   12326 O  OG    . SER   E 4  167 ? 25.975  49.171  114.320 1.00 115.34 ? 167 SER   F OG    1 
ATOM   12327 N  N     . GLU   E 4  168 ? 25.749  48.063  110.595 1.00 113.35 ? 168 GLU   F N     1 
ATOM   12328 C  CA    . GLU   E 4  168 ? 25.139  46.955  109.863 1.00 112.55 ? 168 GLU   F CA    1 
ATOM   12329 C  C     . GLU   E 4  168 ? 24.237  47.498  108.761 1.00 108.22 ? 168 GLU   F C     1 
ATOM   12330 O  O     . GLU   E 4  168 ? 24.097  46.879  107.701 1.00 109.17 ? 168 GLU   F O     1 
ATOM   12331 C  CB    . GLU   E 4  168 ? 24.335  46.035  110.794 1.00 119.19 ? 168 GLU   F CB    1 
ATOM   12332 C  CG    . GLU   E 4  168 ? 25.132  45.418  111.940 1.00 118.62 ? 168 GLU   F CG    1 
ATOM   12333 C  CD    . GLU   E 4  168 ? 24.712  45.960  113.298 1.00 123.17 ? 168 GLU   F CD    1 
ATOM   12334 O  OE1   . GLU   E 4  168 ? 23.489  46.081  113.544 1.00 121.24 ? 168 GLU   F OE1   1 
ATOM   12335 O  OE2   . GLU   E 4  168 ? 25.606  46.277  114.113 1.00 128.10 ? 168 GLU   F OE2   1 
ATOM   12336 N  N     . LEU   E 4  169 ? 23.615  48.651  109.018 1.00 107.64 ? 169 LEU   F N     1 
ATOM   12337 C  CA    . LEU   E 4  169 ? 22.768  49.348  108.054 1.00 96.97  ? 169 LEU   F CA    1 
ATOM   12338 C  C     . LEU   E 4  169 ? 23.611  50.265  107.167 1.00 98.39  ? 169 LEU   F C     1 
ATOM   12339 O  O     . LEU   E 4  169 ? 23.718  50.035  105.959 1.00 99.64  ? 169 LEU   F O     1 
ATOM   12340 C  CB    . LEU   E 4  169 ? 21.669  50.137  108.792 1.00 97.83  ? 169 LEU   F CB    1 
ATOM   12341 C  CG    . LEU   E 4  169 ? 20.302  50.456  108.154 1.00 91.43  ? 169 LEU   F CG    1 
ATOM   12342 C  CD1   . LEU   E 4  169 ? 19.522  49.185  107.775 1.00 82.94  ? 169 LEU   F CD1   1 
ATOM   12343 C  CD2   . LEU   E 4  169 ? 19.462  51.355  109.060 1.00 69.40  ? 169 LEU   F CD2   1 
ATOM   12344 N  N     . LEU   E 4  170 ? 24.230  51.295  107.757 1.00 100.92 ? 170 LEU   F N     1 
ATOM   12345 C  CA    . LEU   E 4  170 ? 25.033  52.224  106.963 1.00 92.04  ? 170 LEU   F CA    1 
ATOM   12346 C  C     . LEU   E 4  170 ? 26.128  51.486  106.213 1.00 98.32  ? 170 LEU   F C     1 
ATOM   12347 O  O     . LEU   E 4  170 ? 26.385  51.767  105.037 1.00 97.72  ? 170 LEU   F O     1 
ATOM   12348 C  CB    . LEU   E 4  170 ? 25.653  53.310  107.846 1.00 84.52  ? 170 LEU   F CB    1 
ATOM   12349 C  CG    . LEU   E 4  170 ? 24.845  53.933  108.989 1.00 97.29  ? 170 LEU   F CG    1 
ATOM   12350 C  CD1   . LEU   E 4  170 ? 25.610  55.081  109.642 1.00 85.50  ? 170 LEU   F CD1   1 
ATOM   12351 C  CD2   . LEU   E 4  170 ? 23.474  54.398  108.516 1.00 106.28 ? 170 LEU   F CD2   1 
ATOM   12352 N  N     . ASP   E 4  171 ? 26.783  50.527  106.876 1.00 106.52 ? 171 ASP   F N     1 
ATOM   12353 C  CA    . ASP   E 4  171 ? 27.884  49.814  106.237 1.00 107.54 ? 171 ASP   F CA    1 
ATOM   12354 C  C     . ASP   E 4  171 ? 27.386  48.827  105.183 1.00 108.30 ? 171 ASP   F C     1 
ATOM   12355 O  O     . ASP   E 4  171 ? 28.083  48.584  104.187 1.00 105.76 ? 171 ASP   F O     1 
ATOM   12356 C  CB    . ASP   E 4  171 ? 28.753  49.114  107.292 1.00 99.04  ? 171 ASP   F CB    1 
ATOM   12357 C  CG    . ASP   E 4  171 ? 28.055  48.958  108.635 1.00 102.25 ? 171 ASP   F CG    1 
ATOM   12358 O  OD1   . ASP   E 4  171 ? 26.807  49.036  108.678 1.00 97.47  ? 171 ASP   F OD1   1 
ATOM   12359 O  OD2   . ASP   E 4  171 ? 28.772  48.758  109.647 1.00 93.36  ? 171 ASP   F OD2   1 
ATOM   12360 N  N     . PHE   E 4  172 ? 26.189  48.260  105.374 1.00 106.33 ? 172 PHE   F N     1 
ATOM   12361 C  CA    . PHE   E 4  172 ? 25.579  47.434  104.333 1.00 100.90 ? 172 PHE   F CA    1 
ATOM   12362 C  C     . PHE   E 4  172 ? 25.607  48.148  102.988 1.00 101.71 ? 172 PHE   F C     1 
ATOM   12363 O  O     . PHE   E 4  172 ? 26.101  47.609  101.991 1.00 101.77 ? 172 PHE   F O     1 
ATOM   12364 C  CB    . PHE   E 4  172 ? 24.142  47.074  104.726 1.00 95.92  ? 172 PHE   F CB    1 
ATOM   12365 C  CG    . PHE   E 4  172 ? 23.330  46.456  103.614 1.00 91.52  ? 172 PHE   F CG    1 
ATOM   12366 C  CD1   . PHE   E 4  172 ? 23.427  45.105  103.335 1.00 92.00  ? 172 PHE   F CD1   1 
ATOM   12367 C  CD2   . PHE   E 4  172 ? 22.454  47.225  102.865 1.00 90.96  ? 172 PHE   F CD2   1 
ATOM   12368 C  CE1   . PHE   E 4  172 ? 22.678  44.540  102.322 1.00 95.26  ? 172 PHE   F CE1   1 
ATOM   12369 C  CE2   . PHE   E 4  172 ? 21.705  46.663  101.852 1.00 88.03  ? 172 PHE   F CE2   1 
ATOM   12370 C  CZ    . PHE   E 4  172 ? 21.816  45.321  101.581 1.00 94.86  ? 172 PHE   F CZ    1 
ATOM   12371 N  N     . ILE   E 4  173 ? 25.076  49.373  102.948 1.00 103.79 ? 173 ILE   F N     1 
ATOM   12372 C  CA    . ILE   E 4  173 ? 25.100  50.167  101.724 1.00 100.52 ? 173 ILE   F CA    1 
ATOM   12373 C  C     . ILE   E 4  173 ? 26.508  50.683  101.458 1.00 105.90 ? 173 ILE   F C     1 
ATOM   12374 O  O     . ILE   E 4  173 ? 26.943  50.775  100.300 1.00 107.71 ? 173 ILE   F O     1 
ATOM   12375 C  CB    . ILE   E 4  173 ? 24.066  51.310  101.820 1.00 97.53  ? 173 ILE   F CB    1 
ATOM   12376 C  CG1   . ILE   E 4  173 ? 24.263  52.357  100.721 1.00 98.31  ? 173 ILE   F CG1   1 
ATOM   12377 C  CG2   . ILE   E 4  173 ? 24.101  51.959  103.194 1.00 90.46  ? 173 ILE   F CG2   1 
ATOM   12378 C  CD1   . ILE   E 4  173 ? 23.201  53.450  100.739 1.00 90.66  ? 173 ILE   F CD1   1 
ATOM   12379 N  N     . ASP   E 4  174 ? 27.252  50.996  102.527 1.00 105.23 ? 174 ASP   F N     1 
ATOM   12380 C  CA    . ASP   E 4  174 ? 28.606  51.514  102.362 1.00 99.25  ? 174 ASP   F CA    1 
ATOM   12381 C  C     . ASP   E 4  174 ? 29.496  50.526  101.619 1.00 99.58  ? 174 ASP   F C     1 
ATOM   12382 O  O     . ASP   E 4  174 ? 30.478  50.927  100.986 1.00 96.70  ? 174 ASP   F O     1 
ATOM   12383 C  CB    . ASP   E 4  174 ? 29.209  51.874  103.721 1.00 90.44  ? 174 ASP   F CB    1 
ATOM   12384 C  CG    . ASP   E 4  174 ? 30.157  53.058  103.634 1.00 88.80  ? 174 ASP   F CG    1 
ATOM   12385 O  OD1   . ASP   E 4  174 ? 29.678  54.207  103.626 1.00 90.56  ? 174 ASP   F OD1   1 
ATOM   12386 O  OD2   . ASP   E 4  174 ? 31.385  52.849  103.558 1.00 90.03  ? 174 ASP   F OD2   1 
ATOM   12387 N  N     . GLU   E 4  175 ? 29.193  49.234  101.702 1.00 103.20 ? 175 GLU   F N     1 
ATOM   12388 C  CA    . GLU   E 4  175 ? 29.798  48.280  100.786 1.00 102.08 ? 175 GLU   F CA    1 
ATOM   12389 C  C     . GLU   E 4  175 ? 29.038  48.206  99.474  1.00 103.55 ? 175 GLU   F C     1 
ATOM   12390 O  O     . GLU   E 4  175 ? 29.646  47.983  98.421  1.00 110.09 ? 175 GLU   F O     1 
ATOM   12391 C  CB    . GLU   E 4  175 ? 29.843  46.874  101.408 1.00 102.31 ? 175 GLU   F CB    1 
ATOM   12392 C  CG    . GLU   E 4  175 ? 28.487  46.180  101.604 1.00 104.06 ? 175 GLU   F CG    1 
ATOM   12393 C  CD    . GLU   E 4  175 ? 28.025  45.388  100.385 1.00 114.93 ? 175 GLU   F CD    1 
ATOM   12394 O  OE1   . GLU   E 4  175 ? 28.781  45.201  99.399  1.00 117.27 ? 175 GLU   F OE1   1 
ATOM   12395 O  OE2   . GLU   E 4  175 ? 26.874  44.947  100.404 1.00 118.39 ? 175 GLU   F OE2   1 
ATOM   12396 N  N     . GLN   E 4  176 ? 27.716  48.409  99.515  1.00 109.87 ? 176 GLN   F N     1 
ATOM   12397 C  CA    . GLN   E 4  176 ? 26.838  47.824  98.497  1.00 119.18 ? 176 GLN   F CA    1 
ATOM   12398 C  C     . GLN   E 4  176 ? 27.327  48.105  97.075  1.00 117.54 ? 176 GLN   F C     1 
ATOM   12399 O  O     . GLN   E 4  176 ? 27.233  47.238  96.194  1.00 113.63 ? 176 GLN   F O     1 
ATOM   12400 C  CB    . GLN   E 4  176 ? 25.392  48.313  98.675  1.00 120.21 ? 176 GLN   F CB    1 
ATOM   12401 C  CG    . GLN   E 4  176 ? 24.340  47.191  98.652  1.00 108.87 ? 176 GLN   F CG    1 
ATOM   12402 C  CD    . GLN   E 4  176 ? 22.922  47.733  98.649  1.00 125.03 ? 176 GLN   F CD    1 
ATOM   12403 O  OE1   . GLN   E 4  176 ? 22.717  48.951  98.652  1.00 126.25 ? 176 GLN   F OE1   1 
ATOM   12404 N  NE2   . GLN   E 4  176 ? 21.934  46.836  98.640  1.00 118.23 ? 176 GLN   F NE2   1 
ATOM   12405 N  N     . GLY   E 4  177 ? 27.869  49.296  96.831  1.00 113.49 ? 177 GLY   F N     1 
ATOM   12406 C  CA    . GLY   E 4  177 ? 28.239  49.660  95.475  1.00 125.41 ? 177 GLY   F CA    1 
ATOM   12407 C  C     . GLY   E 4  177 ? 27.097  50.190  94.639  1.00 119.65 ? 177 GLY   F C     1 
ATOM   12408 O  O     . GLY   E 4  177 ? 27.152  50.142  93.401  1.00 106.02 ? 177 GLY   F O     1 
ATOM   12409 N  N     . GLN   E 4  178 ? 26.035  50.654  95.286  1.00 121.91 ? 178 GLN   F N     1 
ATOM   12410 C  CA    . GLN   E 4  178 ? 24.925  51.303  94.603  1.00 118.16 ? 178 GLN   F CA    1 
ATOM   12411 C  C     . GLN   E 4  178 ? 24.308  52.281  95.594  1.00 112.12 ? 178 GLN   F C     1 
ATOM   12412 O  O     . GLN   E 4  178 ? 23.893  51.878  96.687  1.00 110.59 ? 178 GLN   F O     1 
ATOM   12413 C  CB    . GLN   E 4  178 ? 23.894  50.275  94.105  1.00 111.51 ? 178 GLN   F CB    1 
ATOM   12414 C  CG    . GLN   E 4  178 ? 24.466  49.132  93.255  1.00 103.87 ? 178 GLN   F CG    1 
ATOM   12415 C  CD    . GLN   E 4  178 ? 25.080  48.020  94.099  1.00 124.35 ? 178 GLN   F CD    1 
ATOM   12416 O  OE1   . GLN   E 4  178 ? 24.768  47.885  95.286  1.00 130.73 ? 178 GLN   F OE1   1 
ATOM   12417 N  NE2   . GLN   E 4  178 ? 25.965  47.228  93.493  1.00 119.52 ? 178 GLN   F NE2   1 
ATOM   12418 N  N     . VAL   E 4  179 ? 24.278  53.568  95.228  1.00 105.16 ? 179 VAL   F N     1 
ATOM   12419 C  CA    . VAL   E 4  179 ? 23.718  54.590  96.109  1.00 97.15  ? 179 VAL   F CA    1 
ATOM   12420 C  C     . VAL   E 4  179 ? 22.324  54.178  96.539  1.00 100.23 ? 179 VAL   F C     1 
ATOM   12421 O  O     . VAL   E 4  179 ? 21.475  53.859  95.699  1.00 109.17 ? 179 VAL   F O     1 
ATOM   12422 C  CB    . VAL   E 4  179 ? 23.694  55.961  95.405  1.00 91.88  ? 179 VAL   F CB    1 
ATOM   12423 C  CG1   . VAL   E 4  179 ? 22.899  56.971  96.225  1.00 75.19  ? 179 VAL   F CG1   1 
ATOM   12424 C  CG2   . VAL   E 4  179 ? 25.106  56.473  95.152  1.00 92.26  ? 179 VAL   F CG2   1 
ATOM   12425 N  N     . HIS   E 4  180 ? 22.073  54.184  97.845  1.00 93.48  ? 180 HIS   F N     1 
ATOM   12426 C  CA    . HIS   E 4  180 ? 20.741  53.875  98.342  1.00 97.12  ? 180 HIS   F CA    1 
ATOM   12427 C  C     . HIS   E 4  180 ? 20.303  54.947  99.340  1.00 80.24  ? 180 HIS   F C     1 
ATOM   12428 O  O     . HIS   E 4  180 ? 20.982  55.961  99.545  1.00 74.15  ? 180 HIS   F O     1 
ATOM   12429 C  CB    . HIS   E 4  180 ? 20.681  52.448  98.918  1.00 103.87 ? 180 HIS   F CB    1 
ATOM   12430 C  CG    . HIS   E 4  180 ? 20.010  51.473  97.997  1.00 110.34 ? 180 HIS   F CG    1 
ATOM   12431 N  ND1   . HIS   E 4  180 ? 20.702  50.734  97.061  1.00 111.40 ? 180 HIS   F ND1   1 
ATOM   12432 C  CD2   . HIS   E 4  180 ? 18.700  51.161  97.828  1.00 104.10 ? 180 HIS   F CD2   1 
ATOM   12433 C  CE1   . HIS   E 4  180 ? 19.851  49.992  96.372  1.00 112.20 ? 180 HIS   F CE1   1 
ATOM   12434 N  NE2   . HIS   E 4  180 ? 18.630  50.234  96.817  1.00 104.89 ? 180 HIS   F NE2   1 
ATOM   12435 N  N     . VAL   E 4  181 ? 19.130  54.736  99.933  1.00 70.37  ? 181 VAL   F N     1 
ATOM   12436 C  CA    . VAL   E 4  181 ? 18.460  55.743  100.742 1.00 73.75  ? 181 VAL   F CA    1 
ATOM   12437 C  C     . VAL   E 4  181 ? 18.085  55.125  102.087 1.00 76.01  ? 181 VAL   F C     1 
ATOM   12438 O  O     . VAL   E 4  181 ? 17.834  53.919  102.178 1.00 77.70  ? 181 VAL   F O     1 
ATOM   12439 C  CB    . VAL   E 4  181 ? 17.222  56.293  99.992  1.00 64.08  ? 181 VAL   F CB    1 
ATOM   12440 C  CG1   . VAL   E 4  181 ? 16.400  55.150  99.437  1.00 61.71  ? 181 VAL   F CG1   1 
ATOM   12441 C  CG2   . VAL   E 4  181 ? 16.374  57.171  100.890 1.00 59.72  ? 181 VAL   F CG2   1 
ATOM   12442 N  N     . ILE   E 4  182 ? 18.069  55.958  103.139 1.00 67.07  ? 182 ILE   F N     1 
ATOM   12443 C  CA    . ILE   E 4  182 ? 17.742  55.546  104.509 1.00 67.93  ? 182 ILE   F CA    1 
ATOM   12444 C  C     . ILE   E 4  182 ? 16.426  56.199  104.915 1.00 73.31  ? 182 ILE   F C     1 
ATOM   12445 O  O     . ILE   E 4  182 ? 16.374  57.415  105.141 1.00 73.63  ? 182 ILE   F O     1 
ATOM   12446 C  CB    . ILE   E 4  182 ? 18.842  55.928  105.506 1.00 70.32  ? 182 ILE   F CB    1 
ATOM   12447 C  CG1   . ILE   E 4  182 ? 18.319  55.819  106.945 1.00 75.41  ? 182 ILE   F CG1   1 
ATOM   12448 C  CG2   . ILE   E 4  182 ? 19.307  57.350  105.251 1.00 79.00  ? 182 ILE   F CG2   1 
ATOM   12449 C  CD1   . ILE   E 4  182 ? 17.989  54.399  107.409 1.00 74.85  ? 182 ILE   F CD1   1 
ATOM   12450 N  N     . GLN   E 4  183 ? 15.377  55.393  105.070 1.00 71.36  ? 183 GLN   F N     1 
ATOM   12451 C  CA    . GLN   E 4  183 ? 14.029  55.892  105.327 1.00 70.61  ? 183 GLN   F CA    1 
ATOM   12452 C  C     . GLN   E 4  183 ? 13.469  55.259  106.590 1.00 70.49  ? 183 GLN   F C     1 
ATOM   12453 O  O     . GLN   E 4  183 ? 13.591  54.045  106.785 1.00 67.23  ? 183 GLN   F O     1 
ATOM   12454 C  CB    . GLN   E 4  183 ? 13.117  55.602  104.135 1.00 62.54  ? 183 GLN   F CB    1 
ATOM   12455 C  CG    . GLN   E 4  183 ? 11.689  56.043  104.294 1.00 57.90  ? 183 GLN   F CG    1 
ATOM   12456 C  CD    . GLN   E 4  183 ? 10.870  55.738  103.057 1.00 56.76  ? 183 GLN   F CD    1 
ATOM   12457 O  OE1   . GLN   E 4  183 ? 10.314  54.648  102.930 1.00 57.62  ? 183 GLN   F OE1   1 
ATOM   12458 N  NE2   . GLN   E 4  183 ? 10.804  56.694  102.129 1.00 50.58  ? 183 GLN   F NE2   1 
ATOM   12459 N  N     . LYS   E 4  184 ? 12.849  56.084  107.439 1.00 70.68  ? 184 LYS   F N     1 
ATOM   12460 C  CA    . LYS   E 4  184 ? 12.338  55.605  108.717 1.00 69.82  ? 184 LYS   F CA    1 
ATOM   12461 C  C     . LYS   E 4  184 ? 11.337  54.488  108.465 1.00 69.20  ? 184 LYS   F C     1 
ATOM   12462 O  O     . LYS   E 4  184 ? 10.280  54.722  107.867 1.00 62.79  ? 184 LYS   F O     1 
ATOM   12463 C  CB    . LYS   E 4  184 ? 11.716  56.752  109.536 1.00 64.88  ? 184 LYS   F CB    1 
ATOM   12464 C  CG    . LYS   E 4  184 ? 10.237  57.065  109.240 1.00 69.56  ? 184 LYS   F CG    1 
ATOM   12465 C  CD    . LYS   E 4  184 ? 9.770   58.438  109.793 1.00 64.10  ? 184 LYS   F CD    1 
ATOM   12466 C  CE    . LYS   E 4  184 ? 9.742   58.468  111.319 1.00 60.44  ? 184 LYS   F CE    1 
ATOM   12467 N  NZ    . LYS   E 4  184 ? 9.836   59.845  111.894 1.00 53.50  ? 184 LYS   F NZ    1 
ATOM   12468 N  N     . TYR   E 4  185 ? 11.667  53.263  108.877 1.00 68.70  ? 185 TYR   F N     1 
ATOM   12469 C  CA    . TYR   E 4  185 ? 10.721  52.167  108.716 1.00 65.18  ? 185 TYR   F CA    1 
ATOM   12470 C  C     . TYR   E 4  185 ? 9.525   52.437  109.620 1.00 66.56  ? 185 TYR   F C     1 
ATOM   12471 O  O     . TYR   E 4  185 ? 9.695   52.691  110.821 1.00 61.30  ? 185 TYR   F O     1 
ATOM   12472 C  CB    . TYR   E 4  185 ? 11.372  50.821  109.038 1.00 63.89  ? 185 TYR   F CB    1 
ATOM   12473 C  CG    . TYR   E 4  185 ? 10.492  49.625  108.713 1.00 60.82  ? 185 TYR   F CG    1 
ATOM   12474 C  CD1   . TYR   E 4  185 ? 10.401  49.135  107.414 1.00 51.67  ? 185 TYR   F CD1   1 
ATOM   12475 C  CD2   . TYR   E 4  185 ? 9.744   48.996  109.707 1.00 60.13  ? 185 TYR   F CD2   1 
ATOM   12476 C  CE1   . TYR   E 4  185 ? 9.596   48.053  107.115 1.00 53.72  ? 185 TYR   F CE1   1 
ATOM   12477 C  CE2   . TYR   E 4  185 ? 8.930   47.925  109.418 1.00 56.89  ? 185 TYR   F CE2   1 
ATOM   12478 C  CZ    . TYR   E 4  185 ? 8.860   47.455  108.120 1.00 63.30  ? 185 TYR   F CZ    1 
ATOM   12479 O  OH    . TYR   E 4  185 ? 8.055   46.381  107.828 1.00 65.27  ? 185 TYR   F OH    1 
ATOM   12480 N  N     . LEU   E 4  186 ? 8.325   52.440  109.035 1.00 49.63  ? 186 LEU   F N     1 
ATOM   12481 C  CA    . LEU   E 4  186 ? 7.125   52.729  109.805 1.00 57.85  ? 186 LEU   F CA    1 
ATOM   12482 C  C     . LEU   E 4  186 ? 6.868   51.582  110.762 1.00 56.12  ? 186 LEU   F C     1 
ATOM   12483 O  O     . LEU   E 4  186 ? 6.606   50.455  110.329 1.00 61.02  ? 186 LEU   F O     1 
ATOM   12484 C  CB    . LEU   E 4  186 ? 5.925   52.938  108.888 1.00 57.85  ? 186 LEU   F CB    1 
ATOM   12485 C  CG    . LEU   E 4  186 ? 6.029   54.083  107.878 1.00 64.12  ? 186 LEU   F CG    1 
ATOM   12486 C  CD1   . LEU   E 4  186 ? 4.745   54.174  107.041 1.00 60.15  ? 186 LEU   F CD1   1 
ATOM   12487 C  CD2   . LEU   E 4  186 ? 6.368   55.421  108.559 1.00 44.74  ? 186 LEU   F CD2   1 
ATOM   12488 N  N     . GLU   E 4  187 ? 6.951   51.864  112.062 1.00 55.82  ? 187 GLU   F N     1 
ATOM   12489 C  CA    . GLU   E 4  187 ? 6.862   50.796  113.049 1.00 61.02  ? 187 GLU   F CA    1 
ATOM   12490 C  C     . GLU   E 4  187 ? 5.421   50.395  113.335 1.00 60.41  ? 187 GLU   F C     1 
ATOM   12491 O  O     . GLU   E 4  187 ? 5.163   49.217  113.606 1.00 62.31  ? 187 GLU   F O     1 
ATOM   12492 C  CB    . GLU   E 4  187 ? 7.575   51.208  114.338 1.00 58.65  ? 187 GLU   F CB    1 
ATOM   12493 C  CG    . GLU   E 4  187 ? 9.107   51.140  114.259 1.00 59.74  ? 187 GLU   F CG    1 
ATOM   12494 C  CD    . GLU   E 4  187 ? 9.790   52.033  115.291 1.00 69.07  ? 187 GLU   F CD    1 
ATOM   12495 O  OE1   . GLU   E 4  187 ? 9.123   52.401  116.284 1.00 67.27  ? 187 GLU   F OE1   1 
ATOM   12496 O  OE2   . GLU   E 4  187 ? 10.982  52.383  115.109 1.00 71.64  ? 187 GLU   F OE2   1 
ATOM   12497 N  N     . LYS   E 4  188 ? 4.472   51.342  113.256 1.00 55.72  ? 188 LYS   F N     1 
ATOM   12498 C  CA    . LYS   E 4  188 ? 3.061   51.072  113.532 1.00 57.31  ? 188 LYS   F CA    1 
ATOM   12499 C  C     . LYS   E 4  188 ? 2.241   51.075  112.243 1.00 56.56  ? 188 LYS   F C     1 
ATOM   12500 O  O     . LYS   E 4  188 ? 1.442   51.993  112.011 1.00 54.56  ? 188 LYS   F O     1 
ATOM   12501 C  CB    . LYS   E 4  188 ? 2.469   52.098  114.516 1.00 53.79  ? 188 LYS   F CB    1 
ATOM   12502 C  CG    . LYS   E 4  188 ? 3.083   52.161  115.917 1.00 45.44  ? 188 LYS   F CG    1 
ATOM   12503 C  CD    . LYS   E 4  188 ? 4.455   52.845  115.915 1.00 47.56  ? 188 LYS   F CD    1 
ATOM   12504 C  CE    . LYS   E 4  188 ? 4.716   53.602  117.216 1.00 58.60  ? 188 LYS   F CE    1 
ATOM   12505 N  NZ    . LYS   E 4  188 ? 4.430   52.814  118.463 1.00 52.09  ? 188 LYS   F NZ    1 
ATOM   12506 N  N     . PRO   E 4  189 ? 2.394   50.074  111.386 1.00 55.67  ? 189 PRO   F N     1 
ATOM   12507 C  CA    . PRO   E 4  189 ? 1.532   49.989  110.203 1.00 51.77  ? 189 PRO   F CA    1 
ATOM   12508 C  C     . PRO   E 4  189 ? 0.127   49.516  110.545 1.00 56.44  ? 189 PRO   F C     1 
ATOM   12509 O  O     . PRO   E 4  189 ? -0.063  48.600  111.350 1.00 70.51  ? 189 PRO   F O     1 
ATOM   12510 C  CB    . PRO   E 4  189 ? 2.247   48.955  109.330 1.00 49.22  ? 189 PRO   F CB    1 
ATOM   12511 C  CG    . PRO   E 4  189 ? 2.914   48.074  110.332 1.00 57.75  ? 189 PRO   F CG    1 
ATOM   12512 C  CD    . PRO   E 4  189 ? 3.397   48.999  111.408 1.00 51.95  ? 189 PRO   F CD    1 
ATOM   12513 N  N     . LEU   E 4  190 ? -0.864  50.154  109.923 1.00 48.79  ? 190 LEU   F N     1 
ATOM   12514 C  CA    . LEU   E 4  190 ? -2.199  49.574  109.845 1.00 51.91  ? 190 LEU   F CA    1 
ATOM   12515 C  C     . LEU   E 4  190 ? -2.096  48.144  109.340 1.00 55.99  ? 190 LEU   F C     1 
ATOM   12516 O  O     . LEU   E 4  190 ? -1.466  47.889  108.307 1.00 56.73  ? 190 LEU   F O     1 
ATOM   12517 C  CB    . LEU   E 4  190 ? -3.086  50.389  108.898 1.00 45.52  ? 190 LEU   F CB    1 
ATOM   12518 C  CG    . LEU   E 4  190 ? -4.588  50.141  109.065 1.00 41.20  ? 190 LEU   F CG    1 
ATOM   12519 C  CD1   . LEU   E 4  190 ? -5.178  51.156  110.035 1.00 51.23  ? 190 LEU   F CD1   1 
ATOM   12520 C  CD2   . LEU   E 4  190 ? -5.344  50.166  107.760 1.00 45.65  ? 190 LEU   F CD2   1 
ATOM   12521 N  N     . LEU   E 4  191 ? -2.718  47.210  110.064 1.00 62.11  ? 191 LEU   F N     1 
ATOM   12522 C  CA    . LEU   E 4  191 ? -2.628  45.784  109.753 1.00 61.19  ? 191 LEU   F CA    1 
ATOM   12523 C  C     . LEU   E 4  191 ? -4.027  45.219  109.554 1.00 46.86  ? 191 LEU   F C     1 
ATOM   12524 O  O     . LEU   E 4  191 ? -4.894  45.371  110.424 1.00 51.45  ? 191 LEU   F O     1 
ATOM   12525 C  CB    . LEU   E 4  191 ? -1.884  45.036  110.862 1.00 54.05  ? 191 LEU   F CB    1 
ATOM   12526 C  CG    . LEU   E 4  191 ? -0.530  45.648  111.242 1.00 61.57  ? 191 LEU   F CG    1 
ATOM   12527 C  CD1   . LEU   E 4  191 ? -0.113  45.240  112.653 1.00 64.15  ? 191 LEU   F CD1   1 
ATOM   12528 C  CD2   . LEU   E 4  191 ? 0.549   45.285  110.221 1.00 62.02  ? 191 LEU   F CD2   1 
ATOM   12529 N  N     . LEU   E 4  192 ? -4.240  44.568  108.412 1.00 53.43  ? 192 LEU   F N     1 
ATOM   12530 C  CA    . LEU   E 4  192 ? -5.531  43.961  108.115 1.00 57.84  ? 192 LEU   F CA    1 
ATOM   12531 C  C     . LEU   E 4  192 ? -5.794  42.759  109.016 1.00 57.28  ? 192 LEU   F C     1 
ATOM   12532 O  O     . LEU   E 4  192 ? -4.880  42.151  109.581 1.00 55.03  ? 192 LEU   F O     1 
ATOM   12533 C  CB    . LEU   E 4  192 ? -5.621  43.478  106.669 1.00 50.69  ? 192 LEU   F CB    1 
ATOM   12534 C  CG    . LEU   E 4  192 ? -5.131  44.321  105.514 1.00 41.70  ? 192 LEU   F CG    1 
ATOM   12535 C  CD1   . LEU   E 4  192 ? -4.596  43.377  104.462 1.00 46.61  ? 192 LEU   F CD1   1 
ATOM   12536 C  CD2   . LEU   E 4  192 ? -6.269  45.138  104.958 1.00 43.82  ? 192 LEU   F CD2   1 
ATOM   12537 N  N     . GLU   E 4  193 ? -7.075  42.399  109.109 1.00 60.70  ? 193 GLU   F N     1 
ATOM   12538 C  CA    . GLU   E 4  193 ? -7.582  41.336  109.957 1.00 56.18  ? 193 GLU   F CA    1 
ATOM   12539 C  C     . GLU   E 4  193 ? -8.775  40.744  109.230 1.00 61.25  ? 193 GLU   F C     1 
ATOM   12540 O  O     . GLU   E 4  193 ? -9.604  41.499  108.700 1.00 69.32  ? 193 GLU   F O     1 
ATOM   12541 C  CB    . GLU   E 4  193 ? -8.010  41.863  111.322 1.00 49.70  ? 193 GLU   F CB    1 
ATOM   12542 C  CG    . GLU   E 4  193 ? -6.936  42.664  112.041 1.00 54.10  ? 193 GLU   F CG    1 
ATOM   12543 C  CD    . GLU   E 4  193 ? -5.886  41.774  112.658 1.00 55.02  ? 193 GLU   F CD    1 
ATOM   12544 O  OE1   . GLU   E 4  193 ? -5.829  40.582  112.274 1.00 53.41  ? 193 GLU   F OE1   1 
ATOM   12545 O  OE2   . GLU   E 4  193 ? -5.144  42.263  113.540 1.00 54.65  ? 193 GLU   F OE2   1 
ATOM   12546 N  N     . PRO   E 4  194 ? -8.908  39.423  109.198 1.00 66.35  ? 194 PRO   F N     1 
ATOM   12547 C  CA    . PRO   E 4  194 ? -8.072  38.399  109.851 1.00 70.03  ? 194 PRO   F CA    1 
ATOM   12548 C  C     . PRO   E 4  194 ? -6.672  38.245  109.251 1.00 65.28  ? 194 PRO   F C     1 
ATOM   12549 O  O     . PRO   E 4  194 ? -6.509  38.120  108.038 1.00 64.30  ? 194 PRO   F O     1 
ATOM   12550 C  CB    . PRO   E 4  194 ? -8.908  37.129  109.646 1.00 68.88  ? 194 PRO   F CB    1 
ATOM   12551 C  CG    . PRO   E 4  194 ? -9.645  37.373  108.369 1.00 67.34  ? 194 PRO   F CG    1 
ATOM   12552 C  CD    . PRO   E 4  194 ? -10.027 38.809  108.453 1.00 69.58  ? 194 PRO   F CD    1 
ATOM   12553 N  N     . GLY   E 4  195 ? -5.643  38.251  110.095 1.00 58.43  ? 195 GLY   F N     1 
ATOM   12554 C  CA    . GLY   E 4  195 ? -4.272  38.185  109.629 1.00 54.71  ? 195 GLY   F CA    1 
ATOM   12555 C  C     . GLY   E 4  195 ? -3.273  38.959  110.472 1.00 54.42  ? 195 GLY   F C     1 
ATOM   12556 O  O     . GLY   E 4  195 ? -2.211  38.439  110.820 1.00 62.24  ? 195 GLY   F O     1 
ATOM   12557 N  N     . HIS   E 4  196 ? -3.584  40.203  110.803 1.00 52.75  ? 196 HIS   F N     1 
ATOM   12558 C  CA    . HIS   E 4  196 ? -2.615  41.073  111.460 1.00 61.35  ? 196 HIS   F CA    1 
ATOM   12559 C  C     . HIS   E 4  196 ? -1.421  41.349  110.543 1.00 66.78  ? 196 HIS   F C     1 
ATOM   12560 O  O     . HIS   E 4  196 ? -0.269  41.381  110.982 1.00 68.32  ? 196 HIS   F O     1 
ATOM   12561 C  CB    . HIS   E 4  196 ? -2.155  40.474  112.792 1.00 61.69  ? 196 HIS   F CB    1 
ATOM   12562 C  CG    . HIS   E 4  196 ? -2.046  41.474  113.903 1.00 61.72  ? 196 HIS   F CG    1 
ATOM   12563 N  ND1   . HIS   E 4  196 ? -3.145  41.945  114.591 1.00 69.51  ? 196 HIS   F ND1   1 
ATOM   12564 C  CD2   . HIS   E 4  196 ? -0.969  42.092  114.446 1.00 60.12  ? 196 HIS   F CD2   1 
ATOM   12565 C  CE1   . HIS   E 4  196 ? -2.750  42.812  115.507 1.00 78.48  ? 196 HIS   F CE1   1 
ATOM   12566 N  NE2   . HIS   E 4  196 ? -1.434  42.918  115.441 1.00 84.56  ? 196 HIS   F NE2   1 
ATOM   12567 N  N     . ARG   E 4  197 ? -1.700  41.566  109.256 1.00 71.41  ? 197 ARG   F N     1 
ATOM   12568 C  CA    . ARG   E 4  197 ? -0.677  41.683  108.222 1.00 69.42  ? 197 ARG   F CA    1 
ATOM   12569 C  C     . ARG   E 4  197 ? -0.667  43.079  107.602 1.00 66.52  ? 197 ARG   F C     1 
ATOM   12570 O  O     . ARG   E 4  197 ? -1.687  43.776  107.574 1.00 62.55  ? 197 ARG   F O     1 
ATOM   12571 C  CB    . ARG   E 4  197 ? -0.905  40.637  107.133 1.00 68.79  ? 197 ARG   F CB    1 
ATOM   12572 C  CG    . ARG   E 4  197 ? -2.240  39.941  107.280 1.00 63.21  ? 197 ARG   F CG    1 
ATOM   12573 C  CD    . ARG   E 4  197 ? -2.821  39.582  105.943 1.00 63.91  ? 197 ARG   F CD    1 
ATOM   12574 N  NE    . ARG   E 4  197 ? -4.268  39.500  106.028 1.00 65.46  ? 197 ARG   F NE    1 
ATOM   12575 C  CZ    . ARG   E 4  197 ? -5.073  39.438  104.979 1.00 73.25  ? 197 ARG   F CZ    1 
ATOM   12576 N  NH1   . ARG   E 4  197 ? -4.596  39.462  103.741 1.00 60.94  ? 197 ARG   F NH1   1 
ATOM   12577 N  NH2   . ARG   E 4  197 ? -6.389  39.340  105.178 1.00 70.01  ? 197 ARG   F NH2   1 
ATOM   12578 N  N     . LYS   E 4  198 ? 0.497   43.481  107.096 1.00 63.58  ? 198 LYS   F N     1 
ATOM   12579 C  CA    . LYS   E 4  198 ? 0.622   44.780  106.457 1.00 65.12  ? 198 LYS   F CA    1 
ATOM   12580 C  C     . LYS   E 4  198 ? 0.315   44.675  104.963 1.00 61.21  ? 198 LYS   F C     1 
ATOM   12581 O  O     . LYS   E 4  198 ? 0.358   43.597  104.367 1.00 58.70  ? 198 LYS   F O     1 
ATOM   12582 C  CB    . LYS   E 4  198 ? 2.019   45.361  106.680 1.00 62.92  ? 198 LYS   F CB    1 
ATOM   12583 C  CG    . LYS   E 4  198 ? 3.109   44.767  105.818 1.00 65.69  ? 198 LYS   F CG    1 
ATOM   12584 C  CD    . LYS   E 4  198 ? 4.261   45.744  105.749 1.00 61.15  ? 198 LYS   F CD    1 
ATOM   12585 C  CE    . LYS   E 4  198 ? 4.410   46.447  107.082 1.00 55.75  ? 198 LYS   F CE    1 
ATOM   12586 N  NZ    . LYS   E 4  198 ? 5.370   47.589  107.046 1.00 60.77  ? 198 LYS   F NZ    1 
ATOM   12587 N  N     . PHE   E 4  199 ? -0.017  45.819  104.364 1.00 56.33  ? 199 PHE   F N     1 
ATOM   12588 C  CA    . PHE   E 4  199 ? -0.324  45.880  102.944 1.00 54.28  ? 199 PHE   F CA    1 
ATOM   12589 C  C     . PHE   E 4  199 ? 0.406   47.061  102.321 1.00 50.74  ? 199 PHE   F C     1 
ATOM   12590 O  O     . PHE   E 4  199 ? 1.205   47.743  102.967 1.00 48.25  ? 199 PHE   F O     1 
ATOM   12591 C  CB    . PHE   E 4  199 ? -1.830  45.977  102.698 1.00 51.72  ? 199 PHE   F CB    1 
ATOM   12592 C  CG    . PHE   E 4  199 ? -2.468  47.154  103.357 1.00 51.14  ? 199 PHE   F CG    1 
ATOM   12593 C  CD1   . PHE   E 4  199 ? -2.957  47.056  104.646 1.00 54.19  ? 199 PHE   F CD1   1 
ATOM   12594 C  CD2   . PHE   E 4  199 ? -2.567  48.363  102.698 1.00 49.04  ? 199 PHE   F CD2   1 
ATOM   12595 C  CE1   . PHE   E 4  199 ? -3.539  48.140  105.258 1.00 52.91  ? 199 PHE   F CE1   1 
ATOM   12596 C  CE2   . PHE   E 4  199 ? -3.150  49.451  103.303 1.00 49.45  ? 199 PHE   F CE2   1 
ATOM   12597 C  CZ    . PHE   E 4  199 ? -3.639  49.342  104.583 1.00 51.13  ? 199 PHE   F CZ    1 
ATOM   12598 N  N     . ASP   E 4  200 ? 0.109   47.300  101.047 1.00 55.34  ? 200 ASP   F N     1 
ATOM   12599 C  CA    . ASP   E 4  200 ? 0.828   48.245  100.200 1.00 61.27  ? 200 ASP   F CA    1 
ATOM   12600 C  C     . ASP   E 4  200 ? -0.169  48.735  99.158  1.00 62.30  ? 200 ASP   F C     1 
ATOM   12601 O  O     . ASP   E 4  200 ? -0.868  47.918  98.548  1.00 65.15  ? 200 ASP   F O     1 
ATOM   12602 C  CB    . ASP   E 4  200 ? 2.043   47.560  99.551  1.00 63.42  ? 200 ASP   F CB    1 
ATOM   12603 C  CG    . ASP   E 4  200 ? 2.761   48.429  98.545  1.00 69.68  ? 200 ASP   F CG    1 
ATOM   12604 O  OD1   . ASP   E 4  200 ? 3.376   49.428  98.969  1.00 74.41  ? 200 ASP   F OD1   1 
ATOM   12605 O  OD2   . ASP   E 4  200 ? 2.742   48.087  97.336  1.00 66.71  ? 200 ASP   F OD2   1 
ATOM   12606 N  N     . ILE   E 4  201 ? -0.274  50.055  98.985  1.00 57.30  ? 201 ILE   F N     1 
ATOM   12607 C  CA    . ILE   E 4  201 ? -1.265  50.649  98.089  1.00 51.55  ? 201 ILE   F CA    1 
ATOM   12608 C  C     . ILE   E 4  201 ? -0.578  51.067  96.795  1.00 51.97  ? 201 ILE   F C     1 
ATOM   12609 O  O     . ILE   E 4  201 ? 0.426   51.794  96.818  1.00 51.62  ? 201 ILE   F O     1 
ATOM   12610 C  CB    . ILE   E 4  201 ? -1.971  51.846  98.745  1.00 52.78  ? 201 ILE   F CB    1 
ATOM   12611 C  CG1   . ILE   E 4  201 ? -2.746  51.406  99.993  1.00 42.60  ? 201 ILE   F CG1   1 
ATOM   12612 C  CG2   . ILE   E 4  201 ? -2.889  52.519  97.741  1.00 50.50  ? 201 ILE   F CG2   1 
ATOM   12613 C  CD1   . ILE   E 4  201 ? -4.217  51.340  99.796  1.00 38.52  ? 201 ILE   F CD1   1 
ATOM   12614 N  N     . ARG   E 4  202 ? -1.108  50.599  95.667  1.00 44.16  ? 202 ARG   F N     1 
ATOM   12615 C  CA    . ARG   E 4  202 ? -0.655  51.015  94.347  1.00 40.03  ? 202 ARG   F CA    1 
ATOM   12616 C  C     . ARG   E 4  202 ? -1.789  51.760  93.660  1.00 44.95  ? 202 ARG   F C     1 
ATOM   12617 O  O     . ARG   E 4  202 ? -2.878  51.203  93.471  1.00 42.74  ? 202 ARG   F O     1 
ATOM   12618 C  CB    . ARG   E 4  202 ? -0.213  49.821  93.503  1.00 38.72  ? 202 ARG   F CB    1 
ATOM   12619 C  CG    . ARG   E 4  202 ? -0.361  50.026  91.990  1.00 44.15  ? 202 ARG   F CG    1 
ATOM   12620 C  CD    . ARG   E 4  202 ? 0.612   51.067  91.418  1.00 42.21  ? 202 ARG   F CD    1 
ATOM   12621 N  NE    . ARG   E 4  202 ? 1.985   50.867  91.878  1.00 49.01  ? 202 ARG   F NE    1 
ATOM   12622 C  CZ    . ARG   E 4  202 ? 2.859   50.037  91.320  1.00 50.37  ? 202 ARG   F CZ    1 
ATOM   12623 N  NH1   . ARG   E 4  202 ? 2.544   49.307  90.260  1.00 44.36  ? 202 ARG   F NH1   1 
ATOM   12624 N  NH2   . ARG   E 4  202 ? 4.080   49.935  91.841  1.00 42.88  ? 202 ARG   F NH2   1 
ATOM   12625 N  N     . SER   E 4  203 ? -1.537  53.020  93.314  1.00 41.43  ? 203 SER   F N     1 
ATOM   12626 C  CA    . SER   E 4  203 ? -2.436  53.820  92.497  1.00 38.44  ? 203 SER   F CA    1 
ATOM   12627 C  C     . SER   E 4  203 ? -1.760  54.114  91.171  1.00 35.93  ? 203 SER   F C     1 
ATOM   12628 O  O     . SER   E 4  203 ? -0.573  54.452  91.133  1.00 36.55  ? 203 SER   F O     1 
ATOM   12629 C  CB    . SER   E 4  203 ? -2.811  55.142  93.174  1.00 38.05  ? 203 SER   F CB    1 
ATOM   12630 O  OG    . SER   E 4  203 ? -3.483  54.941  94.400  1.00 36.11  ? 203 SER   F OG    1 
ATOM   12631 N  N     . TRP   E 4  204 ? -2.521  53.973  90.094  1.00 35.23  ? 204 TRP   F N     1 
ATOM   12632 C  CA    . TRP   E 4  204 ? -2.047  54.241  88.744  1.00 39.59  ? 204 TRP   F CA    1 
ATOM   12633 C  C     . TRP   E 4  204 ? -2.492  55.634  88.338  1.00 39.39  ? 204 TRP   F C     1 
ATOM   12634 O  O     . TRP   E 4  204 ? -3.681  55.971  88.419  1.00 34.29  ? 204 TRP   F O     1 
ATOM   12635 C  CB    . TRP   E 4  204 ? -2.559  53.186  87.754  1.00 42.77  ? 204 TRP   F CB    1 
ATOM   12636 C  CG    . TRP   E 4  204 ? -1.986  51.834  88.048  1.00 43.75  ? 204 TRP   F CG    1 
ATOM   12637 C  CD1   . TRP   E 4  204 ? -0.723  51.402  87.765  1.00 46.49  ? 204 TRP   F CD1   1 
ATOM   12638 C  CD2   . TRP   E 4  204 ? -2.635  50.756  88.735  1.00 48.95  ? 204 TRP   F CD2   1 
ATOM   12639 N  NE1   . TRP   E 4  204 ? -0.550  50.118  88.221  1.00 54.86  ? 204 TRP   F NE1   1 
ATOM   12640 C  CE2   . TRP   E 4  204 ? -1.710  49.698  88.818  1.00 52.28  ? 204 TRP   F CE2   1 
ATOM   12641 C  CE3   . TRP   E 4  204 ? -3.910  50.581  89.284  1.00 49.75  ? 204 TRP   F CE3   1 
ATOM   12642 C  CZ2   . TRP   E 4  204 ? -2.023  48.483  89.422  1.00 43.18  ? 204 TRP   F CZ2   1 
ATOM   12643 C  CZ3   . TRP   E 4  204 ? -4.213  49.377  89.884  1.00 43.58  ? 204 TRP   F CZ3   1 
ATOM   12644 C  CH2   . TRP   E 4  204 ? -3.273  48.347  89.950  1.00 41.39  ? 204 TRP   F CH2   1 
ATOM   12645 N  N     . VAL   E 4  205 ? -1.534  56.454  87.933  1.00 41.03  ? 205 VAL   F N     1 
ATOM   12646 C  CA    . VAL   E 4  205 ? -1.812  57.836  87.581  1.00 37.16  ? 205 VAL   F CA    1 
ATOM   12647 C  C     . VAL   E 4  205 ? -1.320  58.054  86.156  1.00 31.88  ? 205 VAL   F C     1 
ATOM   12648 O  O     . VAL   E 4  205 ? -0.163  57.762  85.836  1.00 32.80  ? 205 VAL   F O     1 
ATOM   12649 C  CB    . VAL   E 4  205 ? -1.170  58.820  88.573  1.00 31.02  ? 205 VAL   F CB    1 
ATOM   12650 C  CG1   . VAL   E 4  205 ? -1.799  60.173  88.440  1.00 28.85  ? 205 VAL   F CG1   1 
ATOM   12651 C  CG2   . VAL   E 4  205 ? -1.340  58.321  90.003  1.00 31.53  ? 205 VAL   F CG2   1 
ATOM   12652 N  N     . LEU   E 4  206 ? -2.212  58.525  85.302  1.00 27.43  ? 206 LEU   F N     1 
ATOM   12653 C  CA    . LEU   E 4  206 ? -1.922  58.833  83.916  1.00 25.31  ? 206 LEU   F CA    1 
ATOM   12654 C  C     . LEU   E 4  206 ? -1.889  60.339  83.756  1.00 34.97  ? 206 LEU   F C     1 
ATOM   12655 O  O     . LEU   E 4  206 ? -2.836  61.023  84.155  1.00 41.85  ? 206 LEU   F O     1 
ATOM   12656 C  CB    . LEU   E 4  206 ? -2.999  58.241  83.017  1.00 36.50  ? 206 LEU   F CB    1 
ATOM   12657 C  CG    . LEU   E 4  206 ? -3.011  58.460  81.516  1.00 38.83  ? 206 LEU   F CG    1 
ATOM   12658 C  CD1   . LEU   E 4  206 ? -1.735  57.906  80.872  1.00 36.96  ? 206 LEU   F CD1   1 
ATOM   12659 C  CD2   . LEU   E 4  206 ? -4.262  57.782  80.980  1.00 32.04  ? 206 LEU   F CD2   1 
ATOM   12660 N  N     . VAL   E 4  207 ? -0.813  60.856  83.170  1.00 32.46  ? 207 VAL   F N     1 
ATOM   12661 C  CA    . VAL   E 4  207 ? -0.679  62.281  82.900  1.00 29.97  ? 207 VAL   F CA    1 
ATOM   12662 C  C     . VAL   E 4  207 ? -0.552  62.453  81.393  1.00 32.21  ? 207 VAL   F C     1 
ATOM   12663 O  O     . VAL   E 4  207 ? 0.420   61.978  80.792  1.00 35.08  ? 207 VAL   F O     1 
ATOM   12664 C  CB    . VAL   E 4  207 ? 0.524   62.885  83.638  1.00 30.87  ? 207 VAL   F CB    1 
ATOM   12665 C  CG1   . VAL   E 4  207 ? 0.705   64.333  83.236  1.00 27.40  ? 207 VAL   F CG1   1 
ATOM   12666 C  CG2   . VAL   E 4  207 ? 0.360   62.716  85.163  1.00 23.39  ? 207 VAL   F CG2   1 
ATOM   12667 N  N     . ASP   E 4  208 ? -1.540  63.118  80.782  1.00 32.74  ? 208 ASP   F N     1 
ATOM   12668 C  CA    . ASP   E 4  208 ? -1.572  63.352  79.338  1.00 30.92  ? 208 ASP   F CA    1 
ATOM   12669 C  C     . ASP   E 4  208 ? -0.730  64.585  78.972  1.00 33.39  ? 208 ASP   F C     1 
ATOM   12670 O  O     . ASP   E 4  208 ? -0.016  65.162  79.800  1.00 29.55  ? 208 ASP   F O     1 
ATOM   12671 C  CB    . ASP   E 4  208 ? -3.022  63.459  78.840  1.00 26.01  ? 208 ASP   F CB    1 
ATOM   12672 C  CG    . ASP   E 4  208 ? -3.763  64.689  79.378  1.00 27.49  ? 208 ASP   F CG    1 
ATOM   12673 O  OD1   . ASP   E 4  208 ? -3.118  65.606  79.892  1.00 26.41  ? 208 ASP   F OD1   1 
ATOM   12674 O  OD2   . ASP   E 4  208 ? -5.005  64.748  79.288  1.00 30.00  ? 208 ASP   F OD2   1 
ATOM   12675 N  N     . HIS   E 4  209 ? -0.812  64.997  77.700  1.00 34.87  ? 209 HIS   F N     1 
ATOM   12676 C  CA    . HIS   E 4  209 ? -0.019  66.119  77.190  1.00 33.73  ? 209 HIS   F CA    1 
ATOM   12677 C  C     . HIS   E 4  209 ? -0.488  67.476  77.738  1.00 33.83  ? 209 HIS   F C     1 
ATOM   12678 O  O     . HIS   E 4  209 ? 0.327   68.394  77.900  1.00 34.84  ? 209 HIS   F O     1 
ATOM   12679 C  CB    . HIS   E 4  209 ? -0.088  66.121  75.670  1.00 28.30  ? 209 HIS   F CB    1 
ATOM   12680 C  CG    . HIS   E 4  209 ? -1.490  66.169  75.154  1.00 30.85  ? 209 HIS   F CG    1 
ATOM   12681 N  ND1   . HIS   E 4  209 ? -2.355  65.105  75.265  1.00 33.38  ? 209 HIS   F ND1   1 
ATOM   12682 C  CD2   . HIS   E 4  209 ? -2.199  67.173  74.587  1.00 31.27  ? 209 HIS   F CD2   1 
ATOM   12683 C  CE1   . HIS   E 4  209 ? -3.527  65.441  74.758  1.00 33.14  ? 209 HIS   F CE1   1 
ATOM   12684 N  NE2   . HIS   E 4  209 ? -3.459  66.690  74.339  1.00 29.74  ? 209 HIS   F NE2   1 
ATOM   12685 N  N     . LEU   E 4  210 ? -1.789  67.633  77.996  1.00 27.40  ? 210 LEU   F N     1 
ATOM   12686 C  CA    . LEU   E 4  210 ? -2.329  68.824  78.646  1.00 29.54  ? 210 LEU   F CA    1 
ATOM   12687 C  C     . LEU   E 4  210 ? -1.978  68.920  80.133  1.00 29.58  ? 210 LEU   F C     1 
ATOM   12688 O  O     . LEU   E 4  210 ? -2.290  69.949  80.740  1.00 33.88  ? 210 LEU   F O     1 
ATOM   12689 C  CB    . LEU   E 4  210 ? -3.851  68.865  78.504  1.00 27.84  ? 210 LEU   F CB    1 
ATOM   12690 C  CG    . LEU   E 4  210 ? -4.502  68.661  77.137  1.00 26.00  ? 210 LEU   F CG    1 
ATOM   12691 C  CD1   . LEU   E 4  210 ? -5.996  68.661  77.322  1.00 30.37  ? 210 LEU   F CD1   1 
ATOM   12692 C  CD2   . LEU   E 4  210 ? -4.108  69.755  76.191  1.00 23.67  ? 210 LEU   F CD2   1 
ATOM   12693 N  N     . TYR   E 4  211 ? -1.346  67.894  80.716  1.00 27.54  ? 211 TYR   F N     1 
ATOM   12694 C  CA    . TYR   E 4  211 ? -1.049  67.793  82.156  1.00 25.23  ? 211 TYR   F CA    1 
ATOM   12695 C  C     . TYR   E 4  211 ? -2.303  67.634  83.008  1.00 33.41  ? 211 TYR   F C     1 
ATOM   12696 O  O     . TYR   E 4  211 ? -2.331  68.061  84.161  1.00 35.73  ? 211 TYR   F O     1 
ATOM   12697 C  CB    . TYR   E 4  211 ? -0.225  68.968  82.683  1.00 21.81  ? 211 TYR   F CB    1 
ATOM   12698 C  CG    . TYR   E 4  211 ? 0.926   68.509  83.552  1.00 23.71  ? 211 TYR   F CG    1 
ATOM   12699 C  CD1   . TYR   E 4  211 ? 2.125   68.097  82.979  1.00 23.63  ? 211 TYR   F CD1   1 
ATOM   12700 C  CD2   . TYR   E 4  211 ? 0.814   68.468  84.935  1.00 24.68  ? 211 TYR   F CD2   1 
ATOM   12701 C  CE1   . TYR   E 4  211 ? 3.177   67.666  83.751  1.00 31.67  ? 211 TYR   F CE1   1 
ATOM   12702 C  CE2   . TYR   E 4  211 ? 1.871   68.026  85.735  1.00 25.84  ? 211 TYR   F CE2   1 
ATOM   12703 C  CZ    . TYR   E 4  211 ? 3.054   67.623  85.135  1.00 34.02  ? 211 TYR   F CZ    1 
ATOM   12704 O  OH    . TYR   E 4  211 ? 4.136   67.187  85.888  1.00 27.35  ? 211 TYR   F OH    1 
ATOM   12705 N  N     . ASN   E 4  212 ? -3.349  67.036  82.446  1.00 29.08  ? 212 ASN   F N     1 
ATOM   12706 C  CA    . ASN   E 4  212 ? -4.436  66.515  83.254  1.00 27.73  ? 212 ASN   F CA    1 
ATOM   12707 C  C     . ASN   E 4  212 ? -3.937  65.319  84.054  1.00 35.81  ? 212 ASN   F C     1 
ATOM   12708 O  O     . ASN   E 4  212 ? -3.295  64.419  83.500  1.00 39.28  ? 212 ASN   F O     1 
ATOM   12709 C  CB    . ASN   E 4  212 ? -5.598  66.096  82.361  1.00 39.97  ? 212 ASN   F CB    1 
ATOM   12710 C  CG    . ASN   E 4  212 ? -6.282  67.267  81.720  1.00 43.64  ? 212 ASN   F CG    1 
ATOM   12711 O  OD1   . ASN   E 4  212 ? -6.433  68.309  82.341  1.00 44.01  ? 212 ASN   F OD1   1 
ATOM   12712 N  ND2   . ASN   E 4  212 ? -6.700  67.107  80.465  1.00 42.32  ? 212 ASN   F ND2   1 
ATOM   12713 N  N     . ILE   E 4  213 ? -4.232  65.298  85.352  1.00 35.24  ? 213 ILE   F N     1 
ATOM   12714 C  CA    . ILE   E 4  213 ? -3.821  64.203  86.224  1.00 39.01  ? 213 ILE   F CA    1 
ATOM   12715 C  C     . ILE   E 4  213 ? -5.014  63.273  86.422  1.00 42.63  ? 213 ILE   F C     1 
ATOM   12716 O  O     . ILE   E 4  213 ? -5.950  63.587  87.166  1.00 47.90  ? 213 ILE   F O     1 
ATOM   12717 C  CB    . ILE   E 4  213 ? -3.270  64.711  87.554  1.00 31.78  ? 213 ILE   F CB    1 
ATOM   12718 C  CG1   . ILE   E 4  213 ? -1.932  65.415  87.305  1.00 34.35  ? 213 ILE   F CG1   1 
ATOM   12719 C  CG2   . ILE   E 4  213 ? -3.142  63.541  88.500  1.00 29.49  ? 213 ILE   F CG2   1 
ATOM   12720 C  CD1   . ILE   E 4  213 ? -1.439  66.257  88.451  1.00 39.06  ? 213 ILE   F CD1   1 
ATOM   12721 N  N     . TYR   E 4  214 ? -4.985  62.121  85.752  1.00 38.10  ? 214 TYR   F N     1 
ATOM   12722 C  CA    . TYR   E 4  214 ? -6.016  61.103  85.893  1.00 40.66  ? 214 TYR   F CA    1 
ATOM   12723 C  C     . TYR   E 4  214 ? -5.586  60.079  86.930  1.00 40.42  ? 214 TYR   F C     1 
ATOM   12724 O  O     . TYR   E 4  214 ? -4.436  59.634  86.947  1.00 43.76  ? 214 TYR   F O     1 
ATOM   12725 C  CB    . TYR   E 4  214 ? -6.307  60.429  84.546  1.00 40.85  ? 214 TYR   F CB    1 
ATOM   12726 C  CG    . TYR   E 4  214 ? -6.800  61.437  83.543  1.00 43.15  ? 214 TYR   F CG    1 
ATOM   12727 C  CD1   . TYR   E 4  214 ? -8.077  61.945  83.632  1.00 42.73  ? 214 TYR   F CD1   1 
ATOM   12728 C  CD2   . TYR   E 4  214 ? -5.968  61.934  82.551  1.00 48.81  ? 214 TYR   F CD2   1 
ATOM   12729 C  CE1   . TYR   E 4  214 ? -8.529  62.903  82.755  1.00 45.67  ? 214 TYR   F CE1   1 
ATOM   12730 C  CE2   . TYR   E 4  214 ? -6.418  62.896  81.652  1.00 43.54  ? 214 TYR   F CE2   1 
ATOM   12731 C  CZ    . TYR   E 4  214 ? -7.703  63.380  81.765  1.00 45.26  ? 214 TYR   F CZ    1 
ATOM   12732 O  OH    . TYR   E 4  214 ? -8.183  64.343  80.892  1.00 49.98  ? 214 TYR   F OH    1 
ATOM   12733 N  N     . LEU   E 4  215 ? -6.506  59.738  87.816  1.00 41.95  ? 215 LEU   F N     1 
ATOM   12734 C  CA    . LEU   E 4  215 ? -6.309  58.679  88.796  1.00 37.02  ? 215 LEU   F CA    1 
ATOM   12735 C  C     . LEU   E 4  215 ? -7.265  57.549  88.447  1.00 39.46  ? 215 LEU   F C     1 
ATOM   12736 O  O     . LEU   E 4  215 ? -8.482  57.757  88.360  1.00 37.81  ? 215 LEU   F O     1 
ATOM   12737 C  CB    . LEU   E 4  215 ? -6.554  59.200  90.207  1.00 33.10  ? 215 LEU   F CB    1 
ATOM   12738 C  CG    . LEU   E 4  215 ? -6.325  58.234  91.352  1.00 32.49  ? 215 LEU   F CG    1 
ATOM   12739 C  CD1   . LEU   E 4  215 ? -4.940  57.609  91.272  1.00 34.88  ? 215 LEU   F CD1   1 
ATOM   12740 C  CD2   . LEU   E 4  215 ? -6.522  58.994  92.659  1.00 31.34  ? 215 LEU   F CD2   1 
ATOM   12741 N  N     . TYR   E 4  216 ? -6.713  56.376  88.188  1.00 35.03  ? 216 TYR   F N     1 
ATOM   12742 C  CA    . TYR   E 4  216 ? -7.547  55.234  87.863  1.00 37.32  ? 216 TYR   F CA    1 
ATOM   12743 C  C     . TYR   E 4  216 ? -8.374  54.871  89.091  1.00 43.48  ? 216 TYR   F C     1 
ATOM   12744 O  O     . TYR   E 4  216 ? -7.841  54.758  90.203  1.00 49.46  ? 216 TYR   F O     1 
ATOM   12745 C  CB    . TYR   E 4  216 ? -6.650  54.082  87.415  1.00 37.99  ? 216 TYR   F CB    1 
ATOM   12746 C  CG    . TYR   E 4  216 ? -7.326  52.793  87.037  1.00 40.50  ? 216 TYR   F CG    1 
ATOM   12747 C  CD1   . TYR   E 4  216 ? -8.667  52.742  86.665  1.00 37.49  ? 216 TYR   F CD1   1 
ATOM   12748 C  CD2   . TYR   E 4  216 ? -6.600  51.608  87.067  1.00 43.67  ? 216 TYR   F CD2   1 
ATOM   12749 C  CE1   . TYR   E 4  216 ? -9.255  51.530  86.327  1.00 46.90  ? 216 TYR   F CE1   1 
ATOM   12750 C  CE2   . TYR   E 4  216 ? -7.166  50.408  86.736  1.00 45.55  ? 216 TYR   F CE2   1 
ATOM   12751 C  CZ    . TYR   E 4  216 ? -8.486  50.359  86.366  1.00 48.47  ? 216 TYR   F CZ    1 
ATOM   12752 O  OH    . TYR   E 4  216 ? -9.007  49.121  86.047  1.00 41.68  ? 216 TYR   F OH    1 
ATOM   12753 N  N     . ARG   E 4  217 ? -9.688  54.721  88.907  1.00 45.40  ? 217 ARG   F N     1 
ATOM   12754 C  CA    . ARG   E 4  217 ? -10.551 54.504  90.066  1.00 42.57  ? 217 ARG   F CA    1 
ATOM   12755 C  C     . ARG   E 4  217 ? -10.178 53.220  90.810  1.00 48.64  ? 217 ARG   F C     1 
ATOM   12756 O  O     . ARG   E 4  217 ? -10.098 53.216  92.047  1.00 40.68  ? 217 ARG   F O     1 
ATOM   12757 C  CB    . ARG   E 4  217 ? -12.024 54.501  89.648  1.00 40.20  ? 217 ARG   F CB    1 
ATOM   12758 C  CG    . ARG   E 4  217 ? -12.395 53.557  88.511  1.00 46.88  ? 217 ARG   F CG    1 
ATOM   12759 C  CD    . ARG   E 4  217 ? -13.922 53.360  88.473  1.00 53.84  ? 217 ARG   F CD    1 
ATOM   12760 N  NE    . ARG   E 4  217 ? -14.467 52.941  87.181  1.00 58.85  ? 217 ARG   F NE    1 
ATOM   12761 C  CZ    . ARG   E 4  217 ? -14.369 51.716  86.675  1.00 62.05  ? 217 ARG   F CZ    1 
ATOM   12762 N  NH1   . ARG   E 4  217 ? -13.679 50.763  87.288  1.00 60.91  ? 217 ARG   F NH1   1 
ATOM   12763 N  NH2   . ARG   E 4  217 ? -14.980 51.439  85.525  1.00 49.42  ? 217 ARG   F NH2   1 
ATOM   12764 N  N     . GLU   E 4  218 ? -9.911  52.131  90.082  1.00 42.99  ? 218 GLU   F N     1 
ATOM   12765 C  CA    . GLU   E 4  218 ? -9.542  50.873  90.723  1.00 45.91  ? 218 GLU   F CA    1 
ATOM   12766 C  C     . GLU   E 4  218 ? -8.050  50.844  91.064  1.00 43.07  ? 218 GLU   F C     1 
ATOM   12767 O  O     . GLU   E 4  218 ? -7.204  51.063  90.192  1.00 49.41  ? 218 GLU   F O     1 
ATOM   12768 C  CB    . GLU   E 4  218 ? -9.926  49.691  89.832  1.00 53.48  ? 218 GLU   F CB    1 
ATOM   12769 C  CG    . GLU   E 4  218 ? -11.164 48.920  90.347  1.00 61.92  ? 218 GLU   F CG    1 
ATOM   12770 C  CD    . GLU   E 4  218 ? -11.165 48.734  91.887  1.00 66.08  ? 218 GLU   F CD    1 
ATOM   12771 O  OE1   . GLU   E 4  218 ? -10.190 48.177  92.459  1.00 54.95  ? 218 GLU   F OE1   1 
ATOM   12772 O  OE2   . GLU   E 4  218 ? -12.151 49.163  92.530  1.00 68.01  ? 218 GLU   F OE2   1 
ATOM   12773 N  N     . GLY   E 4  219 ? -7.737  50.594  92.341  1.00 43.72  ? 219 GLY   F N     1 
ATOM   12774 C  CA    . GLY   E 4  219 ? -6.390  50.329  92.802  1.00 42.06  ? 219 GLY   F CA    1 
ATOM   12775 C  C     . GLY   E 4  219 ? -6.302  48.963  93.468  1.00 45.14  ? 219 GLY   F C     1 
ATOM   12776 O  O     . GLY   E 4  219 ? -7.285  48.221  93.532  1.00 52.67  ? 219 GLY   F O     1 
ATOM   12777 N  N     . VAL   E 4  220 ? -5.104  48.634  93.963  1.00 34.58  ? 220 VAL   F N     1 
ATOM   12778 C  CA    . VAL   E 4  220 ? -4.886  47.358  94.647  1.00 45.71  ? 220 VAL   F CA    1 
ATOM   12779 C  C     . VAL   E 4  220 ? -4.024  47.562  95.883  1.00 50.76  ? 220 VAL   F C     1 
ATOM   12780 O  O     . VAL   E 4  220 ? -3.054  48.329  95.860  1.00 39.48  ? 220 VAL   F O     1 
ATOM   12781 C  CB    . VAL   E 4  220 ? -4.233  46.270  93.753  1.00 45.65  ? 220 VAL   F CB    1 
ATOM   12782 C  CG1   . VAL   E 4  220 ? -5.091  45.963  92.552  1.00 55.25  ? 220 VAL   F CG1   1 
ATOM   12783 C  CG2   . VAL   E 4  220 ? -2.807  46.642  93.364  1.00 37.73  ? 220 VAL   F CG2   1 
ATOM   12784 N  N     . LEU   E 4  221 ? -4.370  46.840  96.958  1.00 53.94  ? 221 LEU   F N     1 
ATOM   12785 C  CA    . LEU   E 4  221 ? -3.475  46.641  98.091  1.00 52.62  ? 221 LEU   F CA    1 
ATOM   12786 C  C     . LEU   E 4  221 ? -2.649  45.387  97.837  1.00 59.35  ? 221 LEU   F C     1 
ATOM   12787 O  O     . LEU   E 4  221 ? -3.198  44.335  97.478  1.00 57.23  ? 221 LEU   F O     1 
ATOM   12788 C  CB    . LEU   E 4  221 ? -4.245  46.501  99.409  1.00 56.03  ? 221 LEU   F CB    1 
ATOM   12789 C  CG    . LEU   E 4  221 ? -4.958  47.704  100.049 1.00 49.26  ? 221 LEU   F CG    1 
ATOM   12790 C  CD1   . LEU   E 4  221 ? -6.215  48.082  99.272  1.00 52.25  ? 221 LEU   F CD1   1 
ATOM   12791 C  CD2   . LEU   E 4  221 ? -5.295  47.432  101.503 1.00 45.85  ? 221 LEU   F CD2   1 
ATOM   12792 N  N     . ARG   E 4  222 ? -1.332  45.519  97.984  1.00 58.36  ? 222 ARG   F N     1 
ATOM   12793 C  CA    . ARG   E 4  222 ? -0.399  44.396  97.956  1.00 61.40  ? 222 ARG   F CA    1 
ATOM   12794 C  C     . ARG   E 4  222 ? -0.262  43.908  99.396  1.00 65.09  ? 222 ARG   F C     1 
ATOM   12795 O  O     . ARG   E 4  222 ? 0.559   44.402  100.176 1.00 58.84  ? 222 ARG   F O     1 
ATOM   12796 C  CB    . ARG   E 4  222 ? 0.942   44.821  97.366  1.00 65.23  ? 222 ARG   F CB    1 
ATOM   12797 C  CG    . ARG   E 4  222 ? 0.859   45.974  96.388  1.00 61.18  ? 222 ARG   F CG    1 
ATOM   12798 C  CD    . ARG   E 4  222 ? 0.812   45.491  94.946  1.00 64.40  ? 222 ARG   F CD    1 
ATOM   12799 N  NE    . ARG   E 4  222 ? 2.141   45.287  94.373  1.00 81.37  ? 222 ARG   F NE    1 
ATOM   12800 C  CZ    . ARG   E 4  222 ? 2.997   46.260  94.075  1.00 77.65  ? 222 ARG   F CZ    1 
ATOM   12801 N  NH1   . ARG   E 4  222 ? 2.738   47.528  94.374  1.00 52.80  ? 222 ARG   F NH1   1 
ATOM   12802 N  NH2   . ARG   E 4  222 ? 4.143   45.956  93.466  1.00 73.06  ? 222 ARG   F NH2   1 
ATOM   12803 N  N     . THR   E 4  223 ? -1.078  42.922  99.752  1.00 65.75  ? 223 THR   F N     1 
ATOM   12804 C  CA    . THR   E 4  223 ? -1.175  42.434  101.119 1.00 63.40  ? 223 THR   F CA    1 
ATOM   12805 C  C     . THR   E 4  223 ? -0.076  41.423  101.422 1.00 62.84  ? 223 THR   F C     1 
ATOM   12806 O  O     . THR   E 4  223 ? 0.473   40.779  100.528 1.00 60.72  ? 223 THR   F O     1 
ATOM   12807 C  CB    . THR   E 4  223 ? -2.542  41.799  101.355 1.00 63.22  ? 223 THR   F CB    1 
ATOM   12808 O  OG1   . THR   E 4  223 ? -2.583  40.516  100.719 1.00 61.70  ? 223 THR   F OG1   1 
ATOM   12809 C  CG2   . THR   E 4  223 ? -3.640  42.685  100.758 1.00 63.51  ? 223 THR   F CG2   1 
ATOM   12810 N  N     . SER   E 4  224 ? 0.240   41.297  102.711 1.00 77.23  ? 224 SER   F N     1 
ATOM   12811 C  CA    . SER   E 4  224 ? 1.194   40.315  103.217 1.00 73.90  ? 224 SER   F CA    1 
ATOM   12812 C  C     . SER   E 4  224 ? 0.442   39.095  103.735 1.00 72.36  ? 224 SER   F C     1 
ATOM   12813 O  O     . SER   E 4  224 ? -0.609  39.231  104.367 1.00 78.33  ? 224 SER   F O     1 
ATOM   12814 C  CB    . SER   E 4  224 ? 2.050   40.911  104.338 1.00 68.75  ? 224 SER   F CB    1 
ATOM   12815 O  OG    . SER   E 4  224 ? 3.047   40.004  104.762 1.00 68.64  ? 224 SER   F OG    1 
ATOM   12816 N  N     . SER   E 4  225 ? 0.971   37.898  103.443 1.00 77.13  ? 225 SER   F N     1 
ATOM   12817 C  CA    . SER   E 4  225 ? 0.341   36.650  103.882 1.00 79.29  ? 225 SER   F CA    1 
ATOM   12818 C  C     . SER   E 4  225 ? 0.781   36.238  105.274 1.00 77.55  ? 225 SER   F C     1 
ATOM   12819 O  O     . SER   E 4  225 ? 0.014   35.596  106.001 1.00 76.14  ? 225 SER   F O     1 
ATOM   12820 C  CB    . SER   E 4  225 ? 0.662   35.493  102.923 1.00 77.70  ? 225 SER   F CB    1 
ATOM   12821 O  OG    . SER   E 4  225 ? 0.517   35.849  101.557 1.00 77.98  ? 225 SER   F OG    1 
ATOM   12822 N  N     . GLU   E 4  226 ? 2.009   36.576  105.642 1.00 79.00  ? 226 GLU   F N     1 
ATOM   12823 C  CA    . GLU   E 4  226 ? 2.544   36.235  106.944 1.00 82.24  ? 226 GLU   F CA    1 
ATOM   12824 C  C     . GLU   E 4  226 ? 2.238   37.370  107.913 1.00 80.20  ? 226 GLU   F C     1 
ATOM   12825 O  O     . GLU   E 4  226 ? 2.658   38.508  107.665 1.00 80.10  ? 226 GLU   F O     1 
ATOM   12826 C  CB    . GLU   E 4  226 ? 4.048   35.984  106.853 1.00 84.79  ? 226 GLU   F CB    1 
ATOM   12827 C  CG    . GLU   E 4  226 ? 4.450   34.663  106.157 1.00 75.83  ? 226 GLU   F CG    1 
ATOM   12828 C  CD    . GLU   E 4  226 ? 4.233   34.667  104.634 1.00 92.86  ? 226 GLU   F CD    1 
ATOM   12829 O  OE1   . GLU   E 4  226 ? 4.999   35.360  103.924 1.00 97.06  ? 226 GLU   F OE1   1 
ATOM   12830 O  OE2   . GLU   E 4  226 ? 3.306   33.969  104.146 1.00 85.04  ? 226 GLU   F OE2   1 
ATOM   12831 N  N     . PRO   E 4  227 ? 1.481   37.120  108.997 1.00 85.27  ? 227 PRO   F N     1 
ATOM   12832 C  CA    . PRO   E 4  227 ? 1.130   38.192  109.945 1.00 76.87  ? 227 PRO   F CA    1 
ATOM   12833 C  C     . PRO   E 4  227 ? 2.308   39.045  110.383 1.00 71.20  ? 227 PRO   F C     1 
ATOM   12834 O  O     . PRO   E 4  227 ? 3.314   38.524  110.868 1.00 71.64  ? 227 PRO   F O     1 
ATOM   12835 C  CB    . PRO   E 4  227 ? 0.532   37.416  111.121 1.00 77.22  ? 227 PRO   F CB    1 
ATOM   12836 C  CG    . PRO   E 4  227 ? -0.136  36.238  110.446 1.00 80.26  ? 227 PRO   F CG    1 
ATOM   12837 C  CD    . PRO   E 4  227 ? 0.763   35.866  109.286 1.00 81.30  ? 227 PRO   F CD    1 
ATOM   12838 N  N     . TYR   E 4  228 ? 2.178   40.364  110.218 1.00 76.29  ? 228 TYR   F N     1 
ATOM   12839 C  CA    . TYR   E 4  228 ? 3.306   41.277  110.395 1.00 79.56  ? 228 TYR   F CA    1 
ATOM   12840 C  C     . TYR   E 4  228 ? 3.800   41.244  111.829 1.00 76.05  ? 228 TYR   F C     1 
ATOM   12841 O  O     . TYR   E 4  228 ? 3.057   41.575  112.755 1.00 77.65  ? 228 TYR   F O     1 
ATOM   12842 C  CB    . TYR   E 4  228 ? 2.914   42.705  110.009 1.00 72.09  ? 228 TYR   F CB    1 
ATOM   12843 C  CG    . TYR   E 4  228 ? 3.908   43.738  110.487 1.00 70.45  ? 228 TYR   F CG    1 
ATOM   12844 C  CD1   . TYR   E 4  228 ? 5.079   43.994  109.777 1.00 70.16  ? 228 TYR   F CD1   1 
ATOM   12845 C  CD2   . TYR   E 4  228 ? 3.683   44.445  111.656 1.00 65.93  ? 228 TYR   F CD2   1 
ATOM   12846 C  CE1   . TYR   E 4  228 ? 5.990   44.937  110.223 1.00 66.80  ? 228 TYR   F CE1   1 
ATOM   12847 C  CE2   . TYR   E 4  228 ? 4.584   45.380  112.107 1.00 63.75  ? 228 TYR   F CE2   1 
ATOM   12848 C  CZ    . TYR   E 4  228 ? 5.730   45.624  111.394 1.00 63.04  ? 228 TYR   F CZ    1 
ATOM   12849 O  OH    . TYR   E 4  228 ? 6.603   46.568  111.871 1.00 70.34  ? 228 TYR   F OH    1 
ATOM   12850 N  N     . ASN   E 4  229 ? 5.063   40.873  112.009 1.00 75.39  ? 229 ASN   F N     1 
ATOM   12851 C  CA    . ASN   E 4  229 ? 5.608   40.575  113.328 1.00 79.39  ? 229 ASN   F CA    1 
ATOM   12852 C  C     . ASN   E 4  229 ? 6.731   41.556  113.652 1.00 76.40  ? 229 ASN   F C     1 
ATOM   12853 O  O     . ASN   E 4  229 ? 7.808   41.488  113.052 1.00 71.38  ? 229 ASN   F O     1 
ATOM   12854 C  CB    . ASN   E 4  229 ? 6.085   39.121  113.374 1.00 85.73  ? 229 ASN   F CB    1 
ATOM   12855 C  CG    . ASN   E 4  229 ? 7.130   38.872  114.443 1.00 100.62 ? 229 ASN   F CG    1 
ATOM   12856 O  OD1   . ASN   E 4  229 ? 8.305   38.705  114.131 1.00 100.84 ? 229 ASN   F OD1   1 
ATOM   12857 N  ND2   . ASN   E 4  229 ? 6.708   38.835  115.709 1.00 98.81  ? 229 ASN   F ND2   1 
ATOM   12858 N  N     . SER   E 4  230 ? 6.472   42.459  114.605 1.00 77.61  ? 230 SER   F N     1 
ATOM   12859 C  CA    . SER   E 4  230 ? 7.504   43.344  115.130 1.00 77.68  ? 230 SER   F CA    1 
ATOM   12860 C  C     . SER   E 4  230 ? 8.617   42.544  115.797 1.00 89.33  ? 230 SER   F C     1 
ATOM   12861 O  O     . SER   E 4  230 ? 8.389   41.482  116.380 1.00 95.30  ? 230 SER   F O     1 
ATOM   12862 C  CB    . SER   E 4  230 ? 6.912   44.324  116.140 1.00 75.07  ? 230 SER   F CB    1 
ATOM   12863 O  OG    . SER   E 4  230 ? 7.945   45.033  116.806 1.00 73.83  ? 230 SER   F OG    1 
ATOM   12864 N  N     . ALA   E 4  231 ? 9.834   43.083  115.722 1.00 93.45  ? 231 ALA   F N     1 
ATOM   12865 C  CA    . ALA   E 4  231 ? 11.092  42.468  116.177 1.00 96.84  ? 231 ALA   F CA    1 
ATOM   12866 C  C     . ALA   E 4  231 ? 11.656  41.521  115.128 1.00 89.89  ? 231 ALA   F C     1 
ATOM   12867 O  O     . ALA   E 4  231 ? 12.647  40.825  115.393 1.00 91.06  ? 231 ALA   F O     1 
ATOM   12868 C  CB    . ALA   E 4  231 ? 10.943  41.723  117.507 1.00 85.77  ? 231 ALA   F CB    1 
ATOM   12869 N  N     . ASN   E 4  232 ? 11.056  41.477  113.940 1.00 92.54  ? 232 ASN   F N     1 
ATOM   12870 C  CA    . ASN   E 4  232 ? 11.515  40.648  112.833 1.00 96.81  ? 232 ASN   F CA    1 
ATOM   12871 C  C     . ASN   E 4  232 ? 12.084  41.490  111.697 1.00 101.74 ? 232 ASN   F C     1 
ATOM   12872 O  O     . ASN   E 4  232 ? 12.000  41.098  110.530 1.00 106.23 ? 232 ASN   F O     1 
ATOM   12873 C  CB    . ASN   E 4  232 ? 10.376  39.773  112.309 1.00 100.71 ? 232 ASN   F CB    1 
ATOM   12874 C  CG    . ASN   E 4  232 ? 10.556  38.317  112.656 1.00 106.47 ? 232 ASN   F CG    1 
ATOM   12875 O  OD1   . ASN   E 4  232 ? 11.323  37.978  113.559 1.00 98.37  ? 232 ASN   F OD1   1 
ATOM   12876 N  ND2   . ASN   E 4  232 ? 9.831   37.445  111.958 1.00 99.12  ? 232 ASN   F ND2   1 
ATOM   12877 N  N     . PHE   E 4  233 ? 12.655  42.654  112.023 1.00 102.31 ? 233 PHE   F N     1 
ATOM   12878 C  CA    . PHE   E 4  233 ? 13.085  43.586  110.984 1.00 98.28  ? 233 PHE   F CA    1 
ATOM   12879 C  C     . PHE   E 4  233 ? 13.962  42.909  109.931 1.00 111.82 ? 233 PHE   F C     1 
ATOM   12880 O  O     . PHE   E 4  233 ? 14.029  43.371  108.783 1.00 114.69 ? 233 PHE   F O     1 
ATOM   12881 C  CB    . PHE   E 4  233 ? 13.833  44.770  111.606 1.00 97.58  ? 233 PHE   F CB    1 
ATOM   12882 C  CG    . PHE   E 4  233 ? 13.196  45.323  112.856 1.00 98.37  ? 233 PHE   F CG    1 
ATOM   12883 C  CD1   . PHE   E 4  233 ? 11.947  45.925  112.817 1.00 88.92  ? 233 PHE   F CD1   1 
ATOM   12884 C  CD2   . PHE   E 4  233 ? 13.877  45.267  114.071 1.00 106.57 ? 233 PHE   F CD2   1 
ATOM   12885 C  CE1   . PHE   E 4  233 ? 11.379  46.441  113.969 1.00 97.79  ? 233 PHE   F CE1   1 
ATOM   12886 C  CE2   . PHE   E 4  233 ? 13.320  45.780  115.231 1.00 102.83 ? 233 PHE   F CE2   1 
ATOM   12887 C  CZ    . PHE   E 4  233 ? 12.070  46.369  115.183 1.00 107.31 ? 233 PHE   F CZ    1 
ATOM   12888 N  N     . GLN   E 4  234 ? 14.640  41.823  110.293 1.00 111.39 ? 234 GLN   F N     1 
ATOM   12889 C  CA    . GLN   E 4  234 ? 15.428  41.045  109.348 1.00 111.10 ? 234 GLN   F CA    1 
ATOM   12890 C  C     . GLN   E 4  234 ? 14.646  39.859  108.771 1.00 114.60 ? 234 GLN   F C     1 
ATOM   12891 O  O     . GLN   E 4  234 ? 15.217  39.039  108.041 1.00 113.10 ? 234 GLN   F O     1 
ATOM   12892 C  CB    . GLN   E 4  234 ? 16.725  40.589  110.030 1.00 103.55 ? 234 GLN   F CB    1 
ATOM   12893 C  CG    . GLN   E 4  234 ? 17.517  39.515  109.309 1.00 116.09 ? 234 GLN   F CG    1 
ATOM   12894 C  CD    . GLN   E 4  234 ? 17.882  39.896  107.889 1.00 120.73 ? 234 GLN   F CD    1 
ATOM   12895 O  OE1   . GLN   E 4  234 ? 17.461  39.244  106.928 1.00 126.04 ? 234 GLN   F OE1   1 
ATOM   12896 N  NE2   . GLN   E 4  234 ? 18.679  40.951  107.747 1.00 107.85 ? 234 GLN   F NE2   1 
ATOM   12897 N  N     . ASP   E 4  235 ? 13.341  39.767  109.053 1.00 112.49 ? 235 ASP   F N     1 
ATOM   12898 C  CA    . ASP   E 4  235 ? 12.542  38.682  108.485 1.00 108.31 ? 235 ASP   F CA    1 
ATOM   12899 C  C     . ASP   E 4  235 ? 12.311  38.874  106.991 1.00 112.95 ? 235 ASP   F C     1 
ATOM   12900 O  O     . ASP   E 4  235 ? 12.403  37.912  106.219 1.00 119.02 ? 235 ASP   F O     1 
ATOM   12901 C  CB    . ASP   E 4  235 ? 11.201  38.562  109.200 1.00 100.11 ? 235 ASP   F CB    1 
ATOM   12902 C  CG    . ASP   E 4  235 ? 10.414  37.364  108.728 1.00 98.95  ? 235 ASP   F CG    1 
ATOM   12903 O  OD1   . ASP   E 4  235 ? 11.041  36.415  108.214 1.00 91.04  ? 235 ASP   F OD1   1 
ATOM   12904 O  OD2   . ASP   E 4  235 ? 9.173   37.377  108.851 1.00 102.72 ? 235 ASP   F OD2   1 
ATOM   12905 N  N     . LYS   E 4  236 ? 11.991  40.096  106.566 1.00 105.32 ? 236 LYS   F N     1 
ATOM   12906 C  CA    . LYS   E 4  236 ? 11.870  40.412  105.143 1.00 99.10  ? 236 LYS   F CA    1 
ATOM   12907 C  C     . LYS   E 4  236 ? 10.756  39.594  104.494 1.00 96.20  ? 236 LYS   F C     1 
ATOM   12908 O  O     . LYS   E 4  236 ? 10.868  39.155  103.348 1.00 104.50 ? 236 LYS   F O     1 
ATOM   12909 C  CB    . LYS   E 4  236 ? 13.200  40.185  104.411 1.00 106.01 ? 236 LYS   F CB    1 
ATOM   12910 C  CG    . LYS   E 4  236 ? 14.430  40.774  105.093 1.00 101.87 ? 236 LYS   F CG    1 
ATOM   12911 C  CD    . LYS   E 4  236 ? 14.348  42.289  105.161 1.00 98.31  ? 236 LYS   F CD    1 
ATOM   12912 C  CE    . LYS   E 4  236 ? 15.567  42.879  105.854 1.00 100.87 ? 236 LYS   F CE    1 
ATOM   12913 N  NZ    . LYS   E 4  236 ? 16.819  42.624  105.087 1.00 103.56 ? 236 LYS   F NZ    1 
ATOM   12914 N  N     . THR   E 4  237 ? 9.674   39.374  105.231 1.00 87.45  ? 237 THR   F N     1 
ATOM   12915 C  CA    . THR   E 4  237 ? 8.628   38.488  104.739 1.00 84.13  ? 237 THR   F CA    1 
ATOM   12916 C  C     . THR   E 4  237 ? 7.264   39.044  105.095 1.00 87.61  ? 237 THR   F C     1 
ATOM   12917 O  O     . THR   E 4  237 ? 6.474   39.403  104.218 1.00 80.44  ? 237 THR   F O     1 
ATOM   12918 C  CB    . THR   E 4  237 ? 8.779   37.097  105.344 1.00 95.04  ? 237 THR   F CB    1 
ATOM   12919 O  OG1   . THR   E 4  237 ? 10.169  36.775  105.462 1.00 105.09 ? 237 THR   F OG1   1 
ATOM   12920 C  CG2   . THR   E 4  237 ? 8.091   36.074  104.478 1.00 83.39  ? 237 THR   F CG2   1 
ATOM   12921 N  N     . CYS   E 4  238 ? 6.978   39.058  106.399 1.00 91.85  ? 238 CYS   F N     1 
ATOM   12922 C  CA    . CYS   E 4  238 ? 5.861   39.825  106.931 1.00 80.42  ? 238 CYS   F CA    1 
ATOM   12923 C  C     . CYS   E 4  238 ? 6.124   41.320  106.835 1.00 80.09  ? 238 CYS   F C     1 
ATOM   12924 O  O     . CYS   E 4  238 ? 5.180   42.104  106.671 1.00 78.46  ? 238 CYS   F O     1 
ATOM   12925 C  CB    . CYS   E 4  238 ? 5.620   39.441  108.390 1.00 78.85  ? 238 CYS   F CB    1 
ATOM   12926 S  SG    . CYS   E 4  238 ? 6.933   40.032  109.529 1.00 75.81  ? 238 CYS   F SG    1 
ATOM   12927 N  N     . HIS   E 4  239 ? 7.397   41.727  106.943 1.00 77.00  ? 239 HIS   F N     1 
ATOM   12928 C  CA    . HIS   E 4  239 ? 7.783   43.137  106.917 1.00 81.63  ? 239 HIS   F CA    1 
ATOM   12929 C  C     . HIS   E 4  239 ? 7.738   43.738  105.513 1.00 84.44  ? 239 HIS   F C     1 
ATOM   12930 O  O     . HIS   E 4  239 ? 7.614   44.962  105.385 1.00 76.54  ? 239 HIS   F O     1 
ATOM   12931 C  CB    . HIS   E 4  239 ? 9.201   43.311  107.487 1.00 87.21  ? 239 HIS   F CB    1 
ATOM   12932 C  CG    . HIS   E 4  239 ? 9.253   43.674  108.943 1.00 82.85  ? 239 HIS   F CG    1 
ATOM   12933 N  ND1   . HIS   E 4  239 ? 8.487   43.049  109.903 1.00 81.01  ? 239 HIS   F ND1   1 
ATOM   12934 C  CD2   . HIS   E 4  239 ? 10.018  44.576  109.605 1.00 82.40  ? 239 HIS   F CD2   1 
ATOM   12935 C  CE1   . HIS   E 4  239 ? 8.763   43.564  111.088 1.00 87.15  ? 239 HIS   F CE1   1 
ATOM   12936 N  NE2   . HIS   E 4  239 ? 9.688   44.494  110.935 1.00 86.73  ? 239 HIS   F NE2   1 
ATOM   12937 N  N     . LEU   E 4  240 ? 7.843   42.912  104.467 1.00 87.71  ? 240 LEU   F N     1 
ATOM   12938 C  CA    . LEU   E 4  240 ? 7.901   43.358  103.078 1.00 67.67  ? 240 LEU   F CA    1 
ATOM   12939 C  C     . LEU   E 4  240 ? 6.692   42.855  102.309 1.00 74.26  ? 240 LEU   F C     1 
ATOM   12940 O  O     . LEU   E 4  240 ? 6.388   41.659  102.329 1.00 79.30  ? 240 LEU   F O     1 
ATOM   12941 C  CB    . LEU   E 4  240 ? 9.159   42.854  102.389 1.00 73.83  ? 240 LEU   F CB    1 
ATOM   12942 C  CG    . LEU   E 4  240 ? 10.221  43.889  102.074 1.00 74.45  ? 240 LEU   F CG    1 
ATOM   12943 C  CD1   . LEU   E 4  240 ? 10.777  44.503  103.347 1.00 57.60  ? 240 LEU   F CD1   1 
ATOM   12944 C  CD2   . LEU   E 4  240 ? 11.299  43.208  101.264 1.00 76.86  ? 240 LEU   F CD2   1 
ATOM   12945 N  N     . THR   E 4  241 ? 6.030   43.761  101.605 1.00 78.61  ? 241 THR   F N     1 
ATOM   12946 C  CA    . THR   E 4  241 ? 4.802   43.446  100.896 1.00 78.25  ? 241 THR   F CA    1 
ATOM   12947 C  C     . THR   E 4  241 ? 5.011   43.298  99.399  1.00 81.89  ? 241 THR   F C     1 
ATOM   12948 O  O     . THR   E 4  241 ? 4.036   43.082  98.666  1.00 76.30  ? 241 THR   F O     1 
ATOM   12949 C  CB    . THR   E 4  241 ? 3.769   44.532  101.163 1.00 67.75  ? 241 THR   F CB    1 
ATOM   12950 O  OG1   . THR   E 4  241 ? 3.727   45.409  100.033 1.00 78.35  ? 241 THR   F OG1   1 
ATOM   12951 C  CG2   . THR   E 4  241 ? 4.180   45.324  102.395 1.00 53.95  ? 241 THR   F CG2   1 
ATOM   12952 N  N     . ASN   E 4  242 ? 6.251   43.432  98.932  1.00 86.44  ? 242 ASN   F N     1 
ATOM   12953 C  CA    . ASN   E 4  242 ? 6.610   43.226  97.538  1.00 91.02  ? 242 ASN   F CA    1 
ATOM   12954 C  C     . ASN   E 4  242 ? 5.946   41.976  96.987  1.00 93.23  ? 242 ASN   F C     1 
ATOM   12955 O  O     . ASN   E 4  242 ? 6.183   40.868  97.479  1.00 96.87  ? 242 ASN   F O     1 
ATOM   12956 C  CB    . ASN   E 4  242 ? 8.128   43.104  97.415  1.00 89.69  ? 242 ASN   F CB    1 
ATOM   12957 C  CG    . ASN   E 4  242 ? 8.788   44.419  97.095  1.00 94.61  ? 242 ASN   F CG    1 
ATOM   12958 O  OD1   . ASN   E 4  242 ? 8.249   45.490  97.387  1.00 103.46 ? 242 ASN   F OD1   1 
ATOM   12959 N  ND2   . ASN   E 4  242 ? 9.961   44.350  96.483  1.00 83.94  ? 242 ASN   F ND2   1 
ATOM   12960 N  N     . HIS   E 4  243 ? 5.119   42.148  95.957  1.00 86.07  ? 243 HIS   F N     1 
ATOM   12961 C  CA    . HIS   E 4  243 ? 4.372   41.031  95.394  1.00 81.27  ? 243 HIS   F CA    1 
ATOM   12962 C  C     . HIS   E 4  243 ? 5.247   39.807  95.151  1.00 86.07  ? 243 HIS   F C     1 
ATOM   12963 O  O     . HIS   E 4  243 ? 4.785   38.668  95.276  1.00 90.49  ? 243 HIS   F O     1 
ATOM   12964 C  CB    . HIS   E 4  243 ? 3.705   41.434  94.089  1.00 81.31  ? 243 HIS   F CB    1 
ATOM   12965 C  CG    . HIS   E 4  243 ? 2.684   40.449  93.631  1.00 87.41  ? 243 HIS   F CG    1 
ATOM   12966 N  ND1   . HIS   E 4  243 ? 1.431   40.371  94.199  1.00 88.31  ? 243 HIS   F ND1   1 
ATOM   12967 C  CD2   . HIS   E 4  243 ? 2.740   39.469  92.699  1.00 83.80  ? 243 HIS   F CD2   1 
ATOM   12968 C  CE1   . HIS   E 4  243 ? 0.748   39.407  93.611  1.00 85.01  ? 243 HIS   F CE1   1 
ATOM   12969 N  NE2   . HIS   E 4  243 ? 1.519   38.840  92.702  1.00 82.29  ? 243 HIS   F NE2   1 
ATOM   12970 N  N     . CYS   E 4  244 ? 6.507   40.030  94.793  1.00 90.98  ? 244 CYS   F N     1 
ATOM   12971 C  CA    . CYS   E 4  244 ? 7.450   38.938  94.599  1.00 92.30  ? 244 CYS   F CA    1 
ATOM   12972 C  C     . CYS   E 4  244 ? 7.618   38.138  95.885  1.00 93.14  ? 244 CYS   F C     1 
ATOM   12973 O  O     . CYS   E 4  244 ? 7.047   37.048  96.029  1.00 89.97  ? 244 CYS   F O     1 
ATOM   12974 C  CB    . CYS   E 4  244 ? 8.798   39.487  94.125  1.00 95.49  ? 244 CYS   F CB    1 
ATOM   12975 S  SG    . CYS   E 4  244 ? 8.666   40.918  93.014  1.00 98.76  ? 244 CYS   F SG    1 
ATOM   12976 N  N     . ILE   E 4  245 ? 8.374   38.700  96.833  1.00 91.87  ? 245 ILE   F N     1 
ATOM   12977 C  CA    . ILE   E 4  245 ? 8.785   38.008  98.055  1.00 97.06  ? 245 ILE   F CA    1 
ATOM   12978 C  C     . ILE   E 4  245 ? 7.585   37.427  98.801  1.00 91.34  ? 245 ILE   F C     1 
ATOM   12979 O  O     . ILE   E 4  245 ? 7.741   36.556  99.666  1.00 87.59  ? 245 ILE   F O     1 
ATOM   12980 C  CB    . ILE   E 4  245 ? 9.605   38.945  98.970  1.00 92.48  ? 245 ILE   F CB    1 
ATOM   12981 C  CG1   . ILE   E 4  245 ? 8.711   39.938  99.717  1.00 94.66  ? 245 ILE   F CG1   1 
ATOM   12982 C  CG2   . ILE   E 4  245 ? 10.625  39.724  98.160  1.00 91.48  ? 245 ILE   F CG2   1 
ATOM   12983 C  CD1   . ILE   E 4  245 ? 8.280   39.469  101.101 1.00 94.51  ? 245 ILE   F CD1   1 
ATOM   12984 N  N     . GLN   E 4  246 ? 6.379   37.900  98.476  1.00 85.12  ? 246 GLN   F N     1 
ATOM   12985 C  CA    . GLN   E 4  246 ? 5.185   37.328  99.084  1.00 83.58  ? 246 GLN   F CA    1 
ATOM   12986 C  C     . GLN   E 4  246 ? 4.726   36.085  98.337  1.00 92.26  ? 246 GLN   F C     1 
ATOM   12987 O  O     . GLN   E 4  246 ? 4.204   35.148  98.952  1.00 93.02  ? 246 GLN   F O     1 
ATOM   12988 C  CB    . GLN   E 4  246 ? 4.067   38.365  99.137  1.00 77.79  ? 246 GLN   F CB    1 
ATOM   12989 C  CG    . GLN   E 4  246 ? 4.144   39.272  100.344 1.00 80.20  ? 246 GLN   F CG    1 
ATOM   12990 C  CD    . GLN   E 4  246 ? 3.968   38.521  101.642 1.00 83.62  ? 246 GLN   F CD    1 
ATOM   12991 O  OE1   . GLN   E 4  246 ? 3.197   37.565  101.715 1.00 82.69  ? 246 GLN   F OE1   1 
ATOM   12992 N  NE2   . GLN   E 4  246 ? 4.688   38.948  102.678 1.00 83.37  ? 246 GLN   F NE2   1 
ATOM   12993 N  N     . LYS   E 4  247 ? 4.913   36.045  97.014  1.00 94.64  ? 247 LYS   F N     1 
ATOM   12994 C  CA    . LYS   E 4  247 ? 4.568   34.831  96.283  1.00 95.48  ? 247 LYS   F CA    1 
ATOM   12995 C  C     . LYS   E 4  247 ? 5.495   33.684  96.650  1.00 96.33  ? 247 LYS   F C     1 
ATOM   12996 O  O     . LYS   E 4  247 ? 5.204   32.531  96.313  1.00 102.92 ? 247 LYS   F O     1 
ATOM   12997 C  CB    . LYS   E 4  247 ? 4.582   35.079  94.771  1.00 87.64  ? 247 LYS   F CB    1 
ATOM   12998 C  CG    . LYS   E 4  247 ? 3.303   35.757  94.233  1.00 89.86  ? 247 LYS   F CG    1 
ATOM   12999 C  CD    . LYS   E 4  247 ? 2.019   34.944  94.499  1.00 79.54  ? 247 LYS   F CD    1 
ATOM   13000 C  CE    . LYS   E 4  247 ? 1.572   34.998  95.964  1.00 65.67  ? 247 LYS   F CE    1 
ATOM   13001 N  NZ    . LYS   E 4  247 ? 0.562   33.965  96.277  1.00 70.20  ? 247 LYS   F NZ    1 
ATOM   13002 N  N     . GLU   E 4  248 ? 6.586   33.972  97.366  1.00 93.77  ? 248 GLU   F N     1 
ATOM   13003 C  CA    . GLU   E 4  248 ? 7.468   32.914  97.846  1.00 87.89  ? 248 GLU   F CA    1 
ATOM   13004 C  C     . GLU   E 4  248 ? 6.830   32.106  98.975  1.00 92.90  ? 248 GLU   F C     1 
ATOM   13005 O  O     . GLU   E 4  248 ? 7.087   30.903  99.085  1.00 98.74  ? 248 GLU   F O     1 
ATOM   13006 C  CB    . GLU   E 4  248 ? 8.798   33.510  98.307  1.00 87.64  ? 248 GLU   F CB    1 
ATOM   13007 C  CG    . GLU   E 4  248 ? 10.015  32.701  97.922  1.00 81.33  ? 248 GLU   F CG    1 
ATOM   13008 C  CD    . GLU   E 4  248 ? 11.234  33.569  97.628  1.00 90.38  ? 248 GLU   F CD    1 
ATOM   13009 O  OE1   . GLU   E 4  248 ? 11.790  34.171  98.574  1.00 92.74  ? 248 GLU   F OE1   1 
ATOM   13010 O  OE2   . GLU   E 4  248 ? 11.630  33.658  96.444  1.00 82.30  ? 248 GLU   F OE2   1 
ATOM   13011 N  N     . TYR   E 4  249 ? 5.984   32.731  99.812  1.00 96.43  ? 249 TYR   F N     1 
ATOM   13012 C  CA    . TYR   E 4  249 ? 5.512   32.102  101.052 1.00 92.15  ? 249 TYR   F CA    1 
ATOM   13013 C  C     . TYR   E 4  249 ? 3.995   32.000  101.176 1.00 95.33  ? 249 TYR   F C     1 
ATOM   13014 O  O     . TYR   E 4  249 ? 3.484   30.960  101.626 1.00 84.77  ? 249 TYR   F O     1 
ATOM   13015 C  CB    . TYR   E 4  249 ? 6.076   32.859  102.264 1.00 74.68  ? 249 TYR   F CB    1 
ATOM   13016 C  CG    . TYR   E 4  249 ? 7.552   33.149  102.144 1.00 91.17  ? 249 TYR   F CG    1 
ATOM   13017 C  CD1   . TYR   E 4  249 ? 8.489   32.129  102.211 1.00 85.64  ? 249 TYR   F CD1   1 
ATOM   13018 C  CD2   . TYR   E 4  249 ? 8.009   34.444  101.961 1.00 99.08  ? 249 TYR   F CD2   1 
ATOM   13019 C  CE1   . TYR   E 4  249 ? 9.840   32.393  102.100 1.00 88.19  ? 249 TYR   F CE1   1 
ATOM   13020 C  CE2   . TYR   E 4  249 ? 9.361   34.720  101.857 1.00 96.86  ? 249 TYR   F CE2   1 
ATOM   13021 C  CZ    . TYR   E 4  249 ? 10.271  33.690  101.923 1.00 95.46  ? 249 TYR   F CZ    1 
ATOM   13022 O  OH    . TYR   E 4  249 ? 11.620  33.961  101.811 1.00 99.90  ? 249 TYR   F OH    1 
ATOM   13023 N  N     . SER   E 4  250 ? 3.261   33.059  100.829 1.00 98.35  ? 250 SER   F N     1 
ATOM   13024 C  CA    . SER   E 4  250 ? 1.783   33.118  100.884 1.00 93.06  ? 250 SER   F CA    1 
ATOM   13025 C  C     . SER   E 4  250 ? 1.138   32.235  101.954 1.00 83.81  ? 250 SER   F C     1 
ATOM   13026 O  O     . SER   E 4  250 ? -0.091  32.227  102.081 1.00 70.98  ? 250 SER   F O     1 
ATOM   13027 C  CB    . SER   E 4  250 ? 1.178   32.772  99.508  1.00 77.97  ? 250 SER   F CB    1 
ATOM   13028 O  OG    . SER   E 4  250 ? -0.237  32.892  99.509  1.00 90.41  ? 250 SER   F OG    1 
ATOM   13029 N  N     . ARG   E 4  255 ? -3.176  33.275  100.097 1.00 62.65  ? 255 ARG   F N     1 
ATOM   13030 C  CA    . ARG   E 4  255 ? -4.174  32.627  100.955 1.00 68.47  ? 255 ARG   F CA    1 
ATOM   13031 C  C     . ARG   E 4  255 ? -5.554  33.294  100.957 1.00 81.44  ? 255 ARG   F C     1 
ATOM   13032 O  O     . ARG   E 4  255 ? -6.506  32.745  100.386 1.00 89.34  ? 255 ARG   F O     1 
ATOM   13033 C  CB    . ARG   E 4  255 ? -3.684  32.549  102.404 1.00 70.36  ? 255 ARG   F CB    1 
ATOM   13034 C  CG    . ARG   E 4  255 ? -4.827  32.249  103.387 1.00 77.55  ? 255 ARG   F CG    1 
ATOM   13035 C  CD    . ARG   E 4  255 ? -4.356  31.860  104.798 1.00 89.77  ? 255 ARG   F CD    1 
ATOM   13036 N  NE    . ARG   E 4  255 ? -5.482  31.582  105.690 1.00 98.27  ? 255 ARG   F NE    1 
ATOM   13037 C  CZ    . ARG   E 4  255 ? -5.373  31.145  106.939 1.00 100.09 ? 255 ARG   F CZ    1 
ATOM   13038 N  NH1   . ARG   E 4  255 ? -4.193  30.891  107.484 1.00 97.86  ? 255 ARG   F NH1   1 
ATOM   13039 N  NH2   . ARG   E 4  255 ? -6.476  30.960  107.662 1.00 85.93  ? 255 ARG   F NH2   1 
ATOM   13040 N  N     . TYR   E 4  256 ? -5.672  34.451  101.631 1.00 77.18  ? 256 TYR   F N     1 
ATOM   13041 C  CA    . TYR   E 4  256 ? -6.968  35.125  101.722 1.00 73.09  ? 256 TYR   F CA    1 
ATOM   13042 C  C     . TYR   E 4  256 ? -7.330  35.807  100.409 1.00 69.36  ? 256 TYR   F C     1 
ATOM   13043 O  O     . TYR   E 4  256 ? -8.495  35.797  99.987  1.00 67.24  ? 256 TYR   F O     1 
ATOM   13044 C  CB    . TYR   E 4  256 ? -6.972  36.164  102.841 1.00 62.27  ? 256 TYR   F CB    1 
ATOM   13045 C  CG    . TYR   E 4  256 ? -6.059  35.887  104.006 1.00 71.52  ? 256 TYR   F CG    1 
ATOM   13046 C  CD1   . TYR   E 4  256 ? -6.465  35.088  105.067 1.00 84.81  ? 256 TYR   F CD1   1 
ATOM   13047 C  CD2   . TYR   E 4  256 ? -4.798  36.455  104.066 1.00 73.12  ? 256 TYR   F CD2   1 
ATOM   13048 C  CE1   . TYR   E 4  256 ? -5.625  34.850  106.148 1.00 80.28  ? 256 TYR   F CE1   1 
ATOM   13049 C  CE2   . TYR   E 4  256 ? -3.958  36.228  105.140 1.00 74.93  ? 256 TYR   F CE2   1 
ATOM   13050 C  CZ    . TYR   E 4  256 ? -4.371  35.424  106.177 1.00 72.91  ? 256 TYR   F CZ    1 
ATOM   13051 O  OH    . TYR   E 4  256 ? -3.519  35.207  107.244 1.00 74.19  ? 256 TYR   F OH    1 
ATOM   13052 N  N     . GLU   E 4  257 ? -6.351  36.423  99.765  1.00 59.47  ? 257 GLU   F N     1 
ATOM   13053 C  CA    . GLU   E 4  257 ? -6.554  37.140  98.523  1.00 65.95  ? 257 GLU   F CA    1 
ATOM   13054 C  C     . GLU   E 4  257 ? -5.910  36.351  97.392  1.00 71.08  ? 257 GLU   F C     1 
ATOM   13055 O  O     . GLU   E 4  257 ? -4.842  35.757  97.571  1.00 77.57  ? 257 GLU   F O     1 
ATOM   13056 C  CB    . GLU   E 4  257 ? -5.963  38.556  98.618  1.00 64.11  ? 257 GLU   F CB    1 
ATOM   13057 C  CG    . GLU   E 4  257 ? -6.723  39.514  99.557  1.00 64.59  ? 257 GLU   F CG    1 
ATOM   13058 C  CD    . GLU   E 4  257 ? -6.563  39.195  101.058 1.00 74.03  ? 257 GLU   F CD    1 
ATOM   13059 O  OE1   . GLU   E 4  257 ? -5.424  39.311  101.575 1.00 67.85  ? 257 GLU   F OE1   1 
ATOM   13060 O  OE2   . GLU   E 4  257 ? -7.581  38.846  101.722 1.00 63.16  ? 257 GLU   F OE2   1 
ATOM   13061 N  N     . GLU   E 4  258 ? -6.576  36.322  96.238  1.00 68.15  ? 258 GLU   F N     1 
ATOM   13062 C  CA    . GLU   E 4  258 ? -6.000  35.721  95.039  1.00 76.06  ? 258 GLU   F CA    1 
ATOM   13063 C  C     . GLU   E 4  258 ? -4.685  36.408  94.659  1.00 75.12  ? 258 GLU   F C     1 
ATOM   13064 O  O     . GLU   E 4  258 ? -4.687  37.533  94.148  1.00 72.67  ? 258 GLU   F O     1 
ATOM   13065 C  CB    . GLU   E 4  258 ? -7.008  35.789  93.887  1.00 75.27  ? 258 GLU   F CB    1 
ATOM   13066 C  CG    . GLU   E 4  258 ? -6.402  35.593  92.503  1.00 73.07  ? 258 GLU   F CG    1 
ATOM   13067 C  CD    . GLU   E 4  258 ? -6.278  34.137  92.105  1.00 79.39  ? 258 GLU   F CD    1 
ATOM   13068 O  OE1   . GLU   E 4  258 ? -5.824  33.312  92.933  1.00 77.83  ? 258 GLU   F OE1   1 
ATOM   13069 O  OE2   . GLU   E 4  258 ? -6.649  33.821  90.953  1.00 76.39  ? 258 GLU   F OE2   1 
ATOM   13070 N  N     . GLY   E 4  259 ? -3.558  35.742  94.911  1.00 75.83  ? 259 GLY   F N     1 
ATOM   13071 C  CA    . GLY   E 4  259 ? -2.255  36.336  94.655  1.00 73.41  ? 259 GLY   F CA    1 
ATOM   13072 C  C     . GLY   E 4  259 ? -1.955  37.573  95.476  1.00 69.82  ? 259 GLY   F C     1 
ATOM   13073 O  O     . GLY   E 4  259 ? -1.285  38.484  94.987  1.00 73.84  ? 259 GLY   F O     1 
ATOM   13074 N  N     . ASN   E 4  260 ? -2.440  37.641  96.710  1.00 65.39  ? 260 ASN   F N     1 
ATOM   13075 C  CA    . ASN   E 4  260 ? -2.190  38.753  97.630  1.00 74.29  ? 260 ASN   F CA    1 
ATOM   13076 C  C     . ASN   E 4  260 ? -2.702  40.109  97.136  1.00 68.77  ? 260 ASN   F C     1 
ATOM   13077 O  O     . ASN   E 4  260 ? -2.297  41.146  97.675  1.00 59.21  ? 260 ASN   F O     1 
ATOM   13078 C  CB    . ASN   E 4  260 ? -0.698  38.868  97.969  1.00 70.50  ? 260 ASN   F CB    1 
ATOM   13079 C  CG    . ASN   E 4  260 ? -0.245  37.838  99.000  1.00 63.24  ? 260 ASN   F CG    1 
ATOM   13080 O  OD1   . ASN   E 4  260 ? 0.667   38.085  99.787  1.00 61.42  ? 260 ASN   F OD1   1 
ATOM   13081 N  ND2   . ASN   E 4  260 ? -0.884  36.680  98.996  1.00 75.50  ? 260 ASN   F ND2   1 
ATOM   13082 N  N     . GLU   E 4  261 ? -3.598  40.142  96.153  1.00 66.54  ? 261 GLU   F N     1 
ATOM   13083 C  CA    . GLU   E 4  261 ? -4.172  41.388  95.658  1.00 65.29  ? 261 GLU   F CA    1 
ATOM   13084 C  C     . GLU   E 4  261 ? -5.550  41.577  96.281  1.00 62.23  ? 261 GLU   F C     1 
ATOM   13085 O  O     . GLU   E 4  261 ? -6.475  40.802  96.007  1.00 59.49  ? 261 GLU   F O     1 
ATOM   13086 C  CB    . GLU   E 4  261 ? -4.262  41.389  94.130  1.00 61.82  ? 261 GLU   F CB    1 
ATOM   13087 C  CG    . GLU   E 4  261 ? -2.934  41.632  93.426  1.00 62.42  ? 261 GLU   F CG    1 
ATOM   13088 C  CD    . GLU   E 4  261 ? -2.990  41.361  91.929  1.00 71.12  ? 261 GLU   F CD    1 
ATOM   13089 O  OE1   . GLU   E 4  261 ? -4.069  40.962  91.428  1.00 71.90  ? 261 GLU   F OE1   1 
ATOM   13090 O  OE2   . GLU   E 4  261 ? -1.948  41.547  91.258  1.00 60.17  ? 261 GLU   F OE2   1 
ATOM   13091 N  N     . MET   E 4  262 ? -5.693  42.605  97.112  1.00 57.33  ? 262 MET   F N     1 
ATOM   13092 C  CA    . MET   E 4  262 ? -7.014  43.050  97.535  1.00 59.90  ? 262 MET   F CA    1 
ATOM   13093 C  C     . MET   E 4  262 ? -7.348  44.326  96.779  1.00 58.22  ? 262 MET   F C     1 
ATOM   13094 O  O     . MET   E 4  262 ? -6.520  45.241  96.703  1.00 54.07  ? 262 MET   F O     1 
ATOM   13095 C  CB    . MET   E 4  262 ? -7.114  43.284  99.048  1.00 51.10  ? 262 MET   F CB    1 
ATOM   13096 C  CG    . MET   E 4  262 ? -8.454  43.935  99.432  1.00 50.97  ? 262 MET   F CG    1 
ATOM   13097 S  SD    . MET   E 4  262 ? -8.913  43.989  101.185 1.00 54.10  ? 262 MET   F SD    1 
ATOM   13098 C  CE    . MET   E 4  262 ? -7.356  44.477  101.913 1.00 48.43  ? 262 MET   F CE    1 
ATOM   13099 N  N     . PHE   E 4  263 ? -8.548  44.365  96.203  1.00 57.44  ? 263 PHE   F N     1 
ATOM   13100 C  CA    . PHE   E 4  263 ? -9.020  45.490  95.411  1.00 56.25  ? 263 PHE   F CA    1 
ATOM   13101 C  C     . PHE   E 4  263 ? -9.850  46.413  96.300  1.00 56.20  ? 263 PHE   F C     1 
ATOM   13102 O  O     . PHE   E 4  263 ? -9.941  46.220  97.518  1.00 55.40  ? 263 PHE   F O     1 
ATOM   13103 C  CB    . PHE   E 4  263 ? -9.788  44.990  94.183  1.00 59.06  ? 263 PHE   F CB    1 
ATOM   13104 C  CG    . PHE   E 4  263 ? -8.912  44.314  93.175  1.00 56.67  ? 263 PHE   F CG    1 
ATOM   13105 C  CD1   . PHE   E 4  263 ? -8.500  43.008  93.371  1.00 60.77  ? 263 PHE   F CD1   1 
ATOM   13106 C  CD2   . PHE   E 4  263 ? -8.457  44.996  92.053  1.00 63.95  ? 263 PHE   F CD2   1 
ATOM   13107 C  CE1   . PHE   E 4  263 ? -7.658  42.373  92.455  1.00 68.71  ? 263 PHE   F CE1   1 
ATOM   13108 C  CE2   . PHE   E 4  263 ? -7.616  44.367  91.126  1.00 65.35  ? 263 PHE   F CE2   1 
ATOM   13109 C  CZ    . PHE   E 4  263 ? -7.214  43.051  91.331  1.00 56.78  ? 263 PHE   F CZ    1 
ATOM   13110 N  N     . PHE   E 4  264 ? -10.472 47.434  95.698  1.00 58.31  ? 264 PHE   F N     1 
ATOM   13111 C  CA    . PHE   E 4  264 ? -10.965 48.531  96.525  1.00 48.85  ? 264 PHE   F CA    1 
ATOM   13112 C  C     . PHE   E 4  264 ? -12.302 48.226  97.177  1.00 48.91  ? 264 PHE   F C     1 
ATOM   13113 O  O     . PHE   E 4  264 ? -12.515 48.607  98.332  1.00 52.45  ? 264 PHE   F O     1 
ATOM   13114 C  CB    . PHE   E 4  264 ? -11.040 49.811  95.716  1.00 46.26  ? 264 PHE   F CB    1 
ATOM   13115 C  CG    . PHE   E 4  264 ? -9.784  50.617  95.791  1.00 51.68  ? 264 PHE   F CG    1 
ATOM   13116 C  CD1   . PHE   E 4  264 ? -8.673  50.114  96.455  1.00 47.42  ? 264 PHE   F CD1   1 
ATOM   13117 C  CD2   . PHE   E 4  264 ? -9.713  51.881  95.235  1.00 42.16  ? 264 PHE   F CD2   1 
ATOM   13118 C  CE1   . PHE   E 4  264 ? -7.523  50.844  96.538  1.00 44.32  ? 264 PHE   F CE1   1 
ATOM   13119 C  CE2   . PHE   E 4  264 ? -8.572  52.612  95.322  1.00 33.06  ? 264 PHE   F CE2   1 
ATOM   13120 C  CZ    . PHE   E 4  264 ? -7.472  52.094  95.961  1.00 43.53  ? 264 PHE   F CZ    1 
ATOM   13121 N  N     . GLU   E 4  265 ? -13.206 47.529  96.474  1.00 53.09  ? 265 GLU   F N     1 
ATOM   13122 C  CA    . GLU   E 4  265 ? -14.519 47.229  97.054  1.00 50.79  ? 265 GLU   F CA    1 
ATOM   13123 C  C     . GLU   E 4  265 ? -14.385 46.388  98.321  1.00 51.34  ? 265 GLU   F C     1 
ATOM   13124 O  O     . GLU   E 4  265 ? -15.103 46.612  99.306  1.00 54.89  ? 265 GLU   F O     1 
ATOM   13125 C  CB    . GLU   E 4  265 ? -15.416 46.525  96.033  1.00 40.89  ? 265 GLU   F CB    1 
ATOM   13126 C  CG    . GLU   E 4  265 ? -16.897 46.556  96.380  1.00 40.10  ? 265 GLU   F CG    1 
ATOM   13127 C  CD    . GLU   E 4  265 ? -17.731 45.661  95.474  1.00 48.31  ? 265 GLU   F CD    1 
ATOM   13128 O  OE1   . GLU   E 4  265 ? -17.156 44.733  94.863  1.00 48.36  ? 265 GLU   F OE1   1 
ATOM   13129 O  OE2   . GLU   E 4  265 ? -18.964 45.879  95.370  1.00 58.35  ? 265 GLU   F OE2   1 
ATOM   13130 N  N     . GLU   E 4  266 ? -13.463 45.427  98.323  1.00 42.96  ? 266 GLU   F N     1 
ATOM   13131 C  CA    . GLU   E 4  266 ? -13.193 44.668  99.538  1.00 52.03  ? 266 GLU   F CA    1 
ATOM   13132 C  C     . GLU   E 4  266 ? -12.565 45.552  100.611 1.00 58.18  ? 266 GLU   F C     1 
ATOM   13133 O  O     . GLU   E 4  266 ? -13.022 45.575  101.761 1.00 53.67  ? 266 GLU   F O     1 
ATOM   13134 C  CB    . GLU   E 4  266 ? -12.289 43.480  99.219  1.00 51.71  ? 266 GLU   F CB    1 
ATOM   13135 C  CG    . GLU   E 4  266 ? -11.936 42.627  100.414 1.00 52.67  ? 266 GLU   F CG    1 
ATOM   13136 C  CD    . GLU   E 4  266 ? -11.193 41.373  99.996  1.00 60.53  ? 266 GLU   F CD    1 
ATOM   13137 O  OE1   . GLU   E 4  266 ? -11.148 41.125  98.770  1.00 59.50  ? 266 GLU   F OE1   1 
ATOM   13138 O  OE2   . GLU   E 4  266 ? -10.650 40.653  100.871 1.00 55.73  ? 266 GLU   F OE2   1 
ATOM   13139 N  N     . PHE   E 4  267 ? -11.520 46.303  100.252 1.00 53.73  ? 267 PHE   F N     1 
ATOM   13140 C  CA    . PHE   E 4  267 ? -10.864 47.130  101.255 1.00 43.61  ? 267 PHE   F CA    1 
ATOM   13141 C  C     . PHE   E 4  267 ? -11.807 48.193  101.796 1.00 49.61  ? 267 PHE   F C     1 
ATOM   13142 O  O     . PHE   E 4  267 ? -11.725 48.563  102.973 1.00 54.73  ? 267 PHE   F O     1 
ATOM   13143 C  CB    . PHE   E 4  267 ? -9.611  47.784  100.697 1.00 35.83  ? 267 PHE   F CB    1 
ATOM   13144 C  CG    . PHE   E 4  267 ? -8.819  48.511  101.739 1.00 45.03  ? 267 PHE   F CG    1 
ATOM   13145 C  CD1   . PHE   E 4  267 ? -8.606  47.935  102.984 1.00 42.75  ? 267 PHE   F CD1   1 
ATOM   13146 C  CD2   . PHE   E 4  267 ? -8.296  49.769  101.488 1.00 45.54  ? 267 PHE   F CD2   1 
ATOM   13147 C  CE1   . PHE   E 4  267 ? -7.872  48.581  103.948 1.00 42.47  ? 267 PHE   F CE1   1 
ATOM   13148 C  CE2   . PHE   E 4  267 ? -7.561  50.428  102.448 1.00 43.24  ? 267 PHE   F CE2   1 
ATOM   13149 C  CZ    . PHE   E 4  267 ? -7.351  49.833  103.683 1.00 55.38  ? 267 PHE   F CZ    1 
ATOM   13150 N  N     . ASN   E 4  268 ? -12.704 48.711  100.953 1.00 49.43  ? 268 ASN   F N     1 
ATOM   13151 C  CA    . ASN   E 4  268 ? -13.687 49.665  101.454 1.00 53.36  ? 268 ASN   F CA    1 
ATOM   13152 C  C     . ASN   E 4  268 ? -14.550 49.003  102.511 1.00 53.67  ? 268 ASN   F C     1 
ATOM   13153 O  O     . ASN   E 4  268 ? -14.634 49.482  103.651 1.00 47.18  ? 268 ASN   F O     1 
ATOM   13154 C  CB    . ASN   E 4  268 ? -14.551 50.223  100.311 1.00 51.23  ? 268 ASN   F CB    1 
ATOM   13155 C  CG    . ASN   E 4  268 ? -15.289 51.525  100.700 1.00 47.04  ? 268 ASN   F CG    1 
ATOM   13156 O  OD1   . ASN   E 4  268 ? -14.679 52.591  100.875 1.00 46.51  ? 268 ASN   F OD1   1 
ATOM   13157 N  ND2   . ASN   E 4  268 ? -16.600 51.433  100.825 1.00 41.27  ? 268 ASN   F ND2   1 
ATOM   13158 N  N     . GLN   E 4  269 ? -15.165 47.870  102.150 1.00 52.63  ? 269 GLN   F N     1 
ATOM   13159 C  CA    . GLN   E 4  269 ? -15.942 47.070  103.095 1.00 56.17  ? 269 GLN   F CA    1 
ATOM   13160 C  C     . GLN   E 4  269 ? -15.218 46.892  104.430 1.00 51.23  ? 269 GLN   F C     1 
ATOM   13161 O  O     . GLN   E 4  269 ? -15.718 47.315  105.476 1.00 50.65  ? 269 GLN   F O     1 
ATOM   13162 C  CB    . GLN   E 4  269 ? -16.277 45.709  102.479 1.00 55.82  ? 269 GLN   F CB    1 
ATOM   13163 C  CG    . GLN   E 4  269 ? -17.582 45.700  101.706 1.00 53.11  ? 269 GLN   F CG    1 
ATOM   13164 C  CD    . GLN   E 4  269 ? -18.727 46.154  102.563 1.00 52.29  ? 269 GLN   F CD    1 
ATOM   13165 O  OE1   . GLN   E 4  269 ? -18.601 46.225  103.788 1.00 51.91  ? 269 GLN   F OE1   1 
ATOM   13166 N  NE2   . GLN   E 4  269 ? -19.852 46.468  101.937 1.00 48.87  ? 269 GLN   F NE2   1 
ATOM   13167 N  N     . TYR   E 4  270 ? -14.040 46.256  104.420 1.00 49.09  ? 270 TYR   F N     1 
ATOM   13168 C  CA    . TYR   E 4  270 ? -13.322 46.060  105.677 1.00 47.85  ? 270 TYR   F CA    1 
ATOM   13169 C  C     . TYR   E 4  270 ? -13.171 47.375  106.429 1.00 53.56  ? 270 TYR   F C     1 
ATOM   13170 O  O     . TYR   E 4  270 ? -13.390 47.429  107.646 1.00 55.62  ? 270 TYR   F O     1 
ATOM   13171 C  CB    . TYR   E 4  270 ? -11.951 45.440  105.428 1.00 48.19  ? 270 TYR   F CB    1 
ATOM   13172 C  CG    . TYR   E 4  270 ? -10.999 45.564  106.616 1.00 49.98  ? 270 TYR   F CG    1 
ATOM   13173 C  CD1   . TYR   E 4  270 ? -11.125 44.743  107.727 1.00 43.97  ? 270 TYR   F CD1   1 
ATOM   13174 C  CD2   . TYR   E 4  270 ? -9.968  46.489  106.614 1.00 49.50  ? 270 TYR   F CD2   1 
ATOM   13175 C  CE1   . TYR   E 4  270 ? -10.256 44.836  108.797 1.00 41.15  ? 270 TYR   F CE1   1 
ATOM   13176 C  CE2   . TYR   E 4  270 ? -9.094  46.591  107.687 1.00 47.68  ? 270 TYR   F CE2   1 
ATOM   13177 C  CZ    . TYR   E 4  270 ? -9.247  45.762  108.772 1.00 48.97  ? 270 TYR   F CZ    1 
ATOM   13178 O  OH    . TYR   E 4  270 ? -8.385  45.861  109.838 1.00 57.49  ? 270 TYR   F OH    1 
ATOM   13179 N  N     . LEU   E 4  271 ? -12.800 48.449  105.716 1.00 56.74  ? 271 LEU   F N     1 
ATOM   13180 C  CA    . LEU   E 4  271 ? -12.639 49.757  106.351 1.00 52.81  ? 271 LEU   F CA    1 
ATOM   13181 C  C     . LEU   E 4  271 ? -13.932 50.221  107.014 1.00 52.30  ? 271 LEU   F C     1 
ATOM   13182 O  O     . LEU   E 4  271 ? -13.893 50.940  108.020 1.00 52.77  ? 271 LEU   F O     1 
ATOM   13183 C  CB    . LEU   E 4  271 ? -12.162 50.784  105.319 1.00 43.07  ? 271 LEU   F CB    1 
ATOM   13184 C  CG    . LEU   E 4  271 ? -10.645 50.826  105.138 1.00 47.32  ? 271 LEU   F CG    1 
ATOM   13185 C  CD1   . LEU   E 4  271 ? -10.281 51.770  104.008 1.00 41.55  ? 271 LEU   F CD1   1 
ATOM   13186 C  CD2   . LEU   E 4  271 ? -9.904  51.185  106.457 1.00 44.39  ? 271 LEU   F CD2   1 
ATOM   13187 N  N     . MET   E 4  272 ? -15.079 49.830  106.461 1.00 42.29  ? 272 MET   F N     1 
ATOM   13188 C  CA    . MET   E 4  272 ? -16.359 50.151  107.071 1.00 48.55  ? 272 MET   F CA    1 
ATOM   13189 C  C     . MET   E 4  272 ? -16.660 49.219  108.233 1.00 60.15  ? 272 MET   F C     1 
ATOM   13190 O  O     . MET   E 4  272 ? -16.909 49.673  109.355 1.00 61.96  ? 272 MET   F O     1 
ATOM   13191 C  CB    . MET   E 4  272 ? -17.460 50.056  106.022 1.00 46.79  ? 272 MET   F CB    1 
ATOM   13192 C  CG    . MET   E 4  272 ? -17.290 51.039  104.895 1.00 54.17  ? 272 MET   F CG    1 
ATOM   13193 S  SD    . MET   E 4  272 ? -18.768 51.135  103.881 1.00 63.60  ? 272 MET   F SD    1 
ATOM   13194 C  CE    . MET   E 4  272 ? -18.861 49.484  103.208 1.00 50.75  ? 272 MET   F CE    1 
ATOM   13195 N  N     . ASP   E 4  273 ? -16.629 47.908  107.966 1.00 60.26  ? 273 ASP   F N     1 
ATOM   13196 C  CA    . ASP   E 4  273 ? -16.982 46.891  108.954 1.00 46.15  ? 273 ASP   F CA    1 
ATOM   13197 C  C     . ASP   E 4  273 ? -16.161 47.043  110.243 1.00 51.36  ? 273 ASP   F C     1 
ATOM   13198 O  O     . ASP   E 4  273 ? -16.720 47.034  111.348 1.00 58.71  ? 273 ASP   F O     1 
ATOM   13199 C  CB    . ASP   E 4  273 ? -16.818 45.494  108.325 1.00 55.70  ? 273 ASP   F CB    1 
ATOM   13200 C  CG    . ASP   E 4  273 ? -17.846 45.211  107.181 1.00 58.08  ? 273 ASP   F CG    1 
ATOM   13201 O  OD1   . ASP   E 4  273 ? -18.919 45.851  107.161 1.00 53.69  ? 273 ASP   F OD1   1 
ATOM   13202 O  OD2   . ASP   E 4  273 ? -17.593 44.327  106.319 1.00 50.51  ? 273 ASP   F OD2   1 
ATOM   13203 N  N     . ALA   E 4  274 ? -14.835 47.164  110.131 1.00 36.30  ? 274 ALA   F N     1 
ATOM   13204 C  CA    . ALA   E 4  274 ? -14.020 47.694  111.215 1.00 43.07  ? 274 ALA   F CA    1 
ATOM   13205 C  C     . ALA   E 4  274 ? -13.784 49.173  110.936 1.00 61.97  ? 274 ALA   F C     1 
ATOM   13206 O  O     . ALA   E 4  274 ? -14.280 49.716  109.947 1.00 65.64  ? 274 ALA   F O     1 
ATOM   13207 C  CB    . ALA   E 4  274 ? -12.698 46.944  111.343 1.00 39.96  ? 274 ALA   F CB    1 
ATOM   13208 N  N     . LEU   E 4  275 ? -13.040 49.847  111.812 1.00 49.95  ? 275 LEU   F N     1 
ATOM   13209 C  CA    A LEU   E 4  275 ? -12.665 51.237  111.560 1.00 52.35  ? 275 LEU   F CA    1 
ATOM   13210 C  CA    B LEU   E 4  275 ? -12.666 51.239  111.559 0.00 52.24  ? 275 LEU   F CA    1 
ATOM   13211 C  C     . LEU   E 4  275 ? -13.861 52.180  111.360 1.00 49.82  ? 275 LEU   F C     1 
ATOM   13212 O  O     . LEU   E 4  275 ? -13.817 53.338  111.795 1.00 43.15  ? 275 LEU   F O     1 
ATOM   13213 C  CB    A LEU   E 4  275 ? -11.729 51.308  110.353 1.00 50.51  ? 275 LEU   F CB    1 
ATOM   13214 C  CB    B LEU   E 4  275 ? -11.732 51.309  110.345 0.00 50.59  ? 275 LEU   F CB    1 
ATOM   13215 C  CG    A LEU   E 4  275 ? -10.335 50.745  110.609 1.00 50.49  ? 275 LEU   F CG    1 
ATOM   13216 C  CG    B LEU   E 4  275 ? -10.431 50.503  110.449 0.00 50.61  ? 275 LEU   F CG    1 
ATOM   13217 C  CD1   A LEU   E 4  275 ? -9.903  50.970  112.062 1.00 46.53  ? 275 LEU   F CD1   1 
ATOM   13218 C  CD1   B LEU   E 4  275 ? -10.540 49.179  109.701 0.00 51.30  ? 275 LEU   F CD1   1 
ATOM   13219 C  CD2   A LEU   E 4  275 ? -10.333 49.279  110.253 1.00 53.06  ? 275 LEU   F CD2   1 
ATOM   13220 C  CD2   B LEU   E 4  275 ? -9.233  51.308  109.958 0.00 50.05  ? 275 LEU   F CD2   1 
ATOM   13221 N  N     . ASN   E 4  276 ? -14.932 51.729  110.691 1.00 46.80  ? 276 ASN   F N     1 
ATOM   13222 C  CA    . ASN   E 4  276 ? -16.162 52.527  110.661 1.00 56.75  ? 276 ASN   F CA    1 
ATOM   13223 C  C     . ASN   E 4  276 ? -16.066 53.711  109.689 1.00 61.21  ? 276 ASN   F C     1 
ATOM   13224 O  O     . ASN   E 4  276 ? -16.773 54.721  109.821 1.00 55.01  ? 276 ASN   F O     1 
ATOM   13225 C  CB    . ASN   E 4  276 ? -16.473 53.003  112.097 1.00 63.74  ? 276 ASN   F CB    1 
ATOM   13226 C  CG    . ASN   E 4  276 ? -17.875 53.606  112.269 1.00 65.98  ? 276 ASN   F CG    1 
ATOM   13227 O  OD1   . ASN   E 4  276 ? -18.811 53.308  111.518 1.00 56.36  ? 276 ASN   F OD1   1 
ATOM   13228 N  ND2   . ASN   E 4  276 ? -18.015 54.455  113.292 1.00 64.86  ? 276 ASN   F ND2   1 
ATOM   13229 N  N     . THR   E 4  277 ? -15.209 53.594  108.684 1.00 56.13  ? 277 THR   F N     1 
ATOM   13230 C  CA    A THR   E 4  277 ? -14.992 54.699  107.769 0.98 49.18  ? 277 THR   F CA    1 
ATOM   13231 C  CA    B THR   E 4  277 ? -14.910 54.695  107.770 0.02 49.38  ? 277 THR   F CA    1 
ATOM   13232 C  C     . THR   E 4  277 ? -15.155 54.260  106.324 1.00 48.93  ? 277 THR   F C     1 
ATOM   13233 O  O     . THR   E 4  277 ? -15.640 53.153  106.048 1.00 47.31  ? 277 THR   F O     1 
ATOM   13234 C  CB    A THR   E 4  277 ? -13.601 55.268  107.975 0.98 49.91  ? 277 THR   F CB    1 
ATOM   13235 C  CB    B THR   E 4  277 ? -13.461 55.184  107.941 0.02 50.01  ? 277 THR   F CB    1 
ATOM   13236 O  OG1   A THR   E 4  277 ? -13.298 56.182  106.916 0.98 52.07  ? 277 THR   F OG1   1 
ATOM   13237 O  OG1   B THR   E 4  277 ? -13.177 56.189  106.962 0.02 51.36  ? 277 THR   F OG1   1 
ATOM   13238 C  CG2   A THR   E 4  277 ? -12.580 54.139  107.982 0.98 48.79  ? 277 THR   F CG2   1 
ATOM   13239 C  CG2   B THR   E 4  277 ? -12.481 54.028  107.768 0.02 49.24  ? 277 THR   F CG2   1 
ATOM   13240 N  N     . THR   E 4  278 ? -14.793 55.141  105.397 1.00 49.80  ? 278 THR   F N     1 
ATOM   13241 C  CA    . THR   E 4  278 ? -14.752 54.823  103.980 1.00 48.70  ? 278 THR   F CA    1 
ATOM   13242 C  C     . THR   E 4  278 ? -13.300 54.813  103.539 1.00 46.42  ? 278 THR   F C     1 
ATOM   13243 O  O     . THR   E 4  278 ? -12.432 55.425  104.175 1.00 39.72  ? 278 THR   F O     1 
ATOM   13244 C  CB    . THR   E 4  278 ? -15.536 55.829  103.128 1.00 50.00  ? 278 THR   F CB    1 
ATOM   13245 O  OG1   . THR   E 4  278 ? -16.856 55.961  103.645 1.00 56.98  ? 278 THR   F OG1   1 
ATOM   13246 C  CG2   . THR   E 4  278 ? -15.629 55.356  101.670 1.00 57.74  ? 278 THR   F CG2   1 
ATOM   13247 N  N     . LEU   E 4  279 ? -13.043 54.085  102.450 1.00 47.02  ? 279 LEU   F N     1 
ATOM   13248 C  CA    . LEU   E 4  279 ? -11.754 54.198  101.780 1.00 48.16  ? 279 LEU   F CA    1 
ATOM   13249 C  C     . LEU   E 4  279 ? -11.540 55.624  101.267 1.00 54.09  ? 279 LEU   F C     1 
ATOM   13250 O  O     . LEU   E 4  279 ? -10.435 56.179  101.381 1.00 49.86  ? 279 LEU   F O     1 
ATOM   13251 C  CB    . LEU   E 4  279 ? -11.681 53.159  100.656 1.00 42.60  ? 279 LEU   F CB    1 
ATOM   13252 C  CG    . LEU   E 4  279 ? -10.599 53.185  99.574  1.00 40.96  ? 279 LEU   F CG    1 
ATOM   13253 C  CD1   . LEU   E 4  279 ? -9.196  53.234  100.146 1.00 39.76  ? 279 LEU   F CD1   1 
ATOM   13254 C  CD2   . LEU   E 4  279 ? -10.773 51.986  98.662  1.00 39.21  ? 279 LEU   F CD2   1 
ATOM   13255 N  N     . GLU   E 4  280 ? -12.607 56.252  100.753 1.00 50.77  ? 280 GLU   F N     1 
ATOM   13256 C  CA    . GLU   E 4  280 ? -12.523 57.633  100.280 1.00 46.37  ? 280 GLU   F CA    1 
ATOM   13257 C  C     . GLU   E 4  280 ? -12.022 58.587  101.365 1.00 48.95  ? 280 GLU   F C     1 
ATOM   13258 O  O     . GLU   E 4  280 ? -11.073 59.348  101.151 1.00 53.34  ? 280 GLU   F O     1 
ATOM   13259 C  CB    . GLU   E 4  280 ? -13.884 58.093  99.773  1.00 53.25  ? 280 GLU   F CB    1 
ATOM   13260 C  CG    . GLU   E 4  280 ? -13.875 59.543  99.358  1.00 53.20  ? 280 GLU   F CG    1 
ATOM   13261 C  CD    . GLU   E 4  280 ? -12.822 59.814  98.306  1.00 57.10  ? 280 GLU   F CD    1 
ATOM   13262 O  OE1   . GLU   E 4  280 ? -12.868 59.164  97.230  1.00 54.46  ? 280 GLU   F OE1   1 
ATOM   13263 O  OE2   . GLU   E 4  280 ? -11.939 60.660  98.570  1.00 52.90  ? 280 GLU   F OE2   1 
ATOM   13264 N  N     . ASN   E 4  281 ? -12.674 58.596  102.527 1.00 47.94  ? 281 ASN   F N     1 
ATOM   13265 C  CA    . ASN   E 4  281 ? -12.376 59.630  103.512 1.00 42.50  ? 281 ASN   F CA    1 
ATOM   13266 C  C     . ASN   E 4  281 ? -11.024 59.391  104.183 1.00 44.56  ? 281 ASN   F C     1 
ATOM   13267 O  O     . ASN   E 4  281 ? -10.194 60.302  104.299 1.00 45.14  ? 281 ASN   F O     1 
ATOM   13268 C  CB    . ASN   E 4  281 ? -13.489 59.690  104.560 1.00 45.39  ? 281 ASN   F CB    1 
ATOM   13269 C  CG    . ASN   E 4  281 ? -14.833 60.115  103.992 1.00 44.14  ? 281 ASN   F CG    1 
ATOM   13270 O  OD1   . ASN   E 4  281 ? -15.124 59.934  102.810 1.00 44.89  ? 281 ASN   F OD1   1 
ATOM   13271 N  ND2   . ASN   E 4  281 ? -15.674 60.667  104.858 1.00 46.80  ? 281 ASN   F ND2   1 
ATOM   13272 N  N     . SER   E 4  282 ? -10.790 58.168  104.640 1.00 52.72  ? 282 SER   F N     1 
ATOM   13273 C  CA    . SER   E 4  282 ? -9.620  57.875  105.455 1.00 48.37  ? 282 SER   F CA    1 
ATOM   13274 C  C     . SER   E 4  282 ? -8.326  57.951  104.648 1.00 42.07  ? 282 SER   F C     1 
ATOM   13275 O  O     . SER   E 4  282 ? -7.339  58.531  105.112 1.00 36.46  ? 282 SER   F O     1 
ATOM   13276 C  CB    . SER   E 4  282 ? -9.792  56.493  106.090 1.00 46.41  ? 282 SER   F CB    1 
ATOM   13277 O  OG    . SER   E 4  282 ? -10.377 55.586  105.161 1.00 39.44  ? 282 SER   F OG    1 
ATOM   13278 N  N     . ILE   E 4  283 ? -8.313  57.388  103.434 1.00 43.01  ? 283 ILE   F N     1 
ATOM   13279 C  CA    . ILE   E 4  283 ? -7.081  57.131  102.697 1.00 43.56  ? 283 ILE   F CA    1 
ATOM   13280 C  C     . ILE   E 4  283 ? -7.011  57.917  101.386 1.00 49.97  ? 283 ILE   F C     1 
ATOM   13281 O  O     . ILE   E 4  283 ? -6.040  58.644  101.138 1.00 43.14  ? 283 ILE   F O     1 
ATOM   13282 C  CB    . ILE   E 4  283 ? -6.894  55.624  102.431 1.00 47.97  ? 283 ILE   F CB    1 
ATOM   13283 C  CG1   . ILE   E 4  283 ? -6.868  54.853  103.751 1.00 55.73  ? 283 ILE   F CG1   1 
ATOM   13284 C  CG2   . ILE   E 4  283 ? -5.615  55.405  101.644 1.00 51.59  ? 283 ILE   F CG2   1 
ATOM   13285 C  CD1   . ILE   E 4  283 ? -6.165  53.503  103.675 1.00 53.06  ? 283 ILE   F CD1   1 
ATOM   13286 N  N     . LEU   E 4  284 ? -8.033  57.775  100.524 1.00 44.05  ? 284 LEU   F N     1 
ATOM   13287 C  CA    A LEU   E 4  284 ? -7.920  58.282  99.157  1.00 42.85  ? 284 LEU   F CA    1 
ATOM   13288 C  CA    B LEU   E 4  284 ? -7.940  58.281  99.155  0.00 42.98  ? 284 LEU   F CA    1 
ATOM   13289 C  C     . LEU   E 4  284 ? -7.829  59.800  99.102  1.00 45.43  ? 284 LEU   F C     1 
ATOM   13290 O  O     . LEU   E 4  284 ? -7.224  60.344  98.174  1.00 48.22  ? 284 LEU   F O     1 
ATOM   13291 C  CB    A LEU   E 4  284 ? -9.089  57.790  98.313  1.00 42.34  ? 284 LEU   F CB    1 
ATOM   13292 C  CB    B LEU   E 4  284 ? -9.148  57.813  98.342  0.00 42.51  ? 284 LEU   F CB    1 
ATOM   13293 C  CG    A LEU   E 4  284 ? -8.652  56.935  97.127  1.00 38.70  ? 284 LEU   F CG    1 
ATOM   13294 C  CG    B LEU   E 4  284 ? -9.321  56.304  98.164  0.00 43.08  ? 284 LEU   F CG    1 
ATOM   13295 C  CD1   A LEU   E 4  284 ? -9.757  55.996  96.642  1.00 38.60  ? 284 LEU   F CD1   1 
ATOM   13296 C  CD1   B LEU   E 4  284 ? -10.554 56.006  97.325  0.00 42.53  ? 284 LEU   F CD1   1 
ATOM   13297 C  CD2   A LEU   E 4  284 ? -8.181  57.845  96.005  1.00 42.17  ? 284 LEU   F CD2   1 
ATOM   13298 C  CD2   B LEU   E 4  284 ? -8.080  55.688  97.537  0.00 41.91  ? 284 LEU   F CD2   1 
ATOM   13299 N  N     . LEU   E 4  285 ? -8.412  60.503  100.068 1.00 48.02  ? 285 LEU   F N     1 
ATOM   13300 C  CA    . LEU   E 4  285 ? -8.261  61.952  100.102 1.00 42.78  ? 285 LEU   F CA    1 
ATOM   13301 C  C     . LEU   E 4  285 ? -6.790  62.345  100.191 1.00 44.52  ? 285 LEU   F C     1 
ATOM   13302 O  O     . LEU   E 4  285 ? -6.318  63.191  99.427  1.00 55.44  ? 285 LEU   F O     1 
ATOM   13303 C  CB    . LEU   E 4  285 ? -9.044  62.527  101.273 1.00 48.25  ? 285 LEU   F CB    1 
ATOM   13304 C  CG    . LEU   E 4  285 ? -10.194 63.422  100.844 1.00 51.72  ? 285 LEU   F CG    1 
ATOM   13305 C  CD1   . LEU   E 4  285 ? -10.834 64.030  102.079 1.00 52.16  ? 285 LEU   F CD1   1 
ATOM   13306 C  CD2   . LEU   E 4  285 ? -9.675  64.495  99.903  1.00 51.28  ? 285 LEU   F CD2   1 
ATOM   13307 N  N     . GLN   E 4  286 ? -6.045  61.735  101.115 1.00 42.66  ? 286 GLN   F N     1 
ATOM   13308 C  CA    . GLN   E 4  286 ? -4.599  61.957  101.168 1.00 46.02  ? 286 GLN   F CA    1 
ATOM   13309 C  C     . GLN   E 4  286 ? -3.915  61.584  99.856  1.00 39.79  ? 286 GLN   F C     1 
ATOM   13310 O  O     . GLN   E 4  286 ? -2.954  62.238  99.440  1.00 46.42  ? 286 GLN   F O     1 
ATOM   13311 C  CB    . GLN   E 4  286 ? -3.964  61.132  102.295 1.00 48.46  ? 286 GLN   F CB    1 
ATOM   13312 C  CG    . GLN   E 4  286 ? -3.878  61.753  103.663 1.00 33.71  ? 286 GLN   F CG    1 
ATOM   13313 C  CD    . GLN   E 4  286 ? -4.781  61.044  104.626 1.00 40.19  ? 286 GLN   F CD    1 
ATOM   13314 O  OE1   . GLN   E 4  286 ? -5.978  60.889  104.358 1.00 43.41  ? 286 GLN   F OE1   1 
ATOM   13315 N  NE2   . GLN   E 4  286 ? -4.220  60.577  105.742 1.00 38.68  ? 286 GLN   F NE2   1 
ATOM   13316 N  N     . ILE   E 4  287 ? -4.351  60.494  99.227  1.00 39.02  ? 287 ILE   F N     1 
ATOM   13317 C  CA    . ILE   E 4  287 ? -3.668  59.998  98.036  1.00 43.74  ? 287 ILE   F CA    1 
ATOM   13318 C  C     . ILE   E 4  287 ? -3.793  61.009  96.901  1.00 42.20  ? 287 ILE   F C     1 
ATOM   13319 O  O     . ILE   E 4  287 ? -2.791  61.492  96.358  1.00 35.35  ? 287 ILE   F O     1 
ATOM   13320 C  CB    . ILE   E 4  287 ? -4.216  58.613  97.643  1.00 42.69  ? 287 ILE   F CB    1 
ATOM   13321 C  CG1   . ILE   E 4  287 ? -3.596  57.537  98.532  1.00 46.46  ? 287 ILE   F CG1   1 
ATOM   13322 C  CG2   . ILE   E 4  287 ? -3.911  58.292  96.200  1.00 44.11  ? 287 ILE   F CG2   1 
ATOM   13323 C  CD1   . ILE   E 4  287 ? -4.212  56.181  98.336  1.00 36.33  ? 287 ILE   F CD1   1 
ATOM   13324 N  N     . LYS   E 4  288 ? -5.032  61.359  96.540  1.00 42.56  ? 288 LYS   F N     1 
ATOM   13325 C  CA    . LYS   E 4  288 ? -5.244  62.390  95.528  1.00 39.28  ? 288 LYS   F CA    1 
ATOM   13326 C  C     . LYS   E 4  288 ? -4.416  63.628  95.832  1.00 42.63  ? 288 LYS   F C     1 
ATOM   13327 O  O     . LYS   E 4  288 ? -3.930  64.294  94.910  1.00 49.18  ? 288 LYS   F O     1 
ATOM   13328 C  CB    . LYS   E 4  288 ? -6.722  62.768  95.440  1.00 34.57  ? 288 LYS   F CB    1 
ATOM   13329 C  CG    . LYS   E 4  288 ? -7.680  61.670  95.005  1.00 29.87  ? 288 LYS   F CG    1 
ATOM   13330 C  CD    . LYS   E 4  288 ? -9.005  61.881  95.720  1.00 32.09  ? 288 LYS   F CD    1 
ATOM   13331 C  CE    . LYS   E 4  288 ? -10.174 61.269  94.981  1.00 35.29  ? 288 LYS   F CE    1 
ATOM   13332 N  NZ    . LYS   E 4  288 ? -11.442 61.922  95.441  1.00 40.36  ? 288 LYS   F NZ    1 
ATOM   13333 N  N     . HIS   E 4  289 ? -4.238  63.950  97.123  1.00 36.45  ? 289 HIS   F N     1 
ATOM   13334 C  CA    . HIS   E 4  289 ? -3.470  65.135  97.499  1.00 35.21  ? 289 HIS   F CA    1 
ATOM   13335 C  C     . HIS   E 4  289 ? -1.990  64.950  97.229  1.00 42.39  ? 289 HIS   F C     1 
ATOM   13336 O  O     . HIS   E 4  289 ? -1.291  65.920  96.901  1.00 43.22  ? 289 HIS   F O     1 
ATOM   13337 C  CB    . HIS   E 4  289 ? -3.660  65.488  98.973  1.00 39.54  ? 289 HIS   F CB    1 
ATOM   13338 C  CG    . HIS   E 4  289 ? -2.862  66.683  99.407  1.00 44.09  ? 289 HIS   F CG    1 
ATOM   13339 N  ND1   . HIS   E 4  289 ? -1.755  66.583  100.222 1.00 46.82  ? 289 HIS   F ND1   1 
ATOM   13340 C  CD2   . HIS   E 4  289 ? -3.004  68.002  99.129  1.00 38.46  ? 289 HIS   F CD2   1 
ATOM   13341 C  CE1   . HIS   E 4  289 ? -1.251  67.788  100.430 1.00 38.47  ? 289 HIS   F CE1   1 
ATOM   13342 N  NE2   . HIS   E 4  289 ? -1.993  68.667  99.781  1.00 41.00  ? 289 HIS   F NE2   1 
ATOM   13343 N  N     . ILE   E 4  290 ? -1.489  63.721  97.385  1.00 44.48  ? 290 ILE   F N     1 
ATOM   13344 C  CA    . ILE   E 4  290 ? -0.060  63.477  97.216  1.00 38.75  ? 290 ILE   F CA    1 
ATOM   13345 C  C     . ILE   E 4  290 ? 0.289   63.381  95.741  1.00 35.34  ? 290 ILE   F C     1 
ATOM   13346 O  O     . ILE   E 4  290 ? 1.322   63.890  95.302  1.00 39.81  ? 290 ILE   F O     1 
ATOM   13347 C  CB    . ILE   E 4  290 ? 0.358   62.220  97.996  1.00 39.31  ? 290 ILE   F CB    1 
ATOM   13348 C  CG1   . ILE   E 4  290 ? 0.178   62.482  99.502  1.00 40.36  ? 290 ILE   F CG1   1 
ATOM   13349 C  CG2   . ILE   E 4  290 ? 1.789   61.837  97.653  1.00 36.11  ? 290 ILE   F CG2   1 
ATOM   13350 C  CD1   . ILE   E 4  290 ? 0.193   61.255  100.400 1.00 30.36  ? 290 ILE   F CD1   1 
ATOM   13351 N  N     . ILE   E 4  291 ? -0.573  62.753  94.949  1.00 29.89  ? 291 ILE   F N     1 
ATOM   13352 C  CA    . ILE   E 4  291 ? -0.349  62.710  93.511  1.00 31.06  ? 291 ILE   F CA    1 
ATOM   13353 C  C     . ILE   E 4  291 ? -0.349  64.121  92.932  1.00 37.05  ? 291 ILE   F C     1 
ATOM   13354 O  O     . ILE   E 4  291 ? 0.533   64.494  92.148  1.00 29.78  ? 291 ILE   F O     1 
ATOM   13355 C  CB    . ILE   E 4  291 ? -1.415  61.837  92.836  1.00 34.53  ? 291 ILE   F CB    1 
ATOM   13356 C  CG1   . ILE   E 4  291 ? -1.442  60.439  93.452  1.00 33.05  ? 291 ILE   F CG1   1 
ATOM   13357 C  CG2   . ILE   E 4  291 ? -1.185  61.811  91.334  1.00 35.74  ? 291 ILE   F CG2   1 
ATOM   13358 C  CD1   . ILE   E 4  291 ? -2.647  59.626  92.997  1.00 30.54  ? 291 ILE   F CD1   1 
ATOM   13359 N  N     . ARG   E 4  292 ? -1.354  64.922  93.287  1.00 34.52  ? 292 ARG   F N     1 
ATOM   13360 C  CA    . ARG   E 4  292 ? -1.405  66.278  92.762  1.00 38.94  ? 292 ARG   F CA    1 
ATOM   13361 C  C     . ARG   E 4  292 ? -0.191  67.081  93.218  1.00 39.15  ? 292 ARG   F C     1 
ATOM   13362 O  O     . ARG   E 4  292 ? 0.447   67.769  92.418  1.00 34.23  ? 292 ARG   F O     1 
ATOM   13363 C  CB    . ARG   E 4  292 ? -2.704  66.964  93.181  1.00 41.62  ? 292 ARG   F CB    1 
ATOM   13364 C  CG    . ARG   E 4  292 ? -3.714  67.154  92.060  1.00 53.41  ? 292 ARG   F CG    1 
ATOM   13365 C  CD    . ARG   E 4  292 ? -4.676  68.322  92.324  1.00 51.18  ? 292 ARG   F CD    1 
ATOM   13366 N  NE    . ARG   E 4  292 ? -4.870  68.567  93.750  1.00 50.70  ? 292 ARG   F NE    1 
ATOM   13367 C  CZ    . ARG   E 4  292 ? -5.720  67.899  94.531  1.00 65.63  ? 292 ARG   F CZ    1 
ATOM   13368 N  NH1   . ARG   E 4  292 ? -6.523  66.952  94.041  1.00 47.84  ? 292 ARG   F NH1   1 
ATOM   13369 N  NH2   . ARG   E 4  292 ? -5.765  68.185  95.838  1.00 58.39  ? 292 ARG   F NH2   1 
ATOM   13370 N  N     . SER   E 4  293 ? 0.163   66.989  94.502  1.00 34.28  ? 293 SER   F N     1 
ATOM   13371 C  CA    . SER   E 4  293 ? 1.285   67.787  94.999  1.00 36.88  ? 293 SER   F CA    1 
ATOM   13372 C  C     . SER   E 4  293 ? 2.596   67.420  94.312  1.00 34.55  ? 293 SER   F C     1 
ATOM   13373 O  O     . SER   E 4  293 ? 3.402   68.301  93.989  1.00 37.00  ? 293 SER   F O     1 
ATOM   13374 C  CB    . SER   E 4  293 ? 1.430   67.632  96.512  1.00 35.28  ? 293 SER   F CB    1 
ATOM   13375 O  OG    . SER   E 4  293 ? 0.310   68.178  97.169  1.00 36.03  ? 293 SER   F OG    1 
ATOM   13376 N  N     . CYS   E 4  294 ? 2.846   66.123  94.111  1.00 39.89  ? 294 CYS   F N     1 
ATOM   13377 C  CA    . CYS   E 4  294 ? 4.096   65.700  93.487  1.00 38.50  ? 294 CYS   F CA    1 
ATOM   13378 C  C     . CYS   E 4  294 ? 4.151   66.119  92.024  1.00 36.96  ? 294 CYS   F C     1 
ATOM   13379 O  O     . CYS   E 4  294 ? 5.119   66.747  91.587  1.00 33.20  ? 294 CYS   F O     1 
ATOM   13380 C  CB    . CYS   E 4  294 ? 4.267   64.187  93.616  1.00 31.73  ? 294 CYS   F CB    1 
ATOM   13381 S  SG    . CYS   E 4  294 ? 4.582   63.631  95.286  1.00 43.88  ? 294 CYS   F SG    1 
ATOM   13382 N  N     . LEU   E 4  295 ? 3.113   65.791  91.254  1.00 36.94  ? 295 LEU   F N     1 
ATOM   13383 C  CA    . LEU   E 4  295 ? 3.187   65.997  89.811  1.00 37.57  ? 295 LEU   F CA    1 
ATOM   13384 C  C     . LEU   E 4  295 ? 3.232   67.478  89.465  1.00 36.88  ? 295 LEU   F C     1 
ATOM   13385 O  O     . LEU   E 4  295 ? 3.932   67.885  88.530  1.00 44.43  ? 295 LEU   F O     1 
ATOM   13386 C  CB    . LEU   E 4  295 ? 2.013   65.311  89.108  1.00 35.58  ? 295 LEU   F CB    1 
ATOM   13387 C  CG    . LEU   E 4  295 ? 2.078   63.781  89.117  1.00 32.52  ? 295 LEU   F CG    1 
ATOM   13388 C  CD1   . LEU   E 4  295 ? 0.776   63.173  88.576  1.00 29.55  ? 295 LEU   F CD1   1 
ATOM   13389 C  CD2   . LEU   E 4  295 ? 3.298   63.300  88.345  1.00 23.95  ? 295 LEU   F CD2   1 
ATOM   13390 N  N     . MET   E 4  296 ? 2.502   68.306  90.202  1.00 32.19  ? 296 MET   F N     1 
ATOM   13391 C  CA    . MET   E 4  296 ? 2.538   69.730  89.902  1.00 34.25  ? 296 MET   F CA    1 
ATOM   13392 C  C     . MET   E 4  296 ? 3.865   70.358  90.317  1.00 37.02  ? 296 MET   F C     1 
ATOM   13393 O  O     . MET   E 4  296 ? 4.367   71.265  89.640  1.00 37.41  ? 296 MET   F O     1 
ATOM   13394 C  CB    . MET   E 4  296 ? 1.384   70.437  90.588  1.00 39.31  ? 296 MET   F CB    1 
ATOM   13395 C  CG    . MET   E 4  296 ? 0.068   70.382  89.869  1.00 38.79  ? 296 MET   F CG    1 
ATOM   13396 S  SD    . MET   E 4  296 ? -1.015  71.133  91.095  1.00 82.77  ? 296 MET   F SD    1 
ATOM   13397 C  CE    . MET   E 4  296 ? 0.092   72.352  91.849  1.00 47.56  ? 296 MET   F CE    1 
ATOM   13398 N  N     . CYS   E 4  297 ? 4.446   69.913  91.430  1.00 30.18  ? 297 CYS   F N     1 
ATOM   13399 C  CA    . CYS   E 4  297 ? 5.757   70.420  91.806  1.00 24.48  ? 297 CYS   F CA    1 
ATOM   13400 C  C     . CYS   E 4  297 ? 6.714   70.484  90.613  1.00 37.65  ? 297 CYS   F C     1 
ATOM   13401 O  O     . CYS   E 4  297 ? 7.396   71.491  90.391  1.00 41.14  ? 297 CYS   F O     1 
ATOM   13402 C  CB    . CYS   E 4  297 ? 6.333   69.545  92.899  1.00 22.71  ? 297 CYS   F CB    1 
ATOM   13403 S  SG    . CYS   E 4  297 ? 8.022   69.998  93.270  1.00 40.00  ? 297 CYS   F SG    1 
ATOM   13404 N  N     . ILE   E 4  298 ? 6.760   69.406  89.823  1.00 31.61  ? 298 ILE   F N     1 
ATOM   13405 C  CA    . ILE   E 4  298 ? 7.665   69.293  88.688  1.00 27.61  ? 298 ILE   F CA    1 
ATOM   13406 C  C     . ILE   E 4  298 ? 7.045   69.775  87.383  1.00 35.54  ? 298 ILE   F C     1 
ATOM   13407 O  O     . ILE   E 4  298 ? 7.710   69.716  86.334  1.00 32.04  ? 298 ILE   F O     1 
ATOM   13408 C  CB    . ILE   E 4  298 ? 8.105   67.827  88.486  1.00 28.10  ? 298 ILE   F CB    1 
ATOM   13409 C  CG1   . ILE   E 4  298 ? 6.888   66.973  88.082  1.00 30.59  ? 298 ILE   F CG1   1 
ATOM   13410 C  CG2   . ILE   E 4  298 ? 8.795   67.308  89.715  1.00 26.00  ? 298 ILE   F CG2   1 
ATOM   13411 C  CD1   . ILE   E 4  298 ? 7.116   65.468  88.015  1.00 28.08  ? 298 ILE   F CD1   1 
ATOM   13412 N  N     . GLU   E 4  299 ? 5.788   70.218  87.397  1.00 29.73  ? 299 GLU   F N     1 
ATOM   13413 C  CA    . GLU   E 4  299 ? 5.139   70.543  86.131  1.00 31.32  ? 299 GLU   F CA    1 
ATOM   13414 C  C     . GLU   E 4  299 ? 5.922   71.558  85.312  1.00 31.92  ? 299 GLU   F C     1 
ATOM   13415 O  O     . GLU   E 4  299 ? 6.053   71.349  84.093  1.00 39.75  ? 299 GLU   F O     1 
ATOM   13416 C  CB    . GLU   E 4  299 ? 3.711   71.037  86.359  1.00 26.19  ? 299 GLU   F CB    1 
ATOM   13417 C  CG    . GLU   E 4  299 ? 3.106   71.552  85.099  1.00 25.97  ? 299 GLU   F CG    1 
ATOM   13418 C  CD    . GLU   E 4  299 ? 1.615   71.799  85.197  1.00 41.41  ? 299 GLU   F CD    1 
ATOM   13419 O  OE1   . GLU   E 4  299 ? 1.028   71.674  86.296  1.00 55.32  ? 299 GLU   F OE1   1 
ATOM   13420 O  OE2   . GLU   E 4  299 ? 1.019   72.124  84.154  1.00 40.92  ? 299 GLU   F OE2   1 
ATOM   13421 N  N     . PRO   E 4  300 ? 6.458   72.642  85.882  1.00 27.09  ? 300 PRO   F N     1 
ATOM   13422 C  CA    . PRO   E 4  300 ? 7.260   73.570  85.077  1.00 31.49  ? 300 PRO   F CA    1 
ATOM   13423 C  C     . PRO   E 4  300 ? 8.487   72.942  84.435  1.00 35.83  ? 300 PRO   F C     1 
ATOM   13424 O  O     . PRO   E 4  300 ? 9.020   73.505  83.464  1.00 36.36  ? 300 PRO   F O     1 
ATOM   13425 C  CB    . PRO   E 4  300 ? 7.660   74.641  86.093  1.00 24.20  ? 300 PRO   F CB    1 
ATOM   13426 C  CG    . PRO   E 4  300 ? 7.591   73.973  87.368  1.00 31.25  ? 300 PRO   F CG    1 
ATOM   13427 C  CD    . PRO   E 4  300 ? 6.401   73.086  87.277  1.00 31.27  ? 300 PRO   F CD    1 
ATOM   13428 N  N     . ALA   E 4  301 ? 8.962   71.803  84.934  1.00 31.19  ? 301 ALA   F N     1 
ATOM   13429 C  CA    . ALA   E 4  301 ? 10.182  71.229  84.401  1.00 22.18  ? 301 ALA   F CA    1 
ATOM   13430 C  C     . ALA   E 4  301 ? 9.955   70.115  83.391  1.00 26.52  ? 301 ALA   F C     1 
ATOM   13431 O  O     . ALA   E 4  301 ? 10.931  69.688  82.770  1.00 33.97  ? 301 ALA   F O     1 
ATOM   13432 C  CB    . ALA   E 4  301 ? 11.052  70.705  85.534  1.00 20.32  ? 301 ALA   F CB    1 
ATOM   13433 N  N     . ILE   E 4  302 ? 8.716   69.637  83.197  1.00 29.05  ? 302 ILE   F N     1 
ATOM   13434 C  CA    . ILE   E 4  302 ? 8.453   68.528  82.275  1.00 29.25  ? 302 ILE   F CA    1 
ATOM   13435 C  C     . ILE   E 4  302 ? 7.203   68.738  81.433  1.00 34.76  ? 302 ILE   F C     1 
ATOM   13436 O  O     . ILE   E 4  302 ? 6.926   67.938  80.530  1.00 40.83  ? 302 ILE   F O     1 
ATOM   13437 C  CB    . ILE   E 4  302 ? 8.310   67.178  83.004  1.00 31.24  ? 302 ILE   F CB    1 
ATOM   13438 C  CG1   . ILE   E 4  302 ? 7.081   67.190  83.908  1.00 23.78  ? 302 ILE   F CG1   1 
ATOM   13439 C  CG2   . ILE   E 4  302 ? 9.580   66.801  83.746  1.00 27.73  ? 302 ILE   F CG2   1 
ATOM   13440 C  CD1   . ILE   E 4  302 ? 6.893   65.926  84.557  1.00 24.41  ? 302 ILE   F CD1   1 
ATOM   13441 N  N     . SER   E 4  303 ? 6.408   69.762  81.742  1.00 31.20  ? 303 SER   F N     1 
ATOM   13442 C  CA    . SER   E 4  303 ? 5.306   70.111  80.852  1.00 28.84  ? 303 SER   F CA    1 
ATOM   13443 C  C     . SER   E 4  303 ? 5.805   70.190  79.410  1.00 33.06  ? 303 SER   F C     1 
ATOM   13444 O  O     . SER   E 4  303 ? 6.867   70.758  79.129  1.00 36.34  ? 303 SER   F O     1 
ATOM   13445 C  CB    . SER   E 4  303 ? 4.676   71.444  81.266  1.00 26.81  ? 303 SER   F CB    1 
ATOM   13446 O  OG    . SER   E 4  303 ? 3.422   71.634  80.620  1.00 22.36  ? 303 SER   F OG    1 
ATOM   13447 N  N     . THR   E 4  304 ? 5.045   69.592  78.494  1.00 36.95  ? 304 THR   F N     1 
ATOM   13448 C  CA    . THR   E 4  304 ? 5.315   69.699  77.064  1.00 32.96  ? 304 THR   F CA    1 
ATOM   13449 C  C     . THR   E 4  304 ? 4.291   70.591  76.363  1.00 35.75  ? 304 THR   F C     1 
ATOM   13450 O  O     . THR   E 4  304 ? 4.056   70.463  75.161  1.00 38.23  ? 304 THR   F O     1 
ATOM   13451 C  CB    . THR   E 4  304 ? 5.354   68.313  76.431  1.00 32.76  ? 304 THR   F CB    1 
ATOM   13452 O  OG1   . THR   E 4  304 ? 4.042   67.739  76.452  1.00 34.66  ? 304 THR   F OG1   1 
ATOM   13453 C  CG2   . THR   E 4  304 ? 6.282   67.437  77.217  1.00 29.29  ? 304 THR   F CG2   1 
ATOM   13454 N  N     . LYS   E 4  305 ? 3.683   71.510  77.114  1.00 38.94  ? 305 LYS   F N     1 
ATOM   13455 C  CA    . LYS   E 4  305 ? 2.639   72.368  76.572  1.00 46.63  ? 305 LYS   F CA    1 
ATOM   13456 C  C     . LYS   E 4  305 ? 3.086   73.070  75.286  1.00 49.38  ? 305 LYS   F C     1 
ATOM   13457 O  O     . LYS   E 4  305 ? 2.366   73.077  74.281  1.00 45.83  ? 305 LYS   F O     1 
ATOM   13458 C  CB    . LYS   E 4  305 ? 2.230   73.383  77.646  1.00 51.23  ? 305 LYS   F CB    1 
ATOM   13459 C  CG    . LYS   E 4  305 ? 0.783   73.879  77.561  1.00 60.92  ? 305 LYS   F CG    1 
ATOM   13460 C  CD    . LYS   E 4  305 ? -0.208  72.716  77.367  1.00 60.87  ? 305 LYS   F CD    1 
ATOM   13461 C  CE    . LYS   E 4  305 ? -1.660  73.173  77.559  1.00 61.22  ? 305 LYS   F CE    1 
ATOM   13462 N  NZ    . LYS   E 4  305 ? -1.994  74.416  76.776  1.00 62.89  ? 305 LYS   F NZ    1 
ATOM   13463 N  N     . HIS   E 4  306 ? 4.263   73.685  75.302  1.00 43.33  ? 306 HIS   F N     1 
ATOM   13464 C  CA    . HIS   E 4  306 ? 4.702   74.531  74.197  1.00 51.82  ? 306 HIS   F CA    1 
ATOM   13465 C  C     . HIS   E 4  306 ? 5.936   73.939  73.520  1.00 48.21  ? 306 HIS   F C     1 
ATOM   13466 O  O     . HIS   E 4  306 ? 6.828   74.652  73.044  1.00 37.93  ? 306 HIS   F O     1 
ATOM   13467 C  CB    . HIS   E 4  306 ? 4.943   75.960  74.686  1.00 59.68  ? 306 HIS   F CB    1 
ATOM   13468 C  CG    . HIS   E 4  306 ? 3.731   76.593  75.306  1.00 67.75  ? 306 HIS   F CG    1 
ATOM   13469 N  ND1   . HIS   E 4  306 ? 3.625   76.837  76.660  1.00 64.83  ? 306 HIS   F ND1   1 
ATOM   13470 C  CD2   . HIS   E 4  306 ? 2.557   76.999  74.758  1.00 68.39  ? 306 HIS   F CD2   1 
ATOM   13471 C  CE1   . HIS   E 4  306 ? 2.445   77.376  76.918  1.00 65.21  ? 306 HIS   F CE1   1 
ATOM   13472 N  NE2   . HIS   E 4  306 ? 1.778   77.487  75.782  1.00 69.17  ? 306 HIS   F NE2   1 
ATOM   13473 N  N     . LEU   E 4  307 ? 5.966   72.614  73.448  1.00 39.12  ? 307 LEU   F N     1 
ATOM   13474 C  CA    . LEU   E 4  307 ? 7.138   71.860  73.048  1.00 32.04  ? 307 LEU   F CA    1 
ATOM   13475 C  C     . LEU   E 4  307 ? 6.865   71.221  71.699  1.00 34.52  ? 307 LEU   F C     1 
ATOM   13476 O  O     . LEU   E 4  307 ? 5.710   70.957  71.361  1.00 39.02  ? 307 LEU   F O     1 
ATOM   13477 C  CB    . LEU   E 4  307 ? 7.459   70.784  74.083  1.00 27.21  ? 307 LEU   F CB    1 
ATOM   13478 C  CG    . LEU   E 4  307 ? 8.885   70.284  74.051  1.00 27.64  ? 307 LEU   F CG    1 
ATOM   13479 C  CD1   . LEU   E 4  307 ? 9.749   71.416  74.501  1.00 23.17  ? 307 LEU   F CD1   1 
ATOM   13480 C  CD2   . LEU   E 4  307 ? 9.039   69.078  74.947  1.00 26.82  ? 307 LEU   F CD2   1 
ATOM   13481 N  N     . HIS   E 4  308 ? 7.935   70.967  70.931  1.00 31.00  ? 308 HIS   F N     1 
ATOM   13482 C  CA    . HIS   E 4  308 ? 7.794   70.419  69.577  1.00 32.51  ? 308 HIS   F CA    1 
ATOM   13483 C  C     . HIS   E 4  308 ? 7.438   68.939  69.557  1.00 31.61  ? 308 HIS   F C     1 
ATOM   13484 O  O     . HIS   E 4  308 ? 7.279   68.390  68.460  1.00 28.16  ? 308 HIS   F O     1 
ATOM   13485 C  CB    . HIS   E 4  308 ? 9.074   70.641  68.768  1.00 26.29  ? 308 HIS   F CB    1 
ATOM   13486 C  CG    . HIS   E 4  308 ? 10.316  70.433  69.554  1.00 23.02  ? 308 HIS   F CG    1 
ATOM   13487 N  ND1   . HIS   E 4  308 ? 10.853  71.411  70.362  1.00 34.79  ? 308 HIS   F ND1   1 
ATOM   13488 C  CD2   . HIS   E 4  308 ? 11.119  69.353  69.683  1.00 30.09  ? 308 HIS   F CD2   1 
ATOM   13489 C  CE1   . HIS   E 4  308 ? 11.935  70.941  70.958  1.00 28.65  ? 308 HIS   F CE1   1 
ATOM   13490 N  NE2   . HIS   E 4  308 ? 12.119  69.695  70.563  1.00 33.22  ? 308 HIS   F NE2   1 
ATOM   13491 N  N     . TYR   E 4  309 ? 7.331   68.295  70.721  1.00 29.11  ? 309 TYR   F N     1 
ATOM   13492 C  CA    . TYR   E 4  309 ? 6.737   66.974  70.853  1.00 26.55  ? 309 TYR   F CA    1 
ATOM   13493 C  C     . TYR   E 4  309 ? 5.894   66.951  72.115  1.00 26.64  ? 309 TYR   F C     1 
ATOM   13494 O  O     . TYR   E 4  309 ? 6.047   67.793  72.996  1.00 31.97  ? 309 TYR   F O     1 
ATOM   13495 C  CB    . TYR   E 4  309 ? 7.783   65.866  70.920  1.00 25.97  ? 309 TYR   F CB    1 
ATOM   13496 C  CG    . TYR   E 4  309 ? 8.629   65.866  72.185  1.00 27.28  ? 309 TYR   F CG    1 
ATOM   13497 C  CD1   . TYR   E 4  309 ? 9.804   66.590  72.245  1.00 24.79  ? 309 TYR   F CD1   1 
ATOM   13498 C  CD2   . TYR   E 4  309 ? 8.272   65.111  73.300  1.00 20.53  ? 309 TYR   F CD2   1 
ATOM   13499 C  CE1   . TYR   E 4  309 ? 10.581  66.591  73.385  1.00 24.64  ? 309 TYR   F CE1   1 
ATOM   13500 C  CE2   . TYR   E 4  309 ? 9.063   65.099  74.432  1.00 22.95  ? 309 TYR   F CE2   1 
ATOM   13501 C  CZ    . TYR   E 4  309 ? 10.213  65.846  74.464  1.00 22.60  ? 309 TYR   F CZ    1 
ATOM   13502 O  OH    . TYR   E 4  309 ? 11.014  65.867  75.578  1.00 31.68  ? 309 TYR   F OH    1 
ATOM   13503 N  N     . GLN   E 4  310 ? 5.007   65.971  72.195  1.00 26.67  ? 310 GLN   F N     1 
ATOM   13504 C  CA    . GLN   E 4  310 ? 4.087   65.815  73.310  1.00 25.66  ? 310 GLN   F CA    1 
ATOM   13505 C  C     . GLN   E 4  310 ? 4.463   64.568  74.097  1.00 30.75  ? 310 GLN   F C     1 
ATOM   13506 O  O     . GLN   E 4  310 ? 4.879   63.562  73.512  1.00 28.89  ? 310 GLN   F O     1 
ATOM   13507 C  CB    . GLN   E 4  310 ? 2.633   65.692  72.821  1.00 32.22  ? 310 GLN   F CB    1 
ATOM   13508 C  CG    . GLN   E 4  310 ? 1.985   66.980  72.277  1.00 29.14  ? 310 GLN   F CG    1 
ATOM   13509 C  CD    . GLN   E 4  310 ? 2.220   68.161  73.188  1.00 40.44  ? 310 GLN   F CD    1 
ATOM   13510 O  OE1   . GLN   E 4  310 ? 2.124   68.057  74.413  1.00 45.44  ? 310 GLN   F OE1   1 
ATOM   13511 N  NE2   . GLN   E 4  310 ? 2.558   69.293  72.595  1.00 50.32  ? 310 GLN   F NE2   1 
ATOM   13512 N  N     . SER   E 4  311 ? 4.301   64.638  75.423  1.00 30.00  ? 311 SER   F N     1 
ATOM   13513 C  CA    . SER   E 4  311 ? 4.452   63.495  76.316  1.00 25.86  ? 311 SER   F CA    1 
ATOM   13514 C  C     . SER   E 4  311 ? 3.129   63.219  77.019  1.00 31.28  ? 311 SER   F C     1 
ATOM   13515 O  O     . SER   E 4  311 ? 2.363   64.149  77.305  1.00 32.35  ? 311 SER   F O     1 
ATOM   13516 C  CB    . SER   E 4  311 ? 5.538   63.733  77.385  1.00 26.86  ? 311 SER   F CB    1 
ATOM   13517 O  OG    . SER   E 4  311 ? 6.864   63.767  76.874  1.00 26.54  ? 311 SER   F OG    1 
ATOM   13518 N  N     . PHE   E 4  312 ? 2.843   61.933  77.236  1.00 30.70  ? 312 PHE   F N     1 
ATOM   13519 C  CA    . PHE   E 4  312 ? 2.004   61.447  78.329  1.00 32.75  ? 312 PHE   F CA    1 
ATOM   13520 C  C     . PHE   E 4  312 ? 2.833   60.391  79.062  1.00 36.80  ? 312 PHE   F C     1 
ATOM   13521 O  O     . PHE   E 4  312 ? 3.938   60.051  78.628  1.00 34.04  ? 312 PHE   F O     1 
ATOM   13522 C  CB    . PHE   E 4  312 ? 0.638   60.899  77.839  1.00 26.83  ? 312 PHE   F CB    1 
ATOM   13523 C  CG    . PHE   E 4  312 ? 0.730   59.635  77.022  1.00 31.91  ? 312 PHE   F CG    1 
ATOM   13524 C  CD1   . PHE   E 4  312 ? 0.685   58.384  77.632  1.00 38.16  ? 312 PHE   F CD1   1 
ATOM   13525 C  CD2   . PHE   E 4  312 ? 0.854   59.691  75.647  1.00 35.22  ? 312 PHE   F CD2   1 
ATOM   13526 C  CE1   . PHE   E 4  312 ? 0.778   57.210  76.884  1.00 31.39  ? 312 PHE   F CE1   1 
ATOM   13527 C  CE2   . PHE   E 4  312 ? 0.948   58.522  74.892  1.00 36.08  ? 312 PHE   F CE2   1 
ATOM   13528 C  CZ    . PHE   E 4  312 ? 0.913   57.281  75.514  1.00 32.92  ? 312 PHE   F CZ    1 
ATOM   13529 N  N     . GLN   E 4  313 ? 2.337   59.887  80.196  1.00 37.81  ? 313 GLN   F N     1 
ATOM   13530 C  CA    . GLN   E 4  313 ? 3.086   58.861  80.921  1.00 34.07  ? 313 GLN   F CA    1 
ATOM   13531 C  C     . GLN   E 4  313 ? 2.263   58.344  82.086  1.00 33.77  ? 313 GLN   F C     1 
ATOM   13532 O  O     . GLN   E 4  313 ? 1.521   59.095  82.721  1.00 34.97  ? 313 GLN   F O     1 
ATOM   13533 C  CB    . GLN   E 4  313 ? 4.424   59.389  81.441  1.00 30.51  ? 313 GLN   F CB    1 
ATOM   13534 C  CG    . GLN   E 4  313 ? 5.277   58.330  82.115  1.00 28.79  ? 313 GLN   F CG    1 
ATOM   13535 C  CD    . GLN   E 4  313 ? 6.535   58.929  82.728  1.00 34.30  ? 313 GLN   F CD    1 
ATOM   13536 O  OE1   . GLN   E 4  313 ? 6.897   60.069  82.412  1.00 31.68  ? 313 GLN   F OE1   1 
ATOM   13537 N  NE2   . GLN   E 4  313 ? 7.202   58.175  83.619  1.00 30.55  ? 313 GLN   F NE2   1 
ATOM   13538 N  N     . LEU   E 4  314 ? 2.438   57.064  82.380  1.00 34.05  ? 314 LEU   F N     1 
ATOM   13539 C  CA    . LEU   E 4  314 ? 1.707   56.384  83.439  1.00 33.09  ? 314 LEU   F CA    1 
ATOM   13540 C  C     . LEU   E 4  314 ? 2.639   56.162  84.620  1.00 31.11  ? 314 LEU   F C     1 
ATOM   13541 O  O     . LEU   E 4  314 ? 3.737   55.615  84.459  1.00 32.77  ? 314 LEU   F O     1 
ATOM   13542 C  CB    . LEU   E 4  314 ? 1.138   55.055  82.936  1.00 34.81  ? 314 LEU   F CB    1 
ATOM   13543 C  CG    . LEU   E 4  314 ? 0.313   54.135  83.830  1.00 30.36  ? 314 LEU   F CG    1 
ATOM   13544 C  CD1   . LEU   E 4  314 ? -1.105  54.630  83.944  1.00 31.86  ? 314 LEU   F CD1   1 
ATOM   13545 C  CD2   . LEU   E 4  314 ? 0.320   52.770  83.210  1.00 32.57  ? 314 LEU   F CD2   1 
ATOM   13546 N  N     . PHE   E 4  315 ? 2.206   56.617  85.789  1.00 32.00  ? 315 PHE   F N     1 
ATOM   13547 C  CA    . PHE   E 4  315 ? 2.953   56.517  87.027  1.00 29.43  ? 315 PHE   F CA    1 
ATOM   13548 C  C     . PHE   E 4  315 ? 2.250   55.549  87.960  1.00 37.12  ? 315 PHE   F C     1 
ATOM   13549 O  O     . PHE   E 4  315 ? 1.014   55.474  87.978  1.00 38.68  ? 315 PHE   F O     1 
ATOM   13550 C  CB    . PHE   E 4  315 ? 3.072   57.882  87.706  1.00 31.70  ? 315 PHE   F CB    1 
ATOM   13551 C  CG    . PHE   E 4  315 ? 3.788   58.908  86.881  1.00 31.87  ? 315 PHE   F CG    1 
ATOM   13552 C  CD1   . PHE   E 4  315 ? 5.177   58.989  86.902  1.00 35.39  ? 315 PHE   F CD1   1 
ATOM   13553 C  CD2   . PHE   E 4  315 ? 3.078   59.797  86.083  1.00 31.74  ? 315 PHE   F CD2   1 
ATOM   13554 C  CE1   . PHE   E 4  315 ? 5.852   59.941  86.133  1.00 31.91  ? 315 PHE   F CE1   1 
ATOM   13555 C  CE2   . PHE   E 4  315 ? 3.734   60.746  85.319  1.00 28.37  ? 315 PHE   F CE2   1 
ATOM   13556 C  CZ    . PHE   E 4  315 ? 5.129   60.815  85.343  1.00 30.03  ? 315 PHE   F CZ    1 
ATOM   13557 N  N     . GLY   E 4  316 ? 3.040   54.812  88.731  1.00 29.43  ? 316 GLY   F N     1 
ATOM   13558 C  CA    . GLY   E 4  316 ? 2.479   53.984  89.772  1.00 30.87  ? 316 GLY   F CA    1 
ATOM   13559 C  C     . GLY   E 4  316 ? 2.919   54.514  91.113  1.00 37.69  ? 316 GLY   F C     1 
ATOM   13560 O  O     . GLY   E 4  316 ? 4.115   54.484  91.413  1.00 46.45  ? 316 GLY   F O     1 
ATOM   13561 N  N     . PHE   E 4  317 ? 1.999   55.031  91.921  1.00 33.02  ? 317 PHE   F N     1 
ATOM   13562 C  CA    . PHE   E 4  317 ? 2.363   55.540  93.236  1.00 39.61  ? 317 PHE   F CA    1 
ATOM   13563 C  C     . PHE   E 4  317 ? 2.160   54.446  94.277  1.00 41.48  ? 317 PHE   F C     1 
ATOM   13564 O  O     . PHE   E 4  317 ? 1.196   53.672  94.203  1.00 38.85  ? 317 PHE   F O     1 
ATOM   13565 C  CB    . PHE   E 4  317 ? 1.549   56.783  93.603  1.00 40.24  ? 317 PHE   F CB    1 
ATOM   13566 C  CG    . PHE   E 4  317 ? 1.951   58.033  92.858  1.00 34.01  ? 317 PHE   F CG    1 
ATOM   13567 C  CD1   . PHE   E 4  317 ? 1.667   58.181  91.507  1.00 29.78  ? 317 PHE   F CD1   1 
ATOM   13568 C  CD2   . PHE   E 4  317 ? 2.576   59.076  93.525  1.00 30.93  ? 317 PHE   F CD2   1 
ATOM   13569 C  CE1   . PHE   E 4  317 ? 2.020   59.337  90.829  1.00 28.80  ? 317 PHE   F CE1   1 
ATOM   13570 C  CE2   . PHE   E 4  317 ? 2.923   60.235  92.854  1.00 30.73  ? 317 PHE   F CE2   1 
ATOM   13571 C  CZ    . PHE   E 4  317 ? 2.648   60.367  91.499  1.00 24.12  ? 317 PHE   F CZ    1 
ATOM   13572 N  N     . ASP   E 4  318 ? 3.090   54.361  95.228  1.00 40.64  ? 318 ASP   F N     1 
ATOM   13573 C  CA    . ASP   E 4  318 ? 3.058   53.324  96.253  1.00 42.94  ? 318 ASP   F CA    1 
ATOM   13574 C  C     . ASP   E 4  318 ? 2.902   53.989  97.616  1.00 42.12  ? 318 ASP   F C     1 
ATOM   13575 O  O     . ASP   E 4  318 ? 3.746   54.796  98.018  1.00 39.55  ? 318 ASP   F O     1 
ATOM   13576 C  CB    . ASP   E 4  318 ? 4.317   52.452  96.192  1.00 48.63  ? 318 ASP   F CB    1 
ATOM   13577 C  CG    . ASP   E 4  318 ? 4.439   51.661  94.877  1.00 49.91  ? 318 ASP   F CG    1 
ATOM   13578 O  OD1   . ASP   E 4  318 ? 3.401   51.253  94.306  1.00 37.76  ? 318 ASP   F OD1   1 
ATOM   13579 O  OD2   . ASP   E 4  318 ? 5.591   51.441  94.419  1.00 58.15  ? 318 ASP   F OD2   1 
ATOM   13580 N  N     . PHE   E 4  319 ? 1.819   53.652  98.319  1.00 43.54  ? 319 PHE   F N     1 
ATOM   13581 C  CA    . PHE   E 4  319 ? 1.457   54.289  99.573  1.00 45.97  ? 319 PHE   F CA    1 
ATOM   13582 C  C     . PHE   E 4  319 ? 1.428   53.286  100.715 1.00 44.89  ? 319 PHE   F C     1 
ATOM   13583 O  O     . PHE   E 4  319 ? 1.247   52.084  100.507 1.00 43.07  ? 319 PHE   F O     1 
ATOM   13584 C  CB    . PHE   E 4  319 ? 0.090   54.965  99.472  1.00 46.62  ? 319 PHE   F CB    1 
ATOM   13585 C  CG    . PHE   E 4  319 ? 0.060   56.094  98.512  1.00 43.09  ? 319 PHE   F CG    1 
ATOM   13586 C  CD1   . PHE   E 4  319 ? 0.520   57.336  98.885  1.00 44.20  ? 319 PHE   F CD1   1 
ATOM   13587 C  CD2   . PHE   E 4  319 ? -0.411  55.911  97.228  1.00 44.06  ? 319 PHE   F CD2   1 
ATOM   13588 C  CE1   . PHE   E 4  319 ? 0.509   58.378  97.993  1.00 45.56  ? 319 PHE   F CE1   1 
ATOM   13589 C  CE2   . PHE   E 4  319 ? -0.434  56.947  96.336  1.00 38.48  ? 319 PHE   F CE2   1 
ATOM   13590 C  CZ    . PHE   E 4  319 ? 0.026   58.179  96.715  1.00 42.85  ? 319 PHE   F CZ    1 
ATOM   13591 N  N     . MET   E 4  320 ? 1.574   53.827  101.932 1.00 51.41  ? 320 MET   F N     1 
ATOM   13592 C  CA    . MET   E 4  320 ? 1.530   53.086  103.195 1.00 48.32  ? 320 MET   F CA    1 
ATOM   13593 C  C     . MET   E 4  320 ? 0.527   53.742  104.139 1.00 47.43  ? 320 MET   F C     1 
ATOM   13594 O  O     . MET   E 4  320 ? 0.758   54.867  104.584 1.00 51.14  ? 320 MET   F O     1 
ATOM   13595 C  CB    . MET   E 4  320 ? 2.913   53.057  103.863 1.00 43.49  ? 320 MET   F CB    1 
ATOM   13596 C  CG    . MET   E 4  320 ? 3.824   51.902  103.443 1.00 55.53  ? 320 MET   F CG    1 
ATOM   13597 S  SD    . MET   E 4  320 ? 3.090   50.302  103.825 1.00 72.75  ? 320 MET   F SD    1 
ATOM   13598 C  CE    . MET   E 4  320 ? 2.471   50.639  105.478 1.00 52.39  ? 320 MET   F CE    1 
ATOM   13599 N  N     . VAL   E 4  321 ? -0.583  53.038  104.461 1.00 46.96  ? 321 VAL   F N     1 
ATOM   13600 C  CA    . VAL   E 4  321 ? -1.497  53.456  105.530 1.00 45.08  ? 321 VAL   F CA    1 
ATOM   13601 C  C     . VAL   E 4  321 ? -0.891  53.073  106.875 1.00 45.37  ? 321 VAL   F C     1 
ATOM   13602 O  O     . VAL   E 4  321 ? -0.219  52.041  106.988 1.00 49.73  ? 321 VAL   F O     1 
ATOM   13603 C  CB    . VAL   E 4  321 ? -2.879  52.794  105.346 1.00 45.80  ? 321 VAL   F CB    1 
ATOM   13604 C  CG1   . VAL   E 4  321 ? -3.969  53.534  106.123 1.00 43.31  ? 321 VAL   F CG1   1 
ATOM   13605 C  CG2   . VAL   E 4  321 ? -3.231  52.667  103.872 1.00 49.01  ? 321 VAL   F CG2   1 
ATOM   13606 N  N     . ASP   E 4  322 ? -1.118  53.877  107.916 1.00 43.65  ? 322 ASP   F N     1 
ATOM   13607 C  CA    . ASP   E 4  322 ? -0.575  53.514  109.231 1.00 47.24  ? 322 ASP   F CA    1 
ATOM   13608 C  C     . ASP   E 4  322 ? -1.672  53.442  110.302 1.00 51.73  ? 322 ASP   F C     1 
ATOM   13609 O  O     . ASP   E 4  322 ? -2.864  53.604  110.024 1.00 52.56  ? 322 ASP   F O     1 
ATOM   13610 C  CB    . ASP   E 4  322 ? 0.565   54.454  109.639 1.00 39.47  ? 322 ASP   F CB    1 
ATOM   13611 C  CG    . ASP   E 4  322 ? 0.096   55.730  110.298 1.00 48.56  ? 322 ASP   F CG    1 
ATOM   13612 O  OD1   . ASP   E 4  322 ? -1.134  56.017  110.297 1.00 42.85  ? 322 ASP   F OD1   1 
ATOM   13613 O  OD2   . ASP   E 4  322 ? 0.994   56.449  110.817 1.00 43.67  ? 322 ASP   F OD2   1 
ATOM   13614 N  N     . GLU   E 4  323 ? -1.242  53.168  111.542 1.00 54.96  ? 323 GLU   F N     1 
ATOM   13615 C  CA    . GLU   E 4  323 ? -2.171  52.853  112.634 1.00 55.65  ? 323 GLU   F CA    1 
ATOM   13616 C  C     . GLU   E 4  323 ? -3.297  53.877  112.741 1.00 50.22  ? 323 GLU   F C     1 
ATOM   13617 O  O     . GLU   E 4  323 ? -4.473  53.513  112.885 1.00 40.22  ? 323 GLU   F O     1 
ATOM   13618 C  CB    . GLU   E 4  323 ? -1.409  52.764  113.965 1.00 56.62  ? 323 GLU   F CB    1 
ATOM   13619 C  CG    . GLU   E 4  323 ? -1.559  51.428  114.731 1.00 53.59  ? 323 GLU   F CG    1 
ATOM   13620 C  CD    . GLU   E 4  323 ? -0.894  51.463  116.107 1.00 63.58  ? 323 GLU   F CD    1 
ATOM   13621 O  OE1   . GLU   E 4  323 ? -0.501  52.567  116.545 1.00 75.90  ? 323 GLU   F OE1   1 
ATOM   13622 O  OE2   . GLU   E 4  323 ? -0.768  50.400  116.760 1.00 59.48  ? 323 GLU   F OE2   1 
ATOM   13623 N  N     . GLU   E 4  324 ? -2.954  55.167  112.679 1.00 46.32  ? 324 GLU   F N     1 
ATOM   13624 C  CA    . GLU   E 4  324 ? -3.926  56.242  112.815 1.00 46.73  ? 324 GLU   F CA    1 
ATOM   13625 C  C     . GLU   E 4  324 ? -4.553  56.649  111.480 1.00 46.01  ? 324 GLU   F C     1 
ATOM   13626 O  O     . GLU   E 4  324 ? -5.162  57.724  111.389 1.00 46.05  ? 324 GLU   F O     1 
ATOM   13627 C  CB    . GLU   E 4  324 ? -3.279  57.438  113.504 1.00 34.32  ? 324 GLU   F CB    1 
ATOM   13628 C  CG    . GLU   E 4  324 ? -2.953  57.169  114.967 1.00 40.29  ? 324 GLU   F CG    1 
ATOM   13629 C  CD    . GLU   E 4  324 ? -1.951  58.171  115.555 1.00 68.73  ? 324 GLU   F CD    1 
ATOM   13630 O  OE1   . GLU   E 4  324 ? -0.754  58.123  115.166 1.00 48.68  ? 324 GLU   F OE1   1 
ATOM   13631 O  OE2   . GLU   E 4  324 ? -2.361  59.005  116.406 1.00 69.11  ? 324 GLU   F OE2   1 
ATOM   13632 N  N     . LEU   E 4  325 ? -4.454  55.793  110.461 1.00 48.00  ? 325 LEU   F N     1 
ATOM   13633 C  CA    . LEU   E 4  325 ? -5.079  56.026  109.163 1.00 41.29  ? 325 LEU   F CA    1 
ATOM   13634 C  C     . LEU   E 4  325 ? -4.533  57.294  108.506 1.00 42.11  ? 325 LEU   F C     1 
ATOM   13635 O  O     . LEU   E 4  325 ? -5.286  58.132  108.004 1.00 46.49  ? 325 LEU   F O     1 
ATOM   13636 C  CB    . LEU   E 4  325 ? -6.598  56.084  109.303 1.00 39.53  ? 325 LEU   F CB    1 
ATOM   13637 C  CG    . LEU   E 4  325 ? -7.306  54.727  109.330 1.00 45.59  ? 325 LEU   F CG    1 
ATOM   13638 C  CD1   . LEU   E 4  325 ? -8.755  54.904  109.672 1.00 44.25  ? 325 LEU   F CD1   1 
ATOM   13639 C  CD2   . LEU   E 4  325 ? -7.190  53.979  107.997 1.00 46.63  ? 325 LEU   F CD2   1 
ATOM   13640 N  N     . LYS   E 4  326 ? -3.204  57.430  108.521 1.00 33.12  ? 326 LYS   F N     1 
ATOM   13641 C  CA    . LYS   E 4  326 ? -2.499  58.523  107.861 1.00 35.32  ? 326 LYS   F CA    1 
ATOM   13642 C  C     . LYS   E 4  326 ? -1.651  57.972  106.715 1.00 45.41  ? 326 LYS   F C     1 
ATOM   13643 O  O     . LYS   E 4  326 ? -0.768  57.141  106.945 1.00 47.01  ? 326 LYS   F O     1 
ATOM   13644 C  CB    . LYS   E 4  326 ? -1.617  59.268  108.850 1.00 33.24  ? 326 LYS   F CB    1 
ATOM   13645 C  CG    . LYS   E 4  326 ? -0.399  59.889  108.193 1.00 42.83  ? 326 LYS   F CG    1 
ATOM   13646 C  CD    . LYS   E 4  326 ? 0.195   61.008  109.041 1.00 42.82  ? 326 LYS   F CD    1 
ATOM   13647 C  CE    . LYS   E 4  326 ? 1.419   61.607  108.379 1.00 35.27  ? 326 LYS   F CE    1 
ATOM   13648 N  NZ    . LYS   E 4  326 ? 1.845   62.846  109.081 1.00 52.12  ? 326 LYS   F NZ    1 
ATOM   13649 N  N     . VAL   E 4  327 ? -1.889  58.454  105.490 1.00 39.76  ? 327 VAL   F N     1 
ATOM   13650 C  CA    . VAL   E 4  327 ? -1.235  57.881  104.317 1.00 32.90  ? 327 VAL   F CA    1 
ATOM   13651 C  C     . VAL   E 4  327 ? 0.215   58.363  104.203 1.00 45.42  ? 327 VAL   F C     1 
ATOM   13652 O  O     . VAL   E 4  327 ? 0.542   59.517  104.509 1.00 46.16  ? 327 VAL   F O     1 
ATOM   13653 C  CB    . VAL   E 4  327 ? -2.042  58.202  103.054 1.00 32.68  ? 327 VAL   F CB    1 
ATOM   13654 C  CG1   . VAL   E 4  327 ? -1.377  57.598  101.839 1.00 44.13  ? 327 VAL   F CG1   1 
ATOM   13655 C  CG2   . VAL   E 4  327 ? -3.436  57.648  103.183 1.00 46.74  ? 327 VAL   F CG2   1 
ATOM   13656 N  N     . TRP   E 4  328 ? 1.101   57.460  103.764 1.00 48.89  ? 328 TRP   F N     1 
ATOM   13657 C  CA    . TRP   E 4  328 ? 2.508   57.755  103.518 1.00 40.67  ? 328 TRP   F CA    1 
ATOM   13658 C  C     . TRP   E 4  328 ? 2.890   57.288  102.119 1.00 52.16  ? 328 TRP   F C     1 
ATOM   13659 O  O     . TRP   E 4  328 ? 2.374   56.279  101.624 1.00 52.48  ? 328 TRP   F O     1 
ATOM   13660 C  CB    . TRP   E 4  328 ? 3.422   57.066  104.530 1.00 48.77  ? 328 TRP   F CB    1 
ATOM   13661 C  CG    . TRP   E 4  328 ? 3.136   57.438  105.946 1.00 49.23  ? 328 TRP   F CG    1 
ATOM   13662 C  CD1   . TRP   E 4  328 ? 2.157   56.921  106.762 1.00 43.08  ? 328 TRP   F CD1   1 
ATOM   13663 C  CD2   . TRP   E 4  328 ? 3.841   58.404  106.727 1.00 44.33  ? 328 TRP   F CD2   1 
ATOM   13664 N  NE1   . TRP   E 4  328 ? 2.209   57.522  107.998 1.00 44.38  ? 328 TRP   F NE1   1 
ATOM   13665 C  CE2   . TRP   E 4  328 ? 3.231   58.436  108.001 1.00 43.02  ? 328 TRP   F CE2   1 
ATOM   13666 C  CE3   . TRP   E 4  328 ? 4.920   59.254  106.469 1.00 39.04  ? 328 TRP   F CE3   1 
ATOM   13667 C  CZ2   . TRP   E 4  328 ? 3.664   59.283  109.005 1.00 38.22  ? 328 TRP   F CZ2   1 
ATOM   13668 C  CZ3   . TRP   E 4  328 ? 5.347   60.089  107.463 1.00 42.56  ? 328 TRP   F CZ3   1 
ATOM   13669 C  CH2   . TRP   E 4  328 ? 4.724   60.097  108.723 1.00 43.21  ? 328 TRP   F CH2   1 
ATOM   13670 N  N     . LEU   E 4  329 ? 3.798   58.033  101.484 1.00 51.25  ? 329 LEU   F N     1 
ATOM   13671 C  CA    . LEU   E 4  329 ? 4.321   57.706  100.164 1.00 45.74  ? 329 LEU   F CA    1 
ATOM   13672 C  C     . LEU   E 4  329 ? 5.719   57.102  100.294 1.00 51.42  ? 329 LEU   F C     1 
ATOM   13673 O  O     . LEU   E 4  329 ? 6.461   57.431  101.225 1.00 51.08  ? 329 LEU   F O     1 
ATOM   13674 C  CB    . LEU   E 4  329 ? 4.368   58.959  99.288  1.00 41.88  ? 329 LEU   F CB    1 
ATOM   13675 C  CG    . LEU   E 4  329 ? 4.924   58.814  97.873  1.00 39.59  ? 329 LEU   F CG    1 
ATOM   13676 C  CD1   . LEU   E 4  329 ? 3.878   58.281  96.917  1.00 33.08  ? 329 LEU   F CD1   1 
ATOM   13677 C  CD2   . LEU   E 4  329 ? 5.503   60.140  97.405  1.00 31.42  ? 329 LEU   F CD2   1 
ATOM   13678 N  N     . ILE   E 4  330 ? 6.079   56.213  99.353  1.00 53.31  ? 330 ILE   F N     1 
ATOM   13679 C  CA    . ILE   E 4  330 ? 7.429   55.635  99.328  1.00 48.88  ? 330 ILE   F CA    1 
ATOM   13680 C  C     . ILE   E 4  330 ? 8.039   55.655  97.930  1.00 46.81  ? 330 ILE   F C     1 
ATOM   13681 O  O     . ILE   E 4  330 ? 8.988   56.400  97.673  1.00 54.76  ? 330 ILE   F O     1 
ATOM   13682 C  CB    . ILE   E 4  330 ? 7.465   54.189  99.857  1.00 57.63  ? 330 ILE   F CB    1 
ATOM   13683 C  CG1   . ILE   E 4  330 ? 6.417   53.956  100.948 1.00 45.45  ? 330 ILE   F CG1   1 
ATOM   13684 C  CG2   . ILE   E 4  330 ? 8.898   53.837  100.310 1.00 52.29  ? 330 ILE   F CG2   1 
ATOM   13685 C  CD1   . ILE   E 4  330 ? 5.434   52.867  100.564 1.00 47.07  ? 330 ILE   F CD1   1 
ATOM   13686 N  N     . GLU   E 4  331 ? 7.563   54.769  97.050  1.00 52.74  ? 331 GLU   F N     1 
ATOM   13687 C  CA    . GLU   E 4  331 ? 8.042   54.678  95.670  1.00 57.85  ? 331 GLU   F CA    1 
ATOM   13688 C  C     . GLU   E 4  331 ? 7.072   55.453  94.784  1.00 51.06  ? 331 GLU   F C     1 
ATOM   13689 O  O     . GLU   E 4  331 ? 5.852   55.317  94.927  1.00 49.33  ? 331 GLU   F O     1 
ATOM   13690 C  CB    . GLU   E 4  331 ? 8.135   53.208  95.178  1.00 55.60  ? 331 GLU   F CB    1 
ATOM   13691 C  CG    . GLU   E 4  331 ? 9.501   52.421  95.282  1.00 58.02  ? 331 GLU   F CG    1 
ATOM   13692 C  CD    . GLU   E 4  331 ? 9.472   50.971  94.634  1.00 90.04  ? 331 GLU   F CD    1 
ATOM   13693 O  OE1   . GLU   E 4  331 ? 9.305   50.857  93.394  1.00 75.46  ? 331 GLU   F OE1   1 
ATOM   13694 O  OE2   . GLU   E 4  331 ? 9.631   49.943  95.357  1.00 87.74  ? 331 GLU   F OE2   1 
ATOM   13695 N  N     . VAL   E 4  332 ? 7.604   56.276  93.887  1.00 46.79  ? 332 VAL   F N     1 
ATOM   13696 C  CA    . VAL   E 4  332 ? 6.903   56.591  92.649  1.00 43.66  ? 332 VAL   F CA    1 
ATOM   13697 C  C     . VAL   E 4  332 ? 7.593   55.792  91.561  1.00 43.08  ? 332 VAL   F C     1 
ATOM   13698 O  O     . VAL   E 4  332 ? 8.828   55.826  91.446  1.00 39.49  ? 332 VAL   F O     1 
ATOM   13699 C  CB    . VAL   E 4  332 ? 6.899   58.094  92.319  1.00 38.24  ? 332 VAL   F CB    1 
ATOM   13700 C  CG1   . VAL   E 4  332 ? 5.763   58.385  91.361  1.00 34.44  ? 332 VAL   F CG1   1 
ATOM   13701 C  CG2   . VAL   E 4  332 ? 6.756   58.936  93.577  1.00 45.20  ? 332 VAL   F CG2   1 
ATOM   13702 N  N     . ASN   E 4  333 ? 6.796   55.052  90.791  1.00 35.61  ? 333 ASN   F N     1 
ATOM   13703 C  CA    . ASN   E 4  333 ? 7.260   54.053  89.837  1.00 36.17  ? 333 ASN   F CA    1 
ATOM   13704 C  C     . ASN   E 4  333 ? 7.042   54.604  88.436  1.00 37.81  ? 333 ASN   F C     1 
ATOM   13705 O  O     . ASN   E 4  333 ? 5.901   54.893  88.064  1.00 43.08  ? 333 ASN   F O     1 
ATOM   13706 C  CB    . ASN   E 4  333 ? 6.494   52.734  90.029  1.00 43.77  ? 333 ASN   F CB    1 
ATOM   13707 C  CG    . ASN   E 4  333 ? 7.409   51.504  90.127  1.00 56.50  ? 333 ASN   F CG    1 
ATOM   13708 O  OD1   . ASN   E 4  333 ? 8.359   51.472  90.921  1.00 67.23  ? 333 ASN   F OD1   1 
ATOM   13709 N  ND2   . ASN   E 4  333 ? 7.110   50.478  89.325  1.00 60.74  ? 333 ASN   F ND2   1 
ATOM   13710 N  N     . GLY   E 4  334 ? 8.126   54.728  87.658  1.00 36.25  ? 334 GLY   F N     1 
ATOM   13711 C  CA    . GLY   E 4  334 ? 8.031   55.359  86.349  1.00 35.20  ? 334 GLY   F CA    1 
ATOM   13712 C  C     . GLY   E 4  334 ? 7.498   54.473  85.241  1.00 43.99  ? 334 GLY   F C     1 
ATOM   13713 O  O     . GLY   E 4  334 ? 6.913   54.972  84.272  1.00 43.86  ? 334 GLY   F O     1 
ATOM   13714 N  N     . ALA   E 4  335 ? 7.682   53.164  85.356  1.00 47.47  ? 335 ALA   F N     1 
ATOM   13715 C  CA    . ALA   E 4  335 ? 7.180   52.207  84.374  1.00 46.38  ? 335 ALA   F CA    1 
ATOM   13716 C  C     . ALA   E 4  335 ? 6.383   51.127  85.091  1.00 42.34  ? 335 ALA   F C     1 
ATOM   13717 O  O     . ALA   E 4  335 ? 6.779   49.959  85.104  1.00 48.18  ? 335 ALA   F O     1 
ATOM   13718 C  CB    . ALA   E 4  335 ? 8.330   51.605  83.565  1.00 47.75  ? 335 ALA   F CB    1 
ATOM   13719 N  N     . PRO   E 4  336 ? 5.235   51.480  85.676  1.00 43.78  ? 336 PRO   F N     1 
ATOM   13720 C  CA    . PRO   E 4  336 ? 4.495   50.514  86.505  1.00 40.83  ? 336 PRO   F CA    1 
ATOM   13721 C  C     . PRO   E 4  336 ? 3.833   49.425  85.680  1.00 42.01  ? 336 PRO   F C     1 
ATOM   13722 O  O     . PRO   E 4  336 ? 3.317   49.682  84.594  1.00 51.59  ? 336 PRO   F O     1 
ATOM   13723 C  CB    . PRO   E 4  336 ? 3.435   51.384  87.179  1.00 40.82  ? 336 PRO   F CB    1 
ATOM   13724 C  CG    . PRO   E 4  336 ? 3.128   52.409  86.128  1.00 44.13  ? 336 PRO   F CG    1 
ATOM   13725 C  CD    . PRO   E 4  336 ? 4.485   52.738  85.506  1.00 41.40  ? 336 PRO   F CD    1 
ATOM   13726 N  N     . ALA   E 4  337 ? 3.834   48.201  86.211  1.00 51.62  ? 337 ALA   F N     1 
ATOM   13727 C  CA    . ALA   E 4  337 ? 2.972   47.153  85.669  1.00 58.55  ? 337 ALA   F CA    1 
ATOM   13728 C  C     . ALA   E 4  337 ? 1.587   47.232  86.321  1.00 57.13  ? 337 ALA   F C     1 
ATOM   13729 O  O     . ALA   E 4  337 ? 1.361   47.991  87.271  1.00 58.11  ? 337 ALA   F O     1 
ATOM   13730 C  CB    . ALA   E 4  337 ? 3.595   45.770  85.878  1.00 40.40  ? 337 ALA   F CB    1 
ATOM   13731 N  N     . CYS   E 4  338 ? 0.641   46.447  85.815  1.00 41.07  ? 338 CYS   F N     1 
ATOM   13732 C  CA    . CYS   E 4  338 ? -0.723  46.534  86.318  1.00 42.61  ? 338 CYS   F CA    1 
ATOM   13733 C  C     . CYS   E 4  338 ? -1.210  45.196  86.862  1.00 52.68  ? 338 CYS   F C     1 
ATOM   13734 O  O     . CYS   E 4  338 ? -0.872  44.142  86.327  1.00 66.52  ? 338 CYS   F O     1 
ATOM   13735 C  CB    . CYS   E 4  338 ? -1.669  47.012  85.239  1.00 40.09  ? 338 CYS   F CB    1 
ATOM   13736 S  SG    . CYS   E 4  338 ? -3.296  47.292  85.908  1.00 57.03  ? 338 CYS   F SG    1 
ATOM   13737 N  N     . ALA   E 4  339 ? -2.011  45.241  87.927  1.00 47.25  ? 339 ALA   F N     1 
ATOM   13738 C  CA    . ALA   E 4  339 ? -2.690  44.048  88.423  1.00 44.86  ? 339 ALA   F CA    1 
ATOM   13739 C  C     . ALA   E 4  339 ? -3.397  43.321  87.287  1.00 56.37  ? 339 ALA   F C     1 
ATOM   13740 O  O     . ALA   E 4  339 ? -4.088  43.943  86.474  1.00 52.33  ? 339 ALA   F O     1 
ATOM   13741 C  CB    . ALA   E 4  339 ? -3.698  44.440  89.505  1.00 47.24  ? 339 ALA   F CB    1 
ATOM   13742 N  N     . GLN   E 4  340 ? -3.236  41.995  87.238  1.00 53.01  ? 340 GLN   F N     1 
ATOM   13743 C  CA    . GLN   E 4  340 ? -3.736  41.261  86.081  1.00 48.17  ? 340 GLN   F CA    1 
ATOM   13744 C  C     . GLN   E 4  340 ? -5.217  41.532  85.844  1.00 49.57  ? 340 GLN   F C     1 
ATOM   13745 O  O     . GLN   E 4  340 ? -5.644  41.700  84.694  1.00 42.99  ? 340 GLN   F O     1 
ATOM   13746 C  CB    . GLN   E 4  340 ? -3.468  39.770  86.242  1.00 51.52  ? 340 GLN   F CB    1 
ATOM   13747 C  CG    . GLN   E 4  340 ? -3.994  38.920  85.088  1.00 51.33  ? 340 GLN   F CG    1 
ATOM   13748 C  CD    . GLN   E 4  340 ? -5.480  38.608  85.249  1.00 71.19  ? 340 GLN   F CD    1 
ATOM   13749 O  OE1   . GLN   E 4  340 ? -5.997  38.580  86.375  1.00 67.79  ? 340 GLN   F OE1   1 
ATOM   13750 N  NE2   . GLN   E 4  340 ? -6.180  38.411  84.129  1.00 64.83  ? 340 GLN   F NE2   1 
ATOM   13751 N  N     . LYS   E 4  341 ? -6.012  41.606  86.917  1.00 49.03  ? 341 LYS   F N     1 
ATOM   13752 C  CA    . LYS   E 4  341 ? -7.447  41.864  86.773  1.00 56.22  ? 341 LYS   F CA    1 
ATOM   13753 C  C     . LYS   E 4  341 ? -7.725  43.100  85.910  1.00 64.42  ? 341 LYS   F C     1 
ATOM   13754 O  O     . LYS   E 4  341 ? -8.612  43.081  85.041  1.00 54.36  ? 341 LYS   F O     1 
ATOM   13755 C  CB    . LYS   E 4  341 ? -8.096  42.024  88.160  1.00 51.21  ? 341 LYS   F CB    1 
ATOM   13756 C  CG    . LYS   E 4  341 ? -9.635  42.156  88.137  1.00 54.76  ? 341 LYS   F CG    1 
ATOM   13757 C  CD    . LYS   E 4  341 ? -10.225 42.815  89.412  1.00 58.70  ? 341 LYS   F CD    1 
ATOM   13758 C  CE    . LYS   E 4  341 ? -11.765 43.000  89.344  1.00 52.04  ? 341 LYS   F CE    1 
ATOM   13759 N  NZ    . LYS   E 4  341 ? -12.311 44.021  90.312  1.00 43.55  ? 341 LYS   F NZ    1 
ATOM   13760 N  N     . LEU   E 4  342 ? -6.960  44.177  86.122  1.00 62.53  ? 342 LEU   F N     1 
ATOM   13761 C  CA    . LEU   E 4  342 ? -7.317  45.509  85.648  1.00 57.91  ? 342 LEU   F CA    1 
ATOM   13762 C  C     . LEU   E 4  342 ? -6.670  45.881  84.313  1.00 58.83  ? 342 LEU   F C     1 
ATOM   13763 O  O     . LEU   E 4  342 ? -6.961  46.963  83.794  1.00 55.13  ? 342 LEU   F O     1 
ATOM   13764 C  CB    . LEU   E 4  342 ? -6.952  46.554  86.720  1.00 52.76  ? 342 LEU   F CB    1 
ATOM   13765 C  CG    . LEU   E 4  342 ? -7.335  46.264  88.189  1.00 49.71  ? 342 LEU   F CG    1 
ATOM   13766 C  CD1   . LEU   E 4  342 ? -6.536  47.096  89.173  1.00 42.94  ? 342 LEU   F CD1   1 
ATOM   13767 C  CD2   . LEU   E 4  342 ? -8.803  46.479  88.447  1.00 54.07  ? 342 LEU   F CD2   1 
ATOM   13768 N  N     . TYR   E 4  343 ? -5.818  45.023  83.738  1.00 53.30  ? 343 TYR   F N     1 
ATOM   13769 C  CA    . TYR   E 4  343 ? -5.172  45.358  82.467  1.00 48.85  ? 343 TYR   F CA    1 
ATOM   13770 C  C     . TYR   E 4  343 ? -6.194  45.762  81.407  1.00 53.25  ? 343 TYR   F C     1 
ATOM   13771 O  O     . TYR   E 4  343 ? -6.026  46.772  80.717  1.00 56.81  ? 343 TYR   F O     1 
ATOM   13772 C  CB    . TYR   E 4  343 ? -4.333  44.181  81.958  1.00 46.74  ? 343 TYR   F CB    1 
ATOM   13773 C  CG    . TYR   E 4  343 ? -2.878  44.188  82.388  1.00 55.33  ? 343 TYR   F CG    1 
ATOM   13774 C  CD1   . TYR   E 4  343 ? -1.946  45.030  81.782  1.00 53.33  ? 343 TYR   F CD1   1 
ATOM   13775 C  CD2   . TYR   E 4  343 ? -2.427  43.333  83.386  1.00 58.58  ? 343 TYR   F CD2   1 
ATOM   13776 C  CE1   . TYR   E 4  343 ? -0.603  45.030  82.177  1.00 45.86  ? 343 TYR   F CE1   1 
ATOM   13777 C  CE2   . TYR   E 4  343 ? -1.093  43.320  83.780  1.00 53.71  ? 343 TYR   F CE2   1 
ATOM   13778 C  CZ    . TYR   E 4  343 ? -0.183  44.174  83.183  1.00 54.95  ? 343 TYR   F CZ    1 
ATOM   13779 O  OH    . TYR   E 4  343 ? 1.143   44.154  83.593  1.00 55.83  ? 343 TYR   F OH    1 
ATOM   13780 N  N     . ALA   E 4  344 ? -7.260  44.976  81.250  1.00 58.91  ? 344 ALA   F N     1 
ATOM   13781 C  CA    . ALA   E 4  344 ? -8.227  45.261  80.191  1.00 55.79  ? 344 ALA   F CA    1 
ATOM   13782 C  C     . ALA   E 4  344 ? -8.644  46.721  80.206  1.00 56.18  ? 344 ALA   F C     1 
ATOM   13783 O  O     . ALA   E 4  344 ? -8.690  47.376  79.159  1.00 57.14  ? 344 ALA   F O     1 
ATOM   13784 C  CB    . ALA   E 4  344 ? -9.463  44.366  80.335  1.00 43.11  ? 344 ALA   F CB    1 
ATOM   13785 N  N     . GLU   E 4  345 ? -8.926  47.253  81.397  1.00 59.61  ? 345 GLU   F N     1 
ATOM   13786 C  CA    . GLU   E 4  345 ? -9.612  48.535  81.516  1.00 52.32  ? 345 GLU   F CA    1 
ATOM   13787 C  C     . GLU   E 4  345 ? -8.630  49.699  81.475  1.00 54.01  ? 345 GLU   F C     1 
ATOM   13788 O  O     . GLU   E 4  345 ? -8.741  50.583  80.619  1.00 57.51  ? 345 GLU   F O     1 
ATOM   13789 C  CB    . GLU   E 4  345 ? -10.432 48.565  82.810  1.00 53.77  ? 345 GLU   F CB    1 
ATOM   13790 C  CG    . GLU   E 4  345 ? -11.367 49.739  82.902  1.00 48.68  ? 345 GLU   F CG    1 
ATOM   13791 C  CD    . GLU   E 4  345 ? -12.180 49.738  84.162  1.00 42.34  ? 345 GLU   F CD    1 
ATOM   13792 O  OE1   . GLU   E 4  345 ? -11.597 49.870  85.249  1.00 41.72  ? 345 GLU   F OE1   1 
ATOM   13793 O  OE2   . GLU   E 4  345 ? -13.410 49.624  84.061  1.00 51.15  ? 345 GLU   F OE2   1 
ATOM   13794 N  N     . LEU   E 4  346 ? -7.658  49.712  82.398  1.00 51.55  ? 346 LEU   F N     1 
ATOM   13795 C  CA    . LEU   E 4  346 ? -6.634  50.754  82.400  1.00 47.16  ? 346 LEU   F CA    1 
ATOM   13796 C  C     . LEU   E 4  346 ? -6.000  50.910  81.024  1.00 52.84  ? 346 LEU   F C     1 
ATOM   13797 O  O     . LEU   E 4  346 ? -5.860  52.027  80.514  1.00 51.37  ? 346 LEU   F O     1 
ATOM   13798 C  CB    . LEU   E 4  346 ? -5.558  50.447  83.443  1.00 41.68  ? 346 LEU   F CB    1 
ATOM   13799 C  CG    . LEU   E 4  346 ? -4.409  51.462  83.524  1.00 35.28  ? 346 LEU   F CG    1 
ATOM   13800 C  CD1   . LEU   E 4  346 ? -4.871  52.814  84.087  1.00 36.20  ? 346 LEU   F CD1   1 
ATOM   13801 C  CD2   . LEU   E 4  346 ? -3.250  50.926  84.343  1.00 39.42  ? 346 LEU   F CD2   1 
ATOM   13802 N  N     . CYS   E 4  347 ? -5.603  49.795  80.403  1.00 49.05  ? 347 CYS   F N     1 
ATOM   13803 C  CA    . CYS   E 4  347 ? -4.926  49.899  79.117  1.00 42.81  ? 347 CYS   F CA    1 
ATOM   13804 C  C     . CYS   E 4  347 ? -5.845  50.492  78.060  1.00 52.72  ? 347 CYS   F C     1 
ATOM   13805 O  O     . CYS   E 4  347 ? -5.399  51.288  77.224  1.00 57.74  ? 347 CYS   F O     1 
ATOM   13806 C  CB    . CYS   E 4  347 ? -4.387  48.538  78.686  1.00 50.09  ? 347 CYS   F CB    1 
ATOM   13807 S  SG    . CYS   E 4  347 ? -2.894  48.027  79.637  1.00 44.43  ? 347 CYS   F SG    1 
ATOM   13808 N  N     . GLN   E 4  348 ? -7.136  50.152  78.089  1.00 46.55  ? 348 GLN   F N     1 
ATOM   13809 C  CA    . GLN   E 4  348 ? -8.044  50.820  77.164  1.00 48.46  ? 348 GLN   F CA    1 
ATOM   13810 C  C     . GLN   E 4  348 ? -8.163  52.296  77.506  1.00 49.13  ? 348 GLN   F C     1 
ATOM   13811 O  O     . GLN   E 4  348 ? -8.218  53.148  76.610  1.00 44.18  ? 348 GLN   F O     1 
ATOM   13812 C  CB    . GLN   E 4  348 ? -9.421  50.160  77.166  1.00 47.00  ? 348 GLN   F CB    1 
ATOM   13813 C  CG    . GLN   E 4  348 ? -10.415 50.848  76.212  1.00 46.29  ? 348 GLN   F CG    1 
ATOM   13814 C  CD    . GLN   E 4  348 ? -10.102 50.620  74.740  1.00 48.44  ? 348 GLN   F CD    1 
ATOM   13815 O  OE1   . GLN   E 4  348 ? -9.221  49.834  74.398  1.00 55.76  ? 348 GLN   F OE1   1 
ATOM   13816 N  NE2   . GLN   E 4  348 ? -10.833 51.299  73.862  1.00 45.83  ? 348 GLN   F NE2   1 
ATOM   13817 N  N     . GLY   E 4  349 ? -8.181  52.616  78.801  1.00 49.81  ? 349 GLY   F N     1 
ATOM   13818 C  CA    . GLY   E 4  349 ? -8.286  54.007  79.209  1.00 40.99  ? 349 GLY   F CA    1 
ATOM   13819 C  C     . GLY   E 4  349 ? -7.091  54.830  78.773  1.00 45.93  ? 349 GLY   F C     1 
ATOM   13820 O  O     . GLY   E 4  349 ? -7.238  55.989  78.379  1.00 46.61  ? 349 GLY   F O     1 
ATOM   13821 N  N     . ILE   E 4  350 ? -5.886  54.246  78.847  1.00 48.18  ? 350 ILE   F N     1 
ATOM   13822 C  CA    . ILE   E 4  350 ? -4.698  54.916  78.316  1.00 41.83  ? 350 ILE   F CA    1 
ATOM   13823 C  C     . ILE   E 4  350 ? -4.926  55.291  76.857  1.00 41.67  ? 350 ILE   F C     1 
ATOM   13824 O  O     . ILE   E 4  350 ? -4.804  56.461  76.473  1.00 37.61  ? 350 ILE   F O     1 
ATOM   13825 C  CB    . ILE   E 4  350 ? -3.443  54.032  78.483  1.00 46.54  ? 350 ILE   F CB    1 
ATOM   13826 C  CG1   . ILE   E 4  350 ? -3.144  53.753  79.967  1.00 44.12  ? 350 ILE   F CG1   1 
ATOM   13827 C  CG2   . ILE   E 4  350 ? -2.243  54.674  77.785  1.00 38.86  ? 350 ILE   F CG2   1 
ATOM   13828 C  CD1   . ILE   E 4  350 ? -2.013  52.749  80.215  1.00 37.19  ? 350 ILE   F CD1   1 
ATOM   13829 N  N     . VAL   E 4  351 ? -5.287  54.299  76.029  1.00 42.14  ? 351 VAL   F N     1 
ATOM   13830 C  CA    . VAL   E 4  351 ? -5.604  54.560  74.626  1.00 37.37  ? 351 VAL   F CA    1 
ATOM   13831 C  C     . VAL   E 4  351 ? -6.648  55.658  74.506  1.00 46.14  ? 351 VAL   F C     1 
ATOM   13832 O  O     . VAL   E 4  351 ? -6.570  56.526  73.624  1.00 40.46  ? 351 VAL   F O     1 
ATOM   13833 C  CB    . VAL   E 4  351 ? -6.085  53.274  73.933  1.00 45.95  ? 351 VAL   F CB    1 
ATOM   13834 C  CG1   . VAL   E 4  351 ? -6.819  53.632  72.658  1.00 37.34  ? 351 VAL   F CG1   1 
ATOM   13835 C  CG2   . VAL   E 4  351 ? -4.910  52.345  73.637  1.00 55.43  ? 351 VAL   F CG2   1 
ATOM   13836 N  N     . ASP   E 4  352 ? -7.645  55.637  75.393  1.00 47.58  ? 352 ASP   F N     1 
ATOM   13837 C  CA    . ASP   E 4  352 ? -8.775  56.551  75.275  1.00 43.34  ? 352 ASP   F CA    1 
ATOM   13838 C  C     . ASP   E 4  352 ? -8.386  57.978  75.630  1.00 42.39  ? 352 ASP   F C     1 
ATOM   13839 O  O     . ASP   E 4  352 ? -8.508  58.892  74.804  1.00 54.38  ? 352 ASP   F O     1 
ATOM   13840 C  CB    . ASP   E 4  352 ? -9.918  56.068  76.157  1.00 52.40  ? 352 ASP   F CB    1 
ATOM   13841 C  CG    . ASP   E 4  352 ? -10.673 54.912  75.537  1.00 59.94  ? 352 ASP   F CG    1 
ATOM   13842 O  OD1   . ASP   E 4  352 ? -11.389 55.148  74.546  1.00 52.85  ? 352 ASP   F OD1   1 
ATOM   13843 O  OD2   . ASP   E 4  352 ? -10.535 53.765  76.018  1.00 68.00  ? 352 ASP   F OD2   1 
ATOM   13844 N  N     . VAL   E 4  353 ? -7.901  58.194  76.851  1.00 40.76  ? 353 VAL   F N     1 
ATOM   13845 C  CA    A VAL   E 4  353 ? -7.649  59.558  77.306  0.33 41.11  ? 353 VAL   F CA    1 
ATOM   13846 C  CA    B VAL   E 4  353 ? -7.656  59.562  77.294  0.67 41.13  ? 353 VAL   F CA    1 
ATOM   13847 C  C     . VAL   E 4  353 ? -6.309  60.086  76.793  1.00 36.13  ? 353 VAL   F C     1 
ATOM   13848 O  O     . VAL   E 4  353 ? -6.201  61.261  76.430  1.00 36.59  ? 353 VAL   F O     1 
ATOM   13849 C  CB    A VAL   E 4  353 ? -7.747  59.628  78.842  0.33 39.89  ? 353 VAL   F CB    1 
ATOM   13850 C  CB    B VAL   E 4  353 ? -7.772  59.652  78.831  0.67 39.88  ? 353 VAL   F CB    1 
ATOM   13851 C  CG1   A VAL   E 4  353 ? -9.140  59.228  79.297  0.33 39.49  ? 353 VAL   F CG1   1 
ATOM   13852 C  CG1   B VAL   E 4  353 ? -8.709  58.576  79.360  0.67 37.84  ? 353 VAL   F CG1   1 
ATOM   13853 C  CG2   A VAL   E 4  353 ? -6.715  58.735  79.482  0.33 39.17  ? 353 VAL   F CG2   1 
ATOM   13854 C  CG2   B VAL   E 4  353 ? -6.415  59.554  79.503  0.67 39.30  ? 353 VAL   F CG2   1 
ATOM   13855 N  N     . ALA   E 4  354 ? -5.274  59.235  76.738  1.00 36.19  ? 354 ALA   F N     1 
ATOM   13856 C  CA    . ALA   E 4  354 ? -3.890  59.659  76.494  1.00 39.49  ? 354 ALA   F CA    1 
ATOM   13857 C  C     . ALA   E 4  354 ? -3.449  59.650  75.031  1.00 42.65  ? 354 ALA   F C     1 
ATOM   13858 O  O     . ALA   E 4  354 ? -2.650  60.508  74.637  1.00 42.70  ? 354 ALA   F O     1 
ATOM   13859 C  CB    . ALA   E 4  354 ? -2.920  58.784  77.300  1.00 35.25  ? 354 ALA   F CB    1 
ATOM   13860 N  N     . ILE   E 4  355 ? -3.923  58.702  74.220  1.00 41.01  ? 355 ILE   F N     1 
ATOM   13861 C  CA    . ILE   E 4  355 ? -3.475  58.532  72.837  1.00 39.16  ? 355 ILE   F CA    1 
ATOM   13862 C  C     . ILE   E 4  355 ? -4.535  58.996  71.842  1.00 43.14  ? 355 ILE   F C     1 
ATOM   13863 O  O     . ILE   E 4  355 ? -4.236  59.741  70.907  1.00 43.11  ? 355 ILE   F O     1 
ATOM   13864 C  CB    . ILE   E 4  355 ? -3.073  57.066  72.552  1.00 36.10  ? 355 ILE   F CB    1 
ATOM   13865 C  CG1   . ILE   E 4  355 ? -1.822  56.679  73.325  1.00 34.32  ? 355 ILE   F CG1   1 
ATOM   13866 C  CG2   . ILE   E 4  355 ? -2.874  56.851  71.061  1.00 31.74  ? 355 ILE   F CG2   1 
ATOM   13867 C  CD1   . ILE   E 4  355 ? -1.635  55.192  73.452  1.00 37.63  ? 355 ILE   F CD1   1 
ATOM   13868 N  N     . SER   E 4  356 ? -5.777  58.536  72.005  1.00 47.48  ? 356 SER   F N     1 
ATOM   13869 C  CA    . SER   E 4  356 ? -6.828  58.962  71.081  1.00 50.71  ? 356 SER   F CA    1 
ATOM   13870 C  C     . SER   E 4  356 ? -7.183  60.426  71.284  1.00 45.74  ? 356 SER   F C     1 
ATOM   13871 O  O     . SER   E 4  356 ? -7.629  61.096  70.345  1.00 41.64  ? 356 SER   F O     1 
ATOM   13872 C  CB    . SER   E 4  356 ? -8.069  58.079  71.235  1.00 47.80  ? 356 SER   F CB    1 
ATOM   13873 O  OG    . SER   E 4  356 ? -8.058  57.039  70.261  1.00 45.71  ? 356 SER   F OG    1 
ATOM   13874 N  N     . SER   E 4  357 ? -6.993  60.935  72.500  1.00 46.57  ? 357 SER   F N     1 
ATOM   13875 C  CA    . SER   E 4  357 ? -7.194  62.354  72.743  1.00 35.63  ? 357 SER   F CA    1 
ATOM   13876 C  C     . SER   E 4  357 ? -6.423  63.193  71.748  1.00 34.58  ? 357 SER   F C     1 
ATOM   13877 O  O     . SER   E 4  357 ? -6.886  64.266  71.357  1.00 41.02  ? 357 SER   F O     1 
ATOM   13878 C  CB    . SER   E 4  357 ? -6.760  62.696  74.155  1.00 34.40  ? 357 SER   F CB    1 
ATOM   13879 O  OG    . SER   E 4  357 ? -5.421  62.285  74.341  1.00 43.35  ? 357 SER   F OG    1 
ATOM   13880 N  N     . VAL   E 4  358 ? -5.253  62.720  71.330  1.00 37.75  ? 358 VAL   F N     1 
ATOM   13881 C  CA    . VAL   E 4  358 ? -4.373  63.447  70.427  1.00 33.84  ? 358 VAL   F CA    1 
ATOM   13882 C  C     . VAL   E 4  358 ? -4.553  62.998  68.987  1.00 40.45  ? 358 VAL   F C     1 
ATOM   13883 O  O     . VAL   E 4  358 ? -4.428  63.799  68.062  1.00 45.84  ? 358 VAL   F O     1 
ATOM   13884 C  CB    . VAL   E 4  358 ? -2.906  63.277  70.859  1.00 36.86  ? 358 VAL   F CB    1 
ATOM   13885 C  CG1   . VAL   E 4  358 ? -1.986  63.714  69.719  1.00 25.65  ? 358 VAL   F CG1   1 
ATOM   13886 C  CG2   . VAL   E 4  358 ? -2.642  64.038  72.158  1.00 33.04  ? 358 VAL   F CG2   1 
ATOM   13887 N  N     . PHE   E 4  359 ? -4.807  61.713  68.781  1.00 47.09  ? 359 PHE   F N     1 
ATOM   13888 C  CA    . PHE   E 4  359 ? -5.029  61.170  67.445  1.00 38.43  ? 359 PHE   F CA    1 
ATOM   13889 C  C     . PHE   E 4  359 ? -6.425  60.568  67.400  1.00 42.91  ? 359 PHE   F C     1 
ATOM   13890 O  O     . PHE   E 4  359 ? -6.622  59.417  67.829  1.00 46.19  ? 359 PHE   F O     1 
ATOM   13891 C  CB    . PHE   E 4  359 ? -3.955  60.143  67.113  1.00 35.45  ? 359 PHE   F CB    1 
ATOM   13892 C  CG    . PHE   E 4  359 ? -2.570  60.619  67.427  1.00 36.06  ? 359 PHE   F CG    1 
ATOM   13893 C  CD1   . PHE   E 4  359 ? -2.009  61.666  66.716  1.00 31.43  ? 359 PHE   F CD1   1 
ATOM   13894 C  CD2   . PHE   E 4  359 ? -1.828  60.034  68.444  1.00 42.73  ? 359 PHE   F CD2   1 
ATOM   13895 C  CE1   . PHE   E 4  359 ? -0.721  62.120  67.004  1.00 30.27  ? 359 PHE   F CE1   1 
ATOM   13896 C  CE2   . PHE   E 4  359 ? -0.533  60.485  68.741  1.00 39.05  ? 359 PHE   F CE2   1 
ATOM   13897 C  CZ    . PHE   E 4  359 ? 0.020   61.527  68.014  1.00 32.81  ? 359 PHE   F CZ    1 
ATOM   13898 N  N     . PRO   E 4  360 ? -7.423  61.321  66.929  1.00 47.64  ? 360 PRO   F N     1 
ATOM   13899 C  CA    . PRO   E 4  360 ? -8.818  60.866  66.954  1.00 41.51  ? 360 PRO   F CA    1 
ATOM   13900 C  C     . PRO   E 4  360 ? -9.165  59.970  65.765  1.00 53.23  ? 360 PRO   F C     1 
ATOM   13901 O  O     . PRO   E 4  360 ? -8.352  59.728  64.871  1.00 54.56  ? 360 PRO   F O     1 
ATOM   13902 C  CB    . PRO   E 4  360 ? -9.596  62.185  66.915  1.00 37.21  ? 360 PRO   F CB    1 
ATOM   13903 C  CG    . PRO   E 4  360 ? -8.629  63.220  67.399  1.00 38.97  ? 360 PRO   F CG    1 
ATOM   13904 C  CD    . PRO   E 4  360 ? -7.345  62.784  66.796  1.00 40.61  ? 360 PRO   F CD    1 
ATOM   13905 N  N     . LEU   E 4  361 ? -10.424 59.512  65.748  1.00 57.94  ? 361 LEU   F N     1 
ATOM   13906 C  CA    . LEU   E 4  361 ? -10.813 58.357  64.942  1.00 53.46  ? 361 LEU   F CA    1 
ATOM   13907 C  C     . LEU   E 4  361 ? -11.988 58.593  63.989  1.00 70.97  ? 361 LEU   F C     1 
ATOM   13908 O  O     . LEU   E 4  361 ? -11.799 58.576  62.765  1.00 73.45  ? 361 LEU   F O     1 
ATOM   13909 C  CB    . LEU   E 4  361 ? -11.127 57.194  65.885  1.00 41.47  ? 361 LEU   F CB    1 
ATOM   13910 C  CG    . LEU   E 4  361 ? -9.908  56.800  66.704  1.00 37.60  ? 361 LEU   F CG    1 
ATOM   13911 C  CD1   . LEU   E 4  361 ? -10.280 55.854  67.789  1.00 26.85  ? 361 LEU   F CD1   1 
ATOM   13912 C  CD2   . LEU   E 4  361 ? -8.889  56.178  65.771  1.00 44.44  ? 361 LEU   F CD2   1 
ATOM   13913 N  N     . ALA   E 4  362 ? -13.202 58.771  64.522  1.00 73.37  ? 362 ALA   F N     1 
ATOM   13914 C  CA    . ALA   E 4  362 ? -14.414 58.870  63.687  1.00 78.58  ? 362 ALA   F CA    1 
ATOM   13915 C  C     . ALA   E 4  362 ? -15.722 58.860  64.509  1.00 84.68  ? 362 ALA   F C     1 
ATOM   13916 O  O     . ALA   E 4  362 ? -16.838 58.804  63.961  1.00 74.52  ? 362 ALA   F O     1 
ATOM   13917 C  CB    . ALA   E 4  362 ? -14.430 57.733  62.657  1.00 71.56  ? 362 ALA   F CB    1 
ATOM   13918 N  N     . THR   E 4  372 ? -18.827 56.698  83.620  1.00 68.76  ? 372 THR   F N     1 
ATOM   13919 C  CA    . THR   E 4  372 ? -18.356 56.338  82.285  1.00 72.45  ? 372 THR   F CA    1 
ATOM   13920 C  C     . THR   E 4  372 ? -16.834 56.285  82.256  1.00 90.03  ? 372 THR   F C     1 
ATOM   13921 O  O     . THR   E 4  372 ? -16.252 55.217  82.066  1.00 98.51  ? 372 THR   F O     1 
ATOM   13922 C  CB    . THR   E 4  372 ? -18.839 57.326  81.214  1.00 77.15  ? 372 THR   F CB    1 
ATOM   13923 O  OG1   . THR   E 4  372 ? -20.268 57.329  81.173  1.00 86.02  ? 372 THR   F OG1   1 
ATOM   13924 C  CG2   . THR   E 4  372 ? -18.318 56.922  79.853  1.00 86.21  ? 372 THR   F CG2   1 
ATOM   13925 N  N     . SER   E 4  373 ? -16.199 57.444  82.441  1.00 87.73  ? 373 SER   F N     1 
ATOM   13926 C  CA    . SER   E 4  373 ? -14.744 57.517  82.543  1.00 61.84  ? 373 SER   F CA    1 
ATOM   13927 C  C     . SER   E 4  373 ? -14.231 56.685  83.719  1.00 57.51  ? 373 SER   F C     1 
ATOM   13928 O  O     . SER   E 4  373 ? -14.760 56.764  84.833  1.00 61.12  ? 373 SER   F O     1 
ATOM   13929 C  CB    . SER   E 4  373 ? -14.313 58.977  82.699  1.00 69.44  ? 373 SER   F CB    1 
ATOM   13930 O  OG    . SER   E 4  373 ? -13.216 59.106  83.588  1.00 64.44  ? 373 SER   F OG    1 
ATOM   13931 N  N     . ILE   E 4  374 ? -13.187 55.886  83.464  1.00 50.61  ? 374 ILE   F N     1 
ATOM   13932 C  CA    . ILE   E 4  374 ? -12.571 55.065  84.507  1.00 49.78  ? 374 ILE   F CA    1 
ATOM   13933 C  C     . ILE   E 4  374 ? -11.618 55.844  85.395  1.00 48.54  ? 374 ILE   F C     1 
ATOM   13934 O  O     . ILE   E 4  374 ? -11.091 55.279  86.364  1.00 42.95  ? 374 ILE   F O     1 
ATOM   13935 C  CB    . ILE   E 4  374 ? -11.772 53.892  83.911  1.00 44.39  ? 374 ILE   F CB    1 
ATOM   13936 C  CG1   . ILE   E 4  374 ? -10.694 54.431  82.962  1.00 49.78  ? 374 ILE   F CG1   1 
ATOM   13937 C  CG2   . ILE   E 4  374 ? -12.704 52.927  83.203  1.00 51.01  ? 374 ILE   F CG2   1 
ATOM   13938 C  CD1   . ILE   E 4  374 ? -9.449  53.547  82.829  1.00 45.35  ? 374 ILE   F CD1   1 
ATOM   13939 N  N     . PHE   E 4  375 ? -11.371 57.116  85.089  1.00 47.23  ? 375 PHE   F N     1 
ATOM   13940 C  CA    . PHE   E 4  375 ? -10.383 57.931  85.777  1.00 50.33  ? 375 PHE   F CA    1 
ATOM   13941 C  C     . PHE   E 4  375 ? -11.050 59.004  86.630  1.00 47.42  ? 375 PHE   F C     1 
ATOM   13942 O  O     . PHE   E 4  375 ? -12.192 59.403  86.389  1.00 57.27  ? 375 PHE   F O     1 
ATOM   13943 C  CB    . PHE   E 4  375 ? -9.428  58.586  84.771  1.00 50.69  ? 375 PHE   F CB    1 
ATOM   13944 C  CG    . PHE   E 4  375 ? -8.501  57.621  84.099  1.00 42.19  ? 375 PHE   F CG    1 
ATOM   13945 C  CD1   . PHE   E 4  375 ? -7.606  56.870  84.843  1.00 39.23  ? 375 PHE   F CD1   1 
ATOM   13946 C  CD2   . PHE   E 4  375 ? -8.514  57.475  82.728  1.00 39.02  ? 375 PHE   F CD2   1 
ATOM   13947 C  CE1   . PHE   E 4  375 ? -6.753  55.985  84.229  1.00 44.00  ? 375 PHE   F CE1   1 
ATOM   13948 C  CE2   . PHE   E 4  375 ? -7.661  56.597  82.110  1.00 40.62  ? 375 PHE   F CE2   1 
ATOM   13949 C  CZ    . PHE   E 4  375 ? -6.781  55.847  82.863  1.00 41.90  ? 375 PHE   F CZ    1 
ATOM   13950 N  N     . ILE   E 4  376 ? -10.314 59.469  87.638  1.00 36.72  ? 376 ILE   F N     1 
ATOM   13951 C  CA    . ILE   E 4  376 ? -10.714 60.602  88.467  1.00 40.30  ? 376 ILE   F CA    1 
ATOM   13952 C  C     . ILE   E 4  376 ? -9.702  61.710  88.205  1.00 43.17  ? 376 ILE   F C     1 
ATOM   13953 O  O     . ILE   E 4  376 ? -8.550  61.633  88.658  1.00 37.13  ? 376 ILE   F O     1 
ATOM   13954 C  CB    . ILE   E 4  376 ? -10.778 60.232  89.957  1.00 34.54  ? 376 ILE   F CB    1 
ATOM   13955 C  CG1   . ILE   E 4  376 ? -11.990 59.354  90.220  1.00 39.92  ? 376 ILE   F CG1   1 
ATOM   13956 C  CG2   . ILE   E 4  376 ? -10.849 61.457  90.832  1.00 27.62  ? 376 ILE   F CG2   1 
ATOM   13957 C  CD1   . ILE   E 4  376 ? -11.657 58.081  90.953  1.00 41.79  ? 376 ILE   F CD1   1 
ATOM   13958 N  N     . LYS   E 4  377 ? -10.124 62.729  87.454  1.00 44.44  ? 377 LYS   F N     1 
ATOM   13959 C  CA    . LYS   E 4  377 ? -9.260  63.862  87.138  1.00 45.09  ? 377 LYS   F CA    1 
ATOM   13960 C  C     . LYS   E 4  377 ? -8.970  64.655  88.412  1.00 41.05  ? 377 LYS   F C     1 
ATOM   13961 O  O     . LYS   E 4  377 ? -9.893  65.155  89.060  1.00 42.53  ? 377 LYS   F O     1 
ATOM   13962 C  CB    . LYS   E 4  377 ? -9.937  64.741  86.085  1.00 46.31  ? 377 LYS   F CB    1 
ATOM   13963 C  CG    . LYS   E 4  377 ? -9.030  65.675  85.297  1.00 42.74  ? 377 LYS   F CG    1 
ATOM   13964 C  CD    . LYS   E 4  377 ? -9.793  66.939  84.858  1.00 58.78  ? 377 LYS   F CD    1 
ATOM   13965 C  CE    . LYS   E 4  377 ? -9.237  67.556  83.572  1.00 59.70  ? 377 LYS   F CE    1 
ATOM   13966 N  NZ    . LYS   E 4  377 ? -9.753  66.870  82.343  1.00 58.37  ? 377 LYS   F NZ    1 
ATOM   13967 N  N     . LEU   E 4  378 ? -7.695  64.770  88.778  1.00 33.76  ? 378 LEU   F N     1 
ATOM   13968 C  CA    . LEU   E 4  378 ? -7.296  65.473  89.999  1.00 31.58  ? 378 LEU   F CA    1 
ATOM   13969 C  C     . LEU   E 4  378 ? -7.160  66.963  89.690  1.00 42.08  ? 378 LEU   F C     1 
ATOM   13970 O  O     . LEU   E 4  378 ? -6.167  67.405  89.103  1.00 48.20  ? 378 LEU   F O     1 
ATOM   13971 C  CB    . LEU   E 4  378 ? -6.006  64.881  90.550  1.00 30.92  ? 378 LEU   F CB    1 
ATOM   13972 C  CG    . LEU   E 4  378 ? -5.945  63.368  90.809  1.00 32.83  ? 378 LEU   F CG    1 
ATOM   13973 C  CD1   . LEU   E 4  378 ? -4.758  63.010  91.722  1.00 37.27  ? 378 LEU   F CD1   1 
ATOM   13974 C  CD2   . LEU   E 4  378 ? -7.241  62.831  91.392  1.00 27.82  ? 378 LEU   F CD2   1 
ATOM   13975 N  N     . HIS   E 4  379 ? -8.166  67.742  90.102  1.00 60.05  ? 379 HIS   F N     1 
ATOM   13976 C  CA    . HIS   E 4  379 ? -8.334  69.117  89.629  1.00 63.03  ? 379 HIS   F CA    1 
ATOM   13977 C  C     . HIS   E 4  379 ? -7.292  70.049  90.238  1.00 70.60  ? 379 HIS   F C     1 
ATOM   13978 O  O     . HIS   E 4  379 ? -7.088  70.063  91.458  1.00 68.63  ? 379 HIS   F O     1 
ATOM   13979 C  CB    . HIS   E 4  379 ? -9.739  69.641  89.958  1.00 66.23  ? 379 HIS   F CB    1 
ATOM   13980 C  CG    . HIS   E 4  379 ? -10.820 69.128  89.050  1.00 69.17  ? 379 HIS   F CG    1 
ATOM   13981 N  ND1   . HIS   E 4  379 ? -10.567 68.321  87.960  1.00 71.35  ? 379 HIS   F ND1   1 
ATOM   13982 C  CD2   . HIS   E 4  379 ? -12.164 69.301  89.082  1.00 75.68  ? 379 HIS   F CD2   1 
ATOM   13983 C  CE1   . HIS   E 4  379 ? -11.706 68.022  87.360  1.00 69.77  ? 379 HIS   F CE1   1 
ATOM   13984 N  NE2   . HIS   E 4  379 ? -12.691 68.604  88.021  1.00 77.34  ? 379 HIS   F NE2   1 
ATOM   13985 N  N     . HIS   E 4  380 ? -6.666  70.857  89.379  1.00 71.47  ? 380 HIS   F N     1 
ATOM   13986 C  CA    . HIS   E 4  380 ? -5.654  71.830  89.781  1.00 69.41  ? 380 HIS   F CA    1 
ATOM   13987 C  C     . HIS   E 4  380 ? -5.580  72.991  88.772  1.00 73.09  ? 380 HIS   F C     1 
ATOM   13988 O  O     . HIS   E 4  380 ? -5.841  74.159  89.097  1.00 67.08  ? 380 HIS   F O     1 
ATOM   13989 C  CB    . HIS   E 4  380 ? -4.289  71.146  89.914  1.00 62.60  ? 380 HIS   F CB    1 
ATOM   13990 C  CG    . HIS   E 4  380 ? -3.753  70.600  88.624  1.00 66.90  ? 380 HIS   F CG    1 
ATOM   13991 N  ND1   . HIS   E 4  380 ? -2.547  71.006  88.087  1.00 69.47  ? 380 HIS   F ND1   1 
ATOM   13992 C  CD2   . HIS   E 4  380 ? -4.248  69.668  87.773  1.00 65.90  ? 380 HIS   F CD2   1 
ATOM   13993 C  CE1   . HIS   E 4  380 ? -2.330  70.358  86.957  1.00 57.50  ? 380 HIS   F CE1   1 
ATOM   13994 N  NE2   . HIS   E 4  380 ? -3.347  69.541  86.743  1.00 60.95  ? 380 HIS   F NE2   1 
ATOM   13995 N  N     . MET   F 2  1   ? 27.973  78.759  31.251  1.00 56.75  ? 1   MET   B N     1 
ATOM   13996 C  CA    . MET   F 2  1   ? 26.946  77.826  31.722  1.00 67.02  ? 1   MET   B CA    1 
ATOM   13997 C  C     . MET   F 2  1   ? 27.405  76.361  31.662  1.00 57.99  ? 1   MET   B C     1 
ATOM   13998 O  O     . MET   F 2  1   ? 28.391  76.038  30.992  1.00 60.34  ? 1   MET   B O     1 
ATOM   13999 C  CB    . MET   F 2  1   ? 25.653  78.002  30.913  1.00 67.73  ? 1   MET   B CB    1 
ATOM   14000 C  CG    . MET   F 2  1   ? 25.840  78.060  29.389  1.00 72.15  ? 1   MET   B CG    1 
ATOM   14001 S  SD    . MET   F 2  1   ? 26.759  79.511  28.797  1.00 95.41  ? 1   MET   B SD    1 
ATOM   14002 C  CE    . MET   F 2  1   ? 25.993  80.843  29.736  1.00 63.84  ? 1   MET   B CE    1 
ATOM   14003 N  N     . ARG   F 2  2   ? 26.711  75.480  32.384  1.00 43.01  ? 2   ARG   B N     1 
ATOM   14004 C  CA    . ARG   F 2  2   ? 26.989  74.054  32.298  1.00 36.86  ? 2   ARG   B CA    1 
ATOM   14005 C  C     . ARG   F 2  2   ? 26.252  73.526  31.065  1.00 41.49  ? 2   ARG   B C     1 
ATOM   14006 O  O     . ARG   F 2  2   ? 25.018  73.585  30.981  1.00 37.17  ? 2   ARG   B O     1 
ATOM   14007 C  CB    . ARG   F 2  2   ? 26.600  73.338  33.594  1.00 35.47  ? 2   ARG   B CB    1 
ATOM   14008 C  CG    . ARG   F 2  2   ? 27.363  73.814  34.852  1.00 36.42  ? 2   ARG   B CG    1 
ATOM   14009 C  CD    . ARG   F 2  2   ? 28.554  72.909  35.299  1.00 38.28  ? 2   ARG   B CD    1 
ATOM   14010 N  NE    . ARG   F 2  2   ? 28.162  71.546  35.669  1.00 42.85  ? 2   ARG   B NE    1 
ATOM   14011 C  CZ    . ARG   F 2  2   ? 29.006  70.563  35.980  1.00 42.97  ? 2   ARG   B CZ    1 
ATOM   14012 N  NH1   . ARG   F 2  2   ? 30.309  70.770  36.077  1.00 44.03  ? 2   ARG   B NH1   1 
ATOM   14013 N  NH2   . ARG   F 2  2   ? 28.533  69.334  36.180  1.00 35.62  ? 2   ARG   B NH2   1 
ATOM   14014 N  N     . GLU   F 2  3   ? 27.019  73.089  30.068  1.00 46.66  ? 3   GLU   B N     1 
ATOM   14015 C  CA    . GLU   F 2  3   ? 26.482  72.585  28.817  1.00 34.26  ? 3   GLU   B CA    1 
ATOM   14016 C  C     . GLU   F 2  3   ? 26.355  71.073  28.885  1.00 29.17  ? 3   GLU   B C     1 
ATOM   14017 O  O     . GLU   F 2  3   ? 27.095  70.388  29.593  1.00 33.58  ? 3   GLU   B O     1 
ATOM   14018 C  CB    . GLU   F 2  3   ? 27.352  72.974  27.620  1.00 30.85  ? 3   GLU   B CB    1 
ATOM   14019 C  CG    . GLU   F 2  3   ? 27.309  74.431  27.249  1.00 31.59  ? 3   GLU   B CG    1 
ATOM   14020 C  CD    . GLU   F 2  3   ? 28.528  75.170  27.741  1.00 41.34  ? 3   GLU   B CD    1 
ATOM   14021 O  OE1   . GLU   F 2  3   ? 29.266  74.582  28.554  1.00 44.09  ? 3   GLU   B OE1   1 
ATOM   14022 O  OE2   . GLU   F 2  3   ? 28.758  76.326  27.326  1.00 43.07  ? 3   GLU   B OE2   1 
ATOM   14023 N  N     . ILE   F 2  4   ? 25.382  70.571  28.150  1.00 31.67  ? 4   ILE   B N     1 
ATOM   14024 C  CA    . ILE   F 2  4   ? 25.133  69.151  28.005  1.00 26.94  ? 4   ILE   B CA    1 
ATOM   14025 C  C     . ILE   F 2  4   ? 25.227  68.852  26.509  1.00 32.29  ? 4   ILE   B C     1 
ATOM   14026 O  O     . ILE   F 2  4   ? 24.656  69.581  25.691  1.00 30.84  ? 4   ILE   B O     1 
ATOM   14027 C  CB    . ILE   F 2  4   ? 23.762  68.776  28.610  1.00 19.56  ? 4   ILE   B CB    1 
ATOM   14028 C  CG1   . ILE   F 2  4   ? 23.785  69.018  30.134  1.00 24.43  ? 4   ILE   B CG1   1 
ATOM   14029 C  CG2   . ILE   F 2  4   ? 23.414  67.353  28.292  1.00 26.27  ? 4   ILE   B CG2   1 
ATOM   14030 C  CD1   . ILE   F 2  4   ? 22.532  68.652  30.928  1.00 13.80  ? 4   ILE   B CD1   1 
ATOM   14031 N  N     . VAL   F 2  5   ? 26.002  67.836  26.143  1.00 31.54  ? 5   VAL   B N     1 
ATOM   14032 C  CA    . VAL   F 2  5   ? 26.053  67.359  24.760  1.00 34.44  ? 5   VAL   B CA    1 
ATOM   14033 C  C     . VAL   F 2  5   ? 25.098  66.165  24.616  1.00 27.98  ? 5   VAL   B C     1 
ATOM   14034 O  O     . VAL   F 2  5   ? 25.247  65.134  25.292  1.00 20.41  ? 5   VAL   B O     1 
ATOM   14035 C  CB    . VAL   F 2  5   ? 27.495  67.013  24.333  1.00 29.14  ? 5   VAL   B CB    1 
ATOM   14036 C  CG1   . VAL   F 2  5   ? 27.515  66.365  22.973  1.00 27.43  ? 5   VAL   B CG1   1 
ATOM   14037 C  CG2   . VAL   F 2  5   ? 28.349  68.273  24.289  1.00 27.38  ? 5   VAL   B CG2   1 
ATOM   14038 N  N     . HIS   F 2  6   ? 24.100  66.328  23.748  1.00 24.53  ? 6   HIS   B N     1 
ATOM   14039 C  CA    . HIS   F 2  6   ? 23.094  65.317  23.470  1.00 21.26  ? 6   HIS   B CA    1 
ATOM   14040 C  C     . HIS   F 2  6   ? 23.534  64.521  22.246  1.00 27.51  ? 6   HIS   B C     1 
ATOM   14041 O  O     . HIS   F 2  6   ? 23.880  65.103  21.218  1.00 30.69  ? 6   HIS   B O     1 
ATOM   14042 C  CB    . HIS   F 2  6   ? 21.728  65.985  23.256  1.00 19.60  ? 6   HIS   B CB    1 
ATOM   14043 C  CG    . HIS   F 2  6   ? 20.678  65.097  22.641  1.00 34.88  ? 6   HIS   B CG    1 
ATOM   14044 N  ND1   . HIS   F 2  6   ? 19.699  64.470  23.384  1.00 31.48  ? 6   HIS   B ND1   1 
ATOM   14045 C  CD2   . HIS   F 2  6   ? 20.436  64.760  21.347  1.00 33.42  ? 6   HIS   B CD2   1 
ATOM   14046 C  CE1   . HIS   F 2  6   ? 18.918  63.768  22.580  1.00 29.64  ? 6   HIS   B CE1   1 
ATOM   14047 N  NE2   . HIS   F 2  6   ? 19.339  63.931  21.338  1.00 29.50  ? 6   HIS   B NE2   1 
ATOM   14048 N  N     . ILE   F 2  7   ? 23.564  63.196  22.377  1.00 26.99  ? 7   ILE   B N     1 
ATOM   14049 C  CA    . ILE   F 2  7   ? 23.816  62.272  21.279  1.00 25.32  ? 7   ILE   B CA    1 
ATOM   14050 C  C     . ILE   F 2  7   ? 22.579  61.398  21.140  1.00 28.57  ? 7   ILE   B C     1 
ATOM   14051 O  O     . ILE   F 2  7   ? 22.036  60.933  22.149  1.00 26.21  ? 7   ILE   B O     1 
ATOM   14052 C  CB    . ILE   F 2  7   ? 25.066  61.405  21.551  1.00 22.12  ? 7   ILE   B CB    1 
ATOM   14053 C  CG1   . ILE   F 2  7   ? 26.216  62.269  22.038  1.00 22.99  ? 7   ILE   B CG1   1 
ATOM   14054 C  CG2   . ILE   F 2  7   ? 25.485  60.608  20.344  1.00 12.88  ? 7   ILE   B CG2   1 
ATOM   14055 C  CD1   . ILE   F 2  7   ? 27.473  61.507  22.213  1.00 17.94  ? 7   ILE   B CD1   1 
ATOM   14056 N  N     . GLN   F 2  8   ? 22.125  61.179  19.902  1.00 27.38  ? 8   GLN   B N     1 
ATOM   14057 C  CA    . GLN   F 2  8   ? 20.993  60.292  19.633  1.00 25.85  ? 8   GLN   B CA    1 
ATOM   14058 C  C     . GLN   F 2  8   ? 21.326  59.369  18.472  1.00 26.59  ? 8   GLN   B C     1 
ATOM   14059 O  O     . GLN   F 2  8   ? 21.744  59.838  17.410  1.00 30.24  ? 8   GLN   B O     1 
ATOM   14060 C  CB    . GLN   F 2  8   ? 19.739  61.084  19.320  1.00 21.25  ? 8   GLN   B CB    1 
ATOM   14061 C  CG    . GLN   F 2  8   ? 19.867  61.900  18.075  1.00 25.75  ? 8   GLN   B CG    1 
ATOM   14062 C  CD    . GLN   F 2  8   ? 18.696  62.851  17.910  1.00 28.94  ? 8   GLN   B CD    1 
ATOM   14063 O  OE1   . GLN   F 2  8   ? 18.362  63.621  18.828  1.00 26.24  ? 8   GLN   B OE1   1 
ATOM   14064 N  NE2   . GLN   F 2  8   ? 18.042  62.782  16.756  1.00 24.89  ? 8   GLN   B NE2   1 
ATOM   14065 N  N     . ALA   F 2  9   ? 21.124  58.066  18.671  1.00 19.70  ? 9   ALA   B N     1 
ATOM   14066 C  CA    . ALA   F 2  9   ? 21.696  57.047  17.799  1.00 17.90  ? 9   ALA   B CA    1 
ATOM   14067 C  C     . ALA   F 2  9   ? 20.693  55.941  17.511  1.00 18.72  ? 9   ALA   B C     1 
ATOM   14068 O  O     . ALA   F 2  9   ? 20.013  55.449  18.419  1.00 31.18  ? 9   ALA   B O     1 
ATOM   14069 C  CB    . ALA   F 2  9   ? 22.948  56.440  18.434  1.00 15.49  ? 9   ALA   B CB    1 
ATOM   14070 N  N     . GLY   F 2  10  ? 20.617  55.536  16.253  1.00 13.74  ? 10  GLY   B N     1 
ATOM   14071 C  CA    . GLY   F 2  10  ? 19.690  54.503  15.844  1.00 17.69  ? 10  GLY   B CA    1 
ATOM   14072 C  C     . GLY   F 2  10  ? 18.276  55.025  15.604  1.00 24.29  ? 10  GLY   B C     1 
ATOM   14073 O  O     . GLY   F 2  10  ? 17.943  56.193  15.851  1.00 24.15  ? 10  GLY   B O     1 
ATOM   14074 N  N     . GLN   F 2  11  ? 17.427  54.131  15.094  1.00 13.85  ? 11  GLN   B N     1 
ATOM   14075 C  CA    . GLN   F 2  11  ? 16.034  54.471  14.850  1.00 22.56  ? 11  GLN   B CA    1 
ATOM   14076 C  C     . GLN   F 2  11  ? 15.365  55.000  16.123  1.00 22.87  ? 11  GLN   B C     1 
ATOM   14077 O  O     . GLN   F 2  11  ? 15.089  56.201  16.243  1.00 21.28  ? 11  GLN   B O     1 
ATOM   14078 C  CB    . GLN   F 2  11  ? 15.287  53.257  14.291  1.00 27.19  ? 11  GLN   B CB    1 
ATOM   14079 C  CG    . GLN   F 2  11  ? 14.087  53.573  13.373  1.00 40.26  ? 11  GLN   B CG    1 
ATOM   14080 C  CD    . GLN   F 2  11  ? 13.142  52.372  13.205  1.00 53.39  ? 11  GLN   B CD    1 
ATOM   14081 O  OE1   . GLN   F 2  11  ? 13.552  51.282  12.755  1.00 57.70  ? 11  GLN   B OE1   1 
ATOM   14082 N  NE2   . GLN   F 2  11  ? 11.877  52.559  13.601  1.00 39.15  ? 11  GLN   B NE2   1 
ATOM   14083 N  N     . CYS   F 2  12  ? 15.123  54.120  17.094  1.00 20.65  ? 12  CYS   B N     1 
ATOM   14084 C  CA    . CYS   F 2  12  ? 14.522  54.561  18.346  1.00 15.37  ? 12  CYS   B CA    1 
ATOM   14085 C  C     . CYS   F 2  12  ? 15.219  55.809  18.866  1.00 20.32  ? 12  CYS   B C     1 
ATOM   14086 O  O     . CYS   F 2  12  ? 14.608  56.873  18.982  1.00 23.55  ? 12  CYS   B O     1 
ATOM   14087 C  CB    . CYS   F 2  12  ? 14.566  53.436  19.380  1.00 15.54  ? 12  CYS   B CB    1 
ATOM   14088 S  SG    . CYS   F 2  12  ? 13.865  53.889  20.972  1.00 18.40  ? 12  CYS   B SG    1 
ATOM   14089 N  N     . GLY   F 2  13  ? 16.514  55.697  19.164  1.00 24.15  ? 13  GLY   B N     1 
ATOM   14090 C  CA    . GLY   F 2  13  ? 17.296  56.823  19.616  1.00 17.17  ? 13  GLY   B CA    1 
ATOM   14091 C  C     . GLY   F 2  13  ? 17.004  58.108  18.872  1.00 20.88  ? 13  GLY   B C     1 
ATOM   14092 O  O     . GLY   F 2  13  ? 16.768  59.132  19.502  1.00 23.84  ? 13  GLY   B O     1 
ATOM   14093 N  N     . ASN   F 2  14  ? 16.994  58.074  17.540  1.00 23.73  ? 14  ASN   B N     1 
ATOM   14094 C  CA    . ASN   F 2  14  ? 16.880  59.306  16.756  1.00 25.98  ? 14  ASN   B CA    1 
ATOM   14095 C  C     . ASN   F 2  14  ? 15.466  59.863  16.753  1.00 24.77  ? 14  ASN   B C     1 
ATOM   14096 O  O     . ASN   F 2  14  ? 15.277  61.049  16.479  1.00 26.50  ? 14  ASN   B O     1 
ATOM   14097 C  CB    . ASN   F 2  14  ? 17.327  59.069  15.314  1.00 23.33  ? 14  ASN   B CB    1 
ATOM   14098 C  CG    . ASN   F 2  14  ? 18.773  59.331  15.135  1.00 22.76  ? 14  ASN   B CG    1 
ATOM   14099 O  OD1   . ASN   F 2  14  ? 19.207  60.480  15.151  1.00 22.64  ? 14  ASN   B OD1   1 
ATOM   14100 N  ND2   . ASN   F 2  14  ? 19.547  58.277  14.983  1.00 22.33  ? 14  ASN   B ND2   1 
ATOM   14101 N  N     . GLN   F 2  15  ? 14.464  59.030  17.023  1.00 24.30  ? 15  GLN   B N     1 
ATOM   14102 C  CA    . GLN   F 2  15  ? 13.078  59.476  16.965  1.00 28.56  ? 15  GLN   B CA    1 
ATOM   14103 C  C     . GLN   F 2  15  ? 12.552  60.002  18.290  1.00 25.27  ? 15  GLN   B C     1 
ATOM   14104 O  O     . GLN   F 2  15  ? 11.749  60.942  18.311  1.00 23.65  ? 15  GLN   B O     1 
ATOM   14105 C  CB    . GLN   F 2  15  ? 12.193  58.338  16.485  1.00 27.80  ? 15  GLN   B CB    1 
ATOM   14106 C  CG    . GLN   F 2  15  ? 12.418  57.990  15.045  1.00 31.24  ? 15  GLN   B CG    1 
ATOM   14107 C  CD    . GLN   F 2  15  ? 11.178  57.412  14.483  1.00 43.30  ? 15  GLN   B CD    1 
ATOM   14108 O  OE1   . GLN   F 2  15  ? 10.910  56.205  14.640  1.00 34.97  ? 15  GLN   B OE1   1 
ATOM   14109 N  NE2   . GLN   F 2  15  ? 10.353  58.274  13.886  1.00 42.43  ? 15  GLN   B NE2   1 
ATOM   14110 N  N     . ILE   F 2  16  ? 12.944  59.390  19.406  1.00 26.53  ? 16  ILE   B N     1 
ATOM   14111 C  CA    . ILE   F 2  16  ? 12.600  60.023  20.661  1.00 25.43  ? 16  ILE   B CA    1 
ATOM   14112 C  C     . ILE   F 2  16  ? 13.449  61.261  20.826  1.00 27.25  ? 16  ILE   B C     1 
ATOM   14113 O  O     . ILE   F 2  16  ? 13.034  62.215  21.499  1.00 33.65  ? 16  ILE   B O     1 
ATOM   14114 C  CB    . ILE   F 2  16  ? 12.756  59.064  21.853  1.00 17.54  ? 16  ILE   B CB    1 
ATOM   14115 C  CG1   . ILE   F 2  16  ? 14.228  58.731  22.098  1.00 20.93  ? 16  ILE   B CG1   1 
ATOM   14116 C  CG2   . ILE   F 2  16  ? 11.936  57.809  21.629  1.00 14.50  ? 16  ILE   B CG2   1 
ATOM   14117 C  CD1   . ILE   F 2  16  ? 14.450  57.855  23.341  1.00 19.71  ? 16  ILE   B CD1   1 
ATOM   14118 N  N     . GLY   F 2  17  ? 14.612  61.287  20.177  1.00 21.18  ? 17  GLY   B N     1 
ATOM   14119 C  CA    . GLY   F 2  17  ? 15.506  62.416  20.339  1.00 22.60  ? 17  GLY   B CA    1 
ATOM   14120 C  C     . GLY   F 2  17  ? 14.981  63.640  19.629  1.00 26.30  ? 17  GLY   B C     1 
ATOM   14121 O  O     . GLY   F 2  17  ? 14.933  64.731  20.200  1.00 27.64  ? 17  GLY   B O     1 
ATOM   14122 N  N     . ALA   F 2  18  ? 14.566  63.468  18.374  1.00 31.11  ? 18  ALA   B N     1 
ATOM   14123 C  CA    . ALA   F 2  18  ? 13.912  64.554  17.652  1.00 27.45  ? 18  ALA   B CA    1 
ATOM   14124 C  C     . ALA   F 2  18  ? 12.686  65.058  18.407  1.00 24.33  ? 18  ALA   B C     1 
ATOM   14125 O  O     . ALA   F 2  18  ? 12.507  66.266  18.587  1.00 34.11  ? 18  ALA   B O     1 
ATOM   14126 C  CB    . ALA   F 2  18  ? 13.536  64.082  16.253  1.00 23.35  ? 18  ALA   B CB    1 
ATOM   14127 N  N     . LYS   F 2  19  ? 11.838  64.145  18.878  1.00 26.85  ? 19  LYS   B N     1 
ATOM   14128 C  CA    . LYS   F 2  19  ? 10.667  64.548  19.654  1.00 35.07  ? 19  LYS   B CA    1 
ATOM   14129 C  C     . LYS   F 2  19  ? 11.069  65.369  20.873  1.00 28.83  ? 19  LYS   B C     1 
ATOM   14130 O  O     . LYS   F 2  19  ? 10.557  66.470  21.082  1.00 27.66  ? 19  LYS   B O     1 
ATOM   14131 C  CB    . LYS   F 2  19  ? 9.848   63.319  20.065  1.00 32.63  ? 19  LYS   B CB    1 
ATOM   14132 C  CG    . LYS   F 2  19  ? 8.719   62.970  19.089  1.00 30.48  ? 19  LYS   B CG    1 
ATOM   14133 C  CD    . LYS   F 2  19  ? 7.492   63.877  19.294  1.00 49.72  ? 19  LYS   B CD    1 
ATOM   14134 C  CE    . LYS   F 2  19  ? 6.794   63.627  20.659  1.00 53.40  ? 19  LYS   B CE    1 
ATOM   14135 N  NZ    . LYS   F 2  19  ? 5.513   64.398  20.868  1.00 47.48  ? 19  LYS   B NZ    1 
ATOM   14136 N  N     . PHE   F 2  20  ? 11.984  64.848  21.694  1.00 27.92  ? 20  PHE   B N     1 
ATOM   14137 C  CA    . PHE   F 2  20  ? 12.508  65.647  22.798  1.00 30.72  ? 20  PHE   B CA    1 
ATOM   14138 C  C     . PHE   F 2  20  ? 12.856  67.064  22.353  1.00 30.17  ? 20  PHE   B C     1 
ATOM   14139 O  O     . PHE   F 2  20  ? 12.520  68.042  23.035  1.00 32.18  ? 20  PHE   B O     1 
ATOM   14140 C  CB    . PHE   F 2  20  ? 13.733  64.970  23.399  1.00 28.18  ? 20  PHE   B CB    1 
ATOM   14141 C  CG    . PHE   F 2  20  ? 14.530  65.848  24.330  1.00 25.33  ? 20  PHE   B CG    1 
ATOM   14142 C  CD1   . PHE   F 2  20  ? 14.092  66.088  25.617  1.00 22.58  ? 20  PHE   B CD1   1 
ATOM   14143 C  CD2   . PHE   F 2  20  ? 15.734  66.413  23.918  1.00 28.71  ? 20  PHE   B CD2   1 
ATOM   14144 C  CE1   . PHE   F 2  20  ? 14.836  66.876  26.489  1.00 23.97  ? 20  PHE   B CE1   1 
ATOM   14145 C  CE2   . PHE   F 2  20  ? 16.500  67.207  24.784  1.00 25.47  ? 20  PHE   B CE2   1 
ATOM   14146 C  CZ    . PHE   F 2  20  ? 16.049  67.429  26.077  1.00 26.19  ? 20  PHE   B CZ    1 
ATOM   14147 N  N     . TRP   F 2  21  ? 13.507  67.200  21.199  1.00 29.66  ? 21  TRP   B N     1 
ATOM   14148 C  CA    . TRP   F 2  21  ? 13.977  68.520  20.784  1.00 33.47  ? 21  TRP   B CA    1 
ATOM   14149 C  C     . TRP   F 2  21  ? 12.818  69.440  20.435  1.00 32.17  ? 21  TRP   B C     1 
ATOM   14150 O  O     . TRP   F 2  21  ? 12.810  70.615  20.828  1.00 30.39  ? 21  TRP   B O     1 
ATOM   14151 C  CB    . TRP   F 2  21  ? 14.967  68.396  19.619  1.00 30.29  ? 21  TRP   B CB    1 
ATOM   14152 C  CG    . TRP   F 2  21  ? 16.344  68.208  20.149  1.00 24.73  ? 21  TRP   B CG    1 
ATOM   14153 C  CD1   . TRP   F 2  21  ? 17.095  67.083  20.108  1.00 24.63  ? 21  TRP   B CD1   1 
ATOM   14154 C  CD2   . TRP   F 2  21  ? 17.097  69.170  20.880  1.00 26.31  ? 21  TRP   B CD2   1 
ATOM   14155 N  NE1   . TRP   F 2  21  ? 18.285  67.282  20.755  1.00 24.17  ? 21  TRP   B NE1   1 
ATOM   14156 C  CE2   . TRP   F 2  21  ? 18.314  68.566  21.231  1.00 30.76  ? 21  TRP   B CE2   1 
ATOM   14157 C  CE3   . TRP   F 2  21  ? 16.868  70.497  21.257  1.00 32.82  ? 21  TRP   B CE3   1 
ATOM   14158 C  CZ2   . TRP   F 2  21  ? 19.311  69.250  21.943  1.00 33.89  ? 21  TRP   B CZ2   1 
ATOM   14159 C  CZ3   . TRP   F 2  21  ? 17.853  71.172  21.968  1.00 32.16  ? 21  TRP   B CZ3   1 
ATOM   14160 C  CH2   . TRP   F 2  21  ? 19.054  70.548  22.305  1.00 28.63  ? 21  TRP   B CH2   1 
ATOM   14161 N  N     . GLU   F 2  22  ? 11.820  68.926  19.721  1.00 27.42  ? 22  GLU   B N     1 
ATOM   14162 C  CA    . GLU   F 2  22  ? 10.715  69.791  19.358  1.00 28.92  ? 22  GLU   B CA    1 
ATOM   14163 C  C     . GLU   F 2  22  ? 9.897   70.192  20.585  1.00 30.72  ? 22  GLU   B C     1 
ATOM   14164 O  O     . GLU   F 2  22  ? 9.350   71.301  20.616  1.00 35.45  ? 22  GLU   B O     1 
ATOM   14165 C  CB    . GLU   F 2  22  ? 9.855   69.110  18.298  1.00 33.69  ? 22  GLU   B CB    1 
ATOM   14166 C  CG    . GLU   F 2  22  ? 8.959   68.023  18.817  1.00 39.66  ? 22  GLU   B CG    1 
ATOM   14167 C  CD    . GLU   F 2  22  ? 7.929   67.577  17.785  1.00 50.47  ? 22  GLU   B CD    1 
ATOM   14168 O  OE1   . GLU   F 2  22  ? 8.340   67.089  16.698  1.00 42.23  ? 22  GLU   B OE1   1 
ATOM   14169 O  OE2   . GLU   F 2  22  ? 6.713   67.713  18.076  1.00 55.09  ? 22  GLU   B OE2   1 
ATOM   14170 N  N     . VAL   F 2  23  ? 9.830   69.324  21.608  1.00 37.47  ? 23  VAL   B N     1 
ATOM   14171 C  CA    . VAL   F 2  23  ? 9.089   69.630  22.834  1.00 28.65  ? 23  VAL   B CA    1 
ATOM   14172 C  C     . VAL   F 2  23  ? 9.801   70.696  23.646  1.00 32.65  ? 23  VAL   B C     1 
ATOM   14173 O  O     . VAL   F 2  23  ? 9.170   71.643  24.132  1.00 32.59  ? 23  VAL   B O     1 
ATOM   14174 C  CB    . VAL   F 2  23  ? 8.893   68.388  23.714  1.00 27.70  ? 23  VAL   B CB    1 
ATOM   14175 C  CG1   . VAL   F 2  23  ? 8.188   68.842  24.965  1.00 30.43  ? 23  VAL   B CG1   1 
ATOM   14176 C  CG2   . VAL   F 2  23  ? 8.116   67.300  23.018  1.00 27.16  ? 23  VAL   B CG2   1 
ATOM   14177 N  N     . ILE   F 2  24  ? 11.105  70.507  23.892  1.00 29.25  ? 24  ILE   B N     1 
ATOM   14178 C  CA    . ILE   F 2  24  ? 11.820  71.512  24.680  1.00 34.53  ? 24  ILE   B CA    1 
ATOM   14179 C  C     . ILE   F 2  24  ? 12.023  72.779  23.857  1.00 35.78  ? 24  ILE   B C     1 
ATOM   14180 O  O     . ILE   F 2  24  ? 12.092  73.883  24.412  1.00 38.92  ? 24  ILE   B O     1 
ATOM   14181 C  CB    . ILE   F 2  24  ? 13.171  70.998  25.235  1.00 28.87  ? 24  ILE   B CB    1 
ATOM   14182 C  CG1   . ILE   F 2  24  ? 14.092  70.542  24.110  1.00 31.77  ? 24  ILE   B CG1   1 
ATOM   14183 C  CG2   . ILE   F 2  24  ? 12.998  69.945  26.320  1.00 21.35  ? 24  ILE   B CG2   1 
ATOM   14184 C  CD1   . ILE   F 2  24  ? 15.579  70.650  24.472  1.00 32.35  ? 24  ILE   B CD1   1 
ATOM   14185 N  N     . SER   F 2  25  ? 12.126  72.655  22.535  1.00 33.03  ? 25  SER   B N     1 
ATOM   14186 C  CA    . SER   F 2  25  ? 12.265  73.849  21.715  1.00 32.45  ? 25  SER   B CA    1 
ATOM   14187 C  C     . SER   F 2  25  ? 11.036  74.732  21.843  1.00 36.66  ? 25  SER   B C     1 
ATOM   14188 O  O     . SER   F 2  25  ? 11.146  75.959  21.933  1.00 44.51  ? 25  SER   B O     1 
ATOM   14189 C  CB    . SER   F 2  25  ? 12.516  73.468  20.259  1.00 37.04  ? 25  SER   B CB    1 
ATOM   14190 O  OG    . SER   F 2  25  ? 13.893  73.592  19.936  1.00 41.49  ? 25  SER   B OG    1 
ATOM   14191 N  N     . ASP   F 2  26  ? 9.853   74.130  21.865  1.00 34.16  ? 26  ASP   B N     1 
ATOM   14192 C  CA    . ASP   F 2  26  ? 8.655   74.897  22.181  1.00 32.97  ? 26  ASP   B CA    1 
ATOM   14193 C  C     . ASP   F 2  26  ? 8.768   75.501  23.581  1.00 38.37  ? 26  ASP   B C     1 
ATOM   14194 O  O     . ASP   F 2  26  ? 8.748   76.724  23.749  1.00 35.41  ? 26  ASP   B O     1 
ATOM   14195 C  CB    . ASP   F 2  26  ? 7.429   73.994  22.038  1.00 26.67  ? 26  ASP   B CB    1 
ATOM   14196 C  CG    . ASP   F 2  26  ? 6.149   74.644  22.507  1.00 51.04  ? 26  ASP   B CG    1 
ATOM   14197 O  OD1   . ASP   F 2  26  ? 6.152   75.844  22.839  1.00 70.97  ? 26  ASP   B OD1   1 
ATOM   14198 O  OD2   . ASP   F 2  26  ? 5.119   73.939  22.547  1.00 64.96  ? 26  ASP   B OD2   1 
ATOM   14199 N  N     . GLU   F 2  27  ? 8.949   74.649  24.597  1.00 43.21  ? 27  GLU   B N     1 
ATOM   14200 C  CA    . GLU   F 2  27  ? 9.119   75.079  25.981  1.00 35.71  ? 27  GLU   B CA    1 
ATOM   14201 C  C     . GLU   F 2  27  ? 10.003  76.320  26.103  1.00 37.67  ? 27  GLU   B C     1 
ATOM   14202 O  O     . GLU   F 2  27  ? 9.698   77.228  26.882  1.00 37.12  ? 27  GLU   B O     1 
ATOM   14203 C  CB    . GLU   F 2  27  ? 9.706   73.940  26.814  1.00 25.48  ? 27  GLU   B CB    1 
ATOM   14204 C  CG    . GLU   F 2  27  ? 8.786   72.775  27.024  1.00 20.78  ? 27  GLU   B CG    1 
ATOM   14205 C  CD    . GLU   F 2  27  ? 9.014   72.082  28.366  1.00 28.03  ? 27  GLU   B CD    1 
ATOM   14206 O  OE1   . GLU   F 2  27  ? 10.049  72.325  29.017  1.00 27.05  ? 27  GLU   B OE1   1 
ATOM   14207 O  OE2   . GLU   F 2  27  ? 8.149   71.301  28.794  1.00 33.02  ? 27  GLU   B OE2   1 
ATOM   14208 N  N     . HIS   F 2  28  ? 11.096  76.362  25.342  1.00 27.27  ? 28  HIS   B N     1 
ATOM   14209 C  CA    . HIS   F 2  28  ? 12.052  77.452  25.382  1.00 25.60  ? 28  HIS   B CA    1 
ATOM   14210 C  C     . HIS   F 2  28  ? 11.773  78.529  24.344  1.00 41.90  ? 28  HIS   B C     1 
ATOM   14211 O  O     . HIS   F 2  28  ? 12.525  79.506  24.265  1.00 39.19  ? 28  HIS   B O     1 
ATOM   14212 C  CB    . HIS   F 2  28  ? 13.460  76.912  25.187  1.00 23.76  ? 28  HIS   B CB    1 
ATOM   14213 C  CG    . HIS   F 2  28  ? 14.016  76.242  26.402  1.00 29.01  ? 28  HIS   B CG    1 
ATOM   14214 N  ND1   . HIS   F 2  28  ? 14.457  76.945  27.502  1.00 33.97  ? 28  HIS   B ND1   1 
ATOM   14215 C  CD2   . HIS   F 2  28  ? 14.198  74.934  26.697  1.00 28.60  ? 28  HIS   B CD2   1 
ATOM   14216 C  CE1   . HIS   F 2  28  ? 14.891  76.104  28.422  1.00 30.09  ? 28  HIS   B CE1   1 
ATOM   14217 N  NE2   . HIS   F 2  28  ? 14.741  74.876  27.960  1.00 38.91  ? 28  HIS   B NE2   1 
ATOM   14218 N  N     . GLY   F 2  29  ? 10.728  78.372  23.536  1.00 40.65  ? 29  GLY   B N     1 
ATOM   14219 C  CA    . GLY   F 2  29  ? 10.332  79.405  22.605  1.00 38.00  ? 29  GLY   B CA    1 
ATOM   14220 C  C     . GLY   F 2  29  ? 11.089  79.435  21.295  1.00 42.43  ? 29  GLY   B C     1 
ATOM   14221 O  O     . GLY   F 2  29  ? 10.878  80.354  20.492  1.00 49.55  ? 29  GLY   B O     1 
ATOM   14222 N  N     . ILE   F 2  30  ? 11.956  78.472  21.050  1.00 37.17  ? 30  ILE   B N     1 
ATOM   14223 C  CA    . ILE   F 2  30  ? 12.689  78.417  19.791  1.00 43.93  ? 30  ILE   B CA    1 
ATOM   14224 C  C     . ILE   F 2  30  ? 11.811  77.820  18.701  1.00 43.32  ? 30  ILE   B C     1 
ATOM   14225 O  O     . ILE   F 2  30  ? 11.134  76.796  18.906  1.00 38.55  ? 30  ILE   B O     1 
ATOM   14226 C  CB    . ILE   F 2  30  ? 13.987  77.614  19.957  1.00 39.06  ? 30  ILE   B CB    1 
ATOM   14227 C  CG1   . ILE   F 2  30  ? 14.740  78.094  21.203  1.00 42.91  ? 30  ILE   B CG1   1 
ATOM   14228 C  CG2   . ILE   F 2  30  ? 14.830  77.741  18.698  1.00 46.02  ? 30  ILE   B CG2   1 
ATOM   14229 C  CD1   . ILE   F 2  30  ? 14.707  79.608  21.389  1.00 46.67  ? 30  ILE   B CD1   1 
ATOM   14230 N  N     . ASP   F 2  31  ? 11.828  78.461  17.536  1.00 45.25  ? 31  ASP   B N     1 
ATOM   14231 C  CA    . ASP   F 2  31  ? 10.982  78.067  16.420  1.00 49.52  ? 31  ASP   B CA    1 
ATOM   14232 C  C     . ASP   F 2  31  ? 11.756  77.151  15.492  1.00 51.05  ? 31  ASP   B C     1 
ATOM   14233 O  O     . ASP   F 2  31  ? 12.983  77.037  15.575  1.00 47.24  ? 31  ASP   B O     1 
ATOM   14234 C  CB    . ASP   F 2  31  ? 10.421  79.313  15.710  1.00 44.17  ? 31  ASP   B CB    1 
ATOM   14235 C  CG    . ASP   F 2  31  ? 11.431  80.033  14.794  1.00 47.93  ? 31  ASP   B CG    1 
ATOM   14236 O  OD1   . ASP   F 2  31  ? 12.576  80.342  15.196  1.00 53.08  ? 31  ASP   B OD1   1 
ATOM   14237 O  OD2   . ASP   F 2  31  ? 11.048  80.358  13.662  1.00 52.00  ? 31  ASP   B OD2   1 
ATOM   14238 N  N     . PRO   F 2  32  ? 11.066  76.460  14.602  1.00 41.75  ? 32  PRO   B N     1 
ATOM   14239 C  CA    . PRO   F 2  32  ? 11.733  75.407  13.839  1.00 39.71  ? 32  PRO   B CA    1 
ATOM   14240 C  C     . PRO   F 2  32  ? 12.881  75.935  13.005  1.00 45.71  ? 32  PRO   B C     1 
ATOM   14241 O  O     . PRO   F 2  32  ? 13.451  75.180  12.214  1.00 57.20  ? 32  PRO   B O     1 
ATOM   14242 C  CB    . PRO   F 2  32  ? 10.610  74.813  12.970  1.00 39.77  ? 32  PRO   B CB    1 
ATOM   14243 C  CG    . PRO   F 2  32  ? 9.421   75.676  13.160  1.00 41.78  ? 32  PRO   B CG    1 
ATOM   14244 C  CD    . PRO   F 2  32  ? 9.609   76.453  14.413  1.00 43.91  ? 32  PRO   B CD    1 
ATOM   14245 N  N     . THR   F 2  33  ? 13.245  77.211  13.175  1.00 49.01  ? 33  THR   B N     1 
ATOM   14246 C  CA    . THR   F 2  33  ? 14.367  77.801  12.454  1.00 50.06  ? 33  THR   B CA    1 
ATOM   14247 C  C     . THR   F 2  33  ? 15.520  78.204  13.361  1.00 56.58  ? 33  THR   B C     1 
ATOM   14248 O  O     . THR   F 2  33  ? 16.580  78.585  12.850  1.00 57.29  ? 33  THR   B O     1 
ATOM   14249 C  CB    . THR   F 2  33  ? 13.927  79.041  11.665  1.00 42.81  ? 33  THR   B CB    1 
ATOM   14250 O  OG1   . THR   F 2  33  ? 13.988  80.183  12.526  1.00 49.97  ? 33  THR   B OG1   1 
ATOM   14251 C  CG2   . THR   F 2  33  ? 12.508  78.892  11.144  1.00 43.03  ? 33  THR   B CG2   1 
ATOM   14252 N  N     . GLY   F 2  34  ? 15.336  78.162  14.678  1.00 57.65  ? 34  GLY   B N     1 
ATOM   14253 C  CA    . GLY   F 2  34  ? 16.384  78.507  15.618  1.00 52.77  ? 34  GLY   B CA    1 
ATOM   14254 C  C     . GLY   F 2  34  ? 16.342  79.909  16.190  1.00 51.21  ? 34  GLY   B C     1 
ATOM   14255 O  O     . GLY   F 2  34  ? 17.373  80.392  16.669  1.00 60.80  ? 34  GLY   B O     1 
ATOM   14256 N  N     . SER   F 2  35  ? 15.196  80.577  16.166  1.00 53.83  ? 35  SER   B N     1 
ATOM   14257 C  CA    . SER   F 2  35  ? 15.108  81.965  16.593  1.00 60.23  ? 35  SER   B CA    1 
ATOM   14258 C  C     . SER   F 2  35  ? 14.121  82.082  17.748  1.00 53.72  ? 35  SER   B C     1 
ATOM   14259 O  O     . SER   F 2  35  ? 13.061  81.452  17.737  1.00 48.36  ? 35  SER   B O     1 
ATOM   14260 C  CB    . SER   F 2  35  ? 14.708  82.864  15.415  1.00 60.35  ? 35  SER   B CB    1 
ATOM   14261 O  OG    . SER   F 2  35  ? 15.717  82.833  14.406  1.00 68.27  ? 35  SER   B OG    1 
ATOM   14262 N  N     . TYR   F 2  36  ? 14.481  82.870  18.760  1.00 58.41  ? 36  TYR   B N     1 
ATOM   14263 C  CA    . TYR   F 2  36  ? 13.665  82.932  19.962  1.00 54.18  ? 36  TYR   B CA    1 
ATOM   14264 C  C     . TYR   F 2  36  ? 12.415  83.761  19.719  1.00 48.49  ? 36  TYR   B C     1 
ATOM   14265 O  O     . TYR   F 2  36  ? 12.478  84.846  19.146  1.00 52.06  ? 36  TYR   B O     1 
ATOM   14266 C  CB    . TYR   F 2  36  ? 14.455  83.514  21.138  1.00 58.62  ? 36  TYR   B CB    1 
ATOM   14267 C  CG    . TYR   F 2  36  ? 13.593  83.713  22.373  1.00 52.56  ? 36  TYR   B CG    1 
ATOM   14268 C  CD1   . TYR   F 2  36  ? 12.841  82.672  22.888  1.00 49.30  ? 36  TYR   B CD1   1 
ATOM   14269 C  CD2   . TYR   F 2  36  ? 13.521  84.934  23.007  1.00 47.80  ? 36  TYR   B CD2   1 
ATOM   14270 C  CE1   . TYR   F 2  36  ? 12.043  82.844  23.982  1.00 45.38  ? 36  TYR   B CE1   1 
ATOM   14271 C  CE2   . TYR   F 2  36  ? 12.724  85.108  24.104  1.00 51.99  ? 36  TYR   B CE2   1 
ATOM   14272 C  CZ    . TYR   F 2  36  ? 11.982  84.059  24.582  1.00 51.43  ? 36  TYR   B CZ    1 
ATOM   14273 O  OH    . TYR   F 2  36  ? 11.182  84.223  25.690  1.00 59.08  ? 36  TYR   B OH    1 
ATOM   14274 N  N     . HIS   F 2  37  ? 11.271  83.248  20.173  1.00 53.25  ? 37  HIS   B N     1 
ATOM   14275 C  CA    . HIS   F 2  37  ? 10.029  83.991  20.023  1.00 54.92  ? 37  HIS   B CA    1 
ATOM   14276 C  C     . HIS   F 2  37  ? 9.111   83.837  21.221  1.00 54.59  ? 37  HIS   B C     1 
ATOM   14277 O  O     . HIS   F 2  37  ? 7.888   83.824  21.065  1.00 69.98  ? 37  HIS   B O     1 
ATOM   14278 C  CB    . HIS   F 2  37  ? 9.300   83.581  18.752  1.00 59.84  ? 37  HIS   B CB    1 
ATOM   14279 C  CG    . HIS   F 2  37  ? 9.852   84.242  17.535  1.00 65.71  ? 37  HIS   B CG    1 
ATOM   14280 N  ND1   . HIS   F 2  37  ? 10.657  83.584  16.634  1.00 68.21  ? 37  HIS   B ND1   1 
ATOM   14281 C  CD2   . HIS   F 2  37  ? 9.771   85.522  17.105  1.00 63.19  ? 37  HIS   B CD2   1 
ATOM   14282 C  CE1   . HIS   F 2  37  ? 11.022  84.421  15.679  1.00 73.46  ? 37  HIS   B CE1   1 
ATOM   14283 N  NE2   . HIS   F 2  37  ? 10.498  85.604  15.944  1.00 74.92  ? 37  HIS   B NE2   1 
ATOM   14284 N  N     . GLY   F 2  38  ? 9.669   83.753  22.426  1.00 51.54  ? 38  GLY   B N     1 
ATOM   14285 C  CA    . GLY   F 2  38  ? 8.879   83.635  23.630  1.00 52.14  ? 38  GLY   B CA    1 
ATOM   14286 C  C     . GLY   F 2  38  ? 8.703   84.963  24.339  1.00 53.15  ? 38  GLY   B C     1 
ATOM   14287 O  O     . GLY   F 2  38  ? 8.995   86.035  23.806  1.00 46.93  ? 38  GLY   B O     1 
ATOM   14288 N  N     . ASP   F 2  39  ? 8.218   84.872  25.578  1.00 56.65  ? 39  ASP   B N     1 
ATOM   14289 C  CA    . ASP   F 2  39  ? 8.106   86.015  26.475  1.00 49.67  ? 39  ASP   B CA    1 
ATOM   14290 C  C     . ASP   F 2  39  ? 9.061   85.873  27.654  1.00 58.02  ? 39  ASP   B C     1 
ATOM   14291 O  O     . ASP   F 2  39  ? 10.169  86.419  27.623  1.00 70.90  ? 39  ASP   B O     1 
ATOM   14292 C  CB    . ASP   F 2  39  ? 6.670   86.159  26.965  1.00 46.72  ? 39  ASP   B CB    1 
ATOM   14293 C  CG    . ASP   F 2  39  ? 5.874   84.906  26.759  1.00 59.76  ? 39  ASP   B CG    1 
ATOM   14294 O  OD1   . ASP   F 2  39  ? 6.079   83.948  27.534  1.00 71.26  ? 39  ASP   B OD1   1 
ATOM   14295 O  OD2   . ASP   F 2  39  ? 5.064   84.861  25.808  1.00 55.10  ? 39  ASP   B OD2   1 
ATOM   14296 N  N     . SER   F 2  40  ? 8.640   85.143  28.687  1.00 52.10  ? 40  SER   B N     1 
ATOM   14297 C  CA    . SER   F 2  40  ? 9.432   84.912  29.892  1.00 54.69  ? 40  SER   B CA    1 
ATOM   14298 C  C     . SER   F 2  40  ? 10.917  84.753  29.593  1.00 58.46  ? 40  SER   B C     1 
ATOM   14299 O  O     . SER   F 2  40  ? 11.319  83.894  28.804  1.00 59.77  ? 40  SER   B O     1 
ATOM   14300 C  CB    . SER   F 2  40  ? 8.916   83.660  30.610  1.00 63.21  ? 40  SER   B CB    1 
ATOM   14301 O  OG    . SER   F 2  40  ? 9.827   83.199  31.605  1.00 60.56  ? 40  SER   B OG    1 
ATOM   14302 N  N     . ASP   F 2  41  ? 11.745  85.574  30.234  1.00 62.47  ? 41  ASP   B N     1 
ATOM   14303 C  CA    . ASP   F 2  41  ? 13.183  85.371  30.119  1.00 60.08  ? 41  ASP   B CA    1 
ATOM   14304 C  C     . ASP   F 2  41  ? 13.640  84.089  30.813  1.00 62.12  ? 41  ASP   B C     1 
ATOM   14305 O  O     . ASP   F 2  41  ? 14.820  83.721  30.695  1.00 51.24  ? 41  ASP   B O     1 
ATOM   14306 C  CB    . ASP   F 2  41  ? 13.901  86.602  30.672  1.00 62.75  ? 41  ASP   B CB    1 
ATOM   14307 C  CG    . ASP   F 2  41  ? 13.426  87.896  30.009  1.00 71.95  ? 41  ASP   B CG    1 
ATOM   14308 O  OD1   . ASP   F 2  41  ? 13.807  88.142  28.841  1.00 72.88  ? 41  ASP   B OD1   1 
ATOM   14309 O  OD2   . ASP   F 2  41  ? 12.643  88.651  30.637  1.00 68.63  ? 41  ASP   B OD2   1 
ATOM   14310 N  N     . LEU   F 2  42  ? 12.726  83.406  31.527  1.00 58.47  ? 42  LEU   B N     1 
ATOM   14311 C  CA    . LEU   F 2  42  ? 13.020  82.087  32.081  1.00 53.80  ? 42  LEU   B CA    1 
ATOM   14312 C  C     . LEU   F 2  42  ? 13.273  81.076  30.982  1.00 47.61  ? 42  LEU   B C     1 
ATOM   14313 O  O     . LEU   F 2  42  ? 14.021  80.108  31.185  1.00 47.98  ? 42  LEU   B O     1 
ATOM   14314 C  CB    . LEU   F 2  42  ? 11.867  81.600  32.963  1.00 59.82  ? 42  LEU   B CB    1 
ATOM   14315 C  CG    . LEU   F 2  42  ? 11.690  82.226  34.345  1.00 55.31  ? 42  LEU   B CG    1 
ATOM   14316 C  CD1   . LEU   F 2  42  ? 10.986  83.556  34.201  1.00 67.24  ? 42  LEU   B CD1   1 
ATOM   14317 C  CD2   . LEU   F 2  42  ? 10.917  81.278  35.276  1.00 46.25  ? 42  LEU   B CD2   1 
ATOM   14318 N  N     . GLN   F 2  43  ? 12.640  81.281  29.822  1.00 46.55  ? 45  GLN   B N     1 
ATOM   14319 C  CA    . GLN   F 2  43  ? 12.924  80.477  28.639  1.00 39.96  ? 45  GLN   B CA    1 
ATOM   14320 C  C     . GLN   F 2  43  ? 14.388  80.597  28.229  1.00 42.81  ? 45  GLN   B C     1 
ATOM   14321 O  O     . GLN   F 2  43  ? 15.063  79.592  27.982  1.00 45.28  ? 45  GLN   B O     1 
ATOM   14322 C  CB    . GLN   F 2  43  ? 12.016  80.907  27.485  1.00 42.22  ? 45  GLN   B CB    1 
ATOM   14323 C  CG    . GLN   F 2  43  ? 10.526  80.714  27.737  1.00 38.99  ? 45  GLN   B CG    1 
ATOM   14324 C  CD    . GLN   F 2  43  ? 9.656   81.199  26.584  1.00 46.73  ? 45  GLN   B CD    1 
ATOM   14325 O  OE1   . GLN   F 2  43  ? 9.600   82.389  26.272  1.00 51.20  ? 45  GLN   B OE1   1 
ATOM   14326 N  NE2   . GLN   F 2  43  ? 8.966   80.271  25.951  1.00 53.04  ? 45  GLN   B NE2   1 
ATOM   14327 N  N     . LEU   F 2  44  ? 14.901  81.823  28.137  1.00 49.94  ? 46  LEU   B N     1 
ATOM   14328 C  CA    . LEU   F 2  44  ? 16.269  81.997  27.661  1.00 43.31  ? 46  LEU   B CA    1 
ATOM   14329 C  C     . LEU   F 2  44  ? 17.305  81.867  28.758  1.00 36.30  ? 46  LEU   B C     1 
ATOM   14330 O  O     . LEU   F 2  44  ? 18.475  81.626  28.450  1.00 35.75  ? 46  LEU   B O     1 
ATOM   14331 C  CB    . LEU   F 2  44  ? 16.434  83.359  26.992  1.00 46.95  ? 46  LEU   B CB    1 
ATOM   14332 C  CG    . LEU   F 2  44  ? 15.903  83.376  25.573  1.00 43.74  ? 46  LEU   B CG    1 
ATOM   14333 C  CD1   . LEU   F 2  44  ? 16.668  84.406  24.808  1.00 56.45  ? 46  LEU   B CD1   1 
ATOM   14334 C  CD2   . LEU   F 2  44  ? 16.114  82.007  24.988  1.00 44.47  ? 46  LEU   B CD2   1 
ATOM   14335 N  N     . GLU   F 2  45  ? 16.902  82.020  30.022  1.00 39.57  ? 47  GLU   B N     1 
ATOM   14336 C  CA    . GLU   F 2  45  ? 17.877  82.181  31.092  1.00 37.43  ? 47  GLU   B CA    1 
ATOM   14337 C  C     . GLU   F 2  45  ? 18.836  81.001  31.187  1.00 44.66  ? 47  GLU   B C     1 
ATOM   14338 O  O     . GLU   F 2  45  ? 20.002  81.191  31.555  1.00 43.34  ? 47  GLU   B O     1 
ATOM   14339 C  CB    . GLU   F 2  45  ? 17.167  82.399  32.422  1.00 47.95  ? 47  GLU   B CB    1 
ATOM   14340 C  CG    . GLU   F 2  45  ? 18.109  82.468  33.611  1.00 46.90  ? 47  GLU   B CG    1 
ATOM   14341 C  CD    . GLU   F 2  45  ? 17.462  83.135  34.803  1.00 60.44  ? 47  GLU   B CD    1 
ATOM   14342 O  OE1   . GLU   F 2  45  ? 18.188  83.505  35.752  1.00 62.51  ? 47  GLU   B OE1   1 
ATOM   14343 O  OE2   . GLU   F 2  45  ? 16.222  83.293  34.786  1.00 68.28  ? 47  GLU   B OE2   1 
ATOM   14344 N  N     . ARG   F 2  46  ? 18.387  79.779  30.872  1.00 42.93  ? 48  ARG   B N     1 
ATOM   14345 C  CA    . ARG   F 2  46  ? 19.298  78.635  30.862  1.00 36.43  ? 48  ARG   B CA    1 
ATOM   14346 C  C     . ARG   F 2  46  ? 19.375  77.967  29.489  1.00 44.81  ? 48  ARG   B C     1 
ATOM   14347 O  O     . ARG   F 2  46  ? 19.835  76.818  29.373  1.00 37.92  ? 48  ARG   B O     1 
ATOM   14348 C  CB    . ARG   F 2  46  ? 18.894  77.619  31.921  1.00 31.57  ? 48  ARG   B CB    1 
ATOM   14349 C  CG    . ARG   F 2  46  ? 18.834  78.191  33.294  1.00 29.84  ? 48  ARG   B CG    1 
ATOM   14350 C  CD    . ARG   F 2  46  ? 19.829  77.486  34.149  1.00 34.59  ? 48  ARG   B CD    1 
ATOM   14351 N  NE    . ARG   F 2  46  ? 19.267  76.345  34.862  1.00 32.86  ? 48  ARG   B NE    1 
ATOM   14352 C  CZ    . ARG   F 2  46  ? 19.982  75.295  35.254  1.00 36.89  ? 48  ARG   B CZ    1 
ATOM   14353 N  NH1   . ARG   F 2  46  ? 21.257  75.156  34.908  1.00 39.94  ? 48  ARG   B NH1   1 
ATOM   14354 N  NH2   . ARG   F 2  46  ? 19.407  74.361  36.012  1.00 33.30  ? 48  ARG   B NH2   1 
ATOM   14355 N  N     . ILE   F 2  47  ? 18.968  78.680  28.435  1.00 44.62  ? 49  ILE   B N     1 
ATOM   14356 C  CA    . ILE   F 2  47  ? 18.877  78.097  27.103  1.00 37.33  ? 49  ILE   B CA    1 
ATOM   14357 C  C     . ILE   F 2  47  ? 20.175  77.447  26.655  1.00 40.78  ? 49  ILE   B C     1 
ATOM   14358 O  O     . ILE   F 2  47  ? 20.145  76.556  25.801  1.00 40.54  ? 49  ILE   B O     1 
ATOM   14359 C  CB    . ILE   F 2  47  ? 18.426  79.176  26.106  1.00 38.92  ? 49  ILE   B CB    1 
ATOM   14360 C  CG1   . ILE   F 2  47  ? 17.828  78.538  24.863  1.00 37.23  ? 49  ILE   B CG1   1 
ATOM   14361 C  CG2   . ILE   F 2  47  ? 19.574  80.096  25.770  1.00 33.84  ? 49  ILE   B CG2   1 
ATOM   14362 C  CD1   . ILE   F 2  47  ? 16.565  77.839  25.159  1.00 34.94  ? 49  ILE   B CD1   1 
ATOM   14363 N  N     . ASN   F 2  48  ? 21.316  77.843  27.215  1.00 36.30  ? 50  ASN   B N     1 
ATOM   14364 C  CA    . ASN   F 2  48  ? 22.584  77.353  26.691  1.00 38.14  ? 50  ASN   B CA    1 
ATOM   14365 C  C     . ASN   F 2  48  ? 23.027  76.047  27.328  1.00 36.47  ? 50  ASN   B C     1 
ATOM   14366 O  O     . ASN   F 2  48  ? 24.088  75.536  26.963  1.00 36.16  ? 50  ASN   B O     1 
ATOM   14367 C  CB    . ASN   F 2  48  ? 23.685  78.418  26.835  1.00 52.31  ? 50  ASN   B CB    1 
ATOM   14368 C  CG    . ASN   F 2  48  ? 23.730  79.398  25.630  1.00 58.43  ? 50  ASN   B CG    1 
ATOM   14369 O  OD1   . ASN   F 2  48  ? 24.381  79.134  24.606  1.00 56.59  ? 50  ASN   B OD1   1 
ATOM   14370 N  ND2   . ASN   F 2  48  ? 23.031  80.531  25.762  1.00 47.26  ? 50  ASN   B ND2   1 
ATOM   14371 N  N     . VAL   F 2  49  ? 22.249  75.499  28.267  1.00 40.34  ? 51  VAL   B N     1 
ATOM   14372 C  CA    . VAL   F 2  49  ? 22.456  74.125  28.731  1.00 33.18  ? 51  VAL   B CA    1 
ATOM   14373 C  C     . VAL   F 2  49  ? 22.247  73.139  27.582  1.00 37.82  ? 51  VAL   B C     1 
ATOM   14374 O  O     . VAL   F 2  49  ? 22.992  72.156  27.432  1.00 31.44  ? 51  VAL   B O     1 
ATOM   14375 C  CB    . VAL   F 2  49  ? 21.501  73.818  29.898  1.00 28.89  ? 51  VAL   B CB    1 
ATOM   14376 C  CG1   . VAL   F 2  49  ? 21.823  72.482  30.520  1.00 33.66  ? 51  VAL   B CG1   1 
ATOM   14377 C  CG2   . VAL   F 2  49  ? 21.503  74.943  30.922  1.00 31.55  ? 51  VAL   B CG2   1 
ATOM   14378 N  N     . TYR   F 2  50  ? 21.216  73.381  26.757  1.00 31.62  ? 52  TYR   B N     1 
ATOM   14379 C  CA    . TYR   F 2  50  ? 20.922  72.525  25.626  1.00 28.23  ? 52  TYR   B CA    1 
ATOM   14380 C  C     . TYR   F 2  50  ? 21.085  73.189  24.256  1.00 35.41  ? 52  TYR   B C     1 
ATOM   14381 O  O     . TYR   F 2  50  ? 21.182  72.462  23.266  1.00 39.40  ? 52  TYR   B O     1 
ATOM   14382 C  CB    . TYR   F 2  50  ? 19.502  71.947  25.748  1.00 22.67  ? 52  TYR   B CB    1 
ATOM   14383 C  CG    . TYR   F 2  50  ? 19.368  70.766  26.702  1.00 28.70  ? 52  TYR   B CG    1 
ATOM   14384 C  CD1   . TYR   F 2  50  ? 19.740  69.476  26.318  1.00 24.90  ? 52  TYR   B CD1   1 
ATOM   14385 C  CD2   . TYR   F 2  50  ? 18.843  70.935  27.981  1.00 29.50  ? 52  TYR   B CD2   1 
ATOM   14386 C  CE1   . TYR   F 2  50  ? 19.604  68.399  27.188  1.00 23.20  ? 52  TYR   B CE1   1 
ATOM   14387 C  CE2   . TYR   F 2  50  ? 18.721  69.867  28.865  1.00 23.20  ? 52  TYR   B CE2   1 
ATOM   14388 C  CZ    . TYR   F 2  50  ? 19.094  68.599  28.466  1.00 25.87  ? 52  TYR   B CZ    1 
ATOM   14389 O  OH    . TYR   F 2  50  ? 18.958  67.546  29.347  1.00 18.67  ? 52  TYR   B OH    1 
ATOM   14390 N  N     . TYR   F 2  51  ? 21.156  74.520  24.154  1.00 36.62  ? 53  TYR   B N     1 
ATOM   14391 C  CA    . TYR   F 2  51  ? 21.302  75.159  22.842  1.00 38.25  ? 53  TYR   B CA    1 
ATOM   14392 C  C     . TYR   F 2  51  ? 22.623  75.923  22.709  1.00 43.93  ? 53  TYR   B C     1 
ATOM   14393 O  O     . TYR   F 2  51  ? 23.338  76.167  23.685  1.00 45.63  ? 53  TYR   B O     1 
ATOM   14394 C  CB    . TYR   F 2  51  ? 20.129  76.095  22.555  1.00 34.42  ? 53  TYR   B CB    1 
ATOM   14395 C  CG    . TYR   F 2  51  ? 18.806  75.388  22.431  1.00 38.71  ? 53  TYR   B CG    1 
ATOM   14396 C  CD1   . TYR   F 2  51  ? 18.099  74.990  23.564  1.00 37.61  ? 53  TYR   B CD1   1 
ATOM   14397 C  CD2   . TYR   F 2  51  ? 18.250  75.119  21.182  1.00 39.47  ? 53  TYR   B CD2   1 
ATOM   14398 C  CE1   . TYR   F 2  51  ? 16.872  74.334  23.457  1.00 33.95  ? 53  TYR   B CE1   1 
ATOM   14399 C  CE2   . TYR   F 2  51  ? 17.014  74.464  21.064  1.00 34.17  ? 53  TYR   B CE2   1 
ATOM   14400 C  CZ    . TYR   F 2  51  ? 16.336  74.081  22.204  1.00 36.96  ? 53  TYR   B CZ    1 
ATOM   14401 O  OH    . TYR   F 2  51  ? 15.122  73.449  22.094  1.00 39.47  ? 53  TYR   B OH    1 
ATOM   14402 N  N     . ASN   F 2  52  ? 22.949  76.304  21.470  1.00 45.07  ? 54  ASN   B N     1 
ATOM   14403 C  CA    . ASN   F 2  52  ? 24.197  76.994  21.165  1.00 45.33  ? 54  ASN   B CA    1 
ATOM   14404 C  C     . ASN   F 2  52  ? 23.910  78.322  20.491  1.00 48.56  ? 54  ASN   B C     1 
ATOM   14405 O  O     . ASN   F 2  52  ? 22.946  78.454  19.733  1.00 51.15  ? 54  ASN   B O     1 
ATOM   14406 C  CB    . ASN   F 2  52  ? 25.087  76.169  20.259  1.00 41.40  ? 54  ASN   B CB    1 
ATOM   14407 C  CG    . ASN   F 2  52  ? 26.372  75.804  20.918  1.00 48.77  ? 54  ASN   B CG    1 
ATOM   14408 O  OD1   . ASN   F 2  52  ? 26.946  76.613  21.655  1.00 60.56  ? 54  ASN   B OD1   1 
ATOM   14409 N  ND2   . ASN   F 2  52  ? 26.837  74.579  20.685  1.00 42.34  ? 54  ASN   B ND2   1 
ATOM   14410 N  N     . GLU   F 2  53  ? 24.771  79.300  20.754  1.00 58.76  ? 55  GLU   B N     1 
ATOM   14411 C  CA    . GLU   F 2  53  ? 24.553  80.668  20.287  1.00 63.77  ? 55  GLU   B CA    1 
ATOM   14412 C  C     . GLU   F 2  53  ? 25.217  80.885  18.931  1.00 56.40  ? 55  GLU   B C     1 
ATOM   14413 O  O     . GLU   F 2  53  ? 26.426  80.666  18.782  1.00 66.99  ? 55  GLU   B O     1 
ATOM   14414 C  CB    . GLU   F 2  53  ? 25.095  81.679  21.300  1.00 69.12  ? 55  GLU   B CB    1 
ATOM   14415 C  CG    . GLU   F 2  53  ? 24.472  81.599  22.692  1.00 69.15  ? 55  GLU   B CG    1 
ATOM   14416 C  CD    . GLU   F 2  53  ? 23.468  82.715  22.969  1.00 72.41  ? 55  GLU   B CD    1 
ATOM   14417 O  OE1   . GLU   F 2  53  ? 23.586  83.800  22.353  1.00 72.36  ? 55  GLU   B OE1   1 
ATOM   14418 O  OE2   . GLU   F 2  53  ? 22.561  82.505  23.811  1.00 69.08  ? 55  GLU   B OE2   1 
ATOM   14419 N  N     . ALA   F 2  54  ? 24.434  81.333  17.954  1.00 56.46  ? 56  ALA   B N     1 
ATOM   14420 C  CA    . ALA   F 2  54  ? 24.959  81.804  16.680  1.00 73.52  ? 56  ALA   B CA    1 
ATOM   14421 C  C     . ALA   F 2  54  ? 24.461  83.224  16.404  1.00 80.75  ? 56  ALA   B C     1 
ATOM   14422 O  O     . ALA   F 2  54  ? 23.461  83.676  16.975  1.00 77.26  ? 56  ALA   B O     1 
ATOM   14423 C  CB    . ALA   F 2  54  ? 24.560  80.863  15.537  1.00 67.67  ? 56  ALA   B CB    1 
ATOM   14424 N  N     . THR   F 2  55  ? 25.171  83.937  15.525  1.00 77.35  ? 57  THR   B N     1 
ATOM   14425 C  CA    . THR   F 2  55  ? 24.772  85.302  15.202  1.00 74.02  ? 57  THR   B CA    1 
ATOM   14426 C  C     . THR   F 2  55  ? 23.452  85.288  14.450  1.00 70.40  ? 57  THR   B C     1 
ATOM   14427 O  O     . THR   F 2  55  ? 23.274  84.530  13.492  1.00 66.48  ? 57  THR   B O     1 
ATOM   14428 C  CB    . THR   F 2  55  ? 25.838  86.022  14.374  1.00 87.75  ? 57  THR   B CB    1 
ATOM   14429 O  OG1   . THR   F 2  55  ? 26.950  86.377  15.210  1.00 103.40 ? 57  THR   B OG1   1 
ATOM   14430 C  CG2   . THR   F 2  55  ? 25.259  87.297  13.772  1.00 76.37  ? 57  THR   B CG2   1 
ATOM   14431 N  N     . GLY   F 2  56  ? 22.534  86.142  14.890  1.00 78.80  ? 58  GLY   B N     1 
ATOM   14432 C  CA    . GLY   F 2  56  ? 21.177  86.181  14.384  1.00 68.00  ? 58  GLY   B CA    1 
ATOM   14433 C  C     . GLY   F 2  56  ? 20.189  85.983  15.514  1.00 74.11  ? 58  GLY   B C     1 
ATOM   14434 O  O     . GLY   F 2  56  ? 18.985  85.816  15.280  1.00 71.17  ? 58  GLY   B O     1 
ATOM   14435 N  N     . ASN   F 2  57  ? 20.699  86.042  16.751  1.00 75.42  ? 59  ASN   B N     1 
ATOM   14436 C  CA    . ASN   F 2  57  ? 19.984  85.576  17.941  1.00 77.45  ? 59  ASN   B CA    1 
ATOM   14437 C  C     . ASN   F 2  57  ? 19.361  84.206  17.659  1.00 77.71  ? 59  ASN   B C     1 
ATOM   14438 O  O     . ASN   F 2  57  ? 18.170  83.963  17.889  1.00 78.88  ? 59  ASN   B O     1 
ATOM   14439 C  CB    . ASN   F 2  57  ? 18.939  86.601  18.410  1.00 84.09  ? 59  ASN   B CB    1 
ATOM   14440 C  CG    . ASN   F 2  57  ? 18.742  86.612  19.947  1.00 85.57  ? 59  ASN   B CG    1 
ATOM   14441 O  OD1   . ASN   F 2  57  ? 19.120  85.672  20.650  1.00 75.83  ? 59  ASN   B OD1   1 
ATOM   14442 N  ND2   . ASN   F 2  57  ? 18.126  87.681  20.458  1.00 78.19  ? 59  ASN   B ND2   1 
ATOM   14443 N  N     . LYS   F 2  58  ? 20.199  83.304  17.138  1.00 65.69  ? 60  LYS   B N     1 
ATOM   14444 C  CA    . LYS   F 2  58  ? 19.791  81.976  16.704  1.00 58.93  ? 60  LYS   B CA    1 
ATOM   14445 C  C     . LYS   F 2  58  ? 20.395  80.904  17.605  1.00 59.37  ? 60  LYS   B C     1 
ATOM   14446 O  O     . LYS   F 2  58  ? 21.498  81.062  18.142  1.00 61.20  ? 60  LYS   B O     1 
ATOM   14447 C  CB    . LYS   F 2  58  ? 20.185  81.736  15.242  1.00 59.85  ? 60  LYS   B CB    1 
ATOM   14448 C  CG    . LYS   F 2  58  ? 19.138  82.259  14.258  1.00 67.52  ? 60  LYS   B CG    1 
ATOM   14449 C  CD    . LYS   F 2  58  ? 19.749  82.618  12.917  1.00 70.02  ? 60  LYS   B CD    1 
ATOM   14450 C  CE    . LYS   F 2  58  ? 18.967  83.738  12.232  1.00 74.88  ? 60  LYS   B CE    1 
ATOM   14451 N  NZ    . LYS   F 2  58  ? 19.738  85.015  12.156  1.00 56.58  ? 60  LYS   B NZ    1 
ATOM   14452 N  N     . TYR   F 2  59  ? 19.650  79.807  17.751  1.00 50.71  ? 61  TYR   B N     1 
ATOM   14453 C  CA    . TYR   F 2  59  ? 19.889  78.789  18.767  1.00 39.87  ? 61  TYR   B CA    1 
ATOM   14454 C  C     . TYR   F 2  59  ? 19.921  77.418  18.111  1.00 43.56  ? 61  TYR   B C     1 
ATOM   14455 O  O     . TYR   F 2  59  ? 18.924  76.980  17.529  1.00 44.04  ? 61  TYR   B O     1 
ATOM   14456 C  CB    . TYR   F 2  59  ? 18.805  78.851  19.845  1.00 46.07  ? 61  TYR   B CB    1 
ATOM   14457 C  CG    . TYR   F 2  59  ? 18.898  80.109  20.672  1.00 48.19  ? 61  TYR   B CG    1 
ATOM   14458 C  CD1   . TYR   F 2  59  ? 19.842  80.214  21.681  1.00 41.32  ? 61  TYR   B CD1   1 
ATOM   14459 C  CD2   . TYR   F 2  59  ? 18.072  81.197  20.429  1.00 50.90  ? 61  TYR   B CD2   1 
ATOM   14460 C  CE1   . TYR   F 2  59  ? 19.969  81.348  22.426  1.00 41.59  ? 61  TYR   B CE1   1 
ATOM   14461 C  CE2   . TYR   F 2  59  ? 18.185  82.351  21.190  1.00 58.17  ? 61  TYR   B CE2   1 
ATOM   14462 C  CZ    . TYR   F 2  59  ? 19.143  82.415  22.189  1.00 57.85  ? 61  TYR   B CZ    1 
ATOM   14463 O  OH    . TYR   F 2  59  ? 19.288  83.545  22.963  1.00 68.74  ? 61  TYR   B OH    1 
ATOM   14464 N  N     . VAL   F 2  60  ? 21.057  76.743  18.215  1.00 47.34  ? 62  VAL   B N     1 
ATOM   14465 C  CA    . VAL   F 2  60  ? 21.306  75.460  17.563  1.00 42.68  ? 62  VAL   B CA    1 
ATOM   14466 C  C     . VAL   F 2  60  ? 21.340  74.382  18.643  1.00 45.93  ? 62  VAL   B C     1 
ATOM   14467 O  O     . VAL   F 2  60  ? 22.186  74.452  19.550  1.00 39.76  ? 62  VAL   B O     1 
ATOM   14468 C  CB    . VAL   F 2  60  ? 22.624  75.479  16.770  1.00 36.25  ? 62  VAL   B CB    1 
ATOM   14469 C  CG1   . VAL   F 2  60  ? 22.690  74.326  15.778  1.00 35.15  ? 62  VAL   B CG1   1 
ATOM   14470 C  CG2   . VAL   F 2  60  ? 22.806  76.805  16.077  1.00 33.43  ? 62  VAL   B CG2   1 
ATOM   14471 N  N     . PRO   F 2  61  ? 20.456  73.382  18.597  1.00 40.34  ? 63  PRO   B N     1 
ATOM   14472 C  CA    . PRO   F 2  61  ? 20.598  72.229  19.497  1.00 33.35  ? 63  PRO   B CA    1 
ATOM   14473 C  C     . PRO   F 2  61  ? 22.024  71.707  19.504  1.00 35.14  ? 63  PRO   B C     1 
ATOM   14474 O  O     . PRO   F 2  61  ? 22.632  71.498  18.450  1.00 35.44  ? 63  PRO   B O     1 
ATOM   14475 C  CB    . PRO   F 2  61  ? 19.628  71.200  18.910  1.00 27.52  ? 63  PRO   B CB    1 
ATOM   14476 C  CG    . PRO   F 2  61  ? 18.561  72.037  18.262  1.00 36.28  ? 63  PRO   B CG    1 
ATOM   14477 C  CD    . PRO   F 2  61  ? 19.222  73.313  17.790  1.00 35.28  ? 63  PRO   B CD    1 
ATOM   14478 N  N     . ARG   F 2  62  ? 22.566  71.505  20.710  1.00 40.08  ? 64  ARG   B N     1 
ATOM   14479 C  CA    . ARG   F 2  62  ? 23.871  70.862  20.874  1.00 35.63  ? 64  ARG   B CA    1 
ATOM   14480 C  C     . ARG   F 2  62  ? 23.703  69.340  20.789  1.00 29.75  ? 64  ARG   B C     1 
ATOM   14481 O  O     . ARG   F 2  62  ? 24.059  68.574  21.683  1.00 31.09  ? 64  ARG   B O     1 
ATOM   14482 C  CB    . ARG   F 2  62  ? 24.522  71.304  22.175  1.00 23.73  ? 64  ARG   B CB    1 
ATOM   14483 C  CG    . ARG   F 2  62  ? 26.002  70.983  22.227  1.00 28.64  ? 64  ARG   B CG    1 
ATOM   14484 C  CD    . ARG   F 2  62  ? 26.662  71.480  23.503  1.00 37.19  ? 64  ARG   B CD    1 
ATOM   14485 N  NE    . ARG   F 2  62  ? 26.509  72.921  23.654  1.00 43.54  ? 64  ARG   B NE    1 
ATOM   14486 C  CZ    . ARG   F 2  62  ? 25.611  73.501  24.438  1.00 39.27  ? 64  ARG   B CZ    1 
ATOM   14487 N  NH1   . ARG   F 2  62  ? 24.814  72.789  25.226  1.00 35.54  ? 64  ARG   B NH1   1 
ATOM   14488 N  NH2   . ARG   F 2  62  ? 25.504  74.826  24.427  1.00 29.29  ? 64  ARG   B NH2   1 
ATOM   14489 N  N     . ALA   F 2  63  ? 23.155  68.923  19.651  1.00 31.39  ? 65  ALA   B N     1 
ATOM   14490 C  CA    . ALA   F 2  63  ? 22.772  67.552  19.356  1.00 27.41  ? 65  ALA   B CA    1 
ATOM   14491 C  C     . ALA   F 2  63  ? 23.607  66.959  18.218  1.00 28.73  ? 65  ALA   B C     1 
ATOM   14492 O  O     . ALA   F 2  63  ? 24.006  67.654  17.280  1.00 31.20  ? 65  ALA   B O     1 
ATOM   14493 C  CB    . ALA   F 2  63  ? 21.296  67.495  18.981  1.00 26.76  ? 65  ALA   B CB    1 
ATOM   14494 N  N     . ILE   F 2  64  ? 23.834  65.649  18.298  1.00 28.56  ? 66  ILE   B N     1 
ATOM   14495 C  CA    . ILE   F 2  64  ? 24.586  64.885  17.311  1.00 28.09  ? 66  ILE   B CA    1 
ATOM   14496 C  C     . ILE   F 2  64  ? 23.729  63.701  16.899  1.00 26.92  ? 66  ILE   B C     1 
ATOM   14497 O  O     . ILE   F 2  64  ? 23.437  62.829  17.724  1.00 35.02  ? 66  ILE   B O     1 
ATOM   14498 C  CB    . ILE   F 2  64  ? 25.931  64.401  17.874  1.00 28.44  ? 66  ILE   B CB    1 
ATOM   14499 C  CG1   . ILE   F 2  64  ? 26.710  65.588  18.440  1.00 34.65  ? 66  ILE   B CG1   1 
ATOM   14500 C  CG2   . ILE   F 2  64  ? 26.726  63.656  16.827  1.00 23.47  ? 66  ILE   B CG2   1 
ATOM   14501 C  CD1   . ILE   F 2  64  ? 27.985  65.195  19.157  1.00 33.88  ? 66  ILE   B CD1   1 
ATOM   14502 N  N     . LEU   F 2  65  ? 23.360  63.649  15.629  1.00 25.64  ? 67  LEU   B N     1 
ATOM   14503 C  CA    . LEU   F 2  65  ? 22.523  62.585  15.087  1.00 27.82  ? 67  LEU   B CA    1 
ATOM   14504 C  C     . LEU   F 2  65  ? 23.382  61.472  14.491  1.00 25.88  ? 67  LEU   B C     1 
ATOM   14505 O  O     . LEU   F 2  65  ? 24.108  61.704  13.518  1.00 26.62  ? 67  LEU   B O     1 
ATOM   14506 C  CB    . LEU   F 2  65  ? 21.589  63.174  14.034  1.00 32.42  ? 67  LEU   B CB    1 
ATOM   14507 C  CG    . LEU   F 2  65  ? 20.679  64.234  14.672  1.00 31.97  ? 67  LEU   B CG    1 
ATOM   14508 C  CD1   . LEU   F 2  65  ? 21.383  65.575  14.886  1.00 26.10  ? 67  LEU   B CD1   1 
ATOM   14509 C  CD2   . LEU   F 2  65  ? 19.406  64.390  13.865  1.00 27.61  ? 67  LEU   B CD2   1 
ATOM   14510 N  N     . VAL   F 2  66  ? 23.284  60.260  15.053  1.00 27.34  ? 68  VAL   B N     1 
ATOM   14511 C  CA    . VAL   F 2  66  ? 24.094  59.117  14.630  1.00 23.34  ? 68  VAL   B CA    1 
ATOM   14512 C  C     . VAL   F 2  66  ? 23.204  57.956  14.198  1.00 22.22  ? 68  VAL   B C     1 
ATOM   14513 O  O     . VAL   F 2  66  ? 22.230  57.628  14.882  1.00 23.59  ? 68  VAL   B O     1 
ATOM   14514 C  CB    . VAL   F 2  66  ? 25.043  58.675  15.760  1.00 20.48  ? 68  VAL   B CB    1 
ATOM   14515 C  CG1   . VAL   F 2  66  ? 25.774  57.404  15.378  1.00 21.53  ? 68  VAL   B CG1   1 
ATOM   14516 C  CG2   . VAL   F 2  66  ? 26.028  59.781  16.054  1.00 25.32  ? 68  VAL   B CG2   1 
ATOM   14517 N  N     . ASP   F 2  67  ? 23.540  57.328  13.067  1.00 29.11  ? 69  ASP   B N     1 
ATOM   14518 C  CA    . ASP   F 2  67  ? 22.942  56.044  12.682  1.00 27.96  ? 69  ASP   B CA    1 
ATOM   14519 C  C     . ASP   F 2  67  ? 23.814  55.339  11.641  1.00 33.08  ? 69  ASP   B C     1 
ATOM   14520 O  O     . ASP   F 2  67  ? 24.522  55.982  10.860  1.00 27.59  ? 69  ASP   B O     1 
ATOM   14521 C  CB    . ASP   F 2  67  ? 21.524  56.214  12.126  1.00 24.96  ? 69  ASP   B CB    1 
ATOM   14522 C  CG    . ASP   F 2  67  ? 20.594  55.024  12.449  1.00 29.75  ? 69  ASP   B CG    1 
ATOM   14523 O  OD1   . ASP   F 2  67  ? 21.067  53.896  12.768  1.00 25.22  ? 69  ASP   B OD1   1 
ATOM   14524 O  OD2   . ASP   F 2  67  ? 19.359  55.228  12.362  1.00 28.63  ? 69  ASP   B OD2   1 
ATOM   14525 N  N     . LEU   F 2  68  ? 23.745  54.006  11.638  1.00 31.31  ? 70  LEU   B N     1 
ATOM   14526 C  CA    . LEU   F 2  68  ? 24.462  53.176  10.680  1.00 25.01  ? 70  LEU   B CA    1 
ATOM   14527 C  C     . LEU   F 2  68  ? 23.711  53.020  9.367   1.00 31.96  ? 70  LEU   B C     1 
ATOM   14528 O  O     . LEU   F 2  68  ? 24.151  52.263  8.491   1.00 39.69  ? 70  LEU   B O     1 
ATOM   14529 C  CB    . LEU   F 2  68  ? 24.751  51.801  11.284  1.00 22.73  ? 70  LEU   B CB    1 
ATOM   14530 C  CG    . LEU   F 2  68  ? 25.910  51.710  12.284  1.00 23.85  ? 70  LEU   B CG    1 
ATOM   14531 C  CD1   . LEU   F 2  68  ? 26.225  50.266  12.629  1.00 24.43  ? 70  LEU   B CD1   1 
ATOM   14532 C  CD2   . LEU   F 2  68  ? 27.129  52.390  11.745  1.00 19.10  ? 70  LEU   B CD2   1 
ATOM   14533 N  N     . GLU   F 2  69  ? 22.598  53.731  9.206   1.00 38.56  ? 71  GLU   B N     1 
ATOM   14534 C  CA    . GLU   F 2  69  ? 21.796  53.675  7.999   1.00 39.47  ? 71  GLU   B CA    1 
ATOM   14535 C  C     . GLU   F 2  69  ? 21.130  55.008  7.692   1.00 41.66  ? 71  GLU   B C     1 
ATOM   14536 O  O     . GLU   F 2  69  ? 20.620  55.671  8.608   1.00 45.89  ? 71  GLU   B O     1 
ATOM   14537 C  CB    . GLU   F 2  69  ? 20.728  52.614  8.133   1.00 39.53  ? 71  GLU   B CB    1 
ATOM   14538 C  CG    . GLU   F 2  69  ? 19.572  52.892  7.260   1.00 52.36  ? 71  GLU   B CG    1 
ATOM   14539 C  CD    . GLU   F 2  69  ? 18.470  51.969  7.590   1.00 61.92  ? 71  GLU   B CD    1 
ATOM   14540 O  OE1   . GLU   F 2  69  ? 18.637  51.272  8.626   1.00 44.61  ? 71  GLU   B OE1   1 
ATOM   14541 O  OE2   . GLU   F 2  69  ? 17.475  51.938  6.827   1.00 64.67  ? 71  GLU   B OE2   1 
ATOM   14542 N  N     . PRO   F 2  70  ? 21.079  55.412  6.427   1.00 53.53  ? 72  PRO   B N     1 
ATOM   14543 C  CA    . PRO   F 2  70  ? 20.637  56.782  6.125   1.00 51.68  ? 72  PRO   B CA    1 
ATOM   14544 C  C     . PRO   F 2  70  ? 19.154  57.011  6.353   1.00 56.04  ? 72  PRO   B C     1 
ATOM   14545 O  O     . PRO   F 2  70  ? 18.735  58.169  6.486   1.00 53.61  ? 72  PRO   B O     1 
ATOM   14546 C  CB    . PRO   F 2  70  ? 21.025  56.961  4.655   1.00 43.60  ? 72  PRO   B CB    1 
ATOM   14547 C  CG    . PRO   F 2  70  ? 21.088  55.590  4.106   1.00 53.03  ? 72  PRO   B CG    1 
ATOM   14548 C  CD    . PRO   F 2  70  ? 21.451  54.654  5.221   1.00 53.73  ? 72  PRO   B CD    1 
ATOM   14549 N  N     . GLY   F 2  71  ? 18.356  55.955  6.439   1.00 60.13  ? 73  GLY   B N     1 
ATOM   14550 C  CA    . GLY   F 2  71  ? 16.934  56.107  6.667   1.00 54.08  ? 73  GLY   B CA    1 
ATOM   14551 C  C     . GLY   F 2  71  ? 16.548  57.182  7.661   1.00 54.97  ? 73  GLY   B C     1 
ATOM   14552 O  O     . GLY   F 2  71  ? 15.926  58.181  7.292   1.00 60.61  ? 73  GLY   B O     1 
ATOM   14553 N  N     . THR   F 2  72  ? 16.918  56.998  8.930   1.00 62.24  ? 74  THR   B N     1 
ATOM   14554 C  CA    . THR   F 2  72  ? 16.365  57.859  9.969   1.00 56.89  ? 74  THR   B CA    1 
ATOM   14555 C  C     . THR   F 2  72  ? 16.897  59.282  9.867   1.00 60.43  ? 74  THR   B C     1 
ATOM   14556 O  O     . THR   F 2  72  ? 16.168  60.230  10.175  1.00 60.71  ? 74  THR   B O     1 
ATOM   14557 C  CB    . THR   F 2  72  ? 16.649  57.268  11.347  1.00 60.85  ? 74  THR   B CB    1 
ATOM   14558 O  OG1   . THR   F 2  72  ? 17.554  56.151  11.210  1.00 50.27  ? 74  THR   B OG1   1 
ATOM   14559 C  CG2   . THR   F 2  72  ? 15.319  56.848  12.040  1.00 43.27  ? 74  THR   B CG2   1 
ATOM   14560 N  N     . MET   F 2  73  ? 18.148  59.461  9.430   1.00 61.27  ? 75  MET   B N     1 
ATOM   14561 C  CA    . MET   F 2  73  ? 18.639  60.813  9.172   1.00 62.37  ? 75  MET   B CA    1 
ATOM   14562 C  C     . MET   F 2  73  ? 17.641  61.581  8.307   1.00 53.83  ? 75  MET   B C     1 
ATOM   14563 O  O     . MET   F 2  73  ? 17.164  62.659  8.684   1.00 52.21  ? 75  MET   B O     1 
ATOM   14564 C  CB    . MET   F 2  73  ? 20.032  60.774  8.509   1.00 62.46  ? 75  MET   B CB    1 
ATOM   14565 C  CG    . MET   F 2  73  ? 21.114  59.844  9.178   1.00 65.27  ? 75  MET   B CG    1 
ATOM   14566 S  SD    . MET   F 2  73  ? 21.935  60.342  10.752  1.00 46.04  ? 75  MET   B SD    1 
ATOM   14567 C  CE    . MET   F 2  73  ? 20.589  60.127  11.908  1.00 37.00  ? 75  MET   B CE    1 
ATOM   14568 N  N     . ASP   F 2  74  ? 17.265  61.006  7.169   1.00 50.80  ? 76  ASP   B N     1 
ATOM   14569 C  CA    . ASP   F 2  74  ? 16.411  61.730  6.236   1.00 54.14  ? 76  ASP   B CA    1 
ATOM   14570 C  C     . ASP   F 2  74  ? 15.024  61.995  6.799   1.00 50.70  ? 76  ASP   B C     1 
ATOM   14571 O  O     . ASP   F 2  74  ? 14.411  63.010  6.466   1.00 51.35  ? 76  ASP   B O     1 
ATOM   14572 C  CB    . ASP   F 2  74  ? 16.316  60.965  4.923   1.00 51.07  ? 76  ASP   B CB    1 
ATOM   14573 C  CG    . ASP   F 2  74  ? 17.650  60.890  4.222   1.00 68.46  ? 76  ASP   B CG    1 
ATOM   14574 O  OD1   . ASP   F 2  74  ? 17.732  60.245  3.153   1.00 74.06  ? 76  ASP   B OD1   1 
ATOM   14575 O  OD2   . ASP   F 2  74  ? 18.625  61.472  4.763   1.00 73.47  ? 76  ASP   B OD2   1 
ATOM   14576 N  N     . SER   F 2  75  ? 14.506  61.104  7.637   1.00 57.34  ? 77  SER   B N     1 
ATOM   14577 C  CA    . SER   F 2  75  ? 13.187  61.333  8.216   1.00 51.73  ? 77  SER   B CA    1 
ATOM   14578 C  C     . SER   F 2  75  ? 13.200  62.544  9.131   1.00 47.36  ? 77  SER   B C     1 
ATOM   14579 O  O     . SER   F 2  75  ? 12.314  63.398  9.049   1.00 50.01  ? 77  SER   B O     1 
ATOM   14580 C  CB    . SER   F 2  75  ? 12.732  60.106  8.992   1.00 56.03  ? 77  SER   B CB    1 
ATOM   14581 O  OG    . SER   F 2  75  ? 13.707  59.757  9.962   1.00 67.64  ? 77  SER   B OG    1 
ATOM   14582 N  N     . VAL   F 2  76  ? 14.201  62.629  10.014  1.00 43.65  ? 78  VAL   B N     1 
ATOM   14583 C  CA    . VAL   F 2  76  ? 14.267  63.731  10.969  1.00 43.28  ? 78  VAL   B CA    1 
ATOM   14584 C  C     . VAL   F 2  76  ? 14.594  65.034  10.263  1.00 47.68  ? 78  VAL   B C     1 
ATOM   14585 O  O     . VAL   F 2  76  ? 13.987  66.069  10.555  1.00 53.16  ? 78  VAL   B O     1 
ATOM   14586 C  CB    . VAL   F 2  76  ? 15.272  63.433  12.100  1.00 45.52  ? 78  VAL   B CB    1 
ATOM   14587 C  CG1   . VAL   F 2  76  ? 14.885  62.143  12.840  1.00 43.38  ? 78  VAL   B CG1   1 
ATOM   14588 C  CG2   . VAL   F 2  76  ? 16.703  63.375  11.572  1.00 51.53  ? 78  VAL   B CG2   1 
ATOM   14589 N  N     . ARG   F 2  77  ? 15.548  65.017  9.321   1.00 56.76  ? 79  ARG   B N     1 
ATOM   14590 C  CA    . ARG   F 2  77  ? 15.846  66.241  8.575   1.00 51.63  ? 79  ARG   B CA    1 
ATOM   14591 C  C     . ARG   F 2  77  ? 14.603  66.774  7.878   1.00 50.13  ? 79  ARG   B C     1 
ATOM   14592 O  O     . ARG   F 2  77  ? 14.488  67.983  7.660   1.00 54.10  ? 79  ARG   B O     1 
ATOM   14593 C  CB    . ARG   F 2  77  ? 16.965  66.001  7.558   1.00 54.55  ? 79  ARG   B CB    1 
ATOM   14594 C  CG    . ARG   F 2  77  ? 17.658  67.272  7.041   1.00 45.84  ? 79  ARG   B CG    1 
ATOM   14595 C  CD    . ARG   F 2  77  ? 18.677  66.923  5.959   1.00 49.83  ? 79  ARG   B CD    1 
ATOM   14596 N  NE    . ARG   F 2  77  ? 19.444  65.710  6.237   1.00 53.17  ? 79  ARG   B NE    1 
ATOM   14597 C  CZ    . ARG   F 2  77  ? 20.752  65.674  6.480   1.00 63.60  ? 79  ARG   B CZ    1 
ATOM   14598 N  NH1   . ARG   F 2  77  ? 21.486  66.780  6.523   1.00 53.66  ? 79  ARG   B NH1   1 
ATOM   14599 N  NH2   . ARG   F 2  77  ? 21.342  64.495  6.677   1.00 57.19  ? 79  ARG   B NH2   1 
ATOM   14600 N  N     . SER   F 2  78  ? 13.665  65.892  7.528   1.00 49.68  ? 80  SER   B N     1 
ATOM   14601 C  CA    . SER   F 2  78  ? 12.362  66.275  6.986   1.00 50.51  ? 80  SER   B CA    1 
ATOM   14602 C  C     . SER   F 2  78  ? 11.251  66.096  8.015   1.00 49.29  ? 80  SER   B C     1 
ATOM   14603 O  O     . SER   F 2  78  ? 10.153  65.636  7.692   1.00 50.13  ? 80  SER   B O     1 
ATOM   14604 C  CB    . SER   F 2  78  ? 12.061  65.488  5.713   1.00 56.54  ? 80  SER   B CB    1 
ATOM   14605 O  OG    . SER   F 2  78  ? 12.310  64.103  5.900   1.00 61.76  ? 80  SER   B OG    1 
ATOM   14606 N  N     . GLY   F 2  79  ? 11.530  66.444  9.272   1.00 52.38  ? 81  GLY   B N     1 
ATOM   14607 C  CA    . GLY   F 2  79  ? 10.525  66.516  10.305  1.00 46.70  ? 81  GLY   B CA    1 
ATOM   14608 C  C     . GLY   F 2  79  ? 10.218  67.968  10.612  1.00 55.17  ? 81  GLY   B C     1 
ATOM   14609 O  O     . GLY   F 2  79  ? 10.764  68.877  9.977   1.00 55.38  ? 81  GLY   B O     1 
ATOM   14610 N  N     . PRO   F 2  80  ? 9.337   68.225  11.584  1.00 49.29  ? 82  PRO   B N     1 
ATOM   14611 C  CA    . PRO   F 2  80  ? 8.979   69.616  11.886  1.00 47.44  ? 82  PRO   B CA    1 
ATOM   14612 C  C     . PRO   F 2  80  ? 10.217  70.467  12.133  1.00 54.06  ? 82  PRO   B C     1 
ATOM   14613 O  O     . PRO   F 2  80  ? 10.453  71.460  11.429  1.00 46.10  ? 82  PRO   B O     1 
ATOM   14614 C  CB    . PRO   F 2  80  ? 8.097   69.495  13.140  1.00 44.77  ? 82  PRO   B CB    1 
ATOM   14615 C  CG    . PRO   F 2  80  ? 8.336   68.107  13.673  1.00 45.42  ? 82  PRO   B CG    1 
ATOM   14616 C  CD    . PRO   F 2  80  ? 8.676   67.269  12.491  1.00 51.80  ? 82  PRO   B CD    1 
ATOM   14617 N  N     . PHE   F 2  81  ? 11.032  70.067  13.113  1.00 48.40  ? 83  PHE   B N     1 
ATOM   14618 C  CA    . PHE   F 2  81  ? 12.235  70.809  13.466  1.00 47.56  ? 83  PHE   B CA    1 
ATOM   14619 C  C     . PHE   F 2  81  ? 13.475  70.265  12.773  1.00 54.98  ? 83  PHE   B C     1 
ATOM   14620 O  O     . PHE   F 2  81  ? 14.598  70.544  13.216  1.00 54.42  ? 83  PHE   B O     1 
ATOM   14621 C  CB    . PHE   F 2  81  ? 12.435  70.818  14.985  1.00 45.17  ? 83  PHE   B CB    1 
ATOM   14622 C  CG    . PHE   F 2  81  ? 11.492  71.731  15.725  1.00 48.81  ? 83  PHE   B CG    1 
ATOM   14623 C  CD1   . PHE   F 2  81  ? 10.128  71.490  15.732  1.00 39.35  ? 83  PHE   B CD1   1 
ATOM   14624 C  CD2   . PHE   F 2  81  ? 11.976  72.828  16.427  1.00 53.30  ? 83  PHE   B CD2   1 
ATOM   14625 C  CE1   . PHE   F 2  81  ? 9.270   72.326  16.418  1.00 38.40  ? 83  PHE   B CE1   1 
ATOM   14626 C  CE2   . PHE   F 2  81  ? 11.111  73.672  17.110  1.00 44.04  ? 83  PHE   B CE2   1 
ATOM   14627 C  CZ    . PHE   F 2  81  ? 9.760   73.415  17.106  1.00 39.51  ? 83  PHE   B CZ    1 
ATOM   14628 N  N     . GLY   F 2  82  ? 13.294  69.514  11.691  1.00 52.84  ? 84  GLY   B N     1 
ATOM   14629 C  CA    . GLY   F 2  82  ? 14.405  68.898  11.004  1.00 49.11  ? 84  GLY   B CA    1 
ATOM   14630 C  C     . GLY   F 2  82  ? 15.492  69.861  10.578  1.00 55.12  ? 84  GLY   B C     1 
ATOM   14631 O  O     . GLY   F 2  82  ? 16.610  69.449  10.239  1.00 53.87  ? 84  GLY   B O     1 
ATOM   14632 N  N     . GLN   F 2  83  ? 15.184  71.155  10.597  1.00 58.57  ? 85  GLN   B N     1 
ATOM   14633 C  CA    . GLN   F 2  83  ? 16.114  72.137  10.066  1.00 55.40  ? 85  GLN   B CA    1 
ATOM   14634 C  C     . GLN   F 2  83  ? 16.947  72.849  11.125  1.00 56.92  ? 85  GLN   B C     1 
ATOM   14635 O  O     . GLN   F 2  83  ? 17.826  73.629  10.754  1.00 59.92  ? 85  GLN   B O     1 
ATOM   14636 C  CB    . GLN   F 2  83  ? 15.362  73.179  9.231   1.00 58.95  ? 85  GLN   B CB    1 
ATOM   14637 C  CG    . GLN   F 2  83  ? 14.130  73.762  9.913   1.00 65.56  ? 85  GLN   B CG    1 
ATOM   14638 C  CD    . GLN   F 2  83  ? 13.574  74.981  9.177   1.00 75.89  ? 85  GLN   B CD    1 
ATOM   14639 O  OE1   . GLN   F 2  83  ? 14.328  75.846  8.720   1.00 62.54  ? 85  GLN   B OE1   1 
ATOM   14640 N  NE2   . GLN   F 2  83  ? 12.245  75.049  9.056   1.00 81.57  ? 85  GLN   B NE2   1 
ATOM   14641 N  N     . ILE   F 2  84  ? 16.724  72.618  12.418  1.00 49.80  ? 86  ILE   B N     1 
ATOM   14642 C  CA    . ILE   F 2  84  ? 17.431  73.391  13.439  1.00 48.37  ? 86  ILE   B CA    1 
ATOM   14643 C  C     . ILE   F 2  84  ? 18.670  72.667  13.963  1.00 49.53  ? 86  ILE   B C     1 
ATOM   14644 O  O     . ILE   F 2  84  ? 19.207  73.057  15.000  1.00 51.07  ? 86  ILE   B O     1 
ATOM   14645 C  CB    . ILE   F 2  84  ? 16.524  73.797  14.611  1.00 58.00  ? 86  ILE   B CB    1 
ATOM   14646 C  CG1   . ILE   F 2  84  ? 15.920  72.576  15.315  1.00 53.37  ? 86  ILE   B CG1   1 
ATOM   14647 C  CG2   . ILE   F 2  84  ? 15.459  74.800  14.175  1.00 59.36  ? 86  ILE   B CG2   1 
ATOM   14648 C  CD1   . ILE   F 2  84  ? 15.268  72.938  16.635  1.00 46.84  ? 86  ILE   B CD1   1 
ATOM   14649 N  N     . PHE   F 2  85  ? 19.146  71.637  13.268  1.00 50.39  ? 87  PHE   B N     1 
ATOM   14650 C  CA    . PHE   F 2  85  ? 20.314  70.886  13.712  1.00 38.13  ? 87  PHE   B CA    1 
ATOM   14651 C  C     . PHE   F 2  85  ? 21.537  71.234  12.865  1.00 37.70  ? 87  PHE   B C     1 
ATOM   14652 O  O     . PHE   F 2  85  ? 21.445  71.315  11.637  1.00 39.73  ? 87  PHE   B O     1 
ATOM   14653 C  CB    . PHE   F 2  85  ? 20.038  69.381  13.642  1.00 35.25  ? 87  PHE   B CB    1 
ATOM   14654 C  CG    . PHE   F 2  85  ? 18.987  68.895  14.617  1.00 33.43  ? 87  PHE   B CG    1 
ATOM   14655 C  CD1   . PHE   F 2  85  ? 19.306  68.656  15.941  1.00 28.81  ? 87  PHE   B CD1   1 
ATOM   14656 C  CD2   . PHE   F 2  85  ? 17.691  68.636  14.199  1.00 41.00  ? 87  PHE   B CD2   1 
ATOM   14657 C  CE1   . PHE   F 2  85  ? 18.356  68.196  16.826  1.00 27.90  ? 87  PHE   B CE1   1 
ATOM   14658 C  CE2   . PHE   F 2  85  ? 16.724  68.167  15.099  1.00 27.33  ? 87  PHE   B CE2   1 
ATOM   14659 C  CZ    . PHE   F 2  85  ? 17.060  67.952  16.400  1.00 26.09  ? 87  PHE   B CZ    1 
ATOM   14660 N  N     . ARG   F 2  86  ? 22.692  71.438  13.530  1.00 39.95  ? 88  ARG   B N     1 
ATOM   14661 C  CA    . ARG   F 2  86  ? 23.982  71.627  12.859  1.00 31.80  ? 88  ARG   B CA    1 
ATOM   14662 C  C     . ARG   F 2  86  ? 24.171  70.516  11.830  1.00 38.06  ? 88  ARG   B C     1 
ATOM   14663 O  O     . ARG   F 2  86  ? 24.418  69.360  12.206  1.00 40.30  ? 88  ARG   B O     1 
ATOM   14664 C  CB    . ARG   F 2  86  ? 25.138  71.627  13.881  1.00 39.31  ? 88  ARG   B CB    1 
ATOM   14665 C  CG    . ARG   F 2  86  ? 26.305  72.627  13.593  1.00 48.07  ? 88  ARG   B CG    1 
ATOM   14666 C  CD    . ARG   F 2  86  ? 27.434  72.641  14.668  1.00 49.11  ? 88  ARG   B CD    1 
ATOM   14667 N  NE    . ARG   F 2  86  ? 27.397  73.818  15.544  1.00 69.21  ? 88  ARG   B NE    1 
ATOM   14668 C  CZ    . ARG   F 2  86  ? 28.316  74.136  16.459  1.00 71.75  ? 88  ARG   B CZ    1 
ATOM   14669 N  NH1   . ARG   F 2  86  ? 29.401  73.392  16.652  1.00 55.56  ? 88  ARG   B NH1   1 
ATOM   14670 N  NH2   . ARG   F 2  86  ? 28.146  75.234  17.200  1.00 57.95  ? 88  ARG   B NH2   1 
ATOM   14671 N  N     . PRO   F 2  87  ? 24.102  70.821  10.527  1.00 47.38  ? 89  PRO   B N     1 
ATOM   14672 C  CA    . PRO   F 2  87  ? 24.069  69.741  9.518   1.00 37.86  ? 89  PRO   B CA    1 
ATOM   14673 C  C     . PRO   F 2  87  ? 25.328  68.881  9.470   1.00 35.21  ? 89  PRO   B C     1 
ATOM   14674 O  O     . PRO   F 2  87  ? 25.248  67.721  9.059   1.00 42.08  ? 89  PRO   B O     1 
ATOM   14675 C  CB    . PRO   F 2  87  ? 23.857  70.500  8.203   1.00 36.49  ? 89  PRO   B CB    1 
ATOM   14676 C  CG    . PRO   F 2  87  ? 23.563  71.930  8.582   1.00 28.17  ? 89  PRO   B CG    1 
ATOM   14677 C  CD    . PRO   F 2  87  ? 24.206  72.150  9.904   1.00 42.78  ? 89  PRO   B CD    1 
ATOM   14678 N  N     . ASP   F 2  88  ? 26.491  69.406  9.858   1.00 42.86  ? 90  ASP   B N     1 
ATOM   14679 C  CA    . ASP   F 2  88  ? 27.651  68.540  10.031  1.00 42.66  ? 90  ASP   B CA    1 
ATOM   14680 C  C     . ASP   F 2  88  ? 27.487  67.580  11.189  1.00 40.41  ? 90  ASP   B C     1 
ATOM   14681 O  O     . ASP   F 2  88  ? 28.322  66.678  11.343  1.00 37.06  ? 90  ASP   B O     1 
ATOM   14682 C  CB    . ASP   F 2  88  ? 28.895  69.369  10.270  1.00 45.54  ? 90  ASP   B CB    1 
ATOM   14683 C  CG    . ASP   F 2  88  ? 28.990  70.503  9.321   1.00 56.61  ? 90  ASP   B CG    1 
ATOM   14684 O  OD1   . ASP   F 2  88  ? 29.340  70.243  8.143   1.00 61.33  ? 90  ASP   B OD1   1 
ATOM   14685 O  OD2   . ASP   F 2  88  ? 28.655  71.633  9.744   1.00 55.17  ? 90  ASP   B OD2   1 
ATOM   14686 N  N     . ASN   F 2  89  ? 26.463  67.785  12.024  1.00 37.88  ? 91  ASN   B N     1 
ATOM   14687 C  CA    . ASN   F 2  89  ? 26.211  66.980  13.210  1.00 34.39  ? 91  ASN   B CA    1 
ATOM   14688 C  C     . ASN   F 2  89  ? 25.405  65.723  12.889  1.00 36.08  ? 91  ASN   B C     1 
ATOM   14689 O  O     . ASN   F 2  89  ? 25.032  64.974  13.803  1.00 31.33  ? 91  ASN   B O     1 
ATOM   14690 C  CB    . ASN   F 2  89  ? 25.513  67.836  14.271  1.00 25.08  ? 91  ASN   B CB    1 
ATOM   14691 C  CG    . ASN   F 2  89  ? 26.488  68.668  15.078  1.00 32.32  ? 91  ASN   B CG    1 
ATOM   14692 O  OD1   . ASN   F 2  89  ? 27.410  69.290  14.541  1.00 38.45  ? 91  ASN   B OD1   1 
ATOM   14693 N  ND2   . ASN   F 2  89  ? 26.305  68.665  16.379  1.00 32.47  ? 91  ASN   B ND2   1 
ATOM   14694 N  N     . PHE   F 2  90  ? 25.132  65.496  11.603  1.00 31.04  ? 92  PHE   B N     1 
ATOM   14695 C  CA    . PHE   F 2  90  ? 24.544  64.259  11.118  1.00 29.55  ? 92  PHE   B CA    1 
ATOM   14696 C  C     . PHE   F 2  90  ? 25.679  63.317  10.729  1.00 32.72  ? 92  PHE   B C     1 
ATOM   14697 O  O     . PHE   F 2  90  ? 26.376  63.561  9.741   1.00 36.20  ? 92  PHE   B O     1 
ATOM   14698 C  CB    . PHE   F 2  90  ? 23.642  64.544  9.925   1.00 31.89  ? 92  PHE   B CB    1 
ATOM   14699 C  CG    . PHE   F 2  90  ? 22.328  65.171  10.276  1.00 29.85  ? 92  PHE   B CG    1 
ATOM   14700 C  CD1   . PHE   F 2  90  ? 22.227  66.525  10.513  1.00 34.26  ? 92  PHE   B CD1   1 
ATOM   14701 C  CD2   . PHE   F 2  90  ? 21.178  64.406  10.327  1.00 35.74  ? 92  PHE   B CD2   1 
ATOM   14702 C  CE1   . PHE   F 2  90  ? 20.993  67.104  10.822  1.00 39.26  ? 92  PHE   B CE1   1 
ATOM   14703 C  CE2   . PHE   F 2  90  ? 19.948  64.980  10.623  1.00 40.18  ? 92  PHE   B CE2   1 
ATOM   14704 C  CZ    . PHE   F 2  90  ? 19.856  66.326  10.870  1.00 35.25  ? 92  PHE   B CZ    1 
ATOM   14705 N  N     . VAL   F 2  91  ? 25.886  62.256  11.510  1.00 28.51  ? 93  VAL   B N     1 
ATOM   14706 C  CA    . VAL   F 2  91  ? 26.879  61.230  11.203  1.00 26.17  ? 93  VAL   B CA    1 
ATOM   14707 C  C     . VAL   F 2  91  ? 26.119  59.947  10.882  1.00 35.75  ? 93  VAL   B C     1 
ATOM   14708 O  O     . VAL   F 2  91  ? 25.347  59.454  11.716  1.00 37.88  ? 93  VAL   B O     1 
ATOM   14709 C  CB    . VAL   F 2  91  ? 27.866  61.023  12.361  1.00 30.12  ? 93  VAL   B CB    1 
ATOM   14710 C  CG1   . VAL   F 2  91  ? 28.956  60.049  11.969  1.00 28.13  ? 93  VAL   B CG1   1 
ATOM   14711 C  CG2   . VAL   F 2  91  ? 28.468  62.345  12.808  1.00 31.79  ? 93  VAL   B CG2   1 
ATOM   14712 N  N     . PHE   F 2  92  ? 26.306  59.416  9.666   1.00 38.47  ? 94  PHE   B N     1 
ATOM   14713 C  CA    . PHE   F 2  92  ? 25.535  58.249  9.252   1.00 39.90  ? 94  PHE   B CA    1 
ATOM   14714 C  C     . PHE   F 2  92  ? 26.262  57.414  8.201   1.00 36.21  ? 94  PHE   B C     1 
ATOM   14715 O  O     . PHE   F 2  92  ? 26.886  57.964  7.291   1.00 37.63  ? 94  PHE   B O     1 
ATOM   14716 C  CB    . PHE   F 2  92  ? 24.146  58.678  8.749   1.00 44.51  ? 94  PHE   B CB    1 
ATOM   14717 C  CG    . PHE   F 2  92  ? 24.155  59.785  7.726   1.00 53.46  ? 94  PHE   B CG    1 
ATOM   14718 C  CD1   . PHE   F 2  92  ? 24.237  61.118  8.120   1.00 52.87  ? 94  PHE   B CD1   1 
ATOM   14719 C  CD2   . PHE   F 2  92  ? 24.030  59.493  6.366   1.00 55.82  ? 94  PHE   B CD2   1 
ATOM   14720 C  CE1   . PHE   F 2  92  ? 24.229  62.148  7.163   1.00 59.49  ? 94  PHE   B CE1   1 
ATOM   14721 C  CE2   . PHE   F 2  92  ? 24.026  60.513  5.407   1.00 49.57  ? 94  PHE   B CE2   1 
ATOM   14722 C  CZ    . PHE   F 2  92  ? 24.122  61.840  5.806   1.00 57.86  ? 94  PHE   B CZ    1 
ATOM   14723 N  N     . GLY   F 2  93  ? 26.163  56.088  8.344   1.00 37.37  ? 95  GLY   B N     1 
ATOM   14724 C  CA    . GLY   F 2  93  ? 26.662  55.060  7.413   1.00 34.47  ? 95  GLY   B CA    1 
ATOM   14725 C  C     . GLY   F 2  93  ? 25.601  54.544  6.454   1.00 39.37  ? 95  GLY   B C     1 
ATOM   14726 O  O     . GLY   F 2  93  ? 24.621  55.229  6.144   1.00 37.03  ? 95  GLY   B O     1 
ATOM   14727 N  N     . GLN   F 2  94  ? 25.786  53.311  5.973   1.00 46.65  ? 96  GLN   B N     1 
ATOM   14728 C  CA    . GLN   F 2  94  ? 24.981  52.814  4.857   1.00 42.25  ? 96  GLN   B CA    1 
ATOM   14729 C  C     . GLN   F 2  94  ? 24.505  51.391  5.070   1.00 35.24  ? 96  GLN   B C     1 
ATOM   14730 O  O     . GLN   F 2  94  ? 23.331  51.074  4.873   1.00 44.88  ? 96  GLN   B O     1 
ATOM   14731 C  CB    . GLN   F 2  94  ? 25.787  52.895  3.558   1.00 37.55  ? 96  GLN   B CB    1 
ATOM   14732 C  CG    . GLN   F 2  94  ? 25.569  54.189  2.790   1.00 52.46  ? 96  GLN   B CG    1 
ATOM   14733 C  CD    . GLN   F 2  94  ? 24.116  54.390  2.400   1.00 59.02  ? 96  GLN   B CD    1 
ATOM   14734 O  OE1   . GLN   F 2  94  ? 23.257  53.559  2.718   1.00 58.96  ? 96  GLN   B OE1   1 
ATOM   14735 N  NE2   . GLN   F 2  94  ? 23.832  55.492  1.706   1.00 45.73  ? 96  GLN   B NE2   1 
ATOM   14736 N  N     . SER   F 2  95  ? 25.443  50.530  5.415   1.00 35.70  ? 97  SER   B N     1 
ATOM   14737 C  CA    . SER   F 2  95  ? 25.206  49.151  5.796   1.00 35.17  ? 97  SER   B CA    1 
ATOM   14738 C  C     . SER   F 2  95  ? 23.964  48.963  6.655   1.00 39.84  ? 97  SER   B C     1 
ATOM   14739 O  O     . SER   F 2  95  ? 23.174  48.039  6.437   1.00 42.49  ? 97  SER   B O     1 
ATOM   14740 C  CB    . SER   F 2  95  ? 26.412  48.661  6.581   1.00 46.93  ? 97  SER   B CB    1 
ATOM   14741 O  OG    . SER   F 2  95  ? 26.703  49.558  7.659   1.00 38.46  ? 97  SER   B OG    1 
ATOM   14742 N  N     . GLY   F 2  96  ? 23.801  49.816  7.650   1.00 29.06  ? 98  GLY   B N     1 
ATOM   14743 C  CA    . GLY   F 2  96  ? 22.938  49.492  8.762   1.00 27.86  ? 98  GLY   B CA    1 
ATOM   14744 C  C     . GLY   F 2  96  ? 23.569  48.445  9.666   1.00 27.08  ? 98  GLY   B C     1 
ATOM   14745 O  O     . GLY   F 2  96  ? 24.646  47.903  9.401   1.00 31.74  ? 98  GLY   B O     1 
ATOM   14746 N  N     . ALA   F 2  97  ? 22.867  48.159  10.762  1.00 17.37  ? 99  ALA   B N     1 
ATOM   14747 C  CA    . ALA   F 2  97  ? 23.351  47.227  11.766  1.00 14.97  ? 99  ALA   B CA    1 
ATOM   14748 C  C     . ALA   F 2  97  ? 22.451  46.012  11.944  1.00 23.37  ? 99  ALA   B C     1 
ATOM   14749 O  O     . ALA   F 2  97  ? 22.769  45.140  12.767  1.00 22.13  ? 99  ALA   B O     1 
ATOM   14750 C  CB    . ALA   F 2  97  ? 23.519  47.944  13.111  1.00 19.58  ? 99  ALA   B CB    1 
ATOM   14751 N  N     . GLY   F 2  98  ? 21.339  45.932  11.203  1.00 22.62  ? 100 GLY   B N     1 
ATOM   14752 C  CA    . GLY   F 2  98  ? 20.467  44.782  11.207  1.00 8.87   ? 100 GLY   B CA    1 
ATOM   14753 C  C     . GLY   F 2  98  ? 20.149  44.182  12.559  1.00 17.19  ? 100 GLY   B C     1 
ATOM   14754 O  O     . GLY   F 2  98  ? 20.374  42.992  12.754  1.00 20.69  ? 100 GLY   B O     1 
ATOM   14755 N  N     . ASN   F 2  99  ? 19.610  44.977  13.486  1.00 23.97  ? 101 ASN   B N     1 
ATOM   14756 C  CA    . ASN   F 2  99  ? 19.179  44.522  14.817  1.00 16.46  ? 101 ASN   B CA    1 
ATOM   14757 C  C     . ASN   F 2  99  ? 20.198  43.618  15.474  1.00 17.15  ? 101 ASN   B C     1 
ATOM   14758 O  O     . ASN   F 2  99  ? 19.841  42.606  16.076  1.00 17.07  ? 101 ASN   B O     1 
ATOM   14759 C  CB    . ASN   F 2  99  ? 17.849  43.802  14.759  1.00 14.40  ? 101 ASN   B CB    1 
ATOM   14760 C  CG    . ASN   F 2  99  ? 16.708  44.731  14.511  1.00 20.63  ? 101 ASN   B CG    1 
ATOM   14761 O  OD1   . ASN   F 2  99  ? 16.593  45.788  15.138  1.00 15.45  ? 101 ASN   B OD1   1 
ATOM   14762 N  ND2   . ASN   F 2  99  ? 15.851  44.357  13.569  1.00 35.10  ? 101 ASN   B ND2   1 
ATOM   14763 N  N     . ASN   F 2  100 ? 21.476  43.993  15.352  1.00 16.89  ? 102 ASN   B N     1 
ATOM   14764 C  CA    . ASN   F 2  100 ? 22.610  43.178  15.789  1.00 17.25  ? 102 ASN   B CA    1 
ATOM   14765 C  C     . ASN   F 2  100 ? 23.521  44.047  16.643  1.00 22.19  ? 102 ASN   B C     1 
ATOM   14766 O  O     . ASN   F 2  100 ? 24.145  44.995  16.142  1.00 23.59  ? 102 ASN   B O     1 
ATOM   14767 C  CB    . ASN   F 2  100 ? 23.380  42.608  14.598  1.00 15.54  ? 102 ASN   B CB    1 
ATOM   14768 C  CG    . ASN   F 2  100 ? 24.337  41.497  15.003  1.00 21.31  ? 102 ASN   B CG    1 
ATOM   14769 O  OD1   . ASN   F 2  100 ? 24.958  41.554  16.059  1.00 24.96  ? 102 ASN   B OD1   1 
ATOM   14770 N  ND2   . ASN   F 2  100 ? 24.444  40.470  14.175  1.00 19.04  ? 102 ASN   B ND2   1 
ATOM   14771 N  N     . TRP   F 2  101 ? 23.590  43.730  17.935  1.00 22.31  ? 103 TRP   B N     1 
ATOM   14772 C  CA    . TRP   F 2  101 ? 24.446  44.492  18.840  1.00 22.32  ? 103 TRP   B CA    1 
ATOM   14773 C  C     . TRP   F 2  101 ? 25.888  44.450  18.368  1.00 21.98  ? 103 TRP   B C     1 
ATOM   14774 O  O     . TRP   F 2  101 ? 26.564  45.485  18.302  1.00 27.91  ? 103 TRP   B O     1 
ATOM   14775 C  CB    . TRP   F 2  101 ? 24.317  43.933  20.260  1.00 24.17  ? 103 TRP   B CB    1 
ATOM   14776 C  CG    . TRP   F 2  101 ? 24.887  44.794  21.328  1.00 25.49  ? 103 TRP   B CG    1 
ATOM   14777 C  CD1   . TRP   F 2  101 ? 24.272  45.842  21.943  1.00 24.67  ? 103 TRP   B CD1   1 
ATOM   14778 C  CD2   . TRP   F 2  101 ? 26.171  44.657  21.950  1.00 23.95  ? 103 TRP   B CD2   1 
ATOM   14779 N  NE1   . TRP   F 2  101 ? 25.104  46.387  22.892  1.00 23.53  ? 103 TRP   B NE1   1 
ATOM   14780 C  CE2   . TRP   F 2  101 ? 26.274  45.677  22.918  1.00 21.91  ? 103 TRP   B CE2   1 
ATOM   14781 C  CE3   . TRP   F 2  101 ? 27.258  43.790  21.761  1.00 24.25  ? 103 TRP   B CE3   1 
ATOM   14782 C  CZ2   . TRP   F 2  101 ? 27.410  45.849  23.702  1.00 20.49  ? 103 TRP   B CZ2   1 
ATOM   14783 C  CZ3   . TRP   F 2  101 ? 28.391  43.961  22.543  1.00 20.42  ? 103 TRP   B CZ3   1 
ATOM   14784 C  CH2   . TRP   F 2  101 ? 28.454  44.981  23.503  1.00 22.62  ? 103 TRP   B CH2   1 
ATOM   14785 N  N     . ALA   F 2  102 ? 26.358  43.256  17.995  1.00 21.26  ? 104 ALA   B N     1 
ATOM   14786 C  CA    . ALA   F 2  102 ? 27.747  43.048  17.606  1.00 20.19  ? 104 ALA   B CA    1 
ATOM   14787 C  C     . ALA   F 2  102 ? 28.141  43.878  16.389  1.00 17.74  ? 104 ALA   B C     1 
ATOM   14788 O  O     . ALA   F 2  102 ? 29.285  44.309  16.288  1.00 17.89  ? 104 ALA   B O     1 
ATOM   14789 C  CB    . ALA   F 2  102 ? 27.979  41.568  17.341  1.00 17.23  ? 104 ALA   B CB    1 
ATOM   14790 N  N     . LYS   F 2  103 ? 27.213  44.127  15.466  1.00 22.83  ? 105 LYS   B N     1 
ATOM   14791 C  CA    . LYS   F 2  103 ? 27.505  44.996  14.328  1.00 23.23  ? 105 LYS   B CA    1 
ATOM   14792 C  C     . LYS   F 2  103 ? 27.538  46.463  14.728  1.00 24.32  ? 105 LYS   B C     1 
ATOM   14793 O  O     . LYS   F 2  103 ? 28.260  47.263  14.114  1.00 29.76  ? 105 LYS   B O     1 
ATOM   14794 C  CB    . LYS   F 2  103 ? 26.471  44.810  13.223  1.00 15.48  ? 105 LYS   B CB    1 
ATOM   14795 C  CG    . LYS   F 2  103 ? 26.324  43.385  12.807  1.00 18.84  ? 105 LYS   B CG    1 
ATOM   14796 C  CD    . LYS   F 2  103 ? 25.293  43.221  11.703  1.00 15.86  ? 105 LYS   B CD    1 
ATOM   14797 C  CE    . LYS   F 2  103 ? 25.225  41.772  11.288  1.00 18.69  ? 105 LYS   B CE    1 
ATOM   14798 N  NZ    . LYS   F 2  103 ? 24.742  41.573  9.911   1.00 26.73  ? 105 LYS   B NZ    1 
ATOM   14799 N  N     . GLY   F 2  104 ? 26.753  46.855  15.726  1.00 21.29  ? 106 GLY   B N     1 
ATOM   14800 C  CA    . GLY   F 2  104 ? 26.794  48.244  16.140  1.00 25.63  ? 106 GLY   B CA    1 
ATOM   14801 C  C     . GLY   F 2  104 ? 28.021  48.555  16.963  1.00 22.02  ? 106 GLY   B C     1 
ATOM   14802 O  O     . GLY   F 2  104 ? 28.532  49.676  16.917  1.00 24.77  ? 106 GLY   B O     1 
ATOM   14803 N  N     . HIS   F 2  105 ? 28.524  47.567  17.696  1.00 19.10  ? 107 HIS   B N     1 
ATOM   14804 C  CA    . HIS   F 2  105 ? 29.563  47.760  18.704  1.00 22.48  ? 107 HIS   B CA    1 
ATOM   14805 C  C     . HIS   F 2  105 ? 30.954  47.494  18.182  1.00 25.18  ? 107 HIS   B C     1 
ATOM   14806 O  O     . HIS   F 2  105 ? 31.913  48.087  18.684  1.00 30.78  ? 107 HIS   B O     1 
ATOM   14807 C  CB    . HIS   F 2  105 ? 29.330  46.813  19.892  1.00 24.17  ? 107 HIS   B CB    1 
ATOM   14808 C  CG    . HIS   F 2  105 ? 29.955  47.264  21.176  1.00 29.48  ? 107 HIS   B CG    1 
ATOM   14809 N  ND1   . HIS   F 2  105 ? 29.489  48.348  21.893  1.00 29.95  ? 107 HIS   B ND1   1 
ATOM   14810 C  CD2   . HIS   F 2  105 ? 30.995  46.764  21.883  1.00 27.20  ? 107 HIS   B CD2   1 
ATOM   14811 C  CE1   . HIS   F 2  105 ? 30.214  48.490  22.988  1.00 28.47  ? 107 HIS   B CE1   1 
ATOM   14812 N  NE2   . HIS   F 2  105 ? 31.131  47.540  23.009  1.00 23.78  ? 107 HIS   B NE2   1 
ATOM   14813 N  N     . TYR   F 2  106 ? 31.074  46.619  17.181  1.00 27.48  ? 108 TYR   B N     1 
ATOM   14814 C  CA    . TYR   F 2  106 ? 32.304  45.899  16.910  1.00 19.17  ? 108 TYR   B CA    1 
ATOM   14815 C  C     . TYR   F 2  106 ? 32.764  46.006  15.477  1.00 27.64  ? 108 TYR   B C     1 
ATOM   14816 O  O     . TYR   F 2  106 ? 33.952  46.220  15.219  1.00 43.36  ? 108 TYR   B O     1 
ATOM   14817 C  CB    . TYR   F 2  106 ? 32.117  44.431  17.223  1.00 20.72  ? 108 TYR   B CB    1 
ATOM   14818 C  CG    . TYR   F 2  106 ? 32.367  44.101  18.639  1.00 23.78  ? 108 TYR   B CG    1 
ATOM   14819 C  CD1   . TYR   F 2  106 ? 33.441  44.673  19.328  1.00 27.39  ? 108 TYR   B CD1   1 
ATOM   14820 C  CD2   . TYR   F 2  106 ? 31.535  43.217  19.303  1.00 23.90  ? 108 TYR   B CD2   1 
ATOM   14821 C  CE1   . TYR   F 2  106 ? 33.672  44.377  20.666  1.00 24.26  ? 108 TYR   B CE1   1 
ATOM   14822 C  CE2   . TYR   F 2  106 ? 31.749  42.907  20.626  1.00 31.41  ? 108 TYR   B CE2   1 
ATOM   14823 C  CZ    . TYR   F 2  106 ? 32.814  43.492  21.307  1.00 30.20  ? 108 TYR   B CZ    1 
ATOM   14824 O  OH    . TYR   F 2  106 ? 32.996  43.156  22.623  1.00 25.52  ? 108 TYR   B OH    1 
ATOM   14825 N  N     . THR   F 2  107 ? 31.849  45.802  14.536  1.00 28.99  ? 109 THR   B N     1 
ATOM   14826 C  CA    . THR   F 2  107 ? 32.210  45.705  13.125  1.00 28.03  ? 109 THR   B CA    1 
ATOM   14827 C  C     . THR   F 2  107 ? 31.741  46.937  12.363  1.00 25.71  ? 109 THR   B C     1 
ATOM   14828 O  O     . THR   F 2  107 ? 32.560  47.776  11.989  1.00 34.18  ? 109 THR   B O     1 
ATOM   14829 C  CB    . THR   F 2  107 ? 31.662  44.409  12.531  1.00 22.83  ? 109 THR   B CB    1 
ATOM   14830 O  OG1   . THR   F 2  107 ? 30.239  44.430  12.540  1.00 21.25  ? 109 THR   B OG1   1 
ATOM   14831 C  CG2   . THR   F 2  107 ? 32.126  43.243  13.371  1.00 21.26  ? 109 THR   B CG2   1 
ATOM   14832 N  N     . GLU   F 2  108 ? 30.441  47.109  12.167  1.00 23.52  ? 110 GLU   B N     1 
ATOM   14833 C  CA    . GLU   F 2  108 ? 29.983  48.272  11.416  1.00 26.73  ? 110 GLU   B CA    1 
ATOM   14834 C  C     . GLU   F 2  108 ? 30.194  49.559  12.196  1.00 32.30  ? 110 GLU   B C     1 
ATOM   14835 O  O     . GLU   F 2  108 ? 30.643  50.567  11.628  1.00 27.99  ? 110 GLU   B O     1 
ATOM   14836 C  CB    . GLU   F 2  108 ? 28.520  48.097  11.060  1.00 29.32  ? 110 GLU   B CB    1 
ATOM   14837 C  CG    . GLU   F 2  108 ? 28.243  46.708  10.594  1.00 25.27  ? 110 GLU   B CG    1 
ATOM   14838 C  CD    . GLU   F 2  108 ? 28.616  46.555  9.178   1.00 28.19  ? 110 GLU   B CD    1 
ATOM   14839 O  OE1   . GLU   F 2  108 ? 27.880  47.121  8.360   1.00 29.57  ? 110 GLU   B OE1   1 
ATOM   14840 O  OE2   . GLU   F 2  108 ? 29.651  45.922  8.885   1.00 41.55  ? 110 GLU   B OE2   1 
ATOM   14841 N  N     . GLY   F 2  109 ? 29.846  49.548  13.491  1.00 27.44  ? 111 GLY   B N     1 
ATOM   14842 C  CA    . GLY   F 2  109 ? 29.950  50.746  14.296  1.00 23.10  ? 111 GLY   B CA    1 
ATOM   14843 C  C     . GLY   F 2  109 ? 31.372  51.233  14.427  1.00 36.27  ? 111 GLY   B C     1 
ATOM   14844 O  O     . GLY   F 2  109 ? 31.594  52.430  14.668  1.00 36.34  ? 111 GLY   B O     1 
ATOM   14845 N  N     . ALA   F 2  110 ? 32.343  50.328  14.259  1.00 34.45  ? 112 ALA   B N     1 
ATOM   14846 C  CA    . ALA   F 2  110 ? 33.748  50.714  14.298  1.00 34.08  ? 112 ALA   B CA    1 
ATOM   14847 C  C     . ALA   F 2  110 ? 34.067  51.731  13.208  1.00 31.53  ? 112 ALA   B C     1 
ATOM   14848 O  O     . ALA   F 2  110 ? 34.487  52.856  13.502  1.00 36.83  ? 112 ALA   B O     1 
ATOM   14849 C  CB    . ALA   F 2  110 ? 34.629  49.477  14.172  1.00 38.16  ? 112 ALA   B CB    1 
ATOM   14850 N  N     . GLU   F 2  111 ? 33.851  51.364  11.939  1.00 26.97  ? 113 GLU   B N     1 
ATOM   14851 C  CA    . GLU   F 2  111 ? 34.116  52.299  10.844  1.00 34.52  ? 113 GLU   B CA    1 
ATOM   14852 C  C     . GLU   F 2  111 ? 33.607  53.710  11.197  1.00 31.87  ? 113 GLU   B C     1 
ATOM   14853 O  O     . GLU   F 2  111 ? 34.359  54.692  11.174  1.00 34.07  ? 113 GLU   B O     1 
ATOM   14854 C  CB    . GLU   F 2  111 ? 33.485  51.803  9.510   1.00 29.15  ? 113 GLU   B CB    1 
ATOM   14855 C  CG    . GLU   F 2  111 ? 33.542  50.264  9.175   1.00 37.73  ? 113 GLU   B CG    1 
ATOM   14856 C  CD    . GLU   F 2  111 ? 33.304  49.961  7.657   1.00 57.62  ? 113 GLU   B CD    1 
ATOM   14857 O  OE1   . GLU   F 2  111 ? 33.609  50.878  6.847   1.00 46.18  ? 113 GLU   B OE1   1 
ATOM   14858 O  OE2   . GLU   F 2  111 ? 32.823  48.836  7.275   1.00 38.99  ? 113 GLU   B OE2   1 
ATOM   14859 N  N     . LEU   F 2  112 ? 32.338  53.816  11.589  1.00 28.37  ? 114 LEU   B N     1 
ATOM   14860 C  CA    . LEU   F 2  112 ? 31.675  55.110  11.671  1.00 26.63  ? 114 LEU   B CA    1 
ATOM   14861 C  C     . LEU   F 2  112 ? 32.052  55.915  12.902  1.00 30.39  ? 114 LEU   B C     1 
ATOM   14862 O  O     . LEU   F 2  112 ? 31.902  57.141  12.878  1.00 31.57  ? 114 LEU   B O     1 
ATOM   14863 C  CB    . LEU   F 2  112 ? 30.161  54.910  11.653  1.00 23.85  ? 114 LEU   B CB    1 
ATOM   14864 C  CG    . LEU   F 2  112 ? 29.238  56.112  11.809  1.00 21.19  ? 114 LEU   B CG    1 
ATOM   14865 C  CD1   . LEU   F 2  112 ? 29.434  57.083  10.686  1.00 20.41  ? 114 LEU   B CD1   1 
ATOM   14866 C  CD2   . LEU   F 2  112 ? 27.781  55.635  11.872  1.00 27.69  ? 114 LEU   B CD2   1 
ATOM   14867 N  N     . VAL   F 2  113 ? 32.551  55.265  13.959  1.00 30.34  ? 115 VAL   B N     1 
ATOM   14868 C  CA    . VAL   F 2  113 ? 32.558  55.872  15.293  1.00 28.71  ? 115 VAL   B CA    1 
ATOM   14869 C  C     . VAL   F 2  113 ? 33.449  57.119  15.340  1.00 30.46  ? 115 VAL   B C     1 
ATOM   14870 O  O     . VAL   F 2  113 ? 33.037  58.181  15.828  1.00 28.92  ? 115 VAL   B O     1 
ATOM   14871 C  CB    . VAL   F 2  113 ? 32.977  54.827  16.341  1.00 25.12  ? 115 VAL   B CB    1 
ATOM   14872 C  CG1   . VAL   F 2  113 ? 34.432  54.495  16.204  1.00 28.47  ? 115 VAL   B CG1   1 
ATOM   14873 C  CG2   . VAL   F 2  113 ? 32.682  55.309  17.725  1.00 22.70  ? 115 VAL   B CG2   1 
ATOM   14874 N  N     . ASP   F 2  114 ? 34.695  57.009  14.874  1.00 34.09  ? 116 ASP   B N     1 
ATOM   14875 C  CA    . ASP   F 2  114 ? 35.573  58.166  14.987  1.00 26.94  ? 116 ASP   B CA    1 
ATOM   14876 C  C     . ASP   F 2  114 ? 34.937  59.382  14.350  1.00 27.49  ? 116 ASP   B C     1 
ATOM   14877 O  O     . ASP   F 2  114 ? 35.143  60.507  14.804  1.00 33.30  ? 116 ASP   B O     1 
ATOM   14878 C  CB    . ASP   F 2  114 ? 36.933  57.893  14.356  1.00 19.54  ? 116 ASP   B CB    1 
ATOM   14879 C  CG    . ASP   F 2  114 ? 37.661  56.764  15.018  1.00 33.40  ? 116 ASP   B CG    1 
ATOM   14880 O  OD1   . ASP   F 2  114 ? 37.155  56.250  16.038  1.00 36.67  ? 116 ASP   B OD1   1 
ATOM   14881 O  OD2   . ASP   F 2  114 ? 38.743  56.385  14.520  1.00 49.03  ? 116 ASP   B OD2   1 
ATOM   14882 N  N     . SER   F 2  115 ? 34.151  59.186  13.309  1.00 24.94  ? 117 SER   B N     1 
ATOM   14883 C  CA    . SER   F 2  115 ? 33.509  60.334  12.701  1.00 20.73  ? 117 SER   B CA    1 
ATOM   14884 C  C     . SER   F 2  115 ? 32.489  60.922  13.650  1.00 24.36  ? 117 SER   B C     1 
ATOM   14885 O  O     . SER   F 2  115 ? 32.324  62.140  13.713  1.00 30.28  ? 117 SER   B O     1 
ATOM   14886 C  CB    . SER   F 2  115 ? 32.891  59.917  11.374  1.00 29.02  ? 117 SER   B CB    1 
ATOM   14887 O  OG    . SER   F 2  115 ? 33.535  58.723  10.907  1.00 35.91  ? 117 SER   B OG    1 
ATOM   14888 N  N     . VAL   F 2  116 ? 31.829  60.078  14.437  1.00 29.33  ? 118 VAL   B N     1 
ATOM   14889 C  CA    . VAL   F 2  116 ? 30.954  60.585  15.486  1.00 25.80  ? 118 VAL   B CA    1 
ATOM   14890 C  C     . VAL   F 2  116 ? 31.771  61.313  16.554  1.00 25.73  ? 118 VAL   B C     1 
ATOM   14891 O  O     . VAL   F 2  116 ? 31.429  62.429  16.962  1.00 24.31  ? 118 VAL   B O     1 
ATOM   14892 C  CB    . VAL   F 2  116 ? 30.101  59.447  16.079  1.00 24.11  ? 118 VAL   B CB    1 
ATOM   14893 C  CG1   . VAL   F 2  116 ? 29.290  59.953  17.285  1.00 26.38  ? 118 VAL   B CG1   1 
ATOM   14894 C  CG2   . VAL   F 2  116 ? 29.149  58.898  15.037  1.00 23.66  ? 118 VAL   B CG2   1 
ATOM   14895 N  N     . LEU   F 2  117 ? 32.874  60.716  17.011  1.00 25.93  ? 119 LEU   B N     1 
ATOM   14896 C  CA    . LEU   F 2  117 ? 33.612  61.346  18.107  1.00 26.86  ? 119 LEU   B CA    1 
ATOM   14897 C  C     . LEU   F 2  117 ? 34.165  62.721  17.725  1.00 34.93  ? 119 LEU   B C     1 
ATOM   14898 O  O     . LEU   F 2  117 ? 34.213  63.612  18.581  1.00 43.05  ? 119 LEU   B O     1 
ATOM   14899 C  CB    . LEU   F 2  117 ? 34.731  60.438  18.583  1.00 24.40  ? 119 LEU   B CB    1 
ATOM   14900 C  CG    . LEU   F 2  117 ? 34.186  59.161  19.190  1.00 31.66  ? 119 LEU   B CG    1 
ATOM   14901 C  CD1   . LEU   F 2  117 ? 35.257  58.085  19.247  1.00 30.39  ? 119 LEU   B CD1   1 
ATOM   14902 C  CD2   . LEU   F 2  117 ? 33.607  59.439  20.579  1.00 26.05  ? 119 LEU   B CD2   1 
ATOM   14903 N  N     . ASP   F 2  118 ? 34.565  62.924  16.456  1.00 32.05  ? 120 ASP   B N     1 
ATOM   14904 C  CA    . ASP   F 2  118 ? 35.010  64.245  15.988  1.00 27.75  ? 120 ASP   B CA    1 
ATOM   14905 C  C     . ASP   F 2  118 ? 33.974  65.329  16.268  1.00 31.13  ? 120 ASP   B C     1 
ATOM   14906 O  O     . ASP   F 2  118 ? 34.308  66.420  16.752  1.00 33.63  ? 120 ASP   B O     1 
ATOM   14907 C  CB    . ASP   F 2  118 ? 35.268  64.223  14.492  1.00 31.48  ? 120 ASP   B CB    1 
ATOM   14908 C  CG    . ASP   F 2  118 ? 36.504  63.511  14.132  1.00 37.59  ? 120 ASP   B CG    1 
ATOM   14909 O  OD1   . ASP   F 2  118 ? 37.265  63.172  15.074  1.00 42.96  ? 120 ASP   B OD1   1 
ATOM   14910 O  OD2   . ASP   F 2  118 ? 36.698  63.314  12.902  1.00 27.91  ? 120 ASP   B OD2   1 
ATOM   14911 N  N     . VAL   F 2  119 ? 32.716  65.072  15.904  1.00 24.19  ? 121 VAL   B N     1 
ATOM   14912 C  CA    . VAL   F 2  119 ? 31.686  66.057  16.189  1.00 23.98  ? 121 VAL   B CA    1 
ATOM   14913 C  C     . VAL   F 2  119 ? 31.477  66.194  17.681  1.00 34.67  ? 121 VAL   B C     1 
ATOM   14914 O  O     . VAL   F 2  119 ? 31.062  67.256  18.154  1.00 42.15  ? 121 VAL   B O     1 
ATOM   14915 C  CB    . VAL   F 2  119 ? 30.380  65.690  15.488  1.00 21.71  ? 121 VAL   B CB    1 
ATOM   14916 C  CG1   . VAL   F 2  119 ? 29.417  66.838  15.527  1.00 26.75  ? 121 VAL   B CG1   1 
ATOM   14917 C  CG2   . VAL   F 2  119 ? 30.674  65.291  14.087  1.00 25.01  ? 121 VAL   B CG2   1 
ATOM   14918 N  N     . VAL   F 2  120 ? 31.739  65.137  18.456  1.00 28.31  ? 122 VAL   B N     1 
ATOM   14919 C  CA    . VAL   F 2  120 ? 31.534  65.251  19.892  1.00 27.35  ? 122 VAL   B CA    1 
ATOM   14920 C  C     . VAL   F 2  120 ? 32.623  66.116  20.494  1.00 38.31  ? 122 VAL   B C     1 
ATOM   14921 O  O     . VAL   F 2  120 ? 32.363  66.942  21.381  1.00 39.12  ? 122 VAL   B O     1 
ATOM   14922 C  CB    . VAL   F 2  120 ? 31.463  63.861  20.547  1.00 31.53  ? 122 VAL   B CB    1 
ATOM   14923 C  CG1   . VAL   F 2  120 ? 31.402  63.972  22.066  1.00 22.68  ? 122 VAL   B CG1   1 
ATOM   14924 C  CG2   . VAL   F 2  120 ? 30.250  63.108  20.032  1.00 36.95  ? 122 VAL   B CG2   1 
ATOM   14925 N  N     . ARG   F 2  121 ? 33.854  65.952  20.003  1.00 40.80  ? 123 ARG   B N     1 
ATOM   14926 C  CA    . ARG   F 2  121 ? 34.950  66.843  20.366  1.00 38.08  ? 123 ARG   B CA    1 
ATOM   14927 C  C     . ARG   F 2  121 ? 34.640  68.275  19.967  1.00 44.07  ? 123 ARG   B C     1 
ATOM   14928 O  O     . ARG   F 2  121 ? 34.748  69.195  20.787  1.00 48.94  ? 123 ARG   B O     1 
ATOM   14929 C  CB    . ARG   F 2  121 ? 36.230  66.385  19.680  1.00 31.79  ? 123 ARG   B CB    1 
ATOM   14930 C  CG    . ARG   F 2  121 ? 37.506  66.607  20.443  1.00 41.60  ? 123 ARG   B CG    1 
ATOM   14931 C  CD    . ARG   F 2  121 ? 38.255  65.298  20.413  1.00 43.02  ? 123 ARG   B CD    1 
ATOM   14932 N  NE    . ARG   F 2  121 ? 38.110  64.736  19.075  1.00 60.23  ? 123 ARG   B NE    1 
ATOM   14933 C  CZ    . ARG   F 2  121 ? 38.055  63.445  18.779  1.00 55.58  ? 123 ARG   B CZ    1 
ATOM   14934 N  NH1   . ARG   F 2  121 ? 38.152  62.514  19.717  1.00 49.90  ? 123 ARG   B NH1   1 
ATOM   14935 N  NH2   . ARG   F 2  121 ? 37.879  63.080  17.508  1.00 52.94  ? 123 ARG   B NH2   1 
ATOM   14936 N  N     . LYS   F 2  122 ? 34.267  68.486  18.697  1.00 39.27  ? 124 LYS   B N     1 
ATOM   14937 C  CA    . LYS   F 2  122 ? 34.042  69.844  18.203  1.00 38.11  ? 124 LYS   B CA    1 
ATOM   14938 C  C     . LYS   F 2  122 ? 32.980  70.551  19.025  1.00 42.92  ? 124 LYS   B C     1 
ATOM   14939 O  O     . LYS   F 2  122 ? 33.075  71.760  19.273  1.00 44.43  ? 124 LYS   B O     1 
ATOM   14940 C  CB    . LYS   F 2  122 ? 33.634  69.820  16.728  1.00 44.78  ? 124 LYS   B CB    1 
ATOM   14941 C  CG    . LYS   F 2  122 ? 33.427  71.206  16.104  1.00 45.88  ? 124 LYS   B CG    1 
ATOM   14942 C  CD    . LYS   F 2  122 ? 32.251  71.212  15.136  1.00 56.12  ? 124 LYS   B CD    1 
ATOM   14943 C  CE    . LYS   F 2  122 ? 30.947  70.749  15.813  1.00 57.55  ? 124 LYS   B CE    1 
ATOM   14944 N  NZ    . LYS   F 2  122 ? 29.844  70.354  14.852  1.00 47.49  ? 124 LYS   B NZ    1 
ATOM   14945 N  N     . GLU   F 2  123 ? 31.957  69.806  19.452  1.00 46.54  ? 125 GLU   B N     1 
ATOM   14946 C  CA    . GLU   F 2  123 ? 30.923  70.349  20.327  1.00 43.45  ? 125 GLU   B CA    1 
ATOM   14947 C  C     . GLU   F 2  123 ? 31.450  70.563  21.743  1.00 37.16  ? 125 GLU   B C     1 
ATOM   14948 O  O     . GLU   F 2  123 ? 31.264  71.632  22.329  1.00 39.40  ? 125 GLU   B O     1 
ATOM   14949 C  CB    . GLU   F 2  123 ? 29.719  69.413  20.322  1.00 36.23  ? 125 GLU   B CB    1 
ATOM   14950 C  CG    . GLU   F 2  123 ? 28.807  69.649  19.145  1.00 32.54  ? 125 GLU   B CG    1 
ATOM   14951 C  CD    . GLU   F 2  123 ? 28.151  71.001  19.227  1.00 41.99  ? 125 GLU   B CD    1 
ATOM   14952 O  OE1   . GLU   F 2  123 ? 28.396  71.708  20.236  1.00 43.47  ? 125 GLU   B OE1   1 
ATOM   14953 O  OE2   . GLU   F 2  123 ? 27.395  71.355  18.297  1.00 42.55  ? 125 GLU   B OE2   1 
ATOM   14954 N  N     . SER   F 2  124 ? 32.120  69.554  22.301  1.00 35.65  ? 126 SER   B N     1 
ATOM   14955 C  CA    . SER   F 2  124 ? 32.673  69.670  23.644  1.00 35.15  ? 126 SER   B CA    1 
ATOM   14956 C  C     . SER   F 2  124 ? 33.717  70.767  23.726  1.00 42.41  ? 126 SER   B C     1 
ATOM   14957 O  O     . SER   F 2  124 ? 33.801  71.488  24.726  1.00 40.35  ? 126 SER   B O     1 
ATOM   14958 C  CB    . SER   F 2  124 ? 33.289  68.341  24.067  1.00 34.63  ? 126 SER   B CB    1 
ATOM   14959 O  OG    . SER   F 2  124 ? 32.287  67.352  24.225  1.00 39.26  ? 126 SER   B OG    1 
ATOM   14960 N  N     . GLU   F 2  125 ? 34.554  70.881  22.702  1.00 52.31  ? 127 GLU   B N     1 
ATOM   14961 C  CA    . GLU   F 2  125 ? 35.660  71.822  22.779  1.00 55.06  ? 127 GLU   B CA    1 
ATOM   14962 C  C     . GLU   F 2  125 ? 35.181  73.258  22.911  1.00 45.45  ? 127 GLU   B C     1 
ATOM   14963 O  O     . GLU   F 2  125 ? 35.934  74.101  23.401  1.00 47.27  ? 127 GLU   B O     1 
ATOM   14964 C  CB    . GLU   F 2  125 ? 36.561  71.663  21.552  1.00 58.50  ? 127 GLU   B CB    1 
ATOM   14965 C  CG    . GLU   F 2  125 ? 37.224  70.293  21.456  1.00 57.55  ? 127 GLU   B CG    1 
ATOM   14966 C  CD    . GLU   F 2  125 ? 38.242  70.052  22.560  1.00 72.90  ? 127 GLU   B CD    1 
ATOM   14967 O  OE1   . GLU   F 2  125 ? 39.272  70.774  22.580  1.00 86.84  ? 127 GLU   B OE1   1 
ATOM   14968 O  OE2   . GLU   F 2  125 ? 38.005  69.149  23.403  1.00 52.13  ? 127 GLU   B OE2   1 
ATOM   14969 N  N     . SER   F 2  126 ? 33.958  73.559  22.481  1.00 40.87  ? 128 SER   B N     1 
ATOM   14970 C  CA    . SER   F 2  126 ? 33.408  74.906  22.596  1.00 39.92  ? 128 SER   B CA    1 
ATOM   14971 C  C     . SER   F 2  126 ? 32.415  75.000  23.748  1.00 43.71  ? 128 SER   B C     1 
ATOM   14972 O  O     . SER   F 2  126 ? 31.366  75.650  23.651  1.00 55.01  ? 128 SER   B O     1 
ATOM   14973 C  CB    . SER   F 2  126 ? 32.774  75.345  21.273  1.00 41.41  ? 128 SER   B CB    1 
ATOM   14974 O  OG    . SER   F 2  126 ? 31.419  74.951  21.165  1.00 43.06  ? 128 SER   B OG    1 
ATOM   14975 N  N     . CYS   F 2  127 ? 32.727  74.346  24.860  1.00 43.58  ? 129 CYS   B N     1 
ATOM   14976 C  CA    . CYS   F 2  127 ? 31.916  74.404  26.067  1.00 42.49  ? 129 CYS   B CA    1 
ATOM   14977 C  C     . CYS   F 2  127 ? 32.723  75.055  27.180  1.00 42.78  ? 129 CYS   B C     1 
ATOM   14978 O  O     . CYS   F 2  127 ? 33.844  74.617  27.472  1.00 43.02  ? 129 CYS   B O     1 
ATOM   14979 C  CB    . CYS   F 2  127 ? 31.472  73.005  26.497  1.00 33.67  ? 129 CYS   B CB    1 
ATOM   14980 S  SG    . CYS   F 2  127 ? 29.938  72.471  25.782  1.00 42.52  ? 129 CYS   B SG    1 
ATOM   14981 N  N     . ASP   F 2  128 ? 32.151  76.097  27.801  1.00 39.26  ? 130 ASP   B N     1 
ATOM   14982 C  CA    . ASP   F 2  128 ? 32.793  76.682  28.977  1.00 41.01  ? 130 ASP   B CA    1 
ATOM   14983 C  C     . ASP   F 2  128 ? 32.800  75.702  30.142  1.00 42.27  ? 130 ASP   B C     1 
ATOM   14984 O  O     . ASP   F 2  128 ? 33.817  75.549  30.826  1.00 36.15  ? 130 ASP   B O     1 
ATOM   14985 C  CB    . ASP   F 2  128 ? 32.110  77.989  29.395  1.00 51.66  ? 130 ASP   B CB    1 
ATOM   14986 C  CG    . ASP   F 2  128 ? 32.223  79.079  28.340  1.00 67.82  ? 130 ASP   B CG    1 
ATOM   14987 O  OD1   . ASP   F 2  128 ? 31.255  79.856  28.202  1.00 62.89  ? 130 ASP   B OD1   1 
ATOM   14988 O  OD2   . ASP   F 2  128 ? 33.261  79.159  27.640  1.00 77.33  ? 130 ASP   B OD2   1 
ATOM   14989 N  N     . CYS   F 2  129 ? 31.670  75.009  30.376  1.00 47.71  ? 131 CYS   B N     1 
ATOM   14990 C  CA    . CYS   F 2  129 ? 31.543  74.076  31.487  1.00 44.56  ? 131 CYS   B CA    1 
ATOM   14991 C  C     . CYS   F 2  129 ? 30.716  72.867  31.031  1.00 44.72  ? 131 CYS   B C     1 
ATOM   14992 O  O     . CYS   F 2  129 ? 29.581  72.651  31.442  1.00 51.09  ? 131 CYS   B O     1 
ATOM   14993 C  CB    . CYS   F 2  129 ? 30.913  74.754  32.709  1.00 49.65  ? 131 CYS   B CB    1 
ATOM   14994 S  SG    . CYS   F 2  129 ? 31.406  74.066  34.302  1.00 53.18  ? 131 CYS   B SG    1 
ATOM   14995 N  N     . LEU   F 2  130 ? 31.293  72.040  30.170  1.00 40.09  ? 132 LEU   B N     1 
ATOM   14996 C  CA    . LEU   F 2  130 ? 30.668  70.766  29.846  1.00 38.34  ? 132 LEU   B CA    1 
ATOM   14997 C  C     . LEU   F 2  130 ? 30.355  70.003  31.126  1.00 39.11  ? 132 LEU   B C     1 
ATOM   14998 O  O     . LEU   F 2  130 ? 31.257  69.715  31.920  1.00 40.51  ? 132 LEU   B O     1 
ATOM   14999 C  CB    . LEU   F 2  130 ? 31.606  69.944  28.962  1.00 37.08  ? 132 LEU   B CB    1 
ATOM   15000 C  CG    . LEU   F 2  130 ? 31.132  68.603  28.439  1.00 20.45  ? 132 LEU   B CG    1 
ATOM   15001 C  CD1   . LEU   F 2  130 ? 30.276  68.824  27.232  1.00 26.49  ? 132 LEU   B CD1   1 
ATOM   15002 C  CD2   . LEU   F 2  130 ? 32.331  67.823  28.115  1.00 21.42  ? 132 LEU   B CD2   1 
ATOM   15003 N  N     . GLN   F 2  131 ? 29.079  69.673  31.342  1.00 27.70  ? 133 GLN   B N     1 
ATOM   15004 C  CA    . GLN   F 2  131 ? 28.763  68.885  32.520  1.00 35.17  ? 133 GLN   B CA    1 
ATOM   15005 C  C     . GLN   F 2  131 ? 28.656  67.396  32.222  1.00 34.49  ? 133 GLN   B C     1 
ATOM   15006 O  O     . GLN   F 2  131 ? 28.800  66.572  33.139  1.00 31.01  ? 133 GLN   B O     1 
ATOM   15007 C  CB    . GLN   F 2  131 ? 27.484  69.395  33.183  1.00 30.37  ? 133 GLN   B CB    1 
ATOM   15008 C  CG    . GLN   F 2  131 ? 26.339  69.694  32.273  1.00 31.43  ? 133 GLN   B CG    1 
ATOM   15009 C  CD    . GLN   F 2  131 ? 25.103  70.143  33.062  1.00 31.01  ? 133 GLN   B CD    1 
ATOM   15010 O  OE1   . GLN   F 2  131 ? 24.830  69.646  34.160  1.00 28.08  ? 133 GLN   B OE1   1 
ATOM   15011 N  NE2   . GLN   F 2  131 ? 24.360  71.089  32.506  1.00 29.43  ? 133 GLN   B NE2   1 
ATOM   15012 N  N     . GLY   F 2  132 ? 28.473  67.034  30.968  1.00 31.70  ? 134 GLY   B N     1 
ATOM   15013 C  CA    . GLY   F 2  132 ? 28.377  65.645  30.581  1.00 26.51  ? 134 GLY   B CA    1 
ATOM   15014 C  C     . GLY   F 2  132 ? 27.565  65.527  29.314  1.00 26.31  ? 134 GLY   B C     1 
ATOM   15015 O  O     . GLY   F 2  132 ? 27.342  66.501  28.607  1.00 23.95  ? 134 GLY   B O     1 
ATOM   15016 N  N     . PHE   F 2  133 ? 27.111  64.309  29.059  1.00 30.46  ? 135 PHE   B N     1 
ATOM   15017 C  CA    . PHE   F 2  133 ? 26.385  63.991  27.843  1.00 23.83  ? 135 PHE   B CA    1 
ATOM   15018 C  C     . PHE   F 2  133 ? 25.085  63.290  28.203  1.00 27.31  ? 135 PHE   B C     1 
ATOM   15019 O  O     . PHE   F 2  133 ? 24.965  62.666  29.262  1.00 26.12  ? 135 PHE   B O     1 
ATOM   15020 C  CB    . PHE   F 2  133 ? 27.209  63.103  26.934  1.00 19.60  ? 135 PHE   B CB    1 
ATOM   15021 C  CG    . PHE   F 2  133 ? 28.643  63.482  26.863  1.00 20.36  ? 135 PHE   B CG    1 
ATOM   15022 C  CD1   . PHE   F 2  133 ? 29.518  63.127  27.872  1.00 21.69  ? 135 PHE   B CD1   1 
ATOM   15023 C  CD2   . PHE   F 2  133 ? 29.118  64.192  25.782  1.00 21.36  ? 135 PHE   B CD2   1 
ATOM   15024 C  CE1   . PHE   F 2  133 ? 30.846  63.496  27.813  1.00 25.92  ? 135 PHE   B CE1   1 
ATOM   15025 C  CE2   . PHE   F 2  133 ? 30.444  64.566  25.715  1.00 28.71  ? 135 PHE   B CE2   1 
ATOM   15026 C  CZ    . PHE   F 2  133 ? 31.314  64.216  26.728  1.00 28.25  ? 135 PHE   B CZ    1 
ATOM   15027 N  N     . GLN   F 2  134 ? 24.105  63.385  27.318  1.00 21.87  ? 136 GLN   B N     1 
ATOM   15028 C  CA    . GLN   F 2  134 ? 22.919  62.563  27.459  1.00 24.24  ? 136 GLN   B CA    1 
ATOM   15029 C  C     . GLN   F 2  134 ? 22.646  61.915  26.118  1.00 24.48  ? 136 GLN   B C     1 
ATOM   15030 O  O     . GLN   F 2  134 ? 22.517  62.612  25.111  1.00 26.51  ? 136 GLN   B O     1 
ATOM   15031 C  CB    . GLN   F 2  134 ? 21.723  63.378  27.942  1.00 28.50  ? 136 GLN   B CB    1 
ATOM   15032 C  CG    . GLN   F 2  134 ? 21.137  64.338  26.943  1.00 22.17  ? 136 GLN   B CG    1 
ATOM   15033 C  CD    . GLN   F 2  134 ? 19.828  64.893  27.452  1.00 20.92  ? 136 GLN   B CD    1 
ATOM   15034 O  OE1   . GLN   F 2  134 ? 19.523  64.775  28.620  1.00 29.92  ? 136 GLN   B OE1   1 
ATOM   15035 N  NE2   . GLN   F 2  134 ? 19.054  65.487  26.581  1.00 23.82  ? 136 GLN   B NE2   1 
ATOM   15036 N  N     . LEU   F 2  135 ? 22.585  60.586  26.099  1.00 25.22  ? 137 LEU   B N     1 
ATOM   15037 C  CA    . LEU   F 2  135 ? 22.338  59.836  24.879  1.00 23.75  ? 137 LEU   B CA    1 
ATOM   15038 C  C     . LEU   F 2  135 ? 20.941  59.231  24.901  1.00 28.04  ? 137 LEU   B C     1 
ATOM   15039 O  O     . LEU   F 2  135 ? 20.539  58.598  25.891  1.00 24.87  ? 137 LEU   B O     1 
ATOM   15040 C  CB    . LEU   F 2  135 ? 23.374  58.727  24.691  1.00 22.71  ? 137 LEU   B CB    1 
ATOM   15041 C  CG    . LEU   F 2  135 ? 22.872  57.566  23.819  1.00 22.01  ? 137 LEU   B CG    1 
ATOM   15042 C  CD1   . LEU   F 2  135 ? 23.340  57.713  22.385  1.00 18.51  ? 137 LEU   B CD1   1 
ATOM   15043 C  CD2   . LEU   F 2  135 ? 23.322  56.260  24.389  1.00 22.76  ? 137 LEU   B CD2   1 
ATOM   15044 N  N     . THR   F 2  136 ? 20.216  59.410  23.800  1.00 20.99  ? 138 THR   B N     1 
ATOM   15045 C  CA    . THR   F 2  136 ? 18.990  58.668  23.560  1.00 20.23  ? 138 THR   B CA    1 
ATOM   15046 C  C     . THR   F 2  136 ? 19.263  57.492  22.624  1.00 24.31  ? 138 THR   B C     1 
ATOM   15047 O  O     . THR   F 2  136 ? 19.943  57.634  21.599  1.00 21.77  ? 138 THR   B O     1 
ATOM   15048 C  CB    . THR   F 2  136 ? 17.901  59.563  22.977  1.00 21.07  ? 138 THR   B CB    1 
ATOM   15049 O  OG1   . THR   F 2  136 ? 18.378  60.170  21.773  1.00 28.64  ? 138 THR   B OG1   1 
ATOM   15050 C  CG2   . THR   F 2  136 ? 17.511  60.633  23.976  1.00 22.15  ? 138 THR   B CG2   1 
ATOM   15051 N  N     . HIS   F 2  137 ? 18.733  56.325  22.990  1.00 19.88  ? 139 HIS   B N     1 
ATOM   15052 C  CA    . HIS   F 2  137 ? 18.884  55.127  22.181  1.00 20.72  ? 139 HIS   B CA    1 
ATOM   15053 C  C     . HIS   F 2  137 ? 17.918  54.069  22.698  1.00 20.54  ? 139 HIS   B C     1 
ATOM   15054 O  O     . HIS   F 2  137 ? 17.302  54.223  23.758  1.00 21.78  ? 139 HIS   B O     1 
ATOM   15055 C  CB    . HIS   F 2  137 ? 20.327  54.621  22.209  1.00 16.45  ? 139 HIS   B CB    1 
ATOM   15056 C  CG    . HIS   F 2  137 ? 20.764  54.143  23.560  1.00 24.08  ? 139 HIS   B CG    1 
ATOM   15057 N  ND1   . HIS   F 2  137 ? 21.793  53.241  23.739  1.00 21.68  ? 139 HIS   B ND1   1 
ATOM   15058 C  CD2   . HIS   F 2  137 ? 20.309  54.443  24.800  1.00 20.53  ? 139 HIS   B CD2   1 
ATOM   15059 C  CE1   . HIS   F 2  137 ? 21.952  53.009  25.030  1.00 22.42  ? 139 HIS   B CE1   1 
ATOM   15060 N  NE2   . HIS   F 2  137 ? 21.066  53.729  25.696  1.00 19.89  ? 139 HIS   B NE2   1 
ATOM   15061 N  N     . SER   F 2  138 ? 17.804  52.989  21.925  1.00 17.84  ? 140 SER   B N     1 
ATOM   15062 C  CA    . SER   F 2  138 ? 17.125  51.754  22.289  1.00 18.38  ? 140 SER   B CA    1 
ATOM   15063 C  C     . SER   F 2  138 ? 18.145  50.684  22.635  1.00 19.55  ? 140 SER   B C     1 
ATOM   15064 O  O     . SER   F 2  138 ? 19.304  50.747  22.229  1.00 20.91  ? 140 SER   B O     1 
ATOM   15065 C  CB    . SER   F 2  138 ? 16.262  51.256  21.144  1.00 14.65  ? 140 SER   B CB    1 
ATOM   15066 O  OG    . SER   F 2  138 ? 16.976  51.469  19.945  1.00 35.45  ? 140 SER   B OG    1 
ATOM   15067 N  N     . LEU   F 2  139 ? 17.696  49.684  23.385  1.00 19.14  ? 141 LEU   B N     1 
ATOM   15068 C  CA    . LEU   F 2  139 ? 18.577  48.621  23.833  1.00 16.35  ? 141 LEU   B CA    1 
ATOM   15069 C  C     . LEU   F 2  139 ? 18.325  47.317  23.108  1.00 18.24  ? 141 LEU   B C     1 
ATOM   15070 O  O     . LEU   F 2  139 ? 19.171  46.419  23.181  1.00 18.30  ? 141 LEU   B O     1 
ATOM   15071 C  CB    . LEU   F 2  139 ? 18.440  48.397  25.354  1.00 16.35  ? 141 LEU   B CB    1 
ATOM   15072 C  CG    . LEU   F 2  139 ? 18.709  49.578  26.285  1.00 13.82  ? 141 LEU   B CG    1 
ATOM   15073 C  CD1   . LEU   F 2  139 ? 18.961  49.095  27.711  1.00 13.33  ? 141 LEU   B CD1   1 
ATOM   15074 C  CD2   . LEU   F 2  139 ? 19.872  50.410  25.777  1.00 9.31   ? 141 LEU   B CD2   1 
ATOM   15075 N  N     . GLY   F 2  140 ? 17.196  47.196  22.403  1.00 14.01  ? 142 GLY   B N     1 
ATOM   15076 C  CA    . GLY   F 2  140 ? 16.842  45.970  21.727  1.00 11.34  ? 142 GLY   B CA    1 
ATOM   15077 C  C     . GLY   F 2  140 ? 17.327  45.834  20.303  1.00 14.48  ? 142 GLY   B C     1 
ATOM   15078 O  O     . GLY   F 2  140 ? 17.256  44.738  19.738  1.00 18.80  ? 142 GLY   B O     1 
ATOM   15079 N  N     . GLY   F 2  141 ? 17.811  46.905  19.690  1.00 18.42  ? 143 GLY   B N     1 
ATOM   15080 C  CA    . GLY   F 2  141 ? 18.282  46.854  18.318  1.00 16.12  ? 143 GLY   B CA    1 
ATOM   15081 C  C     . GLY   F 2  141 ? 19.784  46.686  18.222  1.00 20.88  ? 143 GLY   B C     1 
ATOM   15082 O  O     . GLY   F 2  141 ? 20.435  46.126  19.115  1.00 23.36  ? 143 GLY   B O     1 
ATOM   15083 N  N     . GLY   F 2  142 ? 20.348  47.193  17.134  1.00 15.00  ? 144 GLY   B N     1 
ATOM   15084 C  CA    . GLY   F 2  142 ? 21.749  46.981  16.894  1.00 15.21  ? 144 GLY   B CA    1 
ATOM   15085 C  C     . GLY   F 2  142 ? 22.588  48.231  16.888  1.00 16.96  ? 144 GLY   B C     1 
ATOM   15086 O  O     . GLY   F 2  142 ? 23.687  48.215  17.437  1.00 17.08  ? 144 GLY   B O     1 
ATOM   15087 N  N     . THR   F 2  143 ? 22.121  49.303  16.238  1.00 18.03  ? 145 THR   B N     1 
ATOM   15088 C  CA    . THR   F 2  143 ? 22.905  50.539  16.209  1.00 15.85  ? 145 THR   B CA    1 
ATOM   15089 C  C     . THR   F 2  143 ? 22.884  51.234  17.563  1.00 17.19  ? 145 THR   B C     1 
ATOM   15090 O  O     . THR   F 2  143 ? 23.919  51.365  18.218  1.00 24.20  ? 145 THR   B O     1 
ATOM   15091 C  CB    . THR   F 2  143 ? 22.398  51.493  15.131  1.00 15.47  ? 145 THR   B CB    1 
ATOM   15092 O  OG1   . THR   F 2  143 ? 22.741  50.976  13.848  1.00 12.94  ? 145 THR   B OG1   1 
ATOM   15093 C  CG2   . THR   F 2  143 ? 23.022  52.873  15.334  1.00 15.18  ? 145 THR   B CG2   1 
ATOM   15094 N  N     . GLY   F 2  144 ? 21.711  51.704  17.989  1.00 18.08  ? 146 GLY   B N     1 
ATOM   15095 C  CA    . GLY   F 2  144 ? 21.645  52.435  19.239  1.00 17.37  ? 146 GLY   B CA    1 
ATOM   15096 C  C     . GLY   F 2  144 ? 22.079  51.582  20.407  1.00 18.19  ? 146 GLY   B C     1 
ATOM   15097 O  O     . GLY   F 2  144 ? 22.767  52.047  21.314  1.00 21.47  ? 146 GLY   B O     1 
ATOM   15098 N  N     . SER   F 2  145 ? 21.677  50.320  20.399  1.00 20.53  ? 147 SER   B N     1 
ATOM   15099 C  CA    . SER   F 2  145 ? 22.092  49.390  21.434  1.00 15.08  ? 147 SER   B CA    1 
ATOM   15100 C  C     . SER   F 2  145 ? 23.605  49.238  21.445  1.00 21.18  ? 147 SER   B C     1 
ATOM   15101 O  O     . SER   F 2  145 ? 24.264  49.417  22.482  1.00 15.62  ? 147 SER   B O     1 
ATOM   15102 C  CB    . SER   F 2  145 ? 21.410  48.046  21.174  1.00 19.26  ? 147 SER   B CB    1 
ATOM   15103 O  OG    . SER   F 2  145 ? 21.664  47.098  22.181  1.00 25.41  ? 147 SER   B OG    1 
ATOM   15104 N  N     . GLY   F 2  146 ? 24.170  48.904  20.280  1.00 23.05  ? 148 GLY   B N     1 
ATOM   15105 C  CA    . GLY   F 2  146 ? 25.518  48.384  20.156  1.00 18.56  ? 148 GLY   B CA    1 
ATOM   15106 C  C     . GLY   F 2  146 ? 26.520  49.473  19.892  1.00 19.41  ? 148 GLY   B C     1 
ATOM   15107 O  O     . GLY   F 2  146 ? 27.576  49.514  20.533  1.00 22.39  ? 148 GLY   B O     1 
ATOM   15108 N  N     . MET   F 2  147 ? 26.195  50.373  18.962  1.00 18.83  ? 149 MET   B N     1 
ATOM   15109 C  CA    . MET   F 2  147 ? 27.036  51.548  18.751  1.00 21.18  ? 149 MET   B CA    1 
ATOM   15110 C  C     . MET   F 2  147 ? 26.850  52.610  19.847  1.00 22.82  ? 149 MET   B C     1 
ATOM   15111 O  O     . MET   F 2  147 ? 27.807  53.322  20.190  1.00 20.03  ? 149 MET   B O     1 
ATOM   15112 C  CB    . MET   F 2  147 ? 26.769  52.139  17.363  1.00 18.44  ? 149 MET   B CB    1 
ATOM   15113 C  CG    . MET   F 2  147 ? 27.861  53.103  16.896  1.00 20.79  ? 149 MET   B CG    1 
ATOM   15114 S  SD    . MET   F 2  147 ? 27.563  53.835  15.289  1.00 30.26  ? 149 MET   B SD    1 
ATOM   15115 C  CE    . MET   F 2  147 ? 28.809  55.112  15.202  1.00 26.28  ? 149 MET   B CE    1 
ATOM   15116 N  N     . GLY   F 2  148 ? 25.647  52.727  20.418  1.00 21.49  ? 150 GLY   B N     1 
ATOM   15117 C  CA    . GLY   F 2  148 ? 25.459  53.666  21.512  1.00 19.02  ? 150 GLY   B CA    1 
ATOM   15118 C  C     . GLY   F 2  148 ? 26.364  53.355  22.689  1.00 21.44  ? 150 GLY   B C     1 
ATOM   15119 O  O     . GLY   F 2  148 ? 27.043  54.234  23.229  1.00 20.99  ? 150 GLY   B O     1 
ATOM   15120 N  N     . THR   F 2  149 ? 26.391  52.091  23.095  1.00 18.05  ? 151 THR   B N     1 
ATOM   15121 C  CA    . THR   F 2  149 ? 27.218  51.704  24.215  1.00 15.79  ? 151 THR   B CA    1 
ATOM   15122 C  C     . THR   F 2  149 ? 28.700  51.719  23.860  1.00 27.42  ? 151 THR   B C     1 
ATOM   15123 O  O     . THR   F 2  149 ? 29.540  51.905  24.753  1.00 28.78  ? 151 THR   B O     1 
ATOM   15124 C  CB    . THR   F 2  149 ? 26.762  50.349  24.707  1.00 13.05  ? 151 THR   B CB    1 
ATOM   15125 O  OG1   . THR   F 2  149 ? 26.686  49.464  23.603  1.00 18.60  ? 151 THR   B OG1   1 
ATOM   15126 C  CG2   . THR   F 2  149 ? 25.374  50.476  25.287  1.00 16.97  ? 151 THR   B CG2   1 
ATOM   15127 N  N     . LEU   F 2  150 ? 29.042  51.579  22.578  1.00 25.50  ? 152 LEU   B N     1 
ATOM   15128 C  CA    . LEU   F 2  150 ? 30.426  51.784  22.184  1.00 21.54  ? 152 LEU   B CA    1 
ATOM   15129 C  C     . LEU   F 2  150 ? 30.813  53.251  22.343  1.00 23.51  ? 152 LEU   B C     1 
ATOM   15130 O  O     . LEU   F 2  150 ? 31.767  53.578  23.054  1.00 23.30  ? 152 LEU   B O     1 
ATOM   15131 C  CB    . LEU   F 2  150 ? 30.639  51.304  20.754  1.00 23.67  ? 152 LEU   B CB    1 
ATOM   15132 C  CG    . LEU   F 2  150 ? 32.024  51.562  20.167  1.00 21.89  ? 152 LEU   B CG    1 
ATOM   15133 C  CD1   . LEU   F 2  150 ? 33.044  50.760  20.916  1.00 18.14  ? 152 LEU   B CD1   1 
ATOM   15134 C  CD2   . LEU   F 2  150 ? 32.041  51.240  18.680  1.00 20.57  ? 152 LEU   B CD2   1 
ATOM   15135 N  N     . LEU   F 2  151 ? 30.071  54.159  21.698  1.00 26.30  ? 153 LEU   B N     1 
ATOM   15136 C  CA    . LEU   F 2  151 ? 30.300  55.594  21.899  1.00 22.49  ? 153 LEU   B CA    1 
ATOM   15137 C  C     . LEU   F 2  151 ? 30.424  55.953  23.384  1.00 23.79  ? 153 LEU   B C     1 
ATOM   15138 O  O     . LEU   F 2  151 ? 31.254  56.785  23.761  1.00 25.66  ? 153 LEU   B O     1 
ATOM   15139 C  CB    . LEU   F 2  151 ? 29.168  56.400  21.257  1.00 16.10  ? 153 LEU   B CB    1 
ATOM   15140 C  CG    . LEU   F 2  151 ? 29.203  56.478  19.745  1.00 19.45  ? 153 LEU   B CG    1 
ATOM   15141 C  CD1   . LEU   F 2  151 ? 27.813  56.700  19.198  1.00 26.66  ? 153 LEU   B CD1   1 
ATOM   15142 C  CD2   . LEU   F 2  151 ? 30.122  57.618  19.334  1.00 17.73  ? 153 LEU   B CD2   1 
ATOM   15143 N  N     . ILE   F 2  152 ? 29.590  55.357  24.243  1.00 24.91  ? 154 ILE   B N     1 
ATOM   15144 C  CA    . ILE   F 2  152 ? 29.654  55.670  25.670  1.00 22.89  ? 154 ILE   B CA    1 
ATOM   15145 C  C     . ILE   F 2  152 ? 31.018  55.275  26.239  1.00 23.74  ? 154 ILE   B C     1 
ATOM   15146 O  O     . ILE   F 2  152 ? 31.640  56.044  26.974  1.00 25.11  ? 154 ILE   B O     1 
ATOM   15147 C  CB    . ILE   F 2  152 ? 28.476  54.998  26.414  1.00 24.34  ? 154 ILE   B CB    1 
ATOM   15148 C  CG1   . ILE   F 2  152 ? 27.157  55.710  26.106  1.00 23.38  ? 154 ILE   B CG1   1 
ATOM   15149 C  CG2   . ILE   F 2  152 ? 28.670  55.002  27.911  1.00 21.64  ? 154 ILE   B CG2   1 
ATOM   15150 C  CD1   . ILE   F 2  152 ? 25.942  54.964  26.601  1.00 20.05  ? 154 ILE   B CD1   1 
ATOM   15151 N  N     . SER   F 2  153 ? 31.512  54.081  25.889  1.00 30.47  ? 155 SER   B N     1 
ATOM   15152 C  CA    . SER   F 2  153 ? 32.862  53.653  26.278  1.00 25.56  ? 155 SER   B CA    1 
ATOM   15153 C  C     . SER   F 2  153 ? 33.929  54.615  25.752  1.00 28.08  ? 155 SER   B C     1 
ATOM   15154 O  O     . SER   F 2  153 ? 34.886  54.963  26.459  1.00 29.65  ? 155 SER   B O     1 
ATOM   15155 C  CB    . SER   F 2  153 ? 33.117  52.237  25.749  1.00 28.97  ? 155 SER   B CB    1 
ATOM   15156 O  OG    . SER   F 2  153 ? 34.113  51.536  26.465  1.00 33.77  ? 155 SER   B OG    1 
ATOM   15157 N  N     . LYS   F 2  154 ? 33.789  55.049  24.506  1.00 29.00  ? 156 LYS   B N     1 
ATOM   15158 C  CA    . LYS   F 2  154 ? 34.782  55.947  23.937  1.00 30.91  ? 156 LYS   B CA    1 
ATOM   15159 C  C     . LYS   F 2  154 ? 34.678  57.349  24.529  1.00 27.69  ? 156 LYS   B C     1 
ATOM   15160 O  O     . LYS   F 2  154 ? 35.705  58.008  24.731  1.00 30.98  ? 156 LYS   B O     1 
ATOM   15161 C  CB    . LYS   F 2  154 ? 34.643  55.948  22.413  1.00 28.95  ? 156 LYS   B CB    1 
ATOM   15162 C  CG    . LYS   F 2  154 ? 34.831  54.539  21.835  1.00 28.02  ? 156 LYS   B CG    1 
ATOM   15163 C  CD    . LYS   F 2  154 ? 35.275  54.538  20.373  1.00 35.68  ? 156 LYS   B CD    1 
ATOM   15164 C  CE    . LYS   F 2  154 ? 36.679  53.918  20.203  1.00 36.66  ? 156 LYS   B CE    1 
ATOM   15165 N  NZ    . LYS   F 2  154 ? 36.809  52.513  20.724  1.00 39.62  ? 156 LYS   B NZ    1 
ATOM   15166 N  N     . ILE   F 2  155 ? 33.466  57.798  24.867  1.00 25.46  ? 157 ILE   B N     1 
ATOM   15167 C  CA    . ILE   F 2  155 ? 33.292  59.122  25.468  1.00 25.99  ? 157 ILE   B CA    1 
ATOM   15168 C  C     . ILE   F 2  155 ? 33.833  59.160  26.904  1.00 27.71  ? 157 ILE   B C     1 
ATOM   15169 O  O     . ILE   F 2  155 ? 34.535  60.104  27.291  1.00 24.97  ? 157 ILE   B O     1 
ATOM   15170 C  CB    . ILE   F 2  155 ? 31.817  59.550  25.388  1.00 19.50  ? 157 ILE   B CB    1 
ATOM   15171 C  CG1   . ILE   F 2  155 ? 31.488  59.959  23.963  1.00 18.63  ? 157 ILE   B CG1   1 
ATOM   15172 C  CG2   . ILE   F 2  155 ? 31.543  60.694  26.324  1.00 23.16  ? 157 ILE   B CG2   1 
ATOM   15173 C  CD1   . ILE   F 2  155 ? 30.053  60.259  23.741  1.00 22.37  ? 157 ILE   B CD1   1 
ATOM   15174 N  N     . ARG   F 2  156 ? 33.545  58.135  27.708  1.00 23.35  ? 158 ARG   B N     1 
ATOM   15175 C  CA    . ARG   F 2  156 ? 34.120  58.105  29.045  1.00 25.75  ? 158 ARG   B CA    1 
ATOM   15176 C  C     . ARG   F 2  156 ? 35.649  58.123  28.997  1.00 32.97  ? 158 ARG   B C     1 
ATOM   15177 O  O     . ARG   F 2  156 ? 36.295  58.664  29.904  1.00 34.63  ? 158 ARG   B O     1 
ATOM   15178 C  CB    . ARG   F 2  156 ? 33.604  56.886  29.827  1.00 23.01  ? 158 ARG   B CB    1 
ATOM   15179 C  CG    . ARG   F 2  156 ? 34.269  56.689  31.208  1.00 25.93  ? 158 ARG   B CG    1 
ATOM   15180 C  CD    . ARG   F 2  156 ? 33.428  55.873  32.175  1.00 29.71  ? 158 ARG   B CD    1 
ATOM   15181 N  NE    . ARG   F 2  156 ? 32.338  56.683  32.703  1.00 44.58  ? 158 ARG   B NE    1 
ATOM   15182 C  CZ    . ARG   F 2  156 ? 31.765  56.490  33.882  1.00 49.59  ? 158 ARG   B CZ    1 
ATOM   15183 N  NH1   . ARG   F 2  156 ? 32.156  55.505  34.680  1.00 50.24  ? 158 ARG   B NH1   1 
ATOM   15184 N  NH2   . ARG   F 2  156 ? 30.782  57.308  34.270  1.00 25.30  ? 158 ARG   B NH2   1 
ATOM   15185 N  N     . GLU   F 2  157 ? 36.257  57.553  27.954  1.00 33.79  ? 159 GLU   B N     1 
ATOM   15186 C  CA    . GLU   F 2  157 ? 37.717  57.512  27.925  1.00 33.32  ? 159 GLU   B CA    1 
ATOM   15187 C  C     . GLU   F 2  157 ? 38.323  58.874  27.610  1.00 36.10  ? 159 GLU   B C     1 
ATOM   15188 O  O     . GLU   F 2  157 ? 39.406  59.191  28.111  1.00 38.66  ? 159 GLU   B O     1 
ATOM   15189 C  CB    . GLU   F 2  157 ? 38.189  56.478  26.915  1.00 35.24  ? 159 GLU   B CB    1 
ATOM   15190 C  CG    . GLU   F 2  157 ? 39.683  56.398  26.746  1.00 36.75  ? 159 GLU   B CG    1 
ATOM   15191 C  CD    . GLU   F 2  157 ? 40.099  55.170  25.943  1.00 45.52  ? 159 GLU   B CD    1 
ATOM   15192 O  OE1   . GLU   F 2  157 ? 39.234  54.634  25.214  1.00 41.11  ? 159 GLU   B OE1   1 
ATOM   15193 O  OE2   . GLU   F 2  157 ? 41.269  54.728  26.059  1.00 50.81  ? 159 GLU   B OE2   1 
ATOM   15194 N  N     . GLU   F 2  158 ? 37.646  59.696  26.811  1.00 24.29  ? 160 GLU   B N     1 
ATOM   15195 C  CA    . GLU   F 2  158 ? 38.126  61.046  26.576  1.00 29.05  ? 160 GLU   B CA    1 
ATOM   15196 C  C     . GLU   F 2  158 ? 37.644  62.049  27.621  1.00 33.86  ? 160 GLU   B C     1 
ATOM   15197 O  O     . GLU   F 2  158 ? 38.242  63.124  27.749  1.00 27.99  ? 160 GLU   B O     1 
ATOM   15198 C  CB    . GLU   F 2  158 ? 37.698  61.529  25.185  1.00 29.69  ? 160 GLU   B CB    1 
ATOM   15199 C  CG    . GLU   F 2  158 ? 38.532  60.999  24.031  1.00 41.68  ? 160 GLU   B CG    1 
ATOM   15200 C  CD    . GLU   F 2  158 ? 38.365  61.823  22.758  1.00 51.81  ? 160 GLU   B CD    1 
ATOM   15201 O  OE1   . GLU   F 2  158 ? 38.375  63.092  22.856  1.00 37.23  ? 160 GLU   B OE1   1 
ATOM   15202 O  OE2   . GLU   F 2  158 ? 38.223  61.190  21.674  1.00 41.42  ? 160 GLU   B OE2   1 
ATOM   15203 N  N     . TYR   F 2  159 ? 36.577  61.727  28.353  1.00 31.58  ? 161 TYR   B N     1 
ATOM   15204 C  CA    . TYR   F 2  159 ? 35.953  62.644  29.308  1.00 25.29  ? 161 TYR   B CA    1 
ATOM   15205 C  C     . TYR   F 2  159 ? 35.630  61.881  30.578  1.00 28.30  ? 161 TYR   B C     1 
ATOM   15206 O  O     . TYR   F 2  159 ? 34.476  61.822  31.017  1.00 30.08  ? 161 TYR   B O     1 
ATOM   15207 C  CB    . TYR   F 2  159 ? 34.688  63.258  28.720  1.00 24.97  ? 161 TYR   B CB    1 
ATOM   15208 C  CG    . TYR   F 2  159 ? 34.936  64.006  27.442  1.00 34.46  ? 161 TYR   B CG    1 
ATOM   15209 C  CD1   . TYR   F 2  159 ? 34.965  63.340  26.235  1.00 35.24  ? 161 TYR   B CD1   1 
ATOM   15210 C  CD2   . TYR   F 2  159 ? 35.138  65.383  27.437  1.00 26.48  ? 161 TYR   B CD2   1 
ATOM   15211 C  CE1   . TYR   F 2  159 ? 35.176  64.010  25.065  1.00 32.98  ? 161 TYR   B CE1   1 
ATOM   15212 C  CE2   . TYR   F 2  159 ? 35.351  66.057  26.277  1.00 26.19  ? 161 TYR   B CE2   1 
ATOM   15213 C  CZ    . TYR   F 2  159 ? 35.365  65.364  25.083  1.00 37.06  ? 161 TYR   B CZ    1 
ATOM   15214 O  OH    . TYR   F 2  159 ? 35.576  66.007  23.885  1.00 45.63  ? 161 TYR   B OH    1 
ATOM   15215 N  N     . PRO   F 2  160 ? 36.639  61.262  31.189  1.00 27.51  ? 162 PRO   B N     1 
ATOM   15216 C  CA    . PRO   F 2  160 ? 36.381  60.340  32.307  1.00 20.98  ? 162 PRO   B CA    1 
ATOM   15217 C  C     . PRO   F 2  160 ? 35.727  60.996  33.512  1.00 28.46  ? 162 PRO   B C     1 
ATOM   15218 O  O     . PRO   F 2  160 ? 35.253  60.276  34.410  1.00 29.02  ? 162 PRO   B O     1 
ATOM   15219 C  CB    . PRO   F 2  160 ? 37.782  59.819  32.655  1.00 26.95  ? 162 PRO   B CB    1 
ATOM   15220 C  CG    . PRO   F 2  160 ? 38.722  60.855  32.132  1.00 22.15  ? 162 PRO   B CG    1 
ATOM   15221 C  CD    . PRO   F 2  160 ? 38.072  61.437  30.909  1.00 25.63  ? 162 PRO   B CD    1 
ATOM   15222 N  N     . ASP   F 2  161 ? 35.679  62.330  33.537  1.00 22.64  ? 163 ASP   B N     1 
ATOM   15223 C  CA    . ASP   F 2  161 ? 35.251  63.140  34.663  1.00 19.18  ? 163 ASP   B CA    1 
ATOM   15224 C  C     . ASP   F 2  161 ? 34.092  64.061  34.315  1.00 25.52  ? 163 ASP   B C     1 
ATOM   15225 O  O     . ASP   F 2  161 ? 33.881  65.061  35.002  1.00 32.65  ? 163 ASP   B O     1 
ATOM   15226 C  CB    . ASP   F 2  161 ? 36.399  64.009  35.117  1.00 32.35  ? 163 ASP   B CB    1 
ATOM   15227 C  CG    . ASP   F 2  161 ? 36.513  65.223  34.260  1.00 37.98  ? 163 ASP   B CG    1 
ATOM   15228 O  OD1   . ASP   F 2  161 ? 36.499  65.054  33.017  1.00 32.72  ? 163 ASP   B OD1   1 
ATOM   15229 O  OD2   . ASP   F 2  161 ? 36.545  66.335  34.818  1.00 49.69  ? 163 ASP   B OD2   1 
ATOM   15230 N  N     . ARG   F 2  162 ? 33.400  63.810  33.220  1.00 27.36  ? 164 ARG   B N     1 
ATOM   15231 C  CA    . ARG   F 2  162 ? 32.151  64.483  32.919  1.00 28.00  ? 164 ARG   B CA    1 
ATOM   15232 C  C     . ARG   F 2  162 ? 31.047  63.450  33.078  1.00 21.73  ? 164 ARG   B C     1 
ATOM   15233 O  O     . ARG   F 2  162 ? 31.307  62.250  33.067  1.00 28.98  ? 164 ARG   B O     1 
ATOM   15234 C  CB    . ARG   F 2  162 ? 32.178  65.099  31.513  1.00 25.91  ? 164 ARG   B CB    1 
ATOM   15235 C  CG    . ARG   F 2  162 ? 33.334  66.076  31.280  1.00 27.99  ? 164 ARG   B CG    1 
ATOM   15236 C  CD    . ARG   F 2  162 ? 33.108  67.459  31.923  1.00 35.48  ? 164 ARG   B CD    1 
ATOM   15237 N  NE    . ARG   F 2  162 ? 33.769  67.641  33.218  1.00 51.43  ? 164 ARG   B NE    1 
ATOM   15238 C  CZ    . ARG   F 2  162 ? 33.260  68.323  34.246  1.00 57.70  ? 164 ARG   B CZ    1 
ATOM   15239 N  NH1   . ARG   F 2  162 ? 32.049  68.871  34.191  1.00 42.89  ? 164 ARG   B NH1   1 
ATOM   15240 N  NH2   . ARG   F 2  162 ? 33.977  68.448  35.367  1.00 48.33  ? 164 ARG   B NH2   1 
ATOM   15241 N  N     . ILE   F 2  163 ? 29.831  63.904  33.280  1.00 24.04  ? 165 ILE   B N     1 
ATOM   15242 C  CA    . ILE   F 2  163 ? 28.760  62.978  33.634  1.00 25.76  ? 165 ILE   B CA    1 
ATOM   15243 C  C     . ILE   F 2  163 ? 28.200  62.342  32.368  1.00 27.32  ? 165 ILE   B C     1 
ATOM   15244 O  O     . ILE   F 2  163 ? 28.126  62.973  31.298  1.00 23.25  ? 165 ILE   B O     1 
ATOM   15245 C  CB    . ILE   F 2  163 ? 27.659  63.697  34.447  1.00 26.11  ? 165 ILE   B CB    1 
ATOM   15246 C  CG1   . ILE   F 2  163 ? 28.183  64.124  35.818  1.00 18.83  ? 165 ILE   B CG1   1 
ATOM   15247 C  CG2   . ILE   F 2  163 ? 26.442  62.789  34.643  1.00 22.83  ? 165 ILE   B CG2   1 
ATOM   15248 C  CD1   . ILE   F 2  163 ? 28.326  62.964  36.791  1.00 20.06  ? 165 ILE   B CD1   1 
ATOM   15249 N  N     . MET   F 2  164 ? 27.811  61.072  32.489  1.00 21.34  ? 166 MET   B N     1 
ATOM   15250 C  CA    . MET   F 2  164 ? 27.249  60.314  31.376  1.00 20.12  ? 166 MET   B CA    1 
ATOM   15251 C  C     . MET   F 2  164 ? 25.813  59.919  31.712  1.00 22.94  ? 166 MET   B C     1 
ATOM   15252 O  O     . MET   F 2  164 ? 25.564  59.215  32.701  1.00 21.09  ? 166 MET   B O     1 
ATOM   15253 C  CB    . MET   F 2  164 ? 28.113  59.091  31.054  1.00 21.02  ? 166 MET   B CB    1 
ATOM   15254 C  CG    . MET   F 2  164 ? 27.542  58.095  30.063  1.00 23.31  ? 166 MET   B CG    1 
ATOM   15255 S  SD    . MET   F 2  164 ? 27.464  58.791  28.391  1.00 25.14  ? 166 MET   B SD    1 
ATOM   15256 C  CE    . MET   F 2  164 ? 29.112  59.427  28.250  1.00 23.06  ? 166 MET   B CE    1 
ATOM   15257 N  N     . ASN   F 2  165 ? 24.877  60.383  30.883  1.00 18.74  ? 167 ASN   B N     1 
ATOM   15258 C  CA    . ASN   F 2  165 ? 23.438  60.251  31.087  1.00 22.90  ? 167 ASN   B CA    1 
ATOM   15259 C  C     . ASN   F 2  165 ? 22.804  59.606  29.854  1.00 25.06  ? 167 ASN   B C     1 
ATOM   15260 O  O     . ASN   F 2  165 ? 23.097  59.998  28.714  1.00 21.42  ? 167 ASN   B O     1 
ATOM   15261 C  CB    . ASN   F 2  165 ? 22.828  61.638  31.350  1.00 30.16  ? 167 ASN   B CB    1 
ATOM   15262 C  CG    . ASN   F 2  165 ? 21.407  61.588  31.875  1.00 31.55  ? 167 ASN   B CG    1 
ATOM   15263 O  OD1   . ASN   F 2  165 ? 20.444  61.625  31.108  1.00 31.02  ? 167 ASN   B OD1   1 
ATOM   15264 N  ND2   . ASN   F 2  165 ? 21.274  61.571  33.189  1.00 28.20  ? 167 ASN   B ND2   1 
ATOM   15265 N  N     . THR   F 2  166 ? 21.974  58.588  30.068  1.00 21.99  ? 168 THR   B N     1 
ATOM   15266 C  CA    A THR   F 2  166 ? 21.301  57.930  28.961  1.00 22.83  ? 168 THR   B CA    1 
ATOM   15267 C  CA    B THR   F 2  166 ? 21.303  57.902  28.972  0.00 22.32  ? 168 THR   B CA    1 
ATOM   15268 C  C     . THR   F 2  166 ? 19.820  57.746  29.272  1.00 25.52  ? 168 THR   B C     1 
ATOM   15269 O  O     . THR   F 2  166 ? 19.435  57.477  30.416  1.00 17.78  ? 168 THR   B O     1 
ATOM   15270 C  CB    A THR   F 2  166 ? 21.915  56.566  28.626  1.00 20.97  ? 168 THR   B CB    1 
ATOM   15271 C  CB    B THR   F 2  166 ? 21.916  56.522  28.713  0.00 21.46  ? 168 THR   B CB    1 
ATOM   15272 O  OG1   A THR   F 2  166 ? 21.171  55.548  29.286  1.00 16.50  ? 168 THR   B OG1   1 
ATOM   15273 O  OG1   B THR   F 2  166 ? 21.781  55.720  29.890  0.00 19.76  ? 168 THR   B OG1   1 
ATOM   15274 C  CG2   A THR   F 2  166 ? 23.347  56.500  29.053  1.00 19.02  ? 168 THR   B CG2   1 
ATOM   15275 C  CG2   B THR   F 2  166 ? 23.391  56.660  28.364  0.00 19.92  ? 168 THR   B CG2   1 
ATOM   15276 N  N     . PHE   F 2  167 ? 18.994  57.939  28.239  1.00 22.49  ? 169 PHE   B N     1 
ATOM   15277 C  CA    . PHE   F 2  167 ? 17.603  57.512  28.236  1.00 20.82  ? 169 PHE   B CA    1 
ATOM   15278 C  C     . PHE   F 2  167 ? 17.594  56.261  27.390  1.00 20.71  ? 169 PHE   B C     1 
ATOM   15279 O  O     . PHE   F 2  167 ? 17.786  56.345  26.174  1.00 24.24  ? 169 PHE   B O     1 
ATOM   15280 C  CB    . PHE   F 2  167 ? 16.673  58.548  27.622  1.00 23.33  ? 169 PHE   B CB    1 
ATOM   15281 C  CG    . PHE   F 2  167 ? 16.614  59.816  28.369  1.00 23.51  ? 169 PHE   B CG    1 
ATOM   15282 C  CD1   . PHE   F 2  167 ? 17.718  60.639  28.431  1.00 20.23  ? 169 PHE   B CD1   1 
ATOM   15283 C  CD2   . PHE   F 2  167 ? 15.446  60.200  28.990  1.00 24.69  ? 169 PHE   B CD2   1 
ATOM   15284 C  CE1   . PHE   F 2  167 ? 17.668  61.809  29.112  1.00 25.64  ? 169 PHE   B CE1   1 
ATOM   15285 C  CE2   . PHE   F 2  167 ? 15.379  61.382  29.671  1.00 26.09  ? 169 PHE   B CE2   1 
ATOM   15286 C  CZ    . PHE   F 2  167 ? 16.491  62.187  29.740  1.00 31.97  ? 169 PHE   B CZ    1 
ATOM   15287 N  N     . SER   F 2  168 ? 17.378  55.106  28.015  1.00 22.25  ? 170 SER   B N     1 
ATOM   15288 C  CA    . SER   F 2  168 ? 17.547  53.813  27.349  1.00 22.08  ? 170 SER   B CA    1 
ATOM   15289 C  C     . SER   F 2  168 ? 16.197  53.100  27.191  1.00 19.83  ? 170 SER   B C     1 
ATOM   15290 O  O     . SER   F 2  168 ? 15.615  52.655  28.183  1.00 17.86  ? 170 SER   B O     1 
ATOM   15291 C  CB    . SER   F 2  168 ? 18.545  52.967  28.141  1.00 18.44  ? 170 SER   B CB    1 
ATOM   15292 O  OG    . SER   F 2  168 ? 19.806  53.623  28.241  1.00 19.10  ? 170 SER   B OG    1 
ATOM   15293 N  N     . VAL   F 2  169 ? 15.714  52.951  25.950  1.00 16.54  ? 171 VAL   B N     1 
ATOM   15294 C  CA    . VAL   F 2  169 ? 14.438  52.264  25.734  1.00 17.82  ? 171 VAL   B CA    1 
ATOM   15295 C  C     . VAL   F 2  169 ? 14.632  50.747  25.775  1.00 16.69  ? 171 VAL   B C     1 
ATOM   15296 O  O     . VAL   F 2  169 ? 15.337  50.177  24.934  1.00 17.39  ? 171 VAL   B O     1 
ATOM   15297 C  CB    . VAL   F 2  169 ? 13.776  52.688  24.416  1.00 15.75  ? 171 VAL   B CB    1 
ATOM   15298 C  CG1   . VAL   F 2  169 ? 12.525  51.860  24.221  1.00 13.68  ? 171 VAL   B CG1   1 
ATOM   15299 C  CG2   . VAL   F 2  169 ? 13.413  54.166  24.443  1.00 16.76  ? 171 VAL   B CG2   1 
ATOM   15300 N  N     . MET   F 2  170 ? 13.947  50.079  26.727  1.00 11.67  ? 172 MET   B N     1 
ATOM   15301 C  CA    . MET   F 2  170 ? 14.011  48.639  26.971  1.00 14.73  ? 172 MET   B CA    1 
ATOM   15302 C  C     . MET   F 2  170 ? 12.996  47.893  26.110  1.00 16.87  ? 172 MET   B C     1 
ATOM   15303 O  O     . MET   F 2  170 ? 11.840  48.336  25.970  1.00 13.79  ? 172 MET   B O     1 
ATOM   15304 C  CB    . MET   F 2  170 ? 13.737  48.323  28.436  1.00 17.39  ? 172 MET   B CB    1 
ATOM   15305 C  CG    . MET   F 2  170 ? 14.503  49.179  29.413  1.00 18.31  ? 172 MET   B CG    1 
ATOM   15306 S  SD    . MET   F 2  170 ? 16.237  48.747  29.493  0.66 22.07  ? 172 MET   B SD    1 
ATOM   15307 C  CE    . MET   F 2  170 ? 16.894  50.204  30.301  0.38 18.20  ? 172 MET   B CE    1 
ATOM   15308 N  N     . PRO   F 2  171 ? 13.418  46.751  25.579  1.00 18.17  ? 173 PRO   B N     1 
ATOM   15309 C  CA    . PRO   F 2  171 ? 12.561  45.978  24.675  1.00 17.78  ? 173 PRO   B CA    1 
ATOM   15310 C  C     . PRO   F 2  171 ? 11.437  45.247  25.392  1.00 20.40  ? 173 PRO   B C     1 
ATOM   15311 O  O     . PRO   F 2  171 ? 11.558  44.825  26.542  1.00 22.31  ? 173 PRO   B O     1 
ATOM   15312 C  CB    . PRO   F 2  171 ? 13.536  44.979  24.051  1.00 15.47  ? 173 PRO   B CB    1 
ATOM   15313 C  CG    . PRO   F 2  171 ? 14.561  44.798  25.092  1.00 15.99  ? 173 PRO   B CG    1 
ATOM   15314 C  CD    . PRO   F 2  171 ? 14.747  46.145  25.738  1.00 20.13  ? 173 PRO   B CD    1 
ATOM   15315 N  N     . SER   F 2  172 ? 10.327  45.078  24.678  1.00 20.08  ? 174 SER   B N     1 
ATOM   15316 C  CA    . SER   F 2  172 ? 9.217   44.302  25.206  1.00 17.95  ? 174 SER   B CA    1 
ATOM   15317 C  C     . SER   F 2  172 ? 8.609   43.509  24.050  1.00 22.70  ? 174 SER   B C     1 
ATOM   15318 O  O     . SER   F 2  172 ? 8.391   44.075  22.958  1.00 26.10  ? 174 SER   B O     1 
ATOM   15319 C  CB    . SER   F 2  172 ? 8.166   45.193  25.869  1.00 21.65  ? 174 SER   B CB    1 
ATOM   15320 O  OG    . SER   F 2  172 ? 6.909   44.541  25.919  1.00 29.90  ? 174 SER   B OG    1 
ATOM   15321 N  N     . PRO   F 2  173 ? 8.352   42.209  24.224  1.00 20.51  ? 175 PRO   B N     1 
ATOM   15322 C  CA    . PRO   F 2  173 ? 7.689   41.452  23.159  1.00 24.99  ? 175 PRO   B CA    1 
ATOM   15323 C  C     . PRO   F 2  173 ? 6.223   41.809  22.973  1.00 24.33  ? 175 PRO   B C     1 
ATOM   15324 O  O     . PRO   F 2  173 ? 5.573   41.225  22.108  1.00 26.04  ? 175 PRO   B O     1 
ATOM   15325 C  CB    . PRO   F 2  173 ? 7.875   39.994  23.609  1.00 19.92  ? 175 PRO   B CB    1 
ATOM   15326 C  CG    . PRO   F 2  173 ? 8.110   40.049  24.993  1.00 17.55  ? 175 PRO   B CG    1 
ATOM   15327 C  CD    . PRO   F 2  173 ? 8.813   41.317  25.292  1.00 22.41  ? 175 PRO   B CD    1 
ATOM   15328 N  N     . LYS   F 2  174 ? 5.676   42.730  23.768  1.00 28.17  ? 176 LYS   B N     1 
ATOM   15329 C  CA    . LYS   F 2  174 ? 4.366   43.288  23.468  1.00 27.28  ? 176 LYS   B CA    1 
ATOM   15330 C  C     . LYS   F 2  174 ? 4.424   44.222  22.272  1.00 33.48  ? 176 LYS   B C     1 
ATOM   15331 O  O     . LYS   F 2  174 ? 3.401   44.432  21.614  1.00 35.65  ? 176 LYS   B O     1 
ATOM   15332 C  CB    . LYS   F 2  174 ? 3.808   44.033  24.679  1.00 23.52  ? 176 LYS   B CB    1 
ATOM   15333 C  CG    . LYS   F 2  174 ? 3.549   43.130  25.892  1.00 34.05  ? 176 LYS   B CG    1 
ATOM   15334 C  CD    . LYS   F 2  174 ? 3.031   43.915  27.092  1.00 33.62  ? 176 LYS   B CD    1 
ATOM   15335 C  CE    . LYS   F 2  174 ? 2.699   43.015  28.267  1.00 31.04  ? 176 LYS   B CE    1 
ATOM   15336 N  NZ    . LYS   F 2  174 ? 1.738   43.714  29.214  1.00 35.79  ? 176 LYS   B NZ    1 
ATOM   15337 N  N     . VAL   F 2  175 ? 5.599   44.761  21.961  1.00 26.99  ? 177 VAL   B N     1 
ATOM   15338 C  CA    . VAL   F 2  175 ? 5.725   45.774  20.927  1.00 20.49  ? 177 VAL   B CA    1 
ATOM   15339 C  C     . VAL   F 2  175 ? 6.644   45.349  19.804  1.00 25.82  ? 177 VAL   B C     1 
ATOM   15340 O  O     . VAL   F 2  175 ? 6.544   45.901  18.694  1.00 31.39  ? 177 VAL   B O     1 
ATOM   15341 C  CB    . VAL   F 2  175 ? 6.205   47.101  21.533  1.00 21.49  ? 177 VAL   B CB    1 
ATOM   15342 C  CG1   . VAL   F 2  175 ? 6.499   48.108  20.448  1.00 22.35  ? 177 VAL   B CG1   1 
ATOM   15343 C  CG2   . VAL   F 2  175 ? 5.158   47.615  22.497  1.00 20.87  ? 177 VAL   B CG2   1 
ATOM   15344 N  N     . SER   F 2  176 ? 7.507   44.375  20.027  1.00 24.14  ? 178 SER   B N     1 
ATOM   15345 C  CA    . SER   F 2  176 ? 8.449   43.932  19.024  1.00 18.08  ? 178 SER   B CA    1 
ATOM   15346 C  C     . SER   F 2  176 ? 8.337   42.421  18.903  1.00 24.93  ? 178 SER   B C     1 
ATOM   15347 O  O     . SER   F 2  176 ? 7.826   41.742  19.805  1.00 24.49  ? 178 SER   B O     1 
ATOM   15348 C  CB    . SER   F 2  176 ? 9.867   44.362  19.409  1.00 18.83  ? 178 SER   B CB    1 
ATOM   15349 O  OG    . SER   F 2  176 ? 10.771  44.165  18.353  1.00 28.65  ? 178 SER   B OG    1 
ATOM   15350 N  N     . ASP   F 2  177 ? 8.797   41.892  17.759  1.00 22.78  ? 179 ASP   B N     1 
ATOM   15351 C  CA    . ASP   F 2  177 ? 8.819   40.447  17.555  1.00 19.08  ? 179 ASP   B CA    1 
ATOM   15352 C  C     . ASP   F 2  177 ? 10.141  39.937  16.992  1.00 23.44  ? 179 ASP   B C     1 
ATOM   15353 O  O     . ASP   F 2  177 ? 10.174  38.827  16.451  1.00 23.05  ? 179 ASP   B O     1 
ATOM   15354 C  CB    . ASP   F 2  177 ? 7.653   39.987  16.676  1.00 18.00  ? 179 ASP   B CB    1 
ATOM   15355 C  CG    . ASP   F 2  177 ? 7.560   40.732  15.350  1.00 26.79  ? 179 ASP   B CG    1 
ATOM   15356 O  OD1   . ASP   F 2  177 ? 8.582   41.274  14.855  1.00 25.05  ? 179 ASP   B OD1   1 
ATOM   15357 O  OD2   . ASP   F 2  177 ? 6.439   40.769  14.797  1.00 29.81  ? 179 ASP   B OD2   1 
ATOM   15358 N  N     . THR   F 2  178 ? 11.239  40.690  17.158  1.00 24.47  ? 180 THR   B N     1 
ATOM   15359 C  CA    . THR   F 2  178 ? 12.583  40.189  16.854  1.00 20.80  ? 180 THR   B CA    1 
ATOM   15360 C  C     . THR   F 2  178 ? 13.118  39.320  18.000  1.00 17.87  ? 180 THR   B C     1 
ATOM   15361 O  O     . THR   F 2  178 ? 13.194  39.754  19.154  1.00 20.92  ? 180 THR   B O     1 
ATOM   15362 C  CB    . THR   F 2  178 ? 13.533  41.345  16.565  1.00 19.62  ? 180 THR   B CB    1 
ATOM   15363 O  OG1   . THR   F 2  178 ? 13.042  42.069  15.435  1.00 22.59  ? 180 THR   B OG1   1 
ATOM   15364 C  CG2   . THR   F 2  178 ? 14.928  40.818  16.264  1.00 12.45  ? 180 THR   B CG2   1 
ATOM   15365 N  N     . VAL   F 2  179 ? 13.520  38.098  17.666  1.00 20.05  ? 181 VAL   B N     1 
ATOM   15366 C  CA    . VAL   F 2  179 ? 13.817  37.085  18.667  1.00 20.09  ? 181 VAL   B CA    1 
ATOM   15367 C  C     . VAL   F 2  179 ? 15.088  37.379  19.448  1.00 16.07  ? 181 VAL   B C     1 
ATOM   15368 O  O     . VAL   F 2  179 ? 15.247  36.880  20.571  1.00 23.00  ? 181 VAL   B O     1 
ATOM   15369 C  CB    . VAL   F 2  179 ? 13.919  35.710  17.969  1.00 18.34  ? 181 VAL   B CB    1 
ATOM   15370 C  CG1   . VAL   F 2  179 ? 15.189  35.644  17.121  1.00 15.19  ? 181 VAL   B CG1   1 
ATOM   15371 C  CG2   . VAL   F 2  179 ? 13.876  34.579  18.980  1.00 16.45  ? 181 VAL   B CG2   1 
ATOM   15372 N  N     . VAL   F 2  180 ? 16.027  38.142  18.879  1.00 14.50  ? 182 VAL   B N     1 
ATOM   15373 C  CA    . VAL   F 2  180 ? 17.322  38.333  19.525  1.00 17.63  ? 182 VAL   B CA    1 
ATOM   15374 C  C     . VAL   F 2  180 ? 17.388  39.574  20.407  1.00 21.74  ? 182 VAL   B C     1 
ATOM   15375 O  O     . VAL   F 2  180 ? 18.437  39.830  21.010  1.00 22.80  ? 182 VAL   B O     1 
ATOM   15376 C  CB    . VAL   F 2  180 ? 18.479  38.409  18.512  1.00 16.71  ? 182 VAL   B CB    1 
ATOM   15377 C  CG1   . VAL   F 2  180 ? 18.515  37.148  17.693  1.00 16.79  ? 182 VAL   B CG1   1 
ATOM   15378 C  CG2   . VAL   F 2  180 ? 18.357  39.637  17.640  1.00 18.04  ? 182 VAL   B CG2   1 
ATOM   15379 N  N     . GLU   F 2  181 ? 16.306  40.333  20.540  1.00 22.09  ? 183 GLU   B N     1 
ATOM   15380 C  CA    . GLU   F 2  181 ? 16.367  41.532  21.373  1.00 19.78  ? 183 GLU   B CA    1 
ATOM   15381 C  C     . GLU   F 2  181 ? 16.845  41.273  22.795  1.00 18.41  ? 183 GLU   B C     1 
ATOM   15382 O  O     . GLU   F 2  181 ? 17.585  42.117  23.322  1.00 16.99  ? 183 GLU   B O     1 
ATOM   15383 C  CB    . GLU   F 2  181 ? 15.004  42.227  21.374  1.00 18.93  ? 183 GLU   B CB    1 
ATOM   15384 C  CG    . GLU   F 2  181 ? 14.532  42.585  19.979  1.00 17.39  ? 183 GLU   B CG    1 
ATOM   15385 C  CD    . GLU   F 2  181 ? 13.527  43.687  19.988  1.00 15.06  ? 183 GLU   B CD    1 
ATOM   15386 O  OE1   . GLU   F 2  181 ? 12.670  43.714  20.882  1.00 24.43  ? 183 GLU   B OE1   1 
ATOM   15387 O  OE2   . GLU   F 2  181 ? 13.597  44.542  19.111  1.00 19.56  ? 183 GLU   B OE2   1 
ATOM   15388 N  N     . PRO   F 2  182 ? 16.485  40.171  23.463  1.00 19.17  ? 184 PRO   B N     1 
ATOM   15389 C  CA    . PRO   F 2  182 ? 17.031  39.927  24.814  1.00 18.30  ? 184 PRO   B CA    1 
ATOM   15390 C  C     . PRO   F 2  182 ? 18.545  39.867  24.844  1.00 20.53  ? 184 PRO   B C     1 
ATOM   15391 O  O     . PRO   F 2  182 ? 19.162  40.206  25.863  1.00 19.47  ? 184 PRO   B O     1 
ATOM   15392 C  CB    . PRO   F 2  182 ? 16.418  38.572  25.198  1.00 15.04  ? 184 PRO   B CB    1 
ATOM   15393 C  CG    . PRO   F 2  182 ? 15.195  38.493  24.441  1.00 16.50  ? 184 PRO   B CG    1 
ATOM   15394 C  CD    . PRO   F 2  182 ? 15.480  39.163  23.105  1.00 17.11  ? 184 PRO   B CD    1 
ATOM   15395 N  N     . TYR   F 2  183 ? 19.157  39.404  23.751  1.00 19.67  ? 185 TYR   B N     1 
ATOM   15396 C  CA    . TYR   F 2  183 ? 20.607  39.411  23.639  1.00 20.90  ? 185 TYR   B CA    1 
ATOM   15397 C  C     . TYR   F 2  183 ? 21.130  40.839  23.632  1.00 20.43  ? 185 TYR   B C     1 
ATOM   15398 O  O     . TYR   F 2  183 ? 21.959  41.212  24.470  1.00 20.17  ? 185 TYR   B O     1 
ATOM   15399 C  CB    . TYR   F 2  183 ? 21.042  38.675  22.368  1.00 17.00  ? 185 TYR   B CB    1 
ATOM   15400 C  CG    . TYR   F 2  183 ? 21.074  37.175  22.487  1.00 18.29  ? 185 TYR   B CG    1 
ATOM   15401 C  CD1   . TYR   F 2  183 ? 21.168  36.556  23.725  1.00 18.43  ? 185 TYR   B CD1   1 
ATOM   15402 C  CD2   . TYR   F 2  183 ? 21.015  36.370  21.354  1.00 22.47  ? 185 TYR   B CD2   1 
ATOM   15403 C  CE1   . TYR   F 2  183 ? 21.210  35.168  23.831  1.00 20.99  ? 185 TYR   B CE1   1 
ATOM   15404 C  CE2   . TYR   F 2  183 ? 21.053  34.983  21.443  1.00 23.66  ? 185 TYR   B CE2   1 
ATOM   15405 C  CZ    . TYR   F 2  183 ? 21.154  34.390  22.686  1.00 24.01  ? 185 TYR   B CZ    1 
ATOM   15406 O  OH    . TYR   F 2  183 ? 21.190  33.019  22.778  1.00 20.95  ? 185 TYR   B OH    1 
ATOM   15407 N  N     . ASN   F 2  184 ? 20.642  41.650  22.686  1.00 16.22  ? 186 ASN   B N     1 
ATOM   15408 C  CA    . ASN   F 2  184 ? 21.078  43.037  22.567  1.00 20.21  ? 186 ASN   B CA    1 
ATOM   15409 C  C     . ASN   F 2  184 ? 20.865  43.808  23.871  1.00 21.12  ? 186 ASN   B C     1 
ATOM   15410 O  O     . ASN   F 2  184 ? 21.676  44.671  24.235  1.00 22.40  ? 186 ASN   B O     1 
ATOM   15411 C  CB    . ASN   F 2  184 ? 20.328  43.735  21.421  1.00 24.53  ? 186 ASN   B CB    1 
ATOM   15412 C  CG    . ASN   F 2  184 ? 20.542  43.066  20.070  1.00 22.00  ? 186 ASN   B CG    1 
ATOM   15413 O  OD1   . ASN   F 2  184 ? 21.435  42.236  19.897  1.00 19.73  ? 186 ASN   B OD1   1 
ATOM   15414 N  ND2   . ASN   F 2  184 ? 19.715  43.435  19.106  1.00 19.75  ? 186 ASN   B ND2   1 
ATOM   15415 N  N     . ALA   F 2  185 ? 19.770  43.525  24.579  1.00 19.00  ? 187 ALA   B N     1 
ATOM   15416 C  CA    . ALA   F 2  185 ? 19.476  44.281  25.786  1.00 17.73  ? 187 ALA   B CA    1 
ATOM   15417 C  C     . ALA   F 2  185 ? 20.462  43.933  26.889  1.00 20.55  ? 187 ALA   B C     1 
ATOM   15418 O  O     . ALA   F 2  185 ? 21.016  44.830  27.536  1.00 30.25  ? 187 ALA   B O     1 
ATOM   15419 C  CB    . ALA   F 2  185 ? 18.034  44.040  26.231  1.00 18.45  ? 187 ALA   B CB    1 
ATOM   15420 N  N     . THR   F 2  186 ? 20.720  42.636  27.102  1.00 19.65  ? 188 THR   B N     1 
ATOM   15421 C  CA    . THR   F 2  186 ? 21.677  42.233  28.134  1.00 24.43  ? 188 THR   B CA    1 
ATOM   15422 C  C     . THR   F 2  186 ? 23.088  42.732  27.824  1.00 22.24  ? 188 THR   B C     1 
ATOM   15423 O  O     . THR   F 2  186 ? 23.802  43.189  28.724  1.00 19.69  ? 188 THR   B O     1 
ATOM   15424 C  CB    . THR   F 2  186 ? 21.676  40.711  28.301  1.00 19.48  ? 188 THR   B CB    1 
ATOM   15425 O  OG1   . THR   F 2  186 ? 20.326  40.244  28.400  1.00 18.73  ? 188 THR   B OG1   1 
ATOM   15426 C  CG2   . THR   F 2  186 ? 22.435  40.304  29.553  1.00 11.99  ? 188 THR   B CG2   1 
ATOM   15427 N  N     . LEU   F 2  187 ? 23.513  42.654  26.563  1.00 17.46  ? 189 LEU   B N     1 
ATOM   15428 C  CA    . LEU   F 2  187 ? 24.829  43.189  26.218  1.00 23.24  ? 189 LEU   B CA    1 
ATOM   15429 C  C     . LEU   F 2  187 ? 24.903  44.687  26.502  1.00 27.08  ? 189 LEU   B C     1 
ATOM   15430 O  O     . LEU   F 2  187 ? 25.953  45.195  26.910  1.00 29.17  ? 189 LEU   B O     1 
ATOM   15431 C  CB    . LEU   F 2  187 ? 25.171  42.890  24.749  1.00 23.05  ? 189 LEU   B CB    1 
ATOM   15432 C  CG    . LEU   F 2  187 ? 25.369  41.425  24.293  1.00 19.43  ? 189 LEU   B CG    1 
ATOM   15433 C  CD1   . LEU   F 2  187 ? 25.439  41.326  22.780  1.00 19.74  ? 189 LEU   B CD1   1 
ATOM   15434 C  CD2   . LEU   F 2  187 ? 26.588  40.782  24.893  1.00 10.98  ? 189 LEU   B CD2   1 
ATOM   15435 N  N     . SER   F 2  188 ? 23.791  45.406  26.318  1.00 24.31  ? 190 SER   B N     1 
ATOM   15436 C  CA    . SER   F 2  188 ? 23.763  46.847  26.542  1.00 17.93  ? 190 SER   B CA    1 
ATOM   15437 C  C     . SER   F 2  188 ? 23.642  47.195  28.015  1.00 22.31  ? 190 SER   B C     1 
ATOM   15438 O  O     . SER   F 2  188 ? 24.229  48.183  28.472  1.00 22.67  ? 190 SER   B O     1 
ATOM   15439 C  CB    . SER   F 2  188 ? 22.606  47.463  25.768  1.00 17.90  ? 190 SER   B CB    1 
ATOM   15440 O  OG    . SER   F 2  188 ? 22.774  47.214  24.381  1.00 19.92  ? 190 SER   B OG    1 
ATOM   15441 N  N     . VAL   F 2  189 ? 22.879  46.407  28.776  1.00 22.58  ? 191 VAL   B N     1 
ATOM   15442 C  CA    . VAL   F 2  189 ? 22.751  46.672  30.206  1.00 20.53  ? 191 VAL   B CA    1 
ATOM   15443 C  C     . VAL   F 2  189 ? 24.101  46.490  30.889  1.00 23.11  ? 191 VAL   B C     1 
ATOM   15444 O  O     . VAL   F 2  189 ? 24.560  47.342  31.659  1.00 26.28  ? 191 VAL   B O     1 
ATOM   15445 C  CB    . VAL   F 2  189 ? 21.665  45.774  30.820  1.00 23.25  ? 191 VAL   B CB    1 
ATOM   15446 C  CG1   . VAL   F 2  189 ? 21.645  45.936  32.340  1.00 17.69  ? 191 VAL   B CG1   1 
ATOM   15447 C  CG2   . VAL   F 2  189 ? 20.277  46.068  30.170  1.00 19.42  ? 191 VAL   B CG2   1 
ATOM   15448 N  N     . HIS   F 2  190 ? 24.766  45.383  30.589  1.00 23.99  ? 192 HIS   B N     1 
ATOM   15449 C  CA    . HIS   F 2  190 ? 26.132  45.148  31.043  1.00 20.44  ? 192 HIS   B CA    1 
ATOM   15450 C  C     . HIS   F 2  190 ? 27.035  46.363  30.824  1.00 26.07  ? 192 HIS   B C     1 
ATOM   15451 O  O     . HIS   F 2  190 ? 27.841  46.717  31.690  1.00 30.48  ? 192 HIS   B O     1 
ATOM   15452 C  CB    . HIS   F 2  190 ? 26.678  43.934  30.305  1.00 26.65  ? 192 HIS   B CB    1 
ATOM   15453 C  CG    . HIS   F 2  190 ? 28.063  43.574  30.698  1.00 31.55  ? 192 HIS   B CG    1 
ATOM   15454 N  ND1   . HIS   F 2  190 ? 28.553  43.799  31.966  1.00 32.45  ? 192 HIS   B ND1   1 
ATOM   15455 C  CD2   . HIS   F 2  190 ? 29.066  42.999  29.996  1.00 31.34  ? 192 HIS   B CD2   1 
ATOM   15456 C  CE1   . HIS   F 2  190 ? 29.806  43.390  32.026  1.00 32.31  ? 192 HIS   B CE1   1 
ATOM   15457 N  NE2   . HIS   F 2  190 ? 30.140  42.898  30.846  1.00 37.67  ? 192 HIS   B NE2   1 
ATOM   15458 N  N     . GLN   F 2  191 ? 26.932  46.999  29.660  1.00 23.05  ? 193 GLN   B N     1 
ATOM   15459 C  CA    . GLN   F 2  191 ? 27.702  48.206  29.409  1.00 16.88  ? 193 GLN   B CA    1 
ATOM   15460 C  C     . GLN   F 2  191 ? 27.229  49.343  30.296  1.00 26.47  ? 193 GLN   B C     1 
ATOM   15461 O  O     . GLN   F 2  191 ? 28.049  50.072  30.863  1.00 26.01  ? 193 GLN   B O     1 
ATOM   15462 C  CB    . GLN   F 2  191 ? 27.577  48.614  27.949  1.00 21.48  ? 193 GLN   B CB    1 
ATOM   15463 C  CG    . GLN   F 2  191 ? 28.092  47.626  26.967  1.00 19.32  ? 193 GLN   B CG    1 
ATOM   15464 C  CD    . GLN   F 2  191 ? 29.576  47.626  26.934  1.00 18.68  ? 193 GLN   B CD    1 
ATOM   15465 O  OE1   . GLN   F 2  191 ? 30.210  48.685  26.921  1.00 22.05  ? 193 GLN   B OE1   1 
ATOM   15466 N  NE2   . GLN   F 2  191 ? 30.159  46.439  26.943  1.00 19.47  ? 193 GLN   B NE2   1 
ATOM   15467 N  N     . LEU   F 2  192 ? 25.899  49.527  30.404  1.00 30.04  ? 194 LEU   B N     1 
ATOM   15468 C  CA    . LEU   F 2  192 ? 25.344  50.672  31.136  1.00 21.65  ? 194 LEU   B CA    1 
ATOM   15469 C  C     . LEU   F 2  192 ? 25.677  50.584  32.615  1.00 21.55  ? 194 LEU   B C     1 
ATOM   15470 O  O     . LEU   F 2  192 ? 25.974  51.604  33.249  1.00 23.11  ? 194 LEU   B O     1 
ATOM   15471 C  CB    . LEU   F 2  192 ? 23.823  50.778  30.933  1.00 16.44  ? 194 LEU   B CB    1 
ATOM   15472 C  CG    . LEU   F 2  192 ? 23.247  51.045  29.530  1.00 18.64  ? 194 LEU   B CG    1 
ATOM   15473 C  CD1   . LEU   F 2  192 ? 21.755  50.777  29.442  1.00 13.10  ? 194 LEU   B CD1   1 
ATOM   15474 C  CD2   . LEU   F 2  192 ? 23.549  52.465  29.063  1.00 21.24  ? 194 LEU   B CD2   1 
ATOM   15475 N  N     . VAL   F 2  193 ? 25.675  49.371  33.178  1.00 17.80  ? 195 VAL   B N     1 
ATOM   15476 C  CA    . VAL   F 2  193 ? 26.098  49.227  34.569  1.00 22.95  ? 195 VAL   B CA    1 
ATOM   15477 C  C     . VAL   F 2  193 ? 27.458  49.873  34.788  1.00 24.97  ? 195 VAL   B C     1 
ATOM   15478 O  O     . VAL   F 2  193 ? 27.663  50.599  35.765  1.00 29.96  ? 195 VAL   B O     1 
ATOM   15479 C  CB    . VAL   F 2  193 ? 26.122  47.748  34.993  1.00 19.48  ? 195 VAL   B CB    1 
ATOM   15480 C  CG1   . VAL   F 2  193 ? 26.857  47.643  36.275  1.00 18.93  ? 195 VAL   B CG1   1 
ATOM   15481 C  CG2   . VAL   F 2  193 ? 24.724  47.229  35.190  1.00 22.08  ? 195 VAL   B CG2   1 
ATOM   15482 N  N     . GLU   F 2  194 ? 28.413  49.615  33.886  1.00 27.40  ? 196 GLU   B N     1 
ATOM   15483 C  CA    . GLU   F 2  194 ? 29.804  50.000  34.103  1.00 21.39  ? 196 GLU   B CA    1 
ATOM   15484 C  C     . GLU   F 2  194 ? 30.112  51.433  33.682  1.00 22.16  ? 196 GLU   B C     1 
ATOM   15485 O  O     . GLU   F 2  194 ? 31.015  52.051  34.259  1.00 26.26  ? 196 GLU   B O     1 
ATOM   15486 C  CB    . GLU   F 2  194 ? 30.748  49.041  33.362  1.00 17.93  ? 196 GLU   B CB    1 
ATOM   15487 C  CG    . GLU   F 2  194 ? 30.390  47.530  33.440  1.00 24.89  ? 196 GLU   B CG    1 
ATOM   15488 C  CD    . GLU   F 2  194 ? 30.737  46.850  34.774  1.00 39.20  ? 196 GLU   B CD    1 
ATOM   15489 O  OE1   . GLU   F 2  194 ? 31.568  47.391  35.540  1.00 44.41  ? 196 GLU   B OE1   1 
ATOM   15490 O  OE2   . GLU   F 2  194 ? 30.171  45.765  35.056  1.00 35.06  ? 196 GLU   B OE2   1 
ATOM   15491 N  N     . ASN   F 2  195 ? 29.370  52.005  32.730  1.00 20.37  ? 197 ASN   B N     1 
ATOM   15492 C  CA    . ASN   F 2  195 ? 29.801  53.239  32.090  1.00 23.66  ? 197 ASN   B CA    1 
ATOM   15493 C  C     . ASN   F 2  195 ? 28.829  54.425  32.101  1.00 26.35  ? 197 ASN   B C     1 
ATOM   15494 O  O     . ASN   F 2  195 ? 29.150  55.449  31.495  1.00 30.94  ? 197 ASN   B O     1 
ATOM   15495 C  CB    . ASN   F 2  195 ? 30.189  52.956  30.632  1.00 21.87  ? 197 ASN   B CB    1 
ATOM   15496 C  CG    . ASN   F 2  195 ? 31.520  52.228  30.511  1.00 30.09  ? 197 ASN   B CG    1 
ATOM   15497 O  OD1   . ASN   F 2  195 ? 32.443  52.448  31.309  1.00 33.53  ? 197 ASN   B OD1   1 
ATOM   15498 N  ND2   . ASN   F 2  195 ? 31.629  51.359  29.507  1.00 29.31  ? 197 ASN   B ND2   1 
ATOM   15499 N  N     . THR   F 2  196 ? 27.681  54.354  32.753  1.00 18.12  ? 198 THR   B N     1 
ATOM   15500 C  CA    . THR   F 2  196 ? 26.852  55.545  32.841  1.00 20.66  ? 198 THR   B CA    1 
ATOM   15501 C  C     . THR   F 2  196 ? 26.631  55.936  34.303  1.00 28.35  ? 198 THR   B C     1 
ATOM   15502 O  O     . THR   F 2  196 ? 26.565  55.077  35.199  1.00 20.80  ? 198 THR   B O     1 
ATOM   15503 C  CB    . THR   F 2  196 ? 25.489  55.362  32.141  1.00 19.14  ? 198 THR   B CB    1 
ATOM   15504 O  OG1   . THR   F 2  196 ? 24.707  54.380  32.826  1.00 22.40  ? 198 THR   B OG1   1 
ATOM   15505 C  CG2   . THR   F 2  196 ? 25.668  54.929  30.735  1.00 19.02  ? 198 THR   B CG2   1 
ATOM   15506 N  N     . ASP   F 2  197 ? 26.506  57.253  34.535  1.00 23.00  ? 199 ASP   B N     1 
ATOM   15507 C  CA    . ASP   F 2  197 ? 26.164  57.752  35.869  1.00 20.66  ? 199 ASP   B CA    1 
ATOM   15508 C  C     . ASP   F 2  197 ? 24.662  57.660  36.158  1.00 23.29  ? 199 ASP   B C     1 
ATOM   15509 O  O     . ASP   F 2  197 ? 24.267  57.255  37.259  1.00 22.06  ? 199 ASP   B O     1 
ATOM   15510 C  CB    . ASP   F 2  197 ? 26.635  59.191  36.008  1.00 27.82  ? 199 ASP   B CB    1 
ATOM   15511 C  CG    . ASP   F 2  197 ? 28.077  59.336  35.702  1.00 22.41  ? 199 ASP   B CG    1 
ATOM   15512 O  OD1   . ASP   F 2  197 ? 28.856  58.785  36.496  1.00 23.46  ? 199 ASP   B OD1   1 
ATOM   15513 O  OD2   . ASP   F 2  197 ? 28.414  59.959  34.665  1.00 25.00  ? 199 ASP   B OD2   1 
ATOM   15514 N  N     . GLU   F 2  198 ? 23.816  58.022  35.183  1.00 24.08  ? 200 GLU   B N     1 
ATOM   15515 C  CA    . GLU   F 2  198 ? 22.363  57.988  35.329  1.00 24.14  ? 200 GLU   B CA    1 
ATOM   15516 C  C     . GLU   F 2  198 ? 21.721  57.444  34.066  1.00 23.57  ? 200 GLU   B C     1 
ATOM   15517 O  O     . GLU   F 2  198 ? 21.956  57.985  32.983  1.00 31.24  ? 200 GLU   B O     1 
ATOM   15518 C  CB    . GLU   F 2  198 ? 21.804  59.383  35.593  1.00 22.32  ? 200 GLU   B CB    1 
ATOM   15519 C  CG    . GLU   F 2  198 ? 22.567  60.149  36.639  1.00 22.17  ? 200 GLU   B CG    1 
ATOM   15520 C  CD    . GLU   F 2  198 ? 22.730  61.605  36.261  1.00 27.52  ? 200 GLU   B CD    1 
ATOM   15521 O  OE1   . GLU   F 2  198 ? 22.880  61.925  35.054  1.00 28.63  ? 200 GLU   B OE1   1 
ATOM   15522 O  OE2   . GLU   F 2  198 ? 22.699  62.436  37.182  1.00 26.23  ? 200 GLU   B OE2   1 
ATOM   15523 N  N     . THR   F 2  199 ? 20.885  56.412  34.210  1.00 22.25  ? 201 THR   B N     1 
ATOM   15524 C  CA    . THR   F 2  199 ? 20.109  55.840  33.112  1.00 18.93  ? 201 THR   B CA    1 
ATOM   15525 C  C     . THR   F 2  199 ? 18.625  55.819  33.464  1.00 20.63  ? 201 THR   B C     1 
ATOM   15526 O  O     . THR   F 2  199 ? 18.238  55.218  34.472  1.00 22.43  ? 201 THR   B O     1 
ATOM   15527 C  CB    . THR   F 2  199 ? 20.598  54.430  32.787  1.00 20.66  ? 201 THR   B CB    1 
ATOM   15528 O  OG1   . THR   F 2  199 ? 21.850  54.542  32.114  1.00 25.41  ? 201 THR   B OG1   1 
ATOM   15529 C  CG2   . THR   F 2  199 ? 19.589  53.665  31.880  1.00 17.06  ? 201 THR   B CG2   1 
ATOM   15530 N  N     . TYR   F 2  200 ? 17.797  56.472  32.635  1.00 16.64  ? 202 TYR   B N     1 
ATOM   15531 C  CA    . TYR   F 2  200 ? 16.341  56.364  32.727  1.00 16.61  ? 202 TYR   B CA    1 
ATOM   15532 C  C     . TYR   F 2  200 ? 15.880  55.135  31.952  1.00 18.23  ? 202 TYR   B C     1 
ATOM   15533 O  O     . TYR   F 2  200 ? 16.249  54.956  30.787  1.00 20.82  ? 202 TYR   B O     1 
ATOM   15534 C  CB    . TYR   F 2  200 ? 15.644  57.622  32.187  1.00 15.05  ? 202 TYR   B CB    1 
ATOM   15535 C  CG    . TYR   F 2  200 ? 16.066  58.916  32.850  1.00 21.22  ? 202 TYR   B CG    1 
ATOM   15536 C  CD1   . TYR   F 2  200 ? 15.635  59.232  34.142  1.00 21.11  ? 202 TYR   B CD1   1 
ATOM   15537 C  CD2   . TYR   F 2  200 ? 16.883  59.833  32.182  1.00 19.29  ? 202 TYR   B CD2   1 
ATOM   15538 C  CE1   . TYR   F 2  200 ? 16.017  60.435  34.768  1.00 21.89  ? 202 TYR   B CE1   1 
ATOM   15539 C  CE2   . TYR   F 2  200 ? 17.264  61.030  32.778  1.00 22.76  ? 202 TYR   B CE2   1 
ATOM   15540 C  CZ    . TYR   F 2  200 ? 16.836  61.329  34.078  1.00 30.57  ? 202 TYR   B CZ    1 
ATOM   15541 O  OH    . TYR   F 2  200 ? 17.238  62.513  34.676  1.00 23.16  ? 202 TYR   B OH    1 
ATOM   15542 N  N     . CYS   F 2  201 ? 15.077  54.290  32.590  1.00 16.13  ? 203 CYS   B N     1 
ATOM   15543 C  CA    . CYS   F 2  201 ? 14.631  53.039  31.970  1.00 16.49  ? 203 CYS   B CA    1 
ATOM   15544 C  C     . CYS   F 2  201 ? 13.248  53.237  31.386  1.00 16.55  ? 203 CYS   B C     1 
ATOM   15545 O  O     . CYS   F 2  201 ? 12.244  53.013  32.055  1.00 23.12  ? 203 CYS   B O     1 
ATOM   15546 C  CB    . CYS   F 2  201 ? 14.614  51.909  32.976  1.00 18.41  ? 203 CYS   B CB    1 
ATOM   15547 S  SG    . CYS   F 2  201 ? 16.186  51.690  33.665  1.00 32.35  ? 203 CYS   B SG    1 
ATOM   15548 N  N     . ILE   F 2  202 ? 13.199  53.677  30.133  1.00 18.77  ? 204 ILE   B N     1 
ATOM   15549 C  CA    . ILE   F 2  202 ? 11.946  53.758  29.389  1.00 18.57  ? 204 ILE   B CA    1 
ATOM   15550 C  C     . ILE   F 2  202 ? 11.636  52.365  28.850  1.00 20.24  ? 204 ILE   B C     1 
ATOM   15551 O  O     . ILE   F 2  202 ? 12.265  51.879  27.908  1.00 22.55  ? 204 ILE   B O     1 
ATOM   15552 C  CB    . ILE   F 2  202 ? 12.016  54.789  28.266  1.00 17.56  ? 204 ILE   B CB    1 
ATOM   15553 C  CG1   . ILE   F 2  202 ? 12.187  56.166  28.886  1.00 10.13  ? 204 ILE   B CG1   1 
ATOM   15554 C  CG2   . ILE   F 2  202 ? 10.775  54.684  27.384  1.00 15.22  ? 204 ILE   B CG2   1 
ATOM   15555 C  CD1   . ILE   F 2  202 ? 13.593  56.547  28.988  1.00 14.61  ? 204 ILE   B CD1   1 
ATOM   15556 N  N     . ASP   F 2  203 ? 10.679  51.718  29.468  1.00 18.19  ? 205 ASP   B N     1 
ATOM   15557 C  CA    . ASP   F 2  203 ? 10.341  50.346  29.183  1.00 14.45  ? 205 ASP   B CA    1 
ATOM   15558 C  C     . ASP   F 2  203 ? 9.195   50.325  28.185  1.00 15.75  ? 205 ASP   B C     1 
ATOM   15559 O  O     . ASP   F 2  203 ? 8.172   50.994  28.387  1.00 13.26  ? 205 ASP   B O     1 
ATOM   15560 C  CB    . ASP   F 2  203 ? 9.960   49.693  30.503  1.00 18.96  ? 205 ASP   B CB    1 
ATOM   15561 C  CG    . ASP   F 2  203 ? 9.786   48.231  30.402  1.00 19.82  ? 205 ASP   B CG    1 
ATOM   15562 O  OD1   . ASP   F 2  203 ? 9.824   47.675  29.293  1.00 22.81  ? 205 ASP   B OD1   1 
ATOM   15563 O  OD2   . ASP   F 2  203 ? 9.597   47.632  31.466  1.00 28.05  ? 205 ASP   B OD2   1 
ATOM   15564 N  N     . ASN   F 2  204 ? 9.366   49.575  27.099  1.00 16.33  ? 206 ASN   B N     1 
ATOM   15565 C  CA    . ASN   F 2  204 ? 8.290   49.535  26.120  1.00 19.21  ? 206 ASN   B CA    1 
ATOM   15566 C  C     . ASN   F 2  204 ? 7.128   48.674  26.584  1.00 21.47  ? 206 ASN   B C     1 
ATOM   15567 O  O     . ASN   F 2  204 ? 6.016   48.842  26.073  1.00 23.35  ? 206 ASN   B O     1 
ATOM   15568 C  CB    . ASN   F 2  204 ? 8.807   49.081  24.752  1.00 19.53  ? 206 ASN   B CB    1 
ATOM   15569 C  CG    . ASN   F 2  204 ? 9.211   50.249  23.877  1.00 17.65  ? 206 ASN   B CG    1 
ATOM   15570 O  OD1   . ASN   F 2  204 ? 9.179   51.395  24.302  1.00 22.37  ? 206 ASN   B OD1   1 
ATOM   15571 N  ND2   . ASN   F 2  204 ? 9.609   49.963  22.666  1.00 19.49  ? 206 ASN   B ND2   1 
ATOM   15572 N  N     . GLU   F 2  205 ? 7.339   47.799  27.569  1.00 17.57  ? 207 GLU   B N     1 
ATOM   15573 C  CA    . GLU   F 2  205 ? 6.202   47.136  28.199  1.00 19.36  ? 207 GLU   B CA    1 
ATOM   15574 C  C     . GLU   F 2  205 ? 5.292   48.144  28.886  1.00 20.98  ? 207 GLU   B C     1 
ATOM   15575 O  O     . GLU   F 2  205 ? 4.074   48.147  28.668  1.00 27.94  ? 207 GLU   B O     1 
ATOM   15576 C  CB    . GLU   F 2  205 ? 6.672   46.086  29.198  1.00 24.80  ? 207 GLU   B CB    1 
ATOM   15577 C  CG    . GLU   F 2  205 ? 5.569   45.151  29.640  1.00 26.71  ? 207 GLU   B CG    1 
ATOM   15578 C  CD    . GLU   F 2  205 ? 6.006   43.702  29.590  1.00 36.22  ? 207 GLU   B CD    1 
ATOM   15579 O  OE1   . GLU   F 2  205 ? 6.768   43.368  28.643  1.00 26.94  ? 207 GLU   B OE1   1 
ATOM   15580 O  OE2   . GLU   F 2  205 ? 5.604   42.914  30.495  1.00 35.93  ? 207 GLU   B OE2   1 
ATOM   15581 N  N     . ALA   F 2  206 ? 5.867   49.015  29.721  1.00 18.39  ? 208 ALA   B N     1 
ATOM   15582 C  CA    . ALA   F 2  206 ? 5.070   50.032  30.397  1.00 15.88  ? 208 ALA   B CA    1 
ATOM   15583 C  C     . ALA   F 2  206 ? 4.451   51.014  29.401  1.00 21.23  ? 208 ALA   B C     1 
ATOM   15584 O  O     . ALA   F 2  206 ? 3.257   51.326  29.486  1.00 21.17  ? 208 ALA   B O     1 
ATOM   15585 C  CB    . ALA   F 2  206 ? 5.923   50.763  31.427  1.00 16.72  ? 208 ALA   B CB    1 
ATOM   15586 N  N     . LEU   F 2  207 ? 5.242   51.501  28.434  1.00 20.82  ? 209 LEU   B N     1 
ATOM   15587 C  CA    . LEU   F 2  207 ? 4.698   52.398  27.410  1.00 20.78  ? 209 LEU   B CA    1 
ATOM   15588 C  C     . LEU   F 2  207 ? 3.550   51.754  26.639  1.00 22.70  ? 209 LEU   B C     1 
ATOM   15589 O  O     . LEU   F 2  207 ? 2.571   52.427  26.298  1.00 20.63  ? 209 LEU   B O     1 
ATOM   15590 C  CB    . LEU   F 2  207 ? 5.787   52.832  26.434  1.00 21.26  ? 209 LEU   B CB    1 
ATOM   15591 C  CG    . LEU   F 2  207 ? 6.921   53.607  27.073  1.00 19.71  ? 209 LEU   B CG    1 
ATOM   15592 C  CD1   . LEU   F 2  207 ? 7.909   53.904  26.005  1.00 15.94  ? 209 LEU   B CD1   1 
ATOM   15593 C  CD2   . LEU   F 2  207 ? 6.360   54.881  27.660  1.00 19.38  ? 209 LEU   B CD2   1 
ATOM   15594 N  N     . TYR   F 2  208 ? 3.658   50.462  26.319  1.00 26.53  ? 210 TYR   B N     1 
ATOM   15595 C  CA    . TYR   F 2  208 ? 2.535   49.802  25.656  1.00 25.77  ? 210 TYR   B CA    1 
ATOM   15596 C  C     . TYR   F 2  208 ? 1.344   49.646  26.607  1.00 26.69  ? 210 TYR   B C     1 
ATOM   15597 O  O     . TYR   F 2  208 ? 0.206   49.946  26.235  1.00 25.82  ? 210 TYR   B O     1 
ATOM   15598 C  CB    . TYR   F 2  208 ? 2.967   48.449  25.073  1.00 25.54  ? 210 TYR   B CB    1 
ATOM   15599 C  CG    . TYR   F 2  208 ? 1.799   47.581  24.620  1.00 23.30  ? 210 TYR   B CG    1 
ATOM   15600 C  CD1   . TYR   F 2  208 ? 1.233   47.715  23.352  1.00 19.06  ? 210 TYR   B CD1   1 
ATOM   15601 C  CD2   . TYR   F 2  208 ? 1.264   46.632  25.469  1.00 25.35  ? 210 TYR   B CD2   1 
ATOM   15602 C  CE1   . TYR   F 2  208 ? 0.144   46.921  22.963  1.00 24.89  ? 210 TYR   B CE1   1 
ATOM   15603 C  CE2   . TYR   F 2  208 ? 0.198   45.851  25.093  1.00 24.34  ? 210 TYR   B CE2   1 
ATOM   15604 C  CZ    . TYR   F 2  208 ? -0.373  45.993  23.851  1.00 22.01  ? 210 TYR   B CZ    1 
ATOM   15605 O  OH    . TYR   F 2  208 ? -1.448  45.187  23.529  1.00 23.47  ? 210 TYR   B OH    1 
ATOM   15606 N  N     . ASP   F 2  209 ? 1.577   49.201  27.848  1.00 24.82  ? 211 ASP   B N     1 
ATOM   15607 C  CA    . ASP   F 2  209 ? 0.445   48.972  28.743  1.00 28.80  ? 211 ASP   B CA    1 
ATOM   15608 C  C     . ASP   F 2  209 ? -0.332  50.262  28.994  1.00 26.62  ? 211 ASP   B C     1 
ATOM   15609 O  O     . ASP   F 2  209 ? -1.566  50.266  28.947  1.00 29.41  ? 211 ASP   B O     1 
ATOM   15610 C  CB    . ASP   F 2  209 ? 0.908   48.335  30.060  1.00 36.12  ? 211 ASP   B CB    1 
ATOM   15611 C  CG    . ASP   F 2  209 ? 1.170   46.811  29.928  1.00 53.33  ? 211 ASP   B CG    1 
ATOM   15612 O  OD1   . ASP   F 2  209 ? 2.334   46.406  29.695  1.00 50.11  ? 211 ASP   B OD1   1 
ATOM   15613 O  OD2   . ASP   F 2  209 ? 0.209   46.008  30.050  1.00 68.40  ? 211 ASP   B OD2   1 
ATOM   15614 N  N     . ILE   F 2  210 ? 0.364   51.369  29.244  1.00 20.34  ? 212 ILE   B N     1 
ATOM   15615 C  CA    . ILE   F 2  210 ? -0.318  52.654  29.386  1.00 16.47  ? 212 ILE   B CA    1 
ATOM   15616 C  C     . ILE   F 2  210 ? -1.170  52.945  28.146  1.00 31.09  ? 212 ILE   B C     1 
ATOM   15617 O  O     . ILE   F 2  210 ? -2.397  53.108  28.225  1.00 32.89  ? 212 ILE   B O     1 
ATOM   15618 C  CB    . ILE   F 2  210 ? 0.704   53.776  29.631  1.00 13.63  ? 212 ILE   B CB    1 
ATOM   15619 C  CG1   . ILE   F 2  210 ? 1.482   53.573  30.929  1.00 18.39  ? 212 ILE   B CG1   1 
ATOM   15620 C  CG2   . ILE   F 2  210 ? 0.025   55.124  29.632  1.00 20.76  ? 212 ILE   B CG2   1 
ATOM   15621 C  CD1   . ILE   F 2  210 ? 2.652   54.527  31.059  1.00 17.96  ? 212 ILE   B CD1   1 
ATOM   15622 N  N     . CYS   F 2  211 ? -0.522  53.024  26.978  1.00 26.62  ? 213 CYS   B N     1 
ATOM   15623 C  CA    . CYS   F 2  211 ? -1.211  53.388  25.746  1.00 18.89  ? 213 CYS   B CA    1 
ATOM   15624 C  C     . CYS   F 2  211 ? -2.414  52.488  25.468  1.00 32.17  ? 213 CYS   B C     1 
ATOM   15625 O  O     . CYS   F 2  211 ? -3.466  52.969  25.025  1.00 35.58  ? 213 CYS   B O     1 
ATOM   15626 C  CB    . CYS   F 2  211 ? -0.238  53.322  24.574  1.00 17.67  ? 213 CYS   B CB    1 
ATOM   15627 S  SG    . CYS   F 2  211 ? 0.914   54.681  24.437  1.00 24.85  ? 213 CYS   B SG    1 
ATOM   15628 N  N     . PHE   F 2  212 ? -2.275  51.173  25.687  1.00 32.83  ? 214 PHE   B N     1 
ATOM   15629 C  CA    . PHE   F 2  212 ? -3.306  50.229  25.246  1.00 27.27  ? 214 PHE   B CA    1 
ATOM   15630 C  C     . PHE   F 2  212 ? -4.462  50.156  26.233  1.00 27.24  ? 214 PHE   B C     1 
ATOM   15631 O  O     . PHE   F 2  212 ? -5.615  50.415  25.871  1.00 33.57  ? 214 PHE   B O     1 
ATOM   15632 C  CB    . PHE   F 2  212 ? -2.706  48.837  25.032  1.00 26.99  ? 214 PHE   B CB    1 
ATOM   15633 C  CG    . PHE   F 2  212 ? -3.683  47.843  24.492  1.00 26.51  ? 214 PHE   B CG    1 
ATOM   15634 C  CD1   . PHE   F 2  212 ? -4.200  47.989  23.212  1.00 26.51  ? 214 PHE   B CD1   1 
ATOM   15635 C  CD2   . PHE   F 2  212 ? -4.089  46.768  25.255  1.00 27.35  ? 214 PHE   B CD2   1 
ATOM   15636 C  CE1   . PHE   F 2  212 ? -5.111  47.090  22.712  1.00 26.42  ? 214 PHE   B CE1   1 
ATOM   15637 C  CE2   . PHE   F 2  212 ? -5.000  45.856  24.755  1.00 30.17  ? 214 PHE   B CE2   1 
ATOM   15638 C  CZ    . PHE   F 2  212 ? -5.511  46.017  23.484  1.00 31.05  ? 214 PHE   B CZ    1 
ATOM   15639 N  N     . ARG   F 2  213 ? -4.173  49.781  27.478  1.00 23.74  ? 215 ARG   B N     1 
ATOM   15640 C  CA    . ARG   F 2  213 ? -5.138  49.857  28.569  1.00 28.43  ? 215 ARG   B CA    1 
ATOM   15641 C  C     . ARG   F 2  213 ? -5.511  51.297  28.905  1.00 31.55  ? 215 ARG   B C     1 
ATOM   15642 O  O     . ARG   F 2  213 ? -6.408  51.874  28.289  1.00 36.61  ? 215 ARG   B O     1 
ATOM   15643 C  CB    . ARG   F 2  213 ? -4.576  49.165  29.800  1.00 31.56  ? 215 ARG   B CB    1 
ATOM   15644 C  CG    . ARG   F 2  213 ? -4.243  47.712  29.534  1.00 46.04  ? 215 ARG   B CG    1 
ATOM   15645 C  CD    . ARG   F 2  213 ? -3.380  47.143  30.633  1.00 52.72  ? 215 ARG   B CD    1 
ATOM   15646 N  NE    . ARG   F 2  213 ? -3.615  47.832  31.895  1.00 65.26  ? 215 ARG   B NE    1 
ATOM   15647 C  CZ    . ARG   F 2  213 ? -2.817  47.741  32.952  1.00 75.06  ? 215 ARG   B CZ    1 
ATOM   15648 N  NH1   . ARG   F 2  213 ? -1.761  46.937  32.954  1.00 65.34  ? 215 ARG   B NH1   1 
ATOM   15649 N  NH2   . ARG   F 2  213 ? -3.078  48.483  34.028  1.00 57.99  ? 215 ARG   B NH2   1 
ATOM   15650 N  N     . THR   F 2  214 ? -4.804  51.903  29.855  1.00 28.76  ? 216 THR   B N     1 
ATOM   15651 C  CA    . THR   F 2  214 ? -5.161  53.232  30.343  1.00 31.76  ? 216 THR   B CA    1 
ATOM   15652 C  C     . THR   F 2  214 ? -5.682  54.195  29.257  1.00 33.23  ? 216 THR   B C     1 
ATOM   15653 O  O     . THR   F 2  214 ? -6.844  54.627  29.312  1.00 33.57  ? 216 THR   B O     1 
ATOM   15654 C  CB    . THR   F 2  214 ? -3.965  53.823  31.091  1.00 25.13  ? 216 THR   B CB    1 
ATOM   15655 O  OG1   . THR   F 2  214 ? -3.892  53.222  32.391  1.00 29.98  ? 216 THR   B OG1   1 
ATOM   15656 C  CG2   . THR   F 2  214 ? -4.116  55.327  31.237  1.00 22.09  ? 216 THR   B CG2   1 
ATOM   15657 N  N     . LEU   F 2  215 ? -4.861  54.554  28.265  1.00 26.15  ? 217 LEU   B N     1 
ATOM   15658 C  CA    . LEU   F 2  215 ? -5.354  55.501  27.264  1.00 26.72  ? 217 LEU   B CA    1 
ATOM   15659 C  C     . LEU   F 2  215 ? -6.260  54.850  26.228  1.00 25.79  ? 217 LEU   B C     1 
ATOM   15660 O  O     . LEU   F 2  215 ? -6.766  55.548  25.347  1.00 27.08  ? 217 LEU   B O     1 
ATOM   15661 C  CB    . LEU   F 2  215 ? -4.203  56.215  26.539  1.00 26.28  ? 217 LEU   B CB    1 
ATOM   15662 C  CG    . LEU   F 2  215 ? -3.122  56.877  27.382  1.00 23.54  ? 217 LEU   B CG    1 
ATOM   15663 C  CD1   . LEU   F 2  215 ? -2.153  57.655  26.500  1.00 25.20  ? 217 LEU   B CD1   1 
ATOM   15664 C  CD2   . LEU   F 2  215 ? -3.756  57.778  28.428  1.00 23.97  ? 217 LEU   B CD2   1 
ATOM   15665 N  N     . LYS   F 2  216 ? -6.474  53.543  26.297  1.00 23.74  ? 218 LYS   B N     1 
ATOM   15666 C  CA    . LYS   F 2  216 ? -7.431  52.880  25.408  1.00 31.01  ? 218 LYS   B CA    1 
ATOM   15667 C  C     . LYS   F 2  216 ? -7.070  53.079  23.940  1.00 31.65  ? 218 LYS   B C     1 
ATOM   15668 O  O     . LYS   F 2  216 ? -7.935  53.320  23.099  1.00 36.47  ? 218 LYS   B O     1 
ATOM   15669 C  CB    . LYS   F 2  216 ? -8.863  53.359  25.672  1.00 28.77  ? 218 LYS   B CB    1 
ATOM   15670 C  CG    . LYS   F 2  216 ? -9.345  53.168  27.115  1.00 35.05  ? 218 LYS   B CG    1 
ATOM   15671 C  CD    . LYS   F 2  216 ? -9.341  51.709  27.522  1.00 32.61  ? 218 LYS   B CD    1 
ATOM   15672 C  CE    . LYS   F 2  216 ? -9.490  51.564  29.025  1.00 38.41  ? 218 LYS   B CE    1 
ATOM   15673 N  NZ    . LYS   F 2  216 ? -9.251  50.153  29.473  1.00 48.16  ? 218 LYS   B NZ    1 
ATOM   15674 N  N     . LEU   F 2  217 ? -5.784  52.973  23.627  1.00 34.12  ? 219 LEU   B N     1 
ATOM   15675 C  CA    . LEU   F 2  217 ? -5.308  53.066  22.250  1.00 30.10  ? 219 LEU   B CA    1 
ATOM   15676 C  C     . LEU   F 2  217 ? -5.311  51.663  21.651  1.00 33.23  ? 219 LEU   B C     1 
ATOM   15677 O  O     . LEU   F 2  217 ? -4.407  50.861  21.887  1.00 33.52  ? 219 LEU   B O     1 
ATOM   15678 C  CB    . LEU   F 2  217 ? -3.936  53.721  22.202  1.00 26.68  ? 219 LEU   B CB    1 
ATOM   15679 C  CG    . LEU   F 2  217 ? -3.965  55.207  22.552  1.00 28.51  ? 219 LEU   B CG    1 
ATOM   15680 C  CD1   . LEU   F 2  217 ? -2.573  55.793  22.491  1.00 27.75  ? 219 LEU   B CD1   1 
ATOM   15681 C  CD2   . LEU   F 2  217 ? -4.863  55.938  21.585  1.00 23.81  ? 219 LEU   B CD2   1 
ATOM   15682 N  N     . THR   F 2  218 ? -6.339  51.385  20.858  1.00 40.67  ? 220 THR   B N     1 
ATOM   15683 C  CA    . THR   F 2  218 ? -6.620  50.034  20.390  1.00 32.39  ? 220 THR   B CA    1 
ATOM   15684 C  C     . THR   F 2  218 ? -5.507  49.517  19.477  1.00 33.05  ? 220 THR   B C     1 
ATOM   15685 O  O     . THR   F 2  218 ? -5.173  48.321  19.494  1.00 27.53  ? 220 THR   B O     1 
ATOM   15686 C  CB    . THR   F 2  218 ? -7.978  50.070  19.681  1.00 22.68  ? 220 THR   B CB    1 
ATOM   15687 O  OG1   . THR   F 2  218 ? -8.225  48.860  18.961  1.00 46.41  ? 220 THR   B OG1   1 
ATOM   15688 C  CG2   . THR   F 2  218 ? -8.024  51.271  18.711  1.00 31.43  ? 220 THR   B CG2   1 
ATOM   15689 N  N     . THR   F 2  219 ? -4.927  50.403  18.669  1.00 28.26  ? 221 THR   B N     1 
ATOM   15690 C  CA    . THR   F 2  219 ? -3.899  50.044  17.693  1.00 30.28  ? 221 THR   B CA    1 
ATOM   15691 C  C     . THR   F 2  219 ? -2.749  51.028  17.853  1.00 25.66  ? 221 THR   B C     1 
ATOM   15692 O  O     . THR   F 2  219 ? -2.568  51.938  17.039  1.00 27.33  ? 221 THR   B O     1 
ATOM   15693 C  CB    . THR   F 2  219 ? -4.455  50.041  16.262  1.00 27.44  ? 221 THR   B CB    1 
ATOM   15694 O  OG1   . THR   F 2  219 ? -5.183  51.247  16.009  1.00 29.04  ? 221 THR   B OG1   1 
ATOM   15695 C  CG2   . THR   F 2  219 ? -5.381  48.863  16.047  1.00 19.18  ? 221 THR   B CG2   1 
ATOM   15696 N  N     . PRO   F 2  220 ? -1.958  50.878  18.910  1.00 28.35  ? 222 PRO   B N     1 
ATOM   15697 C  CA    . PRO   F 2  220 ? -0.954  51.896  19.235  1.00 28.25  ? 222 PRO   B CA    1 
ATOM   15698 C  C     . PRO   F 2  220 ? 0.195   51.928  18.232  1.00 30.60  ? 222 PRO   B C     1 
ATOM   15699 O  O     . PRO   F 2  220 ? 0.447   50.984  17.477  1.00 24.81  ? 222 PRO   B O     1 
ATOM   15700 C  CB    . PRO   F 2  220 ? -0.474  51.474  20.627  1.00 27.41  ? 222 PRO   B CB    1 
ATOM   15701 C  CG    . PRO   F 2  220 ? -0.715  49.977  20.647  1.00 23.07  ? 222 PRO   B CG    1 
ATOM   15702 C  CD    . PRO   F 2  220 ? -1.970  49.772  19.889  1.00 23.05  ? 222 PRO   B CD    1 
ATOM   15703 N  N     . THR   F 2  221 ? 0.904   53.050  18.242  1.00 27.02  ? 223 THR   B N     1 
ATOM   15704 C  CA    . THR   F 2  221 ? 2.014   53.269  17.337  1.00 25.11  ? 223 THR   B CA    1 
ATOM   15705 C  C     . THR   F 2  221 ? 3.192   53.808  18.119  1.00 25.29  ? 223 THR   B C     1 
ATOM   15706 O  O     . THR   F 2  221 ? 3.049   54.300  19.235  1.00 27.38  ? 223 THR   B O     1 
ATOM   15707 C  CB    . THR   F 2  221 ? 1.676   54.276  16.255  1.00 24.27  ? 223 THR   B CB    1 
ATOM   15708 O  OG1   . THR   F 2  221 ? 1.546   55.549  16.882  1.00 23.29  ? 223 THR   B OG1   1 
ATOM   15709 C  CG2   . THR   F 2  221 ? 0.379   53.903  15.543  1.00 15.45  ? 223 THR   B CG2   1 
ATOM   15710 N  N     . TYR   F 2  222 ? 4.369   53.737  17.507  1.00 30.18  ? 224 TYR   B N     1 
ATOM   15711 C  CA    . TYR   F 2  222 ? 5.545   54.304  18.157  1.00 24.49  ? 224 TYR   B CA    1 
ATOM   15712 C  C     . TYR   F 2  222 ? 5.364   55.798  18.417  1.00 22.70  ? 224 TYR   B C     1 
ATOM   15713 O  O     . TYR   F 2  222 ? 5.905   56.329  19.387  1.00 27.55  ? 224 TYR   B O     1 
ATOM   15714 C  CB    . TYR   F 2  222 ? 6.793   54.011  17.311  1.00 15.46  ? 224 TYR   B CB    1 
ATOM   15715 C  CG    . TYR   F 2  222 ? 7.368   52.651  17.601  1.00 16.22  ? 224 TYR   B CG    1 
ATOM   15716 C  CD1   . TYR   F 2  222 ? 7.515   52.215  18.924  1.00 21.48  ? 224 TYR   B CD1   1 
ATOM   15717 C  CD2   . TYR   F 2  222 ? 7.705   51.769  16.581  1.00 12.01  ? 224 TYR   B CD2   1 
ATOM   15718 C  CE1   . TYR   F 2  222 ? 8.041   50.952  19.234  1.00 17.28  ? 224 TYR   B CE1   1 
ATOM   15719 C  CE2   . TYR   F 2  222 ? 8.206   50.494  16.873  1.00 12.49  ? 224 TYR   B CE2   1 
ATOM   15720 C  CZ    . TYR   F 2  222 ? 8.388   50.098  18.208  1.00 18.51  ? 224 TYR   B CZ    1 
ATOM   15721 O  OH    . TYR   F 2  222 ? 8.918   48.863  18.543  1.00 21.47  ? 224 TYR   B OH    1 
ATOM   15722 N  N     . GLY   F 2  223 ? 4.602   56.494  17.571  1.00 31.14  ? 225 GLY   B N     1 
ATOM   15723 C  CA    . GLY   F 2  223 ? 4.294   57.888  17.835  1.00 22.78  ? 225 GLY   B CA    1 
ATOM   15724 C  C     . GLY   F 2  223 ? 3.471   58.085  19.092  1.00 27.13  ? 225 GLY   B C     1 
ATOM   15725 O  O     . GLY   F 2  223 ? 3.558   59.150  19.709  1.00 29.51  ? 225 GLY   B O     1 
ATOM   15726 N  N     . ASP   F 2  224 ? 2.652   57.086  19.462  1.00 23.93  ? 226 ASP   B N     1 
ATOM   15727 C  CA    . ASP   F 2  224 ? 1.894   57.106  20.709  1.00 21.48  ? 226 ASP   B CA    1 
ATOM   15728 C  C     . ASP   F 2  224 ? 2.803   56.836  21.885  1.00 24.08  ? 226 ASP   B C     1 
ATOM   15729 O  O     . ASP   F 2  224 ? 2.765   57.555  22.888  1.00 26.46  ? 226 ASP   B O     1 
ATOM   15730 C  CB    . ASP   F 2  224 ? 0.770   56.056  20.715  1.00 26.26  ? 226 ASP   B CB    1 
ATOM   15731 C  CG    . ASP   F 2  224 ? -0.177  56.177  19.527  1.00 39.21  ? 226 ASP   B CG    1 
ATOM   15732 O  OD1   . ASP   F 2  224 ? -0.308  57.308  18.970  1.00 41.81  ? 226 ASP   B OD1   1 
ATOM   15733 O  OD2   . ASP   F 2  224 ? -0.804  55.139  19.167  1.00 32.96  ? 226 ASP   B OD2   1 
ATOM   15734 N  N     . LEU   F 2  225 ? 3.578   55.754  21.801  1.00 25.18  ? 227 LEU   B N     1 
ATOM   15735 C  CA    . LEU   F 2  225 ? 4.620   55.501  22.785  1.00 21.80  ? 227 LEU   B CA    1 
ATOM   15736 C  C     . LEU   F 2  225 ? 5.470   56.746  22.985  1.00 24.44  ? 227 LEU   B C     1 
ATOM   15737 O  O     . LEU   F 2  225 ? 5.554   57.303  24.086  1.00 21.73  ? 227 LEU   B O     1 
ATOM   15738 C  CB    . LEU   F 2  225 ? 5.486   54.346  22.316  1.00 15.77  ? 227 LEU   B CB    1 
ATOM   15739 C  CG    . LEU   F 2  225 ? 5.024   53.021  22.863  1.00 21.66  ? 227 LEU   B CG    1 
ATOM   15740 C  CD1   . LEU   F 2  225 ? 3.583   52.777  22.469  1.00 16.19  ? 227 LEU   B CD1   1 
ATOM   15741 C  CD2   . LEU   F 2  225 ? 5.969   51.972  22.322  1.00 20.39  ? 227 LEU   B CD2   1 
ATOM   15742 N  N     . ASN   F 2  226 ? 6.101   57.192  21.896  1.00 23.31  ? 228 ASN   B N     1 
ATOM   15743 C  CA    . ASN   F 2  226 ? 7.016   58.315  21.927  1.00 21.36  ? 228 ASN   B CA    1 
ATOM   15744 C  C     . ASN   F 2  226 ? 6.349   59.556  22.463  1.00 26.69  ? 228 ASN   B C     1 
ATOM   15745 O  O     . ASN   F 2  226 ? 7.049   60.508  22.819  1.00 35.94  ? 228 ASN   B O     1 
ATOM   15746 C  CB    . ASN   F 2  226 ? 7.570   58.596  20.527  1.00 19.52  ? 228 ASN   B CB    1 
ATOM   15747 C  CG    . ASN   F 2  226 ? 8.495   57.507  20.020  1.00 20.32  ? 228 ASN   B CG    1 
ATOM   15748 O  OD1   . ASN   F 2  226 ? 8.733   56.495  20.682  1.00 23.75  ? 228 ASN   B OD1   1 
ATOM   15749 N  ND2   . ASN   F 2  226 ? 9.013   57.709  18.827  1.00 23.20  ? 228 ASN   B ND2   1 
ATOM   15750 N  N     . HIS   F 2  227 ? 5.016   59.583  22.506  1.00 20.13  ? 229 HIS   B N     1 
ATOM   15751 C  CA    . HIS   F 2  227 ? 4.339   60.711  23.130  1.00 23.49  ? 229 HIS   B CA    1 
ATOM   15752 C  C     . HIS   F 2  227 ? 4.533   60.685  24.645  1.00 29.54  ? 229 HIS   B C     1 
ATOM   15753 O  O     . HIS   F 2  227 ? 4.801   61.723  25.264  1.00 27.35  ? 229 HIS   B O     1 
ATOM   15754 C  CB    . HIS   F 2  227 ? 2.859   60.691  22.763  1.00 27.98  ? 229 HIS   B CB    1 
ATOM   15755 C  CG    . HIS   F 2  227 ? 2.041   61.712  23.488  1.00 29.34  ? 229 HIS   B CG    1 
ATOM   15756 N  ND1   . HIS   F 2  227 ? 1.985   63.032  23.102  1.00 25.48  ? 229 HIS   B ND1   1 
ATOM   15757 C  CD2   . HIS   F 2  227 ? 1.238   61.602  24.574  1.00 29.51  ? 229 HIS   B CD2   1 
ATOM   15758 C  CE1   . HIS   F 2  227 ? 1.186   63.693  23.923  1.00 27.52  ? 229 HIS   B CE1   1 
ATOM   15759 N  NE2   . HIS   F 2  227 ? 0.716   62.848  24.822  1.00 25.64  ? 229 HIS   B NE2   1 
ATOM   15760 N  N     . LEU   F 2  228 ? 4.407   59.498  25.254  1.00 32.28  ? 230 LEU   B N     1 
ATOM   15761 C  CA    . LEU   F 2  228 ? 4.769   59.315  26.658  1.00 28.91  ? 230 LEU   B CA    1 
ATOM   15762 C  C     . LEU   F 2  228 ? 6.268   59.545  26.890  1.00 26.71  ? 230 LEU   B C     1 
ATOM   15763 O  O     . LEU   F 2  228 ? 6.669   60.139  27.897  1.00 20.08  ? 230 LEU   B O     1 
ATOM   15764 C  CB    . LEU   F 2  228 ? 4.354   57.911  27.111  1.00 22.39  ? 230 LEU   B CB    1 
ATOM   15765 C  CG    . LEU   F 2  228 ? 2.864   57.590  26.984  1.00 16.53  ? 230 LEU   B CG    1 
ATOM   15766 C  CD1   . LEU   F 2  228 ? 2.453   56.241  27.609  1.00 13.18  ? 230 LEU   B CD1   1 
ATOM   15767 C  CD2   . LEU   F 2  228 ? 2.089   58.695  27.577  1.00 19.34  ? 230 LEU   B CD2   1 
ATOM   15768 N  N     . VAL   F 2  229 ? 7.113   59.092  25.965  1.00 27.27  ? 231 VAL   B N     1 
ATOM   15769 C  CA    . VAL   F 2  229 ? 8.543   59.279  26.157  1.00 24.12  ? 231 VAL   B CA    1 
ATOM   15770 C  C     . VAL   F 2  229 ? 8.920   60.738  26.003  1.00 22.66  ? 231 VAL   B C     1 
ATOM   15771 O  O     . VAL   F 2  229 ? 9.904   61.191  26.580  1.00 29.99  ? 231 VAL   B O     1 
ATOM   15772 C  CB    . VAL   F 2  229 ? 9.318   58.378  25.191  1.00 21.17  ? 231 VAL   B CB    1 
ATOM   15773 C  CG1   . VAL   F 2  229 ? 10.799  58.636  25.311  1.00 20.45  ? 231 VAL   B CG1   1 
ATOM   15774 C  CG2   . VAL   F 2  229 ? 9.014   56.928  25.511  1.00 18.27  ? 231 VAL   B CG2   1 
ATOM   15775 N  N     . SER   F 2  230 ? 8.139   61.503  25.259  1.00 26.23  ? 232 SER   B N     1 
ATOM   15776 C  CA    . SER   F 2  230 ? 8.416   62.926  25.098  1.00 21.02  ? 232 SER   B CA    1 
ATOM   15777 C  C     . SER   F 2  230 ? 8.146   63.695  26.386  1.00 27.08  ? 232 SER   B C     1 
ATOM   15778 O  O     . SER   F 2  230 ? 9.008   64.430  26.882  1.00 28.21  ? 232 SER   B O     1 
ATOM   15779 C  CB    . SER   F 2  230 ? 7.568   63.485  23.960  1.00 21.39  ? 232 SER   B CB    1 
ATOM   15780 O  OG    . SER   F 2  230 ? 8.226   64.574  23.365  1.00 39.35  ? 232 SER   B OG    1 
ATOM   15781 N  N     . ALA   F 2  231 ? 6.936   63.554  26.932  1.00 25.44  ? 233 ALA   B N     1 
ATOM   15782 C  CA    . ALA   F 2  231 ? 6.567   64.245  28.158  1.00 20.00  ? 233 ALA   B CA    1 
ATOM   15783 C  C     . ALA   F 2  231 ? 7.509   63.904  29.312  1.00 24.76  ? 233 ALA   B C     1 
ATOM   15784 O  O     . ALA   F 2  231 ? 7.927   64.788  30.070  1.00 28.63  ? 233 ALA   B O     1 
ATOM   15785 C  CB    . ALA   F 2  231 ? 5.128   63.895  28.519  1.00 26.71  ? 233 ALA   B CB    1 
ATOM   15786 N  N     . THR   F 2  232 ? 7.834   62.621  29.475  1.00 20.24  ? 234 THR   B N     1 
ATOM   15787 C  CA    . THR   F 2  232 ? 8.766   62.205  30.519  1.00 18.08  ? 234 THR   B CA    1 
ATOM   15788 C  C     . THR   F 2  232 ? 10.109  62.919  30.369  1.00 22.11  ? 234 THR   B C     1 
ATOM   15789 O  O     . THR   F 2  232 ? 10.657  63.450  31.339  1.00 21.36  ? 234 THR   B O     1 
ATOM   15790 C  CB    . THR   F 2  232 ? 8.916   60.680  30.468  1.00 17.61  ? 234 THR   B CB    1 
ATOM   15791 O  OG1   . THR   F 2  232 ? 7.633   60.090  30.718  1.00 17.89  ? 234 THR   B OG1   1 
ATOM   15792 C  CG2   . THR   F 2  232 ? 9.936   60.130  31.483  1.00 11.53  ? 234 THR   B CG2   1 
ATOM   15793 N  N     . MET   F 2  233 ? 10.637  62.969  29.147  1.00 23.88  ? 235 MET   B N     1 
ATOM   15794 C  CA    . MET   F 2  233 ? 11.945  63.565  28.927  1.00 17.94  ? 235 MET   B CA    1 
ATOM   15795 C  C     . MET   F 2  233 ? 11.935  65.027  29.292  1.00 19.06  ? 235 MET   B C     1 
ATOM   15796 O  O     . MET   F 2  233 ? 12.854  65.525  29.946  1.00 21.76  ? 235 MET   B O     1 
ATOM   15797 C  CB    . MET   F 2  233 ? 12.363  63.383  27.475  1.00 16.12  ? 235 MET   B CB    1 
ATOM   15798 C  CG    . MET   F 2  233 ? 12.738  61.952  27.159  1.00 25.63  ? 235 MET   B CG    1 
ATOM   15799 S  SD    . MET   F 2  233 ? 13.714  61.807  25.679  1.00 27.48  ? 235 MET   B SD    1 
ATOM   15800 C  CE    . MET   F 2  233 ? 12.442  62.252  24.452  1.00 27.65  ? 235 MET   B CE    1 
ATOM   15801 N  N     . SER   F 2  234 ? 10.912  65.739  28.856  1.00 28.37  ? 236 SER   B N     1 
ATOM   15802 C  CA    . SER   F 2  234 ? 10.766  67.123  29.274  1.00 25.20  ? 236 SER   B CA    1 
ATOM   15803 C  C     . SER   F 2  234 ? 10.699  67.210  30.789  1.00 24.09  ? 236 SER   B C     1 
ATOM   15804 O  O     . SER   F 2  234 ? 11.411  68.012  31.405  1.00 23.57  ? 236 SER   B O     1 
ATOM   15805 C  CB    . SER   F 2  234 ? 9.518   67.722  28.631  1.00 24.47  ? 236 SER   B CB    1 
ATOM   15806 O  OG    . SER   F 2  234 ? 9.378   69.077  28.982  1.00 34.62  ? 236 SER   B OG    1 
ATOM   15807 N  N     . GLY   F 2  235 ? 9.886   66.355  31.409  1.00 22.42  ? 237 GLY   B N     1 
ATOM   15808 C  CA    . GLY   F 2  235 ? 9.756   66.333  32.857  1.00 22.93  ? 237 GLY   B CA    1 
ATOM   15809 C  C     . GLY   F 2  235 ? 11.067  66.253  33.617  1.00 24.05  ? 237 GLY   B C     1 
ATOM   15810 O  O     . GLY   F 2  235 ? 11.423  67.158  34.376  1.00 24.82  ? 237 GLY   B O     1 
ATOM   15811 N  N     . VAL   F 2  236 ? 11.807  65.167  33.403  1.00 23.48  ? 238 VAL   B N     1 
ATOM   15812 C  CA    . VAL   F 2  236 ? 13.013  64.915  34.174  1.00 22.22  ? 238 VAL   B CA    1 
ATOM   15813 C  C     . VAL   F 2  236 ? 14.152  65.867  33.840  1.00 23.37  ? 238 VAL   B C     1 
ATOM   15814 O  O     . VAL   F 2  236 ? 15.177  65.851  34.530  1.00 24.16  ? 238 VAL   B O     1 
ATOM   15815 C  CB    . VAL   F 2  236 ? 13.428  63.447  33.959  1.00 26.57  ? 238 VAL   B CB    1 
ATOM   15816 C  CG1   . VAL   F 2  236 ? 12.180  62.600  33.707  1.00 22.14  ? 238 VAL   B CG1   1 
ATOM   15817 C  CG2   . VAL   F 2  236 ? 14.419  63.331  32.810  1.00 21.94  ? 238 VAL   B CG2   1 
ATOM   15818 N  N     . THR   F 2  237 ? 14.017  66.685  32.798  1.00 25.15  ? 239 THR   B N     1 
ATOM   15819 C  CA    . THR   F 2  237 ? 15.047  67.659  32.455  1.00 22.20  ? 239 THR   B CA    1 
ATOM   15820 C  C     . THR   F 2  237 ? 14.640  69.083  32.785  1.00 25.88  ? 239 THR   B C     1 
ATOM   15821 O  O     . THR   F 2  237 ? 15.395  70.000  32.448  1.00 27.37  ? 239 THR   B O     1 
ATOM   15822 C  CB    . THR   F 2  237 ? 15.419  67.585  30.961  1.00 18.52  ? 239 THR   B CB    1 
ATOM   15823 O  OG1   . THR   F 2  237 ? 14.247  67.769  30.169  1.00 25.09  ? 239 THR   B OG1   1 
ATOM   15824 C  CG2   . THR   F 2  237 ? 16.054  66.251  30.600  1.00 20.59  ? 239 THR   B CG2   1 
ATOM   15825 N  N     . THR   F 2  238 ? 13.458  69.299  33.390  1.00 24.11  ? 240 THR   B N     1 
ATOM   15826 C  CA    . THR   F 2  238 ? 13.043  70.654  33.754  1.00 18.75  ? 240 THR   B CA    1 
ATOM   15827 C  C     . THR   F 2  238 ? 14.099  71.312  34.622  1.00 20.04  ? 240 THR   B C     1 
ATOM   15828 O  O     . THR   F 2  238 ? 14.511  72.445  34.361  1.00 21.38  ? 240 THR   B O     1 
ATOM   15829 C  CB    . THR   F 2  238 ? 11.689  70.647  34.481  1.00 22.97  ? 240 THR   B CB    1 
ATOM   15830 O  OG1   . THR   F 2  238 ? 10.704  69.989  33.687  1.00 28.69  ? 240 THR   B OG1   1 
ATOM   15831 C  CG2   . THR   F 2  238 ? 11.194  72.029  34.702  1.00 23.28  ? 240 THR   B CG2   1 
ATOM   15832 N  N     . CYS   F 2  239 ? 14.591  70.582  35.628  1.00 22.92  ? 241 CYS   B N     1 
ATOM   15833 C  CA    . CYS   F 2  239 ? 15.541  71.115  36.593  1.00 17.82  ? 241 CYS   B CA    1 
ATOM   15834 C  C     . CYS   F 2  239 ? 16.880  71.486  35.975  1.00 25.63  ? 241 CYS   B C     1 
ATOM   15835 O  O     . CYS   F 2  239 ? 17.670  72.199  36.607  1.00 31.09  ? 241 CYS   B O     1 
ATOM   15836 C  CB    . CYS   F 2  239 ? 15.768  70.102  37.701  1.00 20.07  ? 241 CYS   B CB    1 
ATOM   15837 S  SG    . CYS   F 2  239 ? 14.375  69.890  38.753  1.00 41.69  ? 241 CYS   B SG    1 
ATOM   15838 N  N     . LEU   F 2  240 ? 17.183  71.002  34.782  1.00 31.20  ? 242 LEU   B N     1 
ATOM   15839 C  CA    . LEU   F 2  240 ? 18.387  71.467  34.113  1.00 29.36  ? 242 LEU   B CA    1 
ATOM   15840 C  C     . LEU   F 2  240 ? 18.149  72.724  33.280  1.00 27.51  ? 242 LEU   B C     1 
ATOM   15841 O  O     . LEU   F 2  240 ? 19.104  73.461  33.001  1.00 31.85  ? 242 LEU   B O     1 
ATOM   15842 C  CB    . LEU   F 2  240 ? 18.960  70.348  33.230  1.00 19.65  ? 242 LEU   B CB    1 
ATOM   15843 C  CG    . LEU   F 2  240 ? 19.000  68.948  33.855  1.00 22.44  ? 242 LEU   B CG    1 
ATOM   15844 C  CD1   . LEU   F 2  240 ? 19.693  67.963  32.931  1.00 24.20  ? 242 LEU   B CD1   1 
ATOM   15845 C  CD2   . LEU   F 2  240 ? 19.690  68.940  35.206  1.00 24.08  ? 242 LEU   B CD2   1 
ATOM   15846 N  N     . ARG   F 2  241 ? 16.904  73.011  32.905  1.00 21.78  ? 243 ARG   B N     1 
ATOM   15847 C  CA    . ARG   F 2  241 ? 16.648  73.956  31.826  1.00 31.15  ? 243 ARG   B CA    1 
ATOM   15848 C  C     . ARG   F 2  241 ? 16.025  75.262  32.282  1.00 31.05  ? 243 ARG   B C     1 
ATOM   15849 O  O     . ARG   F 2  241 ? 16.082  76.248  31.541  1.00 38.13  ? 243 ARG   B O     1 
ATOM   15850 C  CB    . ARG   F 2  241 ? 15.744  73.305  30.760  1.00 32.25  ? 243 ARG   B CB    1 
ATOM   15851 C  CG    . ARG   F 2  241 ? 16.197  71.886  30.414  1.00 21.23  ? 243 ARG   B CG    1 
ATOM   15852 C  CD    . ARG   F 2  241 ? 15.500  71.358  29.205  1.00 27.93  ? 243 ARG   B CD    1 
ATOM   15853 N  NE    . ARG   F 2  241 ? 14.170  70.840  29.498  1.00 28.32  ? 243 ARG   B NE    1 
ATOM   15854 C  CZ    . ARG   F 2  241 ? 13.037  71.472  29.232  1.00 24.88  ? 243 ARG   B CZ    1 
ATOM   15855 N  NH1   . ARG   F 2  241 ? 13.026  72.665  28.658  1.00 28.28  ? 243 ARG   B NH1   1 
ATOM   15856 N  NH2   . ARG   F 2  241 ? 11.887  70.897  29.559  1.00 25.90  ? 243 ARG   B NH2   1 
ATOM   15857 N  N     . PHE   F 2  242 ? 15.435  75.292  33.466  1.00 34.02  ? 244 PHE   B N     1 
ATOM   15858 C  CA    . PHE   F 2  242 ? 14.941  76.530  34.034  1.00 27.71  ? 244 PHE   B CA    1 
ATOM   15859 C  C     . PHE   F 2  242 ? 15.664  76.806  35.346  1.00 35.57  ? 244 PHE   B C     1 
ATOM   15860 O  O     . PHE   F 2  242 ? 16.373  75.929  35.865  1.00 26.33  ? 244 PHE   B O     1 
ATOM   15861 C  CB    . PHE   F 2  242 ? 13.437  76.441  34.231  1.00 28.00  ? 244 PHE   B CB    1 
ATOM   15862 C  CG    . PHE   F 2  242 ? 12.688  76.223  32.960  1.00 36.46  ? 244 PHE   B CG    1 
ATOM   15863 C  CD1   . PHE   F 2  242 ? 12.425  77.279  32.107  1.00 42.68  ? 244 PHE   B CD1   1 
ATOM   15864 C  CD2   . PHE   F 2  242 ? 12.246  74.965  32.610  1.00 33.51  ? 244 PHE   B CD2   1 
ATOM   15865 C  CE1   . PHE   F 2  242 ? 11.733  77.080  30.921  1.00 39.17  ? 244 PHE   B CE1   1 
ATOM   15866 C  CE2   . PHE   F 2  242 ? 11.558  74.769  31.443  1.00 31.58  ? 244 PHE   B CE2   1 
ATOM   15867 C  CZ    . PHE   F 2  242 ? 11.305  75.823  30.593  1.00 35.30  ? 244 PHE   B CZ    1 
ATOM   15868 N  N     . PRO   F 2  243 ? 15.501  78.005  35.912  1.00 40.02  ? 245 PRO   B N     1 
ATOM   15869 C  CA    . PRO   F 2  243 ? 16.221  78.346  37.144  1.00 26.70  ? 245 PRO   B CA    1 
ATOM   15870 C  C     . PRO   F 2  243 ? 15.678  77.573  38.331  1.00 28.76  ? 245 PRO   B C     1 
ATOM   15871 O  O     . PRO   F 2  243 ? 14.475  77.341  38.443  1.00 33.54  ? 245 PRO   B O     1 
ATOM   15872 C  CB    . PRO   F 2  243 ? 15.974  79.849  37.292  1.00 32.12  ? 245 PRO   B CB    1 
ATOM   15873 C  CG    . PRO   F 2  243 ? 15.477  80.303  35.930  1.00 42.61  ? 245 PRO   B CG    1 
ATOM   15874 C  CD    . PRO   F 2  243 ? 14.721  79.141  35.398  1.00 35.09  ? 245 PRO   B CD    1 
ATOM   15875 N  N     . GLY   F 2  244 ? 16.577  77.160  39.219  1.00 30.29  ? 246 GLY   B N     1 
ATOM   15876 C  CA    . GLY   F 2  244 ? 16.139  76.416  40.383  1.00 23.79  ? 246 GLY   B CA    1 
ATOM   15877 C  C     . GLY   F 2  244 ? 17.289  75.983  41.272  1.00 41.43  ? 246 GLY   B C     1 
ATOM   15878 O  O     . GLY   F 2  244 ? 18.474  76.234  41.004  1.00 30.22  ? 246 GLY   B O     1 
ATOM   15879 N  N     . GLN   F 2  245 ? 16.892  75.305  42.342  1.00 44.81  ? 247 GLN   B N     1 
ATOM   15880 C  CA    . GLN   F 2  245 ? 17.690  74.889  43.480  1.00 35.64  ? 247 GLN   B CA    1 
ATOM   15881 C  C     . GLN   F 2  245 ? 18.170  73.463  43.351  1.00 34.47  ? 247 GLN   B C     1 
ATOM   15882 O  O     . GLN   F 2  245 ? 19.330  73.154  43.633  1.00 46.73  ? 247 GLN   B O     1 
ATOM   15883 C  CB    . GLN   F 2  245 ? 16.833  74.984  44.740  1.00 43.74  ? 247 GLN   B CB    1 
ATOM   15884 C  CG    . GLN   F 2  245 ? 16.572  76.374  45.161  1.00 43.18  ? 247 GLN   B CG    1 
ATOM   15885 C  CD    . GLN   F 2  245 ? 17.803  76.925  45.785  1.00 48.16  ? 247 GLN   B CD    1 
ATOM   15886 O  OE1   . GLN   F 2  245 ? 18.225  76.451  46.847  1.00 48.37  ? 247 GLN   B OE1   1 
ATOM   15887 N  NE2   . GLN   F 2  245 ? 18.437  77.884  45.113  1.00 40.63  ? 247 GLN   B NE2   1 
ATOM   15888 N  N     . LEU   F 2  246 ? 17.266  72.591  42.956  1.00 32.39  ? 248 LEU   B N     1 
ATOM   15889 C  CA    . LEU   F 2  246 ? 17.390  71.172  43.190  1.00 31.36  ? 248 LEU   B CA    1 
ATOM   15890 C  C     . LEU   F 2  246 ? 17.742  70.460  41.900  1.00 32.02  ? 248 LEU   B C     1 
ATOM   15891 O  O     . LEU   F 2  246 ? 17.176  70.744  40.845  1.00 32.76  ? 248 LEU   B O     1 
ATOM   15892 C  CB    . LEU   F 2  246 ? 16.085  70.622  43.749  1.00 24.03  ? 248 LEU   B CB    1 
ATOM   15893 C  CG    . LEU   F 2  246 ? 15.963  69.107  43.836  1.00 28.33  ? 248 LEU   B CG    1 
ATOM   15894 C  CD1   . LEU   F 2  246 ? 16.554  68.561  45.140  1.00 31.75  ? 248 LEU   B CD1   1 
ATOM   15895 C  CD2   . LEU   F 2  246 ? 14.506  68.693  43.653  1.00 38.81  ? 248 LEU   B CD2   1 
ATOM   15896 N  N     . ASN   F 2  247 ? 18.674  69.525  41.993  1.00 32.76  ? 249 ASN   B N     1 
ATOM   15897 C  CA    . ASN   F 2  247 ? 18.975  68.658  40.878  1.00 23.42  ? 249 ASN   B CA    1 
ATOM   15898 C  C     . ASN   F 2  247 ? 19.135  69.478  39.604  1.00 24.36  ? 249 ASN   B C     1 
ATOM   15899 O  O     . ASN   F 2  247 ? 18.600  69.138  38.549  1.00 28.50  ? 249 ASN   B O     1 
ATOM   15900 C  CB    . ASN   F 2  247 ? 17.879  67.613  40.715  1.00 22.87  ? 249 ASN   B CB    1 
ATOM   15901 C  CG    . ASN   F 2  247 ? 17.773  66.713  41.887  1.00 22.88  ? 249 ASN   B CG    1 
ATOM   15902 O  OD1   . ASN   F 2  247 ? 18.716  66.583  42.651  1.00 27.70  ? 249 ASN   B OD1   1 
ATOM   15903 N  ND2   . ASN   F 2  247 ? 16.634  66.064  42.043  1.00 31.44  ? 249 ASN   B ND2   1 
ATOM   15904 N  N     . ALA   F 2  248 ? 19.862  70.585  39.702  1.00 20.95  ? 250 ALA   B N     1 
ATOM   15905 C  CA    . ALA   F 2  248 ? 19.863  71.521  38.587  1.00 25.74  ? 250 ALA   B CA    1 
ATOM   15906 C  C     . ALA   F 2  248 ? 21.015  71.304  37.622  1.00 25.63  ? 250 ALA   B C     1 
ATOM   15907 O  O     . ALA   F 2  248 ? 21.112  72.039  36.631  1.00 26.61  ? 250 ALA   B O     1 
ATOM   15908 C  CB    . ALA   F 2  248 ? 19.878  72.965  39.091  1.00 27.62  ? 250 ALA   B CB    1 
ATOM   15909 N  N     . ASP   F 2  249 ? 21.892  70.338  37.901  1.00 21.22  ? 251 ASP   B N     1 
ATOM   15910 C  CA    . ASP   F 2  249 ? 22.919  69.900  36.971  1.00 22.37  ? 251 ASP   B CA    1 
ATOM   15911 C  C     . ASP   F 2  249 ? 23.052  68.386  37.086  1.00 27.87  ? 251 ASP   B C     1 
ATOM   15912 O  O     . ASP   F 2  249 ? 22.577  67.768  38.045  1.00 22.39  ? 251 ASP   B O     1 
ATOM   15913 C  CB    . ASP   F 2  249 ? 24.257  70.587  37.242  1.00 17.67  ? 251 ASP   B CB    1 
ATOM   15914 C  CG    . ASP   F 2  249 ? 24.918  70.075  38.495  1.00 26.06  ? 251 ASP   B CG    1 
ATOM   15915 O  OD1   . ASP   F 2  249 ? 25.382  68.911  38.479  1.00 27.85  ? 251 ASP   B OD1   1 
ATOM   15916 O  OD2   . ASP   F 2  249 ? 24.962  70.820  39.507  1.00 28.81  ? 251 ASP   B OD2   1 
ATOM   15917 N  N     . LEU   F 2  250 ? 23.731  67.786  36.101  1.00 26.35  ? 252 LEU   B N     1 
ATOM   15918 C  CA    . LEU   F 2  250 ? 23.803  66.330  36.058  1.00 22.96  ? 252 LEU   B CA    1 
ATOM   15919 C  C     . LEU   F 2  250 ? 24.573  65.746  37.253  1.00 24.66  ? 252 LEU   B C     1 
ATOM   15920 O  O     . LEU   F 2  250 ? 24.229  64.666  37.734  1.00 21.61  ? 252 LEU   B O     1 
ATOM   15921 C  CB    . LEU   F 2  250 ? 24.403  65.900  34.718  1.00 23.81  ? 252 LEU   B CB    1 
ATOM   15922 C  CG    . LEU   F 2  250 ? 23.480  66.190  33.537  1.00 22.26  ? 252 LEU   B CG    1 
ATOM   15923 C  CD1   . LEU   F 2  250 ? 24.242  66.195  32.224  1.00 16.61  ? 252 LEU   B CD1   1 
ATOM   15924 C  CD2   . LEU   F 2  250 ? 22.337  65.189  33.523  1.00 19.05  ? 252 LEU   B CD2   1 
ATOM   15925 N  N     . ARG   F 2  251 ? 25.603  66.428  37.760  1.00 22.60  ? 253 ARG   B N     1 
ATOM   15926 C  CA    . ARG   F 2  251 ? 26.298  65.891  38.922  1.00 19.27  ? 253 ARG   B CA    1 
ATOM   15927 C  C     . ARG   F 2  251 ? 25.407  65.940  40.149  1.00 24.16  ? 253 ARG   B C     1 
ATOM   15928 O  O     . ARG   F 2  251 ? 25.171  64.920  40.807  1.00 25.16  ? 253 ARG   B O     1 
ATOM   15929 C  CB    . ARG   F 2  251 ? 27.599  66.645  39.189  1.00 20.90  ? 253 ARG   B CB    1 
ATOM   15930 C  CG    . ARG   F 2  251 ? 28.586  65.823  39.997  1.00 17.41  ? 253 ARG   B CG    1 
ATOM   15931 C  CD    . ARG   F 2  251 ? 29.910  66.481  40.032  1.00 19.88  ? 253 ARG   B CD    1 
ATOM   15932 N  NE    . ARG   F 2  251 ? 30.366  66.743  38.681  1.00 23.87  ? 253 ARG   B NE    1 
ATOM   15933 C  CZ    . ARG   F 2  251 ? 30.895  65.813  37.901  1.00 34.94  ? 253 ARG   B CZ    1 
ATOM   15934 N  NH1   . ARG   F 2  251 ? 31.068  64.569  38.332  1.00 30.56  ? 253 ARG   B NH1   1 
ATOM   15935 N  NH2   . ARG   F 2  251 ? 31.256  66.137  36.660  1.00 33.28  ? 253 ARG   B NH2   1 
ATOM   15936 N  N     . LYS   F 2  252 ? 24.890  67.128  40.464  1.00 23.51  ? 254 LYS   B N     1 
ATOM   15937 C  CA    . LYS   F 2  252 ? 24.052  67.282  41.647  1.00 23.62  ? 254 LYS   B CA    1 
ATOM   15938 C  C     . LYS   F 2  252 ? 22.861  66.327  41.632  1.00 26.72  ? 254 LYS   B C     1 
ATOM   15939 O  O     . LYS   F 2  252 ? 22.482  65.792  42.688  1.00 29.70  ? 254 LYS   B O     1 
ATOM   15940 C  CB    . LYS   F 2  252 ? 23.610  68.742  41.791  1.00 17.23  ? 254 LYS   B CB    1 
ATOM   15941 C  CG    . LYS   F 2  252 ? 24.601  69.498  42.683  1.00 27.15  ? 254 LYS   B CG    1 
ATOM   15942 C  CD    . LYS   F 2  252 ? 24.459  70.998  42.615  1.00 30.73  ? 254 LYS   B CD    1 
ATOM   15943 C  CE    . LYS   F 2  252 ? 24.883  71.673  43.934  1.00 21.00  ? 254 LYS   B CE    1 
ATOM   15944 N  NZ    . LYS   F 2  252 ? 24.654  73.143  43.788  1.00 27.48  ? 254 LYS   B NZ    1 
ATOM   15945 N  N     . LEU   F 2  253 ? 22.282  66.068  40.456  1.00 21.05  ? 255 LEU   B N     1 
ATOM   15946 C  CA    . LEU   F 2  253 ? 21.277  65.017  40.362  1.00 19.60  ? 255 LEU   B CA    1 
ATOM   15947 C  C     . LEU   F 2  253 ? 21.852  63.680  40.805  1.00 22.02  ? 255 LEU   B C     1 
ATOM   15948 O  O     . LEU   F 2  253 ? 21.281  63.000  41.667  1.00 22.91  ? 255 LEU   B O     1 
ATOM   15949 C  CB    . LEU   F 2  253 ? 20.738  64.927  38.939  1.00 25.94  ? 255 LEU   B CB    1 
ATOM   15950 C  CG    . LEU   F 2  253 ? 19.851  63.731  38.574  1.00 25.67  ? 255 LEU   B CG    1 
ATOM   15951 C  CD1   . LEU   F 2  253 ? 18.528  63.721  39.349  1.00 18.63  ? 255 LEU   B CD1   1 
ATOM   15952 C  CD2   . LEU   F 2  253 ? 19.617  63.706  37.063  1.00 19.57  ? 255 LEU   B CD2   1 
ATOM   15953 N  N     . ALA   F 2  254 ? 23.013  63.303  40.260  1.00 24.75  ? 256 ALA   B N     1 
ATOM   15954 C  CA    . ALA   F 2  254 ? 23.563  61.983  40.557  1.00 22.24  ? 256 ALA   B CA    1 
ATOM   15955 C  C     . ALA   F 2  254 ? 23.870  61.837  42.034  1.00 20.58  ? 256 ALA   B C     1 
ATOM   15956 O  O     . ALA   F 2  254 ? 23.597  60.792  42.628  1.00 21.17  ? 256 ALA   B O     1 
ATOM   15957 C  CB    . ALA   F 2  254 ? 24.813  61.704  39.727  1.00 18.31  ? 256 ALA   B CB    1 
ATOM   15958 N  N     . VAL   F 2  255 ? 24.433  62.876  42.653  1.00 22.13  ? 257 VAL   B N     1 
ATOM   15959 C  CA    . VAL   F 2  255 ? 24.780  62.764  44.061  1.00 19.63  ? 257 VAL   B CA    1 
ATOM   15960 C  C     . VAL   F 2  255 ? 23.541  62.589  44.925  1.00 26.46  ? 257 VAL   B C     1 
ATOM   15961 O  O     . VAL   F 2  255 ? 23.653  62.145  46.077  1.00 21.63  ? 257 VAL   B O     1 
ATOM   15962 C  CB    . VAL   F 2  255 ? 25.565  63.990  44.540  1.00 17.85  ? 257 VAL   B CB    1 
ATOM   15963 C  CG1   . VAL   F 2  255 ? 26.001  63.776  45.964  1.00 18.10  ? 257 VAL   B CG1   1 
ATOM   15964 C  CG2   . VAL   F 2  255 ? 26.739  64.230  43.651  1.00 18.39  ? 257 VAL   B CG2   1 
ATOM   15965 N  N     . ASN   F 2  256 ? 22.355  62.924  44.386  1.00 30.41  ? 258 ASN   B N     1 
ATOM   15966 C  CA    . ASN   F 2  256 ? 21.082  62.868  45.105  1.00 22.34  ? 258 ASN   B CA    1 
ATOM   15967 C  C     . ASN   F 2  256 ? 20.328  61.573  44.844  1.00 19.69  ? 258 ASN   B C     1 
ATOM   15968 O  O     . ASN   F 2  256 ? 19.564  61.118  45.701  1.00 20.77  ? 258 ASN   B O     1 
ATOM   15969 C  CB    . ASN   F 2  256 ? 20.202  64.062  44.706  1.00 20.40  ? 258 ASN   B CB    1 
ATOM   15970 C  CG    . ASN   F 2  256 ? 20.308  65.230  45.680  1.00 24.72  ? 258 ASN   B CG    1 
ATOM   15971 O  OD1   . ASN   F 2  256 ? 21.002  65.149  46.682  1.00 28.79  ? 258 ASN   B OD1   1 
ATOM   15972 N  ND2   . ASN   F 2  256 ? 19.607  66.318  45.388  1.00 27.03  ? 258 ASN   B ND2   1 
ATOM   15973 N  N     . MET   F 2  257 ? 20.550  60.955  43.687  1.00 19.63  ? 259 MET   B N     1 
ATOM   15974 C  CA    . MET   F 2  257 ? 19.831  59.763  43.280  1.00 17.08  ? 259 MET   B CA    1 
ATOM   15975 C  C     . MET   F 2  257 ? 20.639  58.468  43.407  1.00 21.92  ? 259 MET   B C     1 
ATOM   15976 O  O     . MET   F 2  257 ? 20.038  57.393  43.522  1.00 24.04  ? 259 MET   B O     1 
ATOM   15977 C  CB    . MET   F 2  257 ? 19.375  59.925  41.832  1.00 22.62  ? 259 MET   B CB    1 
ATOM   15978 C  CG    . MET   F 2  257 ? 18.439  61.105  41.608  1.00 26.19  ? 259 MET   B CG    1 
ATOM   15979 S  SD    . MET   F 2  257 ? 16.918  60.968  42.560  1.00 22.82  ? 259 MET   B SD    1 
ATOM   15980 C  CE    . MET   F 2  257 ? 16.183  59.507  41.883  1.00 23.15  ? 259 MET   B CE    1 
ATOM   15981 N  N     . VAL   F 2  258 ? 21.969  58.522  43.398  1.00 18.29  ? 260 VAL   B N     1 
ATOM   15982 C  CA    . VAL   F 2  258 ? 22.764  57.299  43.281  1.00 20.71  ? 260 VAL   B CA    1 
ATOM   15983 C  C     . VAL   F 2  258 ? 23.511  57.007  44.579  1.00 27.14  ? 260 VAL   B C     1 
ATOM   15984 O  O     . VAL   F 2  258 ? 24.631  57.507  44.774  1.00 27.06  ? 260 VAL   B O     1 
ATOM   15985 C  CB    . VAL   F 2  258 ? 23.741  57.386  42.091  1.00 19.08  ? 260 VAL   B CB    1 
ATOM   15986 C  CG1   . VAL   F 2  258 ? 24.548  56.076  41.938  1.00 16.52  ? 260 VAL   B CG1   1 
ATOM   15987 C  CG2   . VAL   F 2  258 ? 22.976  57.731  40.805  1.00 17.11  ? 260 VAL   B CG2   1 
ATOM   15988 N  N     . PRO   F 2  259 ? 22.952  56.199  45.486  1.00 20.58  ? 261 PRO   B N     1 
ATOM   15989 C  CA    . PRO   F 2  259 ? 23.659  55.925  46.744  1.00 21.34  ? 261 PRO   B CA    1 
ATOM   15990 C  C     . PRO   F 2  259 ? 24.754  54.877  46.608  1.00 26.25  ? 261 PRO   B C     1 
ATOM   15991 O  O     . PRO   F 2  259 ? 25.638  54.802  47.484  1.00 25.20  ? 261 PRO   B O     1 
ATOM   15992 C  CB    . PRO   F 2  259 ? 22.538  55.458  47.677  1.00 17.09  ? 261 PRO   B CB    1 
ATOM   15993 C  CG    . PRO   F 2  259 ? 21.586  54.823  46.771  1.00 21.47  ? 261 PRO   B CG    1 
ATOM   15994 C  CD    . PRO   F 2  259 ? 21.608  55.616  45.477  1.00 19.52  ? 261 PRO   B CD    1 
ATOM   15995 N  N     . PHE   F 2  260 ? 24.722  54.074  45.543  1.00 19.62  ? 262 PHE   B N     1 
ATOM   15996 C  CA    . PHE   F 2  260 ? 25.794  53.157  45.201  1.00 21.36  ? 262 PHE   B CA    1 
ATOM   15997 C  C     . PHE   F 2  260 ? 26.021  53.177  43.691  1.00 21.69  ? 262 PHE   B C     1 
ATOM   15998 O  O     . PHE   F 2  260 ? 25.051  53.278  42.924  1.00 22.59  ? 262 PHE   B O     1 
ATOM   15999 C  CB    . PHE   F 2  260 ? 25.472  51.738  45.664  1.00 18.42  ? 262 PHE   B CB    1 
ATOM   16000 C  CG    . PHE   F 2  260 ? 25.005  51.655  47.057  1.00 15.17  ? 262 PHE   B CG    1 
ATOM   16001 C  CD1   . PHE   F 2  260 ? 25.906  51.605  48.112  1.00 21.26  ? 262 PHE   B CD1   1 
ATOM   16002 C  CD2   . PHE   F 2  260 ? 23.654  51.603  47.338  1.00 25.68  ? 262 PHE   B CD2   1 
ATOM   16003 C  CE1   . PHE   F 2  260 ? 25.460  51.511  49.473  1.00 20.02  ? 262 PHE   B CE1   1 
ATOM   16004 C  CE2   . PHE   F 2  260 ? 23.194  51.502  48.695  1.00 32.56  ? 262 PHE   B CE2   1 
ATOM   16005 C  CZ    . PHE   F 2  260 ? 24.107  51.452  49.756  1.00 17.60  ? 262 PHE   B CZ    1 
ATOM   16006 N  N     . PRO   F 2  261 ? 27.282  53.096  43.229  1.00 23.35  ? 263 PRO   B N     1 
ATOM   16007 C  CA    . PRO   F 2  261 ? 27.553  53.358  41.797  1.00 20.77  ? 263 PRO   B CA    1 
ATOM   16008 C  C     . PRO   F 2  261 ? 26.720  52.543  40.803  1.00 17.83  ? 263 PRO   B C     1 
ATOM   16009 O  O     . PRO   F 2  261 ? 26.181  53.102  39.840  1.00 13.52  ? 263 PRO   B O     1 
ATOM   16010 C  CB    . PRO   F 2  261 ? 29.056  53.063  41.685  1.00 10.11  ? 263 PRO   B CB    1 
ATOM   16011 C  CG    . PRO   F 2  261 ? 29.434  52.375  42.952  1.00 13.69  ? 263 PRO   B CG    1 
ATOM   16012 C  CD    . PRO   F 2  261 ? 28.538  52.926  43.982  1.00 18.50  ? 263 PRO   B CD    1 
ATOM   16013 N  N     . ARG   F 2  262 ? 26.574  51.241  41.019  1.00 17.60  ? 264 ARG   B N     1 
ATOM   16014 C  CA    . ARG   F 2  262 ? 25.861  50.436  40.028  1.00 22.19  ? 264 ARG   B CA    1 
ATOM   16015 C  C     . ARG   F 2  262 ? 24.352  50.708  40.029  1.00 18.50  ? 264 ARG   B C     1 
ATOM   16016 O  O     . ARG   F 2  262 ? 23.709  50.623  38.979  1.00 15.16  ? 264 ARG   B O     1 
ATOM   16017 C  CB    . ARG   F 2  262 ? 26.164  48.956  40.275  1.00 23.06  ? 264 ARG   B CB    1 
ATOM   16018 C  CG    . ARG   F 2  262 ? 27.650  48.724  40.271  1.00 19.02  ? 264 ARG   B CG    1 
ATOM   16019 C  CD    . ARG   F 2  262 ? 28.072  47.368  40.658  1.00 12.29  ? 264 ARG   B CD    1 
ATOM   16020 N  NE    . ARG   F 2  262 ? 27.964  46.458  39.539  1.00 22.48  ? 264 ARG   B NE    1 
ATOM   16021 C  CZ    . ARG   F 2  262 ? 27.183  45.388  39.524  1.00 29.12  ? 264 ARG   B CZ    1 
ATOM   16022 N  NH1   . ARG   F 2  262 ? 26.449  45.051  40.576  1.00 28.05  ? 264 ARG   B NH1   1 
ATOM   16023 N  NH2   . ARG   F 2  262 ? 27.155  44.622  38.438  1.00 25.10  ? 264 ARG   B NH2   1 
ATOM   16024 N  N     . LEU   F 2  263 ? 23.772  51.066  41.176  1.00 24.53  ? 265 LEU   B N     1 
ATOM   16025 C  CA    . LEU   F 2  263 ? 22.322  51.268  41.275  1.00 23.79  ? 265 LEU   B CA    1 
ATOM   16026 C  C     . LEU   F 2  263 ? 21.938  52.679  40.819  1.00 18.11  ? 265 LEU   B C     1 
ATOM   16027 O  O     . LEU   F 2  263 ? 21.469  53.513  41.590  1.00 21.80  ? 265 LEU   B O     1 
ATOM   16028 C  CB    . LEU   F 2  263 ? 21.853  50.998  42.695  1.00 22.27  ? 265 LEU   B CB    1 
ATOM   16029 C  CG    . LEU   F 2  263 ? 22.336  49.642  43.204  1.00 20.83  ? 265 LEU   B CG    1 
ATOM   16030 C  CD1   . LEU   F 2  263 ? 21.501  49.186  44.376  1.00 18.64  ? 265 LEU   B CD1   1 
ATOM   16031 C  CD2   . LEU   F 2  263 ? 22.235  48.671  42.083  1.00 21.87  ? 265 LEU   B CD2   1 
ATOM   16032 N  N     . HIS   F 2  264 ? 22.126  52.922  39.524  1.00 18.67  ? 266 HIS   B N     1 
ATOM   16033 C  CA    . HIS   F 2  264 ? 21.801  54.177  38.868  1.00 17.92  ? 266 HIS   B CA    1 
ATOM   16034 C  C     . HIS   F 2  264 ? 20.753  53.979  37.773  1.00 21.77  ? 266 HIS   B C     1 
ATOM   16035 O  O     . HIS   F 2  264 ? 20.772  54.656  36.739  1.00 22.82  ? 266 HIS   B O     1 
ATOM   16036 C  CB    . HIS   F 2  264 ? 23.059  54.825  38.293  1.00 19.13  ? 266 HIS   B CB    1 
ATOM   16037 C  CG    . HIS   F 2  264 ? 23.751  54.003  37.232  1.00 27.45  ? 266 HIS   B CG    1 
ATOM   16038 N  ND1   . HIS   F 2  264 ? 24.740  53.082  37.518  1.00 18.75  ? 266 HIS   B ND1   1 
ATOM   16039 C  CD2   . HIS   F 2  264 ? 23.612  53.993  35.880  1.00 25.58  ? 266 HIS   B CD2   1 
ATOM   16040 C  CE1   . HIS   F 2  264 ? 25.176  52.549  36.391  1.00 18.25  ? 266 HIS   B CE1   1 
ATOM   16041 N  NE2   . HIS   F 2  264 ? 24.503  53.078  35.385  1.00 17.64  ? 266 HIS   B NE2   1 
ATOM   16042 N  N     . PHE   F 2  265 ? 19.807  53.067  37.984  1.00 19.10  ? 267 PHE   B N     1 
ATOM   16043 C  CA    . PHE   F 2  265 ? 18.749  52.837  37.008  1.00 20.86  ? 267 PHE   B CA    1 
ATOM   16044 C  C     . PHE   F 2  265 ? 17.429  53.381  37.540  1.00 22.67  ? 267 PHE   B C     1 
ATOM   16045 O  O     . PHE   F 2  265 ? 16.920  52.922  38.568  1.00 24.94  ? 267 PHE   B O     1 
ATOM   16046 C  CB    . PHE   F 2  265 ? 18.674  51.359  36.640  1.00 17.90  ? 267 PHE   B CB    1 
ATOM   16047 C  CG    . PHE   F 2  265 ? 19.863  50.913  35.855  1.00 18.23  ? 267 PHE   B CG    1 
ATOM   16048 C  CD1   . PHE   F 2  265 ? 19.917  51.113  34.476  1.00 13.71  ? 267 PHE   B CD1   1 
ATOM   16049 C  CD2   . PHE   F 2  265 ? 20.968  50.389  36.493  1.00 15.75  ? 267 PHE   B CD2   1 
ATOM   16050 C  CE1   . PHE   F 2  265 ? 21.005  50.740  33.744  1.00 8.99   ? 267 PHE   B CE1   1 
ATOM   16051 C  CE2   . PHE   F 2  265 ? 22.080  50.011  35.751  1.00 18.27  ? 267 PHE   B CE2   1 
ATOM   16052 C  CZ    . PHE   F 2  265 ? 22.091  50.179  34.373  1.00 13.37  ? 267 PHE   B CZ    1 
ATOM   16053 N  N     . PHE   F 2  266 ? 16.886  54.357  36.831  1.00 17.55  ? 268 PHE   B N     1 
ATOM   16054 C  CA    . PHE   F 2  266 ? 15.796  55.173  37.317  1.00 16.61  ? 268 PHE   B CA    1 
ATOM   16055 C  C     . PHE   F 2  266 ? 14.477  54.730  36.714  1.00 17.73  ? 268 PHE   B C     1 
ATOM   16056 O  O     . PHE   F 2  266 ? 14.414  54.322  35.554  1.00 20.98  ? 268 PHE   B O     1 
ATOM   16057 C  CB    . PHE   F 2  266 ? 16.069  56.630  36.988  1.00 16.56  ? 268 PHE   B CB    1 
ATOM   16058 C  CG    . PHE   F 2  266 ? 17.258  57.181  37.710  1.00 25.80  ? 268 PHE   B CG    1 
ATOM   16059 C  CD1   . PHE   F 2  266 ? 17.699  56.584  38.884  1.00 18.95  ? 268 PHE   B CD1   1 
ATOM   16060 C  CD2   . PHE   F 2  266 ? 17.944  58.284  37.226  1.00 27.53  ? 268 PHE   B CD2   1 
ATOM   16061 C  CE1   . PHE   F 2  266 ? 18.784  57.083  39.571  1.00 19.18  ? 268 PHE   B CE1   1 
ATOM   16062 C  CE2   . PHE   F 2  266 ? 19.048  58.775  37.913  1.00 28.77  ? 268 PHE   B CE2   1 
ATOM   16063 C  CZ    . PHE   F 2  266 ? 19.463  58.168  39.090  1.00 21.73  ? 268 PHE   B CZ    1 
ATOM   16064 N  N     . MET   F 2  267 ? 13.432  54.800  37.517  1.00 18.40  ? 269 MET   B N     1 
ATOM   16065 C  CA    . MET   F 2  267 ? 12.087  54.468  37.097  1.00 17.04  ? 269 MET   B CA    1 
ATOM   16066 C  C     . MET   F 2  267 ? 11.319  55.777  36.934  1.00 20.01  ? 269 MET   B C     1 
ATOM   16067 O  O     . MET   F 2  267 ? 11.112  56.488  37.928  1.00 26.11  ? 269 MET   B O     1 
ATOM   16068 C  CB    . MET   F 2  267 ? 11.438  53.566  38.150  1.00 16.90  ? 269 MET   B CB    1 
ATOM   16069 C  CG    . MET   F 2  267 ? 9.975   53.271  37.934  1.00 28.10  ? 269 MET   B CG    1 
ATOM   16070 S  SD    . MET   F 2  267 ? 9.388   51.884  38.932  1.00 41.50  ? 269 MET   B SD    1 
ATOM   16071 C  CE    . MET   F 2  267 ? 10.907  51.453  39.748  1.00 24.02  ? 269 MET   B CE    1 
ATOM   16072 N  N     . PRO   F 2  268 ? 10.968  56.197  35.727  1.00 20.43  ? 270 PRO   B N     1 
ATOM   16073 C  CA    . PRO   F 2  268 ? 10.239  57.461  35.576  1.00 18.95  ? 270 PRO   B CA    1 
ATOM   16074 C  C     . PRO   F 2  268 ? 8.746   57.237  35.744  1.00 25.36  ? 270 PRO   B C     1 
ATOM   16075 O  O     . PRO   F 2  268 ? 8.260   56.112  35.794  1.00 28.94  ? 270 PRO   B O     1 
ATOM   16076 C  CB    . PRO   F 2  268 ? 10.573  57.927  34.154  1.00 15.40  ? 270 PRO   B CB    1 
ATOM   16077 C  CG    . PRO   F 2  268 ? 11.637  56.953  33.646  1.00 17.28  ? 270 PRO   B CG    1 
ATOM   16078 C  CD    . PRO   F 2  268 ? 11.492  55.700  34.446  1.00 23.08  ? 270 PRO   B CD    1 
ATOM   16079 N  N     . GLY   F 2  269 ? 8.027   58.347  35.848  1.00 27.90  ? 271 GLY   B N     1 
ATOM   16080 C  CA    . GLY   F 2  269 ? 6.594   58.344  36.056  1.00 23.58  ? 271 GLY   B CA    1 
ATOM   16081 C  C     . GLY   F 2  269 ? 6.044   59.729  35.790  1.00 26.52  ? 271 GLY   B C     1 
ATOM   16082 O  O     . GLY   F 2  269 ? 6.634   60.727  36.213  1.00 27.44  ? 271 GLY   B O     1 
ATOM   16083 N  N     . PHE   F 2  270 ? 4.931   59.808  35.068  1.00 28.04  ? 272 PHE   B N     1 
ATOM   16084 C  CA    . PHE   F 2  270 ? 4.327   61.069  34.658  1.00 24.22  ? 272 PHE   B CA    1 
ATOM   16085 C  C     . PHE   F 2  270 ? 2.859   61.082  35.043  1.00 23.01  ? 272 PHE   B C     1 
ATOM   16086 O  O     . PHE   F 2  270 ? 2.181   60.059  34.939  1.00 27.28  ? 272 PHE   B O     1 
ATOM   16087 C  CB    . PHE   F 2  270 ? 4.441   61.269  33.136  1.00 21.16  ? 272 PHE   B CB    1 
ATOM   16088 C  CG    . PHE   F 2  270 ? 4.278   62.686  32.713  1.00 25.33  ? 272 PHE   B CG    1 
ATOM   16089 C  CD1   . PHE   F 2  270 ? 5.353   63.566  32.769  1.00 29.78  ? 272 PHE   B CD1   1 
ATOM   16090 C  CD2   . PHE   F 2  270 ? 3.054   63.159  32.297  1.00 27.76  ? 272 PHE   B CD2   1 
ATOM   16091 C  CE1   . PHE   F 2  270 ? 5.217   64.886  32.397  1.00 30.84  ? 272 PHE   B CE1   1 
ATOM   16092 C  CE2   . PHE   F 2  270 ? 2.896   64.481  31.926  1.00 29.53  ? 272 PHE   B CE2   1 
ATOM   16093 C  CZ    . PHE   F 2  270 ? 3.980   65.350  31.974  1.00 35.14  ? 272 PHE   B CZ    1 
ATOM   16094 N  N     . ALA   F 2  271 ? 2.362   62.237  35.473  1.00 23.13  ? 273 ALA   B N     1 
ATOM   16095 C  CA    . ALA   F 2  271 ? 0.910   62.442  35.583  1.00 25.81  ? 273 ALA   B CA    1 
ATOM   16096 C  C     . ALA   F 2  271 ? 0.589   63.872  35.163  1.00 27.99  ? 273 ALA   B C     1 
ATOM   16097 O  O     . ALA   F 2  271 ? 1.340   64.804  35.500  1.00 28.28  ? 273 ALA   B O     1 
ATOM   16098 C  CB    . ALA   F 2  271 ? 0.362   62.178  36.997  1.00 19.71  ? 273 ALA   B CB    1 
ATOM   16099 N  N     . PRO   F 2  272 ? -0.503  64.081  34.400  1.00 29.83  ? 274 PRO   B N     1 
ATOM   16100 C  CA    . PRO   F 2  272 ? -1.462  63.101  33.881  1.00 24.01  ? 274 PRO   B CA    1 
ATOM   16101 C  C     . PRO   F 2  272 ? -1.018  62.447  32.593  1.00 27.03  ? 274 PRO   B C     1 
ATOM   16102 O  O     . PRO   F 2  272 ? -0.360  63.041  31.738  1.00 25.87  ? 274 PRO   B O     1 
ATOM   16103 C  CB    . PRO   F 2  272 ? -2.688  63.959  33.616  1.00 21.80  ? 274 PRO   B CB    1 
ATOM   16104 C  CG    . PRO   F 2  272 ? -2.082  65.198  33.063  1.00 24.05  ? 274 PRO   B CG    1 
ATOM   16105 C  CD    . PRO   F 2  272 ? -0.862  65.435  33.938  1.00 28.59  ? 274 PRO   B CD    1 
ATOM   16106 N  N     . LEU   F 2  273 ? -1.393  61.192  32.422  1.00 30.27  ? 275 LEU   B N     1 
ATOM   16107 C  CA    . LEU   F 2  273 ? -1.152  60.531  31.156  1.00 21.49  ? 275 LEU   B CA    1 
ATOM   16108 C  C     . LEU   F 2  273 ? -2.161  61.030  30.136  1.00 22.10  ? 275 LEU   B C     1 
ATOM   16109 O  O     . LEU   F 2  273 ? -3.321  61.284  30.461  1.00 23.28  ? 275 LEU   B O     1 
ATOM   16110 C  CB    . LEU   F 2  273 ? -1.228  59.021  31.346  1.00 15.67  ? 275 LEU   B CB    1 
ATOM   16111 C  CG    . LEU   F 2  273 ? -0.218  58.635  32.423  1.00 23.12  ? 275 LEU   B CG    1 
ATOM   16112 C  CD1   . LEU   F 2  273 ? -0.569  57.313  33.061  1.00 26.59  ? 275 LEU   B CD1   1 
ATOM   16113 C  CD2   . LEU   F 2  273 ? 1.230   58.626  31.868  1.00 22.86  ? 275 LEU   B CD2   1 
ATOM   16114 N  N     . THR   F 2  274 ? -1.709  61.201  28.899  1.00 29.27  ? 276 THR   B N     1 
ATOM   16115 C  CA    . THR   F 2  274 ? -2.562  61.791  27.881  1.00 25.94  ? 276 THR   B CA    1 
ATOM   16116 C  C     . THR   F 2  274 ? -2.238  61.189  26.524  1.00 27.76  ? 276 THR   B C     1 
ATOM   16117 O  O     . THR   F 2  274 ? -1.064  61.135  26.146  1.00 30.94  ? 276 THR   B O     1 
ATOM   16118 C  CB    . THR   F 2  274 ? -2.380  63.316  27.838  1.00 26.36  ? 276 THR   B CB    1 
ATOM   16119 O  OG1   . THR   F 2  274 ? -1.013  63.647  27.536  1.00 30.30  ? 276 THR   B OG1   1 
ATOM   16120 C  CG2   . THR   F 2  274 ? -2.742  63.912  29.169  1.00 28.75  ? 276 THR   B CG2   1 
ATOM   16121 N  N     . SER   F 2  275 ? -3.271  60.745  25.804  1.00 25.47  ? 277 SER   B N     1 
ATOM   16122 C  CA    . SER   F 2  275 ? -3.154  60.513  24.366  1.00 26.98  ? 277 SER   B CA    1 
ATOM   16123 C  C     . SER   F 2  275 ? -2.909  61.832  23.657  1.00 25.98  ? 277 SER   B C     1 
ATOM   16124 O  O     . SER   F 2  275 ? -3.508  62.850  23.989  1.00 38.67  ? 277 SER   B O     1 
ATOM   16125 C  CB    . SER   F 2  275 ? -4.426  59.871  23.808  1.00 31.46  ? 277 SER   B CB    1 
ATOM   16126 N  N     . ARG   F 2  276 ? -2.025  61.827  22.680  1.00 33.60  ? 278 ARG   B N     1 
ATOM   16127 C  CA    . ARG   F 2  276 ? -1.796  63.060  21.954  1.00 32.22  ? 278 ARG   B CA    1 
ATOM   16128 C  C     . ARG   F 2  276 ? -3.087  63.483  21.269  1.00 44.40  ? 278 ARG   B C     1 
ATOM   16129 O  O     . ARG   F 2  276 ? -4.006  62.679  21.077  1.00 45.25  ? 278 ARG   B O     1 
ATOM   16130 C  CB    . ARG   F 2  276 ? -0.656  62.881  20.961  1.00 33.36  ? 278 ARG   B CB    1 
ATOM   16131 C  CG    . ARG   F 2  276 ? -0.526  61.459  20.455  1.00 39.34  ? 278 ARG   B CG    1 
ATOM   16132 C  CD    . ARG   F 2  276 ? 0.718   61.308  19.583  1.00 39.53  ? 278 ARG   B CD    1 
ATOM   16133 N  NE    . ARG   F 2  276 ? 0.603   60.234  18.603  1.00 40.20  ? 278 ARG   B NE    1 
ATOM   16134 C  CZ    . ARG   F 2  276 ? 0.523   60.428  17.297  1.00 42.33  ? 278 ARG   B CZ    1 
ATOM   16135 N  NH1   . ARG   F 2  276 ? 0.506   61.649  16.787  1.00 44.31  ? 278 ARG   B NH1   1 
ATOM   16136 N  NH2   . ARG   F 2  276 ? 0.473   59.371  16.482  1.00 44.01  ? 278 ARG   B NH2   1 
ATOM   16137 N  N     . GLY   F 2  277 ? -3.161  64.770  20.930  1.00 50.99  ? 279 GLY   B N     1 
ATOM   16138 C  CA    . GLY   F 2  277 ? -4.412  65.377  20.532  1.00 50.35  ? 279 GLY   B CA    1 
ATOM   16139 C  C     . GLY   F 2  277 ? -5.536  65.276  21.546  1.00 60.26  ? 279 GLY   B C     1 
ATOM   16140 O  O     . GLY   F 2  277 ? -6.691  65.505  21.178  1.00 57.85  ? 279 GLY   B O     1 
ATOM   16141 N  N     . SER   F 2  278 ? -5.249  64.919  22.804  1.00 63.80  ? 280 SER   B N     1 
ATOM   16142 C  CA    . SER   F 2  278 ? -6.279  64.797  23.841  1.00 53.56  ? 280 SER   B CA    1 
ATOM   16143 C  C     . SER   F 2  278 ? -6.667  66.188  24.321  1.00 53.15  ? 280 SER   B C     1 
ATOM   16144 O  O     . SER   F 2  278 ? -5.893  66.845  25.022  1.00 73.40  ? 280 SER   B O     1 
ATOM   16145 C  CB    . SER   F 2  278 ? -5.779  63.952  25.014  1.00 33.42  ? 280 SER   B CB    1 
ATOM   16146 N  N     . GLN   F 2  279 ? -7.872  66.629  23.984  1.00 42.72  ? 281 GLN   B N     1 
ATOM   16147 C  CA    . GLN   F 2  279 ? -8.364  67.880  24.534  1.00 53.46  ? 281 GLN   B CA    1 
ATOM   16148 C  C     . GLN   F 2  279 ? -8.300  67.815  26.053  1.00 52.54  ? 281 GLN   B C     1 
ATOM   16149 O  O     . GLN   F 2  279 ? -8.849  66.894  26.668  1.00 62.79  ? 281 GLN   B O     1 
ATOM   16150 C  CB    . GLN   F 2  279 ? -9.793  68.143  24.057  1.00 60.35  ? 281 GLN   B CB    1 
ATOM   16151 N  N     . GLN   F 2  280 ? -7.610  68.768  26.667  1.00 47.83  ? 282 GLN   B N     1 
ATOM   16152 C  CA    . GLN   F 2  280 ? -7.491  68.791  28.124  1.00 67.92  ? 282 GLN   B CA    1 
ATOM   16153 C  C     . GLN   F 2  280 ? -8.602  69.675  28.700  1.00 64.97  ? 282 GLN   B C     1 
ATOM   16154 O  O     . GLN   F 2  280 ? -8.629  70.890  28.459  1.00 61.74  ? 282 GLN   B O     1 
ATOM   16155 C  CB    . GLN   F 2  280 ? -6.097  69.259  28.544  1.00 64.90  ? 282 GLN   B CB    1 
ATOM   16156 C  CG    . GLN   F 2  280 ? -5.027  68.151  28.519  1.00 54.35  ? 282 GLN   B CG    1 
ATOM   16157 C  CD    . GLN   F 2  280 ? -5.402  66.962  29.398  1.00 59.54  ? 282 GLN   B CD    1 
ATOM   16158 O  OE1   . GLN   F 2  280 ? -5.557  65.842  28.908  1.00 60.89  ? 282 GLN   B OE1   1 
ATOM   16159 N  NE2   . GLN   F 2  280 ? -5.554  67.203  30.704  1.00 57.10  ? 282 GLN   B NE2   1 
ATOM   16160 N  N     . TYR   F 2  281 ? -9.531  69.058  29.447  1.00 59.28  ? 283 TYR   B N     1 
ATOM   16161 C  CA    . TYR   F 2  281 ? -10.723 69.741  29.955  1.00 53.95  ? 283 TYR   B CA    1 
ATOM   16162 C  C     . TYR   F 2  281 ? -10.568 70.234  31.388  1.00 56.51  ? 283 TYR   B C     1 
ATOM   16163 O  O     . TYR   F 2  281 ? -11.060 71.318  31.722  1.00 59.45  ? 283 TYR   B O     1 
ATOM   16164 C  CB    . TYR   F 2  281 ? -11.964 68.830  29.855  1.00 39.81  ? 283 TYR   B CB    1 
ATOM   16165 C  CG    . TYR   F 2  281 ? -12.270 68.449  28.421  1.00 61.07  ? 283 TYR   B CG    1 
ATOM   16166 C  CD1   . TYR   F 2  281 ? -11.860 69.276  27.376  1.00 58.55  ? 283 TYR   B CD1   1 
ATOM   16167 C  CD2   . TYR   F 2  281 ? -12.916 67.251  28.102  1.00 58.93  ? 283 TYR   B CD2   1 
ATOM   16168 C  CE1   . TYR   F 2  281 ? -12.094 68.950  26.063  1.00 59.22  ? 283 TYR   B CE1   1 
ATOM   16169 C  CE2   . TYR   F 2  281 ? -13.166 66.904  26.766  1.00 54.89  ? 283 TYR   B CE2   1 
ATOM   16170 C  CZ    . TYR   F 2  281 ? -12.737 67.770  25.746  1.00 75.37  ? 283 TYR   B CZ    1 
ATOM   16171 O  OH    . TYR   F 2  281 ? -12.944 67.506  24.398  1.00 78.98  ? 283 TYR   B OH    1 
ATOM   16172 N  N     . ARG   F 2  282 ? -9.905  69.474  32.250  1.00 50.37  ? 284 ARG   B N     1 
ATOM   16173 C  CA    . ARG   F 2  282 ? -9.729  69.887  33.631  1.00 45.82  ? 284 ARG   B CA    1 
ATOM   16174 C  C     . ARG   F 2  282 ? -8.259  69.774  34.013  1.00 46.34  ? 284 ARG   B C     1 
ATOM   16175 O  O     . ARG   F 2  282 ? -7.524  68.936  33.480  1.00 45.88  ? 284 ARG   B O     1 
ATOM   16176 C  CB    . ARG   F 2  282 ? -10.607 69.045  34.575  1.00 40.73  ? 284 ARG   B CB    1 
ATOM   16177 C  CG    . ARG   F 2  282 ? -11.012 69.752  35.861  1.00 42.14  ? 284 ARG   B CG    1 
ATOM   16178 C  CD    . ARG   F 2  282 ? -11.669 68.767  36.838  1.00 53.99  ? 284 ARG   B CD    1 
ATOM   16179 N  NE    . ARG   F 2  282 ? -10.833 67.602  37.134  1.00 54.80  ? 284 ARG   B NE    1 
ATOM   16180 C  CZ    . ARG   F 2  282 ? -9.809  67.609  37.980  1.00 49.16  ? 284 ARG   B CZ    1 
ATOM   16181 N  NH1   . ARG   F 2  282 ? -9.446  68.710  38.617  1.00 49.54  ? 284 ARG   B NH1   1 
ATOM   16182 N  NH2   . ARG   F 2  282 ? -9.122  66.488  38.179  1.00 45.95  ? 284 ARG   B NH2   1 
ATOM   16183 N  N     . ALA   F 2  283 ? -7.830  70.645  34.923  1.00 41.19  ? 285 ALA   B N     1 
ATOM   16184 C  CA    . ALA   F 2  283 ? -6.515  70.505  35.526  1.00 35.34  ? 285 ALA   B CA    1 
ATOM   16185 C  C     . ALA   F 2  283 ? -6.545  69.464  36.636  1.00 45.90  ? 285 ALA   B C     1 
ATOM   16186 O  O     . ALA   F 2  283 ? -7.576  69.237  37.279  1.00 46.75  ? 285 ALA   B O     1 
ATOM   16187 C  CB    . ALA   F 2  283 ? -6.038  71.840  36.092  1.00 42.95  ? 285 ALA   B CB    1 
ATOM   16188 N  N     . LEU   F 2  284 ? -5.402  68.828  36.866  1.00 46.15  ? 286 LEU   B N     1 
ATOM   16189 C  CA    . LEU   F 2  284 ? -5.276  67.954  38.024  1.00 41.65  ? 286 LEU   B CA    1 
ATOM   16190 C  C     . LEU   F 2  284 ? -5.041  68.803  39.271  1.00 38.59  ? 286 LEU   B C     1 
ATOM   16191 O  O     . LEU   F 2  284 ? -4.260  69.757  39.238  1.00 45.79  ? 286 LEU   B O     1 
ATOM   16192 C  CB    . LEU   F 2  284 ? -4.130  66.965  37.817  1.00 33.82  ? 286 LEU   B CB    1 
ATOM   16193 C  CG    . LEU   F 2  284 ? -4.398  65.721  36.974  1.00 35.39  ? 286 LEU   B CG    1 
ATOM   16194 C  CD1   . LEU   F 2  284 ? -5.141  64.714  37.790  1.00 33.80  ? 286 LEU   B CD1   1 
ATOM   16195 C  CD2   . LEU   F 2  284 ? -5.185  66.079  35.718  1.00 35.56  ? 286 LEU   B CD2   1 
ATOM   16196 N  N     . THR   F 2  285 ? -5.749  68.489  40.358  1.00 37.95  ? 287 THR   B N     1 
ATOM   16197 C  CA    . THR   F 2  285 ? -5.449  69.127  41.638  1.00 40.82  ? 287 THR   B CA    1 
ATOM   16198 C  C     . THR   F 2  285 ? -4.143  68.569  42.192  1.00 36.29  ? 287 THR   B C     1 
ATOM   16199 O  O     . THR   F 2  285 ? -3.749  67.447  41.875  1.00 33.99  ? 287 THR   B O     1 
ATOM   16200 C  CB    . THR   F 2  285 ? -6.580  68.909  42.659  1.00 36.55  ? 287 THR   B CB    1 
ATOM   16201 O  OG1   . THR   F 2  285 ? -6.533  67.576  43.203  1.00 32.19  ? 287 THR   B OG1   1 
ATOM   16202 C  CG2   . THR   F 2  285 ? -7.911  69.115  42.015  1.00 35.89  ? 287 THR   B CG2   1 
ATOM   16203 N  N     . VAL   F 2  286 ? -3.472  69.353  43.034  1.00 38.10  ? 288 VAL   B N     1 
ATOM   16204 C  CA    . VAL   F 2  286 ? -2.142  68.962  43.515  1.00 36.01  ? 288 VAL   B CA    1 
ATOM   16205 C  C     . VAL   F 2  286 ? -2.210  67.574  44.158  1.00 35.84  ? 288 VAL   B C     1 
ATOM   16206 O  O     . VAL   F 2  286 ? -1.323  66.737  43.916  1.00 30.71  ? 288 VAL   B O     1 
ATOM   16207 C  CB    . VAL   F 2  286 ? -1.543  70.026  44.459  1.00 31.06  ? 288 VAL   B CB    1 
ATOM   16208 C  CG1   . VAL   F 2  286 ? -0.639  69.396  45.514  1.00 30.51  ? 288 VAL   B CG1   1 
ATOM   16209 C  CG2   . VAL   F 2  286 ? -0.733  71.035  43.655  1.00 29.10  ? 288 VAL   B CG2   1 
ATOM   16210 N  N     . PRO   F 2  287 ? -3.236  67.252  44.954  1.00 31.81  ? 289 PRO   B N     1 
ATOM   16211 C  CA    . PRO   F 2  287 ? -3.310  65.887  45.493  1.00 27.70  ? 289 PRO   B CA    1 
ATOM   16212 C  C     . PRO   F 2  287 ? -3.579  64.862  44.425  1.00 31.48  ? 289 PRO   B C     1 
ATOM   16213 O  O     . PRO   F 2  287 ? -3.196  63.699  44.584  1.00 36.49  ? 289 PRO   B O     1 
ATOM   16214 C  CB    . PRO   F 2  287 ? -4.451  65.965  46.514  1.00 22.00  ? 289 PRO   B CB    1 
ATOM   16215 C  CG    . PRO   F 2  287 ? -4.505  67.411  46.871  1.00 27.50  ? 289 PRO   B CG    1 
ATOM   16216 C  CD    . PRO   F 2  287 ? -4.250  68.121  45.563  1.00 26.08  ? 289 PRO   B CD    1 
ATOM   16217 N  N     . GLU   F 2  288 ? -4.204  65.251  43.320  1.00 33.46  ? 290 GLU   B N     1 
ATOM   16218 C  CA    . GLU   F 2  288 ? -4.310  64.322  42.209  1.00 30.02  ? 290 GLU   B CA    1 
ATOM   16219 C  C     . GLU   F 2  288 ? -2.944  64.080  41.589  1.00 29.14  ? 290 GLU   B C     1 
ATOM   16220 O  O     . GLU   F 2  288 ? -2.522  62.932  41.423  1.00 37.73  ? 290 GLU   B O     1 
ATOM   16221 C  CB    . GLU   F 2  288 ? -5.303  64.848  41.183  1.00 35.18  ? 290 GLU   B CB    1 
ATOM   16222 C  CG    . GLU   F 2  288 ? -6.735  64.668  41.621  1.00 37.78  ? 290 GLU   B CG    1 
ATOM   16223 C  CD    . GLU   F 2  288 ? -7.706  65.521  40.828  1.00 39.54  ? 290 GLU   B CD    1 
ATOM   16224 O  OE1   . GLU   F 2  288 ? -7.281  66.526  40.216  1.00 35.37  ? 290 GLU   B OE1   1 
ATOM   16225 O  OE2   . GLU   F 2  288 ? -8.903  65.182  40.821  1.00 42.56  ? 290 GLU   B OE2   1 
ATOM   16226 N  N     . LEU   F 2  289 ? -2.216  65.152  41.276  1.00 33.23  ? 291 LEU   B N     1 
ATOM   16227 C  CA    . LEU   F 2  289 ? -0.891  64.994  40.692  1.00 25.28  ? 291 LEU   B CA    1 
ATOM   16228 C  C     . LEU   F 2  289 ? -0.023  64.085  41.545  1.00 28.81  ? 291 LEU   B C     1 
ATOM   16229 O  O     . LEU   F 2  289 ? 0.624   63.170  41.028  1.00 35.37  ? 291 LEU   B O     1 
ATOM   16230 C  CB    . LEU   F 2  289 ? -0.222  66.344  40.539  1.00 27.59  ? 291 LEU   B CB    1 
ATOM   16231 C  CG    . LEU   F 2  289 ? -0.636  67.333  39.474  1.00 25.76  ? 291 LEU   B CG    1 
ATOM   16232 C  CD1   . LEU   F 2  289 ? 0.375   68.453  39.580  1.00 33.67  ? 291 LEU   B CD1   1 
ATOM   16233 C  CD2   . LEU   F 2  289 ? -0.570  66.706  38.114  1.00 29.37  ? 291 LEU   B CD2   1 
ATOM   16234 N  N     . THR   F 2  290 ? -0.017  64.319  42.863  1.00 31.32  ? 292 THR   B N     1 
ATOM   16235 C  CA    . THR   F 2  290 ? 0.771   63.519  43.807  1.00 31.34  ? 292 THR   B CA    1 
ATOM   16236 C  C     . THR   F 2  290 ? 0.385   62.045  43.765  1.00 31.11  ? 292 THR   B C     1 
ATOM   16237 O  O     . THR   F 2  290 ? 1.235   61.174  43.568  1.00 33.95  ? 292 THR   B O     1 
ATOM   16238 C  CB    . THR   F 2  290 ? 0.589   64.076  45.220  1.00 33.66  ? 292 THR   B CB    1 
ATOM   16239 O  OG1   . THR   F 2  290 ? 1.310   65.302  45.346  1.00 33.28  ? 292 THR   B OG1   1 
ATOM   16240 C  CG2   . THR   F 2  290 ? 1.076   63.111  46.249  1.00 30.62  ? 292 THR   B CG2   1 
ATOM   16241 N  N     . GLN   F 2  291 ? -0.897  61.742  43.969  1.00 34.18  ? 293 GLN   B N     1 
ATOM   16242 C  CA    . GLN   F 2  291 ? -1.325  60.347  44.015  1.00 36.34  ? 293 GLN   B CA    1 
ATOM   16243 C  C     . GLN   F 2  291 ? -0.935  59.609  42.745  1.00 36.82  ? 293 GLN   B C     1 
ATOM   16244 O  O     . GLN   F 2  291 ? -0.397  58.494  42.792  1.00 41.03  ? 293 GLN   B O     1 
ATOM   16245 C  CB    . GLN   F 2  291 ? -2.837  60.265  44.241  1.00 31.89  ? 293 GLN   B CB    1 
ATOM   16246 C  CG    . GLN   F 2  291 ? -3.248  60.602  45.679  1.00 55.41  ? 293 GLN   B CG    1 
ATOM   16247 C  CD    . GLN   F 2  291 ? -2.231  60.110  46.724  1.00 65.59  ? 293 GLN   B CD    1 
ATOM   16248 O  OE1   . GLN   F 2  291 ? -1.919  58.914  46.796  1.00 64.19  ? 293 GLN   B OE1   1 
ATOM   16249 N  NE2   . GLN   F 2  291 ? -1.701  61.045  47.530  1.00 52.37  ? 293 GLN   B NE2   1 
ATOM   16250 N  N     . GLN   F 2  292 ? -1.205  60.212  41.596  1.00 27.59  ? 294 GLN   B N     1 
ATOM   16251 C  CA    . GLN   F 2  292 ? -0.988  59.513  40.342  1.00 27.11  ? 294 GLN   B CA    1 
ATOM   16252 C  C     . GLN   F 2  292 ? 0.490   59.242  40.106  1.00 31.56  ? 294 GLN   B C     1 
ATOM   16253 O  O     . GLN   F 2  292 ? 0.873   58.124  39.749  1.00 35.06  ? 294 GLN   B O     1 
ATOM   16254 C  CB    . GLN   F 2  292 ? -1.579  60.323  39.195  1.00 27.76  ? 294 GLN   B CB    1 
ATOM   16255 C  CG    . GLN   F 2  292 ? -3.055  60.567  39.333  1.00 22.25  ? 294 GLN   B CG    1 
ATOM   16256 C  CD    . GLN   F 2  292 ? -3.646  61.146  38.067  1.00 29.99  ? 294 GLN   B CD    1 
ATOM   16257 O  OE1   . GLN   F 2  292 ? -3.028  61.096  36.999  1.00 35.58  ? 294 GLN   B OE1   1 
ATOM   16258 N  NE2   . GLN   F 2  292 ? -4.848  61.687  38.169  1.00 31.68  ? 294 GLN   B NE2   1 
ATOM   16259 N  N     . MET   F 2  293 ? 1.340   60.253  40.298  1.00 27.90  ? 295 MET   B N     1 
ATOM   16260 C  CA    . MET   F 2  293 ? 2.735   60.115  39.912  1.00 26.33  ? 295 MET   B CA    1 
ATOM   16261 C  C     . MET   F 2  293 ? 3.419   58.986  40.668  1.00 27.75  ? 295 MET   B C     1 
ATOM   16262 O  O     . MET   F 2  293 ? 4.382   58.399  40.155  1.00 27.23  ? 295 MET   B O     1 
ATOM   16263 C  CB    . MET   F 2  293 ? 3.466   61.439  40.125  1.00 28.52  ? 295 MET   B CB    1 
ATOM   16264 C  CG    . MET   F 2  293 ? 4.032   61.621  41.534  1.00 33.77  ? 295 MET   B CG    1 
ATOM   16265 S  SD    . MET   F 2  293 ? 4.621   63.300  41.852  1.00 38.48  ? 295 MET   B SD    1 
ATOM   16266 C  CE    . MET   F 2  293 ? 5.589   63.655  40.386  1.00 32.15  ? 295 MET   B CE    1 
ATOM   16267 N  N     . PHE   F 2  294 ? 2.925   58.645  41.854  1.00 19.13  ? 296 PHE   B N     1 
ATOM   16268 C  CA    . PHE   F 2  294 ? 3.491   57.550  42.632  1.00 26.83  ? 296 PHE   B CA    1 
ATOM   16269 C  C     . PHE   F 2  294 ? 2.826   56.213  42.348  1.00 23.15  ? 296 PHE   B C     1 
ATOM   16270 O  O     . PHE   F 2  294 ? 3.279   55.193  42.870  1.00 26.65  ? 296 PHE   B O     1 
ATOM   16271 C  CB    . PHE   F 2  294 ? 3.410   57.868  44.130  1.00 23.69  ? 296 PHE   B CB    1 
ATOM   16272 C  CG    . PHE   F 2  294 ? 4.502   58.753  44.603  1.00 19.50  ? 296 PHE   B CG    1 
ATOM   16273 C  CD1   . PHE   F 2  294 ? 4.447   60.108  44.384  1.00 19.70  ? 296 PHE   B CD1   1 
ATOM   16274 C  CD2   . PHE   F 2  294 ? 5.615   58.219  45.228  1.00 24.19  ? 296 PHE   B CD2   1 
ATOM   16275 C  CE1   . PHE   F 2  294 ? 5.483   60.924  44.793  1.00 24.78  ? 296 PHE   B CE1   1 
ATOM   16276 C  CE2   . PHE   F 2  294 ? 6.651   59.021  45.648  1.00 21.14  ? 296 PHE   B CE2   1 
ATOM   16277 C  CZ    . PHE   F 2  294 ? 6.589   60.379  45.434  1.00 20.10  ? 296 PHE   B CZ    1 
ATOM   16278 N  N     . ASP   F 2  295 ? 1.788   56.215  41.519  1.00 27.17  ? 297 ASP   B N     1 
ATOM   16279 C  CA    . ASP   F 2  295 ? 0.984   55.046  41.186  1.00 34.06  ? 297 ASP   B CA    1 
ATOM   16280 C  C     . ASP   F 2  295 ? 1.683   54.215  40.113  1.00 32.10  ? 297 ASP   B C     1 
ATOM   16281 O  O     . ASP   F 2  295 ? 2.273   54.755  39.173  1.00 31.08  ? 297 ASP   B O     1 
ATOM   16282 C  CB    . ASP   F 2  295 ? -0.400  55.538  40.707  1.00 34.36  ? 297 ASP   B CB    1 
ATOM   16283 C  CG    . ASP   F 2  295 ? -1.334  54.427  40.198  1.00 36.48  ? 297 ASP   B CG    1 
ATOM   16284 O  OD1   . ASP   F 2  295 ? -0.986  53.229  40.121  1.00 41.30  ? 297 ASP   B OD1   1 
ATOM   16285 O  OD2   . ASP   F 2  295 ? -2.469  54.783  39.863  1.00 41.17  ? 297 ASP   B OD2   1 
ATOM   16286 N  N     . SER   F 2  296 ? 1.600   52.891  40.255  1.00 33.03  ? 298 SER   B N     1 
ATOM   16287 C  CA    . SER   F 2  296 ? 2.213   51.979  39.291  1.00 24.47  ? 298 SER   B CA    1 
ATOM   16288 C  C     . SER   F 2  296 ? 1.630   52.126  37.896  1.00 26.89  ? 298 SER   B C     1 
ATOM   16289 O  O     . SER   F 2  296 ? 2.331   51.913  36.906  1.00 28.75  ? 298 SER   B O     1 
ATOM   16290 C  CB    . SER   F 2  296 ? 2.035   50.540  39.753  1.00 29.66  ? 298 SER   B CB    1 
ATOM   16291 O  OG    . SER   F 2  296 ? 2.301   50.413  41.145  1.00 56.13  ? 298 SER   B OG    1 
ATOM   16292 N  N     . LYS   F 2  297 ? 0.347   52.449  37.782  1.00 29.43  ? 299 LYS   B N     1 
ATOM   16293 C  CA    . LYS   F 2  297 ? -0.182  52.669  36.447  1.00 30.34  ? 299 LYS   B CA    1 
ATOM   16294 C  C     . LYS   F 2  297 ? 0.550   53.793  35.717  1.00 25.68  ? 299 LYS   B C     1 
ATOM   16295 O  O     . LYS   F 2  297 ? 0.421   53.908  34.496  1.00 28.47  ? 299 LYS   B O     1 
ATOM   16296 C  CB    . LYS   F 2  297 ? -1.695  52.948  36.529  1.00 34.29  ? 299 LYS   B CB    1 
ATOM   16297 C  CG    . LYS   F 2  297 ? -2.577  51.717  36.854  1.00 24.95  ? 299 LYS   B CG    1 
ATOM   16298 C  CD    . LYS   F 2  297 ? -4.068  52.057  36.809  1.00 31.05  ? 299 LYS   B CD    1 
ATOM   16299 C  CE    . LYS   F 2  297 ? -4.626  52.389  38.189  1.00 50.98  ? 299 LYS   B CE    1 
ATOM   16300 N  NZ    . LYS   F 2  297 ? -4.708  51.172  39.054  1.00 40.26  ? 299 LYS   B NZ    1 
ATOM   16301 N  N     . ASN   F 2  298 ? 1.333   54.603  36.423  1.00 27.33  ? 300 ASN   B N     1 
ATOM   16302 C  CA    . ASN   F 2  298 ? 1.925   55.814  35.866  1.00 31.91  ? 300 ASN   B CA    1 
ATOM   16303 C  C     . ASN   F 2  298 ? 3.436   55.700  35.659  1.00 27.43  ? 300 ASN   B C     1 
ATOM   16304 O  O     . ASN   F 2  298 ? 4.082   56.706  35.345  1.00 27.65  ? 300 ASN   B O     1 
ATOM   16305 C  CB    . ASN   F 2  298 ? 1.622   57.023  36.770  1.00 33.49  ? 300 ASN   B CB    1 
ATOM   16306 C  CG    . ASN   F 2  298 ? 0.249   57.651  36.510  1.00 27.03  ? 300 ASN   B CG    1 
ATOM   16307 O  OD1   . ASN   F 2  298 ? -0.779  57.024  36.708  1.00 38.93  ? 300 ASN   B OD1   1 
ATOM   16308 N  ND2   . ASN   F 2  298 ? 0.240   58.903  36.130  1.00 22.55  ? 300 ASN   B ND2   1 
ATOM   16309 N  N     . MET   F 2  299 ? 4.019   54.514  35.836  1.00 28.32  ? 301 MET   B N     1 
ATOM   16310 C  CA    . MET   F 2  299 ? 5.461   54.373  35.675  1.00 23.46  ? 301 MET   B CA    1 
ATOM   16311 C  C     . MET   F 2  299 ? 5.813   54.149  34.213  1.00 25.52  ? 301 MET   B C     1 
ATOM   16312 O  O     . MET   F 2  299 ? 4.989   53.712  33.413  1.00 34.28  ? 301 MET   B O     1 
ATOM   16313 C  CB    . MET   F 2  299 ? 6.015   53.217  36.507  1.00 21.08  ? 301 MET   B CB    1 
ATOM   16314 C  CG    . MET   F 2  299 ? 5.861   53.343  38.000  1.00 26.39  ? 301 MET   B CG    1 
ATOM   16315 S  SD    . MET   F 2  299 ? 6.350   54.945  38.672  1.00 32.47  ? 301 MET   B SD    1 
ATOM   16316 C  CE    . MET   F 2  299 ? 6.122   54.591  40.412  1.00 29.24  ? 301 MET   B CE    1 
ATOM   16317 N  N     . MET   F 2  300 ? 7.063   54.456  33.868  1.00 25.41  ? 302 MET   B N     1 
ATOM   16318 C  CA    . MET   F 2  300 ? 7.582   54.241  32.526  1.00 21.13  ? 302 MET   B CA    1 
ATOM   16319 C  C     . MET   F 2  300 ? 8.481   53.007  32.481  1.00 18.28  ? 302 MET   B C     1 
ATOM   16320 O  O     . MET   F 2  300 ? 9.142   52.744  31.468  1.00 10.66  ? 302 MET   B O     1 
ATOM   16321 C  CB    . MET   F 2  300 ? 8.316   55.502  32.050  1.00 20.96  ? 302 MET   B CB    1 
ATOM   16322 C  CG    . MET   F 2  300 ? 7.477   56.793  32.115  1.00 18.18  ? 302 MET   B CG    1 
ATOM   16323 S  SD    . MET   F 2  300 ? 6.107   56.762  30.960  1.00 24.94  ? 302 MET   B SD    1 
ATOM   16324 C  CE    . MET   F 2  300 ? 5.254   58.270  31.337  1.00 26.06  ? 302 MET   B CE    1 
ATOM   16325 N  N     . ALA   F 2  301 ? 8.529   52.269  33.582  1.00 14.06  ? 303 ALA   B N     1 
ATOM   16326 C  CA    . ALA   F 2  301 ? 9.212   50.999  33.695  1.00 16.09  ? 303 ALA   B CA    1 
ATOM   16327 C  C     . ALA   F 2  301 ? 8.200   50.028  34.284  1.00 19.37  ? 303 ALA   B C     1 
ATOM   16328 O  O     . ALA   F 2  301 ? 7.573   50.338  35.299  1.00 22.28  ? 303 ALA   B O     1 
ATOM   16329 C  CB    . ALA   F 2  301 ? 10.463  51.126  34.582  1.00 14.60  ? 303 ALA   B CB    1 
ATOM   16330 N  N     . ALA   F 2  302 ? 8.012   48.867  33.658  1.00 17.68  ? 304 ALA   B N     1 
ATOM   16331 C  CA    . ALA   F 2  302 ? 6.967   47.951  34.122  1.00 17.45  ? 304 ALA   B CA    1 
ATOM   16332 C  C     . ALA   F 2  302 ? 7.486   47.166  35.320  1.00 20.91  ? 304 ALA   B C     1 
ATOM   16333 O  O     . ALA   F 2  302 ? 7.900   46.012  35.209  1.00 21.55  ? 304 ALA   B O     1 
ATOM   16334 C  CB    . ALA   F 2  302 ? 6.520   47.030  33.005  1.00 16.85  ? 304 ALA   B CB    1 
ATOM   16335 N  N     . CYS   F 2  303 ? 7.467   47.829  36.483  1.00 18.90  ? 305 CYS   B N     1 
ATOM   16336 C  CA    . CYS   F 2  303 ? 7.842   47.257  37.769  1.00 17.96  ? 305 CYS   B CA    1 
ATOM   16337 C  C     . CYS   F 2  303 ? 6.878   47.717  38.848  1.00 24.21  ? 305 CYS   B C     1 
ATOM   16338 O  O     . CYS   F 2  303 ? 6.494   48.888  38.886  1.00 29.41  ? 305 CYS   B O     1 
ATOM   16339 C  CB    . CYS   F 2  303 ? 9.244   47.683  38.179  1.00 29.72  ? 305 CYS   B CB    1 
ATOM   16340 S  SG    . CYS   F 2  303 ? 10.441  47.515  36.869  1.00 35.46  ? 305 CYS   B SG    1 
ATOM   16341 N  N     . ASP   F 2  304 ? 6.517   46.811  39.742  1.00 29.04  ? 306 ASP   B N     1 
ATOM   16342 C  CA    . ASP   F 2  304 ? 5.627   47.175  40.841  1.00 35.85  ? 306 ASP   B CA    1 
ATOM   16343 C  C     . ASP   F 2  304 ? 6.368   47.936  41.937  1.00 30.34  ? 306 ASP   B C     1 
ATOM   16344 O  O     . ASP   F 2  304 ? 7.131   47.333  42.703  1.00 31.06  ? 306 ASP   B O     1 
ATOM   16345 C  CB    . ASP   F 2  304 ? 4.985   45.934  41.452  1.00 29.26  ? 306 ASP   B CB    1 
ATOM   16346 C  CG    . ASP   F 2  304 ? 3.722   46.261  42.245  1.00 39.76  ? 306 ASP   B CG    1 
ATOM   16347 O  OD1   . ASP   F 2  304 ? 3.475   47.466  42.586  1.00 32.84  ? 306 ASP   B OD1   1 
ATOM   16348 O  OD2   . ASP   F 2  304 ? 2.974   45.284  42.497  1.00 36.50  ? 306 ASP   B OD2   1 
ATOM   16349 N  N     . PRO   F 2  305 ? 6.163   49.238  42.083  1.00 22.72  ? 307 PRO   B N     1 
ATOM   16350 C  CA    . PRO   F 2  305 ? 6.922   49.925  43.126  1.00 30.71  ? 307 PRO   B CA    1 
ATOM   16351 C  C     . PRO   F 2  305 ? 6.644   49.352  44.524  1.00 30.54  ? 307 PRO   B C     1 
ATOM   16352 O  O     . PRO   F 2  305 ? 7.569   49.274  45.344  1.00 30.23  ? 307 PRO   B O     1 
ATOM   16353 C  CB    . PRO   F 2  305 ? 6.520   51.406  42.940  1.00 23.82  ? 307 PRO   B CB    1 
ATOM   16354 C  CG    . PRO   F 2  305 ? 5.343   51.440  42.122  1.00 19.45  ? 307 PRO   B CG    1 
ATOM   16355 C  CD    . PRO   F 2  305 ? 5.299   50.157  41.324  1.00 30.10  ? 307 PRO   B CD    1 
ATOM   16356 N  N     . ARG   F 2  306 ? 5.417   48.893  44.807  1.00 29.64  ? 308 ARG   B N     1 
ATOM   16357 C  CA    . ARG   F 2  306 ? 5.139   48.281  46.108  1.00 28.46  ? 308 ARG   B CA    1 
ATOM   16358 C  C     . ARG   F 2  306 ? 5.849   46.945  46.278  1.00 31.14  ? 308 ARG   B C     1 
ATOM   16359 O  O     . ARG   F 2  306 ? 5.811   46.376  47.373  1.00 39.39  ? 308 ARG   B O     1 
ATOM   16360 C  CB    . ARG   F 2  306 ? 3.623   48.080  46.336  1.00 35.96  ? 308 ARG   B CB    1 
ATOM   16361 C  CG    . ARG   F 2  306 ? 2.712   49.358  46.367  1.00 49.57  ? 308 ARG   B CG    1 
ATOM   16362 C  CD    . ARG   F 2  306 ? 2.160   49.784  44.938  1.00 58.86  ? 308 ARG   B CD    1 
ATOM   16363 N  NE    . ARG   F 2  306 ? 1.904   51.227  44.808  1.00 50.98  ? 308 ARG   B NE    1 
ATOM   16364 C  CZ    . ARG   F 2  306 ? 1.262   51.799  43.800  1.00 30.67  ? 308 ARG   B CZ    1 
ATOM   16365 N  NH1   . ARG   F 2  306 ? 0.742   51.082  42.825  1.00 30.65  ? 308 ARG   B NH1   1 
ATOM   16366 N  NH2   . ARG   F 2  306 ? 1.147   53.121  43.769  1.00 30.17  ? 308 ARG   B NH2   1 
ATOM   16367 N  N     . HIS   F 2  307 ? 6.489   46.430  45.231  1.00 32.53  ? 309 HIS   B N     1 
ATOM   16368 C  CA    . HIS   F 2  307 ? 7.271   45.204  45.311  1.00 30.18  ? 309 HIS   B CA    1 
ATOM   16369 C  C     . HIS   F 2  307 ? 8.702   45.454  45.734  1.00 35.56  ? 309 HIS   B C     1 
ATOM   16370 O  O     . HIS   F 2  307 ? 9.476   44.500  45.822  1.00 37.49  ? 309 HIS   B O     1 
ATOM   16371 C  CB    . HIS   F 2  307 ? 7.291   44.487  43.966  1.00 35.16  ? 309 HIS   B CB    1 
ATOM   16372 C  CG    . HIS   F 2  307 ? 6.195   43.489  43.793  1.00 43.52  ? 309 HIS   B CG    1 
ATOM   16373 N  ND1   . HIS   F 2  307 ? 4.887   43.853  43.554  1.00 45.54  ? 309 HIS   B ND1   1 
ATOM   16374 C  CD2   . HIS   F 2  307 ? 6.213   42.137  43.806  1.00 47.04  ? 309 HIS   B CD2   1 
ATOM   16375 C  CE1   . HIS   F 2  307 ? 4.144   42.767  43.439  1.00 47.68  ? 309 HIS   B CE1   1 
ATOM   16376 N  NE2   . HIS   F 2  307 ? 4.924   41.712  43.591  1.00 52.31  ? 309 HIS   B NE2   1 
ATOM   16377 N  N     . GLY   F 2  308 ? 9.079   46.705  45.965  1.00 34.43  ? 310 GLY   B N     1 
ATOM   16378 C  CA    . GLY   F 2  308 ? 10.418  47.020  46.412  1.00 28.03  ? 310 GLY   B CA    1 
ATOM   16379 C  C     . GLY   F 2  308 ? 10.421  48.147  47.418  1.00 30.48  ? 310 GLY   B C     1 
ATOM   16380 O  O     . GLY   F 2  308 ? 9.444   48.330  48.156  1.00 28.35  ? 310 GLY   B O     1 
ATOM   16381 N  N     . ARG   F 2  309 ? 11.527  48.897  47.457  1.00 32.64  ? 311 ARG   B N     1 
ATOM   16382 C  CA    . ARG   F 2  309 ? 11.683  50.049  48.331  1.00 24.39  ? 311 ARG   B CA    1 
ATOM   16383 C  C     . ARG   F 2  309 ? 12.376  51.157  47.557  1.00 22.96  ? 311 ARG   B C     1 
ATOM   16384 O  O     . ARG   F 2  309 ? 13.284  50.911  46.760  1.00 23.63  ? 311 ARG   B O     1 
ATOM   16385 C  CB    . ARG   F 2  309 ? 12.478  49.709  49.597  1.00 21.76  ? 311 ARG   B CB    1 
ATOM   16386 C  CG    . ARG   F 2  309 ? 12.060  48.409  50.250  1.00 30.58  ? 311 ARG   B CG    1 
ATOM   16387 C  CD    . ARG   F 2  309 ? 12.583  48.299  51.663  1.00 33.57  ? 311 ARG   B CD    1 
ATOM   16388 N  NE    . ARG   F 2  309 ? 11.916  49.252  52.543  1.00 44.22  ? 311 ARG   B NE    1 
ATOM   16389 C  CZ    . ARG   F 2  309 ? 12.323  49.570  53.767  1.00 43.10  ? 311 ARG   B CZ    1 
ATOM   16390 N  NH1   . ARG   F 2  309 ? 13.426  49.050  54.290  1.00 40.33  ? 311 ARG   B NH1   1 
ATOM   16391 N  NH2   . ARG   F 2  309 ? 11.604  50.433  54.484  1.00 34.89  ? 311 ARG   B NH2   1 
ATOM   16392 N  N     . TYR   F 2  310 ? 11.927  52.378  47.783  1.00 23.59  ? 312 TYR   B N     1 
ATOM   16393 C  CA    . TYR   F 2  310 ? 12.561  53.529  47.169  1.00 23.19  ? 312 TYR   B CA    1 
ATOM   16394 C  C     . TYR   F 2  310 ? 13.868  53.833  47.886  1.00 27.35  ? 312 TYR   B C     1 
ATOM   16395 O  O     . TYR   F 2  310 ? 13.873  54.089  49.103  1.00 23.83  ? 312 TYR   B O     1 
ATOM   16396 C  CB    . TYR   F 2  310 ? 11.621  54.724  47.212  1.00 23.05  ? 312 TYR   B CB    1 
ATOM   16397 C  CG    . TYR   F 2  310 ? 10.501  54.624  46.221  1.00 22.05  ? 312 TYR   B CG    1 
ATOM   16398 C  CD1   . TYR   F 2  310 ? 10.763  54.424  44.883  1.00 22.76  ? 312 TYR   B CD1   1 
ATOM   16399 C  CD2   . TYR   F 2  310 ? 9.185   54.691  46.630  1.00 20.16  ? 312 TYR   B CD2   1 
ATOM   16400 C  CE1   . TYR   F 2  310 ? 9.737   54.318  43.967  1.00 26.27  ? 312 TYR   B CE1   1 
ATOM   16401 C  CE2   . TYR   F 2  310 ? 8.161   54.586  45.731  1.00 22.15  ? 312 TYR   B CE2   1 
ATOM   16402 C  CZ    . TYR   F 2  310 ? 8.432   54.405  44.389  1.00 26.77  ? 312 TYR   B CZ    1 
ATOM   16403 O  OH    . TYR   F 2  310 ? 7.398   54.306  43.472  1.00 27.68  ? 312 TYR   B OH    1 
ATOM   16404 N  N     . LEU   F 2  311 ? 14.971  53.788  47.131  1.00 18.57  ? 313 LEU   B N     1 
ATOM   16405 C  CA    . LEU   F 2  311 ? 16.260  54.232  47.649  1.00 16.28  ? 313 LEU   B CA    1 
ATOM   16406 C  C     . LEU   F 2  311 ? 16.322  55.760  47.703  1.00 18.78  ? 313 LEU   B C     1 
ATOM   16407 O  O     . LEU   F 2  311 ? 16.513  56.348  48.773  1.00 21.85  ? 313 LEU   B O     1 
ATOM   16408 C  CB    . LEU   F 2  311 ? 17.387  53.652  46.788  1.00 16.44  ? 313 LEU   B CB    1 
ATOM   16409 C  CG    . LEU   F 2  311 ? 17.633  52.141  46.900  1.00 18.62  ? 313 LEU   B CG    1 
ATOM   16410 C  CD1   . LEU   F 2  311 ? 18.838  51.731  46.069  1.00 25.06  ? 313 LEU   B CD1   1 
ATOM   16411 C  CD2   . LEU   F 2  311 ? 17.834  51.698  48.360  1.00 18.19  ? 313 LEU   B CD2   1 
ATOM   16412 N  N     . THR   F 2  312 ? 16.166  56.420  46.550  1.00 19.75  ? 314 THR   B N     1 
ATOM   16413 C  CA    . THR   F 2  312 ? 15.995  57.868  46.450  1.00 18.49  ? 314 THR   B CA    1 
ATOM   16414 C  C     . THR   F 2  312 ? 14.863  58.163  45.466  1.00 20.57  ? 314 THR   B C     1 
ATOM   16415 O  O     . THR   F 2  312 ? 14.442  57.287  44.697  1.00 17.16  ? 314 THR   B O     1 
ATOM   16416 C  CB    . THR   F 2  312 ? 17.265  58.550  45.967  1.00 20.07  ? 314 THR   B CB    1 
ATOM   16417 O  OG1   . THR   F 2  312 ? 17.561  58.055  44.655  1.00 25.80  ? 314 THR   B OG1   1 
ATOM   16418 C  CG2   . THR   F 2  312 ? 18.424  58.255  46.879  1.00 17.12  ? 314 THR   B CG2   1 
ATOM   16419 N  N     . VAL   F 2  313 ? 14.385  59.416  45.478  1.00 16.44  ? 315 VAL   B N     1 
ATOM   16420 C  CA    . VAL   F 2  313 ? 13.214  59.848  44.706  1.00 17.75  ? 315 VAL   B CA    1 
ATOM   16421 C  C     . VAL   F 2  313 ? 13.232  61.362  44.486  1.00 16.84  ? 315 VAL   B C     1 
ATOM   16422 O  O     . VAL   F 2  313 ? 13.436  62.130  45.426  1.00 16.48  ? 315 VAL   B O     1 
ATOM   16423 C  CB    . VAL   F 2  313 ? 11.906  59.441  45.413  1.00 16.21  ? 315 VAL   B CB    1 
ATOM   16424 C  CG1   . VAL   F 2  313 ? 10.713  60.130  44.774  1.00 12.76  ? 315 VAL   B CG1   1 
ATOM   16425 C  CG2   . VAL   F 2  313 ? 11.732  57.936  45.416  1.00 22.54  ? 315 VAL   B CG2   1 
ATOM   16426 N  N     . ALA   F 2  314 ? 12.992  61.810  43.253  1.00 20.79  ? 316 ALA   B N     1 
ATOM   16427 C  CA    . ALA   F 2  314 ? 12.907  63.233  42.928  1.00 23.58  ? 316 ALA   B CA    1 
ATOM   16428 C  C     . ALA   F 2  314 ? 11.555  63.519  42.294  1.00 23.30  ? 316 ALA   B C     1 
ATOM   16429 O  O     . ALA   F 2  314 ? 11.135  62.797  41.385  1.00 28.27  ? 316 ALA   B O     1 
ATOM   16430 C  CB    . ALA   F 2  314 ? 14.027  63.676  41.976  1.00 16.55  ? 316 ALA   B CB    1 
ATOM   16431 N  N     . ALA   F 2  315 ? 10.878  64.567  42.765  1.00 25.64  ? 317 ALA   B N     1 
ATOM   16432 C  CA    . ALA   F 2  315 ? 9.549   64.933  42.284  1.00 26.17  ? 317 ALA   B CA    1 
ATOM   16433 C  C     . ALA   F 2  315 ? 9.615   66.343  41.715  1.00 27.83  ? 317 ALA   B C     1 
ATOM   16434 O  O     . ALA   F 2  315 ? 10.046  67.275  42.405  1.00 26.30  ? 317 ALA   B O     1 
ATOM   16435 C  CB    . ALA   F 2  315 ? 8.503   64.841  43.397  1.00 18.57  ? 317 ALA   B CB    1 
ATOM   16436 N  N     . ILE   F 2  316 ? 9.208   66.491  40.454  1.00 22.82  ? 318 ILE   B N     1 
ATOM   16437 C  CA    . ILE   F 2  316 ? 9.167   67.784  39.778  1.00 24.90  ? 318 ILE   B CA    1 
ATOM   16438 C  C     . ILE   F 2  316 ? 7.705   68.132  39.493  1.00 23.47  ? 318 ILE   B C     1 
ATOM   16439 O  O     . ILE   F 2  316 ? 6.970   67.333  38.906  1.00 26.56  ? 318 ILE   B O     1 
ATOM   16440 C  CB    . ILE   F 2  316 ? 10.022  67.782  38.494  1.00 27.62  ? 318 ILE   B CB    1 
ATOM   16441 C  CG1   . ILE   F 2  316 ? 11.455  67.341  38.799  1.00 23.58  ? 318 ILE   B CG1   1 
ATOM   16442 C  CG2   . ILE   F 2  316 ? 10.068  69.165  37.846  1.00 20.89  ? 318 ILE   B CG2   1 
ATOM   16443 C  CD1   . ILE   F 2  316 ? 11.813  65.960  38.303  0.00 23.13  ? 318 ILE   B CD1   1 
ATOM   16444 N  N     . PHE   F 2  317 ? 7.274   69.302  39.959  1.00 26.51  ? 319 PHE   B N     1 
ATOM   16445 C  CA    . PHE   F 2  317 ? 5.930   69.812  39.723  1.00 28.81  ? 319 PHE   B CA    1 
ATOM   16446 C  C     . PHE   F 2  317 ? 6.042   70.985  38.757  1.00 29.63  ? 319 PHE   B C     1 
ATOM   16447 O  O     . PHE   F 2  317 ? 6.998   71.763  38.825  1.00 32.75  ? 319 PHE   B O     1 
ATOM   16448 C  CB    . PHE   F 2  317 ? 5.245   70.244  41.048  1.00 20.66  ? 319 PHE   B CB    1 
ATOM   16449 C  CG    . PHE   F 2  317 ? 4.818   69.084  41.934  1.00 20.55  ? 319 PHE   B CG    1 
ATOM   16450 C  CD1   . PHE   F 2  317 ? 5.739   68.431  42.755  1.00 26.54  ? 319 PHE   B CD1   1 
ATOM   16451 C  CD2   . PHE   F 2  317 ? 3.504   68.645  41.950  1.00 20.98  ? 319 PHE   B CD2   1 
ATOM   16452 C  CE1   . PHE   F 2  317 ? 5.350   67.365  43.560  1.00 27.89  ? 319 PHE   B CE1   1 
ATOM   16453 C  CE2   . PHE   F 2  317 ? 3.110   67.569  42.752  1.00 23.83  ? 319 PHE   B CE2   1 
ATOM   16454 C  CZ    . PHE   F 2  317 ? 4.033   66.924  43.541  1.00 23.88  ? 319 PHE   B CZ    1 
ATOM   16455 N  N     . ARG   F 2  318 ? 5.083   71.110  37.848  1.00 31.62  ? 320 ARG   B N     1 
ATOM   16456 C  CA    . ARG   F 2  318 ? 5.096   72.219  36.902  1.00 31.43  ? 320 ARG   B CA    1 
ATOM   16457 C  C     . ARG   F 2  318 ? 3.696   72.805  36.785  1.00 33.97  ? 320 ARG   B C     1 
ATOM   16458 O  O     . ARG   F 2  318 ? 2.696   72.106  36.978  1.00 35.50  ? 320 ARG   B O     1 
ATOM   16459 C  CB    . ARG   F 2  318 ? 5.607   71.783  35.530  1.00 28.87  ? 320 ARG   B CB    1 
ATOM   16460 C  CG    . ARG   F 2  318 ? 6.842   70.938  35.603  1.00 29.35  ? 320 ARG   B CG    1 
ATOM   16461 C  CD    . ARG   F 2  318 ? 7.346   70.630  34.228  1.00 35.96  ? 320 ARG   B CD    1 
ATOM   16462 N  NE    . ARG   F 2  318 ? 7.865   71.825  33.582  1.00 37.46  ? 320 ARG   B NE    1 
ATOM   16463 C  CZ    . ARG   F 2  318 ? 8.047   71.943  32.276  1.00 39.27  ? 320 ARG   B CZ    1 
ATOM   16464 N  NH1   . ARG   F 2  318 ? 7.794   70.939  31.452  1.00 36.37  ? 320 ARG   B NH1   1 
ATOM   16465 N  NH2   . ARG   F 2  318 ? 8.483   73.099  31.783  1.00 40.54  ? 320 ARG   B NH2   1 
ATOM   16466 N  N     . GLY   F 2  319 ? 3.645   74.097  36.469  1.00 34.20  ? 321 GLY   B N     1 
ATOM   16467 C  CA    . GLY   F 2  319 ? 2.433   74.890  36.431  1.00 37.16  ? 321 GLY   B CA    1 
ATOM   16468 C  C     . GLY   F 2  319 ? 2.234   75.713  37.699  1.00 41.45  ? 321 GLY   B C     1 
ATOM   16469 O  O     . GLY   F 2  319 ? 2.843   75.471  38.747  1.00 42.82  ? 321 GLY   B O     1 
ATOM   16470 N  N     . ARG   F 2  320 ? 1.354   76.709  37.598  1.00 38.60  ? 322 ARG   B N     1 
ATOM   16471 C  CA    . ARG   F 2  320 ? 1.092   77.599  38.726  1.00 36.87  ? 322 ARG   B CA    1 
ATOM   16472 C  C     . ARG   F 2  320 ? 0.312   76.853  39.808  1.00 26.75  ? 322 ARG   B C     1 
ATOM   16473 O  O     . ARG   F 2  320 ? -0.809  76.406  39.562  1.00 33.08  ? 322 ARG   B O     1 
ATOM   16474 C  CB    . ARG   F 2  320 ? 0.311   78.839  38.267  1.00 45.84  ? 322 ARG   B CB    1 
ATOM   16475 C  CG    . ARG   F 2  320 ? 0.674   79.432  36.885  1.00 45.75  ? 322 ARG   B CG    1 
ATOM   16476 C  CD    . ARG   F 2  320 ? 1.938   80.274  36.887  1.00 51.16  ? 322 ARG   B CD    1 
ATOM   16477 N  NE    . ARG   F 2  320 ? 1.926   81.310  37.918  1.00 71.42  ? 322 ARG   B NE    1 
ATOM   16478 C  CZ    . ARG   F 2  320 ? 2.940   82.132  38.164  1.00 75.80  ? 322 ARG   B CZ    1 
ATOM   16479 N  NH1   . ARG   F 2  320 ? 4.067   82.068  37.471  1.00 65.01  ? 322 ARG   B NH1   1 
ATOM   16480 N  NH2   . ARG   F 2  320 ? 2.820   83.043  39.127  1.00 73.95  ? 322 ARG   B NH2   1 
ATOM   16481 N  N     . MET   F 2  321 ? 0.885   76.728  41.007  1.00 23.30  ? 323 MET   B N     1 
ATOM   16482 C  CA    . MET   F 2  321 ? 0.226   76.015  42.101  1.00 18.86  ? 323 MET   B CA    1 
ATOM   16483 C  C     . MET   F 2  321 ? 0.883   76.412  43.425  1.00 25.33  ? 323 MET   B C     1 
ATOM   16484 O  O     . MET   F 2  321 ? 1.760   77.279  43.460  1.00 35.18  ? 323 MET   B O     1 
ATOM   16485 C  CB    . MET   F 2  321 ? 0.320   74.513  41.885  1.00 23.88  ? 323 MET   B CB    1 
ATOM   16486 C  CG    . MET   F 2  321 ? 1.799   74.087  41.905  1.00 28.36  ? 323 MET   B CG    1 
ATOM   16487 S  SD    . MET   F 2  321 ? 2.168   72.414  41.440  1.00 27.06  ? 323 MET   B SD    1 
ATOM   16488 C  CE    . MET   F 2  321 ? 1.843   72.477  39.650  1.00 30.17  ? 323 MET   B CE    1 
ATOM   16489 N  N     . SER   F 2  322 ? 0.487   75.727  44.512  1.00 21.43  ? 324 SER   B N     1 
ATOM   16490 C  CA    . SER   F 2  322 ? 0.799   76.095  45.890  1.00 19.05  ? 324 SER   B CA    1 
ATOM   16491 C  C     . SER   F 2  322 ? 1.901   75.197  46.441  1.00 31.45  ? 324 SER   B C     1 
ATOM   16492 O  O     . SER   F 2  322 ? 1.651   74.043  46.814  1.00 28.64  ? 324 SER   B O     1 
ATOM   16493 C  CB    . SER   F 2  322 ? -0.449  75.990  46.765  1.00 22.83  ? 324 SER   B CB    1 
ATOM   16494 O  OG    . SER   F 2  322 ? -0.163  76.127  48.158  1.00 29.45  ? 324 SER   B OG    1 
ATOM   16495 N  N     . MET   F 2  323 ? 3.112   75.741  46.540  1.00 32.04  ? 325 MET   B N     1 
ATOM   16496 C  CA    . MET   F 2  323 ? 4.155   75.029  47.262  1.00 32.53  ? 325 MET   B CA    1 
ATOM   16497 C  C     . MET   F 2  323 ? 3.691   74.609  48.651  1.00 34.44  ? 325 MET   B C     1 
ATOM   16498 O  O     . MET   F 2  323 ? 4.071   73.535  49.136  1.00 33.14  ? 325 MET   B O     1 
ATOM   16499 C  CB    . MET   F 2  323 ? 5.402   75.895  47.350  1.00 37.60  ? 325 MET   B CB    1 
ATOM   16500 C  CG    . MET   F 2  323 ? 6.048   76.164  46.010  1.00 41.82  ? 325 MET   B CG    1 
ATOM   16501 S  SD    . MET   F 2  323 ? 7.815   76.273  46.288  1.00 67.43  ? 325 MET   B SD    1 
ATOM   16502 C  CE    . MET   F 2  323 ? 8.098   74.676  47.088  1.00 38.12  ? 325 MET   B CE    1 
ATOM   16503 N  N     . LYS   F 2  324 ? 2.855   75.422  49.305  1.00 35.29  ? 326 LYS   B N     1 
ATOM   16504 C  CA    . LYS   F 2  324 ? 2.355   75.014  50.613  1.00 38.52  ? 326 LYS   B CA    1 
ATOM   16505 C  C     . LYS   F 2  324 ? 1.603   73.686  50.537  1.00 41.73  ? 326 LYS   B C     1 
ATOM   16506 O  O     . LYS   F 2  324 ? 1.675   72.870  51.473  1.00 33.05  ? 326 LYS   B O     1 
ATOM   16507 C  CB    . LYS   F 2  324 ? 1.464   76.098  51.216  1.00 35.91  ? 326 LYS   B CB    1 
ATOM   16508 C  CG    . LYS   F 2  324 ? 1.225   75.913  52.727  1.00 41.83  ? 326 LYS   B CG    1 
ATOM   16509 C  CD    . LYS   F 2  324 ? -0.208  75.553  53.094  1.00 38.78  ? 326 LYS   B CD    1 
ATOM   16510 C  CE    . LYS   F 2  324 ? -0.446  75.704  54.597  1.00 48.20  ? 326 LYS   B CE    1 
ATOM   16511 N  NZ    . LYS   F 2  324 ? -1.897  75.750  54.964  1.00 57.10  ? 326 LYS   B NZ    1 
ATOM   16512 N  N     . GLU   F 2  325 ? 0.906   73.444  49.421  1.00 40.28  ? 327 GLU   B N     1 
ATOM   16513 C  CA    . GLU   F 2  325 ? 0.108   72.243  49.200  1.00 33.84  ? 327 GLU   B CA    1 
ATOM   16514 C  C     . GLU   F 2  325 ? 0.938   71.090  48.629  1.00 32.75  ? 327 GLU   B C     1 
ATOM   16515 O  O     . GLU   F 2  325 ? 0.837   69.956  49.117  1.00 28.35  ? 327 GLU   B O     1 
ATOM   16516 C  CB    . GLU   F 2  325 ? -1.066  72.588  48.276  1.00 27.79  ? 327 GLU   B CB    1 
ATOM   16517 C  CG    . GLU   F 2  325 ? -2.185  71.569  48.220  1.00 33.92  ? 327 GLU   B CG    1 
ATOM   16518 C  CD    . GLU   F 2  325 ? -3.305  72.005  47.285  1.00 41.65  ? 327 GLU   B CD    1 
ATOM   16519 O  OE1   . GLU   F 2  325 ? -3.238  73.165  46.810  1.00 38.72  ? 327 GLU   B OE1   1 
ATOM   16520 O  OE2   . GLU   F 2  325 ? -4.240  71.198  47.024  1.00 52.64  ? 327 GLU   B OE2   1 
ATOM   16521 N  N     . VAL   F 2  326 ? 1.753   71.358  47.596  1.00 30.49  ? 328 VAL   B N     1 
ATOM   16522 C  CA    . VAL   F 2  326 ? 2.719   70.359  47.129  1.00 32.01  ? 328 VAL   B CA    1 
ATOM   16523 C  C     . VAL   F 2  326 ? 3.468   69.772  48.319  1.00 34.50  ? 328 VAL   B C     1 
ATOM   16524 O  O     . VAL   F 2  326 ? 3.523   68.545  48.509  1.00 27.69  ? 328 VAL   B O     1 
ATOM   16525 C  CB    . VAL   F 2  326 ? 3.697   70.973  46.104  1.00 26.27  ? 328 VAL   B CB    1 
ATOM   16526 C  CG1   . VAL   F 2  326 ? 4.860   70.035  45.844  1.00 22.01  ? 328 VAL   B CG1   1 
ATOM   16527 C  CG2   . VAL   F 2  326 ? 2.996   71.284  44.791  1.00 27.03  ? 328 VAL   B CG2   1 
ATOM   16528 N  N     . ASP   F 2  327 ? 4.030   70.659  49.153  1.00 31.43  ? 329 ASP   B N     1 
ATOM   16529 C  CA    . ASP   F 2  327 ? 4.791   70.243  50.324  1.00 28.14  ? 329 ASP   B CA    1 
ATOM   16530 C  C     . ASP   F 2  327 ? 3.927   69.424  51.273  1.00 31.07  ? 329 ASP   B C     1 
ATOM   16531 O  O     . ASP   F 2  327 ? 4.364   68.387  51.793  1.00 32.74  ? 329 ASP   B O     1 
ATOM   16532 C  CB    . ASP   F 2  327 ? 5.361   71.471  51.042  1.00 25.22  ? 329 ASP   B CB    1 
ATOM   16533 C  CG    . ASP   F 2  327 ? 6.592   72.053  50.349  1.00 30.95  ? 329 ASP   B CG    1 
ATOM   16534 O  OD1   . ASP   F 2  327 ? 7.147   71.412  49.418  1.00 39.17  ? 329 ASP   B OD1   1 
ATOM   16535 O  OD2   . ASP   F 2  327 ? 7.017   73.153  50.754  1.00 24.39  ? 329 ASP   B OD2   1 
ATOM   16536 N  N     . GLU   F 2  328 ? 2.696   69.880  51.520  1.00 30.44  ? 330 GLU   B N     1 
ATOM   16537 C  CA    . GLU   F 2  328 ? 1.788   69.112  52.363  1.00 26.77  ? 330 GLU   B CA    1 
ATOM   16538 C  C     . GLU   F 2  328 ? 1.553   67.739  51.768  1.00 29.14  ? 330 GLU   B C     1 
ATOM   16539 O  O     . GLU   F 2  328 ? 1.604   66.720  52.475  1.00 27.07  ? 330 GLU   B O     1 
ATOM   16540 C  CB    . GLU   F 2  328 ? 0.460   69.847  52.525  1.00 32.98  ? 330 GLU   B CB    1 
ATOM   16541 C  CG    . GLU   F 2  328 ? 0.193   70.413  53.903  1.00 30.08  ? 330 GLU   B CG    1 
ATOM   16542 C  CD    . GLU   F 2  328 ? -0.562  71.726  53.836  1.00 46.50  ? 330 GLU   B CD    1 
ATOM   16543 O  OE1   . GLU   F 2  328 ? -0.194  72.686  54.555  1.00 45.72  ? 330 GLU   B OE1   1 
ATOM   16544 O  OE2   . GLU   F 2  328 ? -1.518  71.801  53.032  1.00 60.11  ? 330 GLU   B OE2   1 
ATOM   16545 N  N     . GLN   F 2  329 ? 1.318   67.695  50.448  1.00 31.93  ? 331 GLN   B N     1 
ATOM   16546 C  CA    . GLN   F 2  329 ? 0.915   66.453  49.803  1.00 29.48  ? 331 GLN   B CA    1 
ATOM   16547 C  C     . GLN   F 2  329 ? 2.081   65.490  49.669  1.00 25.86  ? 331 GLN   B C     1 
ATOM   16548 O  O     . GLN   F 2  329 ? 1.917   64.282  49.879  1.00 25.20  ? 331 GLN   B O     1 
ATOM   16549 C  CB    . GLN   F 2  329 ? 0.284   66.756  48.450  1.00 32.52  ? 331 GLN   B CB    1 
ATOM   16550 C  CG    . GLN   F 2  329 ? -1.232  66.895  48.533  1.00 31.42  ? 331 GLN   B CG    1 
ATOM   16551 C  CD    . GLN   F 2  329 ? -1.897  65.638  49.078  1.00 33.75  ? 331 GLN   B CD    1 
ATOM   16552 O  OE1   . GLN   F 2  329 ? -1.338  64.528  49.019  1.00 40.21  ? 331 GLN   B OE1   1 
ATOM   16553 N  NE2   . GLN   F 2  329 ? -3.090  65.802  49.614  1.00 26.34  ? 331 GLN   B NE2   1 
ATOM   16554 N  N     . MET   F 2  330 ? 3.264   66.006  49.336  1.00 24.56  ? 332 MET   B N     1 
ATOM   16555 C  CA    . MET   F 2  330 ? 4.434   65.134  49.251  1.00 30.32  ? 332 MET   B CA    1 
ATOM   16556 C  C     . MET   F 2  330 ? 4.772   64.525  50.608  1.00 30.73  ? 332 MET   B C     1 
ATOM   16557 O  O     . MET   F 2  330 ? 5.207   63.368  50.689  1.00 30.58  ? 332 MET   B O     1 
ATOM   16558 C  CB    . MET   F 2  330 ? 5.644   65.891  48.685  1.00 27.25  ? 332 MET   B CB    1 
ATOM   16559 C  CG    . MET   F 2  330 ? 5.550   66.267  47.207  1.00 24.34  ? 332 MET   B CG    1 
ATOM   16560 S  SD    . MET   F 2  330 ? 5.422   64.795  46.158  1.00 34.42  ? 332 MET   B SD    1 
ATOM   16561 C  CE    . MET   F 2  330 ? 6.812   63.851  46.751  1.00 29.48  ? 332 MET   B CE    1 
ATOM   16562 N  N     . LEU   F 2  331 ? 4.599   65.288  51.691  1.00 28.30  ? 333 LEU   B N     1 
ATOM   16563 C  CA    . LEU   F 2  331 ? 4.845   64.722  53.015  1.00 23.79  ? 333 LEU   B CA    1 
ATOM   16564 C  C     . LEU   F 2  331 ? 3.900   63.564  53.286  1.00 28.07  ? 333 LEU   B C     1 
ATOM   16565 O  O     . LEU   F 2  331 ? 4.323   62.478  53.689  1.00 27.21  ? 333 LEU   B O     1 
ATOM   16566 C  CB    . LEU   F 2  331 ? 4.710   65.809  54.080  1.00 23.16  ? 333 LEU   B CB    1 
ATOM   16567 C  CG    . LEU   F 2  331 ? 6.046   66.534  54.260  1.00 27.11  ? 333 LEU   B CG    1 
ATOM   16568 C  CD1   . LEU   F 2  331 ? 5.979   67.755  55.176  1.00 19.96  ? 333 LEU   B CD1   1 
ATOM   16569 C  CD2   . LEU   F 2  331 ? 7.085   65.522  54.746  1.00 19.25  ? 333 LEU   B CD2   1 
ATOM   16570 N  N     . ASN   F 2  332 ? 2.609   63.782  53.038  1.00 33.38  ? 334 ASN   B N     1 
ATOM   16571 C  CA    . ASN   F 2  332 ? 1.591   62.782  53.331  1.00 30.43  ? 334 ASN   B CA    1 
ATOM   16572 C  C     . ASN   F 2  332 ? 1.899   61.456  52.643  1.00 32.13  ? 334 ASN   B C     1 
ATOM   16573 O  O     . ASN   F 2  332 ? 1.682   60.385  53.219  1.00 37.90  ? 334 ASN   B O     1 
ATOM   16574 C  CB    . ASN   F 2  332 ? 0.232   63.360  52.916  1.00 38.12  ? 334 ASN   B CB    1 
ATOM   16575 C  CG    . ASN   F 2  332 ? -0.757  62.314  52.506  0.00 37.69  ? 334 ASN   B CG    1 
ATOM   16576 O  OD1   . ASN   F 2  332 ? -1.468  61.773  53.345  1.00 40.96  ? 334 ASN   B OD1   1 
ATOM   16577 N  ND2   . ASN   F 2  332 ? -0.838  62.042  51.202  1.00 38.93  ? 334 ASN   B ND2   1 
ATOM   16578 N  N     . VAL   F 2  333 ? 2.423   61.511  51.414  1.00 37.32  ? 335 VAL   B N     1 
ATOM   16579 C  CA    . VAL   F 2  333 ? 2.800   60.301  50.678  1.00 36.76  ? 335 VAL   B CA    1 
ATOM   16580 C  C     . VAL   F 2  333 ? 3.780   59.472  51.497  1.00 37.25  ? 335 VAL   B C     1 
ATOM   16581 O  O     . VAL   F 2  333 ? 3.525   58.305  51.830  1.00 39.87  ? 335 VAL   B O     1 
ATOM   16582 C  CB    . VAL   F 2  333 ? 3.403   60.671  49.309  1.00 28.10  ? 335 VAL   B CB    1 
ATOM   16583 C  CG1   . VAL   F 2  333 ? 3.513   59.451  48.424  1.00 24.50  ? 335 VAL   B CG1   1 
ATOM   16584 C  CG2   . VAL   F 2  333 ? 2.582   61.744  48.641  1.00 24.85  ? 335 VAL   B CG2   1 
ATOM   16585 N  N     . GLN   F 2  334 ? 4.931   60.068  51.818  1.00 32.30  ? 336 GLN   B N     1 
ATOM   16586 C  CA    . GLN   F 2  334 ? 5.942   59.366  52.601  1.00 39.08  ? 336 GLN   B CA    1 
ATOM   16587 C  C     . GLN   F 2  334 ? 5.425   58.984  53.972  1.00 35.64  ? 336 GLN   B C     1 
ATOM   16588 O  O     . GLN   F 2  334 ? 5.933   58.037  54.579  1.00 39.97  ? 336 GLN   B O     1 
ATOM   16589 C  CB    . GLN   F 2  334 ? 7.196   60.228  52.737  1.00 27.53  ? 336 GLN   B CB    1 
ATOM   16590 C  CG    . GLN   F 2  334 ? 7.217   61.312  51.706  1.00 24.81  ? 336 GLN   B CG    1 
ATOM   16591 C  CD    . GLN   F 2  334 ? 8.471   62.107  51.728  1.00 23.72  ? 336 GLN   B CD    1 
ATOM   16592 O  OE1   . GLN   F 2  334 ? 9.562   61.551  51.815  1.00 27.15  ? 336 GLN   B OE1   1 
ATOM   16593 N  NE2   . GLN   F 2  334 ? 8.340   63.429  51.628  1.00 23.76  ? 336 GLN   B NE2   1 
ATOM   16594 N  N     . ASN   F 2  335 ? 4.417   59.679  54.473  1.00 35.62  ? 337 ASN   B N     1 
ATOM   16595 C  CA    . ASN   F 2  335 ? 4.005   59.375  55.831  1.00 41.92  ? 337 ASN   B CA    1 
ATOM   16596 C  C     . ASN   F 2  335 ? 2.992   58.234  55.875  1.00 39.26  ? 337 ASN   B C     1 
ATOM   16597 O  O     . ASN   F 2  335 ? 2.998   57.449  56.832  1.00 37.78  ? 337 ASN   B O     1 
ATOM   16598 C  CB    . ASN   F 2  335 ? 3.502   60.652  56.505  1.00 33.54  ? 337 ASN   B CB    1 
ATOM   16599 C  CG    . ASN   F 2  335 ? 4.651   61.513  57.040  0.93 39.02  ? 337 ASN   B CG    1 
ATOM   16600 O  OD1   . ASN   F 2  335 ? 5.703   60.982  57.437  1.00 36.63  ? 337 ASN   B OD1   1 
ATOM   16601 N  ND2   . ASN   F 2  335 ? 4.455   62.845  57.061  1.00 39.67  ? 337 ASN   B ND2   1 
ATOM   16602 N  N     . LYS   F 2  336 ? 2.180   58.077  54.832  1.00 34.40  ? 338 LYS   B N     1 
ATOM   16603 C  CA    . LYS   F 2  336 ? 1.188   57.009  54.784  1.00 42.23  ? 338 LYS   B CA    1 
ATOM   16604 C  C     . LYS   F 2  336 ? 1.688   55.738  54.099  1.00 40.58  ? 338 LYS   B C     1 
ATOM   16605 O  O     . LYS   F 2  336 ? 0.989   54.716  54.117  1.00 40.07  ? 338 LYS   B O     1 
ATOM   16606 C  CB    . LYS   F 2  336 ? -0.083  57.528  54.097  1.00 42.87  ? 338 LYS   B CB    1 
ATOM   16607 C  CG    . LYS   F 2  336 ? -1.032  58.215  55.083  1.00 43.87  ? 338 LYS   B CG    1 
ATOM   16608 C  CD    . LYS   F 2  336 ? -1.977  59.188  54.425  1.00 48.37  ? 338 LYS   B CD    1 
ATOM   16609 C  CE    . LYS   F 2  336 ? -3.101  59.518  55.376  1.00 42.49  ? 338 LYS   B CE    1 
ATOM   16610 N  NZ    . LYS   F 2  336 ? -3.844  58.267  55.726  1.00 57.95  ? 338 LYS   B NZ    1 
ATOM   16611 N  N     . ASN   F 2  337 ? 2.876   55.768  53.511  1.00 40.98  ? 339 ASN   B N     1 
ATOM   16612 C  CA    . ASN   F 2  337 ? 3.484   54.598  52.883  1.00 45.60  ? 339 ASN   B CA    1 
ATOM   16613 C  C     . ASN   F 2  337 ? 4.948   54.518  53.244  1.00 43.97  ? 339 ASN   B C     1 
ATOM   16614 O  O     . ASN   F 2  337 ? 5.820   54.344  52.386  1.00 32.88  ? 339 ASN   B O     1 
ATOM   16615 C  CB    . ASN   F 2  337 ? 3.326   54.656  51.384  1.00 38.70  ? 339 ASN   B CB    1 
ATOM   16616 C  CG    . ASN   F 2  337 ? 1.974   55.089  51.000  1.00 40.93  ? 339 ASN   B CG    1 
ATOM   16617 O  OD1   . ASN   F 2  337 ? 1.073   54.265  50.846  1.00 46.22  ? 339 ASN   B OD1   1 
ATOM   16618 N  ND2   . ASN   F 2  337 ? 1.791   56.402  50.877  1.00 32.07  ? 339 ASN   B ND2   1 
ATOM   16619 N  N     . SER   F 2  338 ? 5.225   54.649  54.544  1.00 41.61  ? 340 SER   B N     1 
ATOM   16620 C  CA    . SER   F 2  338 ? 6.574   54.967  54.974  1.00 34.98  ? 340 SER   B CA    1 
ATOM   16621 C  C     . SER   F 2  338 ? 7.491   53.771  54.878  1.00 26.52  ? 340 SER   B C     1 
ATOM   16622 O  O     . SER   F 2  338 ? 8.709   53.949  54.799  1.00 33.15  ? 340 SER   B O     1 
ATOM   16623 C  CB    . SER   F 2  338 ? 6.561   55.513  56.400  1.00 36.60  ? 340 SER   B CB    1 
ATOM   16624 O  OG    . SER   F 2  338 ? 6.319   54.477  57.330  1.00 37.47  ? 340 SER   B OG    1 
ATOM   16625 N  N     . SER   F 2  339 ? 6.948   52.561  54.864  1.00 25.93  ? 341 SER   B N     1 
ATOM   16626 C  CA    . SER   F 2  339 ? 7.834   51.413  54.725  1.00 34.18  ? 341 SER   B CA    1 
ATOM   16627 C  C     . SER   F 2  339 ? 8.375   51.278  53.309  1.00 34.62  ? 341 SER   B C     1 
ATOM   16628 O  O     . SER   F 2  339 ? 9.398   50.619  53.112  1.00 40.42  ? 341 SER   B O     1 
ATOM   16629 C  CB    . SER   F 2  339 ? 7.120   50.128  55.111  1.00 23.92  ? 341 SER   B CB    1 
ATOM   16630 O  OG    . SER   F 2  339 ? 6.243   49.746  54.066  1.00 41.03  ? 341 SER   B OG    1 
ATOM   16631 N  N     . TYR   F 2  340 ? 7.725   51.887  52.325  1.00 24.97  ? 342 TYR   B N     1 
ATOM   16632 C  CA    . TYR   F 2  340 ? 8.201   51.819  50.955  1.00 29.64  ? 342 TYR   B CA    1 
ATOM   16633 C  C     . TYR   F 2  340 ? 9.415   52.712  50.680  1.00 33.13  ? 342 TYR   B C     1 
ATOM   16634 O  O     . TYR   F 2  340 ? 9.830   52.807  49.515  1.00 38.07  ? 342 TYR   B O     1 
ATOM   16635 C  CB    . TYR   F 2  340 ? 7.049   52.154  50.011  1.00 33.40  ? 342 TYR   B CB    1 
ATOM   16636 C  CG    . TYR   F 2  340 ? 6.044   51.041  49.993  1.00 37.36  ? 342 TYR   B CG    1 
ATOM   16637 C  CD1   . TYR   F 2  340 ? 6.459   49.724  49.805  1.00 41.94  ? 342 TYR   B CD1   1 
ATOM   16638 C  CD2   . TYR   F 2  340 ? 4.704   51.279  50.204  1.00 37.35  ? 342 TYR   B CD2   1 
ATOM   16639 C  CE1   . TYR   F 2  340 ? 5.566   48.684  49.808  1.00 35.53  ? 342 TYR   B CE1   1 
ATOM   16640 C  CE2   . TYR   F 2  340 ? 3.790   50.237  50.204  1.00 40.61  ? 342 TYR   B CE2   1 
ATOM   16641 C  CZ    . TYR   F 2  340 ? 4.230   48.943  50.009  1.00 38.60  ? 342 TYR   B CZ    1 
ATOM   16642 O  OH    . TYR   F 2  340 ? 3.331   47.901  50.003  1.00 35.13  ? 342 TYR   B OH    1 
ATOM   16643 N  N     . PHE   F 2  341 ? 9.991   53.351  51.702  1.00 27.18  ? 343 PHE   B N     1 
ATOM   16644 C  CA    . PHE   F 2  341 ? 11.213  54.138  51.583  1.00 22.85  ? 343 PHE   B CA    1 
ATOM   16645 C  C     . PHE   F 2  341 ? 12.210  53.587  52.581  1.00 29.29  ? 343 PHE   B C     1 
ATOM   16646 O  O     . PHE   F 2  341 ? 11.860  53.372  53.745  1.00 39.09  ? 343 PHE   B O     1 
ATOM   16647 C  CB    . PHE   F 2  341 ? 10.966  55.616  51.867  1.00 14.31  ? 343 PHE   B CB    1 
ATOM   16648 C  CG    . PHE   F 2  341 ? 9.906   56.210  51.019  1.00 18.98  ? 343 PHE   B CG    1 
ATOM   16649 C  CD1   . PHE   F 2  341 ? 8.567   56.068  51.359  1.00 29.19  ? 343 PHE   B CD1   1 
ATOM   16650 C  CD2   . PHE   F 2  341 ? 10.233  56.901  49.870  1.00 21.98  ? 343 PHE   B CD2   1 
ATOM   16651 C  CE1   . PHE   F 2  341 ? 7.576   56.614  50.569  1.00 27.03  ? 343 PHE   B CE1   1 
ATOM   16652 C  CE2   . PHE   F 2  341 ? 9.250   57.459  49.049  1.00 19.91  ? 343 PHE   B CE2   1 
ATOM   16653 C  CZ    . PHE   F 2  341 ? 7.923   57.312  49.400  1.00 32.67  ? 343 PHE   B CZ    1 
ATOM   16654 N  N     . VAL   F 2  342 ? 13.444  53.350  52.141  1.00 28.79  ? 344 VAL   B N     1 
ATOM   16655 C  CA    . VAL   F 2  342 ? 14.428  52.827  53.078  1.00 28.46  ? 344 VAL   B CA    1 
ATOM   16656 C  C     . VAL   F 2  342 ? 14.602  53.813  54.231  1.00 26.08  ? 344 VAL   B C     1 
ATOM   16657 O  O     . VAL   F 2  342 ? 14.784  55.021  54.019  1.00 20.30  ? 344 VAL   B O     1 
ATOM   16658 C  CB    . VAL   F 2  342 ? 15.749  52.525  52.355  1.00 20.10  ? 344 VAL   B CB    1 
ATOM   16659 C  CG1   . VAL   F 2  342 ? 15.537  51.395  51.376  1.00 23.01  ? 344 VAL   B CG1   1 
ATOM   16660 C  CG2   . VAL   F 2  342 ? 16.272  53.762  51.659  1.00 19.40  ? 344 VAL   B CG2   1 
ATOM   16661 N  N     . GLU   F 2  343 ? 14.523  53.299  55.467  1.00 25.82  ? 345 GLU   B N     1 
ATOM   16662 C  CA    . GLU   F 2  343 ? 14.775  54.134  56.634  1.00 23.99  ? 345 GLU   B CA    1 
ATOM   16663 C  C     . GLU   F 2  343 ? 16.246  54.483  56.819  1.00 28.78  ? 345 GLU   B C     1 
ATOM   16664 O  O     . GLU   F 2  343 ? 16.537  55.395  57.602  1.00 31.68  ? 345 GLU   B O     1 
ATOM   16665 C  CB    . GLU   F 2  343 ? 14.249  53.481  57.915  1.00 31.40  ? 345 GLU   B CB    1 
ATOM   16666 C  CG    . GLU   F 2  343 ? 15.011  52.311  58.439  1.00 30.09  ? 345 GLU   B CG    1 
ATOM   16667 C  CD    . GLU   F 2  343 ? 14.865  51.118  57.538  1.00 40.65  ? 345 GLU   B CD    1 
ATOM   16668 O  OE1   . GLU   F 2  343 ? 14.632  51.335  56.329  1.00 36.01  ? 345 GLU   B OE1   1 
ATOM   16669 O  OE2   . GLU   F 2  343 ? 14.971  49.970  58.026  1.00 48.69  ? 345 GLU   B OE2   1 
ATOM   16670 N  N     . TRP   F 2  344 ? 17.169  53.818  56.120  1.00 20.76  ? 346 TRP   B N     1 
ATOM   16671 C  CA    . TRP   F 2  344 ? 18.585  54.112  56.273  1.00 20.74  ? 346 TRP   B CA    1 
ATOM   16672 C  C     . TRP   F 2  344 ? 19.101  55.113  55.243  1.00 25.77  ? 346 TRP   B C     1 
ATOM   16673 O  O     . TRP   F 2  344 ? 20.319  55.301  55.126  1.00 24.48  ? 346 TRP   B O     1 
ATOM   16674 C  CB    . TRP   F 2  344 ? 19.407  52.819  56.230  1.00 20.64  ? 346 TRP   B CB    1 
ATOM   16675 C  CG    . TRP   F 2  344 ? 19.039  51.871  55.138  1.00 24.14  ? 346 TRP   B CG    1 
ATOM   16676 C  CD1   . TRP   F 2  344 ? 18.099  50.886  55.193  1.00 22.58  ? 346 TRP   B CD1   1 
ATOM   16677 C  CD2   . TRP   F 2  344 ? 19.599  51.820  53.805  1.00 26.50  ? 346 TRP   B CD2   1 
ATOM   16678 N  NE1   . TRP   F 2  344 ? 18.035  50.233  53.976  1.00 26.93  ? 346 TRP   B NE1   1 
ATOM   16679 C  CE2   . TRP   F 2  344 ? 18.951  50.787  53.118  1.00 22.32  ? 346 TRP   B CE2   1 
ATOM   16680 C  CE3   . TRP   F 2  344 ? 20.575  52.563  53.127  1.00 21.88  ? 346 TRP   B CE3   1 
ATOM   16681 C  CZ2   . TRP   F 2  344 ? 19.267  50.464  51.803  1.00 21.48  ? 346 TRP   B CZ2   1 
ATOM   16682 C  CZ3   . TRP   F 2  344 ? 20.868  52.244  51.816  1.00 15.93  ? 346 TRP   B CZ3   1 
ATOM   16683 C  CH2   . TRP   F 2  344 ? 20.228  51.209  51.176  1.00 18.81  ? 346 TRP   B CH2   1 
ATOM   16684 N  N     . ILE   F 2  345 ? 18.217  55.752  54.493  1.00 25.80  ? 347 ILE   B N     1 
ATOM   16685 C  CA    . ILE   F 2  345 ? 18.513  57.018  53.830  1.00 21.76  ? 347 ILE   B CA    1 
ATOM   16686 C  C     . ILE   F 2  345 ? 17.468  58.025  54.280  1.00 23.91  ? 347 ILE   B C     1 
ATOM   16687 O  O     . ILE   F 2  345 ? 16.360  58.079  53.717  1.00 26.69  ? 347 ILE   B O     1 
ATOM   16688 C  CB    . ILE   F 2  345 ? 18.557  56.898  52.305  1.00 19.74  ? 347 ILE   B CB    1 
ATOM   16689 C  CG1   . ILE   F 2  345 ? 19.456  55.752  51.839  1.00 18.89  ? 347 ILE   B CG1   1 
ATOM   16690 C  CG2   . ILE   F 2  345 ? 19.007  58.230  51.696  1.00 17.95  ? 347 ILE   B CG2   1 
ATOM   16691 C  CD1   . ILE   F 2  345 ? 19.585  55.698  50.308  1.00 16.39  ? 347 ILE   B CD1   1 
ATOM   16692 N  N     . PRO   F 2  346 ? 17.744  58.810  55.300  1.00 21.35  ? 348 PRO   B N     1 
ATOM   16693 C  CA    . PRO   F 2  346 ? 16.783  59.817  55.724  1.00 17.91  ? 348 PRO   B CA    1 
ATOM   16694 C  C     . PRO   F 2  346 ? 16.428  60.785  54.597  1.00 20.03  ? 348 PRO   B C     1 
ATOM   16695 O  O     . PRO   F 2  346 ? 17.239  61.096  53.725  1.00 13.13  ? 348 PRO   B O     1 
ATOM   16696 C  CB    . PRO   F 2  346 ? 17.495  60.518  56.885  1.00 18.52  ? 348 PRO   B CB    1 
ATOM   16697 C  CG    . PRO   F 2  346 ? 18.404  59.453  57.440  1.00 21.43  ? 348 PRO   B CG    1 
ATOM   16698 C  CD    . PRO   F 2  346 ? 18.871  58.673  56.250  1.00 20.93  ? 348 PRO   B CD    1 
ATOM   16699 N  N     . ASN   F 2  347 ? 15.190  61.263  54.633  1.00 22.54  ? 349 ASN   B N     1 
ATOM   16700 C  CA    . ASN   F 2  347 ? 14.770  62.398  53.828  1.00 21.84  ? 349 ASN   B CA    1 
ATOM   16701 C  C     . ASN   F 2  347 ? 15.238  62.230  52.391  1.00 17.40  ? 349 ASN   B C     1 
ATOM   16702 O  O     . ASN   F 2  347 ? 15.876  63.105  51.806  1.00 13.08  ? 349 ASN   B O     1 
ATOM   16703 C  CB    . ASN   F 2  347 ? 15.291  63.713  54.415  1.00 22.40  ? 349 ASN   B CB    1 
ATOM   16704 C  CG    . ASN   F 2  347 ? 15.033  63.843  55.907  1.00 22.85  ? 349 ASN   B CG    1 
ATOM   16705 O  OD1   . ASN   F 2  347 ? 15.960  64.067  56.686  1.00 16.72  ? 349 ASN   B OD1   1 
ATOM   16706 N  ND2   . ASN   F 2  347 ? 13.771  63.699  56.310  1.00 28.93  ? 349 ASN   B ND2   1 
ATOM   16707 N  N     . ASN   F 2  348 ? 14.884  61.078  51.818  1.00 20.84  ? 350 ASN   B N     1 
ATOM   16708 C  CA    . ASN   F 2  348 ? 15.383  60.670  50.512  1.00 19.11  ? 350 ASN   B CA    1 
ATOM   16709 C  C     . ASN   F 2  348 ? 14.447  61.055  49.366  1.00 16.89  ? 350 ASN   B C     1 
ATOM   16710 O  O     . ASN   F 2  348 ? 14.538  60.468  48.282  1.00 23.11  ? 350 ASN   B O     1 
ATOM   16711 C  CB    . ASN   F 2  348 ? 15.676  59.163  50.506  1.00 16.44  ? 350 ASN   B CB    1 
ATOM   16712 C  CG    . ASN   F 2  348 ? 14.430  58.327  50.519  1.00 22.57  ? 350 ASN   B CG    1 
ATOM   16713 O  OD1   . ASN   F 2  348 ? 13.400  58.745  51.040  1.00 25.81  ? 350 ASN   B OD1   1 
ATOM   16714 N  ND2   . ASN   F 2  348 ? 14.503  57.143  49.917  1.00 21.83  ? 350 ASN   B ND2   1 
ATOM   16715 N  N     . VAL   F 2  349 ? 13.578  62.046  49.571  1.00 23.78  ? 351 VAL   B N     1 
ATOM   16716 C  CA    . VAL   F 2  349 ? 12.630  62.524  48.559  1.00 16.96  ? 351 VAL   B CA    1 
ATOM   16717 C  C     . VAL   F 2  349 ? 12.777  64.037  48.457  1.00 21.54  ? 351 VAL   B C     1 
ATOM   16718 O  O     . VAL   F 2  349 ? 12.443  64.760  49.404  1.00 25.69  ? 351 VAL   B O     1 
ATOM   16719 C  CB    . VAL   F 2  349 ? 11.182  62.156  48.903  1.00 15.74  ? 351 VAL   B CB    1 
ATOM   16720 C  CG1   . VAL   F 2  349 ? 10.279  62.516  47.766  1.00 17.38  ? 351 VAL   B CG1   1 
ATOM   16721 C  CG2   . VAL   F 2  349 ? 11.052  60.679  49.258  1.00 18.77  ? 351 VAL   B CG2   1 
ATOM   16722 N  N     . LYS   F 2  350 ? 13.268  64.517  47.314  1.00 25.18  ? 352 LYS   B N     1 
ATOM   16723 C  CA    . LYS   F 2  350 ? 13.452  65.939  47.049  1.00 24.00  ? 352 LYS   B CA    1 
ATOM   16724 C  C     . LYS   F 2  350 ? 12.450  66.402  45.997  1.00 28.34  ? 352 LYS   B C     1 
ATOM   16725 O  O     . LYS   F 2  350 ? 12.186  65.697  45.021  1.00 25.71  ? 352 LYS   B O     1 
ATOM   16726 C  CB    . LYS   F 2  350 ? 14.875  66.250  46.580  1.00 22.77  ? 352 LYS   B CB    1 
ATOM   16727 C  CG    . LYS   F 2  350 ? 15.976  66.031  47.621  1.00 16.76  ? 352 LYS   B CG    1 
ATOM   16728 C  CD    . LYS   F 2  350 ? 15.494  66.203  49.045  1.00 19.22  ? 352 LYS   B CD    1 
ATOM   16729 C  CE    . LYS   F 2  350 ? 16.685  66.439  49.975  1.00 28.47  ? 352 LYS   B CE    1 
ATOM   16730 N  NZ    . LYS   F 2  350 ? 16.515  65.817  51.331  1.00 24.37  ? 352 LYS   B NZ    1 
ATOM   16731 N  N     . THR   F 2  351 ? 11.885  67.590  46.209  1.00 33.80  ? 353 THR   B N     1 
ATOM   16732 C  CA    . THR   F 2  351 ? 10.746  68.067  45.437  1.00 21.87  ? 353 THR   B CA    1 
ATOM   16733 C  C     . THR   F 2  351 ? 11.057  69.440  44.885  1.00 25.69  ? 353 THR   B C     1 
ATOM   16734 O  O     . THR   F 2  351 ? 11.446  70.346  45.628  1.00 33.20  ? 353 THR   B O     1 
ATOM   16735 C  CB    . THR   F 2  351 ? 9.467   68.144  46.276  1.00 20.53  ? 353 THR   B CB    1 
ATOM   16736 O  OG1   . THR   F 2  351 ? 9.297   66.929  47.021  1.00 31.26  ? 353 THR   B OG1   1 
ATOM   16737 C  CG2   . THR   F 2  351 ? 8.244   68.367  45.373  1.00 28.40  ? 353 THR   B CG2   1 
ATOM   16738 N  N     . ALA   F 2  352 ? 10.896  69.584  43.587  1.00 25.94  ? 354 ALA   B N     1 
ATOM   16739 C  CA    . ALA   F 2  352 ? 11.090  70.851  42.928  1.00 20.49  ? 354 ALA   B CA    1 
ATOM   16740 C  C     . ALA   F 2  352 ? 9.759   71.295  42.356  1.00 29.02  ? 354 ALA   B C     1 
ATOM   16741 O  O     . ALA   F 2  352 ? 8.863   70.481  42.107  1.00 27.01  ? 354 ALA   B O     1 
ATOM   16742 C  CB    . ALA   F 2  352 ? 12.150  70.734  41.826  1.00 31.33  ? 354 ALA   B CB    1 
ATOM   16743 N  N     . VAL   F 2  353 ? 9.632   72.603  42.165  1.00 32.39  ? 355 VAL   B N     1 
ATOM   16744 C  CA    . VAL   F 2  353 ? 8.466   73.187  41.523  1.00 28.24  ? 355 VAL   B CA    1 
ATOM   16745 C  C     . VAL   F 2  353 ? 8.948   74.171  40.463  1.00 31.95  ? 355 VAL   B C     1 
ATOM   16746 O  O     . VAL   F 2  353 ? 9.767   75.045  40.753  1.00 40.05  ? 355 VAL   B O     1 
ATOM   16747 C  CB    . VAL   F 2  353 ? 7.531   73.853  42.550  1.00 24.89  ? 355 VAL   B CB    1 
ATOM   16748 C  CG1   . VAL   F 2  353 ? 6.441   74.609  41.856  1.00 28.85  ? 355 VAL   B CG1   1 
ATOM   16749 C  CG2   . VAL   F 2  353 ? 6.897   72.787  43.438  1.00 23.80  ? 355 VAL   B CG2   1 
ATOM   16750 N  N     . CYS   F 2  354 ? 8.482   73.993  39.227  1.00 31.64  ? 356 CYS   B N     1 
ATOM   16751 C  CA    . CYS   F 2  354 ? 8.722   74.927  38.134  1.00 28.90  ? 356 CYS   B CA    1 
ATOM   16752 C  C     . CYS   F 2  354 ? 7.411   75.609  37.778  1.00 29.91  ? 356 CYS   B C     1 
ATOM   16753 O  O     . CYS   F 2  354 ? 6.407   74.933  37.556  1.00 33.31  ? 356 CYS   B O     1 
ATOM   16754 C  CB    . CYS   F 2  354 ? 9.284   74.207  36.911  1.00 28.11  ? 356 CYS   B CB    1 
ATOM   16755 S  SG    . CYS   F 2  354 ? 9.548   75.278  35.468  1.00 45.91  ? 356 CYS   B SG    1 
ATOM   16756 N  N     . ASP   F 2  355 ? 7.411   76.943  37.724  1.00 34.44  ? 357 ASP   B N     1 
ATOM   16757 C  CA    . ASP   F 2  355 ? 6.152   77.646  37.483  1.00 37.49  ? 357 ASP   B CA    1 
ATOM   16758 C  C     . ASP   F 2  355 ? 5.667   77.463  36.053  1.00 39.17  ? 357 ASP   B C     1 
ATOM   16759 O  O     . ASP   F 2  355 ? 4.448   77.449  35.815  1.00 35.69  ? 357 ASP   B O     1 
ATOM   16760 C  CB    . ASP   F 2  355 ? 6.288   79.141  37.776  1.00 42.62  ? 357 ASP   B CB    1 
ATOM   16761 C  CG    . ASP   F 2  355 ? 6.973   79.417  39.090  1.00 62.17  ? 357 ASP   B CG    1 
ATOM   16762 O  OD1   . ASP   F 2  355 ? 8.177   79.069  39.223  1.00 67.36  ? 357 ASP   B OD1   1 
ATOM   16763 O  OD2   . ASP   F 2  355 ? 6.310   79.987  39.984  1.00 64.74  ? 357 ASP   B OD2   1 
ATOM   16764 N  N     . ILE   F 2  356 ? 6.595   77.352  35.100  1.00 34.50  ? 358 ILE   B N     1 
ATOM   16765 C  CA    . ILE   F 2  356 ? 6.288   77.190  33.679  1.00 32.57  ? 358 ILE   B CA    1 
ATOM   16766 C  C     . ILE   F 2  356 ? 5.766   75.788  33.391  1.00 33.62  ? 358 ILE   B C     1 
ATOM   16767 O  O     . ILE   F 2  356 ? 6.489   74.802  33.597  1.00 35.79  ? 358 ILE   B O     1 
ATOM   16768 C  CB    . ILE   F 2  356 ? 7.517   77.467  32.814  1.00 35.21  ? 358 ILE   B CB    1 
ATOM   16769 C  CG1   . ILE   F 2  356 ? 7.922   78.930  32.930  1.00 37.64  ? 358 ILE   B CG1   1 
ATOM   16770 C  CG2   . ILE   F 2  356 ? 7.231   77.047  31.374  1.00 35.20  ? 358 ILE   B CG2   1 
ATOM   16771 C  CD1   . ILE   F 2  356 ? 9.105   79.303  32.044  1.00 41.93  ? 358 ILE   B CD1   1 
ATOM   16772 N  N     . PRO   F 2  357 ? 4.552   75.646  32.880  1.00 29.06  ? 359 PRO   B N     1 
ATOM   16773 C  CA    . PRO   F 2  357 ? 3.990   74.316  32.667  1.00 34.02  ? 359 PRO   B CA    1 
ATOM   16774 C  C     . PRO   F 2  357 ? 4.370   73.770  31.302  1.00 39.41  ? 359 PRO   B C     1 
ATOM   16775 O  O     . PRO   F 2  357 ? 4.854   74.512  30.431  1.00 38.50  ? 359 PRO   B O     1 
ATOM   16776 C  CB    . PRO   F 2  357 ? 2.479   74.557  32.772  1.00 33.73  ? 359 PRO   B CB    1 
ATOM   16777 C  CG    . PRO   F 2  357 ? 2.304   75.930  32.255  1.00 39.93  ? 359 PRO   B CG    1 
ATOM   16778 C  CD    . PRO   F 2  357 ? 3.604   76.704  32.510  1.00 32.85  ? 359 PRO   B CD    1 
ATOM   16779 N  N     . PRO   F 2  358 ? 4.178   72.478  31.075  1.00 42.28  ? 360 PRO   B N     1 
ATOM   16780 C  CA    . PRO   F 2  358 ? 4.449   71.904  29.759  1.00 41.61  ? 360 PRO   B CA    1 
ATOM   16781 C  C     . PRO   F 2  358 ? 3.328   72.280  28.791  1.00 40.80  ? 360 PRO   B C     1 
ATOM   16782 O  O     . PRO   F 2  358 ? 2.338   72.910  29.165  1.00 33.02  ? 360 PRO   B O     1 
ATOM   16783 C  CB    . PRO   F 2  358 ? 4.484   70.406  30.053  1.00 37.64  ? 360 PRO   B CB    1 
ATOM   16784 C  CG    . PRO   F 2  358 ? 3.483   70.246  31.132  1.00 30.08  ? 360 PRO   B CG    1 
ATOM   16785 C  CD    . PRO   F 2  358 ? 3.638   71.468  32.007  1.00 34.70  ? 360 PRO   B CD    1 
ATOM   16786 N  N     . ARG   F 2  359 ? 3.502   71.872  27.532  1.00 53.04  ? 369 ARG   B N     1 
ATOM   16787 C  CA    . ARG   F 2  359 ? 2.555   72.225  26.476  1.00 50.98  ? 369 ARG   B CA    1 
ATOM   16788 C  C     . ARG   F 2  359 ? 1.209   71.566  26.713  1.00 38.95  ? 369 ARG   B C     1 
ATOM   16789 O  O     . ARG   F 2  359 ? 1.127   70.359  26.960  1.00 43.81  ? 369 ARG   B O     1 
ATOM   16790 C  CB    . ARG   F 2  359 ? 3.096   71.816  25.101  1.00 52.69  ? 369 ARG   B CB    1 
ATOM   16791 C  CG    . ARG   F 2  359 ? 2.063   71.867  23.973  1.00 50.79  ? 369 ARG   B CG    1 
ATOM   16792 C  CD    . ARG   F 2  359 ? 2.415   72.876  22.856  1.00 57.43  ? 369 ARG   B CD    1 
ATOM   16793 N  NE    . ARG   F 2  359 ? 2.618   74.232  23.360  1.00 69.10  ? 369 ARG   B NE    1 
ATOM   16794 C  CZ    . ARG   F 2  359 ? 2.646   75.326  22.605  1.00 77.74  ? 369 ARG   B CZ    1 
ATOM   16795 N  NH1   . ARG   F 2  359 ? 2.450   75.266  21.296  1.00 76.49  ? 369 ARG   B NH1   1 
ATOM   16796 N  NH2   . ARG   F 2  359 ? 2.878   76.509  23.179  1.00 63.09  ? 369 ARG   B NH2   1 
ATOM   16797 N  N     . GLY   F 2  360 ? 0.151   72.367  26.646  1.00 33.82  ? 370 GLY   B N     1 
ATOM   16798 C  CA    . GLY   F 2  360 ? -1.196  71.858  26.723  1.00 36.72  ? 370 GLY   B CA    1 
ATOM   16799 C  C     . GLY   F 2  360 ? -1.641  71.372  28.076  1.00 39.34  ? 370 GLY   B C     1 
ATOM   16800 O  O     . GLY   F 2  360 ? -2.810  71.003  28.220  1.00 48.23  ? 370 GLY   B O     1 
ATOM   16801 N  N     . LEU   F 2  361 ? -0.753  71.327  29.065  1.00 38.85  ? 371 LEU   B N     1 
ATOM   16802 C  CA    . LEU   F 2  361 ? -1.112  71.026  30.441  1.00 33.49  ? 371 LEU   B CA    1 
ATOM   16803 C  C     . LEU   F 2  361 ? -0.986  72.297  31.267  1.00 34.58  ? 371 LEU   B C     1 
ATOM   16804 O  O     . LEU   F 2  361 ? -0.066  73.097  31.056  1.00 46.22  ? 371 LEU   B O     1 
ATOM   16805 C  CB    . LEU   F 2  361 ? -0.235  69.904  31.013  1.00 37.19  ? 371 LEU   B CB    1 
ATOM   16806 C  CG    . LEU   F 2  361 ? -0.437  68.482  30.451  1.00 36.89  ? 371 LEU   B CG    1 
ATOM   16807 C  CD1   . LEU   F 2  361 ? -1.107  67.571  31.441  1.00 29.07  ? 371 LEU   B CD1   1 
ATOM   16808 C  CD2   . LEU   F 2  361 ? -1.244  68.492  29.158  1.00 44.62  ? 371 LEU   B CD2   1 
ATOM   16809 N  N     . LYS   F 2  362 ? -1.966  72.517  32.150  1.00 36.88  ? 372 LYS   B N     1 
ATOM   16810 C  CA    . LYS   F 2  362 ? -1.867  73.526  33.204  1.00 35.55  ? 372 LYS   B CA    1 
ATOM   16811 C  C     . LYS   F 2  362 ? -1.117  72.998  34.414  1.00 34.60  ? 372 LYS   B C     1 
ATOM   16812 O  O     . LYS   F 2  362 ? -0.661  73.783  35.244  1.00 33.50  ? 372 LYS   B O     1 
ATOM   16813 C  CB    . LYS   F 2  362 ? -3.262  73.978  33.683  1.00 38.82  ? 372 LYS   B CB    1 
ATOM   16814 C  CG    . LYS   F 2  362 ? -4.083  74.853  32.734  1.00 48.48  ? 372 LYS   B CG    1 
ATOM   16815 C  CD    . LYS   F 2  362 ? -5.476  75.132  33.328  1.00 49.75  ? 372 LYS   B CD    1 
ATOM   16816 C  CE    . LYS   F 2  362 ? -6.605  75.100  32.273  1.00 51.03  ? 372 LYS   B CE    1 
ATOM   16817 N  NZ    . LYS   F 2  362 ? -7.094  76.455  31.822  1.00 51.50  ? 372 LYS   B NZ    1 
ATOM   16818 N  N     . MET   F 2  363 ? -1.015  71.681  34.543  1.00 41.87  ? 373 MET   B N     1 
ATOM   16819 C  CA    . MET   F 2  363 ? -0.528  71.059  35.765  1.00 32.88  ? 373 MET   B CA    1 
ATOM   16820 C  C     . MET   F 2  363 ? 0.005   69.690  35.401  1.00 34.41  ? 373 MET   B C     1 
ATOM   16821 O  O     . MET   F 2  363 ? -0.730  68.887  34.827  1.00 41.46  ? 373 MET   B O     1 
ATOM   16822 C  CB    . MET   F 2  363 ? -1.651  70.935  36.778  1.00 33.88  ? 373 MET   B CB    1 
ATOM   16823 C  CG    . MET   F 2  363 ? -2.201  72.252  37.255  1.00 42.05  ? 373 MET   B CG    1 
ATOM   16824 S  SD    . MET   F 2  363 ? -1.424  72.764  38.792  1.00 50.61  ? 373 MET   B SD    1 
ATOM   16825 C  CE    . MET   F 2  363 ? -1.996  71.483  39.899  1.00 27.72  ? 373 MET   B CE    1 
ATOM   16826 N  N     . SER   F 2  364 ? 1.262   69.420  35.725  1.00 33.75  ? 374 SER   B N     1 
ATOM   16827 C  CA    . SER   F 2  364 ? 1.811   68.086  35.542  1.00 32.36  ? 374 SER   B CA    1 
ATOM   16828 C  C     . SER   F 2  364 ? 2.759   67.774  36.688  1.00 29.20  ? 374 SER   B C     1 
ATOM   16829 O  O     . SER   F 2  364 ? 3.228   68.666  37.396  1.00 26.08  ? 374 SER   B O     1 
ATOM   16830 C  CB    . SER   F 2  364 ? 2.542   67.939  34.191  1.00 29.83  ? 374 SER   B CB    1 
ATOM   16831 O  OG    . SER   F 2  364 ? 3.559   68.920  34.037  1.00 32.16  ? 374 SER   B OG    1 
ATOM   16832 N  N     . ALA   F 2  365 ? 3.043   66.490  36.861  1.00 28.62  ? 375 ALA   B N     1 
ATOM   16833 C  CA    . ALA   F 2  365 ? 4.112   66.068  37.752  1.00 29.67  ? 375 ALA   B CA    1 
ATOM   16834 C  C     . ALA   F 2  365 ? 4.952   65.007  37.054  1.00 28.48  ? 375 ALA   B C     1 
ATOM   16835 O  O     . ALA   F 2  365 ? 4.451   64.225  36.234  1.00 28.65  ? 375 ALA   B O     1 
ATOM   16836 C  CB    . ALA   F 2  365 ? 3.571   65.536  39.085  1.00 30.48  ? 375 ALA   B CB    1 
ATOM   16837 N  N     . THR   F 2  366 ? 6.248   65.001  37.378  1.00 30.20  ? 376 THR   B N     1 
ATOM   16838 C  CA    . THR   F 2  366 ? 7.196   64.017  36.864  1.00 27.16  ? 376 THR   B CA    1 
ATOM   16839 C  C     . THR   F 2  366 ? 7.969   63.433  38.034  1.00 23.01  ? 376 THR   B C     1 
ATOM   16840 O  O     . THR   F 2  366 ? 8.438   64.170  38.904  1.00 21.13  ? 376 THR   B O     1 
ATOM   16841 C  CB    . THR   F 2  366 ? 8.156   64.614  35.833  1.00 25.36  ? 376 THR   B CB    1 
ATOM   16842 O  OG1   . THR   F 2  366 ? 7.411   65.130  34.718  1.00 24.65  ? 376 THR   B OG1   1 
ATOM   16843 C  CG2   . THR   F 2  366 ? 9.099   63.545  35.347  1.00 19.20  ? 376 THR   B CG2   1 
ATOM   16844 N  N     . PHE   F 2  367 ? 8.081   62.106  38.044  1.00 24.86  ? 377 PHE   B N     1 
ATOM   16845 C  CA    . PHE   F 2  367 ? 8.606   61.319  39.149  1.00 24.83  ? 377 PHE   B CA    1 
ATOM   16846 C  C     . PHE   F 2  367 ? 9.858   60.597  38.662  1.00 24.68  ? 377 PHE   B C     1 
ATOM   16847 O  O     . PHE   F 2  367 ? 9.860   60.034  37.565  1.00 24.09  ? 377 PHE   B O     1 
ATOM   16848 C  CB    . PHE   F 2  367 ? 7.506   60.343  39.644  1.00 30.68  ? 377 PHE   B CB    1 
ATOM   16849 C  CG    . PHE   F 2  367 ? 7.999   59.179  40.523  1.00 28.49  ? 377 PHE   B CG    1 
ATOM   16850 C  CD1   . PHE   F 2  367 ? 8.402   57.975  39.952  1.00 23.67  ? 377 PHE   B CD1   1 
ATOM   16851 C  CD2   . PHE   F 2  367 ? 7.983   59.270  41.912  1.00 25.27  ? 377 PHE   B CD2   1 
ATOM   16852 C  CE1   . PHE   F 2  367 ? 8.845   56.914  40.747  1.00 27.24  ? 377 PHE   B CE1   1 
ATOM   16853 C  CE2   . PHE   F 2  367 ? 8.417   58.202  42.717  1.00 24.56  ? 377 PHE   B CE2   1 
ATOM   16854 C  CZ    . PHE   F 2  367 ? 8.848   57.026  42.131  1.00 22.40  ? 377 PHE   B CZ    1 
ATOM   16855 N  N     . ILE   F 2  368 ? 10.929  60.636  39.453  1.00 20.24  ? 378 ILE   B N     1 
ATOM   16856 C  CA    . ILE   F 2  368 ? 12.152  59.888  39.156  1.00 22.47  ? 378 ILE   B CA    1 
ATOM   16857 C  C     . ILE   F 2  368 ? 12.470  59.054  40.391  1.00 25.52  ? 378 ILE   B C     1 
ATOM   16858 O  O     . ILE   F 2  368 ? 12.898  59.593  41.418  1.00 19.46  ? 378 ILE   B O     1 
ATOM   16859 C  CB    . ILE   F 2  368 ? 13.335  60.802  38.792  1.00 18.27  ? 378 ILE   B CB    1 
ATOM   16860 C  CG1   . ILE   F 2  368 ? 13.029  61.638  37.560  1.00 15.19  ? 378 ILE   B CG1   1 
ATOM   16861 C  CG2   . ILE   F 2  368 ? 14.577  59.997  38.576  1.00 12.20  ? 378 ILE   B CG2   1 
ATOM   16862 C  CD1   . ILE   F 2  368 ? 13.840  62.882  37.508  1.00 15.49  ? 378 ILE   B CD1   1 
ATOM   16863 N  N     . GLY   F 2  369 ? 12.243  57.748  40.306  1.00 27.07  ? 379 GLY   B N     1 
ATOM   16864 C  CA    . GLY   F 2  369 ? 12.424  56.853  41.434  1.00 16.49  ? 379 GLY   B CA    1 
ATOM   16865 C  C     . GLY   F 2  369 ? 13.635  55.968  41.215  1.00 21.77  ? 379 GLY   B C     1 
ATOM   16866 O  O     . GLY   F 2  369 ? 13.846  55.440  40.119  1.00 24.79  ? 379 GLY   B O     1 
ATOM   16867 N  N     . ASN   F 2  370 ? 14.447  55.840  42.257  1.00 19.28  ? 380 ASN   B N     1 
ATOM   16868 C  CA    . ASN   F 2  370 ? 15.514  54.862  42.285  1.00 16.45  ? 380 ASN   B CA    1 
ATOM   16869 C  C     . ASN   F 2  370 ? 15.012  53.781  43.225  1.00 21.39  ? 380 ASN   B C     1 
ATOM   16870 O  O     . ASN   F 2  370 ? 15.298  53.796  44.420  1.00 27.08  ? 380 ASN   B O     1 
ATOM   16871 C  CB    . ASN   F 2  370 ? 16.822  55.478  42.760  1.00 20.33  ? 380 ASN   B CB    1 
ATOM   16872 C  CG    . ASN   F 2  370 ? 18.024  54.510  42.656  1.00 24.01  ? 380 ASN   B CG    1 
ATOM   16873 O  OD1   . ASN   F 2  370 ? 17.868  53.294  42.428  1.00 21.51  ? 380 ASN   B OD1   1 
ATOM   16874 N  ND2   . ASN   F 2  370 ? 19.234  55.059  42.841  1.00 18.19  ? 380 ASN   B ND2   1 
ATOM   16875 N  N     . SER   F 2  371 ? 14.200  52.872  42.698  1.00 18.47  ? 381 SER   B N     1 
ATOM   16876 C  CA    . SER   F 2  371 ? 13.583  51.854  43.534  1.00 22.07  ? 381 SER   B CA    1 
ATOM   16877 C  C     . SER   F 2  371 ? 14.209  50.492  43.284  1.00 23.78  ? 381 SER   B C     1 
ATOM   16878 O  O     . SER   F 2  371 ? 14.455  50.113  42.134  1.00 25.11  ? 381 SER   B O     1 
ATOM   16879 C  CB    . SER   F 2  371 ? 12.086  51.759  43.285  1.00 25.18  ? 381 SER   B CB    1 
ATOM   16880 O  OG    . SER   F 2  371 ? 11.631  50.441  43.575  1.00 30.63  ? 381 SER   B OG    1 
ATOM   16881 N  N     . THR   F 2  372 ? 14.454  49.751  44.369  1.00 20.65  ? 382 THR   B N     1 
ATOM   16882 C  CA    . THR   F 2  372 ? 14.894  48.370  44.212  1.00 25.56  ? 382 THR   B CA    1 
ATOM   16883 C  C     . THR   F 2  372 ? 13.925  47.535  43.394  1.00 21.52  ? 382 THR   B C     1 
ATOM   16884 O  O     . THR   F 2  372 ? 14.286  46.431  42.979  1.00 23.97  ? 382 THR   B O     1 
ATOM   16885 C  CB    . THR   F 2  372 ? 15.104  47.701  45.571  1.00 25.10  ? 382 THR   B CB    1 
ATOM   16886 O  OG1   . THR   F 2  372 ? 13.906  47.805  46.351  1.00 32.00  ? 382 THR   B OG1   1 
ATOM   16887 C  CG2   . THR   F 2  372 ? 16.255  48.360  46.301  1.00 21.11  ? 382 THR   B CG2   1 
ATOM   16888 N  N     . ALA   F 2  373 ? 12.713  48.024  43.153  1.00 21.95  ? 383 ALA   B N     1 
ATOM   16889 C  CA    . ALA   F 2  373 ? 11.744  47.248  42.400  1.00 20.42  ? 383 ALA   B CA    1 
ATOM   16890 C  C     . ALA   F 2  373 ? 12.080  47.165  40.922  1.00 21.07  ? 383 ALA   B C     1 
ATOM   16891 O  O     . ALA   F 2  373 ? 11.393  46.457  40.195  1.00 20.75  ? 383 ALA   B O     1 
ATOM   16892 C  CB    . ALA   F 2  373 ? 10.359  47.851  42.581  1.00 24.92  ? 383 ALA   B CB    1 
ATOM   16893 N  N     . ILE   F 2  374 ? 13.101  47.887  40.452  1.00 27.95  ? 384 ILE   B N     1 
ATOM   16894 C  CA    . ILE   F 2  374 ? 13.472  47.801  39.044  1.00 21.98  ? 384 ILE   B CA    1 
ATOM   16895 C  C     . ILE   F 2  374 ? 14.213  46.512  38.722  1.00 24.12  ? 384 ILE   B C     1 
ATOM   16896 O  O     . ILE   F 2  374 ? 14.326  46.146  37.547  1.00 18.87  ? 384 ILE   B O     1 
ATOM   16897 C  CB    . ILE   F 2  374 ? 14.301  49.024  38.620  1.00 15.22  ? 384 ILE   B CB    1 
ATOM   16898 C  CG1   . ILE   F 2  374 ? 14.142  49.228  37.113  1.00 15.40  ? 384 ILE   B CG1   1 
ATOM   16899 C  CG2   . ILE   F 2  374 ? 15.748  48.820  38.973  1.00 16.41  ? 384 ILE   B CG2   1 
ATOM   16900 C  CD1   . ILE   F 2  374 ? 14.839  50.402  36.587  1.00 16.19  ? 384 ILE   B CD1   1 
ATOM   16901 N  N     . GLN   F 2  375 ? 14.711  45.799  39.734  1.00 29.08  ? 385 GLN   B N     1 
ATOM   16902 C  CA    . GLN   F 2  375 ? 15.180  44.438  39.505  1.00 25.60  ? 385 GLN   B CA    1 
ATOM   16903 C  C     . GLN   F 2  375 ? 14.149  43.605  38.752  1.00 26.59  ? 385 GLN   B C     1 
ATOM   16904 O  O     . GLN   F 2  375 ? 14.511  42.634  38.080  1.00 28.85  ? 385 GLN   B O     1 
ATOM   16905 C  CB    . GLN   F 2  375 ? 15.526  43.759  40.831  1.00 25.31  ? 385 GLN   B CB    1 
ATOM   16906 C  CG    . GLN   F 2  375 ? 14.317  43.250  41.615  1.00 27.66  ? 385 GLN   B CG    1 
ATOM   16907 C  CD    . GLN   F 2  375 ? 14.728  42.465  42.846  1.00 37.74  ? 385 GLN   B CD    1 
ATOM   16908 O  OE1   . GLN   F 2  375 ? 15.452  41.476  42.745  1.00 45.39  ? 385 GLN   B OE1   1 
ATOM   16909 N  NE2   . GLN   F 2  375 ? 14.285  42.911  44.020  1.00 34.43  ? 385 GLN   B NE2   1 
ATOM   16910 N  N     . GLU   F 2  376 ? 12.862  43.940  38.870  1.00 23.74  ? 386 GLU   B N     1 
ATOM   16911 C  CA    . GLU   F 2  376 ? 11.857  43.188  38.126  1.00 21.56  ? 386 GLU   B CA    1 
ATOM   16912 C  C     . GLU   F 2  376 ? 12.102  43.287  36.626  1.00 22.86  ? 386 GLU   B C     1 
ATOM   16913 O  O     . GLU   F 2  376 ? 11.922  42.304  35.901  1.00 18.56  ? 386 GLU   B O     1 
ATOM   16914 C  CB    . GLU   F 2  376 ? 10.449  43.674  38.482  1.00 16.60  ? 386 GLU   B CB    1 
ATOM   16915 C  CG    . GLU   F 2  376 ? 9.967   43.196  39.863  1.00 15.54  ? 386 GLU   B CG    1 
ATOM   16916 C  CD    . GLU   F 2  376 ? 8.493   43.477  40.098  1.00 31.43  ? 386 GLU   B CD    1 
ATOM   16917 O  OE1   . GLU   F 2  376 ? 7.848   44.085  39.198  1.00 32.10  ? 386 GLU   B OE1   1 
ATOM   16918 O  OE2   . GLU   F 2  376 ? 7.982   43.067  41.175  1.00 31.07  ? 386 GLU   B OE2   1 
ATOM   16919 N  N     . LEU   F 2  377 ? 12.525  44.472  36.150  1.00 25.44  ? 387 LEU   B N     1 
ATOM   16920 C  CA    . LEU   F 2  377 ? 12.740  44.713  34.721  1.00 21.99  ? 387 LEU   B CA    1 
ATOM   16921 C  C     . LEU   F 2  377 ? 13.937  43.925  34.203  1.00 24.25  ? 387 LEU   B C     1 
ATOM   16922 O  O     . LEU   F 2  377 ? 13.835  43.205  33.204  1.00 24.07  ? 387 LEU   B O     1 
ATOM   16923 C  CB    . LEU   F 2  377 ? 12.929  46.217  34.461  1.00 16.88  ? 387 LEU   B CB    1 
ATOM   16924 C  CG    . LEU   F 2  377 ? 13.483  46.653  33.103  1.00 14.50  ? 387 LEU   B CG    1 
ATOM   16925 C  CD1   . LEU   F 2  377 ? 12.787  45.861  32.104  1.00 21.10  ? 387 LEU   B CD1   1 
ATOM   16926 C  CD2   . LEU   F 2  377 ? 13.270  48.143  32.781  1.00 15.02  ? 387 LEU   B CD2   1 
ATOM   16927 N  N     . PHE   F 2  378 ? 15.087  44.054  34.867  1.00 25.53  ? 388 PHE   B N     1 
ATOM   16928 C  CA    . PHE   F 2  378 ? 16.248  43.269  34.470  1.00 19.46  ? 388 PHE   B CA    1 
ATOM   16929 C  C     . PHE   F 2  378 ? 15.947  41.790  34.558  1.00 16.46  ? 388 PHE   B C     1 
ATOM   16930 O  O     . PHE   F 2  378 ? 16.410  41.010  33.729  1.00 23.52  ? 388 PHE   B O     1 
ATOM   16931 C  CB    . PHE   F 2  378 ? 17.449  43.660  35.329  1.00 15.49  ? 388 PHE   B CB    1 
ATOM   16932 C  CG    . PHE   F 2  378 ? 17.791  45.114  35.218  1.00 18.91  ? 388 PHE   B CG    1 
ATOM   16933 C  CD1   . PHE   F 2  378 ? 18.176  45.657  33.984  1.00 21.04  ? 388 PHE   B CD1   1 
ATOM   16934 C  CD2   . PHE   F 2  378 ? 17.687  45.959  36.311  1.00 16.81  ? 388 PHE   B CD2   1 
ATOM   16935 C  CE1   . PHE   F 2  378 ? 18.490  47.009  33.858  1.00 16.33  ? 388 PHE   B CE1   1 
ATOM   16936 C  CE2   . PHE   F 2  378 ? 17.992  47.319  36.183  1.00 20.10  ? 388 PHE   B CE2   1 
ATOM   16937 C  CZ    . PHE   F 2  378 ? 18.402  47.837  34.962  1.00 15.84  ? 388 PHE   B CZ    1 
ATOM   16938 N  N     . LYS   F 2  379 ? 15.144  41.391  35.527  1.00 18.27  ? 389 LYS   B N     1 
ATOM   16939 C  CA    . LYS   F 2  379 ? 14.767  39.990  35.625  1.00 24.84  ? 389 LYS   B CA    1 
ATOM   16940 C  C     . LYS   F 2  379 ? 13.954  39.557  34.416  1.00 24.75  ? 389 LYS   B C     1 
ATOM   16941 O  O     . LYS   F 2  379 ? 14.113  38.438  33.919  1.00 27.95  ? 389 LYS   B O     1 
ATOM   16942 C  CB    . LYS   F 2  379 ? 13.980  39.748  36.910  1.00 26.65  ? 389 LYS   B CB    1 
ATOM   16943 C  CG    . LYS   F 2  379 ? 14.708  38.892  37.896  1.00 34.65  ? 389 LYS   B CG    1 
ATOM   16944 C  CD    . LYS   F 2  379 ? 13.867  38.605  39.124  1.00 42.35  ? 389 LYS   B CD    1 
ATOM   16945 C  CE    . LYS   F 2  379 ? 13.959  39.714  40.144  1.00 36.98  ? 389 LYS   B CE    1 
ATOM   16946 N  NZ    . LYS   F 2  379 ? 14.124  39.116  41.498  1.00 57.47  ? 389 LYS   B NZ    1 
ATOM   16947 N  N     . ARG   F 2  380 ? 13.056  40.420  33.947  1.00 23.52  ? 390 ARG   B N     1 
ATOM   16948 C  CA    . ARG   F 2  380 ? 12.267  40.081  32.774  1.00 20.37  ? 390 ARG   B CA    1 
ATOM   16949 C  C     . ARG   F 2  380 ? 13.169  39.811  31.594  1.00 25.49  ? 390 ARG   B C     1 
ATOM   16950 O  O     . ARG   F 2  380 ? 13.033  38.789  30.911  1.00 27.38  ? 390 ARG   B O     1 
ATOM   16951 C  CB    . ARG   F 2  380 ? 11.298  41.205  32.414  1.00 23.33  ? 390 ARG   B CB    1 
ATOM   16952 C  CG    . ARG   F 2  380 ? 10.533  40.856  31.157  1.00 16.57  ? 390 ARG   B CG    1 
ATOM   16953 C  CD    . ARG   F 2  380 ? 9.497   41.840  30.823  1.00 17.12  ? 390 ARG   B CD    1 
ATOM   16954 N  NE    . ARG   F 2  380 ? 10.026  42.923  30.000  1.00 23.77  ? 390 ARG   B NE    1 
ATOM   16955 C  CZ    . ARG   F 2  380 ? 9.954   44.201  30.337  1.00 18.54  ? 390 ARG   B CZ    1 
ATOM   16956 N  NH1   . ARG   F 2  380 ? 9.451   44.581  31.497  1.00 27.70  ? 390 ARG   B NH1   1 
ATOM   16957 N  NH2   . ARG   F 2  380 ? 10.374  45.120  29.484  1.00 25.92  ? 390 ARG   B NH2   1 
ATOM   16958 N  N     . ILE   F 2  381 ? 14.085  40.743  31.323  1.00 23.45  ? 391 ILE   B N     1 
ATOM   16959 C  CA    . ILE   F 2  381 ? 15.030  40.555  30.237  1.00 20.18  ? 391 ILE   B CA    1 
ATOM   16960 C  C     . ILE   F 2  381 ? 15.847  39.298  30.477  1.00 28.10  ? 391 ILE   B C     1 
ATOM   16961 O  O     . ILE   F 2  381 ? 15.965  38.436  29.590  1.00 30.06  ? 391 ILE   B O     1 
ATOM   16962 C  CB    . ILE   F 2  381 ? 15.925  41.788  30.092  1.00 22.08  ? 391 ILE   B CB    1 
ATOM   16963 C  CG1   . ILE   F 2  381 ? 15.126  42.954  29.526  1.00 17.90  ? 391 ILE   B CG1   1 
ATOM   16964 C  CG2   . ILE   F 2  381 ? 17.123  41.452  29.227  1.00 27.24  ? 391 ILE   B CG2   1 
ATOM   16965 C  CD1   . ILE   F 2  381 ? 15.840  44.251  29.683  1.00 17.76  ? 391 ILE   B CD1   1 
ATOM   16966 N  N     . SER   F 2  382 ? 16.385  39.153  31.700  1.00 21.15  ? 392 SER   B N     1 
ATOM   16967 C  CA    . SER   F 2  382 ? 17.291  38.039  32.001  1.00 27.62  ? 392 SER   B CA    1 
ATOM   16968 C  C     . SER   F 2  382 ? 16.643  36.680  31.743  1.00 30.80  ? 392 SER   B C     1 
ATOM   16969 O  O     . SER   F 2  382 ? 17.313  35.737  31.313  1.00 27.81  ? 392 SER   B O     1 
ATOM   16970 C  CB    . SER   F 2  382 ? 17.777  38.111  33.450  1.00 28.05  ? 392 SER   B CB    1 
ATOM   16971 O  OG    . SER   F 2  382 ? 18.623  37.001  33.759  1.00 33.09  ? 392 SER   B OG    1 
ATOM   16972 N  N     . GLU   F 2  383 ? 15.346  36.550  32.007  1.00 35.93  ? 393 GLU   B N     1 
ATOM   16973 C  CA    . GLU   F 2  383 ? 14.723  35.251  31.805  1.00 30.76  ? 393 GLU   B CA    1 
ATOM   16974 C  C     . GLU   F 2  383 ? 14.536  34.947  30.332  1.00 24.86  ? 393 GLU   B C     1 
ATOM   16975 O  O     . GLU   F 2  383 ? 14.659  33.784  29.928  1.00 30.04  ? 393 GLU   B O     1 
ATOM   16976 C  CB    . GLU   F 2  383 ? 13.406  35.173  32.566  1.00 41.51  ? 393 GLU   B CB    1 
ATOM   16977 C  CG    . GLU   F 2  383 ? 13.573  34.552  33.966  1.00 48.10  ? 393 GLU   B CG    1 
ATOM   16978 C  CD    . GLU   F 2  383 ? 12.859  35.344  35.059  1.00 60.72  ? 393 GLU   B CD    1 
ATOM   16979 O  OE1   . GLU   F 2  383 ? 13.452  35.515  36.162  1.00 76.99  ? 393 GLU   B OE1   1 
ATOM   16980 O  OE2   . GLU   F 2  383 ? 11.719  35.801  34.818  1.00 71.24  ? 393 GLU   B OE2   1 
ATOM   16981 N  N     . GLN   F 2  384 ? 14.283  35.969  29.504  1.00 30.48  ? 394 GLN   B N     1 
ATOM   16982 C  CA    . GLN   F 2  384 ? 14.205  35.732  28.060  1.00 26.98  ? 394 GLN   B CA    1 
ATOM   16983 C  C     . GLN   F 2  384 ? 15.572  35.328  27.515  1.00 29.58  ? 394 GLN   B C     1 
ATOM   16984 O  O     . GLN   F 2  384 ? 15.703  34.320  26.804  1.00 26.10  ? 394 GLN   B O     1 
ATOM   16985 C  CB    . GLN   F 2  384 ? 13.675  36.970  27.334  1.00 18.12  ? 394 GLN   B CB    1 
ATOM   16986 C  CG    . GLN   F 2  384 ? 12.654  37.832  28.099  1.00 22.77  ? 394 GLN   B CG    1 
ATOM   16987 C  CD    . GLN   F 2  384 ? 12.058  38.979  27.246  1.00 30.01  ? 394 GLN   B CD    1 
ATOM   16988 O  OE1   . GLN   F 2  384 ? 11.617  38.750  26.118  1.00 44.10  ? 394 GLN   B OE1   1 
ATOM   16989 N  NE2   . GLN   F 2  384 ? 12.054  40.213  27.783  1.00 26.68  ? 394 GLN   B NE2   1 
ATOM   16990 N  N     . PHE   F 2  385 ? 16.608  36.094  27.874  1.00 26.52  ? 395 PHE   B N     1 
ATOM   16991 C  CA    . PHE   F 2  385 ? 17.986  35.758  27.528  1.00 22.70  ? 395 PHE   B CA    1 
ATOM   16992 C  C     . PHE   F 2  385 ? 18.304  34.296  27.846  1.00 24.11  ? 395 PHE   B C     1 
ATOM   16993 O  O     . PHE   F 2  385 ? 18.598  33.499  26.954  1.00 25.43  ? 395 PHE   B O     1 
ATOM   16994 C  CB    . PHE   F 2  385 ? 18.912  36.717  28.284  1.00 23.21  ? 395 PHE   B CB    1 
ATOM   16995 C  CG    . PHE   F 2  385 ? 20.383  36.443  28.112  1.00 20.64  ? 395 PHE   B CG    1 
ATOM   16996 C  CD1   . PHE   F 2  385 ? 20.990  35.382  28.752  1.00 22.54  ? 395 PHE   B CD1   1 
ATOM   16997 C  CD2   . PHE   F 2  385 ? 21.165  37.282  27.351  1.00 15.01  ? 395 PHE   B CD2   1 
ATOM   16998 C  CE1   . PHE   F 2  385 ? 22.347  35.158  28.589  1.00 23.10  ? 395 PHE   B CE1   1 
ATOM   16999 C  CE2   . PHE   F 2  385 ? 22.499  37.052  27.193  1.00 12.31  ? 395 PHE   B CE2   1 
ATOM   17000 C  CZ    . PHE   F 2  385 ? 23.095  36.007  27.813  1.00 13.62  ? 395 PHE   B CZ    1 
ATOM   17001 N  N     . THR   F 2  386 ? 18.259  33.932  29.131  1.00 30.41  ? 396 THR   B N     1 
ATOM   17002 C  CA    . THR   F 2  386 ? 18.531  32.556  29.550  1.00 29.95  ? 396 THR   B CA    1 
ATOM   17003 C  C     . THR   F 2  386 ? 17.782  31.537  28.700  1.00 26.17  ? 396 THR   B C     1 
ATOM   17004 O  O     . THR   F 2  386 ? 18.366  30.539  28.272  1.00 20.48  ? 396 THR   B O     1 
ATOM   17005 C  CB    . THR   F 2  386 ? 18.161  32.384  31.025  1.00 22.69  ? 396 THR   B CB    1 
ATOM   17006 O  OG1   . THR   F 2  386 ? 19.085  33.136  31.815  1.00 40.04  ? 396 THR   B OG1   1 
ATOM   17007 C  CG2   . THR   F 2  386 ? 18.239  30.919  31.441  1.00 28.13  ? 396 THR   B CG2   1 
ATOM   17008 N  N     . ALA   F 2  387 ? 16.480  31.761  28.467  1.00 28.12  ? 397 ALA   B N     1 
ATOM   17009 C  CA    . ALA   F 2  387 ? 15.659  30.760  27.787  1.00 30.79  ? 397 ALA   B CA    1 
ATOM   17010 C  C     . ALA   F 2  387 ? 16.323  30.258  26.525  1.00 27.52  ? 397 ALA   B C     1 
ATOM   17011 O  O     . ALA   F 2  387 ? 16.183  29.085  26.163  1.00 32.84  ? 397 ALA   B O     1 
ATOM   17012 C  CB    . ALA   F 2  387 ? 14.288  31.326  27.428  1.00 27.51  ? 397 ALA   B CB    1 
ATOM   17013 N  N     . MET   F 2  388 ? 17.054  31.121  25.851  1.00 17.23  ? 398 MET   B N     1 
ATOM   17014 C  CA    . MET   F 2  388 ? 17.624  30.763  24.582  1.00 20.17  ? 398 MET   B CA    1 
ATOM   17015 C  C     . MET   F 2  388 ? 19.139  30.790  24.581  1.00 20.88  ? 398 MET   B C     1 
ATOM   17016 O  O     . MET   F 2  388 ? 19.740  30.206  23.676  1.00 22.17  ? 398 MET   B O     1 
ATOM   17017 C  CB    . MET   F 2  388 ? 17.058  31.677  23.471  1.00 21.21  ? 398 MET   B CB    1 
ATOM   17018 C  CG    . MET   F 2  388 ? 17.771  32.983  23.241  1.00 17.50  ? 398 MET   B CG    1 
ATOM   17019 S  SD    . MET   F 2  388 ? 16.758  34.303  22.563  1.00 19.52  ? 398 MET   B SD    1 
ATOM   17020 C  CE    . MET   F 2  388 ? 16.091  33.543  21.084  1.00 14.01  ? 398 MET   B CE    1 
ATOM   17021 N  N     . PHE   F 2  389 ? 19.779  31.411  25.575  1.00 15.93  ? 399 PHE   B N     1 
ATOM   17022 C  CA    . PHE   F 2  389 ? 21.224  31.258  25.658  1.00 18.58  ? 399 PHE   B CA    1 
ATOM   17023 C  C     . PHE   F 2  389 ? 21.612  29.890  26.214  1.00 22.36  ? 399 PHE   B C     1 
ATOM   17024 O  O     . PHE   F 2  389 ? 22.655  29.338  25.831  1.00 26.60  ? 399 PHE   B O     1 
ATOM   17025 C  CB    . PHE   F 2  389 ? 21.856  32.380  26.484  1.00 16.98  ? 399 PHE   B CB    1 
ATOM   17026 C  CG    . PHE   F 2  389 ? 23.368  32.342  26.494  1.00 18.09  ? 399 PHE   B CG    1 
ATOM   17027 C  CD1   . PHE   F 2  389 ? 24.093  32.472  25.311  1.00 20.43  ? 399 PHE   B CD1   1 
ATOM   17028 C  CD2   . PHE   F 2  389 ? 24.067  32.153  27.682  1.00 20.62  ? 399 PHE   B CD2   1 
ATOM   17029 C  CE1   . PHE   F 2  389 ? 25.494  32.428  25.310  1.00 19.32  ? 399 PHE   B CE1   1 
ATOM   17030 C  CE2   . PHE   F 2  389 ? 25.464  32.117  27.695  1.00 18.25  ? 399 PHE   B CE2   1 
ATOM   17031 C  CZ    . PHE   F 2  389 ? 26.176  32.247  26.504  1.00 20.01  ? 399 PHE   B CZ    1 
ATOM   17032 N  N     . ARG   F 2  390 ? 20.781  29.304  27.084  1.00 20.81  ? 400 ARG   B N     1 
ATOM   17033 C  CA    . ARG   F 2  390 ? 21.101  27.972  27.580  1.00 21.05  ? 400 ARG   B CA    1 
ATOM   17034 C  C     . ARG   F 2  390 ? 21.190  26.943  26.453  1.00 19.31  ? 400 ARG   B C     1 
ATOM   17035 O  O     . ARG   F 2  390 ? 21.826  25.911  26.638  1.00 19.62  ? 400 ARG   B O     1 
ATOM   17036 C  CB    . ARG   F 2  390 ? 20.100  27.534  28.670  1.00 21.45  ? 400 ARG   B CB    1 
ATOM   17037 C  CG    . ARG   F 2  390 ? 18.663  27.473  28.227  1.00 36.34  ? 400 ARG   B CG    1 
ATOM   17038 C  CD    . ARG   F 2  390 ? 17.747  26.860  29.288  1.00 49.08  ? 400 ARG   B CD    1 
ATOM   17039 N  NE    . ARG   F 2  390 ? 16.412  26.623  28.742  1.00 58.27  ? 400 ARG   B NE    1 
ATOM   17040 C  CZ    . ARG   F 2  390 ? 15.335  27.333  29.053  1.00 56.98  ? 400 ARG   B CZ    1 
ATOM   17041 N  NH1   . ARG   F 2  390 ? 15.383  28.309  29.952  1.00 53.79  ? 400 ARG   B NH1   1 
ATOM   17042 N  NH2   . ARG   F 2  390 ? 14.177  27.054  28.455  1.00 40.83  ? 400 ARG   B NH2   1 
ATOM   17043 N  N     . ARG   F 2  391 ? 20.604  27.208  25.281  1.00 24.66  ? 401 ARG   B N     1 
ATOM   17044 C  CA    . ARG   F 2  391 ? 20.805  26.388  24.086  1.00 18.75  ? 401 ARG   B CA    1 
ATOM   17045 C  C     . ARG   F 2  391 ? 21.623  27.108  23.008  1.00 21.06  ? 401 ARG   B C     1 
ATOM   17046 O  O     . ARG   F 2  391 ? 21.532  26.750  21.827  1.00 22.24  ? 401 ARG   B O     1 
ATOM   17047 C  CB    . ARG   F 2  391 ? 19.463  25.947  23.502  1.00 18.15  ? 401 ARG   B CB    1 
ATOM   17048 C  CG    . ARG   F 2  391 ? 18.545  25.201  24.457  1.00 23.43  ? 401 ARG   B CG    1 
ATOM   17049 C  CD    . ARG   F 2  391 ? 19.143  23.894  24.902  1.00 17.57  ? 401 ARG   B CD    1 
ATOM   17050 N  NE    . ARG   F 2  391 ? 19.018  22.870  23.880  1.00 15.74  ? 401 ARG   B NE    1 
ATOM   17051 C  CZ    . ARG   F 2  391 ? 17.903  22.191  23.649  1.00 21.54  ? 401 ARG   B CZ    1 
ATOM   17052 N  NH1   . ARG   F 2  391 ? 16.813  22.385  24.376  1.00 17.00  ? 401 ARG   B NH1   1 
ATOM   17053 N  NH2   . ARG   F 2  391 ? 17.876  21.306  22.654  1.00 19.56  ? 401 ARG   B NH2   1 
ATOM   17054 N  N     . LYS   F 2  392 ? 22.416  28.116  23.387  1.00 18.63  ? 402 LYS   B N     1 
ATOM   17055 C  CA    . LYS   F 2  392 ? 23.244  28.876  22.449  1.00 21.53  ? 402 LYS   B CA    1 
ATOM   17056 C  C     . LYS   F 2  392 ? 22.511  29.140  21.133  1.00 24.53  ? 402 LYS   B C     1 
ATOM   17057 O  O     . LYS   F 2  392 ? 23.103  29.062  20.053  1.00 29.97  ? 402 LYS   B O     1 
ATOM   17058 C  CB    . LYS   F 2  392 ? 24.573  28.161  22.215  1.00 12.13  ? 402 LYS   B CB    1 
ATOM   17059 C  CG    . LYS   F 2  392 ? 25.438  28.089  23.487  1.00 31.83  ? 402 LYS   B CG    1 
ATOM   17060 C  CD    . LYS   F 2  392 ? 26.131  26.696  23.702  1.00 45.97  ? 402 LYS   B CD    1 
ATOM   17061 C  CE    . LYS   F 2  392 ? 25.199  25.621  24.362  1.00 43.30  ? 402 LYS   B CE    1 
ATOM   17062 N  NZ    . LYS   F 2  392 ? 25.055  25.706  25.863  1.00 41.27  ? 402 LYS   B NZ    1 
ATOM   17063 N  N     . ALA   F 2  393 ? 21.228  29.489  21.239  1.00 19.74  ? 403 ALA   B N     1 
ATOM   17064 C  CA    . ALA   F 2  393 ? 20.353  29.710  20.100  1.00 17.58  ? 403 ALA   B CA    1 
ATOM   17065 C  C     . ALA   F 2  393 ? 20.471  31.133  19.574  1.00 20.80  ? 403 ALA   B C     1 
ATOM   17066 O  O     . ALA   F 2  393 ? 20.362  32.104  20.328  1.00 20.64  ? 403 ALA   B O     1 
ATOM   17067 C  CB    . ALA   F 2  393 ? 18.900  29.420  20.486  1.00 19.41  ? 403 ALA   B CB    1 
ATOM   17068 N  N     . PHE   F 2  394 ? 20.623  31.251  18.259  1.00 22.56  ? 404 PHE   B N     1 
ATOM   17069 C  CA    . PHE   F 2  394 ? 20.760  32.520  17.559  1.00 20.24  ? 404 PHE   B CA    1 
ATOM   17070 C  C     . PHE   F 2  394 ? 22.122  33.139  17.799  1.00 21.26  ? 404 PHE   B C     1 
ATOM   17071 O  O     . PHE   F 2  394 ? 22.386  34.283  17.386  1.00 20.43  ? 404 PHE   B O     1 
ATOM   17072 C  CB    . PHE   F 2  394 ? 19.624  33.469  17.943  1.00 21.32  ? 404 PHE   B CB    1 
ATOM   17073 C  CG    . PHE   F 2  394 ? 18.288  32.947  17.539  1.00 22.37  ? 404 PHE   B CG    1 
ATOM   17074 C  CD1   . PHE   F 2  394 ? 17.942  32.875  16.201  1.00 21.08  ? 404 PHE   B CD1   1 
ATOM   17075 C  CD2   . PHE   F 2  394 ? 17.395  32.469  18.485  1.00 19.94  ? 404 PHE   B CD2   1 
ATOM   17076 C  CE1   . PHE   F 2  394 ? 16.704  32.372  15.818  1.00 21.83  ? 404 PHE   B CE1   1 
ATOM   17077 C  CE2   . PHE   F 2  394 ? 16.159  31.954  18.098  1.00 16.82  ? 404 PHE   B CE2   1 
ATOM   17078 C  CZ    . PHE   F 2  394 ? 15.816  31.908  16.771  1.00 15.87  ? 404 PHE   B CZ    1 
ATOM   17079 N  N     . LEU   F 2  395 ? 23.016  32.382  18.422  1.00 23.82  ? 405 LEU   B N     1 
ATOM   17080 C  CA    . LEU   F 2  395 ? 24.344  32.877  18.730  1.00 21.22  ? 405 LEU   B CA    1 
ATOM   17081 C  C     . LEU   F 2  395 ? 25.189  33.097  17.481  1.00 15.98  ? 405 LEU   B C     1 
ATOM   17082 O  O     . LEU   F 2  395 ? 26.111  33.914  17.527  1.00 20.10  ? 405 LEU   B O     1 
ATOM   17083 C  CB    . LEU   F 2  395 ? 25.029  31.902  19.686  1.00 16.07  ? 405 LEU   B CB    1 
ATOM   17084 C  CG    . LEU   F 2  395 ? 25.566  32.496  20.978  1.00 16.83  ? 405 LEU   B CG    1 
ATOM   17085 C  CD1   . LEU   F 2  395 ? 24.493  33.295  21.676  1.00 25.88  ? 405 LEU   B CD1   1 
ATOM   17086 C  CD2   . LEU   F 2  395 ? 26.085  31.382  21.880  1.00 25.93  ? 405 LEU   B CD2   1 
ATOM   17087 N  N     . HIS   F 2  396 ? 24.887  32.420  16.364  1.00 15.84  ? 406 HIS   B N     1 
ATOM   17088 C  CA    . HIS   F 2  396 ? 25.765  32.515  15.197  1.00 14.86  ? 406 HIS   B CA    1 
ATOM   17089 C  C     . HIS   F 2  396 ? 25.770  33.919  14.630  1.00 19.63  ? 406 HIS   B C     1 
ATOM   17090 O  O     . HIS   F 2  396 ? 26.827  34.423  14.220  1.00 20.65  ? 406 HIS   B O     1 
ATOM   17091 C  CB    . HIS   F 2  396 ? 25.377  31.498  14.113  1.00 19.28  ? 406 HIS   B CB    1 
ATOM   17092 C  CG    . HIS   F 2  396 ? 24.030  31.721  13.484  1.00 23.02  ? 406 HIS   B CG    1 
ATOM   17093 N  ND1   . HIS   F 2  396 ? 23.843  32.525  12.379  1.00 23.76  ? 406 HIS   B ND1   1 
ATOM   17094 C  CD2   . HIS   F 2  396 ? 22.814  31.201  13.777  1.00 23.23  ? 406 HIS   B CD2   1 
ATOM   17095 C  CE1   . HIS   F 2  396 ? 22.568  32.518  12.039  1.00 18.19  ? 406 HIS   B CE1   1 
ATOM   17096 N  NE2   . HIS   F 2  396 ? 21.923  31.719  12.869  1.00 23.17  ? 406 HIS   B NE2   1 
ATOM   17097 N  N     . TRP   F 2  397 ? 24.595  34.560  14.588  1.00 19.83  ? 407 TRP   B N     1 
ATOM   17098 C  CA    . TRP   F 2  397 ? 24.496  35.958  14.186  1.00 16.07  ? 407 TRP   B CA    1 
ATOM   17099 C  C     . TRP   F 2  397 ? 25.517  36.836  14.880  1.00 20.14  ? 407 TRP   B C     1 
ATOM   17100 O  O     . TRP   F 2  397 ? 25.884  37.892  14.347  1.00 16.37  ? 407 TRP   B O     1 
ATOM   17101 C  CB    . TRP   F 2  397 ? 23.123  36.503  14.514  1.00 17.61  ? 407 TRP   B CB    1 
ATOM   17102 C  CG    . TRP   F 2  397 ? 22.001  35.852  13.822  1.00 20.52  ? 407 TRP   B CG    1 
ATOM   17103 C  CD1   . TRP   F 2  397 ? 20.862  35.341  14.396  1.00 21.31  ? 407 TRP   B CD1   1 
ATOM   17104 C  CD2   . TRP   F 2  397 ? 21.871  35.658  12.422  1.00 17.70  ? 407 TRP   B CD2   1 
ATOM   17105 N  NE1   . TRP   F 2  397 ? 20.037  34.845  13.430  1.00 24.25  ? 407 TRP   B NE1   1 
ATOM   17106 C  CE2   . TRP   F 2  397 ? 20.634  35.027  12.206  1.00 23.40  ? 407 TRP   B CE2   1 
ATOM   17107 C  CE3   . TRP   F 2  397 ? 22.674  35.961  11.326  1.00 17.46  ? 407 TRP   B CE3   1 
ATOM   17108 C  CZ2   . TRP   F 2  397 ? 20.195  34.687  10.947  1.00 17.48  ? 407 TRP   B CZ2   1 
ATOM   17109 C  CZ3   . TRP   F 2  397 ? 22.244  35.610  10.093  1.00 20.04  ? 407 TRP   B CZ3   1 
ATOM   17110 C  CH2   . TRP   F 2  397 ? 21.015  34.977  9.908   1.00 18.49  ? 407 TRP   B CH2   1 
ATOM   17111 N  N     . TYR   F 2  398 ? 25.964  36.429  16.078  1.00 20.53  ? 408 TYR   B N     1 
ATOM   17112 C  CA    . TYR   F 2  398 ? 26.909  37.176  16.899  1.00 17.03  ? 408 TYR   B CA    1 
ATOM   17113 C  C     . TYR   F 2  398 ? 28.336  36.649  16.782  1.00 25.56  ? 408 TYR   B C     1 
ATOM   17114 O  O     . TYR   F 2  398 ? 29.278  37.445  16.641  1.00 28.61  ? 408 TYR   B O     1 
ATOM   17115 C  CB    . TYR   F 2  398 ? 26.451  37.172  18.363  1.00 14.91  ? 408 TYR   B CB    1 
ATOM   17116 C  CG    . TYR   F 2  398 ? 25.129  37.884  18.562  1.00 19.67  ? 408 TYR   B CG    1 
ATOM   17117 C  CD1   . TYR   F 2  398 ? 23.919  37.204  18.432  1.00 17.91  ? 408 TYR   B CD1   1 
ATOM   17118 C  CD2   . TYR   F 2  398 ? 25.086  39.238  18.845  1.00 22.33  ? 408 TYR   B CD2   1 
ATOM   17119 C  CE1   . TYR   F 2  398 ? 22.717  37.846  18.596  1.00 14.28  ? 408 TYR   B CE1   1 
ATOM   17120 C  CE2   . TYR   F 2  398 ? 23.885  39.894  19.011  1.00 20.41  ? 408 TYR   B CE2   1 
ATOM   17121 C  CZ    . TYR   F 2  398 ? 22.700  39.189  18.895  1.00 21.68  ? 408 TYR   B CZ    1 
ATOM   17122 O  OH    . TYR   F 2  398 ? 21.496  39.846  19.069  1.00 21.61  ? 408 TYR   B OH    1 
ATOM   17123 N  N     . THR   F 2  399 ? 28.530  35.323  16.838  1.00 21.25  ? 409 THR   B N     1 
ATOM   17124 C  CA    . THR   F 2  399 ? 29.884  34.805  16.705  1.00 16.78  ? 409 THR   B CA    1 
ATOM   17125 C  C     . THR   F 2  399 ? 30.439  35.057  15.308  1.00 20.23  ? 409 THR   B C     1 
ATOM   17126 O  O     . THR   F 2  399 ? 31.657  35.169  15.145  1.00 29.44  ? 409 THR   B O     1 
ATOM   17127 C  CB    . THR   F 2  399 ? 29.940  33.312  17.061  1.00 15.31  ? 409 THR   B CB    1 
ATOM   17128 O  OG1   . THR   F 2  399 ? 28.938  32.591  16.347  1.00 18.91  ? 409 THR   B OG1   1 
ATOM   17129 C  CG2   . THR   F 2  399 ? 29.716  33.094  18.524  1.00 16.97  ? 409 THR   B CG2   1 
ATOM   17130 N  N     . GLY   F 2  400 ? 29.584  35.184  14.299  1.00 14.68  ? 410 GLY   B N     1 
ATOM   17131 C  CA    . GLY   F 2  400 ? 30.094  35.533  12.985  1.00 18.80  ? 410 GLY   B CA    1 
ATOM   17132 C  C     . GLY   F 2  400 ? 30.554  36.982  12.823  1.00 23.54  ? 410 GLY   B C     1 
ATOM   17133 O  O     . GLY   F 2  400 ? 31.066  37.338  11.749  1.00 20.49  ? 410 GLY   B O     1 
ATOM   17134 N  N     . GLU   F 2  401 ? 30.344  37.828  13.829  1.00 21.15  ? 411 GLU   B N     1 
ATOM   17135 C  CA    . GLU   F 2  401 ? 30.949  39.149  13.837  1.00 23.07  ? 411 GLU   B CA    1 
ATOM   17136 C  C     . GLU   F 2  401 ? 32.227  39.164  14.633  1.00 24.01  ? 411 GLU   B C     1 
ATOM   17137 O  O     . GLU   F 2  401 ? 32.756  40.240  14.902  1.00 23.78  ? 411 GLU   B O     1 
ATOM   17138 C  CB    . GLU   F 2  401 ? 30.017  40.204  14.431  1.00 18.81  ? 411 GLU   B CB    1 
ATOM   17139 C  CG    . GLU   F 2  401 ? 28.734  40.396  13.726  1.00 20.33  ? 411 GLU   B CG    1 
ATOM   17140 C  CD    . GLU   F 2  401 ? 28.893  40.515  12.226  1.00 23.73  ? 411 GLU   B CD    1 
ATOM   17141 O  OE1   . GLU   F 2  401 ? 29.633  41.415  11.729  1.00 20.77  ? 411 GLU   B OE1   1 
ATOM   17142 O  OE2   . GLU   F 2  401 ? 28.231  39.704  11.548  1.00 26.89  ? 411 GLU   B OE2   1 
ATOM   17143 N  N     . GLY   F 2  402 ? 32.705  37.999  15.056  1.00 27.38  ? 412 GLY   B N     1 
ATOM   17144 C  CA    . GLY   F 2  402 ? 33.866  37.913  15.922  1.00 36.08  ? 412 GLY   B CA    1 
ATOM   17145 C  C     . GLY   F 2  402 ? 33.580  37.921  17.416  1.00 32.86  ? 412 GLY   B C     1 
ATOM   17146 O  O     . GLY   F 2  402 ? 34.529  37.970  18.209  1.00 32.90  ? 412 GLY   B O     1 
ATOM   17147 N  N     . MET   F 2  403 ? 32.314  37.905  17.830  1.00 26.85  ? 413 MET   B N     1 
ATOM   17148 C  CA    . MET   F 2  403 ? 32.071  37.758  19.252  1.00 21.50  ? 413 MET   B CA    1 
ATOM   17149 C  C     . MET   F 2  403 ? 32.233  36.294  19.659  1.00 28.77  ? 413 MET   B C     1 
ATOM   17150 O  O     . MET   F 2  403 ? 32.335  35.379  18.832  1.00 35.55  ? 413 MET   B O     1 
ATOM   17151 C  CB    . MET   F 2  403 ? 30.690  38.282  19.643  1.00 19.58  ? 413 MET   B CB    1 
ATOM   17152 C  CG    . MET   F 2  403 ? 30.647  39.763  19.971  1.00 19.16  ? 413 MET   B CG    1 
ATOM   17153 S  SD    . MET   F 2  403 ? 29.006  40.209  20.583  1.00 26.15  ? 413 MET   B SD    1 
ATOM   17154 C  CE    . MET   F 2  403 ? 29.260  39.912  22.322  1.00 13.71  ? 413 MET   B CE    1 
ATOM   17155 N  N     . ASP   F 2  404 ? 32.243  36.083  20.966  1.00 24.85  ? 414 ASP   B N     1 
ATOM   17156 C  CA    . ASP   F 2  404 ? 32.625  34.826  21.570  1.00 19.08  ? 414 ASP   B CA    1 
ATOM   17157 C  C     . ASP   F 2  404 ? 31.663  34.569  22.721  1.00 28.23  ? 414 ASP   B C     1 
ATOM   17158 O  O     . ASP   F 2  404 ? 31.322  35.506  23.450  1.00 24.52  ? 414 ASP   B O     1 
ATOM   17159 C  CB    . ASP   F 2  404 ? 34.077  34.936  22.024  1.00 20.47  ? 414 ASP   B CB    1 
ATOM   17160 C  CG    . ASP   F 2  404 ? 34.605  33.671  22.630  1.00 33.47  ? 414 ASP   B CG    1 
ATOM   17161 O  OD1   . ASP   F 2  404 ? 34.191  33.339  23.760  1.00 35.03  ? 414 ASP   B OD1   1 
ATOM   17162 O  OD2   . ASP   F 2  404 ? 35.450  33.013  21.979  1.00 40.89  ? 414 ASP   B OD2   1 
ATOM   17163 N  N     . GLU   F 2  405 ? 31.187  33.318  22.851  1.00 35.67  ? 415 GLU   B N     1 
ATOM   17164 C  CA    . GLU   F 2  405 ? 30.254  32.956  23.923  1.00 22.78  ? 415 GLU   B CA    1 
ATOM   17165 C  C     . GLU   F 2  405 ? 30.609  33.627  25.245  1.00 30.34  ? 415 GLU   B C     1 
ATOM   17166 O  O     . GLU   F 2  405 ? 29.741  34.195  25.923  1.00 28.30  ? 415 GLU   B O     1 
ATOM   17167 C  CB    . GLU   F 2  405 ? 30.215  31.433  24.123  1.00 24.16  ? 415 GLU   B CB    1 
ATOM   17168 C  CG    . GLU   F 2  405 ? 29.235  30.632  23.246  1.00 38.81  ? 415 GLU   B CG    1 
ATOM   17169 C  CD    . GLU   F 2  405 ? 29.156  29.146  23.639  1.00 53.02  ? 415 GLU   B CD    1 
ATOM   17170 O  OE1   . GLU   F 2  405 ? 29.722  28.769  24.699  1.00 47.12  ? 415 GLU   B OE1   1 
ATOM   17171 O  OE2   . GLU   F 2  405 ? 28.528  28.355  22.886  1.00 49.39  ? 415 GLU   B OE2   1 
ATOM   17172 N  N     . MET   F 2  406 ? 31.889  33.558  25.635  1.00 34.76  ? 416 MET   B N     1 
ATOM   17173 C  CA    . MET   F 2  406 ? 32.332  34.134  26.912  1.00 39.01  ? 416 MET   B CA    1 
ATOM   17174 C  C     . MET   F 2  406 ? 31.736  35.516  27.186  1.00 29.28  ? 416 MET   B C     1 
ATOM   17175 O  O     . MET   F 2  406 ? 31.344  35.808  28.315  1.00 30.54  ? 416 MET   B O     1 
ATOM   17176 C  CB    . MET   F 2  406 ? 33.861  34.205  26.964  1.00 39.07  ? 416 MET   B CB    1 
ATOM   17177 C  CG    . MET   F 2  406 ? 34.477  33.024  27.694  1.00 68.14  ? 416 MET   B CG    1 
ATOM   17178 S  SD    . MET   F 2  406 ? 33.516  32.625  29.185  1.00 92.65  ? 416 MET   B SD    1 
ATOM   17179 C  CE    . MET   F 2  406 ? 32.361  31.375  28.588  1.00 59.92  ? 416 MET   B CE    1 
ATOM   17180 N  N     . GLU   F 2  407 ? 31.663  36.382  26.174  1.00 24.84  ? 417 GLU   B N     1 
ATOM   17181 C  CA    . GLU   F 2  407 ? 31.077  37.699  26.386  1.00 24.41  ? 417 GLU   B CA    1 
ATOM   17182 C  C     . GLU   F 2  407 ? 29.636  37.596  26.868  1.00 27.31  ? 417 GLU   B C     1 
ATOM   17183 O  O     . GLU   F 2  407 ? 29.225  38.332  27.769  1.00 28.51  ? 417 GLU   B O     1 
ATOM   17184 C  CB    . GLU   F 2  407 ? 31.149  38.532  25.108  1.00 20.49  ? 417 GLU   B CB    1 
ATOM   17185 C  CG    . GLU   F 2  407 ? 32.352  39.437  25.014  1.00 25.85  ? 417 GLU   B CG    1 
ATOM   17186 C  CD    . GLU   F 2  407 ? 32.149  40.560  24.012  1.00 25.60  ? 417 GLU   B CD    1 
ATOM   17187 O  OE1   . GLU   F 2  407 ? 31.240  41.382  24.246  1.00 15.80  ? 417 GLU   B OE1   1 
ATOM   17188 O  OE2   . GLU   F 2  407 ? 32.892  40.600  22.999  1.00 21.45  ? 417 GLU   B OE2   1 
ATOM   17189 N  N     . PHE   F 2  408 ? 28.844  36.705  26.272  1.00 23.72  ? 418 PHE   B N     1 
ATOM   17190 C  CA    . PHE   F 2  408 ? 27.447  36.609  26.672  1.00 19.19  ? 418 PHE   B CA    1 
ATOM   17191 C  C     . PHE   F 2  408 ? 27.345  36.166  28.119  1.00 22.15  ? 418 PHE   B C     1 
ATOM   17192 O  O     . PHE   F 2  408 ? 26.499  36.668  28.871  1.00 24.32  ? 418 PHE   B O     1 
ATOM   17193 C  CB    . PHE   F 2  408 ? 26.680  35.642  25.763  1.00 18.86  ? 418 PHE   B CB    1 
ATOM   17194 C  CG    . PHE   F 2  408 ? 26.367  36.193  24.397  1.00 20.39  ? 418 PHE   B CG    1 
ATOM   17195 C  CD1   . PHE   F 2  408 ? 27.362  36.325  23.443  1.00 15.03  ? 418 PHE   B CD1   1 
ATOM   17196 C  CD2   . PHE   F 2  408 ? 25.063  36.560  24.058  1.00 20.97  ? 418 PHE   B CD2   1 
ATOM   17197 C  CE1   . PHE   F 2  408 ? 27.074  36.826  22.191  1.00 16.00  ? 418 PHE   B CE1   1 
ATOM   17198 C  CE2   . PHE   F 2  408 ? 24.770  37.067  22.796  1.00 20.79  ? 418 PHE   B CE2   1 
ATOM   17199 C  CZ    . PHE   F 2  408 ? 25.779  37.202  21.864  1.00 19.78  ? 418 PHE   B CZ    1 
ATOM   17200 N  N     . THR   F 2  409 ? 28.208  35.223  28.521  1.00 24.88  ? 419 THR   B N     1 
ATOM   17201 C  CA    . THR   F 2  409 ? 28.259  34.757  29.906  1.00 23.75  ? 419 THR   B CA    1 
ATOM   17202 C  C     . THR   F 2  409 ? 28.582  35.895  30.874  1.00 20.67  ? 419 THR   B C     1 
ATOM   17203 O  O     . THR   F 2  409 ? 27.983  36.003  31.945  1.00 20.85  ? 419 THR   B O     1 
ATOM   17204 C  CB    . THR   F 2  409 ? 29.279  33.621  30.028  1.00 22.98  ? 419 THR   B CB    1 
ATOM   17205 O  OG1   . THR   F 2  409 ? 28.730  32.412  29.467  1.00 28.18  ? 419 THR   B OG1   1 
ATOM   17206 C  CG2   . THR   F 2  409 ? 29.626  33.368  31.459  1.00 18.73  ? 419 THR   B CG2   1 
ATOM   17207 N  N     . GLU   F 2  410 ? 29.494  36.779  30.489  1.00 27.81  ? 420 GLU   B N     1 
ATOM   17208 C  CA    . GLU   F 2  410 ? 29.834  37.931  31.317  1.00 25.56  ? 420 GLU   B CA    1 
ATOM   17209 C  C     . GLU   F 2  410 ? 28.667  38.904  31.460  1.00 28.83  ? 420 GLU   B C     1 
ATOM   17210 O  O     . GLU   F 2  410 ? 28.234  39.209  32.579  1.00 31.78  ? 420 GLU   B O     1 
ATOM   17211 C  CB    . GLU   F 2  410 ? 31.033  38.643  30.716  1.00 27.98  ? 420 GLU   B CB    1 
ATOM   17212 C  CG    . GLU   F 2  410 ? 32.256  37.782  30.695  1.00 38.92  ? 420 GLU   B CG    1 
ATOM   17213 C  CD    . GLU   F 2  410 ? 33.413  38.497  30.072  1.00 46.71  ? 420 GLU   B CD    1 
ATOM   17214 O  OE1   . GLU   F 2  410 ? 33.202  39.657  29.622  1.00 40.00  ? 420 GLU   B OE1   1 
ATOM   17215 O  OE2   . GLU   F 2  410 ? 34.511  37.891  30.048  1.00 33.83  ? 420 GLU   B OE2   1 
ATOM   17216 N  N     . ALA   F 2  411 ? 28.177  39.444  30.332  1.00 29.99  ? 421 ALA   B N     1 
ATOM   17217 C  CA    . ALA   F 2  411 ? 27.057  40.379  30.371  1.00 20.97  ? 421 ALA   B CA    1 
ATOM   17218 C  C     . ALA   F 2  411 ? 25.917  39.821  31.205  1.00 23.75  ? 421 ALA   B C     1 
ATOM   17219 O  O     . ALA   F 2  411 ? 25.285  40.549  31.976  1.00 23.64  ? 421 ALA   B O     1 
ATOM   17220 C  CB    . ALA   F 2  411 ? 26.580  40.708  28.957  1.00 14.76  ? 421 ALA   B CB    1 
ATOM   17221 N  N     . GLU   F 2  412 ? 25.657  38.522  31.081  1.00 20.51  ? 422 GLU   B N     1 
ATOM   17222 C  CA    . GLU   F 2  412 ? 24.586  37.902  31.851  1.00 19.94  ? 422 GLU   B CA    1 
ATOM   17223 C  C     . GLU   F 2  412 ? 24.913  37.892  33.335  1.00 24.25  ? 422 GLU   B C     1 
ATOM   17224 O  O     . GLU   F 2  412 ? 24.038  38.144  34.170  1.00 22.69  ? 422 GLU   B O     1 
ATOM   17225 C  CB    . GLU   F 2  412 ? 24.342  36.478  31.349  1.00 22.49  ? 422 GLU   B CB    1 
ATOM   17226 C  CG    . GLU   F 2  412 ? 23.256  35.683  32.088  1.00 25.51  ? 422 GLU   B CG    1 
ATOM   17227 C  CD    . GLU   F 2  412 ? 23.247  34.200  31.691  1.00 29.42  ? 422 GLU   B CD    1 
ATOM   17228 O  OE1   . GLU   F 2  412 ? 24.334  33.593  31.598  1.00 34.33  ? 422 GLU   B OE1   1 
ATOM   17229 O  OE2   . GLU   F 2  412 ? 22.159  33.641  31.467  1.00 27.00  ? 422 GLU   B OE2   1 
ATOM   17230 N  N     . SER   F 2  413 ? 26.165  37.592  33.684  1.00 25.57  ? 423 SER   B N     1 
ATOM   17231 C  CA    A SER   F 2  413 ? 26.545  37.536  35.093  0.38 24.03  ? 423 SER   B CA    1 
ATOM   17232 C  CA    B SER   F 2  413 ? 26.540  37.535  35.093  0.62 24.06  ? 423 SER   B CA    1 
ATOM   17233 C  C     . SER   F 2  413 ? 26.486  38.913  35.738  1.00 26.64  ? 423 SER   B C     1 
ATOM   17234 O  O     . SER   F 2  413 ? 26.017  39.053  36.875  1.00 21.35  ? 423 SER   B O     1 
ATOM   17235 C  CB    A SER   F 2  413 ? 27.944  36.943  35.247  0.38 22.59  ? 423 SER   B CB    1 
ATOM   17236 C  CB    B SER   F 2  413 ? 27.933  36.924  35.248  0.62 22.64  ? 423 SER   B CB    1 
ATOM   17237 O  OG    A SER   F 2  413 ? 28.516  37.320  36.493  0.38 23.93  ? 423 SER   B OG    1 
ATOM   17238 O  OG    B SER   F 2  413 ? 27.894  35.514  35.098  0.62 21.25  ? 423 SER   B OG    1 
ATOM   17239 N  N     . ASN   F 2  414 ? 26.966  39.941  35.035  1.00 21.51  ? 424 ASN   B N     1 
ATOM   17240 C  CA    . ASN   F 2  414 ? 26.937  41.281  35.600  1.00 19.61  ? 424 ASN   B CA    1 
ATOM   17241 C  C     . ASN   F 2  414 ? 25.505  41.723  35.851  1.00 28.88  ? 424 ASN   B C     1 
ATOM   17242 O  O     . ASN   F 2  414 ? 25.226  42.403  36.844  1.00 35.73  ? 424 ASN   B O     1 
ATOM   17243 C  CB    . ASN   F 2  414 ? 27.653  42.263  34.672  1.00 24.81  ? 424 ASN   B CB    1 
ATOM   17244 C  CG    . ASN   F 2  414 ? 27.975  43.568  35.341  1.00 26.28  ? 424 ASN   B CG    1 
ATOM   17245 O  OD1   . ASN   F 2  414 ? 28.268  43.604  36.538  1.00 30.45  ? 424 ASN   B OD1   1 
ATOM   17246 N  ND2   . ASN   F 2  414 ? 27.927  44.655  34.579  1.00 30.75  ? 424 ASN   B ND2   1 
ATOM   17247 N  N     . MET   F 2  415 ? 24.573  41.337  34.965  1.00 29.92  ? 425 MET   B N     1 
ATOM   17248 C  CA    . MET   F 2  415 ? 23.173  41.713  35.157  1.00 23.15  ? 425 MET   B CA    1 
ATOM   17249 C  C     . MET   F 2  415 ? 22.552  40.902  36.282  1.00 23.40  ? 425 MET   B C     1 
ATOM   17250 O  O     . MET   F 2  415 ? 21.854  41.454  37.139  1.00 26.60  ? 425 MET   B O     1 
ATOM   17251 C  CB    . MET   F 2  415 ? 22.376  41.548  33.858  1.00 16.35  ? 425 MET   B CB    1 
ATOM   17252 C  CG    . MET   F 2  415 ? 20.997  42.180  33.881  1.00 21.80  ? 425 MET   B CG    1 
ATOM   17253 S  SD    . MET   F 2  415 ? 20.283  42.488  32.252  1.00 21.17  ? 425 MET   B SD    1 
ATOM   17254 C  CE    . MET   F 2  415 ? 19.824  40.827  31.806  1.00 15.33  ? 425 MET   B CE    1 
ATOM   17255 N  N     . ASN   F 2  416 ? 22.816  39.598  36.324  1.00 23.81  ? 426 ASN   B N     1 
ATOM   17256 C  CA    . ASN   F 2  416 ? 22.336  38.818  37.460  1.00 28.24  ? 426 ASN   B CA    1 
ATOM   17257 C  C     . ASN   F 2  416 ? 22.854  39.386  38.779  1.00 30.71  ? 426 ASN   B C     1 
ATOM   17258 O  O     . ASN   F 2  416 ? 22.132  39.370  39.792  1.00 29.22  ? 426 ASN   B O     1 
ATOM   17259 C  CB    . ASN   F 2  416 ? 22.720  37.345  37.297  1.00 19.72  ? 426 ASN   B CB    1 
ATOM   17260 C  CG    . ASN   F 2  416 ? 21.812  36.622  36.309  1.00 30.76  ? 426 ASN   B CG    1 
ATOM   17261 O  OD1   . ASN   F 2  416 ? 20.693  37.078  36.017  1.00 28.23  ? 426 ASN   B OD1   1 
ATOM   17262 N  ND2   . ASN   F 2  416 ? 22.283  35.490  35.794  1.00 38.59  ? 426 ASN   B ND2   1 
ATOM   17263 N  N     . ASP   F 2  417 ? 24.084  39.911  38.779  1.00 26.07  ? 427 ASP   B N     1 
ATOM   17264 C  CA    . ASP   F 2  417 ? 24.609  40.589  39.957  1.00 21.38  ? 427 ASP   B CA    1 
ATOM   17265 C  C     . ASP   F 2  417 ? 23.802  41.833  40.268  1.00 26.65  ? 427 ASP   B C     1 
ATOM   17266 O  O     . ASP   F 2  417 ? 23.326  42.010  41.394  1.00 25.91  ? 427 ASP   B O     1 
ATOM   17267 C  CB    . ASP   F 2  417 ? 26.062  40.976  39.744  1.00 27.14  ? 427 ASP   B CB    1 
ATOM   17268 C  CG    . ASP   F 2  417 ? 26.987  39.786  39.662  1.00 26.08  ? 427 ASP   B CG    1 
ATOM   17269 O  OD1   . ASP   F 2  417 ? 26.663  38.703  40.221  1.00 20.40  ? 427 ASP   B OD1   1 
ATOM   17270 O  OD2   . ASP   F 2  417 ? 28.058  39.967  39.042  1.00 29.24  ? 427 ASP   B OD2   1 
ATOM   17271 N  N     . LEU   F 2  418 ? 23.653  42.718  39.273  1.00 27.74  ? 428 LEU   B N     1 
ATOM   17272 C  CA    . LEU   F 2  418 ? 22.825  43.908  39.441  1.00 25.79  ? 428 LEU   B CA    1 
ATOM   17273 C  C     . LEU   F 2  418 ? 21.497  43.582  40.109  1.00 29.83  ? 428 LEU   B C     1 
ATOM   17274 O  O     . LEU   F 2  418 ? 20.982  44.384  40.902  1.00 31.49  ? 428 LEU   B O     1 
ATOM   17275 C  CB    . LEU   F 2  418 ? 22.567  44.580  38.094  1.00 20.41  ? 428 LEU   B CB    1 
ATOM   17276 C  CG    . LEU   F 2  418 ? 21.727  45.866  38.166  1.00 20.37  ? 428 LEU   B CG    1 
ATOM   17277 C  CD1   . LEU   F 2  418 ? 22.527  47.018  38.701  1.00 14.54  ? 428 LEU   B CD1   1 
ATOM   17278 C  CD2   . LEU   F 2  418 ? 21.140  46.197  36.800  1.00 22.10  ? 428 LEU   B CD2   1 
ATOM   17279 N  N     . VAL   F 2  419 ? 20.922  42.417  39.814  1.00 23.90  ? 429 VAL   B N     1 
ATOM   17280 C  CA    . VAL   F 2  419 ? 19.630  42.099  40.406  1.00 24.00  ? 429 VAL   B CA    1 
ATOM   17281 C  C     . VAL   F 2  419 ? 19.792  41.699  41.864  1.00 25.52  ? 429 VAL   B C     1 
ATOM   17282 O  O     . VAL   F 2  419 ? 19.030  42.135  42.730  1.00 29.52  ? 429 VAL   B O     1 
ATOM   17283 C  CB    . VAL   F 2  419 ? 18.904  41.009  39.600  1.00 24.49  ? 429 VAL   B CB    1 
ATOM   17284 C  CG1   . VAL   F 2  419 ? 17.725  40.474  40.420  1.00 23.60  ? 429 VAL   B CG1   1 
ATOM   17285 C  CG2   . VAL   F 2  419 ? 18.419  41.574  38.277  1.00 17.74  ? 429 VAL   B CG2   1 
ATOM   17286 N  N     . SER   F 2  420 ? 20.789  40.869  42.166  1.00 25.95  ? 430 SER   B N     1 
ATOM   17287 C  CA    . SER   F 2  420 ? 20.999  40.480  43.554  1.00 28.54  ? 430 SER   B CA    1 
ATOM   17288 C  C     . SER   F 2  420 ? 21.398  41.675  44.387  1.00 32.58  ? 430 SER   B C     1 
ATOM   17289 O  O     . SER   F 2  420 ? 21.049  41.773  45.570  1.00 39.23  ? 430 SER   B O     1 
ATOM   17290 C  CB    . SER   F 2  420 ? 22.058  39.399  43.627  1.00 27.95  ? 430 SER   B CB    1 
ATOM   17291 O  OG    . SER   F 2  420 ? 22.789  39.427  42.421  1.00 43.15  ? 430 SER   B OG    1 
ATOM   17292 N  N     . GLU   F 2  421 ? 22.097  42.612  43.767  1.00 34.72  ? 431 GLU   B N     1 
ATOM   17293 C  CA    . GLU   F 2  421 ? 22.506  43.825  44.453  1.00 32.39  ? 431 GLU   B CA    1 
ATOM   17294 C  C     . GLU   F 2  421 ? 21.295  44.667  44.838  1.00 29.74  ? 431 GLU   B C     1 
ATOM   17295 O  O     . GLU   F 2  421 ? 21.181  45.117  45.985  1.00 26.37  ? 431 GLU   B O     1 
ATOM   17296 C  CB    . GLU   F 2  421 ? 23.468  44.577  43.542  1.00 29.22  ? 431 GLU   B CB    1 
ATOM   17297 C  CG    . GLU   F 2  421 ? 24.021  45.856  44.057  1.00 33.32  ? 431 GLU   B CG    1 
ATOM   17298 C  CD    . GLU   F 2  421 ? 25.287  46.175  43.306  1.00 36.96  ? 431 GLU   B CD    1 
ATOM   17299 O  OE1   . GLU   F 2  421 ? 25.719  45.241  42.551  1.00 26.02  ? 431 GLU   B OE1   1 
ATOM   17300 O  OE2   . GLU   F 2  421 ? 25.814  47.318  43.485  1.00 27.69  ? 431 GLU   B OE2   1 
ATOM   17301 N  N     . TYR   F 2  422 ? 20.364  44.872  43.892  1.00 28.12  ? 432 TYR   B N     1 
ATOM   17302 C  CA    . TYR   F 2  422 ? 19.125  45.582  44.209  1.00 29.58  ? 432 TYR   B CA    1 
ATOM   17303 C  C     . TYR   F 2  422 ? 18.329  44.856  45.297  1.00 35.34  ? 432 TYR   B C     1 
ATOM   17304 O  O     . TYR   F 2  422 ? 17.651  45.504  46.110  1.00 36.22  ? 432 TYR   B O     1 
ATOM   17305 C  CB    . TYR   F 2  422 ? 18.272  45.765  42.946  1.00 20.01  ? 432 TYR   B CB    1 
ATOM   17306 C  CG    . TYR   F 2  422 ? 18.476  47.080  42.202  1.00 16.22  ? 432 TYR   B CG    1 
ATOM   17307 C  CD1   . TYR   F 2  422 ? 18.211  48.288  42.823  1.00 21.25  ? 432 TYR   B CD1   1 
ATOM   17308 C  CD2   . TYR   F 2  422 ? 18.898  47.110  40.868  1.00 16.41  ? 432 TYR   B CD2   1 
ATOM   17309 C  CE1   . TYR   F 2  422 ? 18.361  49.513  42.154  1.00 23.49  ? 432 TYR   B CE1   1 
ATOM   17310 C  CE2   . TYR   F 2  422 ? 19.065  48.333  40.177  1.00 18.35  ? 432 TYR   B CE2   1 
ATOM   17311 C  CZ    . TYR   F 2  422 ? 18.794  49.541  40.833  1.00 26.01  ? 432 TYR   B CZ    1 
ATOM   17312 O  OH    . TYR   F 2  422 ? 18.931  50.785  40.211  1.00 24.58  ? 432 TYR   B OH    1 
ATOM   17313 N  N     . GLN   F 2  423 ? 18.421  43.520  45.358  1.00 27.83  ? 433 GLN   B N     1 
ATOM   17314 C  CA    . GLN   F 2  423 ? 17.618  42.777  46.323  1.00 30.81  ? 433 GLN   B CA    1 
ATOM   17315 C  C     . GLN   F 2  423 ? 18.183  42.881  47.739  1.00 32.58  ? 433 GLN   B C     1 
ATOM   17316 O  O     . GLN   F 2  423 ? 17.424  43.034  48.704  1.00 39.93  ? 433 GLN   B O     1 
ATOM   17317 C  CB    . GLN   F 2  423 ? 17.494  41.318  45.881  1.00 31.73  ? 433 GLN   B CB    1 
ATOM   17318 C  CG    . GLN   F 2  423 ? 16.772  40.382  46.867  1.00 37.60  ? 433 GLN   B CG    1 
ATOM   17319 C  CD    . GLN   F 2  423 ? 15.279  40.665  47.054  1.00 38.24  ? 433 GLN   B CD    1 
ATOM   17320 O  OE1   . GLN   F 2  423 ? 14.586  41.134  46.141  1.00 32.63  ? 433 GLN   B OE1   1 
ATOM   17321 N  NE2   . GLN   F 2  423 ? 14.780  40.375  48.257  1.00 38.40  ? 433 GLN   B NE2   1 
ATOM   17322 N  N     . GLN   F 2  424 ? 19.506  42.819  47.891  1.00 36.62  ? 434 GLN   B N     1 
ATOM   17323 C  CA    . GLN   F 2  424 ? 20.094  42.940  49.224  1.00 29.92  ? 434 GLN   B CA    1 
ATOM   17324 C  C     . GLN   F 2  424 ? 19.669  44.237  49.898  1.00 27.57  ? 434 GLN   B C     1 
ATOM   17325 O  O     . GLN   F 2  424 ? 19.453  44.270  51.112  1.00 45.79  ? 434 GLN   B O     1 
ATOM   17326 C  CB    . GLN   F 2  424 ? 21.618  42.846  49.136  1.00 27.80  ? 434 GLN   B CB    1 
ATOM   17327 C  CG    . GLN   F 2  424 ? 22.358  44.118  49.497  1.00 29.44  ? 434 GLN   B CG    1 
ATOM   17328 C  CD    . GLN   F 2  424 ? 23.864  44.016  49.251  1.00 42.52  ? 434 GLN   B CD    1 
ATOM   17329 O  OE1   . GLN   F 2  424 ? 24.674  44.563  50.016  1.00 44.67  ? 434 GLN   B OE1   1 
ATOM   17330 N  NE2   . GLN   F 2  424 ? 24.246  43.319  48.174  1.00 39.20  ? 434 GLN   B NE2   1 
ATOM   17331 N  N     . TYR   F 2  425 ? 19.543  45.315  49.132  1.00 31.02  ? 435 TYR   B N     1 
ATOM   17332 C  CA    . TYR   F 2  425 ? 19.163  46.587  49.712  1.00 27.00  ? 435 TYR   B CA    1 
ATOM   17333 C  C     . TYR   F 2  425 ? 17.670  46.692  49.942  1.00 33.31  ? 435 TYR   B C     1 
ATOM   17334 O  O     . TYR   F 2  425 ? 17.235  47.668  50.566  1.00 38.41  ? 435 TYR   B O     1 
ATOM   17335 C  CB    . TYR   F 2  425 ? 19.656  47.728  48.828  1.00 22.49  ? 435 TYR   B CB    1 
ATOM   17336 C  CG    . TYR   F 2  425 ? 21.162  47.859  48.870  1.00 23.30  ? 435 TYR   B CG    1 
ATOM   17337 C  CD1   . TYR   F 2  425 ? 21.812  48.229  50.031  1.00 20.78  ? 435 TYR   B CD1   1 
ATOM   17338 C  CD2   . TYR   F 2  425 ? 21.935  47.614  47.750  1.00 27.37  ? 435 TYR   B CD2   1 
ATOM   17339 C  CE1   . TYR   F 2  425 ? 23.187  48.348  50.080  1.00 24.86  ? 435 TYR   B CE1   1 
ATOM   17340 C  CE2   . TYR   F 2  425 ? 23.320  47.735  47.782  1.00 28.92  ? 435 TYR   B CE2   1 
ATOM   17341 C  CZ    . TYR   F 2  425 ? 23.945  48.092  48.958  1.00 32.76  ? 435 TYR   B CZ    1 
ATOM   17342 O  OH    . TYR   F 2  425 ? 25.329  48.205  49.007  1.00 30.89  ? 435 TYR   B OH    1 
ATOM   17343 N  N     . GLN   F 2  426 ? 16.884  45.707  49.474  1.00 33.29  ? 436 GLN   B N     1 
ATOM   17344 C  CA    . GLN   F 2  426 ? 15.467  45.611  49.827  1.00 31.29  ? 436 GLN   B CA    1 
ATOM   17345 C  C     . GLN   F 2  426 ? 15.270  45.103  51.241  1.00 44.95  ? 436 GLN   B C     1 
ATOM   17346 O  O     . GLN   F 2  426 ? 14.188  45.282  51.813  1.00 56.47  ? 436 GLN   B O     1 
ATOM   17347 C  CB    . GLN   F 2  426 ? 14.725  44.691  48.866  1.00 32.85  ? 436 GLN   B CB    1 
ATOM   17348 C  CG    . GLN   F 2  426 ? 13.859  45.437  47.874  1.00 38.86  ? 436 GLN   B CG    1 
ATOM   17349 C  CD    . GLN   F 2  426 ? 13.108  44.517  46.924  1.00 36.79  ? 436 GLN   B CD    1 
ATOM   17350 O  OE1   . GLN   F 2  426 ? 12.945  43.321  47.202  1.00 36.15  ? 436 GLN   B OE1   1 
ATOM   17351 N  NE2   . GLN   F 2  426 ? 12.627  45.079  45.801  1.00 26.33  ? 436 GLN   B NE2   1 
ATOM   17352 N  N     . ASP   F 2  427 ? 16.304  44.497  51.821  1.00 47.11  ? 437 ASP   B N     1 
ATOM   17353 C  CA    . ASP   F 2  427 ? 16.273  43.953  53.172  1.00 38.80  ? 437 ASP   B CA    1 
ATOM   17354 C  C     . ASP   F 2  427 ? 17.344  44.666  53.998  1.00 46.41  ? 437 ASP   B C     1 
ATOM   17355 O  O     . ASP   F 2  427 ? 18.537  44.569  53.688  1.00 58.35  ? 437 ASP   B O     1 
ATOM   17356 C  CB    . ASP   F 2  427 ? 16.476  42.437  53.105  1.00 51.99  ? 437 ASP   B CB    1 
ATOM   17357 C  CG    . ASP   F 2  427 ? 15.818  41.805  51.852  1.00 45.94  ? 437 ASP   B CG    1 
ATOM   17358 O  OD1   . ASP   F 2  427 ? 16.492  41.030  51.150  1.00 42.77  ? 437 ASP   B OD1   1 
ATOM   17359 O  OD2   . ASP   F 2  427 ? 14.638  42.083  51.552  1.00 46.98  ? 437 ASP   B OD2   1 
ATOM   17360 N  N     . ALA   F 2  428 ? 16.919  45.407  55.026  1.00 58.72  ? 438 ALA   B N     1 
ATOM   17361 C  CA    . ALA   F 2  428 ? 17.828  46.191  55.880  1.00 48.74  ? 438 ALA   B CA    1 
ATOM   17362 C  C     . ALA   F 2  428 ? 17.751  45.792  57.363  1.00 56.45  ? 438 ALA   B C     1 
ATOM   17363 O  O     . ALA   F 2  428 ? 18.134  46.565  58.251  1.00 49.15  ? 438 ALA   B O     1 
ATOM   17364 C  CB    . ALA   F 2  428 ? 17.526  47.660  55.735  1.00 44.97  ? 438 ALA   B CB    1 
HETATM 17365 P  PG    . GTP   G 5  .   ? 28.039  74.749  46.465  0.00 25.20  ? 501 GTP   A PG    1 
HETATM 17366 O  O1G   . GTP   G 5  .   ? 27.574  73.696  47.443  0.00 25.34  ? 501 GTP   A O1G   1 
HETATM 17367 O  O2G   . GTP   G 5  .   ? 29.499  74.535  46.147  0.00 24.21  ? 501 GTP   A O2G   1 
HETATM 17368 O  O3G   . GTP   G 5  .   ? 27.226  74.657  45.196  0.00 25.10  ? 501 GTP   A O3G   1 
HETATM 17369 O  O3B   . GTP   G 5  .   ? 27.833  76.198  47.137  0.00 26.49  ? 501 GTP   A O3B   1 
HETATM 17370 P  PB    . GTP   G 5  .   ? 26.371  76.659  47.632  0.00 26.66  ? 501 GTP   A PB    1 
HETATM 17371 O  O1B   . GTP   G 5  .   ? 25.392  76.535  46.489  0.00 27.46  ? 501 GTP   A O1B   1 
HETATM 17372 O  O2B   . GTP   G 5  .   ? 26.396  78.071  48.177  0.00 26.34  ? 501 GTP   A O2B   1 
HETATM 17373 O  O3A   . GTP   G 5  .   ? 26.000  75.584  48.772  0.00 26.36  ? 501 GTP   A O3A   1 
HETATM 17374 P  PA    . GTP   G 5  .   ? 26.502  75.766  50.291  0.00 26.43  ? 501 GTP   A PA    1 
HETATM 17375 O  O1A   . GTP   G 5  .   ? 26.927  77.196  50.520  0.00 26.33  ? 501 GTP   A O1A   1 
HETATM 17376 O  O2A   . GTP   G 5  .   ? 27.634  74.819  50.612  0.00 26.73  ? 501 GTP   A O2A   1 
HETATM 17377 O  "O5'" . GTP   G 5  .   ? 25.197  75.456  51.184  0.00 26.20  ? 501 GTP   A "O5'" 1 
HETATM 17378 C  "C5'" . GTP   G 5  .   ? 24.226  74.527  50.753  0.00 26.59  ? 501 GTP   A "C5'" 1 
HETATM 17379 C  "C4'" . GTP   G 5  .   ? 22.990  74.633  51.639  0.00 26.90  ? 501 GTP   A "C4'" 1 
HETATM 17380 O  "O4'" . GTP   G 5  .   ? 22.829  75.953  52.115  0.00 26.49  ? 501 GTP   A "O4'" 1 
HETATM 17381 C  "C3'" . GTP   G 5  .   ? 21.702  74.296  50.907  0.00 28.31  ? 501 GTP   A "C3'" 1 
HETATM 17382 O  "O3'" . GTP   G 5  .   ? 21.353  72.947  51.106  0.00 30.06  ? 501 GTP   A "O3'" 1 
HETATM 17383 C  "C2'" . GTP   G 5  .   ? 20.666  75.205  51.536  0.00 27.60  ? 501 GTP   A "C2'" 1 
HETATM 17384 O  "O2'" . GTP   G 5  .   ? 19.825  74.466  52.390  0.00 28.57  ? 501 GTP   A "O2'" 1 
HETATM 17385 C  "C1'" . GTP   G 5  .   ? 21.459  76.228  52.337  0.00 26.39  ? 501 GTP   A "C1'" 1 
HETATM 17386 N  N9    . GTP   G 5  .   ? 21.143  77.588  51.867  0.00 25.65  ? 501 GTP   A N9    1 
HETATM 17387 C  C8    . GTP   G 5  .   ? 21.514  78.143  50.671  0.00 25.77  ? 501 GTP   A C8    1 
HETATM 17388 N  N7    . GTP   G 5  .   ? 21.036  79.408  50.620  0.00 25.41  ? 501 GTP   A N7    1 
HETATM 17389 C  C5    . GTP   G 5  .   ? 20.372  79.668  51.767  0.00 25.14  ? 501 GTP   A C5    1 
HETATM 17390 C  C6    . GTP   G 5  .   ? 19.700  80.794  52.227  0.00 25.08  ? 501 GTP   A C6    1 
HETATM 17391 O  O6    . GTP   G 5  .   ? 19.640  81.805  51.530  0.00 25.61  ? 501 GTP   A O6    1 
HETATM 17392 N  N1    . GTP   G 5  .   ? 19.101  80.771  53.469  0.00 24.72  ? 501 GTP   A N1    1 
HETATM 17393 C  C2    . GTP   G 5  .   ? 19.173  79.632  54.246  0.00 23.87  ? 501 GTP   A C2    1 
HETATM 17394 N  N2    . GTP   G 5  .   ? 18.596  79.608  55.444  0.00 22.98  ? 501 GTP   A N2    1 
HETATM 17395 N  N3    . GTP   G 5  .   ? 19.842  78.517  53.782  0.00 24.23  ? 501 GTP   A N3    1 
HETATM 17396 C  C4    . GTP   G 5  .   ? 20.432  78.533  52.562  0.00 24.99  ? 501 GTP   A C4    1 
HETATM 17397 CA CA    . CA    H 6  .   ? 31.136  112.147 63.341  0.00 56.46  ? 502 CA    A CA    1 
HETATM 17398 P  PG    . GTP   I 5  .   ? 15.798  18.049  -17.776 0.00 28.30  ? 501 GTP   C PG    1 
HETATM 17399 O  O1G   . GTP   I 5  .   ? 14.457  18.736  -17.866 0.00 28.04  ? 501 GTP   C O1G   1 
HETATM 17400 O  O2G   . GTP   I 5  .   ? 16.034  17.228  -19.021 0.00 29.28  ? 501 GTP   C O2G   1 
HETATM 17401 O  O3G   . GTP   I 5  .   ? 16.892  19.080  -17.633 0.00 27.32  ? 501 GTP   C O3G   1 
HETATM 17402 O  O3B   . GTP   I 5  .   ? 15.790  17.086  -16.486 0.00 28.71  ? 501 GTP   C O3B   1 
HETATM 17403 P  PB    . GTP   I 5  .   ? 15.398  17.667  -15.037 0.00 27.69  ? 501 GTP   C PB    1 
HETATM 17404 O  O1B   . GTP   I 5  .   ? 16.321  18.807  -14.680 0.00 26.56  ? 501 GTP   C O1B   1 
HETATM 17405 O  O2B   . GTP   I 5  .   ? 15.444  16.581  -13.988 0.00 27.82  ? 501 GTP   C O2B   1 
HETATM 17406 O  O3A   . GTP   I 5  .   ? 13.898  18.220  -15.229 0.00 27.06  ? 501 GTP   C O3A   1 
HETATM 17407 P  PA    . GTP   I 5  .   ? 12.710  17.216  -15.645 0.00 28.07  ? 501 GTP   C PA    1 
HETATM 17408 O  O1A   . GTP   I 5  .   ? 13.121  16.423  -16.862 0.00 30.83  ? 501 GTP   C O1A   1 
HETATM 17409 O  O2A   . GTP   I 5  .   ? 11.427  17.972  -15.895 0.00 27.42  ? 501 GTP   C O2A   1 
HETATM 17410 O  "O5'" . GTP   I 5  .   ? 12.565  16.235  -14.374 0.00 28.33  ? 501 GTP   C "O5'" 1 
HETATM 17411 C  "C5'" . GTP   I 5  .   ? 11.699  16.538  -13.302 0.00 27.40  ? 501 GTP   C "C5'" 1 
HETATM 17412 C  "C4'" . GTP   I 5  .   ? 12.391  17.484  -12.330 0.00 26.05  ? 501 GTP   C "C4'" 1 
HETATM 17413 O  "O4'" . GTP   I 5  .   ? 12.764  18.660  -13.016 0.00 25.07  ? 501 GTP   C "O4'" 1 
HETATM 17414 C  "C3'" . GTP   I 5  .   ? 11.480  17.916  -11.195 0.00 24.90  ? 501 GTP   C "C3'" 1 
HETATM 17415 O  "O3'" . GTP   I 5  .   ? 11.761  17.183  -10.026 0.00 25.24  ? 501 GTP   C "O3'" 1 
HETATM 17416 C  "C2'" . GTP   I 5  .   ? 11.799  19.382  -10.986 0.00 23.17  ? 501 GTP   C "C2'" 1 
HETATM 17417 O  "O2'" . GTP   I 5  .   ? 12.604  19.543  -9.842  0.00 22.78  ? 501 GTP   C "O2'" 1 
HETATM 17418 C  "C1'" . GTP   I 5  .   ? 12.563  19.816  -12.228 0.00 23.25  ? 501 GTP   C "C1'" 1 
HETATM 17419 N  N9    . GTP   I 5  .   ? 11.793  20.794  -13.024 0.00 21.85  ? 501 GTP   C N9    1 
HETATM 17420 C  C8    . GTP   I 5  .   ? 12.152  21.241  -14.269 0.00 21.45  ? 501 GTP   C C8    1 
HETATM 17421 N  N7    . GTP   I 5  .   ? 11.230  22.130  -14.697 0.00 20.98  ? 501 GTP   C N7    1 
HETATM 17422 C  C5    . GTP   I 5  .   ? 10.286  22.266  -13.742 0.00 21.25  ? 501 GTP   C C5    1 
HETATM 17423 C  C6    . GTP   I 5  .   ? 9.136   23.043  -13.677 0.00 21.76  ? 501 GTP   C C6    1 
HETATM 17424 O  O6    . GTP   I 5  .   ? 8.834   23.778  -14.615 0.00 22.25  ? 501 GTP   C O6    1 
HETATM 17425 N  N1    . GTP   I 5  .   ? 8.334   22.985  -12.556 0.00 22.24  ? 501 GTP   C N1    1 
HETATM 17426 C  C2    . GTP   I 5  .   ? 8.682   22.157  -11.509 0.00 21.64  ? 501 GTP   C C2    1 
HETATM 17427 N  N2    . GTP   I 5  .   ? 7.912   22.098  -10.426 0.00 21.82  ? 501 GTP   C N2    1 
HETATM 17428 N  N3    . GTP   I 5  .   ? 9.826   21.389  -11.583 0.00 21.44  ? 501 GTP   C N3    1 
HETATM 17429 C  C4    . GTP   I 5  .   ? 10.624  21.436  -12.680 0.00 21.22  ? 501 GTP   C C4    1 
HETATM 17430 MG MG    . MG    J 7  .   ? 21.132  18.259  -18.165 0.00 22.98  ? 502 MG    C MG    1 
HETATM 17431 CA CA    . CA    K 6  .   ? 14.134  56.604  -6.312  0.00 44.88  ? 503 CA    C CA    1 
HETATM 17432 C  C10   . A1EPQ L 8  .   ? 4.015   39.138  17.350  1.00 28.76  ? 504 A1EPQ C C10   1 
HETATM 17433 C  C13   . A1EPQ L 8  .   ? 3.276   42.504  18.785  1.00 29.09  ? 504 A1EPQ C C13   1 
HETATM 17434 C  C15   . A1EPQ L 8  .   ? 1.246   42.876  19.004  1.00 22.51  ? 504 A1EPQ C C15   1 
HETATM 17435 C  C17   . A1EPQ L 8  .   ? 0.158   45.154  18.046  1.00 20.42  ? 504 A1EPQ C C17   1 
HETATM 17436 C  C20   . A1EPQ L 8  .   ? 0.403   43.090  20.322  1.00 23.23  ? 504 A1EPQ C C20   1 
HETATM 17437 C  C21   . A1EPQ L 8  .   ? 2.184   40.562  18.088  1.00 30.99  ? 504 A1EPQ C C21   1 
HETATM 17438 C  C22   . A1EPQ L 8  .   ? 0.114   40.118  17.002  1.00 30.97  ? 504 A1EPQ C C22   1 
HETATM 17439 C  C24   . A1EPQ L 8  .   ? 0.650   42.212  22.780  1.00 32.07  ? 504 A1EPQ C C24   1 
HETATM 17440 C  C28   . A1EPQ L 8  .   ? -1.225  39.355  23.376  1.00 45.17  ? 504 A1EPQ C C28   1 
HETATM 17441 C  C01   . A1EPQ L 8  .   ? 4.091   45.434  11.312  1.00 30.36  ? 504 A1EPQ C C01   1 
HETATM 17442 C  C04   . A1EPQ L 8  .   ? 1.704   41.142  20.793  1.00 27.39  ? 504 A1EPQ C C04   1 
HETATM 17443 C  C05   . A1EPQ L 8  .   ? 1.332   39.683  20.540  1.00 27.15  ? 504 A1EPQ C C05   1 
HETATM 17444 C  C06   . A1EPQ L 8  .   ? 0.487   39.620  19.428  1.00 27.85  ? 504 A1EPQ C C06   1 
HETATM 17445 C  C07   . A1EPQ L 8  .   ? 1.097   39.654  18.123  1.00 32.16  ? 504 A1EPQ C C07   1 
HETATM 17446 C  C08   . A1EPQ L 8  .   ? 1.505   38.157  17.674  1.00 25.09  ? 504 A1EPQ C C08   1 
HETATM 17447 C  C09   . A1EPQ L 8  .   ? 2.906   38.035  17.012  1.00 29.03  ? 504 A1EPQ C C09   1 
HETATM 17448 C  C12   . A1EPQ L 8  .   ? 4.404   41.312  18.426  1.00 21.17  ? 504 A1EPQ C C12   1 
HETATM 17449 C  C14   . A1EPQ L 8  .   ? 2.059   41.704  19.183  1.00 23.61  ? 504 A1EPQ C C14   1 
HETATM 17450 C  C16   . A1EPQ L 8  .   ? 1.080   43.939  17.877  1.00 26.31  ? 504 A1EPQ C C16   1 
HETATM 17451 C  C18   . A1EPQ L 8  .   ? -0.678  45.345  19.358  1.00 28.07  ? 504 A1EPQ C C18   1 
HETATM 17452 C  C19   . A1EPQ L 8  .   ? -0.525  44.295  20.509  1.00 23.73  ? 504 A1EPQ C C19   1 
HETATM 17453 C  C23   . A1EPQ L 8  .   ? 0.694   39.961  15.570  1.00 27.63  ? 504 A1EPQ C C23   1 
HETATM 17454 C  C25   . A1EPQ L 8  .   ? 0.586   39.271  21.906  1.00 31.85  ? 504 A1EPQ C C25   1 
HETATM 17455 C  C31   . A1EPQ L 8  .   ? -1.557  38.242  19.375  1.00 31.81  ? 504 A1EPQ C C31   1 
HETATM 17456 C  C32   . A1EPQ L 8  .   ? -2.261  36.865  19.355  1.00 33.95  ? 504 A1EPQ C C32   1 
HETATM 17457 C  C35   . A1EPQ L 8  .   ? -2.580  46.201  20.459  1.00 25.21  ? 504 A1EPQ C C35   1 
HETATM 17458 C  C36   . A1EPQ L 8  .   ? 1.050   47.322  17.267  1.00 24.19  ? 504 A1EPQ C C36   1 
HETATM 17459 C  C37   . A1EPQ L 8  .   ? 2.430   47.008  17.961  1.00 26.39  ? 504 A1EPQ C C37   1 
HETATM 17460 C  C38   . A1EPQ L 8  .   ? 3.075   48.357  18.450  1.00 24.97  ? 504 A1EPQ C C38   1 
HETATM 17461 C  C39   . A1EPQ L 8  .   ? 3.764   49.211  17.358  1.00 25.05  ? 504 A1EPQ C C39   1 
HETATM 17462 C  C40   . A1EPQ L 8  .   ? 4.760   48.272  16.646  1.00 27.03  ? 504 A1EPQ C C40   1 
HETATM 17463 C  C42   . A1EPQ L 8  .   ? 3.688   46.838  14.735  1.00 28.34  ? 504 A1EPQ C C42   1 
HETATM 17464 C  C43   . A1EPQ L 8  .   ? 2.230   47.146  14.377  1.00 26.69  ? 504 A1EPQ C C43   1 
HETATM 17465 C  C44   . A1EPQ L 8  .   ? 1.271   45.902  14.558  1.00 23.38  ? 504 A1EPQ C C44   1 
HETATM 17466 C  C45   . A1EPQ L 8  .   ? 1.230   45.015  13.502  1.00 22.95  ? 504 A1EPQ C C45   1 
HETATM 17467 C  C46   . A1EPQ L 8  .   ? 1.955   44.977  12.131  1.00 26.06  ? 504 A1EPQ C C46   1 
HETATM 17468 C  C47   . A1EPQ L 8  .   ? 1.628   43.830  11.223  1.00 20.80  ? 504 A1EPQ C C47   1 
HETATM 17469 C  C48   . A1EPQ L 8  .   ? 0.655   42.789  11.599  1.00 19.77  ? 504 A1EPQ C C48   1 
HETATM 17470 C  C49   . A1EPQ L 8  .   ? -0.030  42.837  12.911  1.00 24.74  ? 504 A1EPQ C C49   1 
HETATM 17471 C  C50   . A1EPQ L 8  .   ? 0.307   44.026  13.864  1.00 25.58  ? 504 A1EPQ C C50   1 
HETATM 17472 C  C52   . A1EPQ L 8  .   ? 0.383   45.478  15.559  1.00 26.43  ? 504 A1EPQ C C52   1 
HETATM 17473 C  C53   . A1EPQ L 8  .   ? 0.113   46.175  16.896  1.00 21.75  ? 504 A1EPQ C C53   1 
HETATM 17474 C  C54   . A1EPQ L 8  .   ? 3.388   46.240  17.117  1.00 29.07  ? 504 A1EPQ C C54   1 
HETATM 17475 C  C55   . A1EPQ L 8  .   ? 4.554   50.396  17.882  1.00 24.94  ? 504 A1EPQ C C55   1 
HETATM 17476 C  C56   . A1EPQ L 8  .   ? 4.032   50.989  19.239  1.00 26.07  ? 504 A1EPQ C C56   1 
HETATM 17477 C  C58   . A1EPQ L 8  .   ? -1.340  46.616  16.778  1.00 24.29  ? 504 A1EPQ C C58   1 
HETATM 17478 C  C61   . A1EPQ L 8  .   ? -3.623  45.745  16.684  1.00 22.50  ? 504 A1EPQ C C61   1 
HETATM 17479 F  F62   . A1EPQ L 8  .   ? 2.215   43.720  10.017  1.00 36.92  ? 504 A1EPQ C F62   1 
HETATM 17480 F  F63   . A1EPQ L 8  .   ? 0.365   41.755  10.775  1.00 34.31  ? 504 A1EPQ C F63   1 
HETATM 17481 N  N02   . A1EPQ L 8  .   ? 0.693   41.911  21.348  1.00 28.82  ? 504 A1EPQ C N02   1 
HETATM 17482 N  N11   . A1EPQ L 8  .   ? 3.624   40.057  18.374  1.00 25.63  ? 504 A1EPQ C N11   1 
HETATM 17483 N  N41   . A1EPQ L 8  .   ? 4.064   47.042  16.132  1.00 29.34  ? 504 A1EPQ C N41   1 
HETATM 17484 N  N51   . A1EPQ L 8  .   ? -0.227  44.299  15.123  1.00 25.37  ? 504 A1EPQ C N51   1 
HETATM 17485 O  O03   . A1EPQ L 8  .   ? 2.877   45.981  11.784  1.00 33.93  ? 504 A1EPQ C O03   1 
HETATM 17486 O  O26   . A1EPQ L 8  .   ? 1.159   38.712  22.779  1.00 33.32  ? 504 A1EPQ C O26   1 
HETATM 17487 O  O27   . A1EPQ L 8  .   ? -0.772  39.633  22.067  1.00 30.37  ? 504 A1EPQ C O27   1 
HETATM 17488 O  O29   . A1EPQ L 8  .   ? 2.431   38.849  20.248  1.00 30.97  ? 504 A1EPQ C O29   1 
HETATM 17489 O  O30   . A1EPQ L 8  .   ? -0.161  38.244  19.488  1.00 32.28  ? 504 A1EPQ C O30   1 
HETATM 17490 O  O33   . A1EPQ L 8  .   ? -2.147  39.275  19.304  1.00 32.67  ? 504 A1EPQ C O33   1 
HETATM 17491 O  O34   . A1EPQ L 8  .   ? -1.546  46.444  19.519  1.00 26.84  ? 504 A1EPQ C O34   1 
HETATM 17492 O  O57   . A1EPQ L 8  .   ? 2.778   49.683  16.470  1.00 29.95  ? 504 A1EPQ C O57   1 
HETATM 17493 O  O59   . A1EPQ L 8  .   ? -1.598  47.751  16.524  1.00 26.16  ? 504 A1EPQ C O59   1 
HETATM 17494 O  O60   . A1EPQ L 8  .   ? -2.253  45.545  16.971  1.00 23.48  ? 504 A1EPQ C O60   1 
HETATM 17495 H  H102  . A1EPQ L 8  .   ? 4.227   39.705  16.440  1.00 34.51  ? 504 A1EPQ C H102  1 
HETATM 17496 H  H131  . A1EPQ L 8  .   ? 3.063   43.094  17.902  1.00 34.90  ? 504 A1EPQ C H131  1 
HETATM 17497 H  H132  . A1EPQ L 8  .   ? 3.619   43.103  19.620  1.00 34.90  ? 504 A1EPQ C H132  1 
HETATM 17498 H  H211  . A1EPQ L 8  .   ? 2.173   40.905  17.052  1.00 37.19  ? 504 A1EPQ C H211  1 
HETATM 17499 H  H222  . A1EPQ L 8  .   ? -0.124  41.162  17.163  1.00 37.16  ? 504 A1EPQ C H222  1 
HETATM 17500 H  H221  . A1EPQ L 8  .   ? -0.791  39.527  17.072  1.00 37.16  ? 504 A1EPQ C H221  1 
HETATM 17501 H  H241  . A1EPQ L 8  .   ? -0.378  42.133  23.138  1.00 38.48  ? 504 A1EPQ C H241  1 
HETATM 17502 H  H242  . A1EPQ L 8  .   ? 1.018   43.225  22.950  1.00 38.48  ? 504 A1EPQ C H242  1 
HETATM 17503 H  H243  . A1EPQ L 8  .   ? 1.278   41.502  23.320  1.00 38.48  ? 504 A1EPQ C H243  1 
HETATM 17504 H  H283  . A1EPQ L 8  .   ? -2.230  39.759  23.506  1.00 54.21  ? 504 A1EPQ C H283  1 
HETATM 17505 H  H281  . A1EPQ L 8  .   ? -0.551  39.817  24.099  1.00 54.21  ? 504 A1EPQ C H281  1 
HETATM 17506 H  H282  . A1EPQ L 8  .   ? -1.243  38.276  23.533  1.00 54.21  ? 504 A1EPQ C H282  1 
HETATM 17507 H  H013  . A1EPQ L 8  .   ? 4.917   46.080  11.601  1.00 36.43  ? 504 A1EPQ C H013  1 
HETATM 17508 H  H012  . A1EPQ L 8  .   ? 4.055   45.355  10.227  1.00 36.43  ? 504 A1EPQ C H012  1 
HETATM 17509 H  H011  . A1EPQ L 8  .   ? 4.236   44.445  11.743  1.00 36.43  ? 504 A1EPQ C H011  1 
HETATM 17510 H  H1    . A1EPQ L 8  .   ? 2.491   41.297  21.538  1.00 32.86  ? 504 A1EPQ C H1    1 
HETATM 17511 H  H061  . A1EPQ L 8  .   ? -0.186  40.477  19.506  1.00 33.42  ? 504 A1EPQ C H061  1 
HETATM 17512 H  H081  . A1EPQ L 8  .   ? 0.750   37.383  17.542  1.00 30.11  ? 504 A1EPQ C H081  1 
HETATM 17513 H  H091  . A1EPQ L 8  .   ? 3.129   37.214  16.330  1.00 34.84  ? 504 A1EPQ C H091  1 
HETATM 17514 H  H121  . A1EPQ L 8  .   ? 5.160   41.257  19.213  1.00 25.41  ? 504 A1EPQ C H121  1 
HETATM 17515 H  H122  . A1EPQ L 8  .   ? 4.870   41.510  17.458  1.00 25.41  ? 504 A1EPQ C H122  1 
HETATM 17516 H  H161  . A1EPQ L 8  .   ? 1.633   43.818  16.947  1.00 31.57  ? 504 A1EPQ C H161  1 
HETATM 17517 H  H191  . A1EPQ L 8  .   ? -1.076  44.421  21.440  1.00 28.47  ? 504 A1EPQ C H191  1 
HETATM 17518 H  H231  . A1EPQ L 8  .   ? 1.766   40.164  15.588  1.00 33.16  ? 504 A1EPQ C H231  1 
HETATM 17519 H  H233  . A1EPQ L 8  .   ? 0.202   40.666  14.899  1.00 33.16  ? 504 A1EPQ C H233  1 
HETATM 17520 H  H232  . A1EPQ L 8  .   ? 0.523   38.943  15.218  1.00 33.16  ? 504 A1EPQ C H232  1 
HETATM 17521 H  H322  . A1EPQ L 8  .   ? -1.521  36.077  19.498  1.00 40.74  ? 504 A1EPQ C H322  1 
HETATM 17522 H  H323  . A1EPQ L 8  .   ? -2.759  36.726  18.396  1.00 40.74  ? 504 A1EPQ C H323  1 
HETATM 17523 H  H321  . A1EPQ L 8  .   ? -2.997  36.822  20.157  1.00 40.74  ? 504 A1EPQ C H321  1 
HETATM 17524 H  H352  . A1EPQ L 8  .   ? -3.453  46.800  20.202  1.00 30.25  ? 504 A1EPQ C H352  1 
HETATM 17525 H  H351  . A1EPQ L 8  .   ? -2.235  46.472  21.456  1.00 30.25  ? 504 A1EPQ C H351  1 
HETATM 17526 H  H353  . A1EPQ L 8  .   ? -2.847  45.146  20.442  1.00 30.25  ? 504 A1EPQ C H353  1 
HETATM 17527 H  H362  . A1EPQ L 8  .   ? 1.272   47.858  16.350  1.00 29.03  ? 504 A1EPQ C H362  1 
HETATM 17528 H  H361  . A1EPQ L 8  .   ? 0.501   47.976  17.935  1.00 29.03  ? 504 A1EPQ C H361  1 
HETATM 17529 H  H371  . A1EPQ L 8  .   ? 2.239   46.390  18.843  1.00 31.66  ? 504 A1EPQ C H371  1 
HETATM 17530 H  H382  . A1EPQ L 8  .   ? 3.817   48.116  19.198  1.00 29.96  ? 504 A1EPQ C H382  1 
HETATM 17531 H  H381  . A1EPQ L 8  .   ? 2.291   48.956  18.892  1.00 29.96  ? 504 A1EPQ C H381  1 
HETATM 17532 H  H401  . A1EPQ L 8  .   ? 5.536   47.973  17.353  1.00 32.44  ? 504 A1EPQ C H401  1 
HETATM 17533 H  H402  . A1EPQ L 8  .   ? 5.212   48.802  15.805  1.00 32.44  ? 504 A1EPQ C H402  1 
HETATM 17534 H  H422  . A1EPQ L 8  .   ? 4.323   47.471  14.124  1.00 34.01  ? 504 A1EPQ C H422  1 
HETATM 17535 H  H421  . A1EPQ L 8  .   ? 3.880   45.799  14.487  1.00 34.01  ? 504 A1EPQ C H421  1 
HETATM 17536 H  H431  . A1EPQ L 8  .   ? 2.189   47.467  13.335  1.00 32.03  ? 504 A1EPQ C H431  1 
HETATM 17537 H  H432  . A1EPQ L 8  .   ? 1.878   47.953  15.021  1.00 32.03  ? 504 A1EPQ C H432  1 
HETATM 17538 H  H491  . A1EPQ L 8  .   ? -0.745  42.067  13.201  1.00 29.69  ? 504 A1EPQ C H491  1 
HETATM 17539 H  H542  . A1EPQ L 8  .   ? 2.841   45.449  16.604  1.00 34.88  ? 504 A1EPQ C H542  1 
HETATM 17540 H  H541  . A1EPQ L 8  .   ? 4.135   45.785  17.767  1.00 34.88  ? 504 A1EPQ C H541  1 
HETATM 17541 H  H551  . A1EPQ L 8  .   ? 4.518   51.181  17.136  1.00 29.92  ? 504 A1EPQ C H551  1 
HETATM 17542 H  H552  . A1EPQ L 8  .   ? 5.580   50.079  18.025  1.00 29.92  ? 504 A1EPQ C H552  1 
HETATM 17543 H  H563  . A1EPQ L 8  .   ? 2.948   51.078  19.203  1.00 31.28  ? 504 A1EPQ C H563  1 
HETATM 17544 H  H562  . A1EPQ L 8  .   ? 4.472   51.973  19.398  1.00 31.28  ? 504 A1EPQ C H562  1 
HETATM 17545 H  H561  . A1EPQ L 8  .   ? 4.315   50.328  20.057  1.00 31.28  ? 504 A1EPQ C H561  1 
HETATM 17546 H  H612  . A1EPQ L 8  .   ? -4.152  44.798  16.766  1.00 27.00  ? 504 A1EPQ C H612  1 
HETATM 17547 H  H613  . A1EPQ L 8  .   ? -3.728  46.134  15.673  1.00 27.00  ? 504 A1EPQ C H613  1 
HETATM 17548 H  H611  . A1EPQ L 8  .   ? -4.041  46.457  17.392  1.00 27.00  ? 504 A1EPQ C H611  1 
HETATM 17549 H  H511  . A1EPQ L 8  .   ? -0.911  43.758  15.617  1.00 30.44  ? 504 A1EPQ C H511  1 
HETATM 17550 H  H291  . A1EPQ L 8  .   ? 2.126   37.959  20.076  1.00 37.16  ? 504 A1EPQ C H291  1 
HETATM 17551 H  H571  . A1EPQ L 8  .   ? 2.097   50.096  16.991  1.00 35.94  ? 504 A1EPQ C H571  1 
HETATM 17552 H  H3    . A1EPQ L 8  .   ? 4.924   38.626  17.674  1.00 34.51  ? 504 A1EPQ C H3    1 
HETATM 17553 H  H111  . A1EPQ L 8  .   ? 3.684   39.575  19.255  1.00 30.76  ? 504 A1EPQ C H111  1 
HETATM 17554 P  PB    . GDP   M 9  .   ? 24.219  -10.181 -41.602 0.00 55.25  ? 501 GDP   D PB    1 
HETATM 17555 O  O1B   . GDP   M 9  .   ? 23.385  -9.008  -42.062 0.00 53.73  ? 501 GDP   D O1B   1 
HETATM 17556 O  O2B   . GDP   M 9  .   ? 25.391  -9.677  -40.795 0.00 54.46  ? 501 GDP   D O2B   1 
HETATM 17557 O  O3B   . GDP   M 9  .   ? 24.739  -10.936 -42.801 0.00 56.05  ? 501 GDP   D O3B   1 
HETATM 17558 O  O3A   . GDP   M 9  .   ? 23.337  -11.152 -40.670 0.00 56.11  ? 501 GDP   D O3A   1 
HETATM 17559 P  PA    . GDP   M 9  .   ? 21.996  -11.878 -41.181 0.00 57.21  ? 501 GDP   D PA    1 
HETATM 17560 O  O1A   . GDP   M 9  .   ? 22.301  -12.926 -42.226 0.00 58.73  ? 501 GDP   D O1A   1 
HETATM 17561 O  O2A   . GDP   M 9  .   ? 21.008  -10.849 -41.695 0.00 55.86  ? 501 GDP   D O2A   1 
HETATM 17562 O  "O5'" . GDP   M 9  .   ? 21.461  -12.550 -39.817 0.00 56.66  ? 501 GDP   D "O5'" 1 
HETATM 17563 C  "C5'" . GDP   M 9  .   ? 20.418  -13.526 -39.824 0.00 57.36  ? 501 GDP   D "C5'" 1 
HETATM 17564 C  "C4'" . GDP   M 9  .   ? 19.769  -13.590 -38.437 0.00 57.01  ? 501 GDP   D "C4'" 1 
HETATM 17565 O  "O4'" . GDP   M 9  .   ? 19.005  -12.419 -38.206 0.00 55.39  ? 501 GDP   D "O4'" 1 
HETATM 17566 C  "C3'" . GDP   M 9  .   ? 18.879  -14.795 -38.277 0.00 58.45  ? 501 GDP   D "C3'" 1 
HETATM 17567 O  "O3'" . GDP   M 9  .   ? 19.390  -15.626 -37.214 0.00 59.64  ? 501 GDP   D "O3'" 1 
HETATM 17568 C  "C2'" . GDP   M 9  .   ? 17.533  -14.155 -37.978 0.00 56.91  ? 501 GDP   D "C2'" 1 
HETATM 17569 O  "O2'" . GDP   M 9  .   ? 17.194  -14.647 -36.672 0.00 57.35  ? 501 GDP   D "O2'" 1 
HETATM 17570 C  "C1'" . GDP   M 9  .   ? 17.646  -12.683 -38.073 0.00 55.51  ? 501 GDP   D "C1'" 1 
HETATM 17571 N  N9    . GDP   M 9  .   ? 17.104  -12.182 -39.390 0.00 55.57  ? 501 GDP   D N9    1 
HETATM 17572 C  C8    . GDP   M 9  .   ? 17.658  -12.090 -40.692 0.00 55.35  ? 501 GDP   D C8    1 
HETATM 17573 N  N7    . GDP   M 9  .   ? 16.789  -11.462 -41.499 0.00 55.08  ? 501 GDP   D N7    1 
HETATM 17574 C  C5    . GDP   M 9  .   ? 15.854  -11.207 -40.715 0.00 55.61  ? 501 GDP   D C5    1 
HETATM 17575 C  C6    . GDP   M 9  .   ? 14.595  -10.591 -41.096 0.00 56.63  ? 501 GDP   D C6    1 
HETATM 17576 O  O6    . GDP   M 9  .   ? 14.110  -10.034 -42.191 0.00 56.69  ? 501 GDP   D O6    1 
HETATM 17577 N  N1    . GDP   M 9  .   ? 13.697  -10.430 -40.028 0.00 57.36  ? 501 GDP   D N1    1 
HETATM 17578 C  C2    . GDP   M 9  .   ? 13.840  -10.686 -38.656 0.00 56.86  ? 501 GDP   D C2    1 
HETATM 17579 N  N2    . GDP   M 9  .   ? 12.979  -10.605 -37.710 0.00 56.91  ? 501 GDP   D N2    1 
HETATM 17580 N  N3    . GDP   M 9  .   ? 14.951  -11.406 -38.376 0.00 55.93  ? 501 GDP   D N3    1 
HETATM 17581 C  C4    . GDP   M 9  .   ? 15.904  -11.593 -39.376 0.00 55.54  ? 501 GDP   D C4    1 
HETATM 17582 MG MG    . MG    N 7  .   ? 25.257  74.088  45.680  0.00 26.00  ? 501 MG    B MG    1 
HETATM 17583 P  PB    . GDP   O 9  .   ? 19.614  49.951  15.401  0.00 17.63  ? 502 GDP   B PB    1 
HETATM 17584 O  O1B   . GDP   O 9  .   ? 19.704  49.235  14.076  0.00 17.92  ? 502 GDP   B O1B   1 
HETATM 17585 O  O2B   . GDP   O 9  .   ? 20.936  49.819  16.128  0.00 17.25  ? 502 GDP   B O2B   1 
HETATM 17586 O  O3B   . GDP   O 9  .   ? 19.308  51.409  15.160  0.00 18.33  ? 502 GDP   B O3B   1 
HETATM 17587 O  O3A   . GDP   O 9  .   ? 18.428  49.304  16.275  0.00 18.54  ? 502 GDP   B O3A   1 
HETATM 17588 P  PA    . GDP   O 9  .   ? 16.949  49.156  15.655  0.00 20.00  ? 502 GDP   B PA    1 
HETATM 17589 O  O1A   . GDP   O 9  .   ? 16.963  48.252  14.446  0.00 19.88  ? 502 GDP   B O1A   1 
HETATM 17590 O  O2A   . GDP   O 9  .   ? 16.376  50.506  15.296  0.00 22.01  ? 502 GDP   B O2A   1 
HETATM 17591 O  "O5'" . GDP   O 9  .   ? 16.109  48.493  16.857  0.00 19.34  ? 502 GDP   B "O5'" 1 
HETATM 17592 C  "C5'" . GDP   O 9  .   ? 14.780  48.023  16.646  0.00 19.57  ? 502 GDP   B "C5'" 1 
HETATM 17593 C  "C4'" . GDP   O 9  .   ? 14.053  47.993  17.983  0.00 19.44  ? 502 GDP   B "C4'" 1 
HETATM 17594 O  "O4'" . GDP   O 9  .   ? 13.994  49.320  18.510  0.00 19.50  ? 502 GDP   B "O4'" 1 
HETATM 17595 C  "C3'" . GDP   O 9  .   ? 12.623  47.502  17.833  0.00 19.79  ? 502 GDP   B "C3'" 1 
HETATM 17596 O  "O3'" . GDP   O 9  .   ? 12.476  46.221  18.452  0.00 19.80  ? 502 GDP   B "O3'" 1 
HETATM 17597 C  "C2'" . GDP   O 9  .   ? 11.756  48.525  18.537  0.00 19.46  ? 502 GDP   B "C2'" 1 
HETATM 17598 O  "O2'" . GDP   O 9  .   ? 11.065  47.913  19.630  0.00 19.46  ? 502 GDP   B "O2'" 1 
HETATM 17599 C  "C1'" . GDP   O 9  .   ? 12.701  49.599  19.052  0.00 19.36  ? 502 GDP   B "C1'" 1 
HETATM 17600 N  N9    . GDP   O 9  .   ? 12.245  50.937  18.599  0.00 19.06  ? 502 GDP   B N9    1 
HETATM 17601 C  C8    . GDP   O 9  .   ? 12.484  51.475  17.388  0.00 20.36  ? 502 GDP   B C8    1 
HETATM 17602 N  N7    . GDP   O 9  .   ? 11.934  52.711  17.283  0.00 20.24  ? 502 GDP   B N7    1 
HETATM 17603 C  C5    . GDP   O 9  .   ? 11.327  52.983  18.452  0.00 18.81  ? 502 GDP   B C5    1 
HETATM 17604 C  C6    . GDP   O 9  .   ? 10.555  54.116  19.016  0.00 18.87  ? 502 GDP   B C6    1 
HETATM 17605 O  O6    . GDP   O 9  .   ? 10.338  55.145  18.341  0.00 20.06  ? 502 GDP   B O6    1 
HETATM 17606 N  N1    . GDP   O 9  .   ? 10.098  54.002  20.269  0.00 18.78  ? 502 GDP   B N1    1 
HETATM 17607 C  C2    . GDP   O 9  .   ? 10.317  52.905  21.018  0.00 18.53  ? 502 GDP   B C2    1 
HETATM 17608 N  N2    . GDP   O 9  .   ? 9.818   52.873  22.277  0.00 18.42  ? 502 GDP   B N2    1 
HETATM 17609 N  N3    . GDP   O 9  .   ? 11.015  51.830  20.567  0.00 18.43  ? 502 GDP   B N3    1 
HETATM 17610 C  C4    . GDP   O 9  .   ? 11.535  51.811  19.316  0.00 18.56  ? 502 GDP   B C4    1 
HETATM 17611 O  O     . HOH   P 10 .   ? 11.523  43.533  12.185  1.00 22.48  ? 601 HOH   C O     1 
HETATM 17612 O  O     . HOH   P 10 .   ? 2.117   36.077  20.120  1.00 28.49  ? 602 HOH   C O     1 
HETATM 17613 O  O     . HOH   P 10 .   ? 2.822   48.504  4.867   1.00 32.53  ? 603 HOH   C O     1 
HETATM 17614 O  O     . HOH   P 10 .   ? 5.635   35.736  19.518  1.00 34.13  ? 604 HOH   C O     1 
HETATM 17615 O  O     . HOH   P 10 .   ? -4.119  41.947  21.216  1.00 24.21  ? 605 HOH   C O     1 
HETATM 17616 O  O     . HOH   Q 10 .   ? 15.785  48.589  12.753  1.00 22.37  ? 601 HOH   B O     1 
HETATM 17617 O  O     . HOH   Q 10 .   ? 7.486   59.478  17.108  1.00 16.51  ? 602 HOH   B O     1 
# 
